{"data":[{"acc":"P03265","sequence":"MASREEEQRETTPERGRGAARRPPTMEDVSSPSPSPPPPRAPPKKRMRRRIESEDEEDSSQDALVPRTPSPRPSTSAADLAIAPKKKKKRPSPKPERPPSPEVIVDSEEEREDVALQMVGFSNPPVLIKHGKGGKRTVRRLNEDDPVARGMRTQEEEEEPSEAESEITVMNPLSVPIVSAWEKGMEAARALMDKYHVDNDLKANFKLLPDQVEALAAVCKTWLNEEHRGLQLTFTSKKTFVTMMGRFLQAYLQSFAEVTYKHHEPTGCALWLHRCAEIEGELKCLHGSIMINKEHVIEMDVTSENGQRALKEQSSKAKIVKNRWGRNVVQISNTDARCCVHDAACPANQFSGKSCGMFFSEGAKAQVAFKQIKAFMQALYPNAQTGHGHLLMPLRCECNSKPGHAPFLGRQLPKLTPFALSNAEDLDADLISDKSVLASVHHPALIVFQCCNPVYRNSRAQGGGPNCDFKISAPDLLNALVMVRSLWSENFTELPRMVVPEFKWSTKHQYRNVSLPVAHSDARQNPFDF","creator":"gminervini","dataset":["Viral proteins"],"date":"2016-08-22T14:31:42.000Z","disprot_id":"DP00003","features":{"pfam":[{"id":"PF02236","name":"Viral DNA-binding protein, all alpha domain","start":180,"end":261},{"id":"PF03728","name":"Viral DNA-binding protein, zinc binding domain","start":282,"end":383},{"id":"PF03728","name":"Viral DNA-binding protein, zinc binding domain","start":394,"end":490}],"gene3D":[{"start":470,"end":500,"id":"1.10.269.10","name":"Adenovirus DNA-binding, N-terminal domain","_id":"685af522b4ac24d5329d6fb2"},{"start":174,"end":278,"id":"1.10.269.10","name":"Adenovirus DNA-binding, N-terminal domain","_id":"685af522b4ac24d5329d6fb3"},{"start":309,"end":469,"id":"3.90.148.10","name":"Adenovirus DNA-binding, C-terminal domain superfamily/Adenovirus DNA-binding, zinc binding domain","_id":"685af522b4ac24d5329d6fb4"}]},"genes":[{"name":{"value":"DBP","evidences":[{"source":{"id":"MF_04054","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04054","_id":"685af522b4ac24d5329d6fc7"},"code":"ECO:0000255","_id":"685af522b4ac24d5329d6fc6"}],"_id":"685af522b4ac24d5329d6fc8"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af522b4ac24d5329d6fc5"}],"length":529,"name":"DNA-binding protein","ncbi_taxon_id":28285,"organism":"Human adenovirus C serotype 5","regions_counter":4,"released":"2016_10","taxonomy":["Viruses","Varidnaviria","Bamfordvirae","Preplasmiviricota","Tectiliviricetes","Rowavirales","Adenoviridae","Mastadenovirus"],"UniParc":"UPI000012961D","uniref100":"UniRef100_P03265","uniref50":"UniRef50_P03265","uniref90":"UniRef90_P03265","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1ADV","_id":"685af522b4ac24d5329d6fbb"},{"db":"PDB","id":"1ADU","_id":"685af522b4ac24d5329d6fbc"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":294,"end":334,"interaction_partner":[],"reference_html":"Alternative arrangements of the protein chain are possible for the adenovirus single-stranded DNA binding protein. <i> Kanellopoulos PN, Tsernoglou D, van der Vliet PC, Tucker PA. </i> J Mol Biol, 1996","reference_id":"8632448","region_id":"DP00003r002","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"Five sections of the polypeptidechain are either invisible, or poorly defined in the electron density map. For the first molecule of the dimer in the asymmetric unit they are A174 to A179 (the N terminus of the C-terminal domain), A294 to A334, A401 to A405, A427 to A432 and A454 to A464 whilst for the second molecule they are B174 to B179, B293 to B334, B344 to B349, B401 to B405 and B454 to B464.","_id":"685af522b4ac24d5329d6fba"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","uniprot_changed":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-07-16T14:16:05.729Z","_id":"685af522b4ac24d5329d6fbd"},"version":4,"_id":"685af522b4ac24d5329d6fb9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1ADV","_id":"685af522b4ac24d5329d6fc2"},{"db":"PDB","id":"1ADU","_id":"685af522b4ac24d5329d6fc3"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":454,"end":464,"interaction_partner":[],"reference_html":"Alternative arrangements of the protein chain are possible for the adenovirus single-stranded DNA binding protein. <i> Kanellopoulos PN, Tsernoglou D, van der Vliet PC, Tucker PA. </i> J Mol Biol, 1996","reference_id":"8632448","region_id":"DP00003r004","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"Five sections of the polypeptidechain are either invisible, or poorly defined in the electron density map. For the first molecule of the dimer in the asymmetric unit they are A174 to A179 (the N terminus of the C-terminal domain), A294 to A334, A401 to A405, A427 to A432 and A454 to A464 whilst for the second molecule they are B174 to B179, B293 to B334, B344 to B349, B401 to B405 and B454 to B464.","_id":"685af522b4ac24d5329d6fc1"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","uniprot_changed":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-07-16T14:16:04.850Z","_id":"685af522b4ac24d5329d6fc4"},"version":4,"_id":"685af522b4ac24d5329d6fc0","reference_source":"pmid"}],"__v":0,"disorder_content":0.09829867674858223,"disprot_consensus":{"full":[{"start":294,"end":334,"type":"D"},{"start":454,"end":464,"type":"D"}],"Structural state":[{"start":294,"end":334,"type":"D"},{"start":454,"end":464,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00666","name":"Cathelicidin","start":31,"end":130},{"id":"PF12153","name":"LPS binding domain of CAP18 (C terminal)","start":136,"end":163}],"gene3D":[{"start":28,"end":133,"id":"3.10.450.10","name":"3.10.450.10"}]},"uniref50":"UniRef50_P49913","sequence":"MKTQRDGHSLGRWSLVLLLLGLVMPLAIIAQVLSYKEAVLRAIDGINQRSSDANLYRLLDLDPRPTMDGDPDTPKPVSFTVKETVCPRTTQQSPEDCDFKKDGLVKRCMGTVTLNQARGSFDISCDKDNKRFALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P49913","disprot_id":"DP00004","ncbi_taxon_id":9606,"regions_counter":6,"creator":"jssuarez","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":170,"region_id":"DP00004r001","released":"2022_03","ec_id":"ECO:0006206","reference_html":"Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37. <i> Johansson J, Gudmundsson GH, Rottenberg ME, Berndt KD, Agerberth B. </i> J Biol Chem, 1998","statement":[{"text":"the CD spectrum of LL-37 in water exhibits a minimum around 200 nm, which is indicative of a highly disordered conformation","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":134,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"near-UV circular dichroism evidence used in manual assertion","version":4,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"9452503","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-07T09:29:16.755Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":170,"term_name":"disorder to order","released":"2022_03","ec_name":"near-UV circular dichroism evidence used in manual assertion","reference_html":"Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37. <i> Johansson J, Gudmundsson GH, Rottenberg ME, Berndt KD, Agerberth B. </i> J Biol Chem, 1998","term_id":"IDPO:0000011","curator_id":"esalladini","start":134,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"9452503","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006206","region_id":"DP00004r002","statement":[{"text":"Taken together, this highly cooperative concentration-dependent helix-coil equilibrium is highly reminiscent of the monomer-oligomer transitions common to peptide sequences capable of forming amphipathic α-helices (e.g. melittin; Ref. 27).","type":"Results"},{"text":"15 mmNaCl affects the structure of LL-37 to a very limited extent (Fig. 2 B), and replacement of Na+ with Mg2+ does not have any effect on the structural transitions observed, which shows that the structural changes are predominantly caused by the SO42−, HCO3−, and CF3CO2−anions.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-07T09:29:17.517Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":134,"end":170,"reference_id":"9452503","reference_source":"pmid","reference_html":"Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37. <i> Johansson J, Gudmundsson GH, Rottenberg ME, Berndt KD, Agerberth B. </i> J Biol Chem, 1998","date":"2022-05-27T08:17:13.860Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0019835","term_name":"cytolysis","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0007634","ec_ontology":"ECO","ec_name":"experimental phenotypic evidence used in manual assertion","released":"2022_06","version":4,"region_id":"DP00004r004","statement":[{"text":"The helical, oligomeric conformation of LL-37 is apparently a requirement for activity, since the highest antibacterial activity correlates to maximal helical content, while intermediate and low activities correspond to less helical content and disordered secondary structure (Fig. 5).","type":"Discussion"},{"text":"The minimal inhibitory concentration of LL-37 againstE. coli is 5 μm, and at 13–25 μm the peptide is cytotoxic against several eukaryotic cells.","type":"Abstract"},{"text":"The cytotoxic effect of LL-37 was determined by the ability of intracellular eukaryotic esterases to hydrolyze fluorescein diacetate (FDA) to free fluorescein, followed by flow cytometric analysis (23).","type":"Results"},{"text":"Our data show that the active helical conformation of LL-37 is cytotoxic to eukaryotic cells in the ion compositions and at pH values that are encountered under physiological conditions.","type":"Results"}],"uniprot_changed":true,"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The rupture of cell membranes and the loss of cytoplasm.\" [UniProtKB-KW:KW-0204]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-08T18:24:44.449Z"}},{"start":150,"end":162,"reference_id":"32753597","reference_source":"pmid","reference_html":"The Human LL-37(17-29) antimicrobial peptide reveals a functional supramolecular structure. <i> Engelberg Y, Landau M. </i> Nat Commun, 2020","date":"2022-10-17T08:39:47.639Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","region_id":"DP00004r005","statement":[{"text":"We found that hLL-3717–29 formed long (several micrometers and longer), ribbon-like, fibrils, visualized using transmission electron microscopy (TEM) (Fig. 2).","type":"Results"},{"text":"Cryogenic electron microscopy (CryoEM) showed that the wide (few hundred nanometers) fibrils are composed of lateral association of thinner fibrils (Supplementary Fig. 4).","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-08T18:14:00.082Z"}},{"start":150,"end":162,"reference_id":"32753597","reference_source":"pmid","reference_html":"The Human LL-37(17-29) antimicrobial peptide reveals a functional supramolecular structure. <i> Engelberg Y, Landau M. </i> Nat Commun, 2020","date":"2022-10-17T08:41:00.619Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6S6M"}],"ec_go":"EXP","region_id":"DP00004r006","statement":[{"text":"Our determination of the crystal structure of hLL-3717–29 at 1.35 Å resolution, revealed self-assembly of amphipathic helices into a densely packed and elongated hexameric structure forming a central pore (Table 1, Fig. 3 and Supplementary Movie 1). ","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-08T18:13:49.558Z"}}],"released":"2016_10","uniref100":"UniRef100_P49913","date":"2016-08-10T18:01:35.000Z","acc":"P49913","name":"Cathelicidin antimicrobial peptide","length":170,"organism":"Homo sapiens","dataset":[],"uniparc":"UPI0000000A67","UniParc":"UPI0000000A67","genes":[{"name":{"value":"CAMP","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:1472","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:1472"}}]},"synonyms":[{"value":"CAP18","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8946956","url":"http://www.ncbi.nlm.nih.gov/pubmed/8946956","alternativeUrl":"https://europepmc.org/abstract/MED/8946956"}}]},{"value":"FALL39","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"7529412","url":"http://www.ncbi.nlm.nih.gov/pubmed/7529412","alternativeUrl":"https://europepmc.org/abstract/MED/7529412"}}]}],"orfNames":[{"value":"HSD26"}]}],"alphafold_very_low_content":0.023529411764705882,"disorder_content":0.21764705882352942,"disprot_consensus":{"full":[{"start":134,"end":170,"type":"T"}],"Structural state":[{"start":134,"end":170,"type":"D"}],"Structural transition":[{"start":134,"end":170,"type":"T"}],"Biological process":[{"start":134,"end":170,"type":"F"}]}},{"features":{"pfam":[{"id":"PF11438","name":"36-mer N-terminal peptide of the N protein (N36)","start":2,"end":36}]},"uniref50":"UniRef50_P03045","sequence":"MDAQTRRRERRAEKQAQWKAANPLLVGVSAKPVNRPILSLNRKPKSRVESALNPIDLTVLAEYHKQIESNLQRIERKNQRTWYSKPGERGITCSGRQKIKGKSIPLI","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Uroviricota","Caudoviricetes","Caudovirales","Siphoviridae","Lambdavirus"],"uniref90":"UniRef90_P03045","disprot_id":"DP00005","ncbi_taxon_id":10710,"regions_counter":24,"creator":"aschramm","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":107,"region_id":"DP00005r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Independent ligand-induced folding of the RNA-binding domain and two functionally distinct antitermination regions in the phage lambda N protein. <i> Mogridge J, Legault P, Li J, Van Oene MD, Kay LE, Greenblatt J. </i> Mol Cell, 1998","statement":[{"text":"Using NMR spectroscopy, we also show that N is disordered in solution.","type":"Introduction"},{"text":"Heteronuclear magnetic resonance experiments demonstrate that N is a disordered protein.","type":"Abstract"},{"text":" It can be concluded, therefore, that the full-length N protein and its smaller fragments are disordered in solution.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"9659923","version":4,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-07T15:20:45.299Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":107,"region_id":"DP00005r004","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Fractal dimension of an intrinsically disordered protein: small-angle X-ray scattering and computational study of the bacteriophage λ N protein. <i> Johansen D, Trewhella J, Goldenberg DP. </i> Protein Sci, 2011","statement":[{"text":"Small-angle X-ray scattering (SAXS) was used to characterize the bacteriophage  λ N protein, a 107 residue intrinsically disordered protein (IDP) that functions as a transcriptional antitermination factor.","type":"Abstract"},{"text":"The average radius of gyration from these measurements was 38 ± 3.5 Å, significantly larger than the value predicted for a denaturant-unfolded protein of 107 residues (31 ± 0.1 Å from Eq. (1) and the experimental data compiled by Kohn et al.13).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"21936008","version":4,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-07T15:20:50.973Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":107,"region_id":"DP00005r005","reference_id":"9063900","start":1,"ec_id":"ECO:0006204","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"This suggests that N exists in solution as an unfolded protein.","type":"Results"},{"text":"This conclusion is also supported by circular dichroism (CD) measurements of the uncomplexed N protein. Figure 3B shows that free N protein at 20 °C manifests only a weak CD signal at 223 nm, corresponding to a calculated (from CD) α-helix content of approximately 18%. However, further CD measurements showed that this level of apparent secondary structure is not significantly altered by changing the temperature, and CD melting curves showed that no cooperative melting occurs between 20 and 95 °C (M.R.V.G., unpublished results).","type":"Results"},{"text":"These observations are consistent with the existence of N in solution as an essentially unstructured molecule containing some (fluctuating and transient) secondary structure (Psitsyn, 1987; Kim & Baldwin, 1990).","type":"Results"},{"text":"We have shown above that N protein exists in solution as an unfolded (essentially random coil) molecule.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":4,"reference_html":"Complexes of N antitermination protein of phage lambda with specific and nonspecific RNA target sites on the nascent transcript. <i> Van Gilst MR, Rees WA, Das A, von Hippel PH. </i> Biochemistry, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-07T12:08:06.018Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":107,"region_id":"DP00005r006","reference_id":"9063900","start":1,"term_id":"GO:0003727","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Binding of Nonspecific RNA Does Not Induce α-Helical Structure in N Protein. In principle, the change in secondary structure that occurs when N binds to boxB RNA could be a requirement for (or the result of) specific binding. However, it could also be a trivial consequence of the binding of N to any RNA or DNA oligonucleotide. To test the latter hypothesis, we measured the CD spectrum of N protein bound to the nonspecific (scrambled) single-stranded RNA oligomer used in the binding studies (above). Based on the measured nonspecific Kd of ∼1 × 10-6 M for this oligomer (Figure 2C and Table 1), the RNA oligomer concentration that was used in this experiment should have formed a complex with ∼70% of the total N protein present. Figure 5A shows no observable change in ellipticity for either the N protein or the RNA component on nonspecific complex formation. We conclude that the N protein binds nonspecific RNA in essentially its unstructured solution form.","type":"Discussion"},{"text":"Binding of nonspecific RNA is assessed using CD, and authors specify that ∼70% of N should be complexed with the RNAs used, therefore it is not possible to determine which part of the protein is specifically involved in the binding.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":4,"reference_html":"Complexes of N antitermination protein of phage lambda with specific and nonspecific RNA target sites on the nascent transcript. <i> Van Gilst MR, Rees WA, Das A, von Hippel PH. </i> Biochemistry, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"single-stranded RNA binding","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-07T12:09:40.902Z"},"uniprot_changed":true,"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to single-stranded RNA.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":107,"region_id":"DP00005r007","reference_id":"9063900","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"We have shown above that N protein exists in solution as an unfolded (essentially random coil) molecule.","type":"Results"},{"text":"These observations are consistent with the existence of N in solution as an essentially unstructured molecule containing some (fluctuating and transient) secondary structure (Psitsyn, 1987; Kim & Baldwin, 1990).","type":"Results"},{"text":"A two-dimensional HSMQC NMR analysis was performed on the uncomplexed 15N-labeled N protein at 20 °C (Figure 3A). Peaks corresponding to 100 of the 107 residues of N can be resolved, but the amide resonances are sharp and clustered in the center where they have chemical shifts consistent with those of a random coil structure. This suggests that N exists in solution as an unfolded protein.","type":"Results"},{"text":"Furthermore, on the NMR time-scale we find no significant secondary or tertiary structure interactions.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"reference_html":"Complexes of N antitermination protein of phage lambda with specific and nonspecific RNA target sites on the nascent transcript. <i> Van Gilst MR, Rees WA, Das A, von Hippel PH. </i> Biochemistry, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-07T12:08:07.249Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Biological process","ec_ontology":"ECO","end":107,"region_id":"DP00005r008","reference_id":"9063900","start":1,"term_id":"GO:0006357","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"We have shown that the N protein is also unfolded when free in solution and that it is capable of activating RNA polymerase in this form, though we have no information on its structural state after binding to the transcription complex.","type":"Discussion"},{"text":"The N proteins of the lambdoid family and the Tat protein of HIV are all RNA binding transcriptional activators. ","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":4,"reference_html":"Complexes of N antitermination protein of phage lambda with specific and nonspecific RNA target sites on the nascent transcript. <i> Van Gilst MR, Rees WA, Das A, von Hippel PH. </i> Biochemistry, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"regulation of transcription by RNA polymerase II","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-07T12:09:34.356Z"},"uniprot_changed":true,"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II.\" [GOC:go_curators, GOC:txnOH]","disprot_namespace":"Disorder function","term_is_binding":false},{"term_namespace":"Biological process","ec_ontology":"ECO","end":107,"region_id":"DP00005r009","reference_id":"9063900","start":1,"term_id":"GO:0006357","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"We have shown that the N protein is also unfolded when free in solution and that it is capable of activating RNA polymerase in this form, though we have no information on its structural state after binding to the transcription complex.","type":"Discussion"},{"text":"The N proteins of the lambdoid family and the Tat protein of HIV are all RNA binding transcriptional activators. ","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":4,"reference_html":"Complexes of N antitermination protein of phage lambda with specific and nonspecific RNA target sites on the nascent transcript. <i> Van Gilst MR, Rees WA, Das A, von Hippel PH. </i> Biochemistry, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"regulation of transcription by RNA polymerase II","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-07T12:09:36.077Z"},"uniprot_changed":true,"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II.\" [GOC:go_curators, GOC:txnOH]","disprot_namespace":"Disorder function","term_is_binding":false},{"term_namespace":"Biological process","ec_ontology":"ECO","end":107,"region_id":"DP00005r010","reference_id":"30795892","start":1,"term_id":"GO:0006357","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Intrinsic Disorder Allows λN to Implement a Multi-pronged Anti-pausing and Anti-termination Strategy","type":"Discussion"},{"text":"Our results suggest that λN can bestow pause and termination resistance on the transcriptional apparatus by three main mechanisms.","type":"Discussion"},{"text":"First, λN globally repositions NusA.","type":"Discussion"},{"text":"Second, λN locally remodels RNAP elements.","type":"Discussion"},{"text":"Third, λN seems to stabilize RNAP and nucleic acids to promote processive elongation.","type":"Discussion"},{"text":"C-terminal parts of λN that traverse the hybrid cavity may avert pause-related conformational changes of RNAP, stabilize the hybrid, functionally insulate the exit tunnel from the active site, and possibly enhance the catalytic activity of RNAP via contacts to the connector.","type":"Discussion"},{"text":"Thus, λN resembles a molecular \"Swiss army knife\" with numerous tools that counteract essentially all modes of pausing and termination.","type":"Discussion"},{"text":"Remarkably, λN can comprehensively reprogram RNAP and elongation factors, although it is a very small protein (107 residues). Our results show that, due to its intrinsic disorder (VanGilst and von Hippel, 1997), it can adopt a highly elongated conformation that results in a large exposed interaction surface.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy evidence used in manual assertion","version":5,"reference_html":"Structural Basis for the Action of an All-Purpose Transcription Anti-termination Factor. <i> Krupp F, Said N, Huang YH, Loll B, Bürger J, Mielke T, Spahn CMT, Wahl MC. </i> Mol Cell, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","cross_refs":[{"db":"PDB","id":"6GOV"}],"term_name":"regulation of transcription by RNA polymerase II","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-07T14:36:40.415Z"},"uniprot_changed":true,"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II.\" [GOC:go_curators, GOC:txnOH]","disprot_namespace":"Disorder function","term_is_binding":false},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":107,"region_id":"DP00005r011","reference_id":"30795892","start":1,"term_id":"GO:0070063","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"A 3.7-Å-resolution cryo-electron microscopy structure and structure-informed functional analyses reveal a multi-pronged strategy by which the intrinsically unstructured λN directly modifies RNA polymerase interactions with the nucleic acids and subverts essential functions of NusA, NusE, and NusG to reprogram the transcriptional apparatus. λN repositions NusA and remodels the β subunit flap tip, which likely precludes folding of pause or termination RNA hairpins in the exit tunnel and disrupts termination-supporting interactions of the α subunit C-terminal domains. λN invades and traverses the RNA polymerase hybrid cavity, likely stabilizing the hybrid and impeding pause- or termination-related conformational changes of polymerase. λN also lines upstream DNA, seemingly reinforcing anti-backtracking and anti-swiveling by NusG. Moreover, λN-repositioned NusA and NusE sequester the NusG C-terminal domain, counteracting ρ-dependent termination. Other anti-terminators likely utilize similar mechanisms to enable processive transcription.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy evidence used in manual assertion","version":4,"reference_html":"Structural Basis for the Action of an All-Purpose Transcription Anti-termination Factor. <i> Krupp F, Said N, Huang YH, Loll B, Bürger J, Mielke T, Spahn CMT, Wahl MC. </i> Mol Cell, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","cross_refs":[{"db":"PDB","id":"6GOV"}],"term_name":"RNA polymerase binding","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-07T14:22:59.429Z"},"uniprot_changed":true,"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA polymerase molecule or complex.\" [GOC:BHF, GOC:mah, GOC:txnOH]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":22,"reference_id":"9659923","reference_source":"pmid","reference_html":"Independent ligand-induced folding of the RNA-binding domain and two functionally distinct antitermination regions in the phage lambda N protein. <i> Mogridge J, Legault P, Li J, Van Oene MD, Kay LE, Greenblatt J. </i> Mol Cell, 1998","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00005r012","statement":[{"text":"We have determined the structure of this complex by heteronuclear NMR spectroscopy (P. L. et al., unpublished data) and concluded that changes in N1–22 chemical shifts caused by the addition of boxB RNA reflect both the folding of the arginine-rich domain and extensive interactions with its RNA target.","type":"Results"},{"text":"Interaction with boxB RNA induces only the RNA-binding domain of N to adopt a folded conformation, while the activating regions of the protein remain disordered in the absence of their target proteins.","type":"Abstract"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-07T15:21:00.893Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":34,"end":47,"reference_id":"9659923","reference_source":"pmid","reference_html":"Independent ligand-induced folding of the RNA-binding domain and two functionally distinct antitermination regions in the phage lambda N protein. <i> Mogridge J, Legault P, Li J, Van Oene MD, Kay LE, Greenblatt J. </i> Mol Cell, 1998","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006077","ec_ontology":"ECO","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P0AFF6","partner_start":null,"partner_end":null}],"region_id":"DP00005r013","statement":[{"text":"When amino-terminal deletions of N1–47 fused to GST were used in these experiments, the smallest fragment that bound NusA was N34–47 (Figure 4B, lane 5).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-07T15:21:07.651Z"},"uniprot_changed":true,"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":34,"end":47,"reference_id":"9659923","reference_source":"pmid","reference_html":"Independent ligand-induced folding of the RNA-binding domain and two functionally distinct antitermination regions in the phage lambda N protein. <i> Mogridge J, Legault P, Li J, Van Oene MD, Kay LE, Greenblatt J. </i> Mol Cell, 1998","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P0AFF6","partner_start":null,"partner_end":null}],"region_id":"DP00005r014","statement":[{"text":"To confirm the location of the NusA-binding region in amino acids 34–47 using an independent method (see Figure 4C), gel mobility shift assays were performed using 32P-labeled nut site RNA, purified NusA, and purified N (full-length N and various carboxy-terminal deletion mutants), as described previously (Mogridge et al. 1995). NusA did not form a complex with nut site RNA and N1–22, which contains only the boxB-binding region of N (lanes 3–5). NusA also did not supershift an N1–39/nut site complex (lanes 7–9), but did supershift the nut site RNA complexed with N1–47 (lanes 10–13), the longer N fragments, and full-length N (lanes 14–30). Thus, the results of the gel mobility shift assays were in accord with those of the affinity chromatography experiments.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-07T15:21:17.277Z"},"uniprot_changed":true,"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":22,"reference_id":"9659923","reference_source":"pmid","reference_html":"Independent ligand-induced folding of the RNA-binding domain and two functionally distinct antitermination regions in the phage lambda N protein. <i> Mogridge J, Legault P, Li J, Van Oene MD, Kay LE, Greenblatt J. </i> Mol Cell, 1998","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00005r015","statement":[{"text":"We have determined the structure of this complex by heteronuclear NMR spectroscopy (P. L. et al., unpublished data) and concluded that changes in N1–22 chemical shifts caused by the addition of boxB RNA reflect both the folding of the arginine-rich domain and extensive interactions with its RNA target.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-07T15:21:19.724Z"},"uniprot_changed":true,"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":22,"reference_id":"9659923","reference_source":"pmid","reference_html":"Independent ligand-induced folding of the RNA-binding domain and two functionally distinct antitermination regions in the phage lambda N protein. <i> Mogridge J, Legault P, Li J, Van Oene MD, Kay LE, Greenblatt J. </i> Mol Cell, 1998","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0006357","term_name":"regulation of transcription by RNA polymerase II","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00005r016","statement":[{"text":"No appreciable effect was observed upon addition of N1–22, N1–39, N1–47, N1–58, N1–73, or N1–89 (lanes 2–7), but 69% read-through occurred in the presence of full-length N (lane 8). Thus, the carboxyl terminus of N is essential for its ability to support factor-independent antitermination.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-07T15:21:25.244Z"},"uniprot_changed":true,"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II.\" [GOC:go_curators, GOC:txnOH]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":107,"reference_id":"10759866","reference_source":"pmid","reference_html":"Antitermination in bacteriophage lambda. The structure of the N36 peptide-boxB RNA complex. <i> Schärpf M, Sticht H, Schweimer K, Boehm M, Hoffmann S, Rösch P. </i> Eur J Biochem, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00005r017","statement":[{"text":"The minimum near 200 nm in the far UV-CD spectra of free N protein and N36 peptide is characteristic for a random coil conformation (Fig. 2), consistent with the result of NMR spectroscopic studies.","type":"Results"}],"uniprot_changed":true,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-01-31T15:05:32.590Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":36,"reference_id":"10759866","reference_source":"pmid","reference_html":"Antitermination in bacteriophage lambda. The structure of the N36 peptide-boxB RNA complex. <i> Schärpf M, Sticht H, Schweimer K, Boehm M, Hoffmann S, Rösch P. </i> Eur J Biochem, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00005r018","statement":[{"text":"Thus, the structural changes in the N protein which occur upon binding to boxB RNA are mainly localized within the 36 N-terminal amino acids of the N protein, as indicated previously [[12]].","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-16T14:17:46.287Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2016_10","uniref100":"UniRef100_P03045","date":"2016-09-07T19:11:25.000Z","acc":"P03045","name":"Antitermination protein N","length":107,"organism":"Escherichia phage lambda","dataset":["Viral proteins","RNA-binding proteins"],"uniparc":"UPI000013364C","UniParc":"UPI000013364C","genes":[{"name":{"value":"N"},"olnNames":[{"value":"lambdap49"}]}],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":36,"type":"T"},{"start":37,"end":107,"type":"D"}],"Structural state":[{"start":1,"end":107,"type":"D"}],"Molecular function":[{"start":1,"end":107,"type":"F"}],"Biological process":[{"start":1,"end":107,"type":"F"}],"Structural transition":[{"start":1,"end":36,"type":"T"}]}},{"acc":"P00004","sequence":"MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE","alphafold_very_low_content":"0","creator":"cbassot","dataset":[],"date":"2016-08-29T15:41:17.000Z","disprot_id":"DP00006","features":{"pfam":[{"id":"PF00034","name":"Cytochrome c","start":4,"end":101}],"gene3D":[{"start":2,"end":105,"id":"1.10.760.10","name":"Cytochrome c-like domain","_id":"685af522b4ac24d5329d6fca"}]},"genes":[{"name":{"value":"CYCS","evidences":[],"_id":"685af522b4ac24d5329d6fee"},"synonyms":[{"value":"CYC","evidences":[],"_id":"685af522b4ac24d5329d6fef"}],"olnNames":[],"orfNames":[],"_id":"685af522b4ac24d5329d6fed"}],"length":105,"name":"Cytochrome c","ncbi_taxon_id":9796,"organism":"Equus caballus","regions_counter":14,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Perissodactyla","Equidae","Equus"],"UniParc":"UPI000011054E","uniref100":"UniRef100_P00004","uniref50":"UniRef50_P99999","uniref90":"UniRef90_P00004","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-05T13:33:47.501Z","disprot_namespace":"Structural transition","ec_go":"IDA","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":104,"interaction_partner":[],"reference_html":"Origin of the conformational heterogeneity of cardiolipin-bound cytochrome C. <i> Hong Y, Muenzner J, Grimm SK, Pletneva EV. </i> J Am Chem Soc, 2012","reference_id":"23066867","region_id":"DP00006r011","released":"2022_12","sample":[],"statement":[{"type":"Abstract","text":"A predominantly peripheral binding mechanism, rather than deep protein insertion into the membrane, provides a rationale for the general denaturing effect of the CL surface and the large-scale protein unfolding. These findings closely relate to cyt c folding dynamics and suggest a general strategy for extending the time window in monitoring the kinetics of folding.","_id":"685af522b4ac24d5329d6fe4"}],"states_connection":[],"term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","term_ontology":"IDPO","uniprot_changed":true,"version":3,"_id":"685af522b4ac24d5329d6fe3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-05T13:34:33.369Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":104,"interaction_partner":[],"reference_html":"Origin of the conformational heterogeneity of cardiolipin-bound cytochrome C. <i> Hong Y, Muenzner J, Grimm SK, Pletneva EV. </i> J Am Chem Soc, 2012","reference_id":"23066867","region_id":"DP00006r012","released":"2022_12","sample":[],"statement":[{"type":"Abstract","text":"Interactions of cytochrome c (cyt c) with cardiolipin (CL) partially unfold the protein activating its peroxidase function, a critical event in the execution of apoptosis.","_id":"685af522b4ac24d5329d6fe6"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_id":"GO:0008289","term_is_binding":true,"term_is_obsolete":false,"term_name":"lipid binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","uniprot_changed":true,"version":4,"_id":"685af522b4ac24d5329d6fe5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-01T14:41:39.328Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006325","ec_name":"viscosity measurement evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":105,"interaction_partner":[],"reference_html":"The conformation of horse heart apocytochrome c. <i> Stellwagen E, Rysavy R, Babul G. </i> J Biol Chem, 1972","reference_id":"4344990","region_id":"DP00006r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"A least squares analysis of the data gives an intrinsic viscosity of 15.5 ml per g. This value is nearly identical with an intrinsic viscosity of 15.2 ml per g calculated for the apoprotein in a randomly coiled conformation, using the equation of Tanford et al. (12). ","_id":"685af522b4ac24d5329d6fe8"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-05T13:01:28.661Z","_id":"685af522b4ac24d5329d6fe9"},"version":0,"_id":"685af522b4ac24d5329d6fe7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-01T14:44:04.592Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":105,"interaction_partner":[],"reference_html":"The conformation of horse heart apocytochrome c. <i> Stellwagen E, Rysavy R, Babul G. </i> J Biol Chem, 1972","reference_id":"4344990","region_id":"DP00006r014","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As seen in Fig. 2B, the fractionated apoprotein preparation exhibits negative\nellipticities between 195 and 235 nm with a minimum at 199 nm. A minimum at this wave length is characteristic of a randomly coiled conformation (15).","_id":"685af522b4ac24d5329d6feb"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-05T12:59:51.411Z","_id":"685af522b4ac24d5329d6fec"},"version":0,"_id":"685af522b4ac24d5329d6fea","reference_source":"pmid"}],"__v":0,"disorder_content":0.9904761904761905,"disprot_consensus":{"full":[{"start":1,"end":104,"type":"T"},{"start":105,"end":105,"type":"D"}],"Structural state":[{"start":2,"end":105,"type":"D"}],"Structural transition":[{"start":1,"end":104,"type":"T"}],"Molecular function":[{"start":1,"end":104,"type":"F"}]}},{"acc":"P27695","sequence":"MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGDEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL","alphafold_very_low_content":"0.11320754716981132","creator":"xcastro","dataset":["Age-related disorders proteins"],"date":"2016-09-06T17:27:23.000Z","disprot_id":"DP00007","features":{"pfam":[{"id":"PF03372","name":"Endonuclease/Exonuclease/phosphatase family","start":65,"end":309}],"gene3D":[{"start":35,"end":317,"id":"3.60.10.10","name":"Endonuclease/exonuclease/phosphatase","_id":"685af522b4ac24d5329d6ff1"}]},"genes":[{"name":{"value":"APEX1","evidences":[],"_id":"685af522b4ac24d5329d7012"},"synonyms":[{"value":"APE","evidences":[],"_id":"685af522b4ac24d5329d7013"},{"value":"APE1","evidences":[],"_id":"685af522b4ac24d5329d7014"},{"value":"APEX","evidences":[],"_id":"685af522b4ac24d5329d7015"},{"value":"APX","evidences":[],"_id":"685af522b4ac24d5329d7016"},{"value":"HAP1","evidences":[],"_id":"685af522b4ac24d5329d7017"},{"value":"REF1","evidences":[],"_id":"685af522b4ac24d5329d7018"}],"olnNames":[],"orfNames":[],"_id":"685af522b4ac24d5329d7011"}],"length":318,"name":"DNA-(apurinic or apyrimidinic site) lyase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":10,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000125C38","uniref100":"UniRef100_P27695","uniref50":"UniRef50_P27695","uniref90":"UniRef90_P27695","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1E9N","_id":"685af522b4ac24d5329d6ff9"}],"curator_id":"imicetic","curator_name":"Ivan Mičetić","curator_orcid":"0000-0003-1691-8425","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":42,"interaction_partner":[],"reference_html":"Two divalent metal ions in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1: implications for the catalytic mechanism. <i> Beernink PT, Segelke BW, Hadi MZ, Erzberger JP, Wilson DM, Rupp B. </i> J Mol Biol, 2001","reference_id":"11286553","region_id":"DP00007r002","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"The N-terminal 42 residues were not visible in the electron density map.","_id":"685af522b4ac24d5329d6ff8"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","uniprot_changed":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-06-07T11:17:05.874Z","_id":"685af522b4ac24d5329d6ffa"},"version":3,"_id":"685af522b4ac24d5329d6ff7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":36,"interaction_partner":[],"reference_html":"Domain mapping of human apurinic/apyrimidinic endonuclease. Structural and functional evidence for a disordered amino terminus and a tight globular carboxyl domain. <i> Strauss PR, Holt CM. </i> J Biol Chem, 1998","reference_id":"9603956","region_id":"DP00007r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Native AP Endo Contains a Flexible Amino-terminal Portion and a Tight Globular Domain","_id":"685af522b4ac24d5329d7005"},{"type":"Results","text":"Because the first 36 residues of the amino terminus are readily accessible to proteolysis by all the proteases examined, they are flexible and only loosely associated with the remainder of the molecule.","_id":"685af522b4ac24d5329d7006"},{"type":"Results","text":"Because the first 36 residues of the amino terminus are readily accessible to proteolysis by all the proteases examined, they are flexible and only loosely associated with the remainder of the molecule.","_id":"685af522b4ac24d5329d7007"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","uniprot_changed":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-06-07T11:38:19.841Z","_id":"685af522b4ac24d5329d7008"},"version":2,"_id":"685af522b4ac24d5329d7004","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1BIX","_id":"685af522b4ac24d5329d700a"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":32,"end":43,"interaction_partner":[],"reference_html":"The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites. <i> Gorman MA, Morera S, Rothwell DG, de La Fortelle E, Mol CD, Tainer JA, Hickson ID, Freemont PS. </i> EMBO J, 1997","reference_id":"9351835","region_id":"DP00007r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"This electron density map allowed the interpretation of the majority of residues, although no electron density was visible for 12 N-terminal amino acids (including four vector-derived residues).","_id":"685af522b4ac24d5329d700b"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","uniprot_changed":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-06-07T11:37:14.680Z","_id":"685af522b4ac24d5329d700c"},"version":2,"_id":"685af522b4ac24d5329d7009","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"4IEM","_id":"685af522b4ac24d5329d700e"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":2,"end":40,"interaction_partner":[],"reference_html":"Conserved structural chemistry for incision activity in structurally non-homologous apurinic/apyrimidinic endonuclease APE1 and endonuclease IV DNA repair enzymes. <i> Tsutakawa SE, Shin DS, Mol CD, Izumi T, Arvai AS, Mantha AK, Szczesny B, Ivanov IN, Hosfield DJ, Maiti B, Pique ME, Frankel KA, Hitomi K, Cunningham RP, Mitra S, Tainer JA. </i> J Biol Chem, 2013","reference_id":"23355472","region_id":"DP00007r008","released":"2022_03","sample":[],"statement":[{"type":"Methods","text":"The N terminus (residues 1–40) was evidently flexible because it lacked unambiguous electron density.","_id":"685af522b4ac24d5329d700f"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","uniprot_changed":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-06-07T11:38:21.102Z","_id":"685af522b4ac24d5329d7010"},"version":2,"_id":"685af522b4ac24d5329d700d","reference_source":"pmid"}],"__v":0,"disorder_content":0.13522012578616352,"disprot_consensus":{"full":[{"start":1,"end":43,"type":"D"}],"Structural state":[{"start":1,"end":43,"type":"D"}]}},{"features":{"pfam":[{"id":"PF09310","name":"POU domain, class 2, associating factor 1","start":7,"end":255}]},"uniref50":"UniRef50_Q64693","sequence":"MLWQKSTAPEQAPAPPRPYQGVRVKEPVKELLRRKRGHTSVGAAGPPTAVVLPHQPLATYSTVGPSCLDMEVSASTVTEEGTLCAGWLSQPAPATLQPLAPWTPYTEYVSHEAVSCPYSTDMYVQPVCPSYTVVGPSSVLTYASPPLITNVTPRSTATPAVGPQLEGPEHQAPLTYFPWPQPLSTLPTSSLQYQPPAPTLSGPQFVQLPISIPEPVLQDMDDPRRAISSLTIDKLLLEEEESNTYELNHTLSVEGF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q64693","disprot_id":"DP00008","ncbi_taxon_id":10090,"regions_counter":24,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":256,"region_id":"DP00008r013","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Expression of the Oct-1 transcription factor and characterization of its interactions with the Bob1 coactivator. <i> Lee L, Stollar E, Chang J, Grossmann JG, O'Brien R, Ladbury J, Carpenter B, Roberts S, Luisi B. </i> Biochemistry, 2001","term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"11380252","version":3,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"The SAXS profiles of OctΔC1 and Bob1 indicated that both proteins do not have a folded, globular structure, and a Gaussian chainlike behavior was most appropriate to describe these experimental findings (Figure 4a).","type":"Results"},{"text":"As the polymer dimensions do not reflect the respective protein masses (OctΔC1 is nearly twice as large as Bob1), these results suggest that OctΔC1 retains some structured peptide segments, presumably from the POU domain, while Bob1 exists entirely as a random chain.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-15T10:05:15.183Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":256,"region_id":"DP00008r015","released":"2022_03","ec_id":"ECO:0006232","reference_html":"Oct-1 POU and octamer DNA co-operate to recognise the Bob-1 transcription co-activator via induced folding. <i> Chang JF, Phillips K, Lundbäck T, Gstaiger M, Ladbury JE, Luisi B. </i> J Mol Biol, 1999","term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"10329190","version":3,"ec_name":"differential scanning calorimetry evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"Differential scanning calorimetry (DSC) of Bob1 shows an apparent lack of, or a very broad, melting transition, indicating that Bob1 does not adopt a stable globular fold (data not shown).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-15T10:05:21.100Z"},"uniprot_changed":true,"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":256,"region_id":"DP00008r020","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Oct-1 POU and octamer DNA co-operate to recognise the Bob-1 transcription co-activator via induced folding. <i> Chang JF, Phillips K, Lundbäck T, Gstaiger M, Ladbury JE, Luisi B. </i> J Mol Biol, 1999","term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"10329190","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"The circular dichroism (CD) spectra of Bob1(1–65) and Bob1 are consistent with a poorly ordered fold, but there are additional features characteristic of polyproline II helix (Figure 6(b); Siligardi and Drake 1995, Sreerama and Woody 1994).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-15T10:05:31.204Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":65,"reference_id":"10329190","reference_source":"pmid","reference_html":"Oct-1 POU and octamer DNA co-operate to recognise the Bob-1 transcription co-activator via induced folding. <i> Chang JF, Phillips K, Lundbäck T, Gstaiger M, Ladbury JE, Luisi B. </i> J Mol Biol, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00008r023","statement":[{"text":"The CD spectra of the ternary complex indicate that the helical composition is greater then the expected value calculated from free Bob1(1–65) and the Oct-1 POU/DNA complex (Figure 6(c); Table 3).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-15T10:06:05.644Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":1,"end":256,"reference_id":"10329190","reference_source":"pmid","reference_html":"Oct-1 POU and octamer DNA co-operate to recognise the Bob-1 transcription co-activator via induced folding. <i> Chang JF, Phillips K, Lundbäck T, Gstaiger M, Ladbury JE, Luisi B. </i> J Mol Biol, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","released":"2022_03","version":4,"region_id":"DP00008r024","statement":[{"text":"The integrated heat release for titrations of Bob1 into the pre-formed Oct-1 POU/DNA complex (Figure 2(c)) shows that both Bob1(1–65) and Bob1 have an exothermic reaction with the stable, pre-formed POU/DNA complex.","type":"Results"},{"text":"Electrophoretic DNA mobility experiments showed that the protein is binding Oct-1 POU, not the DNA","type":"Curator statement"}],"uniprot_changed":true,"interaction_partner":[{"db":"UniProt","id":"Q64693","partner_start":null,"partner_end":null}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-23T15:21:47.928Z"}}],"released":"2016_10","uniref100":"UniRef100_Q64693","date":"2016-08-23T14:21:12.000Z","acc":"Q64693","name":"POU domain class 2-associating factor 1","length":256,"organism":"Mus musculus","dataset":[],"uniparc":"UPI000016CC3E","UniParc":"UPI000016CC3E","genes":[{"name":{"value":"Pou2af1","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:105086","url":"http://www.informatics.jax.org/marker/MGI:105086"}}]},"synonyms":[{"value":"Obf-1"}]}],"alphafold_very_low_content":0.46875,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":65,"type":"T"},{"start":66,"end":256,"type":"D"}],"Structural state":[{"start":1,"end":256,"type":"D"}],"Structural transition":[{"start":1,"end":65,"type":"T"}],"Molecular function":[{"start":1,"end":256,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02268","name":"Transcription initiation factor IIA, gamma subunit, helical domain","start":6,"end":52},{"id":"PF02751","name":"Transcription initiation factor IIA, gamma subunit","start":61,"end":118}],"gene3D":[{"start":2,"end":57,"id":"1.10.287.190","name":"Transcription factor IIA gamma subunit, alpha-helical domain"},{"start":58,"end":118,"id":"2.30.18.10","name":"Transcription factor IIA (TFIIA), beta-barrel domain"}]},"uniref50":"UniRef50_P32774","sequence":"MAVPGYYELYRRSTIGNSLVDALDTLISDGRIEASLAMRVLETFDKVVAETLKDNTQSKLTVKGNLDTYGFCDDVWTFIVKNCQVTVEDSHRDASQNGSGDSQSVISVDKLRIVACNSKKSE","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P32774","disprot_id":"DP00009","ncbi_taxon_id":559292,"regions_counter":3,"creator":"dpiovesan","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":103,"region_id":"DP00009r001","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Crystal structure of a yeast TFIIA/TBP/DNA complex. <i> Tan S, Hunziker Y, Sargent DF, Richmond TJ. </i> Nature, 1996","term_id":"IDPO:0000002","curator_id":"vnugnes","start":89,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-09-05T14:13:13.323Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1YTF"}],"reference_id":"8610010","uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P32773"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P13393"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"ENA","id":"KY704470","statements":[{"type":"Article","text":"Oligonucleotides corresponding to CYC1 promoter -129 to -114 (numbered from the translation start site) were synthesized incorporating 5-iodo-dU phosphoramidite (Glen Research) where indicated, and purified on Nucleosil 300-5 C8 (Macherey-Nagel)."},{"type":"Curator statement","text":"Interacting DNA with sequence 5'- TGTATGTATATAAAAC."}]}],"statement":[{"text":"In addition, the non-conserved region cover-ing TOA2 amino acids 89-103 is unobserved.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:18:56.259Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":103,"term_name":"flexible linker","released":"2022_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of a yeast TFIIA/TBP/DNA complex. <i> Tan S, Hunziker Y, Sargent DF, Richmond TJ. </i> Nature, 1996","term_id":"IDPO:0000033","curator_id":"vnugnes","start":89,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"8610010","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2022-09-05T14:16:28.867Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00009r002","uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Disorder function","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P32773"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P13393"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"ENA","id":"KY704470","statements":[{"type":"Article","text":"Oligonucleotides corresponding to CYC1 promoter -129 to -114 (numbered from the translation start site) were synthesized incorporating 5-iodo-dU phosphoramidite (Glen Research) where indicated, and purified on Nucleosil 300-5 C8 (Macherey-Nagel)."},{"type":"Curator statement","text":"Interacting DNA with sequence 5'- TGTATGTATATAAAAC."}]}],"statement":[{"text":"The 15 amino acids of hydrophilic sequence between strands 4 and 5 of TOA2 are unobserved in the structure. They correspond closely to the 14 extra and non-essential residues of the yeast small subunit compared to the human and Drosophila small subunits27. We suggest that this region forms a  flexible and disordered loop between the two B-strands.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:19:01.230Z"}},{"start":90,"end":102,"reference_id":"12972251","reference_source":"pmid","reference_html":"Novel interactions between the components of human and yeast TFIIA/TBP/DNA complexes. <i> Bleichenbacher M, Tan S, Richmond TJ. </i> J Mol Biol, 2003","date":"2022-09-05T15:39:30.578Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"1NH2"}],"region_id":"DP00009r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P13393 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P32773"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Figure","text":"(a) The DNA fragment (14 of 17 bp) derived from the AdML promoter used in the human complex is shown with interactions with protein (arrow, hydrogen bond; line, van der Waals contact) designated by amino acid name (TFIIA interactions are italicized)."},{"type":"Curator statement","text":"Interacting DNA with sequence 5'- TGTAUGTATAUAAAAC."}]}],"statement":[{"text":"The non-conserved 17 residue loop between TOA2 β-strands S4 and S5 is not observed, and it is shortened to a three residue turn in TFIIAγ.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P32774","date":"2016-08-10T18:06:22.000Z","acc":"P32774","name":"Transcription initiation factor IIA subunit 2","length":122,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"uniparc":"UPI00001370FA","UniParc":"UPI00001370FA","genes":[{"name":{"value":"TOA2"},"olnNames":[{"value":"YKL058W"}]}],"alphafold_very_low_content":0.04918032786885246,"disorder_content":0.12295081967213115,"disprot_consensus":{"full":[{"start":89,"end":103,"type":"D"}],"Structural state":[{"start":89,"end":103,"type":"D"}],"Disorder function":[{"start":89,"end":103,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00685","name":"Sulfotransferase domain","start":38,"end":287}],"gene3D":[{"start":1,"end":295,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_P0DMM9","sequence":"MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDMIYQGGDLEKCNRAPIYVRVPFLEVNDPGEPSGLETLKDTPPPRLIKSHLPLALLPQTLLDQKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P0DMM9","disprot_id":"DP00011","ncbi_taxon_id":9606,"regions_counter":7,"creator":"agasparini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":77,"region_id":"DP00011r004","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Crystal structure of human catecholamine sulfotransferase. <i> Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL. </i> J Mol Biol, 1999","term_id":"IDPO:0000002","curator_id":"vnugnes","start":64,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10543947","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-08-16T17:53:35.679Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1CJM"}],"term_name":"disorder","uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The disordered residues cluster into several regions; the N and C termini (residues 1–7 and 294–295) and regions labelled I, II and III in Figure 1 corresponding to residues 64–77, 91–93 and 216–261, respectively.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:18:25.538Z"}},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":77,"term_name":"flexible linker","start":64,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10543947","version":5,"reference_html":"Crystal structure of human catecholamine sulfotransferase. <i> Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL. </i> J Mol Biol, 1999","date":"2023-01-13T13:09:26.685Z","term_id":"IDPO:0000033","ec_id":"ECO:0006220","region_id":"DP00011r005","uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Disorder function","cross_refs":[{"db":"PDB","id":"1CJM"}],"curator_orcid":"0000-0001-8399-7907","statement":[{"text":"An interesting feature of this structure is the loop region connecting helix α3 and strand β7. This loop is positioned close to the active site, but extends away from the core of the enzyme to interact with the active site region of another monomer of SULT1A3, related by crystallographic symmetry (Figure 3).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-16T09:57:20.698Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":261,"region_id":"DP00011r006","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Crystal structure of human catecholamine sulfotransferase. <i> Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL. </i> J Mol Biol, 1999","term_id":"IDPO:0000002","curator_id":"vnugnes","start":216,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10543947","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-08-16T17:54:02.176Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1CJM"}],"term_name":"disorder","uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The disordered residues cluster into several regions; the N and C termini (residues 1–7 and 294–295) and regions labelled I, II and III in Figure 1 corresponding to residues 64–77, 91–93 and 216–261, respectively.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:18:26.973Z"}}],"released":"2016_10","uniref100":"UniRef100_P0DMM9","date":"2016-08-22T09:21:41.000Z","acc":"P0DMM9","name":"Sulfotransferase 1A3","length":295,"organism":"Homo sapiens","dataset":[],"uniparc":"UPI0000046BED","UniParc":"UPI0000046BED","genes":[{"name":{"value":"SULT1A3"},"synonyms":[{"value":"STM"}]}],"alphafold_very_low_content":0.01694915254237288,"disorder_content":0.2033898305084746,"disprot_consensus":{"full":[{"start":64,"end":77,"type":"D"},{"start":216,"end":261,"type":"D"}],"Structural state":[{"start":64,"end":77,"type":"D"},{"start":216,"end":261,"type":"D"}],"Disorder function":[{"start":64,"end":77,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00005","name":"ABC transporter","start":441,"end":575},{"id":"PF00005","name":"ABC transporter","start":1227,"end":1373},{"id":"PF00664","name":"ABC transporter transmembrane region","start":82,"end":350},{"id":"PF00664","name":"ABC transporter transmembrane region","start":863,"end":1147},{"id":"PF14396","name":"Cystic fibrosis TM conductance regulator (CFTR), regulator domain","start":639,"end":849}],"gene3D":[{"start":52,"end":382,"id":"1.20.1560.10","name":"ABC transporter type 1, transmembrane domain"},{"start":834,"end":1174,"id":"1.20.1560.10","name":"ABC transporter type 1, transmembrane domain"},{"start":388,"end":673,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":1191,"end":1442,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_P13569","sequence":"MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELASKKNPKLINALRRCFFWRFMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFLSVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAFWEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTPLQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQANLTELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYLRYITVHKSLIFVLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHSRNNSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEGKPTKSTKPYKNGQLSKVMIIENSHVKKDDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQAISPSDRVKLFPHRNSSKCKSKPQIAALKEETEEEVQDTRL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P13569","disprot_id":"DP00012","ncbi_taxon_id":9606,"regions_counter":30,"creator":"ewagner","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":831,"region_id":"DP00012r005","released":"2022_12","ec_id":"ECO:0006204","reference_html":"A functional R domain from cystic fibrosis transmembrane conductance regulator is predominantly unstructured in solution. <i> Ostedgaard LS, Baldursson O, Vermeer DW, Welsh MJ, Robertson AD. </i> Proc Natl Acad Sci U S A, 2000","statement":[{"text":"Phosphorylated and nonphosphorylated R8 had similar CD spectra in the aqueous buffers (Fig. A), suggesting that phosphorylation did not induce a large structural change in R8.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":708,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10792060","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-09-14T09:17:33.112Z","reference_source":"pmid","term_name":"disorder","uniprot_changed":true,"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-14T12:28:45.285Z"}},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":831,"term_name":"phosphorylation display site","start":708,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"The data show that R8 (residues 708–831 of CFTR) is functional; it stimulated CFTR-ΔR/S660A channel activity. Surprisingly, R8 is predominantly unstructured, exhibiting a CD spectrum characteristic of random coil, both when phosphorylated and nonphosphorylated.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10792060","version":2,"reference_html":"A functional R domain from cystic fibrosis transmembrane conductance regulator is predominantly unstructured in solution. <i> Ostedgaard LS, Baldursson O, Vermeer DW, Welsh MJ, Robertson AD. </i> Proc Natl Acad Sci U S A, 2000","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000045","ec_id":"ECO:0006204","region_id":"DP00012r006","uniprot_changed":true,"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-07T13:07:55.373Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":838,"region_id":"DP00012r007","released":"2022_12","ec_id":"ECO:0006198","reference_html":"CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices. <i> Baker JM, Hudson RP, Kanelis V, Choy WY, Thibodeau PH, Thomas PJ, Forman-Kay JD. </i> Nat Struct Mol Biol, 2007","statement":[{"text":"NMR 1H-15N correlation spectra for the nonphosphorylated R region and the highly phosphorylated R region (superimposed in Fig. 1b) show sharp peaks, with dispersion for backbone amide proton resonances limited to values between approximately 8 and 8.7 p.p.m. in the proton dimension. This limited dispersion is diagnostic of disorder (in contrast to a dispersion of ~7 to 10 p.p.m. for folded proteins) and reflects the rapid interconversion between heterogeneous conformations in disordered proteins, in which all nuclei experience similar average chemical environments","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":654,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17660831","version":3,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2022-09-14T09:16:32.622Z","reference_source":"pmid","term_name":"disorder","uniprot_changed":true,"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"BMRB","id":"15340"},{"db":"BMRB","id":"15336"}],"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":660,"end":660,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":670,"end":670,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":700,"end":700,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":712,"end":712,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":737,"end":737,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":753,"end":753,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":768,"end":768,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":795,"end":795,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":813,"end":813,"position":"Specific residue"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-14T12:28:32.955Z"}},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":838,"term_name":"phosphorylation display site","start":654,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","statement":[{"text":"The R region is disordered independent of phosphorylation.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17660831","version":2,"reference_html":"CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices. <i> Baker JM, Hudson RP, Kanelis V, Choy WY, Thibodeau PH, Thomas PJ, Forman-Kay JD. </i> Nat Struct Mol Biol, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000045","ec_id":"ECO:0006198","region_id":"DP00012r008","uniprot_changed":true,"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-07T12:55:05.077Z"}},{"start":708,"end":831,"reference_id":"10792060","reference_source":"pmid","reference_html":"A functional R domain from cystic fibrosis transmembrane conductance regulator is predominantly unstructured in solution. <i> Ostedgaard LS, Baldursson O, Vermeer DW, Welsh MJ, Robertson AD. </i> Proc Natl Acad Sci U S A, 2000","date":"2022-09-14T09:25:54.059Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00012r010","statement":[{"text":"The tryptic patterns of phosphorylated and nonphosphorylated R8 (Fig. A) show that most of the protein is susceptible to trypsin.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-14T12:28:01.316Z"}},{"start":789,"end":819,"reference_id":"26888287","reference_source":"pmid","reference_html":"Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR. <i> Stevers LM, Lam CV, Leysen SF, Meijer FA, van Scheppingen DS, de Vries RM, Carlile GW, Milroy LG, Thomas DY, Brunsveld L, Ottmann C. </i> Proc Natl Acad Sci U S A, 2016","date":"2024-04-23T14:57:15.357Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0071889","term_name":"14-3-3 protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006277","ec_ontology":"ECO","ec_name":"fluorescence polarization evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"After N-terminal labeling with fluorescein isothiocyanate (FITC), a fluorescence polarization (FP) assay was performed to measure the binding of these labeled peptides to 14-3-3β."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":795,"end":795,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":813,"end":813,"position":"Specific residue"}],"ec_go":"IPI","region_id":"DP00012r012","statement":[{"text":"However, peptides not containing the pS768 binding motif also showed a stronger affinity for 14-3-3β than the singly phosphorylated peptides, especially CFTR_R8, which features pS795 and pS813.","type":"Results"},{"text":"LIG_14-3-3_CanoR_1 corresponds to the SLIM reported for the  792-797 region","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a 14-3-3 protein. A 14-3-3 protein is any of a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells, and have been implicated in the modulation of distinct biological processes by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. Each 14-3-3 protein sequence can be roughly divided into three sections: a divergent amino terminus, the conserved core region and a divergent carboxy-terminus. The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain, a cradle for interacting with client proteins.\" [GOC:cna, GOC:mah, PMID:15167810, PMID:19575580]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"P61981","operator":"and","partner_start":null,"partner_end":null}],"cross_refs":[{"db":"ELM","id":"LIG_14-3-3_CanoR_1"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-23T15:37:51.448Z"}},{"start":762,"end":801,"reference_id":"26888287","reference_source":"pmid","reference_html":"Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR. <i> Stevers LM, Lam CV, Leysen SF, Meijer FA, van Scheppingen DS, de Vries RM, Carlile GW, Milroy LG, Thomas DY, Brunsveld L, Ottmann C. </i> Proc Natl Acad Sci U S A, 2016","date":"2024-04-23T14:58:25.107Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0071889","term_name":"14-3-3 protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006277","ec_ontology":"ECO","ec_name":"fluorescence polarization evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"After N-terminal labeling with fluorescein isothiocyanate (FITC), a fluorescence polarization (FP) assay was performed to measure the binding of these labeled peptides to 14-3-3β."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":768,"end":768,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":795,"end":795,"position":"Specific residue"}],"ec_go":"IPI","region_id":"DP00012r013","statement":[{"text":"The results showed that in all cases 14-3-3γ binds the strongest, followed by η, β, ζ, ε, τ, and σ, respectively (Fig. S1A). The results from this experiment also showed that CFTR_R7 and CFTR_R6 exhibit the strongest binding to all seven 14-3-3 isoforms.","type":"Results"},{"text":"The strongest binder in this assay was CFTR_R7, which features the pS768 and pS795 epitopes, followed by CFTR_R6, featuring pS753 and pS768.","type":"Results"},{"text":"LIG_14-3-3_CanoR_1 corresponds to the SLIM reported for the  766-770 region","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a 14-3-3 protein. A 14-3-3 protein is any of a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells, and have been implicated in the modulation of distinct biological processes by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. Each 14-3-3 protein sequence can be roughly divided into three sections: a divergent amino terminus, the conserved core region and a divergent carboxy-terminus. The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain, a cradle for interacting with client proteins.\" [GOC:cna, GOC:mah, PMID:15167810, PMID:19575580]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"P61981","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q04917","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P31946","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63104","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P62258","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P27348","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P31947","operator":"or","partner_start":null,"partner_end":null}],"cross_refs":[{"db":"ELM","id":"LIG_14-3-3_CanoR_1"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-23T15:38:28.028Z"}},{"start":747,"end":774,"reference_id":"26888287","reference_source":"pmid","reference_html":"Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR. <i> Stevers LM, Lam CV, Leysen SF, Meijer FA, van Scheppingen DS, de Vries RM, Carlile GW, Milroy LG, Thomas DY, Brunsveld L, Ottmann C. </i> Proc Natl Acad Sci U S A, 2016","date":"2024-04-23T15:42:26.187Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0071889","term_name":"14-3-3 protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006277","ec_ontology":"ECO","ec_name":"fluorescence polarization evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"After N-terminal labeling with fluorescein isothiocyanate (FITC), a fluorescence polarization (FP) assay was performed to measure the binding of these labeled peptides to 14-3-3β."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":753,"end":753,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":768,"end":768,"position":"Specific residue"}],"ec_go":"IPI","region_id":"DP00012r014","statement":[{"text":"The results showed that in all cases 14-3-3γ binds the strongest, followed by η, β, ζ, ε, τ, and σ, respectively (Fig. S1A). The results from this experiment also showed that CFTR_R7 and CFTR_R6 exhibit the strongest binding to all seven 14-3-3 isoforms.","type":"Results"},{"text":"LIG_14-3-3_CanoR_1 corresponds to the SLIM reported for the  751-755 region and 766-770 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a 14-3-3 protein. A 14-3-3 protein is any of a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells, and have been implicated in the modulation of distinct biological processes by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. Each 14-3-3 protein sequence can be roughly divided into three sections: a divergent amino terminus, the conserved core region and a divergent carboxy-terminus. The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain, a cradle for interacting with client proteins.\" [GOC:cna, GOC:mah, PMID:15167810, PMID:19575580]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"P61981","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q04917","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P31946","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63104","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P62258","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P27348","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P31947","operator":"or","partner_start":null,"partner_end":null}],"cross_refs":[{"db":"ELM","id":"LIG_14-3-3_CanoR_1"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-23T15:43:54.547Z"}},{"start":747,"end":774,"reference_id":"26888287","reference_source":"pmid","reference_html":"Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR. <i> Stevers LM, Lam CV, Leysen SF, Meijer FA, van Scheppingen DS, de Vries RM, Carlile GW, Milroy LG, Thomas DY, Brunsveld L, Ottmann C. </i> Proc Natl Acad Sci U S A, 2016","date":"2024-04-23T15:42:48.762Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0071889","term_name":"14-3-3 protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":753,"end":753,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":768,"end":768,"position":"Specific residue"}],"ec_go":"IPI","region_id":"DP00012r015","statement":[{"text":"The binding affinities of CFTR_R6, CFTR_R7, and CFTR_R8 for 14-3-3β were 75.8, 24.0, and 370 µM, respectively (Fig. 2 C–E and Fig. S2 A–C).","type":"Results"},{"text":"LIG_14-3-3_CanoR_1 corresponds to the SLIM reported for the  751-755 region and 766-770 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a 14-3-3 protein. A 14-3-3 protein is any of a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells, and have been implicated in the modulation of distinct biological processes by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. Each 14-3-3 protein sequence can be roughly divided into three sections: a divergent amino terminus, the conserved core region and a divergent carboxy-terminus. The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain, a cradle for interacting with client proteins.\" [GOC:cna, GOC:mah, PMID:15167810, PMID:19575580]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"P31946","operator":"and","partner_start":null,"partner_end":null}],"cross_refs":[{"db":"ELM","id":" LIG_14-3-3_CanoR_1"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-23T15:44:05.105Z"}},{"start":762,"end":801,"reference_id":"26888287","reference_source":"pmid","reference_html":"Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR. <i> Stevers LM, Lam CV, Leysen SF, Meijer FA, van Scheppingen DS, de Vries RM, Carlile GW, Milroy LG, Thomas DY, Brunsveld L, Ottmann C. </i> Proc Natl Acad Sci U S A, 2016","date":"2024-04-23T15:43:17.039Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0071889","term_name":"14-3-3 protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":768,"end":768,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":795,"end":795,"position":"Specific residue"}],"ec_go":"IPI","region_id":"DP00012r016","statement":[{"text":"The binding affinities of CFTR_R6, CFTR_R7, and CFTR_R8 for 14-3-3β were 75.8, 24.0, and 370 µM, respectively (Fig. 2 C–E and Fig. S2 A–C).","type":"Results"},{"text":"LIG_14-3-3_CanoR_1 corresponds to the SLIM reported for the  766-770 region and 792-797 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a 14-3-3 protein. A 14-3-3 protein is any of a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells, and have been implicated in the modulation of distinct biological processes by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. Each 14-3-3 protein sequence can be roughly divided into three sections: a divergent amino terminus, the conserved core region and a divergent carboxy-terminus. The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain, a cradle for interacting with client proteins.\" [GOC:cna, GOC:mah, PMID:15167810, PMID:19575580]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"P31946","operator":"and","partner_start":null,"partner_end":null}],"cross_refs":[{"db":"ELM","id":" LIG_14-3-3_CanoR_1"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-23T15:43:56.743Z"}},{"start":789,"end":819,"reference_id":"26888287","reference_source":"pmid","reference_html":"Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR. <i> Stevers LM, Lam CV, Leysen SF, Meijer FA, van Scheppingen DS, de Vries RM, Carlile GW, Milroy LG, Thomas DY, Brunsveld L, Ottmann C. </i> Proc Natl Acad Sci U S A, 2016","date":"2024-04-23T15:02:47.518Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0071889","term_name":"14-3-3 protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":795,"end":795,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":813,"end":813,"position":"Specific residue"}],"ec_go":"IPI","region_id":"DP00012r017","statement":[{"text":"The binding affinities of CFTR_R6, CFTR_R7, and CFTR_R8 for 14-3-3β were 75.8, 24.0, and 370 µM, respectively (Fig. 2 C–E and Fig. S2 A–C).","type":"Results"},{"text":"LIG_14-3-3_CanoR_1 corresponds to the SLIM reported for the  792-797 region","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a 14-3-3 protein. A 14-3-3 protein is any of a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells, and have been implicated in the modulation of distinct biological processes by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. Each 14-3-3 protein sequence can be roughly divided into three sections: a divergent amino terminus, the conserved core region and a divergent carboxy-terminus. The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain, a cradle for interacting with client proteins.\" [GOC:cna, GOC:mah, PMID:15167810, PMID:19575580]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"P31946","operator":"and","partner_start":null,"partner_end":null}],"cross_refs":[{"db":"ELM","id":" LIG_14-3-3_CanoR_1"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-23T15:44:07.958Z"}},{"start":766,"end":770,"reference_id":"26888287","reference_source":"pmid","reference_html":"Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR. <i> Stevers LM, Lam CV, Leysen SF, Meijer FA, van Scheppingen DS, de Vries RM, Carlile GW, Milroy LG, Thomas DY, Brunsveld L, Ottmann C. </i> Proc Natl Acad Sci U S A, 2016","date":"2024-04-23T14:52:17.957Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0071889","term_name":"14-3-3 protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser768Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To confirm that these potential phosphorylated sites are relevant for 14-3-3 binding, the wild-type R domain and the R domain containing a S700A, S753A, or S768A mutation were coexpressed with PKA. These mutations were constructed to prevent phosphorylation of the mutation site to study the influence of each site on the binding of the CFTR R domain to 14-3-3β."}]}],"ec_go":"IMP","region_id":"DP00012r018","statement":[{"text":"Although the coexpression with PKA resulted in only a partially phosphorylated R domain (a variation of three to nine phosphoryl groups was attached to the R domain; Dataset S1, W-AA), eliminating the serine at position 768 shows a significant decrease in binding affinity to 14-3-3β (56.5–125.9 µM) whereas the other positions (700 and 753) resulted in a smaller decrease (59.9 and 92.6 µM, respectively) (Fig. S3 D–H).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a 14-3-3 protein. A 14-3-3 protein is any of a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells, and have been implicated in the modulation of distinct biological processes by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. Each 14-3-3 protein sequence can be roughly divided into three sections: a divergent amino terminus, the conserved core region and a divergent carboxy-terminus. The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain, a cradle for interacting with client proteins.\" [GOC:cna, GOC:mah, PMID:15167810, PMID:19575580]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"P31946","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-23T15:42:22.497Z"}},{"start":766,"end":770,"reference_id":"26888287","reference_source":"pmid","reference_html":"Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR. <i> Stevers LM, Lam CV, Leysen SF, Meijer FA, van Scheppingen DS, de Vries RM, Carlile GW, Milroy LG, Thomas DY, Brunsveld L, Ottmann C. </i> Proc Natl Acad Sci U S A, 2016","date":"2024-04-23T15:23:08.728Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0071889","term_name":"14-3-3 protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":768,"end":768,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":795,"end":795,"position":"Specific residue"}],"ec_go":"EXP","region_id":"DP00012r019","statement":[{"text":"Here, interpretable density was found for 11 of the 40 amino acid residues present in the CFTR_R7 peptide (R766–L770 and K793–P798) (Fig. S5B). The structure of 14-3-3γ–CFTR_R7 shows that, as for the CFTR_R6 structure, both phosphorylated binding motifs are simultaneously bound to the 14-3-3 dimer: pS768 is located in the binding groove of 14-3-3 protomer A, and pS795 is located in protomer B (Fig. S5A).","type":"Results"},{"text":"LIG_14-3-3_CanoR_1 corresponds to the SLIM reported for the 766-770 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a 14-3-3 protein. A 14-3-3 protein is any of a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells, and have been implicated in the modulation of distinct biological processes by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. Each 14-3-3 protein sequence can be roughly divided into three sections: a divergent amino terminus, the conserved core region and a divergent carboxy-terminus. The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain, a cradle for interacting with client proteins.\" [GOC:cna, GOC:mah, PMID:15167810, PMID:19575580]","term_is_obsolete":false,"term_not_annotate":false,"cross_refs":[{"db":"PDB","id":"5D3E"},{"db":"ELM","id":"LIG_14-3-3_CanoR_1"}],"interaction_partner":[{"db":"UniProt","id":"P61981","operator":"or","partner_start":null,"partner_end":null}],"sequence_construct":"QARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQAN","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-23T15:43:34.018Z"}},{"start":751,"end":758,"reference_id":"26888287","reference_source":"pmid","reference_html":"Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR. <i> Stevers LM, Lam CV, Leysen SF, Meijer FA, van Scheppingen DS, de Vries RM, Carlile GW, Milroy LG, Thomas DY, Brunsveld L, Ottmann C. </i> Proc Natl Acad Sci U S A, 2016","date":"2024-04-23T15:26:45.219Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0071889","term_name":"14-3-3 protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":753,"end":753,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":768,"end":768,"position":"Specific residue"}],"ec_go":"EXP","region_id":"DP00012r020","statement":[{"text":"Interpretable density for 19 out of 28 amino acids of the CFTR_R6 peptide (R751–G758 and R764–T774) was found (Fig. 3 A and B). The protein structure shows that both phosphorylated binding motifs of the peptide are simultaneously bound to one 14-3-3 dimer.","type":"Results"},{"text":" LIG_14-3-3_CanoR_1 corresponds to the SLIM reported for the  751-755 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a 14-3-3 protein. A 14-3-3 protein is any of a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells, and have been implicated in the modulation of distinct biological processes by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. Each 14-3-3 protein sequence can be roughly divided into three sections: a divergent amino terminus, the conserved core region and a divergent carboxy-terminus. The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain, a cradle for interacting with client proteins.\" [GOC:cna, GOC:mah, PMID:15167810, PMID:19575580]","term_is_obsolete":false,"term_not_annotate":false,"cross_refs":[{"db":"PDB","id":"5D2D"},{"db":"ELM","id":"LIG_14-3-3_CanoR_1"}],"interaction_partner":[{"db":"UniProt","id":"P63104","operator":"and","partner_start":null,"partner_end":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"}],"sequence_construct":"AILPRISVISTGPTLQARRRQSVLNLMT","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-23T15:43:30.201Z"}},{"start":698,"end":702,"reference_id":"26888287","reference_source":"pmid","reference_html":"Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR. <i> Stevers LM, Lam CV, Leysen SF, Meijer FA, van Scheppingen DS, de Vries RM, Carlile GW, Milroy LG, Thomas DY, Brunsveld L, Ottmann C. </i> Proc Natl Acad Sci U S A, 2016","date":"2024-04-23T14:55:57.566Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0071889","term_name":"14-3-3 protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser700Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To confirm that these potential phosphorylated sites are relevant for 14-3-3 binding, the wild-type R domain and the R domain containing a S700A, S753A, or S768A mutation were coexpressed with PKA. These mutations were constructed to prevent phosphorylation of the mutation site to study the influence of each site on the binding of the CFTR R domain to 14-3-3β."}]}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P31946","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00012r027","statement":[{"text":"Although the coexpression with PKA resulted in only a partially phosphorylated R domain (a variation of three to nine phosphoryl groups was attached to the R domain; Dataset S1, W-AA), eliminating the serine at position 768 shows a significant decrease in binding affinity to 14-3-3β (56.5–125.9 µM) whereas the other positions (700 and 753) resulted in a smaller decrease (59.9 and 92.6 µM, respectively) (Fig. S3 D–H).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a 14-3-3 protein. A 14-3-3 protein is any of a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells, and have been implicated in the modulation of distinct biological processes by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. Each 14-3-3 protein sequence can be roughly divided into three sections: a divergent amino terminus, the conserved core region and a divergent carboxy-terminus. The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain, a cradle for interacting with client proteins.\" [GOC:cna, GOC:mah, PMID:15167810, PMID:19575580]","term_is_obsolete":false,"term_not_annotate":false},{"start":751,"end":755,"reference_id":"26888287","reference_source":"pmid","reference_html":"Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR. <i> Stevers LM, Lam CV, Leysen SF, Meijer FA, van Scheppingen DS, de Vries RM, Carlile GW, Milroy LG, Thomas DY, Brunsveld L, Ottmann C. </i> Proc Natl Acad Sci U S A, 2016","date":"2024-04-23T14:56:13.927Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0071889","term_name":"14-3-3 protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser753Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To confirm that these potential phosphorylated sites are relevant for 14-3-3 binding, the wild-type R domain and the R domain containing a S700A, S753A, or S768A mutation were coexpressed with PKA. These mutations were constructed to prevent phosphorylation of the mutation site to study the influence of each site on the binding of the CFTR R domain to 14-3-3β."}]}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P31946","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00012r028","statement":[{"text":"Although the coexpression with PKA resulted in only a partially phosphorylated R domain (a variation of three to nine phosphoryl groups was attached to the R domain; Dataset S1, W-AA), eliminating the serine at position 768 shows a significant decrease in binding affinity to 14-3-3β (56.5–125.9 µM) whereas the other positions (700 and 753) resulted in a smaller decrease (59.9 and 92.6 µM, respectively) (Fig. S3 D–H).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a 14-3-3 protein. A 14-3-3 protein is any of a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells, and have been implicated in the modulation of distinct biological processes by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. Each 14-3-3 protein sequence can be roughly divided into three sections: a divergent amino terminus, the conserved core region and a divergent carboxy-terminus. The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain, a cradle for interacting with client proteins.\" [GOC:cna, GOC:mah, PMID:15167810, PMID:19575580]","term_is_obsolete":false,"term_not_annotate":false},{"start":764,"end":774,"reference_id":"26888287","reference_source":"pmid","reference_html":"Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR. <i> Stevers LM, Lam CV, Leysen SF, Meijer FA, van Scheppingen DS, de Vries RM, Carlile GW, Milroy LG, Thomas DY, Brunsveld L, Ottmann C. </i> Proc Natl Acad Sci U S A, 2016","date":"2024-04-23T15:22:20.661Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0071889","term_name":"14-3-3 protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":768,"end":768,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":753,"end":753,"position":"Specific residue"}],"cross_refs":[{"db":"ELM","id":"LIG_14-3-3_CanoR_1"},{"db":"PDB","id":"5D2D"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P63104","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00012r029","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"}],"statement":[{"text":"Interpretable density for 19 out of 28 amino acids of the CFTR_R6 peptide (R751–G758 and R764–T774) was found (Fig. 3 A and B). The protein structure shows that both phosphorylated binding motifs of the peptide are simultaneously bound to one 14-3-3 dimer.","type":"Results"},{"text":"LIG_14-3-3_CanoR_1 corresponds to the SLIM reported for the 766-770 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a 14-3-3 protein. A 14-3-3 protein is any of a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells, and have been implicated in the modulation of distinct biological processes by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. Each 14-3-3 protein sequence can be roughly divided into three sections: a divergent amino terminus, the conserved core region and a divergent carboxy-terminus. The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain, a cradle for interacting with client proteins.\" [GOC:cna, GOC:mah, PMID:15167810, PMID:19575580]","term_is_obsolete":false,"term_not_annotate":false,"sequence_construct":"AILPRISVISTGPTLQARRRQSVLNLMT"},{"start":793,"end":798,"reference_id":"26888287","reference_source":"pmid","reference_html":"Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR. <i> Stevers LM, Lam CV, Leysen SF, Meijer FA, van Scheppingen DS, de Vries RM, Carlile GW, Milroy LG, Thomas DY, Brunsveld L, Ottmann C. </i> Proc Natl Acad Sci U S A, 2016","date":"2024-04-23T15:20:52.573Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0071889","term_name":"14-3-3 protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":795,"end":795,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":768,"end":768,"position":"Specific residue"}],"cross_refs":[{"db":"ELM","id":"LIG_14-3-3_CanoR_1"},{"db":"PDB","id":"5D3E"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P61981","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00012r030","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"}],"sequence_construct":"QARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQAN","statement":[{"text":"Here, interpretable density was found for 11 of the 40 amino acid residues present in the CFTR_R7 peptide (R766–L770 and K793–P798) (Fig. S5B). The structure of 14-3-3γ–CFTR_R7 shows that, as for the CFTR_R6 structure, both phosphorylated binding motifs are simultaneously bound to the 14-3-3 dimer: pS768 is located in the binding groove of 14-3-3 protomer A, and pS795 is located in protomer B (Fig. S5A).","type":"Results"},{"text":"LIG_14-3-3_CanoR_1 corresponds to the SLIM reported for the 792-797 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a 14-3-3 protein. A 14-3-3 protein is any of a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells, and have been implicated in the modulation of distinct biological processes by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. Each 14-3-3 protein sequence can be roughly divided into three sections: a divergent amino terminus, the conserved core region and a divergent carboxy-terminus. The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain, a cradle for interacting with client proteins.\" [GOC:cna, GOC:mah, PMID:15167810, PMID:19575580]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_P13569","date":"2016-08-11T10:33:46.000Z","acc":"P13569","name":"Cystic fibrosis transmembrane conductance regulator","length":1480,"organism":"Homo sapiens","dataset":[],"uniparc":"UPI00001428B9","UniParc":"UPI00001428B9","genes":[{"name":{"value":"CFTR"},"synonyms":[{"value":"ABCC7"}]}],"alphafold_very_low_content":0.17432432432432432,"disorder_content":0.125,"disprot_consensus":{"full":[{"start":654,"end":838,"type":"D"}],"Structural state":[{"start":654,"end":838,"type":"D"}],"Disorder function":[{"start":654,"end":838,"type":"F"}],"Molecular function":[{"start":698,"end":702,"type":"F"},{"start":747,"end":819,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00007","name":"Cystine-knot domain","start":27,"end":130}],"gene3D":[{"start":21,"end":131,"id":"2.10.90.10","name":"Cystine-knot cytokines"}]},"uniref50":"UniRef50_P0DN86","sequence":"MEMFQGLLLLLLLSMGGTWASKEPLRPRCRPINATLAVEKEGCPVCITVNTTICAGYCPTMTRVLQGVLPALPQVVCNYRDVRFESIRLPGCPRGVNPVVSYAVALSCQCALCRRSTTDCGGPKDHPLTCDDPRFQDSSSSKAPPPSLPSPSRLPGPSDTPILPQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P0DN86","disprot_id":"DP00013","ncbi_taxon_id":9606,"regions_counter":6,"creator":"imicetic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":165,"region_id":"DP00013r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of human chorionic gonadotropin. <i> Lapthorn AJ, Harris DC, Littlejohn A, Lustbader JW, Canfield RE, Machin KJ, Morgan FJ, Isaacs NW. </i> Nature, 1994","term_id":"IDPO:0000002","curator_id":"fquaglia","start":132,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1HRP"}],"reference_id":"8202136","statement":[{"text":"The final electron density map allows a tracing of the α-subunit from residues 5 to 89 and the β-subunit from 2 to 111. The residue β111 is open to a large 50 A diameter solvent channel and it is assumed that the remaining 34 C-terminal residues adopt a random conformation and are therefore not visible in the map.","type":"Article"},{"text":"The IDR characterized in the publication and spanning the C-terminal residues corresponds to region 132-165 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-20) that is cleaved in the mature secreted protein.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-14T10:33:10.458Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":165,"region_id":"DP00013r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of human chorionic gonadotropin at 2.6 A resolution from MAD analysis of the selenomethionyl protein. <i> Wu H, Lustbader JW, Liu Y, Canfield RE, Hendrickson WA. </i> Structure, 1994","term_id":"IDPO:0000002","curator_id":"fquaglia","start":132,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1HCN"}],"reference_id":"7922031","statement":[{"text":"The carboxy-terminal peptide of the beta-subunit, which is rich in O-linked sugars, is disordered.","type":"Abstract"},{"text":"The carboxyl terminus of the β-subunit projects into a solvent expanse and there is no defined electron density for the last 34 residues.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-14T10:29:54.257Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":165,"region_id":"DP00013r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of a ternary complex between human chorionic gonadotropin (hCG) and two Fv fragments specific for the alpha and beta-subunits. <i> Tegoni M, Spinelli S, Verhoeyen M, Davis P, Cambillau C. </i> J Mol Biol, 1999","term_id":"IDPO:0000002","curator_id":"fquaglia","start":133,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1QFW"}],"reference_id":"10373373","statement":[{"text":"In this model, part of the β-subunit (112B–145B) is not visible in the electron density map, as is the case with most of the N-linked sugar residues.","type":"Results"},{"text":"The IDR characterized in the publication and spanning the C-terminal residues corresponds to region 133-165 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-20) that is cleaved in the mature secreted protein.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-14T10:31:29.399Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":143,"end":165,"reference_id":"25636227","reference_source":"pmid","reference_html":"From individual proteins to proteomic samples: characterization of O-glycosylation sites in human chorionic gonadotropin and human-plasma proteins. <i> Bai X, Li D, Zhu J, Guan Y, Zhang Q, Chi L. </i> Anal Bioanal Chem, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000041","term_name":"glycosylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00013r006","statement":[{"text":"The N52 and N78 from the α-subunit and N13 and N30 from the β-subunit are N-glycosylated, whereas S121, S127, S132, and S138 from the β-subunit are attached with O-glycans [31–33, 39].","type":"Results"},{"text":"All four previously-reported O-glycosylation sites, S121, S127, S132, and S138, are within this peptide sequence.","type":"Results"},{"text":"Only S127, S132, and S138 within this peptide sequence are known O-glycosylation sites, suggesting there is at least one novel O-glycosylation site present in this peptide.","type":"Results"},{"text":"The mentioned glycosylation sites correspond to Ser141, Ser147, Ser152, Ser158.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-14T10:42:31.360Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_P0DN86","date":"2016-09-07T15:04:03.000Z","acc":"P0DN86","name":"Choriogonadotropin subunit beta 3","length":165,"organism":"Homo sapiens","dataset":[],"uniparc":"UPI0000035497","UniParc":"UPI0000035497","genes":[{"name":{"value":"CGB3"},"synonyms":[{"value":"CGB"}]},{"name":{"value":"CGB5"}},{"name":{"value":"CGB8"}}],"alphafold_very_low_content":0.1393939393939394,"disorder_content":0.20606060606060606,"disprot_consensus":{"full":[{"start":132,"end":165,"type":"D"}],"Structural state":[{"start":132,"end":165,"type":"D"}],"Disorder function":[{"start":143,"end":165,"type":"F"}]}},{"acc":"P61926","sequence":"MTDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEEDAQRSSTEQSGEAQGEAAKSES","alphafold_very_low_content":"0.17105263157894737","creator":"ftonello","dataset":[],"date":"2016-09-02T14:16:23.000Z","disprot_id":"DP00015","features":{"pfam":[{"id":"PF02827","name":"cAMP-dependent protein kinase inhibitor","start":2,"end":69}]},"genes":[{"name":{"value":"PKIA","evidences":[],"_id":"685af522b4ac24d5329d70b2"},"synonyms":[{"value":"PRKACN1","evidences":[],"_id":"685af522b4ac24d5329d70b3"}],"olnNames":[],"orfNames":[],"_id":"685af522b4ac24d5329d70b1"}],"length":76,"name":"cAMP-dependent protein kinase inhibitor alpha","ncbi_taxon_id":9986,"organism":"Oryctolagus cuniculus","regions_counter":28,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Lagomorpha","Leporidae","Oryctolagus"],"UniParc":"UPI000012D7F3","uniref100":"UniRef100_P61925","uniref50":"UniRef50_P61925","uniref90":"UniRef90_P61925","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":76,"interaction_partner":[],"reference_html":"Expression in Escherichia coli and characterization of the heat-stable inhibitor of the cAMP-dependent protein kinase. <i> Thomas J, Van Patten SM, Howard P, Day KH, Mitchell RD, Sosnick T, Trewhella J, Walsh DA, Maurer RA. </i> J Biol Chem, 1991","reference_id":"2040607","region_id":"DP00015r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"There is a deep minimum in this spectrum near 200 nm characteristic of a protein with a large proportion of random coil structure (29).","_id":"685af522b4ac24d5329d7047"},{"type":"Results","text":"This result is in good agreement with the FTIR spectra. Thus both CD and FTIR support the conclusion that PKI contains a large proportion of random coil structure. The combined percentages of random coil and turn structures indicated by CD for this protein are unusually large.","_id":"685af522b4ac24d5329d7048"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","uniprot_changed":true,"version":3,"_id":"685af522b4ac24d5329d7046","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006228","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":76,"interaction_partner":[],"reference_html":"Expression in Escherichia coli and characterization of the heat-stable inhibitor of the cAMP-dependent protein kinase. <i> Thomas J, Van Patten SM, Howard P, Day KH, Mitchell RD, Sosnick T, Trewhella J, Walsh DA, Maurer RA. </i> J Biol Chem, 1991","reference_id":"2040607","region_id":"DP00015r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In the amide I' region the PKI spectrum shows a single broad peak whose maximum occurs at 1645 cm-1, the characteristic frequency assigned to random coil structure, indicating that this might be the dominant secondary structure in the protein.","_id":"685af522b4ac24d5329d7052"},{"type":"Results","text":"However, it is clear from the maximum in the spectrum at 1645 cm-1 that a significant portion of the structure of PKI is likely to be random coil in nature. One possible caveat to the interpretation of the FTIR data is that distorted helix structures have been observed to give rise to peaks as low as 1645 cm-1","_id":"685af522b4ac24d5329d7053"},{"type":"Results","text":"This result is in good agreement with the FTIR spectra. Thus both CD and FTIR support the conclusion that PKI contains a large proportion of random coil structure. The combined percentages of random coil and turn structures indicated by CD for this protein are unusually large.","_id":"685af522b4ac24d5329d7054"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","uniprot_changed":true,"version":3,"_id":"685af522b4ac24d5329d7051","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":76,"interaction_partner":[],"reference_html":"Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A. <i> Olivieri C, Wang Y, Li GC, V S M, Kim J, Stultz BR, Neibergall M, Porcelli F, Muretta JM, Thomas DD, Gao J, Blumenthal DK, Taylor SS, Veglia G. </i> Elife, 2020","reference_id":"32338601","region_id":"DP00015r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"PKIα is an intrinsically disordered protein with transient secondary and short-lived tertiary interactions","_id":"685af522b4ac24d5329d705e"},{"type":"Figure","text":"Far-UV circular dichroism (CD) spectrum of PKIα acquired at 25°C in native condition showing the typical CD profile for IDPs, with a minimum around 208 nm","_id":"685af522b4ac24d5329d705f"},{"type":"Results","text":"Altogether, the CD and NMR data reveal that in absence of a binding partner PKIα samples transient secondary structures encompassing the HAR and NES motifs with short-lived tertiary conformations.","_id":"685af522b4ac24d5329d7060"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","uniprot_changed":true,"version":2,"_id":"685af522b4ac24d5329d705d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"50238","_id":"685af522b4ac24d5329d7065"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":76,"interaction_partner":[],"reference_html":"Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A. <i> Olivieri C, Wang Y, Li GC, V S M, Kim J, Stultz BR, Neibergall M, Porcelli F, Muretta JM, Thomas DD, Gao J, Blumenthal DK, Taylor SS, Veglia G. </i> Elife, 2020","reference_id":"32338601","region_id":"DP00015r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"PKIα is an intrinsically disordered protein with transient secondary and short-lived tertiary interactions","_id":"685af522b4ac24d5329d7062"},{"type":"Figure","text":"[1H,15N]-Heteronuclear single quantum correlation (HSQC) spectrum of PKIα free form with resonance assignment. The protein fingerprint features a poor resonance dispersion clustered around eight ppm in the 1H dimension, typical of intrinsically disordered proteins","_id":"685af522b4ac24d5329d7063"},{"type":"Results","text":"Altogether, the CD and NMR data reveal that in absence of a binding partner PKIα samples transient secondary structures encompassing the HAR and NES motifs with short-lived tertiary conformations.","_id":"685af522b4ac24d5329d7064"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","uniprot_changed":true,"version":2,"_id":"685af522b4ac24d5329d7061","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":76,"interaction_partner":[],"reference_html":"Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A. <i> Olivieri C, Wang Y, Li GC, V S M, Kim J, Stultz BR, Neibergall M, Porcelli F, Muretta JM, Thomas DD, Gao J, Blumenthal DK, Taylor SS, Veglia G. </i> Elife, 2020","reference_id":"32338601","region_id":"DP00015r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"These profiles show the typical signatures of intrinsically disordered proteins, with the Kratky plot featuring a plateau at high q values as well as the absence of a bell-shaped curve (Figure 7C, bottom panel). In addition, the P(r) curve shows that PKIα adopts a highly extended conformational ensemble, with an abnormally large Dmax (~110 Å) and Rg (~30 Å) values for a protein of its size, both parameters are indicative of an extended, intrinsically disordered protein (Kikhney and Svergun, 2015; Figure 8D). In fact, the back-calculated SAXS profiles from the RAM-generated ensembles are in excellent agreement with the experimental SAXS scattering profiles (χ = 0.86 for q < 0.2) (Figure 7C). In the bound state, the HAR motif of PKIα is more ordered and adopts a more stable helical conformation; whereas the NES motif is considerably more dynamic and adopts a transient helical conformation (Figure 7E).","_id":"685af522b4ac24d5329d7067"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","uniprot_changed":true,"version":2,"_id":"685af522b4ac24d5329d7066","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":14,"interaction_partner":[],"reference_html":"Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A. <i> Olivieri C, Wang Y, Li GC, V S M, Kim J, Stultz BR, Neibergall M, Porcelli F, Muretta JM, Thomas DD, Gao J, Blumenthal DK, Taylor SS, Veglia G. </i> Elife, 2020","reference_id":"32338601","region_id":"DP00015r014","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"PKA-C recognizes and binds extended PKIα conformations, rigidifying the PSS region and increasing the helicity of the HAR and NES motifs.","_id":"685af522b4ac24d5329d7069"},{"type":"Figure","text":"Chemical shift index (CSI) for Cα and Cβ of free (red) and bound (blue) PKIα. The PSS motif becomes more rigid upon interaction with PKA-C. The HAR and the NES adopt a transient α-helical conformation, which is enhanced upon binding the kinase.","_id":"685af522b4ac24d5329d706a"},{"type":"Results","text":"However, the HAR and PSS resonances display significant chemical shift changes (Figure 3A,B,E), suggesting that these regions of PKI undergo drastic structural rearrangements upon binding the kinase.","_id":"685af522b4ac24d5329d706b"},{"type":"Curator statement","text":"high affinity region (HAR, residues 1–14) of PKIα.","_id":"685af522b4ac24d5329d706c"}],"states_connection":[],"term_id":"IDPO:0000023","term_name":"pre-molten globule to molten globule","term_namespace":"Structural transition","term_ontology":"IDPO","uniprot_changed":true,"version":2,"_id":"685af522b4ac24d5329d7068","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":15,"end":24,"interaction_partner":[],"reference_html":"Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A. <i> Olivieri C, Wang Y, Li GC, V S M, Kim J, Stultz BR, Neibergall M, Porcelli F, Muretta JM, Thomas DD, Gao J, Blumenthal DK, Taylor SS, Veglia G. </i> Elife, 2020","reference_id":"32338601","region_id":"DP00015r015","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"PKA-C recognizes and binds extended PKIα conformations, rigidifying the PSS region and increasing the helicity of the HAR and NES motifs.","_id":"685af522b4ac24d5329d706e"},{"type":"Figure","text":"Chemical shift index (CSI) for Cα and Cβ of free (red) and bound (blue) PKIα. The PSS motif becomes more rigid upon interaction with PKA-C. The HAR and the NES adopt a transient α-helical conformation, which is enhanced upon binding the kinase.","_id":"685af522b4ac24d5329d706f"},{"type":"Results","text":"However, the HAR and PSS resonances display significant chemical shift changes (Figure 3A,B,E), suggesting that these regions of PKI undergo drastic structural rearrangements upon binding the kinase.","_id":"685af522b4ac24d5329d7070"},{"type":"Curator statement","text":"pseudo-substrate recognition sequence (PSS, residues 15–24) of PKIα.","_id":"685af522b4ac24d5329d7071"}],"states_connection":[],"term_id":"IDPO:0000018","term_name":"disorder to molten globule","term_namespace":"Structural transition","term_ontology":"IDPO","uniprot_changed":true,"version":2,"_id":"685af522b4ac24d5329d706d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":38,"end":47,"interaction_partner":[],"reference_html":"Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A. <i> Olivieri C, Wang Y, Li GC, V S M, Kim J, Stultz BR, Neibergall M, Porcelli F, Muretta JM, Thomas DD, Gao J, Blumenthal DK, Taylor SS, Veglia G. </i> Elife, 2020","reference_id":"32338601","region_id":"DP00015r016","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"PKA-C recognizes and binds extended PKIα conformations, rigidifying the PSS region and increasing the helicity of the HAR and NES motifs.","_id":"685af522b4ac24d5329d7073"},{"type":"Figure","text":"Chemical shift index (CSI) for Cα and Cβ of free (red) and bound (blue) PKIα. The PSS motif becomes more rigid upon interaction with PKA-C. The HAR and the NES adopt a transient α-helical conformation, which is enhanced upon binding the kinase.","_id":"685af522b4ac24d5329d7074"},{"type":"Curator statement","text":"nuclear export signal (NES, residues 38–47) of PKIα.","_id":"685af522b4ac24d5329d7075"}],"states_connection":[],"term_id":"IDPO:0000023","term_name":"pre-molten globule to molten globule","term_namespace":"Structural transition","term_ontology":"IDPO","uniprot_changed":true,"version":2,"_id":"685af522b4ac24d5329d7072","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"50243","_id":"685af522b4ac24d5329d707b"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":48,"end":75,"interaction_partner":[{"db":"UniProt","id":"Q9DBC7","partner_start":null,"partner_end":null,"_id":"685af522b4ac24d5329d707c"}],"reference_html":"Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A. <i> Olivieri C, Wang Y, Li GC, V S M, Kim J, Stultz BR, Neibergall M, Porcelli F, Muretta JM, Thomas DD, Gao J, Blumenthal DK, Taylor SS, Veglia G. </i> Elife, 2020","reference_id":"32338601","region_id":"DP00015r017","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"Although the C-terminal tail of PKIα interacts transiently with the kinase’s C-lobe, it remains essentially disordered facilitating the recruitment by the CRM1/RanGTP complex for nuclear export.","_id":"685af522b4ac24d5329d7077"},{"type":"Figure","text":"The C-terminal tail of PKIα interacts transiently with PKA-C.","_id":"685af522b4ac24d5329d7078"},{"type":"Results","text":"The formation of the PKA-C/ATPγN/PKIα (ternary) complex is also reflected by the differences of longitudinal and transverse relaxation rates (ΔR1 and ΔR2) for both the HAR and PSS motifs upon forming the complex, which define a local rigidification of the PKIα backbone upon binding PKA-C, with the C-terminal portion (residues 47–75) remaining essentially unstructured (Figure 4B,C).","_id":"685af522b4ac24d5329d7079"},{"type":"Curator statement","text":"Region corresponding to the C-terminal tail of PKIα.","_id":"685af522b4ac24d5329d707a"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","uniprot_changed":true,"version":4,"_id":"685af522b4ac24d5329d7076","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":48,"end":75,"interaction_partner":[],"reference_html":"Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A. <i> Olivieri C, Wang Y, Li GC, V S M, Kim J, Stultz BR, Neibergall M, Porcelli F, Muretta JM, Thomas DD, Gao J, Blumenthal DK, Taylor SS, Veglia G. </i> Elife, 2020","reference_id":"32338601","region_id":"DP00015r018","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"Although the C-terminal tail of PKIα interacts transiently with the kinase’s C-lobe, it remains essentially disordered facilitating the recruitment by the CRM1/RanGTP complex for nuclear export.","_id":"685af522b4ac24d5329d707e"},{"type":"Results","text":"The formation of the PKA-C/ATPγN/PKIα (ternary) complex is also reflected by the differences of longitudinal and transverse relaxation rates (ΔR1 and ΔR2) for both the HAR and PSS motifs upon forming the complex, which define a local rigidification of the PKIα backbone upon binding PKA-C, with the C-terminal portion (residues 47–75) remaining essentially unstructured (Figure 4B,C).","_id":"685af522b4ac24d5329d707f"},{"type":"Curator statement","text":"Region corresponding to the C-terminal tail of PKIα.","_id":"685af522b4ac24d5329d7080"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","uniprot_changed":true,"version":3,"_id":"685af522b4ac24d5329d707d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":14,"interaction_partner":[],"reference_html":"Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A. <i> Olivieri C, Wang Y, Li GC, V S M, Kim J, Stultz BR, Neibergall M, Porcelli F, Muretta JM, Thomas DD, Gao J, Blumenthal DK, Taylor SS, Veglia G. </i> Elife, 2020","reference_id":"32338601","region_id":"DP00015r019","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"Although the C-terminal tail of PKIα interacts transiently with the kinase’s C-lobe, it remains essentially disordered facilitating the recruitment by the CRM1/RanGTP complex for nuclear export.","_id":"685af522b4ac24d5329d7082"},{"type":"Results","text":"The formation of the PKA-C/ATPγN/PKIα (ternary) complex is also reflected by the differences of longitudinal and transverse relaxation rates (ΔR1 and ΔR2) for both the HAR and PSS motifs upon forming the complex, which define a local rigidification of the PKIα backbone upon binding PKA-C, with the C-terminal portion (residues 47–75) remaining essentially unstructured (Figure 4B,C).","_id":"685af522b4ac24d5329d7083"},{"type":"Curator statement","text":"Region corresponding to the HAR motif of PKIα.","_id":"685af522b4ac24d5329d7084"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","uniprot_changed":true,"version":3,"_id":"685af522b4ac24d5329d7081","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":15,"end":24,"interaction_partner":[],"reference_html":"Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A. <i> Olivieri C, Wang Y, Li GC, V S M, Kim J, Stultz BR, Neibergall M, Porcelli F, Muretta JM, Thomas DD, Gao J, Blumenthal DK, Taylor SS, Veglia G. </i> Elife, 2020","reference_id":"32338601","region_id":"DP00015r020","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"Although the C-terminal tail of PKIα interacts transiently with the kinase’s C-lobe, it remains essentially disordered facilitating the recruitment by the CRM1/RanGTP complex for nuclear export.","_id":"685af522b4ac24d5329d7086"},{"type":"Results","text":"The formation of the PKA-C/ATPγN/PKIα (ternary) complex is also reflected by the differences of longitudinal and transverse relaxation rates (ΔR1 and ΔR2) for both the HAR and PSS motifs upon forming the complex, which define a local rigidification of the PKIα backbone upon binding PKA-C, with the C-terminal portion (residues 47–75) remaining essentially unstructured (Figure 4B,C).","_id":"685af522b4ac24d5329d7087"},{"type":"Curator statement","text":"Region corresponding to the PSS motif of PKIα.","_id":"685af522b4ac24d5329d7088"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","uniprot_changed":true,"version":3,"_id":"685af522b4ac24d5329d7085","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"50243","_id":"685af522b4ac24d5329d708d"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":15,"end":24,"interaction_partner":[],"reference_html":"Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A. <i> Olivieri C, Wang Y, Li GC, V S M, Kim J, Stultz BR, Neibergall M, Porcelli F, Muretta JM, Thomas DD, Gao J, Blumenthal DK, Taylor SS, Veglia G. </i> Elife, 2020","reference_id":"32338601","region_id":"DP00015r021","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"Although the C-terminal tail of PKIα interacts transiently with the kinase’s C-lobe, it remains essentially disordered facilitating the recruitment by the CRM1/RanGTP complex for nuclear export.","_id":"685af522b4ac24d5329d708a"},{"type":"Results","text":"The formation of the PKA-C/ATPγN/PKIα (ternary) complex is also reflected by the differences of longitudinal and transverse relaxation rates (ΔR1 and ΔR2) for both the HAR and PSS motifs upon forming the complex, which define a local rigidification of the PKIα backbone upon binding PKA-C, with the C-terminal portion (residues 47–75) remaining essentially unstructured (Figure 4B,C).","_id":"685af522b4ac24d5329d708b"},{"type":"Curator statement","text":"Region corresponding to the PSS motif of PKIα.","_id":"685af522b4ac24d5329d708c"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","uniprot_changed":true,"version":3,"_id":"685af522b4ac24d5329d7089","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"50243","_id":"685af522b4ac24d5329d7092"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":14,"interaction_partner":[{"db":"UniProt","id":"Q9DBC7","partner_start":null,"partner_end":null,"_id":"685af522b4ac24d5329d7093"}],"reference_html":"Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A. <i> Olivieri C, Wang Y, Li GC, V S M, Kim J, Stultz BR, Neibergall M, Porcelli F, Muretta JM, Thomas DD, Gao J, Blumenthal DK, Taylor SS, Veglia G. </i> Elife, 2020","reference_id":"32338601","region_id":"DP00015r022","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"Although the C-terminal tail of PKIα interacts transiently with the kinase’s C-lobe, it remains essentially disordered facilitating the recruitment by the CRM1/RanGTP complex for nuclear export.","_id":"685af522b4ac24d5329d708f"},{"type":"Results","text":"The formation of the PKA-C/ATPγN/PKIα (ternary) complex is also reflected by the differences of longitudinal and transverse relaxation rates (ΔR1 and ΔR2) for both the HAR and PSS motifs upon forming the complex, which define a local rigidification of the PKIα backbone upon binding PKA-C, with the C-terminal portion (residues 47–75) remaining essentially unstructured (Figure 4B,C).","_id":"685af522b4ac24d5329d7090"},{"type":"Curator statement","text":"Region corresponding to the HAR motif of PKIα.","_id":"685af522b4ac24d5329d7091"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","uniprot_changed":true,"version":4,"_id":"685af522b4ac24d5329d708e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":14,"interaction_partner":[],"reference_html":"Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A. <i> Olivieri C, Wang Y, Li GC, V S M, Kim J, Stultz BR, Neibergall M, Porcelli F, Muretta JM, Thomas DD, Gao J, Blumenthal DK, Taylor SS, Veglia G. </i> Elife, 2020","reference_id":"32338601","region_id":"DP00015r023","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In the bound state, the HAR motif of PKIα is more ordered and adopts a more stable helical conformation; whereas the NES motif is considerably more dynamic and adopts a transient helical conformation (Figure 7E).","_id":"685af522b4ac24d5329d7095"},{"type":"Curator statement","text":"Region corresponding to the HAR motif of PKIα.","_id":"685af522b4ac24d5329d7096"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","uniprot_changed":true,"version":3,"_id":"685af522b4ac24d5329d7094","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":14,"interaction_partner":[],"reference_html":"Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A. <i> Olivieri C, Wang Y, Li GC, V S M, Kim J, Stultz BR, Neibergall M, Porcelli F, Muretta JM, Thomas DD, Gao J, Blumenthal DK, Taylor SS, Veglia G. </i> Elife, 2020","reference_id":"32338601","region_id":"DP00015r024","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In the bound state, the HAR motif of PKIα is more ordered and adopts a more stable helical conformation; whereas the NES motif is considerably more dynamic and adopts a transient helical conformation (Figure 7E).","_id":"685af522b4ac24d5329d7098"},{"type":"Curator statement","text":"Region corresponding to the HAR motif of PKIα.","_id":"685af522b4ac24d5329d7099"}],"states_connection":[],"term_id":"IDPO:0000023","term_name":"pre-molten globule to molten globule","term_namespace":"Structural transition","term_ontology":"IDPO","uniprot_changed":true,"version":2,"_id":"685af522b4ac24d5329d7097","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001183","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":76,"interaction_partner":[{"db":"UniProt","id":"Q9DBC7","partner_start":null,"partner_end":null,"_id":"685af522b4ac24d5329d70a0"}],"reference_html":"Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A. <i> Olivieri C, Wang Y, Li GC, V S M, Kim J, Stultz BR, Neibergall M, Porcelli F, Muretta JM, Thomas DD, Gao J, Blumenthal DK, Taylor SS, Veglia G. </i> Elife, 2020","reference_id":"32338601","region_id":"DP00015r025","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The PKA-C/PKIα complex relaxes through two structurally and kinetically distinct states to form the complex","_id":"685af522b4ac24d5329d709b"},{"type":"Results","text":"To determine the mechanism of binding PKA-C and PKIα, we utilized stopped-flow rapid mixing fluorescence resonance energy transfer (FRET) and analyzed transient and total changes in donor fluorescence during the binding reaction.","_id":"685af522b4ac24d5329d709c"},{"type":"Results","text":"From an initial analysis of the binding curve, we found that the total fluorescence of the Alexa-488 donor emission from the PKA-CDONOR/PKIACCEPTOR changed bi-exponentially through the course of the binding reactions (Figure 6A–D). The bi-exponential behavior suggests the presence of an initial fast binding step followed by a slow structural rearrangement (Table 1; Gianni et al., 2014).","_id":"685af522b4ac24d5329d709d"},{"type":"Figure","text":"Multi-pathway mechanism of PKIα binding to PKA-C revealed by stopped-flow FRET experiments.","_id":"685af522b4ac24d5329d709e"},{"type":"Results","text":"The pre-exponential amplitudes for the fast phases increased hyperbolically, while the slow phase decreased hyperbolically (Figure 6D–H). Taken together, the behavior of the rate constants and the pre-exponential amplitudes for the fast and slow phases are consistent with a multi-pathway mechanism in which there is a fast binding phase of PKIα ensembles competent for binding and a subsequent structural rearrangement of these conformers upon binding (Dogan et al., 2014; Gianni et al., 2014).","_id":"685af522b4ac24d5329d709f"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","uniprot_changed":true,"version":4,"_id":"685af522b4ac24d5329d709a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-08T13:39:08.704Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001183","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":76,"interaction_partner":[{"db":"UniProt","id":"Q9DBC7","operator":"and","partner_start":null,"partner_end":null,"_id":"685af522b4ac24d5329d70a7"}],"reference_html":"Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A. <i> Olivieri C, Wang Y, Li GC, V S M, Kim J, Stultz BR, Neibergall M, Porcelli F, Muretta JM, Thomas DD, Gao J, Blumenthal DK, Taylor SS, Veglia G. </i> Elife, 2020","reference_id":"32338601","region_id":"DP00015r026","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The PKA-C/PKIα complex relaxes through two structurally and kinetically distinct states to form the complex","_id":"685af522b4ac24d5329d70a2"},{"type":"Results","text":"To determine the mechanism of binding PKA-C and PKIα, we utilized stopped-flow rapid mixing fluorescence resonance energy transfer (FRET) and analyzed transient and total changes in donor fluorescence during the binding reaction.","_id":"685af522b4ac24d5329d70a3"},{"type":"Results","text":"From an initial analysis of the binding curve, we found that the total fluorescence of the Alexa-488 donor emission from the PKA-CDONOR/PKIACCEPTOR changed bi-exponentially through the course of the binding reactions (Figure 6A–D). The bi-exponential behavior suggests the presence of an initial fast binding step followed by a slow structural rearrangement (Table 1; Gianni et al., 2014).","_id":"685af522b4ac24d5329d70a4"},{"type":"Figure","text":"Multi-pathway mechanism of PKIα binding to PKA-C revealed by stopped-flow FRET experiments.","_id":"685af522b4ac24d5329d70a5"},{"type":"Results","text":"The pre-exponential amplitudes for the fast phases increased hyperbolically, while the slow phase decreased hyperbolically (Figure 6D–H). Taken together, the behavior of the rate constants and the pre-exponential amplitudes for the fast and slow phases are consistent with a multi-pathway mechanism in which there is a fast binding phase of PKIα ensembles competent for binding and a subsequent structural rearrangement of these conformers upon binding (Dogan et al., 2014; Gianni et al., 2014).","_id":"685af522b4ac24d5329d70a6"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","uniprot_changed":true,"version":4,"_id":"685af522b4ac24d5329d70a1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":76,"interaction_partner":[],"reference_html":"Expression in Escherichia coli and characterization of the heat-stable inhibitor of the cAMP-dependent protein kinase. <i> Thomas J, Van Patten SM, Howard P, Day KH, Mitchell RD, Sosnick T, Trewhella J, Walsh DA, Maurer RA. </i> J Biol Chem, 1991","reference_id":"2040607","region_id":"DP00015r028","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"The heat-stable inhibitor of the CAMP-dependent protein kinase is a small protein which binds to the catalytic subunit of the kinase and inhibits its activity (1, 2)","_id":"685af522b4ac24d5329d70ac"},{"type":"Results","text":"PKI was further purified by ion exchange and gel exclusion chromatography. Again, the purification was monitored by analysis of PKI activity (Fig. 2) and SDS-polyacrylamide gel electrophoresis (Fig. 3). Most of the PKI activity which could be recovered was found to elute in the 100-300 mM fraction on DEAE-chromatography, and gel electrophoresis suggested the presence of only minor contaminants at this stage of the purification. The minor contaminants were readily removed by chromatography on Sephadex G-50 yielding an apparently homogeneous preparation. The results of a typical purification are summarized in Table I. Starting from 6 liters of bacterial culture, a final preparation of 14 mg of purified PKI was obtained with an apparent overall yield of 9%. While analysis of activity suggests that only a 12.8-fold purification was necessary, this is probably an underestimate due to the presence of nonspecific inhibitory activity present in the crude extracts. The recovery was good for most steps, except for the Sephadex G-50 columns. Somewhat low recovery was encountered at this step because of the need to utilize only the peak fractions to avoid contamination with other small proteins. Characteristics of Bacterially Expressed PKI-The bacterially expressed PKI exhibited inhibitory potency identical to that of the native skeletal muscle protein. Both equally titrate the activity of pure CAMP-dependent protein kinase and exhibit identical specific activities (Fig. 4a). Henderson analysis (23) yielded K, values of 0.098 nM for the bacterial protein compared to 0.085 nM for the native protein; these values are identical within experimental error (Fig. 46)","_id":"685af522b4ac24d5329d70ad"},{"type":"Results","text":"The bacterially expressed PKI exhibited inhibitory potency identical to that of the native skeletal muscle protein. Both equally titrate the activity of pure CAMP-dependent protein kinase and exhibit identical specific activities (Fig. 4a)","_id":"685af522b4ac24d5329d70ae"},{"type":"Discussion","text":"The inhibitory activity of bacterially expressed PKI is indistinguishable from that of the native skeletal muscle protein (Fig. 4).","_id":"685af522b4ac24d5329d70af"},{"type":"Methods","text":"Gel electrophoresis characterization of bacterially-expressed and native PKIs. Analysis of PKI activity by SDS gel electrophoresis.","_id":"685af522b4ac24d5329d70b0"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_id":"GO:0140678","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","uniprot_changed":true,"version":3,"_id":"685af522b4ac24d5329d70ab","reference_source":"pmid"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":24,"type":"T"},{"start":25,"end":37,"type":"D"},{"start":38,"end":47,"type":"T"},{"start":48,"end":76,"type":"D"}],"Structural state":[{"start":1,"end":76,"type":"D"}],"Structural transition":[{"start":1,"end":24,"type":"T"},{"start":38,"end":47,"type":"T"}],"Molecular function":[{"start":1,"end":76,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02234","name":"Cyclin-dependent kinase inhibitor","start":21,"end":68}],"gene3D":[{"start":14,"end":89,"id":"4.10.365.10","name":"p27"}]},"uniref50":"UniRef50_P38936","sequence":"MSEPAGDVRQNPCGSKACRRLFGPVDSEQLSRDCDALMAGCIQEARERWNFDFVTETPLEGDFAWERVRGLGLPKLYLPTGPRRGRDELGGGRRPGTSPALLQGTAEEDHVDLSLSCTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P38936","disprot_id":"DP00016","ncbi_taxon_id":9606,"regions_counter":42,"creator":"bleon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":164,"region_id":"DP00016r001","released":"2022_03","ec_id":"ECO:0007689","reference_html":"Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. <i> Kriwacki RW, Hengst L, Tennant L, Reed SI, Wright PE. </i> Proc Natl Acad Sci U S A, 1996","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"8876165","version":3,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Further, no difference in the protease maps was observed in the absence or presence of urea (2.0 M and 4.0 M), as judged using SDS/PAGE and HPLC (data not shown), providing further evidence that p21-F lacks stable structured domains.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-14T17:08:06.968Z"},"uniprot_changed":true,"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":164,"region_id":"DP00016r002","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. <i> Kriwacki RW, Hengst L, Tennant L, Reed SI, Wright PE. </i> Proc Natl Acad Sci U S A, 1996","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"8876165","version":3,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Detailed analysis of trypsin cleavage products using MALDI mass spectrometry (22) showed that p21-F is cleaved at all predicted trypsin sites (Fig.1B) and reveals that globular protease-resistant domains do not exist.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-14T17:08:06.163Z"},"uniprot_changed":true,"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":164,"region_id":"DP00016r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. <i> Kriwacki RW, Hengst L, Tennant L, Reed SI, Wright PE. </i> Proc Natl Acad Sci U S A, 1996","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"8876165","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"CD spectropolarimetry was used to investigate the secondary structure of the p21 NH2 terminus. CD spectra for p21-F, -A, and -B are very similar (Fig.3A) and indicate that (i) despite the clear demonstration of Cdk inhibitory activity, p21 and its fragments possess very little regular secondary structure, and (ii) the lack of secondary structure within the NH2-terminal fragments is not due to a requirement that COOH-terminal domains be present to promote a stable fold.","type":"Results"},{"text":"The CD data thus indicate that p21 does not exhibit the characteristic cooperative unfolding behavior expected of a globular protein but rather provide further evidence that the protein is highly flexible and disordered in the free solution state.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-14T17:08:04.126Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":94,"region_id":"DP00016r006","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. <i> Kriwacki RW, Hengst L, Tennant L, Reed SI, Wright PE. </i> Proc Natl Acad Sci U S A, 1996","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"8876165","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The 1H-15N correlation spectrum of p21-A (Fig.4A) reveals resonances that are clustered with in a narrow chemical shift range (total 1H chemical shift dispersion of backbone amides 0.80 ppm) and indicates that the chemical environment of each amide group, as reported by 1H and 15N chemical shifts, is influenced predominantly by the chemical nature of its own amino acid side chain and not by long-range effects due to secondary or tertiary structure. The spectrum lacks the chemical shift dispersion expected for a folded globular protein.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-14T17:08:03.184Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":84,"term_name":"disorder to order","start":9,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"8876165","version":3,"reference_html":"Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. <i> Kriwacki RW, Hengst L, Tennant L, Reed SI, Wright PE. </i> Proc Natl Acad Sci U S A, 1996","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00016r008","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In sharp contrast to the disordered free state, however, the p21 NH2 terminus adopts an ordered stable conformation when bound to Cdk2, as shown directly by NMR spectroscopy. We have, thus, identified a striking disorder-order transition for p21 upon binding to one of its biological targets, Cdk2. This structural transition has profound implications in light of the ability of p21 to bind and inhibit a diverse family of cyclin-Cdk complexes, including cyclin A-Cdk2, cyclin E-Cdk2, and cyclin D-Cdk4.","type":"Abstract"},{"text":"The conformational state of p21-B, which is 18 amino acids shorter than p21-A but has similar biochemical activity (Fig.2), is dramatically changed upon addition of a stoichiometric amount of unlabeled Cdk2, as revealed by 1H-15N correlated spectra (Fig.5). Upon binding to Cdk2 (Fig.SB), there is a large increase in resonance dispersion (total 1H chemical shift dispersion of backbone amides ≈ 1.25 ppm).","type":"Results"},{"text":"Representative 15N line widths at half height for Cdk2-bound p21-B range from 9Hz to 16Hz, consistent with a monodisperse 44-kDa protein-protein complex.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-14T17:08:08.962Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":84,"term_name":"protein binding","start":9,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"8876165","version":4,"reference_html":"Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. <i> Kriwacki RW, Hengst L, Tennant L, Reed SI, Wright PE. </i> Proc Natl Acad Sci U S A, 1996","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00016r009","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In sharp contrast to the disordered free state, however, the p21 NH2 terminus adopts an ordered stable conformation when bound to Cdk2, as shown directly by NMR spectroscopy. We have, thus, identified a striking disorder-order transition for p21 upon binding to one of its biological targets, Cdk2. This structural transition has profound implications in light of the ability of p21 to bind and inhibit a diverse family of cyclin-Cdk complexes, including cyclin A-Cdk2, cyclin E-Cdk2, and cyclin D-Cdk4.","type":"Abstract"},{"text":"The conformational state of p21-B, which is 18 amino acids shorter than p21-A but has similar biochemical activity (Fig.2), is dramatically changed upon addition of a stoichiometric amount of unlabeled Cdk2, as revealed by 1H-15N correlated spectra (Fig.5). Upon binding to Cdk2 (Fig.SB), there is a large increase in resonance dispersion (total 1H chemical shift dispersion of backbone amides ≈ 1.25 ppm).","type":"Results"},{"text":"Representative 15N line widths at half height for Cdk2-bound p21-B range from 9Hz to 16Hz, consistent with a monodisperse 44-kDa protein-protein complex.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-14T17:08:13.623Z"},"uniprot_changed":true,"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":9,"end":84,"reference_id":"8876165","reference_source":"pmid","reference_html":"Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. <i> Kriwacki RW, Hengst L, Tennant L, Reed SI, Wright PE. </i> Proc Natl Acad Sci U S A, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00016r012","statement":[{"text":"CD spectropolarimetry was used to investigate the secondary structure of the p21 NH2 terminus. CD spectra for p21-F, -A, and -B are very similar (Fig.3A) and indicate that (i) despite the clear demonstration of Cdk inhibitory activity, p21 and its fragments possess very little regular secondary structure, and (ii) the lack of secondary structure within the NH2-terminal fragments is not due to a requirement that COOH-terminal domains be present to promote a stable fold.","type":"Results"},{"text":"The CD data thus indicate that p21 does not exhibit the characteristic cooperative unfolding behavior expected of a globular protein but rather provide further evidence that the protein is highly flexible and disordered in the free solution state.","type":"Results"},{"text":"Fragment corresponding to p21-B.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-14T17:08:01.115Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":94,"reference_id":"8876165","reference_source":"pmid","reference_html":"Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. <i> Kriwacki RW, Hengst L, Tennant L, Reed SI, Wright PE. </i> Proc Natl Acad Sci U S A, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00016r013","statement":[{"text":"CD spectropolarimetry was used to investigate the secondary structure of the p21 NH2 terminus. CD spectra for p21-F, -A, and -B are very similar (Fig.3A) and indicate that (i) despite the clear demonstration of Cdk inhibitory activity, p21 and its fragments possess very little regular secondary structure, and (ii) the lack of secondary structure within the NH2-terminal fragments is not due to a requirement that COOH-terminal domains be present to promote a stable fold.","type":"Results"},{"text":"The CD data thus indicate that p21 does not exhibit the characteristic cooperative unfolding behavior expected of a globular protein but rather provide further evidence that the protein is highly flexible and disordered in the free solution state.","type":"Results"},{"text":"Fragment corresponding to p21-F.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-14T17:07:59.422Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":94,"reference_id":"8876165","reference_source":"pmid","reference_html":"Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. <i> Kriwacki RW, Hengst L, Tennant L, Reed SI, Wright PE. </i> Proc Natl Acad Sci U S A, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00016r014","statement":[{"text":"The inhibitory activity of p21-F, -A, and -B toward Cdks was tested in vitro using cyclin A-Cdk2 purified from HeLa cells by immunoprecipitation and using histone H1 as the kinase substrate. The concentration producing 50% inhibition for all three p21 proteins is between 32 pM and 320 pM (Fig.2A). Cdk2 inhibitory activity was tested at 32 nM under the solution conditions used for structural studies (vide infra), including (i) high ionic strength, pH 7.0 (Fig.2A, B Left, and C Left), (ii) high ionic strength with sodium thiocyanate, pH 7.0 (Fig.2A, B Middle, and C Middle), and (iii) low ionic strength, pH 5.0 (Fig.2A, B Right, and C Right). Cdk2 kinase activity is diminished under conditions ii and iii compared with condition i (Fig.2B); significantly, however, p21-F, -A, and -B are potent Cdk2 inhibitors under all solution conditions (Fig.2C).","type":"Results"},{"text":"Fragment corresponding to p21-A.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-14T17:08:17.096Z"},"uniprot_changed":true,"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":94,"reference_id":"8876165","reference_source":"pmid","reference_html":"Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. <i> Kriwacki RW, Hengst L, Tennant L, Reed SI, Wright PE. </i> Proc Natl Acad Sci U S A, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00016r015","statement":[{"text":"The inhibitory activity of p21-F, -A, and -B toward Cdks was tested in vitro using cyclin A-Cdk2 purified from HeLa cells by immunoprecipitation and using histone H1 as the kinase substrate. The concentration producing 50% inhibition for all three p21 proteins is between 32 pM and 320 pM (Fig.2A). Cdk2 inhibitory activity was tested at 32 nM under the solution conditions used for structural studies (vide infra), including (i) high ionic strength, pH 7.0 (Fig.2A, B Left, and C Left), (ii) high ionic strength with sodium thiocyanate, pH 7.0 (Fig.2A, B Middle, and C Middle), and (iii) low ionic strength, pH 5.0 (Fig.2A, B Right, and C Right). Cdk2 kinase activity is diminished under conditions ii and iii compared with condition i (Fig.2B); significantly, however, p21-F, -A, and -B are potent Cdk2 inhibitors under all solution conditions (Fig.2C).","type":"Results"},{"text":"Fragment corresponding to p21-A.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-14T17:08:12.128Z"},"uniprot_changed":true,"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":9,"end":84,"reference_id":"8876165","reference_source":"pmid","reference_html":"Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. <i> Kriwacki RW, Hengst L, Tennant L, Reed SI, Wright PE. </i> Proc Natl Acad Sci U S A, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00016r016","statement":[{"text":"The inhibitory activity of p21-F, -A, and -B toward Cdks was tested in vitro using cyclin A-Cdk2 purified from HeLa cells by immunoprecipitation and using histone H1 as the kinase substrate. The concentration producing 50% inhibition for all three p21 proteins is between 32 pM and 320 pM (Fig.2A). Cdk2 inhibitory activity was tested at 32 nM under the solution conditions used for structural studies (vide infra), including (i) high ionic strength, pH 7.0 (Fig.2A, B Left, and C Left), (ii) high ionic strength with sodium thiocyanate, pH 7.0 (Fig.2A, B Middle, and C Middle), and (iii) low ionic strength, pH 5.0 (Fig.2A, B Right, and C Right). Cdk2 kinase activity is diminished under conditions ii and iii compared with condition i (Fig.2B); significantly, however, p21-F, -A, and -B are potent Cdk2 inhibitors under all solution conditions (Fig.2C).","type":"Results"},{"text":"Fragment corresponding to p21-B.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-14T17:08:11.342Z"},"uniprot_changed":true,"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":9,"end":84,"reference_id":"8876165","reference_source":"pmid","reference_html":"Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. <i> Kriwacki RW, Hengst L, Tennant L, Reed SI, Wright PE. </i> Proc Natl Acad Sci U S A, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00016r017","statement":[{"text":"The inhibitory activity of p21-F, -A, and -B toward Cdks was tested in vitro using cyclin A-Cdk2 purified from HeLa cells by immunoprecipitation and using histone H1 as the kinase substrate. The concentration producing 50% inhibition for all three p21 proteins is between 32 pM and 320 pM (Fig.2A). Cdk2 inhibitory activity was tested at 32 nM under the solution conditions used for structural studies (vide infra), including (i) high ionic strength, pH 7.0 (Fig.2A, B Left, and C Left), (ii) high ionic strength with sodium thiocyanate, pH 7.0 (Fig.2A, B Middle, and C Middle), and (iii) low ionic strength, pH 5.0 (Fig.2A, B Right, and C Right). Cdk2 kinase activity is diminished under conditions ii and iii compared with condition i (Fig.2B); significantly, however, p21-F, -A, and -B are potent Cdk2 inhibitors under all solution conditions (Fig.2C).","type":"Results"},{"text":"Fragment corresponding to p21-B.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-14T17:08:16.238Z"},"uniprot_changed":true,"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":164,"reference_id":"8876165","reference_source":"pmid","reference_html":"Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. <i> Kriwacki RW, Hengst L, Tennant L, Reed SI, Wright PE. </i> Proc Natl Acad Sci U S A, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00016r018","statement":[{"text":"The inhibitory activity of p21-F, -A, and -B toward Cdks was tested in vitro using cyclin A-Cdk2 purified from HeLa cells by immunoprecipitation and using histone H1 as the kinase substrate. The concentration producing 50% inhibition for all three p21 proteins is between 32 pM and 320 pM (Fig.2A). Cdk2 inhibitory activity was tested at 32 nM under the solution conditions used for structural studies (vide infra), including (i) high ionic strength, pH 7.0 (Fig.2A, B Left, and C Left), (ii) high ionic strength with sodium thiocyanate, pH 7.0 (Fig.2A, B Middle, and C Middle), and (iii) low ionic strength, pH 5.0 (Fig.2A, B Right, and C Right). Cdk2 kinase activity is diminished under conditions ii and iii compared with condition i (Fig.2B); significantly, however, p21-F, -A, and -B are potent Cdk2 inhibitors under all solution conditions (Fig.2C).","type":"Results"},{"text":"Fragment corresponding to p21-F.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-14T17:08:14.632Z"},"uniprot_changed":true,"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":164,"reference_id":"8876165","reference_source":"pmid","reference_html":"Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. <i> Kriwacki RW, Hengst L, Tennant L, Reed SI, Wright PE. </i> Proc Natl Acad Sci U S A, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00016r019","statement":[{"text":"The inhibitory activity of p21-F, -A, and -B toward Cdks was tested in vitro using cyclin A-Cdk2 purified from HeLa cells by immunoprecipitation and using histone H1 as the kinase substrate. The concentration producing 50% inhibition for all three p21 proteins is between 32 pM and 320 pM (Fig.2A). Cdk2 inhibitory activity was tested at 32 nM under the solution conditions used for structural studies (vide infra), including (i) high ionic strength, pH 7.0 (Fig.2A, B Left, and C Left), (ii) high ionic strength with sodium thiocyanate, pH 7.0 (Fig.2A, B Middle, and C Middle), and (iii) low ionic strength, pH 5.0 (Fig.2A, B Right, and C Right). Cdk2 kinase activity is diminished under conditions ii and iii compared with condition i (Fig.2B); significantly, however, p21-F, -A, and -B are potent Cdk2 inhibitors under all solution conditions (Fig.2C).","type":"Results"},{"text":"Fragment corresponding to p21-F.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-14T17:08:09.719Z"},"uniprot_changed":true,"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":164,"reference_id":"22869755","reference_source":"pmid","reference_html":"Cyclin-dependent kinase 8 mediates chemotherapy-induced tumor-promoting paracrine activities. <i> Porter DC, Farmaki E, Altilia S, Schools GP, West DK, Chen M, Chang BD, Puzyrev AT, Lim CU, Rokow-Kittell R, Friedhoff LT, Papavassiliou AG, Kalurupalle S, Hurteau G, Shi J, Baran PS, Gyorffy B, Wentland MP, Broude EV, Kiaris H, Roninson IB. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0001934","term_name":"positive regulation of protein phosphorylation","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0005648","ec_ontology":"ECO","ec_name":"luciferase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00016r020","statement":[{"text":"Surprisingly, we have found that p21 stimulates CDK8 kinase activity. p21 activation of CDK8, leading to transcriptional stimulation, stands in striking contrast to its inhibition of CDK2, the cell-cycle regulator primarily responsible for the ability of p21 to stop cell-cycle progression.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-14T10:40:59.735Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to amino acids within a protein.\" [GOC:hjd]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":164,"reference_id":"7958916","reference_source":"pmid","reference_html":"DNA damage triggers a prolonged p53-dependent G1 arrest and long-term induction of Cip1 in normal human fibroblasts. <i> Di Leonardo A, Linke SP, Clarkin K, Wahl GM. </i> Genes Dev, 1994","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0001933","term_name":"negative regulation of protein phosphorylation","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP00016r021","statement":[{"text":"Thus, inactivation of Cdks by sustained expression of p21 may be the biochemical mechanism underlying the observed long-term cell cycle arrest.","type":"Discussion"},{"text":"Here, we present results that strongly suggest that this subunit mediates PCNA binding to DNA polymerase δ and corresponds to the subunit whose interaction with PCNA is targeted by p21Cip1.","type":"Abstract"}],"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that stops, prevents or reduces the rate of addition of phosphate groups to amino acids within a protein.\" [GOC:hjd]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-22T18:19:00.387Z"}},{"start":1,"end":164,"reference_id":"23026136","reference_source":"pmid","reference_html":"E3 ubiquitin ligase RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation. <i> Zhi X, Zhao D, Wang Z, Zhou Z, Wang C, Chen W, Liu R, Chen C. </i> Cancer Res, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"Q9BV68","partner_start":null,"partner_end":null}],"region_id":"DP00016r022","statement":[{"text":"We showed that RNF126 interacts with p21 and RNF126 overexpression increased p21\nprotein ubiquitination in an E3 ligase activity-dependent manner. ","type":"Abstract"},{"text":"When\nFlag-RNF126 was immunoprecipitated by anti-Flag Ab, the\nendogenous p21 protein could be detected in the protein\ncomplex (Fig. 3A). In addition, the protein–protein interaction\nbetween endogenous RNF126 and endogenous p21 was\ndetected in MDA-MB-231 (Fig. 3B). These results suggest that\nRNF126 and p21 proteins interact with each other under\nphysiologic conditions. ","type":"Results"},{"text":"RNF126 and p21 proteins interact with each other.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-14T10:08:02.225Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":164,"reference_id":"23026136","reference_source":"pmid","reference_html":"E3 ubiquitin ligase RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation. <i> Zhi X, Zhao D, Wang Z, Zhou Z, Wang C, Chen W, Liu R, Chen C. </i> Cancer Res, 2013","date":"2022-02-21T16:02:29.012Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000046","term_name":"ubiquitination display site","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0005644","ec_ontology":"ECO","ec_name":"immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00016r023","statement":[{"text":"These findings suggest that RNF126 promotes cancer cell proliferation by targeting p21 for ubiquitin-mediated degradation.","type":"Abstract"}],"ec_go":"IPI","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-22T18:18:54.104Z"}},{"start":139,"end":160,"reference_id":"11595739","reference_source":"pmid","reference_html":"Mediation of proliferating cell nuclear antigen (PCNA)-dependent DNA replication through a conserved p21(Cip1)-like PCNA-binding motif present in the third subunit of human DNA polymerase delta. <i> Ducoux M, Urbach S, Baldacci G, Hübscher U, Koundrioukoff S, Christensen J, Hughes P. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005581","ec_ontology":"ECO","ec_name":"enzyme-linked immunoabsorbent assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"interaction_partner":[{"db":"UniProt","id":"Q15054","partner_start":null,"partner_end":null}],"region_id":"DP00016r024","statement":[{"text":"To demonstrate p21Cip1 inhibition of the binding of the C-terminal domain of p66 to PCNA, the wells were coated with a streptavidin-biotinated p66 peptide complex by adding 50 μl of 20 μg/ml streptavidin plus 100 ng of biotinated p66 peptide in PBS to each well for 1 h.","type":"Methods"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-22T18:18:43.576Z"}},{"start":139,"end":160,"reference_id":"11595739","reference_source":"pmid","reference_html":"Mediation of proliferating cell nuclear antigen (PCNA)-dependent DNA replication through a conserved p21(Cip1)-like PCNA-binding motif present in the third subunit of human DNA polymerase delta. <i> Ducoux M, Urbach S, Baldacci G, Hübscher U, Koundrioukoff S, Christensen J, Hughes P. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0140311","term_name":"protein sequestering activity","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0007738","ec_ontology":"ECO","ec_name":"protein detection assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met147Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"A similar peptide (mutant p21 peptide) containing the entire C-terminal region of p21 Cip1 but with a substitution of isoleucine for alanine within the consensus PCNA-binding domain was ineffective, confirming previous results that this amino acid is critical for p21 Cip1 function"}]}],"region_id":"DP00016r025","sequence_construct":"GRKRRQTSMTDFYHSKRRLIFS","statement":[{"text":"Conversely, p66 interacts with the domain-interconnecting loop of PCNA, a region previously shown to be important for DNA polymerase delta activity and for binding of the cell cycle inhibitor p21 Cip1 . In accordance with this, a peptide containing the PCNA-binding domain of p21 Cip1 inhibited p66 binding to PCNA and the activity of native three-subunit DNA polymerase delta","type":"Abstract"},{"text":"In Fig. 4, we show that a peptide of 22 amino acids containing the PCNA-binding domain of p21 Cip1 inhibits both p66 peptide binding to PCNA and DNA synthesis by a mouse DNA polymerase delta fraction containing p66 (30) (Fig. 4B, inset).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-14T10:31:17.953Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a specific protein, to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:1493333]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":164,"reference_id":"10208428","reference_source":"pmid","reference_html":"Comparison of the effectiveness of adenovirus vectors expressing cyclin kinase inhibitors p16INK4A, p18INK4C, p19INK4D, p21(WAF1/CIP1) and p27KIP1 in inducing cell cycle arrest, apoptosis and inhibition of tumorigenicity. <i> Schreiber M, Muller WJ, Singh G, Graham FL. </i> Oncogene, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0008285","term_name":"negative regulation of cell population proliferation","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0005638","ec_ontology":"ECO","ec_name":"cell growth regulation assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00016r026","statement":[{"text":"Cell death was greatest in MT1A2 and A549 cells transduced with Ad vectors expressing p16, p18 and p27 (Figure 2 and Table 2), whereas p19 and p21 expression had a more cytostatic effect on cell proliferation. ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-14T10:09:05.895Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that stops, prevents or reduces the rate or extent of cell proliferation.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":164,"reference_id":"17553787","reference_source":"pmid","reference_html":"The cyclin-dependent kinase inhibitors p15INK4B and p21CIP1 are critical regulators of fibrillar collagen-induced tumor cell cycle arrest. <i> Wall SJ, Zhong ZD, DeClerck YA. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0140677","term_name":"molecular function activator activity","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0001585","ec_ontology":"ECO","ec_name":"small interfering RNA knockdown evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00016r027","statement":[{"text":"Additionally, we demonstrate that fibrillar collagen can also arrest cells at the G 2 phase, which is mediated in part by p21 CIP1","type":"Abstract"},{"text":"p21 CIP1 siRNA alone had a minimal effect on cell cycle distribution and did not significantly increase cell proliferation (data not shown), indicating that it is the cooperation between p15 INK4b and p21 CIP1 that is responsible for the cell cycle arrest observed when M24met cells are plated in the presence of FC. ","type":"Results"},{"text":"FC means fibrillar collagen\n","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-14T10:08:58.151Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":152,"end":158,"reference_id":"23213251","reference_source":"pmid","reference_html":"TRIM39 regulates cell cycle progression and DNA damage responses via stabilizing p21. <i> Zhang L, Mei Y, Fu NY, Guan L, Xie W, Liu HH, Yu CD, Yin Z, Yu VC, You H. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"Q9HCM9","partner_start":null,"partner_end":null}],"region_id":"DP00016r028","statement":[{"text":"Data from GST pull-down experiments suggest that the C-terminal region (amino acids 152–158) of p21 mediates TRIM39-p21 association (Fig. 2C). ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-14T10:05:59.710Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":164,"reference_id":"17420273","reference_source":"pmid","reference_html":"CDK4 and CDK6 delay senescence by kinase-dependent and p16INK4a-independent mechanisms. <i> Ruas M, Gregory F, Jones R, Poolman R, Starborg M, Rowe J, Brookes S, Peters G. </i> Mol Cell Biol, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"P11802","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q00534","partner_start":null,"partner_end":null}],"region_id":"DP00016r029","statement":[{"text":"Immunoprecipitation and immunoblotting confirmed that cyclin D1 and p21CIP1 were associated with CDK4 and CDK6 in complexes of this size (see Fig. S1 in the supplemental material; also data not shown).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-14T10:05:39.479Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":164,"reference_id":"23213251","reference_source":"pmid","reference_html":"TRIM39 regulates cell cycle progression and DNA damage responses via stabilizing p21. <i> Zhang L, Mei Y, Fu NY, Guan L, Xie W, Liu HH, Yu CD, Yin Z, Yu VC, You H. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"Q9HCM9","partner_start":null,"partner_end":null}],"region_id":"DP00016r030","statement":[{"text":"Mechanistically, TRIM39 interacts with p21, which subsequently prevents Cdt2 from binding to p21, therefore blocking ubiquitylation and proteasomal degradation of p21 mediated by CRL4(Cdt2) E3 ligase. ","type":"Abstract"},{"text":"To test if TRIM39 associates with endogenous p21 protein, we introduced TRIM39α-Myc or TRIM39β-Myc into HCT116 WT cells and then performed immunoprecipitation with anti-Myc antibody. The association between p21 and TRIM39α or TRIM39β was readily detected (Fig. 2B)","type":"Results"},{"text":"In this study, we identified TRIM39 as a binding partner of p21 in the nucleus. Exogenous TRIM39 stabilized p21 by preventing its ubiquitylation, whereas TRIM39 depletion resulted in destabilization of p21, which was accompanied by increased ubiquitylation.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-14T10:05:19.388Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":143,"end":147,"reference_id":"11463845","reference_source":"pmid","reference_html":"Akt-dependent phosphorylation of p21(Cip1) regulates PCNA binding and proliferation of endothelial cells. <i> Rössig L, Jadidi AS, Urbich C, Badorff C, Zeiher AM, Dimmeler S. </i> Mol Cell Biol, 2001","date":"2024-04-30T14:15:26.613Z","curator_id":"bleon","curator_name":"Beltina Leon","curator_orcid":"0000-0001-9322-9442","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr145Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To identify the phosphate acceptor amino acid,\nthe putative Akt site Thr 145 of p21Cip1 was replaced by alanine (p21 T145A). "}]},{"term_id":"MI:0522","term_name":"myc","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"A plasmid encoding the human p21Cip1 was cloned by PCR into the pcDNA3.1-Myc-His vector (Invitrogen)."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"A plasmid encoding the human p21Cip1 was cloned by PCR into the pcDNA3.1-Myc-His vector (Invitrogen)."}]}],"cross_refs":[{"db":"ELM","id":"MOD_PKB_1"}],"ec_go":"IMP","region_id":"DP00016r031","statement":[{"text":"Inactivation of Thr 145 markedly reduced the Akt-dependent phosphorylation of p21Cip1 (Fig.2A). This suggests that Thr 145 serves as the Akt phosphorylation acceptor amino acid.","type":"Results"},{"text":"This annotation refers to the phosphorylation of the Thr 145 residue, included in the consensus motif for Akt-mediated phosphorylation MOD_PKB_1 that comprises the residues 140 to 148.","type":"Curator statement"}],"term_comment":"","term_def":"\"The process of introducing a phosphate group on to a protein.\" [GOC:hb]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-30T14:19:02.478Z"}},{"start":143,"end":147,"reference_id":"11463845","reference_source":"pmid","reference_html":"Akt-dependent phosphorylation of p21(Cip1) regulates PCNA binding and proliferation of endothelial cells. <i> Rössig L, Jadidi AS, Urbich C, Badorff C, Zeiher AM, Dimmeler S. </i> Mol Cell Biol, 2001","date":"2024-04-30T14:15:57.998Z","curator_id":"bleon","curator_name":"Beltina Leon","curator_orcid":"0000-0001-9322-9442","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001202","ec_ontology":"ECO","ec_name":"in vitro protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0522","term_name":"myc","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"A plasmid encoding the human p21Cip1 was cloned by PCR into the pcDNA3.1-Myc-His vector (Invitrogen)."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"A plasmid encoding the human p21Cip1 was cloned by PCR into the pcDNA3.1-Myc-His vector (Invitrogen)."}]}],"cross_refs":[{"db":"ELM","id":"MOD_PKB_1"}],"ec_go":"IDA","region_id":"DP00016r032","statement":[{"text":"In vitro kinase assay analysis confirms that Akt and PKA both phosphorylate p21Cip1 at the same site (Thr 145) (Fig. ​2B). ","type":"Results"},{"text":"This annotation refers to the phosphorylation of the Thr 145 residue, included in the consensus motif for Akt-mediated phosphorylation MOD_PKB_1 that comprises the residues 140 to 148.","type":"Curator statement"}],"term_comment":"","term_def":"\"The process of introducing a phosphate group on to a protein.\" [GOC:hb]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-30T14:19:07.172Z"}},{"start":139,"end":160,"reference_id":"8861913","reference_source":"pmid","reference_html":"Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA. <i> Gulbis JM, Kelman Z, Hurwitz J, O'Donnell M, Kuriyan J. </i> Cell, 1996","date":"2024-04-30T13:22:12.864Z","curator_id":"bleon","curator_name":"Beltina Leon","curator_orcid":"0000-0001-9322-9442","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006222","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"ELM","id":"LIG_PCNA_PIPBox_1"},{"db":"PDB","id":"1AXC"}],"ec_go":"EXP","region_id":"DP00016r033","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P12004","statements":[{"type":"Methods","text":"A 1.5-fold molar excess of synthetic p21 peptide (139GRKRRQTSMTDFYHSKRRLIFS160) was incubated with human PCNA (20 mg/ml). "}]}],"statement":[{"text":"A 22 residue peptide is bound to each of the three PCNA subunits of the ring (Figure 1 and Figure 2). Binding of the p21 peptide to PCNA involves an extensive set of interactions spanning the entire length of the peptide and burying 2,242 Å2 of total surface area at the intermolecular interface (57% on the peptide, 43% on PCNA).","type":"Results"},{"text":"The PCNA binding motif LIG_PCNA_PIPBox_1 reported for the region spanning residues 144 to 153, is located within the annotated region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"P12004","operator":null,"partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-30T14:09:22.770Z"}},{"start":139,"end":143,"reference_id":"12417334","reference_source":"pmid","reference_html":"Identification of the nuclear localization signal of p21(cip1) and consequences of its mutation on cell proliferation. <i> Rodríguez-Vilarrupla A, Díaz C, Canela N, Rahn HP, Bachs O, Agell N. </i> FEBS Lett, 2002","date":"2024-04-30T13:33:26.696Z","curator_id":"bleon","curator_name":"Beltina Leon","curator_orcid":"0000-0001-9322-9442","term_id":"GO:0051170","term_name":"import into nucleus","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg140Ala","start":null,"end":null,"position":null,"statements":[{"type":"Figure","text":"NIH3T3 cells were transfected with p21WT, p21AAA140–142-AAA161–163, p21AAA140–142, p21AAA161–163 fused to either GFP or DsRed. "},{"type":"Results","text":"The following mutations were performed: p21AAA140–142-AAA161–163, p21AAA140–142, p21AAA161–163 (Fig. 1C)."},{"type":"Methods","text":"The p21AAA140–142-AAA161–163 and the p21AAA140–142 were obtained by two-stage PCR using megaprimers. The first PCR reaction was performed using a 45-mer middle forward oligonucleotide (5′-ggACCTggAgACTCTCAgggTgCggCCgCgCggCAgACCAgCATg-3′) carrying the corresponding mutations (shown in bold) and a reverse terminal oligonucleotide wild type or carrying the AAA161–163 mutation as shown above. The second PCR product was performed using the 32-mer initial forward oligonucleotide (for the full-length construct) or the 30-mer middle forward oligonucleotide (for the carboxy-terminal construct) and the first PCR product (megaprimer of 114 bp) as reverse mutated primer."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys141Ala","start":null,"end":null,"position":null,"statements":[{"type":"Figure","text":"NIH3T3 cells were transfected with p21WT, p21AAA140–142-AAA161–163, p21AAA140–142, p21AAA161–163 fused to either GFP or DsRed. "},{"type":"Results","text":"The following mutations were performed: p21AAA140–142-AAA161–163, p21AAA140–142, p21AAA161–163 (Fig. 1C)."},{"type":"Methods","text":"The p21AAA140–142-AAA161–163 and the p21AAA140–142 were obtained by two-stage PCR using megaprimers. The first PCR reaction was performed using a 45-mer middle forward oligonucleotide (5′-ggACCTggAgACTCTCAgggTgCggCCgCgCggCAgACCAgCATg-3′) carrying the corresponding mutations (shown in bold) and a reverse terminal oligonucleotide wild type or carrying the AAA161–163 mutation as shown above. The second PCR product was performed using the 32-mer initial forward oligonucleotide (for the full-length construct) or the 30-mer middle forward oligonucleotide (for the carboxy-terminal construct) and the first PCR product (megaprimer of 114 bp) as reverse mutated primer."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg142Ala","start":null,"end":null,"position":null,"statements":[{"type":"Figure","text":"NIH3T3 cells were transfected with p21WT, p21AAA140–142-AAA161–163, p21AAA140–142, p21AAA161–163 fused to either GFP or DsRed. "},{"type":"Results","text":"The following mutations were performed: p21AAA140–142-AAA161–163, p21AAA140–142, p21AAA161–163 (Fig. 1C)."},{"type":"Methods","text":"The p21AAA140–142-AAA161–163 and the p21AAA140–142 were obtained by two-stage PCR using megaprimers. The first PCR reaction was performed using a 45-mer middle forward oligonucleotide (5′-ggACCTggAgACTCTCAgggTgCggCCgCgCggCAgACCAgCATg-3′) carrying the corresponding mutations (shown in bold) and a reverse terminal oligonucleotide wild type or carrying the AAA161–163 mutation as shown above. The second PCR product was performed using the 32-mer initial forward oligonucleotide (for the full-length construct) or the 30-mer middle forward oligonucleotide (for the carboxy-terminal construct) and the first PCR product (megaprimer of 114 bp) as reverse mutated primer."}]},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"unspecified","statements":[{"type":"Figure","text":"NIH3T3 cells were transfected with p21WT, p21AAA140–142-AAA161–163, p21AAA140–142, p21AAA161–163 fused to either GFP or DsRed. "},{"type":"Methods","text":"Digestions with NdeI and HindIII allowed cloning into a modified pGEX-KG and digestions with EcoRI and BamHI allowed cloning into pDsRed and pEGFP-C1 (GFP, green fluorescent protein) (Clontech)."}]}],"cross_refs":[{"db":"ELM","id":"TRG_NLS_Bipartite_1"}],"ec_go":"IMP","region_id":"DP00016r034","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0594","statements":[{"type":"Results","text":"Wild-type p21 (p21WT) and the various mutations were fused to GFP or to DsRed and transfected to NIH3T3 (Fig. 2 ) and to COS (data not shown) cells in order to analyze subcellular localization."}],"entry_name":"3T3-Swiss"}],"statement":[{"text":"Here we identified the amino acids of p21 that are essential for its nuclear translocation and examined the consequences of their mutation. While the RKR140–142 sequence was essential for nuclear localization of p21, the KRK161–163 was not.","type":"Discussion"},{"text":"The annotated region is part of the TRG_NLS_Bipartite_1 motif associated with the nuclear localization signal (NLS), which has been described for the region spanning residues 142 to 158.","type":"Curator statement"}],"term_comment":"","term_def":"\"The directed movement of substances into the nucleus.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-30T14:11:08.127Z"}},{"start":143,"end":147,"reference_id":"11463845","reference_source":"pmid","reference_html":"Akt-dependent phosphorylation of p21(Cip1) regulates PCNA binding and proliferation of endothelial cells. <i> Rössig L, Jadidi AS, Urbich C, Badorff C, Zeiher AM, Dimmeler S. </i> Mol Cell Biol, 2001","date":"2024-04-30T14:07:30.954Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0032091","term_name":"negative regulation of protein binding","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr145Asp","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To characterize the role of Thr 145 phosphorylation for p21Cip1-PCNA complex formation, we used a phospho-mimetic p21Cip1 construct, where Thr 145 was replaced by aspartic acid (p21 T145D)."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"A plasmid encoding the human p21Cip1 was cloned by PCR into the pcDNA3.1-Myc-His vector  (Invitrogen)."}]},{"term_id":"MI:0522","term_name":"myc","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"A plasmid encoding the human p21Cip1 was cloned by PCR into the pcDNA3.1-Myc-His vector  (Invitrogen)."}]}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P12004","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P24941","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP00016r035","statement":[{"text":"Simulated p21Cip1 phosphorylation at Thr 145 completely prevented p21Cip1-PCNA binding, whereas the nonphosphorylatable p21 T145A construct displayed no change in PCNA binding compared to p21 wt (Fig. 4A and B).","type":"Results"},{"text":"Therefore, we designed additional p21Cip1 constructs carrying a mutation to an unphosphorylatable (S146A) or to a phosphomimetic amino acid (S146D) at position 146. Coimmunoprecipitation experiments confirmed that in mammalian cells stimulation of p21Cip1 phosphorylation at serine 146 indeed decreases PCNA binding (Fig. 4D). However, phosphorylation of p21Cip1 at the Akt phosphorylation site Thr 145 exerts a more pronounced inhibition of complex formation with PCNA than Ser 146 phosphorylation (Fig. 4D). Taken together, Akt regulates p21Cip1-PCNA binding via specific phosphorylation of the Thr 145 residue.","type":"Results"},{"text":"Simulation of p21Cip1 phosphorylation at Thr 145 (T145D) reduced Cdk2 binding in endothelial cells by 59% ± 15% (Fig. ​5A) and affected complex formation with Cdk4 to a minor degree (Fig. ​5B), whereas both p21 wt and the T145A construct complexed with Cdk2 and Cdk4 to similar extents (Fig. ​5).","type":"Results"},{"text":"Through the analysis of a mimetic mutant, the authors show the phosphorylation of the 145 residue is a potent inhibitor of the binding to both PCNA and CDK2.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of protein binding.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"For detection of Akt phosphorylation of p21Cip1 in vitro, COS cells were transfected with myc-tagged p21Cip1 constructs, and whole-cell lysates (1 mg/sample) were immunoprecipitated with anti-myc antibodies."}]}]},{"start":1,"end":164,"reference_id":"11463845","reference_source":"pmid","reference_html":"Akt-dependent phosphorylation of p21(Cip1) regulates PCNA binding and proliferation of endothelial cells. <i> Rössig L, Jadidi AS, Urbich C, Badorff C, Zeiher AM, Dimmeler S. </i> Mol Cell Biol, 2001","date":"2024-04-29T15:52:45.719Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0004861","term_name":"cyclin-dependent protein serine/threonine kinase inhibitor activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001218","ec_ontology":"ECO","ec_name":"in vivo protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr145Asp","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To characterize the role of Thr 145 phosphorylation for p21Cip1-PCNA complex formation, we used a phospho-mimetic p21Cip1 construct, where Thr 145 was replaced by aspartic acid (p21 T145D)."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"},{"term_id":"MI:0522","term_name":"myc","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P24941","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00016r036","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_2959","entry_name":"HUV-EC-C"}],"statement":[{"text":"Overexpression of p21Cip1 significantly reduced the kinase activity of Cdk2 (35% ± 6% of vector-transfected cells; P < 0.001). However, cells transfected with the Akt–phospho-mimetic p21Cip1 T145D construct displayed reduced inhibition of Cdk2 activity compared to cells overexpressing either p21 wt or the p21Cip1 T145A construct (Fig. 6C).","type":"Results"}],"term_comment":"","term_def":"\"Binds to and stops, prevents or reduces the activity of a cyclin-dependent protein serine/threonine kinase.\" [GOC:mah, GOC:pr]","term_is_obsolete":false,"term_not_annotate":false},{"start":143,"end":147,"reference_id":"11463845","reference_source":"pmid","reference_html":"Akt-dependent phosphorylation of p21(Cip1) regulates PCNA binding and proliferation of endothelial cells. <i> Rössig L, Jadidi AS, Urbich C, Badorff C, Zeiher AM, Dimmeler S. </i> Mol Cell Biol, 2001","date":"2024-04-30T14:16:30.485Z","curator_id":"bleon","curator_name":"Beltina Leon","curator_orcid":"0000-0001-9322-9442","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001218","ec_ontology":"ECO","ec_name":"in vivo protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0522","term_name":"myc","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"A plasmid encoding the human p21Cip1 was cloned by PCR into the pcDNA3.1-Myc-His vector (Invitrogen)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr145Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Transfection of Akt stimulated the incorporation of 32P in cells overexpressing the p21Cip1 wild type (p21 wt), whereas radioactive labeling of the T145A construct in response to Akt overexpression was markedly lower (Fig. 3C)."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"A plasmid encoding the human p21Cip1 was cloned by PCR into the pcDNA3.1-Myc-His vector (Invitrogen)."}]}],"cross_refs":[{"db":"ELM","id":"MOD_PKB_1"}],"region_id":"DP00016r037","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_2959","statements":[{"type":"Figure","text":"In vivo phosphorylation of p21Cip1. (A) Detection of phosphorylated p21Cip1 by immunoblot analysis of HUVEC extracts using a phospho-specific antibody against the Akt phosphorylation consensus motif. Right lane, effect of Ly294002 (10 μM) for 1 h before lysis."},{"type":"Figure","text":"(B) In vivo phosphorylation of p21Cip1 by a serum-induced, PI3K-sensitive mechanism. HUVEC were labeled with 32P and starved for 1 h in FCS-free medium before the addition of 10% phosphate-free FCS and Ly294002 (10 μM) for 30 min as indicated. Endogenous p21Cip1 was immunoprecipitated (IP) with anti-p21Cip1 antibodies."}],"entry_name":"HUV-EC-C"},{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0224","statements":[{"type":"Figure","text":"(C). In vivo phosphorylation of p21Cip1 by Akt. COS-7 cells overexpressing myc-tagged p21Cip1 constructs and vector (pcDNA3.1) or Akt constructs were labeled with 32P for 3 h, and p21Cip1 was immunoprecipitated with anti-myc antibodies. In panels B and C, representative autoradiographs are shown: lower panels, expression of p21Cip1 as a loading control."}],"entry_name":"CV-1 in Origin Simian-7"}],"statement":[{"text":"To confirm that phosphorylation of p21Cip1 at Thr 145 occurs in vivo, we labeled intact cells with [32P]orthophosphate. Stimulation with serum induced the incorporation of 32P into endogenous p21Cip1 (Fig.3B).","type":"Results"},{"text":"These results indicate that serum induces phosphorylation of the peptide 144QTSMTDFYHSK154, which contains the Akt site Thr 145, in a PI3K-dependent manner. Taken together, the present data demonstrate that Akt interacts with and phosphorylates p21Cip1 in vitro and in vivo at Thr 145.","type":"Results"},{"text":"This annotation refers to the phosphorylation of the Thr 145 residue, included in the consensus motif for Akt-mediated phosphorylation MOD_PKB_1 that comprises the residues 140 to 148.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-30T14:19:28.746Z"}},{"start":1,"end":164,"reference_id":"11463845","reference_source":"pmid","reference_html":"Akt-dependent phosphorylation of p21(Cip1) regulates PCNA binding and proliferation of endothelial cells. <i> Rössig L, Jadidi AS, Urbich C, Badorff C, Zeiher AM, Dimmeler S. </i> Mol Cell Biol, 2001","date":"2024-04-30T14:17:01.272Z","curator_id":"bleon","curator_name":"Beltina Leon","curator_orcid":"0000-0001-9322-9442","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0522","term_name":"myc","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"A plasmid encoding the human p21Cip1 was cloned by PCR into the pcDNA3.1-Myc-His vector (Invitrogen)."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"A plasmid encoding the human p21Cip1 was cloned by PCR into the pcDNA3.1-Myc-His vector (Invitrogen)."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P12004","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00016r038","statement":[{"text":"p21 wt binds to PCNA as shown by coimmunoprecipitation studies with anti-myc antibodies for immunoprecipitation of myc-tagged p21 wt followed by Western blotting against endogenous PCNA (Fig. ​4A), as well as by immunoblot analysis of p21 bound to immunoprecipitates of endogenous PCNA (Fig. 4B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-30T14:18:50.715Z"}},{"start":1,"end":164,"reference_id":"11463845","reference_source":"pmid","reference_html":"Akt-dependent phosphorylation of p21(Cip1) regulates PCNA binding and proliferation of endothelial cells. <i> Rössig L, Jadidi AS, Urbich C, Badorff C, Zeiher AM, Dimmeler S. </i> Mol Cell Biol, 2001","date":"2024-04-30T14:17:31.055Z","curator_id":"bleon","curator_name":"Beltina Leon","curator_orcid":"0000-0001-9322-9442","term_id":"GO:0070557","term_name":"PCNA-p21 complex","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0522","term_name":"myc","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"A plasmid encoding the human p21Cip1 was cloned by PCR into the pcDNA3.1-Myc-His vector (Invitrogen)."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"A plasmid encoding the human p21Cip1 was cloned by PCR into the pcDNA3.1-Myc-His vector (Invitrogen)."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P12004","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00016r039","statement":[{"text":"p21 wt binds to PCNA as shown by coimmunoprecipitation studies with anti-myc antibodies for immunoprecipitation of myc-tagged p21 wt followed by Western blotting against endogenous PCNA (Fig. ​4A), as well as by immunoblot analysis of p21 bound to immunoprecipitates of endogenous PCNA (Fig. 4B).","type":"Results"}],"term_comment":"","term_def":"\"A protein complex that contains the cyclin-dependent protein kinase inhibitor p21WAF1/CIP1 bound to PCNA; formation of the complex inhibits DNA replication.\" [GOC:mah, PMID:7911228, PMID:7915843]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-30T14:18:27.604Z"}},{"start":1,"end":164,"reference_id":"11463845","reference_source":"pmid","reference_html":"Akt-dependent phosphorylation of p21(Cip1) regulates PCNA binding and proliferation of endothelial cells. <i> Rössig L, Jadidi AS, Urbich C, Badorff C, Zeiher AM, Dimmeler S. </i> Mol Cell Biol, 2001","date":"2024-04-30T14:19:14.636Z","curator_id":"bleon","curator_name":"Beltina Leon","curator_orcid":"0000-0001-9322-9442","term_id":"GO:0120283","term_name":"protein serine/threonine kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P24941","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00016r040","statement":[{"text":"Simulation of p21Cip1 phosphorylation at Thr 145 (T145D) reduced Cdk2 binding in endothelial cells by 59% ± 15% (Fig. ​5A) and affected complex formation with Cdk4 to a minor degree (Fig. ​5B), whereas both p21 wt and the T145A construct complexed with Cdk2 and Cdk4 to similar extents (Fig. ​5).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein serine/threonine kinase.\" [GOC:krc, GOC:sl, PMID:28608965]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0522","term_name":"myc","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"A plasmid encoding the human p21Cip1 was cloned by PCR into the pcDNA3.1-Myc-His vector (Invitrogen)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr145Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Simulation of p21Cip1 phosphorylation at Thr 145 (T145D) reduced Cdk2 binding in endothelial cells by 59% ± 15% (Fig. ​5A) and affected complex formation with Cdk4 to a minor degree (Fig. ​5B), whereas both p21 wt and the T145A construct complexed with Cdk2 and Cdk4 to similar extents (Fig. 5)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr145Asp","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"The Akt–phospho-mimetic p21Cip1 T145D construct induced no further increase in cyclin D-Cdk4 assembly. However, prevention of p21Cip1 phosphorylation by Akt in cells transfected with the p21Cip1 T145A construct resulted in a significant decrease in cyclin D-Cdk complex formation (Fig. 6A and B). Overexpression of the p21Cip1 T145D and T145A constructs had no effect on cyclin E-Cdk2 assembly (data not shown)."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"A plasmid encoding the human p21Cip1 was cloned by PCR into the pcDNA3.1-Myc-His vector (Invitrogen)."}]}],"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_2959","statements":[{"type":"Figure","text":"Regulation of Cdk function by p21Cip1 phosphorylation at Thr 145. (A) Effect of p21Cip1 phosphorylation at Thr 145 on cyclin D-Cdk4 assembly. Endogenous cyclin D was detected in Cdk4 immunoprecipitates (IP) from HUVEC overexpressing the various Thr 145 constructs of p21Cip1 (n = 4)."}],"entry_name":"HUV-EC-C"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-30T14:19:26.165Z"}},{"start":1,"end":49,"reference_id":"28425505","reference_source":"pmid","reference_html":"Novel interactions of the von Hippel-Lindau (pVHL) tumor suppressor with the CDKN1 family of cell cycle inhibitors. <i> Minervini G, Lopreiato R, Bortolotto R, Falconieri A, Sartori G, Tosatto SCE. </i> Sci Rep, 2017","date":"2024-09-11T14:37:38.630Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005805","ec_ontology":"ECO","ec_name":"yeast 2-hybrid evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"DisProt","id":"DP00287r060"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P40337","operator":null,"partner_start":54,"partner_end":157}],"region_id":"DP00016r041","statement":[{"text":"The pVHL β-domain is able to bind any member of the CDKN1 family, as indicated by yeast cell growth (Fig. 4B, Supplementary Figures S5 and S7).","type":"Results"},{"text":"Yeast plasmids expressing either their N-terminal tail containing the CDI domain (p27-NT residues: 1–60; p21-NT: 1–49; p57-NT: 1–61) or the corresponding C-terminal moiety lacking the N-terminus (p27-ΔN residues: 61–198; p21-ΔN: 50–164; p57-ΔN: 62–316) were generated to test the effects of CDKN1 binding to pVHL30. As shown in Fig. 4D, loss of the p27 N-terminus clearly disrupts its ability to associate with pVHL30, as yeast cells expressing the C-terminus of p27 were all unable to grow in selective medium. Similar data have been also obtained for both p21 and p57 (Supplementary Figures S9 and S10), strongly supporting the notion that the CDI domain is responsible for CDKN1 binding to pVHL30.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0693","term_name":"Gal4 DNA-binding domain tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-18T10:50:48.168Z"}},{"start":1,"end":164,"reference_id":"28425505","reference_source":"pmid","reference_html":"Novel interactions of the von Hippel-Lindau (pVHL) tumor suppressor with the CDKN1 family of cell cycle inhibitors. <i> Minervini G, Lopreiato R, Bortolotto R, Falconieri A, Sartori G, Tosatto SCE. </i> Sci Rep, 2017","date":"2024-08-05T13:11:16.767Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"For each transfection, approximatively 5 μg of total DNA, i.e. pcDNA3.1-derived plasmids (empty, and/or expressing either HA-pVHL30 or FLAG-CDKN1) were used"}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P40337","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00016r042","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063\t","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"Our data (Fig. 2B) indicates that all three CDKN1 proteins were able to interact with pVHL30, as demonstrated by their presence in the immunoprecipitate revealed with the anti-Flag antibody (bottom panels). Taken together, the experiments show that these proteins can form at least binary complexes in human, and notably kidney cells.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"cross_refs":[{"db":"DisProt","id":"DP00287r063"}]}],"released":"2016_10","uniref100":"UniRef100_P38936","date":"2016-08-23T15:25:23.000Z","acc":"P38936","name":"Cyclin-dependent kinase inhibitor 1","length":164,"organism":"Homo sapiens","dataset":["Cancer-related proteins","Autophagy-related proteins"],"uniparc":"UPI00004E1857","UniParc":"UPI00004E1857","genes":[{"name":{"value":"CDKN1A"},"synonyms":[{"value":"CAP20"},{"value":"CDKN1"},{"value":"CIP1"},{"value":"MDA6"},{"value":"PIC1"},{"value":"SDI1"},{"value":"WAF1"}]}],"alphafold_very_low_content":0.2621951219512195,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":8,"type":"D"},{"start":9,"end":84,"type":"T"},{"start":85,"end":164,"type":"D"}],"Structural state":[{"start":1,"end":164,"type":"D"}],"Structural transition":[{"start":9,"end":84,"type":"T"}],"Molecular function":[{"start":1,"end":164,"type":"F"}],"Biological process":[{"start":1,"end":164,"type":"F"}],"Disorder function":[{"start":1,"end":164,"type":"F"}],"Cellular component":[{"start":1,"end":164,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02234","name":"Cyclin-dependent kinase inhibitor","start":32,"end":82}],"gene3D":[{"start":25,"end":104,"id":"4.10.365.10","name":"p27"}]},"uniref50":"UniRef50_P49918","sequence":"MSDASLRSTSTMERLVARGTFPVLVRTSACRSLFGPVDHEELSRELQARLAELNAEDQNRWDYDFQQDMPLRGPGRLQWTEVDSDSVPAFYRETVQVGRCRLLLAPRPVAVAVAVSPPLEPAAESLDGLEEAPEQLPSVPVPAPASTPPPVPVLAPAPAPAPAPVAAPVAAPVAVAVLAPAPAPAPAPAPAPAPVAAPAPAPAPAPAPAPAPAPAPDAAPQESAEQGANQGQRGQEPLADQLHSGISGRPAAGTAAASANGAAIKKLSGPLISDFFAKRKRSAPEKSSGDVPAPCPSPSAAPGVGSVEQTPRKRLR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P49918","disprot_id":"DP00017","ncbi_taxon_id":9606,"regions_counter":19,"creator":"ewagner","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":316,"region_id":"DP00017r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Intrinsic structural disorder and sequence features of the cell cycle inhibitor p57Kip2. <i> Adkins JN, Lumb KJ. </i> Proteins, 2002","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11746698","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The CD spectrum of p57 lacks the features that are characteristic of helical or β-sheet secondary structure and instead exhibits a strong negative band at approximately 203 nm that is reminiscent of an unfolded protein [Fig. 3(A)].","type":"Results"},{"text":"The CD spectra at 5 and 80°C are characteristic of an unfolded protein.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-14T11:07:08.487Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":316,"region_id":"DP00017r004","released":"2022_03","ec_id":"ECO:0001249","reference_html":"Intrinsic structural disorder and sequence features of the cell cycle inhibitor p57Kip2. <i> Adkins JN, Lumb KJ. </i> Proteins, 2002","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11746698","version":3,"ec_name":"fluorescence evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Fluorescence emission spectrum of p57 (10 mM sodium phosphate, 50 mM NaCl, 1 mM DTT, pH 7.0, 30°C). The spectrum, collected with excitation at 280 nm, is characteristic of a solvent-exposed, unfolded protein.","type":"Figure"},{"text":"The fluorescence emission spectrum exhibits a maximum at 350 nm [Fig. 3(B)], as expected for a solvent-exposed, unfolded protein.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-14T11:07:13.479Z"},"uniprot_changed":true,"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":316,"region_id":"DP00017r007","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Intrinsic structural disorder and sequence features of the cell cycle inhibitor p57Kip2. <i> Adkins JN, Lumb KJ. </i> Proteins, 2002","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11746698","version":3,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The hydrodynamic radius of p57 determined with gel filtration is 32 Å (data not shown). A protein the size of p57 (316 amino acids) is expected to have hydrodynamic radii of 25 and 59 Å in globular and highly unfolded states, respectively.31 The hydrodynamic radius of p57 is approximately 1.3 times larger than expected for a monomeric, folded, globular protein, but significantly less than expected for a highly denatured protein.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-14T11:07:14.936Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":97,"region_id":"DP00017r010","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Intrinsic structural disorder and sequence features of the cell cycle inhibitor p57Kip2. <i> Adkins JN, Lumb KJ. </i> Proteins, 2002","term_id":"IDPO:0000002","curator_id":"fquaglia","start":27,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11746698","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":" Intrinsic Disorder of the p57 CDK-Inhibition Domain","type":"Results"},{"text":"The CD spectrum of p57ID is reminiscent of an unfolded protein, with a negative minimum at 202 nm [Fig. 5(A)].","type":"Results"},{"text":"CD analysis of p57ID (10 mM sodium phosphate, 50 mM NaCl, 1 mM DTT, pH 7.0). The CD spectra at 5 and 80°C are characteristic of an unfolded protein.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-14T11:07:16.017Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":97,"region_id":"DP00017r013","released":"2022_03","ec_id":"ECO:0001249","reference_html":"Intrinsic structural disorder and sequence features of the cell cycle inhibitor p57Kip2. <i> Adkins JN, Lumb KJ. </i> Proteins, 2002","term_id":"IDPO:0000002","curator_id":"fquaglia","start":27,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11746698","version":3,"ec_name":"fluorescence evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Intrinsic Disorder of the p57 CDK-Inhibition Domain","type":"Results"},{"text":"The fluorescence spectrum of p27ID collected with an excitation wavelength of 280 nm exhibits an emission maximum at 350 nm [Fig. 5(B)], as expected for solvent-exposed aromatic residues in an unfolded protein.","type":"Results"},{"text":"Fluorescence emission spectrum of p57ID (10 mM sodium phosphate, 50 mM NaCl, 1 mM DTT, pH 7.0, 30 °C). The spectrum, collected with excitation at 280 nm, is characteristic of a solvent-exposed, unfolded protein.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-14T11:07:17.354Z"},"uniprot_changed":true,"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":27,"end":97,"reference_id":"11746698","reference_source":"pmid","reference_html":"Intrinsic structural disorder and sequence features of the cell cycle inhibitor p57Kip2. <i> Adkins JN, Lumb KJ. </i> Proteins, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00017r016","statement":[{"text":"Intrinsic Disorder of the p57 CDK-Inhibition Domain","type":"Results"},{"text":"The HN chemical shifts of p57ID span 7.8–8.5 ppm (Fig. 6), which are within the ranges expected of unfolded proteins.","type":"Results"},{"text":"1H-15N HSQC spectrum of p57ID (17 μM p57ID, 10 mM sodium phosphate, 50 mM NaCl, 1 mM DTT, pH 6.0, 30°C). Seventy resolved amide cross-peaks are observed from an expected total of 71 (76 residues minus Thr 1 and four Pro residues). The lack of HN chemical shift dispersion suggests that p57ID lacks stable secondary structure.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-14T11:07:18.444Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":27,"end":97,"reference_id":"11746698","reference_source":"pmid","reference_html":"Intrinsic structural disorder and sequence features of the cell cycle inhibitor p57Kip2. <i> Adkins JN, Lumb KJ. </i> Proteins, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00017r017","statement":[{"text":"Similar to full-length p57, p57ID inhibits approximately 90% of the activity of cyclin A-CDK2 at a 1:1 molar ratio (Fig. 4), showing that the p57 CDK-inhibition domain is localized to the N-terminus, as expected from sequence comparisons with p21 and p27.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-14T11:07:06.777Z"},"uniprot_changed":true,"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":61,"reference_id":"28425505","reference_source":"pmid","reference_html":"Novel interactions of the von Hippel-Lindau (pVHL) tumor suppressor with the CDKN1 family of cell cycle inhibitors. <i> Minervini G, Lopreiato R, Bortolotto R, Falconieri A, Sartori G, Tosatto SCE. </i> Sci Rep, 2017","date":"2024-09-11T14:38:03.261Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005805","ec_ontology":"ECO","ec_name":"yeast 2-hybrid evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"DisProt","id":"DP00287r060"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P40337","operator":null,"partner_start":54,"partner_end":157}],"region_id":"DP00017r018","statement":[{"text":"The pVHL β-domain is able to bind any member of the CDKN1 family, as indicated by yeast cell growth (Fig. 4B, Supplementary Figures S5 and S7). ","type":"Results"},{"text":"Yeast plasmids expressing either their N-terminal tail containing the CDI domain (p27-NT residues: 1–60; p21-NT: 1–49; p57-NT: 1–61) or the corresponding C-terminal moiety lacking the N-terminus (p27-ΔN residues: 61–198; p21-ΔN: 50–164; p57-ΔN: 62–316) were generated to test the effects of CDKN1 binding to pVHL30. As shown in Fig. 4D, loss of the p27 N-terminus clearly disrupts its ability to associate with pVHL30, as yeast cells expressing the C-terminus of p27 were all unable to grow in selective medium. Similar data have been also obtained for both p21 and p57 (Supplementary Figures S9 and S10), strongly supporting the notion that the CDI domain is responsible for CDKN1 binding to pVHL30.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0693","term_name":"Gal4 DNA-binding domain tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-18T10:51:04.611Z"}},{"start":1,"end":316,"reference_id":"28425505","reference_source":"pmid","reference_html":"Novel interactions of the von Hippel-Lindau (pVHL) tumor suppressor with the CDKN1 family of cell cycle inhibitors. <i> Minervini G, Lopreiato R, Bortolotto R, Falconieri A, Sartori G, Tosatto SCE. </i> Sci Rep, 2017","date":"2024-08-05T13:04:59.172Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"For each transfection, approximatively 5 μg of total DNA, i.e. pcDNA3.1-derived plasmids (empty, and/or expressing either HA-pVHL30 or FLAG-CDKN1) were used."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P40337","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00017r019","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"Our data (Fig. 2B) indicates that all three CDKN1 proteins were able to interact with pVHL30, as demonstrated by their presence in the immunoprecipitate revealed with the anti-Flag antibody (bottom panels). Taken together, the experiments show that these proteins can form at least binary complexes in human, and notably kidney cells.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"cross_refs":[{"db":"DisProt","id":"DP00287r063"}]}],"released":"2016_10","uniref100":"UniRef100_P49918","date":"2016-08-11T10:35:36.000Z","acc":"P49918","name":"Cyclin-dependent kinase inhibitor 1C","length":316,"organism":"Homo sapiens","dataset":[],"uniparc":"UPI0000127442","UniParc":"UPI0000127442","genes":[{"name":{"value":"CDKN1C"},"synonyms":[{"value":"KIP2"}]}],"alphafold_very_low_content":0.2689873417721519,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":316,"type":"D"}],"Structural state":[{"start":1,"end":316,"type":"D"}],"Molecular function":[{"start":1,"end":316,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02234","name":"Cyclin-dependent kinase inhibitor","start":31,"end":79}],"gene3D":[{"start":23,"end":106,"id":"4.10.365.10","name":"p27"}]},"uniref50":"UniRef50_P46527","sequence":"MSNVRVSNGSPSLERMDARQAEHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQESQDVSGSRPAAPLIGAPANSEDTHLVDPKTDPSDSQTGLAEQCAGIRKRPATDDSSTQNKRANRTEENVSDGSPNAGSVEQTPKKPGLRRRQT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P46527","disprot_id":"DP00018","ncbi_taxon_id":9606,"regions_counter":57,"creator":"tlazar","regions":[{"term_namespace":"Disorder function","ec_ontology":"ECO","end":59,"term_name":"flexible linker","released":"2022_03","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","reference_html":"p27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding. <i> Lacy ER, Filippov I, Lewis WS, Otieno S, Xiao L, Weiss S, Hengst L, Kriwacki RW. </i> Nat Struct Mol Biol, 2004","term_id":"IDPO:0000033","curator_id":"fquaglia","start":38,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15024385","version":4,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006198","region_id":"DP00018r002","statement":[{"text":"We call this segment the linker helix because it connects two domains, termed domain 1 and domain 2, that are conserved in the human CKIs (Fig. 1c).","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:25:28.195Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":59,"term_name":"disorder to order","released":"2022_03","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","reference_html":"p27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding. <i> Lacy ER, Filippov I, Lewis WS, Otieno S, Xiao L, Weiss S, Hengst L, Kriwacki RW. </i> Nat Struct Mol Biol, 2004","term_id":"IDPO:0000011","curator_id":"fquaglia","start":38,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15024385","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006198","region_id":"DP00018r003","statement":[{"text":"We determined backbone 1HN, 13Cα and 15N chemical shifts for p27-KID (BioMagResBank entry 6112) and used secondary 13Cα chemical shift values (δΔ 13Cα)23 to identify those residues shown by CD to adopt helical secondary structure (Fig. 1a)24. Most residues show near random coil 13Cα chemical shift values (near zero δΔ 13Cα values). However, all residues between positions 37 and 59 show positive δΔ 13Cα values, consistent with α-helical secondary structure.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-03T15:24:37.069Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":198,"region_id":"DP00018r008","start":105,"ec_id":"ECO:0006198","curator_id":"fquaglia","released":"2022_03","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18177895","version":5,"reference_html":"Role of intrinsic flexibility in signal transduction mediated by the cell cycle regulator, p27 Kip1. <i> Galea CA, Nourse A, Wang Y, Sivakolundu SG, Heller WT, Kriwacki RW. </i> J Mol Biol, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"p27 is comprised of an N-terminal domain (p27-KID, residues 22–104) that binds and inhibits Cdk/cyclin complexes and a C-terminal domain (residues 105–198, p27-C) that contains several sites of post-translational modification, including T187 (Fig. 1a).","type":"Results"},{"text":"We probed the structure and dynamics of the p27 C-terminus using NMR spectroscopy, first by studying the isolated C-terminal domain (p27-C) and second by studying isotope-labeled p27 bound to Cdk2/cyclin A. The 2D 1H-15N HSQC spectrum of 15N-labeled p27-C (Fig. 1b, green) exhibited the limited chemical shift dispersion that is typical of intrinsically unstructured proteins (IUPs). Further, secondary 13Cα chemical shift values (Δδ 13Cα) (Supplementary Fig. 1a) did not indicate the existence of highly populated secondary structure and {1H}-15N heteronuclear (hetNOE) values (Supplementary Fig. 1b) were almost exclusively negative, consistent with frequent, random amide group fluctuations on the high ps-low ns time scale. In addition, the chemical shift values of most amides within p27-C were very similar for the isolated domain and this domain in the context of 2H/15N-p27 bound to Cdk2/cyclin A (Fig. 1b, red). The structural independence of p27-C was confirmed by showing that resonances for p27-KID bound to Cdk2/cyclin A (Fig. 1c, blue) were recapitulated in the 2D 1H-15N TROSY spectrum of 2H/15N-p27/Cdk2/cyclin A (Fig. 1c, red). Together, these results indicated that p27-C in the p27/Cdk2/cyclin A complex is an independent, flexible domain that lacks secondary structure.","type":"Results"},{"text":"While the N-terminal KID of free p27 contained regions of transient structure, the C-terminal domain (p27-C, residues 105–198) lacked detectable secondary structure.","type":"Discussion"},{"text":"Here we have shown that the C-terminal domain of p27 adopts a disordered and quite highly extended conformation when p27 is bound to Cdk2/cyclin A.","type":"Discussion"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:24:53.655Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":198,"region_id":"DP00018r011","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Functional consequences of preorganized helical structure in the intrinsically disordered cell-cycle inhibitor p27(Kip1). <i> Bienkiewicz EA, Adkins JN, Lumb KJ. </i> Biochemistry, 2002","statement":[{"text":"In contrast, the unbound p27 Cdk-inhibition domain is intrinsically disordered (natively unfolded) as shown by circular dichroism spectroscopy, lack of chemical-shift dispersion, and negative heteronuclear nuclear Overhauser effects. The intrinsic disorder is not due to the excision of the Cdk-inhibition domain from p27, since circular dichroism spectra of the full-length protein are also indicative of a largely unfolded protein.","type":"Abstract"},{"text":"Intrinsic Structural Disorder of p27. The full-length p27 used here inhibits histone H1 phosphorylation by cyclin A-Cdk2 (Figure 2). The CD spectrum of full-length human p27 is characteristic of an unfolded protein (Figure 3). The minimum at 200 nm is indicative of an unfolded conformation, and the weak negative shoulder at 222 nm suggests the absence of significant amounts of helix or β-strand. The helix content is estimated at 2 or 6% from [θ]222 or CDPro, respectively. The results indicate that full-length p27, while active as a Cdk inhibitor, is largely unfolded.","type":"Results"},{"text":"The negative ellipticity at 200 nm and the lack of significant ellipticity at 216 nm and above are typical of the CD spectra of unfolded proteins.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11790096","version":4,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:24:56.040Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":95,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Mapping Interactions between p27 and RhoA that Stimulate Cell Migration. <i> Phillips AH, Ou L, Gay A, Besson A, Kriwacki RW. </i> J Mol Biol, 2018","term_id":"GO:0005515","curator_id":"fquaglia","start":55,"term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"29410088","version":4,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00018r019","statement":[{"text":"Titration of RhoA into 13C/15N-labeled p27 resulted in 2D CoN spectra exhibiting extensive resonance broadening for a region in the N-terminus encompassing residues 55–95 (Fig. 2). The finding that this region of p27 mediates interactions with RhoA is consistent with our observations that p27-C does not detectably associate with RhoA (Supplemental Fig. 2).","type":"Results"},{"text":"Using NMR spectroscopy and GDP exchange assays, we have shown that a region in the N-terminal region of p27 mediates binding to RhoA and interferes with nucleotide exchange.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:25:08.736Z"},"uniprot_changed":true,"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":50,"reference_id":"28666995","reference_source":"pmid","reference_html":"Structural basis of divergent cyclin-dependent kinase activation by Spy1/RINGO proteins. <i> McGrath DA, Fifield BA, Marceau AH, Tripathi S, Porter LA, Rubin SM. </i> EMBO J, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5UQ3"}],"region_id":"DP00018r020","statement":[{"text":"Electron density is only observable for p27 residues 51–91, which corresponds to the region that binds Cdk2.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:24:52.041Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":97,"end":197,"reference_id":"28666995","reference_source":"pmid","reference_html":"Structural basis of divergent cyclin-dependent kinase activation by Spy1/RINGO proteins. <i> McGrath DA, Fifield BA, Marceau AH, Tripathi S, Porter LA, Rubin SM. </i> EMBO J, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5UQ3"}],"region_id":"DP00018r021","statement":[{"text":"Electron density is only observable for p27 residues 51–91, which corresponds to the region that binds Cdk2.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:24:51.484Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":22,"end":97,"reference_id":"11790096","reference_source":"pmid","reference_html":"Functional consequences of preorganized helical structure in the intrinsically disordered cell-cycle inhibitor p27(Kip1). <i> Bienkiewicz EA, Adkins JN, Lumb KJ. </i> Biochemistry, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00018r022","statement":[{"text":"The NMR properties of p27ID at 30 °C are characteristic of an unfolded protein. 1H chemical-shift ranges were obtained from DQF COSY (pH 4.4) or TOCSY−HSQC (pH 7.0) spectra using gradients for solvent suppression. The Hα and HN chemical shifts at pH 4.4 span 3.9−4.6 and 7.8−8.6 ppm, respectively, and at pH 7.0 span 4.05−4.59 and 7.77−8.58 ppm, respectively (data not shown). These chemical-shift ranges are typical of those observed in unfolded proteins (28). The amide 1H−15N NOE is negative (approximately −1 to −3.9) for each of 64 resolved mainchain amide cross-peaks at pH 4.4 (from an expected total of 70; data not shown), indicating that the p27ID main chain is highly flexible with motion on a time scale characteristic of unfolded proteins (29, 30). ","type":"Results"},{"text":"NMR study of the inhibitory domain of p27 (p27ID), spanning residues 22-97.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:24:49.901Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":22,"end":97,"reference_id":"11790096","reference_source":"pmid","reference_html":"Functional consequences of preorganized helical structure in the intrinsically disordered cell-cycle inhibitor p27(Kip1). <i> Bienkiewicz EA, Adkins JN, Lumb KJ. </i> Biochemistry, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00018r023","statement":[{"text":"The CD spectra of p27ID in kinase-assay buffer at 30 and 60 °C are also characteristic of an unfolded protein (Figure 5). The minimum at 204 nm is indicative of an unfolded conformation, and the weak negative shoulder at 222 nm suggests the absence of significant amounts of helix or β-strand. The CD spectrum of p27ID at 25 °C is independent of pH in the range 4 to 7.5 and concentration in the range 20 μM to 1 mM (data not shown). The spectroscopic data collectively indicate that the p27 Cdk-inhibition domain is intrinsically disordered in isolation under conditions where the domain is functional as a kinase inhibitor, in contrast to the ordered structure adopted upon binding cyclin A-Cdk2 (Figure 1A). ","type":"Results"},{"text":"p27ID inhibits histone H1 phosphorylation by cyclin A-Cdk2 (25 mM HEPES, 50 mM NaCl, and 5 mM MgCl2, pH 7.5, 30 °C). Reactions contained 50 nM cyclin A-Cdk2 and 0 or 50 nM p27ID. The cyclin A-Cdk2 used here is over 90% active, as calibrated with staurosporine (16).","type":"Figure"},{"text":"CD far-UV study of the inhibitory domain of p27 (p27ID), spanning residues 22-97.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:24:49.157Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":22,"end":97,"reference_id":"11790096","reference_source":"pmid","reference_html":"Functional consequences of preorganized helical structure in the intrinsically disordered cell-cycle inhibitor p27(Kip1). <i> Bienkiewicz EA, Adkins JN, Lumb KJ. </i> Biochemistry, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000019","term_name":"disorder to pre-molten globule","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00018r024","statement":[{"text":"The CD spectra of p27ID in kinase-assay buffer at 30 and 60 °C are also characteristic of an unfolded protein (Figure 5). The minimum at 204 nm is indicative of an unfolded conformation, and the weak negative shoulder at 222 nm suggests the absence of significant amounts of helix or β-strand. The CD spectrum of p27ID at 25 °C is independent of pH in the range 4 to 7.5 and concentration in the range 20 μM to 1 mM (data not shown). The spectroscopic data collectively indicate that the p27 Cdk-inhibition domain is intrinsically disordered in isolation Local Helix Formation in the p27 Cdk-Inhibition Domain. CD spectroscopy indicates that p27ID becomes partially helical at lower temperature (Figure 5). The lack of a folded baseline and differing estimates of [θ]222 for a fully formed helix hinder quantitative determinations of helical content in largely unfolded proteins such as p27ID. Using the method of Chen et al. (19) and CDPro (20), the helix content of p27ID at 5 °C is estimated to be 10 and 16%, respectively. Both estimates are less than the total α and 310 helix content of 33% observed in the crystal structure of the domain bound to cyclin A-Cdk2 (9). The temperature dependence of the CD signal at 222 nm indicates that the helix is only marginally stable (Figure 6). Thus, although intrinsically disordered at physiological temperature, p27ID exhibits an inherent propensity to adopt helical structure.","type":"Results"},{"text":"CD far-UV study of the inhibitory domain of p27 (p27ID), spanning residues 22-97.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:24:59.674Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":22,"end":97,"reference_id":"11790096","reference_source":"pmid","reference_html":"Functional consequences of preorganized helical structure in the intrinsically disordered cell-cycle inhibitor p27(Kip1). <i> Bienkiewicz EA, Adkins JN, Lumb KJ. </i> Biochemistry, 2002","date":"2022-06-13T15:54:39.741Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","released":"2022_06","version":4,"region_id":"DP00018r025","statement":[{"text":"p27ID binds cyclin A-Cdk2 with a Kd of 8 ± 2 nM at 30 °C (Figure 9). The L41P mutant, which contains approximately half of the helix in unbound p27ID, binds with essentially the same affinity (Kd = 9 ± 1 nM at 30 °C) as p27ID. The K47P and A55P mutants, in which helix formation is essentially abolished, bind with slightly lower affinities (16 ± 3 and 13 ± 2 nM, respectively, at 30 °C). At 15 °C, where the helix is more populated, the Kd values for p27ID and L41P are 8 ± 1 and 10 ± 2 nM, respectively (data not shown). Thus, some correlation exists between loss of α-helix in the unbound inhibitor and an increase in Kd. However, the differences are very small in free energy terms (ΔΔG = 0.1 to 0.4 ± 0.4 kcal mol-1) as compared to the free energy of binding (ΔG = −11.4 ± 0.3 kcal mol-1 for p27ID).","type":"Results"},{"text":"Helix Stabilization with Alanine Substitutions. The importance of preformed local helix formation can be addressed by stabilizing helices with multiple alanine substitutions (37).2 Three sites in the α-helix (Gln 40, Asp 44, and Lys 47) were substituted simultaneously with Ala. These residues do not make quaternary contacts with cyclin A-Cdk2 in the crystal structure (9), and AGADIR (38, 39) predicts a 50−100% increase in helix content for residues 38−52 of the α-helix upon their simultaneous substitution with Ala. CD spectroscopy indicates that helix content of the E40A/D44A/K47A mutant is increased as envisaged (Figures 6 and 7), with an estimated helix content at 5 °C of 17 or 22% from [θ]222 or CDPro, respectively. The expected value would be 29% if the α-helix (but not the 310 helix) was fully formed in the mutant (Figure 1B) (9). The Kd of the E40A/D44A/K47A mutant for cyclin A-Cdk2 is increased slightly to 12 ± 3 nM (ΔΔG = 0.4 ± 0.2 kcal mol-1 relative to p27ID; Figure 9).","type":"Results"},{"text":"We conclude that the unbound p27 Cdk-inhibition domain is largely unfolded with a detectable conformational bias toward the α-helix formed upon binding cyclin A-Cdk2. This conformational bias is not beneficial in thermodynamic or kinetic terms for productive folding and binding. Indeed, enhancement of the propensity to form the α-helix impedes kinase inhibition in kinetic terms.","type":"Discussion"}],"uniprot_changed":true,"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gln40Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asn44Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys47Ala","start":null,"end":null,"position":null}]},{"start":25,"end":93,"reference_id":"8684460","reference_source":"pmid","reference_html":"Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex. <i> Russo AA, Jeffrey PD, Patten AK, Massagué J, Pavletich NP. </i> Nature, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1JSU"}],"region_id":"DP00018r026","statement":[{"text":"The crystal structure of the human p27Kip1 kinase inhibitory domain bound to the phosphorylated cyclin A-cyclin-dependent kinase 2 (Cdk2) complex has been determined at 2.3 angstrom. p27Kip1 binds the complex as an extended structure interacting with both cyclin A and Cdk2. On cyclin A, it binds in a groove formed by conserved cyclin box residues. On Cdk2, it binds and rearranges the amino-terminal lobe and also inserts into the catalytic cleft, mimicking ATP.","type":"Abstract"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:24:58.478Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":25,"end":93,"reference_id":"8684460","reference_source":"pmid","reference_html":"Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex. <i> Russo AA, Jeffrey PD, Patten AK, Massagué J, Pavletich NP. </i> Nature, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"1JSU"}],"interaction_partner":[{"db":"UniProt","id":"P24941","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P20248","partner_start":null,"partner_end":null}],"region_id":"DP00018r027","statement":[{"text":"The crystal structure of the human p27Kip1 kinase inhibitory domain bound to the phosphorylated cyclin A-cyclin-dependent kinase 2 (Cdk2) complex has been determined at 2.3 angstrom. p27Kip1 binds the complex as an extended structure interacting with both cyclin A and Cdk2. On cyclin A, it binds in a groove formed by conserved cyclin box residues. On Cdk2, it binds and rearranges the amino-terminal lobe and also inserts into the catalytic cleft, mimicking ATP.","type":"Abstract"},{"text":"Complexes of cyclins with cyclin-dependent kinases (CDKs) play a central role in the control of the eukaryotic cell cycle. The discovery of proteins that bind to and inhibit the catalytic activity of cyclin-CDK complexes has identified kinase inhibition as an intrinsic component of cell-cycle control (reviewed in refs 1-3). These inhibitors (CKIs) induce cell-cycle arrest in response to anti-proliferative signals, including contact inhibition and serum deprivation, TGFβ (ref. 5), myogenic, myeloid and neuronal differentiation, and DNA-damage checkpoints. The inhibitors, which are present in proliferating cells as well, may also help to coordinate cell-cycle progression by their redistribution between different cyclin-CDK complexes.","type":"Introduction"},{"text":"The inhibitory domain of p27 binds the cyclin A-Cdk2 complex as an extended structure interacting with both subunits. Key hydrophobic and hydrogen-bond interactions between a 10-amino-acid region of p27, which contains the conserved LFG sequence motif, and a  shallow groove of cyclin A, which consists of conserved cyclin-box residues, are likely to serve as an anchor point in initial binding, facilitating subsequent interactions with Cdk2. p27 bind-ing inhibits the CDK catalytic activity because its interactions with the N-terminal β-sheet of Cdk2 induce conformational changes that change the shape of the catalytic cleft and because p27 inserts into and fills up the catalytic cleft, eliminating any potential for ATP binding.","type":"Conclusion"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:25:06.177Z"},"uniprot_changed":true,"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":25,"end":93,"reference_id":"8684460","reference_source":"pmid","reference_html":"Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex. <i> Russo AA, Jeffrey PD, Patten AK, Massagué J, Pavletich NP. </i> Nature, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"1JSU"}],"region_id":"DP00018r028","statement":[{"text":"The crystal structure of the human p27Kip1 kinase inhibitory domain bound to the phosphorylated cyclin A-cyclin-dependent kinase 2 (Cdk2) complex has been determined at 2.3 angstrom. p27Kip1 binds the complex as an extended structure interacting with both cyclin A and Cdk2. On cyclin A, it binds in a groove formed by conserved cyclin box residues. On Cdk2, it binds and rearranges the amino-terminal lobe and also inserts into the catalytic cleft, mimicking ATP.","type":"Abstract"},{"text":"Complexes of cyclins with cyclin-dependent kinases (CDKs) play a central role in the control of the eukaryotic cell cycle. The discovery of proteins that bind to and inhibit the catalytic activity of cyclin-CDK complexes has identified kinase inhibition as an intrinsic component of cell-cycle control (reviewed in refs 1-3). These inhibitors (CKIs) induce cell-cycle arrest in response to anti-proliferative signals, including contact inhibition and serum deprivation, TGFβ (ref. 5), myogenic, myeloid and neuronal differentiation, and DNA-damage checkpoints. The inhibitors, which are present in proliferating cells as well, may also help to coordinate cell-cycle progression by their redistribution between different cyclin-CDK complexes.","type":"Introduction"},{"text":"The inhibitory domain of p27 binds the cyclin A-Cdk2 complex as an extended structure interacting with both subunits. Key hydrophobic and hydrogen-bond interactions between a 10-amino-acid region of p27, which contains the conserved LFG sequence motif, and a  shallow groove of cyclin A, which consists of conserved cyclin-box residues, are likely to serve as an anchor point in initial binding, facilitating subsequent interactions with Cdk2. p27 bind-ing inhibits the CDK catalytic activity because its interactions with the N-terminal β-sheet of Cdk2 induce conformational changes that change the shape of the catalytic cleft and because p27 inserts into and fills up the catalytic cleft, eliminating any potential for ATP binding.","type":"Conclusion"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:25:25.352Z"},"uniprot_changed":true,"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":25,"end":93,"reference_id":"8684460","reference_source":"pmid","reference_html":"Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex. <i> Russo AA, Jeffrey PD, Patten AK, Massagué J, Pavletich NP. </i> Nature, 1996","date":"2023-02-16T19:39:25.207Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0019914","term_name":"cyclin-dependent protein kinase activating kinase regulator activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2023_06","version":6,"cross_refs":[{"db":"PDB","id":"1JSU"},{"db":"ELM","id":"DOC_CYCLIN_RxL_1"}],"region_id":"DP00018r029","statement":[{"text":"The crystal structure of the human p27Kip1 kinase inhibitory domain bound to the phosphorylated cyclin A-cyclin-dependent kinase 2 (Cdk2) complex has been determined at 2.3 angstrom. p27Kip1 binds the complex as an extended structure interacting with both cyclin A and Cdk2. On cyclin A, it binds in a groove formed by conserved cyclin box residues. On Cdk2, it binds and rearranges the amino-terminal lobe and also inserts into the catalytic cleft, mimicking ATP.","type":"Abstract"},{"text":"Complexes of cyclins with cyclin-dependent kinases (CDKs) play a central role in the control of the eukaryotic cell cycle. The discovery of proteins that bind to and inhibit the catalytic activity of cyclin-CDK complexes has identified kinase inhibition as an intrinsic component of cell-cycle control (reviewed in refs 1-3). These inhibitors (CKIs) induce cell-cycle arrest in response to anti-proliferative signals, including contact inhibition and serum deprivation, TGFβ (ref. 5), myogenic, myeloid and neuronal differentiation, and DNA-damage checkpoints. The inhibitors, which are present in proliferating cells as well, may also help to coordinate cell-cycle progression by their redistribution between different cyclin-CDK complexes.","type":"Introduction"},{"text":"The inhibitory domain of p27 binds the cyclin A-Cdk2 complex as an extended structure interacting with both subunits. Key hydrophobic and hydrogen-bond interactions between a 10-amino-acid region of p27, which contains the conserved LFG sequence motif, and a  shallow groove of cyclin A, which consists of conserved cyclin-box residues, are likely to serve as an anchor point in initial binding, facilitating subsequent interactions with Cdk2. p27 bind-ing inhibits the CDK catalytic activity because its interactions with the N-terminal β-sheet of Cdk2 induce conformational changes that change the shape of the catalytic cleft and because p27 inserts into and fills up the catalytic cleft, eliminating any potential for ATP binding.","type":"Conclusion"}],"uniprot_changed":true,"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Modulation of the activity of the enzyme cyclin-dependent protein kinase activating kinase.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-22T13:07:01.534Z"}},{"start":181,"end":185,"reference_id":"16209941","reference_source":"pmid","reference_html":"Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase. <i> Hao B, Zheng N, Schulman BA, Wu G, Miller JJ, Pagano M, Pavletich NP. </i> Mol Cell, 2005","date":"2022-08-08T19:46:09.048Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_12","version":5,"cross_refs":[{"db":"PDB","id":"2AST"},{"db":"ELM","id":"DEG_SCF_SKP2-CKS1_1"}],"interaction_partner":[{"db":"UniProt","id":"Q13309","partner_start":null,"partner_end":null}],"region_id":"DP00018r030","statement":[{"text":"We obtained crystals of the ternary Skp1-Skp2-Cks1 complex by using a truncated human Cks1 (residues 5–73) and the previously described truncated Skp1-Skp2 complex (Schulman et al., 2000) (Figures 1A and 1B). For the crystallization of the quaternary Skp1-Skp2-Cks1-p27Kip1 complex, we used a 24 residue p27Kip1 phosphopeptide (residues 175–197; Figure 1C) that we show binds to Skp1-Skp2-Cks1 with an affinity essentially identical to that of full-length phosphorylated p27Kip1 (Table 1). This peptide is from the p27Kip1 C-terminal domain (CTD) that is distinct from the N-terminal domain (residues 22–106; NTD) that inhibits the Cdk2-cyclin A/E complexes (Russo et al., 1996).","type":"Results"},{"text":"In the structure of the quaternary Skp1-Skp2-Cks1-p27Kip1 complex, a ten amino acid segment of the p27Kip1 peptide (residues 181–190) adopts a partially extended conformation and spans the Skp2 LRR domain and Cks1 (Figure 2). The remaining 14 residues of the p27Kip1 peptide do not have interpretable electron density, and we presume they are disordered (Figure S1 available in the Supplemental Data with this article online). The N-terminal portion of the p27Kip1 segment packs with Skp2, a central Glu185 side chain inserts in between Skp2 and Cks1, and the C-terminal portion containing the phosphorylated Thr187 (pThr187) binds to Cks1. p27Kip1 binding does not cause any conformational changes in either Cks1 or Skp2.","type":"Results"},{"text":"The ten amino acid p27Kip1 segment binds to Skp2-Cks1 in a bipartite manner. Residues 181–184 bind to Skp2, residue 185 binds to both Skp2 and Cks1, and residues 186–190 bind to Cks1 (Figures 3C and 3D). The vast majority of the intermolecular contacts are centered on the Glu185 and pThr187 side chains of p27Kip1.","type":"Results"},{"text":"Region of p27 binding to Skp2.","type":"Curator statement"}],"uniprot_changed":true,"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":187,"end":187,"position":"Specific residue"}],"sequence_construct":"SDGSPNAGSVEQTPKKPGLRRRQ"},{"start":181,"end":190,"reference_id":"16209941","reference_source":"pmid","reference_html":"Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase. <i> Hao B, Zheng N, Schulman BA, Wu G, Miller JJ, Pagano M, Pavletich NP. </i> Mol Cell, 2005","date":"2022-06-13T14:51:32.115Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_06","version":3,"cross_refs":[{"db":"PDB","id":"2AST"}],"region_id":"DP00018r031","statement":[{"text":"We obtained crystals of the ternary Skp1-Skp2-Cks1 complex by using a truncated human Cks1 (residues 5–73) and the previously described truncated Skp1-Skp2 complex (Schulman et al., 2000) (Figures 1A and 1B). For the crystallization of the quaternary Skp1-Skp2-Cks1-p27Kip1 complex, we used a 24 residue p27Kip1 phosphopeptide (residues 175–197; Figure 1C) that we show binds to Skp1-Skp2-Cks1 with an affinity essentially identical to that of full-length phosphorylated p27Kip1 (Table 1). This peptide is from the p27Kip1 C-terminal domain (CTD) that is distinct from the N-terminal domain (residues 22–106; NTD) that inhibits the Cdk2-cyclin A/E complexes (Russo et al., 1996).","type":"Results"},{"text":"In the structure of the quaternary Skp1-Skp2-Cks1-p27Kip1 complex, a ten amino acid segment of the p27Kip1 peptide (residues 181–190) adopts a partially extended conformation and spans the Skp2 LRR domain and Cks1 (Figure 2). The remaining 14 residues of the p27Kip1 peptide do not have interpretable electron density, and we presume they are disordered (Figure S1 available in the Supplemental Data with this article online). The N-terminal portion of the p27Kip1 segment packs with Skp2, a central Glu185 side chain inserts in between Skp2 and Cks1, and the C-terminal portion containing the phosphorylated Thr187 (pThr187) binds to Cks1. p27Kip1 binding does not cause any conformational changes in either Cks1 or Skp2.","type":"Results"}],"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural transition","construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":187,"end":187,"position":"Specific residue"}],"sequence_construct":"SDGSPNAGSVEQTPKKPGLRRRQT","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-14T07:34:11.475Z"}},{"start":181,"end":190,"reference_id":"16209941","reference_source":"pmid","reference_html":"Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase. <i> Hao B, Zheng N, Schulman BA, Wu G, Miller JJ, Pagano M, Pavletich NP. </i> Mol Cell, 2005","date":"2022-08-08T19:45:42.930Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990757","term_name":"ubiquitin ligase activator activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_12","version":5,"region_id":"DP00018r032","statement":[{"text":"The ubiquitin-mediated proteolysis of the Cdk2 inhibitor p27(Kip1) plays a central role in cell cycle progression, and enhanced degradation of p27(Kip1) is associated with many common cancers. Proteolysis of p27(Kip1) is triggered by Thr187 phosphorylation, which leads to the binding of the SCF(Skp2) (Skp1-Cul1-Rbx1-Skp2) ubiquitin ligase complex. Unlike other known SCF substrates, p27(Kip1) ubiquitination also requires the accessory protein Cks1.","type":"Abstract"},{"text":"The phosphorylated Thr187 side chain of p27Kip1 is recognized by a Cks1 phosphate binding site, whereas the side chain of an invariant Glu185 inserts into the interface between Skp2 and Cks1, interacting with both. The structure and biochemical data support the proposed model that Cdk2-cyclin A contributes to the recruitment of p27Kip1 to the SCFSkp2-Cks1 complex.","type":"Abstract"},{"text":"We obtained crystals of the ternary Skp1-Skp2-Cks1 complex by using a truncated human Cks1 (residues 5–73) and the previously described truncated Skp1-Skp2 complex (Schulman et al., 2000) (Figures 1A and 1B). For the crystallization of the quaternary Skp1-Skp2-Cks1-p27Kip1 complex, we used a 24 residue p27Kip1 phosphopeptide (residues 175–197; Figure 1C) that we show binds to Skp1-Skp2-Cks1 with an affinity essentially identical to that of full-length phosphorylated p27Kip1 (Table 1). This peptide is from the p27Kip1 C-terminal domain (CTD) that is distinct from the N-terminal domain (residues 22–106; NTD) that inhibits the Cdk2-cyclin A/E complexes (Russo et al., 1996).","type":"Results"},{"text":"In the structure of the quaternary Skp1-Skp2-Cks1-p27Kip1 complex, a ten amino acid segment of the p27Kip1 peptide (residues 181–190) adopts a partially extended conformation and spans the Skp2 LRR domain and Cks1 (Figure 2). The remaining 14 residues of the p27Kip1 peptide do not have interpretable electron density, and we presume they are disordered (Figure S1 available in the Supplemental Data with this article online). The N-terminal portion of the p27Kip1 segment packs with Skp2, a central Glu185 side chain inserts in between Skp2 and Cks1, and the C-terminal portion containing the phosphorylated Thr187 (pThr187) binds to Cks1. p27Kip1 binding does not cause any conformational changes in either Cks1 or Skp2.","type":"Results"}],"uniprot_changed":true,"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binds to and increases the activity of a ubiquitin ligase.\" [GOC:dph, PMID:25619242]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":187,"end":187,"position":"Specific residue"}],"sequence_construct":"SDGSPNAGSVEQTPKKPGLRRRQT","cross_refs":[{"db":"ELM","id":"DEG_SCF_SKP2-CKS1_1"}]},{"start":185,"end":189,"reference_id":"16209941","reference_source":"pmid","reference_html":"Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase. <i> Hao B, Zheng N, Schulman BA, Wu G, Miller JJ, Pagano M, Pavletich NP. </i> Mol Cell, 2005","date":"2022-08-08T19:44:06.756Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_12","version":4,"region_id":"DP00018r033","statement":[{"text":"The ubiquitin-mediated proteolysis of the Cdk2 inhibitor p27(Kip1) plays a central role in cell cycle progression, and enhanced degradation of p27(Kip1) is associated with many common cancers. Proteolysis of p27(Kip1) is triggered by Thr187 phosphorylation, which leads to the binding of the SCF(Skp2) (Skp1-Cul1-Rbx1-Skp2) ubiquitin ligase complex. Unlike other known SCF substrates, p27(Kip1) ubiquitination also requires the accessory protein Cks1.","type":"Abstract"},{"text":"The phosphorylated Thr187 side chain of p27Kip1 is recognized by a Cks1 phosphate binding site, whereas the side chain of an invariant Glu185 inserts into the interface between Skp2 and Cks1, interacting with both. The structure and biochemical data support the proposed model that Cdk2-cyclin A contributes to the recruitment of p27Kip1 to the SCFSkp2-Cks1 complex.","type":"Abstract"},{"text":"We obtained crystals of the ternary Skp1-Skp2-Cks1 complex by using a truncated human Cks1 (residues 5–73) and the previously described truncated Skp1-Skp2 complex (Schulman et al., 2000) (Figures 1A and 1B). For the crystallization of the quaternary Skp1-Skp2-Cks1-p27Kip1 complex, we used a 24 residue p27Kip1 phosphopeptide (residues 175–197; Figure 1C) that we show binds to Skp1-Skp2-Cks1 with an affinity essentially identical to that of full-length phosphorylated p27Kip1 (Table 1). This peptide is from the p27Kip1 C-terminal domain (CTD) that is distinct from the N-terminal domain (residues 22–106; NTD) that inhibits the Cdk2-cyclin A/E complexes (Russo et al., 1996).","type":"Results"},{"text":"In the structure of the quaternary Skp1-Skp2-Cks1-p27Kip1 complex, a ten amino acid segment of the p27Kip1 peptide (residues 181–190) adopts a partially extended conformation and spans the Skp2 LRR domain and Cks1 (Figure 2). The remaining 14 residues of the p27Kip1 peptide do not have interpretable electron density, and we presume they are disordered (Figure S1 available in the Supplemental Data with this article online). The N-terminal portion of the p27Kip1 segment packs with Skp2, a central Glu185 side chain inserts in between Skp2 and Cks1, and the C-terminal portion containing the phosphorylated Thr187 (pThr187) binds to Cks1. p27Kip1 binding does not cause any conformational changes in either Cks1 or Skp2.","type":"Results"},{"text":"Evidence associated to the phosphorylated Thr187 of p27.","type":"Curator statement"}],"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Disorder function","construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":187,"end":187,"position":"Specific residue"}],"sequence_construct":"SDGSPNAGSVEQTPKKPGLRRRQT","cross_refs":[{"db":"ELM","id":"MOD_CDK_SPxK_1"}]},{"start":185,"end":190,"reference_id":"16209941","reference_source":"pmid","reference_html":"Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase. <i> Hao B, Zheng N, Schulman BA, Wu G, Miller JJ, Pagano M, Pavletich NP. </i> Mol Cell, 2005","date":"2022-08-08T19:24:10.784Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031625","term_name":"ubiquitin protein ligase binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_12","version":5,"cross_refs":[{"db":"PDB","id":"2AST"},{"db":"ELM","id":"DEG_SCF_SKP2-CKS1_1"}],"region_id":"DP00018r034","statement":[{"text":"We obtained crystals of the ternary Skp1-Skp2-Cks1 complex by using a truncated human Cks1 (residues 5–73) and the previously described truncated Skp1-Skp2 complex (Schulman et al., 2000) (Figures 1A and 1B). For the crystallization of the quaternary Skp1-Skp2-Cks1-p27Kip1 complex, we used a 24 residue p27Kip1 phosphopeptide (residues 175–197; Figure 1C) that we show binds to Skp1-Skp2-Cks1 with an affinity essentially identical to that of full-length phosphorylated p27Kip1 (Table 1). This peptide is from the p27Kip1 C-terminal domain (CTD) that is distinct from the N-terminal domain (residues 22–106; NTD) that inhibits the Cdk2-cyclin A/E complexes (Russo et al., 1996).","type":"Results"},{"text":"In the structure of the quaternary Skp1-Skp2-Cks1-p27Kip1 complex, a ten amino acid segment of the p27Kip1 peptide (residues 181–190) adopts a partially extended conformation and spans the Skp2 LRR domain and Cks1 (Figure 2). The remaining 14 residues of the p27Kip1 peptide do not have interpretable electron density, and we presume they are disordered (Figure S1 available in the Supplemental Data with this article online). The N-terminal portion of the p27Kip1 segment packs with Skp2, a central Glu185 side chain inserts in between Skp2 and Cks1, and the C-terminal portion containing the phosphorylated Thr187 (pThr187) binds to Cks1. p27Kip1 binding does not cause any conformational changes in either Cks1 or Skp2.","type":"Results"},{"text":"The ten amino acid p27Kip1 segment binds to Skp2-Cks1 in a bipartite manner. Residues 181–184 bind to Skp2, residue 185 binds to both Skp2 and Cks1, and residues 186–190 bind to Cks1 (Figures 3C and 3D). The vast majority of the intermolecular contacts are centered on the Glu185 and pThr187 side chains of p27Kip1.","type":"Results"},{"text":"Region of p27 binding to Csk1.","type":"Curator statement"}],"uniprot_changed":true,"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.\" [GOC:vp]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":187,"end":187,"position":"Specific residue"}],"sequence_construct":"SDGSPNAGSVEQTPKKPGLRRRQT"},{"start":1,"end":198,"reference_id":"29410088","reference_source":"pmid","reference_html":"Mapping Interactions between p27 and RhoA that Stimulate Cell Migration. <i> Phillips AH, Ou L, Gay A, Besson A, Kriwacki RW. </i> J Mol Biol, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00018r035","statement":[{"text":"The initial observation that the C-terminus of p27 is sufficient to co-immunoprecipitate with RhoA was made with a construct that was slightly longer than our p27-C construct [16]; however, extension of our construct to residue 88 (p2788–198) did not restore the migratory phenotype. For completeness, we also tested the complementary N-terminal construct, p271–87, which also did not exhibit a migratory phenotype. In summary, promotion of RhoA-dependent cell migration by p27 requires both the previously identified C-terminal region as well as the N-terminal region of p27 identified here.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:25:18.353Z"},"uniprot_changed":true,"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":22,"end":105,"reference_id":"15024385","reference_source":"pmid","reference_html":"p27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding. <i> Lacy ER, Filippov I, Lewis WS, Otieno S, Xiao L, Weiss S, Hengst L, Kriwacki RW. </i> Nat Struct Mol Biol, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00018r036","statement":[{"text":"To further understand structure-function relationships for p27, we studied p27-FL and p27-KID using solution NMR spectroscopy. Comparison of 2D 1H-15N HSQC NMR spectra for the two polypeptides (Supplementary Fig. 1a,c online) corroborates findings based on CD spectra. The subspectrum in Supplementary Figure 1b online, showing only resonances that appear at the same chemical shift values in Supplementary Figure 1a,c online, shows ∼80% of the resonances observed for p27-KID (Supplementary Fig. 1c online). This illustrates that the conformation of most residues in p27-KID is virtually equivalent in the truncated and full-length molecules. Moreover, spectra for both molecules show limited resonance dispersion (backbone amide protons resonate between 7.8 and 8.5 p.p.m.), a feature typical of intrinsically disordered, biologically active polypeptides","type":"Results"},{"text":"p27-KID spans residues 22-105 of the human p27.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-02T14:01:11.932Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":198,"reference_id":"15024385","reference_source":"pmid","reference_html":"p27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding. <i> Lacy ER, Filippov I, Lewis WS, Otieno S, Xiao L, Weiss S, Hengst L, Kriwacki RW. </i> Nat Struct Mol Biol, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00018r037","statement":[{"text":"To further understand structure-function relationships for p27, we studied p27-FL and p27-KID using solution NMR spectroscopy. Comparison of 2D 1H-15N HSQC NMR spectra for the two polypeptides (Supplementary Fig. 1a,c online) corroborates findings based on CD spectra. The subspectrum in Supplementary Figure 1b online, showing only resonances that appear at the same chemical shift values in Supplementary Figure 1a,c online, shows ∼80% of the resonances observed for p27-KID (Supplementary Fig. 1c online). This illustrates that the conformation of most residues in p27-KID is virtually equivalent in the truncated and full-length molecules. Moreover, spectra for both molecules show limited resonance dispersion (backbone amide protons resonate between 7.8 and 8.5 p.p.m.), a feature typical of intrinsically disordered, biologically active polypeptides","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-02T14:01:10.317Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":28,"end":37,"reference_id":"15024385","reference_source":"pmid","reference_html":"p27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding. <i> Lacy ER, Filippov I, Lewis WS, Otieno S, Xiao L, Weiss S, Hengst L, Kriwacki RW. </i> Nat Struct Mol Biol, 2004","date":"2022-03-08T13:42:40.965Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","released":"2022_03","version":4,"region_id":"DP00018r038","statement":[{"text":"Domain 1, though highly dynamic in solution, is relatively compact (ten residues), and therefore folding to a single conformation on binding cyclin A is associated with a relatively small entropy penalty. In contrast, domain 2 spans 29 residues that fold on binding to Cdk2, and, correspondingly, this reaction is associated with a large entropy penalty. Notably, domains 1 and 2 bind their respective targets with similar affinity, clearly revealing the thermodynamic importance of each of these interactions.","type":"Results"},{"text":"Our data show that interactions mediated by the two conserved domains of p27-KID contribute considerably to the overall ΔG value.","type":"Results"},{"text":"p27-KID binds Cdk2–cyclin A through a sequential mechanism involving extensive folding of p27-KID.","type":"Figure"},{"text":"Evidence corresponding to domain 1 (28-37).","type":"Curator statement"}],"uniprot_changed":true,"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P20248","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-22T18:22:08.968Z"}},{"start":66,"end":88,"reference_id":"15024385","reference_source":"pmid","reference_html":"p27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding. <i> Lacy ER, Filippov I, Lewis WS, Otieno S, Xiao L, Weiss S, Hengst L, Kriwacki RW. </i> Nat Struct Mol Biol, 2004","date":"2022-03-08T13:42:24.506Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","released":"2022_03","version":4,"region_id":"DP00018r039","statement":[{"text":"Domain 1, though highly dynamic in solution, is relatively compact (ten residues), and therefore folding to a single conformation on binding cyclin A is associated with a relatively small entropy penalty. In contrast, domain 2 spans 29 residues that fold on binding to Cdk2, and, correspondingly, this reaction is associated with a large entropy penalty. Notably, domains 1 and 2 bind their respective targets with similar affinity, clearly revealing the thermodynamic importance of each of these interactions.","type":"Results"},{"text":"Our data show that interactions mediated by the two conserved domains of p27-KID contribute considerably to the overall ΔG value.","type":"Results"},{"text":"p27-KID binds Cdk2–cyclin A through a sequential mechanism involving extensive folding of p27-KID.","type":"Figure"},{"text":"Evidence corresponding to domain 2 (66-88).","type":"Curator statement"}],"uniprot_changed":true,"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P20248","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-22T18:22:10.178Z"}},{"start":32,"end":45,"reference_id":"12529437","reference_source":"pmid","reference_html":"CRM1/Ran-mediated nuclear export of p27(Kip1) involves a nuclear export signal and links p27 export and proteolysis. <i> Connor MK, Kotchetkov R, Cariou S, Resch A, Lupetti R, Beniston RG, Melchior F, Hengst L, Slingerland JM. </i> Mol Biol Cell, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00018r042","statement":[{"text":"A putative nuclear export sequence (NES) in p27 is identified. Mutation of this NES reduced nuclear export, impaired p27-CRM1 interactions, and increased p27 stability.","type":"Introduction"},{"text":"p27 Contains an Atypical NES","type":"Results"},{"text":"We identified a putative NES within the Cdk-binding domain of p27 between amino acids 32 and 45 (Figure ​(Figure6A)6A) based on the homology of leucine spacing to a cryptic NES identified in the equine infectious anemia virus (EIAV) Rev protein (Mancuso et al., 1998 blue right-pointing triangle). The spacing of the three leucines in this region of p27 is highly conserved between species.","type":"Results"},{"text":"To obtain additional evidence that amino acids 32 through 45 in p27 comprise a functional NES, we tested its ability to mediate nuclear export of an unrelated protein. For this, peptides containing the putative p27 NES (CRNLFGPVDHEELTRDLE) were coupled to FITC-labeled BSA and were microinjected into nuclei of adherent HeLa cells. As is shown in Figure ​Figure6B,6B, a significant fraction of p27NES-FITC-BSA translocated into the cytoplasm within 45 min. In contrast, the nuclear localization of FITC-BSA remained unchanged. Although p27-NES mediated export of p27NES-FITC-BSA is not very efficient, possibly due to competing events such as the observed accumulation in nuclear speckles, or due to rate-limiting binding partners, these findings support the interpretation that amino acids 32 through 45 in p27 function as an NES.","type":"Results"},{"text":"p27NES Shows Delayed Cytoplasmic Accumulation after Proteasome Inhibition","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:25:14.601Z"},"uniprot_changed":true,"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":8,"end":12,"reference_id":"12529437","reference_source":"pmid","reference_html":"CRM1/Ran-mediated nuclear export of p27(Kip1) involves a nuclear export signal and links p27 export and proteolysis. <i> Connor MK, Kotchetkov R, Cariou S, Resch A, Lupetti R, Beniston RG, Melchior F, Hengst L, Slingerland JM. </i> Mol Biol Cell, 2003","date":"2022-06-14T12:45:35.056Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051168","term_name":"nuclear export","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","released":"2022_06","version":4,"region_id":"DP00018r043","statement":[{"text":"Mutation of S10 But Not of T187 Affects Nuclear Export of p27","type":"Results"},{"text":"Mutation of S10 to alanine strongly inhibited p27 export (Figure ​(Figure6,6, B and C), suggesting that phosphorylation at this site is essential for nuclear export of p27.","type":"Results"}],"uniprot_changed":true,"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The directed movement of substances out of the nucleus.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser10Ala","start":null,"end":null,"position":null}],"sequence_construct":"MSNVRVSNGAPSLERMDARQAEHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQESQDVSGSRPAAPLIGAPANSEDTHLVDPKTDPSDSQTGLAEQCAGIRKRPATDDSSTQNKRANRTEENVSDGSPNAGSVEQTPKKPGLRRRQT","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-15T07:33:10.523Z"}},{"start":8,"end":12,"reference_id":"10831586","reference_source":"pmid","reference_html":"Phosphorylation at serine 10, a major phosphorylation site of p27(Kip1), increases its protein stability. <i> Ishida N, Kitagawa M, Hatakeyama S, Nakayama K. </i> J Biol Chem, 2000","date":"2022-06-13T15:02:40.260Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","released":"2022_06","version":3,"region_id":"DP00018r044","statement":[{"text":"Phosphorylation at serine 10, a major phosphorylation site of p27(Kip1), increases its protein stability","type":"Title"},{"text":"Substitution of Ser(10) with Ala (S10A) markedly reduced the extent of p27(Kip1) phosphorylation and prevented the shift in electrophoretic mobility. Phosphopeptide mapping and phosphoamino acid analysis revealed that phosphorylation at Ser(10) accounted for approximately 70% of the total phosphorylation of p27(Kip1), and the extent of phosphorylation at this site was approximately 25- and 75-fold greater than that at Ser(178) and Thr(187), respectively.","type":"Abstract"},{"text":"Furthermore, a mutant p27(Kip1) in which Ser(10) was replaced with glutamic acid in order to mimic the effect of Ser(10) phosphorylation exhibited a marked increase in stability both in vivo and in vitro compared with the wild-type or S10A mutant proteins. These results suggest that Ser(10) is the major site of phosphorylation of p27(Kip1) and that phosphorylation at this site, like that at Thr(187), contributes to regulation of p27(Kip1) stability.","type":"Abstract"}],"uniprot_changed":true,"ec_go":"IMP","disprot_namespace":"Disorder function","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser10Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser10Glu","start":null,"end":null,"position":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-14T07:34:28.832Z"}},{"start":32,"end":45,"reference_id":"12529437","reference_source":"pmid","reference_html":"CRM1/Ran-mediated nuclear export of p27(Kip1) involves a nuclear export signal and links p27 export and proteolysis. <i> Connor MK, Kotchetkov R, Cariou S, Resch A, Lupetti R, Beniston RG, Melchior F, Hengst L, Slingerland JM. </i> Mol Biol Cell, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00018r045","statement":[{"text":"Delayed Nuclear Export Is Associated with Increased p27 Protein Stability","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:25:11.435Z"},"uniprot_changed":true,"ec_go":"IEP","disprot_namespace":"Disorder function"},{"start":22,"end":105,"reference_id":"16214166","reference_source":"pmid","reference_html":"Disordered p27Kip1 exhibits intrinsic structure resembling the Cdk2/cyclin A-bound conformation. <i> Sivakolundu SG, Bashford D, Kriwacki RW. </i> J Mol Biol, 2005","date":"2023-07-27T13:01:34.112Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP00018r046","statement":[{"text":"Before binding, p27 is at least partially disordered and folds upon binding its Cdk/cyclin targets.","type":"Abstract"},{"text":"Interestingly, the highly conserved, specificity determining segment of p27 is shown to be highly disordered.","type":"Abstract"},{"text":"In summary, these results provide strong evidence for the existence of IFSUs within localized regions of p27-KID; other segments of p27-KID are dynamic and disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T15:23:49.236Z"}},{"start":38,"end":90,"reference_id":"16214166","reference_source":"pmid","reference_html":"Disordered p27Kip1 exhibits intrinsic structure resembling the Cdk2/cyclin A-bound conformation. <i> Sivakolundu SG, Bashford D, Kriwacki RW. </i> J Mol Biol, 2005","date":"2023-08-07T18:04:30.125Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP00018r047","statement":[{"text":"Before binding, p27 is at least partially disordered and folds upon binding its Cdk/cyclin targets.","type":"Abstract"},{"text":"Interestingly, the highly conserved, specificity determining segment of p27 is shown to be highly disordered.","type":"Abstract"},{"text":"In summary, these results provide strong evidence for the existence of IFSUs within localized regions of p27-KID; other segments of p27-KID are dynamic and disordered. Importantly, while domain LH was known to be helical, by monitoring 1HN–1HN NOE correlations, we have detected additional structural features of p27-KID (IFSUs) that were not revealed through our previous NMR studies based on the analysis of Δδ13Cα and hetNOE values.","type":"Results"},{"text":"After domain 1 becomes tethered to the cyclin subunit of a Cdk/cyclin complex, the helical IFSU within domain LH positions domain 2 (containing domains 2.1, 2.2 and 2.3) for reorganization and folding on binding to Cdk2.","type":"Discussion"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20248","statements":[{"type":"Abstract","text":"Before binding, p27 is at least partially disordered and folds upon binding its Cdk/cyclin targets."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P24941","statements":[{"type":"Abstract","text":"Before binding, p27 is at least partially disordered and folds upon binding its Cdk/cyclin targets."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-08T13:58:02.871Z"}},{"start":22,"end":97,"reference_id":"11749217","reference_source":"pmid","reference_html":"Effects of macromolecular crowding on the intrinsically disordered proteins c-Fos and p27(Kip1). <i> Flaugh SL, Lumb KJ. </i> Biomacromolecules, 2001","date":"2023-07-27T13:11:11.087Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP00018r048","statement":[{"text":"In the presence of macromolecular crowding agents, neither the intrinsically disordered C-terminal activation domain of c-Fos nor the kinase-inhibition domain of p27Kip1 undergoes any significant conformational change that is detected by changes in either circular dichroism or fluorescence spectra.","type":"Abstract"},{"text":"While intrinsically disordered at physiological temperatures, marginally stable helix is present in p27ID at 5 °C (Figure 2A).8 Addition of TFE to p27ID induced a marked change in the CD spectrum indicative of a large increase in helix content (Figure 2A). However addition of several crowding agents did not induce any significant change in the CD spectrum of p27ID above 212 nm that reflects formation of helical or strand secondary structure (Figure 2B).","type":"Results"},{"text":"A decrease in the intensity of the CD signal of p27ID at 204 nm was observed in the presence of the 37.5 and 77 kDa dextrans, and the fluorescence emission intensity of p27ID at 350 nm was reduced in the presence of 77 kDa dextran and Ficoll 70 (as observed for FosAD).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T15:25:12.883Z"}},{"start":22,"end":97,"reference_id":"11749217","reference_source":"pmid","reference_html":"Effects of macromolecular crowding on the intrinsically disordered proteins c-Fos and p27(Kip1). <i> Flaugh SL, Lumb KJ. </i> Biomacromolecules, 2001","date":"2023-07-27T13:12:10.549Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006336","ec_ontology":"ECO","ec_name":"intrinsic fluorescence-based protein conformation evidence","unpublished":true,"released":"2023_12","version":0,"region_id":"DP00018r049","statement":[{"text":"In the presence of macromolecular crowding agents, neither the intrinsically disordered C-terminal activation domain of c-Fos nor the kinase-inhibition domain of p27Kip1 undergoes any significant conformational change that is detected by changes in either circular dichroism or fluorescence spectra.","type":"Abstract"},{"text":"Crowding agents did not affect the p27ID fluorescence emission maximum of 350 nm (Figure 2C) or did not affect significantly the fluorescence spectrum of ANS in the presence of p27ID (data not shown).","type":"Results"},{"text":"A decrease in the intensity of the CD signal of p27ID at 204 nm was observed in the presence of the 37.5 and 77 kDa dextrans, and the fluorescence emission intensity of p27ID at 350 nm was reduced in the presence of 77 kDa dextran and Ficoll 70 (as observed for FosAD).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T15:25:03.747Z"}},{"start":22,"end":97,"reference_id":"16214166","reference_source":"pmid","reference_html":"Disordered p27Kip1 exhibits intrinsic structure resembling the Cdk2/cyclin A-bound conformation. <i> Sivakolundu SG, Bashford D, Kriwacki RW. </i> J Mol Biol, 2005","date":"2023-07-27T13:19:13.590Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006336","ec_ontology":"ECO","ec_name":"intrinsic fluorescence-based protein conformation evidence","unpublished":true,"released":"2023_12","version":0,"interaction_partner":[{"db":"UniProt","id":"P20248","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P24941","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP00018r050","statement":[{"text":"Before binding, p27 is at least partially disordered and folds upon binding its Cdk/cyclin targets.","type":"Abstract"},{"text":"After domain 1 becomes tethered to the cyclin subunit of a Cdk/cyclin complex, the helical IFSU within domain LH positions domain 2 (containing domains 2.1, 2.2 and 2.3) for reorganization and folding on binding to Cdk2.","type":"Discussion"},{"text":"The need for structural rearrangement of domain 2.2 of p27-KID and the aforementioned segment of Cdk2 prior to binding Cdk2/cyclin A is likely the principal determinant of the slow kinetics of this interaction.","type":"Discussion"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T15:19:17.273Z"}},{"start":86,"end":90,"reference_id":"17254966","reference_source":"pmid","reference_html":"Cdk-inhibitory activity and stability of p27Kip1 are directly regulated by oncogenic tyrosine kinases. <i> Grimmler M, Wang Y, Mund T, Cilensek Z, Keidel EM, Waddell MB, Jäkel H, Kullmann M, Kriwacki RW, Hengst L. </i> Cell, 2007","date":"2023-07-27T13:40:38.314Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP00018r051","statement":[{"text":"A conserved tyrosine residue (Y88) in the Cdk-binding domain of p27 can be phosphorylated by the Src-family kinase Lyn and the oncogene product BCR-ABL.","type":"Abstract"},{"text":"p27 is phosphorylated on Y88 in vivo. HA-tagged p27 was coexpressed in 293T cells with Lyn (Y508F) or p210 BCR-ABL kinase. Anti-HA immunoprecipitates were incubated with (+) or without calf intestinal alkaline phosphatase (CIAP) and analyzed by western blotting using purified polyclonal anti-phospho-Y88 p27 antibodies. The same blot was subsequently probed with an HRP-conjugated anti-p27 antibody.","type":"Figure"},{"text":"pY88 was annotated with 2-residue flanking regions in both directions.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T15:17:56.856Z"}},{"start":86,"end":90,"reference_id":"17254966","reference_source":"pmid","reference_html":"Cdk-inhibitory activity and stability of p27Kip1 are directly regulated by oncogenic tyrosine kinases. <i> Grimmler M, Wang Y, Mund T, Cilensek Z, Keidel EM, Waddell MB, Jäkel H, Kullmann M, Kriwacki RW, Hengst L. </i> Cell, 2007","date":"2023-07-27T13:49:39.762Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001254","ec_ontology":"ECO","ec_name":"radioisotope assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP00018r052","statement":[{"text":"A conserved tyrosine residue (Y88) in the Cdk-binding domain of p27 can be phosphorylated by the Src-family kinase Lyn and the oncogene product BCR-ABL.","type":"Abstract"},{"text":"(D) Lyn and Abl phosphorylate Y88 of p27 in vitro. Equal amounts of p27 or mutant p27 (tyrosine residues exchanged to phenylalanine; Y1F: Y in position 74 exchanged to F; Y2: Y in position 88; and Y3: Y in position 89) were incubated with recombinant constitutively active Lyn or Abl kinase at 30°C in the presence of γ-[32P]-ATP. Proteins were separated by SDS-PAGE and detected by Coomassie staining (upper panel). The amount of incorporated 32P was shown by autoradiography (lower panel).","type":"Figure"},{"text":"pY88 was annotated with 2-residue flanking regions in both directions.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T15:18:12.139Z"}},{"start":91,"end":96,"reference_id":"17254966","reference_source":"pmid","reference_html":"Cdk-inhibitory activity and stability of p27Kip1 are directly regulated by oncogenic tyrosine kinases. <i> Grimmler M, Wang Y, Mund T, Cilensek Z, Keidel EM, Waddell MB, Jäkel H, Kullmann M, Kriwacki RW, Hengst L. </i> Cell, 2007","date":"2023-07-27T14:11:30.078Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IEP","interaction_partner":[{"db":"UniProt","id":"P07948","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P00519","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP00018r053","statement":[{"text":"A conserved tyrosine residue (Y88) in the Cdk-binding domain of p27 can be phosphorylated by the Src-family kinase Lyn and the oncogene product BCR-ABL.","type":"Abstract"},{"text":"Within the Cdk-inhibitory domain the p27 sequence contains three tyrosine residues near the proline-rich SH3-binding element (Figure 1A). To investigate if phosphorylation of tyrosines influenced binding of p27 to the kinase, we exchanged these tyrosine residues to phenylalanine.","type":"Results"},{"text":"Figure 1  p27Kip1 Binds the Tyrosine Kinase Lyn and Is Phosphorylated on Tyrosine. (A) All tyrosine residues (indicated as Y) of p27 are located in the Cdk-inhibitory domain (dark gray). A proline-rich SH3-binding element (residues 91–96) is represented as a black box. (B) Lyn binds to a p27 mutant protein lacking all three tyrosines.","type":"Figure"},{"text":"Equal amounts of monomeric or cyclin A/Cdk2-bound p27 were incubated with Abl kinase. While monomeric p27 was a better substrate for Abl phosphorylation, tyrosine phosphorylation of cyclin A/Cdk2-bound p27 was clearly detected (Figure 1G).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T15:19:13.058Z"}},{"start":58,"end":105,"reference_id":"28885015","reference_source":"pmid","reference_html":"A Small Molecule Causes a Population Shift in the Conformational Landscape of an Intrinsically Disordered Protein. <i> Ban D, Iconaru LI, Ramanathan A, Zuo J, Kriwacki RW. </i> J Am Chem Soc, 2017","date":"2023-07-27T17:13:57.278Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP00018r054","statement":[{"text":"These RD results, we believe for the first time, define the kinetics for transitions between discrete conformational states for a region of an IDP (p27-D2).","type":"Results"},{"text":"The RD data recorded with the lowest ωeff values (with maximal contributions of conformational exchange) revealed elevated R2,eff values for residues within several regions of the p27-D2 sequence, especially those containing aromatic residues (Figure 1C, gray points). In contrast, the apparent R2,0 (R2,0app) values (Figure 1C, black points) for p27-D2, which were determined from the RD fit procedure, are relatively continuous with few extrema showing that only the relaxation effects of fast segmental motions are retained (as expected for a disordered polypeptide) and that the contribution of Rex is largely quenched.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T15:24:44.435Z"}},{"start":58,"end":105,"reference_id":"28885015","reference_source":"pmid","reference_html":"A Small Molecule Causes a Population Shift in the Conformational Landscape of an Intrinsically Disordered Protein. <i> Ban D, Iconaru LI, Ramanathan A, Zuo J, Kriwacki RW. </i> J Am Chem Soc, 2017","date":"2023-07-27T17:17:29.282Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP00018r055","statement":[{"text":"Analysis using small-angle X-ray scattering (SAXS) (58, 59) showed that the radius of gyration (Rg) for p27-D2 increased from 21 ± 2 to 27 ± 2 Å in the presence of SJ403 ([p27-D2]:[SJ403] ratio of 1:5; Figure 4C), consistent with our hypothesis.","type":"Results"},{"text":"For a 48-residue-long polypeptide chain, Rg of 21 Å is significantly higher than the Rg of a globular protein of this size, 21 Å is characteristic of a typical IDP.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T15:24:35.281Z"}},{"start":1,"end":60,"reference_id":"28425505","reference_source":"pmid","reference_html":"Novel interactions of the von Hippel-Lindau (pVHL) tumor suppressor with the CDKN1 family of cell cycle inhibitors. <i> Minervini G, Lopreiato R, Bortolotto R, Falconieri A, Sartori G, Tosatto SCE. </i> Sci Rep, 2017","date":"2024-09-11T14:37:03.968Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005805","ec_ontology":"ECO","ec_name":"yeast 2-hybrid evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"DisProt","id":"DP00287r060"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P40337","operator":null,"partner_start":54,"partner_end":157}],"region_id":"DP00018r056","statement":[{"text":"The pVHL β-domain is able to bind any member of the CDKN1 family, as indicated by yeast cell growth (Fig. 4B, Supplementary Figures S5 and S7).","type":"Results"},{"text":"Yeast plasmids expressing either their N-terminal tail containing the CDI domain (p27-NT residues: 1–60; p21-NT: 1–49; p57-NT: 1–61) or the corresponding C-terminal moiety lacking the N-terminus (p27-ΔN residues: 61–198; p21-ΔN: 50–164; p57-ΔN: 62–316) were generated to test the effects of CDKN1 binding to pVHL30. As shown in Fig. 4D, loss of the p27 N-terminus clearly disrupts its ability to associate with pVHL30, as yeast cells expressing the C-terminus of p27 were all unable to grow in selective medium.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0693","term_name":"Gal4 DNA-binding domain tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-18T10:50:34.014Z"}},{"start":1,"end":198,"reference_id":"28425505","reference_source":"pmid","reference_html":"Novel interactions of the von Hippel-Lindau (pVHL) tumor suppressor with the CDKN1 family of cell cycle inhibitors. <i> Minervini G, Lopreiato R, Bortolotto R, Falconieri A, Sartori G, Tosatto SCE. </i> Sci Rep, 2017","date":"2024-08-05T13:02:41.770Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"For each transfection, approximatively 5 μg of total DNA, i.e. pcDNA3.1-derived plasmids (empty, and/or expressing either HA-pVHL30 or FLAG-CDKN1) were used."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P40337","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00018r057","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"Our data (Fig. 2B) indicates that all three CDKN1 proteins were able to interact with pVHL30, as demonstrated by their presence in the immunoprecipitate revealed with the anti-Flag antibody (bottom panels). Taken together, the experiments show that these proteins can form at least binary complexes in human, and notably kidney cells.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"cross_refs":[{"db":"DisProt","id":"DP00287r063"}]}],"released":"2016_10","uniref100":"UniRef100_P46527","date":"2016-08-11T10:05:05.000Z","acc":"P46527","name":"Cyclin-dependent kinase inhibitor 1B","length":198,"organism":"Homo sapiens","dataset":["Autophagy-related proteins","Cancer-related proteins"],"uniparc":"UPI0000035C92","UniParc":"UPI0000035C92","genes":[{"name":{"value":"CDKN1B","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"20824794","url":"http://www.ncbi.nlm.nih.gov/pubmed/20824794","alternativeUrl":"https://europepmc.org/abstract/MED/20824794"}}]},"synonyms":[{"value":"KIP1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10831586","url":"http://www.ncbi.nlm.nih.gov/pubmed/10831586","alternativeUrl":"https://europepmc.org/abstract/MED/10831586"}}]},{"value":"p27","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15509543","url":"http://www.ncbi.nlm.nih.gov/pubmed/15509543","alternativeUrl":"https://europepmc.org/abstract/MED/15509543"}}]}]}],"alphafold_very_low_content":0.2222222222222222,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"},{"start":22,"end":97,"type":"T"},{"start":98,"end":180,"type":"D"},{"start":181,"end":190,"type":"T"},{"start":191,"end":198,"type":"D"}],"Structural state":[{"start":1,"end":198,"type":"D"}],"Disorder function":[{"start":8,"end":12,"type":"F"},{"start":32,"end":59,"type":"F"},{"start":86,"end":90,"type":"F"},{"start":185,"end":189,"type":"F"}],"Structural transition":[{"start":22,"end":97,"type":"T"},{"start":181,"end":190,"type":"T"}],"Molecular function":[{"start":1,"end":198,"type":"F"}],"Biological process":[{"start":1,"end":198,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00249","name":"Myb-like DNA-binding domain","start":362,"end":411},{"id":"PF09197","name":"Rap1, DNA-binding","start":448,"end":579},{"id":"PF11626","name":"TRF2-interacting telomeric protein/Rap1 - C terminal domain","start":741,"end":823},{"id":"PF16589","name":"BRCT domain","start":126,"end":206}],"gene3D":[{"start":778,"end":827,"id":"1.10.10.2170","name":"1.10.10.2170"},{"start":115,"end":219,"id":"3.40.50.10190","name":"BRCT domain"},{"start":676,"end":777,"id":"1.20.120.1480","name":"1.20.120.1480"},{"start":360,"end":412,"id":"1.10.10.60","name":"Homeodomain-like"},{"start":447,"end":577,"id":"1.10.10.60","name":"Homeodomain-like"}]},"uniref50":"UniRef50_P11938","sequence":"MSSPDDFETAPAEYVDALDPSMVVVDSGSAAVTAPSDSAAEVKANQNEENTGATAAETSEKVDQTEVEKKDDDDTTEVGVTTTTPSIADTAATANIASTSGASVTEPTTDDTAADEKKEQVSGPPLSNMKFYLNRDADAHDSLNDIDQLARLIRANGGEVLDSKPRESKENVFIVSPYNHTNLPTVTPTYIKACCQSNSLLNMENYLVPYDNFREVVDSRLQEESHSNGVDNSNSNSDNKDSIRPKTEIISTNTNGATEDSTSEKVMVDAEQQARLQEQAQLLRQHVSSTASITSGGHNDLVQIEQPQKDTSNNNNSNVNDEDNDLLTQDNNPQTADEGNASFQAQRSMISRGALPSHNKASFTDEEDEFILDVVRKNPTRRTTHTLYDEISHYVPNHTGNSIRHRFRVYLSKRLEYVYEVDKFGKLVRDDDGNLIKTKVLPPSIKRKFSADEDYTLAIAVKKQFYRDLFQIDPDTGRSLITDEDTPTAIARRNMTMDPNHVPGSEPNFAAYRTQSRRGPIAREFFKHFAEEHAAHTENAWRDRFRKFLLAYGIDDYISYYEAEKAQNREPEPMKNLTNRPKRPGVPTPGNYNSAAKRARNYSSQRNVQPTANAASANAAAAAAAAASNSYAIPENELLDEDTMNFISSLKNDLSNISNSLPFEYPHEIAEAIRSDFSNEDIYDNIDPDTISFPPKIATTDLFLPLFFHFGSTRQFMDKLHEVISGDYEPSQAEKLVQDLCDETGIRKNFSTSILTCLSGDLMVFPRYFLNMFKDNVNPPPNVPGIWTHDDDESLKSNDQEQIRKLVKKHGTGRMEMRKRFFEKDLL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P11938","disprot_id":"DP00020","ncbi_taxon_id":559292,"regions_counter":17,"creator":"agasparini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":123,"region_id":"DP00020r001","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Solution structure of Rap1 BRCT domain from Saccharomyces cerevisiae reveals a novel fold. <i> Zhang W, Zhang J, Zhang X, Xu C, Tu X. </i> Biochem Biophys Res Commun, 2011","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"21187076","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-08-16T19:21:49.675Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2L42"},{"db":"BMRB","id":"17212"}],"term_name":"disorder","uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The solution structure of Rap1 BRCT domain contains three β-strands and three α-helices. Three helices, α1 (residue 31–39), α2 (residue 75–81) and α3 (residue 87–90), face the β-sheet that is formed by strand 1 (residue 16–18), strand 2 (residue 47–48) and strand 3 (residue 59–60).","type":"Results"},{"text":"The proportion of the secondary structure elements in Rap1 BRCT domain is relatively low and there are several long flexible loops among secondary structure elements. Therefore, the global conformation of Rap1 BRCT domain is rather flexible. No resonance signal maintained in 2-D 1H–2H exchange experiment also indicated a loose structure of Rap1 BRCT domain.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:06:44.395Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":512,"region_id":"DP00020r007","released":"2022_12","ec_id":"ECO:0006220","reference_html":"The crystal structure of the DNA-binding domain of yeast RAP1 in complex with telomeric DNA. <i> Konig P, Giraldo R, Chapman L, Rhodes D. </i> Cell, 1996","term_id":"IDPO:0000002","curator_id":"vnugnes","start":482,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"8620531","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-08-16T18:55:40.465Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1IGN"}],"term_name":"disorder","uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Title","text":"The Crystal Structure of the DNA-Binding Domain of Yeast RAP1 in Complex with Telomeric DNA"},{"type":"Curator statement","text":"Intercating DNA with sequence 5'-CCGCACACCCACACACCAG"}]}],"statement":[{"text":"The resulting electron density map was interpretable for the DNA and the protein, with the exception of residues at the termini (residues 353–359 and 595–598), three internal regions (residues 482–512, 565–571, and 579–585), and one of the overhanging bases of the binding site.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:06:49.304Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":675,"region_id":"DP00020r013","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Rif1 and Rif2 shape telomere function and architecture through multivalent Rap1 interactions. <i> Shi T, Bunker RD, Mattarocci S, Ribeyre C, Faty M, Gut H, Scrima A, Rass U, Rubin SM, Shore D, Thomä NH. </i> Cell, 2013","term_id":"IDPO:0000002","curator_id":"vnugnes","start":627,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"23746845","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-08-16T18:35:17.931Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4BJT"}],"term_name":"disorder","uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P29539"}],"statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:17:36.381Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":598,"region_id":"DP00020r015","released":"2022_12","ec_id":"ECO:0006220","reference_html":"The crystal structure of the DNA-binding domain of yeast RAP1 in complex with telomeric DNA. <i> Konig P, Giraldo R, Chapman L, Rhodes D. </i> Cell, 1996","term_id":"IDPO:0000002","curator_id":"vnugnes","start":565,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"8620531","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-08-16T19:05:06.785Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1IGN"}],"term_name":"disorder","uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Title","text":"The Crystal Structure of the DNA-Binding Domain of Yeast RAP1 in Complex with Telomeric DNA"},{"type":"Curator statement","text":"Intercating DNA with sequence 5'-CCGCACACCCACACACCAG."}]}],"statement":[{"text":"The resulting electron density map was interpretable for the DNA and the protein, with the exception of residues at the termini (residues 353–359 and 595–598), three internal regions (residues 482–512, 565–571, and 579–585), and one of the overhanging bases of the binding site.","type":"Results"},{"text":"Although the regions 572-578 and 586-594 have electron density in the PDB, they are not large enough to be ordered, so are considered as unstructured","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:06:50.795Z"}},{"start":627,"end":674,"reference_id":"23746845","reference_source":"pmid","reference_html":"Rif1 and Rif2 shape telomere function and architecture through multivalent Rap1 interactions. <i> Shi T, Bunker RD, Mattarocci S, Ribeyre C, Faty M, Gut H, Scrima A, Rass U, Rubin SM, Shore D, Thomä NH. </i> Cell, 2013","date":"2022-08-16T18:35:46.485Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"4BJ6"}],"region_id":"DP00020r017","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q06208"}],"statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:06:52.260Z"}}],"released":"2016_10","uniref100":"UniRef100_P11938","date":"2016-08-22T10:56:08.000Z","acc":"P11938","name":"DNA-binding protein RAP1","length":827,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"uniparc":"UPI0000169200","UniParc":"UPI0000169200","genes":[{"name":{"value":"RAP1"},"synonyms":[{"value":"GRF1"},{"value":"TUF1"}],"orfNames":[{"value":"N1310"}],"olnNames":[{"value":"YNL216W"}]}],"alphafold_very_low_content":0.34099153567110035,"disorder_content":0.28657799274486095,"disprot_consensus":{"full":[{"start":1,"end":123,"type":"D"},{"start":482,"end":512,"type":"D"},{"start":565,"end":598,"type":"D"},{"start":627,"end":675,"type":"D"}],"Structural state":[{"start":1,"end":123,"type":"D"},{"start":482,"end":512,"type":"D"},{"start":565,"end":598,"type":"D"},{"start":627,"end":675,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00009","name":"Elongation factor Tu GTP binding domain","start":10,"end":282},{"id":"PF00679","name":"Elongation factor G C-terminus","start":601,"end":686},{"id":"PF03144","name":"Elongation factor Tu domain 2","start":323,"end":389},{"id":"PF03764","name":"Elongation factor G, domain IV","start":479,"end":597},{"id":"PF14492","name":"Elongation Factor G, domain III","start":404,"end":478}],"gene3D":[{"start":484,"end":687,"id":"3.30.230.10","name":"3.30.230.10"},{"start":288,"end":400,"id":"2.40.30.10","name":"Translation factors"},{"start":1,"end":286,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":405,"end":483,"id":"3.30.70.870","name":"Elongation Factor G (Translational Gtpase), domain 3"},{"start":604,"end":674,"id":"3.30.70.240","name":"3.30.70.240"}]},"uniref50":"UniRef50_Q5SHN5","sequence":"MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERERGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSETVWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDVLRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEEELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVEIHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHANHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKADQEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQVAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIPAVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPVILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLRSKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ","taxonomy":["Bacteria","Deinococcus-Thermus","Deinococci","Thermales","Thermaceae","Thermus"],"uniref90":"UniRef90_Q5SHN5","disprot_id":"DP00021","ncbi_taxon_id":274,"regions_counter":7,"creator":"imicetic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":64,"region_id":"DP00021r002","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Structural insights into fusidic acid resistance and sensitivity in EF-G. <i> Hansson S, Singh R, Gudkov AT, Liljas A, Logan DT. </i> J Mol Biol, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":40,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-09-05T18:00:35.767Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2BM1"}],"reference_id":"15843024","uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly16Val","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"78408","entry_name":"guanosine 5'-[beta,gamma-imido]triphosphate"}],"sequence_construct":"MAVKVEYDLKRLRNIVIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERERGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSETVWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDVLRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEEELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVEIHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHANHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKADQEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQVAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIPAVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPVILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLRSKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:16:51.931Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":63,"region_id":"DP00021r003","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Structural insights into fusidic acid resistance and sensitivity in EF-G. <i> Hansson S, Singh R, Gudkov AT, Liljas A, Logan DT. </i> J Mol Biol, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":44,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-09-05T18:01:00.233Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2BM0"}],"reference_id":"15843024","uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr84Ala","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"78408","entry_name":"guanosine 5'-[beta,gamma-imido]triphosphate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"}],"statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"sequence_construct":"MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIAEVHEGAATMDFMEQERERGITITAAVTTCFWKDHRINIIDAPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSETVWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDVLRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEEELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVEIHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHANHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKADQEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQVAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIPAVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPVILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLRSKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:16:52.790Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":60,"region_id":"DP00021r004","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Crystal structure of a mutant elongation factor G trapped with a GTP analogue. <i> Hansson S, Singh R, Gudkov AT, Liljas A, Logan DT. </i> FEBS Lett, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":42,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-09-05T17:50:23.443Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2BV3"}],"reference_id":"16083884","uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"78408","entry_name":"guanosine 5'-[beta,gamma-imido]triphosphate"}],"statement":[{"text":"Switch I is invisible between residues 43 and 60, and residues 40–41 and 61–65 can only be built as poly-alanine.","type":"Results"},{"text":"The PDB shows the IDR boundaries are 42-60.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr84Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The T84A mutant was crystallized in the presence of 10 mM GDPNP (Sigma®)."}]}],"sequence_construct":"MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERERGITITAAVTTCFWKDHRINIIDAPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSETVWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDVLRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEEELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVEIHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHANHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKADQEKLSQALARLAEESPTFSVSTHPETGSTIISGMGELSLEIIVDRLKREFKVDANVGKPQVAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIPAVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPVILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLRSKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:16:59.827Z"}},{"start":40,"end":67,"reference_id":"11054294","reference_source":"pmid","reference_html":"Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site. <i> Laurberg M, Kristensen O, Martemyanov K, Gudkov AT, Nagaev I, Hughes D, Liljas A. </i> J Mol Biol, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1FNM"}],"region_id":"DP00021r005","statement":[{"text":"Switch I (the effector loop) is a highly flexible region in all G-proteins.","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-09T12:22:04.092Z"},"uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":416,"end":434,"reference_id":"16083884","reference_source":"pmid","reference_html":"Crystal structure of a mutant elongation factor G trapped with a GTP analogue. <i> Hansson S, Singh R, Gudkov AT, Liljas A, Logan DT. </i> FEBS Lett, 2005","date":"2022-09-05T17:52:31.933Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr84Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The T84A mutant was crystallized in the presence of 10 mM GDPNP (Sigma®)."}]}],"cross_refs":[{"db":"PDB","id":"2BV3"}],"region_id":"DP00021r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"78408","entry_name":"guanosine 5'-[beta,gamma-imido]triphosphate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"}],"sequence_construct":"MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERERGITITAAVTTCFWKDHRINIIDAPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSETVWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDVLRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEEELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVEIHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHANHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKADQEKLSQALARLAEESPTFSVSTHPETGSTIISGMGELSLEIIVDRLKREFKVDANVGKPQVAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIPAVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPVILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLRSKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:17:06.357Z"}},{"start":464,"end":475,"reference_id":"16083884","reference_source":"pmid","reference_html":"Crystal structure of a mutant elongation factor G trapped with a GTP analogue. <i> Hansson S, Singh R, Gudkov AT, Liljas A, Logan DT. </i> FEBS Lett, 2005","date":"2022-09-05T17:52:48.527Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr84Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The T84A mutant was crystallized in the presence of 10 mM GDPNP (Sigma®)."}]}],"cross_refs":[{"db":"PDB","id":"2BV3"}],"region_id":"DP00021r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"78408","entry_name":"guanosine 5'-[beta,gamma-imido]triphosphate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"}],"sequence_construct":"MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERERGITITAAVTTCFWKDHRINIIDAPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSETVWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDVLRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEEELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVEIHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHANHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKADQEKLSQALARLAEESPTFSVSTHPETGSTIISGMGELSLEIIVDRLKREFKVDANVGKPQVAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIPAVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPVILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLRSKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:17:22.030Z"}}],"released":"2016_10","uniref100":"UniRef100_Q5SHN5","date":"2016-09-08T18:04:11.000Z","acc":"P13551","name":"Elongation factor G","length":691,"organism":"Thermus thermophilus","dataset":[],"uniparc":"UPI0000110F2D","UniParc":"UPI0000110F2D","genes":[{"name":{"value":"fusA"},"synonyms":[{"value":"fus"}]}],"alphafold_very_low_content":0.00723589001447178,"disorder_content":0.085383502170767,"disprot_consensus":{"full":[{"start":40,"end":67,"type":"D"},{"start":416,"end":434,"type":"D"},{"start":464,"end":475,"type":"D"}],"Structural state":[{"start":40,"end":67,"type":"D"},{"start":416,"end":434,"type":"D"},{"start":464,"end":475,"type":"D"}]}},{"acc":"P14061","sequence":"MARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSLETLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTVRMLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEVFLTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDVPAKAEAGAEAGGGAGPGAEDEAGRGAVGDPELGDPPAAPQ","alphafold_very_low_content":"0.11890243902439024","creator":"vacs","dataset":[],"date":"2016-08-11T12:06:47.000Z","disprot_id":"DP00023","features":{"pfam":[{"id":"PF00106","name":"short chain dehydrogenase","start":5,"end":196}],"gene3D":[{"start":3,"end":286,"id":"3.40.50.720","name":"NAD(P)-binding Rossmann-like Domain","_id":"685af522b4ac24d5329d70b5"}]},"genes":[{"name":{"value":"HSD17B1","evidences":[{"source":{"id":"HGNC:5210","name":"HGNC","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:5210","_id":"685af522b4ac24d5329d70dd"},"code":"ECO:0000312","_id":"685af522b4ac24d5329d70dc"}],"_id":"685af522b4ac24d5329d70de"},"synonyms":[{"value":"E17KSR","evidences":[],"_id":"685af522b4ac24d5329d70df"},{"value":"EDH17B1","evidences":[],"_id":"685af522b4ac24d5329d70e0"},{"value":"EDH17B2","evidences":[],"_id":"685af522b4ac24d5329d70e1"},{"value":"EDHB17","evidences":[],"_id":"685af522b4ac24d5329d70e2"},{"value":"SDR28C1","evidences":[],"_id":"685af522b4ac24d5329d70e3"}],"olnNames":[],"orfNames":[],"_id":"685af522b4ac24d5329d70db"}],"length":328,"name":"Estradiol 17-beta-dehydrogenase 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":8,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI00001108EB","uniref100":"UniRef100_P14061","uniref50":"UniRef50_P14061","uniref90":"UniRef90_P14061","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1BHS","_id":"685af522b4ac24d5329d70c3"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":286,"end":328,"interaction_partner":[],"reference_html":"Structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase at 2.20 A resolution. <i> Ghosh D, Pletnev VZ, Zhu DW, Wawrzak Z, Duax WL, Pangborn W, Labrie F, Lin SX. </i> Structure, 1995","reference_id":"7663947","region_id":"DP00023r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"However, the α-carbon chain cannot be traced beyond residue 284 because the electron density is so diffuse.","_id":"685af522b4ac24d5329d70c4"},{"type":"Results","text":"Interestingly, the electron density for the C terminus, which is rich in alanine, glycine, proline and other hydrophobic residues, is ill defined beyond the end of αH at position 285. ","_id":"685af522b4ac24d5329d70c5"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","uniprot_changed":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-06-14T13:27:18.533Z","_id":"685af522b4ac24d5329d70c6"},"version":2,"_id":"685af522b4ac24d5329d70c2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1FDU","_id":"685af522b4ac24d5329d70c8"},{"db":"PDB","id":"1FDV","_id":"685af522b4ac24d5329d70c9"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-05-27T12:04:03.454Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":191,"end":199,"interaction_partner":[],"reference_html":"Unusual charge stabilization of NADP+ in 17beta-hydroxysteroid dehydrogenase. <i> Mazza C, Breton R, Housset D, Fontecilla-Camps JC. </i> J Biol Chem, 1998","reference_id":"9525918","region_id":"DP00023r006","released":"2022_06","sample":[],"statement":[{"type":"Abstract","text":"These structures provide a complete picture of the NADP+-enzyme interactions involving the flexible 191–199 loop (well ordered in the H221L mutant) and suggest that the hydrophobic residues Phe192-Met193 could facilitate hydride transfer.","_id":"685af522b4ac24d5329d70ca"},{"type":"Results","text":"In the H221L-NAD1 complex, where a sulfate ion replaces the 2'-phosphate, the electron density corresponding to the 191–199 loop is less well defined even though the NAD1 site appears to be fully occupied. This implies that although the sulfate ion establishes a series of interactions with both the protein and the cofactor, these are less efficient in stabilizing the 191–199 loop than those formed by the covalently bound 2'-phosphate.","_id":"685af522b4ac24d5329d70cb"},{"type":"Discussion","text":" This loop, which becomes well ordered only in the enzyme-\nNADP+-folate complex, has been found to shield the nicotinamide moiety from solvent and to participate on the transition state stabilization (44).","_id":"685af522b4ac24d5329d70cc"},{"type":"Results","text":"The 191–199 loop, located between the bF sheet and the aG helix, seems to be predominantly stabilized by its interactions with the dinucleotide, particularly by the salt bridge between Lys195 and the 2'-phosphate.","_id":"685af522b4ac24d5329d70cd"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","term_id":"IDPO:0000033","term_is_binding":true,"term_is_obsolete":false,"term_name":"flexible linker","term_namespace":"Disorder function","term_not_annotate":true,"term_ontology":"IDPO","uniprot_changed":true,"version":4,"_id":"685af522b4ac24d5329d70c7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1FDU","_id":"685af522b4ac24d5329d70cf"},{"db":"PDB","id":"1FDV","_id":"685af522b4ac24d5329d70d0"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":191,"end":199,"interaction_partner":[{"db":"ChEBI","id":"18009","partner_start":null,"partner_end":null,"_id":"685af522b4ac24d5329d70d1"}],"reference_html":"Unusual charge stabilization of NADP+ in 17beta-hydroxysteroid dehydrogenase. <i> Mazza C, Breton R, Housset D, Fontecilla-Camps JC. </i> J Biol Chem, 1998","reference_id":"9525918","region_id":"DP00023r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In the H221L-NAD1 complex, where a sulfate ion replaces the 2'-phosphate, the electron density corresponding to the 191–199 loop is less well defined even though the NAD1 site appears to be fully occupied. This implies that although the sulfate ion establishes a series of interactions with both the protein and the cofactor, these are less efficient in stabilizing the 191–199 loop than those formed by the covalently bound 2'-phosphate.","_id":"685af522b4ac24d5329d70d2"},{"type":"Results","text":"The 191–199 loop, located between the bF sheet and the aG helix, seems to be predominantly stabilized by its interactions with the dinucleotide, particularly by the salt bridge between Lys195 and the 2'-phosphate.","_id":"685af522b4ac24d5329d70d3"}],"states_connection":[],"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","term_id":"GO:0036094","term_is_binding":true,"term_is_obsolete":false,"term_name":"small molecule binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","uniprot_changed":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-06-14T13:43:54.729Z","_id":"685af522b4ac24d5329d70d4"},"version":3,"_id":"685af522b4ac24d5329d70ce","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1FDU","_id":"685af522b4ac24d5329d70d6"},{"db":"PDB","id":"1FDV","_id":"685af522b4ac24d5329d70d7"},{"db":"PDB","id":"1FDW","_id":"685af522b4ac24d5329d70d8"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":286,"end":328,"interaction_partner":[],"reference_html":"Unusual charge stabilization of NADP+ in 17beta-hydroxysteroid dehydrogenase. <i> Mazza C, Breton R, Housset D, Fontecilla-Camps JC. </i> J Biol Chem, 1998","reference_id":"9525918","region_id":"DP00023r008","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The C-terminal region is missing in the pdb structures.","_id":"685af522b4ac24d5329d70d9"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","uniprot_changed":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-06-14T13:44:03.841Z","_id":"685af522b4ac24d5329d70da"},"version":2,"_id":"685af522b4ac24d5329d70d5","reference_source":"pmid"}],"__v":0,"disorder_content":0.13109756097560976,"disprot_consensus":{"full":[{"start":191,"end":199,"type":"F"},{"start":286,"end":328,"type":"D"}],"Structural state":[{"start":286,"end":328,"type":"D"}],"Disorder function":[{"start":191,"end":199,"type":"F"}],"Molecular function":[{"start":191,"end":199,"type":"F"}]}},{"acc":"P03129","sequence":"MHGDTPTLHEYMLDLQPETTDLYCYEQLNDSSEEEDEIDGPAGQAEPDRAHYNIVTFCCKCDSTLRLCVQSTHVDIRTLEDLLMGTLGIVCPICSQKP","creator":"ewagner","dataset":["Viral proteins"],"date":"2016-08-22T13:35:18.000Z","disprot_id":"DP00024","features":{"pfam":[{"id":"PF00527","name":"E7 protein, Early protein","start":3,"end":94}],"gene3D":[{"start":42,"end":97,"id":"G3DSA:3.30.160.730","_id":"685af522b4ac24d5329d70e5"}]},"genes":[{"name":{"value":"E7","evidences":[{"source":{"id":"MF_04004","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04004","_id":"685af523b4ac24d5329d71a9"},"code":"ECO:0000255","_id":"685af523b4ac24d5329d71a8"}],"_id":"685af523b4ac24d5329d71aa"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d71a7"}],"length":98,"name":"Protein E7","ncbi_taxon_id":333760,"organism":"Human papillomavirus type 16","regions_counter":44,"released":"2016_10","taxonomy":["Viruses","Monodnaviria","Shotokuvirae","Cossaviricota","Papovaviricetes","Zurhausenvirales","Papillomaviridae","Firstpapillomavirinae","Alphapapillomavirus"],"UniParc":"UPI000000034E","uniref100":"UniRef100_P03129","uniref50":"UniRef50_P03129","uniref90":"UniRef90_P03129","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":40,"interaction_partner":[],"reference_html":"The N-terminal module of HPV16 E7 is an intrinsically disordered domain that confers conformational and recognition plasticity to the oncoprotein. <i> García-Alai MM, Alonso LG, de Prat-Gay G. </i> Biochemistry, 2007","reference_id":"17715947","region_id":"DP00024r006","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"When exposed to an acidic environment, E7(1-40) undergoes a structural transition triggered by the\nneutralization of its acidic residues, similar to the full-length HPV16 E7 dimer (7). A decrease in the CD signal at 220 nm at low pH is indicative of the acquisition of R-helix. Moreover, as pH decreases, the CD indicates that the PII content tends to disappear.","_id":"685af522b4ac24d5329d70f2"},{"type":"Results","text":"The N-terminus could thus be responsible for E7's conformational behavior toward pH; it undergoes a conformational transition within a physiological pH range that could correspond to an induction in α-helix and/or loss of PII structure. The difference spectrum between E7(1−40) at pH 7.5 and pH 3.0 displays the positive distinctive band at 218 nm present in PII models (Figure 2b inset).","_id":"685af522b4ac24d5329d70f3"},{"type":"Results","text":"This result is in excellent agreement with the observed conformational transition by CD, where the molar ellipticity at 220 nm decreased when the pH is lowered (not shown).","_id":"685af522b4ac24d5329d70f4"}],"states_connection":[{"source":"DP00024r014","target":"DP00024r031","_id":"685af522b4ac24d5329d70f5"}],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","uniprot_changed":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-17T11:36:01.934Z","_id":"685af522b4ac24d5329d70f6"},"version":3,"_id":"685af522b4ac24d5329d70f1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[{"deviation":null,"statements":[],"term_id":"NCIT:C45997","unit_id":"UO:0000196","unit_name":"pH","value":7.5,"_id":"685af522b4ac24d5329d710a"}],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":40,"interaction_partner":[],"reference_html":"The N-terminal module of HPV16 E7 is an intrinsically disordered domain that confers conformational and recognition plasticity to the oncoprotein. <i> García-Alai MM, Alonso LG, de Prat-Gay G. </i> Biochemistry, 2007","reference_id":"17715947","region_id":"DP00024r014","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The far-UV CD spectrum of the E7 dimer (E72) at pH 7.5 is dominated by a minimum at 205 nm, with a negative band at around 220 nm (Figure 2a, dotted line). The band at 220 nm is indicative of α-helix content, and the minimum at 205 can be the result of a combination of an α-helix (208 nm) and disordered structure (200 nm). When observing the spectrum of the N-terminus of E7, it is reminiscent of that of a disordered polypeptide with a minimum around 200 nm (Figure 2a, full line). To analyze the structural contribution of the E7(1−40) domain to the E72 far-UV−CD, the subtraction of spectra was carried out and presents only the α-helix spectral characteristics, suggesting that the apparently disordered components in the E7 dimer, manifested by the minimum at 205 nm, are introduced by the N-terminal module (Figure 2a, inset), in agreement with the solved structure of HPV 1A E7 where the N-terminal region is absent in the crystal ( 5) and HPV 45 E7 N-terminus not analyzable by NMR ( 4).","_id":"685af522b4ac24d5329d7109"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-17T11:35:58.928Z","_id":"685af522b4ac24d5329d710b"},"version":1,"_id":"685af522b4ac24d5329d7108","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0001184","ec_name":"gel-filtration evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":40,"interaction_partner":[],"reference_html":"The N-terminal module of HPV16 E7 is an intrinsically disordered domain that confers conformational and recognition plasticity to the oncoprotein. <i> García-Alai MM, Alonso LG, de Prat-Gay G. </i> Biochemistry, 2007","reference_id":"17715947","region_id":"DP00024r015","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"At pH 7.5, E7(1−40) elutes at 15 mL, while CI2(1−40) does so at 17 mL, indicating that at neutral pH, E7(1−40) is extended (Figure 3). E7(1−40) elutes with the hydrodynamic volume of a globular protein of 25 kDa, equivalent to a Stokes radius of 20.9 Å, a value even larger than the predicted for a “natively unfolded” polypeptide of this size.","_id":"685af522b4ac24d5329d710d"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-26T07:50:26.402Z","_id":"685af522b4ac24d5329d710e"},"version":1,"_id":"685af522b4ac24d5329d710c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[{"deviation":null,"statements":[],"term_id":"NCIT:C45997","unit_id":"UO:0000196","unit_name":"pH","value":7.5,"_id":"685af522b4ac24d5329d7111"}],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":40,"interaction_partner":[],"reference_html":"The N-terminal module of HPV16 E7 is an intrinsically disordered domain that confers conformational and recognition plasticity to the oncoprotein. <i> García-Alai MM, Alonso LG, de Prat-Gay G. </i> Biochemistry, 2007","reference_id":"17715947","region_id":"DP00024r016","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In addition, we carried out pulse field gradient NMR experiments at 1 mM E7(1−40), and from the diffusion coefficient the domain was shown to be monomeric, with a calculated stokes radius of 21.26 Å, expected for an extended fragment of that number of residues (not shown).","_id":"685af522b4ac24d5329d7110"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-17T11:35:53.097Z","_id":"685af522b4ac24d5329d7112"},"version":1,"_id":"685af522b4ac24d5329d710f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":40,"interaction_partner":[],"reference_html":"The N-terminal module of HPV16 E7 is an intrinsically disordered domain that confers conformational and recognition plasticity to the oncoprotein. <i> García-Alai MM, Alonso LG, de Prat-Gay G. </i> Biochemistry, 2007","reference_id":"17715947","region_id":"DP00024r017","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In addition, we carried out pulse field gradient NMR experiments at 1 mM E7(1−40), and from the diffusion coefficient the domain was shown to be monomeric, with a calculated stokes radius of 21.26 Å, expected for an extended fragment of that number of residues (not shown). When the same experiment is carried out at pH 4.0, the hydrodynamic volume of CI2(1−40) stays unmodified, but E7(1−40) elutes at a larger volume from the column, strongly suggesting that the conformational change induced at low pH yields a more compact structure (Figure 3).","_id":"685af522b4ac24d5329d7114"}],"states_connection":[{"source":"DP00024r016","target":"DP00024r030","_id":"685af522b4ac24d5329d7115"}],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-17T11:36:00.918Z","_id":"685af522b4ac24d5329d7116"},"version":1,"_id":"685af522b4ac24d5329d7113","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":40,"interaction_partner":[],"reference_html":"Conformational dissection of a viral intrinsically disordered domain involved in cellular transformation. <i> Noval MG, Gallo M, Perrone S, Salvay AG, Chemes LB, de Prat-Gay G. </i> PLoS One, 2013","reference_id":"24086265","region_id":"DP00024r018","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Comparison of the far-UV CD spectra of the E7N sub-fragments in 10 mM Tris.Cl buffer at pH 7.5 showed a lack of canonical secondary structure with a general appearance of disorder (Figure 2A). Most sub-fragments presented similar spectra, with molar ellipticity values around −15,000 deg·cm2·dmol−1 resembling those of the previously described E7 (1–40) domain [27].","_id":"685af522b4ac24d5329d7118"},{"type":"Curator statement","text":"They assessed the regions: 1-40, 1-20, 16-40, 16-31, 21-29 and 25-40. For all of them they found typical spectra of unstructured proteins.","_id":"685af522b4ac24d5329d7119"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-26T07:36:30.669Z","_id":"685af522b4ac24d5329d711a"},"version":1,"_id":"685af522b4ac24d5329d7117","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"19269","_id":"685af522b4ac24d5329d711c"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":40,"interaction_partner":[],"reference_html":"Conformational dissection of a viral intrinsically disordered domain involved in cellular transformation. <i> Noval MG, Gallo M, Perrone S, Salvay AG, Chemes LB, de Prat-Gay G. </i> PLoS One, 2013","reference_id":"24086265","region_id":"DP00024r019","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Both RH values obtained for E7N were significantly larger than the RH value expected for a 40 residue globular protein (13.8 Å) [51], confirming the IDP nature of E7N. However, both values were also smaller than the RH value predicted for a fully unfolded polymer (18.1 Å) [51], which suggested some degree of compaction of the domain that may be due to the presence of transient long-range interactions. PFG-NMR experiments showed a further decrease in the RH value at pH 5.0 (14.3±0.3 Å, Table 3), suggesting that protonation of the acidic residues contributed to E7N compaction.","_id":"685af522b4ac24d5329d711d"},{"type":"Results","text":" A first inspection of the one dimensional 1H spectrum of E7N in aqueous solution at pH 5.0 showed poorly dispersed amide proton resonances (data not shown), with most peaks within the 7.8–8.5 ppm range, making assignment a rather challenging task. The methyl proton region also showed poor dispersion of peaks, confirming the expected disordered nature of E7N.","_id":"685af522b4ac24d5329d711e"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-26T07:36:16.773Z","_id":"685af522b4ac24d5329d711f"},"version":1,"_id":"685af522b4ac24d5329d711b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"19442","_id":"685af522b4ac24d5329d7127"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0001238","ec_name":"nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":46,"interaction_partner":[],"reference_html":"The heterogeneous structural behavior of E7 from HPV16 revealed by NMR spectroscopy. <i> Calçada EO, Felli IC, Hošek T, Pierattelli R. </i> Chembiochem, 2013","reference_id":"23940009","region_id":"DP00024r022","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"All the NMR data determined for the E7N region indicate that it is highly flexible and highly disordered, as is also immediately evident from the SSP values as well as from negative 1H–15N heteronuclear NOE. Detailed inspection of these data also indicates short fragments of amino acids characterized by a mild secondary structural propensity, starting at residue 26 onwards (Figure 4).","_id":"685af522b4ac24d5329d7128"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-26T08:09:09.387Z","_id":"685af522b4ac24d5329d7129"},"version":1,"_id":"685af522b4ac24d5329d7126","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"4YOZ","_id":"685af522b4ac24d5329d712e"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":21,"end":29,"interaction_partner":[],"reference_html":"Structural mechanisms of DREAM complex assembly and regulation. <i> Guiley KZ, Liban TJ, Felthousen JG, Ramanan P, Litovchick L, Rubin SM. </i> Genes Dev, 2015","reference_id":"25917549","region_id":"DP00024r024","released":"2022_03","sample":[],"statement":[{"type":"Figure","text":"Crystal structures of the p107 pocket domain in complex with LIN5212–34;phosS28 and E721–29. (Insets, left) The LIN52 and E7 peptides both bind at the LxCxE cleft. (Inset, top) The LIN52 association is mediated by the S28 phosphate, which contacts a p107/p130-specific binding pocket.","_id":"685af522b4ac24d5329d712f"},{"type":"Results","text":"The E7 peptide binds to the LxCxE cleft in the B-box of p107 as previously observed in the Rb–E7 complex structure (Fig. 2; Supplemental Fig. 2B; Lee et al. 1998).","_id":"685af522b4ac24d5329d7130"}],"states_connection":[],"term_comment":"See also the biological process terms 'viral infectious cycle ; GO:0019058' and 'lysogeny ; GO:0030069'.","term_def":"\"A multi-organism process in which a virus is a participant. The other participant is the host. Includes infection of a host cell, replication of the viral genome, and assembly of progeny virus particles. In some cases the viral genetic material may integrate into the host genome and only subsequently, under particular circumstances, 'complete' its life cycle.\" [GOC:bf, GOC:jl, GOC:mah]","term_id":"GO:0016032","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral process","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-26T07:54:01.932Z","_id":"685af522b4ac24d5329d7131"},"version":1,"_id":"685af522b4ac24d5329d712d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"4YOZ","_id":"685af522b4ac24d5329d7133"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":21,"end":29,"interaction_partner":[{"db":"UniProt","id":"P28749","partner_start":null,"partner_end":null,"_id":"685af522b4ac24d5329d7134"}],"reference_html":"Structural mechanisms of DREAM complex assembly and regulation. <i> Guiley KZ, Liban TJ, Felthousen JG, Ramanan P, Litovchick L, Rubin SM. </i> Genes Dev, 2015","reference_id":"25917549","region_id":"DP00024r025","released":"2022_03","sample":[],"statement":[{"type":"Figure","text":"Crystal structures of the p107 pocket domain in complex with LIN5212–34;phosS28 and E721–29. (Insets, left) The LIN52 and E7 peptides both bind at the LxCxE cleft. (Inset, top) The LIN52 association is mediated by the S28 phosphate, which contacts a p107/p130-specific binding pocket.","_id":"685af522b4ac24d5329d7135"},{"type":"Results","text":"The E7 peptide binds to the LxCxE cleft in the B-box of p107 as previously observed in the Rb–E7 complex structure (Fig. 2; Supplemental Fig. 2B; Lee et al. 1998).","_id":"685af522b4ac24d5329d7136"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-26T07:53:54.417Z","_id":"685af522b4ac24d5329d7137"},"version":1,"_id":"685af522b4ac24d5329d7132","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006277","ec_name":"fluorescence polarization evidence used in manual assertion","ec_ontology":"ECO","start":21,"end":29,"interaction_partner":[{"db":"UniProt","id":"Q08999","partner_start":null,"partner_end":null,"_id":"685af522b4ac24d5329d7139"}],"reference_html":"Structural mechanisms of DREAM complex assembly and regulation. <i> Guiley KZ, Liban TJ, Felthousen JG, Ramanan P, Litovchick L, Rubin SM. </i> Genes Dev, 2015","reference_id":"25917549","region_id":"DP00024r026","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"We then quantified the E7 peptide inhibition (Ki = 170 ± 50 nM) by displacing labeled LIN5212–34;phosS28 peptide in the FP assay (Fig. 1F). E721–29 contains an LxCxExL motif and inhibits LIN52 from interacting with p130, indicating that E7 disrupts DREAM by competitive inhibition at the LxCxE cleft of p130.","_id":"685af522b4ac24d5329d713a"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-26T07:53:28.850Z","_id":"685af522b4ac24d5329d713b"},"version":1,"_id":"685af522b4ac24d5329d7138","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0005632","ec_name":"fluorescence anisotropy evidence used in manual assertion","ec_ontology":"ECO","start":16,"end":40,"interaction_partner":[{"db":"UniProt","id":"P06400","partner_start":372,"partner_end":787,"_id":"685af522b4ac24d5329d713d"}],"reference_html":"Targeting mechanism of the retinoblastoma tumor suppressor by a prototypical viral oncoprotein. Structural modularity, intrinsic disorder and phosphorylation of human papillomavirus E7. <i> Chemes LB, Sánchez IE, Smal C, de Prat-Gay G. </i> FEBS J, 2010","reference_id":"20088881","region_id":"DP00024r027","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"This implies that there is one binding site for the E7(1-40) peptide per RbAB monomer and that the stoichiometry of the E7(1-40)–RbAB interaction is 1 : 1.","_id":"685af522b4ac24d5329d713e"},{"type":"Results","text":"The CR1 region does not appear to contribute to RbAB binding within the context of an E7N monomer, as shown by the fact that the E7(16-40) and E7(1-40) peptides have the same affinity for the RbAB domain (Table 1).","_id":"685af522b4ac24d5329d713f"},{"type":"Results","text":"Therefore, our data show that the LxCxE motif contributes about 90% of the total binding energy for the HPV16 E7–RbAB interaction, providing quantitative support to previous results [[47]].","_id":"685af522b4ac24d5329d7140"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-26T08:36:10.574Z","_id":"685af522b4ac24d5329d7141"},"version":1,"_id":"685af522b4ac24d5329d713c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":31,"end":31,"statements":[{"type":null,"text":"The phosphorylated E7(16-40) peptide was obtained by incorporation of phosphoserine, instead of serine, in the synthesis.","_id":"685af523b4ac24d5329d7146"}],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af522b4ac24d5329d7145"},{"start":32,"end":32,"statements":[{"type":null,"text":"The phosphorylated E7(16-40) peptide was obtained by incorporation of phosphoserine, instead of serine, in the synthesis.","_id":"685af523b4ac24d5329d7148"}],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d7147"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":16,"end":40,"interaction_partner":[],"reference_html":"Targeting mechanism of the retinoblastoma tumor suppressor by a prototypical viral oncoprotein. Structural modularity, intrinsic disorder and phosphorylation of human papillomavirus E7. <i> Chemes LB, Sánchez IE, Smal C, de Prat-Gay G. </i> FEBS J, 2010","reference_id":"20088881","region_id":"DP00024r028","released":"2022_03","sample":[],"sequence_construct":"QPETTDLYCYEQLNDSSEEEDEIDG","statement":[{"type":"Results","text":"We tested the E7 CR2 region for PII content by measuring the far-UV CD spectra of the E7(16-40) and the E7(16-40)PP peptides at 5 °C. Both peptides presented a CD spectrum characteristic for a disordered polypeptide with a positive band at 218 nm, which is characteristic of the PII conformation (Fig. 5A).","_id":"685af522b4ac24d5329d7143"},{"type":"Results","text":"Overall, our data indicate that both peptides from the HPV16 E7 CR2 region present residual PII structure in equilibrium with disordered conformations.","_id":"685af522b4ac24d5329d7144"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-26T08:36:02.723Z","_id":"685af523b4ac24d5329d7149"},"version":1,"_id":"685af522b4ac24d5329d7142","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":40,"interaction_partner":[],"reference_html":"Targeting mechanism of the retinoblastoma tumor suppressor by a prototypical viral oncoprotein. Structural modularity, intrinsic disorder and phosphorylation of human papillomavirus E7. <i> Chemes LB, Sánchez IE, Smal C, de Prat-Gay G. </i> FEBS J, 2010","reference_id":"20088881","region_id":"DP00024r029","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Far-UV CD analyses showed that HPV16 E7(1-40) displayed an extended PII structure, which was stabilized by phosphorylation of serine residues S31 and S32 [[23]].","_id":"685af523b4ac24d5329d714b"},{"type":"Results","text":"Both peptides presented a CD spectrum characteristic for a disordered polypeptide with a positive band at 218 nm, which is characteristic of the PII conformation (Fig. 5A).","_id":"685af523b4ac24d5329d714c"},{"type":"Results","text":"Overall, our data indicate that both peptides from the HPV16 E7 CR2 region present residual PII structure in equilibrium with disordered conformations.","_id":"685af523b4ac24d5329d714d"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-26T08:35:57.310Z","_id":"685af523b4ac24d5329d714e"},"version":1,"_id":"685af523b4ac24d5329d714a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[{"deviation":null,"statements":[],"term_id":"NCIT:C45997","unit_id":"UO:0000196","unit_name":"pH","value":4,"_id":"685af523b4ac24d5329d7150"}],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":40,"interaction_partner":[],"reference_html":"The N-terminal module of HPV16 E7 is an intrinsically disordered domain that confers conformational and recognition plasticity to the oncoprotein. <i> García-Alai MM, Alonso LG, de Prat-Gay G. </i> Biochemistry, 2007","reference_id":"17715947","region_id":"DP00024r030","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In addition, we carried out pulse field gradient NMR experiments at 1 mM E7(1−40), and from the diffusion coefficient the domain was shown to be monomeric, with a calculated stokes radius of 21.26 Å, expected for an extended fragment of that number of residues (not shown). When the same experiment is carried out at pH 4.0, the hydrodynamic volume of CI2(1-40) stays unmodified, but E7(1-40) elutes at a larger volume from the column, strongly suggesting that the conformational change induced at low pH yields a more compact structure (Figure 3).","_id":"685af523b4ac24d5329d7151"},{"type":"Discussion","text":"At pH 4.0 and below, the negatively charged residues are neutralized, the charge repulsion decreases, and more R-helix is formed.","_id":"685af523b4ac24d5329d7152"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-17T11:35:47.188Z","_id":"685af523b4ac24d5329d7153"},"version":1,"_id":"685af523b4ac24d5329d714f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[{"deviation":null,"statements":[],"term_id":"NCIT:C45997","unit_id":"UO:0000196","unit_name":"pH","value":3,"_id":"685af523b4ac24d5329d7155"}],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":40,"interaction_partner":[],"reference_html":"The N-terminal module of HPV16 E7 is an intrinsically disordered domain that confers conformational and recognition plasticity to the oncoprotein. <i> García-Alai MM, Alonso LG, de Prat-Gay G. </i> Biochemistry, 2007","reference_id":"17715947","region_id":"DP00024r031","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The difference spectrum between E7(1-40) at pH 7.5 and pH 3.0 displays the positive distinctive band at 218 nm present in PII models (Figure 2b inset).","_id":"685af523b4ac24d5329d7156"},{"type":"Discussion","text":"This result is in excellent agreement with the observed conformational transition by CD, where the molar ellipticity at 220 nm decreased when the pH is lowered (not\nshown).","_id":"685af523b4ac24d5329d7157"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-17T11:35:46.171Z","_id":"685af523b4ac24d5329d7158"},"version":1,"_id":"685af523b4ac24d5329d7154","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":31,"end":31,"statements":[],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d715a"},{"start":32,"end":32,"statements":[],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d715b"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-02-06T20:06:22.515Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":51,"interaction_partner":[],"reference_html":"Characterization of the High-Affinity Fuzzy Complex between the Disordered Domain of the E7 Oncoprotein from High-Risk HPV and the TAZ2 Domain of CBP. <i> Risør MW, Jansma AL, Medici N, Thomas B, Dyson HJ, Wright PE. </i> Biochemistry, 2021","reference_id":"34905914","region_id":"DP00024r032","released":"2023_06","sample":[{"db":"UniProt","deviation":null,"id":"P45481","statements":[],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d715c"}],"statement":[{"type":"Abstract","text":"Using a variety of spectroscopic and biochemical tools, we find that despite its nanomolar affinity, the HPV16 E7 complex with TAZ2 is disordered and highly dynamic. The disordered domain of HPV16 E7 protein does not adopt a single conformation on the surface of TAZ2 but engages promiscuously with its target through multiple interactions involving two conserved motifs, termed CR1 and CR2, that occupy an extensive binding surface on TAZ2.","_id":"685af523b4ac24d5329d715d"},{"type":"Results","text":"It is clear from all of the results shown in Figures 2, 3, 6, and 9 that no single E7 structure will be able to satisfy all of the NOE constraints.","_id":"685af523b4ac24d5329d715e"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-02-07T09:52:21.959Z","_id":"685af523b4ac24d5329d715f"},"version":2,"_id":"685af523b4ac24d5329d7159","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":31,"end":31,"statements":[],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d7161"},{"start":32,"end":32,"statements":[],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d7162"}],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":51,"interaction_partner":[{"db":"UniProt","id":"P45481","partner_start":1764,"partner_end":1855,"_id":"685af523b4ac24d5329d7163"}],"reference_html":"","reference_id":"34905914","region_id":"DP00024r033","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Using a variety of spectroscopic and biochemical tools, we find that despite its nanomolar affinity, the HPV16 E7 complex with TAZ2 is disordered and highly dynamic. The disordered domain of HPV16 E7 protein does not adopt a single conformation on the surface of TAZ2 but engages promiscuously with its target through multiple interactions involving two conserved motifs, termed CR1 and CR2, that occupy an extensive binding surface on TAZ2.","_id":"685af523b4ac24d5329d7164"},{"type":"Results","text":"1H-15N HSQC spectra of 15N-labeled ppE7(1−51) titrated with unlabeled TAZ2 show stepwise chemical shift perturbations as a function of increasing molar amounts of TAZ2 (Figure 2A), an indication that the complex and its components are in fast exchange on the NMR chemical shift timescale.","_id":"685af523b4ac24d5329d7165"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-08-26T18:35:37.741Z","_id":"685af523b4ac24d5329d7166"},"version":1,"_id":"685af523b4ac24d5329d7160","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"All of the TAZ2 interacting partners were expressed as His6-GB1 fusions, including E7(1−51), E7(17−51), the N-terminal fusions E7(1−51)-TAZ2, E7(1−51)-GS3-TAZ2, and E7(1− 40)-TAZ2, the C-terminal fusions TAZ2-E7(1−51) and TAZ2-GS2-E7(1−51), as well as E7(1−51) C24A/A50C for labeling with Alexa 594 for fluorescence anisotropy measurements and E7(1−51)H9C/C24A for incorporation of a nitroxide spin label.","_id":"685af523b4ac24d5329d7169"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys24Ala","_id":"685af523b4ac24d5329d7168"},{"start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"All of the TAZ2 interacting partners were expressed as His6-GB1 fusions, including E7(1−51), E7(17−51), the N-terminal fusions E7(1−51)-TAZ2, E7(1−51)-GS3-TAZ2, and E7(1− 40)-TAZ2, the C-terminal fusions TAZ2-E7(1−51) and TAZ2-GS2-E7(1−51), as well as E7(1−51) C24A/A50C for labeling with Alexa 594 for fluorescence anisotropy measurements and E7(1−51)H9C/C24A for incorporation of a nitroxide spin label.","_id":"685af523b4ac24d5329d716b"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala50Cys","_id":"685af523b4ac24d5329d716a"}],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0005632","ec_name":"fluorescence anisotropy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":51,"interaction_partner":[{"db":"UniProt","id":"P45481","partner_start":1764,"partner_end":1855,"_id":"685af523b4ac24d5329d716c"}],"reference_html":"","reference_id":"34905914","region_id":"DP00024r034","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The anisotropy change was fitted to competition models,55 which provided affinity estimates for the individual competing peptides (Figure 5). The results clearly demonstrate that cooperativity between the CR1 and CR2 binding motifs enhances E7 affinity toward TAZ2.","_id":"685af523b4ac24d5329d716d"},{"type":"Results","text":"Only when CR1 and CR2 are both present in the peptide is E7 able to reach its characteristic nM binding affinity (KD 22 nM,37 compared to 100 nM under the current conditions).","_id":"685af523b4ac24d5329d716e"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-08-26T20:44:53.269Z","_id":"685af523b4ac24d5329d716f"},"version":1,"_id":"685af523b4ac24d5329d7167","reference_source":"pmid"}],"__v":0,"disorder_content":0.5204081632653061,"disprot_consensus":{"full":[{"start":1,"end":40,"type":"T"},{"start":41,"end":51,"type":"D"}],"Structural state":[{"start":1,"end":51,"type":"D"}],"Structural transition":[{"start":1,"end":40,"type":"T"}],"Biological process":[{"start":21,"end":29,"type":"F"}],"Molecular function":[{"start":1,"end":51,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00746","name":"LPXTG cell wall anchor motif","start":975,"end":1016},{"id":"PF02986","name":"Fibronectin binding repeat","start":769,"end":806},{"id":"PF02986","name":"Fibronectin binding repeat","start":807,"end":845},{"id":"PF02986","name":"Fibronectin binding repeat","start":846,"end":877},{"id":"PF04650","name":"YSIRK type signal peptide","start":3,"end":27},{"id":"PF10425","name":"C-terminus of bacterial fibrinogen-binding adhesin","start":349,"end":496},{"id":"PF17961","name":"Bacterial Ig domain","start":219,"end":317}],"gene3D":[{"start":186,"end":337,"id":"2.60.40.1280","name":"2.60.40.1280"},{"start":338,"end":505,"id":"2.60.40.1290","name":"2.60.40.1290"}]},"uniref50":"UniRef50_P14738","sequence":"MKNNLRYGIRKHKLGAASVFLGTMIVVGMGQDKEAAASEQKTTTVEENGNSATDNKTSETQTTATNVNHIEETQSYNATVTEQPSNATQVTTEEAPKAVQAPQTAQPANIETVKEEVVKEEAKPQVKETTQSQDNSGDQRQVDLTPKKATQNQVAETQVEVAQPRTASESKPRVTRSADVAEAKEASNAKVETGTDVTSKVTVEIGSIEGHNNTNKVEPHAGQRAVLKYKLKFENGLHQGDYFDFTLSNNVNTHGVSTARKVPEIKNGSVVMATGEVLEGGKIRYTFTNDIEDKVDVTAELEINLFIDPKTVQTNGNQTITSTLNEEQTSKELDVKYKDGIGNYYANLNGSIETFNKANNRFSHVAFIKPNNGKTTSVTVTGTLMKGSNQNGNQPKVRIFEYLGNNEDIAKSVYANTTDTSKFKEVTSNMSGNLNLQNNGSYSLNIENLDKTYVVHYDGEYLNGTDEVDFRTQMVGHPEQLYKYYYDRGYTLTWDNGLVLYSNKANGNEKNGPIIQNNKFEYKEDTIKETLTGQYDKNLVTTVEEEYDSSTLDIDYHTAIDGGGGYVDGYIETIEETDSSAIDIDYHTAVDSEAGHVGGYTESSEESNPIDFEESTHENSKHHADVVEYEEDTNPGGGQVTTESNLVEFDEESTKGIVTGAVSDHTTVEDTKEYTTESNLIELVDELPEEHGQAQGPVEEITKNNHHISHSGLGTENGHGNYDVIEEIEENSHVDIKSELGYEGGQNSGNQSFEEDTEEDKPKYEQGGNIVDIDFDSVPQIHGQNKGNQSFEEDTEKDKPKYEHGGNIIDIDFDSVPHIHGFNKHTEIIEEDTNKDKPSYQFGGHNSVDFEEDTLPKVSGQNEGQQTIEEDTTPPIVPPTPPTPEVPSEPETPTPPTPEVPSEPETPTPPTPEVPSEPETPTPPTPEVPAEPGKPVPPAKEEPKKPSKPVEQGKVVTPVIEINEKVKAVAPTKKPQSKKSELPETGGEESTNKGMLFGGLFSILGLALLRRNKKNHKA","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Staphylococcaceae","Staphylococcus"],"uniref90":"UniRef90_P14738","disprot_id":"DP00025","ncbi_taxon_id":93061,"regions_counter":10,"creator":"imicetic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":858,"region_id":"DP00025r001","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Conformational changes in the fibronectin binding MSCRAMMs are induced by ligand binding. <i> House-Pompeo K, Xu Y, Joh D, Speziale P, Höök M. </i> J Biol Chem, 1996","term_id":"IDPO:0000002","curator_id":"vnugnes","start":746,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-01-13T13:09:02.199Z","reference_source":"pmid","term_name":"disorder","reference_id":"8576127","uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The far-UV CD spectra of rFNBD-A, rFNBD-B, rFNBD-D, and rFNBD-P were very similar and were dominated by a large minimum at ∼200 nm (Fig. 2). This type of spectra is characteristic of proteins that are predominately composed of random coil and γ-turns and contain a minimum amount of α-helix or β-sheet conformation(15., 16.).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-16T09:57:08.290Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":858,"term_name":"disorder to order","released":"2022_12","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Conformational changes in the fibronectin binding MSCRAMMs are induced by ligand binding. <i> House-Pompeo K, Xu Y, Joh D, Speziale P, Höök M. </i> J Biol Chem, 1996","term_id":"IDPO:0000011","curator_id":"vnugnes","start":746,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"8576127","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-09-05T17:37:15.013Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00025r003","uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02751"}],"statement":[{"text":"Because of the defined, stable, secondary and tertiary structure in N29, the minute change in the intrinsic Trp fluorescence in N29 on binding of rFNBD-A, and the apparent lack of stable ordered conformation in the rFNBD proteins, the large conformational shift seen in the far-UV CD on recombinant adhesin binding to N29 is largely attributed to the rFNBD proteins assuming a predominately β-sheet structure on binding to N29.","type":"Results"},{"text":"N29 peptide corresponds to the NH2-terminal domain of the human fibronectin.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:16:38.290Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":858,"term_name":"protein binding","released":"2022_12","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Conformational changes in the fibronectin binding MSCRAMMs are induced by ligand binding. <i> House-Pompeo K, Xu Y, Joh D, Speziale P, Höök M. </i> J Biol Chem, 1996","term_id":"GO:0005515","curator_id":"vnugnes","start":746,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"8576127","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2022-09-05T17:37:04.721Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00025r004","uniprot_changed":true,"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P02751","operator":"and","partner_start":null,"partner_end":null}],"statement":[{"text":"Because of the defined, stable, secondary and tertiary structure in N29, the minute change in the intrinsic Trp fluorescence in N29 on binding of rFNBD-A, and the apparent lack of stable ordered conformation in the rFNBD proteins, the large conformational shift seen in the far-UV CD on recombinant adhesin binding to N29 is largely attributed to the rFNBD proteins assuming a predominately β-sheet structure on binding to N29.","type":"Results"},{"text":"N29 peptide corresponds to the NH2-terminal domain of the human fibronectin.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:16:40.380Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":874,"region_id":"DP00025r005","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Structural and dynamical characterization of a biologically active unfolded fibronectin-binding protein from Staphylococcus aureus. <i> Penkett CJ, Redfield C, Jones JA, Dodd I, Hubbard J, Smith RA, Smith LJ, Dobson CM. </i> Biochemistry, 1998","term_id":"IDPO:0000002","curator_id":"vnugnes","start":745,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-09-05T16:57:40.401Z","reference_source":"pmid","term_name":"disorder","reference_id":"9836601","uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"In the spectra of D1−D4 there is a large amount of resonance overlap, the limited 1H chemical shift dispersion reflecting the unfolded nature of the protein; this severely hampered the sequential assignment process.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:16:30.015Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":874,"region_id":"DP00025r007","released":"2022_12","ec_id":"ECO:0006165","reference_html":"NMR analysis of main-chain conformational preferences in an unfolded fibronectin-binding protein. <i> Penkett CJ, Redfield C, Dodd I, Hubbard J, McBay DL, Mossakowska DE, Smith RA, Dobson CM, Smith LJ. </i> J Mol Biol, 1997","term_id":"IDPO:0000002","curator_id":"vnugnes","start":745,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-09-05T16:58:12.774Z","reference_source":"pmid","term_name":"disorder","reference_id":"9398523","uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The unfolded nature of D1-D4 gives rise to very high resolution spectra enabling accurate measurement of NMR parameters. The residue-specific NMR data for D1-D4, including chemical shifts, coupling constants and NOEs, reflect the absence of secondary structure and the predominantly unfolded nature of this protein.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:16:32.884Z"}},{"start":745,"end":874,"reference_id":"8576127","reference_source":"pmid","reference_html":"Conformational changes in the fibronectin binding MSCRAMMs are induced by ligand binding. <i> House-Pompeo K, Xu Y, Joh D, Speziale P, Höök M. </i> J Biol Chem, 1996","date":"2025-03-19T16:22:51.105Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006301","ec_ontology":"ECO","ec_name":"protein thermal shift assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"region_id":"DP00025r009","statement":[{"text":"By monitoring the elution volume (Ve) of rFNBD-B using gel-permeation chromatography as the concentration of GdnHCl was increased from 0 to 6 M, it was determined that rFNBD-B does not follow a cooperative unfolding model (Fig. 3).","type":"Results"}]},{"start":745,"end":874,"reference_id":"8576127","reference_source":"pmid","reference_html":"Conformational changes in the fibronectin binding MSCRAMMs are induced by ligand binding. <i> House-Pompeo K, Xu Y, Joh D, Speziale P, Höök M. </i> J Biol Chem, 1996","date":"2022-09-05T17:13:46.843Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00025r010","statement":[{"text":"It was determined that ANS did not bind to rFNBD-A or rFNBD-B under any conditions tested, indicating that the proteins do not appear to be capable of forming localized, stable regions of hydrophobic side chains (data not shown).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:16:36.053Z"}}],"released":"2016_10","uniref100":"UniRef100_P14738","date":"2016-09-12T11:54:00.000Z","acc":"P14738","name":"Fibronectin-binding protein A","length":1018,"organism":"Staphylococcus aureus (strain NCTC 8325)","dataset":["Bacterial virulence-related proteins"],"uniparc":"UPI000012AB21","UniParc":"UPI000012AB21","genes":[{"name":{"value":"fnbA"},"olnNames":[{"value":"SAOUHSC_02803"}]}],"alphafold_very_low_content":0.637524557956778,"disorder_content":0.12770137524557956,"disprot_consensus":{"full":[{"start":745,"end":745,"type":"D"},{"start":746,"end":858,"type":"T"},{"start":859,"end":874,"type":"D"}],"Structural state":[{"start":745,"end":874,"type":"D"}],"Structural transition":[{"start":746,"end":858,"type":"T"}],"Molecular function":[{"start":746,"end":858,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00669","name":"Bacterial flagellin N-terminal helical region","start":5,"end":143},{"id":"PF00700","name":"Bacterial flagellin C-terminal helical region","start":409,"end":494},{"id":"PF08884","name":"Flagellin D3 domain","start":193,"end":280},{"id":"PF21504","name":"Flagellin, barrel domain","start":347,"end":390}],"gene3D":[{"start":191,"end":285,"id":"2.30.220.10","name":"f41 fragment of flagellin, C-terminal domain"},{"start":45,"end":454,"id":"1.20.1330.10","name":"f41 fragment of flagellin, N-terminal domain"},{"start":177,"end":402,"id":"2.170.280.10","name":"f41 fragment of flagellin, middle domain"}]},"uniref50":"UniRef50_P06179","sequence":"MAQVINTNSLSLLTQNNLNKSQSALGTAIERLSSGLRINSAKDDAAGQAIANRFTANIKGLTQASRNANDGISIAQTTEGALNEINNNLQRVRELAVQSANSTNSQSDLDSIQAEITQRLNEIDRVSGQTQFNGVKVLAQDNTLTIQVGANDGETIDIDLKQINSQTLGLDTLNVQQKYKVSDTAATVTGYADTTIALDNSTFKASATGLGGTDQKIDGDLKFDDTTGKYYAKVTVTGGTGKDGYYEVSVDKTNGEVTLAGGATSPLTGGLPATATEDVKNVQVANADLTEAKAALTAAGVTGTASVVKMSYTDNNGKTIDGGLAVKVGDDYYSATQNKDGSISINTTKYTADDGTSKTALNKLGGADGKTEVVSIGGKTYAASKAEGHNFKAQPDLAEAAATTTENPLQKIDAALAQVDTLRSDLGAVQNRFNSAITNLGNTVNNLTSARSRIEDSDYATEVSNMSRAQILQQAGTSVLAQANQVPQNVLSLLR","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"],"uniref90":"UniRef90_P06179","disprot_id":"DP00026","ncbi_taxon_id":99287,"regions_counter":16,"creator":"cbassot","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":65,"region_id":"DP00026r005","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Terminal regions of flagellin are disordered in solution. <i> Vonderviszt F, Kanto S, Aizawa S, Namba K. </i> J Mol Biol, 1989","term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"2810365","version":3,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"It was found that both termini of flagellin are rapidly degraded in the early steps of proteolysis.","type":"Results"},{"text":"This suggests that there are no significant intrinsic structural constraints in the terminal parts to limit the accessibility of the peptide bonds, i.e. these regions have an exceptionally flexible conformation. The readily hydrolysed terminal portions probably do not have any compact tertiary structure and are in extensive contact with the surrounding media. In contrast, the central region of the molecule, which involves the F40 and F27 fragments is quite stable against proteolysis, indicating that it is probably composed of compact structural units.","type":"Results"}],"uniprot_changed":true,"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-05T20:48:55.750Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":494,"region_id":"DP00026r009","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Terminal regions of flagellin are disordered in solution. <i> Vonderviszt F, Kanto S, Aizawa S, Namba K. </i> J Mol Biol, 1989","term_id":"IDPO:0000002","curator_id":"esalladini","start":455,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"2810365","version":3,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"This suggests that there are no significant intrinsic structural constraints in the terminal parts to limit the accessibility of the peptide bonds, i.e. these regions have an exceptionally flexible conformation. The readily hydrolysed terminal portions probably do not have any compact tertiary structure and are in extensive contact with the surrounding media. In contrast, the central region of the molecule, which involves the F40 and F27 fragments is quite stable against proteolysis, indicating that it is probably composed of compact structural units.  ","type":"Results"},{"text":"It was found that both termini of flagellin are rapidly degraded in the early steps of proteolysis.","type":"Results"}],"uniprot_changed":true,"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-05T19:13:31.926Z"}}],"released":"2016_10","uniref100":"UniRef100_P06179","date":"2016-09-02T14:17:09.000Z","acc":"P06179","name":"Flagellin","length":495,"organism":"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","dataset":[],"uniparc":"UPI000012A988","UniParc":"UPI000012A988","genes":[{"name":{"value":"fliC"},"synonyms":[{"value":"flaF"},{"value":"hag"}],"olnNames":[{"value":"STM1959"}]}],"alphafold_very_low_content":0.00404040404040404,"disorder_content":0.21212121212121213,"disprot_consensus":{"full":[{"start":1,"end":65,"type":"D"},{"start":455,"end":494,"type":"D"}],"Structural state":[{"start":1,"end":65,"type":"D"},{"start":455,"end":494,"type":"D"}]}},{"features":{"pfam":[{"id":"PF04316","name":"Anti-sigma-28 factor, FlgM","start":40,"end":87}]},"uniref50":"UniRef50_P26477","sequence":"MSIDRTSPLKPVSTVQTRETSDTPVQKTRQEKTSAATSASVTLSDAQAKLMQPGVSDINMERVEALKTAIRNGELKMDTGKIADSLIREAQSYLQSK","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"],"uniref90":"UniRef90_P26477","disprot_id":"DP00027","ncbi_taxon_id":99287,"regions_counter":6,"creator":"dpiovesan","regions":[{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":97,"term_name":"molecular function inhibitor activity","start":41,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The interaction between the flagellum specific sigma factor, sigma 28, and its inhibitor, FlgM, was examined using multidimensional heteronuclear NMR. Here we observe that free FlgM is mostly unfolded, but about 50% of the residues become structured when bound to sigma 28. Our analysis suggests that the sigma 28 binding domain of FlgM is contained within the last 57 amino acids of the protein while the first 40 amino acids are unstructured in both the free and bound states. ","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"9095196","version":4,"reference_html":"The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28. <i> Daughdrill GW, Chadsey MS, Karlinsey JE, Hughes KT, Dahlquist FW. </i> Nat Struct Biol, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140678","ec_id":"ECO:0006165","region_id":"DP00027r003","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-07T11:26:19.085Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":97,"term_name":"disorder to order","start":41,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The interaction between the flagellum specific sigma factor, sigma 28, and its inhibitor, FlgM, was examined using multidimensional heteronuclear NMR. Here we observe that free FlgM is mostly unfolded, but about 50% of the residues become structured when bound to sigma 28. Our analysis suggests that the sigma 28 binding domain of FlgM is contained within the last 57 amino acids of the protein while the first 40 amino acids are unstructured in both the free and bound states.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9095196","version":3,"reference_html":"The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28. <i> Daughdrill GW, Chadsey MS, Karlinsey JE, Hughes KT, Dahlquist FW. </i> Nat Struct Biol, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00027r004","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-07T11:26:10.718Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":97,"term_name":"protein binding","start":41,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The interaction between the flagellum specific sigma factor, sigma 28, and its inhibitor, FlgM, was examined using multidimensional heteronuclear NMR. Here we observe that free FlgM is mostly unfolded, but about 50% of the residues become structured when bound to sigma 28. Our analysis suggests that the sigma 28 binding domain of FlgM is contained within the last 57 amino acids of the protein while the first 40 amino acids are unstructured in both the free and bound states.","type":"Abstract"},{"text":"The σ28 binding domain of FlgM is in the C-terminal half","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"9095196","version":4,"reference_html":"The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28. <i> Daughdrill GW, Chadsey MS, Karlinsey JE, Hughes KT, Dahlquist FW. </i> Nat Struct Biol, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00027r005","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-07T11:26:15.225Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":97,"region_id":"DP00027r006","start":1,"term_id":"IDPO:0000002","statement":[{"text":"The interaction between the flagellum specific sigma factor, sigma 28, and its inhibitor, FlgM, was examined using multidimensional heteronuclear NMR. Here we observe that free FlgM is mostly unfolded, but about 50% of the residues become structured when bound to sigma 28. Our analysis suggests that the sigma 28 binding domain of FlgM is contained within the last 57 amino acids of the protein while the first 40 amino acids are unstructured in both the free and bound states. ","type":"Abstract"},{"text":"The NH-NOE values for 38 of the first 45 N-terminal residues are shown to the left of the ordinate axis. NH-NOEs for the majority of these residues are large and nega-tive ( < -1.0) indicating the region is very flexible.","type":"Article"},{"text":"The flexibility present in the C-terminal half of FlgM is best indicated by periodic breaks in the positive NH-NOE values. Flexibility in this region is also suggested by the smaller than expected positive NH-NOE values.","type":"Article"},{"text":"The NMR resonances for the N-terminal 40 amino acids of FlgM show no significant chemical shift or line shape changes in the presence of cr28. This demonstrates that the N-terminal 40 amino acid residues are disordered whether or not FlgM is bound to cr28.","type":"Conclusion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9095196","version":2,"reference_html":"The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28. <i> Daughdrill GW, Chadsey MS, Karlinsey JE, Hughes KT, Dahlquist FW. </i> Nat Struct Biol, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-07T11:26:03.063Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P26477","date":"2016-08-11T13:29:58.000Z","acc":"P26477","name":"Negative regulator of flagellin synthesis","length":97,"organism":"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","dataset":[],"UniParc":"UPI0000000EBB","genes":[{"name":{"value":"flgM"},"synonyms":[{"value":"flgR"},{"value":"mviS"}],"olnNames":[{"value":"STM1172"}]}],"alphafold_very_low_content":0.20618556701030927,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":40,"type":"D"},{"start":41,"end":97,"type":"T"}],"Structural state":[{"start":1,"end":97,"type":"D"}],"Molecular function":[{"start":41,"end":97,"type":"F"}],"Structural transition":[{"start":41,"end":97,"type":"T"}]}},{"features":{"pfam":[{"id":"PF05456","name":"Eukaryotic translation initiation factor 4E binding protein (EIF4EBP)","start":5,"end":118}]},"uniref50":"UniRef50_Q13541","sequence":"MSGGSSCSQTPSRAIPATRRVVLGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVTKTPPRDLPTIPGVTSPSSDEPPMEASQSHLRNSPEDKRAGGEESQFEMDI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q13541","disprot_id":"DP00028","ncbi_taxon_id":9606,"regions_counter":46,"creator":"ppereira","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":118,"region_id":"DP00028r007","released":"2023_06","ec_id":"ECO:0006165","reference_html":"The interaction of eIF4E with 4E-BP1 is an induced fit to a completely disordered protein. <i> Fletcher CM, Wagner G. </i> Protein Sci, 1998","term_id":"IDPO:0000002","curator_id":"vnugnes","start":4,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"9684899","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-01-12T15:30:31.689Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser6Pro","start":null,"end":null,"position":null}],"curator_orcid":"0000-0001-8399-7907","statement":[{"text":"NMR  spectra of 4E-BPI displayed  very high  sensitivity due to long relaxation times, typical of unfolded proteins.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:31:07.674Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":66,"term_name":"protein binding","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural basis for mRNA Cap-Binding regulation of eukaryotic initiation factor 4E by 4E-binding protein, studied by spectroscopic, X-ray crystal structural, and molecular dynamics simulation methods. <i> Tomoo K, Matsushita Y, Fujisaki H, Abiko F, Shen X, Taniguchi T, Miyagawa H, Kitamura K, Miura K, Ishida T. </i> Biochim Biophys Acta, 2005","statement":[{"text":"Although it was reported in an SPR experiment [29] that the interaction between eIF4E and m7GpppA is significantly increased in the presence of 4E-BP1, the present X-ray analysis showed that little structural change of the eIF4E cap-binding pocket is caused by the binding of the 4E-BP1 peptide in the solid state.","type":"Results"}],"term_id":"GO:0005515","curator_id":"ppereira","start":47,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"16271312","version":4,"curator_orcid":"0000-0003-0969-5438","date":"2023-02-15T15:06:33.157Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00028r010","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"1WKW"}],"interaction_partner":[{"db":"UniProt","id":"P06730","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-22T15:06:08.036Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":63,"term_name":"protein binding","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural basis for nematode eIF4E binding an m(2,2,7)G-Cap and its implications for translation initiation. <i> Liu W, Jankowska-Anyszka M, Piecyk K, Dickson L, Wallace A, Niedzwiecka A, Stepinski J, Stolarski R, Darzynkiewicz E, Kieft J, Zhao R, Jones DN, Davis RE. </i> Nucleic Acids Res, 2011","statement":[{"text":"Using this shorter construct in the presence of the human 4E-BP1 peptide, we obtained diffraction quality crystals and determined the co-crystal structures of Ascaris eIF4E-3 with m 2,2,7 GTP and m 7 GTP ( Table 3 ).","type":"Results"}],"term_id":"GO:0005515","curator_id":"ppereira","start":51,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"21965542","version":4,"curator_orcid":"0000-0003-0969-5438","date":"2023-02-15T15:07:07.376Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00028r013","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"3M94"},{"db":"PDB","id":"3M93"}],"interaction_partner":[{"db":"UniProt","id":"Q6PKX2","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-22T15:05:55.732Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":68,"term_name":"translation initiation factor binding","released":"2023_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"4E binding proteins inhibit the translation factor eIF4E without folded structure. <i> Fletcher CM, McGuire AM, Gingras AC, Li H, Matsuo H, Sonenberg N, Wagner G. </i> Biochemistry, 1998","statement":[{"text":"A 20 Residue Fragment of 4E-BP1 Binds to eIF4E and Inhibits Translation in Vitro.","type":"Results"},{"text":"Titration of 15N-labeled eIF4E with this peptide produced some, but not all, of the same chemical shift changes as the whole 4E-BP1 (Figure 3C). This indicates that the peptide binds to eIF4E, although it suggests that the peptide does not make as many contacts or bind in quite the same way as the whole 4E-BP1.","type":"Results"}],"term_id":"GO:0031369","curator_id":"vnugnes","start":49,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"9453748","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-01-12T14:30:06.839Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00028r015","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a translation initiation factor, any polypeptide factor involved in the initiation of ribosome-mediated translation.\" [GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser6Pro","start":null,"end":null,"position":null}],"interaction_partner":[{"db":"UniProt","id":"P63073","operator":null,"partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:31:56.001Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":118,"region_id":"DP00028r016","released":"2022_03","ec_id":"ECO:0006204","reference_html":"4E binding proteins inhibit the translation factor eIF4E without folded structure. <i> Fletcher CM, McGuire AM, Gingras AC, Li H, Matsuo H, Sonenberg N, Wagner G. </i> Biochemistry, 1998","statement":[{"text":"The CD spectrum of 4E-BP1 is typical of an unfolded protein, although a very shallow minimum at 220-230 nm suggests a minimal amount of helical secondary structure (Figure 2B).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":5,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"9453748","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-12T13:37:06.977Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":118,"region_id":"DP00028r017","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Effect of temperature on the conformation of natively unfolded protein 4E-BP1 in aqueous and mixed solutions containing trifluoroethanol and hexafluoroisopropanol. <i> Hackl EV. </i> Protein J, 2015","statement":[{"text":"BP1 protein has a distinctive far-UV CD spectrum typical for a protein in the pre-molten globule state (Fig. 1, curve 2) with a characteristic deep minimum in the vicinity of 200 nm and relatively low ellipticity around 220 nm.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":1,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"25503819","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:31:42.097Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":83,"term_name":"protein binding","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"GIGYF1/2 proteins use auxiliary sequences to selectively bind to 4EHP and repress target mRNA expression. <i> Peter D, Weber R, Sandmeir F, Wohlbold L, Helms S, Bawankar P, Valkov E, Igreja C, Izaurralde E. </i> Genes Dev, 2017","statement":[{"text":"The 4E-BP1 and GYF1/2 canonical motifs adopt a helical conformation on the dorsal surface of 4EHP, whereas the noncanonical sequences bind to the lateral surface of 4EHP using a binding mode similar to that described for 4E-BP1 in complex with eIF4E (Fig. 2C–J; Supplemental Fig. S4E,F; Peter et al. 2015a; Sekiyama et al. 2015). ","type":"Results"}],"term_id":"GO:0005515","curator_id":"ppereira","start":49,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"28698298","version":4,"curator_orcid":"0000-0003-0969-5438","date":"2023-02-15T15:13:07.553Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00028r019","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"5NVN"}],"interaction_partner":[{"db":"UniProt","id":"O60573","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-22T15:04:26.921Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":63,"term_name":"protein binding","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural insights into the allosteric effects of 4EBP1 on the eukaryotic translation initiation factor eIF4E. <i> Siddiqui N, Tempel W, Nedyalkova L, Volpon L, Wernimont AK, Osborne MJ, Park HW, Borden KL. </i> J Mol Biol, 2012","statement":[{"text":"Seemingly, binding of the 4EBP1 peptide does not appear to affect the cap binding pocket of eIF4E.","type":"Results"}],"term_id":"GO:0005515","curator_id":"ppereira","start":50,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"22178476","version":4,"curator_orcid":"0000-0003-0969-5438","date":"2023-02-15T15:15:48.906Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00028r021","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"3U7X"}],"interaction_partner":[{"db":"UniProt","id":"P06730","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-22T15:04:12.122Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":118,"region_id":"DP00028r022","released":"2022_03","ec_id":"ECO:0006165","reference_html":"4E binding proteins inhibit the translation factor eIF4E without folded structure. <i> Fletcher CM, McGuire AM, Gingras AC, Li H, Matsuo H, Sonenberg N, Wagner G. </i> Biochemistry, 1998","statement":[{"text":"We concluded that the purified 4E-BPs have little or no folded structure in solution.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":5,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"9453748","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-12T13:36:42.272Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":118,"term_name":"translation initiation factor binding","released":"2023_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"4E binding proteins inhibit the translation factor eIF4E without folded structure. <i> Fletcher CM, McGuire AM, Gingras AC, Li H, Matsuo H, Sonenberg N, Wagner G. </i> Biochemistry, 1998","statement":[{"text":"Furthermore, small but clear changes were observed in the spectra of both 4E-BPs upon addition of an approximately equimolar amount of eIF4E (Figure 4). We concluded that most or all of the unfolded 4E-BP in our samples binds to eIF4E. The broader lines observed for eIF4E upon addition of 4E-BP1 are consistent with the formation of a complex.","type":"Results"}],"term_id":"GO:0031369","curator_id":"vnugnes","start":4,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"9453748","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-01-12T14:31:01.617Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00028r023","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a translation initiation factor, any polypeptide factor involved in the initiation of ribosome-mediated translation.\" [GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser6Pro","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"The 4E-BP1 construct lacked the three N-terminal residues of the native sequence and had a substitution of proline for serine at the third position."}]}],"interaction_partner":[{"db":"UniProt","id":"P63073","operator":null,"partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:31:59.890Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":83,"term_name":"protein binding","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Molecular architecture of 4E-BP translational inhibitors bound to eIF4E. <i> Peter D, Igreja C, Weber R, Wohlbold L, Weiler C, Ebertsch L, Weichenrieder O, Izaurralde E. </i> Mol Cell, 2015","statement":[{"text":"The structures of Dm eIF4E and Hs eIF4E are similar to the structures of free or bound eIF4E from diverse organisms, and no major conformational changes in the proteins occur upon 4E-BP binding (Figures 1B–1H and S2A) (Gross et al., 2003, Kinkelin et al., 2012, Mizuno et al., 2008, Paku et al., 2012, Papadopoulos et al., 2014, Siddiqui et al., 2012, Umenaga et al., 2011, Volpon et al., 2006).","type":"Results"}],"term_id":"GO:0005515","curator_id":"ppereira","start":49,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"25702871","version":4,"curator_orcid":"0000-0003-0969-5438","date":"2023-02-15T15:15:17.940Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00028r025","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"4UED"}],"interaction_partner":[{"db":"UniProt","id":"P06730","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-22T15:03:11.746Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":64,"term_name":"protein binding","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Design of nucleotide-mimetic and non-nucleotide inhibitors of the translation initiation factor eIF4E: Synthesis, structural and functional characterisation. <i> Soukarieh F, Nowicki MW, Bastide A, Pöyry T, Jones C, Dudek K, Patwardhan G, Meullenet F, Oldham NJ, Walkinshaw MD, Willis AE, Fischer PM. </i> Eur J Med Chem, 2016","statement":[{"text":"eIF4E was co-crystallised with either an eIF4G- or a 4E-BP-derived peptide (designated 4G and 4EBP, respectively) and one of three of the m7GMP-derived analogues (squaramides 4a and 4f, sulfonamide 7a).","type":"Results"}],"term_id":"GO:0005515","curator_id":"ppereira","start":51,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"27592390","version":4,"curator_orcid":"0000-0003-0969-5438","date":"2023-02-15T15:14:53.850Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00028r027","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"5EKV"}],"interaction_partner":[{"db":"UniProt","id":"P06730","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-22T15:02:50.908Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":67,"term_name":"protein binding","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Cap-dependent translation initiation in eukaryotes is regulated by a molecular mimic of eIF4G. <i> Marcotrigiano J, Gingras AC, Sonenberg N, Burley SK. </i> Mol Cell, 1999","statement":[{"text":"Both oligopeptides (eIF4GII orange, 4E-BP1 yellow) adopt an L-shaped extended chain/α-helical structure, which interacts with the convex dorsal surface of eIF4E (shown in blue).","type":"Results"}],"term_id":"GO:0005515","curator_id":"ppereira","start":51,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"10394359","version":4,"curator_orcid":"0000-0003-0969-5438","date":"2023-02-15T15:18:32.529Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00028r029","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"1EJH"},{"db":"PDB","id":"1EJ4"}],"interaction_partner":[{"db":"UniProt","id":"P63073","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-22T15:01:56.535Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":84,"term_name":"protein binding","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Molecular mechanism of the dual activity of 4EGI-1: Dissociating eIF4G from eIF4E but stabilizing the binding of unphosphorylated 4E-BP1. <i> Sekiyama N, Arthanari H, Papadopoulos E, Rodriguez-Mias RA, Wagner G, Léger-Abraham M. </i> Proc Natl Acad Sci U S A, 2015","statement":[{"text":"Structure of eIF4E Bound to m7GTP and 4E-BP1.","type":"Results"}],"term_id":"GO:0005515","curator_id":"ppereira","start":50,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"26170285","version":4,"curator_orcid":"0000-0003-0969-5438","date":"2023-02-15T15:18:56.764Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00028r031","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"5BXV"}],"interaction_partner":[{"db":"UniProt","id":"P63073","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-22T15:01:26.635Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":63,"term_name":"protein binding","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural insights into parasite eIF4E binding specificity for m7G and m2,2,7G mRNA caps. <i> Liu W, Zhao R, McFarland C, Kieft J, Niedzwiecka A, Jankowska-Anyszka M, Stepinski J, Darzynkiewicz E, Jones DN, Davis RE. </i> J Biol Chem, 2009","statement":[{"text":"The 4E-BP1 peptide binds to the opposite surface of the protein and forms interactions with schistosome eIF4E almost identical to those previously observed in the human eIF4E·4E-BP complex structure (56).","type":"Results"}],"term_id":"GO:0005515","curator_id":"ppereira","start":50,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"19710013","version":4,"curator_orcid":"0000-0003-0969-5438","date":"2023-02-16T11:18:04.263Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00028r033","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"3HXG"},{"db":"PDB","id":"3HXI"}],"interaction_partner":[{"db":"UniProt","id":"G4VCF5","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-22T14:52:37.137Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":66,"term_name":"protein binding","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structures of the human eIF4E homologous protein, h4EHP, in its m7GTP-bound and unliganded forms. <i> Rosettani P, Knapp S, Vismara MG, Rusconi L, Cameron AD. </i> J Mol Biol, 2007","statement":[{"text":"The peptide is bound as an α-helix almost perpendicular to the α-helices on the convex side of the β-sheet.","type":"Results"}],"term_id":"GO:0005515","curator_id":"ppereira","start":51,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"17368478","version":4,"curator_orcid":"0000-0003-0969-5438","date":"2023-02-13T16:16:23.825Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00028r035","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"2JGC"},{"db":"PDB","id":"2JGB"}],"interaction_partner":[{"db":"UniProt","id":"O60573","operator":null,"partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-14T14:08:26.706Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":64,"term_name":"protein binding","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystallographic and mass spectrometric characterisation of eIF4E with N7-alkylated cap derivatives. <i> Brown CJ, McNae I, Fischer PM, Walkinshaw MD. </i> J Mol Biol, 2007","statement":[{"text":"Crystals were obtained for eIF4E complexed with m7GTP and a 4E-BP1 peptide (RIIYDRKFLMECRN).","type":"Results"}],"term_id":"GO:0005515","curator_id":"ppereira","start":51,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"17631896","version":4,"curator_orcid":"0000-0003-0969-5438","date":"2023-02-13T16:17:45.676Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00028r037","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"2V8X"},{"db":"PDB","id":"2V8W"},{"db":"PDB","id":"2V8Y"}],"interaction_partner":[{"db":"UniProt","id":"P06730","operator":null,"partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-14T14:08:23.686Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":118,"region_id":"DP00028r038","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Mechanisms of mTORC1 activation by RHEB and inhibition by PRAS40. <i> Yang H, Jiang X, Li B, Yang HJ, Miller M, Yang A, Dhar A, Pavletich NP. </i> Nature, 2017","statement":[{"text":"We determined the crystal structures of Arabidopsis thaliana Raptor (atRaptor) bound to TOS motif peptides from human 4EBP1...","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ahatos","start":109,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29236692","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":118,"term_name":"protein binding","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Mechanisms of mTORC1 activation by RHEB and inhibition by PRAS40. <i> Yang H, Jiang X, Li B, Yang HJ, Miller M, Yang A, Dhar A, Pavletich NP. </i> Nature, 2017","statement":[{"text":"The key phenylalanine side chain of the TOS consensus21,22 FXΦDΦ (Φ hydrophobic, X any residue) binds to a pocket together with the preceding TOS residue (thereafter F−1 position). In 4EBP1, this unit consists of the Phe114 aromatic ring making π–π stacking interactions with the Gln113 side chain, whereas in S6K1 and PRAS40 the Phe5 and Phe129 aromatic rings make functionally analogous van der Waals contacts with Val4 and Leu128, respectively (Figs 2b to d). ","type":"Results"}],"term_id":"GO:0005515","curator_id":"ppereira","start":109,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"29236692","version":4,"curator_orcid":"0000-0003-0969-5438","date":"2023-02-27T13:23:00.283Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00028r039","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"5WBJ"}],"interaction_partner":[{"db":"UniProt","id":"Q8N122","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-27T13:30:06.936Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":118,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Mechanisms of mTORC1 activation by RHEB and inhibition by PRAS40. <i> Yang H, Jiang X, Li B, Yang HJ, Miller M, Yang A, Dhar A, Pavletich NP. </i> Nature, 2017","term_id":"IDPO:0000011","curator_id":"ahatos","start":109,"term_ontology":"IDPO","curator_name":"András Hatos","reference_id":"29236692","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00028r040","ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-17T06:58:03.680Z"}},{"start":4,"end":118,"reference_id":"9453748","reference_source":"pmid","reference_html":"4E binding proteins inhibit the translation factor eIF4E without folded structure. <i> Fletcher CM, McGuire AM, Gingras AC, Li H, Matsuo H, Sonenberg N, Wagner G. </i> Biochemistry, 1998","date":"2023-01-12T13:42:33.464Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0017148","term_name":"negative regulation of translation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007717","ec_ontology":"ECO","ec_name":"translation assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser6Pro","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"The 4E-BP1 construct lacked the three N-terminal residues of the native sequence and had a substitution of proline for serine at the third position."}]}],"ec_go":"IDA","region_id":"DP00028r041","statement":[{"text":"In reticulocyte lysate assays, our samples of 4E-BP1 and 4E-BP2 inhibited translation in a dose-dependent manner and this was overcome by addition of purified eIF4E (all the experiments described in this paper used mouse eIF4E, which is 99.5% identical to the human protein).","type":"Results"}],"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA.\" [GOC:isa_complete]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:32:09.970Z"}},{"start":49,"end":68,"reference_id":"9453748","reference_source":"pmid","reference_html":"4E binding proteins inhibit the translation factor eIF4E without folded structure. <i> Fletcher CM, McGuire AM, Gingras AC, Li H, Matsuo H, Sonenberg N, Wagner G. </i> Biochemistry, 1998","date":"2023-01-12T13:55:25.440Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0017148","term_name":"negative regulation of translation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001205","ec_ontology":"ECO","ec_name":"in vitro translation assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser6Pro","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"The 4E-BP1 construct lacked the three N-terminal residues of the native sequence and had a substitution of proline for serine at the third position."}]}],"ec_go":"IDA","region_id":"DP00028r042","statement":[{"text":"Furthermore, in reticulocyte lysate assays, the peptide inhibited translation in a dose-dependent manner (Figure 5). ","type":"Results"},{"text":"Thus, residues 49−68 of 4E-BP1 are sufficient for eIF4E binding and translation inhibition.","type":"Results"}],"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA.\" [GOC:isa_complete]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:32:11.235Z"}},{"start":51,"end":64,"reference_id":"17631896","reference_source":"pmid","reference_html":"Crystallographic and mass spectrometric characterisation of eIF4E with N7-alkylated cap derivatives. <i> Brown CJ, McNae I, Fischer PM, Walkinshaw MD. </i> J Mol Biol, 2007","date":"2023-01-12T14:38:38.757Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2V8W"},{"db":"PDB","id":"2V8Y"},{"db":"PDB","id":"2V8X"}],"region_id":"DP00028r043","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06730"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:135566346"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:135566347"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:16750126"}],"statement":[{"text":"The PDB shows this region becomes ordered when in complex to the translation initiation factor eIF4E and N7-cap derivatives.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-17T06:58:01.802Z"}},{"start":51,"end":67,"reference_id":"17368478","reference_source":"pmid","reference_html":"Structures of the human eIF4E homologous protein, h4EHP, in its m7GTP-bound and unliganded forms. <i> Rosettani P, Knapp S, Vismara MG, Rusconi L, Cameron AD. </i> J Mol Biol, 2007","date":"2023-01-12T14:54:56.078Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031369","term_name":"translation initiation factor binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"O60573","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00028r044","statement":[{"text":"As discussed above, the ITC data demonstrate that the 4E-BP1 peptide binds to h4EHP. This peptide consists of residues Arg51BP1 to Val67BP1 of human 4E-BP1 and includes the recognition motif that has been defined for eIF4E (Tyr-X-X-X-X-Leu-ϕ (where X is variable and ϕ is Leu, Met or Phe)22., 23.).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a translation initiation factor, any polypeptide factor involved in the initiation of ribosome-mediated translation.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:32:13.157Z"}},{"start":51,"end":67,"reference_id":"17368478","reference_source":"pmid","reference_html":"Structures of the human eIF4E homologous protein, h4EHP, in its m7GTP-bound and unliganded forms. <i> Rosettani P, Knapp S, Vismara MG, Rusconi L, Cameron AD. </i> J Mol Biol, 2007","date":"2023-01-12T14:59:36.701Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00028r045","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60573"}],"statement":[{"text":"The peptide is bound as an α-helix almost perpendicular to the α-helices on the convex side of the β-sheet.","type":"Results"},{"text":"In the structure, the peptide is clearly defined in the electron density for all residues apart from the last.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"2JGB"},{"db":"PDB","id":"2JGC"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:31:48.880Z"}},{"start":50,"end":83,"reference_id":"38177902","reference_source":"pmid","reference_html":"eIF4E1b is a non-canonical eIF4E protecting maternal dormant mRNAs.  <i> Lorenzo-Orts L, Strobl M, Steinmetz B, Leesch F, Pribitzer C, Roehsner J, Schutzbier M, Dürnberger G, Pauli A. </i> EMBO Rep, 2023","date":"2024-01-18T13:46:25.133Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008190","term_name":"eukaryotic initiation factor 4E binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"A6NMX2","operator":null,"partner_start":60,"partner_end":242},{"db":"UniProt","id":"Q3UTA9","operator":"and","partner_start":63,"partner_end":244}],"region_id":"DP00028r046","statement":[{"text":"Unlike other class I eIF4Es, neither mouse nor human eIF4E1B interacted with eIF4G, although they bound to eIF4EBP1 and eIF4ENIF1 (Fig. 2D and Appendix Fig. S2F).","type":"Results"}],"term_comment":"","term_def":"\"Binding to eukaryotic initiation factor 4E, a polypeptide factor involved in the initiation of ribosome-mediated translation.\" [ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-17T06:58:06.176Z"}}],"released":"2016_10","uniref100":"UniRef100_Q13541","date":"2016-08-22T13:46:43.000Z","acc":"Q13541","name":"Eukaryotic translation initiation factor 4E-binding protein 1","length":118,"organism":"Homo sapiens","dataset":["Autophagy-related proteins"],"UniParc":"UPI000058E2E5","genes":[{"name":{"value":"EIF4EBP1"}}],"alphafold_very_low_content":0.211864406779661,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":50,"type":"D"},{"start":51,"end":67,"type":"T"},{"start":68,"end":108,"type":"D"},{"start":109,"end":118,"type":"T"}],"Structural state":[{"start":1,"end":118,"type":"D"}],"Molecular function":[{"start":4,"end":118,"type":"F"}],"Structural transition":[{"start":51,"end":67,"type":"T"},{"start":109,"end":118,"type":"T"}],"Biological process":[{"start":4,"end":118,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00019","name":"Transforming growth factor beta like domain","start":118,"end":210}],"gene3D":[{"start":114,"end":211,"id":"2.10.90.10","name":"Cystine-knot cytokines"}]},"uniref50":"UniRef50_Q07731","sequence":"MKLWDVVAVCLVLLHTASAFPLPAGKRLLEAPAEDHSLGHRRVPFALTSDSNMPEDYPDQFDDVMDFIQATIKRLKRSPDKQAAALPRRERNRQAAAASPENSRGKGRRGQRGKNRGCVLTAIHLNVTDLGLGYETKEELIFRYCSGSCEAAETMYDKILKNLSRSRRLTSDKVGQACCRPVAFDDDLSFLDDSLVYHILRKHSAKRCGCI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_Q07731","disprot_id":"DP00029","ncbi_taxon_id":10116,"regions_counter":2,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":113,"region_id":"DP00029r001","released":"2022_12","ec_id":"ECO:0006220","reference_html":"X-ray structure of glial cell-derived neurotrophic factor at 1.9 A resolution and implications for receptor binding. <i> Eigenbrot C, Gerber N. </i> Nat Struct Biol, 1997","term_id":"IDPO:0000002","curator_id":"vnugnes","start":78,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"9187648","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-09-05T18:20:24.358Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1AGQ"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:13:22.117Z"}}],"released":"2016_10","uniref100":"UniRef100_Q07731","date":"2016-09-12T13:39:40.000Z","acc":"Q07731","name":"Glial cell line-derived neurotrophic factor","length":211,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI000012B3A6","genes":[{"name":{"value":"Gdnf"}}],"alphafold_very_low_content":0.2132701421800948,"disorder_content":0.17061611374407584,"disprot_consensus":{"full":[{"start":78,"end":113,"type":"D"}],"Structural state":[{"start":78,"end":113,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00104","name":"Ligand-binding domain of nuclear hormone receptor","start":558,"end":735},{"id":"PF00105","name":"Double treble clef zinc finger, C4 type","start":420,"end":487},{"id":"PF02155","name":"Glucocorticoid receptor","start":26,"end":401}],"gene3D":[{"start":407,"end":500,"id":"3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A"},{"start":518,"end":777,"id":"1.10.565.10","name":"Retinoid X Receptor"}]},"uniref50":"UniRef50_P04150","sequence":"MDSKESLTPGREENPSSVLAQERGDVMDFYKTLRGGATVKVSASSPSLAVASQSDSKQRRLLVDFPKGSVSNAQQPDLSKAVSLSMGLYMGETETKVMGNDLGFPQQGQISLSSGETDLKLLEESIANLNRSTSVPENPKSSASTAVSAAPTEKEFPKTHSDVSSEQQHLKGQTGTNGGNVKLYTTDQSTFDILQDLEFSSGSPGKETNESPWRSDLLIDENCLLSPLAGEDDSFLLEGNSNEDCKPLILPDTKPKIKDNGDLVLSSPSNVTLPQVKTEKEDFIELCTPGVIKQEKLGTVYCQASFPGANIIGNKMSAISVHGVSTSGGQMYHYDMNTASLSQQQDQKPIFNVIPPIPVGSENWNRCQGSGDDNLTSLGTLNFPGRTVFSNGYSSPSMRPDVSSPPSSSSTATTGPPPKLCLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRKCLQAGMNLEARKTKKKIKGIQQATTGVSQETSENPGNKTIVPATLPQLTPTLVSLLEVIEPEVLYAGYDSSVPDSTWRIMTTLNMLGGRQVIAAVKWAKAIPGFRNLHLDDQMTLLQYSWMFLMAFALGWRSYRQSSANLLCFAPDLIINEQRMTLPCMYDQCKHMLYVSSELHRLQVSYEEYLCMKTLLLLSSVPKDGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTKLLDSMHEVVENLLNYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P04150","disprot_id":"DP00030","ncbi_taxon_id":9606,"regions_counter":22,"creator":"crodriguez","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":262,"region_id":"DP00030r001","released":"2023_06","ec_id":"ECO:0007691","reference_html":"Site-specific phosphorylation induces functionally active conformation in the intrinsically disordered N-terminal activation function (AF1) domain of the glucocorticoid receptor. <i> Garza AM, Khan SH, Kumar R. </i> Mol Cell Biol, 2010","term_id":"IDPO:0000002","curator_id":"vnugnes","start":77,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-01-12T16:11:42.182Z","reference_source":"pmid","term_name":"disorder","reference_id":"19841061","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"We further carried out partial proteolytic digestion experiments with three different proteases (trypsin, chymotrypsin, and Endo Gluc-C) to determine tertiary structural changes in AF1 with or without p38 MAPK-mediated phosphorylation. The results of one such partial proteolysis experiment are shown in Fig. ​3. ","type":"Results"},{"text":"Authors show in Fig. 3 that the peptide is susceptible to all the proteases digestion, indicating the lack of structure in this region.  ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:33:26.298Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":262,"region_id":"DP00030r005","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Site-specific phosphorylation induces functionally active conformation in the intrinsically disordered N-terminal activation function (AF1) domain of the glucocorticoid receptor. <i> Garza AM, Khan SH, Kumar R. </i> Mol Cell Biol, 2010","term_id":"IDPO:0000002","curator_id":"vnugnes","start":77,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-01-12T15:54:44.620Z","reference_source":"pmid","term_name":"disorder","reference_id":"19841061","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":" As expected, unphosphorylated AF1 shows characteristics of an ID protein, whereas phosphorylated AF1 adopts significantly higher secondary structural elements in it with helical content increased by >50% at the expense of random coil compared to unphosphorylated AF1 (Fig. 2A and Table ​1).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:33:28.056Z"}},{"start":181,"end":244,"reference_id":"28946939","reference_source":"pmid","reference_html":"An NMR study on the intrinsically disordered core transactivation domain of human glucocorticoid receptor. <i> Kim DH, Wright A, Han KH. </i> BMB Rep, 2017","date":"2022-04-25T21:22:13.615Z","curator_id":"kmuwonge","curator_name":"Kevin Muwonge","curator_orcid":"0000-0002-6149-7431","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP00030r009","statement":[{"text":"A large number of transcriptional activation domains (TADs) are intrinsically unstructured, meaning they are devoid of a three-dimensional structure. The fact that these TADs are transcriptionally active without forming a 3-D structure raises the question of what features in these domains enable them to function. One of two TADs in human glucocorticoid receptor (hGR) is located at its N-terminus and is responsible for ∼70% of the transcriptional activity of hGR. This 58-residue intrinsically-disordered TAD, named tau1c in an earlier study, was shown to form three helices under trifluoroethanol, which might be important for its activity.","type":"Abstract"},{"text":"hGR tau1c was one of the IDPs that was studied in the early days before the PreSMo concept was introduced. Since many transcription factors and TADs contain PreSMos, we wanted to learn whether tau1c also contains PreSMos.","type":"Introduction"},{"text":"Fig. 1 shows a fingerprint region of an 15N-1H heteronuclear single quantum coherence (HSQC) spectrum of hGR tau1c with resonance assignment. Based on the narrow chemical-shift dispersion in both 15N and 1H dimensions, we can confirm its overall unfolded/disordered nature in agreement with the bioinformatics prediction.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-13T14:01:18.588Z"}},{"start":209,"end":213,"reference_id":"19841061","reference_source":"pmid","reference_html":"Site-specific phosphorylation induces functionally active conformation in the intrinsically disordered N-terminal activation function (AF1) domain of the glucocorticoid receptor. <i> Garza AM, Khan SH, Kumar R. </i> Mol Cell Biol, 2010","date":"2023-01-12T16:58:12.173Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001202","ec_ontology":"ECO","ec_name":"in vitro protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00030r014","statement":[{"text":"Using GR S211-phospho site-specific antibody (Fig. ​1B) and MALDI-TOF MS (Fig. ​1C), we confirmed p38 MAPK-mediated in vitro phosphorylation of AF1.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:33:57.424Z"}},{"start":77,"end":262,"reference_id":"19841061","reference_source":"pmid","reference_html":"Site-specific phosphorylation induces functionally active conformation in the intrinsically disordered N-terminal activation function (AF1) domain of the glucocorticoid receptor. <i> Garza AM, Khan SH, Kumar R. </i> Mol Cell Biol, 2010","date":"2023-01-12T16:07:38.315Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00030r015","statement":[{"text":"Consistent with previous reports (11, 20, 21), in the case of unphosphorylated AF1, we detected a very weak interaction with each of these coregulatory proteins. These interactions were increased significantly when AF1 was phosphorylated, suggesting that phosphorylation of AF1 facilitates its interaction with all of the three coregulatory proteins tested (Fig. ​5, compare lanes 2 and 3).","type":"Results"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q92793","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P12931","operator":"or","partner_start":null,"partner_end":null}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:33:58.401Z"}},{"start":77,"end":262,"reference_id":"19841061","reference_source":"pmid","reference_html":"Site-specific phosphorylation induces functionally active conformation in the intrinsically disordered N-terminal activation function (AF1) domain of the glucocorticoid receptor. <i> Garza AM, Khan SH, Kumar R. </i> Mol Cell Biol, 2010","date":"2023-01-12T16:07:23.941Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0017025","term_name":"TBP-class protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P20226","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00030r016","statement":[{"text":"Consistent with previous reports (11, 20, 21), in the case of unphosphorylated AF1, we detected a very weak interaction with each of these coregulatory proteins. These interactions were increased significantly when AF1 was phosphorylated, suggesting that phosphorylation of AF1 facilitates its interaction with all of the three coregulatory proteins tested (Fig. ​5, compare lanes 2 and 3)","type":"Results"}],"term_comment":"","term_def":"\"Binding to a member of the class of TATA-binding proteins (TBP), including any of the TBP-related factors (TRFs).\" [GOC:jl, GOC:txnOH, http://www.mblab.gla.ac.uk/, PMID:16858867]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:34:03.167Z"}},{"start":1,"end":518,"reference_id":"34937942","reference_source":"pmid","reference_html":"Structure of Hsp90-Hsp70-Hop-GR reveals the Hsp90 client-loading mechanism. <i> Wang RY, Noddings CM, Kirschke E, Myasnikov AG, Johnson JL, Agard DA. </i> Nature, 2022","date":"2023-01-12T16:57:33.884Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7KW7"},{"db":"EMDB","id":"23050"}],"region_id":"DP00030r017","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P07900"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0DMV8"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P31948"}],"statement":[{"text":"a, GR (ribbon model) is partially unfolded, with the N-terminal residues simultaneously gripped by Hsp70CSBD-β and HopDP2, and is threaded through the semi-closed lumen of Hsp90.","type":"Figure"},{"text":"The Cryo-EM structure of the of Hsp90-Hsp70-Hop-GR complex, shows this region lacks electron density, indicating it is disordered. ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:33:33.077Z"}},{"start":1,"end":500,"reference_id":"19841061","reference_source":"pmid","reference_html":"Site-specific phosphorylation induces functionally active conformation in the intrinsically disordered N-terminal activation function (AF1) domain of the glucocorticoid receptor. <i> Garza AM, Khan SH, Kumar R. </i> Mol Cell Biol, 2010","date":"2023-01-13T13:42:23.299Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q92793","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P12931","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP00030r018","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"0229","entry_name":"CV-1.K"}],"statement":[{"text":"Further, we tested the FRET efficiency of GR500 interaction with each of the coregulators in a cotransfection assay. Our results show that GR500 interacts directly with TBP (Fig. ​6B), CBP (Fig. ​5C), and SRC-1 (Fig. ​6D) in the nuclei of GR-deficient CV-1 cells cotransfected with GR500 with or without each coregulator (compare lanes 2 and 3).","type":"Figure"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:34:04.510Z"}},{"start":1,"end":500,"reference_id":"19841061","reference_source":"pmid","reference_html":"Site-specific phosphorylation induces functionally active conformation in the intrinsically disordered N-terminal activation function (AF1) domain of the glucocorticoid receptor. <i> Garza AM, Khan SH, Kumar R. </i> Mol Cell Biol, 2010","date":"2023-01-13T13:42:36.718Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0017025","term_name":"TBP-class protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P20226","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00030r019","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0229","entry_name":"CV-1.K"}],"statement":[{"text":"Further, we tested the FRET efficiency of GR500 interaction with each of the coregulators in a cotransfection assay. Our results show that GR500 interacts directly with TBP (Fig. ​6B), CBP (Fig. ​5C), and SRC-1 (Fig. ​6D) in the nuclei of GR-deficient CV-1 cells cotransfected with GR500 with or without each coregulator (compare lanes 2 and 3).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a member of the class of TATA-binding proteins (TBP), including any of the TBP-related factors (TRFs).\" [GOC:jl, GOC:txnOH, http://www.mblab.gla.ac.uk/, PMID:16858867]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:34:05.710Z"}},{"start":275,"end":279,"reference_id":"12144530","reference_source":"pmid","reference_html":"Small ubiquitin-related modifier-1 (SUMO-1) modification of the glucocorticoid receptor. <i> Tian S, Poukka H, Palvimo JJ, Jänne OA. </i> Biochem J, 2002","date":"2024-05-08T14:43:35.793Z","curator_id":"crodriguez","curator_name":"Cecilia Rodriguez","curator_orcid":"0009-0003-7046-9269","term_id":"IDPO:0000037","term_name":"molecular recognition display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IMP","region_id":"DP00030r021","statement":[{"text":"Immunoprecipitation of recipient COS-1 cell extracts revealed that K277R and K293R are poorly sumoylated in comparison with wild-type GR (Figures 1A and 1B, lanes 7–8 and 9–10).","type":"Results"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of the addition of SUMO groups to a protein.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys277Arg","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"\"To verify whether these residues are in vivo acceptors of SUMO-1, point mutations K277R, K293R and K703R were introduced into the Flag-tagged hGR.\""}]},{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0223","entry_name":"CV-1 in Origin Simian-1"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-08T14:53:11.089Z"}},{"start":291,"end":295,"reference_id":"12144530","reference_source":"pmid","reference_html":"Small ubiquitin-related modifier-1 (SUMO-1) modification of the glucocorticoid receptor. <i> Tian S, Poukka H, Palvimo JJ, Jänne OA. </i> Biochem J, 2002","date":"2024-05-08T14:43:19.973Z","curator_id":"crodriguez","curator_name":"Cecilia Rodriguez","curator_orcid":"0009-0003-7046-9269","term_id":"IDPO:0000037","term_name":"molecular recognition display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IMP","region_id":"DP00030r022","statement":[{"text":"Immunoprecipitation of recipient COS-1 cell extracts revealed that K277R and K293R are poorly sumoylated in comparison with wild-type GR (Figures 1A and 1B, lanes 7–8 and 9–10).","type":"Results"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of the addition of SUMO groups to a protein.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys293Arg","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To verify whether these residues are in vivo acceptors of SUMO-1, point mutations K277R, K293R and K703R were introduced into the Flag-tagged hGR."}]},{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0223","entry_name":"CV-1 in Origin Simian-1"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-08T14:53:13.284Z"}}],"released":"2016_10","uniref100":"UniRef100_P04150","date":"2016-08-11T13:42:15.000Z","acc":"P04150","name":"Glucocorticoid receptor","length":777,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI000012B301","genes":[{"name":{"value":"NR3C1"},"synonyms":[{"value":"GRL"}]}],"alphafold_very_low_content":0.5572715572715573,"disorder_content":0.6666666666666666,"disprot_consensus":{"full":[{"start":1,"end":518,"type":"D"}],"Structural state":[{"start":1,"end":518,"type":"D"}],"Disorder function":[{"start":209,"end":213,"type":"F"},{"start":275,"end":279,"type":"F"},{"start":291,"end":295,"type":"F"}],"Molecular function":[{"start":1,"end":500,"type":"F"}]}},{"features":{"pfam":[{"id":"PF13649","name":"Methyltransferase domain","start":61,"end":169}],"gene3D":[{"start":20,"end":244,"id":"3.30.46.10","name":"Glycine N-methyltransferase, chain A, domain 1"},{"start":35,"end":291,"id":"3.40.50.150","name":"Vaccinia Virus protein VP39"}]},"uniref50":"UniRef50_P13255","sequence":"MVDSVYRTRSLGVAAEGIPDQYADGEAARVWQLYIGDTRSRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYALKERWNRRKEPAFDKWVIEEANWLTLDKDVPAGDGFDAVICLGNSFAHLPDSKGDQSEHRLALKNIASMVRPGGLLVIDHRNYDYILSTGCAPPGKNIYYKSDLTKDITTSVLTVNNKAHMVTLDYTVQVPGAGRDGAPGFSKFRLSYYPHCLASFTELVQEAFGGRCQHSVLGDFKPYRPGQAYVPCYFIHVLKKTG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_P13255","disprot_id":"DP00031","ncbi_taxon_id":10116,"regions_counter":12,"creator":"agasparini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":18,"region_id":"DP00031r006","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Catalytic mechanism of glycine N-methyltransferase. <i> Takata Y, Huang Y, Komoto J, Yamada T, Konishi K, Ogawa H, Gomi T, Fujioka M, Takusagawa F. </i> Biochemistry, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12859184","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-08-16T20:32:30.420Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1NBI"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"67040","entry_name":"S-adenosyl-L-methioninate"}],"statement":[{"text":"The model of amino acid residues 18−44 was built in (2Fo − Fc) maps. (Fo − Fc) maps did not give any significant electron density for amino acid residues 1−17, indicating that these residues were heavily disordered.","type":"Methods"},{"text":"Authors are not considering the first Met residue, therefore the disordered region they are referring to is 1-18.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:10:10.483Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":41,"region_id":"DP00031r008","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Mechanisms for auto-inhibition and forced product release in glycine N-methyltransferase: crystal structures of wild-type, mutant R175K and S-adenosylhomocysteine-bound R175K enzymes. <i> Huang Y, Komoto J, Konishi K, Takata Y, Ogawa H, Gomi T, Fujioka M, Takusagawa F. </i> J Mol Biol, 2000","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10756111","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-08-16T20:32:57.564Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1D2H"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg176Lys","start":null,"end":null,"position":null}],"curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16680","entry_name":"S-adenosyl-L-homocysteine"}],"sequence_construct":"VDSVYRTRSLGVAAEGIPDQYADGEAARVWQLYIGDTRSRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYALKERWNRRKEPAFDKWVIEEANWLTLDKDVPAGDGFDAVICLGNSFAHLPDSKGDQSEHRLALKNIASMVRPGGLLVIDHKNYDYILSTGCAPPGKNIYYKSDLTKDITTSVLTVNNKAHMVTLDYTVQVPGAGRDGAPGFSKFRLSYYPHCLASFTELVQEAFGGRCQHSVLGDFKPYRPGQAYVPCYFIHVLKKTG","statement":[{"text":"The crystal structure was refined by the standard refinement procedure in the X-PLOR protocol. A (2Fo−Fc) map computed after a refinement showed no significant electron density for the amino acid residues 1 to 40, indicating that these residues were heavily disordered.","type":"Methods"},{"text":"Authors are not considering the first Met residue, therefore the disordered region they are referring to is 1-41.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:10:11.395Z"}},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":41,"term_name":"self-inhibition","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"vnugnes","released":"2022_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10756111","version":4,"reference_html":"Mechanisms for auto-inhibition and forced product release in glycine N-methyltransferase: crystal structures of wild-type, mutant R175K and S-adenosylhomocysteine-bound R175K enzymes. <i> Huang Y, Komoto J, Konishi K, Takata Y, Ogawa H, Gomi T, Fujioka M, Takusagawa F. </i> J Mol Biol, 2000","date":"2022-08-16T20:21:28.196Z","term_id":"IDPO:0000059","ec_id":"ECO:0006220","region_id":"DP00031r009","ec_go":"EXP","disprot_namespace":"Disorder function","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"By comparing the open structure to the closed structure, mechanisms for auto-inhibition and for the forced release of the product AdoHcy have been revealed in the GNMT structure. The N-terminal section of the adjacent subunit occupies the AdoMet binding site and thus inhibits the methyltransfer reaction, whereas the same N-terminal section forces the departure of the potentially potent inhibitor AdoHcy from the active site and thus facilitates the methyltransfer reaction. Consequently GNMT is less active at a low level of AdoMet concentration, and is only weakly inhibited by AdoHcy.","type":"Abstract"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:10:19.225Z"}},{"start":1,"end":41,"reference_id":"10756111","reference_source":"pmid","reference_html":"Mechanisms for auto-inhibition and forced product release in glycine N-methyltransferase: crystal structures of wild-type, mutant R175K and S-adenosylhomocysteine-bound R175K enzymes. <i> Huang Y, Komoto J, Konishi K, Takata Y, Ogawa H, Gomi T, Fujioka M, Takusagawa F. </i> J Mol Biol, 2000","date":"2022-08-16T20:33:20.528Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"1D2C"},{"db":"PDB","id":"1D2H"}],"region_id":"DP00031r012","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16680","entry_name":"S-adenosyl-L-homocysteine"}],"statement":[{"text":"The binding of AdoMet to the active site of subunit B enhances the movement of the N-terminal domain (residues 1-40) of subunit B.","type":"Discussion"},{"text":"This Arg175 modification study indicates that the binding of AdoMet opens the entrance of the active site and acetate binds to Arg175. Indeed, in the AdoHcy-R175K structure, the active site entrance is opened widely by binding the AdoHcy.","type":"Results"},{"text":"Authors are not considering the first Met residue, therefore the disordered region they are referring to is 1-41.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:10:15.439Z"}}],"released":"2016_10","uniref100":"UniRef100_P13255","date":"2016-08-23T16:37:21.000Z","acc":"P13255","name":"Glycine N-methyltransferase","length":293,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI00001108E8","genes":[{"name":{"value":"Gnmt"},"synonyms":[{"value":"Fbp-cII","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"6587377","url":"http://www.ncbi.nlm.nih.gov/pubmed/6587377","alternativeUrl":"https://europepmc.org/abstract/MED/6587377"}}]}]}],"alphafold_very_low_content":0.05460750853242321,"disorder_content":0.13993174061433447,"disprot_consensus":{"full":[{"start":1,"end":41,"type":"T"}],"Structural state":[{"start":1,"end":41,"type":"D"}],"Disorder function":[{"start":1,"end":41,"type":"F"}],"Structural transition":[{"start":1,"end":41,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00587","name":"tRNA synthetase class II core domain (G, H, P, S and T)","start":182,"end":374},{"id":"PF03129","name":"Anticodon binding domain","start":401,"end":503}],"gene3D":[{"start":394,"end":505,"id":"3.40.50.800","name":"Anticodon-binding domain"}]},"uniref50":"UniRef50_P56206","sequence":"MPASSLDELVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLKQAWWRRNVYERDDMEGLDASVLTHRLVLHYSGHEATFADPMVDNRITKKRYRLDHLLKEQPEEVLKRLYRAMEVEEENLHALVQAMMQAPERAGGAMTAAGVLDPASGEPGDWTPPRYFNMMFKTYVGPVEDEASLAYLRPETAQGIFVNFKNVLDATSRKLPFGIAQIGKAFRNEITPRNFIFRVREFEQMEIEYFVRPGEDEYWHRYWVEERLKWWQEMGLSRENLVPYQQPPEELAHYAKATVDILYRFPHGLEELEGIANRTDFDLGSHTKDQEALGITARVLRNEHSTQRLAYRDPETGKWFVPYVIEPSAGVDRGVLALLAEAFTREELPNGEERIVLKLKPQLAPIKVAVIPLVKNRPEITEYAKRLKARLLALGLGRVLYEDTGNIGKAYRRHDEVGTPFAVTVDYDTIGQSKDGTTRLKDTVTVRDRDTMEQIRLHVDELEGFLRERLRW","taxonomy":["Bacteria","Deinococcus-Thermus","Deinococci","Thermales","Thermaceae","Thermus"],"uniref90":"UniRef90_P56206","disprot_id":"DP00032","ncbi_taxon_id":300852,"regions_counter":2,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":170,"region_id":"DP00032r001","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus. <i> Logan DT, Mazauric MH, Kern D, Moras D. </i> EMBO J, 1995","term_id":"IDPO:0000002","curator_id":"vnugnes","start":85,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"7556056","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-09-06T12:55:50.600Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"1ATI"}],"statement":[{"text":"Our model for the insertion domain is at present incomplete due to crystalline disorder, but it contains conserved residues likely to interact with the acceptor arm of tRNAGlY.","type":"Results"},{"text":"However, electron density between residues 85 and 170 is weak and it has been possible to build only 50 of the intervening 85 residues in one monomer and 45 in the other, in most cases with Ala side chains only.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:09:54.120Z"}}],"released":"2016_10","uniref100":"UniRef100_P56206","date":"2016-08-23T16:44:04.000Z","acc":"P56206","name":"Glycine--tRNA ligase","length":506,"organism":"Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","dataset":[],"UniParc":"UPI0000110644","genes":[{"name":{"value":"glyQS"},"synonyms":[{"value":"glyS","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9490048","url":"http://www.ncbi.nlm.nih.gov/pubmed/9490048","alternativeUrl":"https://europepmc.org/abstract/MED/9490048"}}]}],"olnNames":[{"value":"TTHA0543"}]}],"alphafold_very_low_content":0,"disorder_content":0.16996047430830039,"disprot_consensus":{"full":[{"start":85,"end":170,"type":"D"}],"Structural state":[{"start":85,"end":170,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00041","name":"Fibronectin type III domain","start":170,"end":249},{"id":"PF09067","name":"Erythropoietin receptor, ligand binding","start":47,"end":134},{"id":"PF12772","name":"Growth hormone receptor binding","start":316,"end":617}],"gene3D":[{"start":50,"end":149,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":150,"end":250,"id":"2.60.40.10","name":"Immunoglobulins"}]},"uniref50":"UniRef50_P10912","sequence":"MDLWQLLLTLALAGSSDAFSGSEATAAILSRAPWSLQSVNPGLKTNSSKEPKFTKCRSPERETFSCHWTDEVHHGTKNLGPIQLFYTRRNTQEWTQEWKECPDYVSAGENSCYFNSSFTSIWIPYCIKLTSNGGTVDEKCFSVDEIVQPDPPIALNWTLLNVSLTGIHADIQVRWEAPRNADIQKGWMVLEYELQYKEVNETKWKMMDPILTTSVPVYSLKVDKEYEVRVRSKQRNSGNYGEFSEVLYVTLPQMSQFTCEEDFYFPWLLIIIFGIFGLTVMLFVFLFSKQQRIKMLILPPVPVPKIKGIDPDLLKEGKLEEVNTILAIHDSYKPEFHSDDSWVEFIELDIDEPDEKTEESDTDRLLSSDHEKSHSNLGVKDGDSGRTSCCEPDILETDFNANDIHEGTSEVAQPQRLKGEADLLCLDQKNQNNSPYHDACPATQQPSVIQAEKNKPQPLPTEGAESTHQAAHIQLSNPSSLSNIDFYAQVSDITPAGSVVLSPGQKNKAGMSQCDMHPEMVSLCQENFLMDNAYFCEADAKKCIPVAPHIKVESHIQPSLNQEDIYITTESLTTAAGRPGTGEHVPGSEMPVPDYTSIHIVQSPQGLILNATALPLPDKEFLSSCGYVSTDQLNKIMP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P10912","disprot_id":"DP00033","ncbi_taxon_id":9606,"regions_counter":11,"creator":"rhornyak","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":370,"region_id":"DP00033r001","released":"2022_12","ec_id":"ECO:0006204","reference_html":"Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes. <i> Haxholm GW, Nikolajsen LF, Olsen JG, Fredsted J, Larsen FH, Goffin V, Pedersen SF, Brooks AJ, Waters MJ, Kragelund BB. </i> Biochem J, 2015","term_id":"IDPO:0000002","curator_id":"vnugnes","start":270,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"25846210","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-09-06T14:28:46.489Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Analogously to the PRLR-ICD, two overlapping subdomains were constructed; GHR-ICDmp (Ser270-Ser370) and GHR-ICDmd (Val361–Pro620; Figure 1B). Far-UV CD and NMR spectroscopic analyses confirmed that both subdomains were intrinsically disordered with a low content of secondary structure (Supplementary Figures S5A–S5D) and no significant longrange intramolecular interactions as assessed by cross-titrations (Supplementary Figure S5E).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:09:31.708Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":370,"region_id":"DP00033r005","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes. <i> Haxholm GW, Nikolajsen LF, Olsen JG, Fredsted J, Larsen FH, Goffin V, Pedersen SF, Brooks AJ, Waters MJ, Kragelund BB. </i> Biochem J, 2015","term_id":"IDPO:0000002","curator_id":"vnugnes","start":270,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"25846210","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-09-06T14:28:58.987Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Analogously to the PRLR-ICD, two overlapping subdomains were constructed; GHR-ICDmp (Ser270-Ser370) and GHR-ICDmd (Val361–Pro620; Figure 1B). Far-UV CD and NMR spectroscopic analyses confirmed that both subdomains were intrinsically disordered with a low content of secondary structure (Supplementary Figures S5A–S5D) and no significant longrange intramolecular interactions as assessed by cross-titrations (Supplementary Figure S5E).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:09:33.026Z"}},{"start":361,"end":620,"reference_id":"25846210","reference_source":"pmid","reference_html":"Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes. <i> Haxholm GW, Nikolajsen LF, Olsen JG, Fredsted J, Larsen FH, Goffin V, Pedersen SF, Brooks AJ, Waters MJ, Kragelund BB. </i> Biochem J, 2015","date":"2022-09-06T14:29:46.380Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00033r009","statement":[{"text":"Analogously to the PRLR-ICD, two overlapping subdomains were constructed; GHR-ICDmp (Ser270-Ser370) and GHR-ICDmd (Val361–Pro620; Figure 1B). Far-UV CD and NMR spectroscopic analyses confirmed that both subdomains were intrinsically disordered with a low content of secondary structure (Supplementary Figures S5A–S5D) and no significant longrange intramolecular interactions as assessed by cross-titrations (Supplementary Figure S5E).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:09:35.737Z"}},{"start":361,"end":620,"reference_id":"25846210","reference_source":"pmid","reference_html":"Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes. <i> Haxholm GW, Nikolajsen LF, Olsen JG, Fredsted J, Larsen FH, Goffin V, Pedersen SF, Brooks AJ, Waters MJ, Kragelund BB. </i> Biochem J, 2015","date":"2022-09-06T14:29:55.956Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00033r010","statement":[{"text":"Analogously to the PRLR-ICD, two overlapping subdomains were constructed; GHR-ICDmp (Ser270-Ser370) and GHR-ICDmd (Val361–Pro620; Figure 1B). Far-UV CD and NMR spectroscopic analyses confirmed that both subdomains were intrinsically disordered with a low content of secondary structure (Supplementary Figures S5A–S5D) and no significant longrange intramolecular interactions as assessed by cross-titrations (Supplementary Figure S5E).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:09:38.401Z"}},{"start":270,"end":357,"reference_id":"25846210","reference_source":"pmid","reference_html":"Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes. <i> Haxholm GW, Nikolajsen LF, Olsen JG, Fredsted J, Larsen FH, Goffin V, Pedersen SF, Brooks AJ, Waters MJ, Kragelund BB. </i> Biochem J, 2015","date":"2022-09-06T14:34:45.206Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"74909","operator":null,"partner_start":null,"partner_end":null},{"db":"ChEBI","id":"73001","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP00033r011","statement":[{"text":"We subsequently followed the same strategy as for the PRLR-ICD and chemical shift differences from 1 H-15N-HSQC spectra confirmed POPS specificity for GHRICDmp (Figures 3B and 3C). Pronounced chemical shift changes were observed in the membrane-proximal region of GHR-ICDmp upon POPC/POPS SUV binding (Lys287–Ser357) and signals from many of the N-terminal residues (Ser270–Lys287) disappeared, thereby identifying a LID1 comprising residues Ser270–Ser357 (Figure 3C). Again, to rule out artifacts from truncations, the lipid interaction was confirmed using full-length non-tagged GHRICD (GHR-ICDFL).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:09:41.416Z"}}],"released":"2016_10","uniref100":"UniRef100_P10912","date":"2016-09-23T14:39:24.000Z","acc":"P10912","name":"Growth hormone receptor","length":638,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012B416","genes":[{"name":{"value":"GHR"}}],"alphafold_very_low_content":0.512539184952978,"disorder_content":0.5501567398119123,"disprot_consensus":{"full":[{"start":270,"end":620,"type":"D"}],"Structural state":[{"start":270,"end":620,"type":"D"}],"Molecular function":[{"start":270,"end":357,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05357","name":"Phage Coat Protein A","start":1,"end":65},{"id":"PF05357","name":"Phage Coat Protein A","start":104,"end":176}],"gene3D":[{"start":125,"end":223,"id":"3.90.450.1","name":"Minor Coat Protein; Domain 2"},{"start":18,"end":124,"id":"2.30.27.10","name":"Phage FD Coat Protein,Membrane penetration domain"}]},"uniref50":"UniRef50_P03661","sequence":"MKKLLFAIPLVVPFYSHSAETVESCLAKPHTENSFTNVWKDDKTLDRYANYEGCLWNATGVVVCTGDETQCYGTWVPIGLAIPENEGGGSEGGGSEGGGSEGGGTKPPEYGDTPIPGYTYINPLDGTYPPGTEQNPANPNPSLEESQPLNTFMFQNNRFRNRQGALTVYTGTVTQGTDPVKTYYQYTPVSSKAMYDAYWNGKFRDCAFHSGFNEDPFVCEYQGQSSDLPQPPVNAGGGSGGGSGGGSEGGGSEGGGSEGGGSEGGGSGGGSGSGDFDYEKMANANKGAMTENADENALQSDAKGKLDSVATDYGAAIDGFIGDVSGLANGNGATGDFAGSNSQMAQVGDGDNSPLMNNFRQYLPSLPQSVECRPYVFGAGKPYEFSIDCDKINLFRGVFAFLLYVATFMYVFSTFANILRNKES","taxonomy":["Viruses","Monodnaviria","Loebvirae","Hofneiviricota","Faserviricetes","Tubulavirales","Inoviridae","Inovirus","unclassified Inovirus"],"uniref90":"UniRef90_P03661","disprot_id":"DP00034","ncbi_taxon_id":10864,"regions_counter":4,"creator":"fquaglia","regions":[{"start":86,"end":107,"reference_id":"10329170","reference_source":"pmid","reference_html":"Crystal structure of the two N-terminal domains of g3p from filamentous phage fd at 1.9 A: evidence for conformational lability. <i> Holliger P, Riechmann L, Williams RL. </i> J Mol Biol, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2G3P"}],"region_id":"DP00034r003","statement":[{"text":"In contrast, the Gly-rich linker segment from residue G69-T87 as well as adjacent residues N67-E68 and K88-P90 are not visible in either molecule A or B (Figure 1a).","type":"Results"},{"text":"The Gly-rich linker connecting D1 to D2 is not visible in the electron density map (see above).","type":"Results"},{"text":"The IDR characterized in the publication corresponds to region 86-107 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-18) that is cleaved in the mature secreted protein.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-09T07:12:30.525Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":86,"end":107,"reference_id":"10329170","reference_source":"pmid","reference_html":"Crystal structure of the two N-terminal domains of g3p from filamentous phage fd at 1.9 A: evidence for conformational lability. <i> Holliger P, Riechmann L, Williams RL. </i> J Mol Biol, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"2G3P"}],"region_id":"DP00034r004","statement":[{"text":"In contrast, the Gly-rich linker segment from residue G69-T87 as well as adjacent residues N67-E68 and K88-P90 are not visible in either molecule A or B (Figure 1a).","type":"Results"},{"text":"The Gly-rich linker connecting D1 to D2 is not visible in the electron density map (see above).","type":"Results"},{"text":"The IDR characterized in the publication corresponds to region 86-107 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-18) that is cleaved in the mature secreted protein.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-09T07:13:23.861Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_P03661","date":"2016-08-11T10:52:26.000Z","acc":"P03661","name":"Attachment protein G3P","length":424,"organism":"Enterobacteria phage fd","dataset":["Viral proteins"],"UniParc":"UPI000011F60D","genes":[{"name":{"value":"III"}}],"disorder_content":0.05188679245283019,"disprot_consensus":{"full":[{"start":86,"end":107,"type":"D"}],"Structural state":[{"start":86,"end":107,"type":"D"}],"Disorder function":[{"start":86,"end":107,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00447","name":"HSF-type DNA-binding","start":197,"end":297}],"gene3D":[{"start":189,"end":299,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}]},"uniref50":"UniRef50_P22121","sequence":"MGHNDSVETMDEISNPNNILLPHDGTGLDATGISGSQEPYGMVDVLNPDSLKDDSNVDEPLIEDIVNPSLDPEGVVSAEPSNEVGTPLLQQPISLDHVITRPASAGGVYSIGNSSTSSAAKLSDGDLTNATDPLLNNAHGHGQPSSESQSHSNGYHKQGQSQQPLLSLNKRKLLAKAHVDKHHSKKKLSTTRARPAFVNKLWSMVNDKSNEKFIHWSTSGESIVVPNRERFVQEVLPKYFKHSNFASFVRQLNMYGWHKVQDVKSGSMLSNNDSRWEFENENFKRGKEYLLENIVRQKSNTNILGGTTNAEVDIHILLNELETVKYNQLAIAEDLKRITKDNEMLWKENMMARERHQSQQQVLEKLLRFLSSVFGPNSAKTIGNGFQPDLIHELSDMQVNHMSNNNHNNTGNINPNAYHNETDDPMANVFGPLTPTDQGKVPLQDYKLRPRLLLKNRSMSSSSSSNLNQRQSPQNRIVGQSPPPQQQQQQQQQQGQPQGQQFSYPIQGGNQMMNQLGSPIGTQVGSPVGSQYGNQYGNQYSNQFGNQLQQQTSRPALHHGSNGEIRELTPSIVSSDSPDPAFFQDLQNNIDKQEESIQEIQDWITKLNPGPGEDGNTPIFPELNMPSYFANTGGSGQSEQPSDYGDSQIEELRNSRLHEPDRSFEEKNNGQKRRRAA","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Kluyveromyces"],"uniref90":"UniRef90_P22121","disprot_id":"DP00036","ncbi_taxon_id":284590,"regions_counter":4,"creator":"dpiovesan","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":273,"region_id":"DP00036r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of the DNA-binding domain of the heat shock transcription factor determined by multidimensional heteronuclear magnetic resonance spectroscopy. <i> Damberger FF, Pelton JG, Harrison CJ, Nelson HC, Wemmer DE. </i> Protein Sci, 1994","term_id":"IDPO:0000002","curator_id":"fquaglia","start":260,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"7849597","statement":[{"text":"Unstructured region inside the DNA-binding domain of HSF from K. lactis. The region has been identified from Fig.4, where secondary structure deduced from the NOESY data is indicated below the NOE data. ","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-07T15:41:49.095Z"}},{"start":1,"end":195,"reference_id":"8745404","reference_source":"pmid","reference_html":"Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy. <i> Cho HS, Liu CW, Damberger FF, Pelton JG, Nelson HC, Wemmer DE. </i> Protein Sci, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00036r002","statement":[{"text":"Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy.","type":"Title"},{"text":"The remaining peaks in Figure 2B, all negative in intensity, can be attributed to the N-terminal activation domain. These additional peaks have poor shift dispersion in the proton dimension, as is the case for unstructured proteins. Integrating the volumes of the signals in the spectra could account for approximately 183 of the possible 192 residues; however, only 103 peaks were sufficiently resolved to calculate NOES. These NOE values (Fig. 4) are sorted by proton chemical shift because there are no sequence-specific assignments currently available for this domain. Negative values indicate that all of the residues in this region exhibit a high degree of rapid internal motion, typical for an unstructured protein. ","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-07T15:41:31.455Z"}},{"start":1,"end":195,"reference_id":"8745404","reference_source":"pmid","reference_html":"Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy. <i> Cho HS, Liu CW, Damberger FF, Pelton JG, Nelson HC, Wemmer DE. </i> Protein Sci, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00036r003","statement":[{"text":"Far-UV CD spectroscopy, performed at pH 7.0, also indicate that the N-terminal activation domains of yeast HSF are unstructured. Figure 5A shows CD spectra for the DNA-binding domain, and for the N-terminal activation domain plus the DNA-binding domain, as well as the difference between the two. The difference spectrum is characteristic of a random coil. We also examined the possibility that the N-terminal activation do- main might behave differently when the DNA-binding domain is bound to a DNA-binding site (Fig. 5B). An examination of this CD difference spectrum indicates that binding of the DNA- binding domain to the DNA does not induce any structural changes in the N-terminal activation domain. Identical results were obtained for the K. lactis constructs (not shown).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-07T14:58:11.464Z"}},{"start":1,"end":195,"reference_id":"8745404","reference_source":"pmid","reference_html":"Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy. <i> Cho HS, Liu CW, Damberger FF, Pelton JG, Nelson HC, Wemmer DE. </i> Protein Sci, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140677","term_name":"molecular function activator activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","released":"2022_03","version":3,"region_id":"DP00036r004","statement":[{"text":"Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy.","type":"Title"},{"text":"Using the DNA-binding domain as a structural reference, we show that the protein backbone of the N-terminal activation domain undergoes rapid, large-amplitude motions and is therefore unstructured. Difference CD data also show that the N-terminal activation domain remains random-coil, even in the presence of DNA.","type":"Abstract"},{"text":"In addition, we used two-dimensional heteronuclear 15N{1H} NOE NMR and measurements of 15N relaxation parameters to show that the N-terminal activation domains from both yeast strains have a high degree of flexibility, which is consistent with an unstructured state in solution. The results are particularly compelling because they offer the first positive evidence for a dynamically disordered transcriptional activation domain.","type":"Introduction"}],"term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-07T15:42:31.608Z"}}],"released":"2016_10","uniref100":"UniRef100_P22121","date":"2016-08-11T18:52:14.000Z","acc":"P22121","name":"Heat shock factor protein","length":677,"organism":"Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)","dataset":["Stress response proteins"],"UniParc":"UPI000012CCF2","genes":[{"name":{"value":"HSF","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"1899375","url":"http://www.ncbi.nlm.nih.gov/pubmed/1899375","alternativeUrl":"https://europepmc.org/abstract/MED/1899375"}}]},"olnNames":[{"value":"KLLA0D03322g"}]}],"alphafold_very_low_content":0.6691285081240768,"disorder_content":0.3087149187592319,"disprot_consensus":{"full":[{"start":1,"end":195,"type":"D"},{"start":260,"end":273,"type":"D"}],"Structural state":[{"start":1,"end":195,"type":"D"},{"start":260,"end":273,"type":"D"}],"Molecular function":[{"start":1,"end":195,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_P17096","sequence":"MSESSSKSSQPLASKQEKDGTEKRGRGRPRKQPPVSPGTALVGSQKEPSEVPTPKRPRGRPKGSKNKGAAKTRKTTTTPGRKPRGRPKKLEKEEEEGISQESSEEEQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P17096","disprot_id":"DP00040","ncbi_taxon_id":9606,"regions_counter":42,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":107,"region_id":"DP00040r003","reference_id":"9253416","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In the absence of DNA, the NMR spectrum of HMG-1(2/3) is indicative of a random coil. Upon binding, the two DBDs that contact the DNA become ordered and adopt a well defined conformation in the minor groove.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"reference_html":"The solution structure of an HMG-I(Y)-DNA complex defines a new architectural minor groove binding motif. <i> Huth JR, Bewley CA, Nissen MS, Evans JN, Reeves R, Gronenborn AM, Clore GM. </i> Nat Struct Biol, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","validated":{"curator_id":"bmesza","timestamp":"2020-11-26T12:57:56.148Z","curator_name":"Bálint Mészáros"},"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00040r004","ec_ontology":"ECO","end":75,"term_id":"GO:0003677","start":51,"version":5,"statement":[{"text":"In the absence of DNA, the NMR spectrum of HMG-1(2/3) is indicative of a random coil. Upon binding, the two DBDs that contact the DNA become ordered and adopt a well defined conformation in the minor groove.","type":"Article"},{"text":"The stoichiometry of binding was established by a series of titra-tion experiments using 15N/13C[Gly 11 ]-HMG-1(2/3) and 15N/13C-[Gly 37]-HMG-1(2/3) in which a single glycine in DBD2 and DBD3 respectively was isotopically labelled (Fig. 2a). HMG-1(2/3) binds to the PRDII dodecamer with DBD2 on the slow side of intermediate exchange; at ratios of DNA to protein less than 1:1, the cross-peak of Gly 11 in the 1H-15N correlation spectrum is broadened out (note this may also be due to non-specific interactions resulting in the formation of higher order structures since some precipitation is observed at ratios of DNA to protein below 1: 1 which completely dears up upon further addition of DNA); at a 1: 1 ratio the cross peak is located at the position of the bound form and does not shift upon further addition of DNA, although it does sharpen up slightly. ","type":"Article"},{"text":"The DNA in the DBD2 and DBD3 complexes is essentially B-type (Figs 4, 5).","type":"Article"},{"text":"DNA-binding motifs DBD2 of HMGA1","type":"Curator statement"}],"term_name":"DNA binding","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0001-8399-7907","released":"2022_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"9253416","date":"2022-06-14T17:32:45.077Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2EZD"},{"db":"PDB","id":"2EZE"}],"term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"vnugnes","reference_html":"The solution structure of an HMG-I(Y)-DNA complex defines a new architectural minor groove binding motif. <i> Huth JR, Bewley CA, Nissen MS, Evans JN, Reeves R, Gronenborn AM, Clore GM. </i> Nat Struct Biol, 1997","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting DNA 5'-GGGAAATTCCTC, corresponds to the PRDII element of the IFN-β promoter sequence."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-15T07:35:27.605Z"}},{"region_id":"DP00040r005","ec_ontology":"ECO","end":75,"term_id":"IDPO:0000011","start":51,"version":4,"statement":[{"text":"In the absence of DNA, the NMR spectrum of HMG-1(2/3) is indicative of a random coil. Upon binding, the two DBDs that contact the DNA become ordered and adopt a well defined conformation in the minor groove.","type":"Article"},{"text":"The stoichiometry of binding was established by a series of titra-tion experiments using 15N/13C[Gly 11 ]-HMG-1(2/3) and 15N/13C-[Gly 37]-HMG-1(2/3) in which a single glycine in DBD2 and DBD3 respectively was isotopically labelled (Fig. 2a). HMG-1(2/3) binds to the PRDII dodecamer with DBD2 on the slow side of intermediate exchange; at ratios of DNA to protein less than 1:1, the cross-peak of Gly 11 in the 1H-15N correlation spectrum is broadened out (note this may also be due to non-specific interactions resulting in the formation of higher order structures since some precipitation is observed at ratios of DNA to protein below 1: 1 which completely dears up upon further addition of DNA); at a 1: 1 ratio the cross peak is located at the position of the bound form and does not shift upon further addition of DNA, although it does sharpen up slightly. ","type":"Article"},{"text":"The DNA in the DBD2 and DBD3 complexes is essentially B-type (Figs 4, 5).","type":"Article"},{"text":"DNA-binding motifs DBD2 of HMGA1","type":"Curator statement"}],"term_name":"disorder to order","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0001-8399-7907","released":"2022_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"9253416","date":"2022-06-14T17:35:19.102Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2EZD"},{"db":"PDB","id":"2EZE"}],"term_namespace":"Structural transition","ec_id":"ECO:0006165","curator_id":"vnugnes","reference_html":"The solution structure of an HMG-I(Y)-DNA complex defines a new architectural minor groove binding motif. <i> Huth JR, Bewley CA, Nissen MS, Evans JN, Reeves R, Gronenborn AM, Clore GM. </i> Nat Struct Biol, 1997","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting DNA 5'-GGGAAATTCCTC, corresponds to the PRDII element of the IFN-β promoter sequence."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-15T07:35:01.192Z"}},{"region_id":"DP00040r006","ec_ontology":"ECO","end":89,"term_id":"IDPO:0000011","start":80,"version":4,"statement":[{"text":"In the absence of DNA, the NMR spectrum of HMG-1(2/3) is indicative of a random coil. Upon binding, the two DBDs that contact the DNA become ordered and adopt a well defined conformation in the minor groove.","type":"Article"},{"text":"In contrast, Gly 37 of DBD3 is in fast exchange and its cross peak in the 1H-15N correlation spectrum only begins to shift from its position in the free state at ratios of DNA to protein greater than about 0.8:1, reaching the position of the bound form at a ratio of2:l. Thus, under our experimental conditions, one molecule ofHMG-1(2/3) binds two molecules of the PRDII dodecamer, the equilibrium association constant for the interaction of DBD3 with the PRDII dodecamer is -1.0(±0.5)xl05 M-1, and the affinity of DBD2 for the PRDII dodecamer is about one to two orders of magnitude greater than that ofDBD3.","type":"Article"},{"text":"The DNA in the DBD2 and DBD3 complexes is essentially B-type (Figs 4, 5).","type":"Article"},{"text":"DNA-binding motifs DBD3 of HMGA1","type":"Curator statement"}],"term_name":"disorder to order","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0001-8399-7907","released":"2022_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"9253416","date":"2022-06-14T17:35:47.011Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2EZG"},{"db":"PDB","id":"2EZF"}],"term_namespace":"Structural transition","ec_id":"ECO:0006165","curator_id":"vnugnes","reference_html":"The solution structure of an HMG-I(Y)-DNA complex defines a new architectural minor groove binding motif. <i> Huth JR, Bewley CA, Nissen MS, Evans JN, Reeves R, Gronenborn AM, Clore GM. </i> Nat Struct Biol, 1997","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting DNA 5'-GGGAAATTCCTC, corresponds to the PRDII element of the IFN-β promoter sequence."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-15T07:34:57.290Z"}},{"region_id":"DP00040r007","ec_ontology":"ECO","end":89,"term_id":"GO:0003677","start":80,"version":5,"statement":[{"text":"In the absence of DNA, the NMR spectrum of HMG-1(2/3) is indicative of a random coil. Upon binding, the two DBDs that contact the DNA become ordered and adopt a well defined conformation in the minor groove.","type":"Article"},{"text":"In contrast, Gly 37 of DBD3 is in fast exchange and its cross peak in the 1H-15N correlation spectrum only begins to shift from its position in the free state at ratios of DNA to protein greater than about 0.8:1, reaching the position of the bound form at a ratio of2:l. Thus, under our experimental conditions, one molecule ofHMG-1(2/3) binds two molecules of the PRDII dodecamer, the equilibrium association constant for the interaction of DBD3 with the PRDII dodecamer is -1.0(±0.5)xl05 M-1, and the affinity of DBD2 for the PRDII dodecamer is about one to two orders of magnitude greater than that ofDBD3.","type":"Article"},{"text":"The DNA in the DBD2 and DBD3 complexes is essentially B-type (Figs 4, 5).","type":"Article"},{"text":"DNA-binding motifs DBD3 of HMGA1","type":"Curator statement"}],"term_name":"DNA binding","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0001-8399-7907","released":"2022_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"9253416","date":"2022-06-14T17:33:01.577Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2EZG"},{"db":"PDB","id":"2EZF"}],"term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"vnugnes","reference_html":"The solution structure of an HMG-I(Y)-DNA complex defines a new architectural minor groove binding motif. <i> Huth JR, Bewley CA, Nissen MS, Evans JN, Reeves R, Gronenborn AM, Clore GM. </i> Nat Struct Biol, 1997","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting DNA 5'-GGGAAATTCCTC, corresponds to the PRDII element of the IFN-β promoter sequence."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-15T07:35:28.648Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":89,"region_id":"DP00040r008","reference_id":"22615915","start":80,"term_id":"GO:0008301","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Bending of the DNA is probably due to the presence of the AT-hook, which distorts the minor groove.","type":"Results"}],"curator_id":"vnugnes","released":"2022_06","term_ontology":"GO","curator_name":"Victoria Nugnes","ec_name":"x-ray crystallography evidence used in manual assertion","version":5,"reference_html":"Crystal structure of a complex of DNA with one AT-hook of HMGA1. <i> Fonfría-Subirós E, Acosta-Reyes F, Saperas N, Pous J, Subirana JA, Campos JL. </i> PLoS One, 2012","date":"2022-06-14T17:33:20.289Z","reference_source":"pmid","ec_id":"ECO:0005670","term_name":"DNA binding, bending","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The activity of binding selectively and non-covalently to and distorting the original structure of DNA, typically a straight helix, into a bend, or increasing the bend if the original structure was intrinsically bent due to its sequence.\" [GOC:krc, GOC:vw, PMID:10710711, PMID:19037758]","disprot_namespace":"Disorder function","term_is_binding":true,"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"The concentrations of DNA and peptide were 0.2 mM and 0.4 mM respectively, with a 1[ratio]2 ratio of DNA duplex to peptide."},{"type":"Curator statement","text":"Interacting DNA with sequence CGAATTAATTCG."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-15T07:35:31.806Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":107,"region_id":"DP00040r012","reference_id":"11602345","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Circular dichroism spectrum of the HMGA1a (a.k.a. HMG-I) protein is essentially unstructured while free in solution.","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"circular dichroism evidence used in manual assertion","version":3,"reference_html":"Molecular biology of HMGA proteins: hubs of nuclear function. <i> Reeves R. </i> Gene, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006200","validated":{"curator_id":"bmesza","timestamp":"2020-11-26T13:24:15.230Z","curator_name":"Bálint Mészáros"},"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":55,"region_id":"DP00040r016","reference_id":"7532403","start":51,"term_id":"IDPO:0000045","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"A threonine residue at the beginning of each DNA-binding domain of HMG-I (residue numbers 21, 53, and 78) is conserved among mammalian species and proposed to help stabilize the A.T-hook DNA-binding motif. Phosphorylation of threonines number 53 and 78 of human HMG-I(Y) both in vivo and in vitro leads to a 20 fold reduction in the proteins DNA binding affinity.","type":"Abstract"},{"text":"Replacement of these threonines did not affect the equilibrium binding of these proteins to DNA as compared with wild-type HMG-I and HMG-Y. Molecular modelling of analogous peptides supported this finding. We conclude that these threonines are not directly important for A.T-hook DNA-binding and are conserved phosphorylation sites for down regulation of DNA binding by the A.T-hook motif in the HMG-I(Y) proteins.","type":"Abstract"},{"text":"Phosphorylated Thr53 and flanking regions.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"fluorescence polarization evidence used in manual assertion","version":3,"reference_html":"Replacement of conserved threonines by alanine residues in high mobility group protein HMG-I(Y): effect on DNA binding affinity. <i> Siino JS, Nissen MS, Reeves R. </i> Biochem Biophys Res Commun, 1995","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006277","validated":{"curator_id":"bmesza","timestamp":"2020-11-26T15:24:08.557Z","curator_name":"Bálint Mészáros"},"term_name":"phosphorylation display site","ec_go":"IPI","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":80,"region_id":"DP00040r017","reference_id":"7532403","start":76,"term_id":"IDPO:0000045","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"A threonine residue at the beginning of each DNA-binding domain of HMG-I (residue numbers 21, 53, and 78) is conserved among mammalian species and proposed to help stabilize the A.T-hook DNA-binding motif. Phosphorylation of threonines number 53 and 78 of human HMG-I(Y) both in vivo and in vitro leads to a 20 fold reduction in the proteins DNA binding affinity.","type":"Abstract"},{"text":"Replacement of these threonines did not affect the equilibrium binding of these proteins to DNA as compared with wild-type HMG-I and HMG-Y. Molecular modelling of analogous peptides supported this finding. We conclude that these threonines are not directly important for A.T-hook DNA-binding and are conserved phosphorylation sites for down regulation of DNA binding by the A.T-hook motif in the HMG-I(Y) proteins.","type":"Abstract"},{"text":"Phosphorylated Thr78 and flanking regions.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"fluorescence polarization evidence used in manual assertion","version":3,"reference_html":"Replacement of conserved threonines by alanine residues in high mobility group protein HMG-I(Y): effect on DNA binding affinity. <i> Siino JS, Nissen MS, Reeves R. </i> Biochem Biophys Res Commun, 1995","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006277","validated":{"curator_id":"bmesza","timestamp":"2020-11-26T15:24:09.512Z","curator_name":"Bálint Mészáros"},"term_name":"phosphorylation display site","ec_go":"IPI","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":105,"region_id":"DP00040r018","reference_id":"2806554","start":100,"term_id":"IDPO:0000045","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Sequence analysis of the native peptide (90-107) after treatment, which specifically converts phosphoserine residues to S-ethylcysteine, revealed that 70-80% of serine residues 102 and 103 were phosphorylated in vivo. Both residues were fully phosphorylated in vitro by incubation with casein kinase II. ","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"enzymatic activity assay evidence used in manual assertion","version":3,"reference_html":"Identification of sites on chromosomal protein HMG-I phosphorylated by casein kinase II. <i> Palvimo J, Linnala-Kankkunen A. </i> FEBS Lett, 1989","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005801","validated":{"curator_id":"bmesza","timestamp":"2020-11-26T15:24:51.491Z","curator_name":"Bálint Mészáros"},"term_name":"phosphorylation display site","ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":11,"region_id":"DP00040r019","reference_id":"28190768","start":6,"term_id":"IDPO:0000038","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"High-resolution ETD analysis confirmed ADPr on S499, S507, and S519 in PARP-1, and it revealed five targets of S-ADPr as follows: HMGA1 (S8 and S9), HMGB1 (S181), HMGN1 (S7), NPM1 (S207), and TMA7 (S61) (Figures 3A–3C, S3A, and S3B).","type":"Results"},{"text":"ADP-ribosylation of Ser8 and Ser9 of HMGA1 depends on HPF1.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"protein mass spectrometry evidence used in manual assertion","version":3,"reference_html":"Serine ADP-Ribosylation Depends on HPF1. <i> Bonfiglio JJ, Fontana P, Zhang Q, Colby T, Gibbs-Seymour I, Atanassov I, Bartlett E, Zaja R, Ahel I, Matic I. </i> Mol Cell, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007184","validated":{"curator_id":"bmesza","timestamp":"2020-11-26T15:25:49.565Z","curator_name":"Bálint Mészáros"},"term_name":"ADP-ribosylation display site","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":107,"region_id":"DP00040r020","reference_id":"11602345","start":1,"term_id":"GO:0060090","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Reversible transitions between disordered and ordered configurations of the HMGA proteins, mediated by labile secondary biochemical modifications (Fig. 2), are likely to provide the necessary molecular underpinning for regulating the formation of functional HMGA complexes in cells and thereby controlling the biological activity of these proteins in vivo.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","version":4,"reference_html":"Molecular biology of HMGA proteins: hubs of nuclear function. <i> Reeves R. </i> Gene, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","validated":{"curator_id":"bmesza","timestamp":"2020-11-26T13:24:33.404Z","curator_name":"Bálint Mészáros"},"term_name":"molecular adaptor activity","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":75,"region_id":"DP00040r022","reference_id":"11069991","start":9,"term_id":"GO:0003677","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"A derivative of HMG I lacking amino acids 91 to 108, the acidic C-terminal domain, was also capable of reconstituting integration activity (Fig. ​(Fig.3B,3B, lane 4). Derivatives containing amino acids 9 to 75 or 50 to 91, either A/T hooks 1 plus 2 or 2 plus 3, also reconstituted activity (Fig. ​(Fig.3B,3B, lanes 6, 8, and 9). The 50–91 protein displayed the highest specific activity for reconstitution, retaining activity at 0.2 μg per reaction.","type":"Results"},{"text":"We also demonstrated that the HIV-1 long terminal repeats (LTRs) contain multiple DNA binding sites for HMG I(Y). Tests in vitro revealed that binding of HMG I(Y) apposed LTR DNAs in a manner that promoted intermolecular ligation of dilute DNA solutions. As with assays of PIC reconstitution, these assays of DNA condensation required multiple DNA binding domains in each HMG I(Y) monomer. Taken together, these studies strengthen the idea that HMG I(Y) acts as an architectural cofactor for retroviral cDNA integration complexes and suggest a model for its role.","type":"Introduction"},{"text":"HMGA1 fragment including AT-hook 1 and 2.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"immunodetection assay evidence used in manual assertion","version":4,"reference_html":"Retroviral cDNA integration: stimulation by HMG I family proteins. <i> Li L, Yoder K, Hansen MS, Olvera J, Miller MD, Bushman FD. </i> J Virol, 2000","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","validated":{"curator_id":"bmesza","timestamp":"2020-11-26T14:34:18.793Z","curator_name":"Bálint Mészáros"},"term_name":"DNA binding","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":91,"region_id":"DP00040r023","reference_id":"11069991","start":50,"term_id":"GO:0003677","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"A derivative of HMG I lacking amino acids 91 to 108, the acidic C-terminal domain, was also capable of reconstituting integration activity (Fig. ​(Fig.3B,3B, lane 4). Derivatives containing amino acids 9 to 75 or 50 to 91, either A/T hooks 1 plus 2 or 2 plus 3, also reconstituted activity (Fig. ​(Fig.3B,3B, lanes 6, 8, and 9). The 50–91 protein displayed the highest specific activity for reconstitution, retaining activity at 0.2 μg per reaction.","type":"Results"},{"text":"We also demonstrated that the HIV-1 long terminal repeats (LTRs) contain multiple DNA binding sites for HMG I(Y). Tests in vitro revealed that binding of HMG I(Y) apposed LTR DNAs in a manner that promoted intermolecular ligation of dilute DNA solutions. As with assays of PIC reconstitution, these assays of DNA condensation required multiple DNA binding domains in each HMG I(Y) monomer. Taken together, these studies strengthen the idea that HMG I(Y) acts as an architectural cofactor for retroviral cDNA integration complexes and suggest a model for its role.","type":"Introduction"},{"text":"HMGA1 fragment including AT-hook 2 and 3.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"immunodetection assay evidence used in manual assertion","version":4,"reference_html":"Retroviral cDNA integration: stimulation by HMG I family proteins. <i> Li L, Yoder K, Hansen MS, Olvera J, Miller MD, Bushman FD. </i> J Virol, 2000","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","validated":{"curator_id":"bmesza","timestamp":"2020-11-26T14:34:19.920Z","curator_name":"Bálint Mészáros"},"term_name":"DNA binding","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":107,"region_id":"DP00040r024","reference_id":"11069991","start":1,"term_id":"GO:0060090","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"A derivative of HMG I lacking amino acids 91 to 108, the acidic C-terminal domain, was also capable of reconstituting integration activity (Fig. ​(Fig.3B,3B, lane 4). Derivatives containing amino acids 9 to 75 or 50 to 91, either A/T hooks 1 plus 2 or 2 plus 3, also reconstituted activity (Fig. ​(Fig.3B,3B, lanes 6, 8, and 9). The 50–91 protein displayed the highest specific activity for reconstitution, retaining activity at 0.2 μg per reaction.","type":"Results"},{"text":"We also demonstrated that the HIV-1 long terminal repeats (LTRs) contain multiple DNA binding sites for HMG I(Y). Tests in vitro revealed that binding of HMG I(Y) apposed LTR DNAs in a manner that promoted intermolecular ligation of dilute DNA solutions. As with assays of PIC reconstitution, these assays of DNA condensation required multiple DNA binding domains in each HMG I(Y) monomer. Taken together, these studies strengthen the idea that HMG I(Y) acts as an architectural cofactor for retroviral cDNA integration complexes and suggest a model for its role.","type":"Introduction"},{"text":"The binding of HMGA to AT-rich sites in PICs retroviral cDNAs leads to the formation of integrase-cDNA complexes.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"immunodetection assay evidence used in manual assertion","version":4,"reference_html":"Retroviral cDNA integration: stimulation by HMG I family proteins. <i> Li L, Yoder K, Hansen MS, Olvera J, Miller MD, Bushman FD. </i> J Virol, 2000","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","validated":{"curator_id":"bmesza","timestamp":"2020-11-26T14:34:34.923Z","curator_name":"Bálint Mészáros"},"term_name":"molecular adaptor activity","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00040r025","validated":{"curator_id":"bmesza","timestamp":"2020-11-26T14:36:54.204Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":107,"term_id":"GO:0005515","start":1,"version":4,"statement":[{"text":"Wild type HMG I, as well as 3 block alanine mutants (residues 21–26, 46–52, and 71–74) were found to bind p50 relatively well, although this interaction is abolished with the other alanine mutants (G59A, R60A, P61A4, K62A, and G63A) and GST as a control.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P19838","partner_end":null}],"term_name":"protein binding","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"10400641","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001807","curator_id":"fquaglia","reference_html":"A small region in HMG I(Y) is critical for cooperation with NF-kappaB on DNA. <i> Zhang XM, Verdine GL. </i> J Biol Chem, 1999","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":80,"term_name":"flexible linker","reference_html":"The solution structure of an HMG-I(Y)-DNA complex defines a new architectural minor groove binding motif. <i> Huth JR, Bewley CA, Nissen MS, Evans JN, Reeves R, Gronenborn AM, Clore GM. </i> Nat Struct Biol, 1997","start":70,"region_id":"DP00040r029","term_id":"IDPO:0000033","version":4,"curator_id":"vnugnes","released":"2022_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Third, analysis of 15 N relaxation data 12 for the 2:1 DNA to protein complex (Fig. 3a) delineated two distinct ordered domains comprising a longer DBD2 (residues 7- 22) and a shorter DBD3 (residues 33-41) separated by a highly flexible linker (residues 22- 32).","type":"Results"},{"text":"The flexible linker defined as 22-32 actually corresponds to region 70-80 in the UniProt numbering.","type":"Curator statement"}],"curator_orcid":"0000-0001-8399-7907","date":"2022-06-14T17:33:41.529Z","reference_source":"pmid","ec_id":"ECO:0006165","reference_id":"9253416","ec_go":"EXP","disprot_namespace":"Disorder function","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting DNA 5'-GGGAAATTCCTC, corresponds to the PRDII element of the IFN-β promoter sequence."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-15T07:35:20.518Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":107,"term_name":"DNA binding","reference_html":"Dynamic interaction of HMGA1a proteins with chromatin. <i> Harrer M, Lührs H, Bustin M, Scheer U, Hock R. </i> J Cell Sci, 2004","start":1,"region_id":"DP00040r030","term_id":"GO:0003677","version":3,"curator_id":"bmesza","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","ec_name":"fluorescence recovery after photobleaching evidence used in manual assertion","statement":[{"text":"We identified the first two of the three AT hooks as main players mediating DNA/chromatin binding.","type":"Abstract"},{"text":"AT-hook motifs I and II of HMGA1a are main mediators of DNA binding in vivo","type":"Results"}],"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006067","reference_id":"15213251","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-04-07T08:25:32.441Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":107,"term_name":"RNA binding","reference_html":"7SK small nuclear RNA directly affects HMGA1 function in transcription regulation. <i> Eilebrecht S, Brysbaert G, Wegert T, Urlaub H, Benecke BJ, Benecke A. </i> Nucleic Acids Res, 2011","start":1,"region_id":"DP00040r031","term_id":"GO:0003723","version":4,"curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","statement":[{"text":"EMSAs with 7SK L2 RNA revealed that HMGA1a 3xΔA/T shows not only a decreased DNA-binding activity but also a significantly reduced ability to interact with 7SK L2 RNA (Figure 2C). Furthermore, EMSAs of 7SK L2 RNA with HMGA1 versions containing mutations of each single A/T-hook motif (HMGA1a ΔA/T1, HMGA1a ΔA/T2 and HMGA1a ΔA/T3) identify the first A/T-hook motif of HMGA1a as the site of interaction with 7SK RNA (Figure 2C, upper panel), since the same reduction in binding affinity is observed with the single HMGA1a ΔA/T1 mutant as with the triple mutant. ","type":"Results"}],"curator_orcid":"0000-0002-5152-5953","date":"2022-03-08T15:08:16.330Z","reference_source":"pmid","ec_id":"ECO:0001807","reference_id":"21087998","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"RNAcentral","id":"URS0000734D8F_9606","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-09T16:34:56.129Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":107,"term_name":"RNA binding","reference_html":"7SK small nuclear RNA directly affects HMGA1 function in transcription regulation. <i> Eilebrecht S, Brysbaert G, Wegert T, Urlaub H, Benecke BJ, Benecke A. </i> Nucleic Acids Res, 2011","start":1,"region_id":"DP00040r032","term_id":"GO:0003723","version":4,"curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","ec_name":"co-immunoprecipitation evidence used in manual assertion","statement":[{"text":"HMGA1 co-purifies specifically with 7SK RNA","type":"Results"}],"curator_orcid":"0000-0002-5152-5953","date":"2022-03-08T15:08:01.761Z","reference_source":"pmid","ec_id":"ECO:0006030","reference_id":"21087998","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"RNAcentral","id":"URS0000734D8F_9606","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-09T16:34:58.122Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":107,"term_name":"molecular function activator activity","reference_html":"7SK small nuclear RNA directly affects HMGA1 function in transcription regulation. <i> Eilebrecht S, Brysbaert G, Wegert T, Urlaub H, Benecke BJ, Benecke A. </i> Nucleic Acids Res, 2011","start":1,"region_id":"DP00040r033","term_id":"GO:0140677","version":3,"curator_id":"bmesza","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","ec_name":"RNAi evidence used in manual assertion","statement":[{"text":"Importantly, albeit most genes are repressed in their expression by HMGA1, we also identified several genes that are positively regulated by HMGA1 and 7SK RNA (Figure 7A).","type":"Results"}],"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006052","reference_id":"21087998","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-04-07T08:25:42.663Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00040r034","ec_ontology":"ECO","end":107,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"Figure 1C shows that the HMG I antibody coprecipitates CBP (lane 2) and that the CBP antibody coprecipitates HMG I (lane 4).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q92793","partner_end":null}],"term_name":"protein binding","ec_name":"co-immunoprecipitation evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"9809067","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006030","curator_id":"bmesza","reference_html":"Acetylation of HMG I(Y) by CBP turns off IFN beta expression by disrupting the enhanceosome. <i> Munshi N, Merika M, Yie J, Senger K, Chen G, Thanos D. </i> Mol Cell, 1998","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-04-07T08:25:35.836Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":73,"term_name":"acetylation display site","reference_html":"Acetylation of HMG I(Y) by CBP turns off IFN beta expression by disrupting the enhanceosome. <i> Munshi N, Merika M, Yie J, Senger K, Chen G, Thanos D. </i> Mol Cell, 1998","start":69,"region_id":"DP00040r035","term_id":"IDPO:0000039","version":2,"curator_id":"bmesza","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"radioligand binding assay evidence used in manual assertion","statement":[{"text":"Specifically, CBP preferentially acetylates Lys-65 whereas P/CAF preferentially acetylates Lys-71.","type":"Results"}],"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007009","reference_id":"9809067","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-04-07T08:25:44.378Z"},"ec_go":"IPI","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":67,"term_name":"acetylation display site","reference_html":"Acetylation of HMG I(Y) by CBP turns off IFN beta expression by disrupting the enhanceosome. <i> Munshi N, Merika M, Yie J, Senger K, Chen G, Thanos D. </i> Mol Cell, 1998","start":63,"region_id":"DP00040r036","term_id":"IDPO:0000039","version":2,"curator_id":"bmesza","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"radioligand binding assay evidence used in manual assertion","statement":[{"text":"Specifically, CBP preferentially acetylates Lys-65 whereas P/CAF preferentially acetylates Lys-71.","type":"Results"}],"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007009","reference_id":"9809067","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-04-07T08:25:46.732Z"},"ec_go":"IPI","disprot_namespace":"Disorder function"},{"region_id":"DP00040r037","ec_ontology":"ECO","end":89,"term_id":"GO:0003677","start":81,"version":4,"statement":[{"text":"Here we present the crystal structure of the complex of a DNA oligonucleotide with the third AT-hook (DBD3 in ref. 10) of the HMGA1 protein. ","type":"Introduction"}],"term_name":"DNA binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0001-8399-7907","released":"2022_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"22615915","date":"2022-06-14T17:34:11.703Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3uxw"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"vnugnes","reference_html":"Crystal structure of a complex of DNA with one AT-hook of HMGA1. <i> Fonfría-Subirós E, Acosta-Reyes F, Saperas N, Pous J, Subirana JA, Campos JL. </i> PLoS One, 2012","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting DNA with sequence CGAATTAATTCG."},{"type":"Methods","text":"The concentrations of DNA and peptide were 0.2 mM and 0.4 mM respectively, with a 1[ratio]2 ratio of DNA duplex to peptide."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-15T07:35:14.544Z"}},{"start":50,"end":91,"reference_id":"9253416","reference_source":"pmid","reference_html":"The solution structure of an HMG-I(Y)-DNA complex defines a new architectural minor groove binding motif. <i> Huth JR, Bewley CA, Nissen MS, Evans JN, Reeves R, Gronenborn AM, Clore GM. </i> Nat Struct Biol, 1997","date":"2022-06-14T17:34:42.048Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003713","term_name":"transcription coactivator activity","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":2,"cross_refs":[{"db":"PDB","id":"2EZD"},{"db":"PDB","id":"2EZF"},{"db":"PDB","id":"2EZG"},{"db":"PDB","id":"2EZE"}],"region_id":"DP00040r038","statement":[{"text":"The structure reveals a new architectural minor groove binding motif which stabilizes B-DNA, thereby facilitating the binding of other transcription factors in the opposing major groove. ","type":"Abstract"},{"text":" Hence, it seems likely that the principal architectural role of HMG-1 probably involves reversing and preventing intrinsic distortions in DNA conformation, including bending or kinking, by binding in the minor groove, thereby facilitating specific recognition of the opposing major groove by other transcriptional factors such as NF-KB.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"For usage guidance, see comment in GO:0003712 ; transcription coregulator activity.","term_def":"\"A transcription coregulator activity that activates or increases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coactivators modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. A fourth class of coactivator activity is the bridging of a DNA-binding transcription factor to the general (basal) transcription machinery. The Mediator complex, which bridges sequence-specific DNA binding transcription factors and RNA polymerase, is also a transcription coactivator.\" [GOC:txnOH-2018, PMID:10213677, PMID:16858867]","disprot_namespace":"Disorder function","term_is_binding":false,"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting DNA 5'-GGGAAATTCCTC, corresponds to the PRDII element of the IFN-β promoter sequence."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-15T07:35:07.801Z"}},{"start":1,"end":107,"reference_id":"10428834","reference_source":"pmid","reference_html":"Retinoid-dependent recruitment of a histone H1 displacement activity by retinoic acid receptor. <i> Nagpal S, Ghosn C, DiSepio D, Molina Y, Sutter M, Klein ES, Chandraratna RA. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0003713","term_name":"transcription coactivator activity","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006050","ec_ontology":"ECO","ec_name":"anti-sense experiment evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00040r039","statement":[{"text":"We further show that HMG-I and a novel related protein, HMG-R, also interact with other transcription factors. Using sense and antisense constructs of HMG-I/R in transient transfection assays with a retinoid responsive reporter, we also demonstrate that HMG-I/R is important for retinoid dependent transcriptional activity of RAR. These findings suggest a step wise mechanism by which RARs and other transcription factors can cause a targeted unfolding of compact chromatin as a first step in transcriptional activation, which would then be followed by recruitment of HAT activity and subsequent events.","type":"Abstract"},{"text":"Our data indicate that RARs and other transcription factors are capable of recruiting the H1 displacing activities of HMG-I/HMG-R in a targeted and ligand-dependent manner (Fig. 7). Since HMG-I protein has 19 putative acetylation sites (lysine residues), including two in the DNA binding AzT hook domain (Fig. 2B), the acetylation of HMG-I by CBP/p300 could potentially decrease its ability to displace H1. However, in accordance with its proposed role as a H1 displacement factor, either CBP or p300 (Fig. 5A) did not acetylate HMG-I ","type":"Results"},{"text":"In order to destabilize compact higher order chromatin structures and to liberate DNA from the nucleosome at the site of active transcription and facilitate RNA polymerase II complex assembly, both linker and chromosomal histones need to be released by transcription factors. Our model predicts that nuclear receptors and other transcription factors may recruit HMG-I/HMG-R and HATs in a targeted step wise manner, thereby unraveling linker and core histone assembly and facilitating the formation of transcriptionally competent DNA in the promoter regions of target genes.","type":"Results"},{"text":"We further show that HMG-I and HMG-R interact with RXR-α , PPAR-γ, c-Jun, and CBP, thus indicating recruitment of HMG-I/R by various transcription factors as a common mechanism for enhancer-dependent transcriptional activation. Finally, using transient transfections, we demonstrate that HMG-I/R is required for retinoid-dependent transactivation of a reporter construct by RAR, thus showing the functional consequences of RAR-HMG-I/R interactions. ","type":"Introduction"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-16T12:32:26.990Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"For usage guidance, see comment in GO:0003712 ; transcription coregulator activity.","term_def":"\"A transcription coregulator activity that activates or increases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coactivators modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. A fourth class of coactivator activity is the bridging of a DNA-binding transcription factor to the general (basal) transcription machinery. The Mediator complex, which bridges sequence-specific DNA binding transcription factors and RNA polymerase, is also a transcription coactivator.\" [GOC:txnOH-2018, PMID:10213677, PMID:16858867]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":107,"reference_id":"10428834","reference_source":"pmid","reference_html":"Retinoid-dependent recruitment of a histone H1 displacement activity by retinoic acid receptor. <i> Nagpal S, Ghosn C, DiSepio D, Molina Y, Sutter M, Klein ES, Chandraratna RA. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005805","ec_ontology":"ECO","ec_name":"yeast 2-hybrid evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"P13631","partner_start":90,"partner_end":454}],"region_id":"DP00040r040","statement":[{"text":" In this report, we show that RARs interact in a ligand-dependent manner with HMG-I, which is known to displace histone H1 from chromatin.","type":"Abstract"},{"text":" HMG-I and HMG-R interact with RARγΔAB in yeast. ","type":"Figure"},{"text":"HMG-I and HMG-R proteins interacted specifically with RARγΔAB in the presence but not in the absence of the RAR-specific agonist, TTNPB (15) (Fig. 2A), demonstrating the ligand dependence of RAR/HMG interaction. TTNPB-induced RARγΔΔB interaction with both HMG-I and HMG-R was dose-dependent (data not shown).","type":"Results"},{"text":"HMG-R is a variant of HMG-I with a deletion of 67 nucleotids, being identical in the first 65 AA but differing thereafter. This protein is not listed on UniProt","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-16T12:32:21.028Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":107,"reference_id":"10428834","reference_source":"pmid","reference_html":"Retinoid-dependent recruitment of a histone H1 displacement activity by retinoic acid receptor. <i> Nagpal S, Ghosn C, DiSepio D, Molina Y, Sutter M, Klein ES, Chandraratna RA. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005616","ec_ontology":"ECO","ec_name":"beta-galactosidase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"P13631","partner_start":90,"partner_end":454}],"region_id":"DP00040r041","statement":[{"text":"To demonstrate that the full-length RARγ also interacts with HMG-I/HMG-R in a ligand-dependent manner in vivo, stably transformed RARγ (pAS2-RARγ) yeast cells were further transformed with pACT2-HMG-I/HMG-R and assayed for β-galactosidase activity in the  absence or presence of TTNPB. Full-length RARγ, by virtue of its intrinsic activation functions (2), elicited a low level of β-galactosidase activity in the presence of TTNPB, which was further induced approximately 25-fold in the presence of pACT2-HMG-I and pACT2-HMG-R (Fig. 3A). ","type":"Results"},{"text":"To determine the regions of RAR involved in interaction with HMG in vivo, pGBT-RARγ-DEF, pAS2-RARγΔAB, and pAS2-RARγ transformed yeast cells were used. pACT2-HMG-R interacted poorly with RARγDEF and RARγΔAB but interacted strongly with RARγ (Fig. 3D).","type":"Results"},{"text":"HMG-R is a variant of HMG-I with a deletion of 67 nucleotids, being identical in the first 65 AA but differing thereafter. This protein is not listed on UniProt","type":"Curator statement"},{"text":"Full-length RARγ interacted with both HMG-I and HMG-R in a retinoid dose-dependent manner (Fig. 3E).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-16T12:32:04.175Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P17096","date":"2016-08-23T17:55:46.000Z","acc":"P17096","name":"High mobility group protein HMG-I/HMG-Y","length":107,"organism":"Homo sapiens","dataset":["Cancer-related proteins","RNA-binding proteins"],"UniParc":"UPI000012CA33","genes":[{"name":{"value":"HMGA1"},"synonyms":[{"value":"HMGIY"}]}],"alphafold_very_low_content":0.009345794392523364,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":50,"type":"D"},{"start":51,"end":75,"type":"T"},{"start":76,"end":79,"type":"D"},{"start":80,"end":89,"type":"T"},{"start":90,"end":107,"type":"D"}],"Structural state":[{"start":1,"end":107,"type":"D"}],"Molecular function":[{"start":1,"end":107,"type":"F"}],"Structural transition":[{"start":51,"end":75,"type":"T"},{"start":80,"end":89,"type":"T"}],"Disorder function":[{"start":6,"end":11,"type":"F"},{"start":51,"end":55,"type":"F"},{"start":63,"end":67,"type":"F"},{"start":69,"end":80,"type":"F"},{"start":100,"end":105,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01101","name":"HMG14 and HMG17","start":2,"end":61}]},"uniref50":"UniRef50_P02315","sequence":"MPKRKSATKGDEPARRSARLSARPVPKPAAKPKKAAAPKKAVKGKKAAENGDAKAEAKVQAAGDGAGNAK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Actinopterygii","Neopterygii","Teleostei","Protacanthopterygii","Salmoniformes","Salmonidae","Salmoninae","Oncorhynchus"],"uniref90":"UniRef90_P02315","disprot_id":"DP00042","ncbi_taxon_id":8022,"regions_counter":4,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":70,"region_id":"DP00042r001","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Structural studies of the non-histone chromosomal proteins HMG-T and H6 from trout testis. <i> Cary PD, Crane-Robinson C, Bradbury EM, Dixon GH. </i> Eur J Biochem, 1981","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"6273163","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-09-06T20:40:58.161Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"All the  resonances are sharp  and  are readily  assigned to equivalent  residues of a given type. It is  the spectrum typical of a disordered protein.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:09:15.914Z"}},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":35,"term_name":"nucleic acid binding","start":10,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2022_12","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"6273163","version":4,"reference_html":"Structural studies of the non-histone chromosomal proteins HMG-T and H6 from trout testis. <i> Cary PD, Crane-Robinson C, Bradbury EM, Dixon GH. </i> Eur J Biochem, 1981","date":"2022-09-06T20:45:27.683Z","term_id":"GO:0003676","ec_id":"ECO:0006165","region_id":"DP00042r003","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"statement":[{"text":"The line widths in 0 M NaCl are somewhat  greater than in 500 mM NaCl however and this demonstrates that the H6 does interact with   the DNA under these conditions  but that bound H6 is in rapid  equilibrium with  free solution  H6.","type":"Results"},{"text":"The specific peak broadening observed  suggest that it is largely the N-terminal half of H6 that is involved in inter- actions with DNA. Since the single threonine at position 7 is not markedly  affected,  the interacting segment probably extends from around residue 10 to around residue 35. ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:09:21.148Z"}},{"start":1,"end":70,"reference_id":"6273163","reference_source":"pmid","reference_html":"Structural studies of the non-histone chromosomal proteins HMG-T and H6 from trout testis. <i> Cary PD, Crane-Robinson C, Bradbury EM, Dixon GH. </i> Eur J Biochem, 1981","date":"2022-09-06T20:48:04.113Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00042r004","statement":[{"text":"Circular  dichroism  spectra of H6 obtained  under similar conditions support this conclusion : in the  absence of salt  the ellipticity at 222 nm is z -1000\" and this   changes to - 2000° in 1 M NaCl at pH 7. On the basis of - 1000° for a random coil [21] and -30000° for a  full helical chain [22], -2000°   represents <4% helix or less than three  residues.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:09:16.845Z"}}],"released":"2016_10","uniref100":"UniRef100_P02315","date":"2016-08-22T17:43:47.000Z","acc":"P02315","name":"Non-histone chromosomal protein H6","length":70,"organism":"Oncorhynchus mykiss","dataset":[],"UniParc":"UPI000012C020","genes":[],"alphafold_very_low_content":0.07142857142857142,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":70,"type":"D"}],"Structural state":[{"start":1,"end":70,"type":"D"}],"Molecular function":[{"start":10,"end":35,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03544","name":"Gram-negative bacterial TonB protein C-terminal","start":160,"end":230},{"id":"PF16031","name":"TonB polyproline region","start":33,"end":157}],"gene3D":[{"start":150,"end":239,"id":"3.30.2420.10","name":"TonB"}]},"uniref50":"UniRef50_P02929","sequence":"MTLDLPRRFPWPTLLSVCIHGAVVAGLLYTSVHQVIELPAPAQPISVTMVTPADLEPPQAVQPPPEPVVEPEPEPEPIPEPPKEAPVVIEKPKPKPKPKPKPVKKVQEQPKRDVKPVESRPASPFENTAPARLTSSTATAATSKPVTSVASGPRALSRNQPQYPARAQALRIEGQVKVKFDVTPDGRVDNVQILSAKPANMFEREVKNAMRRWRYEPGKPGSGIVVNILFKINGTTEIQ","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P02929","disprot_id":"DP00043","ncbi_taxon_id":83333,"regions_counter":1,"creator":"mnecci","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":151,"region_id":"DP00043r001","reference_id":"15644214","start":103,"ec_id":"ECO:0006165","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"TonB-CTD is monomeric with an unstructured N terminus (103-151) and a well structured C terminus (152-239).","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":4,"reference_html":"The solution structure of the C-terminal domain of TonB and interaction studies with TonB box peptides. <i> Sean Peacock R, Weljie AM, Peter Howard S, Price FD, Vogel HJ. </i> J Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","cross_refs":[{"db":"PDB","id":"1XX3"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-06T20:15:47.199Z"}}],"released":"2016_10","uniref100":"UniRef100_P02929","date":"2016-09-12T12:08:18.000Z","acc":"P02929","name":"Protein TonB","length":239,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI000016EC8B","genes":[{"name":{"value":"tonB"},"synonyms":[{"value":"exbA"}],"olnNames":[{"value":"b1252"},{"value":"JW5195"}]}],"alphafold_very_low_content":0.03765690376569038,"disorder_content":0.20502092050209206,"disprot_consensus":{"full":[{"start":103,"end":151,"type":"D"}],"Structural state":[{"start":103,"end":151,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00538","name":"linker histone H1 and H5 family","start":26,"end":97}],"gene3D":[{"start":20,"end":110,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}]},"uniref50":"UniRef50_P02259","sequence":"MTESLVLSPAPAKPKRVKASRRSASHPTYSEMIAAAIRAEKSRGGSSRQSIQKYIKSHYKVGHNADLQIKLSIRRLLAAGVLKQTKGVGASGSFRLAKSDKAKRSPGKKKKAVRRSTSPKKAARPRKARSPAKKPKATARKARKKSRASPKKAKKPKTVKAKSRKASKAKKVKRSKPRAKSGARKSPKKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Phasianinae","Gallus"],"uniref90":"UniRef90_P02259","disprot_id":"DP00044","ncbi_taxon_id":9031,"regions_counter":10,"creator":"ftonello","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":21,"region_id":"DP00044r002","released":"2022_12","ec_id":"ECO:0007691","reference_html":"The conformation of histone H5. Isolation and characterisation of the globular segment. <i> Aviles FJ, Chapman GE, Kneale GG, Crane-Robinson C, Bradbury EM. </i> Eur J Biochem, 1978","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"689022","version":3,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-09-07T15:57:39.752Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"This extensive digestion is thought to be a consequence of disordered chain regions, whilst the sequence  22- 100 shows resistance to digestion as a  result  of  being in a  com- pact folded form, i.e. peptide GH5 is a close approxi- mation to the compact region  of intact H5.","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:07:40.364Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":109,"region_id":"DP00044r008","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Crystal structure of globular domain of histone H5 and its implications for nucleosome binding. <i> Ramakrishnan V, Finch JT, Graziano V, Lee PL, Sweet RM. </i> Nature, 1993","term_id":"IDPO:0000002","curator_id":"vnugnes","start":99,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"8384699","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-09-07T15:50:12.560Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1HST"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Thus of the 89 residues in the polypeptide chain, 5  residues at the N terminus and II residues at the C terminus are missing in the current model. ","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:07:42.719Z"}},{"start":102,"end":190,"reference_id":"https://mobidb.org/P02259","reference_source":"mobidb","reference_html":"An Entry Referenced from MobiDB","date":"2022-02-14T09:00:00.000Z","curator_id":"amonzon","curator_name":"Alex Monzon","curator_orcid":"0000-0003-0362-8218","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007759","ec_ontology":"ECO","ec_name":"curator inference from database used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00044r009","statement":[{"text":"This poly-E region is inferred by the curator to be disordered, based on MobiDB-Lite and according to experimental evidence demonstrating that poly-E repeats display random-coil-like conformation (PMID:16949547)","type":"Curator statement"}],"ec_go":"IC","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-13T10:07:44.960Z"}},{"start":101,"end":190,"reference_id":"689022","reference_source":"pmid","reference_html":"The conformation of histone H5. Isolation and characterisation of the globular segment. <i> Aviles FJ, Chapman GE, Kneale GG, Crane-Robinson C, Bradbury EM. </i> Eur J Biochem, 1978","date":"2023-01-13T13:08:34.235Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP00044r010","statement":[{"text":"This extensive digestion is thought to be a consequence of disordered chain regions, whilst the sequence  22- 100 shows resistance to digestion as a  result  of  being in a  com- pact folded form, i.e. peptide GH5 is a close approxi- mation to the compact region  of intact H5.","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-16T09:56:57.883Z"}}],"released":"2016_10","uniref100":"UniRef100_P02259","date":"2016-09-04T10:35:53.000Z","acc":"P02259","name":"Histone H5","length":190,"organism":"Gallus gallus","dataset":[],"UniParc":"UPI000017133E","genes":[],"alphafold_very_low_content":0.23157894736842105,"disorder_content":0.5947368421052631,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"},{"start":99,"end":190,"type":"D"}],"Structural state":[{"start":1,"end":21,"type":"D"},{"start":99,"end":190,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01669","name":"Myelin basic protein","start":13,"end":169}]},"uniref50":"UniRef50_P02687","sequence":"AAQKRPSQRSKYLASASTMDHARHGFLPRHRDTGILDSLGRFFGSDRGAPKRGSGKDGHHAARTTHYGSLPQKAQGHRPQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGLKGHDAQGTLSKIFKLGGRDSRSGSPMARR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P02687","disprot_id":"DP00047","ncbi_taxon_id":9913,"regions_counter":11,"creator":"agasparini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":169,"region_id":"DP00047r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Conformation of bovine myelin basic protein purified with bound lipids. <i> Polverini E, Fasano A, Zito F, Riccio P, Cavatorta P. </i> Eur Biophys J, 1999","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10394626","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In order to acquire insight into the structure of MBP, we have carried out circular dichroism (CD) experiments on the protein both in the lipid-free and in the lipid-bound form. Our data clearly show that lipid-free MBP is mainly disordered with only a small amount having alpha-helix and beta-sheet motifs.","type":"Abstract"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-09T15:45:19.168Z"}},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":169,"term_name":"disorder to order","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10394626","version":3,"reference_html":"Conformation of bovine myelin basic protein purified with bound lipids. <i> Polverini E, Fasano A, Zito F, Riccio P, Cavatorta P. </i> Eur Biophys J, 1999","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00047r003","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"On the other hand, the lipid-bound form of MBP appears to have a consistent amount of ordered secondary structure.","type":"Abstract"},{"text":"In particular, the increase in the ordered α- and antiparallel β-structures on going from a polar (LF-MBP) to an apolar (LB-MBP) environment is quite evident. Such an increase corresponds to a loss of the random coil and, to a lesser extent, of the β-turn structures. The “other” type of contributions totally disappear in the LB-MBP spectrum. These results demonstrate that MBP assumes a more ordered conformation in the lipid-bound form.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-09T15:55:28.444Z"}},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":169,"term_name":"lipid binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"10394626","version":4,"reference_html":"Conformation of bovine myelin basic protein purified with bound lipids. <i> Polverini E, Fasano A, Zito F, Riccio P, Cavatorta P. </i> Eur Biophys J, 1999","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008289","ec_id":"ECO:0006204","region_id":"DP00047r004","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"On the other hand, the lipid-bound form of MBP appears to have a consistent amount of ordered secondary structure.","type":"Abstract"},{"text":"In particular, the increase in the ordered α- and antiparallel β-structures on going from a polar (LF-MBP) to an apolar (LB-MBP) environment is quite evident. Such an increase corresponds to a loss of the random coil and, to a lesser extent, of the β-turn structures. The “other” type of contributions totally disappear in the LB-MBP spectrum. These results demonstrate that MBP assumes a more ordered conformation in the lipid-bound form. ","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-09T15:57:28.729Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":169,"region_id":"DP00047r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Interaction of bovine myelin basic protein with triphosphoinositide. <i> Rivas AA, Castro RM. </i> J Colloid Interface Sci, 2002","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12573634","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The CD far-UV spectrum of MBP shows a a large negative peak around 200 nm in aqueous solution, indicative of a disordered conformation of the protein in the unbound state.","type":"Curator statement"},{"text":"In aqueous solution, MBP showed a random coil structure confirmed by its circular dichroism (CD) spectra.","type":"Abstract"},{"text":"The thermodynamically stable state of aqueous MBP is known to exhibit no secondary structure (15). The CD results also indicate that the protein sample used to examine interaction between MBP and TPI was of a random coil structure. More orderly structures have been ascribed to interactions with other molecules including lipids (22), particularly anionic lipids (25).","type":"Discussion"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-09T15:33:37.457Z"}},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":169,"term_name":"lipid binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_12","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"12573634","version":5,"reference_html":"Interaction of bovine myelin basic protein with triphosphoinositide. <i> Rivas AA, Castro RM. </i> J Colloid Interface Sci, 2002","date":"2022-09-14T08:55:28.689Z","term_id":"GO:0008289","ec_id":"ECO:0006204","region_id":"DP00047r008","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Given that MBP is known to specifically interact with the membrane's lipid components, this study was designed to explore the effects of these lipids on the conformation of the protein by examining its interaction with the lipid triphosphoinositide (TPI). ","type":"Abstract"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"77276","entry_name":"1-stearoyl-2-arachidonoyl-sn-glycero-3-phospho-1D-myo-inositol 4,5-biphosphate"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-14T13:59:20.313Z"}},{"start":1,"end":109,"reference_id":"10394626","reference_source":"pmid","reference_html":"Conformation of bovine myelin basic protein purified with bound lipids. <i> Polverini E, Fasano A, Zito F, Riccio P, Cavatorta P. </i> Eur Biophys J, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00047r011","statement":[{"text":"The presence of the intrinsic lipids around MBP (LB-MBP, spectrum c) causes a further increase in the intensityof the fluorescence emission spectrum and a blue shift of7.5 nm of the maximum.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-09T15:56:00.480Z"}}],"released":"2016_10","uniref100":"UniRef100_P02687","date":"2016-08-24T10:50:35.000Z","acc":"P02687","name":"Myelin basic protein","length":169,"organism":"Bos taurus","dataset":[],"UniParc":"UPI000012ED38","genes":[{"name":{"value":"MBP"}}],"alphafold_very_low_content":0.23668639053254437,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":169,"type":"T"}],"Structural state":[{"start":1,"end":169,"type":"D"}],"Structural transition":[{"start":1,"end":169,"type":"T"}],"Molecular function":[{"start":1,"end":169,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00469","name":"Negative factor, (F-Protein) or Nef","start":2,"end":205}],"gene3D":[{"start":58,"end":206,"id":"3.30.62.10","name":"Nef Regulatory Factor"},{"start":2,"end":57,"id":"4.10.890.10","name":"HIV 1 nef anchor domain"}]},"uniref50":"UniRef50_P03406","sequence":"MGGKWSKSSVVGWPTVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAATNAACAWLEAQEEEEVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGVRYPLTFGWCYKLVPVEPDKVEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"uniref90":"UniRef90_P03406","disprot_id":"DP00048","ncbi_taxon_id":11686,"regions_counter":31,"creator":"esalladini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":77,"region_id":"DP00048r006","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling. <i> Arold S, Franken P, Strub MP, Hoh F, Benichou S, Benarous R, Dumas C. </i> Structure, 1997","term_id":"IDPO:0000002","curator_id":"esalladini","start":58,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"9351809","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1AVV"}],"term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"The  N-terminal  region  from  residue  58  to  the polyproline  motif,  and  the  loop  (residues  149–178)  connecting  strands  βC–βD  are  disordered  and  not  visible  in the electron-density map.","type":"Results"},{"text":"These results seem to support that the polyproline regionis partially disordered without a binding partner, suggesting it is intrinsically flexible.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-12-07T13:50:36.412Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":178,"region_id":"DP00048r011","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling. <i> Arold S, Franken P, Strub MP, Hoh F, Benichou S, Benarous R, Dumas C. </i> Structure, 1997","term_id":"IDPO:0000002","curator_id":"esalladini","start":149,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"9351809","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1AVV"}],"term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"The  N-terminal  region  from  residue  58  to  the polyproline  motif,  and  the  loop  (residues  149–178)  connecting  strands  βC–βD  are  disordered  and  not  visible  in the electron-density map.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-12-07T13:50:37.748Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":178,"term_name":"flexible linker","start":149,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"9351809","version":4,"reference_html":"The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling. <i> Arold S, Franken P, Strub MP, Hoh F, Benichou S, Benarous R, Dumas C. </i> Structure, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006220","region_id":"DP00048r012","cross_refs":[{"db":"PDB","id":"1AVZ"},{"db":"PDB","id":"1AVV"}],"curator_orcid":"0000-0002-5152-5953","statement":[{"text":" The  N-terminal  region  from  residue  58  to  the polyproline  motif,  and  the  loop  (residues  149–178)  connecting  strands  βC–βD  are  disordered  and  not  visible  in the electron-density map. ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-12-07T13:50:51.200Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":54,"end":70,"reference_id":"8681387","reference_source":"pmid","reference_html":"Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain. <i> Lee CH, Saksela K, Mirza UA, Chait BT, Kuriyan J. </i> Cell, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1EFN"}],"region_id":"DP00048r026","statement":[{"text":"Two regions of Nef core are disordered in the crystal and are not modeled: the N-terminal 16 residues and 29 residues in a large internal loop (residues 149–177) that is distant from the SH3-binding surface.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-12-07T13:50:42.332Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":149,"end":177,"reference_id":"8681387","reference_source":"pmid","reference_html":"Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain. <i> Lee CH, Saksela K, Mirza UA, Chait BT, Kuriyan J. </i> Cell, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1EFN"}],"region_id":"DP00048r027","statement":[{"text":"Two regions of Nef core are disordered in the crystal and are not modeled: the N-terminal 16 residues and 29 residues in a large internal loop (residues 149–177) that is distant from the SH3-binding surface.","type":"Results"},{"text":"The disordered loop (residues 149–178) between βC and βD is indicated as a dotted line.","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-12-07T13:50:46.400Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":71,"end":77,"reference_id":"9351809","reference_source":"pmid","reference_html":"The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling. <i> Arold S, Franken P, Strub MP, Hoh F, Benichou S, Benarous R, Dumas C. </i> Structure, 1997","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"1AVZ"}],"interaction_partner":[{"db":"UniProt","id":"P06241","partner_start":null,"partner_end":null}],"region_id":"DP00048r028","statement":[{"text":"Comparison of the bound and unbound Nef structures revealed that a proline-rich motif (Pro-x-x-Pro), which is implicated in SH3 binding, is partially disordered in the absence of the binding partner; this motif only fully adopts a left-handed polyproline type II helix conformation upon complex formation with the Fyn SH3 domain.","type":"Abstract"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-12-07T13:50:47.815Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":71,"end":77,"reference_id":"9351809","reference_source":"pmid","reference_html":"The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling. <i> Arold S, Franken P, Strub MP, Hoh F, Benichou S, Benarous R, Dumas C. </i> Structure, 1997","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0017124","term_name":"SH3 domain binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"1AVZ"}],"region_id":"DP00048r029","statement":[{"text":"Comparison of the bound and unbound Nef structures revealed that a proline-rich motif (Pro-x-x-Pro), which is implicated in SH3 binding, is partially disordered in the absence of the binding partner; this motif only fully adopts a left-handed polyproline type II helix conformation upon complex formation with the Fyn SH3 domain.","type":"Abstract"},{"text":"It is the SH3 domain that restrains its flexibility and stabilizes the PPII helix conformation upon complex formation.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-12-07T13:50:54.865Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins.\" [GOC:go_curators, Pfam:PF00018]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":71,"end":77,"reference_id":"9351809","reference_source":"pmid","reference_html":"The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling. <i> Arold S, Franken P, Strub MP, Hoh F, Benichou S, Benarous R, Dumas C. </i> Structure, 1997","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"GO:0019058","term_name":"viral life cycle","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"1AVZ"},{"db":"PDB","id":"1AVV"}],"region_id":"DP00048r030","statement":[{"text":"Recent genetic and biochemical studies [20] have shown that Nef blocks a receptor-proximal event in the TCR/CD3 pathway, and that this effect is mediated by the interaction of Nef with a specific SH3 domain present in the TCR complex. Combined with these experiments, our structural data support the identification of Fyn SH3 as the candidate target of Nef in T cells and strengthen the hypothesis that the complex of Nef with the wild-type Fyn kinase forms in vivo. Aberrant TCR-mediated signaling may involve dysfunctional regulation of Fyn by Nef.","type":"Discussion"},{"text":"The interaction of Nef with the TCR machinery is likely to be critical for AIDS pathogenesis. The resulting alteration in the T-cell activation status and perturbations in TCR-mediated signaling may lead to an increase in virus production and contribute to the immune unresponsiveness of infected T cells.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T12:50:56.135Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A set of processes which all viruses follow to ensure survival; includes attachment and entry of the virus particle, decoding of genome information, translation of viral mRNA by host ribosomes, genome replication, and assembly and release of viral particles containing the genome.\" [ISBN:1555811272]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":71,"end":77,"reference_id":"8681387","reference_source":"pmid","reference_html":"Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain. <i> Lee CH, Saksela K, Mirza UA, Chait BT, Kuriyan J. </i> Cell, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"1EFN"}],"interaction_partner":[{"db":"UniProt","id":"P06241","partner_start":null,"partner_end":null}],"region_id":"DP00048r031","statement":[{"text":"Residues 71–77 of Nef form a left-handed PP-II helix that spans the strictly conserved PxxP motif. The PP-II helix has side chains emanating in three directions, two of which are utilized for interactions with the SH3 domain (Figure 4).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T10:54:25.264Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P03406","date":"2016-08-23T18:28:12.000Z","acc":"P03406","name":"Protein Nef","length":206,"organism":"Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI)","dataset":["Viral proteins"],"UniParc":"UPI00000000E3","genes":[{"name":{"value":"nef","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04078","url":"https://hamap.expasy.org/unirule/MF_04078"}}]}}],"disorder_content":0.2621359223300971,"disprot_consensus":{"full":[{"start":54,"end":77,"type":"D"},{"start":149,"end":178,"type":"D"}],"Structural state":[{"start":54,"end":77,"type":"D"},{"start":149,"end":178,"type":"D"}],"Disorder function":[{"start":149,"end":178,"type":"F"}],"Molecular function":[{"start":71,"end":77,"type":"F"}],"Biological process":[{"start":71,"end":77,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01530","name":"Zinc finger, C2HC type","start":31,"end":58},{"id":"PF01530","name":"Zinc finger, C2HC type","start":504,"end":530},{"id":"PF01530","name":"Zinc finger, C2HC type","start":548,"end":576},{"id":"PF01530","name":"Zinc finger, C2HC type","start":903,"end":931},{"id":"PF01530","name":"Zinc finger, C2HC type","start":952,"end":980},{"id":"PF01530","name":"Zinc finger, C2HC type","start":1006,"end":1033},{"id":"PF08474","name":"Myelin transcription factor 1","start":620,"end":871}]},"uniref50":"UniRef50_P97500","sequence":"MDVDAEEKRHRTRSKGVRVPVEPAIQELFSCPTPGCDGSGHVSGKYARHRSVYGCPLAKKRKTQDKQPQEPAPKRKPFAVKADSSSVDECYESDGTEDMDDKEEDDDEEFSEDNDEQGDDDDEDEVDREDEEEIEEEDDEDDEDDDDGDDVEEEEDDDDEEEEEEEEEEENEDHQMSCTRIMQDPEKDDNNNDEYDNYDELVAKSLLNLGKIAEDAAYRARTESEMNSNTSNSLEDDSDKNENLGRKSELSLDLDSDVVRETVDSLKLLAQGHGVVLSENISDRSYAEGMSQQDSRNMNYVMLGKPMNNGLMEKMVEESDEEVCLSSLECLRNQCFDLARKLSETNPQDRSQPPNMSVRQHVRQEDDFPGRTPDRSYSDMMNLMRLEEQLSPRSRTFSSCAKEDGCHERDDDTTSVNSDRSEEVFDMTKGNLTLLEKAIALETERAKAMREKMAMDAGRRDNLRSYEDQSPRQLAGEDRKSKSSDSHVKKPYYDPSRTEKRESKCPTPGCDGTGHVTGLYPHHRSLSGCPHKDRVPPEILAMHENVLKCPTPGCTGRGHVNSNRNSHRSLSGCPIAAAEKLAKAQEKHQSCDVSKSNQASDRVLRPMCFVKQLEIPQYGYRNNVPTTTPRSNLAKELEKYSKTSFEYNSYDNHTYGKRAIAPKVQTRDISPKGYDDAKRYCKNASPSSSTTSSYAPSSSSNLSCGGGSSASSTCSKSSFDYTHDMEAAHMAATAILNLSTRCREMPQNLSTKPQDLCTARNPDMEVDENGTLDLSMNKQRPRDSCCPVLTPLEPMSPQQQAVMSSRCFQLSEGDCWDLPVDYTKMKPRRVDEEDPKEITPEDLDPFQEALEERRYPGEVTIPSPKPKYPQCKESKKDLITLSGCPLADKSIRSMLATSSQELKCPTPGCDGSGHITGNYASHRSLSGCPRAKKSGIRIAQSKEDKEDQEPIRCPVPGCDGQGHITGKYASHRSASGCPLAAKRQKDGYLNGSQFSWKSVKTEGMSCPTPGCDGSGHVSGSFLTHRSLSGCPRATSAMKKAKLSGEQMLTIKQRASNGIENDEEIKQLDEEIKELNESNSQMEADMIKLRTQVTITTMESNLKTIEEENKVIEQQNESLLHELANLSQSLIHSLANIQLPHMDPINEQNFDAYVTTLTEMYTNQDRYQSPENKALLENIKQAVRGIQV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_P97500-2","disprot_id":"DP00049","ncbi_taxon_id":10116,"regions_counter":17,"creator":"amonzon","regions":[{"start":487,"end":606,"reference_id":"10606515","reference_source":"pmid","reference_html":"Metal and DNA binding properties of a two-domain fragment of neural zinc finger factor 1, a CCHC-type zinc binding protein. <i> Berkovits HJ, Berg JM. </i> Biochemistry, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00049r006","statement":[{"text":"Proteolytic cleavage of NZF-1a in the absence of zinc initially produced multiple bands. By 60 min the protein was completely digested.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-15T10:08:56.969Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":487,"end":606,"reference_id":"10606515","reference_source":"pmid","reference_html":"Metal and DNA binding properties of a two-domain fragment of neural zinc finger factor 1, a CCHC-type zinc binding protein. <i> Berkovits HJ, Berg JM. </i> Biochemistry, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00049r007","statement":[{"text":"Titration of zinc(II) into the apoprotein led to dispersion of these resonances, indicative of structure formation.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-15T10:09:40.381Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":487,"end":606,"reference_id":"10606515","reference_source":"pmid","reference_html":"Metal and DNA binding properties of a two-domain fragment of neural zinc finger factor 1, a CCHC-type zinc binding protein. <i> Berkovits HJ, Berg JM. </i> Biochemistry, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0007731","ec_ontology":"ECO","ec_name":"spectrometry evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00049r008","statement":[{"text":"These observations support a CysCysHisCys ligand configuration for the NZF1-type zinc binding domains, indicating that one of the conserved histidines is involved in metal ion binding whereas the other plays some other as-yet-undetermined role.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-07T19:05:55.639Z"}},{"start":487,"end":606,"reference_id":"10606515","reference_source":"pmid","reference_html":"Metal and DNA binding properties of a two-domain fragment of neural zinc finger factor 1, a CCHC-type zinc binding protein. <i> Berkovits HJ, Berg JM. </i> Biochemistry, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00049r009","statement":[{"text":"Metal-stabilized structured regions were identified by partial proteolysis and examined for binding to the β-retinoic acid response element (β-RARE).","type":"Abstract"},{"text":"In the presence of zinc, multiple bands were observed at early time points. By 1 h, the major products were two fragments of approximately 10 kDa each. These were stable for up to 3 h of digestion.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-07T18:18:47.242Z"}},{"start":487,"end":606,"reference_id":"10606515","reference_source":"pmid","reference_html":"Metal and DNA binding properties of a two-domain fragment of neural zinc finger factor 1, a CCHC-type zinc binding protein. <i> Berkovits HJ, Berg JM. </i> Biochemistry, 1999","date":"2022-03-08T15:09:21.400Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005631","ec_ontology":"ECO","ec_name":"DNAse footprinting evidence used in manual assertion","released":"2022_03","version":4,"region_id":"DP00049r010","statement":[{"text":"DNase I footprinting was used to further characterize the DNA binding site.","type":"Abstract"},{"text":"Gel shift analysis with the β-RARE DNA binding site showed that both fragments are functional DNA binding domains.","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"NCBIgene","id":"5915","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-07T19:05:45.169Z"}},{"start":487,"end":606,"reference_id":"10606515","reference_source":"pmid","reference_html":"Metal and DNA binding properties of a two-domain fragment of neural zinc finger factor 1, a CCHC-type zinc binding protein. <i> Berkovits HJ, Berg JM. </i> Biochemistry, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0008270","term_name":"zinc ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007731","ec_ontology":"ECO","ec_name":"spectrometry evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00049r011","statement":[{"text":"These observations support a CysCysHisCys ligand configuration for the NZF1-type zinc binding domains, indicating that one of the conserved histidines is involved in metal ion binding whereas the other plays some other as-yet-undetermined role.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-07T19:05:45.481Z"}},{"start":487,"end":606,"reference_id":"10606515","reference_source":"pmid","reference_html":"Metal and DNA binding properties of a two-domain fragment of neural zinc finger factor 1, a CCHC-type zinc binding protein. <i> Berkovits HJ, Berg JM. </i> Biochemistry, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0008270","term_name":"zinc ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00049r012","statement":[{"text":"The cobalt(II) and zinc(II) binding properties of the metal binding domains were investigated, and zinc-induced protein folding was observed by 1H NMR.","type":"Abstract"},{"text":"Titration of zinc(II) into the apoprotein led to dispersion of these resonances, indicative of structure formation.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-07T19:05:46.818Z"}},{"start":487,"end":606,"reference_id":"10606515","reference_source":"pmid","reference_html":"Metal and DNA binding properties of a two-domain fragment of neural zinc finger factor 1, a CCHC-type zinc binding protein. <i> Berkovits HJ, Berg JM. </i> Biochemistry, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0008270","term_name":"zinc ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00049r013","statement":[{"text":"Metal-stabilized structured regions were identified by partial proteolysis and examined for binding to the β-retinoic acid response element (β-RARE).","type":"Abstract"},{"text":"In the presence of zinc, multiple bands were observed at early time points. By 1 h, the major products were two fragments of approximately 10 kDa each. These were stable for up to 3 h of digestion.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-07T19:05:47.862Z"}},{"start":487,"end":606,"reference_id":"10606515","reference_source":"pmid","reference_html":"Metal and DNA binding properties of a two-domain fragment of neural zinc finger factor 1, a CCHC-type zinc binding protein. <i> Berkovits HJ, Berg JM. </i> Biochemistry, 1999","date":"2022-12-06T10:24:27.430Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140487","term_name":"metal ion sequestering activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","released":"2022_12","version":4,"region_id":"DP00049r014","statement":[{"text":"Metal-stabilized structured regions were identified by partial proteolysis and examined for binding to the β-retinoic acid response element (β-RARE).","type":"Abstract"},{"text":"In the presence of zinc, multiple bands were observed at early time points. By 1 h, the major products were two fragments of approximately 10 kDa each. These were stable for up to 3 h of digestion.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a metal ion to prevent it from interacting with sensitive components of a biological system.\" [PMID:12050156]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-06T12:47:44.109Z"}},{"start":487,"end":606,"reference_id":"10606515","reference_source":"pmid","reference_html":"Metal and DNA binding properties of a two-domain fragment of neural zinc finger factor 1, a CCHC-type zinc binding protein. <i> Berkovits HJ, Berg JM. </i> Biochemistry, 1999","date":"2022-12-06T10:24:37.873Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140487","term_name":"metal ion sequestering activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007731","ec_ontology":"ECO","ec_name":"spectrometry evidence used in manual assertion","released":"2022_12","version":4,"region_id":"DP00049r015","statement":[{"text":"These observations support a CysCysHisCys ligand configuration for the NZF1-type zinc binding domains, indicating that one of the conserved histidines is involved in metal ion binding whereas the other plays some other as-yet-undetermined role.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a metal ion to prevent it from interacting with sensitive components of a biological system.\" [PMID:12050156]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-06T12:47:45.398Z"}},{"start":487,"end":606,"reference_id":"10606515","reference_source":"pmid","reference_html":"Metal and DNA binding properties of a two-domain fragment of neural zinc finger factor 1, a CCHC-type zinc binding protein. <i> Berkovits HJ, Berg JM. </i> Biochemistry, 1999","date":"2022-12-06T10:24:50.362Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140487","term_name":"metal ion sequestering activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","released":"2022_12","version":4,"region_id":"DP00049r016","statement":[{"text":"The cobalt(II) and zinc(II) binding properties of the metal binding domains were investigated, and zinc-induced protein folding was observed by 1H NMR.","type":"Abstract"},{"text":"Titration of zinc(II) into the apoprotein led to dispersion of these resonances, indicative of structure formation.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a metal ion to prevent it from interacting with sensitive components of a biological system.\" [PMID:12050156]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-06T12:47:45.648Z"}},{"start":90,"end":172,"reference_id":"https://mobidb.org/P70475","reference_source":"mobidb","reference_html":"An Entry Referenced from MobiDB","date":"2022-02-14T09:00:00.000Z","curator_id":"amonzon","curator_name":"Alex Monzon","curator_orcid":"0000-0003-0362-8218","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007759","ec_ontology":"ECO","ec_name":"curator inference from database used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00049r017","statement":[{"text":"This poly-E region is inferred by the curator to be disordered, based on MobiDB-Lite and according to experimental evidence demonstrating that poly-E repeats display random-coil-like conformation (PMID:16949547)","type":"Curator statement"}],"ec_go":"IC","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P70475","date":"2016-08-11T12:36:25.000Z","acc":"P70475","name":"Myelin transcription factor 1-like protein","length":1187,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI00000E86A7","genes":[{"name":{"value":"Myt1l"},"synonyms":[{"value":"Nzf1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8631881","url":"http://www.ncbi.nlm.nih.gov/pubmed/8631881","alternativeUrl":"https://europepmc.org/abstract/MED/8631881"}}]}]}],"alphafold_very_low_content":0.548441449031171,"disorder_content":0.17101937657961247,"disprot_consensus":{"full":[{"start":90,"end":172,"type":"D"},{"start":487,"end":606,"type":"T"}],"Structural state":[{"start":90,"end":172,"type":"D"},{"start":487,"end":606,"type":"D"}],"Structural transition":[{"start":487,"end":606,"type":"T"}],"Molecular function":[{"start":487,"end":606,"type":"F"}]}},{"acc":"P07805","sequence":"MDIVVNDDLSCRFLEGFNTRDALCKKISMNTCDEGDPFFVADLGDIVRKHETWKKCLPRVTPFYAVKCNDDWRVLGTLAALGTGFDCASNTEIQRVRGIGVPPEKIIYANPCKQISHIRYARDSGVDVMTFDCVDELEKVAKTHPKAKMVLRISTDDSLARCRLSVKFGAKVEDCRFILEQAKKLNIDVTGVSFHVGSGSTDASTFAQAISDSRFVFDMGTELGFNMHILDIGGGFPGTRDAPLKFEEIAGVINNALEKHFPPDLKLTIVAEPGRYYVASAFTLAVNVIAKKVTPGVQTDVGAHAESNAQSFMYYVNDGVYGSFNCILYDHAVVRPLPQREPIPNEKLYPSSVWGPTCDGLDQIVERYYLPEMQVGEWLLFEDMGAYTVVGTSSFNGFQSPTIYYVVSGLPDHVVRELKSQKS","alphafold_very_low_content":"0.0425531914893617","creator":"mnecci","dataset":["Neglected tropical diseases proteins"],"date":"2016-09-12T11:48:04.000Z","disprot_id":"DP00051","features":{"pfam":[{"id":"PF02784","name":"Pyridoxal-dependent decarboxylase, pyridoxal binding domain","start":43,"end":279}],"gene3D":[{"start":17,"end":399,"id":"2.40.37.10","name":"Lyase, Ornithine Decarboxylase; Chain A, domain 1","_id":"685af523b4ac24d5329d71ad"},{"start":44,"end":277,"id":"3.20.20.10","name":"Alanine racemase","_id":"685af523b4ac24d5329d71ae"}]},"genes":[],"length":423,"name":"Ornithine decarboxylase","ncbi_taxon_id":5702,"organism":"Trypanosoma brucei brucei","regions_counter":10,"released":"2016_10","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Trypanosoma"],"UniParc":"UPI0000128FF5","uniref100":"UniRef100_P07805","uniref50":"UniRef50_P00860","uniref90":"UniRef90_P07805","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2TOD","_id":"685af523b4ac24d5329d71c4"},{"db":"PDB","id":"1QU4","_id":"685af523b4ac24d5329d71c5"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-17T10:55:53.478Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":32,"interaction_partner":[],"reference_html":"X-ray structure of ornithine decarboxylase from Trypanosoma brucei: the native structure and the structure in complex with alpha-difluoromethylornithine. <i> Grishin NV, Osterman AL, Brooks HB, Phillips MA, Goldsmith EJ. </i> Biochemistry, 1999","reference_id":"10563800","region_id":"DP00051r006","released":"2022_03","sample":[],"sequence_construct":"GAMDIVVNDDLSCRFLEGFNTRDALCKKISMNTCDEGDPFFVADLGDIVRKHETWKKCLPRVTPFYAVKCNDDWRVLGTLAALGTGFDCASNTEIQRVRGIGVPPEKIIYANPCKQISHIRYARDSGVDVMTFDCVDELEKVAKTHPKAKMVLRISTDDSLARCRLSVKFGAKVEDCRFILEQAKKLNIDVTGVSFHVGSGSTDASTFAQAISDSRFVFDMGTELGFNMHILDIGGGFPGTRDAPLKFEEIAGVINNALEKHFPPDLKLTIVAEPGRYYVASAFTLAVNVIAKKVTPGVQTDVGAHAESNAQSFMYYVNDGVYGSFNCILYDHAVVRPLPQREPIPNEKLYPSSVWGPTCDGLDQIVERYYLPEMQVGEWLLFEDMGAYTVVGTSSFNGFQSPTIYYVVSGLPDHVVRELKSQKS","statement":[{"type":"Results","text":"Although the electron density map for most of the residues is unambiguous, 70 residues could not be interpreted. These regions include the N-terminus (residues 1−35), the C-terminus (residues 412−425), and two loops (residues 158−165 and 298−310).","_id":"685af523b4ac24d5329d71c6"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-07T18:18:31.651Z","_id":"685af523b4ac24d5329d71c7"},"version":0,"_id":"685af523b4ac24d5329d71c3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2TOD","_id":"685af523b4ac24d5329d71c9"},{"db":"PDB","id":"1QU4","_id":"685af523b4ac24d5329d71ca"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-17T10:58:18.375Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":296,"end":308,"interaction_partner":[],"reference_html":"X-ray structure of ornithine decarboxylase from Trypanosoma brucei: the native structure and the structure in complex with alpha-difluoromethylornithine. <i> Grishin NV, Osterman AL, Brooks HB, Phillips MA, Goldsmith EJ. </i> Biochemistry, 1999","reference_id":"10563800","region_id":"DP00051r007","released":"2022_03","sample":[],"sequence_construct":"GAMDIVVNDDLSCRFLEGFNTRDALCKKISMNTCDEGDPFFVADLGDIVRKHETWKKCLPRVTPFYAVKCNDDWRVLGTLAALGTGFDCASNTEIQRVRGIGVPPEKIIYANPCKQISHIRYARDSGVDVMTFDCVDELEKVAKTHPKAKMVLRISTDDSLARCRLSVKFGAKVEDCRFILEQAKKLNIDVTGVSFHVGSGSTDASTFAQAISDSRFVFDMGTELGFNMHILDIGGGFPGTRDAPLKFEEIAGVINNALEKHFPPDLKLTIVAEPGRYYVASAFTLAVNVIAKKVTPGVQTDVGAHAESNAQSFMYYVNDGVYGSFNCILYDHAVVRPLPQREPIPNEKLYPSSVWGPTCDGLDQIVERYYLPEMQVGEWLLFEDMGAYTVVGTSSFNGFQSPTIYYVVSGLPDHVVRELKSQKS","statement":[{"type":"Results","text":"Although the electron density map for most of the residues is unambiguous, 70 residues could not be interpreted. These regions include the N-terminus (residues 1−35), the C-terminus (residues 412−425), and two loops (residues 158−165 and 298−310).","_id":"685af523b4ac24d5329d71cb"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-07T17:32:31.433Z","_id":"685af523b4ac24d5329d71cc"},"version":0,"_id":"685af523b4ac24d5329d71c8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2TOD","_id":"685af523b4ac24d5329d71ce"},{"db":"PDB","id":"1QU4","_id":"685af523b4ac24d5329d71cf"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-17T11:00:20.553Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":410,"end":423,"interaction_partner":[],"reference_html":"X-ray structure of ornithine decarboxylase from Trypanosoma brucei: the native structure and the structure in complex with alpha-difluoromethylornithine. <i> Grishin NV, Osterman AL, Brooks HB, Phillips MA, Goldsmith EJ. </i> Biochemistry, 1999","reference_id":"10563800","region_id":"DP00051r008","released":"2022_03","sample":[],"sequence_construct":"GAMDIVVNDDLSCRFLEGFNTRDALCKKISMNTCDEGDPFFVADLGDIVRKHETWKKCLPRVTPFYAVKCNDDWRVLGTLAALGTGFDCASNTEIQRVRGIGVPPEKIIYANPCKQISHIRYARDSGVDVMTFDCVDELEKVAKTHPKAKMVLRISTDDSLARCRLSVKFGAKVEDCRFILEQAKKLNIDVTGVSFHVGSGSTDASTFAQAISDSRFVFDMGTELGFNMHILDIGGGFPGTRDAPLKFEEIAGVINNALEKHFPPDLKLTIVAEPGRYYVASAFTLAVNVIAKKVTPGVQTDVGAHAESNAQSFMYYVNDGVYGSFNCILYDHAVVRPLPQREPIPNEKLYPSSVWGPTCDGLDQIVERYYLPEMQVGEWLLFEDMGAYTVVGTSSFNGFQSPTIYYVVSGLPDHVVRELKSQKS","statement":[{"type":"Results","text":"Although the electron density map for most of the residues is unambiguous, 70 residues could not be interpreted. These regions include the N-terminus (residues 1−35), the C-terminus (residues 412−425), and two loops (residues 158−165 and 298−310).","_id":"685af523b4ac24d5329d71d0"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-07T17:32:30.536Z","_id":"685af523b4ac24d5329d71d1"},"version":0,"_id":"685af523b4ac24d5329d71cd","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2TOD","_id":"685af523b4ac24d5329d71d3"},{"db":"PDB","id":"1QU4","_id":"685af523b4ac24d5329d71d4"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-17T11:00:36.602Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":410,"end":423,"interaction_partner":[],"reference_html":"X-ray structure of ornithine decarboxylase from Trypanosoma brucei: the native structure and the structure in complex with alpha-difluoromethylornithine. <i> Grishin NV, Osterman AL, Brooks HB, Phillips MA, Goldsmith EJ. </i> Biochemistry, 1999","reference_id":"10563800","region_id":"DP00051r009","released":"2022_03","sample":[],"sequence_construct":"GAMDIVVNDDLSCRFLEGFNTRDALCKKISMNTCDEGDPFFVADLGDIVRKHETWKKCLPRVTPFYAVKCNDDWRVLGTLAALGTGFDCASNTEIQRVRGIGVPPEKIIYANPCKQISHIRYARDSGVDVMTFDCVDELEKVAKTHPKAKMVLRISTDDSLARCRLSVKFGAKVEDCRFILEQAKKLNIDVTGVSFHVGSGSTDASTFAQAISDSRFVFDMGTELGFNMHILDIGGGFPGTRDAPLKFEEIAGVINNALEKHFPPDLKLTIVAEPGRYYVASAFTLAVNVIAKKVTPGVQTDVGAHAESNAQSFMYYVNDGVYGSFNCILYDHAVVRPLPQREPIPNEKLYPSSVWGPTCDGLDQIVERYYLPEMQVGEWLLFEDMGAYTVVGTSSFNGFQSPTIYYVVSGLPDHVVRELKSQKS","statement":[{"type":"Results","text":"Although the electron density map for most of the residues is unambiguous, 70 residues could not be interpreted. These regions include the N-terminus (residues 1−35), the C-terminus (residues 412−425), and two loops (residues 158−165 and 298−310).","_id":"685af523b4ac24d5329d71d5"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-07T17:32:37.657Z","_id":"685af523b4ac24d5329d71d6"},"version":0,"_id":"685af523b4ac24d5329d71d2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2TOD","_id":"685af523b4ac24d5329d71d8"},{"db":"PDB","id":"1QU4","_id":"685af523b4ac24d5329d71d9"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-09-16T08:06:24.605Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":32,"interaction_partner":[],"reference_html":"X-ray structure of ornithine decarboxylase from Trypanosoma brucei: the native structure and the structure in complex with alpha-difluoromethylornithine. <i> Grishin NV, Osterman AL, Brooks HB, Phillips MA, Goldsmith EJ. </i> Biochemistry, 1999","reference_id":"10563800","region_id":"DP00051r010","released":"2024_12","sample":[],"sequence_construct":"GAMDIVVNDDLSCRFLEGFNTRDALCKKISMNTCDEGDPFFVADLGDIVRKHETWKKCLPRVTPFYAVKCNDDWRVLGTLAALGTGFDCASNTEIQRVRGIGVPPEKIIYANPCKQISHIRYARDSGVDVMTFDCVDELEKVAKTHPKAKMVLRISTDDSLARCRLSVKFGAKVEDCRFILEQAKKLNIDVTGVSFHVGSGSTDASTFAQAISDSRFVFDMGTELGFNMHILDIGGGFPGTRDAPLKFEEIAGVINNALEKHFPPDLKLTIVAEPGRYYVASAFTLAVNVIAKKVTPGVQTDVGAHAESNAQSFMYYVNDGVYGSFNCILYDHAVVRPLPQREPIPNEKLYPSSVWGPTCDGLDQIVERYYLPEMQVGEWLLFEDMGAYTVVGTSSFNGFQSPTIYYVVSGLPDHVVRELKSQKS","statement":[{"type":"Results","text":"Although the electron density map for most of the residues is unambiguous, 70 residues could not be interpreted. These regions include the N-terminus (residues 1−35), the C-terminus (residues 412−425), and two loops (residues 158−165 and 298−310).","_id":"685af523b4ac24d5329d71da"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":1,"_id":"685af523b4ac24d5329d71d7","reference_source":"pmid"}],"__v":0,"disorder_content":0.13947990543735225,"disprot_consensus":{"full":[{"start":1,"end":32,"type":"D"},{"start":296,"end":308,"type":"D"},{"start":410,"end":423,"type":"D"}],"Structural state":[{"start":1,"end":32,"type":"D"},{"start":296,"end":308,"type":"D"},{"start":410,"end":423,"type":"D"}],"Disorder function":[{"start":1,"end":32,"type":"F"},{"start":410,"end":423,"type":"F"}]}},{"acc":"P27001","sequence":"MLEEALAAIQNARDLEELKALKARYLGKKGLLTQEMKGLSALPLEERRKRGQELNAIKAALEAALEAREKALEEAALKEALERERVDVSLPGASLFSGGLHPITLMERELVEIFRALGYQAVEGPEVESEFFNFDALNIPEHHPARDMWDTFWLTGEGFRLEGPLGEEVEGRLLLRTHTSPMQVRYMVAHTPPFRIVVPGRVFRFEQTDATHEAVFHQLEGLVVGEGIAMAHLKGAIYELAQALFGPDSKVRFQPVYFPFVEPGAQFAVWWPEGGKWLELGGAGMVHPKVFQAVDAYRERLGLPPAYRGVTGFAFGLGVERLAMLRYGIPDIRYFFGGRLKFLEQFKGVL","alphafold_very_low_content":"0.002857142857142857","creator":"mnecci","dataset":["RNA-binding proteins"],"date":"2016-08-23T19:24:53.000Z","disprot_id":"DP00053","features":{"pfam":[{"id":"PF01409","name":"tRNA synthetases class II core domain (F)","start":86,"end":346},{"id":"PF02912","name":"Aminoacyl tRNA synthetase class II, N-terminal domain","start":14,"end":81}],"gene3D":[{"start":1,"end":350,"id":"3.30.930.10","name":"Bira Bifunctional Protein; Domain 2","_id":"685af523b4ac24d5329d71dd"}]},"genes":[{"name":{"value":"pheS","evidences":[],"_id":"685af523b4ac24d5329d71fb"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d71fa"}],"length":350,"name":"Phenylalanine--tRNA ligase alpha subunit","ncbi_taxon_id":274,"organism":"Thermus thermophilus","regions_counter":6,"released":"2016_10","taxonomy":["Bacteria","Deinococcus-Thermus","Deinococci","Thermales","Thermaceae","Thermus"],"UniParc":"UPI00001107A3","uniref100":"UniRef100_Q5SGX2","uniref50":"UniRef50_Q5SGX2","uniref90":"UniRef90_Q5SGX2","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":101,"interaction_partner":[],"reference_html":"The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate tRNAPhe. <i> Goldgur Y, Mosyak L, Reshetnikova L, Ankilova V, Lavrik O, Khodyreva S, Safro M. </i> Structure, 1997","reference_id":"9016717","region_id":"DP00053r001","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The sequence from Thermus thermophilus HB8 described in this article (Q5SGX2) is 100% identical to P27001.","_id":"685af523b4ac24d5329d71df"},{"type":"Results","text":"The most pronounced difference between the two states is the ordering of the N-terminal region of the α subunit, which appeared to comprise a coiled-coil structure (helical arm). The helices stretch out into the solvent by 65 Å and are apparently flexible in the absence of intermolecular contacts.","_id":"685af523b4ac24d5329d71e0"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-07T21:46:17.334Z","_id":"685af523b4ac24d5329d71e1"},"version":3,"_id":"685af523b4ac24d5329d71de","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1EIY","_id":"685af523b4ac24d5329d71e3"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":101,"interaction_partner":[],"reference_html":"The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate tRNAPhe. <i> Goldgur Y, Mosyak L, Reshetnikova L, Ankilova V, Lavrik O, Khodyreva S, Safro M. </i> Structure, 1997","reference_id":"9016717","region_id":"DP00053r002","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The sequence from Thermus thermophilus HB8 described in this article (Q5SGX2) is 100% identical to P27001.","_id":"685af523b4ac24d5329d71e4"},{"type":"Results","text":"The most pronounced difference between the two states is the ordering of the N-terminal region of the α subunit, which appeared to comprise a coiled-coil structure (helical arm). The helices stretch out into the solvent by 65 Å and are apparently flexible in the absence of intermolecular contacts.","_id":"685af523b4ac24d5329d71e5"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-07T21:46:13.407Z","_id":"685af523b4ac24d5329d71e6"},"version":3,"_id":"685af523b4ac24d5329d71e2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1PYS","_id":"685af523b4ac24d5329d71ed"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":84,"interaction_partner":[],"reference_html":"Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus. <i> Mosyak L, Reshetnikova L, Goldgur Y, Delarue M, Safro MG. </i> Nat Struct Biol, 1995","reference_id":"7664121","region_id":"DP00053r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Residues 1-84 from the amino-terminus of the α-subunit are disordered and were not detected in the electron density maps.","_id":"685af523b4ac24d5329d71ee"},{"type":"Curator statement","text":"The sequence from Thermus thermophilus HB8 described in this article (Q5SGX2) is 100% identical to P27001.","_id":"685af523b4ac24d5329d71ef"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-07T19:12:08.815Z","_id":"685af523b4ac24d5329d71f0"},"version":3,"_id":"685af523b4ac24d5329d71ec","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":84,"interaction_partner":[],"reference_html":"Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus. <i> Mosyak L, Reshetnikova L, Goldgur Y, Delarue M, Safro MG. </i> Nat Struct Biol, 1995","reference_id":"7664121","region_id":"DP00053r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Residues 1-84 from the amino-terminus of the α-subunit are disordered and were not detected in the electron density maps.","_id":"685af523b4ac24d5329d71f2"},{"type":"Curator statement","text":"The sequence from Thermus thermophilus HB8 described in this article (Q5SGX2) is 100% identical to P27001.","_id":"685af523b4ac24d5329d71f3"}],"states_connection":[],"term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-07T21:46:11.932Z","_id":"685af523b4ac24d5329d71f4"},"version":4,"_id":"685af523b4ac24d5329d71f1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1EIY","_id":"685af523b4ac24d5329d71f6"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":101,"interaction_partner":[],"reference_html":"The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate tRNAPhe. <i> Goldgur Y, Mosyak L, Reshetnikova L, Ankilova V, Lavrik O, Khodyreva S, Safro M. </i> Structure, 1997","reference_id":"9016717","region_id":"DP00053r006","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The sequence from Thermus thermophilus HB8 described in this article (Q5SGX2) is 100% identical to P27001.","_id":"685af523b4ac24d5329d71f7"},{"type":"Results","text":"The most pronounced difference between the two states is the ordering of the N-terminal region of the α subunit, which appeared to comprise a coiled-coil structure (helical arm). The helices stretch out into the solvent by 65 Å and are apparently flexible in the absence of intermolecular contacts.","_id":"685af523b4ac24d5329d71f8"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a transfer RNA.\" [GOC:ai]","term_go_domain":"F","term_id":"GO:0000049","term_is_binding":true,"term_is_obsolete":false,"term_name":"tRNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-07T21:46:15.387Z","_id":"685af523b4ac24d5329d71f9"},"version":1,"_id":"685af523b4ac24d5329d71f5","reference_source":"pmid"}],"__v":0,"disorder_content":0.2885714285714286,"disprot_consensus":{"full":[{"start":1,"end":101,"type":"T"}],"Structural state":[{"start":1,"end":101,"type":"D"}],"Structural transition":[{"start":1,"end":101,"type":"T"}],"Disorder function":[{"start":1,"end":84,"type":"F"}],"Molecular function":[{"start":1,"end":101,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01504","name":"Phosphatidylinositol-4-phosphate 5-Kinase","start":127,"end":414}],"gene3D":[{"start":204,"end":326,"id":"3.30.810.10","name":"2-Layer Sandwich"},{"start":25,"end":203,"id":"3.30.800.10","name":"Phosphatidylinositol Phosphate Kinase II Beta"},{"start":329,"end":415,"id":"3.30.810.10","name":"2-Layer Sandwich"}]},"uniref50":"UniRef50_P78356","sequence":"MSSNCTSTTAVAVAPLSASKTKTKKKHFVCQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVDRAEQEEMEVEERAEDEECENDGVGGNLLCSYGTPPDSPGNLLSFPRFFGPGEFDPSVDVYAMKSHESSPKKEVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSNILT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P78356","disprot_id":"DP00054","ncbi_taxon_id":9606,"regions_counter":5,"creator":"dpiovesan","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":33,"region_id":"DP00054r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of type IIbeta phosphatidylinositol phosphate kinase: a protein kinase fold flattened for interfacial phosphorylation. <i> Rao VD, Misra S, Boronenkov IV, Anderson RA, Hurley JH. </i> Cell, 1998","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1BO1"}],"reference_id":"9753329","statement":[{"text":"The N-terminal 33 amino acids are completely disordered.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-07T10:41:02.462Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":342,"region_id":"DP00054r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of type IIbeta phosphatidylinositol phosphate kinase: a protein kinase fold flattened for interfacial phosphorylation. <i> Rao VD, Misra S, Boronenkov IV, Anderson RA, Hurley JH. </i> Cell, 1998","term_id":"IDPO:0000002","curator_id":"fquaglia","start":304,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1BO1"}],"reference_id":"9753329","statement":[{"text":"Residues 304–342, which comprise the central portion of the highly variable insert sequence, are disordered.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-07T10:41:00.288Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":390,"region_id":"DP00054r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of type IIbeta phosphatidylinositol phosphate kinase: a protein kinase fold flattened for interfacial phosphorylation. <i> Rao VD, Misra S, Boronenkov IV, Anderson RA, Hurley JH. </i> Cell, 1998","term_id":"IDPO:0000002","curator_id":"fquaglia","start":373,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1BO1"}],"reference_id":"9753329","statement":[{"text":"Finally, the Lys- and Ala-rich loop from 373–390 is disordered. This loop connects the C terminus of β12 to the N terminus of α8, a distance of 22 Å.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-07T10:40:57.862Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P78356","date":"2016-08-12T15:08:16.000Z","acc":"P78356","name":"Phosphatidylinositol 5-phosphate 4-kinase type-2 beta","length":416,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000032D92","genes":[{"name":{"value":"PIP4K2B","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:8998","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8998"}}]},"synonyms":[{"value":"PIP5K2B"}]}],"alphafold_very_low_content":0.1346153846153846,"disorder_content":0.21634615384615385,"disprot_consensus":{"full":[{"start":1,"end":33,"type":"D"},{"start":304,"end":342,"type":"D"},{"start":373,"end":390,"type":"D"}],"Structural state":[{"start":1,"end":33,"type":"D"},{"start":304,"end":342,"type":"D"},{"start":373,"end":390,"type":"D"}]}},{"acc":"P10688","sequence":"MDSGRDFLTLHGLQDDPDLQALLKGSQLLKVKSSSWRRERFYKLQEDCKTIWQESRKVMRSPESQLFSIEDIQEVRMGHRTEGLEKFARDIPEDRCFSIVFKDQRNTLDLIAPSPADAQHWVQGLRKIIHHSGSMDQRQKLQHWIHSCLRKADKNKDNKMNFKELKDFLKELNIQVDDGYARKIFRECDHSQTDSLEDEEIETFYKMLTQRAEIDRAFEEAAGSAETLSVERLVTFLQHQQREEEAGPALALSLIERYEPSETAKAQRQMTKDGFLMYLLSADGNAFSLAHRRVYQDMDQPLSHYLVSSSHNTYLLEDQLTGPSSTEAYIRALCKGCRCLELDCWDGPNQEPIIYHGYTFTSKILFCDVLRAIRDYAFKASPYPVILSLENHCSLEQQRVMARHLRAILGPILLDQPLDGVTTSLPSPEQLKGKILLKGKKLGGLLPAGGENGSEATDVSDEVEAAEMEDEAVRSQVQHKPKEDKLKLVPELSDMIIYCKSVHFGGFSSPGTSGQAFYEMASFSESRALRLLQESGNGFVRHNVSCLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNFQTPGPEMDVYLGCFQDNGGCGYVLKPAFLRDPNTTFNSRALTQGPWWRPERLRVRIISGQQLPKVNKNKNSIVDPKVIVEIHGVGRDTGSRQTAVITNNGFNPRWDMEFEFEVTVPDLALVRFMVEDYDSSSKNDFIGQSTIPWNSLKQGYRHVHLLSKNGDQHPSATLFVKISIQD","alphafold_very_low_content":"0.01455026455026455","creator":"agasparini","dataset":[],"date":"2016-08-24T11:50:32.000Z","disprot_id":"DP00055","features":{"pfam":[{"id":"PF00168","name":"C2 domain","start":630,"end":734},{"id":"PF00387","name":"Phosphatidylinositol-specific phospholipase C, Y domain","start":492,"end":606},{"id":"PF00388","name":"Phosphatidylinositol-specific phospholipase C, X domain","start":298,"end":441},{"id":"PF09279","name":"Phosphoinositide-specific phospholipase C, efhand-like","start":204,"end":288},{"id":"PF16457","name":"Pleckstrin homology domain","start":19,"end":126}],"gene3D":[{"start":625,"end":756,"id":"2.60.40.150","name":"C2 domain","_id":"685af523b4ac24d5329d7201"},{"start":293,"end":620,"id":"3.20.20.190","name":"Phosphatidylinositol (PI) phosphodiesterase","_id":"685af523b4ac24d5329d7202"},{"start":10,"end":140,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)","_id":"685af523b4ac24d5329d7203"},{"start":208,"end":292,"id":"1.10.238.10","name":"EF-hand","_id":"685af523b4ac24d5329d7204"},{"start":158,"end":207,"id":"1.10.238.10","name":"EF-hand","_id":"685af523b4ac24d5329d7205"}]},"genes":[{"name":{"value":"Plcd1","evidences":[{"source":{"id":"3346","name":"RGD","url":"https://rgd.mcw.edu/tools/genes/genes_view.cgi?id=3346","_id":"685af523b4ac24d5329d7225"},"code":"ECO:0000312","_id":"685af523b4ac24d5329d7224"}],"_id":"685af523b4ac24d5329d7226"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d7223"}],"length":756,"name":"1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions_counter":7,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"UniParc":"UPI00000477A4","uniref100":"UniRef100_P10688","uniref50":"UniRef50_P10688","uniref90":"UniRef90_P10688","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1DJW","_id":"685af523b4ac24d5329d7216"},{"db":"PDB","id":"1DJY","_id":"685af523b4ac24d5329d7217"},{"db":"PDB","id":"1DJX","_id":"685af523b4ac24d5329d7218"},{"db":"PDB","id":"1DJZ","_id":"685af523b4ac24d5329d7219"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-17T12:28:37.363Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":133,"end":157,"interaction_partner":[],"reference_html":"Structural mapping of the catalytic mechanism for a mammalian phosphoinositide-specific phospholipase C. <i> Essen LO, Perisic O, Katan M, Wu Y, Roberts MF, Williams RL. </i> Biochemistry, 1997","reference_id":"9048554","region_id":"DP00055r006","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"Due to missing electron density, no structural model was possible for these residues.","_id":"685af523b4ac24d5329d721a"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-07T19:27:18.242Z","_id":"685af523b4ac24d5329d721b"},"version":0,"_id":"685af523b4ac24d5329d7215","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1DJW","_id":"685af523b4ac24d5329d721d"},{"db":"PDB","id":"1DJY","_id":"685af523b4ac24d5329d721e"},{"db":"PDB","id":"1DJX","_id":"685af523b4ac24d5329d721f"},{"db":"PDB","id":"1DJZ","_id":"685af523b4ac24d5329d7220"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-17T12:29:43.176Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":446,"end":483,"interaction_partner":[],"reference_html":"Structural mapping of the catalytic mechanism for a mammalian phosphoinositide-specific phospholipase C. <i> Essen LO, Perisic O, Katan M, Wu Y, Roberts MF, Williams RL. </i> Biochemistry, 1997","reference_id":"9048554","region_id":"DP00055r007","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"Due to missing electron density, no structural model was possible for these residues.","_id":"685af523b4ac24d5329d7221"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-07T19:27:20.667Z","_id":"685af523b4ac24d5329d7222"},"version":0,"_id":"685af523b4ac24d5329d721c","reference_source":"pmid"}],"__v":0,"disorder_content":0.08333333333333333,"disprot_consensus":{"full":[{"start":133,"end":157,"type":"D"},{"start":446,"end":483,"type":"D"}],"Structural state":[{"start":133,"end":157,"type":"D"},{"start":446,"end":483,"type":"D"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_P15340","sequence":"MARYRRSRTRSRSPRSRRRRRRSGRRRSPRRRRRYGSARRSRRSVGGRRRRYGSRRRRRRRY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Phasianinae","Gallus"],"uniref90":"UniRef90_P15340","disprot_id":"DP00057","ncbi_taxon_id":9031,"regions_counter":8,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":62,"region_id":"DP00057r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Conformation of the fowl protamine, galline, and its binding properties to DNA. <i> Nakano M, Kasai K, Yoshida K, Tanimoto T, Tamaki Y, Tobita T. </i> J Biochem, 1989","term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"2738040","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"CD spectra showed that the fowl protamine, galline, has an unordered structure rich in reverse turns in neutral solution.","type":"Abstract"},{"text":"In ET buffer, the spectrum had a positive peak at 224 nm besides a trough near 200 nm. The former peak is probably due to a reverse turn (β-turn) structure (19, 20) and the latter one to an unordered structure (19, 21).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-14T10:36:27.562Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":62,"term_name":"disorder to order","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"2738040","version":3,"reference_html":"Conformation of the fowl protamine, galline, and its binding properties to DNA. <i> Nakano M, Kasai K, Yoshida K, Tanimoto T, Tamaki Y, Tobita T. </i> J Biochem, 1989","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00057r004","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"Citrate ions bound specifically to the galline molecule, causing a conformational change in it.","type":"Abstract"},{"text":"In fact, [θ224] decreased with an increase in citrate concentration (Fig. 1B).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-14T10:36:28.979Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":62,"term_name":"carboxylic acid binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"2738040","version":4,"reference_html":"Conformation of the fowl protamine, galline, and its binding properties to DNA. <i> Nakano M, Kasai K, Yoshida K, Tanimoto T, Tamaki Y, Tobita T. </i> J Biochem, 1989","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0031406","ec_id":"ECO:0006204","region_id":"DP00057r006","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"Citrate ions bound specifically to the galline molecule, causing a conformational change in it.","type":"Abstract"},{"text":"In fact, [θ224] decreased with an increase in citrate concentration (Fig. 1B).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-14T10:36:36.964Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":62,"reference_id":"2738040","reference_source":"pmid","reference_html":"Conformation of the fowl protamine, galline, and its binding properties to DNA. <i> Nakano M, Kasai K, Yoshida K, Tanimoto T, Tamaki Y, Tobita T. </i> J Biochem, 1989","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007066","ec_ontology":"ECO","ec_name":"static light scattering assay evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00057r007","statement":[{"text":"Spectrophotometric analyses revealed that galline efficiently bound to DNA in 0.25mM EDTA/10mM Tricine-HC1, pH 7.4, but hardly so in 30mM NaC1/3mM sodium citrate, pH7.0.","type":"Abstract"},{"text":"Spectrophotometric analyses showed that galline bound efficiently to DNA in ET buffer, but hardly so in 0.2 X SSC.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-14T12:04:26.818Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P15340","date":"2016-08-23T15:15:20.000Z","acc":"P15340","name":"Sperm histone","length":62,"organism":"Gallus gallus","dataset":[],"UniParc":"UPI000017139D","genes":[],"alphafold_very_low_content":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":62,"type":"T"}],"Structural state":[{"start":1,"end":62,"type":"D"}],"Structural transition":[{"start":1,"end":62,"type":"T"}],"Molecular function":[{"start":1,"end":62,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01555","name":"DNA methylase","start":47,"end":303}]},"uniref50":"UniRef50_P11409","sequence":"MMTLNLQTMSSNDMLNFGKKPAYTTSNGSMYIGDSLELLESFPDESISLVMTSPPFALQRKKEYGNLEQHEYVDWFLSFAKVVNKKLKPDGSFVVDFGGAYMKGVPARSIYNFRVLIRMIDEVGFFLAEDFYWFNPSKLPSPIEWVNKRKIRVKDAVNTVWWFSKTEWPKSDITKVLAPYSDRMKKLIEDPDKFYTPKTRPSGHDIGKSFSKDNGGSIPPNLLQISNSESNGQYLANCKLMGIKAHPARFPAKLPEFFIRMLTEPDDLVVDIFGGSNTTGLVAERESRKWISFEMKPEYVAASAFRFLDNNISEEKITDIYNRILNGESLDLNSII","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Morganellaceae","Proteus"],"uniref90":"UniRef90_P11409","disprot_id":"DP00060","ncbi_taxon_id":183417,"regions_counter":10,"creator":"mnecci","regions":[{"start":179,"end":216,"reference_id":"9207015","reference_source":"pmid","reference_html":"Structure of pvu II DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment. <i> Gong W, O'Gara M, Blumenthal RM, Cheng X. </i> Nucleic Acids Res, 1997","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"region_id":"DP00060r010","statement":[{"text":"In   both   molecules   ∼40   amino   acids (Pro179–Gly216), located immediately after strand β7 and before strand β8, were not modeled in the current structure because of poor electron density. This poor density suggests that these aminoacids are very flexible.","type":"Results"},{"text":"The dashed line indicates a flexible region (amino acids 179–216) which is not modeled in the current structure.","type":"Figure"}],"cross_refs":[{"db":"PDB","id":"1BOO"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-07T10:43:33.017Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P11409","date":"2016-09-12T11:16:23.000Z","acc":"P11409","name":"Modification methylase PvuII","length":336,"organism":"Proteus hauseri","dataset":[],"UniParc":"UPI000016FE18","genes":[{"name":{"value":"pvuIIM","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"2662138","url":"http://www.ncbi.nlm.nih.gov/pubmed/2662138","alternativeUrl":"https://europepmc.org/abstract/MED/2662138"}}]}}],"alphafold_very_low_content":0.05952380952380952,"disorder_content":0.1130952380952381,"disprot_consensus":{"full":[{"start":179,"end":216,"type":"D"}],"Structural state":[{"start":179,"end":216,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01336","name":"OB-fold nucleic acid binding domain","start":197,"end":278},{"id":"PF04057","name":"Replication factor-A protein 1, N-terminal domain","start":5,"end":104},{"id":"PF08646","name":"Replication factor-A C terminal domain","start":461,"end":606},{"id":"PF16900","name":"Replication protein A OB domain","start":305,"end":402}],"gene3D":[{"start":183,"end":292,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"},{"start":297,"end":422,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"},{"start":423,"end":613,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"},{"start":3,"end":120,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}]},"uniref50":"UniRef50_P27694","sequence":"MVGQLSEGAIAAIMQKGDTNIKPILQVINIRPITTGNSPPRYRLLMSDGLNTLSSFMLATQLNPLVEEEQLSSNCVCQIHRFIVNTLKDGRRVVILMELEVLKSAEAVGVKIGNPVPYNEGLGQPQVAPPAPAASPAASSRPQPQNGSSGMGSTVSKAYGASKTFGKAAGPSLSHTSGGTQSKVVPIASLTPYQSKWTICARVTNKSQIRTWSNSRGEGKLFSLELVDESGEIRATAFNEQVDKFFPLIEVNKVYYFSKGTLKIANKQFTAVKNDYEMTFNNETSVMPCEDDHHLPTVQFDFTGIDDLENKSKDSLVDIIGICKSYEDATKITVRSNNREVAKRNIYLMDTSGKVVTATLWGEDADKFDGSRQPVLAIKGARVSDFGGRSLSVLSSSTIIANPDIPEAYKLRGWFDAEGQALDGVSISDLKSGGVGGSNTNWKTLYEVKSENLGQGDKPDYFSSVATVVYLRKENCMYQACPTQDCNKKVIDQQNGLYRCEKCDTEFPNFKYRMILSVNIADFQENQWVTCFQESAEAILGQNAAYLGELKDKNEQAFEEVFQNANFRSFIFRVRVKVETYNDESRIKATVMDVKPVDYREYGRRLVMSIRRSALM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P27694","disprot_id":"DP00061","ncbi_taxon_id":9606,"regions_counter":8,"creator":"ndavey","regions":[{"start":109,"end":168,"reference_id":"10526407","reference_source":"pmid","reference_html":"Human replication protein A: global fold of the N-terminal RPA-70 domain reveals a basic cleft and flexible C-terminal linker. <i> Jacobs DM, Lipton AS, Isern NG, Daughdrill GW, Lowry DF, Gomes X, Wold MS. </i> J Biomol NMR, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00061r005","statement":[{"text":"Human replication protein A: global fold of the N-terminal RPA-70 domain reveals a basic cleft and flexible C-terminal linker","type":"Title"},{"text":"We have solved the global fold of the fragment corresponding to this domain (RPA70 delta 169) and we find residues 8-108 of the N-terminal domain are structured. The remaining C-terminal residues are unstructured and may form a flexible linker to the DNA-binding domain of RPA70.","type":"Abstract"},{"text":"A heteronuclear 15N-1H NOE spectrum labeled with assigned resonances from the C-terminal linker region. All labeled resonances are negative relative to a control spectrum, indicating fast internal backbone motion in the linker. Almost all other unlabeled resonances are also negative and not from the globular region, we assume they are also from the linker.","type":"Figure"},{"text":"The longest (1665 ms) time point of the 15N-T1 experiment shows that the resonances in (a) also have long 15N-T1’s; another strong indication that the C-terminus is flexible","type":"Figure"},{"text":"The N-terminal 8–108 amino acid residues form a five-stranded β-barrel capped on both ends by short helices. A 60 residue long flexible segment links the structured domain with the tandem DNA-binding domains of RPA70.","type":"Conclusion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-09T12:20:04.105Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":109,"end":168,"reference_id":"10526407","reference_source":"pmid","reference_html":"Human replication protein A: global fold of the N-terminal RPA-70 domain reveals a basic cleft and flexible C-terminal linker. <i> Jacobs DM, Lipton AS, Isern NG, Daughdrill GW, Lowry DF, Gomes X, Wold MS. </i> J Biomol NMR, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00061r006","statement":[{"text":"Human replication protein A: global fold of the N-terminal RPA-70 domain reveals a basic cleft and flexible C-terminal linker","type":"Title"},{"text":"We have solved the global fold of the fragment corresponding to this domain (RPA70 delta 169) and we find residues 8-108 of the N-terminal domain are structured. The remaining C-terminal residues are unstructured and may form a flexible linker to the DNA-binding domain of RPA70.","type":"Abstract"},{"text":"A heteronuclear 15N-1H NOE spectrum labeled with assigned resonances from the C-terminal linker region. All labeled resonances are negative relative to a control spectrum, indicating fast internal backbone motion in the linker. Almost all other unlabeled resonances are also negative and not from the globular region, we assume they are also from the linker.","type":"Figure"},{"text":"The longest (1665 ms) time point of the 15N-T1 experiment shows that the resonances in (a) also have long 15N-T1’s; another strong indication that the C-terminus is flexible","type":"Figure"},{"text":"The N-terminal 8–108 amino acid residues form a five-stranded β-barrel capped on both ends by short helices. A 60 residue long flexible segment links the structured domain with the tandem DNA-binding domains of RPA70.","type":"Conclusion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-09T12:20:07.558Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":105,"end":180,"reference_id":"17721672","reference_source":"pmid","reference_html":"Dynamic behavior of an intrinsically unstructured linker domain is conserved in the face of negligible amino acid sequence conservation. <i> Daughdrill GW, Narayanaswami P, Gilmore SH, Belczyk A, Brown CJ. </i> J Mol Evol, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00061r007","statement":[{"text":"Dynamic Behavior of an Intrinsically Unstructured Linker Domain Is Conserved in the Face of Negligible Amino Acid Sequence Conservation","type":"Title"},{"text":"The IULD functions to tether two high affinity single stranded DNA binding domains (DBD A and B) to an N-terminal single stranded DNA (ssDNA) binding and protein interaction domain (DBD F; see Fig. 1 for domain structure of RPA70) (Daughdrill et al. 2001).","type":"Introduction"},{"text":"Plot showing the values for the reduced spectral density function at 0 frequency, J(0). J(0) values are plotted on the vertical axis and residue number is plotted on the horizontal axis. ","type":"Figure"},{"text":"Unstructured linker domain (IULD) connecting two compact globular regions - the N-terminal DBD F domain and the ss-DNA binding DBD A domain - in the 70 kDa subunit of replication protein A (RPA70).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-09T12:20:02.947Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":105,"end":180,"reference_id":"17721672","reference_source":"pmid","reference_html":"Dynamic behavior of an intrinsically unstructured linker domain is conserved in the face of negligible amino acid sequence conservation. <i> Daughdrill GW, Narayanaswami P, Gilmore SH, Belczyk A, Brown CJ. </i> J Mol Evol, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00061r008","statement":[{"text":"Dynamic Behavior of an Intrinsically Unstructured Linker Domain Is Conserved in the Face of Negligible Amino Acid Sequence Conservation","type":"Title"},{"text":"The IULD functions to tether two high affinity single stranded DNA binding domains (DBD A and B) to an N-terminal single stranded DNA (ssDNA) binding and protein interaction domain (DBD F; see Fig. 1 for domain structure of RPA70) (Daughdrill et al. 2001).","type":"Introduction"},{"text":"Plot showing the values for the reduced spectral density function at 0 frequency, J(0). J(0) values are plotted on the vertical axis and residue number is plotted on the horizontal axis.","type":"Figure"},{"text":"Unstructured linker domain (IULD) connecting two compact globular regions - the N-terminal DBD F domain and the ss-DNA binding DBD A domain - in the 70 kDa subunit of replication protein A (RPA70).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-09T12:20:05.993Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_P27694","date":"2016-08-12T15:31:37.000Z","acc":"P27694","name":"Replication protein A 70 kDa DNA-binding subunit","length":616,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00001739BE","genes":[{"name":{"value":"RPA1"},"synonyms":[{"value":"REPA1"},{"value":"RPA70"}]}],"alphafold_very_low_content":0.11525974025974026,"disorder_content":0.12337662337662338,"disprot_consensus":{"full":[{"start":105,"end":180,"type":"D"}],"Structural state":[{"start":105,"end":180,"type":"D"}],"Disorder function":[{"start":105,"end":180,"type":"F"}]}},{"acc":"P19793","sequence":"MDTKHFLPLDFSTQVNSSLTSPTGRGSMAAPSLHPSLGPGIGSPGQLHSPISTLSSPINGMGPPFSVISSPMGPHSMSVPTTPTLGFSTGSPQLSSPMNPVSSSEDIKPPLGLNGVLKVPAHPSGNMASFTKHICAICGDRSSGKHYGVYSCEGCKGFFKRTVRKDLTYTCRDNKDCLIDKRQRNRCQYCRYQKCLAMGMKREAVQEERQRGKDRNENEVESTSSANEDMPVERILEAELAVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEWAKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEAYCKHKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT","alphafold_very_low_content":"0.3051948051948052","creator":"lpaladin","dataset":[],"date":"2016-09-05T15:44:09.000Z","disprot_id":"DP00062","features":{"pfam":[{"id":"PF00104","name":"Ligand-binding domain of nuclear hormone receptor","start":265,"end":441},{"id":"PF00105","name":"Double treble clef zinc finger, C4 type","start":134,"end":202},{"id":"PF11825","name":"Nuclear/hormone receptor activator site AF-1","start":18,"end":127}],"gene3D":[{"start":126,"end":230,"id":"3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A","_id":"685af523b4ac24d5329d722a"},{"start":231,"end":462,"id":"1.10.565.10","name":"Retinoid X Receptor","_id":"685af523b4ac24d5329d722b"}]},"genes":[{"name":{"value":"RXRA","evidences":[],"_id":"685af523b4ac24d5329d7272"},"synonyms":[{"value":"NR2B1","evidences":[],"_id":"685af523b4ac24d5329d7273"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d7271"}],"length":462,"name":"Retinoic acid receptor RXR-alpha","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":27,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000042A9A","uniref100":"UniRef100_P19793","uniref50":"UniRef50_P19793","uniref90":"UniRef90_P19793","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":130,"interaction_partner":[],"reference_html":"Solution Behavior of the Intrinsically Disordered N-Terminal Domain of Retinoid X Receptor α in the Context of the Full-Length Protein. <i> Belorusova A, Osz J, Petoukhov MV, Peluso-Iltis C, Kieffer B, Svergun DI, Rochel N. </i> Biochemistry, 2016","reference_id":"26937780","region_id":"DP00062r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"For the NTD–DBD–DNA complex, the representative ensemble shown in Figure 4E is in agreement with NMR data indicating a highly disordered and flexible domain.","_id":"685af523b4ac24d5329d722d"},{"type":"Results","text":"Overall, these data demonstrate a high degree of flexibility of the NTDs that is restrained by the space occupied by the hinge and LBD dimer in the context of the full-length protein.","_id":"685af523b4ac24d5329d722e"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-09T15:05:29.287Z","_id":"685af523b4ac24d5329d722f"},"version":3,"_id":"685af523b4ac24d5329d722c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":130,"interaction_partner":[],"reference_html":"Solution Behavior of the Intrinsically Disordered N-Terminal Domain of Retinoid X Receptor α in the Context of the Full-Length Protein. <i> Belorusova A, Osz J, Petoukhov MV, Peluso-Iltis C, Kieffer B, Svergun DI, Rochel N. </i> Biochemistry, 2016","reference_id":"26937780","region_id":"DP00062r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Experimental evidence of the disordered state of the RXRα NTD was provided by liquid state NMR.","_id":"685af523b4ac24d5329d7231"},{"type":"Results","text":"These observations suggest that the RXRα NTD is disordered in solution.","_id":"685af523b4ac24d5329d7232"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-09T15:05:30.345Z","_id":"685af523b4ac24d5329d7233"},"version":4,"_id":"685af523b4ac24d5329d7230","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1RXR","_id":"685af523b4ac24d5329d7241"}],"curator_id":"ftonello","curator_name":"Fiorella Tonello","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":178,"end":187,"interaction_partner":[],"reference_html":"High-resolution solution structure of the retinoid X receptor DNA-binding domain. <i> Holmbeck SM, Foster MP, Casimiro DR, Sem DS, Dyson HJ, Wright PE. </i> J Mol Biol, 1998","reference_id":"9698548","region_id":"DP00062r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The {1H}-15N NOEs  show that residues 178 to 187 clearly exhibit smaller than average NOE values, indicating increased flexibility in this region.","_id":"685af523b4ac24d5329d7240"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2022-02-17T13:10:45.899Z","_id":"685af523b4ac24d5329d7242"},"version":3,"_id":"685af523b4ac24d5329d723f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1RXR","_id":"685af523b4ac24d5329d7248"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":178,"end":187,"interaction_partner":[],"reference_html":"High-resolution solution structure of the retinoid X receptor DNA-binding domain. <i> Holmbeck SM, Foster MP, Casimiro DR, Sem DS, Dyson HJ, Wright PE. </i> J Mol Biol, 1998","reference_id":"9698548","region_id":"DP00062r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The second zinc ion is complexed by cysteine residues 171, 177, 187 and 190, forming a second zinc loop.","_id":"685af523b4ac24d5329d7249"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","term_id":"GO:0008270","term_is_binding":true,"term_is_obsolete":false,"term_name":"zinc ion binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-09T15:05:28.133Z","_id":"685af523b4ac24d5329d724a"},"version":4,"_id":"685af523b4ac24d5329d7247","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1RXR","_id":"685af523b4ac24d5329d724f"}],"curator_id":"ftonello","curator_name":"Fiorella Tonello","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":169,"end":189,"interaction_partner":[],"reference_html":"High-resolution solution structure of the retinoid X receptor DNA-binding domain. <i> Holmbeck SM, Foster MP, Casimiro DR, Sem DS, Dyson HJ, Wright PE. </i> J Mol Biol, 1998","reference_id":"9698548","region_id":"DP00062r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The non-helical regions of the structure are less well-ordered, in particular the region between the first and second helix, residues 169 to 189.","_id":"685af523b4ac24d5329d724e"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2022-02-17T13:10:44.288Z","_id":"685af523b4ac24d5329d7250"},"version":3,"_id":"685af523b4ac24d5329d724d","reference_source":"pmid"}],"__v":0,"disorder_content":0.3268398268398268,"disprot_consensus":{"full":[{"start":1,"end":130,"type":"D"},{"start":169,"end":189,"type":"D"}],"Structural state":[{"start":1,"end":130,"type":"D"},{"start":169,"end":189,"type":"D"}],"Molecular function":[{"start":178,"end":187,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00615","name":"Regulator of G protein signaling domain","start":62,"end":177}],"gene3D":[{"start":51,"end":88,"id":"1.10.196.10","name":"1.10.196.10"},{"start":160,"end":183,"id":"1.10.196.10","name":"1.10.196.10"},{"start":89,"end":159,"id":"1.10.167.10","name":"Regulator of G-protein Signalling 4, domain 2"}]},"uniref50":"UniRef50_P49799","sequence":"MCKGLAGLPASCLRSAKDMKHRLGFLLQKSDSCEHSSSHSKKDKVVTCQRVSQEEVKKWAESLENLINHECGLAAFKAFLKSEYSEENIDFWISCEEYKKIKSPSKLSPKAKKIYNEFISVQATKEVNLDSCTREETSRNMLEPTITCFDEAQKKIFNLMEKDSYRRFLKSRFYLDLTNPSSCGAEKQKGAKSSADCTSLVPQCA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_P49799","disprot_id":"DP00063","ncbi_taxon_id":10116,"regions_counter":2,"creator":"lkalmar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":50,"region_id":"DP00063r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis. <i> Tesmer JJ, Berman DM, Gilman AG, Sprang SR. </i> Cell, 1997","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1AGR"}],"reference_id":"9108480","statement":[{"text":"Iterative rounds of four-fold noncrystallographic symmetry (NCS) averaging, solvent flattening, and electron density map interpretation yielded a model comprising 128 residues of RGS4 and virtually all of the Giα1 subunit.","type":"Results"},{"text":"The current model of RGS4–Giα1 contains two molecules of Giα1 (chain A, residues 5–354; chain D, residues 11–354), two molecules of RGS4 (chain E, residues 51–178; chain H, residues 60–175), two citrate ions, and 56 water molecules.","type":"Results"},{"text":"Accordingly, the arms of RGS4 are disordered and play no obvious role either in binding Giα1 or in stabilizing the RGS box.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-17T13:34:39.644Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":205,"region_id":"DP00063r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis. <i> Tesmer JJ, Berman DM, Gilman AG, Sprang SR. </i> Cell, 1997","term_id":"IDPO:0000002","curator_id":"fquaglia","start":179,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1AGR"}],"reference_id":"9108480","statement":[{"text":"Iterative rounds of four-fold noncrystallographic symmetry (NCS) averaging, solvent flattening, and electron density map interpretation yielded a model comprising 128 residues of RGS4 and virtually all of the Giα1 subunit.","type":"Results"},{"text":"The current model of RGS4–Giα1 contains two molecules of Giα1 (chain A, residues 5–354; chain D, residues 11–354), two molecules of RGS4 (chain E, residues 51–178; chain H, residues 60–175), two citrate ions, and 56 water molecules.","type":"Results"},{"text":"Accordingly, the arms of RGS4 are disordered and play no obvious role either in binding Giα1 or in stabilizing the RGS box.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-17T13:34:40.440Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P49799","date":"2016-08-21T17:21:42.000Z","acc":"P49799","name":"Regulator of G-protein signaling 4","length":205,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI00001104EE","genes":[{"name":{"value":"Rgs4"}}],"alphafold_very_low_content":0.2048780487804878,"disorder_content":0.375609756097561,"disprot_consensus":{"full":[{"start":1,"end":50,"type":"D"},{"start":179,"end":205,"type":"D"}],"Structural state":[{"start":1,"end":50,"type":"D"},{"start":179,"end":205,"type":"D"}]}},{"acc":"P03607","sequence":"MSGLFHHRTKPREIRAFVMATRLTKKQLAQAIQNTLPNPPRRKRRAKRRAAQVPKPTQAGVSMAPIAQGTMVKLRPPMLRSSMDVTILSHCELSTELAVTVTIVVTSELVMPFTVGTWLRGVAQNWSKYAWVAIRYTYLPSCPTTTSGAIHMGFQYDMADTLPVSVNQLSNLKGYVTGPVWEGQSGLCFVNNTKCPDTSRAITIALDTNEVSEKRYPFKTATDYATAVGVNANIGNILVPARLVTAMEGGSSKTAVNTGRLYASYTIRLIEPIAAALNL","creator":"mnecci","dataset":["Viral proteins"],"date":"2016-08-24T10:00:43.000Z","disprot_id":"DP00064","features":{"pfam":[{"id":"PF00729","name":"Viral coat protein (S domain)","start":60,"end":274}],"gene3D":[{"start":58,"end":279,"id":"2.60.120.20","name":"2.60.120.20","_id":"685af523b4ac24d5329d7275"}]},"genes":[{"synonyms":[],"olnNames":[],"orfNames":[{"value":"ORF3","evidences":[],"_id":"685af523b4ac24d5329d7288"}],"_id":"685af523b4ac24d5329d7287"}],"length":279,"name":"Capsid protein","ncbi_taxon_id":196398,"organism":"Southern cowpea mosaic virus","regions_counter":6,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Sobelivirales","Solemoviridae","Sobemovirus"],"UniParc":"UPI0000127D97","uniref100":"UniRef100_P03607","uniref50":"UniRef50_P03607","uniref90":"UniRef90_P03607","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"4SBV","_id":"685af523b4ac24d5329d7284"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":20,"end":57,"interaction_partner":[],"reference_html":"Subunit interactions in southern bean mosaic virus. <i> Rossmann MG, Abad-Zapatero C, Hermodson MA, Erickson JW. </i> J Mol Biol, 1983","reference_id":"6854633","region_id":"DP00064r006","released":"2022_03","sample":[],"statement":[{"type":"Figure","text":"Residues 1 to 38 are disordered and buried in the RNA in all subunits. Residues 39 to 62 are ordered only in the C subunit.","_id":"685af523b4ac24d5329d7285"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-06T14:05:06.282Z","_id":"685af523b4ac24d5329d7286"},"version":1,"_id":"685af523b4ac24d5329d7283","reference_source":"pmid"}],"__v":0,"disorder_content":0.13620071684587814,"disprot_consensus":{"full":[{"start":20,"end":57,"type":"D"}],"Structural state":[{"start":20,"end":57,"type":"D"}]}},{"acc":"O86488","sequence":"MLNRENKTAITRKGMVSNRLNKFSIRKYTVGTASILVGTTLIFGLGNQEAKAAESTNKELNEATTSASDNQSSDKVDMQQLNQEDNTKNDNQKEMVSSQGNETTSNGNKLIEKESVQSTTGNKVEVSTAKSDEQASPKSTNEDLNTKQTISNQEALQPDLQENKSVVNVQPTNEENKKVDAKTESTTLNVKSDAIKSNDETLVDNNSNSNNENNADIILPKSTAPKRLNTRMRIAAVQPSSTEAKNVNDLITSNTTLTVVDADKNNKIVPAQDYLSLKSQITVDDKVKSGDYFTIKYSDTVQVYGLNPEDIKNIGDIKDPNNGETIATAKHDTANNLITYTFTDYVDRFNSVQMGINYSIYMDADTIPVSKNDVEFNVTIGNTTTKTTANIQYPDYVVNEKNSIGSAFTETVSHVGNKENPGYYKQTIYVNPSENSLTNAKLKVQAYHSSYPNNIGQINKDVTDIKIYQVPKGYTLNKGYDVNTKELTDVTNQYLQKITYGDNNSAVIDFGNADSAYVVMVNTKFQYTNSESPTLVQMATLSSTGNKSVSTGNALGFTNNQSGGAGQEVYKIGNYVWEDTNKNGVQELGEKGVGNVTVTVFDNNTNTKVGEAVTKEDGSYLIPNLPNGDYRVEFSNLPKGYEVTPSKQGNNEELDSNGLSSVITVNGKDNLSADLGIYKPKYNLGDYVWEDTNKNGIQDQDEKGISGVTVTLKDENGNVLKTVTTDADGKYKFTDLDNGNYKVEFTTPEGYTPTTVTSGSDIEKDSNGLTTTGVINGADNMTLDSGFYKTPKYNLGNYVWEDTNKDGKQDSTEKGISGVTVTLKNENGEVLQTTKTDKDGKYQFTGLENGTYKVEFETPSGYTPTQVGSGTDEGIDSNGTSTTGVIKDKDNDTIDSGFYKPTYNLGDYVWEDTNKNGVQDKDEKGISGVTVTLKDENDKVLKTVTTDENGKYQFTDLNNGTYKVEFETPSGYTPTSVTSGNDTEKDSNGLTTTGVIKDADNMTLDSGFYKTPKYSLGDYVWYDSNKDGKQDSTEKGIKDVKVTLLNEKGEVIGTTKTDENGKYCFDNLDSGKYKVIFEKPAGLTQTGTNTTEDDKDADGGEVDVTITDHDDFTLDNGYYEEETSDSDSDSDSDSDSDRDSDSDSDSDSDSDSDSDSDSDSDSDSDSDRDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDAGKHTPVKPMSTTKDHHNKAKALPETGNENSGSNNATLFGGLFAALGSLLLFGRRKKQNK","alphafold_very_low_content":"0.3315589353612167","creator":"amonzon","dataset":[],"date":"2016-08-11T12:46:11.000Z","disprot_id":"DP00065","features":{"pfam":[{"id":"PF00746","name":"LPXTG cell wall anchor motif","start":1272,"end":1315},{"id":"PF04650","name":"YSIRK type signal peptide","start":18,"end":43},{"id":"PF10425","name":"C-terminus of bacterial fibrinogen-binding adhesin","start":404,"end":548},{"id":"PF17210","name":"SdrD B-like domain","start":571,"end":675},{"id":"PF17210","name":"SdrD B-like domain","start":683,"end":786},{"id":"PF17210","name":"SdrD B-like domain","start":794,"end":897},{"id":"PF17210","name":"SdrD B-like domain","start":904,"end":1007},{"id":"PF17210","name":"SdrD B-like domain","start":1015,"end":1118},{"id":"PF17961","name":"Bacterial Ig domain","start":271,"end":371}],"gene3D":[{"start":794,"end":902,"id":"2.60.40.10","name":"Immunoglobulins","_id":"685af523b4ac24d5329d7292"},{"start":903,"end":1012,"id":"2.60.40.10","name":"Immunoglobulins","_id":"685af523b4ac24d5329d7293"},{"start":1013,"end":1131,"id":"2.60.40.10","name":"Immunoglobulins","_id":"685af523b4ac24d5329d7294"},{"start":241,"end":394,"id":"2.60.40.1280","name":"2.60.40.1280","_id":"685af523b4ac24d5329d7295"},{"start":682,"end":793,"id":"2.60.40.10","name":"Immunoglobulins","_id":"685af523b4ac24d5329d7296"},{"start":568,"end":681,"id":"2.60.40.10","name":"Immunoglobulins","_id":"685af523b4ac24d5329d7297"},{"start":395,"end":555,"id":"2.60.40.1290","name":"2.60.40.1290","_id":"685af523b4ac24d5329d7298"}]},"genes":[{"name":{"value":"sdrD","evidences":[],"_id":"685af523b4ac24d5329d72c0"},"synonyms":[],"olnNames":[{"value":"NWMN_0524","evidences":[],"_id":"685af523b4ac24d5329d72c1"}],"orfNames":[],"_id":"685af523b4ac24d5329d72bf"}],"length":1315,"name":"Serine-aspartate repeat-containing protein D","ncbi_taxon_id":426430,"organism":"Staphylococcus aureus (strain Newman)","regions_counter":13,"released":"2016_10","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Staphylococcaceae","Staphylococcus"],"UniParc":"UPI0000052285","uniref100":"UniRef100_O86488","uniref50":"UniRef50_Q2G0L4","uniref90":"UniRef90_Q2G0L4","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":569,"end":1123,"interaction_partner":[],"reference_html":"The binding of calcium to the B-repeat segment of SdrD, a cell surface protein of Staphylococcus aureus. <i> Josefsson E, O'Connell D, Foster TJ, Durussel I, Cox JA. </i> J Biol Chem, 1998","reference_id":"9813018","region_id":"DP00065r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"However, on a TSK gel filtration column equilibrated in buffer A containing 1 mm EGTA or 1 mm Ca2+, it eluted with apparent molecular masses of 320 and 250 kDa, respectively.","_id":"685af523b4ac24d5329d729a"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-10-06T18:42:08.248Z","_id":"685af523b4ac24d5329d729b"},"version":3,"_id":"685af523b4ac24d5329d7299","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":569,"end":1123,"interaction_partner":[],"reference_html":"The binding of calcium to the B-repeat segment of SdrD, a cell surface protein of Staphylococcus aureus. <i> Josefsson E, O'Connell D, Foster TJ, Durussel I, Cox JA. </i> J Biol Chem, 1998","reference_id":"9813018","region_id":"DP00065r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Equilibrium gel filtration experiments at low (10 mm Tris-HCl, pH 7.5) as well as moderately high ionic strength (50 mm Tris-HCl, pH 7.5, 150 mm KCl) and a free Ca2+ concentration of 40–60 μm showed that B1–B5 binds 14–15 mol of Ca2+/mol, which seems to be a very good estimation of the total capacity.","_id":"685af523b4ac24d5329d729f"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","term_id":"GO:0005509","term_is_binding":true,"term_is_obsolete":false,"term_name":"calcium ion binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-10-06T20:41:20.973Z","_id":"685af523b4ac24d5329d72a0"},"version":4,"_id":"685af523b4ac24d5329d729e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":569,"end":1123,"interaction_partner":[],"reference_html":"The binding of calcium to the B-repeat segment of SdrD, a cell surface protein of Staphylococcus aureus. <i> Josefsson E, O'Connell D, Foster TJ, Durussel I, Cox JA. </i> J Biol Chem, 1998","reference_id":"9813018","region_id":"DP00065r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Because, except for a blue shift of the minimum to 197 nm, the spectrum of metal-free B1–B5 at 25 °C is very similar, this form must contain very little organized secondary structure.","_id":"685af523b4ac24d5329d72a2"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-10-06T20:41:27.885Z","_id":"685af523b4ac24d5329d72a3"},"version":3,"_id":"685af523b4ac24d5329d72a1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":569,"end":1123,"interaction_partner":[],"reference_html":"The binding of calcium to the B-repeat segment of SdrD, a cell surface protein of Staphylococcus aureus. <i> Josefsson E, O'Connell D, Foster TJ, Durussel I, Cox JA. </i> J Biol Chem, 1998","reference_id":"9813018","region_id":"DP00065r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In contrast, the Ca2+-loaded protein shows discrete peaks: one positive peak at 228 nm, which may be attributable to aromatic residues (26), and two negative peaks at 215 and 195 nm.","_id":"685af523b4ac24d5329d72a5"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-10-06T20:41:25.536Z","_id":"685af523b4ac24d5329d72a6"},"version":3,"_id":"685af523b4ac24d5329d72a4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":569,"end":1123,"interaction_partner":[],"reference_html":"The binding of calcium to the B-repeat segment of SdrD, a cell surface protein of Staphylococcus aureus. <i> Josefsson E, O'Connell D, Foster TJ, Durussel I, Cox JA. </i> J Biol Chem, 1998","reference_id":"9813018","region_id":"DP00065r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In contrast, the Ca2+-loaded protein shows discrete peaks: one positive peak at 228 nm, which may be attributable to aromatic residues (26), and two negative peaks at 215 and 195 nm.","_id":"685af523b4ac24d5329d72a8"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","term_id":"GO:0005509","term_is_binding":true,"term_is_obsolete":false,"term_name":"calcium ion binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-10-06T20:41:21.212Z","_id":"685af523b4ac24d5329d72a9"},"version":4,"_id":"685af523b4ac24d5329d72a7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006206","ec_name":"near-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":569,"end":1123,"interaction_partner":[],"reference_html":"The binding of calcium to the B-repeat segment of SdrD, a cell surface protein of Staphylococcus aureus. <i> Josefsson E, O'Connell D, Foster TJ, Durussel I, Cox JA. </i> J Biol Chem, 1998","reference_id":"9813018","region_id":"DP00065r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Removal of Ca2+ changed the intensity of ellipticity only slightly, with a 2-nm blue shift, indicating that microenvironment of the Tyr residues in apoB1–B5 is asymmetric and therefore structured.","_id":"685af523b4ac24d5329d72ab"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-10-06T18:42:03.948Z","_id":"685af523b4ac24d5329d72ac"},"version":3,"_id":"685af523b4ac24d5329d72aa","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006206","ec_name":"near-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":569,"end":1123,"interaction_partner":[],"reference_html":"The binding of calcium to the B-repeat segment of SdrD, a cell surface protein of Staphylococcus aureus. <i> Josefsson E, O'Connell D, Foster TJ, Durussel I, Cox JA. </i> J Biol Chem, 1998","reference_id":"9813018","region_id":"DP00065r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Removal of Ca2+ changed the intensity of ellipticity only slightly, with a 2-nm blue shift, indicating that microenvironment of the Tyr residues in apoB1–B5 is asymmetric and therefore structured.","_id":"685af523b4ac24d5329d72ae"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-10-06T18:42:10.089Z","_id":"685af523b4ac24d5329d72af"},"version":3,"_id":"685af523b4ac24d5329d72ad","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006206","ec_name":"near-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":569,"end":1123,"interaction_partner":[],"reference_html":"The binding of calcium to the B-repeat segment of SdrD, a cell surface protein of Staphylococcus aureus. <i> Josefsson E, O'Connell D, Foster TJ, Durussel I, Cox JA. </i> J Biol Chem, 1998","reference_id":"9813018","region_id":"DP00065r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Removal of Ca2+ changed the intensity of ellipticity only slightly, with a 2-nm blue shift, indicating that microenvironment of the Tyr residues in apoB1–B5 is asymmetric and therefore structured.","_id":"685af523b4ac24d5329d72b1"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","term_id":"GO:0005509","term_is_binding":true,"term_is_obsolete":false,"term_name":"calcium ion binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-10-06T18:42:13.786Z","_id":"685af523b4ac24d5329d72b2"},"version":4,"_id":"685af523b4ac24d5329d72b0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":569,"end":1123,"interaction_partner":[],"reference_html":"The binding of calcium to the B-repeat segment of SdrD, a cell surface protein of Staphylococcus aureus. <i> Josefsson E, O'Connell D, Foster TJ, Durussel I, Cox JA. </i> J Biol Chem, 1998","reference_id":"9813018","region_id":"DP00065r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The spectrum of the metal-free protein is quite similar to that of the guanidine-HCl-denatured form, although its intensity is 20% higher, and the maximum blue shifted by 5 nm.","_id":"685af523b4ac24d5329d72b4"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-10-06T20:41:37.749Z","_id":"685af523b4ac24d5329d72b5"},"version":3,"_id":"685af523b4ac24d5329d72b3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"IDA","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":569,"end":1123,"interaction_partner":[],"reference_html":"The binding of calcium to the B-repeat segment of SdrD, a cell surface protein of Staphylococcus aureus. <i> Josefsson E, O'Connell D, Foster TJ, Durussel I, Cox JA. </i> J Biol Chem, 1998","reference_id":"9813018","region_id":"DP00065r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The Ca2+-saturated protein shows a 2.5-fold higher fluorescence intensity and a blue shift from 345 to 323 nm compared with the metal-free state, suggesting that with Ca2+ binding a well organized hydrophobic core is formed around the Trp residue (31).","_id":"685af523b4ac24d5329d72b7"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-10-06T18:42:10.713Z","_id":"685af523b4ac24d5329d72b8"},"version":3,"_id":"685af523b4ac24d5329d72b6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":569,"end":1123,"interaction_partner":[],"reference_html":"The binding of calcium to the B-repeat segment of SdrD, a cell surface protein of Staphylococcus aureus. <i> Josefsson E, O'Connell D, Foster TJ, Durussel I, Cox JA. </i> J Biol Chem, 1998","reference_id":"9813018","region_id":"DP00065r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The Ca2+-saturated protein shows a 2.5-fold higher fluorescence intensity and a blue shift from 345 to 323 nm compared with the metal-free state, suggesting that with Ca2+ binding a well organized hydrophobic core is formed around the Trp residue (31).","_id":"685af523b4ac24d5329d72ba"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","term_id":"GO:0005509","term_is_binding":true,"term_is_obsolete":false,"term_name":"calcium ion binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-10-06T18:42:13.199Z","_id":"685af523b4ac24d5329d72bb"},"version":4,"_id":"685af523b4ac24d5329d72b9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"amonzon","curator_name":"Alex Monzon","curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IC","ec_id":"ECO:0007759","ec_name":"curator inference from database used in manual assertion","ec_ontology":"ECO","start":1117,"end":1250,"interaction_partner":[],"reference_html":"An Entry Referenced from MobiDB","reference_id":"https://mobidb.org/O86488","region_id":"DP00065r013","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"This poly-E region is inferred by the curator to be disordered, based on MobiDB-Lite and according to experimental evidence demonstrating that poly-E repeats display random-coil-like conformation (PMID:16949547)","_id":"685af523b4ac24d5329d72bd"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2022-02-17T13:36:59.115Z","_id":"685af523b4ac24d5329d72be"},"version":1,"_id":"685af523b4ac24d5329d72bc","reference_source":"mobidb"}],"__v":0,"disorder_content":0.5186311787072243,"disprot_consensus":{"full":[{"start":569,"end":1123,"type":"T"},{"start":1124,"end":1250,"type":"D"}],"Structural state":[{"start":569,"end":1250,"type":"D"}],"Molecular function":[{"start":569,"end":1123,"type":"F"}],"Structural transition":[{"start":569,"end":1123,"type":"T"}]}},{"acc":"Q57733","sequence":"MFGRDPFDSLFERMFKEFFATPMTGTTMIQSSTGIQISGKGFMPISIIEGDQHIKVIAWLPGVNKEDIILNAVGDTLEIRAKRSPLMITESERIIYSEIPEEEEIYRTIKLPATVKEENASAKFENGVLSVILPKAESSIKKGINIE","alphafold_very_low_content":"0.04081632653061224","creator":"gminervini","dataset":["Stress response proteins"],"date":"2016-08-23T11:29:56.000Z","disprot_id":"DP00067","features":{"pfam":[{"id":"PF00011","name":"Hsp20/alpha crystallin family","start":47,"end":146}],"gene3D":[{"start":34,"end":147,"id":"2.60.40.790","name":"2.60.40.790","_id":"685af523b4ac24d5329d72d4"}]},"genes":[{"synonyms":[],"olnNames":[{"value":"MJ0285","evidences":[],"_id":"685af523b4ac24d5329d72f4"}],"orfNames":[],"_id":"685af523b4ac24d5329d72f3"}],"length":147,"name":"Small heat shock protein HSP16.5","ncbi_taxon_id":243232,"organism":"Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)","regions_counter":11,"released":"2016_10","taxonomy":["Archaea","Euryarchaeota","Methanomada group","Methanococci","Methanococcales","Methanocaldococcaceae","Methanocaldococcus"],"UniParc":"UPI0000112CDC","uniref100":"UniRef100_Q57733","uniref50":"UniRef50_Q57733","uniref90":"UniRef90_Q57733","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1SHS","_id":"685af523b4ac24d5329d72d6"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":32,"interaction_partner":[],"reference_html":"Crystal structure of a small heat-shock protein. <i> Kim KK, Kim R, Kim SH. </i> Nature, 1998","reference_id":"9707123","region_id":"DP00067r001","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"The amino-terminal 32 residues are highly disordered, but from residue 33 onwards, including the entire α-crystallin domain (residues 46–135) and thecarboxy-terminal extension, they are well ordered.","_id":"685af523b4ac24d5329d72d7"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d72d5","reference_source":"pmid","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-08T16:24:36.908Z"}},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":32,"interaction_partner":[],"reference_html":"Crystal structure of a small heat-shock protein. <i> Kim KK, Kim R, Kim SH. </i> Nature, 1998","reference_id":"9707123","region_id":"DP00067r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The amino-terminal 32 residues are highly disordered, but from residue 33 onwards, including the entire α-crystallin domain (residues 46–135) and thecarboxy-terminal extension, they are well ordered.","_id":"685af523b4ac24d5329d72db"}],"states_connection":[],"term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","version":4,"_id":"685af523b4ac24d5329d72da","reference_source":"pmid","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-08T16:45:14.604Z"}},{"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg107Gly","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"4I88","_id":"685af523b4ac24d5329d72e8"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2025-10-08T16:01:00.116Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":33,"reference_html":"Changes in the quaternary structure and function of MjHSP16.5 attributable to deletion of the IXI motif and introduction of the substitution, R107G, in the α-crystallin domain. <i> Quinlan RA, Zhang Y, Lansbury A, Williamson I, Pohl E, Sun F. </i> Philos Trans R Soc Lond B Biol Sci, 2013","reference_id":"23530263","region_id":"DP00067r009","released":"2025_12","statement":[{"type":"Curator statement","text":"The region is missing from the pdb structure.","_id":"685af523b4ac24d5329d72e9"}],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":1,"_id":"685af523b4ac24d5329d72e7","reference_source":"pmid"},{"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg107Gly","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"4I88","_id":"685af523b4ac24d5329d72eb"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2025-10-08T16:43:20.844Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":33,"reference_html":"Changes in the quaternary structure and function of MjHSP16.5 attributable to deletion of the IXI motif and introduction of the substitution, R107G, in the α-crystallin domain. <i> Quinlan RA, Zhang Y, Lansbury A, Williamson I, Pohl E, Sun F. </i> Philos Trans R Soc Lond B Biol Sci, 2013","reference_id":"23530263","region_id":"DP00067r010","released":"2025_12","statement":[{"type":"Curator statement","text":"The region is missing from the pdb structure.","_id":"685af523b4ac24d5329d72ec"}],"term_go_domain":null,"term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":1,"_id":"685af523b4ac24d5329d72ea","reference_source":"pmid"}],"__v":0,"disorder_content":0.22448979591836735,"disprot_consensus":{"full":[{"start":1,"end":33,"type":"D"}],"Structural state":[{"start":1,"end":33,"type":"D"}],"Disorder function":[{"start":1,"end":33,"type":"F"}]}},{"acc":"P60881","sequence":"MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTDLGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG","alphafold_very_low_content":"0.11650485436893204","creator":"ftonello","dataset":[],"date":"2016-09-05T16:35:55.000Z","disprot_id":"DP00068","features":{"pfam":[{"id":"PF00835","name":"SNAP-25 family","start":91,"end":142},{"id":"PF05739","name":"SNARE domain","start":146,"end":202}],"gene3D":[{"start":1,"end":82,"id":"1.20.5.110","name":"1.20.5.110","_id":"685af523b4ac24d5329d72f6"},{"start":120,"end":206,"id":"1.20.5.110","name":"1.20.5.110","_id":"685af523b4ac24d5329d72f7"}]},"genes":[{"name":{"value":"Snap25","evidences":[],"_id":"685af523b4ac24d5329d7327"},"synonyms":[{"value":"Snap","evidences":[],"_id":"685af523b4ac24d5329d7328"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d7326"}],"length":206,"name":"Synaptosomal-associated protein 25","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions_counter":22,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"UniParc":"UPI0000001103","uniref100":"UniRef100_P60880","uniref50":"UniRef50_P60880","uniref90":"UniRef90_P60880","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-17T14:57:41.590Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":120,"end":206,"interaction_partner":[],"reference_html":"Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly. <i> Fasshauer D, Eliason WK, Brünger AT, Jahn R. </i> Biochemistry, 1998","reference_id":"9671503","region_id":"DP00068r017","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Synaptobrevin and both SNAP-25 fragments were largely unstructured, similar to previous results (not shown; see refs 18 and 19).","_id":"685af523b4ac24d5329d7319"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":0,"_id":"685af523b4ac24d5329d7318","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006305","ec_name":"native protein gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":83,"interaction_partner":[{"db":"UniProt","id":"P32851","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d731b"}],"reference_html":"Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly. <i> Fasshauer D, Eliason WK, Brünger AT, Jahn R. </i> Biochemistry, 1998","reference_id":"9671503","region_id":"DP00068r018","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Furthermore, the syntaxin fragment formed stable complexes either with the N-terminal or with both fragments of SNAP-25 but not with the C-terminal fragment alone (Figure 4, lanes 9 and 10), again consistent with previous results (18).","_id":"685af523b4ac24d5329d731c"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":1,"_id":"685af523b4ac24d5329d731a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":83,"interaction_partner":[{"db":"UniProt","id":"P32851","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d731e"}],"reference_html":"Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly. <i> Fasshauer D, Eliason WK, Brünger AT, Jahn R. </i> Biochemistry, 1998","reference_id":"9671503","region_id":"DP00068r019","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Formation of these subcomplexes was associated with an increase in α-helical content that was more pronounced than that observed previously for the full-length proteins (Figure 3, columns 13−15; see ref 18].","_id":"685af523b4ac24d5329d731f"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":1,"_id":"685af523b4ac24d5329d731d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-17T15:09:35.667Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":83,"interaction_partner":[],"reference_html":"Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly. <i> Fasshauer D, Eliason WK, Brünger AT, Jahn R. </i> Biochemistry, 1998","reference_id":"9671503","region_id":"DP00068r020","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Formation of these subcomplexes was associated with an increase in α-helical content that was more pronounced than that observed previously for the full-length proteins (Figure 3, columns 13−15; see ref 18].","_id":"685af523b4ac24d5329d7321"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":0,"_id":"685af523b4ac24d5329d7320","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-17T15:08:26.616Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":84,"end":119,"interaction_partner":[],"reference_html":"Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly. <i> Fasshauer D, Eliason WK, Brünger AT, Jahn R. </i> Biochemistry, 1998","reference_id":"9671503","region_id":"DP00068r021","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Analysis of the fragments derived from SNAP-25 revealed that both proteases excised the middle region which contains the putative membrane anchor domain. The resulting N- and C-terminal fragments remained in the SDS-resistant core complex. The N-terminal fragments generated by the two proteases were identical (residues 2−83). The C-terminal fragments generated by trypsin extended from residues 120 or 125 to the C-terminal end of the SNAP-25 construct, including the entire His6 tag.","_id":"685af523b4ac24d5329d7323"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":0,"_id":"685af523b4ac24d5329d7322","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-17T15:09:26.233Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":83,"interaction_partner":[],"reference_html":"Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly. <i> Fasshauer D, Eliason WK, Brünger AT, Jahn R. </i> Biochemistry, 1998","reference_id":"9671503","region_id":"DP00068r022","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Synaptobrevin and both SNAP-25 fragments were largely unstructured, similar to previous results (not shown; see refs 18 and 19).","_id":"685af523b4ac24d5329d7325"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":0,"_id":"685af523b4ac24d5329d7324","reference_source":"pmid"}],"__v":0,"disorder_content":0.9951456310679612,"disprot_consensus":{"full":[{"start":2,"end":83,"type":"T"},{"start":84,"end":206,"type":"D"}],"Structural state":[{"start":2,"end":206,"type":"D"}],"Molecular function":[{"start":2,"end":83,"type":"F"}],"Structural transition":[{"start":2,"end":83,"type":"T"}]}},{"acc":"P63027","sequence":"MSATAATAPPAAPAGEGGPPAPPPNLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAAKLKRKYWWKNLKMMIILGVICAIILIIIIVYFST","alphafold_very_low_content":"0.034482758620689655","creator":"dpiovesan","dataset":["NDDs-related proteins"],"date":"2016-08-18T13:34:04.000Z","disprot_id":"DP00069","features":{"pfam":[{"id":"PF00957","name":"Synaptobrevin","start":31,"end":111}],"gene3D":[{"start":1,"end":116,"id":"1.20.5.110","name":"1.20.5.110","_id":"685af523b4ac24d5329d732a"}]},"genes":[{"name":{"value":"VAMP2","evidences":[{"source":{"id":"HGNC:12643","name":"HGNC","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:12643","_id":"685af523b4ac24d5329d7340"},"code":"ECO:0000312","_id":"685af523b4ac24d5329d733f"}],"_id":"685af523b4ac24d5329d7341"},"synonyms":[{"value":"SYB2","evidences":[],"_id":"685af523b4ac24d5329d7342"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d733e"}],"length":116,"name":"Vesicle-associated membrane protein 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":7,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI00001380F0","uniref100":"UniRef100_P63027","uniref50":"UniRef50_P63027","uniref90":"UniRef90_P63027","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-17T15:30:23.826Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":40,"end":67,"interaction_partner":[],"reference_html":"Assembly of a ternary complex by the predicted minimal coiled-coil-forming domains of syntaxin, SNAP-25, and synaptobrevin. A circular dichroism study. <i> Cánaves JM, Montal M. </i> J Biol Chem, 1998","reference_id":"9852083","region_id":"DP00069r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In aqueous media, all peptides (alone or in mixtures) were unstructured, and neither increasing peptide concentration nor changing pH, ionic strength, or divalent cation concentration increased the α-helical content.","_id":"685af523b4ac24d5329d7338"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-08T19:51:50.616Z","_id":"685af523b4ac24d5329d7339"},"version":0,"_id":"685af523b4ac24d5329d7337","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-17T15:35:26.239Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":40,"end":67,"interaction_partner":[],"reference_html":"Assembly of a ternary complex by the predicted minimal coiled-coil-forming domains of syntaxin, SNAP-25, and synaptobrevin. A circular dichroism study. <i> Cánaves JM, Montal M. </i> J Biol Chem, 1998","reference_id":"9852083","region_id":"DP00069r007","released":"2022_03","sample":[{"db":"ChEBI","deviation":null,"entry_name":"2,2,2-trifluoroethanol","id":"42330","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d733b"}],"statement":[{"type":"Results","text":"In the presence of increasing concentrations of TFE (Fig.2, A–C), there was a significant increase in the α-helical content. The minimal concentration at which the peptides underwent a transition from mostly unstructured to partially structured was approximately 30%.","_id":"685af523b4ac24d5329d733c"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-08T19:51:51.762Z","_id":"685af523b4ac24d5329d733d"},"version":0,"_id":"685af523b4ac24d5329d733a","reference_source":"pmid"}],"__v":0,"disorder_content":0.2413793103448276,"disprot_consensus":{"full":[{"start":40,"end":67,"type":"T"}],"Structural state":[{"start":40,"end":67,"type":"D"}],"Structural transition":[{"start":40,"end":67,"type":"T"}]}},{"features":{"pfam":[{"id":"PF01387","name":"Synuclein","start":1,"end":130}],"gene3D":[{"start":1,"end":140,"id":"1.10.287.700","name":"Helix hairpin bin"}]},"uniref50":"UniRef50_P37840","sequence":"MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P37840","disprot_id":"DP00070","ncbi_taxon_id":9606,"regions_counter":40,"creator":"ireményi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":140,"region_id":"DP00070r001","released":"2022_03","ec_id":"ECO:0007689","reference_html":"NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. <i> Weinreb PH, Zhen W, Poon AW, Conway KA, Lansbury PT. </i> Biochemistry, 1996","statement":[{"text":"NACP Exhibits Properties Characteristic of an Extended Protein. The exact molecular weight of the NACP used in this work was found to be [M + H+] = 14 463 (±4.6) by MALDI-TOF mass spectrometry, consistent with the molecular weight of 14 460 predicted on the basis of the encoded amino acid sequence. On SDS−polyacrylamide gel electrophoresis (SDS−PAGE), the protein exhibits an apparent Mr of approximately 19 000 (Uéda et al., 1993), which may be attributable to abnormally low binding of SDS by the highly acidic NACP C-terminal sequence. A similar abnormal mobility has been demonstrated by other highly charged proteins (Williams et al., 1986; Yoo & Albanesi, 1990; Thomas et al., 1991; Gast et al., 1995). ","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"8901511","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-01-13T19:37:44.560Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":140,"region_id":"DP00070r007","released":"2025_06","ec_id":"ECO:0006165","reference_html":"Conformational properties of alpha-synuclein in its free and lipid-associated states. <i> Eliezer D, Kutluay E, Bussell R, Browne G. </i> J Mol Biol, 2001","statement":[{"text":"In contrast, the final 40 residues of αS exhibit secondary shifts that are more evenly distributed between the α and β regions of conformational space, suggesting that they are more highly unfolded and extended.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":100,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2025-01-13T18:52:35.484Z","reference_source":"pmid","term_name":"disorder","reference_id":"11286556","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":140,"region_id":"DP00070r011","released":"2022_03","ec_id":"ECO:0006204","reference_html":"α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer. <i> Fauvet B, Mbefo MK, Fares MB, Desobry C, Michael S, Ardah MT, Tsika E, Coune P, Prudent M, Lion N, Eliezer D, Moore DJ, Schneider B, Aebischer P, El-Agnaf OM, Masliah E, Lashuel HA. </i> J Biol Chem, 2012","statement":[{"text":"α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer.","type":"Title"},{"text":"Our findings demonstrate that both human and rodent α-syn expressed in the central nervous system exist predominantly as an unfolded monomer.","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22315227","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-01-13T19:37:13.465Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":140,"term_name":"lipid binding","released":"2025_06","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Far-UV CD spectroscopy performed at a protein concentration of 5 μM revealed that both native and heat-treated recombinant α-syn were mostly devoid of any significant secondary structure, as shown by a single spectral minimum at ~195 nm (Fig. 1C). Moreover, we confirmed that both native and denatured preparations are able to bind lipids and adopt an α-helical structure upon binding to 100-nm POPG small unilamellar vesicles.","type":"Results"}],"term_id":"GO:0008289","curator_id":"vnugnes","start":1,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"22315227","version":5,"reference_html":"α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer. <i> Fauvet B, Mbefo MK, Fares MB, Desobry C, Michael S, Ardah MT, Tsika E, Coune P, Prudent M, Lion N, Eliezer D, Moore DJ, Schneider B, Aebischer P, El-Agnaf OM, Masliah E, Lashuel HA. </i> J Biol Chem, 2012","date":"2025-01-13T19:37:05.613Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00070r012","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"ChEBI","id":"34080","operator":"and","partner_start":null,"partner_end":null}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":92,"region_id":"DP00070r013","released":"2022_03","ec_id":"ECO:0006289","reference_html":"A combinatorial NMR and EPR approach for evaluating the structural ensemble of partially folded proteins. <i> Rao JN, Jao CC, Hegde BG, Langen R, Ulmer TS. </i> J Am Chem Soc, 2010","statement":[{"text":"To advance the understanding of protein-micelle interactions, the present study concludes by showing that, in marked contrast to secondary structure stability, helix dynamics of SLAS-bound αS correlate with the degree of protein-induced departures from free micelle dimensions.","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":42,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2KKW"}],"reference_id":"20524659","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-01-13T19:37:37.380Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":92,"term_name":"disorder to order","released":"2022_03","ec_name":"site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"To advance the understanding of protein-micelle interactions, the present study concludes by showing that, in marked contrast to secondary structure stability, helix dynamics of SLAS-bound αS correlate with the degree of protein-induced departures from free micelle dimensions.","type":"Abstract"}],"term_id":"IDPO:0000011","curator_id":"fquaglia","start":42,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20524659","version":3,"reference_html":"A combinatorial NMR and EPR approach for evaluating the structural ensemble of partially folded proteins. <i> Rao JN, Jao CC, Hegde BG, Langen R, Ulmer TS. </i> J Am Chem Soc, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006289","region_id":"DP00070r014","ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-01-13T19:38:02.767Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":92,"term_name":"lipid binding","released":"2022_03","ec_name":"site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"To advance the understanding of protein-micelle interactions, the present study concludes by showing that, in marked contrast to secondary structure stability, helix dynamics of SLAS-bound αS correlate with the degree of protein-induced departures from free micelle dimensions.","type":"Abstract"}],"term_id":"GO:0008289","curator_id":"fquaglia","start":42,"term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"20524659","version":4,"reference_html":"A combinatorial NMR and EPR approach for evaluating the structural ensemble of partially folded proteins. <i> Rao JN, Jao CC, Hegde BG, Langen R, Ulmer TS. </i> J Am Chem Soc, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006289","region_id":"DP00070r015","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-01-13T19:38:40.720Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":140,"region_id":"DP00070r016","released":"2022_03","ec_id":"ECO:0006204","reference_html":"α-Synuclein is a Novel Microtubule Dynamase. <i> Cartelli D, Aliverti A, Barbiroli A, Santambrogio C, Ragg EM, Casagrande FV, Cantele F, Beltramone S, Marangon J, De Gregorio C, Pandini V, Emanuele M, Chieregatti E, Pieraccini S, Holmqvist S, Bubacco L, Roybon L, Pezzoli G, Grandori R, Arnal I, Cappelletti G. </i> Sci Rep, 2016","statement":[{"text":"α-Synuclein is a presynaptic protein associated to Parkinson's disease, which is unstructured when free in the cytoplasm and adopts α helical conformation when bound to vesicles.","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27628239","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-01-13T19:34:07.951Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":140,"term_name":"disorder to order","released":"2025_06","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"α-Synuclein is a presynaptic protein associated to Parkinson's disease, which is unstructured when free in the cytoplasm and adopts α helical conformation when bound to vesicles.","type":"Abstract"},{"text":"Syn binds to MTs and folds upon interaction with the tubulin α2β2 tetramer","type":"Results"},{"text":"Our data confirmed that Syn is unfolded in the absence of the ligand, whereas an equimolar Syn/tubulin mixture gives an overall secondary structure CD signal, which is more intense than the sum of the signals of the two individual proteins (Fig. 2a). Moreover, the CD signal originating in the mixture shows a gain of signal at 220 nm, which is typical of α-helix structures. Considering that (i) the interaction of tubulin with ligands is widely studied and an increase in its α-helix content has never been observed, and (ii) Syn is a soluble, intrinsically unfolded protein which is able to adopt α-helix structure in adequate conditions","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27628239","version":4,"reference_html":"α-Synuclein is a Novel Microtubule Dynamase. <i> Cartelli D, Aliverti A, Barbiroli A, Santambrogio C, Ragg EM, Casagrande FV, Cantele F, Beltramone S, Marangon J, De Gregorio C, Pandini V, Emanuele M, Chieregatti E, Pieraccini S, Holmqvist S, Bubacco L, Roybon L, Pezzoli G, Grandori R, Arnal I, Cappelletti G. </i> Sci Rep, 2016","date":"2025-01-13T19:33:59.084Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00070r018","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P68363"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P07437"}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":140,"term_name":"tubulin binding","released":"2025_06","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Syn binds to MTs and folds upon interaction with the tubulin α2β2 tetramer","type":"Results"},{"text":"Our data confirmed that Syn is unfolded in the absence of the ligand, whereas an equimolar Syn/tubulin mixture gives an overall secondary structure CD signal, which is more intense than the sum of the signals of the two individual proteins (Fig. 2a). Moreover, the CD signal originating in the mixture shows a gain of signal at 220 nm, which is typical of α-helix structures. Considering that (i) the interaction of tubulin with ligands is widely studied and an increase in its α-helix content has never been observed, and (ii) Syn is a soluble, intrinsically unfolded protein which is able to adopt α-helix structure in adequate conditions","type":"Results"}],"term_id":"GO:0015631","curator_id":"vnugnes","start":1,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"27628239","version":5,"reference_html":"α-Synuclein is a Novel Microtubule Dynamase. <i> Cartelli D, Aliverti A, Barbiroli A, Santambrogio C, Ragg EM, Casagrande FV, Cantele F, Beltramone S, Marangon J, De Gregorio C, Pandini V, Emanuele M, Chieregatti E, Pieraccini S, Holmqvist S, Bubacco L, Roybon L, Pezzoli G, Grandori R, Arnal I, Cappelletti G. </i> Sci Rep, 2016","date":"2025-01-13T19:35:31.167Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00070r019","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to monomeric or multimeric forms of tubulin, including microtubules.\" [GOC:clt]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P68363","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P07437","operator":"and","partner_start":null,"partner_end":null}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":140,"region_id":"DP00070r020","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Conformational properties of alpha-synuclein in its free and lipid-associated states. <i> Eliezer D, Kutluay E, Bussell R, Browne G. </i> J Mol Biol, 2001","statement":[{"text":"Far-UV CD data from wild-type αS in the presence and absence of SDS micelles, under conditions and protein concentrations (100 μM) identical to those used in the NMR experiments. A large conformational change is evident, with a high degree of helicity (indicated by the characteristic double minima at 208 and 222 nm) formed in the presence of micelles.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"11286556","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-01-13T18:57:07.964Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":102,"term_name":"disorder to order","released":"2025_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"A comparison of this spectrum with an equivalent spectrum from the free protein (Figure 7), shows that the Cα chemical shifts of the micelle associated residues are in general larger by approximately 2 ppm than they are in the free protein. This provides strong evidence for significant, persistent helical structure in the micelle associated region of αS.","type":"Results"},{"text":"Thus, it appears that the interaction of αS with synthetic lipid vesicles is quite similar to its interaction with SDS detergent micelles, as nearly identical regions of the protein remain free from or are bound to the micelle or vesicle in both cases.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"11286556","version":4,"reference_html":"Conformational properties of alpha-synuclein in its free and lipid-associated states. <i> Eliezer D, Kutluay E, Bussell R, Browne G. </i> J Mol Biol, 2001","date":"2025-01-13T19:10:27.714Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00070r026","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"132565","entry_name":"phosphatidic acid 16:0"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"73001","entry_name":"1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine"}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":102,"term_name":"lipid binding","released":"2025_06","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Our observations indicate a partition of αS into two functionally distinct regions. The N-terminal region is responsible for lipid binding. The NMR data suggest that the boundary for this region occurs between residues 102 and 103. Interestingly, the first three exons in the coding region of the αS gene encode residues 1 to 102, and a recent report indicates that the lipid binding capacity of αS is distributed across this region of the protein (Perrin et al., 2000). The close correspondence between the exon-defined boundary and the boundary we observe in our NMR data supports a distinct functional role (lipid binding) for this region of αS.","type":"Discussion"}],"term_id":"GO:0008289","curator_id":"vnugnes","start":1,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"11286556","version":5,"reference_html":"Conformational properties of alpha-synuclein in its free and lipid-associated states. <i> Eliezer D, Kutluay E, Bussell R, Browne G. </i> J Mol Biol, 2001","date":"2025-01-13T19:20:03.778Z","reference_source":"pmid","ec_id":"ECO:0006198","region_id":"DP00070r027","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"ChEBI","id":"73001","operator":"and","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"132565","operator":"and","partner_start":null,"partner_end":null}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":140,"region_id":"DP00070r028","start":1,"term_id":"IDPO:0000002","statement":[{"text":"the disordered nature of monomeric α-synuclein is stably preserved in non-neuronal and neuronal cells","type":"Abstract"},{"text":"Our results show that exogenously delivered αSyn exists as an N-terminally acetylated, disordered and highly dynamic monomer in neuronal and non-neuronal cells, without detectable signs of oligomerization, spontaneous aggregation, or targeted degradation.","type":"Discussion"},{"text":"αSyn is disordered in mammalian cells","type":"Article"},{"text":"αSyn is N-terminally acetylated in cells","type":"Article"},{"text":"αSyn interacts with the cytoplasm","type":"Article"},{"text":"αSyn adopts compact structures in cells","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26808899","version":2,"reference_html":"Structural disorder of monomeric α-synuclein persists in mammalian cells. <i> Theillet FX, Binolfi A, Bekei B, Martorana A, Rose HM, Stuiver M, Verzini S, Lorenz D, van Rossum M, Goldfarb D, Selenko P. </i> Nature, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-01-13T19:40:29.296Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":140,"region_id":"DP00070r030","reference_id":"8901511","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Circular dichroism (CD) and Fourier-transform infrared spectroscopy (FTIR) indicate the absence of significant amounts of secondary structure in NACP, while CD and ultraviolet spectroscopy suggest the lack of a hydrophobic core.","type":"Abstract"},{"text":"CD, UV, and FTIR Spectroscopy Indicate NACP Has a “Random Coil” Conformation.","type":"Results"},{"text":"These features indicate that NACP exists as a mixture of rapidly equilibrating extended conformers and is representative of a class of \"natively unfolded\" proteins, many of which potentiate protein-protein interactions.","type":"Abstract"},{"text":"NACP Is a “Natively Unfolded” Protein. The results presented herein provide evidence that, in solution, NACP exists as a mixture of rapidly equilibrating monomeric conformers which, on average, contain little secondary structure and no hydrophobic core. This conclusion is based on spectroscopic and hydrodynamic probes of protein structure, as well as the behavior of the protein in the presence of additives and cosolvents. ","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"circular dichroism evidence used in manual assertion","version":3,"reference_html":"NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. <i> Weinreb PH, Zhen W, Poon AW, Conway KA, Lansbury PT. </i> Biochemistry, 1996","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006200","term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-17T16:02:32.320Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":140,"region_id":"DP00070r031","reference_id":"8901511","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Circular dichroism (CD) and Fourier-transform infrared spectroscopy (FTIR) indicate the absence of significant amounts of secondary structure in NACP, while CD and ultraviolet spectroscopy suggest the lack of a hydrophobic core.","type":"Abstract"},{"text":"CD, UV, and FTIR Spectroscopy Indicate NACP Has a “Random Coil” Conformation.","type":"Results"},{"text":"These features indicate that NACP exists as a mixture of rapidly equilibrating extended conformers and is representative of a class of \"natively unfolded\" proteins, many of which potentiate protein-protein interactions.","type":"Abstract"},{"text":"NACP Is a “Natively Unfolded” Protein. The results presented herein provide evidence that, in solution, NACP exists as a mixture of rapidly equilibrating monomeric conformers which, on average, contain little secondary structure and no hydrophobic core. This conclusion is based on spectroscopic and hydrodynamic probes of protein structure, as well as the behavior of the protein in the presence of additives and cosolvents. ","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"spectrometry evidence used in manual assertion","version":3,"reference_html":"NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. <i> Weinreb PH, Zhen W, Poon AW, Conway KA, Lansbury PT. </i> Biochemistry, 1996","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007731","term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-17T16:02:19.820Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":140,"region_id":"DP00070r032","reference_id":"8901511","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Circular dichroism (CD) and Fourier-transform infrared spectroscopy (FTIR) indicate the absence of significant amounts of secondary structure in NACP, while CD and ultraviolet spectroscopy suggest the lack of a hydrophobic core.","type":"Abstract"},{"text":"CD, UV, and FTIR Spectroscopy Indicate NACP Has a “Random Coil” Conformation.","type":"Results"},{"text":"These features indicate that NACP exists as a mixture of rapidly equilibrating extended conformers and is representative of a class of \"natively unfolded\" proteins, many of which potentiate protein-protein interactions.","type":"Abstract"},{"text":"NACP Is a “Natively Unfolded” Protein. The results presented herein provide evidence that, in solution, NACP exists as a mixture of rapidly equilibrating monomeric conformers which, on average, contain little secondary structure and no hydrophobic core. This conclusion is based on spectroscopic and hydrodynamic probes of protein structure, as well as the behavior of the protein in the presence of additives and cosolvents. ","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","version":3,"reference_html":"NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. <i> Weinreb PH, Zhen W, Poon AW, Conway KA, Lansbury PT. </i> Biochemistry, 1996","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006228","term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-17T16:01:59.455Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Biological process","ec_ontology":"ECO","end":95,"region_id":"DP00070r033","reference_id":"8901511","start":61,"term_id":"GO:1990000","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The “non-Aβ component of Alzheimer's disease amyloid plaque” (NAC) is a minor peptide component of the insoluble fibrillar core of the Alzheimer's disease (AD) neuritic plaque. NAC amyloid fibrils seed the polymerization of Aβ1−40, the major AD amyloid protein. NAC is derived from a 14 kDa precursor protein, designated NACP, a member of a highly conserved family of heat-stable brain-specific acidic proteins which have been suggested to be involved in synapse formation and/or stabilization.","type":"Abstract"},{"text":"This behavior suggests that NAC amyloid may accelerate AD amyloidogenesis by seeding in vivo plaque formation (Han et al., 1995). ","type":"Introduction"},{"text":"NAC is indicated with bold lettering, and the other peptides used in this work (NACP19−48 and NACP96−125) are underlined.","type":"Figure"},{"text":"In contrast to the spectra of the other two peptides, the CD spectrum of a saturated solution (11 μM) of the NAC peptide (NACP61−95) in aqueous buffer indicated a significant degree of β-sheet structure (ca. 35% β, Figure 3B). Similar CD spectra have been measured for aqueous solutions of Aβ amyloid peptides (Barrow & Zagorski, 1991). ","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"circular dichroism evidence used in manual assertion","version":4,"reference_html":"NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. <i> Weinreb PH, Zhen W, Poon AW, Conway KA, Lansbury PT. </i> Biochemistry, 1996","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006200","term_name":"amyloid fibril formation","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-01-13T19:38:20.372Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":102,"region_id":"DP00070r034","reference_id":"11286556","start":1,"term_id":"GO:0008289","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"CD data (Figure 4) confirm that αS undergoes a large conformational transition to an α-helical state in the presence of SDS micelles, as it does in the presence of lipid vesicles, confirming that the protein interacts with the micelles, possibly in a similar fashion.","type":"Results"},{"text":"Far-UV CD data from wild-type αS in the presence and absence of SDS micelles, under conditions and protein concentrations (100 μM) identical to those used in the NMR experiments. A large conformational change is evident, with a high degree of helicity (indicated by the characteristic double minima at 208 and 222 nm) formed in the presence of micelles.","type":"Figure"},{"text":"Lipid vesicles were prepared by mixing equal amounts of freshly procured 1-palmitoyl 2-oleoyl PC and PA in chloroform (Avanti Polar Lipids).","type":"Methods"}],"curator_id":"vnugnes","released":"2025_06","term_ontology":"GO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":5,"reference_html":"Conformational properties of alpha-synuclein in its free and lipid-associated states. <i> Eliezer D, Kutluay E, Bussell R, Browne G. </i> J Mol Biol, 2001","date":"2025-01-13T19:16:01.031Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"lipid binding","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"ChEBI","id":"73001","operator":"and","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"132565","operator":"and","partner_start":null,"partner_end":null}]},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":102,"region_id":"DP00070r035","reference_id":"11286556","start":1,"term_id":"IDPO:0000011","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Our observations indicate a partition of αS into two functionally distinct regions. The N-terminal region is responsible for lipid binding. The NMR data suggest that the boundary for this region occurs between residues 102 and 103. Interestingly, the first three exons in the coding region of the αS gene encode residues 1 to 102, and a recent report indicates that the lipid binding capacity of αS is distributed across this region of the protein (Perrin et al., 2000). The close correspondence between the exon-defined boundary and the boundary we observe in our NMR data supports a distinct functional role (lipid binding) for this region of αS.","type":"Discussion"},{"text":"CD data (Figure 4) confirm that αS undergoes a large conformational transition to an α-helical state in the presence of SDS micelles, as it does in the presence of lipid vesicles, confirming that the protein interacts with the micelles, possibly in a similar fashion.","type":"Results"},{"text":"Far-UV CD data from wild-type αS in the presence and absence of SDS micelles, under conditions and protein concentrations (100 μM) identical to those used in the NMR experiments. A large conformational change is evident, with a high degree of helicity (indicated by the characteristic double minima at 208 and 222 nm) formed in the presence of micelles.","type":"Figure"},{"text":"Thus, it appears that the interaction of αS with synthetic lipid vesicles is quite similar to its interaction with SDS detergent micelles, as nearly identical regions of the protein remain free from or are bound to the micelle or vesicle in both cases.","type":"Results"}],"curator_id":"vnugnes","released":"2025_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":4,"reference_html":"Conformational properties of alpha-synuclein in its free and lipid-associated states. <i> Eliezer D, Kutluay E, Bussell R, Browne G. </i> J Mol Biol, 2001","date":"2025-01-13T19:11:47.772Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"disorder to order","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"73001","entry_name":"1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"132565","entry_name":"phosphatidic acid 16:0"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":103,"region_id":"DP00070r037","reference_id":"11286556","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"To attempt to observe NMR resonances from the remaining, N-terminal 102 residues of αS, we raised the temperature of our sample from 10 to 40 °C. At this temperature, we observe a greater number of residues than at 10 °C, as shown in Figure 6. An examination of these resonances shows that they do not, in general correspond to resonances observed for either the free protein, or the protein in the presence of micelles at 10 °C. The number of backbone resonances visible is more than 100, suggesting that these resonances include the missing N-terminal resonances not observed at 10 °C. Many resonances from the free C-terminal portion of the protein are no longer observed, probably because at this temperature, the exchange of the backbone amide protons (which are unprotected in this unfolded segment of the protein) with solvent protons is far more rapid than at the lower temperature, and leads to the broadening of these signals.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"reference_html":"Conformational properties of alpha-synuclein in its free and lipid-associated states. <i> Eliezer D, Kutluay E, Bussell R, Browne G. </i> J Mol Biol, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-17T16:01:48.692Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":101,"end":140,"reference_id":"33797711","reference_source":"pmid","reference_html":"Partial magic angle spinning NMR <sup>1</sup>H, <sup>13</sup>C, <sup>15</sup>N resonance assignments of the flexible regions of a monomeric alpha-synuclein: conformation of C-terminus in the lipid-bound and amyloid fibril states. <i> Medeiros J, Bamm VV, Jany C, Coackley C, Ward ME, Harauz G, Ryan SD, Ladizhansky V. </i> Biomol NMR Assign, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00070r039","statement":[{"text":"Although the C-terminus is more dynamically constrained in fibrils and in α-syn bound to TOCL:DOPC vesicles, a direct comparison of carbon chemical shifts detected using through bond two-dimensional spectroscopy indicates that the C-terminus is flexible and unstructured in all the three samples.\n","type":"Abstract"},{"text":"The detected backbone chemical shifts indicate that the C-terminus is unstructured when bound to DOPA:DOPC lipid vesicles (Figure S1), in agreement with previous solution and solid-state NMR data (Ulmer et al. 2005; Fusco et al. 2014).\n","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-09T16:11:41.505Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P37840","date":"2016-08-11T15:46:32.000Z","acc":"P37840","name":"Alpha-synuclein","length":140,"organism":"Homo sapiens","dataset":["Condensates-related proteins","Age-related disorders proteins"],"UniParc":"UPI000003173B","genes":[{"name":{"value":"SNCA"},"synonyms":[{"value":"NACP"},{"value":"PARK1"}]}],"alphafold_very_low_content":0.14285714285714285,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":140,"type":"T"}],"Structural state":[{"start":1,"end":140,"type":"D"}],"Molecular function":[{"start":1,"end":140,"type":"F"}],"Structural transition":[{"start":1,"end":140,"type":"T"}],"Biological process":[{"start":61,"end":95,"type":"F"}]}},{"acc":"P23441","sequence":"MSMSPKHTTPFSVSDILSPLEESYKKVGMEGGGLGAPLAAYRQGQAAPPAAAMQQHAVGHHGAVTAAYHMTAAGVPQLSHSAVGGYCNGNLGNMSELPPYQDTMRNSASGPGWYGANPDPRFPAISRFMGPASGMNMSGMGGLGSLGDVSKNMAPLPSAPRRKRRVLFSQAQVYELERRFKQQKYLSAPEREHLASMIHLTPTQVKIWFQNHRYKMKRQAKDKAAQQQLQQDSGGGGGGGGGAGCPQQQQAQQQSPRRVAVPVLVKDGKPCQAGAPAPGAASLQGHAQQQAQQQAQAAQAAAAAISVGSGGAGLGAHPGHQPGSAGQSPDLAHHAASPAALQGQVSSLSHLNSSGSDYGAMSCSTLLYGRTW","alphafold_very_low_content":"0.553763440860215","creator":"eleonardi","dataset":[],"date":"2016-08-22T10:08:55.000Z","disprot_id":"DP00071","features":{"pfam":[{"id":"PF00046","name":"Homeodomain","start":162,"end":218}],"gene3D":[{"start":157,"end":235,"id":"1.10.10.60","name":"Homeodomain-like","_id":"685af523b4ac24d5329d7344"}]},"genes":[{"name":{"value":"Nkx2-1","evidences":[{"source":{"id":"3866","name":"RGD","url":"https://rgd.mcw.edu/tools/genes/genes_view.cgi?id=3866","_id":"685af523b4ac24d5329d7371"},"code":"ECO:0000312","_id":"685af523b4ac24d5329d7370"}],"_id":"685af523b4ac24d5329d7372"},"synonyms":[{"value":"Nkx-2.1","evidences":[],"_id":"685af523b4ac24d5329d7373"},{"value":"Titf1","evidences":[],"_id":"685af523b4ac24d5329d7374"},{"value":"Ttf-1","evidences":[],"_id":"685af523b4ac24d5329d7375"},{"value":"Ttf1","evidences":[],"_id":"685af523b4ac24d5329d7376"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d736f"}],"length":372,"name":"Homeobox protein Nkx-2.1","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions_counter":13,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"UniParc":"UPI0000137790","uniref100":"UniRef100_P23441","uniref50":"UniRef50_P50220","uniref90":"UniRef90_P23441","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":156,"interaction_partner":[],"reference_html":"Structural and functional properties of the N transcriptional activation domain of thyroid transcription factor-1: similarities with the acidic activation domains. <i> Tell G, Perrone L, Fabbro D, Pellizzari L, Pucillo C, De Felice M, Acquaviva R, Formisano S, Damante G. </i> Biochem J, 1998","reference_id":"9425125","region_id":"DP00071r001","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"In fact, under these experimental conditions, the CD trace lacks the characteristic local minima at 208/222 nm (Figure 2, spectrum a).","_id":"685af523b4ac24d5329d7346"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-08T20:37:53.753Z","_id":"685af523b4ac24d5329d7347"},"version":3,"_id":"685af523b4ac24d5329d7345","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":156,"interaction_partner":[],"reference_html":"Structural and functional properties of the N transcriptional activation domain of thyroid transcription factor-1: similarities with the acidic activation domains. <i> Tell G, Perrone L, Fabbro D, Pellizzari L, Pucillo C, De Felice M, Acquaviva R, Formisano S, Damante G. </i> Biochem J, 1998","reference_id":"9425125","region_id":"DP00071r002","released":"2022_03","sample":[{"db":"ChEBI","deviation":null,"entry_name":"2,2,2-trifluoroethanol","id":"42330","statements":[{"type":"Article","text":"Thus spectra were also collected in the presence of TFE to simulate a more hydrophobic milieu.","_id":"685af523b4ac24d5329d734a"}],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7349"}],"statement":[{"type":"Article","text":"The addition of TFE significantly alters the structure of the N domain.","_id":"685af523b4ac24d5329d734b"},{"type":"Article","text":"The amount of induced secondary structure reaches a plateau between 40 and 50% TFE.","_id":"685af523b4ac24d5329d734c"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-08T20:37:56.135Z","_id":"685af523b4ac24d5329d734d"},"version":3,"_id":"685af523b4ac24d5329d7348","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":58,"end":78,"interaction_partner":[],"reference_html":"Structural and functional properties of the N transcriptional activation domain of thyroid transcription factor-1: similarities with the acidic activation domains. <i> Tell G, Perrone L, Fabbro D, Pellizzari L, Pucillo C, De Felice M, Acquaviva R, Formisano S, Damante G. </i> Biochem J, 1998","reference_id":"9425125","region_id":"DP00071r005","released":"2022_03","sample":[{"db":"ChEBI","deviation":null,"entry_name":"2,2,2-trifluoroethanol","id":"42330","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7353"}],"statement":[{"type":"Article","text":"In the presence of 50% TFE, TTF-1 N domain is almost undigested (lane 3), confirming the evidence of gain of secondary structure (α-helix) obtained from CD studies.","_id":"685af523b4ac24d5329d7354"},{"type":"Results","text":"The fragment of approx. 2 kDa was eluted from gel and subjected to N-terminal protein sequencing. The sequence identifies a fragment of 20 residues between residues 58 and 78 (Figure 1, left-hand panel, boxed).","_id":"685af523b4ac24d5329d7355"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-08T20:37:55.285Z","_id":"685af523b4ac24d5329d7356"},"version":3,"_id":"685af523b4ac24d5329d7352","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-21T08:47:50.795Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":156,"interaction_partner":[],"reference_html":"Structural and functional properties of the N transcriptional activation domain of thyroid transcription factor-1: similarities with the acidic activation domains. <i> Tell G, Perrone L, Fabbro D, Pellizzari L, Pucillo C, De Felice M, Acquaviva R, Formisano S, Damante G. </i> Biochem J, 1998","reference_id":"9425125","region_id":"DP00071r011","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"The SDS/PAGE analysis of the proteolysis mixture after 6 h reaction at 25 °C (Figure 3) reveals that, in the absence of TFE, the TTF-1 N domain is completely digested by thermolysin into small peptides which are not stained by Coomassie Blue (lane 2).","_id":"685af523b4ac24d5329d7366"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-08T20:37:53.140Z","_id":"685af523b4ac24d5329d7367"},"version":0,"_id":"685af523b4ac24d5329d7365","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007632","ec_name":"transcriptional activation assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":156,"interaction_partner":[],"reference_html":"Structural and functional properties of the N transcriptional activation domain of thyroid transcription factor-1: similarities with the acidic activation domains. <i> Tell G, Perrone L, Fabbro D, Pellizzari L, Pucillo C, De Felice M, Acquaviva R, Formisano S, Damante G. </i> Biochem J, 1998","reference_id":"9425125","region_id":"DP00071r012","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"Therefore these data indicate that the TTF-1 N domain is able to efficiently activate transcription in yeast, a property typical of acidic activation domains.","_id":"685af523b4ac24d5329d7369"}],"states_connection":[],"term_comment":"For usage guidance, see comment in GO:0003712 ; transcription coregulator activity.","term_def":"\"A transcription coregulator activity that activates or increases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coactivators modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. A fourth class of coactivator activity is the bridging of a DNA-binding transcription factor to the general (basal) transcription machinery. The Mediator complex, which bridges sequence-specific DNA binding transcription factors and RNA polymerase, is also a transcription coactivator.\" [GOC:txnOH-2018, PMID:10213677, PMID:16858867]","term_go_domain":"F","term_id":"GO:0003713","term_is_binding":false,"term_is_obsolete":false,"term_name":"transcription coactivator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-08T20:38:02.415Z","_id":"685af523b4ac24d5329d736a"},"version":1,"_id":"685af523b4ac24d5329d7368","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006077","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":156,"interaction_partner":[{"db":"UniProt","id":"P13393","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d736c"}],"reference_html":"Structural and functional properties of the N transcriptional activation domain of thyroid transcription factor-1: similarities with the acidic activation domains. <i> Tell G, Perrone L, Fabbro D, Pellizzari L, Pucillo C, De Felice M, Acquaviva R, Formisano S, Damante G. </i> Biochem J, 1998","reference_id":"9425125","region_id":"DP00071r013","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"As shown in Figure 7(A), only the N domain was able to retain TBP. This interaction is specific, as confirmed by the SDS/PAGE shown in Figure 7(B), which demonstrates that only the TBP band (arrow) is enriched after elution.","_id":"685af523b4ac24d5329d736d"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-08T20:37:57.954Z","_id":"685af523b4ac24d5329d736e"},"version":1,"_id":"685af523b4ac24d5329d736b","reference_source":"pmid"}],"__v":0,"disorder_content":0.41935483870967744,"disprot_consensus":{"full":[{"start":1,"end":156,"type":"T"}],"Structural state":[{"start":1,"end":156,"type":"D"}],"Structural transition":[{"start":1,"end":156,"type":"T"}],"Molecular function":[{"start":1,"end":156,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00041","name":"Fibronectin type III domain","start":14019,"end":14102},{"id":"PF00041","name":"Fibronectin type III domain","start":14120,"end":14208},{"id":"PF00041","name":"Fibronectin type III domain","start":14220,"end":14307},{"id":"PF00041","name":"Fibronectin type III domain","start":14416,"end":14499},{"id":"PF00041","name":"Fibronectin type III domain","start":14516,"end":14604},{"id":"PF00041","name":"Fibronectin type III domain","start":14713,"end":14798},{"id":"PF00041","name":"Fibronectin type III domain","start":14812,"end":14900},{"id":"PF00041","name":"Fibronectin type III domain","start":14913,"end":15000},{"id":"PF00041","name":"Fibronectin type III domain","start":15012,"end":15097},{"id":"PF00041","name":"Fibronectin type III domain","start":15113,"end":15201},{"id":"PF00041","name":"Fibronectin type III domain","start":15213,"end":15303},{"id":"PF00041","name":"Fibronectin type III domain","start":15411,"end":15491},{"id":"PF00041","name":"Fibronectin type III domain","start":15508,"end":15597},{"id":"PF00041","name":"Fibronectin type III domain","start":15731,"end":15815},{"id":"PF00041","name":"Fibronectin type III domain","start":15831,"end":15919},{"id":"PF00041","name":"Fibronectin type III domain","start":15935,"end":16016},{"id":"PF00041","name":"Fibronectin type III domain","start":16140,"end":16207},{"id":"PF00041","name":"Fibronectin type III domain","start":16224,"end":16313},{"id":"PF00041","name":"Fibronectin type III domain","start":16426,"end":16510},{"id":"PF00041","name":"Fibronectin type III domain","start":16528,"end":16621},{"id":"PF00041","name":"Fibronectin type III domain","start":16634,"end":16722},{"id":"PF00041","name":"Fibronectin type III domain","start":16841,"end":16928},{"id":"PF00041","name":"Fibronectin type III domain","start":16941,"end":17032},{"id":"PF00041","name":"Fibronectin type III domain","start":17147,"end":17229},{"id":"PF00041","name":"Fibronectin type III domain","start":17246,"end":17337},{"id":"PF00041","name":"Fibronectin type III domain","start":17354,"end":17438},{"id":"PF00041","name":"Fibronectin type III domain","start":17552,"end":17630},{"id":"PF00041","name":"Fibronectin type III domain","start":17646,"end":17730},{"id":"PF00041","name":"Fibronectin type III domain","start":17842,"end":17922},{"id":"PF00041","name":"Fibronectin type III domain","start":17940,"end":18029},{"id":"PF00041","name":"Fibronectin type III domain","start":18041,"end":18127},{"id":"PF00041","name":"Fibronectin type III domain","start":18239,"end":18321},{"id":"PF00041","name":"Fibronectin type III domain","start":18339,"end":18420},{"id":"PF00041","name":"Fibronectin type III domain","start":18533,"end":18617},{"id":"PF00041","name":"Fibronectin type III domain","start":18632,"end":18719},{"id":"PF00041","name":"Fibronectin type III domain","start":18733,"end":18819},{"id":"PF00041","name":"Fibronectin type III domain","start":18931,"end":19011},{"id":"PF00041","name":"Fibronectin type III domain","start":19030,"end":19113},{"id":"PF00041","name":"Fibronectin type III domain","start":19226,"end":19310},{"id":"PF00041","name":"Fibronectin type III domain","start":19327,"end":19413},{"id":"PF00041","name":"Fibronectin type III domain","start":19426,"end":19516},{"id":"PF00041","name":"Fibronectin type III domain","start":19628,"end":19710},{"id":"PF00041","name":"Fibronectin type III domain","start":19727,"end":19811},{"id":"PF00041","name":"Fibronectin type III domain","start":19921,"end":20004},{"id":"PF00041","name":"Fibronectin type III domain","start":20020,"end":20109},{"id":"PF00041","name":"Fibronectin type III domain","start":20118,"end":20209},{"id":"PF00041","name":"Fibronectin type III domain","start":20318,"end":20400},{"id":"PF00041","name":"Fibronectin type III domain","start":20423,"end":20504},{"id":"PF00041","name":"Fibronectin type III domain","start":20518,"end":20604},{"id":"PF00041","name":"Fibronectin type III domain","start":20716,"end":20800},{"id":"PF00041","name":"Fibronectin type III domain","start":20813,"end":20898},{"id":"PF00041","name":"Fibronectin type III domain","start":21009,"end":21094},{"id":"PF00041","name":"Fibronectin type III domain","start":21105,"end":21193},{"id":"PF00041","name":"Fibronectin type III domain","start":21202,"end":21292},{"id":"PF00041","name":"Fibronectin type III domain","start":21402,"end":21484},{"id":"PF00041","name":"Fibronectin type III domain","start":21501,"end":21588},{"id":"PF00041","name":"Fibronectin type III domain","start":21602,"end":21686},{"id":"PF00041","name":"Fibronectin type III domain","start":21797,"end":21884},{"id":"PF00041","name":"Fibronectin type III domain","start":21893,"end":21981},{"id":"PF00041","name":"Fibronectin type III domain","start":22088,"end":22170},{"id":"PF00041","name":"Fibronectin type III domain","start":22188,"end":22276},{"id":"PF00041","name":"Fibronectin type III domain","start":22292,"end":22375},{"id":"PF00041","name":"Fibronectin type III domain","start":22484,"end":22567},{"id":"PF00041","name":"Fibronectin type III domain","start":22583,"end":22671},{"id":"PF00041","name":"Fibronectin type III domain","start":22685,"end":22769},{"id":"PF00041","name":"Fibronectin type III domain","start":22881,"end":22966},{"id":"PF00041","name":"Fibronectin type III domain","start":22978,"end":23061},{"id":"PF00041","name":"Fibronectin type III domain","start":23170,"end":23254},{"id":"PF00041","name":"Fibronectin type III domain","start":23270,"end":23358},{"id":"PF00041","name":"Fibronectin type III domain","start":23367,"end":23454},{"id":"PF00041","name":"Fibronectin type III domain","start":23566,"end":23655},{"id":"PF00041","name":"Fibronectin type III domain","start":23665,"end":23753},{"id":"PF00041","name":"Fibronectin type III domain","start":23767,"end":23850},{"id":"PF00041","name":"Fibronectin type III domain","start":23962,"end":24046},{"id":"PF00041","name":"Fibronectin type III domain","start":24060,"end":24145},{"id":"PF00041","name":"Fibronectin type III domain","start":24252,"end":24341},{"id":"PF00041","name":"Fibronectin type III domain","start":24352,"end":24440},{"id":"PF00041","name":"Fibronectin type III domain","start":24458,"end":24535},{"id":"PF00041","name":"Fibronectin type III domain","start":24648,"end":24731},{"id":"PF00041","name":"Fibronectin type III domain","start":24748,"end":24835},{"id":"PF00041","name":"Fibronectin type III domain","start":24849,"end":24937},{"id":"PF00041","name":"Fibronectin type III domain","start":25045,"end":25126},{"id":"PF00041","name":"Fibronectin type III domain","start":25141,"end":25223},{"id":"PF00041","name":"Fibronectin type III domain","start":25335,"end":25416},{"id":"PF00041","name":"Fibronectin type III domain","start":25434,"end":25523},{"id":"PF00041","name":"Fibronectin type III domain","start":25531,"end":25617},{"id":"PF00041","name":"Fibronectin type III domain","start":25731,"end":25814},{"id":"PF00041","name":"Fibronectin type III domain","start":25831,"end":25919},{"id":"PF00041","name":"Fibronectin type III domain","start":25932,"end":26016},{"id":"PF00041","name":"Fibronectin type III domain","start":26127,"end":26214},{"id":"PF00041","name":"Fibronectin type III domain","start":26225,"end":26307},{"id":"PF00041","name":"Fibronectin type III domain","start":26417,"end":26504},{"id":"PF00041","name":"Fibronectin type III domain","start":26516,"end":26602},{"id":"PF00041","name":"Fibronectin type III domain","start":26613,"end":26700},{"id":"PF00041","name":"Fibronectin type III domain","start":26816,"end":26897},{"id":"PF00041","name":"Fibronectin type III domain","start":26911,"end":26998},{"id":"PF00041","name":"Fibronectin type III domain","start":27012,"end":27099},{"id":"PF00041","name":"Fibronectin type III domain","start":27207,"end":27289},{"id":"PF00041","name":"Fibronectin type III domain","start":27303,"end":27386},{"id":"PF00041","name":"Fibronectin type III domain","start":27499,"end":27580},{"id":"PF00041","name":"Fibronectin type III domain","start":27599,"end":27687},{"id":"PF00041","name":"Fibronectin type III domain","start":27697,"end":27783},{"id":"PF00041","name":"Fibronectin type III domain","start":27896,"end":27978},{"id":"PF00041","name":"Fibronectin type III domain","start":27995,"end":28084},{"id":"PF00041","name":"Fibronectin type III domain","start":28096,"end":28180},{"id":"PF00041","name":"Fibronectin type III domain","start":28297,"end":28381},{"id":"PF00041","name":"Fibronectin type III domain","start":28392,"end":28474},{"id":"PF00041","name":"Fibronectin type III domain","start":28586,"end":28668},{"id":"PF00041","name":"Fibronectin type III domain","start":28686,"end":28775},{"id":"PF00041","name":"Fibronectin type III domain","start":28783,"end":28869},{"id":"PF00041","name":"Fibronectin type III domain","start":28985,"end":29064},{"id":"PF00041","name":"Fibronectin type III domain","start":29087,"end":29167},{"id":"PF00041","name":"Fibronectin type III domain","start":29183,"end":29266},{"id":"PF00041","name":"Fibronectin type III domain","start":29378,"end":29460},{"id":"PF00041","name":"Fibronectin type III domain","start":29475,"end":29559},{"id":"PF00041","name":"Fibronectin type III domain","start":29675,"end":29755},{"id":"PF00041","name":"Fibronectin type III domain","start":29769,"end":29857},{"id":"PF00041","name":"Fibronectin type III domain","start":29867,"end":29951},{"id":"PF00041","name":"Fibronectin type III domain","start":30073,"end":30158},{"id":"PF00041","name":"Fibronectin type III domain","start":30181,"end":30258},{"id":"PF00041","name":"Fibronectin type III domain","start":30271,"end":30359},{"id":"PF00041","name":"Fibronectin type III domain","start":30470,"end":30550},{"id":"PF00041","name":"Fibronectin type III domain","start":30565,"end":30652},{"id":"PF00041","name":"Fibronectin type III domain","start":30761,"end":30847},{"id":"PF00041","name":"Fibronectin type III domain","start":30861,"end":30949},{"id":"PF00041","name":"Fibronectin type III domain","start":30962,"end":31047},{"id":"PF00041","name":"Fibronectin type III domain","start":31162,"end":31240},{"id":"PF00041","name":"Fibronectin type III domain","start":31259,"end":31347},{"id":"PF00041","name":"Fibronectin type III domain","start":31359,"end":31444},{"id":"PF00041","name":"Fibronectin type III domain","start":31652,"end":31739},{"id":"PF00041","name":"Fibronectin type III domain","start":31754,"end":31842},{"id":"PF00041","name":"Fibronectin type III domain","start":32050,"end":32138},{"id":"PF00069","name":"Protein kinase domain","start":32179,"end":32432},{"id":"PF02818","name":"PPAK motif","start":10503,"end":10529},{"id":"PF02818","name":"PPAK motif","start":10587,"end":10613},{"id":"PF02818","name":"PPAK motif","start":10615,"end":10641},{"id":"PF02818","name":"PPAK motif","start":10762,"end":10787},{"id":"PF02818","name":"PPAK motif","start":10901,"end":10925},{"id":"PF02818","name":"PPAK motif","start":10927,"end":10953},{"id":"PF02818","name":"PPAK motif","start":10955,"end":10981},{"id":"PF02818","name":"PPAK motif","start":10983,"end":11009},{"id":"PF02818","name":"PPAK motif","start":11698,"end":11724},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":6,"end":97},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":104,"end":193},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":944,"end":1032},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":1082,"end":1171},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":1293,"end":1381},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":1457,"end":1547},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":1556,"end":1647},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":1704,"end":1794},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":1842,"end":1929},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":2078,"end":2168},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":2175,"end":2259},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":2268,"end":2343},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":2358,"end":2428},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":2447,"end":2528},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":2534,"end":2609},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":2622,"end":2703},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":2708,"end":2778},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":2796,"end":2878},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":2883,"end":2963},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":2971,"end":3051},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":3059,"end":3137},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":3239,"end":3328},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":3345,"end":3432},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":3504,"end":3592},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":3621,"end":3711},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":4289,"end":4377},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":4383,"end":4472},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":4478,"end":4567},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":4571,"end":4660},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":4665,"end":4752},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":4758,"end":4843},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":4851,"end":4940},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":4946,"end":5033},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":5040,"end":5128},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":5133,"end":5222},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":5228,"end":5315},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":5320,"end":5408},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":5413,"end":5502},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":5508,"end":5595},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":5602,"end":5691},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":5695,"end":5784},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":5788,"end":5878},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":5882,"end":5969},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":5975,"end":6064},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":6069,"end":6157},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":6164,"end":6253},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":6257,"end":6346},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":6350,"end":6440},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":6444,"end":6532},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":6537,"end":6627},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":6633,"end":6720},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":6727,"end":6816},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":6820,"end":6909},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":6914,"end":6998},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":7006,"end":7091},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":7102,"end":7190},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":7198,"end":7287},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":7291,"end":7381},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":7385,"end":7473},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":7478,"end":7568},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":7573,"end":7661},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":7668,"end":7757},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":7761,"end":7850},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":7855,"end":7943},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":7947,"end":8035},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":8043,"end":8130},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":8139,"end":8228},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":8232,"end":8322},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":8327,"end":8409},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":8419,"end":8509},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":8514,"end":8602},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":8609,"end":8698},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":8702,"end":8790},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":8796,"end":8882},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":8888,"end":8977},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":8984,"end":9071},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":9080,"end":9169},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":9176,"end":9263},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":9273,"end":9362},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":9383,"end":9471},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":9586,"end":9657},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":9674,"end":9747},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":9762,"end":9848},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":12059,"end":12134},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":12237,"end":12309},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":12415,"end":12488},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":12502,"end":12577},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":12590,"end":12672},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":12769,"end":12844},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":12857,"end":12937},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":12945,"end":13017},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":13127,"end":13197},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":13213,"end":13287},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":13302,"end":13375},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":13391,"end":13463},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":13480,"end":13552},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":13568,"end":13654},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":13662,"end":13735},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":13751,"end":13826},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":13840,"end":13916},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":13927,"end":14013},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":14341,"end":14411},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":14625,"end":14707},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":15314,"end":15403},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":15615,"end":15725},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":16041,"end":16120},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":16334,"end":16421},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":16747,"end":16835},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":17053,"end":17140},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":17459,"end":17539},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":17754,"end":17835},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":18153,"end":18233},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":18445,"end":18527},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":18844,"end":18925},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":19137,"end":19220},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":19543,"end":19622},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":19832,"end":19915},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":20232,"end":20312},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":20630,"end":20710},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":20921,"end":20999},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":21315,"end":21396},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":21711,"end":21791},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":22002,"end":22082},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":22397,"end":22478},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":22797,"end":22875},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":23076,"end":23164},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":23479,"end":23560},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":23879,"end":23957},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":24163,"end":24243},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":24560,"end":24642},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":24959,"end":25039},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":25244,"end":25328},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":25643,"end":25725},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":26043,"end":26122},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":26324,"end":26410},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":26725,"end":26806},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":27121,"end":27201},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":27410,"end":27491},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":27808,"end":27889},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":28207,"end":28288},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":28498,"end":28569},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":28896,"end":28975},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":29293,"end":29372},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":29583,"end":29664},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":29984,"end":30064},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":30381,"end":30461},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":30672,"end":30754},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":31073,"end":31151},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":31461,"end":31547},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":31568,"end":31645},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":31855,"end":31946},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":31963,"end":32045},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":32503,"end":32585},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":32617,"end":32709},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":32722,"end":32812},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":33301,"end":33390},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":33489,"end":33577},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":33658,"end":33732},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":33779,"end":33868},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":33969,"end":34052},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":34061,"end":34150},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":34256,"end":34347},{"id":"PF09042","name":"Titin Z","start":418,"end":454},{"id":"PF09042","name":"Titin Z","start":693,"end":739},{"id":"PF18362","name":"Tri-helix bundle domain","start":9505,"end":9535}],"gene3D":[{"start":22878,"end":22972,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":26611,"end":26712,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":18040,"end":18141,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":21597,"end":21694,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":25823,"end":25926,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":16937,"end":17039,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":21201,"end":21301,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":3145,"end":3236,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":12500,"end":12589,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":12322,"end":12411,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":24645,"end":24741,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":12677,"end":12765,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":8326,"end":8416,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":5973,"end":6066,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":8887,"end":8981,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":5226,"end":5318,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":7667,"end":7760,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":16525,"end":16631,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":24745,"end":24846,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":21002,"end":21097,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":25728,"end":25820,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":19025,"end":19125,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":4288,"end":4378,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":7854,"end":7945,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":5038,"end":5132,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":4477,"end":4569,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":14420,"end":14514,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":19627,"end":19723,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":17239,"end":17343,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":2968,"end":3054,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":2442,"end":2532,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":25331,"end":25426,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":18236,"end":18330,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":19724,"end":19822,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1835,"end":1937,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":7004,"end":7099,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":8512,"end":8607,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":8794,"end":8886,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":26419,"end":26513,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":16632,"end":16741,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":14220,"end":14329,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":20810,"end":20914,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":9673,"end":9758,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":13121,"end":13209,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":18730,"end":18830,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":8135,"end":8230,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1288,"end":1384,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":5599,"end":5694,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":940,"end":1045,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":5695,"end":5787,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":12135,"end":12229,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":24847,"end":24959,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":25431,"end":25528,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":23960,"end":24054,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":7478,"end":7570,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":6537,"end":6629,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":8417,"end":8511,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":3618,"end":3714,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":22577,"end":22679,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":25927,"end":26029,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":15210,"end":15311,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":15828,"end":15924,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":20408,"end":20511,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":20117,"end":20216,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":12854,"end":12944,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":2621,"end":2706,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":22481,"end":22575,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":21794,"end":21890,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1081,"end":1192,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1,"end":98,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":7761,"end":7853,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":3498,"end":3606,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":6726,"end":6819,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":26514,"end":26610,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":20018,"end":20116,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":6351,"end":6444,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":99,"end":209,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":7571,"end":7666,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":4379,"end":4476,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":14810,"end":14908,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":22975,"end":23079,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":12234,"end":12321,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":2707,"end":2794,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":12590,"end":12676,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":19918,"end":20013,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":7946,"end":8036,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":3055,"end":3144,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":6257,"end":6350,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":6067,"end":6162,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1552,"end":1659,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":5133,"end":5225,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":15729,"end":15827,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":21102,"end":21200,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":23363,"end":23466,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":2171,"end":2265,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":13210,"end":13298,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":23167,"end":23262,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":21399,"end":21495,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":16424,"end":16521,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":22680,"end":22775,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":6630,"end":6725,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":9272,"end":9374,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":4847,"end":4944,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":6445,"end":6536,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":14118,"end":14219,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":21499,"end":21596,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":25048,"end":25135,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":9580,"end":9671,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":2073,"end":2170,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":2266,"end":2352,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":12945,"end":13031,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":2881,"end":2967,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":2533,"end":2620,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":24249,"end":24343,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":19223,"end":19320,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":17141,"end":17238,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":23563,"end":23660,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":17542,"end":17638,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":17838,"end":17935,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":9375,"end":9474,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":7195,"end":7292,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":5882,"end":5972,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":9074,"end":9174,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":9175,"end":9271,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":7100,"end":7191,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":15111,"end":15209,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":14018,"end":14117,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":18632,"end":18729,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":18535,"end":18631,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":3237,"end":3331,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":8231,"end":8325,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":17344,"end":17447,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":23264,"end":23362,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":23661,"end":23758,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":24344,"end":24444,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":20512,"end":20612,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":14909,"end":15009,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":12766,"end":12853,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":13299,"end":13388,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":3346,"end":3454,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":22083,"end":22179,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":5319,"end":5411,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":6163,"end":6256,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":6820,"end":6912,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":8608,"end":8701,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":5412,"end":5506,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":8982,"end":9073,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":16838,"end":16936,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":15011,"end":15110,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":18930,"end":19024,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":12412,"end":12499,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":2353,"end":2441,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":20713,"end":20808,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":20315,"end":20407,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":24055,"end":24152,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":4663,"end":4755,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":7385,"end":7477,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":7293,"end":7384,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":8702,"end":8793,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":8037,"end":8132,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":18337,"end":18444,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":17938,"end":18039,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":21891,"end":21997,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":15406,"end":15503,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":23759,"end":23864,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":19421,"end":19527,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":4756,"end":4846,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":4570,"end":4662,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":24445,"end":24548,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":16215,"end":16320,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":15925,"end":16026,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":9759,"end":9854,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":12037,"end":12134,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":16123,"end":16212,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":26125,"end":26219,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":14709,"end":14804,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":25136,"end":25231,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":5788,"end":5881,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":4945,"end":5037,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":5507,"end":5598,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":6913,"end":7003,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":14515,"end":14621,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":19322,"end":19420,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":26909,"end":27009,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1451,"end":1551,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1697,"end":1798,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":22182,"end":22280,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":15504,"end":15603,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":25529,"end":25630,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":26220,"end":26318,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":17639,"end":17743,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":22281,"end":22384,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":2795,"end":2880,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":13032,"end":13120,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":32257,"end":32492,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"},{"start":32172,"end":32255,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"}]},"uniref50":"UniRef50_Q8WZ42","sequence":"MTTQAPTFTQPLQSVVVLEGSTATFEAHISGFPVPEVSWFRDGQVISTSTLPGVQISFSDGRAKLTIPAVTKANSGRYSLKATNGSGQATSTAELLVKAETAPPNFVQRLQSMTVRQGSQVRLQVRVTGIPTPVVKFYRDGAEIQSSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATNSVGRATSTAELLVQGEEEVPAKKTKTIVSTAQISESRQTRIEKKIEAHFDARSIATVEMVIDGAAGQQLPHKTPPRIPPKPKSRSPTPPSIAAKAQLARQQSPSPIRHSPSPVRHVRAPTPSPVRSVSPAARISTSPIRSVRSPLLMRKTQASTVATGPEVPPPWKQEGYVASSSEAEMRETTLTTSTQIRTEERWEGRYGVQEQVTISGAAGAAASVSASASYAAEAVATGAKEVKQDADKSAAVATVVAAVDMARVREPVISAVEQTAQRTTTTAVHIQPAQEQVRKEAEKTAVTKVVVAADKAKEQELKSRTKEVITTKQEQMHVTHEQIRKETEKTFVPKVVISAAKAKEQETRISEEITKKQKQVTQEAIRQETEITAASMVVVATAKSTKLETVPGAQEETTTQQDQMHLSYEKIMKETRKTVVPKVIVATPKVKEQDLVSRGREGITTKREQVQITQEKMRKEAEKTALSTIAVATAKAKEQETILRTRETMATRQEQIQVTHGKVDVGKKAEAVATVVAAVDQARVREPREPGHLEESYAQQTTLEYGYKERISAAKVAEPPQRPASEPHVVPKAVKPRVIQAPSETHIKTTDQKGMHISSQIKKTTDLTTERLVHVDKRPRTASPHFTVSKISVPKTEHGYEASIAGSAIATLQKELSATSSAQKITKSVKAPTVKPSETRVRAEPTPLPQFPFADTPDTYKSEAGVEVKKEVGVSITGTTVREERFEVLHGREAKVTETARVPAPVEIPVTPPTLVSGLKNVTVIEGESVTLECHISGYPSPTVTWYREDYQIESSIDFQITFQSGIARLMIREAFAEDSGRFTCSAVNEAGTVSTSCYLAVQVSEEFEKETTAVTEKFTTEEKRFVESRDVVMTDTSLTEEQAGPGEPAAPYFITKPVVQKLVEGGSVVFGCQVGGNPKPHVYWKKSGVPLTTGYRYKVSYNKQTGECKLVISMTFADDAGEYTIVVRNKHGETSASASLLEEADYELLMKSQQEMLYQTQVTAFVQEPKVGETAPGFVYSEYEKEYEKEQALIRKKMAKDTVVVRTYVEDQEFHISSFEERLIKEIEYRIIKTTLEELLEEDGEEKMAVDISESEAVESGFDSRIKNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIKHGERYQMDFLQDGRASLRIPVVLPEDEGIYTAFASNIKGNAICSGKLYVEPAAPLGAPTYIPTLEPVSRIRSLSPRSVSRSPIRMSPARMSPARMSPARMSPARMSPGRRLEETDESQLERLYKPVFVLKPVSFKCLEGQTARFDLKVVGRPMPETFWFHDGQQIVNDYTHKVVIKEDGTQSLIIVPATPSDSGEWTVVAQNRAGRSSISVILTVEAVEHQVKPMFVEKLKNVNIKEGSRLEMKVRATGNPNPDIVWLKNSDIIVPHKYPKIRIEGTKGEAALKIDSTVSQDSAWYTATAINKAGRDTTRCKVNVEVEFAEPEPERKLIIPRGTYRAKEIAAPELEPLHLRYGQEQWEEGDLYDKEKQQKPFFKKKLTSLRLKRFGPAHFECRLTPIGDPTMVVEWLHDGKPLEAANRLRMINEFGYCSLDYGVAYSRDSGIITCRATNKYGTDHTSATLIVKDEKSLVEESQLPEGRKGLQRIEELERMAHEGALTGVTTDQKEKQKPDIVLYPEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFRVRYDGIHYLDIVDCKSYDTGEVKVTAENPEGVIEHKVKLEIQQREDFRSVLRRAPEPRPEFHVHEPGKLQFEVQKVDRPVDTTETKEVVKLKRAERITHEKVPEESEELRSKFKRRTEEGYYEAITAVELKSRKKDESYEELLRKTKDELLHWTKELTEEEKKALAEEGKITIPTFKPDKIELSPSMEAPKIFERIQSQTVGQGSDAHFRVRVVGKPDPECEWYKNGVKIERSDRIYWYWPEDNVCELVIRDVTAEDSASIMVKAINIAGETSSHAFLLVQAKQLITFTQELQDVVAKEKDTMATFECETSEPFVKVKWYKDGMEVHEGDKYRMHSDRKVHFLSILTIDTSDAEDYSCVLVEDENVKTTAKLIVEGAVVEFVKELQDIEVPESYSGELECIVSPENIEGKWYHNDVELKSNGKYTITSRRGRQNLTVKDVTKEDQGEYSFVIDGKKTTCKLKMKPRPIAILQGLSDQKVCEGDIVQLEVKVSLESVEGVWMKDGQEVQPSDRVHIVIDKQSHMLLIEDMTKEDAGNYSFTIPALGLSTSGRVSVYSVDVITPLKDVNVIEGTKAVLECKVSVPDVTSVKWYLNDEQIKPDDRVQAIVKGTKQRLVINRTHASDEGPYKLIVGRVETNCNLSVEKIKIIRGLRDLTCTETQNVVFEVELSHSGIDVLWNFKDKEIKPSSKYKIEAHGKIYKLTVLNMMKDDEGKYTFYAGENMTSGKLTVAGGAISKPLTDQTVAESQEAVFECEVANPDSKGEWLRDGKHLPLTNNIRSESDGHKRRLIIAATKLDDIGEYTYKVATSKTSAKLKVEAVKIKKTLKNLTVTETQDAVFTVELTHPNVKGVQWIKNGVVLESNEKYAISVKGTIYSLRIKNCAIVDESVYGFRLGRLGASARLHVETVKIIKKPKDVTALENATVAFEVSVSHDTVPVKWFHKSVEIKPSDKHRLVSERKVHKLMLQNISPSDAGEYTAVVGQLECKAKLFVETLHITKTMKNIEVPETKTASFECEVSHFNVPSMWLKNGVEIEMSEKFKIVVQGKLHQLIIMNTSTEDSAEYTFVCGNDQVSATLTVTPIMITSMLKDINAEEKDTITFEVTVNYEGISYKWLKNGVEIKSTDKCQMRTKKLTHSLNIRNVHFGDAADYTFVAGKATSTATLYVEARHIEFRKHIKDIKVLEKKRAMFECEVSEPDITVQWMKDDQELQITDRIKIQKEKYVHRLLIPSTRMSDAGKYTVVAGGNVSTAKLFVEGRDVRIRSIKKEVQVIEKQRAVVEFEVNEDDVDAHWYKDGIEINFQVQERHKYVVERRIHRMFISETRQSDAGEYTFVAGRNRSSVTLYVNAPEPPQVLQELQPVTVQSGKPARFCAVISGRPQPKISWYKEEQLLSTGFKCKFLHDGQEYTLLLIEAFPEDAAVYTCEAKNDYGVATTSASLSVEVPEVVSPDQEMPVYPPAIITPLQDTVTSEGQPARFQCRVSGTDLKVSWYSKDKKIKPSRFFRMTQFEDTYQLEIAEAYPEDEGTYTFVASNAVGQVSSTANLSLEAPESILHERIEQEIEMEMKEFSSSFLSAEEEGLHSAELQLSKINETLELLSESPVYPTKFDSEKEGTGPIFIKEVSNADISMGDVATLSVTVIGIPKPKIQWFFNGVLLTPSADYKFVFDGDDHSLIILFTKLEDEGEYTCMASNDYGKTICSAYLKINSKGEGHKDTETESAVAKSLEKLGGPCPPHFLKELKPIRCAQGLPAIFEYTVVGEPAPTVTWFKENKQLCTSVYYTIIHNPNGSGTFIVNDPQREDSGLYICKAENMLGESTCAAELLVLLEDTDMTDTPCKAKSTPEAPEDFPQTPLKGPAVEALDSEQEIATFVKDTILKAALITEENQQLSYEHIAKANELSSQLPLGAQELQSILEQDKLTPESTREFLCINGSIHFQPLKEPSPNLQLQIVQSQKTFSKEGILMPEEPETQAVLSDTEKIFPSAMSIEQINSLTVEPLKTLLAEPEGNYPQSSIEPPMHSYLTSVAEEVLSPKEKTVSDTNREQRVTLQKQEAQSALILSQSLAEGHVESLQSPDVMISQVNYEPLVPSEHSCTEGGKILIESANPLENAGQDSAVRIEEGKSLRFPLALEEKQVLLKEEHSDNVVMPPDQIIESKREPVAIKKVQEVQGRDLLSKESLLSGIPEEQRLNLKIQICRALQAAVASEQPGLFSEWLRNIEKVEVEAVNITQEPRHIMCMYLVTSAKSVTEEVTIIIEDVDPQMANLKMELRDALCAIIYEEIDILTAEGPRIQQGAKTSLQEEMDSFSGSQKVEPITEPEVESKYLISTEEVSYFNVQSRVKYLDATPVTKGVASAVVSDEKQDESLKPSEEKEESSSESGTEEVATVKIQEAEGGLIKEDGPMIHTPLVDTVSEEGDIVHLTTSITNAKEVNWYFENKLVPSDEKFKCLQDQNTYTLVIDKVNTEDHQGEYVCEALNDSGKTATSAKLTVVKRAAPVIKRKIEPLEVALGHLAKFTCEIQSAPNVRFQWFKAGREIYESDKCSIRSSKYISSLEILRTQVVDCGEYTCKASNEYGSVSCTATLTVTEAYPPTFLSRPKSLTTFVGKAAKFICTVTGTPVIETIWQKDGAALSPSPNWRISDAENKHILELSNLTIQDRGVYSCKASNKFGADICQAELIIIDKPHFIKELEPVQSAINKKVHLECQVDEDRKVTVTWSKDGQKLPPGKDYKICFEDKIATLEIPLAKLKDSGTYVCTASNEAGSSSCSATVTVREPPSFVKKVDPSYLMLPGESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMYFVNSEAILDITDVKVEDSGSYSCEAVNDVGSDSCSTEIVIKEPPSFIKTLEPADIVRGTNALLQCEVSGTGPFEISWFKDKKQIRSSKKYRLFSQKSLVCLEIFSFNSADVGEYECVVANEVGKCGCMATHLLKEPPTFVKKVDDLIALGGQTVTLQAAVRGSEPISVTWMKGQEVIREDGKIKMSFSNGVAVLIIPDVQISFGGKYTCLAENEAGSQTSVGELIVKEPAKIIERAELIQVTAGDPATLEYTVAGTPELKPKWYKDGRPLVASKKYRISFKNNVAQLKFYSAELHDSGQYTFEISNEVGSSSCETTFTVLDRDIAPFFTKPLRNVDSVVNGTCRLDCKIAGSLPMRVSWFKDGKEIAASDRYRIAFVEGTASLEIIRVDMNDAGNFTCRATNSVGSKDSSGALIVQEPPSFVTKPGSKDVLPGSAVCLKSTFQGSTPLTIRWFKGNKELVSGGSCYITKEALESSLELYLVKTSDSGTYTCKVSNVAGGVECSANLFVKEPATFVEKLEPSQLLKKGDATQLACKVTGTPPIKITWFANDREIKESSKHRMSFVESTAVLRLTDVGIEDSGEYMCEAQNEAGSDHCSSIVIVKESPYFTKEFKPIEVLKEYDVMLLAEVAGTPPFEITWFKDNTILRSGRKYKTFIQDHLVSLQILKFVAADAGEYQCRVTNEVGSSICSARVTLREPPSFIKKIESTSSLRGGTAAFQATLKGSLPITVTWLKDSDEITEDDNIRMTFENNVASLYLSGIEVKHDGKYVCQAKNDAGIQRCSALLSVKEPATITEEAVSIDVTQGDPATLQVKFSGTKEITAKWFKDGQELTLGSKYKISVTDTVSILKIISTEKKDSGEYTFEVQNDVGRSSCKARINVLDLIIPPSFTKKLKKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEISASEKYKFSFHDNTAFLEISQLEGTDSGTYTCSATNKAGHNQCSGHLTVKEPPYFVEKPQSQDVNPNTRVQLKALVGGTAPMTIKWFKDNKELHSGAARSVWKDDTSTSLELFAAKATDSGTYICQLSNDVGTATSKATLFVKEPPQFIKKPSPVLVLRNGQSTTFECQITGTPKIRVSWYLDGNEITAIQKHGISFIDGLATFQISGARVENSGTYVCEARNDAGTASCSIELKVKEPPTFIRELKPVEVVKYSDVELECEVTGTPPFEVTWLKNNREIRSSKKYTLTDRVSVFNLHITKCDPSDTGEYQCIVSNEGGSCSCSTRVALKEPPSFIKKIENTTTVLKSSATFQSTVAGSPPISITWLKDDQILDEDDNVYISFVDSVATLQIRSVDNGHSGRYTCQAKNESGVERCYAFLLVQEPAQIVEKAKSVDVTEKDPMTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDFGSSSCDAYLRVLDQNIPPSFTKKLTKMDKVLGSSIHMECKVSGSLPISAQWFKDGKEISTSAKYRLVCHERSVSLEVNNLELEDTANYTCKVSNVAGDDACSGILTVKEPPSFLVKPGRQQAIPDSTVEFKAILKGTPPFKIKWFKDDVELVSGPKCFIGLEGSTSFLNLYSVDASKTGQYTCHVTNDVGSDSCTTMLLVTEPPKFVKKLEASKIVKAGDSSRLECKIAGSPEIRVVWFRNEHELPASDKYRMTFIDSVAVIQMNNLSTEDSGDFICEAQNPAGSTSCSTKVIVKEPPVFSSFPPIVETLKNAEVSLECELSGTPPFEVVWYKDKRQLRSSKKYKIASKNFHTSIHILNVDTSDIGEYHCKAQNEVGSDTCVCTVKLKEPPRFVSKLNSLTVVAGEPAELQASIEGAQPIFVQWLKEKEEVIRESENIRITFVENVATLQFAKAEPANAGKYICQIKNDGGMRENMATLMVLEPAVIVEKAGPMTVTVGETCTLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNKISSLRILSVERQDAGTYTFQVQNNVGKSSCTAVVDVSDRAVPPSFTRRLKNTGGVLGASCILECKVAGSSPISVAWFHEKTKIVSGAKYQTTFSDNVCTLQLNSLDSSDMGNYTCVAANVAGSDECRAVLTVQEPPSFVKEPEPLEVLPGKNVTFTSVIRGTPPFKVNWFRGARELVKGDRCNIYFEDTVAELELFNIDISQSGEYTCVVSNNAGQASCTTRLFVKEPAAFLKRLSDHSVEPGKSIILESTYTGTLPISVTWKKDGFNITTSEKCNIVTTEKTCILEILNSTKRDAGQYSCEIENEAGRDVCGALVSTLEPPYFVTELEPLEAAVGDSVSLQCQVAGTPEITVSWYKGDTKLRPTPEYRTYFTNNVATLVFNKVNINDSGEYTCKAENSIGTASSKTVFRIQERQLPPSFARQLKDIEQTVGLPVTLTCRLNGSAPIQVCWYRDGVLLRDDENLQTSFVDNVATLKILQTDLSHSGQYSCSASNPLGTASSSARLTAREPKKSPFFDIKPVSIDVIAGESADFECHVTGAQPMRITWSKDNKEIRPGGNYTITCVGNTPHLRILKVGKGDSGQYTCQATNDVGKDMCSAQLSVKEPPKFVKKLEASKVAKQGESIQLECKISGSPEIKVSWFRNDSELHESWKYNMSFINSVALLTINEASAEDSGDYICEAHNGVGDASCSTALTVKAPPVFTQKPSPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRNSKKFKITSKHFDTSLHILNLEASDVGEYHCKATNEVGSDTCSCSVKFKEPPRFVKKLSDTSTLIGDAVELRAIVEGFQPISVVWLKDRGEVIRESENTRISFIDNIATLQLGSPEASNSGKYICQIKNDAGMRECSAVLTVLEPARIIEKPEPMTVTTGNPFALECVVTGTPELSAKWFKDGRELSADSKHHITFINKVASLKIPCAEMSDKGLYSFEVKNSVGKSNCTVSVHVSDRIVPPSFIRKLKDVNAILGASVVLECRVSGSAPISVGWFQDGNEIVSGPKCQSSFSENVCTLNLSLLEPSDTGIYTCVAANVAGSDECSAVLTVQEPPSFEQTPDSVEVLPGMSLTFTSVIRGTPPFKVKWFKGSRELVPGESCNISLEDFVTELELFEVQPLESGDYSCLVTNDAGSASCTTHLFVKEPATFVKRLADFSVETGSPIVLEATYTGTPPISVSWIKDEYLISQSERCSITMTEKSTILEILESTIEDYAQYSCLIENEAGQDICEALVSVLEPPYFIEPLEHVEAVIGEPATLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYSCKADNSVGAVASSAVLVIKARKLPPFFARKLKDVHETLGFPVAFECRINGSEPLQVSWYKDGVLLKDDANLQTSFVHNVATLQILQTDQSHIGQYNCSASNPLGTASSSAKLILSEHEVPPFFDLKPVSVDLALGESGTFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVENTATLTVLKVGKGDAGQYTCYASNIAGKDSCSAQLGVQEPPRFIKKLEPSRIVKQDEFTRYECKIGGSPEIKVLWYKDETEIQESSKFRMSFVDSVAVLEMHNLSVEDSGDYTCEAHNAAGSASSSTSLKVKEPPIFRKKPHPIETLKGADVHLECELQGTPPFHVSWYKDKRELRSGKKYKIMSENFLTSIHILNVDAADIGEYQCKATNDVGSDTCVGSIALKAPPRFVKKLSDISTVVGKEVQLQTTIEGAEPISVVWFKDKGEIVRESDNIWISYSENIATLQFSRVEPANAGKYTCQIKNDAGMQECFATLSVLEPATIVEKPESIKVTTGDTCTLECTVAGTPELSTKWFKDGKELTSDNKYKISFFNKVSGLKIINVAPSDSGVYSFEVQNPVGKDSCTASLQVSDRTVPPSFTRKLKETNGLSGSSVVMECKVYGSPPISVSWFHEGNEISSGRKYQTTLTDNTCALTVNMLEESDSGDYTCIATNMAGSDECSAPLTVREPPSFVQKPDPMDVLTGTNVTFTSIVKGTPPFSVSWFKGSSELVPGDRCNVSLEDSVAELELFDVDTSQSGEYTCIVSNEAGKASCTTHLYIKAPAKFVKRLNDYSIEKGKPLILEGTFTGTPPISVTWKKNGINVTPSQRCNITTTEKSAILEIPSSTVEDAGQYNCYIENASGKDSCSAQILILEPPYFVKQLEPVKVSVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTTYKMHFRNNVATLVFNQVDINDSGEYICKAENSVGEVSASTFLTVQEQKLPPSFSRQLRDVQETVGLPVVFDCAISGSEPISVSWYKDGKPLKDSPNVQTSFLDNTATLNIFKTDRSLAGQYSCTATNPIGSASSSARLILTEGKNPPFFDIRLAPVDAVVGESADFECHVTGTQPIKVSWAKDSREIRSGGKYQISYLENSAHLTVLKVDKGDSGQYTCYAVNEVGKDSCTAQLNIKERLIPPSFTKRLSETVEETEGNSFKLEGRVAGSQPITVAWYKNNIEIQPTSNCEITFKNNTLVLQVRKAGMNDAGLYTCKVSNDAGSALCTSSIVIKEPKKPPVFDQHLTPVTVSEGEYVQLSCHVQGSEPIRIQWLKAGREIKPSDRCSFSFASGTAVLELRDVAKADSGDYVCKASNVAGSDTTKSKVTIKDKPAVAPATKKAAVDGRLFFVSEPQSIRVVEKTTATFIAKVGGDPIPNVKWTKGKWRQLNQGGRVFIHQKGDEAKLEIRDTTKTDSGLYRCVAFNEHGEIESNVNLQVDERKKQEKIEGDLRAMLKKTPILKKGAGEEEEIDIMELLKNVDPKEYEKYARMYGITDFRGLLQAFELLKQSQEEETHRLEIEEIERSERDEKEFEELVSFIQQRLSQTEPVTLIKDIENQTVLKDNDAVFEIDIKINYPEIKLSWYKGTEKLEPSDKFEISIDGDRHTLRVKNCQLKDQGNYRLVCGPHIASAKLTVIEPAWERHLQDVTLKEGQTCTMTCQFSVPNVKSEWFRNGRILKPQGRHKTEVEHKVHKLTIADVRAEDQGQYTCKYEDLETSAELRIEAEPIQFTKRIQNIVVSEHQSATFECEVSFDDAIVTWYKGPTELTESQKYNFRNDGRCHYMTIHNVTPDDEGVYSVIARLEPRGEARSTAELYLTTKEIKLELKPPDIPDSRVPIPTMPIRAVPPEEIPPVVAPPIPLLLPTPEEKKPPPKRIEVTKKAVKKDAKKVVAKPKEMTPREEIVKKPPPPTTLIPAKAPEIIDVSSKAEEVKIMTITRKKEVQKEKEAVYEKKQAVHKEKRVFIESFEEPYDELEVEPYTEPFEQPYYEEPDEDYEEIKVEAKKEVHEEWEEDFEEGQEYYEREEGYDEGEEEWEEAYQEREVIQVQKEVYEESHERKVPAKVPEKKAPPPPKVIKKPVIEKIEKTSRRMEEEKVQVTKVPEVSKKIVPQKPSRTPVQEEVIEVKVPAVHTKKMVISEEKMFFASHTEEEVSVTVPEVQKEIVTEEKIHVAISKRVEPPPKVPELPEKPAPEEVAPVPIPKKVEPPAPKVPEVPKKPVPEEKKPVPVPKKEPAAPPKVPEVPKKPVPEEKIPVPVAKKKEAPPAKVPEVQKGVVTEEKITIVTQREESPPPAVPEIPKKKVPEERKPVPRKEEEVPPPPKVPALPKKPVPEEKVAVPVPVAKKAPPPRAEVSKKTVVEEKRFVAEEKLSFAVPQRVEVTRHEVSAEEEWSYSEEEEGVSISVYREEEREEEEEAEVTEYEVMEEPEEYVVEEKLHIISKRVEAEPAEVTERQEKKIVLKPKIPAKIEEPPPAKVPEAPKKIVPEKKVPAPVPKKEKVPPPKVPEEPKKPVPEKKVPPKVIKMEEPLPAKVTERHMQITQEEKVLVAVTKKEAPPKARVPEEPKRAVPEEKVLKLKPKREEEPPAKVTEFRKRVVKEEKVSIEAPKREPQPIKEVTIMEEKERAYTLEEEAVSVQREEEYEEYEEYDYKEFEEYEPTEEYDQYEEYEEREYERYEEHEEYITEPEKPIPVKPVPEEPVPTKPKAPPAKVLKKAVPEEKVPVPIPKKLKPPPPKVPEEPKKVFEEKIRISITKREKEQVTEPAAKVPMKPKRVVAEEKVPVPRKEVAPPVRVPEVPKELEPEEVAFEEEVVTHVEEYLVEEEEEYIHEEEEFITEEEVVPVIPVKVPEVPRKPVPEEKKPVPVPKKKEAPPAKVPEVPKKPEEKVPVLIPKKEKPPPAKVPEVPKKPVPEEKVPVPVPKKVEAPPAKVPEVPKKPVPEKKVPVPAPKKVEAPPAKVPEVPKKLIPEEKKPTPVPKKVEAPPPKVPKKREPVPVPVALPQEEEVLFEEEIVPEEEVLPEEEEVLPEEEEVLPEEEEVLPEEEEIPPEEEEVPPEEEYVPEEEEFVPEEEVLPEVKPKVPVPAPVPEIKKKVTEKKVVIPKKEEAPPAKVPEVPKKVEEKRIILPKEEEVLPVEVTEEPEEEPISEEEIPEEPPSIEEVEEVAPPRVPEVIKKAVPEAPTPVPKKVEAPPAKVSKKIPEEKVPVPVQKKEAPPAKVPEVPKKVPEKKVLVPKKEAVPPAKGRTVLEEKVSVAFRQEVVVKERLELEVVEAEVEEIPEEEEFHEVEEYFEEGEFHEVEEFIKLEQHRVEEEHRVEKVHRVIEVFEAEEVEVFEKPKAPPKGPEISEKIIPPKKPPTKVVPRKEPPAKVPEVPKKIVVEEKVRVPEEPRVPPTKVPEVLPPKEVVPEKKVPVPPAKKPEAPPPKVPEAPKEVVPEKKVPVPPPKKPEVPPTKVPEVPKAAVPEKKVPEAIPPKPESPPPEVPEAPKEVVPEKKVPAAPPKKPEVTPVKVPEAPKEVVPEKKVPVPPPKKPEVPPTKVPEVPKVAVPEKKVPEAIPPKPESPPPEVFEEPEEVALEEPPAEVVEEPEPAAPPQVTVPPKKPVPEKKAPAVVAKKPELPPVKVPEVPKEVVPEKKVPLVVPKKPEAPPAKVPEVPKEVVPEKKVAVPKKPEVPPAKVPEVPKKPVLEEKPAVPVPERAESPPPEVYEEPEEIAPEEEIAPEEEKPVPVAEEEEPEVPPPAVPEEPKKIIPEKKVPVIKKPEAPPPKEPEPEKVIEKPKLKPRPPPPPPAPPKEDVKEKIFQLKAIPKKKVPEKPQVPEKVELTPLKVPGGEKKVRKLLPERKPEPKEEVVLKSVLRKRPEEEEPKVEPKKLEKVKKPAVPEPPPPKPVEEVEVPTVTKRERKIPEPTKVPEIKPAIPLPAPEPKPKPEAEVKTIKPPPVEPEPTPIAAPVTVPVVGKKAEAKAPKEEAAKPKGPIKGVPKKTPSPIEAERRKLRPGSGGEKPPDEAPFTYQLKAVPLKFVKEIKDIILTESEFVGSSAIFECLVSPSTAITTWMKDGSNIRESPKHRFIADGKDRKLHIIDVQLSDAGEYTCVLRLGNKEKTSTAKLVVEELPVRFVKTLEEEVTVVKGQPLYLSCELNKERDVVWRKDGKIVVEKPGRIVPGVIGLMRALTINDADDTDAGTYTVTVENANNLECSSCVKVVEVIRDWLVKPIRDQHVKPKGTAIFACDIAKDTPNIKWFKGYDEIPAEPNDKTEILRDGNHLYLKIKNAMPEDIAEYAVEIEGKRYPAKLTLGEREVELLKPIEDVTIYEKESASFDAEISEADIPGQWKLKGELLRPSPTCEIKAEGGKRFLTLHKVKLDQAGEVLYQALNAITTAILTVKEIELDFAVPLKDVTVPERRQARFECVLTREANVIWSKGPDIIKSSDKFDIIADGKKHILVINDSQFDDEGVYTAEVEGKKTSARLFVTGIRLKFMSPLEDQTVKEGETATFVCELSHEKMHVVWFKNDAKLHTSRTVLISSEGKTHKLEMKEVTLDDISQIKAQVKELSSTAQLKVLEADPYFTVKLHDKTAVEKDEITLKCEVSKDVPVKWFKDGEEIVPSPKYSIKADGLRRILKIKKADLKDKGEYVCDCGTDKTKANVTVEARLIKVEKPLYGVEVFVGETAHFEIELSEPDVHGQWKLKGQPLTASPDCEIIEDGKKHILILHNCQLGMTGEVSFQAANAKSAANLKVKELPLIFITPLSDVKVFEKDEAKFECEVSREPKTFRWLKGTQEITGDDRFELIKDGTKHSMVIKSAAFEDEAKYMFEAEDKHTSGKLIIEGIRLKFLTPLKDVTAKEKESAVFTVELSHDNIRVKWFKNDQRLHTTRSVSMQDEGKTHSITFKDLSIDDTSQIRVEAMGMSSEAKLTVLEGDPYFTGKLQDYTGVEKDEVILQCEISKADAPVKWFKDGKEIKPSKNAVIKADGKKRMLILKKALKSDIGQYTCDCGTDKTSGKLDIEDREIKLVRPLHSVEVMETETARFETEISEDDIHANWKLKGEALLQTPDCEIKEEGKIHSLVLHNCRLDQTGGVDFQAANVKSSAHLRVKPRVIGLLRPLKDVTVTAGETATFDCELSYEDIPVEWYLKGKKLEPSDKVVPRSEGKVHTLTLRDVKLEDAGEVQLTAKDFKTHANLFVKEPPVEFTKPLEDQTVEEGATAVLECEVSRENAKVKWFKNGTEILKSKKYEIVADGRVRKLVIHDCTPEDIKTYTCDAKDFKTSCNLNVVPPHVEFLRPLTDLQVREKEMARFECELSRENAKVKWFKDGAEIKKGKKYDIISKGAVRILVINKCLLDDEAEYSCEVRTARTSGMLTVLEEEAVFTKNLANIEVSETDTIKLVCEVSKPGAEVIWYKGDEEIIETGRYEILTEGRKRILVIQNAHLEDAGNYNCRLPSSRTDGKVKVHELAAEFISKPQNLEILEGEKAEFVCSISKESFPVQWKRDDKTLESGDKYDVIADGKKRVLVVKDATLQDMGTYVVMVGAARAAAHLTVIEKLRIVVPLKDTRVKEQQEVVFNCEVNTEGAKAKWFRNEEAIFDSSKYIILQKDLVYTLRIRDAHLDDQANYNVSLTNHRGENVKSAANLIVEEEDLRIVEPLKDIETMEKKSVTFWCKVNRLNVTLKWTKNGEEVPFDNRVSYRVDKYKHMLTIKDCGFPDEGEYIVTAGQDKSVAELLIIEAPTEFVEHLEDQTVTEFDDAVFSCQLSREKANVKWYRNGREIKEGKKYKFEKDGSIHRLIIKDCRLDDECEYACGVEDRKSRARLFVEEIPVEIIRPPQDILEAPGADVVFLAELNKDKVEVQWLRNNMVVVQGDKHQMMSEGKIHRLQICDIKPRDQGEYRFIAKDKEARAKLELAAAPKIKTADQDLVVDVGKPLTMVVPYDAYPKAEAEWFKENEPLSTKTIDTTAEQTSFRILEAKKGDKGRYKIVLQNKHGKAEGFINLKVIDVPGPVRNLEVTETFDGEVSLAWEEPLTDGGSKIIGYVVERRDIKRKTWVLATDRAESCEFTVTGLQKGGVEYLFRVSARNRVGTGEPVETDNPVEARSKYDVPGPPLNVTITDVNRFGVSLTWEPPEYDGGAEITNYVIELRDKTSIRWDTAMTVRAEDLSATVTDVVEGQEYSFRVRAQNRIGVGKPSAATPFVKVADPIERPSPPVNLTSSDQTQSSVQLKWEPPLKDGGSPILGYIIERCEEGKDNWIRCNMKLVPELTYKVTGLEKGNKYLYRVSAENKAGVSDPSEILGPLTADDAFVEPTMDLSAFKDGLEVIVPNPITILVPSTGYPRPTATWCFGDKVLETGDRVKMKTLSAYAELVISPSERSDKGIYTLKLENRVKTISGEIDVNVIARPSAPKELKFGDITKDSVHLTWEPPDDDGGSPLTGYVVEKREVSRKTWTKVMDFVTDLEFTVPDLVQGKEYLFKVCARNKCGPGEPAYVDEPVNMSTPATVPDPPENVKWRDRTANSIFLTWDPPKNDGGSRIKGYIVERCPRGSDKWVACGEPVAETKMEVTGLEEGKWYAYRVKALNRQGASKPSRPTEEIQAVDTQEAPEIFLDVKLLAGLTVKAGTKIELPATVTGKPEPKITWTKADMILKQDKRITIENVPKKSTVTIVDSKRSDTGTYIIEAVNVCGRATAVVEVNVLDKPGPPAAFDITDVTNESCLLTWNPPRDDGGSKITNYVVERRATDSEVWHKLSSTVKDTNFKATKLIPNKEYIFRVAAENMYGVGEPVQASPITAKYQFDPPGPPTRLEPSDITKDAVTLTWCEPDDDGGSPITGYWVERLDPDTDKWVRCNKMPVKDTTYRVKGLTNKKKYRFRVLAENLAGPGKPSKSTEPILIKDPIDPPWPPGKPTVKDVGKTSVRLNWTKPEHDGGAKIESYVIEMLKTGTDEWVRVAEGVPTTQHLLPGLMEGQEYSFRVRAVNKAGESEPSEPSDPVLCREKLYPPSPPRWLEVINITKNTADLKWTVPEKDGGSPITNYIVEKRDVRRKGWQTVDTTVKDTKCTVTPLTEGSLYVFRVAAENAIGQSDYTEIEDSVLAKDTFTTPGPPYALAVVDVTKRHVDLKWEPPKNDGGRPIQRYVIEKKERLGTRWVKAGKTAGPDCNFRVTDVIEGTEVQFQVRAENEAGVGHPSEPTEILSIEDPTSPPSPPLDLHVTDAGRKHIAIAWKPPEKNGGSPIIGYHVEMCPVGTEKWMRVNSRPIKDLKFKVEEGVVPDKEYVLRVRAVNAIGVSEPSEISENVVAKDPDCKPTIDLETHDIIVIEGEKLSIPVPFRAVPVPTVSWHKDGKEVKASDRLTMKNDHISAHLEVPKSVRADAGIYTITLENKLGSATASINVKVIGLPGPCKDIKASDITKSSCKLTWEPPEFDGGTPILHYVLERREAGRRTYIPVMSGENKLSWTVKDLIPNGEYFFRVKAVNKVGGGEYIELKNPVIAQDPKQPPDPPVDVEVHNPTAEAMTITWKPPLYDGGSKIMGYIIEKIAKGEERWKRCNEHLVPILTYTAKGLEEGKEYQFRVRAENAAGISEPSRATPPTKAVDPIDAPKVILRTSLEVKRGDEIALDASISGSPYPTITWIKDENVIVPEEIKKRAAPLVRRRKGEVQEEEPFVLPLTQRLSIDNSKKGESQLRVRDSLRPDHGLYMIKVENDHGIAKAPCTVSVLDTPGPPINFVFEDIRKTSVLCKWEPPLDDGGSEIINYTLEKKDKTKPDSEWIVVTSTLRHCKYSVTKLIEGKEYLFRVRAENRFGPGPPCVSKPLVAKDPFGPPDAPDKPIVEDVTSNSMLVKWNEPKDNGSPILGYWLEKREVNSTHWSRVNKSLLNALKANVDGLLEGLTYVFRVCAENAAGPGKFSPPSDPKTAHDPISPPGPPIPRVTDTSSTTIELEWEPPAFNGGGEIVGYFVDKQLVGTNEWSRCTEKMIKVRQYTVKEIREGADYKLRVSAVNAAGEGPPGETQPVTVAEPQEPPAVELDVSVKGGIQIMAGKTLRIPAVVTGRPVPTKVWTKEEGELDKDRVVIDNVGTKSELIIKDALRKDHGRYVITATNSCGSKFAAARVEVFDVPGPVLDLKPVVTNRKMCLLNWSDPEDDGGSEITGFIIERKDAKMHTWRQPIETERSKCDITGLLEGQEYKFRVIAKNKFGCGPPVEIGPILAVDPLGPPTSPERLTYTERTKSTITLDWKEPRSNGGSPIQGYIIEKRRHDKPDFERVNKRLCPTTSFLVENLDEHQMYEFRVKAVNEIGESEPSLPLNVVIQDDEVPPTIKLRLSVRGDTIKVKAGEPVHIPADVTGLPMPKIEWSKNETVIEKPTDALQITKEEVSRSEAKTELSIPKAVREDKGTYTVTASNRLGSVFRNVHVEVYDRPSPPRNLAVTDIKAESCYLTWDAPLDNGGSEITHYVIDKRDASRKKAEWEEVTNTAVEKRYGIWKLIPNGQYEFRVRAVNKYGISDECKSDKVVIQDPYRLPGPPGKPKVLARTKGSMLVSWTPPLDNGGSPITGYWLEKREEGSPYWSRVSRAPITKVGLKGVEFNVPRLLEGVKYQFRAMAINAAGIGPPSEPSDPEVAGDPIFPPGPPSCPEVKDKTKSSISLGWKPPAKDGGSPIKGYIVEMQEEGTTDWKRVNEPDKLITTCECVVPNLKELRKYRFRVKAVNEAGESEPSDTTGEIPATDIQEEPEVFIDIGAQDCLVCKAGSQIRIPAVIKGRPTPKSSWEFDGKAKKAMKDGVHDIPEDAQLETAENSSVIIIPECKRSHTGKYSITAKNKAGQKTANCRVKVMDVPGPPKDLKVSDITRGSCRLSWKMPDDDGGDRIKGYVIEKRTIDGKAWTKVNPDCGSTTFVVPDLLSEQQYFFRVRAENRFGIGPPVETIQRTTARDPIYPPDPPIKLKIGLITKNTVHLSWKPPKNDGGSPVTHYIVECLAWDPTGTKKEAWRQCNKRDVEELQFTVEDLVEGGEYEFRVKAVNAAGVSKPSATVGPVTVKDQTCPPSIDLKEFMEVEEGTNVNIVAKIKGVPFPTLTWFKAPPKKPDNKEPVLYDTHVNKLVVDDTCTLVIPQSRRSDTGLYTITAVNNLGTASKEMRLNVLGRPGPPVGPIKFESVSADQMTLSWFPPKDDGGSKITNYVIEKREANRKTWVHVSSEPKECTYTIPKLLEGHEYVFRIMAQNKYGIGEPLDSEPETARNLFSVPGAPDKPTVSSVTRNSMTVNWEEPEYDGGSPVTGYWLEMKDTTSKRWKRVNRDPIKAMTLGVSYKVTGLIEGSDYQFRVYAINAAGVGPASLPSDPATARDPIAPPGPPFPKVTDWTKSSADLEWSPPLKDGGSKVTGYIVEYKEEGKEEWEKGKDKEVRGTKLVVTGLKEGAFYKFRVRAVNIAGIGEPGEVTDVIEMKDRLVSPDLQLDASVRDRIVVHAGGVIRIIAYVSGKPPPTVTWNMNERTLPQEATIETTAISSSMVIKNCQRSHQGVYSLLAKNEAGERKKTIIVDVLDVPGPVGTPFLAHNLTNESCKLTWFSPEDDGGSPITNYVIEKRESDRRAWTPVTYTVTRQNATVQGLIQGKAYFFRIAAENSIGMGPFVETSEALVIREPITVPERPEDLEVKEVTKNTVTLTWNPPKYDGGSEIINYVLESRLIGTEKFHKVTNDNLLSRKYTVKGLKEGDTYEYRVSAVNIVGQGKPSFCTKPITCKDELAPPTLHLDFRDKLTIRVGEAFALTGRYSGKPKPKVSWFKDEADVLEDDRTHIKTTPATLALEKIKAKRSDSGKYCVVVENSTGSRKGFCQVNVVDRPGPPVGPVSFDEVTKDYMVISWKPPLDDGGSKITNYIIEKKEVGKDVWMPVTSASAKTTCKVSKLLEGKDYIFRIHAENLYGISDPLVSDSMKAKDRFRVPDAPDQPIVTEVTKDSALVTWNKPHDGGKPITNYILEKRETMSKRWARVTKDPIHPYTKFRVPDLLEGCQYEFRVSAENEIGIGDPSPPSKPVFAKDPIAKPSPPVNPEAIDTTCNSVDLTWQPPRHDGGSKILGYIVEYQKVGDEEWRRANHTPESCPETKYKVTGLRDGQTYKFRVLAVNAAGESDPAHVPEPVLVKDRLEPPELILDANMAREQHIKVGDTLRLSAIIKGVPFPKVTWKKEDRDAPTKARIDVTPVGSKLEIRNAAHEDGGIYSLTVENPAGSKTVSVKVLVLDKPGPPRDLEVSEIRKDSCYLTWKEPLDDGGSVITNYVVERRDVASAQWSPLSATSKKKSHFAKHLNEGNQYLFRVAAENQYGRGPFVETPKPIKALDPLHPPGPPKDLHHVDVDKTEVSLVWNKPDRDGGSPITGYLVEYQEEGTQDWIKFKTVTNLECVVTGLQQGKTYRFRVKAENIVGLGLPDTTIPIECQEKLVPPSVELDVKLIEGLVVKAGTTVRFPAIIRGVPVPTAKWTTDGSEIKTDEHYTVETDNFSSVLTIKNCLRRDTGEYQITVSNAAGSKTVAVHLTVLDVPGPPTGPINILDVTPEHMTISWQPPKDDGGSPVINYIVEKQDTRKDTWGVVSSGSSKTKLKIPHLQKGCEYVFRVRAENKIGVGPPLDSTPTVAKHKFSPPSPPGKPVVTDITENAATVSWTLPKSDGGSPITGYYMERREVTGKWVRVNKTPIADLKFRVTGLYEGNTYEFRVFAENLAGLSKPSPSSDPIKACRPIKPPGPPINPKLKDKSRETADLVWTKPLSDGGSPILGYVVECQKPGTAQWNRINKDELIRQCAFRVPGLIEGNEYRFRIKAANIVGEGEPRELAESVIAKDILHPPEVELDVTCRDVITVRVGQTIRILARVKGRPEPDITWTKEGKVLVREKRVDLIQDLPRVELQIKEAVRADHGKYIISAKNSSGHAQGSAIVNVLDRPGPCQNLKVTNVTKENCTISWENPLDNGGSEITNFIVEYRKPNQKGWSIVASDVTKRLIKANLLANNEYYFRVCAENKVGVGPTIETKTPILAINPIDRPGEPENLHIADKGKTFVYLKWRRPDYDGGSPNLSYHVERRLKGSDDWERVHKGSIKETHYMVDRCVENQIYEFRVQTKNEGGESDWVKTEEVVVKEDLQKPVLDLKLSGVLTVKAGDTIRLEAGVRGKPFPEVAWTKDKDATDLTRSPRVKIDTRADSSKFSLTKAKRSDGGKYVVTATNTAGSFVAYATVNVLDKPGPVRNLKIVDVSSDRCTVCWDPPEDDGGCEIQNYILEKCETKRMVWSTYSATVLTPGTTVTRLIEGNEYIFRVRAENKIGTGPPTESKPVIAKTKYDKPGRPDPPEVTKVSKEEMTVVWNPPEYDGGKSITGYFLEKKEKHSTRWVPVNKSAIPERRMKVQNLLPDHEYQFRVKAENEIGIGEPSLPSRPVVAKDPIEPPGPPTNFRVVDTTKHSITLGWGKPVYDGGAPIIGYVVEMRPKIADASPDEGWKRCNAAAQLVRKEFTVTSLDENQEYEFRVCAQNQVGIGRPAELKEAIKPKEILEPPEIDLDASMRKLVIVRAGCPIRLFAIVRGRPAPKVTWRKVGIDNVVRKGQVDLVDTMAFLVIPNSTRDDSGKYSLTLVNPAGEKAVFVNVRVLDTPGPVSDLKVSDVTKTSCHVSWAPPENDGGSQVTHYIVEKREADRKTWSTVTPEVKKTSFHVTNLVPGNEYYFRVTAVNEYGPGVPTDVPKPVLASDPLSEPDPPRKLEVTEMTKNSATLAWLPPLRDGGAKIDGYITSYREEEQPADRWTEYSVVKDLSLVVTGLKEGKKYKFRVAARNAVGVSLPREAEGVYEAKEQLLPPKILMPEQITIKAGKKLRIEAHVYGKPHPTCKWKKGEDEVVTSSHLAVHKADSSSILIIKDVTRKDSGYYSLTAENSSGTDTQKIKVVVMDAPGPPQPPFDISDIDADACSLSWHIPLEDGGSNITNYIVEKCDVSRGDWVTALASVTKTSCRVGKLIPGQEYIFRVRAENRFGISEPLTSPKMVAQFPFGVPSEPKNARVTKVNKDCIFVAWDRPDSDGGSPIIGYLIERKERNSLLWVKANDTLVRSTEYPCAGLVEGLEYSFRIYALNKAGSSPPSKPTEYVTARMPVDPPGKPEVIDVTKSTVSLIWARPKHDGGSKIIGYFVEACKLPGDKWVRCNTAPHQIPQEEYTATGLEEKAQYQFRAIARTAVNISPPSEPSDPVTILAENVPPRIDLSVAMKSLLTVKAGTNVCLDATVFGKPMPTVSWKKDGTLLKPAEGIKMAMQRNLCTLELFSVNRKDSGDYTITAENSSGSKSATIKLKVLDKPGPPASVKINKMYSDRAMLSWEPPLEDGGSEITNYIVDKRETSRPNWAQVSATVPITSCSVEKLIEGHEYQFRICAENKYGVGDPVFTEPAIAKNPYDPPGRCDPPVISNITKDHMTVSWKPPADDGGSPITGYLLEKRETQAVNWTKVNRKPIIERTLKATGLQEGTEYEFRVTAINKAGPGKPSDASKAAYARDPQYPPGPPAFPKVYDTTRSSVSLSWGKPAYDGGSPIIGYLVEVKRADSDNWVRCNLPQNLQKTRFEVTGLMEDTQYQFRVYAVNKIGYSDPSDVPDKHYPKDILIPPEGELDADLRKTLILRAGVTMRLYVPVKGRPPPKITWSKPNVNLRDRIGLDIKSTDFDTFLRCENVNKYDAGKYILTLENSCGKKEYTIVVKVLDTPGPPVNVTVKEISKDSAYVTWEPPIIDGGSPIINYVVQKRDAERKSWSTVTTECSKTSFRVANLEEGKSYFFRVFAENEYGIGDPGETRDAVKASQTPGPVVDLKVRSVSKSSCSIGWKKPHSDGGSRIIGYVVDFLTEENKWQRVMKSLSLQYSAKDLTEGKEYTFRVSAENENGEGTPSEITVVARDDVVAPDLDLKGLPDLCYLAKENSNFRLKIPIKGKPAPSVSWKKGEDPLATDTRVSVESSAVNTTLIVYDCQKSDAGKYTITLKNVAGTKEGTISIKVVGKPGIPTGPIKFDEVTAEAMTLKWAPPKDDGGSEITNYILEKRDSVNNKWVTCASAVQKTTFRVTRLHEGMEYTFRVSAENKYGVGEGLKSEPIVARHPFDVPDAPPPPNIVDVRHDSVSLTWTDPKKTGGSPITGYHLEFKERNSLLWKRANKTPIRMRDFKVTGLTEGLEYEFRVMAINLAGVGKPSLPSEPVVALDPIDPPGKPEVINITRNSVTLIWTEPKYDGGHKLTGYIVEKRDLPSKSWMKANHVNVPECAFTVTDLVEGGKYEFRIRAKNTAGAISAPSESTETIICKDEYEAPTIVLDPTIKDGLTIKAGDTIVLNAISILGKPLPKSSWSKAGKDIRPSDITQITSTPTSSMLTIKYATRKDAGEYTITATNPFGTKVEHVKVTVLDVPGPPGPVEISNVSAEKATLTWTPPLEDGGSPIKSYILEKRETSRLLWTVVSEDIQSCRHVATKLIQGNEYIFRVSAVNHYGKGEPVQSEPVKMVDRFGPPGPPEKPEVSNVTKNTATVSWKRPVDDGGSEITGYHVERREKKSLRWVRAIKTPVSDLRCKVTGLQEGSTYEFRVSAENRAGIGPPSEASDSVLMKDAAYPPGPPSNPHVTDTTKKSASLAWGKPHYDGGLEITGYVVEHQKVGDEAWIKDTTGTALRITQFVVPDLQTKEKYNFRISAINDAGVGEPAVIPDVEIVEREMAPDFELDAELRRTLVVRAGLSIRIFVPIKGRPAPEVTWTKDNINLKNRANIENTESFTLLIIPECNRYDTGKFVMTIENPAGKKSGFVNVRVLDTPGPVLNLRPTDITKDSVTLHWDLPLIDGGSRITNYIVEKREATRKSYSTATTKCHKCTYKVTGLSEGCEYFFRVMAENEYGIGEPTETTEPVKASEAPSPPDSLNIMDITKSTVSLAWPKPKHDGGSKITGYVIEAQRKGSDQWTHITTVKGLECVVRNLTEGEEYTFQVMAVNSAGRSAPRESRPVIVKEQTMLPELDLRGIYQKLVIAKAGDNIKVEIPVLGRPKPTVTWKKGDQILKQTQRVNFETTATSTILNINECVRSDSGPYPLTARNIVGEVGDVITIQVHDIPGPPTGPIKFDEVSSDFVTFSWDPPENDGGVPISNYVVEMRQTDSTTWVELATTVIRTTYKATRLTTGLEYQFRVKAQNRYGVGPGITSACIVANYPFKVPGPPGTPQVTAVTKDSMTISWHEPLSDGGSPILGYHVERKERNGILWQTVSKALVPGNIFKSSGLTDGIAYEFRVIAENMAGKSKPSKPSEPMLALDPIDPPGKPVPLNITRHTVTLKWAKPEYTGGFKITSYIVEKRDLPNGRWLKANFSNILENEFTVSGLTEDAAYEFRVIAKNAAGAISPPSEPSDAITCRDDVEAPKIKVDVKFKDTVILKAGEAFRLEADVSGRPPPTMEWSKDGKELEGTAKLEIKIADFSTNLVNKDSTRRDSGAYTLTATNPGGFAKHIFNVKVLDRPGPPEGPLAVTEVTSEKCVLSWFPPLDDGGAKIDHYIVQKRETSRLAWTNVASEVQVTKLKVTKLLKGNEYIFRVMAVNKYGVGEPLESEPVLAVNPYGPPDPPKNPEVTTITKDSMVVCWGHPDSDGGSEIINYIVERRDKAGQRWIKCNKKTLTDLRYKVSGLTEGHEYEFRIMAENAAGISAPSPTSPFYKACDTVFKPGPPGNPRVLDTSRSSISIAWNKPIYDGGSEITGYMVEIALPEEDEWQIVTPPAGLKATSYTITGLTENQEYKIRIYAMNSEGLGEPALVPGTPKAEDRMLPPEIELDADLRKVVTIRACCTLRLFVPIKGRPAPEVKWARDHGESLDKASIESTSSYTLLIVGNVNRFDSGKYILTVENSSGSKSAFVNVRVLDTPGPPQDLKVKEVTKTSVTLTWDPPLLDGGSKIKNYIVEKRESTRKAYSTVATNCHKTSWKVDQLQEGCSYYFRVLAENEYGIGLPAETAESVKASERPLPPGKITLMDVTRNSVSLSWEKPEHDGGSRILGYIVEMQTKGSDKWATCATVKVTEATITGLIQGEEYSFRVSAQNEKGISDPRQLSVPVIAKDLVIPPAFKLLFNTFTVLAGEDLKVDVPFIGRPTPAVTWHKDNVPLKQTTRVNAESTENNSLLTIKDACREDVGHYVVKLTNSAGEAIETLNVIVLDKPGPPTGPVKMDEVTADSITLSWGPPKYDGGSSINNYIVEKRDTSTTTWQIVSATVARTTIKACRLKTGCEYQFRIAAENRYGKSTYLNSEPTVAQYPFKVPGPPGTPVVTLSSRDSMEVQWNEPISDGGSRVIGYHLERKERNSILWVKLNKTPIPQTKFKTTGLEEGVEYEFRVSAENIVGIGKPSKVSECYVARDPCDPPGRPEAIIVTRNSVTLQWKKPTYDGGSKITGYIVEKKELPEGRWMKASFTNIIDTHFEVTGLVEDHRYEFRVIARNAAGVFSEPSESTGAITARDEVDPPRISMDPKYKDTIVVHAGESFKVDADIYGKPIPTIQWIKGDQELSNTARLEIKSTDFATSLSVKDAVRVDSGNYILKAKNVAGERSVTVNVKVLDRPGPPEGPVVISGVTAEKCTLAWKPPLQDGGSDIINYIVERRETSRLVWTVVDANVQTLSCKVTKLLEGNEYTFRIMAVNKYGVGEPLESEPVVAKNPFVVPDAPKAPEVTTVTKDSMIVVWERPASDGGSEILGYVLEKRDKEGIRWTRCHKRLIGELRLRVTGLIENHDYEFRVSAENAAGLSEPSPPSAYQKACDPIYKPGPPNNPKVIDITRSSVFLSWSKPIYDGGCEIQGYIVEKCDVSVGEWTMCTPPTGINKTNIEVEKLLEKHEYNFRICAINKAGVGEHADVPGPIIVEEKLEAPDIDLDLELRKIINIRAGGSLRLFVPIKGRPTPEVKWGKVDGEIRDAAIIDVTSSFTSLVLDNVNRYDSGKYTLTLENSSGTKSAFVTVRVLDTPSPPVNLKVTEITKDSVSITWEPPLLDGGSKIKNYIVEKREATRKSYAAVVTNCHKNSWKIDQLQEGCSYYFRVTAENEYGIGLPAQTADPIKVAEVPQPPGKITVDDVTRNSVSLSWTKPEHDGGSKIIQYIVEMQAKHSEKWSECARVKSLQAVITNLTQGEEYLFRVVAVNEKGRSDPRSLAVPIVAKDLVIEPDVKPAFSSYSVQVGQDLKIEVPISGRPKPTITWTKDGLPLKQTTRINVTDSLDLTTLSIKETHKDDGGQYGITVANVVGQKTASIEIVTLDKPDPPKGPVKFDDVSAESITLSWNPPLYTGGCQITNYIVQKRDTTTTVWDVVSATVARTTLKVTKLKTGTEYQFRIFAENRYGQSFALESDPIVAQYPYKEPGPPGTPFATAISKDSMVIQWHEPVNNGGSPVIGYHLERKERNSILWTKVNKTIIHDTQFKAQNLEEGIEYEFRVYAENIVGVGKASKNSECYVARDPCDPPGTPEPIMVKRNEITLQWTKPVYDGGSMITGYIVEKRDLPDGRWMKASFTNVIETQFTVSGLTEDQRYEFRVIAKNAAGAISKPSDSTGPITAKDEVELPRISMDPKFRDTIVVNAGETFRLEADVHGKPLPTIEWLRGDKEIEESARCEIKNTDFKALLIVKDAIRIDGGQYILRASNVAGSKSFPVNVKVLDRPGPPEGPVQVTGVTSEKCSLTWSPPLQDGGSDISHYVVEKRETSRLAWTVVASEVVTNSLKVTKLLEGNEYVFRIMAVNKYGVGEPLESAPVLMKNPFVLPGPPKSLEVTNIAKDSMTVCWNRPDSDGGSEIIGYIVEKRDRSGIRWIKCNKRRITDLRLRVTGLTEDHEYEFRVSAENAAGVGEPSPATVYYKACDPVFKPGPPTNAHIVDTTKNSITLAWGKPIYDGGSEILGYVVEICKADEEEWQIVTPQTGLRVTRFEISKLTEHQEYKIRVCALNKVGLGEATSVPGTVKPEDKLEAPELDLDSELRKGIVVRAGGSARIHIPFKGRPTPEITWSREEGEFTDKVQIEKGVNYTQLSIDNCDRNDAGKYILKLENSSGSKSAFVTVKVLDTPGPPQNLAVKEVRKDSAFLVWEPPIIDGGAKVKNYVIDKRESTRKAYANVSSKCSKTSFKVENLTEGAIYYFRVMAENEFGVGVPVETVDAVKAAEPPSPPGKVTLTDVSQTSASLMWEKPEHDGGSRVLGYVVEMQPKGTEKWSIVAESKVCNAVVTGLSSGQEYQFRVKAYNEKGKSDPRVLGVPVIAKDLTIQPSLKLPFNTYSIQAGEDLKIEIPVIGRPRPNISWVKDGEPLKQTTRVNVEETATSTVLHIKEGNKDDFGKYTVTATNSAGTATENLSVIVLEKPGPPVGPVRFDEVSADFVVISWEPPAYTGGCQISNYIVEKRDTTTTTWHMVSATVARTTIKITKLKTGTEYQFRIFAENRYGKSAPLDSKAVIVQYPFKEPGPPGTPFVTSISKDQMLVQWHEPVNDGGTKIIGYHLEQKEKNSILWVKLNKTPIQDTKFKTTGLDEGLEYEFKVSAENIVGIGKPSKVSECFVARDPCDPPGRPEAIVITRNNVTLKWKKPAYDGGSKITGYIVEKKDLPDGRWMKASFTNVLETEFTVSGLVEDQRYEFRVIARNAAGNFSEPSDSSGAITARDEIDAPNASLDPKYKDVIVVHAGETFVLEADIRGKPIPDVVWSKDGKELEETAARMEIKSTIQKTTLVVKDCIRTDGGQYILKLSNVGGTKSIPITVKVLDRPGPPEGPLKVTGVTAEKCYLAWNPPLQDGGANISHYIIEKRETSRLSWTQVSTEVQALNYKVTKLLPGNEYIFRVMAVNKYGIGEPLESGPVTACNPYKPPGPPSTPEVSAITKDSMVVTWARPVDDGGTEIEGYILEKRDKEGVRWTKCNKKTLTDLRLRVTGLTEGHSYEFRVAAENAAGVGEPSEPSVFYRACDALYPPGPPSNPKVTDTSRSSVSLAWSKPIYDGGAPVKGYVVEVKEAAADEWTTCTPPTGLQGKQFTVTKLKENTEYNFRICAINSEGVGEPATLPGSVVAQERIEPPEIELDADLRKVVVLRASATLRLFVTIKGRPEPEVKWEKAEGILTDRAQIEVTSSFTMLVIDNVTRFDSGRYNLTLENNSGSKTAFVNVRVLDSPSAPVNLTIREVKKDSVTLSWEPPLIDGGAKITNYIVEKRETTRKAYATITNNCTKTTFRIENLQEGCSYYFRVLASNEYGIGLPAETTEPVKVSEPPLPPGRVTLVDVTRNTATIKWEKPESDGGSKITGYVVEMQTKGSEKWSTCTQVKTLEATISGLTAGEEYVFRVAAVNEKGRSDPRQLGVPVIARDIEIKPSVELPFHTFNVKAREQLKIDVPFKGRPQATVNWRKDGQTLKETTRVNVSSSKTVTSLSIKEASKEDVGTYELCVSNSAGSITVPITIIVLDRPGPPGPIRIDEVSCDSITISWNPPEYDGGCQISNYIVEKKETTSTTWHIVSQAVARTSIKIVRLTTGSEYQFRVCAENRYGKSSYSESSAVVAEYPFSPPGPPGTPKVVHATKSTMLVTWQVPVNDGGSRVIGYHLEYKERSSILWSKANKILIADTQMKVSGLDEGLMYEYRVYAENIAGIGKCSKSCEPVPARDPCDPPGQPEVTNITRKSVSLKWSKPHYDGGAKITGYIVERRELPDGRWLKCNYTNIQETYFEVTELTEDQRYEFRVFARNAADSVSEPSESTGPIIVKDDVEPPRVMMDVKFRDVIVVKAGEVLKINADIAGRPLPVISWAKDGIEIEERARTEIISTDNHTLLTVKDCIRRDTGQYVLTLKNVAGTRSVAVNCKVLDKPGPPAGPLEINGLTAEKCSLSWGRPQEDGGADIDYYIVEKRETSHLAWTICEGELQMTSCKVTKLLKGNEYIFRVTGVNKYGVGEPLESVAIKALDPFTVPSPPTSLEITSVTKESMTLCWSRPESDGGSEISGYIIERREKNSLRWVRVNKKPVYDLRVKSTGLREGCEYEYRVYAENAAGLSLPSETSPLIRAEDPVFLPSPPSKPKIVDSGKTTITIAWVKPLFDGGAPITGYTVEYKKSDDTDWKTSIQSLRGTEYTISGLTTGAEYVFRVKSVNKVGASDPSDSSDPQIAKEREEEPLFDIDSEMRKTLIVKAGASFTMTVPFRGRPVPNVLWSKPDTDLRTRAYVDTTDSRTSLTIENANRNDSGKYTLTIQNVLSAASLTLVVKVLDTPGPPTNITVQDVTKESAVLSWDVPENDGGAPVKNYHIEKREASKKAWVSVTNNCNRLSYKVTNLQEGAIYYFRVSGENEFGVGIPAETKEGVKITEKPSPPEKLGVTSISKDSVSLTWLKPEHDGGSRIVHYVVEALEKGQKNWVKCAVAKSTHHVVSGLRENSEYFFRVFAENQAGLSDPRELLLPVLIKEQLEPPEIDMKNFPSHTVYVRAGSNLKVDIPISGKPLPKVTLSRDGVPLKATMRFNTEITAENLTINLKESVTADAGRYEITAANSSGTTKAFINIVVLDRPGPPTGPVVISDITEESVTLKWEPPKYDGGSQVTNYILLKRETSTAVWTEVSATVARTMMKVMKLTTGEEYQFRIKAENRFGISDHIDSACVTVKLPYTTPGPPSTPWVTNVTRESITVGWHEPVSNGGSAVVGYHLEMKDRNSILWQKANKLVIRTTHFKVTTISAGLIYEFRVYAENAAGVGKPSHPSEPVLAIDACEPPRNVRITDISKNSVSLSWQQPAFDGGSKITGYIVERRDLPDGRWTKASFTNVTETQFIISGLTQNSQYEFRVFARNAVGSISNPSEVVGPITCIDSYGGPVIDLPLEYTEVVKYRAGTSVKLRAGISGKPAPTIEWYKDDKELQTNALVCVENTTDLASILIKDADRLNSGCYELKLRNAMGSASATIRVQILDKPGPPGGPIEFKTVTAEKITLLWRPPADDGGAKITHYIVEKRETSRVVWSMVSEHLEECIITTTKIIKGNEYIFRVRAVNKYGIGEPLESDSVVAKNAFVTPGPPGIPEVTKITKNSMTVVWSRPIADGGSDISGYFLEKRDKKSLGWFKVLKETIRDTRQKVTGLTENSDYQYRVCAVNAAGQGPFSEPSEFYKAADPIDPPGPPAKIRIADSTKSSITLGWSKPVYDGGSAVTGYVVEIRQGEEEEWTTVSTKGEVRTTEYVVSNLKPGVNYYFRVSAVNCAGQGEPIEMNEPVQAKDILEAPEIDLDVALRTSVIAKAGEDVQVLIPFKGRPPPTVTWRKDEKNLGSDARYSIENTDSSSLLTIPQVTRNDTGKYILTIENGVGEPKSSTVSVKVLDTPAACQKLQVKHVSRGTVTLLWDPPLIDGGSPIINYVIEKRDATKRTWSVVSHKCSSTSFKLIDLSEKTPFFFRVLAENEIGIGEPCETTEPVKAAEVPAPIRDLSMKDSTKTSVILSWTKPDFDGGSVITEYVVERKGKGEQTWSHAGISKTCEIEVSQLKEQSVLEFRVFAKNEKGLSDPVTIGPITVKELIITPEVDLSDIPGAQVTVRIGHNVHLELPYKGKPKPSISWLKDGLPLKESEFVRFSKTENKITLSIKNAKKEHGGKYTVILDNAVCRIAVPITVITLGPPSKPKGPIRFDEIKADSVILSWDVPEDNGGGEITCYSIEKRETSQTNWKMVCSSVARTTFKVPNLVKDAEYQFRVRAENRYGVSQPLVSSIIVAKHQFRIPGPPGKPVIYNVTSDGMSLTWDAPVYDGGSEVTGFHVEKKERNSILWQKVNTSPISGREYRATGLVEGLDYQFRVYAENSAGLSSPSDPSKFTLAVSPVDPPGTPDYIDVTRETITLKWNPPLRDGGSKIVGYSIEKRQGNERWVRCNFTDVSECQYTVTGLSPGDRYEFRIIARNAVGTISPPSQSSGIIMTRDENVPPIVEFGPEYFDGLIIKSGESLRIKALVQGRPVPRVTWFKDGVEIEKRMNMEITDVLGSTSLFVRDATRDHRGVYTVEAKNASGSAKAEIKVKVQDTPGKVVGPIRFTNITGEKMTLWWDAPLNDGCAPITHYIIEKRETSRLAWALIEDKCEAQSYTAIKLINGNEYQFRVSAVNKFGVGRPLDSDPVVAQIQYTVPDAPGIPEPSNITGNSITLTWARPESDGGSEIQQYILERREKKSTRWVKVISKRPISETRFKVTGLTEGNEYEFHVMAENAAGVGPASGISRLIKCREPVNPPGPPTVVKVTDTSKTTVSLEWSKPVFDGGMEIIGYIIEMCKADLGDWHKVNAEACVKTRYTVTDLQAGEEYKFRVSAINGAGKGDSCEVTGTIKAVDRLTAPELDIDANFKQTHVVRAGASIRLFIAYQGRPTPTAVWSKPDSNLSLRADIHTTDSFSTLTVENCNRNDAGKYTLTVENNSGSKSITFTVKVLDTPGPPGPITFKDVTRGSATLMWDAPLLDGGARIHHYVVEKREASRRSWQVISEKCTRQIFKVNDLAEGVPYYFRVSAVNEYGVGEPYEMPEPIVATEQPAPPRRLDVVDTSKSSAVLAWLKPDHDGGSRITGYLLEMRQKGSDFWVEAGHTKQLTFTVERLVEKTEYEFRVKAKNDAGYSEPREAFSSVIIKEPQIEPTADLTGITNQLITCKAGSPFTIDVPISGRPAPKVTWKLEEMRLKETDRVSITTTKDRTTLTVKDSMRGDSGRYFLTLENTAGVKTFSVTVVVIGRPGPVTGPIEVSSVSAESCVLSWGEPKDGGGTEITNYIVEKRESGTTAWQLVNSSVKRTQIKVTHLTKYMEYSFRVSSENRFGVSKPLESAPIIAEHPFVPPSAPTRPEVYHVSANAMSIRWEEPYHDGGSKIIGYWVEKKERNTILWVKENKVPCLECNYKVTGLVEGLEYQFRTYALNAAGVSKASEASRPIMAQNPVDAPGRPEVTDVTRSTVSLIWSAPAYDGGSKVVGYIIERKPVSEVGDGRWLKCNYTIVSDNFFTVTALSEGDTYEFRVLAKNAAGVISKGSESTGPVTCRDEYAPPKAELDARLHGDLVTIRAGSDLVLDAAVGGKPEPKIIWTKGDKELDLCEKVSLQYTGKRATAVIKFCDRSDSGKYTLTVKNASGTKAVSVMVKVLDSPGPCGKLTVSRVTQEKCTLAWSLPQEDGGAEITHYIVERRETSRLNWVIVEGECPTLSYVVTRLIKNNEYIFRVRAVNKYGPGVPVESEPIVARNSFTIPSPPGIPEEVGTGKEHIIIQWTKPESDGGNEISNYLVDKREKKSLRWTRVNKDYVVYDTRLKVTSLMEGCDYQFRVTAVNAAGNSEPSEASNFISCREPSYTPGPPSAPRVVDTTKHSISLAWTKPMYDGGTDIVGYVLEMQEKDTDQWYRVHTNATIRNTEFTVPDLKMGQKYSFRVAAVNVKGMSEYSESIAEIEPVERIEIPDLELADDLKKTVTIRAGASLRLMVSVSGRPPPVITWSKQGIDLASRAIIDTTESYSLLIVDKVNRYDAGKYTIEAENQSGKKSATVLVKVYDTPGPCPSVKVKEVSRDSVTITWEIPTIDGGAPVNNYIVEKREAAMRAFKTVTTKCSKTLYRISGLVEGTMYYFRVLPENIYGIGEPCETSDAVLVSEVPLVPAKLEVVDVTKSTVTLAWEKPLYDGGSRLTGYVLEACKAGTERWMKVVTLKPTVLEHTVTSLNEGEQYLFRIRAQNEKGVSEPRETVTAVTVQDLRVLPTIDLSTMPQKTIHVPAGRPVELVIPIAGRPPPAASWFFAGSKLRESERVTVETHTKVAKLTIRETTIRDTGEYTLELKNVTGTTSETIKVIILDKPGPPTGPIKIDEIDATSITISWEPPELDGGAPLSGYVVEQRDAHRPGWLPVSESVTRSTFKFTRLTEGNEYVFRVAATNRFGIGSYLQSEVIECRSSIRIPGPPETLQIFDVSRDGMTLTWYPPEDDGGSQVTGYIVERKEVRADRWVRVNKVPVTMTRYRSTGLTEGLEYEHRVTAINARGSGKPSRPSKPIVAMDPIAPPGKPQNPRVTDTTRTSVSLAWSVPEDEGGSKVTGYLIEMQKVDQHEWTKCNTTPTKIREYTLTHLPQGAEYRFRVLACNAGGPGEPAEVPGTVKVTEMLEYPDYELDERYQEGIFVRQGGVIRLTIPIKGKPFPICKWTKEGQDISKRAMIATSETHTELVIKEADRGDSGTYDLVLENKCGKKAVYIKVRVIGSPNSPEGPLEYDDIQVRSVRVSWRPPADDGGADILGYILERREVPKAAWYTIDSRVRGTSLVVKGLKENVEYHFRVSAENQFGISKPLKSEEPVTPKTPLNPPEPPSNPPEVLDVTKSSVSLSWSRPKDDGGSRVTGYYIERKETSTDKWVRHNKTQITTTMYTVTGLVPDAEYQFRIIAQNDVGLSETSPASEPVVCKDPFDKPSQPGELEILSISKDSVTLQWEKPECDGGKEILGYWVEYRQSGDSAWKKSNKERIKDKQFTIGGLLEATEYEFRVFAENETGLSRPRRTAMSIKTKLTSGEAPGIRKEMKDVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELIQSRKYKMSSDGRTHTLTVMTEEQEDEGVYTCIATNEVGEVETSSKLLLQATPQFHPGYPLKEKYYGAVGSTLRLHVMYIGRPVPAMTWFHGQKLLQNSENITIENTEHYTHLVMKNVQRKTHAGKYKVQLSNVFGTVDAILDVEIQDKPDKPTGPIVIEALLKNSAVISWKPPADDGGSWITNYVVEKCEAKEGAEWQLVSSAISVTTCRIVNLTENAGYYFRVSAQNTFGISDPLEVSSVVIIKSPFEKPGAPGKPTITAVTKDSCVVAWKPPASDGGAKIRNYYLEKREKKQNKWISVTTEEIRETVFSVKNLIEGLEYEFRVKCENLGGESEWSEISEPITPKSDVPIQAPHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRIQEFKGGYHQLIIASVTDDDATVYQVRATNQGGSVSGTASLEVEVPAKIHLPKTLEGMGAVHALRGEVVSIKIPFSGKPDPVITWQKGQDLIDNNGHYQVIVTRSFTSLVFPNGVERKDAGFYVVCAKNRFGIDQKTVELDVADVPDPPRGVKVSDVSRDSVNLTWTEPASDGGSKITNYIVEKCATTAERWLRVGQARETRYTVINLFGKTSYQFRVIAENKFGLSKPSEPSEPTITKEDKTRAMNYDEEVDETREVSMTKASHSSTKELYEKYMIAEDLGRGEFGIVHRCVETSSKKTYMAKFVKVKGTDQVLVKKEISILNIARHRNILHLHESFESMEELVMIFEFISGLDIFERINTSAFELNEREIVSYVHQVCEALQFLHSHNIGHFDIRPENIIYQTRRSSTIKIIEFGQARQLKPGDNFRLLFTAPEYYAPEVHQHDVVSTATDMWSLGTLVYVLLSGINPFLAETNQQIIENIMNAEYTFDEEAFKEISIEAMDFVDRLLVKERKSRMTASEALQHPWLKQKIERVSTKVIRTLKHRRYYHTLIKKDLNMVVSAARISCGGAIRSQKGVSVAKVKVASIEIGPVSGQIMHAVGEEGGHVKYVCKIENYDQSTQVTWYFGVRQLENSEKYEITYEDGVAILYVKDITKLDDGTYRCKVVNDYGEDSSYAELFVKGVREVYDYYCRRTMKKIKRRTDTMRLLERPPEFTLPLYNKTAYVGENVRFGVTITVHPEPHVTWYKSGQKIKPGDNDKKYTFESDKGLYQLTINSVTTDDDAEYTVVARNKYGEDSCKAKLTVTLHPPPTDSTLRPMFKRLLANAECQEGQSVCFEIRVSGIPPPTLKWEKDGQPLSLGPNIEIIHEGLDYYALHIRDTLPEDTGYYRVTATNTAGSTSCQAHLQVERLRYKKQEFKSKEEHERHVQKQIDKTLRMAEILSGTESVPLTQVAKEALREAAVLYKPAVSTKTVKGEFRLEIEEKKEERKLRMPYDVPEPRKYKQTTIEEDQRIKQFVPMSDMKWYKKIRDQYEMPGKLDRVVQKRPKRIRLSRWEQFYVMPLPRITDQYRPKWRIPKLSQDDLEIVRPARRRTPSPDYDFYYRPRRRSLGDISDEELLLPIDDYLAMKRTEEERLRLEEELELGFSASPPSRSPPHFELSSLRYSSPQAHVKVEETRKDFRYSTYHIPTKAEASTSYAELRERHAQAAYRQPKQRQRIMAEREDEELLRPVTTTQHLSEYKSELDFMSKEEKSRKKSRRQREVTEITEIEEEYEISKHAQRESSSSASRLLRRRRSLSPTYIELMRPVSELIRSRPQPAEEYEDDTERRSPTPERTRPRSPSPVSSERSLSRFERSARFDIFSRYESMKAALKTQKTSERKYEVLSQQPFTLDHAPRITLRMRSHRVPCGQNTRFILNVQSKPTAEVKWYHNGVELQESSKIHYTNTSGVLTLEILDCHTDDSGTYRAVCTNYKGEASDYATLDVTGGDYTTYASQRRDEEVPRSVFPELTRTEAYAVSSFKKTSEMEASSSVREVKSQMTETRESLSSYEHSASAEMKSAALEEKSLEEKSTTRKIKTTLAARILTKPRSMTVYEGESARFSCDTDGEPVPTVTWLRKGQVLSTSARHQVTTTKYKSTFEISSVQASDEGNYSVVVENSEGKQEAEFTLTIQKARVTEKAVTSPPRVKSPEPRVKSPEAVKSPKRVKSPEPSHPKAVSPTETKPTPTEKVQHLPVSAPPKITQFLKAEASKEIAKLTCVVESSVLRAKEVTWYKDGKKLKENGHFQFHYSADGTYELKINNLTESDQGEYVCEISGEGGTSKTNLQFMGQAFKSIHEKVSKISETKKSDQKTTESTVTRKTEPKAPEPISSKPVIVTGLQDTTVSSDSVAKFAVKATGEPRPTAIWTKDGKAITQGGKYKLSEDKGGFFLEIHKTDTSDSGLYTCTVKNSAGSVSSSCKLTIKAIKDTEAQKVSTQKTSEITPQKKAVVQEEISQKALRSEEIKMSEAKSQEKLALKEEASKVLISEEVKKSAATSLEKSIVHEEITKTSQASEEVRTHAEIKAFSTQMSINEGQRLVLKANIAGATDVKWVLNGVELTNSEEYRYGVSGSDQTLTIKQASHRDEGILTCISKTKEGIVKCQYDLTLSKELSDAPAFISQPRSQNINEGQNVLFTCEISGEPSPEIEWFKNNLPISISSNVSISRSRNVYSLEIRNASVSDSGKYTIKAKNFRGQCSATASLMVLPLVEEPSREVVLRTSGDTSLQGSFSSQSVQMSASKQEASFSSFSSSSASSMTEMKFASMSAQSMSSMQESFVEMSSSSFMGISNMTQLESSTSKMLKAGIRGIPPKIEALPSDISIDEGKVLTVACAFTGEPTPEVTWSCGGRKIHSQEQGRFHIENTDDLTTLIIMDVQKQDGGLYTLSLGNEFGSDSATVNIHIRSI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q8WZ42","disprot_id":"DP00072","ncbi_taxon_id":9606,"regions_counter":4,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":12031,"region_id":"DP00072r001","released":"2022_03","ec_id":"ECO:0001591","reference_html":"PEVK domain of titin: an entropic spring with actin-binding properties. <i> Linke WA, Kulke M, Li H, Fujita-Becker S, Neagoe C, Manstein DJ, Gautel M, Fernandez JM. </i> J Struct Biol, 2002","term_id":"IDPO:0000002","curator_id":"esalladini","start":9880,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"12064946","version":3,"ec_name":"atomic force microscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"The PEVK domain of the giant muscle protein titin is a proline-rich sequence with unknown secondary/tertiary structure. ","type":"Abstract"},{"text":"It is still debated whether the PEVK domain adopts a specific secondary/tertiary structure.","type":"Introduction"}],"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T17:45:16.496Z"}},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":12031,"term_name":"entropic chain","start":9880,"ec_name":"atomic force microscopy evidence used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"12064946","version":4,"reference_html":"PEVK domain of titin: an entropic spring with actin-binding properties. <i> Linke WA, Kulke M, Li H, Fujita-Becker S, Neagoe C, Manstein DJ, Gautel M, Fernandez JM. </i> J Struct Biol, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0001591","region_id":"DP00072r002","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"The analysis revealed that cardiac PEVK titin acts as an entropic spring with the properties of a random coil exhibiting mechanical conformations of different flexibility.","type":"Abstract"}],"ec_go":"IDA","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T17:45:16.140Z"}},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":12031,"term_name":"protein binding","start":9880,"ec_name":"atomic force microscopy evidence used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"12064946","version":4,"reference_html":"PEVK domain of titin: an entropic spring with actin-binding properties. <i> Linke WA, Kulke M, Li H, Fujita-Becker S, Neagoe C, Manstein DJ, Gautel M, Fernandez JM. </i> J Struct Biol, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0001591","region_id":"DP00072r003","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"Thus, the results may be interpreted to indicate binding of the constitutively expressed PEVK segment (“cardiac PEVK”) to actin filaments in both cardiac and skeletal muscle. In contrast, PEVK sequences present only in skeletal titins may exhibit little actin-binding propensity.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T17:45:16.293Z"}},{"start":11045,"end":11070,"reference_id":"16949547","reference_source":"pmid","reference_html":"Studies on titin PEVK peptides and their interaction. <i> Duan Y, DeKeyser JG, Damodaran S, Greaser ML. </i> Arch Biochem Biophys, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":1,"region_id":"DP00072r004","statement":[{"text":"In all of the chemically synthesized and expressed peptides, unordered coils were the major secondary structure identified.","type":"Results"},{"text":"Circular dichroism (CD) experiments demonstrated that both the positively charged PPAK modules and the negatively charged PolyE repeats had similar spectral properties with disordered secondary structure predominating.","type":"Abstract"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T17:45:18.897Z"}}],"released":"2016_10","uniref100":"UniRef100_Q8WZ42","date":"2016-08-24T11:11:34.000Z","acc":"Q8WZ42","name":"Titin","length":34350,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI00001100FC","genes":[{"name":{"value":"TTN"}}],"disorder_content":0.06264919941775837,"disprot_consensus":{"full":[{"start":9880,"end":12031,"type":"D"}],"Structural state":[{"start":9880,"end":12031,"type":"D"}],"Disorder function":[{"start":9880,"end":12031,"type":"F"}],"Molecular function":[{"start":9880,"end":12031,"type":"F"}]}},{"acc":"P04818","sequence":"MPVAGSELPRRPLPPAAQERDAEPRPPHGELQYLGQIQHILRCGVRKDDRTGTGTLSVFGMQARYSLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVKIWDANGSRDFLDSLGFSTREEGDLGPVYGFQWRHFGAEYRDMESDYSGQGVDQLQRVIDTIKTNPDDRRIIMCAWNPRDLPLMALPPCHALCQFYVVNSELSCQLYQRSGDMGLGVPFNIASYALLTYMIAHITGLKPGDFIHTLGDAHIYLNHIEPLKIQLQREPRPFPKLRILRKVEKIDDFKAEDFQIEGYNPHPTIKMEMAV","alphafold_very_low_content":"0.012779552715654952","creator":"mnecci","dataset":[],"date":"2016-09-12T09:55:27.000Z","disprot_id":"DP00073","features":{"pfam":[{"id":"PF00303","name":"Thymidylate synthase","start":32,"end":313}],"gene3D":[{"start":26,"end":313,"id":"3.30.572.10","name":"Thymidylate synthase/dCMP hydroxymethylase domain","_id":"685af523b4ac24d5329d7378"}]},"genes":[{"name":{"value":"TYMS","evidences":[{"source":{"id":"HGNC:12441","name":"HGNC","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:12441","_id":"685af523b4ac24d5329d73a1"},"code":"ECO:0000312","_id":"685af523b4ac24d5329d73a0"}],"_id":"685af523b4ac24d5329d73a2"},"synonyms":[{"value":"TS","evidences":[],"_id":"685af523b4ac24d5329d73a3"}],"olnNames":[],"orfNames":[{"value":"OK/SW-cl.29","evidences":[],"_id":"685af523b4ac24d5329d73a4"}],"_id":"685af523b4ac24d5329d739f"}],"length":313,"name":"Thymidylate synthase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":15,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000001225","uniref100":"UniRef100_P04818","uniref50":"UniRef50_P04818","uniref90":"UniRef90_P04818","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1HW3","_id":"685af523b4ac24d5329d737a"},{"db":"PDB","id":"1HW4","_id":"685af523b4ac24d5329d737b"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":25,"interaction_partner":[],"reference_html":"Structure of human thymidylate synthase suggests advantages of chemotherapy with noncompetitive inhibitors. <i> Phan J, Steadman DJ, Koli S, Ding WC, Minor W, Dunlap RB, Berger SH, Lebioda L. </i> J Biol Chem, 2001","reference_id":"11278511","region_id":"DP00073r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The N terminus is largely disordered; good density starts at Pro-26, and this region does not change between hTS, NTE-hTS, and an inhibitory ternary complex of hTS with dUMP and Tomudex (ZD1694 or raltitrexed) (4) or analogous rat TS complex (PDB entry 2tsr(3)).","_id":"685af523b4ac24d5329d737c"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-01-13T14:56:59.827Z","_id":"685af523b4ac24d5329d737d"},"version":3,"_id":"685af523b4ac24d5329d7379","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1HW3","_id":"685af523b4ac24d5329d7385"},{"db":"PDB","id":"1HW4","_id":"685af523b4ac24d5329d7386"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-13T14:57:33.323Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":107,"end":128,"interaction_partner":[],"reference_html":"Structure of human thymidylate synthase suggests advantages of chemotherapy with noncompetitive inhibitors. <i> Phan J, Steadman DJ, Koli S, Ding WC, Minor W, Dunlap RB, Berger SH, Lebioda L. </i> J Biol Chem, 2001","reference_id":"11278511","region_id":"DP00073r005","released":"2023_06","sample":[],"statement":[{"type":"Results","text":"Region 107–128, which includes the insert, is disordered in the crystals.","_id":"685af523b4ac24d5329d7387"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":4,"_id":"685af523b4ac24d5329d7384","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-13T14:55:11.447Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":27,"interaction_partner":[],"reference_html":"Crystal structure of human thymidylate synthase: a structural mechanism for guiding substrates into the active site. <i> Schiffer CA, Clifton IJ, Davisson VJ, Santi DV, Stroud RM. </i> Biochemistry, 1995","reference_id":"8845352","region_id":"DP00073r010","released":"2023_06","sample":[],"statement":[{"type":"Methods","text":"The search model did not include 27 residues at the amino terminus, and two insertions of 12 and 8 amino acids residues that are highly conserved in eukaryotic species of TS at residues 90 (hi 17) to 101 (hi28), and inserted between 156 and 157 (h 146—hi52) respectively (Perry et al., 1990).","_id":"685af523b4ac24d5329d7391"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":4,"_id":"685af523b4ac24d5329d7390","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-13T14:54:52.654Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":117,"end":128,"interaction_partner":[],"reference_html":"Crystal structure of human thymidylate synthase: a structural mechanism for guiding substrates into the active site. <i> Schiffer CA, Clifton IJ, Davisson VJ, Santi DV, Stroud RM. </i> Biochemistry, 1995","reference_id":"8845352","region_id":"DP00073r013","released":"2023_06","sample":[],"statement":[{"type":"Abstract","text":"The highly conserved, but eukaryote-specific insertion of twelve residues 90—101 (hi 17—128), and of eight residues between 156 and 157 (hl46—hl53) are known to be a-helical in other eukaryotes, and lie close together on the outside of the protein in regions of disordered electron density in this crystal form.","_id":"685af523b4ac24d5329d7399"},{"type":"Methods","text":"The search model did not include 27 residues at the amino terminus, and two insertions of 12 and 8 amino acids residues that are highly conserved in eukaryotic species of TS at residues 90 (hi 17) to 101 (hi28), and inserted between 156 and 157 (h 146—hi52) respectively (Perry et al., 1990).","_id":"685af523b4ac24d5329d739a"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d7398","reference_source":"pmid"}],"__v":0,"disorder_content":0.15654952076677317,"disprot_consensus":{"full":[{"start":1,"end":27,"type":"D"},{"start":107,"end":128,"type":"D"}],"Structural state":[{"start":1,"end":27,"type":"D"},{"start":107,"end":128,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00104","name":"Ligand-binding domain of nuclear hormone receptor","start":337,"end":530},{"id":"PF00105","name":"Double treble clef zinc finger, C4 type","start":184,"end":252},{"id":"PF02159","name":"Oestrogen receptor","start":42,"end":181},{"id":"PF12743","name":"Oestrogen-type nuclear receptor final C-terminal","start":552,"end":595}],"gene3D":[{"start":302,"end":552,"id":"1.10.565.10","name":"Retinoid X Receptor"},{"start":175,"end":278,"id":"3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A"}]},"uniref50":"UniRef50_P03372","sequence":"MTMTLHTKASGMALLHQIQGNELEPLNRPQLKIPLERPLGEVYLDSSKPAVYNYPEGAAYEFNAAAAANAQVYGQTGLPYGPGSEAAAFGSNGLGGFPPLNSVSPSPLMLLHPPPQLSPFLQPHGQQVPYYLENEPSGYTVREAGPPAFYRPNSDNRRQGGRERLASTNDKGSMAMESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDGEGRGEVGSAGDMRAANLWPSPLMIKRSKKNSLALSLTADQMVSALLDAEPPILYSEYDPTRPFSEASMMGLLTNLADRELVHMINWAKRVPGFVDLTLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEGMVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLDKITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDLLLEMLDAHRLHAPTSRGGASVEETDQSHLATAGSTSSHSLQKYYITGEAEGFPATV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P03372","disprot_id":"DP00074","ncbi_taxon_id":9606,"regions_counter":19,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":184,"region_id":"DP00074r001","released":"2022_12","ec_id":"ECO:0006204","reference_html":"The N-terminal regions of estrogen receptor alpha and beta are unstructured in vitro and show different TBP binding properties. <i> Wärnmark A, Wikström A, Wright AP, Gustafsson JA, Härd T. </i> J Biol Chem, 2001","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"11595744","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-07-27T20:23:05.567Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"A random coil sequence yields a very typical CD spectrum, with a sharp negative minimum at 198 nm. The recorded CD spectra of ERα-N and ERβ-N both show this characteristic profile (Figs. 5 and 6). The CD data therefore strengthen the conclusion from NMR that the ERα-N and ERβ-N fragments are unstructured in solution.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:19:01.895Z"}},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":184,"term_name":"disorder to order","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"vnugnes","released":"2022_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"11595744","version":3,"reference_html":"The N-terminal regions of estrogen receptor alpha and beta are unstructured in vitro and show different TBP binding properties. <i> Wärnmark A, Wikström A, Wright AP, Gustafsson JA, Härd T. </i> J Biol Chem, 2001","date":"2022-07-27T20:31:30.246Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00074r002","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P13393"}],"statement":[{"text":"The most likely cause for the observed effect is that the structured TBP induces a folding event in the unstructured ERα-N transactivation region.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:19:16.720Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":184,"region_id":"DP00074r003","released":"2022_12","ec_id":"ECO:0006165","reference_html":"The N-terminal regions of estrogen receptor alpha and beta are unstructured in vitro and show different TBP binding properties. <i> Wärnmark A, Wikström A, Wright AP, Gustafsson JA, Härd T. </i> J Biol Chem, 2001","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"11595744","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-07-27T20:22:19.293Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The HSQC spectra of ERα-N recorded in buffers with a neutral or basic pH contain very few and weak signals compared with the spectra recorded in buffers with acidic pH (data not shown). Likewise, backbone amide NMR signals decrease significantly as the temperature is increased from 5 to 20 °C (data not shown). Both effects reflect significant hydrogen exchange between amide protons and water at higher temperature and pH in the absence of stable intramolecular hydrogen bonds. ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:19:07.276Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":236,"region_id":"DP00074r005","released":"2022_12","ec_id":"ECO:0006165","reference_html":"DNA recognition by the oestrogen receptor: from solution to the crystal. <i> Schwabe JW, Chapman L, Finch JT, Rhodes D, Neuhaus D. </i> Structure, 1993","term_id":"IDPO:0000002","curator_id":"vnugnes","start":214,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16100953","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-07-29T15:47:53.999Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"1HCP"}],"statement":[{"text":"Superpositions onto the appropriate average structure were made using the Ca, N and C atoms of residues 4-35 and 59-74, since the backbone conformation at the termini and between residues 36 and 58 is comparatively poorly defined by the NMR data.","type":"Results"},{"text":"The residues 36-58 of the peptide analized by the autors corresponds to the 214-236 region of the protein.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:19:09.358Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":262,"region_id":"DP00074r008","released":"2022_12","ec_id":"ECO:0006165","reference_html":"DNA recognition by the oestrogen receptor: from solution to the crystal. <i> Schwabe JW, Chapman L, Finch JT, Rhodes D, Neuhaus D. </i> Structure, 1993","term_id":"IDPO:0000002","curator_id":"vnugnes","start":253,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16100953","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-07-29T15:49:49.757Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"1HCP"}],"statement":[{"text":"Superpositions onto the appropriate average structure were made using the Ca, N and C atoms of residues 4-35 and 59-74, since the backbone conformation at the termini and between residues 36 and 58 is comparatively poorly defined by the NMR data.","type":"Results"},{"text":"The residues 75-84 of the peptide analized by the autors, which lacks structure, corresponds to the 252-261 region of the protein.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:19:12.474Z"}},{"start":1,"end":184,"reference_id":"11595744","reference_source":"pmid","reference_html":"The N-terminal regions of estrogen receptor alpha and beta are unstructured in vitro and show different TBP binding properties. <i> Wärnmark A, Wikström A, Wright AP, Gustafsson JA, Härd T. </i> J Biol Chem, 2001","date":"2022-07-27T20:27:59.815Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0017025","term_name":"TBP-class protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P13393","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00074r011","statement":[{"text":"Fig. 3 Aillustrates the injection of purified yTBP over the surfaces captured with ΕRα-N (solid line) and ERβ-N (dotted line), respectively. The sensogram clearly shows binding of TBP to ERα-N but no significant binding to ERβ-N. ","type":"Results"},{"text":"TBP is a key protein of the transcription machinery and has been proposed as a target factor for a number of transcriptional activators.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a member of the class of TATA-binding proteins (TBP), including any of the TBP-related factors (TRFs).\" [GOC:jl, GOC:txnOH, http://www.mblab.gla.ac.uk/, PMID:16858867]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:19:23.154Z"}},{"start":287,"end":305,"reference_id":"22275375","reference_source":"pmid","reference_html":"Structural basis for Ca2+-induced activation and dimerization of estrogen receptor α by calmodulin. <i> Zhang Y, Li Z, Sacks DB, Ames JB. </i> J Biol Chem, 2012","date":"2022-07-27T20:41:41.441Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00074r012","statement":[{"text":"The main chain structure of ER(287–305) in the absence of CaM is unstructured, although it adopts an α-helical structure upon binding to CaM (Fig. 2).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:19:14.264Z"}},{"start":287,"end":305,"reference_id":"22275375","reference_source":"pmid","reference_html":"Structural basis for Ca2+-induced activation and dimerization of estrogen receptor α by calmodulin. <i> Zhang Y, Li Z, Sacks DB, Ames JB. </i> J Biol Chem, 2012","date":"2022-07-27T20:43:58.976Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"2LLO"},{"db":"PDB","id":"2LLQ"}],"region_id":"DP00074r013","statement":[{"text":"The main chain structure of ER(287–305) in the absence of CaM is unstructured, although it adopts an α-helical structure upon binding to CaM (Fig. 2).","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0DP33"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:19:21.424Z"}},{"start":287,"end":305,"reference_id":"22275375","reference_source":"pmid","reference_html":"Structural basis for Ca2+-induced activation and dimerization of estrogen receptor α by calmodulin. <i> Zhang Y, Li Z, Sacks DB, Ames JB. </i> J Biol Chem, 2012","date":"2022-07-27T20:43:37.421Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005516","term_name":"calmodulin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"2LLO"},{"db":"PDB","id":"2LLQ"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P0DP33","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00074r014","statement":[{"text":"The main chain structure of ER(287–305) in the absence of CaM is unstructured, although it adopts an α-helical structure upon binding to CaM (Fig. 2).","type":"Results"}],"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:19:25.896Z"}},{"start":300,"end":304,"reference_id":"18471979","reference_source":"pmid","reference_html":"Regulation of estrogen receptor alpha by the SET7 lysine methyltransferase. <i> Subramanian K, Jia D, Kapoor-Vazirani P, Powell DR, Collins RE, Sharma D, Peng J, Cheng X, Vertino PM. </i> Mol Cell, 2008","date":"2022-07-29T14:30:32.578Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000042","term_name":"methylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00074r015","statement":[{"text":"Recombinant SET7 methylated an ER peptide encompassing amino acids 294-314 of the hinge region, whereas two other histone H3 lysine 9-specific HMTases, G9a and Dim-5, did not (Figure 1B). In contrast, all three enzymes were able to methylate a histone H3 peptide (amino acids 1-24), suggesting that the methylation of the ER peptide by SET7 is specific.","type":"Results"},{"text":"Subsequent MS/MS analysis identified lysine 302 (K302) as the single site of methylation (Figure S1C).","type":"Results"},{"text":"Taken together, these data indicate that SET7-mediated methylation modulates the stability of ER and this effect is mediated through modification at K302.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:19:28.748Z"}},{"start":300,"end":305,"reference_id":"18471979","reference_source":"pmid","reference_html":"Regulation of estrogen receptor alpha by the SET7 lysine methyltransferase. <i> Subramanian K, Jia D, Kapoor-Vazirani P, Powell DR, Collins RE, Sharma D, Peng J, Cheng X, Vertino PM. </i> Mol Cell, 2008","date":"2022-07-27T21:15:20.680Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000042","term_name":"methylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00074r016","statement":[{"text":"Methylated ER was detected in cells expressing wild-type ER, but not the ER-K302R mutant (Figure 2A).","type":"Results"},{"text":"These data indicate that ER is methylated at K302 in vivo, and that the neighboring lysine, K303, impacts methylation of K302 by SET7.","type":"Results"},{"text":"Taken together, these data indicate that SET7-mediated methylation modulates the stability of ER and this effect is mediated through modification at K302.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:19:31.035Z"}},{"start":1,"end":180,"reference_id":"21946067","reference_source":"pmid","reference_html":"The role of 14-3-3β in transcriptional activation of estrogen receptor α and its involvement in proliferation of breast cancer cells. <i> Kim Y, Kim H, Jang SW, Ko J. </i> Biochem Biophys Res Commun, 2011","date":"2022-07-29T14:13:26.037Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0071889","term_name":"14-3-3 protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":167,"end":167,"position":"Specific residue"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P31946","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00074r017","statement":[{"text":"Results showed that 14-3-3β bound to the AF-1 domain of ERα; however, the DBD and AF-2 domains did not bind to 14-3-3β (Fig. 2C).","type":"Results"},{"text":" These results indicate that 14-3-3β interacts with ERα through the AF-1 domain of ERα in a ligand-dependent manner and Akt phosphorylation is critical in this event.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a 14-3-3 protein. A 14-3-3 protein is any of a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells, and have been implicated in the modulation of distinct biological processes by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. Each 14-3-3 protein sequence can be roughly divided into three sections: a divergent amino terminus, the conserved core region and a divergent carboxy-terminus. The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain, a cradle for interacting with client proteins.\" [GOC:cna, GOC:mah, PMID:15167810, PMID:19575580]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:19:36.464Z"}},{"start":301,"end":305,"reference_id":"15604293","reference_source":"pmid","reference_html":"Phosphorylation of estrogen receptor alpha blocks its acetylation and regulates estrogen sensitivity. <i> Cui Y, Zhang M, Pestell R, Curran EM, Welshons WV, Fuqua SA. </i> Cancer Res, 2004","date":"2022-07-29T14:37:18.691Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000039","term_name":"acetylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001190","ec_ontology":"ECO","ec_name":"in vitro acetylation assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00074r018","statement":[{"text":"As expected, autoacetylation of GST-p300 was seen in all of the lanes, and WT ERα was efficiently and selectively acetylated by p300. In contrast, all of the K303 substitutions were hypoacetylated.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:19:39.373Z"}},{"start":301,"end":305,"reference_id":"15604293","reference_source":"pmid","reference_html":"Phosphorylation of estrogen receptor alpha blocks its acetylation and regulates estrogen sensitivity. <i> Cui Y, Zhang M, Pestell R, Curran EM, Welshons WV, Fuqua SA. </i> Cancer Res, 2004","date":"2022-07-29T16:53:36.013Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser305Asp","start":null,"end":null,"position":null}],"region_id":"DP00074r019","statement":[{"text":"We found that the S294A mutation had little effect on ERα phosphorylation but that the S305D mutation greatly reduced the phosphorylation of the ERα fragment.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:19:41.197Z"}}],"released":"2016_10","uniref100":"UniRef100_P03372","date":"2016-08-23T14:25:32.000Z","acc":"P03372","name":"Estrogen receptor","length":595,"organism":"Homo sapiens","dataset":["Cancer-related proteins","Condensates-related proteins"],"UniParc":"UPI0000040F02","genes":[{"name":{"value":"ESR1"},"synonyms":[{"value":"ESR"},{"value":"NR3A1"}]}],"alphafold_very_low_content":0.4672268907563025,"disorder_content":0.39663865546218485,"disprot_consensus":{"full":[{"start":1,"end":184,"type":"T"},{"start":214,"end":236,"type":"D"},{"start":253,"end":262,"type":"D"},{"start":287,"end":305,"type":"T"}],"Structural state":[{"start":1,"end":184,"type":"D"},{"start":214,"end":236,"type":"D"},{"start":253,"end":262,"type":"D"},{"start":287,"end":305,"type":"D"}],"Structural transition":[{"start":1,"end":184,"type":"T"},{"start":287,"end":305,"type":"T"}],"Molecular function":[{"start":1,"end":184,"type":"F"},{"start":287,"end":305,"type":"F"}],"Disorder function":[{"start":300,"end":305,"type":"F"}]}},{"acc":"P11387","sequence":"MSGDHLHNDSQIEADFRLNDSHKHKDKHKDREHRHKEHKKEKDREKSKHSNSEHKDSEKKHKEKEKTKHKDGSSEKHKDKHKDRDKEKRKEEKVRASGDAKIKKEKENGFSSPPQIKDEPEDDGYFVPPKEDIKPLKRPRDEDDADYKPKKIKTEDTKKEKKRKLEEEEDGKLKKPKNKDKDKKVPEPDNKKKKPKKEEEQKWKWWEEERYPEGIKWKFLEHKGPVFAPPYEPLPENVKFYYDGKVMKLSPKAEEVATFFAKMLDHEYTTKEIFRKNFFKDWRKEMTNEEKNIITNLSKCDFTQMSQYFKAQTEARKQMSKEEKLKIKEENEKLLKEYGFCIMDNHKERIANFKIEPPGLFRGRGNHPKMGMLKRRIMPEDIIINCSKDAKVPSPPPGHKWKEVRHDNKVTWLVSWTENIQGSIKYIMLNPSSRIKGEKDWQKYETARRLKKCVDKIRNQYREDWKSKEMKVRQRAVALYFIDKLALRAGNEKEEGETADTVGCCSLRVEHINLHPELDGQEYVVEFDFLGKDSIRYYNKVPVEKRVFKNLQLFMENKQPEDDLFDRLNTGILNKHLQDLMEGLTAKVFRTYNASITLQQQLKELTAPDENIPAKILSYNRANRAVAILCNHQRAPPKTFEKSMMNLQTKIDAKKEQLADARRDLKSAKADAKVMKDAKTKKVVESKKKAVQRLEEQLMKLEVQATDREENKQIALGTSKLNYLDPRITVAWCKKWGVPIEKIYNKTQREKFAWAIDMADEDYEF","alphafold_very_low_content":"0.2601307189542484","creator":"dpiovesan","dataset":["Cancer-related proteins","Condensates-related proteins"],"date":"2016-08-18T15:18:11.000Z","disprot_id":"DP00075","features":{"pfam":[{"id":"PF01028","name":"Eukaryotic DNA topoisomerase I, catalytic core","start":432,"end":664},{"id":"PF02919","name":"Eukaryotic DNA topoisomerase I, DNA binding fragment","start":215,"end":429},{"id":"PF14370","name":"C-terminal topoisomerase domain","start":695,"end":765}],"gene3D":[{"start":432,"end":586,"id":"3.90.15.10","name":"Topoisomerase I; Chain A, domain 3","_id":"685af523b4ac24d5329d73a8"},{"start":587,"end":765,"id":"1.10.132.10","name":"1.10.132.10","_id":"685af523b4ac24d5329d73a9"},{"start":232,"end":319,"id":"1.10.10.41","name":"Yeast DNA topoisomerase - domain 1","_id":"685af523b4ac24d5329d73aa"},{"start":204,"end":429,"id":"2.170.11.10","name":"DNA Topoisomerase I, domain 2","_id":"685af523b4ac24d5329d73ab"}]},"genes":[{"name":{"value":"TOP1","evidences":[],"_id":"685af523b4ac24d5329d73f4"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d73f3"}],"length":765,"name":"DNA topoisomerase 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":22,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI00001421A9","uniref100":"UniRef100_P11387","uniref50":"UniRef50_P11387","uniref90":"UniRef90_P11387","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006206","ec_name":"near-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":174,"interaction_partner":[],"reference_html":"Biochemical and biophysical analyses of recombinant forms of human topoisomerase I. <i> Stewart L, Ireton GC, Parker LH, Madden KR, Champoux JJ. </i> J Biol Chem, 1996","reference_id":"8631793","region_id":"DP00075r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Taking all of the information into account, gel filtration, sedimentation, and CD analyses, we conclude that the amino-terminal 174 resides of Topo I are largely unfolded and are comprised of very little if any extended secondary structure.","_id":"685af523b4ac24d5329d73ad"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-15T07:38:50.109Z","_id":"685af523b4ac24d5329d73ae"},"version":3,"_id":"685af523b4ac24d5329d73ac","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":652,"end":696,"interaction_partner":[],"reference_html":"The domain organization of human topoisomerase I. <i> Stewart L, Ireton GC, Champoux JJ. </i> J Biol Chem, 1996","reference_id":"8631794","region_id":"DP00075r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Evidence from limited proteolysis studies (see accompanying paper(40)) indicates that the former possibility is more likely to be correct. For example limited trypsin digestion of full-length Topo I generates a proteolytically resistant 55-kDa fragment that starts at residue Lys654 and ends somewhere very close to residue Lys654 (Fig. 1A in (40)).","_id":"685af523b4ac24d5329d73b0"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-15T07:38:47.757Z","_id":"685af523b4ac24d5329d73b1"},"version":3,"_id":"685af523b4ac24d5329d73af","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1A31","_id":"685af523b4ac24d5329d73b7"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":636,"end":712,"interaction_partner":[],"reference_html":"Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA. <i> Redinbo MR, Stewart L, Kuhn P, Champoux JJ, Hol WG. </i> Science, 1998","reference_id":"9488644","region_id":"DP00075r005","released":"2022_03","sample":[],"statement":[{"type":"Figure","text":"The side chains of Lys436, His632, and Asn722 and the main chain amide nitrogens of Asn491, Gln633, and Ala635 make contacts closer than 3.5 Å in this complex but not in the covalent complex (Fig. 4G; note that residues 628 to 635 are disordered and are not present in the structure of the covalent complex).","_id":"685af523b4ac24d5329d73b8"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-15T07:38:44.740Z","_id":"685af523b4ac24d5329d73b9"},"version":3,"_id":"685af523b4ac24d5329d73b6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":636,"end":712,"interaction_partner":[],"reference_html":"Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA. <i> Redinbo MR, Stewart L, Kuhn P, Champoux JJ, Hol WG. </i> Science, 1998","reference_id":"9488644","region_id":"DP00075r006","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"Thus, residues ∼636 to 712, which form the so-called linker domain, contribute to but are not required for activity (16).","_id":"685af523b4ac24d5329d73bb"}],"states_connection":[],"term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-15T07:39:10.365Z","_id":"685af523b4ac24d5329d73bc"},"version":4,"_id":"685af523b4ac24d5329d73ba","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1A35","_id":"685af523b4ac24d5329d73be"},{"db":"PDB","id":"1A31","_id":"685af523b4ac24d5329d73bf"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":175,"end":214,"interaction_partner":[],"reference_html":"Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA. <i> Redinbo MR, Stewart L, Kuhn P, Champoux JJ, Hol WG. </i> Science, 1998","reference_id":"9488644","region_id":"DP00075r007","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"The ∼210-residue NH2-terminal region of human topo I is highly charged, contains very few hydrophobic amino acids, and is largely disordered (12).","_id":"685af523b4ac24d5329d73c0"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-15T07:38:41.861Z","_id":"685af523b4ac24d5329d73c1"},"version":3,"_id":"685af523b4ac24d5329d73bd","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1A35","_id":"685af523b4ac24d5329d73cb"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-21T10:55:16.021Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":628,"end":719,"interaction_partner":[],"reference_html":"Crystal structures of human topoisomerase I in covalent and noncovalent complexes with DNA. <i> Redinbo MR, Stewart L, Kuhn P, Champoux JJ, Hol WG. </i> Science, 1998","reference_id":"9488644","region_id":"DP00075r012","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"The only significant differences between the structures occur in the active-site region (as discussed below); in addition, residues 628 to 635 of subdomain III and 715 to 719 of the COOH-terminal domain are ordered in the noncovalent complex but are disordered in the covalent complex.","_id":"685af523b4ac24d5329d73cc"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-15T07:38:39.764Z","_id":"685af523b4ac24d5329d73cd"},"version":0,"_id":"685af523b4ac24d5329d73ca","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-21T11:08:12.340Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":174,"interaction_partner":[],"reference_html":"The domain organization of human topoisomerase I. <i> Stewart L, Ireton GC, Champoux JJ. </i> J Biol Chem, 1996","reference_id":"8631794","region_id":"DP00075r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"While designing the purification scheme, we noticed that long term storage of nuclear extracts leads to proteolysis of the full-length enzyme into a fragments of 75 and 70 kDa, designated f-Topo75 and f-Topo70, respectively (Fig. 2B, lanes 4 and 5). ","_id":"685af523b4ac24d5329d73cf"},{"type":"Results","text":"Amino terminal sequencing confirmed that f-Topo75 was missing the first 137 residues while f-Topo70 was missing the first 174 residues.","_id":"685af523b4ac24d5329d73d0"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-15T07:38:37.787Z","_id":"685af523b4ac24d5329d73d1"},"version":0,"_id":"685af523b4ac24d5329d73ce","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0007737","ec_name":"DNA detection assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":174,"interaction_partner":[],"reference_html":"Residues within the N-terminal domain of human topoisomerase I play a direct role in relaxation. <i> Lisby M, Olesen JR, Skouboe C, Krogh BO, Straub T, Boege F, Velmurugan S, Martensen PM, Andersen AH, Jayaram M, Westergaard O, Knudsen BR. </i> J Biol Chem, 2001","reference_id":"11283003","region_id":"DP00075r014","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In agreement with this finding, an N-terminal fragment of human topo I (amino acids 1–218) binds DNA in a filter binding assay (Fig. 3 B). Taken together, the obtained results suggest a role of the N-terminal domain or at least part of it in non-covalent DNA binding.","_id":"685af523b4ac24d5329d73d3"}],"states_connection":[],"term_comment":"","term_def":"\"The activity of binding selectively and non-covalently to and distorting the original structure of DNA, typically a straight helix, into a bend, or increasing the bend if the original structure was intrinsically bent due to its sequence.\" [GOC:krc, GOC:vw, PMID:10710711, PMID:19037758]","term_go_domain":"F","term_id":"GO:0008301","term_is_binding":true,"term_is_obsolete":false,"term_name":"DNA binding, bending","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-15T07:39:04.412Z","_id":"685af523b4ac24d5329d73d4"},"version":1,"_id":"685af523b4ac24d5329d73d2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0007737","ec_name":"DNA detection assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":174,"interaction_partner":[],"reference_html":"Residues within the N-terminal domain of human topoisomerase I play a direct role in relaxation. <i> Lisby M, Olesen JR, Skouboe C, Krogh BO, Straub T, Boege F, Velmurugan S, Martensen PM, Andersen AH, Jayaram M, Westergaard O, Knudsen BR. </i> J Biol Chem, 2001","reference_id":"11283003","region_id":"DP00075r015","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In agreement with this finding, an N-terminal fragment of human topo I (amino acids 1–218) binds DNA in a filter binding assay (Fig. 3 B). Taken together, the obtained results suggest a role of the N-terminal domain or at least part of it in non-covalent DNA binding.","_id":"685af523b4ac24d5329d73d6"}],"states_connection":[],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_go_domain":"F","term_id":"GO:0003677","term_is_binding":true,"term_is_obsolete":false,"term_name":"DNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-15T07:39:00.998Z","_id":"685af523b4ac24d5329d73d7"},"version":1,"_id":"685af523b4ac24d5329d73d5","reference_source":"pmid"},{"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Here, we investigated the ability of hTOP1 to form liquid condensates by transiently expressing exogenous GFP-tagged hTOP1 in HeLa cells."}]}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2025-12-18T14:59:27.620Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006067","ec_name":"fluorescence recovery after photobleaching evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":214,"reference_html":"Condensation of the N-terminal domain of human topoisomerase 1 is driven by electrostatic interactions and tuned by its charge distribution. <i> Bianchi G, Mangiagalli M, Ami D, Ahmed J, Lombardi S, Longhi S, Natalello A, Tompa P, Brocca S. </i> Int J Biol Macromol, 2024","reference_id":"38287572","region_id":"DP00075r019","released":"2026_06","statement":[{"type":"Title","text":"Condensation of the N-terminal domain of human topoisomerase 1 is driven\nby electrostatic interactions and tuned by its charge distribution","_id":"685af523b4ac24d5329d73db"},{"type":"Results","text":"hTOP1 forms liquid condensates in vivo","_id":"685af523b4ac24d5329d73dc"},{"type":"Results","text":" Here, we investigated the ability of hTOP1 to form liquid condensates by transiently expressing exogenous GFP-tagged hTOP1 in HeLa cells. In our cellular model, hTOP1 indeed forms nucleoplasmatic and nucleolar condensates, giving rise to a sparse punctuate pattern (Fig. 1A). Notably, these condensates exhibit a liquid-like behavior, as indicated by FRAP analyses, with a full fluorescence recovery within 80 s (Fig. 1B). In light of the well- established role of IDRs in LLPS, we reasoned that the formation of hTOP1 condensates might be primarily driven by its hNTD (residues 1–214), which has been identified as intrinsically disordered [39].","_id":"685af523b4ac24d5329d73dd"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_id":"GO:0140693","term_is_obsolete":false,"term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":1,"_id":"685af523b4ac24d5329d73d8","reference_source":"pmid","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":10.5,"statements":[{"type":"Results","text":"To evaluate its propensity to condense, hNTD was prepared in an alkaline buffer at pH 10.5 with 50 mM of NaCl. By subsequently adding a small quantity of HCl, the solution pH was lowered to 7.5."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7.5,"statements":[{"type":"Results","text":"To evaluate its propensity to condense, hNTD was prepared in an alkaline buffer at pH 10.5 with 50 mM of NaCl. By subsequently adding a small quantity of HCl, the solution pH was lowered to 7.5."}]}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2025-12-18T14:58:56.864Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006307","ec_name":"turbidity measurement evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":214,"reference_html":"Condensation of the N-terminal domain of human topoisomerase 1 is driven by electrostatic interactions and tuned by its charge distribution. <i> Bianchi G, Mangiagalli M, Ami D, Ahmed J, Lombardi S, Longhi S, Natalello A, Tompa P, Brocca S. </i> Int J Biol Macromol, 2024","reference_id":"38287572","region_id":"DP00075r020","released":"2023_12","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":50,"db":"ChEBI","id":"26710","statements":[{"type":"Results","text":"To evaluate its propensity to condense, hNTD was prepared in an alkaline buffer at pH 10.5 with 50 mM of NaCl. By subsequently adding a small quantity of HCl, the solution pH was lowered to 7.5."}],"entry_name":null}],"statement":[{"type":"Results","text":"We found that protein concentration influenced the maximum turbidimetry value but not its kinetics (Fig. 3A). To investigate whether electrostatic charges drove the protein condensation, we performed the pH jump in the presence of increasing salt concentrations, which can inhibit electrostatic interactions. We observed a significant decrease in turbidity at 150 mM and 300 mM of NaCl (Fig. 3A), indicating the crucial role of electrostatic interactions in hNTD condensation. Since turbidimetry alone does not specifically confirm LLPS and could be ascribable to the formation of amorphous/fibrillar aggregates, confocal microscopic analyses were conducted to identify LLPS hall­ marks: spherical shape, the ability to undergo fusion events, and liquid- like behavior [41].","_id":"685af523b4ac24d5329d73e1"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_id":"GO:0140693","term_is_obsolete":false,"term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":1,"_id":"685af523b4ac24d5329d73de","reference_source":"pmid","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-12-18T14:58:59.134Z"}},{"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7.5,"statements":[{"type":"Results","text":"To monitor the secondary structure content of the condensates, we utilized Fourier transform infrared (FTIR) spectroscopy directly applied to protein condensates harvested by centrifugating samples after the pH jump (spin assay, Fig. 3E). Before the pH jump, the second derivative spectrum of hNTD showed a main component at ~1644 cm − 1 , indicative of disordered structures [42]."}]}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2025-12-18T14:58:15.812Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006228","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":214,"reference_html":"Condensation of the N-terminal domain of human topoisomerase 1 is driven by electrostatic interactions and tuned by its charge distribution. <i> Bianchi G, Mangiagalli M, Ami D, Ahmed J, Lombardi S, Longhi S, Natalello A, Tompa P, Brocca S. </i> Int J Biol Macromol, 2024","reference_id":"38287572","region_id":"DP00075r021","released":"2026_06","statement":[{"type":"Results","text":"To monitor the secondary structure content of the condensates, we utilized Fourier transform infrared (FTIR) spectroscopy directly applied to protein condensates harvested by centrifugating samples after the pH jump (spin assay, Fig. 3E). Before the pH jump, the second derivative spectrum of hNTD showed a main component at ~1644 cm − 1 , indicative of disordered structures [42]. Additionally, low-intensity peaks at ~1677 and ~1688 cm − 1 , within the spectral re­ gions of turns and β-sheets (black line in Fig. 3E), suggested the existence of some residual secondary structure [43]. These elements of secondary structure were also observed in the far-UV CD spectrum of hNTD recorded in alkaline phosphate buffer (Fig. S4A). After the pH jump, the FTIR spectrum of the supernatant (red line in Fig. 3E) resembled that observed before the pH jump, with the main peak shifted from ~1644 to ~1652 cm − 1 , suggesting that the pH jump induced only minor changes in the secondary structure of unassembled hNTD. The FTIR spectrum of the pellet (blue line in Fig. 3E) collected after the pH jump displayed the main peak at ~1652 cm − 1 and a new component at low intensity around 1630 cm − 1 , implying the formation of intermolecular β-sheets [42]. Overall, our data suggest that pH-induced condensation of hNTD does not induce drastic conformational changes within its disordered structure, and the involvement of intermolecular β-sheet structures in stabilizing protein condensates appears to be minimal. In summary, we have observed that pH jump can initiate the liquid condensation of hNTD.","_id":"685af523b4ac24d5329d73e9"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_id":"GO:0140693","term_is_obsolete":false,"term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":1,"_id":"685af523b4ac24d5329d73e6","reference_source":"pmid","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2025-12-18T14:57:14.758Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0005601","ec_name":"immunofluorescence confocal microscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":214,"reference_html":"Condensation of the N-terminal domain of human topoisomerase 1 is driven by electrostatic interactions and tuned by its charge distribution. <i> Bianchi G, Mangiagalli M, Ami D, Ahmed J, Lombardi S, Longhi S, Natalello A, Tompa P, Brocca S. </i> Int J Biol Macromol, 2024","reference_id":"38287572","region_id":"DP00075r022","released":"2026_06","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":50,"db":"ChEBI","id":"26710","statements":[{"type":"Results","text":"Droplet size decreased with increasing salt concentration: their areas halved from 50 to 150 mM NaCl and were reduced ten times from 50 to 300 mM NaCl (Fig. 3B)."}],"entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":150,"db":"ChEBI","id":"26710","statements":[{"type":"Results","text":"Droplet size decreased with increasing salt concentration: their areas halved from 50 to 150 mM NaCl and were reduced ten times from 50 to 300 mM NaCl (Fig. 3B)."}],"entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":300,"db":"ChEBI","id":"26710","statements":[{"type":"Results","text":"Droplet size decreased with increasing salt concentration: their areas halved from 50 to 150 mM NaCl and were reduced ten times from 50 to 300 mM NaCl (Fig. 3B)."}],"entry_name":null}],"statement":[{"type":"Results","text":"Since turbidimetry alone does not specifically confirm LLPS and could be ascribable to the formation of amorphous/fibrillar aggregates, confocal microscopic analyses were conducted to identify LLPS hall­ marks: spherical shape, the ability to undergo fusion events, and liquid- like behavior [41]. The morphology and material properties of pH- induced condensates were investigated via confocal fluorescence mi­croscopy and FRAP analysis on the hNTD-GFP construct.","_id":"685af523b4ac24d5329d73f1"},{"type":"Results","text":"Condensates of hNTD-GFP obtained at low salt concentration (50 mM NaCl) displayed an average area of 0.65 ± 0.35 μ m 2 (Fig. 3B) and a liquid-like behavior, coalescing readily (Fig. 3C) and recovering fluo­ rescence efficiently after photobleaching (~80 % within 1 min) (Fig. 3D). Droplet size decreased with increasing salt concentration: their areas halved from 50 to 150 mM NaCl and were reduced ten times from 50 to 300 mM NaCl (Fig. 3B).","_id":"685af523b4ac24d5329d73f2"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_id":"GO:0140693","term_is_obsolete":false,"term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":1,"_id":"685af523b4ac24d5329d73ea","reference_source":"pmid","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"}],"__v":0,"disorder_content":0.4,"disprot_consensus":{"full":[{"start":1,"end":214,"type":"D"},{"start":628,"end":719,"type":"D"}],"Structural state":[{"start":1,"end":214,"type":"D"},{"start":628,"end":719,"type":"D"}],"Disorder function":[{"start":636,"end":712,"type":"F"}],"Molecular function":[{"start":1,"end":214,"type":"F"}]}},{"acc":"P06786","sequence":"MSTEPVSASDKYQKISQLEHILKRPDTYIGSVETQEQLQWIYDEETDCMIEKNVTIVPGLFKIFDEILVNAADNKVRDPSMKRIDVNIHAEEHTIEVKNDGKGIPIEIHNKENIYIPEMIFGHLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTEFILETADLNVGQKYVQKWENNMSICHPPKITSYKKGPSYTKVTFKPDLTRFGMKELDNDILGVMRRRVYDINGSVRDINVYLNGKSLKIRNFKNYVELYLKSLEKKRQLDNGEDGAAKSDIPTILYERINNRWEVAFAVSDISFQQISFVNSIATTMGGTHVNYITDQIVKKISEILKKKKKKSVKSFQIKNNMFIFINCLIENPAFTSQTKEQLTTRVKDFGSRCEIPLEYINKIMKTDLATRMFEIADANEENALKKSDGTRKSRITNYPKLEDANKAGTKEGYKCTLVLTEGDSALSLAVAGLAVVGRDYYGCYPLRGKMLNVREASADQILKNAEIQAIKKIMGLQHRKKYEDTKSLRYGHLMIMTDQDHDGSHIKGLIINFLESSFPGLLDIQGFLLEFITPIIKVSITKPTKNTIAFYNMPDYEKWREEESHKFTWKQKYYKGLGTSLAQEVREYFSNLDRHLKIFHSLQGNDKDYIDLAFSKKKADDRKEWLRQYEPGTVLDPTLKEIPISDFINKELILFSLADNIRSIPNVLDGFKPGQRKVLYGCFKKNLKSELKVAQLAPYVSECTAYHHGEQSLAQTIIGLAQNFVGSNNIYLLLPNGAFGTRATGGKDAAAARYIYTELNKLTRKIFHPADDPLYKYIQEDEKTVEPEWYLPILPMILVNGAEGIGTGWSTYIPPFNPLEIIKNIRHLMNDEELEQMHPWFRGWTGTIEEIEPLRYRMYGRIEQIGDNVLEITELPARTWTSTIKEYLLLGLSGNDKIKPWIKDMEEQHDDNIKFIITLSPEEMAKTRKIGFYERFKLISPISLMNMVAFDPHGKIKKYNSVNEILSEFYYVRLEYYQKRKDHMSERLQWEVEKYSFQVKFIKMIIEKELTVTNKPRNAIIQELENLGFPRFNKEGKPYYGSPNDEIAEQINDVKGATSDEEDEESSHEDTENVINGPEELYGTYEYLLGMRIWSLTKERYQKLLKQKQEKETELENLLKLSAKDIWNTDLKAFEVGYQEFLQRDAEARGGNVPNKGSKTKGKGKRKLVDDEDYDPSKKNKKSTARKGKKIKLEDKNFERILLEQKLVTKSKAPTKIKKEKTPSVSETKTEEEENAPSSTSSSSIFDIKKEDKDEGELSKISNKFKKISTIFDKMGSTSATSKENTPEQDDVATKKNQTTAKKTAVKPKLAKKPVRKQQKVVELSGESDLEILDSYTDREDSNKDEDDAIPQRSRRQRSSRAASVPKKSYVETLELSDDSFIEDDEEENQGSDVSFNEED","alphafold_very_low_content":"0.18907563025210083","creator":"eleonardi","dataset":[],"date":"2016-08-26T11:58:38.000Z","disprot_id":"DP00076","features":{"pfam":[{"id":"PF00204","name":"DNA gyrase B","start":247,"end":374},{"id":"PF00521","name":"DNA gyrase/topoisomerase IV, subunit A","start":690,"end":1160},{"id":"PF01751","name":"Toprim domain","start":445,"end":543},{"id":"PF02518","name":"Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase","start":60,"end":167},{"id":"PF16898","name":"C-terminal associated domain of TOPRIM","start":559,"end":688}],"gene3D":[{"start":429,"end":687,"id":"3.40.50.670","name":"3.40.50.670","_id":"685af523b4ac24d5329d73fa"},{"start":279,"end":406,"id":"3.30.230.10","name":"3.30.230.10","_id":"685af523b4ac24d5329d73fb"},{"start":15,"end":258,"id":"3.30.565.10","name":"Histidine kinase-like ATPase, C-terminal domain","_id":"685af523b4ac24d5329d73fc"},{"start":562,"end":608,"id":"3.30.1490.30","name":"3.30.1490.30","_id":"685af523b4ac24d5329d73fd"}]},"genes":[{"name":{"value":"TOP2","evidences":[],"_id":"685af523b4ac24d5329d7460"},"synonyms":[{"value":"TOR3","evidences":[],"_id":"685af523b4ac24d5329d7461"}],"olnNames":[{"value":"YNL088W","evidences":[],"_id":"685af523b4ac24d5329d7463"}],"orfNames":[{"value":"N2244","evidences":[],"_id":"685af523b4ac24d5329d7462"}],"_id":"685af523b4ac24d5329d745f"}],"length":1428,"name":"DNA topoisomerase 2","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":26,"released":"2016_10","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"UniParc":"UPI000015F7DC","uniref100":"UniRef100_P06786","uniref50":"UniRef50_P06786","uniref90":"UniRef90_P06786","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1BJT","_id":"685af523b4ac24d5329d7414"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-18T15:51:11.360Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":632,"end":652,"interaction_partner":[],"reference_html":"Quaternary changes in topoisomerase II may direct orthogonal movement of two DNA strands. <i> Fass D, Bogden CE, Berger JM. </i> Nat Struct Biol, 1999","reference_id":"10201398","region_id":"DP00076r008","released":"2023_06","sample":[],"statement":[{"type":"Curator statement","text":"The PDB structure shows this region lacks electron density, indicating it is disordered.","_id":"685af523b4ac24d5329d7415"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d7413","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1BJT","_id":"685af523b4ac24d5329d7417"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-18T15:51:24.818Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":660,"end":674,"interaction_partner":[],"reference_html":"Quaternary changes in topoisomerase II may direct orthogonal movement of two DNA strands. <i> Fass D, Bogden CE, Berger JM. </i> Nat Struct Biol, 1999","reference_id":"10201398","region_id":"DP00076r009","released":"2023_06","sample":[],"statement":[],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d7416","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1BJT","_id":"685af523b4ac24d5329d7419"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-18T15:52:02.842Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1072,"end":1106,"interaction_partner":[],"reference_html":"Quaternary changes in topoisomerase II may direct orthogonal movement of two DNA strands. <i> Fass D, Bogden CE, Berger JM. </i> Nat Struct Biol, 1999","reference_id":"10201398","region_id":"DP00076r010","released":"2023_06","sample":[],"statement":[{"type":"Curator statement","text":"The PDB structure shows this region lacks electron density, indicating it is disordered.","_id":"685af523b4ac24d5329d741a"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d7418","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1BJT","_id":"685af523b4ac24d5329d741c"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-18T15:50:52.196Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1179,"end":1201,"interaction_partner":[],"reference_html":"Quaternary changes in topoisomerase II may direct orthogonal movement of two DNA strands. <i> Fass D, Bogden CE, Berger JM. </i> Nat Struct Biol, 1999","reference_id":"10201398","region_id":"DP00076r011","released":"2023_06","sample":[],"statement":[{"type":"Curator statement","text":"The PDB structure shows this region lacks electron density, indicating it is disordered.","_id":"685af523b4ac24d5329d741d"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d741b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":782,"end":782,"statements":[],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d742b"}],"cross_refs":[{"db":"PDB","id":"4GFH","_id":"685af523b4ac24d5329d742a"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-18T15:44:03.798Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1071,"end":1106,"interaction_partner":[],"reference_html":"Structure of a topoisomerase II-DNA-nucleotide complex reveals a new control mechanism for ATPase activity. <i> Schmidt BH, Osheroff N, Berger JM. </i> Nat Struct Mol Biol, 2012","reference_id":"23022727","region_id":"DP00076r016","released":"2023_06","sample":[{"db":"ChEBI","deviation":null,"entry_name":"magnesium(2+)","id":"18420","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d742c"},{"db":"ChEBI","deviation":null,"entry_name":"AMP-PNP","id":"47785","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d742d"},{"db":null,"deviation":null,"id":null,"statements":[{"type":"Curator statement","text":"DNA substrate used to obtain this crystal structure :5'-GAGGATGACGATTCGCGGTAGCAGTAGGAG","_id":"685af523b4ac24d5329d742f"}],"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_id":"UO:0000023","unit_name":"µg","value":null,"_id":"685af523b4ac24d5329d742e"}],"statement":[{"type":"Curator statement","text":"The PDB structure shows this region lacks electron density, indicating it is disordered.","_id":"685af523b4ac24d5329d7430"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d7429","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1QZR","_id":"685af523b4ac24d5329d7435"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-18T15:10:51.674Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":259,"end":274,"interaction_partner":[],"reference_html":"Structure of the topoisomerase II ATPase region and its mechanism of inhibition by the chemotherapeutic agent ICRF-187. <i> Classen S, Olland S, Berger JM. </i> Proc Natl Acad Sci U S A, 2003","reference_id":"12963818","region_id":"DP00076r018","released":"2023_06","sample":[{"db":"ChEBI","deviation":null,"entry_name":"magnesium(2+)","id":"18420","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7436"},{"db":"ChEBI","deviation":null,"entry_name":"AMP-PNP","id":"47785","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7437"},{"db":"PubChem","deviation":null,"id":"CID:6918223","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7438"}],"statement":[{"type":"Curator statement","text":"The PDB structure shows this region lacks electron density, indicating it is disordered.","_id":"685af523b4ac24d5329d7439"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d7434","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1BGW","_id":"685af523b4ac24d5329d743d"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":409,"end":418,"interaction_partner":[],"reference_html":"Structure and mechanism of DNA topoisomerase II. <i> Berger JM, Gamblin SJ, Harrison SC, Wang JC. </i> Nature, 1996","reference_id":"8538787","region_id":"DP00076r020","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The disorder region is missing from the pdb but not metioned in the article.","_id":"685af523b4ac24d5329d743e"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-01-13T15:06:19.247Z","_id":"685af523b4ac24d5329d743f"},"version":1,"_id":"685af523b4ac24d5329d743c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1BGW","_id":"685af523b4ac24d5329d7441"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1077,"end":1106,"interaction_partner":[],"reference_html":"Structure and mechanism of DNA topoisomerase II. <i> Berger JM, Gamblin SJ, Harrison SC, Wang JC. </i> Nature, 1996","reference_id":"8538787","region_id":"DP00076r021","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The disorder region is missing from the pdb but not metioned in the article.","_id":"685af523b4ac24d5329d7442"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-01-13T15:05:50.314Z","_id":"685af523b4ac24d5329d7443"},"version":1,"_id":"685af523b4ac24d5329d7440","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1BGW","_id":"685af523b4ac24d5329d7445"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1178,"end":1201,"interaction_partner":[],"reference_html":"Structure and mechanism of DNA topoisomerase II. <i> Berger JM, Gamblin SJ, Harrison SC, Wang JC. </i> Nature, 1996","reference_id":"8538787","region_id":"DP00076r022","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The disorder region is missing from the pdb but not metioned in the article.","_id":"685af523b4ac24d5329d7446"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-01-13T15:04:50.298Z","_id":"685af523b4ac24d5329d7447"},"version":1,"_id":"685af523b4ac24d5329d7444","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1BGW","_id":"685af523b4ac24d5329d7449"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":633,"end":681,"interaction_partner":[],"reference_html":"Structure and mechanism of DNA topoisomerase II. <i> Berger JM, Gamblin SJ, Harrison SC, Wang JC. </i> Nature, 1996","reference_id":"8538787","region_id":"DP00076r023","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The segment of 48 amino acids between the two subfragments (residues 634-681) is disordered.","_id":"685af523b4ac24d5329d744a"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-01-13T15:04:35.493Z","_id":"685af523b4ac24d5329d744b"},"version":1,"_id":"685af523b4ac24d5329d7448","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":782,"end":782,"statements":[],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d744d"}],"cross_refs":[{"db":"PDB","id":"4GFH","_id":"685af523b4ac24d5329d744e"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-18T15:46:15.806Z","disprot_namespace":"Structural state","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":409,"end":420,"interaction_partner":[],"reference_html":"Structure of a topoisomerase II-DNA-nucleotide complex reveals a new control mechanism for ATPase activity. <i> Schmidt BH, Osheroff N, Berger JM. </i> Nat Struct Mol Biol, 2012","reference_id":"23022727","region_id":"DP00076r024","released":"2023_06","sample":[{"db":"ChEBI","deviation":null,"entry_name":"magnesium(2+)","id":"18420","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d744f"},{"db":"ChEBI","deviation":null,"entry_name":"AMP-PNP","id":"47785","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7450"},{"db":null,"deviation":null,"id":"","statements":[{"type":"Curator statement","text":"DNA substrate used to obtain this crystal structure :5'-GAGGATGACGATTCGCGGTAGCAGTAGGAG","_id":"685af523b4ac24d5329d7452"}],"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_id":"UO:0000023","unit_name":"µg","value":null,"_id":"685af523b4ac24d5329d7451"}],"statement":[{"type":"Curator statement","text":"The PDB structure shows this region lacks electron density, indicating it is disordered.","_id":"685af523b4ac24d5329d7453"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d744c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":782,"end":782,"statements":[],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d7455"}],"cross_refs":[{"db":"PDB","id":"4GFH","_id":"685af523b4ac24d5329d7456"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-18T15:46:48.594Z","disprot_namespace":"Structural state","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":259,"end":275,"interaction_partner":[],"reference_html":"Structure of a topoisomerase II-DNA-nucleotide complex reveals a new control mechanism for ATPase activity. <i> Schmidt BH, Osheroff N, Berger JM. </i> Nat Struct Mol Biol, 2012","reference_id":"23022727","region_id":"DP00076r025","released":"2023_06","sample":[{"db":"ChEBI","deviation":null,"entry_name":"magnesium(2+)","id":"18420","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7457"},{"db":"ChEBI","deviation":null,"entry_name":"AMP-PNP","id":"47785","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7458"},{"db":null,"deviation":null,"id":"","statements":[{"type":"Curator statement","text":"DNA substrate used to obtain this crystal structure :5'-GAGGATGACGATTCGCGGTAGCAGTAGGAG","_id":"685af523b4ac24d5329d745a"}],"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_id":"UO:0000023","unit_name":"µg","value":null,"_id":"685af523b4ac24d5329d7459"}],"statement":[{"type":"Curator statement","text":"The PDB structure shows this region lacks electron density, indicating it is disordered.","_id":"685af523b4ac24d5329d745b"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d7454","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1BJT","_id":"685af523b4ac24d5329d745d"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-18T15:53:11.460Z","disprot_namespace":"Structural state","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":409,"end":418,"interaction_partner":[],"reference_html":"Quaternary changes in topoisomerase II may direct orthogonal movement of two DNA strands. <i> Fass D, Bogden CE, Berger JM. </i> Nat Struct Biol, 1999","reference_id":"10201398","region_id":"DP00076r026","released":"2023_06","sample":[],"statement":[{"type":"Curator statement","text":"The PDB structure shows this region lacks electron density, indicating it is disordered.","_id":"685af523b4ac24d5329d745e"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d745c","reference_source":"pmid"}],"__v":0,"disorder_content":0.09733893557422969,"disprot_consensus":{"full":[{"start":259,"end":275,"type":"D"},{"start":409,"end":420,"type":"D"},{"start":632,"end":681,"type":"D"},{"start":1071,"end":1106,"type":"D"},{"start":1178,"end":1201,"type":"D"}],"Structural state":[{"start":259,"end":275,"type":"D"},{"start":409,"end":420,"type":"D"},{"start":632,"end":681,"type":"D"},{"start":1071,"end":1106,"type":"D"},{"start":1178,"end":1201,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00096","name":"Zinc finger, C2H2 type","start":104,"end":126},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":132,"end":155}],"gene3D":[{"start":128,"end":160,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":102,"end":127,"id":"3.30.160.60","name":"Classic Zinc Finger"}]},"uniref50":"UniRef50_P07248","sequence":"MANVEKPNDCSGFPVVDLNSCFSNGFNNEKQEIEMETDDSPILLMSSSASRENSNTFSVIQRTPDGKIITTNNNMNSKINKQLDKLPENLRLNGRTPSGKLRSFVCEVCTRAFARQEHLKRHYRSHTNEKPYPCGLCNRCFTRRDLLIRHAQKIHSGNLGETISHTKKVSRTITKARKNSASSVKFQTPTYGTPDNGNFLNRTTANTRRKASPEANVKRKYLKKLTRRASFSAQSASSYALPDQSSLEQHPKDRVKFSTPELVPLDLKNPELDSSFDLNMNLDLNLNLDSNFNIALNRSDSSGSTMNLDYKLPESANNYTYSSGSPTRAYVGANTNSKNASFNDADLLSSSYWIKAYNDHLFSVSESDETSPMNSELNDTKLIVPDFKSTIHHLKDSRSSSWTVAIDNNSNNNKVSDNQPDFVDFQELLDNDTLGNDLLETTAVLKEFELLHDDSVSATATSNEIDLSHLNLSNSPISPHKLIYKNKEGTNDDMLISFGLDHPSNREDDLDKLCNMTRDVQAIFSQYLKGEESKRSLEDFLSTSNRKEKPDSGNYTFYGLDCLTLSKISRALPASTVNNNQPSHSIESKLFNEPMRNMCIKVLRYYEKFSHDSSESVMDSNPNLLSKELLMPAVSELNEYLDLFKNNFLPHFPIIHPSLLDLDLDSLQRYTNEDGYDDAENAQLFDRLSQGTDKEYDYEHYQILSISKIVCLPLFMATFGSLHKFGYKSQTIELYEMSRRILHSFLETKRRCRSTTVNDSYQNIWLMQSLILSFMFALVADYLEKIDSSLMKRQLSALCSTIRSNCLPTISANSEKSINNNNEPLTFGSPLQYIIFESKIRCTLMAYDFCQFLKCFFHIKFDLSIKEKDVETIYIPDNESKWASESIICNGHVVQKQNFYDFRNFYYSFTYGHLHSIPEFLGSSMIYYEYDLRKGTKSHVFLDRIDTKRLERSLDTSSYGNDNMAATNKNIAILIDDTIILKNNLMSMRFIKQIDRSFTEKVRKGQIAKIYDSFLNSVRLNFLKNYSVEVLCEFLVALNFSIRNISSLYVEEESDCSQRMNSPELPRIHLNNQALSVFNLQGYYYCFILIIKFLLDFEATPNFKLLRIFIELRSLANSILLPTLSRLYPQEFSGFPDVVFTQQFINKDNGMLVPGLSANEHHNGASAAVKTKLAKKINVEGLAMFINEILVNSFNDTSFLNMEDPIRNEFSFDNGDRAVTDLPRSAHFLSDTGLEGINFSGLNDSHQTVSTLNLLRYGENHSSKHKNGGKGQGFAEKYQLSLKYVTIAKLFFTNVKENYIHCHMLDKMASDFHTLENHLKGNS","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P07248","disprot_id":"DP00077","ncbi_taxon_id":559292,"regions_counter":18,"creator":"ftonello","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":103,"region_id":"DP00077r009","released":"2022_03","ec_id":"ECO:0006198","reference_html":"A disorder-to-order transition coupled to DNA binding in the essential zinc-finger DNA-binding domain of yeast ADR1. <i> Hyre DE, Klevit RE. </i> J Mol Biol, 1998","statement":[{"text":"In conjunction with the low hNOE values, lack of protection from exchange, low R1,H values, and random-coil chemical shift values, the results confirm that the N-terminal region displays all the hallmarks of an unstructured polypeptide, right up to S103 or F104, the first hydrogen-bonded residue of the first zinc-finger.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":75,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9642072","version":2,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":103,"term_name":"molecular adaptor activity","start":75,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","statement":[{"text":"Mutation and deletion analyses of ADR1 have identified the two (Cys2,His2) zinc fingers, residues 103 to 155, plus approximately 20 residues preceding the first finger, the proximal region, as the minimal portion of ADR1 capable of sequence-specific binding to the DNA promoter sequence UAS1 (upstream activation sequence 1; Thukral et al 1991a, Thukral et al 1991b).","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"9642072","version":3,"reference_html":"A disorder-to-order transition coupled to DNA binding in the essential zinc-finger DNA-binding domain of yeast ADR1. <i> Hyre DE, Klevit RE. </i> J Mol Biol, 1998","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006198","region_id":"DP00077r010","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":103,"term_name":"nucleic acid binding","start":75,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","statement":[{"text":"We conclude that the region of ADR1-DBD essential for high-affinity binding undergoes a disorder-to-order transition upon binding to its cognate DNA and, together with the zinc fingers, forms a cohesive molecular complex with the nucleic acid.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"9642072","version":3,"reference_html":"A disorder-to-order transition coupled to DNA binding in the essential zinc-finger DNA-binding domain of yeast ADR1. <i> Hyre DE, Klevit RE. </i> J Mol Biol, 1998","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006198","region_id":"DP00077r011","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":103,"term_name":"disorder to order","start":75,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","statement":[{"text":"ADR1-DBD undergoes a disorder-to-order transition upon binding to its cognate DNA, with the largest changes occurring in the N-terminal proximal region.","type":"Conclusion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9642072","version":2,"reference_html":"A disorder-to-order transition coupled to DNA binding in the essential zinc-finger DNA-binding domain of yeast ADR1. <i> Hyre DE, Klevit RE. </i> J Mol Biol, 1998","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006198","region_id":"DP00077r012","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":102,"region_id":"DP00077r013","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A folding transition and novel zinc finger accessory domain in the transcription factor ADR1. <i> Bowers PM, Schaufler LE, Klevit RE. </i> Nat Struct Biol, 1999","statement":[{"text":"We have used a set of HN-HN NOEs derived from a perdeuterated protein–DNA complex to describe the fold of ADR1 bound to the UAS1 binding site.","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":84,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10331877","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2ADR"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":102,"term_name":"nucleic acid binding","start":84,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"The region responsible for sequence-specific DNA binding by the transcription factor ADR1 contains two Cys2–His2 zinc fingers and an additional N-terminal proximal accessory region (PAR).","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"10331877","version":3,"reference_html":"A folding transition and novel zinc finger accessory domain in the transcription factor ADR1. <i> Bowers PM, Schaufler LE, Klevit RE. </i> Nat Struct Biol, 1999","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006165","region_id":"DP00077r014","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":102,"term_name":"disorder to order","start":84,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"The N-terminal (non-finger) PAR is unstructured in the absence of DNA and undergoes a folding transition on binding the DNA transcription target site.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10331877","version":2,"reference_html":"A folding transition and novel zinc finger accessory domain in the transcription factor ADR1. <i> Bowers PM, Schaufler LE, Klevit RE. </i> Nat Struct Biol, 1999","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00077r015","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":102,"region_id":"DP00077r016","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR chemical shift perturbation mapping of DNA binding by a zinc-finger domain from the yeast transcription factor ADR1. <i> Schmiedeskamp M, Rajagopal P, Klevit RE. </i> Protein Sci, 1997","statement":[{"text":"The dramatic chemical shift perturbations of the N-terminus upon DNA binding are remarkably consistent with mutagenesis data that previously defined the essential N-terminal region. 1H and 13C chemical shift perturbation become significant starting at residue 86.\nFurthermore the residues more perturbed lie between P87 and P97, flanking the site of the affinity-enhancing suppressor mutation R91K.","type":"Conclusion"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":86,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9300483","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":102,"term_name":"disorder to order","start":86,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"The study concluded that the two zinc fingers are pre-structured and do not undergo significant conformational change upon DNA binding. In contrast, residues 86 to 102 in the N-terminal proximal region exhibit large chemical shift perturbations upon DNA binding and do not exhibit regular secondary structure in either the free or bound form [from PMID:9642072].","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9300483","version":2,"reference_html":"NMR chemical shift perturbation mapping of DNA binding by a zinc-finger domain from the yeast transcription factor ADR1. <i> Schmiedeskamp M, Rajagopal P, Klevit RE. </i> Protein Sci, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00077r017","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":102,"term_name":"nucleic acid binding","start":86,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"The severely perturbed N-terminus does not appear to interact with the exposed, unperturbed portions of the zinc finger in the protein-DNA complex.\nThese data taken together suggest that the region P87-P97 plays a role in contacting DNA and therby increases the binding affinity of the construct.","type":"Conclusion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"9300483","version":3,"reference_html":"NMR chemical shift perturbation mapping of DNA binding by a zinc-finger domain from the yeast transcription factor ADR1. <i> Schmiedeskamp M, Rajagopal P, Klevit RE. </i> Protein Sci, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006165","region_id":"DP00077r018","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P07248","date":"2016-09-05T16:52:15.000Z","acc":"P07248","name":"Regulatory protein ADR1","length":1323,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000125604","genes":[{"name":{"value":"ADR1"},"orfNames":[{"value":"YD8142.16"},{"value":"YD8142B.08"}],"olnNames":[{"value":"YDR216W"}]}],"alphafold_very_low_content":0.5230536659108088,"disorder_content":0.021919879062736205,"disprot_consensus":{"full":[{"start":75,"end":103,"type":"T"}],"Structural state":[{"start":75,"end":103,"type":"D"}],"Molecular function":[{"start":75,"end":103,"type":"F"}],"Structural transition":[{"start":75,"end":103,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00170","name":"bZIP transcription factor","start":135,"end":194}],"gene3D":[{"start":138,"end":193,"id":"1.20.5.170","name":"1.20.5.170"}]},"uniref50":"UniRef50_P01100","sequence":"MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNAQDFCTDLAVSSANFIPTVTAISTSPDLQWLVQPALVSSVAPSQTRAPHPFGVPAPSAGAYSRAGVVKTMTGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLTGGLPEVATPESEEAFTLPLLNDPEPKPSVEPVKSISSMELKTEPFDDFLFPASSRPSGSETARSVPDMDLSGSFYAADWEPLHSGSLGMGPMATELEPLCTPVVTCTPSCTAYTSSFVFTYPEADSFPSCAAAHRKGSSSNEPSSDSLSSPTLLAL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P01100","disprot_id":"DP00078","ncbi_taxon_id":9606,"regions_counter":3,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":380,"region_id":"DP00078r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Intrinsic structural disorder of the C-terminal activation domain from the bZIP transcription factor Fos. <i> Campbell KM, Terrell AR, Laybourn PJ, Lumb KJ. </i> Biochemistry, 2000","term_id":"IDPO:0000002","curator_id":"esalladini","start":216,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"10704222","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"We show here that the C-terminal activation domain of human c-Fos (residues 216−380; Figure 1), although functionally active, is essentially devoid of the stable helical or β-sheet structure typical of globular proteins. We conclude that c-Fos contains an intrinsically disordered yet biologically active activation domain.","type":"Abstract"},{"text":"Instead, the spectrum contains a negative band at 198 nm and a shoulder centered at 220 nm (above 5 °C), which are indicative of a disordered conformation ( 33).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-10-02T13:47:58.776Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":380,"region_id":"DP00078r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Effects of macromolecular crowding on the intrinsically disordered proteins c-Fos and p27(Kip1). <i> Flaugh SL, Lumb KJ. </i> Biomacromolecules, 2001","term_id":"IDPO:0000002","curator_id":"esalladini","start":216,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"11749217","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"The CD spectrum of FosAD at 5 °C is reminiscent of an unfolded protein (Figure 1A), in accord with previous results.","type":"Article"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-10-02T13:47:59.980Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":380,"region_id":"DP00078r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Intrinsic structural disorder of the C-terminal activation domain from the bZIP transcription factor Fos. <i> Campbell KM, Terrell AR, Laybourn PJ, Lumb KJ. </i> Biochemistry, 2000","term_id":"IDPO:0000002","curator_id":"esalladini","start":216,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"10704222","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"We show here that the C-terminal activation domain of human c-Fos (residues 216−380; Figure 1), although functionally active, is essentially devoid of the stable helical or β-sheet structure typical of globular proteins. We conclude that c-Fos contains an intrinsically disordered yet biologically active activation domain.","type":"Abstract"},{"text":"The heteronuclear 1H-15N NOE provides information on mainchain flexibility. In particular, 1H-15N NOEs are positive in folded, globular proteins and reduced or negative in unfolded and disordered proteins ( 37−41).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-10-02T13:48:02.351Z"}}],"released":"2016_10","uniref100":"UniRef100_P01100","date":"2016-08-24T10:47:38.000Z","acc":"P01100","name":"Proto-oncogene c-Fos","length":380,"organism":"Homo sapiens","dataset":["Autophagy-related proteins"],"UniParc":"UPI000000D8F5","genes":[{"name":{"value":"FOS"},"synonyms":[{"value":"G0S7"}]}],"alphafold_very_low_content":0.5394736842105263,"disorder_content":0.4342105263157895,"disprot_consensus":{"full":[{"start":216,"end":380,"type":"D"}],"Structural state":[{"start":216,"end":380,"type":"D"}]}},{"acc":"Q92731","sequence":"MDIKNSPSSLNSPSSYNCSQSILPLEHGSIYIPSSYVDSHHEYPAMTFYSPAVMNYSIPSNVTNLEGGPGRQTTSPNVLWPTPGHLSPLVVHRQLSHLYAEPQKSPWCEARSLEHTLPVNRETLKRKVSGNRCASPVTGPGSKRDAHFCAVCSDYASGYHYGVWSCEGCKAFFKRSIQGHNDYICPATNQCTIDKNRRKSCQACRLRKCYEVGMVKCGSRRERCGYRLVRRQRSADEQLHCAGKAKRSGGHAPRVRELLLDALSPEQLVLTLLEAEPPHVLISRPSAPFTEASMMMSLTKLADKELVHMISWAKKIPGFVELSLFDQVRLLESCWMEVLMMGLMWRSIDHPGKLIFAPDLVLDRDEGKCVEGILEIFDMLLATTSRFRELKLQHKEYLCVKAMILLNSSMYPLVTATQDADSSRKLAHLLNAVTDALVWVIAKSGISSQQQSMRLANLLMLLSHVRHASNKGMEHLLNMKCKNVVPVYDLLLEMLNAHVLRGCKSSITGSECSPAEDSKSKEGSQNPQSQ","alphafold_very_low_content":"0.4037735849056604","creator":"fquaglia","dataset":["NDDs-related proteins"],"date":"2016-08-17T13:03:38.000Z","disprot_id":"DP00079","features":{"pfam":[{"id":"PF00104","name":"Ligand-binding domain of nuclear hormone receptor","start":287,"end":480},{"id":"PF00105","name":"Double treble clef zinc finger, C4 type","start":148,"end":216},{"id":"PF12497","name":"Estrogen receptor beta","start":12,"end":125}],"gene3D":[{"start":140,"end":246,"id":"3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A","_id":"685af523b4ac24d5329d7467"},{"start":255,"end":509,"id":"1.10.565.10","name":"Retinoid X Receptor","_id":"685af523b4ac24d5329d7468"}]},"genes":[{"name":{"value":"ESR2","evidences":[],"_id":"685af523b4ac24d5329d7478"},"synonyms":[{"value":"ESTRB","evidences":[],"_id":"685af523b4ac24d5329d7479"},{"value":"NR3A2","evidences":[],"_id":"685af523b4ac24d5329d747a"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d7477"}],"length":530,"name":"Estrogen receptor beta","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":6,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI000002EA37","uniref100":"UniRef100_Q92731","uniref50":"UniRef50_Q62986-5","uniref90":"UniRef90_Q92731","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":103,"interaction_partner":[],"reference_html":"The N-terminal regions of estrogen receptor alpha and beta are unstructured in vitro and show different TBP binding properties. <i> Wärnmark A, Wikström A, Wright AP, Gustafsson JA, Härd T. </i> J Biol Chem, 2001","reference_id":"11595744","region_id":"DP00079r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The recorded CD spectra of ERα-N and ERβ-N both show this characteristic profile (Figs. 5 and 6). The CD data therefore strengthen the conclusion from NMR that the ERα-N and ERβ-N fragments are unstructured in solution.","_id":"685af523b4ac24d5329d746a"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-05-02T17:46:37.829Z","_id":"685af523b4ac24d5329d746b"},"version":3,"_id":"685af523b4ac24d5329d7469","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":103,"interaction_partner":[],"reference_html":"The N-terminal regions of estrogen receptor alpha and beta are unstructured in vitro and show different TBP binding properties. <i> Wärnmark A, Wikström A, Wright AP, Gustafsson JA, Härd T. </i> J Biol Chem, 2001","reference_id":"11595744","region_id":"DP00079r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Similarly, the HSQC spectrum of ERβ-N (Fig. 2 B) also has a very limited amide chemical shift dispersion that corresponds well with typical random coil resonance shifts.","_id":"685af523b4ac24d5329d746f"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-05-02T17:46:14.951Z","_id":"685af523b4ac24d5329d7470"},"version":3,"_id":"685af523b4ac24d5329d746e","reference_source":"pmid"}],"__v":0,"disorder_content":0.19433962264150945,"disprot_consensus":{"full":[{"start":1,"end":103,"type":"D"}],"Structural state":[{"start":1,"end":103,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00439","name":"Bromodomain","start":1484,"end":1561},{"id":"PF00439","name":"Bromodomain","start":1602,"end":1680},{"id":"PF09247","name":"TATA box-binding protein binding","start":7,"end":75},{"id":"PF12157","name":"Protein of unknown function (DUF3591)","start":609,"end":1071},{"id":"PF15288","name":"Zinc knuckle","start":1345,"end":1375}],"gene3D":[{"start":11,"end":77,"id":"1.10.1100.10","name":"TAFII-230 TBP-binding domain"},{"start":1586,"end":1707,"id":"1.20.920.10","name":"Bromodomain-like"},{"start":1469,"end":1585,"id":"1.20.920.10","name":"Bromodomain-like"}]},"uniref50":"UniRef50_P51123","sequence":"MEMESDNSDDEGSIGNGLDLTGILFGNIDSEGRLLQDDDGEGRGGTGFDAELRENIGSLSKLGLDSMLLEVIDLKEAEPPSDDEEEEDARPSAVSASEGMSAFDALKAGVKREDGAVKAQDDAIDYSDITELSEDCPRTPPEETSTYDDLEDAIPASKVEAKLTKDDKELMPPPSAPMRSGSGGGIEEPAKSNDASSPSDDSKSTDSKDADRKLDTPLADILPSKYQNVDVRELFPDFRPQKVLRFSRLFGPGKPTSLPQIWRHVRKRRRKRNQSRDQKTTNTGGSDSPSDTEEPRKRGFSLHYAAEPTPAECMSDDEDKLLGDFNSEDVRPEGPDNGENSDQKPKVADWRFGPAQIWYDMLEVPDSGEGFNYGFKTKAASTSSQPQLKDERRVKSPEDDVEDPSIADDAFLMVSQLHWEDDVVWDGNDIKAKVLQKLNSKTNAAGWLPSSGSRTAGAFSQPGKPSMPVGSGSSKQGSGASSKKAQQNAQAKPAEAPDDTWYSLFPVENEELIYYKWEDEVIWDAQQVSKVPKPKVLTLDPNDENIILGIPDDIDPSKINKSTGPPPKIKIPHPHVKKSKILLGKAGVINVLAEDTPPPPPKSPDRDPFNISNDTYYTPKTEPTLRLKVGGNLIQHSTPVVELRAPFVPTHMGPMKLRAFHRPPLKKYSHGPMAQSIPHPVFPLLKTIAKKAKQREVERIASGGGDVFFMRNPEDLSGRDGDIVLAEFCEEHPPLINQVGMCSKIKNYYKRKAEKDSGPQDFVYGEVAFAHTSPFLGILHPGQCIQAIENNMYRAPIYPHKMAHNDFLVIRTRNNYWIRSVNSIYTVGQECPLYEVPGPNSKRANNFTRDFLQVFIYRLFWKSRDNPRRIRMDDIKQAFPAHSESSIRKRLKQCADFKRTGMDSNWWVIKPEFRLPSEEEIRAMVSPEQCCAYFSMIAAEQRLKDAGYGEKFLFAPQEDDDEEAQLKLDDEVKVAPWNTTRAYIQAMRGKCLLQLSGPADPTGCGEGFSYVRVPNKPTQTKEEQESQPKRSVTGTDADLRRLPLQRAKELLRQFKVPEEEIKKLSRWEVIDVVRTLSTEKAKAGEEGMDKFSRGNRFSIAEHQERYKEECQRIFDLQNRVLASSEVLSTDEAESSASEESDLEELGKNLENMLSNKKTSTQLSREREELERQELLRQLDEEHGGPSGSGGAKGAKGKDDPGQQMLATNNQGRILRITRTFRGNDGKEYTRVETVRRQPVIDAYIKIRTTKDEQFIKQFATLDEQQKEEMKREKRRIQEQLRRIKRNQERERLAQLAQNQKLQPGGMPTSLGDPKSSGGHSHKERDSGYKEVSPSRKKFKLKPDLKLKCGACGQVGHMRTNKACPLYSGMQSSLSQSNPSLADDFDEQSEKEMTMDDDDLVNVDGTKVTLSSKILKRHGGDDGKRRSGSSSGFTLKVPRDAMGKKKRRVGGDLHCDYLQRHNKTANRRRTDPVVVLSSILEIIHNELRSMPDVSPFLFPVSAKKVPDYYRVVTKPMDLQTMREYIRQRRYTSREMFLEDLKQIVDNSLIYNGPQSAYTLAAQRMFSSCFELLAEREDKLMRLEKAINPLLDDDDQVALSFIFDKLHSQIKQLPESWPFLKPVNKKQVKDYYTVIKRPMDLETIGKNIEAHRYHSRAEYLADIELIATNCEQYNGSDTRYTKFSKKILEYAQTQLIEFSEHCGQLENNIAKTQERARENAPEFDEAWGNDDYNFDRGSRASSPGDDYIDVEGHGGHASSSNSIHRSMGAEAGSSHTAPAVRKPAPPGPGEVKRGRGRPRKQRDPVEEVKSQNPVKRGRGRPRKDSLASNMSHTQAYFLDEDLQCSTDDEDDDEEEDFQEVSEDENNAASILDQGERINAPADAMDGMFDPKNIKTEIDLEAHQMAEEPIGEDDSQQVAEAMVQLSGVGGYYAQQQQDESMDVDPNYDPSDFLAMHKQRQSLGEPSSLQGAFTNFLSHEQDDNGPYNPAEASTSAASGADLGMDASMAMQMAPEMPVNTMNNGMGIDDDLDISESDEEDDGSRVRIKKEVFDDGDYALQHQQMGQAASQSQIYMVDSSNEPTTLDYQQPPQLDFQQVQEMEQLQHQVMPPMQSEQLQQQQTPQGDNDYAWTF","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_P51123","disprot_id":"DP00081","ncbi_taxon_id":7227,"regions_counter":4,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":77,"region_id":"DP00081r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of a TBP-TAF(II)230 complex: protein mimicry of the minor groove surface of the TATA box unwound by TBP. <i> Liu D, Ishima R, Tong KI, Bagby S, Kokubo T, Muhandiram DR, Kay LE, Nakatani Y, Ikura M. </i> Cell, 1998","term_id":"IDPO:0000002","curator_id":"esalladini","start":11,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"9741622","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1TBA"}],"term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"On the other hand, 1H-15N HSQC and CD spectra of free dTAFII23011–77 indicate that dTAFII23011–77 by itself is largely unfolded (Figure 2C).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":77,"term_name":"disorder to order","start":11,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"9741622","version":3,"reference_html":"Solution structure of a TBP-TAF(II)230 complex: protein mimicry of the minor groove surface of the TATA box unwound by TBP. <i> Liu D, Ishima R, Tong KI, Bagby S, Kokubo T, Muhandiram DR, Kay LE, Nakatani Y, Ikura M. </i> Cell, 1998","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00081r002","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"During a titration experiment in which 1H-15N HSQC spectra of dTAFII23011–77 were recorded with successive additions of TBP, most peaks corresponding to the unfolded state decrease in intensity and appear at new positions corresponding to the folded state, consistent with the high affinity of dTAFII23011–77 for TBP (Kd approximately 10−9 M).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":77,"term_name":"protein binding","start":11,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"9741622","version":4,"reference_html":"Solution structure of a TBP-TAF(II)230 complex: protein mimicry of the minor groove surface of the TATA box unwound by TBP. <i> Liu D, Ishima R, Tong KI, Bagby S, Kokubo T, Muhandiram DR, Kay LE, Nakatani Y, Ikura M. </i> Cell, 1998","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00081r003","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"During a titration experiment in which 1H-15N HSQC spectra of dTAFII23011–77 were recorded with successive additions of TBP, most peaks corresponding to the unfolded state decrease in intensity and appear at new positions corresponding to the folded state, consistent with the high affinity of dTAFII23011–77 for TBP (Kd approximately 10−9 M).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1840,"end":1860,"reference_id":"https://mobidb.org/P51123","reference_source":"mobidb","reference_html":"An Entry Referenced from MobiDB","date":"2022-02-14T09:00:00.000Z","curator_id":"amonzon","curator_name":"Alex Monzon","curator_orcid":"0000-0003-0362-8218","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007759","ec_ontology":"ECO","ec_name":"curator inference from database used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00081r004","statement":[{"text":"This poly-E region is inferred by the curator to be disordered, based on MobiDB-Lite and according to experimental evidence demonstrating that poly-E repeats display random-coil-like conformation (PMID:16949547)","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-21T12:02:07.315Z"},"ec_go":"IC","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P51123","date":"2016-09-12T09:54:34.000Z","acc":"P51123","name":"Transcription initiation factor TFIID subunit 1","length":2129,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI000016BFFE","genes":[{"name":{"value":"Taf1"},"synonyms":[{"value":"TAF250"}],"orfNames":[{"value":"CG17603"}]}],"alphafold_very_low_content":0.5044621888210428,"disorder_content":0.04133395960544857,"disprot_consensus":{"full":[{"start":11,"end":77,"type":"T"},{"start":1840,"end":1860,"type":"D"}],"Structural state":[{"start":11,"end":77,"type":"D"},{"start":1840,"end":1860,"type":"D"}],"Structural transition":[{"start":11,"end":77,"type":"T"}],"Molecular function":[{"start":11,"end":77,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02854","name":"MIF4G domain","start":607,"end":850},{"id":"PF12152","name":"Eukaryotic translation initiation factor 4G1","start":402,"end":469}],"gene3D":[{"start":597,"end":854,"id":"1.25.40.180","name":"1.25.40.180"},{"start":410,"end":478,"id":"1.20.970.30","name":"eIF4G, eIF4E-binding domain"}]},"uniref50":"UniRef50_P39935","sequence":"MTDETAHPTQSASKQESAALKQTGDDQQESQQQRGYTNYNNGSNYTQKKPYNSNRPHQQRGGKFGPNRYNNRGNYNGGGSFRGGHMGANSSNVPWTGYYNNYPVYYQPQQMAAAGSAPANPIPVEEKSPVPTKIEITTKSGEHLDLKEQHKAKLQSQERSTVSPQPESKLKETSDSTSTSTPTPTPSTNDSKASSEENISEAEKTRRNFIEQVKLRKAALEKKRKEQLEGSSGNNNIPMKTTPENVEEKGSDKPEVTEKTKPAEEKSAEPEVKQETPAEEGEQGEKGQIKEESTPKVLTFAERLKLKKQQKEREEKTEGKENKEVPVQEETKSAIESAPVPPSEQVKEETEVAETEQSNIDESATTPAIPTKSDEAEAEVEAEAGDAGTKIGLEAEIETTTDETDDGTNTVSHILNVLKDATPIEDVFSFNYPEGIEGPDIKYKKEHVKYTYGPTFLLQFKDKLNVKADAEWVQSTASKIVIPPGMGRGNRSRDSGRFGNNSSRGHDFRNTSVRNMDDRANSRTSSKRRSKRMNDDRRSNRSYTSRRDRERGSYRNEEKREDDKPKEEVAPLVPSANRWVPKFKSKKTEKKLAPDGKTELLDKDEVERKMKSLLNKLTLEMFDAISSEILAIANISVWETNGETLKAVIEQIFLKACDEPHWSSMYAQLCGKVVKELNPDITDETNEGKTGPKLVLHYLVARCHAEFDKGWTDKLPTNEDGTPLEPEMMSEEYYAAASAKRRGLGLVRFIGFLYRLNLLTGKMMFECFRRLMKDLTDSPSEETLESVVELLNTVGEQFETDSFRTGQATLEGSQLLDSLFGILDNIIQTAKISSRIKFKLIDIKELRHDKNWNSDKKDNGPKTIQQIHEEEERQRQLKNNSRSNSRRTNNSSNRHSFRRDAPPASKDSFITTRTYSQRNSQRAPPPKEEPAAPTSTATNMFSALMGESDDEE","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P39935","disprot_id":"DP00082","ncbi_taxon_id":559292,"regions_counter":23,"creator":"jssuarez","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":490,"region_id":"DP00082r001","reference_id":"14675538","start":393,"ec_id":"ECO:0006165","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The eukaryotic initiation factor 4G (eIF4G) is the core of a multicomponent switch controlling gene expression at the level of translation initiation. It interacts with the small ribosomal subunit interacting protein, eIF3, and the eIF4E/cap-mRNA complex in order to load the ribosome onto mRNA during cap-dependent translation. We describe the solution structure of the complex between yeast eIF4E/cap and eIF4G (393-490). Binding triggers a coupled folding transition of eIF4G (393-490) and the eIF4E N terminus resulting in a molecular bracelet whereby eIF4G (393-490) forms a right-handed helical ring that wraps around the N terminus of eIF4E.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"reference_html":"Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E. <i> Gross JD, Moerke NJ, von der Haar T, Lugovskoy AA, Sachs AB, McCarthy JE, Wagner G. </i> Cell, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","cross_refs":[{"db":"PDB","id":"1RF8"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-21T12:03:17.274Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":490,"term_name":"disorder to order","start":393,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The eukaryotic initiation factor 4G (eIF4G) is the core of a multicomponent switch controlling gene expression at the level of translation initiation. It interacts with the small ribosomal subunit interacting protein, eIF3, and the eIF4E/cap-mRNA complex in order to load the ribosome onto mRNA during cap-dependent translation. We describe the solution structure of the complex between yeast eIF4E/cap and eIF4G (393-490). Binding triggers a coupled folding transition of eIF4G (393-490) and the eIF4E N terminus resulting in a molecular bracelet whereby eIF4G (393-490) forms a right-handed helical ring that wraps around the N terminus of eIF4E.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14675538","version":3,"reference_html":"Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E. <i> Gross JD, Moerke NJ, von der Haar T, Lugovskoy AA, Sachs AB, McCarthy JE, Wagner G. </i> Cell, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00082r002","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-21T12:03:14.610Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P07260","partner_end":null}],"ec_ontology":"ECO","end":490,"term_name":"protein binding","start":393,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The eukaryotic initiation factor 4G (eIF4G) is the core of a multicomponent switch controlling gene expression at the level of translation initiation. It interacts with the small ribosomal subunit interacting protein, eIF3, and the eIF4E/cap-mRNA complex in order to load the ribosome onto mRNA during cap-dependent translation. We describe the solution structure of the complex between yeast eIF4E/cap and eIF4G (393-490). Binding triggers a coupled folding transition of eIF4G (393-490) and the eIF4E N terminus resulting in a molecular bracelet whereby eIF4G (393-490) forms a right-handed helical ring that wraps around the N terminus of eIF4E.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"14675538","version":4,"reference_html":"Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E. <i> Gross JD, Moerke NJ, von der Haar T, Lugovskoy AA, Sachs AB, McCarthy JE, Wagner G. </i> Cell, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00082r003","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-21T12:03:12.957Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":490,"region_id":"DP00082r004","reference_id":"10409688","start":393,"ec_id":"ECO:0006165","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Here we report that a 98-amino acid fragment of S. cerevisiae eIF4G1 that contains this eIF4E binding peptide undergoes an unfolded to folded transition upon binding to eIF4E. The folding of the eIF4G1 domain was evidenced by the eIF4E-dependent changes in its protease sensitivity and (1)H-(15)N HSQC NMR spectrum.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"reference_html":"The Cap-binding protein eIF4E promotes folding of a functional domain of yeast translation initiation factor eIF4G1. <i> Hershey PE, McWhirter SM, Gross JD, Wagner G, Alber T, Sachs AB. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-21T12:03:18.744Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":490,"term_name":"disorder to order","start":393,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Here we report that a 98-amino acid fragment of S. cerevisiae eIF4G1 that contains this eIF4E binding peptide undergoes an unfolded to folded transition upon binding to eIF4E. The folding of the eIF4G1 domain was evidenced by the eIF4E-dependent changes in its protease sensitivity and (1)H-(15)N HSQC NMR spectrum.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10409688","version":3,"reference_html":"The Cap-binding protein eIF4E promotes folding of a functional domain of yeast translation initiation factor eIF4G1. <i> Hershey PE, McWhirter SM, Gross JD, Wagner G, Alber T, Sachs AB. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00082r005","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-21T12:03:15.659Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P07260","partner_end":null}],"ec_ontology":"ECO","end":490,"term_name":"protein binding","start":393,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Here we report that a 98-amino acid fragment of S. cerevisiae eIF4G1 that contains this eIF4E binding peptide undergoes an unfolded to folded transition upon binding to eIF4E. The folding of the eIF4G1 domain was evidenced by the eIF4E-dependent changes in its protease sensitivity and (1)H-(15)N HSQC NMR spectrum.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"10409688","version":4,"reference_html":"The Cap-binding protein eIF4E promotes folding of a functional domain of yeast translation initiation factor eIF4G1. <i> Hershey PE, McWhirter SM, Gross JD, Wagner G, Alber T, Sachs AB. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00082r006","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-21T12:03:13.726Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":249,"reference_id":"36213119","reference_source":"pmid","reference_html":"eIF4G1 N-terminal intrinsically disordered domain is a multi-docking station for RNA, Pab1, Pub1, and self-assembly. <i> Chaves-Arquero B, Martínez-Lumbreras S, Sibille N, Camero S, Bernadó P, Jiménez MÁ, Zorrilla S, Pérez-Cañadillas JM. </i> Front Mol Biosci, 2022","date":"2022-10-14T08:10:30.079Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00082r007","statement":[{"text":"The 1H-15N HSQC NMR spectrum of eIF4G1 1-249 is characteristic of an intrinsically disordered protein (IDP) with low dispersion in the proton dimension and sharp signals (Figure 1B).","type":"Results"}]},{"start":187,"end":239,"reference_id":"36213119","reference_source":"pmid","reference_html":"eIF4G1 N-terminal intrinsically disordered domain is a multi-docking station for RNA, Pab1, Pub1, and self-assembly. <i> Chaves-Arquero B, Martínez-Lumbreras S, Sibille N, Camero S, Bernadó P, Jiménez MÁ, Zorrilla S, Pérez-Cañadillas JM. </i> Front Mol Biosci, 2022","date":"2022-10-14T08:12:00.392Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00082r008","statement":[{"text":"Analysis of eIF4G1 1-249 secondary structure based on 13C chemical shifts, T1/T2 15N relaxation times and residual dipolar couplings (RDCs) revealed the presence of an α-helix within BOX3 (Figure 2A). This finding was confirmed by characteristic sequential amide-amide NOEs measured in a 3D 1H-15N-HSQC-NOESY-1H-15N HSQC spectrum (Supplementary Figure S3). We determined the NMR structure of this α-helix using a BOX3 model peptide (eIF4G1 187-234) (Supplementary Figure S3). No further standard secondary structure elements were identified in eIF4G11-249.","type":"Results"}]},{"start":1,"end":239,"reference_id":"36213119","reference_source":"pmid","reference_html":"eIF4G1 N-terminal intrinsically disordered domain is a multi-docking station for RNA, Pab1, Pub1, and self-assembly. <i> Chaves-Arquero B, Martínez-Lumbreras S, Sibille N, Camero S, Bernadó P, Jiménez MÁ, Zorrilla S, Pérez-Cañadillas JM. </i> Front Mol Biosci, 2022","date":"2022-10-14T08:14:40.586Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00082r009","statement":[{"text":"The SAXS curve evidenced the IDP nature of eIF4G11-249 (Figure 2C).","type":"Results"}]},{"start":39,"end":45,"reference_id":"36213119","reference_source":"pmid","reference_html":"eIF4G1 N-terminal intrinsically disordered domain is a multi-docking station for RNA, Pab1, Pub1, and self-assembly. <i> Chaves-Arquero B, Martínez-Lumbreras S, Sibille N, Camero S, Bernadó P, Jiménez MÁ, Zorrilla S, Pérez-Cañadillas JM. </i> Front Mol Biosci, 2022","date":"2022-10-17T09:24:47.765Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P32588","operator":null,"partner_start":341,"partner_end":413}],"region_id":"DP00082r010","statement":[{"text":"Here we mapped this interaction on eIF4G11-249 by analysis of changes on the 1H-15N HSQC spectra, which indicated three putative binding sites for RRM3 in eIF4G11-249 (orange bar chart in Figure 3A): two in RNA1 (RNA1-1 and RNA1-2) and one in BOX1. Strikingly, these sites have a small consensus sequence motif (YNNxxxY), only present in this region of the eIF4G1.","type":"Results"},{"text":"We tested the ability of short peptides of eIF4G1 that corresponded to the conserved elements (Figure 3B) to bind to 15N-labelled Pub1 RRM3, by monitoring their effect on the Pub1 RRM3 1H-15N HSQC spectrum. Only BOX1 and RNA1-1 peptides caused changes in the Pub1 spectrum arising from direct contacts (Figure 3B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":100,"end":106,"reference_id":"36213119","reference_source":"pmid","reference_html":"eIF4G1 N-terminal intrinsically disordered domain is a multi-docking station for RNA, Pab1, Pub1, and self-assembly. <i> Chaves-Arquero B, Martínez-Lumbreras S, Sibille N, Camero S, Bernadó P, Jiménez MÁ, Zorrilla S, Pérez-Cañadillas JM. </i> Front Mol Biosci, 2022","date":"2022-10-17T09:26:13.058Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P32588","operator":null,"partner_start":341,"partner_end":413}],"region_id":"DP00082r011","statement":[{"text":"Here we mapped this interaction on eIF4G11-249 by analysis of changes on the 1H-15N HSQC spectra, which indicated three putative binding sites for RRM3 in eIF4G11-249 (orange bar chart in Figure 3A): two in RNA1 (RNA1-1 and RNA1-2) and one in BOX1. Strikingly, these sites have a small consensus sequence motif (YNNxxxY), only present in this region of the eIF4G1.","type":"Results"},{"text":"We tested the ability of short peptides of eIF4G1 that corresponded to the conserved elements (Figure 3B) to bind to 15N-labelled Pub1 RRM3, by monitoring their effect on the Pub1 RRM3 1H-15N HSQC spectrum. Only BOX1 and RNA1-1 peptides caused changes in the Pub1 spectrum arising from direct contacts (Figure 3B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":35,"end":49,"reference_id":"36213119","reference_source":"pmid","reference_html":"eIF4G1 N-terminal intrinsically disordered domain is a multi-docking station for RNA, Pab1, Pub1, and self-assembly. <i> Chaves-Arquero B, Martínez-Lumbreras S, Sibille N, Camero S, Bernadó P, Jiménez MÁ, Zorrilla S, Pérez-Cañadillas JM. </i> Front Mol Biosci, 2022","date":"2022-10-17T09:34:21.029Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6Z29"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P32588","operator":null,"partner_start":316,"partner_end":414}],"region_id":"DP00082r012","sequence_construct":"GSGYTNYNNGSNYTQKKQTIGLPPQVNPQAVDHIIRSAPPRVTTAYIGNIPHFATEADLIPLFQNFGFILDFKHYPEKGCCFIKYDTHEQAAVCIVALANFPFQGRNLRTGWGKER","statement":[{"text":"The NMR spectrum of the eIF4G1 peptide fused to the C-terminus of Pub1 was similar to that of Pub1 RRM3 alone (Figure 4A right), whereas that of the N-terminally fused chimera differed significantly (Figure 4A, left), suggesting that the peptide can effectively fold-back into the binding site only in the latter case. Using this latter construct, we obtained enough experimental restraints to calculate the structure of the eIF4G135-49-Pub1 RRM3 chimera (PDB: 6Z29), which shed light on the key elements required for molecular recognition (Figure 4B and Supplementary Figure S8).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":35,"end":49,"reference_id":"36213119","reference_source":"pmid","reference_html":"eIF4G1 N-terminal intrinsically disordered domain is a multi-docking station for RNA, Pab1, Pub1, and self-assembly. <i> Chaves-Arquero B, Martínez-Lumbreras S, Sibille N, Camero S, Bernadó P, Jiménez MÁ, Zorrilla S, Pérez-Cañadillas JM. </i> Front Mol Biosci, 2022","date":"2022-10-17T09:42:46.618Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6Z29"}],"region_id":"DP00082r013","sequence_construct":"GSGYTNYNNGSNYTQKKQTIGLPPQVNPQAVDHIIRSAPPRVTTAYIGNIPHFATEADLIPLFQNFGFILDFKHYPEKGCCFIKYDTHEQAAVCIVALANFPFQGRNLRTGWGKER","statement":[{"text":"The NMR spectrum of the eIF4G1 peptide fused to the C-terminus of Pub1 was similar to that of Pub1 RRM3 alone (Figure 4A right), whereas that of the N-terminally fused chimera differed significantly (Figure 4A, left), suggesting that the peptide can effectively fold-back into the binding site only in the latter case. Using this latter construct, we obtained enough experimental restraints to calculate the structure of the eIF4G135-49-Pub1 RRM3 chimera (PDB: 6Z29), which shed light on the key elements required for molecular recognition (Figure 4B and Supplementary Figure S8).","type":"Results"}]},{"start":35,"end":49,"reference_id":"36213119","reference_source":"pmid","reference_html":"eIF4G1 N-terminal intrinsically disordered domain is a multi-docking station for RNA, Pab1, Pub1, and self-assembly. <i> Chaves-Arquero B, Martínez-Lumbreras S, Sibille N, Camero S, Bernadó P, Jiménez MÁ, Zorrilla S, Pérez-Cañadillas JM. </i> Front Mol Biosci, 2022","date":"2022-10-17T09:42:14.490Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6Z29"}],"region_id":"DP00082r014","sequence_construct":"GSGYTNYNNGSNYTQKKQTIGLPPQVNPQAVDHIIRSAPPRVTTAYIGNIPHFATEADLIPLFQNFGFILDFKHYPEKGCCFIKYDTHEQAAVCIVALANFPFQGRNLRTGWGKER","statement":[{"text":"The NMR spectrum of the eIF4G1 peptide fused to the C-terminus of Pub1 was similar to that of Pub1 RRM3 alone (Figure 4A right), whereas that of the N-terminally fused chimera differed significantly (Figure 4A, left), suggesting that the peptide can effectively fold-back into the binding site only in the latter case. Using this latter construct, we obtained enough experimental restraints to calculate the structure of the eIF4G135-49-Pub1 RRM3 chimera (PDB: 6Z29), which shed light on the key elements required for molecular recognition (Figure 4B and Supplementary Figure S8).","type":"Results"}]},{"start":135,"end":160,"reference_id":"36213119","reference_source":"pmid","reference_html":"eIF4G1 N-terminal intrinsically disordered domain is a multi-docking station for RNA, Pab1, Pub1, and self-assembly. <i> Chaves-Arquero B, Martínez-Lumbreras S, Sibille N, Camero S, Bernadó P, Jiménez MÁ, Zorrilla S, Pérez-Cañadillas JM. </i> Front Mol Biosci, 2022","date":"2022-10-17T09:58:21.259Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P04147","operator":null,"partner_start":1,"partner_end":215}],"region_id":"DP00082r015","statement":[{"text":"We next studied the interaction between eIF4G1 and Pab1 using similar approaches. NMR titrations of unlabeled Pab1 RRM12 over 15N-eIF4G11-249 (blue bar chart in Figure 3A) caused similar pattern of perturbations and signal disappearance than Pub1 RRM3 but with additional changes in BOX2 (aa 135–160) and BOX3 (aa 200–234).","type":"Results"},{"text":"The BOX2 peptide also interacted with RRM2 through a similar interface; but probably weakly because it causes fewer changes than the BOX3 peptide. ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":200,"end":234,"reference_id":"36213119","reference_source":"pmid","reference_html":"eIF4G1 N-terminal intrinsically disordered domain is a multi-docking station for RNA, Pab1, Pub1, and self-assembly. <i> Chaves-Arquero B, Martínez-Lumbreras S, Sibille N, Camero S, Bernadó P, Jiménez MÁ, Zorrilla S, Pérez-Cañadillas JM. </i> Front Mol Biosci, 2022","date":"2022-10-17T09:58:48.971Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P04147","operator":null,"partner_start":1,"partner_end":215}],"region_id":"DP00082r016","statement":[{"text":"We next studied the interaction between eIF4G1 and Pab1 using similar approaches. NMR titrations of unlabeled Pab1 RRM12 over 15N-eIF4G11-249 (blue bar chart in Figure 3A) caused similar pattern of perturbations and signal disappearance than Pub1 RRM3 but with additional changes in BOX2 (aa 135–160) and BOX3 (aa 200–234).","type":"Results"},{"text":"As expected, the BOX3 peptide interacted with Pab1 RRM12 causing significant perturbations in the helix1-helix2 interface of RRM2 (Figure 3C right), an equivalent region to that involved in human eIF4G-PABP1 recognition (Safaee et al., 2012).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":243,"reference_id":"36213119","reference_source":"pmid","reference_html":"eIF4G1 N-terminal intrinsically disordered domain is a multi-docking station for RNA, Pab1, Pub1, and self-assembly. <i> Chaves-Arquero B, Martínez-Lumbreras S, Sibille N, Camero S, Bernadó P, Jiménez MÁ, Zorrilla S, Pérez-Cañadillas JM. </i> Front Mol Biosci, 2022","date":"2022-10-17T10:31:38.539Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P32588","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P04147","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP00082r018","statement":[{"text":"Dynamic light scattering (DLS) indicated that large aggregates were formed in some protein combinations (Figure 6A). In contrast, the individual proteins exhibited autocorrelation functions that did not differ from that of Ficoll-70 alone, suggesting that the individual proteins did not aggregate. Moreover, the curve profiles of the single proteins remained stable for several hours. The Pab1:Pub1 mixture (Figure 6, row 2, column 1) showed the same behavior, but other double protein mixtures and the triple one showed a second phase, evidencing the presence of micrometer-size particles. ","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false},{"start":93,"end":114,"reference_id":"36213119","reference_source":"pmid","reference_html":"eIF4G1 N-terminal intrinsically disordered domain is a multi-docking station for RNA, Pab1, Pub1, and self-assembly. <i> Chaves-Arquero B, Martínez-Lumbreras S, Sibille N, Camero S, Bernadó P, Jiménez MÁ, Zorrilla S, Pérez-Cañadillas JM. </i> Front Mol Biosci, 2022","date":"2022-10-17T10:32:03.829Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P32588","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P04147","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP00082r019","statement":[{"text":"Dynamic light scattering (DLS) indicated that large aggregates were formed in some protein combinations (Figure 6A). In contrast, the individual proteins exhibited autocorrelation functions that did not differ from that of Ficoll-70 alone, suggesting that the individual proteins did not aggregate. Moreover, the curve profiles of the single proteins remained stable for several hours. The Pab1:Pub1 mixture (Figure 6, row 2, column 1) showed the same behavior, but other double protein mixtures and the triple one showed a second phase, evidencing the presence of micrometer-size particles. ","type":"Results"},{"text":"Consistent with this using the eIF4G1 ΔBOX1 mutant in the triple mixture showed no aggregation (Figure 6, row 3, column 2).","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":243,"reference_id":"36213119","reference_source":"pmid","reference_html":"eIF4G1 N-terminal intrinsically disordered domain is a multi-docking station for RNA, Pab1, Pub1, and self-assembly. <i> Chaves-Arquero B, Martínez-Lumbreras S, Sibille N, Camero S, Bernadó P, Jiménez MÁ, Zorrilla S, Pérez-Cañadillas JM. </i> Front Mol Biosci, 2022","date":"2022-10-17T10:33:38.205Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007060","ec_ontology":"ECO","ec_name":"confocal laser scanning microscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P32588","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P04147","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP00082r020","statement":[{"text":"Confocal fluorescence microscopy images of triple mixtures containing Pab1 RRM12, Pub1 RRM123 and Alexa 488 labelled eIF4G11-249 in Ficoll 70 (200 g/L) revealed the presence of discrete rounded particles (∼1 µm and smaller, Figure 6B upper panels). Both, Pab1 and Pub1 were observed to colocalize with eIF4G1 in these assemblies, as observed in fluorescent images in which the proteins were pairwise labelled with spectrally different dyes (Alexa 488 and Alexa 647, Figure 6B middle and lower panels). ","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":82,"reference_id":"36213119","reference_source":"pmid","reference_html":"eIF4G1 N-terminal intrinsically disordered domain is a multi-docking station for RNA, Pab1, Pub1, and self-assembly. <i> Chaves-Arquero B, Martínez-Lumbreras S, Sibille N, Camero S, Bernadó P, Jiménez MÁ, Zorrilla S, Pérez-Cañadillas JM. </i> Front Mol Biosci, 2022","date":"2022-10-17T10:35:53.549Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","region_id":"DP00082r021","statement":[{"text":"We titrate the eIF4G11-82 construct with three poly (A) probes and found that the strength of the interaction is higher with longer oligos (Figure 7A). The chemical shift changes almost doubled when going from A12 to A14 and a new signal appears in the spectra that corresponds to the side chain Arg guanidinium group (Nε-Hε) (Figure 7B).","type":"Results"},{"text":"The interaction with poly(A) maps three regions centered around R34, R55, and G65, peaking at R55PH57. In contrast, the canonical RGG box (R60GG), a well-known RNA binding motif (Thandapani et al., 2013; Chong et al., 2018; Chowdhury and Jin, 2022), is less affected by binding.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":82,"reference_id":"12810920","reference_source":"pmid","reference_html":"RNA-binding activity of translation initiation factor eIF4G1 from Saccharomyces cerevisiae. <i> Berset C, Zurbriggen A, Djafarzadeh S, Altmann M, Trachsel H. </i> RNA, 2003","date":"2022-10-17T10:43:20.781Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001181","ec_ontology":"ECO","ec_name":"filter binding assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","region_id":"DP00082r022","statement":[{"text":"Typical titration curves for three of the proteins are shown in Figure 1C​1C.. We cleaved the GST moiety from the fusion proteins for these experiments; however, control experiments showed that GST fusion proteins behave identically in RNA-binding experiments. Full-length eIF4G11–952 showed the highest affinity for RNA with an estimated KD (KDapprox.) of 5 × 10−8 M whereas the fragments eIF4G11–82, eIF4G1492–539, and eIF4G1883–952 show about 100-fold lower affinity.","type":"Results"},{"text":"The fragments eIF4G1160–492, eIF4G1542–883 (not shown), and eIF4G1592–862, as well as GST (used as negative control) did not bind significant amounts of RNA.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":82,"reference_id":"12810920","reference_source":"pmid","reference_html":"RNA-binding activity of translation initiation factor eIF4G1 from Saccharomyces cerevisiae. <i> Berset C, Zurbriggen A, Djafarzadeh S, Altmann M, Trachsel H. </i> RNA, 2003","date":"2022-10-17T10:46:24.212Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006321","ec_ontology":"ECO","ec_name":"RNA-protein binding evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","region_id":"DP00082r023","statement":[{"text":"We tested full-length eIF4G11–952 and the fragments eIF4G11–82, eIF4G1492–539, and eIF4G1883–952 carrying RNA-binding sites as determined by filter-binding assays. ","type":"Results"},{"text":"We conclude from these results that eIF4G1 contains at least three sites, amino acids 1–82, 492–539, and 883–952, able to interact with RNA.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_P39935","date":"2016-08-23T14:40:53.000Z","acc":"P39935","name":"Eukaryotic initiation factor 4F subunit p150","length":952,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000168E90","genes":[{"name":{"value":"TIF4631","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8336723","url":"http://www.ncbi.nlm.nih.gov/pubmed/8336723","alternativeUrl":"https://europepmc.org/abstract/MED/8336723"}}]},"olnNames":[{"value":"YGR162W"}]}],"alphafold_very_low_content":0.4632352941176471,"disorder_content":0.3644957983193277,"disprot_consensus":{"full":[{"start":1,"end":34,"type":"D"},{"start":35,"end":49,"type":"T"},{"start":50,"end":249,"type":"D"},{"start":393,"end":490,"type":"T"}],"Structural state":[{"start":1,"end":249,"type":"D"},{"start":393,"end":490,"type":"D"}],"Structural transition":[{"start":35,"end":49,"type":"T"},{"start":393,"end":490,"type":"T"}],"Molecular function":[{"start":1,"end":243,"type":"F"},{"start":393,"end":490,"type":"F"}]}},{"features":{"pfam":[{"id":"PF07716","name":"Basic region leucine zipper","start":225,"end":276}],"gene3D":[{"start":220,"end":281,"id":"3.30.160.60","name":"Classic Zinc Finger"}]},"uniref50":"UniRef50_P03069","sequence":"MSEYQPSLFALNPMGFSPLDGSKSTNENVSASTSTAKPMVGQLIFDKFIKTEEDPIIKQDTPSNLDFDFALPQTATAPDAKTVLPIPELDDAVVESFFSSSTDSTPMFEYENLEDNSKEWTSLFDNDIPVTTDDVSLADKAIESTEEVSLVPSNLEVSTTSFLPTPVLEDAKLTQTRKVKKPNSVVKKSHHVGKDDESRLDHLGVVAYNRKQRSIPLSPIVPESSDPAALKRARNTEAARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVGER","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P03069","disprot_id":"DP00083","ncbi_taxon_id":559292,"regions_counter":16,"creator":"ftonello","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":134,"region_id":"DP00083r009","released":"2023_06","ec_id":"ECO:0006165","reference_html":"The acidic transcription activator Gcn4 binds the mediator subunit Gal11/Med15 using a simple protein interface forming a fuzzy complex. <i> Brzovic PS, Heikaus CC, Kisselev L, Vernon R, Herbig E, Pacheco D, Warfield L, Littlefield P, Baker D, Klevit RE, Hahn S. </i> Mol Cell, 2011","term_id":"IDPO:0000002","curator_id":"vnugnes","start":101,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"22195967","version":4,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-01-16T13:59:32.377Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The 1H,15N-HSQC spectra of each individual AD (Gcn4 1–100 and 101–134) overlay almost perfectly with the spectrum of a construct containing both ADs (residues 1–134), indicating that the two regions are structurally independent (Fig S1A). In all three spectra, the dispersion of resonances is over a narrow range in the 1HN-dimension, indicating that both Gcn4 ADs are intrinsically disordered in the absence of binding partners.","type":"Results"},{"text":"Backbone resonance chemical shifts, particularly 1Hα, 13Cα, and 13Cβ shifts, depend on local backbone geometry and provide a means to identify regions of regular secondary structure (Wishart et al., 1991). No patterns could be discerned from the cAD chemical shifts, consistent with a lack of ordered secondary structure.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:21:15.028Z"}},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":127,"term_name":"disorder to order","start":117,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"22195967","version":3,"reference_html":"The acidic transcription activator Gcn4 binds the mediator subunit Gal11/Med15 using a simple protein interface forming a fuzzy complex. <i> Brzovic PS, Heikaus CC, Kisselev L, Vernon R, Herbig E, Pacheco D, Warfield L, Littlefield P, Baker D, Klevit RE, Hahn S. </i> Mol Cell, 2011","date":"2023-01-16T14:26:56.014Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00083r011","ec_go":"EXP","disprot_namespace":"Structural transition","cross_refs":[{"db":"PDB","id":"2LPB"}],"curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P19659"}],"statement":[{"text":"In all three spectra, the dispersion of resonances is over a narrow range in the 1HN-dimension, indicating that both Gcn4 ADs are intrinsically disordered in the absence of binding partners.","type":"Results"},{"text":"Comparison of Gcn4 backbone resonances (1HN, 15N, 13Cα, 13Cβ, and 13C’) in the free and bound states indicates that the cAD adopts an α-helical conformation for binding to ABD1.","type":"Results"},{"text":"13C’ and 1Hα chemical shift values also indicate stabilization of helical structure upon binding: 13C’ resonances of residues 115–122 shift downfield upon addition of Gal11 (Fig S1C) and 1Hα resonances of residues 117–127 resonate upfield when compared to random coil values (Fig S1D; the 1Hα-chemical shifts for free Gcn4-cAD were not assigned).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:35:23.885Z"}},{"start":1,"end":100,"reference_id":"22195967","reference_source":"pmid","reference_html":"The acidic transcription activator Gcn4 binds the mediator subunit Gal11/Med15 using a simple protein interface forming a fuzzy complex. <i> Brzovic PS, Heikaus CC, Kisselev L, Vernon R, Herbig E, Pacheco D, Warfield L, Littlefield P, Baker D, Klevit RE, Hahn S. </i> Mol Cell, 2011","date":"2023-01-16T13:58:25.577Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00083r013","statement":[{"text":"The 1H,15N-HSQC spectra of each individual AD (Gcn4 1–100 and 101–134) overlay almost perfectly with the spectrum of a construct containing both ADs (residues 1–134), indicating that the two regions are structurally independent (Fig S1A). In all three spectra, the dispersion of resonances is over a narrow range in the 1HN-dimension, indicating that both Gcn4 ADs are intrinsically disordered in the absence of binding partners.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:35:20.907Z"}},{"start":101,"end":134,"reference_id":"22195967","reference_source":"pmid","reference_html":"The acidic transcription activator Gcn4 binds the mediator subunit Gal11/Med15 using a simple protein interface forming a fuzzy complex. <i> Brzovic PS, Heikaus CC, Kisselev L, Vernon R, Herbig E, Pacheco D, Warfield L, Littlefield P, Baker D, Klevit RE, Hahn S. </i> Mol Cell, 2011","date":"2023-01-16T14:31:13.274Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0036033","term_name":"mediator complex binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2LPB"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P19659","operator":null,"partner_start":158,"partner_end":238},{"db":"UniProt","id":"P19659","operator":"and","partner_start":496,"partner_end":651}],"region_id":"DP00083r014","statement":[{"text":"Several cAD backbone amide resonances are strongly perturbed upon addition of ABD1. At the endpoint of the NMR titration (three-fold molar excess of ABD1), perturbations of up to 1.0 ppm are observed for residues 121–125 (Fig 1C). Importantly, similar shifts were observed in the spectrum of the tandem Gcn4-ADs when Gcn4 1–134 was titrated with ABD1, suggesting that the mode and affinity of interaction between the cAD and ABD1 is conserved in the context of the tandem Gcn4 ADs (Fig S1B).","type":"Results"},{"text":"cAD chemical shift perturbations observed upon addition of unlabeled Taf12 or ABD3 are remarkably similar to those seen with ABD1 (Fig 1B).","type":"Results"},{"text":"ABD1 corresponds to Gal11 residues 158-238 and ADB3 corresponds to Gal11 residues 496–651.  ","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a mediator complex. The mediator complex is a protein complex that interacts with the carboxy-terminal domain of the largest subunit of RNA polymerase II and plays an active role in transducing the signal from a transcription factor to the transcriptional machinery. The Saccharomyces complex contains several identifiable subcomplexes: a head domain comprising Srb2, -4, and -5, Med6, -8, and -11, and Rox3 proteins; a middle domain comprising Med1, -4, and -7, Nut1 and -2, Cse2, Rgr1, Soh1, and Srb7 proteins; a tail consisting of Gal11p, Med2p, Pgd1p, and Sin4p; and a regulatory subcomplex comprising Ssn2, -3, and -8, and Srb8 proteins. Metazoan mediator complexes have similar modular structures and include homologs of yeast Srb and Med proteins.\" [GOC:yaf, PMID:18391015]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:35:25.896Z"}},{"start":101,"end":134,"reference_id":"22195967","reference_source":"pmid","reference_html":"The acidic transcription activator Gcn4 binds the mediator subunit Gal11/Med15 using a simple protein interface forming a fuzzy complex. <i> Brzovic PS, Heikaus CC, Kisselev L, Vernon R, Herbig E, Pacheco D, Warfield L, Littlefield P, Baker D, Klevit RE, Hahn S. </i> Mol Cell, 2011","date":"2023-01-16T14:39:59.974Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0001094","term_name":"TFIID-class transcription factor complex binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q03761","operator":null,"partner_start":29,"partner_end":259}],"region_id":"DP00083r015","statement":[{"text":"cAD chemical shift perturbations observed upon addition of unlabeled Taf12 or ABD3 are remarkably similar to those seen with ABD1 (Fig 1B). The same Gcn4 residues undergo the largest backbone amide perturbations in each case, though the absolute magnitudes of resonance perturbations are smaller compared to Gcn4 binding to Gal11-ABD1 (compare Figs. 1C and S5).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a general RNA polymerase II transcription factor belonging to the TFIID complex, one of the factors involved in formation of the preinitiation complex (PIC) by RNA polymerase II.\" [GOC:krc, PMID:16858867]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:35:27.773Z"}},{"start":101,"end":134,"reference_id":"22195967","reference_source":"pmid","reference_html":"The acidic transcription activator Gcn4 binds the mediator subunit Gal11/Med15 using a simple protein interface forming a fuzzy complex. <i> Brzovic PS, Heikaus CC, Kisselev L, Vernon R, Herbig E, Pacheco D, Warfield L, Littlefield P, Baker D, Klevit RE, Hahn S. </i> Mol Cell, 2011","date":"2023-01-16T14:40:22.438Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0036033","term_name":"mediator complex binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P19659","operator":null,"partner_start":158,"partner_end":238}],"region_id":"DP00083r016","statement":[{"text":"Binding affinities were measured using isothermal titration calorimetry (Table 2, Fig S3A–E). Wild-type cAD binds ABD1 with a Kd of 10.1 µM, similar to values measured using fluorescence polarization (Herbig et al., 2010).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a mediator complex. The mediator complex is a protein complex that interacts with the carboxy-terminal domain of the largest subunit of RNA polymerase II and plays an active role in transducing the signal from a transcription factor to the transcriptional machinery. The Saccharomyces complex contains several identifiable subcomplexes: a head domain comprising Srb2, -4, and -5, Med6, -8, and -11, and Rox3 proteins; a middle domain comprising Med1, -4, and -7, Nut1 and -2, Cse2, Rgr1, Soh1, and Srb7 proteins; a tail consisting of Gal11p, Med2p, Pgd1p, and Sin4p; and a regulatory subcomplex comprising Ssn2, -3, and -8, and Srb8 proteins. Metazoan mediator complexes have similar modular structures and include homologs of yeast Srb and Med proteins.\" [GOC:yaf, PMID:18391015]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:35:28.488Z"}}],"released":"2016_10","uniref100":"UniRef100_P03069","date":"2016-09-05T17:03:54.000Z","acc":"P03069","name":"General control protein GCN4","length":281,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":["Condensates-related proteins"],"UniParc":"UPI0000047601","genes":[{"name":{"value":"GCN4","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"6387704","url":"http://www.ncbi.nlm.nih.gov/pubmed/6387704","alternativeUrl":"https://europepmc.org/abstract/MED/6387704"}},{"code":"ECO:0000312","source":{"name":"SGD","id":"S000000735","url":"https://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000000735"}}]},"synonyms":[{"value":"AAS101","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"6433345","url":"http://www.ncbi.nlm.nih.gov/pubmed/6433345","alternativeUrl":"https://europepmc.org/abstract/MED/6433345"}},{"code":"ECO:0000312","source":{"name":"SGD","id":"S000000735","url":"https://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000000735"}}]},{"value":"AAS3","evidences":[{"code":"ECO:0000312","source":{"name":"SGD","id":"S000000735","url":"https://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000000735"}}]},{"value":"ARG9","evidences":[{"code":"ECO:0000312","source":{"name":"SGD","id":"S000000735","url":"https://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000000735"}}]}],"olnNames":[{"value":"YEL009C"}]}],"alphafold_very_low_content":0.2313167259786477,"disorder_content":0.47686832740213525,"disprot_consensus":{"full":[{"start":1,"end":116,"type":"D"},{"start":117,"end":127,"type":"T"},{"start":128,"end":134,"type":"D"}],"Structural state":[{"start":1,"end":134,"type":"D"}],"Structural transition":[{"start":117,"end":127,"type":"T"}],"Molecular function":[{"start":101,"end":134,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00010","name":"Helix-loop-helix DNA-binding domain","start":24,"end":74}],"gene3D":[{"start":24,"end":102,"id":"4.10.280.10","name":"Helix-loop-helix DNA-binding domain"}]},"uniref50":"UniRef50_P61244","sequence":"MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P61244","disprot_id":"DP00084","ncbi_taxon_id":9606,"regions_counter":20,"creator":"zskalman","regions":[{"start":1,"end":14,"reference_id":"15342239","reference_source":"pmid","reference_html":"The NMR solution structure of a mutant of the Max b/HLH/LZ free of DNA: insights into the specific and reversible DNA binding mechanism of dimeric transcription factors. <i> Sauvé S, Tremblay L, Lavigne P. </i> J Mol Biol, 2004","date":"2023-01-16T16:02:10.231Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00084r007","statement":[{"text":"This is consistent with the existence of a predominantly unfolded basic region from residues 1–14 with a persistent helical turn from 15 to 18 and contiguous with H1.","type":"Results"},{"text":"As discussed in the text, almost no NOEs were observed in the first 14 residues due to an apparent and mainly unfolded nature and fast HN exchange rate near neutral pH.","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:35:52.397Z"}},{"start":1,"end":21,"reference_id":"36174765","reference_source":"pmid","reference_html":"The Disordered MAX N-terminus Modulates DNA Binding of the Transcription Factor MYC:MAX. <i> Schütz S, Bergsdorf C, Goretzki B, Lingel A, Renatus M, Gossert AD, Jahnke W. </i> J Mol Biol, 2022","date":"2024-11-18T10:43:24.153Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"51505"}],"region_id":"DP00084r008","statement":[{"text":"Different phosphorylation sites have been identified in the C-terminal region (residues 103–160) and in the shorter disordered N-terminus (residues 2–21), which are both enriched in acidic residues and serines.","type":"Introduction"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-03T15:21:40.545Z"}},{"start":1,"end":21,"reference_id":"36174765","reference_source":"pmid","reference_html":"The Disordered MAX N-terminus Modulates DNA Binding of the Transcription Factor MYC:MAX. <i> Schütz S, Bergsdorf C, Goretzki B, Lingel A, Renatus M, Gossert AD, Jahnke W. </i> J Mol Biol, 2022","date":"2024-11-18T10:52:24.360Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006285","ec_ontology":"ECO","ec_name":"magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P01106","operator":null,"partner_start":369,"partner_end":452},{"db":"UniProt","id":"P61244","operator":"and","partner_start":24,"partner_end":102}],"region_id":"DP00084r009","statement":[{"text":"Based on the observed chemical shift perturbations (CSPs), we conclude that the N- and C-terminal MAX regions bind to the MYC:MAX DBD.","type":"Results"},{"text":"Intrinsically disordered MAX regions interact with the MYC:MAX DBD.","type":"Figure"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-03T16:34:55.492Z"}},{"start":103,"end":160,"reference_id":"36174765","reference_source":"pmid","reference_html":"The Disordered MAX N-terminus Modulates DNA Binding of the Transcription Factor MYC:MAX. <i> Schütz S, Bergsdorf C, Goretzki B, Lingel A, Renatus M, Gossert AD, Jahnke W. </i> J Mol Biol, 2022","date":"2025-02-03T15:21:28.731Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00084r010","statement":[{"text":"MAX contains two highly negatively charged disordered regions in its N- and C-terminus.","type":"Results"}]},{"start":103,"end":160,"reference_id":"36174765","reference_source":"pmid","reference_html":"The Disordered MAX N-terminus Modulates DNA Binding of the Transcription Factor MYC:MAX. <i> Schütz S, Bergsdorf C, Goretzki B, Lingel A, Renatus M, Gossert AD, Jahnke W. </i> J Mol Biol, 2022","date":"2025-02-03T18:15:56.270Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P01106","operator":null,"partner_start":369,"partner_end":452},{"db":"UniProt","id":"P61244","operator":"and","partner_start":24,"partner_end":102}],"region_id":"DP00084r011","statement":[{"text":"Based on the observed chemical shift perturbations (CSPs), we conclude that the N- and C-terminal MAX regions bind to the MYC:MAX DBD.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":103,"end":160,"reference_id":"36174765","reference_source":"pmid","reference_html":"The Disordered MAX N-terminus Modulates DNA Binding of the Transcription Factor MYC:MAX. <i> Schütz S, Bergsdorf C, Goretzki B, Lingel A, Renatus M, Gossert AD, Jahnke W. </i> J Mol Biol, 2022","date":"2025-02-03T18:16:05.983Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0071943","term_name":"Myc-Max complex","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP00084r012","statement":[{"text":"Based on the observed chemical shift perturbations (CSPs), we conclude that the N- and C-terminal MAX regions bind to the MYC:MAX DBD.","type":"Results"}],"term_comment":"","term_def":"\"A transcription factor complex that consists of a heterodimer of the bHLH-ZIP proteins Myc and Max.\" [GOC:cna, PMID:16620027, PMID:16620031, PMID:20170194]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":21,"reference_id":"36174765","reference_source":"pmid","reference_html":"The Disordered MAX N-terminus Modulates DNA Binding of the Transcription Factor MYC:MAX. <i> Schütz S, Bergsdorf C, Goretzki B, Lingel A, Renatus M, Gossert AD, Jahnke W. </i> J Mol Biol, 2022","date":"2025-02-03T15:28:48.048Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0071943","term_name":"Myc-Max complex","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP00084r013","statement":[{"text":"Based on the observed chemical shift perturbations (CSPs), we conclude that the N- and C-terminal MAX regions bind to the MYC:MAX DBD.","type":"Results"}],"term_comment":"","term_def":"\"A transcription factor complex that consists of a heterodimer of the bHLH-ZIP proteins Myc and Max.\" [GOC:cna, PMID:16620027, PMID:16620031, PMID:20170194]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":5,"reference_id":"36174765","reference_source":"pmid","reference_html":"The Disordered MAX N-terminus Modulates DNA Binding of the Transcription Factor MYC:MAX. <i> Schütz S, Bergsdorf C, Goretzki B, Lingel A, Renatus M, Gossert AD, Jahnke W. </i> J Mol Biol, 2022","date":"2025-02-03T16:10:49.072Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007687","ec_ontology":"ECO","ec_name":"protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00084r014","statement":[{"text":"We were able to obtain near quantitative phosphorylation of S2 and S11 within MAX(2–103) and could separate the double phosphorylated protein from minor fractions of mono- or unphosphorylated protein with anion-exchange chromatography.","type":"Results"}]},{"start":9,"end":13,"reference_id":"36174765","reference_source":"pmid","reference_html":"The Disordered MAX N-terminus Modulates DNA Binding of the Transcription Factor MYC:MAX. <i> Schütz S, Bergsdorf C, Goretzki B, Lingel A, Renatus M, Gossert AD, Jahnke W. </i> J Mol Biol, 2022","date":"2025-02-03T16:10:56.037Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007687","ec_ontology":"ECO","ec_name":"protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00084r015","statement":[{"text":"We were able to obtain near quantitative phosphorylation of S2 and S11 within MAX(2–103) and could separate the double phosphorylated protein from minor fractions of mono- or unphosphorylated protein with anion-exchange chromatography.","type":"Results"}]},{"start":1,"end":21,"reference_id":"36174765","reference_source":"pmid","reference_html":"The Disordered MAX N-terminus Modulates DNA Binding of the Transcription Factor MYC:MAX. <i> Schütz S, Bergsdorf C, Goretzki B, Lingel A, Renatus M, Gossert AD, Jahnke W. </i> J Mol Biol, 2022","date":"2025-02-03T16:20:57.443Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000057","term_name":"self-regulatory activity","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00084r016","statement":[{"text":"Firstly, the MAX N-terminus confers specificity toward high-affinity DNA binding sites, i.e. E-Box DNA. For MAX(2–160) homodimers, the difference in affinity between E-Box and non-E-Box DNA that we observe is about 50-fold (see Table 2, last column). Contrarily, MAX(22–160) homodimers lacking the N-terminus show only a small change of 3- to 4-fold.","type":"Discussion"}]},{"start":1,"end":21,"reference_id":"36174765","reference_source":"pmid","reference_html":"The Disordered MAX N-terminus Modulates DNA Binding of the Transcription Factor MYC:MAX. <i> Schütz S, Bergsdorf C, Goretzki B, Lingel A, Renatus M, Gossert AD, Jahnke W. </i> J Mol Biol, 2022","date":"2025-02-03T16:34:35.096Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051101","term_name":"regulation of DNA binding","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","region_id":"DP00084r017","statement":[{"text":"Firstly, the MAX N-terminus confers specificity toward high-affinity DNA binding sites, i.e. E-Box DNA. For MAX(2–160) homodimers, the difference in affinity between E-Box and non-E-Box DNA that we observe is about 50-fold (see Table 2, last column). Contrarily, MAX(22–160) homodimers lacking the N-terminus show only a small change of 3- to 4-fold.","type":"Discussion"},{"text":"Taken together, our data suggests that direct binding of the MAX N-terminus to the MYC:MAX or MAX:MAX DBDs modulates DNA binding behavior.","type":"Results"},{"text":"Once bound to the target E-Box sequence, the MAX N-terminus competes for binding to the DBD, which ultimately leads to dissociation of MYC:MAX from the DNA.","type":"Discussion"},{"text":"The MAX N-terminus confers specificity for E-Box DNA and accelerates binding kinetics","type":"Discussion"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of DNA binding. DNA binding is any process in which a gene product interacts selectively with DNA (deoxyribonucleic acid).\" [GOC:ai, GOC:dph, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":21,"reference_id":"36174765","reference_source":"pmid","reference_html":"The Disordered MAX N-terminus Modulates DNA Binding of the Transcription Factor MYC:MAX. <i> Schütz S, Bergsdorf C, Goretzki B, Lingel A, Renatus M, Gossert AD, Jahnke W. </i> J Mol Biol, 2022","date":"2025-02-03T18:17:04.323Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"51505"}],"region_id":"DP00084r018","statement":[{"text":"MAX contains two highly negatively charged disordered regions in its N- and C-terminus.","type":"Results"}]},{"start":103,"end":160,"reference_id":"36174765","reference_source":"pmid","reference_html":"The Disordered MAX N-terminus Modulates DNA Binding of the Transcription Factor MYC:MAX. <i> Schütz S, Bergsdorf C, Goretzki B, Lingel A, Renatus M, Gossert AD, Jahnke W. </i> J Mol Biol, 2022","date":"2025-02-03T18:17:19.227Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00084r019","statement":[{"text":"MAX contains two highly negatively charged disordered regions in its N- and C-terminus.","type":"Results"}]},{"start":1,"end":21,"reference_id":"36174765","reference_source":"pmid","reference_html":"The Disordered MAX N-terminus Modulates DNA Binding of the Transcription Factor MYC:MAX. <i> Schütz S, Bergsdorf C, Goretzki B, Lingel A, Renatus M, Gossert AD, Jahnke W. </i> J Mol Biol, 2022","date":"2025-02-03T18:24:41.038Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00084r020","statement":[{"text":"Notably, the observed CSPs for MAX(1–21) in presence of MYC:MAX DBD are larger than those obtained with MAX:MAX DBD (Suppl. Figure 1A), suggesting a lower affinity for the latter interaction.","type":"Results"},{"text":"Indeed, we find that binding of the MAX:MAX DBD to MAX(1–21) is ionic strength-dependent: we observe pronounced CSPs in buffer with 150 mM NaCl, while the CSPs are even larger at 100 mM NaCl but completely abolished at 300 mM NaCl (Suppl. Figure 2). These results further support electrostatic interactions between the MAX N-terminus and the DBD as the main driving force for binding.","type":"Results"},{"text":"We were able to show that the acidic, disordered MAX N-terminus interacts with the basic, folded DNA binding domain which is formed by dimerization of the MYC and MAX bHLH-LZ motifs, and that this interaction is competitive with DNA binding.","type":"Discussion"}]}],"released":"2016_10","uniref100":"UniRef100_P61244","date":"2016-09-20T11:29:42.000Z","acc":"P61244","name":"Protein max","length":160,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI0000000C63","genes":[{"name":{"value":"MAX","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6913","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6913"}}]},"synonyms":[{"value":"BHLHD4"}]}],"alphafold_very_low_content":0.0125,"disorder_content":0.49375,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"},{"start":103,"end":160,"type":"D"}],"Structural state":[{"start":1,"end":21,"type":"D"},{"start":103,"end":160,"type":"D"}],"Molecular function":[{"start":1,"end":21,"type":"F"},{"start":103,"end":160,"type":"F"}],"Cellular component":[{"start":1,"end":21,"type":"F"},{"start":103,"end":160,"type":"F"}],"Disorder function":[{"start":1,"end":21,"type":"F"},{"start":103,"end":160,"type":"F"}],"Biological process":[{"start":1,"end":21,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00554","name":"Rel homology DNA-binding domain","start":21,"end":186},{"id":"PF16179","name":"Rel homology dimerisation domain","start":195,"end":291}],"gene3D":[{"start":9,"end":187,"id":"2.60.40.340","name":"Rel homology domain (RHD), DNA-binding domain"},{"start":191,"end":304,"id":"2.60.40.10","name":"Immunoglobulins"}]},"uniref50":"UniRef50_Q04206","sequence":"MDELFPLIFPAEPAQASGPYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGFYEAELCPDRCIHSFQNLGIQCVKKRDLEQAISQRIQTNNNPFQVPIEEQRGDYDLNAVRLCFQVTVRDPSGRPLRLPPVLSHPIFDNRAPNTAELKICRVNRNSGSCLGGDEIFLLCDKVQKEDIEVYFTGPGWEARGSFSQADVHRQVAIVFRTPPYADPSLQAPVRVSMQLRRPSDRELSEPMEFQYLPDTDDRHRIEEKRKRTYETFKSIMKKSPFSGPTDPRPPPRRIAVPSRSSASVPKPAPQPYPFTSSLSTINYDEFPTMVFPSGQISQASALAPAPPQVLPQAPAPAPAPAMVSALAQAPAPVPVLAPGPPQAVAPPAPKPTQAGEGTLSEALLQLQFDDEDLGALLGNSTDPAVFTDLASVDNSEFQQLLNQGIPVAPHTTEPMLMEYPEAITRLVTGAQRPPDPAPAPLGAPGLPNGLLSGDEDFSSIADMDFSALLSQISS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q04206","disprot_id":"DP00085","ncbi_taxon_id":9606,"regions_counter":4,"creator":"dpiovesan","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":551,"region_id":"DP00085r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural and functional analysis of the NF-kappa B p65 C terminus. An acidic and modular transactivation domain with the potential to adopt an alpha-helical conformation. <i> Schmitz ML, dos Santos Silva MA, Altmann H, Czisch M, Holak TA, Baeuerle PA. </i> J Biol Chem, 1994","term_id":"IDPO:0000002","curator_id":"esalladini","start":428,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"7929265","statement":[{"text":"The NOE pattern was typical for a random conformation; furthermore, the weakness of the NOEs indicates a large inherent flexibility of the unstructured p65 C terminus. ","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-13T18:55:33.311Z"}},{"start":428,"end":551,"reference_id":"7929265","reference_source":"pmid","reference_html":"Structural and functional analysis of the NF-kappa B p65 C terminus. An acidic and modular transactivation domain with the potential to adopt an alpha-helical conformation. <i> Schmitz ML, dos Santos Silva MA, Altmann H, Czisch M, Holak TA, Baeuerle PA. </i> J Biol Chem, 1994","date":"2022-02-21T15:42:33.735Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":0,"region_id":"DP00085r004","statement":[{"text":"The results of the CD analysis are shown in Fig. 2A. The negative e value at a wavelength of 190 nm and the 0 value near 0 at wavelengths exceeding 210 nm is indicative for a random conformation of the TA, peptides in an aqueous buffer at pH 7.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-13T18:55:33.312Z"}}],"released":"2016_10","uniref100":"UniRef100_Q04206","date":"2016-08-18T16:15:46.000Z","acc":"Q04206","name":"Transcription factor p65","length":551,"organism":"Homo sapiens","dataset":["Autophagy-related proteins"],"UniParc":"UPI0000136C5A","genes":[{"name":{"value":"RELA"},"synonyms":[{"value":"NFKB3"}]}],"alphafold_very_low_content":0.33575317604355714,"disorder_content":0.2250453720508167,"disprot_consensus":{"full":[{"start":428,"end":551,"type":"D"}],"Structural state":[{"start":428,"end":551,"type":"D"}]}},{"acc":"P04637","sequence":"MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD","alphafold_very_low_content":"0.3104325699745547","creator":"tcordero","dataset":["Autophagy-related proteins","Cancer-related proteins","Condensates-related proteins","NDDs-related proteins"],"date":"2016-08-09T14:02:38.000Z","disprot_id":"DP00086","features":{"pfam":[{"id":"PF00870","name":"P53 DNA-binding domain","start":100,"end":288},{"id":"PF07710","name":"P53 tetramerisation motif","start":319,"end":357},{"id":"PF08563","name":"P53 transactivation motif","start":6,"end":30},{"id":"PF18521","name":"Transactivation domain 2","start":35,"end":59}],"gene3D":[{"start":94,"end":293,"id":"2.60.40.720","name":"2.60.40.720","_id":"685af523b4ac24d5329d747f"},{"start":319,"end":360,"id":"4.10.170.10","name":"p53-like tetramerisation domain","_id":"685af523b4ac24d5329d7480"}]},"genes":[{"name":{"value":"TP53","evidences":[],"_id":"685af523b4ac24d5329d764d"},"synonyms":[{"value":"P53","evidences":[],"_id":"685af523b4ac24d5329d764e"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d764c"}],"length":393,"name":"Cellular tumor antigen p53","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":93,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI000014AEB2","uniref100":"UniRef100_P04637","uniref50":"UniRef50_P04637","uniref90":"UniRef90_P04637","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2LY4","_id":"685af523b4ac24d5329d7493"},{"db":"BMRB","id":"18709","_id":"685af523b4ac24d5329d7494"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":12,"interaction_partner":[],"reference_html":"HMGB1-facilitated p53 DNA binding occurs via HMG-Box/p53 transactivation domain interaction, regulated by the acidic tail. <i> Rowell JP, Simpson KL, Stott K, Watson M, Thomas JO. </i> Structure, 2012","reference_id":"23063560","region_id":"DP00086r008","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"We show here that an essential element in the interaction of p53 with HMGB1 is the N-terminal disordered region (Lee et al., 2000; Dawson et al., 2003; Wells et al., 2008), comprising the transactivation domain and the proline-rich region, the major interacting motif being a region of inducible structure in TAD2 (Lee et al., 2000).","_id":"685af523b4ac24d5329d7495"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-12-07T13:49:26.410Z","_id":"685af523b4ac24d5329d7496"},"version":3,"_id":"685af523b4ac24d5329d7492","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":93,"interaction_partner":[],"reference_html":"Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain. <i> Wells M, Tidow H, Rutherford TJ, Markwick P, Jensen MR, Mylonas E, Svergun DI, Blackledge M, Fersht AR. </i> Proc Natl Acad Sci U S A, 2008","reference_id":"18391200","region_id":"DP00086r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"RDC analysis showed that the isolated domain p53(1–93) was an IDP with two regions of nascent secondary structure.","_id":"685af523b4ac24d5329d74a0"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2020-11-26T10:45:00.735Z","_id":"685af523b4ac24d5329d74a1"},"version":3,"_id":"685af523b4ac24d5329d749f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Human p53 core domain (residues 94–312) mutant M133L/V203A/N239Y/N268D was expressed and purified following published protocols (13., 15.). ","_id":"685af523b4ac24d5329d74ae"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met133Leu","_id":"685af523b4ac24d5329d74ad"},{"start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Human p53 core domain (residues 94–312) mutant M133L/V203A/N239Y/N268D was expressed and purified following published protocols (13., 15.). ","_id":"685af523b4ac24d5329d74b0"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val203Ala","_id":"685af523b4ac24d5329d74af"},{"start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Human p53 core domain (residues 94–312) mutant M133L/V203A/N239Y/N268D was expressed and purified following published protocols (13., 15.). ","_id":"685af523b4ac24d5329d74b2"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asn239Tyr","_id":"685af523b4ac24d5329d74b1"},{"start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Human p53 core domain (residues 94–312) mutant M133L/V203A/N239Y/N268D was expressed and purified following published protocols (13., 15.). ","_id":"685af523b4ac24d5329d74b4"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asn268Asp","_id":"685af523b4ac24d5329d74b3"}],"cross_refs":[{"db":"PDB","id":"1UOL","_id":"685af523b4ac24d5329d74ab"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-13T19:51:44.367Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":291,"end":312,"interaction_partner":[],"reference_html":"Crystal structure of a superstable mutant of human p53 core domain. Insights into the mechanism of rescuing oncogenic mutations. <i> Joerger AC, Allen MD, Fersht AR. </i> J Biol Chem, 2004","reference_id":"14534297","region_id":"DP00086r018","released":"2022_06","sample":[],"sequence_construct":"SSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKLFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRAEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCYSSCMGGMNRRPILTIITLEDSSGNLLGRDSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNT","statement":[{"type":"Results","text":"Our final model of the quadruple mutant comprises residues 96–290 for both molecules in the asymmetric unit. As in the structure of wild type, the C-terminal residues up to Thr-312 are disordered.","_id":"685af523b4ac24d5329d74ac"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-14T07:49:20.893Z","_id":"685af523b4ac24d5329d74b5"},"version":4,"_id":"685af523b4ac24d5329d74aa","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":93,"interaction_partner":[],"reference_html":"Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain. <i> Wells M, Tidow H, Rutherford TJ, Markwick P, Jensen MR, Mylonas E, Svergun DI, Blackledge M, Fersht AR. </i> Proc Natl Acad Sci U S A, 2008","reference_id":"18391200","region_id":"DP00086r024","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"SAXS data were accurately reproduced by intensity curves simulated from the ensemble of p53(1–93) conformers that reproduced the RDC data (shown in the form of a semilogarithmic and a Kratky-type plot in Fig. 2), demonstrating that the overall shape of the predicted and measured ensembles was consistent with the model of the unfolded chain described above. The SAXS profile was not consistent with a collapsed structure of the transactivation domain, reported from paramagnetic relaxation enhancement experiments (Fig. S7) (28).","_id":"685af523b4ac24d5329d74c6"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2020-11-26T10:46:15.884Z","_id":"685af523b4ac24d5329d74c7"},"version":3,"_id":"685af523b4ac24d5329d74c5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2GS0","_id":"685af523b4ac24d5329d74d2"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":20,"end":73,"interaction_partner":[{"db":"UniProt","id":"P32776","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d74d1"}],"reference_html":"Structure of the Tfb1/p53 complex: Insights into the interaction between the p62/Tfb1 subunit of TFIIH and the activation domain of p53. <i> Di Lello P, Jenkins LMM, Jones TN, Nguyen BD, Hara T, Yamaguchi H, Dikeakos JD, Appella E, Legault P, Omichinski JG. </i> Mol Cell, 2006","reference_id":"16793543","region_id":"DP00086r027","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"This short helix interacts with the surface of Tfb1 formed by beta strands b5, b6, and b7 and the loop connecting b5 to b6.","_id":"685af523b4ac24d5329d74d0"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-12-07T13:50:01.698Z","_id":"685af523b4ac24d5329d74d3"},"version":5,"_id":"685af523b4ac24d5329d74cf","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":20,"end":73,"interaction_partner":[],"reference_html":"Structure of the Tfb1/p53 complex: Insights into the interaction between the p62/Tfb1 subunit of TFIIH and the activation domain of p53. <i> Di Lello P, Jenkins LMM, Jones TN, Nguyen BD, Hara T, Yamaguchi H, Dikeakos JD, Appella E, Legault P, Omichinski JG. </i> Mol Cell, 2006","reference_id":"16793543","region_id":"DP00086r029","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"The interaction between the p62/Tfb1 subunit of TFIIH and the TAD of p53 has been shown to be important for the recruitment of p53 to the TFIIH complex in both human and yeast. This interaction is directly correlated with the ability of the p53 TAD to stimulate transcriptional elongation (Blau et al., 1996).","_id":"685af523b4ac24d5329d74d9"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_id":"GO:0140677","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-12-07T13:48:39.633Z","_id":"685af523b4ac24d5329d74da"},"version":4,"_id":"685af523b4ac24d5329d74d8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2B3G","_id":"685af523b4ac24d5329d74de"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":37,"end":57,"interaction_partner":[],"reference_html":"Single-stranded DNA mimicry in the p53 transactivation domain interaction with replication protein A. <i> Bochkareva E, Kaustov L, Ayed A, Yi GS, Lu Y, Pineda-Lucena A, Liao JC, Okorokov AL, Milner J, Arrowsmith CH, Bochkarev A. </i> Proc Natl Acad Sci U S A, 2005","reference_id":"16234232","region_id":"DP00086r030","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"In contrast, the N-terminal p53 transactivation domain is largely disordered in solution, but residues 37-57 fold into two amphipathic helices, H1 and H2, upon binding with RPA70N.","_id":"685af523b4ac24d5329d74dd"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:29:54.401Z","_id":"685af523b4ac24d5329d74dc"},"version":3,"_id":"685af523b4ac24d5329d74db","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2B3G","_id":"685af523b4ac24d5329d74e4"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":37,"end":57,"interaction_partner":[{"db":"UniProt","id":"P27694","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d74e3"}],"reference_html":"Single-stranded DNA mimicry in the p53 transactivation domain interaction with replication protein A. <i> Bochkareva E, Kaustov L, Ayed A, Yi GS, Lu Y, Pineda-Lucena A, Liao JC, Okorokov AL, Milner J, Arrowsmith CH, Bochkarev A. </i> Proc Natl Acad Sci U S A, 2005","reference_id":"16234232","region_id":"DP00086r031","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Here we report the crystal structure of RPA residues 1-120 (RPA70N) bound to the N-terminal transactivation domain of p53 (residues 37-57; p53N) and, by using NMR spectroscopy, characterize two mechanisms by which the RPA/p53 interaction can be modulated.","_id":"685af523b4ac24d5329d74e1"},{"type":"Abstract","text":"In contrast, the N-terminal p53 transactivation domain is largely disordered in solution, but residues 37-57 fold into two amphipathic helices, H1 and H2, upon binding with RPA70N.","_id":"685af523b4ac24d5329d74e2"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:30:18.252Z","_id":"685af523b4ac24d5329d74e0"},"version":4,"_id":"685af523b4ac24d5329d74df","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1YCR","_id":"685af523b4ac24d5329d74e8"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":17,"end":29,"interaction_partner":[],"reference_html":"Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. <i> Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP. </i> Science, 1996","reference_id":"8875929","region_id":"DP00086r032","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to a 15-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix.","_id":"685af523b4ac24d5329d74e7"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:29:57.436Z","_id":"685af523b4ac24d5329d74e6"},"version":3,"_id":"685af523b4ac24d5329d74e5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1YCR","_id":"685af523b4ac24d5329d74ed"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":15,"end":29,"interaction_partner":[{"db":"UniProt","id":"Q00987","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d74ec"}],"reference_html":"Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. <i> Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP. </i> Science, 1996","reference_id":"8875929","region_id":"DP00086r033","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to a 15-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix.","_id":"685af523b4ac24d5329d74eb"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:30:19.516Z","_id":"685af523b4ac24d5329d74ea"},"version":4,"_id":"685af523b4ac24d5329d74e9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":382,"end":382,"statements":[],"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d74f2"}],"cross_refs":[{"db":"PDB","id":"1JSP","_id":"685af523b4ac24d5329d74f1"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-13T21:01:12.415Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":367,"end":386,"interaction_partner":[{"db":"UniProt","id":"Q92793","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d74f0"}],"reference_html":"Structural mechanism of the bromodomain of the coactivator CBP in p53 transcriptional activation. <i> Mujtaba S, He Y, Zeng L, Yan S, Plotnikova O, Sachchidanand, Sanchez R, Zeleznik-Le NJ, Ronai Z, Zhou MM. </i> Mol Cell, 2004","reference_id":"14759370","region_id":"DP00086r034","released":"2022_06","sample":[],"sequence_construct":"SHLKSKKGQSTSRHKKLMFK","statement":[{"type":"Abstract","text":"Here, we report that the conserved bromo-domain of the transcriptional coactivator CBP (CREB binding protein) binds specifically to p53 at the C-terminal acetylated lysine 382. This bromodomain/acetyl-lysine binding is responsible for p53 acetylation-dependent coactivator recruitment after DNA damage, a step essential for p53-induced transcriptional activation of the cyclin-dependent kinase inhibitor p21 in G1 cell cycle arrest.","_id":"685af523b4ac24d5329d74ef"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-14T08:21:39.358Z","_id":"685af523b4ac24d5329d74f3"},"version":5,"_id":"685af523b4ac24d5329d74ee","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":382,"end":382,"statements":[],"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d74f9"}],"cross_refs":[{"db":"PDB","id":"1JSP","_id":"685af523b4ac24d5329d74f8"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-13T21:03:41.194Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":367,"end":386,"interaction_partner":[{"db":"UniProt","id":"Q92793","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d74f7"}],"reference_html":"Structural mechanism of the bromodomain of the coactivator CBP in p53 transcriptional activation. <i> Mujtaba S, He Y, Zeng L, Yan S, Plotnikova O, Sachchidanand, Sanchez R, Zeleznik-Le NJ, Ronai Z, Zhou MM. </i> Mol Cell, 2004","reference_id":"14759370","region_id":"DP00086r035","released":"2022_06","sample":[],"sequence_construct":"SHLKSKKGQSTSRHKKLMFK","statement":[{"type":"Results","text":"This binding is dependent upon K382 acetylation of the peptide with a KD of ∼50 μM, as estimated from NMR titration.","_id":"685af523b4ac24d5329d74f5"},{"type":"Results","text":"These results confirm that the CBP bromodomain can specifically interact with p53 acetylated at K382.","_id":"685af523b4ac24d5329d74f6"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-14T08:21:15.289Z","_id":"685af523b4ac24d5329d74fa"},"version":5,"_id":"685af523b4ac24d5329d74f4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":382,"end":382,"statements":[],"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d74fe"}],"cross_refs":[{"db":"PDB","id":"1JSP","_id":"685af523b4ac24d5329d74fd"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-13T21:03:15.580Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":380,"end":384,"interaction_partner":[],"reference_html":"Structural mechanism of the bromodomain of the coactivator CBP in p53 transcriptional activation. <i> Mujtaba S, He Y, Zeng L, Yan S, Plotnikova O, Sachchidanand, Sanchez R, Zeleznik-Le NJ, Ronai Z, Zhou MM. </i> Mol Cell, 2004","reference_id":"14759370","region_id":"DP00086r036","released":"2022_06","sample":[],"sequence_construct":"SHLKSKKGQSTSRHKKLMFK","statement":[{"type":"Results","text":"This binding is dependent upon K382 acetylation of the peptide with a KD of ∼50 μM, as estimated from NMR titration.","_id":"685af523b4ac24d5329d74fc"}],"states_connection":[],"term_id":"IDPO:0000039","term_name":"acetylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-14T08:19:19.196Z","_id":"685af523b4ac24d5329d74ff"},"version":3,"_id":"685af523b4ac24d5329d74fb","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1JSP","_id":"685af523b4ac24d5329d7503"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005581","ec_name":"enzyme-linked immunoabsorbent assay evidence used in manual assertion","ec_ontology":"ECO","start":367,"end":386,"interaction_partner":[],"reference_html":"Structural mechanism of the bromodomain of the coactivator CBP in p53 transcriptional activation. <i> Mujtaba S, He Y, Zeng L, Yan S, Plotnikova O, Sachchidanand, Sanchez R, Zeleznik-Le NJ, Ronai Z, Zhou MM. </i> Mol Cell, 2004","reference_id":"14759370","region_id":"DP00086r037","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"p53-Induced p21 Activation Requires the CBP Bromodomain/p53 AcK382 Interaction","_id":"685af523b4ac24d5329d7502"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_id":"GO:0140677","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:31:00.802Z","_id":"685af523b4ac24d5329d7501"},"version":4,"_id":"685af523b4ac24d5329d7500","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":382,"end":382,"statements":[],"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d7507"}],"cross_refs":[{"db":"PDB","id":"1JSP","_id":"685af523b4ac24d5329d7506"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-13T20:10:36.504Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":367,"end":386,"interaction_partner":[],"reference_html":"Structural mechanism of the bromodomain of the coactivator CBP in p53 transcriptional activation. <i> Mujtaba S, He Y, Zeng L, Yan S, Plotnikova O, Sachchidanand, Sanchez R, Zeleznik-Le NJ, Ronai Z, Zhou MM. </i> Mol Cell, 2004","reference_id":"14759370","region_id":"DP00086r038","released":"2022_06","sample":[{"db":"UniProt","deviation":null,"id":"Q92793","statements":[],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7508"}],"sequence_construct":"SHLKSKKGQSTSRHKKLMFK","statement":[{"type":"Curator statement","text":"P53 region 367-386 binds to CBP upon K382 acetylation and undergoes disorder-to-order transition upon binding","_id":"685af523b4ac24d5329d7505"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-14T07:54:06.582Z","_id":"685af523b4ac24d5329d7509"},"version":4,"_id":"685af523b4ac24d5329d7504","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":46,"end":46,"statements":[{"type":"Introduction","text":"In this study, we have determined the tertiary structure of the Ser46 and Thr55-phosphorylated p53 TAD2 bound to the PH domain of TFIIH p62.","_id":"685af523b4ac24d5329d7510"}],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d750f"},{"start":55,"end":55,"statements":[{"type":"Introduction","text":"In this study, we have determined the tertiary structure of the Ser46 and Thr55-phosphorylated p53 TAD2 bound to the PH domain of TFIIH p62.","_id":"685af523b4ac24d5329d7512"}],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d7511"}],"cross_refs":[{"db":"PDB","id":"2RUK","_id":"685af523b4ac24d5329d750e"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-13T21:00:13.427Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":47,"end":58,"interaction_partner":[{"db":"UniProt","id":"P32780","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d750d"}],"reference_html":"Extended string binding mode of the phosphorylated transactivation domain of tumor suppressor p53. <i> Okuda M, Nishimura Y. </i> J Am Chem Soc, 2014","reference_id":"25216154","region_id":"DP00086r039","released":"2022_06","sample":[],"statement":[{"type":"Abstract","text":"Here, we reveal the recognition mechanism of the phosphorylated TAD2 bound to a pleckstrin homology (PH) domain from human TFIIH subunit p62 in an extended string-like conformation.","_id":"685af523b4ac24d5329d750b"},{"type":"Results","text":"Although the isolated phosphorylated TAD2 seems to be intrinsically disordered, an extended and ordered structure was induced between residues 47–58 upon binding to the PH domain ","_id":"685af523b4ac24d5329d750c"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-15T07:34:23.254Z","_id":"685af523b4ac24d5329d7513"},"version":5,"_id":"685af523b4ac24d5329d750a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":46,"end":46,"statements":[{"type":"Introduction","text":"In this study, we have determined the tertiary structure of the\nSer46 and Thr55-phosphorylated p53 TAD2 bound to the PH\ndomain of TFIIH p62.","_id":"685af523b4ac24d5329d7518"}],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d7517"},{"start":55,"end":55,"statements":[{"type":"Introduction","text":"In this study, we have determined the tertiary structure of the\nSer46 and Thr55-phosphorylated p53 TAD2 bound to the PH\ndomain of TFIIH p62.","_id":"685af523b4ac24d5329d751a"}],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d7519"}],"cross_refs":[{"db":"PDB","id":"2RUK","_id":"685af523b4ac24d5329d7516"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-13T20:11:18.696Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":41,"end":62,"interaction_partner":[],"reference_html":"Extended string binding mode of the phosphorylated transactivation domain of tumor suppressor p53. <i> Okuda M, Nishimura Y. </i> J Am Chem Soc, 2014","reference_id":"25216154","region_id":"DP00086r040","released":"2022_06","sample":[{"db":"UniProt","deviation":null,"id":"P32780","statements":[],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d751b"}],"sequence_construct":"DDLMLSPDDIEQWFTEDPGPDE","statement":[{"type":"Abstract","text":"Here, we reveal the recognition mechanism of the phosphorylated TAD2 bound to a pleckstrin homology (PH) domain from human TFIIH subunit p62 in an extended string-like conformation.","_id":"685af523b4ac24d5329d7515"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-14T07:51:33.153Z","_id":"685af523b4ac24d5329d751c"},"version":4,"_id":"685af523b4ac24d5329d7514","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3DAB","_id":"685af523b4ac24d5329d7526"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":15,"end":29,"interaction_partner":[{"db":"UniProt","id":"O15151","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7525"}],"reference_html":"Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain. <i> Popowicz GM, Czarna A, Holak TA. </i> Cell Cycle, 2008","reference_id":"18677113","region_id":"DP00086r042","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":" We have determined the crystal structure of the N-terminal domain of human Mdmx bound to a 15-residue transactivation domain peptide of human p53.","_id":"685af523b4ac24d5329d7524"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:30:24.723Z","_id":"685af523b4ac24d5329d7523"},"version":4,"_id":"685af523b4ac24d5329d7522","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3DAB","_id":"685af523b4ac24d5329d752b"},{"db":"PDB","id":"3DAC","_id":"685af523b4ac24d5329d752c"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":17,"end":27,"interaction_partner":[],"reference_html":"Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain. <i> Popowicz GM, Czarna A, Holak TA. </i> Cell Cycle, 2008","reference_id":"18677113","region_id":"DP00086r043","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":" We have determined the crystal structure of the N-terminal domain of human Mdmx bound to a 15-residue transactivation domain peptide of human p53.","_id":"685af523b4ac24d5329d7529"},{"type":"Article","text":"The surface area occupied by aminoacids 17–27 of the p53 peptide has 440 Å2 for human Mdmx and 407 Å2 for zebrafish Mdmx.","_id":"685af523b4ac24d5329d752a"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:30:01.911Z","_id":"685af523b4ac24d5329d7528"},"version":3,"_id":"685af523b4ac24d5329d7527","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2LY4","_id":"685af523b4ac24d5329d7531"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":93,"interaction_partner":[{"db":"UniProt","id":"P09429","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7530"}],"reference_html":"HMGB1-facilitated p53 DNA binding occurs via HMG-Box/p53 transactivation domain interaction, regulated by the acidic tail. <i> Rowell JP, Simpson KL, Stott K, Watson M, Thomas JO. </i> Structure, 2012","reference_id":"23063560","region_id":"DP00086r044","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"The A box interacts with residues 38-61 (TAD2) of the p53 transactivation domain. Residues 19-26 (TAD1) bind weakly, but only in the context of p53(1-93) and not as a free TAD1 peptide. We have solved the structure of the A-box/p53(1-93) complex by nuclear magnetic resonance spectroscopy.","_id":"685af523b4ac24d5329d752f"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:30:26.517Z","_id":"685af523b4ac24d5329d752e"},"version":4,"_id":"685af523b4ac24d5329d752d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":93,"interaction_partner":[{"db":"UniProt","id":"P09429","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7535"}],"reference_html":"HMGB1-facilitated p53 DNA binding occurs via HMG-Box/p53 transactivation domain interaction, regulated by the acidic tail. <i> Rowell JP, Simpson KL, Stott K, Watson M, Thomas JO. </i> Structure, 2012","reference_id":"23063560","region_id":"DP00086r045","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Residues with resonances undergoing significant chemical-shift changes were located in the region spanning residues 18–57, which contains the elements of nascent secondary structure, namely TAD1 (residues 14–28) and TAD2 (residues 38–61) (Lee et al., 2000), with the largest changes occurring in TAD2.","_id":"685af523b4ac24d5329d7534"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:30:28.261Z","_id":"685af523b4ac24d5329d7533"},"version":4,"_id":"685af523b4ac24d5329d7532","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005647","ec_name":"isothermal titration calorimetry evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":93,"interaction_partner":[{"db":"UniProt","id":"P09429","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7539"}],"reference_html":"HMGB1-facilitated p53 DNA binding occurs via HMG-Box/p53 transactivation domain interaction, regulated by the acidic tail. <i> Rowell JP, Simpson KL, Stott K, Watson M, Thomas JO. </i> Structure, 2012","reference_id":"23063560","region_id":"DP00086r046","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"The isolated p53(1–93) fragment and the A box interact (Figure 2F), and an estimate of the affinity (Kd 346 nM) was obtained by isothermal titration calorimetry (ITC)","_id":"685af523b4ac24d5329d7538"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:30:29.838Z","_id":"685af523b4ac24d5329d7537"},"version":4,"_id":"685af523b4ac24d5329d7536","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":14,"end":60,"interaction_partner":[],"reference_html":"HMGB1-facilitated p53 DNA binding occurs via HMG-Box/p53 transactivation domain interaction, regulated by the acidic tail. <i> Rowell JP, Simpson KL, Stott K, Watson M, Thomas JO. </i> Structure, 2012","reference_id":"23063560","region_id":"DP00086r047","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Residues with resonances undergoing significant chemical-shift changes were located in the region spanning residues 18–57, which contains the elements of nascent secondary structure, namely TAD1 (residues 14–28) and TAD2 (residues 38–61) (Lee et al., 2000), with the largest changes occurring in TAD2.","_id":"685af523b4ac24d5329d753b"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:30:03.571Z","_id":"685af523b4ac24d5329d753c"},"version":3,"_id":"685af523b4ac24d5329d753a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":372,"end":372,"statements":[],"term_id":"MOD:00429","term_name":"dimethylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d7541"}],"cross_refs":[{"db":"PDB","id":"1XQH","_id":"685af523b4ac24d5329d7540"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-13T20:56:29.805Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":369,"end":377,"interaction_partner":[{"db":"UniProt","id":"Q8WTS6","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d753f"}],"reference_html":"Regulation of p53 activity through lysine methylation. <i> Chuikov S, Kurash JK, Wilson JR, Xiao B, Justin N, Ivanov GS, McKinney K, Tempst P, Prives C, Gamblin SJ, Barlev NA, Reinberg D. </i> Nature, 2004","reference_id":"15525938","region_id":"DP00086r048","released":"2022_06","sample":[],"sequence_construct":"LKSKKGQSTY","statement":[{"type":"Abstract","text":"The crystal structure of a ternary complex of Set9 with a p53 peptide and the cofactor product S-adenosyl-l-homocysteine (AdoHcy) provides the molecular basis for recognition of p53 by this lysine methyltransferase.","_id":"685af523b4ac24d5329d753e"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-14T08:17:34.609Z","_id":"685af523b4ac24d5329d7542"},"version":5,"_id":"685af523b4ac24d5329d753d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2FOO","_id":"685af523b4ac24d5329d7547"},{"db":"PDB","id":"2FOJ","_id":"685af523b4ac24d5329d7548"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":359,"end":367,"interaction_partner":[{"db":"UniProt","id":"Q93009","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7546"}],"reference_html":"Molecular recognition of p53 and MDM2 by USP7/HAUSP. <i> Sheng Y, Saridakis V, Sarkari F, Duan S, Wu T, Arrowsmith CH, Frappier L. </i> Nat Struct Mol Biol, 2006","reference_id":"16474402","region_id":"DP00086r049","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"We show that the N-terminal domain of USP7 binds two closely spaced 4-residue sites in both p53 and MDM2, falling between p53 residues 359-367 and MDM2 residues 147-159.","_id":"685af523b4ac24d5329d7545"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:30:32.884Z","_id":"685af523b4ac24d5329d7544"},"version":4,"_id":"685af523b4ac24d5329d7543","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":370,"end":370,"statements":[],"term_id":"MOD:00429","term_name":"dimethylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d754e"},{"start":382,"end":382,"statements":[],"term_id":"MOD:00429","term_name":"dimethylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d754f"}],"cross_refs":[{"db":"PDB","id":"2MWP","_id":"685af523b4ac24d5329d754c"},{"db":"PDB","id":"2MWO","_id":"685af523b4ac24d5329d754d"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-13T20:53:26.553Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":366,"end":386,"interaction_partner":[{"db":"UniProt","id":"Q12888","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d754b"}],"reference_html":"Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. <i> Tong Q, Cui G, Botuyan MV, Rothbart SB, Hayashi R, Musselman CA, Singh N, Appella E, Strahl BD, Mer G, Kutateladze TG. </i> Structure, 2015","reference_id":"25579814","region_id":"DP00086r050","released":"2022_06","sample":[],"statement":[{"type":"Abstract","text":"Here we detail the molecular mechanisms for the recognition of p53K370me2 and p53K382me2 by 53BP1. The solution structures of TTD in complex with the p53K370me2 and p53K382me2 peptides show a remarkable plasticity of 53BP1 in accommodating these diverse dimethyllysine-containing sequences. We demonstrate that dimeric TTDs are capable of interacting with the two PTMs on a single p53K370me2K382me2 peptide, greatly strengthening the 53BP1-p53 interaction.","_id":"685af523b4ac24d5329d754a"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-14T08:14:25.279Z","_id":"685af523b4ac24d5329d7550"},"version":5,"_id":"685af523b4ac24d5329d7549","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":370,"end":370,"statements":[],"term_id":"MOD:00429","term_name":"dimethylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d7555"},{"start":382,"end":382,"statements":[],"term_id":"MOD:00429","term_name":"dimethylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d7556"}],"cross_refs":[{"db":"PDB","id":"2MWP","_id":"685af523b4ac24d5329d7553"},{"db":"PDB","id":"2MWO","_id":"685af523b4ac24d5329d7554"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-13T20:02:45.868Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":366,"end":386,"interaction_partner":[],"reference_html":"Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. <i> Tong Q, Cui G, Botuyan MV, Rothbart SB, Hayashi R, Musselman CA, Singh N, Appella E, Strahl BD, Mer G, Kutateladze TG. </i> Structure, 2015","reference_id":"25579814","region_id":"DP00086r051","released":"2022_06","sample":[],"statement":[{"type":"Abstract","text":"Here we detail the molecular mechanisms for the recognition of p53K370me2 and p53K382me2 by 53BP1. The solution structures of TTD in complex with the p53K370me2 and p53K382me2 peptides show a remarkable plasticity of 53BP1 in accommodating these diverse dimethyllysine-containing sequences. We demonstrate that dimeric TTDs are capable of interacting with the two PTMs on a single p53K370me2K382me2 peptide, greatly strengthening the 53BP1-p53 interaction.","_id":"685af523b4ac24d5329d7552"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-14T07:50:02.762Z","_id":"685af523b4ac24d5329d7557"},"version":4,"_id":"685af523b4ac24d5329d7551","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":370,"end":370,"statements":[],"term_id":"MOD:00429","term_name":"dimethylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d755b"},{"start":382,"end":382,"statements":[],"term_id":"MOD:00429","term_name":"dimethylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d755c"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-13T20:52:26.498Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":366,"end":386,"interaction_partner":[{"db":"UniProt","id":"Q12888","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d755a"}],"reference_html":"Structural plasticity of methyllysine recognition by the tandem tudor domain of 53BP1. <i> Tong Q, Cui G, Botuyan MV, Rothbart SB, Hayashi R, Musselman CA, Singh N, Appella E, Strahl BD, Mer G, Kutateladze TG. </i> Structure, 2015","reference_id":"25579814","region_id":"DP00086r052","released":"2022_06","sample":[],"statement":[{"type":"Abstract","text":"Here we detail the molecular mechanisms for the recognition of p53K370me2 and p53K382me2 by 53BP1. The solution structures of TTD in complex with the p53K370me2 and p53K382me2 peptides show a remarkable plasticity of 53BP1 in accommodating these diverse dimethyllysine-containing sequences. We demonstrate that dimeric TTDs are capable of interacting with the two PTMs on a single p53K370me2K382me2 peptide, greatly strengthening the 53BP1-p53 interaction.","_id":"685af523b4ac24d5329d7559"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-14T08:13:30.821Z","_id":"685af523b4ac24d5329d755d"},"version":5,"_id":"685af523b4ac24d5329d7558","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":387,"end":387,"statements":[],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d7561"}],"cross_refs":[{"db":"PDB","id":"3LW1","_id":"685af523b4ac24d5329d7560"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-14T12:58:53.321Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":385,"end":393,"interaction_partner":[],"reference_html":"Structure of the p53 C-terminus bound to 14-3-3: implications for stabilization of the p53 tetramer. <i> Schumacher B, Mondry J, Thiel P, Weyand M, Ottmann C. </i> FEBS Lett, 2010","reference_id":"20206173","region_id":"DP00086r053","released":"2022_06","sample":[],"sequence_construct":"FKTEGPDSD","statement":[{"type":"Abstract","text":"Here, we report the crystal structure of the extreme C-terminus (residues 385-393, p53pT387) of p53 in complex with 14-3-3sigma at a resolution of 1.28A.","_id":"685af523b4ac24d5329d755f"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a 14-3-3 protein. A 14-3-3 protein is any of a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells, and have been implicated in the modulation of distinct biological processes by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. Each 14-3-3 protein sequence can be roughly divided into three sections: a divergent amino terminus, the conserved core region and a divergent carboxy-terminus. The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain, a cradle for interacting with client proteins.\" [GOC:cna, GOC:mah, PMID:15167810, PMID:19575580]","term_id":"GO:0071889","term_is_binding":true,"term_is_obsolete":false,"term_name":"14-3-3 protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-15T07:34:14.960Z","_id":"685af523b4ac24d5329d7562"},"version":5,"_id":"685af523b4ac24d5329d755e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2H4J","_id":"685af523b4ac24d5329d7567"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":372,"end":389,"interaction_partner":[{"db":"UniProt","id":"Q9WYW0","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7566"}],"reference_html":"Insights into the sirtuin mechanism from ternary complexes containing NAD+ and acetylated peptide. <i> Hoff KG, Avalos JL, Sens K, Wolberger C. </i> Structure, 2006","reference_id":"16905097","region_id":"DP00086r054","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"Crystal structure of Sir2, residues 1-246, bound to the C-terminal domain of p53, residues 372-389.","_id":"685af523b4ac24d5329d7565"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:30:39.053Z","_id":"685af523b4ac24d5329d7564"},"version":3,"_id":"685af523b4ac24d5329d7563","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2H4J","_id":"685af523b4ac24d5329d756b"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":375,"end":385,"interaction_partner":[],"reference_html":"Insights into the sirtuin mechanism from ternary complexes containing NAD+ and acetylated peptide. <i> Hoff KG, Avalos JL, Sens K, Wolberger C. </i> Structure, 2006","reference_id":"16905097","region_id":"DP00086r055","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"Crystal structure of Sir2, residues 1-246, bound to the C-terminal domain of p53, residues 372-389.","_id":"685af523b4ac24d5329d756a"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:30:06.562Z","_id":"685af523b4ac24d5329d7569"},"version":3,"_id":"685af523b4ac24d5329d7568","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1DT7","_id":"685af523b4ac24d5329d7570"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":367,"end":388,"interaction_partner":[{"db":"UniProt","id":"P04631","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d756f"}],"reference_html":"Structure of the negative regulatory domain of p53 bound to S100B(betabeta). <i> Rustandi RR, Baldisseri DM, Weber DJ. </i> Nat Struct Biol, 2000","reference_id":"10876243","region_id":"DP00086r056","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"A peptide derived from this region of p53 (residues 367-388) was found to have no regular structure in its native form by NMR spectroscopy, but becomes helical when bound to Ca2+ loaded S100B(betabeta).","_id":"685af523b4ac24d5329d756e"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:30:40.518Z","_id":"685af523b4ac24d5329d756d"},"version":4,"_id":"685af523b4ac24d5329d756c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1DT7","_id":"685af523b4ac24d5329d7574"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":367,"end":388,"interaction_partner":[],"reference_html":"Structure of the negative regulatory domain of p53 bound to S100B(betabeta). <i> Rustandi RR, Baldisseri DM, Weber DJ. </i> Nat Struct Biol, 2000","reference_id":"10876243","region_id":"DP00086r057","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"A peptide derived from this region of p53 (residues 367-388) was found to have no regular structure in its native form by NMR spectroscopy, but becomes helical when bound to Ca2+ loaded S100B(betabeta).","_id":"685af523b4ac24d5329d7573"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:30:07.793Z","_id":"685af523b4ac24d5329d7572"},"version":3,"_id":"685af523b4ac24d5329d7571","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1H26","_id":"685af523b4ac24d5329d757a"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":376,"end":386,"interaction_partner":[{"db":"UniProt","id":"P24941","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7578"},{"db":"UniProt","id":"P20248","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7579"}],"reference_html":"Specificity determinants of recruitment peptides bound to phospho-CDK2/cyclin A. <i> Lowe ED, Tews I, Cheng KY, Brown NR, Gul S, Noble ME, Gamblin SJ, Johnson LN. </i> Biochemistry, 2002","reference_id":"12501191","region_id":"DP00086r058","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"Crystal structure of a C-terminal 11-residue recruitment peptide of P53 in complex with CDK2/CyclinA","_id":"685af523b4ac24d5329d7577"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:30:41.588Z","_id":"685af523b4ac24d5329d7576"},"version":4,"_id":"685af523b4ac24d5329d7575","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2H2D","_id":"685af523b4ac24d5329d757f"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":372,"end":389,"interaction_partner":[{"db":"UniProt","id":"Q9WYW0","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d757e"}],"reference_html":"The structural basis of sirtuin substrate affinity. <i> Cosgrove MS, Bever K, Avalos JL, Muhammad S, Zhang X, Wolberger C. </i> Biochemistry, 2006","reference_id":"16768447","region_id":"DP00086r059","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"Crystal structure of a C-terminal acetylated (Lys382) peptide of P53 bound to Sir2 homologue from Thermatoga maritima (Sir2Tm). ","_id":"685af523b4ac24d5329d757d"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:30:43.363Z","_id":"685af523b4ac24d5329d757c"},"version":4,"_id":"685af523b4ac24d5329d757b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3TG5","_id":"685af523b4ac24d5329d7584"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":365,"end":375,"interaction_partner":[{"db":"UniProt","id":"Q9NRG4","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7583"}],"reference_html":"Structure of human SMYD2 protein reveals the basis of p53 tumor suppressor methylation. <i> Wang L, Li L, Zhang H, Luo X, Dai J, Zhou S, Gu J, Zhu J, Atadja P, Lu C, Li E, Zhao K. </i> J Biol Chem, 2011","reference_id":"21880715","region_id":"DP00086r060","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"We have solved the high resolution crystal structures of the full-length SMYD2 protein in binary complex with its cofactor S-adenosylmethionine and in ternary complex with cofactor product S-adenosylhomocysteine and p53 substrate peptide (residues 368-375), respectively.","_id":"685af523b4ac24d5329d7582"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:30:45.305Z","_id":"685af523b4ac24d5329d7581"},"version":4,"_id":"685af523b4ac24d5329d7580","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3TG5","_id":"685af523b4ac24d5329d7589"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007704","ec_name":"methylation assay evidence used in manual assertion","ec_ontology":"ECO","start":368,"end":372,"interaction_partner":[],"reference_html":"Structure of human SMYD2 protein reveals the basis of p53 tumor suppressor methylation. <i> Wang L, Li L, Zhang H, Luo X, Dai J, Zhou S, Gu J, Zhu J, Atadja P, Lu C, Li E, Zhao K. </i> J Biol Chem, 2011","reference_id":"21880715","region_id":"DP00086r061","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"SMYD2 belongs to a subfamily of histone lysine methyltransferase and was recently identified to methylate tumor suppressor p53 and Rb. Here we report that SMYD2 prefers to methylate p53 Lys-370 over histone substrates in vitro. Consistently, the level of endogenous p53 Lys-370 monomethylation is significantly elevated when SMYD2 is overexpressed in vivo.","_id":"685af523b4ac24d5329d7587"},{"type":"Results","text":"CTD Domain and EDEE Motif Are Important for p53 Lys-370 Methylation by SMYD2","_id":"685af523b4ac24d5329d7588"}],"states_connection":[],"term_id":"IDPO:0000042","term_name":"methylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:31:04.240Z","_id":"685af523b4ac24d5329d7586"},"version":3,"_id":"685af523b4ac24d5329d7585","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":382,"end":382,"statements":[],"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d758e"}],"cross_refs":[{"db":"PDB","id":"4ZZJ","_id":"685af523b4ac24d5329d758d"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-13T20:29:38.684Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":379,"end":385,"interaction_partner":[{"db":"UniProt","id":"Q96EB6","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d758c"}],"reference_html":"Crystallographic structure of a small molecule SIRT1 activator-enzyme complex. <i> Dai H, Case AW, Riera TV, Considine T, Lee JE, Hamuro Y, Zhao H, Jiang Y, Sweitzer SM, Pietrak B, Schwartz B, Blum CA, Disch JS, Caldwell R, Szczepankiewicz B, Oalmann C, Yee Ng P, White BH, Casaubon R, Narayan R, Koppetsch K, Bourbonais F, Wu B, Wang J, Qian D, Jiang F, Mao C, Wang M, Hu E, Wu JC, Perni RB, Vlasuk GP, Ellis JL. </i> Nat Commun, 2015","reference_id":"26134520","region_id":"DP00086r062","released":"2022_06","sample":[],"sequence_construct":"RHKKLLF","statement":[{"type":"Curator statement","text":"Crystal structure of a C-terminal peptide of P53 in complex with Sirt1","_id":"685af523b4ac24d5329d758b"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-14T08:23:10.469Z","_id":"685af523b4ac24d5329d758f"},"version":5,"_id":"685af523b4ac24d5329d758a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2K8F","_id":"685af523b4ac24d5329d7594"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":39,"interaction_partner":[{"db":"UniProt","id":"Q09472","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7593"}],"reference_html":"Structural basis for p300 Taz2-p53 TAD1 binding and modulation by phosphorylation. <i> Feng H, Jenkins LM, Durell SR, Hayashi R, Mazur SJ, Cherry S, Tropea JE, Miller M, Wlodawer A, Appella E, Bai Y. </i> Structure, 2009","reference_id":"19217391","region_id":"DP00086r063","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Here, we report the NMR structure of the complex of the Taz2 (C/H3) domain of p300 and the N-terminal transactivation domain of p53. In the complex, p53 forms a short alpha helix and interacts with the Taz2 domain through an extended surface.","_id":"685af523b4ac24d5329d7592"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:30:48.113Z","_id":"685af523b4ac24d5329d7591"},"version":3,"_id":"685af523b4ac24d5329d7590","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2K8F","_id":"685af523b4ac24d5329d7598"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":39,"interaction_partner":[],"reference_html":"Structural basis for p300 Taz2-p53 TAD1 binding and modulation by phosphorylation. <i> Feng H, Jenkins LM, Durell SR, Hayashi R, Mazur SJ, Cherry S, Tropea JE, Miller M, Wlodawer A, Appella E, Bai Y. </i> Structure, 2009","reference_id":"19217391","region_id":"DP00086r064","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Here, we report the NMR structure of the complex of the Taz2 (C/H3) domain of p300 and the N-terminal transactivation domain of p53. In the complex, p53 forms a short alpha helix and interacts with the Taz2 domain through an extended surface.","_id":"685af523b4ac24d5329d7597"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:30:09.164Z","_id":"685af523b4ac24d5329d7596"},"version":3,"_id":"685af523b4ac24d5329d7595","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":15,"end":15,"statements":[{"type":"Results","text":" To investigate these effects in detail, ITC experiments were performed in which p53 phosphorylated at Ser15, Thr18 or both sites was titrated into Taz2 at 15, 25, and 35 °C","_id":"685af523b4ac24d5329d759d"}],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d759c"},{"start":18,"end":18,"statements":[{"type":"Results","text":" To investigate these effects in detail, ITC experiments were performed in which p53 phosphorylated at Ser15, Thr18 or both sites was titrated into Taz2 at 15, 25, and 35 °C","_id":"685af523b4ac24d5329d759f"}],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d759e"}],"cross_refs":[{"db":"PDB","id":"2K8F","_id":"685af523b4ac24d5329d759b"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-13T20:20:33.154Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005647","ec_name":"isothermal titration calorimetry evidence used in manual assertion","ec_ontology":"ECO","start":14,"end":19,"interaction_partner":[],"reference_html":"Structural basis for p300 Taz2-p53 TAD1 binding and modulation by phosphorylation. <i> Feng H, Jenkins LM, Durell SR, Hayashi R, Mazur SJ, Cherry S, Tropea JE, Miller M, Wlodawer A, Appella E, Bai Y. </i> Structure, 2009","reference_id":"19217391","region_id":"DP00086r065","released":"2022_06","sample":[],"statement":[{"type":"Discussion","text":"Our structural and binding studies allow better understanding of the molecular basis for the increased binding affinity between Taz2 and p531-39 upon phosphorylation at Ser15 and Thr18.","_id":"685af523b4ac24d5329d759a"}],"states_connection":[],"term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-14T08:06:42.665Z","_id":"685af523b4ac24d5329d75a0"},"version":4,"_id":"685af523b4ac24d5329d7599","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":42,"end":56,"interaction_partner":[],"reference_html":"NMR chemical shift and relaxation measurements provide evidence for the coupled folding and binding of the p53 transactivation domain. <i> Vise PD, Baral B, Latos AJ, Daughdrill GW. </i> Nucleic Acids Res, 2005","reference_id":"15824059","region_id":"DP00086r066","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Figure 5a shows that residues 39–59 have the largest resonance intensity changes in the presence of hRPA701–168 with residues 42–56 having intensity ratios that are >10.","_id":"685af523b4ac24d5329d75a2"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:30:10.462Z","_id":"685af523b4ac24d5329d75a3"},"version":3,"_id":"685af523b4ac24d5329d75a1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":42,"end":56,"interaction_partner":[{"db":"UniProt","id":"P27694","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d75a7"}],"reference_html":"NMR chemical shift and relaxation measurements provide evidence for the coupled folding and binding of the p53 transactivation domain. <i> Vise PD, Baral B, Latos AJ, Daughdrill GW. </i> Nucleic Acids Res, 2005","reference_id":"15824059","region_id":"DP00086r067","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"The amide 1H and 15N chemical shifts of an uniformly 15N-labeled sample of p53TAD were also monitored before and after the addition of unlabeled hRPA701-168. In the presence of unlabeled hRPA701-168, resonance lineshapes increased and corresponding intensity reductions were observed for specific p53TAD residues. The largest intensity reductions were observed for p53TAD residues 42-56.","_id":"685af523b4ac24d5329d75a6"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-11-26T10:30:49.717Z","_id":"685af523b4ac24d5329d75a5"},"version":4,"_id":"685af523b4ac24d5329d75a4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":73,"interaction_partner":[],"reference_html":"NMR chemical shift and relaxation measurements provide evidence for the coupled folding and binding of the p53 transactivation domain. <i> Vise PD, Baral B, Latos AJ, Daughdrill GW. </i> Nucleic Acids Res, 2005","reference_id":"15824059","region_id":"DP00086r071","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"For instance, the mean values of R1, R2, R1ρ and the NHNOE for free p53TAD are consistent with values expected for an intrinsically unstructured protein (67).","_id":"685af523b4ac24d5329d75b5"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2020-11-26T10:40:08.672Z","_id":"685af523b4ac24d5329d75b4"},"version":2,"_id":"685af523b4ac24d5329d75b3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":73,"interaction_partner":[],"reference_html":"Transactivation ability of p53 transcriptional activation domain is directly related to the binding affinity to TATA-binding protein. <i> Chang J, Kim DH, Lee SW, Choi KY, Sung YC. </i> J Biol Chem, 1995","reference_id":"7559631","region_id":"DP00086r072","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The CD spectrum of p53 TAD peptide at neutral pH showed no apparent alpha-helical structure when analyzed byYang’s method (Fig. 4A; Ref. 50).","_id":"685af523b4ac24d5329d75b8"},{"type":"Curator statement","text":"Although the text only mentions the lack of a helical structure, the CD spectrum shows that the peptide is in fact disordered.","_id":"685af523b4ac24d5329d75b9"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2020-11-26T10:58:51.401Z","_id":"685af523b4ac24d5329d75b7"},"version":2,"_id":"685af523b4ac24d5329d75b6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-08T15:10:04.570Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006077","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":73,"interaction_partner":[{"db":"UniProt","id":"P20226","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d75bd"}],"reference_html":"Transactivation ability of p53 transcriptional activation domain is directly related to the binding affinity to TATA-binding protein. <i> Chang J, Kim DH, Lee SW, Choi KY, Sung YC. </i> J Biol Chem, 1995","reference_id":"7559631","region_id":"DP00086r073","released":"2022_03","sample":[],"statement":[{"type":"Figure","text":"The p53 TAD and mutant derivatives were assayed for the ability to bind in vitro translated human TBP in a GST pull-down assay as described under“Materials and Methods.”","_id":"685af523b4ac24d5329d75bb"},{"type":"Results","text":"As shown in Fig.3Band Table I, the levels of TBP precipitated by GST-p53 TAD and mutant derivatives are linearly correlated with the abilityof transactivation in vivo. ","_id":"685af523b4ac24d5329d75bc"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_id":"GO:0140677","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-07-11T13:14:38.789Z","_id":"685af523b4ac24d5329d75be"},"version":4,"_id":"685af523b4ac24d5329d75ba","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006077","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":73,"interaction_partner":[{"db":"UniProt","id":"7559631","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d75c2"}],"reference_html":"Transactivation ability of p53 transcriptional activation domain is directly related to the binding affinity to TATA-binding protein. <i> Chang J, Kim DH, Lee SW, Choi KY, Sung YC. </i> J Biol Chem, 1995","reference_id":"7559631","region_id":"DP00086r074","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As shown in Fig.3Band Table I, the levels of TBP precipitated by GST-p53 TAD and mutant derivatives are linearly correlated with the abilityof transactivation in vivo. ","_id":"685af523b4ac24d5329d75c1"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2020-11-26T11:08:46.997Z","_id":"685af523b4ac24d5329d75c0"},"version":3,"_id":"685af523b4ac24d5329d75bf","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2GS0","_id":"685af523b4ac24d5329d75c4"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":20,"end":46,"interaction_partner":[],"reference_html":"Structure of the Tfb1/p53 complex: Insights into the interaction between the p62/Tfb1 subunit of TFIIH and the activation domain of p53. <i> Di Lello P, Jenkins LMM, Jones TN, Nguyen BD, Hara T, Yamaguchi H, Dikeakos JD, Appella E, Legault P, Omichinski JG. </i> Mol Cell, 2006","reference_id":"16793543","region_id":"DP00086r075","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The p53 TAD2 in the complex is unstructured except for a short amphipathic α helix involving residues 47–55.","_id":"685af523b4ac24d5329d75c5"},{"type":"Results","text":"Chemical shift analysis and the NOE pattern demonstrated that p53 in complex with Tfb1 adopts an a-helical fold that extends from Pro47 to Thr55. Outside this region, p53 is flexible, as also supported by the 15N-1H heteronuclear NOE data.","_id":"685af523b4ac24d5329d75c6"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-12-07T13:49:45.178Z","_id":"685af523b4ac24d5329d75c7"},"version":1,"_id":"685af523b4ac24d5329d75c3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2GS0","_id":"685af523b4ac24d5329d75c9"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":56,"end":70,"interaction_partner":[],"reference_html":"Structure of the Tfb1/p53 complex: Insights into the interaction between the p62/Tfb1 subunit of TFIIH and the activation domain of p53. <i> Di Lello P, Jenkins LMM, Jones TN, Nguyen BD, Hara T, Yamaguchi H, Dikeakos JD, Appella E, Legault P, Omichinski JG. </i> Mol Cell, 2006","reference_id":"16793543","region_id":"DP00086r076","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The p53 TAD2 in the complex is unstructured except for a short amphipathic α helix involving residues 47–55.","_id":"685af523b4ac24d5329d75ca"},{"type":"Results","text":"Chemical shift analysis and the NOE pattern demonstrated that p53 in complex with Tfb1 adopts an a-helical fold that extends from Pro47 to Thr55. Outside this region, p53 is flexible, as also supported by the 15N-1H heteronuclear NOE data.","_id":"685af523b4ac24d5329d75cb"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-12-07T13:49:49.507Z","_id":"685af523b4ac24d5329d75cc"},"version":1,"_id":"685af523b4ac24d5329d75c8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":1,"end":61,"statements":[{"type":"Results","text":"To reduce spectral overlap and obtain high-quality NMR spectra, we utilized intein splicing to segmentally label the NTAD within tetrameric p53.","_id":"685af523b4ac24d5329d75cf"}],"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","_id":"685af523b4ac24d5329d75ce"},{"start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"To improve expression levels, stabilizing mutations (M133L/V203A/N239Y/N268D) were introduced into the DNA-binding domain.","_id":"685af523b4ac24d5329d75d1"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met133Leu","_id":"685af523b4ac24d5329d75d0"},{"start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"To improve expression levels, stabilizing mutations (M133L/V203A/N239Y/N268D) were introduced into the DNA-binding domain.","_id":"685af523b4ac24d5329d75d3"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val203Ala","_id":"685af523b4ac24d5329d75d2"},{"start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"To improve expression levels, stabilizing mutations (M133L/V203A/N239Y/N268D) were introduced into the DNA-binding domain.","_id":"685af523b4ac24d5329d75d5"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asn239Tyr","_id":"685af523b4ac24d5329d75d4"},{"start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"To improve expression levels, stabilizing mutations (M133L/V203A/N239Y/N268D) were introduced into the DNA-binding domain.","_id":"685af523b4ac24d5329d75d7"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asn268Asp","_id":"685af523b4ac24d5329d75d6"}],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-05-09T15:08:12.802Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":61,"interaction_partner":[],"reference_html":"Long-range regulation of p53 DNA binding by its intrinsically disordered N-terminal transactivation domain. <i> Krois AS, Dyson HJ, Wright PE. </i> Proc Natl Acad Sci U S A, 2018","reference_id":"30420502","region_id":"DP00086r077","released":"2022_06","sample":[{"db":"ChEBI","deviation":null,"entry_name":"sodium chloride","id":"26710","statements":[{"type":"Methods","text":"Salt titrations for p53(1–312) and p53(1–61) were carried out with protein concentrations of 150 μM. The initial titration point had a NaCl concentration of 150 mM, and NaCl from a 5-M concentrated stock was added to this sample at 50-mM increments up to 500 mM NaCl. ","_id":"685af523b4ac24d5329d75db"}],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":150,"_id":"685af523b4ac24d5329d75da"},{"db":"ChEBI","deviation":null,"entry_name":"sodium chloride","id":"26710","statements":[{"type":"Methods","text":"Salt titrations for p53(1–312) and p53(1–61) were carried out with protein concentrations of 150 μM. The initial titration point had a NaCl concentration of 150 mM, and NaCl from a 5-M concentrated stock was added to this sample at 50-mM increments up to 500 mM NaCl. ","_id":"685af523b4ac24d5329d75dd"}],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":500,"_id":"685af523b4ac24d5329d75dc"}],"sequence_construct":"MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDGSCFNGTEAPRMPEAAPPVAPAPAAPTPAAPAPAPSPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKLFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRAEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCYSSCMGGMNRRPILTIITLEDSSGNLLGRDSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD\n\n","statement":[{"type":"Abstract","text":"The N-terminal region is dynamically disordered in the full-length p53 tetramer, fluctuating between states in which it is free and fully exposed to solvent and states in which it makes transient contacts with the DNA-binding domain (DBD).","_id":"685af523b4ac24d5329d75d8"},{"type":"Results","text":"The cross-peaks in the spectrum of uniformly labeled p53 (black in Fig. 1C) are from residues in the disordered regions: The resonances of the folded DBD and TET domains are severely broadened in HSQC spectra of the 180-kDa tetramer, and their resonances are not visible.","_id":"685af523b4ac24d5329d75d9"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-07-11T13:15:02.855Z","_id":"685af523b4ac24d5329d75de"},"version":2,"_id":"685af523b4ac24d5329d75cd","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":1,"end":61,"statements":[{"type":"Results","text":"To reduce spectral overlap and obtain high-quality NMR spectra, we utilized intein splicing to segmentally label the NTAD within tetrameric p53.","_id":"685af523b4ac24d5329d75e1"}],"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","_id":"685af523b4ac24d5329d75e0"}],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":61,"interaction_partner":[{"db":"UniProt","id":"P04637","partner_start":95,"partner_end":312,"_id":"685af523b4ac24d5329d75e5"}],"reference_html":"Long-range regulation of p53 DNA binding by its intrinsically disordered N-terminal transactivation domain. <i> Krois AS, Dyson HJ, Wright PE. </i> Proc Natl Acad Sci U S A, 2018","reference_id":"30420502","region_id":"DP00086r078","released":"2022_03","sample":[],"sequence_construct":"MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD","statement":[{"type":"Abstract","text":"The N-terminal region is dynamically disordered in the full-length p53 tetramer, fluctuating between states in which it is free and fully exposed to solvent and states in which it makes transient contacts with the DNA-binding domain (DBD).","_id":"685af523b4ac24d5329d75e2"},{"type":"Results","text":"In addition to the chemical shift changes, residues in both AD1 and AD2 have decreased cross-peak intensity in the p53 tetramer relative to the peptide (Fig. 2C). While the intensity loss is greater for AD2 than AD1, it is clear that intramolecular interactions within full-length p53 affect the conformational ensemble and dynamics of both motifs.","_id":"685af523b4ac24d5329d75e3"},{"type":"Results","text":"Cross-peaks in spectra of 15N-labeled p53(1–61), p53(1–312), and 15NNTAD–p53 fall along a line, suggesting that p53(1–312) and the segmentally labeled full-length p53 experience the same two-site exchange process between states in which the NTAD is free or bound to the DBD.","_id":"685af523b4ac24d5329d75e4"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-12-07T13:48:48.888Z","_id":"685af523b4ac24d5329d75e6"},"version":1,"_id":"685af523b4ac24d5329d75df","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"A cysteine-knockout mutant of p53(1–312) was generated in which all exposed and semiexposed cysteine residues were mutated to serine, and nonnative cysteine residues were introduced by mutating either S15 or P58.","_id":"685af523b4ac24d5329d75f4"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser15Cys","_id":"685af523b4ac24d5329d75f3"},{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"A cysteine-knockout mutant of p53(1–312) was generated in which all exposed and semiexposed cysteine residues were mutated to serine, and nonnative cysteine residues were introduced by mutating either S15 or P58.","_id":"685af523b4ac24d5329d75f6"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro58Cys","_id":"685af523b4ac24d5329d75f5"},{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"A cysteine-knockout mutant of p53(1–312) was generated in which all exposed and semiexposed cysteine residues were mutated to serine, and nonnative cysteine residues were introduced by mutating either S15 or P58.","_id":"685af523b4ac24d5329d75f8"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys124Ser","_id":"685af523b4ac24d5329d75f7"},{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"A cysteine-knockout mutant of p53(1–312) was generated in which all exposed and semiexposed cysteine residues were mutated to serine, and nonnative cysteine residues were introduced by mutating either S15 or P58.","_id":"685af523b4ac24d5329d75fa"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys182Ser","_id":"685af523b4ac24d5329d75f9"},{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"A cysteine-knockout mutant of p53(1–312) was generated in which all exposed and semiexposed cysteine residues were mutated to serine, and nonnative cysteine residues were introduced by mutating either S15 or P58.","_id":"685af523b4ac24d5329d75fc"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys229Ser","_id":"685af523b4ac24d5329d75fb"},{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"A cysteine-knockout mutant of p53(1–312) was generated in which all exposed and semiexposed cysteine residues were mutated to serine, and nonnative cysteine residues were introduced by mutating either S15 or P58.","_id":"685af523b4ac24d5329d75fe"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys275Ser","_id":"685af523b4ac24d5329d75fd"},{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"A cysteine-knockout mutant of p53(1–312) was generated in which all exposed and semiexposed cysteine residues were mutated to serine, and nonnative cysteine residues were introduced by mutating either S15 or P58.","_id":"685af523b4ac24d5329d7600"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys277Ser","_id":"685af523b4ac24d5329d75ff"}],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":14,"end":28,"interaction_partner":[{"db":"UniProt","id":"P04637","partner_start":95,"partner_end":312,"_id":"685af523b4ac24d5329d7601"}],"reference_html":"Long-range regulation of p53 DNA binding by its intrinsically disordered N-terminal transactivation domain. <i> Krois AS, Dyson HJ, Wright PE. </i> Proc Natl Acad Sci U S A, 2018","reference_id":"30420502","region_id":"DP00086r081","released":"2022_03","sample":[{"db":"ChEBI","deviation":null,"entry_name":"4-maleimido-TEMPO","id":"180675","statements":[{"type":"Methods","text":"4-Maleimido-TEMPO (Sigma) was used for PRE spin-label experiments with p53(1–312) superstable C5×S/S15C, C5×S/P58C, and C5×/S121C proteins.","_id":"685af523b4ac24d5329d7605"}],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7604"}],"statement":[{"type":"Results","text":"With the spin label at S15C, cross-peaks of residues in both the AD1 and AD2 regions are broadened; similarly, attachment of the spin label at P58C broadens resonances associated with both the AD2 and AD1 motifs, confirming the presence of interactions between these motifs (SI Appendix, Fig. S4). Transient interactions between the AD1 and AD2 regions have been observed previously in isolated NTAD peptides (59). In addition, selective resonance broadening is observed for several DBD cross-peaks (SI Appendix, Fig. S4), indicating intramolecular interactions between the spin labeled NTAD and the DBD.","_id":"685af523b4ac24d5329d7602"},{"type":"Results","text":"With the spin label at P58C (AD2), the largest PRE is observed for residues located in the DNA-binding site; these include T118 and V122 in the L1 loop, G245 and to a lesser extent N247 in the L3 loop, A276, and G279, R280, and R283 in the C-terminal helix.","_id":"685af523b4ac24d5329d7603"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-02-28T13:54:36.794Z","_id":"685af523b4ac24d5329d7606"},"version":2,"_id":"685af523b4ac24d5329d75f2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"A cysteine-knockout mutant of p53(1–312) was generated in which all exposed and semiexposed cysteine residues were mutated to serine, and nonnative cysteine residues were introduced by mutating either S15 or P58.","_id":"685af523b4ac24d5329d7609"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser15Cys","_id":"685af523b4ac24d5329d7608"},{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"A cysteine-knockout mutant of p53(1–312) was generated in which all exposed and semiexposed cysteine residues were mutated to serine, and nonnative cysteine residues were introduced by mutating either S15 or P58.","_id":"685af523b4ac24d5329d760b"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro58Cys","_id":"685af523b4ac24d5329d760a"},{"start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Unless otherwise stated, all DBD-containing p53 constructs contained the quadruple M133L/V203A/N239Y/N268D superstabilizing mutations (45, 46). p53(1–393), the p53(88–312) cysteine-knockout mutant (C124S/C182S/C229S/C275S/C277S; C5×S), and all variations of p53(1–312) (e.g., wild type, M133L/V203A/N239Y/N268D, C5×S/S15C, C5×S/P58C, and C5×S/S121C) were expressed with N-terminal H6GB1 tags with a tobacco etch virus (TEV) protease cleavage site.","_id":"685af523b4ac24d5329d760d"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys124Ser","_id":"685af523b4ac24d5329d760c"},{"start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Unless otherwise stated, all DBD-containing p53 constructs contained the quadruple M133L/V203A/N239Y/N268D superstabilizing mutations (45, 46). p53(1–393), the p53(88–312) cysteine-knockout mutant (C124S/C182S/C229S/C275S/C277S; C5×S), and all variations of p53(1–312) (e.g., wild type, M133L/V203A/N239Y/N268D, C5×S/S15C, C5×S/P58C, and C5×S/S121C) were expressed with N-terminal H6GB1 tags with a tobacco etch virus (TEV) protease cleavage site.","_id":"685af523b4ac24d5329d760f"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys182Ser","_id":"685af523b4ac24d5329d760e"},{"start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Unless otherwise stated, all DBD-containing p53 constructs contained the quadruple M133L/V203A/N239Y/N268D superstabilizing mutations (45, 46). p53(1–393), the p53(88–312) cysteine-knockout mutant (C124S/C182S/C229S/C275S/C277S; C5×S), and all variations of p53(1–312) (e.g., wild type, M133L/V203A/N239Y/N268D, C5×S/S15C, C5×S/P58C, and C5×S/S121C) were expressed with N-terminal H6GB1 tags with a tobacco etch virus (TEV) protease cleavage site.","_id":"685af523b4ac24d5329d7611"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys229Ser","_id":"685af523b4ac24d5329d7610"},{"start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Unless otherwise stated, all DBD-containing p53 constructs contained the quadruple M133L/V203A/N239Y/N268D superstabilizing mutations (45, 46). p53(1–393), the p53(88–312) cysteine-knockout mutant (C124S/C182S/C229S/C275S/C277S; C5×S), and all variations of p53(1–312) (e.g., wild type, M133L/V203A/N239Y/N268D, C5×S/S15C, C5×S/P58C, and C5×S/S121C) were expressed with N-terminal H6GB1 tags with a tobacco etch virus (TEV) protease cleavage site.","_id":"685af523b4ac24d5329d7613"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys275Ser","_id":"685af523b4ac24d5329d7612"},{"start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Unless otherwise stated, all DBD-containing p53 constructs contained the quadruple M133L/V203A/N239Y/N268D superstabilizing mutations (45, 46). p53(1–393), the p53(88–312) cysteine-knockout mutant (C124S/C182S/C229S/C275S/C277S; C5×S), and all variations of p53(1–312) (e.g., wild type, M133L/V203A/N239Y/N268D, C5×S/S15C, C5×S/P58C, and C5×S/S121C) were expressed with N-terminal H6GB1 tags with a tobacco etch virus (TEV) protease cleavage site.","_id":"685af523b4ac24d5329d7615"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys277Ser","_id":"685af523b4ac24d5329d7614"}],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":38,"end":61,"interaction_partner":[{"db":"UniProt","id":"P04637","partner_start":95,"partner_end":312,"_id":"685af523b4ac24d5329d7616"}],"reference_html":"Long-range regulation of p53 DNA binding by its intrinsically disordered N-terminal transactivation domain. <i> Krois AS, Dyson HJ, Wright PE. </i> Proc Natl Acad Sci U S A, 2018","reference_id":"30420502","region_id":"DP00086r082","released":"2022_03","sample":[{"db":"ChEBI","deviation":null,"entry_name":"4-maleimido-TEMPO","id":"180675","statements":[{"type":"Methods","text":"4-Maleimido-TEMPO (Sigma) was used for PRE spin-label experiments with p53(1–312) superstable C5×S/S15C, C5×S/P58C, and C5×/S121C proteins.","_id":"685af523b4ac24d5329d761a"}],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7619"}],"statement":[{"type":"Results","text":"With the spin label at S15C, cross-peaks of residues in both the AD1 and AD2 regions are broadened; similarly, attachment of the spin label at P58C broadens resonances associated with both the AD2 and AD1 motifs, confirming the presence of interactions between these motifs (SI Appendix, Fig. S4). Transient interactions between the AD1 and AD2 regions have been observed previously in isolated NTAD peptides (59). In addition, selective resonance broadening is observed for several DBD cross-peaks (SI Appendix, Fig. S4), indicating intramolecular interactions between the spin labeled NTAD and the DBD.","_id":"685af523b4ac24d5329d7617"},{"type":"Results","text":"With the spin label at P58C (AD2), the largest PRE is observed for residues located in the DNA-binding site; these include T118 and V122 in the L1 loop, G245 and to a lesser extent N247 in the L3 loop, A276, and G279, R280, and R283 in the C-terminal helix.","_id":"685af523b4ac24d5329d7618"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-02-28T13:54:44.043Z","_id":"685af523b4ac24d5329d761b"},"version":2,"_id":"685af523b4ac24d5329d7607","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0005632","ec_name":"fluorescence anisotropy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":61,"interaction_partner":[],"reference_html":"Long-range regulation of p53 DNA binding by its intrinsically disordered N-terminal transactivation domain. <i> Krois AS, Dyson HJ, Wright PE. </i> Proc Natl Acad Sci U S A, 2018","reference_id":"30420502","region_id":"DP00086r083","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Taken together, the NMR and fluorescence data suggest a model in which the p53 NTAD can inhibit binding to nontarget DNA but does not affect binding to a cognate recognition element.","_id":"685af523b4ac24d5329d761d"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000059","term_name":"self-inhibition","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-12-07T13:50:12.766Z","_id":"685af523b4ac24d5329d761e"},"version":1,"_id":"685af523b4ac24d5329d761c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":61,"interaction_partner":[],"reference_html":"Long-range regulation of p53 DNA binding by its intrinsically disordered N-terminal transactivation domain. <i> Krois AS, Dyson HJ, Wright PE. </i> Proc Natl Acad Sci U S A, 2018","reference_id":"30420502","region_id":"DP00086r084","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Taken together, the NMR and fluorescence data suggest a model in which the p53 NTAD can inhibit binding to nontarget DNA but does not affect binding to a cognate recognition element.","_id":"685af523b4ac24d5329d7620"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000059","term_name":"self-inhibition","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-12-07T13:50:11.721Z","_id":"685af523b4ac24d5329d7621"},"version":1,"_id":"685af523b4ac24d5329d761f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-04-07T12:09:01.526Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":361,"end":393,"interaction_partner":[],"reference_html":"Latent and active p53 are identical in conformation. <i> Ayed A, Mulder FA, Yi GS, Lu Y, Kay LE, Arrowsmith CH. </i> Nat Struct Biol, 2001","reference_id":"11524676","region_id":"DP00086r085","released":"2022_06","sample":[],"statement":[{"type":"Results","text":"In addition, all of the new resonance peaks observed in the p53 construct containing the C-terminal domain (Fig. 3b) appear at frequencies typical of unstructured amides (-8 p.p.m. in the proton dimension). This suggests that the C-terminal domain is not likely to be folded into regular secondary structure.","_id":"685af523b4ac24d5329d7623"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-07-11T13:15:01.498Z","_id":"685af523b4ac24d5329d7624"},"version":2,"_id":"685af523b4ac24d5329d7622","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":361,"end":393,"interaction_partner":[],"reference_html":"Regulation of DNA binding of p53 by its C-terminal domain. <i> Weinberg RL, Freund SM, Veprintsev DB, Bycroft M, Fersht AR. </i> J Mol Biol, 2004","reference_id":"15342238","region_id":"DP00086r086","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In contrast, the behavior of the C-terminal domain was best characterized as unstructured and highly mobile, with chemical shift values close to random coil.","_id":"685af523b4ac24d5329d7626"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-07-11T13:15:00.544Z","_id":"685af523b4ac24d5329d7627"},"version":1,"_id":"685af523b4ac24d5329d7625","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1YCR","_id":"685af523b4ac24d5329d7629"},{"db":"ELM","id":"deg_mdm2_1","_id":"685af523b4ac24d5329d762a"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-08-08T18:37:30.631Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":19,"end":26,"interaction_partner":[{"db":"UniProt","id":"Q00987","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d762b"}],"reference_html":"Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. <i> Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP. </i> Science, 1996","reference_id":"8875929","region_id":"DP00086r087","released":"2022_12","sample":[],"statement":[{"type":"Article","text":"The position of the p53 helix allows Phe19, Trp23, and Leu26, which are aligned along its hydrophobic face, to insert deep inside the MDM2 cleft (Fig. 5A), and pack with the cleft in a complementary fashion (Fig. 5B).","_id":"685af523b4ac24d5329d762c"},{"type":"Abstract","text":"In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53.","_id":"685af523b4ac24d5329d762d"},{"type":"Article","text":"In normal cells, MDM2 and p53 form a negative feedback loop that helps to limit the growth-suppressing activity of p53.","_id":"685af523b4ac24d5329d762e"},{"type":"Curator statement","text":"The region 19-26 corresponds to a destruction/degron motif that binds to the MDM2 E3 ubiquitin-protein ligase.","_id":"685af523b4ac24d5329d762f"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.\" [GOC:vp]","term_id":"GO:0031625","term_is_obsolete":false,"term_name":"ubiquitin protein ligase binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2024-01-17T15:17:31.916Z","_id":"685af523b4ac24d5329d7630"},"version":0,"_id":"685af523b4ac24d5329d7628","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2023-12-12T10:37:58.064Z","disprot_namespace":"Structural state","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":367,"end":388,"interaction_partner":[],"reference_html":"Identifying intrinsically disordered protein regions likely to undergo binding-induced helical transitions. <i> Glover K, Mei Y, Sinha SC. </i> Biochim Biophys Acta, 2016","reference_id":"27179590","region_id":"DP00086r088","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"Secondary structure content estimated by analysis of CD spectra for each of the thirteen IDRs showed that none contained more than two residues in a helical conformation (Figures 1-3, Table 3-5), which is insufficient for the formation of a stable α-helix requiring a minimum of six residues. Formation of a minimal beta-structure requires six residues [38], and seven of the thirteen IDRs (Table 3-5) appear to have between six to eight residues in extended or β-conformation which may be sufficient for forming short stable β-hairpins (Table 3-5). Thus, while none of the selected IDRs had stable helical structure, several may have short β-strands.","_id":"685af523b4ac24d5329d7632"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2024-12-17T14:34:44.965Z","_id":"685af523b4ac24d5329d7633"},"version":0,"_id":"685af523b4ac24d5329d7631","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[{"deviation":null,"statements":[{"type":"Methods","text":"Circular dichroism spectra were recorded using a J-715 spectropolarimeter equipped with a PTC343 peltier unit (Jasco) in 20 mM sodium phosphate (pH 7.5), 300 mM sodium chloride at 20 °C in a 0.1 cm or 0.5 cm quartz cuvette for far-UV CD or near-UV CD spectroscopy, respectively.","_id":"685af523b4ac24d5329d7636"}],"term_id":"NCIT:C25206","unit_id":"UO:0000027","unit_name":"°C","value":20,"_id":"685af523b4ac24d5329d7635"},{"deviation":null,"statements":[],"term_id":"NCIT:C45997","unit_id":"UO:0000196","unit_name":"pH","value":7.5,"_id":"685af523b4ac24d5329d7637"}],"construct_alterations":[],"cross_refs":[],"curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","date":"2024-12-18T08:36:24.632Z","disprot_namespace":"Structural state","ec_id":"ECO:0006206","ec_name":"near-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":93,"interaction_partner":[],"reference_html":"The N-terminal domain of p53 is natively unfolded. <i> Dawson R, Müller L, Dehner A, Klein C, Kessler H, Buchner J. </i> J Mol Biol, 2003","reference_id":"14499615","region_id":"DP00086r089","released":"2025_06","sample":[],"statement":[{"type":"Results","text":"For Np53, signals in the near-UV region are largely missing. Under denaturing conditions (4 M GdmCl), no significant change in the near-UV CD signal of Np53 could be detected (Figure 2(C)). The low ellipticity values of the CD signal, together with the insensitivity to denaturation account for a solvent-exposed, unstructured protein.","_id":"685af523b4ac24d5329d7638"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2024-12-19T16:17:07.786Z","_id":"685af523b4ac24d5329d7639"},"version":0,"_id":"685af523b4ac24d5329d7634","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","date":"2024-12-18T08:34:45.455Z","disprot_namespace":"Structural state","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":93,"interaction_partner":[],"reference_html":"The N-terminal domain of p53 is natively unfolded. <i> Dawson R, Müller L, Dehner A, Klein C, Kessler H, Buchner J. </i> J Mol Biol, 2003","reference_id":"14499615","region_id":"DP00086r090","released":"2025_06","sample":[],"statement":[{"type":"Results","text":"The spectrum of the isolated NTD of p53 exhibits a minimum at 200 nm. The ΘMRW values above 200 nm suggest that α-helices and β-strands are largely missing. Far-UV CD spectra of Np53 analyzed under denaturing conditions (4 M GdmCl) showed only minor structural differences from spectra recorded under native conditions (Figure 2(A)). Taken together, the CD spectra indicate a remarkably high content of unstructured regions in Np53","_id":"685af523b4ac24d5329d763b"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2024-12-19T16:16:49.067Z","_id":"685af523b4ac24d5329d763c"},"version":0,"_id":"685af523b4ac24d5329d763a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","date":"2024-12-17T08:30:59.467Z","disprot_namespace":"Structural state","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":93,"interaction_partner":[],"reference_html":"The N-terminal domain of p53 is natively unfolded. <i> Dawson R, Müller L, Dehner A, Klein C, Kessler H, Buchner J. </i> J Mol Biol, 2003","reference_id":"14499615","region_id":"DP00086r091","released":"2025_06","sample":[],"statement":[{"type":"Results","text":"Spectra recorded under native as well as under denaturing conditions (4 M GdmCl) did not show significant changes in the maximum emission wavelength or the emission intensity (Figure 2(D)). The emission maximum of the standard N-acetyl-tryptophan-amide (Sigma) was 360 nm. Under native conditions, the fluorescence emission maximum of Np53 was 357 nm, under denaturing conditions 356 nm, both indicating complete solvent exposure. The existence of a well-defined tertiary structure could therefore be excluded","_id":"685af523b4ac24d5329d763e"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2024-12-17T14:43:26.316Z","_id":"685af523b4ac24d5329d763f"},"version":0,"_id":"685af523b4ac24d5329d763d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","date":"2024-12-17T08:48:59.486Z","disprot_namespace":"Structural state","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":93,"interaction_partner":[],"reference_html":"The N-terminal domain of p53 is natively unfolded. <i> Dawson R, Müller L, Dehner A, Klein C, Kessler H, Buchner J. </i> J Mol Biol, 2003","reference_id":"14499615","region_id":"DP00086r092","released":"2025_06","sample":[{"db":"ChEBI","deviation":null,"entry_name":"sodium azide","id":"278547","statements":[{"type":"Methods","text":"15N Np53 samples (1.2 mM) in 20 mM sodium phosphate (pH 7.5), 300 mM sodium chloride and 0.01 (w/v) sodium azide were used for NMR experiments.","_id":"685af523b4ac24d5329d7642"}],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":1.54,"_id":"685af523b4ac24d5329d7641"},{"db":"ChEBI","deviation":null,"entry_name":"sodium phosphate","id":"37586","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":20,"_id":"685af523b4ac24d5329d7643"},{"db":"ChEBI","deviation":null,"entry_name":"sodium chloride","id":"26710","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":300,"_id":"685af523b4ac24d5329d7644"}],"statement":[{"type":"Results","text":"We observed small proton resonance dispersion in a spectral range of 7.5–8.7 ppm, characteristic for a highly unfolded protein. In addition, the seven NH2 side-chain signals of asparagine and glutamine residues accumulate in their characteristic random coil region of 7.59 ppm/6.88 ppm. The same was observed for the side-chain signals of the three tryptophan residues of Np53, which appear at 10.2 ppm. Taken together, the spectrum shows, at the level of amino acids, that residues 1–93 of p53 are mostly unstructured","_id":"685af523b4ac24d5329d7645"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2024-12-17T14:44:28.015Z","_id":"685af523b4ac24d5329d7646"},"version":0,"_id":"685af523b4ac24d5329d7640","reference_source":"pmid"}],"__v":0,"disorder_content":0.37659033078880405,"disprot_consensus":{"full":[{"start":1,"end":62,"type":"T"},{"start":63,"end":93,"type":"D"},{"start":291,"end":312,"type":"D"},{"start":359,"end":360,"type":"F"},{"start":361,"end":365,"type":"D"},{"start":366,"end":388,"type":"T"},{"start":389,"end":393,"type":"D"}],"Structural state":[{"start":1,"end":93,"type":"D"},{"start":291,"end":312,"type":"D"},{"start":361,"end":393,"type":"D"}],"Molecular function":[{"start":1,"end":93,"type":"F"},{"start":359,"end":393,"type":"F"}],"Structural transition":[{"start":1,"end":62,"type":"T"},{"start":366,"end":388,"type":"T"}],"Disorder function":[{"start":1,"end":61,"type":"F"},{"start":368,"end":372,"type":"F"},{"start":380,"end":384,"type":"F"}]}},{"acc":"P68336","sequence":"MDLLVDDLFADADGVSPPPPRPAGGPKNTPAAPPLYATGRLSQAQLMPSPPMPVPPAALFNRLLDDLGFSAGPALCTMLDTWNEDLFSGFPTNADMYRECKFLSTLPSDVIDWGDAHVPERSPIDIRAHGDVAFPTLPATRDELPSYYEAMAQFFRGELRAREESYRTVLANFCSALYRYLRASVRQLHRQAHMRGRNRDLREMLRTTIADRYYRETARLARVLFLHLYLFLSREILWAAYAEQMMRPDLFDGLCCDLESWRQLACLFQPLMFINGSLTVRGVPVEARRLRELNHIREHLNLPLVRSAAAEEPGAPLTTPPVLQGNQARSSGYFMLLIRAKLDSYSSVATSEGESVMREHAYSRGRTRNNYGSTIEGLLDLPDDDDAPAEAGLVAPRMSFLSAGQRPRRLSTTAPITDVSLGDELRLDGEEVDMTPADALDDFDLEMLGDVESPSPGMTHDPVSYGALDVDDFEFEQMFTDAMGIDDFGG","creator":"mnecci","dataset":["Viral proteins"],"date":"2016-08-24T11:31:31.000Z","disprot_id":"DP00087","features":{"pfam":[{"id":"PF02232","name":"Alpha trans-inducing protein (Alpha-TIF)","start":42,"end":384},{"id":"PF12149","name":"Herpes simplex virus virion protein 16 C terminal","start":461,"end":490}],"gene3D":[{"start":45,"end":359,"id":"1.10.1290.10","name":"Alpha trans-inducing (Alpha-TIF)","_id":"685af523b4ac24d5329d7651"}]},"genes":[{"synonyms":[],"olnNames":[],"orfNames":[{"value":"UL48","evidences":[],"_id":"685af523b4ac24d5329d7697"}],"_id":"685af523b4ac24d5329d7696"}],"length":490,"name":"Tegument protein VP16","ncbi_taxon_id":10315,"organism":"Human herpesvirus 2 (strain HG52)","regions_counter":20,"released":"2016_10","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Peploviricota","Herviviricetes","Herpesvirales","Herpesviridae","Alphaherpesvirinae","Simplexvirus"],"UniParc":"UPI0000126250","uniref100":"UniRef100_P68336","uniref50":"UniRef50_P06492","uniref90":"UniRef90_P68336","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IPI","ec_id":"ECO:0006327","ec_name":"dynamic fluorescence quenching evidence used in manual assertion","ec_ontology":"ECO","start":413,"end":490,"interaction_partner":[],"reference_html":"Transcriptional activation domain of the herpesvirus protein VP16 becomes conformationally constrained upon interaction with basal transcription factors. <i> Shen F, Triezenberg SJ, Hensley P, Porter D, Knutson JR. </i> J Biol Chem, 1996","reference_id":"8617752","region_id":"DP00087r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Dynamic quenching constants for both GV-5HW442 and GV-5HW473 are thus of the same order of magnitude as that for free 5-OH-Trp. Consistent with the quenching study of GAL4-VP16 containing natural Trp(64), these results suggest that residues 442 and 473 are solvent-exposed.","_id":"685af523b4ac24d5329d766b"},{"type":"Curator statement","text":"GV-5HW442 and GV-5HW473 are in-frame fusions of GV to the VP16 activation domain (amino acids 413-490) with the incorporation of 5-hydroxytryptophan at position 442 or 473, respectively.","_id":"685af523b4ac24d5329d766c"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-27T07:26:42.521Z","_id":"685af523b4ac24d5329d766d"},"version":3,"_id":"685af523b4ac24d5329d766a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-08T15:10:54.768Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006327","ec_name":"dynamic fluorescence quenching evidence used in manual assertion","ec_ontology":"ECO","start":413,"end":490,"interaction_partner":[{"db":"UniProt","id":"P20226","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7671"}],"reference_html":"Transcriptional activation domain of the herpesvirus protein VP16 becomes conformationally constrained upon interaction with basal transcription factors. <i> Shen F, Triezenberg SJ, Hensley P, Porter D, Knutson JR. </i> J Biol Chem, 1996","reference_id":"8617752","region_id":"DP00087r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The presence of TBP altered the solvent accessibility of both residue 442 and 473. The downward curves of the Stern-Volmer plots were best fit to a two-species model, with approximately 40% of the probe molecules being inaccessible to acrylamide (assumed Ksv of 0) and an accessible fraction of approximately 60% having a Ka of 4.0 M-1 or 7.0 M-1 for GV-7AW442 or GV-7AW473, respectively.\" Results \"However, TFIIB did alter the solvent accessibility of GV-7AW473. Its Stern-Volmer plot was downward curved; in a two-species model, approximately 30% of the probe was inaccessible, and the accessible fraction had a Ka of 4.9 M-1.","_id":"685af523b4ac24d5329d766f"},{"type":"Curator statement","text":"GV-5HW442 and GV-5HW473 are in-frame fusions of GV to the VP16 activation domain (amino acids 413-490) with the incorporation of 5-hydroxytryptophan at position 442 or 473, respectively.","_id":"685af523b4ac24d5329d7670"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_id":"GO:0140677","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-23T14:15:18.266Z","_id":"685af523b4ac24d5329d7672"},"version":5,"_id":"685af523b4ac24d5329d766e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006327","ec_name":"dynamic fluorescence quenching evidence used in manual assertion","ec_ontology":"ECO","start":413,"end":490,"interaction_partner":[{"db":"UniProt","id":"P62380","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7676"},{"db":"UniProt","id":"Q00403","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7677"}],"reference_html":"Transcriptional activation domain of the herpesvirus protein VP16 becomes conformationally constrained upon interaction with basal transcription factors. <i> Shen F, Triezenberg SJ, Hensley P, Porter D, Knutson JR. </i> J Biol Chem, 1996","reference_id":"8617752","region_id":"DP00087r014","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The presence of TBP altered the solvent accessibility of both residue 442 and 473. The downward curves of the Stern-Volmer plots were best fit to a two-species model, with approximately 40% of the probe molecules being inaccessible to acrylamide (assumed Ksv of 0) and an accessible fraction of approximately 60% having a Ka of 4.0 M-1 or 7.0 M-1 for GV-7AW442 or GV-7AW473, respectively.","_id":"685af523b4ac24d5329d7678"},{"type":"Results","text":"However, TFIIB did alter the solvent accessibility of GV-7AW473. Its Stern-Volmer plot was downward curved; in a two-species model, approximately 30% of the probe was inaccessible, and the accessible fraction had a Ka of 4.9 M-1.","_id":"685af523b4ac24d5329d7679"},{"type":"Curator statement","text":"GV-5HW442 and GV-5HW473 are in-frame fusions of GV to the VP16 activation domain (amino acids 413-490) with the incorporation of 5-hydroxytryptophan at position 442 or 473, respectively.","_id":"685af523b4ac24d5329d767a"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-27T07:27:34.169Z","_id":"685af523b4ac24d5329d767b"},"version":4,"_id":"685af523b4ac24d5329d7675","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0005632","ec_name":"fluorescence anisotropy evidence used in manual assertion","ec_ontology":"ECO","start":413,"end":490,"interaction_partner":[],"reference_html":"Transcriptional activation domain of the herpesvirus protein VP16 becomes conformationally constrained upon interaction with basal transcription factors. <i> Shen F, Triezenberg SJ, Hensley P, Porter D, Knutson JR. </i> J Biol Chem, 1996","reference_id":"8617752","region_id":"DP00087r016","released":"2022_03","sample":[],"sequence_construct":"TAPITDVSLGDELRLDGEEVDMTPADALDWFDLEMLGDVESPSPGMTHDPVSYGALDVDDFEFEQMFTDAMGIDDFGG","statement":[{"type":"Results","text":"The anisotropy decays of the activator proteins (tested in the absence of target proteins) were best fit to two components: a subnanosecond fast decay component representing segmental motion around the 5-OH-Trp fluorophore and the slower decay component in the range of 2-6 ns. In all of these proteins, the segmental motion contributed at least 60% of the anisotropy decay. The extent of these segmental motions were comparable with those of the known most flexible proteins(42).","_id":"685af523b4ac24d5329d767f"},{"type":"Curator statement","text":"The peptides GV-5HW442 and GV-5HW473, studied in this publication, are in-frame fusions of GV to the VP16 activation domain (amino acids 413-490) with the incorporation of 5-hydroxytryptophan at position 442 or 473, respectively.","_id":"685af523b4ac24d5329d7680"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-27T07:26:38.719Z","_id":"685af523b4ac24d5329d7681"},"version":1,"_id":"685af523b4ac24d5329d767e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0005632","ec_name":"fluorescence anisotropy evidence used in manual assertion","ec_ontology":"ECO","start":413,"end":490,"interaction_partner":[{"db":"UniProt","id":"P62380","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7683"}],"reference_html":"Transcriptional activation domain of the herpesvirus protein VP16 becomes conformationally constrained upon interaction with basal transcription factors. <i> Shen F, Triezenberg SJ, Hensley P, Porter D, Knutson JR. </i> J Biol Chem, 1996","reference_id":"8617752","region_id":"DP00087r017","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The addition of TBP to GV-5HW442 resulted in a large saturable increment in its anisotropy (Fig. 6A), indicating a large decrease in the mobility of the 5-OH-Trp fluorophore. Assuming a 1:1 stoichiometry for the GAL4-VP16•TBP complex, the dissociation constant for the interaction was calculated to be 3.3 (± 1.7) × 10-7M.","_id":"685af523b4ac24d5329d7684"},{"type":"Results","text":"When the analog was incorporated at position 473 of the full-length activation domain (GV-5HW473), the anisotropy also increased rapidly as TBP was added to the system, and the anisotropy reached a limiting value (Fig. 6C). The calculated dissociation constant for this interaction is 2.6 (± 0.6) × 10-8M.","_id":"685af523b4ac24d5329d7685"},{"type":"Curator statement","text":"GV-5HW442 and GV-5HW473 are in-frame fusions of GV to the VP16 activation domain (amino acids 413-490) with the incorporation of 5-hydroxytryptophan at position 442 or 473, respectively.","_id":"685af523b4ac24d5329d7686"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-27T07:26:55.509Z","_id":"685af523b4ac24d5329d7687"},"version":1,"_id":"685af523b4ac24d5329d7682","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0005632","ec_name":"fluorescence anisotropy evidence used in manual assertion","ec_ontology":"ECO","start":413,"end":490,"interaction_partner":[],"reference_html":"Transcriptional activation domain of the herpesvirus protein VP16 becomes conformationally constrained upon interaction with basal transcription factors. <i> Shen F, Triezenberg SJ, Hensley P, Porter D, Knutson JR. </i> J Biol Chem, 1996","reference_id":"8617752","region_id":"DP00087r018","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The addition of TBP to GV-5HW442 resulted in a large saturable increment in its anisotropy (Fig. 6A), indicating a large decrease in the mobility of the 5-OH-Trp fluorophore. Assuming a 1:1 stoichiometry for the GAL4-VP16•TBP complex, the dissociation constant for the interaction was calculated to be 3.3 (± 1.7) × 10-7M.","_id":"685af523b4ac24d5329d7689"},{"type":"Results","text":"When the analog was incorporated at position 473 of the full-length activation domain (GV-5HW473), the anisotropy also increased rapidly as TBP was added to the system, and the anisotropy reached a limiting value (Fig. 6C). The calculated dissociation constant for this interaction is 2.6 (± 0.6) × 10-8M.","_id":"685af523b4ac24d5329d768a"},{"type":"Curator statement","text":"GV-5HW442 and GV-5HW473 are in-frame fusions of GV to the VP16 activation domain (amino acids 413-490) with the incorporation of 5-hydroxytryptophan at position 442 or 473, respectively.","_id":"685af523b4ac24d5329d768b"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_go_domain":"F","term_id":"GO:0140677","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-27T07:27:43.626Z","_id":"685af523b4ac24d5329d768c"},"version":1,"_id":"685af523b4ac24d5329d7688","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":413,"end":490,"interaction_partner":[],"reference_html":"Critical amino acids in the transcriptional activation domain of the herpesvirus protein VP16 are solvent-exposed in highly mobile protein segments. An intrinsic fluorescence study. <i> Shen F, Triezenberg SJ, Hensley P, Porter D, Knutson JR. </i> J Biol Chem, 1996","reference_id":"8617751","region_id":"DP00087r019","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The Trp473 in the full-length activation domain context displayed an emission maximum centered at 349 ± 2 nm, while a C subdomain yielded an emission maximum centered at 348 ± 2 nm. All of these emission wavelength maxima resemble those of fully exposed Trp residues, suggesting that both Trp442 and Trp473 are accessible to solvent.","_id":"685af523b4ac24d5329d768e"},{"type":"Discussion","text":"The fluorescence studies of the VP16 AAD described here showed that this domain was highly flexible and mobile, suggesting that it is poorly structured.","_id":"685af523b4ac24d5329d768f"},{"type":"Curator statement","text":"To obtain unique intrinsic fluorescence probes at key positions within the VP16 AAD, Trp mutations were introduced at either position 442 or 473.","_id":"685af523b4ac24d5329d7690"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-27T07:26:35.795Z","_id":"685af523b4ac24d5329d7691"},"version":1,"_id":"685af523b4ac24d5329d768d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0005632","ec_name":"fluorescence anisotropy evidence used in manual assertion","ec_ontology":"ECO","start":413,"end":490,"interaction_partner":[],"reference_html":"Critical amino acids in the transcriptional activation domain of the herpesvirus protein VP16 are solvent-exposed in highly mobile protein segments. An intrinsic fluorescence study. <i> Shen F, Triezenberg SJ, Hensley P, Porter D, Knutson JR. </i> J Biol Chem, 1996","reference_id":"8617751","region_id":"DP00087r020","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"These small values, in the range of 0.059-0.079, suggest that probes at either position were associated with fast segmental motion as seen in the flexible polypeptide adrenocorticotropin, where rss = 0.06(50).","_id":"685af523b4ac24d5329d7693"},{"type":"Curator statement","text":"To obtain unique intrinsic fluorescence probes at key positions within the VP16 AAD, Trp mutations were introduced at either position 442 or 473.","_id":"685af523b4ac24d5329d7694"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-27T07:26:34.085Z","_id":"685af523b4ac24d5329d7695"},"version":1,"_id":"685af523b4ac24d5329d7692","reference_source":"pmid"}],"__v":0,"disorder_content":0.15918367346938775,"disprot_consensus":{"full":[{"start":413,"end":490,"type":"D"}],"Structural state":[{"start":413,"end":490,"type":"D"}],"Molecular function":[{"start":413,"end":490,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00115","name":"Cytochrome C and Quinol oxidase polypeptide I","start":56,"end":504}],"gene3D":[{"start":52,"end":552,"id":"1.20.210.10","name":"Cytochrome c oxidase-like, subunit I domain"}]},"uniref50":"UniRef50_P0ABJ0","sequence":"MFGKLSLDAVPFHEPIVMVTIAGIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPQFHTMLMIAASGAVLIALGILCLVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHERDAFWEMKEKGEAYKKPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPVAEIEKLENQHFDEITKAGLKNGN","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0ABJ0","disprot_id":"DP00088","ncbi_taxon_id":83333,"regions_counter":3,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":663,"region_id":"DP00088r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site. <i> Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikström M. </i> Nat Struct Biol, 2000","term_id":"IDPO:0000002","curator_id":"fquaglia","start":553,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11017202","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1FFT"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Out of the 1,291 residues in cytochrome bo3 ubiquinol oxidase we could assign the sequence for 967 residues (subunit I, 52–81, 96–179, 186–488, 490–520 and 541–552; subunit II, 36–112 and 125–283; subunit III, 19–51, 66–124 and 134–203; subunit IV, 1–109).","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-08T08:50:47.303Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":51,"region_id":"DP00088r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site. <i> Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikström M. </i> Nat Struct Biol, 2000","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11017202","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1FFT"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Out of the 1,291 residues in cytochrome bo3 ubiquinol oxidase we could assign the sequence for 967 residues (subunit I, 52–81, 96–179, 186–488, 490–520 and 541–552; subunit II, 36–112 and 125–283; subunit III, 19–51, 66–124 and 134–203; subunit IV, 1–109).","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-08T08:50:46.482Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P0ABJ0","date":"2016-08-11T14:34:36.000Z","acc":"P0ABI8","name":"Cytochrome bo(3) ubiquinol oxidase subunit 1","length":663,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI0000111624","genes":[{"name":{"value":"cyoB"},"olnNames":[{"value":"b0431"},{"value":"JW0421"}]}],"alphafold_very_low_content":0.0030165912518853697,"disorder_content":0.24434389140271492,"disprot_consensus":{"full":[{"start":1,"end":51,"type":"D"},{"start":553,"end":663,"type":"D"}],"Structural state":[{"start":1,"end":51,"type":"D"},{"start":553,"end":663,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00116","name":"Cytochrome C oxidase subunit II, periplasmic domain","start":149,"end":218},{"id":"PF06481","name":"COX Aromatic Rich Motif","start":239,"end":285}],"gene3D":[{"start":113,"end":282,"id":"2.60.40.420","name":"Cupredoxins -  blue copper proteins"},{"start":27,"end":112,"id":"1.10.287.90","name":"1.10.287.90"}]},"uniref50":"UniRef50_P0ABJ2","sequence":"MRLRKYNKSLGWLSLFAGTVLLSGCNSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYRASNKDAKYSPNWSHSNKVEAVVWTVPILIIIFLAVLTWKTTHALEPSKPLAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATPDRAAFDQWVAKAKQSPNTMSDMAAFEKLAAPSEYNQVEYFSNVKPDLFADVINKFMAHGKSMDMTQPEGEHSAHEGMEGMDMSHAESAH","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0ABJ2","disprot_id":"DP00089","ncbi_taxon_id":83333,"regions_counter":8,"creator":"mnecci","regions":[{"start":284,"end":315,"reference_id":"8618822","reference_source":"pmid","reference_html":"Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper center. <i> Wilmanns M, Lappalainen P, Kelly M, Sauer-Eriksson E, Saraste M. </i> Proc Natl Acad Sci U S A, 1995","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1CYW"},{"db":"PDB","id":"1CYX"}],"region_id":"DP00089r006","statement":[{"text":"The 14 N-terminal and 33 C-terminal residues in both CyoA structures are not defined in the electron density (Fig.1).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-08T09:01:11.931Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":26,"reference_id":"11017202","reference_source":"pmid","reference_html":"The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site. <i> Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikström M. </i> Nat Struct Biol, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1FFT"}],"region_id":"DP00089r007","statement":[{"text":"Out of the 1,291 residues in cytochrome bo3 ubiquinol oxidase we could assign the sequence for 967 residues (subunit I, 52–81, 96–179, 186–488, 490–520 and 541–552; subunit II, 36–112 and 125–283; subunit III, 19–51, 66–124 and 134–203; subunit IV, 1–109).","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-08T08:54:29.747Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":284,"end":315,"reference_id":"11017202","reference_source":"pmid","reference_html":"The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site. <i> Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikström M. </i> Nat Struct Biol, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1FFT"}],"region_id":"DP00089r008","statement":[{"text":"Out of the 1,291 residues in cytochrome bo3 ubiquinol oxidase we could assign the sequence for 967 residues (subunit I, 52–81, 96–179, 186–488, 490–520 and 541–552; subunit II, 36–112 and 125–283; subunit III, 19–51, 66–124 and 134–203; subunit IV, 1–109).","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-08T08:54:27.548Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P0ABJ2","date":"2016-09-12T09:37:22.000Z","acc":"P0ABJ1","name":"Cytochrome bo(3) ubiquinol oxidase subunit 2","length":315,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI0000111625","genes":[{"name":{"value":"cyoA"},"olnNames":[{"value":"b0432"},{"value":"JW0422"}]}],"alphafold_very_low_content":0.09206349206349207,"disorder_content":0.18412698412698414,"disprot_consensus":{"full":[{"start":1,"end":26,"type":"D"},{"start":284,"end":315,"type":"D"}],"Structural state":[{"start":1,"end":26,"type":"D"},{"start":284,"end":315,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00248","name":"Aldo/keto reductase family","start":104,"end":407}],"gene3D":[{"start":89,"end":413,"id":"3.20.20.100","name":"NADP-dependent oxidoreductase domain"}]},"uniref50":"UniRef50_Q14722","sequence":"MLAARTGAAGSQISEENTKLRRQSGFSVAGKDKSPKKASENAKDSSLSPSGESQLRARQLALLREVEMNWYLKLCDLSSEHTTVCTTGMPHRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKPYSKKDYRS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q14722","disprot_id":"DP00090","ncbi_taxon_id":9606,"regions_counter":4,"creator":"dpiovesan","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":62,"region_id":"DP00090r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR structure and functional characteristics of the hydrophilic N terminus of the potassium channel beta-subunit Kvbeta1.1. <i> Wissmann R, Baukrowitz T, Kalbacher H, Kalbitzer HR, Ruppersberg JP, Pongs O, Antz C, Fakler B. </i> J Biol Chem, 1999","term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"10585425","statement":[{"text":" In summary, these results indicated that βN-(1–62) does not exhibit a well defined structure in solution, but rather behaves like a flexible peptide showing only transient formation of local structures.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T16:37:16.896Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":62,"term_name":"flexible N-terminal tail","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"NMR structure and functional characteristics of the hydrophilic N terminus of the potassium channel beta-subunit Kvbeta1.1. <i> Wissmann R, Baukrowitz T, Kalbacher H, Kalbitzer HR, Ruppersberg JP, Pongs O, Antz C, Fakler B. </i> J Biol Chem, 1999","term_id":"IDPO:0000032","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"10585425","version":4,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00090r002","statement":[{"text":" In summary, these results indicated that βN-(1–62) does not exhibit a well defined structure in solution, but rather behaves like a flexible peptide showing only transient formation of local structures.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T16:37:09.429Z"}},{"start":1,"end":62,"reference_id":"10585425","reference_source":"pmid","reference_html":"NMR structure and functional characteristics of the hydrophilic N terminus of the potassium channel beta-subunit Kvbeta1.1. <i> Wissmann R, Baukrowitz T, Kalbacher H, Kalbitzer HR, Ruppersberg JP, Pongs O, Antz C, Fakler B. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006006","ec_ontology":"ECO","ec_name":"electrophysiology assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00090r003","statement":[{"text":"As shown in Fig. 1 B, βN-(1–62) induced rapid inactivation of these channels when present at 50 μm on the cytoplasmic side of the patch; the time-course of inactivation depended on the peptide concentration (not shown).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T16:38:18.115Z"}},{"start":1,"end":62,"reference_id":"10585425","reference_source":"pmid","reference_html":"NMR structure and functional characteristics of the hydrophilic N terminus of the potassium channel beta-subunit Kvbeta1.1. <i> Wissmann R, Baukrowitz T, Kalbacher H, Kalbitzer HR, Ruppersberg JP, Pongs O, Antz C, Fakler B. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006006","ec_ontology":"ECO","ec_name":"electrophysiology assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"Q09470","partner_start":null,"partner_end":null}],"region_id":"DP00090r004","statement":[{"text":"Wash-off of βN-(1–62), which should reflect unbinding of the peptide from the receptor, exhibited a time constant of ≈100 ms (99.9 ± 16.8 ms, n = 3) and could be well fitted with a monoexponential (Fig. 2 B, right). This indicated that interaction between βN-(1–62) and its receptor on the α-subunit is a first order reaction, with on and off rates (k on, k off) calculated as 1.7 × 106 mol−1 s−1 and 10.3 s−1 (Fig. 2 C).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T16:37:36.976Z"}}],"released":"2016_10","uniref100":"UniRef100_Q14722","date":"2016-08-18T17:05:38.000Z","acc":"Q14722","name":"Voltage-gated potassium channel subunit beta-1","length":419,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012E169","genes":[{"name":{"value":"KCNAB1"},"synonyms":[{"value":"KCNA1B"}]}],"alphafold_very_low_content":0.12171837708830549,"disorder_content":0.14797136038186157,"disprot_consensus":{"full":[{"start":1,"end":62,"type":"D"}],"Structural state":[{"start":1,"end":62,"type":"D"}],"Disorder function":[{"start":1,"end":62,"type":"F"}],"Molecular function":[{"start":1,"end":62,"type":"F"}]}},{"acc":"P27088","sequence":"MEPEPEPEQEANKEEEKILSAAVRAKIERNRQRALMLRQARLACRPYPTGEGISTVKAPPKVIDSGGGFFIEEEEAEEQHVENVVRQPGPVLECDYLICEECGKDFMDSYLSNHFDLAVCDSCRDAEEKHKLITRTEAKQEYLLKDCDIDKREPVLKFILKKNPHNTHWGDMKLYLKAQVIKRSLEVWGSEEALEEAKEVRKDNRDKMKQKKFDKKVKELRRTVRSSLWKKEASGHQHEYGPEEHVEEDSYKKTCITCGYEMNYEKM","alphafold_very_low_content":"0.10112359550561797","creator":"gminervini","dataset":[],"date":"2016-08-23T15:14:56.000Z","disprot_id":"DP00091","features":{"pfam":[{"id":"PF01286","name":"XPA protein N-terminal","start":98,"end":127},{"id":"PF05181","name":"XPA protein C-terminus","start":129,"end":180}],"gene3D":[{"start":92,"end":202,"id":"3.90.530.10","name":"XPA C-terminal domain","_id":"685af523b4ac24d5329d769a"}]},"genes":[{"name":{"value":"xpa","evidences":[],"_id":"685af523b4ac24d5329d76b2"},"synonyms":[{"value":"xpac","evidences":[],"_id":"685af523b4ac24d5329d76b3"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d76b1"}],"length":267,"name":"DNA repair protein complementing XP-A cells homolog","ncbi_taxon_id":8355,"organism":"Xenopus laevis","regions_counter":7,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Amphibia","Batrachia","Anura","Pipoidea","Pipidae","Xenopodinae","Xenopus","Xenopus"],"UniParc":"UPI000013900C","uniref100":"UniRef100_P27088","uniref50":"UniRef50_P23025","uniref90":"UniRef90_P27088","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006283","ec_name":"electrospray ionization fourier transform ion cyclotron resonance mass spectrometry evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":84,"interaction_partner":[],"reference_html":"Identification of intrinsic order and disorder in the DNA repair protein XPA. <i> Iakoucheva LM, Kimzey AL, Masselon CD, Bruce JE, Garner EC, Brown CJ, Dunker AK, Smith RD, Ackerman EJ. </i> Protein Sci, 2001","reference_id":"11344324","region_id":"DP00091r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The highly convoluted spectrum clearly showed there were different charge states of mainly four fragments, all beginning at position Q85 and terminating at R199, R203, K205, and K207.","_id":"685af523b4ac24d5329d769e"},{"type":"Results","text":"Thus, we conclude position R84 was more accessible to protease than the uncut sites.","_id":"685af523b4ac24d5329d769f"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-29T18:14:52.214Z","_id":"685af523b4ac24d5329d76a0"},"version":3,"_id":"685af523b4ac24d5329d769d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-22T09:01:18.311Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0001191","ec_name":"in vitro cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":84,"interaction_partner":[],"reference_html":"Identification of intrinsic order and disorder in the DNA repair protein XPA. <i> Iakoucheva LM, Kimzey AL, Masselon CD, Bruce JE, Garner EC, Brown CJ, Dunker AK, Smith RD, Ackerman EJ. </i> Protein Sci, 2001","reference_id":"11344324","region_id":"DP00091r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Our proteolysis data show long regions of either disorder or flexibility in xXPA, thereby providing an opportunity to evaluate the reliability of PONDR, a neural network predictor originally developed from literature searches of intrinsically ordered and disordered regions in proteins (Romero et al. 1997; Li et al. 1999).","_id":"685af523b4ac24d5329d76a6"},{"type":"Results","text":"The highly convoluted spectrum clearly showed there were different charge states of mainly four fragments, all beginning at position Q85 and terminating at R199, R203, K205, and K207.","_id":"685af523b4ac24d5329d76a7"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-29T18:14:50.043Z","_id":"685af523b4ac24d5329d76a8"},"version":0,"_id":"685af523b4ac24d5329d76a5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-22T09:02:06.723Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0001191","ec_name":"in vitro cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":199,"end":265,"interaction_partner":[],"reference_html":"Identification of intrinsic order and disorder in the DNA repair protein XPA. <i> Iakoucheva LM, Kimzey AL, Masselon CD, Bruce JE, Garner EC, Brown CJ, Dunker AK, Smith RD, Ackerman EJ. </i> Protein Sci, 2001","reference_id":"11344324","region_id":"DP00091r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Our proteolysis data show long regions of either disorder or flexibility in xXPA, thereby providing an opportunity to evaluate the reliability of PONDR, a neural network predictor originally developed from literature searches of intrinsically ordered and disordered regions in proteins (Romero et al. 1997; Li et al. 1999).","_id":"685af523b4ac24d5329d76aa"},{"type":"Results","text":"The highly convoluted spectrum clearly showed there were different charge states of mainly four fragments, all beginning at position Q85 and terminating at R199, R203, K205, and K207.","_id":"685af523b4ac24d5329d76ab"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-29T17:17:18.476Z","_id":"685af523b4ac24d5329d76ac"},"version":0,"_id":"685af523b4ac24d5329d76a9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-22T09:03:03.352Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006283","ec_name":"electrospray ionization fourier transform ion cyclotron resonance mass spectrometry evidence used in manual assertion","ec_ontology":"ECO","start":199,"end":265,"interaction_partner":[],"reference_html":"Identification of intrinsic order and disorder in the DNA repair protein XPA. <i> Iakoucheva LM, Kimzey AL, Masselon CD, Bruce JE, Garner EC, Brown CJ, Dunker AK, Smith RD, Ackerman EJ. </i> Protein Sci, 2001","reference_id":"11344324","region_id":"DP00091r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Our proteolysis data show long regions of either disorder or flexibility in xXPA, thereby providing an opportunity to evaluate the reliability of PONDR, a neural network predictor originally developed from literature searches of intrinsically ordered and disordered regions in proteins (Romero et al. 1997; Li et al. 1999).","_id":"685af523b4ac24d5329d76ae"},{"type":"Results","text":"The highly convoluted spectrum clearly showed there were different charge states of mainly four fragments, all beginning at position Q85 and terminating at R199, R203, K205, and K207.","_id":"685af523b4ac24d5329d76af"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-29T17:17:13.690Z","_id":"685af523b4ac24d5329d76b0"},"version":0,"_id":"685af523b4ac24d5329d76ad","reference_source":"pmid"}],"__v":0,"disorder_content":0.5655430711610487,"disprot_consensus":{"full":[{"start":1,"end":84,"type":"D"},{"start":199,"end":265,"type":"D"}],"Structural state":[{"start":1,"end":84,"type":"D"},{"start":199,"end":265,"type":"D"}]}},{"acc":"Q08209","sequence":"MSEPKAIDPKLSTTDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESVALRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTVRGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICSDDELGSEEDGFDGATAAARKEVIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLSGGKQTLQSATVEAIEADEAIKGFSPQHKITSFEEAKGLDRINERMPPRRDAMPSDANLNSINKALTSETNGTDSNGSNSSNIQ","alphafold_very_low_content":"0.07677543186180422","creator":"mnecci","dataset":["NDDs-related proteins"],"date":"2016-08-26T15:52:53.000Z","disprot_id":"DP00092","features":{"pfam":[{"id":"PF00149","name":"Calcineurin-like phosphoesterase","start":84,"end":283}],"gene3D":[{"start":7,"end":425,"id":"3.60.21.10","name":"3.60.21.10","_id":"685af523b4ac24d5329d76b5"}]},"genes":[{"name":{"value":"PPP3CA","evidences":[{"source":{"id":"HGNC:9314","name":"HGNC","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9314","_id":"685af523b4ac24d5329d7758"},"code":"ECO:0000312","_id":"685af523b4ac24d5329d7757"}],"_id":"685af523b4ac24d5329d7759"},"synonyms":[{"value":"CALNA","evidences":[],"_id":"685af523b4ac24d5329d775a"},{"value":"CNA","evidences":[],"_id":"685af523b4ac24d5329d775b"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d7756"}],"length":521,"name":"Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":47,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000110660","uniref100":"UniRef100_Q08209","uniref50":"UniRef50_Q08209","uniref90":"UniRef90_Q08209","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1AUI","_id":"685af523b4ac24d5329d76b7"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-17T14:08:50.991Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":13,"interaction_partner":[],"reference_html":"Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex. <i> Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW. </i> Nature, 1995","reference_id":"8524402","region_id":"DP00092r001","released":"2023_06","sample":[{"db":"UniProt","deviation":null,"id":"P63098","statements":[],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d76b9"}],"statement":[{"type":"Article","text":"CaNA residues 1-13, 374-468 and 487-521 are not visible in the electron density map.","_id":"685af523b4ac24d5329d76b8"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-01-18T10:36:15.099Z","_id":"685af523b4ac24d5329d76ba"},"version":4,"_id":"685af523b4ac24d5329d76b6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1AUI","_id":"685af523b4ac24d5329d76bc"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-17T14:09:02.790Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":374,"end":468,"interaction_partner":[],"reference_html":"Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex. <i> Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW. </i> Nature, 1995","reference_id":"8524402","region_id":"DP00092r002","released":"2023_06","sample":[{"db":"UniProt","deviation":null,"id":"P63098","statements":[],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d76be"}],"statement":[{"type":"Article","text":"CaNA residues 1-13, 374-468 and 487-521 are not visible in the electron density map.","_id":"685af523b4ac24d5329d76bd"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-01-18T10:36:17.219Z","_id":"685af523b4ac24d5329d76bf"},"version":4,"_id":"685af523b4ac24d5329d76bb","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1AUI","_id":"685af523b4ac24d5329d76d0"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-17T14:09:14.340Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":487,"end":521,"interaction_partner":[],"reference_html":"Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex. <i> Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW. </i> Nature, 1995","reference_id":"8524402","region_id":"DP00092r010","released":"2023_06","sample":[{"db":"UniProt","deviation":null,"id":"P63098","statements":[],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d76d2"}],"statement":[{"type":"Article","text":"CaNA residues 1-13, 374-468 and 487-521 are not visible in the electron density map.","_id":"685af523b4ac24d5329d76d1"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-01-18T10:36:18.539Z","_id":"685af523b4ac24d5329d76d3"},"version":4,"_id":"685af523b4ac24d5329d76cf","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[],"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","_id":"685af523b4ac24d5329d76e2"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-17T14:31:19.254Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":373,"end":466,"interaction_partner":[],"reference_html":"The distal helix in the regulatory domain of calcineurin is important for domain stability and enzyme function. <i> Dunlap TB, Cook EC, Rumi-Masante J, Arvin HG, Lester TE, Creamer TP. </i> Biochemistry, 2013","reference_id":"24191726","region_id":"DP00092r017","released":"2023_06","sample":[],"sequence_construct":"MWGSDDELGSEEDGFDGATAAARKEVIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLSGGKQTLQSATVEAIEADEAIKGFSPQHKITGCGGLEHHHHHH","statement":[{"type":"Results","text":"To analyze the secondary structure of the RD, we obtained CD spectra of the RD alone. The spectrum is consistent with that of an unstructured polypeptide chain (Figure 4a).","_id":"685af523b4ac24d5329d76e3"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-01-18T10:36:19.874Z","_id":"685af523b4ac24d5329d76e4"},"version":3,"_id":"685af523b4ac24d5329d76e1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[],"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","_id":"685af523b4ac24d5329d76e8"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-17T14:50:48.149Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":373,"end":466,"interaction_partner":[],"reference_html":"The distal helix in the regulatory domain of calcineurin is important for domain stability and enzyme function. <i> Dunlap TB, Cook EC, Rumi-Masante J, Arvin HG, Lester TE, Creamer TP. </i> Biochemistry, 2013","reference_id":"24191726","region_id":"DP00092r019","released":"2023_06","sample":[{"db":"UniProt","deviation":null,"id":"P0DP23","statements":[],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d76e9"}],"sequence_construct":"MWGSDDELGSEEDGFDGATAAARKEVIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLSGGKQTLQSATVEAIEADEAIKGFSPQHKITGCGGLEHHHHHH","statement":[{"type":"Results","text":"To analyze the secondary structure of the RD, we obtained CD spectra of the RD alone. The spectrum is consistent with that of an unstructured polypeptide chain (Figure 4a).","_id":"685af523b4ac24d5329d76ea"},{"type":"Results","text":"However, an equimolar mixture of CaM and the RD demonstrates that the RD:CaM complex has greater helical content than the pCaN:CaM complex (Figure 4a).","_id":"685af523b4ac24d5329d76eb"}],"states_connection":[{"source":"DP00092r017","target":"DP00092r040","_id":"685af523b4ac24d5329d76ec"}],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-01-18T10:36:24.620Z","_id":"685af523b4ac24d5329d76ed"},"version":3,"_id":"685af523b4ac24d5329d76e7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[],"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","_id":"685af523b4ac24d5329d76ef"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-17T14:47:34.757Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":373,"end":466,"interaction_partner":[{"db":"UniProt","id":"P0DP23","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d76f0"}],"reference_html":"The distal helix in the regulatory domain of calcineurin is important for domain stability and enzyme function. <i> Dunlap TB, Cook EC, Rumi-Masante J, Arvin HG, Lester TE, Creamer TP. </i> Biochemistry, 2013","reference_id":"24191726","region_id":"DP00092r020","released":"2023_06","sample":[],"sequence_construct":"MWGSDDELGSEEDGFDGATAAARKEVIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLSGGKQTLQSATVEAIEADEAIKGFSPQHKITGCGGLEHHHHHH","statement":[{"type":"Results","text":"However, an equimolar mixture of CaM and the RD demonstrates that the RD:CaM complex has greater helical content than the pCaN:CaM complex (Figure 4a).","_id":"685af523b4ac24d5329d76f1"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","term_id":"GO:0005516","term_is_binding":true,"term_is_obsolete":false,"term_name":"calmodulin binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-01-18T10:36:28.549Z","_id":"685af523b4ac24d5329d76f2"},"version":4,"_id":"685af523b4ac24d5329d76ee","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-17T15:24:48.987Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":373,"end":468,"interaction_partner":[],"reference_html":"Calcineurin in a Crowded World. <i> Cook EC, Creamer TP. </i> Biochemistry, 2016","reference_id":"27187005","region_id":"DP00092r032","released":"2023_06","sample":[{"db":"UniProt","deviation":null,"id":"P0DP23","statements":[],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d770c"}],"statement":[{"type":"Curator statement","text":"Authors show that when in complex with calmodulin, this region of the protein has greater helical content.","_id":"685af523b4ac24d5329d770d"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d770b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[],"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","_id":"685af523b4ac24d5329d770f"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-17T15:46:27.667Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":373,"end":468,"interaction_partner":[{"db":"UniProt","id":"P0DP23","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7710"}],"reference_html":"Calcineurin in a Crowded World. <i> Cook EC, Creamer TP. </i> Biochemistry, 2016","reference_id":"27187005","region_id":"DP00092r033","released":"2023_06","sample":[],"statement":[{"type":"Curator statement","text":"Authors show that when in presence of calmodulin the CD spectra changes, indicating the formation of a complex.","_id":"685af523b4ac24d5329d7711"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","term_id":"GO:0005516","term_is_binding":true,"term_is_obsolete":false,"term_name":"calmodulin binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-01-18T10:36:30.048Z","_id":"685af523b4ac24d5329d7712"},"version":4,"_id":"685af523b4ac24d5329d770e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1AUI","_id":"685af523b4ac24d5329d771c"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-17T16:31:01.744Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":13,"interaction_partner":[],"reference_html":"Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex. <i> Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW. </i> Nature, 1995","reference_id":"8524402","region_id":"DP00092r038","released":"2023_06","sample":[{"db":"UniProt","deviation":null,"id":"P63098","statements":[],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d771e"}],"statement":[{"type":"Results","text":"CaNA residues 1-13, 374-468 and 487-521 are not visible in the electron density map.","_id":"685af523b4ac24d5329d771d"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-01-18T10:36:31.878Z","_id":"685af523b4ac24d5329d771f"},"version":1,"_id":"685af523b4ac24d5329d771b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1AUI","_id":"685af523b4ac24d5329d7721"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-22T09:38:57.957Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":487,"end":521,"interaction_partner":[],"reference_html":"Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex. <i> Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW. </i> Nature, 1995","reference_id":"8524402","region_id":"DP00092r039","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"CaNA residues 1-13, 374-468 and 487-521 are not visible in the electron density map.","_id":"685af523b4ac24d5329d7722"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-01-16T17:18:16.545Z","_id":"685af523b4ac24d5329d7723"},"version":0,"_id":"685af523b4ac24d5329d7720","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[],"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","_id":"685af523b4ac24d5329d7725"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-17T14:50:09.101Z","disprot_namespace":"Structural state","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":373,"end":466,"interaction_partner":[],"reference_html":"The distal helix in the regulatory domain of calcineurin is important for domain stability and enzyme function. <i> Dunlap TB, Cook EC, Rumi-Masante J, Arvin HG, Lester TE, Creamer TP. </i> Biochemistry, 2013","reference_id":"24191726","region_id":"DP00092r040","released":"2023_06","sample":[{"db":"UniProt","deviation":null,"id":"P0DP23","statements":[],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7726"}],"sequence_construct":"MWGSDDELGSEEDGFDGATAAARKEVIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLSGGKQTLQSATVEAIEADEAIKGFSPQHKITGCGGLEHHHHHH","statement":[{"type":"Results","text":"However, an equimolar mixture of CaM and the RD demonstrates that the RD:CaM complex has greater helical content than the pCaN:CaM complex (Figure 4a).","_id":"685af523b4ac24d5329d7727"}],"states_connection":[],"term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-01-18T10:36:21.074Z","_id":"685af523b4ac24d5329d7728"},"version":0,"_id":"685af523b4ac24d5329d7724","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[],"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","_id":"685af523b4ac24d5329d772a"},{"start":null,"end":null,"position":null,"statements":[],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala389Cys","_id":"685af523b4ac24d5329d772b"},{"start":389,"end":389,"statements":[],"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","_id":"685af523b4ac24d5329d772c"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-17T15:04:03.518Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001183","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","ec_ontology":"ECO","start":388,"end":466,"interaction_partner":[{"db":"UniProt","id":"P0DP23","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d772d"}],"reference_html":"The distal helix in the regulatory domain of calcineurin is important for domain stability and enzyme function. <i> Dunlap TB, Cook EC, Rumi-Masante J, Arvin HG, Lester TE, Creamer TP. </i> Biochemistry, 2013","reference_id":"24191726","region_id":"DP00092r041","released":"2023_06","sample":[],"sequence_construct":"MAGTAAARKEVIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLSGGKQTLQSATVEAIEADEAIKGFSPQHKITGWGGGLEHHHHHH","statement":[{"type":"Results","text":"Ensemble average distances (rFRET) for this FRET pair in the RDc bound to CaM at 20 and 50 °C are shown in Figure 5a.","_id":"685af523b4ac24d5329d772e"},{"type":"Results","text":"CaM Binding Brings the Termini of the RD Together","_id":"685af523b4ac24d5329d772f"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","term_id":"GO:0005516","term_is_obsolete":false,"term_name":"calmodulin binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-01-18T10:36:33.708Z","_id":"685af523b4ac24d5329d7730"},"version":0,"_id":"685af523b4ac24d5329d7729","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[],"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","_id":"685af523b4ac24d5329d7732"},{"start":null,"end":null,"position":null,"statements":[],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala389Cys","_id":"685af523b4ac24d5329d7733"},{"start":389,"end":389,"statements":[],"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","_id":"685af523b4ac24d5329d7734"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-17T15:07:56.825Z","disprot_namespace":"Structural transition","ec_id":"ECO:0001183","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","ec_ontology":"ECO","start":388,"end":466,"interaction_partner":[],"reference_html":"The distal helix in the regulatory domain of calcineurin is important for domain stability and enzyme function. <i> Dunlap TB, Cook EC, Rumi-Masante J, Arvin HG, Lester TE, Creamer TP. </i> Biochemistry, 2013","reference_id":"24191726","region_id":"DP00092r042","released":"2023_06","sample":[{"db":"UniProt","deviation":null,"id":"P0DP23","statements":[],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7735"}],"sequence_construct":"MAGTAAARKEVIRNKIRAIGKMARVFSVLREESESVLTLKGLTPTGMLPSGVLSGGKQTLQSATVEAIEADEAIKGFSPQHKITGWGGGLEHHHHHH","statement":[{"type":"Results","text":"Ensemble average distances (rFRET) for this FRET pair in the RDc bound to CaM at 20 and 50 °C are shown in Figure 5a. At 20 °C, the average distance between the fluorophores is ∼10 Å, indicating that the two termini of RDc are relatively close to one another. ","_id":"685af523b4ac24d5329d7736"},{"type":"Discussion","text":"This distance is ∼6 Å shorter than the ensemble average distance measured for the RDc alone and suggests that, in the complex, the N-terminus of the CaMBR is relatively close to the C-terminal end of the putative structured region. This supports the hypothesis that upon CaM binding the RD folds into a hairpinlike structure that provides sufficient free energy for the removal of the AID from the active site.","_id":"685af523b4ac24d5329d7737"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-01-18T10:36:26.129Z","_id":"685af523b4ac24d5329d7738"},"version":0,"_id":"685af523b4ac24d5329d7731","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-17T16:20:08.626Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006305","ec_name":"native protein gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":389,"end":413,"interaction_partner":[{"db":"UniProt","id":"P0DP23","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d773a"}],"reference_html":"The complex structure of calmodulin bound to a calcineurin peptide. <i> Ye Q, Wang H, Zheng J, Wei Q, Jia Z. </i> Proteins, 2008","reference_id":"18384083","region_id":"DP00092r043","released":"2023_06","sample":[],"statement":[{"type":"Results","text":"In the absence of CaMBD and presence of either 2 mM or 10 mM Ca2+, only one CaM band was visible, which corresponds to CaM monomer. However, in the presence of CaMBD and presence of 2 mM or 10 mM Ca2+, two bands with molecular weight higher than CaM monomer, were clearly visible. The lower band corresponds to the monomer of the CaM/CaMBD complex, whilst the higher band matches CaM/CaMBD dimer (see Fig. 6). ","_id":"685af523b4ac24d5329d773b"},{"type":"Discussion","text":"Native PAGE results verified that dimers of CaM/CaMBD do exist in solution and a CaM pull-down assay unambiguously revealed that CaM does adopt an elongated conformation to bind to CaMBD.","_id":"685af523b4ac24d5329d773c"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","term_id":"GO:0005516","term_is_obsolete":false,"term_name":"calmodulin binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-01-18T10:36:37.881Z","_id":"685af523b4ac24d5329d773d"},"version":0,"_id":"685af523b4ac24d5329d7739","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-17T16:19:50.447Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006077","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","ec_ontology":"ECO","start":389,"end":413,"interaction_partner":[{"db":"UniProt","id":"P0DP23","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d773f"}],"reference_html":"The complex structure of calmodulin bound to a calcineurin peptide. <i> Ye Q, Wang H, Zheng J, Wei Q, Jia Z. </i> Proteins, 2008","reference_id":"18384083","region_id":"DP00092r044","released":"2023_06","sample":[],"statement":[{"type":"Results","text":"s shown in Figure 7(E), SDS-PAGE analysis revealed unbound, free CaM and CaMBD as well as unbound CaM/CaMBD in fractions containing the flow-through (Lane 3) and the washes (Lanes 4–5).","_id":"685af523b4ac24d5329d7740"},{"type":"Discussion","text":"Native PAGE results verified that dimers of CaM/CaMBD do exist in solution and a CaM pull-down assay unambiguously revealed that CaM does adopt an elongated conformation to bind to CaMBD.","_id":"685af523b4ac24d5329d7741"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","term_id":"GO:0005516","term_is_obsolete":false,"term_name":"calmodulin binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-01-18T10:36:39.229Z","_id":"685af523b4ac24d5329d7742"},"version":0,"_id":"685af523b4ac24d5329d773e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2R28","_id":"685af523b4ac24d5329d7744"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-17T16:24:52.146Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":393,"end":411,"interaction_partner":[{"db":"UniProt","id":"P0DP23","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7745"}],"reference_html":"The complex structure of calmodulin bound to a calcineurin peptide. <i> Ye Q, Wang H, Zheng J, Wei Q, Jia Z. </i> Proteins, 2008","reference_id":"18384083","region_id":"DP00092r045","released":"2023_06","sample":[{"db":"ChEBI","deviation":null,"entry_name":"calcium(2+)","id":"29108","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7746"}],"statement":[{"type":"Methods","text":"The refined final structure of the CaM/CaMBD complex is well-defined in the electron density map, with the following exceptions: Met-1, Ala-2, Asp-3, Gln-4, and Leu-5 in the first CaM molecule, and Met-1, Ala-2, Asp-3, and Gln-4 in the second CaM molecule. For the two peptides, out of 25 amino acids we were able to observe and model 15 residues (396–410 a.a.) in monomer A and 19 residues (393–411 a.a.) in monomer B, similar to those found in the fusion protein structure (15 and 21).24 These residues represent central core amino acids that make direct contact with CaM.","_id":"685af523b4ac24d5329d7747"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","term_id":"GO:0005516","term_is_obsolete":false,"term_name":"calmodulin binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-01-18T10:36:41.170Z","_id":"685af523b4ac24d5329d7748"},"version":0,"_id":"685af523b4ac24d5329d7743","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2R28","_id":"685af523b4ac24d5329d774a"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-17T16:27:31.663Z","disprot_namespace":"Structural state","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":393,"end":411,"interaction_partner":[],"reference_html":"The complex structure of calmodulin bound to a calcineurin peptide. <i> Ye Q, Wang H, Zheng J, Wei Q, Jia Z. </i> Proteins, 2008","reference_id":"18384083","region_id":"DP00092r046","released":"2023_06","sample":[{"db":"ChEBI","deviation":null,"entry_name":"calcium(2+)","id":"29108","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d774b"},{"db":"UniProt","deviation":null,"id":"P0DP23","statements":[],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d774c"}],"statement":[{"type":"Results","text":"The CaMBD peptides adopt α-helical conformation, as confirmed by the well-defined electron density (see Fig. 2).","_id":"685af523b4ac24d5329d774d"}],"states_connection":[],"term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-01-18T10:36:23.087Z","_id":"685af523b4ac24d5329d774e"},"version":0,"_id":"685af523b4ac24d5329d7749","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2R28","_id":"685af523b4ac24d5329d7750"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-01-17T16:29:24.381Z","disprot_namespace":"Structural transition","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":393,"end":411,"interaction_partner":[],"reference_html":"The complex structure of calmodulin bound to a calcineurin peptide. <i> Ye Q, Wang H, Zheng J, Wei Q, Jia Z. </i> Proteins, 2008","reference_id":"18384083","region_id":"DP00092r047","released":"2023_06","sample":[{"db":"ChEBI","deviation":null,"entry_name":"calcium(2+)","id":"29108","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7751"},{"db":"UniProt","deviation":null,"id":"P0DP23","statements":[],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7752"}],"statement":[{"type":"Results","text":"The CaMBD peptides adopt α-helical conformation, as confirmed by the well-defined electron density (see Fig. 2).","_id":"685af523b4ac24d5329d7753"}],"states_connection":[{"source":"DP00092r002","target":"DP00092r046","_id":"685af523b4ac24d5329d7754"}],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-01-18T10:36:27.588Z","_id":"685af523b4ac24d5329d7755"},"version":0,"_id":"685af523b4ac24d5329d774f","reference_source":"pmid"}],"__v":0,"disorder_content":0.2763915547024952,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"D"},{"start":373,"end":468,"type":"T"},{"start":487,"end":521,"type":"D"}],"Structural state":[{"start":1,"end":13,"type":"D"},{"start":373,"end":468,"type":"D"},{"start":487,"end":521,"type":"D"}],"Structural transition":[{"start":373,"end":468,"type":"T"}],"Molecular function":[{"start":373,"end":468,"type":"F"}],"Disorder function":[{"start":1,"end":13,"type":"F"},{"start":487,"end":521,"type":"F"}]}},{"acc":"P04177","sequence":"MPTPSAPSPQPKGFRRAVSEQDAKQAEAVTSPRFIGRRQSLIEDARKEREAAAAAAAAAVASSEPGNPLEAVVFEERDGNAVLNLLFSLRGTKPSSLSRAVKVFETFEAKIHHLETRPAQRPLAGSPHLEYFVRFEVPSGDLAALLSSVRRVSDDVRSAREDKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYKHGEPIPHVEYTAEEIATWKEVYVTLKGLYATHACREHLEGFQLLERYCGYREDSIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTVYWFTVEFGLCKQNGELKAYGAGLLSSYGELLHSLSEEPEVRAFDPDTAAVQPYQDQTYQPVYFVSESFNDAKDKLRNYASRIQRPFSVKFDPYTLAIDVLDSPHTIQRSLEGVQDELHTLAHALSAIS","alphafold_very_low_content":"0.0963855421686747","creator":"ftonello","dataset":[],"date":"2016-09-08T10:19:13.000Z","disprot_id":"DP00094","features":{"pfam":[{"id":"PF00351","name":"Biopterin-dependent aromatic amino acid hydroxylase","start":165,"end":494},{"id":"PF12549","name":"Tyrosine hydroxylase N terminal","start":2,"end":26},{"id":"PF12549","name":"Tyrosine hydroxylase N terminal","start":30,"end":49},{"id":"PF21417","name":"Tyrosine 3-monooxygenase-like, ACT domain","start":81,"end":149}],"gene3D":[{"start":158,"end":498,"id":"1.10.800.10","name":"Aromatic amino acid hydroxylase","_id":"685af523b4ac24d5329d775f"},{"start":65,"end":157,"id":"3.30.70.260","name":"3.30.70.260","_id":"685af523b4ac24d5329d7760"}]},"genes":[{"name":{"value":"Th","evidences":[],"_id":"685af523b4ac24d5329d77b9"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d77b8"}],"length":498,"name":"Tyrosine 3-monooxygenase","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions_counter":30,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"UniParc":"UPI000013786D","uniref100":"UniRef100_P04177","uniref50":"UniRef50_P07101-2","uniref90":"UniRef90_P04177","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":33,"end":50,"interaction_partner":[],"reference_html":"Limited proteolysis of tyrosine hydroxylase identifies residues 33-50 as conformationally sensitive to phosphorylation state and dopamine binding. <i> McCulloch RI, Fitzpatrick PF. </i> Arch Biochem Biophys, 1999","reference_id":"10375411","region_id":"DP00094r007","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"From residue 33 to residue 50 of tyrosine hydroxylase, the sequence is RFIGRRQSLIEDARKERE. All of the observed cleavage sites are within this region, occurring after arginines 33, 37, 38, and 49.","_id":"685af523b4ac24d5329d776f"},{"type":"Article","text":"When combined with the kinetics of digestion, the sequencing results establish that the conformation of the region from residue 33 to residue 50 in tyrosine hydroxylase is sensitive to the phosphorylation state and to dopamine binding. Phosphorylation of serine 40 by protein kinase A renders this region more susceptible to proteolysis, consistent with a more exposed conformation, whereas this region becomes less accessible when dopamine is bound.","_id":"685af523b4ac24d5329d7770"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d776e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":33,"end":50,"interaction_partner":[],"reference_html":"Limited proteolysis of tyrosine hydroxylase identifies residues 33-50 as conformationally sensitive to phosphorylation state and dopamine binding. <i> McCulloch RI, Fitzpatrick PF. </i> Arch Biochem Biophys, 1999","reference_id":"10375411","region_id":"DP00094r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"When combined with the kinetics of digestion, the sequencing results establish that the conformation of the region from residue 33 to residue 50 in tyrosine hydroxylase is sensitive to the phosphorylation state and to dopamine binding. Phosphorylation of serine 40 by protein kinase A renders this region more susceptible to proteolysis, consistent with a more exposed conformation, whereas this region becomes less accessible when dopamine is bound.","_id":"685af523b4ac24d5329d7772"}],"states_connection":[],"term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d7771","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":33,"end":50,"interaction_partner":[{"db":"ChEBI","id":"18243","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7778"}],"reference_html":"Limited proteolysis of tyrosine hydroxylase identifies residues 33-50 as conformationally sensitive to phosphorylation state and dopamine binding. <i> McCulloch RI, Fitzpatrick PF. </i> Arch Biochem Biophys, 1999","reference_id":"10375411","region_id":"DP00094r011","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"When combined with the kinetics of digestion, the sequencing results establish that the conformation of the region from residue 33 to residue 50 in tyrosine hydroxylase is sensitive to the phosphorylation state and to dopamine binding. Phosphorylation of serine 40 by protein kinase A renders this region more susceptible to proteolysis, consistent with a more exposed conformation, whereas this region becomes less accessible when dopamine is bound.","_id":"685af523b4ac24d5329d7779"}],"states_connection":[],"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","term_id":"GO:0036094","term_is_binding":true,"term_is_obsolete":false,"term_name":"small molecule binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","version":4,"_id":"685af523b4ac24d5329d7777","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-22T09:58:28.631Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":72,"interaction_partner":[],"reference_html":"The solution structure of the regulatory domain of tyrosine hydroxylase. <i> Zhang S, Huang T, Ilangovan U, Hinck AP, Fitzpatrick PF. </i> J Mol Biol, 2014","reference_id":"24361276","region_id":"DP00094r024","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The backbone resonances of the N-terminal 70 residues of RDTyrH could be assigned using sensitivity-enhanced TROSY-based HNCACB, HN(CO)CACB, HNCA and HN(CO)CA triple-resonance experiments,22; 23 with the exception of the amide resonances of Met1, Pro11, Lys12, Gln39, Ser40, Leu41, and Pro68.","_id":"685af523b4ac24d5329d7793"},{"type":"Results","text":"This indicated that RDTyrH is composed of a largely unstructured N-terminal region (residues 1-72) and a more ordered and well-folded C-terminal portion (residues 73-159).","_id":"685af523b4ac24d5329d7794"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":0,"_id":"685af523b4ac24d5329d7792","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2MDA","_id":"685af523b4ac24d5329d7796"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-22T09:59:36.927Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":85,"end":96,"interaction_partner":[],"reference_html":"The solution structure of the regulatory domain of tyrosine hydroxylase. <i> Zhang S, Huang T, Ilangovan U, Hinck AP, Fitzpatrick PF. </i> J Mol Biol, 2014","reference_id":"24361276","region_id":"DP00094r025","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"There are two highly flexible loop regions, L2 (residues 85-96) and L4 (residues 119-130).","_id":"685af523b4ac24d5329d7797"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":0,"_id":"685af523b4ac24d5329d7795","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2MDA","_id":"685af523b4ac24d5329d7799"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-22T09:59:45.812Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":119,"end":130,"interaction_partner":[],"reference_html":"The solution structure of the regulatory domain of tyrosine hydroxylase. <i> Zhang S, Huang T, Ilangovan U, Hinck AP, Fitzpatrick PF. </i> J Mol Biol, 2014","reference_id":"24361276","region_id":"DP00094r026","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"There are two highly flexible loop regions, L2 (residues 85-96) and L4 (residues 119-130).","_id":"685af523b4ac24d5329d779a"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":0,"_id":"685af523b4ac24d5329d7798","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-22T10:01:39.373Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":38,"end":42,"interaction_partner":[],"reference_html":"The solution structure of the regulatory domain of tyrosine hydroxylase. <i> Zhang S, Huang T, Ilangovan U, Hinck AP, Fitzpatrick PF. </i> J Mol Biol, 2014","reference_id":"24361276","region_id":"DP00094r027","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"TyrH is phosphorylated at Ser40 by protein kinase A.","_id":"685af523b4ac24d5329d779c"},{"type":"Results","text":"The backbone assignments of phosphorylated RDTyrH could be made using the same methods as for RDTyrH; these included Ser40 and the adjacent Gln39 and Leu41. All the assigned residues retain the same chemical shifts as in RDTyrH except for Gly36, Arg37, Gln39, Ser40, Leu41, Ile42, and Glu43. This suggests that after phosphorylation the core structure of RDTyrH remains the same as that in unphosphorylated RDTyrH, and a local structural change takes place around Ser40.","_id":"685af523b4ac24d5329d779d"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":0,"_id":"685af523b4ac24d5329d779b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":40,"end":40,"statements":[{"type":"Methods","text":"The preparation of TyrH stoichiometrically phosphorylated at Ser 40 was performed as previously described (41) with minor modifications.","_id":"685af523b4ac24d5329d77a0"}],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d779f"}],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-22T10:12:43.296Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006236","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","ec_ontology":"ECO","start":28,"end":71,"interaction_partner":[],"reference_html":"Identification by hydrogen/deuterium exchange of structural changes in tyrosine hydroxylase associated with regulation. <i> Wang S, Sura GR, Dangott LJ, Fitzpatrick PF. </i> Biochemistry, 2009","reference_id":"19371093","region_id":"DP00094r028","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The most N-terminal peptides, illustrated in Figure 2A by residues 28-34, exhibit complete exchange after only 7 s, the earliest time point used here. This suggests that the very N-terminus of the protein is highly dynamic.","_id":"685af523b4ac24d5329d77a1"},{"type":"Results","text":"The three peptides covering residues 28-71 of the regulatory domain exhibit complete exchange in less than 7 s, illustrating that this portion of the protein is highly mobile.","_id":"685af523b4ac24d5329d77a2"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":0,"_id":"685af523b4ac24d5329d779e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":40,"end":40,"statements":[{"type":"Methods","text":"The preparation of TyrH stoichiometrically phosphorylated at Ser 40 was performed as previously described (41) with minor modifications.","_id":"685af523b4ac24d5329d77a5"}],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d77a4"}],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006236","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","ec_ontology":"ECO","start":42,"end":71,"interaction_partner":[{"db":"ChEBI","id":"18243","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d77a6"}],"reference_html":"Identification by hydrogen/deuterium exchange of structural changes in tyrosine hydroxylase associated with regulation. <i> Wang S, Sura GR, Dangott LJ, Fitzpatrick PF. </i> Biochemistry, 2009","reference_id":"19371093","region_id":"DP00094r029","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Three peptides (35-41, 42-71, 295-299) show dramatic decreases in the rates of deuterium incorporation when dopamine is bound (Figure 4). The first two fragments are on the regulatory domain and show complete exchange within 7 s in the absence of dopamine.","_id":"685af523b4ac24d5329d77a7"}],"states_connection":[],"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","term_go_domain":"F","term_id":"GO:0036094","term_is_binding":true,"term_is_obsolete":false,"term_name":"small molecule binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":1,"_id":"685af523b4ac24d5329d77a3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"There are three tryptophan residues in TyrH, at positions 166, 233 and 372. Mutation of all three to phenylalanine yields a tryptophan-free enzyme (F3 TyrH) with wild-type enzyme activity (13).","_id":"685af523b4ac24d5329d77aa"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp166Phe","_id":"685af523b4ac24d5329d77a9"},{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"There are three tryptophan residues in TyrH, at positions 166, 233 and 372. Mutation of all three to phenylalanine yields a tryptophan-free enzyme (F3 TyrH) with wild-type enzyme activity (13).","_id":"685af523b4ac24d5329d77ac"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp233Phe","_id":"685af523b4ac24d5329d77ab"},{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"There are three tryptophan residues in TyrH, at positions 166, 233 and 372. Mutation of all three to phenylalanine yields a tryptophan-free enzyme (F3 TyrH) with wild-type enzyme activity (13).","_id":"685af523b4ac24d5329d77ae"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp372Phe","_id":"685af523b4ac24d5329d77ad"},{"start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The introduction of a single tryptophan at position 14, 34 or 74 was performed by QuikChange site-directed mutagenesis (Stratagene).","_id":"685af523b4ac24d5329d77b0"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe14Trp","_id":"685af523b4ac24d5329d77af"},{"start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The introduction of a single tryptophan at position 14, 34 or 74 was performed by QuikChange site-directed mutagenesis (Stratagene).","_id":"685af523b4ac24d5329d77b2"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe34Trp","_id":"685af523b4ac24d5329d77b1"},{"start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The introduction of a single tryptophan at position 14, 34 or 74 was performed by QuikChange site-directed mutagenesis (Stratagene).","_id":"685af523b4ac24d5329d77b4"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe74Trp","_id":"685af523b4ac24d5329d77b3"},{"start":40,"end":40,"statements":[{"type":"Methods","text":"Stoichiometric phosphorylation of TyrH by protein kinase A and purification of the phosphorylated enzymes were performed as previously described (6, 12).","_id":"685af523b4ac24d5329d77b6"}],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d77b5"}],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-22T10:27:54.245Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0005632","ec_name":"fluorescence anisotropy evidence used in manual assertion","ec_ontology":"ECO","start":14,"end":34,"interaction_partner":[],"reference_html":"Fluorescence spectroscopy as a probe of the effect of phosphorylation at serine 40 of tyrosine hydroxylase on the conformation of its regulatory domain. <i> Wang S, Lasagna M, Daubner SC, Reinhart GD, Fitzpatrick PF. </i> Biochemistry, 2011","reference_id":"21302933","region_id":"DP00094r030","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"This is consistent with increased flexibility at of the side chains at positions 14 and 34, with the largest effect on the residue closer to the phosphorylation site.","_id":"685af523b4ac24d5329d77b7"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":0,"_id":"685af523b4ac24d5329d77a8","reference_source":"pmid"}],"__v":0,"disorder_content":0.1927710843373494,"disprot_consensus":{"full":[{"start":1,"end":72,"type":"D"},{"start":85,"end":96,"type":"D"},{"start":119,"end":130,"type":"D"}],"Structural state":[{"start":1,"end":72,"type":"D"},{"start":85,"end":96,"type":"D"},{"start":119,"end":130,"type":"D"}],"Disorder function":[{"start":33,"end":50,"type":"F"}],"Molecular function":[{"start":33,"end":71,"type":"F"}]}},{"features":{"pfam":[{"id":"PF21948","name":"Lipoyl protein ligase A/B catalytic domain","start":15,"end":218}],"gene3D":[{"start":1,"end":262,"id":"3.30.930.10","name":"Bira Bifunctional Protein; Domain 2"}]},"uniref50":"UniRef50_Q9HKT1","sequence":"MEGRLLLLETPGNTRMSLAYDEAIYRSFQYGDKPILRFYRHDRSVIIGYFQVAEEEVDLDYMKKNGIMLARRYTGGGAVYHDLGDLNFSVVRSSDDMDITSMFRTMNEAVVNSLRILGLDARPGELNDVSIPVNKKTDIMAGEKKIMGAAGAMRKGAKLWHAAMLVHTDLDMLSAVLKVPDEKFRDKIAKSTRERVANVTDFVDVSIDEVRNALIRGFSETLHIDFREDTITEKEESLARELFDKKYSTEEWNMGLLRKEVV","taxonomy":["Archaea","Candidatus Thermoplasmatota","Thermoplasmata","Thermoplasmatales","Thermoplasmataceae","Thermoplasma"],"uniref90":"UniRef90_Q9HKT1","disprot_id":"DP00096","ncbi_taxon_id":273075,"regions_counter":4,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":193,"region_id":"DP00096r001","reference_id":"16384580","start":179,"ec_id":"ECO:0007691","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"A second loop comprising residues 179-193 was disordered in the T.acidophilum structure; tryptic cleavage of the corresponding loop in the E.coli LplA under non-denaturing conditions rendered the enzyme catalytically inactive, emphasizing its importance.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cleavage assay evidence used in manual assertion","version":4,"reference_html":"Structure of a putative lipoate protein ligase from Thermoplasma acidophilum and the mechanism of target selection for post-translational modification. <i> McManus E, Luisi BF, Perham RN. </i> J Mol Biol, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","cross_refs":[{"db":"PDB","id":"2C8M"}],"term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":193,"region_id":"DP00096r003","reference_id":"16384580","start":179,"ec_id":"ECO:0006220","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"A second loop comprising residues 179-193 was disordered in the T.acidophilum structure; tryptic cleavage of the corresponding loop in the E.coli LplA under non-denaturing conditions rendered the enzyme catalytically inactive, emphasizing its importance.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"Structure of a putative lipoate protein ligase from Thermoplasma acidophilum and the mechanism of target selection for post-translational modification. <i> McManus E, Luisi BF, Perham RN. </i> J Mol Biol, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","cross_refs":[{"db":"PDB","id":"2C8M"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q9HKT1","date":"2016-08-11T15:05:56.000Z","acc":"Q9HKT1","name":"Lipoate-protein ligase A subunit 1","length":262,"organism":"Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)","dataset":[],"UniParc":"UPI000012E6FE","genes":[{"name":{"value":"lplA"},"olnNames":[{"value":"Ta0514"}]}],"alphafold_very_low_content":0.04961832061068702,"disorder_content":0.05725190839694656,"disprot_consensus":{"full":[{"start":179,"end":193,"type":"D"}],"Structural state":[{"start":179,"end":193,"type":"D"}]}},{"acc":"P10922","sequence":"MTENSTSAPAAKPKRAKASKKSTDHPKYSDMIVAAIQAEKNRAGSSRQSIQKYIKSHYKVGENADSQIKLSIKRLVTTGVLKQTKGVGASGSFRLAKGDEPKRSVAFKKTKKEVKKVATPKKAAKPKKAASKAPSKKPKATPVKKAKKKPAATPKKAKKPKVVKVKPVKASKPKKAKTVKPKAKSSAKRASKKK","alphafold_very_low_content":"0.18556701030927836","creator":"gminervini","dataset":[],"date":"2016-08-23T15:26:38.000Z","disprot_id":"DP00097","features":{"pfam":[{"id":"PF00538","name":"linker histone H1 and H5 family","start":25,"end":96}],"gene3D":[{"start":19,"end":109,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain","_id":"685af523b4ac24d5329d77bb"}]},"genes":[{"name":{"value":"H1-0","evidences":[],"_id":"685af523b4ac24d5329d780c"},"synonyms":[{"value":"H1f0","evidences":[],"_id":"685af523b4ac24d5329d780d"},{"value":"H1fv","evidences":[],"_id":"685af523b4ac24d5329d780e"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d780b"}],"length":194,"name":"Histone H1.0","ncbi_taxon_id":10090,"organism":"Mus musculus","regions_counter":29,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"UniParc":"UPI0000163839","uniref100":"UniRef100_P10922","uniref50":"UniRef50_P07305","uniref90":"UniRef90_P07305","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-22T11:04:00.544Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":31,"interaction_partner":[],"reference_html":"DNA-induced alpha-helical structure in the NH2-terminal domain of histone H1. <i> Vila R, Ponte I, Collado M, Arrondo JL, Jiménez MA, Rico M, Suau P. </i> J Biol Chem, 2001","reference_id":"11584004","region_id":"DP00097r021","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The CD spectrum of both peptides in H2O was dominated by the contribution of the random coil. The mean residue molar ellipticity at 222 nm ([θ]222), taken as criterion of helix formation, was negligible in water. However, the small positive peak at 215 nm, characteristic of the random coil, was not observed, suggesting that a small amount of structure could be present in water (Fig.1).","_id":"685af523b4ac24d5329d77e5"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-05-08T19:49:49.970Z","_id":"685af523b4ac24d5329d77e6"},"version":0,"_id":"685af523b4ac24d5329d77e4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-22T11:14:19.094Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006228","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":31,"interaction_partner":[],"reference_html":"DNA-induced alpha-helical structure in the NH2-terminal domain of histone H1. <i> Vila R, Ponte I, Collado M, Arrondo JL, Jiménez MA, Rico M, Suau P. </i> J Biol Chem, 2001","reference_id":"11584004","region_id":"DP00097r024","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In aqueous (D2O) solution, the amide I′ of both NH-1 and NH-2 was dominated by the random coil band at 1641 cm−1(representing 42% of the total amide I′ intensity in NH-1 and 44% in NH-2) (30).","_id":"685af523b4ac24d5329d77f1"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-05-08T19:49:47.058Z","_id":"685af523b4ac24d5329d77f2"},"version":0,"_id":"685af523b4ac24d5329d77f0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006228","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":31,"interaction_partner":[],"reference_html":"DNA-induced alpha-helical structure in the NH2-terminal domain of histone H1. <i> Vila R, Ponte I, Collado M, Arrondo JL, Jiménez MA, Rico M, Suau P. </i> J Biol Chem, 2001","reference_id":"11584004","region_id":"DP00097r026","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As the percentage of α-helix in aqueous solution was only 6–8%, these results indicate that interaction with the DNA stabilizes the helical structure of the peptides. The amounts of helical structure observed in the complexes with the DNA are similar to those observed in TFE solution, by both IR and CD.","_id":"685af523b4ac24d5329d77fa"}],"states_connection":[],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_go_domain":"F","term_id":"GO:0003677","term_is_binding":true,"term_is_obsolete":false,"term_name":"DNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-05-08T19:50:04.909Z","_id":"685af523b4ac24d5329d77fb"},"version":1,"_id":"685af523b4ac24d5329d77f9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Results","text":"This construct, denoted as C-H1.0, corresponds to residues 98–193 of mouse histone H1.0 (Fig. 1a), and contains an additional N-terminal Met residue, two extra amino acids added by the restriction enzyme used for cloning, and a C-terminal 6xHis-tag, which are required for expression and purification of the protein.","_id":"685af523b4ac24d5329d77fe"}],"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","_id":"685af523b4ac24d5329d77fd"}],"cross_refs":[{"db":"BMRB","id":"27537","_id":"685af523b4ac24d5329d77ff"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-05-08T19:37:48.070Z","disprot_namespace":"Structural state","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":93,"end":194,"interaction_partner":[],"reference_html":"A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study. <i> Chaves-Arquero B, Pantoja-Uceda D, Roque A, Ponte I, Suau P, Jiménez MA. </i> J Biomol NMR, 2018","reference_id":"30414042","region_id":"DP00097r027","released":"2023_06","sample":[],"sequence_construct":"MDEPKRSVAFKKTKKEVKKVATPKKAAKPKKAASKAPSKKPKATPVKKAKKKPAATPKKAKKPKVVKVKPVKASKPKKAK TVKPKAKSSAKRASKKKRSHHHHHH","statement":[{"type":"Results","text":"Furthermore, C-H1.0 is an intrinsically disorder protein, which shows very little dispersion in the 1HN nuclei; all amide protons appear in 0.51 ppm (Fig. 1c).","_id":"685af523b4ac24d5329d7800"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d77fc","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Results","text":"This construct, denoted as C-H1.0, corresponds to residues 98–193 of mouse histone H1.0 (Fig. 1a), and contains an additional N-terminal Met residue, two extra amino acids added by the restriction enzyme used for cloning, and a C-terminal 6xHis-tag, which are required for expression and purification of the protein.","_id":"685af523b4ac24d5329d7803"}],"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","_id":"685af523b4ac24d5329d7802"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-05-08T19:42:25.153Z","disprot_namespace":"Structural state","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":93,"end":194,"interaction_partner":[],"reference_html":"A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study. <i> Chaves-Arquero B, Pantoja-Uceda D, Roque A, Ponte I, Suau P, Jiménez MA. </i> J Biomol NMR, 2018","reference_id":"30414042","region_id":"DP00097r028","released":"2023_06","sample":[],"sequence_construct":"MDEPKRSVAFKKTKKEVKKVATPKKAAKPKKAASKAPSKKPKATPVKKAKKKPAATPKKAKKPKVVKVKPVKASKPKKAK TVKPKAKSSAKRASKKKRSHHHHHH","statement":[{"type":"Results","text":"Circular dichroism (CD) data of C-H1.0 and pT-C-H1.0 also indicate that phosphorylation does not induce any conformational change (see Suppl. Fig. S2).","_id":"685af523b4ac24d5329d7804"},{"type":"Curator statement","text":"Fig. S2 shows this region is intrinsically unstructured by its large negative ellipticity at 200 nm and moderate ellipticity at 190 nm.","_id":"685af523b4ac24d5329d7805"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d7801","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Results","text":"This construct, denoted as C-H1.0, corresponds to residues 98–193 of mouse histone H1.0 (Fig. 1a), and contains an additional N-terminal Met residue, two extra amino acids added by the restriction enzyme used for cloning, and a C-terminal 6xHis-tag, which are required for expression and purification of the protein.","_id":"685af523b4ac24d5329d7808"}],"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","_id":"685af523b4ac24d5329d7807"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-05-08T19:49:01.482Z","disprot_namespace":"Disorder function","ec_id":"ECO:0001230","ec_name":"mass spectrometry evidence used in manual assertion","ec_ontology":"ECO","start":21,"end":25,"interaction_partner":[],"reference_html":"A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study. <i> Chaves-Arquero B, Pantoja-Uceda D, Roque A, Ponte I, Suau P, Jiménez MA. </i> J Biomol NMR, 2018","reference_id":"30414042","region_id":"DP00097r029","released":"2023_06","sample":[],"sequence_construct":"MDEPKRSVAFKKTKKEVKKVATPKKAAKPKKAASKAPSKKPKATPVKKAKKKPAATPKKAKKPKVVKVKPVKASKPKKAK TVKPKAKSSAKRASKKKRSHHHHHH","statement":[{"type":"Methods","text":"The extent of phosphorylation was evaluated by MALDI-TOF mass spectrometry.","_id":"685af523b4ac24d5329d7809"},{"type":"Results","text":"Therefore, we proceeded to acquire NMR spectra of pT-C-H1.0, in which the Thr residues of the three phosphorylation-motifs present in its sequence (22TPKK25, 44TPVK47, and 56TPKK59; Fig. 1a) are phosphorylated. ","_id":"685af523b4ac24d5329d780a"}],"states_connection":[],"term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d7806","reference_source":"pmid"}],"__v":0,"disorder_content":0.6804123711340206,"disprot_consensus":{"full":[{"start":2,"end":31,"type":"D"},{"start":93,"end":194,"type":"D"}],"Structural state":[{"start":2,"end":31,"type":"D"},{"start":93,"end":194,"type":"D"}],"Molecular function":[{"start":2,"end":31,"type":"F"}],"Disorder function":[{"start":21,"end":25,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05737","name":"Collagen binding domain","start":174,"end":296},{"id":"PF05738","name":"Cna protein B-type domain","start":435,"end":528},{"id":"PF05738","name":"Cna protein B-type domain","start":537,"end":619},{"id":"PF05738","name":"Cna protein B-type domain","start":628,"end":716},{"id":"PF05738","name":"Cna protein B-type domain","start":724,"end":806},{"id":"PF05738","name":"Cna protein B-type domain","start":815,"end":903},{"id":"PF05738","name":"Cna protein B-type domain","start":911,"end":993},{"id":"PF05738","name":"Cna protein B-type domain","start":1002,"end":1090},{"id":"PF17802","name":"Prealbumin-like fold domain","start":331,"end":422}],"gene3D":[{"start":23,"end":164,"id":"2.60.40.1280","name":"2.60.40.1280"},{"start":333,"end":432,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":814,"end":906,"id":"2.60.40.1140","name":"Collagen-binding surface protein Cna, B-type domain"},{"start":1001,"end":1093,"id":"2.60.40.1140","name":"Collagen-binding surface protein Cna, B-type domain"},{"start":907,"end":1000,"id":"2.60.40.1140","name":"Collagen-binding surface protein Cna, B-type domain"},{"start":165,"end":332,"id":"2.60.40.740","name":"2.60.40.740"},{"start":433,"end":534,"id":"2.60.40.1140","name":"Collagen-binding surface protein Cna, B-type domain"},{"start":720,"end":813,"id":"2.60.40.1140","name":"Collagen-binding surface protein Cna, B-type domain"},{"start":535,"end":626,"id":"2.60.40.1140","name":"Collagen-binding surface protein Cna, B-type domain"},{"start":627,"end":719,"id":"2.60.40.1140","name":"Collagen-binding surface protein Cna, B-type domain"}]},"uniref50":"UniRef50_Q53654","sequence":"MNKNVLKFMVFIMLLNIITPLFNKNEAFAARDISSTNVTDLTVSPSKIEDGGKTTVKMTFDDKNGKIQNGDMIKVAWPTSGTVKIEGYSKTVPLTVKGEQVGQAVITPDGATITFNDKVEKLSDVSGFAEFEVQGRNLTQTNTSDDKVATITSGNKSTNVTVHKSEAGTSSVFYYKTGDMLPEDTTHVRWFLNINNEKSYVSKDITIKDQIQGGQQLDLSTLNINVTGTHSNYYSGQSAITDFEKAFPGSKITVDNTKNTIDVTIPQGYGSYNSFSINYKTKITNEQQKEFVNNSQAWYQEHGKEEVNGKSFNHTVHNINANAGIEGTVKGELKVLKQDKDTKAPIANVKFKLSKKDGSVVKDNQKEIEIITDANGIANIKALPSGDYILKEIEAPRPYTFDKDKEYPFTMKDTDNQGYFTTIENAKAIEKTKDVSAQKVWEGTQKVKPTIYFKLYKQDDNQNTTPVDKAEIKKLEDGTTKVTWSNLPENDKNGKAIKYLVKEVNAQGEDTTPEGYTKKENGLVVTNTEKPIETTSISGEKVWDDKDNQDGKRPEKVSVNLLANGEKVKTLDVTSETNWKYEFKDLPKYDEGKKIEYTVTEDHVKDYTTDINGTTITNKYTPGETSATVTKNWDDNNNQDGKRPTEIKVELYQDGKATGKTAILNESNNWTHTWTGLDEKAKGQQVKYTVEELTKVKGYTTHVDNNDMGNLIVTNKYTPETTSISGEKVWDDKDNQDGKRPEKVSVNLLADGEKVKTLDVTSETNWKYEFKDLPKYDEGKKIEYTVTEDHVKDYTTDINGTTITNKYTPGETSATVTKNWDDNNNQDGKRPTEIKVELYQDGKATGKTAILNESNNWTHTWTGLDEKAKGQQVKYTVEELTKVKGYTTHVDNNDMGNLIVTNKYTPETTSISGEKVWDDKDNQDGKRPEKVSVNLLANGEKVKTLDVTSETNWKYEFKDLPKYDEGKKIEYTVTEDHVKDYTTDINGTTITNKYTPGETSATVTKNWDDNNNQDGKRPTEIKVELYQDGKATGKTAILNESNNWTHTWTGLDEKAKGQQVKYTVDELTKVNGYTTHVDNNDMGNLIVTNKYTPKKPNKPIYPEKPKDKTPPTKPDHSNKVKPTPPDKPSKVDKDDQPKDNKTKPENPLKELPKTGMKIITSWITWVFIGILGLYLILRKRFNS","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Staphylococcaceae","Staphylococcus"],"uniref90":"UniRef90_Q53654","disprot_id":"DP00098","ncbi_taxon_id":1280,"regions_counter":4,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":344,"region_id":"DP00098r001","released":"2023_06","ec_id":"ECO:0006220","reference_html":"A 'Collagen Hug' model for Staphylococcus aureus CNA binding to collagen. <i> Zong Y, Xu Y, Liang X, Keene DR, Höök A, Gurusiddappa S, Höök M, Narayana SV. </i> EMBO J, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":332,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16362049","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-01-17T16:40:33.785Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The N2 domain ends at residue 318 and the C-terminal extension of this domain (residues 319–329) stretches towards the N1 domain and forms a β strand (G′) that complements one of the β-sheets of the N1 domain (Figure 3A), while the following residues 332–344 are disordered and extend into the solvent region.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"2F68"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:38:34.126Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":173,"region_id":"DP00098r003","released":"2023_06","ec_id":"ECO:0005670","reference_html":"A 'Collagen Hug' model for Staphylococcus aureus CNA binding to collagen. <i> Zong Y, Xu Y, Liang X, Keene DR, Höök A, Gurusiddappa S, Höök M, Narayana SV. </i> EMBO J, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":164,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16362049","version":3,"ec_name":"x-ray crystallography evidence used in manual assertion","date":"2023-01-17T16:39:51.879Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2F68"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The electron density for the main chain atoms of the 164–173 linker is poorly defined suggesting some flexibility in this linker segment.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:38:41.266Z"}},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":173,"term_name":"flexible linker","start":164,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16362049","version":4,"reference_html":"A 'Collagen Hug' model for Staphylococcus aureus CNA binding to collagen. <i> Zong Y, Xu Y, Liang X, Keene DR, Höök A, Gurusiddappa S, Höök M, Narayana SV. </i> EMBO J, 2005","date":"2023-01-17T16:40:50.171Z","term_id":"IDPO:0000033","ec_id":"ECO:0006220","region_id":"DP00098r004","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Disorder function","cross_refs":[{"db":"PDB","id":"2F68"}],"statement":[{"text":"The electron density for the main chain atoms of the 164–173 linker is poorly defined suggesting some flexibility in this linker segment.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:38:42.745Z"}}],"released":"2016_10","uniref100":"UniRef100_Q53654","date":"2016-09-08T11:37:46.000Z","acc":"Q53654","name":"Collagen adhesin","length":1183,"organism":"Staphylococcus aureus","dataset":["Bacterial virulence-related proteins"],"UniParc":"UPI0000127C08","genes":[{"name":{"value":"cna"}}],"alphafold_very_low_content":0.0989010989010989,"disorder_content":0.01944209636517329,"disprot_consensus":{"full":[{"start":164,"end":173,"type":"D"},{"start":332,"end":344,"type":"D"}],"Structural state":[{"start":164,"end":173,"type":"D"},{"start":332,"end":344,"type":"D"}],"Disorder function":[{"start":164,"end":173,"type":"F"}]}},{"features":{"gene3D":[{"start":64,"end":423,"id":"3.75.10.10","name":"L-arginine/glycine Amidinotransferase; Chain A"}],"pfam":[]},"uniref50":"UniRef50_P50440","sequence":"MLRVRCLRGGSRGAEAVHYIGSRLGRTLTGWVQRTFQSTQAATASSRNSCAADDKATEPLPKDCPVSSYNEWDPLEEVIVGRAENACVPPFTIEVKANTYEKYWPFYQKQGGHYFPKDHLKKAVAEIEEMCNILKTEGVTVRRPDPIDWSLKYKTPDFESTGLYSAMPRDILIVVGNEIIEAPMAWRSRFFEYRAYRSIIKDYFHRGAKWTTAPKPTMADELYNQDYPIHSVEDRHKLAAQGKFVTTEFEPCFDAADFIRAGRDIFAQRSQVTNYLGIEWMRRHLAPDYRVHIISFKDPNPMHIDATFNIIGPGIVLSNPDRPCHQIDLFKKAGWTIITPPTPIIPDDHPLWMSSKWLSMNVLMLDEKRVMVDANEVPIQKMFEKLGITTIKVNIRNANSLGGGFHCWTCDVRRRGTLQSYLD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P50440","disprot_id":"DP00099","ncbi_taxon_id":9606,"regions_counter":1,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":63,"region_id":"DP00099r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis. <i> Humm A, Fritsche E, Steinbacher S, Huber R. </i> EMBO J, 1997","term_id":"IDPO:0000002","curator_id":"esalladini","start":38,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"9218780","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","cross_refs":[{"db":"PDB","id":"1JDW"},{"db":"PDB","id":"4JDW"},{"db":"PDB","id":"2JDW"},{"db":"PDB","id":"3JDW"}],"statement":[{"text":"Residues 38–63 as well as the 14 amino acid fusion peptide that had been cloned to the N-terminus of the protein for affinity purification are not visible in the electron density map and are mobile or disordered.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T17:52:10.314Z"}}],"released":"2016_10","uniref100":"UniRef100_P50440","date":"2016-08-24T14:18:52.000Z","acc":"P50440","name":"Glycine amidinotransferase, mitochondrial","length":423,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI0000111EFD","genes":[{"name":{"value":"GATM"},"synonyms":[{"value":"AGAT"}]}],"alphafold_very_low_content":0.13238770685579196,"disorder_content":0.061465721040189124,"disprot_consensus":{"full":[{"start":38,"end":63,"type":"D"}],"Structural state":[{"start":38,"end":63,"type":"D"}]}},{"acc":"P0A6H5","sequence":"MSEMTPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLNEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYVGKEVDSIIRDLTDAAVKMVRVQAIEKNRYRAEELAEERILDVLIPPAKNNWGQTEQQQEPSAARQAFRKKLREGQLDDKEIEIDLAAAPMGVEIMAPPGMEEMTSQLQSMFQNLGGQKQKARKLKIKDAMKLLIEEEAAKLVNPEELKQDAIDAVEQHGIVFIDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGAFQIAKPSDLIPELQGRLPIRVELQALTTSDFERILTEPNASITVQYKALMATEGVNIEFTDSGIKRIAEAAWQVNESTENIGARRLHTVLERLMEEISYDASDLSGQNITIDADYVSKHLDALVADEDLSRFIL","alphafold_very_low_content":"0.009029345372460496","creator":"mnecci","dataset":["Stress response proteins"],"date":"2016-09-12T09:18:44.000Z","disprot_id":"DP00100","features":{"pfam":[{"id":"PF00004","name":"ATPase family associated with various cellular activities (AAA)","start":53,"end":105},{"id":"PF07724","name":"AAA domain (Cdc48 subfamily)","start":187,"end":329}],"gene3D":[{"start":335,"end":440,"id":"1.10.8.60","name":"1.10.8.60","_id":"685af523b4ac24d5329d7812"}]},"genes":[{"name":{"value":"hslU","evidences":[],"_id":"685af523b4ac24d5329d7823"},"synonyms":[{"value":"htpI","evidences":[],"_id":"685af523b4ac24d5329d7824"}],"olnNames":[{"value":"b3931","evidences":[],"_id":"685af523b4ac24d5329d7825"},{"value":"JW3902","evidences":[],"_id":"685af523b4ac24d5329d7826"}],"orfNames":[],"_id":"685af523b4ac24d5329d7822"}],"length":443,"name":"ATP-dependent protease ATPase subunit HslU","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions_counter":5,"released":"2016_10","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"UniParc":"UPI0000112FF5","uniref100":"UniRef100_P0A6H6","uniref50":"UniRef50_P0A6H6","uniref90":"UniRef90_P0A6H6","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1DO0","_id":"685af523b4ac24d5329d7814"},{"db":"PDB","id":"1DO2","_id":"685af523b4ac24d5329d7815"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":175,"end":209,"interaction_partner":[],"reference_html":"The structures of HsIU and the ATP-dependent protease HsIU-HsIV. <i> Bochtler M, Hartmann C, Song HK, Bourenkov GP, Bartunik HD, Huber R. </i> Nature, 2000","reference_id":"10693812","region_id":"DP00100r001","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"Their entirely disordered segment I175–Q209 may act as a bait and/or an adaptor to substrate molecules and promote binding.","_id":"685af523b4ac24d5329d7816"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d7813","reference_source":"pmid","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-01T17:09:38.191Z"}}],"__v":0,"disorder_content":0.07900677200902935,"disprot_consensus":{"full":[{"start":175,"end":209,"type":"D"}],"Structural state":[{"start":175,"end":209,"type":"D"}]}},{"acc":"P12493","sequence":"MGARASVLSGGELDKWEKIRLRPGGKKQYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTIAVLYCVHQRIDVKDTKEALDKIEEEQNKSKKKAQQAAADTGNNSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTHNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPGATLEEMMTACQGVGGPGHKARVLAEAMSQVTNPATIMIQKGNFRNQRKTVKCFNCGKEGHIAKNCRAPRKKGCWKCGKEGHQMKDCTERQANFLGKIWPSHKGRPGNFLQSRPEPTAPPEESFRFGEETTTPSQKQEPIDKELYPLASLRSLFGSDPSSQ","creator":"fquaglia","dataset":["Viral proteins","RNA-binding proteins"],"date":"2016-08-23T16:48:08.000Z","disprot_id":"DP00101","features":{"pfam":[{"id":"PF00098","name":"Zinc knuckle","start":391,"end":406},{"id":"PF00098","name":"Zinc knuckle","start":412,"end":428},{"id":"PF00540","name":"gag gene protein p17 (matrix protein)","start":2,"end":132},{"id":"PF00607","name":"gag protein p24 N-terminal domain","start":144,"end":252},{"id":"PF08705","name":"Gag protein p6","start":449,"end":486},{"id":"PF19317","name":"Gag protein p24 C-terminal domain","start":276,"end":349}],"gene3D":[{"start":283,"end":347,"id":"1.10.1200.30","name":"1.10.1200.30","_id":"685af523b4ac24d5329d782c"},{"start":1,"end":132,"id":"1.10.150.90","name":"Immunodeficiency lentiviruses, gag gene matrix protein p17","_id":"685af523b4ac24d5329d782d"},{"start":133,"end":278,"id":"1.10.375.10","name":"Human Immunodeficiency Virus Type 1 Capsid Protein","_id":"685af523b4ac24d5329d782e"},{"start":348,"end":387,"id":"1.20.5.760","name":"Single helix bin","_id":"685af523b4ac24d5329d782f"},{"start":388,"end":431,"id":"4.10.60.10","name":"Zinc finger, CCHC-type","_id":"685af523b4ac24d5329d7830"}]},"genes":[{"name":{"value":"gag","evidences":[],"_id":"685af523b4ac24d5329d784f"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d784e"}],"length":500,"name":"Gag polyprotein","ncbi_taxon_id":11698,"organism":"Human immunodeficiency virus type 1 group M subtype B (isolate NY5)","regions_counter":10,"released":"2016_10","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"UniParc":"UPI000011F382","uniref100":"UniRef100_P12493","uniref50":"UniRef50_P12493","uniref90":"UniRef90_P12493","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2C55","_id":"685af523b4ac24d5329d7845"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":467,"end":480,"interaction_partner":[],"reference_html":"Solution structure of the human immunodeficiency virus type 1 p6 protein. <i> Fossen T, Wray V, Bruns K, Rachmat J, Henklein P, Tessmer U, Maczurek A, Klinger P, Schubert U. </i> J Biol Chem, 2005","reference_id":"16234236","region_id":"DP00101r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The quantitative NOE data for full-length sp6-(1–52) allow the definition of two α-helical structured regions extending from Ser-14 to Gly-18 and from Lys-33 to Ser-43 (Fig. 8, A and B, respectively), connected by a more flexible region that allows orientational freedom of the two helices.","_id":"685af523b4ac24d5329d7846"},{"type":"Curator statement","text":"The 19-32 region, described as disordered, corresponds to the 467-480 region of the Gag polyprotein.","_id":"685af523b4ac24d5329d7847"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-04T11:33:37.679Z","_id":"685af523b4ac24d5329d7848"},"version":1,"_id":"685af523b4ac24d5329d7844","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2C55","_id":"685af523b4ac24d5329d784a"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":449,"end":461,"interaction_partner":[],"reference_html":"Solution structure of the human immunodeficiency virus type 1 p6 protein. <i> Fossen T, Wray V, Bruns K, Rachmat J, Henklein P, Tessmer U, Maczurek A, Klinger P, Schubert U. </i> J Biol Chem, 2005","reference_id":"16234236","region_id":"DP00101r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The quantitative NOE data for full-length sp6-(1–52) allow the definition of two α-helical structured regions extending from Ser-14 to Gly-18 and from Lys-33 to Ser-43 (Fig. 8, A and B, respectively), connected by a more flexible region that allows orientational freedom of the two helices.","_id":"685af523b4ac24d5329d784b"},{"type":"Curator statement","text":"The 1-13 region, described as disordered, corresponds to the 449-461 region of the Gag polyprotein.","_id":"685af523b4ac24d5329d784c"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-04T11:33:36.750Z","_id":"685af523b4ac24d5329d784d"},"version":1,"_id":"685af523b4ac24d5329d7849","reference_source":"pmid"}],"__v":0,"disorder_content":0.054,"disprot_consensus":{"full":[{"start":449,"end":461,"type":"D"},{"start":467,"end":480,"type":"D"}],"Structural state":[{"start":449,"end":461,"type":"D"},{"start":467,"end":480,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00063","name":"Myosin head (motor domain)","start":86,"end":777},{"id":"PF01576","name":"Myosin tail","start":854,"end":1934},{"id":"PF02736","name":"Myosin N-terminal SH3-like domain","start":22,"end":79}],"gene3D":[{"start":79,"end":718,"id":"3.40.850.10","name":"Kinesin motor domain"},{"start":791,"end":848,"id":"4.10.270.10","name":"Myosin, subunit A"},{"start":38,"end":78,"id":"2.30.30.360","name":"Myosin S1 fragment, N-terminal"},{"start":469,"end":676,"id":"1.20.58.530","name":"1.20.58.530"},{"start":849,"end":970,"id":"1.20.5.340","name":"1.20.5.340"},{"start":344,"end":649,"id":"1.20.120.720","name":"Myosin VI head, motor domain, U50 subdomain"},{"start":971,"end":1086,"id":"1.20.5.340","name":"1.20.5.340"}]},"uniref50":"UniRef50_Q61879","sequence":"MSQKPLSDDEKFLFVDKNFVNNPLAQADWSAKKLVWVPSEKHGFEAASIKEEKGDEVTVELQENGKKVTLSKDDIQKMNPPKFSKVEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVINPYKQLPIYSEKIIDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSITQGPSFSYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHIFYYLIAGASEQMRNDLLLEGFNNYTFLSNGHVPIPAQQDDEMFQETLEAMTIMGFTEEEQTSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAIEALAKAKFERLFRWILTRVNKALDKTKRQGASFLGILDIAGFEIFEINSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPTNPPGVLALLDEECWFPKATDTSFVEKLIQEQGNHAKFQKSKQLKDKTEFCILHYAGKVTYNASAWLTKNMDPLNDNVTSLLNQSSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYKEQLTKLMTTLRNTNPNFVRCIIPNHEKRAGKLDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFRTGVLAHLEEERDLKITDVIIAFQAQCRGYLARKAFAKRQQQLTAMKVIQRNCAAYLKLRNWQWWRLFTKVKPLLQVTRQEEEMQAKDEELQRTKERQQKAEAELKELEQKHTQLCEEKNLLQEKLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARIEEEEERSQQLQAEKKKMQQQMLDLEEQLEEEEAARQKLQLEKVTADGKIKKMEDDILIMEDQNNKLTKERKLLEERVSDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKIKRKLEGESSDLHEQIAELQAQIAELKAQLAKKEEELQAALARLEDETSQKNNALKKIRELESHISDLQEDLESEKAARNKAEKQKRDLSEELEALKTELEDTLDTTATQQELRAKREQEVTVLKRALEEETRTHEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKTKQTLEKDNADLANEIRSLSQAKQDVEHKKKKLEVQLQDLQSKYSDGERVRTELNEKVHKLQIEVENVTSLLNEAESKNIKLTKDVATLGSQLQDTQELLQEETRQKLNVTTKLRQLEDDKNSLQEQLDEEVEAKQNLERHISTLTIQLSDSKKKLQEFTATVETMEEGKKKLQREIESLTQQFEEKAASYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQMLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRTLEQQVEEMKTQLEELEDELQAAEDAKLRLEVNMQAMKSQFERDLQARDEQNEEKRRQLLKQLHEHETELEDERKQRALAAAAKKKLEVDVKDLESQVDSANKAREEAIKQLRKLQAQMKDYQRDLDDARAAREEIFATARENEKKAKNLEAELIQLQEDLAAAERARKQADLEKEEMAEELASANSGRTSLQDEKRRLEARIAQLEEELDEEHSNIETMSDRMRKAVQQAEQLNNELATERATAQKNENARQQLERQNKELRSKLQEMEGAVKSKFKSTIAALEAKIASLEEQLEQEAREKQAAAKTLRQKDKKLKDALLQVEDERKQAEQYKDQAEKGNLRLKQLKRQLEEAEEESQRINANRRKLQRELDEATESNDALGREVAALKSKLRRGNEPVSFAPPRRSGGRRVIENATDGGEEEIDGRDGDFNGKASE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Phasianinae","Gallus"],"uniref90":"UniRef90_P10587","disprot_id":"DP00102","ncbi_taxon_id":9031,"regions_counter":5,"creator":"dpiovesan","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":217,"region_id":"DP00102r001","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state. <i> Dominguez R, Freyzon Y, Trybus KM, Cohen C. </i> Cell, 1998","term_id":"IDPO:0000002","curator_id":"vnugnes","start":200,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-01-17T19:08:08.980Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1BR2"}],"reference_id":"9741621","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30111","entry_name":"tetrafluoroaluminate(1-)"}],"statement":[{"text":"The PDB structure shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:39:55.860Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":415,"region_id":"DP00102r002","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state. <i> Dominguez R, Freyzon Y, Trybus KM, Cohen C. </i> Cell, 1998","term_id":"IDPO:0000002","curator_id":"vnugnes","start":406,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-01-17T19:06:37.050Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1BR2"}],"reference_id":"9741621","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30111","entry_name":"tetrafluoroaluminate(1-)"}],"statement":[{"text":"The PDB structure shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:39:57.236Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":656,"region_id":"DP00102r005","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state. <i> Dominguez R, Freyzon Y, Trybus KM, Cohen C. </i> Cell, 1998","term_id":"IDPO:0000002","curator_id":"vnugnes","start":627,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-01-17T19:06:56.451Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1BR2"}],"reference_id":"9741621","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30111","entry_name":"tetrafluoroaluminate(1-)"}],"statement":[{"text":"The PDB structure shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-18T10:39:58.685Z"}}],"released":"2016_10","uniref100":"UniRef100_P10587","date":"2016-08-18T17:14:11.000Z","acc":"P10587","name":"Myosin-11","length":1979,"organism":"Gallus gallus","dataset":[],"UniParc":"UPI0000171370","genes":[{"name":{"value":"MYH11"}}],"alphafold_very_low_content":0.04699343102577059,"disorder_content":0.029307731177362305,"disprot_consensus":{"full":[{"start":200,"end":217,"type":"D"},{"start":406,"end":415,"type":"D"},{"start":627,"end":656,"type":"D"}],"Structural state":[{"start":200,"end":217,"type":"D"},{"start":406,"end":415,"type":"D"},{"start":627,"end":656,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01025","name":"GrpE","start":36,"end":194}],"gene3D":[{"start":138,"end":194,"id":"2.30.22.10","name":"Head domain of nucleotide exchange factor GrpE"},{"start":34,"end":137,"id":"3.90.20.20","name":"3.90.20.20"}]},"uniref50":"UniRef50_C4ZYN1","sequence":"MSSKEQKTPEGQAPEEIIMDQHEEIEAVEPEASAEQVDPRDEKVANLEAQLAEAQTRERDGILRVKAEMENLRRRTELDIEKAHKFALEKFINELLPVIDSLDRALEVADKANPDMSAMVEGIELTLKSMLDVVRKFGVEVIAETNVPLDPNVHQAIAMVESDDVAPGNVLGIMQKGYTLNGRTIRAAMVTVAKAKA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_C4ZYN1","disprot_id":"DP00103","ncbi_taxon_id":83333,"regions_counter":4,"creator":"eleonardi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":32,"region_id":"DP00103r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. <i> Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J. </i> Science, 1997","term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1DKG"}],"reference_id":"9103205","statement":[{"text":"The final model includes residues 3 to 383 of DnaK (except residues 184 and 210 to 213, which are disordered) and residues 34 to 197 (except residues 108 to 115) for the GrpE monomer that is proximal to DnaK in the complex, and residues 38 to 195 (except residues 108 to 115) for the GrpE monomer that is distal to DnaK, 28 water molecules, and 8 uranyl acetate ions, modeled as single sites. ","type":"Table"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-01T17:13:47.512Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":32,"term_name":"flexible N-terminal tail","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. <i> Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J. </i> Science, 1997","term_id":"IDPO:0000032","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"9103205","version":4,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00103r002","statement":[{"text":"The final model includes residues 3 to 383 of DnaK (except residues 184 and 210 to 213, which are disordered) and residues 34 to 197 (except residues 108 to 115) for the GrpE monomer that is proximal to DnaK in the complex, and residues 38 to 195 (except residues 108 to 115) for the GrpE monomer that is distal to DnaK, 28 water molecules, and 8 uranyl acetate ions, modeled as single sites. ","type":"Table"}],"ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-01T17:13:47.884Z"}}],"released":"2016_10","uniref100":"UniRef100_C4ZYN1","date":"2016-08-30T16:17:11.000Z","acc":"P09372","name":"Protein GrpE","length":197,"organism":"Escherichia coli (strain K12)","dataset":["Stress response proteins"],"UniParc":"UPI000012BB1F","genes":[{"name":{"value":"grpE"},"olnNames":[{"value":"b2614"},{"value":"JW2594"}]}],"alphafold_very_low_content":0.17766497461928935,"disorder_content":0.16243654822335024,"disprot_consensus":{"full":[{"start":1,"end":32,"type":"D"}],"Structural state":[{"start":1,"end":32,"type":"D"}],"Disorder function":[{"start":1,"end":32,"type":"F"}]}},{"acc":"P32773","sequence":"MSNAEASRVYEIIVESVVNEVREDFENAGIDEQTLQDLKNIWQKKLTETKVTTFSWDNQFNEGNINGVQNDLNFNLATPGVNSSEFNIKEENTGNEGLILPNINSNNNIPHSGETNINTNTVEATNNSGATLNTNTSGNTNADVTSQPKIEVKPEIELTINNANITTVENIDDESEKKDDEEKEEDVEKTRKEKEQIEQVKLQAKKEKRSALLDTDEVGSELDDSDDDYLISEGEEDGPDENLMLCLYDKVTRTKARWKCSLKDGVVTINRNDYTFQKAQVEAEWV","alphafold_very_low_content":"0.4090909090909091","creator":"mnecci","dataset":[],"date":"2016-08-09T11:16:39.000Z","disprot_id":"DP00104","features":{"pfam":[{"id":"PF03153","name":"Transcription factor IIA, alpha/beta subunit","start":9,"end":158},{"id":"PF03153","name":"Transcription factor IIA, alpha/beta subunit","start":172,"end":285}],"gene3D":[{"start":228,"end":286,"id":"2.30.18.10","name":"Transcription factor IIA (TFIIA), beta-barrel domain","_id":"685af523b4ac24d5329d7852"},{"start":2,"end":54,"id":"1.10.287.100","name":"1.10.287.100","_id":"685af523b4ac24d5329d7853"}]},"genes":[{"name":{"value":"TOA1","evidences":[],"_id":"685af523b4ac24d5329d785f"},"synonyms":[],"olnNames":[{"value":"YOR194C","evidences":[],"_id":"685af523b4ac24d5329d7860"}],"orfNames":[],"_id":"685af523b4ac24d5329d785e"}],"length":286,"name":"Transcription initiation factor IIA large subunit","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":4,"released":"2016_10","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"UniParc":"UPI00001370F9","uniref100":"UniRef100_P32773","uniref50":"UniRef50_P32773","uniref90":"UniRef90_P32773","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1YTF","_id":"685af523b4ac24d5329d7857"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":210,"end":240,"interaction_partner":[],"reference_html":"Crystal structure of a yeast TFIIA/TBP/DNA complex. <i> Tan S, Hunziker Y, Sargent DF, Richmond TJ. </i> Nature, 1996","reference_id":"8610010","region_id":"DP00104r002","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"The electron density for the N-terminal 31 amino acids of TOAlC (210-240) is not well defined, and indicates that this stretch of highly hydrophilic polypeptide is disordered (long shoelace).","_id":"685af523b4ac24d5329d7858"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d7856","reference_source":"pmid"}],"__v":0,"disorder_content":0.10839160839160839,"disprot_consensus":{"full":[{"start":210,"end":240,"type":"D"}],"Structural state":[{"start":210,"end":240,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00268","name":"Ribonucleotide reductase, small chain","start":31,"end":332}],"gene3D":[{"start":2,"end":340,"id":"1.10.620.20","name":"Ribonucleotide Reductase, subunit A"}]},"uniref50":"UniRef50_P69925","sequence":"MAYTTFSQTKNDQLKEPMFFGQPVNVARYDQQKYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLISIPELETWVETWAFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEQIQKRAEGISSYYDELIEMTSYWHLLGEGTHTVNGKTVTVSLRELKKKLYLCLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLLRSGADDPEMAEIAEECKQECYDLFVQAAQQEKDWADYLFRDGSMIGLNKDILCQYVEYITNIRMQAVGLDLPFQTRSNPIPWINTWLVSDNVQVAPQEVEVSSYLVGQIDSEVDTDDLSNFQL","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P69925","disprot_id":"DP00107","ncbi_taxon_id":83333,"regions_counter":2,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":376,"region_id":"DP00107r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of reduced protein R2 of ribonucleotide reductase: the structural basis for oxygen activation at a dinuclear iron site. <i> Logan DT, Su XD, Aberg A, Regnström K, Hajdu J, Eklund H, Nordlund P. </i> Structure, 1996","term_id":"IDPO:0000002","curator_id":"esalladini","start":342,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"8805591","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1XIK"}],"term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"The C-terminus is missing from the crystal structure but not mentioned in the article.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":342,"end":376,"reference_id":"8805591","reference_source":"pmid","reference_html":"Crystal structure of reduced protein R2 of ribonucleotide reductase: the structural basis for oxygen activation at a dinuclear iron site. <i> Logan DT, Su XD, Aberg A, Regnström K, Hajdu J, Eklund H, Nordlund P. </i> Structure, 1996","date":"2022-02-23T10:35:45.214Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":0,"cross_refs":[{"db":"PDB","id":"1XIK"}],"region_id":"DP00107r002","statement":[{"text":"The C-terminus is missing from the crystal structure but not mentioned in the article.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_P69925","date":"2016-08-23T15:40:14.000Z","acc":"P69924","name":"Ribonucleoside-diphosphate reductase 1 subunit beta","length":376,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI0000111FF8","genes":[{"name":{"value":"nrdB"},"synonyms":[{"value":"ftsB"}],"olnNames":[{"value":"b2235"},{"value":"JW2229"}]}],"alphafold_very_low_content":0.0398936170212766,"disorder_content":0.09308510638297872,"disprot_consensus":{"full":[{"start":342,"end":376,"type":"D"}],"Structural state":[{"start":342,"end":376,"type":"D"}],"Disorder function":[{"start":342,"end":376,"type":"F"}]}},{"acc":"P07598","sequence":"MSRTVMERIEYEMHTPDPKADPDKLHFVQIDEAKCIGCDTCSQYCPTAAIFGEMGEPHSIPHIEACINCGQCLTHCPENAIYEAQSWVPEVEKKLKDGKVKCIAMPAPAVRYALGDAFGMPVGSVTTGKMLAALQKLGFAHCWDTEFTADVTIWEEGSEFVERLTKKSDMPLPQFTSCCPGWQKYAETYYPELLPHFSTCKSPIGMNGALAKTYGAERMKYDPKQVYTVSIMPCIAKKYEGLRPELKSSGMRDIDATLTTRELAYMIKKAGIDFAKLPDGKRDSLMGESTGGATIFGVTGGVMEAALRFAYEAVTGKKPDSWDFKAVRGLDGIKEATVNVGGTDVKVAVVHGAKRFKQVCDDVKAGKSPYHFIEYMACPGGCVCGGGQPVMPGVLEAMDRTTTRLYAGLKKRLAMASANKA","alphafold_very_low_content":"0","creator":"ftonello","dataset":[],"date":"2016-09-08T11:55:10.000Z","disprot_id":"DP00108","features":{"pfam":[{"id":"PF02906","name":"Iron only hydrogenase large subunit, C-terminal domain","start":101,"end":386},{"id":"PF13237","name":"4Fe-4S dicluster domain","start":28,"end":77}],"gene3D":[{"start":149,"end":380,"id":"3.40.950.10","name":"Fe-only Hydrogenase (Larger Subunit); Chain L, domain 3","_id":"685af523b4ac24d5329d7863"},{"start":29,"end":390,"id":"3.40.50.1780","name":"3.40.50.1780","_id":"685af523b4ac24d5329d7864"},{"start":30,"end":81,"id":"3.30.70.20","name":"3.30.70.20","_id":"685af523b4ac24d5329d7865"}]},"genes":[{"name":{"value":"hydA","evidences":[],"_id":"685af523b4ac24d5329d7870"},"synonyms":[],"olnNames":[{"value":"DVU_1769","evidences":[],"_id":"685af523b4ac24d5329d7871"}],"orfNames":[],"_id":"685af523b4ac24d5329d786f"}],"length":421,"name":"Periplasmic [Fe] hydrogenase large subunit","ncbi_taxon_id":882,"organism":"Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)","regions_counter":3,"released":"2016_10","taxonomy":["Bacteria","Proteobacteria","Deltaproteobacteria","Desulfovibrionales","Desulfovibrionaceae","Desulfovibrio"],"UniParc":"UPI0000111B46","uniref100":"UniRef100_P07598","uniref50":"UniRef50_P07598","uniref90":"UniRef90_P07598","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1HFE","_id":"685af523b4ac24d5329d786a"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-23T10:38:20.403Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":399,"end":421,"interaction_partner":[],"reference_html":"Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center. <i> Nicolet Y, Piras C, Legrand P, Hatchikian CE, Fontecilla-Camps JC. </i> Structure, 1999","reference_id":"10368269","region_id":"DP00108r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The tracing of the large subunit of DdHase in the electron-density maps showed that the last 24 amino acid residues at the C terminus, as determined by DNA sequence analysis of the gene (Figure 1), were either missing or highly disordered.","_id":"685af523b4ac24d5329d786b"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":0,"_id":"685af523b4ac24d5329d7869","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1HFE","_id":"685af523b4ac24d5329d786d"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-23T10:38:28.593Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":399,"end":421,"interaction_partner":[],"reference_html":"Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center. <i> Nicolet Y, Piras C, Legrand P, Hatchikian CE, Fontecilla-Camps JC. </i> Structure, 1999","reference_id":"10368269","region_id":"DP00108r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The tracing of the large subunit of DdHase in the electron-density maps showed that the last 24 amino acid residues at the C terminus, as determined by DNA sequence analysis of the gene (Figure 1), were either missing or highly disordered.","_id":"685af523b4ac24d5329d786e"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":0,"_id":"685af523b4ac24d5329d786c","reference_source":"pmid"}],"__v":0,"disorder_content":0.05463182897862233,"disprot_consensus":{"full":[{"start":399,"end":421,"type":"D"}],"Structural state":[{"start":399,"end":421,"type":"D"}],"Disorder function":[{"start":399,"end":421,"type":"F"}]}},{"features":{"pfam":[],"gene3D":[{"start":36,"end":247,"id":"2.160.10.10","name":"Hexapeptide repeat proteins"}]},"uniref50":"UniRef50_P40881","sequence":"MMFNKQIFTILILSLSLALAGSGCISEGAEDNVAQEITVDEFSNIRENPVTPWNPEPSAPVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGMPIFVGDRSNVQDGVVLHALETINEEGEPIEDNIVEVDGKEYAVYIGNNVSLAHQSQVHGPAAVGDDTFIGMQAFVFKSKVGNNCVLEPRSAAIGVTIPDGRYIPAGMVVTSQAEADKLPEVTDDYAYSHTNEAVVYVNVHLAEGYKETS","taxonomy":["Archaea","Euryarchaeota","Stenosarchaea group","Methanomicrobia","Methanosarcinales","Methanosarcinaceae","Methanosarcina"],"uniref90":"UniRef90_P40881","disprot_id":"DP00110","ncbi_taxon_id":2210,"regions_counter":2,"creator":"dpiovesan","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":37,"region_id":"DP00110r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila. <i> Iverson TM, Alber BE, Kisker C, Ferry JG, Rees DC. </i> Biochemistry, 2000","term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1QRE"},{"db":"PDB","id":"1QQ0"}],"reference_id":"10924115","statement":[{"text":"However, in the remainder of the models, the N-termini are disordered.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":37,"reference_id":"10924115","reference_source":"pmid","reference_html":"A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila. <i> Iverson TM, Alber BE, Kisker C, Ferry JG, Rees DC. </i> Biochemistry, 2000","date":"2022-02-23T10:49:41.671Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":0,"cross_refs":[{"db":"PDB","id":"1QRE"},{"db":"PDB","id":"1QQ0"}],"region_id":"DP00110r002","statement":[{"text":"However, in the remainder of the models, the N-termini are disordered.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_P40881","date":"2016-08-22T11:42:17.000Z","acc":"P40881","name":"Carbonic anhydrase","length":247,"organism":"Methanosarcina thermophila","dataset":[],"UniParc":"UPI0000112B59","genes":[{"orfNames":[{"value":"MSTHT_0588"}]}],"alphafold_very_low_content":0.13765182186234817,"disorder_content":0.14979757085020243,"disprot_consensus":{"full":[{"start":1,"end":37,"type":"D"}],"Structural state":[{"start":1,"end":37,"type":"D"}],"Disorder function":[{"start":1,"end":37,"type":"F"}]}},{"acc":"P27577","sequence":"MKAAVDLKPTLTIIKTEKVDLELFPSPDMECADVPLLTPSSKEMMSQALKATFSGFTKEQQRLGIPKDPRQWTETHVRDWVMWAVNEFSLKGVDFQKFCMSGAALCALGKECFLELAPDFVGDILWEHLEILQKEDVKPYQVNGANPTYPESCYTSDYFISYGIEHAQCVPPSEFSEPSFITESYQTLHPISSEELLSLKYENDYPSVILQDPLQTDTLQTDYFAIKQEVLTPDNMCLGRASRGKLGGQDSFESVESYDSCDRLTQSWSSQSSFNSLQRVPSYDSFDYEDYPAALPNHKPKGTFKDYVRDRADLNKDKPVIPAAALAGYTGSGPIQLWQFLLELLTDKSCQSFISWTGDGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTAGKRYVYRFVCDLQSLLGYTPEELHAMLDVKPDAD","alphafold_very_low_content":"0.45227272727272727","creator":"bjuhasz","dataset":[],"date":"2016-09-04T18:05:58.000Z","disprot_id":"DP00111","features":{"pfam":[{"id":"PF00178","name":"Ets-domain","start":335,"end":415},{"id":"PF02198","name":"Sterile alpha motif (SAM)/Pointed domain","start":54,"end":135},{"id":"PF19525","name":"Ets1 N-terminal flanking region of Ets domain","start":148,"end":332}],"gene3D":[{"start":297,"end":436,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain","_id":"685af523b4ac24d5329d7874"},{"start":42,"end":138,"id":"1.10.150.50","name":"Transcription Factor, Ets-1","_id":"685af523b4ac24d5329d7875"}]},"genes":[{"name":{"value":"Ets1","evidences":[],"_id":"685af523b4ac24d5329d788e"},"synonyms":[{"value":"Ets-1","evidences":[],"_id":"685af523b4ac24d5329d788f"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d788d"}],"length":440,"name":"Protein C-ets-1","ncbi_taxon_id":10090,"organism":"Mus musculus","regions_counter":12,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"UniParc":"UPI000016CD40","uniref100":"UniRef100_P27577","uniref50":"UniRef50_P14921","uniref90":"UniRef90_P27577","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":244,"end":301,"interaction_partner":[],"reference_html":"Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region. <i> Pufall MA, Lee GM, Nelson ML, Kang HS, Velyvis A, Kay LE, McIntosh LP, Graves BJ. </i> Science, 2005","reference_id":"15994560","region_id":"DP00111r001","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"ΔN2445P, a form which is homogenously phosphorylated by CaMKII, contains five specific phosphoserines in the serine-rich region (SRR, residues 244 to 300) (Fig. 1C) and appears to undergo the same structural transition upon DNA binding as do unmodified ΔN244 (fig. S1E) and other Ets-1 species (3, 7, 11).","_id":"685af523b4ac24d5329d7877"},{"type":"Article","text":"The phosphorylated SRR was found to be predominantly unstructured and highly flexible. Based on main-chain 1H and 13C chemical shifts, NMR spectra revealed no predominant secondary structure within this region (17) (Fig. 2A), and the amide hydrogen exchange (HX) rates were comparable to those of a random coil polypeptide (Fig. 2B).","_id":"685af523b4ac24d5329d7878"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d7876","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":244,"end":301,"interaction_partner":[],"reference_html":"Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region. <i> Pufall MA, Lee GM, Nelson ML, Kang HS, Velyvis A, Kay LE, McIntosh LP, Graves BJ. </i> Science, 2005","reference_id":"15994560","region_id":"DP00111r002","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"ΔN2445P, a form which is homogenously phosphorylated by CaMKII, contains five specific phosphoserines in the serine-rich region (SRR, residues 244 to 300) (Fig. 1C) and appears to undergo the same structural transition upon DNA binding as do unmodified ΔN244 (fig. S1E) and other Ets-1 species (3, 7, 11).","_id":"685af523b4ac24d5329d787a"}],"states_connection":[],"term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","version":4,"_id":"685af523b4ac24d5329d7879","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":244,"end":301,"interaction_partner":[],"reference_html":"Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region. <i> Pufall MA, Lee GM, Nelson ML, Kang HS, Velyvis A, Kay LE, McIntosh LP, Graves BJ. </i> Science, 2005","reference_id":"15994560","region_id":"DP00111r003","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"ΔN2445P, a form which is homogenously phosphorylated by CaMKII, contains five specific phosphoserines in the serine-rich region (SRR, residues 244 to 300) (Fig. 1C) and appears to undergo the same structural transition upon DNA binding as do unmodified ΔN244 (fig. S1E) and other Ets-1 species (3, 7, 11).","_id":"685af523b4ac24d5329d787c"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d787b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":244,"end":301,"interaction_partner":[],"reference_html":"Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region. <i> Pufall MA, Lee GM, Nelson ML, Kang HS, Velyvis A, Kay LE, McIntosh LP, Graves BJ. </i> Science, 2005","reference_id":"15994560","region_id":"DP00111r004","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"ΔN2445P, a form which is homogenously phosphorylated by CaMKII, contains five specific phosphoserines in the serine-rich region (SRR, residues 244 to 300) (Fig. 1C) and appears to undergo the same structural transition upon DNA binding as do unmodified ΔN244 (fig. S1E) and other Ets-1 species (3, 7, 11).","_id":"685af523b4ac24d5329d787e"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","term_id":"GO:0003676","term_is_binding":true,"term_is_obsolete":false,"term_name":"nucleic acid binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","version":4,"_id":"685af523b4ac24d5329d787d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2JV3","_id":"685af523b4ac24d5329d7880"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":29,"end":49,"interaction_partner":[],"reference_html":"Structure of the Ets-1 pointed domain and mitogen-activated protein kinase phosphorylation site. <i> Slupsky CM, Gentile LN, Donaldson LW, Mackereth CD, Seidel JJ, Graves BJ, McIntosh LP. </i> Proc Natl Acad Sci U S A, 1998","reference_id":"9770451","region_id":"DP00111r005","released":"2022_03","sample":[],"statement":[{"type":"Figure","text":"In contrast, residues 31–34, 36–37, 43–45, and 47–49 at the N terminus and 135–138 at the C terminus of Ets-1(29–138) are motionally disordered on a nano- to picosecond time scale as evident by NOEs < 0.5.","_id":"685af523b4ac24d5329d7881"},{"type":"Figure","text":"The N and C termini of the molecule (residues 29–49 and 135–138) are disordered as evidenced by both high structural rms deviations and 15N NMR relaxation data.","_id":"685af523b4ac24d5329d7882"},{"type":"Results","text":"The region of Ets-1(29–138) that precedes helix H1 is disordered.","_id":"685af523b4ac24d5329d7883"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d787f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":29,"end":49,"interaction_partner":[],"reference_html":"Structure of the Ets-1 pointed domain and mitogen-activated protein kinase phosphorylation site. <i> Slupsky CM, Gentile LN, Donaldson LW, Mackereth CD, Seidel JJ, Graves BJ, McIntosh LP. </i> Proc Natl Acad Sci U S A, 1998","reference_id":"9770451","region_id":"DP00111r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As shown in Fig. ​Fig.22D, the chemical shift perturbations caused by the modifications were highly localized to the amino acids immediately adjacent to Leu-36 and Thr-38. Thus, within the context of Ets-1(29–138), phosphorylation of Thr-38 does not significantly perturb the disordered character of the MAP kinase substrate site or its adjacent amino acids, nor alter the structure or oligomerization state of the PNT domain.","_id":"685af523b4ac24d5329d7885"}],"states_connection":[],"term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d7884","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2JV3","_id":"685af523b4ac24d5329d7889"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-23T11:35:59.218Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":29,"end":49,"interaction_partner":[],"reference_html":"Structure of the Ets-1 pointed domain and mitogen-activated protein kinase phosphorylation site. <i> Slupsky CM, Gentile LN, Donaldson LW, Mackereth CD, Seidel JJ, Graves BJ, McIntosh LP. </i> Proc Natl Acad Sci U S A, 1998","reference_id":"9770451","region_id":"DP00111r008","released":"2022_03","sample":[],"statement":[{"type":"Figure","text":"In contrast, residues 31–34, 36–37, 43–45, and 47–49 at the N terminus and 135–138 at the C terminus of Ets-1(29–138) are motionally disordered on a nano- to picosecond time scale as evident by NOEs < 0.5.","_id":"685af523b4ac24d5329d788a"},{"type":"Figure","text":"The N and C termini of the molecule (residues 29–49 and 135–138) are disordered as evidenced by both high structural rms deviations and 15N NMR relaxation data.","_id":"685af523b4ac24d5329d788b"},{"type":"Results","text":"The region of Ets-1(29–138) that precedes helix H1 is disordered.","_id":"685af523b4ac24d5329d788c"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":0,"_id":"685af523b4ac24d5329d7888","reference_source":"pmid"}],"__v":0,"disorder_content":0.17954545454545454,"disprot_consensus":{"full":[{"start":29,"end":49,"type":"D"},{"start":244,"end":301,"type":"T"}],"Structural state":[{"start":29,"end":49,"type":"D"},{"start":244,"end":301,"type":"D"}],"Disorder function":[{"start":29,"end":49,"type":"F"},{"start":244,"end":301,"type":"F"}],"Structural transition":[{"start":244,"end":301,"type":"T"}],"Molecular function":[{"start":244,"end":301,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00257","name":"Dehydrin","start":13,"end":153}]},"uniref50":"UniRef50_P22239","sequence":"MAQFGGEKYGGRHTDEYGNPIQQGAGAHRGGGIMGGGQQAGQHGTTGVLGHGTAGQHGTTGGGLGHGTAGTGGALGGQHRRSGSSSSSSSSESDGEGGRRKKGMKDKMKEKLPGGHGTTTDQQQYGTAATHGQAQQHEKKGIMDKIKEKLPGGQH","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","lamiids","Lamiales","Linderniaceae","Craterostigma"],"uniref90":"UniRef90_P22239","disprot_id":"DP00112","ncbi_taxon_id":4153,"regions_counter":9,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":155,"region_id":"DP00112r004","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The recombinant dehydrin-like desiccation stress protein from the resurrection plant Craterostigma plantagineum displays no defined three-dimensional structure in its native state. <i> Lisse T, Bartels D, Kalbitzer HR, Jaenicke R. </i> Biol Chem, 1996","term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"9067253","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"The CD (circular dichroism) spectra in the far-UV show a strong minimum at 198 nm in the native state which indicates a largely random conformation.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-08T19:54:38.976Z"}},{"start":1,"end":155,"reference_id":"9067253","reference_source":"pmid","reference_html":"The recombinant dehydrin-like desiccation stress protein from the resurrection plant Craterostigma plantagineum displays no defined three-dimensional structure in its native state. <i> Lisse T, Bartels D, Kalbitzer HR, Jaenicke R. </i> Biol Chem, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00112r007","statement":[{"text":"1H-NMR(nuclear magnetic resonance) spectra in aqueous solution are characterized by a small chemical shift dispersion typical for an unfolded protein; however, the observed line-widths are not typical  for a highly mobile random coil structure.","type":"Abstract"},{"text":"In order to get some deeper insight into the structure, one-dimensional 1H-NMR spectra were recorded under different conditions (pH 2.3, 4.4 and 6.6, 0 and 100 mM KCI, 10 °C and 35 °C. They were typical for a predominantly non-folded protein.","type":"Results"},{"text":"Assuming that essentially all amide Hα cross peaks are visible in the spectrum, the frequency distribution suggests the protein to be essentially unstructured.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-08T19:52:39.432Z"}},{"start":1,"end":155,"reference_id":"9067253","reference_source":"pmid","reference_html":"The recombinant dehydrin-like desiccation stress protein from the resurrection plant Craterostigma plantagineum displays no defined three-dimensional structure in its native state. <i> Lisse T, Bartels D, Kalbitzer HR, Jaenicke R. </i> Biol Chem, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00112r008","statement":[{"text":"As a consequence of its loose structure, Dsp16 is extremely sensitive towards proteolysis unless its structure is stabilized by structure-making additives such as trifluoroethanol.","type":"Abstract"},{"text":"At 20 °C, the protein undergoes slow proteolytic degradation in the course of the equilibration.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-08T19:51:39.520Z"}},{"start":1,"end":155,"reference_id":"9067253","reference_source":"pmid","reference_html":"The recombinant dehydrin-like desiccation stress protein from the resurrection plant Craterostigma plantagineum displays no defined three-dimensional structure in its native state. <i> Lisse T, Bartels D, Kalbitzer HR, Jaenicke R. </i> Biol Chem, 1996","date":"2025-10-08T19:51:01.618Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"region_id":"DP00112r009","statement":[{"text":"The protein exhibits anomalous elution behavior, showing a\nhomogeneous band at = 20 kDa; using an anti-Dspl 6 antiserum (Schneider ef a/., 1993), the authenticity of the protein was clearly confirmed in a Western blot (Figure 4).","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P22239","date":"2016-08-24T14:35:29.000Z","acc":"P22239","name":"Desiccation-related protein clone PCC6-19","length":155,"organism":"Craterostigma plantagineum","dataset":["Stress response proteins"],"UniParc":"UPI00001292D1","genes":[],"alphafold_very_low_content":0.45161290322580644,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":155,"type":"D"}],"Structural state":[{"start":1,"end":155,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00957","name":"Synaptobrevin","start":29,"end":108}],"gene3D":[{"start":2,"end":113,"id":"1.20.5.110","name":"1.20.5.110"}]},"uniref50":"UniRef50_P31109","sequence":"MSSSTPFDPYALSEHDEERPQNVQSKSRTAELQAEIDDTVGIMRDNINKVAERGERLTSIEDKADNLAVSAQGFKRGANRVRKAMWYKDLKMKMCLALVIIILLVVIIVPIAVHFSR","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P31109","disprot_id":"DP00113","ncbi_taxon_id":559292,"regions_counter":12,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":93,"region_id":"DP00113r001","reference_id":"9326367","start":1,"ec_id":"ECO:0006204","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The evolutionarily conserved SNARE (SNAP receptor) proteins and their complexes are key players in the docking and fusion of secretory vesicles with their target membrane. Biophysical techniques were used to characterize structural and energetic properties of the cytoplasmic domains of the yeast SNAREs Snc1 and Sso1, of the SNAP-25-like domain of Sec9, and of the Sso1:Sec9 and Sso1:Sec9:Snc1 complexes. Individually, all three SNAREs are monomeric; Sso1 shows significant secondary structure while Snc1 and Sec9 are largely unstructured. Ternary SNARE complex formation (KD <50 nM) is accompanied by a more than two-fold increase in secondary structure. This binding induced structure, the large increase in thermal stability, and the self-association of the ternary complex represent conserved properties of SNAREs that are probably important in vesicle docking and fusion.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"reference_html":"Formation of a yeast SNARE complex is accompanied by significant structural changes. <i> Rice LM, Brennwald P, Brünger AT. </i> FEBS Lett, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":93,"region_id":"DP00113r002","reference_id":"9326367","start":1,"ec_id":"ECO:0006317","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The evolutionarily conserved SNARE (SNAP receptor) proteins and their complexes are key players in the docking and fusion of secretory vesicles with their target membrane. Biophysical techniques were used to characterize structural and energetic properties of the cytoplasmic domains of the yeast SNAREs Snc1 and Sso1, of the SNAP-25-like domain of Sec9, and of the Sso1:Sec9 and Sso1:Sec9:Snc1 complexes. Individually, all three SNAREs are monomeric; Sso1 shows significant secondary structure while Snc1 and Sec9 are largely unstructured. Ternary SNARE complex formation (KD <50 nM) is accompanied by a more than two-fold increase in secondary structure. This binding induced structure, the large increase in thermal stability, and the self-association of the ternary complex represent conserved properties of SNAREs that are probably important in vesicle docking and fusion.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","version":3,"reference_html":"Formation of a yeast SNARE complex is accompanied by significant structural changes. <i> Rice LM, Brennwald P, Brünger AT. </i> FEBS Lett, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":93,"region_id":"DP00113r003","reference_id":"9326367","start":1,"term_id":"IDPO:0000011","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Individual SNAREs and the Sso1:Sec9c complex are monomeric; the Sso1:Sec9c:Snc1 complex self‐associates.","type":"Results"},{"text":"The individual SNAREs, the Sso1:Sec9c complex, and the Sso1:Sec9c:Snc1 complex are all well‐defined entities (Figs. 1 and 2) that can be isolated chromatographically. CD spectroscopy can therefore be used to investigate possible structural changes that may accompany binding events.","type":"Results"},{"text":"The spectra for Sec9c and Snc1 are very similar to each other and are suggestive of largely random coil conformation. The unstructured state of Sec9c and Snc1 was recently confirmed by ongoing NMR studies (Fiebig et al., unpublished).","type":"Results"},{"text":"Fig. 4 (right panel) shows the CD spectrum recorded from the purified ternary complex. It too shows a significant α‐helical signal, in large excess of that expected from computing the theoretical non‐interacting CD spectrum from spectra of the three individual proteins, or from the observed Sso1:Sec9c complex spectrum and that of Snc1. Again, this increase in mean residue ellipticity could result from increases in any of the individual protein's secondary structure content although most of the changes are likely to occur in Sec9c and in Snc1. The high mean residue ellipticity observed for the ternary complex suggests a large α‐helical content.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"reference_html":"Formation of a yeast SNARE complex is accompanied by significant structural changes. <i> Rice LM, Brennwald P, Brünger AT. </i> FEBS Lett, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"disorder to order","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":93,"region_id":"DP00113r004","reference_id":"9326367","start":1,"term_id":"GO:0005515","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Individual SNAREs and the Sso1:Sec9c complex are monomeric; the Sso1:Sec9c:Snc1 complex self‐associates.","type":"Results"},{"text":"The individual SNAREs, the Sso1:Sec9c complex, and the Sso1:Sec9c:Snc1 complex are all well‐defined entities (Figs. 1 and 2) that can be isolated chromatographically. CD spectroscopy can therefore be used to investigate possible structural changes that may accompany binding events.","type":"Results"},{"text":"Fig. 4 (right panel) shows the CD spectrum recorded from the purified ternary complex. It too shows a significant α‐helical signal, in large excess of that expected from computing the theoretical non‐interacting CD spectrum from spectra of the three individual proteins, or from the observed Sso1:Sec9c complex spectrum and that of Snc1. Again, this increase in mean residue ellipticity could result from increases in any of the individual protein's secondary structure content although most of the changes are likely to occur in Sec9c and in Snc1. The high mean residue ellipticity observed for the ternary complex suggests a large α‐helical content.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":4,"reference_html":"Formation of a yeast SNARE complex is accompanied by significant structural changes. <i> Rice LM, Brennwald P, Brünger AT. </i> FEBS Lett, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"protein binding","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":93,"region_id":"DP00113r005","reference_id":"9326367","start":1,"term_id":"GO:0060090","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Individual SNAREs and the Sso1:Sec9c complex are monomeric; the Sso1:Sec9c:Snc1 complex self‐associates.","type":"Results"},{"text":"The individual SNAREs, the Sso1:Sec9c complex, and the Sso1:Sec9c:Snc1 complex are all well‐defined entities (Figs. 1 and 2) that can be isolated chromatographically. CD spectroscopy can therefore be used to investigate possible structural changes that may accompany binding events.","type":"Results"},{"text":"Fig. 4 (right panel) shows the CD spectrum recorded from the purified ternary complex. It too shows a significant α‐helical signal, in large excess of that expected from computing the theoretical non‐interacting CD spectrum from spectra of the three individual proteins, or from the observed Sso1:Sec9c complex spectrum and that of Snc1. Again, this increase in mean residue ellipticity could result from increases in any of the individual protein's secondary structure content although most of the changes are likely to occur in Sec9c and in Snc1. The high mean residue ellipticity observed for the ternary complex suggests a large α‐helical content.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":4,"reference_html":"Formation of a yeast SNARE complex is accompanied by significant structural changes. <i> Rice LM, Brennwald P, Brünger AT. </i> FEBS Lett, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"molecular adaptor activity","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":93,"region_id":"DP00113r006","reference_id":"9326367","start":1,"term_id":"GO:0060090","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Increase in tryptophan fluorescence upon formation of the Sso1:Sec9c:Snc1 complex.","type":"Results"},{"text":"There is a single tryptophan in the Sso1:Sec9c:Snc1 complex, at position 86 in Snc1 which is close to (within ten residues) its putative transmembrane domain. Fig. 6 shows the result of titrating Snc1 with increasing amounts of binary complex. Formation of the ternary complex causes a significant increase in fluorescence intensity. The increase in fluorescence is saturable and up to saturation is linear with concentration. This behavior could be explained by tight binding and by structural re‐arrangements in the vicinity of the tryptophan residue.","type":"Results"},{"text":"Changes in tryptophan fluorescence resulting from formation of the Sso1:Sec9c:Snc1 complex. The fluorescence intensity ratio is the measured fluorescence intensity divided by the fluorescence intensity of 2.5 μM Snc1 at 350 nm. The increase in fluoresence intensity is saturable, and up to saturation increases linearly with Sso1:Sec9c complex concentration, suggesting very tight binding. All measurements were performed at 25°C.","type":"Figure"},{"text":"Increase in fluorescence intensity ratio as a function of Sso1:Sec9c complex concentration.","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"experimental evidence used in manual assertion","version":4,"reference_html":"Formation of a yeast SNARE complex is accompanied by significant structural changes. <i> Rice LM, Brennwald P, Brünger AT. </i> FEBS Lett, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000269","term_name":"molecular adaptor activity","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":93,"region_id":"DP00113r007","reference_id":"9326367","start":1,"term_id":"IDPO:0000011","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Increase in tryptophan fluorescence upon formation of the Sso1:Sec9c:Snc1 complex.","type":"Results"},{"text":"There is a single tryptophan in the Sso1:Sec9c:Snc1 complex, at position 86 in Snc1 which is close to (within ten residues) its putative transmembrane domain. Fig. 6 shows the result of titrating Snc1 with increasing amounts of binary complex. Formation of the ternary complex causes a significant increase in fluorescence intensity. The increase in fluorescence is saturable and up to saturation is linear with concentration. This behavior could be explained by tight binding and by structural re‐arrangements in the vicinity of the tryptophan residue.","type":"Results"},{"text":"Changes in tryptophan fluorescence resulting from formation of the Sso1:Sec9c:Snc1 complex. The fluorescence intensity ratio is the measured fluorescence intensity divided by the fluorescence intensity of 2.5 μM Snc1 at 350 nm. The increase in fluoresence intensity is saturable, and up to saturation increases linearly with Sso1:Sec9c complex concentration, suggesting very tight binding. All measurements were performed at 25°C.","type":"Figure"},{"text":"Increase in fluorescence intensity ratio as a function of Sso1:Sec9c complex concentration.","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"experimental evidence used in manual assertion","version":3,"reference_html":"Formation of a yeast SNARE complex is accompanied by significant structural changes. <i> Rice LM, Brennwald P, Brünger AT. </i> FEBS Lett, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000269","term_name":"disorder to order","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":93,"region_id":"DP00113r008","reference_id":"9326367","start":1,"term_id":"GO:0005515","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Increase in tryptophan fluorescence upon formation of the Sso1:Sec9c:Snc1 complex.","type":"Results"},{"text":"There is a single tryptophan in the Sso1:Sec9c:Snc1 complex, at position 86 in Snc1 which is close to (within ten residues) its putative transmembrane domain. Fig. 6 shows the result of titrating Snc1 with increasing amounts of binary complex. Formation of the ternary complex causes a significant increase in fluorescence intensity. The increase in fluorescence is saturable and up to saturation is linear with concentration. This behavior could be explained by tight binding and by structural re‐arrangements in the vicinity of the tryptophan residue.","type":"Results"},{"text":"Changes in tryptophan fluorescence resulting from formation of the Sso1:Sec9c:Snc1 complex. The fluorescence intensity ratio is the measured fluorescence intensity divided by the fluorescence intensity of 2.5 μM Snc1 at 350 nm. The increase in fluoresence intensity is saturable, and up to saturation increases linearly with Sso1:Sec9c complex concentration, suggesting very tight binding. All measurements were performed at 25°C.","type":"Figure"},{"text":"Increase in fluorescence intensity ratio as a function of Sso1:Sec9c complex concentration.","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"experimental evidence used in manual assertion","version":4,"reference_html":"Formation of a yeast SNARE complex is accompanied by significant structural changes. <i> Rice LM, Brennwald P, Brünger AT. </i> FEBS Lett, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000269","term_name":"protein binding","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":93,"region_id":"DP00113r009","reference_id":"9326367","start":1,"term_id":"GO:0005515","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"As a first step towards characterizing the energetics of SNARE assembly, we have measured thermal denaturation profiles of Sso1, the Sso1:Sec9c complex, and the Sso1:Sec9c:Snc1 complex. Fig. 5 (left panel) shows the thermal denaturation profiles for Sso1 and the binary Sso1:Sec9c complex, and Fig. 5 (right panel) shows the thermal denaturation profiles for Sso1 and the ternary Sso1:Sec9c:Snc1 complex. Sso1 melts with a single transition with a T m of about 48°C. The Sso1:Sec9c complex also unfolds in a single transition with a T m of about 50°C. The melting profile of the ternary complex is more complicated, but it shows a cooperative transition at about 71°C.","type":"Results"},{"text":"Thermal stability of Sso1 and of the Sso1:Sec9c and Sso1:Sec9c:Snc1 complexes. Change in mean residue ellipticity at 222 nm (Θ222) was measured as a function of temperature. Buffer conditions were as in Figs. 3 and 4. Measurements were made at 1° temperature increments after 1 min of equilibration, and averaged for 30 s. The dashed line shows the denaturation profile for Sso1 in both panels. Left panel: thermal denaturation profiles for Sso1 and the Sso1:Sec9c complex (solid line), right panel: thermal denaturation profiles for Sso1 and the Sso1:Sec9c:Snc1 complex (solid line).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","version":4,"reference_html":"Formation of a yeast SNARE complex is accompanied by significant structural changes. <i> Rice LM, Brennwald P, Brünger AT. </i> FEBS Lett, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006317","term_name":"protein binding","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":93,"region_id":"DP00113r010","reference_id":"9326367","start":1,"term_id":"IDPO:0000011","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"As a first step towards characterizing the energetics of SNARE assembly, we have measured thermal denaturation profiles of Sso1, the Sso1:Sec9c complex, and the Sso1:Sec9c:Snc1 complex. Fig. 5 (left panel) shows the thermal denaturation profiles for Sso1 and the binary Sso1:Sec9c complex, and Fig. 5 (right panel) shows the thermal denaturation profiles for Sso1 and the ternary Sso1:Sec9c:Snc1 complex. Sso1 melts with a single transition with a T m of about 48°C. The Sso1:Sec9c complex also unfolds in a single transition with a T m of about 50°C. The melting profile of the ternary complex is more complicated, but it shows a cooperative transition at about 71°C.","type":"Results"},{"text":"Thermal stability of Sso1 and of the Sso1:Sec9c and Sso1:Sec9c:Snc1 complexes. Change in mean residue ellipticity at 222 nm (Θ222) was measured as a function of temperature. Buffer conditions were as in Figs. 3 and 4. Measurements were made at 1° temperature increments after 1 min of equilibration, and averaged for 30 s. The dashed line shows the denaturation profile for Sso1 in both panels. Left panel: thermal denaturation profiles for Sso1 and the Sso1:Sec9c complex (solid line), right panel: thermal denaturation profiles for Sso1 and the Sso1:Sec9c:Snc1 complex (solid line).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","version":3,"reference_html":"Formation of a yeast SNARE complex is accompanied by significant structural changes. <i> Rice LM, Brennwald P, Brünger AT. </i> FEBS Lett, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006317","term_name":"disorder to order","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":93,"region_id":"DP00113r011","reference_id":"9326367","start":1,"term_id":"GO:0060090","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"As a first step towards characterizing the energetics of SNARE assembly, we have measured thermal denaturation profiles of Sso1, the Sso1:Sec9c complex, and the Sso1:Sec9c:Snc1 complex. Fig. 5 (left panel) shows the thermal denaturation profiles for Sso1 and the binary Sso1:Sec9c complex, and Fig. 5 (right panel) shows the thermal denaturation profiles for Sso1 and the ternary Sso1:Sec9c:Snc1 complex. Sso1 melts with a single transition with a T m of about 48°C. The Sso1:Sec9c complex also unfolds in a single transition with a T m of about 50°C. The melting profile of the ternary complex is more complicated, but it shows a cooperative transition at about 71°C.","type":"Results"},{"text":"Thermal stability of Sso1 and of the Sso1:Sec9c and Sso1:Sec9c:Snc1 complexes. Change in mean residue ellipticity at 222 nm (Θ222) was measured as a function of temperature. Buffer conditions were as in Figs. 3 and 4. Measurements were made at 1° temperature increments after 1 min of equilibration, and averaged for 30 s. The dashed line shows the denaturation profile for Sso1 in both panels. Left panel: thermal denaturation profiles for Sso1 and the Sso1:Sec9c complex (solid line), right panel: thermal denaturation profiles for Sso1 and the Sso1:Sec9c:Snc1 complex (solid line).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","version":4,"reference_html":"Formation of a yeast SNARE complex is accompanied by significant structural changes. <i> Rice LM, Brennwald P, Brünger AT. </i> FEBS Lett, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006317","term_name":"molecular adaptor activity","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":93,"region_id":"DP00113r012","reference_id":"9326367","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"There is a single tryptophan in the Sso1:Sec9c:Snc1 complex, at position 86 in Snc1 which is close to (within ten residues) its putative transmembrane domain. Fig. 6 shows the result of titrating Snc1 with increasing amounts of binary complex. Formation of the ternary complex causes a significant increase in fluorescence intensity. The increase in fluorescence is saturable and up to saturation is linear with concentration. This behavior could be explained by tight binding and by structural re‐arrangements in the vicinity of the tryptophan residue.","type":"Results"},{"text":"Changes in tryptophan fluorescence resulting from formation of the Sso1:Sec9c:Snc1 complex. The fluorescence intensity ratio is the measured fluorescence intensity divided by the fluorescence intensity of 2.5 μM Snc1 at 350 nm. The increase in fluoresence intensity is saturable, and up to saturation increases linearly with Sso1:Sec9c complex concentration, suggesting very tight binding. All measurements were performed at 25°C. (a) Emission spectra of Snc1 (2.5 μM) (lower line) and of Snc1 (2.5 μM) combined with purified Sso1:Sec9c complex (3.2 μM) (upper line). (b) Increase in fluorescence intensity ratio as a function of Sso1:Sec9c complex concentration.","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"experimental evidence used in manual assertion","version":3,"reference_html":"Formation of a yeast SNARE complex is accompanied by significant structural changes. <i> Rice LM, Brennwald P, Brünger AT. </i> FEBS Lett, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000269","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P31109","date":"2016-09-13T15:08:06.000Z","acc":"P31109","name":"Synaptobrevin homolog 1","length":117,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000135B22","genes":[{"name":{"value":"SNC1"},"olnNames":[{"value":"YAL030W"}]}],"alphafold_very_low_content":0.03418803418803419,"disorder_content":0.7948717948717948,"disprot_consensus":{"full":[{"start":1,"end":93,"type":"T"}],"Structural state":[{"start":1,"end":93,"type":"D"}],"Structural transition":[{"start":1,"end":93,"type":"T"}],"Molecular function":[{"start":1,"end":93,"type":"F"}]}},{"features":{"pfam":[{"id":"PF25890","name":"Osteocalcin, C-terminal domain","start":14,"end":48}]},"uniref50":"UniRef50_P02818","sequence":"YLDSGLGAPVPYPDPLEPKREVCELNPNCDELADHIGFQEAYQRFYGPV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Carnivora","Caniformia","Canidae","Canis"],"uniref90":"UniRef90_P81455","disprot_id":"DP00116","ncbi_taxon_id":9615,"regions_counter":3,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":49,"region_id":"DP00116r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Metal ion binding to dog osteocalcin studied by 1H NMR spectroscopy. <i> Isbell DT, Du S, Schroering AG, Colombo G, Shelling JG. </i> Biochemistry, 1993","term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"8218200","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"Neither the 3,5 (6.70-6.90 ppm) nor the 2.6 (7.00-7.24 ppm) resonances of the four Tyr residues in apo BGP were equivalent, indicating that the apoprotein had some tertiary structure (Figure 1A).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-09T15:26:51.873Z"}},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":49,"term_name":"disorder to order","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"8218200","version":3,"reference_html":"Metal ion binding to dog osteocalcin studied by 1H NMR spectroscopy. <i> Isbell DT, Du S, Schroering AG, Colombo G, Shelling JG. </i> Biochemistry, 1993","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00116r002","curator_orcid":"0000-0002-5152-5953","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"These results showed that dog osteocalcin undergoes a major conformational change when it associates with calcium and that its calcium affinity is relatively strong (Kd < 10-4 M).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-09T15:26:50.680Z"}},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":49,"term_name":"calcium ion binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"8218200","version":4,"reference_html":"Metal ion binding to dog osteocalcin studied by 1H NMR spectroscopy. <i> Isbell DT, Du S, Schroering AG, Colombo G, Shelling JG. </i> Biochemistry, 1993","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005509","ec_id":"ECO:0006165","region_id":"DP00116r003","curator_orcid":"0000-0002-5152-5953","interaction_partner":[{"db":"ChEBI","id":"29108","partner_start":null,"partner_end":null}],"statement":[{"text":"These results showed that dog osteocalcin undergoes a major conformational change when it associates with calcium and that its calcium affinity is relatively strong (Kd < 10-4 M).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-09T15:26:52.630Z"}}],"released":"2016_10","uniref100":"UniRef100_P81455","date":"2016-08-23T15:57:38.000Z","acc":"P81455","name":"Osteocalcin","length":49,"organism":"Canis lupus familiaris","dataset":[],"UniParc":"UPI0000130EDA","genes":[{"name":{"value":"BGLAP"}}],"alphafold_very_low_content":0.12244897959183673,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":49,"type":"T"}],"Structural state":[{"start":1,"end":49,"type":"D"}],"Structural transition":[{"start":1,"end":49,"type":"T"}],"Molecular function":[{"start":1,"end":49,"type":"F"}]}},{"acc":"P05059","sequence":"MRSAAVLALLLCAGQVIALPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSKECFETLRGDERILSILRHQNLLKELQDLALQGAKERTHQQKKHSSYEDELSEVLEKPNDQAEPKEVTEEVSSKDAAEKRDDFKEVEKSDEDSDGDRPQASPGLGPGPKVEEDNQAPGEEEEAPSNAHPLASLPSPKYPGPQAKEDSEGPSQGPASREKGLSAEQGRQTEREEEEEKWEEAEAREKAVPEEESPPTAAFKPPPSLGNKETQRAAPGWPEDGAGKMGAEEAKPPEGKGEWAHSRQEEEEMARAPQVLFRGGKSGEPEQEEQLSKEWEDAKRWSKMDQLAKELTAEKRLEGEEEEEEDPDRSMRLSFRARGYGFRGPGLQLRRGWRPNSREDSVEAGLPLQVRGYPEEKKEEEGSANRRPEDQELESLSAIEAELEKVAHQLEELRRG","alphafold_very_low_content":"0.48775055679287305","creator":"ftonello","dataset":[],"date":"2016-09-08T12:01:24.000Z","disprot_id":"DP00118","features":{"pfam":[{"id":"PF01271","name":"Granin (chromogranin or secretogranin)","start":88,"end":449}]},"genes":[{"name":{"value":"CHGA","evidences":[],"_id":"685af523b4ac24d5329d78be"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d78bd"}],"length":449,"name":"Chromogranin-A","ncbi_taxon_id":9913,"organism":"Bos taurus","regions_counter":15,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"UniParc":"UPI0000127BCC","uniref100":"UniRef100_P05059","uniref50":"UniRef50_P05059","uniref90":"UniRef90_P05059","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":449,"interaction_partner":[],"reference_html":"The character of the stored molecules in chromaffin granules of the adrenal medulla: a nuclear magnetic resonance study. <i> Daniels AJ, Williams RJ, Wright PE. </i> Neuroscience, 1978","reference_id":"692872","region_id":"DP00118r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The NMR spectrum of purified chromogranin A in D2O at pH 6.05 shown in Fig. 7(a) is in general closely similar to that computed for an extended random coil by the method of MACDONALD & PHILLIPS (1969) shown in Fig. 7(c).","_id":"685af523b4ac24d5329d7893"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2024-11-14T13:19:43.854Z","_id":"685af523b4ac24d5329d7894"},"version":3,"_id":"685af523b4ac24d5329d7892","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[{"deviation":null,"statements":[],"term_id":"NCIT:C45997","unit_id":"UO:0000196","unit_name":"pH","value":7.5,"_id":"685af523b4ac24d5329d78a0"}],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":407,"end":431,"interaction_partner":[],"reference_html":"Nature of the pH-induced conformational changes and exposure of the C-terminal region of chromogranin A. <i> Yoo SH, Ferretti JA. </i> FEBS Lett, 1993","reference_id":"8243650","region_id":"DP00118r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The CD spectra showed that the magnitude of molar ellipticity at 222 nm increased as the pH was changed from 7.5 to 5.5. The increase in the magnitude of the molar ellipticity in the region from -207 to -225 nm indicates an increase of a-helicity at pH 5.5, while the decrease in the magnitude of molar ellipticity at -200 nm indicates a  decrease of coil structure as the pH changed from 7.5 to 5.5 [13-15].","_id":"685af523b4ac24d5329d78a1"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2024-11-14T13:19:36.408Z","_id":"685af523b4ac24d5329d78a2"},"version":3,"_id":"685af523b4ac24d5329d789f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[{"deviation":null,"statements":[],"term_id":"NCIT:C45997","unit_id":"UO:0000196","unit_name":"pH","value":7.5,"_id":"685af523b4ac24d5329d78a4"}],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":407,"end":431,"interaction_partner":[],"reference_html":"Nature of the pH-induced conformational changes and exposure of the C-terminal region of chromogranin A. <i> Yoo SH, Ferretti JA. </i> FEBS Lett, 1993","reference_id":"8243650","region_id":"DP00118r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The CD spectra showed that the magnitude of molar ellipticity at 222 nm increased as the pH was changed from 7.5 to 5.5. The increase in the magnitude of the molar ellipticity in the region from -207 to -225 nm indicates an increase of a-helicity at pH 5.5, while the decrease in the magnitude of molar ellipticity at -200 nm indicates a  decrease of coil structure as the pH changed from 7.5 to 5.5 [13-15].","_id":"685af523b4ac24d5329d78a5"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2025-02-20T17:32:36.991Z","_id":"685af523b4ac24d5329d78a6"},"version":3,"_id":"685af523b4ac24d5329d78a3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-24T10:27:28.352Z","disprot_namespace":"Structural transition","ec_go":"IDA","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":449,"interaction_partner":[],"reference_html":"Ca2(+)-induced conformational change and aggregation of chromogranin A. <i> Yoo SH, Albanesi JP. </i> J Biol Chem, 1990","reference_id":"2387861","region_id":"DP00118r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Therefore, the increased binding of bis-ANS is probably due to a Ca2+-induced conformational change in CGA rather than a mere charge neutralization of bis-ANS by Ca2+.","_id":"685af523b4ac24d5329d78aa"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2025-02-20T17:32:32.833Z","_id":"685af523b4ac24d5329d78ab"},"version":0,"_id":"685af523b4ac24d5329d78a9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-11-14T13:21:01.905Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":449,"interaction_partner":[],"reference_html":"Ca2(+)-induced conformational change and aggregation of chromogranin A. <i> Yoo SH, Albanesi JP. </i> J Biol Chem, 1990","reference_id":"2387861","region_id":"DP00118r011","released":"2024_12","sample":[],"statement":[{"type":"Results","text":"Therefore, the increased binding of bis-ANS is probably due to a Ca2+-induced conformational change in CGA rather than a mere charge neutralization of bis-ANS by Ca2+.","_id":"685af523b4ac24d5329d78ad"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a calcium ion (Ca2+).\" [GOC:ai]","term_go_domain":"F","term_id":"GO:0005509","term_is_binding":true,"term_is_obsolete":false,"term_name":"calcium ion binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":2,"_id":"685af523b4ac24d5329d78ac","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[{"deviation":null,"statements":[],"term_id":"NCIT:C45997","unit_id":"UO:0000196","unit_name":"pH","value":5.5,"_id":"685af523b4ac24d5329d78af"}],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-11-14T13:20:45.616Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":449,"interaction_partner":[],"reference_html":"Ca2(+)-induced conformational change and aggregation of chromogranin A. <i> Yoo SH, Albanesi JP. </i> J Biol Chem, 1990","reference_id":"2387861","region_id":"DP00118r012","released":"2024_12","sample":[],"statement":[{"type":"Results","text":"The nature of the Ca2+-induced conformational changes of CGA was studied by circular dichroism in the presence and absence of Ca2+. As shown in Fig. 2, the CD spectrum of CGA at pH 5.5 was significantly changed in the presence of 15 mM Ca2+.","_id":"685af523b4ac24d5329d78b0"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a calcium ion (Ca2+).\" [GOC:ai]","term_go_domain":"F","term_id":"GO:0005509","term_is_binding":true,"term_is_obsolete":false,"term_name":"calcium ion binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":2,"_id":"685af523b4ac24d5329d78ae","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[{"deviation":null,"statements":[],"term_id":"NCIT:C45997","unit_id":"UO:0000196","unit_name":"pH","value":5.5,"_id":"685af523b4ac24d5329d78b2"}],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-24T10:30:15.585Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":449,"interaction_partner":[],"reference_html":"Ca2(+)-induced conformational change and aggregation of chromogranin A. <i> Yoo SH, Albanesi JP. </i> J Biol Chem, 1990","reference_id":"2387861","region_id":"DP00118r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The nature of the Ca2+-induced conformational changes of CGA was studied by circular dichroism in the presence and absence of Ca2+. As shown in Fig. 2, the CD spectrum of CGA at pH 5.5 was significantly changed in the presence of 15 mM Ca2+.","_id":"685af523b4ac24d5329d78b3"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2025-02-20T17:32:43.059Z","_id":"685af523b4ac24d5329d78b4"},"version":0,"_id":"685af523b4ac24d5329d78b1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[{"deviation":null,"statements":[],"term_id":"NCIT:C45997","unit_id":"UO:0000196","unit_name":"pH","value":5.5,"_id":"685af523b4ac24d5329d78b6"}],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-24T10:46:22.752Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":449,"interaction_partner":[],"reference_html":"Nature of the pH-induced conformational changes and exposure of the C-terminal region of chromogranin A. <i> Yoo SH, Ferretti JA. </i> FEBS Lett, 1993","reference_id":"8243650","region_id":"DP00118r014","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As shown in Fig. 1A, chromogranin A was proteolyzed into small fragments by trypsin at pH 5.5.","_id":"685af523b4ac24d5329d78b7"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2024-11-14T13:19:32.330Z","_id":"685af523b4ac24d5329d78b8"},"version":0,"_id":"685af523b4ac24d5329d78b5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[{"deviation":null,"statements":[],"term_id":"NCIT:C45997","unit_id":"UO:0000196","unit_name":"pH","value":7.5,"_id":"685af523b4ac24d5329d78ba"}],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-24T10:48:00.987Z","disprot_namespace":"Structural transition","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":449,"interaction_partner":[],"reference_html":"Nature of the pH-induced conformational changes and exposure of the C-terminal region of chromogranin A. <i> Yoo SH, Ferretti JA. </i> FEBS Lett, 1993","reference_id":"8243650","region_id":"DP00118r015","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"A with a  size of -60 kDa remained relatively intact at pH 7.5 whereas the same fragment was proteolyzed continuously by trypsin at pH 5.5, suggesting that the N-terminal core structure is more compact and better protected at pH 7.5. ","_id":"685af523b4ac24d5329d78bb"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2025-02-20T17:33:07.529Z","_id":"685af523b4ac24d5329d78bc"},"version":0,"_id":"685af523b4ac24d5329d78b9","reference_source":"pmid"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":449,"type":"T"}],"Structural state":[{"start":1,"end":449,"type":"D"}],"Structural transition":[{"start":1,"end":449,"type":"T"}],"Molecular function":[{"start":1,"end":449,"type":"F"}]}},{"acc":"P10163","sequence":"MLLILLSVALLALSSAESSSEDVSQEESLFLISGKPEGRRPQGGNQPQRPPPPPGKPQGPPPQGGNQSQGPPPPPGKPEGRPPQGGNQSQGPPPHPGKPERPPPQGGNQSQGPPPHPGKPESRPPQGGHQSQGPPPTPGKPEGPPPQGGNQSQGTPPPPGKPEGRPPQGGNQSQGPPPHPGKPERPPPQGGNQSHRPPPPPGKPERPPPQGGNQSQGPPPHPGKPEGPPPQEGNKSRSARSPPGKPQGPPQQEGNKPQGPPPPGKPQGPPPAGGNPQQPQAPPAGKPQGPPPPPQGGRPPRPAQGQQPPQ","alphafold_very_low_content":"0.4","creator":"mnecci","dataset":[],"date":"2016-08-24T15:01:18.000Z","disprot_id":"DP00119","features":{"pfam":[{"id":"PF15240","name":"Proline-rich protein","start":1,"end":177},{"id":"PF15240","name":"Proline-rich protein","start":198,"end":304}]},"genes":[{"name":{"value":"PRB4","evidences":[],"_id":"685af523b4ac24d5329d78c9"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d78c8"}],"length":310,"name":"Basic salivary proline-rich protein 4","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":3,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI00015B3CEA","uniref100":"UniRef100_P10163","uniref50":"UniRef50_Q04118","uniref90":"UniRef90_P10163","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":17,"end":310,"interaction_partner":[],"reference_html":"Circular dichroism and fluorescence spectroscopic analyses of a proline-rich glycoprotein from human parotid saliva. <i> Loomis RE, Bergey EJ, Levine MJ, Tabak LA. </i> Int J Pept Protein Res, 1985","reference_id":"4093242","region_id":"DP00119r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Since the PRG CD spectrum differed from the poly-L-proline II helical structure and did not respond to CaCl1, the implication was that the proline present in PRG exists in a disordered state (i.e. a mixture of cis and/ or trans isomers).","_id":"685af523b4ac24d5329d78c3"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d78c2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-24T11:04:11.571Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":17,"end":310,"interaction_partner":[],"reference_html":"Circular dichroism and fluorescence spectroscopic analyses of a proline-rich glycoprotein from human parotid saliva. <i> Loomis RE, Bergey EJ, Levine MJ, Tabak LA. </i> Int J Pept Protein Res, 1985","reference_id":"4093242","region_id":"DP00119r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"These data imply that all of the lysine residues in Dns-PRG are exposed to solvent in the native form.","_id":"685af523b4ac24d5329d78c7"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":0,"_id":"685af523b4ac24d5329d78c6","reference_source":"pmid"}],"__v":0,"disorder_content":0.9483870967741935,"disprot_consensus":{"full":[{"start":17,"end":310,"type":"D"}],"Structural state":[{"start":17,"end":310,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02029","name":"Caldesmon","start":31,"end":223},{"id":"PF02029","name":"Caldesmon","start":242,"end":738}]},"uniref50":"UniRef50_P12957","sequence":"MDDFERRRELRRQKREEMRLEAERLSYQRNDDDEEEAARERRRRARQERLRQKEEGDVSGEVTEKSEVNAQNSVAEEETKRSTDDEAALLERLARREERRQKRLQEALERQKEFDPTITDGSLSVPSRREVNNVEENEITGKEEKVETRQGRCEIEETETVTKSYQRNNWRQDGEEEGKKEEKDSEEEKPKEVPTEENQVDVAVEKSTDKEEVVETKTLAVNAENDTNAMLEGEQSITDAADKEKEEAEKEREKLEAEEKERLKAEEEKKAAEEKQKAEEEKKAAEERERAKAEEEKRAAEERERAKAEEERKAAEERERAKAEEERKAAEERAKAEEERKAAEERAKAEEERKAAEERAKAEKERKAAEERERAKAEEEKRAAEEKARLEAEKLKEKKKMEEKKAQEEKAQANLLRKQEEDKEAKVEAKKESLPEKLQPTSKKDQVKDNKDKEKAPKEEMKSVWDRKRGVPEQKAQNGERELTTPKLKSTENAFGRSNLKGAANAEAGSEKLKEKQQEAAVELDELKKRREERRKILEEEEQKKKQEEAERKIREEEEKKRMKEEIERRRAEAAEKRQKVPEDGVSEEKKPFKCFSPKGSSLKIEERAEFLNKSAQKSGMKPAHTTAVVSKIDSRLEQYTSAVVGNKAAKPAKPAASDLPVPAEGVRNIKSMWEKGNVFSSPGGTGTPNKETAGLKVGVSSRINEWLTKTPEGNKSPAPKPSDLRPGDVSGKRNLWEKQSVEKPAASSSKVTATGKKSETNGLRQFEKEP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Phasianinae","Gallus"],"uniref90":"UniRef90_P12957","disprot_id":"DP00120","ncbi_taxon_id":9031,"regions_counter":27,"creator":"fquaglia","regions":[{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":771,"term_name":"calmodulin binding","start":636,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"This spectrum was calculated assuming that both proteins are completely involved into the complex formation and a difference between the measured CaD136‐CaM and CaM spectra are due to the partial folding of CaD136 rather than a partial unfolding of CaM; i.e., as [(CaD136‐CaM − 0.5 ÷ CaM)/0.5].","type":"Figure"},{"text":"Figure 7 shows that the formation of CaD136–CaM complex led to a partial folding of the natively unfolded CaD136. As it was already pointed out, in the absence of CaM CaD136 possesses a far‐UV CD spectrum typical of an essentially unfolded polypeptide chain; i.e., a spectrum with an intense minimum in the vicinity of 200 nm, and the absence of characteristic bands in the 210–230 nm region. However, as the CaD136–CaM complex was formed, the minimum at 200 nm became less intense and shifted toward the longer wavelength, whereas the negative intensity of the spectrum around 222 nm increased, reflecting the formation of ordered secondary structure. Importantly, the extent of this folding was relatively low and CaD136 remained substantially unstructured even after the effective binding to CaM. Potentially, there is an alternative scenario of CaD136 binding to CaM, where CaD136 gains some sort of rigid but nonregular structure as a result of complex formation.","type":"Results"}],"curator_id":"fquaglia","released":"2023_06","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"14635127","version":5,"reference_html":"Natively unfolded C-terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin. <i> Permyakov SE, Millett IS, Doniach S, Permyakov EA, Uversky VN. </i> Proteins, 2003","date":"2023-01-19T14:15:59.004Z","term_id":"GO:0005516","ec_id":"ECO:0006204","region_id":"DP00120r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P62149","operator":"and","partner_start":null,"partner_end":null}]},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":771,"region_id":"DP00120r009","reference_id":"14635127","start":636,"ec_id":"ECO:0007680","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"To obtain information about the hydrodynamic dimensions of CaD136, the gel‐filtration behavior of this protein at neutral pH in the absence or in the presence of 6 M GdmCl was studied. Chromatographic analysis confirmed the results of other techniques and showed that CaD136 was essentially unfolded under the conditions of neutral pH. In fact, we have established that the hydrodynamic dimensions of CaD136 are relatively close to those measured in the presence of 6 M GdmCl (RS = 28.1 ± 0.8 and 35.3 ± 0.8 Å, respectively), confirming the fact that CaD136 is essentially unfolded even in the absence of denaturant.","type":"Results"},{"text":"We are showing in this article that the functionally important C‐terminal domain of CaD, CaD136, is an intrinsically unstructured. In fact, it shows large hydrodynamic dimensions (gel‐filtration and SAXS), does not have cooperatively melted tertiary structure (DSC), possesses absence of globular structure (SAXS), and is characterized by low content of ordered secondary structure (far‐UV CD).","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"chromatography evidence used in manual assertion","version":3,"reference_html":"Natively unfolded C-terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin. <i> Permyakov SE, Millett IS, Doniach S, Permyakov EA, Uversky VN. </i> Proteins, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-19T12:44:20.159Z"}},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":771,"region_id":"DP00120r013","reference_id":"14635127","start":636,"ec_id":"ECO:0006210","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Figure 5(A) represents the results of Guinier analysis of the scattering data for CaD136. The linear Guinier plot indicates that the solution of this protein was homogeneous. The radius of gyration of a random coil, Rurn:x-wiley:08873585:media:PROT10481:tex2gif-stack-6, may be estimated from the corresponding Stokes radius, Rurn:x-wiley:08873585:media:PROT10481:tex2gif-stack-7, using the relation Rurn:x-wiley:08873585:media:PROT10481:tex2gif-stack-8/Rurn:x-wiley:08873585:media:PROT10481:tex2gif-stack-9 = 1.51.45 The observed Rg value for CaD136 (40.8 ± 0.8 Å) is smaller than that estimated for a random coil conformation for a protein of this size (51.9 Å), indicating that the natively unfolded conformation of this protein is in fact more compact than that of a random coil. Finally, analysis of the X‐ray scattering data in a form of the Kratky plot shows that CaD136 does not have any well‐developed globular structure [Fig. 5(B)]. ","type":"Results"},{"text":"We are showing in this article that the functionally important C‐terminal domain of CaD, CaD136, is an intrinsically unstructured. In fact, it shows large hydrodynamic dimensions (gel‐filtration and SAXS), does not have cooperatively melted tertiary structure (DSC), possesses absence of globular structure (SAXS), and is characterized by low content of ordered secondary structure (far‐UV CD).","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":3,"reference_html":"Natively unfolded C-terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin. <i> Permyakov SE, Millett IS, Doniach S, Permyakov EA, Uversky VN. </i> Proteins, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-19T12:38:49.049Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":771,"region_id":"DP00120r021","reference_id":"14635127","start":636,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The effect of temperature on CaD136 structure was further analyzed by DSC. We have established that CaD136 is characterized by the absence of distinct heat sorption peaks within the temperature region from 10°C to 110°C, indicative of the absence of rigid tertiary structure for the protein.","type":"Results"},{"text":"We are showing in this article that the functionally important C‐terminal domain of CaD, CaD136, is an intrinsically unstructured. In fact, it shows large hydrodynamic dimensions (gel‐filtration and SAXS), does not have cooperatively melted tertiary structure (DSC), possesses absence of globular structure (SAXS), and is characterized by low content of ordered secondary structure (far‐UV CD).","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"differential scanning calorimetry evidence used in manual assertion","version":3,"reference_html":"Natively unfolded C-terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin. <i> Permyakov SE, Millett IS, Doniach S, Permyakov EA, Uversky VN. </i> Proteins, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006232","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-19T12:37:40.673Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":771,"region_id":"DP00120r022","reference_id":"14635127","start":636,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Figure 2 represents tryptophan fluorescence spectra of CD136. It is clearly seen that the spectrum of free CaD136 has maximum at about 350.2 nm; i.e., it is close to that of tryptophan in water (351.5 nm). This indicates that the CaD136 tryptophan residues are almost totally exposed to water. ","type":"Results"}],"curator_id":"fquaglia","released":"2023_06","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"fluorescence evidence used in manual assertion","version":4,"reference_html":"Natively unfolded C-terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin. <i> Permyakov SE, Millett IS, Doniach S, Permyakov EA, Uversky VN. </i> Proteins, 2003","date":"2023-01-19T14:10:28.684Z","reference_source":"pmid","ec_id":"ECO:0001249","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":771,"region_id":"DP00120r023","reference_id":"14635127","start":636,"term_id":"GO:0005516","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Chicken gizzard CaD contains five tryptophan residues per protein molecule; three of them, Trp674, Trp707, and Trp737, are located within the CaD136 domain. On the other hand, CaM does not have any Trp residues. This implies changes in the CaD136 intrinsic tryptophan fluorescence as fast and easy method to detect CaD‐CaM complex formation.","type":"Results"},{"text":"Figure 2 compares the tryptophan fluorescence spectra (excitation at 296.7 nm) of CaD136 measured in the absence or presence of CaM. Notably, excess of Ca2+ (5 mM CaCl2) was used to saturate CaM by calcium, which is a necessary condition of effective binding of CaM by CaD.11 The temperature was kept at 20°C in order to distance from thermal transition of Ca2+‐loaded CaM. It can be seen that CaM binding to CaD136 led to the considerable (1.9‐fold) increase in the fluorescence quantum yield and an essential (17 nm) blue shift of the CaD136 fluorescence spectrum, reflecting the transfer of tryptophans into the less mobile and polar environment.","type":"Results"},{"text":"This most likely reflects some CaM‐induced compaction of a polypeptide chain at least in the vicinity of tryptophans or these changes in fluorescence are due to the insertion of Trp into a hydrophobic binding pocket on the CaM. These observations have been used to evaluate the binding parameters of CaD136‐CaM complex (see Fig. 6). It should be noted that the characteristic bend of the CaM‐titration curve in Figure 6, corresponding to saturation of CaD136 by CaM, takes place around CaM to CaD136 ratio about 1, which is an evidence of the binding of a single CaM molecule per CaD136 molecule","type":"Results"}],"curator_id":"fquaglia","released":"2023_06","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"experimental evidence used in manual assertion","version":5,"reference_html":"Natively unfolded C-terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin. <i> Permyakov SE, Millett IS, Doniach S, Permyakov EA, Uversky VN. </i> Proteins, 2003","date":"2023-01-19T14:15:47.298Z","reference_source":"pmid","ec_id":"ECO:0000269","term_name":"calmodulin binding","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P62149","operator":"and","partner_start":null,"partner_end":null}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":771,"region_id":"DP00120r025","reference_id":"14635127","start":636,"term_id":"IDPO:0000004","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Figure 1(A) represents far‐UV CD spectra of CaD136 measured at different temperatures. At low temperature this protein is characterized by a far‐UV CD spectrum typical of an essentially unfolded polypeptide chain. On the other hand, more detailed analysis of far UV CD spectrum shows that CaD136, being considerably distorted, is still far from to be completely unfolded and preserves some residual structure [e.g., [θ]222 ∼ −2500° cm2 dmol−1, the minimum is located at 200, rather than at 196–198 nm; see Fig. 1(A)].","type":"Results"},{"text":"It has been noted that such structure forming effect of heating, being typical of the intrinsically unstructured proteins, might be ascribed to the heat‐induced intensification of the hydrophobic interactions.","type":"Results"},{"text":"As it was already pointed out, in the absence of CaM CaD136 possesses a far‐UV CD spectrum typical of an essentially unfolded polypeptide chain; i.e., a spectrum with an intense minimum in the vicinity of 200 nm, and the absence of characteristic bands in the 210–230 nm region.","type":"Results"},{"text":"We are showing in this article that the functionally important C‐terminal domain of CaD, CaD136, is an intrinsically unstructured. In fact, it shows large hydrodynamic dimensions (gel‐filtration and SAXS), does not have cooperatively melted tertiary structure (DSC), possesses absence of globular structure (SAXS), and is characterized by low content of ordered secondary structure (far‐UV CD).","type":"Discussion"},{"text":"Moreover, our data are consistent with the conclusion that CaD136 is not completely unfolded, belonging to the subclass of the native premolten globules, according to its hydrodynamic properties and far‐UV CD spectrum.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"reference_html":"Natively unfolded C-terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin. <i> Permyakov SE, Millett IS, Doniach S, Permyakov EA, Uversky VN. </i> Proteins, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"pre-molten globule","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-19T12:30:42.942Z"}}],"released":"2016_10","uniref100":"UniRef100_P12957","date":"2016-08-11T15:22:00.000Z","acc":"P12957","name":"Caldesmon","length":771,"organism":"Gallus gallus","dataset":[],"UniParc":"UPI00001713AB","genes":[{"name":{"value":"CALD1"},"synonyms":[{"value":"CAD"}]}],"alphafold_very_low_content":0.4059662775616083,"disorder_content":0.17639429312581065,"disprot_consensus":{"full":[{"start":636,"end":771,"type":"D"}],"Structural state":[{"start":636,"end":771,"type":"D"}],"Molecular function":[{"start":636,"end":771,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00418","name":"Tau and MAP protein, tubulin-binding repeat","start":1667,"end":1694},{"id":"PF00418","name":"Tau and MAP protein, tubulin-binding repeat","start":1695,"end":1725},{"id":"PF00418","name":"Tau and MAP protein, tubulin-binding repeat","start":1726,"end":1756},{"id":"PF00418","name":"Tau and MAP protein, tubulin-binding repeat","start":1757,"end":1788},{"id":"PF08377","name":"MAP2/Tau projection domain","start":378,"end":1512}]},"uniref50":"UniRef50_P15146","sequence":"MADERKDEGKAPHWTSASLTEAAAHPHSPEMKDQGGSGEGLSRSANGFPYREEEEGAFGEHGSQGTYSDTKENGINGELTSADRETAEEVSARIVQVVTAEAVAVLKGEQEKEAQHKDQPAALPLAAEETVNLPPSPPPSPASEQTAALEEDLLTASKMEFPEQQKLPSSFAEPLDKEETEFKMQSKPGEDFEHAALVPQPDTSKTPQDKKDPQDMEGEKSPASPFAQTFGTNLEDIKQITEPSITVPSIGLSAEPLAPKDQKDWFIEMPVESKKDEWGLAAPISPGPLTPMREKDVLEDIPRWEGKQFDSPMPSPFHGGSFTLPLDTVKDERVTEGSQPFAPVFFQSDDKMSLQDTSGSATSKESSKDEEPQKDKADKVADVPVSEATTVLGDVHSPAVEGFVGENISGEEKGTTDQEKKETSTPSVQEPTLTETEPQTKLEETSKVSIEETVAKEEESLKLKDDKAGVIQTSTEQSFSKEDQKGQEQTIEALKQDSFPISLEQAVTDAAMATKTLEKVTSEPEAVSEKREIQGLFEEDIADKSKLEGAGSATVAEVEMPFYEDKSGMSKYFETSALKEDVTRSTGLGSDYYELSDSRGNAQESLDTVSPKNQQDEKELLAKASQPSPPAHEAGYSTLAQSYTSDHPSELPEEPSSPQERMFTIDPKVYGEKRDLHSKNKDDLTLSRSLGLGGRSAIEQRSMSINLPMSCLDSIALGFNFGRGHDLSPLASDILTNTSGSMDEGDDYLPPTTPAVEKIPCFPIESKEEEDKTEQAKVTGGQTTQVETSSESPFPAKEYYKNGTVMAPDLPEMLDLAGTRSRLASVSADAEVARRKSVPSEAVVAESSTGLPPVADDSQPVKPDSQLEDMGYCVFNKYTVPLPSPVQDSENLSGESGSFYEGTDDKVRRDLATDLSLIEVKLAAAGRVKDEFTAEKEASPPSSADKSGLSREFDQDRKANDKLDTVLEKSEEHVDSKEHAKESEEVGDKVELFGLGVTYEQTSAKELITTKETAPERAEKGLSSVPEVAEVETTTKADQGLDVAAKKDDQSPLDIKVSDFGQMASGMSVDAGKTIELKFEVDQQLTLSSEAPQETDSFMGIESSHVKDGAKVSETEVKEKVAKPDLVHQEAVDKEESYESSGEHESLTMESLKPDEGKKETSPETSLIQDEVALKLSVEIPCPPPVSEADSSIDEKAEVQMEFIQLPKEESTETPDIPAIPSDVTQPQPEAVVSEPAEVRGEEEEIEAEGEYDKLLFRSDTLQITDLLVPGSREEFVETCPGEHKGVVESVVTIEDDFITVVQTTTDEGELGSHSVRFAAPVQPEEERRPYPHDEELEVLMAAEAQAEPKDGSPDAPATPEKEEVPFSEYKTETYDDYKDETTIDDSIMDADSLWVDTQDDDRSILTEQLETIPKEERAEKEARRPSLEKHRKEKPFKTGRGRISTPERREVAKKEPSTVSRDEVRRKKAVYKKAELAKESEVQAHSPSRKLILKPAIKYTRPTHLSCVKRKTTATSGESAQAPSAFKQAKDKVTDGITKSPEKRSSLPRPSSILPPRRGVSGDREENSFSLNSSISSARRTTRSEPIRRAGKSGTSTPTTPGSTAITPGTPPSYSSRTPGTPGTPSYPRTPGTPKSGILVPSEKKVAIIRTPPKSPATPKQLRLINQPLPDLKNVKSKIGSTDNIKYQPKGGQVRILNKKMDFSKVQSRCGSKDNIKHSAGGGNVQIVTKKIDLSHVTSKCGSLKNIRHRPGGGRVKIESVKLDFKEKAQAKVGSLDNAHHVPGGGNVKIDSQKLNFREHAKARVDHGAEIITQSPSRSSVASPRRLSNVSSSGSINLLESPQLATLAEDVTAALAKQGL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_P15146","disprot_id":"DP00122","ncbi_taxon_id":10116,"regions_counter":9,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":135,"region_id":"DP00122r001","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Primary contact sites in intrinsically unstructured proteins: the case of calpastatin and microtubule-associated protein 2. <i> Csizmók V, Bokor M, Bánki P, Klement E, Medzihradszky KF, Friedrich P, Tompa K, Tompa P. </i> Biochemistry, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15751971","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-01-18T16:23:30.664Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The spectra of the two halves in this case are very similar, and their sum reproduces the spectrum of the full-length protein within experimental error. This finding is consistent with the overall random structure of MAP2c and the lack of appreciable long-range interactions between its two halves.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":467,"region_id":"DP00122r003","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Primary contact sites in intrinsically unstructured proteins: the case of calpastatin and microtubule-associated protein 2. <i> Csizmók V, Bokor M, Bánki P, Klement E, Medzihradszky KF, Friedrich P, Tompa K, Tompa P. </i> Biochemistry, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":298,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15751971","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-01-18T16:23:18.196Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The spectra of the two halves in this case are very similar, and their sum reproduces the spectrum of the full-length protein within experimental error. This finding is consistent with the overall random structure of MAP2c and the lack of appreciable long-range interactions between its two halves.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":297,"region_id":"DP00122r005","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Primary contact sites in intrinsically unstructured proteins: the case of calpastatin and microtubule-associated protein 2. <i> Csizmók V, Bokor M, Bánki P, Klement E, Medzihradszky KF, Friedrich P, Tompa K, Tompa P. </i> Biochemistry, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":136,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15751971","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-01-18T16:18:30.492Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The spectrum of MAP2c also shows a characteristic minimum at 200 nm and is compatible with a random-coil conformation (Figure 5B).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":297,"region_id":"DP00122r008","released":"2023_06","ec_id":"ECO:0007691","reference_html":"Primary contact sites in intrinsically unstructured proteins: the case of calpastatin and microtubule-associated protein 2. <i> Csizmók V, Bokor M, Bánki P, Klement E, Medzihradszky KF, Friedrich P, Tompa K, Tompa P. </i> Biochemistry, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":136,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15751971","version":3,"ec_name":"cleavage assay evidence used in manual assertion","date":"2023-01-18T16:17:45.967Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"Limited proteolysis of MAP2c (Figure 2) also results in a nonrandom cleavage, demonstrating different accessibility of its large number of potentially vulnerable sites.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P15146","date":"2016-09-14T14:38:47.000Z","acc":"P15146","name":"Microtubule-associated protein 2","length":1861,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI000012EBBC","genes":[{"name":{"value":"Map2"},"synonyms":[{"value":"Mtap2"}]}],"alphafold_very_low_content":0.8699623858140785,"disorder_content":0.2509403546480387,"disprot_consensus":{"full":[{"start":1,"end":467,"type":"D"}],"Structural state":[{"start":1,"end":467,"type":"D"}]}},{"acc":"P01730","sequence":"MNRGVPFRHLLLVLQLALLPAATQGKKVVLGKKGDTVELTCTASQKKSIQFHWKNSNQIKILGNQGSFLTKGPSKLNDRADSRRSLWDQGNFPLIIKNLKIEDSDTYICEVEDQKEEVQLLVFGLTANSDTHLLQGQSLTLTLESPPGSSPSVQCRSPRGKNIQGGKTLSVSQLELQDSGTWTCTVLQNQKKVEFKIDIVVLAFQKASSIVYKKEGEQVEFSFPLAFTVEKLTGSGELWWQAERASSSKSWITFDLKNKEVSVKRVTQDPKLQMGKKLPLHLTLPQALPQYAGSGNLTLALEAKTGKLHQEVNLVVMRATQLQKNLTCEVWGPTSPKLMLSLKLENKEAKVSKREKAVWVLNPEAGMWQCLLSDSGQVLLESNIKVLPTWSTPVQPMALIVLGGVAGLLLFIGLGIFFCVRCRHRRRQAERMSQIKRLLSEKKTCQCPHRFQKTCSPI","alphafold_very_low_content":"0.0851528384279476","creator":"gminervini","dataset":[],"date":"2016-08-23T16:16:58.000Z","disprot_id":"DP00123","features":{"pfam":[{"id":"PF00047","name":"Immunoglobulin domain","start":29,"end":119},{"id":"PF05790","name":"Immunoglobulin C2-set domain","start":126,"end":202},{"id":"PF05790","name":"Immunoglobulin C2-set domain","start":317,"end":389},{"id":"PF09191","name":"CD4, extracellular","start":206,"end":316},{"id":"PF12104","name":"T cell CD4 receptor C terminal region","start":402,"end":449}],"gene3D":[{"start":317,"end":388,"id":"2.60.40.10","name":"Immunoglobulins","_id":"685af523b4ac24d5329d78cf"},{"start":206,"end":316,"id":"2.60.40.10","name":"Immunoglobulins","_id":"685af523b4ac24d5329d78d0"},{"start":124,"end":198,"id":"2.60.40.10","name":"Immunoglobulins","_id":"685af523b4ac24d5329d78d1"},{"start":23,"end":123,"id":"2.60.40.10","name":"Immunoglobulins","_id":"685af523b4ac24d5329d78d2"},{"start":390,"end":458,"id":"1.20.5.900","name":"transmembrane domain of human cd4","_id":"685af523b4ac24d5329d78d3"}]},"genes":[{"name":{"value":"CD4","evidences":[],"_id":"685af523b4ac24d5329d790d"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d790c"}],"length":458,"name":"T-cell surface glycoprotein CD4","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":16,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000001294","uniref100":"UniRef100_P01730","uniref50":"UniRef50_P01730","uniref90":"UniRef90_P01730","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-24T11:29:39.462Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":396,"end":433,"interaction_partner":[],"reference_html":"Solution structure of the cytoplasmic domain of the human CD4 glycoprotein by CD and 1H NMR spectroscopy: implications for biological functions. <i> Wray V, Mertins D, Kiess M, Henklein P, Trowitzsch-Kienast W, Schubert U. </i> Biochemistry, 1998","reference_id":"9622505","region_id":"DP00123r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In the absence of TFE, the initial shallow negative CD curve with a minimum at ca. 200 nm and a very small negative ellipticity value at 220 nm was characteristic of a disordered peptide conformation with very little evidence of stable secondary structure (Figure 1).","_id":"685af523b4ac24d5329d78e6"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":0,"_id":"685af523b4ac24d5329d78e5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":403,"end":415,"interaction_partner":[],"reference_html":"Solution structure of the cytoplasmic domain of the human CD4 glycoprotein by CD and 1H NMR spectroscopy: implications for biological functions. <i> Wray V, Mertins D, Kiess M, Henklein P, Trowitzsch-Kienast W, Schubert U. </i> Biochemistry, 1998","reference_id":"9622505","region_id":"DP00123r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Our CD analysis indicates that CD4CYTO adopts a stable secondary structure only when a membrane-like environment was present.","_id":"685af523b4ac24d5329d78f3"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_go_domain":"F","term_id":"GO:0008289","term_is_binding":true,"term_is_obsolete":false,"term_name":"lipid binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":1,"_id":"685af523b4ac24d5329d78f2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2KLU","_id":"685af523b4ac24d5329d78fe"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-11-24T10:43:35.872Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":372,"end":395,"interaction_partner":[],"reference_html":"NMR structure of the transmembrane and cytoplasmic domains of human CD4 in micelles. <i> Wittlich M, Thiagarajan P, Koenig BW, Hartmann R, Willbold D. </i> Biochim Biophys Acta, 2010","reference_id":"19781520","region_id":"DP00123r014","released":"2023_12","sample":[{"db":"ChEBI","deviation":null,"entry_name":"dodecylphosphocholine","id":"78018","statements":[{"type":"Methods","text":"The NMR sample contained 1 mM of CD4mut in 90% H2O/10 % 2H2O micellar solution (200 mM DPC-d38, 20 mM sodium phosphate, 150 mM NaCl, 0.02% (w/v) NaN3, pH 6.2).","_id":"685af523b4ac24d5329d7900"}],"term_id":"IDPO:00488","term_name":"interacting lipid","unit_id":"UO:0000063","unit_name":"mM","value":200,"_id":"685af523b4ac24d5329d78ff"}],"statement":[{"type":"Results","text":"Nearly complete resonance assignment of DPC micelle-inserted CD4mut has been reported earlier [32]. Secondary chemical shift analysis predicted a transmembrane α-helix from 372 to 395 and a short α-helix from residue 407 to 412.","_id":"685af523b4ac24d5329d7901"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":1,"_id":"685af523b4ac24d5329d78fd","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2KLU","_id":"685af523b4ac24d5329d7903"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-11-24T10:44:57.161Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":372,"end":395,"interaction_partner":[],"reference_html":"NMR structure of the transmembrane and cytoplasmic domains of human CD4 in micelles. <i> Wittlich M, Thiagarajan P, Koenig BW, Hartmann R, Willbold D. </i> Biochim Biophys Acta, 2010","reference_id":"19781520","region_id":"DP00123r015","released":"2023_12","sample":[{"db":"ChEBI","deviation":null,"entry_name":"dodecylphosphocholine","id":"78018","statements":[{"type":"Methods","text":"The NMR sample contained 1 mM of CD4mut in 90% H2O/10 % 2H2O micellar solution (200 mM DPC-d38, 20 mM sodium phosphate, 150 mM NaCl, 0.02% (w/v) NaN3, pH 6.2).","_id":"685af523b4ac24d5329d7905"}],"term_id":"IDPO:00488","term_name":"interacting lipid","unit_id":"UO:0000063","unit_name":"mM","value":200,"_id":"685af523b4ac24d5329d7904"}],"statement":[{"type":"Results","text":"Nearly complete resonance assignment of DPC micelle-inserted CD4mut has been reported earlier [32]. Secondary chemical shift analysis predicted a transmembrane α-helix from 372 to 395 and a short α-helix from residue 407 to 412.","_id":"685af523b4ac24d5329d7906"}],"states_connection":[{"source":"DP00123r008","target":"DP00123r014","_id":"685af523b4ac24d5329d7907"}],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":1,"_id":"685af523b4ac24d5329d7902","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2KLU","_id":"685af523b4ac24d5329d7909"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":372,"end":395,"interaction_partner":[{"db":"ChEBI","id":"78018","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d790b"}],"reference_html":"NMR structure of the transmembrane and cytoplasmic domains of human CD4 in micelles. <i> Wittlich M, Thiagarajan P, Koenig BW, Hartmann R, Willbold D. </i> Biochim Biophys Acta, 2010","reference_id":"19781520","region_id":"DP00123r016","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Nearly complete resonance assignment of DPC micelle-inserted CD4mut has been reported earlier [32]. Secondary chemical shift analysis predicted a transmembrane α-helix from 372 to 395 and a short α-helix from residue 407 to 412.","_id":"685af523b4ac24d5329d790a"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_go_domain":"F","term_id":"GO:0008289","term_is_binding":true,"term_is_obsolete":false,"term_name":"lipid binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":1,"_id":"685af523b4ac24d5329d7908","reference_source":"pmid"}],"__v":0,"disorder_content":0.13537117903930132,"disprot_consensus":{"full":[{"start":372,"end":395,"type":"T"},{"start":396,"end":433,"type":"D"}],"Structural state":[{"start":372,"end":395,"type":"S"},{"start":396,"end":433,"type":"D"}],"Molecular function":[{"start":372,"end":395,"type":"F"},{"start":403,"end":415,"type":"F"}],"Structural transition":[{"start":372,"end":395,"type":"T"}]}},{"features":{"gene3D":[{"start":431,"end":500,"id":"1.20.5.110","name":"1.20.5.110"},{"start":587,"end":650,"id":"1.20.5.110","name":"1.20.5.110"}],"pfam":[]},"uniref50":"UniRef50_P40357","sequence":"MGLKKFFKIKPPEEATPEQNKDTLMELGISVKNPSKKRKEKFAAYGKFANDKAEDKVYAPPGYEQYARPQDELEDLNASPLDANANEATAGSNRGSSGTQDLGNGAESNSMQDPYAIENDDYRYDDDPYARFQANKSNGRGSVNAAPYGDYGGGYNGTSLNSYNNDGPYSNQNTSNSWVNANGRNSLNHSNSTLNVGPSRQTRQPPVSTSTNSLSLDQRSPLANPMQEKRNPYADMNSYGGAYDSNTNRSSGTRQGSSKNANPYASMANDSYSNGNLNRSANPYSSRSVRQPQSQQAPMTYTPSFIASDEAARNSEVDLNEEPRTGEFDFEEVYADKSAENRAALDEPDLNAVMTNEDSIDLNASEVDHSSRQQQQQQWFMDEQQQQQQHFNATNNQYGDQRGYKTFEEIQKEEEARQQQEEDEAVDEIKQEIKFTKQSSVASTRNTLKMAQDAERAGMNTLGMLGHQSEQLNNVEGNLDLMKVQNKVADEKVAELKKLNRSILAVHVSNPFNSKRRRREREEQLKNRKIEEKLMREQTSQQLSQSTQRIEGAMNANNNISEVRERYQRKNVLEKAKRYQFENDEEDDEMELEIDRNLDQIQQVSNRLKKMALTTGKELDSQQKRLNNIEESTDDLDINLHMNTNRLAGIR","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P40357","disprot_id":"DP00128","ncbi_taxon_id":559292,"regions_counter":2,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":651,"region_id":"DP00128r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Formation of a yeast SNARE complex is accompanied by significant structural changes. <i> Rice LM, Brennwald P, Brünger AT. </i> FEBS Lett, 1997","term_id":"IDPO:0000002","curator_id":"esalladini","start":401,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"9326367","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"The spectra for Sec9c and Snc1 are very similar to each other and are suggestive of largely random coil conformation.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":401,"end":651,"reference_id":"9326367","reference_source":"pmid","reference_html":"Formation of a yeast SNARE complex is accompanied by significant structural changes. <i> Rice LM, Brennwald P, Brünger AT. </i> FEBS Lett, 1997","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006305","ec_ontology":"ECO","ec_name":"native protein gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"P32867","partner_start":null,"partner_end":null}],"region_id":"DP00128r002","statement":[{"text":"Sso1, the purified binary complex of Sso1 and Sec9c, and the purified ternary complex of Sso1, Sec9c, and Snc1 all migrate as well-defined bands on the native gel.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P40357","date":"2016-09-13T15:10:35.000Z","acc":"P40357","name":"Protein transport protein SEC9","length":651,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000013575B","genes":[{"name":{"value":"SEC9"},"synonyms":[{"value":"HSS7"}],"olnNames":[{"value":"YGR009C"}]}],"alphafold_very_low_content":0.445468509984639,"disorder_content":0.38556067588325654,"disprot_consensus":{"full":[{"start":401,"end":651,"type":"D"}],"Structural state":[{"start":401,"end":651,"type":"D"}],"Molecular function":[{"start":401,"end":651,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00554","name":"Rel homology DNA-binding domain","start":21,"end":186},{"id":"PF16179","name":"Rel homology dimerisation domain","start":195,"end":291}],"gene3D":[{"start":9,"end":187,"id":"2.60.40.340","name":"Rel homology domain (RHD), DNA-binding domain"},{"start":191,"end":304,"id":"2.60.40.10","name":"Immunoglobulins"}]},"uniref50":"UniRef50_Q04206-4","sequence":"MDDLFPLIFPSEPAQASGPYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGYYEADLCPDRSIHSFQNLGIQCVKKRDLEQAISQRIQTNNNPFHVPIEEQRGDYDLNAVRLCFQVTVRDPAGRPLLLTPVLSHPIFDNRAPNTAELKICRVNRNSGSCLGGDEIFLLCDKVQKEDIEVYFTGPGWEARGSFSQADVHRQVAIVFRTPPYADPSLQAPVRVSMQLRRPSDRELSEPMEFQYLPDTDDRHRIEEKRKRTYETFKSIMKKSPFNGPTEPRPPTRRIAVPTRNSTSVPKPAPQPYTFPASLSTINFDEFSPMLLPSGQISNQALALAPSSAPVLAQTMVPSSAMVPLAQPPAPAPVLTPGPPQSLSAPVPKSTQAGEGTLSEALLHLQFDADEDLGALLGNSTDPGVFTDLASVDNSEFQQLLNQGVSMSHSTAEPMLMEYPEAITRLVTGSQRPPDPAPTPLGTSGLPNGLSGDEDFSSIADMDFSALLSQISS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q04207","disprot_id":"DP00129","ncbi_taxon_id":10090,"regions_counter":2,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":304,"region_id":"DP00129r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The role of DNA in the mechanism of NFkappaB dimer formation: crystal structures of the dimerization domains of the p50 and p65 subunits. <i> Huang DB, Huxford T, Chen YQ, Ghosh G. </i> Structure, 1997","term_id":"IDPO:0000002","curator_id":"esalladini","start":295,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"9384558","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"The final ten amino acids of p65dd are disordered in the structure.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":304,"term_name":"entropic chain","start":295,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"9384558","version":4,"reference_html":"The role of DNA in the mechanism of NFkappaB dimer formation: crystal structures of the dimerization domains of the p50 and p65 subunits. <i> Huang DB, Huxford T, Chen YQ, Ghosh G. </i> Structure, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0006220","region_id":"DP00129r002","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"The final ten amino acids of p65dd are disordered in the structure.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_Q04207","date":"2016-09-09T14:16:37.000Z","acc":"Q04207","name":"Transcription factor p65","length":549,"organism":"Mus musculus","dataset":[],"UniParc":"UPI000000088B","genes":[{"name":{"value":"Rela"},"synonyms":[{"value":"Nfkb3"}]}],"alphafold_very_low_content":0.33879781420765026,"disorder_content":0.018214936247723135,"disprot_consensus":{"full":[{"start":295,"end":304,"type":"D"}],"Structural state":[{"start":295,"end":304,"type":"D"}],"Disorder function":[{"start":295,"end":304,"type":"F"}]}},{"acc":"P22531","sequence":"MSYQQQQCKQPCQPPPVCPTPKCPEPCPPPKCPEPCPPPKCPQPCPPQQCQQKCPPVTPSPPCQPKCPPKSK","alphafold_very_low_content":"0","creator":"gminervini","dataset":[],"date":"2016-08-23T16:41:24.000Z","disprot_id":"DP00130","features":{"pfam":[{"id":"PF14820","name":"Small proline-rich 2","start":2,"end":69}]},"genes":[{"name":{"value":"SPRR2E","evidences":[],"_id":"685af523b4ac24d5329d792f"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d792e"}],"length":72,"name":"Small proline-rich protein 2E","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":13,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000135D76","uniref100":"UniRef100_P22531","uniref50":"UniRef50_P22531","uniref90":"UniRef90_P22531","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-24T13:35:49.873Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":20,"interaction_partner":[],"reference_html":"Structural and transglutaminase substrate properties of the small proline-rich 2 family of cornified cell envelope proteins. <i> Tarcsa E, Candi E, Kartasova T, Idler WW, Marekov LN, Steinert PM. </i> J Biol Chem, 1998","reference_id":"9722562","region_id":"DP00130r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Together, these data suggest that only the central peptide repeat domain of SPR2 proteins possesses an organized structure.","_id":"685af523b4ac24d5329d7920"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-01-18T16:53:04.714Z","_id":"685af523b4ac24d5329d7921"},"version":0,"_id":"685af523b4ac24d5329d791f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-24T13:36:06.388Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":20,"interaction_partner":[],"reference_html":"Structural and transglutaminase substrate properties of the small proline-rich 2 family of cornified cell envelope proteins. <i> Tarcsa E, Candi E, Kartasova T, Idler WW, Marekov LN, Steinert PM. </i> J Biol Chem, 1998","reference_id":"9722562","region_id":"DP00130r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Together, these data suggest that only the central peptide repeat domain of SPR2 proteins possesses an organized structure.","_id":"685af523b4ac24d5329d7923"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-01-18T16:55:05.108Z","_id":"685af523b4ac24d5329d7924"},"version":0,"_id":"685af523b4ac24d5329d7922","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-24T13:36:59.014Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":48,"end":72,"interaction_partner":[],"reference_html":"Structural and transglutaminase substrate properties of the small proline-rich 2 family of cornified cell envelope proteins. <i> Tarcsa E, Candi E, Kartasova T, Idler WW, Marekov LN, Steinert PM. </i> J Biol Chem, 1998","reference_id":"9722562","region_id":"DP00130r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Together, these data suggest that only the central peptide repeat domain of SPR2 proteins possesses an organized structure.","_id":"685af523b4ac24d5329d7929"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-01-18T16:53:03.353Z","_id":"685af523b4ac24d5329d792a"},"version":0,"_id":"685af523b4ac24d5329d7928","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-24T13:37:08.310Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":48,"end":72,"interaction_partner":[],"reference_html":"Structural and transglutaminase substrate properties of the small proline-rich 2 family of cornified cell envelope proteins. <i> Tarcsa E, Candi E, Kartasova T, Idler WW, Marekov LN, Steinert PM. </i> J Biol Chem, 1998","reference_id":"9722562","region_id":"DP00130r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Together, these data suggest that only the central peptide repeat domain of SPR2 proteins possesses an organized structure.","_id":"685af523b4ac24d5329d792c"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-01-18T16:55:05.964Z","_id":"685af523b4ac24d5329d792d"},"version":0,"_id":"685af523b4ac24d5329d792b","reference_source":"pmid"}],"__v":0,"disorder_content":0.6111111111111112,"disprot_consensus":{"full":[{"start":2,"end":20,"type":"D"},{"start":48,"end":72,"type":"D"}],"Structural state":[{"start":2,"end":20,"type":"D"},{"start":48,"end":72,"type":"D"}],"Disorder function":[{"start":2,"end":20,"type":"F"},{"start":48,"end":72,"type":"F"}]}},{"acc":"P07221","sequence":"MNAADRMGARVALLLLLVLGSPQSGVHGEEGLDFPEYDGVDRVINVNAKNYKNVFKKYEVLALLYHEPPEDDKASQRQFEMEELILELAAQVLEDKGVGFGLVDSEKDAAVAKKLGLTEEDSIYVFKEDEVIEYDGEFSADTLVEFLLDVLEDPVELIEGERELQAFENIEDEIKLIGYFKNKDSEHYKAFKEAAEEFHPYIPFFATFDSKVAKKLTLKLNEIDFYEAFMEEPVTIPDKPNSEEEIVNFVEEHRRSTLRKLKPESMYETWEDDMDGIHIVAFAEEADPDGYEFLEILKSVAQDNTDNPDLSIIWIDPDDFPLLVPYWEKTFDIDLSAPQIGVVNVTDADSVWMEMDDEEDLPSAEELEDWLEDVLEGEINTEDDDDEDDDDDDDD","alphafold_very_low_content":"0.08354430379746836","creator":"dpiovesan","dataset":[],"date":"2016-08-23T11:58:49.000Z","disprot_id":"DP00132","features":{"pfam":[{"id":"PF01216","name":"Calsequestrin","start":7,"end":390}],"gene3D":[{"start":257,"end":395,"id":"3.40.30.10","name":"Glutaredoxin","_id":"685af523b4ac24d5329d7931"},{"start":155,"end":256,"id":"3.40.30.10","name":"Glutaredoxin","_id":"685af523b4ac24d5329d7932"},{"start":43,"end":154,"id":"3.40.30.10","name":"Glutaredoxin","_id":"685af523b4ac24d5329d7933"}]},"genes":[{"name":{"value":"CASQ1","evidences":[],"_id":"685af523b4ac24d5329d7965"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d7964"}],"length":395,"name":"Calsequestrin-1","ncbi_taxon_id":9986,"organism":"Oryctolagus cuniculus","regions_counter":13,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Lagomorpha","Leporidae","Oryctolagus"],"UniParc":"UPI0000126F12","uniref100":"UniRef100_P07221","uniref50":"UniRef50_P07221","uniref90":"UniRef90_P07221","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1A8Y","_id":"685af523b4ac24d5329d7938"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":376,"end":395,"interaction_partner":[],"reference_html":"Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum. <i> Wang S, Trumble WR, Liao H, Wesson CR, Dunker AK, Kang CH. </i> Nat Struct Biol, 1998","reference_id":"9628486","region_id":"DP00132r002","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The C-terminal region is missing from the crystal structure.","_id":"685af523b4ac24d5329d7939"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-06T11:21:36.588Z","_id":"685af523b4ac24d5329d793a"},"version":3,"_id":"685af523b4ac24d5329d7937","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":395,"interaction_partner":[],"reference_html":"Characterization of skeletal muscle calsequestrin by 1H NMR spectroscopy. <i> Aaron BM, Oikawa K, Reithmeier RA, Sykes BD. </i> J Biol Chem, 1984","reference_id":"6480588","region_id":"DP00132r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Fig. 1 shows the 270-MHz 1H NMR spectrum of calsequestrin in the calcium-free form. The spectrum is characteristic of a protein known to be largely in the random coil conformation in the apo form (5, 7, 8, 10), in the sense that there is no dispersion of chemical shifts of the resonances of any of the amino acids from their random coil positions in the spectrum and the resonances are relatively narrow for a protein of this size (Mr = 44,000).","_id":"685af523b4ac24d5329d7942"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-06T11:21:35.188Z","_id":"685af523b4ac24d5329d7943"},"version":3,"_id":"685af523b4ac24d5329d7941","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-12-06T11:21:06.849Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":395,"interaction_partner":[],"reference_html":"Characterization of skeletal muscle calsequestrin by 1H NMR spectroscopy. <i> Aaron BM, Oikawa K, Reithmeier RA, Sykes BD. </i> J Biol Chem, 1984","reference_id":"6480588","region_id":"DP00132r007","released":"2022_12","sample":[],"statement":[{"type":"Results","text":"The addition of KCl to calsequestrin (Fig. 3) resulted in the broadening and concomitant loss of intensity of resonances throughout both the aromatic and\naliphatic regions of the spectrum. This broadening was dependent on the concentration of KCl and there was no evidence of any selective changes in the NMR spectrum (Fig. 3, A and B). This is consistent with K+ binding to several sites on the extended structure of calsequestrin (7).","_id":"685af523b4ac24d5329d7945"},{"type":"Results","text":"The addition of CaCl2 to calsequestrin (Fig. 4) had the same general effect as KCI; that is, a broadening of the resonances and loss of intensities throughout the NMR spectrum.","_id":"685af523b4ac24d5329d7946"},{"type":"Results","text":"Unlike the KCl titration curve (Figs. 3 and 6), which showed binding to a single class of independent sites, the calcium titration curve showed a flatter region at the initial stages of the titration (Fig. 4C, curves a and b). This type of curve indicates the presence of some positive cooperativity for the binding of calcium to calsequestrin (10).","_id":"685af523b4ac24d5329d7947"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a calcium ion (Ca2+).\" [GOC:ai]","term_id":"GO:0005509","term_is_binding":false,"term_is_obsolete":false,"term_name":"calcium ion binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-20T20:42:38.645Z","_id":"685af523b4ac24d5329d7948"},"version":5,"_id":"685af523b4ac24d5329d7944","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":395,"interaction_partner":[],"reference_html":"Characterization of skeletal muscle calsequestrin by 1H NMR spectroscopy. <i> Aaron BM, Oikawa K, Reithmeier RA, Sykes BD. </i> J Biol Chem, 1984","reference_id":"6480588","region_id":"DP00132r008","released":"2022_03","sample":[{"db":"ChEBI","deviation":null,"entry_name":"potassium chloride","id":"32588","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d794a"},{"db":"ChEBI","deviation":null,"entry_name":"calcium dichloride","id":"3312","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d794b"}],"statement":[{"type":"Results","text":"The addition of KCl to calsequestrin (Fig. 3) resulted in the broadening and concomitant loss of intensity of resonances throughout both the aromatic and\naliphatic regions of the spectrum. This broadening was dependent on the concentration of KCl and there was no evidence of any selective changes in the NMR spectrum (Fig. 3, A and B). This is consistent with K+ binding to several sites on the extended structure of calsequestrin (7).","_id":"685af523b4ac24d5329d794c"},{"type":"Results","text":"The addition of CaCl2 to calsequestrin (Fig. 4) had the same general effect as KCI; that is, a broadening of the resonances and loss of intensities throughout the NMR spectrum.","_id":"685af523b4ac24d5329d794d"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-06T11:21:33.349Z","_id":"685af523b4ac24d5329d794e"},"version":3,"_id":"685af523b4ac24d5329d7949","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-02-01T14:29:51.738Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":395,"interaction_partner":[{"db":"ChEBI","id":"29103","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7950"}],"reference_html":"Characterization of skeletal muscle calsequestrin by 1H NMR spectroscopy. <i> Aaron BM, Oikawa K, Reithmeier RA, Sykes BD. </i> J Biol Chem, 1984","reference_id":"6480588","region_id":"DP00132r009","released":"2024_06","sample":[{"db":"ChEBI","deviation":null,"entry_name":"potassium chloride","id":"32588","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7954"}],"statement":[{"type":"Results","text":"The addition of KCl to calsequestrin (Fig. 3) resulted in the broadening and concomitant loss of intensity of resonances throughout both the aromatic and\naliphatic regions of the spectrum. This broadening was dependent on the concentration of KCl and there was no evidence of any selective changes in the NMR spectrum (Fig. 3, A and B). This is consistent with K+ binding to several sites on the extended structure of calsequestrin (7).","_id":"685af523b4ac24d5329d7951"},{"type":"Results","text":"The addition of CaCl2 to calsequestrin (Fig. 4) had the same general effect as KCI; that is, a broadening of the resonances and loss of intensities throughout the NMR spectrum.","_id":"685af523b4ac24d5329d7952"},{"type":"Results","text":"Unlike the KCl titration curve (Figs. 3 and 6), which showed binding to a single class of independent sites, the calcium titration curve showed a flatter region at the initial stages of the titration (Fig. 4C, curves a and b). This type of curve indicates the presence of some positive cooperativity for the binding of calcium to calsequestrin (10).","_id":"685af523b4ac24d5329d7953"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a potassium ion (K+).\" [GOC:mah]","term_id":"GO:0030955","term_is_binding":true,"term_is_obsolete":false,"term_name":"potassium ion binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2024-02-01T17:05:05.474Z","_id":"685af523b4ac24d5329d7955"},"version":5,"_id":"685af523b4ac24d5329d794f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-25T08:40:57.085Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":395,"interaction_partner":[],"reference_html":"Characterization of skeletal muscle calsequestrin by 1H NMR spectroscopy. <i> Aaron BM, Oikawa K, Reithmeier RA, Sykes BD. </i> J Biol Chem, 1984","reference_id":"6480588","region_id":"DP00132r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The CD spectrum obtained for calsequestrin in this study (Fig. 5A) is similar to the published CD spectra of this protein (8, 10) which indicate that the calcium-free protein is predominantly in the random coil form.","_id":"685af523b4ac24d5329d7957"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-06T11:21:33.904Z","_id":"685af523b4ac24d5329d7958"},"version":0,"_id":"685af523b4ac24d5329d7956","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-25T08:41:04.290Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":395,"interaction_partner":[],"reference_html":"Characterization of skeletal muscle calsequestrin by 1H NMR spectroscopy. <i> Aaron BM, Oikawa K, Reithmeier RA, Sykes BD. </i> J Biol Chem, 1984","reference_id":"6480588","region_id":"DP00132r011","released":"2022_03","sample":[{"db":"ChEBI","deviation":null,"entry_name":"calcium dichloride","id":"3312","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d795a"}],"statement":[{"type":"Results","text":"The addition of calcium to the protein results in an increase in the a-helix content (8-10) to 35% in the calcium-saturated form (Fig. 5, A and B). The shape of the calcium titration curve obtained from the CD experiments (Fig. 5B) is very similar to that obtained from the NMR studies (Fig. 4C, curves a and b), with a region at the low calcium concentrations which is indicative of positive cooperativity.","_id":"685af523b4ac24d5329d795b"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-06T11:21:31.894Z","_id":"685af523b4ac24d5329d795c"},"version":0,"_id":"685af523b4ac24d5329d7959","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":395,"interaction_partner":[{"db":"ChEBI","id":"29108","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d795e"}],"reference_html":"Characterization of skeletal muscle calsequestrin by 1H NMR spectroscopy. <i> Aaron BM, Oikawa K, Reithmeier RA, Sykes BD. </i> J Biol Chem, 1984","reference_id":"6480588","region_id":"DP00132r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The addition of calcium to the protein results in an increase in the a-helix content (8-10) to 35% in the calcium-saturated form (Fig. 5, A and B). The shape of the calcium titration curve obtained from the CD experiments (Fig. 5B) is very similar to that obtained from the NMR studies (Fig. 4C, curves a and b), with a region at the low calcium concentrations which is indicative of positive cooperativity. ","_id":"685af523b4ac24d5329d795f"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","term_go_domain":"F","term_id":"GO:0046872","term_is_binding":true,"term_is_obsolete":false,"term_name":"metal ion binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-06T11:21:28.560Z","_id":"685af523b4ac24d5329d7960"},"version":1,"_id":"685af523b4ac24d5329d795d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-12-06T11:21:26.158Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":395,"interaction_partner":[],"reference_html":"Characterization of skeletal muscle calsequestrin by 1H NMR spectroscopy. <i> Aaron BM, Oikawa K, Reithmeier RA, Sykes BD. </i> J Biol Chem, 1984","reference_id":"6480588","region_id":"DP00132r013","released":"2022_12","sample":[],"statement":[{"type":"Results","text":"The addition of calcium to the protein results in an increase in the a-helix content (8-10) to 35% in the calcium-saturated form (Fig. 5, A and B). The shape of the calcium titration curve obtained from the CD experiments (Fig. 5B) is very similar to that obtained from the NMR studies (Fig. 4C, curves a and b), with a region at the low calcium concentrations which is indicative of positive cooperativity. ","_id":"685af523b4ac24d5329d7962"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a calcium ion (Ca2+).\" [GOC:ai]","term_go_domain":"P","term_id":"GO:0005509","term_is_binding":false,"term_is_obsolete":false,"term_name":"calcium ion binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-20T20:42:40.492Z","_id":"685af523b4ac24d5329d7963"},"version":2,"_id":"685af523b4ac24d5329d7961","reference_source":"pmid"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":395,"type":"T"}],"Structural state":[{"start":1,"end":395,"type":"D"}],"Molecular function":[{"start":1,"end":395,"type":"F"}],"Structural transition":[{"start":1,"end":395,"type":"T"}]}},{"acc":"P03422","sequence":"MAEEQARHVKNGLECIRALKAEPIGSLAIEEAMAAWSEISDNPGQERATCREEKAGSSGLSKPCLSAIGSTEGGAPRIRGQGPGESDDDAETLGIPPRNLQASSTGLQCYYVYDHSGEAVKGIQDADSIMVQSGLDGDSTLSGGDNESENSDVDIGEPDTEGYAITDRGSAPISMGFRASDVETAEGGEIHELLRLQSRGNNFPKLGKTLNVPPPPDPGRASTSGTPIKKGTERRLASFGTEIASLLTGGATQCARKSPSEPSGPGAPAGNVPECVSNAALIQEWTPESGTTISPRSQNNEEGGDYYDDELFSDVQDIKTALAKIHEDNQKIISKLESLLLLKGEVESIKKQINRQNISISTLEGHLSSIMIAIPGLGKDPNDPTADVEINPDLKPIIGRDSGRALAEVLKKPVASRQLQGMTNGRTSSRGQLLKEFQLKPIGKKMSSAVGFVPDTGPASRSVIRSIIKSSRLEEDRKRYLMTLLDDIKGANDLAKFHQMLMKIIMK","creator":"slonghi","dataset":["Viral proteins","Condensates-related proteins"],"date":"2016-09-02T15:07:23.000Z","disprot_id":"DP00133","features":{"pfam":[{"id":"PF03210","name":"Paramyxovirus P/V phosphoprotein C-terminal","start":330,"end":502},{"id":"PF13825","name":"Paramyxovirus structural protein V/P N-terminus","start":4,"end":312}],"gene3D":[{"start":457,"end":507,"id":"1.10.8.10","name":"DNA helicase RuvA subunit, C-terminal domain","_id":"685af523b4ac24d5329d7968"},{"start":304,"end":371,"id":"1.20.5.110","name":"1.20.5.110","_id":"685af523b4ac24d5329d7969"}]},"genes":[{"name":{"value":"P/V","evidences":[],"_id":"685af523b4ac24d5329d79d1"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d79d0"}],"length":507,"name":"Phosphoprotein","ncbi_taxon_id":11235,"organism":"Measles virus (strain Edmonston)","regions_counter":38,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Paramyxoviridae","Orthoparamyxovirinae","Morbillivirus"],"UniParc":"UPI0000134B60","uniref100":"UniRef100_P03422","uniref50":"UniRef50_P35974","uniref90":"UniRef90_P35974","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":230,"interaction_partner":[],"reference_html":"The N-terminal domain of the phosphoprotein of Morbilliviruses belongs to the natively unfolded class of proteins. <i> Karlin D, Longhi S, Receveur V, Canard B. </i> Virology, 2002","reference_id":"12069524","region_id":"DP00133r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The CD spectrum o fPNT at neutral pH lacks evidence of any significant ordered secondary structure, as seen from its large negative ellipticity at 198 nm and nil ellipticity at 185 nm (Fig. 4).\n","_id":"685af523b4ac24d5329d796b"},{"type":"Results","text":"On the other hand, the hypothesis of an unfolded protein is consistent with the CD  and  NMR  data,  which  show  that  PNT  lacks  stable secondary structure.","_id":"685af523b4ac24d5329d796c"},{"type":"Discussion","text":"Moreover,CD studies further confirm that PNT is unfolded in aqueous solution.","_id":"685af523b4ac24d5329d796d"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T14:06:02.455Z","_id":"685af523b4ac24d5329d796e"},"version":3,"_id":"685af523b4ac24d5329d796a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006198","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":230,"interaction_partner":[],"reference_html":"The N-terminal domain of the phosphoprotein of Morbilliviruses belongs to the natively unfolded class of proteins. <i> Karlin D, Longhi S, Receveur V, Canard B. </i> Virology, 2002","reference_id":"12069524","region_id":"DP00133r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The very small spread of the resonance  frequencies for amide protons (between 7.8 and 8.7 ppm,see box in Fig. 3) together with the absence of NOEs in the  amide–amide  region  is  typical  of a  protein  without any  constant  secondary  structure.","_id":"685af523b4ac24d5329d7976"},{"type":"Discussion","text":"NMR  data show that PNT exhibits no short-range interactions, indicating the lack of any constant secondary structure as well as the absence of any stable oligomers.","_id":"685af523b4ac24d5329d7977"},{"type":"Results","text":"On the other hand, the hypothesis of an unfolded protein is consistent with the CD  and  NMR  data,  which  show  that  PNT  lacks  stable secondary structure.","_id":"685af523b4ac24d5329d7978"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T14:05:55.159Z","_id":"685af523b4ac24d5329d7979"},"version":3,"_id":"685af523b4ac24d5329d7975","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":230,"interaction_partner":[],"reference_html":"The N-terminal domain of the phosphoprotein of Morbilliviruses belongs to the natively unfolded class of proteins. <i> Karlin D, Longhi S, Receveur V, Canard B. </i> Virology, 2002","reference_id":"12069524","region_id":"DP00133r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As shown in Fig. 2, PNT displays an abnormally  slow  migration  in  SDS–PAGE  with  an  apparentmolecular  weight  (MW)  o  f33  kDa  (expected  weight  25kDa). This abnormal behavior has been reported previously for all P proteins of Morbilliviruses and Paramyxoviruses (Lamb and Kolakofsky, 2001) and attributed to the occurrence of acidic stretches in PNT, which is consistent with our result.","_id":"685af523b4ac24d5329d7981"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T14:05:53.469Z","_id":"685af523b4ac24d5329d7982"},"version":3,"_id":"685af523b4ac24d5329d7980","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":230,"interaction_partner":[],"reference_html":"The N-terminal domain of the phosphoprotein of Morbilliviruses belongs to the natively unfolded class of proteins. <i> Karlin D, Longhi S, Receveur V, Canard B. </i> Virology, 2002","reference_id":"12069524","region_id":"DP00133r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":" In the absence of TFE, PNT is entirely digested in 6 h, wherea sit shows resistance to digestion in the presence of 15% TFE (compare lanes C and 4).","_id":"685af523b4ac24d5329d798a"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T10:21:22.027Z","_id":"685af523b4ac24d5329d798b"},"version":3,"_id":"685af523b4ac24d5329d7989","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":50,"interaction_partner":[],"reference_html":"Self-Assembly of Measles Virus Nucleocapsid-like Particles: Kinetics and RNA Sequence Dependence. <i> Milles S, Jensen MR, Communie G, Maurin D, Schoehn G, Ruigrok RW, Blackledge M. </i> Angew Chem Int Ed Engl, 2016","reference_id":"27270664","region_id":"DP00133r024","released":"2022_03","sample":[],"statement":[{"type":"Article","text":" The minimal peptide required to form the complex was identified using NMR spectroscopy as P1‐50 (Figure S2), resulting in a high‐yielding, soluble, and stable N0P complex. ","_id":"685af523b4ac24d5329d79a2"},{"type":"Figure","text":"P50 is bound to N so that peaks are too weak to be observed","_id":"685af523b4ac24d5329d79a3"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T10:23:06.702Z","_id":"685af523b4ac24d5329d79a4"},"version":4,"_id":"685af523b4ac24d5329d79a1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":300,"interaction_partner":[],"reference_html":"Structure of the tetramerization domain of measles virus phosphoprotein. <i> Communie G, Crépin T, Maurin D, Jensen MR, Blackledge M, Ruigrok RW. </i> J Virol, 2013","reference_id":"23576502","region_id":"DP00133r025","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"The coiled coil is too large to be observed by standard solution NMR analysis because of the effective rotational correlation time, and only the flexible residues give rise to sharp signals. By this method, all amino acids up to residue 300 could be identified, proving the absence of the additional helices that were observed in the Sendai virus domain.","_id":"685af523b4ac24d5329d79a6"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T10:21:13.377Z","_id":"685af523b4ac24d5329d79a7"},"version":3,"_id":"685af523b4ac24d5329d79a5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0001591","ec_name":"atomic force microscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":229,"interaction_partner":[],"reference_html":"Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy. <i> Kodera N, Noshiro D, Dora SK, Mori T, Habchi J, Blocquel D, Gruet A, Dosnon M, Salladini E, Bignon C, Fujioka Y, Oda T, Noda NN, Sato M, Lotti M, Mizuguchi M, Longhi S, Ando T. </i> Nat Nanotechnol, 2021","reference_id":"33230318","region_id":"DP00133r030","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"PNT-GFP exhibited a thin and flexible tail-like structure with a temporarily appearing and disappearing small globule at the N-terminal end, together with the C-terminal GFP (Fig. 4e and Supplementary Video 7).","_id":"685af523b4ac24d5329d79b3"},{"type":"Results","text":"The R2D histogram of the IDR was best fitted to a double Gaussian with peaks at 8.9 ± 0.33 and 14.3 ± 9.26 nm (Fig. 4i). The mean height of the IDR was 0.4–0.5 nm, in both metastable shorter and longer states (Extended Data Fig. 5b), indicating that the IDR is fully disordered even on disorder-to-order transition of the small globule.","_id":"685af523b4ac24d5329d79b4"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T09:51:29.252Z","_id":"685af523b4ac24d5329d79b5"},"version":3,"_id":"685af523b4ac24d5329d79b2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":50,"interaction_partner":[],"reference_html":"Self-Assembly of Measles Virus Nucleocapsid-like Particles: Kinetics and RNA Sequence Dependence. <i> Milles S, Jensen MR, Communie G, Maurin D, Schoehn G, Ruigrok RW, Blackledge M. </i> Angew Chem Int Ed Engl, 2016","reference_id":"27270664","region_id":"DP00133r031","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"The minimal peptide required to form the complex was identified using NMR spectroscopy as P1‐50 (Figure S2), resulting in a high‐yielding, soluble, and stable N0P complex.","_id":"685af523b4ac24d5329d79b7"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","term_id":"GO:0044183","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein folding chaperone","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T10:23:23.478Z","_id":"685af523b4ac24d5329d79b8"},"version":1,"_id":"685af523b4ac24d5329d79b6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007064","ec_name":"dynamic light scattering assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":230,"interaction_partner":[],"reference_html":"The N-terminal domain of the phosphoprotein of Morbilliviruses belongs to the natively unfolded class of proteins. <i> Karlin D, Longhi S, Receveur V, Canard B. </i> Virology, 2002","reference_id":"12069524","region_id":"DP00133r032","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Thus, the Rso fPNT measured by DLS corresponds to the value expected for a fully unfolded protein.","_id":"685af523b4ac24d5329d79ba"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T09:45:49.010Z","_id":"685af523b4ac24d5329d79bb"},"version":1,"_id":"685af523b4ac24d5329d79b9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0001184","ec_name":"gel-filtration evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":230,"interaction_partner":[],"reference_html":"The N-terminal domain of the phosphoprotein of Morbilliviruses belongs to the natively unfolded class of proteins. <i> Karlin D, Longhi S, Receveur V, Canard B. </i> Virology, 2002","reference_id":"12069524","region_id":"DP00133r033","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Therefore, the Stokes radius measured for PNT (41 Å) is not compatible with a monomeric, globular protein. Such a large value for the Stokes radius could be attributed either to a high degree of multimerization  or  to  a  monomeric,  unfolded  protein (RsU predicted: 46 Å). Multimers in the form of nonspecific aggregates would have led to a broad peak in gel filtration, which is not the case here. ","_id":"685af523b4ac24d5329d79bd"},{"type":"Discussion","text":"The  hydrodynamic  properties  of  PNT  inferred  from both  gel  filtration  and  dynamic  light-scattering  experiments  are  consistent  with  PNT  being  either  a  stableoligomer  or  a  monomeric,  unfolded  protein. ","_id":"685af523b4ac24d5329d79be"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T14:05:44.792Z","_id":"685af523b4ac24d5329d79bf"},"version":1,"_id":"685af523b4ac24d5329d79bc","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":304,"interaction_partner":[],"reference_html":"An ultraweak interaction in the intrinsically disordered replication machinery is essential for measles virus function. <i> Milles S, Jensen MR, Lazert C, Guseva S, Ivashchenko S, Communie G, Maurin D, Gerlier D, Ruigrok RWH, Blackledge M. </i> Sci Adv, 2018","reference_id":"30140745","region_id":"DP00133r034","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"We used NMR spectroscopy to investigate the conformational behavior of MeV PNTD in its free state and to describe the structural, dynamic, and kinetic behavior of this highly disordered 90-kDa complex. Although unfolded, PNTD exhibits transient helical propensities in the N-terminal N binding site (α1/2), around residues 87 to 93 (α3) and 189 to 198 (α4), linked by long, highly dynamic segments (Fig. 1).","_id":"685af523b4ac24d5329d79c1"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T09:48:58.461Z","_id":"685af523b4ac24d5329d79c2"},"version":1,"_id":"685af523b4ac24d5329d79c0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":377,"end":457,"interaction_partner":[],"reference_html":"Measles virus nucleo- and phosphoproteins form liquid-like phase-separated compartments that promote nucleocapsid assembly. <i> Guseva S, Milles S, Jensen MR, Salvi N, Kleman JP, Maurin D, Ruigrok RWH, Blackledge M. </i> Sci Adv, 2020","reference_id":"32270045","region_id":"DP00133r035","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Carbon chemical shifts of P304–507 did not change significantly in comparison with PLOOP, demonstrating that PLOOP remains disordered in the context of the construct that links the tetramerization domain and XD and that is required for phase separation (see fig. S6).","_id":"685af523b4ac24d5329d79c4"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T09:48:57.481Z","_id":"685af523b4ac24d5329d79c5"},"version":1,"_id":"685af523b4ac24d5329d79c3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006323","ec_name":"fluorescence microscopy evidence used in manual assertion","ec_ontology":"ECO","start":377,"end":457,"interaction_partner":[],"reference_html":"Measles virus nucleo- and phosphoproteins form liquid-like phase-separated compartments that promote nucleocapsid assembly. <i> Guseva S, Milles S, Jensen MR, Salvi N, Kleman JP, Maurin D, Ruigrok RWH, Blackledge M. </i> Sci Adv, 2020","reference_id":"32270045","region_id":"DP00133r036","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Several mixtures formed condensed phases: P50N525 + P1–507, P304N525 + P304–507, and P50N525 + P304–507 (Fig. 1B). P50N525 + P304–507 was thus identified as the minimal phase-separating system, forming spherical bimolecular condensates as measured by fluorescence microscopy (Fig. 1B) and showing increased turbidity (Fig. 1D).","_id":"685af523b4ac24d5329d79c7"},{"type":"Results","text":"Both proteins therefore remain liquid in the condensed phase, although their rotational dynamics are slowed, possibly due to increased viscosity in the droplets. In summary, these results confirm that LLPS occurs under near-physiological protein and salt concentrations upon mixing of full-length N- and the C-terminal domains of P in vitro, complementing recent in vivo observations (32).","_id":"685af523b4ac24d5329d79c8"}],"states_connection":[],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_id":"GO:0140693","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T09:48:52.056Z","_id":"685af523b4ac24d5329d79c9"},"version":1,"_id":"685af523b4ac24d5329d79c6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":377,"end":457,"interaction_partner":[],"reference_html":"Measles virus nucleo- and phosphoproteins form liquid-like phase-separated compartments that promote nucleocapsid assembly. <i> Guseva S, Milles S, Jensen MR, Salvi N, Kleman JP, Maurin D, Ruigrok RWH, Blackledge M. </i> Sci Adv, 2020","reference_id":"32270045","region_id":"DP00133r037","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"An additional interaction between PLOOP and N was identified using NMR spectroscopy (Fig. 4, A and B), suggesting that the role of this domain, which is present in all constructs involved in phase separation, involves a direct interaction with N rather than acting as a simple spacer (35).","_id":"685af523b4ac24d5329d79cb"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T09:48:44.266Z","_id":"685af523b4ac24d5329d79cc"},"version":1,"_id":"685af523b4ac24d5329d79ca","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":377,"end":457,"interaction_partner":[],"reference_html":"Measles virus nucleo- and phosphoproteins form liquid-like phase-separated compartments that promote nucleocapsid assembly. <i> Guseva S, Milles S, Jensen MR, Salvi N, Kleman JP, Maurin D, Ruigrok RWH, Blackledge M. </i> Sci Adv, 2020","reference_id":"32270045","region_id":"DP00133r038","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Carbon chemical shifts of P304–507 did not change significantly in comparison with PLOOP, demonstrating that PLOOP remains disordered in the context of the construct that links the tetramerization domain and XD and that is required for phase separation (see fig. S6).","_id":"685af523b4ac24d5329d79ce"}],"states_connection":[],"term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T09:48:49.680Z","_id":"685af523b4ac24d5329d79cf"},"version":1,"_id":"685af523b4ac24d5329d79cd","reference_source":"pmid"}],"__v":0,"disorder_content":0.7593688362919132,"disprot_consensus":{"full":[{"start":1,"end":304,"type":"D"},{"start":377,"end":457,"type":"D"}],"Structural state":[{"start":1,"end":304,"type":"D"},{"start":377,"end":457,"type":"D"}],"Molecular function":[{"start":1,"end":50,"type":"F"},{"start":377,"end":457,"type":"F"}],"Disorder function":[{"start":377,"end":457,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00013","name":"KH domain","start":221,"end":278},{"id":"PF00013","name":"KH domain","start":285,"end":331},{"id":"PF05641","name":"Agenet domain","start":63,"end":117},{"id":"PF12235","name":"Fragile X-related 1 protein core C terminal","start":420,"end":542},{"id":"PF16098","name":"Fragile X messenger ribonucleoprotein 1, C-terminal region 2","start":549,"end":632},{"id":"PF17904","name":"FMRP KH0 domain","start":123,"end":207},{"id":"PF18336","name":"Fragile X messenger ribonucleoprotein 1, Tudor domain","start":4,"end":52}],"gene3D":[{"start":216,"end":279,"id":"3.30.1370.10","name":"K Homology domain, type 1"},{"start":1,"end":50,"id":"2.30.30.140","name":"2.30.30.140"},{"start":51,"end":132,"id":"2.30.30.140","name":"2.30.30.140"}]},"uniref50":"UniRef50_Q06787","sequence":"MEELVVEVRGSNGAFYKAFVKDVHEDSITVAFENNWQPDRQIPFHDVRFPPPVGYNKDINESDEVEVYSRANEKEPCCWWLAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKDTFHKIKLDVPEDLRQMCAKEAAHKDFKKAVGAFSVTYDPENYQLVILSINEVTSKRAHMLIDMHFRSLRTKLSLIMRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGANIQQARKVPGVTAIDLDEDTCTFHIYGEDQDAVKKARSFLEFAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEAENEKNVPQEEEIMPPNSLPSNNSRVGPNAPEEKKHLDIKENSTHFSQPNSTKVQRVLVASSVVAGESQKPELKAWQGMVPFVFVGTKDSIANATVLLDYHLNYLKEVDQLRLERLQIDEQLRQIGASSRPPPNRTDKEKSYVTDDGQGMGRGSRPYRNRGHGRRGPGYTSGTNSEASNASETESDHRDELSDWSLAPTEEERESFLRRGDGRRRGGGGRGQGGRGRGGGFKGNDDHSRTDNRPRNPREAKGRTTDGSLQIRVDCNNERSVHTKTLQNTSSEGSRLRTGKDRNQKKEKPDSVDGQQPLVNGVP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q06787","disprot_id":"DP00134","ncbi_taxon_id":9606,"regions_counter":22,"creator":"mbuitron","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":422,"region_id":"DP00134r001","released":"2023_06","ec_id":"ECO:0006198","reference_html":"Dissecting FMR1, the protein responsible for fragile X syndrome, in its structural and functional domains. <i> Adinolfi S, Bagni C, Musco G, Gibson T, Mazzarella L, Pastore A. </i> RNA, 1999","term_id":"IDPO:0000002","curator_id":"vnugnes","start":281,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-01-19T13:21:26.773Z","reference_source":"pmid","term_name":"disorder","reference_id":"10496225","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The one-dimensional 1 H spectrum is typical of an unfolded and monomeric peptide with very little resonance dispersion (Fig. 4B).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:24:21.650Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":632,"term_name":"poly(A) binding","released":"2023_06","ec_name":"qualitative western immunoblotting evidence used in manual assertion","reference_html":"Dissecting FMR1, the protein responsible for fragile X syndrome, in its structural and functional domains. <i> Adinolfi S, Bagni C, Musco G, Gibson T, Mazzarella L, Pastore A. </i> RNA, 1999","term_id":"GO:0008143","curator_id":"vnugnes","start":516,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"10496225","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-01-19T13:50:44.567Z","reference_source":"pmid","ec_id":"ECO:0000279","region_id":"DP00134r006","ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a sequence of adenylyl residues in an RNA molecule, such as the poly(A) tail, a sequence of adenylyl residues at the 3' end of eukaryotic mRNA.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"statement":[{"text":"The binding of the FCT domain is so strong that it shows comparable affinity for poly-(rA), (rG) and (rU).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:24:40.541Z"}},{"start":444,"end":632,"reference_id":"30765518","reference_source":"pmid","reference_html":"Phosphoregulated FMRP phase separation models activity-dependent translation through bidirectional control of mRNA granule formation. <i> Tsang B, Arsenault J, Vernon RM, Lin H, Sonenberg N, Wang LY, Bah A, Forman-Kay JD. </i> Proc Natl Acad Sci U S A, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"GO:0043232","term_name":"intracellular non-membrane-bounded organelle","term_namespace":"Cellular component","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00134r008","statement":[{"text":"(C) DIC and fluorescent images of FMRP, FMRPΔLCR, and FMRPLCR protein (50 μM) mixed with Cy3-labeled sc1 RNA (5 μM) in 25 mM Na2PO4, pH 7.4, 30 mM NaCl, 2 mM DTT. Images show that only FMRP and FMRPLCR form droplets with sc1 RNA. (Scale bar, 10 μm.)","type":"Figure"},{"text":"Upon addition of Cy3-labeled sc1 RNA, droplets were formed with FMRP and FMRPLCR, but not with FMRPΔLCR (Fig. 1C). Our results show that FMRPLCR alone is necessary and sufficient to drive phase separation with sc1 RNA in vitro.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-03T10:46:41.449Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Organized structure of distinctive morphology and function, not bounded by a lipid bilayer membrane and occurring within the cell. Includes ribosomes, the cytoskeleton and chromosomes.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":444,"end":632,"reference_id":"30765518","reference_source":"pmid","reference_html":"Phosphoregulated FMRP phase separation models activity-dependent translation through bidirectional control of mRNA granule formation. <i> Tsang B, Arsenault J, Vernon RM, Lin H, Sonenberg N, Wang LY, Bah A, Forman-Kay JD. </i> Proc Natl Acad Sci U S A, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00134r009","statement":[{"text":"Overlay of 1H-15N heteronuclear single-quantum coherence spectra of the protein-depleted (i.e., monomeric) and condensed phases shows almost identical chemical shifts with narrow amide proton dispersion (∼8.0–8.7 ppm), reflecting similar global disordered character (SI Appendix, Fig. S3B).","type":"Results"},{"text":"In contrast, our solution NMR data show FMRPLCR to be primarily structurally disordered in the condensed phase.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-03T10:44:09.559Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":445,"end":632,"reference_id":"31439799","reference_source":"pmid","reference_html":"Phospho-dependent phase separation of FMRP and CAPRIN1 recapitulates regulation of translation and deadenylation. <i> Kim TH, Tsang B, Vernon RM, Sonenberg N, Kay LE, Forman-Kay JD. </i> Science, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00134r010","statement":[{"text":"To address these questions, we first reconstituted a model biomolecular condensate containing the intrinsically disordered C-terminal regions of FMRP (445–632, hereafter referred to as FMRP) and CAPRIN1 (607–709, hereafter referred to as CAPRIN1) for biophysical studies (Fig. 1A). ","type":"Article"},{"text":"Using isothermal titration calorimetry (ITC), we detected no FMRP-CAPRIN1 interaction; however, after in vitro phosphorylation of FMRP (pFMRP; fig. S3, A and B) by casein kinase II (CK2), a known kinase that Ser/Thr-phosphorylates FMRP in vivo (22, 23), we observed an effective 1 μM CAPRIN1-pFMRP binding affinity (fig. S4, A and B).","type":"Article"}],"interaction_partner":[{"db":"UniProt","id":"Q14444","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-03T10:57:41.994Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":445,"end":632,"reference_id":"31439799","reference_source":"pmid","reference_html":"Phospho-dependent phase separation of FMRP and CAPRIN1 recapitulates regulation of translation and deadenylation. <i> Kim TH, Tsang B, Vernon RM, Sonenberg N, Kay LE, Forman-Kay JD. </i> Science, 2019","date":"2023-01-19T14:45:17.193Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","released":"2023_06","version":4,"interaction_partner":[{"db":"UniProt","id":"Q14444","partner_start":null,"partner_end":null}],"region_id":"DP00134r011","statement":[{"text":"To address these questions, we first reconstituted a model biomolecular condensate containing the intrinsically disordered C-terminal regions of FMRP (445–632, hereafter referred to as FMRP) and CAPRIN1 (607–709, hereafter referred to as CAPRIN1) for biophysical studies (Fig. 1A). ","type":"Article"},{"text":"Fluorescence resonance energy transfer (FRET) experiments between highly phosphorylated Cy3-labeled pFMRP and Cy5-labeled CAPRIN1 yielded an apparent 6 μM binding affinity, with decreasing affinities corresponding to lower numbers of phosphate groups on pFMRP (Fig. 1B and fig. S3).","type":"Article"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:24:45.426Z"}},{"start":445,"end":632,"reference_id":"31439799","reference_source":"pmid","reference_html":"Phospho-dependent phase separation of FMRP and CAPRIN1 recapitulates regulation of translation and deadenylation. <i> Kim TH, Tsang B, Vernon RM, Sonenberg N, Kay LE, Forman-Kay JD. </i> Science, 2019","date":"2023-05-02T17:54:03.050Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","released":"2023_06","version":4,"region_id":"DP00134r012","statement":[{"text":"To address these questions, we first reconstituted a model biomolecular condensate containing the intrinsically disordered C-terminal regions of FMRP (445–632, hereafter referred to as FMRP) and CAPRIN1 (607–709, hereafter referred to as CAPRIN1) for biophysical studies (Fig. 1A). ","type":"Article"},{"text":"Using fluorescence microscopy, we observed that CAPRIN1 does not co–phase-separate with FMRP (fig. S4, C to E) even at protein concentrations of 1 mM, but does so with pFMRP over a wide range of concentrations (Fig. 1, C and D, and fig. S4D).","type":"Article"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q14444","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:24:47.792Z"}},{"start":445,"end":632,"reference_id":"31439799","reference_source":"pmid","reference_html":"Phospho-dependent phase separation of FMRP and CAPRIN1 recapitulates regulation of translation and deadenylation. <i> Kim TH, Tsang B, Vernon RM, Sonenberg N, Kay LE, Forman-Kay JD. </i> Science, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00134r013","statement":[{"text":"To identify residues mediating pFMRP-CAPRIN1 interactions, we used nuclear magnetic resonance (NMR) spectroscopy and assigned the CAPRIN1 resonances (fig. S5). Titrating pFMRP into [15N]CAPRIN1 resulted in co–phase separation, forming a turbid mixture containing many small droplets. Our results show global decreases in [15N]CAPRIN1 amide peak intensities with no sizable chemical shift perturbations (CSPs) (fig. S6).","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-03T10:58:03.548Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":527,"end":541,"reference_id":"21642970","reference_source":"pmid","reference_html":"Structure-function studies of FMRP RGG peptide recognition of an RNA duplex-quadruplex junction. <i> Phan AT, Kuryavyi V, Darnell JC, Serganov A, Majumdar A, Ilin S, Raslin T, Polonskaia A, Chen C, Clain D, Darnell RB, Patel DJ. </i> Nat Struct Mol Biol, 2011","date":"2022-07-19T13:09:26.833Z","curator_id":"mbuitron","curator_name":"Martín González Buitrón","curator_orcid":"0000-0003-1123-9853","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":6.8,"statements":[{"type":"Results","text":"NMR spectra of both peptide and RNA in 50 mM K-acetate, pH 6.8 at 25 °C, clearly indicated that the RGG peptide binds to sc1 RNA to form a stable complex. "}]},{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":null,"value":298,"statements":[{"type":"Results","text":"NMR spectra of both peptide and RNA in 50 mM K-acetate, pH 6.8 at 25 °C, clearly indicated that the RGG peptide binds to sc1 RNA to form a stable complex. "}]}],"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Curator statement","text":"\"GP\" are from TAG."}]}],"cross_refs":[{"db":"PDB","id":"2LA5"}],"region_id":"DP00134r014","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS000080DFC8","statements":[{"type":"Article","text":"In vitro selection identified guanine-rich RNA motifs that can bind tightly to FMRP, such as the 36-nt r(GCUGCGGUGUGGAAGGAGUGGUCGGGUUGCGCAGCG) sequence named sc1."}]}],"sequence_construct":"GPRRGDGRRRGGGGRGQ","statement":[{"text":"RNA-bound peptide (Fig. 1c) revealed a transition from a ‘random coil’ to a well-ordered conformation of the peptide upon RNA binding. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-19T14:29:40.536Z"}},{"start":527,"end":541,"reference_id":"21642970","reference_source":"pmid","reference_html":"Structure-function studies of FMRP RGG peptide recognition of an RNA duplex-quadruplex junction. <i> Phan AT, Kuryavyi V, Darnell JC, Serganov A, Majumdar A, Ilin S, Raslin T, Polonskaia A, Chen C, Clain D, Darnell RB, Patel DJ. </i> Nat Struct Mol Biol, 2011","date":"2023-04-26T13:35:34.445Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0002151","term_name":"G-quadruplex RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"cross_refs":[{"db":"PDB","id":"2LA5"}],"ec_go":"EXP","interaction_partner":[{"db":"RNAcentral","id":"URS000080DFC8","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00134r015","term_comment":"The structures of RNA and DNA G quartets differ regarding sugar conformation so that a protein binding to the RNA structure might not bind to the DNA structure.","term_def":"\"Binding to a G-quadruplex RNA structure, in which groups of four guanines adopt a flat, cyclic hydrogen-bonding arrangement known as a guanine tetrad.\" [PMID:18294969, PMID:18568163, PMID:19330720]","term_is_obsolete":false,"term_not_annotate":false,"statement":[{"text":"The N-terminal amino acids of the peptide are poorly defined in both crystal and NMR structures in agreement with the observation that only 10 residues in the middle of the peptide facilitate the G-quadruplex formation (37). ","type":"Results"},{"text":"These data suggest that the most important intermolecular interactions between RGG motif and sc1 RNA involve residues 6–18 of the peptide.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:24:52.738Z"}},{"start":529,"end":542,"reference_id":"26374839","reference_source":"pmid","reference_html":"Crystal structure reveals specific recognition of a G-quadruplex RNA by a β-turn in the RGG motif of FMRP. <i> Vasilyev N, Polonskaia A, Darnell JC, Darnell RB, Patel DJ, Serganov A. </i> Proc Natl Acad Sci U S A, 2015","date":"2023-04-26T13:31:07.679Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg527Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"To prepare the complex, chemically synthesized 35-mer sc1 RNA and 18-mer RGG peptide (residues 527–544, Uniprot ID: Q06787-1; Arg1Ala mutation) were mixed at 0.2 mM concentration in 50 mM K-Acetate (pH 6.7), heated at 95 °C for 2 min, and chilled on ice as previously described for the NMR studies."}]}],"cross_refs":[{"db":"PDB","id":"5DE5"},{"db":"PDB","id":"5DEA"},{"db":"PDB","id":"5DE8"}],"region_id":"DP00134r017","sequence_construct":"ARGDGRRRGGGGRGQGGR","statement":[{"text":"Although a solid evidence for the formation of β-turns in the unbound RGG box is missing, our structural data clearly shows feasibility of the turn formation in the RGG motif.","type":"Discussion"},{"text":"The structure contained two RNA-peptide complexes in the asymmetric unit, with all nucleotides and 13 amino acids of peptide chain present in the electron density map.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:813"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:104967"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:49867156"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS0000868538_32630"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:24:37.991Z"}},{"start":529,"end":542,"reference_id":"26374839","reference_source":"pmid","reference_html":"Crystal structure reveals specific recognition of a G-quadruplex RNA by a β-turn in the RGG motif of FMRP. <i> Vasilyev N, Polonskaia A, Darnell JC, Darnell RB, Patel DJ, Serganov A. </i> Proc Natl Acad Sci U S A, 2015","date":"2023-04-26T13:30:52.956Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0002151","term_name":"G-quadruplex RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"cross_refs":[{"db":"PDB","id":"5DE8"},{"db":"PDB","id":"5DEA"},{"db":"PDB","id":"5DE5"}],"ec_go":"EXP","interaction_partner":[{"db":"RNAcentral","id":"URS0000868538","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00134r018","term_comment":"The structures of RNA and DNA G quartets differ regarding sugar conformation so that a protein binding to the RNA structure might not bind to the DNA structure.","term_def":"\"Binding to a G-quadruplex RNA structure, in which groups of four guanines adopt a flat, cyclic hydrogen-bonding arrangement known as a guanine tetrad.\" [PMID:18294969, PMID:18568163, PMID:19330720]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg527Ala","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:813"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:104967"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:49867156"}],"statement":[{"text":"The structure contained two RNA-peptide complexes in the asymmetric unit, with all nucleotides and 13 amino acids of peptide chain present in the electron density map.","type":"Results"},{"text":"Our crystal structure provides the molecular basis for previous biochemical (21) and NMR (37) observations that formation of the sc1 RNA structure and RGG peptide binding critically depend on K+ cations.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:24:55.293Z"}},{"start":281,"end":422,"reference_id":"10496225","reference_source":"pmid","reference_html":"Dissecting FMR1, the protein responsible for fragile X syndrome, in its structural and functional domains. <i> Adinolfi S, Bagni C, Musco G, Gibson T, Mazzarella L, Pastore A. </i> RNA, 1999","date":"2023-01-19T13:22:44.035Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00134r019","statement":[{"text":"In the far-UV CD spectrum, the two expected helical peaks at 208 and 222 nm collapse into a single minimum shifted at 200 nm (Fig. 4A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:24:27.748Z"}},{"start":516,"end":632,"reference_id":"10496225","reference_source":"pmid","reference_html":"Dissecting FMR1, the protein responsible for fragile X syndrome, in its structural and functional domains. <i> Adinolfi S, Bagni C, Musco G, Gibson T, Mazzarella L, Pastore A. </i> RNA, 1999","date":"2023-01-19T13:23:43.707Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00134r020","statement":[{"text":"Its CD spectrum consists of a single minimum around 200 nm (Fig+ 5), characteristic\nof an unfolded state.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:24:29.888Z"}},{"start":516,"end":632,"reference_id":"10496225","reference_source":"pmid","reference_html":"Dissecting FMR1, the protein responsible for fragile X syndrome, in its structural and functional domains. <i> Adinolfi S, Bagni C, Musco G, Gibson T, Mazzarella L, Pastore A. </i> RNA, 1999","date":"2023-01-19T13:43:41.834Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0034046","term_name":"poly(G) binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IEP","region_id":"DP00134r021","statement":[{"text":"The binding of the FCT domain is so strong that it shows comparable affinity for poly-(rA), (rG) and (rU).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a sequence of guanine residues in an RNA molecule.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:24:57.733Z"}},{"start":516,"end":632,"reference_id":"10496225","reference_source":"pmid","reference_html":"Dissecting FMR1, the protein responsible for fragile X syndrome, in its structural and functional domains. <i> Adinolfi S, Bagni C, Musco G, Gibson T, Mazzarella L, Pastore A. </i> RNA, 1999","date":"2023-01-19T13:54:57.564Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008266","term_name":"poly(U) RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IEP","region_id":"DP00134r022","statement":[{"text":"The binding of the FCT domain is so strong that it shows comparable affinity for poly-(rA), (rG) and (rU).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a sequence of uracil residues in an RNA molecule.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:24:59.158Z"}}],"released":"2016_10","uniref100":"UniRef100_Q06787","date":"2016-09-04T18:53:04.000Z","acc":"Q06787","name":"Synaptic functional regulator FMR1","length":632,"organism":"Homo sapiens","dataset":["NDDs-related proteins","Condensates-related proteins","RNA-binding proteins"],"UniParc":"UPI000012AACA","genes":[{"name":{"value":"FMR1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:3775","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:3775"}}]}}],"alphafold_very_low_content":0.3987341772151899,"disorder_content":0.5237341772151899,"disprot_consensus":{"full":[{"start":281,"end":422,"type":"D"},{"start":444,"end":526,"type":"D"},{"start":527,"end":542,"type":"T"},{"start":543,"end":632,"type":"D"}],"Structural state":[{"start":281,"end":422,"type":"D"},{"start":444,"end":632,"type":"D"}],"Molecular function":[{"start":445,"end":632,"type":"F"}],"Cellular component":[{"start":444,"end":632,"type":"F"}],"Structural transition":[{"start":527,"end":542,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00447","name":"HSF-type DNA-binding","start":175,"end":274}],"gene3D":[{"start":166,"end":276,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}]},"uniref50":"UniRef50_P10961","sequence":"MNNAANTGTTNESNVSDAPRIEPLPSLNDDDIEKILQPNDIFTTDRTDASTTSSTAIEDIINPSLDPQSAASPVPSSSFFHDSRKPSTSTHLVRRGTPLGIYQTNLYGHNSRENTNPNSTLLSSKLLAHPPVPYGQNPDLLQHAVYRAQPSSGTTNAQPRQTTRRYQSHKSRPAFVNKLWSMLNDDSNTKLIQWAEDGKSFIVTNREEFVHQILPKYFKHSNFASFVRQLNMYGWHKVQDVKSGSIQSSSDDKWQFENENFIRGREDLLEKIIRQKGSSNNHNSPSGNGNPANGSNIPLDNAAGSNNSNNNISSSNSFFNNGHLLQGKTLRLMNEANLGDKNDVTAILGELEQIKYNQIAISKDLLRINKDNELLWQENMMARERHRTQQQALEKMFRFLTSIVPHLDPKMIMDGLGDPKVNNEKLNSANNIGLNRDNTGTIDELKSNDSFINDDRNSFTNATTNARNNMSPNNDDNSIDTASTNTTNRKKNIDENIKNNNDIINDIIFNTNLANNLSNYNSNNNAGSPIRPYKQRYLLKNRANSSTSSENPSLTPFDIESNNDRKISEIPFDDEEEEETDFRPFTSRDPNNQTSENTFDPNRFTMLSDDDLKKDSHTNDNKHNESDLFWDNVHRNIDEQDARLQNLENMVHILSPGYPNKSFNNKTSSTNTNSNMESAVNVNSPGFNLQDYLTGESNSPNSVHSVPSNGSGSTPLPMPNDNDTEHASTSVNQGENGSGLTPFLTVDDHTLNDNNTSEGSTRVSPDIKFSATENTKVSDNLPSFNDHSYSTQADTAPENAKKRFVEEIPEPAIVEIQDPTEYNDHRLPKRAKK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P10961","disprot_id":"DP00135","ncbi_taxon_id":559292,"regions_counter":7,"creator":"ameszaros","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":167,"region_id":"DP00135r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy. <i> Cho HS, Liu CW, Damberger FF, Pelton JG, Nelson HC, Wemmer DE. </i> Protein Sci, 1996","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"8745404","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy.","type":"Title"},{"text":"Using the DNA-binding domain as a structural reference, we show that the protein backbone of the N-terminal activation domain undergoes rapid, large-amplitude motions and is therefore unstructured. Difference CD data also show that the N-terminal activation domain remains random-coil, even in the presence of DNA.","type":"Abstract"},{"text":"In addition, we used two-dimensional heteronuclear 15N{1h} NOE NMR and measurements of 15N relaxation parameters to show that the N-terminal activation domains from both yeast strains have a high degree of flexibility, which is consistent with an unstructured state in solution. The results are particularly compelling because they offer the first positive evidence for a dynamically disordered transcriptional activation domain.","type":"Introduction"},{"text":"N-terminal activation domain of yeast HSF is unstructured","type":"Results"},{"text":"The remaining signals, attributable to the N-terminal activation domain, all had negative NOEs indicative of rapid, large-amplitude motions. This shows that the N-terminal activation domain of S. cerevisiae also behaves as an unstructured protein.","type":"Results"},{"text":"To confirm that the N-terminal activation domains were not unstructured because of denaturation at low pH, further NMR spectroscopic studies were performed at pH 5.75 (data not shown). Comparison of the chemical shift distribution in spectra acquired at higher pH with those at lower pH indicated no change in the structural state of the constructs. The DNA- binding domains remained folded, whereas the activation do- mains persisted in an unstructured state.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":260,"end":332,"reference_id":"8175654","reference_source":"pmid","reference_html":"Yeast heat shock transcription factor contains a flexible linker between the DNA-binding and trimerization domains. Implications for DNA binding by trimeric proteins. <i> Flick KE, Gonzalez L, Harrison CJ, Nelson HC. </i> J Biol Chem, 1994","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00135r004","statement":[{"text":"Yeast heat shock transcription factor contains a flexible linker between the DNA-binding and trimerization domains","type":"Title"},{"text":"The Proposed Linker Region Has No Ordered Secondary Structure-To look directly at the secondary structure of the linker, the CD spectra of the DNA-binding domain (S. cerevisiae residues 171-259) and the trimerization domain (S. cerevisiae residues 333-424) were subtracted from each of the CD spectra of the HSF derivatives. As shown in Fig. 4 B , it is apparent that the difference CD spectrum representing the linker region of Sc-DT(21L) is characteristic of random coil with a minimum at 230 nm and maximum at 220 nm (27).","type":"Results"},{"text":"The molar ellipticity (qprot) of the Sc-DT series of protein were each subtracted by the molar ellipticity of the isolated DNA-binding domain and the molar ellipticity of the isolated trimerization domain. The resulting difference spectra should approximate the spectra of the linker region alone. The difference circular dichroism spectra of Sc-DT(21L) and Sc-D(21L) show that the linker has no ordered secondary structure.","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-25T14:01:40.142Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":260,"end":332,"reference_id":"8175654","reference_source":"pmid","reference_html":"Yeast heat shock transcription factor contains a flexible linker between the DNA-binding and trimerization domains. Implications for DNA binding by trimeric proteins. <i> Flick KE, Gonzalez L, Harrison CJ, Nelson HC. </i> J Biol Chem, 1994","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00135r005","statement":[{"text":"Yeast heat shock transcription factor contains a flexible linker between the DNA-binding and trimerization domains","type":"Title"},{"text":"The Proposed Linker Region Has No Ordered Secondary Structure-To look directly at the secondary structure of the linker, the CD spectra of the DNA-binding domain (S. cerevisiae residues 171-259) and the trimerization domain (S. cerevisiae residues 333-424) were subtracted from each of the CD spectra of the HSF derivatives. As shown in Fig. 4 B , it is apparent that the difference CD spectrum representing the linker region of Sc-DT(21L) is characteristic of random coil with a minimum at 230 nm and maximum at 220 nm (27).","type":"Results"},{"text":"The molar ellipticity (qprot) of the Sc-DT series of protein were each subtracted by the molar ellipticity of the isolated DNA-binding domain and the molar ellipticity of the isolated trimerization domain. The resulting difference spectra should approximate the spectra of the linker region alone. The difference circular dichroism spectra of Sc-DT(21L) and Sc-D(21L) show that the linker has no ordered secondary structure.","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-25T14:01:49.101Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":1,"end":167,"reference_id":"8745404","reference_source":"pmid","reference_html":"Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy. <i> Cho HS, Liu CW, Damberger FF, Pelton JG, Nelson HC, Wemmer DE. </i> Protein Sci, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140677","term_name":"molecular function activator activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","released":"2022_03","version":3,"region_id":"DP00135r006","statement":[{"text":"Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy.","type":"Title"},{"text":"Using the DNA-binding domain as a structural reference, we show that the protein backbone of the N-terminal activation domain undergoes rapid, large-amplitude motions and is therefore unstructured. Difference CD data also show that the N-terminal activation domain remains random-coil, even in the presence of DNA.","type":"Abstract"},{"text":"Deletions of the entire C-terminal region result in a functional HSF at physiological temperatures (Nieto-Sotelo et al., 1990; Sorger, 1990); this implies that the N-terminal activation domain is sufficient for the required constitutive level of transcriptional activity.","type":"Introduction"},{"text":"In addition, we used two-dimensional heteronuclear 15N{1H} NOE NMR and measurements of 15N relaxation parameters to show that the N-terminal activation domains from both yeast strains have a high degree of flexibility, which is consistent with an unstructured state in solution. The results are particularly compelling because they offer the first positive evidence for a dynamically disordered transcriptional activation domain.","type":"Introduction"}],"term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":167,"reference_id":"8745404","reference_source":"pmid","reference_html":"Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy. <i> Cho HS, Liu CW, Damberger FF, Pelton JG, Nelson HC, Wemmer DE. </i> Protein Sci, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00135r007","statement":[{"text":"Far-UV CD spectroscopy, performed at pH 7.0, also indicate that the N-terminal activation domains of yeast HSF are unstructured. Figure 5A shows CD spectra for the DNA-binding domain, and for the N-terminal activation domain plus the DNA-binding domain, as well as the difference between the two. The difference spectrum is characteristic of a random coil. We also examined the possibility that the N-terminal activation do- main might behave differently when the DNA-binding domain is bound to a DNA-binding site (Fig. 5B). An examination of this CD difference spectrum indicates that binding of the DNA- binding domain to the DNA does not induce any structural changes in the N-terminal activation domain.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P10961","date":"2016-08-24T15:45:09.000Z","acc":"P10961","name":"Heat shock factor protein","length":833,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":["Condensates-related proteins","Stress response proteins"],"UniParc":"UPI000012CCF6","genes":[{"name":{"value":"HSF1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"3044612","url":"http://www.ncbi.nlm.nih.gov/pubmed/3044612","alternativeUrl":"https://europepmc.org/abstract/MED/3044612"}}]},"olnNames":[{"value":"YGL073W"}]}],"alphafold_very_low_content":0.6926770708283313,"disorder_content":0.28811524609843936,"disprot_consensus":{"full":[{"start":1,"end":167,"type":"D"},{"start":260,"end":332,"type":"D"}],"Structural state":[{"start":1,"end":167,"type":"D"},{"start":260,"end":332,"type":"D"}],"Disorder function":[{"start":260,"end":332,"type":"F"}],"Molecular function":[{"start":1,"end":167,"type":"F"}]}},{"acc":"P15865","sequence":"MSETAPAAPAAPAPAEKTPIKKKARKAAGGAKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKKAGAAKAKKPAGAAKKPKKATGTATPKKSTKKTPKKAKKPAAAAGAKKAKSPKKAKATKAKKAPKSPAKARAVKPKAAKPKTSKPKAAKPKKTAAKKK","alphafold_very_low_content":"0.3561643835616438","creator":"fquaglia","dataset":[],"date":"2016-08-11T15:48:13.000Z","disprot_id":"DP00136","features":{"pfam":[{"id":"PF00538","name":"linker histone H1 and H5 family","start":38,"end":108}],"gene3D":[{"start":35,"end":109,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain","_id":"685af523b4ac24d5329d79d3"}]},"genes":[{"name":{"value":"H1-4","evidences":[{"source":{"id":"P10412","name":"UniProtKB","url":"https://www.uniprot.org/uniprot/P10412","_id":"685af523b4ac24d5329d7a03"},"code":"ECO:0000250","_id":"685af523b4ac24d5329d7a02"}],"_id":"685af523b4ac24d5329d7a04"},"synonyms":[{"value":"H1f4","evidences":[{"source":{"id":"2776","name":"RGD","url":"https://rgd.mcw.edu/tools/genes/genes_view.cgi?id=2776","_id":"685af523b4ac24d5329d7a07"},"code":"ECO:0000312","_id":"685af523b4ac24d5329d7a06"}],"_id":"685af523b4ac24d5329d7a05"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d7a01"}],"length":219,"name":"Histone H1.4","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions_counter":20,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"UniParc":"UPI0000167967","uniref100":"UniRef100_P15865","uniref50":"UniRef50_P16401","uniref90":"UniRef90_P10412","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-25T09:24:17.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":219,"interaction_partner":[],"reference_html":"Nucleotide and calcium-induced conformational changes in histone H1. <i> Tarkka T, Oikarinen J, Grundström T. </i> FEBS Lett, 1997","reference_id":"9109385","region_id":"DP00136r018","released":"2022_03","sample":[],"statement":[{"type":"Results","text":" Without Pi in the solution, only 4.5±0.7% of the protein appeared folded into α-helix and an increase up to 10.5% was observed when the Pi concentration was increased to 50 mM (Fig. 1B).","_id":"685af523b4ac24d5329d79f7"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":0,"_id":"685af523b4ac24d5329d79f6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-25T10:27:36.997Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":219,"interaction_partner":[],"reference_html":"Nucleotide and calcium-induced conformational changes in histone H1. <i> Tarkka T, Oikarinen J, Grundström T. </i> FEBS Lett, 1997","reference_id":"9109385","region_id":"DP00136r019","released":"2022_03","sample":[{"db":"ChEBI","deviation":null,"entry_name":"sodium phosphate","id":"37586","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d79f9"},{"db":"ChEBI","deviation":null,"entry_name":"ATP","id":"15422","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d79fa"},{"db":null,"deviation":null,"id":null,"statements":[],"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_id":"UO:0000023","unit_name":"µg","value":null,"_id":"685af523b4ac24d5329d79fb"}],"statement":[{"type":"Results","text":"The presence of 10 mM sodium phosphate (Pi) had a large effect on its CD spectrum (Fig. 1 A). The changes obtained in the presence of Pi are characteristic of a large increase in the α-helicity of H1.","_id":"685af523b4ac24d5329d79fc"},{"type":"Results","text":"As little as 100 μM ATP produced corresponding effects on the CD spectrum of H1 as 10 mM sodium phosphate (Pi) did (cf. Fig. 1A,C). An increase in the α-helicity of H1 to 10.4±0.5% was obtained at a concentration of 500 μM ATP (Fig. 1D).","_id":"685af523b4ac24d5329d79fd"},{"type":"Results","text":"Addition of double-stranded poly(dA-dT) or poly(dI-dC) DNA to H1 resulted in an increase in the α-helicity of H1 (Fig. 2B and 3A). It increased from 4.5% up to a maximum of 9.4±0.2% and 8.3±0.6% respectively. Increasing DNA concentrations increased linearly the α-helicity of H1 up to a concentration where the H1-binding sites on the DNA could be estimated to correspond to the amount of H1 (data not shown).","_id":"685af523b4ac24d5329d79fe"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":0,"_id":"685af523b4ac24d5329d79f8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":219,"interaction_partner":[],"reference_html":"Nucleotide and calcium-induced conformational changes in histone H1. <i> Tarkka T, Oikarinen J, Grundström T. </i> FEBS Lett, 1997","reference_id":"9109385","region_id":"DP00136r020","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Addition of double-stranded poly(dA-dT) or poly(dI-dC) DNA to H1 resulted in an increase in the α-helicity of H1 (Fig. 2B and 3A). It increased from 4.5% up to a maximum of 9.4±0.2% and 8.3±0.6% respectively. Increasing DNA concentrations increased linearly the α-helicity of H1 up to a concentration where the H1-binding sites on the DNA could be estimated to correspond to the amount of H1 (data not shown).","_id":"685af523b4ac24d5329d7a00"}],"states_connection":[],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_go_domain":"F","term_id":"GO:0003677","term_is_binding":true,"term_is_obsolete":false,"term_name":"DNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":1,"_id":"685af523b4ac24d5329d79ff","reference_source":"pmid"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":219,"type":"T"}],"Structural state":[{"start":1,"end":219,"type":"D"}],"Structural transition":[{"start":1,"end":219,"type":"T"}],"Molecular function":[{"start":1,"end":219,"type":"F"}]}},{"acc":"P01050","sequence":"VVYTDCTESGQNLCLCEGSNVCGQGNKCILGSDGEKNQCVTGEGTPKPQSHNDGDFEEIPEEYLQ","alphafold_very_low_content":"0","creator":"gminervini","dataset":[],"date":"2016-08-23T16:51:52.000Z","disprot_id":"DP00137","features":{"pfam":[{"id":"PF00713","name":"Hirudin","start":1,"end":64}],"gene3D":[{"start":1,"end":65,"id":"2.70.10.10","name":"Thrombin Inhibitor (Hirudin), subunit I","_id":"685af523b4ac24d5329d7a09"}]},"genes":[],"length":65,"name":"Hirudin variant-1","ncbi_taxon_id":6421,"organism":"Hirudo medicinalis","regions_counter":9,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Spiralia","Lophotrochozoa","Annelida","Clitellata","Hirudinea","Hirudinida","Hirudiniformes","Hirudinidae","Hirudo"],"UniParc":"UPI000002BA98","uniref100":"UniRef100_P01050","uniref50":"UniRef50_P01050","uniref90":"UniRef90_P01050","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6HIR","_id":"685af523b4ac24d5329d7a15"},{"db":"PDB","id":"2HIR","_id":"685af523b4ac24d5329d7a16"},{"db":"PDB","id":"5HIR","_id":"685af523b4ac24d5329d7a17"},{"db":"PDB","id":"4HIR","_id":"685af523b4ac24d5329d7a18"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":50,"end":65,"interaction_partner":[],"reference_html":"Solution structure of recombinant hirudin and the Lys-47----Glu mutant: a nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study. <i> Folkers PJ, Clore GM, Driscoll PC, Dodt J, Köhler S, Gronenborn AM. </i> Biochemistry, 1989","reference_id":"2567183","region_id":"DP00137r005","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Analysis of the NOE data indicates that hirudin consists of an N-terminal compact domain (residues 1-49) held together by three disulfide linkages and a disordered C-terminal tail (residues 50-65) which does not fold back on the rest of the protein.","_id":"685af523b4ac24d5329d7a19"},{"type":"Results","text":"This was important as residues 55, 56, 57, and 59 possess virtually degenerate NH chemical shifts under all conditions studied. ","_id":"685af523b4ac24d5329d7a1a"},{"type":"Results","text":"We therefore conclude that there is no evidence that the C-terminus (residues 50-65) has an ordered structure or folds back onto the rest of the protein. The high degree of NH chemical shift degeneracy over a range of temperature and the absence of slowly exchanging amide protons are consistent with a “random-coil” structure for this portion of the molecule","_id":"685af523b4ac24d5329d7a1b"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d7a14","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1AHT","_id":"685af523b4ac24d5329d7a20"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":55,"end":64,"interaction_partner":[{"db":"UniProt","id":"P00734","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7a1d"}],"reference_html":"Crystal structure of human alpha-thrombin complexed with hirugen and p-amidinophenylpyruvate at 1.6 A resolution. <i> Chen Z, Li Y, Mulichak AM, Lewis SD, Shafer JA. </i> Arch Biochem Biophys, 1995","reference_id":"7574675","region_id":"DP00137r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Crystals of thrombin complexed with hirugen and APPA were obtained by soaking an α-thrombin-hirugen crystal in a solution of APPA.","_id":"685af523b4ac24d5329d7a1e"},{"type":"Results","text":"The rest of the hirugen molecule from residue Asp55' to Gln64' is well defined.","_id":"685af523b4ac24d5329d7a1f"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":1,"_id":"685af523b4ac24d5329d7a1c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1AHT","_id":"685af523b4ac24d5329d7a22"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-28T10:14:42.587Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":55,"end":64,"interaction_partner":[],"reference_html":"Crystal structure of human alpha-thrombin complexed with hirugen and p-amidinophenylpyruvate at 1.6 A resolution. <i> Chen Z, Li Y, Mulichak AM, Lewis SD, Shafer JA. </i> Arch Biochem Biophys, 1995","reference_id":"7574675","region_id":"DP00137r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Crystals of thrombin complexed with hirugen and APPA were obtained by soaking an α-thrombin-hirugen crystal in a solution of APPA.","_id":"685af523b4ac24d5329d7a23"},{"type":"Results","text":"The rest of the hirugen molecule from residue Asp55' to Gln64' is well defined.","_id":"685af523b4ac24d5329d7a24"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":0,"_id":"685af523b4ac24d5329d7a21","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1HRT","_id":"685af523b4ac24d5329d7a26"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":50,"end":65,"interaction_partner":[{"db":"UniProt","id":"P00735","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7a27"}],"reference_html":"The structure of a complex of bovine alpha-thrombin and recombinant hirudin at 2.8-A resolution. <i> Vitali J, Martin PD, Malkowski MG, Robertson WD, Lazar JB, Winant RC, Johnson PH, Edwards BF. </i> J Biol Chem, 1992","reference_id":"1517214","region_id":"DP00137r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In the complex with bovine α-thrombin, hirudin variant 1, whose sequence is shown in Fig. 2, has a compact NH2-terminal domain, comprised of residues 1h through 48h, and an extended COOH-terminal polypeptide chain, comprised of residues 49h through 65h (Figs. 3 and 4).","_id":"685af523b4ac24d5329d7a28"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":1,"_id":"685af523b4ac24d5329d7a25","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1HRT","_id":"685af523b4ac24d5329d7a2a"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-28T11:03:22.954Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":50,"end":65,"interaction_partner":[],"reference_html":"The structure of a complex of bovine alpha-thrombin and recombinant hirudin at 2.8-A resolution. <i> Vitali J, Martin PD, Malkowski MG, Robertson WD, Lazar JB, Winant RC, Johnson PH, Edwards BF. </i> J Biol Chem, 1992","reference_id":"1517214","region_id":"DP00137r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In the complex with bovine α-thrombin, hirudin variant 1, whose sequence is shown in Fig. 2, has a compact NH2-terminal domain, comprised of residues 1h through 48h, and an extended COOH-terminal polypeptide chain, comprised of residues 49h through 65h (Figs. 3 and 4).","_id":"685af523b4ac24d5329d7a2b"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":0,"_id":"685af523b4ac24d5329d7a29","reference_source":"pmid"}],"__v":0,"disorder_content":0.24615384615384617,"disprot_consensus":{"full":[{"start":50,"end":65,"type":"T"}],"Structural state":[{"start":50,"end":65,"type":"D"}],"Molecular function":[{"start":50,"end":65,"type":"F"}],"Structural transition":[{"start":50,"end":65,"type":"T"}]}},{"features":{"pfam":[{"id":"PF01279","name":"Parathyroid hormone family","start":35,"end":128}]},"uniref50":"UniRef50_P12272","sequence":"MQRRLVQQWSVAVFLLSYAVPSCGRSVEGLSRRLKRAVSEHQLLHDKGKSIQDLRRRFFLHHLIAEIHTAEIRATSEVSPNSKPSPNTKNHPVRFGSDDEGRYLTQETNKVETYKEQPLKTPGKKKKGKPGKRKEQEKKKRRTRSAWLDSGVTGSGLEGDHLSDTSTTSLELDSRRH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P12272","disprot_id":"DP00138","ncbi_taxon_id":9606,"regions_counter":10,"creator":"ftonello","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":50,"region_id":"DP00138r009","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for antibody discrimination between two hormones that recognize the parathyroid hormone receptor. <i> McKinstry WJ, Polekhina G, Diefenbach-Jagger H, Ho PW, Sato K, Onuma E, Gillespie MT, Martin TJ, Parker MW. </i> J Biol Chem, 2009","statement":[{"text":"Of 108 residues, only residues 14–31 of PTHrP were visible in the final electron density map, with residues 14–29 adopting a helical conformation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":37,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19346515","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3FFD"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-28T11:05:58.813Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":144,"region_id":"DP00138r010","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for antibody discrimination between two hormones that recognize the parathyroid hormone receptor. <i> McKinstry WJ, Polekhina G, Diefenbach-Jagger H, Ho PW, Sato K, Onuma E, Gillespie MT, Martin TJ, Parker MW. </i> J Biol Chem, 2009","statement":[{"text":"Of 108 residues, only residues 14–31 of PTHrP were visible in the final electron density map, with residues 14–29 adopting a helical conformation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":68,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19346515","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3FFD"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-28T11:05:56.279Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P12272","date":"2016-09-08T14:49:57.000Z","acc":"P12272","name":"Parathyroid hormone-related protein","length":177,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000047E25","genes":[{"name":{"value":"PTHLH"},"synonyms":[{"value":"PTHRP"}]}],"alphafold_very_low_content":0.1977401129943503,"disorder_content":0.5141242937853108,"disprot_consensus":{"full":[{"start":37,"end":50,"type":"D"},{"start":68,"end":144,"type":"D"}],"Structural state":[{"start":37,"end":50,"type":"D"},{"start":68,"end":144,"type":"D"}]}},{"acc":"P0A7L8","sequence":"MAHKKAGGSTRNGRDSEAKRLGVKRFGGESVLAGSIIVRQRGTKFHAGANVGCGRDHTLFAKADGKVKFEVKGPKNRKFISIEAE","alphafold_very_low_content":"0.011764705882352941","creator":"mnecci","dataset":["RNA-binding proteins"],"date":"2016-08-24T16:18:00.000Z","disprot_id":"DP00140","features":{"pfam":[{"id":"PF01016","name":"Ribosomal L27 protein","start":2,"end":82}],"gene3D":[{"start":21,"end":85,"id":"2.40.50.100","name":"2.40.50.100","_id":"685af523b4ac24d5329d7a2d"}]},"genes":[{"name":{"value":"rpmA","evidences":[],"_id":"685af523b4ac24d5329d7a41"},"synonyms":[],"olnNames":[{"value":"b3185","evidences":[],"_id":"685af523b4ac24d5329d7a42"},{"value":"JW3152","evidences":[],"_id":"685af523b4ac24d5329d7a43"}],"orfNames":[],"_id":"685af523b4ac24d5329d7a40"}],"length":85,"name":"50S ribosomal protein L27","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions_counter":8,"released":"2016_10","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"UniParc":"UPI0000133E00","uniref100":"UniRef100_A7ZS81","uniref50":"UniRef50_C5BFA2","uniref90":"UniRef90_A7ZS81","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-28T11:14:00.318Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":85,"interaction_partner":[],"reference_html":"Differential effects of replacing Escherichia coli ribosomal protein L27 with its homologue from Aquifex aeolicus. <i> Maguire BA, Manuilov AV, Zimmermann RA. </i> J Bacteriol, 2001","reference_id":"11673426","region_id":"DP00140r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The CD spectrum of E. coli L27 (Fig. 3a) indicates that the protein is unstructured.","_id":"685af523b4ac24d5329d7a3b"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-08-18T13:23:33.432Z","_id":"685af523b4ac24d5329d7a3c"},"version":0,"_id":"685af523b4ac24d5329d7a3a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-28T11:14:20.559Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":85,"interaction_partner":[],"reference_html":"Differential effects of replacing Escherichia coli ribosomal protein L27 with its homologue from Aquifex aeolicus. <i> Maguire BA, Manuilov AV, Zimmermann RA. </i> J Bacteriol, 2001","reference_id":"11673426","region_id":"DP00140r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"This inference was reinforced by 2D heteronuclear NMR analysis of a 15N-labeled sample of the E. coli protein, which demonstrated that there was no dispersion of the backbone amide or side-chain amine resonances (data not shown).","_id":"685af523b4ac24d5329d7a3e"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-08-18T13:23:32.287Z","_id":"685af523b4ac24d5329d7a3f"},"version":0,"_id":"685af523b4ac24d5329d7a3d","reference_source":"pmid"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":85,"type":"D"}],"Structural state":[{"start":1,"end":85,"type":"D"}]}},{"acc":"O95405","sequence":"MENYFQAEAYNLDKVLDEFEQNEDETVSSTLLDTKWNKILDPPSHRLSFNPTLASVNESAVSNESQPQLKVFSLAHSAPLTTEEEDHCANGQDCNLNPEIATMWIDENAVAEDQLIKRNYSWDDQCSAVEVGEKKCGNLACLPDEKNVLVVAVMHNCDKRTLQNDLQDCNNYNSQSLMDAFSCSLDNENRQTDQFSFSINESTEKDMNSEKQMDPLNRPKTEGRSVNHLCPTSSDSLASVCSPSQLKDDGSIGRDPSMSAITSLTVDSVISSQGTDGCPAVKKQENYIPDEDLTGKISSPRTDLGSPNSFSHMSEGILMKKEPAEESTTEESLRSGLPLLLKPDMPNGSGRNNDCERCSDCLVPNEVRADENEGYEHEETLGTTEFLNMTEHFSESQDMTNWKLTKLNEMNDSQVNEEKEKFLQISQPEDTNGDSGGQCVGLADAGLDLKGTCISESEECDFSTVIDTPAANYLSNGCDSYGMQDPGVSFVPKTLPSKEDSVTEEKEIEESKSECYSNIYEQRGNEATEGSGLLLNSTGDLMKKNYLHNFCSQVPSVLGQSSPKVVASLPSISVPFGGARPKQPSNLKLQIPKPLSDHLQNDFPANSGNNTKNKNDILGKAKLGENSATNVCSPSLGNISNVDTNGEHLESYEAEISTRPCLALAPDSPDNDLRAGQFGISARKPFTTLGEVAPVWVPDSQAPNCMKCEARFTFTKRRHHCRACGKVFCASCCSLKCKLLYMDRKEARVCVICHSVLMNAQAWENMMSASSQSPNPNNPAEYCSTIPPLQQAQASGALSSPPPTVMVPVGVLKHPGAEVAQPREQRRVWFADGILPNGEVADAAKLTMNGTSSAGTLAVSHDPVKPVTTSPLPAETDICLFSGSITQVGSPVGSAMNLIPEDGLPPILISTGVKGDYAVEEKPSQISVMQQLEDGGPDPLVFVLNANLLSMVKIVNYVNRKCWCFTTKGMHAVGQSEIVILLQCLPDEKCLPKDIFNHFVQLYRDALAGNVVSNLGHSFFSQSFLGSKEHGGFLYVTSTYQSLQDLVLPTPPYLFGILIQKWETPWAKVFPIRLMLRLGAEYRLYPCPLFSVRFRKPLFGETGHTIMNLLADFRNYQYTLPVVQGLVVDMEVRKTSIKIPSNRYNEMMKAMNKSNEHVLAGGACFNEKADSHLVCVQNDDGNYQTQAISIHNQPRKVTGASFFVFSGALKSSSGYLAKSSIVEDGVMVQITAENMDSLRQALREMKDFTITCGKADAEEPQEHIHIQWVDDDKNVSKGVVSPIDGKSMETITNVKIFHGSEYKANGKVIRWTEVFFLENDDQHNCLSDPADHSRLTEHVAKAFCLALCPHLKLLKEDGMTKLGLRVTLDSDQVGYQAGSNGQPLPSQYMNDLDSALVPVIHGGACQLSEGPVVMELIFYILENIV","alphafold_very_low_content":"0.5368421052631579","creator":"mnecci","dataset":[],"date":"2016-09-09T13:40:25.000Z","disprot_id":"DP00141","features":{"pfam":[{"id":"PF01363","name":"FYVE zinc finger","start":696,"end":757},{"id":"PF11409","name":"Smad anchor for receptor activation (SARA)","start":773,"end":811},{"id":"PF11979","name":"Smad anchor for receptor activation-like, C-terminal","start":1048,"end":1400}],"gene3D":[{"start":686,"end":772,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)","_id":"685af523b4ac24d5329d7a47"},{"start":773,"end":811,"id":"4.10.720.10","name":"Smad anchor for receptor activation, Smad-binding domain","_id":"685af523b4ac24d5329d7a48"},{"start":1168,"end":1272,"id":"3.30.1360.220","name":"Domain of unknown function (DUF3480), N-terminal subdomain","_id":"685af523b4ac24d5329d7a49"},{"start":1273,"end":1425,"id":"3.30.500.40","name":"3.30.500.40","_id":"685af523b4ac24d5329d7a4a"}]},"genes":[{"name":{"value":"ZFYVE9","evidences":[],"_id":"685af523b4ac24d5329d7a59"},"synonyms":[{"value":"MADHIP","evidences":[],"_id":"685af523b4ac24d5329d7a5a"},{"value":"SARA","evidences":[],"_id":"685af523b4ac24d5329d7a5b"},{"value":"SMADIP","evidences":[],"_id":"685af523b4ac24d5329d7a5c"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d7a58"}],"length":1425,"name":"Zinc finger FYVE domain-containing protein 9","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":6,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000167B33","uniref100":"UniRef100_O95405","uniref50":"UniRef50_O95405","uniref90":"UniRef90_O95405","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-28T11:38:50.512Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":766,"end":823,"interaction_partner":[],"reference_html":"Disorder in a target for the smad2 mad homology 2 domain and its implications for binding and specificity. <i> Chong PA, Ozdamar B, Wrana JL, Forman-Kay JD. </i> J Biol Chem, 2004","reference_id":"15231848","region_id":"DP00141r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The proton-nitrogen (1H,15N) HSQC spectrum of SARA SBD revealed a narrow range of amide proton chemical shifts characteristic of disordered proteins (Fig. 2).","_id":"685af523b4ac24d5329d7a54"},{"type":"Results","text":"These data provide strong evidence that the unbound SBD is disordered in solution.","_id":"685af523b4ac24d5329d7a55"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":0,"_id":"685af523b4ac24d5329d7a53","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":766,"end":823,"interaction_partner":[],"reference_html":"Disorder in a target for the smad2 mad homology 2 domain and its implications for binding and specificity. <i> Chong PA, Ozdamar B, Wrana JL, Forman-Kay JD. </i> J Biol Chem, 2004","reference_id":"15231848","region_id":"DP00141r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Although the full SBD bound with a dissociation constant of 240 \b 30 nM, the affinities for any single element of the SBD were \u00012500 – 8500-fold lower.","_id":"685af523b4ac24d5329d7a57"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":1,"_id":"685af523b4ac24d5329d7a56","reference_source":"pmid"}],"__v":0,"disorder_content":0.04070175438596491,"disprot_consensus":{"full":[{"start":766,"end":823,"type":"D"}],"Structural state":[{"start":766,"end":823,"type":"D"}],"Molecular function":[{"start":766,"end":823,"type":"F"}]}},{"acc":"P14602","sequence":"MTERRVPFSLLRSPSWEPFRDWYPAHSRLFDQAFGVPRLPDEWSQWFSAAGWPGYVRPLPAATAEGPAAVTLAAPAFSRALNRQLSSGVSEIRQTADRWRVSLDVNHFAPEELTVKTKEGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTLVSSSLSPEGTLTVEAPLPKAVTQSAEITIPVTFEARAQIGGPEAGKSEQSGAK","alphafold_very_low_content":"0.2727272727272727","creator":"dpiovesan","dataset":["Stress response proteins"],"date":"2016-08-23T12:32:53.000Z","disprot_id":"DP00142","features":{"pfam":[{"id":"PF00011","name":"Hsp20/alpha crystallin family","start":92,"end":188}],"gene3D":[{"start":71,"end":199,"id":"2.60.40.790","name":"2.60.40.790","_id":"685af523b4ac24d5329d7a5e"}]},"genes":[{"name":{"value":"Hspb1","evidences":[],"_id":"685af523b4ac24d5329d7a6c"},"synonyms":[{"value":"Hsp25","evidences":[],"_id":"685af523b4ac24d5329d7a6d"},{"value":"Hsp27","evidences":[],"_id":"685af523b4ac24d5329d7a6e"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d7a6b"}],"length":209,"name":"Heat shock protein beta-1","ncbi_taxon_id":10090,"organism":"Mus musculus","regions_counter":9,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"UniParc":"UPI00001707AE","uniref100":"UniRef100_P14602","uniref50":"UniRef50_P04792","uniref90":"UniRef90_P42930","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":192,"end":209,"interaction_partner":[],"reference_html":"1H NMR spectroscopy reveals that mouse Hsp25 has a flexible C-terminal extension of 18 amino acids. <i> Carver JA, Esposito G, Schwedersky G, Gaestel M. </i> FEBS Lett, 1995","reference_id":"7649277","region_id":"DP00142r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The C-terminal extension in Hsp25 (and those in c-crystallin) therefore have characteristics of many peptides in an aqueous environment, i.e. flexibility and no defined conformation [16].","_id":"685af523b4ac24d5329d7a60"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d7a5f","reference_source":"pmid","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-09T13:04:45.538Z"}},{"start":199,"end":204,"reference_id":"19021764","reference_source":"pmid","reference_html":"Glutamic acid residues in the C-terminal extension of small heat shock protein 25 are critical for structural and functional integrity. <i> Morris AM, Treweek TM, Aquilina JA, Carver JA, Walker MJ. </i> FEBS J, 2008","date":"2025-10-14T18:18:22.274Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0050821","term_name":"protein stabilization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu199Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu204Ala","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP00142r007","statement":[{"text":"Complete suppression [45] of yeast ADH precipitation was observed for wild-type Hsp25 at a molar ratio of 1.4 : 1.0 Hsp25 : ADH (Fig. 6). A decrease in suppression of ADH precipitation was observed at this ratio for all of the glutamic acid residue mutants. At all other ratios, the E199A mutant showed minor reductions in suppression of ADH precipitation compared with wild-type Hsp25, whereas the E190A and E204A mutants showed markedly reduced suppression. The Q194A mutant showed similar levels of suppression of aggregation to the wild-type protein at all ratios.","type":"Results"}],"term_comment":"","term_def":"\"Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":199,"end":204,"reference_id":"19021764","reference_source":"pmid","reference_html":"Glutamic acid residues in the C-terminal extension of small heat shock protein 25 are critical for structural and functional integrity. <i> Morris AM, Treweek TM, Aquilina JA, Carver JA, Walker MJ. </i> FEBS J, 2008","date":"2025-10-14T18:18:11.851Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0044183","term_name":"protein folding chaperone","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu199Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu204Ala","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP00142r008","statement":[{"text":" Taken together, the thermal and reduction stress assays demonstrate that each of the glutamic acid mutants, in particular E190A and E204A, are significantly less effective chaperones than is wild-type Hsp25 (Table 2).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","term_is_obsolete":false,"term_not_annotate":false},{"start":192,"end":209,"reference_id":"10727931","reference_source":"pmid","reference_html":"Mouse Hsp25, a small shock protein. The role of its C-terminal extension in oligomerization and chaperone action. <i> Lindner RA, Carver JA, Ehrnsperger M, Buchner J, Esposito G, Behlke J, Lutsch G, Kotlyarov A, Gaestel M. </i> Eur J Biochem, 2000","date":"2025-10-09T14:05:26.238Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0044183","term_name":"protein folding chaperone","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Arg192Lys209del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP00142r009","statement":[{"text":"As is shown in Fig. 4B, however, Hsp25ΔC18 did not stabilize α-lactalbumin in such an assay. In fact, with increasing amounts of Hsp25ΔC18, a proportional increase in precipitation of protein was observed suggesting that in addition to the precipitation of α-lactalbumin, Hsp25ΔC18 also precipitated out of solution upon addition of dithiothreitol.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","term_is_obsolete":false,"term_not_annotate":false}],"__v":0,"disorder_content":0.0861244019138756,"disprot_consensus":{"full":[{"start":192,"end":209,"type":"D"}],"Structural state":[{"start":192,"end":209,"type":"D"}],"Biological process":[{"start":199,"end":204,"type":"F"}],"Molecular function":[{"start":192,"end":209,"type":"F"}]}},{"features":{"pfam":[{"id":"PF15247","name":"Histone RNA hairpin-binding protein RNA-binding domain","start":191,"end":258}],"gene3D":[{"start":184,"end":258,"id":"1.10.8.1120","name":"Histone RNA hairpin-binding protein RNA-binding domain"}]},"uniref50":"UniRef50_Q9VAN6","sequence":"MLCEDQHMSVENTPQKGSGSLNSSASSISIDVKPTMQSWAQEVRAEFGHSDEASSSLNSSAASCGSLAKKETADGNLESKDGEGREMAFEFLDGVNEVKFERLVKEEKLKTPYKRRHSFTPPSNENSRSNSPNSSNSSANGDAAAPKGGNNPHSRNSKKSGNFRAHKEEKRVRHNSYTSSTSSSSSYTEADPAILSRRQKQIDYGKNTAAYERYVEMVPKDERTRDHPRTPNKYGKYSRRAFDGLVKIWRKSLHIYDPPTQARDTAKDSNSDSDSD","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_Q9VAN6","disprot_id":"DP00144","ncbi_taxon_id":7227,"regions_counter":18,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":276,"region_id":"DP00144r013","released":"2024_06","ec_id":"ECO:0006220","reference_html":"Molecular mechanisms for the regulation of histone mRNA stem-loop-binding protein by phosphorylation. <i> Zhang J, Tan D, DeRose EF, Perera L, Dominski Z, Marzluff WF, Tong L, Hall TM. </i> Proc Natl Acad Sci U S A, 2014","term_id":"IDPO:0000002","curator_id":"vnugnes","start":258,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-03-26T13:46:02.913Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4TUX"}],"reference_id":"25002523","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS000080E236_32630"}],"statement":[{"text":"Unexpectedly, the C-terminal region was disordered in structures of dSLBP with or without phosphorylation mimicry (dSLBP RPD-5E and dSLBP RPD-WT, respectively).","type":"Results"}]},{"start":108,"end":172,"reference_id":"15260482","reference_source":"pmid","reference_html":"The N-terminal domain of the Drosophila histone mRNA binding protein, SLBP, is intrinsically disordered with nascent helical structure. <i> Thapar R, Mueller GA, Marzluff WF. </i> Biochemistry, 2004","date":"2023-01-18T17:09:40.876Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00144r014","statement":[{"text":"Drosophila SLBP (dSLBP) gives two protease-resistant fragments when digested with a number of proteases ( 15). One fragment corresponds to the C-terminus of dSLBP, which contains the region necessary for histone pre-mRNA processing consisting of residues H172−D276, and the second fragment contains a portion of the amino terminus from residues G17−K108 (Figure 1). The remainder of the protein (amino acids 108−172) is very glycine- and serine-rich and likely unstructured.","type":"Results"}]},{"start":1,"end":16,"reference_id":"15260482","reference_source":"pmid","reference_html":"The N-terminal domain of the Drosophila histone mRNA binding protein, SLBP, is intrinsically disordered with nascent helical structure. <i> Thapar R, Mueller GA, Marzluff WF. </i> Biochemistry, 2004","date":"2023-01-18T17:13:55.799Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00144r015","statement":[{"text":"The mean molar ellipticity at 222 nm is a rough measure of helical content in proteins, and this value is quite small for both N-terminal constructs (θ222 = −2110 and θ222 = −1842 for residues 1−175 and 17−108, respectively). Therefore, only a small percentage of the molecule exists in a helical conformation at neutral pH and 25 °C. Surprisingly, no appreciable increase in helical content (as interpreted from the ellipticity at 222 nm) is observed for the 175-residue construct compared to the 91 residue domain suggesting that residues that lie outside the 91-residue domain are mostly flexible and unstructured.","type":"Results"}]},{"start":109,"end":175,"reference_id":"15260482","reference_source":"pmid","reference_html":"The N-terminal domain of the Drosophila histone mRNA binding protein, SLBP, is intrinsically disordered with nascent helical structure. <i> Thapar R, Mueller GA, Marzluff WF. </i> Biochemistry, 2004","date":"2023-01-18T17:14:06.302Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00144r016","statement":[{"text":"The mean molar ellipticity at 222 nm is a rough measure of helical content in proteins, and this value is quite small for both N-terminal constructs (θ222 = −2110 and θ222 = −1842 for residues 1−175 and 17−108, respectively). Therefore, only a small percentage of the molecule exists in a helical conformation at neutral pH and 25 °C. Surprisingly, no appreciable increase in helical content (as interpreted from the ellipticity at 222 nm) is observed for the 175-residue construct compared to the 91 residue domain suggesting that residues that lie outside the 91-residue domain are mostly flexible and unstructured.","type":"Results"}]},{"start":1,"end":175,"reference_id":"15260482","reference_source":"pmid","reference_html":"The N-terminal domain of the Drosophila histone mRNA binding protein, SLBP, is intrinsically disordered with nascent helical structure. <i> Thapar R, Mueller GA, Marzluff WF. </i> Biochemistry, 2004","date":"2023-01-18T17:17:53.041Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00144r017","statement":[{"text":"Remarkably, the chemical shifts of resonances in both the full-length protein and the 175-residue and 91-residue N-terminal domains have a very narrow dispersion in the amide proton region of 0.4 ppm that is centered around the random coil chemical shift (between 8.2 and 8.4 ppm) (Figure 3).","type":"Results"}]},{"start":17,"end":108,"reference_id":"15260482","reference_source":"pmid","reference_html":"The N-terminal domain of the Drosophila histone mRNA binding protein, SLBP, is intrinsically disordered with nascent helical structure. <i> Thapar R, Mueller GA, Marzluff WF. </i> Biochemistry, 2004","date":"2023-01-18T17:18:42.190Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00144r018","statement":[{"text":"Remarkably, the chemical shifts of resonances in both the full-length protein and the 175-residue and 91-residue N-terminal domains have a very narrow dispersion in the amide proton region of 0.4 ppm that is centered around the random coil chemical shift (between 8.2 and 8.4 ppm) (Figure 3).","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_Q9VAN6","date":"2016-08-23T16:59:59.000Z","acc":"Q9VAN6","name":"Histone RNA hairpin-binding protein","length":276,"organism":"Drosophila melanogaster","dataset":["RNA-binding proteins"],"UniParc":"UPI00000009AA","genes":[{"name":{"value":"Slbp"},"orfNames":[{"value":"CG11886"}]}],"alphafold_very_low_content":0.3079710144927536,"disorder_content":0.7028985507246377,"disprot_consensus":{"full":[{"start":1,"end":175,"type":"D"},{"start":258,"end":276,"type":"D"}],"Structural state":[{"start":1,"end":175,"type":"D"},{"start":258,"end":276,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00203","name":"Ribosomal protein S19","start":3,"end":83}],"gene3D":[{"start":1,"end":92,"id":"3.30.860.10","name":"30s Ribosomal Protein S19; Chain A"}]},"uniref50":"UniRef50_A0T0X6","sequence":"MPRSLKKGPFIDLHLLKKVEKAVESGDKKPLRTWSRRSTIFPNMIGLTIAVHNGRQHVPVFVTDEMVGHKLGEFAPTRTYRGHAADKKAKKK","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_Q7MYF5","disprot_id":"DP00147","ncbi_taxon_id":83333,"regions_counter":1,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":92,"region_id":"DP00147r001","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Structural analysis of kasugamycin inhibition of translation. <i> Schuwirth BS, Day JM, Hau CW, Janssen GR, Dahlberg AE, Cate JH, Vila-Sanjurjo A. </i> Nat Struct Mol Biol, 2006","term_id":"IDPO:0000002","curator_id":"vnugnes","start":82,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16998486","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-01-19T14:59:27.598Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4V4H"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The X-ray structure of the bacterial ribosome from Escherichia coli in complex with the antibiotic kasugamyin shows this region of the S19 protein lacks electron density, indicating it is disordered. ","type":"Curator statement"}]}],"released":"2016_10","uniref100":"UniRef100_A8AQL3","date":"2016-08-24T12:23:12.000Z","acc":"P0A7U3","name":"30S ribosomal protein S19","length":92,"organism":"Escherichia coli (strain K12)","dataset":["RNA-binding proteins"],"UniParc":"UPI0000134DD7","genes":[{"name":{"value":"rpsS"},"olnNames":[{"value":"b3316"},{"value":"JW3278"}]}],"alphafold_very_low_content":0.010869565217391304,"disorder_content":0.11956521739130435,"disprot_consensus":{"full":[{"start":82,"end":92,"type":"D"}],"Structural state":[{"start":82,"end":92,"type":"D"}]}},{"acc":"P03347","sequence":"MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAADTGHSSQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNTATIMMQRGNFRNQRKMVKCFNCGKEGHTARNCRAPRKKGCWKCGKEGHQMKDCTERQANFLGKIWPSYKGRPGNFLQSRPEPTAPPFLQSRPEPTAPPEESFRSGVETTTPPQKQEPIDKELYPLTSLRSLFGNDPSSQ","creator":"fquaglia","dataset":["Viral proteins","RNA-binding proteins"],"date":"2016-08-24T14:43:24.000Z","disprot_id":"DP00148","features":{"pfam":[{"id":"PF00098","name":"Zinc knuckle","start":391,"end":406},{"id":"PF00098","name":"Zinc knuckle","start":412,"end":428},{"id":"PF00540","name":"gag gene protein p17 (matrix protein)","start":2,"end":132},{"id":"PF00607","name":"gag protein p24 N-terminal domain","start":144,"end":251},{"id":"PF08705","name":"Gag protein p6","start":461,"end":498},{"id":"PF19317","name":"Gag protein p24 C-terminal domain","start":276,"end":349}],"gene3D":[{"start":133,"end":278,"id":"1.10.375.10","name":"Human Immunodeficiency Virus Type 1 Capsid Protein","_id":"685af523b4ac24d5329d7a74"},{"start":1,"end":132,"id":"1.10.150.90","name":"Immunodeficiency lentiviruses, gag gene matrix protein p17","_id":"685af523b4ac24d5329d7a75"},{"start":283,"end":347,"id":"1.10.1200.30","name":"1.10.1200.30","_id":"685af523b4ac24d5329d7a76"},{"start":390,"end":432,"id":"4.10.60.10","name":"Zinc finger, CCHC-type","_id":"685af523b4ac24d5329d7a77"},{"start":348,"end":389,"id":"1.20.5.760","name":"Single helix bin","_id":"685af523b4ac24d5329d7a78"}]},"genes":[{"name":{"value":"gag","evidences":[],"_id":"685af523b4ac24d5329d7a8a"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d7a89"}],"length":512,"name":"Gag polyprotein","ncbi_taxon_id":11678,"organism":"Human immunodeficiency virus type 1 group M subtype B (isolate BH10)","regions_counter":6,"released":"2016_10","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"UniParc":"UPI000014D17B","uniref100":"UniRef100_P03347","uniref50":"UniRef50_P04591","uniref90":"UniRef90_P03347","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0001238","ec_name":"nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":378,"end":389,"interaction_partner":[],"reference_html":"Determination of the structure of the nucleocapsid protein NCp7 from the human immunodeficiency virus type 1 by 1H NMR. <i> Morellet N, Jullian N, De Rocquigny H, Maigret B, Darlix JL, Roques BP. </i> EMBO J, 1992","reference_id":"1639074","region_id":"DP00148r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"An important observation was that no additional slowly exchanging protons arising from the (1-12) and (51-72) sequences surrounding the two fingers were observed in the spectrum of NCp7 (Figure 3c), suggesting that the N and C-terminal sequences were less structured than the central (13-51) domain of NCp7. ","_id":"685af523b4ac24d5329d7a82"},{"type":"Curator statement","text":"The residues 1-12 of the Nucleocapsid protein p7 (NCp7) corresponds to the region  378-389 of the Gag polyprotein.","_id":"685af523b4ac24d5329d7a83"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T10:09:42.822Z","_id":"685af523b4ac24d5329d7a84"},"version":1,"_id":"685af523b4ac24d5329d7a81","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0001238","ec_name":"nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":428,"end":449,"interaction_partner":[],"reference_html":"Determination of the structure of the nucleocapsid protein NCp7 from the human immunodeficiency virus type 1 by 1H NMR. <i> Morellet N, Jullian N, De Rocquigny H, Maigret B, Darlix JL, Roques BP. </i> EMBO J, 1992","reference_id":"1639074","region_id":"DP00148r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"An important observation was that no additional slowly exchanging protons arising from the (1-12) and (51-72) sequences surrounding the two fingers were observed in the spectrum of NCp7 (Figure 3c), suggesting that the N and C-terminal sequences were less structured than the central (13-51) domain of NCp7. ","_id":"685af523b4ac24d5329d7a86"},{"type":"Curator statement","text":"The residues 51-72 of the Nucleocapsid protein p7 (NCp7) corresponds to the region 428-449 of the Gag polyprotein.","_id":"685af523b4ac24d5329d7a87"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T10:09:43.857Z","_id":"685af523b4ac24d5329d7a88"},"version":1,"_id":"685af523b4ac24d5329d7a85","reference_source":"pmid"}],"__v":0,"disorder_content":0.06640625,"disprot_consensus":{"full":[{"start":378,"end":389,"type":"D"},{"start":428,"end":449,"type":"D"}],"Structural state":[{"start":378,"end":389,"type":"D"},{"start":428,"end":449,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00038","name":"Intermediate filament protein","start":88,"end":399},{"id":"PF04732","name":"Intermediate filament head (DNA binding) region","start":9,"end":87}],"gene3D":[{"start":122,"end":238,"id":"1.20.5.1160","name":"Vasodilator-stimulated phosphoprotein"},{"start":321,"end":400,"id":"1.20.5.170","name":"1.20.5.170"},{"start":252,"end":320,"id":"1.20.5.500","name":"Single helix bin"}]},"uniref50":"UniRef50_P07196","sequence":"MSSFYSEPYYSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGLMPSLENLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAQLLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRTTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRLSFTSVGSLTTGYSQSSQVFGRSAYGGLQTSSYLMSTRSFPSYYTSHVQEEQIEVEETIEAAKAEEAKDEPPSEGEAEEEGKEKEEAEAEAEAEEEGAQEEEEAAEKEESEEAKEEEGGEGEQGEETKEAEEEEKKDEGAGEEQATKKKD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Suina","Suidae","Sus"],"uniref90":"UniRef90_P02547","disprot_id":"DP00151","ncbi_taxon_id":9823,"regions_counter":3,"creator":"ftonello","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":549,"region_id":"DP00151r001","released":"2023_06","ec_id":"ECO:0006228","reference_html":"Specific recognition of coiled coils by infrared spectroscopy: analysis of the three structural domains of type III intermediate filament proteins. <i> Heimburg T, Schuenemann J, Weber K, Geisler N. </i> Biochemistry, 1996","term_id":"IDPO:0000002","curator_id":"vnugnes","start":444,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"8634266","version":3,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","date":"2023-01-19T15:14:01.103Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Band shape and maximum are very similar to those of polylysine at pH 7 (Kleinschmidt, 1993), myelin basic protein (Surewicz et al., 1987), and apocytochrome c (Muga et al., 1991a), all of which have predominantly random-coil structure.","type":"Results"}]},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":549,"term_name":"flexible C-terminal tail","start":444,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"8634266","version":4,"reference_html":"Specific recognition of coiled coils by infrared spectroscopy: analysis of the three structural domains of type III intermediate filament proteins. <i> Heimburg T, Schuenemann J, Weber K, Geisler N. </i> Biochemistry, 1996","date":"2023-01-19T15:13:51.309Z","term_id":"IDPO:0000031","ec_id":"ECO:0006228","region_id":"DP00151r002","ec_go":"EXP","disprot_namespace":"Disorder function","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Band shape and maximum are very similar to those of polylysine at pH 7 (Kleinschmidt, 1993), myelin basic protein (Surewicz et al., 1987), and apocytochrome c (Muga et al., 1991a), all of which have predominantly random-coil structure.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P02547","date":"2016-09-08T16:09:16.000Z","acc":"P02547","name":"Neurofilament light polypeptide","length":549,"organism":"Sus scrofa","dataset":[],"UniParc":"UPI0000F53704","genes":[{"name":{"value":"NEFL"}}],"alphafold_very_low_content":0.3114754098360656,"disorder_content":0.1930783242258652,"disprot_consensus":{"full":[{"start":444,"end":549,"type":"D"}],"Structural state":[{"start":444,"end":549,"type":"D"}],"Disorder function":[{"start":444,"end":549,"type":"F"}]}},{"features":{"pfam":[{"id":"PF06632","name":"XRCC4 N-terminal domain","start":17,"end":113},{"id":"PF21924","name":"XRCC4 coiled-coil","start":117,"end":194},{"id":"PF21925","name":"XRCC4 C-terminal region","start":223,"end":334}],"gene3D":[{"start":119,"end":213,"id":"1.20.5.370","name":"1.20.5.370"},{"start":1,"end":118,"id":"2.170.210.10","name":"DNA double-strand break repair and VJ recombination XRCC4, N-terminal"}]},"uniref50":"UniRef50_Q13426","sequence":"MERKISRIHLVSEPSITHFLQVSWEKTLESGFVITLTDGHSAWTGTVSESEISQEADDMAMEKGKYVGELRKALLSGAGPADVYTFNFSKESCYFFFEKNLKDVSFRLGSFNLEKVENPAEVIRELICYCLDTIAENQAKNEHLQKENERLLRDWNDVQGRFEKCVSAKEALETDLYKRFILVLNEKKTKIRSLHNKLLNAAQEREKDIKQEGETAICSEMTADRDPVYDESTDEESENQTDLSGLASAAVSKDDSIISSLDVTDIAPSRKRRQRMQRNLGTEPKMAPQENQLQEKENSRPDSSLPETSKKEHISAENMSLETLRNSSPEDLFDEI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q13426","disprot_id":"DP00152","ncbi_taxon_id":9606,"regions_counter":11,"creator":"zskalman","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":265,"region_id":"DP00152r008","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Crystal structure of the Xrcc4 DNA repair protein and implications for end joining. <i> Junop MS, Modesti M, Guarné A, Ghirlando R, Gellert M, Yang W. </i> EMBO J, 2000","term_id":"IDPO:0000002","curator_id":"vnugnes","start":204,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-01-19T15:20:36.441Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1FU1"}],"reference_id":"11080143","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Even though residues 204–265 are present, they are disordered in the crystal structure.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-20T10:00:15.533Z"}},{"start":202,"end":336,"reference_id":"34352203","reference_source":"pmid","reference_html":"Cryo-EM of NHEJ supercomplexes provides insights into DNA repair. <i> Chaplin AK, Hardwick SW, Stavridi AK, Buehl CJ, Goff NJ, Ropars V, Liang S, De Oliveira TM, Chirgadze DY, Meek K, Charbonnier JB, Blundell TL. </i> Mol Cell, 2021","date":"2023-01-19T15:38:00.480Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7NFC"},{"db":"PDB","id":"7NFE"}],"region_id":"DP00152r009","statement":[{"text":"The electron microscopy structures of the NHEJ super-complex, both in the monomer and dimer version, shows this region of the XRCC4 lacks electron density, indicating it is disordered. ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-20T10:00:17.146Z"}},{"start":262,"end":288,"reference_id":"38898102","reference_source":"pmid","reference_html":"Multivalent interactions of the disordered regions of XLF and XRCC4 foster robust cellular NHEJ and drive the formation of ligation-boosting condensates in vitro. <i> Vu DD, Bonucci A, Brenière M, Cisneros-Aguirre M, Pelupessy P, Wang Z, Carlier L, Bouvignies G, Cortes P, Aggarwal AK, Blackledge M, Gueroui Z, Belle V, Stark JM, Modesti M, Ferrage F. </i> Nat Struct Mol Biol, 2024","date":"2024-11-11T18:19:52.760Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"EXP","region_id":"DP00152r010","statement":[{"text":"When titrating the XRCC4CTR with 21mer double-stranded DNA, small changes in the chemical shift of residues within the DIM region were observed, suggesting that this region can bind transiently to DNA (Supplementary Fig. 8a,b).","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false},{"start":202,"end":336,"reference_id":"38898102","reference_source":"pmid","reference_html":"Multivalent interactions of the disordered regions of XLF and XRCC4 foster robust cellular NHEJ and drive the formation of ligation-boosting condensates in vitro. <i> Vu DD, Bonucci A, Brenière M, Cisneros-Aguirre M, Pelupessy P, Wang Z, Carlier L, Bouvignies G, Cortes P, Aggarwal AK, Blackledge M, Gueroui Z, Belle V, Stark JM, Modesti M, Ferrage F. </i> Nat Struct Mol Biol, 2024","date":"2024-11-11T18:21:05.367Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"BMRB","id":"52398"}],"region_id":"DP00152r011","statement":[{"text":"The 1H–15N HSQC spectrum of XRCC4 and XRCC4CTR displayed low proton chemical shift dispersion, a signature of disordered protein regions (Fig. 3a and Supplementary Fig. 2e–g), with no detectable signal from the folded domain.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_Q13426","date":"2016-09-08T21:59:06.000Z","acc":"Q13426","name":"DNA repair protein XRCC4","length":336,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI0000072B0A","genes":[{"name":{"value":"XRCC4","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8548796","url":"http://www.ncbi.nlm.nih.gov/pubmed/8548796","alternativeUrl":"https://europepmc.org/abstract/MED/8548796"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:12831","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:12831"}}]}}],"alphafold_very_low_content":0.31845238095238093,"disorder_content":0.4017857142857143,"disprot_consensus":{"full":[{"start":202,"end":336,"type":"D"}],"Structural state":[{"start":202,"end":336,"type":"D"}],"Molecular function":[{"start":262,"end":288,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00071","name":"Ras family","start":5,"end":164}],"gene3D":[{"start":1,"end":179,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_P01112","sequence":"MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLAARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMSCKCVLS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P01112","disprot_id":"DP00153","ncbi_taxon_id":9606,"regions_counter":21,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":189,"region_id":"DP00153r021","released":"2022_06","ec_id":"ECO:0006220","reference_html":"Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins. <i> Milburn MV, Tong L, deVos AM, Brünger A, Yamaizumi Z, Nishimura S, Kim SH. </i> Science, 1990","statement":[{"text":"The COOH-terminal 18 residues that are lacking or disordered in the crystal structures are represented as a shaded string.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":170,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"2406906","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-06-14T18:51:41.530Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4Q21"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17552","entry_name":"GDP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"}]}],"released":"2016_10","uniref100":"UniRef100_P01112","date":"2016-09-12T14:21:26.000Z","acc":"P01112","name":"GTPase HRas","length":189,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI0000001251","genes":[{"name":{"value":"HRAS"},"synonyms":[{"value":"HRAS1"}]}],"alphafold_very_low_content":0.06349206349206349,"disorder_content":0.10582010582010581,"disprot_consensus":{"full":[{"start":170,"end":189,"type":"D"}],"Structural state":[{"start":170,"end":189,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00804","name":"Syntaxin","start":28,"end":180},{"id":"PF05739","name":"SNARE domain","start":194,"end":271}],"gene3D":[{"start":180,"end":288,"id":"1.20.5.110","name":"1.20.5.110"},{"start":24,"end":150,"id":"1.20.58.70","name":"1.20.58.70"}]},"uniref50":"UniRef50_Q16623","sequence":"MKDRTQELRTAKDSDDDDDVTVTVDRDRFMDEFFEQVEEIRGFIDKIAENVEEVKRKHSAILASPNPDEKTKEELEELMSDIKKTANKVRSKLKSIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMSEYNATQSDYRERCKGRIQRQLEITGRTTTSEELEDMLESGNPAIFASGIIMDSSISKQALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVILGIIIASTIGGIFG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_P32851","disprot_id":"DP00155","ncbi_taxon_id":10116,"regions_counter":8,"creator":"agasparini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":26,"region_id":"DP00155r005","released":"2022_12","ec_id":"ECO:0005670","reference_html":"Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide. <i> Burkhardt P, Hattendorf DA, Weis WI, Fasshauer D. </i> EMBO J, 2008","term_id":"IDPO:0000002","curator_id":"vnugnes","start":10,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18337752","version":3,"ec_name":"x-ray crystallography evidence used in manual assertion","date":"2022-08-17T18:53:10.200Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3C98"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61765 "}],"statement":[{"text":"The dashed line represents residues 10–26 of syntaxin, which are not visible in the electron density maps.","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-20T10:01:18.375Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":26,"region_id":"DP00155r007","released":"2022_12","ec_id":"ECO:0005670","reference_html":"Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformation. <i> Colbert KN, Hattendorf DA, Weiss TM, Burkhardt P, Fasshauer D, Weis WI. </i> Proc Natl Acad Sci U S A, 2013","term_id":"IDPO:0000002","curator_id":"vnugnes","start":10,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"23858467","version":3,"ec_name":"x-ray crystallography evidence used in manual assertion","date":"2022-08-17T18:48:14.092Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4JEU"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61765"}],"statement":[{"text":"Syx1a N-peptide residues 10–26 were disordered (dashed line).","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-20T10:01:19.991Z"}}],"released":"2016_10","uniref100":"UniRef100_P32851","date":"2016-08-24T16:46:03.000Z","acc":"P32851","name":"Syntaxin-1A","length":288,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI0000136066","genes":[{"name":{"value":"Stx1a"},"synonyms":[{"value":"Sap"}]}],"alphafold_very_low_content":0.041666666666666664,"disorder_content":0.059027777777777776,"disprot_consensus":{"full":[{"start":10,"end":26,"type":"D"}],"Structural state":[{"start":10,"end":26,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00240","name":"Ubiquitin family","start":5,"end":78},{"id":"PF00627","name":"UBA/TS-N domain","start":162,"end":198},{"id":"PF00627","name":"UBA/TS-N domain","start":321,"end":355},{"id":"PF09280","name":"XPC-binding domain","start":232,"end":287}],"gene3D":[{"start":222,"end":288,"id":"1.10.10.540","name":"XPC-binding domain"},{"start":311,"end":361,"id":"1.10.8.10","name":"DNA helicase RuvA subunit, C-terminal domain"},{"start":156,"end":204,"id":"1.10.8.10","name":"DNA helicase RuvA subunit, C-terminal domain"},{"start":1,"end":82,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"}]},"uniref50":"UniRef50_P54725","sequence":"MAVTITLKTLQQQTFKIRMEPDETVKVLKEKIEAEKGRDAFPVAGQKLIYAGKILSDDVPIRDYRIDEKNFVVVMVTKTKAGQGTSAPPEASPTAAPESSTSFPPAPTSGMSHPPPAAREDKSPSEESAPTTSPESVSGSVPSSGSSGREEDAASTLVTGSEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTGIPGSPEPEHGSVQESQVSEQPATEAAGENPLEFLRDQPQFQNMRQVIQQNPALLPALLQQLGQENPQLLQQISRHQEQFIQMLNEPPGELADISDVEGEVGAIGEEAPQMNYIQVTPQEKEAIERLKALGFPESLVIQAYFACEKNENLAANFLLSQNFDDE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P54725","disprot_id":"DP00156","ncbi_taxon_id":9606,"regions_counter":6,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":160,"region_id":"DP00156r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"DNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5a. <i> Walters KJ, Lech PJ, Goh AM, Wang Q, Howley PM. </i> Proc Natl Acad Sci U S A, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":79,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14557549","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-01-23T15:51:06.136Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1OQY"},{"db":"PDB","id":"1QZE"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The hHR23a protein has four structural domains (Fig. 1A), which are connected by unstructured linker regions.","type":"Results"},{"text":"The average backbone rms deviations to the mean structure for the UBL (3–78), UBA1 (161–200), XPC-binding (232–282), and UBA2 (317–359) domains are 0.410, 0.530, 0.461, and 0.402, respectively.","type":"Figure"}]},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":160,"term_name":"flexible linker","start":79,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14557549","version":4,"reference_html":"DNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5a. <i> Walters KJ, Lech PJ, Goh AM, Wang Q, Howley PM. </i> Proc Natl Acad Sci U S A, 2003","date":"2023-01-23T15:52:18.194Z","term_id":"IDPO:0000033","ec_id":"ECO:0006165","region_id":"DP00156r002","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Disorder function","cross_refs":[{"db":"PDB","id":"1QZE"},{"db":"PDB","id":"1OQY"}],"statement":[{"text":"The hHR23a protein has four structural domains (Fig. 1A), which are connected by unstructured linker regions.","type":"Results"},{"text":"The average backbone rms deviations to the mean structure for the UBL (3–78), UBA1 (161–200), XPC-binding (232–282), and UBA2 (317–359) domains are 0.410, 0.530, 0.461, and 0.402, respectively.","type":"Figure"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":231,"region_id":"DP00156r003","released":"2023_06","ec_id":"ECO:0006165","reference_html":"DNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5a. <i> Walters KJ, Lech PJ, Goh AM, Wang Q, Howley PM. </i> Proc Natl Acad Sci U S A, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":201,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14557549","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-01-23T15:50:42.501Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1OQY"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The hHR23a protein has four structural domains (Fig. 1A), which are connected by unstructured linker regions.","type":"Results"},{"text":"The average backbone rms deviations to the mean structure for the UBL (3–78), UBA1 (161–200), XPC-binding (232–282), and UBA2 (317–359) domains are 0.410, 0.530, 0.461, and 0.402, respectively.","type":"Figure"}]},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":231,"term_name":"flexible linker","start":201,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14557549","version":4,"reference_html":"DNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5a. <i> Walters KJ, Lech PJ, Goh AM, Wang Q, Howley PM. </i> Proc Natl Acad Sci U S A, 2003","date":"2023-01-23T15:51:58.753Z","term_id":"IDPO:0000033","ec_id":"ECO:0006165","region_id":"DP00156r004","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Disorder function","cross_refs":[{"db":"PDB","id":"1QZE"},{"db":"PDB","id":"1OQY"}],"statement":[{"text":"The hHR23a protein has four structural domains (Fig. 1A), which are connected by unstructured linker regions.","type":"Results"},{"text":"The average backbone rms deviations to the mean structure for the UBL (3–78), UBA1 (161–200), XPC-binding (232–282), and UBA2 (317–359) domains are 0.410, 0.530, 0.461, and 0.402, respectively.","type":"Figure"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":316,"region_id":"DP00156r005","released":"2023_06","ec_id":"ECO:0006165","reference_html":"DNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5a. <i> Walters KJ, Lech PJ, Goh AM, Wang Q, Howley PM. </i> Proc Natl Acad Sci U S A, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":283,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14557549","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-01-23T15:50:11.903Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1OQY"},{"db":"PDB","id":"1QZE"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The hHR23a protein has four structural domains (Fig. 1A), which are connected by unstructured linker regions.","type":"Results"},{"text":"The average backbone rms deviations to the mean structure for the UBL (3–78), UBA1 (161–200), XPC-binding (232–282), and UBA2 (317–359) domains are 0.410, 0.530, 0.461, and 0.402, respectively.","type":"Figure"}]},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":316,"term_name":"flexible linker","start":283,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14557549","version":4,"reference_html":"DNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5a. <i> Walters KJ, Lech PJ, Goh AM, Wang Q, Howley PM. </i> Proc Natl Acad Sci U S A, 2003","date":"2023-01-23T15:51:37.393Z","term_id":"IDPO:0000033","ec_id":"ECO:0006165","region_id":"DP00156r006","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Disorder function","cross_refs":[{"db":"PDB","id":"1QZE"},{"db":"PDB","id":"1OQY"}],"statement":[{"text":"The hHR23a protein has four structural domains (Fig. 1A), which are connected by unstructured linker regions.","type":"Results"},{"text":"The average backbone rms deviations to the mean structure for the UBL (3–78), UBA1 (161–200), XPC-binding (232–282), and UBA2 (317–359) domains are 0.410, 0.530, 0.461, and 0.402, respectively.","type":"Figure"}]}],"released":"2016_10","uniref100":"UniRef100_P54725","date":"2016-09-09T11:55:42.000Z","acc":"P54725","name":"UV excision repair protein RAD23 homolog A","length":363,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000000D7F7","genes":[{"name":{"value":"RAD23A"}}],"alphafold_very_low_content":0.3140495867768595,"disorder_content":0.4049586776859504,"disprot_consensus":{"full":[{"start":79,"end":160,"type":"D"},{"start":201,"end":231,"type":"D"},{"start":283,"end":316,"type":"D"}],"Structural state":[{"start":79,"end":160,"type":"D"},{"start":201,"end":231,"type":"D"},{"start":283,"end":316,"type":"D"}],"Disorder function":[{"start":79,"end":160,"type":"F"},{"start":201,"end":231,"type":"F"},{"start":283,"end":316,"type":"F"}]}},{"features":{"pfam":[{"id":"PF09052","name":"SipA N-terminal domain","start":50,"end":263},{"id":"PF22163","name":"Salmonella Invasion protein A, C-terminal actin binding domain","start":520,"end":655}],"gene3D":[{"start":49,"end":263,"id":"1.10.4150.10","name":"SipA N-terminal domain-like"},{"start":514,"end":670,"id":"1.10.4110.10","name":"Salmonella invasion protein A, C-terminal actin-binding domain"}]},"uniref50":"UniRef50_E1WAC6","sequence":"MVTSVRTQPPVIMPGMQTEIKTQATNLAANLSAVRESATATLSGEIKGPQLEDFPALIKQASLDALFKCGKDAEALKEVFTNSNNVAGKKAIMEFAGLFRSALNATSDSPEAKTLLMKVGAEYTAQIIKDGLKEKSAFGPWLPETKKAEAKLENLEKQLLDIIKNNTGGELSKLSTNLVMQEVMPYIASCIEHNFGCTLDPLTRSNLTHLVDKAAAKAVEALDMCHQKLTQEQGTSVGREARHLEMQTLIPLLLRNVFAQIPADKLPDPKIPEPAAGPVPDGGKKAEPTGINININIDSSNHSVDNSKHINNSRSHVDNSQRHIDNSNHDNSRKTIDNSRTFIDNSQRNGESHHSTNSSNVSHSHSRVDSTTHQTETAHSASTGAIDHGIAGKIDVTAHATAEAVTNASSESKDGKVVTSEKGTTGETTSFDEVDGVTSKSIIGKPVQATVHGVDDNKQQSQTAEIVNVKPLASQLAGVENVKTDTLQSDTTVITGNKAGTTDNDNSQTDKTGPFSGLKFKQNSFLSTVPSVTNMHSMHFDARETFLGVIRKALEPDTSTPFPVRRAFDGLRAEILPNDTIKSAALKAQCSDIDKHPELKAKMETLKEVITHHPQKEKLAEIALQFAREAGLTRLKGETDYVLSNVLDGLIGDGSWRAGPAYESYLNKPGVDRVITTVDGLHMQR","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"],"uniref90":"UniRef90_E1WAC6","disprot_id":"DP00157","ncbi_taxon_id":99287,"regions_counter":21,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":513,"region_id":"DP00157r001","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms. <i> Lilic M, Galkin VE, Orlova A, VanLoock MS, Egelman EH, Stebbins CE. </i> Science, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":497,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14512630","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-01-19T18:42:51.950Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"1Q5Z"}],"statement":[{"text":"In the crystal, the protein is ordered only between residues 513 and 657 (with 16 and 12 residues disordered at the N- and C-termini, respectively), and the termini are located at opposite sides of the molecule.","type":"Article"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":670,"region_id":"DP00157r004","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms. <i> Lilic M, Galkin VE, Orlova A, VanLoock MS, Egelman EH, Stebbins CE. </i> Science, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":659,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14512630","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-01-19T18:43:33.284Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"1Q5Z"}],"statement":[{"text":"In the crystal, the protein is ordered only between residues 513 and 657 (with 16 and 12 residues disordered at the N- and C-termini, respectively), and the termini are located at opposite sides of the molecule.","type":"Article"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":513,"region_id":"DP00157r007","released":"2023_06","ec_id":"ECO:0006003","reference_html":"Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms. <i> Lilic M, Galkin VE, Orlova A, VanLoock MS, Egelman EH, Stebbins CE. </i> Science, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":446,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14512630","version":3,"ec_name":"electron microscopy evidence used in manual assertion","date":"2023-01-23T16:05:20.379Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"The density between the two SipA constructs differs most dramatically in the length of the elongated regions that extend from opposite ends of the globular core (Fig. 2, A and B). When the crystal structure is fit into the globular region of the EM density, the best positioning occurs with the N- and C-termini located proximal to each arm (Fig. 2, A and B). There is an ambiguity about the up-down orientation of the crystal structure within the reconstruction, but all reasonable fits place the disordered regions from the crystallized construct in a perfect position to contribute to the elongated density.","type":"Article"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":685,"region_id":"DP00157r010","released":"2023_06","ec_id":"ECO:0006003","reference_html":"Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms. <i> Lilic M, Galkin VE, Orlova A, VanLoock MS, Egelman EH, Stebbins CE. </i> Science, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":659,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14512630","version":3,"ec_name":"electron microscopy evidence used in manual assertion","date":"2023-01-23T16:06:00.350Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"The density between the two SipA constructs differs most dramatically in the length of the elongated regions that extend from opposite ends of the globular core (Fig. 2, A and B). When the crystal structure is fit into the globular region of the EM density, the best positioning occurs with the N- and C-termini located proximal to each arm (Fig. 2, A and B). There is an ambiguity about the up-down orientation of the crystal structure within the reconstruction, but all reasonable fits place the disordered regions from the crystallized construct in a perfect position to contribute to the elongated density.","type":"Article"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":513,"region_id":"DP00157r013","released":"2023_06","ec_id":"ECO:0007691","reference_html":"Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms. <i> Lilic M, Galkin VE, Orlova A, VanLoock MS, Egelman EH, Stebbins CE. </i> Science, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":426,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14512630","version":3,"ec_name":"cleavage assay evidence used in manual assertion","date":"2023-01-23T16:13:34.841Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"To further probe this hypothesis of flexible polypeptides at the N- and C-termini of the molecule, we subjected a larger construct, SipA425–684, to limited proteolysis with the relatively nonspecific protease subtilisin (Fig. 3E) (11). The protease cut very effectively until it approached a construct that was ordered in the crystals (SipA513–657), producing trimmed constructs that when subcloned and overexpressed were highly soluble, stable, and active to bind F-actin (Fig. 3, E and F).","type":"Article"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":685,"region_id":"DP00157r016","released":"2023_06","ec_id":"ECO:0007691","reference_html":"Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms. <i> Lilic M, Galkin VE, Orlova A, VanLoock MS, Egelman EH, Stebbins CE. </i> Science, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":659,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14512630","version":3,"ec_name":"cleavage assay evidence used in manual assertion","date":"2023-01-23T16:12:49.351Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"To further probe this hypothesis of flexible polypeptides at the N- and C-termini of the molecule, we subjected a larger construct, SipA425–684, to limited proteolysis with the relatively nonspecific protease subtilisin (Fig. 3E) (11). The protease cut very effectively until it approached a construct that was ordered in the crystals (SipA513–657), producing trimmed constructs that when subcloned and overexpressed were highly soluble, stable, and active to bind F-actin (Fig. 3, E and F).","type":"Article"}]},{"start":426,"end":513,"reference_id":"14512630","reference_source":"pmid","reference_html":"Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms. <i> Lilic M, Galkin VE, Orlova A, VanLoock MS, Egelman EH, Stebbins CE. </i> Science, 2003","date":"2023-01-23T16:11:04.863Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00157r019","statement":[{"text":"We determined the hydrodynamic radius of various SipA constructs (Fig. 3F) and found not only that the ordered core (as found in the crystals) was globular in solution but also that SipA constructs with additional polypeptide arms were elongated in solution and became increasingly elongated as more arm polypeptide was added (Fig. 3F).","type":"Article"}]},{"start":659,"end":685,"reference_id":"14512630","reference_source":"pmid","reference_html":"Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms. <i> Lilic M, Galkin VE, Orlova A, VanLoock MS, Egelman EH, Stebbins CE. </i> Science, 2003","date":"2023-01-23T16:11:33.834Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00157r020","statement":[{"text":"We determined the hydrodynamic radius of various SipA constructs (Fig. 3F) and found not only that the ordered core (as found in the crystals) was globular in solution but also that SipA constructs with additional polypeptide arms were elongated in solution and became increasingly elongated as more arm polypeptide was added (Fig. 3F).","type":"Article"}]},{"start":229,"end":242,"reference_id":"16507363","reference_source":"pmid","reference_html":"A common structural motif in the binding of virulence factors to bacterial secretion chaperones. <i> Lilic M, Vujanac M, Stebbins CE. </i> Mol Cell, 2006","date":"2025-02-06T11:58:15.875Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001171","ec_ontology":"ECO","ec_name":"crystallography evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"2FM9"}],"region_id":"DP00157r021","statement":[{"text":"Two N-terminal helices pack more loosely against this core fold, forming a small subdomain that extends into solution (protrusion) with the last ten amino acids as a random coil that is characterized by partial disorder and high temperature factors (Figure 1B).","type":"Results"},{"text":"(B) The overall fold of SipA48–264 drawn as a ribbon diagram with secondary structure elements and NH2-terminal protrusion labeled. Regions disordered in the crystal structure are shown as dotted lines connecting the appropriate regions of secondary structure.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-10T15:00:50.642Z"}}],"released":"2016_10","uniref100":"UniRef100_E1WAC6","date":"2016-08-24T17:38:29.000Z","acc":"P0CL52","name":"Cell invasion protein SipA","length":685,"organism":"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","dataset":["Bacterial virulence-related proteins"],"UniParc":"UPI00000CD31C","genes":[{"name":{"value":"sipA"},"synonyms":[{"value":"sspA"}],"olnNames":[{"value":"STM2882"}]}],"alphafold_very_low_content":0.4364963503649635,"disorder_content":0.18832116788321168,"disprot_consensus":{"full":[{"start":229,"end":242,"type":"D"},{"start":426,"end":513,"type":"D"},{"start":659,"end":685,"type":"D"}],"Structural state":[{"start":229,"end":242,"type":"D"},{"start":426,"end":513,"type":"D"},{"start":659,"end":685,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00028","name":"Cadherin domain","start":162,"end":255},{"id":"PF00028","name":"Cadherin domain","start":270,"end":367},{"id":"PF00028","name":"Cadherin domain","start":382,"end":479},{"id":"PF00028","name":"Cadherin domain","start":494,"end":584},{"id":"PF00028","name":"Cadherin domain","start":605,"end":688},{"id":"PF01049","name":"Cadherin, Y-type LIR-motif","start":820,"end":879},{"id":"PF08758","name":"Cadherin prodomain like","start":29,"end":118}],"gene3D":[{"start":788,"end":884,"id":"4.10.900.10","name":"TCF3-CBD (Catenin binding domain)"},{"start":593,"end":703,"id":"2.60.40.60","name":"Cadherins"},{"start":370,"end":483,"id":"2.60.40.60","name":"Cadherins"},{"start":148,"end":262,"id":"2.60.40.60","name":"Cadherins"},{"start":32,"end":119,"id":"2.60.40.60","name":"Cadherins"},{"start":263,"end":369,"id":"2.60.40.60","name":"Cadherins"},{"start":487,"end":592,"id":"2.60.40.60","name":"Cadherins"}]},"uniref50":"UniRef50_P09803","sequence":"MGARCRSFSALLLLLQVSSWLCQELEPESCSPGFSSEVYTFPVPERHLERGHVLGRVRFEGCTGRPRTAFFSEDSRFKVATDGTITVKRHLKLHKLETSFLVRARDSSHRELSTKVTLKSMGHHHHRHHHRDPASESNPELLMFPSVYPGLRRQKRDWVIPPISCPENEKGEFPKNLVQIKSNRDKETKVFYSITGQGADKPPVGVFIIERETGWLKVTQPLDREAIAKYILYSHAVSSNGEAVEDPMEIVITVTDQNDNRPEFTQEVFEGSVAEGAVPGTSVMKVSATDADDDVNTYNAAIAYTIVSQDPELPHKNMFTVNRDTGVISVLTSGLDRESYPTYTLVVQAADLQGEGLSTTAKAVITVKDINDNAPVFNPSTYQGQVPENEVNARIATLKVTDDDAPNTPAWKAVYTVVNDPDQQFVVVTDPTTNDGILKTAKGLDFEAKQQYILHVRVENEEPFEGSLVPSTATVTVDVVDVNEAPIFMPAERRVEVPEDFGVGQEITSYTAREPDTFMDQKITYRIWRDTANWLEINPETGAIFTRAEMDREDAEHVKNSTYVALIIATDDGSPIATGTGTLLLVLLDVNDNAPIPEPRNMQFCQRNPQPHIITILDPDLPPNTSPFTAELTHGASVNWTIEYNDAAQESLILQPRKDLEIGEYKIHLKLADNQNKDQVTTLDVHVCDCEGTVNNCMKAGIVAAGLQVPAILGILGGILALLILILLLLLFLRRRTVVKEPLLPPDDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPQYRPRPANPDEIGNFIDENLKAADSDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDQDQDYDYLNEWGNRFKKLADMYGGGEDD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P09803","disprot_id":"DP00159","ncbi_taxon_id":10090,"regions_counter":30,"creator":"fquaglia","regions":[{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":884,"term_name":"molecular adaptor activity","start":812,"ec_name":"experimental evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Cadherins are single pass transmembrane proteins that mediate Ca(2+)-dependent homophilic cell-cell adhesion by linking the cytoskeletons of adjacent cells. In adherens junctions, the cytoplasmic domain of cadherins bind to beta-catenin, which in turn binds to the actin-associated protein alpha-catenin. ","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11121423","version":4,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0000269","region_id":"DP00159r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":884,"term_name":"disorder to order","start":812,"ec_name":"experimental evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Our analysis shows that the cadherin cytoplasmic tail is unstructured in isolation but appears to become structured upon binding to β-catenin.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11121423","version":3,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0000269","region_id":"DP00159r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q02248","partner_end":null}],"ec_ontology":"ECO","end":884,"term_name":"protein binding","start":812,"ec_name":"experimental evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The physical properties of the E-cadherin cytoplasmic domain and its interactions with beta-catenin have been investigated. Proteolytic sensitivity, tryptophan fluorescence, circular dichroism, and (1)H NMR measurements indicate that murine E-cadherin cytoplasmic domain is unstructured. Upon binding to beta-catenin, the domain becomes resistant to proteolysis, suggesting that it structures upon binding. Cadherin-beta-catenin complex stability is modestly dependent on ionic strength, indicating that, contrary to previous proposals, the interaction is not dominated by electrostatics.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11121423","version":4,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0000269","region_id":"DP00159r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":884,"term_name":"molecular adaptor activity","start":812,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Cadherins are single pass transmembrane proteins that mediate Ca(2+)-dependent homophilic cell-cell adhesion by linking the cytoskeletons of adjacent cells. In adherens junctions, the cytoplasmic domain of cadherins bind to beta-catenin, which in turn binds to the actin-associated protein alpha-catenin. ","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11121423","version":4,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006204","region_id":"DP00159r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":884,"term_name":"disorder to order","start":812,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Our analysis shows that the cadherin cytoplasmic tail is unstructured in isolation but appears to become structured upon binding to β-catenin.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11121423","version":3,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00159r007","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q02248","partner_end":null}],"ec_ontology":"ECO","end":884,"term_name":"protein binding","start":812,"ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The physical properties of the E-cadherin cytoplasmic domain and its interactions with beta-catenin have been investigated. Proteolytic sensitivity, tryptophan fluorescence, circular dichroism, and (1)H NMR measurements indicate that murine E-cadherin cytoplasmic domain is unstructured. Upon binding to beta-catenin, the domain becomes resistant to proteolysis, suggesting that it structures upon binding. Cadherin-beta-catenin complex stability is modestly dependent on ionic strength, indicating that, contrary to previous proposals, the interaction is not dominated by electrostatics.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11121423","version":4,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00159r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":884,"term_name":"molecular adaptor activity","start":812,"ec_name":"cleavage assay evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Cadherins are single pass transmembrane proteins that mediate Ca(2+)-dependent homophilic cell-cell adhesion by linking the cytoskeletons of adjacent cells. In adherens junctions, the cytoplasmic domain of cadherins bind to beta-catenin, which in turn binds to the actin-associated protein alpha-catenin. ","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11121423","version":4,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0007691","region_id":"DP00159r010","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":884,"term_name":"disorder to order","start":812,"ec_name":"cleavage assay evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Our analysis shows that the cadherin cytoplasmic tail is unstructured in isolation but appears to become structured upon binding to β-catenin.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11121423","version":3,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0007691","region_id":"DP00159r011","ec_go":"IDA","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q02248","partner_end":null}],"ec_ontology":"ECO","end":884,"term_name":"protein binding","start":812,"ec_name":"cleavage assay evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The physical properties of the E-cadherin cytoplasmic domain and its interactions with beta-catenin have been investigated. Proteolytic sensitivity, tryptophan fluorescence, circular dichroism, and (1)H NMR measurements indicate that murine E-cadherin cytoplasmic domain is unstructured. Upon binding to beta-catenin, the domain becomes resistant to proteolysis, suggesting that it structures upon binding. Cadherin-beta-catenin complex stability is modestly dependent on ionic strength, indicating that, contrary to previous proposals, the interaction is not dominated by electrostatics.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11121423","version":4,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007691","region_id":"DP00159r012","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":884,"term_name":"molecular adaptor activity","start":812,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Cadherins are single pass transmembrane proteins that mediate Ca(2+)-dependent homophilic cell-cell adhesion by linking the cytoskeletons of adjacent cells. In adherens junctions, the cytoplasmic domain of cadherins bind to beta-catenin, which in turn binds to the actin-associated protein alpha-catenin. ","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11121423","version":4,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP00159r014","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":884,"term_name":"disorder to order","start":812,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Our analysis shows that the cadherin cytoplasmic tail is unstructured in isolation but appears to become structured upon binding to β-catenin.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11121423","version":3,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00159r015","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q02248","partner_end":null}],"ec_ontology":"ECO","end":884,"term_name":"protein binding","start":812,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The physical properties of the E-cadherin cytoplasmic domain and its interactions with beta-catenin have been investigated. Proteolytic sensitivity, tryptophan fluorescence, circular dichroism, and (1)H NMR measurements indicate that murine E-cadherin cytoplasmic domain is unstructured. Upon binding to beta-catenin, the domain becomes resistant to proteolysis, suggesting that it structures upon binding. Cadherin-beta-catenin complex stability is modestly dependent on ionic strength, indicating that, contrary to previous proposals, the interaction is not dominated by electrostatics.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11121423","version":4,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00159r016","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00159r017","ec_ontology":"ECO","end":884,"term_id":"GO:0005515","start":732,"version":4,"statement":[{"text":"Plakoglobin binds to the full 152-amino acid cytoplasmic domain of E-cadherin (Ecyto) with a dissociation constant KD of 85 nm.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P14923","partner_end":null}],"term_name":"protein binding","ec_name":"isothermal titration calorimetry evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19759396","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3IFQ"}],"term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"fquaglia","reference_html":"Interactions of plakoglobin and beta-catenin with desmosomal cadherins: basis of selective exclusion of alpha- and beta-catenin from desmosomes. <i> Choi HJ, Gross JC, Pokutta S, Weis WI. </i> J Biol Chem, 2009","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00159r018","ec_ontology":"ECO","end":884,"term_id":"GO:0005515","start":778,"version":4,"statement":[{"text":"Here, we report structural, biophysical, and biochemical studies aimed at understanding the molecular basis of selective exclusion of β-catenin and α-catenin from desmosomes. The crystal structure of the plakoglobin armadillo domain bound to phosphorylated E-cadherin shows virtually identical interactions to those observed between β-catenin and E-cadherin.","type":"Abstract"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P14923","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19759396","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3IFQ"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"fquaglia","reference_html":"Interactions of plakoglobin and beta-catenin with desmosomal cadherins: basis of selective exclusion of alpha- and beta-catenin from desmosomes. <i> Choi HJ, Gross JC, Pokutta S, Weis WI. </i> J Biol Chem, 2009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":852,"region_id":"DP00159r019","reference_id":"19759396","start":784,"term_id":"IDPO:0000011","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Here, we report structural, biophysical, and biochemical studies aimed at understanding the molecular basis of selective exclusion of β-catenin and α-catenin from desmosomes. The crystal structure of the plakoglobin armadillo domain bound to phosphorylated E-cadherin shows virtually identical interactions to those observed between β-catenin and E-cadherin.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"x-ray crystallography evidence used in manual assertion","version":3,"reference_html":"Interactions of plakoglobin and beta-catenin with desmosomal cadherins: basis of selective exclusion of alpha- and beta-catenin from desmosomes. <i> Choi HJ, Gross JC, Pokutta S, Weis WI. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"3IFQ"}],"term_name":"disorder to order","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":881,"region_id":"DP00159r020","reference_id":"19759396","start":855,"term_id":"IDPO:0000011","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Here, we report structural, biophysical, and biochemical studies aimed at understanding the molecular basis of selective exclusion of β-catenin and α-catenin from desmosomes. The crystal structure of the plakoglobin armadillo domain bound to phosphorylated E-cadherin shows virtually identical interactions to those observed between β-catenin and E-cadherin.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"x-ray crystallography evidence used in manual assertion","version":3,"reference_html":"Interactions of plakoglobin and beta-catenin with desmosomal cadherins: basis of selective exclusion of alpha- and beta-catenin from desmosomes. <i> Choi HJ, Gross JC, Pokutta S, Weis WI. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"3IFQ"}],"term_name":"disorder to order","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":884,"region_id":"DP00159r021","reference_id":"19759396","start":778,"term_id":"IDPO:0000045","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Here, we report structural, biophysical, and biochemical studies aimed at understanding the molecular basis of selective exclusion of β-catenin and α-catenin from desmosomes. The crystal structure of the plakoglobin armadillo domain bound to phosphorylated E-cadherin shows virtually identical interactions to those observed between β-catenin and E-cadherin.","type":"Abstract"},{"text":"Phosphorylated residues are Ser840, Ser 842 and Ser848.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"x-ray crystallography evidence used in manual assertion","version":3,"reference_html":"Interactions of plakoglobin and beta-catenin with desmosomal cadherins: basis of selective exclusion of alpha- and beta-catenin from desmosomes. <i> Choi HJ, Gross JC, Pokutta S, Weis WI. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"3IFQ"}],"term_name":"phosphorylation display site","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":884,"region_id":"DP00159r022","reference_id":"11121423","start":736,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Proteolytic sensitivity, tryptophan fluorescence, circular dichroism, and (1)H NMR measurements indicate that murine E-cadherin cytoplasmic domain is unstructured. Upon binding to beta-catenin, the domain becomes resistant to proteolysis, suggesting that it structures upon binding.","type":"Abstract"},{"text":"The fluoresence anisotropy data suggest that the Ecyto and DEcyto domains are unfolded under native conditions.","type":"Results"},{"text":"The cytoplasmic tail is the most highly conserved domain among type I cadherins (34). With a length of ∼150 residues, it is easily large enough to be an independently folded structural unit. We expressed the E- and DE-cadherin cytoplasmic domains in E. coli and purified them to homogeneity. Tryptophan fluorescence, circular dichroism, and one-dimensional proton NMR studies all lead to the same surprising conclusion: rEcyto and rDEcyto are unfolded in solution.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"experimental evidence used in manual assertion","version":3,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000269","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":884,"region_id":"DP00159r023","reference_id":"11121423","start":736,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Proteolytic sensitivity, tryptophan fluorescence, circular dichroism, and (1)H NMR measurements indicate that murine E-cadherin cytoplasmic domain is unstructured. Upon binding to beta-catenin, the domain becomes resistant to proteolysis, suggesting that it structures upon binding.","type":"Abstract"},{"text":"CD spectroscopy was therefore used to probe for the presence regular protein secondary structure. The spectra measured for rEcyto and rDEcyto at 0 °C are essentially identical and feature a single minimum in mean residue ellipticity at ∼202 nm (Fig. 1). This spectrum indicates a lack of secondary structure, which would be expected of an unstructured polypeptide. ","type":"Results"},{"text":"The cytoplasmic tail is the most highly conserved domain among type I cadherins (34). With a length of ∼150 residues, it is easily large enough to be an independently folded structural unit. We expressed the E- and DE-cadherin cytoplasmic domains in E. coli and purified them to homogeneity. Tryptophan fluorescence, circular dichroism, and one-dimensional proton NMR studies all lead to the same surprising conclusion: rEcyto and rDEcyto are unfolded in solution.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":884,"region_id":"DP00159r024","reference_id":"11121423","start":736,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Proteolytic sensitivity, tryptophan fluorescence, circular dichroism, and (1)H NMR measurements indicate that murine E-cadherin cytoplasmic domain is unstructured. Upon binding to beta-catenin, the domain becomes resistant to proteolysis, suggesting that it structures upon binding.","type":"Abstract"},{"text":"β-Catenin Binding Protects Ecyto from Proteolysis.","type":"Results"},{"text":"The cytoplasmic tail is the most highly conserved domain among type I cadherins (34). With a length of ∼150 residues, it is easily large enough to be an independently folded structural unit. We expressed the E- and DE-cadherin cytoplasmic domains in E. coli and purified them to homogeneity. Tryptophan fluorescence, circular dichroism, and one-dimensional proton NMR studies all lead to the same surprising conclusion: rEcyto and rDEcyto are unfolded in solution.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cleavage assay evidence used in manual assertion","version":3,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":884,"region_id":"DP00159r025","reference_id":"11121423","start":736,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Proteolytic sensitivity, tryptophan fluorescence, circular dichroism, and (1)H NMR measurements indicate that murine E-cadherin cytoplasmic domain is unstructured. Upon binding to beta-catenin, the domain becomes resistant to proteolysis, suggesting that it structures upon binding.","type":"Abstract"},{"text":"The cytoplasmic tail is the most highly conserved domain among type I cadherins (34). With a length of ∼150 residues, it is easily large enough to be an independently folded structural unit. We expressed the E- and DE-cadherin cytoplasmic domains in E. coli and purified them to homogeneity. Tryptophan fluorescence, circular dichroism, and one-dimensional proton NMR studies all lead to the same surprising conclusion: rEcyto and rDEcyto are unfolded in solution.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":884,"region_id":"DP00159r026","reference_id":"11121423","start":812,"term_id":"GO:0098772","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"It is proposed that binding of cadherins to beta-catenin prevents recognition of degradation signals that are exposed in the unstructured cadherin cytoplasmic domain, favoring a cell surface population of catenin-bound cadherins capable of participating in cell adhesion.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"experimental evidence used in manual assertion","version":4,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000269","term_name":"molecular function regulator","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":884,"region_id":"DP00159r027","reference_id":"11121423","start":812,"term_id":"GO:0098772","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"It is proposed that binding of cadherins to beta-catenin prevents recognition of degradation signals that are exposed in the unstructured cadherin cytoplasmic domain, favoring a cell surface population of catenin-bound cadherins capable of participating in cell adhesion.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":4,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"molecular function regulator","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":884,"region_id":"DP00159r028","reference_id":"11121423","start":812,"term_id":"GO:0098772","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"It is proposed that binding of cadherins to beta-catenin prevents recognition of degradation signals that are exposed in the unstructured cadherin cytoplasmic domain, favoring a cell surface population of catenin-bound cadherins capable of participating in cell adhesion.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"cleavage assay evidence used in manual assertion","version":4,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","term_name":"molecular function regulator","ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":884,"region_id":"DP00159r029","reference_id":"11121423","start":812,"term_id":"GO:0098772","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"It is proposed that binding of cadherins to beta-catenin prevents recognition of degradation signals that are exposed in the unstructured cadherin cytoplasmic domain, favoring a cell surface population of catenin-bound cadherins capable of participating in cell adhesion.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":4,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"molecular function regulator","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q02248","partner_end":null}],"ec_ontology":"ECO","end":884,"region_id":"DP00159r030","reference_id":"11121423","start":736,"term_id":"GO:0005515","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Mixtures of rEcyto or rDEcyto and various β-catenin constructs were incubated for more than 1 h at 4 °C and injected onto an Amersham Pharmacia Biotech HR 10/30 Superdex 200 size exclusion column equilibrated with 50 mm Tris-HCl, pH 8, 200 mm NaCl, 20 mm EDTA, and 1 mmDTT. ","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"chromatography evidence used in manual assertion","version":4,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","term_name":"protein binding","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P09803","date":"2016-08-22T14:32:00.000Z","acc":"P09803","name":"Cadherin-1","length":884,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000274CA","genes":[{"name":{"value":"Cdh1"}}],"alphafold_very_low_content":0.16855203619909503,"disorder_content":0.16855203619909503,"disprot_consensus":{"full":[{"start":732,"end":735,"type":"F"},{"start":736,"end":783,"type":"D"},{"start":784,"end":884,"type":"T"}],"Structural state":[{"start":736,"end":884,"type":"D"}],"Molecular function":[{"start":732,"end":884,"type":"F"}],"Structural transition":[{"start":784,"end":884,"type":"T"}],"Disorder function":[{"start":778,"end":884,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04354","name":"ZipA, C-terminal FtsZ-binding domain","start":194,"end":317}],"gene3D":[{"start":189,"end":328,"id":"3.30.1400.10","name":"ZipA, C-terminal FtsZ-binding domain"}]},"uniref50":"UniRef50_Q8FFC0","sequence":"MMQDLRLILIIVGAIAIIALLVHGFWTSRKERSSMFRDRPLKRMKSKRDDDSYDEDVEDDEGVGEVRVHRVNHAPANAQEHEAARPSPQHQYQPPYASAQPRQPVQQPPEAQVPPQHAPHPAQPVQQPAYQPQPEQPLQQPVSPQVAPAPQPVHSAPQPAQQAFQPAEPVAAPQPEPVAEPAPVMDKPKRKEAVIIMNVAAHHGSELNGELLLNSIQQAGFIFGDMNIYHRHLSPDGSGPALFSLANMVKPGTFDPEMKDFTTPGVTIFMQVPSYGDELQNFKLMLQSAQHIADEVGGVVLDDQRRMMTPQKLREYQDIIREVKDANA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_Q8FFC0","disprot_id":"DP00161","ncbi_taxon_id":83333,"regions_counter":2,"creator":"dpiovesan","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":185,"region_id":"DP00161r001","released":"2023_06","ec_id":"ECO:0006281","reference_html":"Structural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the C-terminal FtsZ-binding domain. <i> Ohashi T, Hale CA, de Boer PA, Erickson HP. </i> J Bacteriol, 2002","term_id":"IDPO:0000002","curator_id":"vnugnes","start":29,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"rotary shadowing electron microscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-01-23T16:26:39.330Z","reference_source":"pmid","term_name":"disorder","reference_id":"12107152","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"Occasionally, a very small globular particle or a thin extension could be seen close to the main globular particle but, for the most part, there was no visible structure corresponding to the charged and P/Q domains in ZipA(23-328). This suggested that the P/Q domain may be a largely unfolded polypeptide and invisible in the rotary shadowed specimen, consistent with the previous prediction from the sequence (3). We suggest that the charged domain may be unstructured as well because, in our experience, a 60-aa globular domain should be visible in rotary shadowing.","type":"Article"}]},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":185,"term_name":"flexible linker","released":"2023_06","ec_name":"rotary shadowing electron microscopy evidence used in manual assertion","reference_html":"Structural evidence that the P/Q domain of ZipA is an unstructured, flexible tether between the membrane and the C-terminal FtsZ-binding domain. <i> Ohashi T, Hale CA, de Boer PA, Erickson HP. </i> J Bacteriol, 2002","term_id":"IDPO:0000033","curator_id":"vnugnes","start":29,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12107152","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-01-23T16:30:54.104Z","reference_source":"pmid","ec_id":"ECO:0006281","region_id":"DP00161r002","ec_go":"IDA","disprot_namespace":"Disorder function","statement":[{"text":"Occasionally, a very small globular particle or a thin extension could be seen close to the main globular particle but, for the most part, there was no visible structure corresponding to the charged and P/Q domains in ZipA(23-328). This suggested that the P/Q domain may be a largely unfolded polypeptide and invisible in the rotary shadowed specimen, consistent with the previous prediction from the sequence (3). We suggest that the charged domain may be unstructured as well because, in our experience, a 60-aa globular domain should be visible in rotary shadowing.","type":"Article"},{"text":"We propose, on the basis of our EM analyses, that the tether is flexible and can span a maximum distance of 60 nm.","type":"Article"}]}],"released":"2016_10","uniref100":"UniRef100_C4ZVU3","date":"2016-08-23T16:12:06.000Z","acc":"P77173","name":"Cell division protein ZipA","length":328,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI000013C3E4","genes":[{"name":{"value":"zipA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00509","url":"https://hamap.expasy.org/unirule/MF_00509"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"9008158","url":"http://www.ncbi.nlm.nih.gov/pubmed/9008158","alternativeUrl":"https://europepmc.org/abstract/MED/9008158"}}]},"olnNames":[{"value":"b2412"},{"value":"JW2404"}]}],"alphafold_very_low_content":0.16158536585365854,"disorder_content":0.47865853658536583,"disprot_consensus":{"full":[{"start":29,"end":185,"type":"D"}],"Structural state":[{"start":29,"end":185,"type":"D"}],"Disorder function":[{"start":29,"end":185,"type":"F"}]}},{"features":{"pfam":[{"id":"PF09049","name":"Stannin transmembrane","start":2,"end":33},{"id":"PF09050","name":"Stannin unstructured linker","start":34,"end":59},{"id":"PF09051","name":"Stannin cytoplasmic","start":61,"end":87}],"gene3D":[{"start":1,"end":88,"id":"4.10.280.20","name":"membrane protein stannin"}]},"uniref50":"UniRef50_O75324","sequence":"MSIMDHSPTTGVVTVIVILIAIAALGALILGCWCYLRLQRISQSEDEESIVGDGETKEPFLLVQYSAKGPCVERKAKLMTPNGPEVHG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O75324","disprot_id":"DP00162","ncbi_taxon_id":9606,"regions_counter":5,"creator":"agasparini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":60,"region_id":"DP00162r001","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Structure, dynamics, and membrane topology of stannin: a mediator of neuronal cell apoptosis induced by trimethyltin chloride. <i> Buck-Koehntop BA, Mascioni A, Buffy JJ, Veglia G. </i> J Mol Biol, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":34,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16246365","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-08-17T19:06:59.210Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1ZZA"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The structure is composed of a single transmembrane helix from residues 10–33, a large dynamic unstructured linker region, and a distorted cytoplasmic helix from residues 61–79 that interacts with the surface of the lipid bilayer.","type":"Discussion"}]},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":60,"term_name":"flexible linker","start":34,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2022_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16246365","version":4,"reference_html":"Structure, dynamics, and membrane topology of stannin: a mediator of neuronal cell apoptosis induced by trimethyltin chloride. <i> Buck-Koehntop BA, Mascioni A, Buffy JJ, Veglia G. </i> J Mol Biol, 2005","date":"2022-08-17T19:08:17.593Z","term_id":"IDPO:0000033","ec_id":"ECO:0006165","region_id":"DP00162r003","ec_go":"EXP","disprot_namespace":"Disorder function","cross_refs":[{"db":"PDB","id":"1ZZA"}],"curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The structure is composed of a single transmembrane helix from residues 10–33, a large dynamic unstructured linker region, and a distorted cytoplasmic helix from residues 61–79 that interacts with the surface of the lipid bilayer.","type":"Discussion"},{"text":"Another distinguishing feature that separates SNN from the structures of the aforementioned proteins is that the two helical domains of SNN are connected by a rather long unstructured linker.","type":"Discussion"}]}],"released":"2016_10","uniref100":"UniRef100_O75324","date":"2016-08-25T11:55:43.000Z","acc":"O75324","name":"Stannin","length":88,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000001656","genes":[{"name":{"value":"SNN"}}],"alphafold_very_low_content":0.2159090909090909,"disorder_content":0.3068181818181818,"disprot_consensus":{"full":[{"start":34,"end":60,"type":"D"}],"Structural state":[{"start":34,"end":60,"type":"D"}],"Disorder function":[{"start":34,"end":60,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05773","name":"RWD domain","start":5,"end":155}]},"uniref50":"UniRef50_Q03768","sequence":"MDYKEEQKQELEVLESIYPDELRIINDEYPKIKFEVAIKLELDTGDSTSVLTKEHTIIAEFKLPENYPDEPCLISLEAQEVALNDNEEDNEEDEDEVEYDDHGNKVLKKFENLPDLISFKGYLPELTVQLESQIETDMLLGMQMCFALISSIKERCEQWYSEQLNKLEKQYELEAQEREKKEQAKFHGTKVTRESYLEWRSKFRQELKLDERDQVRRMKAHHGKLTGKQMFEQGVVGTGDEYMEEDDASVDDVAKGLAKTEIANQ","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q03768","disprot_id":"DP00163","ncbi_taxon_id":559292,"regions_counter":5,"creator":"ftonello","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":166,"region_id":"DP00163r002","released":"2023_06","ec_id":"ECO:0007689","reference_html":"Gir2 is an intrinsically unstructured protein that is present in Saccharomyces cerevisiae as a group of heterogeneously electrophoretic migrating forms. <i> Alves VS, Castilho BA. </i> Biochem Biophys Res Commun, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15896712","version":3,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2023-01-23T16:46:57.936Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Significantly, the N-terminal half containing residues 1–166 migrated with more than double the expected mass, thus surpassing the complete protein in the ratio expected/observed mass. These results clearly indicated that the amino-terminal half of Gir2 is responsible for the characteristic abnormal migration of Gir2 on SDS–PAGE.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":265,"region_id":"DP00163r003","released":"2023_06","ec_id":"ECO:0001191","reference_html":"Gir2 is an intrinsically unstructured protein that is present in Saccharomyces cerevisiae as a group of heterogeneously electrophoretic migrating forms. <i> Alves VS, Castilho BA. </i> Biochem Biophys Res Commun, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15896712","version":3,"ec_name":"in vitro cleavage assay evidence used in manual assertion","date":"2023-01-23T16:44:40.688Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"As shown in Fig. 1 (upper panel), Gir2 is extremely sensitive to proteolysis when compared to GST in the conditions used here. At 1:100 ratio of enzyme/substrate, Gir2 is readily degraded whereas GST is intact. Remarkably, even when using the lowest amount of enzyme (1:4000), proteolysis of Gir2 is readily detected.","type":"Results"}]},{"start":1,"end":166,"reference_id":"15896712","reference_source":"pmid","reference_html":"Gir2 is an intrinsically unstructured protein that is present in Saccharomyces cerevisiae as a group of heterogeneously electrophoretic migrating forms. <i> Alves VS, Castilho BA. </i> Biochem Biophys Res Commun, 2005","date":"2023-01-23T16:44:23.707Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001191","ec_ontology":"ECO","ec_name":"in vitro cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00163r004","statement":[{"text":" We also employed in these assays a truncated Gir2 protein comprising residues 1–166. His6–Gir2[1–166] seemed to be more sensitive to proteolysis than the complete protein, when the assays are normalized by the molar ratio of enzyme/substrate (Fig. 1, lower panel)","type":"Results"}]},{"start":1,"end":265,"reference_id":"14715270","reference_source":"pmid","reference_html":"Biophysical characterization of Gir2, a highly acidic protein of Saccharomyces cerevisiae with anomalous electrophoretic behavior. <i> Alves VS, Pimenta DC, Sattlegger E, Castilho BA. </i> Biochem Biophys Res Commun, 2004","date":"2023-01-23T16:53:47.427Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"region_id":"DP00163r005","statement":[{"text":"The similarity between the predicted Rs by gel filtration experiments (3.23 nm for His6-Gir2[1–265] and 3.18 nm for His6-Gir2[1–166]) and that predicted from conformational class (3.67 nm for His6-Gir2[1–265] and 3.21 nm for His6-Gir2[1–166]) suggests that this protein is a pre-molten globule (PMG).","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_Q03768","date":"2016-09-08T16:16:48.000Z","acc":"Q03768","name":"Protein GIR2","length":265,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":["Stress response proteins"],"UniParc":"UPI00000694E0","genes":[{"name":{"value":"GIR2"},"synonyms":[{"value":"DFRP2"}],"orfNames":[{"value":"YD8358.08"}],"olnNames":[{"value":"YDR152W"}]}],"alphafold_very_low_content":0.14339622641509434,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":265,"type":"D"}],"Structural state":[{"start":1,"end":265,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00428","name":"60s Acidic ribosomal protein","start":20,"end":105}],"gene3D":[{"start":1,"end":61,"id":"1.10.10.1410","name":"1.10.10.1410"}]},"uniref50":"UniRef50_P05318","sequence":"MSTESALSYAALILADSEIEISSEKLLTLTNAANVPVENIWADIFAKALDGQNLKDLLVNFSAGAAAPAGVAGGVAGGEAGEAEAEKEEEEAKEESDDDMGFGLFD","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P05318","disprot_id":"DP00164","ncbi_taxon_id":559292,"regions_counter":5,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":106,"region_id":"DP00164r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structural differences between Saccharomyces cerevisiae ribosomal stalk proteins P1 and P2 support their functional diversity. <i> Zurdo J, González C, Sanz JM, Rico M, Remacha M, Ballesta JP. </i> Biochemistry, 2000","term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"10913306","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"The P1α CD spectra show features of a virtually unordered protein with some negative ellipticiy around 222 nm which disappears completely when high concentrations of urea are added to the protein (data not shown). This suggests a residual α-helical content even though the protein seems to be mainly random-coil.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-14T13:22:10.156Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":106,"region_id":"DP00164r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural differences between Saccharomyces cerevisiae ribosomal stalk proteins P1 and P2 support their functional diversity. <i> Zurdo J, González C, Sanz JM, Rico M, Remacha M, Ballesta JP. </i> Biochemistry, 2000","term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"10913306","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"In agreement with the previous observations, NMR studies on the intact protein show very little signal dispersion (Figure 4) and very fast amide exchange when protein is incubated in the presence of deuterated water (data not shown).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-14T13:23:06.235Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":106,"reference_id":"10913306","reference_source":"pmid","reference_html":"Structural differences between Saccharomyces cerevisiae ribosomal stalk proteins P1 and P2 support their functional diversity. <i> Zurdo J, González C, Sanz JM, Rico M, Remacha M, Ballesta JP. </i> Biochemistry, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P02400","partner_start":null,"partner_end":null}],"region_id":"DP00164r004","statement":[{"text":"Incubation of both proteins was followed by far-UV CD and 1D-NMR measurements, and spectra were compared with those of the isolated proteins under the same conditions. The CD spectra of the protein mixture, when compared to the arithmetical addition of spectra from the individual proteins indicate that some secondary structural changes take place upon incubation of both proteins together (Figure 9A).","type":"Results"},{"text":"Protein interactions seems to increase the secondary structure of one or both proteins.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-14T13:23:12.765Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":106,"reference_id":"10913306","reference_source":"pmid","reference_html":"Structural differences between Saccharomyces cerevisiae ribosomal stalk proteins P1 and P2 support their functional diversity. <i> Zurdo J, González C, Sanz JM, Rico M, Remacha M, Ballesta JP. </i> Biochemistry, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P02400","partner_start":null,"partner_end":null}],"region_id":"DP00164r005","statement":[{"text":"Incubation of both proteins was followed by far-UV CD and 1D-NMR measurements, and spectra were compared with those of the isolated proteins under the same conditions. The CD spectra of the protein mixture, when compared to the arithmetical addition of spectra from the individual proteins indicate that some secondary structural changes take place upon incubation of both proteins together (Figure 9A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-14T13:23:19.367Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P05318","date":"2016-08-24T18:17:26.000Z","acc":"P05318","name":"60S acidic ribosomal protein P1-alpha","length":106,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000013424C","genes":[{"name":{"value":"RPP1A","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9559554","url":"http://www.ncbi.nlm.nih.gov/pubmed/9559554","alternativeUrl":"https://europepmc.org/abstract/MED/9559554"}}]},"synonyms":[{"value":"L12EIIA"},{"value":"RPA1"},{"value":"RPLA1"}],"olnNames":[{"value":"YDL081C"}]}],"alphafold_very_low_content":0.22641509433962265,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":106,"type":"D"}],"Structural state":[{"start":1,"end":106,"type":"D"}],"Molecular function":[{"start":1,"end":106,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00992","name":"Troponin","start":46,"end":177},{"id":"PF11636","name":"Troponin I residues 1-32","start":1,"end":31}],"gene3D":[{"start":31,"end":191,"id":"1.20.5.350","name":"1.20.5.350"}]},"uniref50":"UniRef50_P19429","sequence":"MADGSSDAAREPRPAPAPIRRRSSNYRAYATEPHAKKKSKISASRKLQLKTLLLQIAKQELEREAEERRGEKGRALSTRCQPLELAGLGFAELQDLCRQLHARVDKVDEERYDIEAKVTKNITEIADLTQKIFDLRGKFKRPTLRRVRISADAMMQALLGARAKESLDLRAHLKQVKKEDTEKENREVGDWRKNIDALSGMEGRKKKFES","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P19429","disprot_id":"DP00166","ncbi_taxon_id":9606,"regions_counter":11,"creator":"dpiovesan","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":210,"region_id":"DP00166r004","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form. <i> Takeda S, Yamashita A, Maeda K, Maéda Y. </i> Nature, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":192,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-01-23T17:16:26.614Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1J1D"}],"reference_id":"12840750","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63316"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P45379"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"As described above, most of the electron densities associated with the potential actin–tropomyosin interfaces are ambiguous. These include the inhibitory region (residues 137–148) and the C-terminus of TnI (residues 163–210 in Tn52KA and 192–210 in Tn52KB), and the C-TnT (residues 272–288).","type":"Article"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr31Met","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys80Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys97Ala","start":null,"end":null,"position":null}],"sequence_construct":"MEPHAKKKSKISASRKLQLKTLLLQIAKQELEREAEERRGEKGRALSTRAQPLELAGLGFAELQDLARQLHARVDKVDEERYDIEAKVTKNITEIADLTQKIFDLRGKFKRPTLRRVRISADAMMQALLGARAKESLDLRAHLKQVKKEDTEKENREVGDWRKNIDALSGMEGRKKKFES"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":148,"region_id":"DP00166r005","reference_id":"12840750","start":137,"term_id":"IDPO:0000002","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"As described above, most of the electron densities associated with the potential actin–tropomyosin interfaces are ambiguous. These include the inhibitory region (residues 137–148) and the C-terminus of TnI (residues 163–210 in Tn52KA and 192–210 in Tn52KB), and the C-TnT (residues 272–288).","type":"Article"},{"text":"Third, the link through TnI, the inhibitory region that connects H2(I) and H3(I), is not well defined in the present structures, indicating that this link is also flexible.","type":"Article"}],"curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form. <i> Takeda S, Yamashita A, Maeda K, Maéda Y. </i> Nature, 2003","date":"2023-01-23T17:17:15.670Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1J1E"},{"db":"PDB","id":"1J1D"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63316"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P45379"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr31Met","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys80Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys97Ala","start":null,"end":null,"position":null}],"sequence_construct":"MEPHAKKKSKISASRKLQLKTLLLQIAKQELEREAEERRGEKGRALSTRAQPLELAGLGFAELQDLARQLHARVDKVDEERYDIEAKVTKNITEIADLTQKIFDLRGKFKRPTLRRVRISADAMMQALLGARAKESLDLRAHLKQVKKEDTEKENREVGDWRKNIDALSGMEGRKKKFES"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":148,"region_id":"DP00166r007","reference_id":"12840750","start":137,"term_id":"IDPO:0000033","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"As described above, most of the electron densities associated with the potential actin–tropomyosin interfaces are ambiguous. These include the inhibitory region (residues 137–148) and the C-terminus of TnI (residues 163–210 in Tn52KA and 192–210 in Tn52KB), and the C-TnT (residues 272–288).","type":"Article"},{"text":"Third, the link through TnI, the inhibitory region that connects H2(I) and H3(I), is not well defined in the present structures, indicating that this link is also flexible.","type":"Article"}],"curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":5,"reference_html":"Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form. <i> Takeda S, Yamashita A, Maeda K, Maéda Y. </i> Nature, 2003","date":"2023-03-21T18:44:23.260Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1J1E"},{"db":"PDB","id":"1J1D"}],"term_name":"flexible linker","ec_go":"EXP","disprot_namespace":"Disorder function","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr31Met","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys80Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys97Ala","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63316"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P45379"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"sequence_construct":"MEPHAKKKSKISASRKLQLKTLLLQIAKQELEREAEERRGEKGRALSTRAQPLELAGLGFAELQDLARQLHARVDKVDEERYDIEAKVTKNITEIADLTQKIFDLRGKFKRPTLRRVRISADAMMQALLGARAKESLDLRAHLKQVKKEDTEKENREVGDWRKNIDALSGMEGRKKKFES"},{"start":1,"end":40,"reference_id":"32521240","reference_source":"pmid","reference_html":"Protein-Protein Docking Reveals Dynamic Interactions of Tropomyosin on Actin Filaments. <i> Pavadai E, Lehman W, Rynkiewicz MJ. </i> Biophys J, 2020","date":"2023-01-23T17:32:18.624Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7UTL"},{"db":"PDB","id":"7UTI"}],"region_id":"DP00166r009","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P68135"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P09493"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P45379-6"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63316 "}],"statement":[{"text":"The electron microscopy structure of the tropomyosin in human cardiac thin filament (both bounded and unbounded to calcium) show this region of the Troponin I protein lacks electron density, indicating it is disordered. ","type":"Curator statement"}]},{"start":167,"end":210,"reference_id":"32521240","reference_source":"pmid","reference_html":"Protein-Protein Docking Reveals Dynamic Interactions of Tropomyosin on Actin Filaments. <i> Pavadai E, Lehman W, Rynkiewicz MJ. </i> Biophys J, 2020","date":"2023-01-23T17:34:05.392Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7UTI"}],"region_id":"DP00166r010","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P68135"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P09493"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P45379-6"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63316 "}],"statement":[{"text":"The electron microscopy structure of the tropomyosin in human cardiac thin filament show this region of the Troponin I protein lacks electron density when bounded to calcium, indicating this region is disordered. ","type":"Curator statement"}]},{"start":167,"end":210,"reference_id":"32521240","reference_source":"pmid","reference_html":"Protein-Protein Docking Reveals Dynamic Interactions of Tropomyosin on Actin Filaments. <i> Pavadai E, Lehman W, Rynkiewicz MJ. </i> Biophys J, 2020","date":"2023-01-23T17:35:39.871Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7UTI"},{"db":"PDB","id":"7UTL"}],"region_id":"DP00166r011","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P68135"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P09493"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P45379-6"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63316 "}],"statement":[{"text":"The electron microscopy structure of the tropomyosin in human cardiac thin filament show this region of the Troponin I protein lacks electron density when bounded to calcium, indicating this region is disordered.","type":"Curator statement"}]}],"released":"2016_10","uniref100":"UniRef100_P19429","date":"2016-08-23T16:42:35.000Z","acc":"P19429","name":"Troponin I, cardiac muscle","length":210,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00001373A1","genes":[{"name":{"value":"TNNI3"},"synonyms":[{"value":"TNNC1"}]}],"alphafold_very_low_content":0.02857142857142857,"disorder_content":0.45714285714285713,"disprot_consensus":{"full":[{"start":1,"end":40,"type":"D"},{"start":137,"end":148,"type":"D"},{"start":167,"end":210,"type":"T"}],"Structural state":[{"start":1,"end":40,"type":"D"},{"start":137,"end":148,"type":"D"},{"start":167,"end":210,"type":"D"}],"Disorder function":[{"start":137,"end":148,"type":"F"}],"Structural transition":[{"start":167,"end":210,"type":"T"}]}},{"features":{"pfam":[{"id":"PF01243","name":"Pyridoxamine 5'-phosphate oxidase","start":75,"end":194},{"id":"PF10590","name":"Pyridoxine 5'-phosphate oxidase C-terminal dimerisation region","start":206,"end":261}],"gene3D":[{"start":49,"end":261,"id":"2.30.110.10","name":"Electron Transport, Fmn-binding Protein; Chain A"}]},"uniref50":"UniRef50_Q9NVS9","sequence":"MTCWLRGVTATFGRPAEWPGYLSHLCGRSAAMDLGPMRKSYRGDREAFEETHLTSLDPVKQFAAWFEEAVQCPDIGEANAMCLATCTRDGKPSARMLLLKGFGKDGFRFFTNFESRKGKELDSNPFASLVFYWEPLNRQVRVEGPVKKLPEEEAECYFHSRPKSSQIGAVVSHQSSVIPDREYLRKKNEELEQLYQDQEVPKPKSWGGYVLYPQVMEFWQGQTNRLHDRIVFRRGLPTGDSPLGPMTHRGEEDWLYERLAP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9NVS9","disprot_id":"DP00168","ncbi_taxon_id":9606,"regions_counter":3,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":48,"region_id":"DP00168r001","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Structure and properties of recombinant human pyridoxine 5'-phosphate oxidase. <i> Musayev FN, Di Salvo ML, Ko TP, Schirch V, Safo MK. </i> Protein Sci, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12824491","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-01-23T17:42:09.534Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1NRG"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17621","entry_name":"FMN"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"41218","entry_name":"mercaptoethanol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18405","entry_name":"pyridoxal 5'-phosphate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18367","entry_name":"phosphate(3-)"}],"statement":[{"text":" Like the E. coli (PDB code 1G79) and yeast PNPOx (PDB code IC10) structures, which are missing the first 19 and 23 N-terminal amino acid residues, the first 48 N-terminal amino acid residues of human PNPOx are also absent in the structure because of disorder.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_Q9NVS9","date":"2016-09-08T11:52:01.000Z","acc":"Q9NVS9","name":"Pyridoxine-5'-phosphate oxidase","length":261,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI000004A13F","genes":[{"name":{"value":"PNPO"}}],"alphafold_very_low_content":0.09961685823754789,"disorder_content":0.1839080459770115,"disprot_consensus":{"full":[{"start":1,"end":48,"type":"D"}],"Structural state":[{"start":1,"end":48,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00091","name":"Tubulin/FtsZ family, GTPase domain","start":3,"end":211},{"id":"PF03953","name":"Tubulin C-terminal domain","start":261,"end":382}],"gene3D":[{"start":374,"end":445,"id":"1.10.287.600","name":"Helix hairpin bin"},{"start":1,"end":263,"id":"3.40.50.1440","name":"Tubulin/FtsZ, GTPase domain"},{"start":264,"end":373,"id":"3.30.1330.20","name":"Tubulin/FtsZ, C-terminal domain"}]},"uniref50":"UniRef50_P32882","sequence":"MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEGEEDEA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Phasianinae","Gallus"],"uniref90":"UniRef90_P32882","disprot_id":"DP00169","ncbi_taxon_id":9031,"regions_counter":1,"creator":"dpiovesan","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":445,"region_id":"DP00169r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Helicity of alpha(404-451) and beta(394-445) tubulin C-terminal recombinant peptides. <i> Jimenez MA, Evangelio JA, Aranda C, Lopez-Brauet A, Andreu D, Rico M, Lagos R, Andreu JM, Monasterio O. </i> Protein Sci, 1999","term_id":"IDPO:0000002","curator_id":"esalladini","start":432,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"10211825","statement":[{"text":"Two-dimensional 1H-NMR parameters (nonsequential nuclear Overhauser effects (NOE) and conformational CaH shifts) in 30% TFE permitted to conclude that about 25% of a(404–451) and 40% of b(394–451) form well-defined helices encompassing residues 418–432 and 408–431, respectively, flanked by disordered N- and C-segments.","type":"Abstract"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P32882","date":"2016-09-06T12:00:10.000Z","acc":"P32882","name":"Tubulin beta-2 chain","length":445,"organism":"Gallus gallus","dataset":[],"UniParc":"UPI00001369D7","genes":[],"alphafold_very_low_content":0.017977528089887642,"disorder_content":0.03146067415730337,"disprot_consensus":{"full":[{"start":432,"end":445,"type":"D"}],"Structural state":[{"start":432,"end":445,"type":"D"}]}},{"acc":"P04049","sequence":"MEHIQGAWKTISNGFGFKDAVFDGSSCISPTIVQQFGYQRRASDDGKLTDPSKTSNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDWSNIRQLLLFPNSTIGDSGVPALPSLTMRRMRESVSRMPVSSQHRYSTPHAFTFNTSSPSSEGSLSQRQRSTSTPNVHMVSTTLPVDSRMIEDAIRSHSESASPSALSSSPNNLSPTGWSQPKTPVPAQRERAPVSGTQEKNKIRPRGQRDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYKNCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQHSLPKINRSASEPSLHRAAHTEDINACTLTTSPRLPVF","alphafold_very_low_content":"0.35030864197530864","creator":"grivas","dataset":["Cancer-related proteins","Autophagy-related proteins","NDDs-related proteins","Condensates-related proteins"],"date":"2016-08-25T12:26:54.000Z","disprot_id":"DP00171","features":{"pfam":[{"id":"PF00130","name":"Phorbol esters/diacylglycerol binding domain (C1 domain)","start":139,"end":185},{"id":"PF02196","name":"Raf-like Ras-binding domain","start":57,"end":130},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":351,"end":605}],"gene3D":[{"start":426,"end":618,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1","_id":"685af523b4ac24d5329d7b74"},{"start":56,"end":140,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1","_id":"685af523b4ac24d5329d7b75"},{"start":141,"end":187,"id":"3.30.60.20","name":"3.30.60.20","_id":"685af523b4ac24d5329d7b76"},{"start":340,"end":425,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1","_id":"685af523b4ac24d5329d7b77"}]},"genes":[{"name":{"value":"RAF1","evidences":[{"source":{"id":"HGNC:9829","name":"HGNC","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9829","_id":"685af523b4ac24d5329d7b97"},"code":"ECO:0000312","_id":"685af523b4ac24d5329d7b96"}],"_id":"685af523b4ac24d5329d7b98"},"synonyms":[{"value":"RAF","evidences":[],"_id":"685af523b4ac24d5329d7b99"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d7b95"}],"length":648,"name":"RAF proto-oncogene serine/threonine-protein kinase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":10,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000049CFC","uniref100":"UniRef100_P04049","uniref50":"UniRef50_P04049","uniref90":"UniRef90_P04049","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":233,"end":233,"statements":[],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d7b89"},{"start":256,"end":256,"statements":[],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d7b8a"}],"cross_refs":[{"db":"PDB","id":"4FJ3","_id":"685af523b4ac24d5329d7b88"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-02-06T20:48:24.046Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":236,"end":255,"interaction_partner":[],"reference_html":"Synergistic binding of the phosphorylated S233- and S259-binding sites of C-RAF to one 14-3-3ζ dimer. <i> Molzan M, Ottmann C. </i> J Mol Biol, 2012","reference_id":"22922483","region_id":"DP00171r006","released":"2023_06","sample":[{"db":"UniProt","deviation":null,"id":"P63104","statements":[],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7b8b"}],"sequence_construct":"QHRYSTPHAFTFNTSSPSSEGSLSQRQRSTSTPNVH","statement":[{"type":"Article","text":"The 20-amino‐acid stretch between pS233 and pS259 could not be traced, presumably due to its intrinsic disorder and lack of contacts to the 14-3-3ζ protein.","_id":"685af523b4ac24d5329d7b87"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-02-07T09:52:41.949Z","_id":"685af523b4ac24d5329d7b8c"},"version":4,"_id":"685af523b4ac24d5329d7b86","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":233,"end":233,"statements":[],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d7b90"},{"start":256,"end":256,"statements":[],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d7b91"}],"cross_refs":[{"db":"PDB","id":"4IHL","_id":"685af523b4ac24d5329d7b8e"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-14T19:08:47.097Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":238,"end":254,"interaction_partner":[],"reference_html":"Stabilization of physical RAF/14-3-3 interaction by cotylenin A as treatment strategy for RAS mutant cancers. <i> Molzan M, Kasper S, Röglin L, Skwarczynska M, Sassa T, Inoue T, Breitenbuecher F, Ohkanda J, Kato N, Schuler M, Ottmann C. </i> ACS Chem Biol, 2013","reference_id":"23808890","region_id":"DP00171r007","released":"2022_06","sample":[{"db":"UniProt","deviation":null,"id":"P63104","statements":[],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7b92"},{"db":"ChEBI","deviation":null,"entry_name":"potassium(1+)","id":"29103","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7b93"}],"sequence_construct":"QHRYSTPHAFTFNTSSPSSEGSLSQRQRSTSTPNVH","statement":[{"type":"Curator statement","text":"The missing electron density region from PDB:4IHL corresponds to the disordered stretch between pS233 and pS259 described in PMID:22922483","_id":"685af523b4ac24d5329d7b8f"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-02-07T09:52:43.114Z","_id":"685af523b4ac24d5329d7b94"},"version":3,"_id":"685af523b4ac24d5329d7b8d","reference_source":"pmid"}],"__v":0,"disorder_content":0.030864197530864196,"disprot_consensus":{"full":[{"start":236,"end":255,"type":"D"}],"Structural state":[{"start":236,"end":255,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02017","name":"CIDE-N domain","start":19,"end":94},{"id":"PF09033","name":"DNA Fragmentation factor 45kDa, C terminal domain","start":100,"end":264}],"gene3D":[{"start":222,"end":307,"id":"1.10.1490.10","name":"C-terminal domain of DFF45/ICAD (DFF-C domain)"},{"start":113,"end":193,"id":"1.10.1490.10","name":"C-terminal domain of DFF45/ICAD (DFF-C domain)"},{"start":1,"end":100,"id":"3.10.20.10","name":"3.10.20.10"}]},"uniref50":"UniRef50_O00273","sequence":"MEVTGDAGVPESGEIRTLKPCLLRRNYSREQHGVAASCLEDLRSKACDILAIDKSLTPVTLVLAEDGTIVDDDDYFLCLPSNTKFVALASNEKWAYNNSDGGTAWISQESFDVDETDSGAGLKWKNVARQLKEDLSSIILLSEEDLQMLVDAPCSDLAQELRQSCATVQRLQHTLQQVLDQREEVRQSKQLLQLYLQALEKEGSLLSKQEESKAAFGEEVDAVDTGISRETSSDVALASHILTALREKQAPELSLSSQDLELVTKEDPKALAVALNWDIKKTETVQEACERELALRLQQTQSLHSLRSISASKASPPGDLQNPKRARQDPT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O00273","disprot_id":"DP00173","ncbi_taxon_id":9606,"regions_counter":8,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":100,"region_id":"DP00173r001","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45. <i> Zhou P, Lugovskoy AA, McCarty JS, Li P, Wagner G. </i> Proc Natl Acad Sci U S A, 2001","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"11371636","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-01-24T14:48:34.553Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Because nonspecific aggregation can also lead to such an appearance of the HSQC spectra, we recorded a CD spectrum of DFF45 NTD (1), which showed a lack of secondary structure (Fig. ​2B) and confirmed that NTD of DFF45 is indeed disordered.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":100,"region_id":"DP00173r005","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45. <i> Zhou P, Lugovskoy AA, McCarty JS, Li P, Wagner G. </i> Proc Natl Acad Sci U S A, 2001","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"11371636","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-01-24T14:37:59.468Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"In contrast, the NTD of DFF45 exhibits a spectrum typical for a disordered protein (Fig. ​2C).","type":"Results"}]},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":100,"term_name":"disorder to order","start":12,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"11371636","version":3,"reference_html":"Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45. <i> Zhou P, Lugovskoy AA, McCarty JS, Li P, Wagner G. </i> Proc Natl Acad Sci U S A, 2001","date":"2023-01-24T14:48:09.347Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00173r007","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural transition","construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Because the complex of these two constructs had very low solubility and stability, we designed a chimera in which the highly soluble streptococcal protein G B1 domain (residue 1–56) was fused to the N terminus of DFF45 NTD (residue 12–100) as a solubility enhancement tag (22)."}]}],"cross_refs":[{"db":"PDB","id":"1IBX"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O76075"}],"statement":[{"text":"To reconcile these conflicting observations, we performed NMR titration of 15N-labeled DFF45 NTD with unlabeled DFF40. The 1:1 complex displays well dispersed HSQC spectra (Fig. 2D), suggesting that folding of DFF45 NTD is induced upon binding to DFF40.","type":"Results"}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":100,"term_name":"protein binding","start":12,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"11371636","version":4,"reference_html":"Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45. <i> Zhou P, Lugovskoy AA, McCarty JS, Li P, Wagner G. </i> Proc Natl Acad Sci U S A, 2001","date":"2023-01-24T14:47:44.248Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00173r008","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Because the complex of these two constructs had very low solubility and stability, we designed a chimera in which the highly soluble streptococcal protein G B1 domain (residue 1–56) was fused to the N terminus of DFF45 NTD (residue 12–100) as a solubility enhancement tag (22)."}]}],"cross_refs":[{"db":"PDB","id":"1IBX"}],"interaction_partner":[{"db":"UniProt","id":"O76075","operator":"and","partner_start":1,"partner_end":80}],"statement":[{"text":"To reconcile these conflicting observations, we performed NMR titration of 15N-labeled DFF45 NTD with unlabeled DFF40. The 1:1 complex displays well dispersed HSQC spectra (Fig. ​2D), suggesting that folding of DFF45 NTD is induced upon binding to DFF40.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_O00273","date":"2016-08-11T15:57:03.000Z","acc":"O00273","name":"DNA fragmentation factor subunit alpha","length":331,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00001291FA","genes":[{"name":{"value":"DFFA"},"synonyms":[{"value":"DFF1"},{"value":"DFF45"}],"orfNames":[{"value":"H13"}]}],"alphafold_very_low_content":0.1782477341389728,"disorder_content":0.3021148036253776,"disprot_consensus":{"full":[{"start":1,"end":11,"type":"D"},{"start":12,"end":100,"type":"T"}],"Structural state":[{"start":1,"end":100,"type":"D"}],"Structural transition":[{"start":12,"end":100,"type":"T"}],"Molecular function":[{"start":12,"end":100,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00505","name":"HMG (high mobility group) box","start":350,"end":418},{"id":"PF08347","name":"N-terminal CTNNB1 binding","start":5,"end":259},{"id":"PF27556","name":"Zinc finger protein 704 C-terminal domain","start":462,"end":489}],"gene3D":[{"start":1,"end":62,"id":"4.10.900.10","name":"TCF3-CBD (Catenin binding domain)"},{"start":348,"end":433,"id":"1.10.30.10","name":"High mobility group box domain"}]},"uniref50":"UniRef50_Q9NQB0","sequence":"MPQLNGGGGDDLGANDELISFKDEGEQEEKSSENSSAERDLADVKSSLVNESETNQNSSSDSEAERRPPPRSESFRDKSRESLEEAAKRQDGGLFKGPPYPGYPFIMIPDLTSPYLPNGSLSPTARTLHFQSGSTHYSAYKTIEHQIAVQYLQMKWPLLDVQAGSLQSRQALKDARSPSPAHIVSNKVPVVQHPHHVHPLTPLITYSNEHFTPGNPPPHLPADVDPKTGIPRPPHPPDISPYYPLSPGTVGQIPHPLGWLVPQQGQPVYPITTGGFRHPYPTALTVNASMSRFPPHMVPPHHTLHTTGIPHPAIVTPTVKQESSQSDVGSLHSSKHQDSKKEEEKKKPHIKKPLNAFMLYMKEMRAKVVAECTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKKRKRDKQPGETNEHSECFLNPCLSLPPITDLSAPKKCRARFGLDQQNNWCGPCRRKKKCVRYIQGEGSCLSPPSSDGSLLDSPPPSPNLLGSPPRDAKSQTEQTQPLSLSLKPDPLAHLSMMPPPPALLLAEATHKASALCPNGALDLPPAALQPAAPSSSIAQPSTSSLHSHSSLAGTQPQPLSLVTKSLE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9NQB0","disprot_id":"DP00175","ncbi_taxon_id":9606,"regions_counter":29,"creator":"ftonello","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":56,"region_id":"DP00175r001","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Thermodynamics of the high-affinity interaction of TCF4 with beta-catenin. <i> Knapp S, Zamai M, Volpi D, Nardese V, Avanzi N, Breton J, Plyte S, Flocco M, Marconi M, Isacchi A, Caiolfa VR. </i> J Mol Biol, 2001","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"11237626","version":4,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-01-24T13:30:28.117Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"TCF4 (1-53) as well as TCF4 (1-56; not shown) showed a strongly negative CD signal at 200 nM, indicative of random-coil structure. ","type":"Results"}]},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":50,"term_name":"disorder to order","start":40,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"11713476","version":3,"reference_html":"Structure of a human Tcf4-beta-catenin complex. <i> Poy F, Lepourcelet M, Shivdasani RA, Eck MJ. </i> Nat Struct Biol, 2001","date":"2023-01-24T13:58:48.580Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00175r009","ec_go":"EXP","disprot_namespace":"Structural transition","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly7Ser","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"1JPW"}],"curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P35222"}],"sequence_construct":"GSGGDDLGANDELISFKDEGEQEEKSSENSSAERDLADVKSSLVNESET","statement":[{"text":"The Tcf4 peptide (yellow) has two sites of interaction with the armadillo repeat region of β-catenin (blue): an 'extended region' composed of residues 13–25 (labeled N in yellow) and a more C-terminal helical region composed of residues 40–50 (labeled C in yellow). The intervening 14 residues are disordered, as are residues 8–12 at the N-terminus and 51–54 at the C-terminus.","type":"Figure"}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":50,"term_name":"beta-catenin binding","start":40,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"11713476","version":4,"reference_html":"Structure of a human Tcf4-beta-catenin complex. <i> Poy F, Lepourcelet M, Shivdasani RA, Eck MJ. </i> Nat Struct Biol, 2001","date":"2023-01-24T14:02:13.341Z","term_id":"GO:0008013","ec_id":"ECO:0006220","region_id":"DP00175r010","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a catenin beta subunit.\" [GOC:bf]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly7Ser","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"1JPW"}],"curator_orcid":"0000-0001-8399-7907","interaction_partner":[{"db":"UniProt","id":"P35222","operator":null,"partner_start":131,"partner_end":670}],"sequence_construct":"GSGGDDLGANDELISFKDEGEQEEKSSENSSAERDLADVKSSLVNESET","statement":[{"text":"The Tcf4 peptide (yellow) has two sites of interaction with the armadillo repeat region of β-catenin (blue): an 'extended region' composed of residues 13–25 (labeled N in yellow) and a more C-terminal helical region composed of residues 40–50 (labeled C in yellow). The intervening 14 residues are disordered, as are residues 8–12 at the N-terminus and 51–54 at the C-terminus.","type":"Figure"}]},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":25,"term_name":"disorder to order","start":13,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"11713476","version":3,"reference_html":"Structure of a human Tcf4-beta-catenin complex. <i> Poy F, Lepourcelet M, Shivdasani RA, Eck MJ. </i> Nat Struct Biol, 2001","date":"2023-01-24T13:57:38.570Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00175r014","ec_go":"EXP","disprot_namespace":"Structural transition","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly7Ser","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"1JPW"}],"curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P35222"}],"sequence_construct":"GSGGDDLGANDELISFKDEGEQEEKSSENSSAERDLADVKSSLVNESET","statement":[{"text":"The Tcf4 peptide (yellow) has two sites of interaction with the armadillo repeat region of β-catenin (blue): an 'extended region' composed of residues 13–25 (labeled N in yellow) and a more C-terminal helical region composed of residues 40–50 (labeled C in yellow). The intervening 14 residues are disordered, as are residues 8–12 at the N-terminus and 51–54 at the C-terminus.","type":"Figure"}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":25,"term_name":"beta-catenin binding","start":13,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"11713476","version":4,"reference_html":"Structure of a human Tcf4-beta-catenin complex. <i> Poy F, Lepourcelet M, Shivdasani RA, Eck MJ. </i> Nat Struct Biol, 2001","date":"2023-01-24T14:01:14.868Z","term_id":"GO:0008013","ec_id":"ECO:0006220","region_id":"DP00175r015","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a catenin beta subunit.\" [GOC:bf]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly7Ser","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"1JPW"}],"curator_orcid":"0000-0001-8399-7907","interaction_partner":[{"db":"UniProt","id":"P35222","operator":null,"partner_start":131,"partner_end":670}],"sequence_construct":"GSGGDDLGANDELISFKDEGEQEEKSSENSSAERDLADVKSSLVNESET","statement":[{"text":"The Tcf4 peptide (yellow) has two sites of interaction with the armadillo repeat region of β-catenin (blue): an 'extended region' composed of residues 13–25 (labeled N in yellow) and a more C-terminal helical region composed of residues 40–50 (labeled C in yellow). The intervening 14 residues are disordered, as are residues 8–12 at the N-terminus and 51–54 at the C-terminus.","type":"Figure"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":53,"region_id":"DP00175r016","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Thermodynamics of the high-affinity interaction of TCF4 with beta-catenin. <i> Knapp S, Zamai M, Volpi D, Nardese V, Avanzi N, Breton J, Plyte S, Flocco M, Marconi M, Isacchi A, Caiolfa VR. </i> J Mol Biol, 2001","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-01-24T13:46:10.669Z","reference_source":"pmid","term_name":"disorder","reference_id":"11237626","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"TCF4 (1-53) as well as TCF4 (1-56; not shown) showed a strongly negative CD signal at 200 nM, indicative of random-coil structure.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":130,"region_id":"DP00175r021","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Thermodynamics of the high-affinity interaction of TCF4 with beta-catenin. <i> Knapp S, Zamai M, Volpi D, Nardese V, Avanzi N, Breton J, Plyte S, Flocco M, Marconi M, Isacchi A, Caiolfa VR. </i> J Mol Biol, 2001","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-01-24T13:46:42.853Z","reference_source":"pmid","term_name":"disorder","reference_id":"11237626","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"A similar spectrum was observed for the elongated construct (TCF4 1-130; Figure 2). Therefore, the lack of defined secondary-structure formation is not a result of the short construct length.","type":"Results"}]},{"start":1,"end":53,"reference_id":"11237626","reference_source":"pmid","reference_html":"Thermodynamics of the high-affinity interaction of TCF4 with beta-catenin. <i> Knapp S, Zamai M, Volpi D, Nardese V, Avanzi N, Breton J, Plyte S, Flocco M, Marconi M, Isacchi A, Caiolfa VR. </i> J Mol Biol, 2001","date":"2023-01-24T13:33:58.184Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008013","term_name":"beta-catenin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P35222","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00175r026","statement":[{"text":"The observed binding curves revealed a tight and reversible binding of β-catenin to immobilized TCF4 with a dissociation constant (KD) of 8.4(±0.3) nM (KB=1.2×108 M−1; Figure 3).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a catenin beta subunit.\" [GOC:bf]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":53,"reference_id":"11237626","reference_source":"pmid","reference_html":"Thermodynamics of the high-affinity interaction of TCF4 with beta-catenin. <i> Knapp S, Zamai M, Volpi D, Nardese V, Avanzi N, Breton J, Plyte S, Flocco M, Marconi M, Isacchi A, Caiolfa VR. </i> J Mol Biol, 2001","date":"2023-01-24T13:37:55.318Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008013","term_name":"beta-catenin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006329","ec_ontology":"ECO","ec_name":"static fluorescence quenching evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P35222","operator":null,"partner_start":134,"partner_end":671}],"region_id":"DP00175r027","statement":[{"text":"Titration of TCF4 (1-53) into a solution of β-catenin resulted in the determination of a dissociation constant (KD) of 11.7(±0.3)nM at 25 °C (Table 1) which corresponds to a change in free energy of −10.8 kcal/mol.","type":"Results"},{"text":"The comparison of this dissociation constant with the one measured using full-length β-catenin indicates that the armadillo region is sufficient for the high-affinity interaction with TCF4 in solution.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a catenin beta subunit.\" [GOC:bf]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":53,"reference_id":"11237626","reference_source":"pmid","reference_html":"Thermodynamics of the high-affinity interaction of TCF4 with beta-catenin. <i> Knapp S, Zamai M, Volpi D, Nardese V, Avanzi N, Breton J, Plyte S, Flocco M, Marconi M, Isacchi A, Caiolfa VR. </i> J Mol Biol, 2001","date":"2023-01-24T13:41:03.573Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008013","term_name":"beta-catenin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P35222","operator":null,"partner_start":134,"partner_end":671}],"region_id":"DP00175r028","statement":[{"text":"The analysis revealed that the binding thermodynamics of TCF4 (1-53) and TCF4 (1-56) were indistinguishable within the error of the measurements. Furthermore, elongation of the construct length to 130 residues altered neither the binding constants nor the thermodynamic parameters.","type":"Results"},{"text":"Since comparable binding constants and thermodynamic parameters were obtained for the three constructs, it can be concluded that the first 53 amino acid residues of TCF4 are sufficient for high-affinity binding to β-catenin/armadillo.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a catenin beta subunit.\" [GOC:bf]","term_is_obsolete":false,"term_not_annotate":false},{"start":26,"end":39,"reference_id":"11713476","reference_source":"pmid","reference_html":"Structure of a human Tcf4-beta-catenin complex. <i> Poy F, Lepourcelet M, Shivdasani RA, Eck MJ. </i> Nat Struct Biol, 2001","date":"2023-01-24T13:53:43.825Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly7Ser","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"1JPW"}],"region_id":"DP00175r029","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P35222 "}],"sequence_construct":"GSGGDDLGANDELISFKDEGEQEEKSSENSSAERDLADVKSSLVNESET","statement":[{"text":"The Tcf4 peptide (yellow) has two sites of interaction with the armadillo repeat region of β-catenin (blue): an 'extended region' composed of residues 13–25 (labeled N in yellow) and a more C-terminal helical region composed of residues 40–50 (labeled C in yellow). The intervening 14 residues are disordered, as are residues 8–12 at the N-terminus and 51–54 at the C-terminus.","type":"Figure"}]}],"released":"2016_10","uniref100":"UniRef100_Q9NQB0","date":"2016-09-08T16:22:27.000Z","acc":"Q9NQB0","name":"Transcription factor 7-like 2","length":619,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI0000161083","genes":[{"name":{"value":"TCF7L2"},"synonyms":[{"value":"TCF4"}]}],"alphafold_very_low_content":0.6203554119547657,"disorder_content":0.210016155088853,"disprot_consensus":{"full":[{"start":1,"end":12,"type":"D"},{"start":13,"end":25,"type":"T"},{"start":26,"end":39,"type":"D"},{"start":40,"end":50,"type":"T"},{"start":51,"end":130,"type":"D"}],"Structural state":[{"start":1,"end":130,"type":"D"}],"Structural transition":[{"start":13,"end":25,"type":"T"},{"start":40,"end":50,"type":"T"}],"Molecular function":[{"start":1,"end":53,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00593","name":"TonB dependent receptor-like, beta-barrel","start":288,"end":688},{"id":"PF07715","name":"TonB-dependent Receptor Plug Domain","start":76,"end":174}],"gene3D":[{"start":183,"end":720,"id":"2.40.170.20","name":"TonB-dependent receptor, beta-barrel domain"},{"start":54,"end":182,"id":"2.170.130.10","name":"TonB-dependent receptor, plug domain"}]},"uniref50":"UniRef50_P42512","sequence":"MKTETKVIKGRQGIARNRHTPLCLGLLLALSPLAAAVADARKDGETELPDMVISGESTSATQPPGVTTLGKVPLKPRELPQSASVIDHERLEQQNLFSLDEAMQQATGVTVQPFQLLTTAYYVRGFKVDSFELDGVPALLGNTASSPQDMAIYERVEILRGSNGLLHGTGNPAATVNLVRKRPQREFAASTTLSAGRWDRYRAEVDVGGPLSASGNVRGRAVAAYEDRDYFYDVADQGTRLLYGVTEFDLSPDTLLTVGAQYQHIDSITNMAGVPMAKDGSNLGLSRDTYLDVDWDRFKWDTYRAFGSLEQQLGGGWKGKVSAEYQEADSRLRYAGSFGAIDPQTGDGGQLMGAAYKFKSIQRSLDANLNGPVRLFGLTHELLGGVTYAQGETRQDTARFLNLPNTPVNVYRWDPHGVPRPQIGQYTSPGTTTTTQKGLYALGRIKLAEPLTLVVGGRESWWDQDTPATRFKPGRQFTPYGGLIWDFARDWSWYVSYAEVYQPQADRQTWNSEPLSPVEGKTYETGIKGELADGRLNLSLAAFRIDLENNPQEDPDHPGPPNNPFYISGGKVRSQGFELEGTGYLTPYWSLSAGYTYTSTEYLKDSQNDSGTRYSTFTPRHLLRLWSNYDLPWQDRRWSVGGGLQAQSDYSVDYRGVSMRQGGYALVNMRLGYKIDEHWTAAVNVNNLFDRTYYQSLSNPNWNNRYGEPRSFNVSLRGAF","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Pseudomonadales","Pseudomonadaceae","Pseudomonas"],"uniref90":"UniRef90_P42512","disprot_id":"DP00176","ncbi_taxon_id":208964,"regions_counter":9,"creator":"dpiovesan","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":55,"region_id":"DP00176r001","released":"2023_06","ec_id":"ECO:0005670","reference_html":"Crystal structure at high resolution of ferric-pyochelin and its membrane receptor FptA from Pseudomonas aeruginosa. <i> Cobessi D, Celia H, Pattus F. </i> J Mol Biol, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":38,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"x-ray crystallography evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-01-24T15:10:47.361Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1XKW"}],"reference_id":"16139844","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":" No electron density is observed for the N-terminal part of the receptor (residues Asp38 to Gly55) and the first residues observed in the electron density have high B-factors (B-factor average from Glu56 to Ser59: 47.14 Å2).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":513,"region_id":"DP00176r008","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Crystal structure at high resolution of ferric-pyochelin and its membrane receptor FptA from Pseudomonas aeruginosa. <i> Cobessi D, Celia H, Pattus F. </i> J Mol Biol, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":504,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-01-24T15:10:20.082Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1XKW"}],"reference_id":"16139844","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"131762","entry_name":"dodecyldimethylamine N-oxide"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"23976","entry_name":"ethanediol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:7885058"}],"statement":[{"text":"The poor quality of the electron density from Gln504 to Glu513 prevented the rebuilding of loop L7. The analysis of electron density maps calculated in space group P1 before and after the density modification by solvent flattening and density averaging did not provide details for the disordered parts of the model observed at 2.0 Å resolution.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P42512","date":"2016-09-06T12:26:56.000Z","acc":"P42512","name":"Fe(3+)-pyochelin receptor","length":720,"organism":"Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)","dataset":[],"UniParc":"UPI000012ABC9","genes":[{"name":{"value":"fptA"},"olnNames":[{"value":"PA4221"}]}],"alphafold_very_low_content":0.08194444444444444,"disorder_content":0.03888888888888889,"disprot_consensus":{"full":[{"start":38,"end":55,"type":"D"},{"start":504,"end":513,"type":"D"}],"Structural state":[{"start":38,"end":55,"type":"D"},{"start":504,"end":513,"type":"D"}]}},{"acc":"Q9Y5B0","sequence":"MEVPAAGRVPAEGAPTAAVAEVRCPGPAPLRLLEWRVAAGAAVRIGSVLAVFEAAASAQSSGASQSRVASGGCVRPARPERRLRSERAGVVRELCAQPGQVVAPGAVLVRLEGCSHPVVMKGLCAECGQDLTQLQSKNGKQQVPLSTATVSMVHSVPELMVSSEQAEQLGREDQQRLHRNRKLVLMVDLDQTLIHTTEQHCQQMSNKGIFHFQLGRGEPMLHTRLRPHCKDFLEKIAKLYELHVFTFGSRLYAHTIAGFLDPEKKLFSHRILSRDECIDPFSKTGNLRNLFPCGDSMVCIIDDREDVWKFAPNLITVKKYVYFQGTGDMNAPPGSRESQTRKKVNHSRGTEVSEPSPPVRDPEGVTQAPGVEPSNGLEKPARELNGSEAATPRDSPRPGKPDERDIWPPAQAPTSSQELAGAPEPQGSCAQGGRVAPGQRPAQGATGTDLDFDLSSDSESSSESEGTKSSSSASDGESEGKRGRQKPKAAPEGAGALAQGSSLEPGRPAAPSLPGEAEPGAHAPDKEPELGGQEEGERDGLCGLGNGCADRKEAETESQNSELSGVTAGESLDQSMEEEEEEDTDEDDHLIYLEEILVRVHTDYYAKYDRYLNKEIEEAPDIRKIVPELKSKVLADVAIIFSGLHPTNFPIEKTREHYHATALGAKILTRLVLSPDAPDRATHLIAARAGTEKVLQAQECGHLHVVNPDWLWSCLERWDKVEEQLFPLRDDHTKAQRENSPAAFPDREGVPPTALFHPMPVLPKAQPGPEVRIYDSNTGKLIRTGARGPPAPSSSLPIRQEPSSFRAVPPPQPQMFGEELPDAQDGEQPGPSRRKRQPSMSETMPLYTLCKEDLESMDKEVDDILGEGSDDSDSEKRRPEEQEEEPQPRKPGTRRERTLGAPASSERSAAGGRGPRGHKRKLNEEDAASESSRESSNEDEGSSSEADEMAKALEAELNDLM","alphafold_very_low_content":"0.4599375650364204","creator":"achasapi","dataset":["NDDs-related proteins"],"date":"2016-08-24T19:15:17.000Z","disprot_id":"DP00177","features":{"pfam":[{"id":"PF00533","name":"BRCA1 C Terminus (BRCT) domain","start":660,"end":715},{"id":"PF03031","name":"NLI interacting factor-like phosphatase","start":184,"end":321},{"id":"PF09309","name":"FCP1, C-terminal","start":716,"end":961},{"id":"PF26077","name":"Fcp1 barrel-sandwich hybrid domain","start":19,"end":113}],"gene3D":[{"start":166,"end":352,"id":"3.40.50.1000","name":"HAD superfamily/HAD-like","_id":"685af523b4ac24d5329d7b9c"},{"start":633,"end":728,"id":"3.40.50.10190","name":"BRCT domain","_id":"685af523b4ac24d5329d7b9d"},{"start":19,"end":113,"id":"2.40.50.100","name":"2.40.50.100","_id":"685af523b4ac24d5329d7b9e"}]},"genes":[{"name":{"value":"CTDP1","evidences":[],"_id":"685af523b4ac24d5329d7bcb"},"synonyms":[{"value":"FCP1","evidences":[],"_id":"685af523b4ac24d5329d7bcc"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d7bca"}],"length":961,"name":"RNA polymerase II subunit A C-terminal domain phosphatase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":10,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000071F1B","uniref100":"UniRef100_Q9Y5B0","uniref50":"UniRef50_Q9Y5B0","uniref90":"UniRef90_Q9Y5B0","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1ONV","_id":"685af523b4ac24d5329d7ba2"},{"db":"BMRB","id":"5685","_id":"685af523b4ac24d5329d7ba3"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-06-13T16:22:53.015Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":879,"end":944,"interaction_partner":[],"reference_html":"NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1. <i> Nguyen BD, Abbott KL, Potempa K, Kobor MS, Archambault J, Greenblatt J, Legault P, Omichinski JG. </i> Proc Natl Acad Sci U S A, 2003","reference_id":"12732728","region_id":"DP00177r001","released":"2023_06","sample":[],"statement":[{"type":"Abstract","text":"Interestingly, the cterFCP protein is completely disordered in the unbound state, but forms an α-helix (H1'; E945–M961) in the complex.","_id":"685af523b4ac24d5329d7ba0"},{"type":"Results","text":"The free cterFCP protein is devoid of any stable structural element but adopts a 17-residue α-helix (H1') at its carboxyl terminus (E945-M961) on inter- action with cterRAP74 (Fig. 1A).","_id":"685af523b4ac24d5329d7ba1"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":5,"_id":"685af523b4ac24d5329d7b9f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"16296","_id":"685af523b4ac24d5329d7bb6"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":879,"end":961,"interaction_partner":[],"reference_html":"NMR assignment of the intrinsically disordered C-terminal region of Homo sapiens FCP1 in the unbound state. <i> Showalter SA. </i> Biomol NMR Assign, 2009","reference_id":"19888685","region_id":"DP00177r006","released":"2022_03","sample":[],"statement":[{"type":"Title","text":"NMR assignment of the intrinsically disordered C-terminal region of Homo sapiens FCP1 in the unbound state","_id":"685af523b4ac24d5329d7bb4"},{"type":"Abstract","text":"The acidic C-terminal region of FCP1 is disordered in the free state, but adopts an alpha-helical conformation upon binding to the heavy chain of TFIIF. Here we report (1)H, (13)C, and (15)N resonance assignments for the intrinsically disordered unbound form of human C-terminal FCP1 (residues 879-961).","_id":"685af523b4ac24d5329d7bb5"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-30T09:44:03.588Z","_id":"685af523b4ac24d5329d7bb7"},"version":3,"_id":"685af523b4ac24d5329d7bb3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1ONV","_id":"685af523b4ac24d5329d7bb9"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":945,"end":961,"interaction_partner":[],"reference_html":"NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1. <i> Nguyen BD, Abbott KL, Potempa K, Kobor MS, Archambault J, Greenblatt J, Legault P, Omichinski JG. </i> Proc Natl Acad Sci U S A, 2003","reference_id":"12732728","region_id":"DP00177r007","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Interestingly, the cterFCP protein is completely disordered in the unbound state, but forms an α-helix (H1'; E945–M961) in the complex.","_id":"685af523b4ac24d5329d7bba"},{"type":"Results","text":"The free cterFCP protein is devoid of any stable structural element but adopts a 17-residue α-helix (H1') at its carboxyl terminus (E945-M961) on interaction with cterRAP74 (Fig. 1A). These residues of cterFCP\nthat are involved in formation of the alpha-helix display significant\nchanges in amide 1 H and 15 N chemical shifts between the free\nstate and the complex. Chemical shift index (CSI) analysis of\nthe H-alpha , C-alpha , C-beta, and C' chemical shifts of cterFCP also supports\nthe presence of the H1' helix for residues E945–M961 in the\ncomplex, but not in the free form.","_id":"685af523b4ac24d5329d7bbb"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-30T09:46:34.410Z","_id":"685af523b4ac24d5329d7bbc"},"version":1,"_id":"685af523b4ac24d5329d7bb8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"5685","_id":"685af523b4ac24d5329d7bbe"},{"db":"PDB","id":"1ONV","_id":"685af523b4ac24d5329d7bbf"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":945,"end":961,"interaction_partner":[{"db":"UniProt","id":"P35269","partner_start":470,"partner_end":502,"_id":"685af523b4ac24d5329d7bc0"}],"reference_html":"NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1. <i> Nguyen BD, Abbott KL, Potempa K, Kobor MS, Archambault J, Greenblatt J, Legault P, Omichinski JG. </i> Proc Natl Acad Sci U S A, 2003","reference_id":"12732728","region_id":"DP00177r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The importance of the H1' helix for interaction with cterRAP74 is supported by numerous intermolecular NOEs between the H1' alpha-helix of\ncterFCP and cterRAP74","_id":"685af523b4ac24d5329d7bc1"},{"type":"Figure","text":"Those amino acids that show intermolecular NOEs are indicated by an asterisk below the residue.","_id":"685af523b4ac24d5329d7bc2"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-30T09:46:33.728Z","_id":"685af523b4ac24d5329d7bc3"},"version":1,"_id":"685af523b4ac24d5329d7bbd","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":944,"end":961,"interaction_partner":[],"reference_html":"The disordered C-terminus of the RNA polymerase II phosphatase FCP1 is partially helical in the unbound state. <i> Lawrence CW, Bonny A, Showalter SA. </i> Biochem Biophys Res Commun, 2011","reference_id":"21672523","region_id":"DP00177r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"We therefore chose to measure circular dichroism\nusing both the ctFCP1 construct from the NMR samples and a\nshorter synthetic peptide (comprising residues 944–961) in which\nthe fraction of helical residues should be enriched. The spectra for\nthe peptide and for ctFCP1 are shown black in Fig. 3A and B, respec-\ntively. While both are characteristic of CD spectra for IDPs, they\nalso feature a subtle minimum near 222 nm – the hallmark of an\nalpha-helix.","_id":"685af523b4ac24d5329d7bc5"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-06-13T16:22:58.065Z","_id":"685af523b4ac24d5329d7bc6"},"version":1,"_id":"685af523b4ac24d5329d7bc4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":950,"end":961,"interaction_partner":[],"reference_html":"The disordered C-terminus of the RNA polymerase II phosphatase FCP1 is partially helical in the unbound state. <i> Lawrence CW, Bonny A, Showalter SA. </i> Biochem Biophys Res Commun, 2011","reference_id":"21672523","region_id":"DP00177r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Consensus analysis of chemical shifts indicates strong enough secondary shifting to assign a helical conformation to residues 945–949, which are found in the\nN-terminal portion of the RAP74 binding helix. The analysis indicates that the remainder of ctFCP1 is in a disordered state, although there is significant tendency towards helical chemical shifts in many other residues composing the RAP74 binding interface as well.","_id":"685af523b4ac24d5329d7bc8"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-05-02T18:02:44.516Z","_id":"685af523b4ac24d5329d7bc9"},"version":1,"_id":"685af523b4ac24d5329d7bc7","reference_source":"pmid"}],"__v":0,"disorder_content":0.08636836628511967,"disprot_consensus":{"full":[{"start":879,"end":944,"type":"D"},{"start":945,"end":961,"type":"T"}],"Structural state":[{"start":879,"end":961,"type":"D"}],"Structural transition":[{"start":945,"end":961,"type":"T"}],"Molecular function":[{"start":945,"end":961,"type":"F"}]}},{"features":{"pfam":[{"id":"PF10466","name":"Saccharopepsin inhibitor I34","start":1,"end":68}]},"uniref50":"UniRef50_P01094","sequence":"MNTDQQKVSEIFQSSKEKLQGDAKVVSDAFKKMASQDKDGKTTDADESEKHNYQEQYNKLKGAGHKKE","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P01094","disprot_id":"DP00179","ncbi_taxon_id":559292,"regions_counter":30,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":68,"region_id":"DP00179r001","released":"2023_06","ec_id":"ECO:0006204","reference_html":"The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix. <i> Li M, Phylip LH, Lees WE, Winther JR, Dunn BM, Wlodawer A, Kay J, Gustchina A. </i> Nat Struct Biol, 2000","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10655612","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-01-24T16:12:03.171Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Circular dichroism (CD) measurements were also performed on the peptide (residues 2–34) and protein forms of the free inhibitor in solution. Inspection of both spectra (data not shown) gave no indication of the presence of any ordered structure, be it helical or extended. Instead, the spectra were compatible with random coil.","type":"Article"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":34,"region_id":"DP00179r004","released":"2023_06","ec_id":"ECO:0006204","reference_html":"The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix. <i> Li M, Phylip LH, Lees WE, Winther JR, Dunn BM, Wlodawer A, Kay J, Gustchina A. </i> Nat Struct Biol, 2000","term_id":"IDPO:0000002","curator_id":"vnugnes","start":2,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10655612","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-01-24T15:50:49.909Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Circular dichroism (CD) measurements were also performed on the peptide (residues 2–34) and protein forms of the free inhibitor in solution. Inspection of both spectra (data not shown) gave no indication of the presence of any ordered structure, be it helical or extended. Instead, the spectra were compatible with random coil.","type":"Article"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":68,"region_id":"DP00179r007","released":"2023_06","ec_id":"ECO:0006220","reference_html":"The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix. <i> Li M, Phylip LH, Lees WE, Winther JR, Dunn BM, Wlodawer A, Kay J, Gustchina A. </i> Nat Struct Biol, 2000","term_id":"IDPO:0000002","curator_id":"vnugnes","start":33,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10655612","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-01-24T16:10:20.609Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1DP5"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P07267"}],"statement":[{"text":"In the resulting structures (Fig. 1 ), residues 2–32 of IA3 become ordered and form a near-perfect amphipathic α-helix (Fig. 2). In contrast, the remaining 36 residues from the C-terminus of the inhibitor are unstructured.","type":"Article"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys31Met","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys32Met","start":null,"end":null,"position":null}]},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":32,"term_name":"disorder to order","start":2,"ec_name":"x-ray crystallography evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10655612","version":3,"reference_html":"The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix. <i> Li M, Phylip LH, Lees WE, Winther JR, Dunn BM, Wlodawer A, Kay J, Gustchina A. </i> Nat Struct Biol, 2000","date":"2023-03-21T18:59:37.747Z","term_id":"IDPO:0000011","ec_id":"ECO:0005670","region_id":"DP00179r012","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural transition","cross_refs":[{"db":"PDB","id":"1DPJ"},{"db":"PDB","id":"1DP5"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P07267"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"506227","entry_name":"N-acetyl-D-glucosamine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"In the resulting structures (Fig. 1 ), residues 2–32 of IA3 become ordered and form a near-perfect amphipathic α-helix (Fig. 2). In contrast, the remaining 36 residues from the C-terminus of the inhibitor are unstructured.","type":"Article"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys31Met","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys32Met","start":null,"end":null,"position":null}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":32,"term_name":"protein binding","start":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"10655612","version":4,"reference_html":"The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix. <i> Li M, Phylip LH, Lees WE, Winther JR, Dunn BM, Wlodawer A, Kay J, Gustchina A. </i> Nat Struct Biol, 2000","date":"2023-01-24T16:09:47.624Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00179r013","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys31Met","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys32Met","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"1DPJ"},{"db":"PDB","id":"1DP5"}],"interaction_partner":[{"db":"UniProt","id":"P07267","operator":"and","partner_start":null,"partner_end":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"506227","entry_name":"N-acetyl-D-glucosamine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"In the resulting structures (Fig. 1 ), residues 2–32 of IA3 become ordered and form a near-perfect amphipathic α-helix (Fig. 2). In contrast, the remaining 36 residues from the C-terminus of the inhibitor are unstructured.","type":"Article"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":68,"region_id":"DP00179r014","released":"2023_06","ec_id":"ECO:0006204","reference_html":"IA3, an aspartic proteinase inhibitor from Saccharomyces cerevisiae, is intrinsically unstructured in solution. <i> Green TB, Ganesh O, Perry K, Smith L, Phylip LH, Logan TM, Hagen SJ, Dunn BM, Edison AS. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15065849","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-01-24T15:25:22.035Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Although Figure 2B shows a slight inflection around 222 nm that may represent a very small amount of α-helix, the CD spectrum of IA3 is characteristic of an unfolded protein with a strong minimum peak at ∼200 nm for all of the above temperatures.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":68,"region_id":"DP00179r022","released":"2023_06","ec_id":"ECO:0006165","reference_html":"IA3, an aspartic proteinase inhibitor from Saccharomyces cerevisiae, is intrinsically unstructured in solution. <i> Green TB, Ganesh O, Perry K, Smith L, Phylip LH, Logan TM, Hagen SJ, Dunn BM, Edison AS. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15065849","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-01-24T15:27:43.267Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The 15N HSQC NMR spectrum of free IA3 in solution is characteristic of an unfolded protein (Figure 4A).","type":"Results"},{"text":"Therefore, we measured heteronuclear 1H−15N NOEs ( 18) on [15N]IA3 (Figure 5). As expected for an unfolded protein, all of the NOEs in IA3 are very small (<0.3) or negative, clearly indicating that the protein is disordered in solution.","type":"Results"}],"cross_refs":[{"db":"BMRB","id":"6078"}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":68,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"15065849","version":4,"reference_html":"IA3, an aspartic proteinase inhibitor from Saccharomyces cerevisiae, is intrinsically unstructured in solution. <i> Green TB, Ganesh O, Perry K, Smith L, Phylip LH, Logan TM, Hagen SJ, Dunn BM, Edison AS. </i> Biochemistry, 2004","date":"2023-01-24T15:36:27.184Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00179r025","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"statement":[{"text":"The 15N−1H HSQC spectrum of the IA3−YprA complex (Figure 4B) is largely different from the spectrum of free IA3 (Figure 4A).","type":"Results"},{"text":"YprA corresponds to the yeast aspartic protease A (yscA, NC_001148.4), absent in UniProt resource.","type":"Curator statement"}]},{"start":2,"end":34,"reference_id":"10655612","reference_source":"pmid","reference_html":"The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix. <i> Li M, Phylip LH, Lees WE, Winther JR, Dunn BM, Wlodawer A, Kay J, Gustchina A. </i> Nat Struct Biol, 2000","date":"2023-01-24T15:57:56.183Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0004866","term_name":"endopeptidase inhibitor activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001191","ec_ontology":"ECO","ec_name":"in vitro cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P07267","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00179r030","statement":[{"text":"The recombinant wild type protein inhibited yeast proteinase A effectively at pH 3.1 (Table 1), and its potency increased even further at higher pH values.","type":"Article"},{"text":". A synthetic peptide spanning residues 2–34 of IA3 also showed a potency comparable to that of the full-length protein inhibitor, as measured by Ki values (Table 1). This suggests that the initiator Met residue and residues 35–68 in the IA3 sequence19 are not important for inhibitory function. Peptides 2–15 and 16–34 did not inhibit the enzyme when added either alone or together.","type":"Article"},{"text":"Thus, a contiguous stretch of residues from 2–34 not only prevents cleavage of this peptide by proteinase A but also acts an effective inhibitor of the enzyme.","type":"Article"}],"term_comment":"","term_def":"\"Binds to and stops, prevents or reduces the activity of an endopeptidase, any enzyme that hydrolyzes nonterminal peptide bonds in polypeptides.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_P01094","date":"2016-09-14T17:47:18.000Z","acc":"P01094","name":"Protease A inhibitor 3","length":68,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000036C85","genes":[{"name":{"value":"PAI3"},"orfNames":[{"value":"YM8010.04C"}],"olnNames":[{"value":"YMR174C"}]}],"alphafold_very_low_content":0.07352941176470588,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":1,"type":"D"},{"start":2,"end":32,"type":"T"},{"start":33,"end":68,"type":"D"}],"Structural state":[{"start":1,"end":68,"type":"D"}],"Structural transition":[{"start":2,"end":32,"type":"T"}],"Molecular function":[{"start":1,"end":68,"type":"F"}]}},{"features":{"gene3D":[{"start":146,"end":222,"id":"3.30.44.10","name":"Smk Toxin, beta chain"},{"start":19,"end":81,"id":"4.10.420.10","name":"Smk Toxin, alpha chain"}],"pfam":[{"id":"PF21414","name":"Salt-mediated killer protoxin 1, beta subunit","start":131,"end":220},{"id":"PF21415","name":"SMK1 alpha subunit","start":20,"end":81}]},"uniref50":"UniRef50_P19972","sequence":"MRKETLIGLAFITANVIAWSLRWRMQKSTTIAAIAGCSGAATFGGLAGGIVGCIAAGILAILQGFEVNWHNGGGGDRSNPVKRSSDSFSIVNHNGEKVDSYAHLVPGKVGKVIIDNIELSAIRYANNHTSLGYHFTSDGSGPAARGEATTIWGVGADEAIDKGTPSKNDLQNMSADLAKNGFKGHQGVACSTVKDGNKDVYMIKFSLAGGSNDPGGSPCSDD","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Debaryomycetaceae","Millerozyma"],"uniref90":"UniRef90_P19972","disprot_id":"DP00180","dataset":["Unicellular toxins and antitoxins"],"ncbi_taxon_id":4920,"regions_counter":6,"creator":"agasparini","regions":[{"region_id":"DP00180r003","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T11:02:43.438Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":222,"term_id":"IDPO:0000002","start":146,"version":2,"statement":[{"text":"SMK toxin is a killer toxin produced by a halotolerant yeast, Pichia farinosa. It is a heterodimer consisting of α (63 aa) and β (77 aa) subunits, between which no disulfide bond exists. The two subunits interact tightly with each other below pH 5. However, the subunits dissociate under neutral conditions, resulting in the aggregation of the α subunit and the concomitant loss of killer activity. CD spectral measurements showed that the secondary structure of the SMK toxin changes drastically in the pH range 5.1–5.5 and that after the dissociation of the subunits, the soluble βsubunit alone cannot take any secondary structure.","type":"Abstract"},{"text":"After removing theαsubunit from the turbid solution at pH 7.0 by centrifugation, the soluble β subunit gives a CD spectrum which is identical with that of a peptide in the random coil (Figure 1). This result clearly indicates that the β subunit cannot take any secondary structure in the absence of the α subunit.","type":"Results"},{"text":"The α and β subunits consist of amino acid residues 19-81 and 146-222, as previously described in PMID:8300637","type":"Curator statement"}],"term_name":"disorder","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9089808","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006204","curator_id":"fquaglia","reference_html":"Circular dichroism analysis of the interaction between the alpha and beta subunits in a killer toxin produced by a halotolerant yeast, Pichia farinosa. <i> Suzuki C, Kashiwagi T, Tsuchiya F, Kunishima N, Morikawa K, Nikkuni S, Arata Y. </i> Protein Eng, 1997","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00180r004","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T11:03:05.771Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":222,"term_id":"IDPO:0000011","start":146,"version":2,"statement":[{"text":"SMK toxin is a killer toxin produced by a halotolerant yeast, Pichia farinosa. It is a heterodimer consisting of alpha (63 aa) and beta (77 aa) subunits, between which no disulfide bond exists. The two subunits interact tightly with each other below pH 5. However, the subunits dissociate under neutral conditions, resulting in the aggregation of the alpha subunit and the concomitant loss of killer activity. CD spectral measurements showed that the secondary structure of the SMK toxin changes drastically in the pH range 5.1-5.5 and that after the dissociation of the subunits, the soluble beta subunit alone cannot take any secondary structure. ","type":"Abstract"}],"term_name":"disorder to order","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9089808","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural transition","ec_id":"ECO:0006204","curator_id":"fquaglia","reference_html":"Circular dichroism analysis of the interaction between the alpha and beta subunits in a killer toxin produced by a halotolerant yeast, Pichia farinosa. <i> Suzuki C, Kashiwagi T, Tsuchiya F, Kunishima N, Morikawa K, Nikkuni S, Arata Y. </i> Protein Eng, 1997","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00180r005","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T13:11:15.109Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":222,"term_id":"GO:0005515","start":146,"version":3,"statement":[{"text":"The crystal structure of the SMK toxin indicates that about 60% of the surface of the β subunit comprises hydrophobic residues, that almost all of hydrophobic residues of the β subunit are involved with the interactions with the α subunit and that four pairs of acidic residues, i.e. Asp76(β4)–Asp213(L6),Asp161(L4)–Asp195(β4),Glu158(L4)–Asp222(L6)andAsp199(β5)–Asp222(L6), exist, in each of which the distance between the carboxyl groups is sufficiently short for the formation of hydrogen bonds (Figure 2).","type":"Results"}],"term_name":"protein binding","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"9089808","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006204","curator_id":"fquaglia","reference_html":"Circular dichroism analysis of the interaction between the alpha and beta subunits in a killer toxin produced by a halotolerant yeast, Pichia farinosa. <i> Suzuki C, Kashiwagi T, Tsuchiya F, Kunishima N, Morikawa K, Nikkuni S, Arata Y. </i> Protein Eng, 1997","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00180r006","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T10:59:55.956Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":222,"term_id":"GO:0097351","start":146,"version":3,"statement":[{"text":"In a previous paper (Suzuki and Nikkuni, 1994), we suggested that the inactivation of the SMK toxin at neutral pH is caused by the dissociation of the two subunits. The CD analyses described here clearly indicate that the structure of the SMK toxin changes under such conditions.","type":"Discussion"}],"term_name":"toxin sequestering activity","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"9089808","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006204","curator_id":"fquaglia","reference_html":"Circular dichroism analysis of the interaction between the alpha and beta subunits in a killer toxin produced by a halotolerant yeast, Pichia farinosa. <i> Suzuki C, Kashiwagi T, Tsuchiya F, Kunishima N, Morikawa K, Nikkuni S, Arata Y. </i> Protein Eng, 1997","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a toxic protein, disabling its function. There may be more than one antitoxin to a toxic protein. Instances of this activity are known only in prokaryotes, where the toxic protein may be a ribonuclease, a DNA gyrase, or other.\" [GOC:rs, PMID:19143615, PMID:19325885, PMID:21819231, PMID:22545240, PMID:24806488, Wikipedia:Toxin-antitoxin_system#Type_II]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P19972","date":"2016-08-25T15:51:08.000Z","acc":"P19972","name":"Salt-mediated killer protoxin 1","length":222,"organism":"Millerozyma farinosa","UniParc":"UPI000017CBCA","genes":[{"name":{"value":"SMK1"}}],"alphafold_very_low_content":0.12162162162162163,"disorder_content":0.34684684684684686,"disprot_consensus":{"full":[{"start":146,"end":222,"type":"T"}],"Structural state":[{"start":146,"end":222,"type":"D"}],"Structural transition":[{"start":146,"end":222,"type":"T"}],"Molecular function":[{"start":146,"end":222,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00623","name":"RNA polymerase Rpb1, domain 2","start":356,"end":521},{"id":"PF04983","name":"RNA polymerase Rpb1, domain 3","start":525,"end":691},{"id":"PF04990","name":"RNA polymerase Rpb1, domain 7","start":1164,"end":1299},{"id":"PF04992","name":"RNA polymerase Rpb1, domain 6","start":896,"end":1079},{"id":"PF04997","name":"RNA polymerase Rpb1, domain 1","start":16,"end":354},{"id":"PF04998","name":"RNA polymerase Rpb1, domain 5","start":830,"end":895},{"id":"PF04998","name":"RNA polymerase Rpb1, domain 5","start":1080,"end":1163},{"id":"PF04998","name":"RNA polymerase Rpb1, domain 5","start":1300,"end":1425},{"id":"PF05000","name":"RNA polymerase Rpb1, domain 4","start":718,"end":823},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1589,"end":1600},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1616,"end":1629},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1630,"end":1643},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1644,"end":1657},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1658,"end":1671},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1672,"end":1685},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1686,"end":1699},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1700,"end":1713},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1714,"end":1727},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1728,"end":1741},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1742,"end":1755},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1757,"end":1769},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1770,"end":1783},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1784,"end":1797},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1798,"end":1811},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1826,"end":1839},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1841,"end":1853},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1855,"end":1867},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1868,"end":1881},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1896,"end":1909},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1910,"end":1923},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1924,"end":1936},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1941,"end":1954}],"gene3D":[{"start":525,"end":686,"id":"1.10.274.100","name":"RNA polymerase Rpb1, domain 3"},{"start":1164,"end":1300,"id":"3.30.1360.140","name":"3.30.1360.140"},{"start":687,"end":832,"id":"1.10.132.30","name":"1.10.132.30"},{"start":269,"end":319,"id":"1.20.120.1280","name":"RNA polymerase II, clamp domain"},{"start":9,"end":122,"id":"1.20.120.1280","name":"RNA polymerase II, clamp domain"},{"start":1427,"end":1471,"id":"1.10.150.390","name":"1.10.150.390"},{"start":346,"end":516,"id":"2.40.40.20","name":"2.40.40.20"},{"start":389,"end":452,"id":"3.30.1490.180","name":"RNA polymerase ii"}]},"uniref50":"UniRef50_P24928","sequence":"MHGGGPPSGDSACPLRTIKRVQFGVLSPDELKRMSVTEGGIKYPETTEGGRPKLGGLMDPRQGVIERTGRCQTCAGNMTECPGHFGHIELAKPVFHVGFLVKTMKVLRCVCFFCSKLLVDSNNPKIKDILAKSKGQPKKRLTHVYDLCKGKNICEGGEEMDNKFGVEQPEGDEDLTKEKGHGGCGRYQPRIRRSGLELYAEWKHVNEDSQEKKILLSPERVHEIFKRISDEECFVLGMEPRYARPEWMIVTVLPVPPLSVRPAVVMQGSARNQDDLTHKLADIVKINNQLRRNEQNGAAAHVIAEDVKLLQFHVATMVDNELPGLPRAMQKSGRPLKSLKQRLKGKEGRVRGNLMGKRVDFSARTVITPDPNLSIDQVGVPRSIAANMTFAEIVTPFNIDRLQELVRRGNSQYPGAKYIIRDNGDRIDLRFHPKPSDLHLQTGYKVERHMCDGDIVIFNRQPTLHKMSMMGHRVRILPWSTFRLNLSVTTPYNADFDGDEMNLHLPQSLETRAEIQELAMVPRMIVTPQSNRPVMGIVQDTLTAVRKFTKRDVFLERGEVMNLLMFLSTWDGKVPQPAILKPRPLWTGKQIFSLIIPGHINCIRTHSTHPDDEDSGPYKHISPGDTKVVVENGELIMGILCKKSLGTSAGSLVHISYLEMGHDITRLFYSNIQTVINNWLLIEGHTIGIGDSIADSKTYQDIQNTIKKAKQDVIEVIEKAHNNELEPTPGNTLRQTFENQVNRILNDARDKTGSSAQKSLSEYNNFKSMVVSGAKGSKINISQVIAVVGQQNVEGKRIPFGFKHRTLPHFIKDDYGPESRGFVENSYLAGLTPTEFFFHAMGGREGLIDTAVKTAETGYIQRRLIKSMESVMVKYDATVRNSINQVVQLRYGEDGLAGESVEFQNLATLKPSNKAFEKKFRFDYTNERALRRTLQEDLVKDVLSNAHIQNELEREFERMREDREVLRVIFPTGDSKVVLPCNLLRMIWNAQKIFHINPRLPSDLHPIKVVEGVKELSKKLVIVNGDDPLSRQAQENATLLFNIHLRSTLCSRRMAEEFRLSGEAFDWLLGEIESKFNQAIAHPGEMVGALAAQSLGEPATQMTLNTFHYAGVSAKNVTLGVPRLKELINISKKPKTPSLTVFLLGQSARDAERAKDILCRLEHTTLRKVTANTAIYYDPNPQSTVVAEDQEWVNVYYEMPDFDVARISPWLLRVELDRKHMTDRKLTMEQIAEKINAGFGDDLNCIFNDDNAEKLVLRIRIMNSDENKMQEEEEVVDKMDDDVFLRCIESNMLTDMTLQGIEQISKVYMHLPQTDNKKKIIITEDGEFKALQEWILETDGVSLMRVLSEKDVDPVRTTSNDIVEIFTVLGIEAVRKALERELYHVISFDGSYVNYRHLALLCDTMTCRGHLMAITRHGVNRQDTGPLMKCSFEETVDVLMEAAAHGESDPMKGVSENIMLGQLAPAGTGCFDLLLDAEKCKYGMEIPTNIPGLGAAGPTGMFFGSAPSPMGGISPAMTPWNQGATPAYGAWSPSVGSGMTPGAAGFSPSAASDASGFSPGYSPAWSPTPGSPGSPGPSSPYIPSPGGAMSPSYSPTSPAYEPRSPGGYTPQSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPNYTPTSPSYSPTSPSYSPTSPNYTPTSPNYSPTSPSYSPTSPSYSPTSPSYSPSSPRYTPQSPTYTPSSPSYSPSSPSYSPTSPKYTPTSPSYSPSSPEYTPASPKYSPTSPKYSPTSPKYSPTSPTYSPTTPKYSPTSPTYSPTSPVYTPTSPKYSPTSPTYSPTSPKYSPTSPTYSPTSPKGSTYSPTSPGYSPTSPTYSLTSPAISPDDSDEEN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P24928","disprot_id":"DP00181","ncbi_taxon_id":10090,"regions_counter":1,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1959,"region_id":"DP00181r001","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Conformation of the RNA polymerase II C-terminal domain: circular dichroism of long and short fragments. <i> Bienkiewicz EA, Moon Woody A, Woody RW. </i> J Mol Biol, 2000","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1529,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10704311","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-01-24T16:43:08.689Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The CD spectrum in water resembles that of an essentially unordered peptide, with a strong negative band at 197 nm.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:25:23.913Z"}}],"released":"2016_10","uniref100":"UniRef100_P08775","date":"2016-09-08T10:47:54.000Z","acc":"P08775","name":"DNA-directed RNA polymerase II subunit RPB1","length":1970,"organism":"Mus musculus","dataset":["Condensates-related proteins"],"UniParc":"UPI000002783A","genes":[{"name":{"value":"Polr2a"},"synonyms":[{"value":"Rpii215"},{"value":"Rpo2-1"}]}],"alphafold_very_low_content":0.2512690355329949,"disorder_content":0.21878172588832487,"disprot_consensus":{"full":[{"start":1529,"end":1959,"type":"D"}],"Structural state":[{"start":1529,"end":1959,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00718","name":"Polyomavirus coat protein","start":27,"end":319}],"gene3D":[{"start":2,"end":344,"id":"2.60.175.10","name":"Capsid protein VP1,Polyomavirus"}]},"uniref50":"UniRef50_P03087","sequence":"MAPTKRKGSCPGAAPKKPKEPVQVPKLVIKGGIEVLGVKTGVDSFTEVECFLNPQMGNPDEHQKGLSKSLAAEKQFTDDSPDKEQLPCYSVARIPLPNINEDLTCGNILMWEAVTVKTEVIGVTAMLNLHSGTQKTHENGAGKPIQGSNFHFFAVGGEPLELQGVLANYRTKYPAQTVTPKNATVDSQQMNTDHKAVLDKDNAYPVECWVPDPSKNENTRYFGTYTGGENVPPVLHITNTATTVLLDEQGVGPLCKADSLYVSAVDICGLFTNTSGTQQWKGLPRYFKITLRKRSVKNPYPISFLLSDLINRRTQRVDGQPMIGMSSQVEEVRVYEDTEELPGDPDMIRYIDEFGQTTTRMQ","taxonomy":["Viruses","Monodnaviria","Shotokuvirae","Cossaviricota","Papovaviricetes","Sepolyvirales","Polyomaviridae","Betapolyomavirus"],"uniref90":"UniRef90_P03087","disprot_id":"DP00182","ncbi_taxon_id":1891767,"regions_counter":5,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":13,"region_id":"DP00182r001","reference_id":"8805523","start":1,"ec_id":"ECO:0006220","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"We note three regions in which the electron density is poorly defined. The first encompasses the N-terminal 13 amino acid residues, which are not visible at all. This part of the monomer is probably disordered, and it is not contained in our model.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"The structure of simian virus 40 refined at 3.1 A resolution. <i> Stehle T, Gamblin SJ, Yan Y, Harrison SC. </i> Structure, 1996","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","cross_refs":[{"db":"PDB","id":"1SVA"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":362,"region_id":"DP00182r003","reference_id":"8805523","start":344,"ec_id":"ECO:0006220","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The C-terminal 6 residues of VP1 monomers α and α″ and the C-terminal 18 residues of β are disordered and excluded from the model presented here.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"The structure of simian virus 40 refined at 3.1 A resolution. <i> Stehle T, Gamblin SJ, Yan Y, Harrison SC. </i> Structure, 1996","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","cross_refs":[{"db":"PDB","id":"1SVA"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":21,"region_id":"DP00182r004","released":"2022_03","ec_id":"ECO:0007689","reference_html":"Simian virus 40 Vp1 DNA-binding domain is functionally separable from the overlapping nuclear localization signal and is required for effective virion formation and full viability. <i> Li PP, Nakanishi A, Shum D, Sun PC, Salazar AM, Fernandez CF, Chan SW, Kasamatsu H. </i> J Virol, 2001","statement":[{"text":"A DNA-binding domain (DBD) was identified on simian virus 40 (SV40) major capsid protein Vp1, and the domain's function in the SV40 life cycle was examined. The N-terminal location of the DBD is consistent with the crystallographic structure of the virion in which the Vp1 N terminus is oriented toward the minichromosomal core and is disordered. [extracts from abstract and discussion]","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11462004","version":2,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1SVA"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":21,"term_name":"molecular adaptor activity","start":1,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","statement":[{"text":"Collective results support a role for Vp1 NLS2-DBD2 in the assembly of virion particles. The results also suggest that this determinant can function in the infection of new cells.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11462004","version":3,"reference_html":"Simian virus 40 Vp1 DNA-binding domain is functionally separable from the overlapping nuclear localization signal and is required for effective virion formation and full viability. <i> Li PP, Nakanishi A, Shum D, Sun PC, Salazar AM, Fernandez CF, Chan SW, Kasamatsu H. </i> J Virol, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0007689","region_id":"DP00182r005","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P03087","date":"2016-09-14T17:35:15.000Z","acc":"P03087","name":"Major capsid protein VP1","length":362,"organism":"Simian virus 40","dataset":["Viral proteins"],"UniParc":"UPI000183887D","genes":[],"disorder_content":0.11049723756906077,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"},{"start":344,"end":362,"type":"D"}],"Structural state":[{"start":1,"end":21,"type":"D"},{"start":344,"end":362,"type":"D"}],"Molecular function":[{"start":1,"end":21,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00104","name":"Ligand-binding domain of nuclear hormone receptor","start":228,"end":402},{"id":"PF00105","name":"Double treble clef zinc finger, C4 type","start":23,"end":91}],"gene3D":[{"start":123,"end":425,"id":"1.10.565.10","name":"Retinoid X Receptor"},{"start":16,"end":106,"id":"3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A"}]},"uniref50":"UniRef50_P11473","sequence":"MEAMAASTSLPDPGDFDRNVPRICGVCGDRATGFHFNAMTCEGCKGFFRRSMKRKALFTCPFNGDCRITKDNRRHCQACRLKRCVDIGMMKEFILTDEEVQRKREMILKRKEEEALKDSLRPKLSEEQQRIIAILLDAHHKTYDPTYSDFCQFRPPVRVNDGGGSHPSRPNSRHTPSFSGDSSSSCSDHCITSSDMMDSSSFSNLDLSEEDSDDPSVTLELSQLSMLPHLADLVSYSIQKVIGFAKMIPGFRDLTSEDQIVLLKSSAIEVIMLRSNESFTMDDMSWTCGNQDYKYRVSDVTKAGHSLELIEPLIKFQVGLKKLNLHEEEHVLLMAICIVSPDRPGVQDAALIEAIQDRLSNTLQTYIRCRHPPPGSHLLYAKMIQKLADLRSLNEEHSKQYRCLSFQPECSMKLTPLVLEVFGNEIS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P11473","disprot_id":"DP00184","ncbi_taxon_id":9606,"regions_counter":7,"creator":"gminervini","regions":[{"start":165,"end":215,"reference_id":"11179963","reference_source":"pmid","reference_html":"Functional and structural characterization of the insertion region in the ligand binding domain of the vitamin D nuclear receptor. <i> Rochel N, Tocchini-Valentini G, Egea PF, Juntunen K, Garnier JM, Vihko P, Moras D. </i> Eur J Biochem, 2001","date":"2023-01-24T17:04:05.526Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00184r007","statement":[{"text":"The radii of gyration (Table 1) of VDRwt and VDRmt complexed to 1,25(OH)2D3 are 26.2 and 23.4 Å, respectively. The difference of 2.8 Å observed between the radii of gyration of the two proteins corresponds to an increase in volume of 35% for a spherical object. A similar difference (2.2 Å) has been observed by small angle neutron scattering (data not shown) between VDRwt and VDRmt. This difference is rather large and suggests a disordered insertion domain.","type":"Results"},{"text":"The difference of 15 Å between the Dmax values of VDRmt and VDRwt is rather large for an additional domain of 50 residues, suggesting that this insertion domain is not well ordered and may adopt several conformations in solution.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P11473","date":"2016-08-24T16:20:41.000Z","acc":"P11473","name":"Vitamin D3 receptor","length":427,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI000003C12F","genes":[{"name":{"value":"VDR"},"synonyms":[{"value":"NR1I1"}]}],"alphafold_very_low_content":0.1686182669789227,"disorder_content":0.11943793911007025,"disprot_consensus":{"full":[{"start":165,"end":215,"type":"D"}],"Structural state":[{"start":165,"end":215,"type":"D"}]}},{"features":{"pfam":[],"gene3D":[{"start":12,"end":142,"id":"1.20.120.20","name":"Apolipoprotein"}]},"uniref50":"UniRef50_Q95V77","sequence":"MSSQQNQNRQGEQQEQGYMEAAKEKVVNAWESTKETLSSTAQAAAEKTAEFRDSAGETIRDLTGQAQEKGQEFKERAGEKAEETKQRAGEKMDETKQRAGEMRENAGQKMEEYKQQGKGKAEELRDTAAEKLHQAGEKVKGRD","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Tylenchina","Tylenchomorpha","Aphelenchoidea","Aphelenchidae","Aphelenchus"],"uniref90":"UniRef90_Q95V77","disprot_id":"DP00186","ncbi_taxon_id":70226,"regions_counter":7,"creator":"ftonello","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":143,"region_id":"DP00186r001","released":"2023_06","ec_id":"ECO:0006228","reference_html":"Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein. <i> Goyal K, Tisi L, Basran A, Browne J, Burnell A, Zurdo J, Tunnacliffe A. </i> J Biol Chem, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12569097","version":3,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","date":"2023-01-24T17:21:09.730Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"FT-IR spectra collected from soluble AavLEA1 samples in 2H2O show an amide I pattern indicative of a mainly disordered polypeptide (Fig. 7A), in agreement with CD data. Second derivative analysis of the amide I band showed two main peaks at 1644 cm−1 and 1667 cm−1, characteristic of random coil structures (42).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":143,"region_id":"DP00186r003","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein. <i> Goyal K, Tisi L, Basran A, Browne J, Burnell A, Zurdo J, Tunnacliffe A. </i> J Biol Chem, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12569097","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-01-24T17:15:12.348Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"However, significant defined secondary structure was not detected for AavLEA1; signatures of α-helix and β-sheet were absent, with the spectrum showing instead that the protein is most likely unstructured through a temperature range of 4 to 75 °C (Fig.5).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":143,"region_id":"DP00186r005","released":"2023_06","ec_id":"ECO:0001249","reference_html":"Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein. <i> Goyal K, Tisi L, Basran A, Browne J, Burnell A, Zurdo J, Tunnacliffe A. </i> J Biol Chem, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12569097","version":3,"ec_name":"fluorescence evidence used in manual assertion","date":"2023-01-24T17:18:13.730Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The single tryptophan residue in AavLEA1, at position 49 of 162 (allowing for the His tag, position 30 of 143 in the native nematode sequence; Fig. 1), gives rise to a λmax at 4 °C of 355 nm, which is indicative of a solvent-exposed side chain (Fig. 6).","type":"Results"}]},{"start":1,"end":143,"reference_id":"12569097","reference_source":"pmid","reference_html":"Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein. <i> Goyal K, Tisi L, Basran A, Browne J, Burnell A, Zurdo J, Tunnacliffe A. </i> J Biol Chem, 2003","date":"2023-01-24T17:14:07.268Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00186r007","statement":[{"text":"The Stokes' radius (Rs sed) of AavLEA1 was calculated from sedimentation analysis to be 3.91 nm. This is larger than expected if AavLEA1 were globular in structure but is consistent with it being an extended or highly swollen protein.","type":"Results"},{"text":"The gel filtration column was calibrated using globular proteins with known Rsas standards, allowing Rs gel for AavLEA1 to be estimated at 3.38 nm. This is somewhat lower than the value obtained from ultracentrifugation, possibly because of matrix interaction effects, but is still far in excess of the expectedRs value for a globular protein of similar mass and supports the model of AavLEA1 having low compactness. ","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_Q95V77","date":"2016-09-08T16:32:51.000Z","acc":"Q95V77","name":"Late embryogenesis abundant protein 1","length":143,"organism":"Aphelenchus avenae","dataset":[],"UniParc":"UPI000012E395","genes":[],"alphafold_very_low_content":0.5104895104895105,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":143,"type":"D"}],"Structural state":[{"start":1,"end":143,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00377","name":"Prion/Doppel alpha-helical domain","start":134,"end":252},{"id":"PF03991","name":"Copper binding octapeptide repeat region","start":50,"end":95},{"id":"PF11587","name":"Major prion protein bPrPp - N terminal","start":1,"end":28}],"gene3D":[{"start":90,"end":231,"id":"1.10.790.10","name":"Prion/Doppel protein, beta-ribbon domain"}]},"uniref50":"UniRef50_P04156","sequence":"MANLSYWLLALFVAMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGNDWEDRYYRENMNRYPNQVYYRPVDQYNNQNNFVHDCVNITIKQHTVTTTTKGENFTETDIKIMERVVEQMCTTQYQKESQAYYDGRRSSAVLFSSPPVILLISFLIFLMVG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Cricetidae","Cricetinae","Mesocricetus"],"uniref90":"UniRef90_P04156","disprot_id":"DP00187","ncbi_taxon_id":10036,"regions_counter":17,"creator":"agasparini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":106,"region_id":"DP00187r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of the flexible amino-terminal domain of prion protein bound to a sulfated glycan. <i> Taubner LM, Bienkiewicz EA, Copié V, Caughey B. </i> J Mol Biol, 2010","term_id":"IDPO:0000002","curator_id":"esalladini","start":23,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"19913031","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2KKG"}],"term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"Two dimensional 1H/15N correlation (HSQC) 50 NMR spectra collected on hamster PrP 23–106 both with and without PPS exhibited limited chemical shift dispersion (~ 1 ppm), consistent with extensive conformational averaging and a lack of well defined, compact structure (Figure 1).","type":"Results"},{"text":"The majority of chemical shifts of backbone and sidechain atoms were close to random coil values, consistent with the disordered nature of PrP 23–106 58.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-17T20:02:31.889Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":126,"region_id":"DP00187r004","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. <i> James TL, Liu H, Ulyanov NB, Farr-Jones S, Zhang H, Donne DG, Kaneko K, Groth D, Mehlhorn I, Prusiner SB, Cohen FE. </i> Proc Natl Acad Sci U S A, 1997","term_id":"IDPO:0000002","curator_id":"vnugnes","start":90,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"9294167","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-08-17T19:57:10.891Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1B10"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Essentially three parts to the protein are readily reflected in simple NMR spectral features: residues 90–112 are characterized by narrow (18 Hz) 15N heteronuclear single quantum coherence (HSQC) spectral signals and few long-range NOE crosspeaks; residues 113–126 have relatively narrow (ca. 18 Hz) 15N HSQC spectral (ca. 18Hz) signals and many NOE crosspeaks; and most of the remaining residues exhibit ca. 6 Hz broader HSQC signals and numerous NOE crosspeaks.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":122,"region_id":"DP00187r007","released":"2022_12","ec_id":"ECO:0006220","reference_html":"X-ray structural and molecular dynamical studies of the globular domains of cow, deer, elk and Syrian hamster prion proteins. <i> Baral PK, Swayampakula M, Aguzzi A, James MN. </i> J Struct Biol, 2015","term_id":"IDPO:0000002","curator_id":"vnugnes","start":90,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"26320075","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-08-17T19:45:51.234Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4YXL"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ABCD","id":"ABCD_AG808"}],"statement":[{"text":"The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]},{"start":23,"end":106,"reference_id":"19913031","reference_source":"pmid","reference_html":"Structure of the flexible amino-terminal domain of prion protein bound to a sulfated glycan. <i> Taubner LM, Bienkiewicz EA, Copié V, Caughey B. </i> J Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00187r013","statement":[{"text":"The fluorescence spectrum of PrP 23–106 exhibited a maximum around 356 nm indicating that the aromatic residues are exposed to the aqueous solvent (Figure 5(a)).","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-17T20:01:10.263Z"}},{"start":23,"end":106,"reference_id":"19913031","reference_source":"pmid","reference_html":"Structure of the flexible amino-terminal domain of prion protein bound to a sulfated glycan. <i> Taubner LM, Bienkiewicz EA, Copié V, Caughey B. </i> J Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00187r014","statement":[{"text":"An isodichroic point at ~206–208 nm indicated a β-turn/PPII conformational transition 67, 68, consistent with the β-turn conformation detected by NMR without PPS (described above) and earlier studies of N-terminal PrP fragments, in which PPII and β-turn conformations were recognized 40–43.","type":"Results"},{"text":"The pentosan polysulfate (PPS) is one of the most potent anti-prion.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-17T20:04:10.451Z"}},{"start":23,"end":106,"reference_id":"19913031","reference_source":"pmid","reference_html":"Structure of the flexible amino-terminal domain of prion protein bound to a sulfated glycan. <i> Taubner LM, Bienkiewicz EA, Copié V, Caughey B. </i> J Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00187r015","statement":[{"text":"An isodichroic point at ~206–208 nm indicated a β-turn/PPII conformational transition 67, 68, consistent with the β-turn conformation detected by NMR without PPS (described above) and earlier studies of N-terminal PrP fragments, in which PPII and β-turn conformations were recognized 40–43.","type":"Results"},{"text":"The pentosan polysulfate (PPS) is one of the most potent anti-prion.","type":"Curator statement"},{"text":"These findings indicated that addition of PPS to PrP 23–106 enhanced the latter’s β-turn component, again consistent with NMR data.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-17T20:04:57.420Z"}},{"start":23,"end":106,"reference_id":"19913031","reference_source":"pmid","reference_html":"Structure of the flexible amino-terminal domain of prion protein bound to a sulfated glycan. <i> Taubner LM, Bienkiewicz EA, Copié V, Caughey B. </i> J Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00187r016","statement":[{"text":"In contrast, NMR spectra recorded on free PrP 23–106 (i.e. no PPS) but otherwise under identical sample conditions (i.e. buffer/20% DMSO) revealed large differences with NMR spectra acquired on the PrP 23–106/PPS complex.","type":"Results"},{"text":"The pentosan polysulfate (PPS) is one of the most potent anti-prion.","type":"Curator statement"},{"text":"The 3D 15N-edited 1H-1H NOESY spectrum acquired on PrP 23–106 without PPS exhibited far fewer NOE cross-peaks for the octarepeat residues.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-17T20:04:40.330Z"}},{"start":23,"end":106,"reference_id":"19913031","reference_source":"pmid","reference_html":"Structure of the flexible amino-terminal domain of prion protein bound to a sulfated glycan. <i> Taubner LM, Bienkiewicz EA, Copié V, Caughey B. </i> J Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00187r017","statement":[{"text":"In contrast, NMR spectra recorded on free PrP 23–106 (i.e. no PPS) but otherwise under identical sample conditions (i.e. buffer/20% DMSO) revealed large differences with NMR spectra acquired on the PrP 23–106/PPS complex.","type":"Results"},{"text":"The pentosan polysulfate (PPS) is one of the most potent anti-prion.","type":"Curator statement"},{"text":"The 3D 15N-edited 1H-1H NOESY spectrum acquired on PrP 23–106 without PPS exhibited far fewer NOE cross-peaks for the octarepeat residues.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-17T20:03:17.785Z"}}],"released":"2016_10","uniref100":"UniRef100_P04273","date":"2016-08-25T16:39:39.000Z","acc":"P04273","name":"Major prion protein","length":254,"organism":"Mesocricetus auratus","dataset":["Condensates-related proteins"],"UniParc":"UPI0000033C29","genes":[{"name":{"value":"PRNP"},"synonyms":[{"value":"PRP"}]}],"alphafold_very_low_content":0.4094488188976378,"disorder_content":0.4094488188976378,"disprot_consensus":{"full":[{"start":23,"end":106,"type":"T"},{"start":107,"end":126,"type":"D"}],"Structural state":[{"start":23,"end":126,"type":"D"}],"Structural transition":[{"start":23,"end":106,"type":"T"}],"Biological process":[{"start":23,"end":106,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01716","name":"Manganese-stabilising protein / photosystem II polypeptide","start":97,"end":329}],"gene3D":[{"start":129,"end":330,"id":"2.40.160.30","name":"Photosystem II, cytochrome c-550 precursor"},{"start":236,"end":274,"id":"3.30.2050.10","name":"photosynthetic oxygen evolving center domain"}]},"uniref50":"UniRef50_P12359","sequence":"MAASLQASTTFLQPTKVASRNTLQLRSTQNVCKAFGVESASSGGRLSLSLQSDLKELANKCVDATKLAGLALATSALIASGANAEGGKRLTYDEIQSKTYLEVKGTGTANQCPTVEGGVDSFAFKPGKYTAKKFCLEPTKFAVKAEGISKNSGPDFQNTKLMTRLTYTLDEIEGPFEVSSDGTVKFEEKDGIDYAAVTVQLPGGERVPFLFTIKQLVASGKPESFSGDFLVPSYRGSSFLDPKGRGGSTGYDNAVALPAGGRGDEEELQKENNKNVASSKGTITLSVTSSKPETGEVIGVFQSLQPSDTDLGAKVPKDVKIEGVWYAQLEQQ","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","Caryophyllales","Chenopodiaceae","Chenopodioideae","Anserineae","Spinacia"],"uniref90":"UniRef90_P12359","disprot_id":"DP00188","ncbi_taxon_id":3562,"regions_counter":5,"creator":"mnecci","regions":[{"start":1,"end":88,"reference_id":"27251276","reference_source":"pmid","reference_html":"Structure of spinach photosystem II-LHCII supercomplex at 3.2 Å resolution. <i> Wei X, Su X, Cao P, Liu X, Chang W, Li M, Zhang X, Liu Z. </i> Nature, 2016","date":"2023-02-09T13:14:23.981Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"EMDB","id":"6617"},{"db":"PDB","id":"3JCU"}],"region_id":"DP00188r005","statement":[{"text":"The cryo-EM structure of spinach PSII-LHCII supercomplex, shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"released":"2016_10","uniref100":"UniRef100_P12359","date":"2016-08-24T19:42:45.000Z","acc":"P12359","name":"Oxygen-evolving enhancer protein 1, chloroplastic","length":332,"organism":"Spinacia oleracea","dataset":[],"UniParc":"UPI0000132723","genes":[{"name":{"value":"PSBO"}}],"alphafold_very_low_content":0.24397590361445784,"disorder_content":0.26506024096385544,"disprot_consensus":{"full":[{"start":1,"end":88,"type":"D"}],"Structural state":[{"start":1,"end":88,"type":"D"}]}},{"acc":"P04324","sequence":"MGGKWSKSSVVGWPAVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAANNAACAWLEAQEEEKVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGIRYPLTFGWCYKLVPVEPEKLEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC","creator":"jbergier","dataset":["Viral proteins"],"date":"2016-08-25T16:26:52.000Z","disprot_id":"DP00189","features":{"pfam":[{"id":"PF00469","name":"Negative factor, (F-Protein) or Nef","start":2,"end":205}],"gene3D":[{"start":2,"end":57,"id":"4.10.890.10","name":"HIV 1 nef anchor domain","_id":"685af523b4ac24d5329d7bce"},{"start":58,"end":206,"id":"3.30.62.10","name":"Nef Regulatory Factor","_id":"685af523b4ac24d5329d7bcf"}]},"genes":[{"name":{"value":"nef","evidences":[{"source":{"id":"MF_04078","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04078","_id":"685af523b4ac24d5329d7c01"},"code":"ECO:0000255","_id":"685af523b4ac24d5329d7c00"}],"_id":"685af523b4ac24d5329d7c02"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d7bff"}],"length":206,"name":"Protein Nef","ncbi_taxon_id":11679,"organism":"Human immunodeficiency virus type 1 group M subtype B (isolate PCV12)","regions_counter":10,"released":"2016_10","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"UniParc":"UPI000012FEF9","uniref100":"UniRef100_P04324","uniref50":"UniRef50_P03406","uniref90":"UniRef90_P04601","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1QA5","_id":"685af523b4ac24d5329d7bd8"},{"db":"PDB","id":"1QA4","_id":"685af523b4ac24d5329d7bd9"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":42,"end":57,"interaction_partner":[],"reference_html":"Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein. <i> Geyer M, Munte CE, Schorr J, Kellner R, Kalbitzer HR. </i> J Mol Biol, 1999","reference_id":"10339411","region_id":"DP00189r003","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"Here, we investigate the solution structures of the myristoylated and non-myristoylated HIV-1 Nef anchor domain (2–57) under buffer conditions as close to physiological conditions as possible.","_id":"685af523b4ac24d5329d7bda"},{"type":"Results","text":"The structure of the domain was studied under nearly physiological conditions in aqueous solution; the experimental data show that the isolated domain is not compactly folded and does not have a unique structure. The only canonic secondary structure element found in the non-myristyolated anchor domain is a short α-helical element (helix H2) from Arg35 to Gly41 (Figure 4).","_id":"685af523b4ac24d5329d7bdb"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-06T08:37:48.944Z","_id":"685af523b4ac24d5329d7bdc"},"version":3,"_id":"685af523b4ac24d5329d7bd7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1QA5","_id":"685af523b4ac24d5329d7be8"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":14,"interaction_partner":[],"reference_html":"Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein. <i> Geyer M, Munte CE, Schorr J, Kellner R, Kalbitzer HR. </i> J Mol Biol, 1999","reference_id":"10339411","region_id":"DP00189r007","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"Here, we investigate the solution structures of the myristoylated and non-myristoylated HIV-1 Nef anchor domain (2–57) under buffer conditions as close to physiological conditions as possible.","_id":"685af523b4ac24d5329d7be9"},{"type":"Results","text":"Myristoylation induces a change of the conformational states of the anchor domain, leading to the stabilization of helix H2 and to the induction of the first helical element H1 (Pro14 to Arg22).","_id":"685af523b4ac24d5329d7bea"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-06T08:37:50.250Z","_id":"685af523b4ac24d5329d7beb"},"version":1,"_id":"685af523b4ac24d5329d7be7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1QA4","_id":"685af523b4ac24d5329d7bed"},{"db":"PDB","id":"1QA5","_id":"685af523b4ac24d5329d7bee"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":34,"interaction_partner":[],"reference_html":"Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein. <i> Geyer M, Munte CE, Schorr J, Kellner R, Kalbitzer HR. </i> J Mol Biol, 1999","reference_id":"10339411","region_id":"DP00189r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The structure of the domain was studied under nearly physiological conditions in aqueous solution; the experimental data show that the isolated domain is not compactly folded and does not have a unique structure. The only canonic secondary structure element found in the non-myristyolated anchor domain is a short α-helical element (helix H2) from Arg35 to Gly41 (Figure 4). ","_id":"685af523b4ac24d5329d7bef"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-06T08:37:51.759Z","_id":"685af523b4ac24d5329d7bf0"},"version":1,"_id":"685af523b4ac24d5329d7bec","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":2,"end":2,"statements":[{"type":"Results","text":"The myristic moiety at Gly2 itself covers the large hydrophobic ring system of Trp5, thereby forming a loop with Gly2, Gly3 and Lys4 in the kink region and exposing the side-chain of the succeeding residue Ser6 to the solvent (Figure 7). ","_id":"685af523b4ac24d5329d7bf7"}],"term_id":"MOD:00068","term_name":"N-myristoylglycine","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d7bf6"}],"cross_refs":[{"db":"PDB","id":"1QA5","_id":"685af523b4ac24d5329d7bf2"},{"db":"PDB","id":"1QA4","_id":"685af523b4ac24d5329d7bf3"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":14,"interaction_partner":[],"reference_html":"Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein. <i> Geyer M, Munte CE, Schorr J, Kellner R, Kalbitzer HR. </i> J Mol Biol, 1999","reference_id":"10339411","region_id":"DP00189r009","released":"2022_03","sample":[],"sequence_construct":"GGKWSKSSVVGWPAVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAANNAACAW","statement":[{"type":"Introduction","text":"Here, we investigate the solution structures of the myristoylated and non-myristoylated HIV-1 Nef anchor domain (2–57) under buffer conditions as close to physiological conditions as possible.","_id":"685af523b4ac24d5329d7bf4"},{"type":"Results","text":"Myristoylation induces a change of the conformational states of the anchor domain, leading to the stabilization of helix H2 and to the induction of the first helical element H1 (Pro14 to Arg22).","_id":"685af523b4ac24d5329d7bf5"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T11:24:14.542Z","_id":"685af523b4ac24d5329d7bf8"},"version":1,"_id":"685af523b4ac24d5329d7bf1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":2,"end":2,"statements":[{"type":"Results","text":"The myristic moiety at Gly2 itself covers the large hydrophobic ring system of Trp5, thereby forming a loop with Gly2, Gly3 and Lys4 in the kink region and exposing the side-chain of the succeeding residue Ser6 to the solvent (Figure 7). ","_id":"685af523b4ac24d5329d7bfd"}],"term_id":"MOD:00068","term_name":"N-myristoylglycine","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d7bfc"}],"cross_refs":[{"db":"PDB","id":"1QA5","_id":"685af523b4ac24d5329d7bfa"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":14,"interaction_partner":[],"reference_html":"Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein. <i> Geyer M, Munte CE, Schorr J, Kellner R, Kalbitzer HR. </i> J Mol Biol, 1999","reference_id":"10339411","region_id":"DP00189r010","released":"2022_03","sample":[],"sequence_construct":"GGKWSKSSVVGWPAVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAANNAACAW","statement":[{"type":"Results","text":"Myristoylation induces a change of the conformational states of the anchor domain, leading to the stabilization of helix H2 and to the induction of the first helical element H1 (Pro14 to Arg22).","_id":"685af523b4ac24d5329d7bfb"}],"states_connection":[],"term_id":"IDPO:0000040","term_name":"fatty acylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T11:24:16.462Z","_id":"685af523b4ac24d5329d7bfe"},"version":1,"_id":"685af523b4ac24d5329d7bf9","reference_source":"pmid"}],"__v":0,"disorder_content":0.23786407766990292,"disprot_consensus":{"full":[{"start":2,"end":14,"type":"T"},{"start":15,"end":34,"type":"D"},{"start":42,"end":57,"type":"D"}],"Structural state":[{"start":2,"end":34,"type":"D"},{"start":42,"end":57,"type":"D"}],"Structural transition":[{"start":2,"end":14,"type":"T"}],"Disorder function":[{"start":2,"end":14,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00175","name":"Oxidoreductase NAD-binding domain","start":457,"end":563},{"id":"PF00258","name":"Flavodoxin","start":66,"end":197},{"id":"PF00667","name":"FAD binding domain","start":230,"end":424}],"gene3D":[{"start":445,"end":599,"id":"3.40.50.80","name":"Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module"},{"start":280,"end":384,"id":"1.20.990.10","name":"NADPH-cytochrome p450 Reductase; Chain A, domain 3"},{"start":53,"end":219,"id":"3.40.50.360","name":"3.40.50.360"},{"start":232,"end":439,"id":"2.40.30.10","name":"Translation factors"}]},"uniref50":"UniRef50_P38038","sequence":"MTTQVPPSALLPLNPEQLARLQAATTDLTPTQLAWVSGYFWGVLNQQPAALAATPAPAAEMPGITIISASQTGNARRVAEALRDDLLAAKLNVKLVNAGDYKFKQIASEKLLIVVTSTQGEGEPPEEAVALHKFLFSKKAPKLENTAFAVFSLGDSSYEFFCQSGKDFDSKLAELGGERLLDRVDADVEYQAAASEWRARVVDALKSRAPVAAPSQSVATGAVNEIHTSPYSKDAPLVASLSVNQKITGRNSEKDVRHIEIDLGDSGMRYQPGDALGVWYQNDPALVKELVELLWLKGDEPVTVEGKTLPLNEALQWHFELTVNTANIVENYATLTRSETLLPLVGDKAKLQHYAATTPIVDMVRFSPAQLDAEALINLLRPLTPRLYSIASSQAEVENEVHVTVGVVRYDVEGRARAGGASSFLADRVEEEGEVRVFIEHNDNFRLPANPETPVIMIGPGTGIAPFRAFMQQRAADEAPGKNWLFFGNPHFTEDFLYQVEWQRYVKDGVLTRIDLAWSRDQKEKVYVQDKLREQGAELWRWINDGAHIYVCGDANRMAKDVEQALLEVIAEFGGMDTEAADEFLSELRVERRYQRDVY","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P38038","disprot_id":"DP00190","ncbi_taxon_id":83333,"regions_counter":4,"creator":"mnecci","regions":[{"start":52,"end":62,"reference_id":"15966732","reference_source":"pmid","reference_html":"Solution structure of the sulfite reductase flavodoxin-like domain from Escherichia coli. <i> Sibille N, Blackledge M, Brutscher B, Covès J, Bersch B. </i> Biochemistry, 2005","date":"2023-01-24T18:00:28.676Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1YKG"}],"region_id":"DP00190r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30527","entry_name":"flavin"}],"statement":[{"text":"The well-folded domain consists of residues 63−208, whereas residues 52−62 and 209−218, which were present in the molecular construct, are disordered. ","type":"Results"}]},{"start":209,"end":218,"reference_id":"15966732","reference_source":"pmid","reference_html":"Solution structure of the sulfite reductase flavodoxin-like domain from Escherichia coli. <i> Sibille N, Blackledge M, Brutscher B, Covès J, Bersch B. </i> Biochemistry, 2005","date":"2023-01-24T18:00:36.425Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1YKG"}],"region_id":"DP00190r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30527","entry_name":"flavin"}],"statement":[{"text":"The well-folded domain consists of residues 63−208, whereas residues 52−62 and 209−218, which were present in the molecular construct, are disordered. ","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P38038","date":"2016-09-08T10:01:22.000Z","acc":"P38038","name":"Sulfite reductase [NADPH] flavoprotein alpha-component","length":599,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI000016815B","genes":[{"name":{"value":"cysJ","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01541","url":"https://hamap.expasy.org/unirule/MF_01541"}}]},"olnNames":[{"value":"b2764"},{"value":"JW2734"}]}],"alphafold_very_low_content":0.0651085141903172,"disorder_content":0.035058430717863104,"disprot_consensus":{"full":[{"start":52,"end":62,"type":"D"},{"start":209,"end":218,"type":"D"}],"Structural state":[{"start":52,"end":62,"type":"D"},{"start":209,"end":218,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00997","name":"Kappa casein","start":23,"end":188}]},"uniref50":"UniRef50_P02668","sequence":"MMKSFFLVVTILALTLPFLGAQEQNQEQPIRCEKDERFFSDKIAKYIPIQYVLSRYPSYGLNYYQQKPVALINNQFLPYPYYAKPAAVRSPAQILQWQVLSNTVPAKSCQAQPTTMARHPHPHLSFMAIPPKKNQDKTEIPTINTIASGEPTSTPTTEAVESTVATLEDSPEVIESPPEINTVQVTSTAV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P02668","disprot_id":"DP00192","ncbi_taxon_id":9913,"regions_counter":4,"creator":"agasparini","regions":[{"start":1,"end":190,"reference_id":"30851321","reference_source":"pmid","reference_html":"Characterization of structural conformers of κ-casein utilizing fluorescence spectroscopy. <i> Mirdha L, Chakraborty H. </i> Int J Biol Macromol, 2019","date":"2023-01-27T19:06:46.064Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00192r004","statement":[{"text":"The far-UV circular dichroic spectra of κ-casein at different pH and concentration of CTAB have been shown in Fig. 9.","type":"Results"},{"text":"The far-UV circular dichroic spectra shows a large negative ellipticity at 200 nm and moderate ellipticity at 190 nm, indicating it is disordered.","type":"Curator statement"}]}],"released":"2016_10","uniref100":"UniRef100_P02668","date":"2016-08-25T16:56:18.000Z","acc":"P02668","name":"Kappa-casein","length":190,"organism":"Bos taurus","dataset":[],"UniParc":"UPI0000126FE5","genes":[{"name":{"value":"CSN3"},"synonyms":[{"value":"CSN10"},{"value":"CSNK"}]}],"alphafold_very_low_content":0.4105263157894737,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":190,"type":"D"}],"Structural state":[{"start":1,"end":190,"type":"D"}]}},{"features":{"pfam":[{"id":"PF04386","name":"Stringent starvation protein B","start":9,"end":165}],"gene3D":[{"start":1,"end":118,"id":"2.30.30.220","name":"SspB-like"}]},"uniref50":"UniRef50_Q83Q08","sequence":"MDLSQLTPRRPYLLRAFYEWLLDNQLTPHLVVDVTLPGVQVPMEYARDGQIVLNIAPRAVGNLELANDEVRFNARFGGIPRQVSVPLAAVLAIYARENGAGTMFEPEAAYDEDTSIMNDEEASADNETVMSVIDGDKPDHDDDTHPDDEPPQPPRGGRPALRVVK","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_Q83Q08","disprot_id":"DP00194","ncbi_taxon_id":83333,"regions_counter":14,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":165,"region_id":"DP00194r001","released":"2023_06","ec_id":"ECO:0007691","reference_html":"Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease. <i> Wah DA, Levchenko I, Rieckhof GE, Bolon DN, Baker TA, Sauer RT. </i> Mol Cell, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":111,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14536075","version":3,"ec_name":"cleavage assay evidence used in manual assertion","date":"2023-01-31T16:06:11.073Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"The proteolytic sensitivity, variable length, and poor sequence conservation of the C-terminal residues of SspB suggest that this region (residues 111–165 in E. coli SspB) might be unstructured.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":165,"region_id":"DP00194r005","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease. <i> Wah DA, Levchenko I, Rieckhof GE, Bolon DN, Baker TA, Sauer RT. </i> Mol Cell, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":118,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14536075","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-01-31T16:06:44.276Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Indeed, the circular-dichroism (CD) spectrum of residues 118 to 165 in intact E. coli SspB (Figure 2B, inset; determined by subtracting the spectrum for the 1–117 fragment from the spectrum of the intact protein) had a minimum at 198 nm, as would be expected if the C-terminal 48 residues of E. coli SspB form an ensemble of random-coil conformations (Ausio et al. 1987).","type":"Results"}]},{"start":112,"end":154,"reference_id":"14536075","reference_source":"pmid","reference_html":"Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease. <i> Wah DA, Levchenko I, Rieckhof GE, Bolon DN, Baker TA, Sauer RT. </i> Mol Cell, 2003","date":"2023-01-31T16:11:24.806Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Glu112-Pro154del","start":null,"end":null,"position":null}],"region_id":"DP00194r009","statement":[{"text":"To create a more dramatic change in the length of the linker, we deleted residues 112–154, leaving approximately eight residues between Tyr110, the last fully-structured residue in the substrate binding domain (Levchenko et al. 2003), and the conserved sequence in the XB module. As shown in Figure 5 (experiment k), this mutant protein was also able to stimulate degradation, but only about 60% as well as full-length SspB. These experiments show that large variations in the composition and length of the linker can be tolerated with retention of substantial SspB activity, but also suggest that sufficient length or linker flexibility is required for full SspB function.","type":"Results"}]},{"start":156,"end":165,"reference_id":"14536075","reference_source":"pmid","reference_html":"Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease. <i> Wah DA, Levchenko I, Rieckhof GE, Bolon DN, Baker TA, Sauer RT. </i> Mol Cell, 2003","date":"2025-12-23T12:41:19.057Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0045732","term_name":"positive regulation of protein catabolic process","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"ec_go":"IDA","region_id":"DP00194r010","statement":[{"text":"Full-length E. coli SspB (1–165) stimulates ClpXP-mediated degradation of GFP-ssrA (Levchenko et al. 2000, Flynn et al. 2001). By contrast, neither the purified proteolytic fragment containing the SspB substrate binding domain (1–117) nor the substrate binding domain plus linker (1–155) enhanced ClpXP-degradation of GFP-ssrA (Figure 1C). Thus, residues at the extreme C terminus of SspB are required, either directly or indirectly, for this protein to stimulate ClpXP of degradation ssrA-tagged substrates.","type":"Results"}],"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":156,"end":165,"reference_id":"14536075","reference_source":"pmid","reference_html":"Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease. <i> Wah DA, Levchenko I, Rieckhof GE, Bolon DN, Baker TA, Sauer RT. </i> Mol Cell, 2003","date":"2023-02-23T13:17:42.502Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0032781","term_name":"positive regulation of ATP-dependent activity","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IDA","region_id":"DP00194r011","statement":[{"text":"Full-length E. coli SspB (1–165) stimulates ClpXP-mediated degradation of GFP-ssrA (Levchenko et al. 2000, Flynn et al. 2001). By contrast, neither the purified proteolytic fragment containing the SspB substrate binding domain (1–117) nor the substrate binding domain plus linker (1–155) enhanced ClpXP-degradation of GFP-ssrA (Figure 1C). Thus, residues at the extreme C terminus of SspB are required, either directly or indirectly, for this protein to stimulate ClpXP of degradation ssrA-tagged substrates.","type":"Results"}],"term_comment":"","term_def":"\"Any process that activates or increases the rate of an ATP-dependent activity.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":118,"end":165,"reference_id":"14536075","reference_source":"pmid","reference_html":"Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease. <i> Wah DA, Levchenko I, Rieckhof GE, Bolon DN, Baker TA, Sauer RT. </i> Mol Cell, 2003","date":"2023-01-31T16:55:45.831Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P0A6H1","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00194r012","statement":[{"text":"Gel-filtration experiments showed that the C-terminal residues of SspB are also required for formation of stable delivery complexes with ssrA-tagged substrates and ClpX. As expected (Wah et al. 2002), incubation of GFP-ssrA, full-length SspB, and ClpX resulted in formation of a stable ternary complex (Figure 3, top trace). By contrast, when the isolated substrate binding domain was substituted for full-length SspB, no delivery complex was observed, and all of the GFP-ssrA migrated at a position expected for a complex of a dimer of the substrate binding domain with two molecules of GFP-ssrA (Figure 3, bottom trace).","type":"Results"},{"text":"ssrA tag contains the sequence AANDENYALAA.","type":"Curator statement"}],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false},{"start":156,"end":165,"reference_id":"14536075","reference_source":"pmid","reference_html":"Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease. <i> Wah DA, Levchenko I, Rieckhof GE, Bolon DN, Baker TA, Sauer RT. </i> Mol Cell, 2003","date":"2023-01-31T17:04:39.327Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005632","ec_ontology":"ECO","ec_name":"fluorescence anisotropy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P0A6H1","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00194r013","statement":[{"text":"A synthetic BODIPY-labeled peptide containing the C-terminal 10 residues of SspB (156–165) bound ClpX with a Kd of 23 ± 5 μM (Figure 4A).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":156,"end":165,"reference_id":"14536075","reference_source":"pmid","reference_html":"Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease. <i> Wah DA, Levchenko I, Rieckhof GE, Bolon DN, Baker TA, Sauer RT. </i> Mol Cell, 2003","date":"2023-01-31T17:08:41.062Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0032781","term_name":"positive regulation of ATP-dependent activity","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001258","ec_ontology":"ECO","ec_name":"spectrophotometry evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"EXP","region_id":"DP00194r014","statement":[{"text":"The unlabeled XB peptide stimulated the ATPase activity of ClpX with a half-maximal value (19 ± 5 μM; Figure 4B) in good agreement with the Kd for binding. At saturation, the XB peptide stimulated the ATPase activity of ClpX by a factor of roughly 2-fold, a value similar to the stimulation observed with full-length SspB (Wah et al. 2002). By contrast, SspB fragments containing just the substrate binding domain or substrate binding plus linker regions showed no significant stimulation of ATPase activity (data not shown).","type":"Results"}],"term_comment":"","term_def":"\"Any process that activates or increases the rate of an ATP-dependent activity.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_P0AFZ4","date":"2016-09-08T09:34:31.000Z","acc":"P0AFZ3","name":"Stringent starvation protein B","length":165,"organism":"Escherichia coli (strain K12)","dataset":["Stress response proteins"],"UniParc":"UPI000003EB00","genes":[{"name":{"value":"sspB"},"olnNames":[{"value":"b3228"},{"value":"JW3197"}]}],"alphafold_very_low_content":0.10303030303030303,"disorder_content":0.3333333333333333,"disprot_consensus":{"full":[{"start":111,"end":165,"type":"D"}],"Structural state":[{"start":111,"end":165,"type":"D"}],"Disorder function":[{"start":112,"end":154,"type":"F"}],"Biological process":[{"start":156,"end":165,"type":"F"}],"Molecular function":[{"start":118,"end":165,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01101","name":"HMG14 and HMG17","start":2,"end":89}]},"uniref50":"UniRef50_P02313","sequence":"MPKRKAEGDAEGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKDGNNPAENGDAKTDQAQKAEGAGDAK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P02313","disprot_id":"DP00195","ncbi_taxon_id":9913,"regions_counter":13,"creator":"ftonello","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":90,"region_id":"DP00195r001","released":"2022_12","ec_id":"ECO:0006228","reference_html":"Studies on the conformational properties of the high-mobility-group chromosomal protein HMG 17 and its interaction with DNA. <i> Abercrombie BD, Kneale GG, Crane-Robinson C, Bradbury EM, Goodwin GH, Walker JM, Johns EW. </i> Eur J Biochem, 1978","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"565710","version":3,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","date":"2022-09-06T20:06:27.481Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The 6-pm region of the infrared spectrum of protein HMG 17 was obtained in solution at pH 6.8,1 M NaCl to check for the formation of p-structure. The amide 1 band was centred at  1644cm-1 and showed no evi- dence of any low-frequency components between 1630 and 1610 cm-1  that would indicate the formation of 8-structure [16,17].","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":90,"region_id":"DP00195r005","released":"2022_12","ec_id":"ECO:0006214","reference_html":"Studies on the conformational properties of the high-mobility-group chromosomal protein HMG 17 and its interaction with DNA. <i> Abercrombie BD, Kneale GG, Crane-Robinson C, Bradbury EM, Goodwin GH, Walker JM, Johns EW. </i> Eur J Biochem, 1978","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"565710","version":3,"ec_name":"small-angle neutron scattering evidence used in manual assertion","date":"2022-09-06T19:49:23.311Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The high R, value must  therefore be the result of a  disordered structure.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":90,"region_id":"DP00195r009","released":"2022_12","ec_id":"ECO:0006204","reference_html":"Studies on the conformational properties of the high-mobility-group chromosomal protein HMG 17 and its interaction with DNA. <i> Abercrombie BD, Kneale GG, Crane-Robinson C, Bradbury EM, Goodwin GH, Walker JM, Johns EW. </i> Eur J Biochem, 1978","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"565710","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-09-06T19:47:57.183Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The circular dichroism spectrum of protein HMG 17 in a  high-ionic-strength  buffer at pH 7.9  is shown in Fig. 1 ; the low ellipticity at 222 nm  indicates that under these conditions the protein has little or no helicity. Changing the pH and ionic strength does not alter  the ellipticity at 222 nm substantially  (Table 1) nor the overall shape of the curve.","type":"Results"}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":41,"term_name":"nucleic acid binding","start":16,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2022_12","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"565710","version":4,"reference_html":"Studies on the conformational properties of the high-mobility-group chromosomal protein HMG 17 and its interaction with DNA. <i> Abercrombie BD, Kneale GG, Crane-Robinson C, Bradbury EM, Goodwin GH, Walker JM, Johns EW. </i> Eur J Biochem, 1978","date":"2022-09-06T20:02:10.420Z","term_id":"GO:0003676","ec_id":"ECO:0006165","region_id":"DP00195r012","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"curator_orcid":"0000-0001-8399-7907","statement":[{"text":"This was done as described in Materials and Methods, using the same ratio of DNA/ protein as in the NMR experiments,  with NACl added to 0.35,O. 1 and 0 M. No free protein was found in the NaC1-free and 0.1 M NaCl  solutions,  but 75 2, of the  input  protein was  recovered from the 0.35 M NaCl  solution.","type":"Results"},{"text":" It is  striking that when the protein is bound at low ionic strength, certain resonan- ces are only  slightly affected whilst others are consid- erable reduced in apparent area by line broadening. Thus the arginine,  proline, serine, and to a  certain extent,  valine,  plus leucine  residues are bound. This indicates that the region  between about residues  15 and 40 is the primary binding site.","type":"Results"},{"text":"Since authors do not consider the first Met residue, the binding region boundaries are 16-41.","type":"Curator statement"}]},{"start":1,"end":90,"reference_id":"565710","reference_source":"pmid","reference_html":"","date":"2022-09-06T19:47:47.382Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00195r013","statement":[{"text":"Both spectra look like that of a  random coil protein with  residues of the same type giving a single sharp peak not showing any spread of chemical shift values. Furthermore, no meth- yl resonances are observed   between 0 and 1 ppm as is normally found with globular  proteins.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P02313","date":"2016-09-08T16:40:38.000Z","acc":"P02313","name":"Non-histone chromosomal protein HMG-17","length":90,"organism":"Bos taurus","dataset":[],"UniParc":"UPI000012C6B6","genes":[{"name":{"value":"HMGN2"},"synonyms":[{"value":"HMG17"}]}],"alphafold_very_low_content":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":90,"type":"D"}],"Structural state":[{"start":1,"end":90,"type":"D"}],"Molecular function":[{"start":16,"end":41,"type":"F"}]}},{"acc":"P20810","sequence":"MNPTETKAIPVSQQMEGPHLPNKKKHKKQAVKTEPEKKSQSTKLSVVHEKKSQEGKPKEHTEPKSLPKQASDTGSNDAHNKKAVSRSAEQQPSEKSTEPKTKPQDMISAGGESVAGITAISGKPGDKKKEKKSLTPAVPVESKPDKPSGKSGMDAALDDLIDTLGGPEETEEENTTYTGPEVSDPMSSTYIEELGKREVTIPPKYRELLAKKEGITGPPADSSKPIGPDDAIDALSSDFTCGSPTAAGKKTEKEESTEVLKAQSAGTVRSAAPPQEKKRKVEKDTMSDQALEALSASLGTRQAEPELDLRSIKEVDEAKAKEEKLEKCGEDDETIPSEYRLKPATDKDGKPLLPEPEEKPKPRSESELIDELSEDFDRSECKEKPSKPTEKTEESKAAAPAPVSEAVCRTSMCSIQSAPPEPATLKGTVPDDAVEALADSLGKKEADPEDGKPVMDKVKEKAKEEDREKLGEKEETIPPDYRLEEVKDKDGKPLLPKESKEQLPPMSEDFLLDALSEDFSGPQNASSLKFEDAKLAAAISEVVSQTPASTTQAGAPPRDTSQSDKDLDDALDKLSDSLGQRQPDPDENKPMEDKVKEKAKAEHRDKLGERDDTIPPEYRHLLDDNGQDKPVKPPTKKSEDSKKPADDQDPIDALSGDLDSCPSTTETSQNTAKDKCKKAASSSKAPKNGGKAKDSAKTTEETSKPKDD","alphafold_very_low_content":"0.4435028248587571","creator":"mnecci","dataset":[],"date":"2016-08-31T11:33:28.000Z","disprot_id":"DP00196","features":{"pfam":[{"id":"PF00748","name":"Calpain inhibitor","start":86,"end":214},{"id":"PF00748","name":"Calpain inhibitor","start":231,"end":354},{"id":"PF00748","name":"Calpain inhibitor","start":368,"end":496},{"id":"PF00748","name":"Calpain inhibitor","start":511,"end":633}]},"genes":[{"name":{"value":"CAST","evidences":[],"_id":"685af523b4ac24d5329d7c2b"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d7c2a"}],"length":708,"name":"Calpastatin","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":11,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI000016A731","uniref100":"UniRef100_P20810","uniref50":"UniRef50_P20810","uniref90":"UniRef90_P20810","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":137,"end":277,"interaction_partner":[],"reference_html":"Primary contact sites in intrinsically unstructured proteins: the case of calpastatin and microtubule-associated protein 2. <i> Csizmók V, Bokor M, Bánki P, Klement E, Medzihradszky KF, Friedrich P, Tompa K, Tompa P. </i> Biochemistry, 2005","reference_id":"15751971","region_id":"DP00196r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In accordance with this expectation, proteolysis of CSD1 and MAP2c under such conditions results in a picture typical of limited proteolysis, featuring the formation of only a few, relatively stable, fragments.","_id":"685af523b4ac24d5329d7c08"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-12-14T14:56:25.953Z","_id":"685af523b4ac24d5329d7c09"},"version":3,"_id":"685af523b4ac24d5329d7c07","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":137,"end":277,"interaction_partner":[],"reference_html":"Primary contact sites in intrinsically unstructured proteins: the case of calpastatin and microtubule-associated protein 2. <i> Csizmók V, Bokor M, Bánki P, Klement E, Medzihradszky KF, Friedrich P, Tompa K, Tompa P. </i> Biochemistry, 2005","reference_id":"15751971","region_id":"DP00196r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"For CSD1, the CD spectrum of the full-length protein has a minimum at 201 nm, characteristic of a protein in a largely disordered conformation (Figure 5A). The spectra of the two halves of the protein, however, are different, with the minimum of the C-terminal half shifted to about 205 nm.","_id":"685af523b4ac24d5329d7c0f"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-12-14T14:56:28.919Z","_id":"685af523b4ac24d5329d7c10"},"version":3,"_id":"685af523b4ac24d5329d7c0e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":137,"end":277,"interaction_partner":[],"reference_html":"Primary contact sites in intrinsically unstructured proteins: the case of calpastatin and microtubule-associated protein 2. <i> Csizmók V, Bokor M, Bánki P, Klement E, Medzihradszky KF, Friedrich P, Tompa K, Tompa P. </i> Biochemistry, 2005","reference_id":"15751971","region_id":"DP00196r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Because the mean hydrophobicity of MAP2c and CSD1 is practically the same (-0.780 for CSD1 and -0.781 for MAP2c, cf. other methods), the difference in their hydration indicates a substantial difference in the extent of their intramolecular interactions: judged simply by the amount of water that they bind, CSD1 appears more ordered than MAP2c.","_id":"685af523b4ac24d5329d7c16"},{"type":"Results","text":"In other words, its two halves interact in the intact molecule and partially replace each other’s bound water.","_id":"685af523b4ac24d5329d7c17"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-12-14T14:56:18.463Z","_id":"685af523b4ac24d5329d7c18"},"version":3,"_id":"685af523b4ac24d5329d7c15","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":137,"end":277,"interaction_partner":[],"reference_html":"Primary contact sites in intrinsically unstructured proteins: the case of calpastatin and microtubule-associated protein 2. <i> Csizmók V, Bokor M, Bánki P, Klement E, Medzihradszky KF, Friedrich P, Tompa K, Tompa P. </i> Biochemistry, 2005","reference_id":"15751971","region_id":"DP00196r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In accordance with this expectation, proteolysis of CSD1 and MAP2c under such conditions results in a picture typical of limited proteolysis, featuring the formation of only a few, relatively stable, fragments.","_id":"685af523b4ac24d5329d7c1e"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000048","term_name":"limited proteolysis display site","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-12-14T14:56:23.064Z","_id":"685af523b4ac24d5329d7c1f"},"version":1,"_id":"685af523b4ac24d5329d7c1d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[{"deviation":null,"statements":[{"type":"Methods","text":"The pH dependence of both proteins, full-length hCSD1 and its C-terminal half, was investigated by measuring 1H−15N amide cross-peak intensities from the appropriate HSQC spectra collected at 298 K and at pH 4.3, 5.23, and 6.17 for hCSD1(67−141) as well as pH 3.85, 5.53, 6.07, and 7.25 for hCSD1.","_id":"685af523b4ac24d5329d7c22"},{"type":"Results","text":"Since the physiological pH is ~7, measurements were carried out to approach this value. We found that an increasing pH (from 4.3 to 6.4) resulted in insignificant peak drifting with rather similar line shape characteristics. However, at pH >6.5, changes in both Hα and HN chemical shifts stopped but the extent of line broadening due to chemical exchange increased dramatically. As a consequence of these observations, we have carried out our measurements at 298 K and pH ~6.1.","_id":"685af523b4ac24d5329d7c23"}],"term_id":"NCIT:C45997","unit_id":"UO:0000196","unit_name":"pH","value":3.85,"_id":"685af523b4ac24d5329d7c21"},{"deviation":null,"statements":[{"type":"Methods","text":"The pH dependence of both proteins, full-length hCSD1 and its C-terminal half, was investigated by measuring 1H−15N amide cross-peak intensities from the appropriate HSQC spectra collected at 298 K and at pH 4.3, 5.23, and 6.17 for hCSD1(67−141) as well as pH 3.85, 5.53, 6.07, and 7.25 for hCSD1.","_id":"685af523b4ac24d5329d7c25"},{"type":"Results","text":"Since the physiological pH is ~7, measurements were carried out to approach this value. We found that an increasing pH (from 4.3 to 6.4) resulted in insignificant peak drifting with rather similar line shape characteristics. However, at pH >6.5, changes in both Hα and HN chemical shifts stopped but the extent of line broadening due to chemical exchange increased dramatically. As a consequence of these observations, we have carried out our measurements at 298 K and pH ~6.1.","_id":"685af523b4ac24d5329d7c26"}],"term_id":"NCIT:C45997","unit_id":"UO:0000196","unit_name":"pH","value":7.25,"_id":"685af523b4ac24d5329d7c24"}],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":137,"end":277,"interaction_partner":[],"reference_html":"Local structural preferences of calpastatin, the intrinsically unstructured protein inhibitor of calpain. <i> Kiss R, Kovács D, Tompa P, Perczel A. </i> Biochemistry, 2008","reference_id":"18537264","region_id":"DP00196r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The flexible nature of the backbone leads to narrower, lines resulting in an adequate signal-to-noise ratio.","_id":"685af523b4ac24d5329d7c27"},{"type":"Results","text":"As the typical helical 3JHNCR value is 4 Hz, the observed values correspond to the mainly random character of hCSD1 (data not shown).","_id":"685af523b4ac24d5329d7c28"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-12-14T14:56:10.307Z","_id":"685af523b4ac24d5329d7c29"},"version":1,"_id":"685af523b4ac24d5329d7c20","reference_source":"pmid"}],"__v":0,"disorder_content":0.19915254237288135,"disprot_consensus":{"full":[{"start":137,"end":277,"type":"D"}],"Structural state":[{"start":137,"end":277,"type":"D"}],"Disorder function":[{"start":137,"end":277,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00707","name":"Translation initiation factor IF-3, C-terminal domain","start":91,"end":177},{"id":"PF05198","name":"Translation initiation factor IF-3, N-terminal domain","start":15,"end":84}],"gene3D":[{"start":84,"end":180,"id":"3.30.110.10","name":"Translation initiation factor 3 (IF-3), C-terminal domain"},{"start":10,"end":83,"id":"3.10.20.80","name":"Translation initiation factor 3 (IF-3), N-terminal domain"}]},"uniref50":"UniRef50_P33321","sequence":"MKGGKRVQTARPNRINGEIRAQEVRLTGLEGEQLGIVSLREALEKAEEAGVDLVEISPNAEPPVCRIMDYGKFLYEKSKSSKEQKKKQKVIQVKEIKFRPGTDEGDYQVKLRSLIRFLEEGDKAKITLRFRGREMAHQQIGMEVLNRVKDDLQELAVVESFPTKIEGRQMIMVLAPKKKQ","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P33321","disprot_id":"DP00197","ncbi_taxon_id":83333,"regions_counter":3,"creator":"dpiovesan","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":89,"region_id":"DP00197r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Heteronuclear NMR studies of E. coli translation initiation factor IF3. Evidence that the inter-domain region is disordered in solution. <i> Moreau M, de Cock E, Fortier PL, Garcia C, Albaret C, Blanquet S, Lallemand JY, Dardel F. </i> J Mol Biol, 1997","term_id":"IDPO:0000002","curator_id":"vnugnes","start":78,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-01-31T19:17:42.443Z","reference_source":"pmid","term_name":"disorder","reference_id":"9054966","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Taken altogether, these results strongly suggest that, in solution, the inter-domain linker is disordered rather than α-helical. Indeed, most of the chemical shifts of the amide groups of these residues are clustered in the “random coil” region.","type":"Article"}],"construct_alterations":[{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Article","text":"Indeed, 7 of the 19 lysines of E. coli IF3 (short form) cluster in the central region (K77, K79, K82, K85, K88, K87, K89) and we have therefore produced an [α-15N]lysine labelled IF3 sample as a tool to specifically investigate the conformation and dynamics of this region."}]}]},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":89,"term_name":"flexible linker","released":"2023_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Heteronuclear NMR studies of E. coli translation initiation factor IF3. Evidence that the inter-domain region is disordered in solution. <i> Moreau M, de Cock E, Fortier PL, Garcia C, Albaret C, Blanquet S, Lallemand JY, Dardel F. </i> J Mol Biol, 1997","term_id":"IDPO:0000033","curator_id":"vnugnes","start":78,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"9054966","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-01-31T19:18:35.456Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00197r002","ec_go":"EXP","disprot_namespace":"Disorder function","construct_alterations":[{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Article","text":"Indeed, 7 of the 19 lysines of E. coli IF3 (short form) cluster in the central region (K77, K79, K82, K85, K88, K87, K89) and we have therefore produced an [α-15N]lysine labelled IF3 sample as a tool to specifically investigate the conformation and dynamics of this region."}]}],"statement":[{"text":"Taken altogether, these results strongly suggest that, in solution, the inter-domain linker is disordered rather than α-helical. Indeed, most of the chemical shifts of the amide groups of these residues are clustered in the “random coil” region.","type":"Article"}]}],"released":"2016_10","uniref100":"UniRef100_B7USA1","date":"2016-09-06T16:01:03.000Z","acc":"P0A707","name":"Translation initiation factor IF-3","length":180,"organism":"Escherichia coli (strain K12)","dataset":["RNA-binding proteins"],"UniParc":"UPI0000047CBD","genes":[{"name":{"value":"infC","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00080","url":"https://hamap.expasy.org/unirule/MF_00080"}}]},"synonyms":[{"value":"fit"},{"value":"srjA"}],"olnNames":[{"value":"b1718"},{"value":"JW5829"}]}],"alphafold_very_low_content":0.044444444444444446,"disorder_content":0.06666666666666667,"disprot_consensus":{"full":[{"start":78,"end":89,"type":"D"}],"Structural state":[{"start":78,"end":89,"type":"D"}],"Disorder function":[{"start":78,"end":89,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02189","name":"Immunoreceptor tyrosine-based activation motif","start":69,"end":88},{"id":"PF02189","name":"Immunoreceptor tyrosine-based activation motif","start":139,"end":158},{"id":"PF11628","name":"T-cell surface glycoprotein CD3 zeta chain","start":28,"end":58}]},"uniref50":"UniRef50_P20963","sequence":"MKWKALFTAAILQAQLPITEAQSFGLLDPKLCYLLDGILFIYGVILTALFLRVKFSRSADAPAYQQGQNQLYNELNLGRREEYDVLDKRRGRDPEMGGKPQRRKNPQEGLYNELQKDKMAEAYSEIGMKGERRRGKGHDGLYQGLSTATKDTYDALHMQALPPR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P20963","disprot_id":"DP00200","ncbi_taxon_id":9606,"regions_counter":9,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":164,"region_id":"DP00200r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif. <i> Sigalov A, Aivazian D, Stern L. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":49,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14967045","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-02-03T13:52:44.725Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"As shown in Figure 4B, the spectrum presents features resembling that of an unfolded state, particularly with the backbone amide 1H chemical shifts spanning only 7.6−8.6 ppm (1.0 ppm). This low dispersion of the backbone amide 1H chemical shifts is typical for unfolded or intrinsically disordered proteins (54, 55, 57)   .","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":164,"region_id":"DP00200r002","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif. <i> Sigalov A, Aivazian D, Stern L. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":49,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14967045","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-02-03T13:51:06.325Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"ζcyt Is an Unstructured, Random-Coil Protein, and Its Oligomerization Does Not Result in Formation of Detectable Secondary or Tertiary Structure. (1) CD Spectroscopy. The far-ultraviolet CD spectra of ζcyt show the characteristics of an unfolded protein (Figure 4A), consistent with earlier published results ( 40, 49).","type":"Results"}]},{"start":49,"end":164,"reference_id":"14967045","reference_source":"pmid","reference_html":"Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif. <i> Sigalov A, Aivazian D, Stern L. </i> Biochemistry, 2004","date":"2023-02-03T14:00:10.217Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051259","term_name":"protein complex oligomerization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"EXP","region_id":"DP00200r007","statement":[{"text":"The ζcyt Is Predominantly Dimeric, and the Oligomerization Is Reversible and Dependent on Concentration and Temperature. The apparent molecular mass of ζcyt was determined using gel filtration, sedimentation equilibrium, and light scattering (Table 1). As compared to the molecular mass predicted from the sequence and confirmed by mass spectroscopy (13157 Da), the native apparent molecular mass indicated the formation of oligomeric forms, with the predominant species a dimer in rapid equilibrium with monomer and larger oligomers.","type":"Results"},{"text":"The apparent native molecular mass of ζcyt−ζcyt (0.3 mg/mL) as determined by gel filtration was ∼27 kDa (data not shown), as expected for the covalent dimer and consistent with the molecular mass observed by ES-MS and predicted by the protein sequence (27118 Da).","type":"Results"},{"text":"The analysis estimated the apparent monomer−dimer and the dimer−tetramer equilibrium dissociation constants, Kd(monomer-dimer) and Kd(dimer-tetramer), as 9.2 ± 1.6 μM and 0.9 ± 0.2 mM (mean ± a standard deviation), respectively.","type":"Results"}],"term_comment":"","term_def":"\"The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of component monomers; protein oligomers may be composed of different or identical monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.\" [GOC:ai, PMID:18293929]","term_is_obsolete":false,"term_not_annotate":false},{"start":49,"end":164,"reference_id":"14967045","reference_source":"pmid","reference_html":"Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif. <i> Sigalov A, Aivazian D, Stern L. </i> Biochemistry, 2004","date":"2023-02-03T14:01:22.150Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051259","term_name":"protein complex oligomerization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001170","ec_ontology":"ECO","ec_name":"cross-linking evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P20963","operator":null,"partner_start":49,"partner_end":164}],"region_id":"DP00200r008","statement":[{"text":"The ζcyt Is Predominantly Dimeric, and the Oligomerization Is Reversible and Dependent on Concentration and Temperature. The apparent molecular mass of ζcyt was determined using gel filtration, sedimentation equilibrium, and light scattering (Table 1). As compared to the molecular mass predicted from the sequence and confirmed by mass spectroscopy (13157 Da), the native apparent molecular mass indicated the formation of oligomeric forms, with the predominant species a dimer in rapid equilibrium with monomer and larger oligomers.","type":"Results"},{"text":"Neither glutaraldehyde nor dimethyl suberimidate cross-linking resulted in detectable amounts of ζcyt oligomers, as analyzed by SDS−PAGE, but bis(sulfosuccinimidyl) suberate (BS3) cross-linking (Figure 1C, inset) resulted in monomeric (∼13 kDa), dimeric (∼26 kDa), trimeric (∼39 kDa), and tetrameric (∼52 kDa) species.","type":"Results"}],"term_comment":"","term_def":"\"The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of component monomers; protein oligomers may be composed of different or identical monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.\" [GOC:ai, PMID:18293929]","term_is_obsolete":false,"term_not_annotate":false},{"start":49,"end":164,"reference_id":"14967045","reference_source":"pmid","reference_html":"Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif. <i> Sigalov A, Aivazian D, Stern L. </i> Biochemistry, 2004","date":"2023-02-03T14:03:30.863Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051259","term_name":"protein complex oligomerization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P20963","operator":null,"partner_start":49,"partner_end":164}],"region_id":"DP00200r009","statement":[{"text":"The ζcyt Is Predominantly Dimeric, and the Oligomerization Is Reversible and Dependent on Concentration and Temperature. The apparent molecular mass of ζcyt was determined using gel filtration, sedimentation equilibrium, and light scattering (Table 1). As compared to the molecular mass predicted from the sequence and confirmed by mass spectroscopy (13157 Da), the native apparent molecular mass indicated the formation of oligomeric forms, with the predominant species a dimer in rapid equilibrium with monomer and larger oligomers.","type":"Results"},{"text":"The best fit, as judged by (1) estimated monomeric molecular mass closest to that predicted from the amino acid sequence and confirmed by ES-MS, (2) the lowest goodness-of-fit value, and (3) random distribution of residuals, was obtained with a model for reversible monomer−dimer−tetramer equilibrium (Figure 2, solid line).","type":"Results"}],"term_comment":"","term_def":"\"The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of component monomers; protein oligomers may be composed of different or identical monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.\" [GOC:ai, PMID:18293929]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_P20963","date":"2016-08-24T16:56:45.000Z","acc":"P20963","name":"T-cell surface glycoprotein CD3 zeta chain","length":164,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000158590","genes":[{"name":{"value":"CD247"},"synonyms":[{"value":"CD3Z"},{"value":"T3Z"},{"value":"TCRZ"}]}],"alphafold_very_low_content":0.21341463414634146,"disorder_content":0.7073170731707317,"disprot_consensus":{"full":[{"start":49,"end":164,"type":"D"}],"Structural state":[{"start":49,"end":164,"type":"D"}],"Biological process":[{"start":49,"end":164,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05511","name":"Mitochondrial ATP synthase coupling factor 6","start":1,"end":97}],"gene3D":[{"start":39,"end":101,"id":"1.10.246.110","name":"Mitochondrial ATP synthase-coupling factor 6"}]},"uniref50":"UniRef50_P02721","sequence":"MILQRLFRLSSAVQSAISVSWRRNIGITAVAFNKELDPVQKLFVDKIREYRTKRQTSGGPVDAGPEYQQDLDRELFKLKQMYGKADMNTFPNFTFEDPKFEVVEKPQS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P02721","disprot_id":"DP00201","ncbi_taxon_id":9913,"regions_counter":9,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":66,"region_id":"DP00201r004","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Solution structure of subunit F(6) from the peripheral stalk region of ATP synthase from bovine heart mitochondria. <i> Carbajo RJ, Silvester JA, Runswick MJ, Walker JE, Neuhaus D. </i> J Mol Biol, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":55,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15327958","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-02-03T16:31:22.025Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1VZS"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"However, it is clear both from the superpositions and from the identities of the particularly sharp signals in the spectra that most of the residues not involved in the helices are substantially disordered. In addition to the N and C termini, these regions also include the loop connecting the two helices (residues 23–33).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":108,"region_id":"DP00201r007","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Solution structure of subunit F(6) from the peripheral stalk region of ATP synthase from bovine heart mitochondria. <i> Carbajo RJ, Silvester JA, Runswick MJ, Walker JE, Neuhaus D. </i> J Mol Biol, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":84,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15327958","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-02-03T16:32:12.082Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1VZS"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"However, it is clear both from the superpositions and from the identities of the particularly sharp signals in the spectra that most of the residues not involved in the helices are substantially disordered.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P02721","date":"2016-09-08T08:43:09.000Z","acc":"P02721","name":"ATP synthase-coupling factor 6, mitochondrial","length":108,"organism":"Bos taurus","dataset":[],"UniParc":"UPI0000174214","genes":[{"name":{"value":"ATP5PF","evidences":[{"code":"ECO:0000250","source":{"name":"UniProtKB","id":"P18859","url":"https://www.uniprot.org/uniprot/P18859"}}]},"synonyms":[{"value":"ATP5J"}]}],"alphafold_very_low_content":0,"disorder_content":0.3425925925925926,"disprot_consensus":{"full":[{"start":55,"end":66,"type":"D"},{"start":84,"end":108,"type":"D"}],"Structural state":[{"start":55,"end":66,"type":"D"},{"start":84,"end":108,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03884","name":"DNA gyrase inhibitor YacG","start":7,"end":56}],"gene3D":[{"start":1,"end":65,"id":"3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A"}]},"uniref50":"UniRef50_P44921","sequence":"MSETITVNCPTCGKTVVWGEISPFRPFCSKRCQLIDLGEWAAEEKRIPSSGDLSESDDWSEEPKQ","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_A8ALJ6","disprot_id":"DP00202","ncbi_taxon_id":83334,"regions_counter":1,"creator":"dpiovesan","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":65,"region_id":"DP00202r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"NMR structure of the Escherichia coli protein YacG: a novel sequence motif in the zinc-finger family of proteins. <i> Ramelot TA, Cort JR, Yee AA, Semesi A, Edwards AM, Arrowsmith CH, Kennedy MA. </i> Proteins, 2002","term_id":"IDPO:0000002","curator_id":"vnugnes","start":40,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-02-03T16:49:10.223Z","reference_source":"pmid","term_name":"disorder","reference_id":"12211008","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"1LV3"},{"db":"DisProt","id":"DP01714r002"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"The first 3 and last 25 residues are unstructured and shown in a random configuration.","type":"Results"},{"text":"Protein sequence is 100% identical to the one from K12 strain, used in this publication.","type":"Curator statement"}]}],"released":"2016_10","uniref100":"UniRef100_A7ZHJ2","date":"2016-09-06T16:11:18.000Z","acc":"P0A8H9","name":"DNA gyrase inhibitor YacG","length":65,"organism":"Escherichia coli O157:H7","dataset":[],"UniParc":"UPI000013A025","genes":[{"name":{"value":"yacG","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00649","url":"https://hamap.expasy.org/unirule/MF_00649"}}]},"olnNames":[{"value":"Z0111"},{"value":"ECs0105"}]}],"alphafold_very_low_content":0,"disorder_content":0.4,"disprot_consensus":{"full":[{"start":40,"end":65,"type":"D"}],"Structural state":[{"start":40,"end":65,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00575","name":"S1 RNA binding domain","start":36,"end":117},{"id":"PF10150","name":"Ribonuclease E/G family","start":121,"end":391},{"id":"PF12111","name":"Polyribonucleotide phosphorylase C terminal","start":1022,"end":1058},{"id":"PF20833","name":"RNase E/G, Thioredoxin-like domain","start":403,"end":488}],"gene3D":[{"start":32,"end":125,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"},{"start":401,"end":510,"id":"3.40.1260.20","name":"Ribonuclease E, catalytic domain"}]},"uniref50":"UniRef50_P21513","sequence":"MKRMLINATQQEELRVALVDGQRLYDLDIESPGHEQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPLKEIAREYFPANYSAHGRPNIKDVLREGQEVIVQIDKEERGNKGAALTTFISLAGSYLVLMPNNPRAGGISRRIEGDDRTELKEALASLELPEGMGLIVRTAGVGKSAEALQWDLSFRLKHWEAIKKAAESRPAPFLIHQESNVIVRAFRDYLRQDIGEILIDNPKVLELARQHIAALGRPDFSSKIKLYTGEIPLFSHYQIESQIESAFQREVRLPSGGSIVIDSTEALTAIDINSARATRGGDIEETAFNTNLEAADEIARQLRLRDLGGLIVIDFIDMTPVRHQRAVENRLREAVRQDRARIQISHISRFGLLEMSRQRLSPSLGESSHHVCPRCSGTGTVRDNESLSLSILRLIEEEALKENTQEVHAIVPVPIASYLLNEKRSAVNAIETRQDGVRCVIVPNDQMETPHYHVLRVRKGEETPTLSYMLPKLHEEAMALPSEEEFAERKRPEQPALATFAMPDVPPAPTPAEPAAPVVAPAPKAAPATPAAPAQPGLLSRFFGALKALFSGGEETKPTEQPAPKAEAKPERQQDRRKPRQNNRRDRNERRDTRSERTEGSDNREENRRNRRQAQQQTAETRESRQQAEVTEKARTADEQQAPRRERSRRRNDDKRQAQQEAKALNVEEQSVQETEQEERVRPVQPRRKQRQLNQKVRYEQSVAEEAVVAPVVEETVAAEPIVQEAPAPRTELVKVPLPVVAQTAPEQQEENNADNRDNGGMPRRSRRSPRHLRVSGQRRRRYRDERYPTQSPMPLTVACASPELASGKVWIRYPIVRPQDVQVEEQREQEEVHVQPMVTEVPVAAAIEPVVSAPVVEEVAGVVEAPVQVAEPQPEVVETTHPEVIAAAVTEQPQVITESDVAVAQEVAEQAEPVVEPQEETADIEEVVETAEVVVAEPEVVAQPAAPVVAEVAAEVETVAAVEPEVTVEHNHATAPMTRAPAPEYVPEAPRHSDWQRPTFAFEGKGAAGGHTATHHASAAPARPQPVE","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P21513","disprot_id":"DP00207","ncbi_taxon_id":83333,"regions_counter":26,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1061,"region_id":"DP00207r001","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. <i> Callaghan AJ, Aurikko JP, Ilag LL, Günter Grossmann J, Chandran V, Kühnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF. </i> J Mol Biol, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":498,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15236960","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-02-07T16:33:02.155Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The CD spectra display the characteristics of a partly unstructured protein: a large negative peak at 200 nm and a value close to zero at 220 nm. A temperature-melt experiment indicated a loss of CD spectral signal at 200 nm, suggesting that some secondary structural elements are present.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":843,"region_id":"DP00207r004","released":"2023_06","ec_id":"ECO:0007680","reference_html":"Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. <i> Callaghan AJ, Aurikko JP, Ilag LL, Günter Grossmann J, Chandran V, Kühnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF. </i> J Mol Biol, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":628,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15236960","version":3,"ec_name":"chromatography evidence used in manual assertion","date":"2023-02-07T16:55:12.034Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0A8J8"}],"statement":[{"text":". In this regard we also note that the complex elutes aberrantly in size-exclusion chromatography (>500 kDa) and is well in excess of its predicted mass of 74 kDa, which further suggests that it has a largely unstructured portion.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1061,"region_id":"DP00207r007","released":"2023_06","ec_id":"ECO:0007689","reference_html":"Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. <i> Callaghan AJ, Aurikko JP, Ilag LL, Günter Grossmann J, Chandran V, Kühnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF. </i> J Mol Biol, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":498,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15236960","version":3,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2023-02-07T16:00:35.705Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"The predicted weight of the CTD is 67.7 kDa, but the purified protein runs closer to 90 kDa by SDS-PAGE. ","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":850,"region_id":"DP00207r009","start":603,"term_id":"IDPO:0000002","statement":[{"text":"The native ESI mass spectrometry analysis also reveals that RNase E 603–850 has a broad charge distribution in the spectra, which indicates that it has conformational disordered character.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"electrospray ionization fourier transform ion cyclotron resonance mass spectrometry evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29136196","version":2,"reference_html":"Analysis of the natively unstructured RNA/protein-recognition core in the Escherichia coli RNA degradosome and its interactions with regulatory RNA/Hfq complexes. <i> Bruce HA, Du D, Matak-Vinkovic D, Bandyra KJ, Broadhurst RW, Martin E, Sobott F, Shkumatov AV, Luisi BF. </i> Nucleic Acids Res, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006283","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-07T15:55:27.105Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":850,"region_id":"DP00207r010","start":603,"term_id":"IDPO:0000002","statement":[{"text":"To further investigate the overall structural conformation and degree of flexibility of the subassemblies in solution, SAXS was employed (Figure 3). The Guinier derived radius of gyration (Rg) values for RNase E 603–850, the binary complex and the ternary complex are ∼53, ∼54 and ∼64 Å, respectively (Supplementary Table S1). Comparing these values with expectations for globular proteins of the corresponding Mw suggests that all three particles have non-globular shapes.","type":"Results"},{"text":"The comparatively featureless scattering intensity curve and the smooth and extended P(r) distribution function of RNase E 603–850 indicate that the protein is highly flexible in solution (Figure 3A and B, respectively). Moreover, the dimensionless Kratky profile (dKratky) (54) of this RNase E segment is characteristic of an intrinsically disordered protein (IDP), with the intensity increasing gradually and the absence of a peak at lower angles (Figure 3C).","type":"Results"},{"text":"The calculated distribution of Rg values from the ensemble samples a similar space to that of the random pool, suggesting that the isolated RNase E 603–850, in the absence of its helicase and enolase partners, is indeed highly flexible (Rflex values of the ensemble and random pool are very close at 89.4% and 87.3%, respectively). Interestingly, the average Rg value of the ensemble distribution is slightly higher than that of the random pool. Furthermore, the experimental Rg of RNase E 603–850 is greater than the value of ∼46 Å predicted for a typical IDP of the same length (45,55), indicating that the construct is not only highly flexible but also favors extended conformations in solution.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29136196","version":2,"reference_html":"Analysis of the natively unstructured RNA/protein-recognition core in the Escherichia coli RNA degradosome and its interactions with regulatory RNA/Hfq complexes. <i> Bruce HA, Du D, Matak-Vinkovic D, Bandyra KJ, Broadhurst RW, Martin E, Sobott F, Shkumatov AV, Luisi BF. </i> Nucleic Acids Res, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-07T15:55:22.895Z"}},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P0A6P9","partner_end":null}],"ec_ontology":"ECO","end":850,"region_id":"DP00207r011","start":816,"term_id":"GO:0005515","statement":[{"text":"We have structurally characterized a subassembly of the degradosome-comprising a 248-residue segment of the natively unstructured part of RNase E, the DEAD-box helicase RhlB and the glycolytic enzyme enolase, and provide evidence that it serves as a flexible recognition centre that can co-recruit small regulatory RNA and the RNA chaperone Hfq","type":"Abstract"},{"text":"In this model, the binding of RhlB and enolase facilitates their partner RNase E 603–850 to transition from a highly dynamic state to a molten globule with transient secondary structure elements","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"29136196","version":3,"reference_html":"Analysis of the natively unstructured RNA/protein-recognition core in the Escherichia coli RNA degradosome and its interactions with regulatory RNA/Hfq complexes. <i> Bruce HA, Du D, Matak-Vinkovic D, Bandyra KJ, Broadhurst RW, Martin E, Sobott F, Shkumatov AV, Luisi BF. </i> Nucleic Acids Res, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"5OHG"}],"term_name":"protein binding","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-07T15:55:18.723Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":850,"region_id":"DP00207r012","start":816,"term_id":"IDPO:0000018","statement":[{"text":"We have structurally characterized a subassembly of the degradosome-comprising a 248-residue segment of the natively unstructured part of RNase E, the DEAD-box helicase RhlB and the glycolytic enzyme enolase, and provide evidence that it serves as a flexible recognition centre that can co-recruit small regulatory RNA and the RNA chaperone Hfq","type":"Abstract"},{"text":"In this model, the binding of RhlB and enolase facilitates their partner RNase E 603–850 to transition from a highly dynamic state to a molten globule with transient secondary structure elements","type":"Discussion"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29136196","version":3,"reference_html":"Analysis of the natively unstructured RNA/protein-recognition core in the Escherichia coli RNA degradosome and its interactions with regulatory RNA/Hfq complexes. <i> Bruce HA, Du D, Matak-Vinkovic D, Bandyra KJ, Broadhurst RW, Martin E, Sobott F, Shkumatov AV, Luisi BF. </i> Nucleic Acids Res, 2018","date":"2023-02-08T16:13:13.019Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"5OHG"}],"term_name":"disorder to molten globule","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0A6P9"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-08T16:38:16.718Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":850,"region_id":"DP00207r013","start":816,"term_id":"GO:0060090","statement":[{"text":"The RNA degradosome is a multi-enzyme assembly that plays a central role in the RNA metabolism of Escherichia coli and numerous other bacterial species including pathogens. At the core of the assembly is the endoribonuclease RNase E, one of the largest E. coli proteins and also one that bears the greatest region predicted to be natively unstructured. This extensive unstructured region, situated in the C-terminal half of RNase E, is punctuated with conserved short linear motifs that recruit partner proteins, direct RNA interactions, and enable association with the cytoplasmic membrane.","type":"Abstract"},{"text":"We have structurally characterized a subassembly of the degradosome–comprising a 248-residue segment of the natively unstructured part of RNase E, the DEAD-box helicase RhlB and the glycolytic enzyme enolase, and provide evidence that it serves as a flexible recognition centre that can co-recruit small regulatory RNA and the RNA chaperone Hfq.","type":"Abstract"},{"text":"Our results support a model in which the degradosome captures substrates and regulatory RNAs through the recognition centre, facilitates pairing to cognate transcripts and presents the target to the ribonuclease active sites of the greater assembly for cooperative degradation or processing.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"29136196","version":3,"reference_html":"Analysis of the natively unstructured RNA/protein-recognition core in the Escherichia coli RNA degradosome and its interactions with regulatory RNA/Hfq complexes. <i> Bruce HA, Du D, Matak-Vinkovic D, Bandyra KJ, Broadhurst RW, Martin E, Sobott F, Shkumatov AV, Luisi BF. </i> Nucleic Acids Res, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"5OHG"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-07T15:55:08.469Z"}},{"start":498,"end":1061,"reference_id":"15236960","reference_source":"pmid","reference_html":"Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. <i> Callaghan AJ, Aurikko JP, Ilag LL, Günter Grossmann J, Chandran V, Kühnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF. </i> J Mol Biol, 2004","date":"2023-02-07T16:04:24.484Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00207r015","statement":[{"text":"The scattering profile for the CTD has the characteristics of less well-folded proteins, such as the asymptotic behaviour of the Kratky plot (Figure 2A, green profile in the inset) that is characteristic of random chains.","type":"Results"}]},{"start":498,"end":1061,"reference_id":"15236960","reference_source":"pmid","reference_html":"Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. <i> Callaghan AJ, Aurikko JP, Ilag LL, Günter Grossmann J, Chandran V, Kühnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF. </i> J Mol Biol, 2004","date":"2023-02-07T16:14:06.819Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001170","ec_ontology":"ECO","ec_name":"cross-linking evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P0A8J8","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00207r016","statement":[{"text":"Protein–protein interactions were tested using the chemical cross-linking agent dimethyl suberimidate (DMS) (Figure 3A). Using denaturing gels, a cross-linked complex was observed with helicase (Figure 3A, lane 4).","type":"Results"},{"text":"The circled band was shown to contain both helicase RhlB and CTD using in-gel protease digestion and MALDI-mass spectrometry analysis.","type":"Figure"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":498,"end":1061,"reference_id":"15236960","reference_source":"pmid","reference_html":"Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. <i> Callaghan AJ, Aurikko JP, Ilag LL, Günter Grossmann J, Chandran V, Kühnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF. </i> J Mol Biol, 2004","date":"2023-02-07T17:12:47.965Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051259","term_name":"protein complex oligomerization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001170","ec_ontology":"ECO","ec_name":"cross-linking evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P21513","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00207r017","statement":[{"text":"The CTD was also observed to self-associate (Figure 3A, lane 2).","type":"Results"},{"text":"The circled band corresponds to a homodimer of the CTD. ","type":"Figure"},{"text":"We have found that the CTD can be cross-linked to itself, which is consistent with the findings reported by Vanzo et al.,19 that RNase E can self-interact.","type":"Discussion"}],"term_comment":"","term_def":"\"The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of component monomers; protein oligomers may be composed of different or identical monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.\" [GOC:ai, PMID:18293929]","term_is_obsolete":false,"term_not_annotate":false},{"start":628,"end":843,"reference_id":"15236960","reference_source":"pmid","reference_html":"Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. <i> Callaghan AJ, Aurikko JP, Ilag LL, Günter Grossmann J, Chandran V, Kühnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF. </i> J Mol Biol, 2004","date":"2023-02-07T17:14:00.166Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008312","term_name":"7S RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"RNAcentral","id":"URS0000D56C4B_559292","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00207r018","statement":[{"text":"The refolded CTD was also tested for RNA binding by an electrophoretic mobility-shift assay. It was observed to bind to 7 S rRNA with high affinity forming two well-defined complexes (Figure 3B).","type":"Results"},{"text":"The ability of R-domain to bind to structured RNA was tested by electrophoretic mobility-shift assays. Like the CTD, shown in Figure 3B, the R-domain was also observed to form two complexes with 7 S rRNA (Figure 5C).","type":"Results"},{"text":"The affinity of the R-domain for the 7 S rRNA is comparable to that of the CTD (Figure 3B). Therefore, it is likely that the coiled-coil region identified here is involved in binding to structured RNAs.","type":"Discussion"}],"term_comment":"","term_def":"\"Binding to a 7S RNA, the RNA component of the signal recognition particle (SRP).\" [GOC:jl, PMID:6181418]","term_is_obsolete":false,"term_not_annotate":false},{"start":628,"end":843,"reference_id":"15236960","reference_source":"pmid","reference_html":"Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. <i> Callaghan AJ, Aurikko JP, Ilag LL, Günter Grossmann J, Chandran V, Kühnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF. </i> J Mol Biol, 2004","date":"2023-02-07T16:32:27.684Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P0A8J8","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00207r019","statement":[{"text":"Purified helicase RhlB binds avidly to this domain, and the R-domain–helicase complex can be isolated by size-exclusion chromatography as an earlier-eluting species in an approximate 1 : 1 stoichiometric complex (Figure 5A, Lane 1). ","type":"Results"},{"text":"Lane 1 corresponds to the first peak, identified as a complex of R-domain and helicase RhlB.","type":"Figure"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":628,"end":843,"reference_id":"15236960","reference_source":"pmid","reference_html":"Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. <i> Callaghan AJ, Aurikko JP, Ilag LL, Günter Grossmann J, Chandran V, Kühnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF. </i> J Mol Biol, 2004","date":"2023-02-23T13:18:24.766Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0032781","term_name":"positive regulation of ATP-dependent activity","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IDA","region_id":"DP00207r020","statement":[{"text":"In comparison with the ATPase activity of the isolated helicase, the purified helicase RhlB–R-domain complex is 25-fold more active. This suggests that the protein–protein interaction is stimulatory, in agreement with the findings reported by Vanzo et al.","type":"Results"}],"term_comment":"","term_def":"\"Any process that activates or increases the rate of an ATP-dependent activity.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":628,"end":843,"reference_id":"15236960","reference_source":"pmid","reference_html":"Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. <i> Callaghan AJ, Aurikko JP, Ilag LL, Günter Grossmann J, Chandran V, Kühnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF. </i> J Mol Biol, 2004","date":"2023-02-07T16:51:09.686Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P0A8J8","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00207r021","statement":[{"text":"Series B corresponds to the R-domain with a measured mass of 29,044(±41) Da (theoretical mass of 28,822 Da) and the charge state series C with a mass of 76,763(±13) Da corresponds to one R-domain bound to one helicase RhlB (theoretical mass 75,817 Da) (Figure 6A).","type":"Results"},{"text":"Tandem mass spectrometry (MS/MS) of the complex ion (C+19) confirmed the composition of the species to be that of R-domain and helicase RhlB (Figure 6B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":628,"end":843,"reference_id":"15236960","reference_source":"pmid","reference_html":"Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. <i> Callaghan AJ, Aurikko JP, Ilag LL, Günter Grossmann J, Chandran V, Kühnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF. </i> J Mol Biol, 2004","date":"2023-02-07T16:52:53.625Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00207r022","statement":[{"text":"Circular dichroism indicates that the R-domain is predominantly unstructured and that the R-domain–helicase RhlB complex has the same secondary structural composition as the helicase RhlB alone. Thus, it seems that the R-domain does not undergo appreciable folding on interaction with the helicase, despite the apparent avidity of the complex.","type":"Results"}]},{"start":580,"end":1038,"reference_id":"15236960","reference_source":"pmid","reference_html":"Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. <i> Callaghan AJ, Aurikko JP, Ilag LL, Günter Grossmann J, Chandran V, Kühnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF. </i> J Mol Biol, 2004","date":"2023-02-07T17:00:46.450Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00207r023","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0A6P9"}],"statement":[{"text":"Based on its elution volume from the S200 column, the apparent molecular mass of the complex was 103 kDa, which is nearly three times the expected size for an enolase dimer with two CTD proteins bound. The apparently large mass of the complex is most likely due to the anomalous volume of the predominantly unstructured CTD. ","type":"Results"}]},{"start":816,"end":1038,"reference_id":"15236960","reference_source":"pmid","reference_html":"Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. <i> Callaghan AJ, Aurikko JP, Ilag LL, Günter Grossmann J, Chandran V, Kühnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF. </i> J Mol Biol, 2004","date":"2023-02-07T17:04:28.705Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P0A6P9","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00207r024","statement":[{"text":"The native-CTD–enolase complex is very sensitive to partial proteolysis by protease K. It is less sensitive to partial digestion by chymotrypsin (Figure 7B), and this enabled identification of the minimal binding fragment of native-CTD to enolase by native PAGE and N-terminal sequencing analysis. The fragment bound to enolase was found to start at residue 816 of RNase E (Figure 7C), and from its molecular mass was presumed to extend roughly to residue 1038. ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":833,"end":850,"reference_id":"15236960","reference_source":"pmid","reference_html":"Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. <i> Callaghan AJ, Aurikko JP, Ilag LL, Günter Grossmann J, Chandran V, Kühnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF. </i> J Mol Biol, 2004","date":"2023-02-07T17:07:01.190Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P0A6P9","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00207r025","statement":[{"text":"Series B with a molecular mass of 93,158(±14) Da, corresponding to an enolase dimer with one peptide C bound, was the predominant species observed (theoretical mass of 93,089 Da). In addition we observe a charge state series C with a mass of 95,195(±12) Da, corresponding to one enolase dimer bound to two peptide C molecules (theoretical mass 95,131 Da). MS/MS analysis of the B+19 complex ion confirmed the composition of the species to be that of an enolase dimer bound to peptide C (Figure 8B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1021,"end":1061,"reference_id":"15236960","reference_source":"pmid","reference_html":"Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. <i> Callaghan AJ, Aurikko JP, Ilag LL, Günter Grossmann J, Chandran V, Kühnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF. </i> J Mol Biol, 2004","date":"2023-02-07T17:11:41.291Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P05055","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00207r026","statement":[{"text":"Addition of Peptide D to PNPase in stoichiometric excess gave evidence for a charge series corresponding to a species with a molecular mass of 497,442(±15) Da, (Figure 9, red trace, series D). This is consistent with a dimer of PNPase trimers with six peptide D molecules bound, which equates to one peptide D per PNPase monomer (theoretical mass of 496,950 Da). Also, we observed a trimer of PNPase with three and four peptide D molecules bound (Figure 9, series B and C respectively). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_P21513","date":"2016-09-07T15:08:47.000Z","acc":"P21513","name":"Ribonuclease E","length":1061,"organism":"Escherichia coli (strain K12)","dataset":["RNA-binding proteins"],"UniParc":"UPI000016F18C","genes":[{"name":{"value":"rne","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00970","url":"https://hamap.expasy.org/unirule/MF_00970"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"2011493","url":"http://www.ncbi.nlm.nih.gov/pubmed/2011493","alternativeUrl":"https://europepmc.org/abstract/MED/2011493"}}]},"synonyms":[{"value":"ams","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"1704367","url":"http://www.ncbi.nlm.nih.gov/pubmed/1704367","alternativeUrl":"https://europepmc.org/abstract/MED/1704367"}}]},{"value":"hmp1"}],"olnNames":[{"value":"b1084"},{"value":"JW1071"}]}],"alphafold_very_low_content":0.40339302544769085,"disorder_content":0.5315739868049011,"disprot_consensus":{"full":[{"start":498,"end":815,"type":"D"},{"start":816,"end":850,"type":"T"},{"start":851,"end":1061,"type":"D"}],"Structural state":[{"start":498,"end":1061,"type":"D"}],"Molecular function":[{"start":498,"end":1061,"type":"F"}],"Structural transition":[{"start":816,"end":850,"type":"T"}],"Biological process":[{"start":498,"end":1061,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00865","name":"Osteopontin","start":21,"end":314}]},"uniref50":"UniRef50_P10451","sequence":"MRIAVICFCLLGITCAIPVKQADSGSSEEKQLYNKYPDAVATWLNPDPSQKQNLLAPQNAVSSEETNDFKQETLPSKSNESHDHMDDMDDEDDDDHVDSQDSIDSNDSDDVDDTDDSHQSDESHHSDESDELVTDFPTDLPATEVFTPVVPTVDTYDGRGDSVVYGLRSKSKKFRRPDIQYPDATDEDITSHMESEELNGAYKAIPVAQDLNAPSDWDSRGKDSYETSQLDDQSAETHSHKQSRLYKRKANDESNEHSDVIDSQELSKVSREFHSHEFHSHEDMLVVDPKSKEEDKHLKFRISHELDSASSEVN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P10451","disprot_id":"DP00214","ncbi_taxon_id":9606,"regions_counter":20,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":314,"region_id":"DP00214r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin. <i> Fisher LW, Torchia DA, Fohr B, Young MF, Fedarko NS. </i> Biochem Biophys Res Commun, 2001","term_id":"IDPO:0000002","curator_id":"rpancsa","start":1,"term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"11162539","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","statement":[{"text":"The narrow spread of the peptide backbone amide NH peaks (7.8–8.6 ppm) and the side chain NH peaks (6.6–7.4 ppm) are indicative of a lack of ordered structures over the NMR time scale.","type":"Results"},{"text":"Furthermore, the average proton T2 relaxation times for both of these molecules were on the\norder of 60 ms. This is fully consistent with the two proteins being extended and flexible in solution.","type":"Results"},{"text":"Therefore, both BSP and OPN, when purified and isolated in solution, are flexible along their entire length and have no significant regions that persist in a single structural environment for more than a few milliseconds.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T16:06:04.479Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":314,"reference_id":"11162539","reference_source":"pmid","reference_html":"Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin. <i> Fisher LW, Torchia DA, Fohr B, Young MF, Fedarko NS. </i> Biochem Biophys Res Commun, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006309","ec_ontology":"ECO","ec_name":"competitive binding evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00214r006","statement":[{"text":"Furthermore, our current supply of antisera against OPN also appears to be unable to bind to the OPN when complexed with Factor H (data not shown). This all suggests that essentially\nthe full length of this SIBLING is tightly bound to either Factor H or to HA and that specific portions of OPN can bind to either of two independent cell surface receptors or to additional regions of Factor H.","type":"Results"}],"interaction_partner":[{"db":"UniProt","id":"P08603","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T16:06:20.300Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":314,"reference_id":"11162539","reference_source":"pmid","reference_html":"Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin. <i> Fisher LW, Torchia DA, Fohr B, Young MF, Fedarko NS. </i> Biochem Biophys Res Commun, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P16070","partner_start":null,"partner_end":null}],"region_id":"DP00214r007","statement":[{"text":"In addition to binding to integrins, OPN has been reported to be able to bind to CD44.","type":"Introduction"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T16:06:22.292Z"},"term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":314,"reference_id":"8560266","reference_source":"pmid","reference_html":"Receptor-ligand interaction between CD44 and osteopontin (Eta-1). <i> Weber GF, Ashkar S, Glimcher MJ, Cantor H. </i> Science, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006309","ec_ontology":"ECO","ec_name":"competitive binding evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P16070","partner_start":null,"partner_end":null}],"region_id":"DP00214r008","statement":[{"text":"The binding of biotin-labeled Opn to A31.C1 CD44 transfectants was dependent on dose, was specific, and was inhibited by an antibody to CD44 but not by an irrelevant antibody.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T16:06:23.265Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":314,"reference_id":"8560266","reference_source":"pmid","reference_html":"Receptor-ligand interaction between CD44 and osteopontin (Eta-1). <i> Weber GF, Ashkar S, Glimcher MJ, Cantor H. </i> Science, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006077","ec_ontology":"ECO","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P16070","partner_start":null,"partner_end":null}],"region_id":"DP00214r009","statement":[{"text":"We confirmed this by analyzing proteins that bound to recombinant glutathione-S- transferase (GST)-Opn (which lacks glycosyl moieties, including HA)\nimmobilized on Sepharose 4B. Coomassie-stained electrophoresis gels of the desalted eluate showed comigration of the most prominent band with CD44 purified from the same cell line.","type":"Article"},{"text":"Depletion of CD44 from cell lysates with antibody removed this band from the material eluted from the GST-Opn columns.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T16:06:24.415Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":314,"reference_id":"10747989","reference_source":"pmid","reference_html":"Factor H binding to bone sialoprotein and osteopontin enables tumor cell evasion of complement-mediated attack. <i> Fedarko NS, Fohr B, Robey PG, Young MF, Fisher LW. </i> J Biol Chem, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P08603","partner_start":null,"partner_end":null}],"region_id":"DP00214r010","statement":[{"text":"The addition of tween  BSP  or  OPN  and  Factor  H  can  be  readily  studied  by intrinsic steady state fluorescence. Titration of purified human complement Factor H with rBSPor rOPN was followed by excitation at 295 nm and monitoring emission  between  300  and  450  nm.  The  emission  profile  of Factor H alone yields a peak at 347 nm. The addition of rBSP or rOPN in nanomolar increments causes a relative fluorescent  intensity  quenching.  Conversion  of  the  fluorescent intensity  titration  into  a  binding  curve  by  determining  the fraction of binding sites occupied as the fractional change influorescence quenching at 347 nm yields a saturable binding curves. By steady state fluorescence, the binding of BSP  and  OPN  by  Factor  H  are  saturable  and  possess  a  1:1 stoichiometry, have binding constants in the nanomolar range, given the serum concentration of Factor H (0.5 mg/ml), virtually all BSP and OPN in serum will be complexed with Factor H.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T16:06:25.726Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":314,"reference_id":"10747989","reference_source":"pmid","reference_html":"Factor H binding to bone sialoprotein and osteopontin enables tumor cell evasion of complement-mediated attack. <i> Fedarko NS, Fohr B, Robey PG, Young MF, Fisher LW. </i> J Biol Chem, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006309","ec_ontology":"ECO","ec_name":"competitive binding evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P16070","partner_start":null,"partner_end":null}],"region_id":"DP00214r011","statement":[{"text":"Pretreatment of MEL cells with hyaluronan, anatural  ligand  for  CD44,  as  well  as  with  an anti-CD44 antibody also reduced the protective effect of added rOPN.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T16:06:27.101Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":158,"end":162,"reference_id":"10747989","reference_source":"pmid","reference_html":"Factor H binding to bone sialoprotein and osteopontin enables tumor cell evasion of complement-mediated attack. <i> Fedarko NS, Fohr B, Robey PG, Young MF, Fisher LW. </i> J Biol Chem, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006309","ec_ontology":"ECO","ec_name":"competitive binding evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P08648","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P05106","partner_start":null,"partner_end":null}],"region_id":"DP00214r012","statement":[{"text":"For OPN, pretreatment with GRGDS peptide or the aVb3 antibody reduced cell survival, although the magnitude of reduction was not as great as that seen for BSP.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T16:06:28.429Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":314,"reference_id":"24928493","reference_source":"pmid","reference_html":"Osteopontin binds multiple calcium ions with high affinity and independently of phosphorylation status. <i> Kläning E, Christensen B, Sørensen ES, Vorup-Jensen T, Jensen JK. </i> Bone, 2014","date":"2022-03-08T15:11:24.368Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","released":"2022_03","version":4,"region_id":"DP00214r013","statement":[{"text":"Human milk OPN binds Ca2+with high affinity, and with similar strong exothermicsignal which reaches full saturation at ~90μM.","type":"Results"},{"text":"In separate experiments, a strong endothermic signal for human OPN interaction with Mg2+ was observed.","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"ChEBI","id":"29108","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-18T15:01:44.179Z"}},{"start":17,"end":314,"reference_id":"25616494","reference_source":"pmid","reference_html":"(1)H, (15)N, (13)C resonance assignment of human osteopontin. <i> Platzer G, Żerko S, Saxena S, Koźmiński W, Konrat R. </i> Biomol NMR Assign, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00214r014","statement":[{"text":"As expected for an intrinsically disordered protein the proton chemical shift dispersion of the 1H–15N HSQC spectrum shows a narrow profile with chemical shift values close to random coil values.","type":"Article"}],"cross_refs":[{"db":"BMRB","id":"19999"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T16:06:07.661Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":17,"end":314,"reference_id":"33876640","reference_source":"pmid","reference_html":"Hyperphosphorylation of Human Osteopontin and Its Impact on Structural Dynamics and Molecular Recognition. <i> Mateos B, Holzinger J, Conrad-Billroth C, Platzer G, Żerko S, Sealey-Cardona M, Anrather D, Koźmiński W, Konrat R. </i> Biochemistry, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00214r015","statement":[{"text":"The total sequence coverage of the MS/MS experiments is 68.5%, and 28 phosphorylation events are identified.","type":"Results"},{"text":"There were so many phosphosites identified that basically the whole protein is hyperphosphorylated.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T16:06:34.578Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":17,"end":314,"reference_id":"33876640","reference_source":"pmid","reference_html":"Hyperphosphorylation of Human Osteopontin and Its Impact on Structural Dynamics and Molecular Recognition. <i> Mateos B, Holzinger J, Conrad-Billroth C, Platzer G, Żerko S, Sealey-Cardona M, Anrather D, Koźmiński W, Konrat R. </i> Biochemistry, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00214r016","statement":[{"text":"Twentyeight phosphorylation events are identified on the basis of the 1HN downfield shifts.","type":"Results"},{"text":"There were so many phosphosites identified that basically the whole protein is hyperphosphorylated.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T16:06:35.381Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":17,"end":314,"reference_id":"33876640","reference_source":"pmid","reference_html":"Hyperphosphorylation of Human Osteopontin and Its Impact on Structural Dynamics and Molecular Recognition. <i> Mateos B, Holzinger J, Conrad-Billroth C, Platzer G, Żerko S, Sealey-Cardona M, Anrather D, Koźmiński W, Konrat R. </i> Biochemistry, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"BMRB","id":"50447"}],"region_id":"DP00214r017","statement":[{"text":"1H–15N HSQC NMR spectra of OPN before (black) and after (red) phosphorylation by Fam20C.","type":"Figure"},{"text":"Very narrow chemical shift dispersion is evident from the figure for both the unphosphorylated and phosphorylated osteopontin.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T16:06:15.720Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":85,"end":116,"reference_id":"33914399","reference_source":"pmid","reference_html":"Binding Mode Characterization of Osteopontin on Hydroxyapatite by Solution NMR Spectroscopy. <i> Holzinger J, Kotisch H, Richter KW, Konrat R. </i> Chembiochem, 2021","date":"2022-03-08T15:11:42.680Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":4,"region_id":"DP00214r018","statement":[{"text":"OPN shows Ca2+-binding mainly in the aspartate-rich regime (poly-D regime; 85–116), accompanied by less pronounced perturbations in the other negatively charged regions 70–79, 130–136, 178–188 and 245–260, revealing binding affinities in the lower millimolar range (4–16(3) mM).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"ChEBI","id":"29108","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-18T15:01:38.043Z"}},{"start":85,"end":116,"reference_id":"33914399","reference_source":"pmid","reference_html":"Binding Mode Characterization of Osteopontin on Hydroxyapatite by Solution NMR Spectroscopy. <i> Holzinger J, Kotisch H, Richter KW, Konrat R. </i> Chembiochem, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0036094","term_name":"small molecule binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00214r019","statement":[{"text":"Similar to the binding to Ca2+ cations, both OPN and OPNp show CSPs mainly in the negatively charged regions upon the interaction with HAP surfaces. Again, OPN binds to HAP predominantly in the poly-D regime (residues 85 ff.).","type":"Results"},{"text":"CSP stands for chemical shift perturbation, HAP stands for hydroxyapatite. The poly-D regime was already stated to be between residues 85 and 116 when the bindig of Ca2+ ions was investigated.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T16:06:33.963Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":314,"reference_id":"11162539","reference_source":"pmid","reference_html":"Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin. <i> Fisher LW, Torchia DA, Fohr B, Young MF, Fedarko NS. </i> Biochem Biophys Res Commun, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","released":"2022_03","version":3,"region_id":"DP00214r020","statement":[{"text":"It has been proposed that osteoclasts use OPN to bridge between the integrins on the cell surface and the mineral phase during resorption of bone matrix. We have shown that Factor H also binds to OPN already complexed to either avb3 integrin or CD44 and this complex can stop the alternate complement lysis pathway. ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T20:51:27.117Z"},"term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P10451","date":"2016-08-31T12:00:49.000Z","acc":"P10451","name":"Osteopontin","length":314,"organism":"Homo sapiens","dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000000E0B","genes":[{"name":{"value":"SPP1"},"synonyms":[{"value":"BNSP"},{"value":"OPN"}],"orfNames":[{"value":"PSEC0156"}]}],"alphafold_very_low_content":0.3821656050955414,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":314,"type":"D"}],"Structural state":[{"start":1,"end":314,"type":"D"}],"Molecular function":[{"start":1,"end":314,"type":"F"}],"Disorder function":[{"start":17,"end":314,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03066","name":"Nucleoplasmin/nucleophosmin domain","start":17,"end":120}],"gene3D":[{"start":1,"end":124,"id":"2.60.120.340","name":"Nucleoplasmin core domain"}]},"uniref50":"UniRef50_P05221","sequence":"MASTVSNTSKLEKPVSLIWGCELNEQDKTFEFKVEDDEEKCEHQLALRTVCLGDKAKDEFNIVEIVTQEEGAEKSVPIATLKPSILPMATMVGIELTPPVTFRLKAGSGPLYISGQHVAMEEDYSWAEEEDEGEAEGEEEEEEEEDQESPPKAVKRPAATKKAGQAKKKKLDKEDESSEEDSPTKKGKGAGRGRKPAAKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Amphibia","Batrachia","Anura","Pipoidea","Pipidae","Xenopodinae","Xenopus","Xenopus"],"uniref90":"UniRef90_P05221","disprot_id":"DP00217","ncbi_taxon_id":8355,"regions_counter":6,"creator":"gminervini","regions":[{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":171,"term_name":"importin-alpha family protein binding","start":153,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"10745017","version":4,"reference_html":"Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin alpha. <i> Conti E, Kuriyan J. </i> Structure, 2000","date":"2023-02-07T19:38:34.530Z","term_id":"GO:0061676","ec_id":"ECO:0006220","region_id":"DP00217r002","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a member of the importin-alpha family.\" [PMID:15350979, PMID:17170104, PMID:23734157]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q02821","operator":null,"partner_start":null,"partner_end":null}],"statement":[{"text":"The bipartite NLS (154VKRPAATKKAGQAKKKKLD172) of Xenopus nucleoplasmin binds along the surface groove of Kapα50 with the upstream basic cluster (residues 155–156) at the small site and the downstream basic cluster (residues 167–170) at the large site.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"1EE5"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":200,"region_id":"DP00217r003","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Structural and functional properties of Escherichia coli-derived nucleoplasmin. A comparative study of recombinant and natural proteins. <i> Hierro A, Arizmendi JM, De Las Rivas J, Urbaneja MA, Prado A, Muga A. </i> Eur J Biochem, 2001","term_id":"IDPO:0000002","curator_id":"vnugnes","start":120,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"11248694","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-02-07T19:28:44.584Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The spectrum of the full-length protein (dotted line) displays a minimun at 198 nm, that has been related with nonregular conformations. In contrast, that of the truncated protein is located at 213 nm, being the ellipticity value at 198 nm positive (solid line).","type":"Results"}]},{"start":1,"end":10,"reference_id":"11684019","reference_source":"pmid","reference_html":"The crystal structure of nucleoplasmin-core: implications for histone binding and nucleosome assembly. <i> Dutta S, Akey IV, Dingwall C, Hartman KL, Laue T, Nolte RT, Head JF, Akey CW. </i> Mol Cell, 2001","date":"2023-02-07T19:45:57.446Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00217r005","statement":[{"text":"A truncated N-terminal domain of Np was produced by proteolysis","type":"Methods"},{"text":"N-terminal sequencing and mass spectrometry indicated that native Np-core extended from Lys10-Tyr124.","type":"Methods"}]},{"start":125,"end":200,"reference_id":"11684019","reference_source":"pmid","reference_html":"The crystal structure of nucleoplasmin-core: implications for histone binding and nucleosome assembly. <i> Dutta S, Akey IV, Dingwall C, Hartman KL, Laue T, Nolte RT, Head JF, Akey CW. </i> Mol Cell, 2001","date":"2023-02-07T19:46:11.064Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00217r006","statement":[{"text":"A truncated N-terminal domain of Np was produced by proteolysis","type":"Methods"},{"text":"N-terminal sequencing and mass spectrometry indicated that native Np-core extended from Lys10-Tyr124.","type":"Methods"}]}],"released":"2016_10","uniref100":"UniRef100_P05221","date":"2016-08-24T17:08:05.000Z","acc":"P05221","name":"Nucleoplasmin","length":200,"organism":"Xenopus laevis","dataset":[],"UniParc":"UPI0000130A30","genes":[],"alphafold_very_low_content":0.19,"disorder_content":0.455,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"},{"start":120,"end":200,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":120,"end":200,"type":"D"}],"Molecular function":[{"start":153,"end":171,"type":"F"}]}},{"features":{"pfam":[{"id":"PF07491","name":"Protein phosphatase inhibitor","start":30,"end":80}]},"uniref50":"UniRef50_O60927","sequence":"MAEAGAGLSETVTETTVTVTTEPENRSLTIKLRKRKPEKKVEWTSDTVDNEHMGRRSSKCCCIYEKPRAFGESSTESDEEEEEGCGHTHCVRGHRKGRRRATLGPTPTTPPQPPDPSQPPPGPMQH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O60927","disprot_id":"DP00219","ncbi_taxon_id":9606,"regions_counter":6,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":126,"region_id":"DP00219r001","released":"2023_06","ec_id":"ECO:0007689","reference_html":"Identification and characterization of the human HCG V gene product as a novel inhibitor of protein phosphatase-1. <i> Zhang J, Zhang L, Zhao S, Lee EY. </i> Biochemistry, 1998","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"9843442","version":3,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2023-02-09T13:41:14.781Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"The recombinant protein behaved anomalously on SDS−PAGE with a relative molecular mass of 23 kDa, much higher than its estimated molecular mass of 14 kDa (Figure 4). This may be due to the high content of hydrophilic amino acids in the polypeptide, which could result in a lower binding of SDS and a lower motility on SDS−PAGE.","type":"Results"}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":126,"term_name":"protein phosphatase inhibitor activity","start":1,"ec_name":"radioisotope quantification assay evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"9843442","version":4,"reference_html":"Identification and characterization of the human HCG V gene product as a novel inhibitor of protein phosphatase-1. <i> Zhang J, Zhang L, Zhao S, Lee EY. </i> Biochemistry, 1998","date":"2023-02-09T13:48:41.663Z","term_id":"GO:0004864","ec_id":"ECO:0007846","region_id":"DP00219r002","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binds to and stops, prevents or reduces the activity of a protein phosphatase, an enzyme that hydrolyzes phosphate groups from phosphorylated proteins.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P01099","operator":null,"partner_start":null,"partner_end":null}],"statement":[{"text":"Both forms of PP1 are potently inhibited by inhibitor-3 in the nanomolar range. However the recombinant Co(II)-PP1 is inhibited ca. 20-fold more strongly than the Mn2+-dependent PP1 (Figure 6). The IC50s for Co(II)-PP1 and Mn2+ PP1 were found to be 0.3 and 6 nM, respectively (mean of two determinations with different preparations of I-3 and PP1).","type":"Results"}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":126,"term_name":"phosphatase binding","start":14,"ec_name":"yeast 2-hybrid evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"9843442","version":4,"reference_html":"Identification and characterization of the human HCG V gene product as a novel inhibitor of protein phosphatase-1. <i> Zhang J, Zhang L, Zhao S, Lee EY. </i> Biochemistry, 1998","date":"2023-02-09T13:55:30.077Z","term_id":"GO:0019902","ec_id":"ECO:0005805","region_id":"DP00219r003","curator_orcid":"0000-0001-8399-7907","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a phosphatase.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"statement":[{"text":" A human brain cDNA expression library expressing the proteins fused with the GAL4 activation domain was used for the screening of PP1-binding proteins by the yeast two-hybrid system (Experimental Procedures).","type":"Results"},{"text":"Clone 45 was completely sequenced and found to consist of 768 base pairs that were identical to the cDNA for HCG V, except for a 138 bp deletion at the 5‘ end, such that it starts at amino acid 14 of the encoded sequence, and a 614 bp deletion in the 3‘-noncoding region (662−1275) (Figure 1).","type":"Results"}],"interaction_partner":[{"db":"UniProt","id":"P01099","operator":"and","partner_start":null,"partner_end":null}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":126,"region_id":"DP00219r004","released":"2023_06","ec_id":"ECO:0001184","reference_html":"Identification and characterization of the human HCG V gene product as a novel inhibitor of protein phosphatase-1. <i> Zhang J, Zhang L, Zhao S, Lee EY. </i> Biochemistry, 1998","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"9843442","version":3,"ec_name":"gel-filtration evidence used in manual assertion","date":"2023-02-09T13:58:11.571Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The protein also behaved anomalously on HPLC gel filtration, with an apparent molecular weight of 55 000 (Figure 5).","type":"Results"}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":126,"term_name":"phosphatase binding","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"9843442","version":4,"reference_html":"Identification and characterization of the human HCG V gene product as a novel inhibitor of protein phosphatase-1. <i> Zhang J, Zhang L, Zhao S, Lee EY. </i> Biochemistry, 1998","date":"2023-02-09T13:53:28.966Z","term_id":"GO:0019902","ec_id":"ECO:0007680","region_id":"DP00219r006","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a phosphatase.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P01099","operator":null,"partner_start":null,"partner_end":null}],"statement":[{"text":"To confirm that the clone 45/HCG V protein binds to PP1, the crude bacterial lysate expressing the GST−HCG V fusion protein was chromatographed on a PP1−Sepharose column. The results are shown in Figure 3. The 43 kDa protein was bound to PP1−Sepharose while the GST protein (29 kDa) did not bind to the column.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_O60927","date":"2016-08-31T12:04:39.000Z","acc":"O60927","name":"E3 ubiquitin-protein ligase PPP1R11","length":126,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000000D734","genes":[{"name":{"value":"PPP1R11"},"synonyms":[{"value":"HCGV"},{"value":"TCTE5"}]}],"alphafold_very_low_content":0.10317460317460317,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":126,"type":"D"}],"Structural state":[{"start":1,"end":126,"type":"D"}],"Molecular function":[{"start":1,"end":126,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00335","name":"Tetraspanin family","start":19,"end":281}],"gene3D":[{"start":122,"end":232,"id":"1.10.1450.10","name":"Tetraspanin"}]},"uniref50":"UniRef50_P23942","sequence":"MALLKVKFDQKKRVKLAQGLWLMNWFSVLAGIIIFGLGLFLKIELRKRSDVMNNSESHFVPNSLIGVGVLSCVFNSLAGKICYDALDPAKYAKWKPWLKPYLAVCVLFNVVLFLVALCCFLLRGSLESTLAHGLKNGMKFYRDTDTPGRCFMKKTIDMLQIEFKCCGNNGFRDWFEIQWISNRYLDFSSKEVKDRIKSNVDGRYLVDGVPFSCCNPNSPRPCIQYQLTNNSAHYSYDHQTEELNLWLRGCRAALLSYYSNLMNTTGAVTLLVWLFEVTITVGLRYLHTALEGMANPEDPECESEGWLLEKSVPETWKAFLESVKKLGKGNQVEAEGEDAGQAPAAG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P23942","disprot_id":"DP00220","ncbi_taxon_id":9913,"regions_counter":5,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":346,"region_id":"DP00220r001","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Predicted and measured disorder in peripherin/rds, a retinal tetraspanin. <i> Ritter LM, Arakawa T, Goldberg AF. </i> Protein Pept Lett, 2005","term_id":"IDPO:0000002","curator_id":"esalladini","start":284,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"16522184","version":3,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","uniprot_changed":true,"curator_orcid":"0000-0002-5152-5953","statement":[{"text":"These findings demonstrate that the C-terminus is relatively accessible to limited proteolysis and are consistent with the extensive regions of disorder predicted by structure modeling.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-11-14T13:25:41.741Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":346,"region_id":"DP00220r002","released":"2022_03","ec_id":"ECO:0001249","reference_html":"Predicted and measured disorder in peripherin/rds, a retinal tetraspanin. <i> Ritter LM, Arakawa T, Goldberg AF. </i> Protein Pept Lett, 2005","term_id":"IDPO:0000002","curator_id":"esalladini","start":284,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"16522184","version":3,"ec_name":"fluorescence evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","uniprot_changed":true,"curator_orcid":"0000-0002-5152-5953","statement":[{"text":"We measured intrinsic tryptophan fluorescence of CTER under a variety of solution conditions and found this to be so. Fig. 6A (solid line) shows an emission spectrum of CTER, using an excitation wavelength of 295 nm. The characteristic broad peak at 348 nm suggested to us that the two tryptophans contained within this domain were rather solvent exposed, as had been predicted by the SEC and AUC results.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-11-14T13:25:48.114Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":346,"region_id":"DP00220r003","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Predicted and measured disorder in peripherin/rds, a retinal tetraspanin. <i> Ritter LM, Arakawa T, Goldberg AF. </i> Protein Pept Lett, 2005","term_id":"IDPO:0000002","curator_id":"esalladini","start":284,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"16522184","version":3,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","uniprot_changed":true,"curator_orcid":"0000-0002-5152-5953","statement":[{"text":"The rigorous determination that CTER is monomeric (by AUC) combined with a substantially retarded hydrodynamic elution position (observed by SEC) suggests that CTER possesses an extended conformation and may have a weak affinity for the SEC matrix.","type":"Results"},{"text":"Overall these results suggest that CTER structure, like that in other disordered domains is not affected by macromolecular crowding effects [22], but is appreciably increased in the presence of a hydrophobic environment.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-11-14T13:25:56.749Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":346,"region_id":"DP00220r004","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Predicted and measured disorder in peripherin/rds, a retinal tetraspanin. <i> Ritter LM, Arakawa T, Goldberg AF. </i> Protein Pept Lett, 2005","term_id":"IDPO:0000002","curator_id":"esalladini","start":284,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"16522184","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","uniprot_changed":true,"curator_orcid":"0000-0002-5152-5953","statement":[{"text":"As expected from SEC, AUC, intrinsic tryptophan fluorescence and previous CD measurements, the spectra also indicate strong contributions from random coil elements (estimated here at ~36%).","type":"Results"},{"text":"Overall these results suggest that CTER structure, like that in other disordered domains is not affected by macromolecular crowding effects [22], but is appreciably increased in the presence of a hydrophobic environment.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-11-14T13:25:59.824Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":346,"region_id":"DP00220r005","released":"2022_03","ec_id":"ECO:0006275","reference_html":"Predicted and measured disorder in peripherin/rds, a retinal tetraspanin. <i> Ritter LM, Arakawa T, Goldberg AF. </i> Protein Pept Lett, 2005","term_id":"IDPO:0000002","curator_id":"esalladini","start":284,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"16522184","version":3,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","uniprot_changed":true,"curator_orcid":"0000-0002-5152-5953","statement":[{"text":"The rigorous determination that CTER is monomeric (by AUC) combined with a substantially retarded hydrodynamic elution position (observed by SEC) suggests that CTER possesses an extended conformation and may have a weak affinity for the SEC matrix.","type":"Results"},{"text":"Overall these results suggest that CTER structure, like that in other disordered domains is not affected by macromolecular crowding effects [22], but is appreciably increased in the presence of a hydrophobic environment.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-11-14T13:26:01.914Z"}}],"released":"2016_10","uniref100":"UniRef100_P17810","date":"2016-08-11T17:44:05.000Z","acc":"P17810","name":"Peripherin-2","length":346,"organism":"Bos taurus","dataset":[],"uniparc":"UPI00001334A0","UniParc":"UPI00001334A0","genes":[{"name":{"value":"PRPH2"},"synonyms":[{"value":"RDS"}]}],"alphafold_very_low_content":0.05202312138728324,"disorder_content":0.18208092485549132,"disprot_consensus":{"full":[{"start":284,"end":346,"type":"D"}],"Structural state":[{"start":284,"end":346,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00638","name":"RanBP1 domain","start":598,"end":718},{"id":"PF08911","name":"NUP50 (Nucleoporin 50 kDa)","start":2,"end":72}],"gene3D":[{"start":503,"end":716,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"}]},"uniref50":"UniRef50_P32499","sequence":"MAKRVADAQIQRETYDSNESDDDVTPSTKVASSAVMNRRKIAMPKRRMAFKPFGSAKSDETKQASSFSFLNRADGTGEAQVDNSPTTESNSRLKALNLQFKAKVDDLVLGKPLADLRPLFTRYELYIKNILEAPVKSIENPTQTKGNDAKPAKVEDVQKSSDSSSEDEVKVEGPKFTIDAKPPISDSVFSFGPKKENRKKDESDSENDIEIKGPEFKFSGTVSSDVFKLNPSTDKNEKKTETNAKPFSFSSATSTTEQTKSKNPLSLTEATKTNVDNNSKAEASFTFGTKHAADSQNNKPSFVFGQAAAKPSLEKSSFTFGSTTIEKKNDENSTSNSKPEKSSDSNDSNPSFSFSIPSKNTPDASKPSFSFGVPNSSKNETSKPVFSFGAATPSAKEASQEDDNNNVEKPSSKPAFNLISNAGTEKEKESKKDSKPAFSFGISNGSESKDSDKPSLPSAVDGENDKKEATKPAFSFGINTNTTKTADTKAPTFTFGSSALADNKEDVKKPFSFGTSQPNNTPSFSFGKTTANLPANSSTSPAPSIPSTGFKFSLPFEQKGSQTTTNDSKEESTTEATGNESQDATKVDATPEESKPINLQNGEEDEVALFSQKAKLMTFNAETKSYDSRGVGEMKLLKKKDDPSKVRLLCRSDGMGNVLLNATVVDSFKYEPLAPGNDNLIKAPTVAADGKLVTYIVKFKQKEEGRSFTKAIEDAKKEMK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P32499","disprot_id":"DP00222","ncbi_taxon_id":559292,"regions_counter":17,"creator":"ftonello","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":720,"region_id":"DP00222r001","reference_id":"12065587","start":1,"ec_id":"ECO:0006204","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Analyses of the Nup2p structure by far-UV circular dichroism (CD) spectroscopy, Fourier transform infrared (FTIR) spectroscopy, protease sensitivity, gel filtration, and sedimentation velocity experiments indicate that Nup2p is a \"natively unfolded protein,\" belonging to a class of proteins that exhibit little secondary structure, high flexibility, and low compactness.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"reference_html":"The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein. <i> Denning DP, Uversky V, Patel SS, Fink AL, Rexach M. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":720,"region_id":"DP00222r004","reference_id":"12065587","start":1,"ec_id":"ECO:0006228","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Analyses of the Nup2p structure by far-UV circular dichroism (CD) spectroscopy, Fourier transform infrared (FTIR) spectroscopy, protease sensitivity, gel filtration, and sedimentation velocity experiments indicate that Nup2p is a \"natively unfolded protein,\" belonging to a class of proteins that exhibit little secondary structure, high flexibility, and low compactness.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","version":3,"reference_html":"The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein. <i> Denning DP, Uversky V, Patel SS, Fink AL, Rexach M. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":720,"region_id":"DP00222r007","reference_id":"12065587","start":1,"ec_id":"ECO:0007691","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Analyses of the Nup2p structure by far-UV circular dichroism (CD) spectroscopy, Fourier transform infrared (FTIR) spectroscopy, protease sensitivity, gel filtration, and sedimentation velocity experiments indicate that Nup2p is a \"natively unfolded protein,\" belonging to a class of proteins that exhibit little secondary structure, high flexibility, and low compactness.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cleavage assay evidence used in manual assertion","version":3,"reference_html":"The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein. <i> Denning DP, Uversky V, Patel SS, Fink AL, Rexach M. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":720,"region_id":"DP00222r010","reference_id":"12065587","start":1,"ec_id":"ECO:0007680","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Analyses of the Nup2p structure by far-UV circular dichroism (CD) spectroscopy, Fourier transform infrared (FTIR) spectroscopy, protease sensitivity, gel filtration, and sedimentation velocity experiments indicate that Nup2p is a \"natively unfolded protein,\" belonging to a class of proteins that exhibit little secondary structure, high flexibility, and low compactness.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"chromatography evidence used in manual assertion","version":3,"reference_html":"The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein. <i> Denning DP, Uversky V, Patel SS, Fink AL, Rexach M. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":720,"term_name":"protein binding","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"A second chromatography step was sufficient  to  obtain  purified  Nup2p  in  complex  with  its  binding partner  Kap60p  (data  not  shown).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"12065587","version":4,"reference_html":"The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein. <i> Denning DP, Uversky V, Patel SS, Fink AL, Rexach M. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007680","region_id":"DP00222r012","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":720,"region_id":"DP00222r013","reference_id":"12065587","start":1,"ec_id":"ECO:0006275","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Analyses of the Nup2p structure by far-UV circular dichroism (CD) spectroscopy, Fourier transform infrared (FTIR) spectroscopy, protease sensitivity, gel filtration, and sedimentation velocity experiments indicate that Nup2p is a \"natively unfolded protein,\" belonging to a class of proteins that exhibit little secondary structure, high flexibility, and low compactness.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"analytical ultracentrifugation evidence used in manual assertion","version":3,"reference_html":"The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein. <i> Denning DP, Uversky V, Patel SS, Fink AL, Rexach M. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":527,"term_name":"entropic chain","reference_id":"17418788","released":"2022_03","term_id":"IDPO:0000030","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","start":185,"term_ontology":"IDPO","version":3,"curator_name":"Federica Quaglia","ec_name":"deletion mutation phenotypic evidence used in manual assertion","statement":[{"text":"Our finding that FxFG domains of nuclear basket nups (Nup1, Nup2, and Nup60) are functional elements of the NPC permeability barrier (Figure 7B) supports the virtual-gate model because these FG domains behave as noncohesive filaments (Figures 2 and 5A).","type":"Discussion"},{"text":"Contrary to a central prediction made by the selective-phase model (i.e., that all FG domains of nups interact by virtue of their FG motifs), we demonstrated here in vivo and in vitro that some FG domains of nups are not cohesive, including the FxFG domains of Nsp1, Nup1, Nup2, and Nup60 and the SAFGxPSFG domain of Nup159 (Figure 2, Figure 3, Figure 4, Figure 5 and S4). This finding supports the notion that some FG domains of nups function exclusively as repulsive bristles due to Brownian motion, consistent with the virtual-gate model (Rout et al., 2000).","type":"Discussion"},{"text":"We also demonstrate that the FG domains of nups are structural components of the NPC permeability barrier in vivo.","type":"Introduction"},{"text":"The virtual-gate model proposes that FG domains are noncohesive, entropic bristles that repel the entry of non-karyophilic proteins into the NPC through Brownian motion.","type":"Figure"},{"text":"The integrity of the NPC permeability barrier was tested in ΔFG yeast lacking the GLFG domain of Nup116 or Nup100, the SAFGxPSFG domain of Nup42, or the FxFG domain of Nsp1, Nup60, Nup1, or Nup2.","type":"Introduction"}],"reference_html":"Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex. <i> Patel SS, Belmont BJ, Sante JM, Rexach MF. </i> Cell, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001175","region_id":"DP00222r016","ec_go":"IMP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":720,"term_name":"protein binding","reference_id":"11535617","released":"2022_03","term_id":"GO:0005515","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","start":562,"term_ontology":"GO","version":3,"curator_name":"Federica Quaglia","ec_name":"qualitative western immunoblotting evidence used in manual assertion","statement":[{"text":"We find that Nup60p binds to Nup2p and serves as a docking site for Kap95p-Kap60p heterodimers and Kap123p.","type":"Abstract"},{"text":"First, Nup60p binds to Nup2p in the absence of additional proteins (KD ∼396 nM) (Fig. 3, A and D) and in crude yeast extracts in the presence of thousands of competitor proteins (Figs. 1 B and 3 C).","type":"Discussion"},{"text":"Additional evidence suggests that the association between Nup2p and Nup60p at the NPC is dynamic. First, Nup2p fails to copurify with other Nups during the isolation of NPCs (Rout et al., 2000), implying that Nup2p dissociates readily from the NPC. Second, Nup2p–GFP accumulates in the nucleoplasm and cytoplasm of yeast lacking Nup60p (Fig. 2 A, middle), raising the possibility that Nup2p shuttles in and out of the nucleus and uses Nup60p as a rest-stop. Third, Nup2p can be tethered (indirectly) to a subset of FG Nups (Nup42p, Nup49p, Nup57p, Nup100p, and Nup116p) via the Kap95p–Kap60p heterodimer (Allen et al., 2001 and data not shown), suggesting that Nup2p moves across the NPC in a Kap95p–Kap60p-dependent manner.","type":"Discussion"}],"reference_html":"The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p at the nuclear pore complex. <i> Denning D, Mykytka B, Allen NP, Huang L, Al Burlingame, Rexach M. </i> J Cell Biol, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000279","region_id":"DP00222r017","ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P32499","date":"2016-09-09T10:21:45.000Z","acc":"P32499","name":"Nucleoporin NUP2","length":720,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000130A2C","genes":[{"name":{"value":"NUP2"},"orfNames":[{"value":"L8300.9"}],"olnNames":[{"value":"YLR335W"}]}],"alphafold_very_low_content":0.6,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":720,"type":"D"}],"Structural state":[{"start":1,"end":720,"type":"D"}],"Molecular function":[{"start":1,"end":720,"type":"F"}],"Disorder function":[{"start":185,"end":527,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00134","name":"Cyclin, N-terminal domain","start":173,"end":297},{"id":"PF02984","name":"Cyclin, C-terminal domain","start":300,"end":417}],"gene3D":[{"start":173,"end":414,"id":"1.10.472.10","name":"Cyclin-like"},{"start":187,"end":298,"id":"1.10.472.10","name":"Cyclin-like"}]},"uniref50":"UniRef50_P14635","sequence":"MALRVTRNSKINAENKAKINMAGAKRVPTAPAATSKPGLRPRTALGDIGNKVSEQLQAKMPMKKEAKPSATGKVIDKKLPKPLEKVPMLVPVPVSEPVPEPEPEPEPEPVKEEKLSPEPILVDTASPSPMETSGCAPAEEDLCQAFSDVILAVNDVDAEDGADPNLCSEYVKDIYAYLRQLEEEQAVRPKYLLGREVTGNMRAILIDWLVQVQMKFRLLQETMYMTVSIIDRFMQNNCVPKKMLQLVGVTAMFIASKYEEMYPPEIGDFAFVTDNTYTKHQIRQMEMKILRALNFGLGRPLPLHFLRRASKIGEVDVEQHTLAKYLMELTMLDYDMVHFPPSQIAAGAFCLALKILDNGEWTPTLQHYLSYTEESLLPVMQHLAKNVVMVNQGLTKHMTVKNKYATSKHAKISTLPQLNSALVQDLAKAVAKV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P14635","disprot_id":"DP00223","ncbi_taxon_id":9606,"regions_counter":6,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":78,"region_id":"DP00223r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"The regions of securin and cyclin B proteins recognized by the ubiquitination machinery are natively unfolded. <i> Cox CJ, Dutta K, Petri ET, Hwang WC, Lin Y, Pascal SM, Basavappa R. </i> FEBS Lett, 2002","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12220679","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-02-09T14:52:31.809Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The lack of dispersion seen for the amide chemical shifts in the WATERGATE spectra indicates a very similar environment for all amide hydrogen atoms in the proteins and therefore a random coil state for the polypeptide. Further indication of the unfolded state of both N-terminal fragments comes from examination of the methyl proton region of the spectra. As shown in Fig. 4B, the methyl protons display little dispersion. Furthermore, the methyl proton peaks are clustered in the region of ∼1.0–0.8 ppm, whereas peaks from methyl protons in a hydrophobic environment typically are shifted upfield to ∼0.5–0.0 ppm. Thus, 1H-NMR studies strongly indicate a largely unfolded conformation for both N-terminal fragments.","type":"Results"},{"text":"Of the observable NOEs, almost all have negative values, indicating fast tumbling and local flexibility. Thus, 1H,15N NOE analysis provides little indication of stable structure.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":78,"region_id":"DP00223r004","released":"2023_06","ec_id":"ECO:0006204","reference_html":"The regions of securin and cyclin B proteins recognized by the ubiquitination machinery are natively unfolded. <i> Cox CJ, Dutta K, Petri ET, Hwang WC, Lin Y, Pascal SM, Basavappa R. </i> FEBS Lett, 2002","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12220679","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-02-09T14:33:44.757Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The CD spectra of ND-cycB and ND-Pds1 (Fig. 3) are devoid of the significant signatures of secondary structure, most notably negative bands at 222 nm and 208 nm for α-helix and a negative band at 217 nm for β-sheet. Instead, the predominant feature is a strong negative band at 200 nm, which is correlated with a predominantly unstructured polypeptide.","type":"Results"},{"text":"A more compelling analysis involves examination of the degree of cooperativity in the change of CD spectra with increasing temperature. Cooperativity seems to be an unfailing hallmark of the folded-to-unfolded transition. As can be seen from measurements at the two characteristic wavelengths of 200 nm and 222 nm (Fig. 3), the variation of the ellipticity values with temperature does not display cooperativity; instead, the values vary linearly. ","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P14635","date":"2016-08-31T13:04:01.000Z","acc":"P14635","name":"G2/mitotic-specific cyclin-B1","length":433,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00001275A9","genes":[{"name":{"value":"CCNB1"},"synonyms":[{"value":"CCNB"}]}],"alphafold_very_low_content":0.302540415704388,"disorder_content":0.18013856812933027,"disprot_consensus":{"full":[{"start":1,"end":78,"type":"D"}],"Structural state":[{"start":1,"end":78,"type":"D"}]}},{"features":{"pfam":[{"id":"PF07651","name":"ANTH domain","start":22,"end":283}],"gene3D":[{"start":1,"end":146,"id":"1.25.40.90","name":"1.25.40.90"},{"start":147,"end":294,"id":"1.20.58.150","name":"ANTH domain"}]},"uniref50":"UniRef50_Q05140","sequence":"MSGQTLTDRIAAAQYSVTGSAVARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFDFARVKKGADGVMRTMVPEKLLKSMPILQGQIDALLEFDVHPNELTNGVINAAFMLLFKDLIKLFACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSEFLKVADEVGIDKGDIPDLTQAPSSLMETLEQHLNTLEGKKPGNNEGSGAPSPLSKSSPATTVTSPNSTPAKTIDTSPPVDIFATASAAAPVSSAKPSSDLLDLQPDFSGARAGAAAPVPPPTGGATAWGDLLGEDSLAALSSVPSEAPISDPFAPEPSPPTTTTEPASASASATTAVTAATTEVDLFGDAFAASPGEAPAASEGATAPATPAPVAAALDACSGNDPFAPSEGSAEAAPELDLFAMKPPETSAPVVTPTASTAPPVPATAPSPAPTAVAATAATTTAAAAATTTATTSAAAATTAAAPPALDIFGDLFDSAPEVAAASKPDVAPSIDLFGTDAFSSPPRGASPVPESSLTADLLSGSGFHCAEDDRHVPLFFTAVDAFAAPSPASTASPAKAESSGVIDLFGDAFGSSASETQPAPQAVSSSSASADLLAGFGGSFMAPSTTPVTPAQNNLLQPNFEAAFGTTPSTSSSSSFDPSGDLLMPTMAPSGQPAPVSMVPPSPAMSASKGLGSDLDSSLASLVGNLGISGTTSKKGDLQWNAGEKKLTGGANWQPKVTPATWSAGVPPQGTVPPTSSVPPGAGAPSVGQPGAGYGMPPAGTGMTMMPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPATQSPKKPPAKDPLADLNIKDFL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_Q05140","disprot_id":"DP00225","ncbi_taxon_id":10116,"regions_counter":15,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":896,"region_id":"DP00225r001","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Unusual structural organization of the endocytic proteins AP180 and epsin 1. <i> Kalthoff C, Alves J, Urbanke C, Knorr R, Ungewickell EJ. </i> J Biol Chem, 2002","term_id":"IDPO:0000002","curator_id":"vnugnes","start":745,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-02-10T12:46:01.792Z","reference_source":"pmid","term_name":"disorder","reference_id":"11756460","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sequence_construct":"GQPAPVSMVPPSPAMSASKGLGSDLDSSLASLVGNLGISGTTSKKGDLQWNAGEKKLTGGANWQPKVTPATWSAGVPPQGTVPPTSSVPPGAGAPSVGQPGAGYGMPPAGTGMTMMPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPATQSPKKPPAKDPLADLNIKDFL","statement":[{"text":"The first fragment extended from Val328to Gly745, and the second from Gly745 to Leu896. As expected, the spectra of both fragments revealed little secondary structure; but more important, the sum of the molar ellipticities in the spectra of the three recombinant AP180 fragments (His6-AP180-(1–329), -(328–745), and -(745–896)) was identical to that in the spectrum of recombinant full-length AP180 and similar to that in the spectrum of AP180 isolated from pig brain (Fig.4 D).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":896,"region_id":"DP00225r004","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Unusual structural organization of the endocytic proteins AP180 and epsin 1. <i> Kalthoff C, Alves J, Urbanke C, Knorr R, Ungewickell EJ. </i> J Biol Chem, 2002","term_id":"IDPO:0000002","curator_id":"vnugnes","start":328,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-02-10T12:44:45.821Z","reference_source":"pmid","term_name":"disorder","reference_id":"11756460","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sequence_construct":"VDIFATASAAAPVSSAKPSSDLLDLQPDFSGARAGAAAPVPPPTGGATAWGDLLGEDSLAALSSVPSEAPISDPFAPEPSPPTTTTEPASASASATTAVTAATTEVDLFGDAFAASPGEAPAASEGATAPATPAPVAAALDACSGNDPFAPSEGSAEAAPELDLFAMKPPETSAPVVTPTASTAPPVPATAPSPAPTAVAATAATTTAAAAATTTATTSAAAATTAAAPPALDIFGDLFDSAPEVAAASKPDVAPSIDLFGTDAFSSPPRGASPVPESSLTADLLSGSGFHCAEDDRHVPLFFTAVDAFAAPSPASTASPAKAESSGVIDLFGDAFGSSASETQPAPQAVSSSSASADLLAGFGGSFMAPSTTPVTPAQNNLLQPNFEAAFGTTPSTSSSSSFDPSGDLLMPTMAPSGQPAPVSMVPPSPAMSASKGLGSDLDSSLASLVGNLGISGTTSKKGDLQWNAGEKKLTGGANWQPKVTPATWSAGVPPQGTVPPTSSVPPGAGAPSVGQPGAGYGMPPAGTGMTMMPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPATQSPKKPPAKDPLADLNIKDFL","statement":[{"text":"In the spectra of the fragments lacking the ENTH domains (His6-epsin 1-(144–575) and His6-AP180-(328–896)), the α-helical characteristics were almost completely lost, whereas the content of random structures increased from 56 to 66% for the epsin 1 fragment and from 55 to 84% for the AP180 fragment (Fig. 4,A and B).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":745,"region_id":"DP00225r007","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Unusual structural organization of the endocytic proteins AP180 and epsin 1. <i> Kalthoff C, Alves J, Urbanke C, Knorr R, Ungewickell EJ. </i> J Biol Chem, 2002","term_id":"IDPO:0000002","curator_id":"vnugnes","start":328,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"11756460","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-02-10T12:46:49.967Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sequence_construct":"VDIFATASAAAPVSSAKPSSDLLDLQPDFSGARAGAAAPVPPPTGGATAWGDLLGEDSLAALSSVPSEAPISDPFAPEPSPPTTTTEPASASASATTAVTAATTEVDLFGDAFAASPGEAPAASEGATAPATPAPVAAALDACSGNDPFAPSEGSAEAAPELDLFAMKPPETSAPVVTPTASTAPPVPATAPSPAPTAVAATAATTTAAAAATTTATTSAAAATTAAAPPALDIFGDLFDSAPEVAAASKPDVAPSIDLFGTDAFSSPPRGASPVPESSLTADLLSGSGFHCAEDDRHVPLFFTAVDAFAAPSPASTASPAKAESSGVIDLFGDAFGSSASETQPAPQAVSSSSASADLLAGFGGSFMAPSTTPVTPAQNNLLQPNFEAAFGTTPSTSSSSSFDPSGDLLMPTMAPSG","statement":[{"text":"The first fragment extended from Val328to Gly745, and the second from Gly745 to Leu896. As expected, the spectra of both fragments revealed little secondary structure; but more important, the sum of the molar ellipticities in the spectra of the three recombinant AP180 fragments (His6-AP180-(1–329), -(328–745), and -(745–896)) was identical to that in the spectrum of recombinant full-length AP180 and similar to that in the spectrum of AP180 isolated from pig brain (Fig.4 D).","type":"Results"}]},{"start":328,"end":896,"reference_id":"11756460","reference_source":"pmid","reference_html":"Unusual structural organization of the endocytic proteins AP180 and epsin 1. <i> Kalthoff C, Alves J, Urbanke C, Knorr R, Ungewickell EJ. </i> J Biol Chem, 2002","date":"2023-02-10T12:40:47.838Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00225r010","statement":[{"text":"The observed hydrodynamic size is consistent with either an extended rod with a thickness of 1.5–2.0 nm and a length of some 50 nm or, alternatively, a poorly folded polypeptide chain. Taken together, our data obtained from quantitative gel filtration chromatography and ultracentrifugation strongly suggest that the carboxyl-terminal parts of epsin 1 and AP180 are rather extended, with the consequence that they behave like very large proteins on gel filtration columns and like molecular parachutes during ultracentrifugation.","type":"Results"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sequence_construct":"VDIFATASAAAPVSSAKPSSDLLDLQPDFSGARAGAAAPVPPPTGGATAWGDLLGEDSLAALSSVPSEAPISDPFAPEPSPPTTTTEPASASASATTAVTAATTEVDLFGDAFAASPGEAPAASEGATAPATPAPVAAALDACSGNDPFAPSEGSAEAAPELDLFAMKPPETSAPVVTPTASTAPPVPATAPSPAPTAVAATAATTTAAAAATTTATTSAAAATTAAAPPALDIFGDLFDSAPEVAAASKPDVAPSIDLFGTDAFSSPPRGASPVPESSLTADLLSGSGFHCAEDDRHVPLFFTAVDAFAAPSPASTASPAKAESSGVIDLFGDAFGSSASETQPAPQAVSSSSASADLLAGFGGSFMAPSTTPVTPAQNNLLQPNFEAAFGTTPSTSSSSSFDPSGDLLMPTMAPSGQPAPVSMVPPSPAMSASKGLGSDLDSSLASLVGNLGISGTTSKKGDLQWNAGEKKLTGGANWQPKVTPATWSAGVPPQGTVPPTSSVPPGAGAPSVGQPGAGYGMPPAGTGMTMMPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPATQSPKKPPAKDPLADLNIKDFL"},{"start":328,"end":896,"reference_id":"11756460","reference_source":"pmid","reference_html":"Unusual structural organization of the endocytic proteins AP180 and epsin 1. <i> Kalthoff C, Alves J, Urbanke C, Knorr R, Ungewickell EJ. </i> J Biol Chem, 2002","date":"2023-02-10T12:40:27.884Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00225r011","statement":[{"text":"The observed hydrodynamic size is consistent with either an extended rod with a thickness of 1.5–2.0 nm and a length of some 50 nm or, alternatively, a poorly folded polypeptide chain. Taken together, our data obtained from quantitative gel filtration chromatography and ultracentrifugation strongly suggest that the carboxyl-terminal parts of epsin 1 and AP180 are rather extended, with the consequence that they behave like very large proteins on gel filtration columns and like molecular parachutes during ultracentrifugation.","type":"Results"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sequence_construct":"VDIFATASAAAPVSSAKPSSDLLDLQPDFSGARAGAAAPVPPPTGGATAWGDLLGEDSLAALSSVPSEAPISDPFAPEPSPPTTTTEPASASASATTAVTAATTEVDLFGDAFAASPGEAPAASEGATAPATPAPVAAALDACSGNDPFAPSEGSAEAAPELDLFAMKPPETSAPVVTPTASTAPPVPATAPSPAPTAVAATAATTTAAAAATTTATTSAAAATTAAAPPALDIFGDLFDSAPEVAAASKPDVAPSIDLFGTDAFSSPPRGASPVPESSLTADLLSGSGFHCAEDDRHVPLFFTAVDAFAAPSPASTASPAKAESSGVIDLFGDAFGSSASETQPAPQAVSSSSASADLLAGFGGSFMAPSTTPVTPAQNNLLQPNFEAAFGTTPSTSSSSSFDPSGDLLMPTMAPSGQPAPVSMVPPSPAMSASKGLGSDLDSSLASLVGNLGISGTTSKKGDLQWNAGEKKLTGGANWQPKVTPATWSAGVPPQGTVPPTSSVPPGAGAPSVGQPGAGYGMPPAGTGMTMMPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPATQSPKKPPAKDPLADLNIKDFL"},{"start":328,"end":896,"reference_id":"11756460","reference_source":"pmid","reference_html":"Unusual structural organization of the endocytic proteins AP180 and epsin 1. <i> Kalthoff C, Alves J, Urbanke C, Knorr R, Ungewickell EJ. </i> J Biol Chem, 2002","date":"2025-03-19T16:22:12.085Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006301","ec_ontology":"ECO","ec_name":"protein thermal shift assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"region_id":"DP00225r012","sequence_construct":"VDIFATASAAAPVSSAKPSSDLLDLQPDFSGARAGAAAPVPPPTGGATAWGDLLGEDSLAALSSVPSEAPISDPFAPEPSPPTTTTEPASASASATTAVTAATTEVDLFGDAFAASPGEAPAASEGATAPATPAPVAAALDACSGNDPFAPSEGSAEAAPELDLFAMKPPETSAPVVTPTASTAPPVPATAPSPAPTAVAATAATTTAAAAATTTATTSAAAATTAAAPPALDIFGDLFDSAPEVAAASKPDVAPSIDLFGTDAFSSPPRGASPVPESSLTADLLSGSGFHCAEDDRHVPLFFTAVDAFAAPSPASTASPAKAESSGVIDLFGDAFGSSASETQPAPQAVSSSSASADLLAGFGGSFMAPSTTPVTPAQNNLLQPNFEAAFGTTPSTSSSSSFDPSGDLLMPTMAPSGQPAPVSMVPPSPAMSASKGLGSDLDSSLASLVGNLGISGTTSKKGDLQWNAGEKKLTGGANWQPKVTPATWSAGVPPQGTVPPTSSVPPGAGAPSVGQPGAGYGMPPAGTGMTMMPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPATQSPKKPPAKDPLADLNIKDFL","statement":[{"text":"SDS-PAGE analysis of the supernatant and pellet fractions indeed demonstrated that His6-epsin 1-(144–625) and His6-AP180-(328–896) were both heat-stable, whereas the full-length proteins and GST added as a carrier and internal standard did almost quantitatively precipitate (Fig.5 A). ","type":"Results"}]},{"start":328,"end":896,"reference_id":"11756460","reference_source":"pmid","reference_html":"Unusual structural organization of the endocytic proteins AP180 and epsin 1. <i> Kalthoff C, Alves J, Urbanke C, Knorr R, Ungewickell EJ. </i> J Biol Chem, 2002","date":"2023-02-10T13:04:14.859Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0030276","term_name":"clathrin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q00610","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00225r013","sequence_construct":"VDIFATASAAAPVSSAKPSSDLLDLQPDFSGARAGAAAPVPPPTGGATAWGDLLGEDSLAALSSVPSEAPISDPFAPEPSPPTTTTEPASASASATTAVTAATTEVDLFGDAFAASPGEAPAASEGATAPATPAPVAAALDACSGNDPFAPSEGSAEAAPELDLFAMKPPETSAPVVTPTASTAPPVPATAPSPAPTAVAATAATTTAAAAATTTATTSAAAATTAAAPPALDIFGDLFDSAPEVAAASKPDVAPSIDLFGTDAFSSPPRGASPVPESSLTADLLSGSGFHCAEDDRHVPLFFTAVDAFAAPSPASTASPAKAESSGVIDLFGDAFGSSASETQPAPQAVSSSSASADLLAGFGGSFMAPSTTPVTPAQNNLLQPNFEAAFGTTPSTSSSSSFDPSGDLLMPTMAPSGQPAPVSMVPPSPAMSASKGLGSDLDSSLASLVGNLGISGTTSKKGDLQWNAGEKKLTGGANWQPKVTPATWSAGVPPQGTVPPTSSVPPGAGAPSVGQPGAGYGMPPAGTGMTMMPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPATQSPKKPPAKDPLADLNIKDFL","statement":[{"text":"Binding of the boiled protein fragments to clathrin and the adaptor was assessed by pull-down experiments using the immobilized recombinant α-appendage domain and the clathrin amino-terminal domain as baits. No significant differences between the untreated and heat-treated His6-AP180-(328–896) fragments were observed (Fig.5 B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a clathrin heavy or light chain, the main components of the coat of coated vesicles and coated pits, and which also occurs in synaptic vesicles.\" [GOC:jl, GOC:mah, ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false},{"start":328,"end":896,"reference_id":"11756460","reference_source":"pmid","reference_html":"Unusual structural organization of the endocytic proteins AP180 and epsin 1. <i> Kalthoff C, Alves J, Urbanke C, Knorr R, Ungewickell EJ. </i> J Biol Chem, 2002","date":"2023-02-10T13:29:39.676Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0048268","term_name":"clathrin coat assembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"Q00610","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00225r014","sequence_construct":"VDIFATASAAAPVSSAKPSSDLLDLQPDFSGARAGAAAPVPPPTGGATAWGDLLGEDSLAALSSVPSEAPISDPFAPEPSPPTTTTEPASASASATTAVTAATTEVDLFGDAFAASPGEAPAASEGATAPATPAPVAAALDACSGNDPFAPSEGSAEAAPELDLFAMKPPETSAPVVTPTASTAPPVPATAPSPAPTAVAATAATTTAAAAATTTATTSAAAATTAAAPPALDIFGDLFDSAPEVAAASKPDVAPSIDLFGTDAFSSPPRGASPVPESSLTADLLSGSGFHCAEDDRHVPLFFTAVDAFAAPSPASTASPAKAESSGVIDLFGDAFGSSASETQPAPQAVSSSSASADLLAGFGGSFMAPSTTPVTPAQNNLLQPNFEAAFGTTPSTSSSSSFDPSGDLLMPTMAPSGQPAPVSMVPPSPAMSASKGLGSDLDSSLASLVGNLGISGTTSKKGDLQWNAGEKKLTGGANWQPKVTPATWSAGVPPQGTVPPTSSVPPGAGAPSVGQPGAGYGMPPAGTGMTMMPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPATQSPKKPPAKDPLADLNIKDFL","statement":[{"text":"Similarly, heating did not affect the ability of the fragment to induce clathrin assembly (Fig. 5 C).","type":"Results"},{"text":"A, Coomassie Blue staining/SDS-PAGE of the supernatants (s) and pellets (p) after ultracentrifugation of the reaction mixtures showed that full-length epsin 1 very efficiently assembled clathrin. His6-epsin 1-(144–575) also assembled clathrin, albeit less efficiently than the full-length protein.","type":"Figure"}],"term_comment":"","term_def":"\"The process that results in the assembly of clathrin triskelia into the ordered structure known as a clathrin cage.\" [GOC:jid, PMID:11460887, PMID:11977118, PMID:9531549]","term_is_obsolete":false,"term_not_annotate":false},{"start":328,"end":896,"reference_id":"11756460","reference_source":"pmid","reference_html":"Unusual structural organization of the endocytic proteins AP180 and epsin 1. <i> Kalthoff C, Alves J, Urbanke C, Knorr R, Ungewickell EJ. </i> J Biol Chem, 2002","date":"2023-02-10T13:28:54.753Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0048268","term_name":"clathrin coat assembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"Q00610","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00225r015","sequence_construct":"VDIFATASAAAPVSSAKPSSDLLDLQPDFSGARAGAAAPVPPPTGGATAWGDLLGEDSLAALSSVPSEAPISDPFAPEPSPPTTTTEPASASASATTAVTAATTEVDLFGDAFAASPGEAPAASEGATAPATPAPVAAALDACSGNDPFAPSEGSAEAAPELDLFAMKPPETSAPVVTPTASTAPPVPATAPSPAPTAVAATAATTTAAAAATTTATTSAAAATTAAAPPALDIFGDLFDSAPEVAAASKPDVAPSIDLFGTDAFSSPPRGASPVPESSLTADLLSGSGFHCAEDDRHVPLFFTAVDAFAAPSPASTASPAKAESSGVIDLFGDAFGSSASETQPAPQAVSSSSASADLLAGFGGSFMAPSTTPVTPAQNNLLQPNFEAAFGTTPSTSSSSSFDPSGDLLMPTMAPSGQPAPVSMVPPSPAMSASKGLGSDLDSSLASLVGNLGISGTTSKKGDLQWNAGEKKLTGGANWQPKVTPATWSAGVPPQGTVPPTSSVPPGAGAPSVGQPGAGYGMPPAGTGMTMMPQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPATQSPKKPPAKDPLADLNIKDFL","statement":[{"text":"As expected, this epsin 1 fragment also possessed assembly activity, although it was somewhat lower compared with that of the full-length protein. Electron micrographs showed that the cages were slightly larger and less homogeneous than those assembled by AP180 or His6-AP180-(328–896) (Fig. 6).","type":"Results"},{"text":"Free clathrin triskelia were incubated with recombinant full-length epsin 1, a recombinantly expressed fragment of epsin 1 lacking the ENTH domain, and 6x-His-AP180-(328–896) as a positive control.","type":"Figure"}],"term_comment":"","term_def":"\"The process that results in the assembly of clathrin triskelia into the ordered structure known as a clathrin cage.\" [GOC:jid, PMID:11460887, PMID:11977118, PMID:9531549]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_Q05140","date":"2016-08-25T10:18:27.000Z","acc":"Q05140","name":"Clathrin coat assembly protein AP180","length":915,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI0000124FB4","genes":[{"name":{"value":"Snap91"}}],"alphafold_very_low_content":0.6513661202185792,"disorder_content":0.6218579234972678,"disprot_consensus":{"full":[{"start":328,"end":896,"type":"D"}],"Structural state":[{"start":328,"end":896,"type":"D"}],"Molecular function":[{"start":328,"end":896,"type":"F"}],"Biological process":[{"start":328,"end":896,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04969","name":"CS domain","start":78,"end":157},{"id":"PF05002","name":"SGS domain","start":164,"end":218},{"id":"PF09032","name":"Siah interacting protein, N terminal","start":4,"end":76}],"gene3D":[{"start":72,"end":177,"id":"2.60.40.790","name":"2.60.40.790"},{"start":1,"end":48,"id":"4.10.860.10","name":"UVR domain"}]},"uniref50":"UniRef50_Q9HB71","sequence":"MASVLEELQKDLEEVKVLLEKSTRKRLRDTLTSEKSKIETELKNKMQQKSQKKPELDNEKPAAVVAPLTTGYTVKISNYGWDQSDKFVKIYITLTGVHQVPTENVQVHFTERSFDLLVKNLNGKNYSMIVNNLLKPISVESSSKKVKTDTVIILCRKKAENTRWDYLTQVEKECKEKEKPSYDTEADPSEGLMNVLKKIYEDGDDDMKRTINKAWVESREKQAREDTEF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q9CXW3","disprot_id":"DP00226","ncbi_taxon_id":10090,"regions_counter":7,"creator":"eleonardi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":77,"region_id":"DP00226r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"The modular structure of SIP facilitates its role in stabilizing multiprotein assemblies. <i> Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A, Kuznicki J, Chazin WJ. </i> Biochemistry, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":48,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-02-14T16:52:44.070Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1YSM"}],"reference_id":"15996101","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The 30 C-terminal residues corresponding to SIP(48−77) did not form regular secondary structure.","type":"Results"}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":77,"term_name":"molecular adaptor activity","released":"2023_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The modular structure of SIP facilitates its role in stabilizing multiprotein assemblies. <i> Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A, Kuznicki J, Chazin WJ. </i> Biochemistry, 2005","term_id":"GO:0060090","curator_id":"vnugnes","start":48,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"15996101","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-02-14T17:27:04.852Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00226r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P61092","operator":"and","partner_start":null,"partner_end":null}],"statement":[{"text":"SIP appears not to engage in specific catalytic activity but is part of a growing family of adaptor proteins that mediate the correct assembly of ubiquitination complexes to achieve functional diversity.","type":"Conclusion"},{"text":"The core of the complex is formed by a novel Cullin-1-like adaptor protein SIP, which provides a physical link between the RING domain of Siah-1 and the substrate engaged by the Skp1/Ebi F-Box protein (Figure 1).","type":"Article"}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":77,"term_name":"ubiquitin protein ligase binding","released":"2023_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The modular structure of SIP facilitates its role in stabilizing multiprotein assemblies. <i> Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A, Kuznicki J, Chazin WJ. </i> Biochemistry, 2005","term_id":"GO:0031625","curator_id":"vnugnes","start":48,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"15996101","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-02-14T17:14:35.550Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00226r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.\" [GOC:vp]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P61092","operator":null,"partner_start":90,"partner_end":282}],"statement":[{"text":"NMR titrations of unlabeled Siah(90−282) into 15N-labeled intact SIP resulted in a loss of peak intensity and chemical shift changes for residues (Met46−Gly71) in the linker and, surprisingly, the disappearance of residues from the CS domain (Figure 6A).","type":"Results"},{"text":"For the SIP N-terminal region (residues 1−77), differential line broadening, chemical shift perturbations, and a loss in peak intensity of residues located in the linker region are observed as in the intact protein (Figure 6B). In contrast, the NMR signals of the isolated CS domain behaved differently than those in the intact protein, as no perturbations in the CS domain were observed (Supporting Information).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":229,"region_id":"DP00226r004","released":"2023_06","ec_id":"ECO:0006165","reference_html":"The modular structure of SIP facilitates its role in stabilizing multiprotein assemblies. <i> Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A, Kuznicki J, Chazin WJ. </i> Biochemistry, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":178,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-02-14T16:41:10.437Z","reference_source":"pmid","term_name":"disorder","reference_id":"15996101","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Figure 2 shows the HSQC spectra for residues 1−77, 74−178, and 178−229. The dispersion of NMR resonances clearly shows that the N-terminal and central fragments contain independent folded globular domains, whereas the C-terminal fragment is not folded. Additional spectra were acquired for residues 155−229 and 73−229 (Supporting Information), but the lack of signal dispersion for the C-terminal residues was not affected by extending the N-terminus of these constructs.","type":"Results"}]},{"start":48,"end":77,"reference_id":"15996101","reference_source":"pmid","reference_html":"The modular structure of SIP facilitates its role in stabilizing multiprotein assemblies. <i> Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A, Kuznicki J, Chazin WJ. </i> Biochemistry, 2005","date":"2023-02-14T16:55:14.260Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00226r007","statement":[{"text":"The 30 C-terminal residues corresponding to SIP(48−77) did not form regular secondary structure.","type":"Results"},{"text":"Structural characterization of SIP(1−77) revealed the putative Siah-1 binding region (Pro61−Pro67, PAAVVAP) is part of the unstructured linker region (residues 48−73) that connects the N-terminal helical domain of SIP and the CS domain.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_Q9CXW3","date":"2016-09-04T18:34:50.000Z","acc":"Q9CXW3","name":"Calcyclin-binding protein","length":229,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000E8A82","genes":[{"name":{"value":"Cacybp"},"synonyms":[{"value":"Sip"}]}],"alphafold_very_low_content":0.08296943231441048,"disorder_content":0.35807860262008734,"disprot_consensus":{"full":[{"start":48,"end":77,"type":"D"},{"start":178,"end":229,"type":"D"}],"Structural state":[{"start":48,"end":77,"type":"D"},{"start":178,"end":229,"type":"D"}],"Molecular function":[{"start":48,"end":77,"type":"F"}],"Disorder function":[{"start":48,"end":77,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00520","name":"Ion transport protein","start":51,"end":344},{"id":"PF00520","name":"Ion transport protein","start":432,"end":669},{"id":"PF00520","name":"Ion transport protein","start":799,"end":1074},{"id":"PF00520","name":"Ion transport protein","start":1118,"end":1391},{"id":"PF08763","name":"Voltage gated calcium channel IQ domain","start":1464,"end":1536},{"id":"PF16905","name":"Voltage-dependent L-type calcium channel, IQ-associated","start":1401,"end":1454}],"gene3D":[{"start":1107,"end":1252,"id":"1.20.120.350","name":"Voltage-gated potassium channels. Chain C"},{"start":41,"end":180,"id":"1.20.120.350","name":"Voltage-gated potassium channels. Chain C"},{"start":422,"end":544,"id":"1.20.120.350","name":"Voltage-gated potassium channels. Chain C"},{"start":788,"end":910,"id":"1.20.120.350","name":"Voltage-gated potassium channels. Chain C"},{"start":1385,"end":1506,"id":"1.10.238.10","name":"EF-hand"},{"start":1253,"end":1384,"id":"1.10.287.70","name":"1.10.287.70"},{"start":545,"end":669,"id":"1.10.287.70","name":"1.10.287.70"}]},"uniref50":"UniRef50_P07293","sequence":"MEPSSPQDEGLRKKQPKKPLPEVLPRPPRALFCLTLQNPLRKACISIVEWKPFETIILLTIFANCVALAVYLPMPEDDNNSLNLGLEKLEYFFLTVFSIEAAMKIIAYGFLFHQDAYLRSGWNVLDFIIVFLGVFTAILEQVNVIQSNTAPMSSKGAGLDVKALRAFRVLRPLRLVSGVPSLQVVLNSIFKAMLPLFHIALLVLFMVIIYAIIGLELFKGKMHKTCYYIGTDIVATVENEKPSPCARTGSGRPCTINGSECRGGWPGPNHGITHFDNFGFSMLTVYQCITMEGWTDVLYWVNDAIGNEWPWIYFVTLILLGSFFILNLVLGVLSGEFTKEREKAKSRGTFQKLREKQQLEEDLRGYMSWITQGEVMDVEDLREGKLSLEEGGSDTESLYEIEGLNKIIQFIRHWRQWNRVFRWKCHDLVKSRVFYWLVILIVALNTLSIASEHHNQPLWLTHLQDIANRVLLSLFTIEMLLKMYGLGLRQYFMSIFNRFDCFVVCSGILELLLVESGAMTPLGISVLRCIRLLRLFKITKYWTSLSNLVASLLNSIRSIASLLLLLFLFIIIFALLGMQLFGGRYDFEDTEVRRSNFDNFPQALISVFQVLTGEDWNSVMYNGIMAYGGPSYPGVLVCIYFIILFVCGNYILLNVFLAIAVDNLAEAESLTSAQKAKAEERKRRKMSRGLPDKTEEEKSVMAKKLEQKPKGEGIPTTAKLKVDEFESNVNEVKDPYPSADFPGDDEEDEPEIPVSPRPRPLAELQLKEKAVPIPEASSFFIFSPTNKVRVLCHRIVNATWFTNFILLFILLSSAALAAEDPIRAESVRNQILGYFDIAFTSVFTVEIVLKMTTYGAFLHKGSFCRNYFNILDLLVVAVSLISMGLESSTISVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIVLVTTLLQFMFACIGVQLFKGKFFSCNDLSKMTEEECRGYYYVYKDGDPTQMELRPRQWIHNDFHFDNVLSAMMSLFTVSTFEGWPQLLYRAIDSNEEDMGPVYNNRVEMAIFFIIYIILIAFFMMNIFVGFVIVTFQEQGETEYKNCELDKNQRQCVQYALKARPLRCYIPKNPYQYQVWYVVTSSYFEYLMFALIMLNTICLGMQHYHQSEEMNHISDILNVAFTIIFTLEMILKLLAFKARGYFGDPWNVFDFLIVIGSIIDVILSEIDTFLASSGGLYCLGGGCGNVDPDESARISSAFFRLFRVMRLIKLLSRAEGVRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQMFGKIALVDGTQINRNNNFQTFPQAVLLLFRCATGEAWQEILLACSYGKLCDPESDYAPGEEYTCGTNFAYYYFISFYMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKAIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKFCPHRVACKRLVGMNMPLNSDGTVTFNATLFALVRTALKIKTEGNFEQANEELRAIIKKIWKRTSMKLLDQVIPPIGDDEVTVGKFYATFLIQEHFRKFMKRQEEYYGYRPKKDTVQIQAGLRTIEEEAAPEIRRTISGDLTAEEELERAMVEAAMEERIFRRTGGLFGQVDTFLERTNSLPPVMANQRPLQFAEIEMEELESPVFLEDFPQDARTNPLARANTNNANANVAYGNSNHSNNQMFSSVHCEREFPGEAETPAAGRGALSHSHRALGPHSKPCAGKLNGQLVQPGMPINQAPPAPCQQPSTDPPERGQRRTSLTGSLQDEAPQRRSSEGSTPRRPAPATALLIQEALVRGGLDTLAADAGFVTATSQALADACQMEPEEVEVAATELLKARESVQGMASVPGSLSRRSSLGSLDQVQGSQETLIPPRP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Lagomorpha","Leporidae","Oryctolagus"],"uniref90":"UniRef90_P07293","disprot_id":"DP00228","ncbi_taxon_id":9986,"regions_counter":12,"creator":"ftonello","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":760,"region_id":"DP00228r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The random-coil 'C' fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors. <i> Haarmann CS, Green D, Casarotto MG, Laver DR, Dulhunty AF. </i> Biochem J, 2003","term_id":"IDPO:0000002","curator_id":"ftonello","start":724,"term_ontology":"IDPO","curator_name":"Fiorella Tonello","reference_id":"12620094","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":760,"term_name":"disorder to order","start":724,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"ftonello","released":"2022_03","term_ontology":"IDPO","curator_name":"Fiorella Tonello","reference_id":"12620094","version":2,"reference_html":"The random-coil 'C' fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors. <i> Haarmann CS, Green D, Casarotto MG, Laver DR, Dulhunty AF. </i> Biochem J, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00228r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":760,"term_name":"protein binding","start":724,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"ftonello","released":"2022_03","term_ontology":"GO","curator_name":"Fiorella Tonello","reference_id":"12620094","version":3,"reference_html":"The random-coil 'C' fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors. <i> Haarmann CS, Green D, Casarotto MG, Laver DR, Dulhunty AF. </i> Biochem J, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00228r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":760,"region_id":"DP00228r005","released":"2023_06","ec_id":"ECO:0006275","reference_html":"The random-coil 'C' fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors. <i> Haarmann CS, Green D, Casarotto MG, Laver DR, Dulhunty AF. </i> Biochem J, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":724,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12620094","version":3,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","date":"2023-02-14T17:32:41.411Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Maxima and minima in the CD spectra, which indicate a helical structure for peptide A, were not seen for peptide C (Figure 7C). Thus peptide C has a random-coil structure and therefore adopts different conformations, each maintained briefly.","type":"Results"}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":760,"term_name":"molecular function regulator","start":724,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","curator_id":"ftonello","released":"2022_03","term_ontology":"GO","curator_name":"Fiorella Tonello","reference_id":"12620094","version":3,"reference_html":"The random-coil 'C' fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors. <i> Haarmann CS, Green D, Casarotto MG, Laver DR, Dulhunty AF. </i> Biochem J, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006275","region_id":"DP00228r006","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":760,"term_name":"protein binding","start":724,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","curator_id":"ftonello","released":"2022_03","term_ontology":"GO","curator_name":"Fiorella Tonello","reference_id":"12620094","version":3,"reference_html":"The random-coil 'C' fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors. <i> Haarmann CS, Green D, Casarotto MG, Laver DR, Dulhunty AF. </i> Biochem J, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006275","region_id":"DP00228r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":760,"region_id":"DP00228r009","released":"2023_06","ec_id":"ECO:0006165","reference_html":"The random-coil 'C' fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors. <i> Haarmann CS, Green D, Casarotto MG, Laver DR, Dulhunty AF. </i> Biochem J, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":724,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12620094","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-02-14T17:32:01.265Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The simplicity of cross peaks in the amide-α region also indicates a lack of one predominant structure (Figure 7A).","type":"Results"}]},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":760,"term_name":"disorder to order","start":724,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ftonello","released":"2022_03","term_ontology":"IDPO","curator_name":"Fiorella Tonello","reference_id":"12620094","version":2,"reference_html":"The random-coil 'C' fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors. <i> Haarmann CS, Green D, Casarotto MG, Laver DR, Dulhunty AF. </i> Biochem J, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00228r011","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":760,"term_name":"protein binding","start":724,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ftonello","released":"2022_03","term_ontology":"GO","curator_name":"Fiorella Tonello","reference_id":"12620094","version":3,"reference_html":"The random-coil 'C' fragment of the dihydropyridine receptor II-III loop can activate or inhibit native skeletal ryanodine receptors. <i> Haarmann CS, Green D, Casarotto MG, Laver DR, Dulhunty AF. </i> Biochem J, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00228r012","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P07293","date":"2016-09-09T10:46:05.000Z","acc":"P07293","name":"Voltage-dependent L-type calcium channel subunit alpha-1S","length":1873,"organism":"Oryctolagus cuniculus","dataset":[],"UniParc":"UPI000005031B","genes":[{"name":{"value":"CACNA1S"},"synonyms":[{"value":"CACH1"},{"value":"CACNL1A3"}]}],"alphafold_very_low_content":0.21356113187399894,"disorder_content":0.019754404698344902,"disprot_consensus":{"full":[{"start":724,"end":760,"type":"T"}],"Structural state":[{"start":724,"end":760,"type":"D"}],"Structural transition":[{"start":724,"end":760,"type":"T"}],"Molecular function":[{"start":724,"end":760,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":113,"end":178},{"id":"PF05383","name":"La domain","start":17,"end":74},{"id":"PF08777","name":"RNA binding motif","start":231,"end":334}],"gene3D":[{"start":1,"end":90,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"start":214,"end":334,"id":"3.30.70.330","name":"3.30.70.330"},{"start":103,"end":202,"id":"3.30.70.330","name":"3.30.70.330"}]},"uniref50":"UniRef50_P05455","sequence":"MAENGDNEKMAALEAKICHQIEYYFGDFNLPRDKFLKEQIKLDEGWVPLEIMIKFNRLNRLTTDFNVIVEALSKSKAELMEISEDKTKIRRSPSKPLPEVTDEYKNDVKNRSVYIKGFPTDATLDDIKEWLEDKGQVLNIQMRRTLHKAFKGSIFVVFDSIESAKKFVETPGQKYKETDLLILFKDDYFAKKNEERKQNKVEAKLRAKQEQEAKQKLEEDAEMKSLEEKIGCLLKFSGDLDDQTCREDLHILFSNHGEIKWIDFVRGAKEGIILFKEKAKEALGKAKDANNGNLQLRNKEVTWEVLEGEVEKEALKKIIEDQQESLNKWKSKGRRFKGKGKGNKAAQPGSGKGKVQFQGKKTKFASDDEHDEHDENGATGPVKRAREETDKEEPASKQQKTENGAGDQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P05455","disprot_id":"DP00229","ncbi_taxon_id":9606,"regions_counter":7,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":408,"region_id":"DP00229r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Structure of the C-terminal domain of human La protein reveals a novel RNA recognition motif coupled to a helical nuclear retention element. <i> Jacks A, Babon J, Kelly G, Manolaridis I, Cary PD, Curry S, Conte MR. </i> Structure, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":326,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12842046","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-02-14T17:47:00.513Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"NMR analysis of this series of deletion mutants allowed us to identify a core globular domain, comprising residues 231–325 (Jacks et al. 2002; and see below), flanked by a short flexible N terminus (residues 225–230) and a long, flexible C terminus (residues 326–408).","type":"Results"},{"text":"In particular, comparison of 1H-15N HSQC spectra of La225–408, La225–359, and La225–334 (Figure 2) indicated that all well-dispersed peaks correspond to residues assigned in the 230–325 region (Jacks et al. 2002) and suggests, first, that the three-dimensional structure of this fragment is very similar in all three cases, regardless of the length of the C-terminal tail and, second, that the C-terminal tail (326–408) is itself unstructured.","type":"Results"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sequence_construct":"SLEEKIGCLLKFSGDLDDQTCREDLHILFSNHGEIKWIDFVRGAKEGIILFKEKAKEALGKAKDANNGNLQLRNKEVTWEVLEGEVEKEALKKIIEDQQESLNKWKSKGRRFKGKGKGNKAAQPGSGKGKVQFQGKKTKFASDDEHDEHDENGATGPVKRAREETDKEEPASKQQKTENGAGDQ"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":408,"region_id":"DP00229r004","released":"2023_06","ec_id":"ECO:0007691","reference_html":"Structure of the C-terminal domain of human La protein reveals a novel RNA recognition motif coupled to a helical nuclear retention element. <i> Jacks A, Babon J, Kelly G, Manolaridis I, Cary PD, Curry S, Conte MR. </i> Structure, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":326,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12842046","version":3,"ec_name":"cleavage assay evidence used in manual assertion","date":"2023-02-14T17:42:40.073Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"Proteolysis during expression gave rise to a hexahistidine-tagged recombinant protein fragment (La225–334), which was purified by affinity chromatography in a single step on a Ni-NTA resin column (Qiagen; Jacks et al. 2002).","type":"Results"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sequence_construct":"SLEEKIGCLLKFSGDLDDQTCREDLHILFSNHGEIKWIDFVRGAKEGIILFKEKAKEALGKAKDANNGNLQLRNKEVTWEVLEGEVEKEALKKIIEDQQESLNKWKSKGRRFKGKGKGNKAAQPGSGKGKVQFQGKKTKFASDDEHDEHDENGATGPVKRAREETDKEEPASKQQKTENGAGDQ"},{"start":335,"end":408,"reference_id":"12842046","reference_source":"pmid","reference_html":"Structure of the C-terminal domain of human La protein reveals a novel RNA recognition motif coupled to a helical nuclear retention element. <i> Jacks A, Babon J, Kelly G, Manolaridis I, Cary PD, Curry S, Conte MR. </i> Structure, 2003","date":"2023-07-11T14:38:28.575Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008266","term_name":"poly(U) RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","region_id":"DP00229r007","statement":[{"text":"Together, these data reveal that a region present in La225–359 and La225–408, but absent in La225–334, is capable of binding in a nonspecific fashion with 5′-monophosphorylated 10 nt oligo(U) RNA. The interacting portion therefore does not encompass the atypical C-terminal RRM (231–325), and probably involves the unstructured SBM that spans residues 328–363, an observation that is consistent with previous work on pre-tRNA (Fan et al. 1998), Hepatitis C virus IRES (Ali et al. 2000), and 5′-triphosphate RNA targets (Bhattacharya et al. 2002).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a sequence of uracil residues in an RNA molecule.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"ChEBI","id":"8758","operator":"and","partner_start":null,"partner_end":null}]}],"released":"2016_10","uniref100":"UniRef100_P05455","date":"2016-09-07T14:09:24.000Z","acc":"P05455","name":"Lupus La protein","length":408,"organism":"Homo sapiens","dataset":["RNA-binding proteins"],"UniParc":"UPI0000072D81","genes":[{"name":{"value":"SSB"}}],"alphafold_very_low_content":0.18382352941176472,"disorder_content":0.2034313725490196,"disprot_consensus":{"full":[{"start":326,"end":408,"type":"D"}],"Structural state":[{"start":326,"end":408,"type":"D"}],"Molecular function":[{"start":335,"end":408,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00017","name":"SH2 domain","start":439,"end":520},{"id":"PF00169","name":"PH domain","start":236,"end":340},{"id":"PF08947","name":"BPS (Between PH and SH2)","start":369,"end":414},{"id":"PF21989","name":"RA like domain","start":106,"end":191}],"gene3D":[{"start":195,"end":356,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":421,"end":540,"id":"3.30.505.10","name":"SH2 domain"},{"start":100,"end":194,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"}]},"uniref50":"UniRef50_Q14449","sequence":"MTTSLQDGQSAASRAAARDSPLAAQVCGAAQGRGDAHDLAPAPWLHARALLPLPDGTRGCAADRRKKKDLDVPEMPSIPNPFPELCCSPFTSVLSADLFPKANSRKKQVIKVYSEDETSRALDVPSDITARDVCQLLILKNHYIDDHSWTLFEHLPHIGVERTIEDHELVIEVLSNWGIEEENKLYFRKNYAKYEFFKNPMYFFPEHMVSFATETNGEISPTQILQMFLSSSTYPEIHGFLHAKEQGKKSWKKIYFFLRRSGLYFSTKGTSKEPRHLQFFSEFGNSDIYVSLAGKKKHGAPTNYGFCFKPNKAGGPRDLKMLCAEEEQSRTCWVTAIRLLKYGMQLYQNYMHPYQGRSGCSSQSISPMRSISENSLVAMDFSGQKSRVIENPTEALSVAVEEGLAWRKKGCLRLGTHGSPTASSQSSATNMAIHRSQPWFHHKISRDEAQRLIIQQGLVDGVFLVRDSQSNPKTFVLSMSHGQKIKHFQIIPVEDDGEMFHTLDDGHTRFTDLIQLVEFYQLNKGVLPCKLKHYCARIAL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q14449","disprot_id":"DP00230","ncbi_taxon_id":9606,"regions_counter":4,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":435,"region_id":"DP00230r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The PIR domain of Grb14 is an intrinsically unstructured protein: implication in insulin signaling. <i> Moncoq K, Broutin I, Larue V, Perdereau D, Cailliau K, Cailliau K, Browaeys-Poly E, Burnol AF, Ducruix A. </i> FEBS Lett, 2003","term_id":"IDPO:0000002","curator_id":"mnecci","start":361,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"14623073","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":435,"term_name":"molecular adaptor activity","start":361,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"14623073","version":3,"reference_html":"The PIR domain of Grb14 is an intrinsically unstructured protein: implication in insulin signaling. <i> Moncoq K, Broutin I, Larue V, Perdereau D, Cailliau K, Cailliau K, Browaeys-Poly E, Burnol AF, Ducruix A. </i> FEBS Lett, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP00230r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":435,"term_name":"disorder to order","start":361,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"14623073","version":2,"reference_html":"The PIR domain of Grb14 is an intrinsically unstructured protein: implication in insulin signaling. <i> Moncoq K, Broutin I, Larue V, Perdereau D, Cailliau K, Cailliau K, Browaeys-Poly E, Burnol AF, Ducruix A. </i> FEBS Lett, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00230r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":435,"term_name":"protein binding","start":361,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"14623073","version":3,"reference_html":"The PIR domain of Grb14 is an intrinsically unstructured protein: implication in insulin signaling. <i> Moncoq K, Broutin I, Larue V, Perdereau D, Cailliau K, Cailliau K, Browaeys-Poly E, Burnol AF, Ducruix A. </i> FEBS Lett, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00230r004","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q14449","date":"2016-08-31T13:14:59.000Z","acc":"Q14449","name":"Growth factor receptor-bound protein 14","length":540,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012BA85","genes":[{"name":{"value":"GRB14"}}],"alphafold_very_low_content":0.26296296296296295,"disorder_content":0.1388888888888889,"disprot_consensus":{"full":[{"start":361,"end":435,"type":"T"}],"Structural state":[{"start":361,"end":435,"type":"D"}],"Molecular function":[{"start":361,"end":435,"type":"F"}],"Structural transition":[{"start":361,"end":435,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00046","name":"Homeodomain","start":380,"end":436},{"id":"PF00157","name":"Pou domain - N-terminal to homeobox domain","start":284,"end":354},{"id":"PF19536","name":"POU domain, class 2, transcription factor 1 C-terminal","start":447,"end":729}],"gene3D":[{"start":382,"end":429,"id":"1.10.10.60","name":"Homeodomain-like"},{"start":284,"end":354,"id":"1.10.260.40","name":"lambda repressor-like DNA-binding domains"}]},"uniref50":"UniRef50_P14859","sequence":"MNNPSETSKPSMESGDGNTGTQTNGLDFQKQPVPVGGAISTAQAQAFLGHLHQVQLAGTSLQAAAQSLNVQSKSNEESGDSQQPSQPSQQPSVQAAIPQTQLMLAGGQITGLTLTPAQQQLLLQQAQAQAQLLAAAVQQHSASQQHSAAGATISASAATPMTQIPLSQPIQIAQDLQQLQQLQQQNLNLQQFVLVHPTTNLQPAQFIISQTPQGQQGLLQAQNLLTQLPQQSQANLLQSQPSITLTSQPATPTRTIAATPIQTLPQSQSTPKRIDTPSLEEPSDLEELEQFAKTFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAENLSSDSSLSSPSALNSPGIEGLSRRRKKRTSIETNIRVALEKSFLENQKPTSEEITMIADQLNMEKEVIRVWFCNRRQKEKRINPPSSGGTSSSPIKAIFPSPTSLVATTPSLVTSSAATTLTVSPVLPLTSAAVTNLSVTGTSDTTSNNTATVISTAPPASSAVTSPSLSPSPSASASTSEASSASETSTTQTTSTPLSSPLGTSQVMVTASGLQTAAAAALQGAAQLPANASLAAMAAAAGLNPSLMAPSQFAAGGALLSLNPGTLSGALSPALMSNSTLATIQALASGGSLPITSLDATGNLVFANAGGAPNIVTAPLFLNPQNLSLLTSNPVSLVSAAAASAGNSAPVASLHATSTSAESIQNSLFTVASASGAASTTTTASKAQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P14859","disprot_id":"DP00231","ncbi_taxon_id":9606,"regions_counter":8,"creator":"zdosztanyi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":200,"region_id":"DP00231r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Expression of the Oct-1 transcription factor and characterization of its interactions with the Bob1 coactivator. <i> Lee L, Stollar E, Chang J, Grossmann JG, O'Brien R, Ladbury J, Carpenter B, Roberts S, Luisi B. </i> Biochemistry, 2001","term_id":"IDPO:0000002","curator_id":"zdosztanyi","start":1,"term_ontology":"IDPO","curator_name":"Zsuzsanna Dosztányi","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"11380252","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":200,"term_name":"molecular function regulator","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Expression of the Oct-1 transcription factor and characterization of its interactions with the Bob1 coactivator. <i> Lee L, Stollar E, Chang J, Grossmann JG, O'Brien R, Ladbury J, Carpenter B, Roberts S, Luisi B. </i> Biochemistry, 2001","term_id":"GO:0098772","curator_id":"zdosztanyi","start":1,"term_ontology":"GO","curator_name":"Zsuzsanna Dosztányi","reference_id":"11380252","version":3,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00231r002","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":200,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Expression of the Oct-1 transcription factor and characterization of its interactions with the Bob1 coactivator. <i> Lee L, Stollar E, Chang J, Grossmann JG, O'Brien R, Ladbury J, Carpenter B, Roberts S, Luisi B. </i> Biochemistry, 2001","term_id":"GO:0005515","curator_id":"zdosztanyi","start":1,"term_ontology":"GO","curator_name":"Zsuzsanna Dosztányi","reference_id":"11380252","version":3,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00231r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":200,"region_id":"DP00231r004","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Expression of the Oct-1 transcription factor and characterization of its interactions with the Bob1 coactivator. <i> Lee L, Stollar E, Chang J, Grossmann JG, O'Brien R, Ladbury J, Carpenter B, Roberts S, Luisi B. </i> Biochemistry, 2001","term_id":"IDPO:0000002","curator_id":"zdosztanyi","start":1,"term_ontology":"IDPO","curator_name":"Zsuzsanna Dosztányi","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"11380252","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":200,"term_name":"molecular function regulator","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","reference_html":"Expression of the Oct-1 transcription factor and characterization of its interactions with the Bob1 coactivator. <i> Lee L, Stollar E, Chang J, Grossmann JG, O'Brien R, Ladbury J, Carpenter B, Roberts S, Luisi B. </i> Biochemistry, 2001","term_id":"GO:0098772","curator_id":"zdosztanyi","start":1,"term_ontology":"GO","curator_name":"Zsuzsanna Dosztányi","reference_id":"11380252","version":3,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","region_id":"DP00231r005","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":200,"term_name":"protein binding","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","reference_html":"Expression of the Oct-1 transcription factor and characterization of its interactions with the Bob1 coactivator. <i> Lee L, Stollar E, Chang J, Grossmann JG, O'Brien R, Ladbury J, Carpenter B, Roberts S, Luisi B. </i> Biochemistry, 2001","term_id":"GO:0005515","curator_id":"zdosztanyi","start":1,"term_ontology":"GO","curator_name":"Zsuzsanna Dosztányi","reference_id":"11380252","version":3,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","region_id":"DP00231r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":379,"region_id":"DP00231r007","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules. <i> Klemm JD, Rould MA, Aurora R, Herr W, Pabo CO. </i> Cell, 1994","term_id":"IDPO:0000002","curator_id":"zdosztanyi","start":355,"term_ontology":"IDPO","curator_name":"Zsuzsanna Dosztányi","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1OCT"}],"reference_id":"8156594","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":379,"term_name":"flexible linker","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules. <i> Klemm JD, Rould MA, Aurora R, Herr W, Pabo CO. </i> Cell, 1994","term_id":"IDPO:0000033","curator_id":"zdosztanyi","start":355,"term_ontology":"IDPO","curator_name":"Zsuzsanna Dosztányi","reference_id":"8156594","version":3,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00231r008","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_P14859","date":"2016-09-08T12:37:12.000Z","acc":"P14859","name":"POU domain, class 2, transcription factor 1","length":743,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000163B4E","genes":[{"name":{"value":"POU2F1"},"synonyms":[{"value":"OCT1"},{"value":"OTF1"}]}],"alphafold_very_low_content":0.7375504710632571,"disorder_content":0.3028263795423957,"disprot_consensus":{"full":[{"start":1,"end":200,"type":"D"},{"start":355,"end":379,"type":"D"}],"Structural state":[{"start":1,"end":200,"type":"D"},{"start":355,"end":379,"type":"D"}],"Molecular function":[{"start":1,"end":200,"type":"F"}],"Disorder function":[{"start":355,"end":379,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00147","name":"Fibrinogen beta and gamma chains, C-terminal globular domain","start":504,"end":737},{"id":"PF08702","name":"Fibrinogen alpha/beta chain family","start":49,"end":191},{"id":"PF12160","name":"Fibrinogen alpha C domain","start":302,"end":345}],"gene3D":[{"start":45,"end":236,"id":"1.20.5.50","name":"1.20.5.50"}]},"uniref50":"UniRef50_P14448","sequence":"MIPVTILCVLLCLNLAWAQDGKTTFEKEGGGGRGPRILENMHESSCKYEKNWPICVDDDWGTKCPSCCRMQGIIDDTDQNYSQRIDNIRQQLADSQNKYKTSNRVIVETINILKPGLEGAQQLDENYGHVSTELRRRIVTLKQRVATQVNRIKALQNSIQEQVVEMKRLEVDIDIKIRACKGSCARSFDYQVDKEGYDNIQKHLTQASSIDMHPDFQTTTLSTLKMRPLKDSNVPEHFKLKPSPEMQAMSAFNNIKQMQVVLERPETDHVAEARGDSSPSHTGKLITSSHRRESPSLVDKTSSASSVHRCTRTVTKKVISGPDGPREEIVEKMVSSDGSDCSHLQGGREGSTYHFSGTGDFHKLDRLLPDLESFFTHDSVSTSSRHSIGSSTSSHVTGAGSSHLGTGGKDKFTDLGEEEEDDFGGLQPSGFAAGSASHSKTVLTSSSSSFNKGGSTFETKSLKTRETSEQLGGVQHDQSAEDTPDFKARSFRPAAMSTRRSYNGKDCDDIRQKHTSGAKSGIFKIKPEGSNKVLSVYCDQETTLGGWLLIQQRMDGSVNFNRTWQDYRRGFGSVDGKGQGELWLGNENIHLLTQNDTLLRVELEDWDGNAAYAEYIVQVGTEAEGYALTVSSYEGTAGDALVAGWLEEGSEYTSHAQMQFSTFDRDQDHWEESCAEVYGGGWWYNSCQAANLNGIYYPGGHYDPRYNVPYEIENGVVWIPFRASDYSLKVVRMKIRPLETL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Phasianinae","Gallus"],"uniref90":"UniRef90_P14448","disprot_id":"DP00233","ncbi_taxon_id":9031,"regions_counter":2,"creator":"eleonardi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":44,"region_id":"DP00233r001","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Crystal structure of native chicken fibrinogen at 2.7 A resolution. <i> Yang Z, Kollman JM, Pandi L, Doolittle RF. </i> Biochemistry, 2001","term_id":"IDPO:0000002","curator_id":"vnugnes","start":19,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-02-15T15:05:24.931Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1M1J"}],"reference_id":"11601975","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q02020"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"28009","entry_name":"N-acetyl-beta-D-glucosamine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"44278","entry_name":"N-acetyl-alpha-D-glucosamine"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O93568"}],"statement":[{"text":"The amino-terminal segments of the α and β chains, including fibrinopeptides A and B, are not visible in electron density maps, however, and must be highly disordered. The αC domain is also very disordered.","type":"Abstract"},{"text":"Electron density maps barely reveal the outlines of the disordered carboxyl regions of the α chains (Figure 2), and the amino-terminal segments of the α and β chains, including fibrinopeptides A and B, could not be resolved. The reasonable R-factors found after refinement (Table 1) indicate that these parts of the molecule do not contribute significantly to the diffraction and must be highly disordered. That the missing portions had not been lost to degradation during incubations leading to crystallization was ascertained by SDS gels and amino-terminal sequencing.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":505,"region_id":"DP00233r002","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Crystal structure of native chicken fibrinogen at 2.7 A resolution. <i> Yang Z, Kollman JM, Pandi L, Doolittle RF. </i> Biochemistry, 2001","term_id":"IDPO:0000002","curator_id":"vnugnes","start":239,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-02-15T15:09:39.838Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1M1J"}],"reference_id":"11601975","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q02020"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O93568"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"28009","entry_name":"N-acetyl-beta-D-glucosamine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"44278","entry_name":"N-acetyl-alpha-D-glucosamine"}],"statement":[{"text":"The αC domain is also very disordered.","type":"Abstract"},{"text":"The disordered αC domains reside in the sinuses of the coiled coils mostly away from the central domain (Figure 2).","type":"Results"},{"text":"Electron density maps barely reveal the outlines of the disordered carboxyl regions of the α chains (Figure 2), and the amino-terminal segments of the α and β chains, including fibrinopeptides A and B, could not be resolved. The reasonable R-factors found after refinement (Table 1) indicate that these parts of the molecule do not contribute significantly to the diffraction and must be highly disordered. That the missing portions had not been lost to degradation during incubations leading to crystallization was ascertained by SDS gels and amino-terminal sequencing.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P14448","date":"2016-09-04T18:46:34.000Z","acc":"P14448","name":"Fibrinogen alpha chain","length":741,"organism":"Gallus gallus","dataset":[],"UniParc":"UPI000059C9D0","genes":[{"name":{"value":"FGA"}}],"alphafold_very_low_content":0.34143049932523617,"disorder_content":0.39541160593792174,"disprot_consensus":{"full":[{"start":19,"end":44,"type":"D"},{"start":239,"end":505,"type":"D"}],"Structural state":[{"start":19,"end":44,"type":"D"},{"start":239,"end":505,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01669","name":"Myelin basic protein","start":149,"end":304}]},"uniref50":"UniRef50_P02686","sequence":"MGNHAGKRELNAEKASTNSETNRGESEKKRNLGELSRTTSEDNEVFGEADANQNNGTSSQDTAVTDSKRTADPKNAWQDAHPADPGSRPHLIRLFSRDAPGREDNTFKDRPSESDELQTIQEDSAATSESLDVMASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFGGDRGAPKRGSGKDSHHPARTAHYGSLPQKSHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQRPGFGYGGRASDYKSAHKGFKGVDAQGTLSKIFKLGGRDSRSGSPMARR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P02686","disprot_id":"DP00236","ncbi_taxon_id":9606,"regions_counter":10,"creator":"ldobson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":304,"region_id":"DP00236r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Three isoforms of human myelin basic protein: purification and structure. <i> Deibler GE, Burlin TV, Stone AL. </i> J Neurosci Res, 1995","term_id":"IDPO:0000002","curator_id":"droche","start":134,"term_ontology":"IDPO","curator_name":"Daniel Roche","reference_id":"7500383","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":219,"end":229,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T14:06:53.224Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"6857"}],"region_id":"DP00236r004","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:162343649"}],"statement":[{"text":"The CSI analyses of our assignments, shown in Fig. 3, indicate a noticeable tendency of a central 10-residue segment of the polypeptide to adopt a helical conformation from residues 5′ to 14′, for samples in TFE-d2 (Fig. 3B) and in DPC-d38 (Fig. 3C), but not in KCl (Fig. 3A).","type":"Results"}]},{"start":215,"end":231,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T14:05:16.379Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"6857"}],"region_id":"DP00236r005","statement":[{"text":"The CSI analyses of our assignments, shown in Fig. 3, indicate a noticeable tendency of a central 10-residue segment of the polypeptide to adopt a helical conformation from residues 5′ to 14′, for samples in TFE-d2 (Fig. 3B) and in DPC-d38 (Fig. 3C), but not in KCl (Fig. 3A).","type":"Results"}]},{"start":215,"end":231,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T14:12:57.874Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00236r006","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:162343649"}],"statement":[{"text":"In aqueous solution (pure water, and 100 mm KCl, pH 6.5), the spectra indicated that the polypeptide had little or no regular secondary structure. In organic and membrane-mimetic conditions (30% TFE and 20 mm DPC, respectively), the spectra clearly indicated an α-helical conformation.","type":"Results"}]},{"start":215,"end":231,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T14:13:47.765Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00236r007","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:162343649"}],"statement":[{"text":"In aqueous solution (pure water, and 100 mm KCl, pH 6.5), the spectra indicated that the polypeptide had little or no regular secondary structure. In organic and membrane-mimetic conditions (30% TFE and 20 mm DPC, respectively), the spectra clearly indicated an α-helical conformation.","type":"Results"}],"states_connection":[{"source":"DP00236r008","target":"DP00236r006"}]},{"start":215,"end":231,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T14:13:28.459Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00236r008","statement":[{"text":"In aqueous solution (pure water, and 100 mm KCl, pH 6.5), the spectra indicated that the polypeptide had little or no regular secondary structure. In organic and membrane-mimetic conditions (30% TFE and 20 mm DPC, respectively), the spectra clearly indicated an α-helical conformation.","type":"Results"}]},{"start":219,"end":229,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T14:28:41.698Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006287","ec_ontology":"ECO","ec_name":"electron paramagnetic resonance evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"78018","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00236r009","statement":[{"text":"These results demonstrate that the polypeptide α helix forms distinct hydrophobic and electrostatic contacts with the DPC micelles, and are in agreement with the SDSL/EPR mapping and positioning of the α-helical model of this epitope of MBP on the surface of a lipid bilayer [6,7].","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":215,"end":230,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T14:29:49.043Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"78018","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00236r010","statement":[{"text":"In aqueous solution (pure water, and 100 mm KCl, pH 6.5), the spectra indicated that the polypeptide had little or no regular secondary structure. In organic and membrane-mimetic conditions (30% TFE and 20 mm DPC, respectively), the spectra clearly indicated an α-helical conformation.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_P02686","date":"2016-09-06T13:45:10.000Z","acc":"P02686","name":"Myelin basic protein","length":304,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000113626","genes":[{"name":{"value":"MBP"}}],"alphafold_very_low_content":0.3815789473684211,"disorder_content":0.5625,"disprot_consensus":{"full":[{"start":134,"end":214,"type":"D"},{"start":215,"end":231,"type":"T"},{"start":232,"end":304,"type":"D"}],"Structural state":[{"start":134,"end":304,"type":"D"}],"Structural transition":[{"start":215,"end":231,"type":"T"}],"Molecular function":[{"start":215,"end":230,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00097","name":"Zinc finger, C3HC4 type (RING finger)","start":24,"end":64},{"id":"PF00533","name":"BRCA1 C Terminus (BRCT) domain","start":1645,"end":1723},{"id":"PF00533","name":"BRCA1 C Terminus (BRCT) domain","start":1758,"end":1841},{"id":"PF12820","name":"Serine-rich domain associated with BRCT","start":345,"end":508}],"gene3D":[{"start":1756,"end":1859,"id":"3.40.50.10190","name":"BRCT domain"},{"start":1646,"end":1755,"id":"3.40.50.10190","name":"BRCT domain"},{"start":1,"end":112,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"}]},"uniref50":"UniRef50_P38398","sequence":"MDLSALRVEEVQNVINAMQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNDITKRSLQESTRFSQLVEELLKIICAFQLDTGLEYANSYNFAKKENNSPEHLKDEVSIIQSMGYRNRAKRLLQSEPENPSLQETSLSVQLSNLGTVRTLRTKQRIQPQKTSVYIELGSDSSEDTVNKATYCSVGDQELLQITPQGTRDEISLDSAKKAACEFSETDVTNTEHHQPSNNDLNTTEKRAAERHPEKYQGSSVSNLHVEPCGTNTHASSLQHENSSLLLTKDRMNVEKAEFCNKSKQPGLARSQHNRWAGSKETCNDRRTPSTEKKVDLNADPLCERKEWNKQKLPCSENPRDTEDVPWITLNSSIQKVNEWFSRSDELLGSDDSHDGESESNAKVADVLDVLNEVDEYSGSSEKIDLLASDPHEALICKSERVHSKSVESNIEDKIFGKTYRKKASLPNLSHVTENLIIGAFVTEPQIIQERPLTNKLKRKRRPTSGLHPEDFIKKADLAVQKTPEMINQGTNQTEQNGQVMNITNSGHENKTKGDSIQNEKNPNPIESLEKESAFKTKAEPISSSISNMELELNIHNSKAPKKNRLRRKSSTRHIHALELVVSRNLSPPNCTELQIDSCSSSEEIKKKKYNQMPVRHSRNLQLMEGKEPATGAKKSNKPNEQTSKRHDSDTFPELKLTNAPGSFTKCSNTSELKEFVNPSLPREEKEEKLETVKVSNNAEDPKDLMLSGERVLQTERSVESSSISLVPGTDYGTQESISLLEVSTLGKAKTEPNKCVSQCAAFENPKGLIHGCSKDNRNDTEGFKYPLGHEVNHSRETSIEMEESELDAQYLQNTFKVSKRQSFAPFSNPGNAEEECATFSAHSGSLKKQSPKVTFECEQKEENQGKNESNIKPVQTVNITAGFPVVGQKDKPVDNAKCSIKGGSRFCLSSQFRGNETGLITPNKHGLLQNPYRIPPLFPIKSFVKTKCKKNLLEENFEEHSMSPEREMGNENIPSTVSTISRNNIRENVFKEASSSNINEVGSSTNEVGSSINEIGSSDENIQAELGRNRGPKLNAMLRLGVLQPEVYKQSLPGSNCKHPEIKKQEYEEVVQTVNTDFSPYLISDNLEQPMGSSHASQVCSETPDDLLDDGEIKEDTSFAENDIKESSAVFSKSVQKGELSRSPSPFTHTHLAQGYRRGAKKLESSEENLSSEDEELPCFQHLLFGKVNNIPSQSTRHSTVATECLSKNTEENLLSLKNSLNDCSNQVILAKASQEHHLSEETKCSASLFSSQCSELEDLTANTNTQDPFLIGSSKQMRHQSESQGVGLSDKELVSDDEERGTGLEENNQEEQSMDSNLGEAASGCESETSVSEDCSGLSSQSDILTTQQRDTMQHNLIKLQQEMAELEAVLEQHGSQPSNSYPSIISDSSALEDLRNPEQSTSEKAVLTSQKSSEYPISQNPEGLSADKFEVSADSSTSKNKEPGVERSSPSKCPSLDDRWYMHSCSGSLQNRNYPSQEELIKVVDVEEQQLEESGPHDLTETSYLPRQDLEGTPYLESGISLFSDDPESDPSEDRAPESARVGNIPSSTSALKVPQLKVAESAQSPAAAHTTDTAGYNAMEESVSREKPELTASTERVNKRMSMVVSGLTPEEFMLVYKFARKHHITLTNLITEETTHVVMKTDAEFVCERTLKYFLGIAGGKWVVSYFWVTQSIKERKMLNEHDFEVRGDVVNGRNHQGPKRARESQDRKIFRGLEICCYGPFTNMPTDQLEWMVQLCGASVVKELSSFTLGTGVHPIVVVQPDAWTEDNGFHAIGQMCEAPVVTREWVLDSVALYQCQELDTYLIPQIPHSHY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P38398","disprot_id":"DP00238","ncbi_taxon_id":9606,"regions_counter":29,"creator":"aschramm","regions":[{"start":100,"end":1649,"reference_id":"15571721","reference_source":"pmid","reference_html":"Characterization of segments from the central region of BRCA1: an intrinsically disordered scaffold for multiple protein-protein and protein-DNA interactions? <i> Mark WY, Liao JC, Lu Y, Ayed A, Laister R, Szymczyna B, Chakrabartty A, Arrowsmith CH. </i> J Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00238r008","statement":[{"text":"Here we used NMR spectroscopy in conjunction with CD spectroscopy and limited proteolysis to investigate the biophysical properties of the approximately 1500 residue central region of BRCA1. Our results show that although there are a few small, mildly protease-resistant regions, the majority of the BRCA1 central region lacks any pre-existing independently folded globular domains.","type":"Abstract"},{"text":"NMR spectroscopy was used to characterize the structure of the central region. 1H–15N HSQC spectra were acquired for fragments #2–#21. As shown in Figure 2(A) and Supplementary Figure 1, all 20 proteins had spectra that reflected soluble, non-aggregated, but disordered proteins. Each fragment has very little chemical shift dispersion in the 1H dimension of the HSQC spectrum, and the peak widths were narrow, both features of disordered proteins.","type":"Results"},{"text":"1H–15N HSQC NMR spectra. The majority of the peaks are clustered in between 7.5 ppm and 8.5 ppm in the 1H dimension, indicating an unfolded protein.","type":"Figure"},{"text":"These data taken together suggest that a large portion of the central region of BRCA1 does not contain stable, independently folded domains in the absence of binding partners.","type":"Results"},{"text":"Due to the difficulties in purifying large amounts of the full-length BRCA149 for biophysical analysis, we have designed 20 soluble fragments of BRCA1 and used three biophysical assays to demonstrate that fragments #2–#21 encompassing the central region of BRCA1 are mostly intrinsically disordered, with the possibility of having some small secondary structural elements.","type":"Discussion"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:23:44.298Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":100,"end":1649,"reference_id":"15571721","reference_source":"pmid","reference_html":"Characterization of segments from the central region of BRCA1: an intrinsically disordered scaffold for multiple protein-protein and protein-DNA interactions? <i> Mark WY, Liao JC, Lu Y, Ayed A, Laister R, Szymczyna B, Chakrabartty A, Arrowsmith CH. </i> J Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00238r009","statement":[{"text":"Here we used NMR spectroscopy in conjunction with CD spectroscopy and limited proteolysis to investigate the biophysical properties of the approximately 1500 residue central region of BRCA1. Our results show that although there are a few small, mildly protease-resistant regions, the majority of the BRCA1 central region lacks any pre-existing independently folded globular domains.","type":"Abstract"},{"text":"In order to test for the presence of secondary structure, circular dichroism (CD) spectroscopy was next utilized. Again, most fragments had similar CD spectra reflective of very little secondary structure. Most fragments had a slight minimum near 220 nm (mean residue ellipticity (MRE)∼3000) suggestive of a very small amount of α-helix and a much stronger minimum near 200 nm reflecting a predominantly disordered protein (Figure 2(B) and Supplementary Figure 2).","type":"Results"},{"text":"Circular dichroism spectra. Weak signal at 220 nm may reflect a small amount of helical content, but the majority of these peptides are disordered as evidenced by the minimum near 203–208 nm.","type":"Figure"},{"text":"These data taken together suggest that a large portion of the central region of BRCA1 does not contain stable, independently folded domains in the absence of binding partners.","type":"Results"},{"text":"Due to the difficulties in purifying large amounts of the full-length BRCA149 for biophysical analysis, we have designed 20 soluble fragments of BRCA1 and used three biophysical assays to demonstrate that fragments #2–#21 encompassing the central region of BRCA1 are mostly intrinsically disordered, with the possibility of having some small secondary structural elements.","type":"Discussion"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:23:42.844Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":100,"end":1649,"reference_id":"15571721","reference_source":"pmid","reference_html":"Characterization of segments from the central region of BRCA1: an intrinsically disordered scaffold for multiple protein-protein and protein-DNA interactions? <i> Mark WY, Liao JC, Lu Y, Ayed A, Laister R, Szymczyna B, Chakrabartty A, Arrowsmith CH. </i> J Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00238r010","statement":[{"text":"Here we used NMR spectroscopy in conjunction with CD spectroscopy and limited proteolysis to investigate the biophysical properties of the approximately 1500 residue central region of BRCA1. Our results show that although there are a few small, mildly protease-resistant regions, the majority of the BRCA1 central region lacks any pre-existing independently folded globular domains.","type":"Abstract"},{"text":"As a final test for the existence of folded globular domains, limited proteolysis was performed to see if there were any stable, protease-resistant domains in the central region. Most constructs were degraded by trypsin within minutes compared to a positive control using malate synthase, a globular protein which took more than 21 hours to start to degrade under the same conditions (Figure 2(C) and Supplementary Figure 3).","type":"Results"},{"text":"SDS-PAGE of aliquots from a proteolysis time course monitored over 21 hours after incubation with trypsin. In contrast to the globular enzyme malate synthase which is largely resistant to protease digestion for more than 21 hours (Supplementary Figure 3(A)), these constructs are digested by trypsin within ten minutes.","type":"Figure"},{"text":"These data taken together suggest that a large portion of the central region of BRCA1 does not contain stable, independently folded domains in the absence of binding partners.","type":"Results"},{"text":"Due to the difficulties in purifying large amounts of the full-length BRCA149 for biophysical analysis, we have designed 20 soluble fragments of BRCA1 and used three biophysical assays to demonstrate that fragments #2–#21 encompassing the central region of BRCA1 are mostly intrinsically disordered, with the possibility of having some small secondary structural elements.","type":"Discussion"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:23:41.365Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":498,"end":663,"reference_id":"15571721","reference_source":"pmid","reference_html":"Characterization of segments from the central region of BRCA1: an intrinsically disordered scaffold for multiple protein-protein and protein-DNA interactions? <i> Mark WY, Liao JC, Lu Y, Ayed A, Laister R, Szymczyna B, Chakrabartty A, Arrowsmith CH. </i> J Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00238r011","statement":[{"text":"Electrophoretic mobility shift assay and intrinsic tryptophan fluorescence experiments also demonstrate that, although intrinsically disordered, polypeptides from the central region are able to mediate interactions with DNA and p53 with affinities in the low micromolar range. This supports a model in which the central region may act as a long flexible scaffold for intermolecular interactions, thereby helping to integrate multiple signals in the DNA damage response pathway.","type":"Abstract"},{"text":"The region previously reported to bind non-specifically to DNA (residues 452–1079) is relatively large (>600 residues), yet appears to be largely disordered. Since DNA binding domains are often small (∼60–150), we therefore suspected that the DNA binding region might actually comprise an even smaller region of BRCA1. Each of the 20 soluble fragments were assayed for binding to a 31 bp double-stranded DNA (Figure 3). Fragments #5–#7, #10, #11, #17, #18, #20 and #21 demonstrated DNA binding at protein concentrations in the low micromolar range. Accounting for the overlapping nature of the constructs, these binding experiments implicate two regions in DNA binding, residues 498–663 (DB1) and 936–1057 (DB2).","type":"Results"},{"text":"The region previously reported to bind non-specifically to DNA (residues 452–1079) is relatively large (>600 residues), yet appears to be largely disordered. Since DNA binding domains are often small (∼60–150), we therefore suspected that the DNA binding region might actually comprise an even smaller region of BRCA1. Each of the 20 soluble fragments were assayed for binding to a 31 bp double-stranded DNA (Figure 3). Fragments #5–#7, #10, #11, #17, #18, #20 and #21 demonstrated DNA binding at protein concentrations in the low micromolar range. Accounting for the overlapping nature of the constructs, these binding experiments implicate two regions in DNA binding, residues 498–663 (DB1) and 936–1057 (DB2).","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:23:57.578Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":936,"end":1057,"reference_id":"15571721","reference_source":"pmid","reference_html":"Characterization of segments from the central region of BRCA1: an intrinsically disordered scaffold for multiple protein-protein and protein-DNA interactions? <i> Mark WY, Liao JC, Lu Y, Ayed A, Laister R, Szymczyna B, Chakrabartty A, Arrowsmith CH. </i> J Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00238r012","statement":[{"text":"Electrophoretic mobility shift assay and intrinsic tryptophan fluorescence experiments also demonstrate that, although intrinsically disordered, polypeptides from the central region are able to mediate interactions with DNA and p53 with affinities in the low micromolar range. This supports a model in which the central region may act as a long flexible scaffold for intermolecular interactions, thereby helping to integrate multiple signals in the DNA damage response pathway.","type":"Abstract"},{"text":"The region previously reported to bind non-specifically to DNA (residues 452–1079) is relatively large (>600 residues), yet appears to be largely disordered. Since DNA binding domains are often small (∼60–150), we therefore suspected that the DNA binding region might actually comprise an even smaller region of BRCA1. Each of the 20 soluble fragments were assayed for binding to a 31 bp double-stranded DNA (Figure 3). Fragments #5–#7, #10, #11, #17, #18, #20 and #21 demonstrated DNA binding at protein concentrations in the low micromolar range. Accounting for the overlapping nature of the constructs, these binding experiments implicate two regions in DNA binding, residues 498–663 (DB1) and 936–1057 (DB2).","type":"Results"},{"text":"The region previously reported to bind non-specifically to DNA (residues 452–1079) is relatively large (>600 residues), yet appears to be largely disordered. Since DNA binding domains are often small (∼60–150), we therefore suspected that the DNA binding region might actually comprise an even smaller region of BRCA1. Each of the 20 soluble fragments were assayed for binding to a 31 bp double-stranded DNA (Figure 3). Fragments #5–#7, #10, #11, #17, #18, #20 and #21 demonstrated DNA binding at protein concentrations in the low micromolar range. Accounting for the overlapping nature of the constructs, these binding experiments implicate two regions in DNA binding, residues 498–663 (DB1) and 936–1057 (DB2).","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:23:56.078Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":219,"end":498,"reference_id":"15571721","reference_source":"pmid","reference_html":"Characterization of segments from the central region of BRCA1: an intrinsically disordered scaffold for multiple protein-protein and protein-DNA interactions? <i> Mark WY, Liao JC, Lu Y, Ayed A, Laister R, Szymczyna B, Chakrabartty A, Arrowsmith CH. </i> J Mol Biol, 2005","date":"2022-06-27T13:47:37.146Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0002039","term_name":"p53 binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","released":"2022_06","version":4,"region_id":"DP00238r013","statement":[{"text":"Electrophoretic mobility shift assay and intrinsic tryptophan fluorescence experiments also demonstrate that, although intrinsically disordered, polypeptides from the central region are able to mediate interactions with DNA and p53 with affinities in the low micromolar range. This supports a model in which the central region may act as a long flexible scaffold for intermolecular interactions, thereby helping to integrate multiple signals in the DNA damage response pathway.","type":"Abstract"},{"text":"A small region of BRCA1 binds weakly to p53","type":"Results"},{"text":"Another part of central BRCA1 that has been reported to interact with other molecules is the region from residues 224 to 500. Zhang et al.31 mapped its interaction, in vitro, to the C-terminal domain of p53 and suggested that such physical association could regulate gene expression through BRCA1-dependent stimulation of p53-mediated transcription. To investigate the strength of the interaction, we measured quenching of the intrinsic tryptophan fluorescence of BRCA1 fragment #19 (residues 219–498) upon binding to various p53 C-terminal domains (residues 311–393, 310–360 and 355–393).","type":"Results"},{"text":"As shown in the titration curves in Figure 4 both the p53 C terminus (residues 311–393), which contains the tetramerization domain, and the p53 basic region (residues 355–393) bound to BRCA1 with relatively weak affinity (Kd values of ∼15 μM and ∼68 μM, respectively).","type":"Results"},{"text":"Analysis of p53 binding to BRCA1 by intrinsic tryptophan fluorescence. BRCA1 (residues 219–498) which includes four tryptophan residues was incubated with increasing amounts of p53 peptides 311–393 (●), 355–393 (▴) or 310–360 (□) which all lack a tryptophan residue. Binding was assessed by measuring the total tryptophan fluorescence at 354 nm, using an excitation wavelength of 295 nm. The change in fluorescence signal, as compared with BRCA1 (residues 219–498) alone, was plotted as a function of target peptide concentration.","type":"Figure"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to one of the p53 family of proteins.\" [GOC:hjd]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P04637","operator":null,"partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-27T13:52:09.355Z"}},{"start":175,"end":303,"reference_id":"9788437","reference_source":"pmid","reference_html":"BRCA1 binds c-Myc and inhibits its transcriptional and transforming activity in cells. <i> Wang Q, Zhang H, Kajino K, Greene MI. </i> Oncogene, 1998","date":"2022-06-27T13:45:24.403Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","released":"2022_06","version":4,"region_id":"DP00238r014","statement":[{"text":"We next generated a series of Gal4BD-BRCA1 deletion mutants to map the regions required for interaction with c-Myc. As shown in Figure 1, a small segment of BRCA1 (amino acid residue 433-511, as in pGalBD-BRMS) is both required and sufficient for binding to c-Myc. We designated this region MB1 (for Myc-binding region 1). An N-terminal Myc-binding region (termed MB2) of BRCA1 requires amino acid residues 175-303.","type":"Results"},{"text":"This region corresponds to the first binding site of c-Myc, MB1.","type":"Curator statement"}],"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P01106","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-27T13:52:13.379Z"}},{"start":433,"end":511,"reference_id":"9788437","reference_source":"pmid","reference_html":"BRCA1 binds c-Myc and inhibits its transcriptional and transforming activity in cells. <i> Wang Q, Zhang H, Kajino K, Greene MI. </i> Oncogene, 1998","date":"2022-06-27T13:45:13.074Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","released":"2022_06","version":4,"region_id":"DP00238r015","statement":[{"text":"We next generated a series of Gal4BD-BRCA1 deletion mutants to map the regions required for interaction with c-Myc. As shown in Figure 1, a small segment of BRCA1 (amino acid residue 433-511, as in pGalBD-BRMS) is both required and sufficient for binding to c-Myc. We designated this region MB1 (for Myc-binding region 1). An N-terminal Myc-binding region (termed MB2) of BRCA1 requires amino acid residues 175-303.","type":"Results"},{"text":"This region corresponds to the second binding site of c-Myc, MB2.","type":"Curator statement"}],"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P01106","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-27T13:52:20.242Z"}},{"start":304,"end":394,"reference_id":"10518542","reference_source":"pmid","reference_html":"BRCA1-associated growth arrest is RB-dependent. <i> Aprelikova ON, Fang BS, Meissner EG, Cotter S, Campbell M, Kuthiala A, Bessho M, Jensen RA, Liu ET. </i> Proc Natl Acad Sci U S A, 1999","date":"2022-06-27T13:39:36.353Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","released":"2022_06","version":5,"region_id":"DP00238r018","statement":[{"text":"We further found that the BRCA1 protein complexes with the hypophosphorylated form of pRb. This binding is localized to amino acids 304–394 of BRCA1 protein and requires the ABC domain of pRb.","type":"Abstract"},{"text":"The NH2-terminal 394 aa (ScC7 fragment, amino acids 1–394) also showed stable binding to GST-Rb ABC protein (Fig.6B). However, further truncation of BRCA1 (N-R, amino acids 1–303) completely eliminated the interaction with GST-Rb ABC.","type":"Results"},{"text":"To further demonstrate the binding of pRb to BRCA1, we reversed the probe and target proteins by using GST fusion proteins with BRCA1 fragments GST-N-R (amino acids 1–303) and GST-R-K (amino acids 304–772 shown in Fig. ​Fig.66A) as probe proteins and pRb as target. As before, in vitro-translated Rb protein bound the GST-R-K fragment containing previously identified pRb binding domain in exon 11, but not with the GST-N-R protein or GST alone (Fig. ​(Fig.66C).","type":"Results"},{"text":"BRCA1 Protein Binds to the Hypophosphorylated Form of pRb.","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P06400","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-27T13:54:07.153Z"}},{"start":304,"end":394,"reference_id":"10518542","reference_source":"pmid","reference_html":"BRCA1-associated growth arrest is RB-dependent. <i> Aprelikova ON, Fang BS, Meissner EG, Cotter S, Campbell M, Kuthiala A, Bessho M, Jensen RA, Liu ET. </i> Proc Natl Acad Sci U S A, 1999","date":"2022-06-27T13:32:30.202Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0030308","term_name":"negative regulation of cell growth","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","released":"2022_06","version":4,"region_id":"DP00238r019","statement":[{"text":"BRCA1-associated growth arrest is RB-dependent","type":"Title"},{"text":"Deletion of Amino Acids 303–394 from BRCA1 Protein Inactivates Its Growth-Suppressive Property.","type":"Results"},{"text":"To test the biological role of Rb-BRCA1 interaction, we performed an in-frame deletion of the 92 aa (amino acids 303–394) from BRCA1 which comprised the putative binding region for Rb protein. When used in colony formation assay, BRCA1-delta90 had no effect on growth control (Fig.8). A construct generating the COOH-terminal truncation of BRCA1 was also ineffective in inhibiting colony formation.","type":"Results"},{"text":"A mutant BRCA1 protein bearing a deletion of the Rb binding domain does not suppress cell growth. Colony formation assay was performed in U2OS cells (as in Fig.1) with wild-type BRCA1 or BRCA1 bearing an in-frame deletion of 90 aa (amino acids 303–394) or a COOH-terminal truncation. Each transfection was done in triplicate in three independent experiments.","type":"Figure"}],"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate, extent or direction of cell growth.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-27T13:54:43.864Z"}},{"start":758,"end":1064,"reference_id":"9008167","reference_source":"pmid","reference_html":"Association of BRCA1 with Rad51 in mitotic and meiotic cells. <i> Scully R, Chen J, Plug A, Xiao Y, Weaver D, Feunteun J, Ashley T, Livingston DM. </i> Cell, 1997","date":"2022-06-27T13:29:22.327Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","released":"2022_06","version":4,"region_id":"DP00238r020","statement":[{"text":"BRCA1 residues 758-1064 alone formed Rad51-containing complexes in vitro. Rad51 is also specifically associated with developing synaptonemal complexes in meiotic cells, and BRCA1 and Rad51 were both detected on asynapsed (axial) elements of human synaptonemal complexes. These findings suggest a functional interaction between BRCA1 and Rad51 in the meiotic and mitotic cell cycles, which, in turn, suggests a role for BRCA1 in the control of recombination and of genome integrity.","type":"Abstract"}],"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q06609","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-27T13:54:56.166Z"}},{"start":758,"end":1064,"reference_id":"9008167","reference_source":"pmid","reference_html":"Association of BRCA1 with Rad51 in mitotic and meiotic cells. <i> Scully R, Chen J, Plug A, Xiao Y, Weaver D, Feunteun J, Ashley T, Livingston DM. </i> Cell, 1997","date":"2022-06-23T08:19:30.736Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","released":"2022_06","version":5,"region_id":"DP00238r021","statement":[{"text":"BRCA1 and Rad51 Colocalize in Discrete Nuclear Foci","type":"Figure"},{"text":"Here, we report that BRCA1 and hRad51 colocalize in S phase cells, interact physically, and, in keeping with previous reports of the behavior of hRad51 (2, 53), share common space on the surfaces of zygotene and pachytene meiotic chromosomes.","type":"Introduction"},{"text":"This suggested that the colocalization of BRCA1 and Rad51 is conditional or transient, even in S phase cells. Similar colocalization results were obtained in WI38 and CV-1 cells.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-23T13:41:42.952Z"}},{"start":740,"end":1083,"reference_id":"12354784","reference_source":"pmid","reference_html":"BRCA1 interacts directly with the Fanconi anemia protein FANCA. <i> Folias A, Matkovic M, Bruun D, Reid S, Hejna J, Grompe M, D'Andrea A, Moses R. </i> Hum Mol Genet, 2002","date":"2022-03-09T08:56:28.324Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005805","ec_ontology":"ECO","ec_name":"yeast 2-hybrid evidence used in manual assertion","released":"2022_03","version":4,"region_id":"DP00238r022","statement":[{"text":"Among the known FANC proteins, we find evidence for direct interaction only between the FANCA protein and BRCA1. The evidence rests on three different tests: yeast two-hybrid analysis, coimmunoprecipitation from in vitro synthesis, and coimmunoprecipitation from cell extracts. The amino terminal portion of FANCA and the central part (aa 740-1083) of BRCA1 contain the sites of interaction. The interaction does not depend on DNA damage, thus FANCA and BRCA1 are constitutively interacting. The demonstrated interaction directly connects BRCA1 to the FA pathway of DNA repair.","type":"Abstract"},{"text":"FANCA and BRCA1 interact in the yeast two-hybrid test","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"O15360","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-23T13:41:17.890Z"}},{"start":740,"end":1083,"reference_id":"12354784","reference_source":"pmid","reference_html":"BRCA1 interacts directly with the Fanconi anemia protein FANCA. <i> Folias A, Matkovic M, Bruun D, Reid S, Hejna J, Grompe M, D'Andrea A, Moses R. </i> Hum Mol Genet, 2002","date":"2022-03-08T15:21:01.161Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","released":"2022_03","version":4,"region_id":"DP00238r025","statement":[{"text":"Among the known FANC proteins, we find evidence for direct interaction only between the FANCA protein and BRCA1. The evidence rests on three different tests: yeast two-hybrid analysis, coimmunoprecipitation from in vitro synthesis, and coimmunoprecipitation from cell extracts. The amino terminal portion of FANCA and the central part (aa 740-1083) of BRCA1 contain the sites of interaction. The interaction does not depend on DNA damage, thus FANCA and BRCA1 are constitutively interacting. The demonstrated interaction directly connects BRCA1 to the FA pathway of DNA repair.","type":"Abstract"},{"text":"FANCA and BRCA1 coimmunoprecipitate in vitro","type":"Results"},{"text":"Coimmunoprecipitation of FANCA and BRCA1 in cell extracts","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"O15360","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-23T13:41:06.661Z"}},{"start":1343,"end":1440,"reference_id":"12080089","reference_source":"pmid","reference_html":"JunB potentiates function of BRCA1 activation domain 1 (AD1) through a coiled-coil-mediated interaction. <i> Hu YF, Li R. </i> Genes Dev, 2002","date":"2022-06-27T13:26:43.676Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","released":"2022_06","version":5,"region_id":"DP00238r026","statement":[{"text":"JunB potentiates function of BRCA1 activation domain 1 (AD1) through a coiled-coil-mediated interaction","type":"Title"},{"text":"BRCA1 is involved in the regulation of multiple nuclear events including transcription. AD1, one of the two trans-activation domains in BRCA1, stimulates transcription in a cell context-dependent manner. Here, it is shown that BRCA1 interacts with Jun proteins via a coiled-coil motif in AD1 and the basic leucine zipper (bZIP) region of the Jun proteins. The Jun-interacting domain in BRCA1 is critical for AD1-mediated transcriptional activation. In particular, the strength of AD1 in transcriptional activation is limited by the JunB level and ectopic expression of JunB potentiates the transcriptional activity of AD1. Furthermore, JunB mRNA expression is down-regulated in many ovarian tumor tissues examined. Thus, the coiled-coil-mediated cooperation between BRCA1 and JunB may facilitate the function of these proteins in tissue-specific transcriptional regulation and tumor suppression.","type":"Abstract"},{"text":"AD1 is necessary and sufficient for BRCA1 binding to the Jun proteins","type":"Results"},{"text":"Further deletional studies within AD1 (Fig.3, constructs 13–16) revealed a minimal JunB-binding domain (Fig.3, construct 15; amino acids 1343–1440), which consists of the coiled-coil motif and an ∼60 amino acid upstream sequence. This finding indicates that the AD1 region is both necessary and sufficient for BRCA1 binding to JunB.","type":"Results"}],"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P17275","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-27T13:55:06.752Z"}},{"start":1407,"end":1414,"reference_id":"12080089","reference_source":"pmid","reference_html":"JunB potentiates function of BRCA1 activation domain 1 (AD1) through a coiled-coil-mediated interaction. <i> Hu YF, Li R. </i> Genes Dev, 2002","date":"2022-06-27T13:21:19.690Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0045893","term_name":"positive regulation of transcription, DNA-templated","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","released":"2022_06","version":5,"region_id":"DP00238r027","statement":[{"text":"JunB potentiates function of BRCA1 activation domain 1 (AD1) through a coiled-coil-mediated interaction","type":"Title"},{"text":"BRCA1 is involved in the regulation of multiple nuclear events including transcription. AD1, one of the two trans-activation domains in BRCA1, stimulates transcription in a cell context-dependent manner. Here, it is shown that BRCA1 interacts with Jun proteins via a coiled-coil motif in AD1 and the basic leucine zipper (bZIP) region of the Jun proteins. The Jun-interacting domain in BRCA1 is critical for AD1-mediated transcriptional activation. In particular, the strength of AD1 in transcriptional activation is limited by the JunB level and ectopic expression of JunB potentiates the transcriptional activity of AD1. Furthermore, JunB mRNA expression is down-regulated in many ovarian tumor tissues examined. Thus, the coiled-coil-mediated cooperation between BRCA1 and JunB may facilitate the function of these proteins in tissue-specific transcriptional regulation and tumor suppression.","type":"Abstract"},{"text":"Substitution of two such leucines in the coiled-coil region of BRCA1 (L1407 and L1414) abrogated the BRCA1–JunB interaction (Fig.4A,B, lanes 3–5). Importantly, the same mutations also impaired the transcriptional activity of GAL4–AD in the luciferase reporter assay (Fig.4C, lanes 3–5).","type":"Results"},{"text":"Thus, the affinity of BRCA1 for the Jun proteins strongly correlates with the strength of the trans-activation domain in transcriptional stimulation.","type":"Results"}],"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription.\" [GOC:go_curators, GOC:txnOH]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu1407Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu1414Ala","start":null,"end":null,"position":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-27T14:43:16.417Z"}},{"start":758,"end":1064,"reference_id":"9008167","reference_source":"pmid","reference_html":"Association of BRCA1 with Rad51 in mitotic and meiotic cells. <i> Scully R, Chen J, Plug A, Xiao Y, Weaver D, Feunteun J, Ashley T, Livingston DM. </i> Cell, 1997","date":"2022-06-23T08:19:03.251Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0043232","term_name":"intracellular non-membrane-bounded organelle","term_namespace":"Cellular component","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0005601","ec_ontology":"ECO","ec_name":"immunofluorescence confocal microscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":2,"region_id":"DP00238r029","statement":[{"text":"BRCA1 immunostaining reveals discrete, nuclear foci during S phase of the cell cycle.","type":"Abstract"},{"text":"Here, we report that BRCA1 and hRad51 colocalize in S phase cells, interact physically, and, in keeping with previous reports of the behavior of hRad51 (2, 53), share common space on the surfaces of zygotene and pachytene meiotic chromosomes.","type":"Introduction"},{"text":"These and other results not shown here indicate that the BRCA1 nuclear dot pattern is S phase–specific.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Organized structure of distinctive morphology and function, not bounded by a lipid bilayer membrane and occurring within the cell. Includes ribosomes, the cytoskeleton and chromosomes.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-23T13:38:40.268Z"}}],"released":"2016_10","uniref100":"UniRef100_P38398","date":"2016-09-09T21:03:21.000Z","acc":"P38398","name":"Breast cancer type 1 susceptibility protein","length":1863,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins","Condensates-related proteins","RNA-binding proteins"],"UniParc":"UPI0000126AC8","genes":[{"name":{"value":"BRCA1"},"synonyms":[{"value":"RNF53"}]}],"alphafold_very_low_content":0.8030059044551798,"disorder_content":0.8319914117015567,"disprot_consensus":{"full":[{"start":100,"end":1649,"type":"D"}],"Structural state":[{"start":100,"end":1649,"type":"D"}],"Molecular function":[{"start":175,"end":663,"type":"F"},{"start":740,"end":1083,"type":"F"},{"start":1343,"end":1440,"type":"F"}],"Biological process":[{"start":304,"end":394,"type":"F"},{"start":758,"end":1064,"type":"F"},{"start":1407,"end":1414,"type":"F"}],"Cellular component":[{"start":758,"end":1064,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03063","name":"Prismane/CO dehydrogenase family","start":48,"end":620}],"gene3D":[{"start":63,"end":237,"id":"1.20.1270.30","name":"1.20.1270.30"},{"start":409,"end":636,"id":"3.40.50.2030","name":"3.40.50.2030"},{"start":238,"end":406,"id":"3.40.50.2030","name":"3.40.50.2030"}]},"uniref50":"UniRef50_P31896","sequence":"MTHHDCAHCSSDACATEMLNLAEANSIETAWHRYEKQQPQCGFGSAGLCCRICLKGPCRIDPFGEGPKYGVCGADRDTIVARHLVRMIAAGTAAHSEHGRHIALAMQHISQGELHDYSIRDEAKLYAIAKTLGVATEGRGLLAIVGDLAAITLGDFQNQDYDKPCAWLAASLTPRRVKRLGDLGLLPHNIDASVAQTMSRTHVGCDADPTNLILGGLRVAMADLDGSMLATELSDALFGTPQPVVSAANLGVMKRGAVNIAVNGHNPMLSDIICDVAADLRDEAIAAGAAEGINIIGICCTGHEVMMRHGVPLATNYLSQELPILTGALEAMVVDVQCIMPSLPRIAECFHTQIITTDKHNKISGATHVPFDEHKAVETAKTIIRMAIAAFGRRDPNRVAIPAFKQKSIVGFSAEAVVAALAKVNADDPLKPLVDNVVNGNIQGIVLFVGCNTTKVQQDSAYVDLAKSLAKRNVLVLATGCAAGAFAKAGLMTSEATTQYAGEGLKGVLSAIGTAAGLGGPLPLVMHMGSCVDNSRAVALATALANKLGVDLSDLPLVASAPECMSEKALAIGSWAVTIGLPTHVGSVPPVIGSQIVTKLVTETAKDLVGGYFIVDTDPKSAGDKLYAAIQERRAGLGL","taxonomy":["Bacteria","Proteobacteria","Alphaproteobacteria","Rhodospirillales","Rhodospirillaceae","Rhodospirillum"],"uniref90":"UniRef90_P31896","disprot_id":"DP00239","ncbi_taxon_id":1085,"regions_counter":1,"creator":"esalladini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":27,"region_id":"DP00239r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase. <i> Drennan CL, Heo J, Sintchak MD, Schreiter E, Ludden PW. </i> Proc Natl Acad Sci U S A, 2001","term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"11593006","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1JQK"}],"term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P31896","date":"2016-09-08T15:12:09.000Z","acc":"P31896","name":"Carbon monoxide dehydrogenase","length":639,"organism":"Rhodospirillum rubrum","dataset":[],"UniParc":"UPI0000113209","genes":[{"name":{"value":"cooS"}}],"alphafold_very_low_content":0.001564945226917058,"disorder_content":0.04225352112676056,"disprot_consensus":{"full":[{"start":1,"end":27,"type":"D"}],"Structural state":[{"start":1,"end":27,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00596","name":"Class II Aldolase and Adducin N-terminal domain","start":148,"end":329}],"gene3D":[{"start":135,"end":391,"id":"3.40.225.10","name":"Class II aldolase/adducin N-terminal domain"}]},"uniref50":"UniRef50_P35611","sequence":"MNGDSRAAVVTSPPPTTAPHKERYFDRVDENNPEYLRERNMAPDLRQDFNMMEQKKRVSMILQSPAFCEELESMIQEQFKKGKNPTGLLALQQIADFMTTNVPNVYPAAPQGGMAALNMSLGMVTPVNDLRGSDSIAYDKGEKLLRCKLAAFYRLADLFGWSQLIYNHITTRVNSEQEHFLIVPFGLLYSEVTASSLVKINLQGDIVDRGSTNLGVNQAGFTLHSAIYAARPDVKCVVHIHTPAGAAVSAMKCGLLPISPEALSLGEVAYHDYHGILVDEEEKVLIQKNLGPKSKVLILRNHGLVSVGESVEEAFYYIHNLVVACEIQVRTLASAGGPDNLVLLNPEKYKAKSRSPGSPVGEGTGSPPKWQIGEQEFEALMRMLDNLGYRTGYPYRYPALREKSKKYSDVEVPASVTGYSFASDGDSGTCSPLRHSFQKQQREKTRWLNSGRGDEASEEGQNGSSPKSKTKWTKEDGHRTSTSAVPNLFVPLNTNPKEVQEMRNKIREQNLQDIKTAGPQSQVLCGVVMDRSLVQGELVTASKAIIEKEYQPHVIVSTTGPNPFTTLTDRELEEYRREVERKQKGSEENLDEAREQKEKSPPDQPAVPHPPPSTPIKLEEDLVPEPTTGDDSDAATFKPTLPDLSPDEPSEALGFPMLEKEEEAHRPPSPTEAPTEASPEPAPDPAPVAEEAAPSAVEEGAAADPGSDGSPGKSPSKKKKKFRTPSFLKKSKKKSDS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P35611","disprot_id":"DP00240","ncbi_taxon_id":9606,"regions_counter":5,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":737,"region_id":"DP00240r001","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Adducin: a physical model with implications for function in assembly of spectrin-actin complexes. <i> Hughes CA, Bennett V. </i> J Biol Chem, 1995","term_id":"IDPO:0000002","curator_id":"vnugnes","start":430,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"7642559","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-05-02T18:28:12.477Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Circular dichroism indicated that COOH-terminal tail regions of a- and f3-adducin are unstructured, with no evidence for a-helix or f3-sheet based on signals at 208 and 222 nm, and a negative peak at 200 nm which is indicative of a random coil (Fig. 4B).","type":"Results"}]},{"start":430,"end":737,"reference_id":"7642559","reference_source":"pmid","reference_html":"Adducin: a physical model with implications for function in assembly of spectrin-actin complexes. <i> Hughes CA, Bennett V. </i> J Biol Chem, 1995","date":"2023-05-02T18:34:50.162Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00240r003","statement":[{"text":"The COOH-terminal region of both the α- and β-adducin subunits is hydrophilic and highly protease sensitive, in contrast to the stable\nglobular NH2 terminus (Fig. 3).","type":"Results"}]},{"start":430,"end":737,"reference_id":"7642559","reference_source":"pmid","reference_html":"Adducin: a physical model with implications for function in assembly of spectrin-actin complexes. <i> Hughes CA, Bennett V. </i> J Biol Chem, 1995","date":"2023-05-02T18:27:29.513Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00240r004","statement":[{"text":"Isolated COOH-ter-minal constructs migrated at an apparent 60 kDa, substantially higher than predicted molecular mass of 34 and 33 kDa based on amino acid sequence.","type":"Results"}]},{"start":430,"end":737,"reference_id":"7642559","reference_source":"pmid","reference_html":"Adducin: a physical model with implications for function in assembly of spectrin-actin complexes. <i> Hughes CA, Bennett V. </i> J Biol Chem, 1995","date":"2023-05-02T18:46:37.013Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0046983","term_name":"protein dimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007009","ec_ontology":"ECO","ec_name":"radioligand binding assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P35611","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P35612","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP00240r005","statement":[{"text":"α- and β-adducin tail domains associated with tails of both subunits, as well as the intact erythrocyte adducin protein (panels B and D). This binding is specific, as evidenced by the displacement of binding when 1.3 μM unlabeled α- or β-adducin tail is included in the incubation (panels C and E ). Individual subunit tails were able to form α-α, α-β, and β-β contacts. Neither the α- nor β-tails bound to the NH2-terminal core.","type":"Results"}],"term_comment":"","term_def":"\"The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.\" [ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_P35611","date":"2016-08-25T10:22:14.000Z","acc":"P35611","name":"Alpha-adducin","length":737,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI0000161BC8","genes":[{"name":{"value":"ADD1"},"synonyms":[{"value":"ADDA"}]}],"alphafold_very_low_content":0.4287652645861601,"disorder_content":0.417910447761194,"disprot_consensus":{"full":[{"start":430,"end":737,"type":"D"}],"Structural state":[{"start":430,"end":737,"type":"D"}],"Molecular function":[{"start":430,"end":737,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00596","name":"Class II Aldolase and Adducin N-terminal domain","start":136,"end":317}],"gene3D":[{"start":123,"end":379,"id":"3.40.225.10","name":"Class II aldolase/adducin N-terminal domain"}]},"uniref50":"UniRef50_P35612","sequence":"MSEETVPEAASPPPPQGQPYFDRFSEDDPEYMRLRNRAADLRQDFNLMEQKKRVTMILQSPSFREELEGLIQEQMKKGNNSSNIWALRQIADFMASTSHAVFPTSSMNVSMMTPINDLHTADSLNLAKGERLMRCKISSVYRLLDLYGWAQLSDTYVTLRVSKEQDHFLISPKGVSCSEVTASSLIKVNILGEVVEKGSSCFPVDTTGFCLHSAIYAARPDVRCIIHLHTPATAAVSAMKWGLLPVSHNALLVGDMAYYDFNGEMEQEADRINLQKCLGPTCKILVLRNHGVVALGDTVEEAFYKIFHLQAACEIQVSALSSAGGVENLILLEQEKHRPHEVGSVQWAGSTFGPMQKSRLGEHEFEALMRMLDNLGYRTGYTYRHPFVQEKTKHKSEVEIPATVTAFVFEEDGAPVPALRQHAQKQQKEKTRWLNTPNTYLRVNVADEVQRSMGSPRPKTTWMKADEVEKSSSGMPIRIENPNQFVPLYTDPQEVLEMRNKIREQNRQDVKSAGPQSQLLASVIAEKSRSPSTESQLMSKGDEDTKDDSEETVPNPFSQLTDQELEEYKKEVERKKLELDGEKETAPEEPGSPAKSAPASPVQSPAKEAETKSPLVSPSKSLEEGTKKTETSKAATTEPETTQPEGVVVNGREEEQTAEEILSKGLSQMTTSADTDVDTSKDKTESVTSGPMSPEGSPSKSPSKKKKKFRTPSFLKKSKKKEKVES","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P35612","disprot_id":"DP00241","ncbi_taxon_id":9606,"regions_counter":13,"creator":"ftonello","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":726,"region_id":"DP00241r001","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Adducin: a physical model with implications for function in assembly of spectrin-actin complexes. <i> Hughes CA, Bennett V. </i> J Biol Chem, 1995","term_id":"IDPO:0000002","curator_id":"vnugnes","start":409,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"7642559","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-05-02T18:35:33.812Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Circular dichroism indicated that COOH-terminal tail regions of α- and β-adducin are unstructured, with no evidence for α-helix or β-sheet based on signals at 208 and 222 nm, and a negative peak at 200 nm which is indicative of a random coil (Fig. 4B).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":726,"region_id":"DP00241r005","released":"2023_06","ec_id":"ECO:0007689","reference_html":"Adducin: a physical model with implications for function in assembly of spectrin-actin complexes. <i> Hughes CA, Bennett V. </i> J Biol Chem, 1995","term_id":"IDPO:0000002","curator_id":"vnugnes","start":409,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"7642559","version":3,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2023-05-02T18:35:59.126Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"\"Isolated COOH-ter-minal constructs migrated at an apparent 60 kDa, substantially higher than predicted molecular mass of 34 and 33 kDa based on amino acid sequence.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":726,"region_id":"DP00241r009","released":"2023_06","ec_id":"ECO:0007691","reference_html":"Adducin: a physical model with implications for function in assembly of spectrin-actin complexes. <i> Hughes CA, Bennett V. </i> J Biol Chem, 1995","term_id":"IDPO:0000002","curator_id":"vnugnes","start":409,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"7642559","version":3,"ec_name":"cleavage assay evidence used in manual assertion","date":"2023-05-02T18:35:46.555Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The COOH-terminal region of both the α- and β-adducin subunits is hydrophilic and highly protease sensitive, in contrast to the stable globular NH2 terminus (Fig. 3).","type":"Results"}]},{"start":409,"end":726,"reference_id":"7642559","reference_source":"pmid","reference_html":"Adducin: a physical model with implications for function in assembly of spectrin-actin complexes. <i> Hughes CA, Bennett V. </i> J Biol Chem, 1995","date":"2023-05-02T18:47:11.502Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0046983","term_name":"protein dimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007009","ec_ontology":"ECO","ec_name":"radioligand binding assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P35612","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P35611","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP00241r013","statement":[{"text":"α- and β-adducin tail domains associated with tails of both subunits, as well as the intact erythrocyte adducin protein (panels B and D). This binding is specific, as evidenced by the displacement of binding when 1.3 μM unlabeled α- or β-adducin tail is included in the incubation (panels C and E ). Individual subunit tails were able to form α-α, α-β, and β-β contacts. Neither the α- nor β-tails bound to the NH2-terminal core.","type":"Results"}],"term_comment":"","term_def":"\"The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.\" [ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_P35612","date":"2016-09-09T10:50:55.000Z","acc":"P35612","name":"Beta-adducin","length":726,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000125503","genes":[{"name":{"value":"ADD2"},"synonyms":[{"value":"ADDB"}]}],"alphafold_very_low_content":0.3856749311294766,"disorder_content":0.4380165289256198,"disprot_consensus":{"full":[{"start":409,"end":726,"type":"D"}],"Structural state":[{"start":409,"end":726,"type":"D"}],"Molecular function":[{"start":409,"end":726,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01286","name":"XPA protein N-terminal","start":104,"end":133},{"id":"PF05181","name":"XPA protein C-terminus","start":135,"end":186}],"gene3D":[{"start":98,"end":208,"id":"3.90.530.10","name":"XPA C-terminal domain"}]},"uniref50":"UniRef50_P23025","sequence":"MAAADGALPEAAALEQPAELPASVRASIERKRQRALMLRQARLAARPYSATAAAATGGMANVKAAPKIIDTGGGFILEEEEEEEQKIGKVVHQPGPVMEFDYVICEECGKEFMDSYLMNHFDLPTCDNCRDADDKHKLITKTEAKQEYLLKDCDLEKREPPLKFIVKKNPHHSQWGDMKLYLKLQIVKRSLEVWGSQEALEEAKEVRQENREKMKQKKFDKKVKELRRAVRSSVWKRETIVHQHEYGPEENLEDDMYRKTCTMCGHELTYEKM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P23025","disprot_id":"DP00243","ncbi_taxon_id":9606,"regions_counter":8,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":179,"region_id":"DP00243r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Resonance assignments, solution structure, and backbone dynamics of the DNA- and RPA-binding domain of human repair factor XPA. <i> Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M. </i> J Biochem, 1999","term_id":"IDPO:0000002","curator_id":"vnugnes","start":166,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10050037","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-05-19T16:29:55.549Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The sheet-helix-loop region is composed of an antiparallel β-sheet (strands β3–5), helix α1, and two long loops, L1 and L2. Loop L1 (residues 148–163) connects the α1 helix and the β4 strand, and loop L2 (residues 166–179) connects strands β4 and β5. While the structure of loop L1, except for residues 156–162, has been relatively well defined by hydrophobic contacts with residues in helices α1 and α2, loop L2 apparently does not form a single definite structure based on the observation of few long-range NOEs.","type":"Article"},{"text":"Since we observe few medium- and no long-range NOEs for the C-terminal sequence (residues 211–219) this region was excluded from the structure calculations.","type":"Article"}]},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":179,"term_name":"flexible linker","start":166,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10050037","version":4,"reference_html":"Resonance assignments, solution structure, and backbone dynamics of the DNA- and RPA-binding domain of human repair factor XPA. <i> Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M. </i> J Biochem, 1999","date":"2023-05-19T16:27:48.331Z","term_id":"IDPO:0000033","ec_id":"ECO:0006165","region_id":"DP00243r002","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Disorder function","statement":[{"text":"The sheet-helix-loop region is composed of an antiparallel β-sheet (strands β3–5), helix α1, and two long loops, L1 and L2. Loop L1 (residues 148–163) connects the α1 helix and the β4 strand, and loop L2 (residues 166–179) connects strands β4 and β5. While the structure of loop L1, except for residues 156–162, has been relatively well defined by hydrophobic contacts with residues in helices α1 and α2, loop L2 apparently does not form a single definite structure based on the observation of few long-range NOEs.","type":"Article"}]},{"start":210,"end":219,"reference_id":"10050037","reference_source":"pmid","reference_html":"Resonance assignments, solution structure, and backbone dynamics of the DNA- and RPA-binding domain of human repair factor XPA. <i> Ikegami T, Kuraoka I, Saijo M, Kodo N, Kyogoku Y, Morikawa K, Tanaka K, Shirakawa M. </i> J Biochem, 1999","date":"2023-05-19T16:29:47.212Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00243r007","statement":[{"text":"Since we observe few medium- and no long-range NOEs for the C-terminal sequence (residues 211–219) this region was excluded from the structure calculations.","type":"Article"},{"text":"Steady-state heteronuclear 15N{1H}-NOE values19 smaller than 0.68 were observed for the residues 157–162 in loop L1, for all the residues in loop L2 except residues 171–174 whose signals could not be observed in the HSQC spectra, and for the nine C-terminal residues of the central domain (data not shown). This indicates that L2, part of L1 and the C-terminal flanking sequence are highly mobile in solution.","type":"Article"},{"text":"Since we observe few medium- and no long-range NOEs for the C-terminal sequence (residues 211–219) this region was excluded from the structure calculations.","type":"Article"}]},{"start":1,"end":101,"reference_id":"37076618","reference_source":"pmid","reference_html":"Lesion recognition by XPC, TFIIH and XPA in DNA excision repair. <i> Kim J, Li CL, Chen X, Cui Y, Golebiowski FM, Wang H, Hanaoka F, Sugasawa K, Yang W. </i> Nature, 2023","date":"2023-05-19T16:43:31.107Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00243r008","statement":[{"text":"The N-terminal 100 residues of XPA, which interact with RPA32, are disordered (Fig. 1a).","type":"Results"},{"text":"The Electron Microscopy evidences of the Core7-XPA-DNA complexes, shows this region is disordered. ","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"8EBU"},{"db":"PDB","id":"8EBY"},{"db":"EMDB","id":"27998"},{"db":"EMDB","id":"28002"}]}],"released":"2016_10","uniref100":"UniRef100_P23025","date":"2016-08-31T13:31:55.000Z","acc":"P23025","name":"DNA repair protein complementing XP-A cells","length":273,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI0000043B7A","genes":[{"name":{"value":"XPA"},"synonyms":[{"value":"XPAC"}]}],"alphafold_very_low_content":0.10622710622710622,"disorder_content":0.45787545787545786,"disprot_consensus":{"full":[{"start":1,"end":101,"type":"D"},{"start":166,"end":179,"type":"D"},{"start":210,"end":219,"type":"D"}],"Structural state":[{"start":1,"end":101,"type":"D"},{"start":166,"end":179,"type":"D"},{"start":210,"end":219,"type":"D"}],"Disorder function":[{"start":166,"end":179,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00027","name":"Cyclic nucleotide-binding domain","start":155,"end":235},{"id":"PF00027","name":"Cyclic nucleotide-binding domain","start":273,"end":358},{"id":"PF02197","name":"Regulatory subunit of type II PKA R-subunit","start":24,"end":61}],"gene3D":[{"start":103,"end":236,"id":"2.60.120.10","name":"Jelly Rolls"},{"start":237,"end":377,"id":"2.60.120.10","name":"Jelly Rolls"},{"start":15,"end":72,"id":"1.20.890.10","name":"cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain"}]},"uniref50":"UniRef50_P10644","sequence":"MASGTTASEEERSLRECELYVQKHNIQALLKDSIVQLCTARPERPMAFLREYFEKLEKEEAKQIQNLQKAGSRADSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGSAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P10644","disprot_id":"DP00245","ncbi_taxon_id":9913,"regions_counter":2,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":112,"region_id":"DP00245r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of a complex between the catalytic and regulatory (RIalpha) subunits of PKA. <i> Kim C, Xuong NH, Taylor SS. </i> Science, 2005","term_id":"IDPO:0000002","curator_id":"fquaglia","start":91,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15692043","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":112,"term_name":"disorder to order","start":91,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15692043","version":2,"reference_html":"Crystal structure of a complex between the catalytic and regulatory (RIalpha) subunits of PKA. <i> Kim C, Xuong NH, Taylor SS. </i> Science, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00245r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2016_10","uniref100":"UniRef100_P00514","date":"2016-08-11T17:51:07.000Z","acc":"P00514","name":"cAMP-dependent protein kinase type I-alpha regulatory subunit","length":380,"organism":"Bos taurus","dataset":[],"UniParc":"UPI0000113462","genes":[{"name":{"value":"PRKAR1A"}}],"alphafold_very_low_content":0.060526315789473685,"disorder_content":0.05789473684210526,"disprot_consensus":{"full":[{"start":91,"end":112,"type":"T"}],"Structural state":[{"start":91,"end":112,"type":"D"}],"Structural transition":[{"start":91,"end":112,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00530","name":"Scavenger receptor cysteine-rich domain","start":355,"end":452},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":284,"end":342},{"id":"PF03523","name":"Macrophage scavenger receptor","start":120,"end":168}],"gene3D":[{"start":344,"end":453,"id":"3.10.250.10","name":"SRCR-like domain"}]},"uniref50":"UniRef50_P21758","sequence":"MAQWDDFPDQQEDTDSCTESVKFDARSVTALLPPHPKNGPTLQERMKSYKTALITLYLIVFVVLVPIIGIVAAQLLKWETKNCTVGSVNADISPSPEGKGNGSEDEMRFREAVMERMSNMESRIQYLSDNEANLLDAKNFQNFSITTDQRFNDVLFQLNSLLSSIQEHENIIGDISKSLVGLNTTVLDLQFSIETLNGRVQENAFKQQEEMRKLEERIYNASAEIKSLDEKQVYLEQEIKGEMKLLNNITNDLRLKDWEHSQTLKNITLLQGPPGPPGEKGDRGPPGQNGIPGFPGLIGTPGLKGDRGISGLPGVRGFPGPMGKTGKPGLNGQKGQKGEKGSGSMQRQSNTVRLVGGSGPHEGRVEIFHEGQWGTVCDDRWELRGGLVVCRSLGYKGVQSVHKRAYFGKGTGPIWLNEVFCFGKESSIEECRIRQWGVRACSHDEDAGVTCTT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P21758","disprot_id":"DP00246","ncbi_taxon_id":9913,"regions_counter":7,"creator":"ireményi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":50,"region_id":"DP00246r001","released":"2024_06","ec_id":"ECO:0006204","reference_html":"HSP90, HSP70, and GAPDH directly interact with the cytoplasmic domain of macrophage scavenger receptors. <i> Nakamura T, Hinagata J, Tanaka T, Imanishi T, Wada Y, Kodama T, Doi T. </i> Biochem Biophys Res Commun, 2002","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"11785981","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2024-01-25T17:06:40.028Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys17Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"This linker molecule and C17A peptide (52 amino acids peptide whose 17th cystein residue from N terminus was replaced by alanine and the C-terminal residue was cystein) were mixed in 50 mM NaHCO3-2M GdnHCl at r.t. for 15 h."}]}],"sequence_construct":"MAQWDDFPDQQEDTDSATESVKFDARSVTALLPPHPKNGPTLQERMKSYKGC","statement":[{"text":"The results in phosphate buffer (pH 7.0) shown in Fig. 3 indicated that neither peptide formed a definite secondary structure.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:33:46.839Z"}},{"start":1,"end":50,"reference_id":"11785981","reference_source":"pmid","reference_html":"HSP90, HSP70, and GAPDH directly interact with the cytoplasmic domain of macrophage scavenger receptors. <i> Nakamura T, Hinagata J, Tanaka T, Imanishi T, Wada Y, Kodama T, Doi T. </i> Biochem Biophys Res Commun, 2002","date":"2024-01-25T17:21:29.547Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006082","ec_ontology":"ECO","ec_name":"affinity chromatography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys17Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"This linker molecule and C17A peptide (52 amino acids peptide whose 17th cystein residue from N terminus was replaced by alanine and the C-terminal residue was cystein) were mixed in 50 mM NaHCO3-2M GdnHCl at r.t. for 15 h."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q76LV1","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q27975","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P00727","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q3MHL4","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P10096","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP00246r004","sequence_construct":"MAQWDDFPDQQEDTDSATESVKFDARSVTALLPPHPKNGPTLQERMKSYKGC","statement":[{"text":"Although non-specific binding proteins, which were also detected when using the control resin, appeared on the SDS– PAGE, the specifically binding proteins (shown by the arrows in Fig. 6) were eluted from the gel. And then, the partial amino acid sequences of these proteins were determined as shown in Table 1 (by APRO Life Science Institute).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:33:50.006Z"}},{"start":1,"end":50,"reference_id":"11785981","reference_source":"pmid","reference_html":"HSP90, HSP70, and GAPDH directly interact with the cytoplasmic domain of macrophage scavenger receptors. <i> Nakamura T, Hinagata J, Tanaka T, Imanishi T, Wada Y, Kodama T, Doi T. </i> Biochem Biophys Res Commun, 2002","date":"2024-01-25T17:34:07.952Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys17Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"This linker molecule and C17A peptide (52 amino acids peptide whose 17th cystein residue from N terminus was replaced by alanine and the C-terminal residue was cystein) were mixed in 50 mM NaHCO3-2M GdnHCl at r.t. for 15 h."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P04792","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P11142","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P04406","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP00246r005","sequence_construct":"MAQWDDFPDQQEDTDSATESVKFDARSVTALLPPHPKNGPTLQERMKSYKGC","statement":[{"text":"The results of Western blotting shown in Fig. 7 proved that all HSP90, HSP70 and\nGAPDH could interact with the cytoplasmic domain of MSR.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:33:54.257Z"}},{"start":1,"end":50,"reference_id":"11785981","reference_source":"pmid","reference_html":"HSP90, HSP70, and GAPDH directly interact with the cytoplasmic domain of macrophage scavenger receptors. <i> Nakamura T, Hinagata J, Tanaka T, Imanishi T, Wada Y, Kodama T, Doi T. </i> Biochem Biophys Res Commun, 2002","date":"2024-01-25T17:28:11.588Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031072","term_name":"heat shock protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006082","ec_ontology":"ECO","ec_name":"affinity chromatography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys17Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"This linker molecule and C17A peptide (52 amino acids peptide whose 17th cystein residue from N terminus was replaced by alanine and the C-terminal residue was cystein) were mixed in 50 mM NaHCO3-2M GdnHCl at r.t. for 15 h."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q76LV1","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q27975","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP00246r006","sequence_construct":"MAQWDDFPDQQEDTDSATESVKFDARSVTALLPPHPKNGPTLQERMKSYKGC","statement":[{"text":"Although non-specific binding proteins, which were also detected when using the control resin, appeared on the SDS– PAGE, the specifically binding proteins (shown by the arrows in Fig. 6) were eluted from the gel. And then, the partial amino acid sequences of these proteins were determined as shown in Table 1 (by APRO Life Science Institute). Based on these data, the five known and one unknown protein were identified as the binding proteins (Table 1). Of these proteins, HSP90, HSP70 and GAPDH were the focus of attention for their possible participation in a receptor function.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a heat shock protein, a protein synthesized or activated in response to heat shock.\" [GOC:mah, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:33:57.675Z"}},{"start":1,"end":50,"reference_id":"11785981","reference_source":"pmid","reference_html":"HSP90, HSP70, and GAPDH directly interact with the cytoplasmic domain of macrophage scavenger receptors. <i> Nakamura T, Hinagata J, Tanaka T, Imanishi T, Wada Y, Kodama T, Doi T. </i> Biochem Biophys Res Commun, 2002","date":"2024-01-25T17:38:04.370Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys17Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"This linker molecule and C17A peptide (52 amino acids peptide whose 17th cystein residue from N terminus was replaced by alanine and the C-terminal residue was cystein) were mixed in 50 mM NaHCO3-2M GdnHCl at r.t. for 15 h."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P04406","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P11142","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P04792","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP00246r007","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0224","statements":[{"type":"Figure","text":"Lysates from COS-7 cells were immunoprecipitated with 3F10"}],"entry_name":"CV-1 in Origin Simian-7"}],"sequence_construct":"MAQWDDFPDQQEDTDSATESVKFDARSVTALLPPHPKNGPTLQERMKSYKGC","statement":[{"text":"Following this result, immunoprecipitation assays were performed to investigate whether these interactions occur in the cells or not. The results showed that all three kinds of protein were precipitated with MSR (Fig. 8). This experiments confirmed that HSP90, HSP70 and GAPDH directly associate with the cytoplasmic domain of MSR in vitro and in vivo.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:34:01.533Z"}}],"released":"2016_10","uniref100":"UniRef100_P21758","date":"2016-09-07T18:39:40.000Z","acc":"P21758","name":"Macrophage scavenger receptor types I and II","length":453,"organism":"Bos taurus","dataset":[],"UniParc":"UPI000012F685","genes":[{"name":{"value":"MSR1"}}],"alphafold_very_low_content":0.2119205298013245,"disorder_content":0.11037527593818984,"disprot_consensus":{"full":[{"start":1,"end":50,"type":"D"}],"Structural state":[{"start":1,"end":50,"type":"D"}],"Molecular function":[{"start":1,"end":50,"type":"F"}]}},{"features":{"pfam":[{"id":"PF13499","name":"EF-hand domain pair","start":94,"end":158},{"id":"PF13833","name":"EF-hand domain pair","start":32,"end":84}],"gene3D":[{"start":86,"end":161,"id":"1.10.238.10","name":"EF-hand"},{"start":1,"end":85,"id":"1.10.238.10","name":"EF-hand"}]},"uniref50":"UniRef50_P63315","sequence":"MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEMIDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLEELKIMLQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P63315","disprot_id":"DP00249","ncbi_taxon_id":9913,"regions_counter":3,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":161,"region_id":"DP00249r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Trypsin digestion of bovine cardiac troponin C in the presence and absence of calcium. <i> McCubbin WD, Kay CM. </i> Can J Biochem Cell Biol, 1985","term_id":"IDPO:0000002","curator_id":"gminervini","start":103,"term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"2933134","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":161,"term_name":"disorder to order","start":103,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"gminervini","released":"2022_03","term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"2933134","version":2,"reference_html":"Trypsin digestion of bovine cardiac troponin C in the presence and absence of calcium. <i> McCubbin WD, Kay CM. </i> Can J Biochem Cell Biol, 1985","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00249r002","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":161,"term_name":"ion binding","start":103,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"gminervini","released":"2022_03","term_ontology":"GO","curator_name":"Giovanni Minervini","reference_id":"2933134","version":3,"reference_html":"Trypsin digestion of bovine cardiac troponin C in the presence and absence of calcium. <i> McCubbin WD, Kay CM. </i> Can J Biochem Cell Biol, 1985","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0043167","ec_id":"ECO:0006204","region_id":"DP00249r003","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P63315","date":"2016-08-25T10:38:43.000Z","acc":"P63315","name":"Troponin C, slow skeletal and cardiac muscles","length":161,"organism":"Bos taurus","dataset":[],"UniParc":"UPI0000113596","genes":[{"name":{"value":"TNNC1"},"synonyms":[{"value":"TNNC"}]}],"alphafold_very_low_content":0.037267080745341616,"disorder_content":0.36645962732919257,"disprot_consensus":{"full":[{"start":103,"end":161,"type":"T"}],"Structural state":[{"start":103,"end":161,"type":"D"}],"Structural transition":[{"start":103,"end":161,"type":"T"}],"Molecular function":[{"start":103,"end":161,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01375","name":"Heat-labile enterotoxin alpha chain","start":3,"end":258}],"gene3D":[{"start":213,"end":258,"id":"1.20.5.240","name":"1.20.5.240"},{"start":23,"end":206,"id":"3.90.210.10","name":"Heat-Labile Enterotoxin, subunit A"}]},"uniref50":"UniRef50_P01555","sequence":"MVKIIFVFFIFLSSFSYANDDKLYRADSRPPDEIKQSGGLMPRGQSEYFDRGTQMNINLYDHARGTQTGFVRHDDGYVSTSISLRSAHLVGQTILSGHSTYYIYVIATAPNMFNVNDVLGAYSPHPDEQEVSALGGIPYSQIYGWYRVHFGVLDEQLHRNRGYRDRYYSNLDIAPAADGYGLAGFPPEHRAWREEPWIHHAPPGCGNAPRSSMSNTCDEKTQSLGVKFLDEYQSKVKRQIFSGYQSDIDTHNRIKDEL","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Vibrionales","Vibrionaceae","Vibrio"],"uniref90":"UniRef90_P01555","disprot_id":"DP00250","dataset":["Unicellular toxins and antitoxins","Bacterial virulence-related proteins"],"ncbi_taxon_id":243277,"regions_counter":44,"creator":"ftonello","regions":[{"region_id":"DP00250r001","validated":{"curator_id":"bmesza","timestamp":"2020-12-19T18:42:50.645Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":54,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":44,"version":3,"statement":[{"text":"In this study, we present crystal structures of the intrinsically active CTY30S mutant, providing the first structural views of an active form of CT or LT. To enable accurate structureactivity comparisons, we also independently determined the structure of wild-type CT at higher resolution and accuracy than were previously available (10). Our six new CT structures show an A2 tail conformation that differs markedly from that found in the original CT structure, with interesting implications for toxicity. In addition, the differences between CTY30S and wild-type CT structures permit further insight into the mechanism of CT/LT activation","type":"Introduction"},{"text":"Residues in the 25-36 “activation loop” were ordered in the originally determined wild-type CT structure and in wild-type LT structures but displayed mostly higher than average B-factors in wild-type LT structures. These residues were included in the molecular replacement model used for CTY30S structure determinations, but density in the CTY30S structures did not support the inclusion of activation loop residues in the final models, suggesting that the activation loop is disordered in CTY30S (Figure 2).","type":"Results"},{"text":"The only major structural changes observed between wildtype CT and CTY30S occur in the level of flexibility found in the activation and active site loops\n\n\n","type":"Discussion"},{"text":"B-Factors along the activation loop are higher than the average B-factors for the A1 subunits of the CT/LT structures, suggesting that this loop already has a tendency toward disorder (Figure 5). Missing density in the wild-type CT form 2 structure for residues 33-35 further underscores the high level of thermal motion naturally present in this loop (Figure 2). ","type":"Discussion"},{"text":"The 'activated' state where disorder is observed corresponds to the Y30S point mutant, which is shown to have hogh enzymatic activity, unlike wtCT","type":"Curator statement"},{"text":"Numbering needs to be shifted by 18 residues to match the Uniprot sequence due to the presence of the signal peptide. ","type":"Curator statement"}],"term_name":"disorder","reference_html":"Crystal structures of an intrinsically active cholera toxin mutant yield insight into the toxin activation mechanism. <i> O'Neal CJ, Amaya EI, Jobling MG, Holmes RK, Hol WG. </i> Biochemistry, 2004","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"15049684","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1S5B:A"},{"db":"PDB","id":"1S5C:A"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lchemes","curator_orcid":"0000-0003-0192-9906","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00250r003","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T13:35:01.669Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":54,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":44,"version":3,"statement":[{"text":"In this study, we present crystal structures of the intrinsically active CTY30S mutant, providing the first structural views of an active form of CT or LT. To enable accurate structureactivity comparisons, we also independently determined the structure of wild-type CT at higher resolution and accuracy than were previously available (10). Our six new CT structures show an A2 tail conformation that differs markedly from that found in the original CT structure, with interesting implications for toxicity. In addition, the differences between CTY30S and wild-type CT structures permit further insight into the mechanism of CT/LT activation","type":"Introduction"},{"text":"The fact that the activation loop is consistently disordered in CTY30S structures but is ordered in wild-type CT structures, despite different packing environments among the crystal forms, indicates that the activation loop is not likely to be affected by crystal packing interactions in these structures. In all wild-type CT structures, both the 25-36 activation loop and 47-56 active site loop are ordered, with a minor exception of the activation loop of wild-type CT form 2. ","type":"Results"},{"text":"The only major structural changes observed between wildtype CT and CTY30S occur in the level of flexibility found in the activation and active site loops","type":"Discussion"},{"text":"Role of the ActiVation Loop in the ActiVation Mechanism. Activation loop disorder is the only major conformational difference between the high-resolution wild-type CT structures and all the CTY30S structures. This feature is thus likely to be a key factor for the difference in intrinsic activity between wild-type CT and constitutively active CTY30S, suggesting that disorder in this loop is necessary for the transition between proenzyme and active enzyme\n\n","type":"Discussion"}],"term_name":"order to disorder","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"15049684","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1S5F"},{"db":"PDB","id":"1S5E"}],"term_namespace":"Structural transition","ec_id":"ECO:0006220","curator_id":"lchemes","reference_html":"Crystal structures of an intrinsically active cholera toxin mutant yield insight into the toxin activation mechanism. <i> O'Neal CJ, Amaya EI, Jobling MG, Holmes RK, Hol WG. </i> Biochemistry, 2004","term_id":"IDPO:0000014","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":212,"region_id":"DP00250r010","reference_html":"ADP-ribosylation factor 6 acts as an allosteric activator for the folded but not disordered cholera toxin A1 polypeptide. <i> Banerjee T, Taylor M, Jobling MG, Burress H, Yang Z, Serrano A, Holmes RK, Tatulian SA, Teter K. </i> Mol Microbiol, 2014","ec_id":"ECO:0007691","version":3,"term_id":"IDPO:0000002","curator_id":"lchemes","start":19,"term_ontology":"IDPO","curator_name":"Lucia Chemes","ec_name":"cleavage assay evidence used in manual assertion","statement":[{"text":"the isolated CTA1 polypeptide has a disordered conformation with minimal enzymatic activity against Gs or synthetic substrates at 37°C (Murayama et al., 1993; Ray et al., 2012). When CTA1-ARF interactions have been examined at 37°C, CTA1 and ARF are typically added together before incubation at 37°C (Murayama et al., 1993; Pande et al., 2007). This protocol allows ARF6 to stabilize the folded conformation of CTA1 initially present at low temperature, but it does not determine whether ARF6 can activate the disordered CTA1 subunit. In this paper we examined whether ARF6 can activate a disordered, as well as a structured, CTA1 polypeptide. A biochemical and biophysical analysis of CTA1 structure / function indicated that ARF6 cannot promote the refolding of disordered CTA1 to an active state. Instead, lipid rafts shifted the disordered, 37°C structure of CTA1 to a folded conformation with a basal level of activity that could be further stimulated by ARF6.","type":"Introduction"},{"text":"CTA1-ARF6 interactions were initially examined with a protease sensitivity assay (Fig. 1). The isolated CTA1 polypeptide shifts from a protease-resistant conformation to a protease sensitive conformation with increasing temperature, which is consistent with its intrinsic thermal instability (Pande et al., 2007).","type":"Results"},{"text":"Because free CTA1 is an unstable protein, the translocated pool of toxin would remain in a disordered state at 37°C and must therefore engage components of the host cell to regain an ordered, active conformation","type":"Discussion"}],"curator_orcid":"0000-0003-0192-9906","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T14:05:33.106Z","curator_name":"Bálint Mészáros"},"released":"2022_03","reference_id":"25257027","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","version":3,"ec_ontology":"ECO","end":212,"term_name":"disorder to order","start":19,"ec_name":"cleavage assay evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0003-0192-9906","curator_id":"lchemes","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"25257027","statement":[{"text":"the isolated CTA1 polypeptide has a disordered conformation with minimal enzymatic activity against Gs or synthetic substrates at 37°C (Murayama et al., 1993; Ray et al., 2012). When CTA1-ARF interactions have been examined at 37°C, CTA1 and ARF are typically added together before incubation at 37°C (Murayama et al., 1993; Pande et al., 2007). This protocol allows ARF6 to stabilize the folded conformation of CTA1 initially present at low temperature, but it does not determine whether ARF6 can activate the disordered CTA1 subunit. In this paper we examined whether ARF6 can activate a disordered, as well as a structured, CTA1 polypeptide. A biochemical and biophysical analysis of CTA1 structure / function indicated that ARF6 cannot promote the refolding of disordered CTA1 to an active state. Instead, lipid rafts shifted the disordered, 37°C structure of CTA1 to a folded conformation with a basal level of activity that could be further stimulated by ARF6.","type":"Introduction"},{"text":"ARF6/GTP but not ARF6/GDP prevented the temperature-induced transition of CTA1 to a protease-sensitive conformation (Fig. 1A). This confirmed our previous report (Pande et al., 2007) and demonstrated the active form of ARF6 can stabilize the folded, protease-resistant conformation of CTA1","type":"Results"},{"text":"we heated CTA1 to 37°C before the addition of ARF6. Under this condition, neither ARF6/GDP nor ARF6/GTP protected CTA1 from proteolysis.","type":"Results"},{"text":"In contrast to ARF6, large unilamellar vesicles (LUVs) mimicking the composition of a lipid raft could protect CTA1 from proteolysis even when they were added after toxin unfolding had already occurred (Fig. 1B). This was consistent with previous biophysical measurements demonstrating the chaperone-like ability of lipid rafts to stabilize folded CTA1 and to induce both a gain-of-structure and gain-of-function in the disordered CTA1 polypeptide (Ray et al., 2012). ARF6 and lipid rafts thus exhibited overlapping yet distinct interactions with CTA1: both could prevent the thermal unfolding of CTA1 to a protease-sensitive conformation, but only lipid rafts could shift disordered CTA1 back to a protease-resistant structure","type":"Results"},{"text":"Because CTA1 is disordered at 37°C and ARF6/GTP does not promote the refolding of disordered CTA1 (Fig. 2, Table 1), it is necessary for other host factors such as lipid rafts to participate in shifting CTA1 from a disordered conformation to a partially folded active state that is competent for functional interaction with ARFs. The gain-of-structure resulting from toxin-raft interactions allows ARF6/GTP to induce an additional conformational change (Fig. 4, Table 1) that presumably stabilizes displacement of the occluding CTA1 “activation loop” and consequently optimizes the enzymatic activity of CTA1 (Fig. 5A).","type":"Discussion"}],"reference_html":"ADP-ribosylation factor 6 acts as an allosteric activator for the folded but not disordered cholera toxin A1 polypeptide. <i> Banerjee T, Taylor M, Jobling MG, Burress H, Yang Z, Serrano A, Holmes RK, Tatulian SA, Teter K. </i> Mol Microbiol, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0007691","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T14:25:48.422Z","curator_name":"Bálint Mészáros"},"region_id":"DP00250r013","ec_go":"IDA","disprot_namespace":"Structural transition"},{"region_id":"DP00250r014","validated":{"curator_id":"bmesza","timestamp":"2020-12-19T18:44:39.123Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":212,"ec_name":"cleavage assay evidence used in manual assertion","start":19,"version":4,"statement":[{"text":"the isolated CTA1 polypeptide has a disordered conformation with minimal enzymatic activity against Gs or synthetic substrates at 37°C (Murayama et al., 1993; Ray et al., 2012). When CTA1-ARF interactions have been examined at 37°C, CTA1 and ARF are typically added together before incubation at 37°C (Murayama et al., 1993; Pande et al., 2007). This protocol allows ARF6 to stabilize the folded conformation of CTA1 initially present at low temperature, but it does not determine whether ARF6 can activate the disordered CTA1 subunit. In this paper we examined whether ARF6 can activate a disordered, as well as a structured, CTA1 polypeptide. A biochemical and biophysical analysis of CTA1 structure / function indicated that ARF6 cannot promote the refolding of disordered CTA1 to an active state. Instead, lipid rafts shifted the disordered, 37°C structure of CTA1 to a folded conformation with a basal level of activity that could be further stimulated by ARF6.","type":"Introduction"},{"text":"ARF6/GTP but not ARF6/GDP prevented the temperature-induced transition of CTA1 to a protease-sensitive conformation (Fig. 1A). This confirmed our previous report (Pande et al., 2007) and demonstrated the active form of ARF6 can stabilize the folded, protease-resistant conformation of CTA1","type":"Results"},{"text":"In contrast to ARF6, large unilamellar vesicles (LUVs) mimicking the composition of a lipid raft could protect CTA1 from proteolysis even when they were added after toxin unfolding had already occurred (Fig. 1B). ","type":"Results"},{"text":"Because CTA1 is disordered at 37°C and ARF6/GTP does not promote the refolding of disordered CTA1 (Fig. 2, Table 1), it is necessary for other host factors such as lipid rafts to participate in shifting CTA1 from a disordered conformation to a partially folded active state that is competent for functional interaction with ARFs. The gain-of-structure resulting from toxin-raft interactions allows ARF6/GTP to induce an additional conformational change (Fig. 4, Table 1) that presumably stabilizes displacement of the occluding CTA1 “activation loop” and consequently optimizes the enzymatic activity of CTA1 (Fig. 5A).","type":"Discussion"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P62330","partner_end":null}],"term_name":"protein binding","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"25257027","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0007691","curator_id":"lchemes","reference_html":"ADP-ribosylation factor 6 acts as an allosteric activator for the folded but not disordered cholera toxin A1 polypeptide. <i> Banerjee T, Taylor M, Jobling MG, Burress H, Yang Z, Serrano A, Holmes RK, Tatulian SA, Teter K. </i> Mol Microbiol, 2014","term_id":"GO:0005515","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":212,"region_id":"DP00250r015","reference_html":"ADP-ribosylation factor 6 acts as an allosteric activator for the folded but not disordered cholera toxin A1 polypeptide. <i> Banerjee T, Taylor M, Jobling MG, Burress H, Yang Z, Serrano A, Holmes RK, Tatulian SA, Teter K. </i> Mol Microbiol, 2014","ec_id":"ECO:0006228","version":3,"term_id":"IDPO:0000002","curator_id":"lchemes","start":19,"term_ontology":"IDPO","curator_name":"Lucia Chemes","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","statement":[{"text":"the isolated CTA1 polypeptide has a disordered conformation with minimal enzymatic activity against Gs or synthetic substrates at 37°C (Murayama et al., 1993; Ray et al., 2012). When CTA1-ARF interactions have been examined at 37°C, CTA1 and ARF are typically added together before incubation at 37°C (Murayama et al., 1993; Pande et al., 2007). This protocol allows ARF6 to stabilize the folded conformation of CTA1 initially present at low temperature, but it does not determine whether ARF6 can activate the disordered CTA1 subunit. In this paper we examined whether ARF6 can activate a disordered, as well as a structured, CTA1 polypeptide. A biochemical and biophysical analysis of CTA1 structure / function indicated that ARF6 cannot promote the refolding of disordered CTA1 to an active state. Instead, lipid rafts shifted the disordered, 37°C structure of CTA1 to a folded conformation with a basal level of activity that could be further stimulated by ARF6.","type":"Introduction"},{"text":"CTA1 is in a folded conformation at low temperatures (Pande et al., 2007). We therefore used the FTIR spectrum of CTA1 at 10°C as a reference for the structure of folded CTA1 (Fig. 2A). Analysis of the 10°C FTIR spectrum from CTA1 indicated that the folded toxin contains 35 ± 4% α-helical and 49 ± 3% β-sheet content (Table 1).","type":"Results"},{"text":"Due to its intrinsic thermal instability, heating CTA1 to 37°C resulted in a loss of both α-helical and βsheet structures (Fig. 2B). Concomitant with this loss of secondary structure, the percentage of CTA1 irregular structure shifted from 10 ± 3% at 10°C to 55 ± 2% at 37°C (Table 1). ","type":"Results"},{"text":"Because free CTA1 is an unstable protein, the translocated pool of toxin would remain in a disordered state at 37°C and must therefore engage components of the host cell to regain an ordered, active conformation.","type":"Discussion"}],"curator_orcid":"0000-0003-0192-9906","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T14:37:55.763Z","curator_name":"Bálint Mészáros"},"released":"2022_03","reference_id":"25257027","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","version":3,"ec_ontology":"ECO","end":212,"term_name":"disorder to order","start":19,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0003-0192-9906","curator_id":"lchemes","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"25257027","statement":[{"text":"the isolated CTA1 polypeptide has a disordered conformation with minimal enzymatic activity against Gs or synthetic substrates at 37°C (Murayama et al., 1993; Ray et al., 2012). When CTA1-ARF interactions have been examined at 37°C, CTA1 and ARF are typically added together before incubation at 37°C (Murayama et al., 1993; Pande et al., 2007). This protocol allows ARF6 to stabilize the folded conformation of CTA1 initially present at low temperature, but it does not determine whether ARF6 can activate the disordered CTA1 subunit. In this paper we examined whether ARF6 can activate a disordered, as well as a structured, CTA1 polypeptide. A biochemical and biophysical analysis of CTA1 structure / function indicated that ARF6 cannot promote the refolding of disordered CTA1 to an active state. Instead, lipid rafts shifted the disordered, 37°C structure of CTA1 to a folded conformation with a basal level of activity that could be further stimulated by ARF6.","type":"Introduction"},{"text":"Due to its intrinsic thermal instability, heating CTA1 to 37°C resulted in a loss of both α-helical and βsheet structures (Fig. 2B). Concomitant with this loss of secondary structure, the percentage of CTA1 irregular structure shifted from 10 ± 3% at 10°C to 55 ± 2% at 37°C (Table 1). When ARF6/GTP was added to CTA1 before heating to 37°C, the toxin retained its full αhelical structure and a substantial amount of its β-sheet structure at 37°C (Fig. 2C, Table 1). ","type":"Results"},{"text":"The impact of ARF6/GTP on CTA1 α-helical and β-sheet structure thus represents a partial stabilization of the folded toxin, and this is sufficient to maintain folded CTA1 in a protease-resistant conformation (Fig. 1A).","type":"Results"},{"text":"Collectively, these results demonstrated ARF6/GTP can partially stabilize the folded conformation of CTA1 but cannot promote the refolding of disordered CTA1","type":"Results"},{"text":"The lipochaperone function of lipid rafts (Ray et al., 2012) could act in conjunction with ARF to place disordered CTA1 in a folded, active conformation. This possibility was examined by FTIR spectroscopy (Fig. 4). CTA1 was heated to 37°C for 15 minutes before exposure to lipid raft-mimicking LUVs. Measurements of toxin structure were then recorded after an additional 30 minutes at 37°C (Fig. 4A). In the presence of lipid raft LUVs, the disordered conformation of CTA1 gained both α-helical and β-sheet content (Table 1). An additional gain of β-sheet structure and a further loss of irregular structure were detected when the disordered CTA1 subunit was incubated with both lipid rafts and ARF6/GTP (Fig. 4B). Under this condition, CTA1 exhibited an ordered conformation that matched the structural content of the folded, 10°C toxin (Table 1)","type":"Results"},{"text":"Because CTA1 is disordered at 37°C and ARF6/GTP does not promote the refolding of disordered CTA1 (Fig. 2, Table 1), it is necessary for other host factors such as lipid rafts to participate in shifting CTA1 from a disordered conformation to a partially folded active state that is competent for functional interaction with ARFs. The gain-of-structure resulting from toxin-raft interactions allows ARF6/GTP to induce an additional conformational change (Fig. 4, Table 1) that presumably stabilizes displacement of the occluding CTA1 “activation loop” and consequently optimizes the enzymatic activity of CTA1 (Fig. 5A).","type":"Discussion"}],"reference_html":"ADP-ribosylation factor 6 acts as an allosteric activator for the folded but not disordered cholera toxin A1 polypeptide. <i> Banerjee T, Taylor M, Jobling MG, Burress H, Yang Z, Serrano A, Holmes RK, Tatulian SA, Teter K. </i> Mol Microbiol, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006228","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T14:25:51.186Z","curator_name":"Bálint Mészáros"},"region_id":"DP00250r018","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00250r019","validated":{"curator_id":"bmesza","timestamp":"2020-12-19T18:44:47.236Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":212,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","start":19,"version":4,"statement":[{"text":"the isolated CTA1 polypeptide has a disordered conformation with minimal enzymatic activity against Gs or synthetic substrates at 37°C (Murayama et al., 1993; Ray et al., 2012). When CTA1-ARF interactions have been examined at 37°C, CTA1 and ARF are typically added together before incubation at 37°C (Murayama et al., 1993; Pande et al., 2007). This protocol allows ARF6 to stabilize the folded conformation of CTA1 initially present at low temperature, but it does not determine whether ARF6 can activate the disordered CTA1 subunit. In this paper we examined whether ARF6 can activate a disordered, as well as a structured, CTA1 polypeptide. A biochemical and biophysical analysis of CTA1 structure / function indicated that ARF6 cannot promote the refolding of disordered CTA1 to an active state. Instead, lipid rafts shifted the disordered, 37°C structure of CTA1 to a folded conformation with a basal level of activity that could be further stimulated by ARF6.","type":"Introduction"},{"text":"When ARF6/GTP was added to CTA1 before heating to 37°C, the toxin retained its full αhelical structure and a substantial amount of its β-sheet structure at 37°C (Fig. 2C, Table 1). ","type":"Results"},{"text":"The lipochaperone function of lipid rafts (Ray et al., 2012) could act in conjunction with ARF to place disordered CTA1 in a folded, active conformation. This possibility was examined by FTIR spectroscopy (Fig. 4). CTA1 was heated to 37°C for 15 minutes before exposure to lipid raft-mimicking LUVs. Measurements of toxin structure were then recorded after an additional 30 minutes at 37°C (Fig. 4A). In the presence of lipid raft LUVs, the disordered conformation of CTA1 gained both α-helical and β-sheet content (Table 1). An additional gain of β-sheet structure and a further loss of irregular structure were detected when the disordered CTA1 subunit was incubated with both lipid rafts and ARF6/GTP (Fig. 4B). Under this condition, CTA1 exhibited an ordered conformation that matched the structural content of the folded, 10°C toxin (Table 1)","type":"Results"},{"text":"Because CTA1 is disordered at 37°C and ARF6/GTP does not promote the refolding of disordered CTA1 (Fig. 2, Table 1), it is necessary for other host factors such as lipid rafts to participate in shifting CTA1 from a disordered conformation to a partially folded active state that is competent for functional interaction with ARFs. The gain-of-structure resulting from toxin-raft interactions allows ARF6/GTP to induce an additional conformational change (Fig. 4, Table 1) that presumably stabilizes displacement of the occluding CTA1 “activation loop” and consequently optimizes the enzymatic activity of CTA1 (Fig. 5A)","type":"Discussion"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P62330","partner_end":null}],"term_name":"protein binding","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"25257027","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006228","curator_id":"lchemes","reference_html":"ADP-ribosylation factor 6 acts as an allosteric activator for the folded but not disordered cholera toxin A1 polypeptide. <i> Banerjee T, Taylor M, Jobling MG, Burress H, Yang Z, Serrano A, Holmes RK, Tatulian SA, Teter K. </i> Mol Microbiol, 2014","term_id":"GO:0005515","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00250r025","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T16:06:51.182Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":54,"term_id":"IDPO:0000011","start":44,"version":2,"statement":[{"text":"The CTA1 activation loop (residues 25 to 40), earlier suggested to be important in CT and LT activation (24), interacts with both partners but in different ways. The loop forms an ordered coil when bound by CTA2 in wildtype holo-CT structures, but residues 25 to 33 rearrange to form an amphipathic helix upon binding ARF6-GTP (Figs. 1 and 3).","type":"Results"},{"text":"Interestingly, disorder of activation-loop residues 26 to 36 in a CTA1:Y30S mutant results in a holotoxin variant with intrinsic activity (3). Here, activation of CTA1 by ARF6-GTP leads to a well-structured activation loop.","type":"Discussion"}],"term_name":"disorder to order","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"16099990","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2A5F"},{"db":"PDB","id":"2A5D"}],"term_namespace":"Structural transition","ec_id":"ECO:0005670","curator_id":"lchemes","reference_html":"Structural basis for the activation of cholera toxin by human ARF6-GTP. <i> O'Neal CJ, Jobling MG, Holmes RK, Hol WG. </i> Science, 2005","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00250r026","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T16:07:16.833Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":54,"term_id":"GO:0005515","start":44,"version":3,"statement":[{"text":"The CTA1 activation loop (residues 25 to 40), earlier suggested to be important in CT and LT activation (24), interacts with both partners but in different ways. The loop forms an ordered coil when bound by CTA2 in wildtype holo-CT structures, but residues 25 to 33 rearrange to form an amphipathic helix upon binding ARF6-GTP (Figs. 1 and 3).","type":"Results"},{"text":"Interestingly, disorder of activation-loop residues 26 to 36 in a CTA1:Y30S mutant results in a holotoxin variant with intrinsic activity (3). Here, activation of CTA1 by ARF6-GTP leads to a well-structured activation loop.","type":"Discussion"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P62330","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"16099990","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2A5F"},{"db":"PDB","id":"2A5D"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"lchemes","reference_html":"Structural basis for the activation of cholera toxin by human ARF6-GTP. <i> O'Neal CJ, Jobling MG, Holmes RK, Hol WG. </i> Science, 2005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00250r027","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T15:51:21.346Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":204,"term_id":"IDPO:0000002","start":186,"version":2,"statement":[{"text":"We report the first NMR based solution structural data for the Cholera Toxin enzymatic domain (CTA1). We show that this free enzymatic domain partially unfolds at the C-terminus, and binds its protein partners at both the beginning and end of this activation process.","type":"Abstract"},{"text":"To evaluate whether the unfolded regions detected within full-length CTA1 are localized to the carboxyl-terminus, we generated and analyzed a mutant form of CTA1 without the carboxyl-terminal region, called CTA1-T2 (N1-F167). For CTA1- T2, the sequence was truncated between F167↓P168P169 as P168P169 make extensive contacts with the CTA2 linker in the holotoxin crystal structure (10) and are likely to destabilize the free enzymatic domain. Spectra of the refolded CTA1-T2 sample show similar chemical shift (δ) values and dispersion to the CTA1 sample (Supplementary Figure 4). Most of the changes in the 1H/15N HSQC spectrum corresponded to a decrease in the number of resonances within the random coil region, while leaving unaffected the dispersed resonances, suggesting that the structure of the catalytic core domain was unaffected by the truncation of the Cterminus.","type":"Results"},{"text":"The 2D NMR 1H/15N HSQC spectrum of recombinant CTA1 (N1-G186) (Figure 3a) revealed that CTA1 is partially unfolded and displays the characteristics of a molten globule in solution [for review, see (34)]. Notably, only 20% of the total amide protons resonated either up-field or down-field when compared to the random coil chemical shift region between 7.5 and 8.5 ppm (34–36). Moreover, there is considerable variation in peak intensity within the 1H/15N HSQC spectrum, likely due to intermediate exchange broadening.","type":"Results"},{"text":"The free CTA1 enzymatic domain is partially unfolded, in contrast to when it is complexed with either CTA2 in the holotoxin or with ARF6-GTP following retrotranslocation. Further strengthening this argument was that the refolded recombinant CTA1 is catalytically active (23) and, due to its thermal instability, CTA1 is a substrate for export to the cytosol via the ERAD pathway (33).","type":"Discussion"},{"text":"Numbering needs to be shifted by 18 residues to match the Uniprot sequence","type":"Curator statement"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"18272180","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"15162"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"lchemes","reference_html":"Order-disorder-order transitions mediate the activation of cholera toxin. <i> Ampapathi RS, Creath AL, Lou DI, Craft JW, Blanke SR, Legge GB. </i> J Mol Biol, 2008","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00250r028","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T15:52:39.218Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":204,"term_id":"IDPO:0000011","start":186,"version":2,"statement":[{"text":"We report the first NMR based solution structural data for the Cholera Toxin enzymatic domain (CTA1). We show that this free enzymatic domain partially unfolds at the C-terminus, and binds its protein partners at both the beginning and end of this activation process.","type":"Abstract"},{"text":"Many of the resonances present in the central random-coil region of the free enzyme are dispersed in the NMR spectrum for the active complex sample where CTA1 is selectively labeled. Thus, the binding of ARF6-GTP ligand to CTA1 results in an ordering (folding) of partially unfolded regions within the free enzymatic domain, indicating an allosteric coupling between these interaction partners (37).","type":"Results"},{"text":"The free CTA1 enzymatic domain is partially unfolded, in contrast to when it is complexed with either CTA2 in the holotoxin or with ARF6-GTP following retrotranslocation. Further strengthening this argument was that the refolded recombinant CTA1 is catalytically active (23) and, due to its thermal instability, CTA1 is a substrate for export to the cytosol via the ERAD pathway (33).","type":"Discussion"},{"text":"We propose that the primary role of ARF6- GTP binding is in site-to-site allostery (37) that couples the refolding of the C-terminus of CTA1 with the formation of a high-affinity CTA1:ARF6-GTP complex","type":"Discussion"},{"text":"Thus, CTA1 undergoes an ordered (holotoxin) to disordered (free CTA1) to ordered (CTA1:ARF6-GTP complex) structural transition (Figure 7) to accommodate the dual requirements of retrotranslocation and activation. This model proposes that the partially unfolded free enzyme recruits proteins from the ERAD pathway to promote its own retrotranslocation from the ER to the cytosol.","type":"Discussion"},{"text":"Numbering needs to be shifted by 18 residues to match the Uniprot sequence","type":"Curator statement"}],"term_name":"disorder to order","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"18272180","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"15162"}],"term_namespace":"Structural transition","ec_id":"ECO:0006165","curator_id":"lchemes","reference_html":"Order-disorder-order transitions mediate the activation of cholera toxin. <i> Ampapathi RS, Creath AL, Lou DI, Craft JW, Blanke SR, Legge GB. </i> J Mol Biol, 2008","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00250r029","validated":{"curator_id":"fquaglia","timestamp":"2020-12-19T23:07:47.778Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":204,"term_id":"GO:0005515","start":186,"version":3,"statement":[{"text":"We report the first NMR based solution structural data for the Cholera Toxin enzymatic domain (CTA1). We show that this free enzymatic domain partially unfolds at the C-terminus, and binds its protein partners at both the beginning and end of this activation process.","type":"Abstract"},{"text":"Many of the resonances present in the central random-coil region of the free enzyme are dispersed in the NMR spectrum for the active complex sample where CTA1 is selectively labeled. Thus, the binding of ARF6-GTP ligand to CTA1 results in an ordering (folding) of partially unfolded regions within the free enzymatic domain, indicating an allosteric coupling between these interaction partners (37).","type":"Results"},{"text":"The free CTA1 enzymatic domain is partially unfolded, in contrast to when it is complexed with either CTA2 in the holotoxin or with ARF6-GTP following retrotranslocation. Further strengthening this argument was that the refolded recombinant CTA1 is catalytically active (23) and, due to its thermal instability, CTA1 is a substrate for export to the cytosol via the ERAD pathway (33).","type":"Discussion"},{"text":"We propose that the primary role of ARF6- GTP binding is in site-to-site allostery (37) that couples the refolding of the C-terminus of CTA1 with the formation of a high-affinity CTA1:ARF6-GTP complex","type":"Discussion"},{"text":"Thus, CTA1 undergoes an ordered (holotoxin) to disordered (free CTA1) to ordered (CTA1:ARF6-GTP complex) structural transition (Figure 7) to accommodate the dual requirements of retrotranslocation and activation. This model proposes that the partially unfolded free enzyme recruits proteins from the ERAD pathway to promote its own retrotranslocation from the ER to the cytosol.","type":"Discussion"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P62330","partner_end":null}],"term_name":"protein binding","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"18272180","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"15162"}],"term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"lchemes","reference_html":"Order-disorder-order transitions mediate the activation of cholera toxin. <i> Ampapathi RS, Creath AL, Lou DI, Craft JW, Blanke SR, Legge GB. </i> J Mol Biol, 2008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00250r031","validated":{"curator_id":"fquaglia","timestamp":"2020-12-19T23:11:34.162Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":204,"term_id":"IDPO:0000011","start":186,"version":2,"statement":[{"text":"We report the first NMR based solution structural data for the Cholera Toxin enzymatic domain (CTA1). We show that this free enzymatic domain partially unfolds at the C-terminus, and binds its protein partners at both the beginning and end of this activation process.","type":"Abstract"},{"text":"Partial unfolding of CTA1 is further illustrated by using bis-ANS fluorescence as an indicator of the exposed hydrophobic character of the free enzyme, which is substantially reduced when bound to ARF6-GTP","type":"Abstract"},{"text":"The bis-ANS fluorescence reflects the extent of hydrophobic exposure (38) of CTA1 when compared to both the CTA1:ARF6-GTP complex and Gdm-HCl denatured samples (Figure 4). These data indicate bis-ANS fluorescence of the full length CTA1 sample is reduced in the truncated CTA1-T2 sample, and further reduced in the CTA1:ARF6-GTP sample or in the presence of chemical denaturants. These results indicate a loss of hydrophobic bis-ANS binding sites upon ARF6-GTP binding to the enzymatic domain, when fully unfolded or when truncated at the C-terminus. Therefore, ARF6-GTP binding is sufficient to induce profound changes in CTA1: from a partially disordered state in the free enzyme to an ordered state within the CTA1:ARF6-GTP complex.","type":"Results"},{"text":"The free CTA1 enzymatic domain is partially unfolded, in contrast to when it is complexed with either CTA2 in the holotoxin or with ARF6-GTP following retrotranslocation. Further strengthening this argument was that the refolded recombinant CTA1 is catalytically active (23) and, due to its thermal instability, CTA1 is a substrate for export to the cytosol via the ERAD pathway (33).","type":"Discussion"},{"text":"We propose that the primary role of ARF6- GTP binding is in site-to-site allostery (37) that couples the refolding of the C-terminus of CTA1 with the formation of a high-affinity CTA1:ARF6-GTP complex","type":"Discussion"},{"text":"Thus, CTA1 undergoes an ordered (holotoxin) to disordered (free CTA1) to ordered (CTA1:ARF6-GTP complex) structural transition (Figure 7) to accommodate the dual requirements of retrotranslocation and activation. This model proposes that the partially unfolded free enzyme recruits proteins from the ERAD pathway to promote its own retrotranslocation from the ER to the cytosol.","type":"Discussion"},{"text":"Numbering reported in the publication needs to be shifted by 18 residues to match the Uniprot sequence due to the presence of a signal peptide","type":"Curator statement"}],"term_name":"disorder to order","ec_name":"fluorescence evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"18272180","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural transition","ec_id":"ECO:0001249","curator_id":"lchemes","reference_html":"Order-disorder-order transitions mediate the activation of cholera toxin. <i> Ampapathi RS, Creath AL, Lou DI, Craft JW, Blanke SR, Legge GB. </i> J Mol Biol, 2008","ec_go":"IDA","disprot_namespace":"Structural transition"},{"region_id":"DP00250r034","validated":{"curator_id":"bmesza","timestamp":"2020-12-19T18:45:40.454Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":212,"term_id":"GO:0008289","start":19,"version":3,"statement":[{"text":"the isolated CTA1 polypeptide has a disordered conformation with minimal enzymatic activity against Gs or synthetic substrates at 37°C (Murayama et al., 1993; Ray et al., 2012). When CTA1-ARF interactions have been examined at 37°C, CTA1 and ARF are typically added together before incubation at 37°C (Murayama et al., 1993; Pande et al., 2007). This protocol allows ARF6 to stabilize the folded conformation of CTA1 initially present at low temperature, but it does not determine whether ARF6 can activate the disordered CTA1 subunit. In this paper we examined whether ARF6 can activate a disordered, as well as a structured, CTA1 polypeptide. A biochemical and biophysical analysis of CTA1 structure / function indicated that ARF6 cannot promote the refolding of disordered CTA1 to an active state. Instead, lipid rafts shifted the disordered, 37°C structure of CTA1 to a folded conformation with a basal level of activity that could be further stimulated by ARF6.","type":"Introduction"},{"text":"The lipochaperone function of lipid rafts (Ray et al., 2012) could act in conjunction with ARF to place disordered CTA1 in a folded, active conformation. This possibility was examined by FTIR spectroscopy (Fig. 4). CTA1 was heated to 37°C for 15 minutes before exposure to lipid raft-mimicking LUVs. Measurements of toxin structure were then recorded after an additional 30 minutes at 37°C (Fig. 4A). In the presence of lipid raft LUVs, the disordered conformation of CTA1 gained both α-helical and β-sheet content (Table 1). An additional gain of β-sheet structure and a further loss of irregular structure were detected when the disordered CTA1 subunit was incubated with both lipid rafts and ARF6/GTP (Fig. 4B). Under this condition, CTA1 exhibited an ordered conformation that matched the structural content of the folded, 10°C toxin (Table 1)","type":"Results"},{"text":"Because CTA1 is disordered at 37°C and ARF6/GTP does not promote the refolding of disordered CTA1 (Fig. 2, Table 1), it is necessary for other host factors such as lipid rafts to participate in shifting CTA1 from a disordered conformation to a partially folded active state that is competent for functional interaction with ARFs. The gain-of-structure resulting from toxin-raft interactions allows ARF6/GTP to induce an additional conformational change (Fig. 4, Table 1) that presumably stabilizes displacement of the occluding CTA1 “activation loop” and consequently optimizes the enzymatic activity of CTA1 (Fig. 5A).","type":"Discussion"}],"term_name":"lipid binding","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"25257027","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006228","curator_id":"lchemes","reference_html":"ADP-ribosylation factor 6 acts as an allosteric activator for the folded but not disordered cholera toxin A1 polypeptide. <i> Banerjee T, Taylor M, Jobling MG, Burress H, Yang Z, Serrano A, Holmes RK, Tatulian SA, Teter K. </i> Mol Microbiol, 2014","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00250r035","validated":{"curator_id":"bmesza","timestamp":"2020-12-19T18:45:41.720Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":212,"term_id":"GO:0008289","start":19,"version":3,"statement":[{"text":"the isolated CTA1 polypeptide has a disordered conformation with minimal enzymatic activity against Gs or synthetic substrates at 37°C (Murayama et al., 1993; Ray et al., 2012). When CTA1-ARF interactions have been examined at 37°C, CTA1 and ARF are typically added together before incubation at 37°C (Murayama et al., 1993; Pande et al., 2007). This protocol allows ARF6 to stabilize the folded conformation of CTA1 initially present at low temperature, but it does not determine whether ARF6 can activate the disordered CTA1 subunit. In this paper we examined whether ARF6 can activate a disordered, as well as a structured, CTA1 polypeptide. A biochemical and biophysical analysis of CTA1 structure / function indicated that ARF6 cannot promote the refolding of disordered CTA1 to an active state. Instead, lipid rafts shifted the disordered, 37°C structure of CTA1 to a folded conformation with a basal level of activity that could be further stimulated by ARF6.","type":"Introduction"},{"text":"In contrast to ARF6, large unilamellar vesicles (LUVs) mimicking the composition of a lipid raft could protect CTA1 from proteolysis even when they were added after toxin unfolding had already occurred (Fig. 1B). This was consistent with previous biophysical measurements demonstrating the chaperone-like ability of lipid rafts to stabilize folded CTA1 and to induce both a gain-of-structure and gain-of-function in the disordered CTA1 polypeptide (Ray et al., 2012). ARF6 and lipid rafts thus exhibited overlapping yet distinct interactions with CTA1: both could prevent the thermal unfolding of CTA1 to a protease-sensitive conformation, but only lipid rafts could shift disordered CTA1 back to a protease-resistant structure","type":"Results"},{"text":"Because CTA1 is disordered at 37°C and ARF6/GTP does not promote the refolding of disordered CTA1 (Fig. 2, Table 1), it is necessary for other host factors such as lipid rafts to participate in shifting CTA1 from a disordered conformation to a partially folded active state that is competent for functional interaction with ARFs. The gain-of-structure resulting from toxin-raft interactions allows ARF6/GTP to induce an additional conformational change (Fig. 4, Table 1) that presumably stabilizes displacement of the occluding CTA1 “activation loop” and consequently optimizes the enzymatic activity of CTA1 (Fig. 5A).","type":"Discussion"}],"term_name":"lipid binding","ec_name":"cleavage assay evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"25257027","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0007691","curator_id":"lchemes","reference_html":"ADP-ribosylation factor 6 acts as an allosteric activator for the folded but not disordered cholera toxin A1 polypeptide. <i> Banerjee T, Taylor M, Jobling MG, Burress H, Yang Z, Serrano A, Holmes RK, Tatulian SA, Teter K. </i> Mol Microbiol, 2014","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00250r036","validated":{"curator_id":"fquaglia","timestamp":"2020-12-19T23:11:43.607Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":204,"term_id":"IDPO:0000002","start":186,"version":2,"statement":[{"text":"We report the first NMR based solution structural data for the Cholera Toxin enzymatic domain (CTA1). We show that this free enzymatic domain partially unfolds at the C-terminus, and binds its protein partners at both the beginning and end of this activation process. Deviations from random coil chemical shifts (Δδcoil) indicate helix formation in the activation loop, which is essential to open the toxin’s active site, occurs prior to its association with human protein ARF6","type":"Abstract"},{"text":"Partial unfolding of CTA1 is further illustrated by using bis-ANS fluorescence as an indicator of the exposed hydrophobic character of the free enzyme, which is substantially reduced when bound to ARF6-GTP","type":"Abstract"},{"text":"The bis-ANS fluorescence reflects the extent of hydrophobic exposure (38) of CTA1 when compared to both the CTA1:ARF6-GTP complex and Gdm-HCl denatured samples (Figure 4). These data indicate bis-ANS fluorescence of the full length CTA1 sample is reduced in the truncated CTA1-T2 sample, and further reduced in the CTA1:ARF6-GTP sample or in the presence of chemical denaturants. These results indicate a loss of hydrophobic bis-ANS binding sites upon ARF6-GTP binding to the enzymatic domain, when fully unfolded or when truncated at the C-terminus. Therefore, ARF6-GTP binding is sufficient to induce profound changes in CTA1: from a partially disordered state in the free enzyme to an ordered state within the CTA1:ARF6-GTP complex.","type":"Results"},{"text":"Numbering reported in the publication needs to be shifted by 18 residues to match the Uniprot sequence due to the presence of a signal peptide","type":"Curator statement"}],"term_name":"disorder","ec_name":"fluorescence evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"18272180","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0001249","curator_id":"lchemes","reference_html":"Order-disorder-order transitions mediate the activation of cholera toxin. <i> Ampapathi RS, Creath AL, Lou DI, Craft JW, Blanke SR, Legge GB. </i> J Mol Biol, 2008","ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP00250r037","validated":{"curator_id":"fquaglia","timestamp":"2020-12-20T00:12:24.848Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":258,"term_id":"GO:0051179","start":254,"version":3,"statement":[{"text":"A cholera toxin mutant (CTX–K63) unable to raise cAMP levels was used to study in Vero cells the retrograde transport of the toxin A subunit (CTXA–K63), which possesses a COOH-terminal KDEL retrieval signal. Microinjected GTP-g-S inhibits the internalization as well as Golgi–ER transport of CTXA–K63. ","type":"Abstract"},{"text":"IgGs as well as Fab fragments directed against Erd2p, b-COP, or p23, a new member of the p24 protein family, inhibit or block retrograde transport of CTX-A–K63 from the Golgi without affecting its internalization or its transport to the Golgi. Anti-Erd2p antibodies do not affect the binding of CTX-A to Erd2p, but inhibit the CTX-K63–induced translocation of Erd2p and p53.","type":"Abstract"},{"text":"To analyze for a possible contribution of the cytoplasmically oriented COOH terminus of Erd2p to the sorting and the retrograde transport of the occupied Erd2p we analyzed the effect of antibodies raised against the COOH terminus of Erd2p on the retrograde transport of CTXA–K63. Anti-Erd2p IgGs injected before start of CTX– K63 uptake, did not significantly affect the retrograde transport from the plasma membrane to the Golgi (Table I). However, when the IgGs were injected 10–20 min after start of CTX–K63 uptake, we observed in ~60% of the cells an accumulation of CTX-A–K63 in perinuclear structures and an inhibition of translocation of CTX-A–K63 from the Golgi to the ER (Table I). ","type":"Results"},{"text":"To exclude the possibility that the anti-Erd2p–induced inhibition of retrograde transport of CTX-A–K63 from the Golgi to the ER had resulted from a decreased binding of CTX-A–K63 to Erd2p, we measured the effect of the anti-Erd2p antibodies on the binding of 125I-labeled CTX-A to permeabilized Golgi vesicles from Sf9 cells overexpressing human Erd2p. The antibody binding was performed at pH 7.2, the binding of CTX-A to Erd2p at pH 6. At pH 6 the binding of CTX-A to Erd2p was still sufficiently high (z60% of the binding observed at pH 5, unpublished results). Preincubation of the permeabilized Golgi membranes with anti-Erd2p antibodies did not affect binding of CTX-A to Erd2p (Fig. 9). Binding of CTX-A was specific as CTX-A could be displaced from the membranes by low concentrations of KDEL peptides but not by peptides without a COOH-terminal KDEL sequence (results not shown here). ","type":"Results"},{"text":"This is a true positive KDEL signal in the Eukaryotic Linear Motif Database","type":"Curator statement"}],"term_name":"localization","ec_name":"co-localization evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"9813083","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Biological process","ec_id":"ECO:0001163","curator_id":"lchemes","reference_html":"KDEL receptor (Erd2p)-mediated retrograde transport of the cholera toxin A subunit from the Golgi involves COPI, p23, and the COOH terminus of Erd2p. <i> Majoul I, Sohn K, Wieland FT, Pepperkok R, Pizza M, Hillemann J, Söling HD. </i> J Cell Biol, 1998","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"region_id":"DP00250r038","validated":{"curator_id":"fquaglia","timestamp":"2020-12-20T00:14:16.698Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":212,"term_id":"IDPO:0000014","start":19,"version":2,"statement":[{"text":"Cholera toxin is assembled from two subunits in the periplasm of Vibrio cholerae and disassembled in the analogous compartment of target cells, the lumen of the endoplasmic reticulum (ER), before a fragment of it, the A1 chain, is transported into the cytosol. We show that protein disulfide isomerase (PDI) in the ER lumen functions to disassemble and unfold the toxin once its A chain has been cleaved. ","type":"Abstract"},{"text":"We designed an assay that mimics the postulated disassembly of the toxin in vivo: after arrival in the ER, the B subunits should remain bound to the ganglioside GM1 in the membrane, while the A1 fragment of the toxin should be dissociated. In our assay, membrane bound ganglioside is replaced by GM1 covalently bound to polystyrene beads. Upon incubation with ER proteins, the B subunits are expected to stay with the beads and the A1 chain to be released. The A and B subunits of the toxin were expressed in V. cholerae and the holotoxin was purified (Rodighiero et al., 1999). Due to the presence of high levels of secreted proteases in the growth medium of V. cholerae, most of the toxin molecules (about 90%) had their A subunit cleaved into the A1 and A2 fragments. The purified, nicked holotoxin was bound to GM1-coated beads and incubated under different conditions. ","type":"Results"},{"text":"To test whether the holotoxin is dissociated by ER proteins, we prepared a lumenal extract from canine microsomes and incubated it with the toxin beads. A significant fraction of the A1 subunit was found to be released into the supernatant after collection of the beads (lanes 4 and 6). ","type":"Results"},{"text":"Next, we investigated whether the release of the A1 subunit was accompanied by its unfolding. To this end, we developed a protease protection assay. Addition of high concentrations of trypsin to the folded holotoxin left all polypeptide species intact (Figure 1B, lane 2 versus 1). However, after the addition of an extract derived from the ER lumen, the A and A1 subunits were degraded whereas the B subunit remained unaffected (lanes 4 and 6). Reduction of the disulfide bridge in the A subunit was insufficient to cause trypsin sensitivity (lane 2 versus 1). ","type":"Results"},{"text":"Our results provide insight into the pathway of cholera toxin from its synthesis in bacteria up to its arrival in the lumen of the ER in mammalian cells, where its A1 fragment is released from the rest of the toxin and unfolded in preparation for its translocation into the cytosol. ","type":"Discussion"},{"text":"Our results explain why cholera toxin is assembled and folded in the periplasm of bacteria and disassembled and unfolded in the ER, even though both compartments normally support the folding of polypeptides. One decisive factor is that the A subunit needs to be cleaved into the A1 and A2 fragments for unfolding to occur. The periplasm of bacteria seems to lack proteases that cleave the A chain, and in this compartment, the two subunits can therefore assemble and fold into the native holotoxin.  Once in the ER, PDI binds to the A1 chain and causes it to unfold, but it leaves the ring of B chains intact. ","type":"Discussion"}],"term_name":"order to disorder","ec_name":"cleavage assay evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"11290330","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural transition","ec_id":"ECO:0007691","curator_id":"lchemes","reference_html":"Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. <i> Tsai B, Rodighiero C, Lencer WI, Rapoport TA. </i> Cell, 2001","ec_go":"IDA","disprot_namespace":"Structural transition"},{"region_id":"DP00250r039","validated":{"curator_id":"fquaglia","timestamp":"2020-12-20T00:14:22.885Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":212,"term_id":"GO:0005515","start":19,"version":3,"statement":[{"text":"Cholera toxin is assembled from two subunits in the periplasm of Vibrio cholerae and disassembled in the analogous compartment of target cells, the lumen of the endoplasmic reticulum (ER), before a fragment of it, the A1 chain, is transported into the cytosol. We show that protein disulfide isomerase (PDI) in the ER lumen functions to disassemble and unfold the toxin once its A chain has been cleaved. ","type":"Abstract"},{"text":"To identify the unfolding activity in the ER lumen, we bound the proteins of the lumenal extract to a Q-Sepharose column. Upon elution with a salt gradient, protein fractions were analyzed for their ability to confer trypsin sensitivity to the A and A1 subunits. Addition of fractions 9 or 10 resulted in complete degradation of these toxin polypeptides (Figure 2A, lanes 18 and 20), similar to the effect observed with the unfractionated extract (lane 4). ","type":"Results"},{"text":"Fractions 9 and 10 contained one major band of ap- proximately 60 kDa (Figure 2B, lanes 8 and 9). This band was excised and identified as protein disulfide isomerase (PDI) by mass spectroscopy. Immunoblotting with an antibody directed against PDI confirmed this identifi- cation (Figure 2C, lanes 8 and 9). ","type":"Results"},{"text":"In addition, further purification of the material in fraction 9 on a S-Sepharose column demonstrated perfect cofractionation of PDI and the unfolding activity (Figure 2D). To confirm that the major unfolding activity in the ER lumen can be attributed to PDI, we immunodepleted PDI from the ex- tract (Figure 2E, left panel, lane 2 versus 1). While mock- depleted extract confered trypsin sensitivity to the toxin A and A1 subunits, the PDI-depleted extract was inactive (Figure 2E, right panel, lanes 6 versus 14). ","type":"Results"},{"text":"Our results provide insight into the pathway of cholera toxin from its synthesis in bacteria up to its arrival in the lumen of the ER in mammalian cells, where its A1 fragment is released from the rest of the toxin and unfolded in preparation for its translocation into the cytosol. ","type":"Discussion"},{"text":"Our results explain why cholera toxin is assembled and folded in the periplasm of bacteria and disassembled and unfolded in the ER, even though both compartments normally support the folding of polypeptides. One decisive factor is that the A subunit needs to be cleaved into the A1 and A2 fragments for unfolding to occur. The periplasm of bacteria seems to lack proteases that cleave the A chain, and in this compartment, the two subunits can therefore assemble and fold into the native holotoxin.  Once in the ER, PDI binds to the A1 chain and causes it to unfold, but it leaves the ring of B chains intact. ","type":"Discussion"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"A0A5F4DJ87","partner_end":null}],"term_name":"protein binding","ec_name":"mass spectrometry evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"11290330","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001230","curator_id":"lchemes","reference_html":"Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. <i> Tsai B, Rodighiero C, Lencer WI, Rapoport TA. </i> Cell, 2001","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00250r040","validated":{"curator_id":"fquaglia","timestamp":"2020-12-20T00:14:30.532Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":212,"term_id":"GO:0005515","start":19,"version":3,"statement":[{"text":"Cholera toxin is assembled from two subunits in the periplasm of Vibrio cholerae and disassembled in the analogous compartment of target cells, the lumen of the endoplasmic reticulum (ER), before a fragment of it, the A1 chain, is transported into the cytosol. We show that protein disulfide isomerase (PDI) in the ER lumen functions to disassemble and unfold the toxin once its A chain has been cleaved. ","type":"Abstract"},{"text":"Yeast PDI behaved in a similar way as the mammalian enzyme, despite their low sequence similarity (less than 25% identical amino acids). Purified yeast PDI was un- able to unfold the A subunit under oxidizing conditions (Figure 4A, lane 6 versus 5), but was active under reducing conditions (lane 8 versus 7). Similarly, it gave crosslinks to the A subunit only under reducing conditions (Figure 4B, lane 4 versus 3). ","type":"Results"},{"text":"Our results provide insight into the pathway of cholera toxin from its synthesis in bacteria up to its arrival in the lumen of the ER in mammalian cells, where its A1 fragment is released from the rest of the toxin and unfolded in preparation for its translocation into the cytosol. ","type":"Discussion"},{"text":"Our results explain why cholera toxin is assembled and folded in the periplasm of bacteria and disassembled and unfolded in the ER, even though both compartments normally support the folding of polypeptides. One decisive factor is that the A subunit needs to be cleaved into the A1 and A2 fragments for unfolding to occur. The periplasm of bacteria seems to lack proteases that cleave the A chain, and in this compartment, the two subunits can therefore assemble and fold into the native holotoxin.  Once in the ER, PDI binds to the A1 chain and causes it to unfold, but it leaves the ring of B chains intact. ","type":"Discussion"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P17967","partner_end":null}],"term_name":"protein binding","ec_name":"co-immunoprecipitation evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"11290330","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006030","curator_id":"lchemes","reference_html":"Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. <i> Tsai B, Rodighiero C, Lencer WI, Rapoport TA. </i> Cell, 2001","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00250r041","validated":{"curator_id":"fquaglia","timestamp":"2020-12-20T00:16:31.505Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":106,"term_id":"GO:0005515","start":101,"version":3,"statement":[{"text":"To determine whether HSC70 binds directly to CTA1, we perfused HSC70 over a CTA1-coated surface plasmon resonance (SPR) sensor at 15 or 37 °C (Fig. 4A). Previous studies have shown by CD, tryptophan fluorescence, and FTIR spectroscopy that CTA1 maintains a folded conformation at low temperature but transitions to a partially unfolded state at the physiological temperature of 37 °C (7, 49). HSC70 could bind to both the folded conformation of CTA1 present at 15 °C and the disordered conformation of CTA1 present at 37 °C. ","type":"Results"},{"text":"Both HSC70 and HSP90 form tight complexes with CTA1, as little dissociation is seen after removal of the chaperone from the perfusion buffer (Fig. 4A) (17, 18). We previously calculated a 7 nM KD affinity between HSP90 and CTA1 at 37 °C (17). HSC70 exhibited a similar 5 nM KD affinity for CTA1 at 37 °C (Fig. 4B). However, host-toxin interactions are not identical for the two chaperones: HSC70 will bind to either folded or disordered CTA1, whereas HSP90 only recognizes disordered CTA1 (18). ","type":"Results"},{"text":"To identify the CTA1-binding site(s) for HSC70, we generated a series of peptides that contained overlapping amino acid sequences from the entire length of the CTA1 subunit. As summarized in Table 1, HSC70 bound two consecutive peptides spanning CTA1 amino acid residues 73–98. These peptides contained a shared YYIYVI sequence that likely represented the core HSC70-binding site. The YYIYVI sequence alone could not be generated as a soluble hexapeptide, but we found a truncated GQTILSGHST peptide that lacked the YYIYVI motif and a mutant GQTILSGHSTYYLYVL peptide with leucine for iso- leucine substitutions in the YYIYVI motif could not bind to HSC70 (Table 1). These results indicated the YYIYVI motif was recognized by HSC70.  A competition assay further established the specificity of HSC70 binding to the YYIYVI sequence (Fig. 6). For this experiment, CTA1 was appended to an SPR sensor slide and exposed to perfusion buffer containing either HSC70 alone or HSC70 in combination with a CTA1-related peptide. HSC70 could bind to CTA1 in the absence of peptide and in the presence of the mutant GQTILSGHSTYYLYVL peptide. However, HSC70 could not bind to CTA1 in the presence of the GQTILSGH- STYYIYVI peptide. These observations confirmed HSC70 specifically recognizes the YYIYVI sequence in CTA1. ","type":"Results"},{"text":"18 residues need to be added to the numbering reported by the authors to match the Uniprot entry. The binding site YYIYVI corresponds to residues 101-106. HSP70 from  commercial origin, Enzo Life Sciences (Farmingdale, NY) corresponds to Bovine HSP70","type":"Curator statement"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P19120","partner_end":null}],"term_name":"protein binding","ec_name":"surface plasmon resonance evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"31221799","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001269","curator_id":"lchemes","reference_html":"HSC70 and HSP90 chaperones perform complementary roles in translocation of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol. <i> Burress H, Kellner A, Guyette J, Tatulian SA, Teter K. </i> J Biol Chem, 2019","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00250r042","validated":{"curator_id":"fquaglia","timestamp":"2020-12-21T08:05:12.547Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":212,"term_id":"GO:0005515","start":19,"version":3,"statement":[{"text":"Hsp90 bound to CTA1 in an ATP-dependent manner that was blocked by geldanamycin (GA), an established Hsp90 inhibitor.","type":"Abstract"},{"text":"To address this issue, SPR was used to determine whether Hsp90 could directly interact with the isolated CTA1 subunit at physiological temperature (Fig. 1A). Hsp90 binding to CTA1 occurred in an ATP-dependent manner that was blocked by GA. This demonstrated that Hsp90 could bind to CTA1 at 37 °C. Because CTA1 is in an unfolded conformation at 37 °C (22, 24), this also suggested that Hsp90 recognizes an unfolded conformation of CTA1 during the dislocation event","type":"Results"},{"text":"The interaction between Hsp90 and CTA1 was much stronger than the interaction between GRP94 and CTA1: Hsp90 bound to CTA1 with a KD of 7 nM, whereas GRP94 bound to CTA1 with a KD of 292 nM (Fig. 2 and Table 1). Consistent with the dimeric natures of Hsp90 and GRP94 (31), both chaperones bound to CTA1 in a 2:1 ratio of chaperone:toxin (Fig. 2). The specific, high-affinity interaction between Hsp90-ATP and CTA1 indicated that Hsp90 could be involved with the CT intoxication process","type":"Results"},{"text":"HSP90 origin is extracted from PMID: 31221799 to be Human HSP90 (Commercial origin; Biovision)","type":"Curator statement"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P08238","partner_end":null}],"term_name":"protein binding","ec_name":"surface plasmon resonance evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"20667832","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001269","curator_id":"lchemes","reference_html":"Hsp90 is required for transfer of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol. <i> Taylor M, Navarro-Garcia F, Huerta J, Burress H, Massey S, Ireton K, Teter K. </i> J Biol Chem, 2010","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P01555","date":"2016-09-09T10:58:57.000Z","acc":"P01555","name":"Cholera enterotoxin subunit A","length":258,"organism":"Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)","UniParc":"UPI0000001396","genes":[{"name":{"value":"ctxA"},"synonyms":[{"value":"toxA"}],"olnNames":[{"value":"VC_1457"}]}],"alphafold_very_low_content":0.04263565891472868,"disorder_content":0.751937984496124,"disprot_consensus":{"full":[{"start":19,"end":212,"type":"T"},{"start":254,"end":258,"type":"F"}],"Structural state":[{"start":19,"end":212,"type":"D"}],"Structural transition":[{"start":19,"end":212,"type":"T"}],"Molecular function":[{"start":19,"end":212,"type":"F"}],"Biological process":[{"start":254,"end":258,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01417","name":"ENTH domain","start":17,"end":140}],"gene3D":[{"start":1,"end":144,"id":"1.25.40.90","name":"1.25.40.90"}]},"uniref50":"UniRef50_O88339","sequence":"MSTSSLRRQMKNIVHNYSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREERAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDVQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGAPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTSDPWGSADGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAKASNPFLPSGAPATGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_O88339","disprot_id":"DP00251","ncbi_taxon_id":10116,"regions_counter":11,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":575,"region_id":"DP00251r001","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Unusual structural organization of the endocytic proteins AP180 and epsin 1. <i> Kalthoff C, Alves J, Urbanke C, Knorr R, Ungewickell EJ. </i> J Biol Chem, 2002","term_id":"IDPO:0000002","curator_id":"vnugnes","start":144,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"11756460","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-02-10T12:47:31.503Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sequence_construct":"RAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDVQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGAPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTSDPWGSADGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAKASNPFLPSGAPATGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL","statement":[{"text":"In the spectra of the fragments lacking the ENTH domains (His6-epsin 1-(144–575) and His6-AP180-(328–896)), the α-helical characteristics were almost completely lost, whereas the content of random structures increased from 56 to 66% for the epsin 1 fragment and from 55 to 84% for the AP180 fragment (Fig. 4,A and B).","type":"Results"}]},{"start":144,"end":575,"reference_id":"11756460","reference_source":"pmid","reference_html":"Unusual structural organization of the endocytic proteins AP180 and epsin 1. <i> Kalthoff C, Alves J, Urbanke C, Knorr R, Ungewickell EJ. </i> J Biol Chem, 2002","date":"2023-02-10T12:41:35.532Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00251r007","statement":[{"text":"The observed hydrodynamic size is consistent with either an extended rod with a thickness of 1.5–2.0 nm and a length of some 50 nm or, alternatively, a poorly folded polypeptide chain. Taken together, our data obtained from quantitative gel filtration chromatography and ultracentrifugation strongly suggest that the carboxyl-terminal parts of epsin 1 and AP180 are rather extended, with the consequence that they behave like very large proteins on gel filtration columns and like molecular parachutes during ultracentrifugation.","type":"Results"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sequence_construct":"RAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDVQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGAPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTSDPWGSADGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAKASNPFLPSGAPATGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL"},{"start":144,"end":575,"reference_id":"11756460","reference_source":"pmid","reference_html":"Unusual structural organization of the endocytic proteins AP180 and epsin 1. <i> Kalthoff C, Alves J, Urbanke C, Knorr R, Ungewickell EJ. </i> J Biol Chem, 2002","date":"2023-02-10T12:41:50.932Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00251r008","statement":[{"text":"The observed hydrodynamic size is consistent with either an extended rod with a thickness of 1.5–2.0 nm and a length of some 50 nm or, alternatively, a poorly folded polypeptide chain. Taken together, our data obtained from quantitative gel filtration chromatography and ultracentrifugation strongly suggest that the carboxyl-terminal parts of epsin 1 and AP180 are rather extended, with the consequence that they behave like very large proteins on gel filtration columns and like molecular parachutes during ultracentrifugation.","type":"Results"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sequence_construct":"RAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDVQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGAPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTSDPWGSADGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAKASNPFLPSGAPATGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL"},{"start":144,"end":575,"reference_id":"11756460","reference_source":"pmid","reference_html":"Unusual structural organization of the endocytic proteins AP180 and epsin 1. <i> Kalthoff C, Alves J, Urbanke C, Knorr R, Ungewickell EJ. </i> J Biol Chem, 2002","date":"2023-02-10T12:58:05.439Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006230","ec_ontology":"ECO","ec_name":"heat capacity-based evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"region_id":"DP00251r009","sequence_construct":"RAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDVQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGAPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTSDPWGSADGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAKASNPFLPSGAPATGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL","statement":[{"text":"SDS-PAGE analysis of the supernatant and pellet fractions indeed demonstrated that His6-epsin 1-(144–625) and His6-AP180-(328–896) were both heat-stable, whereas the full-length proteins and GST added as a carrier and internal standard did almost quantitatively precipitate (Fig.5 A). ","type":"Results"}]},{"start":144,"end":575,"reference_id":"11756460","reference_source":"pmid","reference_html":"Unusual structural organization of the endocytic proteins AP180 and epsin 1. <i> Kalthoff C, Alves J, Urbanke C, Knorr R, Ungewickell EJ. </i> J Biol Chem, 2002","date":"2023-02-10T13:27:11.057Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0048268","term_name":"clathrin coat assembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IDA","region_id":"DP00251r010","sequence_construct":"RAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDVQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGAPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTSDPWGSADGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAKASNPFLPSGAPATGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL","statement":[{"text":"Assuming that, in epsin 1, this activity is also located in the carboxyl-terminal part of the protein, we tested fragment His6-epsin 1-(144–575). As expected, this epsin 1 fragment also possessed assembly activity, although it was somewhat lower compared with that of the full-length protein.","type":"Results"}],"term_comment":"","term_def":"\"The process that results in the assembly of clathrin triskelia into the ordered structure known as a clathrin cage.\" [GOC:jid, PMID:11460887, PMID:11977118, PMID:9531549]","term_is_obsolete":false,"term_not_annotate":false},{"start":144,"end":575,"reference_id":"11756460","reference_source":"pmid","reference_html":"Unusual structural organization of the endocytic proteins AP180 and epsin 1. <i> Kalthoff C, Alves J, Urbanke C, Knorr R, Ungewickell EJ. </i> J Biol Chem, 2002","date":"2023-02-10T13:29:54.477Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0048268","term_name":"clathrin coat assembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IDA","region_id":"DP00251r011","sequence_construct":"RAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDVQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGAPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTSDPWGSADGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAKASNPFLPSGAPATGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL","statement":[{"text":"A, Coomassie Blue staining/SDS-PAGE of the supernatants (s) and pellets (p) after ultracentrifugation of the reaction mixtures showed that full-length epsin 1 very efficiently assembled clathrin. His6-epsin 1-(144–575) also assembled clathrin, albeit less efficiently than the full-length protein.","type":"Figure"}],"term_comment":"","term_def":"\"The process that results in the assembly of clathrin triskelia into the ordered structure known as a clathrin cage.\" [GOC:jid, PMID:11460887, PMID:11977118, PMID:9531549]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_O88339","date":"2016-08-31T14:13:26.000Z","acc":"O88339","name":"Epsin-1","length":575,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI00000E61F3","genes":[{"name":{"value":"Epn1"}}],"alphafold_very_low_content":0.41043478260869565,"disorder_content":0.7513043478260869,"disprot_consensus":{"full":[{"start":144,"end":575,"type":"D"}],"Structural state":[{"start":144,"end":575,"type":"D"}],"Biological process":[{"start":144,"end":575,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00290","name":"Tryptophan synthase alpha chain","start":8,"end":266}],"gene3D":[{"start":1,"end":268,"id":"3.20.20.70","name":"Aldolase class I"}]},"uniref50":"UniRef50_Q8ECU9","sequence":"MERYESLFAQLKERKEGAFVPFVTLGDPGIEQSLKIIDTLIEAGADALELGIPFSDPLADGPTIQNATLRAFAAGVTPAQCFEMLALIRQKHPTIPIGLLMYANLVFNKGIDEFYAQCEKVGVDSVLVADVPVEESAPFRQAALRHNVAPIFICPPNADDDLLRQIASYGRGYTYLLSRAGVTGAENRAALPLNHLVAKLKEYNAAPPLQGFGISAPDQVKAAIDAGAAGAISGSAIVKIIEQHINEPEKMLAALKVFVQPMKAATRS","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_Q8X7B5","disprot_id":"DP00252","ncbi_taxon_id":83333,"regions_counter":24,"creator":"eleonardi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":65,"region_id":"DP00252r005","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone. <i> Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K. </i> Biochemistry, 2005","term_id":"IDPO:0000002","curator_id":"eleonardi","start":55,"term_ontology":"IDPO","curator_name":"Emanuela Leonardi","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1V7Y:A"}],"reference_id":"15667212","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":65,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone. <i> Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K. </i> Biochemistry, 2005","term_id":"GO:0060090","curator_id":"eleonardi","start":55,"term_ontology":"GO","curator_name":"Emanuela Leonardi","reference_id":"15667212","version":3,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00252r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":65,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone. <i> Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K. </i> Biochemistry, 2005","term_id":"IDPO:0000011","curator_id":"eleonardi","start":55,"term_ontology":"IDPO","curator_name":"Emanuela Leonardi","reference_id":"15667212","version":2,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00252r007","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":65,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone. <i> Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K. </i> Biochemistry, 2005","term_id":"GO:0005515","curator_id":"eleonardi","start":55,"term_ontology":"GO","curator_name":"Emanuela Leonardi","reference_id":"15667212","version":3,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00252r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":65,"region_id":"DP00252r009","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone. <i> Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K. </i> Biochemistry, 2005","term_id":"IDPO:0000002","curator_id":"eleonardi","start":54,"term_ontology":"IDPO","curator_name":"Emanuela Leonardi","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1V7Y:B"}],"reference_id":"15667212","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":65,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone. <i> Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K. </i> Biochemistry, 2005","term_id":"GO:0060090","curator_id":"eleonardi","start":54,"term_ontology":"GO","curator_name":"Emanuela Leonardi","reference_id":"15667212","version":3,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00252r010","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":65,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone. <i> Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K. </i> Biochemistry, 2005","term_id":"IDPO:0000011","curator_id":"eleonardi","start":54,"term_ontology":"IDPO","curator_name":"Emanuela Leonardi","reference_id":"15667212","version":2,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00252r011","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":65,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone. <i> Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K. </i> Biochemistry, 2005","term_id":"GO:0005515","curator_id":"eleonardi","start":54,"term_ontology":"GO","curator_name":"Emanuela Leonardi","reference_id":"15667212","version":3,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00252r012","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":74,"region_id":"DP00252r017","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structures of wild-type and P28L/Y173F tryptophan synthase alpha-subunits from Escherichia coli. <i> Jeong MS, Jeong JK, Lim WK, Jang SB. </i> Biochem Biophys Res Commun, 2004","term_id":"IDPO:0000002","curator_id":"eleonardi","start":54,"term_ontology":"IDPO","curator_name":"Emanuela Leonardi","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1XCF:A"}],"reference_id":"15451433","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":74,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structures of wild-type and P28L/Y173F tryptophan synthase alpha-subunits from Escherichia coli. <i> Jeong MS, Jeong JK, Lim WK, Jang SB. </i> Biochem Biophys Res Commun, 2004","term_id":"GO:0060090","curator_id":"eleonardi","start":54,"term_ontology":"GO","curator_name":"Emanuela Leonardi","reference_id":"15451433","version":3,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00252r018","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":74,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structures of wild-type and P28L/Y173F tryptophan synthase alpha-subunits from Escherichia coli. <i> Jeong MS, Jeong JK, Lim WK, Jang SB. </i> Biochem Biophys Res Commun, 2004","term_id":"IDPO:0000011","curator_id":"eleonardi","start":54,"term_ontology":"IDPO","curator_name":"Emanuela Leonardi","reference_id":"15451433","version":2,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00252r019","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":74,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structures of wild-type and P28L/Y173F tryptophan synthase alpha-subunits from Escherichia coli. <i> Jeong MS, Jeong JK, Lim WK, Jang SB. </i> Biochem Biophys Res Commun, 2004","term_id":"GO:0005515","curator_id":"eleonardi","start":54,"term_ontology":"GO","curator_name":"Emanuela Leonardi","reference_id":"15451433","version":3,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00252r020","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_C4ZTV3","date":"2016-09-08T22:46:12.000Z","acc":"P0A877","name":"Tryptophan synthase alpha chain","length":268,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI000011F0D1","genes":[{"name":{"value":"trpA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00131","url":"https://hamap.expasy.org/unirule/MF_00131"}}]},"olnNames":[{"value":"b1260"},{"value":"JW1252"}]}],"alphafold_very_low_content":0,"disorder_content":0.07835820895522388,"disprot_consensus":{"full":[{"start":54,"end":74,"type":"T"}],"Structural state":[{"start":54,"end":74,"type":"D"}],"Molecular function":[{"start":54,"end":74,"type":"F"}],"Structural transition":[{"start":54,"end":74,"type":"T"}]}},{"features":{"pfam":[{"id":"PF02063","name":"MARCKS family","start":2,"end":305}]},"uniref50":"UniRef50_P30009","sequence":"MGAQFSKTAAKGEATAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAEPGAKEELQANGSAPAADKEEPASGSAATPAAAEKDEAAAATEPGAGAADKEAAEAEPAEPSSPAAEAEGASASSTSSPKAEDGAAPSPSSETPKKKKKRFSFKKSFKLSGFSFKKSKKESGEGAEAEGATAEGAKDEAAAAAGGEGAAAPGEQAGGAGAEGAAGGEPREAEAAEPEQPEQPEQPAAEEPQAEEQSEAAGEKAEEPAPGATAGDASSAAGPEQEAPAATDEAAASAAPAASPEPQPECSPEAPPAPTAE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P30009","disprot_id":"DP00253","ncbi_taxon_id":10090,"regions_counter":6,"creator":"fquaglia","regions":[{"start":1,"end":309,"reference_id":"9468306","reference_source":"pmid","reference_html":"MARCKS, a major protein kinase C substrate, assumes non-helical conformations both in solution and in complex with Ca2+-calmodulin. <i> Matsubara M, Yamauchi E, Hayashi N, Taniguchi H. </i> FEBS Lett, 1998","date":"2024-03-12T19:44:44.125Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP00253r003","statement":[{"text":"The CD spectrum of myr MARCKS and that of non-myr MARCKS taken under physiological conditions showed single negative peaks at around 200 nm, together with small negative peaks at 220–230 nm, suggesting that the recombinant proteins have a high content of random coil structure with a small amount of α-helix.","type":"Results"},{"text":"Although myr and non-myr MARCKS showed CD spectra with similar characteristics, the intensity of the negative peak at around 220–230 nm is smaller in myr MARCKS (Fig. 1b). This suggests that the presence of a myristoyl moiety may affect part of the three-dimensional structure of MARCKS.","type":"Results"}]},{"start":1,"end":309,"reference_id":"9468306","reference_source":"pmid","reference_html":"MARCKS, a major protein kinase C substrate, assumes non-helical conformations both in solution and in complex with Ca2+-calmodulin. <i> Matsubara M, Yamauchi E, Hayashi N, Taniguchi H. </i> FEBS Lett, 1998","date":"2024-03-12T19:55:31.323Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005516","term_name":"calmodulin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","region_id":"DP00253r004","statement":[{"text":"The addition of 150 nM recombinant myr MARCKS to 50 nM dansyl-calmodulin induced a shift in the fluorescence emission maximum of dansyl calmodulin from 510 to 490 nm as well as a 2-fold increase in the intensity at 490 nm (Fig. 2 a), suggesting that the recombinant protein retained the ability to bind to calmodulin. The dissociation constant determined by the direct fit of titration data to mass equation was 4.5±0.4 nM (n=3), a value comparable to those reported for native and recombinant protein preparations [7, 12].","type":"Results"}],"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":309,"reference_id":"9468306","reference_source":"pmid","reference_html":"MARCKS, a major protein kinase C substrate, assumes non-helical conformations both in solution and in complex with Ca2+-calmodulin. <i> Matsubara M, Yamauchi E, Hayashi N, Taniguchi H. </i> FEBS Lett, 1998","date":"2024-03-12T19:56:34.261Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005516","term_name":"calmodulin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","region_id":"DP00253r005","statement":[{"text":"CD spectra were measured with myr MARCKS mixed with calmodulin at a 1:1 ratio in the presence of Ca2+ or with the individual component alone. The CD spectra obtained with MARCKS alone or with calmodulin alone were mathematically added and the obtained spectrum was compared with the CD spectrum of the mixture (Fig. 2b). Although the depth of the large negative peak at 202 nm showed a difference, the broad peak around 220–230 nm, an indicator of the α-helical content, did not differ significantly. This implies that the full-length myr MARCKS binds to calmodulin in a non-helical structure. This is rather unusual for a calmodulin-binding protein; an increase in the α-helical content is observed upon the binding of a target protein to calmodulin. Similar results were obtained with non-myr MARCKS (data not shown).","type":"Results"}],"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":309,"reference_id":"9468306","reference_source":"pmid","reference_html":"MARCKS, a major protein kinase C substrate, assumes non-helical conformations both in solution and in complex with Ca2+-calmodulin. <i> Matsubara M, Yamauchi E, Hayashi N, Taniguchi H. </i> FEBS Lett, 1998","date":"2024-03-12T19:59:55.233Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000043","term_name":"myristoylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006283","ec_ontology":"ECO","ec_name":"electrospray ionization fourier transform ion cyclotron resonance mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP00253r006","statement":[{"text":"Electrospray mass spectroscopic analysis of the recombinant non-myr MARCKS and myr MARCKS proteins indicated that the mass difference of the two proteins was 210 Da, which corresponded very well to protein myristoylation.","type":"Methods"},{"text":"The recombinant myr MARCKS migrated in a 10% polyacrylamide gel with an apparent molecular mass of 80 kDa, whereas the recombinant non-myr MARCKS showed an apparent molecular mass of 68 kDa. The migrations correspond very well to those of the native myr and non-myr MARCKS proteins purified from bovine brain [16, 17]. Since the difference in mass caused by protein myristoylation is only 210 Da, the shift in migration of about 12 kDa in SDS gel may suggest a conformational change caused by the myristoyl moiety.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P26645","date":"2016-08-24T13:30:32.000Z","acc":"P26645","name":"Myristoylated alanine-rich C-kinase substrate","length":309,"organism":"Mus musculus","dataset":[],"UniParc":"UPI000000BA42","genes":[{"name":{"value":"Marcks"},"synonyms":[{"value":"Macs"}]}],"alphafold_very_low_content":0.6731391585760518,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":309,"type":"D"}],"Structural state":[{"start":1,"end":309,"type":"D"}],"Molecular function":[{"start":1,"end":309,"type":"F"}],"Disorder function":[{"start":1,"end":309,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04856","name":"Securin sister-chromatid separation inhibitor","start":9,"end":365}]},"uniref50":"UniRef50_P40316","sequence":"MMPANEDKENNIVYTGNESSGINFPQTPAHLLKRSHSNILKPPVRLDQLKRDANSNNGNTLKYIQGGKEVSPTKRLHTHAQQQGRLPLAAKDNNRSKSFIFPETSNQSKDADLPQLQNTLSIRKNDQLRKLSQISRSRSRANHNDLLSNSRKLQKYGSVLGYNALPKMKSLVLKDLADSGKNEESSDDDEGNEDSESKLGKKLQSALLKQDSSDGENELNGGLGLFNEQGGLQQLIKNSTKNEQKTKNDKSDKTDDYDIEIAPQRQEPLPYVPEGYSPFQQDDIEKLKTFNSPYKLDLEDEDDTPDKVDLLPLEQIDEEGEKDETECITRNQEEGAALPLLSKNFKEVAAVPTMELVYSEEGLDPEELEDLVT","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P40316","disprot_id":"DP00256","ncbi_taxon_id":559292,"regions_counter":8,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":110,"region_id":"DP00256r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"The regions of securin and cyclin B proteins recognized by the ubiquitination machinery are natively unfolded. <i> Cox CJ, Dutta K, Petri ET, Hwang WC, Lin Y, Pascal SM, Basavappa R. </i> FEBS Lett, 2002","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12220679","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-02-09T14:52:46.387Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The lack of dispersion seen for the amide chemical shifts in the WATERGATE spectra indicates a very similar environment for all amide hydrogen atoms in the proteins and therefore a random coil state for the polypeptide. Further indication of the unfolded state of both N-terminal fragments comes from examination of the methyl proton region of the spectra. As shown in Fig. 4B, the methyl protons display little dispersion. Furthermore, the methyl proton peaks are clustered in the region of ∼1.0–0.8 ppm, whereas peaks from methyl protons in a hydrophobic environment typically are shifted upfield to ∼0.5–0.0 ppm. Thus, 1H-NMR studies strongly indicate a largely unfolded conformation for both N-terminal fragments.","type":"Results"},{"text":"Of the observable NOEs, almost all have negative values, indicating fast tumbling and local flexibility. Thus, 1H,15N NOE analysis provides little indication of stable structure.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":110,"region_id":"DP00256r005","released":"2023_06","ec_id":"ECO:0006204","reference_html":"The regions of securin and cyclin B proteins recognized by the ubiquitination machinery are natively unfolded. <i> Cox CJ, Dutta K, Petri ET, Hwang WC, Lin Y, Pascal SM, Basavappa R. </i> FEBS Lett, 2002","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12220679","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-02-09T14:34:10.984Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The CD spectra of ND-cycB and ND-Pds1 (Fig. 3) are devoid of the significant signatures of secondary structure, most notably negative bands at 222 nm and 208 nm for α-helix and a negative band at 217 nm for β-sheet. Instead, the predominant feature is a strong negative band at 200 nm, which is correlated with a predominantly unstructured polypeptide.","type":"Results"},{"text":"A more compelling analysis involves examination of the degree of cooperativity in the change of CD spectra with increasing temperature. Cooperativity seems to be an unfailing hallmark of the folded-to-unfolded transition. As can be seen from measurements at the two characteristic wavelengths of 200 nm and 222 nm (Fig. 3), the variation of the ellipticity values with temperature does not display cooperativity; instead, the values vary linearly.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P40316","date":"2016-08-25T10:45:00.000Z","acc":"P40316","name":"Securin","length":373,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI00001314DD","genes":[{"name":{"value":"PDS1"},"orfNames":[{"value":"YD9727.08C"}],"olnNames":[{"value":"YDR113C"}]}],"alphafold_very_low_content":0.38337801608579086,"disorder_content":0.2949061662198391,"disprot_consensus":{"full":[{"start":1,"end":110,"type":"D"}],"Structural state":[{"start":1,"end":110,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00080","name":"Copper/zinc superoxide dismutase (SODC)","start":56,"end":188}],"gene3D":[{"start":40,"end":196,"id":"2.60.40.200","name":"Superoxide dismutase, copper/zinc binding domain"}]},"uniref50":"UniRef50_O31851","sequence":"MHRLLLLMMLTALGVAGCGQKKPPDPPNRVPEKKVVETSAFGHHVQLVNREGKAVGFIEIKESDDEGLDIHISANSLRPGASLGFHIYEKGSCVRPDFESAGGPFNPLNKEHGFNNPMGHHAGDLPNLEVGADGKVDVIMNAPDTSLKKGSKLNILDEDGSAFIIHEQADDYLTNPSGNSGARIVCGALLGNNEKQ","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Bacillus"],"uniref90":"UniRef90_O31851","disprot_id":"DP00257","ncbi_taxon_id":224308,"regions_counter":32,"creator":"ftonello","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":125,"region_id":"DP00257r009","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal. <i> Banci L, Bertini I, Calderone V, Cramaro F, Del Conte R, Fantoni A, Mangani S, Quattrone A, Viezzoli MS. </i> Proc Natl Acad Sci U S A, 2005","term_id":"IDPO:0000002","curator_id":"ftonello","start":89,"term_ontology":"IDPO","curator_name":"Fiorella Tonello","reference_id":"15897454","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1U3N"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":125,"term_name":"molecular function regulator","start":89,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ftonello","released":"2022_03","term_ontology":"GO","curator_name":"Fiorella Tonello","reference_id":"15897454","version":3,"reference_html":"A prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal. <i> Banci L, Bertini I, Calderone V, Cramaro F, Del Conte R, Fantoni A, Mangani S, Quattrone A, Viezzoli MS. </i> Proc Natl Acad Sci U S A, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006165","region_id":"DP00257r010","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":125,"term_name":"disorder to order","start":89,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ftonello","released":"2022_03","term_ontology":"IDPO","curator_name":"Fiorella Tonello","reference_id":"15897454","version":2,"reference_html":"A prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal. <i> Banci L, Bertini I, Calderone V, Cramaro F, Del Conte R, Fantoni A, Mangani S, Quattrone A, Viezzoli MS. </i> Proc Natl Acad Sci U S A, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00257r011","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":125,"term_name":"ion binding","start":89,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ftonello","released":"2022_03","term_ontology":"GO","curator_name":"Fiorella Tonello","reference_id":"15897454","version":3,"reference_html":"A prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal. <i> Banci L, Bertini I, Calderone V, Cramaro F, Del Conte R, Fantoni A, Mangani S, Quattrone A, Viezzoli MS. </i> Proc Natl Acad Sci U S A, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0043167","ec_id":"ECO:0006165","region_id":"DP00257r012","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":125,"region_id":"DP00257r013","released":"2022_03","ec_id":"ECO:0006220","reference_html":"A prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal. <i> Banci L, Bertini I, Calderone V, Cramaro F, Del Conte R, Fantoni A, Mangani S, Quattrone A, Viezzoli MS. </i> Proc Natl Acad Sci U S A, 2005","term_id":"IDPO:0000002","curator_id":"ftonello","start":89,"term_ontology":"IDPO","curator_name":"Fiorella Tonello","reference_id":"15897454","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1S4I"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":125,"term_name":"molecular function regulator","start":89,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ftonello","released":"2022_03","term_ontology":"GO","curator_name":"Fiorella Tonello","reference_id":"15897454","version":3,"reference_html":"A prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal. <i> Banci L, Bertini I, Calderone V, Cramaro F, Del Conte R, Fantoni A, Mangani S, Quattrone A, Viezzoli MS. </i> Proc Natl Acad Sci U S A, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006220","region_id":"DP00257r014","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":125,"term_name":"disorder to order","start":89,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ftonello","released":"2022_03","term_ontology":"IDPO","curator_name":"Fiorella Tonello","reference_id":"15897454","version":2,"reference_html":"A prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal. <i> Banci L, Bertini I, Calderone V, Cramaro F, Del Conte R, Fantoni A, Mangani S, Quattrone A, Viezzoli MS. </i> Proc Natl Acad Sci U S A, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00257r015","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":125,"term_name":"ion binding","start":89,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ftonello","released":"2022_03","term_ontology":"GO","curator_name":"Fiorella Tonello","reference_id":"15897454","version":3,"reference_html":"A prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal. <i> Banci L, Bertini I, Calderone V, Cramaro F, Del Conte R, Fantoni A, Mangani S, Quattrone A, Viezzoli MS. </i> Proc Natl Acad Sci U S A, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0043167","ec_id":"ECO:0006220","region_id":"DP00257r016","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_O31851","date":"2016-09-09T12:00:18.000Z","acc":"O31851","name":"Superoxide dismutase-like protein YojM","length":196,"organism":"Bacillus subtilis (strain 168)","dataset":[],"UniParc":"UPI0000060511","genes":[{"name":{"value":"yojM"},"olnNames":[{"value":"BSU19400"}]}],"alphafold_very_low_content":0.04081632653061224,"disorder_content":0.18877551020408162,"disprot_consensus":{"full":[{"start":89,"end":125,"type":"T"}],"Structural state":[{"start":89,"end":125,"type":"D"}],"Molecular function":[{"start":89,"end":125,"type":"F"}],"Structural transition":[{"start":89,"end":125,"type":"T"}]}},{"features":{"pfam":[],"gene3D":[{"start":346,"end":439,"id":"4.10.280.10","name":"Helix-loop-helix DNA-binding domain"}]},"uniref50":"UniRef50_P01106","sequence":"MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P01106","disprot_id":"DP00260","ncbi_taxon_id":9606,"regions_counter":41,"creator":"aelofsson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":88,"region_id":"DP00260r001","released":"2022_06","ec_id":"ECO:0006204","reference_html":"N and C-terminal sub-regions in the c-Myc transactivation region and their joint role in creating versatility in folding and binding. <i> Fladvad M, Zhou K, Moshref A, Pursglove S, Säfsten P, Sunnerhagen M. </i> J Mol Biol, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15663936","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-06-10T16:09:28.901Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The C-terminal sub-region Myc92–167 is partly helical with negative minima at 208 nm and 222 nm, while the N-terminal sub-region Myc1–88 shows little negative ellipticity around 222 nm and a minimum shifted towards 200 nm, which indicates a mainly random structure with low helical content.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T11:38:10.190Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":167,"region_id":"DP00260r004","released":"2022_06","ec_id":"ECO:0006327","reference_html":"N and C-terminal sub-regions in the c-Myc transactivation region and their joint role in creating versatility in folding and binding. <i> Fladvad M, Zhou K, Moshref A, Pursglove S, Säfsten P, Sunnerhagen M. </i> J Mol Biol, 2005","term_id":"IDPO:0000003","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15663936","version":3,"ec_name":"dynamic fluorescence quenching evidence used in manual assertion","date":"2022-06-10T18:01:22.476Z","reference_source":"pmid","term_name":"molten globule","curator_orcid":"0000-0001-8399-7907","ec_go":"IPI","disprot_namespace":"Structural state","statement":[{"text":"Myc1–167, Myc92–167 and Myc1–88 had emission maxima of 348, 342 and 351 nm, respectively, in non-denaturing buffer (Figure 5a) suggesting that the tryptophan residues are not completely buried in any of the proteins.34 All three proteins had an emission maximum at 353–355 nm under denaturing conditions, in agreement with data for unfolded proteins.34 This indicates a decrease in solvent exposure for Myc1–167 and Myc92–167 in native buffer that is in agreement with a partly folded structure, whereas the small change for Myc1–88 suggests that Myc1–88 remains unfolded, in agreement with the CD results.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T11:35:32.256Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":143,"region_id":"DP00260r010","released":"2022_06","ec_id":"ECO:0006204","reference_html":"Functional interaction of the c-Myc transactivation domain with the TATA binding protein: evidence for an induced fit model of transactivation domain folding. <i> McEwan IJ, Dahlman-Wright K, Ford J, Wright AP. </i> Biochemistry, 1996","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"8755740","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-06-10T16:10:48.218Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"In aqueous solution and over a range of temperatures, the c-myc1-143 polypeptide showed little or no secondary structure (Figure 5A). The spectra showed the characteristics of a random conformation with a minimum at around 200 nm and progressively nearing zero at wavelengths above 210 nm.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T11:35:05.438Z"}},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":143,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"vnugnes","released":"2022_12","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"8755740","version":5,"reference_html":"Functional interaction of the c-Myc transactivation domain with the TATA binding protein: evidence for an induced fit model of transactivation domain folding. <i> McEwan IJ, Dahlman-Wright K, Ford J, Wright AP. </i> Biochemistry, 1996","date":"2022-07-05T13:08:20.334Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00260r012","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P13393","operator":"and","partner_start":null,"partner_end":null}],"statement":[{"text":"However, the observed spectrum for the mixture is clearly distinct from the calculated additive spectra (Figure 6B). The most striking difference is the shift to the right and reduction in the minimum at around 200 nm derived from the c-myc1-143 polypeptide. Furthermore, the change in the 200 to 222 nm ratio to near unity is consistent with conversionof a random coil to an α-helical conformation.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T11:42:33.653Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":88,"region_id":"DP00260r016","released":"2022_06","ec_id":"ECO:0006165","reference_html":"Pre-Anchoring of Pin1 to Unphosphorylated c-Myc in a Fuzzy Complex Regulates c-Myc Activity. <i> Helander S, Montecchio M, Pilstål R, Su Y, Kuruvilla J, Elvén M, Ziauddin JME, Anandapadamanaban M, Cristobal S, Lundström P, Sears RC, Wallner B, Sunnerhagen M. </i> Structure, 2015","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-10T15:03:45.944Z","reference_source":"pmid","term_name":"disorder","reference_id":"26655473","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":62,"end":62,"position":"Specific residue","statements":[{"type":"Results","text":"To study the Ser62 phosphorylated state of c-Myc, we performed phosphorylation of c-Myc1–88 in vitro with active CDK2 kinase in complex with CyclinA2, which is known to phosphorylate Ser62-Pro63 in vivo (Hydbring et al., 2010) and in trans (Brown et al., 1999)."}]}],"sequence_construct":"MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDG","statement":[{"text":"Both 15N-R1 and {1H}-15N-nuclear Overhauser effect (NOE) relaxation of pSer62-c-Myc1–88 correspond well to results obtained for c-Myc1–88 at similar concentrations (Figures S1E–S1G), suggesting that the intrinsic disorder with transiently structured regions identified for c-Myc1–88 (Andresen et al., 2012) is maintained upon Ser62 phosphorylation.","type":"Results"}],"cross_refs":[{"db":"BMRB","id":"26663"},{"db":"BMRB","id":"26662"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T11:34:23.749Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":88,"term_name":"protein binding","released":"2022_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Pre-Anchoring of Pin1 to Unphosphorylated c-Myc in a Fuzzy Complex Regulates c-Myc Activity. <i> Helander S, Montecchio M, Pilstål R, Su Y, Kuruvilla J, Elvén M, Ziauddin JME, Anandapadamanaban M, Cristobal S, Lundström P, Sears RC, Wallner B, Sunnerhagen M. </i> Structure, 2015","term_id":"GO:0005515","curator_id":"vnugnes","start":1,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"26655473","version":5,"curator_orcid":"0000-0001-8399-7907","date":"2022-07-06T18:23:37.818Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00260r017","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q13526","operator":"and","partner_start":null,"partner_end":null}],"sequence_construct":"MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDG","statement":[{"text":"These observations are in agreement with the formation of dynamically disordered (Forman-Kay and Mittag, 2013), or “fuzzy” (Fuxreiter and Tompa, 2012), complexes.","type":"Results"},{"text":"Binding of intact Pin1 to non-phosphorylated c-Myc1–88 results in major loss of signal intensity primarily in the conserved, transiently ordered MB0 region, but also affects the MBI region (Figures 3A and 3D). Intact Pin1 binding to pSer62-c-Myc1–88 more clearly affects the phosphorylation site and flanking residues, and perturbations extend into the transiently helical and conserved MBI region around c-Myc1–88-Trp50, while the C-terminal part remains comparatively unperturbed (Figure 3D).","type":"Results"},{"text":"Furthermore, the NMR results suggest that the conserved, transiently structured MB0 region in c-Myc1–88 is central for Pin1 interactions with c-Myc1–88 irrespective of the phosphorylation state of Ser62.","type":"Results"},{"text":"MB0 region corresponds to residues 10–35 and MBI corresponds to the 44-63 region.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-11T13:13:14.735Z"}},{"start":1,"end":88,"reference_id":"22457068","reference_source":"pmid","reference_html":"Transient structure and dynamics in the disordered c-Myc transactivation domain affect Bin1 binding. <i> Andresen C, Helander S, Lemak A, Farès C, Csizmok V, Carlsson J, Penn LZ, Forman-Kay JD, Arrowsmith CH, Lundström P, Sunnerhagen M. </i> Nucleic Acids Res, 2012","date":"2022-06-10T14:51:07.148Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The plasmid pETMCSIII containing human c-Myc residues 1–88 with an N-terminal 6× His tag (31) was transformed into BL21(DE3) cells, incubated at 37°C until OD600 reached a level of 0.8, induced by 0.4 mM IPTG at 37°C for 5 h, harvested and resuspended in native lysis buffer (100 mM NaH2PO4, 10 mM Tris–HCl, 300 mM NaCl, pH 8.0), sonicated on ice 10 × 30 s and centrifuged at 10 000g for 30 min."}]}],"region_id":"DP00260r020","sequence_construct":"MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDG","statement":[{"text":"After extensive buffer optimization, the resolution in the HSQC spectrum of Myc-1–88 (Figure 2) is characteristic of an intrinsically disordered protein, with all amide proton shifts confined to 7.7–8.6 ppm. However, while intrinsically disordered proteins typically have uniformly sharp resonances, the Myc-1–88 spectra demonstrated heterogeneity of peak intensities and peak shapes likely reflecting an interconverting and transiently interacting heterogeneous ensemble of states.","type":"Results"},{"text":"Relaxation parameters for interpretable residues show that in the unbound state, the entire Myc-1–88 behaves as an intrinsically disordered protein with intermediate mobility (Figure 7; empty symbols). The magnitude of the heteronuclear NOEs are consistent with a disordered region, but are higher than expected for single-domain intrinsically disordered proteins. Instead, their magnitude resembles those of longer intrinsically disordered regions linked to well-folded globular domains (61,62).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T11:33:59.993Z"}},{"start":1,"end":88,"reference_id":"26655473","reference_source":"pmid","reference_html":"Pre-Anchoring of Pin1 to Unphosphorylated c-Myc in a Fuzzy Complex Regulates c-Myc Activity. <i> Helander S, Montecchio M, Pilstål R, Su Y, Kuruvilla J, Elvén M, Ziauddin JME, Anandapadamanaban M, Cristobal S, Lundström P, Sears RC, Wallner B, Sunnerhagen M. </i> Structure, 2015","date":"2022-06-10T15:28:10.816Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q13526","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00260r021","sequence_construct":"MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDG","statement":[{"text":"SPR measurements showed significant binding of Pin1 to unphosphorylated c-Myc outside of the Pin1-targeted MBI (Figures 2, S2A, and S2B), and, in agreement NMR mapping of HNCO intensity ratios, suggests that Pin1 primarily binds to the MB0 region (c-Myc10–35) (Figure 3).","type":"Results"},{"text":"MBI corresponds to the 44-63 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T11:47:53.210Z"}},{"start":1,"end":88,"reference_id":"15663936","reference_source":"pmid","reference_html":"N and C-terminal sub-regions in the c-Myc transactivation region and their joint role in creating versatility in folding and binding. <i> Fladvad M, Zhou K, Moshref A, Pursglove S, Säfsten P, Sunnerhagen M. </i> J Mol Biol, 2005","date":"2022-06-10T18:02:35.082Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006327","ec_ontology":"ECO","ec_name":"dynamic fluorescence quenching evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP00260r022","statement":[{"text":"This indicates a decrease in solvent exposure for Myc1–167 and Myc92–167 in native buffer that is in agreement with a partly folded structure, whereas the small change for Myc1–88 suggests that Myc1–88 remains unfolded, in agreement with the CD results.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T11:33:22.074Z"}},{"start":1,"end":167,"reference_id":"15663936","reference_source":"pmid","reference_html":"N and C-terminal sub-regions in the c-Myc transactivation region and their joint role in creating versatility in folding and binding. <i> Fladvad M, Zhou K, Moshref A, Pursglove S, Säfsten P, Sunnerhagen M. </i> J Mol Biol, 2005","date":"2022-06-10T18:06:01.225Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006200","ec_ontology":"ECO","ec_name":"circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP00260r023","statement":[{"text":"Fitting the denaturation curves to a linear extrapolation model assuming two-state unfolding33 shows that both Myc1–167 and Myc92–167 have low cooperative unfolding but that Myc1–167 has a significantly higher melting transition temperature (∼41 °C) than does Myc92–167 (∼32 °C) (Figure 4b).","type":"Results"},{"text":"The low cooperativity in unfolding is also consistent with a molten globule-like state.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T11:33:04.727Z"}},{"start":89,"end":167,"reference_id":"15663936","reference_source":"pmid","reference_html":"N and C-terminal sub-regions in the c-Myc transactivation region and their joint role in creating versatility in folding and binding. <i> Fladvad M, Zhou K, Moshref A, Pursglove S, Säfsten P, Sunnerhagen M. </i> J Mol Biol, 2005","date":"2022-06-10T18:21:32.716Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P20226","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q99471","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP00260r024","statement":[{"text":"After immobilization, the activity of the three c-Myc surfaces was assayed by MM-1 and TBP, which have previously been shown to bind to c-Myc.18, 26 Both of the proteins showed binding to Myc92–167 and Myc1–167 (Figure 7) but no significant binding was seen to Myc1–88, not even at higher concentration of MM-1 or TBP.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T11:54:28.934Z"}},{"start":89,"end":167,"reference_id":"15663936","reference_source":"pmid","reference_html":"N and C-terminal sub-regions in the c-Myc transactivation region and their joint role in creating versatility in folding and binding. <i> Fladvad M, Zhou K, Moshref A, Pursglove S, Säfsten P, Sunnerhagen M. </i> J Mol Biol, 2005","date":"2022-06-10T18:45:51.523Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q99471","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP00260r025","statement":[{"text":"Myc1–167 showed a shift in spectral intensity upon binding to MM-1 consistent with an increase in secondary structure upon binding to MM-1. A much smaller shift was observed for MM-1 with Myc92–167, whereas the spectrum of Myc1–88 with MM-1 was identical with the theoretical additive spectrum.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T11:54:26.134Z"}},{"start":1,"end":143,"reference_id":"8755740","reference_source":"pmid","reference_html":"Functional interaction of the c-Myc transactivation domain with the TATA binding protein: evidence for an induced fit model of transactivation domain folding. <i> McEwan IJ, Dahlman-Wright K, Ford J, Wright AP. </i> Biochemistry, 1996","date":"2022-06-10T19:29:53.107Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006076","ec_ontology":"ECO","ec_name":"protein binding evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P41896","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P13393","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP00260r026","sequence_construct":"MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAK","statement":[{"text":"A selective interaction was observed between c-myc1-143 transactivation domain and TBP and the RAP74 subunit of TFIIF (Figure 2A).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T11:55:07.073Z"}},{"start":1,"end":143,"reference_id":"8755740","reference_source":"pmid","reference_html":"Functional interaction of the c-Myc transactivation domain with the TATA binding protein: evidence for an induced fit model of transactivation domain folding. <i> McEwan IJ, Dahlman-Wright K, Ford J, Wright AP. </i> Biochemistry, 1996","date":"2022-06-10T19:18:29.802Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140537","term_name":"transcription regulator activator activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005616","ec_ontology":"ECO","ec_name":"beta-galactosidase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IEP","region_id":"DP00260r027","sequence_construct":"MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAK","statement":[{"text":"Expression of wild type c-myc1-143 fused to the DBD of the glucocorticoid receptor in yeast cells resulted in strong (almost 200-fold) induction of a lac Z reporter gene driven by a single glucocorticoid response element (Figure 3A).","type":"Results"}],"term_comment":"Usage guidance: transcription regulator activators bind to a transcription regulator to allow it to reach the chromatin or to contact other transcriptional regulators. This activity does not occur at the promoter. For activities that do occur at the promoter, consider GO:0001216 ; DNA-binding transcription activator activity or GO:0003713; transcription coactivator activity; those activities respectively bind DNA themselves or positively regulate a transcription regulator when it is located at the chromatin.","term_def":"\"A molecular function regulator that increases the activity of a transcription regulator via direct binding and/or post-translational modification.\" [PMID:9597751]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T11:55:25.637Z"}},{"start":402,"end":412,"reference_id":"19022175","reference_source":"pmid","reference_html":"Structural rationale for the coupled binding and unfolding of the c-Myc oncoprotein by small molecules. <i> Follis AV, Hammoudeh DI, Wang H, Prochownik EV, Metallo SJ. </i> Chem Biol, 2008","date":"2022-07-05T14:00:38.946Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00260r028","statement":[{"text":"The lack of long and medium-range NOEs shows this region is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T11:32:45.046Z"}},{"start":363,"end":381,"reference_id":"19022175","reference_source":"pmid","reference_html":"Structural rationale for the coupled binding and unfolding of the c-Myc oncoprotein by small molecules. <i> Follis AV, Hammoudeh DI, Wang H, Prochownik EV, Metallo SJ. </i> Chem Biol, 2008","date":"2022-07-05T14:01:29.357Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00260r029","statement":[{"text":"The lack of long and medium-range NOEs shows this region is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T11:32:39.321Z"}},{"start":353,"end":439,"reference_id":"19022175","reference_source":"pmid","reference_html":"Structural rationale for the coupled binding and unfolding of the c-Myc oncoprotein by small molecules. <i> Follis AV, Hammoudeh DI, Wang H, Prochownik EV, Metallo SJ. </i> Chem Biol, 2008","date":"2022-07-05T15:01:11.407Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00260r030","statement":[{"text":"Alone, c-Myc353–437 displayed a CD signal typical of disordered protein regions (Tompa, 2002).","type":"Results"},{"text":"IDR boundaries are 353-439 since region 437-439 is not long enough to be ordered. ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T11:32:18.597Z"}},{"start":367,"end":439,"reference_id":"12769844","reference_source":"pmid","reference_html":"The F-box protein Skp2 participates in c-Myc proteosomal degradation and acts as a cofactor for c-Myc-regulated transcription. <i> von der Lehr N, Johansson S, Wu S, Bahram F, Castell A, Cetinkaya C, Hydbring P, Weidung I, Nakayama K, Nakayama KI, Söderberg O, Kerppola TK, Larsson LG. </i> Mol Cell, 2003","date":"2022-07-05T18:19:30.860Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1905761","term_name":"SCF ubiquitin ligase complex binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","region_id":"DP00260r031","statement":[{"text":"The shortest C-terminal fragment of c-Myc (mutant Δ2–366) was still able to bind to Skp2, suggesting that aa residues 367–439, comprising the HLH-Zip domain of c-Myc, are sufficient for Skp2 binding.","type":"Results"},{"text":"Taken together, these results suggest that the interaction between c-Myc and Skp2 requires an intact MB2 and a region in the HLH-Zip domain of c-Myc.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a SCF ubiquitin ligase complex.\" [GOC:dph, GOC:ha, GOC:TermGenie, PMID:19723762]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"interaction_partner":[{"db":"UniProt","id":"Q13309","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T11:56:11.753Z"}},{"start":129,"end":142,"reference_id":"12769844","reference_source":"pmid","reference_html":"The F-box protein Skp2 participates in c-Myc proteosomal degradation and acts as a cofactor for c-Myc-regulated transcription. <i> von der Lehr N, Johansson S, Wu S, Bahram F, Castell A, Cetinkaya C, Hydbring P, Weidung I, Nakayama K, Nakayama KI, Söderberg O, Kerppola TK, Larsson LG. </i> Mol Cell, 2003","date":"2022-07-05T18:19:42.535Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1905761","term_name":"SCF ubiquitin ligase complex binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","region_id":"DP00260r032","statement":[{"text":"In vitro binding studies showed that deletion of MB2 alone or in combination with MB1 reduced binding of IVT c-Myc to GST-Skp2, whereas deletion of MB1 alone had no effect (Figure 2C, left panel). Deletion of the C-terminal aa 215–439 (mutant ΔC) reduced but did not eliminate binding, whereas the combined ΔC+ΔMB2 deletion abolished the GST-Skp2 interaction.","type":"Results"},{"text":"Taken together, these results suggest that the interaction between c-Myc and Skp2 requires an intact MB2 and a region in the HLH-Zip domain of c-Myc.","type":"Results"},{"text":"MB2 comprised the region 129-142.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a SCF ubiquitin ligase complex.\" [GOC:dph, GOC:ha, GOC:TermGenie, PMID:19723762]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"Q13309","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T11:56:23.913Z"}},{"start":51,"end":69,"reference_id":"15150404","reference_source":"pmid","reference_html":"The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation. <i> Welcker M, Orian A, Jin J, Grim JE, Harper JW, Eisenman RN, Clurman BE. </i> Proc Natl Acad Sci U S A, 2004","date":"2022-07-06T18:25:02.036Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1905761","term_name":"SCF ubiquitin ligase complex binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005644","ec_ontology":"ECO","ec_name":"immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":58,"end":58,"position":"Specific residue"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q969H0","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00260r035","statement":[{"text":"The binding of these peptides to Fbw7 was strongly dependent upon T58 phosphorylation (Fig. 3D).","type":"Results"},{"text":"These data indicate that T58 phosphorylation regulates the physical interaction of Fbw7 with the c-Myc CPD and is required for Fbw7-driven c-Myc turnover.","type":"Results"},{"text":"C-Myc CPD corresponds to the Cdc4 phosphodegron motif 55-62.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a SCF ubiquitin ligase complex.\" [GOC:dph, GOC:ha, GOC:TermGenie, PMID:19723762]","term_is_obsolete":false,"term_not_annotate":false},{"start":55,"end":68,"reference_id":"15992821","reference_source":"pmid","reference_html":"A structure-based model of the c-Myc/Bin1 protein interaction shows alternative splicing of Bin1 and c-Myc phosphorylation are key binding determinants. <i> Pineda-Lucena A, Ho CS, Mao DY, Sheng Y, Laister RC, Muhandiram R, Lu Y, Seet BT, Katz S, Szyperski T, Penn LZ, Arrowsmith CH. </i> J Mol Biol, 2005","date":"2022-08-08T19:00:43.899Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"1MV0"},{"db":"ELM","id":"DEG_SCF_FBW7_1"},{"db":"ELM","id":"LIG_SH3_2"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"O00499","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00260r036","statement":[{"text":"We determined the structure of the complex between Bin1C−12A and a synthetic peptide, c-Myc(55-68), which includes the entire proline-rich region (Figure 5(a) and (b); and Table 1).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":55,"end":68,"reference_id":"15992821","reference_source":"pmid","reference_html":"A structure-based model of the c-Myc/Bin1 protein interaction shows alternative splicing of Bin1 and c-Myc phosphorylation are key binding determinants. <i> Pineda-Lucena A, Ho CS, Mao DY, Sheng Y, Laister RC, Muhandiram R, Lu Y, Seet BT, Katz S, Szyperski T, Penn LZ, Arrowsmith CH. </i> J Mol Biol, 2005","date":"2022-08-08T19:00:28.850Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"1MV0"},{"db":"ELM","id":"DEG_SCF_FBW7_1"},{"db":"ELM","id":"LIG_SH3_2"}],"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"O00499","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00260r037","statement":[{"text":"Both peptides were also able to interact with the Bin1CΔPxxP mutant, yielding Kd values of 18.4 μM for 12A and 9.2 μM for c-Myc.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":56,"end":60,"reference_id":"15103331","reference_source":"pmid","reference_html":"Phosphorylation-dependent degradation of c-Myc is mediated by the F-box protein Fbw7. <i> Yada M, Hatakeyama S, Kamura T, Nishiyama M, Tsunematsu R, Imaki H, Ishida N, Okumura F, Nakayama K, Nakayama KI. </i> EMBO J, 2004","date":"2022-07-05T19:16:44.759Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007719","ec_ontology":"ECO","ec_name":"immunodetection assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00260r038","statement":[{"text":"The His6-c-Myc substrate was shown to be phosphorylated by immunoblot analysis with antibodies that specifically recognize c-Myc phosphorylated on Thr-58 and Ser-62 (Figure 3C); the mutant His6-c-Myc(T58A/S62A) was not phosphorylated.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T12:02:04.301Z"}},{"start":60,"end":64,"reference_id":"15103331","reference_source":"pmid","reference_html":"Phosphorylation-dependent degradation of c-Myc is mediated by the F-box protein Fbw7. <i> Yada M, Hatakeyama S, Kamura T, Nishiyama M, Tsunematsu R, Imaki H, Ishida N, Okumura F, Nakayama K, Nakayama KI. </i> EMBO J, 2004","date":"2022-07-05T19:16:57.453Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007719","ec_ontology":"ECO","ec_name":"immunodetection assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00260r039","statement":[{"text":"The His6-c-Myc substrate was shown to be phosphorylated by immunoblot analysis with antibodies that specifically recognize c-Myc phosphorylated on Thr-58 and Ser-62 (Figure 3C); the mutant His6-c-Myc(T58A/S62A) was not phosphorylated.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T12:02:08.801Z"}},{"start":51,"end":66,"reference_id":"15103331","reference_source":"pmid","reference_html":"Phosphorylation-dependent degradation of c-Myc is mediated by the F-box protein Fbw7. <i> Yada M, Hatakeyama S, Kamura T, Nishiyama M, Tsunematsu R, Imaki H, Ishida N, Okumura F, Nakayama K, Nakayama KI. </i> EMBO J, 2004","date":"2022-07-05T19:30:34.232Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1905761","term_name":"SCF ubiquitin ligase complex binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":58,"end":58,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":62,"end":62,"position":"Specific residue"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q969H0","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00260r040","statement":[{"text":"Recombinant Fbw7 interacted only with the phosphorylated form of the peptide, whereas Skp2, Fbw1a, Fbw2, or Fbw4 did not interact with either form (Figure 3A). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a SCF ubiquitin ligase complex.\" [GOC:dph, GOC:ha, GOC:TermGenie, PMID:19723762]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T12:03:53.312Z"}}],"released":"2016_10","uniref100":"UniRef100_P01106","date":"2016-09-05T14:48:12.000Z","acc":"P01106-1","name":"Myc proto-oncogene protein","length":439,"organism":"Homo sapiens","dataset":["Autophagy-related proteins","Cancer-related proteins"],"UniParc":"UPI0000000C1A","genes":[{"name":{"value":"MYC"},"synonyms":[{"value":"BHLHE39"}]}],"alphafold_very_low_content":0.3690205011389522,"disorder_content":0.5785876993166287,"disprot_consensus":{"full":[{"start":1,"end":167,"type":"D"},{"start":353,"end":439,"type":"D"}],"Structural state":[{"start":1,"end":167,"type":"D"},{"start":353,"end":439,"type":"D"}],"Molecular function":[{"start":1,"end":167,"type":"F"},{"start":367,"end":439,"type":"F"}],"Disorder function":[{"start":56,"end":64,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00989","name":"PAS fold","start":94,"end":149},{"id":"PF08447","name":"PAS fold","start":254,"end":339},{"id":"PF08778","name":"HIF-1 alpha C terminal transactivation domain","start":790,"end":825},{"id":"PF11413","name":"Hypoxia-inducible factor-1","start":555,"end":580},{"id":"PF23171","name":"Hypoxia-inducible factor 1-alpha bHLH domain","start":1,"end":80}],"gene3D":[{"start":7,"end":70,"id":"4.10.280.10","name":"Helix-loop-helix DNA-binding domain"},{"start":237,"end":380,"id":"3.30.450.20","name":"PAS domain"},{"start":87,"end":228,"id":"3.30.450.20","name":"PAS domain"}]},"uniref50":"UniRef50_Q16665","sequence":"MEGAGGANDKKKISSERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNVSSHLDKASVMRLTISYLRVRKLLDAGDLDIEDDMKAQMNCFYLKALDGFVMVLTDDGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREMLTHRNGLVKKGKEQNTQRSFFLRMKCTLTSRGRTMNIKSATWKVLHCTGHIHVYDTNSNQPQCGYKKPPMTCLVLICEPIPHPSNIEIPLDSKTFLSRHSLDMKFSYCDERITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMFTKGQVTTGQYRMLAKRGGYVWVETQATVIYNTKNSQPQCIVCVNYVVSGIIQHDLIFSLQQTECVLKPVESSDMKMTQLFTKVESEDTSSLFDKLKKEPDALTLLAPAAGDTIISLDFGSNDTETDDQQLEEVPLYNDVMLPSPNEKLQNINLAMSPLPTAETPKPLRSSADPALNQEVALKLEPNPESLELSFTMPQIQDQTPSPSDGSTRQSSPEPNSPSEYCFYVDSDMVNEFKLELVEKLFAEDTEAKNPFSTQDTDLDLEMLAPYIPMDDDFQLRSFDQLSPLESSSASPESASPQSTVTVFQQTQIQEPTANATTTTATTDELKTVTKDRMEDIKILIASPSPTHIHKETTSATSSPYRDTQSRTASPNRAGKGVIEQTEKSHPRSPNVLSVALSQRTTVPEEELNPKILALQNAQRKRKMEHDGSLFQAVGIGTLLQQPDDHAATTSLSWKRVKGCKSSEQNGMEQKTIILIPSDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q16665","disprot_id":"DP00262","ncbi_taxon_id":9606,"regions_counter":26,"creator":"grivas","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":698,"region_id":"DP00262r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Binding of natively unfolded HIF-1alpha ODD domain to p53. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Mol Cell, 2005","term_id":"IDPO:0000002","curator_id":"esalladini","start":530,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"15629713","statement":[{"text":"The far-UV CD spectra for HIF-1α 530–698 and HIF-1a 403–603 (Figures 2A and 2C) lacked the typical signatures of secondary structure (negative bands at 222 and 208 nm for α helices and a negative band at 217 nm for β sheets), exhibiting instead only a small signal at 200 nm.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-26T12:47:47.816Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":698,"region_id":"DP00262r002","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Binding of natively unfolded HIF-1alpha ODD domain to p53. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Mol Cell, 2005","term_id":"IDPO:0000002","curator_id":"esalladini","start":530,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"chromatography evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"15629713","statement":[{"text":"HIF-1α 530–698 and HIF-1α 403–603 eluted from the gel filtration column as well-defined peaks corresponding to Mr 95,500 and 134,700, respectively (Figure 1A), values five and six times larger than the calculated theoretical values of 18.8 and 22.3 kDa.","type":"Results"},{"text":"These results imply that both HIF-1α 530–698 and HIF-1α 403–603 have the dimensions of denatured proteins and have extended conformations.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-26T12:47:28.416Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":698,"region_id":"DP00262r003","released":"2022_03","ec_id":"ECO:0006275","reference_html":"Binding of natively unfolded HIF-1alpha ODD domain to p53. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Mol Cell, 2005","term_id":"IDPO:0000002","curator_id":"esalladini","start":530,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"analytical ultracentrifugation evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"15629713","statement":[{"text":"Analysis of the sedimentation equilibrium centrifugation experiment, however, showed that both proteins were monomeric with a Mr of 18,000 ± 120 and 22,000 ± 500 (Figure 1B; as an example for HIF-1α 530–698).","type":"Results"},{"text":"These results imply that both HIF-1α 530–698 and HIF-1α 403–603 have the dimensions of denatured proteins and have extended conformations.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-26T12:47:15.319Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":603,"region_id":"DP00262r004","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Binding of natively unfolded HIF-1alpha ODD domain to p53. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Mol Cell, 2005","term_id":"IDPO:0000002","curator_id":"esalladini","start":403,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"15629713","statement":[{"text":"The far-UV CD spectra for HIF-1α 530–698 and HIF-1a 403–603 (Figures 2A and 2C) lacked the typical signatures of secondary structure (negative bands at 222 and 208 nm for α helices and a negative band at 217 nm for β sheets), exhibiting instead only a small signal at 200 nm.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-26T12:46:51.026Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":603,"region_id":"DP00262r005","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Binding of natively unfolded HIF-1alpha ODD domain to p53. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Mol Cell, 2005","term_id":"IDPO:0000002","curator_id":"esalladini","start":403,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"chromatography evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"15629713","statement":[{"text":"HIF-1α 530–698 and HIF-1α 403–603 eluted from the gel filtration column as well-defined peaks corresponding to Mr 95,500 and 134,700, respectively (Figure 1A), values five and six times larger than the calculated theoretical values of 18.8 and 22.3 kDa.","type":"Results"},{"text":"These results imply that both HIF-1α 530–698 and HIF-1α 403–603 have the dimensions of denatured proteins and have extended conformations.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-26T12:46:26.776Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":826,"region_id":"DP00262r006","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response. <i> Dames SA, Martinez-Yamout M, De Guzman RN, Dyson HJ, Wright PE. </i> Proc Natl Acad Sci U S A, 2002","term_id":"IDPO:0000002","curator_id":"esalladini","start":776,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"11959977","statement":[{"text":"Hif-1α (776–826) in the unbound state is intrinsically disordered; its circular dichroism spectrum is characteristic of a random coil (data not shown) and the NMR spectrum lacks dispersion (Fig.1, red cross peaks).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-26T12:51:27.635Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":603,"region_id":"DP00262r007","released":"2022_03","ec_id":"ECO:0006275","reference_html":"Binding of natively unfolded HIF-1alpha ODD domain to p53. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Mol Cell, 2005","term_id":"IDPO:0000002","curator_id":"esalladini","start":403,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"analytical ultracentrifugation evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"15629713","statement":[{"text":"Analysis of the sedimentation equilibrium centrifugation experiment, however, showed that both proteins were monomeric with a Mr of 18,000 ± 120 and 22,000 ± 500 (Figure 1B; as an example for HIF-1α 530–698).","type":"Results"},{"text":"These results imply that both HIF-1α 530–698 and HIF-1α 403–603 have the dimensions of denatured proteins and have extended conformations.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-26T12:45:32.834Z"}},{"start":791,"end":804,"reference_id":"11959977","reference_source":"pmid","reference_html":"Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response. <i> Dames SA, Martinez-Yamout M, De Guzman RN, Dyson HJ, Wright PE. </i> Proc Natl Acad Sci U S A, 2002","date":"2022-06-14T19:55:48.699Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_06","version":3,"cross_refs":[{"db":"BMRB","id":"5327"},{"db":"PDB","id":"1L8C"}],"region_id":"DP00262r008","statement":[{"text":"The CAD becomes structured upon binding to TAZ1, as evidenced by the pronounced increase in dispersion of the amide proton resonances (Fig.1, black cross peaks).","type":"Results"},{"text":"The structure of the bound Hif-1α CAD is better defined after Gly-791.","type":"Results"},{"text":"The extended region of the Hif-1α CAD leads directly into a short α-helix (residues 796–804), termed αB, which docks in a groove formed by the N-terminal end of α1, helix α3, and the Zn3 site of TAZ1 (Fig.2B). Another helix, αC, is formed by residues 815–824. Helices αB and αC lie on opposite sides of helix α3 of TAZ1 (Fig.2B); residues 804–813 form an irregular bridge over α3 and make numerous contacts with the surface of TAZ1. In particular, the conserved leucines at positions 812 and 813 (Fig.4A) together with Ile-806 form a shallow hydrophobic groove that fits over two turns of helix α3 (Fig.4D).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P45481 "}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-25T14:55:13.796Z"}},{"start":815,"end":824,"reference_id":"11959977","reference_source":"pmid","reference_html":"Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response. <i> Dames SA, Martinez-Yamout M, De Guzman RN, Dyson HJ, Wright PE. </i> Proc Natl Acad Sci U S A, 2002","date":"2022-06-14T19:55:13.953Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_06","version":3,"cross_refs":[{"db":"BMRB","id":"5327"},{"db":"PDB","id":"1L8C"}],"region_id":"DP00262r009","statement":[{"text":"The CAD becomes structured upon binding to TAZ1, as evidenced by the pronounced increase in dispersion of the amide proton resonances (Fig.1, black cross peaks).","type":"Results"},{"text":"The structure of the bound Hif-1α CAD is better defined after Gly-791.","type":"Results"},{"text":"The extended region of the Hif-1α CAD leads directly into a short α-helix (residues 796–804), termed αB, which docks in a groove formed by the N-terminal end of α1, helix α3, and the Zn3 site of TAZ1 (Fig.2B). Another helix, αC, is formed by residues 815–824. Helices αB and αC lie on opposite sides of helix α3 of TAZ1 (Fig.2B); residues 804–813 form an irregular bridge over α3 and make numerous contacts with the surface of TAZ1. In particular, the conserved leucines at positions 812 and 813 (Fig.4A) together with Ile-806 form a shallow hydrophobic groove that fits over two turns of helix α3 (Fig.4D).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P45481 "},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-25T14:55:16.202Z"}},{"start":776,"end":826,"reference_id":"11959977","reference_source":"pmid","reference_html":"Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response. <i> Dames SA, Martinez-Yamout M, De Guzman RN, Dyson HJ, Wright PE. </i> Proc Natl Acad Sci U S A, 2002","date":"2022-06-14T20:30:16.051Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_06","version":4,"cross_refs":[{"db":"BMRB","id":"5327"},{"db":"PDB","id":"1L8C"}],"interaction_partner":[{"db":"UniProt","id":"P45481","partner_start":null,"partner_end":null}],"region_id":"DP00262r010","statement":[{"text":"The CAD becomes structured upon binding to TAZ1, as evidenced by the pronounced increase in dispersion of the amide proton resonances (Fig.1, black cross peaks).","type":"Results"},{"text":"Residues 776–790 in the N-terminal region of the Hif-1α CAD are poorly defined in the structures. Nevertheless, intermolecular NOEs are observed which show that this region of the CAD does bind, albeit weakly, in a broad shallow groove formed by helices α1 and α4 of TAZ1.","type":"Results"},{"text":"The extended region of the Hif-1α CAD leads directly into a short α-helix (residues 796–804), termed αB, which docks in a groove formed by the N-terminal end of α1, helix α3, and the Zn3 site of TAZ1 (Fig.2B). Another helix, αC, is formed by residues 815–824. Helices αB and αC lie on opposite sides of helix α3 of TAZ1 (Fig.2B); residues 804–813 form an irregular bridge over α3 and make numerous contacts with the surface of TAZ1. In particular, the conserved leucines at positions 812 and 813 (Fig.4A) together with Ile-806 form a shallow hydrophobic groove that fits over two turns of helix α3 (Fig.4D).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-25T14:56:08.079Z"}},{"start":776,"end":826,"reference_id":"11959977","reference_source":"pmid","reference_html":"Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response. <i> Dames SA, Martinez-Yamout M, De Guzman RN, Dyson HJ, Wright PE. </i> Proc Natl Acad Sci U S A, 2002","date":"2022-06-14T20:28:59.336Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005805","ec_ontology":"ECO","ec_name":"yeast 2-hybrid evidence used in manual assertion","released":"2022_06","version":4,"interaction_partner":[{"db":"UniProt","id":"P45481","partner_start":null,"partner_end":null}],"region_id":"DP00262r011","statement":[{"text":"Yeast two-hybrid assays confirmed that the constructs used for the NMR experiments, HIF-1α (776–826) and TAZ1 (345–439), interact specifically and with high affinity in vivo.","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-25T14:56:11.826Z"}},{"start":776,"end":826,"reference_id":"11959977","reference_source":"pmid","reference_html":"Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response. <i> Dames SA, Martinez-Yamout M, De Guzman RN, Dyson HJ, Wright PE. </i> Proc Natl Acad Sci U S A, 2002","date":"2022-06-14T20:28:43.560Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","released":"2022_06","version":4,"interaction_partner":[{"db":"UniProt","id":"P45481","partner_start":null,"partner_end":null}],"region_id":"DP00262r012","statement":[{"text":"The dissociation constant of the TAZ1/HIF-1α CAD complex was determined to be 7 ± 1 nM by ITC.","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-25T14:56:13.879Z"}},{"start":530,"end":698,"reference_id":"15629713","reference_source":"pmid","reference_html":"Binding of natively unfolded HIF-1alpha ODD domain to p53. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Mol Cell, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00262r013","statement":[{"text":"In addition, HIF-1α 530–698 and HIF-1α 403–603 both migrated as a 32 kDa protein in an SDS-PAGE gel even after heat denaturation (Figure 1A, inset).","type":"Results"},{"text":"These results imply that both HIF-1α 530–698 and HIF-1α 403–603 have the dimensions of denatured proteins and have extended conformations.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-26T12:45:01.567Z"}},{"start":403,"end":603,"reference_id":"15629713","reference_source":"pmid","reference_html":"Binding of natively unfolded HIF-1alpha ODD domain to p53. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Mol Cell, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00262r014","statement":[{"text":"In addition, HIF-1α 530–698 and HIF-1α 403–603 both migrated as a 32 kDa protein in an SDS-PAGE gel even after heat denaturation (Figure 1A, inset).","type":"Results"},{"text":"These results imply that both HIF-1α 530–698 and HIF-1α 403–603 have the dimensions of denatured proteins and have extended conformations.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-26T12:44:44.699Z"}},{"start":403,"end":603,"reference_id":"15629713","reference_source":"pmid","reference_html":"Binding of natively unfolded HIF-1alpha ODD domain to p53. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Mol Cell, 2005","date":"2022-06-14T20:23:35.114Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0002039","term_name":"p53 binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005632","ec_ontology":"ECO","ec_name":"fluorescence anisotropy evidence used in manual assertion","released":"2022_06","version":4,"interaction_partner":[{"db":"UniProt","id":"P04637","partner_start":null,"partner_end":null}],"region_id":"DP00262r015","statement":[{"text":"In contrast with HIF-1α 530–698, at the highest ionic strength (I 200 mM) it was possible to detect weak binding (Kd 600 μM) between HIF-1α 403–603 and p53 core, while at I 150 mM the binding was slightly tighter, Kd 200 μM.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to one of the p53 family of proteins.\" [GOC:hjd]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-25T14:56:16.093Z"}},{"start":403,"end":603,"reference_id":"15629713","reference_source":"pmid","reference_html":"Binding of natively unfolded HIF-1alpha ODD domain to p53. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Mol Cell, 2005","date":"2022-06-14T20:17:56.810Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0002039","term_name":"p53 binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","released":"2022_06","version":4,"interaction_partner":[{"db":"UniProt","id":"P04637","partner_start":null,"partner_end":null}],"region_id":"DP00262r016","statement":[{"text":"In both cases, however, the AUC data described species of 23 ± 1.2 and 48 ± 1 kDa, suggesting that even when the HIF-1α 403–603 construct contains the two binding sites predicted by Hansson et al. (2002), the stoichiometry of the complex is 1:1 (Figures 4C and 4D).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to one of the p53 family of proteins.\" [GOC:hjd]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-25T14:56:19.028Z"}},{"start":530,"end":698,"reference_id":"15629713","reference_source":"pmid","reference_html":"Binding of natively unfolded HIF-1alpha ODD domain to p53. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Mol Cell, 2005","date":"2022-06-14T20:17:18.072Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0002039","term_name":"p53 binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","released":"2022_06","version":4,"interaction_partner":[{"db":"UniProt","id":"P04637","partner_start":null,"partner_end":null}],"region_id":"DP00262r017","statement":[{"text":"For HIF-1α 530–698, at an ionic strength of 200 mM, no binding was detected, and the data best described a single species of Mr 21,000, corresponding to HIF-1α 530–698 alone. At physiological ionic strength (I 150 mM), the interaction was very weak (Kd 690 μM).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to one of the p53 family of proteins.\" [GOC:hjd]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-25T14:56:21.031Z"}},{"start":530,"end":698,"reference_id":"15629713","reference_source":"pmid","reference_html":"Binding of natively unfolded HIF-1alpha ODD domain to p53. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Mol Cell, 2005","date":"2022-06-14T20:24:00.649Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0002039","term_name":"p53 binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005632","ec_ontology":"ECO","ec_name":"fluorescence anisotropy evidence used in manual assertion","released":"2022_06","version":4,"region_id":"DP00262r018","statement":[{"text":"Using fluorescence anisotropy (Figures 5A and 5B), at lower ionic strengths the binding was tighter, with dissociation constants 30 and 0.16 μM at I 56 and 20 mM. respectively.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to one of the p53 family of proteins.\" [GOC:hjd]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P04637","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-25T14:56:23.990Z"}},{"start":776,"end":813,"reference_id":"17382325","reference_source":"pmid","reference_html":"Modulation of p300 binding by posttranslational modifications of the C-terminal activation domain of hypoxia-inducible factor-1alpha. <i> Cho H, Ahn DR, Park H, Yang EG. </i> FEBS Lett, 2007","date":"2022-06-14T20:28:25.771Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","released":"2022_06","version":4,"cross_refs":[{"db":"IntAct","id":"EBI-7354842"}],"region_id":"DP00262r019","statement":[{"text":"Although the residues 776–790 of HIF-1α, were implicated to interact, albeit weakly, with CBP [17], the two peptides showed similar binding affinities, with the dissociation constants of 196 ± 39 nM for F-HIF-1α-(776–786) and of 198 ± 23 nM for F-HIF-1α-(786–826). On the other hand, FP of F-HIF-1α-(788–822) increased much less, while F-HIF-1α-(776–813) showed no FP increase up to 3 μM GST-CBP (Fig. 2A).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q09472","operator":null,"partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-25T14:56:33.774Z"}},{"start":795,"end":822,"reference_id":"11063749","reference_source":"pmid","reference_html":"Molecular mechanism of hypoxia-inducible factor 1alpha -p300 interaction. A leucine-rich interface regulated by a single cysteine. <i> Gu J, Milligan J, Huang LE. </i> J Biol Chem, 2001","date":"2022-05-27T12:46:34.559Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140537","term_name":"transcription regulator activator activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006297","ec_ontology":"ECO","ec_name":"GAL4-VP16 functional complementation evidence used in manual assertion","released":"2022_06","version":5,"region_id":"DP00262r020","statement":[{"text":"These results confirm that the residues identified by RAMSY are functionally critical for CAD transcriptional activity in mammalian cells.","type":"Results"},{"text":"Therefore, we conclude that Leu-795, Cys-800, Leu-818, and Leu-822 of HIF1a are functionally indispensable for CAD transcriptional activity in mammalian cells.","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Usage guidance: transcription regulator activators bind to a transcription regulator to allow it to reach the chromatin or to contact other transcriptional regulators. This activity does not occur at the promoter. For activities that do occur at the promoter, consider GO:0001216 ; DNA-binding transcription activator activity or GO:0003713; transcription coactivator activity; those activities respectively bind DNA themselves or positively regulate a transcription regulator when it is located at the chromatin.","term_def":"\"A molecular function regulator that increases the activity of a transcription regulator via direct binding and/or post-translational modification.\" [PMID:9597751]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q09472","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-26T12:54:01.890Z"}},{"start":560,"end":567,"reference_id":"12050673","reference_source":"pmid","reference_html":"Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL. <i> Hon WC, Wilson MI, Harlos K, Claridge TD, Schofield CJ, Pugh CW, Maxwell PH, Ratcliffe PJ, Stuart DI, Jones EY. </i> Nature, 2002","date":"2022-08-08T19:13:46.464Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031625","term_name":"ubiquitin protein ligase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"1LQB"},{"db":"ELM","id":"DEG_ODPH_VHL_1"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P40337","operator":null,"partner_start":67,"partner_end":117}],"region_id":"DP00262r021","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15370 ","statements":[{"type":"Methods","text":"The proteins pVHL, elongin B and elongin C were co-expressed in Escherichia coli using vectors provided by N. Pavletich. The protein complex was purified essentially as described previously15."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15369","statements":[{"type":"Methods","text":"The proteins pVHL, elongin B and elongin C were co-expressed in Escherichia coli using vectors provided by N. Pavletich. The protein complex was purified essentially as described previously15."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"In contrast, recognition of HIF-1α by VCB E3 ligase (pVHL, elongins B and C, Cul2 and Rbx1; ref. 10) requires hydroxylation of specific prolyl residues by a group of 2-oxoglutarate-dependent, non-haem dioxygenases11,12.","type":"Article"},{"text":"Electron density for HIF-1α peptide residues 560–577 is of good quality, with only the side chain of E560 poorly defined (Fig. 1). The peptide lies in an extended conformation across one side of the β-domain of pVHL (Fig. 2a, b), binding to one of the β-sheets as if it were a complementary β-strand, although there is no extensive main-chain hydrogen bonding to define it as such.","type":"Article"},{"text":"Within the CODD peptide, residues 560–567 and 571–577 form distinct binding sites (sites 1 and 2, respectively).","type":"Article"},{"text":"Site 1 (EMLAHypYIP) is the primary binding site, contributing more than 60% of the total buried surface area and van der Waals contacts.","type":"Article"}],"term_comment":"","term_def":"\"Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.\" [GOC:vp]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MOD:00678","term_name":"hydroxylated proline","term_namespace":"Protein modification","start":564,"end":564,"position":"Specific residue"}]},{"start":556,"end":574,"reference_id":"12050673","reference_source":"pmid","reference_html":"Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL. <i> Hon WC, Wilson MI, Harlos K, Claridge TD, Schofield CJ, Pugh CW, Maxwell PH, Ratcliffe PJ, Stuart DI, Jones EY. </i> Nature, 2002","date":"2022-07-25T14:38:00.437Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031625","term_name":"ubiquitin protein ligase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"MOD:00678","term_name":"hydroxylated proline","term_namespace":"Protein modification","start":564,"end":564,"position":"Specific residue"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P40337","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00262r022","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15370 ","statements":[{"type":"Methods","text":"The proteins pVHL, elongin B and elongin C were co-expressed in Escherichia coli using vectors provided by N. Pavletich. The protein complex was purified essentially as described previously15."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15369","statements":[{"type":"Methods","text":"The proteins pVHL, elongin B and elongin C were co-expressed in Escherichia coli using vectors provided by N. Pavletich. The protein complex was purified essentially as described previously15."}]}],"statement":[{"text":"In contrast, recognition of HIF-1α by VCB E3 ligase (pVHL, elongins B and C, Cul2 and Rbx1; ref. 10) requires hydroxylation of specific prolyl residues by a group of 2-oxoglutarate-dependent, non-haem dioxygenases11,12.","type":"Article"},{"text":"Hydroxylated human CODD and NODD, and C. elegans ODD peptides, bind VCB with similar kinetics and binding affinities (29–53 nM).","type":"Article"}],"term_comment":"","term_def":"\"Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.\" [GOC:vp]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-25T14:38:37.241Z"}},{"start":561,"end":566,"reference_id":"12004076","reference_source":"pmid","reference_html":"Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling. <i> Min JH, Yang H, Ivan M, Gertler F, Kaelin WG, Pavletich NP. </i> Science, 2002","date":"2022-08-08T19:13:14.752Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031625","term_name":"ubiquitin protein ligase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","region_id":"DP00262r023","statement":[{"text":"It binds pVHL in a bipartite manner, with two discontinuous HIF-1α segments interacting with a continuous site on pVHL. A six-residue NH2-terminal segment (residues 561 to 566; N segment) that is centered on Hyp564 (Hyp is the three-letter code for hydroxyproline), and a four-residue COOH-terminal segment (residues 571 to 574; C segment) are separated by a four–amino acid bulge that does not contact pVHL (Fig. 1B).","type":"Article"},{"text":"A 20-residue HIF-1α ODD region (destruction sequence), conserved in animal orthologs and paralogs, is necessary and sufficient for hydroxylation by HPHs and for binding to pVHL (12, 13).","type":"Article"},{"text":"pVHL is the substrate-recognition subunit of a ubiquitin-protein ligase that also contains ElonginB, ElonginC, Cul2, and Rbx1 (VBC-CR complex) (6–9).","type":"Article"},{"text":"The VBC complex is a E3 ubiquitin ligase.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.\" [GOC:vp]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MOD:00678","term_name":"hydroxylated proline","term_namespace":"Protein modification","start":564,"end":564,"position":"Specific residue"}],"interaction_partner":[{"db":"UniProt","id":"P40337","operator":"and","partner_start":null,"partner_end":null}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15369"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15370"}],"cross_refs":[{"db":"PDB","id":"1LM8"},{"db":"ELM","id":"DEG_ODPH_VHL_1"}]},{"start":571,"end":574,"reference_id":"12004076","reference_source":"pmid","reference_html":"Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling. <i> Min JH, Yang H, Ivan M, Gertler F, Kaelin WG, Pavletich NP. </i> Science, 2002","date":"2022-08-08T19:13:05.210Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031625","term_name":"ubiquitin protein ligase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","region_id":"DP00262r024","statement":[{"text":"It binds pVHL in a bipartite manner, with two discontinuous HIF-1α segments interacting with a continuous site on pVHL. A six-residue NH2-terminal segment (residues 561 to 566; N segment) that is centered on Hyp564 (Hyp is the three-letter code for hydroxyproline), and a four-residue COOH-terminal segment (residues 571 to 574; C segment) are separated by a four–amino acid bulge that does not contact pVHL (Fig. 1B).","type":"Article"},{"text":"A 20-residue HIF-1α ODD region (destruction sequence), conserved in animal orthologs and paralogs, is necessary and sufficient for hydroxylation by HPHs and for binding to pVHL (12, 13).","type":"Article"},{"text":"pVHL is the substrate-recognition subunit of a ubiquitin-protein ligase that also contains ElonginB, ElonginC, Cul2, and Rbx1 (VBC-CR complex) (6–9).","type":"Article"},{"text":"The VBC complex is a E3 ubiquitin ligase.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.\" [GOC:vp]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MOD:00678","term_name":"hydroxylated proline","term_namespace":"Protein modification","start":564,"end":564,"position":"Specific residue"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15369"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15370"}],"interaction_partner":[{"db":"UniProt","id":"P40337","operator":"and","partner_start":null,"partner_end":null}],"cross_refs":[{"db":"PDB","id":"1LM8"},{"db":"ELM","id":"DEG_ODPH_VHL_1"}]},{"start":571,"end":577,"reference_id":"12050673","reference_source":"pmid","reference_html":"Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL. <i> Hon WC, Wilson MI, Harlos K, Claridge TD, Schofield CJ, Pugh CW, Maxwell PH, Ratcliffe PJ, Stuart DI, Jones EY. </i> Nature, 2002","date":"2022-08-08T19:10:48.851Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031625","term_name":"ubiquitin protein ligase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"MOD:00678","term_name":"hydroxylated proline","term_namespace":"Protein modification","start":564,"end":564,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"1LQB"},{"db":"ELM","id":"DEG_ODPH_VHL_1"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P40337","operator":null,"partner_start":67,"partner_end":117}],"region_id":"DP00262r025","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15370","statements":[{"type":"Methods","text":"The proteins pVHL, elongin B and elongin C were co-expressed in Escherichia coli using vectors provided by N. Pavletich. The protein complex was purified essentially as described previously15."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15369","statements":[{"type":"Methods","text":"The proteins pVHL, elongin B and elongin C were co-expressed in Escherichia coli using vectors provided by N. Pavletich. The protein complex was purified essentially as described previously15."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"In contrast, recognition of HIF-1α by VCB E3 ligase (pVHL, elongins B and C, Cul2 and Rbx1; ref. 10) requires hydroxylation of specific prolyl residues by a group of 2-oxoglutarate-dependent, non-haem dioxygenases11,12.","type":"Article"},{"text":"Electron density for HIF-1α peptide residues 560–577 is of good quality, with only the side chain of E560 poorly defined (Fig. 1). The peptide lies in an extended conformation across one side of the β-domain of pVHL (Fig. 2a, b), binding to one of the β-sheets as if it were a complementary β-strand, although there is no extensive main-chain hydrogen bonding to define it as such.","type":"Article"},{"text":"Within the CODD peptide, residues 560–567 and 571–577 form distinct binding sites (sites 1 and 2, respectively).","type":"Article"}],"term_comment":"","term_def":"\"Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.\" [GOC:vp]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_Q16665","date":"2016-09-08T16:45:23.000Z","acc":"Q16665","name":"Hypoxia-inducible factor 1-alpha","length":826,"organism":"Homo sapiens","dataset":["Autophagy-related proteins","Cancer-related proteins"],"UniParc":"UPI0000000A06","genes":[{"name":{"value":"HIF1A","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"7539918","url":"http://www.ncbi.nlm.nih.gov/pubmed/7539918","alternativeUrl":"https://europepmc.org/abstract/MED/7539918"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4910","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4910"}}]},"synonyms":[{"value":"BHLHE78"},{"value":"MOP1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9079689","url":"http://www.ncbi.nlm.nih.gov/pubmed/9079689","alternativeUrl":"https://europepmc.org/abstract/MED/9079689"}}]},{"value":"PASD8"}]}],"alphafold_very_low_content":0.5096852300242131,"disorder_content":0.42009685230024213,"disprot_consensus":{"full":[{"start":403,"end":698,"type":"D"},{"start":776,"end":790,"type":"D"},{"start":791,"end":804,"type":"T"},{"start":805,"end":814,"type":"D"},{"start":815,"end":824,"type":"T"},{"start":825,"end":826,"type":"D"}],"Structural state":[{"start":403,"end":698,"type":"D"},{"start":776,"end":826,"type":"D"}],"Structural transition":[{"start":791,"end":804,"type":"T"},{"start":815,"end":824,"type":"T"}],"Molecular function":[{"start":403,"end":698,"type":"F"},{"start":776,"end":826,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00377","name":"Prion/Doppel alpha-helical domain","start":133,"end":252},{"id":"PF03991","name":"Copper binding octapeptide repeat region","start":51,"end":94},{"id":"PF11587","name":"Major prion protein bPrPp - N terminal","start":1,"end":28}],"gene3D":[{"start":89,"end":230,"id":"1.10.790.10","name":"Prion/Doppel protein, beta-ribbon domain"}]},"uniref50":"UniRef50_P04925","sequence":"MANLGYWLLALFVTMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRSSSTVLFSSPPVILLISFLIFLIVG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P04925","disprot_id":"DP00265","ncbi_taxon_id":10090,"regions_counter":26,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":120,"region_id":"DP00265r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). <i> Riek R, Hornemann S, Wider G, Glockshuber R, Wüthrich K. </i> FEBS Lett, 1997","term_id":"IDPO:0000002","curator_id":"fquaglia","start":23,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"9280298","statement":[{"text":"The recombinant murine prion protein, mPrP(23-231), was expressed in E. coli with uniform 15N-labeling. NMR experiments showed that the previously determined globular three-dimensional structure of the C-terminal domain mPrP(121-231) is preserved in the intact protein, and that the N-terminal polypeptide segment 23-120 is flexibly disordered.","type":"Abstract"},{"text":"Dots represent the 98 residues of the N-terminal segment 23-120, which shows features of a flexible, 'random coil-like' polypeptide, with rotational correlation times for the ''N-'H groups of τc < 1 ns.","type":"Figure"},{"text":"The N-terminal polypeptide segment 23-120 has a small dispersion of the proton chemical shifts and τc-values <1 ns for the 15N-1H moieties, which is typical for a flexible 'random coil-like' polypeptide chain.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-17T08:46:31.426Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":105,"end":119,"reference_id":"17504807","reference_source":"pmid","reference_html":"Cellular prion protein interaction with vitronectin supports axonal growth and is compensated by integrins. <i> Hajj GN, Lopes MH, Mercadante AF, Veiga SS, da Silveira RB, Santos TG, Ribeiro KC, Juliano MA, Jacchieri SG, Zanata SM, Martins VR. </i> J Cell Sci, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P29788","partner_start":null,"partner_end":null}],"region_id":"DP00265r008","statement":[{"text":"We report that PrP(C) interacts with vitronectin but not with fibronectin or collagen. The binding sites mediating this PrP(C)-vitronectin interaction were mapped to residues 105-119 of PrP(C) and the residues 307-320 of vitronectin.","type":"Abstract"},{"text":"Of the twenty peptides from mouse PrPC covering the whole protein sequence used to compete for PrPC-Vn binding, two of them, corresponding to PrPC residues 103-122 and 113-132, effectively blocked (by ∼80%) PrPC-Vn binding (Fig. 2a).","type":"Results"},{"text":"Binding assays performed using four PrPC molecules presenting small deletions on the putative Vn binding site, revealed that the PrPC deletion mutants Δ105-112, Δ113-119, and Δ105-128 did not bind Vn, whereas mutants Δ51-90 and Δ120-125 exhibited binding capacity similar to that of the wild-type molecule (Fig. 2b). These data corroborate that the region comprising a.a. 105-119 of PrPC includes the binding site for Vn.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-17T08:46:43.785Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":95,"end":110,"reference_id":"19242475","reference_source":"pmid","reference_html":"Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. <i> Laurén J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM. </i> Nature, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001189","ec_ontology":"ECO","ec_name":"immunohistochemistry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"P05067","partner_start":null,"partner_end":null}],"region_id":"DP00265r010","statement":[{"text":"To distinguish whether the 95–110 charge cluster or the octapeptide repeat domain is crucial for Aβ42 binding, a mutant lacking the 52–91 segment was expressed. The Δ52–91 mutant exhibits significant Aβ42 binding, implicating the 95–110 region as a principal site for Aβ42-oligomer binding. Consistent with this hypothesis, deletion of 11 aa in the Δ95–105 variant reduces binding by 80%, and there was no further reduction in the Δ70–105 variant. ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T11:22:46.497Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":95,"end":110,"reference_id":"19242475","reference_source":"pmid","reference_html":"Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. <i> Laurén J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM. </i> Nature, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001150","ec_ontology":"ECO","ec_name":"blocking monoclonal antibody evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"P05067","partner_start":null,"partner_end":null}],"region_id":"DP00265r011","statement":[{"text":"Of six antibodies initially tested, only one (6D11) blocked the binding of Aβ42 assemblies to PrPC with an IC50 of 1 nM (Fig. 3b–d, Suppl. Fig. 8–10). The epitope for 6D11 corresponds to aa 93–109 of mouse PrPC, matching the conclusion that the 95–105 region is a primary determinant for binding. To confirm this hypothesis, we examined the effect of an additional antibody (8G8) with an overlapping epitope, aa 95–110. The 8G8 antibody blocked Aβ42-PrPC interaction, though with a lesser potency than 6D11.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T11:14:47.110Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":91,"end":123,"reference_id":"11438695","reference_source":"pmid","reference_html":"Location and properties of metal-binding sites on the human prion protein. <i> Jackson GS, Murray I, Hosszu LL, Gibbs N, Waltho JP, Clarke AR, Collinge J. </i> Proc Natl Acad Sci U S A, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"ChEBI","id":"29036","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"49786","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"29105","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"29035","partner_start":null,"partner_end":null}],"region_id":"DP00265r013","statement":[{"text":"Location and properties of metal-binding sites on the human prion protein","type":"Title"},{"text":"In this protein, residues 91–123 are unstructured and the NMR analysis shows that during titration to stoichiometry the major shifts occur in this region, chiefly centered around histidine residues 96 and 111.\n","type":"Results"},{"text":"Hence, the single binding site for transition metals on PrP (91) is selective and follows the order Cu(II) >> Ni(II) > Zn(II) >> Mn(II).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T11:14:41.010Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":52,"end":98,"reference_id":"11438695","reference_source":"pmid","reference_html":"Location and properties of metal-binding sites on the human prion protein. <i> Jackson GS, Murray I, Hosszu LL, Gibbs N, Waltho JP, Clarke AR, Collinge J. </i> Proc Natl Acad Sci U S A, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"ChEBI","id":"29036","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"49787","partner_start":null,"partner_end":null}],"region_id":"DP00265r014","statement":[{"text":"Location and properties of metal-binding sites on the human prion protein","type":"Title"},{"text":"Fig. ​Fig.33 shows a copper(II) titration of the octapeptide-repeat segment corresponding to residues 52–98.","type":"Figure"},{"text":"Copper(II) binding in the absence of glycine is biphasic; there is an initial phase representing the occupation of a single tight site, giving the ≈40% quench, followed by a weak binding phase with a Kd of 15 μM, which accounts for the remaining 50% loss of indole fluorescence.","type":"Results"},{"text":"Nickel(II) binds with a dissociation constant of 2 × 10−8 M, some six orders of magnitude weaker than copper(II). ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-17T08:46:38.524Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":93,"end":109,"reference_id":"28945221","reference_source":"pmid","reference_html":"α-synuclein interacts with PrP<sup>C</sup> to induce cognitive impairment through mGluR5 and NMDAR2B. <i> Ferreira DG, Temido-Ferreira M, Vicente Miranda H, Batalha VL, Coelho JE, Szegö ÉM, Marques-Morgado I, Vaz SH, Rhee JS, Schmitz M, Zerr I, Lopes LV, Outeiro TF. </i> Nat Neurosci, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001150","ec_ontology":"ECO","ec_name":"blocking monoclonal antibody evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"P37840","partner_start":null,"partner_end":null}],"region_id":"DP00265r016","statement":[{"text":"a-synuclein interacts with PrPC to induce cognitive\nimpairment through mGluR5 and NMDAR2B","type":"Title"},{"text":"To investigate the region(s) of PrPC that mediate the aSyn effects, we targeted three regions in the protein using different antibodies against PrPC: 6D11 (epitope targeting the region 93–109 of PrPC; 100 nM), 8B4 (epitope targeting the N terminus of PrPC; 10 µg) and C-20 (epitope targeting the C terminus of PrPC; 10 µg) (Fig. 1d). In slices pre-treated with 6D11 antibody, the effect of aSyn oligomers on LTP was blocked (P < 0.001; Fig. 1c). In contrast, pre-treatment with 8B4 or C-20 had no effect (P > 0.05; Fig. 1c and Supplementary Fig. 1h). This suggests that the 93–109 segment of PrPC is the crucial region for aSyn-induced toxic effects.","type":"Results"},{"text":"Thus, PrPC deletion or blockade at the 93–109 segment prevents aSyn-oligomer-induced impairments in both LTP and basal synaptic transmission, suggesting that PrPC mediates this synaptic dysfunction in a 6D11-sensitive manner.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T11:37:13.018Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":93,"end":109,"reference_id":"28945221","reference_source":"pmid","reference_html":"α-synuclein interacts with PrP<sup>C</sup> to induce cognitive impairment through mGluR5 and NMDAR2B. <i> Ferreira DG, Temido-Ferreira M, Vicente Miranda H, Batalha VL, Coelho JE, Szegö ÉM, Marques-Morgado I, Vaz SH, Rhee JS, Schmitz M, Zerr I, Lopes LV, Outeiro TF. </i> Nat Neurosci, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0140677","term_name":"molecular function activator activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006170","ec_ontology":"ECO","ec_name":"quantitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00265r017","statement":[{"text":"We asked whether PrPC was required for the observed aSyn-induced Src activation, but we could not detect any effect of aSyn on Src activation in neuronal cultures from Prnp−/− mice (P > 0.05; Fig. 2e). In addition, we found that the 6D11 antibody prevented Src activation by aSyn (P < 0.001; Fig. 2d,e), whereas neither the 8B4 nor C-20 antibodies prevented Src phosphorylation.","type":"Results"},{"text":"Y1472 of NMDAR2B is a major phosphorylation site of Fyn kinase15. We examined total and phosphorylated levels  of Y1472 NMDAR2B in neuronal cultures exposed to aSyn oligomers for different time periods. After 5 min of exposure, an increase in the levels of phospho-NMDAR2B was already detected, with no changes in the total levels of NMDAR2B (Supplementary Fig. 3f,g). This increase was blocked by the 6D11 antibody and the Fyn inhibitor (PP1, 30 μM, 25 min; P < 0.05; Fig. 2f), but was not affected by the 8B4 or C-20 antibodies. Consistent with this, aSyn oligomers failed to induce further NMDAR2B phosphorylation in neuronal cultures from Prnp−/− mice (Fig. 2f).","type":"Results"},{"text":"Thus, aSyn requires PrPC, particularly the 93–109 region, to induce Fyn activation and subsequent NMDAR2B phosphorylation, which may underlie the LTP impairments observed in the presence of aSyn oligomers.","type":"Results"},{"text":"As a consequence of the aSyn-Prp mediated activation of Fun and hyperphosforilation of NMDAR2B, disregulation of Ca2+ occurs and subsequent synaptic disfunction. \n","type":"Curator statement"},{"text":"our data suggest that the amino acid region 93–109 of PrPC is involved in mediating the toxic effects of aSyn.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-17T08:46:54.476Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":93,"end":109,"reference_id":"28945221","reference_source":"pmid","reference_html":"α-synuclein interacts with PrP<sup>C</sup> to induce cognitive impairment through mGluR5 and NMDAR2B. <i> Ferreira DG, Temido-Ferreira M, Vicente Miranda H, Batalha VL, Coelho JE, Szegö ÉM, Marques-Morgado I, Vaz SH, Rhee JS, Schmitz M, Zerr I, Lopes LV, Outeiro TF. </i> Nat Neurosci, 2017","date":"2022-03-08T15:23:53.918Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006076","ec_ontology":"ECO","ec_name":"protein binding evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP00265r018","statement":[{"text":"Next, by pulling down PrPC, we detected Fyn, NMDAR2B and aSyn in the same complex in WT, but not in Prnp−/−, slices in both control and aSyn-exposed slices (Fig. 2h). This was further validated by reverse co-IP, in which we pulled down aSyn and detected NMDAR2B, Fyn and PrPC (Fig. 2h).","type":"Results"},{"text":"Importantly, PrPC is extracellular and both Fyn and NMDAR2B are intracellular proteins. Authors also report that mGluR5 transmembrane protein might act as molecular bridge between PrPC, Fyn and NMDAR2B. Although authors do not provide evidence of a direct interaction. ","type":"Curator statement"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P37840","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-21T13:33:00.637Z"}},{"start":93,"end":109,"reference_id":"28945221","reference_source":"pmid","reference_html":"α-synuclein interacts with PrP<sup>C</sup> to induce cognitive impairment through mGluR5 and NMDAR2B. <i> Ferreira DG, Temido-Ferreira M, Vicente Miranda H, Batalha VL, Coelho JE, Szegö ÉM, Marques-Morgado I, Vaz SH, Rhee JS, Schmitz M, Zerr I, Lopes LV, Outeiro TF. </i> Nat Neurosci, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"P37840","partner_start":null,"partner_end":null}],"region_id":"DP00265r019","statement":[{"text":"When we immunoprecipitated either PrPC or aSyn from the hippocampus of aSyn transgenic mice, we detected the counterpart of the aSyn-PrPC complex (Fig. 2h)","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T11:36:59.618Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":23,"end":51,"reference_id":"30355631","reference_source":"pmid","reference_html":"Cellular Prion Protein Mediates the Disruption of Hippocampal Synaptic Plasticity by Soluble Tau <i>In Vivo</i>. <i> Ondrejcak T, Klyubin I, Corbett GT, Fraser G, Hong W, Mably AJ, Gardener M, Hammersley J, Perkinton MS, Billinton A, Walsh DM, Rowan MJ. </i> J Neurosci, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001150","ec_ontology":"ECO","ec_name":"blocking monoclonal antibody evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"P10636","partner_start":null,"partner_end":null}],"region_id":"DP00265r020","statement":[{"text":"Two antibodies to two different epitopes of PrPC abrogated the inhibition of LTP by two different sources of tau, recombinant soluble aggregated tau and AD brain-soluble extract. On the basis of the present findings, PrPC appears to be a crucial site of action for tau-mediated disruption of synaptic plasticity in vivo. ","type":"Results"},{"text":"Both antibodies target specific regions of the disordered N.terminus of Prp. One of them, MI-0131 antibody targets specifically 23-51 region of Prp. ","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-08T13:40:49.057Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":93,"end":109,"reference_id":"30355631","reference_source":"pmid","reference_html":"Cellular Prion Protein Mediates the Disruption of Hippocampal Synaptic Plasticity by Soluble Tau <i>In Vivo</i>. <i> Ondrejcak T, Klyubin I, Corbett GT, Fraser G, Hong W, Mably AJ, Gardener M, Hammersley J, Perkinton MS, Billinton A, Walsh DM, Rowan MJ. </i> J Neurosci, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001150","ec_ontology":"ECO","ec_name":"blocking monoclonal antibody evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"P10636","partner_start":null,"partner_end":null}],"region_id":"DP00265r021","statement":[{"text":"Two antibodies to two different epitopes of PrPC abrogated the inhibition of LTP by two different sources of tau, recombinant soluble aggregated tau and AD brain-soluble extract. On the basis of the present findings, PrPC appears to be a crucial site of action for tau-mediated disruption of synaptic plasticity in vivo. ","type":"Results"},{"text":"Both antibodies target specific regions of the disordered N.terminus of Prp. 6D11 antibody targets 93-109 region of PRP.\n","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-08T13:40:47.670Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":23,"end":51,"reference_id":"31853635","reference_source":"pmid","reference_html":"PrP is a central player in toxicity mediated by soluble aggregates of neurodegeneration-causing proteins. <i> Corbett GT, Wang Z, Hong W, Colom-Cadena M, Rose J, Liao M, Asfaw A, Hall TC, Ding L, DeSousa A, Frosch MP, Collinge J, Harris DA, Perkinton MS, Spires-Jones TL, Young-Pearse TL, Billinton A, Walsh DM. </i> Acta Neuropathol, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005581","ec_ontology":"ECO","ec_name":"enzyme-linked immunoabsorbent assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"P05067","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P37840","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P10636","partner_start":null,"partner_end":null}],"region_id":"DP00265r022","statement":[{"text":"Authors test whether AB soluble aggregates (SBAs), alpha-synuclein soluble aggregates (SAAs) and TAU soluble aggregates (STAs) are able to bind PrP in the absence and in the presence of competing antibodies, analyzed by ELISA. Being, MI-0131 a specific antibody of the 23-51 region and ICSM35 a specific antibody of the region 93-105. Both regions comprised in the N-terminus intrinsically disordered region of PrP. To confirm the hypothesis, the authors analyzed the interaction of PrP truncations lacking one or both of the hypothesized interacting regions.","type":"Curator statement"},{"text":"AB-->SBAs bound to PrP23–231 with an average EC50 of 38.9 nM, whereas neither Aβ monomers nor fibrils showed appreciable affinity for PrP (Fig. 2a). We tested whether mAbs directed to Site I (MI-0131) and Site II (ICSM35) (Supplementary Table 2) could prevent SPA binding. Both mAbs bound similarly well to PrP (Supplementary Figure 1e) and displaced SBAs to a comparable extent, with ICSM35 always slightly more effective (Fig. 2d).","type":"Results"},{"text":"Alpha-synuclein and TAU --> SAAs (Fig. 2b) and STAs (Fig. 2c) also bound to PrP in a saturable manner with average EC50s of 34.3 nM and 9.5 nM, respectively. Monomeric and fibrillar forms of αSyn and tau exhibited weak or no affinity for PrP23–231. we tested whether mAbs directed to Site I (MI-0131) and Site II (ICSM35) (Supplementary Table 2) could prevent SPA binding. Both mAbs bound similarly well to PrP (Supplementary Figure 1e) and displaced SBAs to a comparable extent, with ICSM35 always slightly more effective (Fig. 2d). Interestingly, comparable IC50 trends were observed for SAAs (Fig. 2e; ICSM35 = 5.2 nM and MI-0131 = 11.9 nM) and STAs (Fig. 2f; ICSM35 = 2.0 nM and MI-0131 = 5.0 nM). Similarly, SAAs and STAs showed little affinity for PrP119–231 and greatly diminished binding to PrP91–231 (Fig. 2h, i).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-08T12:43:51.609Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":93,"end":105,"reference_id":"31853635","reference_source":"pmid","reference_html":"PrP is a central player in toxicity mediated by soluble aggregates of neurodegeneration-causing proteins. <i> Corbett GT, Wang Z, Hong W, Colom-Cadena M, Rose J, Liao M, Asfaw A, Hall TC, Ding L, DeSousa A, Frosch MP, Collinge J, Harris DA, Perkinton MS, Spires-Jones TL, Young-Pearse TL, Billinton A, Walsh DM. </i> Acta Neuropathol, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005581","ec_ontology":"ECO","ec_name":"enzyme-linked immunoabsorbent assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"P05067","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P37840","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P10636","partner_start":null,"partner_end":null}],"region_id":"DP00265r023","statement":[{"text":"Authors test whether AB soluble aggregates (SBAs), alpha-synuclein soluble aggregates (SAAs) and TAU soluble aggregates (STAs) are able to bind PrP in the absence and in the presence of competing antibodies, analyzed by ELISA. Being, MI-0131 a specific antibody of the 23-51 region and ICSM35 a specific antibody of the region 93-105. Both regions comprised in the N-terminus intrinsically disordered region of PrP. To confirm the hypothesis, the authors analyzed the interaction of PrP truncations lacking one or both of the hypothesized interacting regions.","type":"Curator statement"},{"text":"AB-->SBAs bound to PrP23–231 with an average EC50 of 38.9 nM, whereas neither Aβ monomers nor fibrils showed appreciable affinity for PrP (Fig. 2a). We tested whether mAbs directed to Site I (MI-0131) and Site II (ICSM35) (Supplementary Table 2) could prevent SPA binding. Both mAbs bound similarly well to PrP (Supplementary Figure 1e) and displaced SBAs to a comparable extent, with ICSM35 always slightly more effective (Fig. 2d).","type":"Results"},{"text":"Alpha-synuclein and TAU --> SAAs (Fig. 2b) and STAs (Fig. 2c) also bound to PrP in a saturable manner with average EC50s of 34.3 nM and 9.5 nM, respectively. Monomeric and fibrillar forms of αSyn and tau exhibited weak or no affinity for PrP23–231. we tested whether mAbs directed to Site I (MI-0131) and Site II (ICSM35) (Supplementary Table 2) could prevent SPA binding. Both mAbs bound similarly well to PrP (Supplementary Figure 1e) and displaced SBAs to a comparable extent, with ICSM35 always slightly more effective (Fig. 2d). Interestingly, comparable IC50 trends were observed for SAAs (Fig. 2e; ICSM35 = 5.2 nM and MI-0131 = 11.9 nM) and STAs (Fig. 2f; ICSM35 = 2.0 nM and MI-0131 = 5.0 nM). Similarly, SAAs and STAs showed little affinity for PrP119–231 and greatly diminished binding to PrP91–231 (Fig. 2h, i).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-08T12:43:50.097Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":23,"end":114,"reference_id":"34102212","reference_source":"pmid","reference_html":"The N-terminal domain of the prion protein is required and sufficient for liquid-liquid phase separation: A crucial role of the Aβ-binding domain. <i> Kamps J, Lin YH, Oliva R, Bader V, Winter R, Winklhofer KF, Tatzelt J. </i> J Biol Chem, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007060","ec_ontology":"ECO","ec_name":"confocal laser scanning microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00265r024","statement":[{"text":"Authors study LLPS of the full-length protein and truncated versions corresponding to the disordered N-term, occurring in vivo. N1 harbors both interacting regions of the IDR of PrP, while N2 only harbors one interacting region. C1 and C2 correspond to the C-terminus PrP resulting from each cleavage, respectively. Finally, they mutate key charged residues (recognition motifs) and hydrophobic residues (central region of N1) to demonstrate that LLPS of Prp is driven by cation-pi interaction. ","type":"Curator statement"},{"text":"Full-length PrP rapidly formed droplets upon TEV protease cleavage, indicative of LLPS (Fig. 1C, TEV+). N1 underwent phase separation similarly to full-length PrP, indicating that the structural elements in the C-terminal domain are not required for the formation of biomolecular condensates. In contrast, N2 formed irregular assemblies instead of liquid-like droplets. Consequently, we analyzed C1 and C2, the C-terminal fragments generated after α- or β-cleavage, in parallel to N1 or N2 (Fig. 1A). Both before and after TEV cleavage, GFP fluorescence was evenly distributed, indicating that neither C1 nor C2 formed biomolecular condensates under these conditions, corroborating recent results (41).","type":"Results"},{"text":"Full-length PrPs as well as N1 molecules in the droplets were highly dynamic, characteristic of a liquid-like state. In contrast, fluorescence recovery of the irregular N2 structures was greatly delayed, indicating formation of a gel-like or aggregated state (Fig. 2A, lower panels). ","type":"Results"},{"text":"Results: We analyzed the conformation of phase-separated N1 after purifying recombinant N1 lacking both the MBP and GFP tag. The CD spectrum of N1 is characterized by a negative CD band below 210 nm, indicating that the protein displays a fully disordered secondary structure at this condition (46).","type":"Results"},{"text":"On the molecular level, phase separation is governed primarily by basic residues within the Aβ-binding domain, most likely through intermolecular cation–π interactions of the lysines with neighboring aromatic side chains (Fig. 4). ","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-08T13:00:08.990Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":23,"end":114,"reference_id":"34102212","reference_source":"pmid","reference_html":"The N-terminal domain of the prion protein is required and sufficient for liquid-liquid phase separation: A crucial role of the Aβ-binding domain. <i> Kamps J, Lin YH, Oliva R, Bader V, Winter R, Winklhofer KF, Tatzelt J. </i> J Biol Chem, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00265r025","statement":[{"text":"Authors study LLPS of the full-length protein and truncated versions corresponding to the disordered N-term, occurring in vivo. N1 harbors both interacting regions of the IDR of PrP.","type":"Curator statement"},{"text":"Dynamic light scattering (DLS) experiments were carried out to determine the size of the N1 droplets (Fig. 2E). Based on the intensity distribution functions of the hydrodynamic radius, the N1 samples exhibited a largely polydisperse size distribution pattern, indicative of droplet formation of sizes ranging from 40 to several 1000 nm.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-08T13:00:10.136Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":23,"end":114,"reference_id":"29791485","reference_source":"pmid","reference_html":"Alterations in the brain interactome of the intrinsically disordered N-terminal domain of the cellular prion protein (PrPC) in Alzheimer's disease. <i> Ulbrich S, Janning P, Seidel R, Matschke J, Gonsberg A, Jung S, Glatzel M, Engelhard M, Winklhofer KF, Tatzelt J. </i> PLoS One, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00265r026","statement":[{"text":"n total we identified 233 N-PrP-binding partners in the AD brain (Fig 2, S1 Table) and 212 in the non-AD brain (Fig 2, S2 Table). Among those 104 were overlapping interactors found in both brain homogenates (Fig 2, S3 Table), while 129 proteins were exclusively found in AD brain (Fig 2, S4 Table) and 107 in non-AD brain (Fig 2, S5 Table).","type":"Results"},{"text":"These findings support the concept that the intrinsically disordered N-terminal domain is a major mediator of PrP-protein interactions.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-17T08:46:47.265Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P04925","date":"2016-09-10T16:21:27.000Z","acc":"P04925","name":"Major prion protein","length":254,"organism":"Mus musculus","dataset":["Condensates-related proteins"],"UniParc":"UPI000014FB3C","genes":[{"name":{"value":"Prnp"},"synonyms":[{"value":"Prn-p"},{"value":"Prp"}]}],"alphafold_very_low_content":0.3937007874015748,"disorder_content":0.3858267716535433,"disprot_consensus":{"full":[{"start":23,"end":120,"type":"D"},{"start":121,"end":123,"type":"F"}],"Structural state":[{"start":23,"end":120,"type":"D"}],"Molecular function":[{"start":23,"end":123,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00028","name":"Cadherin domain","start":96,"end":186},{"id":"PF00028","name":"Cadherin domain","start":202,"end":291},{"id":"PF00028","name":"Cadherin domain","start":417,"end":493},{"id":"PF00028","name":"Cadherin domain","start":532,"end":613},{"id":"PF00028","name":"Cadherin domain","start":627,"end":722},{"id":"PF01049","name":"Cadherin, Y-type LIR-motif","start":1430,"end":1489},{"id":"PF02210","name":"Laminin G domain","start":1156,"end":1296},{"id":"PF24811","name":"DE-cadherin, Ig-like domain","start":936,"end":1083}],"gene3D":[{"start":1402,"end":1494,"id":"4.10.900.10","name":"TCF3-CBD (Catenin binding domain)"},{"start":413,"end":524,"id":"2.60.40.60","name":"Cadherins"},{"start":525,"end":624,"id":"2.60.40.60","name":"Cadherins"},{"start":194,"end":293,"id":"2.60.40.60","name":"Cadherins"},{"start":730,"end":828,"id":"2.60.40.60","name":"Cadherins"},{"start":1096,"end":1126,"id":"2.10.25.10","name":"Laminin"},{"start":297,"end":412,"id":"2.60.40.60","name":"Cadherins"},{"start":1129,"end":1313,"id":"2.60.120.200","name":"2.60.120.200"},{"start":625,"end":729,"id":"2.60.40.60","name":"Cadherins"},{"start":89,"end":193,"id":"2.60.40.60","name":"Cadherins"}]},"uniref50":"UniRef50_Q24298","sequence":"MSTSVQRMSRSYHCINMSATPQAGHLNPAQQQTHQQHKRKCRDLGRRLIPARLLLGVIVAISLLSPALALHSPPDKNFSGDNRKPAFKNCAGYAPKVKEEQPENTYVLTVEAVDPDPDQVIRYSIVQSPFERPKFFINPSTGVIFTTHTFDRDEPIHEKFVFVTVQATDNGLPPLDDVCTFNVTIEDINDNAPAFNKARYDESMSENAQPDAVVMTISASDFDDGNNSLVEYEILRERDFQYFKIDKESGIIYLKRPIDKRPGQSYAIIVRAYNVVPDPPQDAQIEVRIRVVESSIKPPSFVNPIDTPIYLKENLKNFTHPIATLRAVSNMPDKPEVIFELNTGRTEQTNSKNTFVFNQIGNEVTISLGKTLDYEAITDYTLTMIVRNTHELGTEHQIKIQVEDVNDNIPYYTEVKSGTILENEPPGTPVMQVRAFDMDGTSANNIVSFELADNREYFTIDPNTGNITALTTFDREERDFYNVKVIASDNSPSSLFDNGEPNRGHQVFRISIGDKNDHKPHFQQDKYLAERLLEDANTNTEVIEVKAEDEDNASQILYSIESGNVGDAFKIGLKTGKITVNQKLDYETITEYELKVRAFDGIYDDYTTVVIKIEDVNDNPPVFKQDYSVTILEETTYDDCILTVEAYDPDIKDRNADQHIVYSIHQNDGNRWTIDNSGCLRLVKTLDRDPPNGHKNWQVLIKANDEDGVGTTVSTVKEVTVTLKDINDNAPFLINEMPVYWQENRNPGHVVQLQANDYDDTPGAGNFTFGIDSEATPDIKTKFSMDGDYLHANVQFDREAQKEYFIPIRISDSGVPRQSAVSILHLVIGDVNDNAMSEGSSRIFIYNYKGEAPETDIGRVFVDDLDDWDLEDKYFEWKDLPHDQFRLNPSTGMITMLVHTAEGEYDLSFVVTEDSMFVPRHSVDAYVTVVVRELPEEAVDKSGSIRFINVTKEEFISVPRDFQSPDALSLKDRLQLSLAKLFNTSVSNVDVFTVLQNENHTLDVRFSAHGSPYYAPEKLNGIVAQNQQRLENELDLQMLMVNIDECLIEKFKCEESCTNELHKSSVPYMIYSNTTSFVGVNAFVQAQCVCEAPLMRRCLNGGSPRYGENDVCDCIDGFTGPHCELVSVAFYGSGYAFYEPIAACNNTKISLEITPQIDQGLIMYLGPLNFNPLLAISDFLALELDNGYPVLTVDYGSGAIRIRHQHIKMVADRTYQLDIILQRTSIEMTVDNCRLSTCQTLGAPIGPNEFLNVNAPLQLGGTPVDLEQLGRQLNWTHVPNQKGFFGCIRNLTINEQTYNLGMPSVFRNIDSGCQQSVAVAFSFGIDRNFIIAIIVCLALLLIILLAVVVQKKQKNGWHEKDIDDIRETIINYEDEGGGERDTDYDLNVLRTQPFYEEKLYKDPHALQGNMRDPNDIPDIADFLGDKKENCDRDVGATTVDDVRHYAYEGDGNSDGSLSSLASCTDDGDLNFDYLSNFGPRFRKLADMYGEEPSDTDSNVDDDQGWRI","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_Q24298","disprot_id":"DP00269","ncbi_taxon_id":7227,"regions_counter":12,"creator":"mnecci","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":1507,"region_id":"DP00269r001","reference_id":"11121423","start":1350,"ec_id":"ECO:0000269","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"DEcyto has two tryptophans that are near the N and C termini, the latter in a position distinct from the tryptophan in Ecyto. In a folded protein, the tryptophan indole ring is frequently buried within a hydrophobic core or is otherwise shielded from solvent, resulting in a blue shift of the fluorescence maximum relative to free tryptophan (36). The tryptophan emission maximum for β76, a thrombin-generated fragment of β-catenin (see “Experimental Procedures”), is significantly blue-shifted relative to tryptophan alone, whereas the maxima for Ecyto and DEcyto are not (Table I). Thus, the single Ecyto tryptophan and two DEcyto tryptophans appear to be solvent exposed.","type":"Results"},{"text":"The fluoresence anisotropy data suggest that the Ecyto and DEcyto domains are unfolded under native conditions.","type":"Results"},{"text":"Fluorescence, circular dichroism, and proton NMR were used to characterize the folded state of recombinant E-cadherin and DE-cadherin cytoplasmic domains (rEcyto and rDEcyto respectively).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"experimental evidence used in manual assertion","version":3,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":1507,"term_name":"disorder to order","start":1350,"ec_name":"experimental evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Fluorescence, circular dichroism, and proton NMR were used to characterize the folded state of recombinant E-cadherin and DE-cadherin cytoplasmic domains (rEcyto and rDEcyto respectively).","type":"Results"},{"text":"DEcyto has two tryptophans that are near the N and C termini, the latter in a position distinct from the tryptophan in Ecyto. In a folded protein, the tryptophan indole ring is frequently buried within a hydrophobic core or is otherwise shielded from solvent, resulting in a blue shift of the fluorescence maximum relative to free tryptophan (36). The tryptophan emission maximum for β76, a thrombin-generated fragment of β-catenin (see “Experimental Procedures”), is significantly blue-shifted relative to tryptophan alone, whereas the maxima for Ecyto and DEcyto are not (Table I). Thus, the single Ecyto tryptophan and two DEcyto tryptophans appear to be solvent exposed.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11121423","version":3,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0000269","region_id":"DP00269r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":1507,"region_id":"DP00269r005","reference_id":"11121423","start":1350,"ec_id":"ECO:0006204","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Fluorescence, circular dichroism, and proton NMR were used to characterize the folded state of recombinant E-cadherin and DE-cadherin cytoplasmic domains (rEcyto and rDEcyto respectively).","type":"Results"},{"text":"The spectra measured for rEcyto and rDEcyto at 0 °C are essentially identical and feature a single minimum in mean residue ellipticity at ∼202 nm (Fig. 1). This spectrum indicates a lack of secondary structure, which would be expected of an unstructured polypeptide.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":1507,"term_name":"disorder to order","start":1350,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Fluorescence, circular dichroism, and proton NMR were used to characterize the folded state of recombinant E-cadherin and DE-cadherin cytoplasmic domains (rEcyto and rDEcyto respectively).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11121423","version":3,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00269r007","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":1507,"term_name":"protein binding","start":1350,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"11121423","version":3,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00269r008","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1507,"region_id":"DP00269r009","reference_id":"11121423","start":1350,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"rDEcyto-β-catenin complex was also digested with subtilisin as described for rEcyto.","type":"Methods"},{"text":"However, in the presence of β-catenin, what appears to be full-length rEcyto remains at subtilisin (Fig.5) and endoproteinase Glu-C (data not shown) concentrations that completely degrade rEcyto alone (Fig. 5, lanes 5 and 7 or lanes 12 and14). Similar protection results were obtained with the DEcyto-β-catenin complex and subtilisin (data not shown).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cleavage assay evidence used in manual assertion","version":3,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q02248","partner_end":null}],"ec_ontology":"ECO","end":1507,"region_id":"DP00269r010","reference_id":"11121423","start":1350,"term_id":"GO:0005515","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"rDEcyto-β-catenin complex was also digested with subtilisin as described for rEcyto.","type":"Methods"},{"text":"However, in the presence of β-catenin, what appears to be full-length rEcyto remains at subtilisin (Fig.5) and endoproteinase Glu-C (data not shown) concentrations that completely degrade rEcyto alone (Fig. 5, lanes 5 and 7 or lanes 12 and14). Similar protection results were obtained with the DEcyto-β-catenin complex and subtilisin (data not shown).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"cleavage assay evidence used in manual assertion","version":4,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","term_name":"protein binding","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q02248","partner_end":null}],"ec_ontology":"ECO","end":1507,"region_id":"DP00269r011","reference_id":"11121423","start":1350,"term_id":"GO:0005515","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Mixtures of rEcyto or rDEcyto and various β-catenin constructs were incubated for more than 1 h at 4 °C and injected onto an Amersham Pharmacia Biotech HR 10/30 Superdex 200 size exclusion column equilibrated with 50 mm Tris-HCl, pH 8, 200 mm NaCl, 20 mm EDTA, and 1 mmDTT. ","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"chromatography evidence used in manual assertion","version":4,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","term_name":"protein binding","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1507,"region_id":"DP00269r012","reference_id":"11121423","start":1350,"term_id":"GO:0098772","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"It is proposed that binding of cadherins to beta-catenin prevents recognition of degradation signals that are exposed in the unstructured cadherin cytoplasmic domain, favoring a cell surface population of catenin-bound cadherins capable of participating in cell adhesion.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"cleavage assay evidence used in manual assertion","version":4,"reference_html":"The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. <i> Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","term_name":"molecular function regulator","ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q24298","date":"2016-09-05T15:45:44.000Z","acc":"Q24298","name":"DE-cadherin","length":1507,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI000016BB6F","genes":[{"name":{"value":"shg","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0003391","url":"http://flybase.org/reports/FBgn0003391.html"}}]},"synonyms":[{"value":"E-cadherin","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0003391","url":"http://flybase.org/reports/FBgn0003391.html"}}]}],"orfNames":[{"value":"CG3722","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0003391","url":"http://flybase.org/reports/FBgn0003391.html"}}]}]}],"alphafold_very_low_content":0.14001327140013273,"disorder_content":0.10484406104844061,"disprot_consensus":{"full":[{"start":1350,"end":1507,"type":"T"}],"Structural state":[{"start":1350,"end":1507,"type":"D"}],"Structural transition":[{"start":1350,"end":1507,"type":"T"}],"Molecular function":[{"start":1350,"end":1507,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00001","name":"7 transmembrane receptor (rhodopsin family)","start":55,"end":306},{"id":"PF10413","name":"Amino terminal of the G-protein receptor rhodopsin","start":2,"end":37}],"gene3D":[{"start":1,"end":348,"id":"1.20.1070.10","name":"Rhodopsin 7-helix transmembrane proteins"}]},"uniref50":"UniRef50_P08100","sequence":"MNGTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAYMFLLIMLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGWSRYIPEGMQCSCGIDYYTPHEETNNESFVIYMFVVHFIIPLIVIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWLPYAGVAFYIFTHQGSDFGPIFMTIPAFFAKTSAVYNPVIYIMMNKQFRNCMVTTLCCGKNPLGDDEASTTVSKTETSQVAPA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P08100","disprot_id":"DP00271","ncbi_taxon_id":9913,"regions_counter":4,"creator":"tlazar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":242,"region_id":"DP00271r001","released":"2024_06","ec_id":"ECO:0006220","reference_html":"Crystal structure of rhodopsin: A G protein-coupled receptor. <i> Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, Le Trong I, Teller DC, Okada T, Stenkamp RE, Yamamoto M, Miyano M. </i> Science, 2000","term_id":"IDPO:0000002","curator_id":"tlazar","start":226,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2023-09-28T17:00:38.559Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1F88"}],"reference_id":"10926528","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Thus, although our model demonstrates a highly flexible nature of this region and still lacks the tetrapeptide from Gln236 to Glu239, it is obvious that C-III does not fold over the helical region at all.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T14:52:12.757Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":348,"region_id":"DP00271r002","released":"2024_06","ec_id":"ECO:0006220","reference_html":"Crystal structure of rhodopsin: A G protein-coupled receptor. <i> Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, Le Trong I, Teller DC, Okada T, Stenkamp RE, Yamamoto M, Miyano M. </i> Science, 2000","term_id":"IDPO:0000002","curator_id":"tlazar","start":327,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2023-09-28T16:56:30.574Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1F88"}],"reference_id":"10926528","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The extreme COOH-terminal residues are themost exposed part of rhodopsin molecule and could be involved in vectorial transport of rhodopsin to rod outer segment.","type":"Results"},{"text":"The helical structure appears to be terminated by Gly324 and the following COOH-terminal tail changes the direction. Although current model lacks residues from 328 to 333, the positions of 327 and 334 suggest that this missing part runs covering the short H-VIII helix from the solvent region. As a whole, COOH-terminal tail of rhodopsin occupies the space over only a part of the helical bundle, H-I and H-VII.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T14:52:09.730Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":348,"region_id":"DP00271r003","released":"2024_06","ec_id":"ECO:0006220","reference_html":"Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs). <i> Teller DC, Okada T, Behnke CA, Palczewski K, Stenkamp RE. </i> Biochemistry, 2001","term_id":"IDPO:0000002","curator_id":"tlazar","start":327,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2023-09-28T16:37:19.868Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1HZX"}],"reference_id":"11425302","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"In molecule B, more residues are missing, including the C-terminus beyond residue Asn326 (Figure 2). Almost certainly, the C-terminal residues of rhodopsin are flexible and mobile in the physiological milieu, lacking a definite single conformation (58, 59).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T14:45:35.175Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":348,"region_id":"DP00271r004","released":"2024_06","ec_id":"ECO:0006220","reference_html":"Structure of bovine rhodopsin in a trigonal crystal form. <i> Li J, Edwards PC, Burghammer M, Villa C, Schertler GF. </i> J Mol Biol, 2004","term_id":"IDPO:0000002","curator_id":"tlazar","start":334,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2023-09-28T16:43:15.091Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1GZM"}],"reference_id":"15491621","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The C-terminal tail in the P31 form is located in the solvent channel and disordered, while in the P41 form it is partially resolved only in molecule A, where it is stabilised through contacts with the extracellular domain of a neighbouring molecule. Finding significant NCS differences in the same surface segments indicates an intrinsic conformational variability or flexibility of those segments, and the high B-factors of the segments support this.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T14:44:05.607Z"}}],"released":"2016_10","uniref100":"UniRef100_P02699","date":"2016-09-08T16:42:01.000Z","acc":"P02699","name":"Rhodopsin","length":348,"organism":"Bos taurus","dataset":[],"UniParc":"UPI0000049E71","genes":[{"name":{"value":"RHO"}}],"alphafold_very_low_content":0.05459770114942529,"disorder_content":0.11206896551724138,"disprot_consensus":{"full":[{"start":226,"end":242,"type":"D"},{"start":327,"end":348,"type":"D"}],"Structural state":[{"start":226,"end":242,"type":"D"},{"start":327,"end":348,"type":"D"}]}},{"features":{"pfam":[{"id":"PF05051","name":"Cytochrome C oxidase copper chaperone (COX17)","start":19,"end":65}],"gene3D":[{"start":1,"end":69,"id":"1.10.287.1130","name":"CytochromE C oxidase copper chaperone"}]},"uniref50":"UniRef50_Q12287","sequence":"MTETDKKQEQENHAECEDKPKPCCVCKPEKEERDTCILFNGQDSEKCKEFIEKYKECMKGYGFEVPSAN","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q12287","disprot_id":"DP00277","ncbi_taxon_id":559292,"regions_counter":1,"creator":"lkalmar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":27,"region_id":"DP00277r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Yeast cox17 solution structure and Copper(I) binding. <i> Abajian C, Yatsunyk LA, Ramirez BE, Rosenzweig AC. </i> J Biol Chem, 2004","term_id":"IDPO:0000002","curator_id":"lkalmar","start":1,"term_ontology":"IDPO","curator_name":"Lajos Kalmár","reference_id":"15465825","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1U96"}],"term_name":"disorder","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q12287","date":"2016-09-10T16:40:16.000Z","acc":"Q12287","name":"Cytochrome c oxidase copper chaperone","length":69,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000168392","genes":[{"name":{"value":"COX17"},"orfNames":[{"value":"L1343"}],"olnNames":[{"value":"YLL009C"}]}],"alphafold_very_low_content":0.11594202898550725,"disorder_content":0.391304347826087,"disprot_consensus":{"full":[{"start":1,"end":27,"type":"D"}],"Structural state":[{"start":1,"end":27,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00029","name":"Connexin","start":3,"end":232},{"id":"PF03508","name":"Gap junction alpha-1 protein (Cx43)","start":283,"end":361}],"gene3D":[{"start":315,"end":350,"id":"1.20.5.1130","name":"Connexin43"},{"start":2,"end":244,"id":"1.20.1440.80","name":"Gap junction channel protein cysteine-rich domain"}]},"uniref50":"UniRef50_P17302","sequence":"MGDWSALGKLLDKVQAYSTAGGKVWLSVLFIFRILLLGTAVESAWGDEQSAFRCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSVPTLLYLAHVFYVMRKEEKLNKKEEELKVAQTDGVNVEMHLKQIEIKKFKYGIEEHGKVKMRGGLLRTYIISILFKSVFEVAFLLIQWYIYGFSLSAVYTCKRDPCPHQVDCFLSRPTEKTIFIIFMLVVSLVSLALNIIELFYVFFKGVKDRVKGRSDPYHATTGPLSPSKDCGSPKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNRMGQAGSTISNSHAQPFDFPDDNQNAKKVAAGHELQPLAIVDQRPSSRASSRASSRPRPDDLEI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_P17302","disprot_id":"DP00278","ncbi_taxon_id":10116,"regions_counter":22,"creator":"zkalman","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":314,"region_id":"DP00278r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Structural changes in the carboxyl terminus of the gap junction protein connexin43 indicates signaling between binding domains for c-Src and zonula occludens-1. <i> Sorgen PL, Duffy HS, Sahoo P, Coombs W, Delmar M, Spray DC. </i> J Biol Chem, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":255,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15492000","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-01-23T14:02:28.460Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1R5S"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The overall structure of the Cx43CT was mainly random coiled; however, two regions of helical structure were present (Fig. 1, A and B). These helical regions were superimposed on the basis of backbone coordinates from Ala-315–Thr-326 and Asp-340–Ala-348 (Fig. 1C). The total root mean square deviations for these alignments were 0.27 and 0.34 Å, respectively. Structural statistics are presented in Table I. The predominately random coil structure for the Cx43CT is consistent with the narrow chemical shift dispersions in the 15N HSQC (Fig. 1D).","type":"Results"}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":372,"term_name":"SH3 domain binding","start":264,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"15492000","version":4,"reference_html":"Structural changes in the carboxyl terminus of the gap junction protein connexin43 indicates signaling between binding domains for c-Src and zonula occludens-1. <i> Sorgen PL, Duffy HS, Sahoo P, Coombs W, Delmar M, Spray DC. </i> J Biol Chem, 2004","date":"2023-01-23T14:39:35.252Z","term_id":"GO:0017124","ec_id":"ECO:0006165","region_id":"DP00278r007","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins.\" [GOC:go_curators, Pfam:PF00018]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P00523","operator":null,"partner_start":81,"partner_end":147}],"statement":[{"text":"The addition of the SH3 domain affected the resonance peaks of amino acids Lys-264–Lys-287, Ser-306–Glu-316, His-331–Phe-337, Leu-356–Val-359, and Ala-367–Ser-372 (Fig. 3). Only the region Lys-264–Lys-287 contains the amino acids previously reported to act as an SH3 binding domain (43, 44, 45).","type":"Results"},{"text":"The peptide competition experiments indicated that the Cx43CT-SH3 complex was inhibited by peptides 271–287, 312–336, and 346–360 (Fig. 3B and Supplemental Data 2), as indicated by the re-emergence of all resonance peaks affected in Fig. 3A.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":382,"region_id":"DP00278r008","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Structural changes in the carboxyl terminus of the gap junction protein connexin43 indicates signaling between binding domains for c-Src and zonula occludens-1. <i> Sorgen PL, Duffy HS, Sahoo P, Coombs W, Delmar M, Spray DC. </i> J Biol Chem, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":327,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15492000","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-01-23T14:04:44.254Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1R5S"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The overall structure of the Cx43CT was mainly random coiled; however, two regions of helical structure were present (Fig. 1, A and B). These helical regions were superimposed on the basis of backbone coordinates from Ala-315–Thr-326 and Asp-340–Ala-348 (Fig. 1C). The total root mean square deviations for these alignments were 0.27 and 0.34 Å, respectively. Structural statistics are presented in Table I. The predominately random coil structure for the Cx43CT is consistent with the narrow chemical shift dispersions in the 15N HSQC (Fig. 1D).","type":"Results"},{"text":"The helical region Asp-340–Ala-348 is too short to be considered as structured.","type":"Curator statement"}]},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":382,"term_name":"flexible C-terminal tail","start":327,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15492000","version":4,"reference_html":"Structural changes in the carboxyl terminus of the gap junction protein connexin43 indicates signaling between binding domains for c-Src and zonula occludens-1. <i> Sorgen PL, Duffy HS, Sahoo P, Coombs W, Delmar M, Spray DC. </i> J Biol Chem, 2004","date":"2023-01-23T14:48:20.426Z","term_id":"IDPO:0000031","ec_id":"ECO:0006165","region_id":"DP00278r018","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Disorder function","cross_refs":[{"db":"PDB","id":"1R5S"}],"statement":[{"text":"The overall structure of the Cx43CT was mainly random coiled; however, two regions of helical structure were present (Fig. 1, A and B). These helical regions were superimposed on the basis of backbone coordinates from Ala-315–Thr-326 and Asp-340–Ala-348 (Fig. 1C). The total root mean square deviations for these alignments were 0.27 and 0.34 Å, respectively. Structural statistics are presented in Table I. The predominately random coil structure for the Cx43CT is consistent with the narrow chemical shift dispersions in the 15N HSQC (Fig. 1D).","type":"Results"},{"text":"The helical region Asp-340–Ala-348 is too short to be considered as structured.","type":"Curator statement"}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":382,"term_name":"protein binding","start":364,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"15492000","version":4,"reference_html":"Structural changes in the carboxyl terminus of the gap junction protein connexin43 indicates signaling between binding domains for c-Src and zonula occludens-1. <i> Sorgen PL, Duffy HS, Sahoo P, Coombs W, Delmar M, Spray DC. </i> J Biol Chem, 2004","date":"2023-01-23T14:18:32.779Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00278r021","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"A0A0G2K2P5","operator":"and","partner_start":160,"partner_end":290}],"statement":[{"text":"The addition of the PDZ-2 domain affected the resonance peaks of the last 19 amino acids of the Cx43CT, a region larger than what was expected from the putative “PDZ binding domain” of Cx43 (the final 4 amino acids in the carboxyl terminus (42)). Indeed, as seen in Fig. 2A, the signal from residues Ser-372–Ile-382 completely disappeared (i.e. broadened beyond detection), whereas the amplitude of the peaks corresponding to residues Ser-364–Ala-371 decreased in intensity. These changes can be explained by decreased tumbling rates caused by an increase in molecular weight and/or intermediate chemical exchange rates, both indicative of a structural modification caused by the association of the two molecules.","type":"Results"}]},{"start":255,"end":382,"reference_id":"19808665","reference_source":"pmid","reference_html":"Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains. <i> Bouvier D, Spagnol G, Chenavas S, Kieken F, Vitrac H, Brownell S, Kellezi A, Forge V, Sorgen PL. </i> J Biol Chem, 2009","date":"2023-01-20T16:12:34.244Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00278r022","statement":[{"text":"As expected from the NMR data, Cx40CT and Cx43CT at pH 6.0 present a high proportion of random-coiled structure (major absorption at 200 nm for Cx40CT and 201 nm for Cx43CT) (Fig. 3A).","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P08050","date":"2016-08-12T11:14:29.000Z","acc":"P08050","name":"Gap junction alpha-1 protein","length":382,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI0000163C2B","genes":[{"name":{"value":"Gja1"},"synonyms":[{"value":"Cxn-43"}]}],"alphafold_very_low_content":0.306282722513089,"disorder_content":0.33507853403141363,"disprot_consensus":{"full":[{"start":255,"end":382,"type":"D"}],"Structural state":[{"start":255,"end":382,"type":"D"}],"Molecular function":[{"start":264,"end":382,"type":"F"}],"Disorder function":[{"start":327,"end":382,"type":"F"}]}},{"features":{"pfam":[{"id":"PF06554","name":"Olfactory marker protein","start":11,"end":151}],"gene3D":[{"start":2,"end":163,"id":"2.60.120.390","name":"Olfactory marker"}]},"uniref50":"UniRef50_Q64288","sequence":"MAEDGPQKQQLDMPLVLDQDLTKQMRLRVESLKQRGEKKQDGEKLLRPAESVYRLDFIQQQKLQFDHWNVVLDKPGKVTITGTSQNWTPDLTNLMTRQLLDPAAIFWRKEDSDAMDWNEADALEFGERLSDLAKIRKVMYFLITFGEGVEPANLKASVVFNQL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_Q64288","disprot_id":"DP00279","ncbi_taxon_id":10116,"regions_counter":9,"creator":"eleonardi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":49,"region_id":"DP00279r001","released":"2026_06","ec_id":"ECO:0006165","reference_html":"Backbone dynamics of the olfactory marker protein as studied by 15N NMR relaxation measurements. <i> Gitti RK, Wright NT, Margolis JW, Varney KM, Weber DJ, Margolis FL. </i> Biochemistry, 2005","term_id":"IDPO:0000002","curator_id":"maspromonte","start":35,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2024-09-13T13:21:21.623Z","reference_source":"pmid","term_name":"disorder","reference_id":"16008352","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The disorder of the loop regions of OMP (loop 1, R35−A49; loop 2, F57−W68; and Ω loop 3, S84−L99) is reflected in the observed low NOE values, which are characteristic for fast frequency component contributions to the relaxation of these residues. Additionally, several residues in all three loops have fast R2 relaxation rates or are missing altogether, including residues in loop 1 (E43−A49), the majority of residues in the Ω loop (loop 3; residues 84−99), and three residues in the β-hairpin loop (loop 4; residues F145, G146, E150). ","type":"Results"},{"text":"As found for helix 1, residues in loop 1 (R35, K39, L44, L45, L46, R47) and loop 3 (S84, N86, T87, D90, L94, T96, L99) were confirmed to have exchange contributions to T2 relaxation in a plot of 1DNH versus T1/T2 ratio (Figure 3). Both loop 1 and Ω loop 3 are considerably long, allowing for a large degree of conformational flexibility for these regions of the protein. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-13T14:27:02.432Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":68,"region_id":"DP00279r004","released":"2026_06","ec_id":"ECO:0006165","reference_html":"Backbone dynamics of the olfactory marker protein as studied by 15N NMR relaxation measurements. <i> Gitti RK, Wright NT, Margolis JW, Varney KM, Weber DJ, Margolis FL. </i> Biochemistry, 2005","term_id":"IDPO:0000002","curator_id":"maspromonte","start":57,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2024-09-13T13:19:47.361Z","reference_source":"pmid","term_name":"disorder","reference_id":"16008352","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The disorder of the loop regions of OMP (loop 1, R35−A49; loop 2, F57−W68; and Ω loop 3, S84−L99) is reflected in the observed low NOE values, which are characteristic for fast frequency component contributions to the relaxation of these residues. Additionally, several residues in all three loops have fast R2 relaxation rates or are missing altogether, including residues in loop 1 (E43−A49), the majority of residues in the Ω loop (loop 3; residues 84−99), and three residues in the β-hairpin loop (loop 4; residues F145, G146, E150). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-13T14:29:13.848Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":99,"region_id":"DP00279r007","released":"2026_06","ec_id":"ECO:0006165","reference_html":"Backbone dynamics of the olfactory marker protein as studied by 15N NMR relaxation measurements. <i> Gitti RK, Wright NT, Margolis JW, Varney KM, Weber DJ, Margolis FL. </i> Biochemistry, 2005","term_id":"IDPO:0000002","curator_id":"maspromonte","start":84,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2024-09-13T13:21:51.552Z","reference_source":"pmid","term_name":"disorder","reference_id":"16008352","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The disorder of the loop regions of OMP (loop 1, R35−A49; loop 2, F57−W68; and Ω loop 3, S84−L99) is reflected in the observed low NOE values, which are characteristic for fast frequency component contributions to the relaxation of these residues. Additionally, several residues in all three loops have fast R2 relaxation rates or are missing altogether, including residues in loop 1 (E43−A49), the majority of residues in the Ω loop (loop 3; residues 84−99), and three residues in the β-hairpin loop (loop 4; residues F145, G146, E150). ","type":"Results"},{"text":"As found for helix 1, residues in loop 1 (R35, K39, L44, L45, L46, R47) and loop 3 (S84, N86, T87, D90, L94, T96, L99) were confirmed to have exchange contributions to T2 relaxation in a plot of 1DNH versus T1/T2 ratio (Figure 3). Both loop 1 and Ω loop 3 are considerably long, allowing for a large degree of conformational flexibility for these regions of the protein. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-13T14:25:40.013Z"}}],"released":"2016_10","uniref100":"UniRef100_P08523","date":"2016-09-10T17:26:07.000Z","acc":"P08523","name":"Olfactory marker protein","length":163,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI0000130D28","genes":[{"name":{"value":"Omp"}}],"alphafold_very_low_content":0.024539877300613498,"disorder_content":0.26380368098159507,"disprot_consensus":{"full":[{"start":35,"end":49,"type":"D"},{"start":57,"end":68,"type":"D"},{"start":84,"end":99,"type":"D"}],"Structural state":[{"start":35,"end":49,"type":"D"},{"start":57,"end":68,"type":"D"},{"start":84,"end":99,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00122","name":"P-type ATPase actuator domain","start":833,"end":921},{"id":"PF00403","name":"Heavy-metal-associated domain","start":11,"end":72},{"id":"PF00403","name":"Heavy-metal-associated domain","start":175,"end":234},{"id":"PF00403","name":"Heavy-metal-associated domain","start":280,"end":337},{"id":"PF00403","name":"Heavy-metal-associated domain","start":380,"end":441},{"id":"PF00403","name":"Heavy-metal-associated domain","start":493,"end":551},{"id":"PF00403","name":"Heavy-metal-associated domain","start":570,"end":628},{"id":"PF00702","name":"haloacid dehalogenase-like hydrolase","start":1038,"end":1312}],"gene3D":[{"start":1052,"end":1229,"id":"3.40.1110.10","name":"Calcium-transporting ATPase, cytoplasmic domain N"},{"start":1,"end":79,"id":"3.30.70.100","name":"3.30.70.100"},{"start":376,"end":450,"id":"3.30.70.100","name":"3.30.70.100"},{"start":163,"end":246,"id":"3.30.70.100","name":"3.30.70.100"},{"start":275,"end":361,"id":"3.30.70.100","name":"3.30.70.100"},{"start":486,"end":561,"id":"3.30.70.100","name":"3.30.70.100"},{"start":562,"end":635,"id":"3.30.70.100","name":"3.30.70.100"}]},"uniref50":"UniRef50_Q04656","sequence":"MDPSMGVNSVTISVEGMTCNSCVWTIEQQIGKVNGVHHIKVSLEEKNATIIYDPKLQTPKTLQEAIDDMGFDAVIHNPDPLPVLTDTLFLTVTASLTLPWDHIQSTLLKTKGVTDIKIYPQKRTVAVTIIPSIVNANQIKELVPELSLDTGTLEKKSGACEDHSMAQAGEVVLKMKVEGMTCHSCTSTIEGKIGKLQGVQRIKVSLDNQEATIVYQPHLISVEEMKKQIEAMGFPAFVKKQPKYLKLGAIDVERLKNTPVKSSEGSQQRSPSYTNDSTATFIIDGMHCKSCVSNIESTLSALQYVSSIVVSLENRSAIVKYNASSVTPESLRKAIEAVSPGLYRVSITSEVESTSNSPSSSSLQKIPLNVVSQPLTQETVINIDGMTCNSCVQSIEGVISKKPGVKSIRVSLANSNGTVEYDPLLTSPETLRGAIEDMGFDATLSDTNEPLVVIAQPSSEMPLLTSTNEFYTKGMTPVQDKEEGKNSSKCYIQVTGMTCASCVANIERNLRREEGIYSILVALMAGKAEVRYNPAVIQPPMIAEFIRELGFGATVIENADEGDGVLELVVRGMTCASCVHKIESSLTKHRGILYCSVALATNKAHIKYDPEIIGPRDIIHTIESLGFEASLVKKDRSASHLDHKREIRQWRRSFLVSLFFCIPVMGLMIYMMVMDHHFATLHHNQNMSKEEMINLHSSMFLERQILPGLSVMNLLSFLLCVPVQFFGGWYFYIQAYKALKHKTANMDVLIVLATTIAFAYSLIILLVAMYERAKVNPITFFDTPPMLFVFIALGRWLEHIAKGKTSEALAKLISLQATEATIVTLDSDNILLSEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPGSTVIAGSINQNGSLLICATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFIVFVSIATLLVWIVIGFLNFEIVETYFPGYNRSISRTETIIRFAFQASITVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVVVFDKTGTITHGTPVVNQVKVLTESNRISHHKILAIVGTAESNSEHPLGTAITKYCKQELDTETLGTCIDFQVVPGCGISCKVTNIEGLLHKNNWNIEDNNIKNASLVQIDASNEQSSTSSSMIIDAQISNALNAQQYKVLIGNREWMIRNGLVINNDVNDFMTEHERKGRTAVLVAVDDELCGLIAIADTVKPEAELAIHILKSMGLEVVLMTGDNSKTARSIASQVGITKVFAEVLPSHKVAKVKQLQEEGKRVAMVGDGINDSPALAMANVGIAIGTGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFVFALIYNLVGIPIAAGVFMPIGLVLQPWMGSAAMAASSVSVVLSSLFLKLYRKPTYESYELPARSQIGQKSPSEISVHVGIDDTSRNSPKLGLLDRIVNYSRASINSLLSDKRSLNSVVTSEPDKHSLLVGDFREDDDTAL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q04656","disprot_id":"DP00282","ncbi_taxon_id":9606,"regions_counter":1,"creator":"nveljkovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1176,"region_id":"DP00282r001","released":"2022_12","ec_id":"ECO:0006165","reference_html":"The binding mode of ATP revealed by the solution structure of the N-domain of human ATP7A. <i> Banci L, Bertini I, Cantini F, Inagaki S, Migliardi M, Rosato A. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"maspromonte","start":1125,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-10-14T12:55:32.053Z","reference_source":"pmid","term_name":"disorder","reference_id":"19917612","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15422","statements":[{"type":"Abstract","text":"We report the solution NMR structures of the N-domain of the Menkes protein (ATP7A) in the ATP-free and ATP-bound\nforms."}],"entry_name":"ATP"}],"statement":[{"text":"The region 1125–1176, which constitutes a long loop between strands\nβ3 and β4, is disordered in both structures consistently with the lack of long range NOEs involving these residues and with its afore mentioned dynamics.","type":"Results"},{"text":"A protein loop of 50 amino acids located between β3 and β4 is disordered\nand mobile on the subnanosecond time scale. ","type":"Abstract"},{"text":"The unstructured loop was omitted for simplicity. Bottom panel, the backbone traces for the twenty lowest energy conformers are superimposed.","type":"Figure"},{"text":"Notably, the CopA N-domain lacks the long unstructured loop involving\nresidues 1125–1176 of N-MNK.","type":"Discussion"}],"cross_refs":[{"db":"BMRB","id":"16441"},{"db":"PDB","id":"2KMX"},{"db":"PDB","id":"2KMV"},{"db":"BMRB","id":"16440"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-14T13:50:42.073Z"}}],"released":"2016_10","uniref100":"UniRef100_Q04656","date":"2016-09-07T10:46:13.000Z","acc":"Q04656","name":"Copper-transporting ATPase 1","length":1500,"organism":"Homo sapiens","dataset":["NDDs-related proteins","Age-related disorders proteins"],"UniParc":"UPI0000161BB8","genes":[{"name":{"value":"ATP7A","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"28389643","url":"http://www.ncbi.nlm.nih.gov/pubmed/28389643","alternativeUrl":"https://europepmc.org/abstract/MED/28389643"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:869","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:869"}}]},"synonyms":[{"value":"MC1"},{"value":"MNK"}]}],"alphafold_very_low_content":0.15933333333333333,"disorder_content":0.034666666666666665,"disprot_consensus":{"full":[{"start":1125,"end":1176,"type":"D"}],"Structural state":[{"start":1125,"end":1176,"type":"D"}]}},{"acc":"P16009","sequence":"MEMISNNLNWFVGVVEDRMDPLKLGRVRVRVVGLHPPQRAQGDVMGIPTEKLPWMSVIQPITSAAMSGIGGSVTGPVEGTRVYGHFLDKWKTNGIVLGTYGGIVREKPNRLEGFSDPTGQYPRRLGNDTNVLNQGGEVGYDSSSNVIQDSNLDTAINPDDRPLSEIPTDDNPNMSMAEMLRRDEGLRLKVYWDTEGYPTIGIGHLIMKQPVRDMAQINKVLSKQVGREITGNPGSITMEEATTLFERDLADMQRDIKSHSKVGPVWQAVNRSRQMALENMAFQMGVGGVAKFNTMLTAMLAGDWEKAYKAGRDSLWYQQTKGRASRVTMIILTGNLESYGVEVKTPARSLSAMAATVAKSSDPADPPIPNDSRILFKEPVSSYKGEYPYVHTMETESGHIQEFDDTPGQERYRLVHPTGTYEEVSPSGRRTRKTVDNLYDITNADGNFLVAGDKKTNVGGSEIYYNMDNRLHQIDGSNTIFVRGDETKTVEGNGTILVKGNVTIIVEGNADITVKGDATTLVEGNQTNTVNGNLSWKVAGTVDWDVGGDWTEKMASMSSISSGQYTIDGSRIDIG","creator":"gbalatti","dataset":["Viral proteins"],"date":"2016-09-18T09:03:40.000Z","disprot_id":"DP00284","features":{"pfam":[{"id":"PF00959","name":"Phage lysozyme","start":183,"end":310},{"id":"PF06714","name":"Gp5 N-terminal OB domain","start":33,"end":173},{"id":"PF06715","name":"Gp5 C-terminal repeat (3 copies)","start":484,"end":506},{"id":"PF06715","name":"Gp5 C-terminal repeat (3 copies)","start":508,"end":531},{"id":"PF06715","name":"Gp5 C-terminal repeat (3 copies)","start":532,"end":554}],"gene3D":[{"start":177,"end":340,"id":"1.10.530.40","name":"1.10.530.40","_id":"685af523b4ac24d5329d7c31"},{"start":129,"end":176,"id":"3.10.450.190","name":"3.10.450.190","_id":"685af523b4ac24d5329d7c32"},{"start":1,"end":128,"id":"2.40.50.260","name":"Nucleic acid-binding protein domain","_id":"685af523b4ac24d5329d7c33"},{"start":341,"end":437,"id":"3.10.450.190","name":"3.10.450.190","_id":"685af523b4ac24d5329d7c34"}]},"genes":[{"name":{"value":"5","evidences":[{"source":{"id":"MF_04151","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04151","_id":"685af523b4ac24d5329d7c67"},"code":"ECO:0000255","_id":"685af523b4ac24d5329d7c66"}],"_id":"685af523b4ac24d5329d7c68"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d7c65"}],"length":575,"name":"Baseplate central spike complex protein gp5","ncbi_taxon_id":10665,"organism":"Enterobacteria phage T4","regions_counter":12,"released":"2016_10","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Uroviricota","Caudoviricetes","Caudovirales","Myoviridae","Tevenvirinae","Tequatrovirus"],"UniParc":"UPI000005CB7F","uniref100":"UniRef100_P16009","uniref50":"UniRef50_P16009","uniref90":"UniRef90_P16009","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5IV5","_id":"685af523b4ac24d5329d7c4f"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006224","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":346,"end":361,"interaction_partner":[],"reference_html":"Structure of the T4 baseplate and its function in triggering sheath contraction. <i> Taylor NM, Prokhorov NS, Guerrero-Ferreira RC, Shneider MM, Browning C, Goldie KN, Stahlberg H, Leiman PG. </i> Nature, 2016","reference_id":"27193680","region_id":"DP00284r007","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"Missing residues reported at positions 346-361","_id":"685af523b4ac24d5329d7c50"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-11T14:32:25.161Z","_id":"685af523b4ac24d5329d7c51"},"version":1,"_id":"685af523b4ac24d5329d7c4e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1PDL","_id":"685af523b4ac24d5329d7c53"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006224","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":346,"end":361,"interaction_partner":[],"reference_html":"Three-dimensional structure of bacteriophage T4 baseplate. <i> Kostyuchenko VA, Leiman PG, Chipman PR, Kanamaru S, van Raaij MJ, Arisaka F, Mesyanzhinov VV, Rossmann MG. </i> Nat Struct Biol, 2003","reference_id":"12923574","region_id":"DP00284r008","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"Missing residues reported at positions 346-361","_id":"685af523b4ac24d5329d7c54"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-11T14:32:28.569Z","_id":"685af523b4ac24d5329d7c55"},"version":1,"_id":"685af523b4ac24d5329d7c52","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1K28","_id":"685af523b4ac24d5329d7c57"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006226","ec_name":"cryogenic electron microscopy-based structural model with high relative B-factor values used in manual assertion","ec_ontology":"ECO","start":346,"end":361,"interaction_partner":[],"reference_html":"Structure of the cell-puncturing device of bacteriophage T4. <i> Kanamaru S, Leiman PG, Kostyuchenko VA, Chipman PR, Mesyanzhinov VV, Arisaka F, Rossmann MG. </i> Nature, 2002","reference_id":"11823865","region_id":"DP00284r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Seven residues upstream and nine residues downstream of the cleavage site are\ndisordered in the crystal structure.","_id":"685af523b4ac24d5329d7c58"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-29T11:40:28.663Z","_id":"685af523b4ac24d5329d7c59"},"version":1,"_id":"685af523b4ac24d5329d7c56","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1K28","_id":"685af523b4ac24d5329d7c5b"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006208","ec_name":"cryogenic electron microscopy evidence used in manual assertion","ec_ontology":"ECO","start":346,"end":361,"interaction_partner":[],"reference_html":"Structure of the cell-puncturing device of bacteriophage T4. <i> Kanamaru S, Leiman PG, Kostyuchenko VA, Chipman PR, Mesyanzhinov VV, Arisaka F, Rossmann MG. </i> Nature, 2002","reference_id":"11823865","region_id":"DP00284r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The gp5 lysozyme domain, located on the periphery of the central\nb-helix, is connected to the N-terminal domain by linker 1 and to\nthe C-terminal b-helical domain by linker 2, which contains the\ncleavage site between gp5* and gp5C (Fig. 1a). Seven residues\nupstream and nine residues downstream of the cleavage site are\ndisordered in the crystal structure.","_id":"685af523b4ac24d5329d7c5c"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-29T11:40:45.297Z","_id":"685af523b4ac24d5329d7c5d"},"version":1,"_id":"685af523b4ac24d5329d7c5a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1K28","_id":"685af523b4ac24d5329d7c5f"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006208","ec_name":"cryogenic electron microscopy evidence used in manual assertion","ec_ontology":"ECO","start":350,"end":354,"interaction_partner":[],"reference_html":"Structure of the cell-puncturing device of bacteriophage T4. <i> Kanamaru S, Leiman PG, Kostyuchenko VA, Chipman PR, Mesyanzhinov VV, Arisaka F, Rossmann MG. </i> Nature, 2002","reference_id":"11823865","region_id":"DP00284r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The gp5 lysozyme domain, located on the periphery of the central\nb-helix, is connected to the N-terminal domain by linker 1 and to\nthe C-terminal b-helical domain by linker 2, which contains the\ncleavage site between gp5* and gp5C (Fig. 1a). Seven residues\nupstream and nine residues downstream of the cleavage site are\ndisordered in the crystal structure.","_id":"685af523b4ac24d5329d7c60"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000048","term_name":"limited proteolysis display site","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-29T11:40:42.014Z","_id":"685af523b4ac24d5329d7c61"},"version":1,"_id":"685af523b4ac24d5329d7c5e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":346,"end":361,"interaction_partner":[],"reference_html":"The C-terminal fragment of the precursor tail lysozyme of bacteriophage T4 stays as a structural component of the baseplate after cleavage. <i> Kanamaru S, Gassner NC, Ye N, Takeda S, Arisaka F. </i> J Bacteriol, 1999","reference_id":"10217762","region_id":"DP00284r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The N-terminal sequences of these three bands as determined by Edman degradation were MEMISNN-, MEMISNN-, and AMAATVA-, respectively, indicating that the last two bands were the cleavage products of the first and that the two fragments were held together after cleavage","_id":"685af523b4ac24d5329d7c63"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000048","term_name":"limited proteolysis display site","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-29T11:40:38.484Z","_id":"685af523b4ac24d5329d7c64"},"version":1,"_id":"685af523b4ac24d5329d7c62","reference_source":"pmid"}],"__v":0,"disorder_content":0.02782608695652174,"disprot_consensus":{"full":[{"start":346,"end":361,"type":"D"}],"Structural state":[{"start":346,"end":361,"type":"D"}],"Disorder function":[{"start":346,"end":361,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03157","name":"High molecular weight glutenin subunit","start":1,"end":601}]},"uniref50":"UniRef50_P10388","sequence":"MAKRLVLFVAVVVALVALTVAEGEASEQLQCERELQELQERELKACQQVMDQQLRDISPECHPVVVSPVAGQYEQQIVVPPKGGSFYPGETTPPQQLQQRIFWGIPALLKRYYPSVTCPQQVSYYPGQASPQRPGQGQQPGQGQQGYYPTSPQQPGQWQQPEQGQPRYYPTSPQQSGQLQQPAQGQQPGQGQQGQQPGQGQPGYYPTSSQLQPGQLQQPAQGQQGQQPGQAQQGQQPGQGQQPGQGQQGQQPGQGQQPGQGQQGQQLGQGQQGYYPTSLQQSGQGQPGYYPTSLQQLGQGQSGYYPTSPQQPGQGQQPGQLQQPAQGQQPGQGQQGQQPGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYPTSSQQPTQSQQPGQGQQGQQVGQGQQAQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYLTSPQQSGQGQQPGQLQQSAQGQKGQQPGQGQQPGQGQQGQQPGQGQQGQQPGQGQPGYYPTSPQQSGQGQQPGQWQQPGQGQPGYYPTSPLQPGQGQPGYDPTSPQQPGQGQQPGQLQQPAQGQQGQQLAQGQQGQQPAQVQQGQRPAQGQQGQQPGQGQQGQQLGQGQQGQQPGQGQQGQQPAQGQQGQQPGQGQQGQQPGQGQQGQQPGQGQQPGQGQPWYYPTSPQESGQGQQPGQWQQPGQGQPGYYLTSPLQLGQGQQGYYPTSLQQPGQGQQPGQWQQSGQGQHWYYPTSPQLSGQGQRPGQWLQPGQGQQGYYPTSPQQPGQGQQLGQWLQPGQGQQGYYPTSLQQTGQGQQSGQGQQGYYSSYHVSVEHQAASLKVAKAQQLAAQLPAMCRLEGGDALSASQ","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","BOP clade","Pooideae","Triticodae","Triticeae","Triticinae","Triticum"],"uniref90":"UniRef90_P10388","disprot_id":"DP00285","ncbi_taxon_id":4565,"regions_counter":2,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":461,"region_id":"DP00285r001","released":"2023_12","ec_id":"ECO:0006299","reference_html":"New insight into the solution structures of wheat gluten proteins from Raman optical activity. <i> Blanch EW, Kasarda DD, Hecht L, Nielsen K, Barron LD. </i> Biochemistry, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":168,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12741823","version":3,"ec_name":"Raman spectroscopy evidence used in manual assertion","date":"2023-08-22T15:07:37.096Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gln386_Gly420del","start":null,"end":null,"position":null}],"sequence_construct":"YYPTSPQQPGQLQQPAQGQQPGQGQQGQQPGQGQPGYYPTSSQLQPGQLQQPAQGQQGQQPGQAQQGQQPGQGQQPGQGQQGQQPGQGQQPGQGQQGQQLGQGQQGYYPTSLQQSGQGQPGYYPTSLQQLGQGQSGYYPTSPQQPGQGQQPGQLQQPAQGQQPGQGQQGQQPGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYPTSSQQPTQYY PTSPQQSGQGQPGYY LTSPQQSGQGQQPGQLQQSAQGQK","statement":[{"text":"Similar ROA bands have been reported for a number of proteins with irregular, natively unfolded, and non-native folds (26−28, 53)     and have also been assigned to residues with the PPII-helical conformation in loop regions of a viral coat protein ( 54).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":461,"region_id":"DP00285r002","released":"2023_12","ec_id":"ECO:0007064","reference_html":"New insight into the solution structures of wheat gluten proteins from Raman optical activity. <i> Blanch EW, Kasarda DD, Hecht L, Nielsen K, Barron LD. </i> Biochemistry, 2003","term_id":"IDPO:0000004","curator_id":"vnugnes","start":168,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12741823","version":3,"ec_name":"dynamic light scattering assay evidence used in manual assertion","date":"2023-08-22T15:12:04.934Z","reference_source":"pmid","term_name":"pre-molten globule","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gln386_Gly420del","start":null,"end":null,"position":null}],"sequence_construct":"YYPTSPQQPGQLQQPAQGQQPGQGQQGQQPGQGQPGYYPTSSQLQPGQLQQPAQGQQGQQPGQAQQGQQPGQGQQPGQGQQGQQPGQGQQPGQGQQGQQLGQGQQGYYPTSLQQSGQGQPGYYPTSLQQLGQGQSGYYPTSPQQPGQGQQPGQLQQPAQGQQPGQGQQGQQPGQGQQGQQPGQGQQPGQGQPGYYPTSPQQSGQGQPGYYPTSSQQPTQYYPTSPQQSGQGQPGYYLTSPQQSGQGQQPGQLQQSAQGQK","statement":[{"text":"The ROA spectrum of the T-A-1 peptide indicates the presence of a large amount of PPII helix, which, although it might be expected to promote an extended structure, is apparently imperfect to some degree, as indicated by a hydrodynamic radius of 4.0 nm as measured by dynamic light scattering under the same conditions of pH and temperature as for the ROA spectra. This corresponds to the hydrodynamic radius expected for a natively unfolded premolten-globular protein of the same molecular weight ( 44).","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P10388","date":"2016-09-18T20:55:10.000Z","acc":"P10388","name":"Glutenin, high molecular weight subunit DX5","length":848,"organism":"Triticum aestivum","dataset":[],"UniParc":"UPI000012B803","genes":[{"name":{"value":"GLU-1D-1D"},"synonyms":[{"value":"GLU-D1-1B"}]}],"alphafold_very_low_content":0.8985849056603774,"disorder_content":0.3466981132075472,"disprot_consensus":{"full":[{"start":168,"end":461,"type":"D"}],"Structural state":[{"start":168,"end":461,"type":"D"}]}},{"features":{"pfam":[{"id":"PF16544","name":"Homodimerisation region of STAR domain protein","start":10,"end":62},{"id":"PF16551","name":"Putative nuclear localisation signal of quaking","start":312,"end":341},{"id":"PF22675","name":"KHDC4/BBP-like, KH-domain type I","start":93,"end":180}],"gene3D":[{"start":6,"end":215,"id":"3.30.1370.10","name":"K Homology domain, type 1"}]},"uniref50":"UniRef50_Q32NN2","sequence":"MVGEMETKEKPKPTPDYLMQLMNDKKLMSSLPNFCGIFTHLERLLDEEISRVRKDMYNDTMNSSSNEKRTSELPDGIGPIVQLQEKLYVPVKEYPDFNFVGRILGPRGLTAKQLEAETGCKIMVRGKGSMRDKKKEEQNRGKPNWEHLNEDLHVLITVEDAQNRAELKLKRAVEEVKKLLVPAAEGEDSLKKMQLMELAILNGTYRDANLKSPALAFSLAATGQAPRIITGPAPVLSPAALRTPTPAGHTLMPLIRQIQTAVMPNGTPHPTATLMQQAPEGGLIYTPYEYPYTLAPATSILEYPIEASGVLGAVATKVRRHDMRVHPYQRIVTADRAATGN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Amphibia","Batrachia","Anura","Pipoidea","Pipidae","Xenopodinae","Xenopus","Xenopus"],"uniref90":"UniRef90_Q32NN2","disprot_id":"DP00286","ncbi_taxon_id":8355,"regions_counter":3,"creator":"agasparini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":215,"region_id":"DP00286r003","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Solution structure and backbone dynamics of the KH-QUA2 region of the Xenopus STAR/GSG quaking protein. <i> Maguire ML, Guler-Gane G, Nietlispach D, Raine AR, Zorn AM, Standart N, Broadhurst RW. </i> J Mol Biol, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":203,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15811367","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-08-17T20:23:00.305Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2BL5"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"By contrast, the relaxation parameters for the C-terminal QUA2 region indicate substantial backbone flexibility. In particular, the decreased 15N R2 values and the large negative NOEs observed for residues 183–188 and 202–214 (Figure 3) are characteristic of extensive local motion on the sub-nanosecond timescale.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_Q32NN2","date":"2016-09-09T16:24:11.000Z","acc":"Q32NN2","name":"Protein quaking-A","length":341,"organism":"Xenopus laevis","dataset":["RNA-binding proteins"],"UniParc":"UPI00005DC648","genes":[{"name":{"value":"qki-a"}}],"alphafold_very_low_content":0.3548387096774194,"disorder_content":0.03812316715542522,"disprot_consensus":{"full":[{"start":203,"end":215,"type":"D"}],"Structural state":[{"start":203,"end":215,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01847","name":"VHL beta domain","start":63,"end":144},{"id":"PF17211","name":"VHL box domain","start":156,"end":204}],"gene3D":[{"start":153,"end":204,"id":"1.10.750.10","name":"von Hippel-Lindau disease tumour suppressor, alpha domain"},{"start":51,"end":152,"id":"2.60.40.780","name":"von Hippel-Lindau disease tumour suppressor,  beta domain"}]},"uniref50":"UniRef50_P40337","sequence":"MPRRAENWDEAEVGAEEAGVEEYGPEEDGGEESGAEESGPEESGPEELGAEEEMEAGRPRPVLRSVNSREPSQVIFCNRSPRVVLPVWLNFDGEPQPYPTLPPGTGRRIHSYRGHLWLFRDAGTHDGLLVNQTELFVPSLNVDGQPIFANITLPVYTLKERCLQVVRSLVKPENYRRLDIVRSLYEDLEDHPNVQKDLERLTQERIAHQRMGD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P40337","disprot_id":"DP00287","ncbi_taxon_id":9606,"regions_counter":69,"creator":"vntester","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":59,"region_id":"DP00287r004","reference_id":"25661653","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"VHL residues 1–59 are disordered and not observed in the structure.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Insights into Cullin-RING E3 ubiquitin ligase recruitment: structure of the VHL-EloBC-Cul2 complex. <i> Nguyen HC, Yang H, Fribourgh JL, Wolfe LS, Xiong Y. </i> Structure, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4WQO"}],"term_name":"disorder","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-05-17T14:13:30.596Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":213,"region_id":"DP00287r005","start":54,"term_id":"IDPO:0000003","statement":[{"text":"Yet, the near-UV CD experiments show an absence of a tertiary structure.","type":"Abstract"},{"text":"We therefore conclude that, under native conditions, the non-bound pVHL has a molten globule configuration with marginal stability.","type":"Abstract"},{"text":"The near-UV CD spectra of pVHL at 25 °C shown in Fig. 1B reveals no significant signals originating from aromatic side chains, thus suggesting a dramatic loss of tertiary structure of the soluble and unbound protein in comparison with the complex-related crystal structure.","type":"Results"},{"text":"Here, we present clear evidence of a molten globule conformation of the pVHL tumor suppressor protein under physiologically relevant solvent conditions.","type":"Discussion"},{"text":"The indications of a molten globule structure of pVHL are clear, given that the protein possesses a typical combination of an apparent secondary structure (Fig. 2A) with no tertiary structure","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"near-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14963040","version":2,"reference_html":"The von Hippel-Lindau tumor suppressor protein is a molten globule under native conditions: implications for its physiological activities. <i> Sutovsky H, Gazit E. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006206","term_name":"molten globule","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-05-17T13:47:15.816Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":213,"region_id":"DP00287r006","start":54,"term_id":"IDPO:0000003","statement":[{"text":"Upon the addition of urea, even at very low concentrations, the protein unfolds in a non-reversible manner, leading to the formation of amorphous aggregates.","type":"Abstract"},{"text":"We therefore conclude that, under native conditions, the non-bound pVHL has a molten globule configuration with marginal stability.","type":"Abstract"},{"text":"The degree of denaturation was assessed by monitoring ellipticity changes at 222 and 218 nm as a function of urea concentrations. As can be observed in Fig. 2, the unfolding of pVHL occurs at fairly low urea concentrations. Unfolding as reflected by a significant reduction in ellipticity was observed at urea concentrations as low as 0.25 m at both temperatures. Furthermore, the unfolding event was partially irreversible, and the formation of amorphous aggregates could be visualized by the naked eye.","type":"Results"},{"text":"However, the linear nature of the initial slope of the curve and the aggregative behavior implies that unbound pVHL stability is marginal, as was observed previously with other tumor suppressor proteins","type":"Results"},{"text":"The thermodynamic stability of the secondary structure as observed by CD is also marginal; at very low concentrations of urea the protein undergoes denaturation (Fig. 2), which results in some extent of aggregation.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"pH-induced protein unfolding evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14963040","version":2,"reference_html":"The von Hippel-Lindau tumor suppressor protein is a molten globule under native conditions: implications for its physiological activities. <i> Sutovsky H, Gazit E. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006315","term_name":"molten globule","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-05-17T13:46:48.213Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":213,"region_id":"DP00287r008","start":54,"term_id":"IDPO:0000003","statement":[{"text":"Dynamic light-scattering and gel filtration chromatography of the purified pVHL clearly indicated that the Stokes radius of the protein is larger than what would be expected from its crystal structure. However, under these conditions, the protein shows a clear secondary structure as determined by far-UV circular dichroism.","type":"Abstract"},{"text":"We therefore conclude that, under native conditions, the non-bound pVHL has a molten globule configuration with marginal stability.","type":"Abstract"},{"text":"Size exclusion chromatography was therefore used to estimate the hydrodynamic dimensions of the protein and as a probe for elucidating the compactness of the protein's tertiary structure, because the elution volume of partially or fully unfolded proteins is significantly smaller than that of well folded proteins due to the large increase in the Stokes radius.","type":"Results"},{"text":"Fig. 3A shows the Kav versus Mw plot; the calculated Kav for pVHL was 0.191, corresponding to a molecular mass of 47,130 Da (calculated with curve's equation), which is larger than the theoretical molecular mass value of pVHL (19,000 Da). Fig. 3B shows √-logKav versus Stokes radius (RS); according to this relation, the calculated RS for pVHL is 30.8 Å.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"chromatography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14963040","version":2,"reference_html":"The von Hippel-Lindau tumor suppressor protein is a molten globule under native conditions: implications for its physiological activities. <i> Sutovsky H, Gazit E. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","term_name":"molten globule","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-05-17T13:46:47.083Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":213,"region_id":"DP00287r009","start":54,"term_id":"IDPO:0000003","statement":[{"text":"Dynamic light-scattering and gel filtration chromatography of the purified pVHL clearly indicated that the Stokes radius of the protein is larger than what would be expected from its crystal structure. However, under these conditions, the protein shows a clear secondary structure as determined by far-UV circular dichroism.","type":"Abstract"},{"text":"We therefore conclude that, under native conditions, the non-bound pVHL has a molten globule configuration with marginal stability.","type":"Abstract"},{"text":"The measured hydrodynamic radius was 3 nm, and the estimated molecular mass was 43 kDa. These values, taken together with the size exclusion chromatography results, are significantly larger for the solution form of the protein than the values obtained from the folded pVHL crystal structure. This could indicate a somewhat flexible and non-compact conformation for the unbound protein.","type":"Results"},{"text":"The percent of scattered mass as attributed to the apparent hydrodynamic radius. RH for pVHL is 3 nm and estimated Mw is 43 kDa.","type":"Figure"},{"text":"Here, we present clear evidence of a molten globule conformation of the pVHL tumor suppressor protein under physiologically relevant solvent conditions.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"dynamic light scattering assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14963040","version":2,"reference_html":"The von Hippel-Lindau tumor suppressor protein is a molten globule under native conditions: implications for its physiological activities. <i> Sutovsky H, Gazit E. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007064","term_name":"molten globule","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-05-17T13:46:41.779Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":213,"region_id":"DP00287r010","start":54,"term_id":"IDPO:0000003","statement":[{"text":"The fluorescence of the hydrophobic ANSA probe is much stronger in the presence of molten globular state of proteins than with a rigid, well folded, or fully unfolded state (36). Fig. 5 shows that, upon binding to pVHL, ANSA fluorescence intensity increases by 50-fold, whereas the emission spectrum indicates a blue shift toward 400 nm. This could suggest that the hydrophobic core exists, but in a rather loosely packed conformation, and is therefore consistent with a molten globule tertiary structure.","type":"Results"},{"text":"Furthermore, such a significant increase in ANSA fluorescence (Fig. 5) clearly indicates a molten globule structure rather than the existence of a monomeric or dimeric well folded protein or, alternatively, an unfolded one.","type":"Discussion"},{"text":"Here, we present clear evidence of a molten globule conformation of the pVHL tumor suppressor protein under physiologically relevant solvent conditions.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"fluorescence evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14963040","version":2,"reference_html":"The von Hippel-Lindau tumor suppressor protein is a molten globule under native conditions: implications for its physiological activities. <i> Sutovsky H, Gazit E. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001249","term_name":"molten globule","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-05-17T13:46:39.678Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":213,"region_id":"DP00287r011","start":54,"term_id":"IDPO:0000003","statement":[{"text":"The sedimentation equilibrium data fit well to a single species with a calculated apparent molecular mass of 18,200 Da, implying that pVHL is monomeric in solution. This agrees very well with the Mr established by SDS gel electrophoresis and the Mr of 8,500 Da predicted for pVHL from the DNA sequence. There was some degree of aggregation, as observed at the lower part of the tube. This may reflect a moderate degree of nonspecific aggregation as may be expected for a partially unfolded protein after long incubation at high concentration.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"analytical ultracentrifugation evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14963040","version":2,"reference_html":"The von Hippel-Lindau tumor suppressor protein is a molten globule under native conditions: implications for its physiological activities. <i> Sutovsky H, Gazit E. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006275","term_name":"molten globule","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-05-17T13:46:38.236Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":67,"end":117,"reference_id":"12004076","reference_source":"pmid","reference_html":"Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling. <i> Min JH, Yang H, Ivan M, Gertler F, Kaelin WG, Pavletich NP. </i> Science, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"1LM8"}],"interaction_partner":[{"db":"UniProt","id":"Q16665","partner_start":null,"partner_end":null}],"region_id":"DP00287r013","statement":[{"text":"pVHL binds to HIF only when a conserved proline in HIF is hydroxylated, a modification that is oxygen-dependent. The 1.85 angstrom structure of a 20-residue HIF-1α peptide–pVHL–ElonginB–ElonginC complex shows that HIF-1α binds to pVHL in an extended β strand–like conformation. The hydroxyproline inserts into a gap in the pVHL hydrophobic core, at a site that is a hotspot for tumorigenic mutations, with its 4-hydroxyl group recognized by buried serine and histidine residues.","type":"Abstract"},{"text":"To investigate the targeting of HIF-1α by the VBC-CR ubiquitin-protein ligase and the basis of hydroxyproline recognition in intracellular signaling, we determined the 1.85 Å crystal structure of the pVHL–ElonginB–ElonginC (VBC) complex bound to the hydroxyproline-containing 20-residue destruction sequence of HIF-1α (Table 1 and fig. S1). The structure shows that a 15–amino acid portion of HIF-1α (residues 561 to 575) adopts an extended, β strand–like conformation (Fig. 1A). It binds pVHL in a bipartite manner, with two discontinuous HIF-1α segments interacting with a continuous site on pVHL.","type":"Article"},{"text":"HIF-1α interacts exclusively with the β domain of pVHL. It binds alongside the β sandwich, making five backbone-backbone hydrogen bonds (Fig. 1A). The side of the pVHL β sandwich where HIF-1α binds has the hydrophobic core partially exposed. This exposed hydrophobic patch, together with several partially buried polar residues, makes up the binding site of the hydroxyproline.","type":"Article"},{"text":"The hydroxyproline has a central role in complex formation. It is nearly entirely buried, with 96% of its accessible surface area in a hypothetical free peptide covered by pVHL. The pyrrolidine ring inserts toward the partially exposed hydrophobic core of the pVHL β domain, making multiple van der Waals contacts with Trp88, Tyr98, and Trp117 of pVHL (Fig. 2A). The 4-hydroxyl group inserts farthest into pVHL and forms hydrogen bonds with the Nδ of His115 (2.7 Å) and the OH group of Ser111 (2.7 Å), both of which also form hydrogen bonds with other pVHL groups (Fig. 2A). His115 and Ser111 are partially solvent exposed in the apo-VBC structure (10) but become entirely buried on HIF-1α binding.","type":"Article"},{"text":"The dotted lines indicate hydrogen bonds between the Gln67Oδ1, Tyr98 Oη, His110 NH, and His110 CO groups of pVHL, and the Leu562 NH, Hyp564 CO, Tyr565 NH, and Tyr565 CO groups of HIF-1α.","type":"Figure"},{"text":"Compared with Hyp564, the other N-segment residues make significantly fewer contacts. Among them, Ile566 makes the most contacts, interacting with Pro99 and Ile109 of pVHL. Met561 packs with Phe91 of pVHL, Leu562 with Tyr112and Arg69, Ala563 with Trp88, and Tyr565 with His110 (Fig. 2A).","type":"Article"},{"text":"pVHL residues contacting HIF1α: N67, R69, W88, F91, Y98, P99, I109, H110, S111, Y112, H115, W117.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-05-27T14:00:57.413Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":156,"end":161,"reference_id":"12004076","reference_source":"pmid","reference_html":"Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling. <i> Min JH, Yang H, Ivan M, Gertler F, Kaelin WG, Pavletich NP. </i> Science, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"Q15369","partner_start":null,"partner_end":null}],"region_id":"DP00287r015","statement":[{"text":"To investigate the targeting of HIF-1α by the VBC-CR ubiquitin-protein ligase and the basis of hydroxyproline recognition in intracellular signaling, we determined the 1.85 Å crystal structure of the pVHL–ElonginB–ElonginC (VBC) complex bound to the hydroxyproline-containing 20-residue destruction sequence of HIF-1α (Table 1 and fig. S1).","type":"Article"},{"text":"The α domain binds ElonginC, which, in association with ElonginB, recruits the VBC complex to Cul2-Rbx1 to form the ubiquitin-protein ligase (8–10).","type":"Article"},{"text":"pVHL residues Leu158 and Lys159 contact residue Cys112 of Elongin C.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-05-27T14:00:55.166Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":80,"end":84,"reference_id":"10205047","reference_source":"pmid","reference_html":"Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function. <i> Stebbins CE, Kaelin WG, Pavletich NP. </i> Science, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"1VCB"}],"interaction_partner":[{"db":"UniProt","id":"Q15369","partner_start":null,"partner_end":null}],"region_id":"DP00287r016","statement":[{"text":"Mutation of the VHL tumor suppressor is associated with the inherited von Hippel–Lindau (VHL) cancer syndrome and the majority of kidney cancers. VHL binds the ElonginC-ElonginB complex and regulates levels of hypoxia-inducible proteins. The structure of the ternary complex at 2.7 angstrom resolution shows two interfaces, one between VHL and ElonginC and another between ElonginC and ElonginB. Tumorigenic mutations frequently occur in a 35-residue domain of VHL responsible for ElonginC binding. A mutational patch on a separate domain of VHL indicates a second macromolecular binding site.","type":"Abstract"},{"text":"The VHL-ElonginC interface is almost completely hydrophobic with only a handful of significant hydrogen bonds at the periphery (Fig. 3A). The H1 helix of the VHL α domain fits into the concave surface of ElonginC, inserting hydrophobic side chains into pockets along the surface (Fig. 3A). Reciprocally, the H4 helix of ElonginC, which bulges out from the side of the concave surface, fits into an extended groove formed by the H1, H2, and H3 helices of the VHL α domain and completes the intermolecular four-helix cluster packing (Fig. 3A).","type":"Article"},{"text":"The H1 helix of the VHL α domain coincides with the 12–amino acid segment shown to be important for ElonginC binding (10), and the structure reveals that it makes extensive contacts to ElonginC. The most significant van der Waals contacts are made by Leu158, which protrudes from the H1 helix and fits into an ElonginC pocket, and by Cys162 and Arg161 (Fig. 3A). These are augmented by contacts from the Lys159, Val165, Val166, and Leu169 side chains of VHL (Fig. 3A). The other two helices of the α domain also contribute contacts (Leu178, Ile180, and Leu184), with Leu184 making the most extensive ones in this region (Fig. 3A). Additional contacts are made by residues in the first α-β linker (Leu153 and Val155) and by Arg82 from the β domain (Fig. 3A). The hydrogen bonds made by Arg82, together with those made by Lys159 and Arg161 from the H1 helix, represent the few significant hydrogen-bond contacts made at the VHL-ElonginC interface. The arginine side chains are also anchored in the hydrogen-bond networks of the VHL α-β domain interface (Fig. 2D). ","type":"Article"},{"text":"pVHL residues contacting Elongin C: R82, L153, V155, Y156, L158, K159, R161, V165, V166, L169, L178, I180, L184","type":"Curator statement"},{"text":"This evidence corresponds to the Arg82 site from pVHL β domain.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-05-27T14:00:53.095Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":153,"end":184,"reference_id":"10205047","reference_source":"pmid","reference_html":"Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function. <i> Stebbins CE, Kaelin WG, Pavletich NP. </i> Science, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"1VCB"}],"interaction_partner":[{"db":"UniProt","id":"Q15369","partner_start":null,"partner_end":null}],"region_id":"DP00287r017","statement":[{"text":"Mutation of the VHL tumor suppressor is associated with the inherited von Hippel–Lindau (VHL) cancer syndrome and the majority of kidney cancers. VHL binds the ElonginC-ElonginB complex and regulates levels of hypoxia-inducible proteins. The structure of the ternary complex at 2.7 angstrom resolution shows two interfaces, one between VHL and ElonginC and another between ElonginC and ElonginB. Tumorigenic mutations frequently occur in a 35-residue domain of VHL responsible for ElonginC binding. A mutational patch on a separate domain of VHL indicates a second macromolecular binding site.","type":"Abstract"},{"text":"The VHL-ElonginC interface is almost completely hydrophobic with only a handful of significant hydrogen bonds at the periphery (Fig. 3A). The H1 helix of the VHL α domain fits into the concave surface of ElonginC, inserting hydrophobic side chains into pockets along the surface (Fig. 3A). Reciprocally, the H4 helix of ElonginC, which bulges out from the side of the concave surface, fits into an extended groove formed by the H1, H2, and H3 helices of the VHL α domain and completes the intermolecular four-helix cluster packing (Fig. 3A).","type":"Article"},{"text":"The H1 helix of the VHL α domain coincides with the 12–amino acid segment shown to be important for ElonginC binding (10), and the structure reveals that it makes extensive contacts to ElonginC. The most significant van der Waals contacts are made by Leu158, which protrudes from the H1 helix and fits into an ElonginC pocket, and by Cys162 and Arg161 (Fig. 3A). These are augmented by contacts from the Lys159, Val165, Val166, and Leu169 side chains of VHL (Fig. 3A). The other two helices of the α domain also contribute contacts (Leu178, Ile180, and Leu184), with Leu184 making the most extensive ones in this region (Fig. 3A). Additional contacts are made by residues in the first α-β linker (Leu153 and Val155) and by Arg82 from the β domain (Fig. 3A). The hydrogen bonds made by Arg82, together with those made by Lys159 and Arg161 from the H1 helix, represent the few significant hydrogen-bond contacts made at the VHL-ElonginC interface. The arginine side chains are also anchored in the hydrogen-bond networks of the VHL α-β domain interface (Fig. 2D). ","type":"Article"},{"text":"pVHL residues contacting Elongin C: R82, L153, V155, Y156, L158, K159, R161, V165, V166, L169, L178, I180, L184","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-05-27T14:00:50.254Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":153,"end":184,"reference_id":"10205047","reference_source":"pmid","reference_html":"Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function. <i> Stebbins CE, Kaelin WG, Pavletich NP. </i> Science, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00287r019","statement":[{"text":"Mutation of the VHL tumor suppressor is associated with the inherited von Hippel–Lindau (VHL) cancer syndrome and the majority of kidney cancers. VHL binds the ElonginC-ElonginB complex and regulates levels of hypoxia-inducible proteins. The structure of the ternary complex at 2.7 angstrom resolution shows two interfaces, one between VHL and ElonginC and another between ElonginC and ElonginB. Tumorigenic mutations frequently occur in a 35-residue domain of VHL responsible for ElonginC binding. A mutational patch on a separate domain of VHL indicates a second macromolecular binding site.","type":"Abstract"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-05-27T14:01:03.460Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":67,"end":117,"reference_id":"12004076","reference_source":"pmid","reference_html":"Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling. <i> Min JH, Yang H, Ivan M, Gertler F, Kaelin WG, Pavletich NP. </i> Science, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00287r020","statement":[{"text":"To investigate the targeting of HIF-1α by the VBC-CR ubiquitin-protein ligase and the basis of hydroxyproline recognition in intracellular signaling, we determined the 1.85 Å crystal structure of the pVHL–ElonginB–ElonginC (VBC) complex bound to the hydroxyproline-containing 20-residue destruction sequence of HIF-1α (Table 1 and fig. S1). The structure shows that a 15–amino acid portion of HIF-1α (residues 561 to 575) adopts an extended, β strand–like conformation (Fig. 1A). It binds pVHL in a bipartite manner, with two discontinuous HIF-1α segments interacting with a continuous site on pVHL.","type":"Article"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-05-27T14:01:00.999Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":72,"end":78,"reference_id":"34431623","reference_source":"pmid","reference_html":"Amyloidogenic properties of peptides derived from the VHL tumor suppressor protein. <i> Segal D, Kumar V, Viswanathan GK, Ralhan K, Gazit E. </i> ChemMedChem, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0007044","ec_ontology":"ECO","ec_name":"transmission electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00287r021","statement":[{"text":"Here we report that using in silico approaches, we identified six (3-9 residues long) fragments predicted to harbor propensity to form amyloid fibrils. By a series of complementary biophysical techniques, including ThT binding assay, CD spectroscopy, Congo Red birefringence, transmission electron microscopy (TEM), atomic force microscopy (AFM), and X-ray diffraction, we found that two of the fragments, 72SQVIFCN78 and 147IFANITL153 , self-assembled in vitro and formed canonical amyloid fibrils β-sheets rich structures.","type":"Article"},{"text":"We performed TEM analysis to visualize the morphology of the SN7 and IL7 assemblies. As shown in Figure 2b and 2c, the assemblies exhibited fibrillar morphology for SN7 and IL7 aggregates, respectively.","type":"Article"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-09-06T07:11:59.812Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":147,"end":153,"reference_id":"34431623","reference_source":"pmid","reference_html":"Amyloidogenic properties of peptides derived from the VHL tumor suppressor protein. <i> Segal D, Kumar V, Viswanathan GK, Ralhan K, Gazit E. </i> ChemMedChem, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0007044","ec_ontology":"ECO","ec_name":"transmission electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00287r022","statement":[{"text":"Here we report that using in silico approaches, we identified six (3-9 residues long) fragments predicted to harbor propensity to form amyloid fibrils. By a series of complementary biophysical techniques, including ThT binding assay, CD spectroscopy, Congo Red birefringence, transmission electron microscopy (TEM), atomic force microscopy (AFM), and X-ray diffraction, we found that two of the fragments, 72SQVIFCN78 and 147IFANITL153 , self-assembled in vitro and formed canonical amyloid fibrils β-sheets rich structures.","type":"Article"},{"text":"We performed TEM analysis to visualize the morphology of the SN7 and IL7 assemblies. As shown in Figure 2b and 2c, the assemblies exhibited fibrillar morphology for SN7 and IL7 aggregates, respectively.","type":"Article"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-09-06T07:11:57.300Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":147,"end":153,"reference_id":"34431623","reference_source":"pmid","reference_html":"Amyloidogenic properties of peptides derived from the VHL tumor suppressor protein. <i> Segal D, Kumar V, Viswanathan GK, Ralhan K, Gazit E. </i> ChemMedChem, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0001591","ec_ontology":"ECO","ec_name":"atomic force microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00287r023","statement":[{"text":"Here we report that using in silico approaches, we identified six (3-9 residues long) fragments predicted to harbor propensity to form amyloid fibrils. By a series of complementary biophysical techniques, including ThT binding assay, CD spectroscopy, Congo Red birefringence, transmission electron microscopy (TEM), atomic force microscopy (AFM), and X-ray diffraction, we found that two of the fragments, 72SQVIFCN78 and 147IFANITL153 , self-assembled in vitro and formed canonical amyloid fibrils β-sheets rich structures.","type":"Article"},{"text":"Furthermore, we performed AFM imaging to get additional details regarding the structural parameters such as height and diameter of the amyloid fibrils. Representative AFM images of amyloids formed by SN7 and IL7 are shown in Figure 2e, 2f, respectively. The amyloids of SN7 appeared as clusters of intercalated fibrils with a height of 5-10 nm and of diameter ~30 nm (n=30). The IL7 amyloids were observed to be of 3-13 nm height with a diameter of ~46 nm and varying length (n=30).","type":"Article"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-09-06T07:11:55.242Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":72,"end":78,"reference_id":"34431623","reference_source":"pmid","reference_html":"Amyloidogenic properties of peptides derived from the VHL tumor suppressor protein. <i> Segal D, Kumar V, Viswanathan GK, Ralhan K, Gazit E. </i> ChemMedChem, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0001591","ec_ontology":"ECO","ec_name":"atomic force microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00287r024","statement":[{"text":"Here we report that using in silico approaches, we identified six (3-9 residues long) fragments predicted to harbor propensity to form amyloid fibrils. By a series of complementary biophysical techniques, including ThT binding assay, CD spectroscopy, Congo Red birefringence, transmission electron microscopy (TEM), atomic force microscopy (AFM), and X-ray diffraction, we found that two of the fragments, 72SQVIFCN78 and 147IFANITL153 , self-assembled in vitro and formed canonical amyloid fibrils β-sheets rich structures.","type":"Article"},{"text":"Furthermore, we performed AFM imaging to get additional details regarding the structural parameters such as height and diameter of the amyloid fibrils. Representative AFM images of amyloids formed by SN7 and IL7 are shown in Figure 2e, 2f, respectively. The amyloids of SN7 appeared as clusters of intercalated fibrils with a height of 5-10 nm and of diameter ~30 nm (n=30). The IL7 amyloids were observed to be of 3-13 nm height with a diameter of ~46 nm and varying length (n=30).","type":"Article"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-09-06T07:11:53.393Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":72,"end":78,"reference_id":"34431623","reference_source":"pmid","reference_html":"Amyloidogenic properties of peptides derived from the VHL tumor suppressor protein. <i> Segal D, Kumar V, Viswanathan GK, Ralhan K, Gazit E. </i> ChemMedChem, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00287r025","statement":[{"text":"Here we report that using in silico approaches, we identified six (3-9 residues long) fragments predicted to harbor propensity to form amyloid fibrils. By a series of complementary biophysical techniques, including ThT binding assay, CD spectroscopy, Congo Red birefringence, transmission electron microscopy (TEM), atomic force microscopy (AFM), and X-ray diffraction, we found that two of the fragments, 72SQVIFCN78 and 147IFANITL153 , self-assembled in vitro and formed canonical amyloid fibrils β-sheets rich structures.","type":"Article"},{"text":"Among all the six peptides, two heptapeptides, namely 72SQVIFCN78 and 147IFANITL153 (hereafter termed SN7 and IL7, respectively) Figure. 1d exhibited a significant increase in ThT intensity compared to the other peptides when used at 100 µM, indicating their high propensity to self-assemble into amyloids.","type":"Article"},{"text":"To obtain deeper insights on the SN7 and IL7 aggregation kinetics, the two peptides were subjected to aggregation assay for 48 hours, using ThT as a real-time monitoring probe at physiological pH and temperature in 20 mM sodium phosphate buffer. As shown in Figure. 1e, both peptides displayed rapid aggregation kinetics, with an undetectable lag phase, reaching a plateau after 24-27 hours.","type":"Article"},{"text":"To obtain deeper insights on the SN7 and IL7 aggregation kinetics, the two peptides were subjected to aggregation assay for 48 hours, using ThT as a real-time monitoring probe at physiological pH and temperature in 20 mM sodium phosphate buffer. As shown in Figure. 1e, both peptides displayed rapid aggregation kinetics, with an undetectable lag phase, reaching a plateau after 24-27 hours.","type":"Article"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-09-06T07:11:51.511Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":147,"end":153,"reference_id":"34431623","reference_source":"pmid","reference_html":"Amyloidogenic properties of peptides derived from the VHL tumor suppressor protein. <i> Segal D, Kumar V, Viswanathan GK, Ralhan K, Gazit E. </i> ChemMedChem, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00287r026","statement":[{"text":"Here we report that using in silico approaches, we identified six (3-9 residues long) fragments predicted to harbor propensity to form amyloid fibrils. By a series of complementary biophysical techniques, including ThT binding assay, CD spectroscopy, Congo Red birefringence, transmission electron microscopy (TEM), atomic force microscopy (AFM), and X-ray diffraction, we found that two of the fragments, 72SQVIFCN78 and 147IFANITL153 , self-assembled in vitro and formed canonical amyloid fibrils β-sheets rich structures.","type":"Article"},{"text":"Among all the six peptides, two heptapeptides, namely 72SQVIFCN78 and 147IFANITL153 (hereafter termed SN7 and IL7, respectively) Figure. 1d exhibited a significant increase in ThT intensity compared to the other peptides when used at 100 µM, indicating their high propensity to self-assemble into amyloids.","type":"Article"},{"text":"To obtain deeper insights on the SN7 and IL7 aggregation kinetics, the two peptides were subjected to aggregation assay for 48 hours, using ThT as a real-time monitoring probe at physiological pH and temperature in 20 mM sodium phosphate buffer. As shown in Figure. 1e, both peptides displayed rapid aggregation kinetics, with an undetectable lag phase, reaching a plateau after 24-27 hours.","type":"Article"},{"text":"To obtain deeper insights on the SN7 and IL7 aggregation kinetics, the two peptides were subjected to aggregation assay for 48 hours, using ThT as a real-time monitoring probe at physiological pH and temperature in 20 mM sodium phosphate buffer. As shown in Figure. 1e, both peptides displayed rapid aggregation kinetics, with an undetectable lag phase, reaching a plateau after 24-27 hours.","type":"Article"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-09-06T07:11:49.342Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":147,"end":153,"reference_id":"34431623","reference_source":"pmid","reference_html":"Amyloidogenic properties of peptides derived from the VHL tumor suppressor protein. <i> Segal D, Kumar V, Viswanathan GK, Ralhan K, Gazit E. </i> ChemMedChem, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00287r027","statement":[{"text":"Here we report that using in silico approaches, we identified six (3-9 residues long) fragments predicted to harbor propensity to form amyloid fibrils. By a series of complementary biophysical techniques, including ThT binding assay, CD spectroscopy, Congo Red birefringence, transmission electron microscopy (TEM), atomic force microscopy (AFM), and X-ray diffraction, we found that two of the fragments, 72SQVIFCN78 and 147IFANITL153 , self-assembled in vitro and formed canonical amyloid fibrils β-sheets rich structures.","type":"Article"},{"text":"To further validate the ThT results, we performed CD analysis of these peptides before (t=0 hours) and after the aggregation (t=48 hours) to detect the amyloid-specific secondary structural changes. The concentration used for recording CD spectra was 400 µM to obtain a better signal-to-noise ratio. The CD spectra exhibited a negative ellipticity at 195 nm for IL7 and 200 nm for SN7 at the beginning of the aggregation (t=0), suggesting that the peptides possessed random coil conformation in their monomeric form. At the end of the aggregation period (t=48 hours), the individual peaks shifted to 220-224 nm, which is indicative of the β-sheet rich structures by both peptides (Figure. 2a). β-sheet formation is a characteristic hallmark of amyloid structures, thus substantiating the findings from ThT analysis, suggestive of self-assembly of the heptapeptides to form amyloids.","type":"Article"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-09-06T07:11:47.203Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":72,"end":78,"reference_id":"34431623","reference_source":"pmid","reference_html":"Amyloidogenic properties of peptides derived from the VHL tumor suppressor protein. <i> Segal D, Kumar V, Viswanathan GK, Ralhan K, Gazit E. </i> ChemMedChem, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00287r028","statement":[{"text":"Here we report that using in silico approaches, we identified six (3-9 residues long) fragments predicted to harbor propensity to form amyloid fibrils. By a series of complementary biophysical techniques, including ThT binding assay, CD spectroscopy, Congo Red birefringence, transmission electron microscopy (TEM), atomic force microscopy (AFM), and X-ray diffraction, we found that two of the fragments, 72SQVIFCN78 and 147IFANITL153 , self-assembled in vitro and formed canonical amyloid fibrils β-sheets rich structures.","type":"Article"},{"text":"To further validate the ThT results, we performed CD analysis of these peptides before (t=0 hours) and after the aggregation (t=48 hours) to detect the amyloid-specific secondary structural changes. The concentration used for recording CD spectra was 400 µM to obtain a better signal-to-noise ratio. The CD spectra exhibited a negative ellipticity at 195 nm for IL7 and 200 nm for SN7 at the beginning of the aggregation (t=0), suggesting that the peptides possessed random coil conformation in their monomeric form. At the end of the aggregation period (t=48 hours), the individual peaks shifted to 220-224 nm, which is indicative of the β-sheet rich structures by both peptides (Figure. 2a). β-sheet formation is a characteristic hallmark of amyloid structures, thus substantiating the findings from ThT analysis, suggestive of self-assembly of the heptapeptides to form amyloids.","type":"Article"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-09-06T07:11:45.019Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":72,"end":78,"reference_id":"34431623","reference_source":"pmid","reference_html":"Amyloidogenic properties of peptides derived from the VHL tumor suppressor protein. <i> Segal D, Kumar V, Viswanathan GK, Ralhan K, Gazit E. </i> ChemMedChem, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0006212","ec_ontology":"ECO","ec_name":"particle scattering evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00287r029","statement":[{"text":"Here we report that using in silico approaches, we identified six (3-9 residues long) fragments predicted to harbor propensity to form amyloid fibrils. By a series of complementary biophysical techniques, including ThT binding assay, CD spectroscopy, Congo Red birefringence, transmission electron microscopy (TEM), atomic force microscopy (AFM), and X-ray diffraction, we found that two of the fragments, 72SQVIFCN78 and 147IFANITL153 , self-assembled in vitro and formed canonical amyloid fibrils β-sheets rich structures.","type":"Article"},{"text":"This observation was further corroborated by collecting an X-ray diffraction pattern for the self-assembly of both peptides. Classical amyloid fibrils exhibit a characteristic diffraction pattern that displays the inter-strand distance of 4.5-4.8 Å and inter-sheet distance of 10-11Å, due to the specific arrangement of β-sheets in an amyloid fiber.","type":"Article"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-09-06T07:11:42.998Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":147,"end":153,"reference_id":"34431623","reference_source":"pmid","reference_html":"Amyloidogenic properties of peptides derived from the VHL tumor suppressor protein. <i> Segal D, Kumar V, Viswanathan GK, Ralhan K, Gazit E. </i> ChemMedChem, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0006212","ec_ontology":"ECO","ec_name":"particle scattering evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00287r030","statement":[{"text":"Here we report that using in silico approaches, we identified six (3-9 residues long) fragments predicted to harbor propensity to form amyloid fibrils. By a series of complementary biophysical techniques, including ThT binding assay, CD spectroscopy, Congo Red birefringence, transmission electron microscopy (TEM), atomic force microscopy (AFM), and X-ray diffraction, we found that two of the fragments, 72SQVIFCN78 and 147IFANITL153 , self-assembled in vitro and formed canonical amyloid fibrils β-sheets rich structures.","type":"Article"},{"text":"This observation was further corroborated by collecting an X-ray diffraction pattern for the self-assembly of both peptides. Classical amyloid fibrils exhibit a characteristic diffraction pattern that displays the inter-strand distance of 4.5-4.8 Å and inter-sheet distance of 10-11Å, due to the specific arrangement of β-sheets in an amyloid fiber.","type":"Article"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-09-06T07:11:40.881Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":147,"end":153,"reference_id":"34431623","reference_source":"pmid","reference_html":"Amyloidogenic properties of peptides derived from the VHL tumor suppressor protein. <i> Segal D, Kumar V, Viswanathan GK, Ralhan K, Gazit E. </i> ChemMedChem, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0007157","ec_ontology":"ECO","ec_name":"cell staining evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00287r031","statement":[{"text":"Here we report that using in silico approaches, we identified six (3-9 residues long) fragments predicted to harbor propensity to form amyloid fibrils. By a series of complementary biophysical techniques, including ThT binding assay, CD spectroscopy, Congo Red birefringence, transmission electron microscopy (TEM), atomic force microscopy (AFM), and X-ray diffraction, we found that two of the fragments, 72SQVIFCN78 and 147IFANITL153 , self-assembled in vitro and formed canonical amyloid fibrils β-sheets rich structures.","type":"Article"},{"text":"We subsequently investigated the amyloidogenic nature of SN7 and IL7 aggregates using the amyloid-specific Congo Red (CR) dye. CR is a histopathological dye routinely used to diagnose amyloids formed in vitro and in tissue biopsies. [18] The dye can bind to the cross-β-sheets of amyloids, and this interaction results in the exhibition of apple-green birefringence when observed under cross-polarized light.","type":"Article"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-09-06T07:11:38.478Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":72,"end":78,"reference_id":"34431623","reference_source":"pmid","reference_html":"Amyloidogenic properties of peptides derived from the VHL tumor suppressor protein. <i> Segal D, Kumar V, Viswanathan GK, Ralhan K, Gazit E. </i> ChemMedChem, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0007157","ec_ontology":"ECO","ec_name":"cell staining evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00287r032","statement":[{"text":"Here we report that using in silico approaches, we identified six (3-9 residues long) fragments predicted to harbor propensity to form amyloid fibrils. By a series of complementary biophysical techniques, including ThT binding assay, CD spectroscopy, Congo Red birefringence, transmission electron microscopy (TEM), atomic force microscopy (AFM), and X-ray diffraction, we found that two of the fragments, 72SQVIFCN78 and 147IFANITL153 , self-assembled in vitro and formed canonical amyloid fibrils β-sheets rich structures.","type":"Article"},{"text":"We subsequently investigated the amyloidogenic nature of SN7 and IL7 aggregates using the amyloid-specific Congo Red (CR) dye. CR is a histopathological dye routinely used to diagnose amyloids formed in vitro and in tissue biopsies. [18] The dye can bind to the cross-β-sheets of amyloids, and this interaction results in the exhibition of apple-green birefringence when observed under cross-polarized light.","type":"Article"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-09-06T07:11:35.543Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":213,"reference_id":"24899725","reference_source":"pmid","reference_html":"Regulation of the VHL/HIF-1 pathway by DJ-1. <i> Parsanejad M, Zhang Y, Qu D, Irrcher I, Rousseaux MW, Aleyasin H, Kamkar F, Callaghan S, Slack RS, Mak TW, Lee S, Figeys D, Park DS. </i> J Neurosci, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005644","ec_ontology":"ECO","ec_name":"immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"Q99497","partner_start":null,"partner_end":null}],"region_id":"DP00287r033","statement":[{"text":"We confirmed the physical interaction of DJ-1 and VHL proteins in SH-SY5Y cells by immunoprecipitating VHL using VHL antibody and mouse IgG-conjugated beads and probing for endogenous DJ-1 (Fig. 1A). We observed that endogenous DJ-1 was coimmunoprecipitated with endogenous VHL ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-14T09:28:17.871Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":213,"reference_id":"24899725","reference_source":"pmid","reference_html":"Regulation of the VHL/HIF-1 pathway by DJ-1. <i> Parsanejad M, Zhang Y, Qu D, Irrcher I, Rousseaux MW, Aleyasin H, Kamkar F, Callaghan S, Slack RS, Mak TW, Lee S, Figeys D, Park DS. </i> J Neurosci, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0007184","ec_ontology":"ECO","ec_name":"protein mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"Q99497","partner_start":null,"partner_end":null}],"region_id":"DP00287r034","statement":[{"text":"VHL was one of the baits and analysis of the dataset suggested DJ-1 as one of its interacting candidates with the interaction confidence score of 0.31 an unbiased mass spectrometry screen, which indicated Von Hippel Lindau (VHL) protein as a potential interacting partner.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-16T12:30:03.301Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":59,"end":213,"reference_id":"11641274","reference_source":"pmid","reference_html":"FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity. <i> Mahon PC, Hirota K, Semenza GL. </i> Genes Dev, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"Q13547","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q92769","partner_start":null,"partner_end":null},{"db":"UniProt","id":"O15379","partner_start":null,"partner_end":null}],"region_id":"DP00287r035","statement":[{"text":"In vitro-translated 35 S-labeled VHL interacted with GST–HDAC-1, GST–HDAC-2, and GST–HDAC-3 fusion proteins but not with GST (Fig. 7A).","type":"Results"},{"text":"VHL\nresidues 1–213 or 1–155 bound to the GST–HDAC fusion\nproteins whereas VHL(1–58) and VHL(1–57) did not (Fig.\n7B).","type":"Results"}],"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"[35 S]methionine-labeled proteins were produced in reticulocyte lysates programmed with plasmids encoding HIF-1 alpha, HA–\nFIH-1, or FLAG–VHL sequences."}]}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-14T09:27:07.283Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":213,"reference_id":"11641274","reference_source":"pmid","reference_html":"FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity. <i> Mahon PC, Hirota K, Semenza GL. </i> Genes Dev, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0003714","term_name":"transcription corepressor activity","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005648","ec_ontology":"ECO","ec_name":"luciferase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00287r037","statement":[{"text":"In vitro-translated 35 S-labeled VHL interacted with GST–HDAC-1, GST–HDAC-2, and GST–HDAC-3 fusion proteins but not with GST (Fig. 7A).","type":"Results"},{"text":"Taken together with\nthe cotransfection assays, these studies demonstrate that\nVHL functions as a corepressor by recruiting HDACs to\nHIF-1 alpha.","type":"Results"},{"text":"In addition, we\ndemonstrate that FIH-1 binds to VHL and that VHL also functions as a transcriptional corepressor that\ninhibits HIF-1alpha transactivation function by recruiting histone deacetylases.","type":"Abstract"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-23T12:05:17.651Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"For usage guidance, see comment in GO:0003712 ; transcription coregulator activity.","term_def":"\"A transcription coregulator activity that represses or decreases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Corepressors often act by altering chromatin structure and modifications. For example, one class of transcription corepressors modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators.\" [GOC:txnOH-2018, PMID:10213677, PMID:16858867]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":213,"reference_id":"11641274","reference_source":"pmid","reference_html":"FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity. <i> Mahon PC, Hirota K, Semenza GL. </i> Genes Dev, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"Q16665","partner_start":531,"partner_end":826}],"region_id":"DP00287r038","statement":[{"text":"To demonstrate binding directly and to localize the\nregion of FIH-1 that interacted with VHL and with HIF-\n1 alpha, 35 S-labeled FIH-1 that was either full length (1–349)\nor lacking N-terminal residues (126–349) was synthesized and tested for interaction with FLAG-tagged VHL\nor GST–HIF1 alpha (531–826). FIH-1(1–349) bound to FLAG–VHL or GST–HIF-1 alpha (531–826), whereas FIH-1(126–349)\nbound only to GST–HIF-1 alpha (531–826) ","type":"Results"},{"text":"Whereas VHL residues\n1–155 were sufficient for binding to FIH-1, residues\n1–213 were required for efficient binding to HIF-1 alpha (Fig.\n4C). These studies indicate the presence of distinct bind-\ning sites that allow the simultaneous interaction of FIH-\n1, HIF-1 alpha, and VHL.","type":"Results"}],"construct_alterations":[{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-14T10:53:57.289Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":155,"reference_id":"11641274","reference_source":"pmid","reference_html":"FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity. <i> Mahon PC, Hirota K, Semenza GL. </i> Genes Dev, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"Q9NWT6","partner_start":1,"partner_end":349}],"region_id":"DP00287r039","statement":[{"text":"To demonstrate binding directly and to localize the\nregion of FIH-1 that interacted with VHL and with HIF-\n1 alpha, 35 S-labeled FIH-1 that was either full length (1–349)\nor lacking N-terminal residues (126–349) was synthesized and tested for interaction with FLAG-tagged VHL\nor GST–HIF-1 alpha (531–826). FIH-1(1–349) bound to FLAG–VHL or GST–HIF-1 alpha (531–826), whereas FIH-1(126–349)\nbound only to GST–HIF-1 alpha (531–826) ","type":"Results"},{"text":"Whereas VHL residues\n1–155 were sufficient for binding to FIH-1, residues\n1–213 were required for efficient binding to HIF-1 alpha (Fig.\n4C). These studies indicate the presence of distinct bind-\ning sites that allow the simultaneous interaction of FIH-\n1, HIF-1 alpha, and VHL.","type":"Results"}],"construct_alterations":[{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-14T09:25:42.182Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":213,"reference_id":"23338840","reference_source":"pmid","reference_html":"The VHL tumor suppressor protein regulates tumorigenicity of U87-derived             glioma stem-like cells by inhibiting the JAK/STAT signaling pathway. <i> Kanno H, Sato H, Yokoyama TA, Yoshizumi T, Yamada S. </i> Int J Oncol, 2013","date":"2022-06-06T18:37:54.750Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0010468","term_name":"regulation of gene expression","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0007142","ec_ontology":"ECO","ec_name":"green fluorescent protein immunolocalization evidence used in manual assertion","unpublished":true,"released":"2022_06","version":2,"region_id":"DP00287r040","statement":[{"text":"Regarding the expression of various factors, that of CD133 was decreased in the VHL transfectants and those of STAT3, JAK2 and Elongin A were eliminated.  However, the expression of PTEN and of VHL was upregulated.","type":"Abstract"},{"text":"VHL inhibited STAT3, JAK2 and Elongin A.","type":"Discussion"},{"text":"In addition, VHL upregulated PTEN expression.","type":"Discussion"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"This class covers any process that regulates the rate of production of a mature gene product, and so includes processes that regulate that rate by regulating the level, stability or availability of intermediates in the process of gene expression.  For example, it covers any process that regulates the level, stability or availability of mRNA or circRNA for translation and thereby regulates the rate of production of the encoded protein via translation.","term_def":"\"Any process that modulates the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA).\" [GOC:txnOH-2018]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:49:13.309Z"}},{"start":1,"end":213,"reference_id":"17973242","reference_source":"pmid","reference_html":"Loss of PL6 protein expression in renal clear cell carcinomas and other VHL-deficient tumours. <i> Ivanova AV, Vortmeyer A, Ivanov SV, Nickerson ML, Maher ER, Lerman MI. </i> J Pathol, 2008","date":"2022-06-06T16:12:47.626Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0010468","term_name":"regulation of gene expression","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005653","ec_ontology":"ECO","ec_name":"northern blot evidence used in manual assertion","unpublished":true,"released":"2022_06","version":2,"region_id":"DP00287r041","statement":[{"text":"The restoration of VHL function in vitro in the VHL-deficient CC-RCC cell lines was found to reinstate PL6 expression, thus establishing a direct link between VHL and PL6.","type":"Abstract"},{"text":"We found that functional VHL inactivation caused down-regulation of PL6 expression, thus suggesting transcriptional regulation of PL6 by pVHL.","type":"Discussion"},{"text":"Northern blot analysis demonstrated that PL6 expression was significantly lower in cell lines with mutated VHL as compared to their wtVHL-transfected counterparts or to KRC/Y and 293T cell lines","type":"Results"}],"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"This class covers any process that regulates the rate of production of a mature gene product, and so includes processes that regulate that rate by regulating the level, stability or availability of intermediates in the process of gene expression.  For example, it covers any process that regulates the level, stability or availability of mRNA or circRNA for translation and thereby regulates the rate of production of the encoded protein via translation.","term_def":"\"Any process that modulates the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA).\" [GOC:txnOH-2018]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:49:15.842Z"}},{"start":1,"end":213,"reference_id":"17973242","reference_source":"pmid","reference_html":"Loss of PL6 protein expression in renal clear cell carcinomas and other VHL-deficient tumours. <i> Ivanova AV, Vortmeyer A, Ivanov SV, Nickerson ML, Maher ER, Lerman MI. </i> J Pathol, 2008","date":"2022-06-06T16:14:12.277Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0010468","term_name":"regulation of gene expression","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006031","ec_ontology":"ECO","ec_name":"immunolocalization evidence used in manual assertion","unpublished":true,"released":"2022_06","version":2,"region_id":"DP00287r042","statement":[{"text":"The restoration of VHL function in vitro in the VHL-deficient CC-RCC cell lines was found to reinstate PL6 expression, thus establishing a direct link between VHL and PL6.","type":"Abstract"},{"text":"Immunostaining analysis of VHL-deficient tumours (CC-RCC, haemangioblastoma and epididymal adenocarcinoma) showed no PL6 positivity compared to matched normal tissues and was in line with regulation of PL6 expression by pVHL.","type":"Discussion"},{"text":"Immunostaining of these cells with anti-PL6 antibodies showed no PL6 protein in VHL-deficient cells, while their wtVHL-transfected derivatives were positive for the PL6 protein. KRC/Y and 293T, cell lines with intact VHL gene, had a high PL6 protein level. ","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"This class covers any process that regulates the rate of production of a mature gene product, and so includes processes that regulate that rate by regulating the level, stability or availability of intermediates in the process of gene expression.  For example, it covers any process that regulates the level, stability or availability of mRNA or circRNA for translation and thereby regulates the rate of production of the encoded protein via translation.","term_def":"\"Any process that modulates the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA).\" [GOC:txnOH-2018]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:49:17.384Z"}},{"start":1,"end":213,"reference_id":"12169691","reference_source":"pmid","reference_html":"The von Hippel-Lindau tumor suppressor stabilizes novel plant homeodomain protein Jade-1. <i> Zhou MI, Wang H, Ross JJ, Kuzmin I, Xu C, Cohen HT. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005805","ec_ontology":"ECO","ec_name":"yeast 2-hybrid evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"Q6IE81-3","partner_start":null,"partner_end":null}],"region_id":"DP00287r043","statement":[{"text":"To identify low occupancy VHL protein partners with potential relevance to renal cancer, we screened a human kidney library against human VHL p30 using a yeast two-hybrid approach. Jade-1 (gene for Apoptosis and Differentiation in Epithelia) encodes a previously uncharacterized 64-kDa protein that interacts strongly with VHL protein and is most highly expressed in kidney.","type":"Abstract"},{"text":"The human Jade-1 gene was\nidentified as a particularly strong VHL-interacting clone in a\nyeast two-hybrid screen of human VHL p30","type":"Results"}],"construct_alterations":[{"term_id":"MI:0520","term_name":"HA","term_namespace":"Tag","start":null,"end":null,"position":"unspecified","statements":[{"type":"Figure","text":"FLAG (FL)-tagged Jade-1 and other library clones were cotransfected with hemagglutinin (HA)-tagged VHL in 293T17 cells."}]}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-23T11:38:39.900Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":213,"reference_id":"12169691","reference_source":"pmid","reference_html":"The von Hippel-Lindau tumor suppressor stabilizes novel plant homeodomain protein Jade-1. <i> Zhou MI, Wang H, Ross JJ, Kuzmin I, Xu C, Cohen HT. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"Q6IE81-3","partner_start":1,"partner_end":202},{"db":"UniProt","id":"Q6IE81-3","partner_start":254,"partner_end":311}],"region_id":"DP00287r044","statement":[{"text":"Jade-1 immunoprecipitation of these same cell lysates permitted coimmunoprecipitation of VHL with full-length Jade-1, dd, and del1, but not with del2 (Fig. 3F). Likewise, VHL immunoprecipitation allowed coimmunoprecipitation of full-length Jade-1, dd, and del1, but not del2 (Fig. 3G). The VHL interaction with del1 did appear reduced, even taking into account lower del1 expression. As expected, immunoprecipitation in the absence of either partner did not show the interaction (Fig. 3, F and G, end lanes).Thus, these experiments demonstrate that the Jade-1 carboxyl terminus and PHD regions themselves are not absolutely required and that the amino terminus and the inter-PHD region in particular may be most important for interaction with VHL. These findings also support the specificity of the VHL-Jade-1 interaction.","type":"Results"}],"construct_alterations":[{"term_id":"MI:0520","term_name":"HA","term_namespace":"Tag","start":null,"end":null,"position":"unspecified","statements":[{"type":"Figure","text":"FLAG (FL)-tagged Jade-1 and other library clones were cotransfected with hemagglutinin (HA)-tagged VHL in 293T17 cells."}]}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-23T11:38:47.491Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":213,"reference_id":"15824735","reference_source":"pmid","reference_html":"Identification of novel VHL target genes and relationship to hypoxic response pathways. <i> Maina EN, Morris MR, Zatyka M, Raval RR, Banks RE, Richards FM, Johnson CM, Maher ER. </i> Oncogene, 2005","date":"2022-06-06T18:37:03.969Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0010468","term_name":"regulation of gene expression","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0000272","ec_ontology":"ECO","ec_name":"Affymetrix GeneChip evidence used in manual assertion","unpublished":true,"released":"2022_06","version":2,"region_id":"DP00287r045","statement":[{"text":"We identified 30 genes (0.2 of total genes analysed) that demonstrated a >=X2-fold difference between VHL+ and VHL- cells in both experiments and in the three different clones.","type":"Results"}],"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"This class covers any process that regulates the rate of production of a mature gene product, and so includes processes that regulate that rate by regulating the level, stability or availability of intermediates in the process of gene expression.  For example, it covers any process that regulates the level, stability or availability of mRNA or circRNA for translation and thereby regulates the rate of production of the encoded protein via translation.","term_def":"\"Any process that modulates the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA).\" [GOC:txnOH-2018]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":213,"reference_id":"15824735","reference_source":"pmid","reference_html":"Identification of novel VHL target genes and relationship to hypoxic response pathways. <i> Maina EN, Morris MR, Zatyka M, Raval RR, Banks RE, Richards FM, Johnson CM, Maher ER. </i> Oncogene, 2005","date":"2022-06-06T18:36:50.053Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0010468","term_name":"regulation of gene expression","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005660","ec_ontology":"ECO","ec_name":"quantitative polymerase chain reaction evidence used in manual assertion","unpublished":true,"released":"2022_06","version":2,"region_id":"DP00287r046","statement":[{"text":"Expression of target genes was normalized tob-actin and results for the 11 genes analysed are shown in Table 1. Real-time PCR analysis confirmed the results of the microarray analysis for all 11 genes.","type":"Results"},{"text":"Genes regulated by VHL: MLC2, GPR56, CDKN1C, P311, GLS, DOC-2/DAB2, GNG4, Claudin 4, SPARC, MCT3, E3, VEGF, PAI-1, beta-actin.","type":"Curator statement"},{"text":"We transiently transfected empty vector (pCDNA3.1, In-vitrogen) or the wild-type pVHL (pCDNA 3.1-VHL (1–213) HA) into RCC4 cells to determine whether theresults of transient transfection were consistent withthose for stable transfection. The expression of fourgenes was analysed (CDKN1C, P311, Claudin 4 and E3) by real-time PCR and these demonstrated similar resultsin transient and stable transfections.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"This class covers any process that regulates the rate of production of a mature gene product, and so includes processes that regulate that rate by regulating the level, stability or availability of intermediates in the process of gene expression.  For example, it covers any process that regulates the level, stability or availability of mRNA or circRNA for translation and thereby regulates the rate of production of the encoded protein via translation.","term_def":"\"Any process that modulates the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA).\" [GOC:txnOH-2018]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":213,"reference_id":"15824735","reference_source":"pmid","reference_html":"Identification of novel VHL target genes and relationship to hypoxic response pathways. <i> Maina EN, Morris MR, Zatyka M, Raval RR, Banks RE, Richards FM, Johnson CM, Maher ER. </i> Oncogene, 2005","date":"2022-06-06T17:01:17.689Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0010468","term_name":"regulation of gene expression","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2022_06","version":2,"region_id":"DP00287r047","statement":[{"text":"To determine whether pVHL regulation of target gene transcripts was reflected in protein levels, Western blots of RCC4/VHL+ and RCC4/VHL- protein extracts were probed with anti-CDKNIC and anti CT-3 antibodies. In each case the effect of pVHL on the transcripts was mirrored by the effect on protein levels. Thus pVHL upregulated CDKNIC and downregulated MCT3 protein expression (Figure 2).","type":"Results"}],"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"This class covers any process that regulates the rate of production of a mature gene product, and so includes processes that regulate that rate by regulating the level, stability or availability of intermediates in the process of gene expression.  For example, it covers any process that regulates the level, stability or availability of mRNA or circRNA for translation and thereby regulates the rate of production of the encoded protein via translation.","term_def":"\"Any process that modulates the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA).\" [GOC:txnOH-2018]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":213,"reference_id":"15824735","reference_source":"pmid","reference_html":"Identification of novel VHL target genes and relationship to hypoxic response pathways. <i> Maina EN, Morris MR, Zatyka M, Raval RR, Banks RE, Richards FM, Johnson CM, Maher ER. </i> Oncogene, 2005","date":"2022-06-06T17:01:36.778Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0010468","term_name":"regulation of gene expression","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005802","ec_ontology":"ECO","ec_name":"cell transfection experiment evidence used in manual assertion","unpublished":true,"released":"2022_06","version":2,"region_id":"DP00287r048","statement":[{"text":"The relationship between pVHL regulation of target genes in an isogenic cell line and in primary RCC with VHL inactivation (somatic VHL mutation73p25 allele loss) was analysed in up to nine paired normal–tumour pairs. For CDKN1C (n=8), GNG4 (n=8), GPR56 (n=8), GPR56 (n=8),  MCT3 (n=4), MLC2 (n=6), P311(n=8) and SPARC (n=7), all tumours tested demonstrated altered expression consistent with the cell line data (results showed threshold of X2-fold differential expression).For DOC-2/DAB26/7  clear  cell  RCC  with VHL inactivation  demonstrated  downregulation  comparedto matched normal tissue. However, E3 and CDN4 demonstrated altered expression in only a minority of the primary tumours tested (4/9 and 1/3, respectively)(data not shown).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"This class covers any process that regulates the rate of production of a mature gene product, and so includes processes that regulate that rate by regulating the level, stability or availability of intermediates in the process of gene expression.  For example, it covers any process that regulates the level, stability or availability of mRNA or circRNA for translation and thereby regulates the rate of production of the encoded protein via translation.","term_def":"\"Any process that modulates the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA).\" [GOC:txnOH-2018]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":213,"reference_id":"24899725","reference_source":"pmid","reference_html":"Regulation of the VHL/HIF-1 pathway by DJ-1. <i> Parsanejad M, Zhang Y, Qu D, Irrcher I, Rousseaux MW, Aleyasin H, Kamkar F, Callaghan S, Slack RS, Mak TW, Lee S, Figeys D, Park DS. </i> J Neurosci, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"Q99497","partner_start":null,"partner_end":null}],"region_id":"DP00287r051","statement":[{"text":"VHL was one of the baits and analysis of the dataset suggested DJ-1 as one of its interacting candidates with the interaction confidence score of 0.31 an unbiased mass spectrometry screen, which indicated Von Hippel Lindau (VHL) protein as a potential interacting partner.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-16T12:27:53.860Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":213,"reference_id":"23338840","reference_source":"pmid","reference_html":"The VHL tumor suppressor protein regulates tumorigenicity of U87-derived             glioma stem-like cells by inhibiting the JAK/STAT signaling pathway. <i> Kanno H, Sato H, Yokoyama TA, Yoshizumi T, Yamada S. </i> Int J Oncol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0008285","term_name":"negative regulation of cell population proliferation","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0001157","ec_ontology":"ECO","ec_name":"cell counting evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00287r052","statement":[{"text":"The results of the colony-formation assay in soft agar medium demonstrated significantly greater colony formation in the control vector-transfected compared to the VHL‑expressing vector-transfected U87 GSLCs. ","type":"Results"},{"text":"Neurosphere formation, which is a reflection of the self‑renewal ability, was also significantly greater in the former than in the latter (P<(B) Results for neurosphere formation. After one week, soft agar colony formation of VHL gene‑transfected GSLCs was significantly\ninhibited.0.001) ","type":"Results"},{"text":" (A) Results on soft agar colony formation by control-vector and VHL-vector GSLC transfectants. Colony formation by the VHL transfectants was significantly inhibited. / (B) Results for neurosphere formation. After one week, soft agar colony formation of VHL gene‑transfected GSLCs was significantly inhibited.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-14T09:32:14.439Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that stops, prevents or reduces the rate or extent of cell proliferation.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":213,"reference_id":"23338840","reference_source":"pmid","reference_html":"The VHL tumor suppressor protein regulates tumorigenicity of U87-derived             glioma stem-like cells by inhibiting the JAK/STAT signaling pathway. <i> Kanno H, Sato H, Yokoyama TA, Yoshizumi T, Yamada S. </i> Int J Oncol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0008285","term_name":"negative regulation of cell population proliferation","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0007696","ec_ontology":"ECO","ec_name":"cell proliferation assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00287r053","statement":[{"text":"Proliferation of control vector-transfected U87 GSLCs was significantly more pronounced compared to the VHL gene-transfected GSLCs 7 days following transfection (P<0.01) (Fig. 4C), although the difference between them was smaller than in the case of the soft agar colony or neurosphere formation assay. ","type":"Results"},{"text":"(C) Results of cell-proliferation assay. After 7 days, control gene-transfected GSLCs showed significantly greater proliferation than the VHL gene-transfected GSLCs (P<0.01). * P<0.01, ** P<0.0","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-01-18T13:46:10.146Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that stops, prevents or reduces the rate or extent of cell proliferation.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":213,"reference_id":"23338840","reference_source":"pmid","reference_html":"The VHL tumor suppressor protein regulates tumorigenicity of U87-derived             glioma stem-like cells by inhibiting the JAK/STAT signaling pathway. <i> Kanno H, Sato H, Yokoyama TA, Yoshizumi T, Yamada S. </i> Int J Oncol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0009968","term_name":"negative regulation of signal transduction","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0001186","ec_ontology":"ECO","ec_name":"immunocytochemistry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00287r054","statement":[{"text":"These results suggest that VHL affected the JAK̸/STAT pathway as well as the PTEN/PI3K/Akt pathway; they also suggest that upregulation of PTEN by VHL gene transfer may affect the PI3K/Akt pathway, since PTEN is a PI3K/Akt pathway inhibitor","type":"Discussion"},{"text":"(A) Immunoreactivity rates for control-vector and VHL-vector glioma stem-like cell (GSLC) transfectants are shown. Expressions of CD133, STAT3,\nJAK2 and Elongin A were significantly inhibited, whereas those of VHL and PTEN were significantly increased in VHL-transfectant GSLCs compared to\nthe control cells. Expressions of GFAP, NeuroD and MAP2 were not significantly altered. * P<0.05, ** P<0.01.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-16T12:30:12.686Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction.\" [GOC:sm]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":97,"end":102,"reference_id":"30902965","reference_source":"pmid","reference_html":"Ubiquitination of MAP1LC3B by pVHL is associated with autophagy and cell death in renal cell carcinoma. <i> Kang HM, Noh KH, Chang TK, Park D, Cho HS, Lim JH, Jung CR. </i> Cell Death Dis, 2019","date":"2022-06-19T14:48:41.070Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_06","version":2,"ec_go":"IMP","region_id":"DP00287r055","statement":[{"text":"To determine whether the LIR motif of VHL specifically binds to LC3B, we generated point mutants of the VHL LIR motif (VHL-Y98H; VHL-L101A; VHL-Y98H and L101A, a double point mutant containing Y98H and L101A) using site-directed mutagenesis. Wild-type or mutant VHL and Flag-tagged LC3B were expressed, purified from Escherichia coli, and used in in vitro binding assay with the indicated proteins. Results show that the L101A mutation completely prevented the interaction between VHL and LC3B, whereas the histidine mutation at tyrosine 98 had no effect (Fig. 3g).","type":"Results"},{"text":"Taken together, the N-terminal LC3B and LIR motif of VHL interacted directly both in vitro and in vivo.","type":"Results"},{"text":"The annotated region includes the canonical LIR motif (YPTL) at positions 98-101.","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-25T07:55:37.748Z"}},{"start":97,"end":102,"reference_id":"30902965","reference_source":"pmid","reference_html":"Ubiquitination of MAP1LC3B by pVHL is associated with autophagy and cell death in renal cell carcinoma. <i> Kang HM, Noh KH, Chang TK, Park D, Cho HS, Lim JH, Jung CR. </i> Cell Death Dis, 2019","date":"2022-06-19T14:47:51.317Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_06","version":2,"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q9GZQ8","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00287r056","statement":[{"text":"To determine whether the LIR motif of VHL specifically binds to LC3B, we generated point mutants of the VHL LIR motif (VHL-Y98H; VHL-L101A; VHL-Y98H and L101A, a double point mutant containing Y98H and L101A) using site-directed mutagenesis. Wild-type or mutant VHL and Flag-tagged LC3B were expressed, purified from Escherichia coli, and used in in vitro binding assay with the indicated proteins. Results show that the L101A mutation completely prevented the interaction between VHL and LC3B, whereas the histidine mutation at tyrosine 98 had no effect (Fig. 3g).","type":"Results"},{"text":"Taken together, the N-terminal LC3B and LIR motif of VHL interacted directly both in vitro and in vivo.","type":"Results"},{"text":"VHL directly binds to LC3B, the major marker of autophagy.","type":"Results"},{"text":"The annotated region includes the canonical LIR motif (YPTL) at positions 98-101.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-25T07:56:11.221Z"}},{"start":97,"end":102,"reference_id":"30902965","reference_source":"pmid","reference_html":"Ubiquitination of MAP1LC3B by pVHL is associated with autophagy and cell death in renal cell carcinoma. <i> Kang HM, Noh KH, Chang TK, Park D, Cho HS, Lim JH, Jung CR. </i> Cell Death Dis, 2019","date":"2022-05-31T13:34:35.696Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005601","ec_ontology":"ECO","ec_name":"immunofluorescence confocal microscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"Q9GZQ8","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00287r057","statement":[{"text":"Taken together, the N-terminal LC3B and LIR motif of VHL interacted directly both in vitro and in vivo.","type":"Results"},{"text":"VHL directly binds to LC3B, the major marker of autophagy.","type":"Results"},{"text":"We observed that LC3B co-localized with VHL in the cytosol (Fig. 3b). To determine the region of LC3B that binds to VHL, various truncations of LC3B were generated based on the sequence of the N-terminally Flag-tagged wild-type LC3B.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-05-31T13:42:49.245Z"}},{"start":97,"end":102,"reference_id":"30902965","reference_source":"pmid","reference_html":"Ubiquitination of MAP1LC3B by pVHL is associated with autophagy and cell death in renal cell carcinoma. <i> Kang HM, Noh KH, Chang TK, Park D, Cho HS, Lim JH, Jung CR. </i> Cell Death Dis, 2019","date":"2022-05-31T13:37:31.650Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0010507","term_name":"negative regulation of autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007718","ec_ontology":"ECO","ec_name":"ubiquitination assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IDA","region_id":"DP00287r058","statement":[{"text":"In conclusion, our results showed that pVHL interacts with MAPL1LC3B and inhibits LC3B-mediated autophagy via MAP1LC3B ubiquitination. Furthermore, the activation of autophagy by the proteasome inhibitor MLN9708 induced cell death, indicating that MLN9708 can be used for VHL-deficient RCC therapy.","type":"Abstract"},{"text":"Polyubiquitination of LC3B is induced by the VHL E3 ubiquitin ligase.","type":"Figure"},{"text":"We performed an in vitro ubiquitination assay using each indicated protein and an ATP-regeneration system. We observed that LC3B was polyubiquitinated by the VHL E3 ubiquitin complex in a time-dependent manner (Fig. 4b) and was subsequently degraded via the proteasome.","type":"Results"}],"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.\" [GOC:dph, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-05-31T13:42:46.538Z"}},{"start":97,"end":102,"reference_id":"30902965","reference_source":"pmid","reference_html":"Ubiquitination of MAP1LC3B by pVHL is associated with autophagy and cell death in renal cell carcinoma. <i> Kang HM, Noh KH, Chang TK, Park D, Cho HS, Lim JH, Jung CR. </i> Cell Death Dis, 2019","date":"2022-05-31T13:38:59.167Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0010507","term_name":"negative regulation of autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005601","ec_ontology":"ECO","ec_name":"immunofluorescence confocal microscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IDA","region_id":"DP00287r059","statement":[{"text":"In conclusion, our results showed that pVHL interacts with MAPL1LC3B and inhibits LC3B-mediated autophagy via MAP1LC3B ubiquitination. Furthermore, the activation of autophagy by the proteasome inhibitor MLN9708 induced cell death, indicating that MLN9708 can be used for VHL-deficient RCC therapy.","type":"Abstract"},{"text":"Polyubiquitination of LC3B is induced by the VHL E3 ubiquitin ligase.","type":"Figure"},{"text":"Immunofluorescence staining was performed to identify the localization of LC3B and the 28S proteasome in cells with respect to VHL expression. Results show that Flag-LC3B and the 28S proteasome proteins co-localized more in VHL-deficient 786-o cells than in 786-o cells stably expressing VHL (Fig. 4f). This indicated that VHL ubiquitinated the N-terminal region (1−162 amino acids) of LC3B, and the leucine 101 in the LIR motif of VHL is essential for LC3B ubiquitination. ","type":"Results"}],"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.\" [GOC:dph, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-05-31T13:42:37.775Z"}},{"start":54,"end":157,"reference_id":"28425505","reference_source":"pmid","reference_html":"Novel interactions of the von Hippel-Lindau (pVHL) tumor suppressor with the CDKN1 family of cell cycle inhibitors. <i> Minervini G, Lopreiato R, Bortolotto R, Falconieri A, Sartori G, Tosatto SCE. </i> Sci Rep, 2017","date":"2024-09-11T14:36:25.762Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005805","ec_ontology":"ECO","ec_name":"yeast 2-hybrid evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P46527","operator":null,"partner_start":1,"partner_end":60},{"db":"UniProt","id":"P38936","operator":"and","partner_start":1,"partner_end":49},{"db":"UniProt","id":"P49918","operator":"and","partner_start":1,"partner_end":61}],"region_id":"DP00287r060","statement":[{"text":"The pVHL β-domain is able to bind any member of the CDKN1 family, as indicated by yeast cell growth (Fig. 4B, Supplementary Figures S5 and S7). ","type":"Results"},{"text":"Yeast plasmids expressing either their N-terminal tail containing the CDI domain (p27-NT residues: 1–60; p21-NT: 1–49; p57-NT: 1–61) or the corresponding C-terminal moiety lacking the N-terminus (p27-ΔN residues: 61–198; p21-ΔN: 50–164; p57-ΔN: 62–316) were generated to test the effects of CDKN1 binding to pVHL30. As shown in Fig. 4D, loss of the p27 N-terminus clearly disrupts its ability to associate with pVHL30, as yeast cells expressing the C-terminus of p27 were all unable to grow in selective medium. Similar data have been also obtained for both p21 and p57 (Supplementary Figures S9 and S10), strongly supporting the notion that the CDI domain is responsible for CDKN1 binding to pVHL30.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"cross_refs":[{"db":"DisProt","id":"DP00016r041"},{"db":"DisProt","id":"DP00018r056"},{"db":"DisProt","id":"DP00017r018"}],"construct_alterations":[{"term_id":"MI:0693","term_name":"Gal4 DNA-binding domain tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-18T10:50:11.617Z"}},{"start":1,"end":213,"reference_id":"28425505","reference_source":"pmid","reference_html":"Novel interactions of the von Hippel-Lindau (pVHL) tumor suppressor with the CDKN1 family of cell cycle inhibitors. <i> Minervini G, Lopreiato R, Bortolotto R, Falconieri A, Sartori G, Tosatto SCE. </i> Sci Rep, 2017","date":"2024-08-05T12:50:28.698Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0520","term_name":"HA","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"For each transfection, approximatively 5 μg of total DNA, i.e. pcDNA3.1-derived plasmids (empty, and/or expressing either HA-pVHL30 or FLAG-CDKN1) were used."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P38936","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P46527","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P49918","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP00287r063","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"Our data (Fig. 2B) indicates that all three CDKN1 proteins were able to interact with pVHL30, as demonstrated by their presence in the immunoprecipitate revealed with the anti-Flag antibody (bottom panels). Taken together, the experiments show that these proteins can form at least binary complexes in human, and notably kidney cells.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"cross_refs":[{"db":"DisProt","id":"DP00018r057"},{"db":"DisProt","id":"DP00017r019"},{"db":"DisProt","id":"DP00016r042"}]},{"start":1,"end":213,"reference_id":"28425505","reference_source":"pmid","reference_html":"Novel interactions of the von Hippel-Lindau (pVHL) tumor suppressor with the CDKN1 family of cell cycle inhibitors. <i> Minervini G, Lopreiato R, Bortolotto R, Falconieri A, Sartori G, Tosatto SCE. </i> Sci Rep, 2017","date":"2024-08-02T14:57:20.062Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140297","term_name":"DNA-binding transcription factor binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005805","ec_ontology":"ECO","ec_name":"yeast 2-hybrid evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0693","term_name":"Gal4 DNA-binding domain tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"All recombinant plasmids used in the yeast two-hybrid assays (Supplementary Table S1) are able to express the proteins of interest in fusion with either the DNA binding domain (DBD) or the activation domain (AD) of the Gal4 transcription factor."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q16665","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00287r064","statement":[{"text":"Expression in yeast cells of the Gal4-fusion proteins has been checked by Western blot analysis (Supplementary Figure S15), while the functional status of pVHL was verified testing the well-known pVHL/HIF-1α interaction with and without co-expressing PHD3 (Supplementary Figure S16).","type":"Methods"}],"term_comment":"","term_def":"\"Binding to a DNA-binding transcription factor, a protein that interacts with a specific DNA sequence (sometimes referred to as a motif) within the regulatory region of a gene to modulate transcription.\" [GOC:txnOH-2018]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":213,"reference_id":"23785518","reference_source":"pmid","reference_html":"Identification of pVHL as a novel substrate for Aurora-A in clear cell renal cell carcinoma (ccRCC). <i> Martin B, Chesnel F, Delcros JG, Jouan F, Couturier A, Dugay F, Le Goff X, Patard JJ, Fergelot P, Vigneau C, Rioux-Leclerq N, Arlot-Bonnemains Y. </i> PLoS One, 2013","date":"2024-08-05T14:21:51.023Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0120283","term_name":"protein serine/threonine kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"O14965","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00287r065","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"},{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0498","entry_name":"RCC-4"},{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_1051","entry_name":"786-O RCC"}],"statement":[{"text":"As Aurora-A was co-immunoprecipitated with pVHL in all three cell lines (Figure 4C), we then asked whether pVHL was a phosphorylation substrate of Aurora-A.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein serine/threonine kinase.\" [GOC:krc, GOC:sl, PMID:28608965]","term_is_obsolete":false,"term_not_annotate":false},{"start":70,"end":74,"reference_id":"23785518","reference_source":"pmid","reference_html":"Identification of pVHL as a novel substrate for Aurora-A in clear cell renal cell carcinoma (ccRCC). <i> Martin B, Chesnel F, Delcros JG, Jouan F, Couturier A, Dugay F, Le Goff X, Patard JJ, Fergelot P, Vigneau C, Rioux-Leclerq N, Arlot-Bonnemains Y. </i> PLoS One, 2013","date":"2024-08-08T08:41:14.782Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser72Ala","start":null,"end":null,"position":null}],"region_id":"DP00287r067","statement":[{"text":"This annotation refers to the phosphorylation of the Ser 72 residue of VHL protein by human Aurora kinase A.","type":"Curator statement"},{"text":"Mutation of Ser72 into alanine (VHL SA72) greatly diminished phosphorylation of pVHL by Aurora-A (Figure 5, lane 2).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-03T14:46:26.533Z"}}],"released":"2016_10","uniref100":"UniRef100_P40337","date":"2016-08-24T15:23:56.000Z","acc":"P40337","name":"von Hippel-Lindau disease tumor suppressor","length":213,"organism":"Homo sapiens","dataset":["Cancer-related proteins","Autophagy-related proteins","Condensates-related proteins","Stress response proteins"],"UniParc":"UPI0000146537","genes":[{"name":{"value":"VHL"}}],"alphafold_very_low_content":0.1267605633802817,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":213,"type":"D"}],"Structural state":[{"start":1,"end":213,"type":"D"}],"Molecular function":[{"start":1,"end":213,"type":"F"}],"Biological process":[{"start":1,"end":213,"type":"F"}],"Disorder function":[{"start":70,"end":74,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02604","name":"Antitoxin Phd_YefM, type II toxin-antitoxin system","start":1,"end":51}],"gene3D":[{"start":1,"end":49,"id":"3.40.1620.10","name":"YefM-like domain"}]},"uniref50":"UniRef50_Q06253","sequence":"MQSINFRTARGNLSEVLNNVEAGEEVEITRRGREPAVIVSKATFEAYKKAALDAEFASLFDTLDSTNKELVNR","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Uroviricota","Caudoviricetes","Caudovirales","Myoviridae","Punavirus"],"uniref90":"UniRef90_Q06253","disprot_id":"DP00288","dataset":["Unicellular toxins and antitoxins","Viral proteins"],"ncbi_taxon_id":10678,"regions_counter":51,"creator":"bhajdu","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":73,"region_id":"DP00288r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Doc of prophage P1 is inhibited by its antitoxin partner Phd through fold complementation. <i> Garcia-Pino A, Christensen-Dalsgaard M, Wyns L, Yarmolinsky M, Magnuson RD, Gerdes K, Loris R. </i> J Biol Chem, 2008","statement":[{"text":"Far UV CD experiments show that Phd52–73Se is intrinsically unstructured in its isolated state but gains an appreciable amount of α-helix upon binding to Doc (Fig. 3).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jbergier","start":52,"term_ontology":"IDPO","curator_name":"Julian Bergier","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":5,"curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18757857","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T09:59:06.223Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":73,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Doc of prophage P1 is inhibited by its antitoxin partner Phd through fold complementation. <i> Garcia-Pino A, Christensen-Dalsgaard M, Wyns L, Yarmolinsky M, Magnuson RD, Gerdes K, Loris R. </i> J Biol Chem, 2008","statement":[{"text":"Far UV CD experiments show that Phd52–73Se is intrinsically unstructured in its isolated state but gains an appreciable amount of α-helix upon binding to Doc (Fig. 3).","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"jbergier","start":52,"term_ontology":"IDPO","curator_name":"Julian Bergier","reference_id":"18757857","version":5,"curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00288r003","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T10:00:34.839Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00288r004","validated":{"curator_id":"fquaglia","timestamp":"2020-12-12T22:15:07.880Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":73,"ec_name":"far-UV circular dichroism evidence used in manual assertion","start":52,"version":5,"statement":[{"text":"The action of Doc is suppressed by the antitoxin Phd, which consists of two domains. Its C-terminal domain (residues 52–73) harbors the interaction site with Doc and on its own prevents Doc-mediated growth arrest","type":"Introduction"},{"text":"Far UV CD experiments show that Phd52–73Se is intrinsically unstructured in its isolated state but gains an appreciable amount of α-helix upon binding to Doc (Fig. 3).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q06259","partner_end":null}],"term_name":"protein binding","reference_html":"Doc of prophage P1 is inhibited by its antitoxin partner Phd through fold complementation. <i> Garcia-Pino A, Christensen-Dalsgaard M, Wyns L, Yarmolinsky M, Magnuson RD, Gerdes K, Loris R. </i> J Biol Chem, 2008","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"18757857","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006204","curator_id":"bmesza","curator_orcid":"0000-0003-0919-4449","term_id":"GO:0005515","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":73,"region_id":"DP00288r009","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","statement":[{"text":"The plateau at I(s)s2 > 0 observed in the Kratky plot (Figure 1D) indicates that Phd is partially unstructured (Pollack et al., 1999; Porod, 1982), in agreement with earlier circular dichroism (CD) studies (Gazit and Sauer, 1999).","type":"Results"},{"text":" Using the ensemble optimization method (EOM) (Bernado et al., 2007), we find that the scattering curve can be modeled assuming a fixed conformation for residues 1–40 of Phd and a wide structural ensemble for residues 41–73 (c2 = 0.8, Figure 1D, Table S1). ","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jbergier","start":41,"term_ontology":"IDPO","curator_name":"Julian Bergier","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":4,"curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20603017","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T09:58:28.280Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":73,"region_id":"DP00288r013","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Stability and DNA binding of the phd protein of the phage P1 plasmid addiction system. <i> Gazit E, Sauer RT. </i> J Biol Chem, 1999","statement":[{"text":"The amount of secondary structure was estimated from the CD spectrum (20, 21). At 37 °C in buffer alone, Phd seems to be in a largely unfolded, random-coil conformation. However, at 4 °C or at 37 °C in the presence of trimethylamine N-oxide, Phd has a CD spectra indicative of a folded protein containing approximately 45% a-helix (Fig. 1A).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jbergier","start":1,"term_ontology":"IDPO","curator_name":"Julian Bergier","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":4,"curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"9915794","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T09:56:40.756Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":73,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Stability and DNA binding of the phd protein of the phage P1 plasmid addiction system. <i> Gazit E, Sauer RT. </i> J Biol Chem, 1999","statement":[{"text":"DNA binding induces a dose-dependent increase in Phd structure, suggesting that the folding and site-specific DNA binding of Phd are coupled.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"bmesza","start":1,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"9915794","version":3,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","validated":{"curator_id":"fquaglia","timestamp":"2020-12-12T22:10:35.514Z","curator_name":"Federica Quaglia"},"region_id":"DP00288r014","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00288r016","validated":{"curator_id":"fquaglia","timestamp":"2020-12-12T22:14:55.890Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":73,"ec_name":"far-UV circular dichroism evidence used in manual assertion","start":1,"version":4,"statement":[{"text":"The slope of the initial part of the titration curve shows that the amount of operator DNA needed for induction of fully folded Phd is roughly one-quarter of the protein concentration, suggesting that Phd binds to its operator DNA as a tetramer.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q06253","partner_end":null}],"term_name":"protein binding","reference_html":"Stability and DNA binding of the phd protein of the phage P1 plasmid addiction system. <i> Gazit E, Sauer RT. </i> J Biol Chem, 1999","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"9915794","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006204","curator_id":"bmesza","curator_orcid":"0000-0003-0919-4449","term_id":"GO:0005515","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00288r025","ec_ontology":"ECO","end":73,"term_id":"GO:0001217","start":1,"version":4,"statement":[{"text":"Fig. 5,A and B, show a gel-mobility-shift assay of Phd binding to DNA fragments containing the left and the right operator subsites, respectively. The assays were performed using a DNA concentration low enough (10 pM) to allow the reaction mechanism to be deduced from the dependence of binding on Phd concentration and an equilibrium dissociation constant to be calculated. Two observations suggest that two Phd monomers bind cooperatively to subsite DNA.","type":"Results"}],"term_name":"DNA-binding transcription repressor activity","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","curator_orcid":"0000-0002-5152-5953","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"9915794","date":"2022-03-08T15:25:53.764Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001807","curator_id":"esalladini","reference_html":"Stability and DNA binding of the phd protein of the phage P1 plasmid addiction system. <i> Gazit E, Sauer RT. </i> J Biol Chem, 1999","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"For usage guidance, see comment in GO:0003700 ; DNA-binding transcription factor activity.","term_def":"\"A DNA-binding transcription factor activity that represses or decreases the transcription of specific gene sets.\" [GOC:txnOH-2018]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"NCBIgene","id":"2777473","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-21T15:49:33.408Z"}},{"region_id":"DP00288r026","validated":{"curator_id":"fquaglia","timestamp":"2020-12-12T22:16:52.944Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":73,"term_id":"GO:0001217","start":1,"version":3,"statement":[{"text":"DNA binding induces a dose-dependent increase in Phd structure, suggesting that the folding and site-specific DNA binding of Phd are coupled.","type":"Results"}],"term_name":"DNA-binding transcription repressor activity","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"9915794","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006204","curator_id":"bmesza","reference_html":"Stability and DNA binding of the phd protein of the phage P1 plasmid addiction system. <i> Gazit E, Sauer RT. </i> J Biol Chem, 1999","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"For usage guidance, see comment in GO:0003700 ; DNA-binding transcription factor activity.","term_def":"\"A DNA-binding transcription factor activity that represses or decreases the transcription of specific gene sets.\" [GOC:txnOH-2018]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00288r027","validated":{"curator_id":"fquaglia","timestamp":"2020-12-12T22:02:59.795Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":57,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"When attempting to probe the flexibility of Phd1–57 with hydrogen-deuterium exchange experiments, virtually all amide protons exchange within the set-up time (∼11 min) prior to the start of NMR acquisition, and their 1H-15N cross-peaks are therefore absent in the HSQC spectrum. Such dramatic behavior indicates very low stability and lack of conformational rigidity and is presumably the result of a high overall conformational exchange of Phd between folded and partially folded states (See Extended Experimental Procedures for further details).","type":"Results"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"20603017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006196","curator_id":"bmesza","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00288r028","validated":{"curator_id":"fquaglia","timestamp":"2020-12-12T22:02:31.599Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":57,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"We used NMR to characterize the structure of the N-terminal domain of Phd (Phd1–57—residues 1–57) in solution. This N-terminal domain of Phd examined by two-dimensional (2D) 1H-15N HSQC NMR is in agreement with a conformationally heterogeneous protein that populates folded and disordered states (Figure S1F, in cyan).","type":"Results"},{"text":"Given the expected elevated conformational heterogeneity of Phd1–57, the 15N transverse and longitudinal relaxation rates (R2 and R1) are the best indicators to probe the state of the Phd1–57 ensemble in solution. Figure 1E shows the R2/R1 ratios along the Phd1–57 sequence (represented as red bars). Two regions show significantly high R2/R1 ratios as a result of elevated R2 rates, indicative of a pronounced conformational freedom and high exchange between different conformational states in the μs to ms timescale. Additionally the C-terminal region displays pronounced low R2/R1 ratios, which indicate an increase in fast dynamics (i.e., high degree of flexibility) in agreement with the heteronuclear NOE values found for this region of the domain (Figure S1G).","type":"Results"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"20603017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"bmesza","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00288r029","ec_ontology":"ECO","end":73,"term_id":"IDPO:0000002","start":1,"version":3,"statement":[{"text":"In its unbound state Phd is only marginally stable (Figure 2B). ","type":"Results"},{"text":"This indicates a poorly structured unfolding unit, suggesting that, in agreement with the NMR data, the partly unfolded species dominates in solution.","type":"Results"}],"term_name":"disorder","ec_name":"differential scanning calorimetry evidence used in manual assertion","curator_orcid":"0000-0003-2206-9968","released":"2022_03","term_ontology":"IDPO","curator_name":"Julian Bergier","reference_id":"20603017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006232","curator_id":"jbergier","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T09:55:13.932Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP00288r030","validated":{"curator_id":"fquaglia","timestamp":"2020-12-12T22:11:27.406Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":57,"term_id":"IDPO:0000011","start":1,"version":2,"statement":[{"text":"Differential scanning calorimetry (DSC) unfolding data of Phd and its N-terminal fragment Phd1–57 fit well to a two-state model consisting of a dimer unfolding into monomer species. In its unbound state Phd is only marginally stable (Figure 2B). ","type":"Results"}],"term_name":"disorder to order","ec_name":"differential scanning calorimetry evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"20603017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural transition","ec_id":"ECO:0006232","curator_id":"bmesza","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","ec_go":"IDA","disprot_namespace":"Structural transition"},{"region_id":"DP00288r031","validated":{"curator_id":"fquaglia","timestamp":"2020-12-12T22:17:02.676Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":57,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"Differential scanning calorimetry (DSC) unfolding data of Phd and its N-terminal fragment Phd1–57 fit well to a two-state model consisting of a dimer unfolding into monomer species. In its unbound state Phd is only marginally stable (Figure 2B). ","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q06253","partner_end":null}],"term_name":"protein binding","ec_name":"differential scanning calorimetry evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"20603017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006232","curator_id":"bmesza","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00288r032","validated":{"curator_id":"fquaglia","timestamp":"2020-12-12T22:17:33.076Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":73,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"Our DSC measurements show that binding of DNA or of its toxin partner Doc to Phd significantly increases its thermodynamic stability (Figure 2B, Figure S2C, and Table S2). In both cases the increment in the conformational stability is accompanied by a large increase in the heat of unfolding and the melting temperature of Phd.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q06259","partner_end":null}],"term_name":"protein binding","ec_name":"differential scanning calorimetry evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"20603017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006232","curator_id":"bmesza","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00288r033","validated":{"curator_id":"fquaglia","timestamp":"2020-12-12T22:18:03.487Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":73,"term_id":"GO:0003677","start":1,"version":3,"statement":[{"text":"Our DSC measurements show that binding of DNA or of its toxin partner Doc to Phd significantly increases its thermodynamic stability (Figure 2B, Figure S2C, and Table S2). In both cases the increment in the conformational stability is accompanied by a large increase in the heat of unfolding and the melting temperature of Phd.","type":"Results"}],"term_name":"DNA binding","ec_name":"differential scanning calorimetry evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"20603017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006232","curator_id":"bmesza","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00288r034","validated":{"curator_id":"fquaglia","timestamp":"2020-12-12T22:18:10.072Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":73,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"The effect of Doc on the affinity of Phd for a single DNA-binding site (OR1) was quantified using isothermal titration calorimetry (ITC). The affinity of Phd2Doc for OR1 is 0.3 μM, about 10-fold higher than the binding constant of Phd2 for OR1 (Figures 3D and 3E; Table S4). ","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q06259","partner_end":null}],"term_name":"protein binding","ec_name":"isothermal titration calorimetry evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"20603017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"bmesza","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00288r035","ec_ontology":"ECO","end":73,"term_id":"GO:0003677","start":1,"version":4,"statement":[{"text":"The effect of Doc on the affinity of Phd for a single DNA-binding site (OR1) was quantified using isothermal titration calorimetry (ITC). The affinity of Phd2Doc for OR1 is 0.3 μM, about 10-fold higher than the binding constant of Phd2 for OR1 (Figures 3D and 3E; Table S4). ","type":"Results"}],"term_name":"DNA binding","ec_name":"isothermal titration calorimetry evidence used in manual assertion","curator_orcid":"0000-0002-5152-5953","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"20603017","date":"2022-03-08T15:25:43.156Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"esalladini","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"NCBIgene","id":"2777473","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-21T15:49:30.713Z"}},{"region_id":"DP00288r036","validated":{"curator_id":"fquaglia","timestamp":"2020-12-12T22:19:06.931Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":58,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"Phd crystallizes in two different crystal forms. Form I contains a version of the protein that is truncated at Ser58 (hereafter termed Phd1–57). All four molecules in the asymmetric unit adopt a similar, well-folded conformation encompassing Met1-Phe56. This N-terminal domain forms a small globular homodimer comprising a central six-stranded β sheet decorated with four α helices (two from each monomer), resembling the antitoxin YefM (Kamada and Hanaoka, 2005\n) (Figure 1A ; Figure S1A available online). The N-terminal α helices α1 and α2 form a large positively charged surface that constitutes the DNA-binding region (Figure S1B). The dimer interface is relatively small (about 900 Å2 of water accessible surface buried per dimer).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q06253","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"20603017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3HS2"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"bmesza","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00288r037","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T16:43:52.102Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":58,"term_id":"IDPO:0000011","start":1,"version":3,"statement":[{"text":"Phd crystallizes in two different crystal forms. Form I contains a version of the protein that is truncated at Ser58 (hereafter termed Phd1–57). All four molecules in the asymmetric unit adopt a similar, well-folded conformation encompassing Met1-Phe56. This N-terminal domain forms a small globular homodimer comprising a central six-stranded β sheet decorated with four α helices (two from each monomer), resembling the antitoxin YefM (Kamada and Hanaoka, 2005) (Figure 1A ; Figure S1A available online). The N-terminal α helices α1 and α2 form a large positively charged surface that constitutes the DNA-binding region (Figure S1B). The dimer interface is relatively small (about 900 Å2 of water accessible surface buried per dimer).","type":"Results"},{"text":"In this case the disordered nature of the quoted region does not (only) come from missing residues but also from the large differences between the coordinates of the various copies of the protein in the crystal. This shows that some residues have resolved coordinates only because of crystal contacts, and these have been annotated as disordered as well (in line with the authors' assertion).","type":"Curator statement"}],"term_name":"disorder to order","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"20603017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3HS2"}],"term_namespace":"Structural transition","ec_id":"ECO:0005670","curator_id":"rpancsa","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00288r038","ec_ontology":"ECO","end":73,"term_id":"GO:0005515","start":56,"version":4,"statement":[{"text":"About 25% of the surface of Doc is buried upon interacting with two Phd dimers (Figure 4B). Site H corresponds to the one identified earlier in the crystal structure of a nontoxic mutant of Doc (Garcia-Pino et al., 2008) and recognizes the Phd segment Phe56-Arg73.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q06259","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-2206-9968","released":"2022_03","term_ontology":"GO","curator_name":"Julian Bergier","reference_id":"20603017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3K33"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"jbergier","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T10:01:09.289Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00288r039","validated":{"curator_id":"fquaglia","timestamp":"2020-12-12T22:13:34.644Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":73,"term_id":"IDPO:0000011","start":1,"version":2,"statement":[{"text":"The asymmetric unit of our Phd/Doc cocrystals contains three copies of Phd and one copy of Doc, which through crystal symmetry form a hetero-octameric Phd2-Doc-Phd2-Doc-Phd2 complex (Figure 4A ; Figure S4A).","type":"Results"},{"text":"While the authors do not explicitly state this, the structured state of phd becomes evident when looking at the corresponding complex structure in PDB:3k33.","type":"Curator statement"}],"term_name":"disorder to order","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"20603017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3K33"}],"term_namespace":"Structural transition","ec_id":"ECO:0005670","curator_id":"bmesza","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00288r040","validated":{"curator_id":"fquaglia","timestamp":"2020-12-12T22:19:58.577Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":73,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"Using surface plasmon resonance (SPR), we measured the binding kinetics and affinities for both interaction modes between Phd and Doc (Figure 2C). Consistent with the crystal structure of the complex, the best model that explains the binding data involves two Phd dimers binding to a Doc monomer with affinities of 0.35 μM and 31 μM (Figure 2C; Table S4). ","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q06259","partner_end":null}],"term_name":"protein binding","ec_name":"surface plasmon resonance evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"20603017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001269","curator_id":"bmesza","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00288r041","validated":{"curator_id":"fquaglia","timestamp":"2020-12-12T22:20:05.882Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":73,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"Doc modulates the affinity of Phd for the operator region of the operon as observed in electrophoretic mobility shift assays (Figure 3B). At increasing Doc:Phd ratios between 0 and 1, the band corresponding to unbound DNA disappears and a series of distinct bands appear that we interpret in terms of Phd/Doc/DNA complexes of variable stoichiometry. A first Doc molecule will bridge the two Phd dimers bound to their two sites on the operator DNA and increase affinity through an avidity effect. This interaction will recruit both the high- and low-affinity sites on Doc. A second and third Doc molecule will bind through their high-affinity sites on the two free Phd C termini of the DNA-bound Phd2-Doc-Phd2 complex, resulting in a Doc-Phd2-Doc-Phd2-Doc operator DNA complex.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q06259","partner_end":null}],"term_name":"protein binding","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"20603017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001807","curator_id":"bmesza","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00288r042","ec_ontology":"ECO","end":73,"term_id":"GO:0003677","start":1,"version":4,"statement":[{"text":"Doc modulates the affinity of Phd for the operator region of the operon as observed in electrophoretic mobility shift assays (Figure 3B). At increasing Doc:Phd ratios between 0 and 1, the band corresponding to unbound DNA disappears and a series of distinct bands appear that we interpret in terms of Phd/Doc/DNA complexes of variable stoichiometry. A first Doc molecule will bridge the two Phd dimers bound to their two sites on the operator DNA and increase affinity through an avidity effect. This interaction will recruit both the high- and low-affinity sites on Doc. A second and third Doc molecule will bind through their high-affinity sites on the two free Phd C termini of the DNA-bound Phd2-Doc-Phd2 complex, resulting in a Doc-Phd2-Doc-Phd2-Doc operator DNA complex.","type":"Results"}],"term_name":"DNA binding","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","curator_orcid":"0000-0002-5152-5953","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"20603017","date":"2022-03-08T15:25:04.722Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001807","curator_id":"esalladini","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"NCBIgene","id":"2777473","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-21T15:49:29.743Z"}},{"region_id":"DP00288r043","validated":{"curator_id":"fquaglia","timestamp":"2020-12-12T22:20:58.573Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":73,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"Our mechanistic model for conditional cooperativity predicts that at saturating levels of Doc, a Doc-Phd2-Doc heterotetrameric complex that is far less capable of repressing the phd/doc operon is formed. We used SAXS to characterize this complex and examine its shape and dimensions. Based on our crystal structure, we constructed a series of alternative Phd/Doc complexes with different stoichiometries (including Phd2-Doc-Phd2, Doc-Phd2-Doc, and the two possible Phd2-Doc architectures). The comparison of the experimental scattering data to the calculated scattering curves derived from these models reveals a close correspondence only to the Doc-Phd2-Doc model and very poor fits to other architectures (Table S1). The Rg (27.5 Å) calculated from the Guinier analysis and the bimodal shape and maximum dimension of the particle (Dmax = 85 Å) obtained from the distance distribution function (P(r)) all agree with our V-shaped model of the Doc-Phd2-Doc complex. Moreover the P(r) function and Kratky plot are consistent with a properly folded, homogeneous, and well-structured species (Figures S4B–S4C).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q06259","partner_end":null}],"term_name":"protein binding","ec_name":"small-angle X-ray scattering evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"20603017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006210","curator_id":"bmesza","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00288r044","validated":{"curator_id":"fquaglia","timestamp":"2020-12-12T22:13:41.488Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":73,"term_id":"IDPO:0000011","start":1,"version":2,"statement":[{"text":"Our mechanistic model for conditional cooperativity predicts that at saturating levels of Doc, a Doc-Phd2-Doc heterotetrameric complex that is far less capable of repressing the phd/doc operon is formed. We used SAXS to characterize this complex and examine its shape and dimensions. Based on our crystal structure, we constructed a series of alternative Phd/Doc complexes with different stoichiometries (including Phd2-Doc-Phd2, Doc-Phd2-Doc, and the two possible Phd2-Doc architectures). The comparison of the experimental scattering data to the calculated scattering curves derived from these models reveals a close correspondence only to the Doc-Phd2-Doc model and very poor fits to other architectures (Table S1). The Rg (27.5 Å) calculated from the Guinier analysis and the bimodal shape and maximum dimension of the particle (Dmax = 85 Å) obtained from the distance distribution function (P(r)) all agree with our V-shaped model of the Doc-Phd2-Doc complex. Moreover the P(r) function and Kratky plot are consistent with a properly folded, homogeneous, and well-structured species (Figures S4B–S4C).","type":"Results"}],"term_name":"disorder to order","ec_name":"small-angle X-ray scattering evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"20603017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural transition","ec_id":"ECO:0006210","curator_id":"bmesza","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00288r045","validated":{"curator_id":"fquaglia","timestamp":"2020-12-12T22:22:45.240Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":73,"term_id":"GO:0097351","start":1,"version":3,"statement":[{"text":"We further validated the role of site L in autoregulation (again in a nontoxic DocH66Y background) in vivo using a lacZ repression assay and through an indirect toxicity assay that reports the presence of a functional site H (see Extended Experimental Procedures for details). Knocking out site L is expected to result in a Doc phenotype unable to act as corepressor but still capable of binding Phd through site H. As expected, most mutants (R31A, R31D, I35A, R38A, R38D, A61W, A61D, R64E, and R64W) show a decreased corepression activity (Figure 5B; Table S5), remaining, however, capable of displacing wild-type Doc from site H. This effect is severely marked for the mutants R38D and A61D (in agreement with our in vitro results). These site L mutants disrupt the interaction of Phd with Asp53 (in the case of the R38D mutation) or introduce a negative charge in the hydrophobic pocket that accommodates residues Phe56 and Phe60 of Phd (for A61D) and results in a complete loss of corepression. However, their ability to bind Phd through their H site remains intact (Figure 5C; Table S5). Thus the low-affinity interaction that is required to establish a Doc-bridge between two operator-bound Phd dimers is crucial for Doc-mediated enhancement of repression.","type":"Results"}],"term_name":"toxin sequestering activity","ec_name":"experimental phenotypic evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"20603017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0007634","curator_id":"bmesza","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a toxic protein, disabling its function. There may be more than one antitoxin to a toxic protein. Instances of this activity are known only in prokaryotes, where the toxic protein may be a ribonuclease, a DNA gyrase, or other.\" [GOC:rs, PMID:19143615, PMID:19325885, PMID:21819231, PMID:22545240, PMID:24806488, Wikipedia:Toxin-antitoxin_system#Type_II]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00288r046","validated":{"curator_id":"fquaglia","timestamp":"2020-12-12T22:22:24.647Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":73,"term_id":"GO:0005515","start":51,"version":3,"statement":[{"text":"DocH66Y was crystallized in complex with a peptide encompassing the C-terminal 22 amino acids of Phd with Se-Met substituted for Leu-52 and Leu-70 (Phd52–73Se). This fragment was chosen based upon previous work that delineates the toxin-binding domain of Phd (14, 15).","type":"Results"},{"text":"Phd52–73Se binds into a groove of DocH66Y of which helix α4 forms the base and that is flanked by helix α1 on one side and the loop α4-α5 on the other side (Fig. 1A).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q06259","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"18757857","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3dd7"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"bmesza","reference_html":"Doc of prophage P1 is inhibited by its antitoxin partner Phd through fold complementation. <i> Garcia-Pino A, Christensen-Dalsgaard M, Wyns L, Yarmolinsky M, Magnuson RD, Gerdes K, Loris R. </i> J Biol Chem, 2008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00288r047","ec_ontology":"ECO","end":73,"term_id":"IDPO:0000011","start":51,"version":3,"statement":[{"text":"The PDB shows the antitoxin phd ordered when is bound to Doc.","type":"Curator statement"}],"term_name":"disorder to order","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-2206-9968","released":"2022_03","term_ontology":"IDPO","curator_name":"Julian Bergier","reference_id":"18757857","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3DD7"}],"term_namespace":"Structural transition","ec_id":"ECO:0005670","curator_id":"jbergier","reference_html":"Doc of prophage P1 is inhibited by its antitoxin partner Phd through fold complementation. <i> Garcia-Pino A, Christensen-Dalsgaard M, Wyns L, Yarmolinsky M, Magnuson RD, Gerdes K, Loris R. </i> J Biol Chem, 2008","states_connection":[{"source":"DP00288r001","target":"DP00288r049"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T10:00:17.903Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00288r048","ec_ontology":"ECO","end":73,"term_id":"IDPO:0000002","start":58,"version":4,"statement":[{"text":"The C-terminal domain (Ala57-Arg73) of this dimer is also structured due to lattice interactions (Figure 1B; Figure S1D). The conformations adopted by the C terminus are distinct from each other and from the Doc-bound conformations (see below). They contain variable amounts of a helix and likely sample the conformational ensemble of the Phd C-terminal domain in solution.","type":"Results"},{"text":"In this case the disordered nature of the quoted region does not (only) come from missing residues but also from the large differences between the coordinates of the various copies of the protein in the crystal. This shows that some residues have resolved coordinates only because of crystal contacts, and these have been annotated as disordered as well (in line with the authors' assertion).","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-2206-9968","released":"2022_03","term_ontology":"IDPO","curator_name":"Julian Bergier","reference_id":"20603017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3HRY"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"jbergier","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T10:02:24.676Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":51,"end":73,"reference_id":"18757857","reference_source":"pmid","reference_html":"Doc of prophage P1 is inhibited by its antitoxin partner Phd through fold complementation. <i> Garcia-Pino A, Christensen-Dalsgaard M, Wyns L, Yarmolinsky M, Magnuson RD, Gerdes K, Loris R. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3DD7"}],"region_id":"DP00288r049","statement":[{"text":"The PDB shows the antitoxin phd ordered when is bound to Doc.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q06259"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T09:56:53.655Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":41,"end":57,"reference_id":"20603017","reference_source":"pmid","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3HS2"},{"db":"PDB","id":"3HRY"}],"region_id":"DP00288r050","statement":[{"text":"More significantly, when we map the R2/R1 data on the X-ray structure of Phd (Figure 1F), the “dynamic hot spots” correspond to α helices α2 and α3, two regions that lose structure in the partially disordered conformation observed in the X-ray structure.","type":"Results"},{"text":"This region corresponds to α helix 3.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T09:59:53.298Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":1,"end":73,"reference_id":"20603017","reference_source":"pmid","reference_html":"Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. <i> Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, Magnuson RD, Charlier D, van Nuland NA, Loris R. </i> Cell, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"GO:0045892","term_name":"negative regulation of transcription, DNA-templated","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005616","ec_ontology":"ECO","ec_name":"beta-galactosidase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00288r051","statement":[{"text":"These site L mutants disrupt the interaction of Phd with Asp53 (in the case of the R38D mutation) or introduce a negative charge in the hydrophobic pocket that accommodates residues Phe56 and Phe60 of Phd (for A61D) and results in a complete loss of corepression. However, their ability to bind Phd through their H site remains intact (Figure 5C; Table S5). Thus the low-affinity interaction that is required to establish a Doc-bridge between two operator-bound Phd dimers is crucial for Doc-mediated enhancement of repression.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T10:02:02.230Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription.\" [GOC:go_curators, GOC:txnOH]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2016_10","uniref100":"UniRef100_Q06253","date":"2016-09-06T13:45:00.000Z","acc":"Q06253","name":"Antitoxin phd","length":73,"organism":"Escherichia phage P1","UniParc":"UPI0000000701","genes":[{"name":{"value":"phd"}}],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":73,"type":"T"}],"Structural state":[{"start":1,"end":73,"type":"D"}],"Structural transition":[{"start":1,"end":73,"type":"T"}],"Molecular function":[{"start":1,"end":73,"type":"F"}],"Biological process":[{"start":1,"end":73,"type":"F"}]}},{"features":{"pfam":[{"id":"PF13499","name":"EF-hand domain pair","start":165,"end":237},{"id":"PF13833","name":"EF-hand domain pair","start":133,"end":153}],"gene3D":[{"start":41,"end":256,"id":"1.10.238.10","name":"EF-hand"}]},"uniref50":"UniRef50_Q9Y2W7-3","sequence":"MQRTKEAVKASDGNLLGDPGRIPLSKRESIKWQRPRFTRQALMRCCLIKWILSSAAPQGSDSSDSELELSTVRHQPEGLDQLQAQTKFTKKELQSLYRGFKNECPTGLVDEDTFKLIYSQFFPQGDATTYAHFLFNAFDADGNGAIHFEDFVVGLSILLRGTVHEKLKWAFNLYDINKDGCITKEEMLAIMKSIYDMMGRHTYPILREDAPLEHVERFFQKMDRNQDGVVTIDEFLETCQKDENIMNSMQLFENVI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q9QXT8","disprot_id":"DP00291","ncbi_taxon_id":10090,"regions_counter":22,"creator":"zdosztanyi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":77,"region_id":"DP00291r006","released":"2024_06","ec_id":"ECO:0006165","reference_html":"NMR structure of DREAM: Implications for Ca(2+)-dependent DNA binding and protein dimerization. <i> Lusin JD, Vanarotti M, Li C, Valiveti A, Ames JB. </i> Biochemistry, 2008","term_id":"IDPO:0000002","curator_id":"vnugnes","start":65,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2024-03-13T13:16:42.684Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2JUL"}],"reference_id":"18201103","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271"}],"sequence_construct":"SELELSTVRHQPEGLDQLQAQTKFTKKELQSLYRGFKNECPTGLVDEDTFKLIYSQFFPQGDATTYAHFLFNAFDADGNGAIHFEDFVVGLSILLRGTVHEKLKWAFNLYDINKDGCITKEEMLAIMKSIYDMMGRHTYPILREDAPLEHVERFFQKMDRNQDGVVTIDEFLETCQKDENIMNSMQLFENVI","statement":[{"text":"15N{1H} NOE values less than 0.65 were observed for residues in unstructured regions (residues 65−77 and 198−211). ","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":211,"region_id":"DP00291r007","released":"2023_12","ec_id":"ECO:0006165","reference_html":"NMR structure of DREAM: Implications for Ca(2+)-dependent DNA binding and protein dimerization. <i> Lusin JD, Vanarotti M, Li C, Valiveti A, Ames JB. </i> Biochemistry, 2008","term_id":"IDPO:0000002","curator_id":"vnugnes","start":198,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-31T13:33:55.467Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2JUL"}],"reference_id":"18201103","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271"}],"sequence_construct":"SELELSTVRHQPEGLDQLQAQTKFTKKELQSLYRGFKNECPTGLVDEDTFKLIYSQFFPQGDATTYAHFLFNAFDADGNGAIHFEDFVVGLSILLRGTVHEKLKWAFNLYDINKDGCITKEEMLAIMKSIYDMMGRHTYPILREDAPLEHVERFFQKMDRNQDGVVTIDEFLETCQKDENIMNSMQLFENVI","statement":[{"text":"15N{1H} NOE values less than 0.65 were observed for residues in unstructured regions (residues 65−77 and 198−211). ","type":"Results"}]},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":256,"term_name":"molten globule to order","start":65,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15746104","version":3,"reference_html":"Mg2+ and Ca2+ differentially regulate DNA binding and dimerization of DREAM. <i> Osawa M, Dace A, Tong KI, Valiveti A, Ikura M, Ames JB. </i> J Biol Chem, 2005","date":"2024-03-13T13:55:02.133Z","term_id":"IDPO:0000012","ec_id":"ECO:0006165","region_id":"DP00291r012","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"}],"statement":[{"text":" Mg2+ binding to DREAM-C increased the NMR chemical shift dispersion and promoted long range NOEs in the NOESY spectrum (data not shown), demonstrating that Mg2+-bound DREAM-C adopts at least some stable tertiary structure in contrast to the metal-free protein.","type":"Results"},{"text":"Significant spectral changes induced by adding Ca2+ to the Mg2+-bound protein sample indicated that Ca2+-induced conformational changes are distinct and separate from the Mg2+-induced changes (Fig. 6, B and C).","type":"Results"},{"text":"The HSQC spectrum of Ca2+/Mg2+-saturated DREAM-C exhibited variable peak intensities, suggesting exchange broadening perhaps associated with Ca2+-induced dimerization (see Fig. 5). Pulsed-field gradient diffusion NMR studies determined a hydrodynamic radius of 3.2 nm, corresponding to a stable Ca2+-bound protein dimer that persisted under a wide range of protein concentrations (0.05–1 mm).","type":"Results"}]},{"start":65,"end":256,"reference_id":"15746104","reference_source":"pmid","reference_html":"Mg2+ and Ca2+ differentially regulate DNA binding and dimerization of DREAM. <i> Osawa M, Dace A, Tong KI, Valiveti A, Ikura M, Ames JB. </i> J Biol Chem, 2005","date":"2024-03-13T13:43:12.253Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"29108","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00291r013","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"3312","entry_name":"calcium dichloride"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"6636","entry_name":"magnesium dichloride"}],"statement":[{"text":"Titration of CaCl2 into apoDREAM-C (in the absence of Mg2+) resulted in a binding isotherm that is multiphasic and could be fit by the binding of three or more Ca2+ ions, consistent with previous binding studies (10, 24). The isotherm exhibited stoichiometric binding of two Ca2+ (Kd ∼ 1–10 μm) followed by endothermic binding of one or more Ca2+ ion(s) with much lower affinity.","type":"Results"},{"text":"The presence of physiological levels of Mg2+ (5 mm Mg2+) had a profound affect on the ITC Ca2+ binding isotherms of wild-type and EF-hand mutants (Fig. 3B). The Ca2+ binding isotherm of wild-type in the presence of physiological Mg2+ was saturated with a Ca2+ binding stoichiometry of two, in contrast to a stoichiometry of three in the absence of Mg2+ (Fig. 3A).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a calcium ion (Ca2+).\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":139,"end":150,"reference_id":"15746104","reference_source":"pmid","reference_html":"Mg2+ and Ca2+ differentially regulate DNA binding and dimerization of DREAM. <i> Osawa M, Dace A, Tong KI, Valiveti A, Ikura M, Ames JB. </i> J Biol Chem, 2005","date":"2024-03-13T13:32:41.636Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IMP","interaction_partner":[{"db":"ChEBI","id":"29108","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00291r014","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"3312","entry_name":"calcium dichloride"}],"statement":[{"text":"To simplify the analysis, we have constructed various single-site mutants that disable functional Ca2+ binding to the individual EF-hands (Fig. 1): D150N (EF-2), E186Q (EF-3), and E234Q (EF-4). In each mutant, a negatively charged Glu or Asp at the 12-position in the EF-hand loop has been substituted with a corresponding neutral residue (Gln or Asn) that dramatically lowers the Ca2+ binding affinity of the respective EF-hand outside of the physiological range of Ca2+ (31, 32).","type":"Results"},{"text":"In summary, EF-2 is an endothermic site with low affinity that gives rise to the non-stoichiometric binding in the wild-type isotherm. EF-3 and EF-4 are relatively high affinity sites (stoichiometric binding) whose enthalpies nearly cancel one another in the wild-type isotherm.","type":"Results"},{"text":"The authors refers to the 139-150 region as EF-2.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a calcium ion (Ca2+).\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp150Asn","start":null,"end":null,"position":null}]},{"start":175,"end":186,"reference_id":"15746104","reference_source":"pmid","reference_html":"Mg2+ and Ca2+ differentially regulate DNA binding and dimerization of DREAM. <i> Osawa M, Dace A, Tong KI, Valiveti A, Ikura M, Ames JB. </i> J Biol Chem, 2005","date":"2024-03-13T13:32:28.108Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu186Gln","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"ChEBI","id":"29108","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00291r015","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"3312","entry_name":"calcium dichloride"}],"statement":[{"text":"To simplify the analysis, we have constructed various single-site mutants that disable functional Ca2+ binding to the individual EF-hands (Fig. 1): D150N (EF-2), E186Q (EF-3), and E234Q (EF-4). In each mutant, a negatively charged Glu or Asp at the 12-position in the EF-hand loop has been substituted with a corresponding neutral residue (Gln or Asn) that dramatically lowers the Ca2+ binding affinity of the respective EF-hand outside of the physiological range of Ca2+ (31, 32).","type":"Results"},{"text":"In summary, EF-2 is an endothermic site with low affinity that gives rise to the non-stoichiometric binding in the wild-type isotherm. EF-3 and EF-4 are relatively high affinity sites (stoichiometric binding) whose enthalpies nearly cancel one another in the wild-type isotherm.","type":"Results"},{"text":"The authors refers to the 175-186 region as EF-3.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a calcium ion (Ca2+).\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":223,"end":234,"reference_id":"15746104","reference_source":"pmid","reference_html":"Mg2+ and Ca2+ differentially regulate DNA binding and dimerization of DREAM. <i> Osawa M, Dace A, Tong KI, Valiveti A, Ikura M, Ames JB. </i> J Biol Chem, 2005","date":"2024-03-13T13:33:59.930Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu234Gln","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"ChEBI","id":"29108","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00291r016","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"3312","entry_name":"calcium dichloride"}],"statement":[{"text":"To simplify the analysis, we have constructed various single-site mutants that disable functional Ca2+ binding to the individual EF-hands (Fig. 1): D150N (EF-2), E186Q (EF-3), and E234Q (EF-4). In each mutant, a negatively charged Glu or Asp at the 12-position in the EF-hand loop has been substituted with a corresponding neutral residue (Gln or Asn) that dramatically lowers the Ca2+ binding affinity of the respective EF-hand outside of the physiological range of Ca2+ (31, 32).","type":"Results"},{"text":"In summary, EF-2 is an endothermic site with low affinity that gives rise to the non-stoichiometric binding in the wild-type isotherm. EF-3 and EF-4 are relatively high affinity sites (stoichiometric binding) whose enthalpies nearly cancel one another in the wild-type isotherm.","type":"Results"},{"text":"The authors refers to the 223-234 region as EF-4.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a calcium ion (Ca2+).\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":65,"end":256,"reference_id":"15746104","reference_source":"pmid","reference_html":"Mg2+ and Ca2+ differentially regulate DNA binding and dimerization of DREAM. <i> Osawa M, Dace A, Tong KI, Valiveti A, Ikura M, Ames JB. </i> J Biol Chem, 2005","date":"2024-03-13T13:41:01.882Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0000287","term_name":"magnesium ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","region_id":"DP00291r017","statement":[{"text":"Analysis of the binding isotherm using a “two sites” model (Microcal Origin software) revealed that DREAM-C has one Mg2+ site with relatively high affinity (dissociation constant of 13 μm and ΔH = -0.79 kcal/mol), and two or more sites with much lower affinity (Kd in the millimolar range and ΔH = +3.97 kcal/mol).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a magnesium (Mg) ion.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"ChEBI","id":"18420","operator":"and","partner_start":null,"partner_end":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"6636","entry_name":"magnesium dichloride"}]},{"start":65,"end":256,"reference_id":"15746104","reference_source":"pmid","reference_html":"Mg2+ and Ca2+ differentially regulate DNA binding and dimerization of DREAM. <i> Osawa M, Dace A, Tong KI, Valiveti A, Ikura M, Ames JB. </i> J Biol Chem, 2005","date":"2024-03-13T13:48:15.380Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9QXT8","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00291r018","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"By contrast, Ca2+-saturated DREAM-C in the presence of Mg2+ eluted with an apparent molecular mass of 50 kDa in solution (Fig. 5), indicating that the Ca2+-bound protein forms a stable dimer even at very dilute protein concentrations (10). Similar calcium-sensitive hydrodynamic properties were observed for each of the EF-hand mutants (data not shown), suggesting that each mutant is structurally intact. In summary, DREAM-C appears to be a monomer under basal physiological conditions (5 mm Mg2+ and 100 nm Ca2+) and forms a stable dimer at saturating Ca2+ levels.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":65,"end":256,"reference_id":"15746104","reference_source":"pmid","reference_html":"Mg2+ and Ca2+ differentially regulate DNA binding and dimerization of DREAM. <i> Osawa M, Dace A, Tong KI, Valiveti A, Ikura M, Ames JB. </i> J Biol Chem, 2005","date":"2024-03-13T13:50:43.882Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP00291r019","statement":[{"text":"The poor chemical shift dispersion demonstrates that apoDREAM-C adopts an unstructured molten-globule state similar to that described for apo states of many other EF-hand proteins (30, 34, 35).","type":"Results"}]},{"start":65,"end":256,"reference_id":"15746104","reference_source":"pmid","reference_html":"Mg2+ and Ca2+ differentially regulate DNA binding and dimerization of DREAM. <i> Osawa M, Dace A, Tong KI, Valiveti A, Ikura M, Ames JB. </i> J Biol Chem, 2005","date":"2024-03-13T14:17:04.968Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0000976","term_name":"transcription cis-regulatory region binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","region_id":"DP00291r020","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"}],"statement":[{"text":"Electrophoresis mobility shift assays (EMSA) were performed on the EF-hand mutants to monitor their Ca2+-sensitive binding to duplex oligonucleotide derived from the downstream response element (DRE) of the prodynorphin gene (Fig. 7).","type":"Results"},{"text":"A typical EMSA for DREAM is shown in Fig. 7 and exhibits two shifted bands that represent different oligomeric species of DREAM bound to DRE.","type":"Results"},{"text":"In summary, Mg2+ is required for sequence-specific binding to DRE and Ca2+ binding at either EF-3 or EF-4 is sufficient to abolish DNA binding.","type":"Results"}],"term_comment":"Note that this term is meant to also capture non-specific binding to regulatory regions. Also, to minimize ambiguity in the use of the word \"promoter\" in GO, we have chosen the phrase \"transcription regulatory region\" to refer to all of the regulatory regions. Regulatory regions in the DNA which control initiation may include the \"core promoter\" where the basal transcription machinery binds, the \"core promoter proximal region\" where regulatory factors other than the basal machinery bind. There are also additional regulatory regions, in both the DNA and the RNA transcript, which regulate elongation or termination of transcription.","term_def":"\"Binding to a specific sequence of DNA that is part of a regulatory region that controls transcription of that section of the DNA. The transcribed region might be described as a gene, cistron, or operon.\" [GOC:txnOH]","term_is_obsolete":false,"term_not_annotate":false},{"start":223,"end":234,"reference_id":"15746104","reference_source":"pmid","reference_html":"Mg2+ and Ca2+ differentially regulate DNA binding and dimerization of DREAM. <i> Osawa M, Dace A, Tong KI, Valiveti A, Ikura M, Ames JB. </i> J Biol Chem, 2005","date":"2024-03-13T14:37:30.603Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0043392","term_name":"negative regulation of DNA binding","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","region_id":"DP00291r021","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"In summary, Mg2+ is required for sequence-specific binding to DRE and Ca2+ binding at either EF-3 or EF-4 is sufficient to abolish DNA binding.","type":"Results"},{"text":"A second implication of this study is that Ca2+ binding at EF-3 and EF-4 promotes protein dimerization that somehow disrupts DNA binding by DREAM.","type":"Results"},{"text":"The authors refers to the 223-234 region as EF-4.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that stops or reduces the frequency, rate or extent of DNA binding. DNA binding is any process in which a gene product interacts selectively with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false},{"start":175,"end":186,"reference_id":"15746104","reference_source":"pmid","reference_html":"Mg2+ and Ca2+ differentially regulate DNA binding and dimerization of DREAM. <i> Osawa M, Dace A, Tong KI, Valiveti A, Ikura M, Ames JB. </i> J Biol Chem, 2005","date":"2024-03-13T14:37:46.913Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0043392","term_name":"negative regulation of DNA binding","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","region_id":"DP00291r022","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"In summary, Mg2+ is required for sequence-specific binding to DRE and Ca2+ binding at either EF-3 or EF-4 is sufficient to abolish DNA binding.","type":"Results"},{"text":"A second implication of this study is that Ca2+ binding at EF-3 and EF-4 promotes protein dimerization that somehow disrupts DNA binding by DREAM.","type":"Results"},{"text":"The authors refers to the 175-186 region as EF-3.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that stops or reduces the frequency, rate or extent of DNA binding. DNA binding is any process in which a gene product interacts selectively with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_Q9QXT8","date":"2016-09-08T16:38:44.000Z","acc":"Q9QXT8","name":"Calsenilin","length":256,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000029D2E","genes":[{"name":{"value":"Kcnip3"},"synonyms":[{"value":"Csen"},{"value":"Dream"},{"value":"Kchip3"}]}],"alphafold_very_low_content":0.30078125,"disorder_content":0.75,"disprot_consensus":{"full":[{"start":65,"end":256,"type":"T"}],"Structural state":[{"start":65,"end":256,"type":"D"}],"Structural transition":[{"start":65,"end":256,"type":"T"}],"Molecular function":[{"start":65,"end":256,"type":"F"}],"Biological process":[{"start":175,"end":186,"type":"F"},{"start":223,"end":234,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01627","name":"Hpt domain","start":26,"end":98}],"gene3D":[{"start":1,"end":114,"id":"1.20.120.160","name":"HPT domain"}]},"uniref50":"UniRef50_Q87MX8","sequence":"MNTDVLNQQKIEELSAEIGSDNVPVLLDIFLGEMDSYIGTLTELQGSEQLLYLKEISHALKSSAASFGADRLCERAIAIDKKAKANQLQEQGMETSEMLALLHITRDAYRSWTN","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Vibrionales","Vibrionaceae","Vibrio"],"uniref90":"UniRef90_A7MVC1","disprot_id":"DP00292","ncbi_taxon_id":669,"regions_counter":3,"creator":"maspromonte","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":97,"region_id":"DP00292r003","released":"2022_03","ec_id":"ECO:0006198","reference_html":"Solution structure and dynamics of LuxU from Vibrio harveyi, a phosphotransferase protein involved in bacterial quorum sensing. <i> Ulrich DL, Kojetin D, Bassler BL, Cavanagh J, Loria JP. </i> J Mol Biol, 2005","statement":[{"text":"There are few NOEs for residues 85–97, which connect helices αD and αE.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":85,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15740742","version":2,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1Y6D"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_A7MVC1","date":"2016-09-08T23:10:58.000Z","acc":"P0C5S4","name":"Phosphorelay protein LuxU","length":114,"organism":"Vibrio harveyi","dataset":[],"UniParc":"UPI00002281FF","genes":[{"name":{"value":"luxU"}}],"alphafold_very_low_content":0.02631578947368421,"disorder_content":0.11403508771929824,"disprot_consensus":{"full":[{"start":85,"end":97,"type":"D"}],"Structural state":[{"start":85,"end":97,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00452","name":"Apoptosis regulator proteins, Bcl-2 family","start":97,"end":195},{"id":"PF02180","name":"Bcl-2 homology region 4","start":8,"end":32}]},"uniref50":"UniRef50_P10415","sequence":"MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDVGAAPPGAAPAPGIFSSQPGHTPHPAASRDPVARTSPLQTPAAPGAAAGPALSPVPPVVHLTLRQAGDDFSRRYRRDFAEMSSQLHLTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P10415","disprot_id":"DP00297","ncbi_taxon_id":9606,"regions_counter":4,"creator":"zkalman","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":48,"region_id":"DP00297r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural and biochemical analysis of Bcl-2 interaction with the hepatitis B virus protein HBx. <i> Jiang T, Liu M, Wu J, Shi Y. </i> Proc Natl Acad Sci U S A, 2016","term_id":"IDPO:0000002","curator_id":"droche","start":26,"term_ontology":"IDPO","curator_name":"Daniel Roche","reference_id":"26858413","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5FCG"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":48,"term_name":"molecular adaptor activity","start":26,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"GO","curator_name":"Daniel Roche","reference_id":"26858413","version":3,"reference_html":"Structural and biochemical analysis of Bcl-2 interaction with the hepatitis B virus protein HBx. <i> Jiang T, Liu M, Wu J, Shi Y. </i> Proc Natl Acad Sci U S A, 2016","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006220","region_id":"DP00297r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":48,"term_name":"protein binding","start":26,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"GO","curator_name":"Daniel Roche","reference_id":"26858413","version":3,"reference_html":"Structural and biochemical analysis of Bcl-2 interaction with the hepatitis B virus protein HBx. <i> Jiang T, Liu M, Wu J, Shi Y. </i> Proc Natl Acad Sci U S A, 2016","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00297r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P10415","date":"2016-09-06T14:13:06.000Z","acc":"P10415","name":"Apoptosis regulator Bcl-2","length":239,"organism":"Homo sapiens","dataset":["Autophagy-related proteins","Cancer-related proteins"],"UniParc":"UPI000002F8D7","genes":[{"name":{"value":"BCL2"}}],"alphafold_very_low_content":0.2384937238493724,"disorder_content":0.09623430962343096,"disprot_consensus":{"full":[{"start":26,"end":48,"type":"D"}],"Structural state":[{"start":26,"end":48,"type":"D"}],"Molecular function":[{"start":26,"end":48,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00452","name":"Apoptosis regulator proteins, Bcl-2 family","start":90,"end":188},{"id":"PF02180","name":"Bcl-2 homology region 4","start":1,"end":26}],"gene3D":[{"start":1,"end":209,"id":"1.10.437.10","name":"Blc2-like"}]},"uniref50":"UniRef50_Q07817","sequence":"MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEMETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q07817","disprot_id":"DP00298","ncbi_taxon_id":9606,"regions_counter":10,"creator":"epapa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":80,"region_id":"DP00298r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death. <i> Muchmore SW, Sattler M, Liang H, Meadows RP, Harlan JE, Yoon HS, Nettesheim D, Chang BS, Thompson CB, Wong SL, Ng SL, Fesik SW. </i> Nature, 1996","term_id":"IDPO:0000002","curator_id":"mnecci","start":28,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"8692274","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1LXL"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":80,"term_name":"flexible linker","start":28,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"8692274","version":3,"reference_html":"X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death. <i> Muchmore SW, Sattler M, Liang H, Meadows RP, Harlan JE, Yoon HS, Nettesheim D, Chang BS, Thompson CB, Wong SL, Ng SL, Fesik SW. </i> Nature, 1996","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006165","region_id":"DP00298r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":80,"region_id":"DP00298r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death. <i> Muchmore SW, Sattler M, Liang H, Meadows RP, Harlan JE, Yoon HS, Nettesheim D, Chang BS, Thompson CB, Wong SL, Ng SL, Fesik SW. </i> Nature, 1996","term_id":"IDPO:0000002","curator_id":"mnecci","start":28,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"8692274","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1R2G"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":80,"term_name":"flexible linker","start":28,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"8692274","version":3,"reference_html":"X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death. <i> Muchmore SW, Sattler M, Liang H, Meadows RP, Harlan JE, Yoon HS, Nettesheim D, Chang BS, Thompson CB, Wong SL, Ng SL, Fesik SW. </i> Nature, 1996","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006220","region_id":"DP00298r004","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":80,"region_id":"DP00298r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Regulation of apoptosis by an intrinsically disordered region of Bcl-xL. <i> Follis AV, Llambi F, Kalkavan H, Yao Y, Phillips AH, Park CG, Marassi FM, Green DR, Kriwacki RW. </i> Nat Chem Biol, 2018","statement":[{"text":"This observation suggests that, in the absence of IDR post-translational modifications, the α1-α2 IDR transiently interacts in cis with the folded core of Bcl-xL\n(NOE) spectra for Bcl-xL with the S62E phosphomimetic mutation showed that residues within the α1-α2 IDR exhibited reduced flexibility in comparison to wild-type Bcl-xL","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"epapa","start":28,"term_ontology":"IDPO","curator_name":"Elena Papaleo","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29507390","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":80,"term_name":"phosphorylation display site","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Regulation of apoptosis by an intrinsically disordered region of Bcl-xL. <i> Follis AV, Llambi F, Kalkavan H, Yao Y, Phillips AH, Park CG, Marassi FM, Green DR, Kriwacki RW. </i> Nat Chem Biol, 2018","term_id":"IDPO:0000045","curator_id":"epapa","start":28,"term_ontology":"IDPO","curator_name":"Elena Papaleo","reference_id":"29507390","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00298r006","ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":25,"end":80,"reference_id":"23340338","reference_source":"pmid","reference_html":"PUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis. <i> Follis AV, Chipuk JE, Fisher JC, Yun MK, Grace CR, Nourse A, Baran K, Ou L, Min L, White SW, Green DR, Kriwacki RW. </i> Nat Chem Biol, 2013","date":"2023-08-22T15:43:16.819Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4HNJ"}],"region_id":"DP00298r010","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9BXH1"}],"statement":[{"text":"We used this construct for NMR experiments because intense resonances of the disordered loop overlap and interfere with those of the folded BCL-xL core. The α1-α2 loop was, however, present in the BCL-xLΔC construct, lacking only the C-terminal 22 residues18, used for other functional assays.","type":"Results"},{"text":"The PDB structure shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"released":"2016_10","uniref100":"UniRef100_Q07817","date":"2016-09-05T16:25:30.000Z","acc":"Q07817","name":"Bcl-2-like protein 1","length":233,"organism":"Homo sapiens","dataset":["Autophagy-related proteins"],"UniParc":"UPI0000000CEC","genes":[{"name":{"value":"BCL2L1"},"synonyms":[{"value":"BCL2L"},{"value":"BCLX"}]}],"alphafold_very_low_content":0.296137339055794,"disorder_content":0.24034334763948498,"disprot_consensus":{"full":[{"start":25,"end":80,"type":"D"}],"Structural state":[{"start":25,"end":80,"type":"D"}],"Disorder function":[{"start":28,"end":80,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02452","name":"PemK-like, MazF-like toxin of type II toxin-antitoxin system","start":10,"end":109}],"gene3D":[{"start":1,"end":111,"id":"2.30.30.110","name":"2.30.30.110"}]},"uniref50":"UniRef50_P0AE71","sequence":"MVSRYVPDMGDLIWVDFDPTKGSEQAGHRPAVVLSPFMYNNKTGMCLCVPCTTQSKGYPFEVVLSGQERDGVALADQVKSIAWRARGATKKGTVAPEELQLIKAKINVLIG","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0AE71","disprot_id":"DP00299","dataset":["Unicellular toxins and antitoxins","RNA-binding proteins","Stress response proteins"],"ncbi_taxon_id":83333,"regions_counter":10,"creator":"aschramm","regions":[{"region_id":"DP00299r007","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T12:28:57.807Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":29,"term_id":"IDPO:0000002","start":16,"version":2,"statement":[{"text":"Central in this regulation is an EcMazE-induced double conformational change as follows: a rearrangement of a crucial active site loop and a relative rotation of the two monomers in the EcMazF dimer. Both are induced by the C-terminal residues Asp-78–Trp-82 of EcMazE, which are also responsible for strong negative cooperativity in EcMazE-EcMazF binding","type":"Abstract"},{"text":"Substrate Binding Folds an Otherwise Disordered Substratebinding Loop of EcMazF. Most loop regions are well structured, with exception of loops 1-2 (residues Asp-16– Arg-29) and 4-5 (residues Leu-64–Gly-71) (Fig. 1C). \n","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"27026704","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5CKB"},{"db":"PDB","id":"5CO7"},{"db":"PDB","id":"5CK9"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lchemes","reference_html":"Substrate Recognition and Activity Regulation of the Escherichia coli mRNA Endonuclease MazF. <i> Zorzini V, Mernik A, Lah J, Sterckx YG, De Jonge N, Garcia-Pino A, De Greve H, Versées W, Loris R. </i> J Biol Chem, 2016","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00299r008","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T12:29:16.991Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":29,"term_id":"IDPO:0000011","start":16,"version":2,"statement":[{"text":"Central in this regulation is an EcMazE-induced double conformational change as follows: a rearrangement of a crucial active site loop and a relative rotation of the two monomers in the EcMazF dimer. Both are induced by the C-terminal residues Asp-78–Trp-82 of EcMazE, which are also responsible for strong negative cooperativity in EcMazE-EcMazF binding","type":"Abstract"},{"text":"Substrate Binding Folds an Otherwise Disordered Substratebinding Loop of EcMazF. Most loop regions are well structured, with exception of loops 1-2 (residues Asp-16– Arg-29) and 4-5 (residues Leu-64–Gly-71) (Fig. 1C). [...] The crystal structure of EcMazF in complex with the substrate-mimicking DNA sequence d(A1 U2 A3 C4 A5 U6 A7 ) (from now on referred to as “substrate complex”) was determined at 3.0 Å resolution (Table 1).. Loops 1-2 and 4-5 are fully ordered and adopt identical conformations in all three monomers\n\n","type":"Results"}],"term_name":"disorder to order","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"27026704","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5CR2"},{"db":"PDB","id":"5CQY"},{"db":"PDB","id":"5CQX"}],"term_namespace":"Structural transition","ec_id":"ECO:0005670","curator_id":"lchemes","reference_html":"Substrate Recognition and Activity Regulation of the Escherichia coli mRNA Endonuclease MazF. <i> Zorzini V, Mernik A, Lah J, Sterckx YG, De Jonge N, Garcia-Pino A, De Greve H, Versées W, Loris R. </i> J Biol Chem, 2016","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00299r010","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T12:29:24.188Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":29,"term_id":"GO:0140677","start":16,"version":3,"statement":[{"text":"Central in this regulation is an EcMazE-induced double conformational change as follows: a rearrangement of a crucial active site loop and a relative rotation of the two monomers in the EcMazF dimer. Both are induced by the C-terminal residues Asp-78–Trp-82 of EcMazE, which are also responsible for strong negative cooperativity in EcMazE-EcMazF binding","type":"Abstract"},{"text":"Substrate Binding Folds an Otherwise Disordered Substratebinding Loop of EcMazF. Most loop regions are well structured, with exception of loops 1-2 (residues Asp-16– Arg-29) and 4-5 (residues Leu-64–Gly-71) (Fig. 1C). [...] The crystal structure of EcMazF in complex with the substrate-mimicking DNA sequence d(A1 U2 A3 C4 A5 U6 A7 ) (from now on referred to as “substrate complex”) was determined at 3.0 Å resolution (Table 1).. Loops 1-2 and 4-5 are fully ordered and adopt identical conformations in all three monomers\n\n","type":"Results"},{"text":"Both EcMazF and BsMazF only adapt a catalytically competent conformation for loop 1-2 when a substrate or substrate mimic is bound (27). In both enzymes, the antitoxin also prevents loop 1-2 from adopting this conformation. ","type":"Results"},{"text":"Ordering of the loops occurs only upon binding the substrate, bringing about the catalytically active form","type":"Curator statement"}],"term_name":"molecular function activator activity","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"27026704","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5CR2"},{"db":"PDB","id":"5CQY"},{"db":"PDB","id":"5CQX"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"lchemes","reference_html":"Substrate Recognition and Activity Regulation of the Escherichia coli mRNA Endonuclease MazF. <i> Zorzini V, Mernik A, Lah J, Sterckx YG, De Jonge N, Garcia-Pino A, De Greve H, Versées W, Loris R. </i> J Biol Chem, 2016","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P0AE71","date":"2016-09-09T21:50:37.000Z","acc":"P0AE70","name":"Endoribonuclease toxin MazF","length":111,"organism":"Escherichia coli (strain K12)","UniParc":"UPI00001278B1","genes":[{"name":{"value":"mazF"},"synonyms":[{"value":"chpA"},{"value":"chpAK"}],"olnNames":[{"value":"b2782"},{"value":"JW2753"}]}],"alphafold_very_low_content":0.018018018018018018,"disorder_content":0.12612612612612611,"disprot_consensus":{"full":[{"start":16,"end":29,"type":"T"}],"Structural state":[{"start":16,"end":29,"type":"D"}],"Structural transition":[{"start":16,"end":29,"type":"T"}],"Molecular function":[{"start":16,"end":29,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00186","name":"Dihydrofolate reductase","start":1,"end":158}],"gene3D":[{"start":119,"end":152,"id":"3.40.430.10","name":"Dihydrofolate Reductase, subunit A"},{"start":1,"end":118,"id":"3.40.430.10","name":"Dihydrofolate Reductase, subunit A"}]},"uniref50":"UniRef50_Q8ZRW2","sequence":"MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIGRPLPGRKNIILSSQPGTDDRVTWVKSVDEAIAACGDVPEIMVIGGGRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHSYCFEILERR","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0ABQ5","disprot_id":"DP00301","ncbi_taxon_id":83333,"regions_counter":32,"creator":"esalladini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":72,"region_id":"DP00301r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. <i> Sawaya MR, Kraut J. </i> Biochemistry, 1997","term_id":"IDPO:0000002","curator_id":"esalladini","start":63,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"9012674","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1RX9"}],"term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":72,"term_name":"molecular function regulator","start":63,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"9012674","version":3,"reference_html":"Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. <i> Sawaya MR, Kraut J. </i> Biochemistry, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006220","region_id":"DP00301r002","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":72,"term_name":"disorder to order","start":63,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"9012674","version":2,"reference_html":"Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. <i> Sawaya MR, Kraut J. </i> Biochemistry, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00301r003","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":72,"term_name":"protein binding","start":63,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"9012674","version":3,"reference_html":"Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. <i> Sawaya MR, Kraut J. </i> Biochemistry, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00301r004","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":72,"region_id":"DP00301r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase. <i> Schnell JR, Dyson HJ, Wright PE. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"esalladini","start":63,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"14717591","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":72,"term_name":"molecular function regulator","start":63,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"14717591","version":3,"reference_html":"Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase. <i> Schnell JR, Dyson HJ, Wright PE. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006165","region_id":"DP00301r006","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":72,"term_name":"disorder to order","start":63,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"14717591","version":2,"reference_html":"Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase. <i> Schnell JR, Dyson HJ, Wright PE. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00301r007","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":72,"term_name":"protein binding","start":63,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"14717591","version":3,"reference_html":"Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase. <i> Schnell JR, Dyson HJ, Wright PE. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00301r008","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":132,"region_id":"DP00301r009","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. <i> Sawaya MR, Kraut J. </i> Biochemistry, 1997","term_id":"IDPO:0000002","curator_id":"esalladini","start":116,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"9012674","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1RX9"}],"term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":132,"term_name":"molecular function regulator","start":116,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"9012674","version":3,"reference_html":"Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. <i> Sawaya MR, Kraut J. </i> Biochemistry, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006220","region_id":"DP00301r010","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":132,"term_name":"disorder to order","start":116,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"9012674","version":2,"reference_html":"Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. <i> Sawaya MR, Kraut J. </i> Biochemistry, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00301r011","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":132,"term_name":"protein binding","start":116,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"9012674","version":3,"reference_html":"Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. <i> Sawaya MR, Kraut J. </i> Biochemistry, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00301r012","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":132,"region_id":"DP00301r013","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase. <i> Schnell JR, Dyson HJ, Wright PE. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"esalladini","start":116,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"14717591","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":132,"term_name":"molecular function regulator","start":116,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"14717591","version":3,"reference_html":"Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase. <i> Schnell JR, Dyson HJ, Wright PE. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006165","region_id":"DP00301r014","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":132,"term_name":"disorder to order","start":116,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"14717591","version":2,"reference_html":"Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase. <i> Schnell JR, Dyson HJ, Wright PE. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00301r015","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":132,"term_name":"protein binding","start":116,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"14717591","version":3,"reference_html":"Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase. <i> Schnell JR, Dyson HJ, Wright PE. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00301r016","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":24,"region_id":"DP00301r017","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase. <i> Schnell JR, Dyson HJ, Wright PE. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"esalladini","start":9,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"14717591","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":24,"term_name":"molecular function regulator","start":9,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"14717591","version":3,"reference_html":"Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase. <i> Schnell JR, Dyson HJ, Wright PE. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006165","region_id":"DP00301r018","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":24,"term_name":"disorder to order","start":9,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"14717591","version":2,"reference_html":"Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase. <i> Schnell JR, Dyson HJ, Wright PE. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00301r019","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":24,"term_name":"protein binding","start":9,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"14717591","version":3,"reference_html":"Effect of cofactor binding and loop conformation on side chain methyl dynamics in dihydrofolate reductase. <i> Schnell JR, Dyson HJ, Wright PE. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00301r020","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":24,"region_id":"DP00301r021","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. <i> Sawaya MR, Kraut J. </i> Biochemistry, 1997","term_id":"IDPO:0000002","curator_id":"esalladini","start":9,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"9012674","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1RX9"}],"term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":24,"term_name":"molecular function regulator","start":9,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"9012674","version":3,"reference_html":"Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. <i> Sawaya MR, Kraut J. </i> Biochemistry, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006220","region_id":"DP00301r022","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":24,"term_name":"disorder to order","start":9,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"9012674","version":2,"reference_html":"Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. <i> Sawaya MR, Kraut J. </i> Biochemistry, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00301r023","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":24,"term_name":"protein binding","start":9,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"9012674","version":3,"reference_html":"Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. <i> Sawaya MR, Kraut J. </i> Biochemistry, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00301r024","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P0ABQ5","date":"2016-09-08T15:31:57.000Z","acc":"P0ABQ4","name":"Dihydrofolate reductase","length":159,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI0000110F69","genes":[{"name":{"value":"folA"},"synonyms":[{"value":"tmrA"}],"olnNames":[{"value":"b0048"},{"value":"JW0047"}]}],"alphafold_very_low_content":0,"disorder_content":0.27044025157232704,"disprot_consensus":{"full":[{"start":9,"end":24,"type":"T"},{"start":63,"end":72,"type":"T"},{"start":116,"end":132,"type":"T"}],"Structural state":[{"start":9,"end":24,"type":"D"},{"start":63,"end":72,"type":"D"},{"start":116,"end":132,"type":"D"}],"Molecular function":[{"start":9,"end":24,"type":"F"},{"start":63,"end":72,"type":"F"},{"start":116,"end":132,"type":"F"}],"Structural transition":[{"start":9,"end":24,"type":"T"},{"start":63,"end":72,"type":"T"},{"start":116,"end":132,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":154,"end":409},{"id":"PF00169","name":"PH domain","start":6,"end":106},{"id":"PF00433","name":"Protein kinase C terminal domain","start":430,"end":475}],"gene3D":[{"start":1,"end":125,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":236,"end":430,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"},{"start":149,"end":446,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"}]},"uniref50":"UniRef50_P31751","sequence":"MNEVSVIKEGWLHKRGEYIKTWRPRYFLLKSDGSFIGYKERPEAPDQTLPPLNNFSVAECQLMKTERPRPNTFVIRCLQWTTVIERTFHVDSPDEREEWMRAIQMVANSLKQRAPGEDPMDYKCGSPSDSSTTEEMEVAVSKARAKVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRERVFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITPPDRYDSLGLLELDQRTHFPQFSYSASIRE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P31751","disprot_id":"DP00304","ncbi_taxon_id":9606,"regions_counter":8,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":310,"region_id":"DP00304r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of an inactive Akt2 kinase domain. <i> Huang X, Begley M, Morgenstern KA, Gu Y, Rose P, Zhao H, Zhu X. </i> Structure, 2003","term_id":"IDPO:0000002","curator_id":"fquaglia","start":298,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12517337","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1MRV"},{"db":"PDB","id":"1MRY"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Akt2 residues omitted from the model because of disorder include the N-terminal residues 143–145, residues 190–201 of α helix C, residues 298–310 of the activation loop, and C-terminal residues 441–481.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:22:25.212Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":312,"region_id":"DP00304r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation. <i> Yang J, Cron P, Thompson V, Good VM, Hess D, Hemmings BA, Barford D. </i> Mol Cell, 2002","term_id":"IDPO:0000002","curator_id":"fquaglia","start":297,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12086620","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1GZN"},{"db":"PDB","id":"1GZO"},{"db":"PDB","id":"1GZK"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In all three crystal forms of PKB, a contiguous region of the activation segment (residues 297 to 312) located between the invariant DFG and APE motifs, and including (p)Thr 309, is disordered.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:22:18.137Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":460,"region_id":"DP00304r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation. <i> Yang J, Cron P, Thompson V, Good VM, Hess D, Hemmings BA, Barford D. </i> Mol Cell, 2002","term_id":"IDPO:0000002","curator_id":"fquaglia","start":442,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12086620","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1GZK"},{"db":"PDB","id":"1GZO"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Moreover, in these structures, electron density for residues C-terminal to Asp 441 is not visible, suggesting that they are conformational disordered. However, in the ΔPH-PKB structure, which contains a nonphosphorylated hydrophobic motif and therefore retains the potential to interact with the N lobe, we are also unable to detect visible electron density for residues C-terminal to Asp 441, indicating that the hydrophobic motif is mobile.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:22:23.403Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":480,"region_id":"DP00304r004","released":"2022_06","ec_id":"ECO:0006220","reference_html":"Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation. <i> Yang J, Cron P, Thompson V, Good VM, Hess D, Hemmings BA, Barford D. </i> Mol Cell, 2002","term_id":"IDPO:0000002","curator_id":"vnugnes","start":442,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12086620","version":4,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-06-14T21:05:10.298Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1GZN"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Moreover, in these structures, electron density for residues C-terminal to Asp 441 is not visible, suggesting that they are conformational disordered. However, in the ΔPH-PKB structure, which contains a nonphosphorylated hydrophobic motif and therefore retains the potential to interact with the N lobe, we are also unable to detect visible electron density for residues C-terminal to Asp 441, indicating that the hydrophobic motif is mobile.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":309,"end":309,"position":"Specific residue"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":481,"region_id":"DP00304r005","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of an inactive Akt2 kinase domain. <i> Huang X, Begley M, Morgenstern KA, Gu Y, Rose P, Zhao H, Zhu X. </i> Structure, 2003","term_id":"IDPO:0000002","curator_id":"fquaglia","start":441,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12517337","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1MRV"},{"db":"PDB","id":"1MRY"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Akt2 residues omitted from the model because of disorder include the N-terminal residues 143–145, residues 190–201 of α helix C, residues 298–310 of the activation loop, and C-terminal residues 441–481.","type":"Results"},{"text":"In the structure of inactive Akt2-KD, the C-terminal chain extends over the C-terminal lobe and terminates near the ATP binding site, with the remaining 40 residues disordered.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:22:20.804Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":201,"region_id":"DP00304r006","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of an inactive Akt2 kinase domain. <i> Huang X, Begley M, Morgenstern KA, Gu Y, Rose P, Zhao H, Zhu X. </i> Structure, 2003","term_id":"IDPO:0000002","curator_id":"fquaglia","start":190,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12517337","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1MRV"},{"db":"PDB","id":"1MRY"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Akt2 residues omitted from the model because of disorder include the N-terminal residues 143–145, residues 190–201 of α helix C, residues 298–310 of the activation loop, and C-terminal residues 441–481.","type":"Results"},{"text":"The majority of α helix C in Akt2-KD, however, is disordered.","type":"Results"},{"text":"A distinguishing feature of the Akt2-KD structure is that the first eight residues of α helix C in Akt2-KD are disordered.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:22:19.720Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":298,"end":310,"reference_id":"12517337","reference_source":"pmid","reference_html":"Crystal structure of an inactive Akt2 kinase domain. <i> Huang X, Begley M, Morgenstern KA, Gu Y, Rose P, Zhao H, Zhu X. </i> Structure, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140677","term_name":"molecular function activator activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00304r007","statement":[{"text":"Akt2 residues omitted from the model because of disorder include the N-terminal residues 143–145, residues 190–201 of α helix C, residues 298–310 of the activation loop, and C-terminal residues 441–481.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:22:27.404Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":472,"end":476,"reference_id":"12086620","reference_source":"pmid","reference_html":"Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation. <i> Yang J, Cron P, Thompson V, Good VM, Hess D, Hemmings BA, Barford D. </i> Mol Cell, 2002","date":"2022-06-14T21:07:48.664Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","released":"2022_06","version":3,"region_id":"DP00304r008","statement":[{"text":"Activation of PKB by Ser 474 phosphorylation occurs via a mechanism involving a disorder to order transition of the αC helix of the N-terminal lobe, induced by the association of a phosphorylated hydrophobic motif, with concomitant ordering and restructuring of the activation segment and alignment of catalytic site residues.","type":"Introduction"},{"text":"Phosphorylation of Ser 474 augments the activity of PDK1-phosphorylated PKB by 7- to 10-fold (Alessi et al., 1996), such that phosphorylation of both residues results in greater than 1000-fold increased protein kinase activity.","type":"Introduction"},{"text":"The site of C-terminal regulatory phosphorylation of PKB (Ser 474) is within a hydrophobic sequence motif (F-x-x-F-[S/T]-Y), conserved within a large proportion of AGC kinases Keranen et al. 1995, Pearson et al. 1995.","type":"Introduction"},{"text":"Region including the phosphorylated Ser474.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Disorder function","construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":474,"end":474,"position":"Specific residue"}]}],"released":"2016_10","uniref100":"UniRef100_P31751","date":"2016-09-05T17:22:32.000Z","acc":"P31751","name":"RAC-beta serine/threonine-protein kinase","length":481,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI000016AFC1","genes":[{"name":{"value":"AKT2"}}],"alphafold_very_low_content":0.11226611226611227,"disorder_content":0.14345114345114346,"disprot_consensus":{"full":[{"start":190,"end":201,"type":"D"},{"start":297,"end":312,"type":"D"},{"start":441,"end":481,"type":"D"}],"Structural state":[{"start":190,"end":201,"type":"D"},{"start":297,"end":312,"type":"D"},{"start":441,"end":481,"type":"D"}],"Molecular function":[{"start":298,"end":310,"type":"F"}],"Disorder function":[{"start":472,"end":476,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00059","name":"Lectin C-type domain","start":103,"end":196}],"gene3D":[{"start":70,"end":199,"id":"3.10.100.10","name":"Mannose-Binding Protein A, subunit A"}]},"uniref50":"UniRef50_Q07108","sequence":"MSSENCFVAENSSLHPESGQENDATSPHFSTRHEGSFQVPVLCAVMNVVFITILIIALIALSVGQYNCPGQYTFSMPSDSHVSSCSEDWVGYQRKCYFISTVKRSWTSAQNACSEHGATLAVIDSEKDMNFLKRYAGREEHWVGLKKEPGHPWKWSNGKEFNNWFNVTGSDKCVFLKNTEVSSMECEKNLYWICNKPYK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q07108","disprot_id":"DP00306","ncbi_taxon_id":9606,"regions_counter":3,"creator":"fquaglia","regions":[{"start":64,"end":84,"reference_id":"11101293","reference_source":"pmid","reference_html":"Crystal structure of human CD69: a C-type lectin-like activation marker of hematopoietic cells. <i> Natarajan K, Sawicki MW, Margulies DH, Mariuzza RA. </i> Biochemistry, 2000","date":"2024-03-13T14:45:55.856Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP00306r003","statement":[{"text":"The stem region, which includes residues Gly64 to Val82 in the crystallized recombinant protein, is largely disordered in the structure, except for three residues (Ser78, Asp79, and Ser80) wedged between two symmetry-related molecules.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"1FM5"}]}],"released":"2016_10","uniref100":"UniRef100_Q07108","date":"2016-08-25T11:58:26.000Z","acc":"Q07108","name":"Early activation antigen CD69","length":199,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000622D7","genes":[{"name":{"value":"CD69"},"synonyms":[{"value":"CLEC2C"}]}],"alphafold_very_low_content":0.1708542713567839,"disorder_content":0.10552763819095477,"disprot_consensus":{"full":[{"start":64,"end":84,"type":"D"}],"Structural state":[{"start":64,"end":84,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00134","name":"Cyclin, N-terminal domain","start":75,"end":158},{"id":"PF16899","name":"Cyclin C-terminal domain","start":162,"end":260}],"gene3D":[{"start":11,"end":281,"id":"1.10.472.10","name":"Cyclin-like"},{"start":163,"end":263,"id":"1.10.472.10","name":"Cyclin-like"}]},"uniref50":"UniRef50_P51946","sequence":"MYHNSSQKRHWTFSSEEQLARLRADANRKFRCKAVANGKVLPNDPVFLEPHEEMTLCKYYEKRLLEFCSVFKPAMPRSVVGTACMYFKRFYLNNSVMEYHPRIIMLTCAFLACKVDEFNVSSPQFVGNLRESPLGQEKALEQILEYELLLIQQLNFHLIVHNPYRPFEGFLIDLKTRYPILENPEILRKTADDFLNRIALTDAYLLYTPSQIALTAILSSASRAGITMESYLSESLMLKENRTCLSQLLDIMKSMRNLVKKYEPPRSEEVAVLKQKLERCHSAELALNVITKKRKGYEDDDYVSKKSKHEEEEWTDDDLVESL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P51946","disprot_id":"DP00307","ncbi_taxon_id":9606,"regions_counter":4,"creator":"ahatos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":323,"region_id":"DP00307r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Three-dimensional structure of human cyclin H, a positive regulator of the CDK-activating kinase. <i> Kim KK, Chamberlin HM, Morgan DO, Kim SH. </i> Nat Struct Biol, 1996","term_id":"IDPO:0000002","curator_id":"ahatos","start":288,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1KXU"}],"reference_id":"8836101","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":10,"region_id":"DP00307r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Three-dimensional structure of human cyclin H, a positive regulator of the CDK-activating kinase. <i> Kim KK, Chamberlin HM, Morgan DO, Kim SH. </i> Nat Struct Biol, 1996","term_id":"IDPO:0000002","curator_id":"ahatos","start":1,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1KXU"}],"reference_id":"8836101","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":323,"region_id":"DP00307r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The crystal structure of human cyclin H. <i> Andersen G, Poterszman A, Egly JM, Moras D, Thierry JC. </i> FEBS Lett, 1996","term_id":"IDPO:0000002","curator_id":"ahatos","start":288,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1JKW"}],"reference_id":"8941715","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":10,"region_id":"DP00307r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The crystal structure of human cyclin H. <i> Andersen G, Poterszman A, Egly JM, Moras D, Thierry JC. </i> FEBS Lett, 1996","term_id":"IDPO:0000002","curator_id":"ahatos","start":1,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1JKW"}],"reference_id":"8941715","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P51946","date":"2016-09-07T10:23:56.000Z","acc":"P51946","name":"Cyclin-H","length":323,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000048D5B","genes":[{"name":{"value":"CCNH"}}],"alphafold_very_low_content":0.1021671826625387,"disorder_content":0.14241486068111456,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"},{"start":288,"end":323,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":288,"end":323,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01208","name":"Uroporphyrinogen decarboxylase (URO-D)","start":15,"end":360}],"gene3D":[{"start":1,"end":367,"id":"3.20.20.210","name":"3.20.20.210"}]},"uniref50":"UniRef50_P06132","sequence":"MEANGLGPQGFPELKNDTFLRAAWGEETDYTPVWCMRQAGRYLPEFRETRAAQDFFSTCRSPEACCELTLQPLRRFPLDAAIIFSDILVVPQALGMEVTMVPGKGPSFPEPLREEQDLERLRDPEVVASELGYVFQAITLTRQRLAGRVPLIGFAGAPWTLMTYMVEGGGSSTMAQAKRWLYQRPQASHQLLRILTDALVPYLVGQVVAGAQALQLFESHAGHLGPQLFNKFALPYIRDVAKQVKARLREAGLAPVPMIIFAKDGHFALEELAQAGYEVVGLDWTVAPKKARECVGKTVTLQGNLDPCALYASEEEIGQLVKQMLDDFGPHRYIANLGHGLYPDMDPEHVGAFVDAVHKHSRLLRQN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P06132","disprot_id":"DP00308","ncbi_taxon_id":9606,"regions_counter":2,"creator":"maspromonte","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":10,"region_id":"DP00308r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The crystal structure of the quorum sensing protein TraR bound to its autoinducer and target DNA. <i> Vannini A, Volpari C, Gargioli C, Muraglia E, Cortese R, De Francesco R, Neddermann P, Marco SD. </i> EMBO J, 2002","term_id":"IDPO:0000002","curator_id":"maspromonte","start":1,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1JPH"}],"reference_id":"12198141","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":10,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"The crystal structure of the quorum sensing protein TraR bound to its autoinducer and target DNA. <i> Vannini A, Volpari C, Gargioli C, Muraglia E, Cortese R, De Francesco R, Neddermann P, Marco SD. </i> EMBO J, 2002","term_id":"GO:0005515","curator_id":"maspromonte","start":1,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"12198141","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00308r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P06132","date":"2016-09-09T20:03:12.000Z","acc":"P06132","name":"Uroporphyrinogen decarboxylase","length":367,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000016B2D1","genes":[{"name":{"value":"UROD","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:12591","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:12591"}}]}}],"alphafold_very_low_content":0.010899182561307902,"disorder_content":0.027247956403269755,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"}],"Molecular function":[{"start":1,"end":10,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00757","name":"Furin-like cysteine rich region","start":185,"end":338},{"id":"PF01030","name":"Receptor L domain","start":57,"end":167},{"id":"PF01030","name":"Receptor L domain","start":361,"end":480},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":714,"end":966},{"id":"PF14843","name":"Growth factor receptor domain IV","start":505,"end":637},{"id":"PF21314","name":"Epidermal growth factor receptor transmembrane-juxtamembrane segment","start":646,"end":681}],"gene3D":[{"start":333,"end":529,"id":"3.80.20.20","name":"Receptor L-domain"},{"start":25,"end":213,"id":"3.80.20.20","name":"Receptor L-domain"},{"start":647,"end":667,"id":"1.20.5.420","name":"Immunoglobulin FC, subunit C"},{"start":530,"end":583,"id":"2.10.220.10","name":"Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2"},{"start":584,"end":646,"id":"2.10.220.10","name":"Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2"},{"start":668,"end":792,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":793,"end":995,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"},{"start":214,"end":332,"id":"2.10.220.10","name":"Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2"}]},"uniref50":"UniRef50_P00533","sequence":"MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P00533","disprot_id":"DP00309","ncbi_taxon_id":9606,"regions_counter":12,"creator":"rpancsa","regions":[{"start":985,"end":1012,"reference_id":"12196540","reference_source":"pmid","reference_html":"Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor. <i> Stamos J, Sliwkowski MX, Eigenbrot C. </i> J Biol Chem, 2002","date":"2022-06-14T20:57:42.737Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"1M14"}],"region_id":"DP00309r002","statement":[{"text":"This region lacks electron density indicating it is disordered.","type":"Curator statement"}]},{"start":989,"end":1000,"reference_id":"12196540","reference_source":"pmid","reference_html":"Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor. <i> Stamos J, Sliwkowski MX, Eigenbrot C. </i> J Biol Chem, 2002","date":"2022-06-14T20:59:48.701Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"1M17"}],"region_id":"DP00309r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"114785","entry_name":"erlotinib"}],"statement":[{"text":"This region lacks electron density indicating it is disordered.","type":"Curator statement"}]},{"start":668,"end":1210,"reference_id":"27872189","reference_source":"pmid","reference_html":"Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases. <i> Keppel TR, Sarpong K, Murray EM, Monsey J, Zhu J, Bose R. </i> J Biol Chem, 2017","date":"2025-05-08T14:03:43.685Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00309r004","statement":[{"text":"The most striking result can be seen within the EGFR CTT where we observe that exchange reaches a plateau very rapidly, often within 5 s of exchange, and the %nex values are indicated by orange and red colors on the heat map. This rapid exchange indicates that the tail is unprotected from exchange when compared with the kinase domain. The observed rapid exchange behavior is characteristic of a highly dynamic and/or frequently exchange-competent conformational state, meaning amide hydrogen bonding between residues is transient or weak in these regions.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T22:30:30.513Z"}},{"start":668,"end":1210,"reference_id":"27872189","reference_source":"pmid","reference_html":"Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases. <i> Keppel TR, Sarpong K, Murray EM, Monsey J, Zhu J, Bose R. </i> J Biol Chem, 2017","date":"2025-05-08T14:08:23.739Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00309r005","statement":[{"text":"However, the CD spectrum observed for EGFR CTT shows a minimum between 195 and 200 nm, which is a characteristic of disordered proteins (Fig. 5A). However, the slightly negative ellipticity at 222 nm indicates the possibility of residual secondary structure. Analysis via the CDSSTR algorithm, an algorithm used to assign secondary structure composition to CD spectra, shows 77% unordered character in the EGFR CTT spectrum (Fig. 5C). These results suggest that much of the EGFR CTT construct has an unfolded conformation in solution.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T22:30:27.112Z"}},{"start":668,"end":1210,"reference_id":"27872189","reference_source":"pmid","reference_html":"Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases. <i> Keppel TR, Sarpong K, Murray EM, Monsey J, Zhu J, Bose R. </i> J Biol Chem, 2017","date":"2025-05-08T14:10:18.147Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00309r006","statement":[{"text":"EGFR CTT elutes from the SEC column before 13 ml of buffer volume. Despite having a lower molecular weight, the EGFR CTT elutes earlier than carbonic anhydrase, which elutes just after 15 ml of buffer. The expected Stokes radius of carbonic anhydrase is 2.4 nm (44). This earlier elution indicates that the EGFR CTT conformational ensemble is more extended than that of carbonic anhydrase, which has a globular structure.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T22:30:23.577Z"}},{"start":668,"end":1210,"reference_id":"27872189","reference_source":"pmid","reference_html":"Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases. <i> Keppel TR, Sarpong K, Murray EM, Monsey J, Zhu J, Bose R. </i> J Biol Chem, 2017","date":"2025-05-08T14:12:09.425Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00309r007","statement":[{"text":"The EGFR CTT, which has a molecular mass of 26 kDa, was determined to have a hydrodynamic radius of 5.3 nm. For a comparison, we also analyzed BSA, a globular protein with a molecular mass of 66 kDa, and the hydrodynamic radius of BSA was measured to be 4.8 nm. This demonstrates that EGFR CTT has a larger hydrodynamic radius than a globular protein more than 2.5 times its size.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T22:30:19.816Z"}},{"start":668,"end":1210,"reference_id":"27872189","reference_source":"pmid","reference_html":"Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases. <i> Keppel TR, Sarpong K, Murray EM, Monsey J, Zhu J, Bose R. </i> J Biol Chem, 2017","date":"2025-05-08T14:13:02.442Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00309r008","statement":[{"text":"For a globular protein, the expected f/fmin would fall between 1.15 and 1.3 (47–49). We determined the f/fmin value for EGFR CTT to be much greater, at 1.77, which is consistent with this being an IDR.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T22:30:14.357Z"}},{"start":668,"end":1210,"reference_id":"27872189","reference_source":"pmid","reference_html":"Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases. <i> Keppel TR, Sarpong K, Murray EM, Monsey J, Zhu J, Bose R. </i> J Biol Chem, 2017","date":"2025-05-08T14:13:59.606Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00309r009","statement":[{"text":"In contrast, EGFR CTT shows a hyperbolic shape on the Kratky plot, indicating an intrinsically disordered region (Fig. 7C).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T22:30:15.963Z"}},{"start":1067,"end":1071,"reference_id":"27872189","reference_source":"pmid","reference_html":"Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases. <i> Keppel TR, Sarpong K, Murray EM, Monsey J, Zhu J, Bose R. </i> J Biol Chem, 2017","date":"2025-05-08T14:25:51.612Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00309r010","statement":[{"text":"We show, through Western blotting identification of specific phosphorylated tyrosine residues (EGFR Tyr-1068 and Tyr-1173) in the EGFR CTT (Fig. 4C), that the EGFR CTT is recognized and phosphorylated by the EGFR kinase domain even when these two domains are expressed as separated constructs.","type":"Results"},{"text":"There is some discrepancy in the numbering. Tyr-1068 mentioned in the paper corresponds to Tyr1069 in UniProt sequence, while Tyr-1173 corresponds to Tyr1172 in UniProt sequence.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T22:30:59.084Z"}},{"start":1170,"end":1174,"reference_id":"27872189","reference_source":"pmid","reference_html":"Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases. <i> Keppel TR, Sarpong K, Murray EM, Monsey J, Zhu J, Bose R. </i> J Biol Chem, 2017","date":"2025-05-08T14:26:07.731Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00309r011","statement":[{"text":"We show, through Western blotting identification of specific phosphorylated tyrosine residues (EGFR Tyr-1068 and Tyr-1173) in the EGFR CTT (Fig. 4C), that the EGFR CTT is recognized and phosphorylated by the EGFR kinase domain even when these two domains are expressed as separated constructs.","type":"Results"},{"text":"There is some discrepancy in the numbering. Tyr-1068 mentioned in the paper corresponds to Tyr1069 in UniProt sequence, while Tyr-1173 corresponds to Tyr1172 in UniProt sequence.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T22:30:55.471Z"}},{"start":668,"end":1210,"reference_id":"27872189","reference_source":"pmid","reference_html":"Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases. <i> Keppel TR, Sarpong K, Murray EM, Monsey J, Zhu J, Bose R. </i> J Biol Chem, 2017","date":"2025-05-08T14:30:15.134Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P62993","operator":null,"partner_start":60,"partner_end":152}],"region_id":"DP00309r012","statement":[{"text":"However, once phosphorylated, EGFR CTT was bound by GST-Grb2-SH2 and was pulled down by glutathione-agarose.","type":"Results"},{"text":"The interaction is dependent on phosphorylation of particular Tyr residues within the EGFR C-terminal tail.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T22:30:39.312Z"}}],"released":"2016_10","uniref100":"UniRef100_P00533","date":"2016-09-07T13:07:56.000Z","acc":"P00533","name":"Epidermal growth factor receptor","length":1210,"organism":"Homo sapiens","dataset":["Autophagy-related proteins","Cancer-related proteins"],"UniParc":"UPI0000050F30","genes":[{"name":{"value":"EGFR","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:3236","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:3236"}}]},"synonyms":[{"value":"ERBB"},{"value":"ERBB1"},{"value":"HER1"}]}],"alphafold_very_low_content":0.21735537190082643,"disorder_content":0.4487603305785124,"disprot_consensus":{"full":[{"start":668,"end":1210,"type":"D"}],"Structural state":[{"start":668,"end":1210,"type":"D"}],"Disorder function":[{"start":1067,"end":1071,"type":"F"},{"start":1170,"end":1174,"type":"F"}],"Molecular function":[{"start":668,"end":1210,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03463","name":"eRF1 domain 1","start":13,"end":140},{"id":"PF03464","name":"eRF1 domain 2","start":145,"end":277},{"id":"PF03465","name":"eRF1 domain 3","start":280,"end":417}],"gene3D":[{"start":137,"end":276,"id":"3.30.420.60","name":"eRF1 domain 2"},{"start":278,"end":437,"id":"3.30.1330.30","name":"3.30.1330.30"},{"start":3,"end":136,"id":"3.30.960.10","name":"eRF1 domain 1"}]},"uniref50":"UniRef50_P62495","sequence":"MADDPSAADRNVEIWKIKKLIKSLEAARGNGTSMISLIIPPKDQISRVAKMLADEFGTASNIKSRVNRLSVLGAITSVQQRLKLYNKVPPNGLVVYCGTIVTEEGKEKKVNIDFEPFKPINTSLYLCDNKFHTEALTALLSDDSKFGFIVIDGSGALFGTLQGNTREVLHKFTVDLPKKHGRGGQSALRFARLRMEKRHNYVRKVAETAVQLFISGDKVNVAGLVLAGSADFKTELSQSDMFDQRLQSKVLKLVDISYGGENGFNQAIELSTEVLSNVKFIQEKKLIGRYFDEISQDTGKYCFGVEDTLKALEMGAVEILIVYENLDIMRYVLHCQGTEEEKILYLTPEQEKDKSHFTDKETGQEHELIESMPLLEWFANNYKKFGATLEIVTDKSQEGSQFVKGFGGIGGILRYRVDFQGMEYQGGDDEFFDLDDY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P62495","disprot_id":"DP00310","ncbi_taxon_id":9606,"regions_counter":5,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":342,"region_id":"DP00310r001","released":"2024_06","ec_id":"ECO:0006220","reference_html":"The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. <i> Song H, Mugnier P, Das AK, Webb HM, Evans DR, Tuite MF, Hemmings BA, Barford D. </i> Cell, 2000","term_id":"IDPO:0000002","curator_id":"vnugnes","start":333,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10676813","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2024-03-26T13:54:58.349Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1DT9"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The final structure includes residues 5 to 422. Three regions of the polypeptide are not visible in the electron density map and are assumed to be disordered, namely residues 333–342 and 358–370 and 15 residues at the C terminus.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":370,"region_id":"DP00310r002","released":"2024_06","ec_id":"ECO:0006220","reference_html":"The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. <i> Song H, Mugnier P, Das AK, Webb HM, Evans DR, Tuite MF, Hemmings BA, Barford D. </i> Cell, 2000","term_id":"IDPO:0000002","curator_id":"vnugnes","start":358,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10676813","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2024-03-26T13:54:48.535Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1DT9"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The final structure includes residues 5 to 422. Three regions of the polypeptide are not visible in the electron density map and are assumed to be disordered, namely residues 333–342 and 358–370 and 15 residues at the C terminus.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":437,"region_id":"DP00310r003","released":"2024_06","ec_id":"ECO:0006220","reference_html":"The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. <i> Song H, Mugnier P, Das AK, Webb HM, Evans DR, Tuite MF, Hemmings BA, Barford D. </i> Cell, 2000","term_id":"IDPO:0000002","curator_id":"vnugnes","start":423,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10676813","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2024-03-26T13:54:10.748Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1DT9"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The final structure includes residues 5 to 422. Three regions of the polypeptide are not visible in the electron density map and are assumed to be disordered, namely residues 333–342 and 358–370 and 15 residues at the C terminus.","type":"Results"}]},{"start":414,"end":437,"reference_id":"24452424","reference_source":"pmid","reference_html":"Backbone (1)H, (13)C and (15)N resonance assignments of the human eukaryotic release factor eRF1. <i> Polshakov VI, Eliseev BD, Frolova LY, Chang CF, Huang TH. </i> Biomol NMR Assign, 2015","date":"2024-05-06T16:03:22.083Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0520","term_name":"HA","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"region_id":"DP00310r004","sequence_construct":"MADDPSAADRNVEIWKIKKLIKSLEAARGNGTSMISLIIPPKDQISRVAKMLADEFGTASNIKSRVNRLSVLGAITSVQQRLKLYNKVPPNGLVVYCGTIVTEEGKEKKVNIDFEPFKPINTSLYLCDNKFHTEALTALLSDDSKFGFIVIDGSGALFGTLQGNTREVLHKFTVDLPKKHGRGGQSALRFARLRMEKRHNYVRKVAETAVQLFISGDKVNVAGLVLAGSADFKTELSQSDMFDQRLQSKVLKLVDISYGGENGFNQAIELSTEVLSNVKFIQEKKLIGRYFDEISQDTGKYCFGVEDTLKALEMGAVEILIVYENLDIMRYVLHCQGTEEEKILYLTPEQEKDKSHFTDKETGQEHELIESMPLLEWFANNYKKFGATLEIVTDKSQEGSQFVKGFGGIGGILRYRVDFQGMEYQGGDDEFFDLDDYLEHHHHHH","statement":[{"text":"There are many signals with high intensity due to increased mobility of corresponding residues. These are primarily from unstructured C-terminal tail (residues 414–437) and minidomain 329–372.","type":"Results"}]},{"start":329,"end":372,"reference_id":"24452424","reference_source":"pmid","reference_html":"Backbone (1)H, (13)C and (15)N resonance assignments of the human eukaryotic release factor eRF1. <i> Polshakov VI, Eliseev BD, Frolova LY, Chang CF, Huang TH. </i> Biomol NMR Assign, 2015","date":"2024-05-06T16:03:29.874Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0520","term_name":"HA","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"region_id":"DP00310r005","sequence_construct":"MADDPSAADRNVEIWKIKKLIKSLEAARGNGTSMISLIIPPKDQISRVAKMLADEFGTASNIKSRVNRLSVLGAITSVQQRLKLYNKVPPNGLVVYCGTIVTEEGKEKKVNIDFEPFKPINTSLYLCDNKFHTEALTALLSDDSKFGFIVIDGSGALFGTLQGNTREVLHKFTVDLPKKHGRGGQSALRFARLRMEKRHNYVRKVAETAVQLFISGDKVNVAGLVLAGSADFKTELSQSDMFDQRLQSKVLKLVDISYGGENGFNQAIELSTEVLSNVKFIQEKKLIGRYFDEISQDTGKYCFGVEDTLKALEMGAVEILIVYENLDIMRYVLHCQGTEEEKILYLTPEQEKDKSHFTDKETGQEHELIESMPLLEWFANNYKKFGATLEIVTDKSQEGSQFVKGFGGIGGILRYRVDFQGMEYQGGDDEFFDLDDYLEHHHHHH","statement":[{"text":"There are many signals with high intensity due to increased mobility of corresponding residues. These are primarily from unstructured C-terminal tail (residues 414–437) and minidomain 329–372.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P62495","date":"2016-09-06T10:12:00.000Z","acc":"P62495","name":"Eukaryotic peptide chain release factor subunit 1","length":437,"organism":"Homo sapiens","dataset":["RNA-binding proteins"],"UniParc":"UPI00001110CB","genes":[{"name":{"value":"ETF1"},"synonyms":[{"value":"ERF1"},{"value":"RF1"},{"value":"SUP45L1"}]}],"alphafold_very_low_content":0.041189931350114416,"disorder_content":0.15560640732265446,"disprot_consensus":{"full":[{"start":329,"end":372,"type":"D"},{"start":414,"end":437,"type":"D"}],"Structural state":[{"start":329,"end":372,"type":"D"},{"start":414,"end":437,"type":"D"}]}},{"features":{"gene3D":[{"start":26,"end":120,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":121,"end":215,"id":"2.60.40.10","name":"Immunoglobulins"}],"pfam":[{"id":"PF00047","name":"Immunoglobulin domain","start":134,"end":206}]},"uniref50":"UniRef50_P24071","sequence":"MDPKQTTLLCLVLCLGQRIQAQEGDFPMPFISAKSSPVIPLDGSVKIQCQAIREAYLTQLMIIKNSTYREIGRRLKFWNETDPEFVIDHMDANKAGRYQCQYRIGHYRFRYSDTLELVVTGLYGKPFLSADRGLVLMPGENISLTCSSAHIPFDRFSLAKEGELSLPQHQSGEHPANFSLGPVDLNVSGIYRCYGWYNRSPYLWSFPSNALELVVTDSIHQDYTTQNLIRMAVAGLVLVALLAILVENWHSHTALNKEASADVAEPSWSQQMCQPGLTFARTPSVCK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P24071","disprot_id":"DP00311","ncbi_taxon_id":9606,"regions_counter":1,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":229,"region_id":"DP00311r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the ectodomain of human FcalphaRI. <i> Ding Y, Xu G, Yang M, Yao M, Gao GF, Wang L, Zhang W, Rao Z. </i> J Biol Chem, 2003","term_id":"IDPO:0000002","curator_id":"fquaglia","start":217,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12783876","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1UCT"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P24071","date":"2016-08-12T12:25:28.000Z","acc":"P24071","name":"Immunoglobulin alpha Fc receptor","length":287,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000011B429","genes":[{"name":{"value":"FCAR"},"synonyms":[{"value":"CD89"}]}],"alphafold_very_low_content":0.08362369337979095,"disorder_content":0.04529616724738676,"disprot_consensus":{"full":[{"start":217,"end":229,"type":"D"}],"Structural state":[{"start":217,"end":229,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00790","name":"VHS domain","start":8,"end":143},{"id":"PF02883","name":"Adaptin C-terminal domain","start":514,"end":631},{"id":"PF03127","name":"GAT domain","start":222,"end":300},{"id":"PF18308","name":"N-terminal extension of GAT domain","start":169,"end":207}],"gene3D":[{"start":3,"end":163,"id":"1.25.40.90","name":"1.25.40.90"},{"start":210,"end":314,"id":"1.20.58.160","name":"1.20.58.160"},{"start":164,"end":209,"id":"1.20.5.170","name":"1.20.5.170"},{"start":487,"end":639,"id":"2.60.40.1230","name":"2.60.40.1230"}]},"uniref50":"UniRef50_Q9UJY5","sequence":"MEPAMEPETLEARINRATNPLNKELDWASINGFCEQLNEDFEGPPLATRLLAHKIQSPQEWEAIQALTVLETCMKSCGKRFHDEVGKFRFLNELIKVVSPKYLGSRTSEKVKNKILELLYSWTVGLPEEVKIAEAYQMLKKQGIVKSDPKLPDDTTFPLPPPRPKNVIFEDEEKSKMLARLLKSSHPEDLRAANKLIKEMVQEDQKRMEKISKRVNAIEEVNNNVKLLTEMVMSHSQGGAAAGSSEDLMKELYQRCERMRPTLFRLASDTEDNDEALAEILQANDNLTQVINLYKQLVRGEEVNGDATAGSIPGSTSALLDLSGLDLPPAGTTYPAMPTRPGEQASPEQPSASVSLLDDELMSLGLSDPTPPSGPSLDGTGWNSFQSSDATEPPAPALAQAPSMESRPPAQTSLPASSGLDDLDLLGKTLLQQSLPPESQQVRWEKQQPTPRLTLRDLQNKSSSCSSPSSSATSLLHTVSPEPPRPPQQPVPTELSLASITVPLESIKPSNILPVTVYDQHGFRILFHFARDPLPGRSDVLVVVVSMLSTAPQPIRNIVFQSAVPKVMKVKLQPPSGTELPAFNPIVHPSAITQVLLLANPQKEKVRLRYKLTFTMGDQTYNEMGDVDQFPPPETWGSL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UJY5","disprot_id":"DP00314","ncbi_taxon_id":9606,"regions_counter":4,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":189,"region_id":"DP00314r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the GAT domain of human GGA1: a syntaxin amino-terminal domain fold in an endosomal trafficking adaptor. <i> Suer S, Misra S, Saidi LF, Hurley JH. </i> Proc Natl Acad Sci U S A, 2003","term_id":"IDPO:0000002","curator_id":"mnecci","start":166,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12668765","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1NWM"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":170,"region_id":"DP00314r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the human GGA1 GAT domain. <i> Zhu G, Zhai P, He X, Terzyan S, Zhang R, Joachimiak A, Tang J, Zhang XC. </i> Biochemistry, 2003","term_id":"IDPO:0000002","curator_id":"mnecci","start":144,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12767220","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1OXZ"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":326,"region_id":"DP00314r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the human GGA1 GAT domain. <i> Zhu G, Zhai P, He X, Terzyan S, Zhang R, Joachimiak A, Tang J, Zhang XC. </i> Biochemistry, 2003","term_id":"IDPO:0000002","curator_id":"mnecci","start":303,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12767220","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1OXZ"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q9UJY5","date":"2016-09-06T10:40:15.000Z","acc":"Q9UJY5","name":"ADP-ribosylation factor-binding protein GGA1","length":639,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000001BEE","genes":[{"name":{"value":"GGA1"}}],"alphafold_very_low_content":0.29264475743348983,"disorder_content":0.10954616588419405,"disprot_consensus":{"full":[{"start":144,"end":189,"type":"D"},{"start":303,"end":326,"type":"D"}],"Structural state":[{"start":144,"end":189,"type":"D"},{"start":303,"end":326,"type":"D"}]}},{"features":{"pfam":[{"id":"PF13365","name":"Trypsin-like peptidase domain","start":182,"end":320},{"id":"PF17820","name":"PDZ domain","start":395,"end":443}],"gene3D":[{"start":356,"end":457,"id":"2.30.42.10","name":"2.30.42.10"},{"start":140,"end":351,"id":"2.40.10.120","name":"2.40.10.120"}]},"uniref50":"UniRef50_O43464","sequence":"MAAPRAGRGAGWSLRAWRALGGIRWGRRPRLTPDLRALLTSGTSDPRARVTYGTPSLWARLSVGVTEPRACLTSGTPGPRAQLTAVTPDTRTREASENSGTRSRAWLAVALGAGGAVLLLLWGGGRGPPAVLAAVPSPPPASPRSQYNFIADVVEKTAPAVVYIEILDRHPFLGREVPISNGSGFVVAADGLIVTNAHVVADRRRVRVRLLSGDTYEAVVTAVDPVADIATLRIQTKEPLPTLPLGRSADVRQGEFVVAMGSPFALQNTITSGIVSSAQRPARDLGLPQTNVEYIQTDAAIDFGNSGGPLVNLDGEVIGVNTMKVTAGISFAIPSDRLREFLHRGEKKNSSSGISGSQRRYIGVMMLTLSPSILAELQLREPSFPDVQHGVLIHKVILGSPAHRAGLRPGDVILAIGEQMVQNAEDVYEAVRTQSQLAVQIRRGRETLTLYVTPEVTE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O43464","disprot_id":"DP00315","ncbi_taxon_id":9606,"regions_counter":10,"creator":"smribeiro","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":358,"region_id":"DP00315r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi. <i> Li W, Srinivasula SM, Chai J, Li P, Wu JW, Zhang Z, Alnemri ES, Shi Y. </i> Nat Struct Biol, 2002","statement":[{"text":"The N-terminal 5 residues and a 15-residue linker sequence are disordered in the crystals.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"smribeiro","start":344,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1LCY"}],"reference_id":"11967569","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-22T13:07:12.399Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":292,"region_id":"DP00315r004","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Molecular motion regulates the activity of the Mitochondrial Serine Protease HtrA2. <i> Merski M, Moreira C, Abreu RM, Ramos MJ, Fernandes PA, Martins LM, Pereira PJB, Macedo-Ribeiro S. </i> Cell Death Dis, 2017","statement":[{"text":"There were notable gaps in the electron density for the N- and C-termini, within the L3 loop (between residues R280-V292 with small variations in the different structures), and for the linker region between the protease and PDZ domains (G345-S357) common for all the structures described in this work (Figure 1 and Supplementary Information).","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":280,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-22T13:05:41.469Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5M3N"}],"reference_id":"29022916","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:4478249"}]},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":358,"term_name":"flexible linker","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi. <i> Li W, Srinivasula SM, Chai J, Li P, Wu JW, Zhang Z, Alnemri ES, Shi Y. </i> Nat Struct Biol, 2002","statement":[{"text":"On the other end, the PDZ domain is covalently linked to the protease domain through a flexible linker sequence (residues 211–225).","type":"Results"}],"term_id":"IDPO:0000033","curator_id":"vnugnes","start":344,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"11967569","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-22T13:10:02.147Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00315r005","ec_go":"EXP","disprot_namespace":"Disorder function","cross_refs":[{"db":"PDB","id":"1LCY"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":357,"region_id":"DP00315r006","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Molecular motion regulates the activity of the Mitochondrial Serine Protease HtrA2. <i> Merski M, Moreira C, Abreu RM, Ramos MJ, Fernandes PA, Martins LM, Pereira PJB, Macedo-Ribeiro S. </i> Cell Death Dis, 2017","statement":[{"text":"There were notable gaps in the electron density for the N- and C-termini, within the L3 loop (between residues R280-V292 with small variations in the different structures), and for the linker region between the protease and PDZ domains (G345-S357) common for all the structures described in this work (Figure 1 and Supplementary Information).","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":344,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-22T13:04:12.147Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5M3N"}],"reference_id":"29022916","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:4478249"}]},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":357,"term_name":"flexible linker","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Molecular motion regulates the activity of the Mitochondrial Serine Protease HtrA2. <i> Merski M, Moreira C, Abreu RM, Ramos MJ, Fernandes PA, Martins LM, Pereira PJB, Macedo-Ribeiro S. </i> Cell Death Dis, 2017","term_id":"IDPO:0000033","curator_id":"vnugnes","start":344,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"29022916","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-22T13:04:40.406Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00315r007","ec_go":"EXP","disprot_namespace":"Disorder function","cross_refs":[{"db":"PDB","id":"5M3N"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:4478249"}],"statement":[{"text":"There were notable gaps in the electron density for the N- and C-termini, within the L3 loop (between residues R280-V292 with small variations in the different structures), and for the linker region between the protease and PDZ domains (G345-S357) common for all the structures described in this work (Figure 1 and Supplementary Information).","type":"Methods"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":358,"region_id":"DP00315r008","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Distinct 3D Architecture and Dynamics of the Human HtrA2(Omi) Protease and Its Mutated Variants. <i> Gieldon A, Zurawa-Janicka D, Jarzab M, Wenta T, Golik P, Dubin G, Lipinska B, Ciarkowski J. </i> PLoS One, 2016","statement":[{"text":"1LCY and 5FHT have 3 unresolved regions, viz: the N-terminal IAP-binding motif 134AVPSP138 and 134AVPSPPPA141; L3β8~β9 282ARDLGLPQT290 and 281PARDLG286; and the PD~PDZ linker 344RGEKKNSSSGISGSQ358 and 345GEKKNSSSGISGSQ358, respectively.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"smribeiro","start":345,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5FHT"}],"reference_id":"27571206","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-19T19:29:57.746Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":358,"term_name":"flexible linker","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Distinct 3D Architecture and Dynamics of the Human HtrA2(Omi) Protease and Its Mutated Variants. <i> Gieldon A, Zurawa-Janicka D, Jarzab M, Wenta T, Golik P, Dubin G, Lipinska B, Ciarkowski J. </i> PLoS One, 2016","term_id":"IDPO:0000033","curator_id":"vnugnes","start":345,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27571206","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-19T19:32:26.147Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00315r009","ec_go":"EXP","disprot_namespace":"Disorder function","cross_refs":[{"db":"PDB","id":"5FHT"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:923"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:813"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:4478249"}],"statement":[{"text":"1LCY and 5FHT have 3 unresolved regions, viz: the N-terminal IAP-binding motif 134AVPSP138 and 134AVPSPPPA141; L3β8~β9 282ARDLGLPQT290 and 281PARDLG286; and the PD~PDZ linker 344RGEKKNSSSGISGSQ358 and 345GEKKNSSSGISGSQ358, respectively.","type":"Methods"}]}],"released":"2016_10","uniref100":"UniRef100_O43464","date":"2016-08-12T12:46:22.000Z","acc":"O43464","name":"Serine protease HTRA2, mitochondrial","length":458,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI0000155ED6","genes":[{"name":{"value":"HTRA2"},"synonyms":[{"value":"OMI"},{"value":"PRSS25"}]}],"alphafold_very_low_content":0.32096069868995636,"disorder_content":0.0611353711790393,"disprot_consensus":{"full":[{"start":280,"end":292,"type":"D"},{"start":344,"end":358,"type":"D"}],"Structural state":[{"start":280,"end":292,"type":"D"},{"start":344,"end":358,"type":"D"}],"Disorder function":[{"start":344,"end":358,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00870","name":"P53 DNA-binding domain","start":118,"end":308},{"id":"PF07647","name":"SAM domain (Sterile alpha motif)","start":487,"end":548},{"id":"PF07710","name":"P53 tetramerisation motif","start":345,"end":384}],"gene3D":[{"start":486,"end":548,"id":"1.10.150.50","name":"Transcription Factor, Ets-1"},{"start":349,"end":399,"id":"4.10.170.10","name":"p53-like tetramerisation domain"},{"start":111,"end":318,"id":"2.60.40.720","name":"2.60.40.720"}]},"uniref50":"UniRef50_O15350","sequence":"MAQSTATSPDGGTTFEHLWSSLEPDSTYFDLPQSSRGNNEVVGGTDSSMDVFHLEGMTTSVMAQFNLLSSTMDQMSSRAASASPYTPEHAASVPTHSPYAQPSSTFDTMSPAPVIPSNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDVVKRCPNHELGRDFNEGQSAPASHLIRVEGNNLSQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIIITLEMRDGQVLGRRSFEGRICACPGRDRKADEDHYREQQALNESSAKNGAASKRAFKQSPPAVPALGAGVKKRRHGDEDTYYLQVRGRENFEILMKLKESLELMELVPQPLVDSYRQQQQLLQRPSHLQPPSYGPVLSPMNKVHGGMNKLPSVNQLVGQPPPHSSAATPNLGPVGPGMLNNHGHAVPANGEMSSSHSAQSMVSGSHCTPPPPYHADPSLVSFLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMTIWRGLQDLKQGHDYSTAQQLLRSSNAATISIGGSGELQRQRVMEAVHFRVRHTITIPNRGGPGGGPDEWADFGFDLPDCKARKQPIKEEFTEAEIH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O15350","disprot_id":"DP00319","ncbi_taxon_id":9606,"regions_counter":2,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":564,"region_id":"DP00319r002","released":"2022_06","ec_id":"ECO:0006220","reference_html":"Structure of the C-terminal sterile alpha-motif (SAM) domain of human p73 alpha. <i> Wang WK, Bycroft M, Foster NW, Buckle AM, Fersht AR, Chen YW. </i> Acta Crystallogr D Biol Crystallogr, 2001","term_id":"IDPO:0000002","curator_id":"fquaglia","start":549,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11264583","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-05-16T10:48:14.710Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1DXS"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The high R factor and R free are consistent with a large extent of disorder (23 residues of 80). There is sufficient volume to accommodate these missing residues (seven at the N-terminus and 16 at the C-terminus) in the crystal lattice.","type":"Methods"},{"text":"The first seven N-terminal residues, including two plasmid-encoded residues and residues 487-491, and the C-terminal residues 549-564 are disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T19:07:34.229Z"}}],"released":"2016_10","uniref100":"UniRef100_O15350","date":"2016-09-06T10:52:53.000Z","acc":"O15350","name":"Tumor protein p73","length":636,"organism":"Homo sapiens","dataset":["Autophagy-related proteins","NDDs-related proteins"],"UniParc":"UPI000002E988","genes":[{"name":{"value":"TP73"},"synonyms":[{"value":"P73"}]}],"alphafold_very_low_content":0.4716981132075472,"disorder_content":0.025157232704402517,"disprot_consensus":{"full":[{"start":549,"end":564,"type":"D"}],"Structural state":[{"start":549,"end":564,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00079","name":"Serpin (serine protease inhibitor)","start":35,"end":402}],"gene3D":[{"start":194,"end":402,"id":"2.30.39.10","name":"Alpha-1-antitrypsin, domain 1"},{"start":42,"end":368,"id":"3.30.497.10","name":"Antithrombin, subunit I, domain 2"}]},"uniref50":"UniRef50_P20961","sequence":"MQMSPALTCLVLGLALVFGEGSAVHHPPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAPYEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P05121","disprot_id":"DP00320","ncbi_taxon_id":9606,"regions_counter":4,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":370,"region_id":"DP00320r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of plasminogen activator inhibitor-1 in an active conformation with normal thermodynamic stability. <i> Jensen JK, Thompson LC, Bucci JC, Nissen P, Gettins PG, Peterson CB, Andreasen PA, Morth JP. </i> J Biol Chem, 2011","term_id":"IDPO:0000002","curator_id":"esalladini","start":355,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"21697084","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3Q02"},{"db":"PDB","id":"3Q03"}],"term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"As expected, the electron density of the solvent-exposed flexible RCL (Ser331–Pro349) is missing and reflects the ability of the RCL to adopt different conformations suitable for the interaction with target proteases (10).","type":"Results"},{"text":"The numbering of the IDR that includes the reactive center loop (RCL) of PAI-1, corresponds to region 355-370 of the associated UniProt sequence, since PDB:3Q02 spans residues 24-402 of the protein.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-16T12:22:05.058Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":361,"end":370,"reference_id":"12808446","reference_source":"pmid","reference_html":"How vitronectin binds PAI-1 to modulate fibrinolysis and cell migration. <i> Zhou A, Huntington JA, Pannu NS, Carrell RW, Read RJ. </i> Nat Struct Biol, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1OC0"}],"region_id":"DP00320r003","statement":[{"text":"Dashed lines indicate disordered residues in the reactive center loop (RCL) of PAI-1 and residues leading to the RGD sequence of somatomedin B.","type":"Figure"},{"text":"The final model includes residues 6–337 and 348–379 of PAI-1 and 3–39 of SMB.","type":"Methods"},{"text":"The numbering of the IDR that includes the reactive center loop (RCL) of PAI-1, corresponds to region 361-370 of the associated UniProt sequence, since PDB:1OC0 spans residues 24-402 of the protein.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-08T10:42:13.921Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":355,"end":370,"reference_id":"21697084","reference_source":"pmid","reference_html":"Crystal structure of plasminogen activator inhibitor-1 in an active conformation with normal thermodynamic stability. <i> Jensen JK, Thompson LC, Bucci JC, Nissen P, Gettins PG, Peterson CB, Andreasen PA, Morth JP. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"3Q02"},{"db":"PDB","id":"3Q03"}],"region_id":"DP00320r004","statement":[{"text":"The numbering of the IDR that includes the reactive center loop (RCL) of PAI-1, corresponds to region 355-370 of the associated UniProt sequence, since PDB:3Q02 spans residues 24-402 of the protein.","type":"Curator statement"},{"text":"As expected, the electron density of the solvent-exposed flexible RCL (Ser331–Pro349) is missing and reflects the ability of the RCL to adopt different conformations suitable for the interaction with target proteases (10).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-16T12:36:38.119Z"},"term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P05121","date":"2016-08-22T16:21:41.000Z","acc":"P05121","name":"Plasminogen activator inhibitor 1","length":402,"organism":"Homo sapiens","dataset":["Extracellular matrix proteins","NDDs-related proteins"],"UniParc":"UPI0000000CAB","genes":[{"name":{"value":"SERPINE1"},"synonyms":[{"value":"PAI1"},{"value":"PLANH1"}]}],"alphafold_very_low_content":0.08208955223880597,"disorder_content":0.03980099502487562,"disprot_consensus":{"full":[{"start":355,"end":370,"type":"D"}],"Structural state":[{"start":355,"end":370,"type":"D"}],"Molecular function":[{"start":355,"end":370,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03068","name":"Protein-arginine deiminase (PAD)","start":284,"end":660},{"id":"PF08526","name":"Protein-arginine deiminase (PAD) N-terminal domain","start":1,"end":111},{"id":"PF08527","name":"Protein-arginine deiminase (PAD) middle domain","start":113,"end":273}],"gene3D":[{"start":119,"end":293,"id":"2.60.40.1700","name":"Protein-arginine deiminase, central domain"},{"start":1,"end":118,"id":"2.60.40.1860","name":"Protein-arginine deiminase, N-terminal domain"},{"start":294,"end":663,"id":"3.75.10.10","name":"L-arginine/glycine Amidinotransferase; Chain A"}]},"uniref50":"UniRef50_Q9UM07","sequence":"MAQGTLIRVTPEQPTHAVCVLGTLTQLDICSSAPEDCTSFSINASPGVVVDIAHGPPAKKKSTGSSTWPLDPGVEVTLTMKVASGSTGDQKVQISYYGPKTPPVKALLYLTGVEISLCADITRTGKVKPTRAVKDQRTWTWGPCGQGAILLVNCDRDNLESSAMDCEDDEVLDSEDLQDMSLMTLSTKTPKDFFTNHTLVLHVARSEMDKVRVFQATRGKLSSKCSVVLGPKWPSHYLMVPGGKHNMDFYVEALAFPDTDFPGLITLTISLLDTSNLELPEAVVFQDSVVFRVAPWIMTPNTQPPQEVYACSIFENEDFLKSVTTLAMKAKCKLTICPEEENMDDQWMQDEMEIGYIQAPHKTLPVVFDSPRNRGLKEFPIKRVMGPDFGYVTRGPQTGGISGLDSFGNLEVSPPVTVRGKEYPLGRILFGDSCYPSNDSRQMHQALQDFLSAQQVQAPVKLYSDWLSVGHVDEFLSFVPAPDRKGFRLLLASPRSCYKLFQEQQNEGHGEALLFEGIKKKKQQKIKNILSNKTLREHNSFVERCIDWNRELLKRELGLAESDIIDIPQLFKLKEFSKAEAFFPNMVNMLVLGKHLGIPKPFGPVINGRCCLEEKVCSLLEPLGLQCTFINDFFTYHIRHGEVHCGTNVRRKPFSFKWWNMVP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UM07","disprot_id":"DP00321","ncbi_taxon_id":9606,"regions_counter":11,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":65,"region_id":"DP00321r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for Ca(2+)-induced activation of human PAD4. <i> Arita K, Hashimoto H, Shimizu T, Nakashima K, Yamada M, Sato M. </i> Nat Struct Mol Biol, 2004","term_id":"IDPO:0000002","curator_id":"fquaglia","start":55,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15247907","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1WD8"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":171,"region_id":"DP00321r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for Ca(2+)-induced activation of human PAD4. <i> Arita K, Hashimoto H, Shimizu T, Nakashima K, Yamada M, Sato M. </i> Nat Struct Mol Biol, 2004","term_id":"IDPO:0000002","curator_id":"fquaglia","start":158,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15247907","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1WD8"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":348,"region_id":"DP00321r007","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for Ca(2+)-induced activation of human PAD4. <i> Arita K, Hashimoto H, Shimizu T, Nakashima K, Yamada M, Sato M. </i> Nat Struct Mol Biol, 2004","term_id":"IDPO:0000002","curator_id":"fquaglia","start":338,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15247907","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1WD8"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":387,"region_id":"DP00321r008","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for Ca(2+)-induced activation of human PAD4. <i> Arita K, Hashimoto H, Shimizu T, Nakashima K, Yamada M, Sato M. </i> Nat Struct Mol Biol, 2004","term_id":"IDPO:0000002","curator_id":"fquaglia","start":371,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15247907","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1WD8"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":644,"region_id":"DP00321r011","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for Ca(2+)-induced activation of human PAD4. <i> Arita K, Hashimoto H, Shimizu T, Nakashima K, Yamada M, Sato M. </i> Nat Struct Mol Biol, 2004","term_id":"IDPO:0000002","curator_id":"fquaglia","start":633,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15247907","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1WD8"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q9UM07","date":"2016-08-25T12:34:05.000Z","acc":"Q9UM07","name":"Protein-arginine deiminase type-4","length":663,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00001314B5","genes":[{"name":{"value":"PADI4"},"synonyms":[{"value":"PAD4"},{"value":"PADI5"},{"value":"PDI5"}]}],"alphafold_very_low_content":0.012066365007541479,"disorder_content":0.09803921568627451,"disprot_consensus":{"full":[{"start":55,"end":65,"type":"D"},{"start":158,"end":171,"type":"D"},{"start":338,"end":348,"type":"D"},{"start":371,"end":387,"type":"D"},{"start":633,"end":644,"type":"D"}],"Structural state":[{"start":55,"end":65,"type":"D"},{"start":158,"end":171,"type":"D"},{"start":338,"end":348,"type":"D"},{"start":371,"end":387,"type":"D"},{"start":633,"end":644,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":38,"end":290}],"gene3D":[{"start":125,"end":313,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"},{"start":22,"end":124,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"}]},"uniref50":"UniRef50_P11309","sequence":"MLLSKINSLAHLRAAPCNDLHATKLAPGKEKEPLESQYQVGPLLGSGGFGSVYSGIRVSDNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVLEAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVFFRQRVSSECQHLIRWCLALRPSDRPTFEEIQNHPWMQDVLLPQETAEIHLHSLSPGPSK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P11309","disprot_id":"DP00322","ncbi_taxon_id":9606,"regions_counter":1,"creator":"ameszaros","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":31,"region_id":"DP00322r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis of constitutive activity and a unique nucleotide binding mode of human Pim-1 kinase. <i> Qian KC, Wang L, Hickey ER, Studts J, Barringer K, Peng C, Kronkaitis A, Li J, White A, Mische S, Farmer B. </i> J Biol Chem, 2005","statement":[{"text":"Most residues in the Pim-1 structures are well resolved, except for the N-terminal residues 14–31 and the C-terminal residues 309–313.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":14,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15525646","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1XQZ"}],"term_name":"disorder","uniprot_changed":true,"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-14T21:16:16.087Z"}}],"released":"2016_10","uniref100":"UniRef100_P11309","date":"2016-09-08T12:58:37.000Z","acc":"P11309","name":"Serine/threonine-protein kinase pim-1","length":313,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"uniparc":"UPI000014987C","genes":[{"name":{"value":"PIM1"}}],"alphafold_very_low_content":0.11182108626198083,"disorder_content":0.05750798722044728,"disprot_consensus":{"full":[{"start":14,"end":31,"type":"D"}],"Structural state":[{"start":14,"end":31,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00104","name":"Ligand-binding domain of nuclear hormone receptor","start":243,"end":411},{"id":"PF00105","name":"Double treble clef zinc finger, C4 type","start":40,"end":109}],"gene3D":[{"start":31,"end":138,"id":"3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A"},{"start":142,"end":434,"id":"1.10.565.10","name":"Retinoid X Receptor"}]},"uniref50":"UniRef50_O75469","sequence":"MEVRPKESWNHADFVHCEDTESVPGKPSVNADEEVGGPQICRVCGDKATGYHFNVMTCEGCKGFFRRAMKRNARLRCPFRKGACEITRKTRRQCQACRLRKCLESGMKKEMIMSDEAVEERRALIKRKKSERTGTQPLGVQGLTEEQRMMIRELMDAQMKTFDTTFSHFKNFRLPGVLSSGCELPESLQAPSREEAAKWSQVRKDLCSLKVSLQLRGEDGSVWNYKPPADSGGKEIFSLLPHMADMSTYMFKGIISFAKVISYFRDLPIEDQISLLKGAAFELCQLRFNTVFNAETGTWECGRLSYCLEDTAGGFQQLLLEPMLKFHYMLKKLQLHEEEYVLMQAISLFSPDRPGVLQHRVVDQLQEQFAITLKSYIECNRPQPAHRFLFLKIMAMLTELRSINAQHTQRLLRIQDIHPFATPLMQELFGITGS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O75469","disprot_id":"DP00323","ncbi_taxon_id":9606,"regions_counter":2,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":141,"region_id":"DP00323r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The human nuclear xenobiotic receptor PXR: structural determinants of directed promiscuity. <i> Watkins RE, Wisely GB, Moore LB, Collins JL, Lambert MH, Williams SP, Willson TM, Kliewer SA, Redinbo MR. </i> Science, 2001","term_id":"IDPO:0000002","curator_id":"mnecci","start":130,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"11408620","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1ILG"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":197,"region_id":"DP00323r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The human nuclear xenobiotic receptor PXR: structural determinants of directed promiscuity. <i> Watkins RE, Wisely GB, Moore LB, Collins JL, Lambert MH, Williams SP, Willson TM, Kliewer SA, Redinbo MR. </i> Science, 2001","term_id":"IDPO:0000002","curator_id":"mnecci","start":178,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"11408620","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1ILG"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_O75469","date":"2016-09-06T11:01:57.000Z","acc":"O75469","name":"Nuclear receptor subfamily 1 group I member 2","length":434,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000001272","genes":[{"name":{"value":"NR1I2"},"synonyms":[{"value":"PXR"}]}],"alphafold_very_low_content":0.12442396313364056,"disorder_content":0.07373271889400922,"disprot_consensus":{"full":[{"start":130,"end":141,"type":"D"},{"start":178,"end":197,"type":"D"}],"Structural state":[{"start":130,"end":141,"type":"D"},{"start":178,"end":197,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":16,"end":82},{"id":"PF00076","name":"RNA recognition motif","start":107,"end":166},{"id":"PF11627","name":"Heterogeneous nuclear ribonucleoprotein A1, LC domain","start":307,"end":344}],"gene3D":[{"start":99,"end":180,"id":"3.30.70.330","name":"3.30.70.330"},{"start":1,"end":91,"id":"3.30.70.330","name":"3.30.70.330"}]},"uniref50":"UniRef50_P09651","sequence":"MSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGGYGGGGPGYSGGSRGYGSGGQGYGNQGSGYGGSGSYDSYNNGGGGGFGGGSGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKPRNQGGYGGSSSSSSYGSGRRF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P09651","disprot_id":"DP00324","ncbi_taxon_id":9606,"regions_counter":26,"creator":"bjuhasz","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":102,"region_id":"DP00324r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Correlated alternative side chain conformations in the RNA-recognition motif of heterogeneous nuclear ribonucleoprotein A1. <i> Vitali J, Ding J, Jiang J, Zhang Y, Krainer AR, Xu RM. </i> Nucleic Acids Res, 2002","term_id":"IDPO:0000002","curator_id":"esalladini","start":92,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"11917013","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1L3K"}],"term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"Three regions were not modeled because of poor electron density: the first seven residues at the N-terminus, the last 16 residues at the C-terminus and the internal linker residues Arg92–Leu102. These regions were disordered in the original 1.75 and 1.9 Å structures (35,36) and they remained uninterpretable even in the present high resolution analysis.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T19:05:40.864Z"}},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":102,"term_name":"flexible linker","start":92,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"11917013","version":4,"reference_html":"Correlated alternative side chain conformations in the RNA-recognition motif of heterogeneous nuclear ribonucleoprotein A1. <i> Vitali J, Ding J, Jiang J, Zhang Y, Krainer AR, Xu RM. </i> Nucleic Acids Res, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006220","region_id":"DP00324r003","cross_refs":[{"db":"PDB","id":"1L3K"}],"curator_orcid":"0000-0002-5152-5953","statement":[{"text":"Three regions were not modeled because of poor electron density: the first seven residues at the N-terminus, the last 16 residues at the C-terminus and the internal linker residues Arg92–Leu102. These regions were disordered in the original 1.75 and 1.9 Å structures (35,36) and they remained uninterpretable even in the present high resolution analysis.","type":"Results"},{"text":"The disordered region is positioned between two RRM domains.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T19:10:09.612Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":196,"region_id":"DP00324r006","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Correlated alternative side chain conformations in the RNA-recognition motif of heterogeneous nuclear ribonucleoprotein A1. <i> Vitali J, Ding J, Jiang J, Zhang Y, Krainer AR, Xu RM. </i> Nucleic Acids Res, 2002","term_id":"IDPO:0000002","curator_id":"esalladini","start":182,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"11917013","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1L3K"}],"term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"Three regions were not modeled because of poor electron density: the first seven residues at the N-terminus, the last 16 residues at the C-terminus and the internal linker residues Arg92–Leu102. These regions were disordered in the original 1.75 and 1.9 Å structures (35,36) and they remained uninterpretable even in the present high resolution analysis.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T19:05:41.075Z"}},{"start":92,"end":102,"reference_id":"10323862","reference_source":"pmid","reference_html":"Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA. <i> Ding J, Hayashi MK, Zhang Y, Manche L, Krainer AR, Xu RM. </i> Genes Dev, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2UP1"}],"region_id":"DP00324r010","statement":[{"text":"Second, the linker connecting the two RRMs becomes ordered on TR2 binding (Fig. 2A).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T19:09:16.637Z"}},{"start":92,"end":102,"reference_id":"10323862","reference_source":"pmid","reference_html":"Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA. <i> Ding J, Hayashi MK, Zhang Y, Manche L, Krainer AR, Xu RM. </i> Genes Dev, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"2UP1"}],"region_id":"DP00324r011","statement":[{"text":"Both regions make important contacts with DNA (see below).","type":"Results"},{"text":"The inter-RRM linker segment is defined to include amino acids 90–105. Three residues in this segment make direct contacts with DNA bases. Arg-92 makes contacts with three bases, Gua-4, Gua-5, and Thy-7, and the guanidino moiety is locked between the three bases (Fig.4 and 5A). Ser-95 makes a hydrogen bond with the N2 atom of Gua-4. The imidazole ring of His-101 stacks with the purine ring of Ade-3, which is sandwiched between His-101 and Phe-17.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T19:09:57.283Z"}},{"start":92,"end":102,"reference_id":"10323862","reference_source":"pmid","reference_html":"Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA. <i> Ding J, Hayashi MK, Zhang Y, Manche L, Krainer AR, Xu RM. </i> Genes Dev, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"2UP1"}],"region_id":"DP00324r013","statement":[{"text":"The inter-RRM linker segment is defined to include amino acids 90–105.","type":"Results"},{"text":"Second, the linker connecting the two RRMs becomes ordered on TR2 binding (Fig. 2A).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T19:09:43.616Z"}},{"start":183,"end":190,"reference_id":"10323862","reference_source":"pmid","reference_html":"Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA. <i> Ding J, Hayashi MK, Zhang Y, Manche L, Krainer AR, Xu RM. </i> Genes Dev, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"2UP1"}],"region_id":"DP00324r014","statement":[{"text":"Third, the region near the carboxyl terminus of UP1 (Lys-183–Ser-190), which was disordered in the absence of DNA, also becomes ordered in the presence of DNA and forms an α-helix (Fig. 2A).","type":"Results"},{"text":"The segment including residues 183–190 was disordered in the protein-only structure, but becomes ordered and forms an α-helix when bound to DNA. The amide group of Lys-183 makes a hydrogen bond with Gua-11, and its side chain interacts with the DNA backbone via a water-mediated interaction. Met-186 makes a van der Waals contact with Ade-9, such that the adenine ring is sandwiched between Met-186 and Phe-108.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T19:11:21.379Z"}},{"start":342,"end":357,"reference_id":"16901787","reference_source":"pmid","reference_html":"Rules for nuclear localization sequence recognition by karyopherin beta 2. <i> Lee BJ, Cansizoglu AE, Süel KE, Louis TH, Zhang Z, Chook YM. </i> Cell, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2H4M"}],"region_id":"DP00324r019","statement":[{"text":"The region is missing in the crystal structure but it was not mentioned in the article.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T18:51:29.665Z"}},{"start":182,"end":186,"reference_id":"28084329","reference_source":"pmid","reference_html":"SPSB1-mediated HnRNP A1 ubiquitylation regulates alternative splicing and cell migration in EGF signaling. <i> Wang F, Fu X, Chen P, Wu P, Fan X, Li N, Zhu H, Jia TT, Ji H, Wang Z, Wong CC, Hu R, Hui J. </i> Cell Res, 2017","date":"2023-12-15T19:25:21.612Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000046","term_name":"ubiquitination display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007718","ec_ontology":"ECO","ec_name":"ubiquitination assay evidence used in manual assertion","released":"2023_12","version":3,"region_id":"DP00324r024","statement":[{"text":"Only mutation of Lys183 among the three lysines (Lys166, Lys179 and Lys183) between amino acid residues 161 and 185 resulted in a decreased level of hnRNP A1 ubiquitylation (Supplementary information, Figure S3D).","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Disorder function"},{"start":93,"end":97,"reference_id":"25999341","reference_source":"pmid","reference_html":"DNA-PKcs phosphorylates hnRNP-A1 to facilitate the RPA-to-POT1 switch and telomere capping after replication. <i> Sui J, Lin YF, Xu K, Lee KJ, Wang D, Chen BP. </i> Nucleic Acids Res, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00324r026","statement":[{"text":"IP-western blot revealed that hnRNP-A1 phosphorylation at SQ/TQ motifs was reduced in S95A and S192A single mutant hnRNP-A1 and was eliminated in S95A/S192A double mutant hnRNP-A1 as compared to wild-type hnRNP-A1 (Figure 1C). These results confirm that Ser95 and Ser192 are main phosphorylation residues of hnRNP-A1 and that hnRNP-A1 is phosphorylated by DNA-PKcs in vivo (13,21).","type":"Results"}],"ec_go":"IEP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T19:25:31.854Z"}}],"released":"2016_10","uniref100":"UniRef100_P09651","date":"2016-08-18T16:27:10.000Z","acc":"P09651","name":"Heterogeneous nuclear ribonucleoprotein A1","length":372,"organism":"Homo sapiens","dataset":["Condensates-related proteins","RNA-binding proteins"],"UniParc":"UPI000016B2CF","genes":[{"name":{"value":"HNRNPA1"},"synonyms":[{"value":"HNRPA1"}]}],"alphafold_very_low_content":0.4650537634408602,"disorder_content":0.11290322580645161,"disprot_consensus":{"full":[{"start":92,"end":102,"type":"T"},{"start":182,"end":196,"type":"D"},{"start":342,"end":357,"type":"D"}],"Structural state":[{"start":92,"end":102,"type":"D"},{"start":182,"end":196,"type":"D"},{"start":342,"end":357,"type":"D"}],"Disorder function":[{"start":92,"end":102,"type":"F"},{"start":182,"end":186,"type":"F"}],"Structural transition":[{"start":92,"end":102,"type":"T"}],"Molecular function":[{"start":92,"end":102,"type":"F"},{"start":183,"end":190,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05395","name":"Protein phosphatase inhibitor 1/DARPP-32","start":5,"end":155}]},"uniref50":"UniRef50_Q13522","sequence":"MEQDNSPRKIQFTVPLLEPHLDPEAAEQIRRRRPTPATLVLTSDQSSPEVDEDRIPNPLLKPSLAMSPRQRKKMTRTTPTMKELQMMVEHHLGQQEQGEEPEGAAEGTGAQESQPPGTPGTGAESRLGPSATAQKPAQPSPRAQERRGEEPSTAKTSQDSQGASAV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Lagomorpha","Leporidae","Oryctolagus"],"uniref90":"UniRef90_P01099","disprot_id":"DP00325","ncbi_taxon_id":9986,"regions_counter":4,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":166,"region_id":"DP00325r001","released":"2022_03","ec_id":"ECO:0007680","reference_html":"The regulation of glycogen metabolism. Purification and characterisation of protein phosphatase inhibitor-1 from rabbit skeletal muscle. <i> Nimmo GA, Cohen P. </i> Eur J Biochem, 1978","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"208844","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":166,"term_name":"molecular function inhibitor activity","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"208844","version":3,"reference_html":"The regulation of glycogen metabolism. Purification and characterisation of protein phosphatase inhibitor-1 from rabbit skeletal muscle. <i> Nimmo GA, Cohen P. </i> Eur J Biochem, 1978","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140678","ec_id":"ECO:0007680","region_id":"DP00325r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":166,"region_id":"DP00325r003","released":"2022_03","ec_id":"ECO:0006317","reference_html":"The regulation of glycogen metabolism. Purification and characterisation of protein phosphatase inhibitor-1 from rabbit skeletal muscle. <i> Nimmo GA, Cohen P. </i> Eur J Biochem, 1978","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"208844","version":2,"ec_name":"temperature-induced protein unfolding evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":166,"term_name":"molecular function inhibitor activity","start":1,"ec_name":"temperature-induced protein unfolding evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"208844","version":3,"reference_html":"The regulation of glycogen metabolism. Purification and characterisation of protein phosphatase inhibitor-1 from rabbit skeletal muscle. <i> Nimmo GA, Cohen P. </i> Eur J Biochem, 1978","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140678","ec_id":"ECO:0006317","region_id":"DP00325r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P01099","date":"2016-08-30T13:48:21.000Z","acc":"P01099","name":"Protein phosphatase 1 regulatory subunit 1A","length":166,"organism":"Oryctolagus cuniculus","dataset":[],"UniParc":"UPI000012D803","genes":[{"name":{"value":"PPP1R1A"},"synonyms":[{"value":"IPP1"}]}],"alphafold_very_low_content":0.18674698795180722,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":166,"type":"D"}],"Structural state":[{"start":1,"end":166,"type":"D"}],"Molecular function":[{"start":1,"end":166,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05721","name":"Phytanoyl-CoA dioxygenase (PhyH)","start":61,"end":277}],"gene3D":[{"start":31,"end":338,"id":"2.60.120.620","name":"q2cbj1_9rhob like domain"}]},"uniref50":"UniRef50_O14832","sequence":"MEQLRAAARLQIVLGHLGRPSAGAVVAHPTSGTISSASFHPQQFQYTLDNNVLTLEQRKFYEENGFLVIKNLVPDADIQRFRNEFEKICRKEVKPLGLTVMRDVTISKSEYAPSEKMITKVQDFQEDKELFRYCTLPEILKYVECFTGPNIMAMHTMLINKPPDSGKKTSRHPLHQDLHYFPFRPSDLIVCAWTAMEHISRNNGCLVVLPGTHKGSLKPHDYPKWEGGVNKMFHGIQDYEENKARVHLVMEKGDTVFFHPLLIHGSGQNKTQGFRKAISCHFASADCHYIDVKGTSQENIEKEVVGIAHKFFGAENSVNLKDIWMFRARLVKGERTNL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O14832","disprot_id":"DP00327","ncbi_taxon_id":9606,"regions_counter":4,"creator":"nveljkovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":42,"region_id":"DP00327r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of human phytanoyl-CoA 2-hydroxylase identifies molecular mechanisms of Refsum disease. <i> McDonough MA, Kavanagh KL, Butler D, Searls T, Oppermann U, Schofield CJ. </i> J Biol Chem, 2005","term_id":"IDPO:0000002","curator_id":"nveljkovic","start":31,"term_ontology":"IDPO","curator_name":"Nevena Veljkovic","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-6562-5800","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2A1X"}],"reference_id":"16186124","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":233,"region_id":"DP00327r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of human phytanoyl-CoA 2-hydroxylase identifies molecular mechanisms of Refsum disease. <i> McDonough MA, Kavanagh KL, Butler D, Searls T, Oppermann U, Schofield CJ. </i> J Biol Chem, 2005","term_id":"IDPO:0000002","curator_id":"nveljkovic","start":223,"term_ontology":"IDPO","curator_name":"Nevena Veljkovic","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-6562-5800","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2A1X"}],"reference_id":"16186124","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":318,"region_id":"DP00327r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of human phytanoyl-CoA 2-hydroxylase identifies molecular mechanisms of Refsum disease. <i> McDonough MA, Kavanagh KL, Butler D, Searls T, Oppermann U, Schofield CJ. </i> J Biol Chem, 2005","term_id":"IDPO:0000002","curator_id":"nveljkovic","start":303,"term_ontology":"IDPO","curator_name":"Nevena Veljkovic","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-6562-5800","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2A1X"}],"reference_id":"16186124","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_O14832","date":"2016-09-08T10:27:00.000Z","acc":"O14832","name":"Phytanoyl-CoA dioxygenase, peroxisomal","length":338,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000131215","genes":[{"name":{"value":"PHYH"},"synonyms":[{"value":"PAHX"}]}],"alphafold_very_low_content":0.026627218934911243,"disorder_content":0.11538461538461539,"disprot_consensus":{"full":[{"start":31,"end":42,"type":"D"},{"start":223,"end":233,"type":"D"},{"start":303,"end":318,"type":"D"}],"Structural state":[{"start":31,"end":42,"type":"D"},{"start":223,"end":233,"type":"D"},{"start":303,"end":318,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00651","name":"BTB/POZ domain","start":26,"end":120},{"id":"PF09237","name":"GAGA factor","start":319,"end":372}],"gene3D":[{"start":319,"end":372,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":12,"end":188,"id":"3.30.710.10","name":"Potassium Channel Kv1.1; Chain A"}]},"uniref50":"UniRef50_Q08605","sequence":"MSLPMNSLYSLTWGDYGTSLVSAIQLLRCHGDLVDCTLAAGGRSFPAHKIVLCAASPFLLDLLKNTPCKHPVVMLAGVNANDLEALLEFVYRGEVSVDHAQLPSLLQAAQCLNIQGLAPQTVTKDDYTTHSIQLQHMIPQHHDQDQLIATIATAPQQTVHAQVVEDIHHQGQILQATTQTNAAGQQQTIVTTDAAKHDQAVIQAFLPARKRKPRVKKMSPTAPKISKVEGMDTIMGTPTSSHGSGSVQQVLGENGAEGQLLSSTPIIKSEGQKVETIVTMDPNNMIPVTSANAATGEITPAQGATGSSGGNTSGVLSTPKAKRAKHPPGTEKPRSRSQSEQPATCPICYAVIRQSRNLRRHLELRHFAKPGVKKEKKTTSGKKSSSGSSGSGSGALSSSGSVPQVQTVQSLHTLQGVQVKKDPDAQQQQQQQQQQQQQQQQQAMTVSGATGGQVQQQVQQVQQQVQQQQQQQQQQQQQLQHHQIIDSSGNITTATTSAQAAAAAQQQAAGQQQQLVAQSDGSESGAPLSIAQVQTLQGHQIIGNLNQVNITDFQQQQPQQQQQQQQQQQQQQQQQQQTQQTL","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_Q08605","disprot_id":"DP00328","ncbi_taxon_id":7227,"regions_counter":13,"creator":"maspromonte","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":335,"region_id":"DP00328r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The glutamine-rich domain of the Drosophila GAGA factor is necessary for amyloid fibre formation in vitro, but not for chromatin remodelling. <i> Agianian B, Leonard K, Bonte E, Van der Zandt H, Becker PB, Tucker PA. </i> J Mol Biol, 1999","term_id":"IDPO:0000002","curator_id":"maspromonte","start":310,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1YUI"}],"reference_id":"9878427","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":335,"term_name":"molecular function activator activity","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The glutamine-rich domain of the Drosophila GAGA factor is necessary for amyloid fibre formation in vitro, but not for chromatin remodelling. <i> Agianian B, Leonard K, Bonte E, Van der Zandt H, Becker PB, Tucker PA. </i> J Mol Biol, 1999","term_id":"GO:0140677","curator_id":"maspromonte","start":310,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"9878427","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00328r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":335,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The glutamine-rich domain of the Drosophila GAGA factor is necessary for amyloid fibre formation in vitro, but not for chromatin remodelling. <i> Agianian B, Leonard K, Bonte E, Van der Zandt H, Becker PB, Tucker PA. </i> J Mol Biol, 1999","term_id":"IDPO:0000011","curator_id":"maspromonte","start":310,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","reference_id":"9878427","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00328r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":335,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The glutamine-rich domain of the Drosophila GAGA factor is necessary for amyloid fibre formation in vitro, but not for chromatin remodelling. <i> Agianian B, Leonard K, Bonte E, Van der Zandt H, Becker PB, Tucker PA. </i> J Mol Biol, 1999","term_id":"GO:0003676","curator_id":"maspromonte","start":310,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"9878427","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00328r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":335,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The glutamine-rich domain of the Drosophila GAGA factor is necessary for amyloid fibre formation in vitro, but not for chromatin remodelling. <i> Agianian B, Leonard K, Bonte E, Van der Zandt H, Becker PB, Tucker PA. </i> J Mol Biol, 1999","term_id":"GO:0005515","curator_id":"maspromonte","start":310,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"9878427","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00328r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":348,"region_id":"DP00328r006","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The glutamine-rich domain of the Drosophila GAGA factor is necessary for amyloid fibre formation in vitro, but not for chromatin remodelling. <i> Agianian B, Leonard K, Bonte E, Van der Zandt H, Becker PB, Tucker PA. </i> J Mol Biol, 1999","term_id":"IDPO:0000002","curator_id":"maspromonte","start":281,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1YUI"}],"reference_id":"9878427","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":348,"term_name":"molecular function activator activity","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The glutamine-rich domain of the Drosophila GAGA factor is necessary for amyloid fibre formation in vitro, but not for chromatin remodelling. <i> Agianian B, Leonard K, Bonte E, Van der Zandt H, Becker PB, Tucker PA. </i> J Mol Biol, 1999","term_id":"GO:0140677","curator_id":"maspromonte","start":281,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"9878427","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00328r007","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":348,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The glutamine-rich domain of the Drosophila GAGA factor is necessary for amyloid fibre formation in vitro, but not for chromatin remodelling. <i> Agianian B, Leonard K, Bonte E, Van der Zandt H, Becker PB, Tucker PA. </i> J Mol Biol, 1999","term_id":"GO:0003676","curator_id":"maspromonte","start":281,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"9878427","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00328r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":348,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The glutamine-rich domain of the Drosophila GAGA factor is necessary for amyloid fibre formation in vitro, but not for chromatin remodelling. <i> Agianian B, Leonard K, Bonte E, Van der Zandt H, Becker PB, Tucker PA. </i> J Mol Biol, 1999","term_id":"GO:0005515","curator_id":"maspromonte","start":281,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"9878427","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00328r009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":444,"region_id":"DP00328r010","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The glutamine-rich domain of the Drosophila GAGA factor is necessary for amyloid fibre formation in vitro, but not for chromatin remodelling. <i> Agianian B, Leonard K, Bonte E, Van der Zandt H, Becker PB, Tucker PA. </i> J Mol Biol, 1999","term_id":"IDPO:0000002","curator_id":"maspromonte","start":368,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1YUI"}],"reference_id":"9878427","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":444,"term_name":"molecular function activator activity","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The glutamine-rich domain of the Drosophila GAGA factor is necessary for amyloid fibre formation in vitro, but not for chromatin remodelling. <i> Agianian B, Leonard K, Bonte E, Van der Zandt H, Becker PB, Tucker PA. </i> J Mol Biol, 1999","term_id":"GO:0140677","curator_id":"maspromonte","start":368,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"9878427","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00328r011","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":444,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The glutamine-rich domain of the Drosophila GAGA factor is necessary for amyloid fibre formation in vitro, but not for chromatin remodelling. <i> Agianian B, Leonard K, Bonte E, Van der Zandt H, Becker PB, Tucker PA. </i> J Mol Biol, 1999","term_id":"GO:0003676","curator_id":"maspromonte","start":368,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"9878427","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00328r012","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":444,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The glutamine-rich domain of the Drosophila GAGA factor is necessary for amyloid fibre formation in vitro, but not for chromatin remodelling. <i> Agianian B, Leonard K, Bonte E, Van der Zandt H, Becker PB, Tucker PA. </i> J Mol Biol, 1999","term_id":"GO:0005515","curator_id":"maspromonte","start":368,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"9878427","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00328r013","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q08605","date":"2016-08-30T16:20:16.000Z","acc":"Q08605","name":"Transcription factor GAGA","length":582,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI000012AFE2","genes":[{"name":{"value":"Trl"},"synonyms":[{"value":"Adf-2"},{"value":"GAGA"},{"value":"Nc70F"},{"value":"TFGAGA"}],"orfNames":[{"value":"CG33261"}]}],"alphafold_very_low_content":0.5938037865748709,"disorder_content":0.24914089347079038,"disprot_consensus":{"full":[{"start":281,"end":309,"type":"D"},{"start":310,"end":335,"type":"T"},{"start":336,"end":348,"type":"D"},{"start":368,"end":444,"type":"D"}],"Structural state":[{"start":281,"end":348,"type":"D"},{"start":368,"end":444,"type":"D"}],"Molecular function":[{"start":281,"end":348,"type":"F"},{"start":368,"end":444,"type":"F"}],"Structural transition":[{"start":310,"end":335,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00363","name":"Casein","start":138,"end":217}]},"uniref50":"UniRef50_P02666","sequence":"MKVLILACLVALALARELEELNVPGEIVESLSSSEESITRINKKIEKFQSEEQQQTEDELQDKIHPFAQTQSLVYPFPGPIPNSLPQNIPPLTQTPVVVPPFLQPEVMGVSKVKEAMAPKHKEMPFPKYPVEPFTESQSLTLTDVENLHLPLPLLQSWMHQPHQPLPPTVMFPPQSVLSLSQSKVLPVPQKAVPYPQRDMPIQAFLLYQEPVLGPVRGPFPIIV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P02666","disprot_id":"DP00329","ncbi_taxon_id":9913,"regions_counter":10,"creator":"nveljkovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":25,"region_id":"DP00329r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Two-dimensional nuclear magnetic resonance study of the beta-casein peptide 1-25: resonance assignments and secondary structure. <i> Wahlgren NM, Léonil J, Dejmek P, Drakenberg T. </i> Biochim Biophys Acta, 1993","term_id":"IDPO:0000002","curator_id":"nveljkovic","start":1,"term_ontology":"IDPO","curator_name":"Nevena Veljkovic","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6562-5800","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"8373815","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":224,"region_id":"DP00329r002","released":"2022_03","ec_id":"ECO:0006206","reference_html":"Secondary structure of bovine alpha s1- and beta-casein in solution. <i> Creamer LK, Richardson T, Parry DA. </i> Arch Biochem Biophys, 1981","term_id":"IDPO:0000002","curator_id":"nveljkovic","start":1,"term_ontology":"IDPO","curator_name":"Nevena Veljkovic","ec_name":"near-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6562-5800","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"7305393","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":224,"term_name":"metal ion binding","released":"2022_12","ec_name":"near-UV circular dichroism evidence used in manual assertion","reference_html":"Secondary structure of bovine alpha s1- and beta-casein in solution. <i> Creamer LK, Richardson T, Parry DA. </i> Arch Biochem Biophys, 1981","term_id":"GO:0046872","curator_id":"fquaglia","start":1,"term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"7305393","version":4,"curator_orcid":"0000-0002-0341-4888","date":"2022-12-06T11:10:47.403Z","reference_source":"pmid","ec_id":"ECO:0006206","region_id":"DP00329r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":false},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":224,"term_name":"ion binding","released":"2022_03","ec_name":"near-UV circular dichroism evidence used in manual assertion","reference_html":"Secondary structure of bovine alpha s1- and beta-casein in solution. <i> Creamer LK, Richardson T, Parry DA. </i> Arch Biochem Biophys, 1981","term_id":"GO:0043167","curator_id":"nveljkovic","start":1,"term_ontology":"GO","curator_name":"Nevena Veljkovic","reference_id":"7305393","version":3,"curator_orcid":"0000-0001-6562-5800","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006206","region_id":"DP00329r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":224,"region_id":"DP00329r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Secondary structure of bovine alpha s1- and beta-casein in solution. <i> Creamer LK, Richardson T, Parry DA. </i> Arch Biochem Biophys, 1981","term_id":"IDPO:0000002","curator_id":"nveljkovic","start":1,"term_ontology":"IDPO","curator_name":"Nevena Veljkovic","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6562-5800","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"7305393","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":224,"term_name":"metal ion binding","released":"2022_12","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Secondary structure of bovine alpha s1- and beta-casein in solution. <i> Creamer LK, Richardson T, Parry DA. </i> Arch Biochem Biophys, 1981","term_id":"GO:0046872","curator_id":"fquaglia","start":1,"term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"7305393","version":4,"curator_orcid":"0000-0002-0341-4888","date":"2022-12-06T11:10:32.604Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00329r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":false},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":224,"term_name":"ion binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Secondary structure of bovine alpha s1- and beta-casein in solution. <i> Creamer LK, Richardson T, Parry DA. </i> Arch Biochem Biophys, 1981","term_id":"GO:0043167","curator_id":"nveljkovic","start":1,"term_ontology":"GO","curator_name":"Nevena Veljkovic","reference_id":"7305393","version":3,"curator_orcid":"0000-0001-6562-5800","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00329r007","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":224,"region_id":"DP00329r008","released":"2022_03","ec_id":"ECO:0006214","reference_html":"Dynamics and rigidity in an intrinsically disordered protein, β-casein. <i> Perticaroli S, Nickels JD, Ehlers G, Mamontov E, Sokolov AP. </i> J Phys Chem B, 2014","statement":[{"text":"at all temperatures and\nhydration conditions, the quasielastic intensity of CAS is higher\nthan that in GFP, suggesting that the IDP shows higher\nflexibility and enhanced picosecond dynamics relative to the\nrigid β-barrel","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":1,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"small-angle neutron scattering evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24918971","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":224,"term_name":"disorder to molten globule","released":"2022_03","ec_name":"small-angle neutron scattering evidence used in manual assertion","reference_html":"Dynamics and rigidity in an intrinsically disordered protein, β-casein. <i> Perticaroli S, Nickels JD, Ehlers G, Mamontov E, Sokolov AP. </i> J Phys Chem B, 2014","statement":[{"text":"We show that CAS partially folds and stiffens upon calcium binding, but in the unfolded state, it is softer than folded proteins such as green fluorescence protein (GFP).","type":"Abstract"}],"term_id":"IDPO:0000018","curator_id":"ndavey","start":1,"term_ontology":"IDPO","curator_name":"Norman Davey","reference_id":"24918971","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006214","region_id":"DP00329r009","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":224,"term_name":"calcium ion binding","released":"2022_03","ec_name":"small-angle neutron scattering evidence used in manual assertion","reference_html":"Dynamics and rigidity in an intrinsically disordered protein, β-casein. <i> Perticaroli S, Nickels JD, Ehlers G, Mamontov E, Sokolov AP. </i> J Phys Chem B, 2014","statement":[{"text":"An IDP, β-casein\n(CAS), has been studied in a calcium bound and unbound\nstate using neutron and light scattering techniques.","type":"Abstract"}],"term_id":"GO:0005509","curator_id":"ndavey","start":1,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"24918971","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006214","region_id":"DP00329r010","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P02666","date":"2016-09-09T13:50:00.000Z","acc":"P02666","name":"Beta-casein","length":224,"organism":"Bos taurus","dataset":[],"UniParc":"UPI000016C2CF","genes":[{"name":{"value":"CSN2"}}],"alphafold_very_low_content":0.24553571428571427,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":224,"type":"T"}],"Structural state":[{"start":1,"end":224,"type":"D"}],"Molecular function":[{"start":1,"end":224,"type":"F"}],"Structural transition":[{"start":1,"end":224,"type":"T"}]}},{"features":{"pfam":[{"id":"PF05432","name":"Bone sialoprotein II (BSP-II)","start":17,"end":314}]},"uniref50":"UniRef50_P21815","sequence":"MKTALILLSILGMACAFSMKNLHRRVKIEDSEENGVFKYRPRYYLYKHAYFYPHLKRFPVQGSSDSSEENGDDSSEEEEEEEETSNEGENNEESNEDEDSEAENTTLSATTLGYGEDATPGTGYTGLAAIQLPKKAGDITNKATKEKESDEEEEEEEEGNENEESEAEVDENEQGINGTSTNSTEAENGNGSSGGDNGEEGEEESVTGANAEDTTETGRQGKGTSKTTTSPNGGFEPTTPPQVYRTTSPPFGKTTTVEYEGEYEYTGANEYDNGYEIYESENGEPRGDNYRAYEDEYSYFKGQGYDGYDGQNYYHHQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P21815","disprot_id":"DP00332","ncbi_taxon_id":9606,"regions_counter":13,"creator":"maspromonte","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":317,"region_id":"DP00332r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin. <i> Fisher LW, Torchia DA, Fohr B, Young MF, Fedarko NS. </i> Biochem Biophys Res Commun, 2001","term_id":"IDPO:0000002","curator_id":"rpancsa","start":1,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"11162539","statement":[{"text":"The purified proteins were concentrated to 15 mg/ml and subjected to standard one dimensional proton NMR.","type":"Results"},{"text":"The narrow spread of the peptide backbone amide NH peaks (7.8–8.6 ppm) and the side chain NH peaks (6.6–7.4 ppm) are indicative of a lack of ordered structures over the NMR time scale.","type":"Results"},{"text":"Therefore, both BSP and OPN, when purified and isolated in solution, are flexible along their entire length and have no significant regions that persist in a single structural environment for more than a few milliseconds.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T19:39:56.930Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":317,"reference_id":"11162539","reference_source":"pmid","reference_html":"Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin. <i> Fisher LW, Torchia DA, Fohr B, Young MF, Fedarko NS. </i> Biochem Biophys Res Commun, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0036094","term_name":"small molecule binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","released":"2022_03","version":3,"region_id":"DP00332r004","statement":[{"text":"For example, we have shown previously that BSP can bind strongly to hydroxyapatite (HA) and does so throughout most of its entire length. For BSP to function as an attachment protein for cells to attach to HA (as has been frequently proposed by people in the bone field), the BSP would be bound to HA along its length and yet keep its RGD domain available to bind an integrin such as aVb3.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T19:40:02.715Z"},"term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":317,"reference_id":"11162539","reference_source":"pmid","reference_html":"Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin. <i> Fisher LW, Torchia DA, Fohr B, Young MF, Fedarko NS. </i> Biochem Biophys Res Commun, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","released":"2022_03","version":3,"region_id":"DP00332r005","statement":[{"text":"BSP can also bind first to the alpha-V/beta-3 integrin then it can bind to complement\nFactor H (Fig. 3A). This four-subunit complex stops the lytic pathway of complement in vitro (10). If, however, Factor H binds to BSP before the latter can bind to its integrin, the Factor H binds throughout the length of BSP blocking its ability to subsequently bind to the integrin. The integrin-binding domain of BSP can therefore bind to either the integrin or to specific portions of Factor H.","type":"Results"}],"interaction_partner":[{"db":"UniProt","id":"P08603","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T16:02:55.321Z"},"term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":285,"end":289,"reference_id":"11162539","reference_source":"pmid","reference_html":"Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin. <i> Fisher LW, Torchia DA, Fohr B, Young MF, Fedarko NS. </i> Biochem Biophys Res Commun, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","released":"2022_03","version":3,"region_id":"DP00332r006","statement":[{"text":"RGD domain available to bind an integrin such as alpha-V/beta-3","type":"Results"}],"interaction_partner":[{"db":"UniProt","id":"P06756","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P05106","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T16:03:00.034Z"},"term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":285,"end":289,"reference_id":"10747989","reference_source":"pmid","reference_html":"Factor H binding to bone sialoprotein and osteopontin enables tumor cell evasion of complement-mediated attack. <i> Fedarko NS, Fohr B, Robey PG, Young MF, Fisher LW. </i> J Biol Chem, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006309","ec_ontology":"ECO","ec_name":"competitive binding evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P06756","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P05106","partner_start":null,"partner_end":null}],"region_id":"DP00332r007","statement":[{"text":" Furthermore, preincubation of MEL cells with either GRGDS peptide or an aVb3 antibody (which blocks that integrins binding activity) negated the protective effect of rBSP.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T16:03:04.065Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":285,"end":289,"reference_id":"10747989","reference_source":"pmid","reference_html":"Factor H binding to bone sialoprotein and osteopontin enables tumor cell evasion of complement-mediated attack. <i> Fedarko NS, Fohr B, Robey PG, Young MF, Fisher LW. </i> J Biol Chem, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P06756","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P05106","partner_start":null,"partner_end":null}],"region_id":"DP00332r008","statement":[{"text":"Preincubation  of  MEL  cells  with  rBSP whose  RGD  sequence  had  been  mutated  to  KAE  completely removed the protective affects of this protein.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T16:03:04.975Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":317,"reference_id":"10747989","reference_source":"pmid","reference_html":"Factor H binding to bone sialoprotein and osteopontin enables tumor cell evasion of complement-mediated attack. <i> Fedarko NS, Fohr B, Robey PG, Young MF, Fisher LW. </i> J Biol Chem, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P08603","partner_start":null,"partner_end":null}],"region_id":"DP00332r009","statement":[{"text":"By steady state fluorescence, the binding of BSP  and  OPN  by  Factor  H  are  saturable  and  possess  a  1:1 stoichiometry, have binding constants in the nanomolar range, given the serum concentration of Factor H (0.5 mg/ml), virtually all BSP and OPN in serum will be complexed with Factor H.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T16:03:06.296Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":317,"reference_id":"9258751","reference_source":"pmid","reference_html":"Characterization of native and recombinant bone sialoprotein: delineation of the mineral-binding and cell adhesion domains and structural analysis of the RGD domain. <i> Stubbs JT, Mintz KP, Eanes ED, Torchia DA, Fisher LW. </i> J Bone Miner Res, 1997","date":"2022-03-08T15:26:19.315Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0036094","term_name":"small molecule binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000353","ec_ontology":"ECO","ec_name":"physical interaction evidence used in manual assertion","released":"2022_03","version":4,"region_id":"DP00332r010","statement":[{"text":"BSP has long been known to have an affinity for hydroxyapatite. A UMR-BSP hydroxyapaptite dissociation constant of 2.6 3 1029 M was calculated utilizing a molecular weight of 67.9 kD and a modification of the Scatchard method.","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"ChEBI","id":"52254","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-26T19:45:48.701Z"}},{"start":258,"end":317,"reference_id":"9258751","reference_source":"pmid","reference_html":"Characterization of native and recombinant bone sialoprotein: delineation of the mineral-binding and cell adhesion domains and structural analysis of the RGD domain. <i> Stubbs JT, Mintz KP, Eanes ED, Torchia DA, Fisher LW. </i> J Bone Miner Res, 1997","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00332r011","statement":[{"text":"A 59 amino acid recombinant RGD domain was produced in minimal media using 15NH4Cl as the sole source of nutrient nitrogen. The HSQC two-dimensional\nNMR spectrum showed a narrow spread of chemical shifts characteristic of a flexible structure or “random coil.”","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T16:01:07.727Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":258,"end":317,"reference_id":"9258751","reference_source":"pmid","reference_html":"Characterization of native and recombinant bone sialoprotein: delineation of the mineral-binding and cell adhesion domains and structural analysis of the RGD domain. <i> Stubbs JT, Mintz KP, Eanes ED, Torchia DA, Fisher LW. </i> J Bone Miner Res, 1997","date":"2022-03-08T15:27:13.580Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001143","ec_ontology":"ECO","ec_name":"adhesion assay evidence used in manual assertion","released":"2022_03","version":4,"region_id":"DP00332r012","statement":[{"text":"However, unlike the other recombinant BSP proteins, both the normal 258E–317Q\n(RGD) protein and the mutant 258E–317Q (KAE) protein mediated cell attachment were affected by the addition of GRGDS peptide.","type":"Results"},{"text":"It is clear from the authors' description that with this mutation they tested the integrin binding ability. While the whole protein retained cell attachment ability in the presence of the mutations (it also has another, integrin-independent attachment site), the cell attachment ability of the C-terminal segment was sensitive for the presence of competeing RGD-containing peptides.","type":"Curator statement"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-26T19:45:57.160Z"}},{"start":1,"end":317,"reference_id":"11162539","reference_source":"pmid","reference_html":"Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin. <i> Fisher LW, Torchia DA, Fohr B, Young MF, Fedarko NS. </i> Biochem Biophys Res Commun, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","released":"2022_03","version":3,"region_id":"DP00332r013","statement":[{"text":"Thus, BSP is a protein that can be bound along most of its length separately to at least two different binding partners in vivo. The simplest way to do this is to have a completely unstructured protein essentially alternating sequences that can specifically interact with the different binding partners.","type":"Results"},{"text":"BSP can also bind first to the avb3 integrin then it can bind to complement Factor H. This four-subunit complex stops the lytic pathway of complement in vitro.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T19:40:08.786Z"},"term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P21815","date":"2016-08-31T23:41:05.000Z","acc":"P21815","name":"Bone sialoprotein 2","length":317,"organism":"Homo sapiens","dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000167BD4","genes":[{"name":{"value":"IBSP"},"synonyms":[{"value":"BNSP"}]}],"alphafold_very_low_content":0.5583596214511041,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":317,"type":"D"}],"Structural state":[{"start":1,"end":317,"type":"D"}],"Molecular function":[{"start":1,"end":317,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00262","name":"Calreticulin family","start":23,"end":257},{"id":"PF00262","name":"Calreticulin family","start":259,"end":332}],"gene3D":[{"start":208,"end":278,"id":"2.10.250.10","name":"Calreticulin/calnexin, P domain"},{"start":20,"end":207,"id":"2.60.120.200","name":"2.60.120.200"},{"start":285,"end":368,"id":"2.60.120.200","name":"2.60.120.200"}]},"uniref50":"UniRef50_P27797","sequence":"MLLSVPLLLGLLGLAVAEPAVYFKEQFLDGDGWTSRWIESKHKSDFGKFVLSSGKFYGDEEKDKGLQTSQDARFYALSASFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPNSLDQTDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDPSIYAYDNFGVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P27797","disprot_id":"DP00333","ncbi_taxon_id":9606,"regions_counter":24,"creator":"vsagris","regions":[{"start":367,"end":417,"reference_id":"11101311","reference_source":"pmid","reference_html":"Probing the three-dimensional structure of human calreticulin. <i> Bouvier M, Stafford WF. </i> Biochemistry, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00333r006","statement":[{"text":"Results revealed a MW of 40 634 Da which based on the sequence of human CRT (and thepresence of four additional amino acid residues at the N-terminus, see Experimental Procedures) can be most closely correlated with the cleavage of 51 residues from the C-terminus of the protein. Collectively, these findings are entirely consistent with the presence of a region at the C-terminus of CRT in which the polypeptide backbone is most exposed and conformationally flexible in solution andtherefore more susceptible to proteolysis by thermolysin.","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-15T16:15:40.628Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":367,"end":417,"reference_id":"11101311","reference_source":"pmid","reference_html":"Probing the three-dimensional structure of human calreticulin. <i> Bouvier M, Stafford WF. </i> Biochemistry, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00333r007","statement":[{"text":"Results revealed a MW of 40 634 Da which based on the sequence of human CRT (and thepresence of four additional amino acid residues at the N-terminus, see Experimental Procedures) can be most closely correlated with the cleavage of 51 residues from the C-terminus of the protein. Collectively, these findings are entirely consistent with the presence of a region at the C-terminus of CRT in which the polypeptide backbone is most exposed and conformationally flexible in solution andtherefore more susceptible to proteolysis by thermolysin.","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-16T08:10:27.646Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":18,"end":417,"reference_id":"11101311","reference_source":"pmid","reference_html":"Probing the three-dimensional structure of human calreticulin. <i> Bouvier M, Stafford WF. </i> Biochemistry, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","released":"2022_03","version":4,"region_id":"DP00333r008","statement":[{"text":"These calculations yielded a value of f / f0) 1.65 using a partial specific volume of 0.695 cm3/g and hydration of 0.502 g of H2O/g of protein. Using these values, CRT could be  represented  as  a  prolate  of  ellipsoid  of  revolution  with an apparent axial ratio of 12.2, having a length of 29.8 nm and a diameter of 2.44 nm (Table 1). Based on this model, the  hydrodynamic  dimensions  clearly  indicate  that  monomeric CRT is an asymmetric elongated molecule in solution.","type":"Results"},{"text":"The distinctively  nonspherical  shape  of  CRT  is consistent  with  secondary  structure  predictions  suggesting that  certain  regions  of  the  protein  are  likely  to  adopt  an extended conformation in solution ( 17, 44 ).","type":"Results"},{"text":"Sedimentation equilibrium and velocity experiments clearly established  that  this  anomalous  behavior  arises  from  the highly elongated shape of monomeric CRT.","type":"Discussion"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-15T16:22:11.032Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":18,"end":307,"reference_id":"11101311","reference_source":"pmid","reference_html":"Probing the three-dimensional structure of human calreticulin. <i> Bouvier M, Stafford WF. </i> Biochemistry, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006317","ec_ontology":"ECO","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00333r009","statement":[{"text":"This analysis reveals that proteolytic fragments corresponding to bands 1 and 2 share a common core region  that  includes  most  of  the  N-domain  (residues  60 180) and a major portion of the P-domain (residues 180 \u0018 226), emphasizing that this region of the protein adopts a stable  and  rigid  three-dimensional  structure  in  solution.","type":"Results"},{"text":"N-domain of CRT is likely to fold into a globular structure within the protein   (17,   44),   thus conferring increased protection against proteolysis. The single site of thermolytic cleavage identified in the  N-domain  is  at  position  Leu  60(Table  2)  and is likely  to be  located  in  a  more  surface-exposed region, such as a loop or a turn, within the spatial arrangement of this domain.","type":"Results"},{"text":"The analysis presented in Figure 6 also indicates that band3 corresponds to the P-domain of CRT and encompasses the type 1 and type 2 sequence motifs (17, 44) which have been suggested to be important for the lectin function of CRT (7,18). The presence of this fragment in the proteolytic mixture provides  evidence  that  isolated  domains  of  CRT  can  be independently  stable  in  solution","type":"Results"},{"text":"Collectively, these studies provide experimental evidence that support  and  extend  the  early  structural  characterization  of CRT which predicted from secondary structure analysis that the general shape of the protein is a large globular N-terminus region  followed  by  a  more  elongated  C-terminal  region ( 17, 44 ).","type":"Discussion"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-16T15:29:34.212Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":308,"end":417,"reference_id":"11101311","reference_source":"pmid","reference_html":"Probing the three-dimensional structure of human calreticulin. <i> Bouvier M, Stafford WF. </i> Biochemistry, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006317","ec_ontology":"ECO","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00333r010","statement":[{"text":"Results (Table 2) indicate that two of the fragments (bands 1 and 2) are characterized by extensive loss of residues at the C-terminus of the protein but more limited cleavage at the  N-terminus","type":"Results"},{"text":"This observation suggests that the C-domain may be an important determinant in  initiating  the  thermal  denaturation  of  CRT  and  also  supports the view that this domain is likely to adopt a more loosely  packed  conformation  in  solution  ( 17,  44 ).  Collectively, these studies provide experimental evidence that support  and  extend  the  early  structural  characterization  of CRT which predicted from secondary structure analysis that the general shape of the protein is a large globular N-terminus region  followed  by  a  more  elongated  C-terminal  region ( 17, 44 ). ","type":"Discussion"},{"text":"Interestingly,  results  from Figure 5 (lane at 50°C) indicate that fragments lacking the C-domain   (e.g.,   bands   1-3)   exhibit   increased   thermals tability in comparison to full-length CRT. This observation suggests that the C-domain may be an important determinant in  initiating  the  thermal  denaturation  of  CRT  and  also supports the view that this domain is likely to adopt a moreloosely  packed  conformation  in  solution","type":"Discussion"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-16T15:29:35.169Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":18,"end":417,"reference_id":"11101311","reference_source":"pmid","reference_html":"Probing the three-dimensional structure of human calreticulin. <i> Bouvier M, Stafford WF. </i> Biochemistry, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00333r011","statement":[{"text":"Based on its elution position corresponding to that of a globular protein of MW 158 kDa (Figure 1A), the Stokes radius of CRT was calculated to be 46.2 Å (see Experimental Procedures). This value is considerably larger than the calculated value of 29.4 Å assuming CRT to be a monomeric globular protein in solution (see Experimental Procedures). The experimentally determined Stokes radius of 46.2 Å is, however, significantly different from the calculated value of 64.2 Å assuming CRT to be completely unfolded in solution","type":"Results"},{"text":"Consequently, the apparent large size of CRT determined on the gel filtration column is more likely to be accounted for on the basis of its intrinsic molecular properties such as the presence of partly denatured regions, a welldefined oligomeric state in solution, an asymmetric shape, or a combination of these factors.","type":"Results"},{"text":"Our results from gel filtration chromatography indicate that CRT elutes at a position corresponding to a significantly larger size based on calibration of the column using globular protein standards.","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-16T07:43:29.728Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":18,"end":417,"reference_id":"11101311","reference_source":"pmid","reference_html":"Probing the three-dimensional structure of human calreticulin. <i> Bouvier M, Stafford WF. </i> Biochemistry, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00333r012","statement":[{"text":"Taken together, the CD analysis suggests that although the three-dimensional structure of CRT is overall characterized by well-packed side chains, as evidenced by the pronounced near-UV CD spectrum and the cooperative nature of the thermal denaturation transitions, the relatively low Tm values suggest a marginally stable core structure.","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-16T07:43:36.945Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":199,"end":204,"reference_id":"28655748","reference_source":"pmid","reference_html":"Structural and functional analysis of the GABARAP interaction motif (GIM). <i> Rogov VV, Stolz A, Ravichandran AC, Rios-Szwed DO, Suzuki H, Kniss A, Löhr F, Wakatsuki S, Dötsch V, Dikic I, Dobson RC, McEwan DG. </i> EMBO Rep, 2017","date":"2022-05-31T13:58:50.971Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005581","ec_ontology":"ECO","ec_name":"enzyme-linked immunoabsorbent assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","region_id":"DP00333r013","statement":[{"text":"LIR motifs of known autophagy receptors and adaptors feature mATG8 specificity.","type":"Results"},{"text":"A high number of autophagy receptors or adaptor structures have been reported, yet the basis for their selective interaction with individual members of the ATG8 family is not well understood. We speculated whether the LIR motif alone is able to confer selectivity towards a mATG8 subfamily and whether we could derive a subfamily consensus motif from analysis of known mATG8 interaction partners. To address this question, we screened an array of peptides (presented in Fig EV1A and described in Materials and Methods) with the LIR sequences of 30 known and validated autophagy receptors and adaptors (Table 1) against all six human mATG8s for binding (Figs 1A and EV1B and C). In brief, biotinylated peptides were immobilized on streptavidin‐coated 96‐well plates and incubated with His6‐tagged mATG8 proteins. After washing steps, peptide‐bound mATG8 was detected in an ELISA reader using anti‐His antibodies directly conjugated to HRP (horse radish peroxidase; Fig EV1A).","type":"Results"},{"text":"The annotated region include the LIR motif (WDFL) at position 200-203.","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T09:17:54.889Z"}},{"start":199,"end":204,"reference_id":"28655748","reference_source":"pmid","reference_html":"Structural and functional analysis of the GABARAP interaction motif (GIM). <i> Rogov VV, Stolz A, Ravichandran AC, Rios-Szwed DO, Suzuki H, Kniss A, Löhr F, Wakatsuki S, Dötsch V, Dikic I, Dobson RC, McEwan DG. </i> EMBO Rep, 2017","date":"2022-05-31T14:00:04.975Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005581","ec_ontology":"ECO","ec_name":"enzyme-linked immunoabsorbent assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","region_id":"DP00333r014","statement":[{"text":"LIR motifs of known autophagy receptors and adaptors feature mATG8 specificity.","type":"Results"},{"text":"A high number of autophagy receptors or adaptor structures have been reported, yet the basis for their selective interaction with individual members of the ATG8 family is not well understood. We speculated whether the LIR motif alone is able to confer selectivity towards a mATG8 subfamily and whether we could derive a subfamily consensus motif from analysis of known mATG8 interaction partners. To address this question, we screened an array of peptides (presented in Fig EV1A and described in Materials and Methods) with the LIR sequences of 30 known and validated autophagy receptors and adaptors (Table 1) against all six human mATG8s for binding (Figs 1A and EV1B and C). In brief, biotinylated peptides were immobilized on streptavidin‐coated 96‐well plates and incubated with His6‐tagged mATG8 proteins. After washing steps, peptide‐bound mATG8 was detected in an ELISA reader using anti‐His antibodies directly conjugated to HRP (horse radish peroxidase; Fig EV1A).","type":"Results"},{"text":"The annotated region include the LIR motif (WDFL) at position 200-203.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T09:43:42.446Z"}},{"start":199,"end":204,"reference_id":"17916189","reference_source":"pmid","reference_html":"Identification of calreticulin as a ligand of GABARAP by phage display screening of a peptide library. <i> Mohrlüder J, Stangler T, Hoffmann Y, Wiesehan K, Mataruga A, Willbold D. </i> FEBS J, 2007","date":"2022-06-28T10:06:45.089Z","curator_id":"vpromp","curator_name":"Vasilis J Promponas","curator_orcid":"0000-0003-3352-4831","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001186","ec_ontology":"ECO","ec_name":"immunocytochemistry evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"O95166","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00333r016","statement":[{"text":"Immunocytochemical localization studies in fixed NEURO-2a (N2a) cells showed that both proteins partially colocalize, or at least are not visibly separated, in different cellular compartments (Fig. 6). In addition to the reported cytosolic appearance of both GABARAP and CRT [[4, 18]], these results indicate the possibility for direct interaction.","type":"Results"},{"text":"Figure 6 Localization of GABARAP and CRT in fixed N2a cells. (A) Differential interference contrast image of N2a cells. (B) Immunofluorescence of Alexa488-labelled anti-GABARAP serum in green. (C) Immunofluorescence of Alexa647-labelled anti-CRT serum in red. (D) Merging of (B) and (C).","type":"Figure"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T11:11:11.998Z"}},{"start":199,"end":204,"reference_id":"17916189","reference_source":"pmid","reference_html":"Identification of calreticulin as a ligand of GABARAP by phage display screening of a peptide library. <i> Mohrlüder J, Stangler T, Hoffmann Y, Wiesehan K, Mataruga A, Willbold D. </i> FEBS J, 2007","date":"2022-06-28T12:15:49.085Z","curator_id":"vpromp","curator_name":"Vasilis J Promponas","curator_orcid":"0000-0003-3352-4831","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"O95166","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00333r017","statement":[{"text":"Immunocytochemical localization studies in fixed NEURO-2a (N2a) cells showed that both proteins partially colocalize, or at least are not visibly separated, in different cellular compartments (Fig. 6). In addition to the reported cytosolic appearance of both GABARAP and CRT [[4, 18]], these results indicate the possibility for direct interaction.","type":"Results"},{"text":"Figure 6 Localization of GABARAP and CRT in fixed N2a cells. (A) Differential interference contrast image of N2a cells. (B) Immunofluorescence of Alexa488-labelled anti-GABARAP serum in green. (C) Immunofluorescence of Alexa647-labelled anti-CRT serum in red. (D) Merging of (B) and (C).","type":"Figure"},{"text":"Indeed, Sepharose-immobilized GABARAP was found to interact with endogenous CRT from brain extracts (Fig. 7A). By contrast, Sepharose without immobilized GABARAP, but otherwise identically treated, did not show CRT immunoreactivity.","type":"Results"},{"text":"Figure 7 GABARAP associates with CRT. (A) Endogenous CRT binds to immobilized GABARAP. Control Sepharose alone (lane 2) and Sepharose-coupled GABARAP in the presence (lane 3) and absence (lane 4) of 1150 µm N1 were exposed to rat brain extracts. After extensive washing, bound material was resolved by SDS-PAGE and analysed by immunoblotting with anti-CRT serum. Control Sepharose (lane 2) shows no indication for binding, whereas Sepharose-coupled GABARAP exhibits immunoreactivity for CRT. Only very weak immunoreactivity was observed in the presence of N1 peptide (lane 4). For convenience, lane 1 shows the bands of a prestained protein marker (Prestained Protein Marker, Broad Range, NEB, Beverly, MA, USA). (B) Endogenous GABARAP binds to immobilized CRT. Control Sepharose (lane 2) and Sepharose-coupled CRT were exposed to rat brain extracts. After extensive washing, bound material was resolved by SDS-PAGE and analysed by immunoblotting with anti-GABARAP serum. Two signals with GABARAP immunoreactivity are clearly visible.","type":"Figure"},{"text":"The interaction of CRT and GABARAP was further confirmed by a pull-down experiment of endogenous GABARAP with recombinant CRT immobilized on NHS-activated Sepharose (CRT-Sepharose). CRT-Sepharose was exposed to rat brain extracts, and CRT-Sepharose-associated proteins were separated by SDS-PAGE and probed by western blot analysis for GABARAP immunoreactivity. Sepharose-immobilized CRT was found to interact with endogenous GABARAP from brain extracts (Fig. 7B). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T12:35:42.505Z"}},{"start":199,"end":204,"reference_id":"17916189","reference_source":"pmid","reference_html":"Identification of calreticulin as a ligand of GABARAP by phage display screening of a peptide library. <i> Mohrlüder J, Stangler T, Hoffmann Y, Wiesehan K, Mataruga A, Willbold D. </i> FEBS J, 2007","date":"2022-06-28T10:12:13.184Z","curator_id":"vpromp","curator_name":"Vasilis J Promponas","curator_orcid":"0000-0003-3352-4831","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"O95166","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00333r018","statement":[{"text":"SPR was used to investigate quantitatively the interaction of recombinant GABARAP with recombinant CRT. GABARAP was immobilized on a CM5 sensor chip using standard amine coupling procedures. The injection of CRT on the sensor chip resulted in binding to GABARAP, as indicated by an injection time-dependent increase in the SPR response. Dissociation of bound CRT from the sensor chip was very slow, indicating a very low dissociation rate of CRT from GABARAP. Apart from a small change in the bulk refractive index during injection, no interaction of CRT with the reference surface was observed.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T11:11:07.184Z"}},{"start":199,"end":204,"reference_id":"17916189","reference_source":"pmid","reference_html":"Identification of calreticulin as a ligand of GABARAP by phage display screening of a peptide library. <i> Mohrlüder J, Stangler T, Hoffmann Y, Wiesehan K, Mataruga A, Willbold D. </i> FEBS J, 2007","date":"2022-06-28T10:15:07.887Z","curator_id":"vpromp","curator_name":"Vasilis J Promponas","curator_orcid":"0000-0003-3352-4831","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"O95166","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00333r019","statement":[{"text":"1H–15N correlation NMR (heteronuclear single quantum correlation, HSQC) spectra of GABARAP labelled with the stable isotope 15N were recorded during the course of titration with unlabelled CRT. The NMR spectrum of GABARAP without CRT exhibited the known and expected resonances typical for natively folded GABARAP [[22]]. The addition of CRT to GABARAP resulted in the disappearance of GABARAP resonances, a clear indication of binding (Fig. 3B). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T13:16:47.729Z"}},{"start":18,"end":417,"reference_id":"11149926","reference_source":"pmid","reference_html":"Calreticulin Is a receptor for nuclear export. <i> Holaska JM, Black BE, Love DC, Hanover JA, Leszyk J, Paschal BM. </i> J Cell Biol, 2001","date":"2022-07-26T14:21:26.926Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005049","term_name":"nuclear export signal receptor activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001158","ec_ontology":"ECO","ec_name":"cell permeability assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","region_id":"DP00333r020","statement":[{"text":"These results indicate that nuclear export mediated by CRT requires specific recognition of the NES within PKI. ","type":"Results"},{"text":"Taken together, our data indicate that CRT and Ran cooperate to mediate nuclear export of PKI, and that this pathway involves CRT recognition of the leucine-rich NES of PKI. These properties are consistent with CRT functioning as a nuclear export receptor for PKI.","type":"Results"},{"text":"Thus, CRT and Ran exhibit cooperative binding to the NES. The binding of CRT and Ran in this reaction is specific for a WT NES, since addition of these proteins to a surface containing a mutant NES did not cause a detectable increase in refractive index (light blue tracing).","type":"Results"}],"term_comment":"","term_def":"\"Combining with a nuclear export signal (NES) on a cargo to be transported, to mediate transport of a the cargo through the nuclear pore, from the nuclear lumen to the cytoplasm. The cargo can be either a RNA or a protein.\" [GOC:bf, GOC:mah, GOC:pg, GOC:vw, PMID:11743003, PMID:25802992, PMID:28713609, Wikipedia:Nuclear_transport]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:13:14.822Z"}},{"start":261,"end":278,"reference_id":"9922153","reference_source":"pmid","reference_html":"Evidence that C1q binds specifically to CH2-like immunoglobulin gamma motifs present in the autoantigen calreticulin and interferes with complement activation. <i> Kovacs H, Campbell ID, Strong P, Johnson S, Ward FJ, Reid KB, Eggleton P. </i> Biochemistry, 1998","date":"2022-07-26T14:57:54.781Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0001849","term_name":"complement component C1q complex binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","region_id":"DP00333r021","statement":[{"text":"Interestingly, the mapping studies revealed other unique C1q binding sites in the CRT sequence of a non-CH2-like nature; a site in the N-domain of CRT (peptides 35−40, Figure 1B) was observed to bind to C1q encompassing the amino acids TDMHGDSEYNIMFGPDICGPGTKKVHV (amino acids 103−129). The peptide 51 corresponding to the amino acid sequence FTHLYTLIVRPDNTY (amino acids 150−165) also demonstrated strong binding to C1q. As shown in Figure 2, a non-CH2-like region peptide present in the P-domain (peptide 79−82), WEPPVIQNPEYKGEWKPR (amino acids 244−261), bound to C1q in addition to the CH2-like domain present in the P-domain, WDERAKID.","type":"Results"},{"text":"The region 244−261, mentioned by the authors, corresponds to the 261-278 region of the full protein.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a C1q complex, a component of the classical complement cascade.\" [GOC:add, ISBN:0781735149]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"P02745","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P02746","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P02747","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:13:20.936Z"}},{"start":120,"end":146,"reference_id":"9922153","reference_source":"pmid","reference_html":"Evidence that C1q binds specifically to CH2-like immunoglobulin gamma motifs present in the autoantigen calreticulin and interferes with complement activation. <i> Kovacs H, Campbell ID, Strong P, Johnson S, Ward FJ, Reid KB, Eggleton P. </i> Biochemistry, 1998","date":"2022-07-26T14:56:51.588Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0001849","term_name":"complement component C1q complex binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P02745","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P02746","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P02747","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP00333r022","statement":[{"text":"Interestingly, the mapping studies revealed other unique C1q binding sites in the CRT sequence of a non-CH2-like nature; a site in the N-domain of CRT (peptides 35−40, Figure 1B) was observed to bind to C1q encompassing the amino acids TDMHGDSEYNIMFGPDICGPGTKKVHV (amino acids 103−129). The peptide 51 corresponding to the amino acid sequence FTHLYTLIVRPDNTY (amino acids 150−165) also demonstrated strong binding to C1q. As shown in Figure 2, a non-CH2-like region peptide present in the P-domain (peptide 79−82), WEPPVIQNPEYKGEWKPR (amino acids 244−261), bound to C1q in addition to the CH2-like domain present in the P-domain, WDERAKID.","type":"Results"},{"text":"The region 103−129, mentioned by the authors, corresponds to the 120-146 region of the full protein.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a C1q complex, a component of the classical complement cascade.\" [GOC:add, ISBN:0781735149]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:13:23.350Z"}},{"start":168,"end":182,"reference_id":"9922153","reference_source":"pmid","reference_html":"Evidence that C1q binds specifically to CH2-like immunoglobulin gamma motifs present in the autoantigen calreticulin and interferes with complement activation. <i> Kovacs H, Campbell ID, Strong P, Johnson S, Ward FJ, Reid KB, Eggleton P. </i> Biochemistry, 1998","date":"2022-07-26T14:56:08.968Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0001849","term_name":"complement component C1q complex binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P02745","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P02746","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P02747","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP00333r023","statement":[{"text":"Interestingly, the mapping studies revealed other unique C1q binding sites in the CRT sequence of a non-CH2-like nature; a site in the N-domain of CRT (peptides 35−40, Figure 1B) was observed to bind to C1q encompassing the amino acids TDMHGDSEYNIMFGPDICGPGTKKVHV (amino acids 103−129). The peptide 51 corresponding to the amino acid sequence FTHLYTLIVRPDNTY (amino acids 150−165) also demonstrated strong binding to C1q. As shown in Figure 2, a non-CH2-like region peptide present in the P-domain (peptide 79−82), WEPPVIQNPEYKGEWKPR (amino acids 244−261), bound to C1q in addition to the CH2-like domain present in the P-domain, WDERAKID.","type":"Results"},{"text":"The region 150−165, mentioned by the authors, corresponds to the 168-182 region of the full protein.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a C1q complex, a component of the classical complement cascade.\" [GOC:add, ISBN:0781735149]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:13:25.037Z"}},{"start":219,"end":226,"reference_id":"9922153","reference_source":"pmid","reference_html":"Evidence that C1q binds specifically to CH2-like immunoglobulin gamma motifs present in the autoantigen calreticulin and interferes with complement activation. <i> Kovacs H, Campbell ID, Strong P, Johnson S, Ward FJ, Reid KB, Eggleton P. </i> Biochemistry, 1998","date":"2022-07-26T14:53:42.806Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0001849","term_name":"complement component C1q complex binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P02745","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P02746","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P02747","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP00333r024","statement":[{"text":"Interestingly, the mapping studies revealed other unique C1q binding sites in the CRT sequence of a non-CH2-like nature; a site in the N-domain of CRT (peptides 35−40, Figure 1B) was observed to bind to C1q encompassing the amino acids TDMHGDSEYNIMFGPDICGPGTKKVHV (amino acids 103−129). The peptide 51 corresponding to the amino acid sequence FTHLYTLIVRPDNTY (amino acids 150−165) also demonstrated strong binding to C1q. As shown in Figure 2, a non-CH2-like region peptide present in the P-domain (peptide 79−82), WEPPVIQNPEYKGEWKPR (amino acids 244−261), bound to C1q in addition to the CH2-like domain present in the P-domain, WDERAKID.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a C1q complex, a component of the classical complement cascade.\" [GOC:add, ISBN:0781735149]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:13:26.573Z"}}],"released":"2016_10","uniref100":"UniRef100_P27797","date":"2016-09-18T21:03:25.000Z","acc":"P27797","name":"Calreticulin","length":417,"organism":"Homo sapiens","dataset":["Extracellular matrix proteins","Cancer-related proteins","Autophagy-related proteins"],"UniParc":"UPI000004CEC9","genes":[{"name":{"value":"CALR","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:1455","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:1455"}}]},"synonyms":[{"value":"CRTC"}]}],"alphafold_very_low_content":0.02877697841726619,"disorder_content":0.9592326139088729,"disprot_consensus":{"full":[{"start":18,"end":417,"type":"D"}],"Structural state":[{"start":18,"end":417,"type":"D"}],"Biological process":[{"start":199,"end":204,"type":"F"}],"Molecular function":[{"start":18,"end":417,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00641","name":"Zn-finger in Ran binding protein and others","start":300,"end":327},{"id":"PF02201","name":"SWIB/MDM2 domain","start":34,"end":95},{"id":"PF13920","name":"Zinc finger, C3HC4 type (RING finger)","start":436,"end":484}],"gene3D":[{"start":6,"end":125,"id":"1.10.245.10","name":"SWIB/MDM2 domain"},{"start":428,"end":491,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"}]},"uniref50":"UniRef50_Q00987","sequence":"MCNTNMSVPTDGAVTTSQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEVLFYLGQYIMTKRLYDEKQQHIVYCSNDLLGDLFGVPSFSVKEHRKIYTMIYRNLVVVNQQESSDSGTSVSENRCHLEGGSDQKDLVQELQEEKPSSSHLVSRPSTSSRRRAISETEENSDELSGERQRKRHKSDSISLSFDESLALCVIREICCERSSSSESTGTPSNPDLDAGVSEHSGDWLDQDSVSDQFSVEFEVESLDSEDYSLSEEGQELSDEDDEVYQVTVYQAGESDTDSFEEDPEISLADYWKCTSCNEMNPPLPSHCNRCWALRENWLPEDKGKDKGEISEKAKLENSTQAEEGFDVPDCKKTIVNDSRESCVEENDDKITQASQSQESEDYSQPSTSSSIIYSSQEDVKEFEREETQDKEESVESSLPLNAIEPCVICQGRPKNGCIVHGKTGHLMACFTCAKKLKKRNKPCPVCRQPIQMIVLTYFP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q00987","disprot_id":"DP00334","ncbi_taxon_id":9606,"regions_counter":9,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":24,"region_id":"DP00334r001","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Structure of free MDM2 N-terminal domain reveals conformational adjustments that accompany p53-binding. <i> Uhrinova S, Uhrin D, Powers H, Watt K, Zheleva D, Fischer P, McInnes C, Barlow PN. </i> J Mol Biol, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-30T18:55:05.943Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1Z1M"},{"db":"BMRB","id":"6612"}],"reference_id":"15953616","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Multiple medium and long-range NOEs were observed for most residues between Glu25 and Tyr104, with gaps falling mainly between the elements of secondary structure.","type":"Results"},{"text":"Few long-range NOEs arising from the residues prior to Glu25 were detected, suggesting that this N-terminal segment of the protein is unlikely to interact extensively with the remainder of the MDM2N domain. The exception is Ile19, which exhibits NOEs to His96, Arg97 and Tyr100 in the N-terminal part of α2′. The measurable heteronuclear (1H,15N) NOEs (Figure 2(a)) are indeed negative or very small for N-terminal residues (Met6–Val8, The10–Val14), and T2 values are elevated (Figure 2(b)), consistent with the presence of fast (picosecond to nanosecond timescale) motion in this region.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T08:50:25.495Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":304,"region_id":"DP00334r005","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Direct detection of carbon and nitrogen nuclei for high-resolution analysis of intrinsically disordered proteins using NMR spectroscopy. <i> Gibbs EB, Kriwacki RW. </i> Methods, 2018","statement":[{"text":"Here, we compared spectral resolution and sensitivity for 2D 1H-15N and 13C-15N correlation spectra recorded through direct detection of each of the two correlated nuclei for two protein regions that are entirely disordered (Hdm2-ABD and Surf6-N) and 2D 1H-15N correlation spectra for a ~73 kDa folded, pentameric protein with two short IDRs (N130).","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":210,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"29341926","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-08-30T19:02:42.643Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T08:50:34.397Z"}},{"start":215,"end":300,"reference_id":"36309626","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>15</sup>N and <sup>13</sup>C backbone resonance assignments of the acidic domain of the human MDM2 protein. <i> Song Q, Liu XQ, Rainey JK. </i> Biomol NMR Assign, 2023","date":"2024-02-29T09:32:03.994Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":20,"statements":[{"type":"Article","text":"NMR spectra were acquired at 20.00 °C using a 500 MHz INOVA NMR spectrometer (Varian, Palo Alto, CA) equipped with a triple-resonance HCN probe with Protune."}]}],"cross_refs":[{"db":"BMRB","id":"51334"}],"region_id":"DP00334r007","statement":[{"text":"The narrow dispersion observed for the 1H resonances in the MDM2 AD (Fig. 4) is similar to that observed for the MDMX AD that we recently assigned (Song et al. 2022). Such a narrow dispersion with resonances clustered into the central region of the 1H-15N HSQC is typical for intrinsically disordered regions (Dyson and Wright 2021), as was indeed the case for the MDMX AD.","type":"Article"},{"text":"Consistent with an intrinsically disordered region, δ2D analysis of the chemical shift data demonstrates significant random-coil propensity coupled with polyproline II (PPII) propensity along the entire segment (Fig. 5 A).","type":"Article"},{"text":"Heteronuclear NOE enhancement factors < 0.65 are typically held to be indicative of considerable structural flexibility on the ps-ns time scale (Tjandra et al. 1995). The observed enhancement factors for the AD are all well below this threshold, falling in the range of − 0.2 to − 2.1 (Fig. 5B), which indicates that the AD has a high degree of structural flexibility and is consistent with the characteristics of an intrinsically disordered region.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T10:09:15.502Z"}},{"start":335,"end":437,"reference_id":"26220995","reference_source":"pmid","reference_html":"Structure of human MDM2 complexed with RPL11 reveals the molecular basis of p53 activation. <i> Zheng J, Lang Y, Zhang Q, Cui D, Sun H, Jiang L, Chen Z, Zhang R, Gao Y, Tian W, Wu W, Tang J, Chen Z. </i> Genes Dev, 2015","date":"2024-08-07T16:15:38.706Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"4XXB"}],"region_id":"DP00334r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"14434","entry_name":"imidazole"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"41218","entry_name":"mercaptoethanol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62913"}],"statement":[{"text":"The solved structure contained RPL11 and part of MDM2 (Fig. 1A,B; Supplemental Movie 1), most likely because of MDM2 degradation during the crystallization process. The final model included MDM2 residues 293–334, RPL11 residues 13–178 (residues 139–155 were missing), two zinc ions, one imidazole molecule, one β-mercaptoethanol molecule, and 84 water molecules.","type":"Results"},{"text":"The combination of the missing electron density for this region with the data from AlphaFold and MobiDB predictors, indicates this region is disorder rather than missing from the crystal due to degradation.","type":"Curator statement"}]},{"start":1,"end":24,"reference_id":"15953616","reference_source":"pmid","reference_html":"Structure of free MDM2 N-terminal domain reveals conformational adjustments that accompany p53-binding. <i> Uhrinova S, Uhrin D, Powers H, Watt K, Zheleva D, Fischer P, McInnes C, Barlow PN. </i> J Mol Biol, 2005","date":"2025-04-25T12:34:20.119Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"1Z1M"}],"region_id":"DP00334r009","statement":[{"text":"Few long-range NOEs arising from the residues prior to Glu25 were detected, suggesting that this N-terminal segment of the protein is unlikely to interact extensively with the remainder of the MDM2N domain. The exception is Ile19, which exhibits NOEs to His96, Arg97 and Tyr100 in the N-terminal part of α2′. The measurable heteronuclear (1H,15N) NOEs (Figure 2(a)) are indeed negative or very small for N-terminal residues (Met6–Val8, The10–Val14), and T2 values are elevated (Figure 2(b)), consistent with the presence of fast (picosecond to nanosecond timescale) motion in this region.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T22:31:23.622Z"}}],"released":"2016_10","uniref100":"UniRef100_Q00987","date":"2016-09-06T14:37:01.000Z","acc":"Q00987","name":"E3 ubiquitin-protein ligase Mdm2","length":491,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI000002E23E","genes":[{"name":{"value":"MDM2"}}],"alphafold_very_low_content":0.47657841140529533,"disorder_content":0.45213849287169044,"disprot_consensus":{"full":[{"start":1,"end":24,"type":"D"},{"start":210,"end":304,"type":"D"},{"start":335,"end":437,"type":"D"}],"Structural state":[{"start":1,"end":24,"type":"D"},{"start":210,"end":304,"type":"D"},{"start":335,"end":437,"type":"D"}],"Disorder function":[{"start":1,"end":24,"type":"F"}]}},{"features":{"pfam":[{"id":"PF07392","name":"Cyclin-dependent kinase inhibitor 2a p19Arf N-terminus","start":4,"end":54}]},"uniref50":"UniRef50_Q64364","sequence":"MGRRFLVTVRIQRAGRPLQERVFLVKFVRSRRPRTASCALAFVNMLLRLERILRRGPHRNPGPGDDDGQRSRSSSSAQLRCRFELRGPHYLLPPGARRSAGRLPGHAGGAARVRGSAGCARCLGSPAARLGPRAGTSRHRAIFAFRWVLFVFRWVVFVYRWERRPDRRA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q64364","disprot_id":"DP00335","ncbi_taxon_id":10090,"regions_counter":5,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":37,"region_id":"DP00335r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Defining the molecular basis of Arf and Hdm2 interactions. <i> Bothner B, Lewis WS, DiGiammarino EL, Weber JD, Bothner SJ, Kriwacki RW. </i> J Mol Biol, 2001","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"11718560","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":37,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"11718560","version":3,"reference_html":"Defining the molecular basis of Arf and Hdm2 interactions. <i> Bothner B, Lewis WS, DiGiammarino EL, Weber JD, Bothner SJ, Kriwacki RW. </i> J Mol Biol, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00335r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":37,"region_id":"DP00335r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Defining the molecular basis of Arf and Hdm2 interactions. <i> Bothner B, Lewis WS, DiGiammarino EL, Weber JD, Bothner SJ, Kriwacki RW. </i> J Mol Biol, 2001","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"11718560","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1HN3"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":37,"term_name":"disorder to order","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"11718560","version":2,"reference_html":"Defining the molecular basis of Arf and Hdm2 interactions. <i> Bothner B, Lewis WS, DiGiammarino EL, Weber JD, Bothner SJ, Kriwacki RW. </i> J Mol Biol, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00335r004","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":37,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"11718560","version":3,"reference_html":"Defining the molecular basis of Arf and Hdm2 interactions. <i> Bothner B, Lewis WS, DiGiammarino EL, Weber JD, Bothner SJ, Kriwacki RW. </i> J Mol Biol, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00335r005","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q64364","date":"2016-09-06T11:33:25.000Z","acc":"Q64364","name":"Tumor suppressor ARF","length":169,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000022EE6","genes":[{"name":{"value":"Cdkn2a","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAB35770.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAB35770.1"}},{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:104738","url":"http://www.informatics.jax.org/marker/MGI:104738"}}]}}],"alphafold_very_low_content":0.47337278106508873,"disorder_content":0.21893491124260356,"disprot_consensus":{"full":[{"start":1,"end":37,"type":"T"}],"Structural state":[{"start":1,"end":37,"type":"D"}],"Molecular function":[{"start":1,"end":37,"type":"F"}],"Structural transition":[{"start":1,"end":37,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00692","name":"dUTPase","start":17,"end":150}],"gene3D":[{"start":1,"end":151,"id":"2.70.40.10","name":"2.70.40.10"}]},"uniref50":"UniRef50_P06968","sequence":"MMKKIDVKILDPRVGKEFPLPTYATSGSAGLDLRACLNDAVELAPGDTTLVPTGLAIHIADPSLAAMMLPRSGLGHKHGIVLGNLVGLIDSDYQGQLMISVWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFDATDRGEGGFGHSGRQ","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P06968","disprot_id":"DP00337","ncbi_taxon_id":83333,"regions_counter":4,"creator":"zdosztanyi","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":152,"region_id":"DP00337r001","reference_id":"1311056","start":137,"ec_id":"ECO:0006220","curator_orcid":"0000-0001-9224-9820","statement":[{"text":"The sequence of residues 137-152 (not visible in the electron density maps) is particularly rich in glycines","type":"Article"},{"text":"Figure 2a and b shows a topology diagram and a ribbon representation of the subunit which consists of a polypeptide chain of 152 amino acid residues; the first 136 of these are visible in the crystal structure. ","type":"Article"}],"curator_id":"ahatos","released":"2022_03","term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Crystal structure of a dUTPase. <i> Cedergren-Zeppezauer ES, Larsson G, Nyman PO, Dauter Z, Wilson KS. </i> Nature, 1992","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","cross_refs":[{"db":"PDB","id":"1DUP"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":152,"region_id":"DP00337r002","reference_id":"11257499","start":138,"ec_id":"ECO:0006165","curator_orcid":"0000-0001-9224-9820","curator_id":"ahatos","released":"2022_03","term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"reference_html":"The C-terminus of dUTPase: observation on flexibility using NMR. <i> Nord J, Nyman P, Larsson G, Drakenberg T. </i> FEBS Lett, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P06968","date":"2016-09-08T18:22:32.000Z","acc":"P06968","name":"Deoxyuridine 5'-triphosphate nucleotidohydrolase","length":152,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI0000129979","genes":[{"name":{"value":"dut"},"synonyms":[{"value":"dnaS"},{"value":"sof"}],"olnNames":[{"value":"b3640"},{"value":"JW3615"}]}],"alphafold_very_low_content":0,"disorder_content":0.10526315789473684,"disprot_consensus":{"full":[{"start":137,"end":152,"type":"D"}],"Structural state":[{"start":137,"end":152,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03414","name":"Glycosyltransferase family 6","start":41,"end":353}],"gene3D":[{"start":60,"end":354,"id":"3.90.550.10","name":"Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A"}]},"uniref50":"UniRef50_P16442","sequence":"MAEVLRTLAGKPKCHALRPMILFLIMLVLVLFGYGVLSPRSLMPGSLERGFCMAVREPDHLQRVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQNTTIGLTVFAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRVTLGTGRQLSVLEVRAYKRWQDVSMRRMEMISDFCERRFLSEVDYLVCVDVDMEFRDHVGVEILTPLFGTLHPGFYGSSREAFTYERRPQSQAYIPKDEGDFYYLGGFFGGSVQEVQRLTRACHQAMMVDQANGIEAVWHDESHLNKYLLRHKPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVPKNHQAVRNP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P16442","disprot_id":"DP00339","ncbi_taxon_id":9606,"regions_counter":2,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":194,"region_id":"DP00339r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The structural basis for specificity in human ABO(H) blood group biosynthesis. <i> Patenaude SI, Seto NO, Borisova SN, Szpacenko A, Marcus SL, Palcic MM, Evans SV. </i> Nat Struct Biol, 2002","term_id":"IDPO:0000002","curator_id":"fquaglia","start":179,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12198488","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1LZ0"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":194,"term_name":"entropic chain","start":179,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12198488","version":3,"reference_html":"The structural basis for specificity in human ABO(H) blood group biosynthesis. <i> Patenaude SI, Seto NO, Borisova SN, Szpacenko A, Marcus SL, Palcic MM, Evans SV. </i> Nat Struct Biol, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0006220","region_id":"DP00339r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_P16442","date":"2016-08-25T12:55:26.000Z","acc":"P16442","name":"Histo-blood group ABO system transferase","length":354,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000004EBC0","genes":[{"name":{"value":"ABO"}}],"alphafold_very_low_content":0.11581920903954802,"disorder_content":0.04519774011299435,"disprot_consensus":{"full":[{"start":179,"end":194,"type":"D"}],"Structural state":[{"start":179,"end":194,"type":"D"}],"Disorder function":[{"start":179,"end":194,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00061","name":"Lipocalin / cytosolic fatty-acid binding protein family","start":5,"end":137}],"gene3D":[{"start":2,"end":137,"id":"2.40.128.20","name":"2.40.128.20"}]},"uniref50":"UniRef50_P62965","sequence":"MPNFAGTWKMRSSENFDELLKALGVNAMLRKVAVAAASKPHVEIRQDGDQFYIKTSTTVRTTEINFKVGEGFEEETVDGRKCRSLPTWENENKIHCTQTLLEGDGPKTYWTRELANDELILTFGADDVVCTRIYVRE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P62965","disprot_id":"DP00340","ncbi_taxon_id":10090,"regions_counter":3,"creator":"maspromonte","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":137,"region_id":"DP00340r001","released":"2022_03","ec_id":"ECO:0006236","reference_html":"Crystal structure of cellular retinoic acid binding protein I shows increased access to the binding cavity due to formation of an intermolecular beta-sheet. <i> Thompson JR, Bratt JM, Banaszak LJ. </i> J Mol Biol, 1995","term_id":"IDPO:0000002","curator_id":"maspromonte","start":1,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1CBR"},{"db":"PDB","id":"1CBI"}],"reference_id":"7563063","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":137,"term_name":"order to disorder","released":"2022_03","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","reference_html":"Crystal structure of cellular retinoic acid binding protein I shows increased access to the binding cavity due to formation of an intermolecular beta-sheet. <i> Thompson JR, Bratt JM, Banaszak LJ. </i> J Mol Biol, 1995","term_id":"IDPO:0000014","curator_id":"maspromonte","start":1,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","reference_id":"7563063","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006236","region_id":"DP00340r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":137,"term_name":"protein binding","released":"2022_03","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","reference_html":"Crystal structure of cellular retinoic acid binding protein I shows increased access to the binding cavity due to formation of an intermolecular beta-sheet. <i> Thompson JR, Bratt JM, Banaszak LJ. </i> J Mol Biol, 1995","term_id":"GO:0005515","curator_id":"maspromonte","start":1,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"7563063","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006236","region_id":"DP00340r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P62965","date":"2016-09-03T17:48:02.000Z","acc":"P62965","name":"Cellular retinoic acid-binding protein 1","length":137,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000027652","genes":[{"name":{"value":"Crabp1"}}],"alphafold_very_low_content":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":137,"type":"T"}],"Structural state":[{"start":1,"end":137,"type":"D"}],"Structural transition":[{"start":1,"end":137,"type":"T"}],"Molecular function":[{"start":1,"end":137,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":229,"end":262},{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":351,"end":390},{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":432,"end":473},{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":584,"end":622}],"gene3D":[{"start":133,"end":686,"id":"1.25.10.10","name":"Leucine-rich Repeat Variant"}]},"uniref50":"UniRef50_Q02248","sequence":"MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEALGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q02248","disprot_id":"DP00341","dataset":[],"ncbi_taxon_id":10090,"regions_counter":16,"creator":"gerdos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":781,"region_id":"DP00341r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Biochemical and structural characterization of β-catenin interactions with nonphosphorylated and CK2-phosphorylated Lef-1. <i> Sun J, Weis WI. </i> J Mol Biol, 2011","term_id":"IDPO:0000002","curator_id":"droche","start":664,"term_ontology":"IDPO","curator_name":"Daniel Roche","reference_id":"21075118","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3OUW"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":781,"term_name":"molecular function activator activity","start":664,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"GO","curator_name":"Daniel Roche","reference_id":"21075118","version":3,"reference_html":"Biochemical and structural characterization of β-catenin interactions with nonphosphorylated and CK2-phosphorylated Lef-1. <i> Sun J, Weis WI. </i> J Mol Biol, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140677","ec_id":"ECO:0006220","region_id":"DP00341r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":781,"term_name":"nucleic acid binding","start":664,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"GO","curator_name":"Daniel Roche","reference_id":"21075118","version":3,"reference_html":"Biochemical and structural characterization of β-catenin interactions with nonphosphorylated and CK2-phosphorylated Lef-1. <i> Sun J, Weis WI. </i> J Mol Biol, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006220","region_id":"DP00341r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":133,"region_id":"DP00341r004","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Three-dimensional structure of the armadillo repeat region of beta-catenin. <i> Huber AH, Nelson WJ, Weis WI. </i> Cell, 1997","term_id":"IDPO:0000002","curator_id":"zdosztanyi","start":1,"term_ontology":"IDPO","curator_name":"Zsuzsanna Dosztányi","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"9298899","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":781,"region_id":"DP00341r005","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Three-dimensional structure of the armadillo repeat region of beta-catenin. <i> Huber AH, Nelson WJ, Weis WI. </i> Cell, 1997","term_id":"IDPO:0000002","curator_id":"zdosztanyi","start":672,"term_ontology":"IDPO","curator_name":"Zsuzsanna Dosztányi","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"9298899","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":48,"region_id":"DP00341r006","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Solution structure of a peptide derived from the oncogenic protein beta-Catenin in its phosphorylated and nonphosphorylated states. <i> Megy S, Bertho G, Gharbi-Benarous J, Baleux F, Benarous R, Girault JP. </i> Peptides, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":17,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-22T16:02:25.241Z","reference_source":"pmid","term_name":"disorder","reference_id":"15629534","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Comparison of the NOESY spectra showed significantly less NOEs connectivities for the nonphosphorylated peptide (256 versus 352 for the phosphorylated peptide, Table 5), indicating a less structured state. In the 1HN/1Hα region, the nonphosphorylated peptide showed less dispersed signals for both amide and α protons of the nonphosphorylated peptide.","type":"Results"},{"text":"The global rmsd is high (5.7 Å for the backbone), suggesting an unstructured state, but by superimposing the structures, a general tendency can be detected.","type":"Discussion"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":48,"region_id":"DP00341r011","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Solution structure of a peptide derived from the oncogenic protein beta-Catenin in its phosphorylated and nonphosphorylated states. <i> Megy S, Bertho G, Gharbi-Benarous J, Baleux F, Benarous R, Girault JP. </i> Peptides, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":17,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-22T15:49:31.955Z","reference_source":"pmid","term_name":"disorder","reference_id":"15629534","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"From the CD spectra, the nonphosphorylated peptide does not appear to show any helical structure, even after the addition of TFE. This peptide appears to be less structured and more flexible than P-β-Cat17–48. In addition, the 205 nm negative band could show a possible type I β-turn structure.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_Q02248","date":"2016-09-06T14:31:57.000Z","acc":"Q02248","name":"Catenin beta-1","length":781,"organism":"Mus musculus","UniParc":"UPI000000BC60","genes":[{"name":{"value":"Ctnnb1"},"synonyms":[{"value":"Catnb"}]}],"alphafold_very_low_content":0.19846350832266324,"disorder_content":0.3213828425096031,"disprot_consensus":{"full":[{"start":1,"end":133,"type":"D"},{"start":664,"end":781,"type":"D"}],"Structural state":[{"start":1,"end":133,"type":"D"},{"start":664,"end":781,"type":"D"}],"Molecular function":[{"start":664,"end":781,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03515","name":"Colicin-like bacteriocin tRNase domain","start":31,"end":312},{"id":"PF11570","name":"Coiled-coil receptor-binding R-domain of colicin E2","start":315,"end":447},{"id":"PF21431","name":"Colicin/Pyocin-S2, DNase domain","start":457,"end":580}],"gene3D":[{"start":453,"end":582,"id":"3.90.540.10","name":"Colicin/pyocin, DNase domain"},{"start":294,"end":452,"id":"1.10.287.620","name":"Helix Hairpins"}]},"uniref50":"UniRef50_P09883","sequence":"MSGGDGRGHNTGAHSTSGNINGGPTGIGVSGGASDGSGWSSENNPWGGGSGSGIHWGGGSGRGNGGGNGNSGGGSGTGGNLSAVAAPVAFGFPALSTPGAGGLAVSISASELSAAIAGIIAKLKKVNLKFTPFGVVLSSLIPSEIAKDDPNMMSKIVTSLPADDITESPVSSLPLDKATVNVNVRVVDDVKDERQNISVVSGVPMSVPVVDAKPTERPGVFTASIPGAPVLNISVNDSTPAVQTLSPGVTNNTDKDVRPAGFTQGGNTRDAVIRFPKDSGHNAVYVSVSDVLSPDQVKQRQDEENRRQQEWDATHPVEAAERNYERARAELNQANEDVARNQERQAKAVQVYNSRKSELDAANKTLADAIAEIKQFNRFAHDPMAGGHRMWQMAGLKAQRAQTDVNNKQAAFDAAAKEKSDADAALSAAQERRKQKENKEKDAKDKLDKESKRNKPGKATGKGKPVGDKWLDDAGKDSGAPIPDRIADKLRDKEFKSFDDFRKAVWEEVSKDPELSKNLNPSNKSSVSKGYSPFTPKNQQVGGRKVYELHHDKPISQGGEVYDMDNIRVTTPKRHIDIHRGK","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P09883","disprot_id":"DP00342","dataset":["Unicellular toxins and antitoxins"],"ncbi_taxon_id":562,"regions_counter":17,"creator":"aschramm","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":83,"region_id":"DP00342r001","reference_html":"Structural dynamics of the membrane translocation domain of colicin E9 and its interaction with TolB. <i> Collins ES, Whittaker SB, Tozawa K, MacDonald C, Boetzel R, Penfold CN, Reilly A, Clayden NJ, Osborne MJ, Hemmings AM, Kleanthous C, James R, Moore GR. </i> J Mol Biol, 2002","ec_id":"ECO:0006165","version":3,"term_id":"IDPO:0000002","curator_id":"tlazar","start":1,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"The 1H – 15N HSQC spectrum of colicin E9 (Figure 5) has a relatively narrow 1H chemical shift dispersion for the majority of signals, typical of that for a largely unstructured protein","type":"Results"},{"text":"The N-terminal region of colicin E9 is largely unstructured and flexible","type":"Results"},{"text":"chemical shift differences between the Ca, Cb and 13CO resonances of colicin E9 and those of sequence-corrected random coil values suggest that some of the residues in the N-terminal\nregion of the colicin are not in random coil conformations (Figure 8). The majority of peaks have\nlow-frequency Ca, Cb and 13CO shifts, indicating a preference for populating the b-region of (phi,psi) space, which is normal for random polypeptide chains.","type":"Results"},{"text":"the data presented here show that colicin E9 has a largely unstructured translocation domain without regular secondary structure, and thus it is not a molten globule","type":"Results"}],"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T14:34:10.513Z","curator_name":"Bálint Mészáros"},"released":"2022_03","reference_id":"12054823","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":61,"region_id":"DP00342r002","reference_html":"Characterisation of a mobile protein-binding epitope in the translocation domain of colicin E9. <i> Macdonald CJ, Tozawa K, Collins ES, Penfold CN, James R, Kleanthous C, Clayden NJ, Moore GR. </i> J Biomol NMR, 2004","ec_id":"ECO:0006165","version":3,"term_id":"IDPO:0000002","curator_id":"tlazar","start":1,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Most of the signals of the T1−61 region of the fusion protein had similar chemical shifts to those of intact colicin E9, with chemical shift differences from the sequence-corrected random coil values indicating that it lacked any stable secondary or tertiary structure.","type":"Results"}],"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T10:51:46.120Z","curator_name":"Bálint Mészáros"},"released":"2022_03","reference_id":"15452437","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00342r009","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T10:53:32.385Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":18,"term_id":"IDPO:0000002","start":2,"version":2,"statement":[{"text":"Finally, we report the structure of the OmpF- OBS1 complex that shows the colicin bound within the porin lumen spanning the membrane bilayer. Our study explains how colicins exploit porins to deliver epitope signals to the bacterial periplasm and, more broadly, how the inherent flexibility and narrow cross-sectional area of an IUP domain can endow it with the ability to traverse a biological membrane via the constricted lumen of a β-barrel membrane protein","type":"Abstract"},{"text":"the most important factors in colicin translocation are the flexibility of the polypeptide backbone and the unconstrained nature of the N terminus.","type":"Results"},{"text":"We can now add a further advantage IUPs have over their globular counterparts that centers on their flexibility and lack of structure, characteristics that allow them to traverse a membrane through the narrow channels of a protein pore in order to deliver a signal directly into a cell. The key to this transfer is the intrinsically unstructured nature of an IUP and its narrow cross-sectional area, properties that allow a macromolecule as big as 6,000 Da to pass through a protein pore that has a molecular weight cutoff filter of 600 Da.","type":"Discussion"},{"text":"The disordered character may also be derived from the fact that each of the 6 copies show different conformations – these are probably induced by the fuzzy interaction.","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"21098297","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3O0E"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"tlazar","reference_html":"Directed epitope delivery across the Escherichia coli outer membrane through the porin OmpF. <i> Housden NG, Wojdyla JA, Korczynska J, Grishkovskaya I, Kirkpatrick N, Brzozowski AM, Kleanthous C. </i> Proc Natl Acad Sci U S A, 2010","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00342r010","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T16:18:43.880Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":18,"term_id":"GO:0005515","start":2,"version":3,"statement":[{"text":"detecting binding through isothermal titration calorimetry (ITC) (see Fig. S2 and Table S1 for details). We narrowed down the main OmpF-binding site to a 17-residue epitope from the N terminus of the ColE9 IUTD (residues 2–18), for which a peptide encompassing this sequence bound OmpF with a Kd of approximately 2 μM and a stoichiometry of one colicin peptide/OmpF monomer","type":"Results"},{"text":"We denote this IUTD binding epitope as OmpF-Binding Site 1 (OBS1). The interaction of the OBS1 peptide with OmpF is characterized by a large and favorable enthalpy (ΔH = −19.1 kcal∕mol) and an unfavorable entropy change (ΔS = −37.8 cal∕mol/K), consistent with the disordered peptide becoming ordered upon complex formation.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P02931","partner_end":null}],"term_name":"protein binding","ec_name":"isothermal titration calorimetry evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"21098297","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"tlazar","reference_html":"Directed epitope delivery across the Escherichia coli outer membrane through the porin OmpF. <i> Housden NG, Wojdyla JA, Korczynska J, Grishkovskaya I, Kirkpatrick N, Brzozowski AM, Kleanthous C. </i> Proc Natl Acad Sci U S A, 2010","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00342r011","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T16:19:39.690Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":63,"term_id":"GO:0005515","start":54,"version":3,"statement":[{"text":"Delineation of OBS2 was confirmed through ITC experiments using a synthetic peptide of residues 54 to 63 of the ColE9 IUTD binding to OmpF (Fig. 1B). Although OBS2 binds 10-fold weaker to OmpF than OBS1 (Kd 1⁄4 24 μM) the thermodynamic parameters of complex formation are similar to those of OBS1 (Table S1). Importantly, when OmpF was incubated with an excess of the OBS1 peptide, OBS2 was no longer able to bind OmpF, suggest- ing the two ColE9 IUTD OmpF-binding sites associate with the same region on the porin (Fig. 1B).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P02931","partner_end":null}],"term_name":"protein binding","ec_name":"isothermal titration calorimetry evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"21098297","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"tlazar","reference_html":"Directed epitope delivery across the Escherichia coli outer membrane through the porin OmpF. <i> Housden NG, Wojdyla JA, Korczynska J, Grishkovskaya I, Kirkpatrick N, Brzozowski AM, Kleanthous C. </i> Proc Natl Acad Sci U S A, 2010","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00342r012","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T16:26:49.963Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":47,"term_id":"GO:0005515","start":32,"version":3,"statement":[{"text":"ColE9 yet further, bound TolB with the same equilibrium dissociation constant as intact colicin (Kd = 1 uM) and with very similar thermodynamic parameters. ITC data for Tpep32–47 binding TolB are shown in Fig. 5b and compared with wild-type ColE9 in Table 1. The data show that complex formation is enthalpically driven and has a negative entropy, which is typical of binding-induced disorder–order transitions of natively disordered proteins.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P0A855","partner_end":null}],"term_name":"protein binding","ec_name":"isothermal titration calorimetry evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"16894158","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"tlazar","reference_html":"Competitive recruitment of the periplasmic translocation portal TolB by a natively disordered domain of colicin E9. <i> Loftus SR, Walker D, Maté MJ, Bonsor DA, James R, Moore GR, Kleanthous C. </i> Proc Natl Acad Sci U S A, 2006","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00342r013","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T10:55:01.015Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":46,"term_id":"GO:0005515","start":34,"version":3,"statement":[{"text":"MBP-labeled ColE9 mutants could be readily crosslinked to TolB, but surprisingly these were distributed on either side of the previously identified TolB box sequence, appearing instead to form a photocrosslink footprint that spanned residues 34–46","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P0A855","partner_end":null}],"term_name":"protein binding","ec_name":"cross-linking evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"16894158","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001170","curator_id":"tlazar","reference_html":"Competitive recruitment of the periplasmic translocation portal TolB by a natively disordered domain of colicin E9. <i> Loftus SR, Walker D, Maté MJ, Bonsor DA, James R, Moore GR, Kleanthous C. </i> Proc Natl Acad Sci U S A, 2006","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00342r014","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T16:24:41.135Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":47,"term_id":"GO:0005515","start":32,"version":3,"statement":[{"text":"the structure of the ColE9 Tpep32–47–TolB complex was solved to a resolution of 2.0 Å","type":"Results"},{"text":"ColE9 Tpep32–47 binds to the ‘‘top’’ side of the B-propeller domain, distal to the N-terminal domain, with 15 of the 16 residues (32–46) contacting TolB.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P0A855","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"16894158","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2IVZ"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"tlazar","reference_html":"Competitive recruitment of the periplasmic translocation portal TolB by a natively disordered domain of colicin E9. <i> Loftus SR, Walker D, Maté MJ, Bonsor DA, James R, Moore GR, Kleanthous C. </i> Proc Natl Acad Sci U S A, 2006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00342r015","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T14:34:59.017Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":44,"term_id":"GO:0005515","start":33,"version":3,"statement":[{"text":" a reduction in the backbone segmental motions of the residues giving rise to the signals, and TolB- induced chemical shift changes together with intermediate exchange between free and bound colicin E9. Whichever is the most important mechanism, the NMR data (Figure 11) identify clearly that residues 33 – 44 of colicin E9 are affected by the inter- action with TolB.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P0A855","partner_end":null}],"term_name":"protein binding","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"12054823","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"tlazar","reference_html":"Structural dynamics of the membrane translocation domain of colicin E9 and its interaction with TolB. <i> Collins ES, Whittaker SB, Tozawa K, MacDonald C, Boetzel R, Penfold CN, Reilly A, Clayden NJ, Osborne MJ, Hemmings AM, Kleanthous C, James R, Moore GR. </i> J Mol Biol, 2002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00342r016","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T10:54:02.885Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":18,"term_id":"GO:0005515","start":2,"version":3,"statement":[{"text":"In order to define this common binding site we crystallized OmpF in the presence of the higher affinity OBS1 peptide, the resulting crystals diffracting to 3.0-Å resolution. The monoclinic asymmetric unit contained two OmpF trimers and the electron density maps revealed electron density in the lumen of all six OmpF molecules, indicating the presence of the OBS1 peptide.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P02931","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"21098297","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3O0E"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"tlazar","reference_html":"Directed epitope delivery across the Escherichia coli outer membrane through the porin OmpF. <i> Housden NG, Wojdyla JA, Korczynska J, Grishkovskaya I, Kirkpatrick N, Brzozowski AM, Kleanthous C. </i> Proc Natl Acad Sci U S A, 2010","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00342r017","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T16:55:42.268Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":47,"term_id":"IDPO:0000011","start":32,"version":2,"statement":[{"text":"ColE9 yet further, bound TolB with the same equilibrium dissociation constant as intact colicin (Kd = 1 uM) and with very similar thermodynamic parameters. ITC data for Tpep32–47 binding TolB are shown in Fig. 5b and compared with wild-type ColE9 in Table 1. The data show that complex formation is enthalpically driven and has a negative entropy, which is typical of binding-induced disorder–order transitions of natively disordered proteins.","type":"Results"}],"term_name":"disorder to order","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"16894158","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural transition","ec_id":"ECO:0006317","curator_id":"tlazar","reference_html":"Competitive recruitment of the periplasmic translocation portal TolB by a natively disordered domain of colicin E9. <i> Loftus SR, Walker D, Maté MJ, Bonsor DA, James R, Moore GR, Kleanthous C. </i> Proc Natl Acad Sci U S A, 2006","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2016_10","uniref100":"UniRef100_P09883","date":"2016-09-09T22:05:06.000Z","acc":"P09883","name":"Colicin-E9","length":582,"organism":"Escherichia coli","UniParc":"UPI0000170D11","genes":[{"name":{"value":"col"},"synonyms":[{"value":"cei"}]}],"alphafold_very_low_content":0.14432989690721648,"disorder_content":0.14261168384879724,"disprot_consensus":{"full":[{"start":1,"end":31,"type":"D"},{"start":32,"end":47,"type":"T"},{"start":48,"end":83,"type":"D"}],"Structural state":[{"start":1,"end":83,"type":"D"}],"Molecular function":[{"start":2,"end":18,"type":"F"},{"start":32,"end":47,"type":"F"},{"start":54,"end":63,"type":"F"}],"Structural transition":[{"start":32,"end":47,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00989","name":"PAS fold","start":116,"end":173},{"id":"PF07469","name":"Nuclear receptor coactivator, DUF1518","start":1291,"end":1348},{"id":"PF08815","name":"Nuclear receptor coactivator","start":1045,"end":1093},{"id":"PF08832","name":"Steroid receptor coactivator","start":616,"end":704},{"id":"PF14598","name":"PAS domain","start":265,"end":374},{"id":"PF16279","name":"Domain of unknown function (DUF4927)","start":723,"end":810},{"id":"PF16665","name":"Unstructured region on nuclear receptor coactivator protein","start":459,"end":571},{"id":"PF23172","name":"Nuclear receptor coactivators bHLH domain","start":1,"end":79}],"gene3D":[{"start":33,"end":121,"id":"4.10.280.10","name":"Helix-loop-helix DNA-binding domain"},{"start":122,"end":255,"id":"3.30.450.20","name":"PAS domain"},{"start":262,"end":372,"id":"3.30.450.20","name":"PAS domain"}]},"uniref50":"UniRef50_Q9Y6Q9","sequence":"MSGLGENLDPLASDSRKRKLPCDTPGQGLTCSGEKRRREQESKYIEELAELISANLSDIDNFNVKPDKCAILKETVRQIRQIKEQGKTISNDDDVQKADVSSTGQGVIDKDSLGPLLLQALDGFLFVVNRDGNIVFVSENVTQYLQYKQEDLVNTSVYNILHEEDRKDFLKNLPKSTVNGVSWTNETQRQKSHTFNCRMLMKTPHDILEDINASPEMRQRYETMQCFALSQPRAMMEEGEDLQSCMICVARRITTGERTFPSNPESFITRHDLSGKVVNIDTNSLRSSMRPGFEDIIRRCIQRFFSLNDGQSWSQKRHYQEAYLNGHAETPVYRFSLADGTIVTAQTKSKLFRNPVTNDRHGFVSTHFLQREQNGYRPNPNPVGQGIRPPMAGCNSSVGGMSMSPNQGLQMPSSRAYGLADPSTTGQMSGARYGGSSNIASLTPGPGMQSPSSYQNNNYGLNMSSPPHGSPGLAPNQQNIMISPRNRGSPKIASHQFSPVAGVHSPMASSGNTGNHSFSSSSLSALQAISEGVGTSLLSTLSSPGPKLDNSPNMNITQPSKVSNQDSKSPLGFYCDQNPVESSMCQSNSRDHLSDKESKESSVEGAENQRGPLESKGHKKLLQLLTCSSDDRGHSSLTNSPLDSSCKESSVSVTSPSGVSSSTSGGVSSTSNMHGSLLQEKHRILHKLLQNGNSPAEVAKITAEATGKDTSSITSCGDGNVVKQEQLSPKKKENNALLRYLLDRDDPSDALSKELQPQVEGVDNKMSQCTSSTIPSSSQEKDPKIKTETSEEGSGDLDNLDAILGDLTSSDFYNNSISSNGSHLGTKQQVFQGTNSLGLKSSQSVQSIRPPYNRAVSLDSPVSVGSSPPVKNISAFPMLPKQPMLGGNPRMMDSQENYGSSMGGPNRNVTVTQTPSSGDWGLPNSKAGRMEPMNSNSMGRPGGDYNTSLPRPALGGSIPTLPLRSNSIPGARPVLQQQQQMLQMRPGEIPMGMGANPYGQAAASNQLGSWPDGMLSMEQVSHGTQNRPLLRNSLDDLVGPPSNLEGQSDERALLDQLHTLLSNTDATGLEEIDRALGIPELVNQGQALEPKQDAFQGQEAAVMMDQKAGLYGQTYPAQGPPMQGGFHLQGQSPSFNSMMNQMNQQGNFPLQGMHPRANIMRPRTNTPKQLRMQLQQRLQGQQFLNQSRQALELKMENPTAGGAAVMRPMMQPQVSSQQGFLNAQMVAQRSRELLSHHFRQQRVAMMMQQQQQQQQQQQQQQQQQQQQQQQQQQQQQTQAFSPPPNVTASPSMDGLLAGPTMPQAPPQQFPYQPNYGMGQQPDPAFGRVSSPPNAMMSSRMGPSQNPMMQHPQAASIYQSSEMKGWPSGNLARNSSFSQQQFAHQGNPAVYSMVHMNGSSGHMGQMNMNPMPMSGMPMGPDQKYC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9Y6Q9","disprot_id":"DP00343","ncbi_taxon_id":9606,"regions_counter":15,"creator":"esalladini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1088,"region_id":"DP00343r001","released":"2023_12","ec_id":"ECO:0005642","reference_html":"Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. <i> Demarest SJ, Martinez-Yamout M, Chung J, Chen H, Xu W, Dyson HJ, Evans RM, Wright PE. </i> Nature, 2002","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1018,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"11823864","version":3,"ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","date":"2023-10-19T14:58:55.822Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Both the ACTR domain and the CBP domain are intrinsically unfolded in isolation, as indicated by the limited resonance dispersion in 1H–15N correlated NMR spectra (Fig. 1a, b).","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:29:38.499Z"}},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":1085,"term_name":"disorder to order","start":1045,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"11823864","version":3,"reference_html":"Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. <i> Demarest SJ, Martinez-Yamout M, Chung J, Chen H, Xu W, Dyson HJ, Evans RM, Wright PE. </i> Nature, 2002","date":"2023-10-19T15:03:09.595Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00343r004","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural transition","cross_refs":[{"db":"PDB","id":"1KBH"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P45481"}],"statement":[{"text":"On formation of the complex, however, the two proteins form a single, highly helical and cooperatively folded entity.","type":"Article"},{"text":"ACTR forms an intimate complex with CBP (Fig. 2), burying 1,500 Å2 in the molecular interface. The structure comprises six helices, three from the ACTR domain (denoted Aα1, Aα2 and Aα3) and three from CBP (Cα1, Cα2 and Cα3). The overall architecture seems to be new, and DALI searches11 failed to find matches in the database of known structures. Residues 1,018–1,045 and 1,084–1,088 of ACTR are unstructured in the complex.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:29:43.546Z"}},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":1088,"term_name":"protein binding","start":1018,"ec_name":"isothermal titration calorimetry evidence used in manual assertion","curator_id":"vnugnes","released":"2023_12","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"11823864","version":4,"reference_html":"Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. <i> Demarest SJ, Martinez-Yamout M, Chung J, Chen H, Xu W, Dyson HJ, Evans RM, Wright PE. </i> Nature, 2002","date":"2023-10-19T15:09:19.932Z","term_id":"GO:0005515","ec_id":"ECO:0005647","region_id":"DP00343r005","curator_orcid":"0000-0001-8399-7907","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P45481","operator":null,"partner_start":2059,"partner_end":2117}],"statement":[{"text":"High-affinity binding between CBP and ACTR (dissociation constant (Kd) = 3.4 × 10-8 M, measured by isothermal titration calorimetry; Fig. 1d) is driven by enthalpy (ΔH° = -31.7 ± 1.5 kcal mol-1). This large enthalpy decrease is partly offset by the high entropic cost (TΔS° = -21.3 ± 1.5 kcal mol-1) that is associated with the ACTR and CBP domains folding on complex formation.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:29:45.436Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1045,"region_id":"DP00343r006","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. <i> Demarest SJ, Martinez-Yamout M, Chung J, Chen H, Xu W, Dyson HJ, Evans RM, Wright PE. </i> Nature, 2002","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1018,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"11823864","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-10-19T15:06:47.199Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1KBH"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P45481"}],"statement":[{"text":"ACTR forms an intimate complex with CBP (Fig. 2), burying 1,500 Å2 in the molecular interface. The structure comprises six helices, three from the ACTR domain (denoted Aα1, Aα2 and Aα3) and three from CBP (Cα1, Cα2 and Cα3). The overall architecture seems to be new, and DALI searches11 failed to find matches in the database of known structures. Residues 1,018–1,045 and 1,084–1,088 of ACTR are unstructured in the complex.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:29:41.562Z"}},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":1085,"term_name":"protein binding","start":1045,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2023_12","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"11823864","version":4,"reference_html":"Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. <i> Demarest SJ, Martinez-Yamout M, Chung J, Chen H, Xu W, Dyson HJ, Evans RM, Wright PE. </i> Nature, 2002","date":"2023-10-19T15:06:14.899Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00343r010","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"1KBH"}],"interaction_partner":[{"db":"UniProt","id":"P45481","operator":"and","partner_start":2059,"partner_end":2117}],"statement":[{"text":"The 1H–15N NMR spectra of both CBP and ACTR gain significant amide proton dispersion on formation of the complex (Fig. 1a, b).","type":"Article"},{"text":"ACTR forms an intimate complex with CBP (Fig. 2), burying 1,500 Å2 in the molecular interface. The structure comprises six helices, three from the ACTR domain (denoted Aα1, Aα2 and Aα3) and three from CBP (Cα1, Cα2 and Cα3). The overall architecture seems to be new, and DALI searches11 failed to find matches in the database of known structures. Residues 1,018–1,045 and 1,084–1,088 of ACTR are unstructured in the complex.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:29:48.120Z"}}],"released":"2016_10","uniref100":"UniRef100_Q9Y6Q9","date":"2016-09-08T15:50:30.000Z","acc":"Q9Y6Q9","name":"Nuclear receptor coactivator 3","length":1424,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI000012FE45","genes":[{"name":{"value":"NCOA3"},"synonyms":[{"value":"AIB1"},{"value":"BHLHE42"},{"value":"RAC3"},{"value":"TRAM1"}]}],"alphafold_very_low_content":0.7071629213483146,"disorder_content":0.04985955056179775,"disprot_consensus":{"full":[{"start":1018,"end":1044,"type":"D"},{"start":1045,"end":1085,"type":"T"},{"start":1086,"end":1088,"type":"D"}],"Structural state":[{"start":1018,"end":1088,"type":"D"}],"Structural transition":[{"start":1045,"end":1085,"type":"T"}],"Molecular function":[{"start":1018,"end":1088,"type":"F"}]}},{"features":{"pfam":[{"id":"PF13499","name":"EF-hand domain pair","start":12,"end":73},{"id":"PF13499","name":"EF-hand domain pair","start":83,"end":147}],"gene3D":[{"start":1,"end":75,"id":"1.10.238.10","name":"EF-hand"},{"start":124,"end":149,"id":"1.10.238.10","name":"EF-hand"},{"start":76,"end":123,"id":"1.10.238.10","name":"EF-hand"}]},"uniref50":"UniRef50_P62152","sequence":"MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVTMMTSK","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_P62152","disprot_id":"DP00344","ncbi_taxon_id":7227,"regions_counter":3,"creator":"thorvath","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":83,"region_id":"DP00344r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Determination of the individual roles of the linker residues in the interdomain motions of calmodulin using NMR chemical shifts. <i> Kukic P, Camilloni C, Cavalli A, Vendruscolo M. </i> J Mol Biol, 2014","statement":[{"text":"We find that the conformational fluctuations of the interdomain linker, which are largely responsible for the overall interdomain motions of CaM, can be well described by exploiting the information provided by chemical shifts","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"thorvath","start":74,"term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"24530797","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P62152","date":"2016-09-06T11:51:25.000Z","acc":"P62152","name":"Calmodulin","length":149,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI000011083A","genes":[{"name":{"value":"Cam"},"orfNames":[{"value":"CG8472"}]}],"alphafold_very_low_content":0.020134228187919462,"disorder_content":0.06711409395973154,"disprot_consensus":{"full":[{"start":74,"end":83,"type":"D"}],"Structural state":[{"start":74,"end":83,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":715,"end":750},{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":751,"end":785},{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":791,"end":806},{"id":"PF02382","name":"N-terminal domain in RTX protein","start":283,"end":589},{"id":"PF08339","name":"RTX C-terminal domain","start":808,"end":936}],"gene3D":[{"start":716,"end":883,"id":"2.150.10.10","name":"Serralysin-like metalloprotease, C-terminal"}]},"uniref50":"UniRef50_Q9ETX2","sequence":"MGTRLTTLSNGLKNTLTATKSGLHKAGQSLTQAGSSLKTGAKKIILYIPQNYQYDTEQGNGLQDLVKAAEELGIEVQREERNNIATAQTSLGTIQTAIGLTERGIVLSAPQIDKLLQKTKAGQALGSAESIVQNANKAKTVLSGIQSILGSVLAGMDLDEALQNNSNQHALAKAGLELTNSLIENIANSVKTLDEFGEQISQFGSKLQNIKGLGTLGDKLKNIGGLDKAGLGLDVISGLLSGATAALVLADKNASTAKKVGAGFELANQVVGNITKAVSSYILAQRVAAGLSSTGPVAALIASTVSLAISPLAFAGIADKFNHAKSLESYAERFKKLGYDGDNLLAEYQRGTGTIDASVTAINTALAAIAGGVSAAAAGSVIASPIALLVSGITGVISTILQYSKQAMFEHVANKIHNKIVEWEKNNHGKNYFENGYDARYLANLQDNMKFLLNLNKELQAERVIAITQQQWDNNIGDLAGISRLGEKVLSGKAYVDAFEEGKHIKADKLVQLDSANGIIDVSNSGKAKTQHILFRTPLLTPGTEHRERVQTGKYEYITKLNINRVDSWKITDGAASSTFDLTNVVQRIGIELDNAGNVTKTKETKIIAKLGEGDDNVFVGSGTTEIDGGEGYDRVHYSRGNYGALTIDATKETEQGSYTVNRFVETGKALHEVTSTHTALVGNREEKIEYRHSNNQHHAGYYTKDTLKAVEEIIGTSHNDIFKGSKFNDAFNGGDGVDTIDGNDGNDRLFGGKGDDILDGGNGDDFIDGGKGNDLLHGGKGDDIFVHRKGDGNDIITDSDGNDKLSFSDSNLKDLTFEKVKHNLVITNSKKEKVTIQNWFREADFAKEVPNYKATKDEKIEEIIGQNGERITSKQVDDLIAKGNGKITQDELSKVVDNYELLKHSKNVTNSLDKLISSVSAFTSSNDSRNVLVAPTSMLDQSLSSLQFARAA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Pasteurellales","Pasteurellaceae","Mannheimia"],"uniref90":"UniRef90_P16535","disprot_id":"DP00345","dataset":["Unicellular toxins and antitoxins","Bacterial virulence-related proteins"],"ncbi_taxon_id":75985,"regions_counter":6,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":953,"region_id":"DP00345r001","reference_html":"Secretion and circular dichroism analysis of the C-terminal signal peptides of HlyA and LktA. <i> Zhang F, Yin Y, Arrowsmith CH, Ling V. </i> Biochemistry, 1995","ec_id":"ECO:0006204","version":4,"term_id":"IDPO:0000002","curator_id":"rpancsa","start":884,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"In aqueous solution, the CD spectra of  both HlyA and LktA reflect a predominantly  random conformation (Figures 6 and 7). There is no observed structural change between 23 and 37 “C. A broad range of pH changes (pH 4.5-8) do not affect the structure of  either HlyA or LktA signal  peptide.","type":"Results"},{"text":"The C-terminal signal peptides of HlyA and LktA exhibit similar biophysical behaviors. In aqueous solution, both molecules are mainly in a random conformation.","type":"Discussion"}],"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:42:59.472Z","curator_name":"Bálint Mészáros"},"released":"2022_03","reference_id":"7703231","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00345r002","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:43:01.757Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":953,"term_id":"IDPO:0000011","start":884,"version":3,"statement":[{"text":"Finally, we tested the conformational behaviors of HlyA and LktA  signal peptides in phospholipid vesicles,  a  lipid bilayer environment which more closely resembles a membrane  compared to the  other  reagents  tested.   Uncharged phospholipids  PC  could not induce an ordered  structure (Figure 7G,H), while  the  anionic  phospholipids  (PS,  PG) induced formation of a-helices in both peptides (Figure 7C- F).","type":"Results"},{"text":"In aqueous solution, both molecules are mainly in a random conformation. Membrane mimetic environments such as TFE/H20, SDS micelles, and negatively charged phospholipid vesicles induce formation of a-helices.","type":"Discussion"}],"term_name":"disorder to order","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"7703231","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural transition","ec_id":"ECO:0006204","curator_id":"rpancsa","reference_html":"Secretion and circular dichroism analysis of the C-terminal signal peptides of HlyA and LktA. <i> Zhang F, Yin Y, Arrowsmith CH, Ling V. </i> Biochemistry, 1995","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00345r003","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:43:02.620Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":953,"term_id":"GO:0008289","start":884,"version":4,"statement":[{"text":"Finally, we tested the conformational behaviors of HlyA and LktA  signal peptides in phospholipid vesicles,  a  lipid bilayer environment which more closely resembles a membrane  compared to the  other  reagents  tested.   Uncharged phospholipids  PC  could not induce an ordered structure (Figure 7G,H), while  the  anionic  phospholipids  (PS,  PG) induced formation of a-helices in both peptides (Figure 7C- F).","type":"Results"}],"term_name":"lipid binding","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"7703231","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006204","curator_id":"rpancsa","reference_html":"Secretion and circular dichroism analysis of the C-terminal signal peptides of HlyA and LktA. <i> Zhang F, Yin Y, Arrowsmith CH, Ling V. </i> Biochemistry, 1995","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00345r004","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:43:04.860Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":953,"term_id":"GO:0051179","start":884,"version":4,"statement":[{"text":"This confirms that these  short  sequences  contain  information sufficient  for  recognition and transport, and  that no other sequences  are  required.","type":"Discussion"},{"text":"In order to test the secretion of these signal peptides, C-HA61 or C-LA70 were coexpressed with the transporter proteins HlyB and HlyD in JM83 cells. Cell media were taken at different points during the growth curve. The secreted signal peptides can be detected by Western blot analysis using C494 antibody. As shown in Figure 3 lanes 3, 4, 7, and 8, signal sequence peptides of HlyA and LktA were found in the medium. This secretion requires the presence of both HlyB and HlyD.","type":"Results"},{"text":"Thus, these data show that the signal sequence bearing peptides can be transported by the HlyB/D transporter in a specific manner.","type":"Results"}],"term_name":"localization","ec_name":"qualitative western immunoblotting evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"7703231","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Biological process","ec_id":"ECO:0000279","curator_id":"rpancsa","reference_html":"Secretion and circular dichroism analysis of the C-terminal signal peptides of HlyA and LktA. <i> Zhang F, Yin Y, Arrowsmith CH, Ling V. </i> Biochemistry, 1995","ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"region_id":"DP00345r006","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:43:00.699Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":953,"term_id":"IDPO:0000002","start":884,"version":2,"statement":[{"text":"Signal peptides were labelled with 15N to facilitate the NMR analysis. A striking feature of the NMR spectra of both is the poor dispersion in the 1H nuclei, possibly indicating the presence of a significant amount of random-coil or unfolded protein conformation [27]. The 15N-nuclei, on the other hand, have reasonable chemical shift dispersion as has been shown previously for this nucleus in unfolded proteins [28,29].","type":"Results"},{"text":"Both peptides contained two regions with NMR parameters that are characteristic of a-helices (Fig. 1). Typical helical NOEs were observed for residues 31-43 and 56-66 of LktA.","type":"Results"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"7789505","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"rpancsa","reference_html":"Structural analysis and comparison of the C-terminal transport signal domains of hemolysin A and leukotoxin A. <i> Yin Y, Zhang F, Ling V, Arrowsmith CH. </i> FEBS Lett, 1995","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P16535","date":"2016-09-03T18:36:42.000Z","acc":"P16535","name":"Leukotoxin","length":953,"organism":"Mannheimia haemolytica","UniParc":"UPI0000000ECE","genes":[{"name":{"value":"lktA"}}],"alphafold_very_low_content":0.3357817418677859,"disorder_content":0.07345225603357818,"disprot_consensus":{"full":[{"start":884,"end":953,"type":"T"}],"Structural state":[{"start":884,"end":953,"type":"D"}],"Structural transition":[{"start":884,"end":953,"type":"T"}],"Molecular function":[{"start":884,"end":953,"type":"F"}],"Biological process":[{"start":884,"end":953,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00135","name":"Carboxylesterase family","start":43,"end":601}]},"uniref50":"UniRef50_P07140","sequence":"MAISCRQSRVLPMSLPLPLTIPLPLVLVLSLHLSGVCGVIDRLVVQTSSGPVRGRSVTVQGREVHVYTGIPYAKPPVEDLRFRKPVPAEPWHGVLDATRLSATCVQERYEYFPGFSGEEIWNPNTNVSEDCLYINVWAPAKARLRHGRGANGGEHPNGKQADTDHLIHNGNPQNTTNGLPILIWIYGGGFMTGSATLDIYNADIMAAVGNVIVASFQYRVGAFGFLHLAPEMPSEFAEEAPGNVGLWDQALAIRWLKDNAHAFGGNPEWMTLFGESAGSSSVNAQLMSPVTRGLVKRGMMQSGTMNAPWSHMTSEKAVEIGKALINDCNCNASMLKTNPAHVMSCMRSVDAKTISVQQWNSYSGILSFPSAPTIDGAFLPADPMTLMKTADLKDYDILMGNVRDEGTYFLLYDFIDYFDKDDATALPRDKYLEIMNNIFGKATQAEREAIIFQYTSWEGNPGYQNQQQIGRAVGDHFFTCPTNEYAQALAERGASVHYYYFTHRTSTSLWGEWMGVLHGDEIEYFFGQPLNNSLQYRPVERELGKRMLSAVIEFAKTGNPAQDGEEWPNFSKEDPVYYIFSTDDKIEKLARGPLAARCSFWNDYLPKVRSWAGTCDGDSGSASISPRLQLLGIAALIYICAALRTKRVF","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_P07140","disprot_id":"DP00346","ncbi_taxon_id":7227,"regions_counter":2,"creator":"slonghi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":173,"region_id":"DP00346r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Three-dimensional structures of Drosophila melanogaster acetylcholinesterase and of its complexes with two potent inhibitors. <i> Harel M, Kryger G, Rosenberry TL, Mallender WD, Lewis T, Fletcher RJ, Guss JM, Silman I, Sussman JL. </i> Protein Sci, 2000","term_id":"IDPO:0000002","curator_id":"slonghi","start":142,"term_ontology":"IDPO","curator_name":"Sonia Longhi","reference_id":"10892800","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1QON"}],"term_name":"disorder","curator_orcid":"0000-0002-6829-6771","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":623,"region_id":"DP00346r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Three-dimensional structures of Drosophila melanogaster acetylcholinesterase and of its complexes with two potent inhibitors. <i> Harel M, Kryger G, Rosenberry TL, Mallender WD, Lewis T, Fletcher RJ, Guss JM, Silman I, Sussman JL. </i> Protein Sci, 2000","term_id":"IDPO:0000002","curator_id":"slonghi","start":613,"term_ontology":"IDPO","curator_name":"Sonia Longhi","reference_id":"10892800","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1QON"}],"term_name":"disorder","curator_orcid":"0000-0002-6829-6771","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P07140","date":"2016-09-08T12:48:03.000Z","acc":"P07140","name":"Acetylcholinesterase","length":649,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI0000125213","genes":[{"name":{"value":"Ace"},"orfNames":[{"value":"CG17907"}]}],"alphafold_very_low_content":0.14329738058551617,"disorder_content":0.0662557781201849,"disprot_consensus":{"full":[{"start":142,"end":173,"type":"D"},{"start":613,"end":623,"type":"D"}],"Structural state":[{"start":142,"end":173,"type":"D"},{"start":613,"end":623,"type":"D"}]}},{"features":{"pfam":[{"id":"PF04868","name":"Retinal cGMP phosphodiesterase, gamma subunit","start":11,"end":87}],"gene3D":[{"start":1,"end":86,"id":"4.10.1120.10","name":"Retinal cGMP phosphodiesterase, gamma subunit"}]},"uniref50":"UniRef50_P04972","sequence":"MNLEPPKAEIRSATRVMGGPVTPRKGPPKFKQRQTRQFKSKPPKKGVQGFGDDIPGMEGLGTDITVICPWEAFNHLELHELAQYGII","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P04972","disprot_id":"DP00347","ncbi_taxon_id":9913,"regions_counter":19,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":87,"region_id":"DP00347r001","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Effect of zinc and temperature on the conformation of the gamma subunit of retinal phosphodiesterase: a natively unfolded protein. <i> Uversky VN, Permyakov SE, Zagranichny VE, Rodionov IL, Fink AL, Cherskaya AM, Wasserman LA, Permyakov EA. </i> J Proteome Res, 2002","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12643535","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":87,"term_name":"ion binding","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"12643535","version":3,"reference_html":"Effect of zinc and temperature on the conformation of the gamma subunit of retinal phosphodiesterase: a natively unfolded protein. <i> Uversky VN, Permyakov SE, Zagranichny VE, Rodionov IL, Fink AL, Cherskaya AM, Wasserman LA, Permyakov EA. </i> J Proteome Res, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0043167","ec_id":"ECO:0007680","region_id":"DP00347r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":87,"region_id":"DP00347r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Effect of zinc and temperature on the conformation of the gamma subunit of retinal phosphodiesterase: a natively unfolded protein. <i> Uversky VN, Permyakov SE, Zagranichny VE, Rodionov IL, Fink AL, Cherskaya AM, Wasserman LA, Permyakov EA. </i> J Proteome Res, 2002","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12643535","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":87,"term_name":"disorder to pre-molten globule","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12643535","version":2,"reference_html":"Effect of zinc and temperature on the conformation of the gamma subunit of retinal phosphodiesterase: a natively unfolded protein. <i> Uversky VN, Permyakov SE, Zagranichny VE, Rodionov IL, Fink AL, Cherskaya AM, Wasserman LA, Permyakov EA. </i> J Proteome Res, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000019","ec_id":"ECO:0006204","region_id":"DP00347r004","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":87,"term_name":"ion binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"12643535","version":3,"reference_html":"Effect of zinc and temperature on the conformation of the gamma subunit of retinal phosphodiesterase: a natively unfolded protein. <i> Uversky VN, Permyakov SE, Zagranichny VE, Rodionov IL, Fink AL, Cherskaya AM, Wasserman LA, Permyakov EA. </i> J Proteome Res, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0043167","ec_id":"ECO:0006204","region_id":"DP00347r005","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":87,"region_id":"DP00347r006","released":"2022_03","ec_id":"ECO:0006206","reference_html":"Effect of zinc and temperature on the conformation of the gamma subunit of retinal phosphodiesterase: a natively unfolded protein. <i> Uversky VN, Permyakov SE, Zagranichny VE, Rodionov IL, Fink AL, Cherskaya AM, Wasserman LA, Permyakov EA. </i> J Proteome Res, 2002","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12643535","version":2,"ec_name":"near-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":87,"term_name":"ion binding","start":1,"ec_name":"near-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"12643535","version":3,"reference_html":"Effect of zinc and temperature on the conformation of the gamma subunit of retinal phosphodiesterase: a natively unfolded protein. <i> Uversky VN, Permyakov SE, Zagranichny VE, Rodionov IL, Fink AL, Cherskaya AM, Wasserman LA, Permyakov EA. </i> J Proteome Res, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0043167","ec_id":"ECO:0006206","region_id":"DP00347r007","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":87,"region_id":"DP00347r008","released":"2022_03","ec_id":"ECO:0001249","reference_html":"Effect of zinc and temperature on the conformation of the gamma subunit of retinal phosphodiesterase: a natively unfolded protein. <i> Uversky VN, Permyakov SE, Zagranichny VE, Rodionov IL, Fink AL, Cherskaya AM, Wasserman LA, Permyakov EA. </i> J Proteome Res, 2002","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12643535","version":2,"ec_name":"fluorescence evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":87,"term_name":"ion binding","start":1,"ec_name":"fluorescence evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"12643535","version":3,"reference_html":"Effect of zinc and temperature on the conformation of the gamma subunit of retinal phosphodiesterase: a natively unfolded protein. <i> Uversky VN, Permyakov SE, Zagranichny VE, Rodionov IL, Fink AL, Cherskaya AM, Wasserman LA, Permyakov EA. </i> J Proteome Res, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0043167","ec_id":"ECO:0001249","region_id":"DP00347r009","curator_orcid":"0000-0001-9377-482X","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":87,"region_id":"DP00347r010","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Intrinsically disordered gamma-subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structure. <i> Song J, Guo LW, Muradov H, Artemyev NO, Ruoho AE, Markley JL. </i> Proc Natl Acad Sci U S A, 2008","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"18230733","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2JU4"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":87,"term_name":"molecular adaptor activity","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"18230733","version":3,"reference_html":"Intrinsically disordered gamma-subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structure. <i> Song J, Guo LW, Muradov H, Artemyev NO, Ruoho AE, Markley JL. </i> Proc Natl Acad Sci U S A, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP00347r011","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":87,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"18230733","version":3,"reference_html":"Intrinsically disordered gamma-subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structure. <i> Song J, Guo LW, Muradov H, Artemyev NO, Ruoho AE, Markley JL. </i> Proc Natl Acad Sci U S A, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00347r012","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":21,"region_id":"DP00347r013","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Intrinsically disordered gamma-subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structure. <i> Song J, Guo LW, Muradov H, Artemyev NO, Ruoho AE, Markley JL. </i> Proc Natl Acad Sci U S A, 2008","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"18230733","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2JU4"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":21,"term_name":"molecular adaptor activity","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"18230733","version":3,"reference_html":"Intrinsically disordered gamma-subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structure. <i> Song J, Guo LW, Muradov H, Artemyev NO, Ruoho AE, Markley JL. </i> Proc Natl Acad Sci U S A, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP00347r014","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":21,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"18230733","version":3,"reference_html":"Intrinsically disordered gamma-subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structure. <i> Song J, Guo LW, Muradov H, Artemyev NO, Ruoho AE, Markley JL. </i> Proc Natl Acad Sci U S A, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00347r015","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":78,"region_id":"DP00347r016","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Intrinsically disordered gamma-subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structure. <i> Song J, Guo LW, Muradov H, Artemyev NO, Ruoho AE, Markley JL. </i> Proc Natl Acad Sci U S A, 2008","term_id":"IDPO:0000002","curator_id":"mnecci","start":46,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"18230733","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2JU4"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":78,"term_name":"molecular adaptor activity","start":46,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"18230733","version":3,"reference_html":"Intrinsically disordered gamma-subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structure. <i> Song J, Guo LW, Muradov H, Artemyev NO, Ruoho AE, Markley JL. </i> Proc Natl Acad Sci U S A, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP00347r017","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":78,"term_name":"disorder to order","start":46,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"18230733","version":2,"reference_html":"Intrinsically disordered gamma-subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structure. <i> Song J, Guo LW, Muradov H, Artemyev NO, Ruoho AE, Markley JL. </i> Proc Natl Acad Sci U S A, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00347r018","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":78,"term_name":"protein binding","start":46,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"18230733","version":3,"reference_html":"Intrinsically disordered gamma-subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structure. <i> Song J, Guo LW, Muradov H, Artemyev NO, Ruoho AE, Markley JL. </i> Proc Natl Acad Sci U S A, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00347r019","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P04972","date":"2016-09-16T11:51:56.000Z","acc":"P04972","name":"Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma","length":87,"organism":"Bos taurus","dataset":[],"UniParc":"UPI0000127C37","genes":[{"name":{"value":"PDE6G"},"synonyms":[{"value":"PDEG"}]}],"alphafold_very_low_content":0.08045977011494253,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":87,"type":"T"}],"Structural state":[{"start":1,"end":87,"type":"D"}],"Molecular function":[{"start":1,"end":87,"type":"F"}],"Structural transition":[{"start":1,"end":87,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00439","name":"Bromodomain","start":1105,"end":1179},{"id":"PF00569","name":"Zinc finger, ZZ type","start":1703,"end":1743},{"id":"PF02135","name":"TAZ zinc finger","start":353,"end":429},{"id":"PF02135","name":"TAZ zinc finger","start":1773,"end":1844},{"id":"PF02172","name":"KIX domain","start":587,"end":666},{"id":"PF06001","name":"CREB-binding protein/p300, atypical RING domain","start":1193,"end":1232},{"id":"PF09030","name":"Creb binding","start":2016,"end":2114},{"id":"PF23570","name":"Histone acetyltransferase p300-like, PHD domain","start":1277,"end":1315},{"id":"PF29847","name":"Histone acetyltransferase domain KAT3","start":1343,"end":1650}],"gene3D":[{"start":1274,"end":1319,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":2059,"end":2117,"id":"1.10.1630.10","name":"Nuclear receptor coactivator, CREB-bp-like, interlocking domain"},{"start":340,"end":439,"id":"1.20.1020.10","name":"TAZ domain"},{"start":1762,"end":1873,"id":"1.20.1020.10","name":"TAZ domain"},{"start":1049,"end":1198,"id":"1.20.920.10","name":"Bromodomain-like"},{"start":1207,"end":1273,"id":"2.10.110.40","name":"2.10.110.40"},{"start":586,"end":672,"id":"1.10.246.20","name":"Coactivator CBP, KIX domain"},{"start":1700,"end":1752,"id":"3.30.60.90","name":"3.30.60.90"}]},"uniref50":"UniRef50_P45481","sequence":"MAENLLDGPPNPKRAKLSSPGFSANDNTDFGSLFDLENDLPDELIPNGELSLLNSGNLVPDAASKHKQLSELLRGGSGSSINPGIGNVSASSPVQQGLGGQAQGQPNSTNMASLGAMGKSPLNQGDSSTPNLPKQAASTSGPTPPASQALNPQAQKQVGLVTSSPATSQTGPGICMNANFNQTHPGLLNSNSGHSLMNQAQQGQAQVMNGSLGAAGRGRGAGMPYPAPAMQGATSSVLAETLTQVSPQMAGHAGLNTAQAGGMTKMGMTGTTSPFGQPFSQTGGQQMGATGVNPQLASKQSMVNSLPAFPTDIKNTSVTTVPNMSQLQTSVGIVPTQAIATGPTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWKNCTRHDCPVCLPLKNASDKRNQQTILGSPASGIQNTIGSVGAGQQNATSLSNPNPIDPSSMQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPPAHQQMRTLNALGNNPMSIPAGGITTDQQPPNLISESALPTSLGATNPLMNDGSNSGNIGSLSTIPTAAPPSSTGVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELEEKRRSRLHKQGILGNQPALPASGAQPPVIPPAQSVRPPNGPLPLPVNRMQVSQGMNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMASVPGMAISPSRMPQPPNMMGTHANNIMAQAPTQNQFLPQNQFPSSSGAMSVNSVGMGQPAAQAGVSQGQVPGAALPNPLNMLAPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHPTAPGMTPPQPAAPTQPSTPVSSGQTPTPTPGSVPSAAQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHTQPPGTPLSQAAASIDNRVPTPSSVTSAETSSQQPGPDVPMLEMKTEVQTDDAEPEPTESKGEPRSEMMEEDLQGSSQVKEETDTTEQKSEPMEVEEKKPEVKVEAKEEEENSSNDTASQSTSPSQPRKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQNRYHFCEKCFTEIQGENVTLGDDPSQPQTTISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLKKTGRPRKENKFSAKRLQTTRLGNHLEDRVNKFLRRQNHPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGEMSESFPYRTKALFAFEEIDGVDVCFFGMHVQNTALIAPHQIQGRVYISYLDSIHFFRPRCLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAFAERIINDYKDIFKQANEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKKEESTAASETPEGSQGDSKNAKKKNNKKTNKNKSSISRANKKKPSMPNVSNDLSQKLYATMEKHKEVFFVIHLHAGPVISTQPPIVDPDPLLSCDLMDGRDAFLTLARDKHWEFSSLRRSKWSTLCMLVELHTQGQDRFVYTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHTHKMVKWGLGLDDEGSSQGEPQSKSPQESRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPVCKQLIALCCYHAKHCQENKCPVPFCLNIKHKLRQQQIQHRLQQAQLMRRRMATMNTRNVPQQSLPSPTSAPPGTPTQQPSTPQTPQPPAQPQPSPVNMSPAGFPNVARTQPPTIVSAGKPTNQVPAPPPPAQPPPAAVEAARQIEREAQQQQHLYRANINNGMPPGRAGMGTPGSQMTPVGLNVPRPNQVSGPVMSSMPPGQWQQAPIPQQQPMPGMPRPVMSMQAQAAVAGPRMPNVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYVANQPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPPQPAMGGLNPQGQALNIMNPGHNPNMTNMNPQYREMVRRQLLQHQQQQQQQQQQQQQQQNSASLAGGMAGHSQFQQPQGPGGYAPAMQQQRMQQHLPIQGSSMGQMAAPMGQLGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLSNQVRSPAPVQSPRPQSQPPHSSPSPRIQPQPSPHHVSPQTGSPHPGLAVTMASSMDQGHLGNPEQSAMLPQLNTPNRSALSSELSLVGDTTGDTLEKFVEGL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P45481","disprot_id":"DP00348","ncbi_taxon_id":10090,"regions_counter":20,"creator":"rpancsa","regions":[{"term_namespace":"Molecular function","ec_ontology":"ECO","end":2152,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. <i> Demarest SJ, Martinez-Yamout M, Chung J, Chen H, Xu W, Dyson HJ, Evans RM, Wright PE. </i> Nature, 2002","term_id":"GO:0060090","curator_id":"smribeiro","start":2113,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"11823864","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00348r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":2152,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. <i> Demarest SJ, Martinez-Yamout M, Chung J, Chen H, Xu W, Dyson HJ, Evans RM, Wright PE. </i> Nature, 2002","term_id":"GO:0005515","curator_id":"smribeiro","start":2113,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"11823864","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00348r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":2117,"region_id":"DP00348r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. <i> Demarest SJ, Martinez-Yamout M, Chung J, Chen H, Xu W, Dyson HJ, Evans RM, Wright PE. </i> Nature, 2002","term_id":"IDPO:0000002","curator_id":"smribeiro","start":2059,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1KBH"}],"reference_id":"11823864","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":2117,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. <i> Demarest SJ, Martinez-Yamout M, Chung J, Chen H, Xu W, Dyson HJ, Evans RM, Wright PE. </i> Nature, 2002","term_id":"GO:0060090","curator_id":"smribeiro","start":2059,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"11823864","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00348r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":2117,"term_name":"molten globule to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. <i> Demarest SJ, Martinez-Yamout M, Chung J, Chen H, Xu W, Dyson HJ, Evans RM, Wright PE. </i> Nature, 2002","term_id":"IDPO:0000012","curator_id":"smribeiro","start":2059,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"11823864","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00348r006","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":2117,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators. <i> Demarest SJ, Martinez-Yamout M, Chung J, Chen H, Xu W, Dyson HJ, Evans RM, Wright PE. </i> Nature, 2002","term_id":"GO:0005515","curator_id":"smribeiro","start":2059,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"11823864","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00348r007","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":2118,"region_id":"DP00348r008","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP. <i> Kjaergaard M, Teilum K, Poulsen FM. </i> Proc Natl Acad Sci U S A, 2010","term_id":"IDPO:0000002","curator_id":"smribeiro","start":2059,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2KKJ"}],"reference_id":"20616042","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":2118,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP. <i> Kjaergaard M, Teilum K, Poulsen FM. </i> Proc Natl Acad Sci U S A, 2010","term_id":"GO:0060090","curator_id":"smribeiro","start":2059,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"20616042","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00348r009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":2118,"term_name":"molten globule to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP. <i> Kjaergaard M, Teilum K, Poulsen FM. </i> Proc Natl Acad Sci U S A, 2010","term_id":"IDPO:0000012","curator_id":"smribeiro","start":2059,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"20616042","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00348r010","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":2118,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP. <i> Kjaergaard M, Teilum K, Poulsen FM. </i> Proc Natl Acad Sci U S A, 2010","term_id":"GO:0005515","curator_id":"smribeiro","start":2059,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"20616042","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00348r011","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":2118,"region_id":"DP00348r012","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP. <i> Kjaergaard M, Teilum K, Poulsen FM. </i> Proc Natl Acad Sci U S A, 2010","term_id":"IDPO:0000003","curator_id":"smribeiro","start":2059,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"molten globule","reference_id":"20616042","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":2118,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP. <i> Kjaergaard M, Teilum K, Poulsen FM. </i> Proc Natl Acad Sci U S A, 2010","term_id":"GO:0060090","curator_id":"smribeiro","start":2059,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"20616042","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00348r013","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":2118,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP. <i> Kjaergaard M, Teilum K, Poulsen FM. </i> Proc Natl Acad Sci U S A, 2010","term_id":"GO:0005515","curator_id":"smribeiro","start":2059,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"20616042","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00348r014","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":2118,"region_id":"DP00348r015","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP. <i> Kjaergaard M, Teilum K, Poulsen FM. </i> Proc Natl Acad Sci U S A, 2010","term_id":"IDPO:0000003","curator_id":"smribeiro","start":2059,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"molten globule","reference_id":"20616042","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":2118,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","reference_html":"Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP. <i> Kjaergaard M, Teilum K, Poulsen FM. </i> Proc Natl Acad Sci U S A, 2010","term_id":"GO:0060090","curator_id":"smribeiro","start":2059,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"20616042","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","region_id":"DP00348r016","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":2118,"term_name":"protein binding","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","reference_html":"Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP. <i> Kjaergaard M, Teilum K, Poulsen FM. </i> Proc Natl Acad Sci U S A, 2010","term_id":"GO:0005515","curator_id":"smribeiro","start":2059,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"20616042","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","region_id":"DP00348r017","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":2117,"region_id":"DP00348r018","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A folded excited state of ligand-free nuclear coactivator binding domain (NCBD) underlies plasticity in ligand recognition. <i> Kjaergaard M, Andersen L, Nielsen LD, Teilum K. </i> Biochemistry, 2013","term_id":"IDPO:0000003","curator_id":"smribeiro","start":2059,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"molten globule","reference_id":"23373423","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":2117,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"A folded excited state of ligand-free nuclear coactivator binding domain (NCBD) underlies plasticity in ligand recognition. <i> Kjaergaard M, Andersen L, Nielsen LD, Teilum K. </i> Biochemistry, 2013","term_id":"GO:0060090","curator_id":"smribeiro","start":2059,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"23373423","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00348r019","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":2117,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"A folded excited state of ligand-free nuclear coactivator binding domain (NCBD) underlies plasticity in ligand recognition. <i> Kjaergaard M, Andersen L, Nielsen LD, Teilum K. </i> Biochemistry, 2013","term_id":"GO:0005515","curator_id":"smribeiro","start":2059,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"23373423","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00348r020","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P45481","date":"2016-09-12T12:17:04.000Z","acc":"P45481","name":"CREB-binding protein","length":2441,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00003E0205","genes":[{"name":{"value":"Crebbp"},"synonyms":[{"value":"Cbp"}]}],"alphafold_very_low_content":0.6132732486685785,"disorder_content":0.024580090126997134,"disprot_consensus":{"full":[{"start":2059,"end":2118,"type":"T"},{"start":2119,"end":2152,"type":"F"}],"Structural state":[{"start":2059,"end":2118,"type":"D"}],"Molecular function":[{"start":2059,"end":2152,"type":"F"}],"Structural transition":[{"start":2059,"end":2118,"type":"T"}]}},{"features":{"pfam":[{"id":"PF02237","name":"Biotin protein ligase C terminal domain","start":271,"end":317},{"id":"PF03099","name":"Biotin/lipoate A/B protein ligase family","start":84,"end":208},{"id":"PF08279","name":"HTH domain","start":9,"end":58}],"gene3D":[{"start":1,"end":64,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"start":65,"end":270,"id":"3.30.930.10","name":"Bira Bifunctional Protein; Domain 2"},{"start":271,"end":313,"id":"2.30.30.100","name":"2.30.30.100"}]},"uniref50":"UniRef50_P06709","sequence":"MKDNTVPLKLIALLANGEFHSGEQLGETLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIQLLNAKQILGQLDGGSVAVLPVIDSTNQYLLDRIGELKSGDACIAEYQQAGRGRRGRKWFSPFGANLYLSMFWRLEQGPAAAIGLSLVIGIVMAEVLRKLGADKVRVKWPNDLYLQDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEESVVNQGWITLQEAGINLDRNTLAAMLIRELRAALELFEQEGLAPYLSRWEKLDNFINRPVKLIIGDKEIFGISRGIDKQGALLLEQDGIIKPWMGGEISLRSAEK","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P06709","disprot_id":"DP00349","ncbi_taxon_id":83333,"regions_counter":12,"creator":"maspromonte","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":223,"region_id":"DP00349r009","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. <i> Wilson KP, Shewchuk LM, Brennan RG, Otsuka AJ, Matthews BW. </i> Proc Natl Acad Sci U S A, 1992","term_id":"IDPO:0000002","curator_id":"maspromonte","start":212,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"1409631","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":223,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. <i> Wilson KP, Shewchuk LM, Brennan RG, Otsuka AJ, Matthews BW. </i> Proc Natl Acad Sci U S A, 1992","term_id":"GO:0003676","curator_id":"maspromonte","start":212,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"1409631","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00349r010","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":234,"region_id":"DP00349r011","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Evidence for distinct ligand-bound conformational states of the multifunctional Escherichia coli repressor of biotin biosynthesis. <i> Xu Y, Nenortas E, Beckett D. </i> Biochemistry, 1995","term_id":"IDPO:0000002","curator_id":"maspromonte","start":212,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"8527435","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":234,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Evidence for distinct ligand-bound conformational states of the multifunctional Escherichia coli repressor of biotin biosynthesis. <i> Xu Y, Nenortas E, Beckett D. </i> Biochemistry, 1995","term_id":"GO:0003676","curator_id":"maspromonte","start":212,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"8527435","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00349r012","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P06709","date":"2016-09-04T12:19:22.000Z","acc":"P06709","name":"Bifunctional ligase/repressor BirA","length":321,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI00001108FE","genes":[{"name":{"value":"birA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00978","url":"https://hamap.expasy.org/unirule/MF_00978"}}]},"synonyms":[{"value":"bioR"},{"value":"dhbB"}],"olnNames":[{"value":"b3973"},{"value":"JW3941"}]}],"alphafold_very_low_content":0,"disorder_content":0.07165109034267912,"disprot_consensus":{"full":[{"start":212,"end":234,"type":"D"}],"Structural state":[{"start":212,"end":234,"type":"D"}],"Molecular function":[{"start":212,"end":234,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01584","name":"CheW-like domain","start":12,"end":144}],"gene3D":[{"start":29,"end":142,"id":"2.40.50.180","name":"CheA-289, Domain 4"},{"start":14,"end":136,"id":"2.30.30.40","name":"SH3 Domains"}]},"uniref50":"UniRef50_Q56311","sequence":"MKTLADALKEFEVLSFEIDEQALAFDVDNIEMVIEKSDITPVPKSRHFVEGVINLRGRIIPVVNLAKILGISFDEQKMKSIIVARTKDVEVGFLVDRVLGVLRITENQLDLTNVSDKFGKKSKGLVKTDGRLIIYLDIDKIIEEITVKEGV","taxonomy":["Bacteria","Thermotogae","Thermotogales","Thermotogaceae","Thermotoga"],"uniref90":"UniRef90_Q56311","disprot_id":"DP00350","ncbi_taxon_id":243274,"regions_counter":2,"creator":"ahatos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":49,"region_id":"DP00350r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The solution structure and interactions of CheW from Thermotoga maritima. <i> Griswold IJ, Zhou H, Matison M, Swanson RV, McIntosh LP, Simon MI, Dahlquist FW. </i> Nat Struct Biol, 2002","term_id":"IDPO:0000002","curator_id":"ahatos","start":37,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1K0S"}],"reference_id":"11799399","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":122,"region_id":"DP00350r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The solution structure and interactions of CheW from Thermotoga maritima. <i> Griswold IJ, Zhou H, Matison M, Swanson RV, McIntosh LP, Simon MI, Dahlquist FW. </i> Nat Struct Biol, 2002","term_id":"IDPO:0000002","curator_id":"ahatos","start":109,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1K0S"}],"reference_id":"11799399","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q56311","date":"2016-09-07T10:26:12.000Z","acc":"Q56311","name":"Chemotaxis protein CheW","length":151,"organism":"Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","dataset":[],"UniParc":"UPI000011323B","genes":[{"name":{"value":"cheW"},"olnNames":[{"value":"TM_0701"}]}],"alphafold_very_low_content":0.039735099337748346,"disorder_content":0.17880794701986755,"disprot_consensus":{"full":[{"start":37,"end":49,"type":"D"},{"start":109,"end":122,"type":"D"}],"Structural state":[{"start":37,"end":49,"type":"D"},{"start":109,"end":122,"type":"D"}]}},{"features":{"pfam":[{"id":"PF10409","name":"C2 domain of PTEN tumour-suppressor protein","start":223,"end":361}],"gene3D":[{"start":779,"end":907,"id":"1.10.287.110","name":"DnaJ domain"},{"start":60,"end":219,"id":"3.90.190.10","name":"Protein tyrosine phosphatase superfamily"},{"start":228,"end":352,"id":"2.60.40.1110","name":"2.60.40.1110"}]},"uniref50":"UniRef50_O75061","sequence":"MDSSGASSPDMEPSYGGGLFDMVKGGAGRLFSNLKDNLKDTLKDTSSRVIQSVTSYTKGDLDFTYVTSRIIVMSFPLDSVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQAPSLHNLFAVCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAVRLLYAKRPGIGLSPSHRRYLGYMCDLLADKPYRPHFKPLTIKSITVSPVPFFNKQRNGCRPYCDVLIGETKIYTTCADFERMKEYRVQDGKIFIPLSITVQGDVVVSMYHLRSTIGSRLQAKVTNTQIFQLQFHTGFIPLDTTVLKFTKPELDACDVPEKYPQLFQVTLDVELQPHDKVMELTPPWEHYCTKDVNPSILFSSHQEHQDTLVLGGQAPIDIPPDNPRHFGQGGFFSTLCWQDQKSEKSFCEEDHAALVNQESEQSDDELLTLSSPHGNANGDKPHAARKPSKKQQEPAAPAPPEDVDLLGLEGSAVSKNFSSPAAPPSNSELLSDLFGGGGAAGPVQSGQSGVDDVFHPSGPTSTQSTPRRSATSTSASPTLRVGEGATFDPFGAPSKPSGQDLLGSFLNTASASSDPFLQPTRSPSPTVHASSTPAVNIQPDVSGAWDWHTKPGGFGMGSKSAATSPTGSSHGTPTHQNKPQTLDPFADLGTLGGSSFASKPSTPTGLGGGFPPLSSPQKASPQPMGGGWQQGGGYNWQQTQSKPQSSMPHSSPQNRPNYNVSFSSMPGGQNERGKAAANLEGKQKAADFEDLLSGQGFNAHKDKKGPRTIAEMRKEEMAKEMDPEKLKILEWIEGKERNIRALLSTMHTVLWAGETKWKPVGMADLVTPEQVKKVYRKAVLVVHPDKATGQPYEQYAKMIFMELNDAWSEFENQGQKPLY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_O75061-2","disprot_id":"DP00351","ncbi_taxon_id":9913,"regions_counter":6,"creator":"viglesias","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":813,"region_id":"DP00351r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Molecular and functional characterization of clathrin- and AP-2-binding determinants within a disordered domain of auxilin. <i> Scheele U, Alves J, Frank R, Duwel M, Kalthoff C, Ungewickell E. </i> J Biol Chem, 2003","term_id":"IDPO:0000002","curator_id":"atantos","start":547,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"12732633","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":813,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Molecular and functional characterization of clathrin- and AP-2-binding determinants within a disordered domain of auxilin. <i> Scheele U, Alves J, Frank R, Duwel M, Kalthoff C, Ungewickell E. </i> J Biol Chem, 2003","term_id":"GO:0060090","curator_id":"atantos","start":547,"term_ontology":"GO","curator_name":"Agnes Tantos","reference_id":"12732633","version":3,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00351r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":813,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Molecular and functional characterization of clathrin- and AP-2-binding determinants within a disordered domain of auxilin. <i> Scheele U, Alves J, Frank R, Duwel M, Kalthoff C, Ungewickell E. </i> J Biol Chem, 2003","term_id":"GO:0005515","curator_id":"atantos","start":547,"term_ontology":"GO","curator_name":"Agnes Tantos","reference_id":"12732633","version":3,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00351r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":813,"region_id":"DP00351r004","released":"2022_03","ec_id":"ECO:0006317","reference_html":"Molecular and functional characterization of clathrin- and AP-2-binding determinants within a disordered domain of auxilin. <i> Scheele U, Alves J, Frank R, Duwel M, Kalthoff C, Ungewickell E. </i> J Biol Chem, 2003","term_id":"IDPO:0000002","curator_id":"atantos","start":547,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"12732633","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":813,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","reference_html":"Molecular and functional characterization of clathrin- and AP-2-binding determinants within a disordered domain of auxilin. <i> Scheele U, Alves J, Frank R, Duwel M, Kalthoff C, Ungewickell E. </i> J Biol Chem, 2003","term_id":"GO:0060090","curator_id":"atantos","start":547,"term_ontology":"GO","curator_name":"Agnes Tantos","reference_id":"12732633","version":3,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006317","region_id":"DP00351r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":813,"term_name":"protein binding","released":"2022_03","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","reference_html":"Molecular and functional characterization of clathrin- and AP-2-binding determinants within a disordered domain of auxilin. <i> Scheele U, Alves J, Frank R, Duwel M, Kalthoff C, Ungewickell E. </i> J Biol Chem, 2003","term_id":"GO:0005515","curator_id":"atantos","start":547,"term_ontology":"GO","curator_name":"Agnes Tantos","reference_id":"12732633","version":3,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006317","region_id":"DP00351r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q27974","date":"2016-09-07T13:12:30.000Z","acc":"Q27974","name":"Putative tyrosine-protein phosphatase auxilin","length":910,"organism":"Bos taurus","dataset":[],"UniParc":"UPI0000126666","genes":[{"name":{"value":"DNAJC6","evidences":[{"code":"ECO:0000250","source":{"name":"UniProtKB","id":"O75061","url":"https://www.uniprot.org/uniprot/O75061"}}]}}],"alphafold_very_low_content":0.4725274725274725,"disorder_content":0.2934065934065934,"disprot_consensus":{"full":[{"start":547,"end":813,"type":"D"}],"Structural state":[{"start":547,"end":813,"type":"D"}],"Molecular function":[{"start":547,"end":813,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01551","name":"Peptidase family M23","start":209,"end":298}],"gene3D":[{"start":149,"end":316,"id":"2.70.70.10","name":"Glucose Permease (Domain IIA)"},{"start":45,"end":106,"id":"2.40.50.290","name":"2.40.50.290"}]},"uniref50":"UniRef50_O33599","sequence":"MKKLTAAAIATMGFATFTMAHQADAAETTNTQQAHTQMSTQSQDVSYGTYYTIDSNGDYHHTPDGNWNQAMFDNKEYSYTFVDAQGHTHYFYNCYPKNANANGSGQTYVNPATAGDNNDYTASQSQQHINQYGYQSNVGPDASYYSHSNNNQAYNSHDGNGKVNYPNGTSNQNGGSASKATASGHAKDASWLTSRKQLQPYGQYHGGGAHYGVDYAMPENSPVYSLTDGTVVQAGWSNYGGGNQVTIKEANSNNYQWYMHNNRLTVSAGDKVKAGDQIAYSGSTGNSTAPHVHFQRMSGGIGNQYAVDPTSYLQSR","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Staphylococcaceae","Staphylococcus"],"uniref90":"UniRef90_O33599","disprot_id":"DP00352","ncbi_taxon_id":93061,"regions_counter":5,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":44,"region_id":"DP00352r001","released":"2025_06","ec_id":"ECO:0006220","reference_html":"Latent LytM at 1.3A resolution. <i> Odintsov SG, Sabala I, Marcyjaniak M, Bochtler M. </i> J Mol Biol, 2004","term_id":"IDPO:0000002","curator_id":"tcordero","start":26,"term_ontology":"IDPO","curator_name":"Trinidad Cordero","reference_id":"14687573","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2025-02-03T08:13:13.522Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1QWY"}],"term_name":"disorder","curator_orcid":"0000-0003-4991-7170","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"This implies that 19 residues that are chemically present at the N terminus of our molecule are disordered.","type":"Methods"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-03T12:57:40.678Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":182,"region_id":"DP00352r002","released":"2025_06","ec_id":"ECO:0006220","reference_html":"Latent LytM at 1.3A resolution. <i> Odintsov SG, Sabala I, Marcyjaniak M, Bochtler M. </i> J Mol Biol, 2004","term_id":"IDPO:0000002","curator_id":"tcordero","start":147,"term_ontology":"IDPO","curator_name":"Trinidad Cordero","reference_id":"14687573","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2025-02-03T08:15:21.011Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1QWY"}],"term_name":"disorder","curator_orcid":"0000-0003-4991-7170","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The C-domain (shown at the top of Figure 1) comprises residues 99–316 and can be divided into two ordered regions that are located upstream and downstream of the disordered segment from residue 147 to residue 182.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-03T12:57:58.207Z"}},{"start":108,"end":184,"reference_id":"37742292","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N NMR chemical shift assignment of LytM N-terminal domain (residues 26-184). <i> Pitkänen I, Tossavainen H, Permi P. </i> Biomol NMR Assign, 2023","date":"2025-02-03T08:17:13.760Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00352r003","statement":[{"text":"Based on chemical shift dispersion and bioinformatics, residues downstream 107 are mainly disordered.","type":"Results"}],"cross_refs":[{"db":"BMRB","id":"51662"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-03T12:58:07.808Z"}},{"start":108,"end":184,"reference_id":"37742292","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N NMR chemical shift assignment of LytM N-terminal domain (residues 26-184). <i> Pitkänen I, Tossavainen H, Permi P. </i> Biomol NMR Assign, 2023","date":"2025-02-03T08:29:09.663Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00352r004","statement":[{"text":"The peaks assigned to the linker region (108–184), on the other hand, are all found within 7.8–8.3 ppm in the 1HN dimension, and the signals overlap considerably.","type":"Methods"}],"cross_refs":[{"db":"BMRB","id":"51662"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-03T12:58:41.437Z"}},{"start":147,"end":182,"reference_id":"14687573","reference_source":"pmid","reference_html":"Latent LytM at 1.3A resolution. <i> Odintsov SG, Sabala I, Marcyjaniak M, Bochtler M. </i> J Mol Biol, 2004","date":"2025-01-31T13:30:47.168Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00352r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"The C-domain (shown at the top of Figure 1) comprises residues 99–316 and can be divided into two ordered regions that are located upstream and downstream of the disordered segment from residue 147 to residue 182.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"1QWY"}]}],"released":"2025_06","uniref100":"UniRef100_O33599","date":"2016-08-12T13:44:44.000Z","acc":"O33599","name":"Glycyl-glycine endopeptidase LytM","length":316,"organism":"Staphylococcus aureus (strain NCTC 8325)","dataset":["Bacterial virulence-related proteins"],"UniParc":"UPI000052A49A","genes":[{"name":{"value":"lytM"},"olnNames":[{"value":"SAOUHSC_00248"}]}],"alphafold_very_low_content":0.24050632911392406,"disorder_content":0.3037974683544304,"disprot_consensus":{"full":[{"start":26,"end":44,"type":"D"},{"start":108,"end":184,"type":"D"}],"Structural state":[{"start":26,"end":44,"type":"D"},{"start":108,"end":184,"type":"D"}],"Disorder function":[{"start":108,"end":184,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00043","name":"Glutathione S-transferase, C-terminal domain","start":224,"end":345},{"id":"PF02798","name":"Glutathione S-transferase, N-terminal domain","start":114,"end":190}],"gene3D":[{"start":197,"end":349,"id":"1.20.1050.10","name":"1.20.1050.10"},{"start":95,"end":196,"id":"3.40.30.10","name":"Glutaredoxin"}]},"uniref50":"UniRef50_P23202","sequence":"MMNNNGNQVSNLSNALRQVNIGNRNSNTTTDQSNINFEFSTGVNNNNNNNSSSNNNNVQNNNSGRNGSQNNDNENNIKNTLEQHRQQQQAFSDMSHVEYSRITKFFQEQPLEGYTLFSHRSAPNGFKVAIVLSELGFHYNTIFLDFNLGEHRAPEFVSVNPNARVPALIDHGMDNLSIWESGAILLHLVNKYYKETGNPLLWSDDLADQSQINAWLFFQTSGHAPMIGQALHFRYFHSQKIASAVERYTDEVRRVYGVVEMALAERREALVMELDTENAAAYSAGTTPMSQSRFFDYPVWLVGDKLTIADLAFVPWNNVVDRIGINIKIEFPEVYKWTKHMMRRPAVIKALRGE","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P23202","disprot_id":"DP00353","ncbi_taxon_id":559292,"regions_counter":6,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":90,"region_id":"DP00353r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Is the prion domain of soluble Ure2p unstructured? <i> Pierce MM, Baxa U, Steven AC, Bax A, Wickner RB. </i> Biochemistry, 2005","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15628874","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":90,"region_id":"DP00353r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Stability, folding, dimerization, and assembly properties of the yeast prion Ure2p. <i> Thual C, Bousset L, Komar AA, Walter S, Buchner J, Cullin C, Melki R. </i> Biochemistry, 2001","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11327838","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":90,"region_id":"DP00353r003","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Stability, folding, dimerization, and assembly properties of the yeast prion Ure2p. <i> Thual C, Bousset L, Komar AA, Walter S, Buchner J, Cullin C, Melki R. </i> Biochemistry, 2001","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11327838","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":90,"region_id":"DP00353r004","released":"2022_03","ec_id":"ECO:0001249","reference_html":"Stability, folding, dimerization, and assembly properties of the yeast prion Ure2p. <i> Thual C, Bousset L, Komar AA, Walter S, Buchner J, Cullin C, Melki R. </i> Biochemistry, 2001","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11327838","version":2,"ec_name":"fluorescence evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":294,"region_id":"DP00353r005","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p. <i> Umland TC, Taylor KL, Rhee S, Wickner RB, Davies DR. </i> Proc Natl Acad Sci U S A, 2001","term_id":"IDPO:0000002","curator_id":"fquaglia","start":273,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11171973","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1HQO"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":89,"region_id":"DP00353r006","released":"2022_03","ec_id":"ECO:0006289","reference_html":"Prion domain of yeast Ure2 protein adopts a completely disordered structure: a solid-support EPR study. <i> Ngo S, Chiang V, Ho E, Le L, Guo Z. </i> PLoS One, 2012","statement":[{"text":"Using EPR approach, we investigated the structure of isolated Ure2p prion domain in the construct of Ure2p1–89-M, which is tethered on solid support to prevent protein aggregation. We showed that the pattern of site-specific spin label mobility remains unchanged when the buffer is changed from a strong denaturing buffer to a native buffer, suggesting that the structure of Ure2p1–89-M is completely disordered.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":1,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"23077577","version":2,"ec_name":"site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P23202","date":"2016-08-25T13:03:12.000Z","acc":"P23202","name":"Transcriptional regulator URE2","length":354,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000003993","genes":[{"name":{"value":"URE2"},"orfNames":[{"value":"N1165"}],"olnNames":[{"value":"YNL229C"}]}],"alphafold_very_low_content":0.2033898305084746,"disorder_content":0.3163841807909605,"disprot_consensus":{"full":[{"start":1,"end":90,"type":"D"},{"start":273,"end":294,"type":"D"}],"Structural state":[{"start":1,"end":90,"type":"D"},{"start":273,"end":294,"type":"D"}]}},{"features":{"pfam":[{"id":"PF04487","name":"CITED","start":1,"end":270}]},"uniref50":"UniRef50_O35740","sequence":"MADHMMAMNHGRFPDGTNGLHHHPAHRMGMGQFPSPHHHQQQQPQHAFNALMGEHIHYGAGNMNATSGIRHAMGPGTVNGGHPPSALAPAARFNNSQFMGPPVASQGGSLPASMQLQKLNNQYFNHHPYPHNHYMPDLHPAAGHQMNGTNQHFRDCNPKHSGGSSTPGGSGGSSTPGGSGSSSGGGAGSSNSGGGSGSGNMPASVAHVPAAMLPPNVIDTDFIDEEVLMSLVIEMGLDRIKELPELWLGQNEFDFMTDFVCKQQPSRVSC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O35740-4","disprot_id":"DP00356","ncbi_taxon_id":9606,"regions_counter":18,"creator":"grivas","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":270,"region_id":"DP00356r001","released":"2025_12","ec_id":"ECO:0006204","reference_html":"Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites. <i> De Guzman RN, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> J Biol Chem, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":220,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14594809","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2025-08-13T15:43:28.027Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The free CITED2 activation domain, residues 220-269, is unstructured in solution as indicated by the absence of secondary structural elements in the circular dichroism spectra (Fig. 2A) and the narrow range of amide proton chemical shifts in the two-dimensional 1H-15N HSQC spectrum of 15N-labeled CITED2 (Fig. 2B).","type":"Results"}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":270,"term_name":"protein binding","start":220,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"vnugnes","released":"2025_12","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"14594809","version":4,"reference_html":"Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites. <i> De Guzman RN, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> J Biol Chem, 2004","date":"2025-08-13T16:28:19.625Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00356r004","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P45481","operator":"and","partner_start":340,"partner_end":439}],"statement":[{"text":"The CD spectrum of the complex (Fig. 2A) shows the formation of additional structure compared with the individual proteins, as indicated by a comparison of the spectrum of the complex with the sum of the spectra of the two components. ","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":270,"region_id":"DP00356r005","released":"2025_12","ec_id":"ECO:0006165","reference_html":"Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites. <i> De Guzman RN, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> J Biol Chem, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":258,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14594809","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2025-08-13T16:25:42.319Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1R8U"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P45481"}],"statement":[{"text":"Measurement of the heteronuclear [1H]-15N NOE for CITED2 in the complex (Fig. 3) shows that the carboxyl-terminal 10 residues are relatively mobile.","type":"Results"},{"text":"The carboxyl-terminal end of CITED2, beyond Asp-257 is disordered and is not shown.","type":"Figure"}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":257,"term_name":"protein binding","start":222,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2025_12","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"14594809","version":4,"reference_html":"Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites. <i> De Guzman RN, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> J Biol Chem, 2004","date":"2025-08-13T16:34:11.115Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00356r008","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"1R8U"}],"interaction_partner":[{"db":"UniProt","id":"P45481","operator":"and","partner_start":340,"partner_end":439}],"statement":[{"text":"Upon binding to TAZ1, there is increased dispersion of the CITED2 amide proton chemical shifts, indicating structure formation (Fig. 2B).","type":"Results"},{"text":"Weak intermolecular NOEs from Asp-258, Phe-259, and Val-260 in the CITED2 flexible tail to the α1 residues Pro-343, Thr-344, and Ala-345 probably reflect transient contacts, because the last 10 carboxyl-terminal residues of CITED2 are apparently unstructured, as indicated by diminished [1H]-15N heteronuclear NOE values (Fig. 3).","type":"Results"}]},{"start":220,"end":270,"reference_id":"14594809","reference_source":"pmid","reference_html":"Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites. <i> De Guzman RN, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> J Biol Chem, 2004","date":"2025-08-13T15:46:38.714Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"region_id":"DP00356r009","statement":[{"text":"The free CITED2 activation domain, residues 220-269, is unstructured in solution as indicated by the absence of secondary structural elements in the circular dichroism spectra (Fig. 2A) and the narrow range of amide proton chemical shifts in the two-dimensional 1H-15N HSQC spectrum of 15N-labeled CITED2 (Fig. 2B).","type":"Results"}]},{"start":220,"end":257,"reference_id":"14594809","reference_source":"pmid","reference_html":"Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites. <i> De Guzman RN, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> J Biol Chem, 2004","date":"2025-08-13T16:22:19.589Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"PDB","id":"1R8U"}],"region_id":"DP00356r010","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P45481"}],"statement":[{"text":"Upon binding to TAZ1, there is increased dispersion of the CITED2 amide proton chemical shifts, indicating structure formation (Fig. 2B).","type":"Results"},{"text":"The changes in chemical shifts for the CITED2 protein upon binding indicate the formation of a helical structure in the N terminus, with an extended structure in the center of the sequence.","type":"Results"},{"text":"Measurement of the heteronuclear [1H]-15N NOE for CITED2 in the complex (Fig. 3) shows that the carboxyl-terminal 10 residues are relatively mobile.","type":"Results"}],"states_connection":[{"source":"DP00356r009","target":"DP00356r011"}]},{"start":220,"end":257,"reference_id":"14594809","reference_source":"pmid","reference_html":"Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites. <i> De Guzman RN, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> J Biol Chem, 2004","date":"2025-08-13T16:22:31.191Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"PDB","id":"1R8U"}],"region_id":"DP00356r011","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P45481"}],"statement":[{"text":"Upon binding to TAZ1, there is increased dispersion of the CITED2 amide proton chemical shifts, indicating structure formation (Fig. 2B).","type":"Results"},{"text":"The changes in chemical shifts for the CITED2 protein upon binding indicate the formation of a helical structure in the N terminus, with an extended structure in the center of the sequence.","type":"Results"},{"text":"Measurement of the heteronuclear [1H]-15N NOE for CITED2 in the complex (Fig. 3) shows that the carboxyl-terminal 10 residues are relatively mobile.","type":"Results"}]},{"start":220,"end":257,"reference_id":"14594809","reference_source":"pmid","reference_html":"Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites. <i> De Guzman RN, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> J Biol Chem, 2004","date":"2025-08-13T16:22:01.747Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P45481","operator":null,"partner_start":340,"partner_end":439}],"region_id":"DP00356r012","statement":[{"text":"The shorter CITED2 construct (residues 220-269) showed high affinity to TAZ1 (Kd = 13 nm, Table I) with less tendency to precipitate upon binding to TAZ1 and was therefore used for structure determination.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_Q99967","date":"2016-09-06T11:58:29.000Z","acc":"Q99967","name":"Cbp/p300-interacting transactivator 2","length":270,"organism":"Homo sapiens","dataset":["Stress response proteins"],"UniParc":"UPI000002A68D","genes":[{"name":{"value":"CITED2"},"synonyms":[{"value":"MRG1"}]}],"alphafold_very_low_content":0.5333333333333333,"disorder_content":0.18888888888888888,"disprot_consensus":{"full":[{"start":220,"end":257,"type":"T"},{"start":258,"end":270,"type":"D"}],"Structural state":[{"start":220,"end":270,"type":"D"}],"Molecular function":[{"start":220,"end":270,"type":"F"}],"Structural transition":[{"start":220,"end":257,"type":"T"}]}},{"features":{"pfam":[{"id":"PF01290","name":"Thymosin beta-4 family","start":3,"end":41}],"gene3D":[{"start":2,"end":41,"id":"1.20.5.520","name":"Single helix bin"}]},"uniref50":"UniRef50_P62328","sequence":"MSDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P62328","disprot_id":"DP00357","ncbi_taxon_id":9606,"regions_counter":13,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":44,"region_id":"DP00357r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Conformation of thymosin beta 4 in water determined by NMR spectroscopy. <i> Czisch M, Schleicher M, Hörger S, Voelter W, Holak TA. </i> Eur J Biochem, 1993","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"8269922","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":44,"term_name":"disorder to order","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"8269922","version":2,"reference_html":"Conformation of thymosin beta 4 in water determined by NMR spectroscopy. <i> Czisch M, Schleicher M, Hörger S, Voelter W, Holak TA. </i> Eur J Biochem, 1993","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00357r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":44,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"8269922","version":3,"reference_html":"Conformation of thymosin beta 4 in water determined by NMR spectroscopy. <i> Czisch M, Schleicher M, Hörger S, Voelter W, Holak TA. </i> Eur J Biochem, 1993","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00357r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":44,"region_id":"DP00357r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Coupling of folding and binding of thymosin beta4 upon interaction with monomeric actin monitored by nuclear magnetic resonance. <i> Domanski M, Hertzog M, Coutant J, Gutsche-Perelroizen I, Bontems F, Carlier MF, Guittet E, van Heijenoort C. </i> J Biol Chem, 2004","statement":[{"text":"The assignment of the proton, nitrogen, and carbon resonances of Tβ4 free in solution were obtained using standard procedures. The HSQC spectrum of Tβ4 in solution is typical of an unfolded protein, with a very narrow range of amide proton resonances. NOE correlations for all residues along segment 5-16 indicates that this part of the protein folds as a α-helix.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bhajdu","start":17,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"15039431","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":44,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Coupling of folding and binding of thymosin beta4 upon interaction with monomeric actin monitored by nuclear magnetic resonance. <i> Domanski M, Hertzog M, Coutant J, Gutsche-Perelroizen I, Bontems F, Carlier MF, Guittet E, van Heijenoort C. </i> J Biol Chem, 2004","statement":[{"text":"The small negative Hα and positive Cα shifts relative to the random coil shifts observed for residues 31-37 suggest that this segment has a weak tendency to fold into an α-helix. \nThe large dispersion of amide proton resonances in the bound form (to CaATP-actin) is typical of a fully structured protein.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"bhajdu","start":17,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","reference_id":"15039431","version":2,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00357r006","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":44,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Coupling of folding and binding of thymosin beta4 upon interaction with monomeric actin monitored by nuclear magnetic resonance. <i> Domanski M, Hertzog M, Coutant J, Gutsche-Perelroizen I, Bontems F, Carlier MF, Guittet E, van Heijenoort C. </i> J Biol Chem, 2004","statement":[{"text":"The large spreading of all resonances of Tβ4 testifies that at 25 °C, Tβ4 forms a tight complex with G-actin, in which the environment of all residues of the peptide is drastically modified, either by folding or by making contacts with G-actin.","type":"Results"}],"term_id":"GO:0005515","curator_id":"bhajdu","start":17,"term_ontology":"GO","curator_name":"Borbála Hajdu-Soltész","reference_id":"15039431","version":3,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00357r007","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":44,"region_id":"DP00357r008","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Thymosin beta 4 binds actin in an extended conformation and contacts both the barbed and pointed ends. <i> Safer D, Sosnick TR, Elzinga M. </i> Biochemistry, 1997","statement":[{"text":"The spectrum of free thymosin beta4 is dominated by the deep trough at 200 nm indicating that thymosin beta4 is predominantly in a random coil conformation.  The nonzero value at 222 nm indicates that part of the structure may not be an ideal random coil.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bhajdu","start":1,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"9153421","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":44,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Thymosin beta 4 binds actin in an extended conformation and contacts both the barbed and pointed ends. <i> Safer D, Sosnick TR, Elzinga M. </i> Biochemistry, 1997","statement":[{"text":"The CD spectrum of thymosin â4 was also measured in the presence of equimolar actin.","type":"Results"}],"term_id":"GO:0005515","curator_id":"bhajdu","start":1,"term_ontology":"GO","curator_name":"Borbála Hajdu-Soltész","reference_id":"9153421","version":3,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00357r009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":44,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Thymosin beta 4 binds actin in an extended conformation and contacts both the barbed and pointed ends. <i> Safer D, Sosnick TR, Elzinga M. </i> Biochemistry, 1997","statement":[{"text":"The thymosin beta4 spectrum indicated a predominantly random coil structure, but the increased depth of the trough at 222 nm indicated the formation of some additional ordered structure upon binding actin.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"bhajdu","start":1,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","reference_id":"9153421","version":2,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00357r010","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":44,"region_id":"DP00357r011","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Thymosin beta 4 binds actin in an extended conformation and contacts both the barbed and pointed ends. <i> Safer D, Sosnick TR, Elzinga M. </i> Biochemistry, 1997","statement":[{"text":"One-dimensional 1H NMR spectra of free thymosin beta4 showed narrow line widths and low dispersion, and are consistent with a predominantly random coil structure which is highly mobile on the NMR time scale.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bhajdu","start":1,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"9153421","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":44,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Thymosin beta 4 binds actin in an extended conformation and contacts both the barbed and pointed ends. <i> Safer D, Sosnick TR, Elzinga M. </i> Biochemistry, 1997","statement":[{"text":"The spectrum of thymosin beta4 bound to actin, after subtraction of the actin signal, is very similar to\nthe spectrum of free thymosin beta4.","type":"Results"}],"term_id":"GO:0005515","curator_id":"bhajdu","start":1,"term_ontology":"GO","curator_name":"Borbála Hajdu-Soltész","reference_id":"9153421","version":3,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00357r012","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":44,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Thymosin beta 4 binds actin in an extended conformation and contacts both the barbed and pointed ends. <i> Safer D, Sosnick TR, Elzinga M. </i> Biochemistry, 1997","statement":[{"text":"Overall, the published spectroscopic results and those presented above suggest that in the actin-Tß4 complex, up to 12 residues of thymosin beta4, possibly residues 5-16, are in an alpha-helical conformation, while the rest of the peptide is predominantly in a random coil conformation.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"bhajdu","start":1,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","reference_id":"9153421","version":2,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00357r013","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2016_10","uniref100":"UniRef100_P62328","date":"2016-08-22T16:36:32.000Z","acc":"P62328","name":"Thymosin beta-4","length":44,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000004613E","genes":[{"name":{"value":"TMSB4X"},"synonyms":[{"value":"TB4X"},{"value":"THYB4"},{"value":"TMSB4"}]}],"alphafold_very_low_content":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":44,"type":"T"}],"Structural state":[{"start":1,"end":44,"type":"D"}],"Structural transition":[{"start":1,"end":44,"type":"T"}],"Molecular function":[{"start":1,"end":44,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04969","name":"CS domain","start":6,"end":79}],"gene3D":[{"start":1,"end":125,"id":"2.60.40.790","name":"2.60.40.790"}]},"uniref50":"UniRef50_Q15185","sequence":"MQPASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGESGQSWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNFDRFSEMMNNMGGDEDVDLPEVDGADDDSQDSDDEKMPDLE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q15185","disprot_id":"DP00358","ncbi_taxon_id":9606,"regions_counter":3,"creator":"maspromonte","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":160,"region_id":"DP00358r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function. <i> Weikl T, Abelmann K, Buchner J. </i> J Mol Biol, 1999","term_id":"IDPO:0000002","curator_id":"maspromonte","start":123,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1EJF"}],"reference_id":"10543959","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":160,"term_name":"order to disorder","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function. <i> Weikl T, Abelmann K, Buchner J. </i> J Mol Biol, 1999","term_id":"IDPO:0000014","curator_id":"maspromonte","start":123,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","reference_id":"10543959","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00358r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":160,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function. <i> Weikl T, Abelmann K, Buchner J. </i> J Mol Biol, 1999","term_id":"GO:0005515","curator_id":"maspromonte","start":123,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"10543959","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00358r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q15185","date":"2016-09-05T20:54:18.000Z","acc":"Q15185","name":"Prostaglandin E synthase 3","length":160,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000052BAE","genes":[{"name":{"value":"PTGES3"},"synonyms":[{"value":"P23"},{"value":"TEBP"}]}],"alphafold_very_low_content":0.05,"disorder_content":0.2375,"disprot_consensus":{"full":[{"start":123,"end":160,"type":"T"}],"Structural state":[{"start":123,"end":160,"type":"D"}],"Structural transition":[{"start":123,"end":160,"type":"T"}],"Molecular function":[{"start":123,"end":160,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02672","name":"CP12 domain","start":35,"end":106}]},"uniref50":"UniRef50_A6Q0K5","sequence":"MMLTKSVVISRPAVRPVSTRRAVVVRASGQPAVDLNKKVQDAVKEAEDACAKGTSADCAVAWDTVEELSAAVSHKKDAVKADVTLTDPLEAFCKDAPDADECRVYED","taxonomy":["Eukaryota","Viridiplantae","Chlorophyta","core chlorophytes","Chlorophyceae","CS clade","Chlamydomonadales","Chlamydomonadaceae","Chlamydomonas"],"uniref90":"UniRef90_A6Q0K5","disprot_id":"DP00359","ncbi_taxon_id":3055,"regions_counter":9,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":50,"region_id":"DP00359r002","released":"2024_06","ec_id":"ECO:0006165","reference_html":"The small protein CP12: a protein linker for supramolecular complex assembly. <i> Graciet E, Gans P, Wedel N, Lebreton S, Camadro JM, Gontero B. </i> Biochemistry, 2003","statement":[{"text":"CP12 is an 8.5-kDa nuclear-encoded chloroplast protein, isolated from higher plants. It forms part of a core complex of two dimers of phosphoribulokinase (PRK), two tetramers of glyceraldehyde 3-phosphate dehydrogenase (GAPDH), and CP12. Oxidized, but not reduced, CP12 acts as a linker in the assembly of the complex. Reduced CP12 is mainly unstructured","type":"Curator statement"},{"text":"The reduction of oxidized CP12 caused a very large change in the NMR spectrum. All the correlations in the HSQC having chemical shift values different from those of a random coil disappeared, and all the chemical shift values of the correlations were those for a typical unstructured peptide (Figure 5). In addition, all the heteronuclear nOe effects became very negative, indicating that reduced CP12 was much more mobile than the oxidized form. Thus, CP12 became completely unstructured upon reduction, in agreement with the CD experiments.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12846565","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2024-03-13T15:20:44.931Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":50,"region_id":"DP00359r004","released":"2024_06","ec_id":"ECO:0006204","reference_html":"The small protein CP12: a protein linker for supramolecular complex assembly. <i> Graciet E, Gans P, Wedel N, Lebreton S, Camadro JM, Gontero B. </i> Biochemistry, 2003","statement":[{"text":"CP12 is an 8.5-kDa nuclear-encoded chloroplast protein, isolated from higher plants. It forms part of a core complex of two dimers of phosphoribulokinase (PRK), two tetramers of glyceraldehyde 3-phosphate dehydrogenase (GAPDH), and CP12. Oxidized, but not reduced, CP12 acts as a linker in the assembly of the complex. Reduced CP12 is mainly unstructured","type":"Curator statement"},{"text":"The reduction of oxidized CP12 caused a very large change in the NMR spectrum. All the correlations in the HSQC having chemical shift values different from those of a random coil disappeared, and all the chemical shift values of the correlations were those for a typical unstructured peptide (Figure 5). In addition, all the heteronuclear nOe effects became very negative, indicating that reduced CP12 was much more mobile than the oxidized form. Thus, CP12 became completely unstructured upon reduction, in agreement with the CD experiments.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12846565","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2024-03-13T15:21:01.471Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":60,"region_id":"DP00359r006","released":"2022_03","ec_id":"ECO:0006198","reference_html":"Cryptic Disorder Out of Disorder: Encounter between Conditionally Disordered CP12 and Glyceraldehyde-3-Phosphate Dehydrogenase. <i> Launay H, Barré P, Puppo C, Zhang Y, Maneville S, Gontero B, Receveur-Bréchot V. </i> J Mol Biol, 2018","statement":[{"text":"Low {1H}–15N het-NOE values (< 0.4), typical of a disordered linker between globular domains, are observed for residues A51–D60","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":51,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29501381","version":2,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":60,"term_name":"flexible linker","start":51,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","statement":[{"text":"the N-terminal region is unstable, oscillates at the ms timescale between helical and random conformations, and is connected through a disordered linker to its C-terminus, which forms a stable helical turn.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29501381","version":3,"reference_html":"Cryptic Disorder Out of Disorder: Encounter between Conditionally Disordered CP12 and Glyceraldehyde-3-Phosphate Dehydrogenase. <i> Launay H, Barré P, Puppo C, Zhang Y, Maneville S, Gontero B, Receveur-Bréchot V. </i> J Mol Biol, 2018","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006198","region_id":"DP00359r007","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":78,"region_id":"DP00359r008","released":"2022_03","ec_id":"ECO:0006198","reference_html":"Cryptic Disorder Out of Disorder: Encounter between Conditionally Disordered CP12 and Glyceraldehyde-3-Phosphate Dehydrogenase. <i> Launay H, Barré P, Puppo C, Zhang Y, Maneville S, Gontero B, Receveur-Bréchot V. </i> J Mol Biol, 2018","statement":[{"text":"In C. reinhardtii, the reduction/oxidation regulation of CP12 is mediated via its four cysteine residues, which are involved into two disulfide bridges under oxidized state (C23–C31 and C66–C75) [28]. The disorder to order transition induced by formation of these disulfide bridges endows CP12 with the same peculiar properties as other IDPs named conditionally disordered proteins.","type":"Introduction"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":62,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29501381","version":2,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":78,"term_name":"disorder to order","start":62,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","statement":[{"text":"The most drastic differences are in the C-terminal region L62–Y78, indicating that oxidation triggered the folding of this region. The Cα chemical shifts of this region indicate a helical formation.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29501381","version":2,"reference_html":"Cryptic Disorder Out of Disorder: Encounter between Conditionally Disordered CP12 and Glyceraldehyde-3-Phosphate Dehydrogenase. <i> Launay H, Barré P, Puppo C, Zhang Y, Maneville S, Gontero B, Receveur-Bréchot V. </i> J Mol Biol, 2018","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006198","region_id":"DP00359r009","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2016_10","uniref100":"UniRef100_A6Q0K5","date":"2016-09-06T19:52:05.000Z","acc":"A6Q0K5","name":"Calvin cycle protein CP12, chloroplastic","length":107,"organism":"Chlamydomonas reinhardtii","dataset":[],"UniParc":"UPI0001574C22","genes":[{"name":{"value":"CP12"},"orfNames":[{"value":"CHLREDRAFT_148487"}]}],"alphafold_very_low_content":0.018691588785046728,"disorder_content":0.719626168224299,"disprot_consensus":{"full":[{"start":1,"end":60,"type":"D"},{"start":62,"end":78,"type":"T"}],"Structural state":[{"start":1,"end":60,"type":"D"},{"start":62,"end":78,"type":"D"}],"Disorder function":[{"start":51,"end":60,"type":"F"}],"Structural transition":[{"start":62,"end":78,"type":"T"}]}},{"features":{"pfam":[{"id":"PF01704","name":"UTP--glucose-1-phosphate uridylyltransferase","start":46,"end":451}],"gene3D":[{"start":1,"end":437,"id":"3.90.550.10","name":"Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A"},{"start":460,"end":522,"id":"3.40.1630.20","name":"3.40.1630.20"}]},"uniref50":"UniRef50_Q16222","sequence":"MNINDLKLTLSKAGQEHLLRFWNELEEAQQVELYAELQAMNFEELNFFFQKAIEGFNQSSHQKNVDARMEPVPREVLGSATRDQDQLQAWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYYGNKCIIPWYIMTSGRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGIWSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQKRSSDGRLLFNAGNIANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPYVDTQGQLIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLKNADSQNGKDNPTTARHALMSLHHCWVLNAGGHFIDENGSRLPAIPRSATNGKSETITADVNHNLKDANDVPIQCEISPLISYAGEGLESYVADKEFHAPLIIDENGVHELVKNGI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q16222","disprot_id":"DP00363","ncbi_taxon_id":9606,"regions_counter":3,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":470,"region_id":"DP00363r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture. <i> Peneff C, Ferrari P, Charrier V, Taburet Y, Monnier C, Zamboni V, Winter J, Harnois M, Fassy F, Bourne Y. </i> EMBO J, 2001","term_id":"IDPO:0000002","curator_id":"mnecci","start":454,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"11707391","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1JVD"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":470,"term_name":"flexible linker","start":454,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"11707391","version":3,"reference_html":"Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture. <i> Peneff C, Ferrari P, Charrier V, Taburet Y, Monnier C, Zamboni V, Winter J, Harnois M, Fassy F, Bourne Y. </i> EMBO J, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006220","region_id":"DP00363r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":470,"term_name":"molecular function regulator","start":454,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"11707391","version":3,"reference_html":"Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture. <i> Peneff C, Ferrari P, Charrier V, Taburet Y, Monnier C, Zamboni V, Winter J, Harnois M, Fassy F, Bourne Y. </i> EMBO J, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006220","region_id":"DP00363r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q16222","date":"2016-09-20T11:59:35.000Z","acc":"Q16222","name":"UDP-N-acetylhexosamine pyrophosphorylase","length":522,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000002B673","genes":[{"name":{"value":"UAP1"},"synonyms":[{"value":"SPAG2"}]}],"alphafold_very_low_content":0.040229885057471264,"disorder_content":0.032567049808429116,"disprot_consensus":{"full":[{"start":454,"end":470,"type":"D"}],"Structural state":[{"start":454,"end":470,"type":"D"}],"Disorder function":[{"start":454,"end":470,"type":"F"}],"Molecular function":[{"start":454,"end":470,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00071","name":"Ras family","start":8,"end":167}],"gene3D":[{"start":1,"end":180,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_Q15382","sequence":"MPQSKSRKIAILGYRSVGKSSLTIQFVEGQFVDSYDPTIENTFTKLITVNGQEYHLQLVDTAGQDEYSIFPQTYSIDINGYILVYSVTSIKSFEVIKVIHGKLLDMVGKVQIPIMLVGNKKDLHMERVISYEEGKALAESWNAAFLESSAKENQTAVDVFRRIILEAEKMDGAASQGKSSCSVM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q15382","disprot_id":"DP00364","ncbi_taxon_id":9606,"regions_counter":7,"creator":"ameszaros","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":181,"region_id":"DP00364r005","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Arl2-GTP and Arl3-GTP regulate a GDI-like transport system for farnesylated cargo. <i> Ismail SA, Chen YX, Rusinova A, Chandra A, Bierbaum M, Gremer L, Triola G, Waldmann H, Bastiaens PI, Wittinghofer A. </i> Nat Chem Biol, 2011","term_id":"IDPO:0000002","curator_id":"ameszaros","start":171,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"22002721","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3T5G"}],"term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":181,"term_name":"disorder to order","start":171,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ameszaros","released":"2022_03","term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"22002721","version":2,"reference_html":"Arl2-GTP and Arl3-GTP regulate a GDI-like transport system for farnesylated cargo. <i> Ismail SA, Chen YX, Rusinova A, Chandra A, Bierbaum M, Gremer L, Triola G, Waldmann H, Bastiaens PI, Wittinghofer A. </i> Nat Chem Biol, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00364r006","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":181,"term_name":"protein binding","start":171,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ameszaros","released":"2022_03","term_ontology":"GO","curator_name":"Attila Meszaros","reference_id":"22002721","version":3,"reference_html":"Arl2-GTP and Arl3-GTP regulate a GDI-like transport system for farnesylated cargo. <i> Ismail SA, Chen YX, Rusinova A, Chandra A, Bierbaum M, Gremer L, Triola G, Waldmann H, Bastiaens PI, Wittinghofer A. </i> Nat Chem Biol, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00364r007","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q15382","date":"2016-09-08T13:28:11.000Z","acc":"Q15382","name":"GTP-binding protein Rheb","length":184,"organism":"Homo sapiens","dataset":["Autophagy-related proteins"],"UniParc":"UPI0000133863","genes":[{"name":{"value":"RHEB"},"synonyms":[{"value":"RHEB2"}]}],"alphafold_very_low_content":0.02717391304347826,"disorder_content":0.059782608695652176,"disprot_consensus":{"full":[{"start":171,"end":181,"type":"T"}],"Structural state":[{"start":171,"end":181,"type":"D"}],"Structural transition":[{"start":171,"end":181,"type":"T"}],"Molecular function":[{"start":171,"end":181,"type":"F"}]}},{"features":{"pfam":[{"id":"PF15063","name":"Thyroid cancer protein 1","start":12,"end":85}]},"uniref50":"UniRef50_Q9NR00","sequence":"MKAKRSHQAVIMSTSLRVSPSIHGYHFDTASRKKAVGNIFENTDQESLERLFRNSGDKKAEERAKIIFAIDQDVEEKTRALMALKKRTKDKLFQFLKLRKYSIKVH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9NR00","disprot_id":"DP00372","ncbi_taxon_id":9606,"regions_counter":2,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":106,"region_id":"DP00372r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"TC-1 is a novel tumorigenic and natively disordered protein associated with thyroid cancer. <i> Sunde M, McGrath KC, Young L, Matthews JM, Chua EL, Mackay JP, Death AK. </i> Cancer Res, 2004","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15087392","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":106,"region_id":"DP00372r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"TC-1 is a novel tumorigenic and natively disordered protein associated with thyroid cancer. <i> Sunde M, McGrath KC, Young L, Matthews JM, Chua EL, Mackay JP, Death AK. </i> Cancer Res, 2004","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15087392","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q9NR00","date":"2016-08-25T13:47:13.000Z","acc":"Q9NR00","name":"Transcriptional and immune response regulator","length":106,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000013FBD4","genes":[{"name":{"value":"TCIM","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:1357","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:1357"}}]},"synonyms":[{"value":"C8orf4"},{"value":"TC1"}]}],"alphafold_very_low_content":0.018867924528301886,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":106,"type":"D"}],"Structural state":[{"start":1,"end":106,"type":"D"}]}},{"features":{"pfam":[{"id":"PF04352","name":"ProQ/FINO family","start":8,"end":115},{"id":"PF17516","name":"ProQ C-terminal domain","start":182,"end":232}],"gene3D":[{"start":1,"end":120,"id":"1.10.1710.10","name":"ProQ/FinO domain"}]},"uniref50":"UniRef50_Q8XCM4","sequence":"MENQPKLNSSKEVIAFLAERFPHCFSAEGEARPLKIGIFQDLVDRVAGEMNLSKTQLRSALRLYTSSWRYLYGVKPGATRVDLDGNPCGELDEQHVEHARKQLEEAKARVQAQRAEQQAKKREAAATAGEKEDAPRRERKPRPTTPRRKEGAERKPRAQKPVEKAPKTVKAPREEQHTPVSDISALTVGQALKVKAGQNAMDATVLEITKDGVRVQLNSGMSLIVRAEHLVF","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_Q8XCM4","disprot_id":"DP00377","ncbi_taxon_id":83333,"regions_counter":4,"creator":"nveljkovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":173,"region_id":"DP00377r001","released":"2024_06","ec_id":"ECO:0007691","reference_html":"Structural and functional analysis of ProQ: an osmoregulatory protein of Escherichia coli. <i> Smith MN, Kwok SC, Hodges RS, Wood JM. </i> Biochemistry, 2007","term_id":"IDPO:0000002","curator_id":"vnugnes","start":130,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-03-27T14:14:26.328Z","reference_source":"pmid","term_name":"disorder","reference_id":"17319698","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"Thus, limited trypsin digestion of purified ProQ yielded protease resistant fragments corresponding to the predicted N- and C-terminal domains. In contrast, fragments corresponding to predicted tryptic fragments within the linker region (amino acids 130−173) were not found.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":173,"region_id":"DP00377r002","released":"2024_06","ec_id":"ECO:0006204","reference_html":"Structural and functional analysis of ProQ: an osmoregulatory protein of Escherichia coli. <i> Smith MN, Kwok SC, Hodges RS, Wood JM. </i> Biochemistry, 2007","term_id":"IDPO:0000002","curator_id":"vnugnes","start":130,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-03-27T14:21:14.757Z","reference_source":"pmid","term_name":"disorder","reference_id":"17319698","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"CD experiments for the whole protein show a high disordered content that disappear when the N-terminal and C-terminal domains are assessed alone. This indicates that the linker region is disordered.","type":"Curator statement"}]},{"start":130,"end":173,"reference_id":"17319698","reference_source":"pmid","reference_html":"Structural and functional analysis of ProQ: an osmoregulatory protein of Escherichia coli. <i> Smith MN, Kwok SC, Hodges RS, Wood JM. </i> Biochemistry, 2007","date":"2024-03-27T14:15:25.850Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP00377r004","statement":[{"text":"Thus, limited trypsin digestion of purified ProQ yielded protease resistant fragments corresponding to the predicted N- and C-terminal domains. In contrast, fragments corresponding to predicted tryptic fragments within the linker region (amino acids 130−173) were not found.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_C4ZZI8","date":"2016-09-09T10:57:51.000Z","acc":"P45577","name":"RNA chaperone ProQ","length":232,"organism":"Escherichia coli (strain K12)","dataset":["RNA-binding proteins"],"UniParc":"UPI000016E149","genes":[{"name":{"value":"proQ","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00749","url":"https://hamap.expasy.org/unirule/MF_00749"}}]},"synonyms":[{"value":"yebJ"},{"value":"yobE"},{"value":"yoeC"}],"olnNames":[{"value":"b1831"},{"value":"JW5300"}]}],"alphafold_very_low_content":0.1853448275862069,"disorder_content":0.1896551724137931,"disprot_consensus":{"full":[{"start":130,"end":173,"type":"D"}],"Structural state":[{"start":130,"end":173,"type":"D"}],"Disorder function":[{"start":130,"end":173,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00096","name":"Zinc finger, C2H2 type","start":656,"end":680},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":686,"end":708}],"gene3D":[{"start":653,"end":680,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":681,"end":717,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":617,"end":652,"id":"3.30.160.60","name":"Classic Zinc Finger"}]},"uniref50":"UniRef50_P08047","sequence":"MSDQDHSMDEMTAVVKIEKGVGGNNGGNGNGGGAFSQARSSSTGSSSSTGGGGQESQPSPLALLAATCSRIESPNENSNNSQGPSQSGGTGELDLTATQLSQGANGWQIISSSSGATPTSKEQSGSSTNGSNGSESSKNRTVSGGQYVVAAAPNLQNQQVLTGLPGVMPNIQYQVIPQFQTVDGQQLQFAATGAQVQQDGSGQIQIIPGANQQIITNRGSGGNIIAAMPNLLQQAVPLQGLANNVLSGQTQYVTNVPVALNGNITLLPVNSVSAATLTPSSQAVTISSSGSQESGSQPVTSGTTISSASLVSSQASSSSFFTNANSYSTTTTTSNMGIMNFTTSGSSGTNSQGQTPQRVSGLQGSDALNIQQNQTSGGSLQAGQQKEGEQNQQTQQQQILIQPQLVQGGQALQALQAAPLSGQTFTTQAISQETLQNLQLQAVPNSGPIIIRTPTVGPNGQVSWQTLQLQNLQVQNPQAQTITLAPMQGVSLGQTSSSNTTLTPIASAASIPAGTVTVNAAQLSSMPGLQTINLSALGTSGIQVHPIQGLPLAIANAPGDHGAQLGLHGAGGDGIHDDTAGGEEGENSPDAQPQAGRRTRREACTCPYCKDSEGRGSGDPGKKKQHICHIQGCGKVYGKTSHLRAHLRWHTGERPFMCTWSYCGKRFTRSDELQRHKRTHTGEKKFACPECPKRFMRSDHLSKHIKTHQNKKGGPGVALSVGTLPLDSGAGSEGSGTATPSALITTNMVAMEAICPEGIARLANSGINVMQVADLQSINISGNGF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P08047","disprot_id":"DP00378","ncbi_taxon_id":9606,"regions_counter":20,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":488,"region_id":"DP00378r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Interaction between isolated transcriptional activation domains of Sp1 revealed by heteronuclear magnetic resonance. <i> Hiramatsu N, Hibino E, Matsuzaki K, Kuwahara J, Hoshino M. </i> Protein Sci, 2012","term_id":"IDPO:0000002","curator_id":"jpujols","start":342,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22855260","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":488,"region_id":"DP00378r002","released":"2022_03","ec_id":"ECO:0006275","reference_html":"Interaction between isolated transcriptional activation domains of Sp1 revealed by heteronuclear magnetic resonance. <i> Hiramatsu N, Hibino E, Matsuzaki K, Kuwahara J, Hoshino M. </i> Protein Sci, 2012","term_id":"IDPO:0000002","curator_id":"jpujols","start":342,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"analytical ultracentrifugation evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22855260","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":488,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"analytical ultracentrifugation evidence used in manual assertion","reference_html":"Interaction between isolated transcriptional activation domains of Sp1 revealed by heteronuclear magnetic resonance. <i> Hiramatsu N, Hibino E, Matsuzaki K, Kuwahara J, Hoshino M. </i> Protein Sci, 2012","term_id":"GO:0060090","curator_id":"jpujols","start":342,"term_ontology":"GO","curator_name":"Jordi Pujols Pujol","reference_id":"22855260","version":3,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006275","region_id":"DP00378r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":488,"term_name":"protein binding","released":"2022_03","ec_name":"analytical ultracentrifugation evidence used in manual assertion","reference_html":"Interaction between isolated transcriptional activation domains of Sp1 revealed by heteronuclear magnetic resonance. <i> Hiramatsu N, Hibino E, Matsuzaki K, Kuwahara J, Hoshino M. </i> Protein Sci, 2012","term_id":"GO:0005515","curator_id":"jpujols","start":342,"term_ontology":"GO","curator_name":"Jordi Pujols Pujol","reference_id":"22855260","version":3,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006275","region_id":"DP00378r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":488,"region_id":"DP00378r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Interaction between isolated transcriptional activation domains of Sp1 revealed by heteronuclear magnetic resonance. <i> Hiramatsu N, Hibino E, Matsuzaki K, Kuwahara J, Hoshino M. </i> Protein Sci, 2012","term_id":"IDPO:0000002","curator_id":"jpujols","start":342,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22855260","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":215,"region_id":"DP00378r006","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Interaction between intrinsically disordered regions in transcription factors Sp1 and TAF4. <i> Hibino E, Inoue R, Sugiyama M, Kuwahara J, Matsuzaki K, Hoshino M. </i> Protein Sci, 2016","term_id":"IDPO:0000002","curator_id":"jpujols","start":153,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27515574","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":215,"region_id":"DP00378r007","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Interaction between intrinsically disordered regions in transcription factors Sp1 and TAF4. <i> Hibino E, Inoue R, Sugiyama M, Kuwahara J, Matsuzaki K, Hoshino M. </i> Protein Sci, 2016","term_id":"IDPO:0000002","curator_id":"jpujols","start":153,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27515574","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":215,"region_id":"DP00378r008","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Interaction between intrinsically disordered regions in transcription factors Sp1 and TAF4. <i> Hibino E, Inoue R, Sugiyama M, Kuwahara J, Matsuzaki K, Hoshino M. </i> Protein Sci, 2016","term_id":"IDPO:0000002","curator_id":"jpujols","start":153,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27515574","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":215,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Interaction between intrinsically disordered regions in transcription factors Sp1 and TAF4. <i> Hibino E, Inoue R, Sugiyama M, Kuwahara J, Matsuzaki K, Hoshino M. </i> Protein Sci, 2016","term_id":"GO:0005515","curator_id":"jpujols","start":153,"term_ontology":"GO","curator_name":"Jordi Pujols Pujol","reference_id":"27515574","version":3,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00378r009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":495,"region_id":"DP00378r010","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Interaction between intrinsically disordered regions in transcription factors Sp1 and TAF4. <i> Hibino E, Inoue R, Sugiyama M, Kuwahara J, Matsuzaki K, Hoshino M. </i> Protein Sci, 2016","term_id":"IDPO:0000002","curator_id":"jpujols","start":349,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27515574","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":495,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Interaction between intrinsically disordered regions in transcription factors Sp1 and TAF4. <i> Hibino E, Inoue R, Sugiyama M, Kuwahara J, Matsuzaki K, Hoshino M. </i> Protein Sci, 2016","term_id":"GO:0005515","curator_id":"jpujols","start":349,"term_ontology":"GO","curator_name":"Jordi Pujols Pujol","reference_id":"27515574","version":3,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00378r011","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":495,"region_id":"DP00378r012","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Interaction between intrinsically disordered regions in transcription factors Sp1 and TAF4. <i> Hibino E, Inoue R, Sugiyama M, Kuwahara J, Matsuzaki K, Hoshino M. </i> Protein Sci, 2016","term_id":"IDPO:0000002","curator_id":"jpujols","start":349,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27515574","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":495,"region_id":"DP00378r013","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Interaction between intrinsically disordered regions in transcription factors Sp1 and TAF4. <i> Hibino E, Inoue R, Sugiyama M, Kuwahara J, Matsuzaki K, Hoshino M. </i> Protein Sci, 2016","term_id":"IDPO:0000002","curator_id":"jpujols","start":349,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27515574","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P08047","date":"2016-09-12T12:31:37.000Z","acc":"P08047","name":"Transcription factor Sp1","length":785,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000016B0B8","genes":[{"name":{"value":"SP1"},"synonyms":[{"value":"TSFP1"}]}],"alphafold_very_low_content":0.8726114649681529,"disorder_content":0.2764331210191083,"disprot_consensus":{"full":[{"start":153,"end":215,"type":"D"},{"start":342,"end":495,"type":"D"}],"Structural state":[{"start":153,"end":215,"type":"D"},{"start":342,"end":495,"type":"D"}],"Molecular function":[{"start":153,"end":215,"type":"F"},{"start":342,"end":495,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00111","name":"2Fe-2S iron-sulfur cluster binding domain","start":10,"end":87},{"id":"PF00175","name":"Oxidoreductase NAD-binding domain","start":220,"end":324},{"id":"PF00970","name":"Oxidoreductase FAD-binding domain","start":119,"end":208}],"gene3D":[{"start":208,"end":348,"id":"3.40.50.80","name":"Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module"},{"start":1,"end":98,"id":"3.10.20.30","name":"3.10.20.30"},{"start":99,"end":206,"id":"2.40.30.10","name":"Translation factors"}]},"uniref50":"UniRef50_P22868","sequence":"MQRVHTITAVTEDGESLRFECRSDEDVITAALRQNIFLMSSCREGGCATCKALCSEGDYDLKGCSVQALPPEEEEEGLVLLCRTYPKTDLEIELPYTHCRISFGEVGSFEAEVVGLNWVSSNTVQFLLQKRPDECGNRGVKFEPGQFMDLTIPGTDVSRSYSPANLPNPEGRLEFLIRVLPEGRFSDYLRNDARVGQVLSVKGPLGVFGLKERGMAPRYFVAGGTGLAPVVSMVRQMQEWTAPNETRIYFGVNTEPELFYIDELKSLERSMRNLTVKACVWHPSGDWEGEQGSPIDALREDLESSDANPDIYLCGPPGMIDAACELVRSRGIPGEQVFFEKFLPSGAA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Methylococcales","Methylococcaceae","Methylococcus"],"uniref90":"UniRef90_P22868","disprot_id":"DP00379","ncbi_taxon_id":243233,"regions_counter":4,"creator":"eleonardi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":172,"region_id":"DP00379r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR structure of the flavin domain from soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath). <i> Chatwood LL, Müller J, Gross JD, Wagner G, Lippard SJ. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"eleonardi","start":163,"term_ontology":"IDPO","curator_name":"Emanuela Leonardi","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1TVC:A"}],"reference_id":"15379538","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":146,"region_id":"DP00379r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR structure of the flavin domain from soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath). <i> Chatwood LL, Müller J, Gross JD, Wagner G, Lippard SJ. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"eleonardi","start":131,"term_ontology":"IDPO","curator_name":"Emanuela Leonardi","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1TVC:A"}],"reference_id":"15379538","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P22868","date":"2016-09-09T16:02:12.000Z","acc":"P22868","name":"Methane monooxygenase component C","length":348,"organism":"Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)","dataset":[],"UniParc":"UPI0000171D41","genes":[{"name":{"value":"mmoC"},"olnNames":[{"value":"MCA1200"}]}],"alphafold_very_low_content":0.011494252873563218,"disorder_content":0.07471264367816093,"disprot_consensus":{"full":[{"start":131,"end":146,"type":"D"},{"start":163,"end":172,"type":"D"}],"Structural state":[{"start":131,"end":146,"type":"D"},{"start":163,"end":172,"type":"D"}]}},{"features":{"pfam":[{"id":"PF08951","name":"Bacteriocin immunity protein family","start":4,"end":84}],"gene3D":[{"start":1,"end":111,"id":"1.20.1440.50","name":"Ta0600-like"}]},"uniref50":"UniRef50_P38582","sequence":"MDIKSQTLYLNLSEAYKDPEVKANEFLSKLVVQCAGKLTASNSENSYIEVISLLSRGISSYYLSHKRIIPSSMLTIYTQIQKDIKNGNIDTEKLRKYEIAKGLMSVPYIYF","taxonomy":["Bacteria","Firmicutes","Bacilli","Lactobacillales","Carnobacteriaceae","Carnobacterium"],"uniref90":"UniRef90_P38582","disprot_id":"DP00380","dataset":["Unicellular toxins and antitoxins"],"ncbi_taxon_id":2751,"regions_counter":5,"creator":"sventura","regions":[{"region_id":"DP00380r005","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T15:02:31.207Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":69,"term_id":"IDPO:0000002","start":59,"version":2,"statement":[{"text":"Bacteriocins produced by lactic acid bacteria are potent antimicrobial compounds which are active against closely related bacteria. Producer strains are protected against the effects of their cognate bacteriocins by immunity proteins. However, to date, no structures are available for the corresponding immunity proteins. We report here the NMR solution structure of the 111-amino acid immunity protein for carnobacteriocin B2 (ImB2).","type":"Abstract"},{"text":"Most of the charged and polar residues in the protein face the solvent. Helix 3 is well-defined to residue 55, and a stretch of nascent helix followed by an unstructured loop joins it to helix 4. The loop between helices 3 and 4, and a hydrophobic pocket which it partially masks, may be important for interaction with membrane receptors responsible for sensitivity to class IIa bacteriocins","type":"Results"},{"text":"Amide cross-peaks were broad and weak for residues 56, 58, 65, 66, 69, and 73 and either overlapped or missing for residues 62, 63, 67, 68, and 74 in 15N HSQC spectra. Some of the side chain 1 H-13C cross-peaks for these residues were also not observed in 13C HSQC spectra. Side chain assignments for residues 55, 59, 62, 67, 68, and 71 were partially determined. Higher temperature (28 °C vs 15 °C) resulted in further broadening of the amide cross-peaks in this region and allowed even fewer assignments to be made. Only intraresidue or i + 1 NOEs were observed for 10 of the 20 amino acid residues in this small section of the protein, which is relatively unstructured and forms a conformationally flexible section (see below).\n\nBecause of a lack of NOE data, helix 3 is well defined until only S55 (see below). The nascent helical structure in this region may be forming and dissociating on the NMR time scale, resulting in averaging of chemical shifts and broad peaks that cannot be observed\n\nAs mentioned above, helix 3 is well-defined to residue S55, and NOEs indicative of helical structure are observed to residue I58. From residues 58-71, a relatively unstructured loop is apparent. Data indicate a nascent helix structure can be present up to residue 64. This region may be important for binding a putative receptor in the cell membrane (see below).","type":"Results"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"15362858","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1TDP"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"lchemes","reference_html":"NMR solution structure of ImB2, a protein conferring immunity to antimicrobial activity of the type IIa bacteriocin, carnobacteriocin B2. <i> Sprules T, Kawulka KE, Vederas JC. </i> Biochemistry, 2004","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P38582","date":"2016-09-18T21:40:34.000Z","acc":"P38582","name":"Putative carnobacteriocin-B2 immunity protein","length":111,"organism":"Carnobacterium maltaromaticum","UniParc":"UPI0000127149","genes":[],"alphafold_very_low_content":0,"disorder_content":0.0990990990990991,"disprot_consensus":{"full":[{"start":59,"end":69,"type":"D"}],"Structural state":[{"start":59,"end":69,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00010","name":"Helix-loop-helix DNA-binding domain","start":37,"end":78},{"id":"PF00989","name":"PAS fold","start":114,"end":226},{"id":"PF08447","name":"PAS fold","start":300,"end":382}],"gene3D":[{"start":31,"end":81,"id":"4.10.280.10","name":"Helix-loop-helix DNA-binding domain"},{"start":110,"end":273,"id":"3.30.450.20","name":"PAS domain"},{"start":277,"end":392,"id":"3.30.450.20","name":"PAS domain"}]},"uniref50":"UniRef50_P30561","sequence":"MNSSSANITYASRKRRKPVQKTVKPIPAEGIKSNPSKRHRDRLNTELDRLASLLPFPQDVINKLDKLSVLRLSVSYLRAKSFFDVALKSSPTERNGGQDNCRAANFREGLNLQEGEFLLQALNGFVLVVTTDALVFYASSTIQDYLGFQQSDVIHQSVYELIHTEDRAEFQRQLHWALNPSQCTESGQGIEEATGLPQTVVCYNPDQIPPENSPLMERCFICRLRCLLDNSSGFLAMNFQGKLKYLHGQKKKGKDGSILPPQLALFAIATPLQPPSILEIRTKNFIFRTKHKLDFTPIGCDAKGRIVLGYTEAELCTRGSGYQFIHAADMLYCAESHIRMIKTGESGMIVFRLLTKNNRWTWVQSNARLLYKNGRPDYIIVTQRPLTDEEGTEHLRKRNTKLPFMFTTGEAVLYEATNPFPAIMDPLPLRTKNGTSGKDSATTSTLSKDSLNPSSLLAAMMQQDESIYLYPASSTSSTAPFENNFFNESMNECRNWQDNTAPMGNDTILKHEQIDQPQDVNSFAGGHPGLFQDSKNSDLYSIMKNLGIDFEDIRHMQNEKFFRNDFSGEVDFRDIDLTDEILTYVQDSLSKSPFIPSDYQQQQSLALNSSCMVQEHLHLEQQQQHHQKQVVVEPQQQLCQKMKHMQVNGMFENWNSNQFVPFNCPQQDPQQYNVFTDLHGISQEFPYKSEMDSMPYTQNFISCNQPVLPQHSKCTELDYPMGSFEPSPYPTTSSLEDFVTCLQLPENQKHGLNPQSAIITPQTCYAGAVSMYQCQPEPQHTHVGQMQYNPVLPGQQAFLNKFQNGVLNETYPAELNNINNTQTTTHLQPLHHPSEARPFPDLTSSGFL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P35869","disprot_id":"DP00381","ncbi_taxon_id":9606,"regions_counter":13,"creator":"aelofsson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":713,"region_id":"DP00381r001","released":"2022_12","ec_id":"ECO:0006204","reference_html":"Induced alpha-helix structure in the aryl hydrocarbon receptor transactivation domain modulates protein-protein interactions. <i> Watt K, Jess TJ, Kelly SM, Price NC, McEwan IJ. </i> Biochemistry, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":545,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-30T19:17:42.943Z","reference_source":"pmid","term_name":"disorder","reference_id":"15641800","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The spectra are very similar and are dominated by the minimum at around 200 nm, which is indicative of polypeptides with significant nonordered structure.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":713,"region_id":"DP00381r005","released":"2022_12","ec_id":"ECO:0007691","reference_html":"Induced alpha-helix structure in the aryl hydrocarbon receptor transactivation domain modulates protein-protein interactions. <i> Watt K, Jess TJ, Kelly SM, Price NC, McEwan IJ. </i> Biochemistry, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":545,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-30T19:15:54.193Z","reference_source":"pmid","term_name":"disorder","reference_id":"15641800","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"Figure 6 shows that in the absence of TMAO the AhR−AB polypeptide is extremely sensitive to digestion with chymotrypsin with no clear ladder of fragments observed and no full-length polypeptide remaining after 5 min.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":713,"region_id":"DP00381r009","released":"2022_12","ec_id":"ECO:0001249","reference_html":"Induced alpha-helix structure in the aryl hydrocarbon receptor transactivation domain modulates protein-protein interactions. <i> Watt K, Jess TJ, Kelly SM, Price NC, McEwan IJ. </i> Biochemistry, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":545,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"fluorescence evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-30T19:14:18.148Z","reference_source":"pmid","term_name":"disorder","reference_id":"15641800","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":" After excitation at 278 nm, the main features observed are a λmax for tryptophan emission at 344 nm (average of 343 ± 2 nm, n = 7) and a shoulder at 307 nm for tyrosine (Figure 4A).","type":"Results"},{"text":"The emission spectra for the soluble and refolded AhR TAD polypeptides were essentially indistinguishable (Figure 4B) (see also below). Taken together, these results suggest that removal of the denaturant, urea, leads to folding of the AhR−AB polypeptide into a relatively open conformation that is intrinsic to the polypeptide and not a consequence of the purification process.","type":"Results"}]},{"start":545,"end":713,"reference_id":"15641800","reference_source":"pmid","reference_html":"Induced alpha-helix structure in the aryl hydrocarbon receptor transactivation domain modulates protein-protein interactions. <i> Watt K, Jess TJ, Kelly SM, Price NC, McEwan IJ. </i> Biochemistry, 2005","date":"2022-08-30T19:31:15.788Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0001094","term_name":"TFIID-class transcription factor complex binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006076","ec_ontology":"ECO","ec_name":"protein binding evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P20226","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"O00268","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P49848","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP00381r013","statement":[{"text":"Figure 2 (panels A and B) confirms the interaction with the TBP and also shows interactions with TAF4 and TAF6, other components of the TFIID complex.","type":"Results"},{"text":"Virtually the same levels of TBP binding were observed no matter the method of AhR−AB purification (Figure 2C).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a general RNA polymerase II transcription factor belonging to the TFIID complex, one of the factors involved in formation of the preinitiation complex (PIC) by RNA polymerase II.\" [GOC:krc, PMID:16858867]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_P35869","date":"2016-09-06T15:42:42.000Z","acc":"P35869","name":"Aryl hydrocarbon receptor","length":848,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000151E80","genes":[{"name":{"value":"AHR","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8393992","url":"http://www.ncbi.nlm.nih.gov/pubmed/8393992","alternativeUrl":"https://europepmc.org/abstract/MED/8393992"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:348","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:348"}}]},"synonyms":[{"value":"BHLHE76","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:348","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:348"}}]}]}],"alphafold_very_low_content":0.5507075471698113,"disorder_content":0.19929245283018868,"disprot_consensus":{"full":[{"start":545,"end":713,"type":"D"}],"Structural state":[{"start":545,"end":713,"type":"D"}],"Molecular function":[{"start":545,"end":713,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01868","name":"Ribonuclease P/MRP, subunit p29","start":9,"end":89}],"gene3D":[{"start":1,"end":102,"id":"2.30.30.210","name":"Ribonuclease P/MRP, subunit p29"}]},"uniref50":"UniRef50_O28362","sequence":"MRGRLQGVELIARDWIGLMVEVVESPNHSEVGIKGEVVDETQNTLKIMTEKGLKVVAKRGRTFRVWYKGKIMRIKGDLINFRPEDRIKRGLMMLKRAKGVWI","taxonomy":["Archaea","Euryarchaeota","Archaeoglobi","Archaeoglobales","Archaeoglobaceae","Archaeoglobus"],"uniref90":"UniRef90_O28362","disprot_id":"DP00382","ncbi_taxon_id":224325,"regions_counter":9,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":16,"region_id":"DP00382r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Crystal structure of archaeal ribonuclease P protein aRpp29 from Archaeoglobus fulgidus. <i> Sidote DJ, Heideker J, Hoffman DW. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15518563","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":16,"term_name":"disorder to order","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15518563","version":2,"reference_html":"Crystal structure of archaeal ribonuclease P protein aRpp29 from Archaeoglobus fulgidus. <i> Sidote DJ, Heideker J, Hoffman DW. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00382r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":102,"region_id":"DP00382r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Crystal structure of archaeal ribonuclease P protein aRpp29 from Archaeoglobus fulgidus. <i> Sidote DJ, Heideker J, Hoffman DW. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"mnecci","start":79,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15518563","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":102,"term_name":"disorder to order","start":79,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15518563","version":2,"reference_html":"Crystal structure of archaeal ribonuclease P protein aRpp29 from Archaeoglobus fulgidus. <i> Sidote DJ, Heideker J, Hoffman DW. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00382r004","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":16,"region_id":"DP00382r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Crystal structure of archaeal ribonuclease P protein aRpp29 from Archaeoglobus fulgidus. <i> Sidote DJ, Heideker J, Hoffman DW. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15518563","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":16,"term_name":"disorder to order","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15518563","version":2,"reference_html":"Crystal structure of archaeal ribonuclease P protein aRpp29 from Archaeoglobus fulgidus. <i> Sidote DJ, Heideker J, Hoffman DW. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00382r006","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":102,"term_name":"disorder to order","start":79,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15518563","version":2,"reference_html":"Crystal structure of archaeal ribonuclease P protein aRpp29 from Archaeoglobus fulgidus. <i> Sidote DJ, Heideker J, Hoffman DW. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00382r008","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2016_10","uniref100":"UniRef100_O28362","date":"2016-09-06T12:36:37.000Z","acc":"O28362","name":"Ribonuclease P protein component 1","length":102,"organism":"Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)","dataset":[],"UniParc":"UPI0000056B4B","genes":[{"name":{"value":"rnp1","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00754","url":"https://hamap.expasy.org/unirule/MF_00754"}}]},"olnNames":[{"value":"AF_1917"}]}],"alphafold_very_low_content":0,"disorder_content":0.39215686274509803,"disprot_consensus":{"full":[{"start":1,"end":16,"type":"T"},{"start":79,"end":102,"type":"T"}],"Structural state":[{"start":1,"end":16,"type":"D"},{"start":79,"end":102,"type":"D"}],"Structural transition":[{"start":1,"end":16,"type":"T"},{"start":79,"end":102,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00505","name":"HMG (high mobility group) box","start":95,"end":163},{"id":"PF09011","name":"HMG-box domain","start":6,"end":78}],"gene3D":[{"start":81,"end":166,"id":"1.10.30.10","name":"High mobility group box domain"},{"start":1,"end":80,"id":"1.10.30.10","name":"High mobility group box domain"}]},"uniref50":"UniRef50_P63158","sequence":"MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEDDEEDEEDEEEEEEEEDEDEEEDDDDE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P63158","disprot_id":"DP00384","ncbi_taxon_id":10090,"regions_counter":12,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":90,"region_id":"DP00384r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes. <i> Knapp S, Müller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"fquaglia","start":81,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15379539","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":90,"term_name":"nucleic acid binding","start":81,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15379539","version":3,"reference_html":"The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes. <i> Knapp S, Müller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006165","region_id":"DP00384r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":184,"region_id":"DP00384r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes. <i> Knapp S, Müller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"fquaglia","start":166,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15379539","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":184,"term_name":"nucleic acid binding","start":166,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15379539","version":3,"reference_html":"The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes. <i> Knapp S, Müller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006165","region_id":"DP00384r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":90,"region_id":"DP00384r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes. <i> Knapp S, Müller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"fquaglia","start":81,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15379539","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":90,"term_name":"nucleic acid binding","start":81,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15379539","version":3,"reference_html":"The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes. <i> Knapp S, Müller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006204","region_id":"DP00384r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":215,"region_id":"DP00384r007","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes. <i> Knapp S, Müller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"fquaglia","start":185,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15379539","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":215,"term_name":"nucleic acid binding","start":185,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15379539","version":3,"reference_html":"The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes. <i> Knapp S, Müller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006165","region_id":"DP00384r008","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":184,"region_id":"DP00384r009","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes. <i> Knapp S, Müller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"fquaglia","start":166,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15379539","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":184,"term_name":"nucleic acid binding","start":166,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15379539","version":3,"reference_html":"The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes. <i> Knapp S, Müller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006204","region_id":"DP00384r010","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":215,"region_id":"DP00384r011","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes. <i> Knapp S, Müller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"fquaglia","start":185,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15379539","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":215,"term_name":"nucleic acid binding","start":185,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15379539","version":3,"reference_html":"The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes. <i> Knapp S, Müller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006204","region_id":"DP00384r012","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P63158","date":"2016-08-23T11:04:11.000Z","acc":"P63158","name":"High mobility group protein B1","length":215,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000008A6","genes":[{"name":{"value":"Hmgb1"},"synonyms":[{"value":"Hmg-1"},{"value":"Hmg1"}]}],"alphafold_very_low_content":0.2186046511627907,"disorder_content":0.27906976744186046,"disprot_consensus":{"full":[{"start":81,"end":90,"type":"D"},{"start":166,"end":215,"type":"D"}],"Structural state":[{"start":81,"end":90,"type":"D"},{"start":166,"end":215,"type":"D"}],"Molecular function":[{"start":81,"end":90,"type":"F"},{"start":166,"end":215,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":56,"end":340}],"gene3D":[{"start":137,"end":383,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"},{"start":40,"end":136,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"}]},"uniref50":"UniRef50_P49841","sequence":"MSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALFNFTTQELSSNPPLATILIPPHARIQAAASTPTNATAASDANTGDRGQTNNAASASASNST","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P49841","disprot_id":"DP00385","ncbi_taxon_id":9606,"regions_counter":13,"creator":"eleonardi","regions":[{"term_namespace":"Disorder function","ec_ontology":"ECO","end":392,"region_id":"DP00385r002","released":"2024_12","ec_id":"ECO:0001202","reference_html":"Phosphorylation by p38 MAPK as an alternative pathway for GSK3beta inactivation. <i> Thornton TM, Pedraza-Alva G, Deng B, Wood CD, Aronshtam A, Clements JL, Sabio G, Davis RJ, Matthews DE, Doble B, Rincon M. </i> Science, 2008","term_id":"IDPO:0000045","curator_id":"vnugnes","start":388,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"in vitro protein kinase assay evidence used in manual assertion","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2024-12-09T14:13:23.444Z","reference_source":"pmid","term_name":"phosphorylation display site","reference_id":"18451303","ec_go":"EXP","disprot_namespace":"Disorder function","statement":[{"text":"Thus, Thr390 of GSK3β appears to be specifically phosphorylated by p38 MAPK.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":34,"region_id":"DP00385r003","released":"2024_12","ec_id":"ECO:0006220","reference_html":"Structural characterization of the GSK-3beta active site using selective and non-selective ATP-mimetic inhibitors. <i> Bertrand JA, Thieffine S, Vulpetti A, Cristiani C, Valsasina B, Knapp S, Kalisz HM, Flocco M. </i> J Mol Biol, 2003","term_id":"IDPO:0000002","curator_id":"eleonardi","start":1,"term_ontology":"IDPO","curator_name":"Emanuela Leonardi","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8486-8461","date":"2024-12-08T09:15:44.973Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1Q4L"}],"reference_id":"14529625","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Several sections of the\nstructure lacked interpretable electron density,\nindicating a high degree of disorder. These include\nthe N-terminal segment 1–34, the loop 120–124\nand the C-terminal segment 386–420. In addition,\nthe electron density was weak for the region 285–\n295.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-09T12:54:20.977Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":420,"region_id":"DP00385r004","released":"2024_12","ec_id":"ECO:0006220","reference_html":"Structural characterization of the GSK-3beta active site using selective and non-selective ATP-mimetic inhibitors. <i> Bertrand JA, Thieffine S, Vulpetti A, Cristiani C, Valsasina B, Knapp S, Kalisz HM, Flocco M. </i> J Mol Biol, 2003","term_id":"IDPO:0000002","curator_id":"eleonardi","start":386,"term_ontology":"IDPO","curator_name":"Emanuela Leonardi","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8486-8461","date":"2024-12-08T09:13:29.964Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1Q41"}],"reference_id":"14529625","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Several sections of the structure lacked interpretable electron density,\nindicating a high degree of disorder. These include\nthe N-terminal segment 1–34, the loop 120–124\nand the C-terminal segment 386–420. In addition,\nthe electron density was weak for the region 285–\n295.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-09T12:54:20.499Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":300,"region_id":"DP00385r005","released":"2024_12","ec_id":"ECO:0006220","reference_html":"Design, Structure-Activity Relationships, and In Vivo Evaluation of Potent and Brain-Penetrant Imidazo[1,2-<i>b</i>]pyridazines as Glycogen Synthase Kinase-3β (GSK-3β) Inhibitors. <i> Hartz RA, Ahuja VT, Sivaprakasam P, Xiao H, Krause CM, Clarke WJ, Kish K, Lewis H, Szapiel N, Ravirala R, Mutalik S, Nakmode D, Shah D, Burton CR, Macor JE, Dubowchik GM. </i> J Med Chem, 2023","term_id":"IDPO:0000002","curator_id":"vnugnes","start":285,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2024-12-09T14:09:54.967Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"8DJC"}],"reference_id":"36950863","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"This region lacks electron density in the PDB structure of GSK-3 in complex with A inhibitor 13, indicating it is disordered.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"134551592"}]},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":16,"term_name":"palmitoylation display site","released":"2024_12","ec_name":"mass spectrometry evidence used in manual assertion","reference_html":"GSK3β palmitoylation mediated by ZDHHC4 promotes tumorigenicity of glioblastoma stem cells in temozolomide-resistant glioblastoma through the EZH2-STAT3 axis. <i> Zhao C, Yu H, Fan X, Niu W, Fan J, Sun S, Gong M, Zhao B, Fang Z, Chen X. </i> Oncogenesis, 2022","term_id":"IDPO:0000044","curator_id":"eleonardi","start":12,"term_ontology":"IDPO","curator_name":"Emanuela Leonardi","reference_id":"35606353","version":3,"curator_orcid":"0000-0001-8486-8461","date":"2024-12-08T14:59:27.316Z","reference_source":"pmid","ec_id":"ECO:0001230","region_id":"DP00385r006","ec_go":"EXP","disprot_namespace":"Disorder function","statement":[{"text":"We identified palmitoylation of GSK3β using ABE and\nfound that both the GSK3β mutant (cysteine 14 mutated to\nalanine) and the siRNA silencing of ZDHHC4 made GSK3β\npalmitoylation significantly reduced in SF126 GBM cells, similar\nto the U118MG cell line (Fig. 1E; Supplementary Fig. 1B, C).","type":"Results"},{"text":"Here, we found that GSK3β was noted as a substrate for ZDHHC4-mediated palmitoylation at the Cys14\nresidue, which enhanced GBM temozolomide (TMZ) resistance and GSC self-renewal.","type":"Abstract"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-09T13:49:56.313Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":300,"term_name":"disorder to order","released":"2024_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"The structure of phosphorylated GSK-3beta complexed with a peptide, FRATtide, that inhibits beta-catenin phosphorylation. <i> Bax B, Carter PS, Lewis C, Guy AR, Bridges A, Tanner R, Pettman G, Mannix C, Culbert AA, Brown MJ, Smith DG, Reith AD. </i> Structure, 2001","term_id":"IDPO:0000011","curator_id":"vnugnes","start":285,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"11738041","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2024-12-09T14:23:07.208Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00385r007","ec_go":"EXP","disprot_namespace":"Structural transition","cross_refs":[{"db":"PDB","id":"1GNG"}],"statement":[{"text":"The binding of FRATtide causes a change in the position of residues 286–296 of GSK-3. In crystal form A (without FRATtide), residues 286–296 pack close to and partially cover phenylalanine 229 and the hydrophobic surface of helix G (the 286–296 loop has high temperature factors in crystal form A, suggesting that the packing of Phe 291, Phe 293, and other residues against helix G is not optimal). Upon binding, FRATtide residues 288–294 of GSK-3 move approximately 6 Å away from helix G and open up a hydrophobic groove, between helix G and the 288–294 loop.","type":"Results"},{"text":"Although this region seems to be disordered when the protein is in complex with an inhibitor, when in complex with a peptide derived from the Proto-oncogene FRAT1, it is structured.","type":"Curator statement"}],"construct_alterations":[{"term_id":"MOD:00048","term_name":"O4'-phospho-L-tyrosine","term_namespace":"Non-standard amino acid","start":216,"end":216,"position":"Specific residue"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92837"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46097","entry_name":"Htris"}]},{"start":19,"end":23,"reference_id":"11035810","reference_source":"pmid","reference_html":"Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinase A. <i> Fang X, Yu SX, Lu Y, Bast RC, Woodgett JR, Mills GB. </i> Proc Natl Acad Sci U S A, 2000","date":"2024-12-09T14:24:58.039Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001202","ec_ontology":"ECO","ec_name":"in vitro protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":1,"region_id":"DP00385r010","statement":[{"text":"We demonstrate that serine 21 in GSK-3α and serine 9 in GSK-3β are also physiological substrates of cAMP-dependent protein kinase A (PKA).","type":"Article"}]},{"start":3,"end":12,"reference_id":"12434148","reference_source":"pmid","reference_html":"Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP. <i> Yang J, Cron P, Good VM, Thompson V, Hemmings BA, Barford D. </i> Nat Struct Biol, 2002","date":"2024-12-07T14:34:35.278Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"1O6L"}],"region_id":"DP00385r011","statement":[{"text":"To understand the mechanism of PKB regulation, we determined the crystal structures of activated kinase domains of PKB in complex with a GSK3beta-peptide substrate and an ATP analog.","type":"Abstract"},{"text":"The crystals were grown at 20 °C by\nmixing the protein solution (10 mg ml–1 PKB, 5 mM AMPPNP–\nMnCl2 and 0.6 mM GSK3β-peptide (GRPRTTSFAE)) with a\ncrystallization solution of 20% (w/v) PEG 4000, 10% (v/v) isopropanol,\n0.1 M HEPES, pH 7.5 and 5 mM dithiothreitol in a micro\nbatch under oil.","type":"Methods"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P31751","operator":null,"partner_start":null,"partner_end":null}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-09T13:40:15.234Z"}},{"start":285,"end":299,"reference_id":"11738041","reference_source":"pmid","reference_html":"The structure of phosphorylated GSK-3beta complexed with a peptide, FRATtide, that inhibits beta-catenin phosphorylation. <i> Bax B, Carter PS, Lewis C, Guy AR, Bridges A, Tanner R, Pettman G, Mannix C, Culbert AA, Brown MJ, Smith DG, Reith AD. </i> Structure, 2001","date":"2024-12-08T10:00:57.545Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001171","ec_ontology":"ECO","ec_name":"crystallography evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"1GNG"}],"ec_go":"EXP","region_id":"DP00385r012","statement":[{"text":"The crystal structures of apo GSK-3β (crystal form A) and of GSK-3β complexed with the 39mer peptide FRATtide and a sulphate ion (crystal form FS) were determined and refined to 2.9 Å and 2.6 Å, respectively (see Experimental Procedures for details).","type":"Results"},{"text":"The binding of FRATtide causes a change in the position of residues 286–296 of GSK-3. In crystal form A (without FRATtide), residues 286–296 pack close to and partially cover phenylalanine 229 and the hydrophobic surface of helix G (the 286–296 loop has high temperature factors in crystal form A, suggesting that the packing of Phe 291, Phe 293, and other residues against helix G is not optimal). Upon binding, FRATtide residues 288–294 of GSK-3 move approximately 6 Å away from helix G and open up a hydrophobic groove, between helix G and the 288–294 loop.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"Q92837","operator":"and","partner_start":198,"partner_end":220}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-09T14:14:26.080Z"}},{"start":7,"end":11,"reference_id":"1035810","reference_source":"pmid","reference_html":"[Kinetic studies of platelets labeled with 51Cr (author's transl)]. <i> Mezzano D, Foradori A, Lira P, Grebe G, Vergara M. </i> Rev Med Chil, 1976","date":"2024-12-09T14:26:02.957Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001202","ec_ontology":"ECO","ec_name":"in vitro protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP00385r013","statement":[{"text":"We demonstrate that serine 21 in GSK-3α and serine 9 in GSK-3β are also physiological substrates of cAMP-dependent protein kinase A (PKA).","type":"Article"}]}],"released":"2016_10","uniref100":"UniRef100_P49841","date":"2016-09-10T16:59:13.000Z","acc":"P49841","name":"Glycogen synthase kinase-3 beta","length":420,"organism":"Homo sapiens","dataset":["Age-related disorders proteins"],"UniParc":"UPI000004E93D","genes":[{"name":{"value":"GSK3B"}}],"alphafold_very_low_content":0.12380952380952381,"disorder_content":0.20238095238095238,"disprot_consensus":{"full":[{"start":1,"end":34,"type":"D"},{"start":285,"end":300,"type":"T"},{"start":386,"end":420,"type":"D"}],"Structural state":[{"start":1,"end":34,"type":"D"},{"start":285,"end":300,"type":"D"},{"start":386,"end":420,"type":"D"}],"Disorder function":[{"start":7,"end":16,"type":"F"},{"start":19,"end":23,"type":"F"},{"start":388,"end":392,"type":"F"}],"Structural transition":[{"start":285,"end":300,"type":"T"}],"Molecular function":[{"start":3,"end":12,"type":"F"},{"start":285,"end":299,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00825","name":"Ribonuclease P","start":1,"end":106}],"gene3D":[{"start":1,"end":116,"id":"3.30.230.10","name":"3.30.230.10"}]},"uniref50":"UniRef50_P25814","sequence":"MKKRNRLKKNEDFQKVFKHGTSVANRQFVLYTLDQPENDELRVGLSVSKKIGNAVMRNRIKRLIRQAFLEEKERLKEKDYIIIARKPASQLTYEETKKSLQHLFRKSSLYKKSSSK","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Bacillus"],"uniref90":"UniRef90_P25814","disprot_id":"DP00387","ncbi_taxon_id":224308,"regions_counter":16,"creator":"droche","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":116,"region_id":"DP00387r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Linked folding and anion binding of the Bacillus subtilis ribonuclease P protein. <i> Henkels CH, Kurz JC, Fierke CA, Oas TG. </i> Biochemistry, 2001","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11258888","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":116,"term_name":"molecular adaptor activity","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11258888","version":3,"reference_html":"Linked folding and anion binding of the Bacillus subtilis ribonuclease P protein. <i> Henkels CH, Kurz JC, Fierke CA, Oas TG. </i> Biochemistry, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP00387r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":116,"term_name":"disorder to order","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11258888","version":2,"reference_html":"Linked folding and anion binding of the Bacillus subtilis ribonuclease P protein. <i> Henkels CH, Kurz JC, Fierke CA, Oas TG. </i> Biochemistry, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00387r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":116,"term_name":"DNA binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11258888","version":3,"reference_html":"Linked folding and anion binding of the Bacillus subtilis ribonuclease P protein. <i> Henkels CH, Kurz JC, Fierke CA, Oas TG. </i> Biochemistry, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003677","ec_id":"ECO:0006165","region_id":"DP00387r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":116,"region_id":"DP00387r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Linked folding and anion binding of the Bacillus subtilis ribonuclease P protein. <i> Henkels CH, Kurz JC, Fierke CA, Oas TG. </i> Biochemistry, 2001","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11258888","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":116,"term_name":"molecular adaptor activity","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11258888","version":3,"reference_html":"Linked folding and anion binding of the Bacillus subtilis ribonuclease P protein. <i> Henkels CH, Kurz JC, Fierke CA, Oas TG. </i> Biochemistry, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006204","region_id":"DP00387r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":116,"term_name":"disorder to order","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11258888","version":2,"reference_html":"Linked folding and anion binding of the Bacillus subtilis ribonuclease P protein. <i> Henkels CH, Kurz JC, Fierke CA, Oas TG. </i> Biochemistry, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00387r007","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":116,"term_name":"DNA binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11258888","version":3,"reference_html":"Linked folding and anion binding of the Bacillus subtilis ribonuclease P protein. <i> Henkels CH, Kurz JC, Fierke CA, Oas TG. </i> Biochemistry, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003677","ec_id":"ECO:0006204","region_id":"DP00387r008","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":116,"region_id":"DP00387r009","released":"2022_03","ec_id":"ECO:0006206","reference_html":"Linked folding and anion binding of the Bacillus subtilis ribonuclease P protein. <i> Henkels CH, Kurz JC, Fierke CA, Oas TG. </i> Biochemistry, 2001","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11258888","version":2,"ec_name":"near-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":116,"term_name":"molecular adaptor activity","start":1,"ec_name":"near-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11258888","version":3,"reference_html":"Linked folding and anion binding of the Bacillus subtilis ribonuclease P protein. <i> Henkels CH, Kurz JC, Fierke CA, Oas TG. </i> Biochemistry, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006206","region_id":"DP00387r010","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":116,"term_name":"disorder to order","start":1,"ec_name":"near-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11258888","version":2,"reference_html":"Linked folding and anion binding of the Bacillus subtilis ribonuclease P protein. <i> Henkels CH, Kurz JC, Fierke CA, Oas TG. </i> Biochemistry, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006206","region_id":"DP00387r011","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":116,"term_name":"DNA binding","start":1,"ec_name":"near-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11258888","version":3,"reference_html":"Linked folding and anion binding of the Bacillus subtilis ribonuclease P protein. <i> Henkels CH, Kurz JC, Fierke CA, Oas TG. </i> Biochemistry, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003677","ec_id":"ECO:0006206","region_id":"DP00387r012","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":116,"region_id":"DP00387r013","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Ligand concentration regulates the pathways of coupled protein folding and binding. <i> Daniels KG, Tonthat NK, McClure DR, Chang YC, Liu X, Schumacher MA, Fierke CA, Schmidler SC, Oas TG. </i> J Am Chem Soc, 2014","term_id":"IDPO:0000002","curator_id":"droche","start":1,"term_ontology":"IDPO","curator_name":"Daniel Roche","reference_id":"24364358","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4JG4"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":116,"term_name":"DNA binding","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"GO","curator_name":"Daniel Roche","reference_id":"24364358","version":3,"reference_html":"Ligand concentration regulates the pathways of coupled protein folding and binding. <i> Daniels KG, Tonthat NK, McClure DR, Chang YC, Liu X, Schumacher MA, Fierke CA, Schmidler SC, Oas TG. </i> J Am Chem Soc, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003677","ec_id":"ECO:0006220","region_id":"DP00387r014","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":116,"region_id":"DP00387r015","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Ribonuclease P protein structure: evolutionary origins in the translational apparatus. <i> Stams T, Niranjanakumari S, Fierke CA, Christianson DW. </i> Science, 1998","term_id":"IDPO:0000002","curator_id":"droche","start":1,"term_ontology":"IDPO","curator_name":"Daniel Roche","reference_id":"9563955","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1A6F"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":116,"term_name":"DNA binding","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"GO","curator_name":"Daniel Roche","reference_id":"9563955","version":3,"reference_html":"Ribonuclease P protein structure: evolutionary origins in the translational apparatus. <i> Stams T, Niranjanakumari S, Fierke CA, Christianson DW. </i> Science, 1998","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003677","ec_id":"ECO:0006220","region_id":"DP00387r016","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P25814","date":"2016-08-25T14:02:02.000Z","acc":"P25814","name":"Ribonuclease P protein component","length":116,"organism":"Bacillus subtilis (strain 168)","dataset":[],"UniParc":"UPI000016E8FA","genes":[{"name":{"value":"rnpA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00227","url":"https://hamap.expasy.org/unirule/MF_00227"}}]},"olnNames":[{"value":"BSU41050"}]}],"alphafold_very_low_content":0.02586206896551724,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":116,"type":"T"}],"Structural state":[{"start":1,"end":116,"type":"D"}],"Molecular function":[{"start":1,"end":116,"type":"F"}],"Structural transition":[{"start":1,"end":116,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":616,"end":642},{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":750,"end":784},{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":812,"end":841},{"id":"PF02382","name":"N-terminal domain in RTX protein","start":291,"end":599},{"id":"PF08339","name":"RTX C-terminal domain","start":873,"end":999}],"gene3D":[{"start":807,"end":952,"id":"2.150.10.10","name":"Serralysin-like metalloprotease, C-terminal"},{"start":720,"end":762,"id":"2.150.10.10","name":"Serralysin-like metalloprotease, C-terminal"},{"start":763,"end":806,"id":"2.150.10.10","name":"Serralysin-like metalloprotease, C-terminal"}]},"uniref50":"UniRef50_P09983","sequence":"MPTITAAQIKSTLQSAKQSAANKLHSAGQSTKDALKKAAEQTRNAGNRLILLIPKDYKGQGSSLNDLVRTADELGIEVQYDEKNGTAITKQVFGTAEKLIGLTERGVTIFAPQLDKLLQKYQKAGNKLGGSAENIGDNLGKAGSVLSTFQNFLGTALSSMKIDELIKKQKSGGNVSSSELAKASIELINQLVDTAASLNNVNSFSQQLNKLGSVLSNTKHLNGVGNKLQNLPNLDNIGAGLDTVSGILSAISASFILSNADADTGTKAAAGVELTTKVLGNVGKGISQYIIAQRAAQGLSTSAAAAGLIASVVTLAISPLSFLSIADKFKRANKIEEYSQRFKKLGYDGDSLLAAFHKETGAIDASLTRISTVLASVSSGISAAATTSLVGAPVSALVGAVTGIISGILEASKQAMFEHVASKMADVIAEWEKKHGKNYFENGYDARHAAFLEDNFKILSQYNKEYSVERSVLITQQHWDTLIGELAGVTRNGDKTLSGKSYIDYYEEGKRLEKKPDEFQKQVFDPLKGNIDLSDSKSSTLLKFVTPLLTPGEEIRERRQSGKYEYITELLVKGVDKWTVKGVQDKGSVYDYSNLIQHASVGNNQYREIRIESHLGDGDDKVFLSAGSANIYAGKGHDVVYYDKTDTGYLTIDGTKATEAGNYTVTRVLGGDVKVLQEVVKEQEVSVGKRTEKTQYRSYEFTHINGKNLTETDNLYSVEELIGTTRADKFFGSKFADIFHGADGDDHIEGNDGNDRLYGDKGNDTLSGGNGDDQLYGGDGNDKLIGGAGNNYLNGGDGDDELQVQGNSLAKNVLSGGKGNDKLYGSEGADLLDGGEGNDLLKGGYGNDIYRYLSGYGHHIIDDDGGKDDKLSLADIDFRDVAFRREGNDLIMYKAEGNVLSIGHKNGITFKNWFEKESGDISNHQIEQIFDKDGRVITPDSLKKALEYQQSNNKASYVYGNDALAYGSQGNLNPLINEISKIISAAGNFDVKEERAAASLLQLSGNASDFSYGRNSITLTASA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P09983","disprot_id":"DP00389","dataset":["Unicellular toxins and antitoxins","Bacterial virulence-related proteins"],"ncbi_taxon_id":562,"regions_counter":8,"creator":"esalladini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1023,"region_id":"DP00389r001","reference_html":"Secretion and circular dichroism analysis of the C-terminal signal peptides of HlyA and LktA. <i> Zhang F, Yin Y, Arrowsmith CH, Ling V. </i> Biochemistry, 1995","ec_id":"ECO:0006204","version":4,"term_id":"IDPO:0000002","curator_id":"rpancsa","start":962,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"In aqueous solution, the CD spectra of  both HlyA and LktA reflect a predominantly  random conformation (Figures 6 and 7). There is no observed structural change between 23 and 37 “C. A broad range of pH changes (pH 4.5-8) do not affect the structure of  either HlyA or LktA signal  peptide.","type":"Results"},{"text":"The C-terminal signal peptides of HlyA and LktA exhibit similar biophysical behaviors. In aqueous solution, both molecules are mainly in a random conformation.","type":"Discussion"}],"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T15:48:04.448Z","curator_name":"Bálint Mészáros"},"released":"2022_03","reference_id":"7703231","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1023,"region_id":"DP00389r003","reference_html":"Structural analysis and comparison of the C-terminal transport signal domains of hemolysin A and leukotoxin A. <i> Yin Y, Zhang F, Ling V, Arrowsmith CH. </i> FEBS Lett, 1995","ec_id":"ECO:0006165","version":3,"term_id":"IDPO:0000002","curator_id":"rpancsa","start":962,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Signal peptides were labelled with 15N to facilitate the NMR analysis. A striking feature of the NMR spectra of both is the poor dispersion in the 1H nuclei, possibly indicating the presence of a significant amount of random-coil or unfolded protein conformation [27]. The 15N-nuclei, on the other hand, have reasonable chemical shift dispersion as has been shown previously for\nthis nucleus in unfolded proteins [28,29].","type":"Results"},{"text":"The NMR evidence for the helices in HIyA is not as strong as for LktA, presumably due to instability of the helices. Residues 1-34, 47-56 and 68-83 have for the most part random coil Halpha chemical shifts, 3J(NH-Halpha) values between 6-8 Hz and only short-range sequential NOEs (i, i+1 and i, i+2).","type":"Results"}],"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T15:48:05.690Z","curator_name":"Bálint Mészáros"},"released":"2022_03","reference_id":"7789505","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00389r005","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T15:48:11.670Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":1023,"term_id":"GO:0051179","start":962,"version":4,"statement":[{"text":"In order to test the secretion of these signal peptides, C-HA61 or C-LA70 were coexpressed with the transporter proteins HlyB and HlyD in JM83 cells. Cell media were taken at different points during the growth curve. The secreted signal peptides can be detected by Western blot\nanalysis using C494 antibody. As shown in Figure 3 lanes 3, 4, 7, and 8, signal sequence peptides of HlyA and LktA were found in the medium. This secretion requires the\npresence of both HlyB and HlyD.","type":"Results"},{"text":"Thus, these data show that the signal sequence bearing peptides can be transported by the HlyB/D transporter in a specific manner.","type":"Results"},{"text":"This confirms that these short sequences contain information sufficient for recognition and transport, and that no other sequences are required.","type":"Discussion"}],"term_name":"localization","ec_name":"qualitative western immunoblotting evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"7703231","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Biological process","ec_id":"ECO:0000279","curator_id":"rpancsa","reference_html":"Secretion and circular dichroism analysis of the C-terminal signal peptides of HlyA and LktA. <i> Zhang F, Yin Y, Arrowsmith CH, Ling V. </i> Biochemistry, 1995","ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"region_id":"DP00389r006","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T15:48:07.022Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":1023,"term_id":"IDPO:0000011","start":962,"version":3,"statement":[{"text":"Finally, we tested the conformational behaviors of HlyA and LktA signal peptides in phospholipid vesicles, a lipid bilayer environment which more closely resembles a membrane compared to the other reagents tested. Uncharged phospholipids PC could not induce an ordered structure (Figure 7G,H), while the anionic phospholipids (PS, PG) induced formation of a-helices in both peptides (Figure 7C- F).","type":"Results"},{"text":"In aqueous solution, both molecules are mainly in a random conformation. Membrane\nmimetic environments such as TFE/H20, SDS micelles, and negatively charged phospholipid vesicles induce formation of a-helices.","type":"Discussion"}],"term_name":"disorder to order","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"7703231","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural transition","ec_id":"ECO:0006204","curator_id":"rpancsa","reference_html":"Secretion and circular dichroism analysis of the C-terminal signal peptides of HlyA and LktA. <i> Zhang F, Yin Y, Arrowsmith CH, Ling V. </i> Biochemistry, 1995","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00389r007","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T15:48:08.268Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":1023,"term_id":"GO:0008289","start":962,"version":4,"statement":[{"text":"Finally, we tested the conformational behaviors of HlyA and LktA signal peptides in phospholipid vesicles, a lipid bilayer environment which more closely resembles a membrane compared to the other reagents tested. Uncharged phospholipids PC could not induce an ordered structure (Figure 7G,H), while the anionic phospholipids (PS, PG) induced formation of a-helices in both peptides (Figure 7C- F).","type":"Results"}],"term_name":"lipid binding","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"7703231","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006204","curator_id":"rpancsa","reference_html":"Secretion and circular dichroism analysis of the C-terminal signal peptides of HlyA and LktA. <i> Zhang F, Yin Y, Arrowsmith CH, Ling V. </i> Biochemistry, 1995","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P09983","date":"2016-09-08T16:30:08.000Z","acc":"P09983","name":"Hemolysin, chromosomal","length":1023,"organism":"Escherichia coli","UniParc":"UPI000012C946","genes":[{"name":{"value":"hlyA","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"3894051","url":"http://www.ncbi.nlm.nih.gov/pubmed/3894051","alternativeUrl":"https://europepmc.org/abstract/MED/3894051"}}]}}],"alphafold_very_low_content":0.24633431085043989,"disorder_content":0.06060606060606061,"disprot_consensus":{"full":[{"start":962,"end":1023,"type":"T"}],"Structural state":[{"start":962,"end":1023,"type":"D"}],"Biological process":[{"start":962,"end":1023,"type":"F"}],"Structural transition":[{"start":962,"end":1023,"type":"T"}],"Molecular function":[{"start":962,"end":1023,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00339","name":"Arrestin (or S-antigen), N-terminal domain","start":19,"end":173},{"id":"PF02752","name":"Arrestin (or S-antigen), C-terminal domain","start":193,"end":355}],"gene3D":[{"start":180,"end":386,"id":"2.60.40.640","name":"2.60.40.640"},{"start":2,"end":176,"id":"2.60.40.840","name":"2.60.40.840"}]},"uniref50":"UniRef50_P17870","sequence":"MGDKGTRVFKKASPNGKLTVYLGKRDFVDHIDLVEPVDGVVLVDPEYLKERRVYVTLTCAFRYGREDLDVLGLTFRKDLFVANVQSFPPAPEDKKPLTRLQERLIKKLGEHAYPFTFEIPPNLPCSVTLQPGPEDTGKACGVDYEVKAFCAENLEEKIHKRNSVRLVIRKVQYAPERPGPQPTAETTRQFLMSDKPLHLEASLDKEIYYHGEPISVNVHVTNNTNKTVKKIKISVRQYADICLFNTAQYKCPVAMEEADDTVAPSSTFCKVYTLTPFLANNREKRGLALDGKLKHEDTNLASSTLLREGANREILGIIVSYKVKVKLVVSRGGLLGDLASSDVAVELPFTLMHPKPKEEPPHREVPEHETPVDTNLIELDTNDDDIVFEDFARQRLKGMKDDKEEEEDGTGSPRLNDR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P17870","disprot_id":"DP00390","ncbi_taxon_id":9913,"regions_counter":12,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":309,"region_id":"DP00390r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation. <i> Han M, Gurevich VV, Vishnivetskiy SA, Sigler PB, Schubert C. </i> Structure, 2001","term_id":"IDPO:0000002","curator_id":"mnecci","start":282,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"11566136","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1G4M"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":309,"term_name":"molecular adaptor activity","start":282,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"11566136","version":3,"reference_html":"Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation. <i> Han M, Gurevich VV, Vishnivetskiy SA, Sigler PB, Schubert C. </i> Structure, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006220","region_id":"DP00390r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":309,"term_name":"disorder to order","start":282,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"11566136","version":2,"reference_html":"Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation. <i> Han M, Gurevich VV, Vishnivetskiy SA, Sigler PB, Schubert C. </i> Structure, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00390r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":309,"term_name":"small molecule binding","start":282,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"11566136","version":3,"reference_html":"Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation. <i> Han M, Gurevich VV, Vishnivetskiy SA, Sigler PB, Schubert C. </i> Structure, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0036094","ec_id":"ECO:0006220","region_id":"DP00390r004","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":393,"region_id":"DP00390r007","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation. <i> Han M, Gurevich VV, Vishnivetskiy SA, Sigler PB, Schubert C. </i> Structure, 2001","term_id":"IDPO:0000002","curator_id":"mnecci","start":383,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"11566136","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1G4R"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":393,"term_name":"molecular adaptor activity","start":383,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"11566136","version":3,"reference_html":"Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation. <i> Han M, Gurevich VV, Vishnivetskiy SA, Sigler PB, Schubert C. </i> Structure, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006220","region_id":"DP00390r008","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":393,"term_name":"disorder to order","start":383,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"11566136","version":2,"reference_html":"Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation. <i> Han M, Gurevich VV, Vishnivetskiy SA, Sigler PB, Schubert C. </i> Structure, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00390r009","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":393,"term_name":"small molecule binding","start":383,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"11566136","version":3,"reference_html":"Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation. <i> Han M, Gurevich VV, Vishnivetskiy SA, Sigler PB, Schubert C. </i> Structure, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0036094","ec_id":"ECO:0006220","region_id":"DP00390r010","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P17870","date":"2016-09-06T12:44:48.000Z","acc":"P17870","name":"Beta-arrestin-1","length":418,"organism":"Bos taurus","dataset":[],"UniParc":"UPI0000042307","genes":[{"name":{"value":"ARRB1"}}],"alphafold_very_low_content":0.11483253588516747,"disorder_content":0.09330143540669857,"disprot_consensus":{"full":[{"start":282,"end":309,"type":"T"},{"start":383,"end":393,"type":"T"}],"Structural state":[{"start":282,"end":309,"type":"D"},{"start":383,"end":393,"type":"D"}],"Molecular function":[{"start":282,"end":309,"type":"F"},{"start":383,"end":393,"type":"F"}],"Structural transition":[{"start":282,"end":309,"type":"T"},{"start":383,"end":393,"type":"T"}]}},{"features":{"pfam":[{"id":"PF02854","name":"MIF4G domain","start":30,"end":240},{"id":"PF09088","name":"MIF4G like","start":326,"end":470},{"id":"PF09090","name":"MIF4G like","start":485,"end":759}],"gene3D":[{"start":290,"end":481,"id":"1.25.40.180","name":"1.25.40.180"},{"start":489,"end":685,"id":"1.25.40.180","name":"1.25.40.180"},{"start":1,"end":289,"id":"1.25.40.180","name":"1.25.40.180"}]},"uniref50":"UniRef50_Q09161","sequence":"MSRRRHSDENDGGQPHKRRKTSDANETEDHLESLICKVGEKSACSLESNLEGLAGVLEADLPNYKSKILRLLCTVARLLPEKLTIYTTLVGLLNARNYNFGGEFVEAMIRQLKESLKANNYNEAVYLVRFLSDLVNCHVIAAPSMVAMFENFVSVTQEEDVPQVRRDWYVYAFLSSLPWVGKELYEKKDAEMDRIFANTESYLKRRQKTHVPMLQVWTADKPHPQEEYLDCLWAQIQKLKKDRWQERHILRPYLAFDSILCEALQHNLPPFTPPPHTEDSVYPMPRVIFRMFDYTDDPEGPVMPGSHSVERFVIEENLHCIIKSHWKERKTCAAQLVSYPGKNKIPLNYHIVEVIFAELFQLPAPPHIDVMYTTLLIELCKLQPGSLPQVLAQATEMLYMRLDTMNTTCVDRFINWFSHHLSNFQFRWSWEDWSDCLSQDPESPKPKFVREVLEKCMRLSYHQRILDIVPPTFSALCPANPTCIYKYGDESSNSLPGHSVALCLAVAFKSKATNDEIFSILKDVPNPNQDDDDDEGFSFNPLKIEVFVQTLLHLAAKSFSHSFSALAKFHEVFKTLAESDEGKLHVLRVMFEVWRNHPQMIAVLVDKMIRTQIVDCAAVANWIFSSELSRDFTRLFVWEILHSTIRKMNKHVLKIQKELEEAKEKLARQHKRRSDDDDRSSDRKDGVLEEQIERLQEKVESAQSEQKNLFLVIFQRFIMILTEHLVRCETDGTSVLTPWYKNCIERLQQIFLQHHQIIQQYMVTLENLLFTAELDPHILAVFQQFCALQA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q09161","disprot_id":"DP00392","ncbi_taxon_id":9606,"regions_counter":6,"creator":"eleonardi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":26,"region_id":"DP00392r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the human nuclear cap binding complex. <i> Mazza C, Ohno M, Segref A, Mattaj IW, Cusack S. </i> Mol Cell, 2001","term_id":"IDPO:0000002","curator_id":"eleonardi","start":1,"term_ontology":"IDPO","curator_name":"Emanuela Leonardi","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1H6K:A"}],"reference_id":"11545740","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":26,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of the human nuclear cap binding complex. <i> Mazza C, Ohno M, Segref A, Mattaj IW, Cusack S. </i> Mol Cell, 2001","term_id":"GO:0060090","curator_id":"eleonardi","start":1,"term_ontology":"GO","curator_name":"Emanuela Leonardi","reference_id":"11545740","version":3,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00392r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":684,"region_id":"DP00392r005","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Crystal structure of the human nuclear cap binding complex. <i> Mazza C, Ohno M, Segref A, Mattaj IW, Cusack S. </i> Mol Cell, 2001","term_id":"IDPO:0000002","curator_id":"eleonardi","start":671,"term_ontology":"IDPO","curator_name":"Emanuela Leonardi","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1H6K:A"}],"reference_id":"11545740","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":537,"region_id":"DP00392r006","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the human nuclear cap binding complex. <i> Mazza C, Ohno M, Segref A, Mattaj IW, Cusack S. </i> Mol Cell, 2001","term_id":"IDPO:0000002","curator_id":"eleonardi","start":527,"term_ontology":"IDPO","curator_name":"Emanuela Leonardi","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1H6K:A"}],"reference_id":"11545740","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q09161","date":"2016-09-10T17:32:19.000Z","acc":"Q09161","name":"Nuclear cap-binding protein subunit 1","length":790,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000112754","genes":[{"name":{"value":"NCBP1"},"synonyms":[{"value":"CBP80"},{"value":"NCBP"}]}],"alphafold_very_low_content":0.024050632911392405,"disorder_content":0.06455696202531645,"disprot_consensus":{"full":[{"start":1,"end":26,"type":"D"},{"start":527,"end":537,"type":"D"},{"start":671,"end":684,"type":"D"}],"Structural state":[{"start":1,"end":26,"type":"D"},{"start":527,"end":537,"type":"D"},{"start":671,"end":684,"type":"D"}],"Molecular function":[{"start":1,"end":26,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":42,"end":111}],"gene3D":[{"start":1,"end":126,"id":"3.30.70.330","name":"3.30.70.330"}]},"uniref50":"UniRef50_P52298","sequence":"MSGGLLKALRSDSYVELSQYRDQHFRGDNEEQEKLLKKSCTLYVGNLSFYTTEEQIYELFSKSGDIKKIIMGLDKMKKTACGFCFVEYYSRADAENAMRYINGTRLDDRIIRTDWDAGFKEGRQYGRGRSGGQVRDEYRQDYDAGRGGYGKLAQNQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P52298","disprot_id":"DP00393","ncbi_taxon_id":9606,"regions_counter":4,"creator":"slonghi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":21,"region_id":"DP00393r001","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Crystal structure of the human nuclear cap binding complex. <i> Mazza C, Ohno M, Segref A, Mattaj IW, Cusack S. </i> Mol Cell, 2001","term_id":"IDPO:0000002","curator_id":"slonghi","start":1,"term_ontology":"IDPO","curator_name":"Sonia Longhi","reference_id":"11545740","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-6829-6771","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":156,"region_id":"DP00393r002","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Crystal structure of the human nuclear cap binding complex. <i> Mazza C, Ohno M, Segref A, Mattaj IW, Cusack S. </i> Mol Cell, 2001","term_id":"IDPO:0000002","curator_id":"slonghi","start":121,"term_ontology":"IDPO","curator_name":"Sonia Longhi","reference_id":"11545740","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-6829-6771","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":37,"region_id":"DP00393r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the human nuclear cap binding complex. <i> Mazza C, Ohno M, Segref A, Mattaj IW, Cusack S. </i> Mol Cell, 2001","term_id":"IDPO:0000002","curator_id":"slonghi","start":22,"term_ontology":"IDPO","curator_name":"Sonia Longhi","reference_id":"11545740","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1H6K"}],"term_name":"disorder","curator_orcid":"0000-0002-6829-6771","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":37,"term_name":"DNA binding","start":22,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"slonghi","released":"2022_03","term_ontology":"GO","curator_name":"Sonia Longhi","reference_id":"11545740","version":3,"reference_html":"Crystal structure of the human nuclear cap binding complex. <i> Mazza C, Ohno M, Segref A, Mattaj IW, Cusack S. </i> Mol Cell, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003677","ec_id":"ECO:0006220","region_id":"DP00393r004","curator_orcid":"0000-0002-6829-6771","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P52298","date":"2016-09-08T13:13:37.000Z","acc":"P52298","name":"Nuclear cap-binding protein subunit 2","length":156,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000046578","genes":[{"name":{"value":"NCBP2"},"synonyms":[{"value":"CBP20"}],"orfNames":[{"value":"PIG55"}]}],"alphafold_very_low_content":0.00641025641025641,"disorder_content":0.46794871794871795,"disprot_consensus":{"full":[{"start":1,"end":37,"type":"D"},{"start":121,"end":156,"type":"D"}],"Structural state":[{"start":1,"end":37,"type":"D"},{"start":121,"end":156,"type":"D"}],"Molecular function":[{"start":22,"end":37,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03497","name":"Anthrax toxin LF subunit","start":305,"end":480},{"id":"PF07737","name":"Anthrax toxin lethal factor, N- and C-terminal domain","start":53,"end":271},{"id":"PF20850","name":"Oedema factor (EF), alpha-helical domain","start":631,"end":798}],"gene3D":[{"start":64,"end":291,"id":"3.40.390.10","name":"Collagenase (Catalytic Domain)"},{"start":332,"end":470,"id":"3.90.1760.10","name":"Anthrax toxin, edema factor, central domain"},{"start":646,"end":800,"id":"1.20.140.60","name":"1.20.140.60"}]},"uniref50":"UniRef50_P40136","sequence":"MTRNKFIPNKFSIISFSVLLFAISSSQAIEVNAMNEHYTESDIKRNHKTEKNKTEKEKFKDSINNLVKTEFTNETLDKIQQTQDLLKKIPKDVLEIYSELGGEIYFTDIDLVEHKELQDLSEEEKNSMNSRGEKVPFASRFVFEKKRETPKLIINIKDYAINSEQSKEVYYEIGKGISLDIISKDKSLDPEFLNLIKSLSDDSDSSDLLFSQKFKEKLELNNKSIDINFIKENLTEFQHAFSLAFSYYFAPDHRTVLELYAPDMFEYMNKLEKGGFEKISESLKKEGVEKDRIDVLKGEKALKASGLVPEHADAFKKIARELNTYILFRPVNKLATNLIKSGVATKGLNVHGKSSDWGPVAGYIPFDQDLSKKHGQQLAVEKGNLENKKSITEHEGEIGKIPLKLDHLRIEELKENGIILKGKKEIDNGKKYYLLESNNQVYEFRISDENNEVQYKTKEGKITVLGEKFNWRNIEVMAKNVEGVLKPLTADYDLFALAPSLTEIKKQIPQKEWDKVVNTPNSLEKQKGVTNLLIKYGIERKPDSTKGTLSNWQKQMLDRLNEAVKYTGYTGGDVVNHGTEQDNEEFPEKDNEIFIINPEGEFILTKNWEMTGRFIEKNITGKDYLYYFNRSYNKIAPGNKAYIEWTDPITKAKINTIPTSAEFIKNLSSIRRSSNVGVYKDSGDKDEFAKKESVKKIAGYLSDYYNSANHIFSQEKKRKISIFRGIQAYNEIENVLKSKQIAPEYKNYFQYLKERITNQVQLLLTHQKSNIEFKLLYKQLNFTENETDNFEVFQKIIDEK","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Bacillus","Bacillus cereus group"],"uniref90":"UniRef90_P40136","disprot_id":"DP00395","dataset":["Unicellular toxins and antitoxins","Bacterial virulence-related proteins"],"ncbi_taxon_id":1392,"regions_counter":9,"creator":"agasparini","regions":[{"region_id":"DP00395r006","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T17:56:59.055Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":590,"term_id":"IDPO:0000002","start":580,"version":2,"statement":[{"text":"Switch B (578–591), which lies between switch C and the nucleotide substrate, becomes disordered when CaM is not present. This disorder cannot be attributed to the lack of substrate in the EF-alone structure, because switch B is clearly visible in the structure of substrate-free EF–CaM (Fig. 4).","type":"Article"},{"text":"In addition to the helical domain movement, three segments designated as switch A, B and C undergo large conformational changes in response to CaM binding, leaving the remaining residues relatively unchanged (Figs 1 and 4).","type":"Article"},{"text":"In the EF-alone structure switch B is disordered, but it becomes highly ordered in the EF–CaM complex (Fig. 4).","type":"Article"},{"text":"Although Switch B corresponds to region 578-591, only a smaller part of it is disordered and it corresponds to region 580-590 as also shown in PDB:1K8T","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11807546","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1K8T"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin. <i> Drum CL, Yan SZ, Bard J, Shen YQ, Lu D, Soelaiman S, Grabarek Z, Bohm A, Tang WJ. </i> Nature, 2002","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00395r007","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T17:57:36.527Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":590,"term_id":"IDPO:0000011","start":580,"version":2,"statement":[{"text":"Switch B (578–591), which lies between switch C and the nucleotide substrate, becomes disordered when CaM is not present. This disorder cannot be attributed to the lack of substrate in the EF-alone structure, because switch B is clearly visible in the structure of substrate-free EF–CaM (Fig. 4).","type":"Article"},{"text":"In addition to the helical domain movement, three segments designated as switch A, B and C undergo large conformational changes in response to CaM binding, leaving the remaining residues relatively unchanged (Figs 1 and 4).","type":"Article"},{"text":"In the EF-alone structure switch B is disordered, but it becomes highly ordered in the EF–CaM complex (Fig. 4). This transition is most probably caused by extensive contacts between switch B and the N-terminal portion of switch C. Notably, Asn 639 forms a hydrogen bond with the main-chain carbonyl of Pro 587. Mutation of Asn 639 to alanine results in a 12-fold reduction in the rate of catalysis (Fig. 4c and Table 1). Thus, we propose that the ordering of switch B occurs as a consequence of the CaM-induced movement of switch C.","type":"Article"},{"text":"On calmodulin binding, an oedema factor helical domain of relative molecular mass 15,000 undergoes a 15 Å translation and a 30° rotation away from the oedema factor catalytic core, which stabilizes a disordered loop and leads to enzyme activation.","type":"Abstract"},{"text":"Although Switch B corresponds to region 578-591, only a smaller part of it is disordered and it corresponds to region 580-590 as also shown in PDB:1K8T","type":"Curator statement"}],"term_name":"disorder to order","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11807546","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1K90"},{"db":"PDB","id":"1K93"}],"term_namespace":"Structural transition","ec_id":"ECO:0005670","curator_id":"fquaglia","reference_html":"Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin. <i> Drum CL, Yan SZ, Bard J, Shen YQ, Lu D, Soelaiman S, Grabarek Z, Bohm A, Tang WJ. </i> Nature, 2002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00395r008","ec_ontology":"ECO","end":590,"term_id":"GO:0032564","start":580,"version":5,"statement":[{"text":"Switch B (residues 579–591) contains several residues that either bind ATP directly or stabilize the catalytic residues (Fig. 3).","type":"Article"},{"text":"Phe 586 and Leu 348 lie above and below the plane of the ribose, and the side chain of Asn 583 forms a hydrogen bond with O4′ of the ribose ring. The adenosine ring, although solvent accessible, contacts the backbone of Asp 582 and Asn 583, and the N6 nitrogen is within hydrogen-bonding distance of the main-chain carbonyls of Thr 579 and Thr 548.","type":"Article"}],"interaction_partner":[{"partner_start":null,"db":"ChEBI","id":"16284","partner_end":null}],"term_name":"dATP binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0001-8399-7907","released":"2025_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"11807546","date":"2025-01-22T19:25:51.699Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1K90"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"vnugnes","reference_html":"Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin. <i> Drum CL, Yan SZ, Bard J, Shen YQ, Lu D, Soelaiman S, Grabarek Z, Bohm A, Tang WJ. </i> Nature, 2002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to dATP, deoxyadenosine triphosphate.\" [GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P40136","date":"2016-09-09T16:41:35.000Z","acc":"P40136","name":"Calmodulin-sensitive adenylate cyclase","length":800,"organism":"Bacillus anthracis","UniParc":"UPI000000132F","genes":[{"name":{"value":"cya"},"olnNames":[{"value":"pXO1-122"},{"value":"BXA0141"},{"value":"GBAA_pXO1_0142"}]}],"alphafold_very_low_content":0.0675,"disorder_content":0.01375,"disprot_consensus":{"full":[{"start":580,"end":590,"type":"T"}],"Structural state":[{"start":580,"end":590,"type":"D"}],"Structural transition":[{"start":580,"end":590,"type":"T"}],"Molecular function":[{"start":580,"end":590,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00009","name":"Elongation factor Tu GTP binding domain","start":236,"end":457},{"id":"PF22594","name":"GTP-eEF1A C-terminal domain-like","start":559,"end":657}],"gene3D":[{"start":464,"end":552,"id":"2.40.30.10","name":"Translation factors"},{"start":215,"end":463,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":553,"end":662,"id":"2.40.30.10","name":"Translation factors"}]},"uniref50":"UniRef50_O74718","sequence":"MASNQPNNGEQDEQLAKQTSKLSMSAKAPTFTPKAAPFIPSFQRPGFVPVNNIAGGYPYAQYTGQGQNSNSPHPTKSYQQYYQKPTGNTVDEDKSRVPDFSKKKSFVPPKPAIPKGKVLSLGGNTSAPKSTKPISISLGGTKAPTTTKPAAPAAQSKTETPAPKVTSESTKKETAAPPPQETPTKSADAELAKTPSAPAAALKKAAEAAEPATVTEDATDLQNEVDQELLKDMYGKEHVNIVFIGHVDAGKSTLGGNILFLTGMVDKRTMEKIEREAKEAGKESWYLSWALDSTSEEREKGKTVEVGRAYFETEHRRFSLLDAPGHKGYVTNMINGASQADIGVLVISARRGEFEAGFERGGQTREHAVLARTQGINHLVVVINKMDEPSVQWSEERYKECVDKLSMFLRRVAGYNSKTDVKYMPVSAYTGQNVKDRVDSSVCPWYQGPSLLEYLDSMTHLERKVNAPFIMPIASKYKDLGTILEGKIEAGSIKKNSNVLVMPINQTLEVTAIYDEADEEISSSICGDQVRLRVRGDDSDVQTGYVLTSTKNPVHATTRFIAQIAILELPSILTTGYSCVMHIHTAVEEVSFAKLLHKLDKTNRKSKKPPMFATKGMKIIAELETQTPVCMERFEDYQYMGRFTLRDQGTTVAVGKVVKILD","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"uniref90":"UniRef90_O74718","disprot_id":"DP00396","ncbi_taxon_id":284812,"regions_counter":6,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":214,"region_id":"DP00396r001","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S. pombe. <i> Kong C, Ito K, Walsh MA, Wada M, Liu Y, Kumar S, Barford D, Nakamura Y, Song H. </i> Mol Cell, 2004","term_id":"IDPO:0000002","curator_id":"fquaglia","start":196,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15099522","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-12-07T19:30:08.903Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1R5B"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"In all three structures, three regions of polypeptide are not visible in the electron density map and are assumed to be disordered, namely residues 196-214, 280-307, and 325-335.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-13T15:21:51.000Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":307,"region_id":"DP00396r002","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S. pombe. <i> Kong C, Ito K, Walsh MA, Wada M, Liu Y, Kumar S, Barford D, Nakamura Y, Song H. </i> Mol Cell, 2004","term_id":"IDPO:0000002","curator_id":"fquaglia","start":280,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15099522","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-12-07T19:30:49.827Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1R5B"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"In all three structures, three regions of polypeptide are not visible in the electron density map and are assumed to be disordered, namely residues 196-214, 280-307, and 325-335.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-13T15:21:49.024Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":335,"region_id":"DP00396r004","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S. pombe. <i> Kong C, Ito K, Walsh MA, Wada M, Liu Y, Kumar S, Barford D, Nakamura Y, Song H. </i> Mol Cell, 2004","term_id":"IDPO:0000002","curator_id":"fquaglia","start":325,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15099522","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-12-07T19:31:23.286Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1R5B"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"In all three structures, three regions of polypeptide are not visible in the electron density map and are assumed to be disordered, namely residues 196-214, 280-307, and 325-335.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-13T15:21:49.943Z"}},{"start":301,"end":305,"reference_id":"15099522","reference_source":"pmid","reference_html":"Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S. pombe. <i> Kong C, Ito K, Walsh MA, Wada M, Liu Y, Kumar S, Barford D, Nakamura Y, Song H. </i> Mol Cell, 2004","date":"2026-01-07T18:16:57.489Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0000287","term_name":"magnesium ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006216","ec_ontology":"ECO","ec_name":"author inference used in manual assertion","unpublished":true,"released":"2023_12","version":1,"ec_go":"IC","interaction_partner":[{"db":"ChEBI","id":"18420","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00396r006","statement":[{"text":"The rest of switch I in eRF3c, which contains the conserved metal binding residue Thr303 (Thr61 of EF-Tu), is disordered.","type":"Results"},{"text":"Our observations that Mg²⁺ is absent from the GDP binding site of eRF3c, and at higher concentration promotes GDP release, suggests that the first step of nucleotide exchange in eRF3 is the release of the phosphate moiety prompted by Mg²⁺ binding rather than its removal.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a magnesium (Mg) ion.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-01-07T18:17:03.699Z"}}],"released":"2016_10","uniref100":"UniRef100_O74718","date":"2016-08-23T13:19:47.000Z","acc":"O74718","name":"Eukaryotic peptide chain release factor GTP-binding subunit","length":662,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","dataset":["Condensates-related proteins"],"UniParc":"UPI00001688E0","genes":[{"name":{"value":"sup35"},"orfNames":[{"value":"SPCC584.04"}]}],"alphafold_very_low_content":0.3293051359516616,"disorder_content":0.08761329305135952,"disprot_consensus":{"full":[{"start":196,"end":214,"type":"D"},{"start":280,"end":307,"type":"D"},{"start":325,"end":335,"type":"D"}],"Structural state":[{"start":196,"end":214,"type":"D"},{"start":280,"end":307,"type":"D"},{"start":325,"end":335,"type":"D"}],"Molecular function":[{"start":301,"end":305,"type":"F"}]}},{"features":{"pfam":[{"id":"PF09258","name":"Glycosyl transferase family 64 domain","start":67,"end":321}],"gene3D":[{"start":62,"end":330,"id":"3.90.550.10","name":"Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A"}]},"uniref50":"UniRef50_Q9UBQ6","sequence":"MMRGCHICKLPGRVMGIRVLRFSLVVILVLLLVAGALTNLLPNIKEDKMLTLRREIKSPSKSALDSFTLIMQTYNRTDLLLRLLNHYQAVPSLHKVIVVWNNVGEKGPEELWNSLGPHPIPVIFKPQTANKMRNRLQVFPEVETNAVLMVDDDTLISAQDLVFAFSIWQQFPDQIIGFVPRKHVSTSSGIYSYGGFELQTPGPGNGDQYSMVLIGASFFNSKYLELFQKQPAAVHALIDETQNCDDIAMNFLVTRHTGKPSGIFVKPINMVNLEKETNGYSGMWHRAEHFLQRSYCINKLVNIYDGMPLKYSNIMISQFGFPYANHKSKM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q9ES89","disprot_id":"DP00397","ncbi_taxon_id":10090,"regions_counter":4,"creator":"ahatos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":285,"region_id":"DP00397r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of an alpha 1,4-N-acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis. <i> Pedersen LC, Dong J, Taniguchi F, Kitagawa H, Krahn JM, Pedersen LG, Sugahara K, Negishi M. </i> J Biol Chem, 2003","term_id":"IDPO:0000002","curator_id":"ahatos","start":275,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1OMZ"}],"reference_id":"12562774","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":285,"term_name":"molecular function regulator","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of an alpha 1,4-N-acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis. <i> Pedersen LC, Dong J, Taniguchi F, Kitagawa H, Krahn JM, Pedersen LG, Sugahara K, Negishi M. </i> J Biol Chem, 2003","term_id":"GO:0098772","curator_id":"ahatos","start":275,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"12562774","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00397r002","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":285,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of an alpha 1,4-N-acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis. <i> Pedersen LC, Dong J, Taniguchi F, Kitagawa H, Krahn JM, Pedersen LG, Sugahara K, Negishi M. </i> J Biol Chem, 2003","term_id":"IDPO:0000011","curator_id":"ahatos","start":275,"term_ontology":"IDPO","curator_name":"András Hatos","reference_id":"12562774","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00397r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":285,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of an alpha 1,4-N-acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis. <i> Pedersen LC, Dong J, Taniguchi F, Kitagawa H, Krahn JM, Pedersen LG, Sugahara K, Negishi M. </i> J Biol Chem, 2003","term_id":"GO:0005515","curator_id":"ahatos","start":275,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"12562774","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00397r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q9ES89","date":"2016-09-07T10:26:19.000Z","acc":"Q9ES89","name":"Exostosin-like 2","length":330,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000001A88","genes":[{"name":{"value":"Extl2"},"synonyms":[{"value":"Extr2"}]}],"alphafold_very_low_content":0.048484848484848485,"disorder_content":0.03333333333333333,"disprot_consensus":{"full":[{"start":275,"end":285,"type":"T"}],"Structural state":[{"start":275,"end":285,"type":"D"}],"Molecular function":[{"start":275,"end":285,"type":"F"}],"Structural transition":[{"start":275,"end":285,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00205","name":"Thiamine pyrophosphate enzyme, central domain","start":289,"end":431},{"id":"PF02775","name":"Thiamine pyrophosphate enzyme, C-terminal TPP binding domain","start":496,"end":643},{"id":"PF02776","name":"Thiamine pyrophosphate enzyme, N-terminal TPP binding domain","start":93,"end":207}],"gene3D":[{"start":460,"end":687,"id":"3.40.50.970","name":"3.40.50.970"},{"start":281,"end":458,"id":"3.40.50.1220","name":"TPP-binding domain"},{"start":86,"end":267,"id":"3.40.50.970","name":"3.40.50.970"}]},"uniref50":"UniRef50_P07342","sequence":"MIRQSTLKNFAIKRCFQHIAYRNTPAMRSVALAQRFYSSSSRYYSASPLPASKRPEPAPSFNVDPLEQPAEPSKLAKKLRAEPDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILPVYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFADGIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSGRPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALNQLTSRAQDEFVMQSINKAADLINLAKKPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLGSFDQEDPKSLDMLGMHGCATANLAVQNADLIIAVGARFDDRVTGNISKFAPEARRAAAEGRGGIIHFEVSPKNINKVVQTQIAVEGDATTNLGKMMSKIFPVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKLSKVANDTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKPESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQLNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKKVPVLPMVAGGSGLDEFINFDPEVERQQTELRHKRTGGKH","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P07342","disprot_id":"DP00398","ncbi_taxon_id":559292,"regions_counter":3,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":595,"region_id":"DP00398r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors. <i> Pang SS, Duggleby RG, Guddat LW. </i> J Mol Biol, 2002","term_id":"IDPO:0000002","curator_id":"atantos","start":580,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1JSC"}],"reference_id":"11902841","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":687,"region_id":"DP00398r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors. <i> Pang SS, Duggleby RG, Guddat LW. </i> J Mol Biol, 2002","term_id":"IDPO:0000002","curator_id":"atantos","start":647,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1JSC"}],"reference_id":"11902841","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":687,"term_name":"flexible C-terminal tail","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors. <i> Pang SS, Duggleby RG, Guddat LW. </i> J Mol Biol, 2002","term_id":"IDPO:0000031","curator_id":"atantos","start":647,"term_ontology":"IDPO","curator_name":"Agnes Tantos","reference_id":"11902841","version":3,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00398r003","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_P07342","date":"2016-09-08T10:05:30.000Z","acc":"P07342","name":"Acetolactate synthase catalytic subunit, mitochondrial","length":687,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000012D53A","genes":[{"name":{"value":"ILV2"},"synonyms":[{"value":"SMR1"}],"orfNames":[{"value":"YM9718.07"}],"olnNames":[{"value":"YMR108W"}]}],"alphafold_very_low_content":0.09315866084425037,"disorder_content":0.08296943231441048,"disprot_consensus":{"full":[{"start":580,"end":595,"type":"D"},{"start":647,"end":687,"type":"D"}],"Structural state":[{"start":580,"end":595,"type":"D"},{"start":647,"end":687,"type":"D"}],"Disorder function":[{"start":647,"end":687,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00478","name":"IMP dehydrogenase / GMP reductase domain","start":10,"end":162},{"id":"PF00478","name":"IMP dehydrogenase / GMP reductase domain","start":215,"end":489},{"id":"PF00571","name":"CBS domain","start":163,"end":214}],"gene3D":[{"start":2,"end":502,"id":"3.20.20.70","name":"Aldolase class I"}]},"uniref50":"UniRef50_P50097","sequence":"MAKYYNEPCHTFNEYLLIPGLSTVDCIPSNVNLSTPLVKFQKGQQSEINLKIPLVSAIMQSVSGEKMAIALAREGGISFIFGSQSIESQAAMVHAVKNFKAGFVVSDSNVKPDQTFADVLAISQRTTHNTVAVTDDGTPHGVLLGLVTQRDYPIDLTQTETKVSDMMTPFSKLVTAHQDTKLSEANKIIWEKKLNALPIIDDDQHLRYIVFRKDYDRSQVCHNELVDSQKRYLVGAGINTRDFRERVPALVEAGADVLCIDSSDGFSEWQKITIGWIREKYGDKVKVGAGNIVDGEGFRYLADAGADFIKIGIGGGSICITREQKGIGRGQATAVIDVVAERNKYFEETGIYIPVCSDGGIVYDYHMTLALAMGADFIMLGRYFARFEESPTRKVTINGSVMKEYWGEGSSRARNWQRYDLGGKQKLSFEEGVDSYVPYAGKLKDNVEASLNKVKSTMCNCGALTIPQLQSKAKITLVSSVSIVEGGAHDVIVKDRINDYHPK","taxonomy":["Eukaryota","Metamonada","Parabasalia","Tritrichomonadida","Tritrichomonadidae","Tritrichomonas"],"uniref90":"UniRef90_P50097","disprot_id":"DP00399","ncbi_taxon_id":56690,"regions_counter":5,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":221,"region_id":"DP00399r001","released":"2024_06","ec_id":"ECO:0006220","reference_html":"Crystal structure of Tritrichomonas foetus inosine-5'-monophosphate dehydrogenase and the enzyme-product complex. <i> Whitby FG, Luecke H, Kuhn P, Somoza JR, Huete-Perez JA, Phillips JD, Hill CP, Fletterick RJ, Wang CC. </i> Biochemistry, 1997","term_id":"IDPO:0000002","curator_id":"vnugnes","start":102,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"9271497","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2024-03-13T15:31:05.220Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1AK5"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"The smaller domain, residues 102−220, is not visible in the electron density maps, presumably due to disorder.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":327,"region_id":"DP00399r002","released":"2024_06","ec_id":"ECO:0006220","reference_html":"Crystal structure of Tritrichomonas foetus inosine-5'-monophosphate dehydrogenase and the enzyme-product complex. <i> Whitby FG, Luecke H, Kuhn P, Somoza JR, Huete-Perez JA, Phillips JD, Hill CP, Fletterick RJ, Wang CC. </i> Biochemistry, 1997","term_id":"IDPO:0000002","curator_id":"vnugnes","start":314,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"9271497","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2024-03-13T15:32:23.813Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1AK5"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"Other disordered segments of the IMPDH structure include three flexible loops formed by residues 314−324 (between strand 6 and helix 6 of the barrel), 413−431 (following helix 8 of the barrel), and 484−503 (the C terminus).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":431,"region_id":"DP00399r004","released":"2024_06","ec_id":"ECO:0006220","reference_html":"Crystal structure of Tritrichomonas foetus inosine-5'-monophosphate dehydrogenase and the enzyme-product complex. <i> Whitby FG, Luecke H, Kuhn P, Somoza JR, Huete-Perez JA, Phillips JD, Hill CP, Fletterick RJ, Wang CC. </i> Biochemistry, 1997","term_id":"IDPO:0000002","curator_id":"vnugnes","start":413,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"9271497","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2024-03-13T15:32:50.716Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1AK5"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"Other disordered segments of the IMPDH structure include three flexible loops formed by residues 314−324 (between strand 6 and helix 6 of the barrel), 413−431 (following helix 8 of the barrel), and 484−503 (the C terminus).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":503,"region_id":"DP00399r005","released":"2024_06","ec_id":"ECO:0006220","reference_html":"Crystal structure of Tritrichomonas foetus inosine-5'-monophosphate dehydrogenase and the enzyme-product complex. <i> Whitby FG, Luecke H, Kuhn P, Somoza JR, Huete-Perez JA, Phillips JD, Hill CP, Fletterick RJ, Wang CC. </i> Biochemistry, 1997","term_id":"IDPO:0000002","curator_id":"vnugnes","start":484,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"9271497","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2024-03-13T15:33:26.422Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1AK5"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"Other disordered segments of the IMPDH structure include three flexible loops formed by residues 314−324 (between strand 6 and helix 6 of the barrel), 413−431 (following helix 8 of the barrel), and 484−503 (the C terminus).","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P50097","date":"2016-08-25T14:15:37.000Z","acc":"P50097","name":"Inosine-5'-monophosphate dehydrogenase","length":503,"organism":"Tritrichomonas foetus","dataset":[],"UniParc":"UPI0000110542","genes":[{"name":{"value":"IMPDH","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03156","url":"https://hamap.expasy.org/unirule/MF_03156"}}]}}],"alphafold_very_low_content":0.015904572564612324,"disorder_content":0.34393638170974156,"disprot_consensus":{"full":[{"start":102,"end":221,"type":"D"},{"start":314,"end":327,"type":"D"},{"start":413,"end":431,"type":"D"},{"start":484,"end":503,"type":"D"}],"Structural state":[{"start":102,"end":221,"type":"D"},{"start":314,"end":327,"type":"D"},{"start":413,"end":431,"type":"D"},{"start":484,"end":503,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00685","name":"Sulfotransferase domain","start":60,"end":304}],"gene3D":[{"start":15,"end":312,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_O00204","sequence":"MDGPAEPQIPGLWDTYEDDISEISQKLPGEYFRYKGVPFPVGLYSLESISLAENTQDVRDDDIFIITYPKSGTTWMIEIICLILKEGDPSWIRSVPIWERAPWCETIVGAFSLPDQYSPRLMSSHLPIQIFTKAFFSSKAKVIYMGRNPRDVVVSLYHYSKIAGQLKDPGTPDQFLRDFLKGEVQFGSWFDHIKGWLRMKGKDNFLFITYEELQQDLQGSVERICGFLGRPLGKEALGSVVAHSTFSAMKANTMSNYTLLPPSLLDHRRGAFLRKGVCGDWKNHFTVAQSEAFDRAYRKQMRGMPTFPWDEDPEEDGSPDPEPSPEPEPKPSLEPNTSLEREPRPNSSPSPSPGQASETPHPRPS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O00204","disprot_id":"DP00404","ncbi_taxon_id":9606,"regions_counter":4,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":26,"region_id":"DP00404r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms. <i> Lee KA, Fuda H, Lee YC, Negishi M, Strott CA, Pedersen LC. </i> J Biol Chem, 2003","term_id":"IDPO:0000002","curator_id":"mnecci","start":13,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12923182","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":26,"term_name":"molecular recognition display site","start":13,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12923182","version":2,"reference_html":"Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms. <i> Lee KA, Fuda H, Lee YC, Negishi M, Strott CA, Pedersen LC. </i> J Biol Chem, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000037","ec_id":"ECO:0006220","region_id":"DP00404r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":26,"term_name":"pre-molten globule to order","start":13,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12923182","version":2,"reference_html":"Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms. <i> Lee KA, Fuda H, Lee YC, Negishi M, Strott CA, Pedersen LC. </i> J Biol Chem, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000013","ec_id":"ECO:0006220","region_id":"DP00404r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":26,"term_name":"small molecule binding","start":13,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"12923182","version":3,"reference_html":"Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms. <i> Lee KA, Fuda H, Lee YC, Negishi M, Strott CA, Pedersen LC. </i> J Biol Chem, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0036094","ec_id":"ECO:0006220","region_id":"DP00404r004","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_O00204","date":"2016-09-20T12:18:05.000Z","acc":"O00204","name":"Sulfotransferase 2B1","length":365,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000736D4","genes":[{"name":{"value":"SULT2B1"},"synonyms":[{"value":"HSST2"}]}],"alphafold_very_low_content":0.1095890410958904,"disorder_content":0.038356164383561646,"disprot_consensus":{"full":[{"start":13,"end":26,"type":"T"}],"Structural state":[{"start":13,"end":26,"type":"D"}],"Disorder function":[{"start":13,"end":26,"type":"F"}],"Structural transition":[{"start":13,"end":26,"type":"T"}],"Molecular function":[{"start":13,"end":26,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01584","name":"CheW-like domain","start":514,"end":640},{"id":"PF01627","name":"Hpt domain","start":8,"end":100},{"id":"PF02518","name":"Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase","start":372,"end":508},{"id":"PF02895","name":"Signal transducing histidine kinase, homodimeric domain","start":261,"end":324},{"id":"PF09078","name":"CheY binding","start":161,"end":223}],"gene3D":[{"start":325,"end":508,"id":"3.30.565.10","name":"Histidine kinase-like ATPase, C-terminal domain"},{"start":1,"end":145,"id":"1.20.120.160","name":"HPT domain"},{"start":146,"end":225,"id":"3.30.70.400","name":"CheY-binding domain of CheA"},{"start":261,"end":324,"id":"1.10.287.560","name":"Histidine kinase  CheA-like, homodimeric domain"},{"start":532,"end":596,"id":"2.40.50.180","name":"CheA-289, Domain 4"},{"start":509,"end":637,"id":"2.30.30.40","name":"SH3 Domains"}]},"uniref50":"UniRef50_P07363","sequence":"MSMDISDFYQTFFDEADELLADMEQHLLVLQPEAPDAEQLNAIFRAAHSIKGGAGTFGFSVLQETTHLMENLLDEARRGEMQLNTDIINLFLETKDIMQEQLDAYKQSQEPDAASFDYICQALRQLALEAKGETPSAVTRLSVVAKSEPQDEQSRSQSPRRIILSRLKAGEVDLLEEELGHLTTLTDVVKGADSLSAILPGDIAEDDITAVLCFVIEADQITFETVEVSPKISTPPVLKLAAEQAPTGRVEREKTTRSNESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSELDPVNHGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRYPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLTVSENMSDDEVAMLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQKMGGHVEIQSKQGTGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPREADLHPLAGGERVLEVRGEYLPIVELWKVFNVAGAKTEATQGIVVILQSGGRRYALLVDQLIGQHQVVVKNLESNYRKVPGISAATILGDGSVALIVDVSALQAINREQRMANTAA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P07363","disprot_id":"DP00407","ncbi_taxon_id":83333,"regions_counter":4,"creator":"agasparini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":158,"region_id":"DP00407r001","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy. <i> McEvoy MM, Muhandiram DR, Kay LE, Dahlquist FW. </i> Biochemistry, 1996","term_id":"IDPO:0000002","curator_id":"vnugnes","start":124,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"8639521","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-08-17T20:31:56.500Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1FWP"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The NMR experiments were conducted on a 139 amino acid fragment of CheA which contains the 69 residue CheY-binding domain (residues 159−227) as well as two unstructured domain linkers (residues 124−158 and 228−257).","type":"Results"}],"sequence_construct":"RQLALEAKGETPSAVTRLSVVAKSEPQDEQSRSQSPRRIILSRLKAGEVDLLEEELGHLTTLTDVVKGADSLSAILPGDIAEDDITAVLCFVIEADQITFETVEVSPKISTPPVLKLAAEQAPTGRVEREKTTRIKLGT"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":158,"term_name":"flexible linker","start":124,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2022_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"8639521","version":4,"reference_html":"Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy. <i> McEvoy MM, Muhandiram DR, Kay LE, Dahlquist FW. </i> Biochemistry, 1996","date":"2022-08-17T20:31:32.505Z","term_id":"IDPO:0000033","ec_id":"ECO:0006165","region_id":"DP00407r002","ec_go":"EXP","disprot_namespace":"Disorder function","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The NMR experiments were conducted on a 139 amino acid fragment of CheA which contains the 69 residue CheY-binding domain (residues 159−227) as well as two unstructured domain linkers (residues 124−158 and 228−257).","type":"Results"}],"sequence_construct":"RQLALEAKGETPSAVTRLSVVAKSEPQDEQSRSQSPRRIILSRLKAGEVDLLEEELGHLTTLTDVVKGADSLSAILPGDIAEDDITAVLCFVIEADQITFETVEVSPKISTPPVLKLAAEQAPTGRVEREKTTRIKLGT"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":257,"region_id":"DP00407r003","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy. <i> McEvoy MM, Muhandiram DR, Kay LE, Dahlquist FW. </i> Biochemistry, 1996","term_id":"IDPO:0000002","curator_id":"vnugnes","start":228,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"8639521","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-08-17T20:31:22.568Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1FWP"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The NMR experiments were conducted on a 139 amino acid fragment of CheA which contains the 69 residue CheY-binding domain (residues 159−227) as well as two unstructured domain linkers (residues 124−158 and 228−257).","type":"Results"}],"sequence_construct":"RQLALEAKGETPSAVTRLSVVAKSEPQDEQSRSQSPRRIILSRLKAGEVDLLEEELGHLTTLTDVVKGADSLSAILPGDIAEDDITAVLCFVIEADQITFETVEVSPKISTPPVLKLAAEQAPTGRVEREKTTRIKLGT"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":257,"term_name":"flexible linker","start":228,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2022_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"8639521","version":4,"reference_html":"Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy. <i> McEvoy MM, Muhandiram DR, Kay LE, Dahlquist FW. </i> Biochemistry, 1996","date":"2022-08-17T20:31:42.295Z","term_id":"IDPO:0000033","ec_id":"ECO:0006165","region_id":"DP00407r004","ec_go":"EXP","disprot_namespace":"Disorder function","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The NMR experiments were conducted on a 139 amino acid fragment of CheA which contains the 69 residue CheY-binding domain (residues 159−227) as well as two unstructured domain linkers (residues 124−158 and 228−257).","type":"Results"}],"sequence_construct":"RQLALEAKGETPSAVTRLSVVAKSEPQDEQSRSQSPRRIILSRLKAGEVDLLEEELGHLTTLTDVVKGADSLSAILPGDIAEDDITAVLCFVIEADQITFETVEVSPKISTPPVLKLAAEQAPTGRVEREKTTRIKLGT"}],"released":"2016_10","uniref100":"UniRef100_P07363","date":"2016-09-09T17:05:41.000Z","acc":"P07363","name":"Chemotaxis protein CheA","length":654,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI000016EE50","genes":[{"name":{"value":"cheA"},"olnNames":[{"value":"b1888"},{"value":"JW1877"}]}],"alphafold_very_low_content":0.10703363914373089,"disorder_content":0.09938837920489296,"disprot_consensus":{"full":[{"start":124,"end":158,"type":"D"},{"start":228,"end":257,"type":"D"}],"Structural state":[{"start":124,"end":158,"type":"D"},{"start":228,"end":257,"type":"D"}],"Disorder function":[{"start":124,"end":158,"type":"F"},{"start":228,"end":257,"type":"F"}]}},{"acc":"P12497","sequence":"MGARASVLSGGELDKWEKIRLRPGGKKQYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTIAVLYCVHQRIDVKDTKEALDKIEEEQNKSKKKAQQAAADTGNNSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTHNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPGATLEEMMTACQGVGGPGHKARVLAEAMSQVTNPATIMIQKGNFRNQRKTVKCFNCGKEGHIAKNCRAPRKKGCWKCGKEGHQMKDCTERQANFLREDLAFPQGKAREFSSEQTRANSPTRRELQVWGRDNNSLSEAGADRQGTVSFSFPQITLWQRPLVTIKIGGQLKEALLDTGADDTVLEEMNLPGRWKPKMIGGIGGFIKVRQYDQILIEICGHKAIGTVLVGPTPVNIIGRNLLTQIGCTLNFPISPIETVPVKLKPGMDGPKVKQWPLTEEKIKALVEICTEMEKEGKISKIGPENPYNTPVFAIKKKDSTKWRKLVDFRELNKRTQDFWEVQLGIPHPAGLKQKKSVTVLDVGDAYFSVPLDKDFRKYTAFTIPSINNETPGIRYQYNVLPQGWKGSPAIFQCSMTKILEPFRKQNPDIVIYQYMDDLYVGSDLEIGQHRTKIEELRQHLLRWGFTTPDKKHQKEPPFLWMGYELHPDKWTVQPIVLPEKDSWTVNDIQKLVGKLNWASQIYAGIKVRQLCKLLRGTKALTEVVPLTEEAELELAENREILKEPVHGVYYDPSKDLIAEIQKQGQGQWTYQIYQEPFKNLKTGKYARMKGAHTNDVKQLTEAVQKIATESIVIWGKTPKFKLPIQKETWEAWWTEYWQATWIPEWEFVNTPPLVKLWYQLEKEPIIGAETFYVDGAANRETKLGKAGYVTDRGRQKVVPLTDTTNQKTELQAIHLALQDSGLEVNIVTDSQYALGIIQAQPDKSESELVSQIIEQLIKKEKVYLAWVPAHKGIGGNEQVDGLVSAGIRKVLFLDGIDKAQEEHEKYHSNWRAMASDFNLPPVVAKEIVASCDKCQLKGEAMHGQVDCSPGIWQLDCTHLEGKVILVAVHVASGYIEAEVIPAETGQETAYFLLKLAGRWPVKTVHTDNGSNFTSTTVKAACWWAGIKQEFGIPYNPQSQGVIESMNKELKKIIGQVRDQAEHLKTAVQMAVFIHNFKRKGGIGGYSAGERIVDIIATDIQTKELQKQITKIQNFRVYYRDSRDPVWKGPAKLLWKGEGAVVIQDNSDIKVVPRRKAKIIRDYGKQMAGDDCVASRQDED","creator":"xcastro","dataset":["Viral proteins","RNA-binding proteins"],"date":"2016-09-07T15:18:34.000Z","disprot_id":"DP00410","features":{"pfam":[{"id":"PF00075","name":"RNase H","start":1025,"end":1143},{"id":"PF00077","name":"Retroviral aspartyl protease","start":494,"end":585},{"id":"PF00078","name":"Reverse transcriptase (RNA-dependent DNA polymerase)","start":650,"end":821},{"id":"PF00098","name":"Zinc knuckle","start":391,"end":406},{"id":"PF00098","name":"Zinc knuckle","start":412,"end":428},{"id":"PF00540","name":"gag gene protein p17 (matrix protein)","start":2,"end":132},{"id":"PF00552","name":"Integrase DNA binding domain","start":1372,"end":1415},{"id":"PF00665","name":"Integrase core domain","start":1204,"end":1292},{"id":"PF02022","name":"Integrase Zinc binding domain","start":1155,"end":1191},{"id":"PF06815","name":"Reverse transcriptase connection domain","start":905,"end":1006},{"id":"PF06817","name":"Reverse transcriptase thumb domain","start":828,"end":890},{"id":"PF19317","name":"Gag protein p24 C-terminal domain","start":276,"end":349}],"gene3D":[{"start":1200,"end":1358,"id":"3.30.420.10","name":"Ribonuclease H-like superfamily/Ribonuclease H","_id":"685af523b4ac24d5329d7c75"},{"start":1,"end":132,"id":"1.10.150.90","name":"Immunodeficiency lentiviruses, gag gene matrix protein p17","_id":"685af523b4ac24d5329d7c76"},{"start":1359,"end":1416,"id":"2.30.30.10","name":"Integrase, C-terminal domain superfamily, retroviral","_id":"685af523b4ac24d5329d7c77"},{"start":133,"end":278,"id":"1.10.375.10","name":"Human Immunodeficiency Virus Type 1 Capsid Protein","_id":"685af523b4ac24d5329d7c78"},{"start":283,"end":347,"id":"1.10.1200.30","name":"1.10.1200.30","_id":"685af523b4ac24d5329d7c79"},{"start":1016,"end":1143,"id":"3.30.420.10","name":"Ribonuclease H-like superfamily/Ribonuclease H","_id":"685af523b4ac24d5329d7c7a"},{"start":1147,"end":1199,"id":"1.10.10.200","name":"1.10.10.200","_id":"685af523b4ac24d5329d7c7b"},{"start":489,"end":587,"id":"2.40.70.10","name":"Acid Proteases","_id":"685af523b4ac24d5329d7c7c"},{"start":603,"end":743,"id":"3.10.10.10","name":"HIV Type 1 Reverse Transcriptase, subunit A, domain 1","_id":"685af523b4ac24d5329d7c7d"},{"start":817,"end":906,"id":"3.30.70.270","name":"3.30.70.270","_id":"685af523b4ac24d5329d7c7e"},{"start":680,"end":816,"id":"3.30.70.270","name":"3.30.70.270","_id":"685af523b4ac24d5329d7c7f"},{"start":348,"end":387,"id":"1.20.5.760","name":"Single helix bin","_id":"685af523b4ac24d5329d7c80"},{"start":388,"end":431,"id":"4.10.60.10","name":"Zinc finger, CCHC-type","_id":"685af523b4ac24d5329d7c81"},{"start":907,"end":1015,"id":"3.30.70.270","name":"3.30.70.270","_id":"685af523b4ac24d5329d7c82"}]},"genes":[{"name":{"value":"gag-pol","evidences":[],"_id":"685af523b4ac24d5329d7d12"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d7d11"}],"length":1435,"name":"Gag-Pol polyprotein","ncbi_taxon_id":11698,"organism":"Human immunodeficiency virus type 1 group M subtype B (isolate NY5)","regions_counter":31,"released":"2016_10","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"UniParc":"UPI0000131EEB","uniref100":"UniRef100_P12497","uniref50":"UniRef50_P04585","uniref90":"UniRef90_P04585","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"statements":[{"type":"Abstract","text":"We report the NMR structure of the [W184A/M185A]-CTD mutant in its monomeric form. ","_id":"685af523b4ac24d5329d7c94"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp184Ala","_id":"685af523b4ac24d5329d7c93"},{"statements":[{"type":"Abstract","text":"We report the NMR structure of the [W184A/M185A]-CTD mutant in its monomeric form. ","_id":"685af523b4ac24d5329d7c96"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met1858Ala","_id":"685af523b4ac24d5329d7c95"}],"cross_refs":[{"db":"PDB","id":"2JYG","_id":"685af523b4ac24d5329d7c91"},{"db":"PDB","id":"2JYL","_id":"685af523b4ac24d5329d7c92"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":354,"end":363,"interaction_partner":[],"reference_html":"Solution structure of a double mutant of the carboxy-terminal dimerization domain of the HIV-1 capsid protein. <i> Wong HC, Shin R, Krishna NR. </i> Biochemistry, 2008","reference_id":"18220423","region_id":"DP00410r005","released":"2022_03","sample":[],"sequence_construct":"TSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNAATETLLVQNANPDCKTILKALGPGATLEEMMTACQGVGGPGHKARVL","statement":[{"type":"Results","text":"Residues 222−231 at the carboxy terminus are disordered.","_id":"685af523b4ac24d5329d7c97"},{"type":"Curator statement","text":"Region 222-231 described in the publication corresponds to the 354-363 residues of the Gag-Pol polyprotein.","_id":"685af523b4ac24d5329d7c98"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T10:06:06.459Z","_id":"685af523b4ac24d5329d7c99"},"version":3,"_id":"685af523b4ac24d5329d7c90","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1BAJ","_id":"685af523b4ac24d5329d7c9b"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":351,"end":377,"interaction_partner":[],"reference_html":"Structures of the HIV-1 capsid protein dimerization domain at 2.6 A resolution. <i> Worthylake DK, Wang H, Yoo S, Sundquist WI, Hill CP. </i> Acta Crystallogr D Biol Crystallogr, 1999","reference_id":"10089398","region_id":"DP00410r006","released":"2022_03","sample":[],"sequence_construct":"MSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPGATLEEMMTACQGVGGPGHKARVLAEAMSQVTNPATIM","statement":[{"type":"Curator statement","text":"This region lacks of electron density in the PDB, indicating disorder. The peptide assessed in this publication is derived from the HIV-1 isolate NL4-3, however the IDR is 100% identical to this Uniprot.","_id":"685af523b4ac24d5329d7c9c"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T10:06:00.777Z","_id":"685af523b4ac24d5329d7c9d"},"version":3,"_id":"685af523b4ac24d5329d7c9a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2GOL","_id":"685af523b4ac24d5329d7ca2"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":108,"end":143,"interaction_partner":[],"reference_html":"Implications for viral capsid assembly from crystal structures of HIV-1 Gag(1-278) and CA(N)(133-278). <i> Kelly BN, Howard BR, Wang H, Robinson H, Sundquist WI, Hill CP. </i> Biochemistry, 2006","reference_id":"16981686","region_id":"DP00410r008","released":"2022_03","sample":[],"sequence_construct":"MGARASVLSGGELDKWEKIRLRPGGKKQYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTIAVLYCVHQRIDVKDTKEALDKIEEEQNKSKKKAQQAAADTGNNSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTHNPPIPVGEIYKRWIILGLNKIVRMYS","statement":[{"type":"Results","text":"The crystal structure indicates that Gag1-278 comprises ordered MA and CAN domains that are connected by a flexible linker (Figure 1a and b). ","_id":"685af523b4ac24d5329d7ca3"},{"type":"Results","text":"The last 25 residues of the Gag1-278 MA domain and the first 10 residues of the CAN domain are disordered and have been omitted from the refined model of Gag1-278. This flexibility for residues 108−143 could easily accommodate the ∼40 Å gap between the MA and CAN domains that has been inferred for immature virions from electron microscopy ( 12).","_id":"685af523b4ac24d5329d7ca4"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T10:04:41.983Z","_id":"685af523b4ac24d5329d7ca5"},"version":3,"_id":"685af523b4ac24d5329d7ca1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2GOL","_id":"685af523b4ac24d5329d7cae"},{"db":"PDB","id":"2GON","_id":"685af523b4ac24d5329d7caf"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":108,"end":143,"interaction_partner":[],"reference_html":"Implications for viral capsid assembly from crystal structures of HIV-1 Gag(1-278) and CA(N)(133-278). <i> Kelly BN, Howard BR, Wang H, Robinson H, Sundquist WI, Hill CP. </i> Biochemistry, 2006","reference_id":"16981686","region_id":"DP00410r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The last 25 residues of the Gag1-278 MA domain and the first 10 residues of the CAN domain are disordered and have been omitted from the refined model of Gag1-278. This flexibility for residues 108−143 could easily accommodate the ∼40 Å gap between the MA and CAN domains that has been inferred for immature virions from electron microscopy ( 12).","_id":"685af523b4ac24d5329d7cad"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T10:08:36.374Z","_id":"685af523b4ac24d5329d7cb0"},"version":1,"_id":"685af523b4ac24d5329d7cac","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1L6N","_id":"685af523b4ac24d5329d7cb2"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":123,"end":143,"interaction_partner":[],"reference_html":"Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein. <i> Tang C, Ndassa Y, Summers MF. </i> Nat Struct Biol, 2002","reference_id":"12032547","region_id":"DP00410r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Residues Gly 2–Ser 6, Gly 123–Val 143 and Pro 279–Leu 283 show relatively low {1H}-15N heteronuclear NOE (XNOE) and T2 relaxation values (Fig. 2), as well as few or no medium-range 1H-1H NOEs, indicating that these residues are conformationally labile. ","_id":"685af523b4ac24d5329d7cb3"},{"type":"Results","text":"Because no restraints were used for the mobile residues that connect the folded domains (Gly 123–Val 143) and no NOEs were observed between the domains, the relative orientation of the MA and CAN domains is not defined.","_id":"685af523b4ac24d5329d7cb4"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T10:08:34.822Z","_id":"685af523b4ac24d5329d7cb5"},"version":1,"_id":"685af523b4ac24d5329d7cb1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1L6N","_id":"685af523b4ac24d5329d7cb7"},{"db":"BMRB","id":"5316","_id":"685af523b4ac24d5329d7cb8"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":123,"end":143,"interaction_partner":[],"reference_html":"Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein. <i> Tang C, Ndassa Y, Summers MF. </i> Nat Struct Biol, 2002","reference_id":"12032547","region_id":"DP00410r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Residues Gly 2–Ser 6, Gly 123–Val 143 and Pro 279–Leu 283 show relatively low {1H}-15N heteronuclear NOE (XNOE) and T2 relaxation values (Fig. 2), as well as few or no medium-range 1H-1H NOEs, indicating that these residues are conformationally labile. ","_id":"685af523b4ac24d5329d7cb9"},{"type":"Results","text":"Because no restraints were used for the mobile residues that connect the folded domains (Gly 123–Val 143) and no NOEs were observed between the domains, the relative orientation of the MA and CAN domains is not defined.","_id":"685af523b4ac24d5329d7cba"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T10:03:48.892Z","_id":"685af523b4ac24d5329d7cbb"},"version":1,"_id":"685af523b4ac24d5329d7cb6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1L6N","_id":"685af523b4ac24d5329d7cbd"},{"db":"PDB","id":"1GWP","_id":"685af523b4ac24d5329d7cbe"},{"db":"BMRB","id":"5316","_id":"685af523b4ac24d5329d7cbf"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":217,"end":231,"interaction_partner":[],"reference_html":"Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein. <i> Tang C, Ndassa Y, Summers MF. </i> Nat Struct Biol, 2002","reference_id":"12032547","region_id":"DP00410r014","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Residues Pro 217–Pro 231, which include the CypA-binding site, form a conformationally flexible loop.","_id":"685af523b4ac24d5329d7cc0"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T10:03:43.272Z","_id":"685af523b4ac24d5329d7cc1"},"version":1,"_id":"685af523b4ac24d5329d7cbc","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1L6N","_id":"685af523b4ac24d5329d7cc3"},{"db":"BMRB","id":"5316","_id":"685af523b4ac24d5329d7cc4"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":133,"end":143,"interaction_partner":[],"reference_html":"Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein. <i> Tang C, Ndassa Y, Summers MF. </i> Nat Struct Biol, 2002","reference_id":"12032547","region_id":"DP00410r015","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In contrast, the conformation of residues Pro 133–Val 143 of Gag283 is substantially different from that observed in the mature CAN protein. No intermediate or long-range 1H-1H NOEs were observed for these residues in Gag283, and the chemical shift index data indicate that they exist in a random coil conformation (Fig. 2).","_id":"685af523b4ac24d5329d7cc5"},{"type":"Results","text":"The present findings confirm that the β-hairpin is unfolded in the immature protein and support the proposal that β-hairpin formation occurs subsequent to proteolytic cleavage of Gag, triggering capsid assembly4,12. ","_id":"685af523b4ac24d5329d7cc6"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T10:03:06.890Z","_id":"685af523b4ac24d5329d7cc7"},"version":1,"_id":"685af523b4ac24d5329d7cc2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1A43","_id":"685af523b4ac24d5329d7cc9"},{"db":"PDB","id":"1BAJ","_id":"685af523b4ac24d5329d7cca"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":352,"end":377,"interaction_partner":[],"reference_html":"Structures of the HIV-1 capsid protein dimerization domain at 2.6 A resolution. <i> Worthylake DK, Wang H, Yoo S, Sundquist WI, Hill CP. </i> Acta Crystallogr D Biol Crystallogr, 1999","reference_id":"10089398","region_id":"DP00410r016","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"This region lacks of electron density in the PDB, indicating disorder. The peptide assessed in this publication is derived from the HIV-1 isolate NL4-3, however the IDR is 100% identical to this Uniprot.","_id":"685af523b4ac24d5329d7ccb"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T10:02:24.042Z","_id":"685af523b4ac24d5329d7ccc"},"version":1,"_id":"685af523b4ac24d5329d7cc8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1ITG","_id":"685af523b4ac24d5329d7cce"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1288,"end":1300,"interaction_partner":[],"reference_html":"Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases. <i> Dyda F, Hickman AB, Jenkins TM, Engelman A, Craigie R, Davies DR. </i> Science, 1994","reference_id":"7801124","region_id":"DP00410r017","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"This region lacks of electron density in the PDB, indicating disorder.","_id":"685af523b4ac24d5329d7ccf"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T10:02:12.520Z","_id":"685af523b4ac24d5329d7cd0"},"version":1,"_id":"685af523b4ac24d5329d7ccd","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"position":null,"statements":[],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp131Trp","_id":"685af523b4ac24d5329d7cd4"},{"start":null,"end":null,"position":null,"statements":[],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe185Lys","_id":"685af523b4ac24d5329d7cd5"}],"cross_refs":[{"db":"PDB","id":"6VRG","_id":"685af523b4ac24d5329d7cd6"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1193,"end":1202,"interaction_partner":[],"reference_html":"Influence of the amino-terminal sequence on the structure and function of HIV integrase. <i> Eilers G, Gupta K, Allen A, Zhou J, Hwang Y, Cory MB, Bushman FD, Van Duyne G. </i> Retrovirology, 2020","reference_id":"32867805","region_id":"DP00410r018","released":"2022_03","sample":[],"sequence_construct":"FLDGIDKAQEEHEKYHSNWRAMASDFNLPPVVAKEIVASCDKCQLKGEAMHGQVDCSPGIWQLDCTHLEGKVILVAVHVASGYIEAEVIPAETGQETAYFLLKLAGRWPVKTVHTDNGSNFTSTTVKAACDWAGIKQEDGIPYNPQSQGVIESMNKELKKIIGQVRDQAEHLKTAVQMAVFIHNKKRKGGIGGYSAGERIVDIIATDIQTKE","statement":[{"type":"Results","text":"Four copies of both the NTD and the CCD were present in the asymmetric unit (Fig. 1a), with the inter-domain linker (residues 47–55) unresolved in the electron density.","_id":"685af523b4ac24d5329d7cd2"},{"type":"Curator statement","text":"Authors are referring to the 1193-1202 region of the Gag-Pol polyprotein that, as shown in the PDB, is disordered. ","_id":"685af523b4ac24d5329d7cd3"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-03T13:00:14.766Z","_id":"685af523b4ac24d5329d7cd7"},"version":1,"_id":"685af523b4ac24d5329d7cd1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"position":null,"statements":[],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp131Trp","_id":"685af523b4ac24d5329d7cd9"},{"start":null,"end":null,"position":null,"statements":[],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe185Lys","_id":"685af523b4ac24d5329d7cda"}],"cross_refs":[{"db":"PDB","id":"6VRG","_id":"685af523b4ac24d5329d7cdc"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1286,"end":1295,"interaction_partner":[],"reference_html":"Influence of the amino-terminal sequence on the structure and function of HIV integrase. <i> Eilers G, Gupta K, Allen A, Zhou J, Hwang Y, Cory MB, Bushman FD, Van Duyne G. </i> Retrovirology, 2020","reference_id":"32867805","region_id":"DP00410r019","released":"2022_03","sample":[],"sequence_construct":"FLDGIDKAQEEHEKYHSNWRAMASDFNLPPVVAKEIVASCDKCQLKGEAMHGQVDCSPGIWQLDCTHLEGKVILVAVHVASGYIEAEVIPAETGQETAYFLLKLAGRWPVKTVHTDNGSNFTSTTVKAACDWAGIKQEDGIPYNPQSQGVIESMNKELKKIIGQVRDQAEHLKTAVQMAVFIHNKKRKGGIGGYSAGERIVDIIATDIQTKE","statement":[{"type":"Curator statement","text":"This region lacks electron density, indicating disorder, as shown in the PDB.","_id":"685af523b4ac24d5329d7cdb"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-03T13:00:13.639Z","_id":"685af523b4ac24d5329d7cdd"},"version":1,"_id":"685af523b4ac24d5329d7cd8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2MGU","_id":"685af523b4ac24d5329d7cdf"},{"db":"BMRB","id":"19604","_id":"685af523b4ac24d5329d7ce0"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":8,"end":31,"interaction_partner":[],"reference_html":"Solution structure of calmodulin bound to the binding domain of the HIV-1 matrix protein. <i> Vlach J, Samal AB, Saad JS. </i> J Biol Chem, 2014","reference_id":"24500712","region_id":"DP00410r020","released":"2022_03","sample":[{"db":"UniProt","deviation":null,"id":"P0DP29","statements":[{"type":"Results","text":"A summary of the NOE distance restraints is shown in Table 1. A total of 187 intermolecular NOEs detected between MA-(8–43) and CaM residues were used in the structure calculations. ","_id":"685af523b4ac24d5329d7ce4"}],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7ce3"}],"statement":[{"type":"Results","text":"Consistent with these observations, the CaM·MA-(8–43) structure shows that residues Asp14–Arg20 and Leu31–Glu40 of MA-(8–43) are α-helical, whereas residues Leu21–Gln28 connecting the two MA α-helices, residues Leu8–Leu13 and Leu41–Arg43, lack a regular secondary structure (Fig. 5A).","_id":"685af523b4ac24d5329d7ce1"},{"type":"Curator statement","text":"Region comprised between 14-20 residues is too short to be considered structured. Despite this publication is about Human immunodeficiency virus type 1 group M subtype B (isolate NY5) matrix protein, IDR is 100% identical.","_id":"685af523b4ac24d5329d7ce2"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-03T13:00:12.561Z","_id":"685af523b4ac24d5329d7ce5"},"version":1,"_id":"685af523b4ac24d5329d7cde","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"IDA","ec_id":"ECO:0001191","ec_name":"in vitro cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":44,"end":114,"interaction_partner":[],"reference_html":"NMR, biophysical, and biochemical studies reveal the minimal Calmodulin binding domain of the HIV-1 matrix protein. <i> Samal AB, Ghanam RH, Fernandez TF, Monroe EB, Saad JS. </i> J Biol Chem, 2011","reference_id":"21799007","region_id":"DP00410r021","released":"2022_03","sample":[{"db":"UniProt","deviation":null,"id":"P0DP29","statements":[],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7ce9"}],"statement":[{"type":"Results","text":"Digestion reactions were conducted on the myr(−)MA-CaM complex as well as unbound myr(−)MA and CaM. The complex was subjected to limited proteolysis by the addition of thermolysin (from B. thermoproteolyticus rokko) at 1:1000 (enzyme:complex) molar ratio (see “Experimental Procedures” for more details). After 2 h, the MA protein was readily cleaved, whereas the CaM protein was intact (Fig. 6). Digestion of the complex has resulted in an ∼5-kDa MA peptide that was resistant to proteolysis. Analysis of the digestion products by mass spectrometry revealed that the abundant MA species that was resistant to proteolysis is a peptide spanning residues 7–43 with monoisotopic mass of 4403.47 Da (Fig. 6) as identified by both exact mass measurements and tandem mass spectrometric sequencing. Another closely related minor species for residues 7–44 was also detected (supplemental Fig. S3). On the other hand, digestion of unbound MA resulted in a cleavage of a flexible helix on the C-terminal domain leaving intact residues 1–114 (Fig. 6).","_id":"685af523b4ac24d5329d7ce7"},{"type":"Results","text":"In addition, it appears that when compared with the unbound MA protein, CaM binding to MA induced significant conformational changes that facilitated cleavage by thermolysin.","_id":"685af523b4ac24d5329d7ce8"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-03T13:00:39.161Z","_id":"685af523b4ac24d5329d7cea"},"version":1,"_id":"685af523b4ac24d5329d7ce6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0001191","ec_name":"in vitro cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":44,"end":132,"interaction_partner":[],"reference_html":"NMR, biophysical, and biochemical studies reveal the minimal Calmodulin binding domain of the HIV-1 matrix protein. <i> Samal AB, Ghanam RH, Fernandez TF, Monroe EB, Saad JS. </i> J Biol Chem, 2011","reference_id":"21799007","region_id":"DP00410r022","released":"2022_03","sample":[{"db":"UniProt","deviation":null,"id":"P0DP29","statements":[{"type":"Results","text":"Digestion reactions were conducted on the myr(−)MA-CaM complex as well as unbound myr(−)MA and CaM. The complex was subjected to limited proteolysis by the addition of thermolysin (from B. thermoproteolyticus rokko) at 1:1000 (enzyme:complex) molar ratio (see “Experimental Procedures” for more details). ","_id":"685af523b4ac24d5329d7ced"}],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7cec"}],"statement":[{"type":"Results","text":"Digestion of the complex has resulted in an ∼5-kDa MA peptide that was resistant to proteolysis. Analysis of the digestion products by mass spectrometry revealed that the abundant MA species that was resistant to proteolysis is a peptide spanning residues 7–43 with monoisotopic mass of 4403.47 Da (Fig. 6) as identified by both exact mass measurements and tandem mass spectrometric sequencing.","_id":"685af523b4ac24d5329d7cee"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-03T09:00:05.179Z","_id":"685af523b4ac24d5329d7cef"},"version":1,"_id":"685af523b4ac24d5329d7ceb","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0001191","ec_name":"in vitro cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":115,"end":132,"interaction_partner":[],"reference_html":"NMR, biophysical, and biochemical studies reveal the minimal Calmodulin binding domain of the HIV-1 matrix protein. <i> Samal AB, Ghanam RH, Fernandez TF, Monroe EB, Saad JS. </i> J Biol Chem, 2011","reference_id":"21799007","region_id":"DP00410r023","released":"2022_03","sample":[{"db":"UniProt","deviation":null,"id":"P0DP29","statements":[{"type":"Results","text":"Digestion reactions were conducted on the myr(−)MA-CaM complex as well as unbound myr(−)MA and CaM. The complex was subjected to limited proteolysis by the addition of thermolysin (from B. thermoproteolyticus rokko) at 1:1000 (enzyme:complex) molar ratio (see “Experimental Procedures” for more details). ","_id":"685af523b4ac24d5329d7cf2"}],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7cf1"}],"statement":[{"type":"Results","text":"On the other hand, digestion of unbound MA resulted in a cleavage of a flexible helix on the C-terminal domain leaving intact residues 1–114 (Fig. 6).","_id":"685af523b4ac24d5329d7cf3"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-03T09:00:12.662Z","_id":"685af523b4ac24d5329d7cf4"},"version":1,"_id":"685af523b4ac24d5329d7cf0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":8,"end":43,"interaction_partner":[],"reference_html":"NMR, biophysical, and biochemical studies reveal the minimal Calmodulin binding domain of the HIV-1 matrix protein. <i> Samal AB, Ghanam RH, Fernandez TF, Monroe EB, Saad JS. </i> J Biol Chem, 2011","reference_id":"21799007","region_id":"DP00410r024","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The CD spectrum of the free peptide displays a negative band at ∼200 nm, consistent with a random coil, whereas that of the CaM protein shows two minima at 208 and 222 nm, consistent with a helical structure of the protein.","_id":"685af523b4ac24d5329d7cf6"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-03T09:00:17.346Z","_id":"685af523b4ac24d5329d7cf7"},"version":1,"_id":"685af523b4ac24d5329d7cf5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":8,"end":43,"interaction_partner":[],"reference_html":"NMR, biophysical, and biochemical studies reveal the minimal Calmodulin binding domain of the HIV-1 matrix protein. <i> Samal AB, Ghanam RH, Fernandez TF, Monroe EB, Saad JS. </i> J Biol Chem, 2011","reference_id":"21799007","region_id":"DP00410r025","released":"2022_03","sample":[{"db":"UniProt","deviation":null,"id":"P0DP29","statements":[],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7cfa"}],"statement":[{"type":"Results","text":"The CD spectrum of the free peptide displays a negative band at ∼200 nm, consistent with a random coil, whereas that of the CaM protein shows two minima at 208 and 222 nm, consistent with a helical structure of the protein. The CD spectrum of the complex is similar to that of the CaM protein, with features distinctive of α-helical type (supplemental Fig. S5). Binding of MA-(8–43) results only in a slight increase of CD minima of CaM, suggesting an increase in the α-helical character.","_id":"685af523b4ac24d5329d7cf9"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-03T13:00:33.370Z","_id":"685af523b4ac24d5329d7cfb"},"version":1,"_id":"685af523b4ac24d5329d7cf8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":8,"end":43,"interaction_partner":[],"reference_html":"NMR, biophysical, and biochemical studies reveal the minimal Calmodulin binding domain of the HIV-1 matrix protein. <i> Samal AB, Ghanam RH, Fernandez TF, Monroe EB, Saad JS. </i> J Biol Chem, 2011","reference_id":"21799007","region_id":"DP00410r026","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The two-dimensional HSQC data obtained for a 15N-labeled MA-(8–43) shows a narrow dispersion of the amide proton resonances, indicating a lack of ordered structure (supplemental Fig. S6).","_id":"685af523b4ac24d5329d7cfd"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-03T13:00:18.010Z","_id":"685af523b4ac24d5329d7cfe"},"version":1,"_id":"685af523b4ac24d5329d7cfc","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":8,"end":43,"interaction_partner":[],"reference_html":"NMR, biophysical, and biochemical studies reveal the minimal Calmodulin binding domain of the HIV-1 matrix protein. <i> Samal AB, Ghanam RH, Fernandez TF, Monroe EB, Saad JS. </i> J Biol Chem, 2011","reference_id":"21799007","region_id":"DP00410r027","released":"2022_03","sample":[{"db":"UniProt","deviation":null,"id":"P0DP29","statements":[],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d7d00"}],"statement":[{"type":"Results","text":"The two-dimensional HSQC data obtained for a 15N-labeled MA-(8–43) shows a narrow dispersion of the amide proton resonances, indicating a lack of ordered structure (supplemental Fig. S6). Upon binding of CaM, almost all 1H,15N signals of MA-(8–43) exhibited substantial chemical shift changes resulting in large chemical shift dispersion, which indicates that the peptide adopts an ordered structure upon binding to CaM.","_id":"685af523b4ac24d5329d7d01"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-03T13:00:24.167Z","_id":"685af523b4ac24d5329d7d02"},"version":1,"_id":"685af523b4ac24d5329d7cff","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":8,"end":43,"interaction_partner":[{"db":"UniProt","id":"P0DP29","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7d04"}],"reference_html":"NMR, biophysical, and biochemical studies reveal the minimal Calmodulin binding domain of the HIV-1 matrix protein. <i> Samal AB, Ghanam RH, Fernandez TF, Monroe EB, Saad JS. </i> J Biol Chem, 2011","reference_id":"21799007","region_id":"DP00410r028","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Digestion of the complex has resulted in an ∼5-kDa MA peptide that was resistant to proteolysis. Analysis of the digestion products by mass spectrometry revealed that the abundant MA species that was resistant to proteolysis is a peptide spanning residues 7–43 with monoisotopic mass of 4403.47 Da (Fig. 6) as identified by both exact mass measurements and tandem mass spectrometric sequencing.","_id":"685af523b4ac24d5329d7d05"},{"type":"Results","text":"\nProteolysis data clearly indicate that MA residues 7–43 are protected upon binding to CaM.","_id":"685af523b4ac24d5329d7d06"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-03T14:59:09.191Z","_id":"685af523b4ac24d5329d7d07"},"version":1,"_id":"685af523b4ac24d5329d7d03","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":8,"end":43,"interaction_partner":[{"db":"UniProt","id":"P0DP29","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7d09"}],"reference_html":"NMR, biophysical, and biochemical studies reveal the minimal Calmodulin binding domain of the HIV-1 matrix protein. <i> Samal AB, Ghanam RH, Fernandez TF, Monroe EB, Saad JS. </i> J Biol Chem, 2011","reference_id":"21799007","region_id":"DP00410r029","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Upon binding of CaM, almost all 1H,15N signals of MA-(8–43) exhibited substantial chemical shift changes resulting in large chemical shift dispersion, which indicates that the peptide adopts an ordered structure upon binding to CaM.","_id":"685af523b4ac24d5329d7d0a"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-03T13:00:43.085Z","_id":"685af523b4ac24d5329d7d0b"},"version":1,"_id":"685af523b4ac24d5329d7d08","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005647","ec_name":"isothermal titration calorimetry evidence used in manual assertion","ec_ontology":"ECO","start":8,"end":43,"interaction_partner":[{"db":"UniProt","id":"P0DP29","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7d0d"}],"reference_html":"NMR, biophysical, and biochemical studies reveal the minimal Calmodulin binding domain of the HIV-1 matrix protein. <i> Samal AB, Ghanam RH, Fernandez TF, Monroe EB, Saad JS. </i> J Biol Chem, 2011","reference_id":"21799007","region_id":"DP00410r030","released":"2022_03","sample":[],"statement":[{"type":"Results","text":" Thermodynamic data revealed that MA-(8–43) binds to CaM with 1:1 stoichiometry (Fig. 7). Strikingly, the binding affinity is much tighter (Kd = 25 nm) than that observed for all peptides described above (Table 1). What is even more intriguing is that the binding affinity of MA-(8–43) to CaM is 32-fold tighter than that of MA-(11–46), suggesting that residues Leu-8, Ser-9, and Gly-10 of MA contribute to the stabilization of the complex.","_id":"685af523b4ac24d5329d7d0e"},{"type":"Results","text":"To assess the role of electrostatic and hydrophobic factors, ITC data were obtained for MA-(8–43) as titrated with CaM at high salt concentration (500 mm NaCl). Our data revealed that the binding affinity (Kd = 60 nm) is only reduced by ∼2-fold upon increasing the salt concentration from 50 to 500 mm (Fig. 7), indicating that electrostatic interactions are not important in stabilizing the CaM-MA-(8–43) complex. This result is also consistent with that obtained for CaM binding to the full-length MA protein (46), indicating that interactions between CaM and MA-(8–43) are mainly hydrophobic.","_id":"685af523b4ac24d5329d7d0f"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-03T13:00:41.347Z","_id":"685af523b4ac24d5329d7d10"},"version":1,"_id":"685af523b4ac24d5329d7d0c","reference_source":"pmid"}],"__v":0,"disorder_content":0.14146341463414633,"disprot_consensus":{"full":[{"start":8,"end":114,"type":"T"},{"start":115,"end":143,"type":"D"},{"start":217,"end":231,"type":"D"},{"start":351,"end":377,"type":"D"},{"start":1193,"end":1202,"type":"D"},{"start":1286,"end":1300,"type":"D"}],"Structural state":[{"start":8,"end":143,"type":"D"},{"start":217,"end":231,"type":"D"},{"start":351,"end":377,"type":"D"},{"start":1193,"end":1202,"type":"D"},{"start":1286,"end":1300,"type":"D"}],"Disorder function":[{"start":108,"end":143,"type":"F"}],"Structural transition":[{"start":8,"end":114,"type":"T"}],"Molecular function":[{"start":8,"end":43,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00166","name":"Chaperonin 10 Kd subunit","start":2,"end":95}],"gene3D":[{"start":1,"end":97,"id":"2.30.33.40","name":"GroES chaperonin"}]},"uniref50":"UniRef50_P48228","sequence":"MNIRPLHDRVIVKRKEVETKSAGGIVLTGSAAAKSTRGEVLAVGNGRILENGEVKPLDVKVGDIVIFNDGYGVKSEKIDNEEVLIMSESDILAIVEA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_A7ZV11","disprot_id":"DP00412","ncbi_taxon_id":83334,"regions_counter":4,"creator":"ameszaros","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":31,"region_id":"DP00412r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A mobile loop order-disorder transition modulates the speed of chaperonin cycling. <i> Shewmaker F, Kerner MJ, Hayer-Hartl M, Klein G, Georgopoulos C, Landry SJ. </i> Protein Sci, 2004","term_id":"IDPO:0000002","curator_id":"ameszaros","start":17,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"15238634","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":31,"term_name":"protein folding chaperone","start":17,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ameszaros","released":"2022_03","term_ontology":"GO","curator_name":"Attila Meszaros","reference_id":"15238634","version":3,"reference_html":"A mobile loop order-disorder transition modulates the speed of chaperonin cycling. <i> Shewmaker F, Kerner MJ, Hayer-Hartl M, Klein G, Georgopoulos C, Landry SJ. </i> Protein Sci, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0044183","ec_id":"ECO:0006165","region_id":"DP00412r002","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":31,"term_name":"order to disorder","start":17,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ameszaros","released":"2022_03","term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"15238634","version":2,"reference_html":"A mobile loop order-disorder transition modulates the speed of chaperonin cycling. <i> Shewmaker F, Kerner MJ, Hayer-Hartl M, Klein G, Georgopoulos C, Landry SJ. </i> Protein Sci, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000014","ec_id":"ECO:0006165","region_id":"DP00412r003","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":31,"term_name":"protein binding","start":17,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ameszaros","released":"2022_03","term_ontology":"GO","curator_name":"Attila Meszaros","reference_id":"15238634","version":3,"reference_html":"A mobile loop order-disorder transition modulates the speed of chaperonin cycling. <i> Shewmaker F, Kerner MJ, Hayer-Hartl M, Klein G, Georgopoulos C, Landry SJ. </i> Protein Sci, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00412r004","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_A7ZV11","date":"2016-09-08T13:51:25.000Z","acc":"P0A6G1","name":"10 kDa chaperonin","length":97,"organism":"Escherichia coli O157:H7","dataset":[],"UniParc":"UPI0000000ED3","genes":[{"name":{"value":"groES","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00580","url":"https://hamap.expasy.org/unirule/MF_00580"}}]},"synonyms":[{"value":"groS","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00580","url":"https://hamap.expasy.org/unirule/MF_00580"}}]},{"value":"mopB"}],"olnNames":[{"value":"Z5747"},{"value":"ECs5123"}]}],"alphafold_very_low_content":0,"disorder_content":0.15463917525773196,"disprot_consensus":{"full":[{"start":17,"end":31,"type":"T"}],"Structural state":[{"start":17,"end":31,"type":"D"}],"Molecular function":[{"start":17,"end":31,"type":"F"}],"Structural transition":[{"start":17,"end":31,"type":"T"}]}},{"features":{"pfam":[{"id":"PF01258","name":"Prokaryotic dksA/traR C4-type zinc finger","start":110,"end":142},{"id":"PF21157","name":"DnaK suppressor protein DksA, N-terminal domain","start":36,"end":106}],"gene3D":[{"start":20,"end":150,"id":"1.20.120.910","name":"DksA, coiled-coil domain"}]},"uniref50":"UniRef50_P0ABS3","sequence":"MQEGQNRKTSSLSILAIAGVEPYQEKPGEEYMNEAQLAHFRRILEAWRNQLRDEVDRTVTHMQDEAANFPDPVDRAAQEEEFSLELRNRDRERKLIKKIEKTLKKVEDEDFGYCESCGVEIGIRRLEARPTADLCIDCKTLAEIREKQMAG","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0ABS3","disprot_id":"DP00414","ncbi_taxon_id":83333,"regions_counter":4,"creator":"agasparini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":33,"region_id":"DP00414r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Regulation through the secondary channel--structural framework for ppGpp-DksA synergism during transcription. <i> Perederina A, Svetlov V, Vassylyeva MN, Tahirov TH, Yokoyama S, Artsimovitch I, Vassylyev DG. </i> Cell, 2004","term_id":"IDPO:0000002","curator_id":"agasparini","start":17,"term_ontology":"IDPO","curator_name":"Alessandra Gasparini","reference_id":"15294156","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1TJL"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P0ABS3","date":"2016-09-09T17:15:12.000Z","acc":"P0ABS1","name":"RNA polymerase-binding transcription factor DksA","length":151,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI0000000B51","genes":[{"name":{"value":"dksA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00926","url":"https://hamap.expasy.org/unirule/MF_00926"}}]},"olnNames":[{"value":"b0145"},{"value":"JW0141"}]}],"alphafold_very_low_content":0.0728476821192053,"disorder_content":0.11258278145695365,"disprot_consensus":{"full":[{"start":17,"end":33,"type":"D"}],"Structural state":[{"start":17,"end":33,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00364","name":"Biotin-requiring enzyme","start":83,"end":155},{"id":"PF30639","name":"Domain of unknown function (DUF8684)","start":4,"end":33}],"gene3D":[{"start":77,"end":156,"id":"2.40.50.100","name":"2.40.50.100"}]},"uniref50":"UniRef50_P37799","sequence":"MDIRKIKKLIELVEESGISELEISEGEESVRISRAAPAASFPVMQQAYAAPMMQQPAQSNAAAPATVPSMEAPAAAEISGHIVRSPMVGTFYRTPSPDAKAFIEVGQKVNVGDTLCIVEAMKMMNQIEADKSGTVKAILVESGQPVEFDEPLVVIE","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0ABE0","disprot_id":"DP00415","ncbi_taxon_id":83334,"regions_counter":2,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":76,"region_id":"DP00415r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Interchangeable enzyme modules. Functional replacement of the essential linker of the biotinylated subunit of acetyl-CoA carboxylase with a linker from the lipoylated subunit of pyruvate dehydrogenase. <i> Cronan JE. </i> J Biol Chem, 2002","term_id":"IDPO:0000002","curator_id":"nmurvai","start":49,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"11956202","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":76,"term_name":"flexible linker","start":49,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"11956202","version":3,"reference_html":"Interchangeable enzyme modules. Functional replacement of the essential linker of the biotinylated subunit of acetyl-CoA carboxylase with a linker from the lipoylated subunit of pyruvate dehydrogenase. <i> Cronan JE. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006165","region_id":"DP00415r002","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_P0ABE0","date":"2016-09-07T22:44:52.000Z","acc":"P0ABE0","name":"Biotin carboxyl carrier protein of acetyl-CoA carboxylase","length":156,"organism":"Escherichia coli O157:H7","dataset":[],"UniParc":"UPI00000480B6","genes":[{"name":{"value":"accB"},"olnNames":[{"value":"Z4615"},{"value":"ECs4127"}]}],"alphafold_very_low_content":0.1794871794871795,"disorder_content":0.1794871794871795,"disprot_consensus":{"full":[{"start":49,"end":76,"type":"D"}],"Structural state":[{"start":49,"end":76,"type":"D"}],"Disorder function":[{"start":49,"end":76,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00008","name":"EGF-like domain","start":300,"end":332},{"id":"PF00008","name":"EGF-like domain","start":340,"end":370},{"id":"PF00008","name":"EGF-like domain","start":378,"end":408},{"id":"PF00008","name":"EGF-like domain","start":748,"end":777},{"id":"PF00008","name":"EGF-like domain","start":786,"end":815},{"id":"PF01414","name":"Delta serrate ligand","start":187,"end":231},{"id":"PF07657","name":"N terminus of Notch ligand C2-like domain","start":32,"end":185},{"id":"PF12661","name":"Human growth factor-like EGF","start":714,"end":735},{"id":"PF12661","name":"Human growth factor-like EGF","start":829,"end":849},{"id":"PF21700","name":"Delta-like/Jagged, EGF-like domain","start":272,"end":297},{"id":"PF23575","name":"Protein jagged-1-like, predicted ferredoxin-like domain","start":948,"end":1058},{"id":"PF25024","name":"Teneurin EGF domain","start":433,"end":682}],"gene3D":[{"start":188,"end":233,"id":"2.10.25.140","name":"2.10.25.140"},{"start":32,"end":187,"id":"2.60.40.3510","name":"2.60.40.3510"},{"start":338,"end":376,"id":"2.10.25.10","name":"Laminin"},{"start":632,"end":668,"id":"2.10.25.10","name":"Laminin"},{"start":452,"end":489,"id":"2.10.25.10","name":"Laminin"},{"start":414,"end":451,"id":"2.10.25.10","name":"Laminin"},{"start":490,"end":526,"id":"2.10.25.10","name":"Laminin"},{"start":377,"end":413,"id":"2.10.25.10","name":"Laminin"},{"start":595,"end":631,"id":"2.10.25.10","name":"Laminin"},{"start":669,"end":706,"id":"2.10.25.10","name":"Laminin"},{"start":822,"end":857,"id":"2.10.25.10","name":"Laminin"},{"start":527,"end":562,"id":"2.10.25.10","name":"Laminin"},{"start":747,"end":784,"id":"2.10.25.10","name":"Laminin"},{"start":296,"end":337,"id":"2.10.25.10","name":"Laminin"},{"start":234,"end":295,"id":"2.10.25.10","name":"Laminin"},{"start":785,"end":821,"id":"2.10.25.10","name":"Laminin"},{"start":707,"end":746,"id":"2.10.25.10","name":"Laminin"}]},"uniref50":"UniRef50_P78504","sequence":"MRSPRTRGRSGRPLSLLLALLCALRAKVCGASGQFELEILSMQNVNGELQNGNCCGGARNPGDRKCTRDECDTYFKVCLKEYQSRVTAGGPCSFGSGSTPVIGGNTFNLKASRGNDRNRIVLPFSFAWPRSYTLLVEAWDSSNDTVQPDSIIEKASHSGMINPSRQWQTLKQNTGVAHFEYQIRVTCDDYYYGFGCNKFCRPRDDFFGHYACDQNGNKTCMEGWMGPECNRAICRQGCSPKHGSCKLPGDCRCQYGWQGLYCDKCIPHPGCVHGICNEPWQCLCETNWGGQLCDKDLNYCGTHQPCLNGGTCSNTGPDKYQCSCPEGYSGPNCEIAEHACLSDPCHNRGSCKETSLGFECECSPGWTGPTCSTNIDDCSPNNCSHGGTCQDLVNGFKCVCPPQWTGKTCQLDANECEAKPCVNAKSCKNLIASYYCDCLPGWMGQNCDININDCLGQCQNDASCRDLVNGYRCICPPGYAGDHCERDIDECASNPCLNGGHCQNEINRFQCLCPTGFSGNLCQLDIDYCEPNPCQNGAQCYNRASDYFCKCPEDYEGKNCSHLKDHCRTTPCEVIDSCTVAMASNDTPEGVRYISSNVCGPHGKCKSQSGGKFTCDCNKGFTGTYCHENINDCESNPCRNGGTCIDGVNSYKCICSDGWEGAYCETNINDCSQNPCHNGGTCRDLVNDFYCDCKNGWKGKTCHSRDSQCDEATCNNGGTCYDEGDAFKCMCPGGWEGTTCNIARNSSCLPNPCHNGGTCVVNGESFTCVCKEGWEGPICAQNTNDCSPHPCYNSGTCVDGDNWYRCECAPGFAGPDCRININECQSSPCAFGATCVDEINGYRCVCPPGHSGAKCQEVSGRPCITMGSVIPDGAKWDDDCNTCQCLNGRIACSKVWCGPRPCLLHKGHSECPSGQSCIPILDDQCFVHPCTGVGECRSSSLQPVKTKCTSDSYYQDNCANITFTFNKEMMSPGLTTEHICSELRNLNILKNVSAEYSIYIACEPSPSANNEIHVAISAEDIRDDGNPIKEITDKIIDLVSKRDGNSSLIAAVAEVRVQRRPLKNRTDFLVPLLSSVLTVAWICCLVTAFYWCLRKRRKPGSHTHSASEDNTTNNVREQLNQIKNPIEKHGANTVPIKDYENKNSKMSKIRTHNSEVEEDDMDKHQQKARFAKQPAYTLVDREEKPPNGTPTKHPNWTNKQDNRDLESAQSLNRMEYIV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P78504","disprot_id":"DP00418","ncbi_taxon_id":9606,"regions_counter":21,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1218,"region_id":"DP00418r001","released":"2026_06","ec_id":"ECO:0006204","reference_html":"Gene synthesis, expression, purification, and characterization of human Jagged-1 intracellular region. <i> Popovic M, Coglievina M, Guarnaccia C, Verdone G, Esposito G, Pintar A, Pongor S. </i> Protein Expr Purif, 2006","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1094,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16427310","version":5,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2026-06-17T15:59:54.566Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","statement":[{"text":"Far-UV CD spectra Fig. 6 show a strong minimum at ∼200 nm, which is typical of random coil polypeptides or unfolded proteins.","type":"Results"}]},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":1218,"term_name":"flexible C-terminal tail","start":1094,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"vnugnes","released":"2026_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16427310","version":6,"reference_html":"Gene synthesis, expression, purification, and characterization of human Jagged-1 intracellular region. <i> Popovic M, Coglievina M, Guarnaccia C, Verdone G, Esposito G, Pintar A, Pongor S. </i> Protein Expr Purif, 2006","date":"2026-06-17T16:04:09.154Z","term_id":"IDPO:0000031","ec_id":"ECO:0006204","region_id":"DP00418r002","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Disorder function","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","statement":[{"text":"Overall, CD, fluorescence and NMR data are consistent with the lack of tertiary structure and the presence of very little or no secondary structure, thus suggesting that in the experimental conditions tested JAGIC behaves as a mainly disordered protein in solution [18].","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1218,"region_id":"DP00418r005","released":"2026_06","ec_id":"ECO:0006198","reference_html":"Gene synthesis, expression, purification, and characterization of human Jagged-1 intracellular region. <i> Popovic M, Coglievina M, Guarnaccia C, Verdone G, Esposito G, Pintar A, Pongor S. </i> Protein Expr Purif, 2006","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1094,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16427310","version":5,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2026-06-17T15:59:35.603Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","statement":[{"text":"1H NMR spectra (Fig. 8) show very little dispersion in the chemical shift of both the backbone NH and the Hα protons, most of them being clustered in the 8.0–8.5 and 3.9–4.9 ppm range, respectively.","type":"Results"}]},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":1218,"term_name":"flexible C-terminal tail","start":1094,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2026_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16427310","version":6,"reference_html":"Gene synthesis, expression, purification, and characterization of human Jagged-1 intracellular region. <i> Popovic M, Coglievina M, Guarnaccia C, Verdone G, Esposito G, Pintar A, Pongor S. </i> Protein Expr Purif, 2006","date":"2026-06-17T16:04:23.724Z","term_id":"IDPO:0000031","ec_id":"ECO:0006165","region_id":"DP00418r006","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Disorder function","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","statement":[{"text":"Overall, CD, fluorescence and NMR data are consistent with the lack of tertiary structure and the presence of very little or no secondary structure, thus suggesting that in the experimental conditions tested JAGIC behaves as a mainly disordered protein in solution [18].","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1218,"region_id":"DP00418r009","released":"2026_06","ec_id":"ECO:0001249","reference_html":"Gene synthesis, expression, purification, and characterization of human Jagged-1 intracellular region. <i> Popovic M, Coglievina M, Guarnaccia C, Verdone G, Esposito G, Pintar A, Pongor S. </i> Protein Expr Purif, 2006","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1094,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16427310","version":3,"ec_name":"fluorescence evidence used in manual assertion","date":"2026-06-17T16:00:57.642Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","statement":[{"text":"The mainly disordered nature of JAG1IC in solution was confirmed by the lack of any detectable optical activity in the aromatic region (∼280 nm) (data not shown), by the position of the maximum in the tryptophan fluorescence spectra (355 nm) (Fig. 7) and by the very low value of the tryptophan fluorescence anisotropy (0.06).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1218,"region_id":"DP00418r013","released":"2026_06","ec_id":"ECO:0007691","reference_html":"Gene synthesis, expression, purification, and characterization of human Jagged-1 intracellular region. <i> Popovic M, Coglievina M, Guarnaccia C, Verdone G, Esposito G, Pintar A, Pongor S. </i> Protein Expr Purif, 2006","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1094,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16427310","version":3,"ec_name":"cleavage assay evidence used in manual assertion","date":"2026-06-17T16:01:30.543Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","disprot_namespace":"Structural state","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","statement":[{"text":"The time course of the reaction and the identification of many of the fragments by LC–MS also show that no particular region in JAG1IC is protected against proteolytic cleavage (Fig. 9). These results thus confirm that JAG1IC is essentially unstructured in solution.","type":"Results"}]},{"start":1121,"end":1126,"reference_id":"25747658","reference_source":"pmid","reference_html":"A tail of two sites: a bipartite mechanism for recognition of notch ligands by mind bomb E3 ligases. <i> McMillan BJ, Schnute B, Ohlenhard N, Zimmerman B, Miles L, Beglova N, Klein T, Blacklow SC. </i> Mol Cell, 2015","date":"2026-06-17T16:13:06.660Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031625","term_name":"ubiquitin protein ligase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"4XI7"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q86YT6","operator":null,"partner_start":26,"partner_end":56}],"region_id":"DP00418r017","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":null}],"sequence_construct":"NQIKNPIEKHG","statement":[{"text":"Both the Jag1 and Delta N-box peptides interact with the first Mib-Herc2 element, and are nestled in an elongated channel formed by β-strand 4 and the lengthy β1-β2 linker (Figure 3D,E).","type":"Results"},{"text":"Anchoring the peptide:Mib1 interaction is an invariant Asn residue (peptide position “0”) present in Jag1 and conserved in the aligned sequences of all homologs (N1124 and N684 in human Jag1 and Drosophila Delta, respectively; Figure 3B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.\" [GOC:vp]","term_is_obsolete":false,"term_not_annotate":false},{"start":1114,"end":1140,"reference_id":"25747658","reference_source":"pmid","reference_html":"A tail of two sites: a bipartite mechanism for recognition of notch ligands by mind bomb E3 ligases. <i> McMillan BJ, Schnute B, Ohlenhard N, Zimmerman B, Miles L, Beglova N, Klein T, Blacklow SC. </i> Mol Cell, 2015","date":"2026-06-17T16:27:03.657Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031625","term_name":"ubiquitin protein ligase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q86YT6","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00418r018","statement":[{"text":"Instead, we found an N-terminal segment proximal to the membrane (Figure 3A, in blue) and a segment near the C-terminus (in orange) that each accounted for a portion of the binding enthalpy associated with the full-length tail (in black; thermogram in Figure S2A). These findings suggested that Jag1 utilizes two discontinuous peptide motifs in forming complexes with Mib1.","type":"Results"},{"text":"The fusion protein bound to Mib1 with an affinity comparable to that of the full Jag1 tail (Figure 3A, Table S1) indicating that a combination of N- and C-terminal motifs reconstitutes full-strength binding affinity.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.\" [GOC:vp]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":1191,"end":1210,"reference_id":"25747658","reference_source":"pmid","reference_html":"A tail of two sites: a bipartite mechanism for recognition of notch ligands by mind bomb E3 ligases. <i> McMillan BJ, Schnute B, Ohlenhard N, Zimmerman B, Miles L, Beglova N, Klein T, Blacklow SC. </i> Mol Cell, 2015","date":"2026-06-17T16:26:04.920Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031625","term_name":"ubiquitin protein ligase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q86YT6","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00418r019","statement":[{"text":"Instead, we found an N-terminal segment proximal to the membrane (Figure 3A, in blue) and a segment near the C-terminus (in orange) that each accounted for a portion of the binding enthalpy associated with the full-length tail (in black; thermogram in Figure S2A). These findings suggested that Jag1 utilizes two discontinuous peptide motifs in forming complexes with Mib1.","type":"Results"},{"text":"The fusion protein bound to Mib1 with an affinity comparable to that of the full Jag1 tail (Figure 3A, Table S1) indicating that a combination of N- and C-terminal motifs reconstitutes full-strength binding affinity.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.\" [GOC:vp]","term_is_obsolete":false,"term_not_annotate":false},{"start":1185,"end":1218,"reference_id":"25747658","reference_source":"pmid","reference_html":"A tail of two sites: a bipartite mechanism for recognition of notch ligands by mind bomb E3 ligases. <i> McMillan BJ, Schnute B, Ohlenhard N, Zimmerman B, Miles L, Beglova N, Klein T, Blacklow SC. </i> Mol Cell, 2015","date":"2026-06-17T16:34:24.109Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031625","term_name":"ubiquitin protein ligase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q86YT6","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00418r020","statement":[{"text":"Titration of the Jag1 C-terminal segment into wild-type REP resulted in substantial line broadening of many peaks in the spectrum, consistent with a binding interaction between these two proteins (Figure 4E).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.\" [GOC:vp]","term_is_obsolete":false,"term_not_annotate":false},{"start":1198,"end":1203,"reference_id":"25747658","reference_source":"pmid","reference_html":"A tail of two sites: a bipartite mechanism for recognition of notch ligands by mind bomb E3 ligases. <i> McMillan BJ, Schnute B, Ohlenhard N, Zimmerman B, Miles L, Beglova N, Klein T, Blacklow SC. </i> Mol Cell, 2015","date":"2026-06-17T16:37:48.991Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031625","term_name":"ubiquitin protein ligase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys1199Glu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg1203Glu","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q86YT6","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00418r021","statement":[{"text":"When the KQDNRD epitope of the Jag1 C-box was mutated to EQDNED (K1199E/R1203E of human Jag1), binding of the Jag1 C-terminal segment to the REP protein was no longer detectable by ITC (Figure S3A).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.\" [GOC:vp]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_P78504","date":"2016-09-06T13:08:59.000Z","acc":"P78504","name":"Protein jagged-1","length":1218,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000498B5","genes":[{"name":{"value":"JAG1"},"synonyms":[{"value":"JAGL1"}]}],"alphafold_very_low_content":0.13218390804597702,"disorder_content":0.10262725779967159,"disprot_consensus":{"full":[{"start":1094,"end":1218,"type":"D"}],"Structural state":[{"start":1094,"end":1218,"type":"D"}],"Disorder function":[{"start":1094,"end":1218,"type":"F"}],"Molecular function":[{"start":1114,"end":1140,"type":"F"},{"start":1185,"end":1218,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01248","name":"Ribosomal protein L7Ae/L30e/S12e/Gadd45 family","start":660,"end":757}],"gene3D":[{"start":649,"end":767,"id":"3.30.1330.30","name":"3.30.1330.30"}]},"uniref50":"UniRef50_Q96T21","sequence":"MASEGPREPESEGIKLSADVKPFVPRFAGLNVAWLESSEACVFPSSAATYYPFVQEPPVTEQKIYTEDMAFGASTFPPQYLSSEITLHPYAYSPYTLDSTQNVYSVPGSQYLYNQPSCYRGFQTVKHRNENTCPLPQEMKALFKKKTYDEKKTYDQQKFDSERADGTISSEIKSARGSHHLSIYAENSLKSDGYHKRTDRKSRIIAKNVSTSKPEFEFTTLDFPELQGAENNMSEIQKQPKWGPVHSVSTDISLLREVVKPAAVLSKGEIVVKNNPNESVTANAATNSPSCTRELSWTPMGYVVRQTLSTELSAAPKNVTSMINLKTIASSADPKNVSIPSSEALSSDPSYNKEKHIIHPTQKSKASQGSDLEQNEASRKNKKKKEKSTSKYEVLTVQEPPRIEDAEEFPNLAVASERRDRIETPKFQSKQQPQDNFKNNVKKSQLPVQLDLGGMLTALEKKQHSQHAKQSSKPVVVSVGAVPVLSKECASGERGRRMSQMKTPHNPLDSSAPLMKKGKQREIPKAKKPTSLKKIILKERQERKQRLQENAVSPAFTSDDTQDGESGGDDQFPEQAELSGPEGMDELISTPSVEDKSEEPPGTELQRDTEASHLAPNHTTFPKIHSRRFRDYCSQMLSKEVDACVTDLLKELVRFQDRMYQKDPVKAKTKRRLVLGLREVLKHLKLKKLKCVIISPNCEKIQSKGGLDDTLHTIIDYACEQNIPFVFALNRKALGRSLNKAVPVSVVGIFSYDGAQDQFHKMVELTVAARQAYKTMLENVQQELVGEPRPQAPPSLPTQGPSCPAEDGPPALKEKEEPHYIEIWKKHLEAYSGCTLELEESLEASTSQMMNLNL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q96T21","disprot_id":"DP00420","ncbi_taxon_id":9606,"regions_counter":6,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":600,"region_id":"DP00420r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"SECIS-binding protein 2, a key player in selenoprotein synthesis, is an intrinsically disordered protein. <i> Oliéric V, Wolff P, Takeuchi A, Bec G, Birck C, Vitorino M, Kieffer B, Beniaminov A, Cavigiolio G, Theil E, Allmang C, Krol A, Dumas P. </i> Biochimie, 2009","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19467292","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":600,"term_name":"molecular function regulator","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19467292","version":3,"reference_html":"SECIS-binding protein 2, a key player in selenoprotein synthesis, is an intrinsically disordered protein. <i> Oliéric V, Wolff P, Takeuchi A, Bec G, Birck C, Vitorino M, Kieffer B, Beniaminov A, Cavigiolio G, Theil E, Allmang C, Krol A, Dumas P. </i> Biochimie, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006165","region_id":"DP00420r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":600,"term_name":"DNA binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19467292","version":3,"reference_html":"SECIS-binding protein 2, a key player in selenoprotein synthesis, is an intrinsically disordered protein. <i> Oliéric V, Wolff P, Takeuchi A, Bec G, Birck C, Vitorino M, Kieffer B, Beniaminov A, Cavigiolio G, Theil E, Allmang C, Krol A, Dumas P. </i> Biochimie, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003677","ec_id":"ECO:0006165","region_id":"DP00420r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":854,"region_id":"DP00420r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"SECIS-binding protein 2, a key player in selenoprotein synthesis, is an intrinsically disordered protein. <i> Oliéric V, Wolff P, Takeuchi A, Bec G, Birck C, Vitorino M, Kieffer B, Beniaminov A, Cavigiolio G, Theil E, Allmang C, Krol A, Dumas P. </i> Biochimie, 2009","term_id":"IDPO:0000002","curator_id":"fquaglia","start":776,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19467292","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":854,"term_name":"molecular function regulator","start":776,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19467292","version":3,"reference_html":"SECIS-binding protein 2, a key player in selenoprotein synthesis, is an intrinsically disordered protein. <i> Oliéric V, Wolff P, Takeuchi A, Bec G, Birck C, Vitorino M, Kieffer B, Beniaminov A, Cavigiolio G, Theil E, Allmang C, Krol A, Dumas P. </i> Biochimie, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006165","region_id":"DP00420r005","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":854,"term_name":"DNA binding","start":776,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19467292","version":3,"reference_html":"SECIS-binding protein 2, a key player in selenoprotein synthesis, is an intrinsically disordered protein. <i> Oliéric V, Wolff P, Takeuchi A, Bec G, Birck C, Vitorino M, Kieffer B, Beniaminov A, Cavigiolio G, Theil E, Allmang C, Krol A, Dumas P. </i> Biochimie, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003677","ec_id":"ECO:0006165","region_id":"DP00420r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q96T21","date":"2016-08-12T15:51:26.000Z","acc":"Q96T21","name":"Selenocysteine insertion sequence-binding protein 2","length":854,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000004EC79","genes":[{"name":{"value":"SECISBP2"},"synonyms":[{"value":"SBP2"}]}],"alphafold_very_low_content":0.6451990632318502,"disorder_content":0.7950819672131147,"disprot_consensus":{"full":[{"start":1,"end":600,"type":"D"},{"start":776,"end":854,"type":"D"}],"Structural state":[{"start":1,"end":600,"type":"D"},{"start":776,"end":854,"type":"D"}],"Molecular function":[{"start":1,"end":600,"type":"F"},{"start":776,"end":854,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05395","name":"Protein phosphatase inhibitor 1/DARPP-32","start":2,"end":178}]},"uniref50":"UniRef50_Q9UD71","sequence":"MDPKDRKKIQFSVPAPPSQLDPRQVEMIRRRRPTPAMLFRLSEHSSPEEEASPHQRASGEGHHLKSKRSNPCAYTPPSLKAVQRIAESHLQSISNLGENQASEEEDELGELRELGYPREEEEEEEEEDEEEEEDSQAEVLKGSRGSAGQKTTYGQGLEGPWERPPPLDGPQRDGSSEDQVEDPALNEPGEEPQRPAHPEPGT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P07516","disprot_id":"DP00421","ncbi_taxon_id":9913,"regions_counter":9,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":202,"region_id":"DP00421r001","released":"2022_03","ec_id":"ECO:0007689","reference_html":"DARPP-32, a dopamine- and adenosine 3':5'-monophosphate-regulated phosphoprotein enriched in dopamine-innervated brain regions. II. Purification and characterization of the phosphoprotein from bovine caudate nucleus. <i> Hemmings HC, Nairn AC, Aswad DW, Greengard P. </i> J Neurosci, 1984","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"6319628","version":2,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":202,"term_name":"molecular function inhibitor activity","start":1,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"6319628","version":3,"reference_html":"DARPP-32, a dopamine- and adenosine 3':5'-monophosphate-regulated phosphoprotein enriched in dopamine-innervated brain regions. II. Purification and characterization of the phosphoprotein from bovine caudate nucleus. <i> Hemmings HC, Nairn AC, Aswad DW, Greengard P. </i> J Neurosci, 1984","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140678","ec_id":"ECO:0007689","region_id":"DP00421r002","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":202,"term_name":"protein binding","start":1,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"6319628","version":3,"reference_html":"DARPP-32, a dopamine- and adenosine 3':5'-monophosphate-regulated phosphoprotein enriched in dopamine-innervated brain regions. II. Purification and characterization of the phosphoprotein from bovine caudate nucleus. <i> Hemmings HC, Nairn AC, Aswad DW, Greengard P. </i> J Neurosci, 1984","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007689","region_id":"DP00421r003","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":202,"region_id":"DP00421r004","released":"2022_03","ec_id":"ECO:0006275","reference_html":"DARPP-32, a dopamine- and adenosine 3':5'-monophosphate-regulated phosphoprotein enriched in dopamine-innervated brain regions. II. Purification and characterization of the phosphoprotein from bovine caudate nucleus. <i> Hemmings HC, Nairn AC, Aswad DW, Greengard P. </i> J Neurosci, 1984","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"6319628","version":2,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":202,"term_name":"molecular function inhibitor activity","start":1,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"6319628","version":3,"reference_html":"DARPP-32, a dopamine- and adenosine 3':5'-monophosphate-regulated phosphoprotein enriched in dopamine-innervated brain regions. II. Purification and characterization of the phosphoprotein from bovine caudate nucleus. <i> Hemmings HC, Nairn AC, Aswad DW, Greengard P. </i> J Neurosci, 1984","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140678","ec_id":"ECO:0006275","region_id":"DP00421r005","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":202,"term_name":"protein binding","start":1,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"6319628","version":3,"reference_html":"DARPP-32, a dopamine- and adenosine 3':5'-monophosphate-regulated phosphoprotein enriched in dopamine-innervated brain regions. II. Purification and characterization of the phosphoprotein from bovine caudate nucleus. <i> Hemmings HC, Nairn AC, Aswad DW, Greengard P. </i> J Neurosci, 1984","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006275","region_id":"DP00421r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":202,"region_id":"DP00421r007","released":"2022_03","ec_id":"ECO:0007680","reference_html":"DARPP-32, a dopamine- and adenosine 3':5'-monophosphate-regulated phosphoprotein enriched in dopamine-innervated brain regions. II. Purification and characterization of the phosphoprotein from bovine caudate nucleus. <i> Hemmings HC, Nairn AC, Aswad DW, Greengard P. </i> J Neurosci, 1984","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"6319628","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":202,"term_name":"molecular function inhibitor activity","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"6319628","version":3,"reference_html":"DARPP-32, a dopamine- and adenosine 3':5'-monophosphate-regulated phosphoprotein enriched in dopamine-innervated brain regions. II. Purification and characterization of the phosphoprotein from bovine caudate nucleus. <i> Hemmings HC, Nairn AC, Aswad DW, Greengard P. </i> J Neurosci, 1984","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140678","ec_id":"ECO:0007680","region_id":"DP00421r008","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":202,"term_name":"protein binding","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"6319628","version":3,"reference_html":"DARPP-32, a dopamine- and adenosine 3':5'-monophosphate-regulated phosphoprotein enriched in dopamine-innervated brain regions. II. Purification and characterization of the phosphoprotein from bovine caudate nucleus. <i> Hemmings HC, Nairn AC, Aswad DW, Greengard P. </i> J Neurosci, 1984","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007680","region_id":"DP00421r009","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P07516","date":"2016-08-25T14:48:44.000Z","acc":"P07516","name":"Protein phosphatase 1 regulatory subunit 1B","length":202,"organism":"Bos taurus","dataset":[],"UniParc":"UPI000012D807","genes":[{"name":{"value":"PPP1R1B"}}],"alphafold_very_low_content":0.24752475247524752,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":202,"type":"D"}],"Structural state":[{"start":1,"end":202,"type":"D"}],"Molecular function":[{"start":1,"end":202,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02954","name":"Bacterial regulatory protein, Fis family","start":55,"end":95},{"id":"PF27465","name":"DNA-binding protein Fis N-terminal domain","start":1,"end":47}],"gene3D":[{"start":1,"end":98,"id":"1.10.10.60","name":"Homeodomain-like"}]},"uniref50":"UniRef50_A4WF77","sequence":"MFEQRVNSDVLTVSTVNSQDQVTQKPLRDSVKQALKNYFAQLNGQDVNDLYELVLAEVEQPLLDMVMQYTRGNQTRAALMMGINRGTLRKKLKKYGMN","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_A4WF77","disprot_id":"DP00422","ncbi_taxon_id":83333,"regions_counter":3,"creator":"nveljkovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":23,"region_id":"DP00422r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the factor for inversion stimulation FIS at 2.0 A resolution. <i> Kostrewa D, Granzin J, Stock D, Choe HW, Labahn J, Saenger W. </i> J Mol Biol, 1992","term_id":"IDPO:0000002","curator_id":"nveljkovic","start":1,"term_ontology":"IDPO","curator_name":"Nevena Veljkovic","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-6562-5800","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"1619650","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_A8AQG0","date":"2016-09-08T11:52:13.000Z","acc":"P0A6R3","name":"DNA-binding protein Fis","length":98,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI0000006216","genes":[{"name":{"value":"fis","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00166","url":"https://hamap.expasy.org/unirule/MF_00166"}}]},"olnNames":[{"value":"b3261"},{"value":"JW3229"}]}],"alphafold_very_low_content":0.030612244897959183,"disorder_content":0.23469387755102042,"disprot_consensus":{"full":[{"start":1,"end":23,"type":"D"}],"Structural state":[{"start":1,"end":23,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00538","name":"linker histone H1 and H5 family","start":45,"end":116},{"id":"PF00538","name":"linker histone H1 and H5 family","start":179,"end":250}],"gene3D":[{"start":38,"end":130,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"start":171,"end":258,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}]},"uniref50":"UniRef50_P53551","sequence":"MAPKKSTTKTTSKGKKPATSKGKEKSTSKAAIKKTTAKKEEASSKSYRELIIEGLTALKERKGSSRPALKKFIKENYPIVGSASNFDLYFNNAIKKGVEAGDFEQPKGPAGAVKLAKKKSPEVKKEKEVSPKPKQAATSVSATASKAKAASTKLAPKKVVKKKSPTVTAKKASSPSSLTYKEMILKSMPQLNDGKGSSRIVLKKYVKDTFSSKLKTSSNFDYLFNSAIKKCVENGELVQPKGPSGIIKLNKKKVKLST","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P53551","disprot_id":"DP00423","ncbi_taxon_id":559292,"regions_counter":18,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":258,"region_id":"DP00423r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Two homologous domains of similar structure but different stability in the yeast linker histone, Hho1p. <i> Ali T, Coles P, Stevens TJ, Stott K, Thomas JO. </i> J Mol Biol, 2004","term_id":"IDPO:0000002","curator_id":"mnecci","start":171,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15050829","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":258,"term_name":"disorder to order","start":171,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15050829","version":2,"reference_html":"Two homologous domains of similar structure but different stability in the yeast linker histone, Hho1p. <i> Ali T, Coles P, Stevens TJ, Stott K, Thomas JO. </i> J Mol Biol, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00423r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":258,"term_name":"nucleic acid binding","start":171,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"15050829","version":3,"reference_html":"Two homologous domains of similar structure but different stability in the yeast linker histone, Hho1p. <i> Ali T, Coles P, Stevens TJ, Stott K, Thomas JO. </i> J Mol Biol, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006204","region_id":"DP00423r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":258,"region_id":"DP00423r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Two homologous domains of similar structure but different stability in the yeast linker histone, Hho1p. <i> Ali T, Coles P, Stevens TJ, Stott K, Thomas JO. </i> J Mol Biol, 2004","term_id":"IDPO:0000002","curator_id":"mnecci","start":171,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15050829","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1YQA"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":258,"term_name":"disorder to order","start":171,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15050829","version":2,"reference_html":"Two homologous domains of similar structure but different stability in the yeast linker histone, Hho1p. <i> Ali T, Coles P, Stevens TJ, Stott K, Thomas JO. </i> J Mol Biol, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00423r005","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":258,"term_name":"nucleic acid binding","start":171,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"15050829","version":3,"reference_html":"Two homologous domains of similar structure but different stability in the yeast linker histone, Hho1p. <i> Ali T, Coles P, Stevens TJ, Stott K, Thomas JO. </i> J Mol Biol, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006165","region_id":"DP00423r006","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":252,"region_id":"DP00423r007","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The linker histone homolog Hho1p from Saccharomyces cerevisiae represents a winged helix-turn-helix fold as determined by NMR spectroscopy. <i> Ono K, Kusano O, Shimotakahara S, Shimizu M, Yamazaki T, Shindo H. </i> Nucleic Acids Res, 2003","term_id":"IDPO:0000002","curator_id":"mnecci","start":166,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"14654695","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":252,"term_name":"entropic chain","start":166,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"14654695","version":3,"reference_html":"The linker histone homolog Hho1p from Saccharomyces cerevisiae represents a winged helix-turn-helix fold as determined by NMR spectroscopy. <i> Ono K, Kusano O, Shimotakahara S, Shimizu M, Yamazaki T, Shindo H. </i> Nucleic Acids Res, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0006204","region_id":"DP00423r008","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":252,"term_name":"disorder to order","start":166,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"14654695","version":2,"reference_html":"The linker histone homolog Hho1p from Saccharomyces cerevisiae represents a winged helix-turn-helix fold as determined by NMR spectroscopy. <i> Ono K, Kusano O, Shimotakahara S, Shimizu M, Yamazaki T, Shindo H. </i> Nucleic Acids Res, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00423r009","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":252,"term_name":"nucleic acid binding","start":166,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"14654695","version":3,"reference_html":"The linker histone homolog Hho1p from Saccharomyces cerevisiae represents a winged helix-turn-helix fold as determined by NMR spectroscopy. <i> Ono K, Kusano O, Shimotakahara S, Shimizu M, Yamazaki T, Shindo H. </i> Nucleic Acids Res, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006204","region_id":"DP00423r010","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":258,"region_id":"DP00423r011","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p. <i> Sanderson A, Stott K, Stevens TJ, Thomas JO. </i> J Mol Biol, 2005","term_id":"IDPO:0000002","curator_id":"mnecci","start":171,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15878177","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":258,"term_name":"molecular adaptor activity","start":171,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"15878177","version":3,"reference_html":"Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p. <i> Sanderson A, Stott K, Stevens TJ, Thomas JO. </i> J Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP00423r012","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":258,"term_name":"disorder to order","start":171,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15878177","version":2,"reference_html":"Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p. <i> Sanderson A, Stott K, Stevens TJ, Thomas JO. </i> J Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00423r013","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":258,"term_name":"nucleic acid binding","start":171,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"15878177","version":3,"reference_html":"Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p. <i> Sanderson A, Stott K, Stevens TJ, Thomas JO. </i> J Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006165","region_id":"DP00423r014","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":258,"region_id":"DP00423r015","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p. <i> Sanderson A, Stott K, Stevens TJ, Thomas JO. </i> J Mol Biol, 2005","term_id":"IDPO:0000002","curator_id":"mnecci","start":171,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15878177","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":258,"term_name":"molecular adaptor activity","start":171,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"15878177","version":3,"reference_html":"Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p. <i> Sanderson A, Stott K, Stevens TJ, Thomas JO. </i> J Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006204","region_id":"DP00423r016","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":258,"term_name":"disorder to order","start":171,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15878177","version":2,"reference_html":"Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p. <i> Sanderson A, Stott K, Stevens TJ, Thomas JO. </i> J Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00423r017","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":258,"term_name":"nucleic acid binding","start":171,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"15878177","version":3,"reference_html":"Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p. <i> Sanderson A, Stott K, Stevens TJ, Thomas JO. </i> J Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006204","region_id":"DP00423r018","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P53551","date":"2016-09-06T16:08:30.000Z","acc":"P53551","name":"Histone H1","length":258,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000012BF45","genes":[{"name":{"value":"HHO1"},"orfNames":[{"value":"LPI17C"}],"olnNames":[{"value":"YPL127C"}]}],"alphafold_very_low_content":0.26744186046511625,"disorder_content":0.36046511627906974,"disprot_consensus":{"full":[{"start":166,"end":258,"type":"T"}],"Structural state":[{"start":166,"end":258,"type":"D"}],"Structural transition":[{"start":166,"end":258,"type":"T"}],"Molecular function":[{"start":166,"end":258,"type":"F"}],"Disorder function":[{"start":166,"end":252,"type":"F"}]}},{"acc":"P04325","sequence":"MAGRSGDSDEELLKAVRLIKFLYQSNPPPNPEGTRQARRNRRRRWRERQRQIHSISERILSTYLGRSAEPVPLQLPPLERLTLDCNEDCGTSGTQGVGSPQILVESPTILESGAKE","creator":"aschramm","dataset":["Viral proteins","RNA-binding proteins"],"date":"2016-09-07T20:03:18.000Z","disprot_id":"DP00424","features":{"pfam":[{"id":"PF00424","name":"REV protein (anti-repression trans-activator protein)","start":1,"end":91}]},"genes":[{"name":{"value":"rev","evidences":[{"source":{"id":"MF_04077","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04077","_id":"685af523b4ac24d5329d7d3a"},"code":"ECO:0000255","_id":"685af523b4ac24d5329d7d39"}],"_id":"685af523b4ac24d5329d7d3b"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d7d38"}],"length":116,"name":"Protein Rev","ncbi_taxon_id":11679,"organism":"Human immunodeficiency virus type 1 group M subtype B (isolate PCV12)","regions_counter":11,"released":"2016_10","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"UniParc":"UPI00001336EA","uniref100":"UniRef100_P04325","uniref50":"UniRef50_P69718","uniref90":"UniRef90_P69718","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":34,"end":50,"interaction_partner":[],"reference_html":"The arginine-rich RNA-binding motif of HIV-1 Rev is intrinsically disordered and folds upon RRE binding. <i> Casu F, Duggan BM, Hennig M. </i> Biophys J, 2013","reference_id":"23972852","region_id":"DP00424r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"CD spectra of the Rev ARM peptide in physiological buffer exhibited a minimum around 200 nm, typical of an unfolded state (Fig. 1 A).","_id":"685af523b4ac24d5329d7d17"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T09:59:49.568Z","_id":"685af523b4ac24d5329d7d18"},"version":3,"_id":"685af523b4ac24d5329d7d16","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":34,"end":50,"interaction_partner":[],"reference_html":"The arginine-rich RNA-binding motif of HIV-1 Rev is intrinsically disordered and folds upon RRE binding. <i> Casu F, Duggan BM, Hennig M. </i> Biophys J, 2013","reference_id":"23972852","region_id":"DP00424r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"To obtain residue-specific information regarding the Rev ARM peptide, we recorded 1HN,15N-HSQC spectra (Fig. 2). In aqueous solution, the peptide shows little dispersion of the resonances (Fig. 2 B), indicative of an unfolded peptide and in accordance with the CD data.","_id":"685af523b4ac24d5329d7d1a"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T10:00:02.404Z","_id":"685af523b4ac24d5329d7d1b"},"version":3,"_id":"685af523b4ac24d5329d7d19","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":34,"end":50,"interaction_partner":[],"reference_html":"The arginine-rich RNA-binding motif of HIV-1 Rev is intrinsically disordered and folds upon RRE binding. <i> Casu F, Duggan BM, Hennig M. </i> Biophys J, 2013","reference_id":"23972852","region_id":"DP00424r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Fig. 5 B shows that the [1HN],15N hetNOE values for Rev ARM in aqueous solution at pH 7.4 average 0.47 for residues T34–R50, consistent with a disordered peptide. In contrast, the hetNOEs of the Rev ARM peptide in complex with RRE StemIIB average 0.83 for residues T34–R50, and in 50% TFE average 0.77 for residues T34–R50. These higher hetNOE values indicate higher backbone rigidity and are typical of a well-ordered secondary structure.","_id":"685af523b4ac24d5329d7d1d"},{"type":"Curator statement","text":"RRE StemIIB it's the RNA binding Rev ARM.","_id":"685af523b4ac24d5329d7d1e"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T09:59:44.752Z","_id":"685af523b4ac24d5329d7d1f"},"version":1,"_id":"685af523b4ac24d5329d7d1c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":34,"end":50,"interaction_partner":[],"reference_html":"The arginine-rich RNA-binding motif of HIV-1 Rev is intrinsically disordered and folds upon RRE binding. <i> Casu F, Duggan BM, Hennig M. </i> Biophys J, 2013","reference_id":"23972852","region_id":"DP00424r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Fig. 5 B shows that the [1HN],15N hetNOE values for Rev ARM in aqueous solution at pH 7.4 average 0.47 for residues T34–R50, consistent with a disordered peptide. In contrast, the hetNOEs of the Rev ARM peptide in complex with RRE StemIIB average 0.83 for residues T34–R50, and in 50% TFE average 0.77 for residues T34–R50. These higher hetNOE values indicate higher backbone rigidity and are typical of a well-ordered secondary structure.","_id":"685af523b4ac24d5329d7d21"},{"type":"Curator statement","text":"RRE StemIIB it's the RNA binding Rev ARM.","_id":"685af523b4ac24d5329d7d22"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_go_domain":"F","term_id":"GO:0003723","term_is_binding":true,"term_is_obsolete":false,"term_name":"RNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T09:59:40.641Z","_id":"685af523b4ac24d5329d7d23"},"version":1,"_id":"685af523b4ac24d5329d7d20","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":34,"end":50,"interaction_partner":[],"reference_html":"A solution to limited genomic capacity: using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA. <i> Daugherty MD, D'Orso I, Frankel AD. </i> Mol Cell, 2008","reference_id":"18922466","region_id":"DP00424r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"We further characterized the differences in IA and IIB binding modes using amide proton chemical shifts from 15N HSQC NMR spectra to monitor changes in the peptide-RNA interfaces. There is little peak dispersion of peptide resonances in the absence of RNA (Figure 5C), indicative of a largely unstructured molecule.","_id":"685af523b4ac24d5329d7d25"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T09:59:52.778Z","_id":"685af523b4ac24d5329d7d26"},"version":1,"_id":"685af523b4ac24d5329d7d24","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":34,"end":50,"interaction_partner":[],"reference_html":"A solution to limited genomic capacity: using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA. <i> Daugherty MD, D'Orso I, Frankel AD. </i> Mol Cell, 2008","reference_id":"18922466","region_id":"DP00424r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"We further characterized the differences in IA and IIB binding modes using amide proton chemical shifts from 15N HSQC NMR spectra to monitor changes in the peptide-RNA interfaces. There is little peak dispersion of peptide resonances in the absence of RNA (Figure 5C), indicative of a largely unstructured molecule. However, we observe substantial amide peak dispersion in the presence of either IIB (red) or IA (blue) RNAs (Figure 5C), including the Hε protons of arginine side chains (Figure 5C inset). The overall upfield shifts observed in both 1H and 15N dimensions is consistent with stabilization of peptide α-helical structure upon binding (Wang and Jardetzky, 2002).","_id":"685af523b4ac24d5329d7d28"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T09:59:48.000Z","_id":"685af523b4ac24d5329d7d29"},"version":1,"_id":"685af523b4ac24d5329d7d27","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":34,"end":50,"interaction_partner":[],"reference_html":"A solution to limited genomic capacity: using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA. <i> Daugherty MD, D'Orso I, Frankel AD. </i> Mol Cell, 2008","reference_id":"18922466","region_id":"DP00424r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Given, the purine-rich internal loop of IA, we asked if this amino acid also is essential for IA binding. Interestingly, mutation of Asn40 had no effect on IA binding. Conversely, mutation of Arg41, which does not affect IIB binding (Tan et al., 1993), showed a reproducible 2-fold decrease in IA affinity (Figure 5A). R38A and R46A mutants showed similar 2-fold reductions in IA affinity but had no effect on IIB, while R43A, R44A, and W45A mutants bound IA like the wild type peptide. Helical wheel projections clearly show that different surfaces of the helix are used to recognize IIB and IA RNAs (Figure 5B).","_id":"685af523b4ac24d5329d7d2b"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_go_domain":"F","term_id":"GO:0003723","term_is_binding":true,"term_is_obsolete":false,"term_name":"RNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T09:59:46.038Z","_id":"685af523b4ac24d5329d7d2c"},"version":1,"_id":"685af523b4ac24d5329d7d2a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-08T15:28:32.727Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001807","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","ec_ontology":"ECO","start":35,"end":46,"interaction_partner":[{"db":"Rfam","id":"RF00036","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7d2f"}],"reference_html":"Interactions between HIV Rev and nuclear import and export factors: the Rev nuclear localisation signal mediates specific binding to human importin-beta. <i> Henderson BR, Percipalle P. </i> J Mol Biol, 1997","reference_id":"9405152","region_id":"DP00424r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As shown in a gel mobility shift assay (Figure 2), the addition of Rev normally leads to formation of multimeric complexes with 35S-labelled RRE.","_id":"685af523b4ac24d5329d7d2e"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_go_domain":"F","term_id":"GO:0003723","term_is_binding":true,"term_is_obsolete":false,"term_name":"RNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-08-10T13:31:33.385Z","_id":"685af523b4ac24d5329d7d30"},"version":2,"_id":"685af523b4ac24d5329d7d2d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007688","ec_name":"gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":35,"end":46,"interaction_partner":[],"reference_html":"Interactions between HIV Rev and nuclear import and export factors: the Rev nuclear localisation signal mediates specific binding to human importin-beta. <i> Henderson BR, Percipalle P. </i> J Mol Biol, 1997","reference_id":"9405152","region_id":"DP00424r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The experiment demonstrates the specificity of the Rev-importin-β interaction, as importin-β did not bind to the GST-Rev NLS mutant, or to GST protein. This was an unexpected finding, and identifies Rev as the first protein known to contain an NLS specific for the 97 kDa importin-β receptor, and not importin-α.","_id":"685af523b4ac24d5329d7d32"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T12:29:53.280Z","_id":"685af523b4ac24d5329d7d33"},"version":1,"_id":"685af523b4ac24d5329d7d31","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007106","ec_name":"green fluorescent protein fusion protein localization evidence used in manual assertion","ec_ontology":"ECO","start":35,"end":50,"interaction_partner":[],"reference_html":"Analysis of nuclear targeting activities of transport signals in the human immunodeficiency virus Rev protein. <i> Demart S, Ceccherini-Silberstein F, Schlicht S, Walcher S, Wolff H, Neumann M, Erfle V, Brack-Werner R. </i> Exp Cell Res, 2003","reference_id":"14644169","region_id":"DP00424r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Rev–GFP showed typical predominantly nuclear localization (>80% of fluorescence) (Fig. 2A). In contrast, RevM5–GFP fluorescence was apparent mainly in the cytoplasm, with less than 22% of total fluorescence in the nucleus (Fig. 2A).","_id":"685af523b4ac24d5329d7d35"},{"type":"Curator statement","text":"RevM5 has a mutation in this IDR.","_id":"685af523b4ac24d5329d7d36"}],"states_connection":[],"term_comment":"","term_def":"\"A process in which a protein is transported to, or maintained in, a location within the nucleoplasm.\" [GOC:mah, PMID:22918952]","term_go_domain":"P","term_id":"GO:1990173","term_is_binding":false,"term_is_obsolete":false,"term_name":"protein localization to nucleoplasm","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T12:30:14.058Z","_id":"685af523b4ac24d5329d7d37"},"version":1,"_id":"685af523b4ac24d5329d7d34","reference_source":"pmid"}],"__v":0,"disorder_content":0.14655172413793102,"disprot_consensus":{"full":[{"start":34,"end":50,"type":"T"}],"Structural state":[{"start":34,"end":50,"type":"D"}],"Structural transition":[{"start":34,"end":50,"type":"T"}],"Molecular function":[{"start":34,"end":50,"type":"F"}],"Biological process":[{"start":35,"end":50,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00456","name":"Transketolase, thiamine diphosphate binding domain","start":106,"end":296},{"id":"PF17831","name":"Pyruvate dehydrogenase E1 component middle domain","start":489,"end":700},{"id":"PF22613","name":"Transketolase-like TK C-terminal domain","start":713,"end":845},{"id":"PF28598","name":"Pyruvate dehydrogenase E1 component, N-terminal domain","start":10,"end":51}],"gene3D":[{"start":707,"end":887,"id":"3.40.50.920","name":"3.40.50.920"},{"start":472,"end":706,"id":"3.40.50.970","name":"3.40.50.970"},{"start":57,"end":471,"id":"3.40.50.970","name":"3.40.50.970"}]},"uniref50":"UniRef50_P0AFG9","sequence":"MSERFPNDVDPIETRDWLQAIESVIREEGVERAQYLIDQLLAEARKGGVNVAAGTGISNYINTIPVEEQPEYPGNLELERRIRSAIRWNAIMTVLRASKKDLELGGHMASFQSSATIYDVCFNHFFRARNEQDGGDLVYFQGHISPGVYARAFLEGRLTQEQLDNFRQEVHGNGLSSYPHPKLMPEFWQFPTVSMGLGPIGAIYQAKFLKYLEHRGLKDTSKQTVYAFLGDGEMDEPESKGAITIATREKLDNLVFVINCNLQRLDGPVTGNGKIINELEGIFEGAGWNVIKVMWGSRWDELLRKDTSGKLIQLMNETVDGDYQTFKSKDGAYVREHFFGKYPETAALVADWTDEQIWALNRGGHDPKKIYAAFKKAQETKGKATVILAHTIKGYGMGDAAEGKNIAHQVKKMNMDGVRHIRDRFNVPVSDADIEKLPYITFPEGSEEHTYLHAQRQKLHGYLPSRQPNFTEKLELPSLQDFGALLEEQSKEISTTIAFVRALNVMLKNKSIKDRLVPIIADEARTFGMEGLFRQIGIYSPNGQQYTPQDREQVAYYKEDEKGQILQEGINELGAGCSWLAAATSYSTNNLPMIPFYIYYSMFGFQRIGDLCWAAGDQQARGFLIGGTSGRTTLNGEGLQHEDGHSHIQSLTIPNCISYDPAYAYEVAVIMHDGLERMYGEKQENVYYYITTLNENYHMPAMPEGAEEGIRKGIYKLETIEGSKGKVQLLGSGSILRHVREAAEILAKDYGVGSDVYSVTSFTELARDGQDCERWNMLHPLETPRVPYIAQVMNDAPAVASTDYMKLFAEQVRTYVPADDYRVLGTDGFGRSDSRENLRHHFEVDASYVVVAALGELAKRGEIDKKVVADAIAKFNIDADKVNPRLA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0AFG9","disprot_id":"DP00427","ncbi_taxon_id":83333,"regions_counter":18,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":413,"region_id":"DP00427r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution. <i> Arjunan P, Nemeria N, Brunskill A, Chandrasekhar K, Sax M, Yan Y, Jordan F, Guest JR, Furey W. </i> Biochemistry, 2002","term_id":"IDPO:0000002","curator_id":"jpujols","start":401,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1L8A"}],"reference_id":"11955070","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":55,"region_id":"DP00427r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution. <i> Arjunan P, Nemeria N, Brunskill A, Chandrasekhar K, Sax M, Yan Y, Jordan F, Guest JR, Furey W. </i> Biochemistry, 2002","term_id":"IDPO:0000002","curator_id":"jpujols","start":1,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1L8A"}],"reference_id":"11955070","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":55,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution. <i> Arjunan P, Nemeria N, Brunskill A, Chandrasekhar K, Sax M, Yan Y, Jordan F, Guest JR, Furey W. </i> Biochemistry, 2002","term_id":"GO:0060090","curator_id":"jpujols","start":1,"term_ontology":"GO","curator_name":"Jordi Pujols Pujol","reference_id":"11955070","version":3,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00427r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":557,"region_id":"DP00427r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution. <i> Arjunan P, Nemeria N, Brunskill A, Chandrasekhar K, Sax M, Yan Y, Jordan F, Guest JR, Furey W. </i> Biochemistry, 2002","term_id":"IDPO:0000002","curator_id":"jpujols","start":541,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1L8A"}],"reference_id":"11955070","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":557,"region_id":"DP00427r005","released":"2022_03","ec_id":"ECO:0006220","reference_html":"A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component. <i> Kale S, Arjunan P, Furey W, Jordan F. </i> J Biol Chem, 2007","statement":[{"text":"Our crystallographic studies have shown that two active center loops (an inner loop formed by residues 401–413 and outer loop formed by residues 541–557) of the E1 component of the Escherichia coli pyruvate dehydrogenase complex become organized only on binding a substrate analog that is capable of forming a stable thiamin diphosphate-bound covalent intermediate.","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":541,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17635929","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2QTA"},{"db":"PDB","id":"2QTC"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":557,"term_name":"molecular function regulator","start":541,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"17635929","version":4,"reference_html":"A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component. <i> Kale S, Arjunan P, Furey W, Jordan F. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006220","region_id":"DP00427r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":557,"term_name":"disorder to order","start":541,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","statement":[{"text":"we have demonstrated that disorder to order transformation of active center dynamic loops (particularly the inner loop) modulates steps through LThDP formation. Ordering of loops also facilitates E1ec to E2ec active center communication reconfirming our previous hypothesis, presumably by acting as a recognition site for E2ec lipoyl domain, and acts as a regulatory switch for the next committed step in E1ec catalysis.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17635929","version":3,"reference_html":"A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component. <i> Kale S, Arjunan P, Furey W, Jordan F. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00427r007","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":413,"region_id":"DP00427r008","released":"2022_03","ec_id":"ECO:0006220","reference_html":"A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component. <i> Kale S, Arjunan P, Furey W, Jordan F. </i> J Biol Chem, 2007","statement":[{"text":"Our crystallographic studies have shown that two active center loops (an inner loop formed by residues 401–413 and outer loop formed by residues 541–557) of the E1 component of the Escherichia coli pyruvate dehydrogenase complex become organized only on binding a substrate analog that is capable of forming a stable thiamin diphosphate-bound covalent intermediate.","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":401,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17635929","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2QTA"},{"db":"PDB","id":"2QTC"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":413,"term_name":"molecular function regulator","start":401,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"17635929","version":4,"reference_html":"A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component. <i> Kale S, Arjunan P, Furey W, Jordan F. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006220","region_id":"DP00427r009","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":413,"term_name":"disorder to order","start":401,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","statement":[{"text":"we have demonstrated that disorder to order transformation of active center dynamic loops (particularly the inner loop) modulates steps through LThDP formation. Ordering of loops also facilitates E1ec to E2ec active center communication reconfirming our previous hypothesis, presumably by acting as a recognition site for E2ec lipoyl domain, and acts as a regulatory switch for the next committed step in E1ec catalysis.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17635929","version":3,"reference_html":"A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component. <i> Kale S, Arjunan P, Furey W, Jordan F. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00427r010","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":413,"term_name":"small molecule binding","start":401,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"17635929","version":4,"reference_html":"A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component. <i> Kale S, Arjunan P, Furey W, Jordan F. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0036094","ec_id":"ECO:0006220","region_id":"DP00427r011","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":413,"region_id":"DP00427r012","released":"2022_03","ec_id":"ECO:0006220","reference_html":"A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct. <i> Arjunan P, Sax M, Brunskill A, Chandrasekhar K, Nemeria N, Zhang S, Jordan F, Furey W. </i> J Biol Chem, 2006","term_id":"IDPO:0000002","curator_id":"jpujols","start":401,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2G25"},{"db":"PDB","id":"2G28"}],"reference_id":"16531404","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":413,"term_name":"molecular function regulator","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct. <i> Arjunan P, Sax M, Brunskill A, Chandrasekhar K, Nemeria N, Zhang S, Jordan F, Furey W. </i> J Biol Chem, 2006","term_id":"GO:0098772","curator_id":"jpujols","start":401,"term_ontology":"GO","curator_name":"Jordi Pujols Pujol","reference_id":"16531404","version":3,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00427r013","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":413,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct. <i> Arjunan P, Sax M, Brunskill A, Chandrasekhar K, Nemeria N, Zhang S, Jordan F, Furey W. </i> J Biol Chem, 2006","term_id":"IDPO:0000011","curator_id":"jpujols","start":401,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","reference_id":"16531404","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00427r014","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":413,"term_name":"small molecule binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct. <i> Arjunan P, Sax M, Brunskill A, Chandrasekhar K, Nemeria N, Zhang S, Jordan F, Furey W. </i> J Biol Chem, 2006","term_id":"GO:0036094","curator_id":"jpujols","start":401,"term_ontology":"GO","curator_name":"Jordi Pujols Pujol","reference_id":"16531404","version":3,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00427r015","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":557,"region_id":"DP00427r016","released":"2022_03","ec_id":"ECO:0006220","reference_html":"A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct. <i> Arjunan P, Sax M, Brunskill A, Chandrasekhar K, Nemeria N, Zhang S, Jordan F, Furey W. </i> J Biol Chem, 2006","term_id":"IDPO:0000002","curator_id":"jpujols","start":541,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2G25"},{"db":"PDB","id":"2G28"}],"reference_id":"16531404","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":557,"term_name":"molecular function regulator","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct. <i> Arjunan P, Sax M, Brunskill A, Chandrasekhar K, Nemeria N, Zhang S, Jordan F, Furey W. </i> J Biol Chem, 2006","term_id":"GO:0098772","curator_id":"jpujols","start":541,"term_ontology":"GO","curator_name":"Jordi Pujols Pujol","reference_id":"16531404","version":3,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00427r017","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":557,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct. <i> Arjunan P, Sax M, Brunskill A, Chandrasekhar K, Nemeria N, Zhang S, Jordan F, Furey W. </i> J Biol Chem, 2006","term_id":"IDPO:0000011","curator_id":"jpujols","start":541,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","reference_id":"16531404","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00427r018","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2016_10","uniref100":"UniRef100_P0AFG9","date":"2016-09-08T10:59:17.000Z","acc":"P0AFG8","name":"Pyruvate dehydrogenase E1 component","length":887,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI000011237F","genes":[{"name":{"value":"aceE"},"olnNames":[{"value":"b0114"},{"value":"JW0110"}]}],"alphafold_very_low_content":0.005636978579481398,"disorder_content":0.09582863585118377,"disprot_consensus":{"full":[{"start":1,"end":55,"type":"D"},{"start":401,"end":413,"type":"T"},{"start":541,"end":557,"type":"T"}],"Structural state":[{"start":1,"end":55,"type":"D"},{"start":401,"end":413,"type":"D"},{"start":541,"end":557,"type":"D"}],"Molecular function":[{"start":1,"end":55,"type":"F"},{"start":401,"end":413,"type":"F"},{"start":541,"end":557,"type":"F"}],"Structural transition":[{"start":401,"end":413,"type":"T"},{"start":541,"end":557,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":53,"end":305},{"id":"PF00659","name":"POLO box duplicated region","start":419,"end":476},{"id":"PF00659","name":"POLO box duplicated region","start":517,"end":580}],"gene3D":[{"start":378,"end":587,"id":"3.30.1120.30","name":"POLO box domain"},{"start":412,"end":508,"id":"3.30.1120.30","name":"POLO box domain"},{"start":139,"end":310,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"},{"start":48,"end":136,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"}]},"uniref50":"UniRef50_P53350","sequence":"MSAAVTAGKLARAPADPGKAGVPGVAAPGAPAAAPPAKEIPEVLVDPRSRRRYVRGRFLGKGGFAKCFEISDADTKEVFAGKIVPKSLLLKPHQREKMSMEISIHRSLAHQHVVGFHGFFEDNDFVFVVLELCRRRSLLELHKRRKALTEPEARYYLRQIVLGCQYLHRNRVIHRDLKLGNLFLNEDLEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFEVDVWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTINELLNDEFFTSGYIPARLPITCLTIPPRFSIAPSSLDPSNRKPLTVLNKGLENPLPERPREKEEPVVRETGEVVDCHLSDMLQQLHSVNASKPSERGLVRQEEAEDPACIPIFWVSKWVDYSDKYGLGYQLCDNSVGVLFNDSTRLILYNDGDSLQYIERDGTESYLTVSSHPNSLMKKITLLKYFRNYMSEHLLKAGANITPREGDELARLPYLRTWFRTRSAIILHLSNGSVQINFFQDHTKLILCPLMAAVTYIDEKRDFRTYRLSLLEEYGCCKELASRLRYARTMVDKLLSSRSASNRLKAS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P53350","disprot_id":"DP00428","ncbi_taxon_id":9606,"regions_counter":11,"creator":"tszani","regions":[{"start":495,"end":506,"reference_id":"17307877","reference_source":"pmid","reference_html":"Molecular and structural basis of polo-like kinase 1 substrate recognition: Implications in centrosomal localization. <i> García-Alvarez B, de Cárcer G, Ibañez S, Bragado-Nilsson E, Montoya G. </i> Proc Natl Acad Sci U S A, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2OGQ"}],"region_id":"DP00428r007","statement":[{"text":"Only spanning residues 495-506 are missing from crystal structure 2OGQ, the residues 493, 494 and 507, indicated as boundaries of the disordered loop by the authors are ordered in the structure","type":"Curator statement"},{"text":"After careful comparison of the three models, the main difference arises from the 20-residue loop, which is disordered in the apo and PBD-Cdc25C structures (residues Ala-493–Arg-507 for apo and Glu-488–Arg-507 for the PBD-Cdc25C complex).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":489,"end":506,"reference_id":"17307877","reference_source":"pmid","reference_html":"Molecular and structural basis of polo-like kinase 1 substrate recognition: Implications in centrosomal localization. <i> García-Alvarez B, de Cárcer G, Ibañez S, Bragado-Nilsson E, Montoya G. </i> Proc Natl Acad Sci U S A, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2OJX"}],"region_id":"DP00428r008","statement":[{"text":"Only spanning residues 489-506 are missing from crystal structure 2OJX, the residues 488 and 507, indicated as boundaries of the disordered loop by the authors are ordered in the structure","type":"Curator statement"},{"text":"After careful comparison of the three models, the main difference arises from the 20-residue loop, which is disordered in the apo and PBD-Cdc25C structures (residues Ala-493–Arg-507 for apo and Glu-488–Arg-507 for the PBD-Cdc25C complex).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":489,"end":506,"reference_id":"17307877","reference_source":"pmid","reference_html":"Molecular and structural basis of polo-like kinase 1 substrate recognition: Implications in centrosomal localization. <i> García-Alvarez B, de Cárcer G, Ibañez S, Bragado-Nilsson E, Montoya G. </i> Proc Natl Acad Sci U S A, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3BZI"}],"region_id":"DP00428r009","statement":[{"text":"Although the structure of the PBD among the three different crystals is well conserved (SI Fig. 10a), the loop that connects PBI and PBII is ordered only in the case of the PBD-Cdc25C-P complex","type":"Discussion"}],"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":495,"end":506,"reference_id":"17307877","reference_source":"pmid","reference_html":"Molecular and structural basis of polo-like kinase 1 substrate recognition: Implications in centrosomal localization. <i> García-Alvarez B, de Cárcer G, Ibañez S, Bragado-Nilsson E, Montoya G. </i> Proc Natl Acad Sci U S A, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"2OGQ"}],"region_id":"DP00428r010","statement":[{"text":"Although the structure of the PBD among the three different crystals is well conserved (SI Fig. 10a), the loop that connects PBI and PBII is ordered only in the case of the PBD-Cdc25C-P complex","type":"Discussion"},{"text":"After careful comparison of the three models, the main difference arises from the 20-residue loop, which is disordered in the apo and PBD-Cdc25C structures (residues Ala-493–Arg-507 for apo and Glu-488–Arg-507 for the PBD-Cdc25C complex). This loop [connecting loop (CL)] joins both PB and flanks the binding site of the target peptide (SI Figs. 8 and 10a).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-02-17T17:03:11.698Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":489,"end":506,"reference_id":"17307877","reference_source":"pmid","reference_html":"Molecular and structural basis of polo-like kinase 1 substrate recognition: Implications in centrosomal localization. <i> García-Alvarez B, de Cárcer G, Ibañez S, Bragado-Nilsson E, Montoya G. </i> Proc Natl Acad Sci U S A, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"2OJX"}],"region_id":"DP00428r011","statement":[{"text":"Although the structure of the PBD among the three different crystals is well conserved (SI Fig. 10a), the loop that connects PBI and PBII is ordered only in the case of the PBD-Cdc25C-P complex","type":"Discussion"},{"text":"After careful comparison of the three models, the main difference arises from the 20-residue loop, which is disordered in the apo and PBD-Cdc25C structures (residues Ala-493–Arg-507 for apo and Glu-488–Arg-507 for the PBD-Cdc25C complex). This loop [connecting loop (CL)] joins both PB and flanks the binding site of the target peptide (SI Figs. 8 and 10a).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-02-17T17:03:12.888Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_P53350","date":"2016-09-18T21:46:34.000Z","acc":"P53350","name":"Serine/threonine-protein kinase PLK1","length":603,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000131BF9","genes":[{"name":{"value":"PLK1"},"synonyms":[{"value":"PLK"}]}],"alphafold_very_low_content":0.14593698175787728,"disorder_content":0.029850746268656716,"disprot_consensus":{"full":[{"start":489,"end":506,"type":"T"}],"Structural state":[{"start":489,"end":506,"type":"D"}],"Structural transition":[{"start":489,"end":506,"type":"T"}],"Disorder function":[{"start":489,"end":506,"type":"F"}]}},{"features":{"pfam":[{"id":"PF06134","name":"L-rhamnose isomerase (RhaA)","start":3,"end":418}],"gene3D":[{"start":1,"end":419,"id":"3.20.20.150","name":"Divalent-metal-dependent TIM barrel enzymes"}]},"uniref50":"UniRef50_Q8FBE0","sequence":"MTTQLEQAWELAKQRFAAVGIDVEEALRQLDRLPVSMHCWQGDDVSGFENPEGSLTGGIQATGNYPGKARNASELRADLEQAMRLIPGPKRLNLHAIYLESDTPVSRDQIKPEHFKNWVEWAKANQLGLDFNPSCFSHPLSADGFTLSHADDSIRQFWIDHCKASRRVSAYFGEQLGTPSVMNIWIPDGMKDITVDRLAPRQRLLAALDEVISEKLNPAHHIDAVESKLFGIGAESYTVGSNEFYMGYATSRQTALCLDAGHFHPTEVISDKISAAMLYVPQLLLHVSRPVRWDSDHVVLLDDETQAIASEIVRHDLFDRVHIGLDFFDASINRIAAWVIGTRNMKKALLRALLEPTAELRKLEAAGDYTARLALLEEQKSLPWQAVWEMYCQRHDTPAGSEWLESVRAYEKEILSRRG","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_Q8FBE0","disprot_id":"DP00429","ncbi_taxon_id":83333,"regions_counter":4,"creator":"agasparini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":64,"region_id":"DP00429r001","released":"2022_12","ec_id":"ECO:0005670","reference_html":"The structure of rhamnose isomerase from Escherichia coli and its relation with xylose isomerase illustrates a change between inter and intra-subunit complementation during evolution. <i> Korndörfer IP, Fessner WD, Matthews BW. </i> J Mol Biol, 2000","term_id":"IDPO:0000002","curator_id":"vnugnes","start":50,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10891278","version":3,"ec_name":"x-ray crystallography evidence used in manual assertion","date":"2022-08-18T20:03:28.090Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":37,"end":37,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":83,"end":83,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":182,"end":182,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":190,"end":190,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":246,"end":246,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":277,"end":277,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":345,"end":345,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":390,"end":390,"position":"Specific residue"}],"curator_orcid":"0000-0001-8399-7907","statement":[{"text":"In the refined ``native'' structure (i.e. the SeMet variant), the loop comprising residues 58 through 72 (b1-a1-loop) is completely disordered.","type":"Results"},{"text":"The region the authors are reffering to corresponds to the 50-64 residues of the Uniprot.","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"1D8W"}]},{"start":50,"end":64,"reference_id":"10891278","reference_source":"pmid","reference_html":"The structure of rhamnose isomerase from Escherichia coli and its relation with xylose isomerase illustrates a change between inter and intra-subunit complementation during evolution. <i> Korndörfer IP, Fessner WD, Matthews BW. </i> J Mol Biol, 2000","date":"2022-08-18T20:03:38.495Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":37,"end":37,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":83,"end":83,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":182,"end":182,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":190,"end":190,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":246,"end":246,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":277,"end":277,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":345,"end":345,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":390,"end":390,"position":"Specific residue"}],"region_id":"DP00429r003","statement":[{"text":"In the refined ``native'' structure (i.e. the SeMet variant), the loop comprising residues 58 through 72 (b1-a1-loop) is completely disordered.\" Curator statement \"The region the authors are reffering to corresponds to the 50-64 residues of the Uniprot.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"cross_refs":[{"db":"PDB","id":"1D8W"}]},{"start":50,"end":64,"reference_id":"10891278","reference_source":"pmid","reference_html":"The structure of rhamnose isomerase from Escherichia coli and its relation with xylose isomerase illustrates a change between inter and intra-subunit complementation during evolution. <i> Korndörfer IP, Fessner WD, Matthews BW. </i> J Mol Biol, 2000","date":"2023-11-24T10:47:26.986Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":37,"end":37,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":83,"end":83,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":182,"end":182,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":190,"end":190,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":246,"end":246,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":277,"end":277,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":345,"end":345,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":390,"end":390,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"1DE5"},{"db":"PDB","id":"1DE6"}],"region_id":"DP00429r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"45530","entry_name":"L-rhamnitol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"62345","entry_name":"L-rhamnose"}],"statement":[{"text":"Upon binding of L-rhamnitol, however, this segment, which will be named the b1-a1-loop, closes the top of the (b/a)8-barrel, covers the active site and excludes the bound inhibitor from contact with bulk solvent (Figure 8). The electron density maps and re®nement suggest that the b1-a1-loop becomes essentially as well ordered as neighboring parts of the protein.","type":"Results"},{"text":"It was noted above that the binding of the inhibitor L-rhamnitol, and to a lesser degree the binding of the substrate, L-rhamnose, causes the b1-a1-loop to cover the active site like a lid (Figure 8). ","type":"Results"},{"text":"The structures of complexes of rhamnose isomerase with the inhibitor L-rhamnitol and the natural substrate L-rhamnose were determined and suggest that an extended loop, which is disordered in the native enzyme, becomes ordered on substrate binding, and may exclude bulk solvent during catalysis.","type":"Abstract"}]}],"released":"2016_10","uniref100":"UniRef100_C5A071","date":"2016-08-22T10:52:47.000Z","acc":"P32170","name":"L-rhamnose isomerase","length":419,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI0000133849","genes":[{"name":{"value":"rhaA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00541","url":"https://hamap.expasy.org/unirule/MF_00541"}}]},"olnNames":[{"value":"b3903"},{"value":"JW5561"}]}],"alphafold_very_low_content":0.002386634844868735,"disorder_content":0.03579952267303103,"disprot_consensus":{"full":[{"start":50,"end":64,"type":"T"}],"Structural state":[{"start":50,"end":64,"type":"D"}],"Disorder function":[{"start":50,"end":64,"type":"F"}],"Structural transition":[{"start":50,"end":64,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00505","name":"HMG (high mobility group) box","start":21,"end":89}],"gene3D":[{"start":1,"end":93,"id":"1.10.30.10","name":"High mobility group box domain"}]},"uniref50":"UniRef50_P11632","sequence":"MVTPREPKKRTTRKKKDPNAPKRALSAYMFFANENRDIVRSENPDITFGQVGKKLGEKWKALTPEEKQPYEAKAQADKKRYESEKELYNATLA","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P11632","disprot_id":"DP00432","ncbi_taxon_id":559292,"regions_counter":5,"creator":"zdosztanyi","regions":[{"term_namespace":"Molecular function","ec_ontology":"ECO","end":25,"term_name":"nucleic acid binding","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The S. cerevisiae architectural HMGB protein NHP6A complexed with DNA: DNA and protein conformational changes upon binding. <i> Masse JE, Wong B, Yen YM, Allain FH, Johnson RC, Feigon J. </i> J Mol Biol, 2002","term_id":"GO:0003676","curator_id":"vnugnes","start":1,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"12381320","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-22T16:42:04.629Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00432r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"1J5N"}],"statement":[{"text":"Further electrostatic contacts are made by the side-chains of the extended strand and charged region of the amino-terminal tail located in the major groove. In the extended strand region, Lys22 contacts the phosphate of nucleotide T9.","type":"Results"},{"text":"The N-terminal tail residues Arg10, Arg13, Lys14, and Lys16 all make contact with the DNA backbone in most members of the structure ensemble, consistent with their importance in protein–DNA affinity as shown in previous point mutation and deletion studies.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":25,"region_id":"DP00432r005","released":"2023_12","ec_id":"ECO:0006165","reference_html":"The S. cerevisiae architectural HMGB protein NHP6A complexed with DNA: DNA and protein conformational changes upon binding. <i> Masse JE, Wong B, Yen YM, Allain FH, Johnson RC, Feigon J. </i> J Mol Biol, 2002","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-22T16:39:37.954Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1LWM"}],"reference_id":"12381320","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Helices 1 (residues 27–43) and 2 (residues 47–61) are wrapped around each other to form the short arm of the L. The long arm of the L is formed by helix 3 (residues 64–93) and the extended strand (residues 18–25), which interact extensively via hydrophobic contacts between residues in the extended strand and helix 3, as well as a hydrogen bond between the side-chain carboxyl of Asp77 and the amide proton of Leu25.","type":"Results"},{"text":"This rearrangement of helix 3 probably has only a small energetic cost, as the helix3/extended strand region appears to be inherently flexible for NHP6A as well as other HMGB proteins.","type":"Results"},{"text":"The first nine residues of the N-terminal tail are undefined by the NMR data, and the few assigned resonances have chemical shifts consistent with a random coil.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P11632","date":"2016-09-09T13:42:01.000Z","acc":"P11632","name":"Non-histone chromosomal protein 6A","length":93,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000110C5D","genes":[{"name":{"value":"NHP6A"},"synonyms":[{"value":"NHPA"}],"orfNames":[{"value":"YP9499.09C"}],"olnNames":[{"value":"YPR052C"}]}],"alphafold_very_low_content":0.07526881720430108,"disorder_content":0.26881720430107525,"disprot_consensus":{"full":[{"start":1,"end":25,"type":"D"}],"Structural state":[{"start":1,"end":25,"type":"D"}],"Molecular function":[{"start":1,"end":25,"type":"F"}]}},{"features":{"pfam":[{"id":"PF06201","name":"PITH domain","start":8,"end":173}],"gene3D":[{"start":1,"end":161,"id":"2.60.120.470","name":"PITH domain"}]},"uniref50":"UniRef50_Q9SQZ9","sequence":"MSAESASQIPKGQVDLLDFIDWSGVECLNQSSSHSLPNALKQGYREDEGLNLESDADEQLLIYIPFNQVIKLHSFAIKGPEEEGPKTVKFFSNKEHMCFSNVNDFPPSDTAELTEENLKGKPVVLKYVKFQNVRSLTIFIEANQSGSEVTKVQKIALYGSTVETTDMKGLKKIEDH","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q9SQZ9","disprot_id":"DP00434","ncbi_taxon_id":3702,"regions_counter":6,"creator":"droche","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":12,"region_id":"DP00434r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of At3g04780.1-des15, an Arabidopsis thaliana ortholog of the C-terminal domain of human thioredoxin-like protein. <i> Song J, Tyler RC, Wrobel RL, Frederick RO, Vojtek FC, Jeon WB, Lee MS, Markley JL. </i> Protein Sci, 2005","term_id":"IDPO:0000002","curator_id":"droche","start":2,"term_ontology":"IDPO","curator_name":"Daniel Roche","reference_id":"15741346","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1XOY"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":104,"region_id":"DP00434r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of At3g04780.1-des15, an Arabidopsis thaliana ortholog of the C-terminal domain of human thioredoxin-like protein. <i> Song J, Tyler RC, Wrobel RL, Frederick RO, Vojtek FC, Jeon WB, Lee MS, Markley JL. </i> Protein Sci, 2005","term_id":"IDPO:0000002","curator_id":"droche","start":95,"term_ontology":"IDPO","curator_name":"Daniel Roche","reference_id":"15741346","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1XOY"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q9SQZ9","date":"2016-09-06T15:06:44.000Z","acc":"Q9SQZ9","name":"PITH domain-containing protein At3g04780","length":176,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI00000A997A","genes":[{"orfNames":[{"value":"F7O18.27"},{"value":"T9J14.27"}],"olnNames":[{"value":"At3g04780"}]}],"alphafold_very_low_content":0.09090909090909091,"disorder_content":0.11931818181818182,"disprot_consensus":{"full":[{"start":2,"end":12,"type":"D"},{"start":95,"end":104,"type":"D"}],"Structural state":[{"start":2,"end":12,"type":"D"},{"start":95,"end":104,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00004","name":"ATPase family associated with various cellular activities (AAA)","start":241,"end":370},{"id":"PF00004","name":"ATPase family associated with various cellular activities (AAA)","start":514,"end":647},{"id":"PF02359","name":"Cell division protein 48 (CDC48), N-terminal domain","start":25,"end":106},{"id":"PF02933","name":"Cell division protein 48 (CDC48), domain 2","start":126,"end":190},{"id":"PF17862","name":"AAA+ lid domain","start":393,"end":434},{"id":"PF17862","name":"AAA+ lid domain","start":669,"end":708}],"gene3D":[{"start":205,"end":370,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":2,"end":107,"id":"2.40.40.20","name":"2.40.40.20"},{"start":649,"end":763,"id":"1.10.8.60","name":"1.10.8.60"},{"start":372,"end":467,"id":"1.10.8.60","name":"1.10.8.60"},{"start":108,"end":204,"id":"3.10.330.10","name":"3.10.330.10"},{"start":468,"end":648,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_P55072","sequence":"MASGADSKGDDLSTAILKQKNRPNRLIVDEAINEDNSVVSLSQPKMDELQLFRGDTVLLKGKKRREAVCIVLSDDTCSDEKIRMNRVVRNNLRVRLGDVISIQPCPDVKYGKRIHVLPIDDTVEGITGNLFEVYLKPYFLEAYRPIRKGDIFLVRGGMRAVEFKVVETDPSPYCIVAPDTVIHCEGEPIKREDEEESLNEVGYDDIGGCRKQLAQIKEMVELPLRHPALFKAIGVKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAIIFIDELDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFDREVDIGIPDATGRLEILQIHTKNMKLADDVDLEQVANETHGHVGADLAALCSEAALQAIRKKMDLIDLEDETIDAEVMNSLAVTMDDFRWALSQSNPSALRETVVEVPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLAIRESIESEIRRERERQTNPSAMEVEEDDPVPEIRRDHFEEAMRFARRSVSDNDIRKYEMFAQTLQQSRGFGSFRFPSGNQGGAGPSQGSGGGTGGSVYTEDNDDDLYG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P55072","disprot_id":"DP00435","ncbi_taxon_id":10090,"regions_counter":20,"creator":"agasparini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":16,"region_id":"DP00435r001","released":"2022_12","ec_id":"ECO:0006220","reference_html":"The crystal structure of murine p97/VCP at 3.6A. <i> Huyton T, Pye VE, Briggs LC, Flynn TC, Beuron F, Kondo H, Ma J, Zhang X, Freemont PS. </i> J Struct Biol, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14643202","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-08-22T13:41:43.917Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1R7R"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Our crystal structure of murine p97 comprises residues 17–700 and consists of: complete models for the N terminal substrate binding domain and the D1 AAA domain, and a poly-alanine partial model for the D2 AAA domain, in which the α-helical and C-terminal regions are highly disordered (see representative densities in Fig. 1).","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"}]},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":16,"term_name":"flexible N-terminal tail","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"vnugnes","released":"2022_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14643202","version":4,"reference_html":"The crystal structure of murine p97/VCP at 3.6A. <i> Huyton T, Pye VE, Briggs LC, Flynn TC, Beuron F, Kondo H, Ma J, Zhang X, Freemont PS. </i> J Struct Biol, 2003","date":"2022-08-22T13:42:54.417Z","term_id":"IDPO:0000032","ec_id":"ECO:0006220","region_id":"DP00435r002","ec_go":"EXP","disprot_namespace":"Disorder function","curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"}],"statement":[{"text":"Our crystal structure of murine p97 comprises residues 17–700 and consists of: complete models for the N terminal substrate binding domain and the D1 AAA domain, and a poly-alanine partial model for the D2 AAA domain, in which the α-helical and C-terminal regions are highly disordered (see representative densities in Fig. 1).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":806,"region_id":"DP00435r003","released":"2022_12","ec_id":"ECO:0006220","reference_html":"The crystal structure of murine p97/VCP at 3.6A. <i> Huyton T, Pye VE, Briggs LC, Flynn TC, Beuron F, Kondo H, Ma J, Zhang X, Freemont PS. </i> J Struct Biol, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":736,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14643202","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-08-22T13:45:05.105Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1R7R"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"}],"statement":[{"text":"Our crystal structure of murine p97 comprises residues 17–700 and consists of: complete models for the N terminal substrate binding domain and the D1 AAA domain, and a poly-alanine partial model for the D2 AAA domain, in which the α-helical and C-terminal regions are highly disordered (see representative densities in Fig. 1).","type":"Results"},{"text":"The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":726,"region_id":"DP00435r009","released":"2022_12","ec_id":"ECO:0006220","reference_html":"The crystal structure of murine p97/VCP at 3.6A. <i> Huyton T, Pye VE, Briggs LC, Flynn TC, Beuron F, Kondo H, Ma J, Zhang X, Freemont PS. </i> J Struct Biol, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":703,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14643202","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-08-22T13:41:27.158Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1R7R"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"}],"statement":[{"text":"Our crystal structure of murine p97 comprises residues 17–700 and consists of: complete models for the N terminal substrate binding domain and the D1 AAA domain, and a poly-alanine partial model for the D2 AAA domain, in which the α-helical and C-terminal regions are highly disordered (see representative densities in Fig. 1).","type":"Results"},{"text":"The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]},{"start":708,"end":727,"reference_id":"18462676","reference_source":"pmid","reference_html":"Improved structures of full-length p97, an AAA ATPase: implications for mechanisms of nucleotide-dependent conformational change. <i> Davies JM, Brunger AT, Weis WI. </i> Structure, 2008","date":"2022-08-22T14:16:24.885Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"3CF0"}],"region_id":"DP00435r013","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"}],"statement":[{"text":"The refined model consists of residues 463–707 and 728–763. Electron density was not well defined for the first two and last 42 residues, as well as the loop from 708 to 727.","type":"Results"}]},{"start":708,"end":727,"reference_id":"18462676","reference_source":"pmid","reference_html":"Improved structures of full-length p97, an AAA ATPase: implications for mechanisms of nucleotide-dependent conformational change. <i> Davies JM, Brunger AT, Weis WI. </i> Structure, 2008","date":"2022-08-22T14:19:59.608Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"3CF0"}],"region_id":"DP00435r014","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"}],"statement":[{"text":"The refined model consists of residues 463–707 and 728–763. Electron density was not well defined for the first two and last 42 residues, as well as the loop from 708 to 727.","type":"Results"}]},{"start":1,"end":20,"reference_id":"18462676","reference_source":"pmid","reference_html":"Improved structures of full-length p97, an AAA ATPase: implications for mechanisms of nucleotide-dependent conformational change. <i> Davies JM, Brunger AT, Weis WI. </i> Structure, 2008","date":"2022-08-22T14:31:13.427Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"3CF2"}],"region_id":"DP00435r015","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"47785","entry_name":"AMP-PNP"}],"statement":[{"text":"The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]},{"start":1,"end":20,"reference_id":"18462676","reference_source":"pmid","reference_html":"Improved structures of full-length p97, an AAA ATPase: implications for mechanisms of nucleotide-dependent conformational change. <i> Davies JM, Brunger AT, Weis WI. </i> Structure, 2008","date":"2022-08-22T14:30:03.324Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"3CF2"}],"region_id":"DP00435r016","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"47785","entry_name":"AMP-PNP"}],"statement":[{"text":"The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]},{"start":583,"end":596,"reference_id":"18462676","reference_source":"pmid","reference_html":"Improved structures of full-length p97, an AAA ATPase: implications for mechanisms of nucleotide-dependent conformational change. <i> Davies JM, Brunger AT, Weis WI. </i> Structure, 2008","date":"2022-08-22T14:29:23.954Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"3CF2"}],"region_id":"DP00435r017","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"47785","entry_name":"AMP-PNP"}],"statement":[{"text":"The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]},{"start":583,"end":596,"reference_id":"18462676","reference_source":"pmid","reference_html":"Improved structures of full-length p97, an AAA ATPase: implications for mechanisms of nucleotide-dependent conformational change. <i> Davies JM, Brunger AT, Weis WI. </i> Structure, 2008","date":"2022-08-22T14:29:12.184Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"3CF2"}],"region_id":"DP00435r018","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"47785","entry_name":"AMP-PNP"}],"statement":[{"text":"The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"},{"text":"Resides R586 and R599 are located on a loop at the entrance to the D2 pore, and have been proposed to participate in the denaturing of substrate proteins.","type":"Results"}]},{"start":665,"end":685,"reference_id":"18462676","reference_source":"pmid","reference_html":"Improved structures of full-length p97, an AAA ATPase: implications for mechanisms of nucleotide-dependent conformational change. <i> Davies JM, Brunger AT, Weis WI. </i> Structure, 2008","date":"2022-08-22T14:33:09.922Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"3CF2"}],"region_id":"DP00435r019","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"47785","entry_name":"AMP-PNP"}],"statement":[{"text":"The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]},{"start":705,"end":806,"reference_id":"18462676","reference_source":"pmid","reference_html":"Improved structures of full-length p97, an AAA ATPase: implications for mechanisms of nucleotide-dependent conformational change. <i> Davies JM, Brunger AT, Weis WI. </i> Structure, 2008","date":"2022-08-22T14:33:40.355Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"3CF2"}],"region_id":"DP00435r020","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"47785","entry_name":"AMP-PNP"}],"statement":[{"text":"The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]}],"released":"2016_10","uniref100":"UniRef100_P55072","date":"2016-08-22T13:10:14.000Z","acc":"Q01853","name":"Transitional endoplasmic reticulum ATPase","length":806,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000029436","genes":[{"name":{"value":"Vcp"}}],"alphafold_very_low_content":0.06699751861042183,"disorder_content":0.19727047146401985,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"D"},{"start":583,"end":596,"type":"D"},{"start":665,"end":685,"type":"D"},{"start":703,"end":806,"type":"D"}],"Structural state":[{"start":1,"end":20,"type":"D"},{"start":583,"end":596,"type":"D"},{"start":665,"end":685,"type":"D"},{"start":703,"end":806,"type":"D"}],"Disorder function":[{"start":1,"end":20,"type":"F"},{"start":583,"end":596,"type":"F"},{"start":708,"end":727,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00190","name":"Cupin","start":74,"end":164},{"id":"PF00190","name":"Cupin","start":249,"end":406}],"gene3D":[{"start":41,"end":237,"id":"2.60.120.10","name":"Jelly Rolls"},{"start":246,"end":422,"id":"2.60.120.10","name":"Jelly Rolls"}]},"uniref50":"UniRef50_P07219","sequence":"MAFSARFPLWLLLGVVLLASVSASFAHSGHSGGEAEDESEESRAQNNPYLFRSNKFLTLFKNQHGSLRLLQRFNEDTEKLENLRDYRVLEYCSKPNTLLLPHHSDSDLLVLVLEGQAILVLVNPDGRDTYKLDQGDAIKIQAGTPFYLINPDNNQNLRILKFAITFRRPGTVEDFFLSSTKRLPSYLSAFSKNFLEASYDSPYDEIEQTLLQEEQEGVIVKMPKDQIQEISKHAQSSSRKTLSSQDKPFNLRSRDPIYSNNYGKLYEITPEKNSQLRDLDILLNCLQMNEGALFVPHYNSRATVILVANEGRAEVELVGLEQQQQQGLESMQLRRYAATLSEGDIIVIPSSFPVALKAASDLNMVGIGVNAENNERNFLAGHKENVIRQIPRQVSDLTFPGSGEEVEELLENQKESYFVDGQPRHIDAGGKARRAHLPNLFRTFY","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","fabids","Fabales","Fabaceae","Papilionoideae","50 kb inversion clade","NPAAA clade","indigoferoid/millettioid clade","Phaseoleae","Canavalia"],"uniref90":"UniRef90_P50477","disprot_id":"DP00436","ncbi_taxon_id":3823,"regions_counter":4,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":45,"region_id":"DP00436r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The three-dimensional structure of canavalin from jack bean (Canavalia ensiformis). <i> Ko TP, Ng JD, McPherson A. </i> Plant Physiol, 1993","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"8310056","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2CAU"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":244,"region_id":"DP00436r002","released":"2022_03","ec_id":"ECO:0007691","reference_html":"The three-dimensional structure of canavalin from jack bean (Canavalia ensiformis). <i> Ko TP, Ng JD, McPherson A. </i> Plant Physiol, 1993","term_id":"IDPO:0000002","curator_id":"mnecci","start":228,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"8310056","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":244,"region_id":"DP00436r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The three-dimensional structure of canavalin from jack bean (Canavalia ensiformis). <i> Ko TP, Ng JD, McPherson A. </i> Plant Physiol, 1993","term_id":"IDPO:0000002","curator_id":"mnecci","start":228,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"8310056","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":445,"region_id":"DP00436r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The three-dimensional structure of canavalin from jack bean (Canavalia ensiformis). <i> Ko TP, Ng JD, McPherson A. </i> Plant Physiol, 1993","term_id":"IDPO:0000002","curator_id":"mnecci","start":427,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"8310056","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P50477","date":"2016-09-06T16:25:05.000Z","acc":"P50477","name":"Canavalin","length":445,"organism":"Canavalia ensiformis","dataset":[],"UniParc":"UPI0000110BB4","genes":[],"alphafold_very_low_content":0.14606741573033707,"disorder_content":0.18202247191011237,"disprot_consensus":{"full":[{"start":1,"end":45,"type":"D"},{"start":228,"end":244,"type":"D"},{"start":427,"end":445,"type":"D"}],"Structural state":[{"start":1,"end":45,"type":"D"},{"start":228,"end":244,"type":"D"},{"start":427,"end":445,"type":"D"}]}},{"features":{"pfam":[{"id":"PF04098","name":"Rad52/22 family double-strand break repair protein","start":36,"end":178}],"gene3D":[{"start":32,"end":179,"id":"3.30.390.80","name":"DNA repair protein Rad52/59/22"}]},"uniref50":"UniRef50_P43351","sequence":"MSGTEEAILGGRDSHPAAGGGSVLCFGQCQYTAEEYQAIQKALRQRLGPEYISSRMAGGGQKVCYIEGHRVINLANEMFGYNGWAHSITQQNVDFVDLNNGKFYVGVCAFVRVQLKDGSYHEDVGYGVSEGLKSKALSLEKARKEAVTDGLKRALRSFGNALGNCILDKDYLRSLNKLPRQLPLEVDLTKAKRQDLEPSVEEARYNSCRPNMALGHPQLQQVTSPSRPSHAVIPADQDCSSRSLSSSAVESEATHQRKLRQKQLQQQFRERMEKQQVRVSTPSAEKSEAAPPAPPVTHSTPVTVSEPLLEKDFLAGVTQELIKTLEDNSEKWAVTPDAGDGVVKPSSRADPAQTSDTLALNNQMVTQNRTPHSVCHQKPQAKSGSWDLQTYSADQRTTGNWESHRKSQDMKKRKYDPS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P43351","disprot_id":"DP00437","ncbi_taxon_id":9606,"regions_counter":1,"creator":"aschramm","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":23,"region_id":"DP00437r001","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Structure of the single-strand annealing domain of human RAD52 protein. <i> Singleton MR, Wentzell LM, Liu Y, West SC, Wigley DB. </i> Proc Natl Acad Sci U S A, 2002","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12370410","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-08-26T15:03:53.484Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"1H2I"}],"curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Domain 1 (residues 24–177, the N-terminal 23 residues of the protein are disordered) forms the core of the structure and has a mixed α/β structure.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P43351","date":"2016-09-09T23:32:30.000Z","acc":"P43351","name":"DNA repair protein RAD52 homolog","length":418,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000133035","genes":[{"name":{"value":"RAD52"}}],"alphafold_very_low_content":0.41148325358851673,"disorder_content":0.05502392344497608,"disprot_consensus":{"full":[{"start":1,"end":23,"type":"D"}],"Structural state":[{"start":1,"end":23,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00412","name":"LIM domain","start":10,"end":65},{"id":"PF00412","name":"LIM domain","start":120,"end":176}],"gene3D":[{"start":110,"end":194,"id":"2.10.110.10","name":"Cysteine Rich Protein"},{"start":1,"end":81,"id":"2.10.110.10","name":"Cysteine Rich Protein"}]},"uniref50":"UniRef50_Q62908","sequence":"MPNWGGGNKCGACGRTVYHAEEVQCDGRSFHRCCFLCMVCRKNLDSTTVAIHDAEVYCKSCYGKKYGPKGYGYGQGAGTLNMDRGERLGIKPESSPSPHRPTTNPNTSKFAQKFGGAEKCSRCGDSVYAAEKVIGAGKPWHKNCFRCAKCGKSLESTTLTEKEGEIYCKGCYAKNFGPKGFGYGQGAGALVHAQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Perdicinae","Coturnix"],"uniref90":"UniRef90_Q05158","disprot_id":"DP00438","ncbi_taxon_id":93934,"regions_counter":6,"creator":"esalladini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":115,"region_id":"DP00438r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of cysteine- and glycine-rich protein CRP2. Backbone dynamics reveal motional freedom and independent spatial orientation of the lim domains. <i> Konrat R, Kräutler B, Weiskirchen R, Bister K. </i> J Biol Chem, 1998","term_id":"IDPO:0000002","curator_id":"esalladini","start":68,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"9722554","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1IBI"}],"term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":115,"term_name":"flexible linker","start":68,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"9722554","version":3,"reference_html":"Structure of cysteine- and glycine-rich protein CRP2. Backbone dynamics reveal motional freedom and independent spatial orientation of the lim domains. <i> Konrat R, Kräutler B, Weiskirchen R, Bister K. </i> J Biol Chem, 1998","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006165","region_id":"DP00438r002","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":117,"region_id":"DP00438r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Mutational analysis and NMR spectroscopy of quail cysteine and glycine-rich protein CRP2 reveal an intrinsic segmental flexibility of LIM domains. <i> Kloiber K, Weiskirchen R, Kräutler B, Bister K, Konrat R. </i> J Mol Biol, 1999","term_id":"IDPO:0000002","curator_id":"esalladini","start":82,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"10525413","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1CXX"}],"term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":117,"term_name":"flexible linker","start":82,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"10525413","version":3,"reference_html":"Mutational analysis and NMR spectroscopy of quail cysteine and glycine-rich protein CRP2 reveal an intrinsic segmental flexibility of LIM domains. <i> Kloiber K, Weiskirchen R, Kräutler B, Bister K, Konrat R. </i> J Mol Biol, 1999","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006165","region_id":"DP00438r004","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":194,"region_id":"DP00438r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Mutational analysis and NMR spectroscopy of quail cysteine and glycine-rich protein CRP2 reveal an intrinsic segmental flexibility of LIM domains. <i> Kloiber K, Weiskirchen R, Kräutler B, Bister K, Konrat R. </i> J Mol Biol, 1999","term_id":"IDPO:0000002","curator_id":"esalladini","start":175,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"10525413","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1CXX"}],"term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":194,"term_name":"flexible linker","start":175,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"10525413","version":3,"reference_html":"Mutational analysis and NMR spectroscopy of quail cysteine and glycine-rich protein CRP2 reveal an intrinsic segmental flexibility of LIM domains. <i> Kloiber K, Weiskirchen R, Kräutler B, Bister K, Konrat R. </i> J Mol Biol, 1999","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006165","region_id":"DP00438r006","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_Q05158","date":"2016-09-09T10:17:22.000Z","acc":"Q05158","name":"Cysteine and glycine-rich protein 2","length":194,"organism":"Coturnix japonica","dataset":[],"UniParc":"UPI00001711EB","genes":[{"name":{"value":"CSRP2"}}],"alphafold_very_low_content":0.08762886597938144,"disorder_content":0.36082474226804123,"disprot_consensus":{"full":[{"start":68,"end":117,"type":"D"},{"start":175,"end":194,"type":"D"}],"Structural state":[{"start":68,"end":117,"type":"D"},{"start":175,"end":194,"type":"D"}],"Disorder function":[{"start":68,"end":117,"type":"F"},{"start":175,"end":194,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":551,"end":711},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":762,"end":859},{"id":"PF00570","name":"HRDC domain","start":1156,"end":1216},{"id":"PF01612","name":"3'-5' exonuclease","start":59,"end":228},{"id":"PF09382","name":"RQC domain","start":955,"end":1053},{"id":"PF14493","name":"Helix-turn-helix domain","start":1258,"end":1352},{"id":"PF16124","name":"RecQ zinc-binding","start":871,"end":940}],"gene3D":[{"start":949,"end":1079,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"start":33,"end":236,"id":"3.30.420.10","name":"Ribonuclease H-like superfamily/Ribonuclease H"},{"start":505,"end":731,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":1145,"end":1233,"id":"1.10.150.80","name":"HRDC domain"},{"start":732,"end":948,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_Q14191","sequence":"MSEKKLETTAQQRKCPEWMNVQNKRCAVEERKACVRKSVFEDDLPFLEFTGSIVYSYDASDCSFLSEDISMSLSDGDVVGFDMEWPPLYNRGKLGKVALIQLCVSESKCYLFHVSSMSVFPQGLKMLLENKAVKKAGVGIEGDQWKLLRDFDIKLKNFVELTDVANKKLKCTETWSLNSLVKHLLGKQLLKDKSIRCSNWSKFPLTEDQKLYAATDAYAGFIIYRNLEILDDTVQRFAINKEEEILLSDMNKQLTSISEEVMDLAKHLPHAFSKLENPRRVSILLKDISENLYSLRRMIIGSTNIETELRPSNNLNLLSFEDSTTGGVQQKQIREHEVLIHVEDETWDPTLDHLAKHDGEDVLGNKVERKEDGFEDGVEDNKLKENMERACLMSLDITEHELQILEQQSQEEYLSDIAYKSTEHLSPNDNENDTSYVIESDEDLEMEMLKHLSPNDNENDTSYVIESDEDLEMEMLKSLENLNSGTVEPTHSKCLKMERNLGLPTKEEEEDDENEANEGEEDDDKDFLWPAPNEEQVTCLKMYFGHSSFKPVQWKVIHSVLEERRDNVAVMATGYGKSLCFQYPPVYVGKIGLVISPLISLMEDQVLQLKMSNIPACFLGSAQSENVLTDIKLGKYRIVYVTPEYCSGNMGLLQQLEADIGITLIAVDEAHCISEWGHDFRDSFRKLGSLKTALPMVPIVALTATASSSIREDIVRCLNLRNPQITCTGFDRPNLYLEVRRKTGNILQDLQPFLVKTSSHWEFEGPTIIYCPSRKMTQQVTGELRKLNLSCGTYHAGMSFSTRKDIHHRFVRDEIQCVIATIAFGMGINKADIRQVIHYGAPKDMESYYQEIGRAGRDGLQSSCHVLWAPADINLNRHLLTEIRNEKFRLYKLKMMAKMEKYLHSSRCRRQIILSHFEDKQVQKASLGIMGTEKCCDNCRSRLDHCYSMDDSEDTSWDFGPQAFKLLSAVDILGEKFGIGLPILFLRGSNSQRLADQYRRHSLFGTGKDQTESWWKAFSRQLITEGFLVEVSRYNKFMKICALTKKGRNWLHKANTESQSLILQANEELCPKKLLLPSSKTVSSGTKEHCYNQVPVELSTEKKSNLEKLYSYKPCDKISSGSNISKKSIMVQSPEKAYSSSQPVISAQEQETQIVLYGKLVEARQKHANKMDVPPAILATNKILVDMAKMRPTTVENVKRIDGVSEGKAAMLAPLLEVIKHFCQTNSVQTDLFSSTKPQEEQKTSLVAKNKICTLSQSMAITYSLFQEKKMPLKSIAESRILPLMTIGMHLSQAVKAGCPLDLERAGLTPEVQKIIADVIRNPPVNSDMSKISLIRMLVPENIDTYLIHMAIEILKHGPDSGLQPSCDVNKRRCFPGSEEICSSSKRSKEEVGINTETSSAERKRRLPVWFAKGSDTSKKLMDKTKRGGLFS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q14191","disprot_id":"DP00443","ncbi_taxon_id":9606,"regions_counter":13,"creator":"maspromonte","regions":[{"start":1064,"end":1092,"reference_id":"16339893","reference_source":"pmid","reference_html":"Solution structure of a multifunctional DNA- and protein-binding motif of human Werner syndrome protein. <i> Hu JS, Feng H, Zeng W, Lin GX, Xi XG. </i> Proc Natl Acad Sci U S A, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2AXL"}],"region_id":"DP00443r013","statement":[{"text":"The solution structure of the DPBD, the first of a WRN fragment, has been solved by NMR. DPBD consists of a winged helix-like motif and an unstructured C-terminal region of approximately 20 aa.","type":"Abstract"},{"text":"The ensemble within the box displays all 144 residues and illustrates the disordered N and C termini.","type":"Figure"},{"text":"The C-terminal 24 residues are largely unstructured (Fig. 2). The unstructured C terminus contains two cysteine residues, C1070 and C1090, which most likely contribute to the oligomerization of the protein.","type":"Results"},{"text":"The significance of the unstructured C terminus in the DPBD in the DNA and protein binding remains to be determined.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:27:04.387Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q14191","date":"2016-09-04T21:55:49.000Z","acc":"Q14191","name":"Werner syndrome ATP-dependent helicase","length":1432,"organism":"Homo sapiens","dataset":["Cancer-related proteins","RNA-binding proteins","NDDs-related proteins"],"UniParc":"UPI000013E49D","genes":[{"name":{"value":"WRN"},"synonyms":[{"value":"RECQ3"},{"value":"RECQL2"}]}],"alphafold_very_low_content":0.3128491620111732,"disorder_content":0.020251396648044692,"disprot_consensus":{"full":[{"start":1064,"end":1092,"type":"D"}],"Structural state":[{"start":1064,"end":1092,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00011","name":"Hsp20/alpha crystallin family","start":69,"end":162},{"id":"PF00525","name":"Alpha crystallin A chain, N terminal","start":1,"end":56}],"gene3D":[{"start":52,"end":175,"id":"2.60.40.790","name":"2.60.40.790"}]},"uniref50":"UniRef50_P02511","sequence":"MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P02511","disprot_id":"DP00445","ncbi_taxon_id":9606,"regions_counter":13,"creator":"smribeiro","regions":[{"term_namespace":"Disorder function","ec_ontology":"ECO","end":175,"term_name":"flexible C-terminal tail","released":"2024_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers. <i> Jehle S, Rajagopal P, Bardiaux B, Markovic S, Kühne R, Stout JR, Higman VA, Klevit RE, van Rossum BJ, Oschkinat H. </i> Nat Struct Mol Biol, 2010","term_id":"IDPO:0000031","curator_id":"smribeiro","start":166,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"20802487","version":4,"curator_orcid":"0000-0002-7698-1170","date":"2024-11-30T02:14:24.687Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00445r002","ec_go":"EXP","disprot_namespace":"Disorder function","statement":[{"text":"The heterogeneous region 1 (HR1), the IXI motif, the flexible C-terminal residues Lys166–Lys175 and three disease-related mutations involved in cataract and myopathy (R120G, D140N and Gln151-stop) are indicated.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-02T13:46:15.874Z"}},{"start":153,"end":175,"reference_id":"26458046","reference_source":"pmid","reference_html":"The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client. <i> Mainz A, Peschek J, Stavropoulou M, Back KC, Bardiaux B, Asami S, Prade E, Peters C, Weinkauf S, Buchner J, Reif B. </i> Nat Struct Mol Biol, 2015","date":"2024-12-03T14:33:11.952Z","curator_id":"ralderson","curator_name":"Reid Alderson","curator_orcid":"0000-0001-5163-2276","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"BMRB","id":"26640"}],"region_id":"DP00445r005","statement":[{"text":"The C-terminal residues of αB are highly dynamic and yielded narrow\nresonances in solution-state 1H-15N correlation experiments (Fig. 2a).\nIn contrast to previous studies, in which only residues E164–K175\nhave been observed36,37, in our study we assigned 11 additional\nresidues, thus yielding assignments for the entire C-terminal stretch\nS153–K175 (Supplementary Table 2)","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-04T16:52:35.040Z"}},{"start":166,"end":175,"reference_id":"20802487","reference_source":"pmid","reference_html":"Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers. <i> Jehle S, Rajagopal P, Bardiaux B, Markovic S, Kühne R, Stout JR, Higman VA, Klevit RE, van Rossum BJ, Oschkinat H. </i> Nat Struct Mol Biol, 2010","date":"2024-11-30T02:06:17.083Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7.5,"statements":[{"type":"Results","text":"SAXS data obtained at pH 7.5 for oligomeric αB in solution were used to calculate six bead models, assuming tetrahedral symmetry, consistent with previous electron microscopy studies25."}]}],"region_id":"DP00445r006","statement":[{"text":"The individual bead models (Supplementary Fig. 6b) generated using the program GASBOR38 have extrusions emanating from the central body, which we interpret as flexible C-terminal residues 166–175 of the oligomer39.","type":"Results"},{"text":"We consider this solution as one species in a heterogeneous ensemble of oligomers. Variable conformations of the flexible C-terminal extensions (residues Lys166–Lys175) and variable intermolecular interactions may contribute to the observed heterogeneity.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-02T13:53:37.914Z"}},{"start":151,"end":175,"reference_id":"20802487","reference_source":"pmid","reference_html":"Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers. <i> Jehle S, Rajagopal P, Bardiaux B, Markovic S, Kühne R, Stout JR, Higman VA, Klevit RE, van Rossum BJ, Oschkinat H. </i> Nat Struct Mol Biol, 2010","date":"2024-11-30T19:40:20.811Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP00445r008","statement":[{"text":"At pH 6.5, the involved isoleucines and threonines (Thr132 and Thr134 in β8 and Thr158 and Thr162 of the C terminus) show chemical-shift perturbations or doubling of intraresidual cross-peaks (for example, at ∼59–63 p.p.m., ∼36–39 p.p.m. or 26 p.p.m. in F1 and at 69–72.5 p.p.m. or 9.5–27 p.p.m. in F2), indicating a pH-dependent change in the substrate binding groove (Figs. 3a and 5a). ","type":"Results"},{"text":"Residues 151-175 are unmodeled in PDB entry 2KLR ","type":"Curator statement"},{"text":"NMR spectra collected at pH 7.5 reveal a structurally homogeneous part of the protein comprising α-crystallin domain residues 71–150, with the exception of Ser76, Val77 and Asn78 in the β3 strand, which each show two backbone 15N signals.","type":"Results"}],"cross_refs":[{"db":"ELM","id":"LIG_sHSP_IxI_1"},{"db":"PDB","id":"2KLR"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-09T15:49:30.660Z"}}],"released":"2016_10","uniref100":"UniRef100_P02511","date":"2016-09-13T10:47:06.000Z","acc":"P02511","name":"Alpha-crystallin B chain","length":175,"organism":"Homo sapiens","dataset":["Age-related disorders proteins"],"UniParc":"UPI0000173D33","genes":[{"name":{"value":"CRYAB","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:2389","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:2389"}}]},"synonyms":[{"value":"CRYA2"},{"value":"HSPB5"}]}],"alphafold_very_low_content":0.13142857142857142,"disorder_content":0.14285714285714285,"disprot_consensus":{"full":[{"start":151,"end":175,"type":"D"}],"Structural state":[{"start":151,"end":175,"type":"D"}],"Disorder function":[{"start":166,"end":175,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00017","name":"SH2 domain","start":46,"end":127}],"gene3D":[{"start":18,"end":185,"id":"3.30.505.10","name":"SH2 domain"}]},"uniref50":"UniRef50_O35718","sequence":"MVTHSKFPAAGMSRPLDTSLRLKTFSSKSEYQLVVNAVRKLQESGFYWSAVTGGEANLLLSAEPAGTFLIRDSSDQRHFFTLSVKTQSGTKNLRIQCEGGSFSLQSDPRSTQPVPRFDCVLKLVHHYMPPPGTPSFSLPPTEPSSEVPEQPPAQALPGSTPKRAYYIYSGGEKIPLVLSRPLSSNVATLQHLCRKTVNGHLDSYEKVTQLPGPIREFLDQYDAPL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_O35718","disprot_id":"DP00446","ncbi_taxon_id":10090,"regions_counter":8,"creator":"ahatos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":163,"region_id":"DP00446r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Secondary structure assignment of mouse SOCS3 by NMR defines the domain boundaries and identifies an unstructured insertion in the SH2 domain. <i> Babon JJ, Yao S, DeSouza DP, Harrison CF, Fabri LJ, Liepinsh E, Scrofani SD, Baca M, Norton RS. </i> FEBS J, 2005","term_id":"IDPO:0000002","curator_id":"esalladini","start":128,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"BMRB","id":"6580"}],"reference_id":"16302975","statement":[{"text":"Significantly, there was a large unstructured region between Met128 and Arg163 that contained a high proportion of proline residues (12 out of 35).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":129,"end":163,"reference_id":"16630890","reference_source":"pmid","reference_html":"The structure of SOCS3 reveals the basis of the extended SH2 domain function and identifies an unstructured insertion that regulates stability. <i> Babon JJ, McManus EJ, Yao S, DeSouza DP, Mielke LA, Sprigg NS, Willson TA, Hilton DJ, Nicola NA, Baca M, Nicholson SE, Norton RS. </i> Mol Cell, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2BBU"}],"region_id":"DP00446r002","statement":[{"text":"The SH2 domain is formed by residues Gly45-Asn185, excluding an unstructured insert of 35 residues (Pro129-Arg163).","type":"Results"},{"text":"Following helix B, there is a 35 residue insert, a PEST motif (Rogers et al., 1986). This displays no evidence of structure, and backbone amide NMR relaxation data suggest a high degree of flexibility (see Figures S1 and S2 in the Supplemental Data available with this article online).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":129,"end":163,"reference_id":"16630890","reference_source":"pmid","reference_html":"The structure of SOCS3 reveals the basis of the extended SH2 domain function and identifies an unstructured insertion that regulates stability. <i> Babon JJ, McManus EJ, Yao S, DeSouza DP, Mielke LA, Sprigg NS, Willson TA, Hilton DJ, Nicola NA, Baca M, Nicholson SE, Norton RS. </i> Mol Cell, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000048","term_name":"limited proteolysis display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00446r003","statement":[{"text":"Intracellular levels of SOCS3 are strongly regulated by proteolysis. As PEST motifs are known to be signals for protein degradation in vivo, we measured the half-life of SOCS3 proteins that lacked the PEST motif, as well as constructs lacking both the SOCS box and the N-terminal region.","type":"Results"},{"text":"Pulse-chase experiments show that removing the PEST motif decreases SOCS3 turnover (Figure 5A) in both full-length SOCS3 (Figure 5A, left panel) and SOCS3(22-185) (Figure 5A, right panel). Removing the PEST motif had a greater effect on SOCS3 stability than did removing both the SOCS box and N-terminal domain.","type":"Results"},{"text":"The PEST motif consists of the Pro129-Arg163 residues.","type":"Curator statement"}],"ec_go":"IPI","disprot_namespace":"Disorder function"},{"start":186,"end":225,"reference_id":"18590740","reference_source":"pmid","reference_html":"The SOCS box domain of SOCS3: structure and interaction with the elonginBC-cullin5 ubiquitin ligase. <i> Babon JJ, Sabo JK, Soetopo A, Yao S, Bailey MF, Zhang JG, Nicola NA, Norton RS. </i> J Mol Biol, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00446r004","statement":[{"text":"A 42-residue 15N-labelled recombinant SOCS box peptide was produced; the 1H–15N HSQC spectrum of this isolated peptide is characteristic of that of an unstructured protein (Fig. 4a).","type":"Results"},{"text":"Overhauser enhancement spectroscopy (NOESY) experiments of unlabelled SOCS box domain also suggested that the peptide was completely unstructured in solution (data not shown).","type":"Results"},{"text":"The SOCS box is unstructured in isolation but becomes structured upon elonginBC association\nThese data imply that the C-terminal half of the SOCS box undergoes significant conformational exchange in the absence of bound cullin5 whether as an isolated domain or as part of full-length SOCS3.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":186,"end":197,"reference_id":"18590740","reference_source":"pmid","reference_html":"The SOCS box domain of SOCS3: structure and interaction with the elonginBC-cullin5 ubiquitin ligase. <i> Babon JJ, Sabo JK, Soetopo A, Yao S, Bailey MF, Zhang JG, Nicola NA, Norton RS. </i> J Mol Biol, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2JZ3"}],"region_id":"DP00446r005","statement":[{"text":"Resonances that could be assigned in this region showed α-helical chemical shifts but were significantly broadened and displayed NOEs only to adjacent residues. In contrast, the N-terminal half of the SOCS box, which contains the elonginBC-binding motif (the BC box, residues 1–12) was completely assigned and well structured.","type":"Results"},{"text":"The SOCS box is unstructured in isolation but becomes structured upon elonginBC association\nThese data imply that the C-terminal half of the SOCS box undergoes significant conformational exchange in the absence of bound cullin5 whether as an isolated domain or as part of full-length SOCS3.","type":"Results"},{"text":"This region, the SOCS3 elonginBC binding motif (termed the BC box), which is completely unstructured as an isolated peptide and only adopts structure upon binding, exists as a nine-residue α-helix with a three-residue N-terminal extension.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":186,"end":197,"reference_id":"18590740","reference_source":"pmid","reference_html":"The SOCS box domain of SOCS3: structure and interaction with the elonginBC-cullin5 ubiquitin ligase. <i> Babon JJ, Sabo JK, Soetopo A, Yao S, Bailey MF, Zhang JG, Nicola NA, Norton RS. </i> J Mol Biol, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"2JZ3"}],"region_id":"DP00446r006","statement":[{"text":"Resonances that could be assigned in this region showed α-helical chemical shifts but were significantly broadened and displayed NOEs only to adjacent residues. In contrast, the N-terminal half of the SOCS box, which contains the elonginBC-binding motif (the BC box, residues 1–12) was completely assigned and well structured.","type":"Results"},{"text":"The SOCS box is unstructured in isolation but becomes structured upon elonginBC association\nThese data imply that the C-terminal half of the SOCS box undergoes significant conformational exchange in the absence of bound cullin5 whether as an isolated domain or as part of full-length SOCS3.","type":"Results"},{"text":"This region, the SOCS3 elonginBC binding motif (termed the BC box), which is completely unstructured as an isolated peptide and only adopts structure upon binding, exists as a nine-residue α-helix with a three-residue N-terminal extension.","type":"Results"}],"interaction_partner":[{"db":"UniProt","id":"Q15370","partner_start":null,"partner_end":null}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":186,"end":197,"reference_id":"18590740","reference_source":"pmid","reference_html":"The SOCS box domain of SOCS3: structure and interaction with the elonginBC-cullin5 ubiquitin ligase. <i> Babon JJ, Sabo JK, Soetopo A, Yao S, Bailey MF, Zhang JG, Nicola NA, Norton RS. </i> J Mol Biol, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"Q15370","partner_start":null,"partner_end":null}],"region_id":"DP00446r007","statement":[{"text":"Therefore, the minimal high-affinity binding epitope for elonginBC on SOCS3 is VATLQHLCRKTV 197, corresponding to residues 1–12 of the SOCS box domain.","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":15,"end":28,"reference_id":"16905102","reference_source":"pmid","reference_html":"Structural basis for phosphotyrosine recognition by suppressor of cytokine signaling-3. <i> Bergamin E, Wu J, Hubbard SR. </i> Structure, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2HMH"}],"region_id":"DP00446r008","statement":[{"text":"Residues 15–28, which include residues 22–28 of the kinase inhibitory region, are disordered.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_O35718","date":"2016-09-07T10:26:26.000Z","acc":"O35718","name":"Suppressor of cytokine signaling 3","length":225,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000004085","genes":[{"name":{"value":"Socs3","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:1201791","url":"http://www.informatics.jax.org/marker/MGI:1201791"}}]},"synonyms":[{"value":"Cis3"},{"value":"Cish3"}]}],"alphafold_very_low_content":0.2088888888888889,"disorder_content":0.4,"disprot_consensus":{"full":[{"start":15,"end":28,"type":"D"},{"start":128,"end":163,"type":"D"},{"start":186,"end":197,"type":"T"},{"start":198,"end":225,"type":"D"}],"Structural state":[{"start":15,"end":28,"type":"D"},{"start":128,"end":163,"type":"D"},{"start":186,"end":225,"type":"D"}],"Disorder function":[{"start":129,"end":163,"type":"F"}],"Structural transition":[{"start":186,"end":197,"type":"T"}],"Molecular function":[{"start":186,"end":197,"type":"F"}]}},{"acc":"P12579","sequence":"MEKFAPEFHGEDANNRATKFLESIKGKFTSPKDPKKKDSIISVNSIDIEVTKESPITSNSTIINPTNETDDNAGNKPNYQRKPLVSFKEDPIPSDNPFSKLYKETIETFDNNEEESSYSYEEINDQTNDNITARLDRIDEKLSEILGMLHTLVVASAGPTSARDGIRDAMVGLREEMIEKIRTEALMTNDRLEAMARLRNEESEKMAKDTSDEVSLNPTSEKLNNLLEGNDSDNDLSLEDF","creator":"slonghi","dataset":["Viral proteins"],"date":"2016-09-06T16:52:24.000Z","disprot_id":"DP00447","features":{"pfam":[{"id":"PF02478","name":"Pneumovirus phosphoprotein","start":72,"end":231}]},"genes":[{"name":{"value":"P","evidences":[],"_id":"685af523b4ac24d5329d7db4"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d7db3"}],"length":241,"name":"Phosphoprotein","ncbi_taxon_id":11260,"organism":"Human respiratory syncytial virus A (strain Long)","regions_counter":52,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Pneumoviridae","Orthopneumovirus"],"UniParc":"UPI0000134B5E","uniref100":"UniRef100_P12579","uniref50":"UniRef50_P03421","uniref90":"UniRef90_P03421","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":164,"end":241,"interaction_partner":[],"reference_html":"Structural analysis of the human respiratory syncytial virus phosphoprotein: characterization of an alpha-helical domain involved in oligomerization. <i> Llorente MT, García-Barreno B, Calero M, Camafeita E, López JA, Longhi S, Ferrón F, Varela PF, Melero JA. </i> J Gen Virol, 2006","reference_id":"16361428","region_id":"DP00447r001","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"N-terminal sequencing and MS set the limits of the trypsin-resistant fragment (X) between aa 104 and 163. ","_id":"685af523b4ac24d5329d7d3e"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-04T09:34:26.919Z","_id":"685af523b4ac24d5329d7d3f"},"version":3,"_id":"685af523b4ac24d5329d7d3d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":103,"interaction_partner":[],"reference_html":"Structural analysis of the human respiratory syncytial virus phosphoprotein: characterization of an alpha-helical domain involved in oligomerization. <i> Llorente MT, García-Barreno B, Calero M, Camafeita E, López JA, Longhi S, Ferrón F, Varela PF, Melero JA. </i> J Gen Virol, 2006","reference_id":"16361428","region_id":"DP00447r052","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"N-terminal sequencing and MS set the limits of the trypsin-resistant fragment (X) between aa 104 and 163. ","_id":"685af523b4ac24d5329d7db1"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-04T09:34:25.866Z","_id":"685af523b4ac24d5329d7db2"},"version":1,"_id":"685af523b4ac24d5329d7db0","reference_source":"pmid"}],"__v":0,"disorder_content":0.7510373443983402,"disprot_consensus":{"full":[{"start":1,"end":103,"type":"D"},{"start":164,"end":241,"type":"D"}],"Structural state":[{"start":1,"end":103,"type":"D"},{"start":164,"end":241,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02181","name":"Formin Homology 2 Domain","start":618,"end":987},{"id":"PF18382","name":"Formin N-terminal GBD","start":17,"end":101},{"id":"PF24959","name":"FHOD1/3 FH3 domain","start":174,"end":308}],"gene3D":[{"start":687,"end":1020,"id":"1.20.58.2220","name":"Formin, FH2 domain"},{"start":1,"end":339,"id":"1.25.10.10","name":"Leucine-rich Repeat Variant"}]},"uniref50":"UniRef50_Q9Y613","sequence":"MAGGEDRGDGEPVSVVTVRVQYLEDTDPFACANFPEPRRAPTCSLDGALPLGAQIPAVHRLLGAPLKLEDCALQVSPSGYYLDTELSLEEQREMLEGFYEEISKGRKPTLILRTQLSVRVNAILEKLYSSSGPELRRSLFSLKQIFQEDKDLVPEFVHSEGLSCLIRVGAAADHNYQSYILRALGQLMLFVDGMLGVVAHSDTIQWLYTLCASLSRLVVKTALKLLLVFVEYSENNAPLFIRAVNSVASTTGAPPWANLVSILEEKNGADPELLVYTVTLINKTLAALPDQDSFYDVTDALEQQGMEALVQRHLGTAGTDVDLRTQLVLYENALKLEDGDIEEAPGAGGRRERRKPSSEEGKRSRRSLEGGGCPARAPEPGPTGPASPVGPTSSTGPALLTGPASSPVGPPSGLQASVNLFPTISVAPSADTSSERSIYKARFLENVAAAETEKQVALAQGRAETLAGAMPNEAGGHPDARQLWDSPETAPAARTPQSPAPCVLLRAQRSLAPEPKEPLIPASPKAEPIWELPTRAPRLSIGDLDFSDLGEDEDQDMLNVESVEAGKDIPAPSPPLPLLSGVPPPPPLPPPPPIKGPFPPPPPLPLAAPLPHSVPDSSALPTKRKTVKLFWRELKLAGGHGVSASRFGPCATLWASLDPVSVDTARLEHLFESRAKEVLPSKKAGEGRRTMTTVLDPKRSNAINIGLTTLPPVHVIKAALLNFDEFAVSKDGIEKLLTMMPTEEERQKIEEAQLANPDIPLGPAENFLMTLASIGGLAARLQLWAFKLDYDSMEREIAEPLFDLKVGMEQLVQNATFRCILATLLAVGNFLNGSQSSGFELSYLEKVSEVKDTVRRQSLLHHLCSLVLQTRPESSDLYSEIPALTRCAKVDFEQLTENLGQLERRSRAAEESLRSLAKHELAPALRARLTHFLDQCARRVAMLRIVHRRVCNRFHAFLLYLGYTPQAAREVRIMQFCHTLREFALEYRTCRERVLQQQQKQATYRERNKTRGRMITETEKFSGVAGEAPSNPSVPVAVSSGPGRGDADSHASMKSLLTSRPEDTTHNRRSRGMVQSSSPIMPTVGPSTASPEEPPGSSLPSDTSDEIMDLLVQSVTKSSPRALAARERKRSRGNRKSLRRTLKSGLGDDLVQALGLSKGPGLEV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9Y613","disprot_id":"DP00448","ncbi_taxon_id":9606,"regions_counter":6,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1164,"region_id":"DP00448r001","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1. <i> Schönichen A, Alexander M, Gasteier JE, Cuesta FE, Fackler OT, Geyer M. </i> J Biol Chem, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1104,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16361249","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":1164,"term_name":"disorder to order","start":1104,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16361249","version":2,"reference_html":"Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1. <i> Schönichen A, Alexander M, Gasteier JE, Cuesta FE, Fackler OT, Geyer M. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0007680","region_id":"DP00448r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":1164,"term_name":"protein binding","start":1104,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16361249","version":3,"reference_html":"Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1. <i> Schönichen A, Alexander M, Gasteier JE, Cuesta FE, Fackler OT, Geyer M. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007680","region_id":"DP00448r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1164,"region_id":"DP00448r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1. <i> Schönichen A, Alexander M, Gasteier JE, Cuesta FE, Fackler OT, Geyer M. </i> J Biol Chem, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1104,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16361249","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":1164,"term_name":"disorder to order","start":1104,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16361249","version":2,"reference_html":"Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1. <i> Schönichen A, Alexander M, Gasteier JE, Cuesta FE, Fackler OT, Geyer M. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00448r005","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":1164,"term_name":"protein binding","start":1104,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16361249","version":3,"reference_html":"Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1. <i> Schönichen A, Alexander M, Gasteier JE, Cuesta FE, Fackler OT, Geyer M. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00448r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q9Y613","date":"2016-08-12T17:32:31.000Z","acc":"Q9Y613","name":"FH1/FH2 domain-containing protein 1","length":1164,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012A737","genes":[{"name":{"value":"FHOD1"},"synonyms":[{"value":"FHOS"},{"value":"FHOS1"}]}],"alphafold_very_low_content":0.32216494845360827,"disorder_content":0.05240549828178694,"disprot_consensus":{"full":[{"start":1104,"end":1164,"type":"T"}],"Structural state":[{"start":1104,"end":1164,"type":"D"}],"Structural transition":[{"start":1104,"end":1164,"type":"T"}],"Molecular function":[{"start":1104,"end":1164,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00452","name":"Apoptosis regulator proteins, Bcl-2 family","start":90,"end":188},{"id":"PF02180","name":"Bcl-2 homology region 4","start":1,"end":26}],"gene3D":[{"start":1,"end":209,"id":"1.10.437.10","name":"Blc2-like"}]},"uniref50":"UniRef50_P53563","sequence":"MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEETEPERETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIASWMATYLNDHLEPWIQENGGWDTFVDLYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_P53563","disprot_id":"DP00449","ncbi_taxon_id":10116,"regions_counter":1,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":80,"region_id":"DP00449r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of rat Bcl-xL. Implications for the function of the Bcl-2 protein family. <i> Aritomi M, Kunishima N, Inohara N, Ishibashi Y, Ohta S, Morikawa K. </i> J Biol Chem, 1997","term_id":"IDPO:0000002","curator_id":"atantos","start":31,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1AF3"}],"reference_id":"9346936","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P53563","date":"2016-09-08T12:18:02.000Z","acc":"P53563","name":"Bcl-2-like protein 1","length":233,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI00001708BC","genes":[{"name":{"value":"Bcl2l1"},"synonyms":[{"value":"Bclx"},{"value":"Blc2l"}]}],"alphafold_very_low_content":0.30472103004291845,"disorder_content":0.2145922746781116,"disprot_consensus":{"full":[{"start":31,"end":80,"type":"D"}],"Structural state":[{"start":31,"end":80,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00111","name":"2Fe-2S iron-sulfur cluster binding domain","start":8,"end":77},{"id":"PF00941","name":"FAD binding domain in molybdopterin dehydrogenase","start":234,"end":411},{"id":"PF01315","name":"Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain","start":587,"end":693},{"id":"PF01799","name":"[2Fe-2S] binding domain","start":87,"end":160},{"id":"PF02738","name":"Molybdopterin cofactor-binding domain","start":704,"end":946},{"id":"PF03450","name":"CO dehydrogenase flavoprotein C-terminal domain","start":420,"end":523},{"id":"PF20256","name":"Molybdopterin cofactor-binding domain","start":971,"end":1236}],"gene3D":[{"start":1,"end":1332,"id":"3.30.365.10","name":"Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain"}]},"uniref50":"UniRef50_P22985","sequence":"MTADELVFFVNGKKVVEKNADPETTLLAYLRRKLGLRGTKLGCGEGGCGACTVMLSKYDRLQDKIIHFSANACLAPICTLHHVAVTTVEGIGSTKTRLHPVQERIAKSHGSQCGFCTPGIVMSMYTLLRNQPEPTVEEIEDAFQGNLCRCTGYRPILQGFRTFAKNGGCCGGNGNNPNCCMNQKKDHTVTLSPSLFNPEEFMPLDPTQEPIFPPELLRLKDVPPKQLRFEGERVTWIQASTLKELLDLKAQHPEAKLVVGNTEIGIEMKFKNQLFPMIICPAWIPELNAVEHGPEGISFGAACALSSVEKTLLEAVAKLPTQKTEVFRGVLEQLRWFAGKQVKSVASLGGNIITASPISDLNPVFMASGTKLTIVSRGTRRTVPMDHTFFPSYRKTLLGPEEILLSIEIPYSREDEFFSAFKQASRREDDIAKVTCGMRVLFQPGSMQVKELALCYGGMADRTISALKTTQKQLSKFWNEKLLQDVCAGLAEELSLSPDAPGGMIEFRRTLTLSFFFKFYLTVLKKLGKDSKDKCGKLDPTYTSATLLFQKDPPANIQLFQEVPNGQSKEDTVGRPLPHLAAAMQASGEAVYCDDIPRYENELFLRLVTSTRAHAKIKSIDVSEAQKVPGFVCFLSADDIPGSNETGLFNDETVFAKDTVTCVGHIIGAVVADTPEHAERAAHVVKVTYEDLPAIITIEDAIKNNSFYGSELKIEKGDLKKGFSEADNVVSGELYIGGQDHFYLETHCTIAIPKGEEGEMELFVSTQNAMKTQSFVAKMLGVPVNRILVRVKRMGGGFGGKETRSTLVSVAVALAAYKTGHPVRCMLDRNEDMLITGGRHPFLARYKVGFMKTGTIVALEVDHYSNAGNSRDLSHSIMERALFHMDNCYKIPNIRGTGRLCKTNLSSNTAFRGFGGPQALFIAENWMSEVAVTCGLPAEEVRWKNMYKEGDLTHFNQRLEGFSVPRCWDECLKSSQYYARKSEVDKFNKENCWKKRGLCIIPTKFGISFTVPFLNQAGALIHVYTDGSVLVSHGGTEMGQGLHTKMVQVASKALKIPISKIYISETSTNTVPNSSPTAASVSTDIYGQAVYEACQTILKRLEPFKKKNPDGSWEDWVMAAYQDRVSLSTTGFYRTPNLGYSFETNSGNAFHYFTYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPAIDIGQVEGAFVQGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFGSIPTEFRVSLLRDCPNKKAIYASKAVGEPPLFLGASVFFAIKDAIRAARAQHTNNNTKELFRLDSPATPEKIRNACVDKFTTLCVTGAPGNCKPWSLRV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P80457","disprot_id":"DP00450","ncbi_taxon_id":9913,"regions_counter":4,"creator":"maspromonte","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":191,"region_id":"DP00450r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion. <i> Enroth C, Eger BT, Okamoto K, Nishino T, Nishino T, Pai EF. </i> Proc Natl Acad Sci U S A, 2000","term_id":"IDPO:0000002","curator_id":"maspromonte","start":166,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"11005854","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":191,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion. <i> Enroth C, Eger BT, Okamoto K, Nishino T, Nishino T, Pai EF. </i> Proc Natl Acad Sci U S A, 2000","term_id":"GO:0005515","curator_id":"maspromonte","start":166,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"11005854","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00450r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P80457","date":"2016-09-05T21:26:25.000Z","acc":"P80457","name":"Xanthine dehydrogenase/oxidase","length":1332,"organism":"Bos taurus","dataset":[],"UniParc":"UPI000011366B","genes":[{"name":{"value":"XDH"}}],"alphafold_very_low_content":0.017267267267267267,"disorder_content":0.01951951951951952,"disprot_consensus":{"full":[{"start":166,"end":191,"type":"D"}],"Structural state":[{"start":166,"end":191,"type":"D"}],"Molecular function":[{"start":166,"end":191,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00928","name":"Adaptor complexes medium subunit family","start":160,"end":435},{"id":"PF01217","name":"Clathrin adaptor complex small chain","start":2,"end":125}],"gene3D":[{"start":285,"end":394,"id":"2.60.40.1170","name":"Mu homology domain, subdomain B"},{"start":1,"end":141,"id":"3.30.450.60","name":"3.30.450.60"},{"start":161,"end":432,"id":"2.60.40.1170","name":"Mu homology domain, subdomain B"}]},"uniref50":"UniRef50_Q96CW1","sequence":"MIGGLFIYNHKGEVLISRVYRDDIGRNAVDAFRVNVIHARQQVRSPVTNIARTSFFHVKRSNIWLAAVTKQNVNAAMVFEFLYKMCDVMAAYFGKISEENIKNNFVLIYELLDEILDFGYPQNSETGALKTFITQQGIKSQHQTKEEQSQITSQVTGQIGWRREGIKYRRNELFLDVLESVNLLMSPQGQVLSAHVSGRVVMKSYLSGMPECKFGMNDKIVIEKQGKGTADETSKSGKQSIAIDDCTFHQCVRLSKFDSERSISFIPPDGEFELMRYRTTKDIILPFRVIPLVREVGRTKLEVKVVIKSNFKPSLLAQKIEVRIPTPLNTSGVQVICMKGKAKYKASENAIVWKIKRMAGMKESQISAEIELLPTNDKKKWARPPISMNFEVPFAPSGLKVRYLKVFEPKLNYSDHDVIKWVRYIGRSGIYETRC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_Q96CW1","disprot_id":"DP00455","ncbi_taxon_id":10116,"regions_counter":6,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":158,"region_id":"DP00455r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"A large-scale conformational change couples membrane recruitment to cargo binding in the AP2 clathrin adaptor complex. <i> Jackson LP, Kelly BT, McCoy AJ, Gaffry T, James LC, Collins BM, Höning S, Evans PR, Owen DJ. </i> Cell, 2010","term_id":"IDPO:0000002","curator_id":"bszabo","start":130,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"20603002","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2XA7"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":158,"term_name":"disorder to order","start":130,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"20603002","version":2,"reference_html":"A large-scale conformational change couples membrane recruitment to cargo binding in the AP2 clathrin adaptor complex. <i> Jackson LP, Kelly BT, McCoy AJ, Gaffry T, James LC, Collins BM, Höning S, Evans PR, Owen DJ. </i> Cell, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00455r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":158,"term_name":"protein binding","start":130,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"20603002","version":3,"reference_html":"A large-scale conformational change couples membrane recruitment to cargo binding in the AP2 clathrin adaptor complex. <i> Jackson LP, Kelly BT, McCoy AJ, Gaffry T, James LC, Collins BM, Höning S, Evans PR, Owen DJ. </i> Cell, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00455r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":239,"region_id":"DP00455r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Molecular architecture and functional model of the endocytic AP2 complex. <i> Collins BM, McCoy AJ, Kent HM, Evans PR, Owen DJ. </i> Cell, 2002","term_id":"IDPO:0000002","curator_id":"bszabo","start":223,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"12086608","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2VGL"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":158,"region_id":"DP00455r005","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Molecular architecture and functional model of the endocytic AP2 complex. <i> Collins BM, McCoy AJ, Kent HM, Evans PR, Owen DJ. </i> Cell, 2002","term_id":"IDPO:0000002","curator_id":"bszabo","start":135,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"12086608","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2VGL"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":158,"term_name":"flexible linker","start":135,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"12086608","version":3,"reference_html":"Molecular architecture and functional model of the endocytic AP2 complex. <i> Collins BM, McCoy AJ, Kent HM, Evans PR, Owen DJ. </i> Cell, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006220","region_id":"DP00455r006","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_Q96CW1","date":"2016-09-09T13:17:16.000Z","acc":"P84092","name":"AP-2 complex subunit mu","length":435,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI0000000DD8","genes":[{"name":{"value":"Ap2m1"}}],"alphafold_very_low_content":0.03218390804597701,"disorder_content":0.10574712643678161,"disprot_consensus":{"full":[{"start":130,"end":158,"type":"T"},{"start":223,"end":239,"type":"D"}],"Structural state":[{"start":130,"end":158,"type":"D"},{"start":223,"end":239,"type":"D"}],"Structural transition":[{"start":130,"end":158,"type":"T"}],"Molecular function":[{"start":130,"end":158,"type":"F"}],"Disorder function":[{"start":135,"end":158,"type":"F"}]}},{"features":{"pfam":[{"id":"PF14852","name":"Fis1 N-terminal tetratricopeptide repeat","start":34,"end":62},{"id":"PF14853","name":"Fis1 C-terminal tetratricopeptide repeat","start":71,"end":123}],"gene3D":[{"start":1,"end":151,"id":"1.25.40.10","name":"Tetratricopeptide repeat domain"}]},"uniref50":"UniRef50_Q9Y3D6","sequence":"MEAVLNELVSVEDLLKFEKKFQSEKAAGSVSKSTQFEYAWCLVRSKYNDDIRKGIVLLEELLPKGSKEEQRDYVFYLAVGNYRLKEYEKALKYVRGLLQTEPQNNQAKELERLIDKAMKKDGLVGMAIVGGMALGVAGLAGLIGLAVSKSKS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9Y3D6","disprot_id":"DP00457","ncbi_taxon_id":9606,"regions_counter":4,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":145,"region_id":"DP00457r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The solution structure of human mitochondria fission protein Fis1 reveals a novel TPR-like helix bundle. <i> Suzuki M, Jeong SY, Karbowski M, Youle RJ, Tjandra N. </i> J Mol Biol, 2003","term_id":"IDPO:0000002","curator_id":"eschad","start":121,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1PC2"}],"reference_id":"14623186","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":145,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The solution structure of human mitochondria fission protein Fis1 reveals a novel TPR-like helix bundle. <i> Suzuki M, Jeong SY, Karbowski M, Youle RJ, Tjandra N. </i> J Mol Biol, 2003","term_id":"GO:0060090","curator_id":"eschad","start":121,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"14623186","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00457r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":145,"term_name":"lipid binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The solution structure of human mitochondria fission protein Fis1 reveals a novel TPR-like helix bundle. <i> Suzuki M, Jeong SY, Karbowski M, Youle RJ, Tjandra N. </i> J Mol Biol, 2003","term_id":"GO:0008289","curator_id":"eschad","start":121,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"14623186","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00457r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q9Y3D6","date":"2016-09-09T11:51:26.000Z","acc":"Q9Y3D6","name":"Mitochondrial fission 1 protein","length":152,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000073ACD","genes":[{"name":{"value":"FIS1"},"synonyms":[{"value":"TTC11"}],"orfNames":[{"value":"CGI-135"}]}],"alphafold_very_low_content":0.11842105263157894,"disorder_content":0.16447368421052633,"disprot_consensus":{"full":[{"start":121,"end":145,"type":"D"}],"Structural state":[{"start":121,"end":145,"type":"D"}],"Molecular function":[{"start":121,"end":145,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00996","name":"GDP dissociation inhibitor","start":8,"end":75},{"id":"PF22603","name":"RAE1/2 domain I, C-terminal region","start":449,"end":577}],"gene3D":[{"start":182,"end":601,"id":"3.50.50.60","name":"FAD/NAD(P)-binding domain"},{"start":1,"end":98,"id":"3.50.50.60","name":"FAD/NAD(P)-binding domain"},{"start":195,"end":553,"id":"3.30.519.10","name":"Guanine Nucleotide Dissociation Inhibitor, domain 2"},{"start":271,"end":369,"id":"1.10.405.10","name":"Guanine Nucleotide Dissociation Inhibitor, domain 1"}]},"uniref50":"UniRef50_P37727","sequence":"MADNLPSDFDVIVIGTGLPESIIAAACSRSGQRVLHVDSRSYYGGNWASFSFSGLLSWLKEYQENNDVVTENSMWQEQILENEEAIPLSSKDKTIQHVEVFCYASQDLHKDVEEAGALQKNHASVTSAQSAEAAEAAETSCLPTAVEPLSMGSCEIPAEQSQCPGPESSPEVNDAEATGKKENSDAKSSTEEPSENVPKVQDNTETPKKNRITYSQIIKEGRRFNIDLVSQLLYSRGLLIDLLIKSNVSRYAEFKNITRILAFREGTVEQVPCSRADVFNSKQLTMVEKRMLMKFLTFCVEYEEHPDEYRAYEGTTFSEYLKTQKLTPNLQYFVLHSIAMTSETTSCTVDGLKATKKFLQCLGRYGNTPFLFPLYGQGELPQCFCRMCAVFGGIYCLRHSVQCLVVDKESRKCKAVIDQFGQRIISKHFIIEDSYLSENTCSRVQYRQISRAVLITDGSVLKTDADQQVSILAVPAEEPGSFGVRVIELCSSTMTCMKGTYLVHLTCMSSKTAREDLERVVQKLFTPYTEIEAENEQVEKPRLLWALYFNMRDSSDISRDCYNDLPSNVYVCSGPDSGLGNDNAVKQAETLFQQICPNEDFCPAPPNPEDIVLDGDSSQQEVPESSVTPETNSETPKESTVLGNPEEPSE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_P37727","disprot_id":"DP00458","ncbi_taxon_id":10116,"regions_counter":4,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":208,"region_id":"DP00458r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase. <i> Pylypenko O, Rak A, Reents R, Niculae A, Sidorovitch V, Cioaca MD, Bessolitsyna E, Thomä NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K. </i> Mol Cell, 2003","term_id":"IDPO:0000002","curator_id":"fquaglia","start":108,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12620235","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1LTX"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":650,"region_id":"DP00458r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase. <i> Pylypenko O, Rak A, Reents R, Niculae A, Sidorovitch V, Cioaca MD, Bessolitsyna E, Thomä NH, Waldmann H, Schlichting I, Goody RS, Alexandrov K. </i> Mol Cell, 2003","term_id":"IDPO:0000002","curator_id":"fquaglia","start":615,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12620235","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1LTX"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P37727","date":"2016-08-30T13:59:43.000Z","acc":"P37727","name":"Rab proteins geranylgeranyltransferase component A 1","length":650,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI00001330D3","genes":[{"name":{"value":"Chm"},"synonyms":[{"value":"Rep1"}]}],"alphafold_very_low_content":0.19538461538461538,"disorder_content":0.21076923076923076,"disprot_consensus":{"full":[{"start":108,"end":208,"type":"D"},{"start":615,"end":650,"type":"D"}],"Structural state":[{"start":108,"end":208,"type":"D"},{"start":615,"end":650,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01024","name":"Colicin pore forming domain","start":187,"end":361}],"gene3D":[{"start":188,"end":387,"id":"1.10.490.30","name":"Colicin"},{"start":91,"end":187,"id":"3.30.1120.60","name":"Colicin"}]},"uniref50":"UniRef50_P08083","sequence":"MGSNGADNAHNNAFGGGKNPGIGNTSGAGSNGSASSNRGNSNGWSWSNKPHKNDGFHSDGSYHITFHGDNNSKPKPGGNSGNRGNNGDGASAKVGEITITPDNSKPGRYISSNPEYSLLAKLIDAESIKGTEVYTFHTRKGQYVKVTVPDSNIDKMRVDYVNWKGPKYNNKLVKRFVSQFLLFRKEEKEKNEKEALLKASELVSGMGDKLGEYLGVKYKNVAKEVANDIKNFHGRNIRSYNEAMASLNKVLANPKMKVNKSDKDAIVNAWKQVNAKDMANKIGNLGKAFKVADLAIKVEKIREKSIEGYNTGNWGPLLLEVESWIIGGVVAGVAISLFGAVLSFLPISGLAVTALGVIGIMTISYLSSFIDANRVSNINNIISSVIR","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P08083","disprot_id":"DP00461","dataset":["Unicellular toxins and antitoxins"],"ncbi_taxon_id":562,"regions_counter":32,"creator":"mnecci","regions":[{"region_id":"DP00461r001","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:16:07.656Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":90,"term_id":"IDPO:0000002","start":67,"version":4,"statement":[{"text":"Here, we present the crystal structure, at 3.1 å resolution, of a large fragment of colicin N (missing the first 66 residues) that contains the pore-forming and the receptor-binding domains.","type":"Introduction"},{"text":"The translocation domain, located between residues 17 and 66 [44], has a glycine/proline/serine/asparagine-rich sequence, which is likely to have poorly defined secondary structure. The translocation domain is absent in the 3.1 å resolution structure, but the majority of it is present in the initial crystal form (see the Materials and methods section), which comprises residues 37–387.","type":"Results"},{"text":"There is no evidence of any density for the translocation domain; this is in complete accord with circular dichroism and fluorescence results, which demonstrate that this domain does not adopt any regular secondary structure.","type":"Results"},{"text":"The residue boundaries differ from the ones reported by the authors, because they did not use the UniProt sequence (the latter contains a signal peptide).","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"9687368","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1A87"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"rpancsa","reference_html":"Crystal structure of a colicin N fragment suggests a model for toxicity. <i> Vetter IR, Parker MW, Tucker AD, Lakey JH, Pattus F, Tsernoglou D. </i> Structure, 1998","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","version":3,"ec_ontology":"ECO","end":90,"term_name":"disorder to order","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0001-7496-6711","curator_id":"tlazar","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"15004032","statement":[{"text":"By expressing the far-UV CD spectra in units of dE where concentration is in moles of protein/liter rather than the more conventional moles of residues/liter we can generate the expected spectrum of a 1:1 mixture of TolA-(296 – 421) and T-domain (Fig. 1B). This can be compared with the measured far-UV CD spectrum of the 1:1 complex. The spectra are different, indicating that changes in secondary structure occur upon binding. The difference between TolA-(296 – 421) and the complex is also shown (Fig. 1A). This may correspond to the new structure of the T-domain with a reduction in the unstructured component and its replacement by a secondary structure signal (210–225 nm).","type":"Results"},{"text":"The CD data suggest large scale changes in the secondary structure of the T-domain during TolA binding. The measured spectrum of the complex differs significantly from the summed spectra of the two individual components, and subtraction of the TolA-(296 – 421) spectrum from the complex reveals a “T- domain like” signal, which, however, contains less random and more secondary structure.","type":"Discussion"}],"reference_html":"A natively unfolded toxin domain uses its receptor as a folding template. <i> Anderluh G, Gökçe I, Lakey JH. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T18:50:47.877Z","curator_name":"Bálint Mészáros"},"region_id":"DP00461r004","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00461r011","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T17:05:37.100Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":90,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":2,"version":3,"statement":[{"text":"The 1H– 15N HSQC spectrum of N-labelled intact colicin N confirms that the protein contains a largely unstructured and flexible region (Fig. 1), as indicated by the numerous sharp amide NH resonances with a narrow 1H chemical shift dispersion, between 7.5 and 9 ppm, seen in the spectrum at a high threshold where broad peaks from the folded domains are not visible (Fig. 1). Sequential assignment of these resonances revealed that they belong to the 90 residue T-domain.","type":"Results"},{"text":"resonances for T-domain 2–90 are sharp signals with a relatively narrow 1H chemical shift dispersion as expected for a disordered protein","type":"Results"}],"term_name":"disorder","reference_html":"Self-recognition by an intrinsically disordered protein. <i> Hecht O, Ridley H, Boetzel R, Lewin A, Cull N, Chalton DA, Lakey JH, Moore GR. </i> FEBS Lett, 2008","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"18573254","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"15506"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"tlazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00461r012","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T11:09:01.790Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":90,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":2,"version":4,"statement":[{"text":"All of the 85 expected backbone NH resonances of T-domain 2–90 could be assigned unambiguously (Fig. 3) consistent with an intra-molecular interaction of the T-domain of intact colicin N with one of its folded domains.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P08083","partner_end":null}],"term_name":"protein binding","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"18573254","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"tlazar","reference_html":"Self-recognition by an intrinsically disordered protein. <i> Hecht O, Ridley H, Boetzel R, Lewin A, Cull N, Chalton DA, Lakey JH, Moore GR. </i> FEBS Lett, 2008","term_id":"GO:0005515","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":90,"region_id":"DP00461r013","reference_html":"Discovery of critical Tol A-binding residues in the bactericidal toxin colicin N: a biophysical approach. <i> Raggett EM, Bainbridge G, Evans LJ, Cooper A, Lakey JH. </i> Mol Microbiol, 1998","ec_id":"ECO:0006204","version":3,"term_id":"IDPO:0000002","curator_id":"tlazar","start":1,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"The isolated colicin N N-terminal domain appears to be unstructured in circular dichroism ","type":"Abstract"},{"text":"The isolated T-domain is unstructured. The circular dichroism (CD) spectrum of the isolated T- domain shows a random coil conformation, although the negative signal between 210 and 240nm may indicate some ordered secondary structure","type":"Results"}],"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T17:57:58.526Z","curator_name":"Bálint Mészáros"},"released":"2022_03","reference_id":"9680221","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00461r015","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T17:58:38.058Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":90,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"The isolated colicin N N-terminal domain appears to be unstructured in circular dichroism and fluorescence studies.","type":"Abstract"},{"text":"Consistent with the random coil CD data, the two tryptophans of the isolated T-domain are exposed to the aqueous phase","type":"Results"},{"text":"The aqueous exposure of the tryptophans is further evidence of the unfolded state of the isolated T-domain","type":"Discussion"}],"term_name":"disorder","ec_name":"fluorescence evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"9680221","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0001249","curator_id":"tlazar","reference_html":"Discovery of critical Tol A-binding residues in the bactericidal toxin colicin N: a biophysical approach. <i> Raggett EM, Bainbridge G, Evans LJ, Cooper A, Lakey JH. </i> Mol Microbiol, 1998","ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP00461r016","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T17:59:07.446Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":90,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"We have measured the binding of colicin N to TolA by isothermal titration microcalorimetry (ITC)","type":"Abstract"},{"text":"The isolated N-terminal domain exhibits a higher affinity for TolA (Kd = 1 uM) than does the whole colicin (18 uM)","type":"Abstract"},{"text":"\nIsolated T-domain has a higher TolA binding affinity than colicin N","type":"Results"},{"text":"the isolated T-domain shows more than a 10-fold increase in affinity in ITC experiments","type":"Results"},{"text":"The isolated T-domain has a dissociation constant of 1uM for TolA","type":"Discussion"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P19934","partner_end":null}],"term_name":"protein binding","ec_name":"isothermal titration calorimetry evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"9680221","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"tlazar","reference_html":"Discovery of critical Tol A-binding residues in the bactericidal toxin colicin N: a biophysical approach. <i> Raggett EM, Bainbridge G, Evans LJ, Cooper A, Lakey JH. </i> Mol Microbiol, 1998","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00461r017","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T17:59:24.492Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":90,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"We have measured the binding of colicin N to TolA by isothermal titration microcalorimetry (ITC) and tryptophan fluorescence","type":"Abstract"},{"text":"On complex formation with TolA, the tryptophans of the T-domain become buried with a Stern–Volmer constant of 0.8 M-1.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P19934","partner_end":null}],"term_name":"protein binding","ec_name":"dynamic fluorescence quenching evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"9680221","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006327","curator_id":"tlazar","reference_html":"Discovery of critical Tol A-binding residues in the bactericidal toxin colicin N: a biophysical approach. <i> Raggett EM, Bainbridge G, Evans LJ, Cooper A, Lakey JH. </i> Mol Microbiol, 1998","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00461r018","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T11:10:07.380Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":76,"term_id":"IDPO:0000004","start":40,"version":2,"statement":[{"text":"T-domain does not exist as an extended strand in solution, but rather adopts a compact average conformation without forming long stretches of secondary structure.\nThe initial 1H-15N HSQC spectrum of the T-domain 40–76 peptide in solution showed at least 35 peaks, excluding side chain signals, suggesting that all the backbone NH resonances were detected between 7.7 and 8.7 ppm (1H). NOESY data collected on the peptide showed very few cross-peaks, presumably owing to its flexibility. The 1H-15N HSQC peaks of the T-domain 40–76 are clearly not clustered in the narrow region (~0.45 ppm 1H) to be expected for a random coil, but are more dispersed, covering a range of 1 ppm (1H), which indicates that the peptide has at least some regions of non-random structure. However, if the peptide were rigidly structured the NOESY spectrum would be expected to show considerably more cross-peaks than were observed.","type":"Results"}],"term_name":"pre-molten globule","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"12679333","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"tlazar","reference_html":"Concerted folding and binding of a flexible colicin domain to its periplasmic receptor TolA. <i> Anderluh G, Hong Q, Boetzel R, MacDonald C, Moore GR, Virden R, Lakey JH. </i> J Biol Chem, 2003","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00461r019","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T18:19:17.419Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":90,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"The binding to TolA-II,III was measured by tryptophan fluorescence and SPR (Fig. 2 and Table I). S58C, S61C, N70C, and N71C exhibit binding comparable to the wild-type T-domain.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P19934","partner_end":null}],"term_name":"protein binding","ec_name":"fluorescence evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"12679333","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001249","curator_id":"tlazar","reference_html":"Concerted folding and binding of a flexible colicin domain to its periplasmic receptor TolA. <i> Anderluh G, Hong Q, Boetzel R, MacDonald C, Moore GR, Virden R, Lakey JH. </i> J Biol Chem, 2003","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00461r020","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T18:16:55.799Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":90,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"The binding to TolA-II,III was measured by tryptophan fluorescence and SPR (Fig. 2 and Table I). S58C, S61C, N70C, and N71C exhibit binding comparable to the wild-type T-domain.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P19934","partner_end":null}],"term_name":"protein binding","ec_name":"surface plasmon resonance evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"12679333","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001269","curator_id":"tlazar","reference_html":"Concerted folding and binding of a flexible colicin domain to its periplasmic receptor TolA. <i> Anderluh G, Hong Q, Boetzel R, MacDonald C, Moore GR, Virden R, Lakey JH. </i> J Biol Chem, 2003","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00461r021","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T18:20:05.138Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":90,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"For labeled sample k-1 was five times higher (0.051 +/- 0.037 s-1) than for the unlabeled one (0.011 +/- 0.012 s-1). This gives Kd values of 0.5 uM for N71C and 0.1 uM for N71C-AEDANS. The k1 values are similar to those obtained by the 90-residue wild-type T-domain (1.6 * 10^5 M-1 s-1) in the same system (13), while the k-1 value for the wild-type was higher (0.37 s-1).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P19934","partner_end":null}],"term_name":"protein binding","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"12679333","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001183","curator_id":"tlazar","reference_html":"Concerted folding and binding of a flexible colicin domain to its periplasmic receptor TolA. <i> Anderluh G, Hong Q, Boetzel R, MacDonald C, Moore GR, Virden R, Lakey JH. </i> J Biol Chem, 2003","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00461r022","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T18:51:55.329Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":90,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"Fluorescence and surface plasmon resonance confirm that the new unfolding transition accompanies dissociation of ColN-(1–90). Hence upon binding the disordered structure of ColN-(1–90) converts to a cooperatively folded domain without altering the TolA-(296–421) structure.","type":"Abstract"},{"text":"The binding of full-length (ColN-(1–90)) T-domain to these TolA variants was measured using fluorescence spectroscopy and gel filtration chromatography. The T-domain contains two tryptophans that become buried upon TolA binding causing both an increase and a blue shift of their fluorescence emission (32–34). Both TolA variants with natural C termini bound to T-domain with similar affinity.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P19934","partner_end":null}],"term_name":"protein binding","ec_name":"fluorescence evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"15004032","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001249","curator_id":"tlazar","reference_html":"A natively unfolded toxin domain uses its receptor as a folding template. <i> Anderluh G, Gökçe I, Lakey JH. </i> J Biol Chem, 2004","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00461r023","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T18:51:56.872Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":90,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"The binding of full-length (ColN-(1–90)) T-domain to these TolA variants was measured using fluorescence spectroscopy and gel filtration chromatography. The T-domain contains two tryptophans that become buried upon TolA binding causing both an increase and a blue shift of their fluorescence emission (32–34). Both TolA variants with natural C termini bound to T-domain with similar affinity.","type":"Results"},{"text":"A decrease in elution volume (increase in size) was observed when T-domain was mixed with TolA-(296 – 421) and TolA-(329 – 421) but not in the presence of TolAT.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P19934","partner_end":null}],"term_name":"protein binding","ec_name":"chromatography evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"15004032","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0007680","curator_id":"tlazar","reference_html":"A natively unfolded toxin domain uses its receptor as a folding template. <i> Anderluh G, Gökçe I, Lakey JH. </i> J Biol Chem, 2004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00461r024","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T18:50:29.832Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":90,"term_id":"IDPO:0000004","start":1,"version":2,"statement":[{"text":"As expected the T-domain in solution is predicted to have more random structure (H4/S31/T23/R41), but the strand content is significant.","type":"Results"},{"text":"The disordered nature of this domain is revealed by far-UV CD spectra (Fig. 1 and previous work (19, 33, 34)), and we show here that the T-domain also lacks two further features of folded proteins. The first is cooperative folding/unfolding as revealed by heat denaturation. The far-UV CD spectra recorded at increasing temperatures show a gradual almost linear change with temperature consistent with the isolated unfolding of individual structures rather than the sigmoidal unfolding curves found with proteins folded in cooperative domains (Fig. 4). The fact that the T-domain “unfolds” with temperature is supportive of the possibility that it contains some secondary structure (premolten globule) or polyproline II helix (PII), which can at higher temperatures adopt a different conformation (46).","type":"Discussion"}],"term_name":"pre-molten globule","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"15004032","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006204","curator_id":"tlazar","reference_html":"A natively unfolded toxin domain uses its receptor as a folding template. <i> Anderluh G, Gökçe I, Lakey JH. </i> J Biol Chem, 2004","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00461r025","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T18:53:07.419Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":90,"term_id":"IDPO:0000004","start":1,"version":2,"statement":[{"text":"The gel filtration data here further show that the hydrodynamic radius of free T-domain is only slightly larger than a folded protein of this size.","type":"Discussion"}],"term_name":"pre-molten globule","ec_name":"chromatography evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"15004032","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0007680","curator_id":"tlazar","reference_html":"A natively unfolded toxin domain uses its receptor as a folding template. <i> Anderluh G, Gökçe I, Lakey JH. </i> J Biol Chem, 2004","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00461r026","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T18:52:56.590Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":90,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"The near-UV CD spectra of T-domain is virtually featureless and consistent with its mobile and exposed aromatic residues (Fig. 3A)","type":"Results"}],"term_name":"disorder","ec_name":"near-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"15004032","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006206","curator_id":"tlazar","reference_html":"A natively unfolded toxin domain uses its receptor as a folding template. <i> Anderluh G, Gökçe I, Lakey JH. </i> J Biol Chem, 2004","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00461r027","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T18:51:07.327Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":90,"term_id":"IDPO:0000011","start":1,"version":2,"statement":[{"text":"The difference between the predicted and experimental spectra is shown in Fig. 3C (solid line). This reveals an additional positive signal in the spectrum of the complex in the region 270–290 nm with clearly resolved peaks at 272, 279, and 290 nm. The latter is unique to tryptophan and thus can be directly linked to T-domain folding upon binding.","type":"Results"},{"text":"In fact, the near-UV CD spectrum of the complex provides evidence of an additional tryptophan signal that can only come from ordering of the T-domain.","type":"Discussion"}],"term_name":"disorder to order","ec_name":"near-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"15004032","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural transition","ec_id":"ECO:0006206","curator_id":"tlazar","reference_html":"A natively unfolded toxin domain uses its receptor as a folding template. <i> Anderluh G, Gökçe I, Lakey JH. </i> J Biol Chem, 2004","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00461r028","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T11:11:21.997Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":76,"term_id":"GO:0005515","start":40,"version":3,"statement":[{"text":"The peptide was concentrated with a Speed-Vac (Savant, Albertville, MN) and desalted on PD-10 columns (Amersham Biosciences). Its binding to\nTolA-II,III resembled the binding of the full-length T-domain since a Kd of 1.3 uM was obtained by the surface plasmon resonance (SPR) measurement.","type":"Methods"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P19934","partner_end":null}],"term_name":"protein binding","ec_name":"surface plasmon resonance evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"12679333","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001269","curator_id":"tlazar","reference_html":"Concerted folding and binding of a flexible colicin domain to its periplasmic receptor TolA. <i> Anderluh G, Hong Q, Boetzel R, MacDonald C, Moore GR, Virden R, Lakey JH. </i> J Biol Chem, 2003","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00461r029","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T11:11:44.925Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":76,"term_id":"GO:0005515","start":40,"version":3,"statement":[{"text":"The peptide was concentrated with a Speed-Vac (Savant, Albertville, MN) and desalted on PD-10 columns (Amersham Biosciences). Its binding to\nTolA-II,III resembled the binding of the full-length T-domain since a Kd of 1.3 uM was obtained by the surface plasmon resonance (SPR) measurement. In addition, the tryptophan fluorescence spectrum exhibited the same increase and blue-shift upon TolA-II,III binding.","type":"Methods"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P19934","partner_end":null}],"term_name":"protein binding","ec_name":"fluorescence evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"12679333","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001249","curator_id":"tlazar","reference_html":"Concerted folding and binding of a flexible colicin domain to its periplasmic receptor TolA. <i> Anderluh G, Hong Q, Boetzel R, MacDonald C, Moore GR, Virden R, Lakey JH. </i> J Biol Chem, 2003","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00461r030","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T11:10:52.128Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":76,"term_id":"IDPO:0000013","start":40,"version":2,"statement":[{"text":"Adding unlabeled TolA-III to the labeled T-domain peptide immediately caused new peaks to appear with some of the original peaks reducing in intensity. The number and intensity of the new signals continued to increase with further additions of TolA-III and the intensity of the original peaks reducing further.","type":"Results"},{"text":"Thus, the NMR data clearly demonstrate that the colicin N T-domain 40 –76 peptide and TolA-III formed a complex and that the peptide adopts an organized structure in the complex.","type":"Results"}],"term_name":"pre-molten globule to order","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"12679333","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural transition","ec_id":"ECO:0006165","curator_id":"tlazar","reference_html":"Concerted folding and binding of a flexible colicin domain to its periplasmic receptor TolA. <i> Anderluh G, Hong Q, Boetzel R, MacDonald C, Moore GR, Virden R, Lakey JH. </i> J Biol Chem, 2003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00461r031","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T11:10:37.950Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":76,"term_id":"GO:0005515","start":40,"version":3,"statement":[{"text":"Adding unlabeled TolA-III to the labeled T-domain peptide immediately caused new peaks to appear with some of the original peaks reducing in intensity. The number and intensity of the new signals continued to increase with further additions of TolA-III and the intensity of the original peaks reducing further. This trend continued until a 1:2 molar ratio was obtained. Increasing the ratio to 1:4 gave no further changes, indicating that the proteins were already fully bound.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P19934","partner_end":null}],"term_name":"protein binding","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"12679333","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"tlazar","reference_html":"Concerted folding and binding of a flexible colicin domain to its periplasmic receptor TolA. <i> Anderluh G, Hong Q, Boetzel R, MacDonald C, Moore GR, Virden R, Lakey JH. </i> J Biol Chem, 2003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00461r032","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T11:11:48.081Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":90,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"Complex formation was also checked in the temperature range 20–40 °C by SPR (BIACORE) (Fig. 7). TolA-(296–421) was immobilized, and increasing concentra- tions of T-domain were injected over it. The amount of stably bound T-domain at each temperature was determined by allowing the binding to reach equilibrium. The binding decreased with increasing temperature.","type":"Results"},{"text":"Kd values for the binding of TolA constructs to T-domain of colicin N\nThe averages of two to three independent experiments +/- S.D. are presented.","type":"Table"},{"text":"SPR: TolA-(296–421), 20 °C – Kd: 0.35 +/- 0.02 uM; 30 °C – Kd: 2.72 +/- 1.51 uM","type":"Table"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P19934","partner_end":null}],"term_name":"protein binding","ec_name":"surface plasmon resonance evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"15004032","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001269","curator_id":"tlazar","reference_html":"A natively unfolded toxin domain uses its receptor as a folding template. <i> Anderluh G, Gökçe I, Lakey JH. </i> J Biol Chem, 2004","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P08083","date":"2016-09-06T17:15:56.000Z","acc":"P08083","name":"Colicin-N","length":387,"organism":"Escherichia coli","UniParc":"UPI0000127497","genes":[{"name":{"value":"cna"}}],"alphafold_very_low_content":0.22997416020671835,"disorder_content":0.23255813953488372,"disprot_consensus":{"full":[{"start":1,"end":90,"type":"T"}],"Structural state":[{"start":1,"end":90,"type":"D"}],"Structural transition":[{"start":1,"end":90,"type":"T"}],"Molecular function":[{"start":1,"end":90,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00268","name":"Ribonucleotide reductase, small chain","start":80,"end":347}],"gene3D":[{"start":49,"end":372,"id":"1.10.620.20","name":"Ribonucleotide Reductase, subunit A"}]},"uniref50":"UniRef50_P11157","sequence":"MLSVRTPLATIADQQQLQLSPLKRLTLADKENTPPTLSSTRVLASKAARRIFQDSAELESKAPTNPSVEDEPLLRENPRRFVVFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWEALKPDERHFISHVLAFFAASDGIVNENLVERFSQEVQVTEARCFYGFQIAMENIHSEMYSLLIDTYIKDPKEREYLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPAEQRVREIITNAVRIEQEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFNKIFRVENPFDFMENISLEGKTNFFEKRVGEYQRMGVMSNSTENSFTLDADF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P11157","disprot_id":"DP00462","ncbi_taxon_id":10090,"regions_counter":4,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":390,"region_id":"DP00462r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2. <i> Kauppi B, Nielsen BB, Ramaswamy S, Larsen IK, Thelander M, Thelander L, Eklund H. </i> J Mol Biol, 1996","term_id":"IDPO:0000002","curator_id":"fquaglia","start":353,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"8876648","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1XSM"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":390,"term_name":"disorder to order","start":353,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"8876648","version":2,"reference_html":"The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2. <i> Kauppi B, Nielsen BB, Ramaswamy S, Larsen IK, Thelander M, Thelander L, Eklund H. </i> J Mol Biol, 1996","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00462r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":390,"term_name":"protein binding","start":353,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"8876648","version":3,"reference_html":"The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2. <i> Kauppi B, Nielsen BB, Ramaswamy S, Larsen IK, Thelander M, Thelander L, Eklund H. </i> J Mol Biol, 1996","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00462r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":64,"region_id":"DP00462r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2. <i> Kauppi B, Nielsen BB, Ramaswamy S, Larsen IK, Thelander M, Thelander L, Eklund H. </i> J Mol Biol, 1996","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"8876648","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1XSM"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P11157","date":"2016-09-14T12:12:04.000Z","acc":"P11157","name":"Ribonucleoside-diphosphate reductase subunit M2","length":390,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000041BE","genes":[{"name":{"value":"Rrm2"}}],"alphafold_very_low_content":0.20512820512820512,"disorder_content":0.26153846153846155,"disprot_consensus":{"full":[{"start":1,"end":64,"type":"D"},{"start":353,"end":390,"type":"T"}],"Structural state":[{"start":1,"end":64,"type":"D"},{"start":353,"end":390,"type":"D"}],"Structural transition":[{"start":353,"end":390,"type":"T"}],"Molecular function":[{"start":353,"end":390,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00003","name":"7 transmembrane sweet-taste receptor of 3 GCPR","start":587,"end":855},{"id":"PF00084","name":"Sushi repeat (SCR repeat)","start":118,"end":156},{"id":"PF01094","name":"Receptor family ligand binding region","start":187,"end":543}],"gene3D":[{"start":290,"end":559,"id":"3.40.50.2300","name":"3.40.50.2300"},{"start":176,"end":536,"id":"3.40.50.2300","name":"3.40.50.2300"},{"start":92,"end":159,"id":"2.10.70.10","name":"Complement Module, domain 1"}]},"uniref50":"UniRef50_Q9Z0U4","sequence":"MLLLLLVPLFLRPLGAGGAQTPNATSEGCQIIHPPWEGGIRYRGLTRDQVKAINFLPVDYEIEYVCRGEREVVGPKVRKCLANGSWTDMDTPSRCVRICSKSYLTLENGKVFLTGGDLPALDGARVEFRCDPDFHLVGSSRSVCSQGQWSTPKPHCQVNRTPHSERRAVYIGALFPMSGGWPGGQACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAGIEITFRQSFFSDPAVPVKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIGWYADNWFKTYDPSINCTVEEMTEAVEGHITTEIVMLNPANTRSISNMTSQEFVEKLTKRLKRHPEETGGFQEAPLAYDAIWALALALNKTSGGGGRSGVRLEDFNYNNQTITDQIYRAMNSSSFEGVSGHVVFDASGSRMAWTLIEQLQGGSYKKIGYYDSTKDDLSWSKTDKWIGGSPPADQTLVIKTFRFLSQKLFISVSVLSSLGIVLAVVCLSFNIYNSHVRYIQNSQPNLNNLTAVGCSLALAAVFPLGLDGYHIGRSQFPFVCQARLWLLGLGFSLGYGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDVLTLAIWQIVDPLHRTIETFAKEEPKEDIDVSILPQLEHCSSKKMNTWLGIFYGYKGLLLLLGIFLAYETKSVSTEKINDHRAVGMAIYNVAVLCLITAPVTMILSSQQDAAFAFASLAIVFSSYITLVVLFVPKMRRLITRGEWQSETQDTMKTGSSTNNNEEEKSRLLEKENRELEKIIAEKEERVSELRHQLQSRQQLRSRRHPPTPPDPSGGLPRGPSEPPDRLSCDGSRVHLLYK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_Q9Z0U4","disprot_id":"DP00463","ncbi_taxon_id":10116,"regions_counter":17,"creator":"fquaglia","regions":[{"start":17,"end":98,"reference_id":"15304491","reference_source":"pmid","reference_html":"Structural analysis of the complement control protein (CCP) modules of GABA(B) receptor 1a: only one of the two CCP modules is compactly folded. <i> Blein S, Ginham R, Uhrin D, Smith BO, Soares DC, Veltel S, McIlhinney RA, White JH, Barlow PN. </i> J Biol Chem, 2004","date":"2024-03-22T13:21:30.586Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP00463r013","statement":[{"text":"The 1H-15N HSQC spectrum of CCP1 is characterized by a mixture of sharp and broad resonances. Many of these signals have poor 1H dispersion, implying that there is a substantial part of CCP1 that is not compactly structured. On the other hand, the presence of a number of dispersed non-glycine resonances in its 1H-15N HSQC spectrum indicates some structure within CCP1.","type":"Results"},{"text":"Taken together, the biophysical data suggest that CCP1 contains a mixture of ordered and molten globular parts.","type":"Discussion"}]},{"start":17,"end":98,"reference_id":"15304491","reference_source":"pmid","reference_html":"Structural analysis of the complement control protein (CCP) modules of GABA(B) receptor 1a: only one of the two CCP modules is compactly folded. <i> Blein S, Ginham R, Uhrin D, Smith BO, Soares DC, Veltel S, McIlhinney RA, White JH, Barlow PN. </i> J Biol Chem, 2004","date":"2024-03-22T13:22:01.103Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006232","ec_ontology":"ECO","ec_name":"differential scanning calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP00463r014","statement":[{"text":"In contrast, the CCP1 DSC profile (Fig. 4b) has no heat absorption peak over the temperature range employed (22–100 °C), although a weak negative transition can be observed at ∼52 °C prior to a substantial decline in heat capacity above 60 °C.","type":"Results"},{"text":"This result strongly suggests that recombinant CCP1 has little rigid tertiary structure, in contrast to CCP2.","type":"Results"},{"text":"Taken together, the biophysical data suggest that CCP1 contains a mixture of ordered and molten globular parts.","type":"Discussion"}]},{"start":17,"end":98,"reference_id":"15304491","reference_source":"pmid","reference_html":"Structural analysis of the complement control protein (CCP) modules of GABA(B) receptor 1a: only one of the two CCP modules is compactly folded. <i> Blein S, Ginham R, Uhrin D, Smith BO, Soares DC, Veltel S, McIlhinney RA, White JH, Barlow PN. </i> J Biol Chem, 2004","date":"2024-03-22T13:22:17.741Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP00463r015","statement":[{"text":"CCP1 showed a well defined positive ellipticity in the far-UV region centered at 228 nm (Fig. 5a), which was noteworthy in view of the low extent of folding implied by NMR spectroscopy and the lack of thermal stability inferred from the DSC studies.","type":"Results"},{"text":"Taken together, the biophysical data suggest that CCP1 contains a mixture of ordered and molten globular parts.","type":"Discussion"}]},{"start":17,"end":98,"reference_id":"15304491","reference_source":"pmid","reference_html":"Structural analysis of the complement control protein (CCP) modules of GABA(B) receptor 1a: only one of the two CCP modules is compactly folded. <i> Blein S, Ginham R, Uhrin D, Smith BO, Soares DC, Veltel S, McIlhinney RA, White JH, Barlow PN. </i> J Biol Chem, 2004","date":"2024-03-22T13:21:16.321Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005632","ec_ontology":"ECO","ec_name":"fluorescence anisotropy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP00463r016","statement":[{"text":"By contrast, ANS bound strongly to CCP1 (Fig. 6b). This is evidence of the presence of a substantial number of solvent-accessible non-polar groups in CCP1 and implies strongly that CCP1 is not compactly folded.","type":"Results"},{"text":"Taken together, the biophysical data suggest that CCP1 contains a mixture of ordered and molten globular parts.","type":"Discussion"}]},{"start":17,"end":98,"reference_id":"15304491","reference_source":"pmid","reference_html":"Structural analysis of the complement control protein (CCP) modules of GABA(B) receptor 1a: only one of the two CCP modules is compactly folded. <i> Blein S, Ginham R, Uhrin D, Smith BO, Soares DC, Veltel S, McIlhinney RA, White JH, Barlow PN. </i> J Biol Chem, 2004","date":"2024-03-22T13:28:58.934Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"A0A8I6A720","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00463r017","statement":[{"text":"As shown in Fig. 2d (lower panel), CCP1 (but not CCP2) pulled down full-length fibulin-2.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_Q9Z0U4","date":"2016-08-25T16:09:47.000Z","acc":"Q9Z0U4","name":"Gamma-aminobutyric acid type B receptor subunit 1","length":960,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI000012B267","genes":[{"name":{"value":"Gabbr1"}}],"alphafold_very_low_content":0.11907164480322906,"disorder_content":0.08541666666666667,"disprot_consensus":{"full":[{"start":17,"end":98,"type":"D"}],"Structural state":[{"start":17,"end":98,"type":"D"}],"Molecular function":[{"start":17,"end":98,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03165","name":"MH1 domain","start":37,"end":137},{"id":"PF03166","name":"MH2 domain","start":321,"end":530}],"gene3D":[{"start":314,"end":549,"id":"2.60.200.10","name":"2.60.200.10"},{"start":9,"end":140,"id":"3.90.520.10","name":"SMAD MH1 domain"}]},"uniref50":"UniRef50_Q13485","sequence":"MDNMSITNTPTSNDACLSIVHSLMCHRQGGESETFAKRAIESLVKKLKEKKDELDSLITAITTNGAHPSKCVTIQRTLDGRLQVAGRKGFPHVIYARLWRWPDLHKNELKHVKYCQYAFDLKCDSVCVNPYHYERVVSPGIDLSGLTLQSNAPSSMMVKDEYVHDFEGQPSLSTEGHSIQTIQHPPSNRASTETYSTPALLAPSESNATSTANFPNIPVASTSQPASILGGSHSEGLLQIASGPQPGQQQNGFTGQPATYHHNSTTTWTGSRTAPYTPNLPHHQNGHLQHHPPMPPHPGHYWPVHNELAFQPPISNHPAPEYWCSIAYFEMDVQVGETFKVPSSCPIVTVDGYVDPSGGDRFCLGQLSNVHRTEAIERARLHIGKGVQLECKGEGDVWVRCLSDHAVFVQSYYLDREAGRAPGDAVHKIYPSAYIKVFDLRQCHRQMQQQAATAQAAAAAQAAAVAGNIPGPGSVGGIAPAISLSAAAGIGVDDLRRLCILRMSFVKGWGPDYPRQSIKETPCWIEIHLHRALQLLDEVLHTMPIADPQPLD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q13485","disprot_id":"DP00464","ncbi_taxon_id":9606,"regions_counter":9,"creator":"maspromonte","regions":[{"term_namespace":"Structural transition","ec_ontology":"ECO","end":284,"term_name":"order to disorder","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of a transcriptionally active Smad4 fragment. <i> Qin B, Lam SS, Lin K. </i> Structure, 1999","term_id":"IDPO:0000014","curator_id":"maspromonte","start":273,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","reference_id":"10647180","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00464r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":284,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of a transcriptionally active Smad4 fragment. <i> Qin B, Lam SS, Lin K. </i> Structure, 1999","term_id":"GO:0005515","curator_id":"maspromonte","start":273,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"10647180","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00464r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":306,"term_name":"order to disorder","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of a transcriptionally active Smad4 fragment. <i> Qin B, Lam SS, Lin K. </i> Structure, 1999","term_id":"IDPO:0000014","curator_id":"maspromonte","start":297,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","reference_id":"10647180","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00464r005","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":306,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of a transcriptionally active Smad4 fragment. <i> Qin B, Lam SS, Lin K. </i> Structure, 1999","term_id":"GO:0005515","curator_id":"maspromonte","start":297,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"10647180","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00464r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q13485","date":"2016-09-05T23:45:49.000Z","acc":"Q13485","name":"Mothers against decapentaplegic homolog 4","length":552,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI0000053431","genes":[{"name":{"value":"SMAD4"},"synonyms":[{"value":"DPC4"},{"value":"MADH4"}]}],"alphafold_very_low_content":0.33152173913043476,"disorder_content":0,"disprot_consensus":{"full":[{"start":273,"end":284,"type":"T"},{"start":297,"end":306,"type":"T"}],"Structural state":[],"Structural transition":[{"start":273,"end":284,"type":"T"},{"start":297,"end":306,"type":"T"}],"Molecular function":[{"start":273,"end":284,"type":"F"},{"start":297,"end":306,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00377","name":"Prion/Doppel alpha-helical domain","start":134,"end":251},{"id":"PF03991","name":"Copper binding octapeptide repeat region","start":50,"end":95},{"id":"PF11587","name":"Major prion protein bPrPp - N terminal","start":1,"end":28}],"gene3D":[{"start":90,"end":231,"id":"1.10.790.10","name":"Prion/Doppel protein, beta-ribbon domain"}]},"uniref50":"UniRef50_P04156","sequence":"MANLGCWMLVLFVATWSDLGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGSSMVLFSSPPVILLISFLIFLIVG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P04156","disprot_id":"DP00466","ncbi_taxon_id":9606,"regions_counter":12,"creator":"ldobson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":124,"region_id":"DP00466r003","released":"2023_12","ec_id":"ECO:0006165","reference_html":"NMR solution structure of the human prion protein. <i> Zahn R, Liu A, Lührs T, Riek R, von Schroetter C, López García F, Billeter M, Calzolai L, Wider G, Wüthrich K. </i> Proc Natl Acad Sci U S A, 2000","term_id":"IDPO:0000002","curator_id":"vnugnes","start":23,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10618385","version":4,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-10-19T15:44:44.616Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","cross_refs":[{"db":"PDB","id":"1QLX"},{"db":"PDB","id":"1QLZ"}],"statement":[{"text":"The NMR structure of the intact recombinant human prion protein, hPrP(23–230), contains a globular domain that extends approximately from residues 125–228, a flexibly extended N-terminal tail of residues 23–124, and a short flexible chain end of residues 229–230 ​(Fig. 1a), which is similar to the previously described structure of mPrP(23–231) (14, 15) and the characterization of shPrP(29–231) (16). These global features are qualitatively manifested in the small dispersion of the 1H chemical shifts and negative values of the 15N{1H}-NOEs for the residues 23–124, as described in detail for mPrP(23–231) (14), which contrasts with the fact that the corresponding parameters for the residues 125–228 have typical values for a globular protein of the size of hPrP(23–230).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"GSKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGS"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":124,"term_name":"flexible N-terminal tail","start":23,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10618385","version":4,"reference_html":"NMR solution structure of the human prion protein. <i> Zahn R, Liu A, Lührs T, Riek R, von Schroetter C, López García F, Billeter M, Calzolai L, Wider G, Wüthrich K. </i> Proc Natl Acad Sci U S A, 2000","date":"2023-10-19T15:54:45.063Z","term_id":"IDPO:0000032","ec_id":"ECO:0006165","region_id":"DP00466r004","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Disorder function","cross_refs":[{"db":"PDB","id":"1QLZ"},{"db":"PDB","id":"1QLX"}],"sequence_construct":"GSKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGS","statement":[{"text":"The NMR structure of the intact recombinant human prion protein, hPrP(23–230), contains a globular domain that extends approximately from residues 125–228, a flexibly extended N-terminal tail of residues 23–124, and a short flexible chain end of residues 229–230 ​(Fig. 1a), which is similar to the previously described structure of mPrP(23–231) (14, 15) and the characterization of shPrP(29–231) (16). These global features are qualitatively manifested in the small dispersion of the 1H chemical shifts and negative values of the 15N{1H}-NOEs for the residues 23–124, as described in detail for mPrP(23–231) (14), which contrasts with the fact that the corresponding parameters for the residues 125–228 have typical values for a globular protein of the size of hPrP(23–230).","type":"Results"},{"text":"The region 1-22 corresponds to a signal peptide, absent in the mature form of the protein. Therefore this region corresponds to the N-terminal flexible tail of the mature protein. ","type":"Curator statement"}]},{"start":23,"end":124,"reference_id":"30401430","reference_source":"pmid","reference_html":"Liquid and Hydrogel Phases of PrP<sup>C</sup> Linked to Conformation Shifts and Triggered by Alzheimer's Amyloid-β Oligomers. <i> Kostylev MA, Tuttle MD, Lee S, Klein LE, Takahashi H, Cox TO, Gunther EC, Zilm KW, Strittmatter SM. </i> Mol Cell, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00466r006","statement":[{"text":"Upon Aβo binding and hydrogel formation (Fig. 4B, 4D, 4F), both Gly and Ala spectral regions shift from random coil to α-helical secondary chemical shifts. For Ala, the Cα-Cβ peaks (Fig. 4E, 4F) shift entirely from random coil to α-helical, indicating that a domain including AA113–120 forms an α-helix upon Aßo binding. A similar shift is observed for most Gly resonances. This implies that the octapeptide-repeat region adopts a helical conformation upon Aßo binding.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-08T13:24:05.252Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":23,"end":124,"reference_id":"30401430","reference_source":"pmid","reference_html":"Liquid and Hydrogel Phases of PrP<sup>C</sup> Linked to Conformation Shifts and Triggered by Alzheimer's Amyloid-β Oligomers. <i> Kostylev MA, Tuttle MD, Lee S, Klein LE, Takahashi H, Cox TO, Gunther EC, Zilm KW, Strittmatter SM. </i> Mol Cell, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006067","ec_ontology":"ECO","ec_name":"fluorescence recovery after photobleaching evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00466r007","statement":[{"text":"FRAP demonstrated rapid recovery of PrP-Alexa568 fluorescence due to facile translational diffusion of PrPC (Fig. 1E).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-08T13:29:38.814Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":23,"end":124,"reference_id":"30401430","reference_source":"pmid","reference_html":"Liquid and Hydrogel Phases of PrP<sup>C</sup> Linked to Conformation Shifts and Triggered by Alzheimer's Amyloid-β Oligomers. <i> Kostylev MA, Tuttle MD, Lee S, Klein LE, Takahashi H, Cox TO, Gunther EC, Zilm KW, Strittmatter SM. </i> Mol Cell, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005589","ec_ontology":"ECO","ec_name":"confocal microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00466r008","statement":[{"text":"Time lapse imaging reveals that as PrPC droplets settle, they spread and relax within seconds, accumulating as flat pools. The PrPC layer grows thicker as PrPC droplets settle (Fig. 1F, Fig. S1E, Movie M1). ","type":"Results"},{"text":"Confocal imaging of PrPC liquid droplet spreading on surface. ","type":"Figure"},{"text":"PrPC droplets are dense, settling to form a viscous PrPC liquid layer (Fig. 1B–D). ","type":"Results"},{"text":"3D reconstructions of confocal imaging of LLPS in solutions of increasing PrPC 1 h after PBS addition (120*120*50 µm, x*y*z). Liquid layer thickness is proportional to the pre-LLPS PrPC levle allowing estimation of liquid concentration at 20 mM PrPC.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-08T13:28:58.182Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":23,"end":124,"reference_id":"30401430","reference_source":"pmid","reference_html":"Liquid and Hydrogel Phases of PrP<sup>C</sup> Linked to Conformation Shifts and Triggered by Alzheimer's Amyloid-β Oligomers. <i> Kostylev MA, Tuttle MD, Lee S, Klein LE, Takahashi H, Cox TO, Gunther EC, Zilm KW, Strittmatter SM. </i> Mol Cell, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00466r009","statement":[{"text":"Microscopy of opaque PrPC suspensions by DIC and fluorescence of Alexa 568-tagged PrPC reveals phase transition with demixed spherical droplets (Fig. 1A, Fig. S1A), which dissolve upon dilution.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-08T13:28:52.320Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":23,"end":124,"reference_id":"30401430","reference_source":"pmid","reference_html":"Liquid and Hydrogel Phases of PrP<sup>C</sup> Linked to Conformation Shifts and Triggered by Alzheimer's Amyloid-β Oligomers. <i> Kostylev MA, Tuttle MD, Lee S, Klein LE, Takahashi H, Cox TO, Gunther EC, Zilm KW, Strittmatter SM. </i> Mol Cell, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007056","ec_ontology":"ECO","ec_name":"differential interference contrast microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00466r010","statement":[{"text":"Microscopy of opaque PrPC suspensions by DIC and fluorescence of Alexa 568-tagged PrPC reveals phase transition with demixed spherical droplets (Fig. 1A, Fig. S1A), which dissolve upon dilution.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-08T13:28:41.766Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":23,"end":124,"reference_id":"30401430","reference_source":"pmid","reference_html":"Liquid and Hydrogel Phases of PrP<sup>C</sup> Linked to Conformation Shifts and Triggered by Alzheimer's Amyloid-β Oligomers. <i> Kostylev MA, Tuttle MD, Lee S, Klein LE, Takahashi H, Cox TO, Gunther EC, Zilm KW, Strittmatter SM. </i> Mol Cell, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006067","ec_ontology":"ECO","ec_name":"fluorescence recovery after photobleaching evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00466r011","statement":[{"text":"The mobility of PrPC and mGluR5 were studied by FRAP of CLIP-Surface 547-PrP and SNAP-Alexa 647-mGluR5. Following Aβo, there is parallel reduction of PrPC and mGluR5 mobility (Fig. 5A). Both PrPC and Aβo are necessary to slow mGluR5 mobility, as Aβo-treated cells expressing SNAP-mGluR5 alone or vehicle-treated cells expressing both SNAP-mGluR5 and CLIP-PrP do not repond (Fig. 5B, Fig. S5A). Moreover, mGluR5 recruitment is specific, since Aβo-treatment of cells co-expressing CLIP-PrP and GPI-anchored SNAP tag has no effect on SNAP-GPI mobility (Fig. 5C, 5D, Fig. S5B).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-08T13:28:31.184Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":23,"end":124,"reference_id":"30401430","reference_source":"pmid","reference_html":"Liquid and Hydrogel Phases of PrP<sup>C</sup> Linked to Conformation Shifts and Triggered by Alzheimer's Amyloid-β Oligomers. <i> Kostylev MA, Tuttle MD, Lee S, Klein LE, Takahashi H, Cox TO, Gunther EC, Zilm KW, Strittmatter SM. </i> Mol Cell, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00466r012","statement":[{"text":"In parallel, we sought biochemical evidence for mGluR5 recruitment to Aβo/PrP hydrogels by a centrifugation-based condensation assay. To facilitate mGluR5 expression, we utilized a truncated form (mGluR5-∆ICD). We detected the assembly of Aβo/PrP hydrogels as a shift of PrPC and Aβo from supernatants into pellets (Fig. 5E, 5F). A substantial fraction of mGluR5-∆ICD segregates to hydrogel pellets together with PrPC and Aβo. Neither Aβo nor PrPC alone cause a shift for mGluR5. Moreover, the amount of mGluR5 in the hydrogel decreases with Aβo excess. ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-08T13:27:17.269Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P04156","date":"2016-09-06T18:10:43.000Z","acc":"P04156","name":"Major prion protein","length":253,"organism":"Homo sapiens","dataset":["Condensates-related proteins","Age-related disorders proteins"],"UniParc":"UPI0000033C27","genes":[{"name":{"value":"PRNP"},"synonyms":[{"value":"ALTPRP"},{"value":"PRIP"},{"value":"PRP"}]}],"alphafold_very_low_content":0.391304347826087,"disorder_content":0.4031620553359684,"disprot_consensus":{"full":[{"start":23,"end":124,"type":"T"}],"Structural state":[{"start":23,"end":124,"type":"D"}],"Disorder function":[{"start":23,"end":124,"type":"F"}],"Structural transition":[{"start":23,"end":124,"type":"T"}],"Molecular function":[{"start":23,"end":124,"type":"F"}]}},{"features":{"pfam":[{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":102,"end":164},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":180,"end":245}],"gene3D":[{"start":67,"end":302,"id":"1.25.40.20","name":"Ankyrin repeat-containing domain"}]},"uniref50":"UniRef50_P25963","sequence":"MFQAAERPQEWAMEGPRDGLKKERLLDDRHDSGLDSMKDEEYEQMVKELQEIRLEPQEVPRGSEPWKQQLTEDGDSFLHLAIIHEEKALTMEVIRQVKGDLAFLNFQNNLQQTPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQGCLASVGVLTQSCTTPHLHSILKATNYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEPCNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSPYQLTWGRPSTRIQQQLGQLTLENLQMLPESEDEESYDTESEFTEFTEDELPYDDCVFGGQRLTL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P25963","disprot_id":"DP00468","ncbi_taxon_id":9606,"regions_counter":2,"creator":"gparra","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":66,"region_id":"DP00468r001","released":"2022_03","ec_id":"ECO:0006198","reference_html":"Random coil conformation of a Gly/Ala-rich insert in IkappaB alpha excludes structural stabilization as the mechanism for protection against proteasomal degradation. <i> Leonchiks A, Liepinsh E, Barishev M, Sharipo A, Masucci MG, Otting G. </i> FEBS Lett, 1998","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9872404","version":2,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":317,"region_id":"DP00468r002","released":"2022_03","ec_id":"ECO:0006198","reference_html":"Random coil conformation of a Gly/Ala-rich insert in IkappaB alpha excludes structural stabilization as the mechanism for protection against proteasomal degradation. <i> Leonchiks A, Liepinsh E, Barishev M, Sharipo A, Masucci MG, Otting G. </i> FEBS Lett, 1998","term_id":"IDPO:0000002","curator_id":"fquaglia","start":276,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9872404","version":2,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P25963","date":"2016-08-25T16:25:40.000Z","acc":"P25963","name":"NF-kappa-B inhibitor alpha","length":317,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000004F0A9","genes":[{"name":{"value":"NFKBIA"},"synonyms":[{"value":"IKBA"},{"value":"MAD3"},{"value":"NFKBI"}]}],"alphafold_very_low_content":0.138801261829653,"disorder_content":0.34069400630914826,"disprot_consensus":{"full":[{"start":1,"end":66,"type":"D"},{"start":276,"end":317,"type":"D"}],"Structural state":[{"start":1,"end":66,"type":"D"},{"start":276,"end":317,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00170","name":"bZIP transcription factor","start":86,"end":147}],"gene3D":[{"start":109,"end":150,"id":"1.20.5.490","name":"Single helix bin"}]},"uniref50":"UniRef50_O24646","sequence":"MQEQATSSLAASSLPSSSERSSSSAPHLEIKEGIESDEEIRRVPEFGGEAVGKETSGRESGSATGQERTQATVGESQRKRGRTPAEKENKRLKRLLRNRVSAQQARERKKAYLSELENRVKDLENKNSELEERLSTLQNENQMLRHILKNTTGNKRGGGGGSNADASL","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_O24646","disprot_id":"DP00469","ncbi_taxon_id":3702,"regions_counter":1,"creator":"ameszaros","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":77,"region_id":"DP00469r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Intrinsically unstructured N-terminal domain of bZIP transcription factor HY5. <i> Yoon MK, Shin J, Choi G, Choi BS. </i> Proteins, 2006","term_id":"IDPO:0000002","curator_id":"lkalmar","start":1,"term_ontology":"IDPO","curator_name":"Lajos Kalmár","reference_id":"17001643","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_O24646","date":"2016-09-10T17:29:28.000Z","acc":"O24646","name":"Transcription factor HY5","length":168,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI000012CFC4","genes":[{"name":{"value":"HY5","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9367981","url":"http://www.ncbi.nlm.nih.gov/pubmed/9367981","alternativeUrl":"https://europepmc.org/abstract/MED/9367981"}}]},"synonyms":[{"value":"BZIP56","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11906833","url":"http://www.ncbi.nlm.nih.gov/pubmed/11906833","alternativeUrl":"https://europepmc.org/abstract/MED/11906833"}}]}],"orfNames":[{"value":"F2I11_150","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"CAB96661.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAB96661.1"}}]}],"olnNames":[{"value":"At5g11260","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT5G11260","url":""}}]}]}],"alphafold_very_low_content":0.2976190476190476,"disorder_content":0.4583333333333333,"disprot_consensus":{"full":[{"start":1,"end":77,"type":"D"}],"Structural state":[{"start":1,"end":77,"type":"D"}]}},{"features":{"pfam":[{"id":"PF13181","name":"Tetratricopeptide repeat","start":557,"end":588},{"id":"PF13432","name":"Tetratricopeptide repeat","start":340,"end":402},{"id":"PF13432","name":"Tetratricopeptide repeat","start":502,"end":555}],"gene3D":[{"start":313,"end":639,"id":"1.25.40.10","name":"Tetratricopeptide repeat domain"}]},"uniref50":"UniRef50_P50542","sequence":"MAMRELVEAECGGANPLMKLAGHFTQDKALRQEGLRPGPWPPGAPASEAASKPLGVASEDELVAEFLQDQNAPLVSRAPQTFKMDDLLAEMQQIEQSNFRQAPQRAPGVADLALSENWAQEFLAAGDAVDVTQDYNETDWSQEFISEVTDPLSVSPARWAEEYLEQSEEKLWLGEPEGTATDRWYDEYHPEEDLQHTASDFVAKVDDPKLANSEFLKFVRQIGEGQVSLESGAGSGRAQAEQWAAEFIQQQGTSDAWVDQFTRPVNTSALDMEFERAKSAIESDVDFWDKLQAELEEMAKRDAEAHPWLSDYDDLTSATYDKGYQFEEENPLRDHPQPFEEGLRRLQEGDLPNAVLLFEAAVQQDPKHMEAWQYLGTTQAENEQELLAISALRRCLELKPDNQTALMALAVSFTNESLQRQACETLRDWLRYTPAYAHLVTPAEEGAGGAGLGPSKRILGSLLSDSLFLEVKELFLAAVRLDPTSIDPDVQCGLGVLFNLSGEYDKAVDCFTAALSVRPNDYLLWNKLGATLANGNQSEEAVAAYRRALELQPGYIRSRYNLGISCINLGAHREAVEHFLEALNMQRKSRGPRGEGGAMSENIWSTLRLALSMLGQSDAYGAADARDLSTLLTMFGLPQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P50542","disprot_id":"DP00472","ncbi_taxon_id":9606,"regions_counter":35,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":324,"region_id":"DP00472r001","released":"2023_06","ec_id":"ECO:0006232","reference_html":"The N-terminal half of the peroxisomal cycling receptor Pex5p is a natively unfolded domain. <i> Carvalho AF, Costa-Rodrigues J, Correia I, Costa Pessoa J, Faria TQ, Martins CL, Fransen M, Sá-Miranda C, Azevedo JE. </i> J Mol Biol, 2006","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16403517","version":3,"ec_name":"differential scanning calorimetry evidence used in manual assertion","date":"2023-05-22T15:02:48.554Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"The recombinant His-tagged human Pex5p was obtained as described."}]}],"statement":[{"text":"The DSC analysis of DC1-Pex5p is also presented in Figure 1. Remarkably, the thermogram of this protein corresponds basically to the baseline of the calorimeter. This observation indicates that the N-terminal half of Pex5p lacks any stable tertiary structure.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":324,"region_id":"DP00472r004","released":"2023_06","ec_id":"ECO:0006228","reference_html":"The N-terminal half of the peroxisomal cycling receptor Pex5p is a natively unfolded domain. <i> Carvalho AF, Costa-Rodrigues J, Correia I, Costa Pessoa J, Faria TQ, Martins CL, Fransen M, Sá-Miranda C, Azevedo JE. </i> J Mol Biol, 2006","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16403517","version":3,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","date":"2023-05-22T15:14:33.817Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"The recombinant His-tagged human Pex5p was obtained as described."}]}],"statement":[{"text":"On the other hand, DC1-Pex5p is the most enriched in random coil structure.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":324,"region_id":"DP00472r007","released":"2023_06","ec_id":"ECO:0007680","reference_html":"The N-terminal half of the peroxisomal cycling receptor Pex5p is a natively unfolded domain. <i> Carvalho AF, Costa-Rodrigues J, Correia I, Costa Pessoa J, Faria TQ, Martins CL, Fransen M, Sá-Miranda C, Azevedo JE. </i> J Mol Biol, 2006","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16403517","version":3,"ec_name":"chromatography evidence used in manual assertion","date":"2023-05-22T15:07:43.350Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"The recombinant His-tagged human Pex5p was obtained as described."}]}],"statement":[{"text":"Plotting the molecular mass and the Stokes radius of this protein into the graphic presented in Figure 4(c), reveals that DC1-Pex5p falls in a region between the two straight lines corresponding to natively unfolded intrinsic coils and natively unfolded pre-molten globules.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":324,"region_id":"DP00472r010","released":"2023_06","ec_id":"ECO:0006204","reference_html":"The N-terminal half of the peroxisomal cycling receptor Pex5p is a natively unfolded domain. <i> Carvalho AF, Costa-Rodrigues J, Correia I, Costa Pessoa J, Faria TQ, Martins CL, Fransen M, Sá-Miranda C, Azevedo JE. </i> J Mol Biol, 2006","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16403517","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-05-22T15:05:18.906Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"The recombinant His-tagged human Pex5p was obtained as described."}]}],"statement":[{"text":"This protein displays a maximum of negative ellipticity at 203 nm. Intense negative ellipticity in the vicinity of 200 nm is a property of unfolded polypeptides.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":110,"region_id":"DP00472r014","released":"2023_06","ec_id":"ECO:0006165","reference_html":"A novel Pex14 protein-interacting site of human Pex5 is critical for matrix protein import into peroxisomes. <i> Neuhaus A, Kooshapur H, Wolf J, Meyer NH, Madl T, Saidowsky J, Hambruch E, Lazam A, Jung M, Sattler M, Schliebs W, Erdmann R. </i> J Biol Chem, 2014","statement":[{"text":"NMR fingerprint spectra of 15N-labeled Pex5-(1–110) show very little dispersion, characteristic of an unstructured protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-22T13:27:39.553Z","reference_source":"pmid","term_name":"disorder","reference_id":"24235149","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":71,"term_name":"protein binding","released":"2023_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"A novel Pex14 protein-interacting site of human Pex5 is critical for matrix protein import into peroxisomes. <i> Neuhaus A, Kooshapur H, Wolf J, Meyer NH, Madl T, Saidowsky J, Hambruch E, Lazam A, Jung M, Sattler M, Schliebs W, Erdmann R. </i> J Biol Chem, 2014","statement":[{"text":"However, upon addition of unlabeled Pex14-NTD, the spectrum changes significantly, indicating a strong interaction between Pex5-(1–110) and Pex14-NTD (Fig. 2A).","type":"Results"},{"text":"The binding site of the LVXEF motif on the structure of Pex14-NTD was mapped based on chemical shift perturbations seen upon addition of a 16-mer Pex5 peptide containing the LVAEF sequence to 15N-labeled Pex14-NTD (Fig. 3A). The chemical shift perturbations (data not shown) involve the same set of residues that have been previously shown to bind to a WXXX(F/Y) motif of Pex5, indicating that the new motif interacts with the same surface of Pex14-NTD (16).","type":"Results"},{"text":"The Pex5 LVXEF motif binds in an α-helical conformation to the hydrophobic surface of Pex14-NTD (Fig. 3B). Three conserved residues (Leu-62, Val-63, and Phe-66) of the LVXEF motif are involved in hydrophobic interactions with Pex14-NTD.","type":"Results"}],"term_id":"GO:0005515","curator_id":"vnugnes","start":57,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"24235149","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-22T13:46:46.570Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00472r015","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"4BXU"},{"db":"ELM","id":"LIG_Pex14_3"}],"interaction_partner":[{"db":"UniProt","id":"P50542","operator":"and","partner_start":16,"partner_end":80}]},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":70,"term_name":"disorder to order","released":"2023_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"A novel Pex14 protein-interacting site of human Pex5 is critical for matrix protein import into peroxisomes. <i> Neuhaus A, Kooshapur H, Wolf J, Meyer NH, Madl T, Saidowsky J, Hambruch E, Lazam A, Jung M, Sattler M, Schliebs W, Erdmann R. </i> J Biol Chem, 2014","statement":[{"text":"However, upon addition of unlabeled Pex14-NTD, the spectrum changes significantly, indicating a strong interaction between Pex5-(1–110) and Pex14-NTD (Fig. 2A). Analysis of 13Cα/β secondary chemical shifts revealed that the region including residues Glu-59 to Gln-70 of human Pex5 (59EDELVAEFLQDQ70) forms an α-helix upon interacting with Pex14-NTD (Fig. 2B).","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"vnugnes","start":59,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24235149","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-22T13:41:11.115Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00472r016","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75381"}],"cross_refs":[{"db":"PDB","id":"4BXU"}]},{"start":61,"end":67,"reference_id":"24235149","reference_source":"pmid","reference_html":"A novel Pex14 protein-interacting site of human Pex5 is critical for matrix protein import into peroxisomes. <i> Neuhaus A, Kooshapur H, Wolf J, Meyer NH, Madl T, Saidowsky J, Hambruch E, Lazam A, Jung M, Sattler M, Schliebs W, Erdmann R. </i> J Biol Chem, 2014","date":"2023-05-22T13:51:10.018Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001245","ec_ontology":"ECO","ec_name":"peptide array evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"ELM","id":"LIG_Pex14_3"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P50542","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00472r017","statement":[{"text":"The overlapping region of the new binding site represents 7 amino acids with the sequence ELVAEFL. The core sequence LVAEF resembles the Pex5 WXXX(F/Y) motifs with the major difference that tryptophan is replaced by the hydrophobic amino acid leucine (Fig. 1A).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}]},{"start":1,"end":110,"reference_id":"24235149","reference_source":"pmid","reference_html":"A novel Pex14 protein-interacting site of human Pex5 is critical for matrix protein import into peroxisomes. <i> Neuhaus A, Kooshapur H, Wolf J, Meyer NH, Madl T, Saidowsky J, Hambruch E, Lazam A, Jung M, Sattler M, Schliebs W, Erdmann R. </i> J Biol Chem, 2014","date":"2023-05-22T14:28:45.661Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"ELM","id":"LIG_Pex14_3"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P50542","operator":null,"partner_start":16,"partner_end":80}],"region_id":"DP00472r018","statement":[{"text":"The ITC data show that Pex5-(1–110) binds to Pex14-NTD with a dissociation constant (KD) of 157 ± 9 nm (Fig. 5A), demonstrating high affinity binding, similar to the WXXX(F/Y) motifs (12, 16). The stoichiometry of binding was 1:1, confirming that the identified binding sequence represents the only accessible interacting site within the N-terminal 110 residues of Pex5.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":62,"end":66,"reference_id":"24235149","reference_source":"pmid","reference_html":"A novel Pex14 protein-interacting site of human Pex5 is critical for matrix protein import into peroxisomes. <i> Neuhaus A, Kooshapur H, Wolf J, Meyer NH, Madl T, Saidowsky J, Hambruch E, Lazam A, Jung M, Sattler M, Schliebs W, Erdmann R. </i> J Biol Chem, 2014","date":"2023-05-22T14:29:06.125Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006289","ec_ontology":"ECO","ec_name":"site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"ELM","id":"LIG_Pex14_3"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P50542","operator":null,"partner_start":16,"partner_end":80}],"region_id":"DP00472r019","statement":[{"text":"Analysis of the PRE data for both peptides shows that experimentally observed line broadening effects are in agreement with the theoretically calculated ones based on our NMR structure (Fig. 4). Thus, the PRE data independently confirm that the Pex5 LVXEF motif binds to Pex14 in the same orientation as the Pex5 WXXX(F/Y) peptide.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":62,"end":66,"reference_id":"24235149","reference_source":"pmid","reference_html":"A novel Pex14 protein-interacting site of human Pex5 is critical for matrix protein import into peroxisomes. <i> Neuhaus A, Kooshapur H, Wolf J, Meyer NH, Madl T, Saidowsky J, Hambruch E, Lazam A, Jung M, Sattler M, Schliebs W, Erdmann R. </i> J Biol Chem, 2014","date":"2023-05-22T14:34:48.186Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu62Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val63Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu65Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe66Ala","start":null,"end":null,"position":null}],"cross_refs":[{"db":"ELM","id":"LIG_Pex14_3"}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P50542","operator":null,"partner_start":1,"partner_end":78}],"region_id":"DP00472r020","statement":[{"text":"To study the kinetics of W1-containing Pex5-(1–131), the newly identified LVXEF motif was replaced by penta-alanine. As shown by in vitro binding assays, this mutation abolishes the monovalent interaction between N-terminal fragments of Pex5 and Pex14 (Fig. 6).","type":"Results"},{"text":"A, surface plasmon resonance spectroscopy shows that Pex5-(1–113) binds to immobilized GST-tagged N-terminal domain of Pex14 (GST-Pex14-NTD), although Pex5-(1–113)(LVAEF > AAAAA) lacking the LVXEF motif does not.","type":"Figure"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":62,"end":66,"reference_id":"24235149","reference_source":"pmid","reference_html":"A novel Pex14 protein-interacting site of human Pex5 is critical for matrix protein import into peroxisomes. <i> Neuhaus A, Kooshapur H, Wolf J, Meyer NH, Madl T, Saidowsky J, Hambruch E, Lazam A, Jung M, Sattler M, Schliebs W, Erdmann R. </i> J Biol Chem, 2014","date":"2023-05-22T14:52:27.087Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0016558","term_name":"protein import into peroxisome matrix","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006061","ec_ontology":"ECO","ec_name":"immunofluorescence wide-field microscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu62Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val63Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu65Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe66Ala","start":null,"end":null,"position":null}],"ec_go":"IDA","region_id":"DP00472r021","statement":[{"text":"Wild-type Pex5 rescued the PTS1 import defect of most of the transfected cells (82%), whereas the LVAEF → AAAAA mutant restored peroxisomal protein import in only 43% of the cells. Thus, most cells exhibited no punctate staining, indicative of a complete mislocalization of the peroxisomal marker protein to the cytosol and thus a severe import defect. Moreover, almost all cells that still exhibited a punctate staining upon expression of the LVAEF → AAAAA mutant displayed a partial import defect with strong cytosolic background (Fig. 7A, lower panel). The data indicate that inactivation of the novel Pex14-binding motif strongly affects the efficiency of peroxisomal protein.","type":"Results"}],"term_comment":"","term_def":"\"The import of proteins into the peroxisomal matrix. A peroxisome targeting signal (PTS) binds to a soluble receptor protein in the cytosol, and the resulting complex then binds to a receptor protein in the peroxisome membrane and is imported. The cargo protein is then released into the peroxisome matrix.\" [ISBN:0716731363, PMID:11687502, PMID:11988772]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":100,"reference_id":"16403517","reference_source":"pmid","reference_html":"The N-terminal half of the peroxisomal cycling receptor Pex5p is a natively unfolded domain. <i> Carvalho AF, Costa-Rodrigues J, Correia I, Costa Pessoa J, Faria TQ, Martins CL, Fransen M, Sá-Miranda C, Azevedo JE. </i> J Mol Biol, 2006","date":"2023-05-22T15:09:41.928Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006061","ec_ontology":"ECO","ec_name":"immunofluorescence wide-field microscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"The recombinant His-tagged human Pex5p was obtained as described."}]}],"region_id":"DP00472r022","statement":[{"text":"As shown in Figure 4, the Stokes radii of polypeptides comprising amino acid residues 1–110, 1–197 or 1–268 of Pex5p are compatible with the existence of a natively unfolded conformation in these regions of the protein.","type":"Results"}]},{"start":1,"end":197,"reference_id":"16403517","reference_source":"pmid","reference_html":"The N-terminal half of the peroxisomal cycling receptor Pex5p is a natively unfolded domain. <i> Carvalho AF, Costa-Rodrigues J, Correia I, Costa Pessoa J, Faria TQ, Martins CL, Fransen M, Sá-Miranda C, Azevedo JE. </i> J Mol Biol, 2006","date":"2023-05-22T15:09:45.529Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006061","ec_ontology":"ECO","ec_name":"immunofluorescence wide-field microscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"The recombinant His-tagged human Pex5p was obtained as described."}]}],"region_id":"DP00472r023","statement":[{"text":"As shown in Figure 4, the Stokes radii of polypeptides comprising amino acid residues 1–110, 1–197 or 1–268 of Pex5p are compatible with the existence of a natively unfolded conformation in these regions of the protein.","type":"Results"}]},{"start":1,"end":268,"reference_id":"16403517","reference_source":"pmid","reference_html":"The N-terminal half of the peroxisomal cycling receptor Pex5p is a natively unfolded domain. <i> Carvalho AF, Costa-Rodrigues J, Correia I, Costa Pessoa J, Faria TQ, Martins CL, Fransen M, Sá-Miranda C, Azevedo JE. </i> J Mol Biol, 2006","date":"2023-05-22T15:09:49.648Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006061","ec_ontology":"ECO","ec_name":"immunofluorescence wide-field microscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"The recombinant His-tagged human Pex5p was obtained as described."}]}],"region_id":"DP00472r024","statement":[{"text":"As shown in Figure 4, the Stokes radii of polypeptides comprising amino acid residues 1–110, 1–197 or 1–268 of Pex5p are compatible with the existence of a natively unfolded conformation in these regions of the protein.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P50542","date":"2016-09-07T07:36:09.000Z","acc":"P50542","name":"Peroxisomal targeting signal 1 receptor","length":639,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI000016A16C","genes":[{"name":{"value":"PEX5"},"synonyms":[{"value":"PXR1"}]}],"alphafold_very_low_content":0.28012519561815336,"disorder_content":0.5070422535211268,"disprot_consensus":{"full":[{"start":1,"end":58,"type":"D"},{"start":59,"end":70,"type":"T"},{"start":71,"end":324,"type":"D"}],"Structural state":[{"start":1,"end":324,"type":"D"}],"Molecular function":[{"start":1,"end":110,"type":"F"}],"Structural transition":[{"start":59,"end":70,"type":"T"}],"Biological process":[{"start":62,"end":66,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00875","name":"DNA photolyase","start":24,"end":175},{"id":"PF03441","name":"FAD binding domain of DNA photolyase","start":307,"end":505}],"gene3D":[{"start":22,"end":148,"id":"3.40.50.620","name":"HUPs"},{"start":323,"end":522,"id":"1.10.579.10","name":"DNA Cyclobutane Dipyrimidine Photolyase, subunit A, domain 3"}]},"uniref50":"UniRef50_Q9R194","sequence":"MAATVATAAAVAPAPAPGTDSASSVHWFRKGLRLHDNPALLAAVRGARCVRCVYILDPWFAASSSVGINRWRFLLQSLEDLDTSLRKLNSRLFVVRGQPADVFPRLFKEWGVTRLTFEYDSEPFGKERDAAIMKMAKEAGVEVVTENSHTLYDLDRIIELNGQKPPLTYKRFQAIISRMELPKKPVGLVTSQQMESCRAEIQENHDETYGVPSLEELGFPTEGLGPAVWQGGETEALARLDKHLERKAWVANYERPRMNANSLLASPTGLSPYLRFGCLSCRLFYYRLWDLYKKVKRNSTPPLSLFGQLLWREFFYTAATNNPRFDRMEGNPICIQIPWDRNPEALAKWAEGKTGFPWIDAIMTQLRQEGWIHHLARHAVACFLTRGDLWVSWESGVRVFDELLLDADFSVNAGSWMWLSCSAFFQQFFHCYCPVGFGRRTDPSGDYIRRYLPKLKAFPSRYIYEPWNAPESIQKAAKCIIGVDYPRPIVNHAETSRLNIERMKQIYQQLSRYRGLCLLASVPSCVEDLSHPVAEPSSSQAGSMSSAGPRPLPSGPASPKRKLEAAEEPPGEELSKRARVAELPTPELPSKDA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9R194","disprot_id":"DP00473","ncbi_taxon_id":9606,"regions_counter":9,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":593,"region_id":"DP00473r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Role of structural plasticity in signal transduction by the cryptochrome blue-light photoreceptor. <i> Partch CL, Clarkson MW, Ozgür S, Lee AL, Sancar A. </i> Biochemistry, 2005","term_id":"IDPO:0000002","curator_id":"fquaglia","start":490,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15751956","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":593,"term_name":"disorder to order","start":490,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15751956","version":2,"reference_html":"Role of structural plasticity in signal transduction by the cryptochrome blue-light photoreceptor. <i> Partch CL, Clarkson MW, Ozgür S, Lee AL, Sancar A. </i> Biochemistry, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00473r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":593,"term_name":"protein binding","start":490,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15751956","version":3,"reference_html":"Role of structural plasticity in signal transduction by the cryptochrome blue-light photoreceptor. <i> Partch CL, Clarkson MW, Ozgür S, Lee AL, Sancar A. </i> Biochemistry, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00473r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":593,"region_id":"DP00473r004","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Role of structural plasticity in signal transduction by the cryptochrome blue-light photoreceptor. <i> Partch CL, Clarkson MW, Ozgür S, Lee AL, Sancar A. </i> Biochemistry, 2005","term_id":"IDPO:0000002","curator_id":"fquaglia","start":490,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15751956","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":593,"term_name":"disorder to order","start":490,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15751956","version":2,"reference_html":"Role of structural plasticity in signal transduction by the cryptochrome blue-light photoreceptor. <i> Partch CL, Clarkson MW, Ozgür S, Lee AL, Sancar A. </i> Biochemistry, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00473r005","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":593,"term_name":"protein binding","start":490,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15751956","version":3,"reference_html":"Role of structural plasticity in signal transduction by the cryptochrome blue-light photoreceptor. <i> Partch CL, Clarkson MW, Ozgür S, Lee AL, Sancar A. </i> Biochemistry, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00473r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":593,"region_id":"DP00473r007","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Role of structural plasticity in signal transduction by the cryptochrome blue-light photoreceptor. <i> Partch CL, Clarkson MW, Ozgür S, Lee AL, Sancar A. </i> Biochemistry, 2005","term_id":"IDPO:0000002","curator_id":"fquaglia","start":490,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15751956","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":593,"term_name":"disorder to order","start":490,"ec_name":"cleavage assay evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15751956","version":2,"reference_html":"Role of structural plasticity in signal transduction by the cryptochrome blue-light photoreceptor. <i> Partch CL, Clarkson MW, Ozgür S, Lee AL, Sancar A. </i> Biochemistry, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0007691","region_id":"DP00473r008","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":593,"term_name":"protein binding","start":490,"ec_name":"cleavage assay evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15751956","version":3,"reference_html":"Role of structural plasticity in signal transduction by the cryptochrome blue-light photoreceptor. <i> Partch CL, Clarkson MW, Ozgür S, Lee AL, Sancar A. </i> Biochemistry, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007691","region_id":"DP00473r009","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q49AN0","date":"2016-08-16T10:41:13.000Z","acc":"Q49AN0","name":"Cryptochrome-2","length":593,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000056F15D","genes":[{"name":{"value":"CRY2"},"synonyms":[{"value":"KIAA0658"}]}],"alphafold_very_low_content":0.16863406408094436,"disorder_content":0.17537942664418213,"disprot_consensus":{"full":[{"start":490,"end":593,"type":"T"}],"Structural state":[{"start":490,"end":593,"type":"D"}],"Structural transition":[{"start":490,"end":593,"type":"T"}],"Molecular function":[{"start":490,"end":593,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00875","name":"DNA photolyase","start":14,"end":169},{"id":"PF03441","name":"FAD binding domain of DNA photolyase","start":290,"end":489},{"id":"PF12546","name":"Blue/Ultraviolet sensing protein C terminal","start":519,"end":629}],"gene3D":[{"start":15,"end":213,"id":"3.40.50.620","name":"HUPs"},{"start":141,"end":301,"id":"1.25.40.80","name":"1.25.40.80"},{"start":308,"end":509,"id":"1.10.579.10","name":"DNA Cyclobutane Dipyrimidine Photolyase, subunit A, domain 3"}]},"uniref50":"UniRef50_Q43125","sequence":"MSGSVSGCGSGGCSIVWFRRDLRVEDNPALAAAVRAGPVIALFVWAPEEEGHYHPGRVSRWWLKNSLAQLDSSLRSLGTCLITKRSTDSVASLLDVVKSTGASQIFFNHLYDPLSLVRDHRAKDVLTAQGIAVRSFNADLLYEPWEVTDELGRPFSMFAAFWERCLSMPYDPESPLLPPKKIISGDVSKCVADPLVFEDDSEKGSNALLARAWSPGWSNGDKALTTFINGPLLEYSKNRRKADSATTSFLSPHLHFGEVSVRKVFHLVRIKQVAWANEGNEAGEESVNLFLKSIGLREYSRYISFNHPYSHERPLLGHLKFFPWAVDENYFKAWRQGRTGYPLVDAGMRELWATGWLHDRIRVVVSSFFVKVLQLPWRWGMKYFWDTLLDADLESDALGWQYITGTLPDSREFDRIDNPQFEGYKFDPNGEYVRRWLPELSRLPTDWIHHPWNAPESVLQAAGIELGSNYPLPIVGLDEAKARLHEALSQMWQLEAASRAAIENGSEEGLGDSAEVEEAPIEFPRDITMEETEPTRLNPNRRYEDQMVPSITSSLIRPEEDEESSLNLRNSVGDSRAEVPRNMVNTNQAQQRRAEPASNQVTAMIPEFNIRIVAESTEDSTAESSSSGRRERSGGIVPEWSPGYSEQFPSEENGIGGGSTTSSYLQNHHEILNWRRLSQTG","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q43125","disprot_id":"DP00474","ncbi_taxon_id":3702,"regions_counter":8,"creator":"nveljkovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":681,"region_id":"DP00474r001","released":"2022_03","ec_id":"ECO:0006198","reference_html":"Role of structural plasticity in signal transduction by the cryptochrome blue-light photoreceptor. <i> Partch CL, Clarkson MW, Ozgür S, Lee AL, Sancar A. </i> Biochemistry, 2005","term_id":"IDPO:0000002","curator_id":"fquaglia","start":506,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15751956","version":2,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":681,"term_name":"disorder to order","start":506,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15751956","version":2,"reference_html":"Role of structural plasticity in signal transduction by the cryptochrome blue-light photoreceptor. <i> Partch CL, Clarkson MW, Ozgür S, Lee AL, Sancar A. </i> Biochemistry, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006198","region_id":"DP00474r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":681,"region_id":"DP00474r003","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Role of structural plasticity in signal transduction by the cryptochrome blue-light photoreceptor. <i> Partch CL, Clarkson MW, Ozgür S, Lee AL, Sancar A. </i> Biochemistry, 2005","term_id":"IDPO:0000002","curator_id":"fquaglia","start":506,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15751956","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":681,"term_name":"disorder to order","start":506,"ec_name":"cleavage assay evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15751956","version":2,"reference_html":"Role of structural plasticity in signal transduction by the cryptochrome blue-light photoreceptor. <i> Partch CL, Clarkson MW, Ozgür S, Lee AL, Sancar A. </i> Biochemistry, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0007691","region_id":"DP00474r004","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":681,"region_id":"DP00474r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Role of structural plasticity in signal transduction by the cryptochrome blue-light photoreceptor. <i> Partch CL, Clarkson MW, Ozgür S, Lee AL, Sancar A. </i> Biochemistry, 2005","term_id":"IDPO:0000002","curator_id":"fquaglia","start":506,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15751956","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":681,"term_name":"disorder to order","start":506,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15751956","version":2,"reference_html":"Role of structural plasticity in signal transduction by the cryptochrome blue-light photoreceptor. <i> Partch CL, Clarkson MW, Ozgür S, Lee AL, Sancar A. </i> Biochemistry, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00474r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":12,"region_id":"DP00474r007","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the photolyase-like domain of cryptochrome 1 from Arabidopsis thaliana. <i> Brautigam CA, Smith BS, Ma Z, Palnitkar M, Tomchick DR, Machius M, Deisenhofer J. </i> Proc Natl Acad Sci U S A, 2004","term_id":"IDPO:0000002","curator_id":"nveljkovic","start":1,"term_ontology":"IDPO","curator_name":"Nevena Veljkovic","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-6562-5800","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1U3C"}],"reference_id":"15299148","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":509,"region_id":"DP00474r008","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the photolyase-like domain of cryptochrome 1 from Arabidopsis thaliana. <i> Brautigam CA, Smith BS, Ma Z, Palnitkar M, Tomchick DR, Machius M, Deisenhofer J. </i> Proc Natl Acad Sci U S A, 2004","term_id":"IDPO:0000002","curator_id":"nveljkovic","start":498,"term_ontology":"IDPO","curator_name":"Nevena Veljkovic","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-6562-5800","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1U3C"}],"reference_id":"15299148","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q43125","date":"2016-08-25T16:34:29.000Z","acc":"Q43125","name":"Cryptochrome-1","length":681,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI00001284E1","genes":[{"name":{"value":"CRY1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8953250","url":"http://www.ncbi.nlm.nih.gov/pubmed/8953250","alternativeUrl":"https://europepmc.org/abstract/MED/8953250"}}]},"synonyms":[{"value":"BLU1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12324610","url":"http://www.ncbi.nlm.nih.gov/pubmed/12324610","alternativeUrl":"https://europepmc.org/abstract/MED/12324610"}}]},{"value":"HY4","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8232555","url":"http://www.ncbi.nlm.nih.gov/pubmed/8232555","alternativeUrl":"https://europepmc.org/abstract/MED/8232555"}}]}],"orfNames":[{"value":"T3H13.14","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAD17364.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD17364.1"}}]},{"value":"T3H13.5","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAD17364.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD17364.1"}}]}],"olnNames":[{"value":"At4g08920","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT4G08920","url":""}}]}]}],"alphafold_very_low_content":0.2687224669603524,"disorder_content":0.2878120411160059,"disprot_consensus":{"full":[{"start":1,"end":12,"type":"D"},{"start":498,"end":505,"type":"D"},{"start":506,"end":681,"type":"T"}],"Structural state":[{"start":1,"end":12,"type":"D"},{"start":498,"end":681,"type":"D"}],"Structural transition":[{"start":506,"end":681,"type":"T"}]}},{"features":{"pfam":[{"id":"PF04135","name":"Nucleolar RNA-binding protein, Nop10p family","start":3,"end":52}],"gene3D":[{"start":9,"end":55,"id":"2.20.28.40","name":"H/ACA ribonucleoprotein complex, subunit Nop10"}]},"uniref50":"UniRef50_Q6Q547","sequence":"MHLMYTLGPDGKRIYTLKKVTESGEITKSAHPARFSPDDKYSRQRVTLKKRFGLVPGQ","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q6Q547","disprot_id":"DP00475","ncbi_taxon_id":559292,"regions_counter":3,"creator":"nveljkovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":58,"region_id":"DP00475r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Reconstitution and structural analysis of the yeast box H/ACA RNA-guided pseudouridine synthase. <i> Li S, Duan J, Li D, Yang B, Dong M, Ye K. </i> Genes Dev, 2011","term_id":"IDPO:0000002","curator_id":"nveljkovic","start":49,"term_ontology":"IDPO","curator_name":"Nevena Veljkovic","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-6562-5800","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3U28"}],"reference_id":"22085967","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":38,"region_id":"DP00475r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural study of the H/ACA snoRNP components Nop10p and the 3' hairpin of U65 snoRNA. <i> Khanna M, Wu H, Johansson C, Caizergues-Ferrer M, Feigon J. </i> RNA, 2006","term_id":"IDPO:0000002","curator_id":"nveljkovic","start":17,"term_ontology":"IDPO","curator_name":"Nevena Veljkovic","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6562-5800","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"16373493","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":58,"region_id":"DP00475r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural study of the H/ACA snoRNP components Nop10p and the 3' hairpin of U65 snoRNA. <i> Khanna M, Wu H, Johansson C, Caizergues-Ferrer M, Feigon J. </i> RNA, 2006","term_id":"IDPO:0000002","curator_id":"nveljkovic","start":42,"term_ontology":"IDPO","curator_name":"Nevena Veljkovic","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6562-5800","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"16373493","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q6Q547","date":"2016-09-09T09:25:55.000Z","acc":"Q6Q547","name":"H/ACA ribonucleoprotein complex subunit NOP10","length":58,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000168344","genes":[{"name":{"value":"NOP10"},"olnNames":[{"value":"YHR072W-A"}]}],"alphafold_very_low_content":0,"disorder_content":0.6724137931034483,"disprot_consensus":{"full":[{"start":17,"end":38,"type":"D"},{"start":42,"end":58,"type":"D"}],"Structural state":[{"start":17,"end":38,"type":"D"},{"start":42,"end":58,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00787","name":"PX domain","start":70,"end":157}],"gene3D":[{"start":30,"end":162,"id":"3.30.1520.10","name":"Phox-like domain"}]},"uniref50":"UniRef50_Q08826","sequence":"MPREFKSFGSTEKSLLSKGHGEPSYSEIYAEPENFLEIEVHNPKTHIPNGMDSKGMFTDYEIICRTNLPSFHKRVSKVRRRYSDFEFFRKCLIKEISMLNHPKVMVPHLPGKILLSNRFSNEVIEERRQGLNTWMQSVAGHPLLQSGSKVLVRFIEAEKFVG","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q08826","disprot_id":"DP00482","ncbi_taxon_id":559292,"regions_counter":1,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":29,"region_id":"DP00482r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Crystal structure of the yeast Phox homology (PX) domain protein Grd19p complexed to phosphatidylinositol-3-phosphate. <i> Zhou CZ, Li de La Sierra-Gallay I, Quevillon-Cheruel S, Collinet B, Minard P, Blondeau K, Henckes G, Aufrère R, Leulliot N, Graille M, Sorel I, Savarin P, de la Torre F, Poupon A, Janin J, van Tilbeurgh H. </i> J Biol Chem, 2003","term_id":"IDPO:0000002","curator_id":"jpujols","start":1,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1OCS"}],"reference_id":"14514667","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q08826","date":"2016-09-06T13:10:50.000Z","acc":"Q08826","name":"Sorting nexin-3","length":162,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000135B41","genes":[{"name":{"value":"SNX3"},"synonyms":[{"value":"GRD19"}],"olnNames":[{"value":"YOR357C"}]}],"alphafold_very_low_content":0.04938271604938271,"disorder_content":0.17901234567901234,"disprot_consensus":{"full":[{"start":1,"end":29,"type":"D"}],"Structural state":[{"start":1,"end":29,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00899","name":"ThiF family","start":19,"end":337}],"gene3D":[{"start":1,"end":346,"id":"3.40.50.720","name":"NAD(P)-binding Rossmann-like Domain"}]},"uniref50":"UniRef50_Q9UBE0","sequence":"MVEKEEAGGGISEEEAAQYDRQIRLWGLEAQKRLRASRVLLVGLKGLGAEIAKNLILAGVKGLTMLDHEQVTPEDPGAQFLIRTGSVGRNRAEASLERAQNLNPMVDVKVDTEDIEKKPESFFTQFDAVCLTCCSRDVIVKVDQICHKNSIKFFTGDVFGYHGYTFANLGEHEFVEEKTKVAKVSQGVEDGPDTKRAKLDSSETTMVKKKVVFCPVKEALEVDWSSEKAKAALKRTTSDYFLLQVLLKFRTDKGRDPSSDTYEEDSELLLQIRNDVLDSLGISPDLLPEDFVRYCFSEMAPVCAVVGGILAQEIVKALSQRDPPHNNFFFFDGMKGNGIVECLGPK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UBE0","disprot_id":"DP00485","ncbi_taxon_id":9606,"regions_counter":20,"creator":"sventura","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":203,"region_id":"DP00485r001","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1. <i> Lois LM, Lima CD. </i> EMBO J, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":178,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-09-01T19:30:24.832Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1Y8Q"},{"db":"PDB","id":"1Y8R"}],"reference_id":"15660128","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBE0"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63165"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15422","entry_name":"ATP"}],"statement":[{"text":"Disordered regions not observed in electron density included Sae1 residues 178–203 and 346, and Sae2 residues 1–3, 219–237, 291–304, and 551–640.","type":"Results"}]},{"start":1,"end":24,"reference_id":"20164921","reference_source":"pmid","reference_html":"Active site remodelling accompanies thioester bond formation in the SUMO E1. <i> Olsen SK, Capili AD, Lu X, Tan DS, Lima CD. </i> Nature, 2010","date":"2023-11-24T10:51:12.008Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"3KYD"}],"region_id":"DP00485r013","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBT2 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63165"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:49867821","statements":[{"type":"Curator statement","text":"Interacting with the complex is the syntetic component 5′-(vinylsulfonylaminodeoxy)adenosine tripeptide variant (CGG-AVSN)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":"ethylene glycol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"In SAE1, the N-terminal helices H1 and H2 that lie beneath the Cys domain and UBA2 helix 13 in the open conformation move out of the adenylation active site and become disordered in the closed conformation.","type":"Results"},{"text":"The authors referred as closed conformation the structure formed by the  E1~SUMO1-AVSN complex, whereas mention as open conformation the structure that forms the E1/SUMO1-AMSN complex.","type":"Curator statement"}]},{"start":9,"end":24,"reference_id":"20164921","reference_source":"pmid","reference_html":"Active site remodelling accompanies thioester bond formation in the SUMO E1. <i> Olsen SK, Capili AD, Lu X, Tan DS, Lima CD. </i> Nature, 2010","date":"2023-11-24T10:52:32.665Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"3KYD"},{"db":"PDB","id":"3KYC"}],"region_id":"DP00485r014","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBT2 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63165"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:49867821","statements":[{"type":"Curator statement","text":"Interacting with the close complex is the syntetic component 5′-(vinylsulfonylaminodeoxy)adenosine tripeptide variant (CGG-AVSN)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":"ethylene glycol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:44620962","statements":[{"type":"Curator statement","text":"Interacting with the open complex is a non-hydrolyzable mimic of the acyl-adenylate intermediate (AMSN) was made by linking a cysteylglycylglycyl tripeptide to 5′-(sulfamoylaminodeoxy)adenosine (CGG-AMSN)"}]}],"statement":[{"text":"In SAE1, the N-terminal helices H1 and H2 that lie beneath the Cys domain and UBA2 helix 13 in the open conformation move out of the adenylation active site and become disordered in the closed conformation.","type":"Results"},{"text":"The authors referred as closed conformation the structure formed by the  E1~SUMO1-AVSN complex, whereas mention as open conformation the structure that forms the E1/SUMO1-AMSN complex.","type":"Curator statement"}],"states_connection":[{"source":"DP00485r015","target":"DP00485r013"}]},{"start":9,"end":24,"reference_id":"20164921","reference_source":"pmid","reference_html":"Active site remodelling accompanies thioester bond formation in the SUMO E1. <i> Olsen SK, Capili AD, Lu X, Tan DS, Lima CD. </i> Nature, 2010","date":"2023-11-24T10:51:43.129Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"3KYC"}],"region_id":"DP00485r015","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBT2 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63165"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:44620962","statements":[{"type":"Curator statement","text":"Interacting with the complex is a non-hydrolyzable mimic of the acyl-adenylate intermediate (AMSN) was made by linking a cysteylglycylglycyl tripeptide to 5′-(sulfamoylaminodeoxy)adenosine (CGG-AMSN)"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"In SAE1, the N-terminal helices H1 and H2 that lie beneath the Cys domain and UBA2 helix 13 in the open conformation move out of the adenylation active site and become disordered in the closed conformation.","type":"Results"},{"text":"The authors referred as closed conformation the structure formed by the  E1~SUMO1-AVSN complex, whereas mention as open conformation the structure that forms the E1/SUMO1-AMSN complex.","type":"Curator statement"}]},{"start":181,"end":204,"reference_id":"20164921","reference_source":"pmid","reference_html":"Active site remodelling accompanies thioester bond formation in the SUMO E1. <i> Olsen SK, Capili AD, Lu X, Tan DS, Lima CD. </i> Nature, 2010","date":"2023-11-24T10:50:11.191Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"3KYC"}],"region_id":"DP00485r016","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBT2 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63165"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:44620962","statements":[{"type":"Curator statement","text":"Interacting with the complex is a non-hydrolyzable mimic of the acyl-adenylate intermediate (AMSN) was made by linking a cysteylglycylglycyl tripeptide to 5′-(sulfamoylaminodeoxy)adenosine (CGG-AMSN)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"The final model contained SUMO1(19–97)-AMSN, SAE1 amino acids (aa) 9–180 and 205–345, and UBA2 aa 5–217, 235–291, 305–548 and 608–640. As full-length proteins were used in crystallization, residues not observed in electron density were presumed disordered.","type":"Methods"}]},{"start":184,"end":203,"reference_id":"20164921","reference_source":"pmid","reference_html":"Active site remodelling accompanies thioester bond formation in the SUMO E1. <i> Olsen SK, Capili AD, Lu X, Tan DS, Lima CD. </i> Nature, 2010","date":"2022-09-02T15:25:27.723Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"3KYD"}],"region_id":"DP00485r017","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBT2 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63165"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting with the complex is the syntetic component 5′-(vinylsulfonylaminodeoxy)adenosine tripeptide variant (CGG-AVSN)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":"ethylene glycol"}],"statement":[{"text":"The final model includes SUMO1(20–97)-AVSN, SAE1 aa 25–183 and 204–345 and UBA2 aa 4–197, 240–290, 309–336 and 345–548. SUMO1(1–97)-AVSN, SAE1 and UBA2 (1–550) were crystallized, so residues not observed in electron density were presumed disordered.","type":"Methods"}]},{"start":270,"end":294,"reference_id":"20164921","reference_source":"pmid","reference_html":"Active site remodelling accompanies thioester bond formation in the SUMO E1. <i> Olsen SK, Capili AD, Lu X, Tan DS, Lima CD. </i> Nature, 2010","date":"2023-11-24T10:49:58.128Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006222","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"3KYC"}],"region_id":"DP00485r018","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBT2 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63165"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:44620962","statements":[{"type":"Curator statement","text":"Interacting with the complex is a non-hydrolyzable mimic of the acyl-adenylate intermediate (AMSN) was made by linking a cysteylglycylglycyl tripeptide to 5′-(sulfamoylaminodeoxy)adenosine (CGG-AMSN)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"The PDB data shows this region has high relative B-factor values, indicating it is disordered.","type":"Curator statement"}]},{"start":222,"end":235,"reference_id":"20164921","reference_source":"pmid","reference_html":"Active site remodelling accompanies thioester bond formation in the SUMO E1. <i> Olsen SK, Capili AD, Lu X, Tan DS, Lima CD. </i> Nature, 2010","date":"2023-11-24T10:49:41.350Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006222","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"3KYC"}],"region_id":"DP00485r019","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBT2 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63165"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:44620962","statements":[{"type":"Curator statement","text":"Interacting with the complex is a non-hydrolyzable mimic of the acyl-adenylate intermediate (AMSN) was made by linking a cysteylglycylglycyl tripeptide to 5′-(sulfamoylaminodeoxy)adenosine (CGG-AMSN)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"The PDB data shows this region has high relative B-factor values, indicating it is disordered.","type":"Curator statement"}]},{"start":176,"end":208,"reference_id":"20164921","reference_source":"pmid","reference_html":"Active site remodelling accompanies thioester bond formation in the SUMO E1. <i> Olsen SK, Capili AD, Lu X, Tan DS, Lima CD. </i> Nature, 2010","date":"2023-11-24T10:49:24.701Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006222","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"3KYC"}],"region_id":"DP00485r020","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBT2 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63165"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:44620962","statements":[{"type":"Curator statement","text":"Interacting with the complex is a non-hydrolyzable mimic of the acyl-adenylate intermediate (AMSN) was made by linking a cysteylglycylglycyl tripeptide to 5′-(sulfamoylaminodeoxy)adenosine (CGG-AMSN)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"The PDB data shows this region has high relative B-factor values, indicating it is disordered.","type":"Curator statement"}]}],"released":"2016_10","uniref100":"UniRef100_Q9UBE0","date":"2016-09-06T16:35:36.000Z","acc":"Q9UBE0","name":"SUMO-activating enzyme subunit 1","length":346,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI0000037725","genes":[{"name":{"value":"SAE1"},"synonyms":[{"value":"AOS1"},{"value":"SUA1"},{"value":"UBLE1A"}]}],"alphafold_very_low_content":0.049132947976878616,"disorder_content":0.2774566473988439,"disprot_consensus":{"full":[{"start":1,"end":8,"type":"D"},{"start":9,"end":24,"type":"T"},{"start":176,"end":208,"type":"D"},{"start":222,"end":235,"type":"D"},{"start":270,"end":294,"type":"D"}],"Structural state":[{"start":1,"end":24,"type":"D"},{"start":176,"end":208,"type":"D"},{"start":222,"end":235,"type":"D"},{"start":270,"end":294,"type":"D"}],"Structural transition":[{"start":9,"end":24,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00899","name":"ThiF family","start":14,"end":442},{"id":"PF14732","name":"Ubiquitin/SUMO-activating enzyme ubiquitin-like domain","start":452,"end":538},{"id":"PF16195","name":"SUMO-activating enzyme subunit 2 C-terminus","start":549,"end":631}],"gene3D":[{"start":168,"end":382,"id":"1.10.10.520","name":"Ubiquitin activating enzymes (Uba3). Chain: B, domain 2"},{"start":577,"end":640,"id":"3.10.290.20","name":"Ubiquitin-like 2 activating enzyme e1b. Chain:  B, domain 3"},{"start":445,"end":576,"id":"3.10.290.20","name":"Ubiquitin-like 2 activating enzyme e1b. Chain:  B, domain 3"},{"start":18,"end":444,"id":"3.40.50.720","name":"NAD(P)-binding Rossmann-like Domain"}]},"uniref50":"UniRef50_Q9UBT2","sequence":"MALSRGLPRELAEAVAGGRVLVVGAGGIGCELLKNLVLTGFSHIDLIDLDTIDVSNLNRQFLFQKKHVGRSKAQVAKESVLQFYPKANIVAYHDSIMNPDYNVEFFRQFILVMNALDNRAARNHVNRMCLAADVPLIESGTAGYLGQVTTIKKGVTECYECHPKPTQRTFPGCTIRNTPSEPIHCIVWAKYLFNQLFGEEDADQEVSPDRADPEAAWEPTEAEARARASNEDGDIKRISTKEWAKSTGYDPVKLFTKLFKDDIRYLLTMDKLWRKRKPPVPLDWAEVQSQGEETNASDQQNEPQLGLKDQQVLDVKSYARLFSKSIETLRVHLAEKGDGAELIWDKDDPSAMDFVTSAANLRMHIFSMNMKSRFDIKSMAGNIIPAIATTNAVIAGLIVLEGLKILSGKIDQCRTIFLNKQPNPRKKLLVPCALDPPNPNCYVCASKPEVTVRLNVHKVTVLTLQDKIVKEKFAMVAPDVQIEDGKGTILISSEEGETEANNHKKLSEFGIRNGSRLQADDFLQDYTLLINILHSEDLGKDVEFEVVGDAPEKVGPKQAEDAAKSITNGSDDGAQPSTSTAQEQDDVLIVDSDEEDSSNNADVSEEERSRKRKLDEKENLSAKRSRIEQKEELDDVIALD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UBT2","disprot_id":"DP00486","ncbi_taxon_id":9606,"regions_counter":11,"creator":"aelofsson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":304,"region_id":"DP00486r001","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1. <i> Lois LM, Lima CD. </i> EMBO J, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":291,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-24T10:55:09.786Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1Y8Q"},{"db":"PDB","id":"1Y8R"}],"reference_id":"15660128","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBE0"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63165"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15422","entry_name":"ATP"}],"statement":[{"text":"Disordered regions not observed in electron density included Sae1 residues 178–203 and 346, and Sae2 residues 1–3, 219–237, 291–304, and 551–640.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":640,"region_id":"DP00486r002","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1. <i> Lois LM, Lima CD. </i> EMBO J, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":551,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-09-01T19:24:29.144Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1Y8Q"},{"db":"PDB","id":"1Y8R"}],"reference_id":"15660128","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBE0"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63165"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15422","entry_name":"ATP"}],"statement":[{"text":"Disordered regions not observed in electron density included Sae1 residues 178–203 and 346, and Sae2 residues 1–3, 219–237, 291–304, and 551–640.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":237,"region_id":"DP00486r003","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1. <i> Lois LM, Lima CD. </i> EMBO J, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":219,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-09-01T19:21:24.626Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1Y8Q"},{"db":"PDB","id":"1Y8R"}],"reference_id":"15660128","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBE0"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63165"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15422","entry_name":"ATP"}],"statement":[{"text":"Disordered regions not observed in electron density included Sae1 residues 178–203 and 346, and Sae2 residues 1–3, 219–237, 291–304, and 551–640.","type":"Results"}]},{"start":198,"end":239,"reference_id":"20164921","reference_source":"pmid","reference_html":"Active site remodelling accompanies thioester bond formation in the SUMO E1. <i> Olsen SK, Capili AD, Lu X, Tan DS, Lima CD. </i> Nature, 2010","date":"2023-11-24T10:54:35.486Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"3KYD"}],"region_id":"DP00486r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBE0"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63165"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":"ethylene glycol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:49867821","statements":[{"type":"Curator statement","text":"Interacting with the complex is the syntetic component 5′-(vinylsulfonylaminodeoxy)adenosine tripeptide variant (CGG-AVSN)."}]}],"statement":[{"text":"The final model includes SUMO1(20–97)-AVSN, SAE1 aa 25–183 and 204–345 and UBA2 aa 4–197, 240–290, 309–336 and 345–548. SUMO1(1–97)-AVSN, SAE1 and UBA2 (1–550) were crystallized, so residues not observed in electron density were presumed disordered.","type":"Methods"}]},{"start":218,"end":234,"reference_id":"20164921","reference_source":"pmid","reference_html":"Active site remodelling accompanies thioester bond formation in the SUMO E1. <i> Olsen SK, Capili AD, Lu X, Tan DS, Lima CD. </i> Nature, 2010","date":"2023-11-24T10:54:18.550Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"3KYC"}],"region_id":"DP00486r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBE0"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63165"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:44620962","statements":[{"type":"Curator statement","text":"Interacting with the complex is a non-hydrolyzable mimic of the acyl-adenylate intermediate (AMSN) was made by linking a cysteylglycylglycyl tripeptide to 5′-(sulfamoylaminodeoxy)adenosine (CGG-AMSN)."}]}],"statement":[{"text":"The final model contained SUMO1(19–97)-AMSN, SAE1 amino acids (aa) 9–180 and 205–345, and UBA2 aa 5–217, 235–291, 305–548 and 608–640. As full-length proteins were used in crystallization, residues not observed in electron density were presumed disordered.","type":"Methods"}]},{"start":549,"end":607,"reference_id":"20164921","reference_source":"pmid","reference_html":"Active site remodelling accompanies thioester bond formation in the SUMO E1. <i> Olsen SK, Capili AD, Lu X, Tan DS, Lima CD. </i> Nature, 2010","date":"2023-11-24T10:54:03.184Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"3KYC"}],"region_id":"DP00486r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBE0"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63165"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:44620962","statements":[{"type":"Curator statement","text":"Interacting with the complex is a non-hydrolyzable mimic of the acyl-adenylate intermediate (AMSN) was made by linking a cysteylglycylglycyl tripeptide to 5′-(sulfamoylaminodeoxy)adenosine (CGG-AMSN)."}]}],"statement":[{"text":"The final model contained SUMO1(19–97)-AMSN, SAE1 amino acids (aa) 9–180 and 205–345, and UBA2 aa 5–217, 235–291, 305–548 and 608–640. As full-length proteins were used in crystallization, residues not observed in electron density were presumed disordered.","type":"Methods"}]},{"start":198,"end":217,"reference_id":"20164921","reference_source":"pmid","reference_html":"Active site remodelling accompanies thioester bond formation in the SUMO E1. <i> Olsen SK, Capili AD, Lu X, Tan DS, Lima CD. </i> Nature, 2010","date":"2023-11-24T10:55:48.919Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"3KYC"},{"db":"PDB","id":"3KYD"}],"region_id":"DP00486r007","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBE0"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63165"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:44620962","statements":[{"type":"Curator statement","text":"Interacting with the complex is a non-hydrolyzable mimic of the acyl-adenylate intermediate (AMSN) was made by linking a cysteylglycylglycyl tripeptide to 5′-(sulfamoylaminodeoxy)adenosine (CGG-AMSN)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:49867821","statements":[{"type":"Curator statement","text":"Interacting with the complex is the syntetic component 5′-(vinylsulfonylaminodeoxy)adenosine tripeptide variant (CGG-AVSN)."}]}],"statement":[{"text":"The final model contained SUMO1(19–97)-AMSN, SAE1 amino acids (aa) 9–180 and 205–345, and UBA2 aa 5–217, 235–291, 305–548 and 608–640. As full-length proteins were used in crystallization, residues not observed in electron density were presumed disordered.","type":"Methods"},{"text":"The final model includes SUMO1(20–97)-AVSN, SAE1 aa 25–183 and 204–345 and UBA2 aa 4–197, 240–290, 309–336 and 345–548. SUMO1(1–97)-AVSN, SAE1 and UBA2 (1–550) were crystallized, so residues not observed in electron density were presumed disordered.","type":"Methods"},{"text":"The X-ray evidence shows there is a structure transition between the open and close conformation of the complex. The authors referred as closed conformation the structure formed by the E1~SUMO1-AVSN complex, whereas mention as open conformation the structure that forms the E1/SUMO1-AMSN complex.","type":"Curator statement"}],"states_connection":[{"source":"DP00486r008","target":"DP00486r004"}]},{"start":198,"end":217,"reference_id":"20164921","reference_source":"pmid","reference_html":"Active site remodelling accompanies thioester bond formation in the SUMO E1. <i> Olsen SK, Capili AD, Lu X, Tan DS, Lima CD. </i> Nature, 2010","date":"2023-11-24T10:53:35.393Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"3KYC"}],"region_id":"DP00486r008","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBE0"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63165"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:44620962","statements":[{"type":"Curator statement","text":"Interacting with the complex is a non-hydrolyzable mimic of the acyl-adenylate intermediate (AMSN) was made by linking a cysteylglycylglycyl tripeptide to 5′-(sulfamoylaminodeoxy)adenosine (CGG-AMSN)."}]}],"statement":[{"text":"The final model contained SUMO1(19–97)-AMSN, SAE1 amino acids (aa) 9–180 and 205–345, and UBA2 aa 5–217, 235–291, 305–548 and 608–640. As full-length proteins were used in crystallization, residues not observed in electron density were presumed disordered.","type":"Methods"},{"text":"The final model includes SUMO1(20–97)-AVSN, SAE1 aa 25–183 and 204–345 and UBA2 aa 4–197, 240–290, 309–336 and 345–548. SUMO1(1–97)-AVSN, SAE1 and UBA2 (1–550) were crystallized, so residues not observed in electron density were presumed disordered.","type":"Methods"},{"text":"The X-ray evidence shows there is a structure transition between the open and close conformation of the complex. The authors referred as closed conformation the structure formed by the E1~SUMO1-AVSN complex, whereas mention as open conformation the structure that forms the E1/SUMO1-AMSN complex.","type":"Curator statement"}]},{"start":607,"end":640,"reference_id":"20164921","reference_source":"pmid","reference_html":"Active site remodelling accompanies thioester bond formation in the SUMO E1. <i> Olsen SK, Capili AD, Lu X, Tan DS, Lima CD. </i> Nature, 2010","date":"2023-11-24T10:56:04.193Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"3KYC"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P63165","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00486r009","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBE0"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:44620962","statements":[{"type":"Curator statement","text":"Interacting with the complex is a non-hydrolyzable mimic of the acyl-adenylate intermediate (AMSN) was made by linking a cysteylglycylglycyl tripeptide to 5′-(sulfamoylaminodeoxy)adenosine (CGG-AMSN)."}]}],"statement":[{"text":"Another notable difference was that E1 amino acids 607–640 of UBA2 were observed in contacts with SUMO1 via a C-terminal SIM motif (aa 632–640; ELDDVIALD; Supplemental Fig. 2) although the functional significance of the SIM remains unclear because amino acids 550–640 are dispensible for human E1 activity in vitro and for yeast E1 function in vivo in S. cerevisiae9.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":608,"end":640,"reference_id":"20164921","reference_source":"pmid","reference_html":"Active site remodelling accompanies thioester bond formation in the SUMO E1. <i> Olsen SK, Capili AD, Lu X, Tan DS, Lima CD. </i> Nature, 2010","date":"2023-11-24T10:55:26.738Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"3KYC"}],"region_id":"DP00486r010","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBE0"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63165"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:44620962","statements":[{"type":"Curator statement","text":"Interacting with the complex is a non-hydrolyzable mimic of the acyl-adenylate intermediate (AMSN) was made by linking a cysteylglycylglycyl tripeptide to 5′-(sulfamoylaminodeoxy)adenosine (CGG-AMSN)."}]}],"statement":[{"text":"The PDB shows this region is ordered in the called open conformation of the E1/SUMO1-AMSN complex.","type":"Curator statement"}],"states_connection":[{"source":"DP00486r002","target":"DP00486r011"}]},{"start":608,"end":640,"reference_id":"20164921","reference_source":"pmid","reference_html":"Active site remodelling accompanies thioester bond formation in the SUMO E1. <i> Olsen SK, Capili AD, Lu X, Tan DS, Lima CD. </i> Nature, 2010","date":"2023-11-24T10:53:21.626Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"3KYC"}],"region_id":"DP00486r011","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBE0"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63165"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:44620962","statements":[{"type":"Curator statement","text":"Interacting with the complex is a non-hydrolyzable mimic of the acyl-adenylate intermediate (AMSN) was made by linking a cysteylglycylglycyl tripeptide to 5′-(sulfamoylaminodeoxy)adenosine (CGG-AMSN)."}]}],"statement":[{"text":"The PDB shows this region is ordered in the called open conformation of the E1/SUMO1-AMSN complex.","type":"Curator statement"}]}],"released":"2016_10","uniref100":"UniRef100_Q9UBT2","date":"2016-09-06T16:26:44.000Z","acc":"Q9UBT2","name":"SUMO-activating enzyme subunit 2","length":640,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI0000073E4E","genes":[{"name":{"value":"UBA2"},"synonyms":[{"value":"SAE2"},{"value":"UBLE1B"}],"orfNames":[{"value":"HRIHFB2115"}]}],"alphafold_very_low_content":0.1203125,"disorder_content":0.23125,"disprot_consensus":{"full":[{"start":198,"end":217,"type":"T"},{"start":218,"end":239,"type":"D"},{"start":291,"end":304,"type":"D"},{"start":549,"end":607,"type":"D"},{"start":608,"end":640,"type":"T"}],"Structural state":[{"start":198,"end":239,"type":"D"},{"start":291,"end":304,"type":"D"},{"start":549,"end":640,"type":"D"}],"Structural transition":[{"start":198,"end":217,"type":"T"},{"start":608,"end":640,"type":"T"}],"Molecular function":[{"start":607,"end":640,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00268","name":"Ribonucleotide reductase, small chain","start":85,"end":353}],"gene3D":[{"start":26,"end":359,"id":"1.10.620.20","name":"Ribonucleotide Reductase, subunit A"}]},"uniref50":"UniRef50_P09938","sequence":"MPKETPSKAAADALSDLEIKDSKSNLNKELETLREENRVKSDMLKEKLSKDAENHKAYLKSHQVHRHKLKEMEKEEPLLNEDKERTVLFPIKYHEIWQAYKRAEASFWTAEEIDLSKDIHDWNNRMNENERFFISRVLAFFAASDGIVNENLVENFSTEVQIPEAKSFYGFQIMIENIHSETYSLLIDTYIKDPKESEFLFNAIHTIPEIGEKAEWALRWIQDADALFGERLVAFASIEGVFFSGSFASIFWLKKRGMMPGLTFSNELICRDEGLHTDFACLLFAHLKNKPDPAIVEKIVTEAVEIEQRYFLDALPVALLGMNADLMNQYVEFVADRLLVAFGNKKYYKVENPFDFMENISLAGKTNFFEKRVSDYQKAGVMSKSTKQEAGAFTFNEDF","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P09938","disprot_id":"DP00487","ncbi_taxon_id":559292,"regions_counter":12,"creator":"maspromonte","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":41,"region_id":"DP00487r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer. <i> Voegtli WC, Ge J, Perlstein DL, Stubbe J, Rosenzweig AC. </i> Proc Natl Acad Sci U S A, 2001","term_id":"IDPO:0000002","curator_id":"maspromonte","start":1,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1JK0"}],"reference_id":"11526233","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":41,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer. <i> Voegtli WC, Ge J, Perlstein DL, Stubbe J, Rosenzweig AC. </i> Proc Natl Acad Sci U S A, 2001","term_id":"GO:0060090","curator_id":"maspromonte","start":1,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"11526233","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00487r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":41,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer. <i> Voegtli WC, Ge J, Perlstein DL, Stubbe J, Rosenzweig AC. </i> Proc Natl Acad Sci U S A, 2001","term_id":"IDPO:0000011","curator_id":"maspromonte","start":1,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","reference_id":"11526233","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00487r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":41,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer. <i> Voegtli WC, Ge J, Perlstein DL, Stubbe J, Rosenzweig AC. </i> Proc Natl Acad Sci U S A, 2001","term_id":"GO:0005515","curator_id":"maspromonte","start":1,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"11526233","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00487r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":399,"region_id":"DP00487r009","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer. <i> Voegtli WC, Ge J, Perlstein DL, Stubbe J, Rosenzweig AC. </i> Proc Natl Acad Sci U S A, 2001","term_id":"IDPO:0000002","curator_id":"vnugnes","start":360,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-29T18:05:56.028Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1JK0"}],"reference_id":"11526233","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P49723"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"},{"text":"The Y2 model includes residues 26–359, and the Y4 model includes residues 11–90, 100–263, and 275–295.","type":"Methods"}]}],"released":"2016_10","uniref100":"UniRef100_P09938","date":"2016-09-06T16:52:43.000Z","acc":"P09938","name":"Ribonucleoside-diphosphate reductase small chain 1","length":399,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000168DF7","genes":[{"name":{"value":"RNR2"},"synonyms":[{"value":"CRT6"}],"orfNames":[{"value":"J1271"}],"olnNames":[{"value":"YJL026W"}]}],"alphafold_very_low_content":0.10776942355889724,"disorder_content":0.20300751879699247,"disprot_consensus":{"full":[{"start":1,"end":41,"type":"T"},{"start":360,"end":399,"type":"D"}],"Structural state":[{"start":1,"end":41,"type":"D"},{"start":360,"end":399,"type":"D"}],"Molecular function":[{"start":1,"end":41,"type":"F"}],"Structural transition":[{"start":1,"end":41,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00268","name":"Ribonucleotide reductase, small chain","start":34,"end":300}],"gene3D":[{"start":1,"end":325,"id":"1.10.620.20","name":"Ribonucleotide Reductase, subunit A"}]},"uniref50":"UniRef50_P49723","sequence":"MEAHNQFLKTFQKERHDMKEAEKDEILLMENSRRFVMFPIKYHEIWAAYKKVEASFWTAEEIELAKDTEDFQKLTDDQKTYIGNLLALSISSDNLVNKYLIENFSAQLQNPEGKSFYGFQIMMENIYSEVYSMMVDAFFKDPKNIPLFKEIANLPEVKHKAAFIERWISNDDSLYAERLVAFAAKEGIFQAGNYASMFWLTDKKIMPGLAMANRNICRDRGAYTDFSCLLFAHLRTKPNPKIIEKIITEAVEIEKEYYSNSLPVEKFGMDLKSIHTYIEFVADGLLQGFGNEKYYNAVNPFEFMEDVATAGKTTFFEKKVSDYQKASDMSKSATPSKEINFDDDF","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P49723","disprot_id":"DP00488","ncbi_taxon_id":559292,"regions_counter":6,"creator":"aelofsson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":345,"region_id":"DP00488r001","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer. <i> Voegtli WC, Ge J, Perlstein DL, Stubbe J, Rosenzweig AC. </i> Proc Natl Acad Sci U S A, 2001","term_id":"IDPO:0000002","curator_id":"vnugnes","start":296,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-29T18:01:46.839Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1JK0"}],"reference_id":"11526233","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P09938"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"},{"text":"No electron density is present for the C-terminal 41 residues of Y2 and 51 residues of Y4, suggesting that these regions are disordered.","type":"Results"}]},{"start":1,"end":10,"reference_id":"11526233","reference_source":"pmid","reference_html":"Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer. <i> Voegtli WC, Ge J, Perlstein DL, Stubbe J, Rosenzweig AC. </i> Proc Natl Acad Sci U S A, 2001","date":"2022-08-29T18:03:21.399Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"1JK0"}],"region_id":"DP00488r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P09938"}],"statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":264,"end":274,"reference_id":"11526233","reference_source":"pmid","reference_html":"Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer. <i> Voegtli WC, Ge J, Perlstein DL, Stubbe J, Rosenzweig AC. </i> Proc Natl Acad Sci U S A, 2001","date":"2022-08-29T18:05:09.818Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"1JK0"}],"region_id":"DP00488r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P09938"}],"statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"},{"text":"No electron density was present for Y4 residues 91–99 and 264–274.","type":"Methods"}]}],"released":"2016_10","uniref100":"UniRef100_P49723","date":"2016-09-06T16:47:28.000Z","acc":"P49723","name":"Ribonucleoside-diphosphate reductase small chain 2","length":345,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000005328F","genes":[{"name":{"value":"RNR4"},"synonyms":[{"value":"CRT3"}],"olnNames":[{"value":"YGR180C"}]}],"alphafold_very_low_content":0.11014492753623188,"disorder_content":0.20579710144927535,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"},{"start":264,"end":274,"type":"D"},{"start":296,"end":345,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":264,"end":274,"type":"D"},{"start":296,"end":345,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01462","name":"Leucine rich repeat N-terminal domain","start":55,"end":81},{"id":"PF13855","name":"Leucine rich repeat","start":87,"end":142},{"id":"PF13855","name":"Leucine rich repeat","start":152,"end":213},{"id":"PF13855","name":"Leucine rich repeat","start":222,"end":282}],"gene3D":[{"start":53,"end":360,"id":"3.80.10.10","name":"Ribonuclease Inhibitor"}]},"uniref50":"UniRef50_P07585","sequence":"MKATIIFLLVAQVSWAGPFQQKGLFDFMLEDEASGIGPEEHFPEVPEIEPMGPVCPFRCQCHLRVVQCSDLGLEKVPKDLPPDTALLDLQNNKITEIKDGDFKNLKNLHTLILINNKISKISPGAFAPLVKLERLYLSKNQLKELPEKMPKTLQELRVHENEITKVRKSVFNGLNQMIVVELGTNPLKSSGIENGAFQGMKKLSYIRIADTNITTIPQGLPPSLTELHLDGNKITKVDAASLKGLNNLAKLGLSFNSISAVDNGSLANTPHLRELHLNNNKLVKVPGGLADHKYIQVVYLHNNNISAIGSNDFCPPGYNTKKASYSGVSLFSNPVQYWEIQPSTFRCVYVRAAVQLGNYK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P21793","disprot_id":"DP00489","ncbi_taxon_id":9913,"regions_counter":3,"creator":"aelofsson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":51,"region_id":"DP00489r001","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan. <i> Scott PG, McEwan PA, Dodd CM, Bergmann EM, Bishop PN, Bella J. </i> Proc Natl Acad Sci U S A, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":31,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-30T20:04:13.923Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1XCD"},{"db":"PDB","id":"1XEC"},{"db":"PDB","id":"1XKU"}],"reference_id":"15501918","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"No ordered density was observed for either the 14-aa propeptide (see Supporting Methods) or residues 1-21 of the mature protein, which contain the GAG attachment site.","type":"Methods"}]},{"start":1,"end":14,"reference_id":"15501918","reference_source":"pmid","reference_html":"Crystal structure of the dimeric protein core of decorin, the archetypal small leucine-rich repeat proteoglycan. <i> Scott PG, McEwan PA, Dodd CM, Bergmann EM, Bishop PN, Bella J. </i> Proc Natl Acad Sci U S A, 2004","date":"2022-08-30T20:09:42.794Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00489r003","statement":[{"text":"No ordered density was observed for either the 14-aa propeptide (see Supporting Methods) or residues 1-21 of the mature protein, which contain the GAG attachment site.","type":"Methods"}]}],"released":"2016_10","uniref100":"UniRef100_P21793","date":"2016-09-06T22:37:00.000Z","acc":"P21793","name":"Decorin","length":360,"organism":"Bos taurus","dataset":[],"UniParc":"UPI0000131879","genes":[{"name":{"value":"DCN"}}],"alphafold_very_low_content":0.09444444444444444,"disorder_content":0.09722222222222222,"disprot_consensus":{"full":[{"start":1,"end":14,"type":"D"},{"start":31,"end":51,"type":"D"}],"Structural state":[{"start":1,"end":14,"type":"D"},{"start":31,"end":51,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00017","name":"SH2 domain","start":437,"end":518},{"id":"PF00169","name":"PH domain","start":234,"end":338},{"id":"PF08947","name":"BPS (Between PH and SH2)","start":367,"end":414},{"id":"PF21989","name":"RA like domain","start":104,"end":189}],"gene3D":[{"start":193,"end":353,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":419,"end":538,"id":"3.30.505.10","name":"SH2 domain"},{"start":98,"end":192,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"}]},"uniref50":"UniRef50_O88900","sequence":"MTTSLQDGQSAAGRAGAQDSPLAVQVCRVAQGKGDAQDPAQVPGLHALSPASDATRRGAMDRRKAKDLEVQETPSIPNPFPELCCSPLTSVLSAGLFPRSNSRKKQVIKVYSEDETSRALEVPSDVTARDVCQLLILKNHYVDDNSWTLFEHLSHTGVERTVEDHELLTEVLSHWVMEEDNKLYLRKNYAKYEFFKNPMYFFPEHMVSFATEMNGDRSLTQIPQVFLSSNTYPEIHGFLHAKEQGKKSWKKAYFFLRRSGLYFSTKGTSKEPRHLQFFSEFSTSNVYMSLAGKKKHGAPTPYGFCFKPTKAGGPRDLKMLCAEEDQSRMCWVTAIRLLKYGMQLYQNYMHPSQARSACSSQSVSPMRSVSENSLVAMDFSGQKTRVIDNPTEALSVAVEEGLAWRKKGCLRLGNHGSPTAPSQSSAVNMALHRSQPWFHHRISRDEAQQLITRQGPVDGVFLVRDSQSNPRTFVLSMSHGQKIKHFQIIPVEDDGEVFHTLDDGHTKFTDLIQLVEFYQLNKGVLPCKLKHYCARMAV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_O88900","disprot_id":"DP00490","ncbi_taxon_id":10116,"regions_counter":9,"creator":"aelofsson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":435,"region_id":"DP00490r004","released":"2022_12","ec_id":"ECO:0006210","reference_html":"SAXS study of the PIR domain from the Grb14 molecular adaptor: a natively unfolded protein with a transient structure primer? <i> Moncoq K, Broutin I, Craescu CT, Vachette P, Ducruix A, Durand D. </i> Biophys J, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":361,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-30T20:16:36.158Z","reference_source":"pmid","term_name":"disorder","reference_id":"15465854","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The plot of the PIR pattern, shown in Fig. 2, displays no trace of the bell shape associated with compact, globular particles.","type":"Results"},{"text":"All these observations and simple calculations support the view of PIR as an unfolded molecule with little or no residual structure in solution.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":435,"region_id":"DP00490r007","released":"2022_12","ec_id":"ECO:0006204","reference_html":"SAXS study of the PIR domain from the Grb14 molecular adaptor: a natively unfolded protein with a transient structure primer? <i> Moncoq K, Broutin I, Craescu CT, Vachette P, Ducruix A, Durand D. </i> Biophys J, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":361,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-30T20:18:07.263Z","reference_source":"pmid","term_name":"disorder","reference_id":"15465854","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The CD spectrum of Grb14 PIR exhibits characteristics typical of a random coil, like the large negative ellipticity at 200 nm and the low ellipticity at 185 nm.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_O88900","date":"2016-09-06T21:36:19.000Z","acc":"O88900","name":"Growth factor receptor-bound protein 14","length":538,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI000012BA86","genes":[{"name":{"value":"Grb14"}}],"alphafold_very_low_content":0.26022304832713755,"disorder_content":0.13940520446096655,"disprot_consensus":{"full":[{"start":361,"end":435,"type":"D"}],"Structural state":[{"start":361,"end":435,"type":"D"}]}},{"features":{"pfam":[{"id":"PF05345","name":"Putative Ig domain","start":60,"end":138},{"id":"PF05454","name":"Dystroglycan domain 4","start":605,"end":713},{"id":"PF18424","name":"Alpha-Dystroglycan N-terminal domain 2","start":180,"end":302},{"id":"PF29962","name":"Alpha-Dystroglycan third Ig-like domain","start":491,"end":594}],"gene3D":[{"start":50,"end":163,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":490,"end":601,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":179,"end":313,"id":"3.30.70.1040","name":"Dystroglycan, domain 2"}]},"uniref50":"UniRef50_Q14118","sequence":"MSVDNWLLHPLWGQTFLLLLSVAVAQAHWPSEPSEAVRDWKNQLEASMHSVLSDFQEAVPTVVGIPDGTAVVGRSFRVSIPTDLIASSGEIIKVSAAGKEALPSWLHWDPHSHILEGLPLDTDKGVHYISVSAARLGANGSHVPQTSSVFSIEVYPEDHNEPQSVRAASSDPGEVVPSACAADEPVTVLTVILDADLTKMTPKQRIDLLNRMQSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQNSVPDIRGVETPAREGAMSAQLGYPVVGWHIANKKPTLPKRLRRQIHATPTPVTAIGPPTTAIQEPPSRIVPTPTSPAIAPPTETMAPPVRDPVPGKPTVTIRTRGAIIQTPTLGPIQPTRVSEAGTTVPGQIRPTLTIPGYVEPTAVITPPTTTTKKPRVSTPKPATPSTDSSTTTTRRPTKKPRTPRPVPRVTTKAPITRLETASPPTRIRTTTSGVPRGGEPNQRPELKNHIDRVDAWVGTYFEVKIPSDTFYDNEDTTTDKLKLTLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFMHATDKGGLSAVDAFEIHVHKRPQGDKAPARFKARLAGDPAPVVNDIHKKIALVKKLAFAFGDRNCSSITLQNITRGSIVVEWTNNTLPLEPCPKEQIIGLSRRIADENGKPRPAFSNALEPDFKALSIAVTGSGSCRHLQFIPVAPPSPGSSAAPATEVPDRDPEKSSEDDVYLHTVIPAVVVAAILLIAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSMPETTPLNQDTVGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q14118","disprot_id":"DP00491","ncbi_taxon_id":10090,"regions_counter":8,"creator":"vsagris","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":748,"region_id":"DP00491r001","released":"2022_06","ec_id":"ECO:0006204","reference_html":"Plasticity of secondary structure in the N-terminal region of beta-dystroglycan. <i> Boffi A, Bozzi M, Sciandra F, Woellner C, Bigotti MG, Ilari A, Brancaccio A. </i> Biochim Biophys Acta, 2001","term_id":"IDPO:0000002","curator_id":"fquaglia","start":652,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11257514","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-06-22T13:29:26.541Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The secondary structure content of the N-terminal extracellular domain of beta-dystroglycan (a recombinant fragment extending from positions 654 to 750) has been quantitatively determined by means of CD and FTIR spectroscopies. The elements of secondary structure, namely an 8-10 residue long alpha-helix (10%) and two beta-strands (24%) have been assigned to specific amino acid sequences by means of a GOR constrained prediction method. The remaining 66% of the whole sequence is classified as turns or unordered.","type":"Abstract"}],"sequence_construct":"GSSIVVEWTNNTLPLEPCPKEQIIGLSRRIADENGKPRPAFSNALEPDFKALSIAVTGSGSCRHLQFIPVAPPSPGSSAAPATEVPDRDPEKSSEDDVY","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T12:49:06.340Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":748,"region_id":"DP00491r003","released":"2022_06","ec_id":"ECO:0006228","reference_html":"Plasticity of secondary structure in the N-terminal region of beta-dystroglycan. <i> Boffi A, Bozzi M, Sciandra F, Woellner C, Bigotti MG, Ilari A, Brancaccio A. </i> Biochim Biophys Acta, 2001","term_id":"IDPO:0000003","curator_id":"fquaglia","start":652,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11257514","version":3,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","date":"2022-06-22T13:29:49.756Z","reference_source":"pmid","term_name":"molten globule","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The secondary structure content of the N-terminal extracellular domain of beta-dystroglycan (a recombinant fragment extending from positions 654 to 750) has been quantitatively determined by means of CD and FTIR spectroscopies. The elements of secondary structure, namely an 8-10 residue long alpha-helix (10%) and two beta-strands (24%) have been assigned to specific amino acid sequences by means of a GOR constrained prediction method. The remaining 66% of the whole sequence is classified as turns or unordered.","type":"Abstract"}],"sequence_construct":"GSSIVVEWTNNTLPLEPCPKEQIIGLSRRIADENGKPRPAFSNALEPDFKALSIAVTGSGSCRHLQFIPVAPPSPGSSAAPATEVPDRDPEKSSEDDVY","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T12:48:52.668Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":748,"region_id":"DP00491r005","released":"2022_06","ec_id":"ECO:0006165","reference_html":"Structural characterization by NMR of the natively unfolded extracellular domain of beta-dystroglycan: toward the identification of the binding epitope for alpha-dystroglycan. <i> Bozzi M, Bianchi M, Sciandra F, Paci M, Giardina B, Brancaccio A, Cicero DO. </i> Biochemistry, 2003","statement":[{"text":"All these data provide compelling evidence that  β-DG(654−750) molecules represent an ensemble of different populations of disordered polypeptide chains.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":652,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14622018","version":4,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-06-28T12:35:14.945Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"GSSIVVEWTNNTLPLEPCPKEQIIGLSRRIADENGKPRPAFSNALEPDFKALSIAVTGSGSCRHLQFIPVAPPSPGSSAAPATEVPDRDPEKSSEDDVY","cross_refs":[{"db":"BMRB","id":"5743"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T12:38:41.954Z"}},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":717,"term_name":"protein binding","start":689,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"The binding of β-DG(654−750) to the C-terminal region of the α subunit, α-DG(485−620), has been investigated, showing that the region of β-DG(654−750) between residues 691 and 719 is involved in the interaction.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_06","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"14622018","version":5,"reference_html":"Structural characterization by NMR of the natively unfolded extracellular domain of beta-dystroglycan: toward the identification of the binding epitope for alpha-dystroglycan. <i> Bozzi M, Bianchi M, Sciandra F, Paci M, Giardina B, Brancaccio A, Cicero DO. </i> Biochemistry, 2003","date":"2022-06-22T13:35:50.693Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00491r007","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q62165","operator":"and","partner_start":485,"partner_end":620}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T12:36:22.765Z"}}],"released":"2016_10","uniref100":"UniRef100_Q62165","date":"2016-09-07T11:51:40.000Z","acc":"Q62165","name":"Dystroglycan","length":893,"organism":"Mus musculus","dataset":["Autophagy-related proteins"],"UniParc":"UPI000017C654","genes":[{"name":{"value":"Dag1","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:101864","url":"http://www.informatics.jax.org/marker/MGI:101864"}}]}}],"alphafold_very_low_content":0.3572228443449048,"disorder_content":0.10862262038073908,"disprot_consensus":{"full":[{"start":652,"end":748,"type":"D"}],"Structural state":[{"start":652,"end":748,"type":"D"}],"Molecular function":[{"start":689,"end":717,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00104","name":"Ligand-binding domain of nuclear hormone receptor","start":699,"end":878},{"id":"PF00105","name":"Double treble clef zinc finger, C4 type","start":558,"end":626},{"id":"PF02166","name":"Androgen receptor","start":6,"end":449}],"gene3D":[{"start":551,"end":628,"id":"3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A"},{"start":671,"end":920,"id":"1.10.565.10","name":"Retinoid X Receptor"}]},"uniref50":"UniRef50_P10275","sequence":"MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAASAAPPGASLLLLQQQQQQQQQQQQQQQQQQQQQQQETSPRQQQQQQGEDGSPQAHRRGPTGYLVLDEEQQPSQPQSALECHPERGCVPEPGAAVAASKGLPQQLPAPPDEDDSAAPSTLSLLGPTFPGLSSCSADLKDILSEASTMQLLQQQQQEAVSEGSSSGRAREASGAPTSSKDNYLGGTSTISDNAKELCKAVSVSMGLGVEALEHLSPGEQLRGDCMYAPLLGVPPAVRPTPCAPLAECKGSLLDDSAGKSTEDTAEYSPFKGGYTKGLEGESLGCSGSAAAGSSGTLELPSTLSLYKSGALDEAAAYQSRDYYNFPLALAGPPPPPPPPHPHARIKLENPLDYGSAWAAAAAQCRYGDLASLHGAGAAGPGSGSPSAAASSSWHTLFTAEEGQLYGPCGGGGGGGGGGGGGGGGGGGGGGGEAGAVAPYGYTRPPQGLAGQESDFTAPDVWYPGGMVSRVPYPSPTCVKSEMGPWMDSYSGPYGDMRLETARDHVLPIDYYFPPQKTCLICGDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRNDCTIDKFRRKNCPSCRLRKCYEAGMTLGARKLKKLGNLKLQEEGEASSTTSPTEETTQKLTVSHIEGYECQPIFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAKALPGFRNLHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQITPQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P10275","disprot_id":"DP00492","ncbi_taxon_id":9606,"regions_counter":40,"creator":"tlazar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":485,"region_id":"DP00492r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation. Influence of structure-stabilizing solutes and protein-protein interactions. <i> Reid J, Kelly SM, Watt K, Price NC, McEwan IJ. </i> J Biol Chem, 2002","term_id":"IDPO:0000002","curator_id":"ameszaros","start":142,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"11896058","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-4578-4879","statement":[{"text":"In aqueous solution, the AR polypeptide showed relatively little stable secondary structure. The dominant feature of the CD spectrum was a minimum at around 200 nm, which is characteristic of a non-ordered polypeptide (Fig. 2A). ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-05T08:29:59.555Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":485,"term_name":"disorder to order","start":142,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"ameszaros","released":"2022_03","term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"11896058","version":3,"reference_html":"Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation. Influence of structure-stabilizing solutes and protein-protein interactions. <i> Reid J, Kelly SM, Watt K, Price NC, McEwan IJ. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00492r004","curator_orcid":"0000-0002-4578-4879","statement":[{"text":"In aqueous solution, the AR polypeptide\nshowed relatively little stable secondary structure. The dominant feature of the CD spectrum was a minimum at around 200\nnm, which is characteristic of a non-ordered polypeptide (Fig.\n2A). In contrast, in the presence of increasing amounts of the\nhydrophobic solvent TFE, the CD spectrum was characterized\nby minima at 208 and 222 nm, indicative of a significant\nproportion of alfa-helical structure (Fig. 2A). ","type":"Results"},{"text":"The analysis indicates that the helical content increased from 13 to 40% with a reduction in the turn and other\nstructure contents from 32 to 20% and from 36 to 25%, respectively, as the TFE concentration was increased from 0 to 50%\n(Fig. 2B).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-05T08:30:57.123Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":485,"region_id":"DP00492r006","released":"2022_03","ec_id":"ECO:0001249","reference_html":"Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation. Influence of structure-stabilizing solutes and protein-protein interactions. <i> Reid J, Kelly SM, Watt K, Price NC, McEwan IJ. </i> J Biol Chem, 2002","term_id":"IDPO:0000002","curator_id":"ameszaros","start":142,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"11896058","version":3,"ec_name":"fluorescence evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-4578-4879","statement":[{"text":"The fluorescence spectrum for AR4 is characterized by an emission maximum at 343 nm, due to the tryptophan residues, and a shoulder at 309 nm, resulting from tyrosine emission (Fig. 3A). Fig. 3B shows that in the presence of increasing amounts of acrylamide the fluorescence intensity for the tryptophan maximum after excitation at 295 nm was reduced. From the linear plot, a Stern-Volmer constant (Ksv) of 10.8 M1 was calculated, indicating that both tryptophans have a high degree of exposure to solvent and behave in an identical fashion (35).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-05T08:30:00.517Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":485,"term_name":"disorder to order","start":142,"ec_name":"fluorescence evidence used in manual assertion","curator_id":"ameszaros","released":"2022_03","term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"11896058","version":3,"reference_html":"Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation. Influence of structure-stabilizing solutes and protein-protein interactions. <i> Reid J, Kelly SM, Watt K, Price NC, McEwan IJ. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0001249","region_id":"DP00492r009","curator_orcid":"0000-0002-4578-4879","statement":[{"text":"In the presence of up to 3 M TMAO\nthere was an increase in the quantum yield, the tryptophan\nemission maximum blue shifted to 336 nm, and the shoulder\ndue to tyrosine fluorescence was lost (Fig. 3A). A similar trend\nwas observed with 10 and 20% TFE (data not shown). These\nresults indicate that the two tryptophan residues become less\nsolvent-exposed, and there is an increase in the energy transfer\nfrom tyrosine to tryptophan residues, consistent with the AR\npolypeptide becoming more structured.","type":"Results"},{"text":"Taken together the\nspectroscopy analysis indicates that the AR transactivation\ndomain is structurally flexible and capable of a adopting a more\nfolded conformation in the presence of the alcohol TFE or the\nnatural osmolyte TMAO.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-05T08:30:59.751Z"},"ec_go":"IDA","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":485,"term_name":"molecular adaptor activity","start":142,"ec_name":"cleavage assay evidence used in manual assertion","curator_id":"ameszaros","released":"2022_03","term_ontology":"GO","curator_name":"Attila Meszaros","reference_id":"11896058","version":4,"reference_html":"Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation. Influence of structure-stabilizing solutes and protein-protein interactions. <i> Reid J, Kelly SM, Watt K, Price NC, McEwan IJ. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0007691","region_id":"DP00492r012","curator_orcid":"0000-0002-4578-4879","statement":[{"text":"In the presence of RAP74-CTD\n(amino acids 363–517), the AR polypeptide was markedly less\nsusceptible to cleavage by trypsin (Fig. 7A) and chymotrypsin\n(Fig. 8A).","type":"Results"},{"text":"We interpret these\nresults as providing evidence for at least in part a conformational change in the AR4 polypeptide upon binding of RAP74-\nCTD, which leads to a protease resistant state. ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-05T08:31:40.511Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":485,"term_name":"disorder to order","start":142,"ec_name":"cleavage assay evidence used in manual assertion","curator_id":"ameszaros","released":"2022_03","term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"11896058","version":3,"reference_html":"Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation. Influence of structure-stabilizing solutes and protein-protein interactions. <i> Reid J, Kelly SM, Watt K, Price NC, McEwan IJ. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0007691","region_id":"DP00492r014","curator_orcid":"0000-0002-4578-4879","statement":[{"text":"In the presence of RAP74-CTD\n(amino acids 363–517), the AR polypeptide was markedly less\nsusceptible to cleavage by trypsin (Fig. 7A) and chymotrypsin\n(Fig. 8A).","type":"Results"},{"text":"In the presence of increasing concentrations of TMAO or TFE, AR4 became less susceptible to\ntrypsin cleavage (Fig. 7, B and C).","type":"Results"},{"text":"We interpret these\nresults as providing evidence for at least in part a conformational change in the AR4 polypeptide upon binding of RAP74-\nCTD, which leads to a protease resistant state.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-05T08:31:06.793Z"},"ec_go":"IDA","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":485,"term_name":"protein binding","start":142,"ec_name":"cleavage assay evidence used in manual assertion","curator_id":"ameszaros","released":"2022_03","term_ontology":"GO","curator_name":"Attila Meszaros","reference_id":"11896058","version":4,"reference_html":"Conformational analysis of the androgen receptor amino-terminal domain involved in transactivation. Influence of structure-stabilizing solutes and protein-protein interactions. <i> Reid J, Kelly SM, Watt K, Price NC, McEwan IJ. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007691","region_id":"DP00492r015","curator_orcid":"0000-0002-4578-4879","statement":[{"text":"The GST-AR4 fusion protein was extremely sensitive to proteolytic cleavage, and treatment with trypsin, chymotrypsin, or endoproteinase Glu-C resulted in the generation of a series of stable fragments of relative molecular mass 24,000–30,000 Da, representing the\nGST moiety (Figs. 7 and 8). In the presence of RAP74-CTD (amino acids 363–517), the AR polypeptide was markedly less susceptible to cleavage by trypsin (Fig. 7A) and chymotrypsin (Fig. 8A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-05T08:31:33.872Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":142,"end":485,"reference_id":"15023052","reference_source":"pmid","reference_html":"Induced alpha-helix structure in AF1 of the androgen receptor upon binding transcription factor TFIIF. <i> Kumar R, Betney R, Li J, Thompson EB, McEwan IJ. </i> Biochemistry, 2004","date":"2022-08-17T09:31:07.390Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00492r018","statement":[{"text":"Using Fourier transform infrared (FTIR), we tested whether this interaction can induce structure in the AR AF1. ","type":"Abstract"},{"text":"When the sum of the second-derivative spectra of AF1 and RAP74-CTD are compared with the spectrum of the AF1/RAP74-CTD mixture (Figure 2B), it is evident that the helical content is higher in the AF1/RAP74-CTD mixture than in the summation of the AF1 and RAP74-CTD spectra, suggesting that these changes are not just additive. Comparison of the second-derivative spectra of AF1 with and without RAP74-CTD present indicated a significant increase in helical content in AF1 when mixed with RAP74-CTD (Figure 3A), suggesting that interaction with RAP74-CTD leads to imposition of helical structure on the AF1 domain.","type":"Results"},{"text":"Our results indicate that the AF1 domain has little helical structure until it encounters RAP74. This interaction leads to formation of more helical conformation in AR AF1.  This appears to come as a result of the loss of β-sheet along with an accumulation of small losses of turns, bends, and coil.","type":"Discussion"},{"text":"Our findings herein, showing that AR AF1 adopts a more helical conformation when bound to RAP74, clearly indicate that AF1 can acquire helical structure through an induced-fit mechanism, when it encounters a specific binding partner.","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T19:10:29.357Z"}},{"start":142,"end":485,"reference_id":"15023052","reference_source":"pmid","reference_html":"Induced alpha-helix structure in AF1 of the androgen receptor upon binding transcription factor TFIIF. <i> Kumar R, Betney R, Li J, Thompson EB, McEwan IJ. </i> Biochemistry, 2004","date":"2022-08-17T10:51:31.532Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00492r019","statement":[{"text":"Using Fourier transform infrared (FTIR), we tested whether this interaction can induce structure in the AR AF1. ","type":"Abstract"},{"text":"When the sum of the second-derivative spectra of AF1 and RAP74-CTD are compared with the spectrum of the AF1/RAP74-CTD mixture (Figure 2B), it is evident that the helical content is higher in the AF1/RAP74-CTD mixture than in the summation of the AF1 and RAP74-CTD spectra, suggesting that these changes are not just additive. Comparison of the second-derivative spectra of AF1 with and without RAP74-CTD present indicated a significant increase in helical content in AF1 when mixed with RAP74-CTD (Figure 3A), suggesting that interaction with RAP74-CTD leads to imposition of helical structure on the AF1 domain.","type":"Results"},{"text":"Our results indicate that the AF1 domain has little helical structure until it encounters RAP74. This interaction leads to formation of more helical conformation in AR AF1.  This appears to come as a result of the loss of β-sheet along with an accumulation of small losses of turns, bends, and coil.","type":"Discussion"},{"text":"Our findings herein, showing that AR AF1 adopts a more helical conformation when bound to RAP74, clearly indicate that AF1 can acquire helical structure through an induced-fit mechanism, when it encounters a specific binding partner.","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T19:10:32.144Z"}},{"start":142,"end":485,"reference_id":"15023052","reference_source":"pmid","reference_html":"Induced alpha-helix structure in AF1 of the androgen receptor upon binding transcription factor TFIIF. <i> Kumar R, Betney R, Li J, Thompson EB, McEwan IJ. </i> Biochemistry, 2004","date":"2022-08-17T10:58:19.816Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P35269","operator":null,"partner_start":363,"partner_end":517}],"region_id":"DP00492r020","statement":[{"text":"It has been shown previously that AF1 interacts with transcription factor TFIIF in vitro. Using Fourier transform infrared (FTIR), we tested whether this interaction can induce structure in the AR AF1. ","type":"Abstract"},{"text":"When the sum of the second-derivative spectra of AF1 and RAP74-CTD are compared with the spectrum of the AF1/RAP74-CTD mixture (Figure 2B), it is evident that the helical content is higher in the AF1/RAP74-CTD mixture than in the summation of the AF1 and RAP74-CTD spectra, suggesting that these changes are not just additive. Comparison of the second-derivative spectra of AF1 with and without RAP74-CTD present indicated a significant increase in helical content in AF1 when mixed with RAP74-CTD (Figure 3A), suggesting that interaction with RAP74-CTD leads to imposition of helical structure on the AF1 domain.","type":"Results"},{"text":"Our results indicate that the AF1 domain has little helical structure until it encounters RAP74. This interaction leads to formation of more helical conformation in AR AF1.  This appears to come as a result of the loss of β-sheet along with an accumulation of small losses of turns, bends, and coil.","type":"Discussion"},{"text":"Our findings herein, showing that AR AF1 adopts a more helical conformation when bound to RAP74, clearly indicate that AF1 can acquire helical structure through an induced-fit mechanism, when it encounters a specific binding partner.","type":"Discussion"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T19:10:35.197Z"}},{"start":142,"end":485,"reference_id":"15023052","reference_source":"pmid","reference_html":"Induced alpha-helix structure in AF1 of the androgen receptor upon binding transcription factor TFIIF. <i> Kumar R, Betney R, Li J, Thompson EB, McEwan IJ. </i> Biochemistry, 2004","date":"2022-08-17T11:22:22.128Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001254","ec_ontology":"ECO","ec_name":"radioisotope assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P35269","operator":null,"partner_start":363,"partner_end":517},{"db":"UniProt","id":"Q15788","operator":"and","partner_start":977,"partner_end":1441}],"region_id":"DP00492r021","statement":[{"text":"To test whether induced folding of AR AF1 similarly enhanced coactivator binding, we carried out a series of “pulldown” experiments with the GST−AF1 fusion protein and the radiolabeled SRC-1 C-terminal domain (amino acids 977−1441, SRC-CTD).","type":"Results"},{"text":"Strikingly, a similar enhancement (40-fold) in the level of SRC-CTD binding was observed after preincubation of the GST−AF1 protein with RAP74-CTD.","type":"Results"},{"text":"Our data clearly show that the presence of TMAO and binding of RAP74 each induce a conformation in the AR AF1 domain, which facilitates AF1's interaction with SRC-1.","type":"Discussion"},{"text":"However, it should be emphasized that the main conclusion from the protein−protein interaction data is that preincubation with the binding partner TFIIF (RAP74), but not a noninteracting protein, significantly enhanced the interaction of SRC-CTD. We conclude that conditional folding of the AR AF1 domain is a prerequisite for tight binding of SRC-1 to AF1.","type":"Discussion"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T19:10:34.426Z"}},{"start":142,"end":485,"reference_id":"15023052","reference_source":"pmid","reference_html":"Induced alpha-helix structure in AF1 of the androgen receptor upon binding transcription factor TFIIF. <i> Kumar R, Betney R, Li J, Thompson EB, McEwan IJ. </i> Biochemistry, 2004","date":"2022-08-17T11:26:14.368Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00492r022","statement":[{"text":"As shown in Figure 4, in 3 M TMAO there is a large change in the peak at ∼1656 cm-1, consistent with greatly increased helical content.","type":"Results"},{"text":"TMAO is known to cooperatively fold intrinsically unstructured proteins (9, 31−33) , and cooperative folding of proteins is associated with “native-like” conformations ( 34, 35). This result suggests that the induced AF1 conformation(s) may be physiologically relevant.","type":"Discussion"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":"not relevant","value":3000,"db":"ChEBI","id":"15724","statements":[{"type":"Discussion","text":"TMAO is known to cooperatively fold intrinsically unstructured proteins (9, 31−33) , and cooperative folding of proteins is associated with “native-like” conformations ( 34, 35)."}],"entry_name":"trimethylamine N-oxide"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T19:10:31.214Z"}},{"start":142,"end":485,"reference_id":"18284208","reference_source":"pmid","reference_html":"Structural characterization of the native NH2-terminal transactivation domain of the human androgen receptor: a collapsed disordered conformation underlies structural plasticity and protein-induced folding. <i> Lavery DN, McEwan IJ. </i> Biochemistry, 2008","date":"2022-08-17T11:39:40.887Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001191","ec_ontology":"ECO","ec_name":"in vitro cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00492r023","statement":[{"text":"Native AR-AF1 was rapidly digested by protease treatment, with full-length protein completely digested by 10 to 15 min with trypsin and by 2 min with chymotrypsin, resulting in a stable fragment representing GST (Figure 1 and data not shown).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T19:10:28.128Z"}},{"start":142,"end":485,"reference_id":"18284208","reference_source":"pmid","reference_html":"Structural characterization of the native NH2-terminal transactivation domain of the human androgen receptor: a collapsed disordered conformation underlies structural plasticity and protein-induced folding. <i> Lavery DN, McEwan IJ. </i> Biochemistry, 2008","date":"2022-08-17T11:50:42.829Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00492r024","statement":[{"text":"Purified AR-AF1 was titrated with increasing amounts of ANS which resulted in a hyperbolic curve, and ANS-binding sites appeared saturated above 40 µM (Figure 4A). Incubation of AR-AF1 with ANS resulted in a significant increase in fluorescence intensity and a blue shift for the maximum emission to 465 nm (Figure 4B).","type":"Results"},{"text":"Taken together, these data indicate that AR-AF1 in a native state binds ANS and exhibits ANS binding characteristics similar to those of a well-characterized molten globule state protein.","type":"Results"},{"text":"Second, the fluorescence properties of complexes between AR-AF1 and the hydrophobic probe ANS suggest a partially folded intermediate resembling a pre-molten globule or molten globule state.","type":"Discussion"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":"not relevant","value":null,"db":"ChEBI","id":"39708","statements":[{"type":"Results","text":"In aqueous solution, ANS has limited emission spectra when excited at 370 nm, with an emission maximum at 533 nm, but upon interaction with a molten globule folding state or hydrophobic “patch”, a dramatic enhancement in emission spectra results with a maximum at 480 nm (41, 46)."},{"type":"Results","text":"Purified AR-AF1 was titrated with increasing amounts of ANS which resulted in a hyperbolic curve, and ANS-binding sites appeared saturated above 40 µM (Figure 4A)."}],"entry_name":"8-anilinonaphthalene-1-sulfonic acid"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T19:10:26.984Z"}},{"start":142,"end":485,"reference_id":"18284208","reference_source":"pmid","reference_html":"Structural characterization of the native NH2-terminal transactivation domain of the human androgen receptor: a collapsed disordered conformation underlies structural plasticity and protein-induced folding. <i> Lavery DN, McEwan IJ. </i> Biochemistry, 2008","date":"2022-08-17T11:56:15.167Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00492r025","statement":[{"text":"Coomassie-stained gel of the peak fractions are shown: average elution volume (Ve) for AR-AF1 was calculated to be 57.7 ± 0.6 mL with a gel phase distribution coefficient (Kav) of 0.71 (Figure 6A and data not shown). By comparing these values with those of the standard proteins, we calculated the molecular mass and Stokes radius of AR-AF1 to be 64.7 ± 6.4 kDa and 36.4 ± 1.8 Å, respectively (Figure 6B). These values differ greatly from predicted values (Figure 6B) and strongly suggest AR-AF1 is less compact than a native protein similar in size. Uversky and colleagues have recently collated molecular mass and the Stokes radius for a range of proteins and generated “folding-state” curves for globular, unfolded, molten globule, and pre-molten globule proteins (48, 49, 53).","type":"Results"},{"text":"Figure 6C shows that the predicted molecular mass and Stokes radius for AR-AF1 are positioned on the folding curve for a globular structured protein, but the experimental calculated properties for AR-AF1 place the receptor transactivation domain with proteins in a molten globule state.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T19:10:26.109Z"}},{"start":142,"end":448,"reference_id":"27356095","reference_source":"pmid","reference_html":"EPI-001, A Compound Active against Castration-Resistant Prostate Cancer, Targets Transactivation Unit 5 of the Androgen Receptor. <i> De Mol E, Fenwick RB, Phang CT, Buzón V, Szulc E, de la Fuente A, Escobedo A, García J, Bertoncini CW, Estébanez-Perpiñá E, McEwan IJ, Riera A, Salvatella X. </i> ACS Chem Biol, 2016","date":"2022-08-17T12:37:10.486Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00492r026","statement":[{"text":"In agreement with previous reports based on the use of other biophysical methods, (6) the 1H,15N-HSQC spectrum of AF-1* had the features expected in an ID region such as low HN chemical shift dispersion (Figure 2a).","type":"Results"},{"text":"The results that we obtained indicated the presence of two regions of high helical propensity (defined as ΔδCα–ΔδCβ > 1 ppm and SSP ≈ 0.5, corresponding to a helical propensity of 50%) which correspond to residues 185–200, in Tau-1, and 390–410, in Tau-5. Other regions of intermediate helical propensity (defined as ΔδCα–ΔδCβ ≈ 0.5 ppm and SSP ≈ 0.2) could also be identified, such as the region 230–240, in Tau-1, and 355–365 in Tau-5 (Figure 2b, c). In addition to identifying regions of helical secondary structure, the analysis of the chemical shifts also suggests that residues 144–154 and 270–290 of AF-1* adopt an extended conformation (ΔδCα–ΔδCβ ≈ −0.5 ppm and SSP ≈ −0.3) (Figure 2b, c).","type":"Results"},{"text":"The results that we obtained, presented in Figure 2d, indicate that the regions with nascent secondary structure revealed by the analysis of the 13C chemical shifts (Figure 2b) also display relatively high R2 values. These are especially high, reaching values of ca. 15 s–1, for three regions of sequence found in Tau-5 predicted to have low disorder propensity (26) and presenting, in two cases, high helical propensity.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T19:10:24.948Z"}},{"start":330,"end":448,"reference_id":"33978290","reference_source":"pmid","reference_html":"Low amounts of heavy water increase the phase separation propensity of a fragment of the androgen receptor activation domain. <i> Bielskutė S, Garcia-Cabau C, Frigolé-Vivas M, Szulc E, De Mol E, Pesarrodona M, García J, Salvatella X. </i> Protein Sci, 2021","date":"2023-07-17T14:37:45.225Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP00492r027","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"41981","statements":[{"type":"Title","text":"Low amounts of heavy water increase the phase separation propensity of a fragment of the androgen receptor activation domain"}],"entry_name":"dideuterium oxide"}],"statement":[{"text":"Our results show that the influence of even small amounts of D2O is substantial, changing the cloud point of the ID protein by more than 10°C under solution conditions typical for solution NMR experiments, and that this is likely due to a strengthening of hydrophobic interactions responsible for LCST LLPS.","type":"Introduction"},{"text":"We carried out 1H,15N-BEST-TROSY experiments at concentrations ranging from 25 to 600 μM and observed that the resonances corresponding to a substantial number of residues experienced small but measurable 1HN and 15N chemical shift perturbations as well as decreases in intensity (Figure 2(a)), equivalent to those observed for other phase separating ID proteins under conditions where no phase separation occurs.","type":"Results"},{"text":"The sign of the effect that is, that LCST LLPS is enhanced by heavy water is therefore not a particularly surprising result but the amplitude of the effect, instead, is: we note that the majority of above mentioned studies examined the consequences of replacing H2O with D2O, obtaining measurable but small changes, whereas here we show changes in cloud point as large as 25°C upon replacement of 50% H2O with D2O, that represents a very profound alteration of the phase diagram of an ID protein.","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-27T15:22:33.654Z"}},{"start":330,"end":448,"reference_id":"33978290","reference_source":"pmid","reference_html":"Low amounts of heavy water increase the phase separation propensity of a fragment of the androgen receptor activation domain. <i> Bielskutė S, Garcia-Cabau C, Frigolé-Vivas M, Szulc E, De Mol E, Pesarrodona M, García J, Salvatella X. </i> Protein Sci, 2021","date":"2023-07-17T14:51:40.804Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007056","ec_ontology":"ECO","ec_name":"differential interference contrast microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP00492r028","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"41981","statements":[{"type":"Title","text":"Low amounts of heavy water increase the phase separation propensity of a fragment of the androgen receptor activation domain"}],"entry_name":"dideuterium oxide"}],"statement":[{"text":"We show how replacing even small fractions of H2O with D2O increases the propensity of this fragment to undergo liquid–liquid phase separation, likely reflecting a stabilization of the hydrophobic interactions that drive condensation.","type":"Abstract"},{"text":"We observed that Tau-5* indeed undergoes LLPS, as shown in Figure 1(b), forming droplets capable of fusing (Figure S1). We found however that at equivalent concentrations—in mass per volume units—the AD, composed of 558 residues, has a higher propensity to undergo LLPS than Tau-5*, that contains only 119 residues.","type":"Results"},{"text":"Our results indicate that even modest molar fractions of D2O in a buffer solution can have a substantial effect on the phase diagram of a protein undergoing LCST LLPS.","type":"Discussion"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-27T15:24:17.614Z"}},{"start":142,"end":485,"reference_id":"17073749","reference_source":"pmid","reference_html":"The human androgen receptor AF1 transactivation domain: interactions with transcription factor IIF and molten-globule-like structural characteristics. <i> Lavery DN, McEwan IJ. </i> Biochem Soc Trans, 2006","date":"2023-07-17T15:09:22.769Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006336","ec_ontology":"ECO","ec_name":"intrinsic fluorescence-based protein conformation evidence","unpublished":true,"released":"2023_12","version":0,"region_id":"DP00492r029","statement":[{"text":"Structural flexibility and intrinsic disorder of AR-AF1 were studied using predictive algorithms and fluorescence spectroscopy under different experimental conditions and the results revealed this domain retains characteristics indicative of molten-globule or pre-molten-globule-like structures.","type":"Abstract"},{"text":"Using fluorescence spectroscopy, the λmax for tryptophan emission was found to be intermediate between that expected for a random coil (fully solvent-exposed) and globular structured protein (buried) and the tertiary structure of AR-AF1 could be both stabilized or destabilized by addition of TMAO and urea respectively (Figure 2). Together, these observations suggest that AR-AF1 exists in an unfolded state that is not random coil, but may resemble a molten-globule-like conformation.","type":"Results"},{"text":"Using spectroscopic techniques, we have shown that the structure of AF1 domain can be induced by incubation with TMAO or interestingly RAP74-CTD.","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-27T15:22:27.605Z"}},{"start":144,"end":450,"reference_id":"36229685","reference_source":"pmid","reference_html":"Targeting androgen receptor phase separation to overcome antiandrogen resistance. <i> Xie J, He H, Kong W, Li Z, Gao Z, Xie D, Sun L, Fan X, Jiang X, Zheng Q, Li G, Zhu J, Zhu G. </i> Nat Chem Biol, 2022","date":"2023-07-17T15:31:58.210Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006336","ec_ontology":"ECO","ec_name":"intrinsic fluorescence-based protein conformation evidence","unpublished":true,"released":"2023_12","version":0,"region_id":"DP00492r030","statement":[{"text":"Both structured and unstructured regions of AR contribute to the effective phase separation of AR and disordered N-terminal domain plays a predominant role.","type":"Abstract"},{"text":"The thermal shift results showed that AF-1 is a typical intrinsically disordered protein, which exhibited no obvious emission intensity changes during the heating process; however, incubation with ET516 induced a dose-dependent shift of AF-1 melting temperature (Extended Data Fig. 7e) behaving like a globular protein, suggesting that ET516 binds to a redistributed and stabilized conformational ensemble of AF-1.","type":"Results"},{"text":"Here we comprehensively studied the puncta-forming behavior of AR truncated proteins both in vitro and in vivo (Fig. 2), and found that all AR domains including NTD, DBD and LBD are involved in AR phase separation while the intrinsically disordered NTD plays a predominant role.","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-27T15:22:11.605Z"}},{"start":144,"end":450,"reference_id":"36229685","reference_source":"pmid","reference_html":"Targeting androgen receptor phase separation to overcome antiandrogen resistance. <i> Xie J, He H, Kong W, Li Z, Gao Z, Xie D, Sun L, Fan X, Jiang X, Zheng Q, Li G, Zhu J, Zhu G. </i> Nat Chem Biol, 2022","date":"2023-12-15T13:31:35.052Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006336","ec_ontology":"ECO","ec_name":"intrinsic fluorescence-based protein conformation evidence","unpublished":true,"released":"2023_12","version":1,"region_id":"DP00492r031","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":0.2,"db":"PubChem","id":"CID:165368352","statements":[{"type":"Results","text":"Incubation with ET516 induced a dose-dependent shift of AF-1 melting temperature (Extended Data Fig. 7e) behaving like a globular protein"}]}],"statement":[{"text":"The thermal shift results showed that AF-1 is a typical intrinsically disordered protein, which exhibited no obvious emission intensity changes during the heating process; however, incubation with ET516 induced a dose-dependent shift of AF-1 melting temperature (Extended Data Fig. 7e) behaving like a globular protein, suggesting that ET516 binds to a redistributed and stabilized conformational ensemble of AF-1.","type":"Results"},{"text":"On the basis of the results from thermal shift experiments (Extended Data Fig. 7e) and MD simulation (Extended Data Fig. 7f), ET516 may bind to and stabilize a redistributed AF-1 conformation.","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-15T13:32:47.851Z"}},{"start":144,"end":450,"reference_id":"36229685","reference_source":"pmid","reference_html":"Targeting androgen receptor phase separation to overcome antiandrogen resistance. <i> Xie J, He H, Kong W, Li Z, Gao Z, Xie D, Sun L, Fan X, Jiang X, Zheng Q, Li G, Zhu J, Zhu G. </i> Nat Chem Biol, 2022","date":"2023-07-17T15:47:32.411Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP00492r032","statement":[{"text":"With the aid of PEG3350 that closely simulates the crowding environment, NTD but not DBD or LBD protein, readily formed phase-separated droplets in vitro (Extended Data Fig. 3c), consistent with its predominant LLPS potential in optoDroplets system. FRAP experiments confirmed the liquid-like feature of NTD droplets in vitro (Extended Data Fig. 3d).","type":"Results"},{"text":"Both NLS-fused OptoDroplets system and in vitro LLPS experiments demonstrated that NTD, but not DBD or LBD, possesses the intrinsic LLPS potential (Fig. 2g and Extended Data Fig. 3c).","type":"Discussion"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-27T15:24:30.349Z"}},{"start":144,"end":450,"reference_id":"36229685","reference_source":"pmid","reference_html":"Targeting androgen receptor phase separation to overcome antiandrogen resistance. <i> Xie J, He H, Kong W, Li Z, Gao Z, Xie D, Sun L, Fan X, Jiang X, Zheng Q, Li G, Zhu J, Zhu G. </i> Nat Chem Biol, 2022","date":"2023-09-28T17:09:16.150Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0140694","term_name":"non-membrane-bounded organelle assembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP00492r033","statement":[{"text":"The optoDroplets system fused with NLS and Cry2 is effective to compare the ability of forming nuclear foci for different regions in a more tunable and consistent manner. Time-lapse images showed that blue light induced robust formation of spherical droplets of NTD, while DBD and LBD barely formed droplets (Fig. 2g).","type":"Results"},{"text":"Both NLS-fused OptoDroplets system and in vitro LLPS experiments demonstrated that NTD, but not DBD or LBD, possesses the intrinsic LLPS potential (Fig. 2g and Extended Data Fig. 3c).","type":"Discussion"}],"term_comment":"","term_def":"\"The aggregation, arrangement and bonding together of a set of components to form a non-membrane-bounded organelle.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-27T15:24:35.846Z"}},{"start":1,"end":537,"reference_id":"18762554","reference_source":"pmid","reference_html":"Consequences of poly-glutamine repeat length for the conformation and folding of the androgen receptor amino-terminal domain. <i> Davies P, Watt K, Kelly SM, Clark C, Price NC, McEwan IJ. </i> J Mol Endocrinol, 2008","date":"2023-12-18T14:12:04.281Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006336","ec_ontology":"ECO","ec_name":"intrinsic fluorescence-based protein conformation evidence","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gln78_Gln80del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To measure directly the conformational consequences of changes in the poly-Q amino acid repeat length on the human AR-NTD, we have expressed and purified recombinant polypeptides with 0, 20 or 45 residues."}]}],"region_id":"DP00492r037","statement":[{"text":"The λmax for tryptophan in buffer was 342±2 nm (n=4), which is markedly red shifted to 350 nm in the presence of urea. This is consistent with the tryptophan residues becoming more solvent exposed as the polypeptide chain is unfolded; in addition, a peak was also observed at around 305 nm due to tyrosine residues, indicating less efficient quenching by energy transfer in the unfolded protein (Fig. 2C). These data are consistent with the AR-NTDQ20 having a limited amount of stable folded structure that is lost upon treatment with urea.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:06:25.531Z"}},{"start":1,"end":537,"reference_id":"18762554","reference_source":"pmid","reference_html":"Consequences of poly-glutamine repeat length for the conformation and folding of the androgen receptor amino-terminal domain. <i> Davies P, Watt K, Kelly SM, Clark C, Price NC, McEwan IJ. </i> J Mol Endocrinol, 2008","date":"2023-12-18T14:17:20.535Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006313","ec_ontology":"ECO","ec_name":"urea-induced protein unfolding evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gln78_Gln80del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To measure directly the conformational consequences of changes in the poly-Q amino acid repeat length on the human AR-NTD, we have expressed and purified recombinant polypeptides with 0, 20 or 45 residues."}]}],"region_id":"DP00492r038","statement":[{"text":"The λmax for tryptophan in buffer was 342±2 nm (n=4), which is markedly red shifted to 350 nm in the presence of urea. This is consistent with the tryptophan residues becoming more solvent exposed as the polypeptide chain is unfolded; in addition, a peak was also observed at around 305 nm due to tyrosine residues, indicating less efficient quenching by energy transfer in the unfolded protein (Fig. 2C). These data are consistent with the AR-NTDQ20 having a limited amount of stable folded structure that is lost upon treatment with urea.","type":"Results"},{"text":"Figure 3B shows the loss of ANS fluorescence for each AR-NTD polypeptide with increasing concentrations of urea. All three polypeptides showed non-cooperative unfolding and AR-NTDQ45 was consistently more sensitive to urea denaturation than either the wild-type (Q20) or the AR-NTDΔQ polypeptides. The marked enhancement of ANS fluorescence on binding to the AR-NTD polypeptides taken together with the lack of cooperative unfolding by increasing concentrations of urea indicates that each polypeptide has at least some ‘molten globule’ character with limited stable tertiary structure.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:04:11.629Z"}},{"start":1,"end":537,"reference_id":"18762554","reference_source":"pmid","reference_html":"Consequences of poly-glutamine repeat length for the conformation and folding of the androgen receptor amino-terminal domain. <i> Davies P, Watt K, Kelly SM, Clark C, Price NC, McEwan IJ. </i> J Mol Endocrinol, 2008","date":"2023-12-18T14:22:01.740Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gln78_Gln80del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To measure directly the conformational consequences of changes in the poly-Q amino acid repeat length on the human AR-NTD, we have expressed and purified recombinant polypeptides with 0, 20 or 45 residues."}]}],"region_id":"DP00492r039","statement":[{"text":"Figure 3B shows the loss of ANS fluorescence for each AR-NTD polypeptide with increasing concentrations of urea. All three polypeptides showed non-cooperative unfolding and AR-NTDQ45 was consistently more sensitive to urea denaturation than either the wild-type (Q20) or the AR-NTDΔQ polypeptides. The marked enhancement of ANS fluorescence on binding to the AR-NTD polypeptides taken together with the lack of cooperative unfolding by increasing concentrations of urea indicates that each polypeptide has at least some ‘molten globule’ character with limited stable tertiary structure.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:01:21.482Z"}},{"start":1,"end":537,"reference_id":"18762554","reference_source":"pmid","reference_html":"Consequences of poly-glutamine repeat length for the conformation and folding of the androgen receptor amino-terminal domain. <i> Davies P, Watt K, Kelly SM, Clark C, Price NC, McEwan IJ. </i> J Mol Endocrinol, 2008","date":"2023-12-18T14:27:20.420Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001191","ec_ontology":"ECO","ec_name":"in vitro cleavage assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gln78_Gln80del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To measure directly the conformational consequences of changes in the poly-Q amino acid repeat length on the human AR-NTD, we have expressed and purified recombinant polypeptides with 0, 20 or 45 residues."}]}],"region_id":"DP00492r040","statement":[{"text":"To investigate further the structural implications of poly-Q repeat length on the conformation of the AR-NTD, sensitivity to limited proteolysis was used as a probe for global protein structure. All three polypeptides were sensitive to digestion by endo Glu-C protease, with the full-length protein completely digested between 5 and 15 min (Fig. 4).","type":"Results"},{"text":"Trypsin treatment similarly resulted in digestion of the full-length NTD polypeptides and major N-terminal fragments of 38, 49 and 33 kDa for ARN-Q20, -Q45 and ΔQ respectively (Fig. 5B).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:01:19.309Z"}}],"released":"2016_10","uniref100":"UniRef100_P10275","date":"2016-09-14T10:40:22.000Z","acc":"P10275","name":"Androgen receptor","length":920,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins","Condensates-related proteins"],"UniParc":"UPI000016A2D9","genes":[{"name":{"value":"AR"},"synonyms":[{"value":"DHTR"},{"value":"NR3C4"}]}],"alphafold_very_low_content":0.5804347826086956,"disorder_content":0.5836956521739131,"disprot_consensus":{"full":[{"start":1,"end":141,"type":"D"},{"start":142,"end":485,"type":"T"},{"start":486,"end":537,"type":"D"}],"Structural state":[{"start":1,"end":537,"type":"D"}],"Structural transition":[{"start":142,"end":485,"type":"T"}],"Molecular function":[{"start":142,"end":485,"type":"F"}],"Biological process":[{"start":144,"end":450,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00389","name":"D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain","start":27,"end":123},{"id":"PF00389","name":"D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain","start":307,"end":341},{"id":"PF02826","name":"D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain","start":124,"end":306}],"gene3D":[{"start":114,"end":307,"id":"3.40.50.720","name":"NAD(P)-binding Rossmann-like Domain"},{"start":31,"end":333,"id":"3.40.50.720","name":"NAD(P)-binding Rossmann-like Domain"}]},"uniref50":"UniRef50_P56545","sequence":"MSGVRPPIMNGPMHPRPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGIERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKNCVNKDHLTAATHWASMDPAVVHPELNGAAYSRYPPGVVSVAPTGIPAAVEGIVPSAMSLSHGLPPVAHPPHAPSPGQTVKPEADRDHTTDQL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_Q13363","disprot_id":"DP00499","ncbi_taxon_id":10116,"regions_counter":6,"creator":"aelofsson","regions":[{"start":306,"end":430,"reference_id":"16597837","reference_source":"pmid","reference_html":"The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured. <i> Nardini M, Svergun D, Konarev PV, Spanò S, Fasano M, Bracco C, Pesce A, Donadini A, Cericola C, Secundo F, Luini A, Corda D, Bolognesi M. </i> Protein Sci, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00499r004","statement":[{"text":"In the present communication we apply a combined approach based on bioinformatics, nuclear magnetic resonance, circular dichroism spectroscopy, and small-angle X-ray scattering, and we show that the CtBP C-terminal region is intrinsically unstructured in the full-length CtBP and in constructs lacking the substrate- and/or the nucleotide-binding domains.","type":"Abstract"},{"text":"The C-terminal region of CtBP3 displays sequence and structural features typical of intrinsically unstructured proteins, a property that may be functional to the assembly of CtBP in the core nuclear complex and/or for the recognition of diverse molecular partners.","type":"Introduction"},{"text":"These signals appear to be poorly resolved, mainly due to the reduced spread of amide resonances, falling all in the 7.6–8.7 ppm chemical shift range. This observation usually indicates the absence of structural organization of the backbone (Wüthrich 1986).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":306,"end":430,"reference_id":"16597837","reference_source":"pmid","reference_html":"The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured. <i> Nardini M, Svergun D, Konarev PV, Spanò S, Fasano M, Bracco C, Pesce A, Donadini A, Cericola C, Secundo F, Luini A, Corda D, Bolognesi M. </i> Protein Sci, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00499r005","statement":[{"text":"In the present communication we apply a combined approach based on bioinformatics, nuclear magnetic resonance, circular dichroism spectroscopy, and small-angle X-ray scattering, and we show that the CtBP C-terminal region is intrinsically unstructured in the full-length CtBP and in constructs lacking the substrate- and/or the nucleotide-binding domains.","type":"Abstract"},{"text":"The C-terminal region of CtBP3 displays sequence and structural features typical of intrinsically unstructured proteins, a property that may be functional to the assembly of CtBP in the core nuclear complex and/or for the recognition of diverse molecular partners.","type":"Introduction"},{"text":"The difference spectrum shows a slightly positive trend in the 208–240 nm region, indicating no significant increase of α or β secondary structure in the full-length protein relative to t-CtBP3, and a clear minimum around 200 nm, in the region associated to random coil/unfolded conformation (Hollósi et al. 1993).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":306,"end":430,"reference_id":"16597837","reference_source":"pmid","reference_html":"The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured. <i> Nardini M, Svergun D, Konarev PV, Spanò S, Fasano M, Bracco C, Pesce A, Donadini A, Cericola C, Secundo F, Luini A, Corda D, Bolognesi M. </i> Protein Sci, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"SASBDB","id":"SASDAE4"}],"region_id":"DP00499r006","statement":[{"text":"In the present communication we apply a combined approach based on bioinformatics, nuclear magnetic resonance, circular dichroism spectroscopy, and small-angle X-ray scattering, and we show that the CtBP C-terminal region is intrinsically unstructured in the full-length CtBP and in constructs lacking the substrate- and/or the nucleotide-binding domains.","type":"Abstract"},{"text":"The C-terminal region of CtBP3 displays sequence and structural features typical of intrinsically unstructured proteins, a property that may be functional to the assembly of CtBP in the core nuclear complex and/or for the recognition of diverse molecular partners.","type":"Introduction"},{"text":"The excluded volume (126 ± 10 × 103 Å3) is larger than the value expected for a dimeric construct, which may point to unusual flexibility and high degree of hydration of the overall molecular structure. Remarkably, the values of Rg (56.3 ± 0.7 Å) and Dmax (200 ± 10 Å) exceed those of tetrameric full-length CtBP3, indicating an extremely anisotropic shape for the C-term(2) construct. One can thus conclude that the latter construct must be at least partly unfolded.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q9Z2F5","date":"2016-08-25T16:48:10.000Z","acc":"Q9Z2F5","name":"C-terminal-binding protein 1","length":430,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI000052A256","genes":[{"name":{"value":"Ctbp1"},"synonyms":[{"value":"Bars"},{"value":"Ctbp3"}]}],"alphafold_very_low_content":0.19767441860465115,"disorder_content":0.29069767441860467,"disprot_consensus":{"full":[{"start":306,"end":430,"type":"D"}],"Structural state":[{"start":306,"end":430,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02189","name":"Immunoreceptor tyrosine-based activation motif","start":146,"end":165},{"id":"PF16680","name":"T-cell surface glycoprotein CD3 delta chain","start":30,"end":99}],"gene3D":[{"start":24,"end":92,"id":"2.60.40.10","name":"Immunoglobulins"}]},"uniref50":"UniRef50_P04234","sequence":"MEHSTFLSGLVLATLLSQVSPFKIPIEELEDRVFVNCNTSITWVEGTVGTLLSDITRLDLGKRILDPRGIYRCNGTDIYKDKESTVQVHYRMCQSCVELDPATVAGIIVTDVIATLLLALGVFCFAGHETGRLSGAADTQALLRNDQVYQPLRDRDDAQYSHLGGNWARNK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P04234","disprot_id":"DP00505","ncbi_taxon_id":9606,"regions_counter":7,"creator":"aelofsson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":171,"region_id":"DP00505r002","released":"2022_12","ec_id":"ECO:0006204","reference_html":"Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif. <i> Sigalov A, Aivazian D, Stern L. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":127,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-31T17:19:44.378Z","reference_source":"pmid","term_name":"disorder","reference_id":"14967045","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"CD analysis of CD3εcyt, CD3δcyt, CD3γcyt, FcεRIγcyt, Igαcyt, and Igβcyt showed that these proteins are unstructured, random-coiled proteins. In each case, no detectable secondary or tertiary structure was observed with increasing protein concentration (data not shown).","type":"Results"}]},{"start":127,"end":171,"reference_id":"14967045","reference_source":"pmid","reference_html":"Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif. <i> Sigalov A, Aivazian D, Stern L. </i> Biochemistry, 2004","date":"2022-08-31T17:12:01.343Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00505r005","statement":[{"text":"The gel filtration data indicated that there exists a fast dynamic equilibrium between monomeric and dimeric cytoplasmic domains of all of the ITAM-containing proteins studied, again with the exception of Igαcyt (see below). ","type":"Results"}]},{"start":130,"end":171,"reference_id":"31461748","reference_source":"pmid","reference_html":"Structural basis of assembly of the human T cell receptor-CD3 complex. <i> Dong, Zheng L, Lin J, Zhang B, Zhu Y, Li N, Xie S, Wang Y, Gao N, Huang Z. </i> Nature, 2019","date":"2022-08-31T17:32:52.239Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6JXR"}],"region_id":"DP00505r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20963"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P07766"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P09693"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P01848"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A0K0K1A5"}],"statement":[{"text":"The electron microscopy evidence of the structure of human T cell receptor-CD3 complex shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]},{"start":1,"end":21,"reference_id":"31461748","reference_source":"pmid","reference_html":"Structural basis of assembly of the human T cell receptor-CD3 complex. <i> Dong, Zheng L, Lin J, Zhang B, Zhu Y, Li N, Xie S, Wang Y, Gao N, Huang Z. </i> Nature, 2019","date":"2022-08-31T17:35:54.611Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6JXR"}],"region_id":"DP00505r007","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20963"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P07766"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P09693"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P01848"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A0K0K1A5"}],"statement":[{"text":"The electron microscopy evidence of the structure of human T cell receptor-CD3 complex shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]}],"released":"2016_10","uniref100":"UniRef100_P04234","date":"2016-09-07T12:06:01.000Z","acc":"P04234","name":"T-cell surface glycoprotein CD3 delta chain","length":171,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000127356","genes":[{"name":{"value":"CD3D"},"synonyms":[{"value":"T3D"}]}],"alphafold_very_low_content":0.04678362573099415,"disorder_content":0.38596491228070173,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"},{"start":127,"end":171,"type":"D"}],"Structural state":[{"start":1,"end":21,"type":"D"},{"start":127,"end":171,"type":"D"}],"Disorder function":[{"start":127,"end":171,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02189","name":"Immunoreceptor tyrosine-based activation motif","start":185,"end":204},{"id":"PF16681","name":"Ig-like domain on T-cell surface glycoprotein CD3 epsilon chain","start":36,"end":127}],"gene3D":[{"start":22,"end":126,"id":"2.60.40.10","name":"Immunoglobulins"}]},"uniref50":"UniRef50_P07766","sequence":"MQSGTHWRVLGLCLLSVGVWGQDGNEEMGGITQTPYKVSISGTTVILTCPQYPGSEILWQHNDKNIGGDEDDKNIGSDEDHLSLKEFSELEQSGYYVCYPRGSKPEDANFYLYLRARVCENCMEMDVMSVATIVIVDICITGGLLLLVYYWSKNRKAKAKPVTRGAGAGGRQRGQNKERPPPVPNPDYEPIRKGQRDLYSGLNQRRI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P07766","disprot_id":"DP00506","ncbi_taxon_id":9606,"regions_counter":7,"creator":"gerdos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":11,"region_id":"DP00506r001","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Crystal structure of a human CD3-epsilon/delta dimer in complex with a UCHT1 single-chain antibody fragment. <i> Arnett KL, Harrison SC, Wiley DC. </i> Proc Natl Acad Sci U S A, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-31T20:09:55.765Z","reference_source":"pmid","term_name":"disorder","reference_id":"15534202","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P09693"},{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ABCD","id":"ABCD_AA340","statements":[{"type":"Abstract","text":"We report the crystal structure at 1.9-A resolution of a complex between a human CD3-epsilon/delta ectodomain heterodimer and a single-chain fragment of the UCHT1 antibody."}]}],"statement":[{"text":"Although present in the molecule crystallized, the first 11 residues of CD3-ε had no corresponding electron density.","type":"Methods"}],"cross_refs":[{"db":"PDB","id":"1XIW"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":207,"region_id":"DP00506r002","released":"2022_12","ec_id":"ECO:0006204","reference_html":"Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif. <i> Sigalov A, Aivazian D, Stern L. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":153,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-31T17:10:50.186Z","reference_source":"pmid","term_name":"disorder","reference_id":"14967045","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"CD analysis of CD3εcyt, CD3δcyt, CD3γcyt, FcεRIγcyt, Igαcyt, and Igβcyt showed that these proteins are unstructured, random-coiled proteins. In each case, no detectable secondary or tertiary structure was observed with increasing protein concentration (data not shown).","type":"Results"}]},{"start":153,"end":207,"reference_id":"14967045","reference_source":"pmid","reference_html":"Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif. <i> Sigalov A, Aivazian D, Stern L. </i> Biochemistry, 2004","date":"2022-08-31T17:12:24.271Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00506r005","statement":[{"text":"The gel filtration data indicated that there exists a fast dynamic equilibrium between monomeric and dimeric cytoplasmic domains of all of the ITAM-containing proteins studied, again with the exception of Igαcyt (see below). ","type":"Results"}]},{"start":1,"end":32,"reference_id":"31461748","reference_source":"pmid","reference_html":"Structural basis of assembly of the human T cell receptor-CD3 complex. <i> Dong, Zheng L, Lin J, Zhang B, Zhu Y, Li N, Xie S, Wang Y, Gao N, Huang Z. </i> Nature, 2019","date":"2022-08-31T17:43:24.358Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00506r006","statement":[{"text":"The electron microscopy evidence of the structure of human T cell receptor-CD3 complex shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20963"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04234"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P09693"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P01848"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A0K0K1A5"}],"cross_refs":[{"db":"PDB","id":"6JXR"}]},{"start":157,"end":207,"reference_id":"31461748","reference_source":"pmid","reference_html":"Structural basis of assembly of the human T cell receptor-CD3 complex. <i> Dong, Zheng L, Lin J, Zhang B, Zhu Y, Li N, Xie S, Wang Y, Gao N, Huang Z. </i> Nature, 2019","date":"2022-08-31T17:43:11.683Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6JXR"}],"region_id":"DP00506r007","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20963"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04234"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P09693"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P01848"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A0K0K1A5"}],"statement":[{"text":"The electron microscopy evidence of the structure of human T cell receptor-CD3 complex shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]}],"released":"2016_10","uniref100":"UniRef100_P07766","date":"2016-09-07T11:46:12.000Z","acc":"P07766","name":"T-cell surface glycoprotein CD3 epsilon chain","length":207,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000017704B","genes":[{"name":{"value":"CD3E"},"synonyms":[{"value":"T3E"}]}],"alphafold_very_low_content":0.15942028985507245,"disorder_content":0.42028985507246375,"disprot_consensus":{"full":[{"start":1,"end":32,"type":"D"},{"start":153,"end":207,"type":"D"}],"Structural state":[{"start":1,"end":32,"type":"D"},{"start":153,"end":207,"type":"D"}],"Disorder function":[{"start":153,"end":207,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02189","name":"Immunoreceptor tyrosine-based activation motif","start":157,"end":176},{"id":"PF16680","name":"T-cell surface glycoprotein CD3 delta chain","start":39,"end":110}],"gene3D":[{"start":31,"end":111,"id":"2.60.40.10","name":"Immunoglobulins"}]},"uniref50":"UniRef50_P09693","sequence":"MEQGKGLAVLILAIILLQGTLAQSIKGNHLVKVYDYQEDGSVLLTCDAEAKNITWFKDGKMIGFLTEDKKKWNLGSNAKDPRGMYQCKGSQNKSKPLQVYYRMCQNCIELNAATISGFLFAEIVSIFVLAVGVYFIAGQDGVRQSRASDKQTLLPNDQLYQPLKDREDDQYSHLQGNQLRRN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P09693","disprot_id":"DP00508","ncbi_taxon_id":9606,"regions_counter":7,"creator":"aelofsson","regions":[{"start":139,"end":182,"reference_id":"14967045","reference_source":"pmid","reference_html":"Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif. <i> Sigalov A, Aivazian D, Stern L. </i> Biochemistry, 2004","date":"2022-08-31T17:21:54.325Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00508r004","statement":[{"text":"The gel filtration data indicated that there exists a fast dynamic equilibrium between monomeric and dimeric cytoplasmic domains of all of the ITAM-containing proteins studied, again with the exception of Igαcyt (see below).","type":"Results"}]},{"start":139,"end":182,"reference_id":"14967045","reference_source":"pmid","reference_html":"Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif. <i> Sigalov A, Aivazian D, Stern L. </i> Biochemistry, 2004","date":"2022-08-31T17:22:19.140Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00508r005","statement":[{"text":"CD analysis of CD3εcyt, CD3δcyt, CD3γcyt, FcεRIγcyt, Igαcyt, and Igβcyt showed that these proteins are unstructured, random-coiled proteins. In each case, no detectable secondary or tertiary structure was observed with increasing protein concentration (data not shown).","type":"Results"}]},{"start":1,"end":23,"reference_id":"31461748","reference_source":"pmid","reference_html":"Structural basis of assembly of the human T cell receptor-CD3 complex. <i> Dong, Zheng L, Lin J, Zhang B, Zhu Y, Li N, Xie S, Wang Y, Gao N, Huang Z. </i> Nature, 2019","date":"2022-08-31T17:47:51.994Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6JXR"}],"region_id":"DP00508r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04234 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20963"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P07766"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P01848"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A0K0K1A5"}],"statement":[{"text":"The electron microscopy evidence of the structure of human T cell receptor-CD3 complex shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]},{"start":139,"end":182,"reference_id":"31461748","reference_source":"pmid","reference_html":"Structural basis of assembly of the human T cell receptor-CD3 complex. <i> Dong, Zheng L, Lin J, Zhang B, Zhu Y, Li N, Xie S, Wang Y, Gao N, Huang Z. </i> Nature, 2019","date":"2022-08-31T17:48:10.672Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6JXR"}],"region_id":"DP00508r007","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04234 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20963"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P07766"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P01848"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A0K0K1A5"}],"statement":[{"text":"The electron microscopy evidence of the structure of human T cell receptor-CD3 complex shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]}],"released":"2016_10","uniref100":"UniRef100_P09693","date":"2016-09-07T11:39:33.000Z","acc":"P09693","name":"T-cell surface glycoprotein CD3 gamma chain","length":182,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012735F","genes":[{"name":{"value":"CD3G"},"synonyms":[{"value":"T3G"}]}],"alphafold_very_low_content":0.038461538461538464,"disorder_content":0.36813186813186816,"disprot_consensus":{"full":[{"start":1,"end":23,"type":"D"},{"start":139,"end":182,"type":"D"}],"Structural state":[{"start":1,"end":23,"type":"D"},{"start":139,"end":182,"type":"D"}],"Disorder function":[{"start":139,"end":182,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02189","name":"Immunoreceptor tyrosine-based activation motif","start":62,"end":81},{"id":"PF11628","name":"T-cell surface glycoprotein CD3 zeta chain","start":21,"end":50}]},"uniref50":"UniRef50_P30273","sequence":"MIPAVVLLLLLLVEQAAALGEPQLCYILDAILFLYGIVLTLLYCRLKIQVRKAAITSYEKSDGVYTGLSTRNQETYETLKHEKPPQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P30273","disprot_id":"DP00509","ncbi_taxon_id":9606,"regions_counter":3,"creator":"maspromonte","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":60,"region_id":"DP00509r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif. <i> Sigalov A, Aivazian D, Stern L. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"maspromonte","start":40,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"14967045","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":60,"term_name":"molecular function regulator","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif. <i> Sigalov A, Aivazian D, Stern L. </i> Biochemistry, 2004","term_id":"GO:0098772","curator_id":"maspromonte","start":40,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"14967045","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00509r002","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":60,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif. <i> Sigalov A, Aivazian D, Stern L. </i> Biochemistry, 2004","term_id":"GO:0005515","curator_id":"maspromonte","start":40,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"14967045","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00509r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P30273","date":"2016-09-07T23:23:14.000Z","acc":"P30273","name":"High affinity immunoglobulin epsilon receptor subunit gamma","length":86,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000052756","genes":[{"name":{"value":"FCER1G"}}],"alphafold_very_low_content":0.011627906976744186,"disorder_content":0.2441860465116279,"disprot_consensus":{"full":[{"start":40,"end":60,"type":"D"}],"Structural state":[{"start":40,"end":60,"type":"D"}],"Molecular function":[{"start":40,"end":60,"type":"F"}]}},{"features":{"pfam":[{"id":"PF10195","name":"DNA-binding nuclear phosphoprotein p8","start":22,"end":77}]},"uniref50":"UniRef50_O60356","sequence":"MATFPPATSAPQQPPGPEDEDSSLDESDLYSLAHSYLGGGGRKGRTKREAAANTNRPSPGGHERKLVTKLQNSERKKRGARR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O60356","disprot_id":"DP00510","ncbi_taxon_id":9606,"regions_counter":15,"creator":"aelofsson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":82,"region_id":"DP00510r001","released":"2022_12","ec_id":"ECO:0006204","reference_html":"Human p8 is a HMG-I/Y-like protein with DNA binding activity enhanced by phosphorylation. <i> Encinar JA, Mallo GV, Mizyrycki C, Giono L, Gonzalez-Ros JM, Rico M, Cánepa E, Moreno S, Neira JL, Iovanna JL. </i> J Biol Chem, 2001","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-31T20:30:25.307Z","reference_source":"pmid","term_name":"disorder","reference_id":"11056169","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The spectrum of hp8 at pH 6.0 and 25 °C displays an intense minimum at 205 nm (Fig.3 A) and a shoulder expanding from 220 to 230 nm. Such spectrum resembles, except for the shoulder, that of a random coil structure (17, 18).","type":"Results"},{"text":"The percentage of calculated structure is 2%. Thus, hp8 from the far-UV spectra is mainly random coil.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2025-02-25T20:05:27.957Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":82,"term_name":"DNA binding","released":"2022_12","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","reference_html":"Human p8 is a HMG-I/Y-like protein with DNA binding activity enhanced by phosphorylation. <i> Encinar JA, Mallo GV, Mizyrycki C, Giono L, Gonzalez-Ros JM, Rico M, Cánepa E, Moreno S, Neira JL, Iovanna JL. </i> J Biol Chem, 2001","term_id":"GO:0003677","curator_id":"vnugnes","start":1,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"11056169","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-31T20:53:59.916Z","reference_source":"pmid","ec_id":"ECO:0001807","region_id":"DP00510r002","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"statement":[{"text":"Fig. 10 B shows that DNA binding activity was increased when hp8 recombinant protein was previously phosphorylated by PKA catalytic subunit. A rough estimate of 7-fold increase in affinity can be calculated from the increase in intensity of the complex at similar concentrations of hp8 and PKAhp8 proteins (around 2-fold) and the degree of phosphorylation of PKAhp8, which is around 30% (see before).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2025-02-25T20:05:39.991Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":82,"region_id":"DP00510r005","released":"2022_12","ec_id":"ECO:0006228","reference_html":"Human p8 is a HMG-I/Y-like protein with DNA binding activity enhanced by phosphorylation. <i> Encinar JA, Mallo GV, Mizyrycki C, Giono L, Gonzalez-Ros JM, Rico M, Cánepa E, Moreno S, Neira JL, Iovanna JL. </i> J Biol Chem, 2001","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-31T20:36:30.344Z","reference_source":"pmid","term_name":"disorder","reference_id":"11056169","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The infrared spectrum of nonphosphorylated hp8 (Fig. 4 A) showed an amide I band with a maximum centered near 1644 cm−1, which is characteristic of nonordered conformations.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2025-02-25T20:05:26.240Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":82,"term_name":"phosphorylation display site","released":"2022_12","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","reference_html":"Human p8 is a HMG-I/Y-like protein with DNA binding activity enhanced by phosphorylation. <i> Encinar JA, Mallo GV, Mizyrycki C, Giono L, Gonzalez-Ros JM, Rico M, Cánepa E, Moreno S, Neira JL, Iovanna JL. </i> J Biol Chem, 2001","term_id":"IDPO:0000045","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"11056169","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-31T21:12:14.809Z","reference_source":"pmid","ec_id":"ECO:0006228","region_id":"DP00510r007","ec_go":"EXP","disprot_namespace":"Disorder function","statement":[{"text":"When using unlabeled ATP, protein phosphorylation was checked by observing the 950–1300 cm−1 band of the FTIR spectra (25).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2025-02-25T20:05:35.194Z"}},{"start":1,"end":82,"reference_id":"11056169","reference_source":"pmid","reference_html":"Human p8 is a HMG-I/Y-like protein with DNA binding activity enhanced by phosphorylation. <i> Encinar JA, Mallo GV, Mizyrycki C, Giono L, Gonzalez-Ros JM, Rico M, Cánepa E, Moreno S, Neira JL, Iovanna JL. </i> J Biol Chem, 2001","date":"2022-08-31T20:31:35.025Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006206","ec_ontology":"ECO","ec_name":"near-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00510r009","statement":[{"text":"The near-UV signal of hp8 was null at pH 6.0 and did not change with either the pH or temperature, suggesting the absence of a well fixed structure.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2025-02-25T20:05:24.672Z"}},{"start":1,"end":82,"reference_id":"11056169","reference_source":"pmid","reference_html":"Human p8 is a HMG-I/Y-like protein with DNA binding activity enhanced by phosphorylation. <i> Encinar JA, Mallo GV, Mizyrycki C, Giono L, Gonzalez-Ros JM, Rico M, Cánepa E, Moreno S, Neira JL, Iovanna JL. </i> J Biol Chem, 2001","date":"2022-08-31T20:33:06.193Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00510r010","statement":[{"text":"The lack of a well fixed tertiary structure was also confirmed by fluorescence studies. The fluorescence spectrum of hp8 shows exposed tyrosine residues, with a maximum at 305 nm (data not shown).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2025-02-25T20:05:22.596Z"}},{"start":1,"end":82,"reference_id":"11056169","reference_source":"pmid","reference_html":"Human p8 is a HMG-I/Y-like protein with DNA binding activity enhanced by phosphorylation. <i> Encinar JA, Mallo GV, Mizyrycki C, Giono L, Gonzalez-Ros JM, Rico M, Cánepa E, Moreno S, Neira JL, Iovanna JL. </i> J Biol Chem, 2001","date":"2022-08-31T20:35:46.782Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006230","ec_ontology":"ECO","ec_name":"heat capacity-based evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00510r011","statement":[{"text":"The lack of a well fixed tertiary structure was also confirmed by fluorescence studies. The fluorescence spectrum of hp8 shows exposed tyrosine residues, with a maximum at 305 nm (data not shown).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2025-02-25T20:05:21.367Z"}},{"start":1,"end":82,"reference_id":"11056169","reference_source":"pmid","reference_html":"Human p8 is a HMG-I/Y-like protein with DNA binding activity enhanced by phosphorylation. <i> Encinar JA, Mallo GV, Mizyrycki C, Giono L, Gonzalez-Ros JM, Rico M, Cánepa E, Moreno S, Neira JL, Iovanna JL. </i> J Biol Chem, 2001","date":"2022-08-31T20:38:45.035Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00510r012","statement":[{"text":"The one-dimensional NMR spectra of human hp8 at 5 °C showed small chemical shift dispersion: the amide (Fig. 5 A,left) and the methyl (Fig. 5 A, right) protons were clustered in those regions expected for random coil proteins (24).","type":"Results"},{"text":"Furthermore, the two-dimensional nuclear Overhauser effect spectroscopy experiments showed lack of long-range contacts (data not shown), suggesting the absence of a well fixed tertiary structure.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2025-02-25T20:05:19.372Z"}},{"start":1,"end":82,"reference_id":"11056169","reference_source":"pmid","reference_html":"Human p8 is a HMG-I/Y-like protein with DNA binding activity enhanced by phosphorylation. <i> Encinar JA, Mallo GV, Mizyrycki C, Giono L, Gonzalez-Ros JM, Rico M, Cánepa E, Moreno S, Neira JL, Iovanna JL. </i> J Biol Chem, 2001","date":"2022-08-31T20:55:41.425Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","region_id":"DP00510r013","statement":[{"text":"The spectrum obtained after incubation of PKAhp8 and DNA together was different from that obtained by adding the spectra of both molecules separately.","type":"Results"},{"text":" At 222 nm, the added spectrum showed a more negative ellipticity than that of the complex; conversely, in the region ranging from 225 to 240 nm, the spectrum of the complex showed a lower intensity than that of the added spectrum. These changes suggest that PKAhp8 binds DNA.","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2025-02-25T20:05:33.274Z"}},{"start":1,"end":82,"reference_id":"11056169","reference_source":"pmid","reference_html":"Human p8 is a HMG-I/Y-like protein with DNA binding activity enhanced by phosphorylation. <i> Encinar JA, Mallo GV, Mizyrycki C, Giono L, Gonzalez-Ros JM, Rico M, Cánepa E, Moreno S, Neira JL, Iovanna JL. </i> J Biol Chem, 2001","date":"2022-08-31T21:10:38.225Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001254","ec_ontology":"ECO","ec_name":"radioisotope assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00510r014","statement":[{"text":"The fact that hp8 has a high percentage of serines and threonines prompted us to assay the capacity of being phosphorylated by some of the protein kinases predicted to have putative target sites in hp8. Fig. 6 shows that protein kinase A (PKA) and casein kinase 2 phosphorylated hp8, but that Cdc2k did not.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2025-02-25T20:05:31.484Z"}},{"start":1,"end":82,"reference_id":"11056169","reference_source":"pmid","reference_html":"Human p8 is a HMG-I/Y-like protein with DNA binding activity enhanced by phosphorylation. <i> Encinar JA, Mallo GV, Mizyrycki C, Giono L, Gonzalez-Ros JM, Rico M, Cánepa E, Moreno S, Neira JL, Iovanna JL. </i> J Biol Chem, 2001","date":"2022-08-31T21:11:37.775Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00510r015","statement":[{"text":"Even at highly optimized phosphorylation conditions, only 30% of hp8 could be phosphorylated, assuming that one phosphate was incorporated per molecule; phosphorylation produced the typical shift in electrophoretic mobility of phosphorylated proteins (Fig. 7).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2025-02-25T20:05:29.781Z"}}],"released":"2016_10","uniref100":"UniRef100_O60356","date":"2016-09-07T16:49:29.000Z","acc":"O60356","name":"Nuclear protein 1","length":82,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000013106F","genes":[{"name":{"value":"NUPR1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:29990","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:29990"}}]},"synonyms":[{"value":"COM1"}]}],"alphafold_very_low_content":0.06097560975609756,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":82,"type":"D"}],"Structural state":[{"start":1,"end":82,"type":"D"}],"Molecular function":[{"start":1,"end":82,"type":"F"}],"Disorder function":[{"start":1,"end":82,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00298","name":"Ribosomal protein L11, RNA binding domain","start":63,"end":131},{"id":"PF03946","name":"Ribosomal protein L11, N-terminal domain","start":1,"end":58}],"gene3D":[{"start":64,"end":132,"id":"1.10.10.250","name":"Ribosomal protein L11, C-terminal domain"},{"start":1,"end":63,"id":"3.30.1550.10","name":"Ribosomal protein L11/L12, N-terminal domain"}]},"uniref50":"UniRef50_P56210","sequence":"MKLQIPAGKANPAPPVGPALGQAGVNIMAFCKEFNARTADQAGLIIPVEITVFEDRSFTFITKTPPAAVLLKKAAGIESGSGEPNRNKVATIKRDKVREIAELKMPDLNAASIEAAMRMIEGTARSMGIVVED","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Geobacillus"],"uniref90":"UniRef90_P56210","disprot_id":"DP00512","ncbi_taxon_id":1422,"regions_counter":9,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":87,"region_id":"DP00512r002","released":"2024_06","ec_id":"ECO:0006165","reference_html":"The RNA binding domain of ribosomal protein L11: three-dimensional structure of the RNA-bound form of the protein and its interaction with 23 S rRNA. <i> Hinck AP, Markus MA, Huang S, Grzesiek S, Kustonovich I, Draper DE, Torchia DA. </i> J Mol Biol, 1997","term_id":"IDPO:0000002","curator_id":"vnugnes","start":77,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"9398519","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2024-03-27T13:50:08.600Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"There are, however, two exceptions to this generalization: the six N-terminal residues and residues I20 to N30 in loop 1 both exhibit considerable disorder over the ensemble of calculated structures (Figure 5(a)).","type":"Results"}],"cross_refs":[{"db":"PDB","id":"2FOW"},{"db":"PDB","id":"1FOY"}]},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":87,"term_name":"disorder to order","start":77,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"9398519","version":3,"reference_html":"The RNA binding domain of ribosomal protein L11: three-dimensional structure of the RNA-bound form of the protein and its interaction with 23 S rRNA. <i> Hinck AP, Markus MA, Huang S, Grzesiek S, Kustonovich I, Draper DE, Torchia DA. </i> J Mol Biol, 1997","date":"2024-03-27T13:49:43.127Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00512r003","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS000080DEF4_562"}],"statement":[{"text":"Taken together, these data indicate that loop 1 becomes ordered upon binding to its cognate RNA.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":91,"region_id":"DP00512r005","released":"2024_06","ec_id":"ECO:0006165","reference_html":"High resolution solution structure of ribosomal protein L11-C76, a helical protein with a flexible loop that becomes structured upon binding to RNA. <i> Markus MA, Hinck AP, Huang S, Draper DE, Torchia DA. </i> Nat Struct Biol, 1997","term_id":"IDPO:0000002","curator_id":"vnugnes","start":76,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"8989327","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2024-03-27T13:50:01.240Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1FOX"},{"db":"PDB","id":"1FOW"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Although the structure can be considered high resolution in the core, 15 residues between helix α1 and strand β1 form an extended, unstructured loop.","type":"Abstract"}]},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":91,"term_name":"disorder to order","start":76,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"8989327","version":3,"reference_html":"High resolution solution structure of ribosomal protein L11-C76, a helical protein with a flexible loop that becomes structured upon binding to RNA. <i> Markus MA, Hinck AP, Huang S, Draper DE, Torchia DA. </i> Nat Struct Biol, 1997","date":"2024-03-27T13:48:55.326Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00512r006","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS000080DEF4_562"}],"statement":[{"text":"For L11-C76, the loop between α1 and β1 shows the most striking change in chemical shifts upon binding; for the homeodomain complex, only one contact to the phosphate backbone is made by the loop between helix 1 and helix 2.","type":"Article"}]},{"start":77,"end":87,"reference_id":"9398519","reference_source":"pmid","reference_html":"The RNA binding domain of ribosomal protein L11: three-dimensional structure of the RNA-bound form of the protein and its interaction with 23 S rRNA. <i> Hinck AP, Markus MA, Huang S, Grzesiek S, Kustonovich I, Draper DE, Torchia DA. </i> J Mol Biol, 1997","date":"2024-03-27T13:49:52.058Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019843","term_name":"rRNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","region_id":"DP00512r008","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS000080DEF4_562"}],"statement":[{"text":"The other protein residues that have NOEs to the RNA are S24, E26, and P27 in loop 1. Thus, residues located near the center of loop 1 associate intimately with target RNA. Moreover, the dramatic loop 1 structural and dynamic changes detailed earlier, appear to be the direct result of the interaction of L11-C76 with its target RNA, not merely an indirect structural/dynamic change that accompanies RNA binding.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a ribosomal RNA.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":76,"end":91,"reference_id":"8989327","reference_source":"pmid","reference_html":"High resolution solution structure of ribosomal protein L11-C76, a helical protein with a flexible loop that becomes structured upon binding to RNA. <i> Markus MA, Hinck AP, Huang S, Draper DE, Torchia DA. </i> Nat Struct Biol, 1997","date":"2024-03-27T13:53:04.792Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019843","term_name":"rRNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","region_id":"DP00512r009","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS000080DEF4_562"}],"statement":[{"text":"The flexible loop is important for RNA binding","type":"Article"},{"text":"Chemical shifts differences between the free protein and the bound protein suggest that the loop as well as the C-terminal end of helix α3 are involved in RNA binding. ","type":"Abstract"}],"term_comment":"","term_def":"\"Binding to a ribosomal RNA.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_P56210","date":"2016-09-07T08:14:19.000Z","acc":"P56210","name":"50S ribosomal protein L11","length":133,"organism":"Geobacillus stearothermophilus","dataset":["RNA-binding proteins"],"UniParc":"UPI0000133B70","genes":[{"name":{"value":"rplK","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00736","url":"https://hamap.expasy.org/unirule/MF_00736"}}]}}],"alphafold_very_low_content":0,"disorder_content":0.12030075187969924,"disprot_consensus":{"full":[{"start":76,"end":91,"type":"T"}],"Structural state":[{"start":76,"end":91,"type":"D"}],"Structural transition":[{"start":76,"end":91,"type":"T"}],"Molecular function":[{"start":76,"end":91,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00708","name":"Acylphosphatase","start":18,"end":99}],"gene3D":[{"start":1,"end":101,"id":"3.30.70.100","name":"3.30.70.100"}]},"uniref50":"UniRef50_Q97ZL0","sequence":"MKKWSDTEVFEMLKRMYARVYGLVQGVGFRKFVQIHAIRLGIKGYAKNLPDGSVEVVAEGYEEALSKLLERIKQGPPAAEVEKVDYSFSEYKGEFEDFETY","taxonomy":["Archaea","Crenarchaeota","Thermoprotei","Sulfolobales","Sulfolobaceae","Saccharolobus"],"uniref90":"UniRef90_Q97ZL0","disprot_id":"DP00513","ncbi_taxon_id":273057,"regions_counter":5,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":11,"region_id":"DP00513r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus. <i> Corazza A, Rosano C, Pagano K, Alverdi V, Esposito G, Capanni C, Bemporad F, Plakoutsi G, Stefani M, Chiti F, Zuccotti S, Bolognesi M, Viglino P. </i> Proteins, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16287076","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1Y9O"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":11,"region_id":"DP00513r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus. <i> Corazza A, Rosano C, Pagano K, Alverdi V, Esposito G, Capanni C, Bemporad F, Plakoutsi G, Stefani M, Chiti F, Zuccotti S, Bolognesi M, Viglino P. </i> Proteins, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16287076","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":11,"region_id":"DP00513r003","released":"2022_03","ec_id":"ECO:0006206","reference_html":"Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus. <i> Corazza A, Rosano C, Pagano K, Alverdi V, Esposito G, Capanni C, Bemporad F, Plakoutsi G, Stefani M, Chiti F, Zuccotti S, Bolognesi M, Viglino P. </i> Proteins, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16287076","version":2,"ec_name":"near-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":11,"region_id":"DP00513r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus. <i> Corazza A, Rosano C, Pagano K, Alverdi V, Esposito G, Capanni C, Bemporad F, Plakoutsi G, Stefani M, Chiti F, Zuccotti S, Bolognesi M, Viglino P. </i> Proteins, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16287076","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":11,"region_id":"DP00513r005","released":"2022_03","ec_id":"ECO:0007064","reference_html":"Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus. <i> Corazza A, Rosano C, Pagano K, Alverdi V, Esposito G, Capanni C, Bemporad F, Plakoutsi G, Stefani M, Chiti F, Zuccotti S, Bolognesi M, Viglino P. </i> Proteins, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16287076","version":2,"ec_name":"dynamic light scattering assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q97ZL0","date":"2016-08-16T11:19:37.000Z","acc":"Q97ZL0","name":"Acylphosphatase","length":101,"organism":"Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)","dataset":[],"UniParc":"UPI00000642CB","genes":[{"name":{"value":"acyP"},"olnNames":[{"value":"SSO0887"}]}],"alphafold_very_low_content":0,"disorder_content":0.10891089108910891,"disprot_consensus":{"full":[{"start":1,"end":11,"type":"D"}],"Structural state":[{"start":1,"end":11,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01255","name":"Putative undecaprenyl diphosphate synthase","start":24,"end":244}],"gene3D":[{"start":17,"end":253,"id":"3.40.1180.10","name":"Decaprenyl diphosphate synthase-like"}]},"uniref50":"UniRef50_Q9KPV6","sequence":"MMLSATQPLSEKLPAHGCRHVAIIMDGNGRWAKKQGKIRAFGHKAGAKSVRRAVSFAANNGIEALTLYAFSSENWNRPAQEVSALMELFVWALDSEVKSLHRHNVRLRIIGDTSRFNSRLQERIRKSEALTAGNTGLTLNIAANYGGRWDIVQGVRQLAEKVQQGNLQPDQIDEEMLNQHVCMHELAPVDLVIRTGGEHRISNFLLWQIAYAELYFTDVLWPDFDEQDFEGALNAFANRERRFGGTEPGDETA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P60474","disprot_id":"DP00516","ncbi_taxon_id":83333,"regions_counter":6,"creator":"maspromonte","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":83,"region_id":"DP00516r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli undecaprenyl-pyrophosphate synthase catalysis. <i> Ko TP, Chen YK, Robinson H, Tsai PC, Gao YG, Chen AP, Wang AH, Liang PH. </i> J Biol Chem, 2001","term_id":"IDPO:0000002","curator_id":"maspromonte","start":72,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1V7U"}],"reference_id":"11581264","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":83,"term_name":"small molecule binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli undecaprenyl-pyrophosphate synthase catalysis. <i> Ko TP, Chen YK, Robinson H, Tsai PC, Gao YG, Chen AP, Wang AH, Liang PH. </i> J Biol Chem, 2001","term_id":"GO:0036094","curator_id":"maspromonte","start":72,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"11581264","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00516r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":83,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli undecaprenyl-pyrophosphate synthase catalysis. <i> Ko TP, Chen YK, Robinson H, Tsai PC, Gao YG, Chen AP, Wang AH, Liang PH. </i> J Biol Chem, 2001","term_id":"GO:0005515","curator_id":"maspromonte","start":72,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"11581264","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00516r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":253,"region_id":"DP00516r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Catalytic mechanism revealed by the crystal structure of undecaprenyl pyrophosphate synthase in complex with sulfate, magnesium, and triton. <i> Chang SY, Ko TP, Liang PH, Wang AH. </i> J Biol Chem, 2003","term_id":"IDPO:0000002","curator_id":"maspromonte","start":239,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1V7U"}],"reference_id":"12756244","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":253,"term_name":"small molecule binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Catalytic mechanism revealed by the crystal structure of undecaprenyl pyrophosphate synthase in complex with sulfate, magnesium, and triton. <i> Chang SY, Ko TP, Liang PH, Wang AH. </i> J Biol Chem, 2003","term_id":"GO:0036094","curator_id":"maspromonte","start":239,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"12756244","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00516r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":253,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Catalytic mechanism revealed by the crystal structure of undecaprenyl pyrophosphate synthase in complex with sulfate, magnesium, and triton. <i> Chang SY, Ko TP, Liang PH, Wang AH. </i> J Biol Chem, 2003","term_id":"GO:0005515","curator_id":"maspromonte","start":239,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"12756244","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00516r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P60474","date":"2016-09-08T17:58:30.000Z","acc":"P60472","name":"Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific)","length":253,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI0000137D08","genes":[{"name":{"value":"ispU"},"synonyms":[{"value":"rth"},{"value":"uppS"},{"value":"yaeS"}],"olnNames":[{"value":"b0174"},{"value":"JW0169"}]}],"alphafold_very_low_content":0.043478260869565216,"disorder_content":0.1067193675889328,"disprot_consensus":{"full":[{"start":72,"end":83,"type":"D"},{"start":239,"end":253,"type":"D"}],"Structural state":[{"start":72,"end":83,"type":"D"},{"start":239,"end":253,"type":"D"}],"Molecular function":[{"start":72,"end":83,"type":"F"},{"start":239,"end":253,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00041","name":"Fibronectin type III domain","start":512,"end":600},{"id":"PF00041","name":"Fibronectin type III domain","start":640,"end":729},{"id":"PF00041","name":"Fibronectin type III domain","start":741,"end":827},{"id":"PF00041","name":"Fibronectin type III domain","start":935,"end":1028},{"id":"PF00041","name":"Fibronectin type III domain","start":1041,"end":1128},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":277,"end":369},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":412,"end":486},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":1370,"end":1443},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":1579,"end":1663},{"id":"PF28321","name":"Myomesin-1-like, immunoglobulin-like domain","start":1143,"end":1239}],"gene3D":[{"start":637,"end":741,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":510,"end":632,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1456,"end":1571,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":272,"end":372,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1036,"end":1137,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1244,"end":1358,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1138,"end":1243,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1572,"end":1667,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1359,"end":1447,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":402,"end":505,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":742,"end":836,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":934,"end":1035,"id":"2.60.40.10","name":"Immunoglobulins"}]},"uniref50":"UniRef50_P52179","sequence":"MSLPFYQRCHQHYDLSYRNKDVRSTVSHYQREKKRSAVYTQGSTAYSSRSSAAHRRESEAFRRASASSSQQQASQHALSSEVSRKAASAYDYGSSHGLTDSSLLLDDYSSKLSPKPKRAKHSLLSGEEKENLPSDYMVPIFSGRQKHVSGITDTEEERIKEAAAYIAQRNLLASEEGITTSKQSTASKQTTASKQSTASKQSTASKQSTASRQSTASRQSVVSKQATSALQQEETSEKKSRKVVIREKAERLSLRKTLEETETYHAKLNEDHLLHAPEFIIKPRSHTVWEKENVKLHCSIAGWPEPRVTWYKNQVPINVHANPGKYIIESRYGMHTLEINGCDFEDTAQYRASAMNVKGELSAYASVVVKRYKGEFDETRFHAGASTMPLSFGVTPYGYASRFEIHFDDKFDVSFGREGETMSLGCRVVITPEIKHFQPEIQWYRNGVPLSPSKWVQTLWSGERATLTFSHLNKEDEGLYTIRVRMGEYYEQYSAYVFVRDADAEIEGAPAAPLDVKCLEANKDYIIISWKQPAVDGGSPILGYFIDKCEVGTDSWSQCNDTPVKFARFPVTGLIEGRSYIFRVRAVNKMGIGFPSRVSEPVAALDPAEKARLKSRPSAPWTGQIIVTEEEPSEGIVPGPPTDLSVTEATRSYVVLSWKPPGQRGHEGIMYFVEKCEAGTENWQRVNTELPVKSPRFALFDLAEGKSYCFRVRCSNSAGVGEPSEATEVTVVGDKLDIPKAPGKIIPSRNTDTSVVVSWEESKDAKELVGYYIEASVAGSGKWEPCNNNPVKGSRFTCHGLVTGQSYIFRVRAVNAAGLSEYSQDSEAIEVKAAIGGGVSPDVCPALSDEPGGLTASRGRVHEASPPTFQKDALLGSKPNKPSLPSSSQNLGQTEVSKVSETVQEELTPPPQKAAPQGKSKSDPLKKKTDRAPPSPPCDITCLESFRDSMVLGWKQPDKIGGAEITGYYVNYREVIDGVPGKWREANVKAVSEEAYKISNLKENMVYQFQVAAMNMAGLGAPSAVSECFKCEEWTIAVPGPPHSLKCSEVRKDSLVLQWKPPVHSGRTPVTGYFVDLKEAKAKEDQWRGLNEAAIKNVYLKVRGLKEGVSYVFRVRAINQAGVGKPSDLAGPVVAETRPGTKEVVVNVDDDGVISLNFECDKMTPKSEFSWSKDYVSTEDSPRLEVESKGNKTKMTFKDLGMDDLGIYSCDVTDTDGIASSYLIDEEELKRLLALSHEHKFPTVPVKSELAVEILEKGQVRFWMQAEKLSGNAKVNYIFNEKEIFEGPKYKMHIDRNTGIIEMFMEKLQDEDEGTYTFQLQDGKATNHSTVVLVGDVFKKLQKEAEFQRQEWIRKQGPHFVEYLSWEVTGECNVLLKCKVANIKKETHIVWYKDEREISVDEKHDFKDGICTLLITEFSKKDAGIYEVILKDDRGKDKSRLKLVDEAFKELMMEVCKKIALSATDLKIQSTAEGIQLYSFVTYYVEDLKVNWSHNGSAIRYSDRVKTGVTGEQIWLQINEPTPNDKGKYVMELFDGKTGHQKTVDLSGQAYDEAYAEFQRLKQAAIAEKNRARVLGGLPDVVTIQEGKALNLTCNVWGDPPPEVSWLKNEKALASDDHCNLKFEAGRTAYFTINGVSTADSGKYGLVVKNKYGSETSDFTVSVFIPEEEARMAALESLKGGKKAK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P52179","disprot_id":"DP00517","ncbi_taxon_id":9606,"regions_counter":6,"creator":"wvranken","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":931,"region_id":"DP00517r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Myomesin is a molecular spring with adaptable elasticity. <i> Schoenauer R, Bertoncini P, Machaidze G, Aebi U, Perriard JC, Hegner M, Agarkova I. </i> J Mol Biol, 2005","term_id":"IDPO:0000002","curator_id":"fquaglia","start":836,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15890201","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":931,"term_name":"entropic chain","start":836,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15890201","version":3,"reference_html":"Myomesin is a molecular spring with adaptable elasticity. <i> Schoenauer R, Bertoncini P, Machaidze G, Aebi U, Perriard JC, Hegner M, Agarkova I. </i> J Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0006204","region_id":"DP00517r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":931,"term_name":"entropic chain","start":836,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15890201","version":3,"reference_html":"Myomesin is a molecular spring with adaptable elasticity. <i> Schoenauer R, Bertoncini P, Machaidze G, Aebi U, Perriard JC, Hegner M, Agarkova I. </i> J Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0006204","region_id":"DP00517r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":931,"region_id":"DP00517r004","released":"2022_03","ec_id":"ECO:0001591","reference_html":"Myomesin is a molecular spring with adaptable elasticity. <i> Schoenauer R, Bertoncini P, Machaidze G, Aebi U, Perriard JC, Hegner M, Agarkova I. </i> J Mol Biol, 2005","term_id":"IDPO:0000002","curator_id":"fquaglia","start":836,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15890201","version":2,"ec_name":"atomic force microscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":931,"term_name":"entropic chain","start":836,"ec_name":"atomic force microscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15890201","version":3,"reference_html":"Myomesin is a molecular spring with adaptable elasticity. <i> Schoenauer R, Bertoncini P, Machaidze G, Aebi U, Perriard JC, Hegner M, Agarkova I. </i> J Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0001591","region_id":"DP00517r005","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":931,"term_name":"entropic chain","start":836,"ec_name":"atomic force microscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15890201","version":3,"reference_html":"Myomesin is a molecular spring with adaptable elasticity. <i> Schoenauer R, Bertoncini P, Machaidze G, Aebi U, Perriard JC, Hegner M, Agarkova I. </i> J Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0001591","region_id":"DP00517r006","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_P52179","date":"2016-08-25T17:01:44.000Z","acc":"P52179","name":"Myomesin-1","length":1685,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012FB8B","genes":[{"name":{"value":"MYOM1"}}],"alphafold_very_low_content":0.2747774480712166,"disorder_content":0.05697329376854599,"disprot_consensus":{"full":[{"start":836,"end":931,"type":"D"}],"Structural state":[{"start":836,"end":931,"type":"D"}],"Disorder function":[{"start":836,"end":931,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":523,"end":552},{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":649,"end":689},{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":691,"end":730},{"id":"PF05923","name":"APC repeat","start":1260,"end":1280},{"id":"PF05923","name":"APC repeat","start":1372,"end":1393},{"id":"PF05923","name":"APC repeat","start":1486,"end":1509},{"id":"PF05923","name":"APC repeat","start":1637,"end":1660},{"id":"PF05923","name":"APC repeat","start":1841,"end":1865},{"id":"PF05923","name":"APC repeat","start":1950,"end":1972},{"id":"PF05923","name":"APC repeat","start":2008,"end":2030},{"id":"PF05924","name":"SAMP Motif","start":1567,"end":1588},{"id":"PF05924","name":"SAMP Motif","start":1717,"end":1737},{"id":"PF05924","name":"SAMP Motif","start":2031,"end":2051},{"id":"PF05937","name":"EB-1 Binding Domain","start":2670,"end":2843},{"id":"PF05956","name":"APC basic domain","start":2224,"end":2575},{"id":"PF05972","name":"APC 15 residue motif","start":1020,"end":1034},{"id":"PF05972","name":"APC 15 residue motif","start":1136,"end":1150},{"id":"PF05972","name":"APC 15 residue motif","start":1155,"end":1169},{"id":"PF05972","name":"APC 15 residue motif","start":1172,"end":1186},{"id":"PF11414","name":"Adenomatous polyposis coli tumour suppressor protein","start":134,"end":202},{"id":"PF16629","name":"Armadillo-associated region on APC","start":732,"end":1019},{"id":"PF16630","name":"Unstructured region on APC between 1st and 2nd catenin-bdg motifs","start":1036,"end":1135},{"id":"PF16633","name":"Unstructured region on APC between 1st two creatine-rich regions","start":1282,"end":1368},{"id":"PF16634","name":"Unstructured region on APC between APC_crr and SAMP","start":1662,"end":1715},{"id":"PF16635","name":"Unstructured region on APC between SAMP and APC_crr","start":1746,"end":1839},{"id":"PF16636","name":"Unstructured region on APC between APC_crr regions 5 and 6","start":1867,"end":1947},{"id":"PF16689","name":"Coiled-coil N-terminus of APC, dimerisation domain","start":4,"end":55},{"id":"PF18797","name":"Adenomatous polyposis coli (APC) repeat","start":393,"end":466}],"gene3D":[{"start":326,"end":739,"id":"1.25.10.10","name":"Leucine-rich Repeat Variant"},{"start":2,"end":55,"id":"1.20.5.10","name":"1.20.5.10"},{"start":126,"end":250,"id":"1.10.287.450","name":"Helix hairpin bin"}]},"uniref50":"UniRef50_P25054","sequence":"MAAASYDQLLKQVEALKMENSNLRQELEDNSNHLTKLETEASNMKEVLKQLQGSIEDEAMASSGQIDLLERLKELNLDSSNFPGVKLRSKMSLRSYGSREGSVSSRSGECSPVPMGSFPRRGFVNGSRESTGYLEELEKERSLLLADLDKEEKEKDWYYAQLQNLTKRIDSLPLTENFSLQTDMTRRQLEYEARQIRVAMEEQLGTCQDMEKRAQRRIARIQQIEKDILRIRQLLQSQATEAERSSQNKHETGSHDAERQNEGQGVGEINMATSGNGQGSTTRMDHETASVLSSSSTHSAPRRLTSHLGTKVEMVYSLLSMLGTHDKDDMSRTLLAMSSSQDSCISMRQSGCLPLLIQLLHGNDKDSVLLGNSRGSKEARARASAALHNIIHSQPDDKRGRREIRVLHLLEQIRAYCETCWEWQEAHEPGMDQDKNPMPAPVEHQICPAVCVLMKLSFDEEHRHAMNELGGLQAIAELLQVDCEMYGLTNDHYSITLRRYAGMALTNLTFGDVANKATLCSMKGCMRALVAQLKSESEDLQQVIASVLRNLSWRADVNSKKTLREVGSVKALMECALEVKKESTLKSVLSALWNLSAHCTENKADICAVDGALAFLVGTLTYRSQTNTLAIIESGGGILRNVSSLIATNEDHRQILRENNCLQTLLQHLKSHSLTIVSNACGTLWNLSARNPKDQEALWDMGAVSMLKNLIHSKHKMIAMGSAAALRNLMANRPAKYKDANIMSPGSSLPSLHVRKQKALEAELDAQHLSETFDNIDNLSPKASHRSKQRHKQSLYGDYVFDTNRHDDNRSDNFNTGNMTVLSPYLNTTVLPSSSSSRGSLDSSRSEKDRSLERERGIGLGNYHPATENPGTSSKRGLQISTTAAQIAKVMEEVSAIHTSQEDRSSGSTTELHCVTDERNALRRSSAAHTHSNTYNFTKSENSNRTCSMPYAKLEYKRSSNDSLNSVSSSDGYGKRGQMKPSIESYSEDDESKFCSYGQYPADLAHKIHSANHMDDNDGELDTPINYSLKYSDEQLNSGRQSPSQNERWARPKHIIEDEIKQSEQRQSRNQSTTYPVYTESTDDKHLKFQPHFGQQECVSPYRSRGANGSETNRVGSNHGINQNVSQSLCQEDDYEDDKPTNYSERYSEEEQHEEEERPTNYSIKYNEEKRHVDQPIDYSLKYATDIPSSQKQSFSFSKSSSGQSSKTEHMSSSSENTSTPSSNAKRQNQLHPSSAQSRSGQPQKAATCKVSSINQETIQTYCVEDTPICFSRCSSLSSLSSAEDEIGCNQTTQEADSANTLQIAEIKEKIGTRSAEDPVSEVPAVSQHPRTKSSRLQGSSLSSESARHKAVEFSSGAKSPSKSGAQTPKSPPEHYVQETPLMFSRCTSVSSLDSFESRSIASSVQSEPCSGMVSGIISPSDLPDSPGQTMPPSRSKTPPPPPQTAQTKREVPKNKAPTAEKRESGPKQAAVNAAVQRVQVLPDADTLLHFATESTPDGFSCSSSLSALSLDEPFIQKDVELRIMPPVQENDNGNETESEQPKESNENQEKEAEKTIDSEKDLLDDSDDDDIEILEECIISAMPTKSSRKAKKPAQTASKLPPPVARKPSQLPVYKLLPSQNRLQPQKHVSFTPGDDMPRVYCVEGTPINFSTATSLSDLTIESPPNELAAGEGVRGGAQSGEFEKRDTIPTEGRSTDEAQGGKTSSVTIPELDDNKAEEGDILAECINSAMPKGKSHKPFRVKKIMDQVQQASASSSAPNKNQLDGKKKKPTSPVKPIPQNTEYRTRVRKNADSKNNLNAERVFSDNKDSKKQNLKNNSKVFNDKLPNNEDRVRGSFAFDSPHHYTPIEGTPYCFSRNDSLSSLDFDDDDVDLSREKAELRKAKENKESEAKVTSHTELTSNQQSANKTQAIAKQPINRGQPKPILQKQSTFPQSSKDIPDRGAATDEKLQNFAIENTPVCFSHNSSLSSLSDIDQENNNKENEPIKETEPPDSQGEPSKPQASGYAPKSFHVEDTPVCFSRNSSLSSLSIDSEDDLLQECISSAMPKKKKPSRLKGDNEKHSPRNMGGILGEDLTLDLKDIQRPDSEHGLSPDSENFDWKAIQEGANSIVSSLHQAAAAACLSRQASSDSDSILSLKSGISLGSPFHLTPDQEEKPFTSNKGPRILKPGEKSTLETKKIESESKGIKGGKKVYKSLITGKVRSNSEISGQMKQPLQANMPSISRGRTMIHIPGVRNSSSSTSPVSKKGPPLKTPASKSPSEGQTATTSPRGAKPSVKSELSPVARQTSQIGGSSKAPSRSGSRDSTPSRPAQQPLSRPIQSPGRNSISPGRNGISPPNKLSQLPRTSSPSTASTKSSGSGKMSYTSPGRQMSQQNLTKQTGLSKNASSIPRSESASKGLNQMNNGNGANKKVELSRMSSTKSSGSESDRSERPVLVRQSTFIKEAPSPTLRRKLEESASFESLSPSSRPASPTRSQAQTPVLSPSLPDMSLSTHSSVQAGGWRKLPPNLSPTIEYNDGRPAKRHDIARSHSESPSRLPINRSGTWKREHSKHSSSLPRVSTWRRTGSSSSILSASSESSEKAKSEDEKHVNSISGTKQSKENQVSAKGTWRKIKENEFSPTNSTSQTVSSGATNGAESKTLIYQMAPAVSKTEDVWVRIEDCPINNPRSGRSPTGNTPPVIDSVSEKANPNIKDSKDNQAKQNVGNGSVPMRTVGLENRLNSFIQVDAPDQKGTEIKPGQNNPVPVSETNESSIVERTPFSSSSSSKHSSPSGTVAARVTPFNYNPSPRKSSADSTSARPSQIPTPVNNNTKKRDSKTDSTESSGTQSPKRHSGSYLVTSV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P25054","disprot_id":"DP00519","ncbi_taxon_id":9606,"regions_counter":28,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1745,"region_id":"DP00519r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The third 20 amino acid repeat is the tightest binding site of APC for beta-catenin. <i> Liu J, Xing Y, Hinds TR, Zheng J, Xu W. </i> J Mol Biol, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1362,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16753179","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In addition, our CD and NMR studies demonstrate that the central region of APC is unstructured in the absence of beta-catenin and Axin, and suggest that beta-catenin may interact with each of the APC 15aa and 20aa repeats independently.","type":"Abstract"},{"text":"To determine if the central region of APC has a defined secondary structure, the CD spectra of various purified APC fragments, including APC-R2-R3 and APC-R2-R4, were measured. The CD spectra measured for APC-R2-R4 at 4 °C and 25 °C are essentially identical and feature a single minimum in molar residue ellipticity at ∼200 nm (Figure 3(b)). These spectra, as well as the CD spectra for other APC fragments (data not shown), indicate that all these APC fragments are mostly unstructured.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:23:08.140Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1745,"region_id":"DP00519r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The third 20 amino acid repeat is the tightest binding site of APC for beta-catenin. <i> Liu J, Xing Y, Hinds TR, Zheng J, Xu W. </i> J Mol Biol, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1362,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16753179","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In addition, our CD and NMR studies demonstrate that the central region of APC is unstructured in the absence of beta-catenin and Axin, and suggest that beta-catenin may interact with each of the APC 15aa and 20aa repeats independently.","type":"Abstract"},{"text":"To exclude the possibility that the APC fragment has a defined structure without regular secondary structure, we measured both 1D and 2D NMR spectra of APC-R2-R4, the longest APC fragment that we were able to obtain in large quantity and that has good solubility. 1D NMR shows no obvious chemical shift signal from 5.5 ppm to 8.5 ppm. The poor dispersion of the resonances indicates that the fragment does not have a folded structure (Figure 3(c)). This lack of folded conformation is also demonstrated in the 2D Nuclear Overhauser Effect (NOE) spectra; there is no inter-residue NOE observed in the 2D-NOESY spectrum, which is characteristic of an unfolded structure (data not shown).","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:23:06.427Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q15691","partner_end":null}],"ec_ontology":"ECO","end":2819,"region_id":"DP00519r005","reference_id":"19632184","start":2781,"term_id":"GO:0005515","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The effect of phosphorylation at these sites on binding to the C-terminal domain of EB1 (EB1c) was assessed in vitro by isothermal titration calorimetry (ITC) with a polypeptide corresponding to the sequence of APC39 (APCp1; Bu and Su, 2003, Honnappa et al., 2005). ITC revealed that two APCp1 peptides bind to one EB1c dimer, with an equilibrium dissociation constant, Kd, of 5.8 ± 0.1 μM (Figure S5), consistent with previous findings (Honnappa et al., 2005). Peptides phosphorylated at Ser2789 (Honnappa et al., 2005) or Ser2793 (Figure S5) showed ∼4- and ∼6-fold reduced affinity for EB1c when compared to the wild-type peptide.","type":"Results"}],"curator_id":"vnugnes","released":"2022_12","term_ontology":"GO","curator_name":"Victoria Nugnes","ec_name":"isothermal titration calorimetry evidence used in manual assertion","version":6,"reference_html":"An EB1-binding motif acts as a microtubule tip localization signal. <i> Honnappa S, Gouveia SM, Weisbrich A, Damberger FF, Bhavesh NS, Jawhari H, Grigoriev I, van Rijssel FJ, Buey RM, Lawera A, Jelesarov I, Winkler FK, Wüthrich K, Akhmanova A, Steinmetz MO. </i> Cell, 2009","date":"2022-08-08T20:01:23.077Z","reference_source":"pmid","ec_id":"ECO:0005647","term_name":"protein binding","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":2789,"end":2789,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":2793,"end":2793,"position":"Specific residue"}],"cross_refs":[{"db":"ELM","id":"LIG_SxIP_EBH_1"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:26:21.612Z"}},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q15691","partner_end":null}],"ec_ontology":"ECO","end":2809,"region_id":"DP00519r007","reference_id":"19632184","start":2803,"term_id":"GO:0005515","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In order to determine whether the structural features observed in the EB1cΔC8-MACFp1 complex apply more generally to EB1-mediated +TIP interactions, we performed nuclear magnetic resonance (NMR) experiments on the EB1c-APCp1 complex. 15N{1H}-NOEs demonstrate that whereas APCp1 is unstructured in solution (not shown), the segment 2784–2813 is ordered in the complex with EB1c (Figure 6A). Chemical shift changes and intermolecular 1H-1H NOEs identify residues 2803–2809 encompassing the SxIP motif as a major interaction site, with secondary interactions at residues 2789–2799 (Figure 6A; Figure S7). The remainder of the APCp1 polypeptide is disordered even in the bound state.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":4,"reference_html":"An EB1-binding motif acts as a microtubule tip localization signal. <i> Honnappa S, Gouveia SM, Weisbrich A, Damberger FF, Bhavesh NS, Jawhari H, Grigoriev I, van Rijssel FJ, Buey RM, Lawera A, Jelesarov I, Winkler FK, Wüthrich K, Akhmanova A, Steinmetz MO. </i> Cell, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"protein binding","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:23:14.243Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q15691","partner_end":null}],"ec_ontology":"ECO","end":2799,"region_id":"DP00519r008","reference_id":"19632184","start":2789,"term_id":"GO:0005515","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In order to determine whether the structural features observed in the EB1cΔC8-MACFp1 complex apply more generally to EB1-mediated +TIP interactions, we performed nuclear magnetic resonance (NMR) experiments on the EB1c-APCp1 complex. 15N{1H}-NOEs demonstrate that whereas APCp1 is unstructured in solution (not shown), the segment 2784–2813 is ordered in the complex with EB1c (Figure 6A). Chemical shift changes and intermolecular 1H-1H NOEs identify residues 2803–2809 encompassing the SxIP motif as a major interaction site, with secondary interactions at residues 2789–2799 (Figure 6A; Figure S7). The remainder of the APCp1 polypeptide is disordered even in the bound state.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":4,"reference_html":"An EB1-binding motif acts as a microtubule tip localization signal. <i> Honnappa S, Gouveia SM, Weisbrich A, Damberger FF, Bhavesh NS, Jawhari H, Grigoriev I, van Rijssel FJ, Buey RM, Lawera A, Jelesarov I, Winkler FK, Wüthrich K, Akhmanova A, Steinmetz MO. </i> Cell, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"protein binding","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:23:12.829Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":2819,"region_id":"DP00519r009","reference_id":"19632184","start":2781,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In order to determine whether the structural features observed in the EB1cΔC8-MACFp1 complex apply more generally to EB1-mediated +TIP interactions, we performed nuclear magnetic resonance (NMR) experiments on the EB1c-APCp1 complex. 15N{1H}-NOEs demonstrate that whereas APCp1 is unstructured in solution (not shown), the segment 2784–2813 is ordered in the complex with EB1c (Figure 6A). Chemical shift changes and intermolecular 1H-1H NOEs identify residues 2803–2809 encompassing the SxIP motif as a major interaction site, with secondary interactions at residues 2789–2799 (Figure 6A; Figure S7). The remainder of the APCp1 polypeptide is disordered even in the bound state.","type":"Results"},{"text":"APCp1 corresponds to region Val2781-Lys2819 of human APC.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"reference_html":"An EB1-binding motif acts as a microtubule tip localization signal. <i> Honnappa S, Gouveia SM, Weisbrich A, Damberger FF, Bhavesh NS, Jawhari H, Grigoriev I, van Rijssel FJ, Buey RM, Lawera A, Jelesarov I, Winkler FK, Wüthrich K, Akhmanova A, Steinmetz MO. </i> Cell, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:23:05.447Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":2813,"region_id":"DP00519r010","reference_id":"19632184","start":2784,"term_id":"IDPO:0000011","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In order to determine whether the structural features observed in the EB1cΔC8-MACFp1 complex apply more generally to EB1-mediated +TIP interactions, we performed nuclear magnetic resonance (NMR) experiments on the EB1c-APCp1 complex. 15N{1H}-NOEs demonstrate that whereas APCp1 is unstructured in solution (not shown), the segment 2784–2813 is ordered in the complex with EB1c (Figure 6A). Chemical shift changes and intermolecular 1H-1H NOEs identify residues 2803–2809 encompassing the SxIP motif as a major interaction site, with secondary interactions at residues 2789–2799 (Figure 6A; Figure S7). The remainder of the APCp1 polypeptide is disordered even in the bound state.","type":"Results"},{"text":"APCp1 corresponds to region Val2781-Lys2819 of human APC.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"reference_html":"An EB1-binding motif acts as a microtubule tip localization signal. <i> Honnappa S, Gouveia SM, Weisbrich A, Damberger FF, Bhavesh NS, Jawhari H, Grigoriev I, van Rijssel FJ, Buey RM, Lawera A, Jelesarov I, Winkler FK, Wüthrich K, Akhmanova A, Steinmetz MO. </i> Cell, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder to order","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:23:08.965Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":1459,"end":1532,"reference_id":"16753179","reference_source":"pmid","reference_html":"The third 20 amino acid repeat is the tightest binding site of APC for beta-catenin. <i> Liu J, Xing Y, Hinds TR, Zheng J, Xu W. </i> J Mol Biol, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P35222","partner_start":null,"partner_end":null}],"region_id":"DP00519r011","statement":[{"text":"Despite the sequence homology, each of the seven 20aa repeats binds to β-catenin with dramatically different affinities. When unphosphorylated, APC-R3 can bind β-catenin with a Kd of ∼0.2 μM. The binding of β-catenin with every other unphosphorylated 20aa repeat is at least 60 times weaker than APC-R3, and unlikely to interact with β-catenin at physiological conditions (see Discussion).","type":"Results"},{"text":"However, APC-R3 is obviously the repeat having the highest affinity with β-catenin in both phosphorylated and unphosphorylated states.","type":"Results"},{"text":"The APC-rBC fragment interacts with two β-catenin molecules, indicating each 15aa repeat binds to one β-catenin molecule. In addition, APC-R2-R4 also interacts with two molecules of β-catenin, indicating that both APC-R3 and APC-R4, but not APC-R2, interact with one molecule of β-catenin simutaneously (Table 1). Thus our ITC study confirms the binding stoichiometry of one β-catenin binding repeat of APC to one β-catenin molecule.","type":"Results"},{"text":"This region corresponds to APC repeat 3 (APC-R3, residues 1459–1532).","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:23:11.728Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1614,"end":1679,"reference_id":"16753179","reference_source":"pmid","reference_html":"The third 20 amino acid repeat is the tightest binding site of APC for beta-catenin. <i> Liu J, Xing Y, Hinds TR, Zheng J, Xu W. </i> J Mol Biol, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P35222","partner_start":null,"partner_end":null}],"region_id":"DP00519r012","statement":[{"text":"The APC-rBC fragment interacts with two β-catenin molecules, indicating each 15aa repeat binds to one β-catenin molecule. In addition, APC-R2-R4 also interacts with two molecules of β-catenin, indicating that both APC-R3 and APC-R4, but not APC-R2, interact with one molecule of β-catenin simutaneously (Table 1). Thus our ITC study confirms the binding stoichiometry of one β-catenin binding repeat of APC to one β-catenin molecule.","type":"Results"},{"text":"This region corresponds to APC repeat 4 (APC-R4, residues 1614–1679).","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:23:10.520Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1202,"end":1551,"reference_id":"24130866","reference_source":"pmid","reference_html":"Large extent of disorder in Adenomatous Polyposis Coli offers a strategy to guard Wnt signalling against point mutations. <i> Minde DP, Radli M, Forneris F, Maurice MM, Rüdiger SG. </i> PLoS One, 2013","date":"2022-07-25T13:23:35.706Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001191","ec_ontology":"ECO","ec_name":"in vitro cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00519r014","statement":[{"text":"The two intrinsically disordered proteins (IDPs) AxinCR and β-caseine, however, were entirely digested at low TL concentration (0.001 g/L). Likewise, the band of APC-MCR disappeared at this TL concentration. We conclude that protease susceptibility of APC-MCR is similar to that of the IDPs Axin-CR and β-caseine.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:26:14.264Z"}},{"start":1202,"end":1551,"reference_id":"24130866","reference_source":"pmid","reference_html":"Large extent of disorder in Adenomatous Polyposis Coli offers a strategy to guard Wnt signalling against point mutations. <i> Minde DP, Radli M, Forneris F, Maurice MM, Rüdiger SG. </i> PLoS One, 2013","date":"2022-07-25T13:42:48.953Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00519r015","statement":[{"text":"In non-denaturing buffer and absence of TFE, we observed a minimum near 200 nm and absence of a negative peak at 220 nm indicating low α-helical structure content (Figure 3) [41].","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:15:22.401Z"}},{"start":1202,"end":1551,"reference_id":"24130866","reference_source":"pmid","reference_html":"Large extent of disorder in Adenomatous Polyposis Coli offers a strategy to guard Wnt signalling against point mutations. <i> Minde DP, Radli M, Forneris F, Maurice MM, Rüdiger SG. </i> PLoS One, 2013","date":"2022-07-25T13:47:31.016Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00519r016","statement":[{"text":"We observed a linear decrease of fluorescence emission with increasing temperature, as it is typical for protein in the absence of global conformational changes (Figure 4A,B,C) [42]. We neither detected any thermally induced transition nor temperature-dependent changes in the spectral shape (Figure 4A, B). We conclude that temperature increase does not induce a structural transition that changes the environment of the intrinsic fluorescence probes in APC-MCR.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:15:24.978Z"}},{"start":1202,"end":1551,"reference_id":"24130866","reference_source":"pmid","reference_html":"Large extent of disorder in Adenomatous Polyposis Coli offers a strategy to guard Wnt signalling against point mutations. <i> Minde DP, Radli M, Forneris F, Maurice MM, Rüdiger SG. </i> PLoS One, 2013","date":"2022-07-25T13:49:25.550Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00519r017","statement":[{"text":"The elution time of APC-MCR corresponded to an apparent molecular weight of 200 kDa, 5-fold larger than expected based on its molecular weight of 40 kDa (Figure 5A,B). We conclude that APC-MCR is either predominantly extended or oligomeric.","type":"Results"},{"text":"The protein eluted as a single monomeric peak with a molecular mass of 44.4 ± 4.0 kDa. We conclude that APC-MCR is an extended intrinsically disordered region.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:15:28.400Z"}},{"start":1202,"end":1551,"reference_id":"24130866","reference_source":"pmid","reference_html":"Large extent of disorder in Adenomatous Polyposis Coli offers a strategy to guard Wnt signalling against point mutations. <i> Minde DP, Radli M, Forneris F, Maurice MM, Rüdiger SG. </i> PLoS One, 2013","date":"2022-08-08T19:58:30.469Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019901","term_name":"protein kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001202","ec_ontology":"ECO","ec_name":"in vitro protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P49674","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00519r018","statement":[{"text":"In the presence of ATP and CK1ε, we incubated APC-MCR for up to 16 h and subsequently probed for an eventual change in migration pattern on SDS-PAGE. Additional negative charges locally prevent binding of SDS and, therefore, reduce mobility of the phosphorylated protein in the gel [21,44-47].","type":"Results"},{"text":"Our results demonstrate that APC-MCR can be phosphorylated by CK1ε.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"cross_refs":[{"db":"ELM","id":"MOD_CDK_SPxK_1"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:26:28.849Z"}},{"start":1484,"end":1528,"reference_id":"15327768","reference_source":"pmid","reference_html":"Mechanism of phosphorylation-dependent binding of APC to beta-catenin and its role in beta-catenin degradation. <i> Ha NC, Tonozuka T, Stamos JL, Choi HJ, Weis WI. </i> Mol Cell, 2004","date":"2022-07-25T15:45:02.310Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008013","term_name":"beta-catenin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q02248","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00519r019","statement":[{"text":"Unexpectedly, we were unable to detect binding of purified β-catenin arm repeat domain to GST-R7 immobilized on glutathione agarose beads, whereas robust binding was seen to GST-R3 (data not shown). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a catenin beta subunit.\" [GOC:bf]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:17:16.491Z"}},{"start":1485,"end":1498,"reference_id":"15327768","reference_source":"pmid","reference_html":"Mechanism of phosphorylation-dependent binding of APC to beta-catenin and its role in beta-catenin degradation. <i> Ha NC, Tonozuka T, Stamos JL, Choi HJ, Weis WI. </i> Mol Cell, 2004","date":"2022-07-25T19:14:31.046Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008013","term_name":"beta-catenin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser1501Asp","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser1505Asp","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser1507Asp","start":null,"end":null,"position":null}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P35222","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00519r021","sequence_construct":"DADTLLHFATESTPDGFDCSSDLDALSLDEPFIQKDVELRIMPPVQ","statement":[{"text":"Both this triple Ser→Asp mutant, designated R3-tripleD, and the wild-type construct were used for cocrystallization trials with β-ARM.","type":"Results"},{"text":"Crystals were obtained only with the R3-tripleD (Table 1). Only 14 of the 47 residues of the APC construct are visible in the final electron density map. The final model consists of β-catenin residues 146-549 and 559-664, ICAT 8-53, and APC 1485-1498.","type":"Results"},{"text":"R3-tripleD corresponds to the APC peptide with the mutations S1501D, S1505D, and S1507D.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a catenin beta subunit.\" [GOC:bf]","term_is_obsolete":false,"term_not_annotate":false,"cross_refs":[{"db":"PDB","id":"1T08"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NSA3"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:17:18.218Z"}},{"start":1484,"end":1528,"reference_id":"15327768","reference_source":"pmid","reference_html":"Mechanism of phosphorylation-dependent binding of APC to beta-catenin and its role in beta-catenin degradation. <i> Ha NC, Tonozuka T, Stamos JL, Choi HJ, Weis WI. </i> Mol Cell, 2004","date":"2022-07-25T19:07:44.163Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008013","term_name":"beta-catenin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q02248","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00519r022","statement":[{"text":"Isothermal titration calorimetry (ITC) measurements demonstrated that homogeneously phosphorylated R3 binds to full-length β-catenin with a dissociation constant KD of 10 ± 1.3 nM, as compared to the 3.1 ± 0.3 μM KD of the untreated material (Figures 3A and 3B","type":"Results"}],"term_comment":"","term_def":"\"Binding to a catenin beta subunit.\" [GOC:bf]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1501,"end":1501,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1503,"end":1503,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1504,"end":1504,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1505,"end":1505,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1507,"end":1507,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1510,"end":1510,"position":"Specific residue"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:17:20.502Z"}},{"start":1485,"end":1499,"reference_id":"15327768","reference_source":"pmid","reference_html":"Mechanism of phosphorylation-dependent binding of APC to beta-catenin and its role in beta-catenin degradation. <i> Ha NC, Tonozuka T, Stamos JL, Choi HJ, Weis WI. </i> Mol Cell, 2004","date":"2022-07-25T18:04:50.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008013","term_name":"beta-catenin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1504,"end":1504,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1505,"end":1505,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1507,"end":1507,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1510,"end":1510,"position":"Specific residue"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q02248","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00519r023","statement":[{"text":"Phosphorylated R3 (pR3) was cocrystallized with the arm repeats of β-catenin at pH 6.5, and the structure solved at 2.1 Å. The final model contains β-catenin residues 150-550 and 559-664, and APC 1485-1499 and 1504-1528.","type":"Results"},{"text":"The structure of the pR3/β-catenin complex reveals that residues 1485 to 1499 bind to the arm repeat 5-9 groove identically to that observed in the unphosphorylated complex (Figure 3C).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a catenin beta subunit.\" [GOC:bf]","term_is_obsolete":false,"term_not_annotate":false,"cross_refs":[{"db":"PDB","id":"1V18"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:17:35.350Z"}},{"start":1504,"end":1528,"reference_id":"15327768","reference_source":"pmid","reference_html":"Mechanism of phosphorylation-dependent binding of APC to beta-catenin and its role in beta-catenin degradation. <i> Ha NC, Tonozuka T, Stamos JL, Choi HJ, Weis WI. </i> Mol Cell, 2004","date":"2022-07-25T18:05:14.447Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008013","term_name":"beta-catenin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1504,"end":1504,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1505,"end":1505,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1507,"end":1507,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1510,"end":1510,"position":"Specific residue"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q02248","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00519r024","statement":[{"text":"Phosphorylated R3 (pR3) was cocrystallized with the arm repeats of β-catenin at pH 6.5, and the structure solved at 2.1 Å. The final model contains β-catenin residues 150-550 and 559-664, and APC 1485-1499 and 1504-1528.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a catenin beta subunit.\" [GOC:bf]","term_is_obsolete":false,"term_not_annotate":false,"cross_refs":[{"db":"PDB","id":"1V18"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:18:36.329Z"}},{"start":1504,"end":1528,"reference_id":"15327768","reference_source":"pmid","reference_html":"Mechanism of phosphorylation-dependent binding of APC to beta-catenin and its role in beta-catenin degradation. <i> Ha NC, Tonozuka T, Stamos JL, Choi HJ, Weis WI. </i> Mol Cell, 2004","date":"2022-07-25T18:08:10.597Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1504,"end":1504,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1505,"end":1505,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1507,"end":1507,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1510,"end":1510,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"1V18"}],"region_id":"DP00519r025","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q02248"}],"statement":[{"text":"Phosphorylation results in the structuring of residues 1504-1528, which interact with β-catenin arm repeats 1-5 (Figures 3D and 3E).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:16:10.046Z"}},{"start":1504,"end":1510,"reference_id":"15327768","reference_source":"pmid","reference_html":"Mechanism of phosphorylation-dependent binding of APC to beta-catenin and its role in beta-catenin degradation. <i> Ha NC, Tonozuka T, Stamos JL, Choi HJ, Weis WI. </i> Mol Cell, 2004","date":"2022-07-25T18:17:41.613Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"1V18"}],"region_id":"DP00519r026","statement":[{"text":"Of the six phosphoserines present in the construct, those at positions 1504, 1505, 1507, and 1510, part of the consensus 1501SxxSSLSSLS APC 20-mer motif, are visible, and three of the four form direct contacts with β-catenin.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:18:39.950Z"}},{"start":1501,"end":1510,"reference_id":"15327768","reference_source":"pmid","reference_html":"Mechanism of phosphorylation-dependent binding of APC to beta-catenin and its role in beta-catenin degradation. <i> Ha NC, Tonozuka T, Stamos JL, Choi HJ, Weis WI. </i> Mol Cell, 2004","date":"2022-07-25T18:17:21.131Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"1V18"}],"region_id":"DP00519r027","statement":[{"text":"APC is phosphorylated by GSK-3β and CK1ϵ (Rubinfeld et al. 1996, Rubinfeld et al. 2001). Mass spectrometry analysis of recombinant R3 treated with these two enzymes in vitro demonstrated that six serines are phosphorylated (data not shown).","type":"Results"},{"text":"Ser1505 is “primed” for CK1 phosphorylation by the presence of Asp1512 and Glu1513. Phosphorylated Ser1505 then serves as a priming site for GSK-3β-mediated phosphorylation of Ser1501. With Ser1501 phosphorylated, successive primed phosphorylations by CK1 can occur at Ser1504, Ser1507, and Ser1510. Phosphorylated Ser1507 can also prime a final phosphorylation of Ser1503 by GSK-3β. This scheme accounts for the presence of the six phosphates found in the mass spectroscopic analysis of in vitro-phosphorylated R3.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:18:47.892Z"}}],"released":"2016_10","uniref100":"UniRef100_P25054","date":"2016-09-07T09:11:49.000Z","acc":"P25054","name":"Adenomatous polyposis coli protein","length":2843,"organism":"Homo sapiens","dataset":["Cancer-related proteins","Condensates-related proteins"],"UniParc":"UPI000013CF60","genes":[{"name":{"value":"APC","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:583","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:583"}}]},"synonyms":[{"value":"DP2.5"}]}],"disorder_content":0.2050650721069293,"disprot_consensus":{"full":[{"start":1202,"end":1503,"type":"D"},{"start":1504,"end":1528,"type":"T"},{"start":1529,"end":1745,"type":"D"},{"start":2781,"end":2783,"type":"D"},{"start":2784,"end":2813,"type":"T"},{"start":2814,"end":2819,"type":"D"}],"Structural state":[{"start":1202,"end":1745,"type":"D"},{"start":2781,"end":2819,"type":"D"}],"Molecular function":[{"start":1202,"end":1551,"type":"F"},{"start":1614,"end":1679,"type":"F"},{"start":2781,"end":2819,"type":"F"}],"Structural transition":[{"start":1504,"end":1528,"type":"T"},{"start":2784,"end":2813,"type":"T"}],"Disorder function":[{"start":1501,"end":1510,"type":"F"}]}},{"features":{"gene3D":[{"start":119,"end":160,"id":"1.10.238.10","name":"EF-hand"}],"pfam":[]},"uniref50":"UniRef50_Q969F2","sequence":"MGKLQSKHAAAARKRRESPEGDSFVASAYASGRKGAEEAERRARDKQELPNGDPKEGPFREDQCPLQVALPAEKAEGREHPGQLLSADDGERAANREGPRGPGGQRLNIDALQCDVSVEEDDRQEWTFTLYDFDNCGKVTREDMSSLMHTIYEVVDASVNHSSGSSKTLRVKLTVSPEPSSKRKEGPPAGQDREPTRCRMEGELAEEPRVADRRLSAHVRRPSTDPQPCSERGPYCVDENTERRNHYLDLAGIENYTSRFGPGSPPVQAKQEPQGRASHLQARSRSQEPDTHAVHHRRSQVLVEHVVPASEPAARALDTQPRPKGPEKQFLKSPKGSGKPPGVPASSKSGKAFSYYLPAVLPPQAPQDGHHLPQPPPPPYGHKRYRQKGREGHSPLKAPHAQPATVEHEVVRDLPPTPAGEGYAVPVIQRHEHHHHHEHHHHHHHHHFHPS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q969F2","disprot_id":"DP00520","ncbi_taxon_id":9606,"regions_counter":8,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":217,"region_id":"DP00520r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural studies of human Naked2: a biologically active intrinsically unstructured protein. <i> Hu T, Krezel AM, Li C, Coffey RJ. </i> Biochem Biophys Res Commun, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17045239","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":217,"term_name":"fatty acylation display site","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17045239","version":2,"reference_html":"Structural studies of human Naked2: a biologically active intrinsically unstructured protein. <i> Hu T, Krezel AM, Li C, Coffey RJ. </i> Biochem Biophys Res Commun, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000040","ec_id":"ECO:0006165","region_id":"DP00520r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":217,"term_name":"molecular adaptor activity","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"17045239","version":3,"reference_html":"Structural studies of human Naked2: a biologically active intrinsically unstructured protein. <i> Hu T, Krezel AM, Li C, Coffey RJ. </i> Biochem Biophys Res Commun, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP00520r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":217,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"17045239","version":3,"reference_html":"Structural studies of human Naked2: a biologically active intrinsically unstructured protein. <i> Hu T, Krezel AM, Li C, Coffey RJ. </i> Biochem Biophys Res Commun, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00520r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":217,"region_id":"DP00520r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structural studies of human Naked2: a biologically active intrinsically unstructured protein. <i> Hu T, Krezel AM, Li C, Coffey RJ. </i> Biochem Biophys Res Commun, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17045239","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":217,"term_name":"fatty acylation display site","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17045239","version":2,"reference_html":"Structural studies of human Naked2: a biologically active intrinsically unstructured protein. <i> Hu T, Krezel AM, Li C, Coffey RJ. </i> Biochem Biophys Res Commun, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000040","ec_id":"ECO:0006204","region_id":"DP00520r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":217,"term_name":"molecular adaptor activity","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"17045239","version":3,"reference_html":"Structural studies of human Naked2: a biologically active intrinsically unstructured protein. <i> Hu T, Krezel AM, Li C, Coffey RJ. </i> Biochem Biophys Res Commun, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006204","region_id":"DP00520r007","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":217,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"17045239","version":3,"reference_html":"Structural studies of human Naked2: a biologically active intrinsically unstructured protein. <i> Hu T, Krezel AM, Li C, Coffey RJ. </i> Biochem Biophys Res Commun, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00520r008","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q969F2","date":"2016-08-16T11:36:06.000Z","acc":"Q969F2","name":"Protein naked cuticle homolog 2","length":451,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000073E19","genes":[{"name":{"value":"NKD2"}}],"alphafold_very_low_content":0.4678492239467849,"disorder_content":0.4811529933481153,"disprot_consensus":{"full":[{"start":1,"end":217,"type":"D"}],"Structural state":[{"start":1,"end":217,"type":"D"}],"Disorder function":[{"start":1,"end":217,"type":"F"}],"Molecular function":[{"start":1,"end":217,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04856","name":"Securin sister-chromatid separation inhibitor","start":1,"end":190}]},"uniref50":"UniRef50_O95997","sequence":"MATLIYVDKENGEPGTRVVAKDGLKLGSGPSIKALDGRSQVSTPRFGKTFDAPPALPKATRKALGTVNRATEKSVKTKGPLKQKQPSFSAKKMTEKTVKAKSSVPASDDAYPEIEKFFPFNPLDFESFDLPEEHQIAHLPLSGVPLMILDEERELEKLFQLGPPSPVKMPSPPWESNLLQSPSSILSTLDVELPPVCCDIDI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O95997","disprot_id":"DP00521","ncbi_taxon_id":9606,"regions_counter":15,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":202,"region_id":"DP00521r001","released":"2022_03","ec_id":"ECO:0006198","reference_html":"Human full-length Securin is a natively unfolded protein. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Protein Sci, 2005","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15929994","version":2,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":202,"term_name":"molecular function activator activity","start":1,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15929994","version":3,"reference_html":"Human full-length Securin is a natively unfolded protein. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Protein Sci, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140677","ec_id":"ECO:0006198","region_id":"DP00521r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":202,"term_name":"molecular recognition display site","start":1,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15929994","version":2,"reference_html":"Human full-length Securin is a natively unfolded protein. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Protein Sci, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000037","ec_id":"ECO:0006198","region_id":"DP00521r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":202,"term_name":"disorder to order","start":1,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15929994","version":2,"reference_html":"Human full-length Securin is a natively unfolded protein. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Protein Sci, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006198","region_id":"DP00521r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":202,"term_name":"protein binding","start":1,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15929994","version":3,"reference_html":"Human full-length Securin is a natively unfolded protein. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Protein Sci, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006198","region_id":"DP00521r005","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":202,"region_id":"DP00521r006","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Human full-length Securin is a natively unfolded protein. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Protein Sci, 2005","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15929994","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":202,"term_name":"molecular function activator activity","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15929994","version":3,"reference_html":"Human full-length Securin is a natively unfolded protein. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Protein Sci, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140677","ec_id":"ECO:0006204","region_id":"DP00521r007","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":202,"term_name":"molecular recognition display site","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15929994","version":2,"reference_html":"Human full-length Securin is a natively unfolded protein. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Protein Sci, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000037","ec_id":"ECO:0006204","region_id":"DP00521r008","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":202,"term_name":"disorder to order","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15929994","version":2,"reference_html":"Human full-length Securin is a natively unfolded protein. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Protein Sci, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00521r009","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":202,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15929994","version":3,"reference_html":"Human full-length Securin is a natively unfolded protein. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Protein Sci, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00521r010","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":202,"region_id":"DP00521r011","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Human full-length Securin is a natively unfolded protein. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Protein Sci, 2005","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15929994","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":202,"term_name":"molecular function activator activity","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15929994","version":3,"reference_html":"Human full-length Securin is a natively unfolded protein. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Protein Sci, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140677","ec_id":"ECO:0007680","region_id":"DP00521r012","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":202,"term_name":"molecular recognition display site","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15929994","version":2,"reference_html":"Human full-length Securin is a natively unfolded protein. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Protein Sci, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000037","ec_id":"ECO:0007680","region_id":"DP00521r013","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":202,"term_name":"disorder to order","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15929994","version":2,"reference_html":"Human full-length Securin is a natively unfolded protein. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Protein Sci, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0007680","region_id":"DP00521r014","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":202,"term_name":"protein binding","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15929994","version":3,"reference_html":"Human full-length Securin is a natively unfolded protein. <i> Sánchez-Puig N, Veprintsev DB, Fersht AR. </i> Protein Sci, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007680","region_id":"DP00521r015","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_O95997","date":"2016-08-25T17:10:02.000Z","acc":"O95997","name":"Securin","length":202,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000044DCB","genes":[{"name":{"value":"PTTG1"},"synonyms":[{"value":"EAP1"},{"value":"PTTG"},{"value":"TUTR1"}]}],"alphafold_very_low_content":0.1782178217821782,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":202,"type":"T"}],"Structural state":[{"start":1,"end":202,"type":"D"}],"Molecular function":[{"start":1,"end":202,"type":"F"}],"Disorder function":[{"start":1,"end":202,"type":"F"}],"Structural transition":[{"start":1,"end":202,"type":"T"}]}},{"features":{"pfam":[{"id":"PF17381","name":"Seminal vesicle secretory proteins 4/5/6","start":24,"end":108}]},"uniref50":"UniRef50_P02783","sequence":"MKSTSLFLCSLLLLLVTGAIGRKTKEKYSQSEEVVSESFASGPSSGSSDDELVRDKPYGPKVSGGSFGEEASEEISSRRSKHISRSSGGSNMEGESSYAKKKRSRFAQDVLN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_P02783","disprot_id":"DP00527","ncbi_taxon_id":10116,"regions_counter":6,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":70,"region_id":"DP00527r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structural properties of the protein SV-IV. <i> Caporale C, Caruso C, Colonna G, Facchiano A, Ferranti P, Mamone G, Picariello G, Colonna F, Metafora S, Stiuso P. </i> Eur J Biochem, 2004","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"14717694","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":70,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"14717694","version":3,"reference_html":"Structural properties of the protein SV-IV. <i> Caporale C, Caruso C, Colonna G, Facchiano A, Ferranti P, Mamone G, Picariello G, Colonna F, Metafora S, Stiuso P. </i> Eur J Biochem, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00527r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":70,"region_id":"DP00527r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The self-association of protein SV-IV and its possible functional implications. <i> Stiuso P, Metafora S, Facchiano AM, Colonna G, Ragone R. </i> Eur J Biochem, 1999","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"10583398","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":70,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"10583398","version":3,"reference_html":"The self-association of protein SV-IV and its possible functional implications. <i> Stiuso P, Metafora S, Facchiano AM, Colonna G, Ragone R. </i> Eur J Biochem, 1999","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00527r004","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":70,"region_id":"DP00527r005","released":"2022_03","ec_id":"ECO:0007689","reference_html":"Purification and cell-free synthesis of a major protein from rat seminal vesicle secretion. A potential marker for androgen action. <i> Ostrowski MC, Kistler MK, Kistler WS. </i> J Biol Chem, 1979","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"762067","version":2,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":70,"term_name":"protein binding","start":1,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"762067","version":3,"reference_html":"Purification and cell-free synthesis of a major protein from rat seminal vesicle secretion. A potential marker for androgen action. <i> Ostrowski MC, Kistler MK, Kistler WS. </i> J Biol Chem, 1979","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007689","region_id":"DP00527r006","curator_orcid":"0000-0001-9377-482X","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P02783","date":"2016-09-07T09:42:31.000Z","acc":"P02783","name":"Seminal vesicle secretory protein 4","length":112,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI0000136299","genes":[{"name":{"value":"Svs4"},"synonyms":[{"value":"Svp2"},{"value":"Svp4"}]}],"alphafold_very_low_content":0.20535714285714285,"disorder_content":0.625,"disprot_consensus":{"full":[{"start":1,"end":70,"type":"D"}],"Structural state":[{"start":1,"end":70,"type":"D"}],"Molecular function":[{"start":1,"end":70,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00257","name":"Dehydrin","start":16,"end":168}]},"uniref50":"UniRef50_P12950","sequence":"MEYGQQGQRGHGRTGHVDQYGNPVGGVEHGTGGMRHGTGTTGGMGQLGEHGGAGMGGGQFQPAREEHKTGGILHRSGSSSSSSSEDDGMGGRRKKGIKEKIKEKLPGGHKDDQHATATTGGAYGQQGHTGSAYGQQGHTGGAYATGTEGTGEKKGIMDKIKEKLPGQH","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","PACMAD clade","Panicoideae","Andropogonodae","Andropogoneae","Tripsacinae","Zea"],"uniref90":"UniRef90_P12950","disprot_id":"DP00530","ncbi_taxon_id":4577,"regions_counter":3,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":168,"region_id":"DP00530r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The binding of maize DHN1 to lipid vesicles. Gain of structure and lipid specificity. <i> Koag MC, Fenton RD, Wilkens S, Close TJ. </i> Plant Physiol, 2003","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12529538","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":168,"term_name":"disorder to order","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12529538","version":2,"reference_html":"The binding of maize DHN1 to lipid vesicles. Gain of structure and lipid specificity. <i> Koag MC, Fenton RD, Wilkens S, Close TJ. </i> Plant Physiol, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00530r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":168,"term_name":"lipid binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"12529538","version":3,"reference_html":"The binding of maize DHN1 to lipid vesicles. Gain of structure and lipid specificity. <i> Koag MC, Fenton RD, Wilkens S, Close TJ. </i> Plant Physiol, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008289","ec_id":"ECO:0006204","region_id":"DP00530r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P12950","date":"2016-09-14T11:07:04.000Z","acc":"P12950","name":"Dehydrin DHN1","length":168,"organism":"Zea mays","dataset":["Stress response proteins"],"UniParc":"UPI000016DDCC","genes":[{"name":{"value":"DHN1"}}],"alphafold_very_low_content":0.4583333333333333,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":168,"type":"T"}],"Structural state":[{"start":1,"end":168,"type":"D"}],"Structural transition":[{"start":1,"end":168,"type":"T"}],"Molecular function":[{"start":1,"end":168,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02496","name":"ABA/WDS induced protein","start":24,"end":100}]},"uniref50":"UniRef50_Q08655","sequence":"MEEEKHHHHHLFHHKDKAEEGPVDYEKEIKHHKHLEQIGKLGTVAAGAYALHEKHEAKKDPEHAHKHKIEEEIAAAAAVGAGGFAFHEHHEKKDAKKEEKKKLRGDTTISSKLLF","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","lamiids","Solanales","Solanaceae","Solanoideae","Solaneae","Solanum","Solanum subgen. Lycopersicon"],"uniref90":"UniRef90_Q08655","disprot_id":"DP00531","ncbi_taxon_id":4081,"regions_counter":22,"creator":"lchemes","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":115,"region_id":"DP00531r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Desiccation and zinc binding induce transition of tomato abscisic acid stress ripening 1, a water stress- and salt stress-regulated plant-specific protein, from unfolded to folded state. <i> Goldgur Y, Rom S, Ghirlando R, Shkolnik D, Shadrin N, Konrad Z, Bar-Zvi D. </i> Plant Physiol, 2007","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17189335","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":115,"term_name":"disorder to order","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17189335","version":2,"reference_html":"Desiccation and zinc binding induce transition of tomato abscisic acid stress ripening 1, a water stress- and salt stress-regulated plant-specific protein, from unfolded to folded state. <i> Goldgur Y, Rom S, Ghirlando R, Shkolnik D, Shadrin N, Konrad Z, Bar-Zvi D. </i> Plant Physiol, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00531r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":115,"term_name":"nucleic acid binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"17189335","version":3,"reference_html":"Desiccation and zinc binding induce transition of tomato abscisic acid stress ripening 1, a water stress- and salt stress-regulated plant-specific protein, from unfolded to folded state. <i> Goldgur Y, Rom S, Ghirlando R, Shkolnik D, Shadrin N, Konrad Z, Bar-Zvi D. </i> Plant Physiol, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006204","region_id":"DP00531r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":115,"term_name":"ion binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"17189335","version":3,"reference_html":"Desiccation and zinc binding induce transition of tomato abscisic acid stress ripening 1, a water stress- and salt stress-regulated plant-specific protein, from unfolded to folded state. <i> Goldgur Y, Rom S, Ghirlando R, Shkolnik D, Shadrin N, Konrad Z, Bar-Zvi D. </i> Plant Physiol, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0043167","ec_id":"ECO:0006204","region_id":"DP00531r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":115,"region_id":"DP00531r005","released":"2022_03","ec_id":"ECO:0007064","reference_html":"Desiccation and zinc binding induce transition of tomato abscisic acid stress ripening 1, a water stress- and salt stress-regulated plant-specific protein, from unfolded to folded state. <i> Goldgur Y, Rom S, Ghirlando R, Shkolnik D, Shadrin N, Konrad Z, Bar-Zvi D. </i> Plant Physiol, 2007","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17189335","version":2,"ec_name":"dynamic light scattering assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":115,"term_name":"disorder to order","start":1,"ec_name":"dynamic light scattering assay evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17189335","version":2,"reference_html":"Desiccation and zinc binding induce transition of tomato abscisic acid stress ripening 1, a water stress- and salt stress-regulated plant-specific protein, from unfolded to folded state. <i> Goldgur Y, Rom S, Ghirlando R, Shkolnik D, Shadrin N, Konrad Z, Bar-Zvi D. </i> Plant Physiol, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0007064","region_id":"DP00531r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":115,"term_name":"nucleic acid binding","start":1,"ec_name":"dynamic light scattering assay evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"17189335","version":3,"reference_html":"Desiccation and zinc binding induce transition of tomato abscisic acid stress ripening 1, a water stress- and salt stress-regulated plant-specific protein, from unfolded to folded state. <i> Goldgur Y, Rom S, Ghirlando R, Shkolnik D, Shadrin N, Konrad Z, Bar-Zvi D. </i> Plant Physiol, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0007064","region_id":"DP00531r007","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":115,"term_name":"ion binding","start":1,"ec_name":"dynamic light scattering assay evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"17189335","version":3,"reference_html":"Desiccation and zinc binding induce transition of tomato abscisic acid stress ripening 1, a water stress- and salt stress-regulated plant-specific protein, from unfolded to folded state. <i> Goldgur Y, Rom S, Ghirlando R, Shkolnik D, Shadrin N, Konrad Z, Bar-Zvi D. </i> Plant Physiol, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0043167","ec_id":"ECO:0007064","region_id":"DP00531r008","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":115,"region_id":"DP00531r009","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Desiccation and zinc binding induce transition of tomato abscisic acid stress ripening 1, a water stress- and salt stress-regulated plant-specific protein, from unfolded to folded state. <i> Goldgur Y, Rom S, Ghirlando R, Shkolnik D, Shadrin N, Konrad Z, Bar-Zvi D. </i> Plant Physiol, 2007","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17189335","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":115,"term_name":"disorder to order","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17189335","version":2,"reference_html":"Desiccation and zinc binding induce transition of tomato abscisic acid stress ripening 1, a water stress- and salt stress-regulated plant-specific protein, from unfolded to folded state. <i> Goldgur Y, Rom S, Ghirlando R, Shkolnik D, Shadrin N, Konrad Z, Bar-Zvi D. </i> Plant Physiol, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0007680","region_id":"DP00531r010","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":115,"term_name":"nucleic acid binding","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"17189335","version":3,"reference_html":"Desiccation and zinc binding induce transition of tomato abscisic acid stress ripening 1, a water stress- and salt stress-regulated plant-specific protein, from unfolded to folded state. <i> Goldgur Y, Rom S, Ghirlando R, Shkolnik D, Shadrin N, Konrad Z, Bar-Zvi D. </i> Plant Physiol, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0007680","region_id":"DP00531r011","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":115,"term_name":"ion binding","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"17189335","version":3,"reference_html":"Desiccation and zinc binding induce transition of tomato abscisic acid stress ripening 1, a water stress- and salt stress-regulated plant-specific protein, from unfolded to folded state. <i> Goldgur Y, Rom S, Ghirlando R, Shkolnik D, Shadrin N, Konrad Z, Bar-Zvi D. </i> Plant Physiol, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0043167","ec_id":"ECO:0007680","region_id":"DP00531r012","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":115,"region_id":"DP00531r013","released":"2022_03","ec_id":"ECO:0006228","reference_html":"Desiccation and zinc binding induce transition of tomato abscisic acid stress ripening 1, a water stress- and salt stress-regulated plant-specific protein, from unfolded to folded state. <i> Goldgur Y, Rom S, Ghirlando R, Shkolnik D, Shadrin N, Konrad Z, Bar-Zvi D. </i> Plant Physiol, 2007","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17189335","version":2,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":115,"term_name":"disorder to order","start":1,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17189335","version":2,"reference_html":"Desiccation and zinc binding induce transition of tomato abscisic acid stress ripening 1, a water stress- and salt stress-regulated plant-specific protein, from unfolded to folded state. <i> Goldgur Y, Rom S, Ghirlando R, Shkolnik D, Shadrin N, Konrad Z, Bar-Zvi D. </i> Plant Physiol, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006228","region_id":"DP00531r014","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":115,"term_name":"nucleic acid binding","start":1,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"17189335","version":3,"reference_html":"Desiccation and zinc binding induce transition of tomato abscisic acid stress ripening 1, a water stress- and salt stress-regulated plant-specific protein, from unfolded to folded state. <i> Goldgur Y, Rom S, Ghirlando R, Shkolnik D, Shadrin N, Konrad Z, Bar-Zvi D. </i> Plant Physiol, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006228","region_id":"DP00531r015","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":115,"term_name":"ion binding","start":1,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"17189335","version":3,"reference_html":"Desiccation and zinc binding induce transition of tomato abscisic acid stress ripening 1, a water stress- and salt stress-regulated plant-specific protein, from unfolded to folded state. <i> Goldgur Y, Rom S, Ghirlando R, Shkolnik D, Shadrin N, Konrad Z, Bar-Zvi D. </i> Plant Physiol, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0043167","ec_id":"ECO:0006228","region_id":"DP00531r016","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":115,"region_id":"DP00531r017","released":"2022_03","ec_id":"ECO:0006206","reference_html":"Conformational plasticity of the intrinsically disordered protein ASR1 modulates its function as a drought stress-responsive gene. <i> Wetzler DE, Fuchs Wightman F, Bucci HA, Rinaldi J, Caramelo JJ, Iusem ND, Ricardi MM. </i> PLoS One, 2018","statement":[{"text":"The CD spectrum of ASR1, without any additive, displayed a minimum dichroic peak cen- tered at 200 nm, typical of disordered conformations, and a low signal above 205 nm, charac- teristic of a more ordered structure (Fig 1A). These observations are in accordance with in silico predictions and experimental observations describing ASR1 as a disordered protein [8].","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"lchemes","start":1,"term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"30138481","version":2,"ec_name":"near-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":115,"term_name":"disorder to order","start":1,"ec_name":"near-UV circular dichroism evidence used in manual assertion","statement":[{"text":"We report that ASR1 adopts different conformations such as α-helix or polyproline type II in response to environ- mental changes. Low temperatures and low pH promote the polyproline type II conformation (PII). While NaCl increases PII content and slightly destabilizes α-helix conformation, PEG and glycerol have an important stabilizing effect of α-helix conformation.","type":"Abstract"}],"curator_id":"lchemes","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"30138481","version":2,"reference_html":"Conformational plasticity of the intrinsically disordered protein ASR1 modulates its function as a drought stress-responsive gene. <i> Wetzler DE, Fuchs Wightman F, Bucci HA, Rinaldi J, Caramelo JJ, Iusem ND, Ricardi MM. </i> PLoS One, 2018","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006206","region_id":"DP00531r018","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":115,"term_name":"nucleic acid binding","start":1,"ec_name":"near-UV circular dichroism evidence used in manual assertion","statement":[{"text":"The binding of Zn2 +in the low micromolar range promotes α-helix folding, while extra Zn2+ results in homo- dimerization. The ASR1-DNA binding is sequence specific and dependent on Zn2+.","type":"Abstract"}],"curator_id":"lchemes","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"30138481","version":3,"reference_html":"Conformational plasticity of the intrinsically disordered protein ASR1 modulates its function as a drought stress-responsive gene. <i> Wetzler DE, Fuchs Wightman F, Bucci HA, Rinaldi J, Caramelo JJ, Iusem ND, Ricardi MM. </i> PLoS One, 2018","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006206","region_id":"DP00531r019","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":115,"term_name":"zinc ion binding","start":1,"ec_name":"near-UV circular dichroism evidence used in manual assertion","statement":[{"text":"Follow-\ning the CD signal change at 222 nm in the Zn2+ titration experiment and considering a 1:1\nstoichiometry (see Materials and Methods), we estimated an equilibrium dissociation constant\nbetween ASR1 and Zn2+, KZn2þ , of (9 ± 2) μM.","type":"Results"}],"curator_id":"lchemes","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"30138481","version":3,"reference_html":"Conformational plasticity of the intrinsically disordered protein ASR1 modulates its function as a drought stress-responsive gene. <i> Wetzler DE, Fuchs Wightman F, Bucci HA, Rinaldi J, Caramelo JJ, Iusem ND, Ricardi MM. </i> PLoS One, 2018","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008270","ec_id":"ECO:0006206","region_id":"DP00531r020","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":115,"region_id":"DP00531r021","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Mapping the DNA- and zinc-binding domains of ASR1 (abscisic acid stress ripening), an abiotic-stress regulated plant specific protein. <i> Rom S, Gilad A, Kalifa Y, Konrad Z, Karpasas MM, Goldgur Y, Bar-Zvi D. </i> Biochimie, 2006","statement":[{"text":"Incubation of ASR1 with a variety of proteases resulted in the generation of a large number of low molecular weight proteolytic products (Fig. 4A). Binding of zinc to ASR1 induces conformational changes resulting in a decreased sensitivity to proteases.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"lchemes","start":61,"term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"16387406","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":115,"term_name":"nucleic acid binding","start":61,"ec_name":"cleavage assay evidence used in manual assertion","statement":[{"text":"South-western DNA- binding assays indicate that the carboxy-terminal domain of ASR1 containing residues 61–115 has a zinc-dependent DNA-binding activity, whereas the amino-terminal sequence (residues 1–60) does not (Fig. 1). Using mild acid hydrolysis, and a series of ASR1 carboxy-terminal truncations we show that the zinc-dependent DNA-binding could be mapped to the central/carboxy-terminal domain.","type":"Results"}],"curator_id":"lchemes","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"16387406","version":3,"reference_html":"Mapping the DNA- and zinc-binding domains of ASR1 (abscisic acid stress ripening), an abiotic-stress regulated plant specific protein. <i> Rom S, Gilad A, Kalifa Y, Konrad Z, Karpasas MM, Goldgur Y, Bar-Zvi D. </i> Biochimie, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0007691","region_id":"DP00531r022","curator_orcid":"0000-0003-0192-9906","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q08655","date":"2016-08-25T17:17:34.000Z","acc":"Q08655","name":"Abscisic stress-ripening protein 1","length":115,"organism":"Solanum lycopersicum","dataset":[],"UniParc":"UPI0000126162","genes":[{"name":{"value":"ASR1","evidences":[{"code":"ECO:0000303","source":{"name":"Citation","id":"Ref.2","url":"https://www.uniprot.org/uniprot/null#ref2"}}]}}],"alphafold_very_low_content":0.1565217391304348,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":115,"type":"T"}],"Structural state":[{"start":1,"end":115,"type":"D"}],"Structural transition":[{"start":1,"end":115,"type":"T"}],"Molecular function":[{"start":1,"end":115,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01426","name":"BAH domain","start":50,"end":187},{"id":"PF17872","name":"AAA lid domain","start":737,"end":833},{"id":"PF22344","name":"Regulatory protein SIR3, C-terminal domain","start":851,"end":972}],"gene3D":[{"start":1,"end":229,"id":"2.30.30.490","name":"2.30.30.490"},{"start":842,"end":978,"id":"1.10.10.2450","name":"1.10.10.2450"},{"start":528,"end":724,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_P06701","sequence":"MAKTLKDLDGWQVIITDDQGRVIDDNNRRRSRKRGGENVFLKRISDGLSFGKGESVIFNDNVTETYSVYLIHEIRLNTLNNVVEIWVFSYLRWFELKPKLYYEQFRPDLIKEDHPLEFYKDKFFNEVNKSELYLTAELSEIWLKDFIAVGQILPESQWNDSSIDKIEDRDFLVRYACEPTAEKFVPIDIFQIIRRVKEMEPKQSDEYLKRVSVPVSGQKTNRQVMHKMGVERSSKRLAKKPSMKKIKIEPSADDDVNNGNIPSQRGTSTTHGSISPQEESVSPNISSASPSALTSPTDSSKILQKRSISKELIVSEEIPINSSEQESDYEPNNETSVLSSKPGSKPEKTSTELVDGRENFVYANNPEVSDDGGLEEETDEVSSESSDEAIIPVNKRRGAHGSELSSKIRKIHIQETQEFSKNYTTETDNEMNGNGKPGIPRGNTKIHSMNENPTPEKGNAKMIDFATLSKLKKKYQIILDRFAPDNQVTDSSQLNKLTDEQSSLDVAGLEDKFRKACSSSGRETILSNFNADINLEESIRESLQKRELLKSQVEDFTRIFLPIYDSLMSSQNKLFYITNADDSTKFQLVNDVMDELITSSARKELPIFDYIHIDALELAGMDALYEKIWFAISKENLCGDISLEALNFYITNVPKAKKRKTLILIQNPENLLSEKILQYFEKWISSKNSKLSIICVGGHNVTIREQINIMPSLKAHFTEIKLNKVDKNELQQMIITRLKSLLKPFHVKVNDKKEMTIYNNIREGQNQKIPDNVIVINHKINNKITQLIAKNVANVSGSTEKAFKICEAAVEISKKDFVRKGGLQKGKLVVSQEMVPRYFSEAINGFKDETISKKIIGMSLLMRTFLYTLAQETEGTNRHTLALETVLIKMVKMLRDNPGYKASKEIKKVICGAWEPAITIEKLKQFSWISVVNDLVGEKLVVVVLEEPSASIMVELKLPLEINYAFSMDEEFKNMDCI","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P06701","disprot_id":"DP00533","ncbi_taxon_id":559292,"regions_counter":5,"creator":"wvranken","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":549,"region_id":"DP00533r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Domain organization and quaternary structure of the Saccharomyces cerevisiae silent information regulator 3 protein, Sir3p. <i> McBryant SJ, Krause C, Hansen JC. </i> Biochemistry, 2006","term_id":"IDPO:0000002","curator_id":"wvranken","start":216,"term_ontology":"IDPO","curator_name":"Wim Vranken","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17176117","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":549,"term_name":"entropic chain","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Domain organization and quaternary structure of the Saccharomyces cerevisiae silent information regulator 3 protein, Sir3p. <i> McBryant SJ, Krause C, Hansen JC. </i> Biochemistry, 2006","term_id":"IDPO:0000030","curator_id":"wvranken","start":216,"term_ontology":"IDPO","curator_name":"Wim Vranken","reference_id":"17176117","version":3,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00533r002","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":549,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Domain organization and quaternary structure of the Saccharomyces cerevisiae silent information regulator 3 protein, Sir3p. <i> McBryant SJ, Krause C, Hansen JC. </i> Biochemistry, 2006","term_id":"GO:0005515","curator_id":"wvranken","start":216,"term_ontology":"GO","curator_name":"Wim Vranken","reference_id":"17176117","version":3,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00533r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":549,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Domain organization and quaternary structure of the Saccharomyces cerevisiae silent information regulator 3 protein, Sir3p. <i> McBryant SJ, Krause C, Hansen JC. </i> Biochemistry, 2006","term_id":"GO:0003676","curator_id":"wvranken","start":216,"term_ontology":"GO","curator_name":"Wim Vranken","reference_id":"17176117","version":3,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00533r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":549,"region_id":"DP00533r005","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Domain organization and quaternary structure of the Saccharomyces cerevisiae silent information regulator 3 protein, Sir3p. <i> McBryant SJ, Krause C, Hansen JC. </i> Biochemistry, 2006","term_id":"IDPO:0000002","curator_id":"wvranken","start":216,"term_ontology":"IDPO","curator_name":"Wim Vranken","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17176117","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P06701","date":"2016-09-09T15:20:17.000Z","acc":"P06701","name":"Regulatory protein SIR3","length":978,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000168E34","genes":[{"name":{"value":"SIR3"},"synonyms":[{"value":"CMT1"},{"value":"MAR2"},{"value":"STE8"}],"orfNames":[{"value":"L9753.10"}],"olnNames":[{"value":"YLR442C"}]}],"alphafold_very_low_content":0.294478527607362,"disorder_content":0.34151329243353784,"disprot_consensus":{"full":[{"start":216,"end":549,"type":"D"}],"Structural state":[{"start":216,"end":549,"type":"D"}],"Disorder function":[{"start":216,"end":549,"type":"F"}],"Molecular function":[{"start":216,"end":549,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02672","name":"CP12 domain","start":60,"end":130}]},"uniref50":"UniRef50_Q9LZP9","sequence":"MATIATGLNIATQRVFVTSENRPVCLAGPVHLNNSWNLGSRTTNRMMKLQPIKAAPEGGISDVVEKSIKEAQETCAGDPVSGECVAAWDEVEELSAAASHARDKKKADGSDPLEEYCKDNPETNECRTYDN","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q9LZP9","disprot_id":"DP00534","ncbi_taxon_id":3702,"regions_counter":10,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":131,"region_id":"DP00534r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Conformational selection and folding-upon-binding of intrinsically disordered protein CP12 regulate photosynthetic enzymes assembly. <i> Fermani S, Trivelli X, Sparla F, Thumiger A, Calvaresi M, Marri L, Falini G, Zerbetto F, Trost P. </i> J Biol Chem, 2012","term_id":"IDPO:0000002","curator_id":"mnecci","start":54,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"22514274","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2LJ9"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":131,"term_name":"disorder to order","start":54,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"22514274","version":2,"reference_html":"Conformational selection and folding-upon-binding of intrinsically disordered protein CP12 regulate photosynthetic enzymes assembly. <i> Fermani S, Trivelli X, Sparla F, Thumiger A, Calvaresi M, Marri L, Falini G, Zerbetto F, Trost P. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00534r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":131,"term_name":"protein binding","start":54,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"22514274","version":3,"reference_html":"Conformational selection and folding-upon-binding of intrinsically disordered protein CP12 regulate photosynthetic enzymes assembly. <i> Fermani S, Trivelli X, Sparla F, Thumiger A, Calvaresi M, Marri L, Falini G, Zerbetto F, Trost P. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00534r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":131,"region_id":"DP00534r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Spontaneous assembly of photosynthetic supramolecular complexes as mediated by the intrinsically unstructured protein CP12. <i> Marri L, Trost P, Trivelli X, Gonnelli L, Pupillo P, Sparla F. </i> J Biol Chem, 2008","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"17947231","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":131,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"17947231","version":3,"reference_html":"Spontaneous assembly of photosynthetic supramolecular complexes as mediated by the intrinsically unstructured protein CP12. <i> Marri L, Trost P, Trivelli X, Gonnelli L, Pupillo P, Sparla F. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00534r005","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":131,"region_id":"DP00534r006","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Spontaneous assembly of photosynthetic supramolecular complexes as mediated by the intrinsically unstructured protein CP12. <i> Marri L, Trost P, Trivelli X, Gonnelli L, Pupillo P, Sparla F. </i> J Biol Chem, 2008","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"17947231","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":131,"term_name":"protein binding","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"17947231","version":3,"reference_html":"Spontaneous assembly of photosynthetic supramolecular complexes as mediated by the intrinsically unstructured protein CP12. <i> Marri L, Trost P, Trivelli X, Gonnelli L, Pupillo P, Sparla F. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007680","region_id":"DP00534r007","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":131,"region_id":"DP00534r008","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Conformational selection and folding-upon-binding of intrinsically disordered protein CP12 regulate photosynthetic enzymes assembly. <i> Fermani S, Trivelli X, Sparla F, Thumiger A, Calvaresi M, Marri L, Falini G, Zerbetto F, Trost P. </i> J Biol Chem, 2012","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"22514274","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2LJ9"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":131,"term_name":"disorder to order","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"22514274","version":2,"reference_html":"Conformational selection and folding-upon-binding of intrinsically disordered protein CP12 regulate photosynthetic enzymes assembly. <i> Fermani S, Trivelli X, Sparla F, Thumiger A, Calvaresi M, Marri L, Falini G, Zerbetto F, Trost P. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00534r009","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":131,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"22514274","version":3,"reference_html":"Conformational selection and folding-upon-binding of intrinsically disordered protein CP12 regulate photosynthetic enzymes assembly. <i> Fermani S, Trivelli X, Sparla F, Thumiger A, Calvaresi M, Marri L, Falini G, Zerbetto F, Trost P. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00534r010","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q9LZP9","date":"2016-09-07T10:32:17.000Z","acc":"Q9LZP9","name":"Calvin cycle protein CP12-2, chloroplastic","length":131,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI00000A68CE","genes":[{"name":{"value":"CP12-2"},"orfNames":[{"value":"T12C14.110"}],"olnNames":[{"value":"At3g62410"}]}],"alphafold_very_low_content":0.015267175572519083,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":131,"type":"T"}],"Structural state":[{"start":1,"end":131,"type":"D"}],"Structural transition":[{"start":1,"end":131,"type":"T"}],"Molecular function":[{"start":1,"end":131,"type":"F"}]}},{"features":{"pfam":[],"gene3D":[{"start":121,"end":416,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_O43236","sequence":"MDRSLGWQGNSVPEDRTEAGIKRFLEDTTDDGELSKFVKDFSGNASCHPPEAKTWASRPQVPEPRPQAPDLYDDDLEFRPPSRPQSSDNQQYFCAPAPLSPSARPRSPWGKLDPYDSSEDDKEYVGFATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVNSLFLTDLYRDRKLLGAEERIMQTVEITKHAVDIEEKGVRLRLTIVDTPGFGDAVNNTECWKPVAEYIDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPLDVEFMKALHQRVNIVPILAKADTLTPPEVDHKKRKIREEIEHFGIKIYQFPDCDSDEDEDFKLQDQALKESIPFAVIGSNTVVEARGRRVRGRLYPWGIVEVENPGHCDFVKLRTMLVRTHMQDLKDVTRETHYENYRAQCIQSMTRLVVKERNRNKLTRESGTDFPIPAVPPGTDPETEKLIREKDEELRRMQEMLHKIQKQMKENY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O43236","disprot_id":"DP00537","ncbi_taxon_id":9606,"regions_counter":3,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":119,"region_id":"DP00537r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Dissection of a human septin: definition and characterization of distinct domains within human SEPT4. <i> Garcia W, de Araújo AP, Neto Mde O, Ballestero MR, Polikarpov I, Tanaka M, Tanaka T, Garratt RC. </i> Biochemistry, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17105210","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":119,"region_id":"DP00537r002","released":"2022_03","ec_id":"ECO:0007064","reference_html":"Dissection of a human septin: definition and characterization of distinct domains within human SEPT4. <i> Garcia W, de Araújo AP, Neto Mde O, Ballestero MR, Polikarpov I, Tanaka M, Tanaka T, Garratt RC. </i> Biochemistry, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17105210","version":2,"ec_name":"dynamic light scattering assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":119,"region_id":"DP00537r003","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Dissection of a human septin: definition and characterization of distinct domains within human SEPT4. <i> Garcia W, de Araújo AP, Neto Mde O, Ballestero MR, Polikarpov I, Tanaka M, Tanaka T, Garratt RC. </i> Biochemistry, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17105210","version":2,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_O43236","date":"2016-08-16T11:52:27.000Z","acc":"O43236-1","name":"Septin-4","length":478,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000013585C","genes":[{"name":{"value":"SEPTIN4","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9165","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9165"}}]},"synonyms":[{"value":"C17orf47","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9165","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9165"}}]},{"value":"PNUTL2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9889007","url":"http://www.ncbi.nlm.nih.gov/pubmed/9889007","alternativeUrl":"https://europepmc.org/abstract/MED/9889007"}}]},{"value":"SEP4","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9165","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9165"}}]},{"value":"SEPT4","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9165","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9165"}}]}],"orfNames":[{"value":"hucep-7"}]}],"alphafold_very_low_content":0.24476987447698745,"disorder_content":0.2489539748953975,"disprot_consensus":{"full":[{"start":1,"end":119,"type":"D"}],"Structural state":[{"start":1,"end":119,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01429","name":"Methyl-CpG binding domain","start":96,"end":159}],"gene3D":[{"start":64,"end":195,"id":"3.30.890.10","name":"Methyl-cpg-binding Protein 2; Chain A"}]},"uniref50":"UniRef50_P51608","sequence":"MVAGMLGLREEKSEDQDLQGLKDKPLKFKKVKKDKKEEKEGKHEPVQPSAHHSAEPAEAGKAETSEGSGSAPAVPEASASPKQRRSIIRDRGPMYDDPTLPEGWTRKLKQRKSGRSAGKYDVYLINPQGKAFRSKVELIAYFEKVGDTSLDPNDFDFTVTGRGSPSRREQKPPKKPKSPKAPGTGRGRGRPKGSGTTRPKAATSEGVQVKRVLEKSPGKLLVKMPFQTSPGGKAEGGGATTSTQVMVIKRPGRKRKAEADPQAIPKKRGRKPGSVVAAAAAEAKKKAVKESSIRSVQETVLPIKKRKTRETVSIEVKEVVKPLLVSTLGEKSGKGLKTCKSPGRKSKESSPKGRSSSASSPPKKEHHHHHHHSESPKAPVPLLPPLPPPPPEPESSEDPTSPPEPQDLSSSVCKEEKMPRGGSLESDGCPKEPAKTQPAVATAATAAEKYKHRGEGERKDIVSSSMPRPNREEPVDSRTPVTERVS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P51608","disprot_id":"DP00539","ncbi_taxon_id":9606,"regions_counter":25,"creator":"ireményi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":75,"region_id":"DP00539r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Unique physical properties and interactions of the domains of methylated DNA binding protein 2. <i> Ghosh RP, Ghosh RP, Nikitina T, Horowitz-Scherer RA, Gierasch LM, Uversky VN, Hite K, Hansen JC, Woodcock CL. </i> Biochemistry, 2010","term_id":"IDPO:0000002","curator_id":"eleonardi","start":1,"term_ontology":"IDPO","curator_name":"Emanuela Leonardi","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20405910","statement":[{"text":"Figure 2. Circular dichroism spectra of MeCP2 domains reveal marked differences in secondary structure content. CD spectra are representative of two to four separate acquisitions. (a) Compared to the 195 nm peak indicative of β-sheet structure within the MBD (◼), all the other domains show a negative band in the 195−198 nm region indicative of disorder. NTD (●), TRD (○), and CTD-α (⊙) have lower structure content than ID (☆) and CTD-β (half-filled circles) (see Table 1 for quantitation)","type":"Figure"},{"text":"To construct the NTD (residues 1−90), an amplicon extending 100 bp 5′ of the NdeI site into the pTYB1 vector sequence and carrying a 3′ EcoRI linker (GACCGTGAATTC) was generated by PCR from full-length pTYB1-MeCP2 cDNA carrying MeCP2 cDNA between its NdeI and EcoRI sites, using the following primer pairs: NTD Forward (5′ CCGGTTTAAACCGGGGATCTCGATCC 3′) and NTD Reverse (5′ GTTAGAGAATTCGTCACGGATGATGGAGCGCCGCTG 3′).","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T12:20:55.751Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":310,"region_id":"DP00539r004","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Unique physical properties and interactions of the domains of methylated DNA binding protein 2. <i> Ghosh RP, Ghosh RP, Nikitina T, Horowitz-Scherer RA, Gierasch LM, Uversky VN, Hite K, Hansen JC, Woodcock CL. </i> Biochemistry, 2010","term_id":"IDPO:0000002","curator_id":"eleonardi","start":207,"term_ontology":"IDPO","curator_name":"Emanuela Leonardi","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20405910","statement":[{"text":"To construct the MBD (residues 75−164), ID (residues 165−210), TRD (residues 207−310), CTD-α (residues 261−330), and CTD-β (residues 335−486), we engineered amplicons with 5′ NdeI and 3′ EcoRI linkers","type":"Methods"},{"text":"Figure 2. Circular dichroism spectra of MeCP2 domains reveal marked differences in secondary structure content. CD spectra are representative of two to four separate acquisitions. (a) Compared to the 195 nm peak indicative of β-sheet structure within the MBD (◼), all the other domains show a negative band in the 195−198 nm region indicative of disorder. NTD (●), TRD (○), and CTD-α (⊙) have lower structure content than ID (☆) and CTD-β (half-filled circles) (see Table 1 for quantitation)","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T06:57:25.418Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":310,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Unique physical properties and interactions of the domains of methylated DNA binding protein 2. <i> Ghosh RP, Ghosh RP, Nikitina T, Horowitz-Scherer RA, Gierasch LM, Uversky VN, Hite K, Hansen JC, Woodcock CL. </i> Biochemistry, 2010","term_id":"GO:0003676","curator_id":"eleonardi","start":207,"term_ontology":"GO","curator_name":"Emanuela Leonardi","reference_id":"20405910","version":4,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00539r006","statement":[{"text":"From Table 1 the transcriptional repression domain (TRD) spans 207-310","type":"Curator statement"},{"text":"The ID and TRD, when mixed with an equimolar amount of the 45 bp DNA substrate, resulted in striking changes in far-UV CD profiles, independent of the DNA methylation state (Figure 2b,c).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T12:22:14.655Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":210,"region_id":"DP00539r007","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Unique physical properties and interactions of the domains of methylated DNA binding protein 2. <i> Ghosh RP, Ghosh RP, Nikitina T, Horowitz-Scherer RA, Gierasch LM, Uversky VN, Hite K, Hansen JC, Woodcock CL. </i> Biochemistry, 2010","term_id":"IDPO:0000002","curator_id":"eleonardi","start":165,"term_ontology":"IDPO","curator_name":"Emanuela Leonardi","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20405910","statement":[{"text":"To construct the MBD (residues 75−164), ID (residues 165−210), TRD (residues 207−310), CTD-α (residues 261−330), and CTD-β (residues 335−486), we engineered amplicons with 5′ NdeI and 3′ EcoRI linkers","type":"Methods"},{"text":"Figure 2. Circular dichroism spectra of MeCP2 domains reveal marked differences in secondary structure content. CD spectra are representative of two to four separate acquisitions. (a) Compared to the 195 nm peak indicative of β-sheet structure within the MBD (◼), all the other domains show a negative band in the 195−198 nm region indicative of disorder. NTD (●), TRD (○), and CTD-α (⊙) have lower structure content than ID (☆) and CTD-β (half-filled circles) (see Table 1 for quantitation).","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T12:20:53.516Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":210,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Unique physical properties and interactions of the domains of methylated DNA binding protein 2. <i> Ghosh RP, Ghosh RP, Nikitina T, Horowitz-Scherer RA, Gierasch LM, Uversky VN, Hite K, Hansen JC, Woodcock CL. </i> Biochemistry, 2010","term_id":"GO:0060090","curator_id":"eleonardi","start":165,"term_ontology":"GO","curator_name":"Emanuela Leonardi","reference_id":"20405910","version":4,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00539r008","statement":[{"text":"We also investigated interdomain associations intrans using CD, which can detect changes in secondary structure of one or both components in a mixture of the two (63).","type":"Results"},{"text":"With the NTD+MBD, MBD+ID, and MBD+TRD mixtures, we observed a clear difference between the summed individual CD spectra and the spectrum of an equimolar mixture (Figure 7b,c), indicating that an interaction between domains led to change(s) in secondary structure.","type":"Results"},{"text":"ID domain includes 165-210 residues","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T12:21:30.347Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":486,"region_id":"DP00539r009","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Unique physical properties and interactions of the domains of methylated DNA binding protein 2. <i> Ghosh RP, Ghosh RP, Nikitina T, Horowitz-Scherer RA, Gierasch LM, Uversky VN, Hite K, Hansen JC, Woodcock CL. </i> Biochemistry, 2010","term_id":"IDPO:0000002","curator_id":"eleonardi","start":335,"term_ontology":"IDPO","curator_name":"Emanuela Leonardi","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20405910","statement":[{"text":"To construct the MBD (residues 75−164), ID (residues 165−210), TRD (residues 207−310), CTD-α (residues 261−330), and CTD-β (residues 335−486), we engineered amplicons with 5′ NdeI and 3′ EcoRI linkers","type":"Methods"},{"text":"Figure 2. Circular dichroism spectra of MeCP2 domains reveal marked differences in secondary structure content. CD spectra are representative of two to four separate acquisitions. (a) Compared to the 195 nm peak indicative of β-sheet structure within the MBD (◼), all the other domains show a negative band in the 195−198 nm region indicative of disorder. NTD (●), TRD (○), and CTD-α (⊙) have lower structure content than ID (☆) and CTD-β (half-filled circles) (see Table 1 for quantitation).","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T12:20:52.280Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":330,"region_id":"DP00539r010","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Unique physical properties and interactions of the domains of methylated DNA binding protein 2. <i> Ghosh RP, Ghosh RP, Nikitina T, Horowitz-Scherer RA, Gierasch LM, Uversky VN, Hite K, Hansen JC, Woodcock CL. </i> Biochemistry, 2010","term_id":"IDPO:0000002","curator_id":"eleonardi","start":261,"term_ontology":"IDPO","curator_name":"Emanuela Leonardi","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20405910","statement":[{"text":"To construct the MBD (residues 75−164), ID (residues 165−210), TRD (residues 207−310), CTD-α (residues 261−330), and CTD-β (residues 335−486), we engineered amplicons with 5′ NdeI and 3′ EcoRI linkers","type":"Methods"},{"text":"Figure 2. Circular dichroism spectra of MeCP2 domains reveal marked differences in secondary structure content. CD spectra are representative of two to four separate acquisitions. (a) Compared to the 195 nm peak indicative of β-sheet structure within the MBD (◼), all the other domains show a negative band in the 195−198 nm region indicative of disorder. NTD (●), TRD (○), and CTD-α (⊙) have lower structure content than ID (☆) and CTD-β (half-filled circles) (see Table 1 for quantitation)","type":"Figure"},{"text":"Of the six domains, the MBD was the only one showing a characteristic positive band in its CD spectrum at ∼197 nm, indicative of significant ordered secondary structure (Figure 2a). The others had a negative band in this region, indicating extensive disorder, with the NTD and TRD being the most strongly disordered","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T06:55:49.836Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":165,"end":210,"reference_id":"20405910","reference_source":"pmid","reference_html":"Unique physical properties and interactions of the domains of methylated DNA binding protein 2. <i> Ghosh RP, Ghosh RP, Nikitina T, Horowitz-Scherer RA, Gierasch LM, Uversky VN, Hite K, Hansen JC, Woodcock CL. </i> Biochemistry, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00539r011","statement":[{"text":"(b) Addition of DNA (methylated as well as unmethylated) to the ID induces changes typical of the formation of β-structure, namely a marked increase in positive ellipticity at 195 nm and negative ellipticity in the 220−225 nm range.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-02T12:52:17.892Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":207,"end":310,"reference_id":"20405910","reference_source":"pmid","reference_html":"Unique physical properties and interactions of the domains of methylated DNA binding protein 2. <i> Ghosh RP, Ghosh RP, Nikitina T, Horowitz-Scherer RA, Gierasch LM, Uversky VN, Hite K, Hansen JC, Woodcock CL. </i> Biochemistry, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00539r012","statement":[{"text":"(c) Addition of DNA (methylated as well as unmethylated) to the TRD results in an increase in the level of order irrespective of the methylation status of the DNA.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-02T12:53:03.756Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":335,"end":355,"reference_id":"17371874","reference_source":"pmid","reference_html":"Intrinsic disorder and autonomous domain function in the multifunctional nuclear protein, MeCP2. <i> Adams VH, McBryant SJ, Wade PA, Woodcock CL, Hansen JC. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00539r013","statement":[{"text":"The trypsin-resistant bands were excised from the gel and subjected to Edman sequencing. N-terminal sequences were obtained for bands 1-4 and band 6.","type":"Results"},{"text":"Even without positive identification of the C-terminal residues, it is apparent that the protease-resistant MeCP2 regions overlapped with the MBD, TRD, and C-terminal residues 355-486. Correspondingly, residues in the region between the MBD and TRD, as well as sites near residues 310 and 355, were relative hot spots for trypsin digestion.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T06:53:49.966Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":165,"end":210,"reference_id":"17371874","reference_source":"pmid","reference_html":"Intrinsic disorder and autonomous domain function in the multifunctional nuclear protein, MeCP2. <i> Adams VH, McBryant SJ, Wade PA, Woodcock CL, Hansen JC. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00539r014","statement":[{"text":"The trypsin-resistant bands were excised from the gel and subjected to Edman sequencing. N-terminal sequences were obtained for bands 1-4 and band 6.","type":"Results"},{"text":"Even without positive identification of the C-terminal residues, it is apparent that the protease-resistant MeCP2 regions overlapped with the MBD, TRD, and C-terminal residues 355-486. Correspondingly, residues in the region between the MBD and TRD, as well as sites near residues 310 and 355, were relative hot spots for trypsin digestion.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T06:53:46.877Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":293,"end":310,"reference_id":"17371874","reference_source":"pmid","reference_html":"Intrinsic disorder and autonomous domain function in the multifunctional nuclear protein, MeCP2. <i> Adams VH, McBryant SJ, Wade PA, Woodcock CL, Hansen JC. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00539r015","statement":[{"text":"The trypsin-resistant bands were excised from the gel and subjected to Edman sequencing. N-terminal sequences were obtained for bands 1-4 and band 6. The C-terminal ends of these bands could only be estimated from sizes returned by SDS-PAGE as we were unable to obtain masses from mass spectroscopy. These estimates took into account the anomalously high masses returned by SDS-PAGE.","type":"Results"},{"text":"Even without positive identification of the C-terminal residues, it is apparent that the protease-resistant MeCP2 regions overlapped with the MBD, TRD, and C-terminal residues 355-486. Correspondingly, residues in the region between the MBD and TRD, as well as sites near residues 310 and 355, were relative hot spots for trypsin digestion.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T06:53:26.985Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":168,"end":486,"reference_id":"32698189","reference_source":"pmid","reference_html":"MeCP2 links heterochromatin condensates and neurodevelopmental disease. <i> Li CH, Coffey EL, Dall'Agnese A, Hannett NM, Tang X, Henninger JE, Platt JM, Oksuz O, Zamudio AV, Afeyan LK, Schuijers J, Liu XS, Markoulaki S, Lungjangwa T, LeRoy G, Svoboda DS, Wogram E, Lee TI, Jaenisch R, Young RA. </i> Nature, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00539r016","statement":[{"text":"We conducted droplet formation assays using physiologically relevant concentrations of recombinant MeCP2–GFP domain deletion mutant proteins in the presence of DNA. Although mutant proteins that lack the N-terminal IDR (ΔIDR-1) formed droplets, those that lack the C-terminal IDR (ΔIDR-2) did not (Fig. 2b–d). Furthermore, IDR-1 alone did not form droplets, whereas IDR-2 alone did—albeit with diminished size and number relative to both full-length and mutant ΔIDR-1 proteins (Fig. 2b–d).","type":"Results"},{"text":"MeCP2 full length (WT): residues 1-486; MeCP2 ΔIDR-1: residues 78-486; MeCP2 ΔIDR-2 (R168X): residues 1-167; MeCP2 IDR-1: residues 1-77; MeCP2 IDR-2: residues 168-486; MeCP2 ΔBasic: residues 1-486, removing IDR-2 basic patches (residues 170-181, 184-194, 246-258, 263-274, 282-289, 301-310, and 340-348); MeCP2 ΔAromatic: residues 1-486, removing IDR-2 aromatic residues (F226 and Y450); MeCP2 ΔHistidine: residues 1-486, removing IDR-2 histidine-rich domain (residues 366-372); MeCP2 ΔProline: residues 1-486, removing IDR-2 proline-rich domain (residues 376-405); MeCP2 R133C: residues 1-486, R133C; MeCP2 T158M: residues 1-486, T158M; MeCP2 P225R: residues 1-486, P225R MeCP2 R255X: residues 1-254; MeCP2 R270X: residues 1-269; MeCP2 R294X: residues 1-293; MeCP2 R306C: residues 1-486, R306C; MeCP2 P322L: residues 1-486, P322L; MeCP2 P389X: residues 1-288; MeCP2 Mini: as in the ΔNIC mutant from ref. 22.","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T12:21:24.487Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":285,"end":313,"reference_id":"28348241","reference_source":"pmid","reference_html":"Structure of the MeCP2-TBLR1 complex reveals a molecular basis for Rett syndrome and related disorders. <i> Kruusvee V, Lyst MJ, Taylor C, Tarnauskaitė Ž, Bird AP, Cook AG. </i> Proc Natl Acad Sci U S A, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006077","ec_ontology":"ECO","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"O60907","partner_start":null,"partner_end":null}],"region_id":"DP00539r017","statement":[{"text":"TBL1 WD40 domain was efficiently pulled down by wild-type NID but not by RTT mutant peptides or a peptide containing phosphoThr308, a modification known to interfere with NID binding (24) (Fig. 2C). ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T07:09:18.903Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":285,"end":313,"reference_id":"32698189","reference_source":"pmid","reference_html":"MeCP2 links heterochromatin condensates and neurodevelopmental disease. <i> Li CH, Coffey EL, Dall'Agnese A, Hannett NM, Tang X, Henninger JE, Platt JM, Oksuz O, Zamudio AV, Afeyan LK, Schuijers J, Liu XS, Markoulaki S, Lungjangwa T, LeRoy G, Svoboda DS, Wogram E, Lee TI, Jaenisch R, Young RA. </i> Nature, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00539r018","statement":[{"text":"The R306C mutation was previously shown to disrupt an interaction between the MeCP2 NCoR-interaction domain (NID) and TBLR1—a subunit of the NCoR co-repressor complex13,21. We therefore examined the ability of R306C mutant condensates to incorporate the C-terminal domain of TBLR1 (TBLR1-CTD), which directly interacts with the NID21. Wild-type MeCP2 droplets readily enriched TBLR1-CTD–mCherry, whereas R306C mutant droplets showed less enrichment (Extended Data Fig. 7), which suggests that MeCP2 condensates can contribute to NID-mediated recruitment of NCoR, a key MeCP2 function previously shown to be disrupted in Rett syndrome13,21. These results suggest that missense mutations in IDR-2 that occur in patients with Rett syndrome contribute to condensate disruption.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T07:09:45.802Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":285,"end":309,"reference_id":"28348241","reference_source":"pmid","reference_html":"Structure of the MeCP2-TBLR1 complex reveals a molecular basis for Rett syndrome and related disorders. <i> Kruusvee V, Lyst MJ, Taylor C, Tarnauskaitė Ž, Bird AP, Cook AG. </i> Proc Natl Acad Sci U S A, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000269","ec_ontology":"ECO","ec_name":"experimental evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"Q9BZK7","partner_start":null,"partner_end":null}],"region_id":"DP00539r019","statement":[{"text":"Here, we show that the “NCoR/SMRT interaction domain” (NID) of MeCP2 directly contacts transducin beta-like 1 (TBL1) and TBL1 related (TBLR1), two paralogs that are core components of NCoR/SMRT. We determine the cocrystal structure of the MeCP2 NID in complex with the WD40 domain of TBLR1 and confirm by in vitro and ex vivo assays that mutation of interacting residues of TBLR1 and TBL1 disrupts binding to MeCP2.","type":"Abstract"},{"text":"Fluorescence anisotropy binding with a minimal 11-mer peptide of MeCP2 (residues 298–309). Anisotropy is measured in arbitrary units (A.U.).","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T12:21:07.018Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":285,"end":309,"reference_id":"28348241","reference_source":"pmid","reference_html":"Structure of the MeCP2-TBLR1 complex reveals a molecular basis for Rett syndrome and related disorders. <i> Kruusvee V, Lyst MJ, Taylor C, Tarnauskaitė Ž, Bird AP, Cook AG. </i> Proc Natl Acad Sci U S A, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"Q9BZK7","partner_start":null,"partner_end":null}],"region_id":"DP00539r020","statement":[{"text":"Using surface plasmon resonance (SPR), we measured binding constants (KDs) for alternative NID peptides (NIDs, residues 285–309; or NID, residues 285–313) with the mouse TBLR1-CTD (residues 134–514) (Fig. 2D and Fig. S2B). Wild-type TBLR1-CTD bound MeCP2 NID and MeCP2 NIDS with apparent KDs of 9.5 ± 0.5 μM and 12.9 ± 0.8 μM, respectively.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T07:08:04.460Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":207,"end":310,"reference_id":"20405910","reference_source":"pmid","reference_html":"Unique physical properties and interactions of the domains of methylated DNA binding protein 2. <i> Ghosh RP, Ghosh RP, Nikitina T, Horowitz-Scherer RA, Gierasch LM, Uversky VN, Hite K, Hansen JC, Woodcock CL. </i> Biochemistry, 2010","date":"2022-03-08T15:32:40.801Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0003676","term_name":"nucleic acid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","released":"2022_03","version":4,"region_id":"DP00539r021","statement":[{"text":"Among the individual domains, the NTD and CTD-β stand out as inducing only very minor mobility shifts in DNA, whereas the ID, TRD, and CTD-α fragments all induce marked shifts (Figure 3a).","type":"Results"},{"text":"From table 1 TRD spans 207-310","type":"Curator statement"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"Rfam","id":"URS000072BE72_9606","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T16:52:21.825Z"}}],"released":"2016_10","uniref100":"UniRef100_P51608","date":"2016-09-09T16:12:04.000Z","acc":"P51608","name":"Methyl-CpG-binding protein 2","length":486,"organism":"Homo sapiens","dataset":["NDDs-related proteins","Condensates-related proteins","Age-related disorders proteins"],"UniParc":"UPI000012EEA5","genes":[{"name":{"value":"MECP2"}}],"alphafold_very_low_content":0.41358024691358025,"disorder_content":0.808641975308642,"disprot_consensus":{"full":[{"start":1,"end":75,"type":"D"},{"start":165,"end":310,"type":"T"},{"start":311,"end":330,"type":"D"},{"start":331,"end":334,"type":"F"},{"start":335,"end":486,"type":"D"}],"Structural state":[{"start":1,"end":75,"type":"D"},{"start":165,"end":330,"type":"D"},{"start":335,"end":486,"type":"D"}],"Molecular function":[{"start":165,"end":486,"type":"F"}],"Structural transition":[{"start":165,"end":310,"type":"T"}]}},{"features":{"pfam":[{"id":"PF17903","name":"Krr1 KH1 domain","start":40,"end":120},{"id":"PF21800","name":"KRR1 small subunit processome component, second KH domain","start":123,"end":212}],"gene3D":[{"start":34,"end":120,"id":"3.30.1370.10","name":"K Homology domain, type 1"},{"start":121,"end":223,"id":"3.30.1370.10","name":"K Homology domain, type 1"}]},"uniref50":"UniRef50_Q9VPU8","sequence":"MSESEAEETKISTEPVDNAWSMKIPAFRQEDNPHGMVEESSFATLFPKYRERYLKEVWPLVEQCLAEHHLKAELDLMEGSMVVKTSRKTWDPYIIIKARDMIKLMARSVPFEQAKRVLQDDIGCDIIKIGNLVHKKEKFVKRRQRLIGPNGATLKSIELLTDCYVLVQGNTVSALGPYKGLQQVRDIVLETMNNVHPIYNIKALMIKRELMKDPRLANEDWSRFLPKFKNKNISKRKQPKVKKQKKEYTPFPPSQPESKVDKQLASGEYFLNQEQKQAKRNQERTEKQKEAAKRQDERRNKDFVPPTEESAASSRKKEDGSSSSKVDVKALKAKLIKANKKARSS","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_Q9VPU8","disprot_id":"DP00540","ncbi_taxon_id":7227,"regions_counter":10,"creator":"wvranken","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":345,"region_id":"DP00540r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Biophysical characterisation reveals structural disorder in the nucleolar protein, Dribble. <i> Yiu CP, Beavil RL, Chan HY. </i> Biochem Biophys Res Commun, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16542639","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":345,"region_id":"DP00540r003","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Biophysical characterisation reveals structural disorder in the nucleolar protein, Dribble. <i> Yiu CP, Beavil RL, Chan HY. </i> Biochem Biophys Res Commun, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16542639","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":345,"region_id":"DP00540r005","released":"2022_03","ec_id":"ECO:0001249","reference_html":"Biophysical characterisation reveals structural disorder in the nucleolar protein, Dribble. <i> Yiu CP, Beavil RL, Chan HY. </i> Biochem Biophys Res Commun, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16542639","version":2,"ec_name":"fluorescence evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":345,"region_id":"DP00540r007","released":"2022_03","ec_id":"ECO:0006275","reference_html":"Biophysical characterisation reveals structural disorder in the nucleolar protein, Dribble. <i> Yiu CP, Beavil RL, Chan HY. </i> Biochem Biophys Res Commun, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16542639","version":2,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":345,"region_id":"DP00540r009","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Biophysical characterisation reveals structural disorder in the nucleolar protein, Dribble. <i> Yiu CP, Beavil RL, Chan HY. </i> Biochem Biophys Res Commun, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16542639","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q9VPU8","date":"2016-08-25T17:22:09.000Z","acc":"Q9VPU8","name":"KRR1 small subunit processome component homolog","length":345,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI000007DBB7","genes":[{"name":{"value":"dbe"},"synonyms":[{"value":"dribble","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11359931","url":"http://www.ncbi.nlm.nih.gov/pubmed/11359931","alternativeUrl":"https://europepmc.org/abstract/MED/11359931"}},{"code":"ECO:0000312","source":{"name":"EMBL","id":"CAB09659.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAB09659.1"}}]}],"orfNames":[{"value":"CG4258"}]}],"alphafold_very_low_content":0.06376811594202898,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":345,"type":"D"}],"Structural state":[{"start":1,"end":345,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02318","name":"FYVE-type zinc finger","start":8,"end":125},{"id":"PF04698","name":"Rab effector MyRIP/melanophilin C-terminus","start":445,"end":497}],"gene3D":[{"start":1,"end":146,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"}]},"uniref50":"UniRef50_Q91V27","sequence":"MGKRLDLSTLTDEEAEHVWAVVQRDFDLRRREEERLQGLKGKIQKESSKRELLSDTAHLNETHCARCLQPYRLLLNSRRQCLECSLFVCKSCSHAHPEEQGWLCDPCHLARVVKIGSLEWYYQHVRARFKRFGSAKVIRSLCGRLQGGGGSEPSLEEGNGDSEQTDEDGDLDTEARDQPLNSKKKKRLLSFRDVDFEEDSDHLVQPCSQTLGLSSVPESAHSLQSLSGEPYSEDTTSLEPEGLEETGARALGCRPSPEVQPCSPLPSGEDAHAELDSPAASCKSAFGTTAMPGTDDVRGKHLPSQYLADVDTSDEDSIQGPRAASQHSKRRARTVPETQILELNKRMSAVEHLLVHLENTVLPPSAQEPTVETHPSADTEEETLRRRLEELTSNISGSSTSSEDETKPDGTFLGGSPKVCTDTGHMETQERNPRSPGNPARPTKSTDEELSEMEDRVAMTASEVQQAESEISDIESRIAALRAAGLTVKPSGKPRRKSGIPIFLPRVTEKLDRIPKTPPADPDDQAKMPKATTAVPSLLRRKYSPSSQGVDSGSFDRKSVYRGSLTQRNPNGRRGTARHIFAKPVMAQQP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q91V27","disprot_id":"DP00541","ncbi_taxon_id":10090,"regions_counter":15,"creator":"wvranken","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":403,"region_id":"DP00541r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin. <i> Geething NC, Spudich JA. </i> J Biol Chem, 2007","term_id":"IDPO:0000002","curator_id":"wvranken","start":147,"term_ontology":"IDPO","curator_name":"Wim Vranken","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17513864","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":403,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin. <i> Geething NC, Spudich JA. </i> J Biol Chem, 2007","term_id":"GO:0060090","curator_id":"wvranken","start":147,"term_ontology":"GO","curator_name":"Wim Vranken","reference_id":"17513864","version":3,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00541r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":403,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin. <i> Geething NC, Spudich JA. </i> J Biol Chem, 2007","term_id":"GO:0005515","curator_id":"wvranken","start":147,"term_ontology":"GO","curator_name":"Wim Vranken","reference_id":"17513864","version":3,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00541r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":403,"region_id":"DP00541r004","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin. <i> Geething NC, Spudich JA. </i> J Biol Chem, 2007","term_id":"IDPO:0000002","curator_id":"wvranken","start":147,"term_ontology":"IDPO","curator_name":"Wim Vranken","ec_name":"chromatography evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17513864","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":403,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"chromatography evidence used in manual assertion","reference_html":"Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin. <i> Geething NC, Spudich JA. </i> J Biol Chem, 2007","term_id":"GO:0060090","curator_id":"wvranken","start":147,"term_ontology":"GO","curator_name":"Wim Vranken","reference_id":"17513864","version":3,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","region_id":"DP00541r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":403,"term_name":"protein binding","released":"2022_03","ec_name":"chromatography evidence used in manual assertion","reference_html":"Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin. <i> Geething NC, Spudich JA. </i> J Biol Chem, 2007","term_id":"GO:0005515","curator_id":"wvranken","start":147,"term_ontology":"GO","curator_name":"Wim Vranken","reference_id":"17513864","version":3,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","region_id":"DP00541r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":403,"region_id":"DP00541r007","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin. <i> Geething NC, Spudich JA. </i> J Biol Chem, 2007","term_id":"IDPO:0000002","curator_id":"wvranken","start":147,"term_ontology":"IDPO","curator_name":"Wim Vranken","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17513864","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":403,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","reference_html":"Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin. <i> Geething NC, Spudich JA. </i> J Biol Chem, 2007","term_id":"GO:0060090","curator_id":"wvranken","start":147,"term_ontology":"GO","curator_name":"Wim Vranken","reference_id":"17513864","version":3,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","region_id":"DP00541r008","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":403,"term_name":"protein binding","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","reference_html":"Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin. <i> Geething NC, Spudich JA. </i> J Biol Chem, 2007","term_id":"GO:0005515","curator_id":"wvranken","start":147,"term_ontology":"GO","curator_name":"Wim Vranken","reference_id":"17513864","version":3,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","region_id":"DP00541r009","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":403,"region_id":"DP00541r010","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin. <i> Geething NC, Spudich JA. </i> J Biol Chem, 2007","term_id":"IDPO:0000002","curator_id":"wvranken","start":147,"term_ontology":"IDPO","curator_name":"Wim Vranken","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17513864","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":403,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin. <i> Geething NC, Spudich JA. </i> J Biol Chem, 2007","term_id":"GO:0060090","curator_id":"wvranken","start":147,"term_ontology":"GO","curator_name":"Wim Vranken","reference_id":"17513864","version":3,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00541r011","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":403,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin. <i> Geething NC, Spudich JA. </i> J Biol Chem, 2007","term_id":"GO:0005515","curator_id":"wvranken","start":147,"term_ontology":"GO","curator_name":"Wim Vranken","reference_id":"17513864","version":3,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00541r012","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":403,"region_id":"DP00541r013","released":"2022_03","ec_id":"ECO:0007064","reference_html":"Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin. <i> Geething NC, Spudich JA. </i> J Biol Chem, 2007","term_id":"IDPO:0000002","curator_id":"wvranken","start":147,"term_ontology":"IDPO","curator_name":"Wim Vranken","ec_name":"dynamic light scattering assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17513864","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":403,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"dynamic light scattering assay evidence used in manual assertion","reference_html":"Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin. <i> Geething NC, Spudich JA. </i> J Biol Chem, 2007","term_id":"GO:0060090","curator_id":"wvranken","start":147,"term_ontology":"GO","curator_name":"Wim Vranken","reference_id":"17513864","version":3,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007064","region_id":"DP00541r014","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":403,"term_name":"protein binding","released":"2022_03","ec_name":"dynamic light scattering assay evidence used in manual assertion","reference_html":"Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin. <i> Geething NC, Spudich JA. </i> J Biol Chem, 2007","term_id":"GO:0005515","curator_id":"wvranken","start":147,"term_ontology":"GO","curator_name":"Wim Vranken","reference_id":"17513864","version":3,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007064","region_id":"DP00541r015","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q91V27","date":"2016-09-13T13:20:29.000Z","acc":"Q91V27","name":"Melanophilin","length":590,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000E82B2","genes":[{"name":{"value":"Mlph"},"synonyms":[{"value":"Ln"},{"value":"Slac2a"}]}],"alphafold_very_low_content":0.5288135593220339,"disorder_content":0.43559322033898307,"disprot_consensus":{"full":[{"start":147,"end":403,"type":"D"}],"Structural state":[{"start":147,"end":403,"type":"D"}],"Molecular function":[{"start":147,"end":403,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05051","name":"Cytochrome C oxidase copper chaperone (COX17)","start":19,"end":63}],"gene3D":[{"start":1,"end":63,"id":"1.10.287.1130","name":"CytochromE C oxidase copper chaperone"}]},"uniref50":"UniRef50_Q14061","sequence":"MPGLVDSNPAPPESQEKKPLKPCCACPETKKARDACIIEKGEEHCGHLIEAHKECMRALGFKI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q14061","disprot_id":"DP00543","ncbi_taxon_id":9606,"regions_counter":24,"creator":"ameszaros","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":29,"region_id":"DP00543r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A structural-dynamical characterization of human Cox17. <i> Banci L, Bertini I, Ciofi-Baffoni S, Janicka A, Martinelli M, Kozlowski H, Palumaa P. </i> J Biol Chem, 2008","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"18093982","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2RN9"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":29,"term_name":"entropic chain","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"18093982","version":3,"reference_html":"A structural-dynamical characterization of human Cox17. <i> Banci L, Bertini I, Ciofi-Baffoni S, Janicka A, Martinelli M, Kozlowski H, Palumaa P. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0006165","region_id":"DP00543r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":29,"term_name":"ion binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"18093982","version":3,"reference_html":"A structural-dynamical characterization of human Cox17. <i> Banci L, Bertini I, Ciofi-Baffoni S, Janicka A, Martinelli M, Kozlowski H, Palumaa P. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0043167","ec_id":"ECO:0006165","region_id":"DP00543r004","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":17,"region_id":"DP00543r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A structural-dynamical characterization of human Cox17. <i> Banci L, Bertini I, Ciofi-Baffoni S, Janicka A, Martinelli M, Kozlowski H, Palumaa P. </i> J Biol Chem, 2008","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"18093982","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2RN9"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":17,"term_name":"entropic chain","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"18093982","version":3,"reference_html":"A structural-dynamical characterization of human Cox17. <i> Banci L, Bertini I, Ciofi-Baffoni S, Janicka A, Martinelli M, Kozlowski H, Palumaa P. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0006165","region_id":"DP00543r007","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":17,"term_name":"ion binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"18093982","version":3,"reference_html":"A structural-dynamical characterization of human Cox17. <i> Banci L, Bertini I, Ciofi-Baffoni S, Janicka A, Martinelli M, Kozlowski H, Palumaa P. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0043167","ec_id":"ECO:0006165","region_id":"DP00543r008","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":63,"region_id":"DP00543r014","released":"2022_03","ec_id":"ECO:0006204","reference_html":"A structural-dynamical characterization of human Cox17. <i> Banci L, Bertini I, Ciofi-Baffoni S, Janicka A, Martinelli M, Kozlowski H, Palumaa P. </i> J Biol Chem, 2008","statement":[{"text":"The far-UV CD spectra of reduced hCox17 displays much\nlower ellipticity and a minimum at 205 nm consistent with a mostly disordered structure. This lack of structural transition is in agreement with the NMR and FTIR data, supporting hCox17 being mostly disordered in the reduced state.","type":"Results"}],"term_id":"IDPO:0000003","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"18093982","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"molten globule","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":60,"region_id":"DP00543r016","released":"2022_03","ec_id":"ECO:0006204","reference_html":"A structural-dynamical characterization of human Cox17. <i> Banci L, Bertini I, Ciofi-Baffoni S, Janicka A, Martinelli M, Kozlowski H, Palumaa P. </i> J Biol Chem, 2008","statement":[{"text":"The far-UV CD spectra of reduced hCox17 displays much\nlower ellipticity and a minimum at 205 nm consistent with a mostly disordered structure. This lack of structural transition is in agreement with the NMR and FTIR data, supporting hCox17 being mostly disordered in the reduced state.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ameszaros","start":25,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"18093982","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":60,"term_name":"disorder to order","start":25,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"The far-UV circular dichroism (CD) of native hCox17 is typical of an α-helix containing protein. The far-UV CD spectra of reduced hCox17 displays much\nlower ellipticity and a minimum at 205 nm consistent with a mostly disordered structure.","type":"Results"}],"curator_id":"ameszaros","released":"2022_03","term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"18093982","version":2,"reference_html":"A structural-dynamical characterization of human Cox17. <i> Banci L, Bertini I, Ciofi-Baffoni S, Janicka A, Martinelli M, Kozlowski H, Palumaa P. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00543r017","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":63,"region_id":"DP00543r018","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Disulfide driven folding for a conditionally disordered protein. <i> Fraga H, Pujols J, Gil-Garcia M, Roque A, Bernardo-Seisdedos G, Santambrogio C, Bech-Serra JJ, Canals F, Bernadó P, Grandori R, Millet O, Ventura S. </i> Sci Rep, 2017","statement":[{"text":"This lack of structural transition is in agreement with the NMR and FTIR data, supporting hCox17 being mostly disordered in the reduced state.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ameszaros","start":1,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"29208936","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":60,"region_id":"DP00543r019","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Disulfide driven folding for a conditionally disordered protein. <i> Fraga H, Pujols J, Gil-Garcia M, Roque A, Bernardo-Seisdedos G, Santambrogio C, Bech-Serra JJ, Canals F, Bernadó P, Grandori R, Millet O, Ventura S. </i> Sci Rep, 2017","statement":[{"text":"This lack of structural transition is in agreement with the NMR and FTIR data, supporting hCox17 being mostly disordered in the reduced state.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ameszaros","start":25,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"29208936","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":60,"term_name":"disorder to order","start":25,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"The spectra of the reduced form is typical to disordered protein while the oxidized one is more heterogeneious, like for globular protein.","type":"Results"}],"curator_id":"ameszaros","released":"2022_03","term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"29208936","version":2,"reference_html":"Disulfide driven folding for a conditionally disordered protein. <i> Fraga H, Pujols J, Gil-Garcia M, Roque A, Bernardo-Seisdedos G, Santambrogio C, Bech-Serra JJ, Canals F, Bernadó P, Grandori R, Millet O, Ventura S. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00543r020","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":63,"region_id":"DP00543r021","released":"2022_03","ec_id":"ECO:0006228","reference_html":"Disulfide driven folding for a conditionally disordered protein. <i> Fraga H, Pujols J, Gil-Garcia M, Roque A, Bernardo-Seisdedos G, Santambrogio C, Bech-Serra JJ, Canals F, Bernadó P, Grandori R, Millet O, Ventura S. </i> Sci Rep, 2017","statement":[{"text":"This lack of structural transition is in agreement with the NMR and FTIR data, supporting hCox17 being mostly disordered in the reduced state.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ameszaros","start":1,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"29208936","version":2,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":63,"region_id":"DP00543r022","released":"2022_03","ec_id":"ECO:0006228","reference_html":"Disulfide driven folding for a conditionally disordered protein. <i> Fraga H, Pujols J, Gil-Garcia M, Roque A, Bernardo-Seisdedos G, Santambrogio C, Bech-Serra JJ, Canals F, Bernadó P, Grandori R, Millet O, Ventura S. </i> Sci Rep, 2017","statement":[{"text":"This lack of structural transition is in agreement with the NMR and FTIR data, supporting hCox17 being mostly disordered in the reduced state.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ameszaros","start":25,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"29208936","version":2,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":63,"term_name":"disorder to order","start":25,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","statement":[{"text":"Tese results agree with the Fourier transform infrared spectroscopy (FTIR) spectrum of DTT treated hCox17 in the amide I region, which evidences the lack of signifcant regular secondary structure, whereas the FTIR of spectrum of native hCox17 contains a 44% α-helical content.","type":"Results"}],"curator_id":"ameszaros","released":"2022_03","term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"29208936","version":2,"reference_html":"Disulfide driven folding for a conditionally disordered protein. <i> Fraga H, Pujols J, Gil-Garcia M, Roque A, Bernardo-Seisdedos G, Santambrogio C, Bech-Serra JJ, Canals F, Bernadó P, Grandori R, Millet O, Ventura S. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006228","region_id":"DP00543r023","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":63,"region_id":"DP00543r024","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Disulfide driven folding for a conditionally disordered protein. <i> Fraga H, Pujols J, Gil-Garcia M, Roque A, Bernardo-Seisdedos G, Santambrogio C, Bech-Serra JJ, Canals F, Bernadó P, Grandori R, Millet O, Ventura S. </i> Sci Rep, 2017","statement":[{"text":"This lack of structural transition is in agreement with the NMR and FTIR data, supporting hCox17 being mostly disordered in the reduced state.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ameszaros","start":1,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"29208936","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q14061","date":"2016-08-16T07:41:11.000Z","acc":"Q14061","name":"Cytochrome c oxidase copper chaperone","length":63,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000013D132","genes":[{"name":{"value":"COX17"}}],"alphafold_very_low_content":0.20634920634920634,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":24,"type":"D"},{"start":25,"end":63,"type":"T"}],"Structural state":[{"start":1,"end":63,"type":"D"}],"Disorder function":[{"start":1,"end":29,"type":"F"}],"Molecular function":[{"start":1,"end":29,"type":"F"}],"Structural transition":[{"start":25,"end":63,"type":"T"}]}},{"features":{"pfam":[{"id":"PF10169","name":"LLP homolog","start":3,"end":113}]},"uniref50":"UniRef50_B0FRH7","sequence":"MAKSIRSKHRRQMRNVKREHFAKKDLDRLKRLASKAQELDLDNVVTMKSAEEIKNKPSTSASDADKGMEVDNTKKVFKKKTQQNEDGHYPQWMNQRAVKKQKVKVAKLKTKKKIGKKIKW","taxonomy":["Eukaryota","Metazoa","Spiralia","Lophotrochozoa","Mollusca","Gastropoda","Heterobranchia","Euthyneura","Euopisthobranchia","Aplysiida","Aplysioidea","Aplysiidae","Aplysia"],"uniref90":"UniRef90_B0FRH7","disprot_id":"DP00544","ncbi_taxon_id":6501,"regions_counter":6,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":120,"region_id":"DP00544r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A novel nucleolar transcriptional activator ApLLP for long-term memory formation is intrinsically unstructured but functionally active. <i> Liu J, Song J. </i> Biochem Biophys Res Commun, 2008","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18078811","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":120,"term_name":"nucleic acid binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18078811","version":3,"reference_html":"A novel nucleolar transcriptional activator ApLLP for long-term memory formation is intrinsically unstructured but functionally active. <i> Liu J, Song J. </i> Biochem Biophys Res Commun, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006165","region_id":"DP00544r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":120,"region_id":"DP00544r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"A novel nucleolar transcriptional activator ApLLP for long-term memory formation is intrinsically unstructured but functionally active. <i> Liu J, Song J. </i> Biochem Biophys Res Commun, 2008","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18078811","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":120,"term_name":"nucleic acid binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18078811","version":3,"reference_html":"A novel nucleolar transcriptional activator ApLLP for long-term memory formation is intrinsically unstructured but functionally active. <i> Liu J, Song J. </i> Biochem Biophys Res Commun, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006204","region_id":"DP00544r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":120,"region_id":"DP00544r005","released":"2022_03","ec_id":"ECO:0006206","reference_html":"A novel nucleolar transcriptional activator ApLLP for long-term memory formation is intrinsically unstructured but functionally active. <i> Liu J, Song J. </i> Biochem Biophys Res Commun, 2008","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18078811","version":2,"ec_name":"near-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":120,"term_name":"nucleic acid binding","start":1,"ec_name":"near-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18078811","version":3,"reference_html":"A novel nucleolar transcriptional activator ApLLP for long-term memory formation is intrinsically unstructured but functionally active. <i> Liu J, Song J. </i> Biochem Biophys Res Commun, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006206","region_id":"DP00544r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_B0FRH7","date":"2016-08-16T12:00:25.000Z","acc":"B0FRH7","name":"Protein LLP","length":120,"organism":"Aplysia kurodai","dataset":[],"UniParc":"UPI0000603344","genes":[{"name":{"value":"LLP","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12759182","url":"http://www.ncbi.nlm.nih.gov/pubmed/12759182","alternativeUrl":"https://europepmc.org/abstract/MED/12759182"}}]}}],"alphafold_very_low_content":0.09166666666666666,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":120,"type":"D"}],"Structural state":[{"start":1,"end":120,"type":"D"}],"Molecular function":[{"start":1,"end":120,"type":"F"}]}},{"features":{"pfam":[{"id":"PF19026","name":"HYPK UBA domain","start":80,"end":120}]},"uniref50":"UniRef50_Q9NX55","sequence":"MATEGDVELELETETSGPERPPEKPRKHDSGAADLERVTDYAEEKEIQSSNLETAMSVIGDRRSREQKAKQEREKELAKVTIKKEDLELIMTEMEISRAAAERSLREHMGNVVEALIALTN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9NX55","disprot_id":"DP00546","ncbi_taxon_id":9606,"regions_counter":10,"creator":"wvranken","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":121,"region_id":"DP00546r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Huntingtin interacting protein HYPK is intrinsically unstructured. <i> Raychaudhuri S, Majumder P, Sarkar S, Giri K, Mukhopadhyay D, Bhattacharyya NP. </i> Proteins, 2008","term_id":"IDPO:0000004","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18076027","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"pre-molten globule","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":121,"term_name":"protein folding chaperone","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18076027","version":3,"reference_html":"Huntingtin interacting protein HYPK is intrinsically unstructured. <i> Raychaudhuri S, Majumder P, Sarkar S, Giri K, Mukhopadhyay D, Bhattacharyya NP. </i> Proteins, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0044183","ec_id":"ECO:0006204","region_id":"DP00546r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":121,"term_name":"pre-molten globule to molten globule","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18076027","version":2,"reference_html":"Huntingtin interacting protein HYPK is intrinsically unstructured. <i> Raychaudhuri S, Majumder P, Sarkar S, Giri K, Mukhopadhyay D, Bhattacharyya NP. </i> Proteins, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000023","ec_id":"ECO:0006204","region_id":"DP00546r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":121,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18076027","version":3,"reference_html":"Huntingtin interacting protein HYPK is intrinsically unstructured. <i> Raychaudhuri S, Majumder P, Sarkar S, Giri K, Mukhopadhyay D, Bhattacharyya NP. </i> Proteins, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00546r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":121,"region_id":"DP00546r005","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Huntingtin interacting protein HYPK is intrinsically unstructured. <i> Raychaudhuri S, Majumder P, Sarkar S, Giri K, Mukhopadhyay D, Bhattacharyya NP. </i> Proteins, 2008","term_id":"IDPO:0000004","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18076027","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"pre-molten globule","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":121,"term_name":"protein folding chaperone","start":1,"ec_name":"cleavage assay evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18076027","version":3,"reference_html":"Huntingtin interacting protein HYPK is intrinsically unstructured. <i> Raychaudhuri S, Majumder P, Sarkar S, Giri K, Mukhopadhyay D, Bhattacharyya NP. </i> Proteins, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0044183","ec_id":"ECO:0007691","region_id":"DP00546r006","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":121,"term_name":"protein binding","start":1,"ec_name":"cleavage assay evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18076027","version":3,"reference_html":"Huntingtin interacting protein HYPK is intrinsically unstructured. <i> Raychaudhuri S, Majumder P, Sarkar S, Giri K, Mukhopadhyay D, Bhattacharyya NP. </i> Proteins, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007691","region_id":"DP00546r007","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":121,"region_id":"DP00546r008","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Huntingtin interacting protein HYPK is intrinsically unstructured. <i> Raychaudhuri S, Majumder P, Sarkar S, Giri K, Mukhopadhyay D, Bhattacharyya NP. </i> Proteins, 2008","term_id":"IDPO:0000004","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18076027","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"pre-molten globule","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":121,"term_name":"protein folding chaperone","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18076027","version":3,"reference_html":"Huntingtin interacting protein HYPK is intrinsically unstructured. <i> Raychaudhuri S, Majumder P, Sarkar S, Giri K, Mukhopadhyay D, Bhattacharyya NP. </i> Proteins, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0044183","ec_id":"ECO:0007680","region_id":"DP00546r009","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":121,"term_name":"protein binding","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18076027","version":3,"reference_html":"Huntingtin interacting protein HYPK is intrinsically unstructured. <i> Raychaudhuri S, Majumder P, Sarkar S, Giri K, Mukhopadhyay D, Bhattacharyya NP. </i> Proteins, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007680","region_id":"DP00546r010","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q9NX55","date":"2016-08-26T10:24:00.000Z","acc":"Q9NX55","name":"Huntingtin-interacting protein K","length":121,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000006E16A","genes":[{"name":{"value":"HYPK","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:18418","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:18418"}}]},"synonyms":[{"value":"C15orf63"}],"orfNames":[{"value":"HSPC136"}]}],"alphafold_very_low_content":0.17829457364341086,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":121,"type":"T"}],"Structural state":[{"start":1,"end":121,"type":"D"}],"Molecular function":[{"start":1,"end":121,"type":"F"}],"Structural transition":[{"start":1,"end":121,"type":"T"}]}},{"features":{"pfam":[{"id":"PF12171","name":"Zinc-finger double-stranded RNA-binding","start":61,"end":86}],"gene3D":[{"start":46,"end":112,"id":"3.30.160.60","name":"Classic Zinc Finger"}]},"uniref50":"UniRef50_O00488","sequence":"MGRSRRTGAHRAHSLARQMKAKRRRPDLDEIHRELRPQGSARPQPDPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERAAGMGSYVPPRRLAVPTEVSTEVPEMDTST","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O00488","disprot_id":"DP00549","ncbi_taxon_id":9606,"regions_counter":5,"creator":"wvranken","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":35,"region_id":"DP00549r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The solution structure of ZNF593 from Homo sapiens reveals a zinc finger in a predominantly unstructured protein. <i> Hayes PL, Lytle BL, Volkman BF, Peterson FC. </i> Protein Sci, 2008","term_id":"IDPO:0000002","curator_id":"wvranken","start":1,"term_ontology":"IDPO","curator_name":"Wim Vranken","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"BMRB","id":"6682"}],"reference_id":"18287285","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":77,"region_id":"DP00549r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The solution structure of ZNF593 from Homo sapiens reveals a zinc finger in a predominantly unstructured protein. <i> Hayes PL, Lytle BL, Volkman BF, Peterson FC. </i> Protein Sci, 2008","term_id":"IDPO:0000006","curator_id":"wvranken","start":36,"term_ontology":"IDPO","curator_name":"Wim Vranken","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"order","cross_refs":[{"db":"PDB","id":"1ZR9"}],"reference_id":"18287285","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":116,"region_id":"DP00549r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The solution structure of ZNF593 from Homo sapiens reveals a zinc finger in a predominantly unstructured protein. <i> Hayes PL, Lytle BL, Volkman BF, Peterson FC. </i> Protein Sci, 2008","term_id":"IDPO:0000002","curator_id":"wvranken","start":78,"term_ontology":"IDPO","curator_name":"Wim Vranken","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"BMRB","id":"6682"}],"reference_id":"18287285","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_O00488","date":"2016-09-13T13:43:29.000Z","acc":"O00488","name":"Zinc finger protein 593","length":134,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000013C483","genes":[{"name":{"value":"ZNF593"},"synonyms":[{"value":"ZT86"}]}],"alphafold_very_low_content":0.12686567164179105,"disorder_content":0.8656716417910447,"disprot_consensus":{"full":[{"start":1,"end":35,"type":"D"},{"start":36,"end":77,"type":"S"},{"start":78,"end":116,"type":"D"}],"Structural state":[{"start":1,"end":35,"type":"D"},{"start":36,"end":77,"type":"S"},{"start":78,"end":116,"type":"D"}]}},{"features":{"pfam":[{"id":"PF13499","name":"EF-hand domain pair","start":41,"end":104}],"gene3D":[{"start":1,"end":108,"id":"1.10.238.10","name":"EF-hand"}]},"uniref50":"UniRef50_P32848","sequence":"AKDLLKADDIKKALDAVKAEGSFNHKKFFALVGLKAMSANDVKKVFKAIDADASGFIEEEELKFVLKSFAADGRDLTDAETKAFLKAADKDGDGKIGIDEFETLVHEA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Actinopterygii","Neopterygii","Teleostei","Protacanthopterygii","Esociformes","Esocidae","Esox"],"uniref90":"UniRef90_P02628","disprot_id":"DP00550","ncbi_taxon_id":8010,"regions_counter":6,"creator":"wvranken","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":108,"region_id":"DP00550r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Apo-parvalbumin as an intrinsically disordered protein. <i> Permyakov SE, Bakunts AG, Denesyuk AI, Knyazeva EL, Uversky VN, Permyakov EA. </i> Proteins, 2008","term_id":"IDPO:0000002","curator_id":"wvranken","start":1,"term_ontology":"IDPO","curator_name":"Wim Vranken","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18260106","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":108,"term_name":"ion binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Apo-parvalbumin as an intrinsically disordered protein. <i> Permyakov SE, Bakunts AG, Denesyuk AI, Knyazeva EL, Uversky VN, Permyakov EA. </i> Proteins, 2008","term_id":"GO:0043167","curator_id":"wvranken","start":1,"term_ontology":"GO","curator_name":"Wim Vranken","reference_id":"18260106","version":3,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00550r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":108,"region_id":"DP00550r003","released":"2022_03","ec_id":"ECO:0006206","reference_html":"Apo-parvalbumin as an intrinsically disordered protein. <i> Permyakov SE, Bakunts AG, Denesyuk AI, Knyazeva EL, Uversky VN, Permyakov EA. </i> Proteins, 2008","term_id":"IDPO:0000002","curator_id":"wvranken","start":1,"term_ontology":"IDPO","curator_name":"Wim Vranken","ec_name":"near-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18260106","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":108,"term_name":"ion binding","released":"2022_03","ec_name":"near-UV circular dichroism evidence used in manual assertion","reference_html":"Apo-parvalbumin as an intrinsically disordered protein. <i> Permyakov SE, Bakunts AG, Denesyuk AI, Knyazeva EL, Uversky VN, Permyakov EA. </i> Proteins, 2008","term_id":"GO:0043167","curator_id":"wvranken","start":1,"term_ontology":"GO","curator_name":"Wim Vranken","reference_id":"18260106","version":3,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006206","region_id":"DP00550r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":108,"region_id":"DP00550r005","released":"2022_03","ec_id":"ECO:0006232","reference_html":"Apo-parvalbumin as an intrinsically disordered protein. <i> Permyakov SE, Bakunts AG, Denesyuk AI, Knyazeva EL, Uversky VN, Permyakov EA. </i> Proteins, 2008","term_id":"IDPO:0000002","curator_id":"wvranken","start":1,"term_ontology":"IDPO","curator_name":"Wim Vranken","ec_name":"differential scanning calorimetry evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18260106","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":108,"term_name":"ion binding","released":"2022_03","ec_name":"differential scanning calorimetry evidence used in manual assertion","reference_html":"Apo-parvalbumin as an intrinsically disordered protein. <i> Permyakov SE, Bakunts AG, Denesyuk AI, Knyazeva EL, Uversky VN, Permyakov EA. </i> Proteins, 2008","term_id":"GO:0043167","curator_id":"wvranken","start":1,"term_ontology":"GO","curator_name":"Wim Vranken","reference_id":"18260106","version":3,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006232","region_id":"DP00550r006","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P02628","date":"2016-09-13T14:02:47.000Z","acc":"P02628","name":"Parvalbumin alpha","length":108,"organism":"Esox lucius","dataset":[],"UniParc":"UPI0000132401","genes":[],"alphafold_very_low_content":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":108,"type":"D"}],"Structural state":[{"start":1,"end":108,"type":"D"}],"Molecular function":[{"start":1,"end":108,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00212","name":"Atrial natriuretic peptide","start":98,"end":128}]},"uniref50":"UniRef50_P16860","sequence":"MDPQTAPSRALLLLLFLHLAFLGGRSHPLGSPGSASDLETSGLQEQRNHLQGKLSELQVEQTSLEPLQESPRPTGVWKSREVATEGIRGHRKMVLYTLRAPRSPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P16860","disprot_id":"DP00551","ncbi_taxon_id":9606,"regions_counter":3,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":77,"region_id":"DP00551r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The human cardiac hormone fragment N-terminal pro B-type natriuretic peptide is an intrinsically unstructured protein. <i> Crimmins DL, Kao JL. </i> Arch Biochem Biophys, 2007","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"17399679","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":77,"region_id":"DP00551r002","released":"2022_03","ec_id":"ECO:0007689","reference_html":"The human cardiac hormone fragment N-terminal pro B-type natriuretic peptide is an intrinsically unstructured protein. <i> Crimmins DL, Kao JL. </i> Arch Biochem Biophys, 2007","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"17399679","version":2,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":77,"region_id":"DP00551r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The human cardiac hormone fragment N-terminal pro B-type natriuretic peptide is an intrinsically unstructured protein. <i> Crimmins DL, Kao JL. </i> Arch Biochem Biophys, 2007","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"17399679","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P16860","date":"2016-09-07T11:21:06.000Z","acc":"P16860","name":"Natriuretic peptides B","length":134,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000350A5","genes":[{"name":{"value":"NPPB"}}],"alphafold_very_low_content":0.26865671641791045,"disorder_content":0.5746268656716418,"disprot_consensus":{"full":[{"start":1,"end":77,"type":"D"}],"Structural state":[{"start":1,"end":77,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03872","name":"Anti sigma-E protein RseA, N-terminal domain","start":1,"end":87},{"id":"PF03873","name":"Anti sigma-E protein RseA, C-terminal domain","start":132,"end":186}],"gene3D":[{"start":1,"end":66,"id":"1.10.10.880","name":"Anti sigma-E protein RseA, N-terminal domain"}]},"uniref50":"UniRef50_D0ZSY8","sequence":"MQKEQLSALMDGETLDSELLNELAHNPEMQKTWESYHLIRDSMRGDTPEVLHFDISSRVMAAIEEEPVRQPATLIPEAQPAPHQWQKMPFWQKVRPWAAQLTQMGVAACVSLAVIVGVQHYNGQSETSQQPETPVFNTLPMMGKASPVSLGVPSEATANNGQQQQVQEQRRRINAMLQDYELQRRLHSEQLQFEQAQTQQAAVQVPGIQTLGTQSQ","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0AFX8","disprot_id":"DP00552","ncbi_taxon_id":83333,"regions_counter":8,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":216,"region_id":"DP00552r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Solution structures of RseA and its complex with RseB. <i> Jin KS, Kim DY, Rho Y, Le VB, Kwon E, Kim KK, Ree M. </i> J Synchrotron Radiat, 2008","term_id":"IDPO:0000002","curator_id":"fquaglia","start":121,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18421143","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":216,"term_name":"molecular adaptor activity","start":121,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18421143","version":3,"reference_html":"Solution structures of RseA and its complex with RseB. <i> Jin KS, Kim DY, Rho Y, Le VB, Kwon E, Kim KK, Ree M. </i> J Synchrotron Radiat, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006204","region_id":"DP00552r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":216,"term_name":"disorder to order","start":121,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18421143","version":2,"reference_html":"Solution structures of RseA and its complex with RseB. <i> Jin KS, Kim DY, Rho Y, Le VB, Kwon E, Kim KK, Ree M. </i> J Synchrotron Radiat, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00552r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":216,"term_name":"protein binding","start":121,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18421143","version":3,"reference_html":"Solution structures of RseA and its complex with RseB. <i> Jin KS, Kim DY, Rho Y, Le VB, Kwon E, Kim KK, Ree M. </i> J Synchrotron Radiat, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00552r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":216,"region_id":"DP00552r005","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Solution structures of RseA and its complex with RseB. <i> Jin KS, Kim DY, Rho Y, Le VB, Kwon E, Kim KK, Ree M. </i> J Synchrotron Radiat, 2008","term_id":"IDPO:0000002","curator_id":"fquaglia","start":121,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18421143","version":2,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":216,"term_name":"molecular adaptor activity","start":121,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18421143","version":3,"reference_html":"Solution structures of RseA and its complex with RseB. <i> Jin KS, Kim DY, Rho Y, Le VB, Kwon E, Kim KK, Ree M. </i> J Synchrotron Radiat, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006210","region_id":"DP00552r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":216,"term_name":"disorder to order","start":121,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18421143","version":2,"reference_html":"Solution structures of RseA and its complex with RseB. <i> Jin KS, Kim DY, Rho Y, Le VB, Kwon E, Kim KK, Ree M. </i> J Synchrotron Radiat, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006210","region_id":"DP00552r007","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":216,"term_name":"protein binding","start":121,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18421143","version":3,"reference_html":"Solution structures of RseA and its complex with RseB. <i> Jin KS, Kim DY, Rho Y, Le VB, Kwon E, Kim KK, Ree M. </i> J Synchrotron Radiat, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006210","region_id":"DP00552r008","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P0AFX8","date":"2016-09-14T11:28:28.000Z","acc":"P0AFX7","name":"Anti-sigma-E factor RseA","length":216,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI00001351EC","genes":[{"name":{"value":"rseA"},"synonyms":[{"value":"mclA"},{"value":"yfiJ"}],"olnNames":[{"value":"b2572"},{"value":"JW2556"}]}],"alphafold_very_low_content":0.21296296296296297,"disorder_content":0.4444444444444444,"disprot_consensus":{"full":[{"start":121,"end":216,"type":"T"}],"Structural state":[{"start":121,"end":216,"type":"D"}],"Molecular function":[{"start":121,"end":216,"type":"F"}],"Structural transition":[{"start":121,"end":216,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00135","name":"Carboxylesterase family","start":41,"end":624}],"gene3D":[{"start":41,"end":640,"id":"3.40.50.1820","name":"alpha/beta hydrolase"}]},"uniref50":"UniRef50_Q62889","sequence":"MWLRLGPPSLSLSPKPTVGRSLCLTLWFLSLALRASTQAPAPTVNTHFGKLRGARVPLPSEILGPVDQYLGVPYAAPPIGEKRFLPPEPPPSWSGIRNATHFPPVCPQNIHTAVPEVMLPVWFTANLDIVATYIQEPNEDCLYLNVYVPTEDVKRISKECARKPNKKICRKGGSGAKKQGEDLADNDGDEDEDIRDSGAKPVMVYIHGGSYMEGTGNMIDGSILASYGNVIVITLNYRVGVLGFLSTGDQAAKGNYGLLDQIQALRWVSENIAFFGGDPRRITVFGSGIGASCVSLLTLSHHSEGLFQRAIIQSGSALSSWAVNYQPVKYTSLLADKVGCNVLDTVDMVDCLRQKSAKELVEQDIQPARYHVAFGPVIDGDVIPDDPEILMEQGEFLNYDIMLGVNQGEGLKFVEGVVDPEDGVSGTDFDYSVSNFVDNLYGYPEGKDTLRETIKFMYTDWADRDNPETRRKTLVALFTDHQWVEPSVVTADLHARYGSPTYFYAFYHHCQSLMKPAWSDAAHGDEVPYVFGVPMVGPTDLFPCNFSKNDVMLSAVVMTYWTNFAKTGDPNKPVPQDTKFIHTKANRFEEVAWSKYNPRDQLYLHIGLKPRVRDHYRATKVAFWKHLVPHLYNLHDMFHYTSTTTKVPPPDTTHSSHITRRPNGKTWSTKRPAISPAYSNENAQGSWNGDQDAGPLLVENPRDYSTELSVTIAVGASLLFLNVLAFAALYYRKDKRRQEPLRQPSPQRGAGAPELGAAPEEELAALQLGPTHHECEAGPPHDTLRLTALPDYTLTLRRSPDDIPLMTPNTITMIPNSLVGLQTLHPYNTFAAGFNSTGLPHSHSTTRV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q62889","disprot_id":"DP00553","ncbi_taxon_id":9606,"regions_counter":24,"creator":"wvranken","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":848,"region_id":"DP00553r001","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3. <i> Paz A, Zeev-Ben-Mordehai T, Lundqvist M, Sherman E, Mylonas E, Weiner L, Haran G, Svergun DI, Mulder FA, Sussman JL, Silman I. </i> Biophys J, 2008","term_id":"IDPO:0000002","curator_id":"vnugnes","start":731,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18456828","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-05-04T17:05:28.323Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Abnormal migration of the full-length hNL3-cyt domain on SDS-PAGE, as well as CD analysis of the heterogeneous hNL3-cyt solution in the far UV (Fig. S3 in Data S1), both provided early indications that hNL3-cyt is an IUP.","type":"Results"},{"text":" All three spectra lack any major contributions from α-helices, β-sheets or turns, and are characteristic of an unstructured polypeptide, with a possible PPII contribution (36,70,71).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":848,"region_id":"DP00553r004","released":"2023_06","ec_id":"ECO:0006210","reference_html":"Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3. <i> Paz A, Zeev-Ben-Mordehai T, Lundqvist M, Sherman E, Mylonas E, Weiner L, Haran G, Svergun DI, Mulder FA, Sussman JL, Silman I. </i> Biophys J, 2008","term_id":"IDPO:0000002","curator_id":"vnugnes","start":731,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18456828","version":3,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","date":"2023-05-04T17:04:46.916Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"hNL3-cyt displays a shape typical of unfolded proteins, i.e., a plateau that increases monotonically at higher s values, whereas that for BSA displays a bell-shaped Kratky plot (Fig. 9 C).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":848,"region_id":"DP00553r007","released":"2023_06","ec_id":"ECO:0006275","reference_html":"Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3. <i> Paz A, Zeev-Ben-Mordehai T, Lundqvist M, Sherman E, Mylonas E, Weiner L, Haran G, Svergun DI, Mulder FA, Sussman JL, Silman I. </i> Biophys J, 2008","term_id":"IDPO:0000002","curator_id":"vnugnes","start":731,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18456828","version":3,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","date":"2023-05-04T17:04:03.045Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Both populations of hNL3-cyt have high f/fo values, indicating that both are extended in solution.","type":"Figure"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":848,"region_id":"DP00553r010","released":"2023_06","ec_id":"ECO:0007689","reference_html":"Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3. <i> Paz A, Zeev-Ben-Mordehai T, Lundqvist M, Sherman E, Mylonas E, Weiner L, Haran G, Svergun DI, Mulder FA, Sussman JL, Silman I. </i> Biophys J, 2008","term_id":"IDPO:0000002","curator_id":"vnugnes","start":731,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18456828","version":3,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2023-05-04T16:57:02.725Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Abnormal migration of the full-length hNL3-cyt domain on SDS-PAGE, as well as CD analysis of the heterogeneous hNL3-cyt solution in the far UV (Fig. S3 in Data S1), both provided early indications that hNL3-cyt is an IUP.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":848,"region_id":"DP00553r013","released":"2023_06","ec_id":"ECO:0007691","reference_html":"Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3. <i> Paz A, Zeev-Ben-Mordehai T, Lundqvist M, Sherman E, Mylonas E, Weiner L, Haran G, Svergun DI, Mulder FA, Sussman JL, Silman I. </i> Biophys J, 2008","term_id":"IDPO:0000002","curator_id":"vnugnes","start":731,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18456828","version":3,"ec_name":"cleavage assay evidence used in manual assertion","date":"2023-05-04T16:57:39.537Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"To confirm this susceptibility to proteolytic digestion, the rate of digestion of hNL3-cyt by Proteinase K was compared to that of TcAChE, a globular protein that is known to be resistant to proteases in its native state (69) (Fig. 4). hNL3-cyt is, indeed, much more sensitive to Proteinase K than native TcAChE.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":848,"region_id":"DP00553r016","released":"2023_06","ec_id":"ECO:0007064","reference_html":"Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3. <i> Paz A, Zeev-Ben-Mordehai T, Lundqvist M, Sherman E, Mylonas E, Weiner L, Haran G, Svergun DI, Mulder FA, Sussman JL, Silman I. </i> Biophys J, 2008","term_id":"IDPO:0000002","curator_id":"vnugnes","start":731,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18456828","version":3,"ec_name":"dynamic light scattering assay evidence used in manual assertion","date":"2023-05-04T17:12:58.913Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Evidence shows this peptide is disordered as shown in Table 1.","type":"Curator statement"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":848,"region_id":"DP00553r019","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3. <i> Paz A, Zeev-Ben-Mordehai T, Lundqvist M, Sherman E, Mylonas E, Weiner L, Haran G, Svergun DI, Mulder FA, Sussman JL, Silman I. </i> Biophys J, 2008","term_id":"IDPO:0000002","curator_id":"vnugnes","start":731,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18456828","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-05-04T17:08:56.409Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"NMR spectra recorded for hNL3-cyt are typical of an unfolded protein: The signals are narrow and display very limited dispersion in the proton dimension. As can be seen in Fig. 12 A, the backbone amide proton chemical shifts are restricted to the coil region, i.e., 7.7–8.7 ppm.","type":"Results"},{"text":"The signal attenuation by dipolar cross relaxation (NOE) is so strong that it leads to negative crosspeaks. Such behavior is typical of unfolded proteins (75), whereas attenuation factors of 15% would be expected for the ordered regions in a folded protein with a molecular weight of 15 kDa.","type":"Results"}]},{"start":731,"end":848,"reference_id":"18456828","reference_source":"pmid","reference_html":"Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3. <i> Paz A, Zeev-Ben-Mordehai T, Lundqvist M, Sherman E, Mylonas E, Weiner L, Haran G, Svergun DI, Mulder FA, Sussman JL, Silman I. </i> Biophys J, 2008","date":"2023-05-04T17:00:10.849Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00553r022","statement":[{"text":"Under denaturing conditions, in 8 M urea/100 mM NaH2PO4/10 mM Tris, pH 7.0, the 15 kDa protein eluted at a position corresponding to that to be expected for a ∼80 kDa globular protein, and to a hydrodynamic radius (RH) of ∼39 Å. In the absence of urea it eluted later, at a position corresponding to that for a ∼41 kDa globular protein, and to an RH of ∼28.4 Å, a radius that corresponds to a premolten globule according to the analysis of Uversky (23).","type":"Results"},{"text":"These data show that hNL3-cyt is already substantially unfolded under nondenaturing conditions, but becomes even more extended upon denaturation.","type":"Results"}]},{"start":731,"end":848,"reference_id":"18456828","reference_source":"pmid","reference_html":"Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3. <i> Paz A, Zeev-Ben-Mordehai T, Lundqvist M, Sherman E, Mylonas E, Weiner L, Haran G, Svergun DI, Mulder FA, Sussman JL, Silman I. </i> Biophys J, 2008","date":"2023-05-04T17:02:23.702Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006335","ec_ontology":"ECO","ec_name":"fluorescence correlation spectroscopy evidence","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00553r023","statement":[{"text":"Hydrodynamic radii of the nondenatured and denatured forms of hNL3-cyt, calculated using the Stokes-Einstein equation, were 25.0 ± 0.6 Å and 33.0 ± 0.8 Å, respectively. These values once again demonstrate that hNL3-cyt is disordered in solution, but can be further extended by denaturation.","type":"Results"}]},{"start":731,"end":848,"reference_id":"18456828","reference_source":"pmid","reference_html":"Biophysical characterization of the unstructured cytoplasmic domain of the human neuronal adhesion protein neuroligin 3. <i> Paz A, Zeev-Ben-Mordehai T, Lundqvist M, Sherman E, Mylonas E, Weiner L, Haran G, Svergun DI, Mulder FA, Sussman JL, Silman I. </i> Biophys J, 2008","date":"2023-05-04T17:07:49.483Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006289","ec_ontology":"ECO","ec_name":"site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00553r024","statement":[{"text":"The shape of the ESR spectrum provides a measure of the mobility of the bound nitroxyl radical, which depends on the structure and flexibility of the protein in the vicinity of its site of attachment. The ESR signal of spin-labeled hNL3-cyt in 150 mM NaCl/10 mM sodium phosphate, pH 7.0, at 20°C reveals relatively sharp peaks (Fig. 11 A), indicating only limited restriction of the probe's movement.","type":"Results"},{"text":"Comparison of these values to that for isotropic rotation of the free radical in solution, τR ∼ 10−11−10−10 s, and to values for folded proteins, τR > 10−7 s, indicates limited restriction of the motion of the bound radical in buffer, and more substantial restriction in TFE.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_Q9NZ94","date":"2016-08-26T13:03:40.000Z","acc":"Q9NZ94","name":"Neuroligin-3","length":848,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI000006E386","genes":[{"name":{"value":"NLGN3"},"synonyms":[{"value":"KIAA1480"},{"value":"NL3"}]}],"alphafold_very_low_content":0.27004716981132076,"disorder_content":0.1391509433962264,"disprot_consensus":{"full":[{"start":731,"end":848,"type":"D"}],"Structural state":[{"start":731,"end":848,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00560","name":"Leucine Rich Repeat","start":809,"end":829},{"id":"PF00619","name":"Caspase recruitment domain","start":1380,"end":1461},{"id":"PF02758","name":"PAAD/DAPIN/Pyrin domain","start":9,"end":83},{"id":"PF05729","name":"NACHT domain","start":328,"end":497},{"id":"PF13516","name":"Leucine Rich repeat","start":863,"end":886},{"id":"PF13516","name":"Leucine Rich repeat","start":921,"end":943},{"id":"PF13553","name":"Function to find","start":1092,"end":1224},{"id":"PF17776","name":"NLRC4 helical domain HD2","start":623,"end":733},{"id":"PF17779","name":"NOD2 winged helix domain","start":567,"end":613},{"id":"PF23679","name":"UPA-FIIND domain","start":1231,"end":1350}],"gene3D":[{"start":790,"end":990,"id":"3.80.10.10","name":"Ribonuclease Inhibitor"},{"start":1379,"end":1467,"id":"1.10.533.10","name":"Death Domain, Fas"},{"start":270,"end":466,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":1,"end":97,"id":"1.10.533.10","name":"Death Domain, Fas"}]},"uniref50":"UniRef50_Q9C000","sequence":"MAGGAWGRLACYLEFLKKEELKEFQLLLANKAHSRSSSGETPAQPEKTSGMEVASYLVAQYGEQRAWDLALHTWEQMGLRSLCAQAQEGAGHSPSFPYSPSEPHLGSPSQPTSTAVLMPWIHELPAGCTQGSERRVLRQLPDTSGRRWREISASLLYQALPSSPDHESPSQESPNAPTSTAVLGSWGSPPQPSLAPREQEAPGTQWPLDETSGIYYTEIREREREKSEKGRPPWAAVVGTPPQAHTSLQPHHHPWEPSVRESLCSTWPWKNEDFNQKFTQLLLLQRPHPRSQDPLVKRSWPDYVEENRGHLIEIRDLFGPGLDTQEPRIVILQGAAGIGKSTLARQVKEAWGRGQLYGDRFQHVFYFSCRELAQSKVVSLAELIGKDGTATPAPIRQILSRPERLLFILDGVDEPGWVLQEPSSELCLHWSQPQPADALLGSLLGKTILPEASFLITARTTALQNLIPSLEQARWVEVLGFSESSRKEYFYRYFTDERQAIRAFRLVKSNKELWALCLVPWVSWLACTCLMQQMKRKEKLTLTSKTTTTLCLHYLAQALQAQPLGPQLRDLCSLAAEGIWQKKTLFSPDDLRKHGLDGAIISTFLKMGILQEHPIPLSYSFIHLCFQEFFAAMSYVLEDEKGRGKHSNCIIDLEKTLEAYGIHGLFGASTTRFLLGLLSDEGEREMENIFHCRLSQGRNLMQWVPSLQLLLQPHSLESLHCLYETRNKTFLTQVMAHFEEMGMCVETDMELLVCTFCIKFSRHVKKLQLIEGRQHRSTWSPTMVVLFRWVPVTDAYWQILFSVLKVTRNLKELDLSGNSLSHSAVKSLCKTLRRPRCLLETLRLAGCGLTAEDCKDLAFGLRANQTLTELDLSFNVLTDAGAKHLCQRLRQPSCKLQRLQLVSCGLTSDCCQDLASVLSASPSLKELDLQQNNLDDVGVRLLCEGLRHPACKLIRLGLDQTTLSDEMRQELRALEQEKPQLLIFSRRKPSVMTPTEGLDTGEMSNSTSSLKRQRLGSERAASHVAQANLKLLDVSKIFPIAEIAEESSPEVVPVELLCVPSPASQGDLHTKPLGTDDDFWGPTGPVATEVVDKEKNLYRVHFPVAGSYRWPNTGLCFVMREAVTVEIEFCVWDQFLGEINPQHSWMVAGPLLDIKAEPGAVEAVHLPHFVALQGGHVDTSLFQMAHFKEEGMLLEKPARVELHHIVLENPSFSPLGVLLKMIHNALRFIPVTSVVLLYHRVHPEEVTFHLYLIPSDCSIRKAIDDLEMKFQFVRIHKPPPLTPLYMGCRYTVSGSGSGMLEILPKELELCYRSPGEDQLFSEFYVGHLGSGIRLQVKDKKDETLVWEALVKPGDLMPATTLIPPARIAVPSPLDAPQLLHFVDQYREQLIARVTSVEVVLDKLHGQVLSQEQYERVLAENTRPSQMRKLFSLSQSWDRKCKDGLYQALKETHPHLIMELWEKGSKKGLLPLSS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9C000","disprot_id":"DP00554","ncbi_taxon_id":9606,"regions_counter":2,"creator":"maspromonte","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":50,"region_id":"DP00554r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR structure of the apoptosis- and inflammation-related NALP1 pyrin domain. <i> Hiller S, Kohl A, Fiorito F, Herrmann T, Wider G, Tschopp J, Grütter MG, Wüthrich K. </i> Structure, 2003","term_id":"IDPO:0000002","curator_id":"maspromonte","start":31,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1PN5"}],"reference_id":"14527388","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":50,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"NMR structure of the apoptosis- and inflammation-related NALP1 pyrin domain. <i> Hiller S, Kohl A, Fiorito F, Herrmann T, Wider G, Tschopp J, Grütter MG, Wüthrich K. </i> Structure, 2003","term_id":"GO:0005515","curator_id":"maspromonte","start":31,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"14527388","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00554r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q9C000","date":"2016-09-08T21:46:08.000Z","acc":"Q9C000","name":"NACHT, LRR and PYD domains-containing protein 1","length":1473,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000038309","genes":[{"name":{"value":"NLRP1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"22665479","url":"http://www.ncbi.nlm.nih.gov/pubmed/22665479","alternativeUrl":"https://europepmc.org/abstract/MED/22665479"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:14374","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:14374"}}]},"synonyms":[{"value":"CARD7"},{"value":"DEFCAP","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11076957","url":"http://www.ncbi.nlm.nih.gov/pubmed/11076957","alternativeUrl":"https://europepmc.org/abstract/MED/11076957"}}]},{"value":"KIAA0926","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10231032","url":"http://www.ncbi.nlm.nih.gov/pubmed/10231032","alternativeUrl":"https://europepmc.org/abstract/MED/10231032"}}]},{"value":"NAC","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11113115","url":"http://www.ncbi.nlm.nih.gov/pubmed/11113115","alternativeUrl":"https://europepmc.org/abstract/MED/11113115"}}]},{"value":"NALP1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15285719","url":"http://www.ncbi.nlm.nih.gov/pubmed/15285719","alternativeUrl":"https://europepmc.org/abstract/MED/15285719"}}]}]}],"alphafold_very_low_content":0.26272912423625255,"disorder_content":0.013577732518669382,"disprot_consensus":{"full":[{"start":31,"end":50,"type":"D"}],"Structural state":[{"start":31,"end":50,"type":"D"}],"Molecular function":[{"start":31,"end":50,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01387","name":"Synuclein","start":1,"end":125}],"gene3D":[{"start":1,"end":134,"id":"1.10.287.700","name":"Helix hairpin bin"}]},"uniref50":"UniRef50_Q16143","sequence":"MDVFMKGLSMAKEGVVAAAEKTKQGVTEAAEKTKEGVLYVGSKTREGVVQGVASVAEKTKEQASHLGGAVFSGAGNIAAATGLVKREEFPTDLKPEEVAQEAAEEPLIEPLMEPEGESYEDPPQEEYQEYEPEA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q16143","disprot_id":"DP00555","ncbi_taxon_id":9606,"regions_counter":2,"creator":"wvranken","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":134,"region_id":"DP00555r001","released":"2024_12","ec_id":"ECO:0006165","reference_html":"Structural characterization of the intrinsically unfolded protein beta-synuclein, a natural negative regulator of alpha-synuclein aggregation. <i> Bertoncini CW, Rasia RM, Lamberto GR, Binolfi A, Zweckstetter M, Griesinger C, Fernandez CO. </i> J Mol Biol, 2007","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-12-04T18:25:58.353Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"BMRB","id":"15298"}],"reference_id":"17681539","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The measured values of the hydrodynamic radius for βS in its native state (32.4 Å) and in the presence of 8 M urea (35.4 Å) are both significantly shifted toward the value empirically calculated for a highly denatured state (36.0 Å) (Figure 1(b)).","type":"Results"},{"text":"The resonances are well resolved and sharp, with a limited dispersion of chemical shifts, reflecting the unfolded nature and high degree of backbone mobility.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_Q16143","date":"2016-09-13T14:23:17.000Z","acc":"Q16143","name":"Beta-synuclein","length":134,"organism":"Homo sapiens","dataset":["Age-related disorders proteins"],"UniParc":"UPI000003173C","genes":[{"name":{"value":"SNCB"}}],"alphafold_very_low_content":0.22388059701492538,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":134,"type":"D"}],"Structural state":[{"start":1,"end":134,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00289","name":"Biotin carboxylase, N-terminal domain","start":59,"end":180},{"id":"PF00364","name":"Biotin-requiring enzyme","start":702,"end":767},{"id":"PF01039","name":"Carboxyl transferase domain","start":1574,"end":2130},{"id":"PF02785","name":"Biotin carboxylase C-terminal domain","start":457,"end":563},{"id":"PF02786","name":"Carbamoyl-phosphate synthase L chain, ATP binding domain","start":233,"end":413},{"id":"PF08326","name":"Acetyl-CoA carboxylase, central region","start":768,"end":1479},{"id":"PF21385","name":"Acetyl-CoA carboxylase, BT domain","start":576,"end":695}],"gene3D":[{"start":231,"end":293,"id":"3.30.1490.20","name":"ATP-grasp fold, A domain"},{"start":698,"end":769,"id":"2.40.50.100","name":"2.40.50.100"},{"start":294,"end":566,"id":"3.30.470.20","name":"ATP-grasp fold, B domain"},{"start":1633,"end":1698,"id":"2.40.460.10","name":"Biotin dependent carboxylase carboxyltransferase"},{"start":1485,"end":1811,"id":"3.90.226.10","name":"2-enoyl-CoA Hydratase; Chain A, domain 1"},{"start":1815,"end":2209,"id":"3.90.226.10","name":"2-enoyl-CoA Hydratase; Chain A, domain 1"},{"start":186,"end":230,"id":"3.90.1770.10","name":"PreATP-grasp domain"}]},"uniref50":"UniRef50_Q00955","sequence":"MSEESLFESSPQKMEYEITNYSERHTELPGHFIGLNTVDKLEESPLRDFVKSHGGHTVISKILIANNGIAAVKEIRSVRKWAYETFGDDRTVQFVAMATPEDLEANAEYIRMADQYIEVPGGTNNNNYANVDLIVDIAERADVDAVWAGWGHASENPLLPEKLSQSKRKVIFIGPPGNAMRSLGDKISSTIVAQSAKVPCIPWSGTGVDTVHVDEKTGLVSVDDDIYQKGCCTSPEDGLQKAKRIGFPVMIKASEGGGGKGIRQVEREEDFIALYHQAANEIPGSPIFIMKLAGRARHLEVQLLADQYGTNISLFGRDCSVQRRHQKIIEEAPVTIAKAETFHEMEKAAVRLGKLVGYVSAGTVEYLYSHDDGKFYFLELNPRLQVEHPTTEMVSGVNLPAAQLQIAMGIPMHRISDIRTLYGMNPHSASEIDFEFKTQDATKKQRRPIPKGHCTACRITSEDPNDGFKPSGGTLHELNFRSSSNVWGYFSVGNNGNIHSFSDSQFGHIFAFGENRQASRKHMVVALKELSIRGDFRTTVEYLIKLLETEDFEDNTITTGWLDDLITHKMTAEKPDPTLAVICGAATKAFLASEEARHKYIESLQKGQVLSKDLLQTMFPVDFIHEGKRYKFTVAKSGNDRYTLFINGSKCDIILRQLSDGGLLIAIGGKSHTIYWKEEVAATRLSVDSMTTLLEVENDPTQLRTPSPGKLVKFLVENGEHIIKGQPYAEIEVMKMQMPLVSQENGIVQLLKQPGSTIVAGDIMAIMTLDDPSKVKHALPFEGMLPDFGSPVIEGTKPAYKFKSLVSTLENILKGYDNQVIMNASLQQLIEVLRNPKLPYSEWKLHISALHSRLPAKLDEQMEELVARSLRRGAVFPARQLSKLIDMAVKNPEYNPDKLLGAVVEPLADIAHKYSNGLEAHEHSIFVHFLEEYYEVEKLFNGPNVREENIILKLRDENPKDLDKVALTVLSHSKVSAKNNLILAILKHYQPLCKLSSKVSAIFSTPLQHIVELESKATAKVALQAREILIQGALPSVKERTEQIEHILKSSVVKVAYGSSNPKRSEPDLNILKDLIDSNYVVFDVLLQFLTHQDPVVTAAAAQVYIRRAYRAYTIGDIRVHEGVTVPIVEWKFQLPSAAFSTFPTVKSKMGMNRAVSVSDLSYVANSQSSPLREGILMAVDHLDDVDEILSQSLEVIPRHQSSSNGPAPDRSGSSASLSNVANVCVASTEGFESEEEILVRLREILDLNKQELINASIRRITFMFGFKDGSYPKYYTFNGPNYNENETIRHIEPALAFQLELGRLSNFNIKPIFTDNRNIHVYEAVSKTSPLDKRFFTRGIIRTGHIRDDISIQEYLTSEANRLMSDILDNLEVTDTSNSDLNHIFINFIAVFDISPEDVEAAFGGFLERFGKRLLRLRVSSAEIRIIIKDPQTGAPVPLRALINNVSGYVIKTEMYTEVKNAKGEWVFKSLGKPGSMHLRPIATPYPVKEWLQPKRYKAHLMGTTYVYDFPELFRQASSSQWKNFSADVKLTDDFFISNELIEDENGELTEVEREPGANAIGMVAFKITVKTPEYPRGRQFVVVANDITFKIGSFGPQEDEFFNKVTEYARKRGIPRIYLAANSGARIGMAEEIVPLFQVAWNDAANPDKGFQYLYLTSEGMETLKKFDKENSVLTERTVINGEERFVIKTIIGSEDGLGVECLRGSGLIAGATSRAYHDIFTITLVTCRSVGIGAYLVRLGQRAIQVEGQPIILTGAPAINKMLGREVYTSNLQLGGTQIMYNNGVSHLTAVDDLAGVEKIVEWMSYVPAKRNMPVPILETKDTWDRPVDFTPTNDETYDVRWMIEGRETESGFEYGLFDKGSFFETLSGWAKGVVVGRARLGGIPLGVIGVETRTVENLIPADPANPNSAETLIQEPGQVWHPNSAFKTAQAINDFNNGEQLPMMILANWRGFSGGQRDMFNEVLKYGSFIVDALVDYKQPIIIYIPPTGELRGGSWVVVDPTINADQMEMYADVNARAGVLEPQGMVGIKFRREKLLDTMNRLDDKYRELRSQLSNKSLAPEVHQQISKQLADRERELLPIYGQISLQFADLHDRSSRMVAKGVISKELEWTEARRFFFWRLRRRLNEEYLIKRLSHQVGEASRLEKIARIRSWYPASVDHEDDRQVATWIEENYKTLDDKLKGLKLESFAQDLAKKIRSDHDNAIDGLSEVIKMLSTDDKEKLLKTLK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q00955","disprot_id":"DP00557","ncbi_taxon_id":559292,"regions_counter":1,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":2080,"region_id":"DP00557r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase in complex with CP-640186. <i> Zhang H, Tweel B, Li J, Tong L. </i> Structure, 2004","term_id":"IDPO:0000002","curator_id":"mnecci","start":2048,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15341732","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1OD2"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q00955","date":"2016-09-07T11:31:49.000Z","acc":"Q00955","name":"Acetyl-CoA carboxylase","length":2233,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000145F95","genes":[{"name":{"value":"ACC1"},"synonyms":[{"value":"ABP2"},{"value":"FAS3"},{"value":"MTR7"}],"orfNames":[{"value":"N3175"}],"olnNames":[{"value":"YNR016C"}]}],"alphafold_very_low_content":0.03090013434841021,"disorder_content":0.014778325123152709,"disprot_consensus":{"full":[{"start":2048,"end":2080,"type":"D"}],"Structural state":[{"start":2048,"end":2080,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01239","name":"Protein prenyltransferase alpha subunit repeat","start":114,"end":143},{"id":"PF01239","name":"Protein prenyltransferase alpha subunit repeat","start":148,"end":179},{"id":"PF01239","name":"Protein prenyltransferase alpha subunit repeat","start":183,"end":212},{"id":"PF01239","name":"Protein prenyltransferase alpha subunit repeat","start":216,"end":246},{"id":"PF01239","name":"Protein prenyltransferase alpha subunit repeat","start":256,"end":285}],"gene3D":[{"start":55,"end":379,"id":"1.25.40.120","name":"Protein prenylyltransferase"}]},"uniref50":"UniRef50_P49354","sequence":"MAATEGVGEAAQGGEPGQPAQPPPQPHPPPPQQQHKEEMAAEAGEAVASPMDDGFVSLDSPSYVLYRDRAEWADIDPVPQNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLKSLQKDLHEEMNYITAIIEEQPKNYQVWHHRRVLVEWLRDPSQELEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQYVDQLLKEDVRNNSVWNQRYFVISNTTGYNDRAVLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSKYPNLLNQLLDLQPSHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKEYWRYIGRSLQSKHSTENDSPTNVQQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P49354","disprot_id":"DP00558","ncbi_taxon_id":9606,"regions_counter":4,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":379,"region_id":"DP00558r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics. <i> Long SB, Hancock PJ, Kral AM, Hellinga HW, Beese LS. </i> Proc Natl Acad Sci U S A, 2001","term_id":"IDPO:0000002","curator_id":"fquaglia","start":368,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11687658","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1JCQ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":54,"region_id":"DP00558r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics. <i> Long SB, Hancock PJ, Kral AM, Hellinga HW, Beese LS. </i> Proc Natl Acad Sci U S A, 2001","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11687658","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1JCQ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":54,"term_name":"molecular adaptor activity","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11687658","version":3,"reference_html":"The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics. <i> Long SB, Hancock PJ, Kral AM, Hellinga HW, Beese LS. </i> Proc Natl Acad Sci U S A, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006220","region_id":"DP00558r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":54,"term_name":"molecular recognition display site","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11687658","version":2,"reference_html":"The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics. <i> Long SB, Hancock PJ, Kral AM, Hellinga HW, Beese LS. </i> Proc Natl Acad Sci U S A, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000037","ec_id":"ECO:0006220","region_id":"DP00558r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_P49354","date":"2016-08-16T12:13:16.000Z","acc":"P49354","name":"Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha","length":379,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000013176D","genes":[{"name":{"value":"FNTA"}}],"alphafold_very_low_content":0.1424802110817942,"disorder_content":0.1741424802110818,"disprot_consensus":{"full":[{"start":1,"end":54,"type":"D"},{"start":368,"end":379,"type":"D"}],"Structural state":[{"start":1,"end":54,"type":"D"},{"start":368,"end":379,"type":"D"}],"Molecular function":[{"start":1,"end":54,"type":"F"}],"Disorder function":[{"start":1,"end":54,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01264","name":"Chorismate synthase","start":6,"end":373}]},"uniref50":"UniRef50_O66493","sequence":"MSLRYLRFLTAGESHGKGLTAILEGIPANLPLSEEEINHELRRRQRGYGRGGRMKIEKDTAEILSGVRFGKTLGSPIALFIRNRDWENWKEKMAIEGEPSPSVVPFTRPRPGHADLSGGIKYNQRDLRNILERASARETAARVAVGAVCKKFLSEFGIKIGSFVVSIGQKEVEELKDKSYFANPEKLLSYHEKAEDSELRIPFPEKDEEFKTYIDEVKEKGESLGGVFEVFALNVPPGLGSHIQWDRRIDGRIAQAMMSIQAIKGVEIGLGFEAARRFGSQVHDEIGWSEGKGYFRHSNNLGGTEGGITNGMPIVVRVAMKPIPTLKNPLRSVDIETKEEMKAGKERTDIVAVPAASVVGEAMLAIVLADALLEKLGGDFMEEVKKRFEDYVNHVKSF","taxonomy":["Bacteria","Aquificae","Aquificales","Aquificaceae","Aquifex"],"uniref90":"UniRef90_O66493","disprot_id":"DP00559","ncbi_taxon_id":224324,"regions_counter":3,"creator":"wvranken","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":117,"region_id":"DP00559r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of chorismate synthase from Aquifex aeolicus reveals a novel beta alpha beta sandwich topology. <i> Viola CM, Saridakis V, Christendat D. </i> Proteins, 2004","term_id":"IDPO:0000002","curator_id":"fquaglia","start":87,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14705034","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1Q1L"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":350,"region_id":"DP00559r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of chorismate synthase from Aquifex aeolicus reveals a novel beta alpha beta sandwich topology. <i> Viola CM, Saridakis V, Christendat D. </i> Proteins, 2004","term_id":"IDPO:0000002","curator_id":"fquaglia","start":326,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14705034","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1Q1L"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_O66493","date":"2016-08-26T13:35:32.000Z","acc":"O66493","name":"Chorismate synthase","length":398,"organism":"Aquifex aeolicus (strain VF5)","dataset":[],"UniParc":"UPI0000056268","genes":[{"name":{"value":"aroC","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00300","url":"https://hamap.expasy.org/unirule/MF_00300"}}]},"olnNames":[{"value":"aq_081"}]}],"alphafold_very_low_content":0,"disorder_content":0.1407035175879397,"disprot_consensus":{"full":[{"start":87,"end":117,"type":"D"},{"start":326,"end":350,"type":"D"}],"Structural state":[{"start":87,"end":117,"type":"D"},{"start":326,"end":350,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":34,"end":292},{"id":"PF13499","name":"EF-hand domain pair","start":340,"end":399},{"id":"PF13499","name":"EF-hand domain pair","start":410,"end":471}],"gene3D":[{"start":34,"end":117,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":296,"end":469,"id":"1.10.238.10","name":"EF-hand"},{"start":118,"end":295,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"}]},"uniref50":"UniRef50_Q39016","sequence":"MAAKSSSSSTTTNVVTLKAAWVLPQRTQNIREVYEVGRKLGQGQFGTTFECTRRASGGKFACKSIPKRKLLCKEDYEDVWREIQIMHHLSEHANVVRIEGTYEDSTAVHLVMELCEGGELFDRIVQKGHYSERQAARLIKTIVEVVEACHSLGVMHRDLKPENFLFDTIDEDAKLKATDFGLSVFYKPGESFCDVVGSPYYVAPEVLRKLYGPESDVWSAGVILYILLSGVPPFWAESEPGIFRQILLGKLDFHSEPWPSISDSAKDLIRKMLDQNPKTRLTAHEVLRHPWIVDDNIAPDKPLDSAVLSRLKQFSAMNKLKKMALRVIAERLSEEEIGGLKELFKMIDTDNSGTITFDELKDGLKRVGSELMESEIKDLMDAADIDKSGTIDYGEFIAATVHLNKLEREENLVSAFSYFDKDGSGYITLDEIQQACKDFGLDDIHIDDMIKEIDQDNDGQIDYGEFAAMMRKGNGGIGRRTMRKTLNLRDALGLVDNGSNQVIEGYFK","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","fabids","Fabales","Fabaceae","Papilionoideae","50 kb inversion clade","NPAAA clade","indigoferoid/millettioid clade","Phaseoleae","Glycine","Glycine subgen. Soja"],"uniref90":"UniRef90_P28583","disprot_id":"DP00561","ncbi_taxon_id":3847,"regions_counter":1,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":342,"region_id":"DP00561r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure and backbone dynamics of the N-terminal region of the calcium regulatory domain from soybean calcium-dependent protein kinase alpha. <i> Weljie AM, Gagné SM, Vogel HJ. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"mnecci","start":329,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15568805","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P28583","date":"2016-09-16T23:43:05.000Z","acc":"P28583","name":"Calcium-dependent protein kinase SK5","length":508,"organism":"Glycine max","dataset":[],"UniParc":"UPI0000127448","genes":[],"alphafold_very_low_content":0.10433070866141732,"disorder_content":0.027559055118110236,"disprot_consensus":{"full":[{"start":329,"end":342,"type":"D"}],"Structural state":[{"start":329,"end":342,"type":"D"}]}},{"features":{"pfam":[{"id":"PF04099","name":"Sybindin-like family","start":3,"end":207}],"gene3D":[{"start":102,"end":209,"id":"3.30.450.70","name":"3.30.450.70"},{"start":12,"end":101,"id":"2.30.42.40","name":"2.30.42.40"}]},"uniref50":"UniRef50_Q9Y296","sequence":"MAIFSVYVVNKAGGLIYQLDSYAPRAEAEKTFSYPLDLLLKLHDERVLVAFGQRDGIRVGHAVLAINGMDVNGRYTADGKEVLEYLGNPANYPVSIRFGRPRLTSNEKLMLASMFHSLFAIGSQLSPEQGSSGIEMLETDTFKLHCYQTLTGIKFVVLADPRQAGIDSLLRKIYEIYSDFALKNPFYSLEMPIRCELFDQNLKLALEVAEKAGTFGPGS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9Y296","disprot_id":"DP00562","ncbi_taxon_id":9606,"regions_counter":2,"creator":"wvranken","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":25,"region_id":"DP00562r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of synbindin atypical PDZ domain and interaction with syndecan-2. <i> Fan S, Feng Y, Wei Z, Xia B, Gong W. </i> Protein Pept Lett, 2009","statement":[{"text":"flexible regions 11-25","type":"Table"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":11,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19200043","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2JSN"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T19:11:33.218Z"}}],"released":"2016_10","uniref100":"UniRef100_Q9Y296","date":"2016-09-15T11:28:47.000Z","acc":"Q9Y296","name":"Trafficking protein particle complex subunit 4","length":219,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI0000052E23","genes":[{"name":{"value":"TRAPPC4","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:19943","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:19943"}}]},"synonyms":[{"value":"SBDN","evidences":[{"code":"ECO:0000250","source":{"name":"UniProtKB","id":"Q9ES56","url":"https://www.uniprot.org/uniprot/Q9ES56"}}]}],"orfNames":[{"value":"CGI-104"},{"value":"HSPC172"},{"value":"PTD009"}]}],"alphafold_very_low_content":0.0182648401826484,"disorder_content":0.0684931506849315,"disprot_consensus":{"full":[{"start":11,"end":25,"type":"D"}],"Structural state":[{"start":11,"end":25,"type":"D"}]}},{"features":{"pfam":[{"id":"PF10514","name":"Pro-apoptotic Bcl-2 protein, BAD","start":43,"end":204}]},"uniref50":"UniRef50_Q61337","sequence":"MGTPKQPSLAPAHALGLRKSDPGIRSLGSDAGGRRWRPAAQSMFQIPEFEPSEQEDASATDRGLGPSLTEDQPGPYLAPGLLGSNIHQQGRAATNSHHGGAGAMETRSRHSSYPAGTEEDEGMEEELSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFEGSFKGLPRPKSAGTATQMRQSAGWTRIIQSWWDRNLGKGGSTPSQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q61337","disprot_id":"DP00563","ncbi_taxon_id":10090,"regions_counter":9,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":204,"region_id":"DP00563r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"16645638","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":204,"term_name":"molecular function regulator","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"16645638","version":3,"reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006165","region_id":"DP00563r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":204,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"16645638","version":3,"reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00563r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":204,"region_id":"DP00563r004","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"16645638","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":204,"term_name":"molecular function regulator","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"16645638","version":3,"reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0007680","region_id":"DP00563r005","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":204,"term_name":"protein binding","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"16645638","version":3,"reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007680","region_id":"DP00563r006","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":204,"region_id":"DP00563r007","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"16645638","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":204,"term_name":"molecular function regulator","start":1,"ec_name":"cleavage assay evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"16645638","version":3,"reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0007691","region_id":"DP00563r008","curator_orcid":"0000-0001-9377-482X","ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":204,"term_name":"protein binding","start":1,"ec_name":"cleavage assay evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"16645638","version":3,"reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007691","region_id":"DP00563r009","curator_orcid":"0000-0001-9377-482X","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q61337","date":"2016-09-16T23:52:38.000Z","acc":"Q61337","name":"Bcl2-associated agonist of cell death","length":204,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000018A9","genes":[{"name":{"value":"Bad"},"synonyms":[{"value":"Bbc6"}]}],"alphafold_very_low_content":0.3235294117647059,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":204,"type":"D"}],"Structural state":[{"start":1,"end":204,"type":"D"}],"Molecular function":[{"start":1,"end":204,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01056","name":"Myc amino-terminal region","start":2,"end":158}]},"uniref50":"UniRef50_Q6P8Z1","sequence":"MPLHVSLANGNRDLDYDSVQPYFMCDDEEEDVHHQQPPQPPAPSEDIWKKFELLPTPRPSPGHAGLYSPPCEAVAVSFAPRDHDGDSFSIADLPELPGGDAVKQSFVCDPDDETFVKNIILQDCMWNGFSASAKLVSKLDPYQAVRKEGTGVSLAADVEPATPPDCTCNT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q6P8Z1","disprot_id":"DP00564","ncbi_taxon_id":10090,"regions_counter":6,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":169,"region_id":"DP00564r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"B-myc: N-terminal recognition of myc binding proteins. <i> Burton RA, Mattila S, Taparowsky EJ, Post CB. </i> Biochemistry, 2006","term_id":"IDPO:0000003","curator_id":"mnecci","start":2,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"16893186","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"molten globule","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":169,"term_name":"molecular adaptor activity","start":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"16893186","version":3,"reference_html":"B-myc: N-terminal recognition of myc binding proteins. <i> Burton RA, Mattila S, Taparowsky EJ, Post CB. </i> Biochemistry, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP00564r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":169,"term_name":"protein binding","start":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"16893186","version":3,"reference_html":"B-myc: N-terminal recognition of myc binding proteins. <i> Burton RA, Mattila S, Taparowsky EJ, Post CB. </i> Biochemistry, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00564r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":169,"region_id":"DP00564r004","released":"2022_03","ec_id":"ECO:0006204","reference_html":"B-myc: N-terminal recognition of myc binding proteins. <i> Burton RA, Mattila S, Taparowsky EJ, Post CB. </i> Biochemistry, 2006","term_id":"IDPO:0000003","curator_id":"mnecci","start":2,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"16893186","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"molten globule","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":169,"term_name":"molecular adaptor activity","start":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"16893186","version":3,"reference_html":"B-myc: N-terminal recognition of myc binding proteins. <i> Burton RA, Mattila S, Taparowsky EJ, Post CB. </i> Biochemistry, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006204","region_id":"DP00564r005","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":169,"term_name":"protein binding","start":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"16893186","version":3,"reference_html":"B-myc: N-terminal recognition of myc binding proteins. <i> Burton RA, Mattila S, Taparowsky EJ, Post CB. </i> Biochemistry, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00564r006","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q6P8Z1","date":"2016-09-16T23:58:42.000Z","acc":"Q6P8Z1","name":"Protein B-Myc","length":170,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00002131EF","genes":[{"name":{"value":"Mycb"},"synonyms":[{"value":"Bmyc"}]}],"alphafold_very_low_content":0.21176470588235294,"disorder_content":0.9882352941176471,"disprot_consensus":{"full":[{"start":2,"end":169,"type":"D"}],"Structural state":[{"start":2,"end":169,"type":"D"}],"Molecular function":[{"start":2,"end":169,"type":"F"}]}},{"features":{"pfam":[{"id":"PF13499","name":"EF-hand domain pair","start":21,"end":79},{"id":"PF13499","name":"EF-hand domain pair","start":89,"end":156}],"gene3D":[{"start":1,"end":170,"id":"1.10.238.10","name":"EF-hand"}]},"uniref50":"UniRef50_P63098","sequence":"MGNEASYPLEMCSHFDADEIKRLGKRFKKLDLDNSGSLSVEEFMSLPELQQNPLVQRVIDIFDTDGNGEVDFKEFIEGVSQFSVKGDKEQKLRFAFRIYDMDKDGYISNGELFQVLKMMVGNNLKDTQLQQIVDKTIINADKDGDGRISFEEFCAVVGGLDIHKKMVVDV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P63098","disprot_id":"DP00565","ncbi_taxon_id":9606,"regions_counter":3,"creator":"wvranken","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":14,"region_id":"DP00565r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"1H, 13C, 15N nuclear magnetic resonance backbone assignments and secondary structure of human calcineurin B. <i> Anglister J, Grzesiek S, Wang AC, Ren H, Klee CB, Bax A. </i> Biochemistry, 1994","term_id":"IDPO:0000002","curator_id":"wvranken","start":1,"term_ontology":"IDPO","curator_name":"Wim Vranken","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"8142351","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":169,"region_id":"DP00565r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"1H, 13C, 15N nuclear magnetic resonance backbone assignments and secondary structure of human calcineurin B. <i> Anglister J, Grzesiek S, Wang AC, Ren H, Klee CB, Bax A. </i> Biochemistry, 1994","term_id":"IDPO:0000002","curator_id":"wvranken","start":158,"term_ontology":"IDPO","curator_name":"Wim Vranken","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"8142351","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P63098","date":"2016-09-15T11:33:59.000Z","acc":"P63098","name":"Calcineurin subunit B type 1","length":170,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000110661","genes":[{"name":{"value":"PPP3R1"},"synonyms":[{"value":"CNA2"},{"value":"CNB"}]}],"alphafold_very_low_content":0.047058823529411764,"disorder_content":0.15294117647058825,"disprot_consensus":{"full":[{"start":1,"end":14,"type":"D"},{"start":158,"end":169,"type":"D"}],"Structural state":[{"start":1,"end":14,"type":"D"},{"start":158,"end":169,"type":"D"}]}},{"features":{"pfam":[{"id":"PF17499","name":"Ant venom peptides","start":1,"end":80}]},"uniref50":"UniRef50_Q07932","sequence":"MKLSCLLLTLTIIFVLTIVHAPNVEAKDLADPESEAVGFADAFGEADAVGEADPNAGLGSVFGRLARILGRVIPKVAKKLGPKVAKVLPKVMKEAIPMAVEMAKSQEEQQPQ","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Hymenoptera","Apocrita","Aculeata","Formicoidea","Formicidae","Myrmeciinae","Myrmeciini","Myrmecia"],"uniref90":"UniRef90_Q07932","disprot_id":"DP00567","dataset":[],"ncbi_taxon_id":13618,"regions_counter":2,"creator":"pwarholm","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":76,"region_id":"DP00567r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Identification and optimization of an antimicrobial peptide from the ant venom toxin pilosulin. <i> Zelezetsky I, Pag U, Antcheva N, Sahl HG, Tossi A. </i> Arch Biochem Biophys, 2005","term_id":"IDPO:0000002","curator_id":"pwarholm","start":57,"term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"15639237","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":76,"term_name":"disorder to order","start":57,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"15639237","version":2,"reference_html":"Identification and optimization of an antimicrobial peptide from the ant venom toxin pilosulin. <i> Zelezetsky I, Pag U, Antcheva N, Sahl HG, Tossi A. </i> Arch Biochem Biophys, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00567r002","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2016_10","uniref100":"UniRef100_Q07932","date":"2016-09-07T13:10:31.000Z","acc":"Q07932","name":"M-myrmeciitoxin-Mp1","length":112,"organism":"Myrmecia pilosula","UniParc":"UPI000012FBC9","genes":[],"alphafold_very_low_content":0.3392857142857143,"disorder_content":0.17857142857142858,"disprot_consensus":{"full":[{"start":57,"end":76,"type":"T"}],"Structural state":[{"start":57,"end":76,"type":"D"}],"Structural transition":[{"start":57,"end":76,"type":"T"}]}},{"features":{"pfam":[{"id":"PF01922","name":"SRP19 protein","start":17,"end":114}],"gene3D":[{"start":1,"end":126,"id":"3.30.56.30","name":"Signal recognition particle, SRP19-like subunit"}]},"uniref50":"UniRef50_P09132","sequence":"MACAAARSPADQDRFICIYPAYLNNKKTIAEGRRIPISKAVENPTATEIQDVCSAVGLNVFLEKNKMYSREWNRDVQYRGRVRVQLKQEDGSLCLVQFPSRKSVMLYAAEMIPKLKTRTQKTGGADQSLQQGEGSKKGKGKKKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P09132","disprot_id":"DP00570","ncbi_taxon_id":9606,"regions_counter":3,"creator":"pwarholm","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":144,"region_id":"DP00570r001","released":"2022_03","ec_id":"ECO:0001183","reference_html":"A threefold RNA-protein interface in the signal recognition particle gates native complex assembly. <i> Maity TS, Weeks KM. </i> J Mol Biol, 2007","term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"17434535","version":3,"ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","date":"2022-03-09T09:53:25.314Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"IPI","disprot_namespace":"Structural state","statement":[{"text":"Free SRP19 is a natively unstructured protein.","type":"Results"}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":144,"term_name":"RNA binding","start":1,"ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"17434535","version":4,"reference_html":"A threefold RNA-protein interface in the signal recognition particle gates native complex assembly. <i> Maity TS, Weeks KM. </i> J Mol Biol, 2007","date":"2022-03-09T10:00:59.082Z","term_id":"GO:0003723","ec_id":"ECO:0001183","region_id":"DP00570r003","curator_orcid":"0000-0002-5152-5953","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"RNAcentral","id":"URS000080DE0E_9606","operator":"and","partner_start":null,"partner_end":null}],"statement":[{"text":"Thus, RNA binding and subsequent conformational changes in SRP19 were detected both as the initial change in the resonance energy transfer efficiency to the RNA-tethered Alexa 555 acceptor fluorophore and also as the local change in donor fluorophore environment (Figure 3A).","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P09132","date":"2016-09-07T14:28:36.000Z","acc":"P09132","name":"Signal recognition particle 19 kDa protein","length":144,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000135EB6","genes":[{"name":{"value":"SRP19"}}],"alphafold_very_low_content":0.14583333333333334,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":144,"type":"D"}],"Structural state":[{"start":1,"end":144,"type":"D"}],"Molecular function":[{"start":1,"end":144,"type":"F"}]}},{"acc":"P03305","sequence":"MNTTDCFIALVQAIREIKALFLSRTTGKMELTLYNGEKKTFYSRPNNHDNCWLNAILQLFRYVEEPFFDWVYSSPENLTLEAIKQLEDLTGLELHEGGPPALVIWNIKHLLHTGIGTASRPSEVCMVDGTDMCLADFHAGIFLKGQEHAVFACVTSNGWYAIDDEDFYPWTPDPSDVLVFVPYDQEPLNGEWKAKVQRKLKGAGQSSPATGSQNQSGNTGSIINNYYMQQYQNSMDTQLGDNAISGGSNEGSTDTTSTHTTNTQNNDWFSKLASSAFSGLFGALLADKKTEETTLLEDRILTTRNGHTTSTTQSSVGVTYGYATAEDFVSGPNTSGLETRVVQAERFFKTHLFDWVTSDSFGRCHLLELPTDHKGVYGSLTDSYAYMRNGWDVEVTAVGNQFNGGCLLVAMVPELYSIQKRELYQLTLFPHQFINPRTNMTAHITVPFVGVNRYDQYKVHKPWTLVVMVVAPLTVNTEGAPQIKVYANIAPTNVHVAGEFPSKEGIFPVACSDGYGGLVTTDPKTADPVYGKVFNPPRNQLPGRFTNLLDVAEACPTFLRFEGGVPYVTTKTDSDRVLAQFDMSLAAKQMSNTFLAGLAQYYTQYSGTINLHFMFTGPTDAKARYMVAYAPPGMEPPKTPEAAAHCIHAEWDTGLNSKFTFSIPYLSAADYAYTASGVAETTNVQGWVCLFQITHGKADGDALVVLASAGKDFELRLPVDARAETTSAGESADPVTTTVENYGGETQIQRRQHTDVSFIMDRFVKVTPQNQINILDLMQIPSHTLVGALLRASTYYFSDLEIAVKHEGDLTWVPNGAPEKALDNTTNPTAYHKAPLTRLALPYTAPHRVLATVYNGECRYNRNAVPNLRGDLQVLAQKVARTLPTSFNYGAIKATRVTELLYRMKRAETYCPRPLLAIHPTEARHKQKIVAPVKQTLNFDLLKLAGDVESNPGPFFFSDVRSNFSKLVETINQMQEDMSTKHGPDFNRLVSAFEELAIGVKAIRTGLDEAKPWYKLIKLLSRLSCMAAVAARSKDPVLVAIMLADTGLEILDSTFVVKKISDSLSSLFHVPAPVFSFGAPVLLAGLVKVASSFFRSTPEDLERAEKQLKARDINDIFAILKNGEWLVKLILAIRDWIKAWIASEEKFVTMTDLVPGILEKQRDLNDPSKYKEAKEWLDNARQACLKSGNVHIANLCKVVAPAPSKSRPEPVVVCLRGKSGQGKSFLANVLAQAISTHFTGRIDSVWYCPPDPDHFDGYNQQTVVVMDDLGQNPDGKDFKYFAQMVSTTGFIPPMASLEDKGKPFNSKVIIATTNLYSGFTPRTMVCPDALNRRFHFDIDVSAKDGYKINSKLDIIKALEDTHANPVAMFQYDCALLNGMAVEMKRMQQDMFKPQPPLQNVYQLVQEVIDRVELHEKVSSHPIFKQISIPSQKSVLYFLIEKGQHEAAIEFFEGMVHDSIKEELRPLIQQTSFVKRAFKRLKENFEIVALCLTLLANIVIMIRETRKRQKMVDDAVNEYIEKANITTDDKTLDEAEKSPLETSGASTVGFRERTLPGQKACDDVNSEPAQPVEEQPQAEGPYAGPLERQKPLKVRAKLPQQEGPYAGPMERQKPLKVKAKAPVVKEGPYEGPVKKPVALKVKAKNLIVTESGAPPTDLQKMVMGNTKPVELILDGKTVAICCATGVFGTAYLVPRHLFAEKYDKIMVDGRAMTDSDYRVFEFEIKVKGQDMLSDAALMVLHRGNRVRDITKHFRDTARMKKGTPVVGVINNADVGRLIFSGEALTYKDIVVCMDGDTMPGLFAYRAATKAGYCGGAVLAKDGADTFIVGTHSAGGNGVGYCSCVSRSMLLKMKAHIDPEPHHEGLIVDTRDVEERVHVMRKTKLAPTVAHGVFNPEFGPAALSNKDPRLNEGVVLDEVIFSKHKGDTKMSEEDKALFRRCAADYASRLHSVLGTANAPLSIYEAIKGVDGLDAMEPDTAPGLPWALQGKRRGALIDFENGTVGPEVEAALKLMEKREYKFVCQTFLKDEIRPLEKVRAGKTRIVDVLPVEHILYTRMMIGRFCAQMHSNNGPQIGSAVGCNPDVDWQRFGTHFAQYRNVWDVDYSAFDANHCSDAMNIMFEEVFRTEFGFHPNAEWILKTLVNTEHAYENKRITVGGGMPSGCSATSIINTILNNIYVLYALRRHYEGVELDTYTMISYGDDIVVASDYDLDFEALKPHFKSLGQTITPADKSDKGFVLGHSITDVTFLKRHFHMDYGTGFYKPVMASKTLEAILSFARRGTIQEKLISVAGLAVHSGPDEYRRLFEPFQGLFEIPSYRSLYLRWVNAVCGDA","creator":"agasparini","dataset":["Viral proteins","RNA-binding proteins"],"date":"2016-08-25T17:03:46.000Z","disprot_id":"DP00573","features":{"pfam":[{"id":"PF00073","name":"picornavirus capsid protein","start":311,"end":474},{"id":"PF00073","name":"picornavirus capsid protein","start":536,"end":690},{"id":"PF00073","name":"picornavirus capsid protein","start":722,"end":867},{"id":"PF00548","name":"3C cysteine protease (picornain 3C)","start":1677,"end":1833},{"id":"PF00680","name":"Viral RNA-dependent RNA polymerase","start":1886,"end":2307},{"id":"PF00910","name":"RNA helicase","start":1213,"end":1315},{"id":"PF05408","name":"Foot-and-mouth virus L-proteinase","start":1,"end":201}],"gene3D":[{"start":725,"end":937,"id":"2.60.120.20","name":"2.60.120.20","_id":"685af523b4ac24d5329d7dca"},{"start":287,"end":504,"id":"2.60.120.20","name":"2.60.120.20","_id":"685af523b4ac24d5329d7dcb"},{"start":202,"end":286,"id":"4.10.90.10","name":"Capsid protein VP4 superfamily, Picornavirus","_id":"685af523b4ac24d5329d7dcc"},{"start":505,"end":724,"id":"2.60.120.20","name":"2.60.120.20","_id":"685af523b4ac24d5329d7dcd"},{"start":1649,"end":1748,"id":"2.40.10.10","name":"Trypsin-like serine proteases","_id":"685af523b4ac24d5329d7dce"},{"start":1749,"end":1857,"id":"2.40.10.10","name":"Trypsin-like serine proteases","_id":"685af523b4ac24d5329d7dcf"},{"start":2070,"end":2128,"id":"3.30.70.270","name":"3.30.70.270","_id":"685af523b4ac24d5329d7dd0"},{"start":2129,"end":2265,"id":"3.30.70.270","name":"3.30.70.270","_id":"685af523b4ac24d5329d7dd1"},{"start":2266,"end":2332,"id":"1.20.960.20","name":"1.20.960.20","_id":"685af523b4ac24d5329d7dd2"},{"start":29,"end":195,"id":"3.90.70.10","name":"Cysteine proteinases","_id":"685af523b4ac24d5329d7dd3"}]},"genes":[],"length":2332,"name":"Genome polyprotein","ncbi_taxon_id":73482,"organism":"Foot-and-mouth disease virus (isolate Bovine/Germany/O1Kaufbeuren/1966 serotype O)","regions_counter":4,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Picornavirales","Picornaviridae","Aphthovirus"],"UniParc":"UPI0000131E14","uniref100":"UniRef100_P03305","uniref50":"UniRef50_P03305","uniref90":"UniRef90_P03305","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1QQP","_id":"685af523b4ac24d5329d7dda"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":202,"end":215,"interaction_partner":[],"reference_html":"The structure and function of a foot-and-mouth disease virus-oligosaccharide receptor complex. <i> Fry EE, Lea SM, Jackson T, Newman JW, Ellard FM, Blakemore WE, Abu-Ghazaleh R, Samuel A, King AM, Stuart DI. </i> EMBO J, 1999","reference_id":"9927414","region_id":"DP00573r003","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The PDB shows missing electron densties in this region.","_id":"685af523b4ac24d5329d7ddb"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:31:09.409Z","_id":"685af523b4ac24d5329d7ddc"},"version":1,"_id":"685af523b4ac24d5329d7dd9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1QQP","_id":"685af523b4ac24d5329d7dde"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":241,"end":265,"interaction_partner":[],"reference_html":"The structure and function of a foot-and-mouth disease virus-oligosaccharide receptor complex. <i> Fry EE, Lea SM, Jackson T, Newman JW, Ellard FM, Blakemore WE, Abu-Ghazaleh R, Samuel A, King AM, Stuart DI. </i> EMBO J, 1999","reference_id":"9927414","region_id":"DP00573r004","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The PDB shows missing electron densties in this region.","_id":"685af523b4ac24d5329d7ddf"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:31:08.349Z","_id":"685af523b4ac24d5329d7de0"},"version":1,"_id":"685af523b4ac24d5329d7ddd","reference_source":"pmid"}],"__v":0,"disorder_content":0.01672384219554031,"disprot_consensus":{"full":[{"start":202,"end":215,"type":"D"},{"start":241,"end":265,"type":"D"}],"Structural state":[{"start":202,"end":215,"type":"D"},{"start":241,"end":265,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03243","name":"Alkylmercury lyase","start":76,"end":198},{"id":"PF12324","name":"Helix-turn-helix domain of alkylmercury lyase","start":11,"end":75}],"gene3D":[{"start":1,"end":212,"id":"2.40.10.490","name":"2.40.10.490"}]},"uniref50":"UniRef50_Q8G9P0","sequence":"MKLAPYILELLTSVNRTNGTADLLVPLLRELAKGRPVSRTTLAGILDWPAERVAAVLEQATSTEYDKDGNIIGYGLTLRETSYVFEIDDRRLYAWCALDTLIFPALIGRTARVSSHCAATGAPVSLTVSPSEIQAVEPAGMAVSLVLPQEAADVRQSFCCHVHFFASVPTAEDWASKHQGLEGLAIVSVHEAFGLGQEFNRHLLQTMSSRTP","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P77072","disprot_id":"DP00575","ncbi_taxon_id":562,"regions_counter":6,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":20,"region_id":"DP00575r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR structural studies reveal a novel protein fold for MerB, the organomercurial lyase involved in the bacterial mercury resistance system. <i> Di Lello P, Benison GC, Valafar H, Pitts KE, Summers AO, Legault P, Omichinski JG. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15222745","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1S6L"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":161,"region_id":"DP00575r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR structural studies reveal a novel protein fold for MerB, the organomercurial lyase involved in the bacterial mercury resistance system. <i> Di Lello P, Benison GC, Valafar H, Pitts KE, Summers AO, Legault P, Omichinski JG. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"mnecci","start":146,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15222745","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1S6L"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":161,"term_name":"flexible linker","start":146,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15222745","version":3,"reference_html":"NMR structural studies reveal a novel protein fold for MerB, the organomercurial lyase involved in the bacterial mercury resistance system. <i> Di Lello P, Benison GC, Valafar H, Pitts KE, Summers AO, Legault P, Omichinski JG. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006165","region_id":"DP00575r004","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_P77072","date":"2016-09-17T10:56:50.000Z","acc":"P77072","name":"Alkylmercury lyase","length":212,"organism":"Escherichia coli","dataset":[],"UniParc":"UPI00000BD47F","genes":[{"name":{"value":"merB"}}],"alphafold_very_low_content":0.009433962264150943,"disorder_content":0.16981132075471697,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"D"},{"start":146,"end":161,"type":"D"}],"Structural state":[{"start":1,"end":20,"type":"D"},{"start":146,"end":161,"type":"D"}],"Disorder function":[{"start":146,"end":161,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02099","name":"Josephin","start":9,"end":166},{"id":"PF02809","name":"Ubiquitin interaction motif","start":224,"end":239},{"id":"PF02809","name":"Ubiquitin interaction motif","start":244,"end":259},{"id":"PF02809","name":"Ubiquitin interaction motif","start":335,"end":350},{"id":"PF16619","name":"Unstructured region C-term to UIM in Ataxin3","start":263,"end":329}],"gene3D":[{"start":13,"end":169,"id":"3.90.70.40","name":"3.90.70.40"},{"start":27,"end":70,"id":"1.10.287.10","name":"S15/NS1, RNA-binding"}]},"uniref50":"UniRef50_P54252","sequence":"MESIFHEKQEGSLCAQHCLNNLLQGEYFSPVELSSIAHQLDEEERMRMAEGGVTSEDYRTFLQQPSGNMDDSGFFSIQVISNALKVWGLELILFNSPEYQRLRIDPINERSFICNYKEHWFTVRKLGKQWFNLNSLLTGPELISDTYLALFLAQLQQEGYSIFVVKGDLPDCEADQLLQMIRVQQMHRPKLIGEELAQLKEQRVHKTDLERVLEANDGSGMLDEDEEDLQRALALSRQEIDMEDEEADLRRAIQLSMQGSSRNISQDMTQTSGTNLTSEELRKRREAYFEKQQQKQQQQQQQQQQGDLSGQSSHPCERPATSSGALGSDLGDAMSEEDMLQAAVTMSLETVRNDLKTEGKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P54252","disprot_id":"DP00576","ncbi_taxon_id":9606,"regions_counter":11,"creator":"epapa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":361,"region_id":"DP00576r004","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Domain architecture of the polyglutamine protein ataxin-3: a globular domain followed by a flexible tail. <i> Masino L, Musi V, Menon RP, Fusi P, Kelly G, Frenkiel TA, Trottier Y, Pastore A. </i> FEBS Lett, 2003","term_id":"IDPO:0000002","curator_id":"fquaglia","start":174,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12914917","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":361,"region_id":"DP00576r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Domain architecture of the polyglutamine protein ataxin-3: a globular domain followed by a flexible tail. <i> Masino L, Musi V, Menon RP, Fusi P, Kelly G, Frenkiel TA, Trottier Y, Pastore A. </i> FEBS Lett, 2003","term_id":"IDPO:0000002","curator_id":"fquaglia","start":174,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12914917","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":291,"region_id":"DP00576r006","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The conformational ensemble of the disordered and aggregation-protective 182-291 region of ataxin-3. <i> Invernizzi G, Lambrughi M, Regonesi ME, Tortora P, Papaleo E. </i> Biochim Biophys Acta, 2013","statement":[{"text":"Thus, we employed CD spectroscopy to estimate the secondary structure\ncontent of the AT3182–291 variant (Fig. 2A). Spectra deconvolution\nhighlighted a highly disordered structure (63.7% random) with 22.4%\nof α-helices","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"epapa","start":182,"term_ontology":"IDPO","curator_name":"Elena Papaleo","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23891935","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":291,"region_id":"DP00576r007","released":"2022_03","ec_id":"ECO:0007680","reference_html":"The conformational ensemble of the disordered and aggregation-protective 182-291 region of ataxin-3. <i> Invernizzi G, Lambrughi M, Regonesi ME, Tortora P, Papaleo E. </i> Biochim Biophys Acta, 2013","statement":[{"text":"Two peaks for AT3182–291 were identified with Rg values of 1.95 ± 0.074 nm (Stoke radius 2.44 ± 0.095 nm) and 2.26 ± 0.003 nm (Stokes radius 2.84 ± 0.004 nm), respectively.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"epapa","start":182,"term_ontology":"IDPO","curator_name":"Elena Papaleo","ec_name":"chromatography evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23891935","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":361,"region_id":"DP00576r008","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Ataxin-3 is a multivalent ligand for the parkin Ubl domain. <i> Bai JJ, Safadi SS, Mercier P, Barber KR, Shaw GS. </i> Biochemistry, 2013","statement":[{"text":"the NMR spectrum of UIM_123 is suggestive of α-helical content with a large amount of disordered structure from the regions adjoining the UIM regions. This is in agreement with chemical shift index analysis of the NMR assignment data that showed α-helical stretches for UIM1 and -2 but was inconclusive for UIM3.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"epapa","start":194,"term_ontology":"IDPO","curator_name":"Elena Papaleo","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24063750","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":361,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Ataxin-3 is a multivalent ligand for the parkin Ubl domain. <i> Bai JJ, Safadi SS, Mercier P, Barber KR, Shaw GS. </i> Biochemistry, 2013","term_id":"GO:0005515","curator_id":"epapa","start":194,"term_ontology":"GO","curator_name":"Elena Papaleo","reference_id":"24063750","version":3,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00576r009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":348,"region_id":"DP00576r010","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The Structural Properties in Solution of the Intrinsically Mixed Folded Protein Ataxin-3. <i> Sicorello A, Kelly G, Oregioni A, Nováček J, Sklenář V, Pastore A. </i> Biophys J, 2018","statement":[{"text":"Overall, the C-terminal\ntail is mostly unstructured but with regions of strong\nhelical propensity throughout, with maximal values in the\nthree UIMs (residues 224–240, 244-263, and 331–348), in\nagreement with reports on peptides spanning the isolated\nUIMs (17). Interestingly, also the residues in the polyQ tract\nthat could be assigned (298–305) exhibit some helical propensity.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"epapa","start":224,"term_ontology":"IDPO","curator_name":"Elena Papaleo","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29972812","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":361,"region_id":"DP00576r011","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Domain architecture of the polyglutamine protein ataxin-3: a globular domain followed by a flexible tail. <i> Masino L, Musi V, Menon RP, Fusi P, Kelly G, Frenkiel TA, Trottier Y, Pastore A. </i> FEBS Lett, 2003","term_id":"IDPO:0000002","curator_id":"fquaglia","start":262,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12914917","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P54252","date":"2016-09-17T11:13:58.000Z","acc":"P54252","name":"Ataxin-3","length":361,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000014A814","genes":[{"name":{"value":"ATXN3"},"synonyms":[{"value":"ATX3"},{"value":"MJD"},{"value":"MJD1"},{"value":"SCA3"}]}],"alphafold_very_low_content":0.14681440443213298,"disorder_content":0.5207756232686981,"disprot_consensus":{"full":[{"start":174,"end":361,"type":"D"}],"Structural state":[{"start":174,"end":361,"type":"D"}],"Molecular function":[{"start":194,"end":361,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00156","name":"Phosphoribosyl transferase domain","start":287,"end":395},{"id":"PF13537","name":"Glutamine amidotransferase domain","start":81,"end":214}],"gene3D":[{"start":2,"end":414,"id":"3.60.20.10","name":"Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1"},{"start":279,"end":443,"id":"3.40.50.2020","name":"3.40.50.2020"}]},"uniref50":"UniRef50_P0AG16","sequence":"MCGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDANNCFRLRKANGLVSDVFEARHMQRLQGNMGIGHVRYPTAGSSSASEAQPFYVNSPYGITLAHNGNLTNAHELRKKLFEEKRRHINTTSDSEILLNIFASELDNFRHYPLEADNIFAAIAATNRLIRGAYACVAMIIGHGMVAFRDPNGIRPLVLGKRDIDENRTEYMVASESVALDTLGFDFLRDVAPGEAIYITEEGQLFTRQCADNPVSNPCLFEYVYFARPDSFIDKISVYSARVNMGTKLGEKIAREWEDLDIDVVIPIPETSCDIALEIARILGKPYRQGFVKNRYVGRTFIMPGQQLRRKSVRRKLNANRAEFRDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLASAAPEIRFPNVYGIDMPSATELIAHGREVDEIRQIIGADGLIFQDLNDLIDAVRAENPDIQQFECSVFNGVYVTKDVDQGYLDFLDTLRNDDAKAVQRQNEVENLEMHNEG","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0AG16","disprot_id":"DP00578","ncbi_taxon_id":83333,"regions_counter":1,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":505,"region_id":"DP00578r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site. <i> Krahn JM, Kim JH, Burns MR, Parry RJ, Zalkin H, Smith JL. </i> Biochemistry, 1997","term_id":"IDPO:0000002","curator_id":"fquaglia","start":484,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9333323","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1ECB"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P0AG16","date":"2016-09-14T12:49:38.000Z","acc":"P0AG16","name":"Amidophosphoribosyltransferase","length":505,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI0000111279","genes":[{"name":{"value":"purF","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01931","url":"https://hamap.expasy.org/unirule/MF_01931"}}]},"olnNames":[{"value":"b2312"},{"value":"JW2309"}]}],"alphafold_very_low_content":0.027722772277227723,"disorder_content":0.04356435643564356,"disprot_consensus":{"full":[{"start":484,"end":505,"type":"D"}],"Structural state":[{"start":484,"end":505,"type":"D"}]}},{"features":{"pfam":[{"id":"PF09253","name":"Pollen allergen Ole e 6","start":8,"end":45}],"gene3D":[{"start":1,"end":50,"id":"1.10.287.720","name":"Pollen allergen ole e 6"}]},"uniref50":"UniRef50_O24172","sequence":"DEAQFKECYDTCHKECSDKGNGFTFCEMKCDTDCSVKDVKEKLENYKPKN","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","lamiids","Lamiales","Oleaceae","Oleeae","Olea"],"uniref90":"UniRef90_O24172","disprot_id":"DP00580","ncbi_taxon_id":4146,"regions_counter":1,"creator":"aelofsson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":50,"region_id":"DP00580r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR solution structure of Ole e 6, a major allergen from olive tree pollen. <i> Treviño MA, García-Mayoral MF, Barral P, Villalba M, Santoro J, Rico M, Rodríguez R, Bruix M. </i> J Biol Chem, 2004","term_id":"IDPO:0000002","curator_id":"fquaglia","start":34,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15247256","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1SS3"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_O24172","date":"2016-08-26T14:03:56.000Z","acc":"O24172","name":"Major pollen allergen Ole e 6","length":50,"organism":"Olea europaea","dataset":[],"UniParc":"UPI0000125888","genes":[{"name":{"value":"OLE6"}}],"alphafold_very_low_content":0,"disorder_content":0.34,"disprot_consensus":{"full":[{"start":34,"end":50,"type":"D"}],"Structural state":[{"start":34,"end":50,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00071","name":"Ras family","start":16,"end":176}],"gene3D":[{"start":11,"end":183,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_P11233","sequence":"MAANKPKGQNSLALHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQIDILDTAGQEDYAAIRDNYFRSGEGFLCVFSITEMESFAATADFREQILRVKEDENVPFLLVGNKSDLEDKRQVSVEEAKNRAEQWNVNYVETSAKTRANVDKVFFDLMREIRARKMEDSKEKNGKKKRKSLAKRIRERCCIL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P11233","disprot_id":"DP00581","ncbi_taxon_id":9606,"regions_counter":11,"creator":"tlazar","regions":[{"start":187,"end":203,"reference_id":"34480001","reference_source":"pmid","reference_html":"Calmodulin extracts the Ras family protein RalA from lipid bilayers by engagement with two membrane-targeting motifs.  <i> Chamberlain SG, Gohlke A, Shafiq A, Squires IJ, Owen D, Mott HR. </i> Proc Natl Acad Sci U S A, 2021","date":"2022-08-08T11:51:44.291Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"BMRB","id":"34608"},{"db":"PDB","id":"7NQC"}],"region_id":"DP00581r006","statement":[{"text":"It has also been suggested that there is a second CaM-binding site within the disordered N-terminal extension of RalA (20). To unambiguously define the CaM-binding site on RalA, we carried out NMR-based chemical shift perturbation (CSP) experiments (Fig. 1A and SI Appendix, Fig. S1A) in the presence of Ca2+, utilizing 1H-15N heteronuclear single quantum correlation (HSQC) experiments recorded on 15N-labeled RalA· GMPPNP missing the last three residues (CΔ3, reference SI Appendix, Table S1).","type":"Results"},{"text":"Uniformly 13C,15N-labeled, HVR peptide was expressed in Escherichia coli and lipidated with MFn. NMR titrations of unlabeled CaM into the labeled peptide showed that residues within the core 10-residue motif were most affected (SI Appendix, Fig. S6).","type":"Results"},{"text":"This structure shows that the RalA-HVR forms only a single helical turn, remaining mainly disordered even when in complex with CaM.","type":"Discussion"},{"text":"The partially disordered HVR peptide in this complex, combined with flexibility in the orientations of the N- and C-lobes, is an unusual mode of CaM interaction, and there are only two other CaM-complex structures with this conformational flexibility","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-19T16:45:20.050Z"}},{"start":194,"end":203,"reference_id":"34480001","reference_source":"pmid","reference_html":"Calmodulin extracts the Ras family protein RalA from lipid bilayers by engagement with two membrane-targeting motifs.  <i> Chamberlain SG, Gohlke A, Shafiq A, Squires IJ, Owen D, Mott HR. </i> Proc Natl Acad Sci U S A, 2021","date":"2022-08-08T13:17:08.094Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"BMRB","id":"34608"},{"db":"PDB","id":"7NQC"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P0DP29","operator":null,"partner_start":1,"partner_end":149},{"db":"UniProt","id":"P0DP23","operator":"or","partner_start":1,"partner_end":149}],"region_id":"DP00581r007","statement":[{"text":"It has also been suggested that there is a second CaM-binding site within the disordered N-terminal extension of RalA (20). To unambiguously define the CaM-binding site on RalA, we carried out NMR-based chemical shift perturbation (CSP) experiments (Fig. 1A and SI Appendix, Fig. S1A) in the presence of Ca2+, utilizing 1H-15N heteronuclear single quantum correlation (HSQC) experiments recorded on 15N-labeled RalA· GMPPNP missing the last three residues (CΔ3, reference SI Appendix, Table S1).","type":"Results"},{"text":"The C-terminal Cys203 shifted significantly (CSP 0.19 ppm), but its position could also be tracked during the titrations (SI Appendix, Fig. S1A). In contrast, resonances corresponding to residues 194 to 202 of the HVR (SLAKRIRER) disappeared during the titration and gradually reappeared at different posi- tions as the titration progressed. This is known as slow exchange and indicates that the chemical shift differences between the free and CaM-bound states for these resonances are larger than the rate of exchange between these states. Such behavior demonstrates that these residues are involved in binding CaM, and the slow exchange rate between free and bound states strongly suggests that it is a high affinity interaction.","type":"Results"},{"text":"Overall, this analysis indicates that there is only one CaM-binding site in RalA, the core motif of which corresponds to 10 residues at the C terminus of the HVR.","type":"Results"},{"text":"Uniformly 13C,15N-labeled, HVR peptide was expressed in Escherichia coli and lipidated with MFn. NMR titrations of unlabeled CaM into the labeled peptide showed that residues within the core 10-residue motif were most affected (SI Appendix, Fig. S6).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-19T16:45:13.642Z"}},{"start":194,"end":203,"reference_id":"34480001","reference_source":"pmid","reference_html":"Calmodulin extracts the Ras family protein RalA from lipid bilayers by engagement with two membrane-targeting motifs.  <i> Chamberlain SG, Gohlke A, Shafiq A, Squires IJ, Owen D, Mott HR. </i> Proc Natl Acad Sci U S A, 2021","date":"2022-08-08T13:17:30.142Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001254","ec_ontology":"ECO","ec_name":"radioisotope assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P0DP29","operator":null,"partner_start":1,"partner_end":149},{"db":"UniProt","id":"P0DP23","operator":"or","partner_start":1,"partner_end":149}],"region_id":"DP00581r008","statement":[{"text":"The role of the C terminus of RalA in CaM binding was confirmed using scintillation proximity assays (SPA), where [3H] GTP·RalA was titrated into His-tagged CaM immobilized on an SPA bead (SI Appendix, Fig. S1B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-19T16:45:12.417Z"}},{"start":194,"end":203,"reference_id":"34480001","reference_source":"pmid","reference_html":"Calmodulin extracts the Ras family protein RalA from lipid bilayers by engagement with two membrane-targeting motifs.  <i> Chamberlain SG, Gohlke A, Shafiq A, Squires IJ, Owen D, Mott HR. </i> Proc Natl Acad Sci U S A, 2021","date":"2022-08-08T13:17:53.028Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P0DP29","operator":null,"partner_start":1,"partner_end":149},{"db":"UniProt","id":"P0DP23","operator":"or","partner_start":1,"partner_end":149}],"region_id":"DP00581r009","statement":[{"text":"We synthesized two maleimide-functionalized prenyl anchor mimics (SI Appendix, Fig. S2A), MFn (maleimido-farnesyl), which includes a 15-carbon far- nesyl group, and MGG (maleimido-geranylgeranyl), which includes a 20-carbon geranylgeranyl. RalA CΔ3 prenylated with MGG was insoluble in the absence of detergents but could be stabilized by binding to nanodisc membrane mimics. Titration of CaM into nanodisc-bound RalA CΔ3 MGG resulted in a return of heat changes and an apparent binding affinity of 3.8 μM (Fig. 1B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-19T16:45:11.473Z"}},{"start":194,"end":203,"reference_id":"34480001","reference_source":"pmid","reference_html":"Calmodulin extracts the Ras family protein RalA from lipid bilayers by engagement with two membrane-targeting motifs.  <i> Chamberlain SG, Gohlke A, Shafiq A, Squires IJ, Owen D, Mott HR. </i> Proc Natl Acad Sci U S A, 2021","date":"2022-08-08T13:18:08.126Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P0DP29","operator":null,"partner_start":1,"partner_end":149},{"db":"UniProt","id":"P0DP23","operator":"or","partner_start":1,"partner_end":149}],"region_id":"DP00581r010","statement":[{"text":"CaM was immobilized on the surface of a CM5 sensor chip via amine coupling and multicycle experiments recorded by flowing either RalA CΔ3 or RalA CΔ3-MFn over the immobilized protein (Fig. 1C). Dissociation constants for unmodified and prenylated RalA calculated by 1:1 equilibrium analysis (Fig. 1D) were 214 ± 27 nM and 19 ± 3 nM, respectively.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-19T16:45:10.451Z"}},{"start":1,"end":10,"reference_id":"15530367","reference_source":"pmid","reference_html":"Crystal structures of Ral-GppNHp and Ral-GDP reveal two binding sites that are also present in Ras and Rap. <i> Nicely NI, Kosak J, de Serrano V, Mattos C. </i> Structure, 2004","date":"2023-05-19T16:51:00.917Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00581r011","statement":[{"text":"Even though the N terminus was present in the constructs of Ral used for the present study, the first ten residues are disordered and are not observed in the electron density maps for any of the structures.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:135403657"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O54921"}],"cross_refs":[{"db":"PDB","id":"1UAD"}]}],"released":"2016_10","uniref100":"UniRef100_P11233","date":"2016-09-19T08:09:01.000Z","acc":"P11233","name":"Ras-related protein Ral-A","length":206,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI0000001C8F","genes":[{"name":{"value":"RALA"},"synonyms":[{"value":"RAL"}]}],"alphafold_very_low_content":0.038834951456310676,"disorder_content":0.13106796116504854,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"},{"start":187,"end":203,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":187,"end":203,"type":"D"}],"Molecular function":[{"start":194,"end":203,"type":"F"}]}},{"acc":"P16006","sequence":"MKASTVLQIAYLVSQESKCCSWKVGAVIEKNGRIISTGYNGSPAGGVNCCDYAAEQGWLLNKPKHAIIQGHKPECVSFGSTDRFVLAKEHRSAHSEWSSKNEIHAELNAILFAARNGSSIEGATMYVTLSPCPDCAKAIAQSGIKKLVYCETYDKNKPGWDDILRNAGIEVFNVPKKNLNKLNWENINEFCGE","creator":"mnecci","dataset":["Viral proteins"],"date":"2016-09-19T08:35:58.000Z","disprot_id":"DP00583","features":{"pfam":[{"id":"PF00383","name":"Cytidine and deoxycytidylate deaminase zinc-binding region","start":3,"end":150}],"gene3D":[{"start":1,"end":193,"id":"3.40.140.10","name":"Cytidine Deaminase, domain 2","_id":"685af523b4ac24d5329d7de2"}]},"genes":[{"name":{"value":"CD","evidences":[],"_id":"685af523b4ac24d5329d7ded"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d7dec"}],"length":193,"name":"Deoxycytidylate deaminase","ncbi_taxon_id":10665,"organism":"Enterobacteria phage T4","regions_counter":3,"released":"2016_10","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Uroviricota","Caudoviricetes","Caudovirales","Myoviridae","Tevenvirinae","Tequatrovirus"],"UniParc":"UPI000005CBC5","uniref100":"UniRef100_P16006","uniref50":"UniRef50_P16006","uniref90":"UniRef90_P16006","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1VQ2","_id":"685af523b4ac24d5329d7de9"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":63,"end":82,"interaction_partner":[],"reference_html":"Three-dimensional structure of the R115E mutant of T4-bacteriophage 2'-deoxycytidylate deaminase. <i> Almog R, Maley F, Maley GF, Maccoll R, Van Roey P. </i> Biochemistry, 2004","reference_id":"15504034","region_id":"DP00583r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The final model (Figure 3a) includes residues 1−62 and 84−193 of the 193-residue molecule. The absence of electron density for residues 63−83 indicates that these residues form a highly flexible loop that is disordered in the crystal.","_id":"685af523b4ac24d5329d7dea"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-02T09:23:44.219Z","_id":"685af523b4ac24d5329d7deb"},"version":1,"_id":"685af523b4ac24d5329d7de8","reference_source":"pmid"}],"__v":0,"disorder_content":0.10362694300518134,"disprot_consensus":{"full":[{"start":63,"end":82,"type":"D"}],"Structural state":[{"start":63,"end":82,"type":"D"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_A2VD23","sequence":"MLSRTVFVPLILAFVGVSISAPVSNNNGTDNDESAADQRHIFTVQFNVGTPAPADGDSVTTDGKDSAEKNEAPGDSSDTTEKPGTTDGKDSAEQHGVTTDGKDEAEQHGVTTDGQDSAEKRGEADGAPDKPDTQNGTDDTDSDQETDASHHKTGDSDENKDKPSAEDHTDGNHAGKDSTDSKESPDTTDKPEGPDSDSAPDGDSASAEKTDSDHSPDEDANKSSTEADKDDTSDKDSSQTDEKHDSDASDKDEKHEDKDEKSDEKDSSKDSEDKSQEKSDKSDDGSNSEADEQKESVESKDHDSDSQDSDSAEKKEKHDDKDQDSSDSADSKDSDEDKDKDHSEQKDSEDHEHKEKHTKDKEEHKDSDEGKDDEDKSKSDEHDKDESESKEASKSDESEQEEKKDDKSDSDNSSRDSHSDSDSDSHSDSDSDSHSDSHSDSDSDSHSDSDSDSDSDSDSDSDSDSDSNSRDKDEKKDKSSESRDEDSSDSDSKSNSESSETAEEDTNDDKDSSVEKDKTDSSDSASVEANDSDDEHDDDSKDATPSSEDHTAEKTDEDSHDVSDDDDDIDAHDDEAGVEHGTDEASKPHQEPDHHDDTTHGSDDGRKTSMPIS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Actinopterygii","Neopterygii","Teleostei","Ostariophysi","Cypriniformes","Danionidae","Danioninae","Danio"],"uniref90":"UniRef90_A2VD23","disprot_id":"DP00584","ncbi_taxon_id":7955,"regions_counter":23,"creator":"pwarholm","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":613,"region_id":"DP00584r001","released":"2022_03","ec_id":"ECO:0007689","reference_html":"Starmaker exhibits properties of an intrinsically disordered protein. <i> Kapłon TM, Rymarczyk G, Nocula-Ługowska M, Jakób M, Kochman M, Lisowski M, Szewczuk Z, Ozyhar A. </i> Biomacromolecules, 2008","term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"18636772","version":3,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"It is a well-known fact that binding Coomassie Brilliant Blue R-250 dye depends on a positively charged residue with adjoining hydrophobic residues.(20) This was probably the reason why Stm, a protein of extremely low hydrophobicity, exhibited lowered Commassie-binding.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":613,"region_id":"DP00584r006","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Starmaker exhibits properties of an intrinsically disordered protein. <i> Kapłon TM, Rymarczyk G, Nocula-Ługowska M, Jakób M, Kochman M, Lisowski M, Szewczuk Z, Ozyhar A. </i> Biomacromolecules, 2008","term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"18636772","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"The far-UV CD spectrum of StmΔSP is typical for a disordered protein, as can be seen from its large negative ellipticity at 198 nm (Figure 5B).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":613,"reference_id":"18636772","reference_source":"pmid","reference_html":"Starmaker exhibits properties of an intrinsically disordered protein. <i> Kapłon TM, Rymarczyk G, Nocula-Ługowska M, Jakób M, Kochman M, Lisowski M, Szewczuk Z, Ozyhar A. </i> Biomacromolecules, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00584r016","statement":[{"text":"According to published data, IDPs exhibit a substantially increased hydrodynamic volume relative to globular proteins, leading to a significant increase in their apparent molecular mass.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":613,"reference_id":"18636772","reference_source":"pmid","reference_html":"Starmaker exhibits properties of an intrinsically disordered protein. <i> Kapłon TM, Rymarczyk G, Nocula-Ługowska M, Jakób M, Kochman M, Lisowski M, Szewczuk Z, Ozyhar A. </i> Biomacromolecules, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00584r017","statement":[{"text":"The emission spectrum has a maximum fluorescence (λmax) of 350 nm, suggesting the occurrence of the W residue in a polar environment. This suggests that it is unlikely that Stm possesses an extensive hydrophobic core, otherwise, the W residue would probably be engaged in its formation.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":1,"end":613,"reference_id":"26445027","reference_source":"pmid","reference_html":"Calcium ion binding properties and the effect of phosphorylation on the intrinsically disordered Starmaker protein. <i> Wojtas M, Hołubowicz R, Poznar M, Maciejewska M, Ożyhar A, Dobryszycki P. </i> Biochemistry, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00584r018","statement":[{"text":"We observed different levels of Stm phosphorylation depending on the ATP concentration in the solution. The largest shift in Stm mobility was observed when ATP concentrations in the reaction mixture were 0.5 and 5 mM.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Disorder function"},{"start":1,"end":613,"reference_id":"26445027","reference_source":"pmid","reference_html":"Calcium ion binding properties and the effect of phosphorylation on the intrinsically disordered Starmaker protein. <i> Wojtas M, Hołubowicz R, Poznar M, Maciejewska M, Ożyhar A, Dobryszycki P. </i> Biochemistry, 2015","date":"2024-10-16T15:12:50.541Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","released":"2024_12","version":4,"region_id":"DP00584r019","statement":[{"text":"We determined that Stm is a calcium binding protein by using a quantitative calcium affinity assay(32) based on the competition between Stm and the fluorescent probe sensitive to calcium ions (Rhod-5N) (Figure 2).","type":"Results"},{"text":"Calcium binding by Stm and StmP was observed as a Rhod-5N fluorescence signal in samples containing Stm and StmP lower than that in the control samples (Figure 2). Fluorescence intensities were used to calculate the affinity of Stm and StmP for Ca2+. The results are summarized in Table 2.","type":"Results"},{"text":"The results of the calcium binding assay showed that Stm bound 28 calcium ions per molecule with an apparent KD of 210 μM.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a calcium ion (Ca2+).\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":613,"reference_id":"26445027","reference_source":"pmid","reference_html":"Calcium ion binding properties and the effect of phosphorylation on the intrinsically disordered Starmaker protein. <i> Wojtas M, Hołubowicz R, Poznar M, Maciejewska M, Ożyhar A, Dobryszycki P. </i> Biochemistry, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00584r020","statement":[{"text":"We determined that Stm is a calcium binding protein by using a quantitative calcium affinity assay(32) based on the competition between Stm and the fluorescent probe sensitive to calcium ions (Rhod-5N) (Figure 2).","type":"Results"},{"text":"Calcium binding by Stm and StmP was observed as a Rhod-5N fluorescence signal in samples containing Stm and StmP lower than that in the control samples (Figure 2). Fluorescence intensities were used to calculate the affinity of Stm and StmP for Ca2+. The results are summarized in Table 2.","type":"Results"},{"text":"The results of the calcium binding assay showed that Stm bound 28 calcium ions per molecule with an apparent KD of 210 μM.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":613,"reference_id":"26445027","reference_source":"pmid","reference_html":"Calcium ion binding properties and the effect of phosphorylation on the intrinsically disordered Starmaker protein. <i> Wojtas M, Hołubowicz R, Poznar M, Maciejewska M, Ożyhar A, Dobryszycki P. </i> Biochemistry, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000019","term_name":"disorder to pre-molten globule","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00584r021","statement":[{"text":"Calcium ions caused a decrease in the hydrodynamic radius of both StmP and Stm (Figure 3).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":1,"end":613,"reference_id":"26445027","reference_source":"pmid","reference_html":"Calcium ion binding properties and the effect of phosphorylation on the intrinsically disordered Starmaker protein. <i> Wojtas M, Hołubowicz R, Poznar M, Maciejewska M, Ożyhar A, Dobryszycki P. </i> Biochemistry, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000019","term_name":"disorder to pre-molten globule","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00584r022","statement":[{"text":"In contrast to gel filtration, sedimentation velocity reveals that structures of Stm and StmP are different, as suggested by the difference in the frictional ratio. \nThese results confirm that the decrease in the hydrodynamic radius of Stm and StmP in the presence of calcium is caused by compaction of the molecule rather than by dissociation of the subunits.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":1,"end":613,"reference_id":"26445027","reference_source":"pmid","reference_html":"Calcium ion binding properties and the effect of phosphorylation on the intrinsically disordered Starmaker protein. <i> Wojtas M, Hołubowicz R, Poznar M, Maciejewska M, Ożyhar A, Dobryszycki P. </i> Biochemistry, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00584r023","statement":[{"text":"The CD spectra of Stm and StmP exhibited shapes typical for IDPs. There was a large minimum near 200 nm, which is characteristic for unfolded proteins.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_A2VD23","date":"2016-09-08T13:15:36.000Z","acc":"A2VD23","name":"Protein starmaker","length":613,"organism":"Danio rerio","dataset":[],"UniParc":"UPI0000F22B70","genes":[{"name":{"value":"stm"},"orfNames":[{"value":"si:ch211-80h18.3"}]}],"alphafold_very_low_content":0.5513866231647635,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":613,"type":"T"}],"Structural state":[{"start":1,"end":613,"type":"D"}],"Disorder function":[{"start":1,"end":613,"type":"F"}],"Molecular function":[{"start":1,"end":613,"type":"F"}],"Structural transition":[{"start":1,"end":613,"type":"T"}]}},{"features":{"pfam":[{"id":"PF05773","name":"RWD domain","start":6,"end":111},{"id":"PF16543","name":"DRG Family Regulatory Proteins, Tma46","start":143,"end":204}],"gene3D":[{"start":1,"end":121,"id":"3.10.110.10","name":"Ubiquitin Conjugating Enzyme"}]},"uniref50":"UniRef50_Q9CQK7","sequence":"MTDYGEEQRNELEALESIYPDSFTVLSESPPSFTITVTSEAGENDETVQTTLKFTYSEKYPDETPLYEIFSQENLEDNDVSDILKLLALQAEENLGMVMIFTLVTAVQEKLNEIVDQIKTRREEEKKQKEKEAEEAEKKLFHGTPVTIENFLSWKAKFDAELLEIKKKRMKEEEQAGKNKLSGKQLFETDHNLDTSDIQFLEDAGNNVEVDESLFQEMDDLELEDGEDDPDYNPVAPGSDSSD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q9CQK7","disprot_id":"DP00587","ncbi_taxon_id":10090,"regions_counter":2,"creator":"pwarholm","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":243,"region_id":"DP00587r001","released":"2022_03","ec_id":"ECO:0007689","reference_html":"Rwdd1, a thymus aging related molecule, is a new member of the intrinsically unstructured protein family. <i> Kang N, Chen D, Wang L, Duan L, Liu S, Tang L, Liu Q, Cui L, He W. </i> Cell Mol Immunol, 2008","term_id":"IDPO:0000002","curator_id":"pwarholm","start":1,"term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"18954556","version":2,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-2242-7721","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":243,"region_id":"DP00587r002","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Rwdd1, a thymus aging related molecule, is a new member of the intrinsically unstructured protein family. <i> Kang N, Chen D, Wang L, Duan L, Liu S, Tang L, Liu Q, Cui L, He W. </i> Cell Mol Immunol, 2008","term_id":"IDPO:0000002","curator_id":"pwarholm","start":1,"term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"18954556","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-2242-7721","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q9CQK7","date":"2016-09-08T13:48:15.000Z","acc":"Q9CQK7","name":"RWD domain-containing protein 1","length":243,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000021726","genes":[{"name":{"value":"Rwdd1"},"synonyms":[{"value":"Dfrp2"}]}],"alphafold_very_low_content":0.04938271604938271,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":243,"type":"D"}],"Structural state":[{"start":1,"end":243,"type":"D"}]}},{"acc":"P27958","sequence":"MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARRPEGRTWAQPGYPWPLYGNEGCGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLALLSCLTVPASAYQVRNSSGLYHVTNDCPNSSVVYEAADAILHTPGCVPCVREGNASRCWVAVTPTVATRDGKLPTTQLRRHIDLLVGSATLCSALYVGDLCGSVFLVGQLFTFSPRHHWTTQDCNCSIYPGHITGHRMAWNMMMNWSPTAALVVAQLLRIPQAIMDMIAGAHWGVLAGIKYFSMVGNWAKVLVVLLLFAGVDAETHVTGGNAGRTTAGLVGLLTPGAKQNIQLINTNGSWHINSTALNCNESLNTGWLAGLFYQHKFNSSGCPERLASCRRLTDFAQGWGPISYANGSGLDERPYCWHYPPRPCGIVPAKSVCGPVYCFTPSPVVVGTTDRSGAPTYSWGANDTDVFVLNNTRPPLGNWFGCTWMNSTGFTKVCGAPPCVIGGVGNNTLLCPTDCFRKYPEATYSRCGSGPRITPRCMVDYPYRLWHYPCTINYTIFKVRMYVGGVEHRLEAACNWTRGERCDLEDRDRSELSPLLLSTTQWQVLPCSFTTLPALSTGLIHLHQNIVDVQYLYGVGSSIASWAIKWEYVVLLFLLLADARVCSCLWMMLLISQAEAALENLVILNAASLAGTHGLVSFLVFFCFAWYLKGRWVPGAVYALYGMWPLLLLLLALPQRAYALDTEVAASCGGVVLVGLMALTLSPYYKRYISWCMWWLQYFLTRVEAQLHVWVPPLNVRGGRDAVILLTCVVHPALVFDITKLLLAIFGPLWILQASLLKVPYFVRVQGLLRICALARKIAGGHYVQMAIIKLGALTGTCVYNHLAPLRDWAHNGLRDLAVAVEPVVFSRMETKLITWGADTAACGDIINGLPVSARRGQEILLGPADGMVSKGWRLLAPITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVSTATQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQTYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPTGHAVGLFRAAVCTRGVAKAVDFIPVENLETTMRSPVFTDNSSPPAVPQSFQVAHLHAPTGSGKSTKVPAAYAAKGYKVLVLNPSVAATLGFGAYMSKAHGVDPNIRTGVRTITTGSPITYSTYGKFLADAGCSGGAYDIIICDECHSTDATSISGIGTVLDQAETAGARLVVLATATPPGSVTVSHPNIEEVALSTTGEIPFYGKAIPLEVIKGGRHLIFCHSKKKCDELAAKLVALGINAVAYYRGLDVSVIPTSGDVVVVSTDALMTGFTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTLPQDAVSRTQRRGRTGRGKPGIYRFVAPGERPSGMFDSSVLCECYDAGCAWYELTPAETTVRLRAYMNTPGLPVCQDHLGFWEGVFTGLTHIDAHFLSQTKQSGENFPYLVAYQATVCARAQAPPPSWDQMRKCLIRLKPTLHGPTPLLYRLGAVQNEVTLTHPITKYIMTCMSADLEVVTSTWVLVGGVLAALAAYCLSTGCVVIVGRIVLSGKPAIIPDREVLYQEFDEMEECSQHLPYIEQGMMLAEQFKQKALGLLQTASRHAEVITPAVQTNWQKLEVFWAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTAAVTSPLTTGQTLLFNILGGWVAAQLAAPGAATAFVGAGLAGAALDSVGLGKVLVDILAGYGAGVAGALVAFKIMSGEVPSTEDLVNLLPAILSPGALAVGVVFASILRRRVGPGEGAVQWMNRLIAFASRGNHVSPTHYVPESDAAARVTAILSSLTVTQLLRRLHQWISSECTTPCSGSWLRDIWDWICEVLSDFKTWLKAKLMPQLPGIPFVSCQRGYRGVWRGDGIMHTRCHCGAEITGHVKNGTMRIVGPRTCKNMWSGTFFINAYTTGPCTPLPAPNYKFALWRVSAEEYVEIRRVGDFHYVSGMTTDNLKCPCQIPSPEFFTELDGVRLHRFAPPCKPLLREEVSFRVGLHEYPVGSQLPCEPEPDVAVLTSMLTDPSHITAEAAGRRLARGSPPSMASSSASQLSAPSLKATCTANHDSPDAELIEANLLWRQEMGGNITRVESENKVVILDSFDPLVAEEDEREVSVPAEILRKSRRFAPALPVWARPDYNPLLVETWKKPDYEPPVVHGCPLPPPRSPPVPPPRKKRTVVLTESTLPTALAELATKSFGSSSTSGITGDNTTTSSEPAPSGCPPDSDVESYSSMPPLEGEPGDPDLSDGSWSTVSSGADTEDVVCCSMSYSWTGALVTPCAAEEQKLPINALSNSLLRHHNLVYSTTSRSACQRKKKVTFDRLQVLDSHYQDVLKEVKAAASKVKANLLSVEEACSLAPPHSAKSKFGYGAKDVRCHARKAVAHINSVWKDLLEDSVTPIDTTIMAKNEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVSKLPLAVMGSSYGFQYSPGQRVEFLVQAWKSKKTPMGLSYDTRCFDSTVTESDIRTEEAIYQCCDLDPQARVAIKSLTERLYVGGPLTNSRGENCGYRRCRASRVLTTSCGNTLTRYIKARAACRAAGLQDCTMLVCGDDLVVICESAGVQEDAASLRAFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDGAGKRVYYLTRDPTTPLARAAWETARHTPVNSWLGNIIMFAPTLWARMILMTHFFSVLIARDQLEQALNCEIYGACYSIEPLDLPPIIQRLHGLSAFSLHSYSPGEINRVAACLRKLGVPPLRAWRHRAWSVRARLLARGGKAAICGKYLFNWAVRTKLKLTPITAAGRLDLSGWFTAGYSGGDIYHSVSHARPRWFWFCLLLLAAGVGIYLLPNR","creator":"esalladini","dataset":["Viral proteins","RNA-binding proteins"],"date":"2016-09-08T14:01:57.000Z","disprot_id":"DP00588","features":{"pfam":[{"id":"PF00998","name":"Viral RNA dependent RNA polymerase","start":2423,"end":2932},{"id":"PF01001","name":"Hepatitis C virus non-structural protein NS4b","start":1728,"end":1921},{"id":"PF01006","name":"Hepatitis C virus non-structural protein NS4a","start":1658,"end":1711},{"id":"PF01506","name":"Hepatitis C virus non-structural 5a protein membrane anchor","start":1974,"end":1996},{"id":"PF01538","name":"Hepatitis C virus non-structural protein NS2","start":811,"end":1005},{"id":"PF01539","name":"Hepatitis C virus envelope glycoprotein E1","start":193,"end":382},{"id":"PF01542","name":"Hepatitis C virus core protein","start":116,"end":190},{"id":"PF01543","name":"Hepatitis C virus capsid protein","start":2,"end":115},{"id":"PF01560","name":"Hepatitis C virus non-structural protein E2/NS1","start":386,"end":729},{"id":"PF02907","name":"Hepatitis C virus NS3 protease","start":1056,"end":1203},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1294,"end":1355},{"id":"PF08300","name":"Hepatitis C virus non-structural 5a zinc finger domain","start":2006,"end":2067},{"id":"PF08301","name":"Hepatitis C virus non-structural 5a domain 1b","start":2068,"end":2168},{"id":"PF12941","name":"HCV NS5a protein C-terminal region","start":2179,"end":2420},{"id":"PF22027","name":"NS3 RNA helicase, C-terminal helical domain","start":1516,"end":1656}],"gene3D":[{"start":900,"end":977,"id":"1.20.1280.150","name":"Hepatitis C virus non-structural protein NS2, N-terminal domain","_id":"685af523b4ac24d5329d7dfc"},{"start":2075,"end":2160,"id":"2.20.25.220","name":"Hepatitis C virus NS5A, 1B domain","_id":"685af523b4ac24d5329d7dfd"},{"start":994,"end":1021,"id":"2.30.30.710","name":"Hepatitis C virus non-structural protein NS2, C-terminal domain","_id":"685af523b4ac24d5329d7dfe"},{"start":2014,"end":2074,"id":"2.20.25.210","name":"Hepatitis C NS5A, domain 1B","_id":"685af523b4ac24d5329d7dff"},{"start":1022,"end":1120,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d7e00"},{"start":1513,"end":1641,"id":"1.10.820.10","name":"RNA Helicase Chain A , domain 3","_id":"685af523b4ac24d5329d7e01"},{"start":206,"end":276,"id":"2.30.30.1080","name":"Hepatitis C virus envelope glycoprotein E1, chain C","_id":"685af523b4ac24d5329d7e02"},{"start":1122,"end":1205,"id":"2.40.10.10","name":"Trypsin-like serine proteases","_id":"685af523b4ac24d5329d7e03"},{"start":2,"end":45,"id":"4.10.710.10","name":"Hepatitis C Virus Capsid Protein; Chain A","_id":"685af523b4ac24d5329d7e04"},{"start":2608,"end":2663,"id":"3.30.70.270","name":"3.30.70.270","_id":"685af523b4ac24d5329d7e05"},{"start":1355,"end":1512,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d7e06"},{"start":2689,"end":2788,"id":"3.30.70.270","name":"3.30.70.270","_id":"685af523b4ac24d5329d7e07"},{"start":1206,"end":1354,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d7e08"}]},"genes":[],"length":3011,"name":"Genome polyprotein","ncbi_taxon_id":11108,"organism":"Hepatitis C virus genotype 1a (isolate H)","regions_counter":29,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Hepacivirus"],"UniParc":"UPI000004ACD7","uniref100":"UniRef100_P27958","uniref50":"UniRef50_P27958","uniref90":"UniRef90_P27958","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":82,"interaction_partner":[],"reference_html":"Structure and dynamics of the N-terminal half of hepatitis C virus core protein: an intrinsically unstructured protein. <i> Duvignaud JB, Savard C, Fromentin R, Majeau N, Leclerc D, Gagné SM. </i> Biochem Biophys Res Commun, 2009","reference_id":"18992225","region_id":"DP00588r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"A trypsin digestion test indicates that C82 is significantly sensitive to degradation (Fig. 2C)","_id":"685af523b4ac24d5329d7e0a"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T11:10:20.608Z","_id":"685af523b4ac24d5329d7e0b"},"version":3,"_id":"685af523b4ac24d5329d7e09","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":82,"interaction_partner":[],"reference_html":"Structure and dynamics of the N-terminal half of hepatitis C virus core protein: an intrinsically unstructured protein. <i> Duvignaud JB, Savard C, Fromentin R, Majeau N, Leclerc D, Gagné SM. </i> Biochem Biophys Res Commun, 2009","reference_id":"18992225","region_id":"DP00588r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The C82 CD spectrum shows a minimum near 200 nm indicating that this protein is a random coil that lacks apparent secondary structure (Fig. 3A).","_id":"685af523b4ac24d5329d7e16"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T11:10:13.888Z","_id":"685af523b4ac24d5329d7e17"},"version":3,"_id":"685af523b4ac24d5329d7e15","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"15768","_id":"685af523b4ac24d5329d7e21"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":82,"interaction_partner":[],"reference_html":"Structure and dynamics of the N-terminal half of hepatitis C virus core protein: an intrinsically unstructured protein. <i> Duvignaud JB, Savard C, Fromentin R, Majeau N, Leclerc D, Gagné SM. </i> Biochem Biophys Res Commun, 2009","reference_id":"18992225","region_id":"DP00588r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Although there is a poor 1HN chemical shift distribution in the HSQC of C82 (0.95 ppm), which is typical of proteins that possess little tertiary structure and are disordered, we observed 63 of the 69 expected peaks. Moreover, the NOESY spectra of C82 contain few NOE correlations which is indicative of the absence of secondary structure.","_id":"685af523b4ac24d5329d7e1f"},{"type":"Results","text":"As shown in Figure 4D, CSI Cα of C82 is oscillating around zero, suggesting that C82 exists in an unstructured conformation.","_id":"685af523b4ac24d5329d7e20"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T12:04:25.698Z","_id":"685af523b4ac24d5329d7e22"},"version":3,"_id":"685af523b4ac24d5329d7e1e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":82,"interaction_partner":[],"reference_html":"Structure and dynamics changes induced by 2,2,2-trifluoro-ethanol (TFE) on the N-terminal half of hepatitis C virus core protein. <i> Duvignaud JB, Leclerc D, Gagné SM. </i> Biochem Cell Biol, 2010","reference_id":"20453932","region_id":"DP00588r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The NOEs, with an average of 0.51, are significantly higher than those observed for C82 in water (Duvignaud et al. 2009) (Fig. 4) and indicate that C82 gains significant order in TFE, although probably not as ordered as a typical globular protein (Fig. 4).","_id":"685af523b4ac24d5329d7e2d"},{"type":"Curator statement","text":"In aqueous solution this region is disordered, as shown by NOEs typical of proteins without any stable secondary structure (Fig. 4).","_id":"685af523b4ac24d5329d7e2e"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T11:08:43.436Z","_id":"685af523b4ac24d5329d7e2f"},"version":3,"_id":"685af523b4ac24d5329d7e2c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":82,"interaction_partner":[],"reference_html":"Structure and dynamics changes induced by 2,2,2-trifluoro-ethanol (TFE) on the N-terminal half of hepatitis C virus core protein. <i> Duvignaud JB, Leclerc D, Gagné SM. </i> Biochem Cell Biol, 2010","reference_id":"20453932","region_id":"DP00588r016","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"Authors show the region is intrinsically unstructured by its large negative ellipticity at 200 nm in a circular dichroism study (Fig. 1E).","_id":"685af523b4ac24d5329d7e35"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T11:04:13.810Z","_id":"685af523b4ac24d5329d7e36"},"version":1,"_id":"685af523b4ac24d5329d7e34","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006003","ec_name":"electron microscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":82,"interaction_partner":[],"reference_html":"Structure and dynamics of the N-terminal half of hepatitis C virus core protein: an intrinsically unstructured protein. <i> Duvignaud JB, Savard C, Fromentin R, Majeau N, Leclerc D, Gagné SM. </i> Biochem Biophys Res Commun, 2009","reference_id":"18992225","region_id":"DP00588r018","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"To confirm our final product, we performed an SDS–PAGE electrophoresis (Fig. 2A) and an in vitro assembly assay showing that the C82 was able to assemble into NLPs in presence of tRNA as seen by electron microscopy (Fig. 2B).","_id":"685af523b4ac24d5329d7e3c"},{"type":"Results","text":"However, C82 is able to organize itself in vitro into NLPs in the presence of structured RNA.","_id":"685af523b4ac24d5329d7e3d"}],"states_connection":[],"term_comment":"","term_def":"\"The assembly of a virus capsid from its protein subunits.\" [ISBN:0781702534, UniProtKB-KW:KW-0118]","term_id":"GO:0019069","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral capsid assembly","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-15T10:52:16.819Z","_id":"685af523b4ac24d5329d7e3e"},"version":1,"_id":"685af523b4ac24d5329d7e3b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006003","ec_name":"electron microscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":82,"interaction_partner":[],"reference_html":"Structure and dynamics of the N-terminal half of hepatitis C virus core protein: an intrinsically unstructured protein. <i> Duvignaud JB, Savard C, Fromentin R, Majeau N, Leclerc D, Gagné SM. </i> Biochem Biophys Res Commun, 2009","reference_id":"18992225","region_id":"DP00588r019","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"To confirm our final product, we performed an SDS–PAGE electrophoresis (Fig. 2A) and an in vitro assembly assay showing that the C82 was able to assemble into NLPs in presence of tRNA as seen by electron microscopy (Fig. 2B).","_id":"685af523b4ac24d5329d7e40"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_id":"GO:0003723","term_is_binding":true,"term_is_obsolete":false,"term_name":"RNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T11:13:25.588Z","_id":"685af523b4ac24d5329d7e41"},"version":1,"_id":"685af523b4ac24d5329d7e3f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006003","ec_name":"electron microscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":82,"interaction_partner":[{"db":"UniProt","id":"P27958","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7e46"}],"reference_html":"Structure and dynamics of the N-terminal half of hepatitis C virus core protein: an intrinsically unstructured protein. <i> Duvignaud JB, Savard C, Fromentin R, Majeau N, Leclerc D, Gagné SM. </i> Biochem Biophys Res Commun, 2009","reference_id":"18992225","region_id":"DP00588r021","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"To confirm our final product, we performed an SDS–PAGE electrophoresis (Fig. 2A) and an in vitro assembly assay showing that the C82 was able to assemble into NLPs in presence of tRNA as seen by electron microscopy (Fig. 2B).","_id":"685af523b4ac24d5329d7e47"},{"type":"Results","text":"However, C82 is able to organize itself in vitro into NLPs in the presence of structured RNA.","_id":"685af523b4ac24d5329d7e48"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T11:11:49.666Z","_id":"685af523b4ac24d5329d7e49"},"version":1,"_id":"685af523b4ac24d5329d7e45","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":82,"interaction_partner":[],"reference_html":"Structure and dynamics of the N-terminal half of hepatitis C virus core protein: an intrinsically unstructured protein. <i> Duvignaud JB, Savard C, Fromentin R, Majeau N, Leclerc D, Gagné SM. </i> Biochem Biophys Res Commun, 2009","reference_id":"18992225","region_id":"DP00588r022","released":"2022_03","sample":[],"statement":[{"type":"Figure","text":"It should be noted that C82 migrates at an abnormal molecular weight of ∼15 kDa instead of the expected ∼10 kDa.","_id":"685af523b4ac24d5329d7e4b"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T12:04:17.989Z","_id":"685af523b4ac24d5329d7e4c"},"version":1,"_id":"685af523b4ac24d5329d7e4a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006003","ec_name":"electron microscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":79,"interaction_partner":[],"reference_html":"The N-terminal half of the core protein of hepatitis C virus is sufficient for nucleocapsid formation. <i> Majeau N, Gagné V, Boivin A, Bolduc M, Majeau JA, Ouellet D, Leclerc D. </i> J Gen Virol, 2004","reference_id":"15039539","region_id":"DP00588r023","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"We showed that the N-terminal 75 aa (C 1–75) were sufficient to trigger the formation of NLPs in vitro, while the construct C 1–71 failed. The C 1–75 protein contains only four additional amino acids (PEGR), which delimit the border of the second basic cluster of the C protein, which can play an important role in virus assembly. More than 70 % of the structures observed with the C 1–75 protein were, however, aggregates with a diameter exceeding the expected range for the HCV nucleocapsid. The addition of a further four amino acids in the construct C 1–79 stabilized the particles and gave rise to uniform and structured particles resembling HCV nucleocapsids. Also, the NLPs produced from C 1–82 formed one band with a density of 1·32 g ml−1 in a CsCl gradient, suggesting that all the NLPs were uniform in diameter, appearance and density (Fig. 5F5). Based on these results, we suggest that the minimal assembly domain of the HCV C protein resides in the first 79 aa of the protein. ","_id":"685af523b4ac24d5329d7e4e"}],"states_connection":[],"term_comment":"","term_def":"\"The assembly of a virus capsid from its protein subunits.\" [ISBN:0781702534, UniProtKB-KW:KW-0118]","term_go_domain":"P","term_id":"GO:0019069","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral capsid assembly","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-15T10:52:02.166Z","_id":"685af523b4ac24d5329d7e4f"},"version":1,"_id":"685af523b4ac24d5329d7e4d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2212,"end":2307,"interaction_partner":[],"reference_html":"Molecular and structural characterization of the domain 2 of hepatitis C virus non-structural protein 5A. <i> Liang Y, Kang CB, Yoon HS. </i> Mol Cells, 2006","reference_id":"16951545","region_id":"DP00588r024","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"Our  NMR  data demonstrated that the 1D 1H spectrum of NS5A-D2 lacks  NMR  signals  in  the  region  of  the  methyl  protons  and the 2D 1H -15N HSQC spectrum show a narrow dispersion  in  the  backbone  amide  proton  resonance  signals  which  only  covers  the  range  of  6.7−8.5  ppm.  Taken  together, our data suggest that the NS5A-D2 is natively dis-ordered or dynamic and is not well structured.","_id":"685af523b4ac24d5329d7e51"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-15T10:45:20.716Z","_id":"685af523b4ac24d5329d7e52"},"version":1,"_id":"685af523b4ac24d5329d7e50","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2212,"end":2307,"interaction_partner":[{"db":"UniProt","id":"P27958","partner_start":2559,"partner_end":2575,"_id":"685af523b4ac24d5329d7e54"}],"reference_html":"Molecular and structural characterization of the domain 2 of hepatitis C virus non-structural protein 5A. <i> Liang Y, Kang CB, Yoon HS. </i> Mol Cells, 2006","reference_id":"16951545","region_id":"DP00588r025","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"The NMR result showed that some perturbations  in  the  chemical  shifts  were  detected  in  the  15N-HSQC  spectrum  of  15N  labeled  NS5A-D2  protein  upon  the addition of NS5B MK-17 peptide (Figs. 7A and 7B), indicating  that  the  purified  NS5A-D2  shows  binding  to  the peptide. ","_id":"685af523b4ac24d5329d7e55"},{"type":"Curator statement","text":"NS5A-D2 comprises the region 2212-2307 of the Hepatitis C virus genotype 1a (isolate H) genome polyprotein. The MK-17 peptide consist on the 139−155 residues of NS5B, which corresponds to 2559-2575 region of the Hepatitis C virus genotype 1a (isolate H) genome polyprotein.","_id":"685af523b4ac24d5329d7e56"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-15T10:45:49.625Z","_id":"685af523b4ac24d5329d7e57"},"version":1,"_id":"685af523b4ac24d5329d7e53","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005640","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","ec_ontology":"ECO","start":2242,"end":2307,"interaction_partner":[{"db":"UniProt","id":"P27958","partner_start":2421,"partner_end":2990,"_id":"685af523b4ac24d5329d7e59"}],"reference_html":"Molecular and structural characterization of the domain 2 of hepatitis C virus non-structural protein 5A. <i> Liang Y, Kang CB, Yoon HS. </i> Mol Cells, 2006","reference_id":"16951545","region_id":"DP00588r026","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"Both  NS5AΔN  and  NS5A-D2  were pulled down with GST-NS5Bt (Fig. 3C, lane 2 and lane  5)  but  not  with  GST  (Fig.  3C,  lane  3  and  lane  6),  indicating  the  specific  interaction  of  NS5A-D2  with  NS5B in  vitro.","_id":"685af523b4ac24d5329d7e5a"},{"type":"Curator statement","text":"NS5A-D2 comprises the region 2212-2307 and the NS5Bt peptide consist on the 2421-2990 region of the Hepatitis C virus genotype 1a (isolate H) genome polyprotein.","_id":"685af523b4ac24d5329d7e5b"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-15T10:45:44.056Z","_id":"685af523b4ac24d5329d7e5c"},"version":1,"_id":"685af523b4ac24d5329d7e58","reference_source":"pmid"}],"__v":0,"disorder_content":0.0591165725672534,"disprot_consensus":{"full":[{"start":1,"end":82,"type":"D"},{"start":2212,"end":2307,"type":"D"}],"Structural state":[{"start":1,"end":82,"type":"D"},{"start":2212,"end":2307,"type":"D"}],"Biological process":[{"start":1,"end":82,"type":"F"}],"Molecular function":[{"start":1,"end":82,"type":"F"},{"start":2212,"end":2307,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":1033,"end":1066},{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":1137,"end":1172},{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":1262,"end":1296},{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":1297,"end":1331},{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":1403,"end":1437},{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":1439,"end":1464},{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":1529,"end":1563},{"id":"PF02382","name":"N-terminal domain in RTX protein","start":588,"end":896},{"id":"PF03497","name":"Anthrax toxin LF subunit","start":17,"end":179},{"id":"PF06594","name":"Haemolysin-type calcium binding protein related domain","start":1628,"end":1656}],"gene3D":[{"start":1006,"end":1119,"id":"2.150.10.10","name":"Serralysin-like metalloprotease, C-terminal"},{"start":1128,"end":1227,"id":"2.150.10.10","name":"Serralysin-like metalloprotease, C-terminal"},{"start":44,"end":187,"id":"3.90.1760.10","name":"Anthrax toxin, edema factor, central domain"},{"start":1240,"end":1303,"id":"2.150.10.10","name":"Serralysin-like metalloprotease, C-terminal"},{"start":1529,"end":1681,"id":"2.150.10.10","name":"Serralysin-like metalloprotease, C-terminal"},{"start":1403,"end":1505,"id":"2.150.10.10","name":"Serralysin-like metalloprotease, C-terminal"},{"start":1304,"end":1383,"id":"2.150.10.10","name":"Serralysin-like metalloprotease, C-terminal"},{"start":241,"end":354,"id":"3.30.70.1720","name":"3.30.70.1720"}]},"uniref50":"UniRef50_Q57506","sequence":"MQQSHQAGYANAADRESGIPAAVLDGIKAVAKEKNATLMFRLVNPHSTSLIAEGVATKGLGVHAKSSDWGLQAGYIPVNPNLSKLFGRAPEVIARADNDVNSSLAHGHTAVDLTLSKERLDYLRQAGLVTGMADGVVASNHAGYEQFEFRVKETSDGRYAVQYRRKGGDDFEAVKVIGNAAGIPLTADIDMFAIMPHLSNFRDSARSSVTSGDSVTDYLARTRRAASEATGGLDRERIDLLWKIARAGARSAVGTEARRQFRYDGDMNIGVITDFELEVRNALNRRAHAVGAQDVVQHGTEQNNPFPEADEKIFVVSATGESQMLTRGQLKEYIGQQRGEGYVFYENRAYGVAGKSLFDDGLGAAPGVPSGRSKFSPDVLETVPASPGLRRPSLGAVERQDSGYDSLDGVGSRSFSLGEVSDMAAVEAAELEMTRQVLHAGARQDDAEPGVSGASAHWGQRALQGAQAVAAAQRLVHAIALMTQFGRAGSTNTPQEAASLSAAVFGLGEASSAVAETVSGFFRGSSRWAGGFGVAGGAMALGGGIAAAVGAGMSLTDDAPAGQKAAAGAEIALQLTGGTVELASSIALALAAARGVTSGLQVAGASAGAAAGALAAALSPMEIYGLVQQSHYADQLDKLAQESSAYGYEGDALLAQLYRDKTAAEGAVAGVSAVLSTVGAAVSIAAAASVVGAPVAVVTSLLTGALNGILRGVQQPIIEKLANDYARKIDELGGPQAYFEKNLQARHEQLANSDGLRKMLADLQAGWNASSVIGVQTTEISKSALELAAITGNADNLKSVDVFVDRFVQGERVAGQPVVLDVAAGGIDIASRKGERPALTFITPLAAPGEEQRRRTKTGKSEFTTFVEIVGKQDRWRIRDGAADTTIDLAKVVSQLVDANGVLKHSIKLDVIGGDGDDVVLANASRIHYDGGAGTNTVSYAALGRQDSITVSADGERFNVRKQLNNANVYREGVATQTTAYGKRTENVQYRHVELARVGQLVEVDTLEHVQHIIGGAGNDSITGNAHDNFLAGGSGDDRLDGGAGNDTLVGGEGQNTVIGGAGDDVFLQDLGVWSNQLDGGAGVDTVKYNVHQPSEERLERMGDTGIHADLQKGTVEKWPALNLFSVDHVKNIENLHGSRLNDRIAGDDQDNELWGHDGNDTIRGRGGDDILRGGLGLDTLYGEDGNDIFLQDDETVSDDIDGGAGLDTVDYSAMIHPGRIVAPHEYGFGIEADLSREWVRKASALGVDYYDNVRNVENVIGTSMKDVLIGDAQANTLMGQGGDDTVRGGDGDDLLFGGDGNDMLYGDAGNDTLYGGLGDDTLEGGAGNDWFGQTQAREHDVLRGGDGVDTVDYSQTGAHAGIAAGRIGLGILADLGAGRVDKLGEAGSSAYDTVSGIENVVGTELADRITGDAQANVLRGAGGADVLAGGEGDDVLLGGDGDDQLSGDAGRDRLYGEAGDDWFFQDAANAGNLLDGGDGRDTVDFSGPGRGLDAGAKGVFLSLGKGFASLMDEPETSNVLRNIENAVGSARDDVLIGDAGANVLNGLAGNDVLSGGAGDDVLLGDEGSDLLSGDAGNDDLFGGQGDDTYLFGVGYGHDTIYESGGGHDTIRINAGADQLWFARQGNDLEIRILGTDDALTVHDWYRDADHRVEIIHAANQAVDQAGIEKLVEAMAQYPDPGAAAAAPPAARVPDTLMQSLAVNWR","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Burkholderiales","Alcaligenaceae","Bordetella"],"uniref90":"UniRef90_Q57506","disprot_id":"DP00591","dataset":["Unicellular toxins and antitoxins","Bacterial virulence-related proteins"],"ncbi_taxon_id":568706,"regions_counter":28,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1706,"region_id":"DP00591r003","reference_html":"RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion. <i> Chenal A, Guijarro JI, Raynal B, Delepierre M, Ladant D. </i> J Biol Chem, 2009","ec_id":"ECO:0006204","version":3,"term_id":"IDPO:0000002","curator_id":"bmesza","start":1006,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"The far-UV CD spectrum of the apo-state of RD (apo-RD, in the absence of calcium) was typical of a predominantly unfolded protein, as shown by the strong negative π0-π* band around 200 nm (Fig. 1). ","type":"Results"},{"text":"Here, we have characterized the structural and hydrodynamic properties of the RTX Repeat Domain (RD) of the CyaA toxin from Bordetella pertussis. This 701-amino acid long domain contains about 40 RTX motifs. We showed that, in the absence of calcium, RD was natively disordered, weakly stable, and highly hydrated.","type":"Abstract"},{"text":"In summary, CD and NMR data indicate that the apo-form of RD was largely unfolded with a weak secondary and tertiary structure content, while calcium binding triggered the folding of the protein into a compact and β-rich (>30-35%) conformation.","type":"Results"}],"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"fquaglia","timestamp":"2020-12-15T19:34:26.921Z","curator_name":"Federica Quaglia"},"released":"2022_03","reference_id":"19015266","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","version":3,"ec_ontology":"ECO","end":1706,"term_name":"disorder to order","start":1006,"ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0003-0919-4449","curator_id":"bmesza","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"19015266","statement":[{"text":"Upon addition of 2 mm calcium to apo-RD, secondary structures were formed, as revealed by the concomitant intensity decrease of the π0-π* band and the increase of the n′-π* band in the holo-RD spectrum, as previously reported (10, 26).","type":"Results"},{"text":"In summary, CD and NMR data indicate that the apo-form of RD was largely unfolded with a weak secondary and tertiary structure content, while calcium binding triggered the folding of the protein into a compact and β-rich (>30-35%) conformation.","type":"Results"}],"reference_html":"RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion. <i> Chenal A, Guijarro JI, Raynal B, Delepierre M, Ladant D. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","validated":{"curator_id":"fquaglia","timestamp":"2020-12-15T19:35:16.809Z","curator_name":"Federica Quaglia"},"region_id":"DP00591r004","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1706,"region_id":"DP00591r005","reference_html":"RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion. <i> Chenal A, Guijarro JI, Raynal B, Delepierre M, Ladant D. </i> J Biol Chem, 2009","ec_id":"ECO:0001249","version":3,"term_id":"IDPO:0000002","curator_id":"bmesza","start":1006,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"fluorescence evidence used in manual assertion","statement":[{"text":"Thermal-induced unfolding of RD was followed by intrinsic fluorescence of tryptophan at various calcium concentrations. The ratio of fluorescence intensities at 360 and 320 nm (rFI360/320) was used to follow the unfolding of RD (Fig. 4A). The van't Hoff free enthalpy (ΔHvH) and temperature of half-melting (Tm) were then determined. As shown in Fig. 4B, both Tm and ΔHvH increased with calcium concentrations to reach a plateau above 1.5-2 mm. We obtained similar results from thermal-induced denaturation of RD followed by far- and near-UV CD (data not shown). All together these data indicated that apo-RD was unstable, as expected for a disordered state, while holo-RD was strongly stabilized by calcium binding. ","type":"Results"},{"text":"Here, we have characterized the structural and hydrodynamic properties of the RTX Repeat Domain (RD) of the CyaA toxin from Bordetella pertussis. This 701-amino acid long domain contains about 40 RTX motifs. We showed that, in the absence of calcium, RD was natively disordered, weakly stable, and highly hydrated.","type":"Abstract"}],"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"fquaglia","timestamp":"2020-12-15T19:34:20.858Z","curator_name":"Federica Quaglia"},"released":"2022_03","reference_id":"19015266","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","version":3,"ec_ontology":"ECO","end":1706,"term_name":"disorder to order","start":1006,"ec_name":"fluorescence evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0003-0919-4449","curator_id":"bmesza","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"19015266","statement":[{"text":"Thermal-induced unfolding of RD was followed by intrinsic fluorescence of tryptophan at various calcium concentrations. The ratio of fluorescence intensities at 360 and 320 nm (rFI360/320) was used to follow the unfolding of RD (Fig. 4A). The van't Hoff free enthalpy (ΔHvH) and temperature of half-melting (Tm) were then determined. As shown in Fig. 4B, both Tm and ΔHvH increased with calcium concentrations to reach a plateau above 1.5-2 mm. We obtained similar results from thermal-induced denaturation of RD followed by far- and near-UV CD (data not shown). All together these data indicated that apo-RD was unstable, as expected for a disordered state, while holo-RD was strongly stabilized by calcium binding. ","type":"Results"}],"reference_html":"RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion. <i> Chenal A, Guijarro JI, Raynal B, Delepierre M, Ladant D. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0001249","validated":{"curator_id":"fquaglia","timestamp":"2020-12-15T19:35:31.244Z","curator_name":"Federica Quaglia"},"region_id":"DP00591r006","ec_go":"IDA","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1706,"region_id":"DP00591r007","reference_html":"RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion. <i> Chenal A, Guijarro JI, Raynal B, Delepierre M, Ladant D. </i> J Biol Chem, 2009","ec_id":"ECO:0006198","version":3,"term_id":"IDPO:0000002","curator_id":"bmesza","start":1006,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","statement":[{"text":"The one-dimensional spectrum of apo-RD in the presence of the denaturant GdnHCl (5.3 m) showed no evident secondary chemical shifts, with all peaks appearing at the expected frequencies for an unfolded protein, the so-called “random-coil” chemical shifts (Fig. 2A). The low chemical-shift dispersion was consistent with a protein with no stable secondary and tertiary structures.","type":"Results"},{"text":"Here, we have characterized the structural and hydrodynamic properties of the RTX Repeat Domain (RD) of the CyaA toxin from Bordetella pertussis. This 701-amino acid long domain contains about 40 RTX motifs. We showed that, in the absence of calcium, RD was natively disordered, weakly stable, and highly hydrated.","type":"Abstract"},{"text":"The one-dimensional spectrum of apo-RD in the presence of the denaturant GdnHCl (5.3 m) showed no evident secondary chemical shifts, with all peaks appearing at the expected frequencies for an unfolded protein, the so-called “random-coil” chemical shifts (Fig. 2A). The low chemical-shift dispersion was consistent with a protein with no stable secondary and tertiary structures. The spectrum of the apo-form under native conditions also showed very poor chemical shift dispersion, and resembled that of the protein denatured in GdnHCl, but with somewhat narrower lines. Noticeably, the bands of the apo-RD spectrum were strikingly narrow for a 701-residue long protein, suggesting that apo-RD had a highly dynamic structure in which most of its side-chains could freely reorient in solution. These observations suggested that apo-RD was mainly natively disordered.\" as they test both apo-RD alone and with denaturant (see fig.2a) and \"As shown in Fig. 2C, The nOe build-up curves obtained for apo-RD in 5.3 m GdnHCl showed practically no transfer of saturation, as expected for the disordered conformations adopted by the protein in these conditions. Apo-RD in the absence of denaturant showed also very limited nOes, albeit significantly higher than that of RD in GdnHCl.","type":"Results"},{"text":"In summary, CD and NMR data indicate that the apo-form of RD was largely unfolded with a weak secondary and tertiary structure content, while calcium binding triggered the folding of the protein into a compact and β-rich (>30-35%) conformation.","type":"Results"}],"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"fquaglia","timestamp":"2020-12-15T19:34:30.708Z","curator_name":"Federica Quaglia"},"released":"2022_03","reference_id":"19015266","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","version":3,"ec_ontology":"ECO","end":1706,"term_name":"disorder to order","start":1006,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0003-0919-4449","curator_id":"bmesza","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"19015266","statement":[{"text":"As both states were monomeric (see below), the short T2 value (characteristic of slow dynamic processes) of holo-RD mainly reflected the compactness of the folded protein, while the T2 value of apo-RD most likely resulted from the fast internal motions within the unstructured conformations of the Ca2+-free polypeptide. The high β-sheet content of holo-RD, as evidenced by the envelope of upfield-shifted Hα signals, also strongly suggested that the observed line-broadening resulted from a calcium-induced folding-compaction process.","type":"Results"},{"text":"The NMR spectrum of calcium-bound RD was drastically different. First, it exhibited an increase of the envelope of upfield-shifted Hα protons, providing direct evidence that holo-RD was more structured, with a β-sheet content (calculated as above) of at least 30-35%. Second, the signals became very broad as expected for a compact protein of 72.6 kDa. The line broadening of the 1H spectrum reflected a major change in the dynamic behavior of the protein upon calcium binding.\" and \"The high β-sheet content of holo-RD, as evidenced by the envelope of upfield-shifted Hα signals, also strongly suggested that the observed line-broadening resulted from a calcium-induced folding-compaction process.\" and \"In contrast, holo-RD showed a very efficient transfer of saturation: the apparent cross-relaxation rate of the holo-form (σ = 3.1 ± 0.1 s-1) was respectively, 14- and 100-fold higher than that of apo-RD or that of apo-RD in the presence of GdnHCl. Therefore, the holo state was much more compact than the apo-form.","type":"Results"},{"text":"In summary, CD and NMR data indicate that the apo-form of RD was largely unfolded with a weak secondary and tertiary structure content, while calcium binding triggered the folding of the protein into a compact and β-rich (>30-35%) conformation.","type":"Results"}],"reference_html":"RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion. <i> Chenal A, Guijarro JI, Raynal B, Delepierre M, Ladant D. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006198","validated":{"curator_id":"fquaglia","timestamp":"2020-12-15T19:35:04.571Z","curator_name":"Federica Quaglia"},"region_id":"DP00591r008","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1706,"region_id":"DP00591r009","reference_html":"RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion. <i> Chenal A, Guijarro JI, Raynal B, Delepierre M, Ladant D. </i> J Biol Chem, 2009","ec_id":"ECO:0006275","version":3,"term_id":"IDPO:0000002","curator_id":"bmesza","start":1006,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"analytical ultracentrifugation evidence used in manual assertion","statement":[{"text":"Equilibrium AUC experiments confirmed that apo-RD and holo-RD had both a same molecular mass of 73 kDa (Table 1), while velocity AUC indicated that the two states displayed different sedimentation coefficients (values of 2.5 S and 4.5 S for the apo and holo states, respectively) resulting from distinct hydrodynamic properties.","type":"Results"},{"text":"Here, we have characterized the structural and hydrodynamic properties of the RTX Repeat Domain (RD) of the CyaA toxin from Bordetella pertussis. This 701-amino acid long domain contains about 40 RTX motifs. We showed that, in the absence of calcium, RD was natively disordered, weakly stable, and highly hydrated.","type":"Abstract"}],"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"fquaglia","timestamp":"2020-12-15T19:34:35.168Z","curator_name":"Federica Quaglia"},"released":"2022_03","reference_id":"19015266","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","version":3,"ec_ontology":"ECO","end":1706,"term_name":"disorder to order","start":1006,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0003-0919-4449","curator_id":"bmesza","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"19015266","statement":[{"text":"Equilibrium AUC experiments confirmed that apo-RD and holo-RD had both a same molecular mass of 73 kDa (Table 1), while velocity AUC indicated that the two states displayed different sedimentation coefficients (values of 2.5 S and 4.5 S for the apo and holo states, respectively) resulting from distinct hydrodynamic properties.","type":"Results"}],"reference_html":"RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion. <i> Chenal A, Guijarro JI, Raynal B, Delepierre M, Ladant D. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006275","validated":{"curator_id":"fquaglia","timestamp":"2020-12-15T19:34:55.537Z","curator_name":"Federica Quaglia"},"region_id":"DP00591r010","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00591r011","validated":{"curator_id":"fquaglia","timestamp":"2020-12-15T19:34:14.352Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":1706,"term_id":"IDPO:0000002","start":1006,"version":2,"statement":[{"text":"As shown in Fig. 5A, holo-RD eluted at a retention volume (RV) of 13.8 ml. This RV value was close to that expected for a globular protein of 73 kDa (RV ∼15 ml). In marked contrast, apo-RD eluted at a retention volume of 10.4 ml, a value corresponding to a globular protein of ∼600 kDa. In both cases, the molecular mass determined on-line by static light scattering corresponded to that of the monomeric RD protein (Fig. 5B and Table 1). Hence, the low retention volume of apo-RD was not due to oligomerization.","type":"Results"},{"text":"Here, we have characterized the structural and hydrodynamic properties of the RTX Repeat Domain (RD) of the CyaA toxin from Bordetella pertussis. This 701-amino acid long domain contains about 40 RTX motifs. We showed that, in the absence of calcium, RD was natively disordered, weakly stable, and highly hydrated.","type":"Abstract"}],"term_name":"disorder","ec_name":"dynamic light scattering assay evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"19015266","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0007064","curator_id":"bmesza","reference_html":"RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion. <i> Chenal A, Guijarro JI, Raynal B, Delepierre M, Ladant D. </i> J Biol Chem, 2009","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00591r012","validated":{"curator_id":"fquaglia","timestamp":"2020-12-15T19:35:09.983Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":1706,"term_id":"IDPO:0000011","start":1006,"version":2,"statement":[{"text":"As shown in Fig. 5A, holo-RD eluted at a retention volume (RV) of 13.8 ml. This RV value was close to that expected for a globular protein of 73 kDa (RV ∼15 ml). In marked contrast, apo-RD eluted at a retention volume of 10.4 ml, a value corresponding to a globular protein of ∼600 kDa. In both cases, the molecular mass determined on-line by static light scattering corresponded to that of the monomeric RD protein (Fig. 5B and Table 1). Hence, the low retention volume of apo-RD was not due to oligomerization.","type":"Results"}],"term_name":"disorder to order","ec_name":"dynamic light scattering assay evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"19015266","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural transition","ec_id":"ECO:0007064","curator_id":"bmesza","reference_html":"RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion. <i> Chenal A, Guijarro JI, Raynal B, Delepierre M, Ladant D. </i> J Biol Chem, 2009","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00591r013","validated":{"curator_id":"fquaglia","timestamp":"2020-12-15T19:35:56.701Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":1706,"term_id":"GO:0005509","start":1006,"version":3,"statement":[{"text":"Upon addition of 2 mM calcium to apo-RD, secondary structures were formed, as revealed by the concomitant intensity decrease of the0-* band and the increase of the n-* band in the holo-RD spectrum, as previously reported (10, 26). The structures of holo-RD were readily denatured upon addition of 5MGdnHCl,leading to a spectrum similar to that of the apo-state.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"ChEBI","id":"29108","partner_end":null}],"term_name":"calcium ion binding","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"19015266","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006204","curator_id":"bmesza","reference_html":"RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion. <i> Chenal A, Guijarro JI, Raynal B, Delepierre M, Ladant D. </i> J Biol Chem, 2009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00591r016","validated":{"curator_id":"fquaglia","timestamp":"2020-12-15T19:35:49.068Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":1706,"term_id":"GO:0005509","start":1006,"version":3,"statement":[{"text":"The NMR spectrum of calcium-bound RD was drastically different. First, it exhibited an increase of the envelope of upfield-shifted Ha protons, providing direct evidence that holo-RD was more structured, with a-sheet content (calculated as above) of at least 30–35%. Second, the signals became very broad as expected for a compact protein of 72.6 kDa. The line broadening of the 1H spectrum reflected a major change in the dynamic behavior of the protein upon calcium binding.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"ChEBI","id":"29108","partner_end":null}],"term_name":"calcium ion binding","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"19015266","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"bmesza","reference_html":"RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion. <i> Chenal A, Guijarro JI, Raynal B, Delepierre M, Ladant D. </i> J Biol Chem, 2009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00591r017","validated":{"curator_id":"fquaglia","timestamp":"2020-12-15T19:35:45.502Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":1706,"term_id":"GO:0005509","start":1006,"version":3,"statement":[{"text":"As shown in Fig. 5A, holo-RD eluted at a retention volume (RV) of 13.8 ml. This RV value was close to that expected for a globular proteinof 73 kDa (RV ~15 ml).","type":"Results"},{"text":" Equilibrium AUC experiments confirmed that apo-RD and holo-RD had both a same molecular mass of 73 kDa (Table 1), while velocity AUC indicated that the two states displayed different sedimentation coefficients (values of 2.5 S and 4.5 S for the apo and holo states, respectively) resulting from distinct hydrodynamic properties. In agreement with these data, quasi-elastic light scattering (QELS) analysis showed that upon calcium binding, RD was strongly compacted with its hydrodynamic radius (RH) decreasing from about 7 nm to about 3 nm (Table 1).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"ChEBI","id":"29108","partner_end":null}],"term_name":"calcium ion binding","ec_name":"dynamic light scattering assay evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"19015266","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0007064","curator_id":"bmesza","reference_html":"RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion. <i> Chenal A, Guijarro JI, Raynal B, Delepierre M, Ladant D. </i> J Biol Chem, 2009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00591r020","validated":{"curator_id":"fquaglia","timestamp":"2020-12-15T19:35:40.183Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":1706,"term_id":"GO:0005509","start":1006,"version":3,"statement":[{"text":" Equilibrium AUC experiments confirmed that apo-RD and holo-RD had both a same molecular mass of 73 kDa (Table 1), while velocity AUC indicated that the two states displayed different sedimentation coefficients (values of 2.5 S and 4.5 S for the apo and holo states, respectively) resulting from distinct hydrodynamic properties. In agreement with these data, quasi-elastic light scattering (QELS) analysis showed that upon calcium binding, RD was strongly compacted with its hydrodynamic radius (RH) decreasing from about 7 nm to about 3 nm (Table 1).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"ChEBI","id":"29108","partner_end":null}],"term_name":"calcium ion binding","ec_name":"analytical ultracentrifugation evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"19015266","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006275","curator_id":"bmesza","reference_html":"RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion. <i> Chenal A, Guijarro JI, Raynal B, Delepierre M, Ladant D. </i> J Biol Chem, 2009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00591r021","validated":{"curator_id":"fquaglia","timestamp":"2020-12-15T19:35:34.665Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":1706,"term_id":"GO:0005509","start":1006,"version":3,"statement":[{"text":"Thermal-induced unfolding of RD was followed by intrinsic fluorescence of tryptophan at various calcium concentrations. The ratio of fluorescence intensities at 360 and 320 nm (rFI360/320) was used tofollow the unfolding of RD (Fig. 4A). The van’t Hoff free enthalpy (deltaHvH) and temperature of half-melting (Tm) were then determined. As shown in Fig. 4B, both Tm and deltaHvH increased with calcium concentrations to reach a plateau above 1.5–2 mM. We obtained similar results from thermal-induced denaturation of RD followed by far- and near-UV CD (data not shown). All together these data indicated that apo-RD was unstable, as expected for a disordered state, while holo-RD was strongly stabilized by calcium binding.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"ChEBI","id":"29108","partner_end":null}],"term_name":"calcium ion binding","ec_name":"fluorescence evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"19015266","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001249","curator_id":"bmesza","reference_html":"RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion. <i> Chenal A, Guijarro JI, Raynal B, Delepierre M, Ladant D. </i> J Biol Chem, 2009","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1009,"end":1681,"reference_id":"27058787","reference_source":"pmid","reference_html":"Calcium-Driven Folding of RTX Domain β-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts. <i> Bumba L, Masin J, Macek P, Wald T, Motlova L, Bibova I, Klimova N, Bednarova L, Veverka V, Kachala M, Svergun DI, Barinka C, Sebo P. </i> Mol Cell, 2016","date":"2025-06-05T09:19:07.169Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00591r023","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"3312","statements":[{"type":"Supplementary material","text":"Calcium titration experiments were performed by successive addition of CaCl2."}],"entry_name":"calcium dichloride"}],"statement":[{"text":" A prominent negative peak at 217 nm, corresponding to formation of the β-roll structures (Chenal et al., 2010), was indeed observed for the complete purified CyaA-RTX domain (residues 1,009 to 1,681 of CyaA), which underwent a characteristic Ca2+-induced transition from the intrinsically disordered to the folded state already at 2 mM Ca2+.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T15:20:12.608Z"}},{"start":1009,"end":1681,"reference_id":"27058787","reference_source":"pmid","reference_html":"Calcium-Driven Folding of RTX Domain β-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts. <i> Bumba L, Masin J, Macek P, Wald T, Motlova L, Bibova I, Klimova N, Bednarova L, Veverka V, Kachala M, Svergun DI, Barinka C, Sebo P. </i> Mol Cell, 2016","date":"2025-06-05T09:18:40.016Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00591r024","statement":[{"text":"A prominent negative peak at 217 nm, corresponding to formation of the β-roll structures (Chenal et al., 2010), was indeed observed for the complete purified CyaA-RTX domain (residues 1,009 to 1,681 of CyaA), which underwent a characteristic Ca2+-induced transition from the intrinsically disordered to the folded state already at 2 mM Ca2+.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T15:19:44.858Z"}},{"start":1529,"end":1681,"reference_id":"27058787","reference_source":"pmid","reference_html":"Calcium-Driven Folding of RTX Domain β-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts. <i> Bumba L, Masin J, Macek P, Wald T, Motlova L, Bibova I, Klimova N, Bednarova L, Veverka V, Kachala M, Svergun DI, Barinka C, Sebo P. </i> Mol Cell, 2016","date":"2025-06-05T09:18:13.522Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00591r025","statement":[{"text":"To decipher the folding pathway in a residue-specific manner, Ca2+-induced conformational changes of 15N-labeled CyaA1529-1681 were followed by NMR spectroscopy. In the absence of Ca2+, the 1H-15N HSQC spectrum of the CyaA1529-1681 yielded a characteristic narrow dispersion of amide resonances of a disordered protein that lacks regular conformation (Figure 2B).","type":"Results"},{"text":"Analysis of chemical shifts revealed that in the absence of Ca2+, the secondary structure formation propensities of individual residues were very low, revealing absence of regular structural elements in the apo form.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T15:19:44.682Z"}},{"start":1529,"end":1681,"reference_id":"27058787","reference_source":"pmid","reference_html":"Calcium-Driven Folding of RTX Domain β-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts. <i> Bumba L, Masin J, Macek P, Wald T, Motlova L, Bibova I, Klimova N, Bednarova L, Veverka V, Kachala M, Svergun DI, Barinka C, Sebo P. </i> Mol Cell, 2016","date":"2025-06-05T09:19:24.637Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00591r026","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":10000,"db":"ChEBI","id":"29108","statements":[{"type":"Supplementary material","text":"Coverage of sequence-specific resonance assignment of CyaA1529-1681 in the absence (left panel) and in the presence of 10 Ca2+/mol\nprotein (right panel)."},{"type":"Results","text":"The Ca2+-dependent folding of selected backbone amides was expressed as the relative intensities of the specific crosspeak in the HSQC spectra during calcium titration, where the maximal intensity of the peak was arbitrarily set to 1."}],"entry_name":"calcium(2+)"}],"statement":[{"text":"Upon exposure to Ca2+, these HSQC crosspeaks were replaced by distinct and well-dispersed resonances characteristic of folded proteins.","type":"Results"},{"text":"In contrast, the secondary structure propensities in the Ca2+-loaded CyaA1529-1681 revealed a series of short β strands and a C-terminal α helix (Figure S3; cf. X-ray structure in Figure 1D).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T15:19:48.761Z"}},{"start":1632,"end":1706,"reference_id":"27058787","reference_source":"pmid","reference_html":"Calcium-Driven Folding of RTX Domain β-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts. <i> Bumba L, Masin J, Macek P, Wald T, Motlova L, Bibova I, Klimova N, Bednarova L, Veverka V, Kachala M, Svergun DI, Barinka C, Sebo P. </i> Mol Cell, 2016","date":"2025-06-04T16:24:58.634Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0090729","term_name":"toxin activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Arg1632Arg1706del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP00591r027","statement":[{"text":"The truncated RTX domains were then assessed for the capacity to fold in the presence of Ca2+ ions into a functional structure that would mediate CyaA binding to the CR3 and enable AC toxin penetration into macrophages (El-Azami-El-Idrissi et al., 2003). At physiological Ca2+ concentration (2 mM), these toxin activities were progressively lost with removal of the last 27, 40, 53, or 75 residues of CyaA (Figure 1B).","type":"Results"}],"term_comment":"","term_def":"\"Interacting selectively with one or more biological molecules in another (target) organism, initiating pathogenesis (leading to an abnormal, generally detrimental state) in the target organism. The activity should refer to an evolved function of the active gene product, i.e. one that was selected for. Examples include the activity of botulinum toxin, and snake venom.\" [GOC:pt]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0358","entry_name":"J-774A.1"}]},{"start":1632,"end":1706,"reference_id":"27058787","reference_source":"pmid","reference_html":"Calcium-Driven Folding of RTX Domain β-Rolls Ratchets Translocation of RTX Proteins through Type I Secretion Ducts. <i> Bumba L, Masin J, Macek P, Wald T, Motlova L, Bibova I, Klimova N, Bednarova L, Veverka V, Kachala M, Svergun DI, Barinka C, Sebo P. </i> Mol Cell, 2016","date":"2025-06-04T16:24:44.014Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0046812","term_name":"host cell surface binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Arg1632Arg1706del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP00591r028","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0358","entry_name":"J-774A.1"}],"statement":[{"text":"The truncated RTX domains were then assessed for the capacity to fold in the presence of Ca2+ ions into a functional structure that would mediate CyaA binding to the CR3 and enable AC toxin penetration into macrophages (El-Azami-El-Idrissi et al., 2003). At physiological Ca2+ concentration (2 mM), these toxin activities were progressively lost with removal of the last 27, 40, 53, or 75 residues of CyaA (Figure 1B).","type":"Results"},{"text":"However, the cell-binding activities of CyaAΔC40 and CyaAΔC53, devoid of 40 or 53 C-terminal residues, were almost intact at 10 mM Ca2+","type":"Results"},{"text":"CyaA binding was assessed on J774A.1 cells exposed to 6 nM CyaA for 30 min at 4°C.","type":"Figure"}],"term_comment":"","term_def":"\"Binding to the surface of a host cell.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_J7QLC0","date":"2016-09-14T14:23:05.000Z","acc":"J7QLC0","name":"Bifunctional hemolysin/adenylate cyclase","length":1706,"organism":"Bordetella pertussis (strain ATCC 9797 / DSM 5571 / NCTC 10739 / 18323)","UniParc":"UPI00027AF79A","genes":[{"name":{"value":"cya"},"synonyms":[{"value":"cyaA"}],"olnNames":[{"value":"BN118_0468"}]}],"alphafold_very_low_content":0.36518171160609614,"disorder_content":0.41090269636576787,"disprot_consensus":{"full":[{"start":1006,"end":1706,"type":"T"}],"Structural state":[{"start":1006,"end":1706,"type":"D"}],"Structural transition":[{"start":1006,"end":1706,"type":"T"}],"Molecular function":[{"start":1006,"end":1706,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_P48539","sequence":"MSERQGAGATNGKDKTSGENDGQKKVQEEFDIDMDAPETERAAVAIQSQFRKFQKKKAGSQS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P48539","disprot_id":"DP00592","ncbi_taxon_id":9606,"regions_counter":4,"creator":"pwarholm","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":62,"region_id":"DP00592r001","released":"2022_03","ec_id":"ECO:0006198","reference_html":"PEP-19, an intrinsically disordered regulator of calmodulin signaling. <i> Kleerekoper QK, Putkey JA. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19106096","version":2,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":62,"term_name":"protein binding","start":1,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19106096","version":3,"reference_html":"PEP-19, an intrinsically disordered regulator of calmodulin signaling. <i> Kleerekoper QK, Putkey JA. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006198","region_id":"DP00592r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":62,"region_id":"DP00592r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"PEP-19, an intrinsically disordered regulator of calmodulin signaling. <i> Kleerekoper QK, Putkey JA. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19106096","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":62,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19106096","version":3,"reference_html":"PEP-19, an intrinsically disordered regulator of calmodulin signaling. <i> Kleerekoper QK, Putkey JA. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00592r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P48539","date":"2016-08-26T14:06:24.000Z","acc":"P48539","name":"Calmodulin regulator protein PCP4","length":62,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00001697DE","genes":[{"name":{"value":"PCP4","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8914602","url":"http://www.ncbi.nlm.nih.gov/pubmed/8914602","alternativeUrl":"https://europepmc.org/abstract/MED/8914602"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:8742","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8742"}}]},"synonyms":[{"value":"PEP19","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"21491429","url":"http://www.ncbi.nlm.nih.gov/pubmed/21491429","alternativeUrl":"https://europepmc.org/abstract/MED/21491429"}}]}]}],"alphafold_very_low_content":0.016129032258064516,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":62,"type":"D"}],"Structural state":[{"start":1,"end":62,"type":"D"}],"Molecular function":[{"start":1,"end":62,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00104","name":"Ligand-binding domain of nuclear hormone receptor","start":872,"end":1053},{"id":"PF00105","name":"Double treble clef zinc finger, C4 type","start":742,"end":811}],"gene3D":[{"start":835,"end":1073,"id":"1.10.565.10","name":"Retinoid X Receptor"},{"start":737,"end":834,"id":"3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A"}]},"uniref50":"UniRef50_P49869","sequence":"MMRDRLASLIVVKQEGGSNTSISHHQATAIKCEASLYTESSLFQEINNNSCYRQNLNAPTHQQSHTSHLQHAQQHQTHQQHPLLPPPLPTLPLIYPCRNLFPDGCDINHLACCSSSNSNSNCNSDSNSTSSSPGNSHFFANGNTCAAALTPAPPATEPRKIKPLGAGKLKVGKTDSNSDSNSNCDSRAAAAASTSATSATSATTLAATAAATAAAAEAGGAASAAAAAKISQVRLTNQATTSMLLLQPNSSFSSLSPFDNFSTQTASTTTTTSASAAGHHQHHNHLLHQQHHNQQQQQQQQQQQQQQQQQQQEHLQQQHQQQLVSPQQHLLKSETLLSHEEDQLISNLTDSSVVSHSELFSDLFFPSDSNNSLLSPTTSGYPDNPAEDLTSSIENLTKLTCLRDKRLSSIPEQQLSSEQEQQLCLLSLRSSSDPAIALHAQQQQQQQQQQQQQQQQHQQQQQHLQLQLISPIGGPLSCGSSLPSFQETYSLKYNSSSGSSPQQASSSSTAAPTPTDQVLTLKMDEDCFPPLSGGWSASPPAPSQLQQLHTLQSQAQMSHPNSSNNSSNNAGNSHNNSGGYNYHGHFNAINASANLSPSSSASSLYEYNGVSAADNFYGQQQQQQQQSYQQHNYNSHNGERYSLPTFPTISELAAATAAVEAAAAATVGGPPPVRRASLPVQRTVSPAGSTAQSPKLAKITLNQRHSHAHAHALQLNSAPNSAASSPASADLQAGRLLQAPSQLCAVCGDTAACQHYGVRTCEGCKGFFKRTVQKGSKYVCLADKNCPVDKRRRNRCQFCRFQKCLVVGMVKEVVRTDSLKGRRGRLPSKPKSPQESPPSPPISLITALVRSHVDTTPDPSCLDYSHYEEQSMSEADKVQQFYQLLTSSVDVIKQFAEKIPGYFDLLPEDQELLFQSASLELFVLRLAYRARIDDTKLIFCNGTVLHRTQCLRSFGEWLNDIMEFSRSLHNLEIDISAFACLCALTLITERHGLREPKKVEQLQMKIIGSLRDHVTYNAEAQKKQHYFSRLLGKLPELRSLSVQGLQRIFYLKLEDLVPAPALIENMFVTTLPF","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_P49869","disprot_id":"DP00594","ncbi_taxon_id":7227,"regions_counter":1,"creator":"pwarholm","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":753,"region_id":"DP00594r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"A new method of recording the elastic recovery of dental impression materials. <i> Jörgensen KD. </i> Scand J Dent Res, 1976","term_id":"IDPO:0000002","curator_id":"pwarholm","start":523,"term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"1064127","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P49869","date":"2016-09-08T14:17:22.000Z","acc":"P49869","name":"Probable nuclear hormone receptor HR38","length":1073,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI000016BB7F","genes":[{"name":{"value":"Hr38"},"synonyms":[{"value":"NR4A4"}],"orfNames":[{"value":"CG1864"}]}],"alphafold_very_low_content":0.6178937558247903,"disorder_content":0.21528424976700838,"disprot_consensus":{"full":[{"start":523,"end":753,"type":"D"}],"Structural state":[{"start":523,"end":753,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00573","name":"Ribosomal protein L4/L1 family","start":13,"end":198}],"gene3D":[{"start":1,"end":201,"id":"3.40.1370.10","name":"3.40.1370.10"}]},"uniref50":"UniRef50_P49226","sequence":"MELVLKDAQSALTVSETTFGRDFNEALVHQVVVAYAAGARQGTRAQKTRAEVTGSGKKPWRQKGTGRARSGSIKSPIWRSGGVTFAARPQDHSQKVNKKMYRGALKSILSELVRQDRLIVVEKFSVEAPKTKLLAQKLKDMALEDVLIITGELDENLFLAARNLHKVDVRDATGIDPVSLIAFDKVVMTADAVKQVEEMLA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P49226","disprot_id":"DP00600","ncbi_taxon_id":83333,"regions_counter":6,"creator":"pwarholm","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":103,"region_id":"DP00600r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The role of disordered ribosomal protein extensions in the early steps of eubacterial 50 S ribosomal subunit assembly. <i> Timsit Y, Acosta Z, Allemand F, Chiaruttini C, Springer M. </i> Int J Mol Sci, 2009","term_id":"IDPO:0000002","curator_id":"pwarholm","start":45,"term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"19399222","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1DMG:A"}],"term_name":"disorder","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":103,"term_name":"molecular function regulator","start":45,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"GO","curator_name":"Per Warholm","reference_id":"19399222","version":3,"reference_html":"The role of disordered ribosomal protein extensions in the early steps of eubacterial 50 S ribosomal subunit assembly. <i> Timsit Y, Acosta Z, Allemand F, Chiaruttini C, Springer M. </i> Int J Mol Sci, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006220","region_id":"DP00600r002","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":103,"term_name":"DNA binding","start":45,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"GO","curator_name":"Per Warholm","reference_id":"19399222","version":3,"reference_html":"The role of disordered ribosomal protein extensions in the early steps of eubacterial 50 S ribosomal subunit assembly. <i> Timsit Y, Acosta Z, Allemand F, Chiaruttini C, Springer M. </i> Int J Mol Sci, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003677","ec_id":"ECO:0006220","region_id":"DP00600r003","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":96,"region_id":"DP00600r004","released":"2022_03","ec_id":"ECO:0006204","reference_html":"[Expression of glucocorticoid receptors and blast cell clearance in children with different variants of acute lymphoblastic leukemia]. <i> Torubarova NA, Kopyl'tsova EA, Koshel' IV, Poliakova OA, Maiakova SA. </i> Gematol Transfuziol, 1992","term_id":"IDPO:0000002","curator_id":"pwarholm","start":41,"term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"1618378","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1DMG:A"}],"term_name":"disorder","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":96,"term_name":"molecular function regulator","start":41,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"GO","curator_name":"Per Warholm","reference_id":"1618378","version":3,"reference_html":"[Expression of glucocorticoid receptors and blast cell clearance in children with different variants of acute lymphoblastic leukemia]. <i> Torubarova NA, Kopyl'tsova EA, Koshel' IV, Poliakova OA, Maiakova SA. </i> Gematol Transfuziol, 1992","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006204","region_id":"DP00600r005","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":96,"term_name":"DNA binding","start":41,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"GO","curator_name":"Per Warholm","reference_id":"1618378","version":3,"reference_html":"[Expression of glucocorticoid receptors and blast cell clearance in children with different variants of acute lymphoblastic leukemia]. <i> Torubarova NA, Kopyl'tsova EA, Koshel' IV, Poliakova OA, Maiakova SA. </i> Gematol Transfuziol, 1992","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003677","ec_id":"ECO:0006204","region_id":"DP00600r006","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_A8AQL8","date":"2016-09-08T15:04:37.000Z","acc":"P60723","name":"50S ribosomal protein L4","length":201,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI000003EAE6","genes":[{"name":{"value":"rplD"},"synonyms":[{"value":"eryA"}],"olnNames":[{"value":"b3319"},{"value":"JW3281"}]}],"alphafold_very_low_content":0,"disorder_content":0.31343283582089554,"disprot_consensus":{"full":[{"start":41,"end":103,"type":"D"}],"Structural state":[{"start":41,"end":103,"type":"D"}],"Molecular function":[{"start":41,"end":103,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00400","name":"WD domain, G-beta repeat","start":506,"end":544},{"id":"PF11540","name":"Cytoplasmic dynein 1 intermediate chain 2","start":105,"end":135}],"gene3D":[{"start":300,"end":452,"id":"2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"},{"start":453,"end":656,"id":"2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"}]},"uniref50":"UniRef50_Q24246","sequence":"MDRKAELERKKAKLAALREEKDRRRREKEIKDMEEAAGRIGGGAGIDKDQRKDLDEMLSSLGVAPVSEVLSSLSSVNSMTSDNSNTQTPDASLQATVNGQSGGKKQPLNLSVYNVQATNIPPKETLVYTKQTQTTSTGGGNGDVLSCHSSPLSGYMEDWWRPRKAHATDYYDEYNLNPGLEWEDEFTDDEESSLQNLGNGFTSKLPPGYLTHGLPTVKDVAPAITPLEIKKETEVKKEVNELSEEQKQMIILSENFQRFVVRAGRVIERALSENVDIYTDYIGGGDSEEANDERSHARLSLNRVFYDERWSKNRCITSMDWSTHFPELVVGSYHNNEESPNEPDGVVMVWNTKFKKSTPEDVFHCQSAVMSTCFAKFNPNLILGGTYSGQIVLWDNRVQKRTPIQRTPLSAAAHTHPVYCLQMVGTQNAHNVISISSDGKLCSWSLDMLSQPQDTLELQQRQSKAIAITSMAFPANEINSLVMGSEDGYVYSASRHGLRSGVNEVYERHLGPITGISTHYNQLSPDFGHLFLTSSIDWTIKLWSLKDTKPLYSFEDNSDYVMDVAWSPVHPALFAAVDGSGRLDLWNLNQDTEVPTASIVVAGAPALNRVSWTPSGLHVCIGDEAGKLYVYDVAENLAQPSRDEWSRFNTHLSEIKMNQSDEV","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_Q24246","disprot_id":"DP00605","ncbi_taxon_id":7227,"regions_counter":11,"creator":"zskalman","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":135,"region_id":"DP00605r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Multivalency in the assembly of intrinsically disordered Dynein intermediate chain. <i> Hall J, Karplus PA, Barbar E. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"pwarholm","start":109,"term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"19759397","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3FM7:C"}],"term_name":"disorder","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":135,"term_name":"molecular adaptor activity","start":109,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"GO","curator_name":"Per Warholm","reference_id":"19759397","version":3,"reference_html":"Multivalency in the assembly of intrinsically disordered Dynein intermediate chain. <i> Hall J, Karplus PA, Barbar E. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006220","region_id":"DP00605r002","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":135,"term_name":"disorder to order","start":109,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"19759397","version":2,"reference_html":"Multivalency in the assembly of intrinsically disordered Dynein intermediate chain. <i> Hall J, Karplus PA, Barbar E. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00605r003","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":135,"term_name":"protein binding","start":109,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"GO","curator_name":"Per Warholm","reference_id":"19759397","version":3,"reference_html":"Multivalency in the assembly of intrinsically disordered Dynein intermediate chain. <i> Hall J, Karplus PA, Barbar E. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00605r004","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":135,"region_id":"DP00605r005","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Multivalency in the assembly of intrinsically disordered Dynein intermediate chain. <i> Hall J, Karplus PA, Barbar E. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"pwarholm","start":109,"term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"19759397","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3FM7:C"}],"term_name":"disorder","curator_orcid":"0000-0002-2242-7721","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":135,"term_name":"molecular adaptor activity","start":109,"ec_name":"cleavage assay evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"GO","curator_name":"Per Warholm","reference_id":"19759397","version":3,"reference_html":"Multivalency in the assembly of intrinsically disordered Dynein intermediate chain. <i> Hall J, Karplus PA, Barbar E. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0007691","region_id":"DP00605r006","curator_orcid":"0000-0002-2242-7721","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":135,"term_name":"disorder to order","start":109,"ec_name":"cleavage assay evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"19759397","version":2,"reference_html":"Multivalency in the assembly of intrinsically disordered Dynein intermediate chain. <i> Hall J, Karplus PA, Barbar E. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0007691","region_id":"DP00605r007","curator_orcid":"0000-0002-2242-7721","ec_go":"IDA","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":135,"term_name":"protein binding","start":109,"ec_name":"cleavage assay evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"GO","curator_name":"Per Warholm","reference_id":"19759397","version":3,"reference_html":"Multivalency in the assembly of intrinsically disordered Dynein intermediate chain. <i> Hall J, Karplus PA, Barbar E. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007691","region_id":"DP00605r008","curator_orcid":"0000-0002-2242-7721","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":289,"reference_id":"15581372","reference_source":"pmid","reference_html":"The intermediate chain of cytoplasmic dynein is partially disordered and gains structure upon binding to light-chain LC8. <i> Nyarko A, Hare M, Hays TS, Barbar E. </i> Biochemistry, 2004","date":"2024-05-07T16:28:33.731Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP00605r009","statement":[{"text":"CD, fluorescence, and sedimentation velocity demonstrate\nthat IC1-289 is disordered at physiological temperature and\npH, but upon addition of LC8, it gains CD-detected secondary\nstructure and becomes more resistant to proteolysis (27,\n37).","type":"Discussion"}],"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7.8}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:55:43.792Z"}},{"start":1,"end":30,"reference_id":"15581372","reference_source":"pmid","reference_html":"The intermediate chain of cytoplasmic dynein is partially disordered and gains structure upon binding to light-chain LC8. <i> Nyarko A, Hare M, Hays TS, Barbar E. </i> Biochemistry, 2004","date":"2024-05-07T16:32:24.563Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP00605r010","statement":[{"text":"CD spectra of IC1-143 are consistent with residues\n1-30 being helical, while CD spectra of IC114-260 show no\nevidence of a folded structure (Figure 5), indicating that\nresidues 209-250 are unable to form a helix or a coiled-coil\non their own.","type":"Discussion"},{"text":"This suggests\nthat, while free IC1-289 is unfolded in its native state, it has\na short segment with a propensity for helix formation, which\nis triggered with addition of either LC8 or TMAO.","type":"Discussion"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q24117"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1145"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:55:51.158Z"}},{"start":114,"end":260,"reference_id":"15581372","reference_source":"pmid","reference_html":"The intermediate chain of cytoplasmic dynein is partially disordered and gains structure upon binding to light-chain LC8. <i> Nyarko A, Hare M, Hays TS, Barbar E. </i> Biochemistry, 2004","date":"2024-05-07T16:34:12.333Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007688","ec_ontology":"ECO","ec_name":"gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"Q24117","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00605r011","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q24117"}],"statement":[{"text":"To determine the stoichiometry of binding, a constant\nconcentration of IC114-260 was incubated with increasing\nconcentrations of LC8 and the formation of the complex was\nvisualized using native gel electrophoresis.","type":"Discussion"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:55:54.108Z"}}],"released":"2016_10","uniref100":"UniRef100_Q24246","date":"2016-09-08T15:27:24.000Z","acc":"Q24246","name":"Cytoplasmic dynein 1 intermediate chain","length":663,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI000016BAE0","genes":[{"name":{"value":"sw"},"synonyms":[{"value":"Cdic"},{"value":"Dic19B"}],"orfNames":[{"value":"CG18000"}]}],"alphafold_very_low_content":0.22473604826546004,"disorder_content":0.4358974358974359,"disprot_consensus":{"full":[{"start":1,"end":30,"type":"T"},{"start":31,"end":108,"type":"D"},{"start":109,"end":135,"type":"T"},{"start":136,"end":289,"type":"D"}],"Structural state":[{"start":1,"end":289,"type":"D"}],"Molecular function":[{"start":109,"end":260,"type":"F"}],"Structural transition":[{"start":1,"end":30,"type":"T"},{"start":109,"end":135,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00257","name":"Dehydrin","start":186,"end":245}]},"uniref50":"UniRef50_P42759","sequence":"MAEEYKNTVPEQETPKVATEESSAPEIKERGMFDFLKKKEEVKPQETTTLASEFEHKTQISEPESFVAKHEEEEHKPTLLEQLHQKHEEEEENKPSLLDKLHRSNSSSSSSSDEEGEDGEKKKKEKKKKIVEGDHVKTVEEENQGVMDRIKEKFPLGEKPGGDDVPVVTTMPAPHSVEDHKPEEEEKKGFMDKIKEKLPGHSKKPEDSQVVNTTPLVETATPIADIPEEKKGFMDKIKEKLPGYHAKTTGEEEKKEKVSD","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_P42759","disprot_id":"DP00606","ncbi_taxon_id":3702,"regions_counter":18,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":260,"region_id":"DP00606r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. <i> Kovacs D, Kalmar E, Torok Z, Tompa P. </i> Plant Physiol, 2008","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18359842","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The 1H-NMR spectra of ERD10 and ERD14 (Fig. 3A; only ERD10 is shown) also suggest their disordered nature, because the chemical shift dispersion is narrower than is typical for globular proteins. For globular proteins, 1H chemical shifts usually spread out in the region 9.5 to 6.0 ppm, whereas for IDPs, they are usually confined in the region 8.0 to 8.5 ppm (Dyson and Wright, 2004).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-14T09:51:55.026Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":260,"region_id":"DP00606r003","released":"2022_03","ec_id":"ECO:0007689","reference_html":"Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. <i> Kovacs D, Kalmar E, Torok Z, Tompa P. </i> Plant Physiol, 2008","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18359842","version":3,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In SDS-PAGE, they show a characteristic low mobility: the real molecular mass of ERD10 is 29 kD but it runs at 45 kD, whereas the real molecular mass of ERD14 is 20 kD but it runs at 37 kD (Fig. 2A). This high apparent molecular mass caused by a highly hydrophilic character is often diagnostic of IDPs (Tompa, 2002). In addition, both proteins are heat stable (Fig. 2B) and are very sensitive to proteases (Fig. 2A).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-14T09:51:43.281Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":260,"region_id":"DP00606r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. <i> Kovacs D, Kalmar E, Torok Z, Tompa P. </i> Plant Physiol, 2008","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18359842","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The CD spectra of ERD10 and ERD14 with a minimum close to 200 nm (Fig. 3B) are also typical of disordered proteins, because regular secondary structural elements, such as the α-helix and the β-sheet, in globular proteins give characteristic spectral peaks at 208, 222, and 214 nm, whereas a large negative peak at approximately 200 nm is characteristic of the coil conformation that dominates in IDPs (Receveur-Brechot et al., 2005).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-14T09:51:38.018Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":260,"reference_id":"28275980","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>15</sup>N, <sup>13</sup>C resonance assignment of plant dehydrin early response to dehydration 10 (ERD10). <i> Cedeño C, Żerko S, Tompa P, Koźmiński W. </i> Biomol NMR Assign, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00606r007","statement":[{"text":"Narrow peak dispersion in the 1H dimension of the 1H-15N HSQC indicates that ERD10 is an intrinsically disordered protein (Fig. 1).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-14T09:51:18.209Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":260,"reference_id":"18359842","reference_source":"pmid","reference_html":"Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. <i> Kovacs D, Kalmar E, Torok Z, Tompa P. </i> Plant Physiol, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00606r008","statement":[{"text":"In SDS-PAGE, they show a characteristic low mobility: the real molecular mass of ERD10 is 29 kD but it runs at 45 kD, whereas the real molecular mass of ERD14 is 20 kD but it runs at 37 kD (Fig. 2A). This high apparent molecular mass caused by a highly hydrophilic character is often diagnostic of IDPs (Tompa, 2002). In addition, both proteins are heat stable (Fig. 2B) and are very sensitive to proteases (Fig. 2A).","type":"Results"},{"text":"The polypeptide chain of IDPs is more accessible to proteases than that of globular proteins, which results in much higher protease sensitivity, and this is diagnostic for their open structures. This was tested with proteases of broad substrate specificity (subtilisin and proteinase K) and proteases of narrow substrate specificity (trypsin and chymotrypsin); the pattern of the digestion was similar for all proteases, so we show only the results of proteinase K (Fig. 2A). ERD10 and ERD14 do not show any ordered motifs, which would show resistance against proteolysis.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-14T09:51:14.500Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":1,"end":260,"reference_id":"18359842","reference_source":"pmid","reference_html":"Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. <i> Kovacs D, Kalmar E, Torok Z, Tompa P. </i> Plant Physiol, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000269","ec_ontology":"ECO","ec_name":"experimental evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00606r009","statement":[{"text":"Liposome binding suggested a possible effect of ERD10 and ERD14 on membrane fluidity. This was analyzed by fluorescence anisotropy measurements, which showed no effect of ERD10 or ERD14 on phosphatidylcholine (PC):PS (1:1) vesicles (Fig. 9).","type":"Results"},{"text":"Our results show that these intrinsically disordered proteins have chaperone activity of rather wide substrate specificity and that they interact with phospholipid vesicles through electrostatic forces.","type":"Abstract"},{"text":"Another putative mechanism of the protective function of ERD10 and ERD14 is membrane binding and stabilization. We could address this cryoprotective effect by analyzing their binding of PLVs and their effects on membrane fluidity. Generally, the fluorescence anisotropy is characteristic of the movement rate of the fluorescent dye in the phospholipid layer, which showed no difference in the presence or absence of ERD10 and ERD14.","type":"Discussion"},{"text":"This result suggests that the interaction is electrostatic, affecting membranes only peripherally, via phospholipid head groups.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-14T09:52:13.388Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":260,"reference_id":"18359842","reference_source":"pmid","reference_html":"Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. <i> Kovacs D, Kalmar E, Torok Z, Tompa P. </i> Plant Physiol, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00606r010","statement":[{"text":"The interaction of ERD10 and ERD14 with phospholipid vesicles (PLVs) was analyzed with mini gel filtration columns, as described in “Materials and Methods.” The analysis and comparison with the behavior of a positive control, calpain domain III, which shows calcium-dependent phospholipid binding, and a negative control, BSA, which does not bind to vesicles either in the absence or the presence of calcium (Tompa et al., 2001), confirm that ERD10 and ERD14 bind to PLVs. The interaction was statistically significant, as suggested by Student's t test (P = 0.003 and 0.056 for ERD10 and ERD14, respectively). Under the given conditions, approximately 2 μg of ERD10 and 2.5 μg of ERD14 were bound to 25 μg of PLVs, out of 15 μg total (Fig. 8A).Liposome binding suggested a possible effect of ERD10 and ERD14 on membrane fluidity. This was analyzed by fluorescence anisotropy measurements, which showed no effect of ERD10 or ERD14 on phosphatidylcholine (PC):PS (1:1) vesicles (Fig. 9).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-14T09:52:04.082Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":260,"reference_id":"18359842","reference_source":"pmid","reference_html":"Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. <i> Kovacs D, Kalmar E, Torok Z, Tompa P. </i> Plant Physiol, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0044183","term_name":"protein folding chaperone","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006319","ec_ontology":"ECO","ec_name":"cell aggregation evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00606r011","statement":[{"text":"Here, citrate synthase was incubated at an elevated temperature and aggregation was followed by an increase in absorbance. ERD10 and ERD14 at an equimolar concentration showed significant protective activity (Fig. 5), slowing the rate of aggregation to about half of its control value; this effect was significantly higher than that of BSA but fell short of that of HSP90. Upon increasing ERD10 and ERD14 concentrations further, the protective effect did not change much and did not reach the efficiency of HSP90 (Table I).","type":"Results"},{"text":"Both ERD10 and ERD14 showed significant protective effects on the thermal aggregation of firefly luciferase at a 2× molar excess (Fig. 6). Under these conditions, aggregation was almost completely inhibited, similar to the effect of HSP90 (Table I). BSA was practically ineffective in this assay.","type":"Results"},{"text":"ERD10, ERD14, and HSP90 had similar protective effects on the enzyme activity of lysozyme at substoichiometric ratios of lysozyme:chaperone (7:1; Fig. 7; Table I). Although the time course of the loss of enzyme activity was somewhat different in the presence of ERD10, ERD14, and HSP90, their protective effects, as expressed by residual enzyme activity after 25 min of incubation, were commensurate. BSA, again, had a negligible effect.","type":"Results"},{"text":"To investigate these functions of ERD10 and ERD14, we studied their protective effects on the heat-induced loss of enzyme activity and/or aggregation of four different substrates. The selected assays represent different modes and mechanisms of possible chaperone action and included thermal inactivation of ADH, thermal aggregation of firefly luciferase and citrate synthase, and the chemically induced inactivation of lysozyme. In the analyses shown here, ERD10 and ERD14 demonstrated marked effects on the prevention of aggregation/deactivation of protein substrates.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-14T09:52:17.880Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":260,"reference_id":"20054552","reference_source":"pmid","reference_html":"Physiological roles of ERD10 in abiotic stresses and seed germination of Arabidopsis. <i> Kim SY, Nam KH. </i> Plant Cell Rep, 2010","date":"2025-10-14T18:22:16.531Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0009631","term_name":"cold acclimation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006049","ec_ontology":"ECO","ec_name":"genetic transformation evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":4,"statements":[{"type":"Results","text":"We treated the erd10 mutant and wild-type plants with cold by placing them at 4°C for 24 h."}]}],"ec_go":"IMP","region_id":"DP00606r014","statement":[{"text":" In an alternative approach to detect the function of ERD10, we analyzed the T-DNA insertion knock-out line for ERD10. The T-DNA insertion site was 300 base pairs upstream from the annotated first methionine codon of the ERD10 gene. ","type":"Results"},{"text":"As shown in Fig. 2c, about 40% of the wild-type leaves were damaged by cold treatment. In comparison, 70% of the erd10 mutant leaves showed damage, a much higher rate than that observed for wild-type plants.","type":"Results"}],"term_comment":"","term_def":"\"Any process that increases freezing tolerance of an organism in response to low, nonfreezing temperatures.\" [GOC:syr]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":260,"reference_id":"20054552","reference_source":"pmid","reference_html":"Physiological roles of ERD10 in abiotic stresses and seed germination of Arabidopsis. <i> Kim SY, Nam KH. </i> Plant Cell Rep, 2010","date":"2025-10-14T18:24:31.572Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0009409","term_name":"response to cold","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001808","ec_ontology":"ECO","ec_name":"reverse transcription polymerase chain reaction evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":4,"statements":[{"type":"Results","text":"We treated the erd10 mutant and wild-type plants with cold by placing them at 4°C for 24 h."}]}],"ec_go":"EXP","region_id":"DP00606r015","statement":[{"text":"As expected, activation of the CBF/DREB1 genes by cold stress was remarkable in wild-type plants, while basal expressions levels of these genes were barely detectable in the absence of cold. In contrast, cold inducibility of any of these genes was not distinguishable in the erd10 mutant. ","type":"Results"},{"text":"These results, combined with the result in Fig. 1c showing that the expression of ERD10 dramatically increased by cold treatment, imply that ERD10 is required to activate the CBF/DREB1 genes and their downstream target genes in response to cold stress in Arabidopsis.","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cold stimulus, a temperature stimulus below the optimal temperature for that organism.\" [GOC:lr]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":260,"reference_id":"20054552","reference_source":"pmid","reference_html":"Physiological roles of ERD10 in abiotic stresses and seed germination of Arabidopsis. <i> Kim SY, Nam KH. </i> Plant Cell Rep, 2010","date":"2025-10-14T18:32:19.454Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0009819","term_name":"drought recovery","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006049","ec_ontology":"ECO","ec_name":"genetic transformation evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"IMP","region_id":"DP00606r016","statement":[{"text":"In addition, the erd10 mutant showed reduced tolerance to drought stress relative to wild-type plants. While about 10% of wild-type plants dehydrated for 12 days turned green again after re-watering, erd10 mutants barely recovered from the same stress.","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of prolonged deprivation of water that restores that organism to a normal (non-stressed) condition.\" [GOC:lr]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":260,"reference_id":"20054552","reference_source":"pmid","reference_html":"Physiological roles of ERD10 in abiotic stresses and seed germination of Arabidopsis. <i> Kim SY, Nam KH. </i> Plant Cell Rep, 2010","date":"2025-10-14T18:36:21.539Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:2000034","term_name":"regulation of seed maturation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006049","ec_ontology":"ECO","ec_name":"genetic transformation evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"IMP","region_id":"DP00606r017","statement":[{"text":"However, seed germination itself was affected by the lack of ERD10. The germination rate of the erd10 mutant over 5 days after imbibition was lower than that of wild-type plant (Fig. 4a). More than 80% of wild-type seeds germinated within 2 days. However, only 25 and 45% of erd10 seeds had germinated at 2 and 3 days after imbibitions, respectively.","type":"Results"},{"text":"Compared to wild-type seeds, erd10 seeds are a little smaller, and the groove that is formed between the two folded-cotyledons and the radicle is not distinct in erd10 seeds (Fig. 4c). These results suggest that the accumulation of ERD10 over time is required for seed maturation and germination in Arabidopsis.","type":"Results"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of seed maturation.\" [GOC:obol]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":260,"reference_id":"20054552","reference_source":"pmid","reference_html":"Physiological roles of ERD10 in abiotic stresses and seed germination of Arabidopsis. <i> Kim SY, Nam KH. </i> Plant Cell Rep, 2010","date":"2025-10-14T18:36:00.238Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0010029","term_name":"regulation of seed germination","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006049","ec_ontology":"ECO","ec_name":"genetic transformation evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"IMP","region_id":"DP00606r018","statement":[{"text":"However, seed germination itself was affected by the lack of ERD10. The germination rate of the erd10 mutant over 5 days after imbibition was lower than that of wild-type plant (Fig. 4a). More than 80% of wild-type seeds germinated within 2 days. However, only 25 and 45% of erd10 seeds had germinated at 2 and 3 days after imbibitions, respectively.","type":"Results"},{"text":"Compared to wild-type seeds, erd10 seeds are a little smaller, and the groove that is formed between the two folded-cotyledons and the radicle is not distinct in erd10 seeds (Fig. 4c). These results suggest that the accumulation of ERD10 over time is required for seed maturation and germination in Arabidopsis.","type":"Results"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of seed germination.\" [GOC:sm]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_P42759","date":"2016-08-16T17:20:13.000Z","acc":"P42759","name":"Dehydrin ERD10","length":260,"organism":"Arabidopsis thaliana","dataset":["Stress response proteins"],"UniParc":"UPI00000014F7","genes":[{"name":{"value":"ERD10"},"synonyms":[{"value":"LTI29"},{"value":"LTI45"}],"orfNames":[{"value":"F5M15.21"},{"value":"F5M15_20"}],"olnNames":[{"value":"At1g20450"}]}],"alphafold_very_low_content":0.36153846153846153,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":260,"type":"D"}],"Structural state":[{"start":1,"end":260,"type":"D"}],"Molecular function":[{"start":1,"end":260,"type":"F"}],"Biological process":[{"start":1,"end":260,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01491","name":"Frataxin-like domain","start":89,"end":195}],"gene3D":[{"start":82,"end":210,"id":"3.30.920.10","name":"Frataxin/CyaY"}]},"uniref50":"UniRef50_Q16595","sequence":"MWTLGRRAVAGLLASPSPAQAQTLTRVPRPAELAPLCGRRGLRTDIDATCTPRRASSNQRGLNQIWNVKKQSVYLMNLRKSGTLGHPGSLDETTYERLAEETLDSLAEFFEDLADKPYTFEDYDVSFGSGVLTVKLGGDLGTYVINKQTPNKQIWLSSPSSGPKRYDWTGKNWVYSHDGVSLHELLAAELTKALKTKLDLSSLAYSGKDA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q16595","disprot_id":"DP00607","ncbi_taxon_id":9606,"regions_counter":10,"creator":"agasparini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":92,"region_id":"DP00607r007","released":"2022_12","ec_id":"ECO:0006165","reference_html":"The N-terminus of mature human frataxin is intrinsically unfolded. <i> Prischi F, Giannini C, Adinolfi S, Pastore A. </i> FEBS J, 2009","term_id":"IDPO:0000002","curator_id":"vnugnes","start":81,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19843162","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-08-22T15:09:32.999Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Analysis of the secondary chemical shifts using chemical shift indices [23] supports the hypothesis of am absence of secondary structure in the region 81-92 (Fig. 3A).","type":"Results"}]},{"start":61,"end":74,"reference_id":"19843162","reference_source":"pmid","reference_html":"The N-terminus of mature human frataxin is intrinsically unfolded. <i> Prischi F, Giannini C, Adinolfi S, Pastore A. </i> FEBS J, 2009","date":"2022-08-22T15:12:03.781Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00607r010","statement":[{"text":" The second spans residues 61-210 [hfra(61-210)]. As described previously [11], unless otherwise protected, this construct degrades spontaneously to produce a fragment comprising residues 75-210 [hfra(75-210)]. However, we found that use of the Complete anti-protease cocktail (Roche) prevents proteolytic cleavage.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_Q16595","date":"2016-08-22T09:44:24.000Z","acc":"Q16595","name":"Frataxin, mitochondrial","length":210,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000014E756","genes":[{"name":{"value":"FXN"},"synonyms":[{"value":"FRDA"},{"value":"X25"}]}],"alphafold_very_low_content":0.2,"disorder_content":0.12380952380952381,"disprot_consensus":{"full":[{"start":61,"end":74,"type":"D"},{"start":81,"end":92,"type":"D"}],"Structural state":[{"start":61,"end":74,"type":"D"},{"start":81,"end":92,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02731","name":"SKIP/SNW domain","start":175,"end":335}]},"uniref50":"UniRef50_Q13573","sequence":"MALTSFLPAPTQLSQDQLEAEEKARSQRSRQTSLVSSRREPPPYGYRKGWIPRLLEDFGDGGAFPEIHVAQYPLDMGRKKKMSNALAIQVDSEGKIKYDAIARQGQSKDKVIYSKYTDLVPKEVMNADDPDLQRPDEEAIKEITEKTRVALEKSVSQKVAAAMPVRAADKLAPAQYIRYTPSQQGVAFNSGAKQRVIRMVEMQKDPMEPPRFKINKKIPRGPPSPPAPVMHSPSRKMTVKEQQEWKIPPCISNWKNAKGYTIPLDKRLAADGRGLQTVHINENFAKLAEALYIADRKAREAVEMRAQVERKMAQKEKEKHEEKLREMAQKARERRAGIKTHVEKEDGEARERDEIRHDRRKERQHDRNLSRAAPDKRSKLQRNENRDISEVIALGVPNPRTSNEVQYDQRLFNQSKGMDSGFAGGEDEIYNVYDQAWRGGKDMAQSIYRPSKNLDKDMYGDDLEARIKTNRFVPDKEFSGSDRRQRGREGPVQFEEDPFGLDKFLEEAKQHGGSKRPSDSSRPKEHEHEGKKRRKE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q13573","disprot_id":"DP00608","ncbi_taxon_id":9606,"regions_counter":16,"creator":"pwarholm","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":129,"region_id":"DP00608r001","released":"2022_03","ec_id":"ECO:0006198","reference_html":"A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR. <i> Wang X, Zhang S, Zhang J, Huang X, Xu C, Wang W, Liu Z, Wu J, Shi Y. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"fquaglia","start":59,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20007319","version":2,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":129,"term_name":"molecular function regulator","start":59,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"20007319","version":3,"reference_html":"A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR. <i> Wang X, Zhang S, Zhang J, Huang X, Xu C, Wang W, Liu Z, Wu J, Shi Y. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006198","region_id":"DP00608r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":129,"term_name":"disorder to order","start":59,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20007319","version":2,"reference_html":"A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR. <i> Wang X, Zhang S, Zhang J, Huang X, Xu C, Wang W, Liu Z, Wu J, Shi Y. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006198","region_id":"DP00608r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":129,"term_name":"protein binding","start":59,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"20007319","version":3,"reference_html":"A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR. <i> Wang X, Zhang S, Zhang J, Huang X, Xu C, Wang W, Liu Z, Wu J, Shi Y. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006198","region_id":"DP00608r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":129,"region_id":"DP00608r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR. <i> Wang X, Zhang S, Zhang J, Huang X, Xu C, Wang W, Liu Z, Wu J, Shi Y. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"fquaglia","start":59,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20007319","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":129,"term_name":"molecular function regulator","start":59,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"20007319","version":3,"reference_html":"A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR. <i> Wang X, Zhang S, Zhang J, Huang X, Xu C, Wang W, Liu Z, Wu J, Shi Y. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006204","region_id":"DP00608r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":129,"term_name":"disorder to order","start":59,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20007319","version":2,"reference_html":"A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR. <i> Wang X, Zhang S, Zhang J, Huang X, Xu C, Wang W, Liu Z, Wu J, Shi Y. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00608r007","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":129,"term_name":"protein binding","start":59,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"20007319","version":3,"reference_html":"A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR. <i> Wang X, Zhang S, Zhang J, Huang X, Xu C, Wang W, Liu Z, Wu J, Shi Y. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00608r008","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":129,"region_id":"DP00608r009","released":"2022_03","ec_id":"ECO:0006206","reference_html":"A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR. <i> Wang X, Zhang S, Zhang J, Huang X, Xu C, Wang W, Liu Z, Wu J, Shi Y. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"fquaglia","start":59,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20007319","version":2,"ec_name":"near-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":129,"term_name":"molecular function regulator","start":59,"ec_name":"near-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"20007319","version":3,"reference_html":"A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR. <i> Wang X, Zhang S, Zhang J, Huang X, Xu C, Wang W, Liu Z, Wu J, Shi Y. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006206","region_id":"DP00608r010","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":129,"term_name":"disorder to order","start":59,"ec_name":"near-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20007319","version":2,"reference_html":"A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR. <i> Wang X, Zhang S, Zhang J, Huang X, Xu C, Wang W, Liu Z, Wu J, Shi Y. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006206","region_id":"DP00608r011","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":129,"term_name":"protein binding","start":59,"ec_name":"near-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"20007319","version":3,"reference_html":"A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR. <i> Wang X, Zhang S, Zhang J, Huang X, Xu C, Wang W, Liu Z, Wu J, Shi Y. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006206","region_id":"DP00608r012","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":129,"region_id":"DP00608r013","released":"2022_03","ec_id":"ECO:0006232","reference_html":"A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR. <i> Wang X, Zhang S, Zhang J, Huang X, Xu C, Wang W, Liu Z, Wu J, Shi Y. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"fquaglia","start":59,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20007319","version":2,"ec_name":"differential scanning calorimetry evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":129,"term_name":"molecular function regulator","start":59,"ec_name":"differential scanning calorimetry evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"20007319","version":3,"reference_html":"A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR. <i> Wang X, Zhang S, Zhang J, Huang X, Xu C, Wang W, Liu Z, Wu J, Shi Y. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006232","region_id":"DP00608r014","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":129,"term_name":"disorder to order","start":59,"ec_name":"differential scanning calorimetry evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20007319","version":2,"reference_html":"A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR. <i> Wang X, Zhang S, Zhang J, Huang X, Xu C, Wang W, Liu Z, Wu J, Shi Y. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006232","region_id":"DP00608r015","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":129,"term_name":"protein binding","start":59,"ec_name":"differential scanning calorimetry evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"20007319","version":3,"reference_html":"A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR. <i> Wang X, Zhang S, Zhang J, Huang X, Xu C, Wang W, Liu Z, Wu J, Shi Y. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006232","region_id":"DP00608r016","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q13573","date":"2016-08-26T14:11:35.000Z","acc":"Q13573","name":"SNW domain-containing protein 1","length":536,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000000DB2D","genes":[{"name":{"value":"SNW1"},"synonyms":[{"value":"SKIIP"},{"value":"SKIP","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10713164","url":"http://www.ncbi.nlm.nih.gov/pubmed/10713164","alternativeUrl":"https://europepmc.org/abstract/MED/10713164"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"11371506","url":"http://www.ncbi.nlm.nih.gov/pubmed/11371506","alternativeUrl":"https://europepmc.org/abstract/MED/11371506"}}]}]}],"alphafold_very_low_content":0.08582089552238806,"disorder_content":0.13246268656716417,"disprot_consensus":{"full":[{"start":59,"end":129,"type":"T"}],"Structural state":[{"start":59,"end":129,"type":"D"}],"Molecular function":[{"start":59,"end":129,"type":"F"}],"Structural transition":[{"start":59,"end":129,"type":"T"}]}},{"features":{"pfam":[{"id":"PF04548","name":"AIG1 family","start":856,"end":990},{"id":"PF11886","name":"Translocase of chloroplast 159/132, membrane anchor domain","start":1225,"end":1489}],"gene3D":[{"start":833,"end":1088,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_O81283","sequence":"MDSKSVTPEPTNPFYASSGQSGKTYASVVAAAAAAAADKEDGGAVSSAKELDSSSEAVSGNSDKVGADDLSDSEKEKPNLVGDGKVSDEVDGSLKEDSTTPEATPKPEVVSGETIGVDDVSSLSPKPEAVSDGVGVVEENKKVKEDVEDIKDDGESKIENGSVDVDVKQASTDGESESKVKDVEEEDVGTKKDDEGESELGGKVDVDDKSDNVIEEEGVELTDKGDVIVNSSPVESVHVDVAKPGVVVVGDAEGSEELKINADAETLEVANKFDQIGDDDSGEFEPVSDKAIEEVEEKFTSESDSIADSSKLESVDTSAVEPEVVAAESGSEPKDVEKANGLEKGMTYAEVIKAASAVADNGTKEEESVLGGIVDDAEEGVKLNNKGDFVVDSSAIEAVNVDVAKPGVVVVGDVEVSEVLETDGNIPDVHNKFDPIGQGEGGEVELESDKATEEGGGKLVSEGDSMVDSSVVDSVDADINVAEPGVVVVGAAKEAVIKEDDKDDEVDKTISNIEEPDDLTAAYDGNFELAVKEISEAAKVEPDEPKVGVEVEELPVSESLKVGSVDAEEDSIPAAESQFEVRKVVEGDSAEEDENKLPVEDIVSSREFSFGGKEVDQEPSGEGVTRVDGSESEEETEEMIFGSSEAAKQFLAELEKASSGIEAHSDEANISNNMSDRIDGQIVTDSDEDVDTEDEGEEKMFDTAALAALLKAATGGGSSEGGNFTITSQDGTKLFSMDRPAGLSSSLRPLKPAAAPRANRSNIFSNSNVTMADETEINLSEEEKQKLEKLQSLRVKFLRLLQRLGHSAEDSIAAQVLYRLALLAGRQAGQLFSLDAAKKKAVESEAEGNEELIFSLNILVLGKAGVGKSATINSILGNQIASIDAFGLSTTSVREISGTVNGVKITFIDTPGLKSAAMDQSTNAKMLSSVKKVMKKCPPDIVLYVDRLDTQTRDLNNLPLLRTITASLGTSIWKNAIVTLTHAASAPPDGPSGTPLSYDVFVAQCSHIVQQSIGQAVGDLRLMNPSLMNPVSLVENHPLCRKNREGVKVLPNGQTWRSQLLLLCYSLKVLSETNSLLRPQEPLDHRKVFGFRVRSPPLPYLLSWLLQSRAHPKLPGDQGGDSVDSDIEIDDVSDSEQEDGEDDEYDQLPPFKPLRKTQLAKLSNEQRKAYFEEYDYRVKLLQKKQWREELKRMKEMKKNGKKLGESEFGYPGEEDDPENGAPAAVPVPLPDMVLPPSFDSDNSAYRYRYLEPTSQLLTRPVLDTHGWDHDCGYDGVNAEHSLALASRFPATATVQVTKDKKEFNIHLDSSVSAKHGENGSTMAGFDIQNVGKQLAYVVRGETKFKNLRKNKTTVGGSVTFLGENIATGVKLEDQIALGKRLVLVGSTGTMRSQGDSAYGANLEVRLREADFPIGQDQSSFGLSLVKWRGDLALGANLQSQVSVGRNSKIALRAGLNNKMSGQITVRTSSSDQLQIALTAILPIAMSIYKSIRPEATNDKYSMY","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_O81283","disprot_id":"DP00609","ncbi_taxon_id":3702,"regions_counter":16,"creator":"pwarholm","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":727,"region_id":"DP00609r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains. <i> Richardson LG, Jelokhani-Niaraki M, Smith MD. </i> BMC Biochem, 2009","term_id":"IDPO:0000002","curator_id":"pwarholm","start":1,"term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"20042108","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":727,"term_name":"molecular function regulator","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"GO","curator_name":"Per Warholm","reference_id":"20042108","version":3,"reference_html":"The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains. <i> Richardson LG, Jelokhani-Niaraki M, Smith MD. </i> BMC Biochem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006204","region_id":"DP00609r002","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":727,"term_name":"disorder to order","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"20042108","version":2,"reference_html":"The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains. <i> Richardson LG, Jelokhani-Niaraki M, Smith MD. </i> BMC Biochem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00609r003","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":727,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"GO","curator_name":"Per Warholm","reference_id":"20042108","version":3,"reference_html":"The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains. <i> Richardson LG, Jelokhani-Niaraki M, Smith MD. </i> BMC Biochem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00609r004","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":839,"region_id":"DP00609r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains. <i> Richardson LG, Jelokhani-Niaraki M, Smith MD. </i> BMC Biochem, 2009","term_id":"IDPO:0000002","curator_id":"pwarholm","start":639,"term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"20042108","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":839,"term_name":"molecular function regulator","start":639,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"GO","curator_name":"Per Warholm","reference_id":"20042108","version":3,"reference_html":"The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains. <i> Richardson LG, Jelokhani-Niaraki M, Smith MD. </i> BMC Biochem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006204","region_id":"DP00609r006","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":839,"term_name":"disorder to order","start":639,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"20042108","version":2,"reference_html":"The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains. <i> Richardson LG, Jelokhani-Niaraki M, Smith MD. </i> BMC Biochem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00609r007","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":839,"term_name":"protein binding","start":639,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"GO","curator_name":"Per Warholm","reference_id":"20042108","version":3,"reference_html":"The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains. <i> Richardson LG, Jelokhani-Niaraki M, Smith MD. </i> BMC Biochem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00609r008","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":627,"region_id":"DP00609r009","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains. <i> Richardson LG, Jelokhani-Niaraki M, Smith MD. </i> BMC Biochem, 2009","term_id":"IDPO:0000002","curator_id":"pwarholm","start":408,"term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"20042108","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":627,"term_name":"molecular function regulator","start":408,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"GO","curator_name":"Per Warholm","reference_id":"20042108","version":3,"reference_html":"The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains. <i> Richardson LG, Jelokhani-Niaraki M, Smith MD. </i> BMC Biochem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006204","region_id":"DP00609r010","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":627,"term_name":"disorder to order","start":408,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"20042108","version":2,"reference_html":"The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains. <i> Richardson LG, Jelokhani-Niaraki M, Smith MD. </i> BMC Biochem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00609r011","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":627,"term_name":"protein binding","start":408,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"GO","curator_name":"Per Warholm","reference_id":"20042108","version":3,"reference_html":"The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains. <i> Richardson LG, Jelokhani-Niaraki M, Smith MD. </i> BMC Biochem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00609r012","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":374,"region_id":"DP00609r013","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains. <i> Richardson LG, Jelokhani-Niaraki M, Smith MD. </i> BMC Biochem, 2009","term_id":"IDPO:0000002","curator_id":"pwarholm","start":163,"term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"20042108","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":374,"term_name":"molecular function regulator","start":163,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"GO","curator_name":"Per Warholm","reference_id":"20042108","version":3,"reference_html":"The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains. <i> Richardson LG, Jelokhani-Niaraki M, Smith MD. </i> BMC Biochem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006204","region_id":"DP00609r014","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":374,"term_name":"disorder to order","start":163,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"20042108","version":2,"reference_html":"The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains. <i> Richardson LG, Jelokhani-Niaraki M, Smith MD. </i> BMC Biochem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00609r015","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":374,"term_name":"protein binding","start":163,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"GO","curator_name":"Per Warholm","reference_id":"20042108","version":3,"reference_html":"The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains. <i> Richardson LG, Jelokhani-Niaraki M, Smith MD. </i> BMC Biochem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00609r016","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_O81283","date":"2016-09-08T15:38:05.000Z","acc":"O81283","name":"Translocase of chloroplast 159, chloroplastic","length":1503,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI00000A553E","genes":[{"name":{"value":"TOC159"},"synonyms":[{"value":"PPI2"},{"value":"TOC160"},{"value":"TOC86"}],"orfNames":[{"value":"T10P11.19"},{"value":"T14P8.24"}],"olnNames":[{"value":"At4g02510"}]}],"alphafold_very_low_content":0.5761809713905522,"disorder_content":0.5582168995342648,"disprot_consensus":{"full":[{"start":1,"end":839,"type":"T"}],"Structural state":[{"start":1,"end":839,"type":"D"}],"Molecular function":[{"start":1,"end":839,"type":"F"}],"Structural transition":[{"start":1,"end":839,"type":"T"}]}},{"features":{"pfam":[{"id":"PF04548","name":"AIG1 family","start":575,"end":737},{"id":"PF11886","name":"Translocase of chloroplast 159/132, membrane anchor domain","start":932,"end":1196}],"gene3D":[{"start":541,"end":797,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_Q9SLF3","sequence":"MGDGTEFVVRSDREDKKLAEDRISDEQVVKNELVRSDEVRDDNEDEVFEEAIGSENDEQEEEEDPKRELFESDDLPLVETLKSSMVEHEVEDFEEAVGDLDETSSNEGGVKDFTAVGESHGAGEAEFDVLATKMNGDKGEGGGGGSYDKVESSLDVVDTTENATSTNTNGSNLAAEHVGIENGKTHSFLGNGIASPKNKEVVAEVIPKDDGIEEPWNDGIEVDNWEERVDGIQTEQEVEEGEGTTENQFEKRTEEEVVEGEGTSKNLFEKQTEQDVVEGEGTSKDLFENGSVCMDSESEAERNGETGAAYTSNIVTNASGDNEVSSAVTSSPLEESSSGEKGETEGDSTCLKPEQHLASSPHSYPESTEVHSNSGSPGVTSREHKPVQSANGGHDVQSPQPNKELEKQQSSRVHVDPEITENSHVETEPEVVSSVSPTESRSNPAALPPARPAGLGRASPLLEPASRAPQQSRVNGNGSHNQFQQAEDSTTTEADEHDETREKLQLIRVKFLRLAHRLGQTPHNVVVAQVLYRLGLAEQLRGRNGSRVGAFSFDRASAMAEQLEAAGQDPLDFSCTIMVLGKSGVGKSATINSIFDEVKFCTDAFQMGTKRVQDVEGLVQGIKVRVIDTPGLLPSWSDQAKNEKILNSVKAFIKKNPPDIVLYLDRLDMQSRDSGDMPLLRTISDVFGPSIWFNAIVGLTHAASVPPDGPNGTASSYDMFVTQRSHVIQQAIRQAAGDMRLMNPVSLVENHSACRTNRAGQRVLPNGQVWKPHLLLLSFASKILAEANALLKLQDNIPGRPFAARSKAPPLPFLLSSLLQSRPQPKLPEQQYGDEEDEDDLEESSDSDEESEYDQLPPFKSLTKAQMATLSKSQKKQYLDEMEYREKLLMKKQMKEERKRRKMFKKFAAEIKDLPDGYSENVEEESGGPASVPVPMPDLSLPASFDSDNPTHRYRYLDSSNQWLVRPVLETHGWDHDIGYEGVNAERLFVVKEKIPISVSGQVTKDKKDANVQLEMASSVKHGEGKSTSLGFDMQTVGKELAYTLRSETRFNNFRRNKAAAGLSVTHLGDSVSAGLKVEDKFIASKWFRIVMSGGAMTSRGDFAYGGTLEAQLRDKDYPLGRFLTTLGLSVMDWHGDLAIGGNIQSQVPIGRSSNLIARANLNNRGAGQVSVRVNSSEQLQLAMVAIVPLFKKLLSYYYPQTQYGQ","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q9SLF3","disprot_id":"DP00610","ncbi_taxon_id":3702,"regions_counter":4,"creator":"pwarholm","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":455,"region_id":"DP00610r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains. <i> Richardson LG, Jelokhani-Niaraki M, Smith MD. </i> BMC Biochem, 2009","term_id":"IDPO:0000002","curator_id":"pwarholm","start":1,"term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"20042108","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":455,"term_name":"molecular function regulator","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"GO","curator_name":"Per Warholm","reference_id":"20042108","version":3,"reference_html":"The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains. <i> Richardson LG, Jelokhani-Niaraki M, Smith MD. </i> BMC Biochem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006204","region_id":"DP00610r002","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":455,"term_name":"disorder to order","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"20042108","version":2,"reference_html":"The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains. <i> Richardson LG, Jelokhani-Niaraki M, Smith MD. </i> BMC Biochem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00610r003","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":455,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"GO","curator_name":"Per Warholm","reference_id":"20042108","version":3,"reference_html":"The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains. <i> Richardson LG, Jelokhani-Niaraki M, Smith MD. </i> BMC Biochem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00610r004","curator_orcid":"0000-0002-2242-7721","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q9SLF3","date":"2016-09-08T15:46:52.000Z","acc":"Q9SLF3","name":"Translocase of chloroplast 132, chloroplastic","length":1206,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI00000A8672","genes":[{"name":{"value":"TOC132"},"orfNames":[{"value":"T24I21.5"}],"olnNames":[{"value":"At2g16640"}]}],"alphafold_very_low_content":0.45439469320066334,"disorder_content":0.37728026533996684,"disprot_consensus":{"full":[{"start":1,"end":455,"type":"T"}],"Structural state":[{"start":1,"end":455,"type":"D"}],"Molecular function":[{"start":1,"end":455,"type":"F"}],"Structural transition":[{"start":1,"end":455,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":299,"end":568}],"gene3D":[{"start":288,"end":377,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":378,"end":575,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"}]},"uniref50":"UniRef50_P30291","sequence":"MSFLSRQQPPPPRRAGAACTLRQKLIFSPCSDCEEEEEEEEEEGSGHSTGEDSAFQEPDSPLPPARSPTEPGPERRRSPGPAPGSPGELEEDLLLPGACPGADEAGGGAEGDSWEEEGFGSSSPVKSPAAPYFLGSSFSPVRCGGPGDASPRGCGARRAGEGRRSPRPDHPGTPPHKTFRKLRLFDTPHTPKSLLSKARGIDSSSVKLRGSSLFMDTEKSGKREFDVRQTPQVNINPFTPDSLLLHSSGQCRRRKRTYWNDSCGEDMEASDYELEDETRPAKRITITESNMKSRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLGQHSHVVRYFSAWAEDDHMLIQNEYCNGGSLADAISENYRIMSYFKEAELKDLLLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAASEEGDEDDWASNKVMFKIGDLGHVTRISSPQVEEGDSRFLANEVLQENYTHLPKADIFALALTVVCAAGAEPLPRNGDQWHEIRQGRLPRIPQVLSQEFTELLKVMIHPDPERRPSAMALVKHSVLLSASRKSAEQLRIELNAEKFKNSLLQKELKKAQMAKAAAEERALFTDRMATRSTTQSNRTSRLIGKKMNRSVSLTIY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P30291","disprot_id":"DP00611","ncbi_taxon_id":9606,"regions_counter":5,"creator":"agasparini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":455,"region_id":"DP00611r004","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Structure and inhibition of the human cell cycle checkpoint kinase, Wee1A kinase: an atypical tyrosine kinase with a key role in CDK1 regulation. <i> Squire CJ, Dickson JM, Ivanovic I, Baker EN. </i> Structure, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":436,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15837193","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-08-22T15:50:18.825Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1X8B"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEMBL","id":"214253","statements":[{"type":"Methods","text":"A 50 µl aliquot of Wee1A291–575 protein (concentration ∼7 mg/ml) was mixed with 2.5 µl of PD0407824 (9-hydroxy-4-phenyl-6H-pyrrolo[3,4-c]carbazole-1,3-dione) at a 4 mM concentration in dimethyl sulfoxide."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"}],"statement":[{"text":"All 279 residues of the kinase domain construct have been modeled except for residues 436–455 and 570–575, which had no interpretable electron density.","type":"Results"}]},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":455,"term_name":"flexible linker","start":436,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"vnugnes","released":"2022_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15837193","version":4,"reference_html":"Structure and inhibition of the human cell cycle checkpoint kinase, Wee1A kinase: an atypical tyrosine kinase with a key role in CDK1 regulation. <i> Squire CJ, Dickson JM, Ivanovic I, Baker EN. </i> Structure, 2005","date":"2022-08-22T15:54:16.946Z","term_id":"IDPO:0000033","ec_id":"ECO:0006220","region_id":"DP00611r005","ec_go":"EXP","disprot_namespace":"Disorder function","curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEMBL","id":"214253","statements":[{"type":"Methods","text":"A 50 µl aliquot of Wee1A291–575 protein (concentration ∼7 mg/ml) was mixed with 2.5 µl of PD0407824 (9-hydroxy-4-phenyl-6H-pyrrolo[3,4-c]carbazole-1,3-dione) at a 4 mM concentration in dimethyl sulfoxide."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"}],"statement":[{"text":"The loop 436–455, not located in the structure, has been identified from its sequence as a potential PEST region (Watanabe et al., 1995).","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P30291","date":"2016-08-22T11:54:33.000Z","acc":"P30291","name":"Wee1-like protein kinase","length":646,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000017A3FF","genes":[{"name":{"value":"WEE1"}}],"alphafold_very_low_content":0.43034055727554177,"disorder_content":0.030959752321981424,"disprot_consensus":{"full":[{"start":436,"end":455,"type":"D"}],"Structural state":[{"start":436,"end":455,"type":"D"}],"Disorder function":[{"start":436,"end":455,"type":"F"}]}},{"features":{"pfam":[{"id":"PF15361","name":"Resistance to inhibitors of cholinesterase homologue 3","start":49,"end":205}]},"uniref50":"UniRef50_Q22472","sequence":"MPKTERRRDRDRDRDRERRNRRKRDDSYDDYDEEGGISGWKLGLVFGVIVVCFAMLYPTLFHPMLMGFLGRSPPSSPSINQQRPPIHPAMGGGSGQRHPGGGADVHPAMRMAQAQAESQSGGSKGMFTWMLPVYTIGVVLFLLYTLFKSKGKKSKRKKRNYFDSEDDDDESESETKYGGKFGKKKLEGLQKRLRETESAMSKILEQLESVQAGANPVDLDAADKRSEQLEEDPSVKEAVGLTETNEQYIKDLEVALKEFQSLSKEYDKAKMKKLKRKDSSSDEDEEDEEENSSELSEIEEEEEEVKPVKKSKSSSQSVGKRKNRPKSTSEEEDEGEEESRKVAEDAEEEGIDIDSEIREHAEKEKKDKNVRRRRPKKT","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"uniref90":"UniRef90_Q22472","disprot_id":"DP00613","ncbi_taxon_id":6239,"regions_counter":4,"creator":"pwarholm","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":378,"region_id":"DP00613r001","released":"2022_03","ec_id":"ECO:0007719","reference_html":"Receptor and subunit specific interactions of RIC-3 with nicotinic acetylcholine receptors. <i> Cohen Ben-Ami H, Biala Y, Farah H, Elishevitz E, Battat E, Treinin M. </i> Biochemistry, 2009","term_id":"IDPO:0000002","curator_id":"pwarholm","start":1,"term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"19899809","version":2,"ec_name":"immunodetection assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-2242-7721","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":378,"term_name":"protein folding chaperone","start":1,"ec_name":"immunodetection assay evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"GO","curator_name":"Per Warholm","reference_id":"19899809","version":3,"reference_html":"Receptor and subunit specific interactions of RIC-3 with nicotinic acetylcholine receptors. <i> Cohen Ben-Ami H, Biala Y, Farah H, Elishevitz E, Battat E, Treinin M. </i> Biochemistry, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0044183","ec_id":"ECO:0007719","region_id":"DP00613r002","curator_orcid":"0000-0002-2242-7721","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":378,"term_name":"disorder to order","start":1,"ec_name":"immunodetection assay evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"IDPO","curator_name":"Per Warholm","reference_id":"19899809","version":2,"reference_html":"Receptor and subunit specific interactions of RIC-3 with nicotinic acetylcholine receptors. <i> Cohen Ben-Ami H, Biala Y, Farah H, Elishevitz E, Battat E, Treinin M. </i> Biochemistry, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0007719","region_id":"DP00613r003","curator_orcid":"0000-0002-2242-7721","ec_go":"IDA","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":378,"term_name":"protein binding","start":1,"ec_name":"immunodetection assay evidence used in manual assertion","curator_id":"pwarholm","released":"2022_03","term_ontology":"GO","curator_name":"Per Warholm","reference_id":"19899809","version":3,"reference_html":"Receptor and subunit specific interactions of RIC-3 with nicotinic acetylcholine receptors. <i> Cohen Ben-Ami H, Biala Y, Farah H, Elishevitz E, Battat E, Treinin M. </i> Biochemistry, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007719","region_id":"DP00613r004","curator_orcid":"0000-0002-2242-7721","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q22472","date":"2016-09-08T15:49:16.000Z","acc":"Q22472","name":"Resistance to inhibitors of cholinesterase protein 3","length":378,"organism":"Caenorhabditis elegans","dataset":[],"UniParc":"UPI000007A37B","genes":[{"name":{"value":"ric-3"},"synonyms":[{"value":"des-5"}],"orfNames":[{"value":"T14A8.1"}]}],"alphafold_very_low_content":0.31746031746031744,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":378,"type":"T"}],"Structural state":[{"start":1,"end":378,"type":"D"}],"Molecular function":[{"start":1,"end":378,"type":"F"}],"Structural transition":[{"start":1,"end":378,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00121","name":"Triosephosphate isomerase","start":6,"end":246}],"gene3D":[{"start":1,"end":248,"id":"3.20.20.70","name":"Aldolase class I"}]},"uniref50":"UniRef50_Q7KQM0","sequence":"MARKYFVAANWKCNGTLESIKSLTNSFNNLDFDPSKLDVVVFPVSVHYDHTRKLLQSKFSTGIQNVSKFGNGSYTGEVSAEIAKDLNIEYVIIGHFERRKYFHETDEDVREKLQASLKNNLKAVVCFGESLEQREQNKTIEVITKQVKAFVDLIDNFDNVILAYEPLWAIGTGKTATPEQAQLVHKEIRKIVKDTCGEKQANQIRILYGGSVNTENCSSLIQQEDIDGFLVGNASLKESFVDIIKSAM","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"uniref90":"UniRef90_Q7KQM0","disprot_id":"DP00614","ncbi_taxon_id":5833,"regions_counter":10,"creator":"ktsirigos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":178,"region_id":"DP00614r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design. <i> Velanker SS, Ray SS, Gokhale RS, Suma S, Balaram H, Balaram P, Murthy MR. </i> Structure, 1997","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":165,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"9261072","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":178,"term_name":"molecular recognition display site","start":165,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"9261072","version":2,"reference_html":"Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design. <i> Velanker SS, Ray SS, Gokhale RS, Suma S, Balaram H, Balaram P, Murthy MR. </i> Structure, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000037","ec_id":"ECO:0006220","region_id":"DP00614r002","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":178,"term_name":"protein binding","start":165,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"9261072","version":3,"reference_html":"Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design. <i> Velanker SS, Ray SS, Gokhale RS, Suma S, Balaram H, Balaram P, Murthy MR. </i> Structure, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00614r003","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":80,"region_id":"DP00614r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Tyr74 is essential for the formation, stability and function of Plasmodium falciparum triosephosphate isomerase dimer. <i> Espinoza-Fonseca LM, Wong-Ramírez C, Trujillo-Ferrara JG. </i> Arch Biochem Biophys, 2010","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":66,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19914198","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":80,"term_name":"molecular function regulator","start":66,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19914198","version":3,"reference_html":"Tyr74 is essential for the formation, stability and function of Plasmodium falciparum triosephosphate isomerase dimer. <i> Espinoza-Fonseca LM, Wong-Ramírez C, Trujillo-Ferrara JG. </i> Arch Biochem Biophys, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006220","region_id":"DP00614r005","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":80,"term_name":"disorder to order","start":66,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19914198","version":2,"reference_html":"Tyr74 is essential for the formation, stability and function of Plasmodium falciparum triosephosphate isomerase dimer. <i> Espinoza-Fonseca LM, Wong-Ramírez C, Trujillo-Ferrara JG. </i> Arch Biochem Biophys, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00614r006","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":80,"term_name":"protein binding","start":66,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19914198","version":3,"reference_html":"Tyr74 is essential for the formation, stability and function of Plasmodium falciparum triosephosphate isomerase dimer. <i> Espinoza-Fonseca LM, Wong-Ramírez C, Trujillo-Ferrara JG. </i> Arch Biochem Biophys, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00614r007","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":80,"region_id":"DP00614r008","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design. <i> Velanker SS, Ray SS, Gokhale RS, Suma S, Balaram H, Balaram P, Murthy MR. </i> Structure, 1997","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":66,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"9261072","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":80,"term_name":"molecular recognition display site","start":66,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"9261072","version":2,"reference_html":"Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design. <i> Velanker SS, Ray SS, Gokhale RS, Suma S, Balaram H, Balaram P, Murthy MR. </i> Structure, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000037","ec_id":"ECO:0006220","region_id":"DP00614r009","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":80,"term_name":"protein binding","start":66,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"9261072","version":3,"reference_html":"Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design. <i> Velanker SS, Ray SS, Gokhale RS, Suma S, Balaram H, Balaram P, Murthy MR. </i> Structure, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00614r010","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q7KQM0","date":"2016-09-09T09:35:07.000Z","acc":"Q07412","name":"Triosephosphate isomerase","length":248,"organism":"Plasmodium falciparum","dataset":[],"UniParc":"UPI0000001A19","genes":[{"name":{"value":"TPI","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"7903426","url":"http://www.ncbi.nlm.nih.gov/pubmed/7903426","alternativeUrl":"https://europepmc.org/abstract/MED/7903426"}}]}}],"alphafold_very_low_content":0,"disorder_content":0.11693548387096774,"disprot_consensus":{"full":[{"start":66,"end":80,"type":"T"},{"start":165,"end":178,"type":"D"}],"Structural state":[{"start":66,"end":80,"type":"D"},{"start":165,"end":178,"type":"D"}],"Disorder function":[{"start":66,"end":80,"type":"F"},{"start":165,"end":178,"type":"F"}],"Molecular function":[{"start":66,"end":80,"type":"F"},{"start":165,"end":178,"type":"F"}],"Structural transition":[{"start":66,"end":80,"type":"T"}]}},{"acc":"Q9WMX2","sequence":"MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARQPEGRAWAQPGYPWPLYGNEGLGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLALLSCLTIPASAYEVRNVSGVYHVTNDCSNASIVYEAADMIMHTPGCVPCVRENNSSRCWVALTPTLAARNASVPTTTIRRHVDLLVGAAALCSAMYVGDLCGSVFLVAQLFTFSPRRHETVQDCNCSIYPGHVTGHRMAWDMMMNWSPTAALVVSQLLRIPQAVVDMVAGAHWGVLAGLAYYSMVGNWAKVLIVMLLFAGVDGGTYVTGGTMAKNTLGITSLFSPGSSQKIQLVNTNGSWHINRTALNCNDSLNTGFLAALFYVHKFNSSGCPERMASCSPIDAFAQGWGPITYNESHSSDQRPYCWHYAPRPCGIVPAAQVCGPVYCFTPSPVVVGTTDRFGVPTYSWGENETDVLLLNNTRPPQGNWFGCTWMNSTGFTKTCGGPPCNIGGIGNKTLTCPTDCFRKHPEATYTKCGSGPWLTPRCLVHYPYRLWHYPCTVNFTIFKVRMYVGGVEHRLEAACNWTRGERCNLEDRDRSELSPLLLSTTEWQVLPCSFTTLPALSTGLIHLHQNVVDVQYLYGIGSAVVSFAIKWEYVLLLFLLLADARVCACLWMMLLIAQAEAALENLVVLNAASVAGAHGILSFLVFFCAAWYIKGRLVPGAAYALYGVWPLLLLLLALPPRAYAMDREMAASCGGAVFVGLILLTLSPHYKLFLARLIWWLQYFITRAEAHLQVWIPPLNVRGGRDAVILLTCAIHPELIFTITKILLAILGPLMVLQAGITKVPYFVRAHGLIRACMLVRKVAGGHYVQMALMKLAALTGTYVYDHLTPLRDWAHAGLRDLAVAVEPVVFSDMETKVITWGADTAACGDIILGLPVSARRGREIHLGPADSLEGQGWRLLAPITAYSQQTRGLLGCIITSLTGRDRNQVEGEVQVVSTATQSFLATCVNGVCWTVYHGAGSKTLAGPKGPITQMYTNVDQDLVGWQAPPGARSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPVSYLKGSSGGPLLCPSGHAVGIFRAAVCTRGVAKAVDFVPVESMETTMRSPVFTDNSSPPAVPQTFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIDPNIRTGVRTITTGAPITYSTYGKFLADGGCSGGAYDIIICDECHSTDSTTILGIGTVLDQAETAGARLVVLATATPPGSVTVPHPNIEEVALSSTGEIPFYGKAIPIETIKGGRHLIFCHSKKKCDELAAKLSGLGLNAVAYYRGLDVSVIPTSGDVIVVATDALMTGFTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTVPQDAVSRSQRRGRTGRGRMGIYRFVTPGERPSGMFDSSVLCECYDAGCAWYELTPAETSVRLRAYLNTPGLPVCQDHLEFWESVFTGLTHIDAHFLSQTKQAGDNFPYLVAYQATVCARAQAPPPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEVTTTHPITKYIMACMSADLEVVTSTWVLVGGVLAALAAYCLTTGSVVIVGRIILSGKPAIIPDREVLYREFDEMEECASHLPYIEQGMQLAEQFKQKAIGLLQTATKQAEAAAPVVESKWRTLEAFWAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTASITSPLTTQHTLLFNILGGWVAAQLAPPSAASAFVGAGIAGAAVGSIGLGKVLVDILAGYGAGVAGALVAFKVMSGEMPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLIAFASRGNHVSPTHYVPESDAAARVTQILSSLTITQLLKRLHQWINEDCSTPCSGSWLRDVWDWICTVLTDFKTWLQSKLLPRLPGVPFFSCQRGYKGVWRGDGIMQTTCPCGAQITGHVKNGSMRIVGPRTCSNTWHGTFPINAYTTGPCTPSPAPNYSRALWRVAAEEYVEVTRVGDFHYVTGMTTDNVKCPCQVPAPEFFTEVDGVRLHRYAPACKPLLREEVTFLVGLNQYLVGSQLPCEPEPDVAVLTSMLTDPSHITAETAKRRLARGSPPSLASSSASQLSAPSLKATCTTRHDSPDADLIEANLLWRQEMGGNITRVESENKVVILDSFEPLQAEEDEREVSVPAEILRRSRKFPRAMPIWARPDYNPPLLESWKDPDYVPPVVHGCPLPPAKAPPIPPPRRKRTVVLSESTVSSALAELATKTFGSSESSAVDSGTATASPDQPSDDGDAGSDVESYSSMPPLEGEPGDPDLSDGSWSTVSEEASEDVVCCSMSYTWTGALITPCAAEETKLPINALSNSLLRHHNLVYATTSRSASLRQKKVTFDRLQVLDDHYRDVLKEMKAKASTVKAKLLSVEEACKLTPPHSARSKFGYGAKDVRNLSSKAVNHIRSVWKDLLEDTETPIDTTIMAKNEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVSTLPQAVMGSSYGFQYSPGQRVEFLVNAWKAKKCPMGFAYDTRCFDSTVTENDIRVEESIYQCCDLAPEARQAIRSLTERLYIGGPLTNSKGQNCGYRRCRASGVLTTSCGNTLTCYLKAAAACRAAKLQDCTMLVCGDDLVVICESAGTQEDEASLRAFTEAMTRYSAPPGDPPKPEYDLELITSCSSNVSVAHDASGKRVYYLTRDPTTPLARAAWETARHTPVNSWLGNIIMYAPTLWARMILMTHFFSILLAQEQLEKALDCQIYGACYSIEPLDLPQIIQRLHGLSAFSLHSYSPGEINRVASCLRKLGVPPLRVWRHRARSVRARLLSQGGRAATCGKYLFNWAVRTKLKLTPIPAASQLDLSSWFVAGYSGGDIYHSLSRARPRWFMWCLLLLSVGVGIYLLPNR","creator":"esalladini","dataset":["Viral proteins","RNA-binding proteins"],"date":"2016-09-01T10:46:44.000Z","disprot_id":"DP00615","features":{"pfam":[{"id":"PF00998","name":"Viral RNA dependent RNA polymerase","start":2422,"end":2932},{"id":"PF01001","name":"Hepatitis C virus non-structural protein NS4b","start":1729,"end":1921},{"id":"PF01006","name":"Hepatitis C virus non-structural protein NS4a","start":1658,"end":1711},{"id":"PF01506","name":"Hepatitis C virus non-structural 5a protein membrane anchor","start":1974,"end":1996},{"id":"PF01538","name":"Hepatitis C virus non-structural protein NS2","start":811,"end":1005},{"id":"PF01539","name":"Hepatitis C virus envelope glycoprotein E1","start":193,"end":382},{"id":"PF01542","name":"Hepatitis C virus core protein","start":116,"end":190},{"id":"PF01543","name":"Hepatitis C virus capsid protein","start":2,"end":115},{"id":"PF01560","name":"Hepatitis C virus non-structural protein E2/NS1","start":387,"end":729},{"id":"PF02907","name":"Hepatitis C virus NS3 protease","start":1056,"end":1203},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1294,"end":1355},{"id":"PF08300","name":"Hepatitis C virus non-structural 5a zinc finger domain","start":2006,"end":2067},{"id":"PF08301","name":"Hepatitis C virus non-structural 5a domain 1b","start":2068,"end":2168},{"id":"PF12941","name":"HCV NS5a protein C-terminal region","start":2179,"end":2419},{"id":"PF22027","name":"NS3 RNA helicase, C-terminal helical domain","start":1516,"end":1656}],"gene3D":[{"start":900,"end":977,"id":"1.20.1280.150","name":"Hepatitis C virus non-structural protein NS2, N-terminal domain","_id":"685af523b4ac24d5329d7e76"},{"start":2075,"end":2160,"id":"2.20.25.220","name":"Hepatitis C virus NS5A, 1B domain","_id":"685af523b4ac24d5329d7e77"},{"start":2014,"end":2074,"id":"2.20.25.210","name":"Hepatitis C NS5A, domain 1B","_id":"685af523b4ac24d5329d7e78"},{"start":994,"end":1021,"id":"2.30.30.710","name":"Hepatitis C virus non-structural protein NS2, C-terminal domain","_id":"685af523b4ac24d5329d7e79"},{"start":1355,"end":1512,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d7e7a"},{"start":1122,"end":1205,"id":"2.40.10.10","name":"Trypsin-like serine proteases","_id":"685af523b4ac24d5329d7e7b"},{"start":1022,"end":1120,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d7e7c"},{"start":206,"end":275,"id":"2.30.30.1080","name":"Hepatitis C virus envelope glycoprotein E1, chain C","_id":"685af523b4ac24d5329d7e7d"},{"start":2607,"end":2662,"id":"3.30.70.270","name":"3.30.70.270","_id":"685af523b4ac24d5329d7e7e"},{"start":2,"end":45,"id":"4.10.710.10","name":"Hepatitis C Virus Capsid Protein; Chain A","_id":"685af523b4ac24d5329d7e7f"},{"start":1206,"end":1354,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d7e80"},{"start":1513,"end":1641,"id":"1.10.820.10","name":"RNA Helicase Chain A , domain 3","_id":"685af523b4ac24d5329d7e81"}]},"genes":[],"length":3010,"name":"Genome polyprotein","ncbi_taxon_id":333284,"organism":"Hepatitis C virus genotype 1b (isolate Con1)","regions_counter":46,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Hepacivirus"],"UniParc":"UPI00000F9714","uniref100":"UniRef100_Q9WMX2","uniref50":"UniRef50_P27958","uniref90":"UniRef90_P26662","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"19055","_id":"685af523b4ac24d5329d7eb9"},{"db":"DisProt","id":"DP03511r002","_id":"685af523b4ac24d5329d7eba"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2220,"end":2313,"interaction_partner":[],"reference_html":"A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication. <i> Dujardin M, Madan V, Montserret R, Ahuja P, Huvent I, Launay H, Leroy A, Bartenschlager R, Penin F, Lippens G, Hanoulle X. </i> J Biol Chem, 2015","reference_id":"26085105","region_id":"DP00615r026","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The 1H,15N HSQC spectrum of NS5A-D2 (Con1 strain) displays a narrow 1HN chemical shift dispersion limited to 1 ppm, as expected for a mainly disordered domain (Fig. 1A).","_id":"685af523b4ac24d5329d7eb7"},{"type":"Curator statement","text":"The NS5A fragment used in this publication was derived from the Hepacivirus C UniProtKB:Q9WIK7. IDR is 100% identical to the Hepatitis C virus genotype 1b (isolate Con1) polyprotein.","_id":"685af523b4ac24d5329d7eb8"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T13:42:18.774Z","_id":"685af523b4ac24d5329d7ebb"},"version":1,"_id":"685af523b4ac24d5329d7eb6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"19059","_id":"685af523b4ac24d5329d7ebd"},{"db":"PDB","id":"2m5l","_id":"685af523b4ac24d5329d7ebe"},{"db":"DisProt","id":"DP03511r005","_id":"685af523b4ac24d5329d7ebf"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2280,"end":2299,"interaction_partner":[],"reference_html":"A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication. <i> Dujardin M, Madan V, Montserret R, Ahuja P, Huvent I, Launay H, Leroy A, Bartenschlager R, Penin F, Lippens G, Hanoulle X. </i> J Biol Chem, 2015","reference_id":"26085105","region_id":"DP00615r027","released":"2022_03","sample":[],"statement":[{"type":"Results","text":" The final set of 28 low energy structures that fulfill the experimental restraints displays a well defined small structural motif (from Met313 to Ala317) in PepD2-WT (Fig. 5 and Table 1; PDB code 2M5L), whereas the N and C termini remain highly flexible.","_id":"685af523b4ac24d5329d7ec0"},{"type":"Curator statement","text":"The NS5A fragment used in this publication was derived from the Hepacivirus C UniProtKB:Q9WIK7. IDR is 100% identical to the Hepatitis C virus genotype 1b (isolate Con1) polyprotein. PepD2-WT comprises the region 2280-2299 of the Hepatitis C virus genotype 1b (isolate Con1) genome polyprotein.","_id":"685af523b4ac24d5329d7ec1"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T13:42:06.203Z","_id":"685af523b4ac24d5329d7ec2"},"version":1,"_id":"685af523b4ac24d5329d7ebc","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"DisProt","id":"DP03511r003","_id":"685af523b4ac24d5329d7ec7"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2280,"end":2299,"interaction_partner":[{"db":"UniProt","id":"P62937","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7ec4"}],"reference_html":"A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication. <i> Dujardin M, Madan V, Montserret R, Ahuja P, Huvent I, Launay H, Leroy A, Bartenschlager R, Penin F, Lippens G, Hanoulle X. </i> J Biol Chem, 2015","reference_id":"26085105","region_id":"DP00615r028","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The affinity between CypA and the PW turn containing PepD2-WT peptide (KD = 0.5 mm) is three times better than the one involving the random coil PepD2-I315G peptide (KD = 1.4 mm).","_id":"685af523b4ac24d5329d7ec5"},{"type":"Curator statement","text":"The NS5A fragment used in this publication was derived from the Hepacivirus C UniProtKB:Q9WIK7. IDR is 100% identical to the Hepatitis C virus genotype 1b (isolate Con1) polyprotein. PepD2-WT comprises the region 2280-2299 of the Hepatitis C virus genotype 1b (isolate Con1) genome polyprotein.","_id":"685af523b4ac24d5329d7ec6"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-15T10:35:20.613Z","_id":"685af523b4ac24d5329d7ec8"},"version":1,"_id":"685af523b4ac24d5329d7ec3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"DisProt","id":"DP03511r001","_id":"685af523b4ac24d5329d7ecc"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":2280,"end":2299,"interaction_partner":[],"reference_html":"A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication. <i> Dujardin M, Madan V, Montserret R, Ahuja P, Huvent I, Launay H, Leroy A, Bartenschlager R, Penin F, Lippens G, Hanoulle X. </i> J Biol Chem, 2015","reference_id":"26085105","region_id":"DP00615r029","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"Region 2280-2299 is mainly unstructured, as shown by its large negative ellipticity at 200 nm and moderate ellipticity at 190 nm in the far-UV CD spectra (Figure 7).","_id":"685af523b4ac24d5329d7eca"},{"type":"Curator statement","text":"The NS5A fragment used in this publication was derived from the Hepacivirus C UniProtKB:Q9WIK7. IDR is 100% identical to the Hepatitis C virus genotype 1b (isolate Con1) polyprotein.","_id":"685af523b4ac24d5329d7ecb"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T13:42:00.111Z","_id":"685af523b4ac24d5329d7ecd"},"version":1,"_id":"685af523b4ac24d5329d7ec9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2212,"end":2307,"interaction_partner":[],"reference_html":"Domain 2 of nonstructural protein 5A (NS5A) of hepatitis C virus is natively unfolded. <i> Liang Y, Ye H, Kang CB, Yoon HS. </i> Biochemistry, 2007","reference_id":"17880107","region_id":"DP00615r030","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The chemical shifts of the backbone amide proton resonances are clustered in a narrow 1.3 ppm window from 7.2 to 8.5 ppm, and the dispersion of the 15N chemical shifts is narrowed in 19.2 ppm, as typical signs of an unfolded protein (23).","_id":"685af523b4ac24d5329d7ecf"},{"type":"Results","text":" As shown in Figure 2a, multinuclear (CA, CB, HA, and CO) chemical shift indexing, consensus CSI (30) values are zeros, suggesting that NS5A-D2 largely exists in a random coil conformation.","_id":"685af523b4ac24d5329d7ed0"},{"type":"Results","text":"The steady-state heteronuclear 1H−15N NOE for the backbone amide of NS5A-D2 exhibited a relatively featureless and flattened variation with the amino acid sequences (Figure 3a), as seen in unfolded proteins (33).","_id":"685af523b4ac24d5329d7ed1"},{"type":"Results","text":"The high T2 values measured for NS5A-D2 indicate large amplitude motions on the nanosecond to picosecond time scale, which is characteristic of a random coil conformation.","_id":"685af523b4ac24d5329d7ed2"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T13:41:42.729Z","_id":"685af523b4ac24d5329d7ed3"},"version":1,"_id":"685af523b4ac24d5329d7ece","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":2212,"end":2307,"interaction_partner":[],"reference_html":"Domain 2 of nonstructural protein 5A (NS5A) of hepatitis C virus is natively unfolded. <i> Liang Y, Ye H, Kang CB, Yoon HS. </i> Biochemistry, 2007","reference_id":"17880107","region_id":"DP00615r031","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As shown in Figure 5a, the CD spectrum of NS5A-D2 without TFE exhibits a minimum near 201 nm, with a slight negative ellipticity at about 222 nm, suggesting that it is mainly unfolded.","_id":"685af523b4ac24d5329d7ed5"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T13:41:24.772Z","_id":"685af523b4ac24d5329d7ed6"},"version":1,"_id":"685af523b4ac24d5329d7ed4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2212,"end":2307,"interaction_partner":[{"db":"UniProt","id":"Q9WMX2","partner_start":2558,"partner_end":2574,"_id":"685af523b4ac24d5329d7ed8"}],"reference_html":"Domain 2 of nonstructural protein 5A (NS5A) of hepatitis C virus is natively unfolded. <i> Liang Y, Ye H, Kang CB, Yoon HS. </i> Biochemistry, 2007","reference_id":"17880107","region_id":"DP00615r032","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Our NMR results showed that perturbations in the chemical shifts were observed in 1H−15N HSQC spectrum of 15N-labeled NS5A-D2 in the presence of 5 mM of the MK-17 peptide (Figure 7a), whereas the titration with the peptide SP-24 caused a heavy precipitate upon its addition (data not shown).","_id":"685af523b4ac24d5329d7ed9"},{"type":"Figure","text":"NS5A-D2 interacts with NS5B MK-17 peptide. ","_id":"685af523b4ac24d5329d7eda"},{"type":"Curator statement","text":"NS5A-D2 comprises the region 2212-2307 of the Hepatitis C virus genotype 1b (isolate Con1) genome polyprotein. The MK-17 peptide consist on the 139−155 residues of NS5B, which corresponds to 2558-2574 region of the Hepatitis C virus genotype 1b (isolate Con1) genome polyprotein.","_id":"685af523b4ac24d5329d7edb"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T13:43:53.456Z","_id":"685af523b4ac24d5329d7edc"},"version":1,"_id":"685af523b4ac24d5329d7ed7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"DisProt","id":"DP03511r006","_id":"685af523b4ac24d5329d7ee5"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2280,"end":2299,"interaction_partner":[],"reference_html":"A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication. <i> Dujardin M, Madan V, Montserret R, Ahuja P, Huvent I, Launay H, Leroy A, Bartenschlager R, Penin F, Lippens G, Hanoulle X. </i> J Biol Chem, 2015","reference_id":"26085105","region_id":"DP00615r034","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The affinity between CypA and the PW turn containing PepD2-WT peptide (KD = 0.5 mm) is three times better than the one involving the random coil PepD2-I315G peptide (KD = 1.4 mm).","_id":"685af523b4ac24d5329d7ee3"},{"type":"Curator statement","text":"The NS5A fragment used in this publication was derived from the Hepacivirus C UniProtKB:Q9WIK7. IDR is 100% identical to the Hepatitis C virus genotype 1b (isolate Con1) polyprotein. PepD2-WT comprises the region 2280-2299 of the Hepatitis C virus genotype 1b (isolate Con1) genome polyprotein.","_id":"685af523b4ac24d5329d7ee4"}],"states_connection":[],"term_comment":"","term_def":"\"Any process involved directly in viral genome replication, including viral nucleotide metabolism.\" [ISBN:0781702534]","term_id":"GO:0019079","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral genome replication","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-15T10:34:03.760Z","_id":"685af523b4ac24d5329d7ee6"},"version":1,"_id":"685af523b4ac24d5329d7ee2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":2331,"end":2417,"interaction_partner":[],"reference_html":"Domain 3 of NS5A protein from the hepatitis C virus has intrinsic alpha-helical propensity and is a substrate of cyclophilin A. <i> Verdegem D, Badillo A, Wieruszeski JM, Landrieu I, Leroy A, Bartenschlager R, Penin F, Lippens G, Hanoulle X. </i> J Biol Chem, 2011","reference_id":"21489988","region_id":"DP00615r035","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The CD spectrum of NS5A-D3 is typical for a poorly folded protein with a large negative peak centered at 198 nm.","_id":"685af523b4ac24d5329d7ee8"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T13:41:18.899Z","_id":"685af523b4ac24d5329d7ee9"},"version":1,"_id":"685af523b4ac24d5329d7ee7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2331,"end":2417,"interaction_partner":[{"db":"UniProt","id":"P62937","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7eeb"}],"reference_html":"Domain 3 of NS5A protein from the hepatitis C virus has intrinsic alpha-helical propensity and is a substrate of cyclophilin A. <i> Verdegem D, Badillo A, Wieruszeski JM, Landrieu I, Leroy A, Bartenschlager R, Penin F, Lippens G, Hanoulle X. </i> J Biol Chem, 2011","reference_id":"21489988","region_id":"DP00615r036","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"By comparison with the NS5A-D3 spectra recorded alone, we identified the residues involved in interaction with CypA based on chemical shift perturbations and/or peak broadening. ","_id":"685af523b4ac24d5329d7eec"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-15T10:35:16.715Z","_id":"685af523b4ac24d5329d7eed"},"version":1,"_id":"685af523b4ac24d5329d7eea","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":2331,"end":2417,"interaction_partner":[],"reference_html":"Domain 3 of non-structural protein 5A from hepatitis C virus is natively unfolded. <i> Hanoulle X, Verdegem D, Badillo A, Wieruszeski JM, Penin F, Lippens G. </i> Biochem Biophys Res Commun, 2009","reference_id":"19249289","region_id":"DP00615r037","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The purified protein exhibited the expected mass (9925 Da) as determined by mass spectroscopy (not shown). By SDS–PAGE, NS5A-D3 has an apparent molecular weight (MW) of ∼20 kDa (Fig. 2A). This discrepancy is probably due to the primary sequence of NS5A-D3, which includes many acidic residues and prolines.","_id":"685af523b4ac24d5329d7eef"},{"type":"Curator statement","text":"The anomalous electrophoretic mobility is frequently observed in intrinsically disordered proteins.","_id":"685af523b4ac24d5329d7ef0"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T13:41:09.981Z","_id":"685af523b4ac24d5329d7ef1"},"version":1,"_id":"685af523b4ac24d5329d7eee","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":2331,"end":2417,"interaction_partner":[],"reference_html":"Domain 3 of non-structural protein 5A from hepatitis C virus is natively unfolded. <i> Hanoulle X, Verdegem D, Badillo A, Wieruszeski JM, Penin F, Lippens G. </i> Biochem Biophys Res Commun, 2009","reference_id":"19249289","region_id":"DP00615r038","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The circular dichroism (CD) spectrum of NS5A-D3 exhibits a single negative peak centered at 198 nm (Fig. 2C) that is typical of unfolded polypeptide. The lack of characteristic minima around 208 and 222 nm indicative of α-helix, or the minimum around 215 nm that points to β-sheet elements, confirms the absence of regular secondary structure in NS5A-D3.","_id":"685af523b4ac24d5329d7ef3"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T13:41:06.936Z","_id":"685af523b4ac24d5329d7ef4"},"version":1,"_id":"685af523b4ac24d5329d7ef2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"16166","_id":"685af523b4ac24d5329d7ef8"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2331,"end":2417,"interaction_partner":[],"reference_html":"Domain 3 of non-structural protein 5A from hepatitis C virus is natively unfolded. <i> Hanoulle X, Verdegem D, Badillo A, Wieruszeski JM, Penin F, Lippens G. </i> Biochem Biophys Res Commun, 2009","reference_id":"19249289","region_id":"DP00615r039","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The 1H,15N HSQC spectrum of NS5A-D3 (Fig. 3A) exhibits a rather narrow 1H chemical shift dispersion limited to 0.75 ppm. NS5A-D3 resonances are clustered in three regions of the NMR spectrum corresponding to, respectively, the glycines, the serine and threonine and finally the other residues. This clustering and the limited dispersion in proton dimension are typical of non-structured polypeptides. ","_id":"685af523b4ac24d5329d7ef6"},{"type":"Results","text":"The resulting CSI consensus values are zero (Fig 3B, bottom), confirming the absence in NS5A-D3 of stable secondary structure elements even at the local level.","_id":"685af523b4ac24d5329d7ef7"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T13:41:04.969Z","_id":"685af523b4ac24d5329d7ef9"},"version":1,"_id":"685af523b4ac24d5329d7ef5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":2314,"end":null,"statements":[{"type":"Results","text":"NS5ADII proteins were site-specifically labeled by Cy3-maleimide via maleimide–thiol coupling chemistry at residue C342, which is the only cysteine residue in NS5ADII.","_id":"685af523b4ac24d5329d7f00"}],"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","_id":"685af523b4ac24d5329d7eff"}],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-08T15:34:31.964Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001183","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","ec_ontology":"ECO","start":2222,"end":2314,"interaction_partner":[{"db":"ENA","id":"CS607982.1:1..21:misc_RNA","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7f01"}],"reference_html":"Interactions of the Disordered Domain II of Hepatitis C Virus NS5A with Cyclophilin A, NS5B, and Viral RNA Show Extensive Overlap. <i> Ngure M, Issur M, Shkriabai N, Liu HW, Cosa G, Kvaratskhelia M, Götte M. </i> ACS Infect Dis, 2016","reference_id":"27676132","region_id":"DP00615r041","released":"2022_03","sample":[],"sequence_construct":"PDADLIEANLLWRQEMGGNITRVESENKVVILDSFEPLQAEEDEREVSVPAEILRRSRKFPRAMPIWARPDYNPPLLESWKDPDYVPPVVHGC","statement":[{"type":"Results","text":"Increases in EFRET,apparent with increasing concentrations of RNA provide evidence for binding (Figure 1A). A plateau in the EFRET,apparent indicates that the binding of cy3NS5ADII to cy5rU20 was saturated and reached its equilibrium after the addition of 50 nM RNA substrate. ","_id":"685af523b4ac24d5329d7efe"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_go_domain":"F","term_id":"GO:0003723","term_is_binding":true,"term_is_obsolete":false,"term_name":"RNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-08-12T13:58:01.413Z","_id":"685af523b4ac24d5329d7f02"},"version":2,"_id":"685af523b4ac24d5329d7efd","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":2314,"end":null,"statements":[{"type":"Results","text":"NS5ADII proteins were site-specifically labeled by Cy3-maleimide via maleimide–thiol coupling chemistry at residue C342, which is the only cysteine residue in NS5ADII.","_id":"685af523b4ac24d5329d7f07"}],"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","_id":"685af523b4ac24d5329d7f06"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001183","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","ec_ontology":"ECO","start":2222,"end":2314,"interaction_partner":[{"db":"UniProt","id":"P62937","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7f04"}],"reference_html":"Interactions of the Disordered Domain II of Hepatitis C Virus NS5A with Cyclophilin A, NS5B, and Viral RNA Show Extensive Overlap. <i> Ngure M, Issur M, Shkriabai N, Liu HW, Cosa G, Kvaratskhelia M, Götte M. </i> ACS Infect Dis, 2016","reference_id":"27676132","region_id":"DP00615r042","released":"2022_03","sample":[],"sequence_construct":"PDADLIEANLLWRQEMGGNITRVESENKVVILDSFEPLQAEEDEREVSVPAEILRRSRKFPRAMPIWARPDYNPPLLESWKDPDYVPPVVHGC","statement":[{"type":"Results","text":"The increase in EFRET,apparent is again indicative of binding. A higher maximum EFRET,apparent of 0.4 was reached with CypA, suggesting that NS5ADII bound more efficiently to CypA than RNA.","_id":"685af523b4ac24d5329d7f05"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-15T10:35:13.198Z","_id":"685af523b4ac24d5329d7f08"},"version":1,"_id":"685af523b4ac24d5329d7f03","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0005632","ec_name":"fluorescence anisotropy evidence used in manual assertion","ec_ontology":"ECO","start":2222,"end":2314,"interaction_partner":[{"db":"UniProt","id":"Q9WMX2","partner_start":2442,"partner_end":3011,"_id":"685af523b4ac24d5329d7f0a"}],"reference_html":"Interactions of the Disordered Domain II of Hepatitis C Virus NS5A with Cyclophilin A, NS5B, and Viral RNA Show Extensive Overlap. <i> Ngure M, Issur M, Shkriabai N, Liu HW, Cosa G, Kvaratskhelia M, Götte M. </i> ACS Infect Dis, 2016","reference_id":"27676132","region_id":"DP00615r043","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"With increasing concentrations of NS5B, a significant change in anisotropy was observed, which confirms the formation of a protein–protein complex with NS5B (Figure 1C).","_id":"685af523b4ac24d5329d7f0b"},{"type":"Curator statement","text":"NS5B peptide used corresponds to the 2442-3011 region of the Hepatitis C virus genotype 1b (isolate Con1) genome polyprotein.","_id":"685af523b4ac24d5329d7f0c"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-15T10:35:11.036Z","_id":"685af523b4ac24d5329d7f0d"},"version":1,"_id":"685af523b4ac24d5329d7f09","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"DisProt","id":"DP03511r007","_id":"685af523b4ac24d5329d7f18"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IEP","ec_id":"ECO:0005648","ec_name":"luciferase reporter gene assay evidence used in manual assertion","ec_ontology":"ECO","start":2289,"end":2293,"interaction_partner":[],"reference_html":"A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication. <i> Dujardin M, Madan V, Montserret R, Ahuja P, Huvent I, Launay H, Leroy A, Bartenschlager R, Penin F, Lippens G, Hanoulle X. </i> J Biol Chem, 2015","reference_id":"26085105","region_id":"DP00615r046","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As illustrated in Fig. 8, the sole mutation I315G in NS5A almost completely abolished viral replication that was close to the background as determined with the replicon encoding an inactive NS5B RNA-polymerase (GND mutant). The replication levels corresponding to the I315G and P314A mutations, respectively, were similar.","_id":"685af523b4ac24d5329d7f19"},{"type":"Results","text":"Hence, the short PW turn structural motif in the mainly disordered NS5A-D2 domain plays an essential role for HCV RNA replication.","_id":"685af523b4ac24d5329d7f1a"},{"type":"Curator statement","text":"The NS5A fragment used in this publication was derived from the Hepacivirus C UniProtKB:Q9WIK7. IDR is 100% identical to the Hepatitis C virus genotype 1b (isolate Con1) polyprotein. PepD2-WT comprises the region 2280-2299 of \nPW turn corresponds to the 2290-2292 region of the Hepatitis C virus genotype 1b (isolate Con1) genome polyprotein (P316 -W318 of the Ns5B protein). Although the authors describes this region as a small structural motif, the region is to short to form any secondary structure so is interpreted as disordered here.","_id":"685af523b4ac24d5329d7f1b"}],"states_connection":[],"term_comment":"","term_def":"\"Any process involved directly in viral genome replication, including viral nucleotide metabolism.\" [ISBN:0781702534]","term_go_domain":"P","term_id":"GO:0019079","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral genome replication","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-15T10:35:24.198Z","_id":"685af523b4ac24d5329d7f1c"},"version":1,"_id":"685af523b4ac24d5329d7f17","reference_source":"pmid"}],"__v":0,"disorder_content":0.06279069767441861,"disprot_consensus":{"full":[{"start":2212,"end":2313,"type":"D"},{"start":2314,"end":2314,"type":"F"},{"start":2331,"end":2417,"type":"D"}],"Structural state":[{"start":2212,"end":2313,"type":"D"},{"start":2331,"end":2417,"type":"D"}],"Molecular function":[{"start":2212,"end":2314,"type":"F"},{"start":2331,"end":2417,"type":"F"}],"Biological process":[{"start":2280,"end":2299,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00405","name":"Transferrin","start":25,"end":352},{"id":"PF00405","name":"Transferrin","start":364,"end":695}],"gene3D":[{"start":366,"end":696,"id":"3.40.190.10","name":"Periplasmic binding protein-like II"},{"start":111,"end":269,"id":"3.40.190.10","name":"Periplasmic binding protein-like II"},{"start":465,"end":624,"id":"3.40.190.10","name":"Periplasmic binding protein-like II"},{"start":25,"end":348,"id":"3.40.190.10","name":"Periplasmic binding protein-like II"}]},"uniref50":"UniRef50_P02788","sequence":"MKLVFLVLLFLGALGLCLAGRRRSVQWCAVSQPEATKCFQWQRNMRKVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKGGSFQLNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGADKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGKDKSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQNLRKSEEEVAARRARVVWCAVGEQELRKCNQWSGLSEGSVTCSSASTTEDCIALVLKGEADAMSLDGGYVYTAGKCGLVPVLAENYKSQQSSDPDPNCVDRPVEGYLAVAVVRRSDTSLTWNSVKGKKSCHTAVDRTAGWNIPMGLLFNQTGSCKFDEYFSQSCAPGSDPRSNLCALCIGDEQGENKCVPNSNERYYGYTGAFRCLAENAGDVAFVKDVTVLQNTDGNNNEAWAKDLKLADFALLCLDGKRKPVTEARSCHLAMAPNHAVVSRMDKVERLKQVLLHQQAKFGRNGSDCPDKFCLFQSETKNLLFNDNTECLARLHGKTTYEKYLGPQYVAGITNLKKCSTSPLLEACEFLRK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P02788","disprot_id":"DP00616","ncbi_taxon_id":9606,"regions_counter":6,"creator":"ktsirigos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":59,"region_id":"DP00616r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A cell-penetrating peptide derived from human lactoferrin with conformation-dependent uptake efficiency. <i> Duchardt F, Ruttekolk IR, Verdurmen WPR, Lortat-Jacob H, Bürck J, Hufnagel H, Fischer R, van den Heuvel M, Löwik DWPM, Vuister GW, Ulrich A, de Waard M, Brock R. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":38,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19858187","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":59,"term_name":"molecular function regulator","start":38,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19858187","version":3,"reference_html":"A cell-penetrating peptide derived from human lactoferrin with conformation-dependent uptake efficiency. <i> Duchardt F, Ruttekolk IR, Verdurmen WPR, Lortat-Jacob H, Bürck J, Hufnagel H, Fischer R, van den Heuvel M, Löwik DWPM, Vuister GW, Ulrich A, de Waard M, Brock R. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006165","region_id":"DP00616r002","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":59,"region_id":"DP00616r003","released":"2022_03","ec_id":"ECO:0007719","reference_html":"A cell-penetrating peptide derived from human lactoferrin with conformation-dependent uptake efficiency. <i> Duchardt F, Ruttekolk IR, Verdurmen WPR, Lortat-Jacob H, Bürck J, Hufnagel H, Fischer R, van den Heuvel M, Löwik DWPM, Vuister GW, Ulrich A, de Waard M, Brock R. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":38,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19858187","version":2,"ec_name":"immunodetection assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":59,"term_name":"molecular function regulator","start":38,"ec_name":"immunodetection assay evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19858187","version":3,"reference_html":"A cell-penetrating peptide derived from human lactoferrin with conformation-dependent uptake efficiency. <i> Duchardt F, Ruttekolk IR, Verdurmen WPR, Lortat-Jacob H, Bürck J, Hufnagel H, Fischer R, van den Heuvel M, Löwik DWPM, Vuister GW, Ulrich A, de Waard M, Brock R. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0007719","region_id":"DP00616r004","curator_orcid":"0000-0001-5280-1107","ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":59,"region_id":"DP00616r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"A cell-penetrating peptide derived from human lactoferrin with conformation-dependent uptake efficiency. <i> Duchardt F, Ruttekolk IR, Verdurmen WPR, Lortat-Jacob H, Bürck J, Hufnagel H, Fischer R, van den Heuvel M, Löwik DWPM, Vuister GW, Ulrich A, de Waard M, Brock R. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":38,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19858187","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":59,"term_name":"molecular function regulator","start":38,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19858187","version":3,"reference_html":"A cell-penetrating peptide derived from human lactoferrin with conformation-dependent uptake efficiency. <i> Duchardt F, Ruttekolk IR, Verdurmen WPR, Lortat-Jacob H, Bürck J, Hufnagel H, Fischer R, van den Heuvel M, Löwik DWPM, Vuister GW, Ulrich A, de Waard M, Brock R. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006204","region_id":"DP00616r006","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P02788","date":"2016-09-09T09:47:03.000Z","acc":"P02788","name":"Lactotransferrin","length":710,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000015C582","genes":[{"name":{"value":"LTF"},"synonyms":[{"value":"GIG12"},{"value":"LF"}]}],"alphafold_very_low_content":0.016901408450704224,"disorder_content":0.030985915492957747,"disprot_consensus":{"full":[{"start":38,"end":59,"type":"D"}],"Structural state":[{"start":38,"end":59,"type":"D"}],"Molecular function":[{"start":38,"end":59,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05160","name":"DSS1/SEM1 family","start":6,"end":62}]},"uniref50":"UniRef50_P60896","sequence":"MSEKKQPVDLGLLEEDDEFEEFPAEDWAGLDEDEDAHVWEDNWDDDNVEDDFSNQLRAELEKHGYKMETS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P60896","disprot_id":"DP00617","ncbi_taxon_id":9606,"regions_counter":5,"creator":"zskalman","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":36,"region_id":"DP00617r003","released":"2024_06","ec_id":"ECO:0006220","reference_html":"BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure. <i> Yang H, Jeffrey PD, Miller J, Kinnucan E, Sun Y, Thoma NH, Zheng N, Chen PL, Lee WH, Pavletich NP. </i> Science, 2002","term_id":"IDPO:0000002","curator_id":"vnugnes","start":26,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12228710","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2024-03-13T15:49:52.232Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1MIU"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P97929"}],"statement":[{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":1,"end":51,"reference_id":"34272906","reference_source":"pmid","reference_html":"The disordered PCI-binding human proteins CSNAP and DSS1 have diverged in structure and function. <i> Ruidiaz SF, Dreier JE, Hartmann-Petersen R, Kragelund BB. </i> Protein Sci, 2021","date":"2024-11-18T10:57:30.794Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"50906"}],"region_id":"DP00617r004","sequence_construct":"MSEKKQPVDLGLLEEDDEFEEFPAEDWAGLDEDEDAHVWEDNWDDDNVEDDFSNQLRAELEKHGYKMETS","statement":[{"text":"For both proteins, the assigned 1H-15N HSQC spectra (Figure 2b) demonstrated low dispersion in the proton dimension characteristic of disordered proteins, in full accordance with the CD spectra.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-03T19:08:49.969Z"}},{"start":38,"end":46,"reference_id":"34272906","reference_source":"pmid","reference_html":"The disordered PCI-binding human proteins CSNAP and DSS1 have diverged in structure and function. <i> Ruidiaz SF, Dreier JE, Hartmann-Petersen R, Kragelund BB. </i> Protein Sci, 2021","date":"2025-02-03T19:06:52.091Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0043130","term_name":"ubiquitin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP00617r005","statement":[{"text":"The region binding ubiquitin with the highest affinity, UBS1, was identified from a set of disappearing peaks originating from residues V38‐D46, combined with large CSPs from residues D35‐H37 (Figure 3b).","type":"Results"}],"term_comment":"","term_def":"\"Binding to ubiquitin, a protein that when covalently bound to other cellular proteins marks them for proteolytic degradation.\" [GOC:ecd]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_P60896","date":"2016-09-14T14:58:51.000Z","acc":"P60896","name":"26S proteasome complex subunit SEM1","length":70,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000000162C","genes":[{"name":{"value":"SEM1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:10845","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:10845"}}]},"synonyms":[{"value":"C7orf76"},{"value":"DSS1"},{"value":"SHFDG1"},{"value":"SHFM1"}]}],"alphafold_very_low_content":0.05714285714285714,"disorder_content":0.7285714285714285,"disprot_consensus":{"full":[{"start":1,"end":51,"type":"D"}],"Structural state":[{"start":1,"end":51,"type":"D"}],"Molecular function":[{"start":38,"end":46,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00534","name":"Glycosyl transferases group 1","start":294,"end":466},{"id":"PF15924","name":"ALG11 mannosyltransferase N-terminus","start":72,"end":274}],"gene3D":[{"start":289,"end":483,"id":"3.40.50.2000","name":"Glycogen Phosphorylase B;"}]},"uniref50":"UniRef50_P53954","sequence":"MGSAWTNYNFEEVKSHFGFKKYVVSSLVLVYGLIKVLTWIFRQWVYSSLNPFSKKSSLLNRAVASCGEKNVKVFGFFHPYCNAGGGGEKVLWKAVDITLRKDAKNVIVIYSGDFVNGENVTPENILNNVKAKFDYDLDSDRIFFISLKLRYLVDSSTWKHFTLIGQAIGSMILAFESIIQCPPDIWIDTMGYPFSYPIIARFLRRIPIVTYTHYPIMSKDMLNKLFKMPKKGIKVYGKILYWKVFMLIYQSIGSKIDIVITNSTWTNNHIKQIWQSNTCKIIYPPCSTEKLVDWKQKFGTAKGERLNQAIVLAQFRPEKRHKLIIESFATFLKNLPDSVSPIKLIMAGSTRSKQDENYVKSLQDWSENVLKIPKHLISFEKNLPFDKIEILLNKSTFGVNAMWNEHFGIAVVEYMASGLIPIVHASAGPLLDIVTPWDANGNIGKAPPQWELQKKYFAKLEDDGETTGFFFKEPSDPDYNTTKDPLRYPNLSDLFLQITKLDYDCLRVMGARNQQYSLYKFSDLKFDKDWENFVLNPICKLLEEEERG","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P53954","disprot_id":"DP00618","ncbi_taxon_id":559292,"regions_counter":20,"creator":"ktsirigos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":92,"region_id":"DP00618r001","released":"2022_03","ec_id":"ECO:0007719","reference_html":"Biochemical characterization, membrane association and identification of amino acids essential for the function of Alg11 from Saccharomyces cerevisiae, an alpha1,2-mannosyltransferase catalysing two sequential glycosylation steps in the formation of the lipid-linked core oligosaccharide. <i> Absmanner B, Schmeiser V, Kämpf M, Lehle L. </i> Biochem J, 2010","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":79,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19929855","version":2,"ec_name":"immunodetection assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":92,"term_name":"molecular function regulator","start":79,"ec_name":"immunodetection assay evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19929855","version":3,"reference_html":"Biochemical characterization, membrane association and identification of amino acids essential for the function of Alg11 from Saccharomyces cerevisiae, an alpha1,2-mannosyltransferase catalysing two sequential glycosylation steps in the formation of the lipid-linked core oligosaccharide. <i> Absmanner B, Schmeiser V, Kämpf M, Lehle L. </i> Biochem J, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0007719","region_id":"DP00618r002","curator_orcid":"0000-0001-5280-1107","ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":92,"term_name":"disorder to order","start":79,"ec_name":"immunodetection assay evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19929855","version":2,"reference_html":"Biochemical characterization, membrane association and identification of amino acids essential for the function of Alg11 from Saccharomyces cerevisiae, an alpha1,2-mannosyltransferase catalysing two sequential glycosylation steps in the formation of the lipid-linked core oligosaccharide. <i> Absmanner B, Schmeiser V, Kämpf M, Lehle L. </i> Biochem J, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0007719","region_id":"DP00618r003","curator_orcid":"0000-0001-5280-1107","ec_go":"IDA","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":92,"term_name":"protein binding","start":79,"ec_name":"immunodetection assay evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19929855","version":3,"reference_html":"Biochemical characterization, membrane association and identification of amino acids essential for the function of Alg11 from Saccharomyces cerevisiae, an alpha1,2-mannosyltransferase catalysing two sequential glycosylation steps in the formation of the lipid-linked core oligosaccharide. <i> Absmanner B, Schmeiser V, Kämpf M, Lehle L. </i> Biochem J, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007719","region_id":"DP00618r004","curator_orcid":"0000-0001-5280-1107","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":92,"region_id":"DP00618r005","released":"2022_03","ec_id":"ECO:0007719","reference_html":"Structures and mechanisms of glycosyltransferases. <i> Breton C, Snajdrová L, Jeanneau C, Koca J, Imberty A. </i> Glycobiology, 2006","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":79,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"16037492","version":2,"ec_name":"immunodetection assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":92,"term_name":"molecular function regulator","start":79,"ec_name":"immunodetection assay evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"16037492","version":3,"reference_html":"Structures and mechanisms of glycosyltransferases. <i> Breton C, Snajdrová L, Jeanneau C, Koca J, Imberty A. </i> Glycobiology, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0007719","region_id":"DP00618r006","curator_orcid":"0000-0001-5280-1107","ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":92,"term_name":"disorder to order","start":79,"ec_name":"immunodetection assay evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"16037492","version":2,"reference_html":"Structures and mechanisms of glycosyltransferases. <i> Breton C, Snajdrová L, Jeanneau C, Koca J, Imberty A. </i> Glycobiology, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0007719","region_id":"DP00618r007","curator_orcid":"0000-0001-5280-1107","ec_go":"IDA","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":92,"term_name":"protein binding","start":79,"ec_name":"immunodetection assay evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"16037492","version":3,"reference_html":"Structures and mechanisms of glycosyltransferases. <i> Breton C, Snajdrová L, Jeanneau C, Koca J, Imberty A. </i> Glycobiology, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007719","region_id":"DP00618r008","curator_orcid":"0000-0001-5280-1107","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":92,"region_id":"DP00618r009","released":"2022_03","ec_id":"ECO:0007719","reference_html":"Substrate-induced conformational changes in glycosyltransferases. <i> Qasba PK, Ramakrishnan B, Boeggeman E. </i> Trends Biochem Sci, 2005","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":79,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"15653326","version":2,"ec_name":"immunodetection assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":92,"term_name":"molecular function regulator","start":79,"ec_name":"immunodetection assay evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"15653326","version":3,"reference_html":"Substrate-induced conformational changes in glycosyltransferases. <i> Qasba PK, Ramakrishnan B, Boeggeman E. </i> Trends Biochem Sci, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0007719","region_id":"DP00618r010","curator_orcid":"0000-0001-5280-1107","ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":92,"term_name":"disorder to order","start":79,"ec_name":"immunodetection assay evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"15653326","version":2,"reference_html":"Substrate-induced conformational changes in glycosyltransferases. <i> Qasba PK, Ramakrishnan B, Boeggeman E. </i> Trends Biochem Sci, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0007719","region_id":"DP00618r011","curator_orcid":"0000-0001-5280-1107","ec_go":"IDA","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":92,"term_name":"protein binding","start":79,"ec_name":"immunodetection assay evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"15653326","version":3,"reference_html":"Substrate-induced conformational changes in glycosyltransferases. <i> Qasba PK, Ramakrishnan B, Boeggeman E. </i> Trends Biochem Sci, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007719","region_id":"DP00618r012","curator_orcid":"0000-0001-5280-1107","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":92,"region_id":"DP00618r013","released":"2022_03","ec_id":"ECO:0007719","reference_html":"Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases. <i> Hu Y, Chen L, Ha S, Gross B, Falcone B, Walker D, Mokhtarzadeh M, Walker S. </i> Proc Natl Acad Sci U S A, 2003","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":79,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"12538870","version":2,"ec_name":"immunodetection assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":92,"term_name":"molecular function regulator","start":79,"ec_name":"immunodetection assay evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"12538870","version":3,"reference_html":"Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases. <i> Hu Y, Chen L, Ha S, Gross B, Falcone B, Walker D, Mokhtarzadeh M, Walker S. </i> Proc Natl Acad Sci U S A, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0007719","region_id":"DP00618r014","curator_orcid":"0000-0001-5280-1107","ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":92,"term_name":"disorder to order","start":79,"ec_name":"immunodetection assay evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"12538870","version":2,"reference_html":"Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases. <i> Hu Y, Chen L, Ha S, Gross B, Falcone B, Walker D, Mokhtarzadeh M, Walker S. </i> Proc Natl Acad Sci U S A, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0007719","region_id":"DP00618r015","curator_orcid":"0000-0001-5280-1107","ec_go":"IDA","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":92,"term_name":"protein binding","start":79,"ec_name":"immunodetection assay evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"12538870","version":3,"reference_html":"Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases. <i> Hu Y, Chen L, Ha S, Gross B, Falcone B, Walker D, Mokhtarzadeh M, Walker S. </i> Proc Natl Acad Sci U S A, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007719","region_id":"DP00618r016","curator_orcid":"0000-0001-5280-1107","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":92,"region_id":"DP00618r017","released":"2022_03","ec_id":"ECO:0007719","reference_html":"Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily. <i> Wrabl JO, Grishin NV. </i> J Mol Biol, 2001","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":79,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"11846551","version":2,"ec_name":"immunodetection assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":92,"term_name":"molecular function regulator","start":79,"ec_name":"immunodetection assay evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"11846551","version":3,"reference_html":"Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily. <i> Wrabl JO, Grishin NV. </i> J Mol Biol, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0007719","region_id":"DP00618r018","curator_orcid":"0000-0001-5280-1107","ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":92,"term_name":"disorder to order","start":79,"ec_name":"immunodetection assay evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"11846551","version":2,"reference_html":"Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily. <i> Wrabl JO, Grishin NV. </i> J Mol Biol, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0007719","region_id":"DP00618r019","curator_orcid":"0000-0001-5280-1107","ec_go":"IDA","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":92,"term_name":"protein binding","start":79,"ec_name":"immunodetection assay evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"11846551","version":3,"reference_html":"Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily. <i> Wrabl JO, Grishin NV. </i> J Mol Biol, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007719","region_id":"DP00618r020","curator_orcid":"0000-0001-5280-1107","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P53954","date":"2016-09-09T09:03:43.000Z","acc":"P53954","name":"GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase","length":548,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000125849","genes":[{"name":{"value":"ALG11"},"orfNames":[{"value":"N2510"},{"value":"YNL2510W"}],"olnNames":[{"value":"YNL048W"}]}],"alphafold_very_low_content":0.023722627737226276,"disorder_content":0.025547445255474453,"disprot_consensus":{"full":[{"start":79,"end":92,"type":"T"}],"Structural state":[{"start":79,"end":92,"type":"D"}],"Molecular function":[{"start":79,"end":92,"type":"F"}],"Structural transition":[{"start":79,"end":92,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00266","name":"Aminotransferase class-V","start":20,"end":416}],"gene3D":[{"start":77,"end":282,"id":"3.40.640.10","name":"Type I PLP-dependent aspartate aminotransferase-like (Major domain)"},{"start":20,"end":422,"id":"3.90.1150.10","name":"Aspartate Aminotransferase, domain 1"},{"start":31,"end":326,"id":"1.10.260.50","name":"1.10.260.50"}]},"uniref50":"UniRef50_Q9JLI6","sequence":"MDVARNGARGSVESPPNRKVYMDYNATTPLEPEVIQAVTEAMKEAWGNPSSSYVAGRKAKDIINTARASLAKMIGGKPQDIIFTSGGTESNNLVIHSTVRCFHEQQTLQGRTVDQISPEEGTRPHFITCTVEHDSIRLPLEHLVEDQVAEVTFVPVSKVNGQVEVEDILAAVRPTTCLVTIMLANNETGVIMPISEISRRIKALNQIRAASGLPRVLVHTDAAQALGKRRVDVEDLGVDFLTIVGHKFYGPRIGALYVRGVGKLTPLYPMLFGGGQERNFRPGTENTPMIAGLGKAADLVSENCETYEAHMRDIRDYLEERLEAEFGKRIHLNSRFPGVERLPNTCNFSIQGSQLRGYMVLAQCQTLLASVGASCHSDHEDRPSPVLLSCGIPVDVARNAVRLSVGRSTTRAEVDLIVQDLKQAVNQLEGPV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_Q9JLI6","disprot_id":"DP00620","ncbi_taxon_id":10116,"regions_counter":2,"creator":"ktsirigos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":392,"region_id":"DP00620r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Reaction mechanism and molecular basis for selenium/sulfur discrimination of selenocysteine lyase. <i> Omi R, Kurokawa S, Mihara H, Hayashi H, Goto M, Miyahara I, Kurihara T, Hirotsu K, Esaki N. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":374,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"20164179","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":392,"term_name":"disorder to order","start":374,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"20164179","version":2,"reference_html":"Reaction mechanism and molecular basis for selenium/sulfur discrimination of selenocysteine lyase. <i> Omi R, Kurokawa S, Mihara H, Hayashi H, Goto M, Miyahara I, Kurihara T, Hirotsu K, Esaki N. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00620r002","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2016_10","uniref100":"UniRef100_Q68FT9","date":"2016-09-09T09:54:01.000Z","acc":"Q68FT9","name":"Selenocysteine lyase","length":432,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI00001D02E0","genes":[{"name":{"value":"Scly"}}],"alphafold_very_low_content":0.05555555555555555,"disorder_content":0.04398148148148148,"disprot_consensus":{"full":[{"start":374,"end":392,"type":"T"}],"Structural state":[{"start":374,"end":392,"type":"D"}],"Structural transition":[{"start":374,"end":392,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00084","name":"Sushi repeat (SCR repeat)","start":309,"end":371},{"id":"PF00084","name":"Sushi repeat (SCR repeat)","start":376,"end":439},{"id":"PF00089","name":"Trypsin","start":464,"end":697},{"id":"PF00431","name":"CUB domain","start":25,"end":126},{"id":"PF00431","name":"CUB domain","start":193,"end":302},{"id":"PF14670","name":"Coagulation Factor Xa inhibitory site","start":160,"end":189}],"gene3D":[{"start":193,"end":304,"id":"2.60.120.290","name":"Spermadhesin, CUB domain"},{"start":22,"end":141,"id":"2.60.120.290","name":"Spermadhesin, CUB domain"},{"start":375,"end":450,"id":"2.10.70.10","name":"Complement Module, domain 1"},{"start":142,"end":192,"id":"2.10.25.10","name":"Laminin"},{"start":307,"end":373,"id":"2.10.70.10","name":"Complement Module, domain 1"},{"start":464,"end":691,"id":"2.40.10.10","name":"Trypsin-like serine proteases"},{"start":476,"end":698,"id":"2.40.10.10","name":"Trypsin-like serine proteases"}]},"uniref50":"UniRef50_P00736","sequence":"MWLLYLLVPALFCRAGGSIPIPQKLFGEVTSPLFPKPYPNNFETTTVITVPTGYRVKLVFQQFDLEPSEGCFYDYVKISADKKSLGRFCGQLGSPLGNPPGKKEFMSQGNKMLLTFHTDFSNEENGTIMFYKGFLAYYQAVDLDECASRSKSGEEDPQPQCQHLCHNYVGGYFCSCRPGYELQEDTHSCQAECSSELYTEASGYISSLEYPRSYPPDLRCNYSIRVERGLTLHLKFLEPFDIDDHQQVHCPYDQLQIYANGKNIGEFCGKQRPPDLDTSSNAVDLLFFTDESGDSRGWKLRYTTEIIKCPQPKTLDEFTIIQNLQPQYQFRDYFIATCKQGYQLIEGNQVLHSFTAVCQDDGTWHRAMPRCKIKDCGQPRNLPNGDFRYTTTMGVNTYKARIQYYCHEPYYKMQTRAGSRESEQGVYTCTAQGIWKNEQKGEKIPRCLPVCGKPVNPVEQRQRIIGGQKAKMGNFPWQVFTNIHGRGGGALLGDRWILTAAHTLYPKEHEAQSNASLDVFLGHTNVEELMKLGNHPIRRVSVHPDYRQDESYNFEGDIALLELENSVTLGPNLLPICLPDNDTFYDLGLMGYVSGFGVMEEKIAHDLRFVRLPVANPQACENWLRGKNRMDVFSQNMFCAGHPSLKQDACQGDSGGVFAVRDPNTDRWVATGIVSWGIGCSRGYGFYTKVLNYVDWIKKEMEEED","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P00736","disprot_id":"DP00621","ncbi_taxon_id":9606,"regions_counter":6,"creator":"ktsirigos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":305,"region_id":"DP00621r001","released":"2022_03","ec_id":"ECO:0006196","reference_html":"Calcium-dependent conformational flexibility of a CUB domain controls activation of the complement serine protease C1r. <i> Major B, Kardos J, Kékesi KA, Lorincz Z, Závodszky P, Gál P. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":193,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"20178990","version":2,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":305,"term_name":"molecular sequestering activity","start":193,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"20178990","version":3,"reference_html":"Calcium-dependent conformational flexibility of a CUB domain controls activation of the complement serine protease C1r. <i> Major B, Kardos J, Kékesi KA, Lorincz Z, Závodszky P, Gál P. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140313","ec_id":"ECO:0006196","region_id":"DP00621r002","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":305,"term_name":"disorder to order","start":193,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"20178990","version":2,"reference_html":"Calcium-dependent conformational flexibility of a CUB domain controls activation of the complement serine protease C1r. <i> Major B, Kardos J, Kékesi KA, Lorincz Z, Závodszky P, Gál P. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006196","region_id":"DP00621r003","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":305,"region_id":"DP00621r004","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Calcium-dependent conformational flexibility of a CUB domain controls activation of the complement serine protease C1r. <i> Major B, Kardos J, Kékesi KA, Lorincz Z, Závodszky P, Gál P. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":193,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"20178990","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":305,"term_name":"molecular sequestering activity","start":193,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"20178990","version":3,"reference_html":"Calcium-dependent conformational flexibility of a CUB domain controls activation of the complement serine protease C1r. <i> Major B, Kardos J, Kékesi KA, Lorincz Z, Závodszky P, Gál P. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140313","ec_id":"ECO:0006204","region_id":"DP00621r005","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":305,"term_name":"disorder to order","start":193,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"20178990","version":2,"reference_html":"Calcium-dependent conformational flexibility of a CUB domain controls activation of the complement serine protease C1r. <i> Major B, Kardos J, Kékesi KA, Lorincz Z, Závodszky P, Gál P. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00621r006","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2016_10","uniref100":"UniRef100_P00736","date":"2016-09-09T10:46:32.000Z","acc":"P00736","name":"Complement C1r subcomponent","length":705,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000186C8D3","genes":[{"name":{"value":"C1R"}}],"alphafold_very_low_content":0.0425531914893617,"disorder_content":0.16028368794326242,"disprot_consensus":{"full":[{"start":193,"end":305,"type":"T"}],"Structural state":[{"start":193,"end":305,"type":"D"}],"Molecular function":[{"start":193,"end":305,"type":"F"}],"Structural transition":[{"start":193,"end":305,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00957","name":"Synaptobrevin","start":31,"end":111}]},"uniref50":"UniRef50_P63044","sequence":"MSATAATVPPAAPAGEGGPPAPPPNLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAAKLKRKYWWKNLKMMIILGVICAIILIIIIVYFST","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_P63044","disprot_id":"DP00622","ncbi_taxon_id":10116,"regions_counter":15,"creator":"ktsirigos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":35,"region_id":"DP00622r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation. <i> Ellena JF, Liang B, Wiktor M, Stein A, Cafiso DS, Jahn R, Tamm LK. </i> Proc Natl Acad Sci U S A, 2009","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":1,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19918058","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":35,"term_name":"molecular adaptor activity","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19918058","version":3,"reference_html":"Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation. <i> Ellena JF, Liang B, Wiktor M, Stein A, Cafiso DS, Jahn R, Tamm LK. </i> Proc Natl Acad Sci U S A, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP00622r002","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":35,"term_name":"lipid binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19918058","version":3,"reference_html":"Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation. <i> Ellena JF, Liang B, Wiktor M, Stein A, Cafiso DS, Jahn R, Tamm LK. </i> Proc Natl Acad Sci U S A, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008289","ec_id":"ECO:0006165","region_id":"DP00622r003","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":54,"region_id":"DP00622r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation. <i> Ellena JF, Liang B, Wiktor M, Stein A, Cafiso DS, Jahn R, Tamm LK. </i> Proc Natl Acad Sci U S A, 2009","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":36,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19918058","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":54,"term_name":"molecular adaptor activity","start":36,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19918058","version":3,"reference_html":"Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation. <i> Ellena JF, Liang B, Wiktor M, Stein A, Cafiso DS, Jahn R, Tamm LK. </i> Proc Natl Acad Sci U S A, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP00622r005","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":54,"term_name":"disorder to order","start":36,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19918058","version":2,"reference_html":"Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation. <i> Ellena JF, Liang B, Wiktor M, Stein A, Cafiso DS, Jahn R, Tamm LK. </i> Proc Natl Acad Sci U S A, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00622r006","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":54,"term_name":"lipid binding","start":36,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19918058","version":3,"reference_html":"Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation. <i> Ellena JF, Liang B, Wiktor M, Stein A, Cafiso DS, Jahn R, Tamm LK. </i> Proc Natl Acad Sci U S A, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008289","ec_id":"ECO:0006165","region_id":"DP00622r007","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":76,"region_id":"DP00622r008","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation. <i> Ellena JF, Liang B, Wiktor M, Stein A, Cafiso DS, Jahn R, Tamm LK. </i> Proc Natl Acad Sci U S A, 2009","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":55,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19918058","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":76,"term_name":"molecular adaptor activity","start":55,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19918058","version":3,"reference_html":"Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation. <i> Ellena JF, Liang B, Wiktor M, Stein A, Cafiso DS, Jahn R, Tamm LK. </i> Proc Natl Acad Sci U S A, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP00622r009","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":76,"term_name":"lipid binding","start":55,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19918058","version":3,"reference_html":"Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation. <i> Ellena JF, Liang B, Wiktor M, Stein A, Cafiso DS, Jahn R, Tamm LK. </i> Proc Natl Acad Sci U S A, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008289","ec_id":"ECO:0006165","region_id":"DP00622r010","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":88,"region_id":"DP00622r011","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation. <i> Ellena JF, Liang B, Wiktor M, Stein A, Cafiso DS, Jahn R, Tamm LK. </i> Proc Natl Acad Sci U S A, 2009","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":77,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19918058","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":88,"term_name":"molecular adaptor activity","start":77,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19918058","version":3,"reference_html":"Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation. <i> Ellena JF, Liang B, Wiktor M, Stein A, Cafiso DS, Jahn R, Tamm LK. </i> Proc Natl Acad Sci U S A, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP00622r012","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":88,"term_name":"disorder to order","start":77,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19918058","version":2,"reference_html":"Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation. <i> Ellena JF, Liang B, Wiktor M, Stein A, Cafiso DS, Jahn R, Tamm LK. </i> Proc Natl Acad Sci U S A, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00622r013","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":88,"term_name":"lipid binding","start":77,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19918058","version":3,"reference_html":"Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation. <i> Ellena JF, Liang B, Wiktor M, Stein A, Cafiso DS, Jahn R, Tamm LK. </i> Proc Natl Acad Sci U S A, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008289","ec_id":"ECO:0006165","region_id":"DP00622r014","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":2,"end":24,"reference_id":"9759724","reference_source":"pmid","reference_html":"Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. <i> Sutton RB, Fasshauer D, Jahn R, Brunger AT. </i> Nature, 1998","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"region_id":"DP00622r015","statement":[{"text":"The final model contains residues: Sb 25–93, Sx 188–259, Sn1 7–83 and Sn2 131–204 for complex I; Sb 28–96, Sx 189–261, Sn1 12–83 and Sn2 132–203 for complex II; Sb 26–94, Sx 186–259, Sn1 11–83 and Sn2 132–204 for complex III; 19 water molecules; 13 Sr2+ ions; and 7 MPD molecules.","type":"Methods"},{"text":"The N-terminal region of synaptobrevin (Sb) not visible in the crystal structure spans residues 2-24 in chain A and 2-27 in chain B.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P63044","date":"2016-09-09T11:04:37.000Z","acc":"P63045","name":"Vesicle-associated membrane protein 2","length":116,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI00000041E4","genes":[{"name":{"value":"Vamp2"},"synonyms":[{"value":"Syb2"}]}],"alphafold_very_low_content":0.034482758620689655,"disorder_content":0.7586206896551724,"disprot_consensus":{"full":[{"start":1,"end":35,"type":"D"},{"start":36,"end":54,"type":"T"},{"start":55,"end":76,"type":"D"},{"start":77,"end":88,"type":"T"}],"Structural state":[{"start":1,"end":88,"type":"D"}],"Molecular function":[{"start":1,"end":88,"type":"F"}],"Structural transition":[{"start":36,"end":54,"type":"T"},{"start":77,"end":88,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00046","name":"Homeodomain","start":296,"end":352}]},"uniref50":"UniRef50_P83949","sequence":"MNSYFEQASGFYGHPHQATGMAMGSGGHHDQTASAAAAAYRGFPLSLGMSPYANHHLQRTTQDSPYDASITAACNKIYGDGAGAYKQDCLNIKADAVNGYKDIWNTGGSNGGGGGGGGGGGGGAGGTGGAGNANGGNAANANGQNNPAGGMPVRPSACTPDSRVGGYLDTSGGSPVSHRGGSAGGNVSVSGGNGNAGGVQSGVGVAGAGTAWNANCTISGAAAQTAAASSLHQASNHTFYPWMAIAGECPEDPTKSKIRSDLTQYGGISTDMGKRYSESLAGSLLPDWLGTNGLRRRGRQTYTRYQTLELEKEFHTNHYLTRRRRIEMAHALCLTERQIKIWFQNRRMKLKKEIQAIKELNEQEKQAQAQKAAAAAAAAAAVQGGHLDQ","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_P83949","disprot_id":"DP00623","ncbi_taxon_id":7227,"regions_counter":6,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":174,"region_id":"DP00623r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Multiple intrinsically disordered sequences alter DNA binding by the homeodomain of the Drosophila hox protein ultrabithorax. <i> Liu Y, Matthews KS, Bondos SE. </i> J Biol Chem, 2008","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18508761","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":174,"term_name":"molecular function regulator","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18508761","version":3,"reference_html":"Multiple intrinsically disordered sequences alter DNA binding by the homeodomain of the Drosophila hox protein ultrabithorax. <i> Liu Y, Matthews KS, Bondos SE. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006204","region_id":"DP00623r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":286,"region_id":"DP00623r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Multiple intrinsically disordered sequences alter DNA binding by the homeodomain of the Drosophila hox protein ultrabithorax. <i> Liu Y, Matthews KS, Bondos SE. </i> J Biol Chem, 2008","term_id":"IDPO:0000002","curator_id":"fquaglia","start":235,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18508761","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":286,"term_name":"molecular function regulator","start":235,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18508761","version":3,"reference_html":"Multiple intrinsically disordered sequences alter DNA binding by the homeodomain of the Drosophila hox protein ultrabithorax. <i> Liu Y, Matthews KS, Bondos SE. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006204","region_id":"DP00623r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":216,"region_id":"DP00623r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Multiple intrinsically disordered sequences alter DNA binding by the homeodomain of the Drosophila hox protein ultrabithorax. <i> Liu Y, Matthews KS, Bondos SE. </i> J Biol Chem, 2008","term_id":"IDPO:0000002","curator_id":"fquaglia","start":174,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18508761","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":216,"term_name":"molecular function regulator","start":174,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18508761","version":3,"reference_html":"Multiple intrinsically disordered sequences alter DNA binding by the homeodomain of the Drosophila hox protein ultrabithorax. <i> Liu Y, Matthews KS, Bondos SE. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006204","region_id":"DP00623r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P83949","date":"2016-08-16T14:29:41.000Z","acc":"P83949","name":"Homeotic protein ultrabithorax","length":389,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI00001245A6","genes":[{"name":{"value":"Ubx"},"orfNames":[{"value":"CG10388"}]}],"alphafold_very_low_content":0.6709511568123393,"disorder_content":0.6889460154241646,"disprot_consensus":{"full":[{"start":1,"end":216,"type":"D"},{"start":235,"end":286,"type":"D"}],"Structural state":[{"start":1,"end":216,"type":"D"},{"start":235,"end":286,"type":"D"}],"Molecular function":[{"start":1,"end":216,"type":"F"},{"start":235,"end":286,"type":"F"}]}},{"features":{"pfam":[{"id":"PF07716","name":"Basic region leucine zipper","start":103,"end":151}],"gene3D":[{"start":117,"end":161,"id":"1.20.5.170","name":"1.20.5.170"}]},"uniref50":"UniRef50_P35638","sequence":"MAAESLPFSFGTLSSWELEAWYEDLQEVLSSDENGGTYVSPPGNEEEESKIFTTLDPASLAWLTEEEPEPAEVTSTSQSPHSPDSSQSSLAQEEEEEDQGRTRKRKQSGHSPARAGKQRMKEKEQENERKVAQLAEENERLKQEIERLTREVEATRRALIDRMVNLHQA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P35638","disprot_id":"DP00624","ncbi_taxon_id":9606,"regions_counter":10,"creator":"grivas","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":168,"region_id":"DP00624r001","released":"2025_12","ec_id":"ECO:0006165","reference_html":"Intrinsically disordered human C/EBP homologous protein regulates biological activity of colon cancer cells during calcium stress. <i> Singh VK, Pacheco I, Uversky VN, Smith SP, MacLeod RJ, Jia Z. </i> J Mol Biol, 2008","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18534616","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2025-10-15T15:23:16.446Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The lack of upfield-shifted resonances associated with methyl protons and very little dispersion in the amide proton region of the 1D 1H spectrum of CHOP, shown in Fig. 2A, suggest that CHOP comprises very little globular structure. Analysis of 1H-15N HSQC spectrum of CHOP revealed well-resolved backbone amide resonances for 81 of the expected 168 backbone 1H-15N correlations, which fell between 7.0 and 8.8 ppm (Fig. 2B).","type":"Results"}]},{"term_namespace":"Biological process","reference_source":"pmid","ec_ontology":"ECO","end":168,"term_name":"regulation of transcription by RNA polymerase II","start":1,"ec_name":"quantitative reverse transcription polymerase chain reaction evidence used in manual assertion","curator_id":"vnugnes","released":"2025_12","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"18534616","version":4,"reference_html":"Intrinsically disordered human C/EBP homologous protein regulates biological activity of colon cancer cells during calcium stress. <i> Singh VK, Pacheco I, Uversky VN, Smith SP, MacLeod RJ, Jia Z. </i> J Mol Biol, 2008","date":"2025-10-15T15:56:38.297Z","term_id":"GO:0006357","ec_id":"ECO:0001567","region_id":"DP00624r002","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II.\" [GOC:go_curators, GOC:txnOH]","disprot_namespace":"Disorder function","term_is_binding":true,"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0320","entry_name":"HT 29"}],"statement":[{"text":"Overexpression of full-length CHOP increased the amount of β-catenin reporter inhibition in the presence of CaSR activation (%inhibition of activity in 5 μM Ca2+: 78 ± 5 vs 60 ± 4, p<0.05, n=6, Fig.6D). Overexpression of CHOP101−168 in the presence of CaSR activation did not change the amount of inhibition of the β-catenin reporter (% inhibition: 56 ± 6 vs 60 ± 4, NS, n=6).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":168,"region_id":"DP00624r004","released":"2025_12","ec_id":"ECO:0006206","reference_html":"Intrinsically disordered human C/EBP homologous protein regulates biological activity of colon cancer cells during calcium stress. <i> Singh VK, Pacheco I, Uversky VN, Smith SP, MacLeod RJ, Jia Z. </i> J Mol Biol, 2008","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18534616","version":3,"ec_name":"near-UV circular dichroism evidence used in manual assertion","date":"2025-10-15T15:24:17.835Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":" The fact that this is not the case for CHOP suggests that Trp18, Trp23, and Trp64 are located in the relatively symmetric environment and/or relatively accessible to solvent, indicating they are located in relatively flexible region.","type":"Results"}]},{"start":1,"end":120,"reference_id":"18534616","reference_source":"pmid","reference_html":"Intrinsically disordered human C/EBP homologous protein regulates biological activity of colon cancer cells during calcium stress. <i> Singh VK, Pacheco I, Uversky VN, Smith SP, MacLeod RJ, Jia Z. </i> J Mol Biol, 2008","date":"2025-10-15T15:25:08.870Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"region_id":"DP00624r007","statement":[{"text":"This hypothesis is supported by the red-shifted maximum of the intrinsic fluorescence, λmax=345 nm (Fig. 3B). In fact, it is known that a tryptophan emission maximum is highly dependent on the polarity of its environment. A tryptophan residue in a non-polar environment (i.e., buried inside a protein), has an emission maximum close to 320 nm, while in a polar environment (i.e., solvent exposed) it has an emission maximum close to 350 nm, so-called Stokes shift 41.","type":"Curator statement"}]},{"start":1,"end":168,"reference_id":"18534616","reference_source":"pmid","reference_html":"Intrinsically disordered human C/EBP homologous protein regulates biological activity of colon cancer cells during calcium stress. <i> Singh VK, Pacheco I, Uversky VN, Smith SP, MacLeod RJ, Jia Z. </i> J Mol Biol, 2008","date":"2025-10-15T15:30:42.827Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"region_id":"DP00624r008","statement":[{"text":"The elution peaks observed for full-length CHOP correspond to RS of 44.7 and 72.8 Å while CHOP101−168 peak correspond to 32.3 Å.","type":"Results"},{"text":"If the elution peaks of full-length CHOP and CHOP101−168 are attributed to pre-molten globules, then the corresponding molecular masses are 163.8 kDa and 48.7 kDa for CHOP and 21.8 kDa for the CHOP101−168.","type":"Results"}]},{"start":1,"end":168,"reference_id":"18534616","reference_source":"pmid","reference_html":"Intrinsically disordered human C/EBP homologous protein regulates biological activity of colon cancer cells during calcium stress. <i> Singh VK, Pacheco I, Uversky VN, Smith SP, MacLeod RJ, Jia Z. </i> J Mol Biol, 2008","date":"2025-10-15T15:43:46.029Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042802","term_name":"identical protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P35638","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00624r009","statement":[{"text":"Fitting of the AUC data of CHOP resulted in no distinct peaks because of the large range of species of apparently high molecular mass, suggesting multiple oligomeric forms (data not shown). Conversely, when AUC data of CHOP101−168 were evaluated by a continuous distribution c(S) Lamm equation model, two distinct peaks (1.13S and 2.20 S) were observed (Fig. 4C). Integrating the c(M) distribution, SEDFIT 46 estimated these two peaks with median values of 9.9 kDa, 23.4% of total population and 24.3 kDa, 68% of total population, respectively suggesting a large population of apparent dimer and a small population of monomer. Altogether, these data suggest that when N-terminal region of CHOP is deleted, it can no longer make large oligomers.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein or proteins.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_P35638","date":"2016-08-26T14:31:17.000Z","acc":"P35638","name":"DNA damage-inducible transcript 3 protein","length":169,"organism":"Homo sapiens","dataset":["Autophagy-related proteins","Cancer-related proteins","Stress response proteins"],"UniParc":"UPI0000000C56","genes":[{"name":{"value":"DDIT3"},"synonyms":[{"value":"CHOP"},{"value":"CHOP10"},{"value":"GADD153"}]}],"alphafold_very_low_content":0.30177514792899407,"disorder_content":0.9940828402366864,"disprot_consensus":{"full":[{"start":1,"end":168,"type":"D"}],"Structural state":[{"start":1,"end":168,"type":"D"}],"Biological process":[{"start":1,"end":168,"type":"F"}],"Molecular function":[{"start":1,"end":168,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05182","name":"Fip1 motif","start":180,"end":220}]},"uniref50":"UniRef50_P45976","sequence":"MSSSEDEDDKFLYGSDSELALPSSKRSRDDEADAGASSNPDIVKRQKFDSPVEETPATARDDRSDEDIYSDSSDDDSDSDLEVIISLGPDPTRLDAKLLDSYSTAATSSSKDVISVATDVSNTITKTSDERLITEGEANQGVTATTVKATESDGNVPKAMTGSIDLDKEGIFDSVGITTIDPEVLKEKPWRQPGANLSDYFNYGFNEFTWMEYLHRQEKLQQDYNPRRILMGLLSLQQQGKLNSANDTDSNLGNIIDNNNNVNNANMSNLNSNMGNSMSGTPNPPAPPMHPSFPPLPMFGSFPPFPMPGMMPPMNQQPNQNQNQNSK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P45976","disprot_id":"DP00625","ncbi_taxon_id":559292,"regions_counter":9,"creator":"ktsirigos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":195,"region_id":"DP00625r001","released":"2022_03","ec_id":"ECO:0006206","reference_html":"Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein. <i> Meinke G, Ezeokonkwo C, Balbo P, Stafford W, Moore C, Bohm A. </i> Biochemistry, 2008","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":80,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"18537269","version":2,"ec_name":"near-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":195,"term_name":"disorder to order","start":80,"ec_name":"near-UV circular dichroism evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"18537269","version":2,"reference_html":"Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein. <i> Meinke G, Ezeokonkwo C, Balbo P, Stafford W, Moore C, Bohm A. </i> Biochemistry, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006206","region_id":"DP00625r002","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":195,"term_name":"protein binding","start":80,"ec_name":"near-UV circular dichroism evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"18537269","version":3,"reference_html":"Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein. <i> Meinke G, Ezeokonkwo C, Balbo P, Stafford W, Moore C, Bohm A. </i> Biochemistry, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006206","region_id":"DP00625r003","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":195,"region_id":"DP00625r004","released":"2022_03","ec_id":"ECO:0006275","reference_html":"Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein. <i> Meinke G, Ezeokonkwo C, Balbo P, Stafford W, Moore C, Bohm A. </i> Biochemistry, 2008","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":80,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"18537269","version":2,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":195,"term_name":"disorder to order","start":80,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"18537269","version":2,"reference_html":"Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein. <i> Meinke G, Ezeokonkwo C, Balbo P, Stafford W, Moore C, Bohm A. </i> Biochemistry, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006275","region_id":"DP00625r005","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":195,"term_name":"protein binding","start":80,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"18537269","version":3,"reference_html":"Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein. <i> Meinke G, Ezeokonkwo C, Balbo P, Stafford W, Moore C, Bohm A. </i> Biochemistry, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006275","region_id":"DP00625r006","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":195,"region_id":"DP00625r007","released":"2022_03","ec_id":"ECO:0007064","reference_html":"Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein. <i> Meinke G, Ezeokonkwo C, Balbo P, Stafford W, Moore C, Bohm A. </i> Biochemistry, 2008","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":80,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"18537269","version":2,"ec_name":"dynamic light scattering assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":195,"term_name":"disorder to order","start":80,"ec_name":"dynamic light scattering assay evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"18537269","version":2,"reference_html":"Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein. <i> Meinke G, Ezeokonkwo C, Balbo P, Stafford W, Moore C, Bohm A. </i> Biochemistry, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0007064","region_id":"DP00625r008","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":195,"term_name":"protein binding","start":80,"ec_name":"dynamic light scattering assay evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"18537269","version":3,"reference_html":"Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein. <i> Meinke G, Ezeokonkwo C, Balbo P, Stafford W, Moore C, Bohm A. </i> Biochemistry, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007064","region_id":"DP00625r009","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P45976","date":"2016-09-09T12:03:39.000Z","acc":"P45976","name":"Pre-mRNA polyadenylation factor FIP1","length":327,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000052DD8","genes":[{"name":{"value":"FIP1"},"orfNames":[{"value":"J1911"}],"olnNames":[{"value":"YJR093C"}]}],"alphafold_very_low_content":0.27217125382262997,"disorder_content":0.3547400611620795,"disprot_consensus":{"full":[{"start":80,"end":195,"type":"T"}],"Structural state":[{"start":80,"end":195,"type":"D"}],"Structural transition":[{"start":80,"end":195,"type":"T"}],"Molecular function":[{"start":80,"end":195,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00717","name":"Peptidase S24-like","start":16,"end":132}],"gene3D":[{"start":25,"end":139,"id":"2.10.109.10","name":"Umud Fragment, subunit A"}]},"uniref50":"UniRef50_P0AG12","sequence":"MLFIKPADLREIVTFPLFSDLVQCGFPSPAADYVEQRIDLNQLLIQHPSATYFVKASGDSMIDGGISDGDLLIVDSAITASHGDIVIAAVDGEFTVKKLQLRPTVQLIPMNSAYSPITISSEDTLDVFGVVIHVVKAMR","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0AG12","disprot_id":"DP00626","ncbi_taxon_id":83333,"regions_counter":4,"creator":"ktsirigos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":139,"region_id":"DP00626r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Regulation of Escherichia coli SOS mutagenesis by dimeric intrinsically disordered umuD gene products. <i> Simon SM, Sousa FJ, Mohana-Borges R, Walker GC. </i> Proc Natl Acad Sci U S A, 2008","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":1,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"18216271","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":139,"term_name":"molecular function regulator","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"18216271","version":3,"reference_html":"Regulation of Escherichia coli SOS mutagenesis by dimeric intrinsically disordered umuD gene products. <i> Simon SM, Sousa FJ, Mohana-Borges R, Walker GC. </i> Proc Natl Acad Sci U S A, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006204","region_id":"DP00626r002","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":139,"term_name":"molten globule to order","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"18216271","version":2,"reference_html":"Regulation of Escherichia coli SOS mutagenesis by dimeric intrinsically disordered umuD gene products. <i> Simon SM, Sousa FJ, Mohana-Borges R, Walker GC. </i> Proc Natl Acad Sci U S A, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000012","ec_id":"ECO:0006204","region_id":"DP00626r003","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":139,"term_name":"nucleic acid binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"18216271","version":3,"reference_html":"Regulation of Escherichia coli SOS mutagenesis by dimeric intrinsically disordered umuD gene products. <i> Simon SM, Sousa FJ, Mohana-Borges R, Walker GC. </i> Proc Natl Acad Sci U S A, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006204","region_id":"DP00626r004","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P0AG12","date":"2016-09-09T11:15:22.000Z","acc":"P0AG11","name":"Protein UmuD","length":139,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI0000137C35","genes":[{"name":{"value":"umuD"},"olnNames":[{"value":"b1183"},{"value":"JW1172"}]}],"alphafold_very_low_content":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":139,"type":"T"}],"Structural state":[{"start":1,"end":139,"type":"D"}],"Molecular function":[{"start":1,"end":139,"type":"F"}],"Structural transition":[{"start":1,"end":139,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00328","name":"Histidine phosphatase superfamily (branch 2)","start":34,"end":331}],"gene3D":[{"start":33,"end":386,"id":"3.40.50.1240","name":"Phosphoglycerate mutase-like"}]},"uniref50":"UniRef50_P15309","sequence":"MRAAPLLLARAASLSLGFLFLLFFWLDRSVLAKELKFVTLVFRHGDRSPIDTFPTDPIKESSWPQGFGQLTQLGMEQHYELGEYIRKRYRKFLNESYKHEQVYIRSTDVDRTLMSAMTNLAALFPPEGVSIWNPILLWQPIPVHTVPLSEDQLLYLPFRNCPRFQELESETLKSEEFQKRLHPYKDFIATLGKLSGLHGQDLFGIWSKVYDPLYCESVHNFTLPSWATEDTMTKLRELSELSLLSLYGIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMYSAHDTTVSGLQMALDVYNGLLPPYASCHLTELYFEKGEYFVEMYYRNETQHEPYPLMLPGCSPSCPLERFAELVGPVIPQDWSTECMTTNSHQGTEDSTD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P15309","disprot_id":"DP00628","ncbi_taxon_id":9606,"regions_counter":3,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":286,"region_id":"DP00628r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR structure in a membrane environment reveals putative amyloidogenic regions of the SEVI precursor peptide PAP(248-286). <i> Nanga RP, Brender JR, Vivekanandan S, Popovych N, Ramamoorthy A. </i> J Am Chem Soc, 2009","term_id":"IDPO:0000002","curator_id":"fquaglia","start":248,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19995078","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":286,"term_name":"molecular adaptor activity","start":248,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19995078","version":3,"reference_html":"NMR structure in a membrane environment reveals putative amyloidogenic regions of the SEVI precursor peptide PAP(248-286). <i> Nanga RP, Brender JR, Vivekanandan S, Popovych N, Ramamoorthy A. </i> J Am Chem Soc, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP00628r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":286,"term_name":"disorder to order","start":248,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19995078","version":2,"reference_html":"NMR structure in a membrane environment reveals putative amyloidogenic regions of the SEVI precursor peptide PAP(248-286). <i> Nanga RP, Brender JR, Vivekanandan S, Popovych N, Ramamoorthy A. </i> J Am Chem Soc, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00628r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2016_10","uniref100":"UniRef100_P15309","date":"2016-08-16T14:59:39.000Z","acc":"P15309","name":"Prostatic acid phosphatase","length":386,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000016AE62","genes":[{"name":{"value":"ACP3","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:125","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:125"}}]},"synonyms":[{"value":"ACPP"}]}],"alphafold_very_low_content":0.054404145077720206,"disorder_content":0.10103626943005181,"disprot_consensus":{"full":[{"start":248,"end":286,"type":"T"}],"Structural state":[{"start":248,"end":286,"type":"D"}],"Molecular function":[{"start":248,"end":286,"type":"F"}],"Structural transition":[{"start":248,"end":286,"type":"T"}]}},{"acc":"Q07097","sequence":"MAGLLSTFDTFSSRRSESINKSGGGAVIPGQRSTVSVFVLGPSVTDDADKLFIATTFLAHSLDTDKQHSQRGGFLVSLLAMAYSSPELYLTTNGVNADVKYVIYNIEKDPKRTKTDGFIVKTRDMEYERTTEWLFGPMVNKSPLFQGQRVAADPDTLLQTYGYPACLGAIIVQVWIVLVKAITSSAGLRKGFFNRLEAFRQDGTVKGALVFTGETVEGIGSVMRSQQSLVSLMVETLVTMNTARSDLTTLEKNIQIVGNYIRDAGLASFMNTIKYGVETKMAALTLSNLRPDINKLRSLIDTYLSKGPRAPFICILKDPVHGEFAPGNYPALWSYAMGVAVVQNKAMQQYVTGGTYLDMEMFLLGQAVAKDAESKISSALEDELGVTDTAKERLRHHLANLSGGDGAYHEPTGGGAIEVALDNADIDLETEAHADQDARGWGGESGERWARQVSGGHFVTLHGAERLEEETNDEDVSDIERRIAMRLAERRQEDSATHGDEGRNNGVDHDEDDDAAAVAGIGGI","creator":"ktsirigos","dataset":["Viral proteins","RNA-binding proteins"],"date":"2016-08-26T17:11:03.000Z","disprot_id":"DP00629","features":{"pfam":[{"id":"PF00973","name":"Paramyxovirus nucleocapsid protein","start":1,"end":400}]},"genes":[{"name":{"value":"N","evidences":[],"_id":"685af523b4ac24d5329d7f6a"},"synonyms":[{"value":"NP","evidences":[],"_id":"685af523b4ac24d5329d7f6b"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d7f69"}],"length":524,"name":"Nucleoprotein","ncbi_taxon_id":11195,"organism":"Sendai virus (strain Fushimi)","regions_counter":29,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Paramyxoviridae","Orthoparamyxovirinae","Respirovirus"],"UniParc":"UPI000012FE17","uniref100":"UniRef100_Q07097","uniref50":"UniRef50_Q07097","uniref90":"UniRef90_Q07097","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":443,"end":524,"interaction_partner":[],"reference_html":"Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: application to the molecular recognition element of Sendai virus nucleoprotein. <i> Jensen MR, Houben K, Lescop E, Blanchard L, Ruigrok RW, Blackledge M. </i> J Am Chem Soc, 2008","reference_id":"18507376","region_id":"DP00629r024","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"1DHN RDCs from the majority of the sequence follow the classically observed inverted bell-shaped distribution along the primary sequence, indicative of an unfolded peptide chain.","_id":"685af523b4ac24d5329d7f52"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-28T07:31:09.868Z","_id":"685af523b4ac24d5329d7f53"},"version":1,"_id":"685af523b4ac24d5329d7f51","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":473,"end":492,"interaction_partner":[{"db":"UniProt","id":"P04859","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d7f55"}],"reference_html":"Visualizing the molecular recognition trajectory of an intrinsically disordered protein using multinuclear relaxation dispersion NMR. <i> Schneider R, Maurin D, Communie G, Kragelj J, Hansen DF, Ruigrok RW, Jensen MR, Blackledge M. </i> J Am Chem Soc, 2015","reference_id":"25551399","region_id":"DP00629r025","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"NMR chemical shift titration studies of the NT:PX complex show that resonances of NT from throughout the interaction region (residues 473–492) experience line broadening (Figure S1, Supporting Information). ","_id":"685af523b4ac24d5329d7f56"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-28T07:32:23.985Z","_id":"685af523b4ac24d5329d7f57"},"version":1,"_id":"685af523b4ac24d5329d7f54","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"statements":[{"type":"Methods","text":"The NT domain comprising residues 401–524 of the nucleoprotein of Sendai virus (SeV) strain Harris, whose amino acid sequence corresponds to that of SeV Fushimi strain NT (UniProtKB accession number Q07097) except for the mutation E410K, as well as the PX domain comprising residues 474–568 of the phosphoprotein (UniProtKB P04859) of SeV strain Harris, were expressed and purified as described previously.","_id":"685af523b4ac24d5329d7f5c"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu410Lys","_id":"685af523b4ac24d5329d7f5b"}],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":524,"interaction_partner":[],"reference_html":"Visualizing the molecular recognition trajectory of an intrinsically disordered protein using multinuclear relaxation dispersion NMR. <i> Schneider R, Maurin D, Communie G, Kragelj J, Hansen DF, Ruigrok RW, Jensen MR, Blackledge M. </i> J Am Chem Soc, 2015","reference_id":"25551399","region_id":"DP00629r026","released":"2022_03","sample":[],"sequence_construct":"LSGGDGAYHKPTGGGAIEVALDNADIDLETEAHADQDARGWGGESGERWARQVSGGHFVTLHGAERLEEETNDEDVSDIERRIAMRLAERRQEDSATHGDEGRNNGVDHDEDDDAAAVAGIGGI","statement":[{"type":"Results","text":"No detectable RD is measured in free NT (Figure S3, Supporting Information), confirming the rapid nature of the exchange between the three helical substates and the unfolded state.","_id":"685af523b4ac24d5329d7f59"},{"type":"Conclusion","text":"Multinuclear RD provides an atomic resolution map of the molecular recognition trajectory of intrinsically disordered NT from the highly dynamic free-state equilibrium to the bound state, revealing a three-state interaction process whose binding modes and kinetics are regulated by the intrinsic dynamics of both proteins. ","_id":"685af523b4ac24d5329d7f5a"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-28T07:31:51.375Z","_id":"685af523b4ac24d5329d7f5d"},"version":1,"_id":"685af523b4ac24d5329d7f58","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":476,"end":489,"interaction_partner":[],"reference_html":"Visualizing the molecular recognition trajectory of an intrinsically disordered protein using multinuclear relaxation dispersion NMR. <i> Schneider R, Maurin D, Communie G, Kragelj J, Hansen DF, Ruigrok RW, Jensen MR, Blackledge M. </i> J Am Chem Soc, 2015","reference_id":"25551399","region_id":"DP00629r027","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Structural analysis of the different steps of NT binding to PX. (A) 13C′ secondary chemical shifts of the bound state of NT (derived by adding ΔωAB from the consensus three-state exchange model of Figure 4 to free-state shifts, red bars) and ASTEROIDS minimum ensemble selection against these shifts (blue line). A single ensemble substate, reporting on helix 476–489 populated to 100%, best reproduces the experimental data.","_id":"685af523b4ac24d5329d7f5f"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-28T07:32:26.383Z","_id":"685af523b4ac24d5329d7f60"},"version":1,"_id":"685af523b4ac24d5329d7f5e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":473,"end":492,"interaction_partner":[],"reference_html":"Visualizing the molecular recognition trajectory of an intrinsically disordered protein using multinuclear relaxation dispersion NMR. <i> Schneider R, Maurin D, Communie G, Kragelj J, Hansen DF, Ruigrok RW, Jensen MR, Blackledge M. </i> J Am Chem Soc, 2015","reference_id":"25551399","region_id":"DP00629r028","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"NMR chemical shift titration studies of the NT:PX complex show that resonances of NT from throughout the interaction region (residues 473–492) experience line broadening (Figure S1, Supporting Information).","_id":"685af523b4ac24d5329d7f62"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_go_domain":"F","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-28T07:32:31.246Z","_id":"685af523b4ac24d5329d7f63"},"version":1,"_id":"685af523b4ac24d5329d7f61","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"statements":[{"type":"Methods","text":"Three constructs of the NT domain, comprising residues 401–524 (NTL), 444–524 (NTM), and 444–501 (NTS) of the nucleoprotein of Sendai virus strain Harris, whose sequence corresponds to that of SeV Fushimi strain NT (UniProtKB accession number Q07097) except for mutation E410 K, were expressed and purified as described previously.","_id":"685af523b4ac24d5329d7f66"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu410Lys","_id":"685af523b4ac24d5329d7f65"}],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":524,"interaction_partner":[],"reference_html":"Identification of Dynamic Modes in an Intrinsically Disordered Protein Using Temperature-Dependent NMR Relaxation. <i> Abyzov A, Salvi N, Schneider R, Maurin D, Ruigrok RW, Jensen MR, Blackledge M. </i> J Am Chem Soc, 2016","reference_id":"27112095","region_id":"DP00629r029","released":"2022_03","sample":[],"sequence_construct":"LSGGDGAYHKPTGGGAIEVALDNADIDLETEAHADQDARGWGGESGERWARQVSGGHFVTLHGAERLEEETNDEDVSDIERRIAMRLAERRQEDSATHGDEGRNNGVDHDEDDDAAAVAGIGGI  ","statement":[{"type":"Results","text":"We note that the backbone conformational propensities remain stable with temperature in the unfolded regions of NT, while the predominantly helical region (residues 476–492) shows a slight increase in helical propensity (around 5–7%) at lower temperatures as judged from temperature-corrected (80)13Cα chemical shifts (Figure S5).","_id":"685af523b4ac24d5329d7f67"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-28T07:29:02.803Z","_id":"685af523b4ac24d5329d7f68"},"version":1,"_id":"685af523b4ac24d5329d7f64","reference_source":"pmid"}],"__v":0,"disorder_content":0.2366412213740458,"disprot_consensus":{"full":[{"start":401,"end":475,"type":"D"},{"start":476,"end":489,"type":"T"},{"start":490,"end":524,"type":"D"}],"Structural state":[{"start":401,"end":524,"type":"D"}],"Molecular function":[{"start":473,"end":492,"type":"F"}],"Structural transition":[{"start":476,"end":489,"type":"T"}]}},{"features":{"pfam":[{"id":"PF01387","name":"Synuclein","start":1,"end":122}],"gene3D":[{"start":1,"end":126,"id":"1.10.287.700","name":"Helix hairpin bin"}]},"uniref50":"UniRef50_O76070","sequence":"MDVFKKGFSIAKEGVVGAVEKTKQGVTEAAEKTKEGVMYVGAKTKENVVQSVTSVAEKTKEQANAVSEAVVSSVNTVATKTVEEAENIAVTSGVVRKEDLRPSAPQQEGEASKEKEEVAEEAQSGGD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O76070","disprot_id":"DP00630","ncbi_taxon_id":9606,"regions_counter":6,"creator":"ktsirigos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":127,"region_id":"DP00630r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Synuclein-gamma targeting peptide inhibitor that enhances sensitivity of breast cancer cells to antimicrotubule drugs. <i> Singh VK, Zhou Y, Marsh JA, Uversky VN, Forman-Kay JD, Liu J, Jia Z. </i> Cancer Res, 2007","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":1,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"17234772","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":127,"term_name":"molecular function regulator","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"17234772","version":3,"reference_html":"Synuclein-gamma targeting peptide inhibitor that enhances sensitivity of breast cancer cells to antimicrotubule drugs. <i> Singh VK, Zhou Y, Marsh JA, Uversky VN, Forman-Kay JD, Liu J, Jia Z. </i> Cancer Res, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006165","region_id":"DP00630r002","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":127,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"17234772","version":3,"reference_html":"Synuclein-gamma targeting peptide inhibitor that enhances sensitivity of breast cancer cells to antimicrotubule drugs. <i> Singh VK, Zhou Y, Marsh JA, Uversky VN, Forman-Kay JD, Liu J, Jia Z. </i> Cancer Res, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00630r003","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":127,"region_id":"DP00630r004","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Synuclein-gamma targeting peptide inhibitor that enhances sensitivity of breast cancer cells to antimicrotubule drugs. <i> Singh VK, Zhou Y, Marsh JA, Uversky VN, Forman-Kay JD, Liu J, Jia Z. </i> Cancer Res, 2007","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":1,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"17234772","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":127,"term_name":"molecular function regulator","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"17234772","version":3,"reference_html":"Synuclein-gamma targeting peptide inhibitor that enhances sensitivity of breast cancer cells to antimicrotubule drugs. <i> Singh VK, Zhou Y, Marsh JA, Uversky VN, Forman-Kay JD, Liu J, Jia Z. </i> Cancer Res, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006204","region_id":"DP00630r005","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":127,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"17234772","version":3,"reference_html":"Synuclein-gamma targeting peptide inhibitor that enhances sensitivity of breast cancer cells to antimicrotubule drugs. <i> Singh VK, Zhou Y, Marsh JA, Uversky VN, Forman-Kay JD, Liu J, Jia Z. </i> Cancer Res, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00630r006","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_O76070","date":"2016-09-09T11:10:19.000Z","acc":"O76070","name":"Gamma-synuclein","length":127,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000031738","genes":[{"name":{"value":"SNCG"},"synonyms":[{"value":"BCSG1"},{"value":"PERSYN"},{"value":"PRSN"}]}],"alphafold_very_low_content":0.14960629921259844,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":127,"type":"D"}],"Structural state":[{"start":1,"end":127,"type":"D"}],"Molecular function":[{"start":1,"end":127,"type":"F"}]}},{"features":{"pfam":[{"id":"PF29958","name":"SIC1 C-terminal domain","start":228,"end":271}]},"uniref50":"UniRef50_P38634","sequence":"MTPSTPPRSRGTRYLAQPSGNTSSSALMQGQKTPQKPSQNLVPVTPSTTKSFKNAPLLAPPNSNMGMTSPFNGLTSPQRSPFPKSSVKRTLFQFESHDNGTVREEQEPLGRVNRILFPTQQNVDIDAAEEEEEGEVLLPPSRPTSARQLHLSLERDEFDQTHRKKIIKDVPGTPSDKVITFELAKNWNNNSPKNDARSQESEDEEDIIINPVRVGKNPFASDELVTQEIRNERKRAMLRENPDIEDVITYVNKKGEVVEKRRLTDEEKRRFKPKALFQSRDQEH","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P38634","disprot_id":"DP00631","ncbi_taxon_id":559292,"regions_counter":29,"creator":"eficho","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":90,"region_id":"DP00631r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The meandering of disordered proteins in conformational space. <i> Konrat R. </i> Structure, 2010","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":1,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"20399178","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":90,"term_name":"molecular function regulator","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"20399178","version":3,"reference_html":"The meandering of disordered proteins in conformational space. <i> Konrat R. </i> Structure, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006204","region_id":"DP00631r002","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":90,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"20399178","version":3,"reference_html":"The meandering of disordered proteins in conformational space. <i> Konrat R. </i> Structure, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00631r003","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":90,"region_id":"DP00631r004","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Polyelectrostatic interactions of disordered ligands suggest a physical basis for ultrasensitivity. <i> Borg M, Mittag T, Pawson T, Tyers M, Forman-Kay JD, Chan HS. </i> Proc Natl Acad Sci U S A, 2007","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":1,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"17522259","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":90,"term_name":"molecular function regulator","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"17522259","version":3,"reference_html":"Polyelectrostatic interactions of disordered ligands suggest a physical basis for ultrasensitivity. <i> Borg M, Mittag T, Pawson T, Tyers M, Forman-Kay JD, Chan HS. </i> Proc Natl Acad Sci U S A, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006204","region_id":"DP00631r005","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":90,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"17522259","version":3,"reference_html":"Polyelectrostatic interactions of disordered ligands suggest a physical basis for ultrasensitivity. <i> Borg M, Mittag T, Pawson T, Tyers M, Forman-Kay JD, Chan HS. </i> Proc Natl Acad Sci U S A, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00631r006","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":90,"region_id":"DP00631r007","released":"2022_03","ec_id":"ECO:0006204","reference_html":"CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices. <i> Baker JM, Hudson RP, Kanelis V, Choy WY, Thibodeau PH, Thomas PJ, Forman-Kay JD. </i> Nat Struct Mol Biol, 2007","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":1,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"17660831","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":90,"term_name":"molecular function regulator","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"17660831","version":3,"reference_html":"CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices. <i> Baker JM, Hudson RP, Kanelis V, Choy WY, Thibodeau PH, Thomas PJ, Forman-Kay JD. </i> Nat Struct Mol Biol, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006204","region_id":"DP00631r008","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":90,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"17660831","version":3,"reference_html":"CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices. <i> Baker JM, Hudson RP, Kanelis V, Choy WY, Thibodeau PH, Thomas PJ, Forman-Kay JD. </i> Nat Struct Mol Biol, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00631r009","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":90,"region_id":"DP00631r010","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Six steps to destruction. <i> Ferrell JE. </i> Nature, 2001","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":1,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"11734834","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":90,"term_name":"molecular function regulator","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"11734834","version":3,"reference_html":"Six steps to destruction. <i> Ferrell JE. </i> Nature, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006204","region_id":"DP00631r011","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":90,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"11734834","version":3,"reference_html":"Six steps to destruction. <i> Ferrell JE. </i> Nature, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00631r012","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":90,"region_id":"DP00631r013","released":"2024_06","ec_id":"ECO:0006165","reference_html":"Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase. <i> Mittag T, Marsh J, Grishaev A, Orlicky S, Lin H, Sicheri F, Tyers M, Forman-Kay JD. </i> Structure, 2010","statement":[{"text":"While we observed complete broadening due to the increased relaxation around the spin-labeling sites, as would be expected for random coil ensembles, even residues distant in sequence from these sites exhibited significant PRE effects both in Sic1 and in pSic1.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-01-30T15:41:41.864Z","reference_source":"pmid","term_name":"disorder","reference_id":"20399186","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":90,"region_id":"DP00631r014","released":"2024_06","ec_id":"ECO:0006165","reference_html":"Dynamic equilibrium engagement of a polyvalent ligand with a single-site receptor. <i> Mittag T, Orlicky S, Choy WY, Tang X, Lin H, Sicheri F, Kay LE, Tyers M, Forman-Kay JD. </i> Proc Natl Acad Sci U S A, 2008","statement":[{"text":"1HN-15N correlation spectra (Fig. 1A) of Sic1 (black) and pSic1 (red) display limited amide proton chemical shift dispersion and sharp lines; such spectra are diagnostic of disordered proteins because the rapid interconversion of different conformers, many of which lack tertiary contacts, results in an averaged magnetic environment of the nuclei.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-01-30T15:49:46.974Z","reference_source":"pmid","term_name":"disorder","reference_id":"19008353","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":90,"term_name":"protein binding","released":"2024_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Dynamic equilibrium engagement of a polyvalent ligand with a single-site receptor. <i> Mittag T, Orlicky S, Choy WY, Tang X, Lin H, Sicheri F, Kay LE, Tyers M, Forman-Kay JD. </i> Proc Natl Acad Sci U S A, 2008","statement":[{"text":"Titration of unlabeled Skp1–Cdc4 into a solution of 15N-labeled pSic1 allowed us to monitor the binding interaction by broadening of signals in NMR 1HN-15N correlation spectra.","type":"Results"},{"text":"The unaltered chemical shifts of the observable signals of pSic1 in the presence of Skp1–Cdc4 further demonstrate that pSic1 is disordered when in complex with Skp1–Cdc4.","type":"Results"}],"term_id":"GO:0005515","curator_id":"vnugnes","start":1,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"19008353","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2024-01-30T16:44:05.553Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00631r015","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":5,"end":5,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":33,"end":33,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":45,"end":45,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":69,"end":69,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":76,"end":76,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":80,"end":80,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]},{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":90,"region_id":"DP00631r017","released":"2024_06","ec_id":"ECO:0006210","reference_html":"Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase. <i> Mittag T, Marsh J, Grishaev A, Orlicky S, Lin H, Sicheri F, Tyers M, Forman-Kay JD. </i> Structure, 2010","statement":[{"text":"To obtain additional information on the molecular size distribution and the distribution of heavy atom distances in the ensembles, we collected SAXS data (Figure 2). The Kratky plots (Figure 2B) are typical for disordered protein states.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-01-30T15:47:30.353Z","reference_source":"pmid","term_name":"disorder","reference_id":"20399186","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00631r018","ec_ontology":"ECO","end":284,"term_id":"IDPO:0000002","start":1,"version":3,"statement":[{"text":"Sic1-GFP exhibited a thin and flexible tail-like structure with a temporarily appearing and disappearing small globule at the N-terminal end, together with the C-terminal GFP. The R_2D histogram for the IDR was best fitted to a double Gaussian with peaks at 12.2 +/- 0.66 and 20.5 +/- 2.14 nm. The IDR is fully disordered in both shorter and longer states, as judged from its mean height of 0.4–0.5 nm in both metastable states ","type":"Results"},{"text":"The authors of the publication characterized an engineered fusion protein, i.e. recombinant Sic1 fused with GFP.","type":"Curator statement"}],"term_name":"disorder","ec_name":"atomic force microscopy evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2024_06","term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"33230318","date":"2023-09-28T17:03:22.556Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0001591","curator_id":"tlazar","reference_html":"Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy. <i> Kodera N, Noshiro D, Dora SK, Mori T, Habchi J, Blocquel D, Gruet A, Dosnon M, Salladini E, Bignon C, Fujioka Y, Oda T, Noda NN, Sato M, Lotti M, Mizuguchi M, Longhi S, Ando T. </i> Nat Nanotechnol, 2021","ec_go":"IDA","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Results","text":"Sic1-GFP exhibited a thin and flexible tail-like structure with a temporarily appearing and disappearing small globule at the N-terminal end, together with the C-terminal GFP."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-01-30T16:47:53.505Z"}},{"region_id":"DP00631r019","ec_ontology":"ECO","end":190,"term_id":"IDPO:0000018","start":31,"version":3,"statement":[{"text":"The large number around 190 indicates that as much as about 65% of the whole protein is loosely folded, with only the remaining C-terminal region (encompassing about 95aa) being fully extended. The remarkable difference between 30 and 190 indicates that a large segment containing about 160 residues undergoes a transition between fully unstructured and loosely folded conformations.","type":"Results"},{"text":"The authors of the publication characterized an engineered fusion protein, i.e. recombinant Sic1 fused with GFP.","type":"Curator statement"}],"term_name":"disorder to molten globule","ec_name":"atomic force microscopy evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2024_06","term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"33230318","date":"2023-09-28T17:04:24.408Z","reference_source":"pmid","term_namespace":"Structural transition","ec_id":"ECO:0001591","curator_id":"tlazar","reference_html":"Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy. <i> Kodera N, Noshiro D, Dora SK, Mori T, Habchi J, Blocquel D, Gruet A, Dosnon M, Salladini E, Bignon C, Fujioka Y, Oda T, Noda NN, Sato M, Lotti M, Mizuguchi M, Longhi S, Ando T. </i> Nat Nanotechnol, 2021","ec_go":"IDA","disprot_namespace":"Structural transition","construct_alterations":[{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Results","text":"Sic1-GFP exhibited a thin and flexible tail-like structure with a temporarily appearing and disappearing small globule at the N-terminal end, together with the C-terminal GFP."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-01-30T16:47:57.481Z"}},{"start":3,"end":7,"reference_id":"20399186","reference_source":"pmid","reference_html":"Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase. <i> Mittag T, Marsh J, Grishaev A, Orlicky S, Lin H, Sicheri F, Tyers M, Forman-Kay JD. </i> Structure, 2010","date":"2024-01-30T15:44:26.229Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP00631r020","statement":[{"text":"The identity of phosphorylated residues was confirmed by NMR. The CDK sites at Thr5, Thr33, Thr45, Ser69, Ser76, and Ser80 were phosphorylated, whereas Thr2 was not phosphorylated in this construct.","type":"Methods"}]},{"start":31,"end":35,"reference_id":"20399186","reference_source":"pmid","reference_html":"Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase. <i> Mittag T, Marsh J, Grishaev A, Orlicky S, Lin H, Sicheri F, Tyers M, Forman-Kay JD. </i> Structure, 2010","date":"2024-01-30T15:44:32.452Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP00631r021","statement":[{"text":"The identity of phosphorylated residues was confirmed by NMR. The CDK sites at Thr5, Thr33, Thr45, Ser69, Ser76, and Ser80 were phosphorylated, whereas Thr2 was not phosphorylated in this construct.","type":"Methods"}]},{"start":43,"end":47,"reference_id":"20399186","reference_source":"pmid","reference_html":"Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase. <i> Mittag T, Marsh J, Grishaev A, Orlicky S, Lin H, Sicheri F, Tyers M, Forman-Kay JD. </i> Structure, 2010","date":"2024-01-30T15:46:02.571Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP00631r022","statement":[{"text":"The identity of phosphorylated residues was confirmed by NMR. The CDK sites at Thr5, Thr33, Thr45, Ser69, Ser76, and Ser80 were phosphorylated, whereas Thr2 was not phosphorylated in this construct.","type":"Methods"}]},{"start":67,"end":71,"reference_id":"20399186","reference_source":"pmid","reference_html":"Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase. <i> Mittag T, Marsh J, Grishaev A, Orlicky S, Lin H, Sicheri F, Tyers M, Forman-Kay JD. </i> Structure, 2010","date":"2024-01-30T15:46:08.959Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP00631r023","statement":[{"text":"The identity of phosphorylated residues was confirmed by NMR. The CDK sites at Thr5, Thr33, Thr45, Ser69, Ser76, and Ser80 were phosphorylated, whereas Thr2 was not phosphorylated in this construct.","type":"Methods"}]},{"start":74,"end":78,"reference_id":"20399186","reference_source":"pmid","reference_html":"Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase. <i> Mittag T, Marsh J, Grishaev A, Orlicky S, Lin H, Sicheri F, Tyers M, Forman-Kay JD. </i> Structure, 2010","date":"2024-01-30T15:46:15.529Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP00631r024","statement":[{"text":"The identity of phosphorylated residues was confirmed by NMR. The CDK sites at Thr5, Thr33, Thr45, Ser69, Ser76, and Ser80 were phosphorylated, whereas Thr2 was not phosphorylated in this construct.","type":"Methods"}]},{"start":78,"end":82,"reference_id":"20399186","reference_source":"pmid","reference_html":"Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase. <i> Mittag T, Marsh J, Grishaev A, Orlicky S, Lin H, Sicheri F, Tyers M, Forman-Kay JD. </i> Structure, 2010","date":"2024-01-30T15:46:23.247Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP00631r025","statement":[{"text":"The identity of phosphorylated residues was confirmed by NMR. The CDK sites at Thr5, Thr33, Thr45, Ser69, Ser76, and Ser80 were phosphorylated, whereas Thr2 was not phosphorylated in this construct.","type":"Methods"}]},{"start":1,"end":90,"reference_id":"19008353","reference_source":"pmid","reference_html":"Dynamic equilibrium engagement of a polyvalent ligand with a single-site receptor. <i> Mittag T, Orlicky S, Choy WY, Tang X, Lin H, Sicheri F, Kay LE, Tyers M, Forman-Kay JD. </i> Proc Natl Acad Sci U S A, 2008","date":"2024-01-30T16:05:51.351Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1905761","term_name":"SCF ubiquitin ligase complex binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":5,"end":5,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":33,"end":33,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":45,"end":45,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":69,"end":69,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":76,"end":76,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":80,"end":80,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]}],"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P07834","operator":null,"partner_start":263,"partner_end":744}],"region_id":"DP00631r026","statement":[{"text":"We next evaluated the interaction of 6-fold phosphorylated Sic1 with a monomeric Skp1–Cdc4 complex; the Skp1 subunit of SCFCdc4 is required for soluble expression of Cdc4 but does not interact with substrates (24). Using an intrinsic Trp fluorescence-binding assay, we measured an apparent overall Kd value of ≈0.6 μM between the pSic1 preparation and Skp1–Cdc4, whereas no binding was detected for Sic1.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a SCF ubiquitin ligase complex.\" [GOC:dph, GOC:ha, GOC:TermGenie, PMID:19723762]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":90,"reference_id":"19008353","reference_source":"pmid","reference_html":"Dynamic equilibrium engagement of a polyvalent ligand with a single-site receptor. <i> Mittag T, Orlicky S, Choy WY, Tang X, Lin H, Sicheri F, Kay LE, Tyers M, Forman-Kay JD. </i> Proc Natl Acad Sci U S A, 2008","date":"2024-01-30T16:07:36.329Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":5,"end":5,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":33,"end":33,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":45,"end":45,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":69,"end":69,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":76,"end":76,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":80,"end":80,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]}],"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P07834","operator":null,"partner_start":263,"partner_end":744}],"region_id":"DP00631r027","statement":[{"text":"We next evaluated the interaction of 6-fold phosphorylated Sic1 with a monomeric Skp1–Cdc4 complex; the Skp1 subunit of SCFCdc4 is required for soluble expression of Cdc4 but does not interact with substrates (24). Using an intrinsic Trp fluorescence-binding assay, we measured an apparent overall Kd value of ≈0.6 μM between the pSic1 preparation and Skp1–Cdc4, whereas no binding was detected for Sic1.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":90,"reference_id":"19008353","reference_source":"pmid","reference_html":"Dynamic equilibrium engagement of a polyvalent ligand with a single-site receptor. <i> Mittag T, Orlicky S, Choy WY, Tang X, Lin H, Sicheri F, Kay LE, Tyers M, Forman-Kay JD. </i> Proc Natl Acad Sci U S A, 2008","date":"2024-01-30T16:45:40.458Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1905761","term_name":"SCF ubiquitin ligase complex binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":5,"end":5,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":33,"end":33,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":45,"end":45,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":69,"end":69,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":76,"end":76,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":80,"end":80,"position":"Specific residue","statements":[{"type":"Methods","text":"The CDK sites at Thr-5, Thr-33, Thr-45, Ser-69, Ser-76, and Ser-80 were phosphorylated, whereas Thr-2 was not phosphorylated in this construct."}]},{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P07834","operator":null,"partner_start":263,"partner_end":744}],"region_id":"DP00631r028","statement":[{"text":"Titration of unlabeled Skp1–Cdc4 into a solution of 15N-labeled pSic1 allowed us to monitor the binding interaction by broadening of signals in NMR 1HN-15N correlation spectra. ","type":"Results"},{"text":"The unaltered chemical shifts of the observable signals of pSic1 in the presence of Skp1–Cdc4 further demonstrate that pSic1 is disordered when in complex with Skp1–Cdc4.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a SCF ubiquitin ligase complex.\" [GOC:dph, GOC:ha, GOC:TermGenie, PMID:19723762]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_P38634","date":"2016-09-09T11:08:03.000Z","acc":"P38634","name":"Protein SIC1","length":284,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000052F58","genes":[{"name":{"value":"SIC1"},"synonyms":[{"value":"SDB25"}],"orfNames":[{"value":"L9449.8"}],"olnNames":[{"value":"YLR079W"}]}],"alphafold_very_low_content":0.352112676056338,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":30,"type":"D"},{"start":31,"end":190,"type":"T"},{"start":191,"end":284,"type":"D"}],"Structural state":[{"start":1,"end":284,"type":"D"}],"Molecular function":[{"start":1,"end":90,"type":"F"}],"Structural transition":[{"start":31,"end":190,"type":"T"}],"Disorder function":[{"start":3,"end":7,"type":"F"},{"start":31,"end":35,"type":"F"},{"start":43,"end":47,"type":"F"},{"start":67,"end":71,"type":"F"},{"start":74,"end":82,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00439","name":"Bromodomain","start":1068,"end":1143},{"id":"PF00569","name":"Zinc finger, ZZ type","start":1665,"end":1705},{"id":"PF02135","name":"TAZ zinc finger","start":338,"end":414},{"id":"PF02135","name":"TAZ zinc finger","start":1735,"end":1806},{"id":"PF02172","name":"KIX domain","start":567,"end":646},{"id":"PF06001","name":"CREB-binding protein/p300, atypical RING domain","start":1156,"end":1195},{"id":"PF09030","name":"Creb binding","start":1992,"end":2098},{"id":"PF23570","name":"Histone acetyltransferase p300-like, PHD domain","start":1240,"end":1278},{"id":"PF29847","name":"Histone acetyltransferase domain KAT3","start":1306,"end":1612}],"gene3D":[{"start":1237,"end":1282,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":2043,"end":2099,"id":"1.10.1630.10","name":"Nuclear receptor coactivator, CREB-bp-like, interlocking domain"},{"start":1723,"end":1836,"id":"1.20.1020.10","name":"TAZ domain"},{"start":323,"end":423,"id":"1.20.1020.10","name":"TAZ domain"},{"start":1013,"end":1161,"id":"1.20.920.10","name":"Bromodomain-like"},{"start":1170,"end":1236,"id":"2.10.110.40","name":"2.10.110.40"},{"start":1662,"end":1714,"id":"3.30.60.90","name":"3.30.60.90"},{"start":566,"end":652,"id":"1.10.246.20","name":"Coactivator CBP, KIX domain"}]},"uniref50":"UniRef50_Q09472","sequence":"MAENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGDINQLQTSLGMVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQVMASQAQQSSPGLGLINSMVKSPMTQAGLTSPNMGMGTSGPNQGPTQSTGMMNSPVNQPAMGMNTGMNAGMNPGMLAAGNGQGIMPNQVMNGSIGAGRGRQNMQYPNPGMGSAGNLLTEPLQQGSPQMGGQTGLRGPQPLKMGMMNNPNPYGSPYTQNPGQQIGASGLGLQIQTKTVLSNNLSPFAMDKKAVPGGGMPNMGQQPAPQVQQPGLVTPVAQGMGSGAHTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVCLPLKNAGDKRNQQPILTGAPVGLGNPSSLGVGQQSAPNLSTVSQIDPSSIERAYAALGLPYQVNQMPTQPQVQAKNQQNQQPGQSPQGMRPMSNMSASPMGVNGGVGVQTPSLLSDSMLHSAINSQNPMMSENASVPSLGPMPTAAQPSTTGIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELEEKRRTRLQKQNMLPNAAGMVPVSMNPGPNMGQPQPGMTSNGPLPDPSMIRGSVPNQMMPRITPQSGLNQFGQMSMAQPPIVPRQTPPLQHHGQLAQPGALNPPMGYGPRMQQPSNQGQFLPQTQFPSQGMNVTNIPLAPSSGQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPQLPQPALHQNSPSPVPSRTPTPHHTPPSIGAQQPPATTIPAPVPTPPAMPPGPQSQALHPPPRQTPTPPTTQLPQQVQPSLPAAPSADQPQQQPRSQQSTAASVPTPTAPLLPPQPATPLSQPAVSIEGQVSNPPSTSSTEVNSQAIAEKQPSQEVKMEAKMEVDQPEPADTQPEDISESKVEDCKMESTETEERSTELKTEIKEEEDQPSTSATQSSPAPGQSKKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEIDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHFCEKCFNEIQGESVSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVLHHEIIWPAGFVCDGCLKKSARTRKENKFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKREENTSNESTDVTKGDSKNAKKKNNKKTSKNKSSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDPLIPCDLMDGRDAFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRFVYTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKLGLGLDDESNNQQAAATQSPGDSRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENKCPVPFCLNIKQKLRQQQLQHRLQQAQMLRRRMASMQRTGVVGQQQGLPSPTPATPTTPTGQQPTTPQTPQPTSQPQPTPPNSMPPYLPRTQAAGPVSQGKAAGQVTPPTPPQTAQPPLPGPPPAAVEMAMQIQRAAETQRQMAHVQIFQRPIQHQMPPMTPMAPMGMNPPPMTRGPSGHLEPGMGPTGMQQQPPWSQGGLPQPQQLQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGISPLKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANSNPQPIPGQPGMPQGQPGLQPPTMPGQQGVHSNPAMQNMNPMQAGVQRAGLPQQQPQQQLQPPMGGMSPQAQQMNMNHNTMPSQFRDILRRQQMMQQQQQQGAGPGIGPGMANHNQFQQPQGVGYPPQQQQRMQHHMQQMQQGNMGQIGQLPQALGAEAGASLQAYQQRLLQQQMGSPVQPNPMSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHVSPQTSSPHPGLVAAQANPMEQGHFASPDQNSMLSQLASNPGMANLHGASATDLGLSTDNSDLNSNLSQSTLDIH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q09472","disprot_id":"DP00633","ncbi_taxon_id":9606,"regions_counter":6,"creator":"ktsirigos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":566,"region_id":"DP00633r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53. <i> Teufel DP, Freund SM, Bycroft M, Fersht AR. </i> Proc Natl Acad Sci U S A, 2007","term_id":"IDPO:0000002","curator_id":"vnugnes","start":401,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"17438265","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-05-16T17:19:10.644Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"However, no folded structure could be detected in the IHD.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:29:28.964Z"}},{"start":1,"end":1045,"reference_id":"31314496","reference_source":"pmid","reference_html":"Tumor Suppressor p53-Mediated Structural Reorganization of the Transcriptional Coactivator p300. <i> Ghosh R, Kaypee S, Shasmal M, Kundu TK, Roy S, Sengupta J. </i> Biochemistry, 2019","date":"2023-05-17T18:01:32.303Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6K4N"},{"db":"EMDB","id":"6792"}],"region_id":"DP00633r002","statement":[{"text":"Evidently, significant parts of the unstructured regions at the N- and C-termini (∼650 amino acids, Figure 3A) were not visible in our reconstruction, likely because of the dynamic nature of those regions. Considering that the p300 map encompassed the structured core domain and partly other N- and C-terminal structured domains, the effective molecular mass was adequate. We concluded that, in free form, the central (core) domain of p300 stays in a closely compact conformation as seen in the crystal structure, while unstructured linkers and part of N- and C-terminal domains remains in an ensemble of assorted dynamic conformations.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:29:31.975Z"}},{"start":1665,"end":2414,"reference_id":"31314496","reference_source":"pmid","reference_html":"Tumor Suppressor p53-Mediated Structural Reorganization of the Transcriptional Coactivator p300. <i> Ghosh R, Kaypee S, Shasmal M, Kundu TK, Roy S, Sengupta J. </i> Biochemistry, 2019","date":"2023-05-17T18:01:44.666Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6K4N"},{"db":"EMDB","id":"6792"}],"region_id":"DP00633r003","statement":[{"text":"Evidently, significant parts of the unstructured regions at the N- and C-termini (∼650 amino acids, Figure 3A) were not visible in our reconstruction, likely because of the dynamic nature of those regions. Considering that the p300 map encompassed the structured core domain and partly other N- and C-terminal structured domains, the effective molecular mass was adequate. We concluded that, in free form, the central (core) domain of p300 stays in a closely compact conformation as seen in the crystal structure, while unstructured linkers and part of N- and C-terminal domains remains in an ensemble of assorted dynamic conformations.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:29:36.255Z"}},{"start":1520,"end":1581,"reference_id":"31314496","reference_source":"pmid","reference_html":"Tumor Suppressor p53-Mediated Structural Reorganization of the Transcriptional Coactivator p300. <i> Ghosh R, Kaypee S, Shasmal M, Kundu TK, Roy S, Sengupta J. </i> Biochemistry, 2019","date":"2023-05-17T18:01:22.815Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6K4N"},{"db":"EMDB","id":"6792"}],"region_id":"DP00633r004","statement":[{"text":"Evidently, significant parts of the unstructured regions at the N- and C-termini (∼650 amino acids, Figure 3A) were not visible in our reconstruction, likely because of the dynamic nature of those regions. Considering that the p300 map encompassed the structured core domain and partly other N- and C-terminal structured domains, the effective molecular mass was adequate. We concluded that, in free form, the central (core) domain of p300 stays in a closely compact conformation as seen in the crystal structure, while unstructured linkers and part of N- and C-terminal domains remains in an ensemble of assorted dynamic conformations.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:29:40.257Z"}},{"start":1520,"end":1581,"reference_id":"31314496","reference_source":"pmid","reference_html":"Tumor Suppressor p53-Mediated Structural Reorganization of the Transcriptional Coactivator p300. <i> Ghosh R, Kaypee S, Shasmal M, Kundu TK, Roy S, Sengupta J. </i> Biochemistry, 2019","date":"2023-05-18T13:19:31.168Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"EMDB","id":"6791"},{"db":"PDB","id":"5XZC"}],"region_id":"DP00633r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04637"}],"statement":[{"text":"A model of the autoinhibitory loop was made (using PHYRE2 (50)), which could be accommodated in this loop density (Figure 4D).","type":"Results"},{"text":"Figure 4 shows this region is structured when the protein is in complex with p53.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:29:42.600Z"}},{"start":1520,"end":1581,"reference_id":"31314496","reference_source":"pmid","reference_html":"Tumor Suppressor p53-Mediated Structural Reorganization of the Transcriptional Coactivator p300. <i> Ghosh R, Kaypee S, Shasmal M, Kundu TK, Roy S, Sengupta J. </i> Biochemistry, 2019","date":"2023-05-18T13:23:55.513Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"EMDB","id":"6791"},{"db":"PDB","id":"5XZC"},{"db":"EMDB","id":"6792"},{"db":"PDB","id":"6K4N"}],"region_id":"DP00633r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04637"}],"statement":[{"text":"A model of the autoinhibitory loop was made (using PHYRE2 (50)), which could be accommodated in this loop density (Figure 4D).","type":"Results"},{"text":"While this region lacks electron density in the PDB structure 6K4N,  Figure 4 and PDB 5XZC shows this region is structured when the protein is in complex with p53.","type":"Curator statement"},{"text":"Thus, our structural analyses illustrated that, while conformation of the p300 central (core) domain in free form can be considered as a “closed” configuration, in the complex with p53, it transformed to an “open” conformation.","type":"Results"}],"states_connection":[{"source":"DP00633r004","target":"DP00633r005"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:29:46.602Z"}}],"released":"2016_10","uniref100":"UniRef100_Q09472","date":"2016-09-09T11:05:24.000Z","acc":"Q09472","name":"Histone acetyltransferase p300","length":2414,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins","Condensates-related proteins"],"UniParc":"UPI0000131009","genes":[{"name":{"value":"EP300"},"synonyms":[{"value":"P300"}]}],"alphafold_very_low_content":0.6093620546810273,"disorder_content":0.7692626346313173,"disprot_consensus":{"full":[{"start":1,"end":1045,"type":"D"},{"start":1520,"end":1581,"type":"T"},{"start":1665,"end":2414,"type":"D"}],"Structural state":[{"start":1,"end":1045,"type":"D"},{"start":1520,"end":1581,"type":"D"},{"start":1665,"end":2414,"type":"D"}],"Structural transition":[{"start":1520,"end":1581,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00225","name":"Kinesin motor domain","start":87,"end":416},{"id":"PF13931","name":"Kinesin-associated microtubule-binding","start":997,"end":1037}],"gene3D":[{"start":79,"end":420,"id":"3.40.850.10","name":"Kinesin motor domain"}]},"uniref50":"UniRef50_P17120","sequence":"MAGPQRATSGLPTRRTTTRQPTRRAGSAIPERQTSTASPAVSTKTAAISRTRTLKSPGEPASVLAKRKERDIEREINEDTSIHVVVRCRGRNEREVKENSGVVLQTEGVKGKTVELSMGPNAVSNKTYTFDKVFSAAADQITVYEDVVLPIVTEMLAGYNCTIFAYGQTGTGKTYTMSGDMTDTLGILSDNAGIIPRVLYSLFAKLADTESTVKCSFIELYNEELRDLLSAEENPKLKIYDNEQKKGHMSTLVQGMEETYIDSATAGIKLLQQGSHKRQVAATKCNDLSSRSHTVFTITVNIKRTTESGEEYVCPGKLNLVDLAGSENIGRSGAENKRATEAGLINKSLLTLGRVINALVDKSQHIPYRESKLTRLLQDSLGGRTKTCIIATISPARSNLEETISTLDYAFRAKNIRNKPQINSTMPKMTLLREFTAEIEKLKAELIATRHRNGVYMSVESYEEMKMENESRRIISEEQRAKIESMESSLRHKVQELLTLTSKFNDLKKDNDDTLAALCSTNDVLQQTDIVLQNTRAQLEEEEMLRCAHEETEHQLQDVGKGLISTLGQTVEDINSLQSKLDRKAELDATNAELWRASSTEVSDVTKRIDQRVEAFQTRHAKLLETTSVKVNEFIATEISNIERTRSDLSEYNRSLDAACNNAKAETSSAHEDMNNVLEEIKDLREEVKSKVGEGLNGLSAAAARISEEVIGEFTQLHSQLHTSFNNLGKDLKSIFETMATHLSEQKNEINRLRAELQSSNRQNIETTHKASAHLAQAIEEEHVAAEAEREILMSQIKALVEESRQKQFARLRAKIDGVRTEISASGDMLEQATTQHDRQIDEWVFKSEQFAKDVNASKDEIRTKLQNDWEAFDQRNSTIRKATESVHKETVRIVDVQVDDMGRQMEALDDFVAKARSQNGRYRDAHIATLDTIATGVRDSYSSIEGRVENLTGRMNQFQQEATHHHATLEESIAPLSNDVRKPLTDLSSSFQNRSLEEYVATGVTPKKRKYDYISVLPSTESHEVLKSRLRTTKEMEVLPFNSDDQLSGPSSSPGGSPSKGFVYNDVEDEVGTHAPTVTNVNPSNTGLREVDANVAARPLVYSTGEKSTDQDGSPVVSPDSATEAEGMNGPPSKRRRSNSVVADTKLPNKMLARRMAGMMEGRENVPPPGISNGRRLRGRPSP","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Eurotiomycetes","Eurotiomycetidae","Eurotiales","Aspergillaceae","Aspergillus","Aspergillus subgen. Nidulantes"],"uniref90":"UniRef90_P17120","disprot_id":"DP00636","ncbi_taxon_id":227321,"regions_counter":10,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":71,"region_id":"DP00636r001","released":"2022_03","ec_id":"ECO:0007680","reference_html":"The kinesin family member BimC contains a second microtubule binding region attached to the N terminus of the motor domain. <i> Stock MF, Chu J, Hackney DD. </i> J Biol Chem, 2003","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14530265","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":71,"term_name":"flexible N-terminal tail","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14530265","version":3,"reference_html":"The kinesin family member BimC contains a second microtubule binding region attached to the N terminus of the motor domain. <i> Stock MF, Chu J, Hackney DD. </i> J Biol Chem, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000032","ec_id":"ECO:0007680","region_id":"DP00636r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":71,"term_name":"molecular adaptor activity","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"14530265","version":3,"reference_html":"The kinesin family member BimC contains a second microtubule binding region attached to the N terminus of the motor domain. <i> Stock MF, Chu J, Hackney DD. </i> J Biol Chem, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0007680","region_id":"DP00636r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":71,"term_name":"molecular function regulator","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"14530265","version":3,"reference_html":"The kinesin family member BimC contains a second microtubule binding region attached to the N terminus of the motor domain. <i> Stock MF, Chu J, Hackney DD. </i> J Biol Chem, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0007680","region_id":"DP00636r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":71,"term_name":"protein binding","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"14530265","version":3,"reference_html":"The kinesin family member BimC contains a second microtubule binding region attached to the N terminus of the motor domain. <i> Stock MF, Chu J, Hackney DD. </i> J Biol Chem, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007680","region_id":"DP00636r005","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":71,"region_id":"DP00636r006","released":"2022_03","ec_id":"ECO:0006275","reference_html":"The kinesin family member BimC contains a second microtubule binding region attached to the N terminus of the motor domain. <i> Stock MF, Chu J, Hackney DD. </i> J Biol Chem, 2003","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14530265","version":2,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":71,"term_name":"flexible N-terminal tail","start":1,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14530265","version":3,"reference_html":"The kinesin family member BimC contains a second microtubule binding region attached to the N terminus of the motor domain. <i> Stock MF, Chu J, Hackney DD. </i> J Biol Chem, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000032","ec_id":"ECO:0006275","region_id":"DP00636r007","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":71,"term_name":"molecular adaptor activity","start":1,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"14530265","version":3,"reference_html":"The kinesin family member BimC contains a second microtubule binding region attached to the N terminus of the motor domain. <i> Stock MF, Chu J, Hackney DD. </i> J Biol Chem, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006275","region_id":"DP00636r008","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":71,"term_name":"molecular function regulator","start":1,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"14530265","version":3,"reference_html":"The kinesin family member BimC contains a second microtubule binding region attached to the N terminus of the motor domain. <i> Stock MF, Chu J, Hackney DD. </i> J Biol Chem, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006275","region_id":"DP00636r009","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":71,"term_name":"protein binding","start":1,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"14530265","version":3,"reference_html":"The kinesin family member BimC contains a second microtubule binding region attached to the N terminus of the motor domain. <i> Stock MF, Chu J, Hackney DD. </i> J Biol Chem, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006275","region_id":"DP00636r010","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P17120","date":"2016-08-16T16:13:23.000Z","acc":"P17120","name":"Kinesin-like protein bimC","length":1184,"organism":"Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)","dataset":[],"UniParc":"UPI0000126940","genes":[{"name":{"value":"bimC"},"orfNames":[{"value":"AN3363"}]}],"alphafold_very_low_content":0.20777027027027026,"disorder_content":0.059966216216216214,"disprot_consensus":{"full":[{"start":1,"end":71,"type":"D"}],"Structural state":[{"start":1,"end":71,"type":"D"}],"Disorder function":[{"start":1,"end":71,"type":"F"}],"Molecular function":[{"start":1,"end":71,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00048","name":"Small cytokines (intecrine/chemokine), interleukin-8 like","start":31,"end":88}],"gene3D":[{"start":24,"end":97,"id":"2.40.50.40","name":"2.40.50.40"}]},"uniref50":"UniRef50_P51671","sequence":"MKVSAALLWLLLIAAAFSPQGLAGPASVPTTCCFNLANRKIPLQRLESYRRITSGKCPQKAVIFKTKLAKDICADPKKKWVQDSMKYLDQKSPTPKP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P51671","disprot_id":"DP00641","ncbi_taxon_id":9606,"regions_counter":3,"creator":"droche","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":31,"region_id":"DP00641r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of eotaxin, a chemokine that selectively recruits eosinophils in allergic inflammation. <i> Crump MP, Rajarathnam K, Kim KS, Clark-Lewis I, Sykes BD. </i> J Biol Chem, 1998","term_id":"IDPO:0000002","curator_id":"droche","start":1,"term_ontology":"IDPO","curator_name":"Daniel Roche","reference_id":"9712872","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1EOT"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":31,"term_name":"molecular function regulator","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"GO","curator_name":"Daniel Roche","reference_id":"9712872","version":3,"reference_html":"Solution structure of eotaxin, a chemokine that selectively recruits eosinophils in allergic inflammation. <i> Crump MP, Rajarathnam K, Kim KS, Clark-Lewis I, Sykes BD. </i> J Biol Chem, 1998","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006165","region_id":"DP00641r002","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":31,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"GO","curator_name":"Daniel Roche","reference_id":"9712872","version":3,"reference_html":"Solution structure of eotaxin, a chemokine that selectively recruits eosinophils in allergic inflammation. <i> Crump MP, Rajarathnam K, Kim KS, Clark-Lewis I, Sykes BD. </i> J Biol Chem, 1998","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00641r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P51671","date":"2016-09-12T17:52:08.000Z","acc":"P51671","name":"Eotaxin","length":97,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000050AFD","genes":[{"name":{"value":"CCL11"},"synonyms":[{"value":"SCYA11"}]}],"alphafold_very_low_content":0.010309278350515464,"disorder_content":0.31958762886597936,"disprot_consensus":{"full":[{"start":1,"end":31,"type":"D"}],"Structural state":[{"start":1,"end":31,"type":"D"}],"Molecular function":[{"start":1,"end":31,"type":"F"}]}},{"features":{"pfam":[{"id":"PF15185","name":"Bcl-2-modifying factor, apoptosis","start":7,"end":183}]},"uniref50":"UniRef50_Q91ZE9","sequence":"MEPPQCVEELEDDVFQSEDGEPGTQPGGLLSADLFAQSQLDCPLSRLQLFPLTHCCGPGLRPISQEDKATQTLSPASPSQGVMLPCGVTEEPQRLFYGNAGYRLPLPASFPAGSPLGEQPPEGQFLQHRAEVQIARKLQCIADQFHRLHTQQHQQNRDRAWWQVFLFLQNLALNRQENREGVGPW","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q91ZE9","disprot_id":"DP00645","ncbi_taxon_id":10090,"regions_counter":8,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":185,"region_id":"DP00645r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16645638","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":185,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16645638","version":3,"reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00645r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":185,"region_id":"DP00645r003","released":"2022_03","ec_id":"ECO:0006275","reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16645638","version":2,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":185,"term_name":"protein binding","start":1,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16645638","version":3,"reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006275","region_id":"DP00645r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":185,"region_id":"DP00645r005","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16645638","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":185,"term_name":"protein binding","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16645638","version":3,"reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007680","region_id":"DP00645r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":185,"region_id":"DP00645r007","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16645638","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":185,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16645638","version":3,"reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00645r008","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q91ZE9","date":"2016-08-16T16:33:11.000Z","acc":"Q91ZE9","name":"Bcl-2-modifying factor","length":185,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000024738","genes":[{"name":{"value":"Bmf"}}],"alphafold_very_low_content":0.33513513513513515,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":185,"type":"D"}],"Structural state":[{"start":1,"end":185,"type":"D"}],"Molecular function":[{"start":1,"end":185,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00029","name":"Connexin","start":3,"end":231},{"id":"PF16791","name":"Connexin 40 C-terminal domain","start":258,"end":358}],"gene3D":[{"start":2,"end":242,"id":"1.20.1440.80","name":"Gap junction channel protein cysteine-rich domain"}]},"uniref50":"UniRef50_P36382","sequence":"MGDWSFLGEFLEEVHKHSTVIGKVWLTVLFIFRMLVLGTAAESSWGDEQADFRCDTIQPGCQNVCYDQAFPISHIRYWVLQIIFVSTPSLVYMGHAMHTVRMQEKQKLRDAEKAKEAHRTGAYEYPVAEKAELSCWKEVDGKIVLQGTLLNTYVCTILIRTTMEVAFIVGQYLLYGIFLDTLHVCRRSPCPHPVNCYVSRPTEKNVFIVFMMAVAGLSLFLSLAELYHLGWKKIRQRFGKSRQGVDKHQLPGPPTSLVQSLTPPPDFNQCLKNSSGEKFFSDFSNNMGSRKNPDALATGEVPNQEQIPGEGFIHMHYSQKPEYASGASAGHRLPQGYHSDKRRLSKASSKARSDDLSV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q01231","disprot_id":"DP00646","ncbi_taxon_id":10090,"regions_counter":6,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":355,"region_id":"DP00646r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains. <i> Bouvier D, Spagnol G, Chenavas S, Kieken F, Vitrac H, Brownell S, Kellezi A, Forge V, Sorgen PL. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"fquaglia","start":251,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19808665","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2K7M"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":355,"term_name":"protein binding","start":251,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19808665","version":3,"reference_html":"Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains. <i> Bouvier D, Spagnol G, Chenavas S, Kieken F, Vitrac H, Brownell S, Kellezi A, Forge V, Sorgen PL. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00646r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":355,"region_id":"DP00646r003","released":"2022_03","ec_id":"ECO:0006228","reference_html":"Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains. <i> Bouvier D, Spagnol G, Chenavas S, Kieken F, Vitrac H, Brownell S, Kellezi A, Forge V, Sorgen PL. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"fquaglia","start":251,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19808665","version":2,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2K7M"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":355,"term_name":"protein binding","start":251,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19808665","version":3,"reference_html":"Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains. <i> Bouvier D, Spagnol G, Chenavas S, Kieken F, Vitrac H, Brownell S, Kellezi A, Forge V, Sorgen PL. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006228","region_id":"DP00646r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":355,"region_id":"DP00646r005","released":"2022_03","ec_id":"ECO:0006206","reference_html":"Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains. <i> Bouvier D, Spagnol G, Chenavas S, Kieken F, Vitrac H, Brownell S, Kellezi A, Forge V, Sorgen PL. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"fquaglia","start":251,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19808665","version":2,"ec_name":"near-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2K7M"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":355,"term_name":"protein binding","start":251,"ec_name":"near-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19808665","version":3,"reference_html":"Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains. <i> Bouvier D, Spagnol G, Chenavas S, Kieken F, Vitrac H, Brownell S, Kellezi A, Forge V, Sorgen PL. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006206","region_id":"DP00646r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q01231","date":"2016-08-29T10:42:42.000Z","acc":"Q01231","name":"Gap junction alpha-5 protein","length":358,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000026528","genes":[{"name":{"value":"Gja5"},"synonyms":[{"value":"Cxn-40"}]}],"alphafold_very_low_content":0.3463687150837989,"disorder_content":0.29329608938547486,"disprot_consensus":{"full":[{"start":251,"end":355,"type":"D"}],"Structural state":[{"start":251,"end":355,"type":"D"}],"Molecular function":[{"start":251,"end":355,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00080","name":"Copper/zinc superoxide dismutase (SODC)","start":15,"end":150}],"gene3D":[{"start":2,"end":154,"id":"2.60.40.200","name":"Superoxide dismutase, copper/zinc binding domain"}]},"uniref50":"UniRef50_P00441","sequence":"MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P00441","disprot_id":"DP00652","ncbi_taxon_id":9606,"regions_counter":8,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":78,"region_id":"DP00652r001","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A. <i> Galaleldeen A, Strange RW, Whitson LJ, Antonyuk SV, Narayana N, Taylor AB, Schuermann JP, Holloway SP, Hasnain SS, Hart PJ. </i> Arch Biochem Biophys, 2009","term_id":"IDPO:0000002","curator_id":"vnugnes","start":69,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19800308","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-05-22T15:33:20.673Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3GZQ"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala5Val","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"}],"statement":[{"text":"Residues 67–79 and 126–141 are disordered and not visible in the electron density.","type":"Results"},{"text":"The A4V variant is responsible for the majority of familial ALS cases in North America, causing rapidly progressing paralysis once symptoms begin and the G93A SOD1 variant is overexpressed in often studied murine models of the disease.","type":"Introduction"},{"text":"In the metal-free structures, the metal-binding loop elements are observed to be severely disordered, suggesting that these variants may share mechanisms of aggregation proposed previously for other pathogenic SOD1.","type":"Introduction"},{"text":"Authors refer to the Ala5Val substitution accordingly to the UniProt sequence.","type":"Curator statement"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":142,"region_id":"DP00652r003","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A. <i> Galaleldeen A, Strange RW, Whitson LJ, Antonyuk SV, Narayana N, Taylor AB, Schuermann JP, Holloway SP, Hasnain SS, Hart PJ. </i> Arch Biochem Biophys, 2009","term_id":"IDPO:0000002","curator_id":"vnugnes","start":127,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19800308","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-05-22T15:33:04.675Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3GZQ"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala5Val","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"}],"statement":[{"text":"Residues 67–79 and 126–141 are disordered and not visible in the electron density.","type":"Results"},{"text":"The A4V variant is responsible for the majority of familial ALS cases in North America, causing rapidly progressing paralysis once symptoms begin and the G93A SOD1 variant is overexpressed in often studied murine models of the disease.","type":"Introduction"},{"text":"In the metal-free structures, the metal-binding loop elements are observed to be severely disordered, suggesting that these variants may share mechanisms of aggregation proposed previously for other pathogenic SOD1.","type":"Introduction"},{"text":"Authors refer to the Ala5Val substitution accordingly to the UniProt sequence.","type":"Curator statement"}]},{"start":127,"end":142,"reference_id":"15056757","reference_source":"pmid","reference_html":"Dimer destabilization in superoxide dismutase may result in disease-causing properties: structures of motor neuron disease mutants. <i> Hough MA, Grossmann JG, Antonyuk SV, Strange RW, Doucette PA, Rodriguez JA, Whitson LJ, Hart PJ, Hayward LJ, Valentine JS, Hasnain SS. </i> Proc Natl Acad Sci U S A, 2004","date":"2023-11-24T10:57:23.202Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala5Val","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"1UXM"}],"region_id":"DP00652r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:27099"}],"statement":[{"text":"The molecules of A4V and I113T mutant SOD1 pack into the crystals in a so-called “trimer-of-dimers” motif (Fig. 5, which is published as supporting information on the PNAS web site), involving primarily interactions between residues 128–131 of the electrostatic loop in one molecule and Thr-88, Ser-96, and Ser-98 from the Zn loop of a second SOD1 molecule.","type":"Results"},{"text":"The overall fold observed for wtSOD (12, 13, 34) is largely preserved in the A4V and I113T mutants.","type":"Results"},{"text":"When interacting with Cu+2 and Zn+2 ions, this region of the pathogenic variant (with the mutation Ala5Val, according to the UniProt sequence) is structured.","type":"Curator statement"}]},{"start":69,"end":78,"reference_id":"15056757","reference_source":"pmid","reference_html":"Dimer destabilization in superoxide dismutase may result in disease-causing properties: structures of motor neuron disease mutants. <i> Hough MA, Grossmann JG, Antonyuk SV, Strange RW, Doucette PA, Rodriguez JA, Whitson LJ, Hart PJ, Hayward LJ, Valentine JS, Hasnain SS. </i> Proc Natl Acad Sci U S A, 2004","date":"2023-11-24T10:57:39.527Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala5Val","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"1UXM"}],"region_id":"DP00652r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:27099"}],"statement":[{"text":"The molecules of A4V and I113T mutant SOD1 pack into the crystals in a so-called “trimer-of-dimers” motif (Fig. 5, which is published as supporting information on the PNAS web site), involving primarily interactions between residues 128–131 of the electrostatic loop in one molecule and Thr-88, Ser-96, and Ser-98 from the Zn loop of a second SOD1 molecule.","type":"Results"},{"text":"The overall fold observed for wtSOD (12, 13, 34) is largely preserved in the A4V and I113T mutants.","type":"Results"},{"text":"When interacting with Cu+2 and Zn+2 ions, this region of the pathogenic variant (with the mutation Ala5Val, according to the UniProt sequence) is structured.","type":"Curator statement"}]},{"start":69,"end":78,"reference_id":"19800308","reference_source":"pmid","reference_html":"Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A. <i> Galaleldeen A, Strange RW, Whitson LJ, Antonyuk SV, Narayana N, Taylor AB, Schuermann JP, Holloway SP, Hasnain SS, Hart PJ. </i> Arch Biochem Biophys, 2009","date":"2023-11-24T10:58:37.371Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala5Val","start":null,"end":null,"position":null}],"cross_refs":[{"db":"DisProt","id":"DP00652r006"},{"db":"PDB","id":"3GZQ"}],"region_id":"DP00652r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:27099"}],"statement":[{"text":"As expected, crystal structures of metal-bound forms of A4V SOD1 [30] and metal-bound and metal-reconstituted forms of G93A SOD1 (this study) are similar to that of the wild type enzyme in that they possess well-ordered zinc loop (loop IV, residues 50–83) and electrostatic loop (loop VII, residues 121–142) elements. The molecular basis for why the binding of metal ions (particularly zinc) exerts a stabilizing effect on the conformation of these loop elements is shown in Figure 1. First, in the Cu(II) form of the enzyme, H63 of the zinc loop bridges the copper and zinc ions. This “primary bridge”, also known as the “bridging imidazolate”, is a metal ion coordinating feature unique to SOD1 [51]. Second, the binding of zinc to the zinc-binding site by amino acid residues H63, H71, H80, and D83, induces the zinc loop to adopt a structure in which the proline residues at positions 62, 66, and 74 adopt the trans conformation [17, 52].","type":"Discussion"},{"text":"This region of the pathogenic variant (with the mutation Ala5Val, according to the UniProt sequence) is disordered in solution but when interacting with Cu+2 and Zn+2 ions gets structure, as shown in the cited publication (pmid:15056757, PDB 1UXM)","type":"Curator statement"}],"states_connection":[{"source":"DP00652r001","target":"DP00652r006"}]},{"start":127,"end":142,"reference_id":"19800308","reference_source":"pmid","reference_html":"Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A. <i> Galaleldeen A, Strange RW, Whitson LJ, Antonyuk SV, Narayana N, Taylor AB, Schuermann JP, Holloway SP, Hasnain SS, Hart PJ. </i> Arch Biochem Biophys, 2009","date":"2023-11-24T10:58:25.624Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala5Val","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"3GZQ"},{"db":"DisProt","id":"DP00652r005"}],"region_id":"DP00652r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:27099"}],"statement":[{"text":"As expected, crystal structures of metal-bound forms of A4V SOD1 [30] and metal-bound and metal-reconstituted forms of G93A SOD1 (this study) are similar to that of the wild type enzyme in that they possess well-ordered zinc loop (loop IV, residues 50–83) and electrostatic loop (loop VII, residues 121–142) elements. The molecular basis for why the binding of metal ions (particularly zinc) exerts a stabilizing effect on the conformation of these loop elements is shown in Figure 1. First, in the Cu(II) form of the enzyme, H63 of the zinc loop bridges the copper and zinc ions. This “primary bridge”, also known as the “bridging imidazolate”, is a metal ion coordinating feature unique to SOD1 [51]. Second, the binding of zinc to the zinc-binding site by amino acid residues H63, H71, H80, and D83, induces the zinc loop to adopt a structure in which the proline residues at positions 62, 66, and 74 adopt the trans conformation [17, 52].","type":"Discussion"},{"text":"This region of the pathogenic variant (with the mutation Ala5Val, according to the UniProt sequence) is disordered in solution but when interacting with Cu+2 and Zn+2 ions gets structure, as shown in the cited publication (pmid:15056757, PDB 1UXM)","type":"Curator statement"}],"states_connection":[{"source":"DP00652r003","target":"DP00652r005"}]}],"released":"2016_10","uniref100":"UniRef100_P00441","date":"2016-09-14T15:08:47.000Z","acc":"P00441","name":"Superoxide dismutase [Cu-Zn]","length":154,"organism":"Homo sapiens","dataset":["NDDs-related proteins","Age-related disorders proteins"],"UniParc":"UPI000002D045","genes":[{"name":{"value":"SOD1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11179","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11179"}}]}}],"alphafold_very_low_content":0,"disorder_content":0.16883116883116883,"disprot_consensus":{"full":[{"start":69,"end":78,"type":"T"},{"start":127,"end":142,"type":"T"}],"Structural state":[{"start":69,"end":78,"type":"D"},{"start":127,"end":142,"type":"D"}],"Structural transition":[{"start":69,"end":78,"type":"T"},{"start":127,"end":142,"type":"T"}]}},{"features":{"pfam":[{"id":"PF01608","name":"I/LWEQ domain","start":2386,"end":2531},{"id":"PF02174","name":"PTB domain (IRS-1 type)","start":313,"end":400},{"id":"PF08913","name":"Vinculin Binding Site","start":1849,"end":1973},{"id":"PF09141","name":"Talin, middle domain","start":491,"end":652},{"id":"PF16511","name":"N-terminal or F0 domain of Talin-head FERM","start":4,"end":83},{"id":"PF21692","name":"Talin, R4 domain","start":916,"end":1041},{"id":"PF21865","name":"Talin 1-like, rod segment domain","start":1210,"end":1354},{"id":"PF21865","name":"Talin 1-like, rod segment domain","start":1657,"end":1822},{"id":"PF21865","name":"Talin 1-like, rod segment domain","start":1975,"end":2139},{"id":"PF21896","name":"Talin IBS2B domain","start":1045,"end":1206},{"id":"PF21896","name":"Talin IBS2B domain","start":1463,"end":1579},{"id":"PF21896","name":"Talin IBS2B domain","start":2142,"end":2289},{"id":"PF25177","name":"Talin VBS2 domain","start":794,"end":909}],"gene3D":[{"start":201,"end":307,"id":"1.20.80.10","name":"1.20.80.10"},{"start":308,"end":405,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":482,"end":655,"id":"1.20.1420.10","name":"Talin, central domain"},{"start":1657,"end":1824,"id":"1.20.1420.10","name":"Talin, central domain"},{"start":1205,"end":1357,"id":"1.20.1420.10","name":"Talin, central domain"},{"start":2295,"end":2482,"id":"1.20.1410.10","name":"I/LWEQ domain"},{"start":2141,"end":2293,"id":"1.20.1420.10","name":"Talin, central domain"},{"start":1358,"end":1656,"id":"1.20.1420.10","name":"Talin, central domain"},{"start":80,"end":200,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"},{"start":910,"end":1042,"id":"1.20.120.230","name":"Alpha-catenin/vinculin-like"},{"start":1043,"end":1204,"id":"1.20.1420.10","name":"Talin, central domain"},{"start":786,"end":909,"id":"1.20.120.230","name":"Alpha-catenin/vinculin-like"},{"start":1457,"end":1586,"id":"1.20.120.230","name":"Alpha-catenin/vinculin-like"},{"start":1,"end":79,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"},{"start":1971,"end":2140,"id":"1.20.1420.10","name":"Talin, central domain"},{"start":1846,"end":1970,"id":"1.20.120.230","name":"Alpha-catenin/vinculin-like"}]},"uniref50":"UniRef50_Q9Y490","sequence":"MVALSLKISIGNVVKTMQFEPSTMVYDACRMIRERIPEALAGPPNDFGLFLSDDDPKKGIWLEAGKALDYYMLRNGDTMEYRKKQRPLKIRMLDGTVKTIMVDDSKTVTDMLMTICARIGITNHDEYSLVRELMEEKKDEGTGTLRKDKTLLRDEKKMEKLKQKLHTDDELNWLDHGRTLREQGVEEHETLLLRRKFFYSDQNVDSRDPVQLNLLYVQARDDILNGSHPVSFDKACEFAGFQCQIQFGPHNEQKHKAGFLDLKDFLPKEYVKQKGERKIFQAHKNCGQMSEIEAKVRYVKLARSLKTYGVSFFLVKEKMKGKNKLVPRLLGITKECVMRVDEKTKEVIQEWSLTNIKRWAASPKSFTLDFGDYQDGYYSVQTTEGEQIAQLIAGYIDIILKKKKSKDHFGLEGDEESTMLEDSVSPKKSTVLQQQYNRVGKVEHGSVALPAIMRSGASGPENFQVGSMPPAQQQITSGQMHRGHMPPLTSAQQALTGTINSSMQAVQAAQATLDDFETLPPLGQDAASKAWRKNKMDESKHEIHSQVDAITAGTASVVNLTAGDPAETDYTAVGCAVTTISSNLTEMSRGVKLLAALLEDEGGNGRPLLQAAKGLAGAVSELLRSAQPASAEPRQNLLQAAGNVGQASGELLQQIGESDTDPHFQDVLMQLAKAVASAAAALVLKAKSVAQRTEDSGLQTQVIAAATQCALSTSQLVACTKVVAPTISSPVCQEQLVEAGRLVAKAVEGCVSASQAATEDGQLLRGVGAAATAVTQALNELLQHVKAHATGAGPAGRYDQATDTILTVTENIFSSMGDAGEMVRQARILAQATSDLVNAIKADAEGESDLENSRKLLSAAKILADATAKMVEAAKGAAAHPDSEEQQQRLREAAEGLRMATNAAAQNAIKKKLVQRLEHAAKQAAASATQTIAAAQHAASAPKASAGPQPLLVQSCKAVAEQIPLLVQGVRGSQAQPDSPSAQLALIAASQSFLQPGGKMVAAAKASVPTIQDQASAMQLSQCAKNLGTALAELRTAAQKAQEACGPLEMDSALSVVQNLEKDLQEIKAAARDGKLKPLPGETMEKCTQDLGNSTKAVSSAIAKLLGEIAQGNENYAGIAARDVAGGLRSLAQAARGVAALTSDPAVQAIVLDTASDVLDKASSLIEEAKKASGHPGDPESQQRLAQVAKAVTQALNRCVSCLPGQRDVDNALRAVGDASKRLLSDSLPPSTGTFQEAQSRLNEAAAGLNQAATELVQASRGTPQDLARASGRFGQDFSTFLEAGVEMAGQAPSQEDRAQVVSNLKGISMSSSKLLLAAKALSTDPASPNLKSQLAAAARAVTDSINQLITMCTQQAPGQKECDNALRQLETVRELLENPVQPINDMSYFGCLDSVMENSKVLGEAMTGISQNAKNGNLPEFGDAIATASKALCGFTEAAAQAAYLVGVSDPNSQAGQQGLVEPTQFARANQAIQMACQSLGEPGCTQAQVLSAATIVAKHTSALCNSCRLASARTANPTAKRQFVQSAKEVANSTANLVKTIKALDGDFTEENRAQCRAATAPLLEAVDNLSAFASNPEFSSVPAQISPEGRAAMEPIVISAKTMLESAGGLIQTARALAVNPRDPPRWSVLAGHSRTVSDSIKKLITSMRDKAPGQLECETAIAALNSCLRDLDQASLAAVSQQLAPREGISQEALHTQMLTAVQEISHLIEPLASAARAEASQLGHKVSQMAQYFEPLTLAAVGAASKTLSHPQQMALLDQTKTLAESALQLLYTAKEAGGNPKQAAHTQEALEEAVQMMTEAVEDLTTTLNEAASAAGVVGGMVDSITQAINQLDEGPMGDPEGSFVDYQTTMVRTAKAIAVTVQEMVTKSNTSPEELGPLANQLTSDYGRLASQAKPAAVAAENEEIGAHIKHRVQELGHGCSALVTKAGALQCSPSDVYTKKELIECARRVSEKVSHVLAALQAGNRGTQACITAASAVSGIIADLDTTIMFATAGTLNREGAETFADHREGILKTAKVLVEDTKVLVQNAAGSQEKLAQAAQSSVATITRLADVVKLGAASLGAEDPETQVVLINAVKDVAKALGDLISATKAAAGKVGDDPAVWQLKNSAKVMVTNVTSLLKTVKAVEDEATKGTRALEATTEHIRQELAVFCSPEPPAKTSTPEDFIRMTKGITMATAKAVAAGNSCRQEDVIATANLSRRAIADMLRACKEAAFHPEVAPDVRLRALHYGRECANGYLELLDHVLLTLQKPNPDLKQQLTGHSKRVAGSVTELIQAAEAMKGTEWVDPEDPTVIAENELLGAAAAIEAAAKKLEQLKPRAKPKEADESLNFEEQILEAAKSIAAATSALVKAASAAQRELVAQGKVGAIPANALDDGQWSQGLISAARMVAAATNNLCEAANAAVQGHASQEKLISSAKQVAASTAQLLVACKVKADQDSEAMKRLQAAGNAVKRASDNLVKAAQKAAAFEDQENETVVVKEKMVGGIAQIIAAQEEMLRKERELEEARKKLAQIRQQQYKFLPSELRDEH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q9Y490","disprot_id":"DP00653","ncbi_taxon_id":10090,"regions_counter":4,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":814,"region_id":"DP00653r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle. <i> Papagrigoriou E, Gingras AR, Barsukov IL, Bate N, Fillingham IJ, Patel B, Frank R, Ziegler WH, Roberts GC, Critchley DR, Emsley J. </i> EMBO J, 2004","term_id":"IDPO:0000002","curator_id":"jpujols","start":799,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1U89"}],"reference_id":"15272303","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":814,"term_name":"order to disorder","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle. <i> Papagrigoriou E, Gingras AR, Barsukov IL, Bate N, Fillingham IJ, Patel B, Frank R, Ziegler WH, Roberts GC, Critchley DR, Emsley J. </i> EMBO J, 2004","term_id":"IDPO:0000014","curator_id":"jpujols","start":799,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","reference_id":"15272303","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00653r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":168,"region_id":"DP00653r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The Structure of the talin head reveals a novel extended conformation of the FERM domain. <i> Elliott PR, Goult BT, Kopp PM, Bate N, Grossmann JG, Roberts GC, Critchley DR, Barsukov IL. </i> Structure, 2010","term_id":"IDPO:0000002","curator_id":"jpujols","start":139,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3IVF"}],"reference_id":"20947018","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":168,"term_name":"flexible linker","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The Structure of the talin head reveals a novel extended conformation of the FERM domain. <i> Elliott PR, Goult BT, Kopp PM, Bate N, Grossmann JG, Roberts GC, Critchley DR, Barsukov IL. </i> Structure, 2010","term_id":"IDPO:0000033","curator_id":"jpujols","start":139,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","reference_id":"20947018","version":3,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00653r004","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_P26039","date":"2016-09-18T09:42:21.000Z","acc":"P26039","name":"Talin-1","length":2541,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000273F0","genes":[{"name":{"value":"Tln1"},"synonyms":[{"value":"Tln"}]}],"alphafold_very_low_content":0.05470287288469106,"disorder_content":0.01810310901219992,"disprot_consensus":{"full":[{"start":139,"end":168,"type":"D"},{"start":799,"end":814,"type":"T"}],"Structural state":[{"start":139,"end":168,"type":"D"},{"start":799,"end":814,"type":"D"}],"Structural transition":[{"start":799,"end":814,"type":"T"}],"Disorder function":[{"start":139,"end":168,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00378","name":"Enoyl-CoA hydratase/isomerase","start":16,"end":205},{"id":"PF00725","name":"3-hydroxyacyl-CoA dehydrogenase, C-terminal domain","start":495,"end":588},{"id":"PF02737","name":"3-hydroxyacyl-CoA dehydrogenase, NAD binding domain","start":314,"end":492}],"gene3D":[{"start":1,"end":311,"id":"3.90.226.10","name":"2-enoyl-CoA Hydratase; Chain A, domain 1"},{"start":312,"end":495,"id":"3.40.50.720","name":"NAD(P)-binding Rossmann-like Domain"},{"start":496,"end":710,"id":"1.10.1040.50","name":"1.10.1040.50"}]},"uniref50":"UniRef50_Q9ZPI5","sequence":"MDSRTKGKTVMEVGGDGVAVITLINPPVNSLSFDVLYNLKSNYEEALSRNDVKAIVITGAKGRFSGGFDISGFGEMQKGNVKEPKAGYISIDIITDLLEAARKPSVAAIDGLALGGGLELAMACHARISAPAAQLGLPELQLGVIPGFGGTQRLPRLVGLTKALEMILTSKPVKAEEGHSLGLIDAVVPPAELVTTARRWALDIVGRRKPWVSSVSKTDKLPPLGEAREILTFAKAQTLKRAPNMKHPLMCLDAIEVGIVSGPRAGLEKEAEVASQVVKLDTTKGLIHVFFSQRGTAKVPGVTDRGLVPRKIKKVAIIGGGLMGSGIATALILSNYPVILKEVNEKFLEAGIGRVKANLQSRVRKGSMSQEKFEKTMSLLKGSLDYESFRDVDMVIEAVIENISLKQQIFADLEKYCPQHCILASNTSTIDLNKIGERTKSQDRIVGAHFFSPAHIMPLLEIVRTNHTSAQVIVDLLDVGKKIKKTPVVVGNCTGFAVNRMFFPYTQAAMFLVECGADPYLIDRAISKFGMPMGPFRLCDLVGFGVAIATATQFIENFSERTYKSMIIPLMQEDKRAGEATRKGFYLYDDKRKAKPDPELKKYIEKARSISGVKLDPKLANLSEKDIIEMTFFPVVNEACRVFAEGIAVKAADLDIAGIMGMGFPPYRGGIMFWADSIGSKYIYSRLDEWSKAYGEFFKPCAFLAERGSKGVLLSAPVKQASSRL","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q9ZPI5","disprot_id":"DP00654","ncbi_taxon_id":3702,"regions_counter":2,"creator":"ktsirigos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":82,"region_id":"DP00654r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The multifunctional protein in peroxisomal beta-oxidation: structure and substrate specificity of the Arabidopsis thaliana protein MFP2. <i> Arent S, Christensen CE, Pye VE, Nørgaard A, Henriksen A. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":71,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"20463021","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":596,"region_id":"DP00654r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The multifunctional protein in peroxisomal beta-oxidation: structure and substrate specificity of the Arabidopsis thaliana protein MFP2. <i> Arent S, Christensen CE, Pye VE, Nørgaard A, Henriksen A. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":576,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"20463021","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q9ZPI5","date":"2016-09-13T11:54:35.000Z","acc":"Q9ZPI5","name":"Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2","length":725,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI00000AC7AF","genes":[{"name":{"value":"MFP2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10521521","url":"http://www.ncbi.nlm.nih.gov/pubmed/10521521","alternativeUrl":"https://europepmc.org/abstract/MED/10521521"}}]},"orfNames":[{"value":"F17A9.1","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAF26990.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF26990.1"}}]}],"olnNames":[{"value":"At3g06860","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT3G06860","url":""}}]}]}],"alphafold_very_low_content":0.012413793103448275,"disorder_content":0.04551724137931035,"disprot_consensus":{"full":[{"start":71,"end":82,"type":"D"},{"start":576,"end":596,"type":"D"}],"Structural state":[{"start":71,"end":82,"type":"D"},{"start":576,"end":596,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00373","name":"FERM central domain","start":281,"end":330},{"id":"PF00373","name":"FERM central domain","start":454,"end":570},{"id":"PF18124","name":"Kindlin-2 N-terminal domain","start":9,"end":95}],"gene3D":[{"start":370,"end":509,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":565,"end":659,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":1,"end":98,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"}]},"uniref50":"UniRef50_Q9BQL6","sequence":"MLSSGDLTSASWELVVRVDHANGEQQTEITLRVSGDLHIGGVMLKLVEQMNIAQDWSDYALWWEQKRCWLLKTHWTLDKCGVQADANLLFTPQHKMLRLRLPNAKTVRLRVSFSAVVFKAVADICKVLNIRRPEELSLLKPSSDYCKKKKKKEKNSKEPVIEDILNLESSSTSSGSPVSPGLYSKTMTPTYDPINGTPALSTMTWFGDSPLTEQNCSVLAFSQPPPSPDVLADMFQPRSLVDKAKMNAGWLDSSRSLMEQSIQEDEQLQLRFKYYTFFDLNPKYDAVRINQLYEQARWAVLLEEIDCTEEEMLIFAALQYHISKLSQCAEIQDFATKSEVDEVEAALSSLEVTLEGGKADNTLEDITDIPKLADYLKLFRPKKLMLKACKQYWFVFKDTSIAYFKNKELEQGEPIEKLNLRGCEIVPDVNVSGRKFGIKLLIPVADGMNEVYLRCDHEDQYARWMAACILASKGKTMADSSYQPEVISILSFLKMKNRNSSPLVASSLENMDMNPECLVSPCCAKKHKSKQLAARILEAHHNVAQMPLVEAKLQFIQAWQSLPEFGLTYYLVRFKGSKKDDILGVAYNRLIRIDAVTGIPVTTWRFANMKQWNVNWEIRQVAIEFDQNVSIAFTCLSADCKIVHEYIGGYIFLSTRSKDQNETLDEDLFHKLTGGQD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P59113","disprot_id":"DP00655","ncbi_taxon_id":10090,"regions_counter":3,"creator":"agasparini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":249,"region_id":"DP00655r001","released":"2022_12","ec_id":"ECO:0006165","reference_html":"The structure of the N-terminus of kindlin-1: a domain important for alphaiibbeta3 integrin activation. <i> Goult BT, Bouaouina M, Harburger DS, Bate N, Patel B, Anthis NJ, Campbell ID, Calderwood DA, Barsukov IL, Roberts GC, Critchley DR. </i> J Mol Biol, 2009","term_id":"IDPO:0000002","curator_id":"vnugnes","start":141,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19804783","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-08-22T18:18:34.482Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"(b) 1-->H–15-->N HSQC spectrum of the F1 insert shows that it is predominantly unstructured as indicated by the poor signal dispersion, although some weaker signals may suggest some ordered elements.","type":"Supplementary material"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":11,"region_id":"DP00655r003","released":"2022_12","ec_id":"ECO:0006165","reference_html":"The structure of the N-terminus of kindlin-1: a domain important for alphaiibbeta3 integrin activation. <i> Goult BT, Bouaouina M, Harburger DS, Bate N, Patel B, Anthis NJ, Campbell ID, Calderwood DA, Barsukov IL, Roberts GC, Critchley DR. </i> J Mol Biol, 2009","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19804783","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-08-22T18:08:51.353Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2KMC"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"In the talin F0 structure, the secondary-structure elements begin at residue 3, but in kindlin-1, there are an additional 11 residues (MLSSGDLTSAS) at the N-terminus, which are unstructured (Fig. 2b), as indicated by the lack of long-range nuclear Overhauser enhancements (NOEs).","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P59113","date":"2016-08-23T16:46:18.000Z","acc":"P59113","name":"Fermitin family homolog 1","length":677,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000193621","genes":[{"name":{"value":"Fermt1"},"synonyms":[{"value":"Kind1"},{"value":"Urp1"}]}],"alphafold_very_low_content":0.16248153618906944,"disorder_content":0.17725258493353027,"disprot_consensus":{"full":[{"start":1,"end":11,"type":"D"},{"start":141,"end":249,"type":"D"}],"Structural state":[{"start":1,"end":11,"type":"D"},{"start":141,"end":249,"type":"D"}]}},{"acc":"P07674","sequence":"MTAAQAKTTKKNTAAAAQEAAGAAQPSGLGLDSIGDLSSLLDAPAASQGGSGPIELDLDLIDEDPHQPRTADNPGFSPESIAEIGATIKERGVKSPISVRENQEQPGRYIINHGARRYRGSKWAGKKSIPAFIDNDYNEADQVIENLQRNELTPREIADFIGRELAKGKKKGDIAKEIGKSPAFITQHVTLLDLPEKIADAFNTGRVRDVTVVNELVTAFKKRPEEVEAWLDDDTQEITRGTVKLLREFLDEKGRDPNTVDAFNGQTDAERDAEAGDGQDGEDGDQDGKDAKEKGAKEPDPDKLKKAIVQVEHDERPARLILNRRPPAEGYAWLKYEDDGQEFEANLADVKLVALIEG","alphafold_very_low_content":"0.17597765363128492","creator":"fquaglia","dataset":[],"date":"2016-08-29T11:08:18.000Z","disprot_id":"DP00656","features":{"pfam":[{"id":"PF02195","name":"ParB N-terminal domain","start":55,"end":139},{"id":"PF06613","name":"KorB C-terminal beta-barrel domain","start":300,"end":358},{"id":"PF08535","name":"KorB domain","start":167,"end":253}],"gene3D":[{"start":297,"end":358,"id":"2.30.30.150","name":"KorB, C-terminal domain","_id":"685af523b4ac24d5329d809e"},{"start":139,"end":194,"id":"1.10.10.730","name":"KorB DNA-binding domain","_id":"685af523b4ac24d5329d809f"},{"start":67,"end":135,"id":"3.90.1530.30","name":"3.90.1530.30","_id":"685af523b4ac24d5329d80a0"}]},"genes":[{"name":{"value":"korB","evidences":[],"_id":"685af523b4ac24d5329d80d8"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d80d7"}],"length":358,"name":"Transcriptional repressor protein KorB","ncbi_taxon_id":562,"organism":"Escherichia coli","regions_counter":24,"released":"2016_10","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"UniParc":"UPI000011F55B","uniref100":"UniRef100_P07674","uniref50":"UniRef50_P07674","uniref90":"UniRef90_P07674","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006198","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":252,"end":294,"interaction_partner":[],"reference_html":"Order and disorder in the domain organization of the plasmid partition protein KorB. <i> Rajasekar K, Muntaha ST, Tame JRH, Kommareddy S, Morris G, Wharton CW, Thomas CM, White SA, Hyde EI, Scott DJ. </i> J Biol Chem, 2010","reference_id":"20200158","region_id":"DP00656r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"WT KorB, (N⌬150)KorB, (C⌬60)KorB, and (C⌬105)KorB all exhibited a definite peak in the Kratky plots, a signature of globular structure, although the\ndata did not go to zero at high Q value. This is indicative of some\ndegree of random coil component (40), again in line with the predictions of intrinsic disorder and the CD (Fig. 2B) and NMR (Fig. 3) measurements.","_id":"685af523b4ac24d5329d80b6"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d80b5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006198","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":252,"end":294,"interaction_partner":[],"reference_html":"Order and disorder in the domain organization of the plasmid partition protein KorB. <i> Rajasekar K, Muntaha ST, Tame JRH, Kommareddy S, Morris G, Wharton CW, Thomas CM, White SA, Hyde EI, Scott DJ. </i> J Biol Chem, 2010","reference_id":"20200158","region_id":"DP00656r012","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"The disordered regions are also likely to be important for\nDNA partitioning, as many of the partition proteins need to\nspan two DNA duplexes (or several proteins) to carry out their\nfunction. Flexible interactions between the central and C-terminal domains of a ParB protein have been seen in the crystal\nstructures of central and C-terminal domains of ParB from P1\nplasmid of Escherichia coli bound to different target sequences","_id":"685af523b4ac24d5329d80b8"}],"states_connection":[],"term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","version":4,"_id":"685af523b4ac24d5329d80b7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":252,"end":294,"interaction_partner":[],"reference_html":"Order and disorder in the domain organization of the plasmid partition protein KorB. <i> Rajasekar K, Muntaha ST, Tame JRH, Kommareddy S, Morris G, Wharton CW, Thomas CM, White SA, Hyde EI, Scott DJ. </i> J Biol Chem, 2010","reference_id":"20200158","region_id":"DP00656r015","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The secondary structure content determined from the CD\nanalysis for (N⌬297)KorB agrees well with the crystal structure\nof this domain, whereas that of (N⌬150)KorB agrees with that\npredicted from the two known crystal structures of KorB with\nrandom coil at residues 251–297","_id":"685af523b4ac24d5329d80be"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d80bd","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":252,"end":294,"interaction_partner":[],"reference_html":"Order and disorder in the domain organization of the plasmid partition protein KorB. <i> Rajasekar K, Muntaha ST, Tame JRH, Kommareddy S, Morris G, Wharton CW, Thomas CM, White SA, Hyde EI, Scott DJ. </i> J Biol Chem, 2010","reference_id":"20200158","region_id":"DP00656r016","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"The disordered regions are also likely to be important for\nDNA partitioning, as many of the partition proteins need to\nspan two DNA duplexes (or several proteins) to carry out their\nfunction. Flexible interactions between the central and C-ter-\nminal domains of a ParB protein have been seen in the crystal\nstructures of central and C-terminal domains of ParB from P1\nplasmid of Escherichia coli bound to different target sequences","_id":"685af523b4ac24d5329d80c0"}],"states_connection":[],"term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","version":4,"_id":"685af523b4ac24d5329d80bf","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1R71","_id":"685af523b4ac24d5329d80c6"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":117,"end":137,"interaction_partner":[],"reference_html":"Sequence-specific DNA binding determined by contacts outside the helix-turn-helix motif of the ParB homolog KorB. <i> Khare D, Ziegelin G, Lanka E, Heinemann U. </i> Nat Struct Mol Biol, 2004","reference_id":"15170177","region_id":"DP00656r019","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"The KorB-N domain, for which no structural information is available, is probably connected to helix 1 of KorB-O via a flexible linker, as indicated by residues Arg117–Tyr137, which are disordered in the crystal structure of the KorB-O–DNA complex.","_id":"685af523b4ac24d5329d80c7"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-30T09:09:28.461Z","_id":"685af523b4ac24d5329d80c8"},"version":3,"_id":"685af523b4ac24d5329d80c5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":117,"end":137,"interaction_partner":[],"reference_html":"Sequence-specific DNA binding determined by contacts outside the helix-turn-helix motif of the ParB homolog KorB. <i> Khare D, Ziegelin G, Lanka E, Heinemann U. </i> Nat Struct Mol Biol, 2004","reference_id":"15170177","region_id":"DP00656r020","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"The KorB-N domain, for which no structural information is available, is probably connected to helix 1 of KorB-O via a flexible linker, as indicated by residues Arg117–Tyr137, which are disordered in the crystal structure of the KorB-O–DNA complex.","_id":"685af523b4ac24d5329d80ca"}],"states_connection":[],"term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","version":4,"_id":"685af523b4ac24d5329d80c9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":50,"interaction_partner":[],"reference_html":"Order and disorder in the domain organization of the plasmid partition protein KorB. <i> Rajasekar K, Muntaha ST, Tame JRH, Kommareddy S, Morris G, Wharton CW, Thomas CM, White SA, Hyde EI, Scott DJ. </i> J Biol Chem, 2010","reference_id":"20200158","region_id":"DP00656r021","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In all cases, the CD suggests that the N-terminal 50 amino acids of KorB and the linker between the central and DNA-binding domains are unstructured","_id":"685af523b4ac24d5329d80cc"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":1,"_id":"685af523b4ac24d5329d80cb","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":31,"end":137,"interaction_partner":[],"reference_html":"Order and disorder in the domain organization of the plasmid partition protein KorB. <i> Rajasekar K, Muntaha ST, Tame JRH, Kommareddy S, Morris G, Wharton CW, Thomas CM, White SA, Hyde EI, Scott DJ. </i> J Biol Chem, 2010","reference_id":"20200158","region_id":"DP00656r022","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The NMR data for the N-ter-\nminal domain does show that there is some structure present\n(Fig. 3), however, the peaks between 8.0 and 8.5 ppm could arise\nfrom amide protons in either unstructured or alpha-helical regions.\nThis domain may exists in an equilibrium between a folded and\nunfolded state, and the folded and unfolded conformations of\nthis domain we have generated represent limiting cases.","_id":"685af523b4ac24d5329d80ce"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":1,"_id":"685af523b4ac24d5329d80cd","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1R71","_id":"685af523b4ac24d5329d80d0"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":253,"end":294,"interaction_partner":[],"reference_html":"Sequence-specific DNA binding determined by contacts outside the helix-turn-helix motif of the ParB homolog KorB. <i> Khare D, Ziegelin G, Lanka E, Heinemann U. </i> Nat Struct Mol Biol, 2004","reference_id":"15170177","region_id":"DP00656r023","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"KorB-O and KorB-C are connected by a linker that is probably flexible, as residue Lys253–Lys294 are disordered in the KorB-O–DNA crystal.","_id":"685af523b4ac24d5329d80d1"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-30T09:11:06.147Z","_id":"685af523b4ac24d5329d80d2"},"version":1,"_id":"685af523b4ac24d5329d80cf","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1R71","_id":"685af523b4ac24d5329d80d4"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":253,"end":294,"interaction_partner":[],"reference_html":"Sequence-specific DNA binding determined by contacts outside the helix-turn-helix motif of the ParB homolog KorB. <i> Khare D, Ziegelin G, Lanka E, Heinemann U. </i> Nat Struct Mol Biol, 2004","reference_id":"15170177","region_id":"DP00656r024","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"KorB-O and KorB-C are connected by a linker that is probably flexible, as residue Lys253–Lys294 are disordered in the KorB-O–DNA crystal.","_id":"685af523b4ac24d5329d80d5"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-30T09:25:26.975Z","_id":"685af523b4ac24d5329d80d6"},"version":1,"_id":"685af523b4ac24d5329d80d3","reference_source":"pmid"}],"__v":0,"disorder_content":0.31843575418994413,"disprot_consensus":{"full":[{"start":1,"end":30,"type":"D"},{"start":31,"end":137,"type":"T"},{"start":252,"end":294,"type":"D"}],"Structural state":[{"start":1,"end":50,"type":"D"},{"start":117,"end":137,"type":"D"},{"start":252,"end":294,"type":"D"}],"Disorder function":[{"start":117,"end":137,"type":"F"},{"start":252,"end":294,"type":"F"}],"Structural transition":[{"start":31,"end":137,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00257","name":"Dehydrin","start":79,"end":198}]},"uniref50":"UniRef50_P42759","sequence":"MAEEYKNNVPEHETPTVATEESPATTTEVTDRGLFDFLGKKEEEVKPQETTTLESEFDHKAQISEPELAAEHEEVKENKITLLEELQEKTEEDEENKPSVIEKLHRSNSSSSSSSDEEGEEKKEKKKKIVEGEEDKKGLVEKIKEKLPGHHDKTAEDDVPVSTTIPVPVSESVVEHDHPEEEKKGLVEKIKEKLPGHHDEKAEDSPAVTSTPLVVTEHPVEPTTELPVEHPEEKKGILEKIKEKLPGYHAKTTEEEVKKEKESDD","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_P31168","disprot_id":"DP00657","ncbi_taxon_id":3702,"regions_counter":1,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":265,"region_id":"DP00657r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structural investigation of disordered stress proteins. Comparison of full-length dehydrins with isolated peptides of their conserved segments. <i> Mouillon JM, Gustafsson P, Harryson P. </i> Plant Physiol, 2006","statement":[{"text":"In physiological buffer, the circular dichroism spectra of the full-length dehydrins reveal overall disordered structures with a variable content of poly-Pro helices, a type of elongated secondary structure relying on bridging water molecules.","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":1,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"16565295","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-15T16:27:59.185Z"}}],"released":"2016_10","uniref100":"UniRef100_P31168","date":"2016-09-14T10:23:01.000Z","acc":"P31168","name":"Dehydrin COR47","length":265,"organism":"Arabidopsis thaliana","dataset":["Stress response proteins"],"UniParc":"UPI000016DAE5","genes":[{"name":{"value":"COR47"},"synonyms":[{"value":"RD17"}],"orfNames":[{"value":"F5M15.22"}],"olnNames":[{"value":"At1g20440"}]}],"alphafold_very_low_content":0.3132075471698113,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":265,"type":"D"}],"Structural state":[{"start":1,"end":265,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00257","name":"Dehydrin","start":58,"end":119},{"id":"PF00257","name":"Dehydrin","start":124,"end":156}]},"uniref50":"UniRef50_P42758","sequence":"MNSHQNQTGVQKKGITEKIMEKLPGHHGPTNTGVVHHEKKGMTEKVMEQLPGHHGATGTGGVHHEKKGMTEKVMEQLPGHHGSHQTGTNTTYGTTNTGGVHHEKKSVTEKVMEKLPGHHGSHQTGTNTAYGTNTNVVHHEKKGIAEKIKEQLPGHHGTHKTGTTTSYGNTGVVHHENKSTMDKIKEKLPGGHH","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_P42758","disprot_id":"DP00658","ncbi_taxon_id":3702,"regions_counter":21,"creator":"grivas","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":193,"region_id":"DP00658r001","released":"2025_12","ec_id":"ECO:0006204","reference_html":"Structural investigation of disordered stress proteins. Comparison of full-length dehydrins with isolated peptides of their conserved segments. <i> Mouillon JM, Gustafsson P, Harryson P. </i> Plant Physiol, 2006","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2025-10-15T16:27:15.866Z","reference_source":"pmid","term_name":"disorder","reference_id":"16565295","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"In physiological buffer at 4°C, the circular dichroism (CD) spectra of all four full-length dehydrins display large minima around 200 nm and an ellipticity near zero around 220 nm, indicative of poorly structured conformations with low content of secondary structure (Fig. 2A","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":193,"region_id":"DP00658r002","released":"2025_12","ec_id":"ECO:0006228","reference_html":"Membrane-Induced Folding of the Plant Stress Dehydrin Lti30. <i> Eriksson S, Eremina N, Barth A, Danielsson J, Harryson P. </i> Plant Physiol, 2016","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2025-10-15T17:01:32.381Z","reference_source":"pmid","term_name":"disorder","reference_id":"27208263","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"A strong band at 1,644 cm−1 and a weak band at 1,673 cm−1 at both pH 5 and 8.6 indicate random coil structure (Fig. 5A).","type":"Results"}]},{"start":1,"end":193,"reference_id":"27208263","reference_source":"pmid","reference_html":"Membrane-Induced Folding of the Plant Stress Dehydrin Lti30. <i> Eriksson S, Eremina N, Barth A, Danielsson J, Harryson P. </i> Plant Physiol, 2016","date":"2025-10-15T16:58:38.294Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006337","ec_ontology":"ECO","ec_name":"stopped-flow fluorescence spectroscopy evidence","unpublished":true,"released":"2025_12","version":0,"interaction_partner":[{"db":"ChEBI","id":"60426","operator":null,"partner_start":null,"partner_end":null},{"db":"ChEBI","id":"52360","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP00658r006","statement":[{"text":"As seen in Figure 2, 2% negatively charged lipids are adequate for Lti30 to bind and cluster the vesicles.","type":"Results"},{"text":"The conclusion is that Lti30 has a strong affinity for low concentrations of negative lipids and needs only a few negative lipids to bind and cluster vesicles. This indicates that Lti30 also can bind to different cellular membranes in vivo, since most of these contain higher concentrations of negatively charged phospholipids than tested here (Uemura et al., 1995).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":193,"reference_id":"27208263","reference_source":"pmid","reference_html":"Membrane-Induced Folding of the Plant Stress Dehydrin Lti30. <i> Eriksson S, Eremina N, Barth A, Danielsson J, Harryson P. </i> Plant Physiol, 2016","date":"2025-10-15T17:00:05.028Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"IDA","interaction_partner":[{"db":"ChEBI","id":"60426","operator":null,"partner_start":null,"partner_end":null},{"db":"ChEBI","id":"52360","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP00658r007","statement":[{"text":"The large clusters formed due to Lti30 binding are detectable with a light microscope, and images of the clusters further support the stopped-flow data (Fig. 3).","type":"Results"},{"text":"The conclusion is that Lti30 has a strong affinity for low concentrations of negative lipids and needs only a few negative lipids to bind and cluster vesicles. This indicates that Lti30 also can bind to different cellular membranes in vivo, since most of these contain higher concentrations of negatively charged phospholipids than tested here (Uemura et al., 1995). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":193,"reference_id":"27208263","reference_source":"pmid","reference_html":"Membrane-Induced Folding of the Plant Stress Dehydrin Lti30. <i> Eriksson S, Eremina N, Barth A, Danielsson J, Harryson P. </i> Plant Physiol, 2016","date":"2025-10-15T17:06:00.715Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"region_id":"DP00658r008","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"60426","entry_name":null},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"52360","entry_name":null}],"statement":[{"text":"Accordingly, in the absence of lipid vesicles, Lti30 displays the characteristic fingerprint of a fully disordered chain (Fig. 5A), consistent with previous reports (Mouillon et al., 2006, 2008). Then, upon interaction with DMPC:DMPG vesicles, Lti30 undergoes a conformational shift coupled to perturbation of the lipid bilayer (Fig. 5, B and C).","type":"Results"}]},{"start":62,"end":82,"reference_id":"27208263","reference_source":"pmid","reference_html":"Membrane-Induced Folding of the Plant Stress Dehydrin Lti30. <i> Eriksson S, Eremina N, Barth A, Danielsson J, Harryson P. </i> Plant Physiol, 2016","date":"2025-10-15T17:10:56.629Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"region_id":"DP00658r009","statement":[{"text":"The free KLti30 is soluble in buffer and gives a good one-dimensional 1H-NMR spectrum, typical for a fully disordered peptide (Fig. 6).","type":"Results"}]},{"start":35,"end":55,"reference_id":"27208263","reference_source":"pmid","reference_html":"Membrane-Induced Folding of the Plant Stress Dehydrin Lti30. <i> Eriksson S, Eremina N, Barth A, Danielsson J, Harryson P. </i> Plant Physiol, 2016","date":"2025-10-15T17:11:07.496Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"region_id":"DP00658r010","statement":[{"text":"The free KLti30 is soluble in buffer and gives a good one-dimensional 1H-NMR spectrum, typical for a fully disordered peptide (Fig. 6).","type":"Results"}]},{"start":35,"end":55,"reference_id":"27208263","reference_source":"pmid","reference_html":"Membrane-Induced Folding of the Plant Stress Dehydrin Lti30. <i> Eriksson S, Eremina N, Barth A, Danielsson J, Harryson P. </i> Plant Physiol, 2016","date":"2025-10-15T17:12:44.043Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"60426","operator":null,"partner_start":null,"partner_end":null},{"db":"ChEBI","id":"52360","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP00658r011","statement":[{"text":"Upon the addition of bicelles, however, the chemical shift signatures of the KLti30 segment spectra undergo distinct alterations consistent with binding (Fig. 6).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":62,"end":82,"reference_id":"27208263","reference_source":"pmid","reference_html":"Membrane-Induced Folding of the Plant Stress Dehydrin Lti30. <i> Eriksson S, Eremina N, Barth A, Danielsson J, Harryson P. </i> Plant Physiol, 2016","date":"2025-10-15T17:12:51.114Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"60426","operator":null,"partner_start":null,"partner_end":null},{"db":"ChEBI","id":"52360","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP00658r012","statement":[{"text":"Upon the addition of bicelles, however, the chemical shift signatures of the KLti30 segment spectra undergo distinct alterations consistent with binding (Fig. 6).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":40,"end":49,"reference_id":"27208263","reference_source":"pmid","reference_html":"Membrane-Induced Folding of the Plant Stress Dehydrin Lti30. <i> Eriksson S, Eremina N, Barth A, Danielsson J, Harryson P. </i> Plant Physiol, 2016","date":"2025-10-15T17:18:52.144Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"region_id":"DP00658r013","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"52360","entry_name":null},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"60426","entry_name":null}],"statement":[{"text":"Although the chemical shifts induced upon bicelle binding are moderate at the level of population average (Fig. 6), we conclude from the diffusion data that the chemical shift perturbations of the bound population are twice the observed values and, consequently, in line with the folding of the KLti30 segment into an ordered structure. To determine at atomic resolution the structure of the membrane-bound KLti30, we used deuterated bicelles and two-dimensional NMR. The results reveal six αHi-NHi  +3 nuclear Overhauser effect (NOE) couplings in the central part of the KLti30 segment (Fig. 6C), constraining residues Gly-7 to Gln-15 into a well-ordered α-helix, when bound to bicelles (Figs. 6 and 7).","type":"Results"},{"text":"Structural analysis of membrane-bound KLti30 peptide by NMR. A, The five best structures of bicelle-bound KLti30 peptide from 1H-NMR constraints, where the central nine residues of the peptide adopt a fixed α-helix, whereas the N and C termini are more disordered.","type":"Figure"}]},{"start":67,"end":76,"reference_id":"27208263","reference_source":"pmid","reference_html":"Membrane-Induced Folding of the Plant Stress Dehydrin Lti30. <i> Eriksson S, Eremina N, Barth A, Danielsson J, Harryson P. </i> Plant Physiol, 2016","date":"2025-10-15T17:19:27.873Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"region_id":"DP00658r014","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"52360","entry_name":null},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"60426","entry_name":null}],"statement":[{"text":"Although the chemical shifts induced upon bicelle binding are moderate at the level of population average (Fig. 6), we conclude from the diffusion data that the chemical shift perturbations of the bound population are twice the observed values and, consequently, in line with the folding of the KLti30 segment into an ordered structure. To determine at atomic resolution the structure of the membrane-bound KLti30, we used deuterated bicelles and two-dimensional NMR. The results reveal six αHi-NHi  +3 nuclear Overhauser effect (NOE) couplings in the central part of the KLti30 segment (Fig. 6C), constraining residues Gly-7 to Gln-15 into a well-ordered α-helix, when bound to bicelles (Figs. 6 and 7).","type":"Results"},{"text":"Structural analysis of membrane-bound KLti30 peptide by NMR. A, The five best structures of bicelle-bound KLti30 peptide from 1H-NMR constraints, where the central nine residues of the peptide adopt a fixed α-helix, whereas the N and C termini are more disordered.","type":"Figure"}]}],"released":"2016_10","uniref100":"UniRef100_P42758","date":"2016-09-12T22:47:45.000Z","acc":"P42758","name":"Dehydrin Xero 2","length":193,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI00000014EE","genes":[{"name":{"value":"XERO2"},"synonyms":[{"value":"LTI30"}],"orfNames":[{"value":"F24M12.10"}],"olnNames":[{"value":"At3g50970"}]}],"alphafold_very_low_content":0.48704663212435234,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":193,"type":"T"}],"Structural state":[{"start":1,"end":193,"type":"D"}],"Molecular function":[{"start":1,"end":193,"type":"F"}],"Structural transition":[{"start":1,"end":193,"type":"T"}]}},{"features":{"pfam":[{"id":"PF07404","name":"Telomere-binding protein beta subunit (TEBP beta)","start":23,"end":161}],"gene3D":[{"start":1,"end":224,"id":"2.40.200.10","name":"Telomere-binding Protein Beta Subunit; Chain"}]},"uniref50":"UniRef50_P16458","sequence":"MSKGASAPQQQSAFKQLYTELFNNEGDFSKVSSNLKKPLKCYVKESYPHFLVTDGYFFVAPYFTKEAVNEFHAKFPNVNIVDLTDKVIVINNWSLELRRVNSAEVFTSYANLEARLIVHSFKPNLQERLNPTRYPVNLFRDDEFKTTIQHFRHTALQAAINKTVKGDNLVDISKVADAAGKKGKVDAGIVKASASKGDEFSDFSFKEGNTATLKIADIFVQEKGKDALNKAADHTDGAKVKGGAKGKGKAAAKAAKGKKLSAKKGDSSAADVRKSVDKIVKYTPSKGSRKDTPQKSQAPAAGKSSAKKGGKKAVPSAPSPSGKKSALTTDKMTMAQFVKYLDWHEKKKGGKVSSGGKVLGKRSAGKASATSGKASKASKKTAAKK","taxonomy":["Eukaryota","Sar","Alveolata","Ciliophora","Intramacronucleata","Spirotrichea","Stichotrichia","Sporadotrichida","Oxytrichidae","Stylonychinae","Sterkiella"],"uniref90":"UniRef90_P16458","disprot_id":"DP00659","ncbi_taxon_id":200597,"regions_counter":1,"creator":"ameszaros","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":385,"region_id":"DP00659r001","released":"2022_03","ec_id":"ECO:0006299","reference_html":"Solution conformations and interactions of alpha and beta subunits of the Oxytricha nova telomere binding protein: investigation by Raman spectroscopy. <i> Laporte L, Stultz J, Thomas GJ. </i> Biochemistry, 1997","term_id":"IDPO:0000002","curator_id":"ameszaros","start":233,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"9201953","version":2,"ec_name":"Raman spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P16458","date":"2016-09-17T22:11:58.000Z","acc":"P16458","name":"Telomere-binding protein subunit beta","length":385,"organism":"Sterkiella nova","dataset":[],"UniParc":"UPI0000136B83","genes":[{"name":{"value":"MAC-41A"}},{"name":{"value":"MAC-41S"}}],"alphafold_very_low_content":0.33506493506493507,"disorder_content":0.3974025974025974,"disprot_consensus":{"full":[{"start":233,"end":385,"type":"D"}],"Structural state":[{"start":233,"end":385,"type":"D"}]}},{"features":{"pfam":[{"id":"PF15317","name":"Cardiac transcription factor regulator, Developmental protein","start":18,"end":103}]},"uniref50":"UniRef50_Q9CX60","sequence":"MSVYFPIHCSDYLRSAEMTEVMMNAPSMEEIGLSPRKDGLSYQIFPDPSDFDRCCKLKDRLPSIVVEPTEGEVESGELRWPPEEFLVQEDEQDNCEETTNEKKDQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q9CX60","disprot_id":"DP00661","ncbi_taxon_id":10090,"regions_counter":6,"creator":"aschramm","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":105,"region_id":"DP00661r001","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Biophysical characterization reveals structural disorder in the developmental transcriptional regulator LBH. <i> Al-Ali H, Rieger ME, Seldeen KL, Harris TK, Farooq A, Briegel KJ. </i> Biochem Biophys Res Commun, 2010","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"20005203","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-08-26T15:10:33.241Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":" As shown in Fig. 3C, the majority of backbone amide proton resonances exhibited poor chemical shift dispersion (~7.9–8.7 ppm), indicating substantial regions of structural disorder. In addition, many resonances were broadened, indicating interconversion between multiple conformations occurring within the \"intermediate\" NMR timescale. ","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":105,"region_id":"DP00661r002","released":"2022_12","ec_id":"ECO:0007680","reference_html":"Biophysical characterization reveals structural disorder in the developmental transcriptional regulator LBH. <i> Al-Ali H, Rieger ME, Seldeen KL, Harris TK, Farooq A, Briegel KJ. </i> Biochem Biophys Res Commun, 2010","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"20005203","version":3,"ec_name":"chromatography evidence used in manual assertion","date":"2022-08-26T15:11:24.463Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":" This value is approximately three-fold greater than its theoretical molecular mass of 12.3 kD and could suggest that LBH exists as a higher-order oligomer in solution. However, since determination of molecular mass of proteins from such analysis is highly dependent upon their globular shape, an alternative scenario could be that LBH lacks an intrinsic globular fold allowing it to behave as a structurally disordered polymer.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":105,"region_id":"DP00661r003","released":"2022_12","ec_id":"ECO:0006204","reference_html":"Biophysical characterization reveals structural disorder in the developmental transcriptional regulator LBH. <i> Al-Ali H, Rieger ME, Seldeen KL, Harris TK, Farooq A, Briegel KJ. </i> Biochem Biophys Res Commun, 2010","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"20005203","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-08-26T15:08:45.689Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"As shown in Fig. 3B, CD spectrum of LBH in the far-UV region (180–240 nm) is largely characterized by a negative band centered around 200 nm, which is reminiscent of a structurally disordered protein with little or no secondary structure.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":105,"region_id":"DP00661r004","released":"2022_12","ec_id":"ECO:0006206","reference_html":"Biophysical characterization reveals structural disorder in the developmental transcriptional regulator LBH. <i> Al-Ali H, Rieger ME, Seldeen KL, Harris TK, Farooq A, Briegel KJ. </i> Biochem Biophys Res Commun, 2010","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"20005203","version":3,"ec_name":"near-UV circular dichroism evidence used in manual assertion","date":"2022-08-26T15:09:05.537Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Additionally, the CD spectrum of LBH in the near-UV region (240–300 nm) is completely devoid of a band around 280 nm, which would be expected for a non-globular protein with one or more tryptophan residues.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":105,"region_id":"DP00661r005","released":"2022_12","ec_id":"ECO:0007066","reference_html":"Biophysical characterization reveals structural disorder in the developmental transcriptional regulator LBH. <i> Al-Ali H, Rieger ME, Seldeen KL, Harris TK, Farooq A, Briegel KJ. </i> Biochem Biophys Res Commun, 2010","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"20005203","version":3,"ec_name":"static light scattering assay evidence used in manual assertion","date":"2022-08-26T15:11:36.149Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Thus, the molecular mass determined for LBH from ALS analysis on the basis of first principles of hydrodynamics with no assumptions is in an excellent agreement with a theoretical value of 12.3 kD and suggests that LBH exists as a monomer in solution. Additionally, a value of 234 Å for the radius of gyration of LBH strongly suggests that LBH lacks a globular fold and most likely behaves as a rod-like macromolecule.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":105,"region_id":"DP00661r006","released":"2022_12","ec_id":"ECO:0001249","reference_html":"Biophysical characterization reveals structural disorder in the developmental transcriptional regulator LBH. <i> Al-Ali H, Rieger ME, Seldeen KL, Harris TK, Farooq A, Briegel KJ. </i> Biochem Biophys Res Commun, 2010","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"20005203","version":3,"ec_name":"fluorescence evidence used in manual assertion","date":"2022-08-26T15:08:16.213Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"In Figure 3A, fluorescence spectrum of LBH shows that the single tryptophan residue (Trp-80) within the protein emits with λmax around 350 nm. Given that this is the λmax observed for free tryptophan residues in solution, it can be argued that the tryptophan residue within LBH is completely accessible to the aqueous solvent and that LBH is likely to contain a non-globular fold.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_Q9CX60","date":"2016-09-17T20:36:58.000Z","acc":"Q9CX60","name":"Protein LBH","length":105,"organism":"Mus musculus","dataset":[],"UniParc":"UPI000002221D","genes":[{"name":{"value":"Lbh"}}],"alphafold_very_low_content":0.11428571428571428,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":105,"type":"D"}],"Structural state":[{"start":1,"end":105,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02096","name":"60Kd inner membrane protein","start":139,"end":354}]},"uniref50":"UniRef50_Q8LBP4","sequence":"MARVLVSSPSSFFGSPLIKPSSSLRHSGVGGGGTAQFLPYRSNNNKLFTTSTTVRFSLNEIPPFHGLDSSVDIGAIFTRAESLLYTIADAAVVGADSVVTTDSSAVQKSGGWFGFISDAMELVLKILKDGLSAVHVPYAYGFAIILLTIIVKAATYPLTKQQVESTLAMQNLQPKIKAIQQRYAGNQERIQLETSRLYKQAGVNPLAGCLPTLATIPVWIGLYQALSNVANEGLFTEGFFWIPSLGGPTSIAARQSGSGISWLFPFVDGHPPLGWYDTVAYLVLPVLLIASQYVSMEIMKPPQTDDPAQKNTLLVFKFLPLMIGYFALSVPSGLSIYWLTNNVLSTAQQVYLRKLGGAKPNMDENASKIISAGRAKRSIAQPDDAGERFRQLKEQEKRSKKNKAVAKDTVELVEESQSESEEGSDDEEEEAREGALASSTTSKPLPEVGQRRSKRSKRKRTV","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q8LBP4","disprot_id":"DP00662","ncbi_taxon_id":3702,"regions_counter":8,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":462,"region_id":"DP00662r001","released":"2022_03","ec_id":"ECO:0007680","reference_html":"The C terminus of the Alb3 membrane insertase recruits cpSRP43 to the thylakoid membrane. <i> Falk S, Ravaud S, Koch J, Sinning I. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"fquaglia","start":339,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20018841","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":462,"term_name":"molecular function regulator","start":339,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"20018841","version":3,"reference_html":"The C terminus of the Alb3 membrane insertase recruits cpSRP43 to the thylakoid membrane. <i> Falk S, Ravaud S, Koch J, Sinning I. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0007680","region_id":"DP00662r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":462,"term_name":"disorder to order","start":339,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20018841","version":2,"reference_html":"The C terminus of the Alb3 membrane insertase recruits cpSRP43 to the thylakoid membrane. <i> Falk S, Ravaud S, Koch J, Sinning I. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0007680","region_id":"DP00662r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":462,"term_name":"protein binding","start":339,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"20018841","version":3,"reference_html":"The C terminus of the Alb3 membrane insertase recruits cpSRP43 to the thylakoid membrane. <i> Falk S, Ravaud S, Koch J, Sinning I. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007680","region_id":"DP00662r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":462,"region_id":"DP00662r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The C terminus of the Alb3 membrane insertase recruits cpSRP43 to the thylakoid membrane. <i> Falk S, Ravaud S, Koch J, Sinning I. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"fquaglia","start":339,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20018841","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":462,"term_name":"molecular function regulator","start":339,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"20018841","version":3,"reference_html":"The C terminus of the Alb3 membrane insertase recruits cpSRP43 to the thylakoid membrane. <i> Falk S, Ravaud S, Koch J, Sinning I. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006204","region_id":"DP00662r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":462,"term_name":"disorder to order","start":339,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20018841","version":2,"reference_html":"The C terminus of the Alb3 membrane insertase recruits cpSRP43 to the thylakoid membrane. <i> Falk S, Ravaud S, Koch J, Sinning I. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00662r007","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":462,"term_name":"protein binding","start":339,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"20018841","version":3,"reference_html":"The C terminus of the Alb3 membrane insertase recruits cpSRP43 to the thylakoid membrane. <i> Falk S, Ravaud S, Koch J, Sinning I. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00662r008","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q8LBP4","date":"2016-08-16T16:57:44.000Z","acc":"Q8LBP4","name":"Inner membrane protein ALBINO3, chloroplastic","length":462,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI00000A33B5","genes":[{"name":{"value":"ALB3"},"orfNames":[{"value":"F8N16.9"}],"olnNames":[{"value":"At2g28800"}]}],"alphafold_very_low_content":0.30952380952380953,"disorder_content":0.2683982683982684,"disprot_consensus":{"full":[{"start":339,"end":462,"type":"T"}],"Structural state":[{"start":339,"end":462,"type":"D"}],"Molecular function":[{"start":339,"end":462,"type":"F"}],"Structural transition":[{"start":339,"end":462,"type":"T"}]}},{"features":{"pfam":[{"id":"PF01669","name":"Myelin basic protein","start":15,"end":171}]},"uniref50":"UniRef50_P02687","sequence":"ASQKRPSQRHGSKYLASASTMDHARHGFLPRHRDTGIDSLGRFFGADRGAPKRGSGKDGHHAARTTHYGSLPQKAQHGRPQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRAPDYKPAHKGLKGAQDAQGTLSKIFKLGGRDSRSGSPMARR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Suina","Suidae","Sus"],"uniref90":"UniRef90_P02687","disprot_id":"DP00663","ncbi_taxon_id":9823,"regions_counter":8,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":171,"region_id":"DP00663r001","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Structural analysis of the complex between calmodulin and full-length myelin basic protein, an intrinsically disordered molecule. <i> Majava V, Wang C, Myllykoski M, Kangas SM, Kang SU, Hayashi N, Baumgärtel P, Heape AM, Lubec G, Kursula P. </i> Amino Acids, 2010","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19855925","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":171,"term_name":"protein binding","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19855925","version":3,"reference_html":"Structural analysis of the complex between calmodulin and full-length myelin basic protein, an intrinsically disordered molecule. <i> Majava V, Wang C, Myllykoski M, Kangas SM, Kang SU, Hayashi N, Baumgärtel P, Heape AM, Lubec G, Kursula P. </i> Amino Acids, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007680","region_id":"DP00663r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":171,"region_id":"DP00663r003","released":"2022_03","ec_id":"ECO:0006202","reference_html":"Structural analysis of the complex between calmodulin and full-length myelin basic protein, an intrinsically disordered molecule. <i> Majava V, Wang C, Myllykoski M, Kangas SM, Kang SU, Hayashi N, Baumgärtel P, Heape AM, Lubec G, Kursula P. </i> Amino Acids, 2010","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19855925","version":2,"ec_name":"synchrotron radiation circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":171,"term_name":"protein binding","start":1,"ec_name":"synchrotron radiation circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19855925","version":3,"reference_html":"Structural analysis of the complex between calmodulin and full-length myelin basic protein, an intrinsically disordered molecule. <i> Majava V, Wang C, Myllykoski M, Kangas SM, Kang SU, Hayashi N, Baumgärtel P, Heape AM, Lubec G, Kursula P. </i> Amino Acids, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006202","region_id":"DP00663r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":171,"region_id":"DP00663r005","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Structural analysis of the complex between calmodulin and full-length myelin basic protein, an intrinsically disordered molecule. <i> Majava V, Wang C, Myllykoski M, Kangas SM, Kang SU, Hayashi N, Baumgärtel P, Heape AM, Lubec G, Kursula P. </i> Amino Acids, 2010","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19855925","version":2,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":171,"term_name":"protein binding","start":1,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19855925","version":3,"reference_html":"Structural analysis of the complex between calmodulin and full-length myelin basic protein, an intrinsically disordered molecule. <i> Majava V, Wang C, Myllykoski M, Kangas SM, Kang SU, Hayashi N, Baumgärtel P, Heape AM, Lubec G, Kursula P. </i> Amino Acids, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006210","region_id":"DP00663r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":171,"region_id":"DP00663r007","released":"2022_03","ec_id":"ECO:0006198","reference_html":"Structural analysis of the complex between calmodulin and full-length myelin basic protein, an intrinsically disordered molecule. <i> Majava V, Wang C, Myllykoski M, Kangas SM, Kang SU, Hayashi N, Baumgärtel P, Heape AM, Lubec G, Kursula P. </i> Amino Acids, 2010","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19855925","version":2,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":171,"term_name":"protein binding","start":1,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19855925","version":3,"reference_html":"Structural analysis of the complex between calmodulin and full-length myelin basic protein, an intrinsically disordered molecule. <i> Majava V, Wang C, Myllykoski M, Kangas SM, Kang SU, Hayashi N, Baumgärtel P, Heape AM, Lubec G, Kursula P. </i> Amino Acids, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006198","region_id":"DP00663r008","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P81558","date":"2016-08-29T13:07:06.000Z","acc":"P81558","name":"Myelin basic protein","length":171,"organism":"Sus scrofa","dataset":[],"UniParc":"UPI000012ED3E","genes":[{"name":{"value":"MBP"}}],"alphafold_very_low_content":0.27485380116959063,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":171,"type":"D"}],"Structural state":[{"start":1,"end":171,"type":"D"}],"Molecular function":[{"start":1,"end":171,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03760","name":"Late embryogenesis abundant (LEA) group 1","start":9,"end":85}]},"uniref50":"UniRef50_Q01417","sequence":"MQGGKKAGESIKETATNIGASAKAGMEKTKATVQEKAERMTARDPVQKELATQKKEAKMNQAELDKQAARQHNTAAKQSATTAGHMGHGHHTTGTGTGTATYSTTGEYGQPMGAHQTSAMPGHGTGQPTGHVTEGVVGSHPIGTNRGPGGTATAHNTRAGGKPNDYGYGTGGT","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","fabids","Fabales","Fabaceae","Papilionoideae","50 kb inversion clade","NPAAA clade","indigoferoid/millettioid clade","Phaseoleae","Glycine","Glycine subgen. Soja"],"uniref90":"UniRef90_Q01417","disprot_id":"DP00664","ncbi_taxon_id":3847,"regions_counter":1,"creator":"droche","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":173,"region_id":"DP00664r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Characterization of two soybean (Glycine max L.) LEA IV proteins by circular dichroism and Fourier transform infrared spectrometry. <i> Shih MD, Hsieh TY, Lin TP, Hsing YI, Hoekstra FA. </i> Plant Cell Physiol, 2010","term_id":"IDPO:0000002","curator_id":"droche","start":1,"term_ontology":"IDPO","curator_name":"Daniel Roche","reference_id":"20071374","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q01417","date":"2016-09-12T17:59:59.000Z","acc":"Q01417","name":"18 kDa seed maturation protein","length":173,"organism":"Glycine max","dataset":[],"UniParc":"UPI00000009DF","genes":[{"name":{"value":"GMPM1"}}],"alphafold_very_low_content":0.4797687861271676,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":173,"type":"D"}],"Structural state":[{"start":1,"end":173,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00041","name":"Fibronectin type III domain","start":626,"end":706},{"id":"PF00041","name":"Fibronectin type III domain","start":718,"end":801},{"id":"PF00041","name":"Fibronectin type III domain","start":824,"end":910},{"id":"PF00041","name":"Fibronectin type III domain","start":920,"end":1002},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":337,"end":411},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":437,"end":514},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":519,"end":608},{"id":"PF13882","name":"Bravo-like intracellular region","start":1144,"end":1233},{"id":"PF13927","name":"Immunoglobulin domain","start":34,"end":118},{"id":"PF13927","name":"Immunoglobulin domain","start":239,"end":316}],"gene3D":[{"start":604,"end":723,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":724,"end":803,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":133,"end":238,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":804,"end":917,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":25,"end":132,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":333,"end":423,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":918,"end":1011,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":240,"end":332,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":516,"end":603,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":424,"end":515,"id":"2.60.40.10","name":"Immunoglobulins"}]},"uniref50":"UniRef50_P32004","sequence":"MVVALRYVWPLLLCSPCLLIQIPEEYEGHHVMEPPVITEQSPRRLVVFPTDDISLKCEASGKPEVQFRWTRDGVHFKPKEELGVTVYQSPHSGSFTITGNNSNFAQRFQGIYRCFASNKLGTAMSHEIRLMAEGAPKWPKETVKPVEVEEGESVVLPCNPPPSAEPLRIYWMNSKILHIKQDERVTMGQNGNLYFANVLTSDNHSDYICHAHFPGTRTIIQKEPIDLRVKATNSMIDRKPRLLFPTNSSSHLVALQGQPLVLECIAEGFPTPTIKWLRPSGPMPADRVTYQNHNKTLQLLKVGEEDDGEYRCLAENSLGSARHAYYVTVEAAPYWLHKPQSHLYGPGETARLDCQVQGRPQPEVTWRINGIPVEELAKDQKYRIQRGALILSNVQPSDTMVTQCEARNRHGLLLANAYIYVVQLPAKILTADNQTYMAVQGSTAYLLCKAFGAPVPSVQWLDEDGTTVLQDERFFPYANGTLGIRDLQANDTGRYFCLAANDQNNVTIMANLKVKDATQITQGPRSTIEKKGSRVTFTCQASFDPSLQPSITWRGDGRDLQELGDSDKYFIEDGRLVIHSLDYSDQGNYSCVASTELDVVESRAQLLVVGSPGPVPRLVLSDLHLLTQSQVRVSWSPAEDHNAPIEKYDIEFEDKEMAPEKWYSLGKVPGNQTSTTLKLSPYVHYTFRVTAINKYGPGEPSPVSETVVTPEAAPEKNPVDVKGEGNETTNMVITWKPLRWMDWNAPQVQYRVQWRPQGTRGPWQEQIVSDPFLVVSNTSTFVPYEIKVQAVNSQGKGPEPQVTIGYSGEDYPQAIPELEGIEILNSSAVLVKWRPVDLAQVKGHLRGYNVTYWREGSQRKHSKRHIHKDHVVVPANTTSVILSGLRPYSSYHLEVQAFNGRGSGPASEFTFSTPEGVPGHPEALHLECQSNTSLLLRWQPPLSHNGVLTGYVLSYHPLDEGGKGQLSFNLRDPELRTHNLTDLSPHLRYRFQLQATTKEGPGEAIVREGGTMALSGISDFGNISATAGENYSVVSWVPKEGQCNFRFHILFKALGEEKGGASLSPQYVSYNQSSYTQWDLQPDTDYEIHLFKERMFRHQMAVKTNGTGRVRLPPAGFATEGWFIGFVSAIILLLLVLLILCFIKRSKGGKYSVKDKEDTQVDSEARPMKDETFGEYRSLESDNEEKAFGSSQPSLNGDIKPLGSDDSLADYGGSVDVQFNEDGSFIGQYSGKKEKEAAGGNDSSGATSPINPAVALE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P32004","disprot_id":"DP00666","ncbi_taxon_id":9606,"regions_counter":12,"creator":"esalladini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1257,"region_id":"DP00666r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Characterization of the neuron-specific L1-CAM cytoplasmic tail: naturally disordered in solution it exercises different binding modes for different adaptor proteins. <i> Tyukhtenko S, Deshmukh L, Kumar V, Lary J, Cole J, Lemmon V, Vinogradova O. </i> Biochemistry, 2008","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1144,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18321067","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-05-09T19:47:10.296Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"On the basis of 13Cα and 13Cβ chemical shifts, which do not significantly deviate from the random coil values (Figure 1B), and the narrow distribution of the amide peaks in the 15N-HSQC spectrum (Figure 1C), we conclude that L1-CT is predominantly unstructured in aqueous solution.","type":"Results"}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":1257,"term_name":"protein binding","start":1144,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"18321067","version":4,"reference_html":"Characterization of the neuron-specific L1-CAM cytoplasmic tail: naturally disordered in solution it exercises different binding modes for different adaptor proteins. <i> Tyukhtenko S, Deshmukh L, Kumar V, Lary J, Cole J, Lemmon V, Vinogradova O. </i> Biochemistry, 2008","date":"2023-05-09T20:13:20.365Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00666r003","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P26040","operator":null,"partner_start":7,"partner_end":299},{"db":"UniProt","id":"P84091","operator":"or","partner_start":156,"partner_end":435}],"statement":[{"text":" Titrating the unlabeled proteins, the ezrin FERM domain and the AP2-μ2 chain, into the solution of isotopically labeled L1-CT and monitoring associated perturbations in the 15N-HSQC spectra allowed us to map the binding surface of L1-CT in both complexes.","type":"Results"},{"text":"Surprisingly, in addition to the two ERM binding sites identified in previous studies, the 1176YRSLE region and the juxtamembrane region, we identified a significant line broadening in a third one, composed of residues from 1213G to 1232K (Figure 3A,B). This site overlaps with the classical ankyrin binding motif, 1220NEDGS-FIGQY.","type":"Results"},{"text":"In the case of AP2-μ2, as expected, the1176YRSL motif of L1-CT is in the center of the cluster of resonances with reduced peak intensities (Figure 3E). Thus it is, indeed, the major binding determinant. The residue three amino acids upstream of 1176Y, 1173F, is also involved in the L1-AP2-μ2 complex. Contrary to the L1 interaction with ezrin, the C-terminus of L1-CT is not involved in the interaction with AP2-μ2. Surprisingly enough, we do see additional perturbations in the juxtamembrane region of L1-CT.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1257,"region_id":"DP00666r004","released":"2023_06","ec_id":"ECO:0007064","reference_html":"Characterization of the neuron-specific L1-CAM cytoplasmic tail: naturally disordered in solution it exercises different binding modes for different adaptor proteins. <i> Tyukhtenko S, Deshmukh L, Kumar V, Lary J, Cole J, Lemmon V, Vinogradova O. </i> Biochemistry, 2008","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1144,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18321067","version":3,"ec_name":"dynamic light scattering assay evidence used in manual assertion","date":"2023-05-09T19:51:27.939Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Dynamic light scattering experiments provided us with similar results. The normalized volume distribution for the L1-CT particles in aqueous solution (at 0.03 mM, pH 8.0, IS 300 mM) is presented in Figure 2B. The major peak is observed around a diameter of 5.93 nm with minor features near 15 nm for the higher order aggregates.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1257,"region_id":"DP00666r007","released":"2023_06","ec_id":"ECO:0007680","reference_html":"Characterization of the neuron-specific L1-CAM cytoplasmic tail: naturally disordered in solution it exercises different binding modes for different adaptor proteins. <i> Tyukhtenko S, Deshmukh L, Kumar V, Lary J, Cole J, Lemmon V, Vinogradova O. </i> Biochemistry, 2008","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1144,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18321067","version":3,"ec_name":"chromatography evidence used in manual assertion","date":"2023-05-09T19:52:19.200Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"This elution position, however, does not correspond to a 14.4 kDa globular monomeric protein [Figure 2C (peak 5, myoglobin, 18 kDa; peak 6, cytochrome c, 13 kDa, shown for comparison)], which we believe is due to the disordered nature of the L1-CT monomer characterized by a significantly increased hydrodynamic radius.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1257,"region_id":"DP00666r010","released":"2023_06","ec_id":"ECO:0006275","reference_html":"Characterization of the neuron-specific L1-CAM cytoplasmic tail: naturally disordered in solution it exercises different binding modes for different adaptor proteins. <i> Tyukhtenko S, Deshmukh L, Kumar V, Lary J, Cole J, Lemmon V, Vinogradova O. </i> Biochemistry, 2008","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1144,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18321067","version":3,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","date":"2023-05-09T19:49:33.992Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Global analysis of the two data sets using a hybrid continuous-discrete model yields a best fit molecular mass of 18.2 kDa for the major species, with a corrected sedimentation coefficient of s20,w = 1.63 S and a frictional ratio of f/f0 = 1.59. These data indicate that L1-CT exists as a monomer at this concentration range. However, the deduced molecular mass is somewhat higher than the monomer value of 14.4 kDa.","type":"Results"},{"text":"The frictional ratio is much higher than the value of 1.1–1.3 typically observed for globular proteins and is consistent with the NMR data indicating an unstructured extended conformation.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P32004","date":"2016-09-13T12:30:22.000Z","acc":"P32004","name":"Neural cell adhesion molecule L1","length":1257,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI000016ADC4","genes":[{"name":{"value":"L1CAM"},"synonyms":[{"value":"CAML1"},{"value":"MIC5"}]}],"alphafold_very_low_content":0.1368337311058075,"disorder_content":0.09069212410501193,"disprot_consensus":{"full":[{"start":1144,"end":1257,"type":"D"}],"Structural state":[{"start":1144,"end":1257,"type":"D"}],"Molecular function":[{"start":1144,"end":1257,"type":"F"}]}},{"acc":"P42763","sequence":"MAEEIKNVPEQEVPKVATEESSAEVTDRGLFDFLGKKKDETKPEETPIASEFEQKVHISEPEPEVKHESLLEKLHRSDSSSSSSSEEEGSDGEKRKKKKEKKKPTTEVEVKEEEKKGFMEKLKEKLPGHKKPEDGSAVAAAPVVVPPPVEEAHPVEKKGILEKIKEKLPGYHPKTTVEEEKKDKE","alphafold_very_low_content":"0.20540540540540542","creator":"tcordero","dataset":["Condensates-related proteins","Stress response proteins"],"date":"2016-08-16T17:12:04.000Z","disprot_id":"DP00667","features":{"pfam":[{"id":"PF00257","name":"Dehydrin","start":115,"end":172}]},"genes":[{"name":{"value":"ERD14","evidences":[],"_id":"685af523b4ac24d5329d811e"},"synonyms":[],"olnNames":[{"value":"At1g76180","evidences":[],"_id":"685af523b4ac24d5329d8121"}],"orfNames":[{"value":"T23E18.12","evidences":[],"_id":"685af523b4ac24d5329d811f"},{"value":"T23E18_36","evidences":[],"_id":"685af523b4ac24d5329d8120"}],"_id":"685af523b4ac24d5329d811d"}],"length":185,"name":"Dehydrin ERD14","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions_counter":22,"released":"2016_10","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"UniParc":"UPI0000000B94","uniref100":"UniRef100_P42763","uniref50":"UniRef50_P42763","uniref90":"UniRef90_P42763","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":185,"interaction_partner":[],"reference_html":"Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. <i> Kovacs D, Kalmar E, Torok Z, Tompa P. </i> Plant Physiol, 2008","reference_id":"18359842","region_id":"DP00667r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The 1H-NMR spectra of ERD10 and ERD14 (Fig. 3A; only ERD10 is shown) also suggest their disordered nature, because the chemical shift dispersion is narrower than is typical for globular proteins. For globular proteins, 1H chemical shifts usually spread out in the region 9.5 to 6.0 ppm, whereas for IDPs, they are usually confined in the region 8.0 to 8.5 ppm (Dyson and Wright, 2004).","_id":"685af523b4ac24d5329d80db"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-11-01T14:50:52.280Z","_id":"685af523b4ac24d5329d80dc"},"version":3,"_id":"685af523b4ac24d5329d80da","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":185,"interaction_partner":[],"reference_html":"Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. <i> Kovacs D, Kalmar E, Torok Z, Tompa P. </i> Plant Physiol, 2008","reference_id":"18359842","region_id":"DP00667r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In SDS-PAGE, they show a characteristic low mobility: the real molecular mass of ERD10 is 29 kD but it runs at 45 kD, whereas the real molecular mass of ERD14 is 20 kD but it runs at 37 kD (Fig. 2A). This high apparent molecular mass caused by a highly hydrophilic character is often diagnostic of IDPs (Tompa, 2002). In addition, both proteins are heat stable (Fig. 2B) and are very sensitive to proteases (Fig. 2A).","_id":"685af523b4ac24d5329d80e0"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-11-01T14:48:54.345Z","_id":"685af523b4ac24d5329d80e1"},"version":3,"_id":"685af523b4ac24d5329d80df","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"16876","_id":"685af523b4ac24d5329d80e7"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2023-12-11T09:02:01.275Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006198","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":185,"interaction_partner":[],"reference_html":"Full backbone assignment and dynamics of the intrinsically disordered dehydrin ERD14. <i> Szalainé Ágoston B, Kovács D, Tompa P, Perczel A. </i> Biomol NMR Assign, 2011","reference_id":"21336827","region_id":"DP00667r005","released":"2023_12","sample":[],"statement":[{"type":"Abstract","text":"Herein we present the backbone (1)H, (15)N and (13)C NMR assignment of the 185 amino acid long ERD14 (Early Response to Dehydration 14), which is a K(3)S-type, typical dehydrin of A. thaliana. Secondary chemical shifts as well as NMR relaxation data show that ERD14 is fully disordered under near native conditions, with short regions of somewhat restricted motion and 5-25% helical propensity.","_id":"685af523b4ac24d5329d80e5"},{"type":"Article","text":"The measured NMR data give clear evidence of the almost complete disordered state of ERD14 under native conditions. SCS values and relaxation parameters fall close to the random coil values along the entire chain (Fig. 2), which suggests that the protein is fully flexible.","_id":"685af523b4ac24d5329d80e6"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-12-11T19:31:56.034Z","_id":"685af523b4ac24d5329d80e8"},"version":4,"_id":"685af523b4ac24d5329d80e4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":185,"interaction_partner":[],"reference_html":"Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. <i> Kovacs D, Kalmar E, Torok Z, Tompa P. </i> Plant Physiol, 2008","reference_id":"18359842","region_id":"DP00667r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The CD spectra of ERD10 and ERD14 with a minimum close to 200 nm (Fig. 3B) are also typical of disordered proteins, because regular secondary structural elements, such as the α-helix and the β-sheet, in globular proteins give characteristic spectral peaks at 208, 222, and 214 nm, whereas a large negative peak at approximately 200 nm is characteristic of the coil conformation that dominates in IDPs (Receveur-Brechot et al., 2005).","_id":"685af523b4ac24d5329d80ee"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-11-01T14:48:12.668Z","_id":"685af523b4ac24d5329d80ef"},"version":3,"_id":"685af523b4ac24d5329d80ed","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-11-01T16:22:40.851Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006317","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":185,"interaction_partner":[],"reference_html":"Cold stability of intrinsically disordered proteins. <i> Tantos A, Friedrich P, Tompa P. </i> FEBS Lett, 2009","reference_id":"19121309","region_id":"DP00667r012","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"ERD14 on the other hand, showed no loss of chaperone capacity due to freezing.","_id":"685af523b4ac24d5329d80f7"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","term_id":"GO:0044183","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein folding chaperone","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-12-12T09:01:12.060Z","_id":"685af523b4ac24d5329d80f8"},"version":4,"_id":"685af523b4ac24d5329d80f6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":185,"interaction_partner":[],"reference_html":"Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. <i> Kovacs D, Kalmar E, Torok Z, Tompa P. </i> Plant Physiol, 2008","reference_id":"18359842","region_id":"DP00667r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The polypeptide chain of IDPs is more accessible to proteases than that of globular proteins, which results in much higher protease sensitivity, and this is diagnostic for their open structures. This was tested with proteases of broad substrate specificity (subtilisin and proteinase K) and proteases of narrow substrate specificity (trypsin and chymotrypsin); the pattern of the digestion was similar for all proteases, so we show only the results of proteinase K (Fig. 2A). ERD10 and ERD14 do not show any ordered motifs, which would show resistance against proteolysis.","_id":"685af523b4ac24d5329d80fa"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-11-01T14:45:21.951Z","_id":"685af523b4ac24d5329d80fb"},"version":2,"_id":"685af523b4ac24d5329d80f9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":185,"interaction_partner":[],"reference_html":"Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. <i> Kovacs D, Kalmar E, Torok Z, Tompa P. </i> Plant Physiol, 2008","reference_id":"18359842","region_id":"DP00667r015","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The interaction of ERD10 and ERD14 with phospholipid vesicles (PLVs) was analyzed with mini gel filtration columns, as described in “Materials and Methods.” The analysis and comparison with the behavior of a positive control, calpain domain III, which shows calcium-dependent phospholipid binding, and a negative control, BSA, which does not bind to vesicles either in the absence or the presence of calcium (Tompa et al., 2001), confirm that ERD10 and ERD14 bind to PLVs. The interaction was statistically significant, as suggested by Student's t test (P = 0.003 and 0.056 for ERD10 and ERD14, respectively). Under the given conditions, approximately 2 μg of ERD10 and 2.5 μg of ERD14 were bound to 25 μg of PLVs, out of 15 μg total (Fig. 8A).","_id":"685af523b4ac24d5329d8103"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_id":"GO:0008289","term_is_binding":true,"term_is_obsolete":false,"term_name":"lipid binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-11-01T15:17:30.341Z","_id":"685af523b4ac24d5329d8104"},"version":3,"_id":"685af523b4ac24d5329d8102","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2023-12-11T08:59:35.780Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006317","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":185,"interaction_partner":[],"reference_html":"Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. <i> Kovacs D, Kalmar E, Torok Z, Tompa P. </i> Plant Physiol, 2008","reference_id":"18359842","region_id":"DP00667r017","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"Here, citrate synthase was incubated at an elevated temperature and aggregation was followed by an increase in absorbance. ERD10 and ERD14 at an equimolar concentration showed significant protective activity (Fig. 5), slowing the rate of aggregation to about half of its control value; this effect was significantly higher than that of BSA but fell short of that of HSP90. Upon increasing ERD10 and ERD14 concentrations further, the protective effect did not change much and did not reach the efficiency of HSP90 (Table I).","_id":"685af523b4ac24d5329d8109"},{"type":"Results","text":"Both ERD10 and ERD14 showed significant protective effects on the thermal aggregation of firefly luciferase at a 2× molar excess (Fig. 6). Under these conditions, aggregation was almost completely inhibited, similar to the effect of HSP90 (Table I). BSA was practically ineffective in this assay.","_id":"685af523b4ac24d5329d810a"},{"type":"Results","text":"ERD10, ERD14, and HSP90 had similar protective effects on the enzyme activity of lysozyme at substoichiometric ratios of lysozyme:chaperone (7:1; Fig. 7; Table I). Although the time course of the loss of enzyme activity was somewhat different in the presence of ERD10, ERD14, and HSP90, their protective effects, as expressed by residual enzyme activity after 25 min of incubation, were commensurate. BSA, again, had a negligible effect.","_id":"685af523b4ac24d5329d810b"},{"type":"Discussion","text":"To investigate these functions of ERD10 and ERD14, we studied their protective effects on the heat-induced loss of enzyme activity and/or aggregation of four different substrates. The selected assays represent different modes and mechanisms of possible chaperone action and included thermal inactivation of ADH, thermal aggregation of firefly luciferase and citrate synthase, and the chemically induced inactivation of lysozyme. In the analyses shown here, ERD10 and ERD14 demonstrated marked effects on the prevention of aggregation/deactivation of protein substrates.","_id":"685af523b4ac24d5329d810c"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","term_id":"GO:0044183","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein folding chaperone","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-12-11T19:31:37.496Z","_id":"685af523b4ac24d5329d810d"},"version":4,"_id":"685af523b4ac24d5329d8108","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jglavina","curator_name":"Juliana Glavina","curator_orcid":"0000-0001-6336-1290","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":185,"interaction_partner":[],"reference_html":"Cellular Chaperone Function of Intrinsically Disordered Dehydrin ERD14. <i> Murvai N, Kalmar L, Szabo B, Schad E, Micsonai A, Kardos J, Buday L, Han KH, Tompa P, Tantos A. </i> Int J Mol Sci, 2021","reference_id":"34201246","region_id":"DP00667r018","released":"2022_03","sample":[],"statement":[{"type":"Title","text":"Cellular Chaperone Function of Intrinsically Disordered Dehydrin ERD14","_id":"685af523b4ac24d5329d810f"},{"type":"Abstract","text":"Here, we explored the involvement of each conserved segment in the protective function of the intrinsically disordered stress protein (IDSP) A. thaliana’s Early Response to Dehydration (ERD14).","_id":"685af523b4ac24d5329d8110"},{"type":"Results","text":"In phosphate buffer, all tested proteins showed a CD spectral shape characteristic of a disordered protein (Figure 4A), very similar to that of the wild-type ERD14. Because CD spectroscopy reflects the average secondary structure content, this indicates that the free ERD14 molecules are essentially disordered, and the helices shown by NMR [9] are truly only transient and might be stabilized by interacting with partner molecules.","_id":"685af523b4ac24d5329d8111"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-20T07:12:23.097Z","_id":"685af523b4ac24d5329d8112"},"version":1,"_id":"685af523b4ac24d5329d810e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jglavina","curator_name":"Juliana Glavina","curator_orcid":"0000-0001-6336-1290","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0000269","ec_name":"experimental evidence used in manual assertion","ec_ontology":"ECO","start":156,"end":169,"interaction_partner":[],"reference_html":"Cellular Chaperone Function of Intrinsically Disordered Dehydrin ERD14. <i> Murvai N, Kalmar L, Szabo B, Schad E, Micsonai A, Kardos J, Buday L, Han KH, Tompa P, Tantos A. </i> Int J Mol Sci, 2021","reference_id":"34201246","region_id":"DP00667r019","released":"2022_03","sample":[],"statement":[{"type":"Title","text":"Cellular Chaperone Function of Intrinsically Disordered Dehydrin ERD14","_id":"685af523b4ac24d5329d8114"},{"type":"Abstract","text":"Here, we explored the involvement of each conserved segment in the protective function of the intrinsically disordered stress protein (IDSP) A. thaliana’s Early Response to Dehydration (ERD14). We show that segments that are directly involved in partner binding, and others that are not, are equally necessary for proper function and that cellular protection emerges from the balanced interplay of \ndifferent regions of ERD14.","_id":"685af523b4ac24d5329d8115"},{"type":"Results","text":"These results suggest that Kc and S are the primary sites of activity, together with varying contributions of other segments. These notions were further confirmed by the in vitro chaperone activities of these mutants (Supplementary Figure S3 and Table S4). In these experiments, the ∆Kc and ∆S variants showed similarly reduced chaperone activities as the FS ERD14 variant. This is an interesting observation, especially in light of the fact that all K-segments participate in partner binding within a cell, whereas the S-segment does not [9]. Although partner binding in itself is a property of large amounts of proteins, only a small portion of them exhibit chaperone activity. Beyond the necessary partner binding regions, a chaperone is expected to have segments that contribute to or are responsible for chaperone function, such as the S-segment.\n","_id":"685af523b4ac24d5329d8116"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","term_id":"GO:0044183","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein folding chaperone","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-21T07:28:07.446Z","_id":"685af523b4ac24d5329d8117"},"version":1,"_id":"685af523b4ac24d5329d8113","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jglavina","curator_name":"Juliana Glavina","curator_orcid":"0000-0001-6336-1290","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0000269","ec_name":"experimental evidence used in manual assertion","ec_ontology":"ECO","start":74,"end":85,"interaction_partner":[],"reference_html":"Cellular Chaperone Function of Intrinsically Disordered Dehydrin ERD14. <i> Murvai N, Kalmar L, Szabo B, Schad E, Micsonai A, Kardos J, Buday L, Han KH, Tompa P, Tantos A. </i> Int J Mol Sci, 2021","reference_id":"34201246","region_id":"DP00667r020","released":"2022_03","sample":[],"statement":[{"type":"Title","text":"Cellular Chaperone Function of Intrinsically Disordered Dehydrin ERD14","_id":"685af523b4ac24d5329d8119"},{"type":"Abstract","text":"Here, we explored the involvement of each conserved segment in the protective function of the intrinsically disordered stress protein (IDSP) A. thaliana’s Early Response to Dehydration (ERD14). We show that segments that are directly involved in partner binding, and others that are not, are equally necessary for proper function and that cellular protection emerges from the balanced interplay of \ndifferent regions of ERD14.","_id":"685af523b4ac24d5329d811a"},{"type":"Results","text":"These results suggest that Kc and S are the primary sites of activity, together with varying contributions of other segments. These notions were further confirmed by the in vitro chaperone activities of these mutants (Supplementary Figure S3 and Table S4). In these experiments, the ∆Kc and ∆S variants showed similarly reduced chaperone activities as the FS ERD14 variant. This is an interesting observation, especially in light of the fact that all K-segments participate in partner binding within a cell, whereas the S-segment does not [9]. Although partner binding in itself is a property of large amounts of proteins, only a small portion of them exhibit chaperone activity. Beyond the necessary partner binding regions, a chaperone is expected to have segments that contribute to or are responsible for chaperone function, such as the S-segment.\n","_id":"685af523b4ac24d5329d811b"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","term_id":"GO:0044183","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein folding chaperone","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-21T07:29:51.409Z","_id":"685af523b4ac24d5329d811c"},"version":1,"_id":"685af523b4ac24d5329d8118","reference_source":"pmid"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":185,"type":"D"}],"Structural state":[{"start":1,"end":185,"type":"D"}],"Molecular function":[{"start":1,"end":185,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03347","name":"Vibrio thermostable direct hemolysin","start":25,"end":189}],"gene3D":[{"start":25,"end":189,"id":"2.60.270.30","name":"Vibrio parahaemolyticus thermostable direct hemolysin"}]},"uniref50":"UniRef50_P19250","sequence":"MKYRYFAKKSFLFISMLAAFKTFAFELPSVPFPAPGSDEILFVVRDTTFNTNAPVNVEVSDFWTNRNVKRKPYKDVYGQSVFTTSGTKWLTSYMTVNINDKDYTMAAVSGYKHGHSAVFVKSDQVQLQHSYDSVANFVGEDEDSIPSKMYLDETPEYFVNVEAYESGSGNILVMCISNKESFFECKHQQ","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Vibrionales","Vibrionaceae","Vibrio"],"uniref90":"UniRef90_P19250","disprot_id":"DP00668","dataset":["Unicellular toxins and antitoxins","Bacterial virulence-related proteins"],"ncbi_taxon_id":223926,"regions_counter":5,"creator":"agasparini","regions":[{"region_id":"DP00668r002","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T10:40:16.928Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":35,"term_id":"IDPO:0000002","start":25,"version":2,"statement":[{"text":"There was no electron density observed for the N-terminal region (residues 1–11), suggesting that this region is highly flexible or adopts more than one conformation.","type":"Results"},{"text":"What the authors refer to as residues 1-11 correspond to residues 25-35 in the UniProt sequence","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20335168","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3A57"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structure and functional characterization of Vibrio parahaemolyticus thermostable direct hemolysin. <i> Yanagihara I, Nakahira K, Yamane T, Kaieda S, Mayanagi K, Hamada D, Fukui T, Ohnishi K, Kajiyama S, Shimizu T, Sato M, Ikegami T, Ikeguchi M, Honda T, Hashimoto H. </i> J Biol Chem, 2010","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00668r003","validated":{"curator_id":"bmesza","timestamp":"2020-12-12T21:05:45.498Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":35,"term_id":"IDPO:0000002","start":25,"version":2,"statement":[{"text":"It should also be noted that the three-dimensional TEM analysis did not produce a structure for the N-terminal region that was disordered in the crystal structure.","type":"Results"}],"term_name":"disorder","ec_name":"microscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20335168","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0001232","curator_id":"fquaglia","reference_html":"Structure and functional characterization of Vibrio parahaemolyticus thermostable direct hemolysin. <i> Yanagihara I, Nakahira K, Yamane T, Kaieda S, Mayanagi K, Hamada D, Fukui T, Ohnishi K, Kajiyama S, Shimizu T, Sato M, Ikegami T, Ikeguchi M, Honda T, Hashimoto H. </i> J Biol Chem, 2010","ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP00668r004","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T10:40:22.967Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":35,"term_id":"IDPO:0000002","start":25,"version":2,"statement":[{"text":"The averaged most populated volume envelope from the 20 SAXS models showed that the N-terminal region projected from the central pore and was found primarily on the longitudinal side of the tetramer. The structural model indicated that the missing N-terminal region was exposed to solvent and adopted a highly mobile conformation.","type":"Results"},{"text":"However, the N-terminal region (residues 1–11) was disordered in the crystal structure, and SAXS analysis revealed that this region was exposed to solvent and highly flexible. ","type":"Discussion"},{"text":"What the authors refer to as residues 1-11 correspond to residues 25-35 in the UniProt sequence","type":"Curator statement"}],"term_name":"disorder","ec_name":"small-angle X-ray scattering evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20335168","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006210","curator_id":"fquaglia","reference_html":"Structure and functional characterization of Vibrio parahaemolyticus thermostable direct hemolysin. <i> Yanagihara I, Nakahira K, Yamane T, Kaieda S, Mayanagi K, Hamada D, Fukui T, Ohnishi K, Kajiyama S, Shimizu T, Sato M, Ikegami T, Ikeguchi M, Honda T, Hashimoto H. </i> J Biol Chem, 2010","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00668r005","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T10:40:36.807Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":35,"term_id":"IDPO:0000002","start":25,"version":2,"statement":[{"text":"The N-terminal Pro-rich region (FELPSVPFPAP), however, was apparently hydrophobic, but its structure was not discernable by x-ray crystallography, three-dimensional TEM (Fig. 1), or NMR studies (supplemental Fig. 3)","type":"Results"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20335168","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"fquaglia","reference_html":"Structure and functional characterization of Vibrio parahaemolyticus thermostable direct hemolysin. <i> Yanagihara I, Nakahira K, Yamane T, Kaieda S, Mayanagi K, Hamada D, Fukui T, Ohnishi K, Kajiyama S, Shimizu T, Sato M, Ikegami T, Ikeguchi M, Honda T, Hashimoto H. </i> J Biol Chem, 2010","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P19250","date":"2016-08-24T10:46:37.000Z","acc":"P19250","name":"Thermostable direct hemolysin 2","length":189,"organism":"Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)","UniParc":"UPI000012C94A","genes":[{"name":{"value":"tdh2"},"synonyms":[{"value":"tdh"},{"value":"trh"}],"olnNames":[{"value":"VPA1314"}]}],"alphafold_very_low_content":0.12169312169312169,"disorder_content":0.0582010582010582,"disprot_consensus":{"full":[{"start":25,"end":35,"type":"D"}],"Structural state":[{"start":25,"end":35,"type":"D"}]}},{"acc":"P81019","sequence":"MAPLVGLFLIWAGASVFQQLHPVNGGDIPDPGSKPTPPGMADELPTETYDLPPEIYTTTFLPRTIYPQEEMPYDDKPFPSLLSKANDLNAVFEGPACAFPFTYKGKKYYMCTRKNSVLLWCSLDTEYQGNWKFCTERDEPECVFPFIYRKKSYESCTRVHSFFWRRWCSLTSNYDRDKAWKYC","alphafold_very_low_content":"0.15846994535519127","creator":"eschad","dataset":[],"date":"2016-09-13T13:26:41.000Z","disprot_id":"DP00669","features":{"pfam":[{"id":"PF00040","name":"Fibronectin type II domain","start":97,"end":134},{"id":"PF00040","name":"Fibronectin type II domain","start":142,"end":183}],"gene3D":[{"start":96,"end":134,"id":"2.10.10.10","name":"Fibronectin, type II, collagen-binding","_id":"685af523b4ac24d5329d8124"},{"start":140,"end":183,"id":"2.10.10.10","name":"Fibronectin, type II, collagen-binding","_id":"685af523b4ac24d5329d8125"}]},"genes":[],"length":183,"name":"Seminal plasma protein BSP-30 kDa","ncbi_taxon_id":9913,"organism":"Bos taurus","regions_counter":6,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"UniParc":"UPI000059CE9F","uniref100":"UniRef100_P81019","uniref50":"UniRef50_P81019","uniref90":"UniRef90_P81019","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":26,"end":96,"interaction_partner":[],"reference_html":"The N-terminal part of Binder of SPerm 5 (BSP5), which promotes sperm capacitation in bovine species is intrinsically disordered. <i> Jois PS, Manjunath P. </i> Biochem Biophys Res Commun, 2010","reference_id":"20331968","region_id":"DP00669r001","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"The circular dichroism (CD) spectrum of His-S–N-terminal part exhibits a negative peak at 201.5 nm (Fig. 3B), which is characteristic of a protein in largely unfolded conformation. The lack of characteristic minima around 208 and 222 nm is indicative of the absence of a -helix. There is a broad but weak negative ‘shoulder’ peak between 215 and 230 nm, implying the existence of small proportion of residual secondary structure.","_id":"685af523b4ac24d5329d8127"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-30T09:02:30.419Z","_id":"685af523b4ac24d5329d8128"},"version":3,"_id":"685af523b4ac24d5329d8126","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":26,"end":96,"interaction_partner":[],"reference_html":"The N-terminal part of Binder of SPerm 5 (BSP5), which promotes sperm capacitation in bovine species is intrinsically disordered. <i> Jois PS, Manjunath P. </i> Biochem Biophys Res Commun, 2010","reference_id":"20331968","region_id":"DP00669r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The purified Trx-His-S tagged recombinant proteins, i.e. FL, N-terminal part, A, B, and AB domain showed molecular weights of \u001842, 34, 29, 29 and 32 kDa, respectively. These sizes are \u001818%, 38%, 29%, 28%, and 6% larger for FL,\nN-terminal part (Fig. 2B), A, B, and AB domains, respectively (not shown). The reason for the anomalous migration of recombinant A and B domains is not clear. As depicted in Fig. 2A the His-S–N-terminal part migrated >90% higher than its theoretical molecular mass (12.8 kDa). This is probably due to the primary sequence of N-terminal part of BSP5, which includes many acidic residues and proline (Table 1). Such abnormal behavior has already been\nobserved in other intrinsically disordered proteins and can most\nlikely be ascribed to their unusual sequence and composition","_id":"685af523b4ac24d5329d812c"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-30T09:02:29.387Z","_id":"685af523b4ac24d5329d812d"},"version":3,"_id":"685af523b4ac24d5329d812b","reference_source":"pmid"}],"__v":0,"disorder_content":0.3879781420765027,"disprot_consensus":{"full":[{"start":26,"end":96,"type":"D"}],"Structural state":[{"start":26,"end":96,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00129","name":"Class I Histocompatibility antigen, domains alpha 1 and 2","start":25,"end":198},{"id":"PF07654","name":"Immunoglobulin C1-set domain","start":215,"end":288}],"gene3D":[{"start":207,"end":295,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":24,"end":203,"id":"3.30.500.10","name":"MHC class I-like antigen recognition-like"}]},"uniref50":"UniRef50_Q29983","sequence":"MGLGPVFLLLAGIFPFAPPGAAAEPHSLRYNLTVLSWDGSVQSGFLTEVHLDGQPFLRCDRQKCRAKPQGQWAEDVLGNKTWDRETRDLTGNGKDLRMTLAHIKDQKEGLHSLQEIRVCEIHEDNSTRSSQHFYYDGELFLSQNLETKEWTMPQSSRAQTLAMNVRNFLKEDAMKTKTHYHAMHADCLQELRRYLKSGVVLRRTVPPMVNVTRSEASEGNITVTCRASGFYPWNITLSWRQDGVSLSHDTQQWGDVLPDGNGTYQTWVATRICQGEEQRFTCYMEHSGNHSTHPVPSGKVLVLQSHWQTFHVSAVAAAAIFVIIIFYVRCCKKKTSAAEGPELVSLQVLDQHPVGTSDHRDATQLGFQPLMSDLGSTGSTEGA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q29983","disprot_id":"DP00670","ncbi_taxon_id":9606,"regions_counter":4,"creator":"mnecci","regions":[{"region_id":"DP00670r003","ec_ontology":"ECO","end":184,"term_id":"IDPO:0000002","start":175,"version":2,"statement":[{"text":"In MIC-A, no electron density is observed for ten residues (152–161) in one section of these helices (corresponding to helix 2a in the α2 domain of HLA-B27) or for the polyhistidine purification tag.","type":"Results"},{"text":"The region corresponds to region 175-184 of the protein sequence.","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10367903","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1B3J"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Crystal structure of the MHC class I homolog MIC-A, a gammadelta T cell ligand. <i> Li P, Willie ST, Bauer S, Morris DL, Spies T, Strong RK. </i> Immunity, 1999","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":184,"term_name":"disorder","reference_id":"10367903","released":"2022_03","term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","start":175,"term_ontology":"IDPO","version":2,"curator_name":"Federica Quaglia","ec_name":"cleavage assay evidence used in manual assertion","statement":[{"text":"Preliminary results from limited proteolysis with thermolysin at pH 7.5, in which MIC-A is initially cleaved in the region of this loop, suggest that this loop is exposed and flexible at near neutral pH as well (data not shown).","type":"Results"},{"text":"The region corresponds to region 175-184 of the protein sequence.","type":"Curator statement"}],"reference_html":"Crystal structure of the MHC class I homolog MIC-A, a gammadelta T cell ligand. <i> Li P, Willie ST, Bauer S, Morris DL, Spies T, Strong RK. </i> Immunity, 1999","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","region_id":"DP00670r004","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q29983","date":"2016-09-12T15:58:12.000Z","acc":"Q29983","name":"MHC class I polypeptide-related sequence A","length":383,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000008A7B0","genes":[{"name":{"value":"MICA","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"CAI41907.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAI41907.1"}}]},"synonyms":[{"value":"PERB11.1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8613147","url":"http://www.ncbi.nlm.nih.gov/pubmed/8613147","alternativeUrl":"https://europepmc.org/abstract/MED/8613147"}}]}]}],"alphafold_very_low_content":0.17754569190600522,"disorder_content":0.02610966057441253,"disprot_consensus":{"full":[{"start":175,"end":184,"type":"D"}],"Structural state":[{"start":175,"end":184,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00010","name":"Helix-loop-helix DNA-binding domain","start":93,"end":142}],"gene3D":[{"start":92,"end":150,"id":"4.10.280.10","name":"Helix-loop-helix DNA-binding domain"}]},"uniref50":"UniRef50_Q92886","sequence":"MPARLETCISDLDCASSSGSDLSGFLTDEEDCARLQQAASASGPPAPARRGAPNISRASEVPGAQDDEQERRRRRGRTRVRSEALLHSLRRSRRVKANDRERNRMHNLNAALDALRSVLPSFPDDTKLTKIETLRFAYNYIWALAETLRLADQGLPGGGARERLLPPQCVPCLPGPPSPASDAESWGSGAAAASPLSDPSSPAASEDFTYRPGDPVFSFPSLPKDLLHTTPCFIPYH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q92886","disprot_id":"DP00672","ncbi_taxon_id":9606,"regions_counter":5,"creator":"ktsirigos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":150,"region_id":"DP00672r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"The basic helix-loop-helix region of human neurogenin 1 is a monomeric natively unfolded protein which forms a \"fuzzy\" complex upon DNA binding. <i> Aguado-Llera D, Goormaghtigh E, de Geest N, Quan XJ, Prieto A, Hassan BA, Gómez J, Neira JL. </i> Biochemistry, 2010","term_id":"IDPO:0000002","curator_id":"vnugnes","start":90,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"20102160","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-05-22T16:33:39.098Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The 1D-NMR spectrum of bHLHN at 298 K did not show a chemical shift dispersion in the amide (Figure 3A) nor in the methyl regions (Figure 2 of Supporting Information). In those regions all of the resonances were clustered as expected for random-coil proteins (54), namely, between 8.0 and 8.7 ppm (for the amide signals) (Figure 3A,B) and between 0.8 and 1.0 ppm (for the methyl protons) (Figure 2 of Supporting Information).","type":"Results"}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":150,"term_name":"DNA binding","start":90,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"20102160","version":4,"reference_html":"The basic helix-loop-helix region of human neurogenin 1 is a monomeric natively unfolded protein which forms a \"fuzzy\" complex upon DNA binding. <i> Aguado-Llera D, Goormaghtigh E, de Geest N, Quan XJ, Prieto A, Hassan BA, Gómez J, Neira JL. </i> Biochemistry, 2010","date":"2023-05-22T16:33:02.024Z","term_id":"GO:0003677","ec_id":"ECO:0006204","region_id":"DP00672r004","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"statement":[{"text":"This lack of signal dispersion in the NMR spectra, even though there is an increase of structure (as reported by CD, Figure 5A,B), could be due to the different spectroscopic time scales of far-UV CD and NMR, but it could be also reflecting the presence of a “fuzzy” complex between DNA and bHLHN (20, 68), where the increased amount of secondary structure (as monitored by CD) is flickering and not hydrogen-bonded, and there are still long polypeptide patches which remain disordered.","type":"Discussion"},{"text":"The assayed E-boxes correspond to E3-oligo, 5′-CTCTAACTGGCGACAGATGGGCCACTTTCT-3′, and E1-oligo, 5′-GGACCGGGAAGACCATATGGCGCATGCCGG-3′, which are the boxes recognized by NGN3, when forming heterodimers with the bHLH of the E47 protein (28).","type":"Methods"}]},{"start":90,"end":150,"reference_id":"20102160","reference_source":"pmid","reference_html":"The basic helix-loop-helix region of human neurogenin 1 is a monomeric natively unfolded protein which forms a \"fuzzy\" complex upon DNA binding. <i> Aguado-Llera D, Goormaghtigh E, de Geest N, Quan XJ, Prieto A, Hassan BA, Gómez J, Neira JL. </i> Biochemistry, 2010","date":"2023-05-22T16:27:05.313Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005632","ec_ontology":"ECO","ec_name":"fluorescence anisotropy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00672r005","statement":[{"text":"Our calculations suggest that the size of bHLHN is halfway between that of a molten globule (16.9 Å) and that of a premolten globule (21 Å). Since we have tested that bHLHN does not bind ANS (see above), as happens in other premolten globule structures (18), we suggest that the domain acquires a slightly collapsed premolten globule conformation.","type":"Discussion"}]}],"released":"2016_10","uniref100":"UniRef100_Q92886","date":"2016-09-13T12:45:28.000Z","acc":"Q92886","name":"Neurogenin-1","length":237,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI0000130002","genes":[{"name":{"value":"NEUROG1"},"synonyms":[{"value":"BHLHA6"},{"value":"NEUROD3"},{"value":"NGN"},{"value":"NGN1"}]}],"alphafold_very_low_content":0.28270042194092826,"disorder_content":0.25738396624472576,"disprot_consensus":{"full":[{"start":90,"end":150,"type":"D"}],"Structural state":[{"start":90,"end":150,"type":"D"}],"Molecular function":[{"start":90,"end":150,"type":"F"}]}},{"acc":"P06935","sequence":"MSKKPGGPGKNRAVNMLKRGMPRGLSLIGLKRAMLSLIDGKGPIRFVLALLAFFRFTAIAPTRAVLDRWRGVNKQTAMKHLLSFKKELGTLTSAINRRSTKQKKRGGTAGFTILLGLIACAGAVTLSNFQGKVMMTVNATDVTDVITIPTAAGKNLCIVRAMDVGYLCEDTITYECPVLAAGNDPEDIDCWCTKSSVYVRYGRCTKTRHSRRSRRSLTVQTHGESTLANKKGAWLDSTKATRYLVKTESWILRNPGYALVAAVIGWMLGSNTMQRVVFAILLLLVAPAYSFNCLGMSNRDFLEGVSGATWVDLVLEGDSCVTIMSKDKPTIDVKMMNMEAANLADVRSYCYLASVSDLSTRAACPTMGEAHNEKRADPAFVCKQGVVDRGWGNGCGLFGKGSIDTCAKFACTTKATGWIIQKENIKYEVAIFVHGPTTVESHGKIGATQAGRFSITPSAPSYTLKLGEYGEVTVDCEPRSGIDTSAYYVMSVGEKSFLVHREWFMDLNLPWSSAGSTTWRNRETLMEFEEPHATKQSVVALGSQEGALHQALAGAIPVEFSSNTVKLTSGHLKCRVKMEKLQLKGTTYGVCSKAFKFARTPADTGHGTVVLELQYTGTDGPCKVPISSVASLNDLTPVGRLVTVNPFVSVATANSKVLIELEPPFGDSYIVVGRGEQQINHHWHKSGSSIGKAFTTTLRGAQRLAALGDTAWDFGSVGGVFTSVGKAIHQVFGGAFRSLFGGMSWITQGLLGALLLWMGINARDRSIAMTFLAVGGVLLFLSVNVHADTGCAIDIGRQELRCGSGVFIHNDVEAWMDRYKFYPETPQGLAKIIQKAHAEGVCGLRSVSRLEHQMWEAIKDELNTLLKENGVDLSVVVEKQNGMYKAAPKRLAATTEKLEMGWKAWGKSIIFAPELANNTFVIDGPETEECPTANRAWNSMEVEDFGFGLTSTRMFLRIRETNTTECDSKIIGTAVKNNMAVHSDLSYWIESGLNDTWKLERAVLGEVKSCTWPETHTLWGDGVLESDLIIPITLAGPRSNHNRRPGYKTQNQGPWDEGRVEIDFDYCPGTTVTISDSCEHRGPAARTTTESGKLITDWCCRSCTLPPLRFQTENGCWYGMEIRPTRHDEKTLVQSRVNAYNADMIDPFQLGLMVVFLATQEVLRKRWTAKISIPAIMLALLVLVFGGITYTDVLRYVILVGAAFAEANSGGDVVHLALMATFKIQPVFLVASFLKARWTNQESILLMLAAAFFQMAYYDAKNVLSWEVPDVLNSLSVAWMILRAISFTNTSNVVVPLLALLTPGLKCLNLDVYRILLLMVGVGSLIKEKRSSAAKKKGACLICLALASTGVFNPMILAAGLMACDPNRKRGWPATEVMTAVGLMFAIVGGLAELDIDSMAIPMTIAGLMFAAFVISGKSTDMWIERTADITWESDAEITGSSERVDVRLDDDGNFQLMNDPGAPWKIWMLRMACLAISAYTPWAILPSVIGFWITLQYTKRGGVLWDTPSPKEYKKGDTTTGVYRIMTRGLLGSYQAGAGVMVEGVFHTLWHTTKGAALMSGEGRLDPYWGSVKEDRLCYGGPWKLQHKWNGHDEVQMIVVEPGKNVKNVQTKPGVFKTPEGEIGAVTLDYPTGTSGSPIVDKNGDVIGLYGNGVIMPNGSYISAIVQGERMEEPAPAGFEPEMLRKKQITVLDLHPGAGKTRKILPQIIKEAINKRLRTAVLAPTRVVAAEMSEALRGLPIRYQTSAVHREHSGNEIVDVMCHATLTHRLMSPHRVPNYNLFIMDEAHFTDPASIAARGYIATKVELGEAAAIFMTATPPGTSDPFPESNAPISDMQTEIPDRAWNTGYEWITEYVGKTVWFVPSVKMGNEIALCLQRAGKKVIQLNRKSYETEYPKCKNDDWDFVITTDISEMGANFKASRVIDSRKSVKPTIIEEGDGRVILGEPSAITAASAAQRRGRIGRNPSQVGDEYCYGGHTNEDDSNFAHWTEARIMLDNINMPNGLVAQLYQPEREKVYTMDGEYRLRGEERKNFLEFLRTADLPVWLAYKVAAAGISYHDRKWCFDGPRTNTILEDNNEVEVITKLGERKILRPRWADARVYSDHQALKSFKDFASGKRSQIGLVEVLGRMPEHFMVKTWEALDTMYVVATAEKGGRAHRMALEELPDALQTIVLIALLSVMSLGVFFLLMQRKGIGKIGLGGVILGAATFFCWMAEVPGTKIAGMLLLSLLLMIVLIPEPEKQRSQTDNQLAVFLICVLTLVGAVAANEMGWLDKTKNDIGSLLGHRPEARETTLGVESFLLDLRPATAWSLYAVTTAVLTPLLKHLITSDYINTSLTSINVQASALFTLARGFPFVDVGVSALLLAVGCWGQVTLTVTVTAAALLFCHYAYMVPGWQAEAMRSAQRRTAAGIMKNVVVDGIVATDVPELERTTPVMQKKVGQIILILVSMAAVVVNPSVRTVREAGILTTAAAVTLWENGASSVWNATTAIGLCHIMRGGWLSCLSIMWTLIKNMEKPGLKRGGAKGRTLGEVWKERLNHMTKEEFTRYRKEAITEVDRSAAKHARREGNITGGHPVSRGTAKLRWLVERRFLEPVGKVVDLGCGRGGWCYYMATQKRVQEVKGYTKGGPGHEEPQLVQSYGWNIVTMKSGVDVFYRPSEASDTLLCDIGESSSSAEVEEHRTVRVLEMVEDWLHRGPKEFCIKVLCPYMPKVIEKMETLQRRYGGGLIRNPLSRNSTHEMYWVSHASGNIVHSVNMTSQVLLGRMEKKTWKGPQFEEDVNLGSGTRAVGKPLLNSDTSKIKNRIERLKKEYSSTWHQDANHPYRTWNYHGSYEVKPTGSASSLVNGVVRLLSKPWDTITNVTTMAMTDTTPFGQQRVFKEKVDTKAPEPPEGVKYVLNETTNWLWAFLARDKKPRMCSREEFIGKVNSNAALGAMFEEQNQWKNAREAVEDPKFWEMVDEEREAHLRGECNTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARFLEFEALGFLNEDHWLGRKNSGGGVEGLGLQKLGYILKEVGTKPGGKVYADDTAGWDTRITKADLENEAKVLELLDGEHRRLARSIIELTYRHKVVKVMRPAADGKTVMDVISREDQRGSGQVVTYALNTFTNLAVQLVRMMEGEGVIGPDDVEKLGKGKGPKVRTWLFENGEERLSRMAVSGDDCVVKPLDDRFATSLHFLNAMSKVRKDIQEWKPSTGWYDWQQVPFCSNHFTELIMKDGRTLVVPCRGQDELIGRARISPGAGWNVRDTACLAKSYAQMWLLLYFHRRDLRLMANAICSAVPANWVPTGRTTWSIHAKGEWMTTEDMLAVWNRVWIEENEWMEDKTPVERWSDVPYSGKREDIWCGSLIGTRTRATWAENIHVAINQVRSVIGEEKYVDYMSSLRRYEDTIVVEDTVL","creator":"lchemes","dataset":["Viral proteins","Neglected tropical diseases proteins","RNA-binding proteins"],"date":"2016-09-02T11:37:33.000Z","disprot_id":"DP00673","features":{"pfam":[{"id":"PF00869","name":"Flavivirus glycoprotein, central and dimerisation domains","start":293,"end":585},{"id":"PF00948","name":"Flavivirus non-structural Protein NS1","start":790,"end":1139},{"id":"PF00949","name":"Peptidase S7, Flavivirus NS3 serine protease","start":1519,"end":1668},{"id":"PF00972","name":"Flavivirus RNA-directed RNA polymerase, fingers and palm domains","start":2779,"end":3230},{"id":"PF01002","name":"Flavivirus non-structural protein NS2B","start":1376,"end":1495},{"id":"PF01003","name":"Flavivirus capsid protein C","start":6,"end":123},{"id":"PF01004","name":"Flavivirus envelope glycoprotein M","start":218,"end":290},{"id":"PF01005","name":"Flavivirus non-structural protein NS2A","start":1151,"end":1304},{"id":"PF01349","name":"Flavivirus non-structural protein NS4B","start":2270,"end":2516},{"id":"PF01350","name":"Flavivirus non-structural protein NS4A","start":2126,"end":2267},{"id":"PF01570","name":"Flavivirus polyprotein propeptide","start":133,"end":214},{"id":"PF01728","name":"FtsJ-like methyltransferase","start":2580,"end":2748},{"id":"PF02832","name":"Flavivirus glycoprotein, immunoglobulin-like domain","start":588,"end":685},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1686,"end":1832},{"id":"PF20483","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","start":3234,"end":3397},{"id":"PF20907","name":"Flavivirus NS3 helicase, C-terminal helical domain","start":1976,"end":2118},{"id":"PF21659","name":"Flavivirus envelope glycoprotein E, stem/anchor domain","start":688,"end":782}],"gene3D":[{"start":584,"end":692,"id":"2.60.40.350","name":"2.60.40.350","_id":"685af523b4ac24d5329d8142"},{"start":216,"end":290,"id":"1.10.8.970","name":"Flavivirus envelope glycoprotein M-like","_id":"685af523b4ac24d5329d8143"},{"start":693,"end":787,"id":"1.20.1280.260","name":"1.20.1280.260","_id":"685af523b4ac24d5329d8144"},{"start":291,"end":583,"id":"2.60.98.10","name":"Tick-borne Encephalitis virus Glycoprotein, domain 1","_id":"685af523b4ac24d5329d8145"},{"start":124,"end":205,"id":"2.60.260.50","name":"Flavivirus polyprotein propeptide domain","_id":"685af523b4ac24d5329d8146"},{"start":23,"end":98,"id":"1.10.10.930","name":"1.10.10.930","_id":"685af523b4ac24d5329d8147"},{"start":1415,"end":1464,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d8148"},{"start":1513,"end":1587,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d8149"},{"start":2921,"end":3016,"id":"1.10.260.90","name":"1.10.260.90","_id":"685af523b4ac24d5329d814a"},{"start":3057,"end":3124,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d814b"},{"start":1824,"end":1983,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d814c"},{"start":1512,"end":1670,"id":"2.40.10.10","name":"Trypsin-like serine proteases","_id":"685af523b4ac24d5329d814d"},{"start":1685,"end":2018,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d814e"},{"start":2525,"end":2797,"id":"3.40.50.150","name":"Vaccinia Virus protein VP39","_id":"685af523b4ac24d5329d814f"},{"start":2798,"end":2853,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d8150"},{"start":2856,"end":2904,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d8151"}]},"genes":[],"length":3430,"name":"Genome polyprotein","ncbi_taxon_id":11082,"organism":"West Nile virus","regions_counter":19,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Flavivirus"],"UniParc":"UPI00000011F3","uniref100":"UniRef100_P06935","uniref50":"UniRef50_P06935","uniref90":"UniRef90_P06935","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":24,"interaction_partner":[],"reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","reference_id":"18033802","region_id":"DP00673r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"CD spectroscopy of WNV peptides (1–24) and (80–105) revealed that they are both completely unfolded (Figure 7C; deconvolution data not shown), suggesting that RNA chaperone activity of WNV core protein does not require a well-defined structure.","_id":"685af523b4ac24d5329d815b"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-11T07:32:15.644Z","_id":"685af523b4ac24d5329d815c"},"version":3,"_id":"685af523b4ac24d5329d815a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":80,"end":105,"interaction_partner":[],"reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","reference_id":"18033802","region_id":"DP00673r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"CD spectroscopy of WNV peptides (1–24) and (80–105) revealed that they are both completely unfolded (Figure 7C; deconvolution data not shown), suggesting that RNA chaperone activity of WNV core protein does not require a well-defined structure.","_id":"685af523b4ac24d5329d8164"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-11T07:32:14.600Z","_id":"685af523b4ac24d5329d8165"},"version":3,"_id":"685af523b4ac24d5329d8163","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001807","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":24,"interaction_partner":[],"reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","reference_id":"18033802","region_id":"DP00673r015","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As shown in Figure 7A, WNV 1–24 exhibited only a low level of strand-annealing activity, while WNV 80–105 caused efficient DNA duplex formation.","_id":"685af523b4ac24d5329d8173"}],"states_connection":[],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_id":"GO:0003677","term_is_binding":true,"term_is_obsolete":false,"term_name":"DNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-11T07:32:50.718Z","_id":"685af523b4ac24d5329d8174"},"version":1,"_id":"685af523b4ac24d5329d8172","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001807","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","ec_ontology":"ECO","start":80,"end":105,"interaction_partner":[],"reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","reference_id":"18033802","region_id":"DP00673r016","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As shown in Figure 7A, WNV 1–24 exhibited only a low level of strand-annealing activity, while WNV 80–105 caused efficient DNA duplex formation.","_id":"685af523b4ac24d5329d8176"}],"states_connection":[],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_id":"GO:0003677","term_is_binding":true,"term_is_obsolete":false,"term_name":"DNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-11T07:32:29.257Z","_id":"685af523b4ac24d5329d8177"},"version":1,"_id":"685af523b4ac24d5329d8175","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0005801","ec_name":"enzymatic activity assay evidence used in manual assertion","ec_ontology":"ECO","start":80,"end":105,"interaction_partner":[],"reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","reference_id":"18033802","region_id":"DP00673r017","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The RNA chaperone activity of the WNV (80–105) peptide was further confirmed with the ribozyme cleavage assay, which requires both the strand annealing and helix unwinding activities of a chaperone.","_id":"685af523b4ac24d5329d8179"},{"type":"Results","text":" As expected, all core proteins induced a considerable increase in the cleavage rates, with hepacivirus core proteins demonstrating a higher activity compared to WNV and BVDV cores (Figure 4C).","_id":"685af523b4ac24d5329d817a"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA or an RNA-containing complex to assist the folding process.\" [PMID:31165735]","term_id":"GO:0140691","term_is_binding":false,"term_is_obsolete":false,"term_name":"RNA folding chaperone","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-11T07:32:52.639Z","_id":"685af523b4ac24d5329d817b"},"version":1,"_id":"685af523b4ac24d5329d8178","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0005801","ec_name":"enzymatic activity assay evidence used in manual assertion","ec_ontology":"ECO","start":80,"end":105,"interaction_partner":[],"reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","reference_id":"18033802","region_id":"DP00673r018","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The RNA chaperone activity of the WNV (80–105) peptide was further confirmed with the ribozyme cleavage assay, which requires both the strand annealing and helix unwinding activities of a chaperone.","_id":"685af523b4ac24d5329d817d"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_id":"GO:0003723","term_is_binding":true,"term_is_obsolete":false,"term_name":"RNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-11T07:32:20.764Z","_id":"685af523b4ac24d5329d817e"},"version":1,"_id":"685af523b4ac24d5329d817c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2FP7","_id":"685af523b4ac24d5329d8180"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-20T19:37:59.229Z","disprot_namespace":"Structural state","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1672,"end":1688,"interaction_partner":[],"reference_html":"Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus. <i> Erbel P, Schiering N, D'Arcy A, Renatus M, Kroemer M, Lim SP, Yin Z, Keller TH, Vasudevan SG, Hommel U. </i> Nat Struct Mol Biol, 2006","reference_id":"16532006","region_id":"DP00673r019","released":"2022_12","sample":[{"db":"UniProt","deviation":null,"id":"P06935","statements":[],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d8181"}],"statement":[{"type":"Curator statement","text":"The PDB shows this region lacks electron density, indicating it is disordered.","_id":"685af523b4ac24d5329d8182"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-15T17:06:13.020Z","_id":"685af523b4ac24d5329d8183"},"version":0,"_id":"685af523b4ac24d5329d817f","reference_source":"pmid"}],"__v":0,"disorder_content":0.019533527696793004,"disprot_consensus":{"full":[{"start":1,"end":24,"type":"D"},{"start":80,"end":105,"type":"D"},{"start":1672,"end":1688,"type":"D"}],"Structural state":[{"start":1,"end":24,"type":"D"},{"start":80,"end":105,"type":"D"},{"start":1672,"end":1688,"type":"D"}],"Molecular function":[{"start":1,"end":24,"type":"F"},{"start":80,"end":105,"type":"F"}]}},{"acc":"Q69422","sequence":"MPVISTQTSPVPAPRTRKNKQTQASYPVSIKTSVERGQRAKRKVQRDARPRNYKIAGIHDGLQTLAQAALPAHGWGRQDPRHKSRNLGILLDYPLGWIGDVTTHTPLVGPLVAGAVVRPVCQIVRLLEDGVNWATGWFGVHLFVVCLLSLACPCSGARVTDPDTNTTILTNCCQRNQVIYCSPSTCLHEPGCVICADECWVPANPYISHPSNWTGTDSFLADHIDFVMGALVTCDALDIGELCGACVLVGDWLVRHWLIHIDLNETGTCYLEVPTGIDPGFLGFIGWMAGKVEAVIFLTKLASQVPYAIATMFSSVHYLAVGALIYYASRGKWYQLLLALMLYIEATSGNPIRVPTGCSIAEFCSPLMIPCPCHSYLSENVSEVICYSPKWTRPVTLEYNNSISWYPYTIPGARGCMVKFKNNTWGCCRIRNVPSYCTMGTDAVWNDTRNTYEACGVTPWLTTAWHNGSALKLAILQYPGSKEMFKPHNWMSGHLYFEGSDTPIVYFYDPVNSTLLPPERWARLPGTPPVVRGSWLQVPQGFYSDVKDLATGLITKDKAWKNYQVLYSATGALSLTGVTTKAVVLILLGLCGSKYLILAYLCYLSLCFGRASGYPLRPVLPSQSYLQAGWDVLSKAQVAPFALIFFICCYLRCRLRYAALLGFVPMAAGLPLTFFVAAAAAQPDYDWWVRLLVAGLVLWAGRDRGPRIALLVGPWPLVALLTLLHLATPASAFDTEIIGGLTIPPVVALVVMSRFGFFAHLLPRCALVNSYLWQRWENWFWNVTLRPERFLLVLVCFPGATYDTLVTFCVCHVALLCLTSSAASFFGTDSRVRAHRMLVRLGKCHAWYSHYVLKFFLLVFGENGVFFYKHLHGDVLPNDFASKLPLQEPFFPFEGKARVYRNEGRRLACGDTVDGLPVVARLGDLVFAGLAMPPDGWAITAPFTLQCLSERGTLSAMAVVMTGIDPRTWTGTIFRLGSLATSYMGFVCDNVLYTAHHGSKGRRLAHPTGSIHPITVDAANDQDIYQPPCGAGSLTRCSCGETKGYLVTRLGSLVEVNKSDDPYWCVCGALPMAVAKGSSGAPILCSSGHVIGMFTAARNSGGSVSQIRVRPLVCAGYHPQYTAHATLDTKPTVPNEYSVQILIAPTGSGKSTKLPLSYMQEKYEVLVLNPSVATTASMPKYMHATYGVNPNCYFNGKCTNTGASLTYSTYGMYLTGACSRNYDVIICDECHATDATTVLGIGKVLTEAPSKNVRLVVLATATPPGVIPTPHANITEIQLTDEGTIPFHGKKIKEENLKKGRHLIFEATKKHCDELANELARKGITAVSYYRGCDISKIPEGDCVVVATDALCTGYTGDFDSVYDCSLMVEGTCHVDLDPTFTMGVRVCGVSAIVKGQRRGRTGRGRAGIYYYVDGSCTPSGMVPECNIVEAFDAAKAWYGLSSTEAQTILDTYRTQPGLPAIGANLDEWADLFSMVNPEPSFVNTAKRTADNYVLLTAAQLQLCHQYGYAAPNDAPRWQGARLGKKPCGVLWRLDGADACPGPEPSEVTRYQMCFTEVNTSGTAALAVGVGVAMAYLAIDTFGATCVRRCWSITSVPTGATVAPVVDEEEIVEECASFIPLEAMVAAIDKLKSTITTTSPFTLETALEKLNTFLGPHAATILAIIEYCCGLVTLPDNPFASCVFAFIAGITTPLPHKIKMFLSLFGGAIASKLTDARGALAFMMAGAAGTALGTWTSVGFVFDMLGGYAAASSTACLTFKCLMGEWPTMDQLAGLVYSAFNPAAGVVGVLSACAMFALTTAGPDHWPNRLLTMLARSNTVCNEYFIATRDIRRKILGILEASTPWSVISACIRWLHTPTEDDCGLIAWGLEIWQYVCNFFVICFNVLKAGVQSMVNIPGCPFYSCQKGYKGPWIGSGMLQARCPCGAELIFSVENGFAKLYKGPRTCSNYWRGAVPVNARLCGSARPDPTDWTSLVVNYGVRDYCKYEKLGDHIFVTAVSSPNVCFTQVPPTLRAAVAVDGVQVQCYLGEPKTPWTTSACCYGPDGKGKTVKLPFRVDGHTPGVRMQLNLRDALETNDCNSINNTPSDEAAVSALVFKQELRRTNQLLEAISAGVDTTKLPAPSIEEVVVRKRQFRARTGSLTLPPPPRSVPGVSCPESLQRSDPLEGPSNLPSSPPVLQLAMPMPLLGAGECNPFTAIGCAMTETGGGPDDLPSYPPKKEVSEWSDGSWSTTTTASSYVTGPPYPKIRGKDSTQSAPAKRPTKKKLGKSEFSCSMSYTWTDVISFKTASKVLSATRAITSGFLKQRSLVYVTEPRDAELRKQKVTINRQPLFPPSYHKQVRLAKEKASKVVGVMWDYDEVAAHTPSKSAKSHITGLRGTDVRSGAARKAVLDLQKCVEAGEIPSHYRQTVIVPKEEVFVKTPQKPTKKPPRLISYPHLEMRCVEKMYYGQVAPDVVKAVMGDAYGFVDPRTRVKRLLSMWSPDAVGATCDTVCFDSTITPEDIMVETDIYSAAKLSDQHRAGIHTIARQLYAGGPMIAYDGREIGYRRCRSSGVYTTSSSNSLTCWLKVNAAAEQAGMKNPRFLICGDDCTVIWKSAGADADKQAMRVFASWMKVMGAPQDCVPQPKYSLEELTSCSSNVTSGITKSGKPYYFLTRDPRIPLGRCSAEGLGYNPSAAWIGYLIHHYPCLWVSRVLAVHFMEQMLFEDKLPETVTFDWYGKNYTVPVEDLPSIIAGVHGIEAFSVVRYTNAEILRVSQSLTDMTMPPLRAWRKKARAVLASAKRRGGAHAKLARFLLWHATSRPLPDLDKTSVARYTTFNYCDVYSPEGDVFVTPQRRLQKFLVKYLAVIVFALGLIAVGLAIS","creator":"esalladini","dataset":["Viral proteins","RNA-binding proteins"],"date":"2016-09-02T11:08:57.000Z","disprot_id":"DP00674","features":{"pfam":[{"id":"PF00998","name":"Viral RNA dependent RNA polymerase","start":2277,"end":2783},{"id":"PF01001","name":"Hepatitis C virus non-structural protein NS4b","start":1617,"end":1812},{"id":"PF01006","name":"Hepatitis C virus non-structural protein NS4a","start":1566,"end":1615},{"id":"PF01506","name":"Hepatitis C virus non-structural 5a protein membrane anchor","start":1866,"end":1888},{"id":"PF01539","name":"Hepatitis C virus envelope glycoprotein E1","start":168,"end":343},{"id":"PF01542","name":"Hepatitis C virus core protein","start":84,"end":151},{"id":"PF02907","name":"Hepatitis C virus NS3 protease","start":970,"end":1117},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1206,"end":1273},{"id":"PF08300","name":"Hepatitis C virus non-structural 5a zinc finger domain","start":1901,"end":1959},{"id":"PF08301","name":"Hepatitis C virus non-structural 5a domain 1b","start":1963,"end":2056}],"gene3D":[{"start":1908,"end":1969,"id":"2.20.25.210","name":"Hepatitis C NS5A, domain 1B","_id":"685af523b4ac24d5329d818f"},{"start":2544,"end":2639,"id":"3.30.70.270","name":"3.30.70.270","_id":"685af523b4ac24d5329d8190"},{"start":1265,"end":1420,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d8191"},{"start":2462,"end":2527,"id":"3.30.70.270","name":"3.30.70.270","_id":"685af523b4ac24d5329d8192"},{"start":951,"end":1124,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d8193"},{"start":1125,"end":1264,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d8194"},{"start":172,"end":236,"id":"2.30.30.1080","name":"Hepatitis C virus envelope glycoprotein E1, chain C","_id":"685af523b4ac24d5329d8195"},{"start":1366,"end":1538,"id":"1.10.820.10","name":"RNA Helicase Chain A , domain 3","_id":"685af523b4ac24d5329d8196"}]},"genes":[],"length":2864,"name":"Genome polyprotein","ncbi_taxon_id":39113,"organism":"Hepatitis GB virus B","regions_counter":11,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Hepacivirus"],"UniParc":"UPI00000F3C37","uniref100":"UniRef100_Q69422","uniref50":"UniRef50_Q69422","uniref90":"UniRef90_Q69422","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006317","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":155,"interaction_partner":[],"reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","reference_id":"18033802","region_id":"DP00674r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"FL HCV and GBV-B core proteins retained most of their chaperone activity after boiling for 5 min (∼75%, based on PhosporImager quantification, see lanes 4–6 versus 7–9 in Figure 4A and lanes 29–31 versus 32–34 in Figure 4B).","_id":"685af523b4ac24d5329d8198"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T12:51:54.651Z","_id":"685af523b4ac24d5329d8199"},"version":3,"_id":"685af523b4ac24d5329d8197","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":155,"interaction_partner":[],"reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","reference_id":"18033802","region_id":"DP00674r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The isolated N-terminal domain of HCV core [core(2–117)], as well as the FL HCV and GBV-B core proteins are mostly unstructured in solution, showing an ellipticity minimum at ∼198 nm, characteristically of random-coil like peptides [(36) and Figure 5].","_id":"685af523b4ac24d5329d81a1"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T12:51:49.147Z","_id":"685af523b4ac24d5329d81a2"},"version":3,"_id":"685af523b4ac24d5329d81a0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001807","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":155,"interaction_partner":[],"reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","reference_id":"18033802","region_id":"DP00674r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The ability of purified proteins to stably bind RNA and DNA was verified by means of mobility shift assays. All four proteins bound both to RNA and DNA without a strict sequence specificity, and they caused complete retention of the nucleic acids at the top of the gel (indicative of the formation of large nucleoprotein complexes) at a protein-to-nucleotide molar ratio of ∼1:20 (data not shown).","_id":"685af523b4ac24d5329d81aa"}],"states_connection":[],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_id":"GO:0003677","term_is_binding":true,"term_is_obsolete":false,"term_name":"DNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T12:52:03.213Z","_id":"685af523b4ac24d5329d81ab"},"version":1,"_id":"685af523b4ac24d5329d81a9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001807","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":155,"interaction_partner":[],"reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","reference_id":"18033802","region_id":"DP00674r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The ability of purified proteins to stably bind RNA and DNA was verified by means of mobility shift assays. All four proteins bound both to RNA and DNA without a strict sequence specificity, and they caused complete retention of the nucleic acids at the top of the gel (indicative of the formation of large nucleoprotein complexes) at a protein-to-nucleotide molar ratio of ∼1:20 (data not shown).","_id":"685af523b4ac24d5329d81ad"}],"states_connection":[],"term_comment":"","term_def":"\"The activity of binding selectively and non-covalently to and distorting the original structure of DNA, typically a straight helix, into a bend, or increasing the bend if the original structure was intrinsically bent due to its sequence.\" [GOC:krc, GOC:vw, PMID:10710711, PMID:19037758]","term_id":"GO:0008301","term_is_binding":true,"term_is_obsolete":false,"term_name":"DNA binding, bending","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T12:52:04.418Z","_id":"685af523b4ac24d5329d81ae"},"version":1,"_id":"685af523b4ac24d5329d81ac","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0005801","ec_name":"enzymatic activity assay evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":155,"interaction_partner":[],"reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","reference_id":"18033802","region_id":"DP00674r011","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"By means of classical in vitro RNA chaperone assays (e.g. strand annealing, strand exchange and ribozyme assays; Figures 2 and ​and3,3, and data not shown), we showed that nucleic acid chaperone activity is also conserved between the two hepacivirus core proteins, and that GBV-B core also efficiently facilitates the formation of the most stable nucleic acid structure. ","_id":"685af523b4ac24d5329d81b0"},{"type":"Results","text":" As expected, all core proteins induced a considerable increase in the cleavage rates, with hepacivirus core proteins demonstrating a higher activity compared to WNV and BVDV cores (Figure 4C).","_id":"685af523b4ac24d5329d81b1"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA or an RNA-containing complex to assist the folding process.\" [PMID:31165735]","term_id":"GO:0140691","term_is_binding":false,"term_is_obsolete":false,"term_name":"RNA folding chaperone","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T12:52:02.334Z","_id":"685af523b4ac24d5329d81b2"},"version":1,"_id":"685af523b4ac24d5329d81af","reference_source":"pmid"}],"__v":0,"disorder_content":0.05377094972067039,"disprot_consensus":{"full":[{"start":2,"end":155,"type":"D"}],"Structural state":[{"start":2,"end":155,"type":"D"}],"Molecular function":[{"start":2,"end":155,"type":"F"}]}},{"acc":"P19711","sequence":"MELITNELLYKTYKQKPVGVEEPVYDQAGDPLFGERGAVHPQSTLKLPHKRGERDVPTNLASLPKRGDCRSGNSRGPVSGIYLKPGPLFYQDYKGPVYHRAPLELFEEGSMCETTKRIGRVTGSDGKLYHIYVCIDGCIIIKSATRSYQRVFRWVHNRLDCPLWVTTCSDTKEEGATKKKTQKPDRLERGKMKIVPKESEKDSKTKPPDATIVVEGVKYQVRKKGKTKSKNTQDGLYHNKNKPQESRKKLEKALLAWAIIAIVLFQVTMGENITQWNLQDNGTEGIQRAMFQRGVNRSLHGIWPEKICTGVPSHLATDIELKTIHGMMDASEKTNYTCCRLQRHEWNKHGWCNWYNIEPWILVMNRTQANLTEGQPPRECAVTCRYDRASDLNVVTQARDSPTPLTGCKKGKNFSFAGILMRGPCNFEIAASDVLFKEHERISMFQDTTLYLVDGLTNSLEGARQGTAKLTTWLGKQLGILGKKLENKSKTWFGAYAASPYCDVDRKIGYIWYTKNCTPACLPKNTKIVGPGKFGTNAEDGKILHEMGGHLSEVLLLSLVVLSDFAPETASVMYLILHFSIPQSHVDVMDCDKTQLNLTVELTTAEVIPGSVWNLGKYVCIRPNWWPYETTVVLAFEEVSQVVKLVLRALRDLTRIWNAATTTAFLVCLVKIVRGQMVQGILWLLLITGVQGHLDCKPEFSYAIAKDERIGQLGAEGLTTTWKEYSPGMKLEDTMVIAWCEDGKLMYLQRCTRETRYLAILHTRALPTSVVFKKLFDGRKQEDVVEMNDNFEFGLCPCDAKPIVRGKFNTTLLNGPAFQMVCPIGWTGTVSCTSFNMDTLATTVVRTYRRSKPFPHRQGCITQKNLGEDLHNCILGGNWTCVPGDQLLYKGGSIESCKWCGYQFKESEGLPHYPIGKCKLENETGYRLVDSTSCNREGVAIVPQGTLKCKIGKTTVQVIAMDTKLGPMPCRPYEIISSEGPVEKTACTFNYTKTLKNKYFEPRDSYFQQYMLKGEYQYWFDLEVTDHHRDYFAESILVVVVALLGGRYVLWLLVTYMVLSEQKALGIQYGSGEVVMMGNLLTHNNIEVVTYFLLLYLLLREESVKKWVLLLYHILVVHPIKSVIVILLMIGDVVKADSGGQEYLGKIDLCFTTVVLIVIGLIIARRDPTIVPLVTIMAALRVTELTHQPGVDIAVAVMTITLLMVSYVTDYFRYKKWLQCILSLVSAVFLIRSLIYLGRIEMPEVTIPNWRPLTLILLYLISTTIVTRWKVDVAGLLLQCVPILLLVTTLWADFLTLILILPTYELVKLYYLKTVRTDTERSWLGGIDYTRVDSIYDVDESGEGVYLFPSRQKAQGNFSILLPLIKATLISCVSSKWQLIYMSYLTLDFMYYMHRKVIEEISGGTNIISRLVAALIELNWSMEEEESKGLKKFYLLSGRLRNLIIKHKVRNETVASWYGEEEVYGMPKIMTIIKASTLSKSRHCIICTVCEGREWKGGTCPKCGRHGKPITCGMSLADFEERHYKRIFIREGNFEGMCSRCQGKHRRFEMDREPKSARYCAECNRLHPAEEGDFWAESSMLGLKITYFALMDGKVYDITEWAGCQRVGISPDTHRVPCHISFGSRMPFRQEYNGFVQYTARGQLFLRNLPVLATKVKMLMVGNLGEEIGNLEHLGWILRGPAVCKKITEHEKCHINILDKLTAFFGIMPRGTTPRAPVRFPTSLLKVRRGLETAWAYTHQGGISSVDHVTAGKDLLVCDSMGRTRVVCQSNNRLTDETEYGVKTDSGCPDGARCYVLNPEAVNISGSKGAVVHLQKTGGEFTCVTASGTPAFFDLKNLKGWSGLPIFEASSGRVVGRVKVGKNEESKPTKIMSGIQTVSKNRADLTEMVKKITSMNRGDFKQITLATGAGKTTELPKAVIEEIGRHKRVLVLIPLRAAAESVYQYMRLKHPSISFNLRIGDMKEGDMATGITYASYGYFCQMPQPKLRAAMVEYSYIFLDEYHCATPEQLAIIGKIHRFSESIRVVAMTATPAGSVTTTGQKHPIEEFIAPEVMKGEDLGSQFLDIAGLKIPVDEMKGNMLVFVPTRNMAVEVAKKLKAKGYNSGYYYSGEDPANLRVVTSQSPYVIVATNAIESGVTLPDLDTVIDTGLKCEKRVRVSSKIPFIVTGLKRMAVTVGEQAQRRGRVGRVKPGRYYRSQETATGSKDYHYDLLQAQRYGIEDGINVTKSFREMNYDWSLYEEDSLLITQLEILNNLLISEDLPAAVKNIMARTDHPEPIQLAYNSYEVQVPVLFPKIRNGEVTDTYENYSFLNARKLGEDVPVYIYATEDEDLAVDLLGLDWPDPGNQQVVETGKALKQVTGLSSAENALLVALFGYVGYQALSKRHVPMITDIYTIEDQRLEDTTHLQYAPNAIKTDGTETELKELASGDVEKIMGAISDYAAGGLEFVKSQAEKIKTAPLFKENAEAAKGYVQKFIDSLIENKEEIIRYGLWGTHTALYKSIAARLGHETAFATLVLKWLAFGGESVSDHVKQAAVDLVVYYVMNKPSFPGDSETQQEGRRFVASLFISALATYTYKTWNYHNLSKVVEPALAYLPYATSALKMFTPTRLESVVILSTTIYKTYLSIRKGKSDGLLGTGISAAMEILSQNPVSVGISVMLGVGAIAAHNAIESSEQKRTLLMKVFVKNFLDQAATDELVKENPEKIIMALFEAVQTIGNPLRLIYHLYGVYYKGWEAKELSERTAGRNLFTLIMFEAFELLGMDSQGKIRNLSGNYILDLIYGLHKQINRGLKKMVLGWAPAPFSCDWTPSDERIRLPTDNYLRVETRCPCGYEMKAFKNVGGKLTKVEESGPFLCRNRPGRGPVNYRVTKYYDDNLREIKPVAKLEGQVEHYYKGVTAKIDYSKGKMLLATDKWEVEHGVITRLAKRYTGVGFNGAYLGDEPNHRALVERDCATITKNTVQFLKMKKGCAFTYDLTISNLTRLIELVHRNNLEEKEIPTATVTTWLAYTFVNEDVGTIKPVLGERVIPDPVVDINLQPEVQVDTSEVGITIIGRETLMTTGVTPVLEKVEPDASDNQNSVKIGLDEGNYPGPGIQTHTLTEEIHNRDARPFIMILGSRNSISNRAKTARNINLYTGNDPREIRDLMAAGRMLVVALRDVDPELSEMVDFKGTFLDREALEALSLGQPKPKQVTKEAVRNLIEQKKDVEIPNWFASDDPVFLEVALKNDKYYLVGDVGELKDQAKALGATDQTRIIKEVGSRTYAMKLSSWFLKASNKQMSLTPLFEELLLRCPPATKSNKGHMASAYQLAQGNWEPLGCGVHLGTIPARRVKIHPYEAYLKLKDFIEEEEKKPRVKDTVIREHNKWILKKIRFQGNLNTKKMLNPGKLSEQLDREGRKRNIYNHQIGTIMSSAGIRLEKLPIVRAQTDTKTFHEAIRDKIDKSENRQNPELHNKLLEIFHTIAQPTLKHTYGEVTWEQLEAGVNRKGAAGFLEKKNIGEVLDSEKHLVEQLVRDLKAGRKIKYYETAIPKNEKRDVSDDWQAGDLVVEKRPRVIQYPEAKTRLAITKVMYNWVKQQPVVIPGYEGKTPLFNIFDKVRKEWDSFNEPVAVSFDTKAWDTQVTSKDLQLIGEIQKYYYKKEWHKFIDTITDHMTEVPVITADGEVYIRNGQRGSGQPDTSAGNSMLNVLTMMYGFCESTGVPYKSFNRVARIHVCGDDGFLITEKGLGLKFANKGMQILHEAGKPQKITEGEKMKVAYRFEDIEFCSHTPVPVRWSDNTSSHMAGRDTAVILSKMATRLDSSGERGTTAYEKAVAFSFLLMYSWNPLVRRICLLVLSQQPETDPSKHATYYYKGDPIGAYKDVIGRNLSELKRTGFEKLANLNLSLSTLGVWTKHTSKRIIQDCVAIGKEEGNWLVKPDRLISSKTGHLYIPDKGFTLQGKHYEQLQLRTETNPVMGVGTERYKLGPIVNLLLRRLKILLMTAVGVSS","creator":"esalladini","dataset":["Viral proteins","RNA-binding proteins"],"date":"2016-08-23T17:53:57.000Z","disprot_id":"DP00675","features":{"pfam":[{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":2075,"end":2189},{"id":"PF00998","name":"Viral RNA dependent RNA polymerase","start":3550,"end":3774},{"id":"PF05550","name":"Pestivirus Npro endopeptidase C53","start":1,"end":168},{"id":"PF05578","name":"Pestivirus NS3 polyprotein peptidase S31","start":1680,"end":1890},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1897,"end":2037},{"id":"PF11889","name":"Capsid protein C, pestivirus","start":173,"end":228},{"id":"PF12387","name":"Pestivirus NS2 peptidase","start":1323,"end":1522},{"id":"PF14901","name":"Cleavage inducing molecular chaperone","start":1536,"end":1620},{"id":"PF16329","name":"Pestivirus envelope glycoprotein E2","start":694,"end":1065},{"id":"PF20907","name":"Flavivirus NS3 helicase, C-terminal helical domain","start":2224,"end":2365}],"gene3D":[{"start":780,"end":857,"id":"2.60.40.3000","name":"Pestivirus envelope glycoprotein E2, domain B","_id":"685af523b4ac24d5329d81bc"},{"start":933,"end":1030,"id":"3.30.1360.280","name":"Pestivirus envelope glycoprotein E2, C-terminal domain","_id":"685af523b4ac24d5329d81bd"},{"start":693,"end":779,"id":"2.60.320.20","name":"Pestivirus envelope glycoprotein E2, domain A","_id":"685af523b4ac24d5329d81be"},{"start":100,"end":156,"id":"2.30.140.40","name":"Pestivirus Npro endopeptidase C53, interaction domain","_id":"685af523b4ac24d5329d81bf"},{"start":269,"end":435,"id":"3.90.730.10","name":"Ribonuclease T2-like","_id":"685af523b4ac24d5329d81c0"},{"start":3583,"end":3637,"id":"3.30.70.270","name":"3.30.70.270","_id":"685af523b4ac24d5329d81c1"},{"start":3681,"end":3769,"id":"3.30.70.270","name":"3.30.70.270","_id":"685af523b4ac24d5329d81c2"},{"start":1892,"end":2054,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d81c3"},{"start":2055,"end":2204,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d81c4"}]},"genes":[],"length":3988,"name":"Genome polyprotein","ncbi_taxon_id":11100,"organism":"Bovine viral diarrhea virus (isolate NADL)","regions_counter":15,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Pestivirus"],"UniParc":"UPI0000174A10","uniref100":"UniRef100_P19711","uniref50":"UniRef50_P19711","uniref90":"UniRef90_P19711","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":169,"end":270,"interaction_partner":[],"reference_html":"Bovine viral diarrhea virus core is an intrinsically disordered protein that binds RNA. <i> Murray CL, Marcotrigiano J, Rice CM. </i> J Virol, 2008","reference_id":"18032507","region_id":"DP00675r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Natively unstructured proteins have a large proportion of solvent-exposed residues and are therefore highly susceptible to trace amounts of protease. Treatment of C87 or C90 with endoprotease GluC resulted in almost complete digestion within 1 minute when the core protein was present in a 10-fold excess (Fig. 2B). Similar results were seen with trypsin and chymotrypsin, and, for all three enzymes, proteolysis of C87 was complete within 1 hour even when core protein was in a 300-fold excess (data not shown). These results suggested that the majority of core residues are accessible to proteases.","_id":"685af523b4ac24d5329d81c6"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2022-03-08T15:37:33.946Z","_id":"685af523b4ac24d5329d81c7"},"version":3,"_id":"685af523b4ac24d5329d81c5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":169,"end":270,"interaction_partner":[],"reference_html":"Bovine viral diarrhea virus core is an intrinsically disordered protein that binds RNA. <i> Murray CL, Marcotrigiano J, Rice CM. </i> J Virol, 2008","reference_id":"18032507","region_id":"DP00675r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"We next used intrinsic fluorescence spectroscopy to determine the environment of tyrosine residues within the core protein. The peak emission of C90 was observed at approximately 360 nm. Since an emission maximum at a wavelength greater than 340 nm indicates a high degree of solvent exposure, this again suggested that the core protein lacked significant globular structure (Fig. 2C).","_id":"685af523b4ac24d5329d81c9"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-16T11:38:11.130Z","_id":"685af523b4ac24d5329d81ca"},"version":3,"_id":"685af523b4ac24d5329d81c8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":169,"end":270,"interaction_partner":[],"reference_html":"Bovine viral diarrhea virus core is an intrinsically disordered protein that binds RNA. <i> Murray CL, Marcotrigiano J, Rice CM. </i> J Virol, 2008","reference_id":"18032507","region_id":"DP00675r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The core protein was further analyzed for the presence of secondary structural elements by far-UV CD (reviewed in reference 19). The CD spectrum of C87 indicated a minimum at approximately 195 nm, consistent with a protein that lacks secondary structure ​(Fig. 2D). A minimum at 208 nm or 222 nm, indicative of α-helical or β-sheet secondary structures, was not observed.","_id":"685af523b4ac24d5329d81d0"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-16T11:38:01.047Z","_id":"685af523b4ac24d5329d81d1"},"version":3,"_id":"685af523b4ac24d5329d81cf","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":170,"end":260,"interaction_partner":[],"reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","reference_id":"18033802","region_id":"DP00675r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"BVDV core protein, in agreement with the disorder prediction (Figure 1), was found to be completely unstructured at 20°C, as evidenced by the pronounced minimum in the CD spectrum observed at ∼200 nm (Figure 6D).","_id":"685af523b4ac24d5329d81d3"},{"type":"Discussion","text":"BVDV core protein was found to completely lack a well-defined structure, as evidenced by its CD spectrum at 20°C and 95°C (Figure 6D).","_id":"685af523b4ac24d5329d81d4"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-16T11:37:46.942Z","_id":"685af523b4ac24d5329d81d5"},"version":3,"_id":"685af523b4ac24d5329d81d2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-08T15:38:59.063Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001807","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","ec_ontology":"ECO","start":170,"end":260,"interaction_partner":[],"reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","reference_id":"18033802","region_id":"DP00675r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"All four proteins bound both to RNA and DNA without a strict sequence specificity, and they caused complete retention of the nucleic acids at the top of the gel (indicative of the formation of large nucleoprotein complexes) at a protein-to-nucleotide molar ratio of ∼1:20 (data not shown).","_id":"685af523b4ac24d5329d81db"}],"states_connection":[],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_id":"GO:0003677","term_is_binding":true,"term_is_obsolete":false,"term_name":"DNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-23T13:56:13.399Z","_id":"685af523b4ac24d5329d81dc"},"version":2,"_id":"685af523b4ac24d5329d81da","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-08T15:38:53.032Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001807","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","ec_ontology":"ECO","start":170,"end":260,"interaction_partner":[],"reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","reference_id":"18033802","region_id":"DP00675r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"All four proteins bound both to RNA and DNA without a strict sequence specificity, and they caused complete retention of the nucleic acids at the top of the gel (indicative of the formation of large nucleoprotein complexes) at a protein-to-nucleotide molar ratio of ∼1:20 (data not shown).","_id":"685af523b4ac24d5329d81de"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_id":"GO:0003723","term_is_binding":true,"term_is_obsolete":false,"term_name":"RNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-23T13:56:11.417Z","_id":"685af523b4ac24d5329d81df"},"version":2,"_id":"685af523b4ac24d5329d81dd","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006317","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","ec_ontology":"ECO","start":170,"end":260,"interaction_partner":[],"reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","reference_id":"18033802","region_id":"DP00675r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Surprisingly, both WNV core, a protein with a well-defined 3D structure (40), and BVDV core, which was predicted to be completely unstructured (Figure 1), retained their full activity upon boiling (compare lanes 36–38 and 39–41, and 43–45 and 46–48 in Figure 4B).","_id":"685af523b4ac24d5329d81e1"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-16T11:37:30.262Z","_id":"685af523b4ac24d5329d81e2"},"version":1,"_id":"685af523b4ac24d5329d81e0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0005801","ec_name":"enzymatic activity assay evidence used in manual assertion","ec_ontology":"ECO","start":170,"end":260,"interaction_partner":[],"reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","reference_id":"18033802","region_id":"DP00675r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As expected, all core proteins induced a considerable increase in the cleavage rates, with hepacivirus core proteins demonstrating a higher activity compared to WNV and BVDV cores (Figure 4C). ","_id":"685af523b4ac24d5329d81e4"},{"type":"Discussion","text":"Despite a lack of significant similarity with hepacivirus cores in amino acid sequence or domain organization (Figure 1), core proteins of the flavivirus WNV and the pestivirus BVDV both demonstrated potent RNA chaperone activities in vitro (Figures 2 and 3).","_id":"685af523b4ac24d5329d81e5"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-16T09:00:37.027Z","_id":"685af523b4ac24d5329d81e6"},"version":1,"_id":"685af523b4ac24d5329d81e3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-08T15:38:38.470Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0007009","ec_name":"radioligand binding assay evidence used in manual assertion","ec_ontology":"ECO","start":169,"end":270,"interaction_partner":[],"reference_html":"Bovine viral diarrhea virus core is an intrinsically disordered protein that binds RNA. <i> Murray CL, Marcotrigiano J, Rice CM. </i> J Virol, 2008","reference_id":"18032507","region_id":"DP00675r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"After binding of protein and labeled RNA in solution, reaction mixtures were applied to nitrocellulose filters under vacuum and washed, and RNA retained on the filter was quantified. C87 and C90 were found to bind RNA equivalently and with approximately 1 μM affinity; a slight preference was seen for G and U homo-oligomers ​(Fig. 3 and Table 1).","_id":"685af523b4ac24d5329d81e8"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_go_domain":"F","term_id":"GO:0003723","term_is_binding":true,"term_is_obsolete":false,"term_name":"RNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-23T13:56:06.905Z","_id":"685af523b4ac24d5329d81e9"},"version":2,"_id":"685af523b4ac24d5329d81e7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IEP","ec_id":"ECO:0005648","ec_name":"luciferase reporter gene assay evidence used in manual assertion","ec_ontology":"ECO","start":169,"end":270,"interaction_partner":[],"reference_html":"Bovine viral diarrhea virus core is an intrinsically disordered protein that binds RNA. <i> Murray CL, Marcotrigiano J, Rice CM. </i> J Virol, 2008","reference_id":"18032507","region_id":"DP00675r014","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"At 24 h postelectroporation, cell culture supernatants were harvested, clarified by filtration, and used to infect naïve BHK 21 cells. The infected cells were incubated for 4 h before assay for luciferase activity. Sindbis/luc(CΔ2-96) was severely impaired in infectious virus production, while the less drastic deletions, Sindbis/luc(CΔ50-96) and Sindbis/luc(CΔ72-96), showed only moderate reductions (Fig. ​(Fig.8C).8C). In each case, the inclusion of BVDV sequences led to increased signal compared to the deletion mutants, suggesting that the BVDV residues positively influenced infectious virion production.","_id":"685af523b4ac24d5329d81eb"},{"type":"Results","text":"Taken together, these results suggest that the nonspecific RNA-binding properties of BVDV core observed in vitro are responsible for its ability to functionally replace a heterologous RNA condensation sequence in vivo, and they indicate that the BVDV core protein likely functions by a similar mechanism in packaging its own genomic RNA.","_id":"685af523b4ac24d5329d81ec"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_go_domain":"F","term_id":"GO:0003723","term_is_binding":true,"term_is_obsolete":false,"term_name":"RNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-16T11:40:34.787Z","_id":"685af523b4ac24d5329d81ed"},"version":1,"_id":"685af523b4ac24d5329d81ea","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IEP","ec_id":"ECO:0005648","ec_name":"luciferase reporter gene assay evidence used in manual assertion","ec_ontology":"ECO","start":169,"end":270,"interaction_partner":[],"reference_html":"Bovine viral diarrhea virus core is an intrinsically disordered protein that binds RNA. <i> Murray CL, Marcotrigiano J, Rice CM. </i> J Virol, 2008","reference_id":"18032507","region_id":"DP00675r015","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"At 24 h postelectroporation, cell culture supernatants were harvested, clarified by filtration, and used to infect naïve BHK 21 cells. The infected cells were incubated for 4 h before assay for luciferase activity. Sindbis/luc(CΔ2-96) was severely impaired in infectious virus production, while the less drastic deletions, Sindbis/luc(CΔ50-96) and Sindbis/luc(CΔ72-96), showed only moderate reductions (Fig. ​(Fig.8C).8C). In each case, the inclusion of BVDV sequences led to increased signal compared to the deletion mutants, suggesting that the BVDV residues positively influenced infectious virion production.","_id":"685af523b4ac24d5329d81ef"},{"type":"Results","text":"Taken together, these results suggest that the nonspecific RNA-binding properties of BVDV core observed in vitro are responsible for its ability to functionally replace a heterologous RNA condensation sequence in vivo, and they indicate that the BVDV core protein likely functions by a similar mechanism in packaging its own genomic RNA.","_id":"685af523b4ac24d5329d81f0"}],"states_connection":[],"term_comment":"","term_def":"\"The encapsulation of the viral genome within the capsid.\" [ISBN:0121585336]","term_go_domain":"P","term_id":"GO:0019072","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral genome packaging","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-16T11:41:27.161Z","_id":"685af523b4ac24d5329d81f1"},"version":1,"_id":"685af523b4ac24d5329d81ee","reference_source":"pmid"}],"__v":0,"disorder_content":0.025576730190571714,"disprot_consensus":{"full":[{"start":169,"end":270,"type":"D"}],"Structural state":[{"start":169,"end":270,"type":"D"}],"Molecular function":[{"start":169,"end":270,"type":"F"}],"Biological process":[{"start":169,"end":270,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00011","name":"Hsp20/alpha crystallin family","start":47,"end":150}],"gene3D":[{"start":1,"end":150,"id":"2.60.40.790","name":"2.60.40.790"}]},"uniref50":"UniRef50_P19036","sequence":"MSIVRRSNVFDPFADLWADPFDTFRSIVPAISGGSSETAAFANARVDWKETPEAHVFKVDLPGVKKEEVKVEVEDGNVLVVSGERSREKEDKNDKWHRVERSSGKFVRRFRLPEDAKVEEVKAGLENGVLTVTVPKAEVKKPEVKAIEISG","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","BOP clade","Pooideae","Triticodae","Triticeae","Triticinae","Triticum"],"uniref90":"UniRef90_P12810","disprot_id":"DP00677","ncbi_taxon_id":4565,"regions_counter":8,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":42,"region_id":"DP00677r001","released":"2022_03","ec_id":"ECO:0006275","reference_html":"Crystal structure and assembly of a eukaryotic small heat shock protein. <i> van Montfort RL, Basha E, Friedrich KL, Slingsby C, Vierling E. </i> Nat Struct Biol, 2001","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11702068","version":2,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":42,"term_name":"protein folding chaperone","start":1,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11702068","version":3,"reference_html":"Crystal structure and assembly of a eukaryotic small heat shock protein. <i> van Montfort RL, Basha E, Friedrich KL, Slingsby C, Vierling E. </i> Nat Struct Biol, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0044183","ec_id":"ECO:0006275","region_id":"DP00677r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":42,"term_name":"flexible C-terminal tail","start":1,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11702068","version":3,"reference_html":"Crystal structure and assembly of a eukaryotic small heat shock protein. <i> van Montfort RL, Basha E, Friedrich KL, Slingsby C, Vierling E. </i> Nat Struct Biol, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000031","ec_id":"ECO:0006275","region_id":"DP00677r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":42,"term_name":"protein binding","start":1,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11702068","version":3,"reference_html":"Crystal structure and assembly of a eukaryotic small heat shock protein. <i> van Montfort RL, Basha E, Friedrich KL, Slingsby C, Vierling E. </i> Nat Struct Biol, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006275","region_id":"DP00677r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":42,"region_id":"DP00677r005","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Crystal structure and assembly of a eukaryotic small heat shock protein. <i> van Montfort RL, Basha E, Friedrich KL, Slingsby C, Vierling E. </i> Nat Struct Biol, 2001","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11702068","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":42,"term_name":"protein folding chaperone","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11702068","version":3,"reference_html":"Crystal structure and assembly of a eukaryotic small heat shock protein. <i> van Montfort RL, Basha E, Friedrich KL, Slingsby C, Vierling E. </i> Nat Struct Biol, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0044183","ec_id":"ECO:0007680","region_id":"DP00677r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":42,"term_name":"flexible C-terminal tail","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11702068","version":3,"reference_html":"Crystal structure and assembly of a eukaryotic small heat shock protein. <i> van Montfort RL, Basha E, Friedrich KL, Slingsby C, Vierling E. </i> Nat Struct Biol, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000031","ec_id":"ECO:0007680","region_id":"DP00677r007","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":42,"term_name":"protein binding","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11702068","version":3,"reference_html":"Crystal structure and assembly of a eukaryotic small heat shock protein. <i> van Montfort RL, Basha E, Friedrich KL, Slingsby C, Vierling E. </i> Nat Struct Biol, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007680","region_id":"DP00677r008","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P12810","date":"2016-08-16T17:26:04.000Z","acc":"P12810","name":"16.9 kDa class I heat shock protein 1","length":151,"organism":"Triticum aestivum","dataset":["Stress response proteins"],"UniParc":"UPI0000044D5B","genes":[{"name":{"value":"hsp16.9A"}}],"alphafold_very_low_content":0.006622516556291391,"disorder_content":0.2781456953642384,"disprot_consensus":{"full":[{"start":1,"end":42,"type":"D"}],"Structural state":[{"start":1,"end":42,"type":"D"}],"Molecular function":[{"start":1,"end":42,"type":"F"}],"Disorder function":[{"start":1,"end":42,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00373","name":"FERM central domain","start":292,"end":401},{"id":"PF04382","name":"SAB domain","start":667,"end":715},{"id":"PF05902","name":"4.1 protein C-terminal domain (CTD)","start":753,"end":860},{"id":"PF08736","name":"FERM adjacent (FA)","start":499,"end":542},{"id":"PF09379","name":"FERM N-terminal domain","start":214,"end":276},{"id":"PF09380","name":"FERM C-terminal PH-like domain","start":406,"end":492}],"gene3D":[{"start":288,"end":395,"id":"1.20.80.10","name":"1.20.80.10"},{"start":396,"end":488,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":209,"end":287,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"}]},"uniref50":"UniRef50_P11171","sequence":"MTTEKSLVTEAENSQHQQKEEGEEAINSGQQEPQQEESCQTAAEGDNWCEQKLKASNGDTPTHEDLTKNKERTSESRGLSRLFSSFLKRPKSQVSEEEGKEVESDKEKGEGGQKEIEFGTSLDEEIILKAPIAAPEPELKTDPSLDLHSLSSAETQPAQEELREDPDFEIKEGEGLEECSKIEVKEESPQSKAETELKASQKPIRKHRNMHCKVSLLDDTVYECVVEKHAKGQDLLKRVCEHLNLLEEDYFGLAIWDNATSKTWLDSAKEIKKQVRGVPWNFTFNVKFYPPDPAQLTEDITRYYLCLQLRQDIVAGRLPCSFATLALLGSYTIQSELGDYDPELHGVDYVSDFKLAPNQTKELEEKVMELHKSYRSMTPAQADLEFLENAKKLSMYGVDLHKAKDLEGVDIILGVCSSGLLVYKDKLRINRFPWPKVLKISYKRSSFFIKIRPGEQEQYESTIGFKLPSYRAAKKLWKVCVEHHTFFRLTSTDTIPKSKFLALGSKFRYSGRTQAQTRQASALIDRPAPHFERTASKRASRSLDGAAAVDSADRSPRPTSAPAITQGQVAEGGVLDASAKKTVVPKAQKETVKAEVKKEDEPPEQAEPEPTEAWKVEKTHIEVTVPTSNGDQTQKLAEKTEDLIRMRKKKRERLDGENIYIRHSNLMLEDLDKSQEEIKKHHASISELKKNFMESVPEPRPSEWDKRLSTHSPFRTLNINGQIPTGEGPPLVKTQTVTISDNANAVKSEIPTKDVPIVHTETKTITYEAAQTDDNSGDLDPGVLLTAQTITSETPSSTTTTQITKTVKGGISETRIEKRIVITGDADIDHDQVLVQAIKEAKEQHPDMSVTKVVVHQETEIADE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P11171","disprot_id":"DP00678","ncbi_taxon_id":9606,"regions_counter":6,"creator":"ahatos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":864,"region_id":"DP00678r001","released":"2022_03","ec_id":"ECO:0006198","reference_html":"NMR characterisation of the minimal interacting regions of centrosomal proteins 4.1R and NuMA1: effect of phosphorylation. <i> Treviño MA, Rodríguez-Rodríguez M, Correas I, Marcilla M, Albar JP, Rico M, Jiménez MA, Bruix M. </i> BMC Biochem, 2010","term_id":"IDPO:0000002","curator_id":"fquaglia","start":800,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20109190","version":2,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":864,"term_name":"molecular function regulator","start":800,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"20109190","version":3,"reference_html":"NMR characterisation of the minimal interacting regions of centrosomal proteins 4.1R and NuMA1: effect of phosphorylation. <i> Treviño MA, Rodríguez-Rodríguez M, Correas I, Marcilla M, Albar JP, Rico M, Jiménez MA, Bruix M. </i> BMC Biochem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006198","region_id":"DP00678r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":864,"term_name":"protein binding","start":800,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"20109190","version":3,"reference_html":"NMR characterisation of the minimal interacting regions of centrosomal proteins 4.1R and NuMA1: effect of phosphorylation. <i> Treviño MA, Rodríguez-Rodríguez M, Correas I, Marcilla M, Albar JP, Rico M, Jiménez MA, Bruix M. </i> BMC Biochem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006198","region_id":"DP00678r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":864,"region_id":"DP00678r004","released":"2022_03","ec_id":"ECO:0006204","reference_html":"NMR characterisation of the minimal interacting regions of centrosomal proteins 4.1R and NuMA1: effect of phosphorylation. <i> Treviño MA, Rodríguez-Rodríguez M, Correas I, Marcilla M, Albar JP, Rico M, Jiménez MA, Bruix M. </i> BMC Biochem, 2010","term_id":"IDPO:0000002","curator_id":"fquaglia","start":800,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20109190","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":864,"term_name":"molecular function regulator","start":800,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"20109190","version":3,"reference_html":"NMR characterisation of the minimal interacting regions of centrosomal proteins 4.1R and NuMA1: effect of phosphorylation. <i> Treviño MA, Rodríguez-Rodríguez M, Correas I, Marcilla M, Albar JP, Rico M, Jiménez MA, Bruix M. </i> BMC Biochem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006204","region_id":"DP00678r005","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":864,"term_name":"protein binding","start":800,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"20109190","version":3,"reference_html":"NMR characterisation of the minimal interacting regions of centrosomal proteins 4.1R and NuMA1: effect of phosphorylation. <i> Treviño MA, Rodríguez-Rodríguez M, Correas I, Marcilla M, Albar JP, Rico M, Jiménez MA, Bruix M. </i> BMC Biochem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00678r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P11171","date":"2016-08-29T13:39:15.000Z","acc":"P11171","name":"Protein 4.1","length":864,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000002A2C8","genes":[{"name":{"value":"EPB41","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:3377","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:3377"}}]},"synonyms":[{"value":"E41P"}]}],"alphafold_very_low_content":0.4583333333333333,"disorder_content":0.07523148148148148,"disprot_consensus":{"full":[{"start":800,"end":864,"type":"D"}],"Structural state":[{"start":800,"end":864,"type":"D"}],"Molecular function":[{"start":800,"end":864,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00046","name":"Homeodomain","start":125,"end":181}],"gene3D":[{"start":122,"end":189,"id":"1.10.10.60","name":"Homeodomain-like"}]},"uniref50":"UniRef50_Q99801","sequence":"MLRVPEPRPGEAKAEGAAPPTPSKPLTSFLIQDILRDGAQRQGGRTSSQRQRDPEPEPEPEPEGGRSRAGAQNDQLSTGPRAAPEEAETLAETEPERHLGSYLLDSENTSGALPRLPQTPKQPQKRSRAAFSHTQVIELERKFSHQKYLSAPERAHLAKNLKLTETQVKIWFQNRRYKTKRKQLSSELGDLEKHSSLPALKEEAFSRASLVSVYNSYPYYPYLYCVGSWSPAFW","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q99801","disprot_id":"DP00683","ncbi_taxon_id":9606,"regions_counter":4,"creator":"aschramm","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":113,"region_id":"DP00683r003","released":"2022_12","ec_id":"ECO:0006204","reference_html":"Interactions of the acidic domain and SRF interacting motifs with the NKX3.1 homeodomain. <i> Ju JH, Maeng JS, Lee DY, Piszczek G, Gelmann EP, Gruschus JM. </i> Biochemistry, 2009","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19780584","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-08-26T15:22:10.807Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The CD spectra of the NKX3.1 (1–184), (75–184), (97–184), and (114–184) constructs are consistent with the homeodomain containing significant α-helical content and the N-terminal region consisting of flexible, disordered structure (Figure 1D), as already shown in previous NMR studies (6, 7).","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_Q99801","date":"2016-09-18T18:32:27.000Z","acc":"Q99801","name":"Homeobox protein Nkx-3.1","length":234,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000016B256","genes":[{"name":{"value":"NKX3-1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:7838","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:7838"}}]},"synonyms":[{"value":"NKX3.1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9226374","url":"http://www.ncbi.nlm.nih.gov/pubmed/9226374","alternativeUrl":"https://europepmc.org/abstract/MED/9226374"}}]},{"value":"NKX3A","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11137288","url":"http://www.ncbi.nlm.nih.gov/pubmed/11137288","alternativeUrl":"https://europepmc.org/abstract/MED/11137288"}}]}]}],"alphafold_very_low_content":0.29914529914529914,"disorder_content":0.4829059829059829,"disprot_consensus":{"full":[{"start":1,"end":113,"type":"D"}],"Structural state":[{"start":1,"end":113,"type":"D"}]}},{"acc":"Q98157","sequence":"MDTKGILLVAVLTALLCLQSGDTLGASWHRPDKCCLGYQKRPLPQVLLSSWYPTSQLCSKPGVIFLTKRGRQVCADKSKDWVKKLMQQLPVTAR","creator":"agasparini","dataset":["Viral proteins"],"date":"2016-08-24T15:10:03.000Z","disprot_id":"DP00685","features":{"pfam":[{"id":"PF00048","name":"Small cytokines (intecrine/chemokine), interleukin-8 like","start":33,"end":89}],"gene3D":[{"start":24,"end":94,"id":"2.40.50.40","name":"2.40.50.40","_id":"685af523b4ac24d5329d81f3"}]},"genes":[{"name":{"value":"ORF K4","evidences":[],"_id":"685af523b4ac24d5329d8263"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d8262"}],"length":94,"name":"Viral macrophage inflammatory protein 2","ncbi_taxon_id":868565,"organism":"Human herpesvirus 8 type P (isolate GK18)","regions_counter":32,"released":"2016_10","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Peploviricota","Herviviricetes","Herpesvirales","Herpesviridae","Gammaherpesvirinae","Rhadinovirus"],"UniParc":"UPI00001389A3","uniref100":"UniRef100_Q98157","uniref50":"UniRef50_Q98157","uniref90":"UniRef90_Q98157","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1CM9","_id":"685af523b4ac24d5329d823f"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":21,"end":34,"interaction_partner":[],"reference_html":"Comparison of the structure of vMIP-II with eotaxin-1, RANTES, and MCP-3 suggests a unique mechanism for CCR3 activation. <i> Fernandez EJ, Wilken J, Thompson DA, Peiper SC, Lolis E. </i> Biochemistry, 2000","reference_id":"11041848","region_id":"DP00685r026","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Residues 1−13 in the NMR structure are highly disordered; the subsequent residues (14−19) adopt a different conformation as compared to the crystal structure of vMIP-II.","_id":"685af523b4ac24d5329d823d"},{"type":"Curator statement","text":"Since the peptide used in this publication corresponds to residues 21−94 of vMIP-II,  the region the authors are describing is 21-34.","_id":"685af523b4ac24d5329d823e"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T09:53:50.925Z","_id":"685af523b4ac24d5329d8240"},"version":1,"_id":"685af523b4ac24d5329d823c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006309","ec_name":"competitive binding evidence used in manual assertion","ec_ontology":"ECO","start":21,"end":32,"interaction_partner":[{"db":"UniProt","id":"P61073","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8242"}],"reference_html":"Structure/function of human herpesvirus-8 MIP-II (1-71) and the antagonist N-terminal segment (1-10). <i> Crump MP, Elisseeva E, Gong J, Clark-Lewis I, Sykes BD. </i> FEBS Lett, 2001","reference_id":"11165244","region_id":"DP00685r027","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"However, the binding of vMIP-II(1–11)dimer is only 180-fold less than SDF-1 and is the most tightly binding small peptide that we have observed to date.","_id":"685af523b4ac24d5329d8243"},{"type":"Abstract","text":"Two N-terminal peptides, vMIP-II(1–10) and vMIP-II(1–11)dimer (dimerised through Cys11) were synthesised. Both peptides are shown to bind the CXC chemokine receptor 4 (CXCR4). vMIP-II(1–10) was 1400-fold less potent than the native protein whilst the vMIP-II(1–11)dimer was only 180-fold less potent.","_id":"685af523b4ac24d5329d8244"},{"type":"Curator statement","text":"Since the peptide used in this publication corresponds to residues 21−94 of vMIP-II, the region the authors refered as 1-11 are the residues 21-32 of the Uniprot.","_id":"685af523b4ac24d5329d8245"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T09:53:57.480Z","_id":"685af523b4ac24d5329d8246"},"version":1,"_id":"685af523b4ac24d5329d8241","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1HHV","_id":"685af523b4ac24d5329d8258"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":21,"end":34,"interaction_partner":[],"reference_html":"CCR2 and CCR5 receptor-binding properties of herpesvirus-8 vMIP-II based on sequence analysis and its solution structure. <i> Shao W, Fernandez E, Sachpatzidis A, Wilken J, Thompson DA, Schweitzer BI, Lolis E. </i> Eur J Biochem, 2001","reference_id":"11358512","region_id":"DP00685r031","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"No long-range or medium-range NOEs were observed for the N-terminal residues 1–13 or the last two C-terminal residues.","_id":"685af523b4ac24d5329d8259"},{"type":"Results","text":"The N-terminus (residues 1–13) is disordered up to the first cysteine (Cys14).","_id":"685af523b4ac24d5329d825a"},{"type":"Curator statement","text":"Since the peptide used in this publication corresponds to residues 21−94 of vMIP-II, the region the authors are describing as disordered is 21-34.","_id":"685af523b4ac24d5329d825b"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T09:53:49.075Z","_id":"685af523b4ac24d5329d825c"},"version":1,"_id":"685af523b4ac24d5329d8257","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1VMP","_id":"685af523b4ac24d5329d825e"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":21,"end":34,"interaction_partner":[],"reference_html":"The solution structure of the anti-HIV chemokine vMIP-II. <i> Liwang AC, Wang ZX, Sun Y, Peiper SC, Liwang PJ. </i> Protein Sci, 1999","reference_id":"10595530","region_id":"DP00685r032","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The structure of vMIP-II, shown in Figures 2A and 2B, consists of a disordered N-terminal region having a substantial number of sequential NOE contacts beginning at residue Trp8, but having no long-range NOE contacts until Cys14, with these due largely to the participation of both Cys14 and Cys15 in disulfide bonds (to Cys38 and Cys54, respectively)","_id":"685af523b4ac24d5329d825f"},{"type":"Curator statement","text":"Since the peptide used in this publication corresponds to residues 21−94 of vMIP-II, the region the authors are describing as disordered is 21-34.","_id":"685af523b4ac24d5329d8260"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T09:53:47.041Z","_id":"685af523b4ac24d5329d8261"},"version":1,"_id":"685af523b4ac24d5329d825d","reference_source":"pmid"}],"__v":0,"disorder_content":0.14893617021276595,"disprot_consensus":{"full":[{"start":21,"end":34,"type":"D"}],"Structural state":[{"start":21,"end":34,"type":"D"}],"Molecular function":[{"start":21,"end":32,"type":"F"}]}},{"acc":"Q9IH62","sequence":"MPAENKKVRFENTTSDKGKIPSKVIKSYYGTMDIKKINEGLLDSKILSAFNTVIALLGSIVIIVMNIMIIQNYTRSTDNQAVIKDALQGIQQQIKGLADKIGTEIGPKVSLIDTSSTITIPANIGLLGSKISQSTASINENVNEKCKFTLPPLKIHECNISCPNPLPFREYRPQTEGVSNLVGLPNNICLQKTSNQILKPKLISYTLPVVGQSGTCITDPLLAMDEGYFAYSHLERIGSCSRGVSKQRIIGVGEVLDRGDEVPSLFMTNVWTPPNPNTVYHCSAVYNNEFYYVLCAVSTVGDPILNSTYWSGSLMMTRLAVKPKSNGGGYNQHQLALRSIEKGRYDKVMPYGPSGIKQGDTLYFPAVGFLVRTEFKYNDSNCPITKCQYSKPENCRLSMGIRPNSHYILRSGLLKYNLSDGENPKVVFIEISDQRLSIGSPSKIYDSLGQPVFYQASFSWDTMIKFGDVLTVNPLVVNWRNNTVISRPGQSQCPRFNTCPEICWEGVYNDAFLIDRINWISAGVFLDSNQTAENPVFTVFKDNEILYRAQLASEDTNAQKTITNCFLLKNKIWCISLVEIYDTGDNVIRPKLFAVKIPEQCT","creator":"fquaglia","dataset":["Viral proteins"],"date":"2016-08-16T17:32:56.000Z","disprot_id":"DP00686","features":{"pfam":[{"id":"PF00423","name":"Haemagglutinin-neuraminidase","start":48,"end":598}],"gene3D":[{"start":185,"end":602,"id":"2.120.10.10","name":"2.120.10.10","_id":"685af523b4ac24d5329d8265"}]},"genes":[{"name":{"value":"G","evidences":[],"_id":"685af523b4ac24d5329d828f"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d828e"}],"length":602,"name":"Glycoprotein G","ncbi_taxon_id":121791,"organism":"Nipah virus","regions_counter":13,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Paramyxoviridae","Orthoparamyxovirinae","Henipavirus"],"UniParc":"UPI00000EED49","uniref100":"UniRef100_Q9IH62","uniref50":"UniRef50_Q9IH62","uniref90":"UniRef90_Q9IH62","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2VWD","_id":"685af523b4ac24d5329d8281"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006222","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","ec_ontology":"ECO","start":579,"end":590,"interaction_partner":[],"reference_html":"Crystal structure and carbohydrate analysis of Nipah virus attachment glycoprotein: a template for antiviral and vaccine design. <i> Bowden TA, Crispin M, Harvey DJ, Aricescu AR, Grimes JM, Jones EY, Stuart DI. </i> J Virol, 2008","reference_id":"18815311","region_id":"DP00686r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In the unbound form of NiV-G, the 579-590 loop is relatively flexible in both molecules of the crystallographic asymmetric unit, and 2Fo-Fc electron density for the side chains is poor.","_id":"685af523b4ac24d5329d8282"},{"type":"Results","text":"In addition, the 579-590 and 236-245 loops exhibit high B-factor values in the apo form (Fig. 1B and C).","_id":"685af523b4ac24d5329d8283"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T09:31:44.343Z","_id":"685af523b4ac24d5329d8284"},"version":1,"_id":"685af523b4ac24d5329d8280","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2VWD","_id":"685af523b4ac24d5329d8286"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006222","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","ec_ontology":"ECO","start":236,"end":245,"interaction_partner":[],"reference_html":"Crystal structure and carbohydrate analysis of Nipah virus attachment glycoprotein: a template for antiviral and vaccine design. <i> Bowden TA, Crispin M, Harvey DJ, Aricescu AR, Grimes JM, Jones EY, Stuart DI. </i> J Virol, 2008","reference_id":"18815311","region_id":"DP00686r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In addition, the 236-245 loop is rather disordered in the unbound structure.\" Results \"In addition, the 579-590 and 236-245 loops exhibit high B-factor values in the apo form (Fig. 1B and C).","_id":"685af523b4ac24d5329d8287"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T09:31:42.847Z","_id":"685af523b4ac24d5329d8288"},"version":1,"_id":"685af523b4ac24d5329d8285","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":579,"end":590,"interaction_partner":[{"db":"UniProt","id":"P52799","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d828c"}],"reference_html":"Crystal structure and carbohydrate analysis of Nipah virus attachment glycoprotein: a template for antiviral and vaccine design. <i> Bowden TA, Crispin M, Harvey DJ, Aricescu AR, Grimes JM, Jones EY, Stuart DI. </i> J Virol, 2008","reference_id":"18815311","region_id":"DP00686r013","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Structural differences are particularly pronounced in the 579-590 loop, a major component of the ephrin binding surface.","_id":"685af523b4ac24d5329d828a"},{"type":"Results","text":"Both molecules in the crystallographic asymmetric unit of apo-NiV-G show structural differences from the EFNB2-bound form in the region of the 579-590 loop.","_id":"685af523b4ac24d5329d828b"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T09:31:47.052Z","_id":"685af523b4ac24d5329d828d"},"version":1,"_id":"685af523b4ac24d5329d8289","reference_source":"pmid"}],"__v":0,"disorder_content":0.036544850498338874,"disprot_consensus":{"full":[{"start":236,"end":245,"type":"D"},{"start":579,"end":590,"type":"D"}],"Structural state":[{"start":236,"end":245,"type":"D"},{"start":579,"end":590,"type":"D"}],"Molecular function":[{"start":579,"end":590,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00355","name":"Rieske [2Fe-2S] domain","start":147,"end":200},{"id":"PF02921","name":"Ubiquinol cytochrome reductase transmembrane region","start":32,"end":87}],"gene3D":[{"start":31,"end":85,"id":"1.20.5.270","name":"Ubiquinol cytochrome reductase, transmembrane domain"},{"start":86,"end":215,"id":"2.102.10.10","name":"Rieske [2Fe-2S] iron-sulphur domain"}]},"uniref50":"UniRef50_P08067","sequence":"MLGIRSSVKTCFKPMSLTSKRLISQSLLASKSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAGAKSTVETFISSMTATADVLAMAKVEVNLAAIPLGKNVVVKWQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDPQWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGRIRKGPAPLNLEIPAYEFDGDKVIVG","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P08067","disprot_id":"DP00687","ncbi_taxon_id":559292,"regions_counter":1,"creator":"droche","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":92,"region_id":"DP00687r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Changes to the length of the flexible linker region of the Rieske protein impair the interaction of ubiquinol with the cytochrome bc1 complex. <i> Nett JH, Hunte C, Trumpower BL. </i> Eur J Biochem, 2000","term_id":"IDPO:0000002","curator_id":"droche","start":81,"term_ontology":"IDPO","curator_name":"Daniel Roche","reference_id":"10971589","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1EZV"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P08067","date":"2016-09-12T18:03:49.000Z","acc":"P08067","name":"Cytochrome b-c1 complex subunit Rieske, mitochondrial","length":215,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000137A75","genes":[{"name":{"value":"RIP1"},"olnNames":[{"value":"YEL024W"}]}],"alphafold_very_low_content":0.09302325581395349,"disorder_content":0.05581395348837209,"disprot_consensus":{"full":[{"start":81,"end":92,"type":"D"}],"Structural state":[{"start":81,"end":92,"type":"D"}]}},{"acc":"P30185","sequence":"MASYQNRPGGQATDEYGNPIQQQYDEYGNPMGGGGYGTGGGGGATGGQGYGTGGQGYGSGGQGYGTGGQGYGTGTGTEGFGTGGGARHHGQEQLHKESGGGLGGMLHRSGSGSSSSSEDDGQGGRRKKGITQKIKEKLPGHHDQSGQAQAMGGMGSGYDAGGYGGEHHEKKGMMDKIKEKLPGGGR","alphafold_very_low_content":"0.5645161290322581","creator":"esalladini","dataset":["Stress response proteins"],"date":"2016-09-13T13:32:23.000Z","disprot_id":"DP00689","features":{"pfam":[{"id":"PF00257","name":"Dehydrin","start":22,"end":184}]},"genes":[{"name":{"value":"RAB18","evidences":[],"_id":"685af523b4ac24d5329d82aa"},"synonyms":[],"olnNames":[{"value":"At5g66400","evidences":[],"_id":"685af523b4ac24d5329d82ac"}],"orfNames":[{"value":"K1F13.5","evidences":[],"_id":"685af523b4ac24d5329d82ab"}],"_id":"685af523b4ac24d5329d82a9"}],"length":186,"name":"Dehydrin Rab18","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions_counter":7,"released":"2016_10","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"UniParc":"UPI0000000D48","uniref100":"UniRef100_P30185","uniref50":"UniRef50_P30185","uniref90":"UniRef90_P30185","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2024-04-09T13:15:10.198Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":186,"interaction_partner":[],"reference_html":"Structural investigation of disordered stress proteins. Comparison of full-length dehydrins with isolated peptides of their conserved segments. <i> Mouillon JM, Gustafsson P, Harryson P. </i> Plant Physiol, 2006","reference_id":"16565295","region_id":"DP00689r001","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"In physiological buffer at 4C, the circular dichroism (CD) spectra of all four full-length dehydrins display large minima around 200 nm and an ellipticity near zero around 220 nm, indicative of poorly structured conformations with low content of secondary structure (Fig. 2A).","_id":"685af523b4ac24d5329d8292"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2024-04-30T14:17:34.545Z","_id":"685af523b4ac24d5329d8293"},"version":3,"_id":"685af523b4ac24d5329d8291","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2024-04-09T13:02:15.318Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":186,"interaction_partner":[],"reference_html":"Purification of recombinant Arabidopsis thaliana dehydrins by metal ion affinity chromatography. <i> Svensson J, Palva ET, Welin B. </i> Protein Expr Purif, 2000","reference_id":"11049741","region_id":"DP00689r003","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"We conclude that the dehydrins analyzed in this study have an extended structure.","_id":"685af523b4ac24d5329d8297"},{"type":"Curator statement","text":"In Table 3 is possible to appreciate a difference between the calculated Molecular Weight (18,333 Da) and the one measured from the SDS-PAGE (25 KDa).","_id":"685af523b4ac24d5329d8298"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2024-04-30T14:17:42.100Z","_id":"685af523b4ac24d5329d8299"},"version":3,"_id":"685af523b4ac24d5329d8296","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2024-04-08T15:34:22.711Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":186,"interaction_partner":[],"reference_html":"Purification of recombinant Arabidopsis thaliana dehydrins by metal ion affinity chromatography. <i> Svensson J, Palva ET, Welin B. </i> Protein Expr Purif, 2000","reference_id":"11049741","region_id":"DP00689r005","released":"2024_06","sample":[{"db":"ChEBI","deviation":null,"entry_name":"urea","id":"16199","statements":[{"type":"Methods","text":"Analytical gel filtration was made on a Superose 12 column with the dimensions 3.2 3 300 mm in phosphate-buffered saline (PBS) (8 mM NaH2PO4, 1.4 mM KH2PO4, pH 7.3, 137 mM NaCl, 2.7 mM KCl) and in 20 mM NaH2PO4, pH 6.0, 8 M urea.","_id":"685af523b4ac24d5329d829e"}],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":8000,"_id":"685af523b4ac24d5329d829d"}],"statement":[{"type":"Results","text":"The elution volume (Ve) values under denaturing conditions were slightly lower as compared to the Ve values from native conditions (Table 3), indicating that dehydrins are not globular proteins and have an extended fibrous structure, which thereby gives rise to the anomalous elution behavior in gel filtration.","_id":"685af523b4ac24d5329d829f"},{"type":"Results","text":"We conclude that the dehydrins analyzed in this study have an extended structure.","_id":"685af523b4ac24d5329d82a0"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2024-04-30T14:17:38.976Z","_id":"685af523b4ac24d5329d82a1"},"version":3,"_id":"685af523b4ac24d5329d829c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2024-04-09T13:07:44.270Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006082","ec_name":"affinity chromatography evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":186,"interaction_partner":[{"db":"ChEBI","id":"49786","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d82a5"},{"db":"ChEBI","id":"29036","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d82a6"}],"reference_html":"Purification of recombinant Arabidopsis thaliana dehydrins by metal ion affinity chromatography. <i> Svensson J, Palva ET, Welin B. </i> Protein Expr Purif, 2000","reference_id":"11049741","region_id":"DP00689r007","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"We show that four A. thaliana dehydrins bind strongly to a Cu(II)- or Ni(II)-charged IDA–Sepharose column.","_id":"685af523b4ac24d5329d82a7"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","term_id":"GO:0046872","term_is_obsolete":false,"term_name":"metal ion binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2024-04-30T14:17:33.943Z","_id":"685af523b4ac24d5329d82a8"},"version":0,"_id":"685af523b4ac24d5329d82a4","reference_source":"pmid"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":186,"type":"D"}],"Structural state":[{"start":1,"end":186,"type":"D"}],"Molecular function":[{"start":1,"end":186,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02948","name":"Amelogenin","start":21,"end":189}]},"uniref50":"UniRef50_Q99217","sequence":"MGTWILFACLLGAAFSMPLPPHPGHPGYINFSYEVLTPLKWYQNMIRHPYTSYGYEPMGGWLHHQIIPVVSQQTPQSHALQPHHHIPMVPAQQPGIPQQPMMPLPGQHSMTPTQHHQPNLPLPAQQPFQPQPVQPQPHQPLQPQSPMHPIQPLLPQPPLPPMFSMQSLLPDLPLEAWPATDKTKREEVD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Suina","Suidae","Sus"],"uniref90":"UniRef90_P45561","disprot_id":"DP00693","ncbi_taxon_id":9823,"regions_counter":6,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":173,"region_id":"DP00693r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form. <i> Delak K, Harcup C, Lakshminarayanan R, Sun Z, Fan Y, Moradian-Oldak J, Evans JS. </i> Biochemistry, 2009","term_id":"IDPO:0000002","curator_id":"mnecci","start":2,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"19236004","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":173,"term_name":"protein binding","start":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"19236004","version":3,"reference_html":"The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form. <i> Delak K, Harcup C, Lakshminarayanan R, Sun Z, Fan Y, Moradian-Oldak J, Evans JS. </i> Biochemistry, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00693r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":173,"region_id":"DP00693r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form. <i> Delak K, Harcup C, Lakshminarayanan R, Sun Z, Fan Y, Moradian-Oldak J, Evans JS. </i> Biochemistry, 2009","term_id":"IDPO:0000002","curator_id":"mnecci","start":2,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"19236004","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":173,"term_name":"protein binding","start":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"19236004","version":3,"reference_html":"The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form. <i> Delak K, Harcup C, Lakshminarayanan R, Sun Z, Fan Y, Moradian-Oldak J, Evans JS. </i> Biochemistry, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00693r004","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":28,"region_id":"DP00693r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solid-state NMR studies of proteins immobilized on inorganic surfaces. <i> Shaw WJ. </i> Solid State Nucl Magn Reson, 2015","term_id":"IDPO:0000002","curator_id":"mnecci","start":12,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"25466354","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":28,"term_name":"entropic chain","start":12,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"25466354","version":3,"reference_html":"Solid-state NMR studies of proteins immobilized on inorganic surfaces. <i> Shaw WJ. </i> Solid State Nucl Magn Reson, 2015","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0006165","region_id":"DP00693r006","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_P45561","date":"2016-09-12T16:24:57.000Z","acc":"P45561","name":"Amelogenin","length":189,"organism":"Sus scrofa","dataset":[],"UniParc":"UPI0000125968","genes":[{"name":{"value":"AMEL"}}],"alphafold_very_low_content":0.3333333333333333,"disorder_content":0.91005291005291,"disprot_consensus":{"full":[{"start":2,"end":173,"type":"D"}],"Structural state":[{"start":2,"end":173,"type":"D"}],"Molecular function":[{"start":2,"end":173,"type":"F"}],"Disorder function":[{"start":12,"end":28,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00641","name":"Zn-finger in Ran binding protein and others","start":22,"end":45},{"id":"PF17219","name":"Yaf2/RYBP C-terminal binding motif","start":145,"end":177}],"gene3D":[{"start":14,"end":55,"id":"4.10.1060.10","name":"Zinc finger, RanBP2-type"}]},"uniref50":"UniRef50_Q8N488","sequence":"MTMGDKKSPTRPKRQAKPAADEGFWDCSVCTFRNSAEAFKCSICDVRKGTSTRKPRINSQLVAQQVAQQYATPPPPKKEKKEKVEKQDKEKPEKDKEISPSVTKKNTNKKTKPKSDILKDPPSEANSIQSANATTKTSETNHTSRPRLKNVDRSTAQQLAVTVGNVTVIITDFKEKTRSSSTSSSTVTSSAGSEQQNQSSSGSESTDKGSSRSSTPKGDMSAVNDESF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q8N488","disprot_id":"DP00694","ncbi_taxon_id":9606,"regions_counter":12,"creator":"sventura","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":228,"region_id":"DP00694r001","released":"2022_03","ec_id":"ECO:0006198","reference_html":"The transcriptional repressor RYBP is a natively unfolded protein which folds upon binding to DNA. <i> Neira JL, Román-Trufero M, Contreras LM, Prieto J, Singh G, Barrera FN, Renart ML, Vidal M. </i> Biochemistry, 2009","term_id":"IDPO:0000002","curator_id":"sventura","start":1,"term_ontology":"IDPO","curator_name":"Salvador Ventura","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19170609","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":228,"term_name":"disorder to order","released":"2022_03","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","reference_html":"The transcriptional repressor RYBP is a natively unfolded protein which folds upon binding to DNA. <i> Neira JL, Román-Trufero M, Contreras LM, Prieto J, Singh G, Barrera FN, Renart ML, Vidal M. </i> Biochemistry, 2009","term_id":"IDPO:0000011","curator_id":"sventura","start":1,"term_ontology":"IDPO","curator_name":"Salvador Ventura","reference_id":"19170609","version":2,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006198","region_id":"DP00694r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":228,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","reference_html":"The transcriptional repressor RYBP is a natively unfolded protein which folds upon binding to DNA. <i> Neira JL, Román-Trufero M, Contreras LM, Prieto J, Singh G, Barrera FN, Renart ML, Vidal M. </i> Biochemistry, 2009","term_id":"GO:0003676","curator_id":"sventura","start":1,"term_ontology":"GO","curator_name":"Salvador Ventura","reference_id":"19170609","version":3,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006198","region_id":"DP00694r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":228,"term_name":"protein binding","released":"2022_03","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","reference_html":"The transcriptional repressor RYBP is a natively unfolded protein which folds upon binding to DNA. <i> Neira JL, Román-Trufero M, Contreras LM, Prieto J, Singh G, Barrera FN, Renart ML, Vidal M. </i> Biochemistry, 2009","term_id":"GO:0005515","curator_id":"sventura","start":1,"term_ontology":"GO","curator_name":"Salvador Ventura","reference_id":"19170609","version":3,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006198","region_id":"DP00694r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":228,"region_id":"DP00694r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The transcriptional repressor RYBP is a natively unfolded protein which folds upon binding to DNA. <i> Neira JL, Román-Trufero M, Contreras LM, Prieto J, Singh G, Barrera FN, Renart ML, Vidal M. </i> Biochemistry, 2009","term_id":"IDPO:0000002","curator_id":"sventura","start":1,"term_ontology":"IDPO","curator_name":"Salvador Ventura","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19170609","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":228,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"The transcriptional repressor RYBP is a natively unfolded protein which folds upon binding to DNA. <i> Neira JL, Román-Trufero M, Contreras LM, Prieto J, Singh G, Barrera FN, Renart ML, Vidal M. </i> Biochemistry, 2009","term_id":"IDPO:0000011","curator_id":"sventura","start":1,"term_ontology":"IDPO","curator_name":"Salvador Ventura","reference_id":"19170609","version":2,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00694r006","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":228,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"The transcriptional repressor RYBP is a natively unfolded protein which folds upon binding to DNA. <i> Neira JL, Román-Trufero M, Contreras LM, Prieto J, Singh G, Barrera FN, Renart ML, Vidal M. </i> Biochemistry, 2009","term_id":"GO:0003676","curator_id":"sventura","start":1,"term_ontology":"GO","curator_name":"Salvador Ventura","reference_id":"19170609","version":3,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00694r007","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":228,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"The transcriptional repressor RYBP is a natively unfolded protein which folds upon binding to DNA. <i> Neira JL, Román-Trufero M, Contreras LM, Prieto J, Singh G, Barrera FN, Renart ML, Vidal M. </i> Biochemistry, 2009","term_id":"GO:0005515","curator_id":"sventura","start":1,"term_ontology":"GO","curator_name":"Salvador Ventura","reference_id":"19170609","version":3,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00694r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":179,"region_id":"DP00694r009","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Polycomb group targeting through different binding partners of RING1B C-terminal domain. <i> Wang R, Taylor AB, Leal BZ, Chadwell LV, Ilangovan U, Robinson AK, Schirf V, Hart PJ, Lafer EM, Demeler B, Hinck AP, McEwen DG, Kim CA. </i> Structure, 2010","term_id":"IDPO:0000002","curator_id":"sventura","start":145,"term_ontology":"IDPO","curator_name":"Salvador Ventura","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3IXS"}],"reference_id":"20696397","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":179,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Polycomb group targeting through different binding partners of RING1B C-terminal domain. <i> Wang R, Taylor AB, Leal BZ, Chadwell LV, Ilangovan U, Robinson AK, Schirf V, Hart PJ, Lafer EM, Demeler B, Hinck AP, McEwen DG, Kim CA. </i> Structure, 2010","term_id":"IDPO:0000011","curator_id":"sventura","start":145,"term_ontology":"IDPO","curator_name":"Salvador Ventura","reference_id":"20696397","version":2,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00694r010","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":179,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Polycomb group targeting through different binding partners of RING1B C-terminal domain. <i> Wang R, Taylor AB, Leal BZ, Chadwell LV, Ilangovan U, Robinson AK, Schirf V, Hart PJ, Lafer EM, Demeler B, Hinck AP, McEwen DG, Kim CA. </i> Structure, 2010","term_id":"GO:0005515","curator_id":"sventura","start":145,"term_ontology":"GO","curator_name":"Salvador Ventura","reference_id":"20696397","version":3,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00694r011","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":179,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Polycomb group targeting through different binding partners of RING1B C-terminal domain. <i> Wang R, Taylor AB, Leal BZ, Chadwell LV, Ilangovan U, Robinson AK, Schirf V, Hart PJ, Lafer EM, Demeler B, Hinck AP, McEwen DG, Kim CA. </i> Structure, 2010","term_id":"GO:0003676","curator_id":"sventura","start":145,"term_ontology":"GO","curator_name":"Salvador Ventura","reference_id":"20696397","version":3,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00694r012","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q8N488","date":"2016-09-18T22:42:56.000Z","acc":"Q8N488","name":"RING1 and YY1-binding protein","length":228,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000723EC","genes":[{"name":{"value":"RYBP"},"synonyms":[{"value":"DEDAF"},{"value":"YEAF1"}]}],"alphafold_very_low_content":0.09649122807017543,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":228,"type":"T"}],"Structural state":[{"start":1,"end":228,"type":"D"}],"Structural transition":[{"start":1,"end":228,"type":"T"}],"Molecular function":[{"start":1,"end":228,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00048","name":"Small cytokines (intecrine/chemokine), interleukin-8 like","start":32,"end":87}],"gene3D":[{"start":24,"end":94,"id":"2.40.50.40","name":"2.40.50.40"}]},"uniref50":"UniRef50_Q9Y258","sequence":"MMGLSLASAVLLASLLSLHLGTATRGSDISKTCCFQYSHKPLPWTWVRSYEFTSNSCSQRAVIFTTKRGKKVCTHPRKKWVQKYISLLKTPKQL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9Y258","disprot_id":"DP00696","ncbi_taxon_id":9606,"regions_counter":2,"creator":"ktsirigos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":94,"region_id":"DP00696r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR solution structure and backbone dynamics of the CC chemokine eotaxin-3. <i> Ye J, Mayer KL, Mayer MR, Stone MJ. </i> Biochemistry, 2001","statement":[{"text":"The N- and C-termini are highly flexible, as observed for all other chemokines and in line with the high rmsd values in this region of the structure.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":84,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11425309","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1G2T"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q9Y258","date":"2016-09-13T12:42:39.000Z","acc":"Q9Y258","name":"C-C motif chemokine 26","length":94,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000049E0A","genes":[{"name":{"value":"CCL26","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:10625","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:10625"}}]},"synonyms":[{"value":"SCYA26","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10373330","url":"http://www.ncbi.nlm.nih.gov/pubmed/10373330","alternativeUrl":"https://europepmc.org/abstract/MED/10373330"}}]}],"orfNames":[{"value":"UNQ216/PRO242","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12975309","url":"http://www.ncbi.nlm.nih.gov/pubmed/12975309","alternativeUrl":"https://europepmc.org/abstract/MED/12975309"}}]}]}],"alphafold_very_low_content":0.02127659574468085,"disorder_content":0.11702127659574468,"disprot_consensus":{"full":[{"start":84,"end":94,"type":"D"}],"Structural state":[{"start":84,"end":94,"type":"D"}]}},{"acc":"Q9IK92","sequence":"MSDIFEEAASFRSYQSKLGRDGRASAATATLTTKIRIFVPATNSPELRWELTLFALDVIRSPSAAESMKVGAAFTLISMYSERPGALIRSLLNDPDIEAVIIDVGSMVNGIPVMERRGDKAQEEMEGLMRILKTARDSSKGKTPFVDSRAYGLRITDMSTLVSAVITIEAQIWILIAKAVTAPDTAEESETRRWAKYVQQKRVNPFFALTQQWLTEMRNLLSQSLSVRKFMVEILIEVKKGGSAKGRAVEIISDIGNYVEETGMAGFFATIRFGLETRYPALALNEFQSDLNTIKSLMLLYREIGPRAPYMVLLEESIQTKFAPGGYPLLWSFAMGVATTIDRSMGALNINRGYLEPMYFRLGQKSARHHAGGIDQNMANRLGLSSDQVAELAAAVQETSAGRQESNVQAREAKFAAGGVLIGGSDQDIDEGEEPIEQSGRQSVTFKREMSISSLANSVPSSSVSTSGGTRLTNSLLNLRSRLAAKAAKEAASSNATDDPAISNRTQGESEKKNNQDLKPAQNDLDFVRADV","creator":"vnugnes","dataset":["Viral proteins","RNA-binding proteins"],"date":"2016-09-02T18:07:58.000Z","disprot_id":"DP00697","features":{"pfam":[{"id":"PF00973","name":"Paramyxovirus nucleocapsid protein","start":1,"end":399}]},"genes":[{"name":{"value":"N","evidences":[],"_id":"685af523b4ac24d5329d8351"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d8350"}],"length":532,"name":"Nucleoprotein","ncbi_taxon_id":121791,"organism":"Nipah virus","regions_counter":59,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Paramyxoviridae","Orthoparamyxovirinae","Henipavirus"],"UniParc":"UPI00000F1F60","uniref100":"UniRef100_Q9IK92","uniref50":"UniRef50_Q9IK92","uniref90":"UniRef90_Q9IK92","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00697r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In order to assess the extent of protease sensitivity, we submitted Henipavirus PNT and NTAIL to digestion by thermolysin. As shown in Fig. 4, all the proteins are readily degraded by thermolysin after one hour incubation, a behavior that is consistent with the lack of a packed core and with an overall solvent accessibility of Henipavirus PNT and NTAIL.","_id":"685af523b4ac24d5329d82b8"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T07:53:42.326Z","_id":"685af523b4ac24d5329d82b9"},"version":5,"_id":"685af523b4ac24d5329d82b7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00697r017","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"This abnormal behavior is therefore likely to be ascribed to a rather high content of acidic residues, as already been observed in the case of the intrinsically disordered MeV PNT [18] and NTAIL domains [6], [19], and, more generally, in other IDPs [46].","_id":"685af523b4ac24d5329d82d1"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T07:43:22.332Z","_id":"685af523b4ac24d5329d82d2"},"version":4,"_id":"685af523b4ac24d5329d82d0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. <i> Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. </i> J Biol Chem, 2011","reference_id":"21317293","region_id":"DP00697r021","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"On the other hand, no fragment corresponding to the remaining NTAIL domain was detected, indicating that it is hypersensitive to proteolysis and entirely degraded in the context of the entire N proteins either.","_id":"685af523b4ac24d5329d82da"},{"type":"Discussion","text":"The results presented here show that both N proteins undergo proteolytic cleavage within their NTAIL domains, thus supporting the disordered nature of these domains not only in isolation but also in the context of the entire N proteins.","_id":"685af523b4ac24d5329d82db"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T07:41:19.411Z","_id":"685af523b4ac24d5329d82dc"},"version":4,"_id":"685af523b4ac24d5329d82d9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. <i> Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. </i> J Biol Chem, 2011","reference_id":"21317293","region_id":"DP00697r030","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In addition, both NMR and far-UV CD studies revealed a gain of α-helicity within NTAIL upon binding to PXD, and ITC studies showed that the interaction does not rely on electrostatic contacts, as the KD was not affected by NaCl concentrations as high as 1 m","_id":"685af523b4ac24d5329d82ee"},{"type":"Discussion","text":"The NMR titration experiments of Henipavirus NTAIL with increasing amounts of PXD confirmed that a complex is formed between the two partners. ","_id":"685af523b4ac24d5329d82ef"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T08:04:36.187Z","_id":"685af523b4ac24d5329d82f0"},"version":5,"_id":"685af523b4ac24d5329d82ed","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. <i> Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. </i> J Biol Chem, 2011","reference_id":"21317293","region_id":"DP00697r032","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In addition, both NMR and far-UV CD studies revealed a gain of α-helicity within NTAIL upon binding to PXD, and ITC studies showed that the interaction does not rely on electrostatic contacts, as the KD was not affected by NaCl concentrations as high as 1 m.","_id":"685af523b4ac24d5329d82f4"},{"type":"Discussion","text":"The NMR titration experiments of Henipavirus NTAIL with increasing amounts of PXD confirmed that a complex is formed between the two partners. ","_id":"685af523b4ac24d5329d82f5"},{"type":"Discussion","text":"These observations point toward the intermediate exchange regime often observed for IDPs undergoing folding-upon-binding events (for examples see Refs. 39, 54, 83, and 118).","_id":"685af523b4ac24d5329d82f6"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T08:02:10.926Z","_id":"685af523b4ac24d5329d82f7"},"version":5,"_id":"685af523b4ac24d5329d82f3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006289","ec_name":"site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Assessing induced folding within the intrinsically disordered C-terminal domain of the Henipavirus nucleoproteins by site-directed spin labeling EPR spectroscopy. <i> Martinho M, Habchi J, El Habre Z, Nesme L, Guigliarelli B, Belle V, Longhi S. </i> J Biomol Struct Dyn, 2013","reference_id":"22881220","region_id":"DP00697r038","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"For all the spin labels grafted within\nBox3, the number of possible rotamers built by MMM\non the structural model of the NiV NTAIL–PXD complex\n(i.e. the number of possible rotamers that could be\naccommodated in the available conformational space) is\ncomparable to that obtained with HeV (Figure 6(B)).\n","_id":"685af523b4ac24d5329d8303"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T08:04:16.194Z","_id":"685af523b4ac24d5329d8304"},"version":5,"_id":"685af523b4ac24d5329d8302","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006289","ec_name":"site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Assessing induced folding within the intrinsically disordered C-terminal domain of the Henipavirus nucleoproteins by site-directed spin labeling EPR spectroscopy. <i> Martinho M, Habchi J, El Habre Z, Nesme L, Guigliarelli B, Belle V, Longhi S. </i> J Biomol Struct Dyn, 2013","reference_id":"22881220","region_id":"DP00697r040","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"For all the spin labels grafted within\nBox3, the number of possible rotamers built by MMM\non the structural model of the NiV NTAIL–PXD complex\n(i.e. the number of possible rotamers that could be\naccommodated in the available conformational space) is\ncomparable to that obtained with HeV (Figure 6(B)).\n","_id":"685af523b4ac24d5329d8309"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T08:01:59.198Z","_id":"685af523b4ac24d5329d830a"},"version":5,"_id":"685af523b4ac24d5329d8308","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. <i> Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. </i> J Biol Chem, 2011","reference_id":"21317293","region_id":"DP00697r041","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Hence, this anomalous electrophoretic mobility is rather due to a rather high content of acidic residues, as already observed for other intrinsically disordered domains (for examples see Ref. 6, 45, and 85) and, more generally, in other IDPs (86).","_id":"685af523b4ac24d5329d830c"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T07:40:53.939Z","_id":"685af523b4ac24d5329d830d"},"version":1,"_id":"685af523b4ac24d5329d830b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. <i> Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. </i> J Biol Chem, 2011","reference_id":"21317293","region_id":"DP00697r042","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Conversely, the CD spectra of both NTAIL proteins are typical of predominantly unfolded proteins, as seen by their large negative ellipticity at 198 nm and low ellipticity at 190 nm (Fig. 5, A and B, black lines). Nevertheless, and as already reported (14), the observed ellipticity values at 200 and 222 nm of both Henipavirus NTAIL proteins are consistent with the existence of some residual secondary structure typical of IDPs adopting a PMG conformation (21).","_id":"685af523b4ac24d5329d830f"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T07:38:04.187Z","_id":"685af523b4ac24d5329d8310"},"version":1,"_id":"685af523b4ac24d5329d830e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007064","ec_name":"dynamic light scattering assay evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00697r043","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The obtained RS values (37±2 Å for both NTAIL proteins, and either 55±2 Å or 57±2 Å for NiV and HeV PNT, respectively) highlight a significant increase in the hydrodynamic radius in the presence of urea (see Table 1). These results argue for the presence of residual intramolecular interactions within Henipavirus PNT and NTAIL proteins under native conditions, as expected for proteins adopting a PMG conformation.","_id":"685af523b4ac24d5329d8312"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T07:37:36.709Z","_id":"685af523b4ac24d5329d8313"},"version":1,"_id":"685af523b4ac24d5329d8311","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. <i> Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. </i> J Biol Chem, 2011","reference_id":"21317293","region_id":"DP00697r044","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The experimentally observed spectra of the mixtures support a random-coil to α-helix transition, as judged by the much more pronounced minima at 208 and 222 nm and by the higher ellipticity at 190 nm of the experimentally observed spectra compared with the corresponding theoretical average curves (see Fig. 5, A and B).","_id":"685af523b4ac24d5329d8315"},{"type":"Results","text":"This analysis indicated a significant increase in the α-helical content of the mixtures as compared with average spectra, with this gain in α-helicity being paralleled by a decrease in the content of disordered structure (see Fig. 5, C and D).","_id":"685af523b4ac24d5329d8316"},{"type":"Discussion","text":"Using the same approach, we showed that both NiV and HeV NTAIL undergo α-helical induced folding upon binding to the corresponding P X domain","_id":"685af523b4ac24d5329d8317"}],"states_connection":[],"term_id":"IDPO:0000013","term_name":"pre-molten globule to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T07:59:06.869Z","_id":"685af523b4ac24d5329d8318"},"version":1,"_id":"685af523b4ac24d5329d8314","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005647","ec_name":"isothermal titration calorimetry evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[{"db":"UniProt","id":"Q9IK91","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d831a"}],"reference_html":"Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. <i> Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. </i> J Biol Chem, 2011","reference_id":"21317293","region_id":"DP00697r045","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The estimates for the model parameters (see Table 1) confirm a 1:1 stoichiometry and reveal that the binding reaction is both enthalpy- and entropy-driven, with the exception only of the NiV NTAIL-PXD couple for which a small unfavorable entropic contribution was found.","_id":"685af523b4ac24d5329d831b"},{"type":"Results","text":"Similar experiments carried out in the presence of 1 m NaCl (data not shown) yielded similar results (see Table 1), suggesting that the NTAIL-PXD interaction relies mainly on hydrophobic interactions.","_id":"685af523b4ac24d5329d831c"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T08:01:12.889Z","_id":"685af523b4ac24d5329d831d"},"version":1,"_id":"685af523b4ac24d5329d8319","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[{"db":"UniProt","id":"Q9IK91","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d831f"}],"reference_html":"Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. <i> Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. </i> J Biol Chem, 2011","reference_id":"21317293","region_id":"DP00697r046","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In the case of the study of the NiV NTAIL-PXD complex, upon addition of stoichiometric amounts of PXD, the NTAIL peak shifted toward a lower elution volume (from 8.1 to 7.75 ml), indicating the formation of an NTAIL-PXD complex, as also judged from the estimated mass (25,610 ± 80 Da), a value consistent with the binding of one PXD molecule/NTAIL (expected mass ∼ 22 kDa) (data not shown).","_id":"685af523b4ac24d5329d8320"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T08:01:07.909Z","_id":"685af523b4ac24d5329d8321"},"version":1,"_id":"685af523b4ac24d5329d831e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001269","ec_name":"surface plasmon resonance evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[{"db":"UniProt","id":"Q9IK91","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8323"}],"reference_html":"Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. <i> Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. </i> J Biol Chem, 2011","reference_id":"21317293","region_id":"DP00697r047","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The binding reaction conformed to a 1:1 ligand-substrate (Langmuir) binding model, exhibiting an excellent fit (i.e. χ2 < 1 and residuals within the range of ±2) following global kinetic analysis of sensorgrams as well as when plotting mean equilibrium responses of the data in the steady state analysis.","_id":"685af523b4ac24d5329d8324"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T08:01:01.883Z","_id":"685af523b4ac24d5329d8325"},"version":1,"_id":"685af523b4ac24d5329d8322","reference_source":"pmid"},{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2025-09-15T18:12:45.614Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"reference_html":"Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. <i> Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. </i> J Biol Chem, 2011","reference_id":"21317293","region_id":"DP00697r048","released":"2025_12","statement":[{"type":"Results","text":"Interestingly, in the case of the NiV NTAIL titration, but not of the HeV one, among the correlation peaks that were displaced by PXD, eight underwent an upfield shift (see Fig. 6A) consistent with a random coil to α-helix transition.","_id":"685af523b4ac24d5329d8327"}],"term_id":"IDPO:0000019","term_name":"disorder to pre-molten globule","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":2,"_id":"685af523b4ac24d5329d8326","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00697r049","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"These studies suggest that Henipavirus PNT and NTAIL proteins either adopt a PMG conformation or are folded trimers.","_id":"685af523b4ac24d5329d832a"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T07:31:56.744Z","_id":"685af523b4ac24d5329d832b"},"version":1,"_id":"685af523b4ac24d5329d8329","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006198","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00697r050","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The very small spread of the resonance frequencies for amide protons (between 7.8 ppm and 8.7 ppm, see frames in Fig. 6) together with the scarcity of NOEs in the amide-amide region are typical of proteins without any stable secondary structure (for examples see [6], [18]), thereby supporting lack of a packed core within Henipavirus PNT and NTAIL domains.","_id":"685af523b4ac24d5329d832d"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T07:27:29.063Z","_id":"685af523b4ac24d5329d832e"},"version":1,"_id":"685af523b4ac24d5329d832c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00697r051","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In further support of the absence of an ordered structure, the far-UV CD spectra of Henipavirus PNT and NTAIL at neutral pH are typical of unstructured proteins, as seen from their large negative ellipticity at 198 nm and low ellipticity at 190 nm (Fig. 7A). However, the observed ellipticity values at 200 and 222 nm of Henipavirus NTAIL and of NiV PNT are consistent with the existence of some residual secondary structure, as observed in IDPs adopting a PMG conformation (Fig. 7B).","_id":"685af523b4ac24d5329d8330"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T07:26:40.108Z","_id":"685af523b4ac24d5329d8331"},"version":1,"_id":"685af523b4ac24d5329d832f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Assessing induced folding within the intrinsically disordered C-terminal domain of the Henipavirus nucleoproteins by site-directed spin labeling EPR spectroscopy. <i> Martinho M, Habchi J, El Habre Z, Nesme L, Guigliarelli B, Belle V, Longhi S. </i> J Biomol Struct Dyn, 2013","reference_id":"22881220","region_id":"DP00697r052","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"This anomalous electrophoretic mobility is\nfrequently observed in IDPs and is to be ascribed to a\nrelatively high content in acidic residues (Tompa, 2002),\nand/or to a high degree of protein extension in solution\n(Blocquel et al., 2012).","_id":"685af523b4ac24d5329d8333"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T07:25:06.774Z","_id":"685af523b4ac24d5329d8334"},"version":1,"_id":"685af523b4ac24d5329d8332","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Assessing induced folding within the intrinsically disordered C-terminal domain of the Henipavirus nucleoproteins by site-directed spin labeling EPR spectroscopy. <i> Martinho M, Habchi J, El Habre Z, Nesme L, Guigliarelli B, Belle V, Longhi S. </i> J Biomol Struct Dyn, 2013","reference_id":"22881220","region_id":"DP00697r053","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The Stokes radius value of the monomeric form of\nall Henipavirus NTAIL variants (28 ± 2 Å), as inferred\nfrom the apparent molecular mass observed in SEC, is\nthe same as that observed for both parental HeV and\nNiV NTAIL proteins (data not shown). This value is consistent\nwith the value expected for IDPs adopting a premolten\nglobule state (Uversky, 2002b).","_id":"685af523b4ac24d5329d8336"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T07:19:01.804Z","_id":"685af523b4ac24d5329d8337"},"version":1,"_id":"685af523b4ac24d5329d8335","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Assessing induced folding within the intrinsically disordered C-terminal domain of the Henipavirus nucleoproteins by site-directed spin labeling EPR spectroscopy. <i> Martinho M, Habchi J, El Habre Z, Nesme L, Guigliarelli B, Belle V, Longhi S. </i> J Biomol Struct Dyn, 2013","reference_id":"22881220","region_id":"DP00697r054","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The far-UV CD spectra of spin-labeled NTAIL proteins variants at neutral pH quite well superimpose onto that of parental NTAIL, andare all typical of unstructured proteins, as shown by their large negative ellipticity at 200 nm and moderate ellipticity at 190 nm (Figures 2(A), (B) and S2).","_id":"685af523b4ac24d5329d8339"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T07:18:53.133Z","_id":"685af523b4ac24d5329d833a"},"version":1,"_id":"685af523b4ac24d5329d8338","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[{"db":"UniProt","id":"Q9IK91","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d833e"}],"reference_html":"Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. <i> Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. </i> J Biol Chem, 2011","reference_id":"21317293","region_id":"DP00697r055","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Indeed, the observed CD spectra of the mixtures differed from the corresponding theoretical average curves calculated from the individual NTAIL and PXD spectra (Fig. 5).","_id":"685af523b4ac24d5329d833c"},{"type":"Results","text":"In addition, both NMR and far-UV CD studies revealed a gain of α-helicity within NTAIL upon binding to PXD, and ITC studies showed that the interaction does not rely on electrostatic contacts, as the KD was not affected by NaCl concentrations as high as 1 m.","_id":"685af523b4ac24d5329d833d"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T08:00:14.825Z","_id":"685af523b4ac24d5329d833f"},"version":1,"_id":"685af523b4ac24d5329d833b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. <i> Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. </i> J Biol Chem, 2011","reference_id":"21317293","region_id":"DP00697r056","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Indeed, the observed CD spectra of the mixtures differed from the corresponding theoretical average curves calculated from the individual NTAIL and PXD spectra (Fig. 5).","_id":"685af523b4ac24d5329d8341"},{"type":"Results","text":"In addition, both NMR and far-UV CD studies revealed a gain of α-helicity within NTAIL upon binding to PXD, and ITC studies showed that the interaction does not rely on electrostatic contacts, as the KD was not affected by NaCl concentrations as high as 1 m.","_id":"685af523b4ac24d5329d8342"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T08:04:04.974Z","_id":"685af523b4ac24d5329d8343"},"version":1,"_id":"685af523b4ac24d5329d8340","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. <i> Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. </i> J Biol Chem, 2011","reference_id":"21317293","region_id":"DP00697r058","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In the case of the study of the NiV NTAIL-PXD complex, upon addition of stoichiometric amounts of PXD, the NTAIL peak shifted toward a lower elution volume (from 8.1 to 7.75 ml), indicating the formation of an NTAIL-PXD complex, as also judged from the estimated mass (25,610 ± 80 Da), a value consistent with the binding of one PXD molecule/NTAIL (expected mass ∼ 22 kDa) (data not shown).","_id":"685af523b4ac24d5329d8349"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T08:03:35.504Z","_id":"685af523b4ac24d5329d834a"},"version":1,"_id":"685af523b4ac24d5329d8348","reference_source":"pmid"}],"__v":0,"disorder_content":0.25,"disprot_consensus":{"full":[{"start":400,"end":532,"type":"T"}],"Structural state":[{"start":400,"end":532,"type":"D"}],"Molecular function":[{"start":400,"end":532,"type":"F"}],"Structural transition":[{"start":400,"end":532,"type":"T"}]}},{"acc":"O89339","sequence":"MSDIFDEAASFRSYQSKLGRDGRASAATATLTTKIRIFVPATNSPELRWELTLFALDVIRSPSAAESMKIGAAFTLISMYSERPGALIRSLLNDPDIEAVIIDVGSMLNGIPVMERRGDKAQEEMEGLMRILKTARESSKGKTPFVDSRAYGLRITDMSTLVSAVITIEAQIWILIAKAVTAPDTAEESETRRWAKYVQQKRVNPFFALTQQWLTEMRNLLSQSLSVRKFMVEILMEVKKGGSAKGRAVEIISDIGNYVEETGMAGFFATIRFGLETRYPALALNEFQSDLNTIKGLMLLYREIGPRAPYMVLLEESIQTKFAPGGYPLLWSFAMGVATTIDRSMGALNINRGYLEPMYFRLGQKSARHHAGGIDQNMANKLGLNSDQVAELAAAVQETSVGRQDNNMQAREAKFAAGGVLVGGGEQDIDEEEEPIEHSGRQSVTFKREMSMSSLADSVPSSSVSTSGGTRLTNSLLNLRSRLAAKAIKESTAQSSSERNPPNNRPQADSGRKDDQEPKPAQNDLDFVRADV","creator":"vnugnes","dataset":["Viral proteins","RNA-binding proteins"],"date":"2016-08-16T17:58:53.000Z","disprot_id":"DP00698","features":{"pfam":[{"id":"PF00973","name":"Paramyxovirus nucleocapsid protein","start":1,"end":399}]},"genes":[{"name":{"value":"N","evidences":[],"_id":"685af523b4ac24d5329d83e1"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d83e0"}],"length":532,"name":"Nucleoprotein","ncbi_taxon_id":928303,"organism":"Hendra virus (isolate Horse/Autralia/Hendra/1994)","regions_counter":52,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Paramyxoviridae","Orthoparamyxovirinae","Henipavirus"],"UniParc":"UPI00000F625F","uniref100":"UniRef100_O89339","uniref50":"UniRef50_Q9IK92","uniref90":"UniRef90_Q9IK92","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00698r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Henipavirus PNT and NTAIL were found to be highly sensitive to proteolysis, a property that constitutes a hallmark of structural disorder (see [47] and references therein cited).","_id":"685af523b4ac24d5329d8354"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T08:46:19.113Z","_id":"685af523b4ac24d5329d8355"},"version":3,"_id":"685af523b4ac24d5329d8353","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00698r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"This abnormal behavior is therefore likely to be ascribed to a rather high content of acidic residues, as already been observed in the case of the intrinsically disordered MeV PNT [18] and NTAIL domains [6], [19], and, more generally, in other IDPs [46].","_id":"685af523b4ac24d5329d8365"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T08:46:22.908Z","_id":"685af523b4ac24d5329d8366"},"version":3,"_id":"685af523b4ac24d5329d8364","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006289","ec_name":"site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Assessing induced folding within the intrinsically disordered C-terminal domain of the Henipavirus nucleoproteins by site-directed spin labeling EPR spectroscopy. <i> Martinho M, Habchi J, El Habre Z, Nesme L, Guigliarelli B, Belle V, Longhi S. </i> J Biomol Struct Dyn, 2013","reference_id":"22881220","region_id":"DP00698r014","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Taken together, the EPR analyses of the labeled variants within Box3 bring experimental support for the structural model of HeV NTAIL–PXD complex that we previously proposed (Habchi et al., 2011) (Figure 6(A)).","_id":"685af523b4ac24d5329d8370"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T08:48:07.810Z","_id":"685af523b4ac24d5329d8371"},"version":4,"_id":"685af523b4ac24d5329d836f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006289","ec_name":"site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Assessing induced folding within the intrinsically disordered C-terminal domain of the Henipavirus nucleoproteins by site-directed spin labeling EPR spectroscopy. <i> Martinho M, Habchi J, El Habre Z, Nesme L, Guigliarelli B, Belle V, Longhi S. </i> J Biomol Struct Dyn, 2013","reference_id":"22881220","region_id":"DP00698r016","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Taken together, the EPR analyses of the labeled variants\nwithin Box3 bring experimental support for the\nstructural model of HeV NTAIL–PXD complex that we\npreviously proposed (Habchi et al., 2011) (Figure 6(A)).","_id":"685af523b4ac24d5329d8376"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T08:46:55.687Z","_id":"685af523b4ac24d5329d8377"},"version":4,"_id":"685af523b4ac24d5329d8375","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006198","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00698r021","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The very small spread of the resonance frequencies for amide protons (between 7.8 ppm and 8.7 ppm, see frames in Fig. 6) together with the scarcity of NOEs in the amide-amide region are typical of proteins without any stable secondary structure (for examples see [6], [18]), thereby supporting lack of a packed core within Henipavirus PNT and NTAIL domains.","_id":"685af523b4ac24d5329d8381"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T08:46:00.237Z","_id":"685af523b4ac24d5329d8382"},"version":3,"_id":"685af523b4ac24d5329d8380","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. <i> Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. </i> J Biol Chem, 2011","reference_id":"21317293","region_id":"DP00698r025","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"On the other hand, no fragment corresponding to the remaining NTAIL domain was detected, indicating that it is hypersensitive to proteolysis and entirely degraded in the context of the entire N proteins either.","_id":"685af523b4ac24d5329d838a"},{"type":"Discussion","text":"The results presented here show that both N proteins undergo proteolytic cleavage within their NTAIL domains, thus supporting the disordered nature of these domains not only in isolation but also in the context of the entire N proteins.","_id":"685af523b4ac24d5329d838b"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T08:45:51.630Z","_id":"685af523b4ac24d5329d838c"},"version":3,"_id":"685af523b4ac24d5329d8389","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. <i> Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. </i> J Biol Chem, 2011","reference_id":"21317293","region_id":"DP00698r037","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Conversely, the CD spectra of both NTAIL proteins are typical of predominantly unfolded proteins, as seen by their large negative ellipticity at 198 nm and low ellipticity at 190 nm (Fig. 5, A and B, black lines). Nevertheless, and as already reported (14), the observed ellipticity values at 200 and 222 nm of both Henipavirus NTAIL proteins are consistent with the existence of some residual secondary structure typical of IDPs adopting a PMG conformation (21).","_id":"685af523b4ac24d5329d83a5"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T08:45:43.029Z","_id":"685af523b4ac24d5329d83a6"},"version":1,"_id":"685af523b4ac24d5329d83a4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. <i> Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. </i> J Biol Chem, 2011","reference_id":"21317293","region_id":"DP00698r038","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Hence, this anomalous electrophoretic mobility is rather due to a rather high content of acidic residues, as already observed for other intrinsically disordered domains (for examples see Ref. 6, 45, and 85) and, more generally, in other IDPs (86).","_id":"685af523b4ac24d5329d83a8"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2022-03-08T15:41:03.808Z","_id":"685af523b4ac24d5329d83a9"},"version":1,"_id":"685af523b4ac24d5329d83a7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. <i> Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. </i> J Biol Chem, 2011","reference_id":"21317293","region_id":"DP00698r039","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The experimentally observed spectra of the mixtures support a random-coil to α-helix transition, as judged by the much more pronounced minima at 208 and 222 nm and by the higher ellipticity at 190 nm of the experimentally observed spectra compared with the corresponding theoretical average curves (see Fig. 5, A and B).","_id":"685af523b4ac24d5329d83ab"},{"type":"Results","text":"This analysis indicated a significant increase in the α-helical content of the mixtures as compared with average spectra, with this gain in α-helicity being paralleled by a decrease in the content of disordered structure (see Fig. 5, C and D).","_id":"685af523b4ac24d5329d83ac"},{"type":"Discussion","text":"Using the same approach, we showed that both NiV and HeV NTAIL undergo α-helical induced folding upon binding to the corresponding P X domain.","_id":"685af523b4ac24d5329d83ad"}],"states_connection":[],"term_id":"IDPO:0000013","term_name":"pre-molten globule to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T08:46:07.149Z","_id":"685af523b4ac24d5329d83ae"},"version":1,"_id":"685af523b4ac24d5329d83aa","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005647","ec_name":"isothermal titration calorimetry evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[{"db":"UniProt","id":"O55778","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d83b0"}],"reference_html":"Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. <i> Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. </i> J Biol Chem, 2011","reference_id":"21317293","region_id":"DP00698r040","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The estimates for the model parameters (see Table 1) confirm a 1:1 stoichiometry and reveal that the binding reaction is both enthalpy- and entropy-driven, with the exception only of the NiV NTAIL-PXD couple for which a small unfavorable entropic contribution was found. ","_id":"685af523b4ac24d5329d83b1"},{"type":"Results","text":"Similar experiments carried out in the presence of 1 m NaCl (data not shown) yielded similar results (see Table 1), suggesting that the NTAIL-PXD interaction relies mainly on hydrophobic interactions.","_id":"685af523b4ac24d5329d83b2"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T08:46:45.812Z","_id":"685af523b4ac24d5329d83b3"},"version":1,"_id":"685af523b4ac24d5329d83af","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006198","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[{"db":"UniProt","id":"O55778","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d83b7"}],"reference_html":"Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. <i> Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. </i> J Biol Chem, 2011","reference_id":"21317293","region_id":"DP00698r042","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"The NMR titration experiments of Henipavirus NTAIL with increasing amounts of PXD confirmed that a complex is formed between the two partners. ","_id":"685af523b4ac24d5329d83b8"},{"type":"Results","text":"In addition, both NMR and far-UV CD studies revealed a gain of α-helicity within NTAIL upon binding to PXD, and ITC studies showed that the interaction does not rely on electrostatic contacts, as the KD was not affected by NaCl concentrations as high as 1 m.","_id":"685af523b4ac24d5329d83b9"},{"type":"Discussion","text":"These observations point toward the intermediate exchange regime often observed for IDPs undergoing folding-upon-binding events (for examples see Refs. 39, 54, 83, and 118).","_id":"685af523b4ac24d5329d83ba"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T08:46:36.087Z","_id":"685af523b4ac24d5329d83bb"},"version":1,"_id":"685af523b4ac24d5329d83b6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00698r043","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"These studies suggest that Henipavirus PNT and NTAIL proteins either adopt a PMG conformation or are folded trimers.","_id":"685af523b4ac24d5329d83bd"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T08:22:10.366Z","_id":"685af523b4ac24d5329d83be"},"version":1,"_id":"685af523b4ac24d5329d83bc","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00698r044","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In further support of the absence of an ordered structure, the far-UV CD spectra of Henipavirus PNT and NTAIL at neutral pH are typical of unstructured proteins, as seen from their large negative ellipticity at 198 nm and low ellipticity at 190 nm (Fig. 7A). However, the observed ellipticity values at 200 and 222 nm of Henipavirus NTAIL and of NiV PNT are consistent with the existence of some residual secondary structure, as observed in IDPs adopting a PMG conformation (Fig. 7B).","_id":"685af523b4ac24d5329d83c0"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2022-03-08T15:41:06.607Z","_id":"685af523b4ac24d5329d83c1"},"version":1,"_id":"685af523b4ac24d5329d83bf","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007064","ec_name":"dynamic light scattering assay evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00698r045","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The obtained RS values (37±2 Å for both NTAIL proteins, and either 55±2 Å or 57±2 Å for NiV and HeV PNT, respectively) highlight a significant increase in the hydrodynamic radius in the presence of urea (see Table 1). These results argue for the presence of residual intramolecular interactions within Henipavirus PNT and NTAIL proteins under native conditions, as expected for proteins adopting a PMG conformation.","_id":"685af523b4ac24d5329d83c3"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T08:19:01.720Z","_id":"685af523b4ac24d5329d83c4"},"version":1,"_id":"685af523b4ac24d5329d83c2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Assessing induced folding within the intrinsically disordered C-terminal domain of the Henipavirus nucleoproteins by site-directed spin labeling EPR spectroscopy. <i> Martinho M, Habchi J, El Habre Z, Nesme L, Guigliarelli B, Belle V, Longhi S. </i> J Biomol Struct Dyn, 2013","reference_id":"22881220","region_id":"DP00698r046","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"This anomalous electrophoretic mobility is\nfrequently observed in IDPs and is to be ascribed to a\nrelatively high content in acidic residues (Tompa, 2002),\nand/or to a high degree of protein extension in solution\n(Blocquel et al., 2012).","_id":"685af523b4ac24d5329d83c6"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T08:18:26.071Z","_id":"685af523b4ac24d5329d83c7"},"version":1,"_id":"685af523b4ac24d5329d83c5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Assessing induced folding within the intrinsically disordered C-terminal domain of the Henipavirus nucleoproteins by site-directed spin labeling EPR spectroscopy. <i> Martinho M, Habchi J, El Habre Z, Nesme L, Guigliarelli B, Belle V, Longhi S. </i> J Biomol Struct Dyn, 2013","reference_id":"22881220","region_id":"DP00698r047","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The Stokes radius value of the monomeric form of\nall Henipavirus NTAIL variants (28 ± 2 Å), as inferred\nfrom the apparent molecular mass observed in SEC, is\nthe same as that observed for both parental HeV and\nNiV NTAIL proteins (data not shown). This value is consistent\nwith the value expected for IDPs adopting a premolten\nglobule state (Uversky, 2002b).","_id":"685af523b4ac24d5329d83c9"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T08:15:46.725Z","_id":"685af523b4ac24d5329d83ca"},"version":1,"_id":"685af523b4ac24d5329d83c8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Assessing induced folding within the intrinsically disordered C-terminal domain of the Henipavirus nucleoproteins by site-directed spin labeling EPR spectroscopy. <i> Martinho M, Habchi J, El Habre Z, Nesme L, Guigliarelli B, Belle V, Longhi S. </i> J Biomol Struct Dyn, 2013","reference_id":"22881220","region_id":"DP00698r048","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The far-UV CD spectra of spin-labeled NTAIL proteins variants at neutral pH quite well superimpose onto that of parental NTAIL, and are all typical of unstructured proteins, as shown by their large negative ellipticity at 200 nm and moderate ellipticity at 190 nm (Figures 2(A), (B) and S2).","_id":"685af523b4ac24d5329d83cc"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-04T12:25:45.141Z","_id":"685af523b4ac24d5329d83cd"},"version":1,"_id":"685af523b4ac24d5329d83cb","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006198","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. <i> Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. </i> J Biol Chem, 2011","reference_id":"21317293","region_id":"DP00698r049","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The NMR titration experiments of Henipavirus NTAIL with increasing amounts of PXD confirmed that a complex is formed between the two partners. ","_id":"685af523b4ac24d5329d83cf"},{"type":"Results","text":"In addition, both NMR and far-UV CD studies revealed a gain of α-helicity within NTAIL upon binding to PXD, and ITC studies showed that the interaction does not rely on electrostatic contacts, as the KD was not affected by NaCl concentrations as high as 1 m.","_id":"685af523b4ac24d5329d83d0"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T08:48:08.612Z","_id":"685af523b4ac24d5329d83d1"},"version":1,"_id":"685af523b4ac24d5329d83ce","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[{"db":"UniProt","id":"O55778","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d83d5"}],"reference_html":"Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. <i> Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. </i> J Biol Chem, 2011","reference_id":"21317293","region_id":"DP00698r050","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Indeed, the observed CD spectra of the mixtures differed from the corresponding theoretical average curves calculated from the individual NTAIL and PXD spectra (Fig. 5).","_id":"685af523b4ac24d5329d83d3"},{"type":"Results","text":"In addition, both NMR and far-UV CD studies revealed a gain of α-helicity within NTAIL upon binding to PXD, and ITC studies showed that the interaction does not rely on electrostatic contacts, as the KD was not affected by NaCl concentrations as high as 1 m.","_id":"685af523b4ac24d5329d83d4"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T08:46:30.556Z","_id":"685af523b4ac24d5329d83d6"},"version":1,"_id":"685af523b4ac24d5329d83d2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":532,"interaction_partner":[],"reference_html":"Characterization of the interactions between the nucleoprotein and the phosphoprotein of Henipavirus. <i> Habchi J, Blangy S, Mamelli L, Jensen MR, Blackledge M, Darbon H, Oglesbee M, Shu Y, Longhi S. </i> J Biol Chem, 2011","reference_id":"21317293","region_id":"DP00698r051","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Indeed, the observed CD spectra of the mixtures differed from the corresponding theoretical average curves calculated from the individual NTAIL and PXD spectra (Fig. 5).","_id":"685af523b4ac24d5329d83d8"},{"type":"Results","text":"In addition, both NMR and far-UV CD studies revealed a gain of α-helicity within NTAIL upon binding to PXD, and ITC studies showed that the interaction does not rely on electrostatic contacts, as the KD was not affected by NaCl concentrations as high as 1 m.","_id":"685af523b4ac24d5329d83d9"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T08:47:54.151Z","_id":"685af523b4ac24d5329d83da"},"version":1,"_id":"685af523b4ac24d5329d83d7","reference_source":"pmid"}],"__v":0,"disorder_content":0.25,"disprot_consensus":{"full":[{"start":400,"end":532,"type":"T"}],"Structural state":[{"start":400,"end":532,"type":"D"}],"Molecular function":[{"start":400,"end":532,"type":"F"}],"Structural transition":[{"start":400,"end":532,"type":"T"}]}},{"acc":"Q9IK91","sequence":"MDKLELVNDGLNIIDFIQKNQKEIQKTYGRSSIQQPSIKDQTKAWEDFLQCTSGESEQVEGGMSKDDGDVERRNLEDLSSTSPTDGTIGKRVSNTRDWAEGSDDIQLDPVVTDVVYHDHGGECTGYGFTSSPERGWSDYTSGANNGNVCLVSDAKMLSYAPEIAVSKEDRETDLVHLENKLSTTGLNPTAVPFTLRNLSDPAKDSPVIAEHYYGLGVKEQNVGPQTSRNVNLDSIKLYTSDDEEADQLEFEDEFAGSSSEVIVGISPEDEEPSSVGGKPNESIGRTIEGQSIRDNLQAKDNKSTDVPGAGPKDSAVKEEPPQKRLPMLAEEFECSGSEDPIIRELLKENSLINCQQGKDAQPPYHWSIERSISPDKTEIVNGAVQTADRQRPGTPMPKSRGIPIKKGTDAKYPSAGTENVPGSKSGATRHVRGSPPYQEGKSVNAENVQLNASTAVKETDKSEVNPVDDNDSLDDKYIMPSDDFSNTFFPHDTDRLNYHADHLGDYDLETLCEESVLMGVINSIKLINLDMRLNHIEEQVKEIPKIINKLESIDRVLAKTNTALSTIEGHLVSMMIMIPGKGKGERKGKNNPELKPVIGRDILEQQSLFSFDNVKNFRDGSLTNEPYGAAVQLREDLILPELNFEETNASQFVPMADDSSRDVIKTLIRTHIKDRELRSELIGYLNKAENDEEIQEIANTVNDIIDGNI","creator":"vnugnes","dataset":["Viral proteins"],"date":"2016-08-31T11:04:28.000Z","disprot_id":"DP00699","features":{"pfam":[{"id":"PF03210","name":"Paramyxovirus P/V phosphoprotein C-terminal","start":534,"end":701},{"id":"PF13825","name":"Paramyxovirus structural protein V/P N-terminus","start":397,"end":456},{"id":"PF14313","name":"N-terminal region of Paramyxovirinae phosphoprotein (P)","start":5,"end":52},{"id":"PF14320","name":"Phosphoprotein P region PNT disordered","start":71,"end":351}],"gene3D":[{"start":654,"end":709,"id":"1.10.8.10","name":"DNA helicase RuvA subunit, C-terminal domain","_id":"685af523b4ac24d5329d83e6"}]},"genes":[{"name":{"value":"P/V/C","evidences":[],"_id":"685af523b4ac24d5329d846d"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d846c"}],"length":709,"name":"Phosphoprotein","ncbi_taxon_id":121791,"organism":"Nipah virus","regions_counter":49,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Paramyxoviridae","Orthoparamyxovirinae","Henipavirus"],"UniParc":"UPI00000EF0CF","uniref100":"UniRef100_Q9IK91","uniref50":"UniRef50_Q9IK91","uniref90":"UniRef90_Q9IK91","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006198","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":406,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00699r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The very small spread of the resonance frequencies for amide protons (between 7.8 ppm and 8.7 ppm, see frames in Fig. 6) together with the scarcity of NOEs in the amide-amide region are typical of proteins without any stable secondary structure (for examples see [6], [18]), thereby supporting lack of a packed core within Henipavirus PNT and NTAIL domains.","_id":"685af523b4ac24d5329d83e8"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-21T18:06:34.431Z","_id":"685af523b4ac24d5329d83e9"},"version":3,"_id":"685af523b4ac24d5329d83e7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":406,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00699r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Henipavirus PNT and NTAIL were found to be highly sensitive to proteolysis, a property that constitutes a hallmark of structural disorder (see [47] and references therein cited).","_id":"685af523b4ac24d5329d83f1"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-21T18:06:59.382Z","_id":"685af523b4ac24d5329d83f2"},"version":3,"_id":"685af523b4ac24d5329d83f0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007064","ec_name":"dynamic light scattering assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":406,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00699r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The obtained RS values (37±2 Å for both NTAIL proteins, and either 55±2 Å or 57±2 Å for NiV and HeV PNT, respectively) highlight a significant increase in the hydrodynamic radius in the presence of urea (see Table 1). These results argue for the presence of residual intramolecular interactions within Henipavirus PNT and NTAIL proteins under native conditions, as expected for proteins adopting a PMG conformation.","_id":"685af523b4ac24d5329d83fa"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-21T18:06:48.837Z","_id":"685af523b4ac24d5329d83fb"},"version":3,"_id":"685af523b4ac24d5329d83f9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":406,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00699r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"This abnormal behavior is therefore likely to be ascribed to a rather high content of acidic residues, as already been observed in the case of the intrinsically disordered MeV PNT [18] and NTAIL domains [6], [19], and, more generally, in other IDPs [46].","_id":"685af523b4ac24d5329d8403"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-21T16:24:01.187Z","_id":"685af523b4ac24d5329d8404"},"version":3,"_id":"685af523b4ac24d5329d8402","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":406,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00699r017","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In further support of the absence of an ordered structure, the far-UV CD spectra of Henipavirus PNT and NTAIL at neutral pH are typical of unstructured proteins, as seen from their large negative ellipticity at 198 nm and low ellipticity at 190 nm (Fig. 7A). However, the observed ellipticity values at 200 and 222 nm of Henipavirus NTAIL and of NiV PNT are consistent with the existence of some residual secondary structure, as observed in IDPs adopting a PMG conformation (Fig. 7B).","_id":"685af523b4ac24d5329d840c"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-21T16:24:00.294Z","_id":"685af523b4ac24d5329d840d"},"version":3,"_id":"685af523b4ac24d5329d840b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":406,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00699r029","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"These studies suggest that Henipavirus PNT and NTAIL proteins either adopt a PMG conformation or are folded trimers.","_id":"685af523b4ac24d5329d8426"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-21T16:23:59.901Z","_id":"685af523b4ac24d5329d8427"},"version":3,"_id":"685af523b4ac24d5329d8425","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"50370","_id":"685af523b4ac24d5329d843b"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":406,"interaction_partner":[],"reference_html":"Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS. <i> Schiavina M, Salladini E, Murrali MG, Tria G, Felli IC, Pierattelli R, Longhi S. </i> Sci Rep, 2020","reference_id":"33177626","region_id":"DP00699r037","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"NiV PNT is a very large intrinsically disordered protein (412 residues including the C-terminal His tag and the initial methionine), as can be inferred by inspection of the two 2D spectra, the 1H–15N HSQC (Fig. 2A) and the 13C′–15N CON (Fig. 2B).","_id":"685af523b4ac24d5329d8438"},{"type":"Results","text":"The relaxation rates show an overall trend consistent with the considerably disordered conformation of PNT.","_id":"685af523b4ac24d5329d8439"},{"type":"Results","text":"The NMR data clearly suggest that NiV PNT is disordered and very flexible with few short and transient secondary structure elements.","_id":"685af523b4ac24d5329d843a"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-29T14:48:51.921Z","_id":"685af523b4ac24d5329d843c"},"version":3,"_id":"685af523b4ac24d5329d8437","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"SASBDB","id":"SASDJB5","_id":"685af523b4ac24d5329d8440"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":406,"interaction_partner":[],"reference_html":"Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS. <i> Schiavina M, Salladini E, Murrali MG, Tria G, Felli IC, Pierattelli R, Longhi S. </i> Sci Rep, 2020","reference_id":"33177626","region_id":"DP00699r038","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The experimentally determined Rg is therefore very close to the value expected for an IDP (for comparison the Rg expected for a random coil conformation would be ~ 7253).","_id":"685af523b4ac24d5329d843e"},{"type":"Results","text":"The flexible nature of NiV PNT was qualitatively assessed by using the normalized Kratky plot, where the absence of a well-defined bell shape indicates a protein with intrinsically disordered regions (Fig. 4C).","_id":"685af523b4ac24d5329d843f"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-29T14:48:45.880Z","_id":"685af523b4ac24d5329d8441"},"version":3,"_id":"685af523b4ac24d5329d843d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0001238","ec_name":"nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":100,"interaction_partner":[],"reference_html":"Structure of Nipah virus unassembled nucleoprotein in complex with its viral chaperone. <i> Yabukarski F, Lawrence P, Tarbouriech N, Bourhis JM, Delaforge E, Jensen MR, Ruigrok RW, Blackledge M, Volchkov V, Jamin M. </i> Nat Struct Mol Biol, 2014","reference_id":"25108352","region_id":"DP00699r039","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In addition, the poor chemical-shift dispersion of amide resonances in the HSQC NMR spectrum was typical of disordered protein, but after assigning the NMR spectrum, the secondary-structure propensity (SSP) parameter calculated from Cα and Cβ secondary chemical shifts indicated the presence of five fluctuating α-helices (Supplementary Fig. 2c).","_id":"685af523b4ac24d5329d8443"},{"type":"Figure","text":"The poor chemical shift dispersion of amide 1H resonances in the heteronuclear single quantum coherence (HSQC) NMR spectrum (Supplementary Fig. 1d) is typical of disordered proteins. ","_id":"685af523b4ac24d5329d8444"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-29T14:54:20.965Z","_id":"685af523b4ac24d5329d8445"},"version":1,"_id":"685af523b4ac24d5329d8442","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":100,"interaction_partner":[],"reference_html":"Structure of Nipah virus unassembled nucleoprotein in complex with its viral chaperone. <i> Yabukarski F, Lawrence P, Tarbouriech N, Bourhis JM, Delaforge E, Jensen MR, Ruigrok RW, Blackledge M, Volchkov V, Jamin M. </i> Nat Struct Mol Biol, 2014","reference_id":"25108352","region_id":"DP00699r040","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"By SEC-MALLS, we showed that the peptide is monomeric in solution and that both its hydrodynamic radius measured by SEC and its radius of gyration measured by SAXS were larger than expected for a globular protein of this molecular mass (Supplementary Fig. 2a,b).","_id":"685af523b4ac24d5329d8447"},{"type":"Figure","text":"The hydrodynamic radius of 2.6 ± 0.5 nm measured by SEC (a) and the radius of gyration of 3.1 ± 0.5 nm measured by SAXS (b) are larger than expected for a compact domain of this size.","_id":"685af523b4ac24d5329d8448"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-29T14:47:47.799Z","_id":"685af523b4ac24d5329d8449"},"version":1,"_id":"685af523b4ac24d5329d8446","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":100,"interaction_partner":[],"reference_html":"Structure of Nipah virus unassembled nucleoprotein in complex with its viral chaperone. <i> Yabukarski F, Lawrence P, Tarbouriech N, Bourhis JM, Delaforge E, Jensen MR, Ruigrok RW, Blackledge M, Volchkov V, Jamin M. </i> Nat Struct Mol Biol, 2014","reference_id":"25108352","region_id":"DP00699r041","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"By SEC-MALLS, we showed that the peptide is monomeric in solution and that both its hydrodynamic radius measured by SEC and its radius of gyration measured by SAXS were larger than expected for a globular protein of this molecular mass (Supplementary Fig. 2a,b).","_id":"685af523b4ac24d5329d844b"},{"type":"Figure","text":"The hydrodynamic radius of 2.6 ± 0.5 nm measured by SEC (a) and the radius of gyration of 3.1 ± 0.5 nm measured by SAXS (b) are larger than expected for a compact domain of this size.","_id":"685af523b4ac24d5329d844c"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-29T14:38:06.827Z","_id":"685af523b4ac24d5329d844d"},"version":1,"_id":"685af523b4ac24d5329d844a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"4CO6","_id":"685af523b4ac24d5329d8451"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":35,"interaction_partner":[{"db":"UniProt","id":"Q9IK92","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d844f"}],"reference_html":"Structure of Nipah virus unassembled nucleoprotein in complex with its viral chaperone. <i> Yabukarski F, Lawrence P, Tarbouriech N, Bourhis JM, Delaforge E, Jensen MR, Ruigrok RW, Blackledge M, Volchkov V, Jamin M. </i> Nat Struct Mol Biol, 2014","reference_id":"25108352","region_id":"DP00699r042","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The N-terminal chaperone region of P is stabilized upon binding to its N0 partner, but only the first 35 residues of P, corresponding to the first fluctuating helix observed in solution (helix αP1), were visible in the crystal structure of N32–3830–P50. ","_id":"685af523b4ac24d5329d8450"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-29T14:50:37.767Z","_id":"685af523b4ac24d5329d8452"},"version":1,"_id":"685af523b4ac24d5329d844e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"4CO6","_id":"685af523b4ac24d5329d8455"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":35,"interaction_partner":[],"reference_html":"Structure of Nipah virus unassembled nucleoprotein in complex with its viral chaperone. <i> Yabukarski F, Lawrence P, Tarbouriech N, Bourhis JM, Delaforge E, Jensen MR, Ruigrok RW, Blackledge M, Volchkov V, Jamin M. </i> Nat Struct Mol Biol, 2014","reference_id":"25108352","region_id":"DP00699r043","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The N-terminal chaperone region of P is stabilized upon binding to its N0 partner, but only the first 35 residues of P, corresponding to the first fluctuating helix observed in solution (helix αP1), were visible in the crystal structure of N32–3830–P50. ","_id":"685af523b4ac24d5329d8454"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-29T14:50:00.023Z","_id":"685af523b4ac24d5329d8456"},"version":1,"_id":"685af523b4ac24d5329d8453","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":50,"interaction_partner":[],"reference_html":"Structure of Nipah virus unassembled nucleoprotein in complex with its viral chaperone. <i> Yabukarski F, Lawrence P, Tarbouriech N, Bourhis JM, Delaforge E, Jensen MR, Ruigrok RW, Blackledge M, Volchkov V, Jamin M. </i> Nat Struct Mol Biol, 2014","reference_id":"25108352","region_id":"DP00699r044","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"By size-exclusion chromatography (SEC) combined with multiangle laser light scattering (MALLS) (Fig. 1b) and by small-angle X-ray scattering (SAXS), we found that these reconstituted N0–P core complexes are compact heterodimers with an overall bean-like shape typical of other NNV N proteins18.","_id":"685af523b4ac24d5329d8458"},{"type":"Figure","text":"(c) The heterodimeric N32-3830-P50 complex has a bean shape in solution. The ab initio bead model generated from SAXS data (in grey) accommodates a single N32-3830-P50 copy from the crystal.","_id":"685af523b4ac24d5329d8459"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-29T14:50:29.154Z","_id":"685af523b4ac24d5329d845a"},"version":1,"_id":"685af523b4ac24d5329d8457","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":50,"interaction_partner":[],"reference_html":"Structure of Nipah virus unassembled nucleoprotein in complex with its viral chaperone. <i> Yabukarski F, Lawrence P, Tarbouriech N, Bourhis JM, Delaforge E, Jensen MR, Ruigrok RW, Blackledge M, Volchkov V, Jamin M. </i> Nat Struct Mol Biol, 2014","reference_id":"25108352","region_id":"DP00699r045","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"We then analyzed the HSQC spectrum of P100 bound to N32–402. In a complex of this size (~50 kDa), NMR signals are strongly broadened in protonated samples, thus precluding their detection, but in the HSQC spectrum we observed resonances corresponding to residues 50 to 100, thus indicating that this region remains flexible in the complex and that the N0-binding region is comprised within the first 50 N-terminal amino acids of P (Fig. 1c and Supplementary Fig. 1d).","_id":"685af523b4ac24d5329d845c"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-29T14:50:11.332Z","_id":"685af523b4ac24d5329d845d"},"version":1,"_id":"685af523b4ac24d5329d845b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":50,"interaction_partner":[],"reference_html":"Structure of Nipah virus unassembled nucleoprotein in complex with its viral chaperone. <i> Yabukarski F, Lawrence P, Tarbouriech N, Bourhis JM, Delaforge E, Jensen MR, Ruigrok RW, Blackledge M, Volchkov V, Jamin M. </i> Nat Struct Mol Biol, 2014","reference_id":"25108352","region_id":"DP00699r046","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"We then analyzed the HSQC spectrum of P100 bound to N32–402. In a complex of this size (~50 kDa), NMR signals are strongly broadened in protonated samples, thus precluding their detection, but in the HSQC spectrum we observed resonances corresponding to residues 50 to 100, thus indicating that this region remains flexible in the complex and that the N0-binding region is comprised within the first 50 N-terminal amino acids of P (Fig. 1c and Supplementary Fig. 1d).","_id":"685af523b4ac24d5329d845f"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-29T14:50:51.387Z","_id":"685af523b4ac24d5329d8460"},"version":1,"_id":"685af523b4ac24d5329d845e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":50,"interaction_partner":[],"reference_html":"Structure of Nipah virus unassembled nucleoprotein in complex with its viral chaperone. <i> Yabukarski F, Lawrence P, Tarbouriech N, Bourhis JM, Delaforge E, Jensen MR, Ruigrok RW, Blackledge M, Volchkov V, Jamin M. </i> Nat Struct Mol Biol, 2014","reference_id":"25108352","region_id":"DP00699r047","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"By size-exclusion chromatography (SEC) combined with multiangle laser light scattering (MALLS) (Fig. 1b) and by small-angle X-ray scattering (SAXS), we found that these reconstituted N0–P core complexes are compact heterodimers with an overall bean-like shape typical of other NNV N proteins18.","_id":"685af523b4ac24d5329d8462"},{"type":"Figure","text":"(c) The heterodimeric N32-3830-P50 complex has a bean shape in solution. The ab initio bead model generated from SAXS data (in grey) accommodates a single N32-3830-P50 copy from the crystal.","_id":"685af523b4ac24d5329d8463"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-29T14:50:48.589Z","_id":"685af523b4ac24d5329d8464"},"version":1,"_id":"685af523b4ac24d5329d8461","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"4CO6","_id":"685af523b4ac24d5329d8466"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":35,"interaction_partner":[],"reference_html":"Structure of Nipah virus unassembled nucleoprotein in complex with its viral chaperone. <i> Yabukarski F, Lawrence P, Tarbouriech N, Bourhis JM, Delaforge E, Jensen MR, Ruigrok RW, Blackledge M, Volchkov V, Jamin M. </i> Nat Struct Mol Biol, 2014","reference_id":"25108352","region_id":"DP00699r048","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The N-terminal chaperone region of P is stabilized upon binding to its N0 partner, but only the first 35 residues of P, corresponding to the first fluctuating helix observed in solution (helix αP1), were visible in the crystal structure of N32–3830–P50.","_id":"685af523b4ac24d5329d8467"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-29T14:50:43.603Z","_id":"685af523b4ac24d5329d8468"},"version":1,"_id":"685af523b4ac24d5329d8465","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":100,"interaction_partner":[],"reference_html":"Structure of Nipah virus unassembled nucleoprotein in complex with its viral chaperone. <i> Yabukarski F, Lawrence P, Tarbouriech N, Bourhis JM, Delaforge E, Jensen MR, Ruigrok RW, Blackledge M, Volchkov V, Jamin M. </i> Nat Struct Mol Biol, 2014","reference_id":"25108352","region_id":"DP00699r049","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In addition, the poor chemical-shift dispersion of amide resonances in the HSQC NMR spectrum was typical of disordered protein, but after assigning the NMR spectrum, the secondary-structure propensity (SSP) parameter calculated from Cα and Cβ secondary chemical shifts indicated the presence of five fluctuating α-helices (Supplementary Fig. 2c).","_id":"685af523b4ac24d5329d846a"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-29T14:49:14.988Z","_id":"685af523b4ac24d5329d846b"},"version":1,"_id":"685af523b4ac24d5329d8469","reference_source":"pmid"}],"__v":0,"disorder_content":0.5726375176304654,"disprot_consensus":{"full":[{"start":1,"end":100,"type":"T"},{"start":101,"end":406,"type":"D"}],"Structural state":[{"start":1,"end":406,"type":"D"}],"Molecular function":[{"start":1,"end":50,"type":"F"}],"Structural transition":[{"start":1,"end":100,"type":"T"}]}},{"acc":"O55778","sequence":"MDKLDLVNDGLDIIDFIQKNQKEIQKTYGRSSIQQPSTKDRTRAWEDFLQSTSGEHEQAEGGMPKNDGGTEGRNVEDLSSVTSSDGTIGQRVSNTRAWAEDPDDIQLDPMVTDVVYHDHGGECTGHGPSSSPERGWSYHMSGTHDGNVRAVPDTKVLPNAPKTTVPEEVREIDLIGLEDKFASAGLNPAAVPFVPKNQSTPTEEPPVIPEYYYGSGRRGDLSKSPPRGNVNLDSIKIYTSDDEDENQLEYEDEFAKSSSEVVIDTTPEDNDSINQEEVVGDPSDQGLEHPFPLGKFPEKEETPDVRRKDSLMQDSCKRGGVPKRLPMLSEEFECSGSDDPIIQELEREGSHPGGSLRLREPPQSSGNSRNQPDRQLKTGDAASPGGVQRPGTPMPKSRIMPIKKGTDAKSQYVGTEDVPGSKSGATRYVRGLPPNQESKSVTAENVQLSAPSAVTRNEGHDQEVTSNEDSLDDKYIMPSDDFANTFLPHDTDRLNYHADHLNDYDLETLCEESVLMGIVNAIKLINIDMRLNHIEEQMKEIPKIINKIDSIDRVLAKTNTALSTIEGHLVSMMIMIPGKGKGERKGKTNPELKPVIGRNILEQQELFSFDNLKNFRDGSLTDEPYGGVARIRDDLILPELNFSETNASQFVPLADDASKDVVRTMIRTHIKDRELRSELMDYLNRAETDEEVQEVANTVNDIIDGNI","creator":"tlazar","dataset":["Viral proteins","Condensates-related proteins"],"date":"2016-09-02T17:39:51.000Z","disprot_id":"DP00700","features":{"pfam":[{"id":"PF03210","name":"Paramyxovirus P/V phosphoprotein C-terminal","start":532,"end":699},{"id":"PF13825","name":"Paramyxovirus structural protein V/P N-terminus","start":393,"end":455},{"id":"PF14313","name":"N-terminal region of Paramyxovirinae phosphoprotein (P)","start":5,"end":51},{"id":"PF14320","name":"Phosphoprotein P region PNT disordered","start":71,"end":381}],"gene3D":[{"start":652,"end":707,"id":"1.10.8.10","name":"DNA helicase RuvA subunit, C-terminal domain","_id":"685af523b4ac24d5329d8472"}]},"genes":[{"name":{"value":"P/V/C","evidences":[],"_id":"685af523b4ac24d5329d84c9"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d84c8"}],"length":707,"name":"Phosphoprotein","ncbi_taxon_id":928303,"organism":"Hendra virus (isolate Horse/Autralia/Hendra/1994)","regions_counter":29,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Paramyxoviridae","Orthoparamyxovirinae","Henipavirus"],"UniParc":"UPI00000ECDA8","uniref100":"UniRef100_O55778","uniref50":"UniRef50_Q9IK91","uniref90":"UniRef90_O55778","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":404,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00700r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In further support of the absence of an ordered structure, the far-UV CD spectra of Henipavirus PNT and NTAIL at neutral pH are typical of unstructured proteins, as seen from their large negative ellipticity at 198 nm and low ellipticity at 190 nm (Fig. 7A). However, the observed ellipticity values at 200 and 222 nm of Henipavirus NTAIL and of NiV PNT are consistent with the existence of some residual secondary structure, as observed in IDPs adopting a PMG conformation (Fig. 7B).","_id":"685af523b4ac24d5329d8474"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-04T11:41:19.495Z","_id":"685af523b4ac24d5329d8475"},"version":3,"_id":"685af523b4ac24d5329d8473","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007064","ec_name":"dynamic light scattering assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":404,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00700r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The obtained RS values (37±2 Å for both NTAIL proteins, and either 55±2 Å or 57±2 Å for NiV and HeV PNT, respectively) highlight a significant increase in the hydrodynamic radius in the presence of urea (see Table 1). These results argue for the presence of residual intramolecular interactions within Henipavirus PNT and NTAIL proteins under native conditions, as expected for proteins adopting a PMG conformation.","_id":"685af523b4ac24d5329d847b"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-04T11:40:39.411Z","_id":"685af523b4ac24d5329d847c"},"version":3,"_id":"685af523b4ac24d5329d847a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006198","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":404,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00700r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The very small spread of the resonance frequencies for amide protons (between 7.8 ppm and 8.7 ppm, see frames in Fig. 6) together with the scarcity of NOEs in the amide-amide region are typical of proteins without any stable secondary structure (for examples see [6], [18]), thereby supporting lack of a packed core within Henipavirus PNT and NTAIL domains.","_id":"685af523b4ac24d5329d8482"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-04T11:40:19.627Z","_id":"685af523b4ac24d5329d8483"},"version":3,"_id":"685af523b4ac24d5329d8481","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":404,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00700r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"This abnormal behavior is therefore likely to be ascribed to a rather high content of acidic residues, as already been observed in the case of the intrinsically disordered MeV PNT [18] and NTAIL domains [6], [19], and, more generally, in other IDPs [46].","_id":"685af523b4ac24d5329d8489"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-04T11:40:08.869Z","_id":"685af523b4ac24d5329d848a"},"version":3,"_id":"685af523b4ac24d5329d8488","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":404,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00700r016","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"These studies suggest that Henipavirus PNT and NTAIL proteins either adopt a PMG conformation or are folded trimers.","_id":"685af523b4ac24d5329d8496"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-04T11:40:01.810Z","_id":"685af523b4ac24d5329d8497"},"version":3,"_id":"685af523b4ac24d5329d8495","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":404,"interaction_partner":[],"reference_html":"Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment. <i> Habchi J, Mamelli L, Darbon H, Longhi S. </i> PLoS One, 2010","reference_id":"20657787","region_id":"DP00700r019","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Henipavirus PNT and NTAIL were found to be highly sensitive to proteolysis, a property that constitutes a hallmark of structural disorder (see [47] and references therein cited).","_id":"685af523b4ac24d5329d849d"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-04T11:39:19.289Z","_id":"685af523b4ac24d5329d849e"},"version":1,"_id":"685af523b4ac24d5329d849c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":200,"end":310,"interaction_partner":[],"reference_html":"Identification of a Region in the Common Amino-terminal Domain of Hendra Virus P, V, and W Proteins Responsible for Phase Transition and Amyloid Formation. <i> Salladini E, Gondelaud F, Nilsson JF, Pesce G, Bignon C, Murrali MG, Fabre R, Pierattelli R, Kajava AV, Horvat B, Gerlier D, Mathieu C, Longhi S. </i> Biomolecules, 2021","reference_id":"34572537","region_id":"DP00700r021","released":"2022_03","sample":[],"statement":[{"type":"Results","text":" The CD spectrum of a freshly purified sample of PNT3 was typical of an IDP, as illustrated by the very pronounced negative peak at 200 nm and low ellipticity in the 190–200 nm region (Figure 5).","_id":"685af523b4ac24d5329d84a3"},{"type":"Curator statement","text":"Henipavirus phosphoprotein PNT3 region is comprised within the residues 200-310.","_id":"685af523b4ac24d5329d84a4"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-04T11:37:29.200Z","_id":"685af523b4ac24d5329d84a5"},"version":1,"_id":"685af523b4ac24d5329d84a2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006003","ec_name":"electron microscopy evidence used in manual assertion","ec_ontology":"ECO","start":200,"end":310,"interaction_partner":[],"reference_html":"Identification of a Region in the Common Amino-terminal Domain of Hendra Virus P, V, and W Proteins Responsible for Phase Transition and Amyloid Formation. <i> Salladini E, Gondelaud F, Nilsson JF, Pesce G, Bignon C, Murrali MG, Fabre R, Pierattelli R, Kajava AV, Horvat B, Gerlier D, Mathieu C, Longhi S. </i> Biomolecules, 2021","reference_id":"34572537","region_id":"DP00700r022","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Negative staining transmission electron microscopy (TEM) unequivocally confirmed the presence of amyloid-like fibrils (Figure 4D).","_id":"685af523b4ac24d5329d84a7"}],"states_connection":[],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_id":"GO:1990000","term_is_binding":false,"term_is_obsolete":false,"term_name":"amyloid fibril formation","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-04T11:42:03.706Z","_id":"685af523b4ac24d5329d84a8"},"version":1,"_id":"685af523b4ac24d5329d84a6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":200,"end":310,"interaction_partner":[],"reference_html":"Identification of a Region in the Common Amino-terminal Domain of Hendra Virus P, V, and W Proteins Responsible for Phase Transition and Amyloid Formation. <i> Salladini E, Gondelaud F, Nilsson JF, Pesce G, Bignon C, Murrali MG, Fabre R, Pierattelli R, Kajava AV, Horvat B, Gerlier D, Mathieu C, Longhi S. </i> Biomolecules, 2021","reference_id":"34572537","region_id":"DP00700r023","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"At 2 mg mL−1 (132 μM), the calculated radii of gyration (Rg) obtained after 1 h (Rg = 3.34 ± 0.1 nm) and 1.5 h (Rg = 3.01 ± 0.08 nm) of incubation are consistent with the value expected for a monomeric form of PNT3 in a disordered state according to Flory’s equation (Rg = 3.26 ± 0.03 nm) [58].","_id":"685af523b4ac24d5329d84aa"},{"type":"Results","text":"The distribution of the maximum particle sizes (Dmax) of the selected ensemble ranges from ~50 to 200 Å, centered on ~100 Å (Figure S3D). The selected ensemble exhibits a high flexibility (Rflex = 88.4 %), a value similar to that of the initial pool (87.2%, Rσ = 1.04) and consistent with pure random-coil conformations.","_id":"685af523b4ac24d5329d84ab"},{"type":"Curator statement","text":"Henipavirus phosphoprotein PNT3 region is comprised within the residues 200-310.","_id":"685af523b4ac24d5329d84ac"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-04T11:37:20.907Z","_id":"685af523b4ac24d5329d84ad"},"version":1,"_id":"685af523b4ac24d5329d84a9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":200,"end":310,"interaction_partner":[],"reference_html":"Identification of a Region in the Common Amino-terminal Domain of Hendra Virus P, V, and W Proteins Responsible for Phase Transition and Amyloid Formation. <i> Salladini E, Gondelaud F, Nilsson JF, Pesce G, Bignon C, Murrali MG, Fabre R, Pierattelli R, Kajava AV, Horvat B, Gerlier D, Mathieu C, Longhi S. </i> Biomolecules, 2021","reference_id":"34572537","region_id":"DP00700r024","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"After 2 h of incubation, higher order oligomers/aggregates dominated, as judged from the intensity increase in the low-angle region of the scattering curves (Figure 6A) and from the shape of the total scattered intensities plots (Figure 6B).","_id":"685af523b4ac24d5329d84af"},{"type":"Results","text":"In conclusion, SAXS experiments show that PNT3 was monomeric and disordered in the solution, adopting a typical Gaussian chain distribution of its parameters. However, it rapidly aggregates in a concentration-dependent manner to form rod-like particles, a behavior compatible with the formation of fibrillar species.","_id":"685af523b4ac24d5329d84b0"},{"type":"Curator statement","text":"Henipavirus phosphoprotein PNT3 region is comprised within the residues 200-310.","_id":"685af523b4ac24d5329d84b1"}],"states_connection":[],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_id":"GO:1990000","term_is_binding":false,"term_is_obsolete":false,"term_name":"amyloid fibril formation","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-04T11:41:52.339Z","_id":"685af523b4ac24d5329d84b2"},"version":1,"_id":"685af523b4ac24d5329d84ae","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007157","ec_name":"cell staining evidence used in manual assertion","ec_ontology":"ECO","start":200,"end":310,"interaction_partner":[],"reference_html":"Identification of a Region in the Common Amino-terminal Domain of Hendra Virus P, V, and W Proteins Responsible for Phase Transition and Amyloid Formation. <i> Salladini E, Gondelaud F, Nilsson JF, Pesce G, Bignon C, Murrali MG, Fabre R, Pierattelli R, Kajava AV, Horvat B, Gerlier D, Mathieu C, Longhi S. </i> Biomolecules, 2021","reference_id":"34572537","region_id":"DP00700r025","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"CR-staining experiments showed that cells transfected to express PNT3 capture CR more than cells transfected with an empty vector (Figure 11), providing clues about the formation of PNT3 fibrils also in a cellular context. ","_id":"685af523b4ac24d5329d84b4"},{"type":"Curator statement","text":"Henipavirus phosphoprotein PNT3 region is comprised within the residues 200-310.","_id":"685af523b4ac24d5329d84b5"}],"states_connection":[],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_id":"GO:1990000","term_is_binding":false,"term_is_obsolete":false,"term_name":"amyloid fibril formation","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-04T11:41:40.806Z","_id":"685af523b4ac24d5329d84b6"},"version":1,"_id":"685af523b4ac24d5329d84b3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006067","ec_name":"fluorescence recovery after photobleaching evidence used in manual assertion","ec_ontology":"ECO","start":200,"end":310,"interaction_partner":[],"reference_html":"Identification of a Region in the Common Amino-terminal Domain of Hendra Virus P, V, and W Proteins Responsible for Phase Transition and Amyloid Formation. <i> Salladini E, Gondelaud F, Nilsson JF, Pesce G, Bignon C, Murrali MG, Fabre R, Pierattelli R, Kajava AV, Horvat B, Gerlier D, Mathieu C, Longhi S. </i> Biomolecules, 2021","reference_id":"34572537","region_id":"DP00700r026","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"These experiments, beyond shedding light onto the nature of the PNT3 condensates, also confirmed the ability of PNT3 to phase separate in the absence of crowding agents and revealed that the process takes place even in the sub-micromolar concentration range, although a prolonged incubation period at 37 °C was required.","_id":"685af523b4ac24d5329d84b8"},{"type":"Discussion","text":"PNT3 was shown to phase-separate in vitro into solid-like condensates, as shown by FRAP.","_id":"685af523b4ac24d5329d84b9"},{"type":"Curator statement","text":"Henipavirus phosphoprotein PNT3 region is comprised within the residues 200-310.","_id":"685af523b4ac24d5329d84ba"}],"states_connection":[],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_id":"GO:1990000","term_is_binding":false,"term_is_obsolete":false,"term_name":"amyloid fibril formation","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-04T11:41:32.146Z","_id":"685af523b4ac24d5329d84bb"},"version":1,"_id":"685af523b4ac24d5329d84b7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","date":"2022-04-25T09:13:19.099Z","disprot_namespace":"Structural state","ec_id":"ECO:0001184","ec_name":"gel-filtration evidence used in manual assertion","ec_ontology":"ECO","start":300,"end":406,"interaction_partner":[],"reference_html":"Distribution of Charged Residues Affects the Average Size and Shape of Intrinsically Disordered Proteins. <i> Bianchi G, Mangiagalli M, Barbiroli A, Longhi S, Grandori R, Santambrogio C, Brocca S. </i> Biomolecules, 2022","reference_id":"35454150","region_id":"DP00700r027","released":"2022_06","sample":[],"statement":[{"type":"Results","text":"Size-exclusion chromatography was employed to estimate the Rh values of the three sets of model IDPs (Table 2). Experimental Rh values of wt NTAIL and wt PNT4 (2.71 ± 0.09 and 2.34 ± 0.11 nm, respectively) are close to the theoretical ones (Table 1) and similar to the previously determined ones [9].","_id":"685af523b4ac24d5329d84bd"},{"type":"Curator statement","text":"Experimentally determined Rh matches the theoretical Rh for IDPs [Marsh & Forman-Kay, 2010].","_id":"685af523b4ac24d5329d84be"},{"type":"Table","text":"Rt (nm) = 2.54","_id":"685af523b4ac24d5329d84bf"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2022-04-28T13:32:24.458Z","_id":"685af523b4ac24d5329d84c0"},"version":0,"_id":"685af523b4ac24d5329d84bc","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","date":"2022-04-25T09:13:25.932Z","disprot_namespace":"Structural state","ec_id":"ECO:0006283","ec_name":"electrospray ionization fourier transform ion cyclotron resonance mass spectrometry evidence used in manual assertion","ec_ontology":"ECO","start":300,"end":406,"interaction_partner":[],"reference_html":"Distribution of Charged Residues Affects the Average Size and Shape of Intrinsically Disordered Proteins. <i> Bianchi G, Mangiagalli M, Barbiroli A, Longhi S, Grandori R, Santambrogio C, Brocca S. </i> Biomolecules, 2022","reference_id":"35454150","region_id":"DP00700r028","released":"2022_06","sample":[],"statement":[{"type":"Results","text":"Native MS was employed to assess the conformational properties of the three sets of IDPs. In this approach, the CSDs resulting from the nanoESI process reflect the overall compactness and relative amounts of the main conformers in the original solution [17,18,22]. Native-MS spectra obtained under non-denaturing conditions for the three variants of NTAIL (Figure 4a), NFM, and PNT4 (Figure S3) display multimodal CSDs, highlighting the heterogeneous conformational ensemble typical of IDPs.","_id":"685af523b4ac24d5329d84c2"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2022-04-28T13:32:23.224Z","_id":"685af523b4ac24d5329d84c3"},"version":0,"_id":"685af523b4ac24d5329d84c1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","date":"2022-04-25T09:13:44.387Z","disprot_namespace":"Structural state","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":300,"end":406,"interaction_partner":[],"reference_html":"Distribution of Charged Residues Affects the Average Size and Shape of Intrinsically Disordered Proteins. <i> Bianchi G, Mangiagalli M, Barbiroli A, Longhi S, Grandori R, Santambrogio C, Brocca S. </i> Biomolecules, 2022","reference_id":"35454150","region_id":"DP00700r029","released":"2022_06","sample":[],"statement":[{"type":"Supplementary material","text":"Figure S2. Far-UV CD spectra of model IDPs. CD spectra of NTAIL (a), NFM (b), and PNT4 (c) variants.","_id":"685af523b4ac24d5329d84c5"},{"type":"Curator statement","text":"Typical random coil-like far-UV CD spectrum is displayed for PNT4.","_id":"685af523b4ac24d5329d84c6"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2022-04-28T13:32:21.593Z","_id":"685af523b4ac24d5329d84c7"},"version":0,"_id":"685af523b4ac24d5329d84c4","reference_source":"pmid"}],"__v":0,"disorder_content":0.5742574257425742,"disprot_consensus":{"full":[{"start":1,"end":406,"type":"D"}],"Structural state":[{"start":1,"end":406,"type":"D"}],"Biological process":[{"start":200,"end":310,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00397","name":"WW domain","start":173,"end":202},{"id":"PF00397","name":"WW domain","start":232,"end":261},{"id":"PF15238","name":"Omega loop, TEAD interacting region 3","start":84,"end":99}],"gene3D":[{"start":161,"end":209,"id":"2.20.70.10","name":"2.20.70.10"},{"start":224,"end":264,"id":"2.20.70.10","name":"2.20.70.10"}]},"uniref50":"UniRef50_P46937","sequence":"MDPGQQPPPQPAPQGQGQPPSQPPQGQGPPSGPGQPAPAATQAAPQAPPAGHQIVHVRGDSETDLEALFNAVMNPKTANVPQTVPMRLRKLPDSFFKPPEPKSHSRQASTDAGTAGALTPQHVRAHSSPASLQLGAVSPGTLTPTGVVSGPAATPTAQHLRQSSFEIPDDVPLPAGWEMAKTSSGQRYFLNHIDQTTTWQDPRKAMLSQMNVTAPTSPPVQQNMMNSASGPLPDGWEQAMTQDGEIYYINHKNKTTSWLDPRLDPRFAMNQRISQSAPVKQPPPLAPQSPQGGVMGGSNSNQQQQMRLQQLQMEKERLRLKQQELLRQAMRNINPSTANSPKCQELALRSQLPTLEQDGGTQNPVSSPGMSQELRTMTTNSSDPFLNSGTYHSRDESTDSGLSMSSYSVPRTPDDFLNSVDEMDTGDTINQSTLPSQQNRFPDYLEAIPGTNVDLGTLEGDGMNIEGEELMPSLQEALSSDILNDMESVLAATKLDKESFLTWL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P46937","disprot_id":"DP00702","ncbi_taxon_id":9606,"regions_counter":9,"creator":"eficho","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":171,"region_id":"DP00702r001","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Structural insights into the YAP and TEAD complex. <i> Li Z, Zhao B, Wang P, Chen F, Dong Z, Yang H, Guan KL, Xu Y. </i> Genes Dev, 2010","term_id":"IDPO:0000002","curator_id":"maspromonte","start":101,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2023-06-22T09:47:49.299Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3KYS"}],"reference_id":"20123905","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P28347"}],"statement":[{"text":"There is no electron density for residues 230–238 of TEAD and residues 101–171 of YAP, and therefore these were not built in the model.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-23T13:50:43.230Z"}},{"start":50,"end":171,"reference_id":"29372459","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>13</sup>C, <sup>15</sup>N resonance assignment of human YAP 50-171 fragment. <i> Feichtinger M, Sára T, Platzer G, Mateos B, Bokhovchuk F, Chène P, Konrat R. </i> Biomol NMR Assign, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"BMRB","id":"27290"}],"region_id":"DP00702r008","statement":[{"text":"The very narrow peak dispersion in the 1H dimension of the 1H–15N HSQC spectrum shows that YAP 50–171 is intrinsically disordered.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-05T09:25:03.327Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P46937","date":"2016-09-07T22:34:37.000Z","acc":"P46937","name":"Transcriptional coactivator YAP1","length":504,"organism":"Homo sapiens","dataset":["NDDs-related proteins","Condensates-related proteins"],"UniParc":"UPI000013A141","genes":[{"name":{"value":"YAP1"},"synonyms":[{"value":"YAP65"}]}],"alphafold_very_low_content":0.4523809523809524,"disorder_content":0.24206349206349206,"disprot_consensus":{"full":[{"start":50,"end":171,"type":"D"}],"Structural state":[{"start":50,"end":171,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01248","name":"Ribosomal protein L7Ae/L30e/S12e/Gadd45 family","start":21,"end":116}],"gene3D":[{"start":1,"end":165,"id":"3.30.1330.30","name":"3.30.1330.30"}]},"uniref50":"UniRef50_P24522","sequence":"MTLEEFSAGEQKTERMDKVGDALEEVLSKALSQRTITVGVYEAAKLLNVDPDNVVLCLLAADEDDDRDVALQIHFTLIQAFCCENDINILRVSNPGRLAELLLLETDAGPAASEGAEQPPDLHCVLVTNPHSSQWKDPALSQLICFCRESRYMDQWVPVINLPER","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P24522","disprot_id":"DP00704","ncbi_taxon_id":9606,"regions_counter":6,"creator":"ameszaros","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":16,"region_id":"DP00704r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase. <i> Sánchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"ameszaros","start":1,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"20460379","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2KG4"}],"term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":16,"region_id":"DP00704r002","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase. <i> Sánchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"ameszaros","start":1,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"20460379","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":118,"region_id":"DP00704r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase. <i> Sánchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"ameszaros","start":105,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"20460379","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2KG4"}],"term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":118,"term_name":"molecular function regulator","start":105,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ameszaros","released":"2022_03","term_ontology":"GO","curator_name":"Attila Meszaros","reference_id":"20460379","version":3,"reference_html":"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase. <i> Sánchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006165","region_id":"DP00704r004","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":118,"term_name":"protein binding","start":105,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ameszaros","released":"2022_03","term_ontology":"GO","curator_name":"Attila Meszaros","reference_id":"20460379","version":3,"reference_html":"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase. <i> Sánchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00704r005","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":118,"region_id":"DP00704r006","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase. <i> Sánchez R, Pantoja-Uceda D, Prieto J, Diercks T, Marcaida MJ, Montoya G, Campos-Olivas R, Blanco FJ. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"ameszaros","start":105,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"20460379","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P24522","date":"2016-09-17T23:27:19.000Z","acc":"P24522","name":"Growth arrest and DNA damage-inducible protein GADD45 alpha","length":165,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012AF8C","genes":[{"name":{"value":"GADD45A"},"synonyms":[{"value":"DDIT1"},{"value":"GADD45"}]}],"alphafold_very_low_content":0.08484848484848485,"disorder_content":0.18181818181818182,"disprot_consensus":{"full":[{"start":1,"end":16,"type":"D"},{"start":105,"end":118,"type":"D"}],"Structural state":[{"start":1,"end":16,"type":"D"},{"start":105,"end":118,"type":"D"}],"Molecular function":[{"start":105,"end":118,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04119","name":"Heat shock protein 9/12","start":1,"end":59}],"gene3D":[{"start":1,"end":109,"id":"G3DSA:1.20.58.1260"}]},"uniref50":"UniRef50_P22943","sequence":"MSDAGRKGFGEKASEALKPDSQKSYAEQGKEYITDKADKVAGKVQPEDNKGVFQGVHDSAEKGKDNAEGQGESLADQARDYMGAAKSKLNDAVEYVSGRVHGEEDPTKK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P22943","disprot_id":"DP00705","ncbi_taxon_id":559292,"regions_counter":39,"creator":"bjuhasz","regions":[{"start":1,"end":109,"reference_id":"33485946","reference_source":"pmid","reference_html":"PiP<sub>2</sub> favors an α-helical structure of non-recombinant Hsp12 of Saccharomyces cerevisiae. <i> Léger A, Azouz M, Lecomte S, Dole F, Hocquellet A, Chaignepain S, Cabanne C. </i> Protein Expr Purif, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00705r023","statement":[{"text":"The apparent molecular mass of Hsp12 deduced from the gel was an overestimated value of 14 kDa (Fig. 2A). Hsp12 was also reported earlier to have an apparent mobility corresponding to a protein of 14.4 kDa [3]. IDPs are known to be unusually mobile on SDS-PAGE.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-16T16:14:38.538Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":1,"end":109,"reference_id":"33485946","reference_source":"pmid","reference_html":"PiP<sub>2</sub> favors an α-helical structure of non-recombinant Hsp12 of Saccharomyces cerevisiae. <i> Léger A, Azouz M, Lecomte S, Dole F, Hocquellet A, Chaignepain S, Cabanne C. </i> Protein Expr Purif, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00705r024","statement":[{"text":"For Hsp12, a large negative peak around 200 nm was found in aqueous solution (Fig. 4A). This curve was specific to the random coil structure corresponding to an unstructured protein in solution.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-16T16:22:27.378Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":109,"reference_id":"33485946","reference_source":"pmid","reference_html":"PiP<sub>2</sub> favors an α-helical structure of non-recombinant Hsp12 of Saccharomyces cerevisiae. <i> Léger A, Azouz M, Lecomte S, Dole F, Hocquellet A, Chaignepain S, Cabanne C. </i> Protein Expr Purif, 2021","date":"2022-03-08T15:42:35.385Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","released":"2022_03","version":4,"region_id":"DP00705r025","statement":[{"text":"To characterize the interaction between Hsp12 and phospholipids, ITC and DSC were performed (Fig. 5, Fig. 6). The negative peaks which appeared with each addition of protein showed an exothermic reaction and therefore an interaction between Hsp12 and liposomes (Fig. 5A)","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":false,"interaction_partner":[{"db":"ChEBI","id":"6506401","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-14T15:23:13.933Z"}},{"start":1,"end":109,"reference_id":"33485946","reference_source":"pmid","reference_html":"PiP<sub>2</sub> favors an α-helical structure of non-recombinant Hsp12 of Saccharomyces cerevisiae. <i> Léger A, Azouz M, Lecomte S, Dole F, Hocquellet A, Chaignepain S, Cabanne C. </i> Protein Expr Purif, 2021","date":"2022-03-08T15:42:15.260Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006232","ec_ontology":"ECO","ec_name":"differential scanning calorimetry evidence used in manual assertion","released":"2022_03","version":4,"region_id":"DP00705r026","statement":[{"text":"Thanks to DSC, temperature phase transition was measured at 38 °C with a peak area of 1441 μV/s for the liposome alone (Fig. 6). With Hsp12, a shift of +1 °C was observed indicating that the physicochemical properties of the phospholipid vesicle were changed. An increase in Tm is indicative of membrane rigidification. Moreover, with Hsp12, the peak area was lower (920 μV/s) indicating a change in enthalpy. This reflected a modification in the fatty acid chains, probably due to a partial insertion of Hsp12 in the hydrocarbon moiety. Hsp12 might therefore play a role in the stress‐induced remodeling of membrane lipids.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":false,"interaction_partner":[{"db":"ChEBI","id":"72999","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-14T15:22:48.695Z"}},{"start":1,"end":109,"reference_id":"22848679","reference_source":"pmid","reference_html":"NMR structure of Hsp12, a protein induced by and required for dietary restriction-induced lifespan extension in yeast. <i> Herbert AP, Riesen M, Bloxam L, Kosmidou E, Wareing BM, Johnson JR, Phelan MM, Pennington SR, Lian LY, Morgan A. </i> PLoS One, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"GO:0044183","term_name":"protein folding chaperone","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00705r027","statement":[{"text":"NMR analysis indicated that Hsp12 is monomeric and intrinsically unfolded in solution, but switches to a 4-helical conformation upon binding to membrane-mimetic SDS micelles. The structure of micelle-bound Hsp12 reported here is consistent with its recently proposed function as a membrane-stabilising 'lipid chaperone'. Taken together, our data suggest that DR-induced Hsp12 expression contributes to lifespan extension, possibly via membrane alterations","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-16T16:22:30.892Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":109,"reference_id":"22848679","reference_source":"pmid","reference_html":"NMR structure of Hsp12, a protein induced by and required for dietary restriction-induced lifespan extension in yeast. <i> Herbert AP, Riesen M, Bloxam L, Kosmidou E, Wareing BM, Johnson JR, Phelan MM, Pennington SR, Lian LY, Morgan A. </i> PLoS One, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"BMRB","id":"18523"}],"region_id":"DP00705r028","statement":[{"text":"The 15N-1H HSQC spectrum showed poor resonance dispersion in the proton dimension, which suggested that Hsp12 is intrinsically disordered in aqueous buffer (Fig. 3A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-16T16:25:07.491Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":109,"reference_id":"22848679","reference_source":"pmid","reference_html":"NMR structure of Hsp12, a protein induced by and required for dietary restriction-induced lifespan extension in yeast. <i> Herbert AP, Riesen M, Bloxam L, Kosmidou E, Wareing BM, Johnson JR, Phelan MM, Pennington SR, Lian LY, Morgan A. </i> PLoS One, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00705r029","statement":[{"text":"The 15N-1H HSQC spectra of Hsp12 showed a dose-dependent increase in dispersion in response to SDS, indicating that Hsp12 adopts a folded conformation upon micelle binding (Fig. 3B).\nConsistent with this, analysis of the assigned chemical shifts in Hsp12 using CSI [25] suggested that micelle binding induces the formation of four α-helices (Fig. 4G). These α-helices cover the majority of the polypeptide and comprise residues F9-A16 (Helix I), Q22-A41 (Helix II), V52-G63 (Helix III) and L74-E94 (Helix IV).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-16T16:27:01.192Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":1,"end":109,"reference_id":"20797624","reference_source":"pmid","reference_html":"Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. <i> Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. </i> Mol Cell, 2010","date":"2025-10-14T18:19:13.602Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0070370","term_name":"cellular heat acclimation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006049","ec_ontology":"ECO","ec_name":"genetic transformation evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"IMP","region_id":"DP00705r030","statement":[{"text":"We found that the deletion of HSP12 does not significantly affect growth at elevated temperatures (30°C or 37°C) and that it may cause a slight inhibition of growth at lower temperatures (8°C). However, a strong growth defect was observed when the cells were exposed to a short sublethal heat shock for 20 min at 58°C. The heat-shocked WT cells produced the same number of colony-forming units (cfu) as cultures maintained at 30°C. In contrast, the ΔHSP12 strain showed a drastic loss of viability after exposure to 58°C. This suggests that Hsp12 exhibits an important protective function under heat shock conditions.","type":"Results"}],"term_comment":"","term_def":"\"Any process that increases heat tolerance of a cell in response to high temperatures.\" [GOC:jp]","term_is_obsolete":false,"term_not_annotate":false,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":58}]},{"start":1,"end":109,"reference_id":"20797624","reference_source":"pmid","reference_html":"Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. <i> Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. </i> Mol Cell, 2010","date":"2025-10-14T18:19:27.467Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006979","term_name":"response to oxidative stress","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006049","ec_ontology":"ECO","ec_name":"genetic transformation evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"IMP","region_id":"DP00705r031","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":5,"db":"ChEBI","id":"16240","entry_name":null}],"statement":[{"text":"WT and mutant strains were grown in the presence of 5 mM H2O2. As in the case of the heat-shocked cells, H2O2 did not affect the growth of the WT strain, but the growth of the ΔHSP12 strain was impaired (Figure 1A).","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.\" [GOC:jl, PMID:12115731]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":109,"reference_id":"20797624","reference_source":"pmid","reference_html":"Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. <i> Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. </i> Mol Cell, 2010","date":"2025-10-14T18:19:03.284Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006970","term_name":"response to osmotic stress","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006049","ec_ontology":"ECO","ec_name":"genetic transformation evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"IMP","region_id":"DP00705r032","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":400,"db":"ChEBI","id":"26710","entry_name":null}],"statement":[{"text":"To further analyze the influence of Hsp12 on S. cerevisiae growth under stress conditions, we also determined growth under osmotic stress. In the deletion strain, growth was reduced in the presence of 0.4 M NaCl, whereas the growth of the WT strain was not affected (Figure 1A).","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":109,"reference_id":"20797624","reference_source":"pmid","reference_html":"Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. <i> Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. </i> Mol Cell, 2010","date":"2025-10-14T15:59:40.175Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0016020","term_name":"membrane","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"IEP","region_id":"DP00705r033","statement":[{"text":"Western blot analysis showed that Hsp12 is indeed expressed with increasing cell density. At low optical densities, during the early logarithmic growth phase, Hsp12 was exclusively detected in the cytosolic fraction. Further growth led to additional accumulation of Hsp12, first in the membrane and then in the cell wall fraction. This localization pattern suggests that the protein is present both in soluble and membrane-associated forms.","type":"Results"}],"term_comment":"","term_def":"\"A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.\" [GOC:dos, GOC:mah, ISBN:0815316194]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":109,"reference_id":"20797624","reference_source":"pmid","reference_html":"Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. <i> Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. </i> Mol Cell, 2010","date":"2025-10-14T15:59:21.408Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005829","term_name":"cytosol","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"IEP","region_id":"DP00705r034","statement":[{"text":"Western blot analysis showed that Hsp12 is indeed expressed with increasing cell density. At low optical densities, during the early logarithmic growth phase, Hsp12 was exclusively detected in the cytosolic fraction. Further growth led to additional accumulation of Hsp12, first in the membrane and then in the cell wall fraction. This localization pattern suggests that the protein is present both in soluble and membrane-associated forms.","type":"Results"}],"term_comment":"","term_def":"\"The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.\" [GOC:hjd, GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":109,"reference_id":"20797624","reference_source":"pmid","reference_html":"Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. <i> Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. </i> Mol Cell, 2010","date":"2026-06-10T17:27:09.549Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_12","version":1,"region_id":"DP00705r035","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"60723","entry_name":null}],"statement":[{"text":"When we analyzed the structure by circular dichroism (CD) spectroscopy in the far ultraviolet (UV) region, we found, much to our surprise, that the protein did not exhibit any detectable secondary structure, suggesting that the protein is completely unfolded in solution (Figure 2A). Because of its colocalization with membranes, we investigated the effects of lipids or lipid-like molecules on the structure of Hsp12. Strikingly, the presence of either dimyristoylphosphatidylglycerol (DMPG) or SDS resulted in a Far-UV CD spectrum resembling that of an α-helical protein (Figure 2A).","type":"Results"},{"text":"The highest α-helical content is reached at medium lengths of the fatty acid tail of the phospholipids (10.0 PG, 14.0 PG, or 16.0 PG) (Figure 2B inset); longer fatty acids resulted in a decrease in α-helical content of Hsp12 (18.0 PG).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":1,"end":109,"reference_id":"20797624","reference_source":"pmid","reference_html":"Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. <i> Welker S, Rudolph B, Frenzel E, Hagn F, Liebisch G, Schmitz G, Scheuring J, Kerth A, Blume A, Weinkauf S, Haslbeck M, Kessler H, Buchner J. </i> Mol Cell, 2010","date":"2025-10-14T16:07:11.935Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"60723","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00705r036","statement":[{"text":"When we analyzed the structure by circular dichroism (CD) spectroscopy in the far ultraviolet (UV) region, we found, much to our surprise, that the protein did not exhibit any detectable secondary structure, suggesting that the protein is completely unfolded in solution (Figure 2A). Because of its colocalization with membranes, we investigated the effects of lipids or lipid-like molecules on the structure of Hsp12. Strikingly, the presence of either dimyristoylphosphatidylglycerol (DMPG) or SDS resulted in a Far-UV CD spectrum resembling that of an α-helical protein (Figure 2A).","type":"Results"},{"text":"The highest α-helical content is reached at medium lengths of the fatty acid tail of the phospholipids (10.0 PG, 14.0 PG, or 16.0 PG) (Figure 2B inset); longer fatty acids resulted in a decrease in α-helical content of Hsp12 (18.0 PG).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":9,"end":18,"reference_id":"21998307","reference_source":"pmid","reference_html":"Structural characterization of Hsp12, the heat shock protein from Saccharomyces cerevisiae, in aqueous solution where it is intrinsically disordered and in detergent micelles where it is locally α-helical. <i> Singarapu KK, Tonelli M, Chow DC, Frederick RO, Westler WM, Markley JL. </i> J Biol Chem, 2011","date":"2026-06-10T17:27:25.660Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"not relevant","value":40,"statements":[{"type":"Methods","text":"The temperature of the sample was regulated at 25 °C for Hsp12 in aqueous solution and 40 °C for Hsp12 in the presence of 200 mm SDS (Hsp12_SDS) or 200 mm DPC (Hsp12_DPC). "}]}],"construct_alterations":[{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"We collected \n13\nC-resolved three-dimensional \n1\nH-\n1\nH NOESY and \n15\nN-resolved three-dimensional \n1\nH-\n1\nH NOESY data on 900 MHz for Hsp12_SDS and 600 MHz for Hsp12_DPC for deriving distance constraints.\n"}]}],"cross_refs":[{"db":"PDB","id":"2L9Q"}],"region_id":"DP00705r037","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":"not relevant","value":200,"db":"ChEBI","id":"8984","statements":[{"type":"Methods","text":"The temperature of the sample was regulated at 25 °C for Hsp12 in aqueous solution and 40 °C for Hsp12 in the presence of 200 mm SDS (Hsp12_SDS) or 200 mm DPC (Hsp12_DPC). "}],"entry_name":null}],"statement":[{"text":"Fig. 4 shows the four well defined α-helices consisting of residues Phe\n9\n-Lys\n18\n (αI), Tyr\n25\n-Gly\n42\n (αII), Gln\n54\n-Ser\n59\n (αIII), and Asp\n76\n-Val\n100\n (αIV).\n","type":"Results"},{"text":"Our extensive structural characterization of Hsp12 by NMR, CD, and paramagnetic relaxation experiments show that Hsp12 is intrinsically disordered in aqueous solution but folds to generate four local α-helices in the presence of SDS micelles or one local α-helix in the presence of DPC.","type":"Conclusion"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-10T17:27:28.352Z"}},{"start":25,"end":42,"reference_id":"21998307","reference_source":"pmid","reference_html":"Structural characterization of Hsp12, the heat shock protein from Saccharomyces cerevisiae, in aqueous solution where it is intrinsically disordered and in detergent micelles where it is locally α-helical. <i> Singarapu KK, Tonelli M, Chow DC, Frederick RO, Westler WM, Markley JL. </i> J Biol Chem, 2011","date":"2026-06-10T17:26:18.787Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"not relevant","value":40,"statements":[{"type":"Methods","text":"The temperature of the sample was regulated at 25 °C for Hsp12 in aqueous solution and 40 °C for Hsp12 in the presence of 200 mm SDS (Hsp12_SDS) or 200 mm DPC (Hsp12_DPC). "}]}],"construct_alterations":[{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"We collected \n13\nC-resolved three-dimensional \n1\nH-\n1\nH NOESY and \n15\nN-resolved three-dimensional \n1\nH-\n1\nH NOESY data on 900 MHz for Hsp12_SDS and 600 MHz for Hsp12_DPC for deriving distance constraints.\n"}]}],"cross_refs":[{"db":"PDB","id":"2L9Q"}],"region_id":"DP00705r038","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":"not relevant","value":200,"db":"ChEBI","id":"8984","statements":[{"type":"Methods","text":"The temperature of the sample was regulated at 25 °C for Hsp12 in aqueous solution and 40 °C for Hsp12 in the presence of 200 mm SDS (Hsp12_SDS) or 200 mm DPC (Hsp12_DPC). "}],"entry_name":null}],"statement":[{"text":"Fig. 4 shows the four well defined α-helices consisting of residues Phe\n9\n-Lys\n18\n (αI), Tyr\n25\n-Gly\n42\n (αII), Gln\n54\n-Ser\n59\n (αIII), and Asp\n76\n-Val\n100\n (αIV).\n","type":"Results"},{"text":"Our extensive structural characterization of Hsp12 by NMR, CD, and paramagnetic relaxation experiments show that Hsp12 is intrinsically disordered in aqueous solution but folds to generate four local α-helices in the presence of SDS micelles or one local α-helix in the presence of DPC.","type":"Conclusion"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-10T17:27:31.006Z"}},{"start":76,"end":100,"reference_id":"21998307","reference_source":"pmid","reference_html":"Structural characterization of Hsp12, the heat shock protein from Saccharomyces cerevisiae, in aqueous solution where it is intrinsically disordered and in detergent micelles where it is locally α-helical. <i> Singarapu KK, Tonelli M, Chow DC, Frederick RO, Westler WM, Markley JL. </i> J Biol Chem, 2011","date":"2026-06-10T17:25:16.835Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"not relevant","value":40,"statements":[{"type":"Methods","text":"The temperature of the sample was regulated at 25 °C for Hsp12 in aqueous solution and 40 °C for Hsp12 in the presence of 200 mm SDS (Hsp12_SDS) or 200 mm DPC (Hsp12_DPC). "}]}],"construct_alterations":[{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"We collected \n13\nC-resolved three-dimensional \n1\nH-\n1\nH NOESY and \n15\nN-resolved three-dimensional \n1\nH-\n1\nH NOESY data on 900 MHz for Hsp12_SDS and 600 MHz for Hsp12_DPC for deriving distance constraints.\n"}]}],"cross_refs":[{"db":"PDB","id":"2L9Q"},{"db":"PDB","id":"2LJL"}],"region_id":"DP00705r039","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":"not relevant","value":200,"db":"ChEBI","id":"8984","statements":[{"type":"Methods","text":"The temperature of the sample was regulated at 25 °C for Hsp12 in aqueous solution and 40 °C for Hsp12 in the presence of 200 mm SDS (Hsp12_SDS) or 200 mm DPC (Hsp12_DPC). "}],"entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":"not relevant","value":200,"db":"ChEBI","id":"78018","statements":[{"type":"Methods","text":"The temperature of the sample was regulated at 25 °C for Hsp12 in aqueous solution and 40 °C for Hsp12 in the presence of 200 mm SDS (Hsp12_SDS) or 200 mm DPC (Hsp12_DPC). "}],"entry_name":null}],"statement":[{"text":"Fig. 4 shows the four well defined α-helices consisting of residues Phe\n9\n-Lys\n18\n (αI), Tyr\n25\n-Gly\n42\n (αII), Gln\n54\n-Ser\n59\n (αIII), and Asp\n76\n-Val\n100\n (αIV).\n","type":"Results"},{"text":"Our extensive structural characterization of Hsp12 by NMR, CD, and paramagnetic relaxation experiments show that Hsp12 is intrinsically disordered in aqueous solution but folds to generate four local α-helices in the presence of SDS micelles or one local α-helix in the presence of DPC.","type":"Conclusion"},{"text":"In the presence of DPC, Hsp12 gained a single helix that is similar to helix αIV (Asp\n76\n-Val\n100\n). \n","type":"Results"},{"text":"The helix spanning residues Asp76 to Val100 is observed in both SDS and DPC environments. Although the protein was measured separately in the presence of these two compounds, I cannot annotate the transition of the same fragment twice in DisProt based solely on this difference; therefore, I recorded it as a single piece of evidence.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-10T17:25:25.726Z"}}],"released":"2016_10","uniref100":"UniRef100_P22943","date":"2016-08-24T17:10:46.000Z","acc":"P22943","name":"12 kDa heat shock protein","length":109,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":["Stress response proteins"],"UniParc":"UPI0000036C44","genes":[{"name":{"value":"HSP12"},"synonyms":[{"value":"GLP1"},{"value":"HOR5"}],"olnNames":[{"value":"YFL014W"}]}],"alphafold_very_low_content":0.09174311926605505,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":109,"type":"T"}],"Structural state":[{"start":1,"end":109,"type":"D"}],"Molecular function":[{"start":1,"end":109,"type":"F"}],"Structural transition":[{"start":1,"end":109,"type":"T"}],"Biological process":[{"start":1,"end":109,"type":"F"}],"Cellular component":[{"start":1,"end":109,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_Q15517","sequence":"MGSSRAPWMGRVGGHGMMALLLAGLLLPGTLAKSIGTFSDPCKDPTRITSPNDPCLTGKGDSSGFSSYSGSSSSGSSISSARSSGGGSSGSSSGSSIAQGGSAGSFKPGTGYSQVSYSSGSGSSLQGASGSSQLGSSSSHSGNSGSHSGSSSSHSSSSSSFQFSSSSFQVGNGSALPTNDNSYRGILNPSQPGQSSSSSQTFGVSSSGQSVSSNQRPCSSDIPDSPCSGGPIVSHSGPYIPSSHSVSGGQRPVVVVVDQHGSGAPGVVQGPPCSNGGLPGKPCPPITSVDKSYGGYEVVGGSSDSYLVPGMTYSKGKIYPVGYFTKENPVKGSPGVPSFAAGPPISEGKYFSSNPIIPSQSAASSAIAFQPVGTGGVQLCGGGSTGSKGPCSPSSSRVPSSSSISSSSGLPYHPCGSASQSPCSPPGTGSFSSSSSSQSSGKIILQPCGSKSSSSGHPCMSVSSLTLTGGPDGSPHPDPSAGAKPCGSSSAGKIPCRSIRDILAQVKPLGPQLADPEVFLPQGELLNSP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q15517","disprot_id":"DP00706","ncbi_taxon_id":9606,"regions_counter":7,"creator":"aschramm","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":171,"region_id":"DP00706r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"A new amyloidosis caused by fibrillar aggregates of mutated corneodesmosin. <i> Caubet C, Bousset L, Clemmensen O, Sourigues Y, Bygum A, Chavanas S, Coudane F, Hsu CY, Betz RC, Melki R, Simon M, Serre G. </i> FASEB J, 2010","term_id":"IDPO:0000002","curator_id":"esalladini","start":60,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"20448140","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"Soluble GST-GS was mainly helical, and freeGS was unstructured in solution as determined by CD measurements (Fig. 8E, F).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-18T12:40:51.837Z"}},{"start":60,"end":171,"reference_id":"20448140","reference_source":"pmid","reference_html":"A new amyloidosis caused by fibrillar aggregates of mutated corneodesmosin. <i> Caubet C, Bousset L, Clemmensen O, Sourigues Y, Bygum A, Chavanas S, Coudane F, Hsu CY, Betz RC, Melki R, Simon M, Serre G. </i> FASEB J, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00706r006","statement":[{"text":"In the presence of increasing concentrations of GST-GS, ThT exhibited a dose-dependent enhanced fluorescence emission at 482 nm, consistent with an amyloid-like nature of the fibrillar assemblies (Fig. 7A).","type":"Results"},{"text":"Moreover, fibrillar GST-GS binds CR, as shown by the spectral red shift observed in the CR absorption peak, and CR-stained GST-GS aggregates exhibited green yellow birefringence under polarized light, features considered characteristic of amyloid structures (Supplemental Fig. 1 A, B).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-18T12:40:50.935Z"}},{"start":60,"end":171,"reference_id":"20448140","reference_source":"pmid","reference_html":"A new amyloidosis caused by fibrillar aggregates of mutated corneodesmosin. <i> Caubet C, Bousset L, Clemmensen O, Sourigues Y, Bygum A, Chavanas S, Coudane F, Hsu CY, Betz RC, Melki R, Simon M, Serre G. </i> FASEB J, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00706r007","statement":[{"text":"The recorded FTIR spectrum of fibrillar GST-GS obtained after incubation of the polypeptide at 4°C for 30 d (Fig. 8A) was centered at 1637 cm−1 (Fig. 8D).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-18T12:40:51.226Z"}}],"released":"2016_10","uniref100":"UniRef100_Q15517","date":"2016-09-18T18:43:11.000Z","acc":"Q15517","name":"Corneodesmosin","length":529,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI0001D147B5","genes":[{"name":{"value":"CDSN"}}],"alphafold_very_low_content":0.8998109640831758,"disorder_content":0.21172022684310018,"disprot_consensus":{"full":[{"start":60,"end":171,"type":"D"}],"Structural state":[{"start":60,"end":171,"type":"D"}],"Biological process":[{"start":60,"end":171,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03344","name":"Daxx N-terminal Rassf1C-interacting domain","start":49,"end":145},{"id":"PF20920","name":"Death domain-associated protein 6, histone binding domain","start":296,"end":380}],"gene3D":[{"start":51,"end":144,"id":"1.10.8.810","name":"Daxx helical bundle domain"},{"start":178,"end":389,"id":"1.20.58.2170","name":"1.20.58.2170"}]},"uniref50":"UniRef50_Q9UER7","sequence":"MATANSIIVLDDDDEDEAAAQPGPSHPLPNAASPGAEAPSSSEPHGARGSSSSGGKKCYKLENEKLFEEFLELCKMQTADHPEVVPFLYNRQQRAHSLFLASAEFCNILSRVLSRARSRPAKLYVYINELCTVLKAHSAKKKLNLAPAATTSNEPSGNNPPTHLSLDPTNAENTASQSPRTRGSRRQIQRLEQLLALYVAEIRRLQEKELDLSELDDPDSAYLQEARLKRKLIRLFGRLCELKDCSSLTGRVIEQRIPYRGTRYPEVNRRIERLINKPGPDTFPDYGDVLRAVEKAAARHSLGLPRQQLQLMAQDAFRDVGIRLQERRHLDLIYNFGCHLTDDYRPGVDPALSDPVLARRLRENRSLAMSRLDEVISKYAMLQDKSEEGERKKRRARLQGTSSHSADTPEASLDSGEGPSGMASQGCPSASRAETDDEDDEESDEEEEEEEEEEEEEATDSEEEEDLEQMQEGQEDDEEEDEEEEAAAGKDGDKSPMSSLQISNEKNLEPGKQISRSSGEQQNKGRIVSPSLLSEEPLAPSSIDAESNGEQPEELTLEEESPVSQLFELEIEALPLDTPSSVETDISSSRKQSEEPFTTVLENGAGMVSSTSFNGGVSPHNWGDSGPPCKKSRKEKKQTGSGPLGNSYVERQRSVHEKNGKKICTLPSPPSPLASLAPVADSSTRVDSPSHGLVTSSLCIPSPARLSQTPHSQPPRPGTCKTSVATQCDPEEIIVLSDSD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UER7","disprot_id":"DP00707","ncbi_taxon_id":9606,"regions_counter":8,"creator":"bjuhasz","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":420,"region_id":"DP00707r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C. <i> Escobar-Cabrera E, Lau DK, Giovinazzi S, Ishov AM, McIntosh LP. </i> Structure, 2010","term_id":"IDPO:0000002","curator_id":"esalladini","start":347,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21134643","statement":[{"text":"In contrast, DAXX161-243 and DAXX347-420 appeared partially aggregated or mostly unfolded, respectively.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-15T07:52:43.513Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":740,"region_id":"DP00707r002","reference_id":"30244836","start":495,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"We assigned the NMR resonances of 15N,13C cDAXX (Figures S3A and S3B), which have the limited chemical shift dispersion and sharp line widths of a typical intrinsically disordered region (IDR) (Figure 3A","type":"Results"},{"text":"These spectral properties indicate that many cDAXX conformations are in fast exchange and that the IDR exhibits little structure.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"reference_html":"Cancer Mutations of the Tumor Suppressor SPOP Disrupt the Formation of Active, Phase-Separated Compartments. <i> Bouchard JJ, Otero JH, Scott DC, Szulc E, Martin EW, Sabri N, Granata D, Marzahn MR, Lindorff-Larsen K, Salvatella X, Schulman BA, Mittag T. </i> Mol Cell, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-29T10:54:16.268Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"O43791","partner_end":null}],"ec_ontology":"ECO","end":740,"region_id":"DP00707r003","reference_id":"30244836","start":495,"term_id":"GO:0005515","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"A titration of unlabeled SPOPMATH into 15N,13C cDAXX and monitored by CON spectra resulted in a dose-dependent loss of signal intensity along several cDAXX regions","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":4,"reference_html":"Cancer Mutations of the Tumor Suppressor SPOP Disrupt the Formation of Active, Phase-Separated Compartments. <i> Bouchard JJ, Otero JH, Scott DC, Szulc E, Martin EW, Sabri N, Granata D, Marzahn MR, Lindorff-Larsen K, Salvatella X, Schulman BA, Mittag T. </i> Mol Cell, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"protein binding","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-29T10:54:17.246Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":740,"region_id":"DP00707r004","reference_id":"30244836","start":495,"term_id":"GO:0140693","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"SPOP and DAXX localize to SPOP/DAXX bodies.","type":"Figure"},{"text":"SPOP and DAXX form nuclear bodies with liquid properties.","type":"Figure"},{"text":"DAXX and SPOP therefore both re-localized from their original subcellular location when expressed together. The SPOP/DAXX bodies possess liquid properties as evidenced by their ability to undergo fusion events within minutes (Fig. 1C, D, Supplemental Videos S1, S2). These properties place them into the category of liquid membraneless organelles.","type":"Results"},{"text":" It is clear from these observations that SPOP and DAXX not only bind to each other, but binding shifts them to a different liquid organelle.","type":"Results"},{"text":"This observation suggests that weak multivalent interactions between SPOP and DAXX result in a sol-gel transition coupled to phase separation, as defined by Harmon et al (Harmon et al., 2017).","type":"Results"}],"curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":5,"reference_html":"Cancer Mutations of the Tumor Suppressor SPOP Disrupt the Formation of Active, Phase-Separated Compartments. <i> Bouchard JJ, Otero JH, Scott DC, Szulc E, Martin EW, Sabri N, Granata D, Marzahn MR, Lindorff-Larsen K, Salvatella X, Schulman BA, Mittag T. </i> Mol Cell, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"molecular condensate scaffold activity","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-15T07:52:46.210Z"}},{"start":566,"end":739,"reference_id":"21134643","reference_source":"pmid","reference_html":"Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C. <i> Escobar-Cabrera E, Lau DK, Giovinazzi S, Ishov AM, McIntosh LP. </i> Structure, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00707r005","statement":[{"text":"The C-terminal fragment mDAXX566-739 had random coil 1HN shifts, indicating that indeed, as predicted, it is predominantly disordered.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-15T07:52:39.207Z"}},{"start":161,"end":243,"reference_id":"21134643","reference_source":"pmid","reference_html":"Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C. <i> Escobar-Cabrera E, Lau DK, Giovinazzi S, Ishov AM, McIntosh LP. </i> Structure, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00707r006","statement":[{"text":"In contrast, DAXX161-243 and DAXX347-420 appeared partially aggregated or mostly unfolded, respectively.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-15T07:52:37.672Z"}},{"start":435,"end":486,"reference_id":"https://mobidb.org/Q9UER7","reference_source":"mobidb","reference_html":"An Entry Referenced from MobiDB","date":"2022-02-14T09:00:00.000Z","curator_id":"amonzon","curator_name":"Alex Monzon","curator_orcid":"0000-0003-0362-8218","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007759","ec_ontology":"ECO","ec_name":"curator inference from database used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00707r007","statement":[{"text":"This poly-E region is inferred by the curator to be disordered, based on MobiDB-Lite and according to experimental evidence demonstrating that poly-E repeats display random-coil-like conformation (PMID:16949547)","type":"Curator statement"}],"ec_go":"IC","disprot_namespace":"Structural state"},{"start":1,"end":50,"reference_id":"21134643","reference_source":"pmid","reference_html":"Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C. <i> Escobar-Cabrera E, Lau DK, Giovinazzi S, Ishov AM, McIntosh LP. </i> Structure, 2010","date":"2023-12-11T09:26:54.726Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP00707r008","statement":[{"text":"In addition to the linker between these domains, the ~50 N-terminal and ~340 C-terminal residues of DAXX are predicted to be unstructured. The intrinsic disorder of these regions was confirmed by NMR analysis of DAXX 1-144 (not shown) and mDAXX566-739.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-11T19:41:57.627Z"}}],"released":"2016_10","uniref100":"UniRef100_Q9UER7","date":"2016-09-13T12:31:08.000Z","acc":"Q9UER7","name":"Death domain-associated protein 6","length":740,"organism":"Homo sapiens","dataset":["Condensates-related proteins","Cancer-related proteins"],"UniParc":"UPI0000169890","genes":[{"name":{"value":"DAXX"},"synonyms":[{"value":"BING2"},{"value":"DAP6"}]}],"alphafold_very_low_content":0.5486486486486486,"disorder_content":0.6824324324324325,"disprot_consensus":{"full":[{"start":1,"end":50,"type":"D"},{"start":161,"end":243,"type":"D"},{"start":347,"end":420,"type":"D"},{"start":435,"end":486,"type":"D"},{"start":495,"end":740,"type":"D"}],"Structural state":[{"start":1,"end":50,"type":"D"},{"start":161,"end":243,"type":"D"},{"start":347,"end":420,"type":"D"},{"start":435,"end":486,"type":"D"},{"start":495,"end":740,"type":"D"}],"Molecular function":[{"start":495,"end":740,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03344","name":"Daxx N-terminal Rassf1C-interacting domain","start":55,"end":151},{"id":"PF20920","name":"Death domain-associated protein 6, histone binding domain","start":302,"end":386}],"gene3D":[{"start":57,"end":150,"id":"1.10.8.810","name":"Daxx helical bundle domain"},{"start":184,"end":395,"id":"1.20.58.2170","name":"1.20.58.2170"}]},"uniref50":"UniRef50_Q9UER7","sequence":"MATDDSIIVLDDDDEDEAAAQPGPSNLPPNPASTGPGPGLSQQATGLSEPRVDGGSSNSGSRKCYKLDNEKLFEEFLELCKTETSDHPEVVPFLHKLQQRAQSVFLASAEFCNILSRVLARSRKRPAKIYVYINELCTVLKAHSIKKKLNLAPAASTTSEASGPNPPTEPPSDLTNTENTASEASRTRGSRRQIQRLEQLLALYVAEIRRLQEKELDLSELDDPDSSYLQEARLKRKLIRLFGRLCELKDCSSLTGRVIEQRIPYRGTRYPEVNRRIERLINKPGLDTFPDYGDVLRAVEKAATRHSLGLPRQQLQLLAQDAFRDVGVRLQERRHLDLIYNFGCHLTDDYRPGVDPALSDPTLARRLRENRTLAMNRLDEVISKYAMMQDKTEEGERQKRRARLLGTAPQPSDPPQASSESGEGPSGMASQECPTTSKAETDDDDDDDDDDDEDNEESEEEEEEEEEEKEATEDEDEDLEQLQEDQGGDEEEEGGDNEGNESPTSPSDFFHRRNSEPAEGLRTPEGQQKRGLTETPASPPGASLDPPSTDAESSGEQLLEPLLGDESPVSQLAELEMEALPEERDISSPRKKSEDSLPTILENGAAVVTSTSVNGRVSSHTWRDASPPSKRFRKEKKQLGSGLLGNSYIKEPMAQQDSGQNTSVQPMPSPPLASVASVADSSTRVDSPSHELVTSSLCSPSPSLLLQTPQAQSLRQCIYKTSVATQCDPEEIIVLSDSD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_O35613","disprot_id":"DP00708","ncbi_taxon_id":10090,"regions_counter":5,"creator":"bjuhasz","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":739,"region_id":"DP00708r001","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C. <i> Escobar-Cabrera E, Lau DK, Giovinazzi S, Ishov AM, McIntosh LP. </i> Structure, 2010","term_id":"IDPO:0000002","curator_id":"fquaglia","start":566,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21134643","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-12-11T09:23:19.900Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"In addition to the linker between these domains, the ~50 N-terminal and ~340 C-terminal residues of DAXX are predicted to be unstructured. The intrinsic disorder of these regions was confirmed by NMR analysis of DAXX 1-144 (not shown) and mDAXX566-739.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-11T20:38:09.045Z"}},{"start":441,"end":499,"reference_id":"https://mobidb.org/O35613","reference_source":"mobidb","reference_html":"An Entry Referenced from MobiDB","date":"2022-02-14T09:00:00.000Z","curator_id":"amonzon","curator_name":"Alex Monzon","curator_orcid":"0000-0003-0362-8218","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007759","ec_ontology":"ECO","ec_name":"curator inference from database used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00708r004","statement":[{"text":"\"This poly-E region is inferred by the curator to be disordered, based on MobiDB-Lite and according to experimental evidence demonstrating that poly-E repeats display random-coil-like conformation (PMID:16949547)\"","type":"Curator statement"}],"ec_go":"IC","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_O35613","date":"2016-08-30T16:29:08.000Z","acc":"O35613","name":"Death domain-associated protein 6","length":739,"organism":"Mus musculus","dataset":["Condensates-related proteins"],"UniParc":"UPI00000299C5","genes":[{"name":{"value":"Daxx"}}],"alphafold_very_low_content":0.5358592692828146,"disorder_content":0.3152909336941813,"disprot_consensus":{"full":[{"start":441,"end":499,"type":"D"},{"start":566,"end":739,"type":"D"}],"Structural state":[{"start":441,"end":499,"type":"D"},{"start":566,"end":739,"type":"D"}]}},{"features":{"pfam":[{"id":"PF14645","name":"Chibby family","start":2,"end":116}]},"uniref50":"UniRef50_Q9Y3M2","sequence":"MPFFGNTFSPKKTPPRKSASLSNLHSLDRSTREVELGLEYGSPTMNLAGQSLKFENGQWIAETGVSGGVDRREVQRLRRRNQQLEEENNLLRLKVDILLDMLSESTAESHLMEKELDELRISRKRK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9Y3M2","disprot_id":"DP00709","ncbi_taxon_id":9606,"regions_counter":38,"creator":"gerdos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":63,"region_id":"DP00709r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Structural characterization of partially disordered human Chibby: insights into its function in the Wnt-signaling pathway. <i> Mokhtarzada S, Yu C, Brickenden A, Choy WY. </i> Biochemistry, 2011","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"21182262","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-05-22T17:54:30.503Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The fact that the majority of peaks observed in the 1H−15N HSQC of N-Cby can essentially overlay with the peaks observed in the spectrum of full-length Cby (except for residues 50−63) suggests that at least a large portion of the N-terminal part of the protein is disordered and may not interact significantly with the C-terminal segment (Figure ​2b).","type":"Results"}]},{"term_namespace":"Biological process","reference_source":"pmid","ec_ontology":"ECO","end":63,"term_name":"negative regulation of protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"27082063","version":4,"reference_html":"Conformational characterization of the intrinsically disordered protein Chibby: Interplay between structural elements in target recognition. <i> Killoran RC, Sowole MA, Halim MA, Konermann L, Choy WY. </i> Protein Sci, 2016","date":"2023-05-22T18:24:21.361Z","term_id":"GO:0032091","ec_id":"ECO:0006165","region_id":"DP00709r002","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of protein binding.\" [GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true,"statement":[{"text":"The greater intensity losses observed in the TC-1 spectrum upon titration with C-Cby suggest that C-Cby binds TC-1 with a higher affinity than the full-length protein. This was confirmed by ITC experiments, which revealed that C-Cby binds to TC-1 with a Kd of ∼ 2 μM [Fig. 7(C), Supporting Information Fig. 3(A)].","type":"Results"},{"text":"Alternatively, the disordered N-terminus of Cby may inhibit the interaction by acting as an entropic bristle, that is, an unstructured region that impedes surrounding macromolecules via random, thermally driven motions.","type":"Discussion"}],"interaction_partner":[{"db":"UniProt","id":"Q9NR00","operator":null,"partner_start":null,"partner_end":null}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":63,"region_id":"DP00709r006","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Structural characterization of partially disordered human Chibby: insights into its function in the Wnt-signaling pathway. <i> Mokhtarzada S, Yu C, Brickenden A, Choy WY. </i> Biochemistry, 2011","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"21182262","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-05-22T17:57:45.760Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The disordered nature of N-Cby is also confirmed by CD spectropolarimetry. The CD spectrum of N-Cby (Figure 7b) displays a large and negative signal at 190 nm and negligible ellipticities at 208 and 222 nm, indicating that N-Cby is largely unstructured (48).","type":"Results"}]},{"term_namespace":"Biological process","reference_source":"pmid","ec_ontology":"ECO","end":63,"term_name":"negative regulation of protein binding","start":1,"ec_name":"isothermal titration calorimetry evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"27082063","version":4,"reference_html":"Conformational characterization of the intrinsically disordered protein Chibby: Interplay between structural elements in target recognition. <i> Killoran RC, Sowole MA, Halim MA, Konermann L, Choy WY. </i> Protein Sci, 2016","date":"2023-05-22T18:23:57.034Z","term_id":"GO:0032091","ec_id":"ECO:0005647","region_id":"DP00709r007","curator_orcid":"0000-0001-8399-7907","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of protein binding.\" [GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true,"statement":[{"text":"The greater intensity losses observed in the TC-1 spectrum upon titration with C-Cby suggest that C-Cby binds TC-1 with a higher affinity than the full-length protein. This was confirmed by ITC experiments, which revealed that C-Cby binds to TC-1 with a Kd of ∼ 2 μM [Fig. 7(C), Supporting Information Fig. 3(A)].","type":"Results"},{"text":"Alternatively, the disordered N-terminus of Cby may inhibit the interaction by acting as an entropic bristle, that is, an unstructured region that impedes surrounding macromolecules via random, thermally driven motions.","type":"Discussion"}],"interaction_partner":[{"db":"UniProt","id":"Q9NR00","operator":null,"partner_start":null,"partner_end":null}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":126,"region_id":"DP00709r021","released":"2023_06","ec_id":"ECO:0006236","reference_html":"Conformational characterization of the intrinsically disordered protein Chibby: Interplay between structural elements in target recognition. <i> Killoran RC, Sowole MA, Halim MA, Konermann L, Choy WY. </i> Protein Sci, 2016","term_id":"IDPO:0000002","curator_id":"vnugnes","start":102,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27082063","version":3,"ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","date":"2023-05-22T17:03:41.951Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Similarly, residues 102‐126, which make up the very C‐terminal end of Cby, exhibited extremely rapid deuterium uptake.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":126,"region_id":"DP00709r024","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Conformational characterization of the intrinsically disordered protein Chibby: Interplay between structural elements in target recognition. <i> Killoran RC, Sowole MA, Halim MA, Konermann L, Choy WY. </i> Protein Sci, 2016","term_id":"IDPO:0000002","curator_id":"vnugnes","start":102,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27082063","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-05-22T17:06:34.371Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The data indicate that the C‐terminal 20 residues are not structured and that the helical content of Cby is maintained upon deletion of this disordered extension. Notably, the CD spectrum of a synthetic construct comprising the C‐terminal 25 residues of Cby (CbyC25), shows that the C‐terminal extension is largely disordered but does have α‐helical propensity (deconvolution: 42% helical, 12% strand, and 46% turns/disordered) [Fig. ​4(C)].","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":126,"region_id":"DP00709r027","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Conformational characterization of the intrinsically disordered protein Chibby: Interplay between structural elements in target recognition. <i> Killoran RC, Sowole MA, Halim MA, Konermann L, Choy WY. </i> Protein Sci, 2016","term_id":"IDPO:0000002","curator_id":"vnugnes","start":102,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27082063","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-05-22T17:42:36.900Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Notably, truncation of the C‐terminal extension of Cby does not induce significant chemical shift changes or intensity attenuation to the signals originating from the N‐terminal half, indicating that there are no long‐range interactions between the N‐ and C‐terminal disordered regions of Cby.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":63,"region_id":"DP00709r030","released":"2023_06","ec_id":"ECO:0006236","reference_html":"Conformational characterization of the intrinsically disordered protein Chibby: Interplay between structural elements in target recognition. <i> Killoran RC, Sowole MA, Halim MA, Konermann L, Choy WY. </i> Protein Sci, 2016","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27082063","version":3,"ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","date":"2023-05-22T17:37:57.913Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Deuteration was quasi‐instantaneous for the N‐terminal half of Cby, that is, deuterium levels of >90% were observed already for the first experimental time point of 1 min.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":66,"region_id":"DP00709r033","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Conformational characterization of the intrinsically disordered protein Chibby: Interplay between structural elements in target recognition. <i> Killoran RC, Sowole MA, Halim MA, Konermann L, Choy WY. </i> Protein Sci, 2016","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27082063","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-05-22T17:47:10.965Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Deconvolution of the spectra using the DichroWeb software44 gives 30% helical, 21% strand, and 49% disordered/turn structure for the full‐length Cby and 41% helical, 17% strand, and 42% disordered/turn for CbyΔC20.","type":"Results"},{"text":"Next, we sought to characterize isolated C‐terminal half of Cby in the absence of the disordered N‐terminus. A CD spectrum reveals that C‐Cby (residues 67‐126) is largely helical [Fig. ​4(C)]. ","type":"Results"},{"text":"Circular dichroism spectra shows a large drop of the disordered percentage when the region 1-66 is deleted.","type":"Curator statement"}]}],"released":"2016_10","uniref100":"UniRef100_Q9Y3M2","date":"2016-09-13T13:54:59.000Z","acc":"Q9Y3M2","name":"Protein chibby homolog 1","length":126,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI0000128720","genes":[{"name":{"value":"CBY1"},"synonyms":[{"value":"ARB1"},{"value":"C22orf2"},{"value":"CBY"},{"value":"PGEA1"}],"orfNames":[{"value":"HRIHFB2025"}]}],"alphafold_very_low_content":0.007936507936507936,"disorder_content":0.7222222222222222,"disprot_consensus":{"full":[{"start":1,"end":66,"type":"D"},{"start":102,"end":126,"type":"D"}],"Structural state":[{"start":1,"end":66,"type":"D"},{"start":102,"end":126,"type":"D"}],"Biological process":[{"start":1,"end":63,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00628","name":"PHD-finger","start":312,"end":356},{"id":"PF00628","name":"PHD-finger","start":1179,"end":1221},{"id":"PF00628","name":"PHD-finger","start":1492,"end":1535},{"id":"PF01388","name":"ARID/BRIGHT DNA binding domain","start":100,"end":182},{"id":"PF02373","name":"JmjC domain, hydroxylase","start":486,"end":602},{"id":"PF02375","name":"jmjN domain","start":33,"end":66},{"id":"PF02928","name":"C5HC2 zinc finger","start":692,"end":744},{"id":"PF08429","name":"PLU-1-like protein","start":757,"end":1088},{"id":"PF21323","name":"Lysine-specific demethylase 5, C-terminal helical domain","start":606,"end":660}],"gene3D":[{"start":95,"end":198,"id":"1.10.150.60","name":"ARID DNA-binding domain"},{"start":1170,"end":1227,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":1484,"end":1544,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":339,"end":625,"id":"2.60.120.650","name":"Cupin"},{"start":32,"end":201,"id":"2.60.120.650","name":"Cupin"}]},"uniref50":"UniRef50_Q9UGL1","sequence":"MEAATTLHPGPRPALPLGGPGPLGEFLPPPECPVFEPSWEEFADPFAFIHKIRPIAEQTGICKVRPPPDWQPPFACDVDKLHFTPRIQRLNELEAQTRVKLNFLDQIAKYWELQGSTLKIPHVERKILDLFQLNKLVAEEGGFAVVCKDRKWTKIATKMGFAPGKAVGSHIRGHYERILNPYNLFLSGDSLRCLQKPNLTTDTKDKEYKPHDIPQRQSVQPSETCPPARRAKRMRAEAMNIKIEPEETTEARTHNLRRRMGCPTPKCENEKEMKSSIKQEPIERKDYIVENEKEKPKSRSKKATNAVDLYVCLLCGSGNDEDRLLLCDGCDDSYHTFCLIPPLHDVPKGDWRCPKCLAQECSKPQEAFGFEQAARDYTLRTFGEMADAFKSDYFNMPVHMVPTELVEKEFWRLVSTIEEDVTVEYGADIASKEFGSGFPVRDGKIKLSPEEEEYLDSGWNLNNMPVMEQSVLAHITADICGMKLPWLYVGMCFSSFCWHIEDHWSYSINYLHWGEPKTWYGVPGYAAEQLENVMKKLAPELFVSQPDLLHQLVTIMNPNTLMTHEVPVYRTNQCAGEFVITFPRAYHSGFNQGFNFAEAVNFCTVDWLPLGRQCVEHYRLLHRYCVFSHDEMICKMASKADVLDVVVASTVQKDMAIMIEDEKALRETVRKLGVIDSERMDFELLPDDERQCVKCKTTCFMSAISCSCKPGLLVCLHHVKELCSCPPYKYKLRYRYTLDDLYPMMNALKLRAESYNEWALNVNEALEAKINKKKSLVSFKALIEESEMKKFPDNDLLRHLRLVTQDAEKCASVAQQLLNGKRQTRYRSGGGKSQNQLTVNELRQFVTQLYALPCVLSQTPLLKDLLNRVEDFQQHSQKLLSEETPSAAELQDLLDVSFEFDVELPQLAEMRIRLEQARWLEEVQQACLDPSSLTLDDMRRLIDLGVGLAPYSAVEKAMARLQELLTVSEHWDDKAKSLLKARPRHSLNSLATAVKEIEEIPAYLPNGAALKDSVQRARDWLQDVEGLQAGGRVPVLDTLIELVTRGRSIPVHLNSLPRLETLVAEVQAWKECAVNTFLTENSPYSLLEVLCPRCDIGLLGLKRKQRKLKEPLPNGKKKSTKLESLSDLERALTESKETASAMATLGEARLREMEALQSLRLANEGKLLSPLQDVDIKICLCQKAPAAPMIQCELCRDAFHTSCVAVPSISQGLRIWLCPHCRRSEKPPLEKILPLLASLQRIRVRLPEGDALRYMIERTVNWQHRAQQLLSSGNLKFVQDRVGSGLLYSRWQASAGQVSDTNKVSQPPGTTSFSLPDDWDNRTSYLHSPFSTGRSCIPLHGVSPEVNELLMEAQLLQVSLPEIQELYQTLLAKPSPAQQTDRSSPVRPSSEKNDCCRGKRDGINSLERKLKRRLEREGLSSERWERVKKMRTPKKKKIKLSHPKDMNNFKLERERSYELVRSAETHSLPSDTSYSEQEDSEDEDAICPAVSCLQPEGDEVDWVQCDGSCNQWFHQVCVGVSPEMAEKEDYICVRCTVKDAPSRK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UGL1","disprot_id":"DP00712","ncbi_taxon_id":9606,"regions_counter":17,"creator":"eleonardi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":129,"region_id":"DP00712r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"The flexible loop L1 of the H3K4 demethylase JARID1B ARID domain has a crucial role in DNA-binding activity. <i> Yao W, Peng Y, Lin D. </i> Biochem Biophys Res Commun, 2010","term_id":"IDPO:0000002","curator_id":"vnugnes","start":115,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"20403335","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-05-18T13:54:20.314Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Perturbations to 1H–15N correlation spectra revealed that the flexible loop L1 of ARID was the main DNA-binding interface.","type":"Abstract"},{"text":"The flexible loop L1 makes a major contribution to the protein–DNA interaction.","type":"Results"}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":129,"term_name":"nucleic acid binding","start":115,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"20403335","version":4,"reference_html":"The flexible loop L1 of the H3K4 demethylase JARID1B ARID domain has a crucial role in DNA-binding activity. <i> Yao W, Peng Y, Lin D. </i> Biochem Biophys Res Commun, 2010","date":"2023-05-18T13:56:06.857Z","term_id":"GO:0003676","ec_id":"ECO:0006165","region_id":"DP00712r002","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"statement":[{"text":"Perturbations to 1H–15N correlation spectra revealed that the flexible loop L1 of ARID was the main DNA-binding interface.","type":"Abstract"},{"text":"The flexible loop L1 makes a major contribution to the protein–DNA interaction.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":199,"region_id":"DP00712r005","released":"2023_06","ec_id":"ECO:0006165","reference_html":"The flexible loop L1 of the H3K4 demethylase JARID1B ARID domain has a crucial role in DNA-binding activity. <i> Yao W, Peng Y, Lin D. </i> Biochem Biophys Res Commun, 2010","term_id":"IDPO:0000002","curator_id":"vnugnes","start":188,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"20403335","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-05-18T14:29:08.339Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Like other ARIDs, the human JARID1B ARID domain also includes six helices (H1:E5-Q27, H2:L43-E53, H3:F56-K61, H4:W65-K71, H5:A79-R90, H6:L92-F100) and two loops (loop L1:G28-D42 and loop L2:M72-K78). ","type":"Results"},{"text":"When compared to the ARID domains of Mrf-2, Dri, and RBP2, we found that both SWI1 and JARID1B ARID have a shorter loop L2.","type":"Results"}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":128,"term_name":"nucleic acid binding","start":119,"ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"20403335","version":4,"reference_html":"The flexible loop L1 of the H3K4 demethylase JARID1B ARID domain has a crucial role in DNA-binding activity. <i> Yao W, Peng Y, Lin D. </i> Biochem Biophys Res Commun, 2010","date":"2023-05-18T14:25:13.831Z","term_id":"GO:0003676","ec_id":"ECO:0007089","region_id":"DP00712r006","curator_orcid":"0000-0001-8399-7907","ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"statement":[{"text":"An EMSA experiment showed that the ARID/BRIGHT domain could interact with DNA duplex d (5′-ATTGCACAGTA-3′), which is consistent with a previous study [18]. Moreover, the interaction could only be detected in low salt concentrations, below 50 mM NaCl (Fig. 1C). It can be proposed that the DNA-binding ability of the JARID1B ARID domain is salt-dependent, which is similar to other ARID studies.","type":"Results"},{"text":"Quantitative analysis of DNA binding was performed by fluorescence titration experiments. The equilibrium dissociation constants (Kd) of the different mutants were calculated (Table 1 and Fig. S2). Current experimental evidence has confirmed that the loop L1, especially R38 in loop L1, is an important region in DNA-binding activity. Other residues (K32, H35, and L41) close to R38 on Loop1 that resulted in relatively large chemical shift changes when mutated may participate in the interaction between protein and DNA.","type":"Results"},{"text":"Mutations of JARID1B ARID affect DNA binding in EMSA. Obvious weaker binding occurs using the mutants R38A and 4A (K32A, H35A, R38A, L41A).","type":"Figure"},{"text":"The authors use a different numbering for the residues and (considering the UniProt sequence) are referring to the mutation R125A and the quadruple mutations K119A, H122A, R125A, L128A.","type":"Curator statement"}]},{"start":1,"end":27,"reference_id":"30858420","reference_source":"pmid","reference_html":"Molecular architecture of the Jumonji C family histone demethylase KDM5B. <i> Dorosz J, Kristensen LH, Aduri NG, Mirza O, Mirza O, Lousen R, Bucciarelli S, Mehta V, Sellés-Baiget S, Solbak SMØ, Bach A, Mesa P, Hernandez PA, Montoya G, Nguyen TTTN, Rand KD, Boesen T, Gajhede M. </i> Sci Rep, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00712r007","statement":[{"text":"The HDX data clearly show that the first 27 residues are disordered with corresponding fast HDX, whereas significantly slower HDX is observed in the following jmjN and ARID domain regions.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-18T13:33:14.734Z"}},{"start":198,"end":311,"reference_id":"30858420","reference_source":"pmid","reference_html":"Molecular architecture of the Jumonji C family histone demethylase KDM5B. <i> Dorosz J, Kristensen LH, Aduri NG, Mirza O, Mirza O, Lousen R, Bucciarelli S, Mehta V, Sellés-Baiget S, Solbak SMØ, Bach A, Mesa P, Hernandez PA, Montoya G, Nguyen TTTN, Rand KD, Boesen T, Gajhede M. </i> Sci Rep, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00712r008","statement":[{"text":"The following region (residues 198–375) is characterized by fast HDX and two regions that lack HDX data. However, the PHD1 domain region is characterized by slow HDX, demonstrating the presence of higher-order structure.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-18T13:32:54.936Z"}},{"start":339,"end":375,"reference_id":"30858420","reference_source":"pmid","reference_html":"Molecular architecture of the Jumonji C family histone demethylase KDM5B. <i> Dorosz J, Kristensen LH, Aduri NG, Mirza O, Mirza O, Lousen R, Bucciarelli S, Mehta V, Sellés-Baiget S, Solbak SMØ, Bach A, Mesa P, Hernandez PA, Montoya G, Nguyen TTTN, Rand KD, Boesen T, Gajhede M. </i> Sci Rep, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00712r009","statement":[{"text":"The following region (residues 198–375) is characterized by fast HDX and two regions that lack HDX data. However, the PHD1 domain region is characterized by slow HDX, demonstrating the presence of higher-order structure.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-18T13:32:48.500Z"}},{"start":430,"end":453,"reference_id":"30858420","reference_source":"pmid","reference_html":"Molecular architecture of the Jumonji C family histone demethylase KDM5B. <i> Dorosz J, Kristensen LH, Aduri NG, Mirza O, Mirza O, Lousen R, Bucciarelli S, Mehta V, Sellés-Baiget S, Solbak SMØ, Bach A, Mesa P, Hernandez PA, Montoya G, Nguyen TTTN, Rand KD, Boesen T, Gajhede M. </i> Sci Rep, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00712r010","statement":[{"text":"In the jmjC domain, the segment containing res. 430–453 to seen to display very fast HDX. This agrees well with the KDM5B 1–753 crystal structure19, where the region 442–447 lacked electron density and was omitted from the model. ","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-18T13:31:28.212Z"}},{"start":441,"end":453,"reference_id":"27214403","reference_source":"pmid","reference_html":"Structural analysis of human KDM5B guides histone demethylase inhibitor development. <i> Johansson C, Velupillai S, Tumber A, Szykowska A, Hookway ES, Nowak RP, Strain-Damerell C, Gileadi C, Philpott M, Burgess-Brown N, Wu N, Kopec J, Nuzzi A, Steuber H, Egner U, Badock V, Munro S, LaThangue NB, Westaway S, Brown J, Athanasou N, Prinjha R, Brennan PE, Oppermann U. </i> Nat Chem Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006222","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"DisProt","id":"DP00712r010"},{"db":"PDB","id":"5FPU"}],"region_id":"DP00712r011","statement":[{"text":"Residues 441-444 are missing in the crystal structure and nearby residues have a high relative B-factor values. This agrees with the fast HDX seen for residues 430-453 (pmid:30858420).","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-18T13:30:56.282Z"}},{"start":469,"end":481,"reference_id":"30858420","reference_source":"pmid","reference_html":"Molecular architecture of the Jumonji C family histone demethylase KDM5B. <i> Dorosz J, Kristensen LH, Aduri NG, Mirza O, Mirza O, Lousen R, Bucciarelli S, Mehta V, Sellés-Baiget S, Solbak SMØ, Bach A, Mesa P, Hernandez PA, Montoya G, Nguyen TTTN, Rand KD, Boesen T, Gajhede M. </i> Sci Rep, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00712r012","statement":[{"text":"The region 469–481 also shows fast HDX. As seen in the crystal structure, in particular the region around H474 is suggested to be disordered.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-18T13:29:42.759Z"}},{"start":543,"end":554,"reference_id":"30858420","reference_source":"pmid","reference_html":"Molecular architecture of the Jumonji C family histone demethylase KDM5B. <i> Dorosz J, Kristensen LH, Aduri NG, Mirza O, Mirza O, Lousen R, Bucciarelli S, Mehta V, Sellés-Baiget S, Solbak SMØ, Bach A, Mesa P, Hernandez PA, Montoya G, Nguyen TTTN, Rand KD, Boesen T, Gajhede M. </i> Sci Rep, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00712r013","statement":[{"text":"The fast exchange of the region 543–554 also agrees with the poorly defined electron density around residue 545 in the crystal structure.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-18T13:29:25.451Z"}},{"start":1078,"end":1125,"reference_id":"30858420","reference_source":"pmid","reference_html":"Molecular architecture of the Jumonji C family histone demethylase KDM5B. <i> Dorosz J, Kristensen LH, Aduri NG, Mirza O, Mirza O, Lousen R, Bucciarelli S, Mehta V, Sellés-Baiget S, Solbak SMØ, Bach A, Mesa P, Hernandez PA, Montoya G, Nguyen TTTN, Rand KD, Boesen T, Gajhede M. </i> Sci Rep, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00712r015","statement":[{"text":"A weak coil-coil signature is also observed approximately 100 amino acids downstream of these 3 motifs, at residues 1056–1072. After this the region 1078–1125 displays fast HDX.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-18T13:28:51.245Z"}},{"start":1271,"end":1344,"reference_id":"30858420","reference_source":"pmid","reference_html":"Molecular architecture of the Jumonji C family histone demethylase KDM5B. <i> Dorosz J, Kristensen LH, Aduri NG, Mirza O, Mirza O, Lousen R, Bucciarelli S, Mehta V, Sellés-Baiget S, Solbak SMØ, Bach A, Mesa P, Hernandez PA, Montoya G, Nguyen TTTN, Rand KD, Boesen T, Gajhede M. </i> Sci Rep, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00712r016","statement":[{"text":"Another predicted helical region 1228–1270, supported by the HDX data, is located immediately after the PHD2 domain, again followed by a long unstructured region 1271–1344 with fast HDX.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-18T13:28:31.878Z"}},{"start":1376,"end":1450,"reference_id":"30858420","reference_source":"pmid","reference_html":"Molecular architecture of the Jumonji C family histone demethylase KDM5B. <i> Dorosz J, Kristensen LH, Aduri NG, Mirza O, Mirza O, Lousen R, Bucciarelli S, Mehta V, Sellés-Baiget S, Solbak SMØ, Bach A, Mesa P, Hernandez PA, Montoya G, Nguyen TTTN, Rand KD, Boesen T, Gajhede M. </i> Sci Rep, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00712r017","statement":[{"text":"This region is followed by another predicted helical region 1345–1365 with reduced HDX that in turn is followed by a region 1376–1450 with sparse HDX sequence coverage. Data for the only peptide from this region shows fast HDX demonstrating a disordered structure despite a predicted helicity.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-18T13:28:22.567Z"}}],"released":"2016_10","uniref100":"UniRef100_Q9UGL1","date":"2016-09-14T15:17:34.000Z","acc":"Q9UGL1","name":"Lysine-specific demethylase 5B","length":1544,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI000006F746","genes":[{"name":{"value":"KDM5B"},"synonyms":[{"value":"JARID1B"},{"value":"PLU1"},{"value":"RBBP2H1"}]}],"alphafold_very_low_content":0.22474093264248704,"disorder_content":0.29080310880829013,"disprot_consensus":{"full":[{"start":1,"end":27,"type":"D"},{"start":115,"end":129,"type":"D"},{"start":188,"end":311,"type":"D"},{"start":339,"end":375,"type":"D"},{"start":430,"end":453,"type":"D"},{"start":469,"end":481,"type":"D"},{"start":543,"end":554,"type":"D"},{"start":1078,"end":1125,"type":"D"},{"start":1271,"end":1344,"type":"D"},{"start":1376,"end":1450,"type":"D"}],"Structural state":[{"start":1,"end":27,"type":"D"},{"start":115,"end":129,"type":"D"},{"start":188,"end":311,"type":"D"},{"start":339,"end":375,"type":"D"},{"start":430,"end":453,"type":"D"},{"start":469,"end":481,"type":"D"},{"start":543,"end":554,"type":"D"},{"start":1078,"end":1125,"type":"D"},{"start":1271,"end":1344,"type":"D"},{"start":1376,"end":1450,"type":"D"}],"Molecular function":[{"start":115,"end":129,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00038","name":"Intermediate filament protein","start":30,"end":386},{"id":"PF00932","name":"Lamin Tail Domain","start":434,"end":542}],"gene3D":[{"start":26,"end":120,"id":"1.20.5.1160","name":"Vasodilator-stimulated phosphoprotein"},{"start":401,"end":550,"id":"2.60.40.1260","name":"Lamin Tail domain"},{"start":307,"end":387,"id":"1.20.5.170","name":"1.20.5.170"},{"start":240,"end":306,"id":"1.20.5.500","name":"Single helix bin"}]},"uniref50":"UniRef50_P02545","sequence":"METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTIWAAGAGATHSPPTDLVWKAQNTWGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHGSHCSSSGDPAEYNLRSRTVLCGTCGQPADKASASGSGAQVGGPISSGSSASSVTVTRSYRSVGGSGGGSFGDNLVTRSYLLGNSSPRTQSPQNCSIM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P02545","disprot_id":"DP00716","ncbi_taxon_id":9606,"regions_counter":2,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":664,"region_id":"DP00716r002","reference_id":"29582385","start":567,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"We here report the NMR 1H, 15N, 13CO, 13Cα and 13Cβ chemical shift assignment of the C-terminal region that is specific to prelamin A, from amino acid 567 to amino acid 664. We also report the NMR 1H, 15N, 13CO, 13Cα and 13Cβ chemical shift assignment of the C-terminal region of the progerin variant, from amino acid 567 to amino acid 614. Analysis of these chemical shift data confirms that both prelamin A and progerin C-terminal domains are largely disordered and identifies a common partially populated α-helix from amino acid 576 to amino acid 585.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"reference_html":"<sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N backbone resonance assignment of the lamin C-terminal region specific to prelamin A. <i> Celli F, Petitalot A, Samson C, Theillet FX, Zinn-Justin S. </i> Biomol NMR Assign, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:26:05.275Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P02545","date":"2016-09-18T23:09:04.000Z","acc":"P02545","name":"Prelamin-A/C","length":664,"organism":"Homo sapiens","dataset":["Cancer-related proteins","Condensates-related proteins","Age-related disorders proteins","NDDs-related proteins"],"UniParc":"UPI000012E20D","genes":[{"name":{"value":"LMNA"},"synonyms":[{"value":"LMN1"}]}],"alphafold_very_low_content":0.2605421686746988,"disorder_content":0.14759036144578314,"disprot_consensus":{"full":[{"start":567,"end":664,"type":"D"}],"Structural state":[{"start":567,"end":664,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03517","name":"Regulator of volume decrease after cellular swelling","start":35,"end":155}],"gene3D":[{"start":18,"end":133,"id":"G3DSA:2.30.29.60"}]},"uniref50":"UniRef50_P35521","sequence":"MSFLKSFPPPGSAEGLRQQQPETEAVLNGKGLGTGTLYIAESRLSWLDGSGLGFSLEYPTISLHAVSRDLNAYPREHLYVMVNAKFGEESKESVAEEEDSDDDVEPIAEFRFVPSDKSALEAMFTAMCECQALHPDPEDEDSDDYDGEEYDVEAHEQGQGDIPTFYTYEEGLSHLTAEGQATLERLEGMLSQSVSSQYNMAGVRTEDSTRDYEDGMEVDTTPTVAGQFEDADVDH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Carnivora","Caniformia","Canidae","Canis"],"uniref90":"UniRef90_P35521","disprot_id":"DP00717","ncbi_taxon_id":9615,"regions_counter":8,"creator":"maspromonte","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":85,"region_id":"DP00717r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4. <i> Fürst J, Schedlbauer A, Gandini R, Garavaglia ML, Saino S, Gschwentner M, Sarg B, Lindner H, Jakab M, Ritter M, Bazzini C, Botta G, Meyer G, Kontaxis G, Tilly BC, Konrat R, Paulmichl M. </i> J Biol Chem, 2005","term_id":"IDPO:0000002","curator_id":"maspromonte","start":75,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1ZYI"}],"reference_id":"15905169","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":85,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4. <i> Fürst J, Schedlbauer A, Gandini R, Garavaglia ML, Saino S, Gschwentner M, Sarg B, Lindner H, Jakab M, Ritter M, Bazzini C, Botta G, Meyer G, Kontaxis G, Tilly BC, Konrat R, Paulmichl M. </i> J Biol Chem, 2005","term_id":"GO:0005515","curator_id":"maspromonte","start":75,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"15905169","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00717r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":85,"term_name":"small molecule binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4. <i> Fürst J, Schedlbauer A, Gandini R, Garavaglia ML, Saino S, Gschwentner M, Sarg B, Lindner H, Jakab M, Ritter M, Bazzini C, Botta G, Meyer G, Kontaxis G, Tilly BC, Konrat R, Paulmichl M. </i> J Biol Chem, 2005","term_id":"GO:0036094","curator_id":"maspromonte","start":75,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"15905169","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00717r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":85,"term_name":"lipid binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4. <i> Fürst J, Schedlbauer A, Gandini R, Garavaglia ML, Saino S, Gschwentner M, Sarg B, Lindner H, Jakab M, Ritter M, Bazzini C, Botta G, Meyer G, Kontaxis G, Tilly BC, Konrat R, Paulmichl M. </i> J Biol Chem, 2005","term_id":"GO:0008289","curator_id":"maspromonte","start":75,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"15905169","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00717r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":115,"region_id":"DP00717r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4. <i> Fürst J, Schedlbauer A, Gandini R, Garavaglia ML, Saino S, Gschwentner M, Sarg B, Lindner H, Jakab M, Ritter M, Bazzini C, Botta G, Meyer G, Kontaxis G, Tilly BC, Konrat R, Paulmichl M. </i> J Biol Chem, 2005","term_id":"IDPO:0000002","curator_id":"maspromonte","start":93,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1ZYI"}],"reference_id":"15905169","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":115,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4. <i> Fürst J, Schedlbauer A, Gandini R, Garavaglia ML, Saino S, Gschwentner M, Sarg B, Lindner H, Jakab M, Ritter M, Bazzini C, Botta G, Meyer G, Kontaxis G, Tilly BC, Konrat R, Paulmichl M. </i> J Biol Chem, 2005","term_id":"GO:0005515","curator_id":"maspromonte","start":93,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"15905169","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00717r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":115,"term_name":"small molecule binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4. <i> Fürst J, Schedlbauer A, Gandini R, Garavaglia ML, Saino S, Gschwentner M, Sarg B, Lindner H, Jakab M, Ritter M, Bazzini C, Botta G, Meyer G, Kontaxis G, Tilly BC, Konrat R, Paulmichl M. </i> J Biol Chem, 2005","term_id":"GO:0036094","curator_id":"maspromonte","start":93,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"15905169","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00717r007","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":115,"term_name":"lipid binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4. <i> Fürst J, Schedlbauer A, Gandini R, Garavaglia ML, Saino S, Gschwentner M, Sarg B, Lindner H, Jakab M, Ritter M, Bazzini C, Botta G, Meyer G, Kontaxis G, Tilly BC, Konrat R, Paulmichl M. </i> J Biol Chem, 2005","term_id":"GO:0008289","curator_id":"maspromonte","start":93,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"15905169","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00717r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P35521","date":"2016-09-07T23:56:59.000Z","acc":"P35521","name":"Methylosome subunit pICln","length":235,"organism":"Canis lupus familiaris","dataset":[],"UniParc":"UPI000012D171","genes":[{"name":{"value":"CLNS1A"},"synonyms":[{"value":"ICLN"}]}],"alphafold_very_low_content":0.1276595744680851,"disorder_content":0.14468085106382977,"disprot_consensus":{"full":[{"start":75,"end":85,"type":"D"},{"start":93,"end":115,"type":"D"}],"Structural state":[{"start":75,"end":85,"type":"D"},{"start":93,"end":115,"type":"D"}],"Molecular function":[{"start":75,"end":85,"type":"F"},{"start":93,"end":115,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00104","name":"Ligand-binding domain of nuclear hormone receptor","start":319,"end":485},{"id":"PF00105","name":"Double treble clef zinc finger, C4 type","start":138,"end":204},{"id":"PF12577","name":"PPAR gamma N-terminal region","start":31,"end":108}],"gene3D":[{"start":136,"end":229,"id":"3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A"},{"start":236,"end":504,"id":"1.10.565.10","name":"Retinoid X Receptor"}]},"uniref50":"UniRef50_P37231","sequence":"MGETLGDSPIDPESDSFTDTLSANISQEMTMVDTEMPFWPTNFGISSVDLSVMEDHSHSFDIKPFTTVDFSSISTPHYEDIPFTRTDPVVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKSIPGFVNLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQLLQVIKKTETDMSLHPLLQEIYKDLY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P37231","disprot_id":"DP00718","ncbi_taxon_id":9606,"regions_counter":52,"creator":"ktsirigos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":111,"region_id":"DP00718r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":9,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":111,"term_name":"molecular function regulator","start":9,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006220","region_id":"DP00718r002","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":111,"term_name":"protein binding","start":9,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00718r003","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":111,"region_id":"DP00718r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Dynamic protein-DNA recognition: beyond what can be seen. <i> Fuxreiter M, Simon I, Bondos S. </i> Trends Biochem Sci, 2011","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":9,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"21620710","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":111,"term_name":"molecular function regulator","start":9,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"21620710","version":3,"reference_html":"Dynamic protein-DNA recognition: beyond what can be seen. <i> Fuxreiter M, Simon I, Bondos S. </i> Trends Biochem Sci, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006220","region_id":"DP00718r005","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":111,"term_name":"protein binding","start":9,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"21620710","version":3,"reference_html":"Dynamic protein-DNA recognition: beyond what can be seen. <i> Fuxreiter M, Simon I, Bondos S. </i> Trends Biochem Sci, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00718r006","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":111,"region_id":"DP00718r007","released":"2022_03","ec_id":"ECO:0006196","reference_html":"Dynamic protein-DNA recognition: beyond what can be seen. <i> Fuxreiter M, Simon I, Bondos S. </i> Trends Biochem Sci, 2011","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":9,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"21620710","version":2,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":111,"term_name":"molecular function regulator","start":9,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"21620710","version":3,"reference_html":"Dynamic protein-DNA recognition: beyond what can be seen. <i> Fuxreiter M, Simon I, Bondos S. </i> Trends Biochem Sci, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006196","region_id":"DP00718r008","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":111,"term_name":"protein binding","start":9,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"21620710","version":3,"reference_html":"Dynamic protein-DNA recognition: beyond what can be seen. <i> Fuxreiter M, Simon I, Bondos S. </i> Trends Biochem Sci, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006196","region_id":"DP00718r009","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":111,"region_id":"DP00718r010","released":"2022_03","ec_id":"ECO:0006196","reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":9,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":2,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":111,"term_name":"molecular function regulator","start":9,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006196","region_id":"DP00718r011","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":111,"term_name":"protein binding","start":9,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006196","region_id":"DP00718r012","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":174,"region_id":"DP00718r013","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":112,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":174,"term_name":"molecular function regulator","start":112,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006220","region_id":"DP00718r014","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":174,"term_name":"disorder to order","start":112,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":2,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00718r015","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":174,"term_name":"protein binding","start":112,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00718r016","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":174,"region_id":"DP00718r017","released":"2022_03","ec_id":"ECO:0006196","reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":112,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":2,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":174,"term_name":"molecular function regulator","start":112,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006196","region_id":"DP00718r018","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":174,"term_name":"disorder to order","start":112,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":2,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006196","region_id":"DP00718r019","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":174,"term_name":"protein binding","start":112,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006196","region_id":"DP00718r020","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":211,"region_id":"DP00718r021","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":175,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":211,"term_name":"molecular function regulator","start":175,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006220","region_id":"DP00718r022","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":211,"term_name":"nucleic acid binding","start":175,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006220","region_id":"DP00718r023","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":211,"region_id":"DP00718r024","released":"2022_03","ec_id":"ECO:0006196","reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":175,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":2,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":211,"term_name":"molecular function regulator","start":175,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006196","region_id":"DP00718r025","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":211,"term_name":"nucleic acid binding","start":175,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006196","region_id":"DP00718r026","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":278,"region_id":"DP00718r027","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":238,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":278,"term_name":"molecular function regulator","start":238,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006220","region_id":"DP00718r028","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":278,"term_name":"protein binding","start":238,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00718r029","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":278,"region_id":"DP00718r030","released":"2022_03","ec_id":"ECO:0006196","reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":238,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":2,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":278,"term_name":"molecular function regulator","start":238,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006196","region_id":"DP00718r031","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":278,"term_name":"protein binding","start":238,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006196","region_id":"DP00718r032","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":298,"region_id":"DP00718r033","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":279,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":298,"term_name":"molecular function regulator","start":279,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006220","region_id":"DP00718r034","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":298,"term_name":"disorder to order","start":279,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":2,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00718r035","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":298,"region_id":"DP00718r036","released":"2022_03","ec_id":"ECO:0006196","reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":279,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":2,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":298,"term_name":"molecular function regulator","start":279,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006196","region_id":"DP00718r037","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":298,"term_name":"disorder to order","start":279,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":2,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006196","region_id":"DP00718r038","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":452,"region_id":"DP00718r039","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":443,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":452,"term_name":"molecular function regulator","start":443,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006220","region_id":"DP00718r040","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":452,"term_name":"order to disorder","start":443,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":2,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000014","ec_id":"ECO:0006220","region_id":"DP00718r041","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":452,"term_name":"protein binding","start":443,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00718r042","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":452,"region_id":"DP00718r043","released":"2022_03","ec_id":"ECO:0006196","reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":443,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":2,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":452,"term_name":"molecular function regulator","start":443,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006196","region_id":"DP00718r044","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":452,"term_name":"order to disorder","start":443,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":2,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000014","ec_id":"ECO:0006196","region_id":"DP00718r045","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":452,"term_name":"protein binding","start":443,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006196","region_id":"DP00718r046","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":477,"region_id":"DP00718r047","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":453,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":477,"term_name":"molecular function regulator","start":453,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006220","region_id":"DP00718r048","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":477,"term_name":"protein binding","start":453,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00718r049","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":477,"region_id":"DP00718r050","released":"2022_03","ec_id":"ECO:0006196","reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","term_id":"IDPO:0000002","curator_id":"ktsirigos","start":453,"term_ontology":"IDPO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":2,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":477,"term_name":"molecular function regulator","start":453,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006196","region_id":"DP00718r051","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":477,"term_name":"protein binding","start":453,"ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","curator_id":"ktsirigos","released":"2022_03","term_ontology":"GO","curator_name":"Konstantinos D. Tsirigos","reference_id":"19043829","version":3,"reference_html":"Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA. <i> Chandra V, Huang P, Hamuro Y, Raghuram S, Wang Y, Burris TP, Rastinejad F. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006196","region_id":"DP00718r052","curator_orcid":"0000-0001-5280-1107","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P37231","date":"2016-09-13T14:36:06.000Z","acc":"P37231","name":"Peroxisome proliferator-activated receptor gamma","length":505,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI0000131FED","genes":[{"name":{"value":"PPARG"},"synonyms":[{"value":"NR1C3"}]}],"alphafold_very_low_content":0.2712871287128713,"disorder_content":0.592079207920792,"disprot_consensus":{"full":[{"start":9,"end":111,"type":"D"},{"start":112,"end":174,"type":"T"},{"start":175,"end":211,"type":"D"},{"start":238,"end":278,"type":"D"},{"start":279,"end":298,"type":"T"},{"start":443,"end":452,"type":"T"},{"start":453,"end":477,"type":"D"}],"Structural state":[{"start":9,"end":211,"type":"D"},{"start":238,"end":298,"type":"D"},{"start":443,"end":477,"type":"D"}],"Molecular function":[{"start":9,"end":211,"type":"F"},{"start":238,"end":298,"type":"F"},{"start":443,"end":477,"type":"F"}],"Structural transition":[{"start":112,"end":174,"type":"T"},{"start":279,"end":298,"type":"T"},{"start":443,"end":452,"type":"T"}]}},{"features":{"pfam":[{"id":"PF03167","name":"Uracil DNA glycosylase superfamily","start":129,"end":289}]},"uniref50":"UniRef50_Q13569","sequence":"MEAENAGSYSLQQAQAFYTFPFQQLMAEAPNMAVVNEQQMPEEVPAPAPAQEPVQEAPKGRKRKPRTTEPKQPVEPKKPVESKKSGKSAKSKEKQEKITDTFKVKRKVDRFNGVSEAELLTKTLPDILTFNLDIVIIGINPGLMAAYKGHHYPGPGNHFWKCLFMSGLSEVQLNHMDDHTLPGKYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQKLQKYQPRIAVFNGKCIYEIFSKEVFGVKVKNLEFGLQPHKIPDTETLCYVMPSSSARCAQFPRAQDKVHYYIKLKDLRDQLKGIERNMDVQEVQYTFDLQLAQEDAKKMAVKEEKYDPGYEAAYGGAYGENPCSSEPCGFSSNGLIESVELRGESAFSGIPNGQWMTQSFTDQIPSFSNHCGTQEQEEESHA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q13569","disprot_id":"DP00719","ncbi_taxon_id":9606,"regions_counter":8,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":50,"region_id":"DP00719r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The thymine-DNA glycosylase regulatory domain: residual structure and DNA binding. <i> Smet-Nocca C, Wieruszeski JM, Chaar V, Leroy A, Benecke A. </i> Biochemistry, 2008","term_id":"IDPO:0000002","curator_id":"nmurvai","start":1,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"18512959","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":50,"term_name":"molecular function regulator","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"18512959","version":3,"reference_html":"The thymine-DNA glycosylase regulatory domain: residual structure and DNA binding. <i> Smet-Nocca C, Wieruszeski JM, Chaar V, Leroy A, Benecke A. </i> Biochemistry, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006165","region_id":"DP00719r002","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":111,"region_id":"DP00719r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The thymine-DNA glycosylase regulatory domain: residual structure and DNA binding. <i> Smet-Nocca C, Wieruszeski JM, Chaar V, Leroy A, Benecke A. </i> Biochemistry, 2008","term_id":"IDPO:0000002","curator_id":"nmurvai","start":51,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"18512959","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":111,"term_name":"molecular function regulator","start":51,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"18512959","version":3,"reference_html":"The thymine-DNA glycosylase regulatory domain: residual structure and DNA binding. <i> Smet-Nocca C, Wieruszeski JM, Chaar V, Leroy A, Benecke A. </i> Biochemistry, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006165","region_id":"DP00719r004","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":111,"term_name":"disorder to order","start":51,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"18512959","version":2,"reference_html":"The thymine-DNA glycosylase regulatory domain: residual structure and DNA binding. <i> Smet-Nocca C, Wieruszeski JM, Chaar V, Leroy A, Benecke A. </i> Biochemistry, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00719r005","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":111,"term_name":"nucleic acid binding","start":51,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"18512959","version":3,"reference_html":"The thymine-DNA glycosylase regulatory domain: residual structure and DNA binding. <i> Smet-Nocca C, Wieruszeski JM, Chaar V, Leroy A, Benecke A. </i> Biochemistry, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006165","region_id":"DP00719r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":410,"region_id":"DP00719r007","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The thymine-DNA glycosylase regulatory domain: residual structure and DNA binding. <i> Smet-Nocca C, Wieruszeski JM, Chaar V, Leroy A, Benecke A. </i> Biochemistry, 2008","term_id":"IDPO:0000002","curator_id":"nmurvai","start":340,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"18512959","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":410,"term_name":"self-inhibition","start":340,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"18512959","version":3,"reference_html":"The thymine-DNA glycosylase regulatory domain: residual structure and DNA binding. <i> Smet-Nocca C, Wieruszeski JM, Chaar V, Leroy A, Benecke A. </i> Biochemistry, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000059","ec_id":"ECO:0006165","region_id":"DP00719r008","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_Q13569","date":"2016-09-14T10:51:23.000Z","acc":"Q13569","name":"G/T mismatch-specific thymine DNA glycosylase","length":410,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000043B8A","genes":[{"name":{"value":"TDG"}}],"alphafold_very_low_content":0.4024390243902439,"disorder_content":0.44390243902439025,"disprot_consensus":{"full":[{"start":1,"end":50,"type":"D"},{"start":51,"end":111,"type":"T"},{"start":340,"end":410,"type":"D"}],"Structural state":[{"start":1,"end":111,"type":"D"},{"start":340,"end":410,"type":"D"}],"Molecular function":[{"start":1,"end":111,"type":"F"}],"Structural transition":[{"start":51,"end":111,"type":"T"}],"Disorder function":[{"start":340,"end":410,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00505","name":"HMG (high mobility group) box","start":555,"end":621},{"id":"PF03531","name":"Structure-specific recognition protein (SSRP1)","start":102,"end":190},{"id":"PF08512","name":"Histone chaperone Rttp106-like, middle domain","start":340,"end":427},{"id":"PF17292","name":"POB3-like N-terminal PH domain","start":6,"end":97},{"id":"PF21103","name":"SSRP1 PH domain","start":197,"end":326}],"gene3D":[{"start":329,"end":430,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":1,"end":94,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":553,"end":624,"id":"1.10.30.10","name":"High mobility group box domain"},{"start":95,"end":176,"id":"2.30.29.220","name":"Structure-specific recognition protein (SSRP1)"},{"start":189,"end":327,"id":"2.30.29.150","name":"2.30.29.150"}]},"uniref50":"UniRef50_Q05344","sequence":"MTDSLEYNDINAEVRGVLCSGRLKMTEQNIIFKNTKTGKVEQISAEDIDLINSQKFVGTWGLRVFTKGGVLHRFTGFRDSEHEKLGKFIKAAYSQEMVEKEMCVKGWNWGTARFMGSVLSFDKESKTIFEVPLSHVSQCVTGKNEVTLEFHQNDDAPVGLLEMRFHIPAVESAEEDPVDKFHQNVMSKASVISASGESIAIFREIQILTPRGRYDIKIFSTFFQLHGKTFDYKIPMDSVLRLFMLPHKDSRQMFFVLSLDPPIKQGQTRYHYLVLLFAPDEETTIELPFSEAELRDKYEGKLEKEISGPVYEVMGKVMKVLIGRKITGPGNFIGHSGTAAVGCSFKAAAGYLYPLERGFIYIHKPPLHIRFEEISSVNFARSGGSTRSFDFEVTLKNGTVHIFSSIEKEEYAKLFDYITQKKLHVSNMGKDKSGYKDVDFGDSDNENEPDAYLARLKAEAREKEEDDDDGDSDEESTDEDFKPNENESDVAEEYDSNVESDSDDDSDASGGGGDSDGAKKKKEKKSEKKEKKEKKHKEKERTKKPSKKKKDSGKPKRATTAFMLWLNDTRESIKRENPGIKVTEIAKKGGEMWKELKDKSKWEDAAAKDKQRYHDEMRNYKPEAGGDSDNEKGGKSSKKRKTEPSPSKKANTSGSGFKSKEYISDDDSTSSDDEKDNEPAKKKSKPPSDGDAKKKKAKSESEPEESEEDSNASDEDEEDEASD","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_Q05344","disprot_id":"DP00720","ncbi_taxon_id":7227,"regions_counter":7,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":518,"region_id":"DP00720r001","released":"2022_03","ec_id":"ECO:0001591","reference_html":"Phosphorylated intrinsically disordered region of FACT masks its nucleosomal DNA binding elements. <i> Tsunaka Y, Toga J, Yamaguchi H, Tate S, Hirose S, Morikawa K. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"fquaglia","start":437,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19605348","version":2,"ec_name":"atomic force microscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":554,"region_id":"DP00720r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Phosphorylated intrinsically disordered region of FACT masks its nucleosomal DNA binding elements. <i> Tsunaka Y, Toga J, Yamaguchi H, Tate S, Hirose S, Morikawa K. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"fquaglia","start":519,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19605348","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":554,"term_name":"protein binding","start":519,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19605348","version":3,"reference_html":"Phosphorylated intrinsically disordered region of FACT masks its nucleosomal DNA binding elements. <i> Tsunaka Y, Toga J, Yamaguchi H, Tate S, Hirose S, Morikawa K. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00720r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":554,"region_id":"DP00720r004","released":"2022_03","ec_id":"ECO:0001591","reference_html":"Phosphorylated intrinsically disordered region of FACT masks its nucleosomal DNA binding elements. <i> Tsunaka Y, Toga J, Yamaguchi H, Tate S, Hirose S, Morikawa K. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"fquaglia","start":519,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19605348","version":2,"ec_name":"atomic force microscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":554,"term_name":"protein binding","start":519,"ec_name":"atomic force microscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19605348","version":3,"reference_html":"Phosphorylated intrinsically disordered region of FACT masks its nucleosomal DNA binding elements. <i> Tsunaka Y, Toga J, Yamaguchi H, Tate S, Hirose S, Morikawa K. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0001591","region_id":"DP00720r005","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":518,"region_id":"DP00720r006","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Phosphorylated intrinsically disordered region of FACT masks its nucleosomal DNA binding elements. <i> Tsunaka Y, Toga J, Yamaguchi H, Tate S, Hirose S, Morikawa K. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"fquaglia","start":437,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19605348","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":723,"region_id":"DP00720r007","released":"2022_03","ec_id":"ECO:0001591","reference_html":"Phosphorylated intrinsically disordered region of FACT masks its nucleosomal DNA binding elements. <i> Tsunaka Y, Toga J, Yamaguchi H, Tate S, Hirose S, Morikawa K. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"fquaglia","start":625,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19605348","version":2,"ec_name":"atomic force microscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q05344","date":"2016-09-13T18:03:25.000Z","acc":"Q05344","name":"FACT complex subunit Ssrp1","length":723,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI000016BD88","genes":[{"name":{"value":"Ssrp"},"synonyms":[{"value":"CF5"},{"value":"SSRP1"}],"orfNames":[{"value":"CG4817"}]}],"alphafold_very_low_content":0.2766251728907331,"disorder_content":0.30013831258644535,"disprot_consensus":{"full":[{"start":437,"end":554,"type":"D"},{"start":625,"end":723,"type":"D"}],"Structural state":[{"start":437,"end":554,"type":"D"},{"start":625,"end":723,"type":"D"}],"Molecular function":[{"start":519,"end":554,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00557","name":"Metallopeptidase family M24","start":183,"end":412},{"id":"PF08512","name":"Histone chaperone Rttp106-like, middle domain","start":818,"end":901},{"id":"PF08644","name":"FACT complex subunit (SPT16/CDC68)","start":535,"end":657},{"id":"PF14826","name":"FACT complex subunit SPT16 N-terminal lobe domain","start":6,"end":167},{"id":"PF21091","name":"FACT complex subunit SPT16, C-terminal domain","start":944,"end":1017},{"id":"PF24824","name":"FACT complex subunit SPT16 PH-like domain","start":667,"end":793}],"gene3D":[{"start":4,"end":173,"id":"3.40.350.10","name":"Creatinase/prolidase N-terminal domain"},{"start":805,"end":936,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":175,"end":436,"id":"3.90.230.10","name":"Creatinase/methionine aminopeptidase superfamily"},{"start":507,"end":645,"id":"2.30.29.210","name":"FACT complex subunit Spt16p/Cdc68p"},{"start":650,"end":804,"id":"2.30.29.150","name":"2.30.29.150"}]},"uniref50":"UniRef50_Q8IRG6","sequence":"MSSFVLDKEAFVRRVKRLYTEWRAPSIGHDDALRNLDCIMSIVGVEEDVMYSKSMALQLWLLGYELTDTISVFCSDAVYFLTSKKKIEFLKQTQNITEEGFPEINLLVRDRTDKDQGNFEKLIKALQNSKKGKRLGVFAKDAYPGEFSEAWKKSLTASKFEHVDISTIIAYLMCPKDESEINNIRKASLVSMDIFNKYLKDEIMDIIDSDRKVKHNKLSDGCEAAIGEKKYTSGLDPRLLDMAYPPIIQSGGAYSLKFSAVADKNPLHFGVIVCSLGARYKSYCSNISRTFLVNPTEAMQENYTFLVSVQEEILKLLVPGTKLCDVYEKTLDFVKKEKPSMVDNLPKSFGFAMGLEFRENSIVIGPKCQALLKKNMVFNLHVGISNLTNPEATDKEGKNYALFIGDTVLVGEQSPASVMTPSKKKIKNVGIFIKDDSDEEDVDDKKTAKEDQGTEILGRSKRNAVLESKLRNEINTEEKRKEHQRELAQQLNERAKDRLARQGNSKEVEKVRKNTVSYKSISQMPREPEVKELKLYVDKKYETVIMPVFGIQVPFHISTIKNISQSVEGEYTYLRINFFHPGATMGRNEGGLYPQPEATFVKEVTYRSSNVKEHGEVGAPSANLNNAFRLIKEVQKRFKTREAEEREKEDLVKQDTLILSQNKGNPKLKDLYIRPNIVTKRMTGSLEAHSNGFRYISVRGDKVDILYNNIKSAFFQPCDGEMIILLHFHLKYAIMFGKKKHVDVQFYTEVGEITTDLGKHQHMHDRDDLAAEQAERELRHKLKTAFKSFCEKVETMTKSVVEFDTPFRELGFPGAPFRSTVTLQPTSGSLVNLTEWPPFVITLDDVELVHFERVQFHLRNFDMIFVFKEYNKKVAMVNAIPMNMLDHVKEWLNSCDIRYSEGVQSLNWQKIMKTITDDPEGFFEQGGWTFLDPESGSEGENETAESEEDEAYNPTDAESDEESDEDSEYSEASEDSEESDEDLGSDEESGKDWSDLEREAAEEDRNHDYAADDKPRNGKFDSKKHGKSSKHSPSKSSKDKYNSRDKHHSSSSSGNKSSSKDKDRKRSRDDSRDNGHKSKKSRH","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_Q8IRG6","disprot_id":"DP00721","ncbi_taxon_id":7227,"regions_counter":1,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1044,"region_id":"DP00721r001","released":"2022_03","ec_id":"ECO:0001591","reference_html":"Visualization of intrinsically disordered regions of proteins by high-speed atomic force microscopy. <i> Miyagi A, Tsunaka Y, Uchihashi T, Mayanagi K, Hirose S, Morikawa K, Ando T. </i> Chemphyschem, 2008","term_id":"IDPO:0000002","curator_id":"fquaglia","start":889,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18698566","version":2,"ec_name":"atomic force microscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q8IRG6","date":"2016-08-31T10:03:29.000Z","acc":"Q8IRG6","name":"FACT complex subunit spt16","length":1083,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI00001B98DA","genes":[{"name":{"value":"dre4"},"synonyms":[{"value":"spt16"}],"orfNames":[{"value":"CG1828"}]}],"alphafold_very_low_content":0.17820867959372114,"disorder_content":0.1440443213296399,"disprot_consensus":{"full":[{"start":889,"end":1044,"type":"D"}],"Structural state":[{"start":889,"end":1044,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00436","name":"Single-strand binding protein family","start":6,"end":112}],"gene3D":[{"start":2,"end":146,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}]},"uniref50":"UniRef50_P0AGE2","sequence":"MASRGVNKVILVGNLGQDPEVRYMPNGGAVANITLATSESWRDKATGEMKEQTEWHRVVLFGKLAEVASEYLRKGSQVYIEGQLRTRKWTDQSGQDRYTTEVVVNVGGTMQMLGGRQGGGAPAGGNIGGGQPQGGWGQPQQPQGGNQFSGGAQSRPQQSAPAAPSNEPPMDFDDDIPF","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0AGE2","disprot_id":"DP00722","ncbi_taxon_id":83334,"regions_counter":4,"creator":"ahatos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":177,"region_id":"DP00722r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The C-terminal domain of full-length E. coli SSB is disordered even when bound to DNA. <i> Savvides SN, Raghunathan S, Fütterer K, Kozlov AG, Lohman TM, Waksman G. </i> Protein Sci, 2004","term_id":"IDPO:0000002","curator_id":"ahatos","start":113,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1SRU"}],"reference_id":"15169953","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P0AGE2","date":"2016-09-12T22:48:16.000Z","acc":"P0AGE2","name":"Single-stranded DNA-binding protein","length":178,"organism":"Escherichia coli O157:H7","dataset":[],"UniParc":"UPI0000135FA7","genes":[{"name":{"value":"ssb"},"olnNames":[{"value":"Z5658"},{"value":"ECs5041"}]}],"alphafold_very_low_content":0.14606741573033707,"disorder_content":0.3651685393258427,"disprot_consensus":{"full":[{"start":113,"end":177,"type":"D"}],"Structural state":[{"start":113,"end":177,"type":"D"}]}},{"features":{"pfam":[{"id":"PF07859","name":"alpha/beta hydrolase fold","start":109,"end":322}],"gene3D":[{"start":1,"end":344,"id":"3.40.50.1820","name":"alpha/beta hydrolase"}]},"uniref50":"UniRef50_Q9MAA7","sequence":"MAASDEVNLIESRTVVPLNTWVLISNFKVAYNILRRPDGTFNRHLAEYLDRKVTANANPVDGVFSFDVLIDRRINLLSRVYRPAYADQEQPPSILDLEKPVDGDIVPVILFFHGGSFAHSSANSAIYDTLCRRLVGLCKCVVVSVNYRRAPENPYPCAYDDGWIALNWVNSRSWLKSKKDSKVHIFLAGDSSGGNIAHNVALRAGESGIDVLGNILLNPMFGGNERTESEKSLDGKYFVTVRDRDWYWKAFLPEGEDREHPACNPFSPRGKSLEGVSFPKSLVVVAGLDLIRDWQLAYAEGLKKAGQEVKLMHLEKATVGFYLLPNNNHFHNVMDEISAFVNAEC","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q9MAA7","disprot_id":"DP00723","ncbi_taxon_id":3702,"regions_counter":2,"creator":"ameszaros","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":62,"region_id":"DP00723r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Gibberellin-induced DELLA recognition by the gibberellin receptor GID1. <i> Murase K, Hirano Y, Sun TP, Hakoshima T. </i> Nature, 2008","term_id":"IDPO:0000002","curator_id":"ameszaros","start":50,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"19037309","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2ZSH"}],"term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":62,"term_name":"flexible linker","start":50,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ameszaros","released":"2022_03","term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"19037309","version":3,"reference_html":"Gibberellin-induced DELLA recognition by the gibberellin receptor GID1. <i> Murase K, Hirano Y, Sun TP, Hakoshima T. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006220","region_id":"DP00723r002","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_Q9MAA7","date":"2016-09-17T23:21:25.000Z","acc":"Q9MAA7","name":"Gibberellin receptor GID1A","length":345,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI00000AC731","genes":[{"name":{"value":"GID1A"},"synonyms":[{"value":"CXE10"},{"value":"GID1L1"}],"orfNames":[{"value":"T12H1.8"}],"olnNames":[{"value":"At3g05120"}]}],"alphafold_very_low_content":0.008695652173913044,"disorder_content":0.03768115942028986,"disprot_consensus":{"full":[{"start":50,"end":62,"type":"D"}],"Structural state":[{"start":50,"end":62,"type":"D"}],"Disorder function":[{"start":50,"end":62,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03514","name":"GRAS domain family","start":169,"end":529},{"id":"PF12041","name":"Transcriptional regulator DELLA protein N terminal","start":28,"end":95}],"gene3D":[{"start":26,"end":91,"id":"1.10.10.1290","name":"Transcriptional regulator DELLA, N-terminal domain"}]},"uniref50":"UniRef50_Q9LQT8","sequence":"MKRDHHHHHHQDKKTMMMNEEDDGNGMDELLAVLGYKVRSSEMADVAQKLEQLEVMMSNVQEDDLSQLATETVHYNPAELYTWLDSMLTDLNPPSSNAEYDLKAIPGDAILNQFAIDSASSSNQGGGGDTYTTNKRLKCSNGVVETTTATAESTRHVVLVDSQENGVRLVHALLACAEAVQKENLTVAEALVKQIGFLAVSQIGAMRKVATYFAEALARRIYRLSPSQSPIDHSLSDTLQMHFYETCPYLKFAHFTANQAILEAFQGKKRVHVIDFSMSQGLQWPALMQALALRPGGPPVFRLTGIGPPAPDNFDYLHEVGCKLAHLAEAIHVEFEYRGFVANTLADLDASMLELRPSEIESVAVNSVFELHKLLGRPGAIDKVLGVVNQIKPEIFTVVEQESNHNSPIFLDRFTESLHYYSTLFDSLEGVPSGQDKVMSEVYLGKQICNVVACDGPDRVERHETLSQWRNRFGSAGFAAAHIGSNAFKQASMLLALFNGGEGYRVEESDGCLMLGWHTRPLIATSAWKLSTN","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q9LQT8","disprot_id":"DP00724","ncbi_taxon_id":3702,"regions_counter":8,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":113,"region_id":"DP00724r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Gibberellin-induced DELLA recognition by the gibberellin receptor GID1. <i> Murase K, Hirano Y, Sun TP, Hakoshima T. </i> Nature, 2008","term_id":"IDPO:0000002","curator_id":"fquaglia","start":11,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19037309","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":113,"term_name":"molecular function regulator","start":11,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19037309","version":3,"reference_html":"Gibberellin-induced DELLA recognition by the gibberellin receptor GID1. <i> Murase K, Hirano Y, Sun TP, Hakoshima T. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006220","region_id":"DP00724r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":113,"term_name":"disorder to order","start":11,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19037309","version":2,"reference_html":"Gibberellin-induced DELLA recognition by the gibberellin receptor GID1. <i> Murase K, Hirano Y, Sun TP, Hakoshima T. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00724r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":113,"term_name":"protein binding","start":11,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19037309","version":3,"reference_html":"Gibberellin-induced DELLA recognition by the gibberellin receptor GID1. <i> Murase K, Hirano Y, Sun TP, Hakoshima T. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00724r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":113,"region_id":"DP00724r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Gibberellin-induced DELLA recognition by the gibberellin receptor GID1. <i> Murase K, Hirano Y, Sun TP, Hakoshima T. </i> Nature, 2008","term_id":"IDPO:0000002","curator_id":"fquaglia","start":11,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19037309","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":113,"term_name":"molecular function regulator","start":11,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19037309","version":3,"reference_html":"Gibberellin-induced DELLA recognition by the gibberellin receptor GID1. <i> Murase K, Hirano Y, Sun TP, Hakoshima T. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006204","region_id":"DP00724r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":113,"term_name":"disorder to order","start":11,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19037309","version":2,"reference_html":"Gibberellin-induced DELLA recognition by the gibberellin receptor GID1. <i> Murase K, Hirano Y, Sun TP, Hakoshima T. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00724r007","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":113,"term_name":"protein binding","start":11,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19037309","version":3,"reference_html":"Gibberellin-induced DELLA recognition by the gibberellin receptor GID1. <i> Murase K, Hirano Y, Sun TP, Hakoshima T. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00724r008","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q9LQT8","date":"2016-08-16T18:19:40.000Z","acc":"Q9LQT8","name":"DELLA protein GAI","length":533,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI000009E27F","genes":[{"name":{"value":"GAI","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9389651","url":"http://www.ncbi.nlm.nih.gov/pubmed/9389651","alternativeUrl":"https://europepmc.org/abstract/MED/9389651"}}]},"synonyms":[{"value":"RGA2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9237632","url":"http://www.ncbi.nlm.nih.gov/pubmed/9237632","alternativeUrl":"https://europepmc.org/abstract/MED/9237632"}}]}],"orfNames":[{"value":"F10B6.34","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAF79228.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF79228.1"}}]}],"olnNames":[{"value":"At1g14920","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT1G14920","url":""}}]}]}],"alphafold_very_low_content":0.1894934333958724,"disorder_content":0.19324577861163228,"disprot_consensus":{"full":[{"start":11,"end":113,"type":"T"}],"Structural state":[{"start":11,"end":113,"type":"D"}],"Molecular function":[{"start":11,"end":113,"type":"F"}],"Structural transition":[{"start":11,"end":113,"type":"T"}]}},{"features":{"pfam":[{"id":"PF04612","name":"Type II secretion system (T2SS), protein M","start":88,"end":163},{"id":"PF28880","name":"Type II secretion system (T2SS), protein M transmembrane region","start":8,"end":76}],"gene3D":[{"start":86,"end":165,"id":"3.30.1360.100","name":"General secretion pathway protein M, EpsM"}]},"uniref50":"UniRef50_P41851","sequence":"MKELLAPVQAWWRSVTPREQKMVMGMGALTVLAIAYWGIWQPLSERTAQAQARLQTEKQLLSWVSENANDIVTLRAQGGSDAPSDQPLNQVITNSTRQFNIELIRVQPRGEMMQVWIQPLPFSQLVSWIAYLQERQGVSVDAIDIDRGKVNGVVEVKRLQLKRGG","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Vibrionales","Vibrionaceae","Vibrio"],"uniref90":"UniRef90_P41851","disprot_id":"DP00725","ncbi_taxon_id":243277,"regions_counter":1,"creator":"aschramm","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":85,"region_id":"DP00725r001","released":"2022_12","ec_id":"ECO:0006220","reference_html":"The crystal structure of the periplasmic domain of the type II secretion system protein EpsM from Vibrio cholerae: the simplest version of the ferredoxin fold. <i> Abendroth J, Rice AE, McLuskey K, Bagdasarian M, Hol WG. </i> J Mol Biol, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":44,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15081815","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-08-26T15:56:47.283Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The N-terminal part of the constructs, i.e. residues 44–85, which are just C-terminal of the predicted transmembrane region comprising residues 24–43, are disordered in the present structure. ","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P41851","date":"2016-09-18T18:52:26.000Z","acc":"P41851","name":"Type II secretion system protein M","length":165,"organism":"Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)","dataset":[],"UniParc":"UPI000012BC73","genes":[{"name":{"value":"epsM"},"olnNames":[{"value":"VC_2724"}]}],"alphafold_very_low_content":0.09090909090909091,"disorder_content":0.2545454545454545,"disprot_consensus":{"full":[{"start":44,"end":85,"type":"D"}],"Structural state":[{"start":44,"end":85,"type":"D"}]}},{"acc":"Q5UPJ7","sequence":"MENTDHTNNEHRLTQLLSIAEECETLDRLKQLVDSGRIFTAYNGFEPSGRIHIAQALITVMNTNNIIECGGQMIIYIADWFAKMNLKMNGDINKIRELGRYFIEVFKACGINLDGTRFIWASEFIASNPSYIERMLDIAEFSTISRVKRCCQIMGRNESDCLKASQIFYPCMQAADVFELVPEGIDICQLGIDQRKVNMLAIEYANDRGLKIPISLSHHMLMSLSGPKKKMSKSDPQGAIFMDDTEQEVSEKISRAYCTDETFDNPIFEYIKYLLLRWFGTLNLCGKIYTDIESIQEDFSSMNKRELKTDVANYINTIIDLVREHFKKPELSELLSNVKSYQQPSK","creator":"gbalatti","dataset":["Viral proteins"],"date":"2016-09-08T18:25:24.000Z","disprot_id":"DP00726","features":{"pfam":[{"id":"PF00579","name":"tRNA synthetases class I (W and Y)","start":38,"end":318}],"gene3D":[{"start":1,"end":221,"id":"3.40.50.620","name":"HUPs","_id":"685af523b4ac24d5329d84cb"},{"start":222,"end":346,"id":"1.10.240.10","name":"Tyrosyl-Transfer RNA Synthetase","_id":"685af523b4ac24d5329d84cc"}]},"genes":[{"name":{"value":"YARS","evidences":[],"_id":"685af523b4ac24d5329d84e2"},"synonyms":[],"olnNames":[{"value":"MIMI_L124","evidences":[],"_id":"685af523b4ac24d5329d84e3"}],"orfNames":[],"_id":"685af523b4ac24d5329d84e1"}],"length":346,"name":"Tyrosine--tRNA ligase","ncbi_taxon_id":212035,"organism":"Acanthamoeba polyphaga mimivirus","regions_counter":6,"released":"2016_10","taxonomy":["Viruses","Varidnaviria","Bamfordvirae","Nucleocytoviricota","Megaviricetes","Imitervirales","Mimiviridae","Mimivirus"],"UniParc":"UPI0000465349","uniref100":"UniRef100_Q5UPJ7","uniref50":"UniRef50_Q5UPJ7","uniref90":"UniRef90_Q5UPJ7","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2J5B","_id":"685af523b4ac24d5329d84d5"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":150,"end":166,"interaction_partner":[],"reference_html":"Virus-encoded aminoacyl-tRNA synthetases: structural and functional characterization of mimivirus TyrRS and MetRS. <i> Abergel C, Rudinger-Thirion J, Giegé R, Claverie JM. </i> J Virol, 2007","reference_id":"17855524","region_id":"DP00726r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"This helix is followed by a variable loop disordered in TyrRSapm as well as in the M. jannaschii apo TyrRS structure 1U7D","_id":"685af523b4ac24d5329d84d6"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-11T08:45:54.785Z","_id":"685af523b4ac24d5329d84d7"},"version":1,"_id":"685af523b4ac24d5329d84d4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2J5B","_id":"685af523b4ac24d5329d84d9"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":150,"end":166,"interaction_partner":[{"db":"UniProt","id":"Q5UPJ7 ","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d84da"}],"reference_html":"Virus-encoded aminoacyl-tRNA synthetases: structural and functional characterization of mimivirus TyrRS and MetRS. <i> Abergel C, Rudinger-Thirion J, Giegé R, Claverie JM. </i> J Virol, 2007","reference_id":"17855524","region_id":"DP00726r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The dimer interface should then appear more flexible than the rest of the molecule, leading to higher B-factor values. This region of the TyrRSapm structure is actually more agitated than its surroundings.","_id":"685af523b4ac24d5329d84db"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-11T08:45:56.495Z","_id":"685af523b4ac24d5329d84dc"},"version":1,"_id":"685af523b4ac24d5329d84d8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2J5B","_id":"685af523b4ac24d5329d84de"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":150,"end":166,"interaction_partner":[],"reference_html":"Virus-encoded aminoacyl-tRNA synthetases: structural and functional characterization of mimivirus TyrRS and MetRS. <i> Abergel C, Rudinger-Thirion J, Giegé R, Claverie JM. </i> J Virol, 2007","reference_id":"17855524","region_id":"DP00726r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Forcing the TyrRSapm dimer into the standard conformation would cost 1,000 Å2 of the buried surface area and greatly reduce its stability. Conversely, forcing the other (canonical) TyrRS dimer into the conformation observed for the TyrRSapm dimer would also be energetically unfavorable, again at a cost of about 1,000 Å2.","_id":"685af523b4ac24d5329d84df"}],"states_connection":[],"term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-11T08:45:57.625Z","_id":"685af523b4ac24d5329d84e0"},"version":1,"_id":"685af523b4ac24d5329d84dd","reference_source":"pmid"}],"__v":0,"disorder_content":0.049132947976878616,"disprot_consensus":{"full":[{"start":150,"end":166,"type":"D"}],"Structural state":[{"start":150,"end":166,"type":"D"}],"Molecular function":[{"start":150,"end":166,"type":"F"}],"Disorder function":[{"start":150,"end":166,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00089","name":"Trypsin","start":24,"end":239}],"gene3D":[{"start":24,"end":65,"id":"2.40.10.10","name":"Trypsin-like serine proteases"},{"start":67,"end":148,"id":"2.40.10.10","name":"Trypsin-like serine proteases"},{"start":149,"end":246,"id":"2.40.10.10","name":"Trypsin-like serine proteases"}]},"uniref50":"UniRef50_P00760","sequence":"MKTFIFLALLGAAVAFPVDDDDKIVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P00760","disprot_id":"DP00728","ncbi_taxon_id":9913,"regions_counter":20,"creator":"droche","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":27,"region_id":"DP00728r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Oxyanion-mediated inhibition of serine proteases. <i> Presnell SR, Patil GS, Mura C, Jude KM, Conley JM, Bertrand JA, Kam CM, Powers JC, Williams LD. </i> Biochemistry, 1998","term_id":"IDPO:0000002","curator_id":"droche","start":18,"term_ontology":"IDPO","curator_name":"Daniel Roche","reference_id":"9836602","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1BJU"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":27,"term_name":"protein binding","start":18,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"GO","curator_name":"Daniel Roche","reference_id":"9836602","version":3,"reference_html":"Oxyanion-mediated inhibition of serine proteases. <i> Presnell SR, Patil GS, Mura C, Jude KM, Conley JM, Bertrand JA, Kam CM, Powers JC, Williams LD. </i> Biochemistry, 1998","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00728r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":155,"region_id":"DP00728r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Oxyanion-mediated inhibition of serine proteases. <i> Presnell SR, Patil GS, Mura C, Jude KM, Conley JM, Bertrand JA, Kam CM, Powers JC, Williams LD. </i> Biochemistry, 1998","term_id":"IDPO:0000002","curator_id":"droche","start":145,"term_ontology":"IDPO","curator_name":"Daniel Roche","reference_id":"9836602","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1BJU"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":155,"term_name":"protein binding","start":145,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"GO","curator_name":"Daniel Roche","reference_id":"9836602","version":3,"reference_html":"Oxyanion-mediated inhibition of serine proteases. <i> Presnell SR, Patil GS, Mura C, Jude KM, Conley JM, Bertrand JA, Kam CM, Powers JC, Williams LD. </i> Biochemistry, 1998","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00728r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":198,"region_id":"DP00728r005","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Oxyanion-mediated inhibition of serine proteases. <i> Presnell SR, Patil GS, Mura C, Jude KM, Conley JM, Bertrand JA, Kam CM, Powers JC, Williams LD. </i> Biochemistry, 1998","term_id":"IDPO:0000002","curator_id":"droche","start":187,"term_ontology":"IDPO","curator_name":"Daniel Roche","reference_id":"9836602","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1BJU"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":198,"term_name":"protein binding","start":187,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"GO","curator_name":"Daniel Roche","reference_id":"9836602","version":3,"reference_html":"Oxyanion-mediated inhibition of serine proteases. <i> Presnell SR, Patil GS, Mura C, Jude KM, Conley JM, Bertrand JA, Kam CM, Powers JC, Williams LD. </i> Biochemistry, 1998","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00728r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":47,"region_id":"DP00728r009","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of a serpin-protease complex shows inhibition by deformation. <i> Huntington JA, Read RJ, Carrell RW. </i> Nature, 2000","statement":[{"text":"some 37% was crystallographically disordered (missing residues 16-41, 62-84, 110-120, 139-156, 1860190, 223-224). The presence within this disordered region of all the previously identified sites of proteolytic cleavage is evidence that the disorder represents the changes occurring in vivo.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":4,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1EZX"}],"reference_id":"11057674","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":47,"term_name":"order to disorder","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of a serpin-protease complex shows inhibition by deformation. <i> Huntington JA, Read RJ, Carrell RW. </i> Nature, 2000","statement":[{"text":"showing a loss of stability and an increase in proteolytic vulnerability of proteases in complexes with serpins.","type":"Results"}],"term_id":"IDPO:0000014","curator_id":"ndavey","start":4,"term_ontology":"IDPO","curator_name":"Norman Davey","reference_id":"11057674","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00728r010","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":47,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of a serpin-protease complex shows inhibition by deformation. <i> Huntington JA, Read RJ, Carrell RW. </i> Nature, 2000","statement":[{"text":"we purifed the complex from a reaction mixture containing an excess of a1-antitrypsin over trypsin","type":"Results"}],"term_id":"GO:0005515","curator_id":"ndavey","start":4,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"11057674","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"imex","id":"IM-14510-4"}],"region_id":"DP00728r011","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":125,"region_id":"DP00728r012","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of a serpin-protease complex shows inhibition by deformation. <i> Huntington JA, Read RJ, Carrell RW. </i> Nature, 2000","statement":[{"text":"some 37% was crystallographically disordered (missing residues 16-41, 62-84, 110-120, 139-156, 1860190, 223-224). The presence within this disordered region of all the previously identified sites of proteolytic cleavage is evidence that the disorder represents the changes occurring in vivo.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":115,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1EZX"}],"reference_id":"11057674","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":125,"term_name":"order to disorder","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of a serpin-protease complex shows inhibition by deformation. <i> Huntington JA, Read RJ, Carrell RW. </i> Nature, 2000","statement":[{"text":"showing a loss of stability and an increase in proteolytic vulnerability of proteases in complexes with serpins.","type":"Results"}],"term_id":"IDPO:0000014","curator_id":"ndavey","start":115,"term_ontology":"IDPO","curator_name":"Norman Davey","reference_id":"11057674","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00728r013","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":125,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of a serpin-protease complex shows inhibition by deformation. <i> Huntington JA, Read RJ, Carrell RW. </i> Nature, 2000","statement":[{"text":"we purifed the complex from a reaction mixture containing an excess of a1-antitrypsin over trypsin","type":"Results"}],"term_id":"GO:0005515","curator_id":"ndavey","start":115,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"11057674","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"imex","id":"IM-14510-4"}],"region_id":"DP00728r014","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":89,"region_id":"DP00728r015","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of a serpin-protease complex shows inhibition by deformation. <i> Huntington JA, Read RJ, Carrell RW. </i> Nature, 2000","statement":[{"text":"some 37% was crystallographically disordered (missing residues 16-41, 62-84, 110-120, 139-156, 1860190, 223-224). The presence within this disordered region of all the previously identified sites of proteolytic cleavage is evidence that the disorder represents the changes occurring in vivo.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":68,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1EZX"}],"reference_id":"11057674","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":89,"term_name":"order to disorder","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of a serpin-protease complex shows inhibition by deformation. <i> Huntington JA, Read RJ, Carrell RW. </i> Nature, 2000","statement":[{"text":"showing a loss of stability and an increase in proteolytic vulnerability of proteases in complexes with serpins.","type":"Results"}],"term_id":"IDPO:0000014","curator_id":"ndavey","start":68,"term_ontology":"IDPO","curator_name":"Norman Davey","reference_id":"11057674","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00728r016","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":89,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of a serpin-protease complex shows inhibition by deformation. <i> Huntington JA, Read RJ, Carrell RW. </i> Nature, 2000","statement":[{"text":"we purifed the complex from a reaction mixture containing an excess of a1-antitrypsin over trypsin","type":"Results"}],"term_id":"GO:0005515","curator_id":"ndavey","start":68,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"11057674","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"imex","id":"IM-14510-4"}],"region_id":"DP00728r017","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":159,"region_id":"DP00728r018","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of a serpin-protease complex shows inhibition by deformation. <i> Huntington JA, Read RJ, Carrell RW. </i> Nature, 2000","statement":[{"text":"some 37% was crystallographically disordered (missing residues 16-41, 62-84, 110-120, 139-156, 1860190, 223-224). The presence within this disordered region of all the previously identified sites of proteolytic cleavage is evidence that the disorder represents the changes occurring in vivo.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":142,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1EZX"}],"reference_id":"11057674","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":159,"term_name":"order to disorder","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of a serpin-protease complex shows inhibition by deformation. <i> Huntington JA, Read RJ, Carrell RW. </i> Nature, 2000","statement":[{"text":"showing a loss of stability and an increase in proteolytic vulnerability of proteases in complexes with serpins.","type":"Results"}],"term_id":"IDPO:0000014","curator_id":"ndavey","start":142,"term_ontology":"IDPO","curator_name":"Norman Davey","reference_id":"11057674","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00728r019","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":159,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of a serpin-protease complex shows inhibition by deformation. <i> Huntington JA, Read RJ, Carrell RW. </i> Nature, 2000","statement":[{"text":"we purifed the complex from a reaction mixture containing an excess of a1-antitrypsin over trypsin","type":"Results"}],"term_id":"GO:0005515","curator_id":"ndavey","start":142,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"11057674","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"imex","id":"IM-14510-4"}],"region_id":"DP00728r020","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P00760","date":"2016-09-14T01:20:37.000Z","acc":"P00760","name":"Cationic trypsin","length":246,"organism":"Bos taurus","dataset":[],"UniParc":"UPI0000110A36","genes":[{"name":{"value":"PRSS1"},"synonyms":[{"value":"TRP1"},{"value":"TRY1","evidences":[{"code":"ECO:0000250","source":{"name":"UniProtKB","id":"P07477","url":"https://www.uniprot.org/uniprot/P07477"}}]},{"value":"TRYP1"}]}],"alphafold_very_low_content":0.04878048780487805,"disorder_content":0.4349593495934959,"disprot_consensus":{"full":[{"start":4,"end":47,"type":"T"},{"start":68,"end":89,"type":"T"},{"start":115,"end":125,"type":"T"},{"start":142,"end":159,"type":"T"},{"start":187,"end":198,"type":"D"}],"Structural state":[{"start":4,"end":47,"type":"D"},{"start":68,"end":89,"type":"D"},{"start":115,"end":125,"type":"D"},{"start":142,"end":159,"type":"D"},{"start":187,"end":198,"type":"D"}],"Molecular function":[{"start":4,"end":47,"type":"F"},{"start":68,"end":89,"type":"F"},{"start":115,"end":125,"type":"F"},{"start":142,"end":159,"type":"F"},{"start":187,"end":198,"type":"F"}],"Structural transition":[{"start":4,"end":47,"type":"T"},{"start":68,"end":89,"type":"T"},{"start":115,"end":125,"type":"T"},{"start":142,"end":159,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00014","name":"Kunitz/Bovine pancreatic trypsin inhibitor domain","start":39,"end":90}],"gene3D":[{"start":36,"end":93,"id":"4.10.410.10","name":"Pancreatic trypsin inhibitor Kunitz domain"}]},"uniref50":"UniRef50_P00974","sequence":"MKMSRLCLSVALLVLLGTLAASTPGCDTSNQAKAQRPDFCLEPPYTGPCKARIIRYFYNAKAGLCQTFVYGGCRAKRNNFKSAEDCMRTCGGAIGPWENL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P00974","disprot_id":"DP00729","ncbi_taxon_id":9913,"regions_counter":3,"creator":"maspromonte","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":38,"region_id":"DP00729r001","released":"2022_03","ec_id":"ECO:0000269","reference_html":"Ultrahigh-resolution structure of a BPTI mutant. <i> Addlagatta A, Krzywda S, Czapinska H, Otlewski J, Jaskolski M. </i> Acta Crystallogr D Biol Crystallogr, 2001","term_id":"IDPO:0000003","curator_id":"maspromonte","start":14,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"experimental evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"molten globule","cross_refs":[{"db":"PDB","id":"1F5R"}],"reference_id":"11320305","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":38,"term_name":"molecular function inhibitor activity","released":"2022_03","ec_name":"experimental evidence used in manual assertion","reference_html":"Ultrahigh-resolution structure of a BPTI mutant. <i> Addlagatta A, Krzywda S, Czapinska H, Otlewski J, Jaskolski M. </i> Acta Crystallogr D Biol Crystallogr, 2001","term_id":"GO:0140678","curator_id":"maspromonte","start":14,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"11320305","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000269","region_id":"DP00729r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":38,"term_name":"protein binding","released":"2022_03","ec_name":"experimental evidence used in manual assertion","reference_html":"Ultrahigh-resolution structure of a BPTI mutant. <i> Addlagatta A, Krzywda S, Czapinska H, Otlewski J, Jaskolski M. </i> Acta Crystallogr D Biol Crystallogr, 2001","term_id":"GO:0005515","curator_id":"maspromonte","start":14,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"11320305","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000269","region_id":"DP00729r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P00974","date":"2016-09-08T22:14:25.000Z","acc":"P00974","name":"Pancreatic trypsin inhibitor","length":100,"organism":"Bos taurus","dataset":[],"UniParc":"UPI000014B62A","genes":[],"alphafold_very_low_content":0.05,"disorder_content":0.25,"disprot_consensus":{"full":[{"start":14,"end":38,"type":"D"}],"Structural state":[{"start":14,"end":38,"type":"D"}],"Molecular function":[{"start":14,"end":38,"type":"F"}]}},{"features":{"pfam":[{"id":"PF13499","name":"EF-hand domain pair","start":43,"end":107}],"gene3D":[{"start":2,"end":109,"id":"1.10.238.10","name":"EF-hand"}]},"uniref50":"UniRef50_P02631","sequence":"MSITDILSAEDIAAALQECQDPDTFEPQKFFQTSGLSKMSASQVKDIFRFIDNDQSGYLDGDELKYFLQKFQSDARELTESETKSLMDAADNDGDGKIGADEFQEMVHS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_P02631","disprot_id":"DP00730","ncbi_taxon_id":10116,"regions_counter":9,"creator":"esalladini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":62,"region_id":"DP00730r006","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of Ca2+-free rat beta-parvalbumin (oncomodulin). <i> Henzl MT, Tanner JJ. </i> Protein Sci, 2007","term_id":"IDPO:0000002","curator_id":"fquaglia","start":51,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17766386","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2NLN"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":62,"term_name":"order to disorder","start":51,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17766386","version":3,"reference_html":"Solution structure of Ca2+-free rat beta-parvalbumin (oncomodulin). <i> Henzl MT, Tanner JJ. </i> Protein Sci, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000014","ec_id":"ECO:0006165","region_id":"DP00730r008","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":62,"term_name":"ion binding","start":51,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"17766386","version":4,"reference_html":"Solution structure of Ca2+-free rat beta-parvalbumin (oncomodulin). <i> Henzl MT, Tanner JJ. </i> Protein Sci, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0043167","ec_id":"ECO:0006165","region_id":"DP00730r009","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P02631","date":"2016-09-13T15:41:23.000Z","acc":"P02631","name":"Oncomodulin","length":109,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI0000170A8D","genes":[{"name":{"value":"Ocm"}}],"alphafold_very_low_content":0,"disorder_content":0.11009174311926606,"disprot_consensus":{"full":[{"start":51,"end":62,"type":"T"}],"Structural state":[{"start":51,"end":62,"type":"D"}],"Structural transition":[{"start":51,"end":62,"type":"T"}],"Molecular function":[{"start":51,"end":62,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01742","name":"Clostridial neurotoxin zinc protease","start":4,"end":392},{"id":"PF07951","name":"Clostridium neurotoxin, C-terminal receptor binding","start":1063,"end":1250},{"id":"PF07952","name":"Clostridium neurotoxin, Translocation domain","start":519,"end":838},{"id":"PF07953","name":"Clostridium neurotoxin, N-terminal receptor binding","start":859,"end":1054}],"gene3D":[{"start":517,"end":848,"id":"1.20.1120.10","name":"Clostridium botulinum neurotoxin b, \"coiled-coil\" domain"},{"start":849,"end":1074,"id":"2.60.120.200","name":"2.60.120.200"},{"start":1075,"end":1251,"id":"2.80.10.50","name":"2.80.10.50"},{"start":1,"end":516,"id":"3.90.1240.10","name":"Metalloproteases (\"zincins\"), catalytic domain like"}]},"uniref50":"UniRef50_A7GBG3","sequence":"MPKINSFNYNDPVNDRTILYIKPGGCQEFYKSFNIMKNIWIIPERNVIGTTPQDFHPPTSLKNGDSSYYDPNYLQSDEEKDRFLKIVTKIFNRINNNLSGGILLEELSKANPYLGNDNTPDNQFHIGDASAVEIKFSNGSQDILLPNVIIMGAEPDLFETNSSNISLRNNYMPSNHRFGSIAIVTFSPEYSFRFNDNCMNEFIQDPALTLMHELIHSLHGLYGAKGITTKYTITQKQNPLITNIRGTNIEEFLTFGGTDLNIITSAQSNDIYTNLLADYKKIASKLSKVQVSNPLLNPYKDVFEAKYGLDKDASGIYSVNINKFNDIFKKLYSFTEFDLRTKFQVKCRQTYIGQYKYFKLSNLLNDSIYNISEGYNINNLKVNFRGQNANLNPRIITPITGRGLVKKIIRFCKNIVSVKGIRKSICIEINNGELFFVASENSYNDDNINTPKEIDDTVTSNNNYENDLDQVILNFNSESAPGLSDEKLNLTIQNDAYIPKYDSNGTSDIEQHDVNELNVFFYLDAQKVPEGENNVNLTSSIDTALLEQPKIYTFFSSEFINNVNKPVQAALFVSWIQQVLVDFTTEANQKSTVDKIADISIVVPYIGLALNIGNEAQKGNFKDALELLGAGILLEFEPELLIPTILVFTIKSFLGSSDNKNKVIKAINNALKERDEKWKEVYSFIVSNWMTKINTQFNKRKEQMYQALQNQVNAIKTIIESKYNSYTLEEKNELTNKYDIKQIENELNQKVSIAMNNIDRFLTESSISYLMKIINEVKINKLREYDENVKTYLLNYIIQHGSILGESQQELNSMVTDTLNNSIPFKLSSYTDDKILISYFNKFFKRIKSSSVLNMRYKNDKYVDTSGYDSNININGDVYKYPTNKNQFGIYNDKLSEVNISQNDYIIYDNKYKNFSISFWVRIPNYDNKIVNVNNEYTIINCMRDNNSGWKVSLNHNEIIWTFEDNRGINQKLAFNYGNANGISDYINKWIFVTITNDRLGDSKLYINGNLIDQKSILNLGNIHVSDNILFKIVNCSYTRYIGIRYFNIFDKELDETEIQTLYSNEPNTNILKDFWGNYLLYDKEYYLLNVLKPNNFIDRRKDSTLSINNIRSTILLANRLYSGIKVKIQRVNNSSTNDNLVRKNDQVYINFVASKTHLFPLYADTATTNKEKTIKISSSGNRFNQVVVMNSVGNCTMNFKNNNGNNIGLLGFKADTVVASTWYYTHMRDHTNSNGCFWNFISEEHGWQEK","taxonomy":["Bacteria","Firmicutes","Clostridia","Eubacteriales","Clostridiaceae","Clostridium"],"uniref90":"UniRef90_Q00496","disprot_id":"DP00732","dataset":["Unicellular toxins and antitoxins","Bacterial virulence-related proteins"],"ncbi_taxon_id":1491,"regions_counter":4,"creator":"rdavidovic","regions":[{"region_id":"DP00732r003","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T11:06:47.502Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":245,"term_id":"IDPO:0000002","start":235,"version":3,"statement":[{"text":"The final model is complete, except for residues 234-244 and the 10 C-terminal residues in both molecules because of weak electron density, indicating that the region may be disordered.","type":"Methods"},{"text":"In the mutant (b), the active site is partly covered by the loop 234-244 (top left of the figure), which is missing in the wild type.","type":"Figure"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"15157097","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1T3A"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"rpancsa","reference_html":"Structural analysis of botulinum neurotoxin type E catalytic domain and its mutant Glu212-->Gln reveals the pivotal role of the Glu212 carboxylate in the catalytic pathway. <i> Agarwal R, Eswaramoorthy S, Kumaran D, Binz T, Swaminathan S. </i> Biochemistry, 2004","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00732r004","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T11:06:48.206Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":422,"term_id":"IDPO:0000002","start":413,"version":3,"statement":[{"text":"The final model is complete, except for residues 234-244 and the 10 C-terminal residues in both molecules because of weak electron density, indicating that the region may be disordered.","type":"Methods"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"15157097","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1T3A"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"rpancsa","reference_html":"Structural analysis of botulinum neurotoxin type E catalytic domain and its mutant Glu212-->Gln reveals the pivotal role of the Glu212 carboxylate in the catalytic pathway. <i> Agarwal R, Eswaramoorthy S, Kumaran D, Binz T, Swaminathan S. </i> Biochemistry, 2004","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q00496","date":"2016-09-13T14:01:10.000Z","acc":"Q00496","name":"Botulinum neurotoxin type E","length":1251,"organism":"Clostridium botulinum","UniParc":"UPI000016EA7F","genes":[{"name":{"value":"botE","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"1541280","url":"http://www.ncbi.nlm.nih.gov/pubmed/1541280","alternativeUrl":"https://europepmc.org/abstract/MED/1541280"}}]}}],"alphafold_very_low_content":0.017585931254996003,"disorder_content":0.016786570743405275,"disprot_consensus":{"full":[{"start":235,"end":245,"type":"D"},{"start":413,"end":422,"type":"D"}],"Structural state":[{"start":235,"end":245,"type":"D"},{"start":413,"end":422,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00010","name":"Helix-loop-helix DNA-binding domain","start":35,"end":83},{"id":"PF00989","name":"PAS fold","start":110,"end":177},{"id":"PF14598","name":"PAS domain","start":274,"end":377}],"gene3D":[{"start":42,"end":118,"id":"4.10.280.10","name":"Helix-loop-helix DNA-binding domain"},{"start":263,"end":384,"id":"3.30.450.20","name":"PAS domain"},{"start":119,"end":262,"id":"3.30.450.20","name":"PAS domain"}]},"uniref50":"UniRef50_O08785","sequence":"MVFTVSCSKMSSIVDRDDSSIFDGLVEEDDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKETTAQSDASEIRQDWKPTFLSNEEFTQLMLEALDGFFLAIMTDGSIIYVSESVTSLLEHLPSDLVDQSIFNFIPEGEHSEVYKILSTHLLESDSLTPEYLKSKNQLEFCCHMLRGTIDPKEPSTYEYVRFIGNFKSLTSVSTSTHNGFEGTIQRTHRPSYEDRVCFVATVRLATPQFIKEMCTVEEPNEEFTSRHSLEWKFLFLDHRAPPIIGYLPFEVLGTSGYDYYHVDDLENLAKCHEHLMQYGKGKSCYYRFLTKGQQWIWLQTHYYITYHQWNSRPEFIVCTHTVVSYAEVRAERRRELGIEESLPETAADKSQDSGSDNRINTVSLKEALERFDHSPTPSASSRSSRKSSHTAVSDPSSTPTKIPTDTSTPPRQHLPAHEKMTQRRSSFSSQSINSQSVGPSLTQPAMSQAANLPIPQGMSQFQFSAQLGAMQHLKDQLEQRTRMIEANIHRQQEELRKIQEQLQMVHGQGLQMFLQQSNPGLNFGSVQLSSGNSNIQQLTPVNMQGQVVPANQVQSGHISTGQHMIQQQTLQSTSTQQSQQSVMSGHSQQTSLPSQTPSTLTAPLYNTMVISQPAAGSMVQIPSSMPQNSTQSATVTTFTQDRQIRFSQGQQLVTKLVTAPVACGAVMVPSTMLMGQVVTAYPTFATQQQQAQTLSVTQQQQQQQQQPPQQQQQQQQSSQEQQLPSVQQPAQAQLGQPPQQFLQTSRLLHGNPSTQLILSAAFPLQQSTFPPSHHQQHQPQQQQQLPRHRTDSLTDPSKVQPQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_O08785","disprot_id":"DP00734","ncbi_taxon_id":10090,"regions_counter":6,"creator":"maspromonte","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":107,"region_id":"DP00734r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the heterodimeric CLOCK:BMAL1 transcriptional activator complex. <i> Huang N, Chelliah Y, Shan Y, Taylor CA, Yoo SH, Partch C, Green CB, Zhang H, Takahashi JS. </i> Science, 2012","term_id":"IDPO:0000002","curator_id":"maspromonte","start":89,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4F3L"}],"reference_id":"22653727","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":107,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of the heterodimeric CLOCK:BMAL1 transcriptional activator complex. <i> Huang N, Chelliah Y, Shan Y, Taylor CA, Yoo SH, Partch C, Green CB, Zhang H, Takahashi JS. </i> Science, 2012","term_id":"GO:0005515","curator_id":"maspromonte","start":89,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"22653727","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00734r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":248,"region_id":"DP00734r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the heterodimeric CLOCK:BMAL1 transcriptional activator complex. <i> Huang N, Chelliah Y, Shan Y, Taylor CA, Yoo SH, Partch C, Green CB, Zhang H, Takahashi JS. </i> Science, 2012","term_id":"IDPO:0000002","curator_id":"maspromonte","start":223,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4F3L"}],"reference_id":"22653727","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":248,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of the heterodimeric CLOCK:BMAL1 transcriptional activator complex. <i> Huang N, Chelliah Y, Shan Y, Taylor CA, Yoo SH, Partch C, Green CB, Zhang H, Takahashi JS. </i> Science, 2012","term_id":"GO:0005515","curator_id":"maspromonte","start":223,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"22653727","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00734r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":269,"region_id":"DP00734r005","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the heterodimeric CLOCK:BMAL1 transcriptional activator complex. <i> Huang N, Chelliah Y, Shan Y, Taylor CA, Yoo SH, Partch C, Green CB, Zhang H, Takahashi JS. </i> Science, 2012","term_id":"IDPO:0000002","curator_id":"maspromonte","start":258,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4F3L"}],"reference_id":"22653727","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":269,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of the heterodimeric CLOCK:BMAL1 transcriptional activator complex. <i> Huang N, Chelliah Y, Shan Y, Taylor CA, Yoo SH, Partch C, Green CB, Zhang H, Takahashi JS. </i> Science, 2012","term_id":"GO:0005515","curator_id":"maspromonte","start":258,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"22653727","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00734r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_O08785","date":"2016-09-08T22:58:26.000Z","acc":"O08785","name":"Circadian locomoter output cycles protein kaput","length":855,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000023145","genes":[{"name":{"value":"Clock"}}],"alphafold_very_low_content":0.5345029239766081,"disorder_content":0.06666666666666667,"disprot_consensus":{"full":[{"start":89,"end":107,"type":"D"},{"start":223,"end":248,"type":"D"},{"start":258,"end":269,"type":"D"}],"Structural state":[{"start":89,"end":107,"type":"D"},{"start":223,"end":248,"type":"D"},{"start":258,"end":269,"type":"D"}],"Molecular function":[{"start":89,"end":107,"type":"F"},{"start":223,"end":248,"type":"F"},{"start":258,"end":269,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02170","name":"PAZ domain","start":242,"end":364},{"id":"PF02171","name":"Piwi domain","start":518,"end":817},{"id":"PF08699","name":"Argonaute linker 1 domain","start":176,"end":226},{"id":"PF16486","name":"N-terminal domain of argonaute","start":36,"end":166},{"id":"PF16487","name":"Mid domain of argonaute","start":429,"end":510},{"id":"PF16488","name":"Argonaute linker 2 domain","start":374,"end":420}],"gene3D":[{"start":582,"end":859,"id":"3.30.420.10","name":"Ribonuclease H-like superfamily/Ribonuclease H"},{"start":412,"end":581,"id":"3.40.50.2300","name":"3.40.50.2300"},{"start":221,"end":353,"id":"2.170.260.10","name":"paz domain"}]},"uniref50":"UniRef50_Q9UKV8","sequence":"MYSGAGPALAPPAPPPPIQGYAFKPPPRPDFGTSGRTIKLQANFFEMDIPKIDIYHYELDIKPEKCPRRVNREIVEHMVQHFKTQIFGDRKPVFDGRKNLYTAMPLPIGRDKVELEVTLPGEGKDRIFKVSIKWVSCVSLQALHDALSGRLPSVPFETIQALDVVMRHLPSMRYTPVGRSFFTASEGCSNPLGGGREVWFGFHQSVRPSLWKMMLNIDVSATAFYKAQPVIEFVCEVLDFKSIEEQQKPLTDSQRVKFTKEIKGLKVEITHCGQMKRKYRVCNVTRRPASHQTFPLQQESGQTVECTVAQYFKDRHKLVLRYPHLPCLQVGQEQKHTYLPLEVCNIVAGQRCIKKLTDNQTSTMIRATARSAPDRQEEISKLMRSASFNTDPYVREFGIMVKDEMTDVTGRVLQPPSILYGGRNKAIATPVQGVWDMRNKQFHTGIEIKVWAIACFAPQRQCTEVHLKSFTEQLRKISRDAGMPIQGQPCFCKYAQGADSVEPMFRHLKNTYAGLQLVVVILPGKTPVYAEVKRVGDTVLGMATQCVQMKNVQRTTPQTLSNLCLKINVKLGGVNNILLPQGRPPVFQQPVIFLGADVTHPPAGDGKKPSIAAVVGSMDAHPNRYCATVRVQQHRQEIIQDLAAMVRELLIQFYKSTRFKPTRIIFYRDGVSEGQFQQVLHHELLAIREACIKLEKDYQPGITFIVVQKRHHTRLFCTDKNERVGKSGNIPAGTTVDTKITHPTEFDFYLCSHAGIQGTSRPSHYHVLWDDNRFSSDELQILTYQLCHTYVRCTRSVSIPAPAYYAHLVAFRARYHLVDKEHDSAEGSHTSGQSNGRDHQALAKAVQVHQDTLRTMYFA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UKV8","disprot_id":"DP00736","ncbi_taxon_id":9606,"regions_counter":8,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":22,"region_id":"DP00736r001","released":"2022_12","ec_id":"ECO:0006220","reference_html":"The crystal structure of human Argonaute2. <i> Schirle NT, MacRae IJ. </i> Science, 2012","term_id":"IDPO:0000002","curator_id":"maspromonte","start":1,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","reference_id":"22539551","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-10-13T14:08:07.100Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-4937-6952","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Grey letters indicate disordered loops not observed in the Ago2 crystal structure.","type":"Supplementary material"}],"cross_refs":[{"db":"PDB","id":"4OLA"},{"db":"PDB","id":"4OLB"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15882","entry_name":"phenol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17824","entry_name":"propan-2-ol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"27897","entry_name":"tryptophan"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS000080E10F_9606","statements":[{"type":"Curator statement","text":"This misc RNA sequence is 10 nucleotides long (PDB 4OLA chain B) 5'-AAAAAAAAAU "}]}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser387Asp","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"The best diffracting construct, which was used for both reported structures had five point mutations: S387D, S824A, S828D, S831D, and S834A"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser824Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"The best diffracting construct, which was used for both reported structures had five point mutations: S387D, S824A, S828D, S831D, and S834A"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser828Asp","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"The best diffracting construct, which was used for both reported structures had five point mutations: S387D, S824A, S828D, S831D, and S834A"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser831Asp","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"The best diffracting construct, which was used for both reported structures had five point mutations: S387D, S824A, S828D, S831D, and S834A"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser834Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"The best diffracting construct, which was used for both reported structures had five point mutations: S387D, S824A, S828D, S831D, and S834A"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-17T13:35:00.550Z"}},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":22,"term_name":"flexible N-terminal tail","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"maspromonte","released":"2023_06","term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","reference_id":"22539551","version":5,"reference_html":"The crystal structure of human Argonaute2. <i> Schirle NT, MacRae IJ. </i> Science, 2012","date":"2023-06-22T13:00:36.024Z","term_id":"IDPO:0000032","ec_id":"ECO:0006220","region_id":"DP00736r002","curator_orcid":"0000-0002-4937-6952","ec_go":"EXP","disprot_namespace":"Disorder function","cross_refs":[{"db":"PDB","id":"4OLA"},{"db":"PDB","id":"4OLB"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser387Asp","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"The best diffracting construct, which was used for both reported structures had five point mutations: S387D, S824A, S828D, S831D, and S834A"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser824Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"The best diffracting construct, which was used for both reported structures had five point mutations: S387D, S824A, S828D, S831D, and S834A"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser828Asp","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"The best diffracting construct, which was used for both reported structures had five point mutations: S387D, S824A, S828D, S831D, and S834A"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser831Asp","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"The best diffracting construct, which was used for both reported structures had five point mutations: S387D, S824A, S828D, S831D, and S834A"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser834Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"The best diffracting construct, which was used for both reported structures had five point mutations: S387D, S824A, S828D, S831D, and S834A"}]}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15882","entry_name":"phenol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17824","entry_name":"propan-2-ol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"27897","entry_name":"tryptophan"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS000080E10F_9606","statements":[{"type":"Curator statement","text":"This misc RNA sequence is 10 nucleotides long (PDB 4OLA chain B) 5'-AAAAAAAAAU"}]}],"statement":[{"text":"The authors do not specify about the disordered region (1-22), but these residues are missing in the strucutre.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-22T14:05:44.735Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":838,"region_id":"DP00736r003","released":"2022_12","ec_id":"ECO:0006220","reference_html":"The crystal structure of human Argonaute2. <i> Schirle NT, MacRae IJ. </i> Science, 2012","term_id":"IDPO:0000002","curator_id":"maspromonte","start":818,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","reference_id":"22539551","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-10-18T16:02:29.073Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-4937-6952","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Grey letters indicate disordered loops not observed in the Ago2 crystal structure.","type":"Supplementary material"}],"cross_refs":[{"db":"PDB","id":"4OLA"},{"db":"PDB","id":"4OLB"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15882","entry_name":"phenol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17824","entry_name":"propan-2-ol"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS000080E10F_9606","statements":[{"type":"Curator statement","text":"This misc RNA sequence is 10 nucleotides long (PDB 4OLA chain B) 5'-AAAAAAAAAU "}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"27897","entry_name":"tryptophan"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser387Asp","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"The best diffracting construct, which was used for both reported structures had five point mutations: S387D, S824A, S828D, S831D, and S834A"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser824Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"The best diffracting construct, which was used for both reported structures had five point mutations: S387D, S824A, S828D, S831D, and S834A"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser828Asp","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"The best diffracting construct, which was used for both reported structures had five point mutations: S387D, S824A, S828D, S831D, and S834A"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser831Asp","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"The best diffracting construct, which was used for both reported structures had five point mutations: S387D, S824A, S828D, S831D, and S834A"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser834Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"The best diffracting construct, which was used for both reported structures had five point mutations: S387D, S824A, S828D, S831D, and S834A"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-25T19:08:13.517Z"}},{"start":820,"end":837,"reference_id":"27380263","reference_source":"pmid","reference_html":"Structural Analysis of Human Argonaute-2 Bound to a Modified siRNA Guide. <i> Schirle NT, Kinberger GA, Murray HF, Lima WF, Prakash TP, MacRae IJ. </i> J Am Chem Soc, 2016","date":"2022-10-18T15:59:58.573Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"5JS2"},{"db":"PDB","id":"5JS1"}],"region_id":"DP00736r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15882","entry_name":"phenol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18367","entry_name":"phosphate(3-)"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS0000A76350_32630","statements":[{"type":"Curator statement","text":"siRNA from synthetic construct (PDB 5JS1, chain B) 5'-UUAUCUAUAAUGAUCAGGUAA, Length: 21 nucleotides"},{"type":"Curator statement","text":"siRNA from synthetic construct (PDB 5JS2, chain B) 5'-XUAUCU, Length: 6 nucleotides"}]}],"statement":[{"text":"The PDB evidence shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser387Asp","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-25T19:08:14.447Z"}},{"start":1,"end":22,"reference_id":"27380263","reference_source":"pmid","reference_html":"Structural Analysis of Human Argonaute-2 Bound to a Modified siRNA Guide. <i> Schirle NT, Kinberger GA, Murray HF, Lima WF, Prakash TP, MacRae IJ. </i> J Am Chem Soc, 2016","date":"2022-10-18T16:00:13.623Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"5JS2"},{"db":"PDB","id":"5JS1"}],"region_id":"DP00736r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15882","entry_name":"phenol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18367","entry_name":"phosphate(3-)"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS0000A76350_32630","statements":[{"type":"Curator statement","text":"siRNA from synthetic construct (PDB 5JS1, chain B) 5'-UUAUCUAUAAUGAUCAGGUAA, Length: 21 nucleotides"},{"type":"Curator statement","text":"siRNA from synthetic construct (PDB 5JS2, chain B) 5'-XUAUCU, Length: 6 nucleotides"}]}],"statement":[{"text":"The PDB evidence shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser387Asp","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-25T19:08:46.535Z"}},{"start":1,"end":21,"reference_id":"25359968","reference_source":"pmid","reference_html":"Structural basis for microRNA targeting. <i> Schirle NT, Sheu-Gruttadauria J, MacRae IJ. </i> Science, 2014","date":"2022-10-18T16:00:52.197Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"4W5N"},{"db":"PDB","id":"4W5T"},{"db":"PDB","id":"4W5Q"},{"db":"PDB","id":"4W5O"},{"db":"PDB","id":"4W5R"}],"region_id":"DP00736r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15882","entry_name":"phenol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17824","entry_name":"propan-2-ol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18367","entry_name":"phosphate(3-)"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS000080E33F_32630","statements":[{"type":"Curator statement","text":"Interacting guide RNA with sequence 5'-UUCACAUUGCCCAAGUCUCUU.\nCross reference PDB:4W5N, 4W5Q, 4W5T, 4W5O, 4W5R chain B"},{"type":"Curator statement","text":"Interacting guide RNA with sequence 5'-AAAUGUGAAAA.\nCross reference PDB:4W5Q, 4W5T, 4W5O chain D"},{"type":"Curator statement","text":"Interacting guide RNA with sequence 5'-CCAAAUGUGAAAA.\nCross reference PDB:4W5R chain D"}]}],"statement":[{"text":"The PDB evidence shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser387Asp","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-25T19:08:39.295Z"}},{"start":822,"end":835,"reference_id":"25359968","reference_source":"pmid","reference_html":"Structural basis for microRNA targeting. <i> Schirle NT, Sheu-Gruttadauria J, MacRae IJ. </i> Science, 2014","date":"2022-10-18T16:00:25.999Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"4W5N"},{"db":"PDB","id":"4W5O"},{"db":"PDB","id":"4W5R"},{"db":"PDB","id":"4W5T"},{"db":"PDB","id":"4W5Q"}],"region_id":"DP00736r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15882","entry_name":"phenol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17824","entry_name":"propan-2-ol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18367","entry_name":"phosphate(3-)"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS000080E33F_32630","statements":[{"type":"Curator statement","text":"Interacting guide RNA with sequence 5'-UUCACAUUGCCCAAGUCUCUU. Cross reference PDB:4W5N, 4W5Q, 4W5T, 4W5O, 4W5R chain B"},{"type":"Curator statement","text":"Interacting guide RNA with sequence 5'-AAAUGUGAAAA. Cross reference PDB:4W5Q, 4W5T, 4W5O chain D"},{"type":"Curator statement","text":"Interacting guide RNA with sequence 5'-CCAAAUGUGAAAA. Cross reference PDB:4W5R chain D"}]}],"statement":[{"text":"The PDB evidence shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser387Asp","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-25T19:08:43.541Z"}}],"released":"2016_10","uniref100":"UniRef100_Q9UKV8","date":"2016-09-18T23:38:54.000Z","acc":"Q9UKV8","name":"Protein argonaute-2","length":859,"organism":"Homo sapiens","dataset":["NDDs-related proteins","Condensates-related proteins","RNA-binding proteins"],"UniParc":"UPI000012D07E","genes":[{"name":{"value":"AGO2"},"synonyms":[{"value":"EIF2C2"}]}],"alphafold_very_low_content":0.03841676367869616,"disorder_content":0.050058207217694994,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"},{"start":818,"end":838,"type":"D"}],"Structural state":[{"start":1,"end":22,"type":"D"},{"start":818,"end":838,"type":"D"}],"Disorder function":[{"start":1,"end":22,"type":"F"}]}},{"features":{"pfam":[{"id":"PF09048","name":"Cro","start":1,"end":60}],"gene3D":[{"start":1,"end":66,"id":"3.30.240.10","name":"CRO Repressor"}]},"uniref50":"UniRef50_P03040","sequence":"MEQRITLKDYAMRFGQTKTAKDLGVYQSAINKAIHAGRKIFLTINADGSVYAEEVKPFPSNKKTTA","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Uroviricota","Caudoviricetes","Caudovirales","Siphoviridae","Lambdavirus"],"uniref90":"UniRef90_P03040","disprot_id":"DP00741","ncbi_taxon_id":10710,"regions_counter":31,"creator":"ktsirigos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":66,"region_id":"DP00741r031","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A trade between similar but nonequivalent intrasubunit and intersubunit contacts in Cro dimer evolution. <i> Newlove T, Atkinson KR, Van Dorn LO, Cordes MH. </i> Biochemistry, 2006","statement":[{"text":"Residues 2−4 at the N-terminus and 56−66 at the C-terminus of λ-WDQ showed significant NOE reductions and increases in T2, suggestive of increased mobility, in approximate agreement with the location of poorly defined regions in the ensemble.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jbergier","start":56,"term_ontology":"IDPO","curator_name":"Julian Bergier","reference_id":"16700549","version":4,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2A63"},{"db":"BMRB","id":"6771"}],"term_name":"disorder","curator_orcid":"0000-0003-2206-9968","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala33Trp","start":null,"end":null,"position":null,"statements":[{"type":"Introduction","text":"We now report the solution structure of a λ Cro monomer containing the A33W and F58D mutations."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe58Asp","start":null,"end":null,"position":null,"statements":[{"type":"Introduction","text":"We now report the solution structure of a λ Cro monomer containing the A33W and F58D mutations."}]}],"sequence_construct":"MEQRITLKDYAMRFGQTKTAKDLGVYQSAINKwIHAGRKIFLTINADGSVYAEEVKPdPSNKKTTA","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-29T13:38:01.796Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P03040","date":"2016-09-13T14:49:58.000Z","acc":"P03040","name":"Regulatory protein cro","length":66,"organism":"Escherichia phage lambda","dataset":["Viral proteins"],"UniParc":"UPI000002E129","genes":[{"name":{"value":"cro"},"olnNames":[{"value":"lambdap57"}]}],"disorder_content":0.16666666666666666,"disprot_consensus":{"full":[{"start":56,"end":66,"type":"D"}],"Structural state":[{"start":56,"end":66,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00307","name":"Calponin homology (CH) domain","start":346,"end":446}],"gene3D":[{"start":344,"end":450,"id":"1.10.418.10","name":"Calponin-like domain"}]},"uniref50":"UniRef50_Q99LM3","sequence":"MEQTEGNSSEDGTTVSPTAGNLETPGSQGIAEEVAEGTVGTSDKEGPSDWAEHLCKAASKSGESGGSPGEASILDELKTDLQGEARGKDEAQGDLAEEKVGKEDTTAASQEDTGKKEETKPEPNEVREKEEAMLASEKQKVDEKETNLESKEKSDVNDKAKPEPKEDAGAEVTVNEAETESQEEADVKDQAKPELPEVDGKETGSDTKELVEPESPTEEQEQGKENESEERAAVIPSSPEEWPESPTDEGPSLSPDGLAPESTGETSPSASESSPSEVPGSPTEPQPSEKKKDRAPERRVSAPSRPRGPRAQNRKAIMDKFGGAASGPTALFRNTKAAGAAIGGVKNMLLEWCRAMTRNYEHVDIQNFSSSWSSGMAFCALIHKFFPEAFDYAELDPAKRRHNFTLAFSTAEKLADCAQLLEVDDMVRLAVPDSKCVYTYIQELYRSLVQKGLVKTKKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q99LM3","disprot_id":"DP00742","ncbi_taxon_id":10090,"regions_counter":5,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":341,"region_id":"DP00742r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Intrinsically disordered N-terminus of calponin homology-associated smooth muscle protein (CHASM) interacts with the calponin homology domain to enable tropomyosin binding. <i> MacDonald JA, Ishida H, Butler EI, Ulke-Lemée A, Chappellaz M, Tulk SE, Chik JK, Vogel HJ. </i> Biochemistry, 2012","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22424482","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":341,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"22424482","version":3,"reference_html":"Intrinsically disordered N-terminus of calponin homology-associated smooth muscle protein (CHASM) interacts with the calponin homology domain to enable tropomyosin binding. <i> MacDonald JA, Ishida H, Butler EI, Ulke-Lemée A, Chappellaz M, Tulk SE, Chik JK, Vogel HJ. </i> Biochemistry, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00742r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":341,"region_id":"DP00742r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Intrinsically disordered N-terminus of calponin homology-associated smooth muscle protein (CHASM) interacts with the calponin homology domain to enable tropomyosin binding. <i> MacDonald JA, Ishida H, Butler EI, Ulke-Lemée A, Chappellaz M, Tulk SE, Chik JK, Vogel HJ. </i> Biochemistry, 2012","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22424482","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":341,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"22424482","version":3,"reference_html":"Intrinsically disordered N-terminus of calponin homology-associated smooth muscle protein (CHASM) interacts with the calponin homology domain to enable tropomyosin binding. <i> MacDonald JA, Ishida H, Butler EI, Ulke-Lemée A, Chappellaz M, Tulk SE, Chik JK, Vogel HJ. </i> Biochemistry, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00742r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q99LM3","date":"2016-08-24T16:52:00.000Z","acc":"Q99LM3","name":"Smoothelin-like protein 1","length":459,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000022ABC","genes":[{"name":{"value":"Smtnl1"}}],"alphafold_very_low_content":0.5904139433551199,"disorder_content":0.7429193899782135,"disprot_consensus":{"full":[{"start":1,"end":341,"type":"D"}],"Structural state":[{"start":1,"end":341,"type":"D"}],"Molecular function":[{"start":1,"end":341,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00212","name":"Atrial natriuretic peptide","start":121,"end":146}]},"uniref50":"UniRef50_P01160","sequence":"MSSFSTTTVSFLLLLAFQLLGQTRANPMYNAVSNADLMDFKNLLDHLEEKMPLEDEVVPPQVLSEPNEEAGAALSPLPEVPPWTGEVSPAQRDGGALGRGPWDSSDRSALLKSKLRALLTAPRSLRRSSCFGGRMDRIGAQSGLGCNSFRY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P01160","disprot_id":"DP00747","ncbi_taxon_id":9606,"regions_counter":13,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":123,"region_id":"DP00747r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A 68 residue N-terminal fragment of pro-atrial natriuretic peptide is a monomeric intrinsically unstructured protein. <i> Crimmins DL, Kao JL. </i> J Biochem, 2011","term_id":"IDPO:0000002","curator_id":"esalladini","start":56,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"21508037","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","uniprot_changed":true,"curator_orcid":"0000-0002-5152-5953","statement":[{"text":"Moreover, it was found that the amide resonances disappeared immediately after the freshly prepared protein was dissolved in D2O solution (Fig. 2D). This indicated that the amide protons are accessible to the solvent and the protein has no well-defined hydrogen bonds.","type":"Results"},{"text":"The cross-correlation NH(i) − NH(i + 1) resonance peaks from homonuclear 2D-NOE are essentially absent (supplementary Fig. S1) indicating little overall solution structure for NT-proANP, a result also found for NT-proBNP (11).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":123,"region_id":"DP00747r004","released":"2022_03","ec_id":"ECO:0006198","reference_html":"A 68 residue N-terminal fragment of pro-atrial natriuretic peptide is a monomeric intrinsically unstructured protein. <i> Crimmins DL, Kao JL. </i> J Biochem, 2011","term_id":"IDPO:0000002","curator_id":"esalladini","start":56,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"21508037","version":3,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","uniprot_changed":true,"curator_orcid":"0000-0002-5152-5953","statement":[{"text":"Figure 2B shows the 4°C proton spectra for NT-proANP in 10% D2O. The intensity in the amide region is rather low and confined to a narrow region of ~8–8.6 ppm.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":123,"region_id":"DP00747r008","released":"2022_03","ec_id":"ECO:0007680","reference_html":"A 68 residue N-terminal fragment of pro-atrial natriuretic peptide is a monomeric intrinsically unstructured protein. <i> Crimmins DL, Kao JL. </i> J Biochem, 2011","term_id":"IDPO:0000002","curator_id":"esalladini","start":56,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"21508037","version":3,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","uniprot_changed":true,"curator_orcid":"0000-0002-5152-5953","statement":[{"text":"As myoglobin is known to adopt a compact, folded three-dimensional structure (25), and as the above far-UV CD and NMR data demonstrate that NT-proANP is largely unstructured in physiologic near neutral pH non-denaturing buffer, it is evident that shape, e.g. Rs the Stoke's radius, and not molecular weight is the determining mechanistic factor in SE-HPLC. On the same column, unstructured monomeric NT-proBNP eluted at 20.6′ (data not shown).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":123,"region_id":"DP00747r011","released":"2022_03","ec_id":"ECO:0006204","reference_html":"A 68 residue N-terminal fragment of pro-atrial natriuretic peptide is a monomeric intrinsically unstructured protein. <i> Crimmins DL, Kao JL. </i> J Biochem, 2011","term_id":"IDPO:0000002","curator_id":"esalladini","start":56,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"21508037","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","uniprot_changed":true,"curator_orcid":"0000-0002-5152-5953","statement":[{"text":"Figure 1 displays a room temperature CD spectrum for NT-proANP in a physiologic near neutral pH buffer. A minimum is observed at ~199–200 nm giving a value of –14,800° cm2/dmol indicating that the 68-residue NT-proANP fragment is largely unstructured.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P01160","date":"2016-09-14T18:03:12.000Z","acc":"P01160","name":"Natriuretic peptides A","length":151,"organism":"Homo sapiens","dataset":[],"uniparc":"UPI000000DCD4","genes":[{"name":{"value":"NPPA"},"synonyms":[{"value":"ANP"},{"value":"PND"}]}],"alphafold_very_low_content":0.23841059602649006,"disorder_content":0.4503311258278146,"disprot_consensus":{"full":[{"start":56,"end":123,"type":"D"}],"Structural state":[{"start":56,"end":123,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00017","name":"SH2 domain","start":13,"end":104},{"id":"PF00018","name":"SH3 domain","start":138,"end":184},{"id":"PF07653","name":"Variant SH3 domain","start":239,"end":293}],"gene3D":[{"start":1,"end":215,"id":"3.30.505.10","name":"SH2 domain"},{"start":122,"end":205,"id":"2.30.30.40","name":"SH3 Domains"},{"start":221,"end":296,"id":"2.30.30.40","name":"SH3 Domains"}]},"uniref50":"UniRef50_P46108","sequence":"MAGNFDSEERSSWYWGRLSRQEAVALLQGQRHGVFLVRDSSTSPGDYVLSVSENSRVSHYIINSSGPRPPVPPSPAQPPPGVSPSRLRIGDQEFDSLPALLEFYKIHYLDTTTLIEPVSRSRQGSGVILRQEEAEYVRALFDFNGNDEEDLPFKKGDILRIRDKPEEQWWNAEDSEGKRGMIPVPYVEKYRPASASVSALIGGNQEGSHPQPLGGPEPGPYAQPSVNTPLPNLQNGPIYARVIQKRVPNAYDKTALALEVGELVKVTKINVSGQWEGECNGKRGHFPFTHVRLLDQQNPDEDFS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P46108","disprot_id":"DP00748","ncbi_taxon_id":9606,"regions_counter":13,"creator":"aelofsson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":223,"region_id":"DP00748r003","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK. <i> Kobashigawa Y, Sakai M, Naito M, Yokochi M, Kumeta H, Makino Y, Ogura K, Tanaka S, Inagaki F. </i> Nat Struct Mol Biol, 2007","term_id":"IDPO:0000002","curator_id":"vnugnes","start":192,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-09-01T15:32:10.979Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2EYZ"}],"reference_id":"17515907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The ISC makes contacts with SH2, nSH3 and cSH3. In fact, we identified 54 distance restraints from the ISC to SH2, nSH3 and cSH3, but the other region in the nSH3-cSH3 linker, aside from the ISC, is flexible.","type":"Results"}]},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":223,"term_name":"flexible linker","released":"2022_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK. <i> Kobashigawa Y, Sakai M, Naito M, Yokochi M, Kumeta H, Makino Y, Ogura K, Tanaka S, Inagaki F. </i> Nat Struct Mol Biol, 2007","term_id":"IDPO:0000033","curator_id":"vnugnes","start":192,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"17515907","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2022-09-01T17:20:23.244Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00748r004","ec_go":"EXP","disprot_namespace":"Disorder function","cross_refs":[{"db":"PDB","id":"2EYZ"}],"statement":[{"text":"The ISC makes contacts with SH2, nSH3 and cSH3. In fact, we identified 54 distance restraints from the ISC to SH2, nSH3 and cSH3, but the other region in the nSH3-cSH3 linker, aside from the ISC, is flexible.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":293,"region_id":"DP00748r009","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK. <i> Kobashigawa Y, Sakai M, Naito M, Yokochi M, Kumeta H, Makino Y, Ogura K, Tanaka S, Inagaki F. </i> Nat Struct Mol Biol, 2007","term_id":"IDPO:0000002","curator_id":"vnugnes","start":238,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-09-01T15:42:28.601Z","reference_source":"pmid","term_name":"disorder","reference_id":"17515907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp275Lys","start":null,"end":null,"position":null}],"statement":[{"text":"We recorded the 1H-15N HSQC spectrum of the CRKII mutant containing a W275K mutation. Most of the NMR signals from the ISC as well as from cSH3 in CRKII disappeared for this mutant, and new signals appeared in the disordered region (Supplementary Fig. 4 online). This means that the tertiary structure of cSH3 was disrupted by the W275K mutation, abrogating the interaction between the ISC and cSH3.","type":"Results"}]},{"start":219,"end":223,"reference_id":"17515907","reference_source":"pmid","reference_html":"Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK. <i> Kobashigawa Y, Sakai M, Naito M, Yokochi M, Kumeta H, Makino Y, Ogura K, Tanaka S, Inagaki F. </i> Nat Struct Mol Biol, 2007","date":"2022-09-01T15:47:35.697Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP00748r013","statement":[{"text":"The protein kinase cABL phosphorylates Tyr221 in the SH3 linker.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P46108","date":"2016-09-08T10:50:07.000Z","acc":"P46108","name":"Adapter molecule crk","length":304,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012845B","genes":[{"name":{"value":"CRK"}}],"alphafold_very_low_content":0.2236842105263158,"disorder_content":0.2894736842105263,"disprot_consensus":{"full":[{"start":192,"end":223,"type":"D"},{"start":238,"end":293,"type":"D"}],"Structural state":[{"start":192,"end":223,"type":"D"},{"start":238,"end":293,"type":"D"}],"Disorder function":[{"start":192,"end":223,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02430","name":"Apical membrane antigen 1","start":13,"end":439}],"gene3D":[{"start":344,"end":443,"id":"4.10.1010.10","name":"Apical membrane antigen 1"},{"start":1,"end":54,"id":"3.50.4.10","name":"Hepatocyte Growth Factor"},{"start":275,"end":343,"id":"3.50.4.10","name":"Hepatocyte Growth Factor"},{"start":186,"end":268,"id":"3.50.4.10","name":"Hepatocyte Growth Factor"}]},"uniref50":"UniRef50_P22621","sequence":"PTVERSTRMGNPWKAFMEKYDIERTHSSGVRVDLGEDAEVENAKYRIPAGRCPVFGKGIVIENSDVSFLRPVATGDQKLKDGGFAFPNANDHISPMTLANLKERYKDNVEMMKLNDIALCRTHAASFVMAGDQNSSYRHPAVYDEKEKTCHMLYLSAQENMGPRYCSPDAQNRDAVFCFKPDKNESFENLVYLSKNVRNDWDKKCPRKNLGNAKFGLWVDGNCEEIPYVKEVEAEDLRECNRIVFGASASDQPTQYEEEMTDYQKIQQGFRQNNREMIKSAFLPVGAFNSDNFKSKGRGFNWANFDSVKKKCYIFNTKPTCLINDKNFIATTALSHPQEVDLEFPCSIYKDEIEREIKKQSRNMNLYSVDGERIVLPRIFISNDKESIKCPCEPERISNSTCNFYVCNCVEKRAEIKENNQVVIKEEFRNYYENGEEKSNKQMLL","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Plasmodium)"],"uniref90":"UniRef90_T1SCW6","disprot_id":"DP00749","ncbi_taxon_id":5855,"regions_counter":6,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":445,"region_id":"DP00749r006","start":413,"term_id":"IDPO:0000002","statement":[{"text":"Although the complete recombinant PvAMA1 ectoplasmic region (residues 43–487) and domains II and III of PfAMA1 (residues 303 to 544) were complexed with Fab F8.12.19 in the protein preparations used for crystallisation, only a small but contiguous segment of domain III from these two homologues could be identified in the electron density: the 34-residue segment from Ile421 to Lys454 in PvAMA1 and the equivalent 34-residue segment from Ile479 to Arg512 in PfAMA1 (Figure 4). This part of the antigen could be identified readily in the electron density by the cystine knot formed with Cys432-Cys449 and Cys434-Cys451 in PvAMA1 and Cys490-Cys507 and Cys492-Cys509 in PfAMA1. Additional electron density, observed in the final difference maps of both PvAMA1 and PfAMA1, did not coincide with the complete, superimposed PvAMA1 structure (PDB entry 1W8K) (Figure 5). This region is connected to modelled part of the antigen via the Cys388-Cys444 bridge in PvAMA1 (443Cys-502Cys in PfAMA1) but the electron density was too disordered to propose an unambiguous interpretation. No other region of significant electron density occurred in the maps.","type":"Results"},{"text":"The region defined here is based on the missing residues in the PDB structure 2j4w. Based on the same structure, there is likely disordered regions in the N-terminal part as well, however, a close homologue from P. falciparum indicates that the N-terminal region contains a folded domain (see PDB structure 4r1a).","type":"Curator statement"}],"curator_id":"bmesza","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"17229439","version":2,"reference_html":"Cross-reactivity studies of an anti-Plasmodium vivax apical membrane antigen 1 monoclonal antibody: binding and structural characterisation. <i> Igonet S, Vulliez-Le Normand B, Faure G, Riottot MM, Kocken CH, Thomas AW, Bentley GA. </i> J Mol Biol, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2J4W"}],"term_name":"disorder","curator_orcid":"0000-0003-0919-4449","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q9TY14","date":"2016-08-08T18:12:14.000Z","acc":"Q9TY14","name":"Apical membrane antigen 1","length":445,"organism":"Plasmodium vivax","dataset":[],"UniParc":"UPI000008046F","genes":[{"name":{"value":"AMA-1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAA76546.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA76546.1"}}]}}],"alphafold_very_low_content":0.051685393258426963,"disorder_content":0.07415730337078652,"disprot_consensus":{"full":[{"start":413,"end":445,"type":"D"}],"Structural state":[{"start":413,"end":445,"type":"D"}]}},{"acc":"Q38151","sequence":"MIEKDVVQILKAVSEFYPGRFQPDDLKGTVKAWHRVLAEYELEEIMNNLTDYAKVNKFPPTVSDLLKAQSEQRDRFIPSYEETQRILKEQAEAEEAARNDPDLQAAQEENMRKIREMLGINRGGAR","creator":"mmacossay","dataset":["Viral proteins"],"date":"2016-08-09T14:01:53.000Z","disprot_id":"DP00750","features":{"pfam":[{"id":"PF11417","name":"G39P, N-terminal domain","start":1,"end":65},{"id":"PF27049","name":"G39P, C-terminal domain","start":69,"end":123}],"gene3D":[{"start":1,"end":67,"id":"1.10.8.200","name":"Replisome organizer (g39p helicase loader/inhibitor protein)","_id":"685af523b4ac24d5329d84e5"}]},"genes":[{"name":{"value":"39","evidences":[{"source":{"id":"CAA48062.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/CAA48062.1","_id":"685af523b4ac24d5329d8517"},"code":"ECO:0000313","_id":"685af523b4ac24d5329d8516"}],"_id":"685af523b4ac24d5329d8518"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d8515"}],"length":126,"name":"39 protein","ncbi_taxon_id":10724,"organism":"Bacillus phage SPP1","regions_counter":11,"released":"2016_10","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Uroviricota","Caudoviricetes","Caudovirales","Siphoviridae"],"UniParc":"UPI000009B8A8","uniref100":"UniRef100_Q38151","uniref50":"UniRef50_A0A5P8PJW4","uniref90":"UniRef90_A0A5P8PJW4","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1NO1","_id":"685af523b4ac24d5329d84ed"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":68,"end":126,"interaction_partner":[],"reference_html":"Structural analysis of Bacillus subtilis SPP1 phage helicase loader protein G39P. <i> Bailey S, Sedelnikova SE, Mesa P, Ayora S, Waltho JP, Ashcroft AE, Baron AJ, Alonso JC, Rafferty JB. </i> J Biol Chem, 2003","reference_id":"12588876","region_id":"DP00750r002","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Our structural analyses reveal that G39P has a completely unexpected bipartite structure comprising a folded N-terminal domain and an essentially unfolded C-terminal domain.","_id":"685af523b4ac24d5329d84ee"},{"type":"Results","text":"Our findings strongly support the idea that the disorder observed in the crystal structure for the C-terminal region was not a result of the truncation of the protein nor was it merely some form of crystal artifact but reflected an underlying flexibility that may be closely related to the function of the protein.","_id":"685af523b4ac24d5329d84ef"},{"type":"Discussion","text":"Our structural analysis has shown that the G39P protein has two domains: a stably folded 67-residue N-terminal domain and a highly flexible and largely unfolded 59-residue C-terminal domain.","_id":"685af523b4ac24d5329d84f0"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T13:39:11.109Z","_id":"685af523b4ac24d5329d84f1"},"version":3,"_id":"685af523b4ac24d5329d84ec","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1NO1","_id":"685af523b4ac24d5329d84f3"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006222","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","ec_ontology":"ECO","start":68,"end":126,"interaction_partner":[],"reference_html":"Structural analysis of Bacillus subtilis SPP1 phage helicase loader protein G39P. <i> Bailey S, Sedelnikova SE, Mesa P, Ayora S, Waltho JP, Ashcroft AE, Baron AJ, Alonso JC, Rafferty JB. </i> J Biol Chem, 2003","reference_id":"12588876","region_id":"DP00750r003","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"High relative average B-factor values (38.3 Å2 for chain A/ 38.5 Å2 for chain B/ 38.4 Å2 for chain C) supporting the presence of intrinsic disorder in the C-terminal region of the protein.","_id":"685af523b4ac24d5329d84f4"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T13:39:09.444Z","_id":"685af523b4ac24d5329d84f5"},"version":1,"_id":"685af523b4ac24d5329d84f2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":68,"end":126,"interaction_partner":[],"reference_html":"Structural analysis of Bacillus subtilis SPP1 phage helicase loader protein G39P. <i> Bailey S, Sedelnikova SE, Mesa P, Ayora S, Waltho JP, Ashcroft AE, Baron AJ, Alonso JC, Rafferty JB. </i> J Biol Chem, 2003","reference_id":"12588876","region_id":"DP00750r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"For the C-terminal ~50 residues, i.e. about half the size of G39P, NMR relaxation rates are slow and are thus dominated by internal mobility far in excess of the overall rotation of the protein. Resonances from these residues show little chemical shift dispersion away from their random coil values, indicative of conformational averag- ing, and high intensity cross-peaks in TOCSY spectra, as illustrated by the correlations between the aromatic ring protons of Phe-76 and Tyr-80 in Fig. 3B.","_id":"685af523b4ac24d5329d84f7"},{"type":"Results","text":"Backbone amide proton resonances from the mobile C-terminal domain, upon heating the sample, are severely attenuated in intensity by solvent exchange, following saturation of the water resonance (Fig. 3A). This demonstrates that there is weak or no hydrogen bonding involving this part of the protein backbone other than to solvent molecules.","_id":"685af523b4ac24d5329d84f8"},{"type":"Results","text":"The NMR experiments indicate that in solution the protein behaves as a two-domain entity. One domain, corresponding to approximately the 67 N-terminal residues observed in the electron density map from the x-ray experiment, exists in the fold determined above, although at room temperature it is involved in a thermally labile, self-association process. The second domain, corresponding to the remaining 60 C-terminal residues that are not observed in the electron density map, has rapid internal motion and no well defined and stable fold involving immobilized side chains.","_id":"685af523b4ac24d5329d84f9"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T13:39:08.060Z","_id":"685af523b4ac24d5329d84fa"},"version":1,"_id":"685af523b4ac24d5329d84f6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0001184","ec_name":"gel-filtration evidence used in manual assertion","ec_ontology":"ECO","start":68,"end":126,"interaction_partner":[],"reference_html":"Structural analysis of Bacillus subtilis SPP1 phage helicase loader protein G39P. <i> Bailey S, Sedelnikova SE, Mesa P, Ayora S, Waltho JP, Ashcroft AE, Baron AJ, Alonso JC, Rafferty JB. </i> J Biol Chem, 2003","reference_id":"12588876","region_id":"DP00750r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The observation of a species approximating to the size of a dimer might actually arise from the rapid interchange between the monomeric and aggregated forms of the protein and is further complicated by an increase in the hydrodynamic radius arising from the flexible C-terminal domain.","_id":"685af523b4ac24d5329d84fc"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T13:39:06.645Z","_id":"685af523b4ac24d5329d84fd"},"version":1,"_id":"685af523b4ac24d5329d84fb","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":79,"end":126,"interaction_partner":[],"reference_html":"Structural analysis of Bacillus subtilis SPP1 phage helicase loader protein G39P. <i> Bailey S, Sedelnikova SE, Mesa P, Ayora S, Waltho JP, Ashcroft AE, Baron AJ, Alonso JC, Rafferty JB. </i> J Biol Chem, 2003","reference_id":"12588876","region_id":"DP00750r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"An investigation of the general susceptibility of G39P to proteolytic degradation was performed using proteinase K and both wtG39P and an N- terminal His-tagged variant. The analysis revealed a much more pronounced sensitivity to proteolytic cleavage in the C- terminal half of the protein that resulted in fragments corre- sponding to residues 1–79, 1– 87, 1–90, 1–94, and 1–106 (Fig. 6). The identity of the fragments was confirmed by the corre- spondence of the molecular weights determined by mass spec- trometry and by retention on a Ni-NTA column of equivalent fragments (as assessed by SDS-PAGE) from the N-terminal His-tagged variant.","_id":"685af523b4ac24d5329d84ff"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T13:39:05.408Z","_id":"685af523b4ac24d5329d8500"},"version":1,"_id":"685af523b4ac24d5329d84fe","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007184","ec_name":"protein mass spectrometry evidence used in manual assertion","ec_ontology":"ECO","start":79,"end":126,"interaction_partner":[],"reference_html":"Structural analysis of Bacillus subtilis SPP1 phage helicase loader protein G39P. <i> Bailey S, Sedelnikova SE, Mesa P, Ayora S, Waltho JP, Ashcroft AE, Baron AJ, Alonso JC, Rafferty JB. </i> J Biol Chem, 2003","reference_id":"12588876","region_id":"DP00750r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"An investigation of the general susceptibility of G39P to proteolytic degradation was performed using proteinase K and both wtG39P and an N- terminal His-tagged variant. The analysis revealed a much more pronounced sensitivity to proteolytic cleavage in the C- terminal half of the protein that resulted in fragments corre- sponding to residues 1–79, 1– 87, 1–90, 1–94, and 1–106 (Fig. 6). The identity of the fragments was confirmed by the corre- spondence of the molecular weights determined by mass spec- trometry and by retention on a Ni-NTA column of equivalent fragments (as assessed by SDS-PAGE) from the N-terminal His-tagged variant.","_id":"685af523b4ac24d5329d8502"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T13:39:04.560Z","_id":"685af523b4ac24d5329d8503"},"version":1,"_id":"685af523b4ac24d5329d8501","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IMP","ec_id":"ECO:0001175","ec_name":"deletion mutation phenotypic evidence used in manual assertion","ec_ontology":"ECO","start":69,"end":126,"interaction_partner":[],"reference_html":"Structural analysis of Bacillus subtilis SPP1 phage helicase loader protein G39P. <i> Bailey S, Sedelnikova SE, Mesa P, Ayora S, Waltho JP, Ashcroft AE, Baron AJ, Alonso JC, Rafferty JB. </i> J Biol Chem, 2003","reference_id":"12588876","region_id":"DP00750r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"A series of G39P truncated variants with N termini deleted up to residue 73 still show interaction with G40P-ATP as assessed by affinity chromatography assay, but a variant consisting of the N-terminal residues 1– 68 does not (Fig. 7).","_id":"685af523b4ac24d5329d8505"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T13:39:13.210Z","_id":"685af523b4ac24d5329d8506"},"version":1,"_id":"685af523b4ac24d5329d8504","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":69,"end":126,"interaction_partner":[],"reference_html":"Structural analysis of Bacillus subtilis SPP1 phage helicase loader protein G39P. <i> Bailey S, Sedelnikova SE, Mesa P, Ayora S, Waltho JP, Ashcroft AE, Baron AJ, Alonso JC, Rafferty JB. </i> J Biol Chem, 2003","reference_id":"12588876","region_id":"DP00750r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"A series of G39P truncated variants with N termini deleted up to residue 73 still show interaction with G40P-ATP as assessed by affinity chromatography assay, but a variant consisting of the N-terminal residues 1– 68 does not (Fig. 7).","_id":"685af523b4ac24d5329d8508"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T13:39:12.108Z","_id":"685af523b4ac24d5329d8509"},"version":1,"_id":"685af523b4ac24d5329d8507","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-08T15:43:12.531Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006075","ec_name":"affinity evidence used in manual assertion","ec_ontology":"ECO","start":113,"end":126,"interaction_partner":[{"db":"UniProt","id":"A0A1Y6FJJ7","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d850e"}],"reference_html":"Structural analysis of Bacillus subtilis SPP1 phage helicase loader protein G39P. <i> Bailey S, Sedelnikova SE, Mesa P, Ayora S, Waltho JP, Ashcroft AE, Baron AJ, Alonso JC, Rafferty JB. </i> J Biol Chem, 2003","reference_id":"12588876","region_id":"DP00750r010","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"The G39P protein is proteolytically sensitive, and our binding assays show that the C-terminal domain is essential for helicase interaction and that removal of just the 14 C-terminal residues abolishes interaction with the helicase in vitro. We propose a number of possible scenarios in which the flexibility of the C-terminal domain of G39P and its proteolytic sensitivity may have important roles for the function of G39P in vivo that are consistent with other data on SPP1 phage DNA replication.","_id":"685af523b4ac24d5329d850b"},{"type":"Results","text":"We have observed that removal of just the C-terminal 14 residues impairs G40P binding.","_id":"685af523b4ac24d5329d850c"},{"type":"Results","text":"The full-length wt G39P protein is able to interact with G40P-ATPγS and to inhibit all three associated activities (ssDNA binding, ATPase, and helicase activity (6)). Assays have been performed on fragments of G39P and have shown that the G39P112 variant can neither exert a negative effect on G40P activities nor compete out the wt protein from the G39P-G40P-ATP complex (data not shown). ","_id":"685af523b4ac24d5329d850d"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_id":"GO:0140678","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-21T16:23:46.978Z","_id":"685af523b4ac24d5329d850f"},"version":2,"_id":"685af523b4ac24d5329d850a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006075","ec_name":"affinity evidence used in manual assertion","ec_ontology":"ECO","start":113,"end":126,"interaction_partner":[],"reference_html":"Structural analysis of Bacillus subtilis SPP1 phage helicase loader protein G39P. <i> Bailey S, Sedelnikova SE, Mesa P, Ayora S, Waltho JP, Ashcroft AE, Baron AJ, Alonso JC, Rafferty JB. </i> J Biol Chem, 2003","reference_id":"12588876","region_id":"DP00750r011","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"The G39P protein is proteolytically sensitive, and our binding assays show that the C-terminal domain is essential for helicase interaction and that removal of just the 14 C-terminal residues abolishes interaction with the helicase in vitro. We propose a number of possible scenarios in which the flexibility of the C-terminal domain of G39P and its proteolytic sensitivity may have important roles for the function of G39P in vivo that are consistent with other data on SPP1 phage DNA replication.","_id":"685af523b4ac24d5329d8511"},{"type":"Results","text":"We have observed that removal of just the C-terminal 14 residues impairs G40P binding.","_id":"685af523b4ac24d5329d8512"},{"type":"Results","text":"The full-length wt G39P protein is able to interact with G40P-ATPγS and to inhibit all three associated activities (ssDNA binding, ATPase, and helicase activity (6)). Assays have been performed on fragments of G39P and have shown that the G39P112 variant can neither exert a negative effect on G40P activities nor compete out the wt protein from the G39P-G40P-ATP complex (data not shown). ","_id":"685af523b4ac24d5329d8513"}],"states_connection":[],"term_comment":"","term_def":"\"The disaggregation of a protein-containing macromolecular complex into its constituent components.\" [GOC:mah]","term_id":"GO:0032984","term_is_binding":false,"term_is_obsolete":false,"term_name":"protein-containing complex disassembly","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T13:39:14.573Z","_id":"685af523b4ac24d5329d8514"},"version":1,"_id":"685af523b4ac24d5329d8510","reference_source":"pmid"}],"__v":0,"disorder_content":0.46825396825396826,"disprot_consensus":{"full":[{"start":68,"end":126,"type":"D"}],"Structural state":[{"start":68,"end":126,"type":"D"}],"Molecular function":[{"start":69,"end":126,"type":"F"}],"Biological process":[{"start":113,"end":126,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01599","name":"Ribosomal protein S27a","start":98,"end":141}],"gene3D":[{"start":1,"end":74,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"}]},"uniref50":"UniRef50_I7MMJ4","sequence":"MQVQVKTLEGETKIYTLEQGTSVLDLKSQISQDMGFEIDMMTLVNNGFIAPNTELVTDDVTYYLSLKLLGGKKKKKKKSYTTKKKTKHRHVHTKLGALAFYKLENNGKVSLQQKGCPKCGPGIFMAKHYDRHYCGKCHLTLKIDAETAKKNLEELKKKQDAKKSGAAATDAGAGGAGKKDAKKGKKGKK","taxonomy":["Eukaryota","Sar","Alveolata","Ciliophora","Intramacronucleata","Oligohymenophorea","Hymenostomatida","Tetrahymenina","Tetrahymenidae","Tetrahymena"],"uniref90":"UniRef90_I7MMJ4","disprot_id":"DP00752","ncbi_taxon_id":5911,"regions_counter":3,"creator":"ahatos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":71,"region_id":"DP00752r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1. <i> Rabl J, Leibundgut M, Ataide SF, Haag A, Ban N. </i> Science, 2011","term_id":"IDPO:0000002","curator_id":"ahatos","start":1,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2XZM"}],"reference_id":"21205638","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":71,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1. <i> Rabl J, Leibundgut M, Ataide SF, Haag A, Ban N. </i> Science, 2011","term_id":"GO:0060090","curator_id":"ahatos","start":1,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"21205638","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00752r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":71,"term_name":"DNA binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1. <i> Rabl J, Leibundgut M, Ataide SF, Haag A, Ban N. </i> Science, 2011","term_id":"GO:0003677","curator_id":"ahatos","start":1,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"21205638","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00752r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_I7MMJ4","date":"2016-08-10T10:45:00.000Z","acc":"E6PBU9","name":"40S ribosomal protein rpS31e","length":189,"organism":"Tetrahymena thermophila","dataset":[],"UniParc":"UPI00006CAF49","genes":[],"alphafold_very_low_content":0.12698412698412698,"disorder_content":0.37566137566137564,"disprot_consensus":{"full":[{"start":1,"end":71,"type":"D"}],"Structural state":[{"start":1,"end":71,"type":"D"}],"Molecular function":[{"start":1,"end":71,"type":"F"}]}},{"features":{"pfam":[{"id":"PF13499","name":"EF-hand domain pair","start":17,"end":76},{"id":"PF13499","name":"EF-hand domain pair","start":87,"end":148}],"gene3D":[{"start":1,"end":82,"id":"1.10.238.10","name":"EF-hand"},{"start":83,"end":147,"id":"1.10.238.10","name":"EF-hand"}]},"uniref50":"UniRef50_B0E8K2","sequence":"MSEQKKVLTAEEQQEYKEAFQLFDKDNDNKLTAEELGTVMRALGANPTKQKISEIVKDYDKDNSGKFDQETFLTIMLEYGQEVDSTEDIKKAFEIFDKEKNGYISASELKHVLTTLGEKLTEQEVDDLLKEIGVEEGLINVDDFVKLITSK","taxonomy":["Eukaryota","Amoebozoa","Evosea","Archamoebae","Mastigamoebida","Entamoebidae","Entamoeba"],"uniref90":"UniRef90_B0E8K2","disprot_id":"DP00753","ncbi_taxon_id":5759,"regions_counter":4,"creator":"tlazar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":81,"region_id":"DP00753r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Calmodulin-like protein from Entamoeba histolytica: solution structure and calcium-binding properties of a partially folded protein. <i> Rout AK, Padhan N, Barnwal RP, Bhattacharya A, Chary KV. </i> Biochemistry, 2011","term_id":"IDPO:0000002","curator_id":"tlazar","start":1,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2LC5"}],"reference_id":"21114322","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":81,"term_name":"molten globule to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Calmodulin-like protein from Entamoeba histolytica: solution structure and calcium-binding properties of a partially folded protein. <i> Rout AK, Padhan N, Barnwal RP, Bhattacharya A, Chary KV. </i> Biochemistry, 2011","term_id":"IDPO:0000012","curator_id":"tlazar","start":1,"term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"21114322","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00753r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":81,"term_name":"metal ion binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Calmodulin-like protein from Entamoeba histolytica: solution structure and calcium-binding properties of a partially folded protein. <i> Rout AK, Padhan N, Barnwal RP, Bhattacharya A, Chary KV. </i> Biochemistry, 2011","term_id":"GO:0046872","curator_id":"tlazar","start":1,"term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"21114322","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00753r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":150,"region_id":"DP00753r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Calmodulin-like protein from Entamoeba histolytica: solution structure and calcium-binding properties of a partially folded protein. <i> Rout AK, Padhan N, Barnwal RP, Bhattacharya A, Chary KV. </i> Biochemistry, 2011","term_id":"IDPO:0000002","curator_id":"tlazar","start":82,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2LC5"}],"reference_id":"21114322","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_A0A5K1TYN2","date":"2016-08-10T11:03:40.000Z","acc":"C4M0U8","name":"Calmodulin putative","length":151,"organism":"Entamoeba histolytica","dataset":[],"UniParc":"UPI000049A001","genes":[{"orfNames":[{"value":"EHI_100270","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EAL46322.1","url":"https://www.ebi.ac.uk/ena/browser/view/EAL46322.1"}}]}]}],"alphafold_very_low_content":0.059602649006622516,"disorder_content":0.9933774834437086,"disprot_consensus":{"full":[{"start":1,"end":81,"type":"T"},{"start":82,"end":150,"type":"D"}],"Structural state":[{"start":1,"end":150,"type":"D"}],"Structural transition":[{"start":1,"end":81,"type":"T"}],"Molecular function":[{"start":1,"end":81,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02038","name":"ATP1G1/PLM/MAT8 family","start":27,"end":73}],"gene3D":[{"start":24,"end":87,"id":"1.20.5.780","name":"Single helix bin"}]},"uniref50":"UniRef50_Q70Q12","sequence":"MLGAATGLMVLVAVTQGVWAMDPEGPDNDERFTYDYYRLRVVGLIVAAVLCVIGIIILLAGKCRCKFNQNKRTRSNSGTATAQHLLQPGEATEC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Chondrichthyes","Elasmobranchii","Squalomorphii","Squaliformes","Squalidae","Squalus"],"uniref90":"UniRef90_Q70Q12","disprot_id":"DP00754","ncbi_taxon_id":7797,"regions_counter":2,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":94,"region_id":"DP00754r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the sodium-potassium pump at 2.4 A resolution. <i> Shinoda T, Ogawa H, Cornelius F, Toyoshima C. </i> Nature, 2009","term_id":"IDPO:0000002","curator_id":"rdavidovic","start":62,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2ZXE"}],"reference_id":"19458722","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":94,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of the sodium-potassium pump at 2.4 A resolution. <i> Shinoda T, Ogawa H, Cornelius F, Toyoshima C. </i> Nature, 2009","term_id":"GO:0005515","curator_id":"rdavidovic","start":62,"term_ontology":"GO","curator_name":"Radoslav Davidović","reference_id":"19458722","version":3,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00754r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q70Q12","date":"2016-08-10T12:20:38.000Z","acc":"Q70Q12","name":"FXYD domain-containing ion transport regulator","length":94,"organism":"Squalus acanthias","dataset":[],"UniParc":"UPI00001D46D2","genes":[{"name":{"value":"fxyd10","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAD88978.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAD88978.1"}}]}}],"alphafold_very_low_content":0.24468085106382978,"disorder_content":0.35106382978723405,"disprot_consensus":{"full":[{"start":62,"end":94,"type":"D"}],"Structural state":[{"start":62,"end":94,"type":"D"}],"Molecular function":[{"start":62,"end":94,"type":"F"}]}},{"acc":"Q04884","sequence":"ASEDGGRGPYVQADLAYAYEHITHDYPEPTAPNKNKISTVSDYFRNIRTRSVHPRVSVGYDFGGWRIAADYARYRKWNNNKYSVNIENVRIRKENGIRIDRKTENQENGTFHAVSSLGLSAIYDFQINDKFKPYIGARVAYGHVRHSIDSTKKTIEVTTVPSNAPNGAVTTYNTDPKTQNDYQSNSIRRVGLGVIAGVGFDITPKLTLDAGYRYHNWGRLENTRFKTHEASLGVRYRF","alphafold_very_low_content":"0.5084033613445378","creator":"tlazar","dataset":[],"date":"2016-08-10T17:14:35.000Z","disprot_id":"DP00756","features":{"pfam":[{"id":"PF02462","name":"Opacity family porin protein","start":58,"end":238}],"gene3D":[{"start":5,"end":238,"id":"2.40.160.20","name":"2.40.160.20","_id":"685af523b4ac24d5329d851a"}]},"genes":[{"name":{"value":"opaH","evidences":[],"_id":"685af523b4ac24d5329d8579"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d8578"}],"length":238,"name":"Opacity protein opA60","ncbi_taxon_id":485,"organism":"Neisseria gonorrhoeae","regions_counter":17,"released":"2016_10","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"UniParc":"UPI0000130D5E","uniref100":"UniRef100_Q04884","uniref50":"UniRef50_P09888","uniref90":"UniRef90_Q04884","regions":[{"annotation_extensions":[],"conditions":[{"deviation":null,"statements":[{"type":"Results","text":"A series of 15N, 1H-HSQC spectra were recorded at 10, 20, 30, and 40°C and the peaks were tracked through each spectrum in order to correlate the low temperature assignments to the assignment of the full length Opa60 at 40°C.","_id":"685af523b4ac24d5329d853e"}],"term_id":"NCIT:C25206","unit_id":"UO:0000027","unit_name":"°C","value":20,"_id":"685af523b4ac24d5329d853d"},{"deviation":null,"statements":[{"type":"Results","text":"A series of 15N, 1H-HSQC spectra were recorded at 10, 20, 30, and 40°C and the peaks were tracked through each spectrum in order to correlate the low temperature assignments to the assignment of the full length Opa60 at 40°C.","_id":"685af523b4ac24d5329d8540"}],"term_id":"NCIT:C25206","unit_id":"UO:0000027","unit_name":"°C","value":40,"_id":"685af523b4ac24d5329d853f"}],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":16,"end":55,"interaction_partner":[],"reference_html":"Solution NMR resonance assignment strategies for β-barrel membrane proteins. <i> Fox DA, Columbus L. </i> Protein Sci, 2013","reference_id":"23754333","region_id":"DP00756r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The loops are unstructured based on circular dichroism (data not shown), amide proton chemical shift, and the 15N-edited NOESY spectrum (data not shown).","_id":"685af523b4ac24d5329d8541"},{"type":"Results","text":"Using a series of 3D NMR experiments, the amide proton, nitrogen, and α-carbon were assigned for 27 of the 34 observed resonances (corresponding to residues 1–6 in the N-terminus; 109–110 in loop 2; 152–154, 160, 162–164, 166–175, and 177–178 in loop 3).","_id":"685af523b4ac24d5329d8542"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-10-13T20:26:10.756Z","_id":"685af523b4ac24d5329d8543"},"version":1,"_id":"685af523b4ac24d5329d853c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[{"deviation":null,"statements":[{"type":"Results","text":"A series of 15N, 1H-HSQC spectra were recorded at 10, 20, 30, and 40°C and the peaks were tracked through each spectrum in order to correlate the low temperature assignments to the assignment of the full length Opa60 at 40°C.","_id":"685af523b4ac24d5329d8546"}],"term_id":"NCIT:C25206","unit_id":"UO:0000027","unit_name":"°C","value":20,"_id":"685af523b4ac24d5329d8545"},{"deviation":null,"statements":[{"type":"Results","text":"A series of 15N, 1H-HSQC spectra were recorded at 10, 20, 30, and 40°C and the peaks were tracked through each spectrum in order to correlate the low temperature assignments to the assignment of the full length Opa60 at 40°C.","_id":"685af523b4ac24d5329d8548"}],"term_id":"NCIT:C25206","unit_id":"UO:0000027","unit_name":"°C","value":40,"_id":"685af523b4ac24d5329d8547"}],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":72,"end":116,"interaction_partner":[],"reference_html":"Solution NMR resonance assignment strategies for β-barrel membrane proteins. <i> Fox DA, Columbus L. </i> Protein Sci, 2013","reference_id":"23754333","region_id":"DP00756r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The loops are unstructured based on circular dichroism (data not shown), amide proton chemical shift, and the 15N-edited NOESY spectrum (data not shown).","_id":"685af523b4ac24d5329d8549"},{"type":"Results","text":"Using a series of 3D NMR experiments, the amide proton, nitrogen, and α-carbon were assigned for 27 of the 34 observed resonances (corresponding to residues 1–6 in the N-terminus; 109–110 in loop 2; 152–154, 160, 162–164, 166–175, and 177–178 in loop 3).","_id":"685af523b4ac24d5329d854a"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-10-13T20:26:09.137Z","_id":"685af523b4ac24d5329d854b"},"version":1,"_id":"685af523b4ac24d5329d8544","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[{"deviation":null,"statements":[{"type":"Results","text":"A series of 15N, 1H-HSQC spectra were recorded at 10, 20, 30, and 40°C and the peaks were tracked through each spectrum in order to correlate the low temperature assignments to the assignment of the full length Opa60 at 40°C.","_id":"685af523b4ac24d5329d854e"}],"term_id":"NCIT:C25206","unit_id":"UO:0000027","unit_name":"°C","value":20,"_id":"685af523b4ac24d5329d854d"},{"deviation":null,"statements":[{"type":"Results","text":"A series of 15N, 1H-HSQC spectra were recorded at 10, 20, 30, and 40°C and the peaks were tracked through each spectrum in order to correlate the low temperature assignments to the assignment of the full length Opa60 at 40°C.","_id":"685af523b4ac24d5329d8550"}],"term_id":"NCIT:C25206","unit_id":"UO:0000027","unit_name":"°C","value":40,"_id":"685af523b4ac24d5329d854f"}],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":142,"end":190,"interaction_partner":[],"reference_html":"Solution NMR resonance assignment strategies for β-barrel membrane proteins. <i> Fox DA, Columbus L. </i> Protein Sci, 2013","reference_id":"23754333","region_id":"DP00756r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The loops are unstructured based on circular dichroism (data not shown), amide proton chemical shift, and the 15N-edited NOESY spectrum (data not shown).","_id":"685af523b4ac24d5329d8551"},{"type":"Results","text":"Using a series of 3D NMR experiments, the amide proton, nitrogen, and α-carbon were assigned for 27 of the 34 observed resonances (corresponding to residues 1–6 in the N-terminus; 109–110 in loop 2; 152–154, 160, 162–164, 166–175, and 177–178 in loop 3).","_id":"685af523b4ac24d5329d8552"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-10-13T20:26:08.206Z","_id":"685af523b4ac24d5329d8553"},"version":1,"_id":"685af523b4ac24d5329d854c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[{"deviation":null,"statements":[{"type":"Results","text":"A series of 15N, 1H-HSQC spectra were recorded at 10, 20, 30, and 40°C and the peaks were tracked through each spectrum in order to correlate the low temperature assignments to the assignment of the full length Opa60 at 40°C.","_id":"685af523b4ac24d5329d8556"}],"term_id":"NCIT:C25206","unit_id":"UO:0000027","unit_name":"°C","value":20,"_id":"685af523b4ac24d5329d8555"},{"deviation":null,"statements":[{"type":"Results","text":"A series of 15N, 1H-HSQC spectra were recorded at 10, 20, 30, and 40°C and the peaks were tracked through each spectrum in order to correlate the low temperature assignments to the assignment of the full length Opa60 at 40°C.","_id":"685af523b4ac24d5329d8558"}],"term_id":"NCIT:C25206","unit_id":"UO:0000027","unit_name":"°C","value":40,"_id":"685af523b4ac24d5329d8557"}],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":216,"end":231,"interaction_partner":[],"reference_html":"Solution NMR resonance assignment strategies for β-barrel membrane proteins. <i> Fox DA, Columbus L. </i> Protein Sci, 2013","reference_id":"23754333","region_id":"DP00756r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The loops are unstructured based on circular dichroism (data not shown), amide proton chemical shift, and the 15N-edited NOESY spectrum (data not shown).","_id":"685af523b4ac24d5329d8559"},{"type":"Results","text":"Using a series of 3D NMR experiments, the amide proton, nitrogen, and α-carbon were assigned for 27 of the 34 observed resonances (corresponding to residues 1–6 in the N-terminus; 109–110 in loop 2; 152–154, 160, 162–164, 166–175, and 177–178 in loop 3).","_id":"685af523b4ac24d5329d855a"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-10-13T20:26:06.391Z","_id":"685af523b4ac24d5329d855b"},"version":1,"_id":"685af523b4ac24d5329d8554","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2MAF","_id":"685af523b4ac24d5329d855d"},{"db":"PDB","id":"2MLH","_id":"685af523b4ac24d5329d855e"},{"db":"BMRB","id":"19343","_id":"685af523b4ac24d5329d855f"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":16,"end":55,"interaction_partner":[],"reference_html":"Structure of the Neisserial outer membrane protein Opa₆₀: loop flexibility essential to receptor recognition and bacterial engulfment. <i> Fox DA, Larsson P, Lo RH, Kroncke BM, Kasson PM, Columbus L. </i> J Am Chem Soc, 2014","reference_id":"24813921","region_id":"DP00756r014","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The extracellular loops are intrinsically disordered yet are sampling a restricted volume such that there are interactions between the loops on the nanosecond time scale.","_id":"685af523b4ac24d5329d8560"},{"type":"Results","text":"The β-barrel provides the scaffolding for the functional extracellular loops, which are disordered and sample a diverse ensemble of conformers.","_id":"685af523b4ac24d5329d8561"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-10-13T20:26:05.734Z","_id":"685af523b4ac24d5329d8562"},"version":1,"_id":"685af523b4ac24d5329d855c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2MAF","_id":"685af523b4ac24d5329d8564"},{"db":"PDB","id":"2MLH","_id":"685af523b4ac24d5329d8565"},{"db":"BMRB","id":"19343","_id":"685af523b4ac24d5329d8566"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":72,"end":116,"interaction_partner":[],"reference_html":"Structure of the Neisserial outer membrane protein Opa₆₀: loop flexibility essential to receptor recognition and bacterial engulfment. <i> Fox DA, Larsson P, Lo RH, Kroncke BM, Kasson PM, Columbus L. </i> J Am Chem Soc, 2014","reference_id":"24813921","region_id":"DP00756r015","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The extracellular loops are intrinsically disordered yet are sampling a restricted volume such that there are interactions between the loops on the nanosecond time scale.","_id":"685af523b4ac24d5329d8567"},{"type":"Results","text":"The β-barrel provides the scaffolding for the functional extracellular loops, which are disordered and sample a diverse ensemble of conformers.","_id":"685af523b4ac24d5329d8568"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-10-13T20:26:13.696Z","_id":"685af523b4ac24d5329d8569"},"version":1,"_id":"685af523b4ac24d5329d8563","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2MAF","_id":"685af523b4ac24d5329d856b"},{"db":"PDB","id":"2MLH","_id":"685af523b4ac24d5329d856c"},{"db":"BMRB","id":"19343","_id":"685af523b4ac24d5329d856d"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":142,"end":190,"interaction_partner":[],"reference_html":"Structure of the Neisserial outer membrane protein Opa₆₀: loop flexibility essential to receptor recognition and bacterial engulfment. <i> Fox DA, Larsson P, Lo RH, Kroncke BM, Kasson PM, Columbus L. </i> J Am Chem Soc, 2014","reference_id":"24813921","region_id":"DP00756r016","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The extracellular loops are intrinsically disordered yet are sampling a restricted volume such that there are interactions between the loops on the nanosecond time scale.","_id":"685af523b4ac24d5329d856e"},{"type":"Results","text":"The β-barrel provides the scaffolding for the functional extracellular loops, which are disordered and sample a diverse ensemble of conformers.","_id":"685af523b4ac24d5329d856f"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-10-13T20:26:18.197Z","_id":"685af523b4ac24d5329d8570"},"version":1,"_id":"685af523b4ac24d5329d856a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2MAF","_id":"685af523b4ac24d5329d8572"},{"db":"PDB","id":"2MLH","_id":"685af523b4ac24d5329d8573"},{"db":"BMRB","id":"19343","_id":"685af523b4ac24d5329d8574"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":216,"end":231,"interaction_partner":[],"reference_html":"Structure of the Neisserial outer membrane protein Opa₆₀: loop flexibility essential to receptor recognition and bacterial engulfment. <i> Fox DA, Larsson P, Lo RH, Kroncke BM, Kasson PM, Columbus L. </i> J Am Chem Soc, 2014","reference_id":"24813921","region_id":"DP00756r017","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The extracellular loops are intrinsically disordered yet are sampling a restricted volume such that there are interactions between the loops on the nanosecond time scale.","_id":"685af523b4ac24d5329d8575"},{"type":"Results","text":"The β-barrel provides the scaffolding for the functional extracellular loops, which are disordered and sample a diverse ensemble of conformers.","_id":"685af523b4ac24d5329d8576"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-10-13T20:26:19.853Z","_id":"685af523b4ac24d5329d8577"},"version":1,"_id":"685af523b4ac24d5329d8571","reference_source":"pmid"}],"__v":0,"disorder_content":0.6302521008403361,"disprot_consensus":{"full":[{"start":16,"end":55,"type":"D"},{"start":72,"end":116,"type":"D"},{"start":142,"end":190,"type":"D"},{"start":216,"end":231,"type":"D"}],"Structural state":[{"start":16,"end":55,"type":"D"},{"start":72,"end":116,"type":"D"},{"start":142,"end":190,"type":"D"},{"start":216,"end":231,"type":"D"}]}},{"features":{"pfam":[{"id":"PF06747","name":"CHCH domain","start":58,"end":91},{"id":"PF16860","name":"CHCH-CHCH-like Cx9C, IMS import disulfide relay-system,","start":5,"end":49}]},"uniref50":"UniRef50_Q9BSY4","sequence":"MQAALEVTARYCGRELEQYGQCVAAKPESWQRDCHYLKMSIAQCTSSHPIIRQIRQACAQPFEAFEECLRQNEAAVGNCAEHMRRFLQCAEQVQPPRSPATVEAQPLPAS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9BSY4","disprot_id":"DP00757","ncbi_taxon_id":9606,"regions_counter":1,"creator":"tlazar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":109,"region_id":"DP00757r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural characterization of CHCHD5 and CHCHD7: two atypical human twin CX9C proteins. <i> Banci L, Bertini I, Ciofi-Baffoni S, Jaiswal D, Neri S, Peruzzini R, Winkelmann J. </i> J Struct Biol, 2012","term_id":"IDPO:0000002","curator_id":"tlazar","start":94,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2LQL"}],"reference_id":"22842048","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q9BSY4","date":"2016-08-11T11:36:10.000Z","acc":"Q9BSY4","name":"Coiled-coil-helix-coiled-coil-helix domain-containing protein 5","length":110,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000034E2C","genes":[{"name":{"value":"CHCHD5"},"synonyms":[{"value":"C2orf9"}]}],"alphafold_very_low_content":0.19090909090909092,"disorder_content":0.14545454545454545,"disprot_consensus":{"full":[{"start":94,"end":109,"type":"D"}],"Structural state":[{"start":94,"end":109,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01166","name":"TSC-22/dip/bun family","start":1,"end":55}],"gene3D":[{"start":1,"end":45,"id":"1.20.5.490","name":"Single helix bin"}]},"uniref50":"UniRef50_P80220","sequence":"MDLVKNHLMYAVREEVEILKEQIRELVEKNSQLERENTLLKTLASPEQLEKFQSRLSPEEPAPETPEAPEAPGGSAV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Suina","Suidae","Sus"],"uniref90":"UniRef90_P80220","disprot_id":"DP00759","ncbi_taxon_id":9823,"regions_counter":1,"creator":"tlazar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":77,"region_id":"DP00759r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of porcine delta sleep-inducing peptide immunoreactive peptide A homolog of the shortsighted gene product. <i> Seidel G, Adermann K, Schindler T, Ejchart A, Jaenicke R, Forssmann WG, Rösch P. </i> J Biol Chem, 1997","term_id":"IDPO:0000002","curator_id":"tlazar","start":48,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1DIP"}],"reference_id":"9388238","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P80220","date":"2016-08-11T13:58:32.000Z","acc":"P80220","name":"TSC22 domain family protein 3","length":77,"organism":"Sus scrofa","dataset":[],"UniParc":"UPI000012B4B5","genes":[{"name":{"value":"TSC22D3"},"synonyms":[{"value":"DSIPI"},{"value":"GILZ"}]}],"alphafold_very_low_content":0.09090909090909091,"disorder_content":0.38961038961038963,"disprot_consensus":{"full":[{"start":48,"end":77,"type":"D"}],"Structural state":[{"start":48,"end":77,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03297","name":"S25 ribosomal protein","start":9,"end":106}],"gene3D":[{"start":23,"end":115,"id":"1.10.10.2780","name":"1.10.10.2780"}]},"uniref50":"UniRef50_I7M463","sequence":"MGKQPAAGQKKTKEAIAKAAQAKKGGKKKWTKGKAKDKVNHAVFIEKKNVESIINNPSKVGKVLTVSTVVEKLKVNGSLARQLMRTMADRKLVEKVAKNGNQWVYSVIGGVKEDKTAAPAAAGGKKQQQSKKGAAADKEEVQA","taxonomy":["Eukaryota","Sar","Alveolata","Ciliophora","Intramacronucleata","Oligohymenophorea","Hymenostomatida","Tetrahymenina","Tetrahymenidae","Tetrahymena"],"uniref90":"UniRef90_I7M463","disprot_id":"DP00761","ncbi_taxon_id":5911,"regions_counter":2,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":143,"region_id":"DP00761r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1. <i> Rabl J, Leibundgut M, Ataide SF, Haag A, Ban N. </i> Science, 2011","term_id":"IDPO:0000002","curator_id":"rdavidovic","start":116,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4V5O"}],"reference_id":"21205638","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":22,"region_id":"DP00761r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1. <i> Rabl J, Leibundgut M, Ataide SF, Haag A, Ban N. </i> Science, 2011","term_id":"IDPO:0000002","curator_id":"rdavidovic","start":1,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4V5O"}],"reference_id":"21205638","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_I7M463","date":"2016-08-11T16:38:58.000Z","acc":"E6PBU3","name":"40S ribosomal protein rpS25e","length":143,"organism":"Tetrahymena thermophila","dataset":[],"UniParc":"UPI00019A5B4D","genes":[],"alphafold_very_low_content":0.26573426573426573,"disorder_content":0.34965034965034963,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"},{"start":116,"end":143,"type":"D"}],"Structural state":[{"start":1,"end":22,"type":"D"},{"start":116,"end":143,"type":"D"}]}},{"acc":"O89467","sequence":"MLNLADRRIPGTAEENLQKSSGGVPGQNTGGQEARPNYHCQLCFLRSLGIDYLDASLRKKNKQRLKAIQQGRQPQYLL","creator":"tlazar","dataset":["Viral proteins"],"date":"2016-08-11T17:30:37.000Z","disprot_id":"DP00764","features":{"pfam":[{"id":"PF00539","name":"Transactivating regulatory protein (Tat)","start":36,"end":70}],"gene3D":[{"start":4,"end":78,"id":"4.10.210.10","name":"Transactivator Protein (TAT, TAT EIAVY)","_id":"685af523b4ac24d5329d857b"}]},"genes":[{"name":{"value":"tat","evidences":[{"source":{"id":"AAC24016.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/AAC24016.1","_id":"685af523b4ac24d5329d8588"},"code":"ECO:0000313","_id":"685af523b4ac24d5329d8587"}],"_id":"685af523b4ac24d5329d8589"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d8586"}],"length":78,"name":"Protein Tat","ncbi_taxon_id":11665,"organism":"Equine infectious anemia virus","regions_counter":5,"released":"2016_10","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"UniParc":"UPI00001058E4","uniref100":"UniRef100_O89467","uniref50":"UniRef50_P32544","uniref90":"UniRef90_P32544","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1TVT","_id":"685af523b4ac24d5329d857d"}],"curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":50,"end":78,"interaction_partner":[],"reference_html":"Structure of the equine infectious anemia virus Tat protein. <i> Willbold D, Rosin-Arbesfeld R, Sticht H, Frank R, Rösch P. </i> Science, 1994","reference_id":"7515512","region_id":"DP00764r001","released":"2022_03","sample":[],"statement":[],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":2,"_id":"685af523b4ac24d5329d857c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1TVT","_id":"685af523b4ac24d5329d857f"}],"curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":6,"end":25,"interaction_partner":[],"reference_html":"Structure of the equine infectious anemia virus Tat protein. <i> Willbold D, Rosin-Arbesfeld R, Sticht H, Frank R, Rösch P. </i> Science, 1994","reference_id":"7515512","region_id":"DP00764r002","released":"2022_03","sample":[],"statement":[],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":2,"_id":"685af523b4ac24d5329d857e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":45,"end":61,"interaction_partner":[],"reference_html":"Structural insights into the cyclin T1-Tat-TAR RNA transcription activation complex from EIAV. <i> Anand K, Schulte A, Vogel-Bachmayr K, Scheffzek K, Geyer M. </i> Nat Struct Mol Biol, 2008","reference_id":"19029897","region_id":"DP00764r004","released":"2022_03","sample":[],"statement":[],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","version":2,"_id":"685af523b4ac24d5329d8583","reference_source":"pmid"}],"__v":0,"disorder_content":0.6282051282051282,"disprot_consensus":{"full":[{"start":6,"end":25,"type":"D"},{"start":45,"end":61,"type":"T"},{"start":62,"end":78,"type":"D"}],"Structural state":[{"start":6,"end":25,"type":"D"},{"start":50,"end":78,"type":"D"}],"Structural transition":[{"start":45,"end":61,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00048","name":"Small cytokines (intecrine/chemokine), interleukin-8 like","start":29,"end":90}],"gene3D":[{"start":24,"end":102,"id":"2.40.50.40","name":"2.40.50.40"}]},"uniref50":"UniRef50_O00585","sequence":"MAQSLALSLLILVLAFGIPRTQGSDGGAQDCCLKYSQRKIPAKVVRSYRKQEPSLGCSIPAILFLPRKRSQAELCADPKELWVQQLMQHLDKTPSPQKPAQGCRKDRGASKTGKKGKGSKGCKRTERSQTPKGP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O00585","disprot_id":"DP00765","ncbi_taxon_id":9606,"regions_counter":2,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":134,"region_id":"DP00765r002","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Solution structure of CCL21 and identification of a putative CCR7 binding site. <i> Love M, Sandberg JL, Ziarek JJ, Gerarden KP, Rode RR, Jensen DR, McCaslin DR, Peterson FC, Veldkamp CT. </i> Biochemistry, 2012","term_id":"IDPO:0000002","curator_id":"vnugnes","start":94,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-09T16:30:31.316Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2L4N"}],"reference_id":"22221265","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1_Glu23del","start":null,"end":null,"position":null}],"sequence_construct":"SDGGAQDCCLKYSQRKIPAKVVRSYRKQEPSLGCSIPAILFLPRKRSQAELCADPKELWVQQLMQHLDKTPSPQKPAQGCRKDRGASKTGKKGKGSKGCKRTERSQTPKGPKL","statement":[{"text":"CCL21 also contains an unstructured C-terminus (residues 71–111, not shown for clarity) distinct from most chemokines.","type":"Figure"},{"text":"The core chemokine domain of CCL21 is structured (residues 8–68) while the N-terminus and extended C-terminus are unstructured.","type":"Figure"},{"text":"The authors assessed the mature protein, that lacks the first 23 residues. They describe the 94-134 region of the UniProt protein sequence. ","type":"Curator statement"}]}],"released":"2016_10","uniref100":"UniRef100_O00585","date":"2016-08-11T23:24:50.000Z","acc":"O00585","name":"C-C motif chemokine 21","length":134,"organism":"Homo sapiens","dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000049E0F","genes":[{"name":{"value":"CCL21"},"synonyms":[{"value":"SCYA21"}],"orfNames":[{"value":"UNQ784/PRO1600"}]}],"alphafold_very_low_content":0.11194029850746269,"disorder_content":0.30597014925373134,"disprot_consensus":{"full":[{"start":94,"end":134,"type":"D"}],"Structural state":[{"start":94,"end":134,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00254","name":"FKBP-type peptidyl-prolyl cis-trans isomerase","start":4,"end":78}],"gene3D":[{"start":71,"end":121,"id":"2.40.10.330","name":"2.40.10.330"},{"start":3,"end":154,"id":"3.10.50.40","name":"3.10.50.40"}]},"uniref50":"UniRef50_Q7CFU4","sequence":"MKVAKDLVVSLAYQVRTEDGVLVDESPVSAPLDYLHGHGSLISGLETALEGHEVGDKFDVAVGANDAYGQYDENLVQRVPKDVFMGVDELQVGMRFLAETDQGPVPVEITAVEDDHVVVDGNHMLAGQNLKFNVEVVAIREATEEELAHGHVHGAHDHHHDHDHDGCCGGHGHDHGHEHGGEGCCGGKGNGGCGCH","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0A9L1","disprot_id":"DP00766","ncbi_taxon_id":83333,"regions_counter":1,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":196,"region_id":"DP00766r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The interaction of the Escherichia coli protein SlyD with nickel ions illuminates the mechanism of regulation of its peptidyl-prolyl isomerase activity. <i> Martino L, He Y, Hands-Taylor KL, Valentine ER, Kelly G, Giancola C, Conte MR. </i> FEBS J, 2009","term_id":"IDPO:0000002","curator_id":"rdavidovic","start":153,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2KFW"}],"reference_id":"19645725","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P0A9L1","date":"2016-08-12T10:12:48.000Z","acc":"P0A9K9","name":"FKBP-type peptidyl-prolyl cis-trans isomerase SlyD","length":196,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI0000135A43","genes":[{"name":{"value":"slyD"},"olnNames":[{"value":"b3349"},{"value":"JW3311"}]}],"alphafold_very_low_content":0.20918367346938777,"disorder_content":0.22448979591836735,"disprot_consensus":{"full":[{"start":153,"end":196,"type":"D"}],"Structural state":[{"start":153,"end":196,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00505","name":"HMG (high mobility group) box","start":297,"end":365},{"id":"PF08347","name":"N-terminal CTNNB1 binding","start":7,"end":211}],"gene3D":[{"start":295,"end":380,"id":"1.10.30.10","name":"High mobility group box domain"},{"start":1,"end":63,"id":"4.10.900.10","name":"TCF3-CBD (Catenin binding domain)"}]},"uniref50":"UniRef50_P27782","sequence":"MPQLSGGGGGGDPELCATDEMIPFKDEGDPQKEKIFAEISHPEEEGDLADIKSSLVNESEIIPASNGHEVVRQAPSSQEPYHDKAREHPDEGKHPDGGLYNKGPSYSSYSGYIMMPNMNSDPYMSNGSLSPPIPRTSNKVPVVQPSHAVHPLTPLITYSDEHFSPGSHPSHIPSDVNSKQGMSRHPPAPEIPTFYPLSPGGVGQITPPIGWQGQPVYPITGGFRQPYPSSLSGDTSMSRFSHHMIPGPPGPHTTGIPHPAIVTPQVKQEHPHTDSDLMHVKPQHEQRKEQEPKRPHIKKPLNAFMLYMKEMRANVVAECTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKKRKREKLQESTSGTGPRMTAAYI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P27782","disprot_id":"DP00767","ncbi_taxon_id":10090,"regions_counter":8,"creator":"aghosh","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":370,"region_id":"DP00767r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The LEF-1 high-mobility group domain undergoes a disorder-to-order transition upon formation of a complex with cognate DNA. <i> Love JJ, Li X, Chung J, Dyson HJ, Wright PE. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"dpiovesan","start":361,"term_ontology":"IDPO","curator_name":"Damiano Piovesan","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-8210-2390","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2LEF"}],"reference_id":"15236581","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":370,"term_name":"DNA binding, bending","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The LEF-1 high-mobility group domain undergoes a disorder-to-order transition upon formation of a complex with cognate DNA. <i> Love JJ, Li X, Chung J, Dyson HJ, Wright PE. </i> Biochemistry, 2004","term_id":"GO:0008301","curator_id":"dpiovesan","start":361,"term_ontology":"GO","curator_name":"Damiano Piovesan","reference_id":"15236581","version":3,"curator_orcid":"0000-0001-8210-2390","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00767r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The activity of binding selectively and non-covalently to and distorting the original structure of DNA, typically a straight helix, into a bend, or increasing the bend if the original structure was intrinsically bent due to its sequence.\" [GOC:krc, GOC:vw, PMID:10710711, PMID:19037758]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":370,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The LEF-1 high-mobility group domain undergoes a disorder-to-order transition upon formation of a complex with cognate DNA. <i> Love JJ, Li X, Chung J, Dyson HJ, Wright PE. </i> Biochemistry, 2004","term_id":"IDPO:0000011","curator_id":"dpiovesan","start":361,"term_ontology":"IDPO","curator_name":"Damiano Piovesan","reference_id":"15236581","version":2,"curator_orcid":"0000-0001-8210-2390","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00767r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":370,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The LEF-1 high-mobility group domain undergoes a disorder-to-order transition upon formation of a complex with cognate DNA. <i> Love JJ, Li X, Chung J, Dyson HJ, Wright PE. </i> Biochemistry, 2004","term_id":"GO:0003676","curator_id":"dpiovesan","start":361,"term_ontology":"GO","curator_name":"Damiano Piovesan","reference_id":"15236581","version":3,"curator_orcid":"0000-0001-8210-2390","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00767r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":319,"region_id":"DP00767r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The LEF-1 high-mobility group domain undergoes a disorder-to-order transition upon formation of a complex with cognate DNA. <i> Love JJ, Li X, Chung J, Dyson HJ, Wright PE. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"dpiovesan","start":302,"term_ontology":"IDPO","curator_name":"Damiano Piovesan","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-8210-2390","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"15236581","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":319,"term_name":"DNA binding, bending","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The LEF-1 high-mobility group domain undergoes a disorder-to-order transition upon formation of a complex with cognate DNA. <i> Love JJ, Li X, Chung J, Dyson HJ, Wright PE. </i> Biochemistry, 2004","term_id":"GO:0008301","curator_id":"dpiovesan","start":302,"term_ontology":"GO","curator_name":"Damiano Piovesan","reference_id":"15236581","version":3,"curator_orcid":"0000-0001-8210-2390","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00767r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The activity of binding selectively and non-covalently to and distorting the original structure of DNA, typically a straight helix, into a bend, or increasing the bend if the original structure was intrinsically bent due to its sequence.\" [GOC:krc, GOC:vw, PMID:10710711, PMID:19037758]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":319,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The LEF-1 high-mobility group domain undergoes a disorder-to-order transition upon formation of a complex with cognate DNA. <i> Love JJ, Li X, Chung J, Dyson HJ, Wright PE. </i> Biochemistry, 2004","term_id":"IDPO:0000011","curator_id":"dpiovesan","start":302,"term_ontology":"IDPO","curator_name":"Damiano Piovesan","reference_id":"15236581","version":2,"curator_orcid":"0000-0001-8210-2390","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00767r007","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":319,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The LEF-1 high-mobility group domain undergoes a disorder-to-order transition upon formation of a complex with cognate DNA. <i> Love JJ, Li X, Chung J, Dyson HJ, Wright PE. </i> Biochemistry, 2004","term_id":"GO:0003676","curator_id":"dpiovesan","start":302,"term_ontology":"GO","curator_name":"Damiano Piovesan","reference_id":"15236581","version":3,"curator_orcid":"0000-0001-8210-2390","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00767r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P27782","date":"2016-08-12T14:19:01.000Z","acc":"P27782","name":"Lymphoid enhancer-binding factor 1","length":397,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000022D6D","genes":[{"name":{"value":"Lef1"},"synonyms":[{"value":"Lef-1"}]}],"alphafold_very_low_content":0.5440806045340051,"disorder_content":0.07052896725440806,"disprot_consensus":{"full":[{"start":302,"end":319,"type":"T"},{"start":361,"end":370,"type":"T"}],"Structural state":[{"start":302,"end":319,"type":"D"},{"start":361,"end":370,"type":"D"}],"Molecular function":[{"start":302,"end":319,"type":"F"},{"start":361,"end":370,"type":"F"}],"Structural transition":[{"start":302,"end":319,"type":"T"},{"start":361,"end":370,"type":"T"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MLGWVQRVLPQPPGTPQKTKQEEEGTEPEPELEPKPETAPEETELEEVSLPPEEPCVGKEVAAVTLGPQGTQETALTPPTSLQAQVSVAPEAHSSPRGWVLTWLRKGVEKVVPQPAHSSRPSQNIAAGLESPDQQAGAQILGQCGTGGSDEPSEPSRAEDPGPGPWLLRWFEQNLEKMLPQPPKISEGWRDEPTDAALGPEPPGPALEIKPMLQAQESPSLPAPGPPEPEEEPIPEPQPTIQASSLPPPQDSARLMAWILHRLEMALPQPVIRGKGGEQESDAPVTCDVQTISILPGEQEESHLILEEVDPHWEEDEHQEGSTSTSPRTSEAAPADEEKGEVVEQTPRELPRIQEEKEDEEEEKEDGEEEEEEGREKEEEEGEEKEEEEGREKEEEEGEKKEEEGREKEEEEGGEKEDEEGREKEEEEGRGKEEEEGGEKEEEEGRGKEEVEGREEEEDEEEEQDHSVLLDSYLVPQSEEDQSEESETQDQSEVGGAQTQGEVGGAQALSEESETQDQSEVGGAQDQSEVGGAQAQGEVGGAQEQDGVGGAQDQSTSHQELQEEALADSSGGSFQMSPFEALQECEALKR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"","disprot_id":"DP00768","ncbi_taxon_id":9913,"regions_counter":25,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":99,"region_id":"DP00768r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":14,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16280326","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":99,"term_name":"entropic chain","start":14,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16280326","version":3,"reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0006165","region_id":"DP00768r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":99,"term_name":"entropic chain","start":14,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16280326","version":3,"reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0006165","region_id":"DP00768r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":99,"term_name":"molecular adaptor activity","start":14,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16280326","version":3,"reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP00768r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":99,"term_name":"molecular sequestering activity","start":14,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16280326","version":3,"reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140313","ec_id":"ECO:0006165","region_id":"DP00768r005","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":99,"term_name":"disorder to order","start":14,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16280326","version":2,"reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00768r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":99,"term_name":"protein binding","start":14,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16280326","version":3,"reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00768r007","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":590,"region_id":"DP00768r008","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":272,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16280326","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":590,"term_name":"entropic chain","start":272,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16280326","version":3,"reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0006165","region_id":"DP00768r009","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":590,"term_name":"entropic chain","start":272,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16280326","version":3,"reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0006165","region_id":"DP00768r010","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":590,"term_name":"molecular adaptor activity","start":272,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16280326","version":3,"reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP00768r011","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":590,"term_name":"molecular sequestering activity","start":272,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16280326","version":3,"reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140313","ec_id":"ECO:0006165","region_id":"DP00768r012","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":590,"term_name":"protein binding","start":272,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16280326","version":3,"reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00768r013","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":255,"region_id":"DP00768r014","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":184,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16280326","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":255,"term_name":"entropic chain","start":184,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16280326","version":3,"reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0006165","region_id":"DP00768r015","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":255,"term_name":"entropic chain","start":184,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16280326","version":3,"reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0006165","region_id":"DP00768r016","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":255,"term_name":"molecular adaptor activity","start":184,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16280326","version":3,"reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP00768r017","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":255,"term_name":"molecular sequestering activity","start":184,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16280326","version":3,"reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140313","ec_id":"ECO:0006165","region_id":"DP00768r018","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":255,"term_name":"protein binding","start":184,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16280326","version":3,"reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00768r019","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":166,"region_id":"DP00768r020","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","term_id":"IDPO:0000002","curator_id":"fquaglia","start":117,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16280326","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":166,"term_name":"entropic chain","start":117,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16280326","version":3,"reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0006165","region_id":"DP00768r021","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":166,"term_name":"entropic chain","start":117,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16280326","version":3,"reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0006165","region_id":"DP00768r022","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":166,"term_name":"molecular adaptor activity","start":117,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16280326","version":3,"reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP00768r023","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":166,"term_name":"molecular sequestering activity","start":117,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16280326","version":3,"reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140313","ec_id":"ECO:0006165","region_id":"DP00768r024","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":166,"term_name":"protein binding","start":117,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16280326","version":3,"reference_html":"Glutamic acid-rich proteins of rod photoreceptors are natively unfolded. <i> Batra-Safferling R, Abarca-Heidemann K, Körschen HG, Tziatzios C, Stoldt M, Budyak I, Willbold D, Schwalbe H, Klein-Seetharaman J, Kaupp UB. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00768r025","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"","date":"2016-08-12T17:16:25.000Z","acc":"Q28181-4","name":"Isoform GARP1 of Cyclic nucleotide-gated cation channel beta-1","length":590,"organism":"Bos taurus","dataset":[],"UniParc":"UPI000016C311","genes":[{"name":{"value":"CNGB1"},"synonyms":[{"value":"CNCG4"}]}],"disorder_content":0.8932203389830509,"disprot_consensus":{"full":[{"start":14,"end":99,"type":"T"},{"start":117,"end":166,"type":"D"},{"start":184,"end":255,"type":"D"},{"start":272,"end":590,"type":"D"}],"Structural state":[{"start":14,"end":99,"type":"D"},{"start":117,"end":166,"type":"D"},{"start":184,"end":255,"type":"D"},{"start":272,"end":590,"type":"D"}],"Disorder function":[{"start":14,"end":99,"type":"F"},{"start":117,"end":166,"type":"F"},{"start":184,"end":255,"type":"F"},{"start":272,"end":590,"type":"F"}],"Molecular function":[{"start":14,"end":99,"type":"F"},{"start":117,"end":166,"type":"F"},{"start":184,"end":255,"type":"F"},{"start":272,"end":590,"type":"F"}],"Structural transition":[{"start":14,"end":99,"type":"T"}]}},{"features":{"pfam":[{"id":"PF03501","name":"Plectin/S10 domain","start":6,"end":95}],"gene3D":[{"start":1,"end":102,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}]},"uniref50":"UniRef50_G0R2M7","sequence":"MVHVLKATKIRIYKQLLQDGVFVLKKDFEGHHEETGVPNLHCYILVRSLKDRGFLEEIFNWGFTYYYLNKEGCEYLKTKLGISADNVIPKTFKASNVNFISKEEDEEERPRRQFNKGGRTGERDGRNKRGVGRGTRREGEEAAKEEGAAETAQGNQETPAQE","taxonomy":["Eukaryota","Sar","Alveolata","Ciliophora","Intramacronucleata","Oligohymenophorea","Hymenostomatida","Tetrahymenina","Tetrahymenidae","Tetrahymena"],"uniref90":"UniRef90_Q24F70","disprot_id":"DP00769","ncbi_taxon_id":312017,"regions_counter":1,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":162,"region_id":"DP00769r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1. <i> Rabl J, Leibundgut M, Ataide SF, Haag A, Ban N. </i> Science, 2011","term_id":"IDPO:0000002","curator_id":"rdavidovic","start":106,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21205638","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q24F70","date":"2016-08-12T23:19:31.000Z","acc":"Q24F70","name":"40S ribosomal protein S10, putative","length":162,"organism":"Tetrahymena thermophila (strain SB210)","dataset":[],"UniParc":"UPI00006CA96E","genes":[{"orfNames":[{"value":"TTHERM_01128560","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EAS06405.1","url":"https://www.ebi.ac.uk/ena/browser/view/EAS06405.1"}}]}]}],"alphafold_very_low_content":0.32098765432098764,"disorder_content":0.35185185185185186,"disprot_consensus":{"full":[{"start":106,"end":162,"type":"D"}],"Structural state":[{"start":106,"end":162,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01192","name":"RNA polymerase Rpb6","start":80,"end":131}],"gene3D":[{"start":1,"end":154,"id":"3.90.940.10","name":"3.90.940.10"}]},"uniref50":"UniRef50_P20435","sequence":"MSDYEEAFNDGNENFEDFDVEHFSDEETYEEKPQFKDGETTDANGKTIVTGGNGPEDFQQHEQIRRKTLKEKAIPKDQRATTPYMTKYERARILGTRALQISMNAPVFVDLEGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWSVEELIVDL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P20435","disprot_id":"DP00771","ncbi_taxon_id":559292,"regions_counter":1,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":71,"region_id":"DP00771r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis of transcription: RNA polymerase II at 2.8 angstrom resolution. <i> Cramer P, Bushnell DA, Kornberg RD. </i> Science, 2001","term_id":"IDPO:0000002","curator_id":"rdavidovic","start":1,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4A3G"}],"reference_id":"11313498","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P20435","date":"2016-08-13T15:21:14.000Z","acc":"P20435","name":"DNA-directed RNA polymerases I, II, and III subunit RPABC2","length":155,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000053198","genes":[{"name":{"value":"RPO26"},"synonyms":[{"value":"RPB6"}],"orfNames":[{"value":"P9677.8"}],"olnNames":[{"value":"YPR187W"}]}],"alphafold_very_low_content":0.10967741935483871,"disorder_content":0.45806451612903226,"disprot_consensus":{"full":[{"start":1,"end":71,"type":"D"}],"Structural state":[{"start":1,"end":71,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00512","name":"His Kinase A (phospho-acceptor) domain","start":237,"end":301},{"id":"PF02518","name":"Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase","start":349,"end":445},{"id":"PF08521","name":"Two-component sensor kinase N-terminal","start":23,"end":157},{"id":"PF26769","name":"Sensor protein PhoQ-like, HAMP domain","start":186,"end":231}],"gene3D":[{"start":304,"end":449,"id":"3.30.565.10","name":"Histidine kinase-like ATPase, C-terminal domain"},{"start":129,"end":185,"id":"1.20.5.1040","name":"Sensor protein qsec."},{"start":1,"end":59,"id":"1.20.5.1040","name":"Sensor protein qsec."},{"start":188,"end":303,"id":"1.10.287.130","name":"1.10.287.130"}]},"uniref50":"UniRef50_P40719","sequence":"MKFTQRLSLRVRLTLIFLILASVTWLLSSFVAWKQTTDNVDELFDTQLMLFAKRLSTLDLNEINAADRMAQTPNRLKHGHVDDDALTFAIFTHDGRMVLNDGDNGEDIPYSYQREGFADGQLVGEDDPWRFVWMTSPDGKYRIVVGQEWEYREDMALAIVAGQLIPWLVALPIMLIIMMVLLGRELAPLNKLALALRMRDPDSEKPLNATGVPSEVRPLVESLNQLFARTHAMMVRERRFTSDAAHELRSPLTALKVQTEVAQLSDDDPQARKKALLQLHSGIDRATRLVDQLLTLSRLDSLDNLQDVAEIPLEDLLQSSVMDIYHTAQQAKIDVRLTLNAHSIKRTGQPLLLSLLVRNLLDNAVRYSPQGSVVDVTLNADNFIVRDNGPGVTPEALARIGERFYRPPGQTATGSGLGLSIVQRIAKLHGMNVEFGNAEQGGFEAKVSW","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P40719","disprot_id":"DP00774","ncbi_taxon_id":83333,"regions_counter":4,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":158,"region_id":"DP00774r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Membrane domain structures of three classes of histidine kinase receptors by cell-free expression and rapid NMR analysis. <i> Maslennikov I, Klammt C, Hwang E, Kefala G, Okamura M, Esquivies L, Mörs K, Glaubitz C, Kwiatkowski W, Jeon YH, Choe S. </i> Proc Natl Acad Sci U S A, 2010","term_id":"IDPO:0000002","curator_id":"jpujols","start":35,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2KSE"}],"reference_id":"20498088","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":417,"region_id":"DP00774r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the cytoplasmic segment of histidine kinase receptor QseC, a key player in bacterial virulence. <i> Xie W, Dickson C, Kwiatkowski W, Choe S. </i> Protein Pept Lett, 2010","term_id":"IDPO:0000002","curator_id":"jpujols","start":386,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3JZ3"}],"reference_id":"20594156","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":417,"term_name":"phosphorylation display site","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of the cytoplasmic segment of histidine kinase receptor QseC, a key player in bacterial virulence. <i> Xie W, Dickson C, Kwiatkowski W, Choe S. </i> Protein Pept Lett, 2010","term_id":"IDPO:0000045","curator_id":"jpujols","start":386,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","reference_id":"20594156","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00774r003","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":417,"term_name":"small molecule binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of the cytoplasmic segment of histidine kinase receptor QseC, a key player in bacterial virulence. <i> Xie W, Dickson C, Kwiatkowski W, Choe S. </i> Protein Pept Lett, 2010","term_id":"GO:0036094","curator_id":"jpujols","start":386,"term_ontology":"GO","curator_name":"Jordi Pujols Pujol","reference_id":"20594156","version":3,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00774r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P40719","date":"2016-08-16T04:00:29.000Z","acc":"P40719","name":"Sensor protein QseC","length":449,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI0000132E74","genes":[{"name":{"value":"qseC"},"synonyms":[{"value":"ygiY"}],"olnNames":[{"value":"b3026"},{"value":"JW2994"}]}],"alphafold_very_low_content":0.026726057906458798,"disorder_content":0.34743875278396436,"disprot_consensus":{"full":[{"start":35,"end":158,"type":"D"},{"start":386,"end":417,"type":"D"}],"Structural state":[{"start":35,"end":158,"type":"D"},{"start":386,"end":417,"type":"D"}],"Disorder function":[{"start":386,"end":417,"type":"F"}],"Molecular function":[{"start":386,"end":417,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00373","name":"FERM central domain","start":91,"end":206},{"id":"PF00769","name":"Ezrin/radixin/moesin family C terminal","start":511,"end":586},{"id":"PF09379","name":"FERM N-terminal domain","start":9,"end":68},{"id":"PF09380","name":"FERM C-terminal PH-like domain","start":210,"end":298},{"id":"PF20492","name":"Ezrin/radixin/moesin, alpha-helical domain","start":337,"end":456}],"gene3D":[{"start":84,"end":199,"id":"1.20.80.10","name":"1.20.80.10"},{"start":201,"end":296,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":297,"end":346,"id":"1.20.5.450","name":"1.20.5.450"},{"start":1,"end":83,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"}]},"uniref50":"UniRef50_P15311","sequence":"MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKFYPEDVAEELIQDITQKLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEVHKSGYLSSERLIPQRVMDQHKLTRDQWEDRIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILQLCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQRQLLTLSSELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEAL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P15311","disprot_id":"DP00775","ncbi_taxon_id":9606,"regions_counter":9,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":150,"region_id":"DP00775r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the active N-terminal domain of Ezrin. Conformational and mobility changes identify keystone interactions. <i> Smith WJ, Nassar N, Bretscher A, Cerione RA, Karplus PA. </i> J Biol Chem, 2003","term_id":"IDPO:0000002","curator_id":"jpujols","start":130,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1NI2"}],"reference_id":"12429733","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":150,"term_name":"phosphorylation display site","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of the active N-terminal domain of Ezrin. Conformational and mobility changes identify keystone interactions. <i> Smith WJ, Nassar N, Bretscher A, Cerione RA, Karplus PA. </i> J Biol Chem, 2003","term_id":"IDPO:0000045","curator_id":"jpujols","start":130,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","reference_id":"12429733","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00775r002","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":150,"term_name":"order to disorder","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of the active N-terminal domain of Ezrin. Conformational and mobility changes identify keystone interactions. <i> Smith WJ, Nassar N, Bretscher A, Cerione RA, Karplus PA. </i> J Biol Chem, 2003","term_id":"IDPO:0000014","curator_id":"jpujols","start":130,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","reference_id":"12429733","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00775r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":586,"region_id":"DP00775r004","released":"2022_03","ec_id":"ECO:0006214","reference_html":"Open conformation of ezrin bound to phosphatidylinositol 4,5-bisphosphate and to F-actin revealed by neutron scattering. <i> Jayasundar JJ, Ju JH, He L, Liu D, Meilleur F, Zhao J, Callaway DJ, Bu Z. </i> J Biol Chem, 2012","term_id":"IDPO:0000002","curator_id":"jpujols","start":506,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"small-angle neutron scattering evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22927432","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":586,"term_name":"self-inhibition","released":"2022_03","ec_name":"small-angle neutron scattering evidence used in manual assertion","reference_html":"Open conformation of ezrin bound to phosphatidylinositol 4,5-bisphosphate and to F-actin revealed by neutron scattering. <i> Jayasundar JJ, Ju JH, He L, Liu D, Meilleur F, Zhao J, Callaway DJ, Bu Z. </i> J Biol Chem, 2012","term_id":"IDPO:0000059","curator_id":"jpujols","start":506,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","reference_id":"22927432","version":3,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006214","region_id":"DP00775r005","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":586,"term_name":"order to disorder","released":"2022_03","ec_name":"small-angle neutron scattering evidence used in manual assertion","reference_html":"Open conformation of ezrin bound to phosphatidylinositol 4,5-bisphosphate and to F-actin revealed by neutron scattering. <i> Jayasundar JJ, Ju JH, He L, Liu D, Meilleur F, Zhao J, Callaway DJ, Bu Z. </i> J Biol Chem, 2012","term_id":"IDPO:0000014","curator_id":"jpujols","start":506,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","reference_id":"22927432","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006214","region_id":"DP00775r006","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":515,"region_id":"DP00775r007","reference_id":"27364155","start":298,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The final model of the ezrin FERM domain contains two molecules in the asymmetric unit (molecule A — residues 2–296 and molecule B — residues 2–137, 145–146, 150–296), with Cα root mean square deviation (RMSD) of 0.39 Å.","type":"Methods"},{"text":"The structure of Ezrin-1 contains one molecule in the asymmetric unit (residues 1–297 and 516–586), whereas that of Ezrin-2 contains two molecules in the asymmetric unit (molecule A: residues 1–297, 516–586 and molecule B: residues 3–297, 515–586), with Cα RMSD of 0.73 Å over 365 residues.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structural characterization suggests models for monomeric and dimeric forms of full-length ezrin. <i> Phang JM, Harrop SJ, Duff AP, Sokolova AV, Crossett B, Walsh JC, Beckham SA, Nguyen CD, Davies RB, Glöckner C, Bromley EH, Wilk KE, Curmi PM. </i> Biochem J, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4RMA"},{"db":"PDB","id":"4RM9"},{"db":"PDB","id":"4RM8"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":515,"region_id":"DP00775r008","reference_id":"27364155","start":298,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The final model of the ezrin FERM domain contains two molecules in the asymmetric unit (molecule A — residues 2–296 and molecule B — residues 2–137, 145–146, 150–296), with Cα root mean square deviation (RMSD) of 0.39 Å.","type":"Methods"},{"text":"The structure of Ezrin-1 contains one molecule in the asymmetric unit (residues 1–297 and 516–586), whereas that of Ezrin-2 contains two molecules in the asymmetric unit (molecule A: residues 1–297, 516–586 and molecule B: residues 3–297, 515–586), with Cα RMSD of 0.73 Å over 365 residues.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"reference_html":"Structural characterization suggests models for monomeric and dimeric forms of full-length ezrin. <i> Phang JM, Harrop SJ, Duff AP, Sokolova AV, Crossett B, Walsh JC, Beckham SA, Nguyen CD, Davies RB, Glöckner C, Bromley EH, Wilk KE, Curmi PM. </i> Biochem J, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","cross_refs":[{"db":"PDB","id":"4RMA"},{"db":"PDB","id":"4RM9"},{"db":"PDB","id":"4RM8"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":515,"region_id":"DP00775r009","reference_id":"27364155","start":298,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The final model of the ezrin FERM domain contains two molecules in the asymmetric unit (molecule A — residues 2–296 and molecule B — residues 2–137, 145–146, 150–296), with Cα root mean square deviation (RMSD) of 0.39 Å.","type":"Methods"},{"text":"The structure of Ezrin-1 contains one molecule in the asymmetric unit (residues 1–297 and 516–586), whereas that of Ezrin-2 contains two molecules in the asymmetric unit (molecule A: residues 1–297, 516–586 and molecule B: residues 3–297, 515–586), with Cα RMSD of 0.73 Å over 365 residues.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":3,"reference_html":"Structural characterization suggests models for monomeric and dimeric forms of full-length ezrin. <i> Phang JM, Harrop SJ, Duff AP, Sokolova AV, Crossett B, Walsh JC, Beckham SA, Nguyen CD, Davies RB, Glöckner C, Bromley EH, Wilk KE, Curmi PM. </i> Biochem J, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","cross_refs":[{"db":"PDB","id":"4RMA"},{"db":"PDB","id":"4RM9"},{"db":"PDB","id":"4RM8"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P15311","date":"2016-08-16T05:06:15.000Z","acc":"P15311","name":"Ezrin","length":586,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI000016B2F3","genes":[{"name":{"value":"EZR"},"synonyms":[{"value":"VIL2"}]}],"alphafold_very_low_content":0.052901023890784986,"disorder_content":0.5290102389078498,"disprot_consensus":{"full":[{"start":130,"end":150,"type":"T"},{"start":298,"end":505,"type":"D"},{"start":506,"end":586,"type":"T"}],"Structural state":[{"start":130,"end":150,"type":"D"},{"start":298,"end":586,"type":"D"}],"Disorder function":[{"start":130,"end":150,"type":"F"},{"start":506,"end":586,"type":"F"}],"Structural transition":[{"start":130,"end":150,"type":"T"},{"start":506,"end":586,"type":"T"}]}},{"features":{"gene3D":[{"start":83,"end":262,"id":"2.160.20.70","name":"2.160.20.70"}],"pfam":[]},"uniref50":"UniRef50_P46670","sequence":"MDFTAKIKELERELSETSDYKTLQKKTISLRSELNTLSHSLTSYEKEHFSNDIENVLKSINAKLSESKGKKRLFSFKQKNSSSAVHKNVERTELANAPAYTTTLKKHYVLEKGDSAFENLEFCTVTSTTDYSGNSALSGSLCFRNITKCVINLQRIFFQTGSIFITDCTDSIIFLRSPSDKDFQIRLRDLKNCKILIEKLSPSIDCKQVVIIENCHKCIFNASTRDHLIIQDFSNPFQSEETEDNSAFAFEDFDICNKDTMQLFRAYL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P46670","disprot_id":"DP00778","ncbi_taxon_id":559292,"regions_counter":6,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":245,"region_id":"DP00778r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Tubulin cofactors and Arl2 are cage-like chaperones that regulate the soluble αβ-tubulin pool for microtubule dynamics. <i> Nithianantham S, Le S, Seto E, Jia W, Leary J, Corbett KD, Moore JK, Al-Bassam J. </i> Elife, 2015","term_id":"IDPO:0000002","curator_id":"jpujols","start":220,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5CYA"}],"reference_id":"26208336","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":245,"term_name":"phosphorylation display site","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Tubulin cofactors and Arl2 are cage-like chaperones that regulate the soluble αβ-tubulin pool for microtubule dynamics. <i> Nithianantham S, Le S, Seto E, Jia W, Leary J, Corbett KD, Moore JK, Al-Bassam J. </i> Elife, 2015","term_id":"IDPO:0000045","curator_id":"jpujols","start":220,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","reference_id":"26208336","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00778r002","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":245,"term_name":"small molecule binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Tubulin cofactors and Arl2 are cage-like chaperones that regulate the soluble αβ-tubulin pool for microtubule dynamics. <i> Nithianantham S, Le S, Seto E, Jia W, Leary J, Corbett KD, Moore JK, Al-Bassam J. </i> Elife, 2015","term_id":"GO:0036094","curator_id":"jpujols","start":220,"term_ontology":"GO","curator_name":"Jordi Pujols Pujol","reference_id":"26208336","version":3,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00778r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":30,"region_id":"DP00778r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction. <i> Garcia-Mayoral MF, Castaño R, Fanarraga ML, Zabala JC, Rico M, Bruix M. </i> PLoS One, 2011","term_id":"IDPO:0000002","curator_id":"jpujols","start":1,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2L3L"}],"reference_id":"22028797","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":30,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction. <i> Garcia-Mayoral MF, Castaño R, Fanarraga ML, Zabala JC, Rico M, Bruix M. </i> PLoS One, 2011","term_id":"GO:0060090","curator_id":"jpujols","start":1,"term_ontology":"GO","curator_name":"Jordi Pujols Pujol","reference_id":"22028797","version":3,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00778r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":30,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction. <i> Garcia-Mayoral MF, Castaño R, Fanarraga ML, Zabala JC, Rico M, Bruix M. </i> PLoS One, 2011","term_id":"GO:0005515","curator_id":"jpujols","start":1,"term_ontology":"GO","curator_name":"Jordi Pujols Pujol","reference_id":"22028797","version":3,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00778r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P46670","date":"2016-08-16T06:32:00.000Z","acc":"P46670","name":"Tubulin-specific chaperone C","length":268,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000168A3E","genes":[{"name":{"value":"CIN2"},"orfNames":[{"value":"P1043"}],"olnNames":[{"value":"YPL241C"}]}],"alphafold_very_low_content":0.10820895522388059,"disorder_content":0.208955223880597,"disprot_consensus":{"full":[{"start":1,"end":30,"type":"D"},{"start":220,"end":245,"type":"D"}],"Structural state":[{"start":1,"end":30,"type":"D"},{"start":220,"end":245,"type":"D"}],"Disorder function":[{"start":220,"end":245,"type":"F"}],"Molecular function":[{"start":1,"end":30,"type":"F"},{"start":220,"end":245,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00377","name":"Prion/Doppel alpha-helical domain","start":145,"end":262},{"id":"PF03991","name":"Copper binding octapeptide repeat region","start":70,"end":106},{"id":"PF11587","name":"Major prion protein bPrPp - N terminal","start":1,"end":30}]},"uniref50":"UniRef50_P04925","sequence":"MVKSHIGSWILVLFVAMWSDVGLCKKRPKPGGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGGWGQGGTHGQWNKPSKPKTNMKHVAGAAAAGAVVGGLGGYMLGSAMSRPLIHFGSDYEDRYYRENMHRYPNQVYYRPVDQYSNQNNFVHDCVNITVKEHTVTTTTKGENFTETDIKMMERVVEQMCITQYQRESQAYYQRGASVILFSSPPVILLISFLIFLIVG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_Q95211","disprot_id":"DP00783","ncbi_taxon_id":9913,"regions_counter":6,"creator":"mbuitron","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":121,"region_id":"DP00783r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR structure of the bovine prion protein. <i> López Garcia F, Zahn R, Riek R, Wüthrich K. </i> Proc Natl Acad Sci U S A, 2000","term_id":"IDPO:0000002","curator_id":"esalladini","start":23,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":4,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"10899999","statement":[{"text":"The NMR structures of the recombinant 217-residue polypeptide chain of the mature bovine prion protein, bPrP(23-230), and a C-terminal fragment, bPrP(121-230), include a globular domain extending from residue 125 to residue 227, a short flexible chain end of residues 228-230, and an N-terminal flexibly disordered \"tail\" comprising 108 residues for the intact protein and 4 residues for bPrP(121-230), respectively.","type":"Abstract"},{"text":"The NMR structure of the recombinant bPrP(23–230) (Fig. ​(Fig.11a) contains a globular domain that extends approximately from residue 122 to residue 227, where the residues 128–131 form the β-strand 1, 144–154 the α-helix 1 (which has 310-type structure from residue 153 onward), 161–164 the β-strand 2, 173–194 the α-helix 2, and 200–226 the α-helix 3. At both ends of the globular domain there are flexibly disordered polypeptide segments, as evidenced by near-random coil 1H chemical shifts (29) and negative values of the steady-state 15N{1H}-NOEs (Fig. ​2). The N-terminal tail comprising residues 23–121 (because of insertions relative to hPrP this segment includes 108 residues; see ref. 23 for the numeration used) shows exclusively negative NOEs, and because of signal overlap only one set of values was obtained for all six octapeptide segments (23), as indicated by the box in Fig. ​2. The positive NOEs for residues 122–227 are typical for a globular protein of this size (see also below), whereas increased flexibility is again indicated for the C-terminal tripeptide segment (Fig. 2).","type":"Results"}],"cross_refs":[{"db":"PDB","id":"1DX0"},{"db":"PDB","id":"1DX1"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-29T14:51:51.269Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":230,"region_id":"DP00783r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR structure of the bovine prion protein. <i> López Garcia F, Zahn R, Riek R, Wüthrich K. </i> Proc Natl Acad Sci U S A, 2000","term_id":"IDPO:0000002","curator_id":"esalladini","start":219,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1DX0"},{"db":"PDB","id":"1DX1"}],"reference_id":"10899999","statement":[{"text":"The NMR structure of the recombinant bPrP(23–230) ​(Fig.1) contains a globular domain that extends approximately from residue 122 to residue 227, where the residues 128–131 form the β-strand 1, 144–154 the α-helix 1 (which has 310-type structure from residue 153 onward), 161–164 the β-strand 2, 173–194 the α-helix 2, and 200–226 the α-helix 3. At both ends of the globular domain there are flexibly disordered polypeptide segments, as evidenced by near-random coil 1H chemical shifts (29) and negative values of the steady-state 15N{1H}-NOEs (Fig.2).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-29T14:51:45.021Z"}},{"start":108,"end":119,"reference_id":"24803670","reference_source":"pmid","reference_html":"Binding of an RNA aptamer and a partial peptide of a prion protein: crucial importance of water entropy in molecular recognition. <i> Hayashi T, Oshima H, Mashima T, Nagata T, Katahira M, Kinoshita M. </i> Nucleic Acids Res, 2014","date":"2022-05-31T15:21:32.749Z","curator_id":"mbuitron","curator_name":"Martín González Buitrón","curator_orcid":"0000-0003-1123-9853","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"2RU7"}],"region_id":"DP00783r004","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS000080E0D2_32630"}],"statement":[{"text":"The structure of the aptamer remains unchanged in some cases, and disordered, flexible portions of its targets become structured upon binding.","type":"Introduction"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T12:12:59.143Z"}},{"start":108,"end":119,"reference_id":"24803670","reference_source":"pmid","reference_html":"Binding of an RNA aptamer and a partial peptide of a prion protein: crucial importance of water entropy in molecular recognition. <i> Hayashi T, Oshima H, Mashima T, Nagata T, Katahira M, Kinoshita M. </i> Nucleic Acids Res, 2014","date":"2022-05-31T15:32:02.261Z","curator_id":"mbuitron","curator_name":"Martín González Buitrón","curator_orcid":"0000-0003-1123-9853","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP00783r005","statement":[{"text":"The structure of the aptamer remains unchanged in some cases, and disordered, flexible portions of its targets become structured upon binding.","type":"Introduction"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T12:13:03.547Z"}},{"start":108,"end":119,"reference_id":"24803670","reference_source":"pmid","reference_html":"Binding of an RNA aptamer and a partial peptide of a prion protein: crucial importance of water entropy in molecular recognition. <i> Hayashi T, Oshima H, Mashima T, Nagata T, Katahira M, Kinoshita M. </i> Nucleic Acids Res, 2014","date":"2022-05-31T15:42:28.091Z","curator_id":"mbuitron","curator_name":"Martín González Buitrón","curator_orcid":"0000-0003-1123-9853","term_id":"GO:0002151","term_name":"G-quadruplex RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"annotation_extensions":[],"cross_refs":[{"db":"PDB","id":"2RU7"}],"ec_go":"EXP","interaction_partner":[{"db":"RNAcentral","id":"URS000080E0D2_32630","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00783r006","statement":[{"text":"The structure of the aptamer remains unchanged in some cases, and disordered, flexible portions of its targets become structured upon binding.","type":"Introduction"}],"term_comment":"The structures of RNA and DNA G quartets differ regarding sugar conformation so that a protein binding to the RNA structure might not bind to the DNA structure.","term_def":"\"Binding to a G-quadruplex RNA structure, in which groups of four guanines adopt a flat, cyclic hydrogen-bonding arrangement known as a guanine tetrad.\" [PMID:18294969, PMID:18568163, PMID:19330720]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T12:12:59.996Z"}}],"released":"2016_10","uniref100":"UniRef100_P10279","date":"2016-08-16T07:52:49.000Z","acc":"P10279","name":"Major prion protein","length":264,"organism":"Bos taurus","dataset":["RNA-binding proteins"],"UniParc":"UPI00001777E8","genes":[{"name":{"value":"PRNP"},"synonyms":[{"value":"PRP"}]}],"alphafold_very_low_content":0.4015151515151515,"disorder_content":0.42045454545454547,"disprot_consensus":{"full":[{"start":23,"end":107,"type":"D"},{"start":108,"end":119,"type":"T"},{"start":120,"end":121,"type":"D"},{"start":219,"end":230,"type":"D"}],"Structural state":[{"start":23,"end":121,"type":"D"},{"start":219,"end":230,"type":"D"}],"Structural transition":[{"start":108,"end":119,"type":"T"}],"Molecular function":[{"start":108,"end":119,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02229","name":"Transcriptional Coactivator p15 (PC4)","start":53,"end":104}],"gene3D":[{"start":42,"end":121,"id":"2.30.31.10","name":"Transcriptional Coactivator Pc4; Chain A"}]},"uniref50":"UniRef50_L7IX95","sequence":"MAPKMTSKKRARDEEAQSGGSEAETKPAPVKKAKSKASNPGGSQVDAEGNPFWEISDKRRVGISQFKKMDFINIREYYEAGGEMKPGKKGIGLTVDQYTAFLKAIPAINAELRSRGHDITDDSDGGGAPVVAKPEGNAKKSTKKQEKKANIEATSDEGSGSD","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Sordariomycetidae","Magnaporthales","Pyriculariaceae","Pyricularia"],"uniref90":"UniRef90_L7IX95","disprot_id":"DP00786","ncbi_taxon_id":242507,"regions_counter":2,"creator":"sventura","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":38,"region_id":"DP00786r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Substitution of tryptophan 89 with tyrosine switches the DNA binding mode of PC4. <i> Huang J, Zhao Y, Liu H, Huang D, Cheng X, Zhao W, Taylor IA, Liu J, Peng YL. </i> Sci Rep, 2015","term_id":"IDPO:0000002","curator_id":"sventura","start":1,"term_ontology":"IDPO","curator_name":"Salvador Ventura","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4AGH"}],"reference_id":"25739870","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":158,"region_id":"DP00786r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Substitution of tryptophan 89 with tyrosine switches the DNA binding mode of PC4. <i> Huang J, Zhao Y, Liu H, Huang D, Cheng X, Zhao W, Taylor IA, Liu J, Peng YL. </i> Sci Rep, 2015","term_id":"IDPO:0000002","curator_id":"sventura","start":117,"term_ontology":"IDPO","curator_name":"Salvador Ventura","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4AGH"}],"reference_id":"25739870","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_L7IX95","date":"2016-08-17T19:09:19.000Z","acc":"G4NEJ8","name":"PC4 domain-containing protein","length":162,"organism":"Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)","dataset":[],"UniParc":"UPI000021B8EE","genes":[{"orfNames":[{"value":"MGG_00780","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EHA48628.1","url":"https://www.ebi.ac.uk/ena/browser/view/EHA48628.1"}}]}]}],"alphafold_very_low_content":0.3765432098765432,"disorder_content":0.49382716049382713,"disprot_consensus":{"full":[{"start":1,"end":38,"type":"D"},{"start":117,"end":158,"type":"D"}],"Structural state":[{"start":1,"end":38,"type":"D"},{"start":117,"end":158,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02018","name":"Carbohydrate binding domain","start":32,"end":131},{"id":"PF08787","name":"Alginate lyase","start":197,"end":384}]},"uniref50":"UniRef50_Q9Z6D6","sequence":"MFRFKGIRIMINHKKLFIYSAIATSSALSHAATINNAGFESGFSNWNETDPAAISSDAYSGSKSLKIQGSPARVYQVVDIQPNTEYTLSAYVLGKGQIGVNDLNGLFKNQTFNVSSWTKVTKTFTSANTNSLQVFAKHYNNTSDVRFDNFSLIEGSGSNDGGSDGGSDNSNGSTIPSSITSGSIFDLEGDNPNPLVDDSTLVFVPLEAQHITPNGNGWRHEYKVKESLRVAMTQTYEVFEATVKVEMSDGGKTIISQHHASDTGTISKVYVSDTDESGFNDSVANNGIFDVYVRLRNTSGNEEKFALGTMTSGETFNLRVVNNYGDVEVTAFGNSFGIPVEDDSQSYFKFGNYLQSQDPYTLDKCGEAGNSNSFKNCFEDLGITESKVTMTNVSYTRETN","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Alteromonadales","Pseudoalteromonadaceae","Pseudoalteromonas"],"uniref90":"UniRef90_N6V1L4","disprot_id":"DP00787","ncbi_taxon_id":515257,"regions_counter":1,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":155,"region_id":"DP00787r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Molecular insight into the role of the N-terminal extension in the maturation, substrate recognition, and catalysis of a bacterial alginate lyase from polysaccharide lyase family 18. <i> Dong S, Wei TD, Chen XL, Li CY, Wang P, Xie BB, Qin QL, Zhang XY, Pang XH, Zhou BC, Zhang YZ. </i> J Biol Chem, 2014","term_id":"IDPO:0000002","curator_id":"rdavidovic","start":32,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4Q8K"}],"reference_id":"25210041","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_B2LME8","date":"2016-08-18T10:25:52.000Z","acc":"B2LME8","name":"Alginase","length":400,"organism":"Pseudoalteromonas sp. SM0524","dataset":[],"UniParc":"UPI0004540354","genes":[],"alphafold_very_low_content":0.1175,"disorder_content":0.31,"disprot_consensus":{"full":[{"start":32,"end":155,"type":"D"}],"Structural state":[{"start":32,"end":155,"type":"D"}]}},{"features":{"pfam":[{"id":"PF04000","name":"Sas10/Utp3/C1D family","start":12,"end":89}]},"uniref50":"UniRef50_P38801","sequence":"MEDIEKIKPYVRSFSKALDELKPEIEKLTSKSLDEQLLLLSDERAKLELINRYAYVLSSLMFANMKVLGVKDMSPILGELKRVKSYMDKAKQYDNRITKSNEKSQAEQEKAKNIISNVLDGNKNQFEPSISRSNFQGKHTKFENDELAESTTTKIIDSTDHIRKASSKKSKRLDKVGKKKGGKK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P38801","disprot_id":"DP00788","ncbi_taxon_id":559292,"regions_counter":1,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":184,"region_id":"DP00788r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"RNA degradation paths in a 12-subunit nuclear exosome complex. <i> Makino DL, Schuch B, Stegmann E, Baumgärtner M, Basquin C, Conti E. </i> Nature, 2015","term_id":"IDPO:0000002","curator_id":"rdavidovic","start":118,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"26222026","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P38801","date":"2016-08-18T13:40:44.000Z","acc":"P38801","name":"Exosome complex protein LRP1","length":184,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000005318B","genes":[{"name":{"value":"LRP1"},"synonyms":[{"value":"RRP47"},{"value":"YC1D"}],"olnNames":[{"value":"YHR081W"}]}],"alphafold_very_low_content":0.14130434782608695,"disorder_content":0.3641304347826087,"disprot_consensus":{"full":[{"start":118,"end":184,"type":"D"}],"Structural state":[{"start":118,"end":184,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01253","name":"Translation initiation factor SUI1","start":31,"end":102}],"gene3D":[{"start":28,"end":108,"id":"3.30.780.10","name":"SUI1-like domain"}]},"uniref50":"UniRef50_P08245","sequence":"MSDSNSRLVYSTETGRIDEPKAAPVRPKGDGVVRIQRQTSGRKGKGVCLITGVDLDDAELTKLAAELKKKCGCGGAVKDGVIEIQGDKRDLLKSLLEAKGMKVKLAGG","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P08245","disprot_id":"DP00790","ncbi_taxon_id":83333,"regions_counter":1,"creator":"ameszaros","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":31,"region_id":"DP00790r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A phylogenetic approach to target selection for structural genomics: solution structure of YciH. <i> Cort JR, Koonin EV, Bash PA, Kennedy MA. </i> Nucleic Acids Res, 1999","term_id":"IDPO:0000002","curator_id":"ameszaros","start":1,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"10497266","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1D1R"}],"term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P08245","date":"2016-08-18T16:02:45.000Z","acc":"P08245","name":"Uncharacterized protein YciH","length":108,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI000013A6BE","genes":[{"name":{"value":"yciH"},"olnNames":[{"value":"b1282"},{"value":"JW1274"}]}],"alphafold_very_low_content":0.07407407407407407,"disorder_content":0.28703703703703703,"disprot_consensus":{"full":[{"start":1,"end":31,"type":"D"}],"Structural state":[{"start":1,"end":31,"type":"D"}]}},{"features":{"pfam":[{"id":"PF13397","name":"RNA polymerase-binding protein","start":4,"end":106}],"gene3D":[{"start":1,"end":79,"id":"2.20.28.270","name":"RNA polymerase-binding protein A"}]},"uniref50":"UniRef50_P9WHJ4","sequence":"MADRVLRGSRLGAVSYETDRNHDLAPRQIARYRTDNGEEFEVPFADDAEIPGTWLCRNGMEGTLIEGDLPEPKKVKPPRTHWDMLLERRSIEELEELLKERLELIRSRRRG","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"uniref90":"UniRef90_P9WHJ4","disprot_id":"DP00791","ncbi_taxon_id":83332,"regions_counter":5,"creator":"tlazar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":25,"region_id":"DP00791r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Mycobacterium tuberculosis RNA polymerase-binding protein A (RbpA) and its interactions with sigma factors. <i> Bortoluzzi A, Muskett FW, Waters LC, Addis PW, Rieck B, Munder T, Schleier S, Forti F, Ghisotti D, Carr MD, O'Hare HM. </i> J Biol Chem, 2013","term_id":"IDPO:0000002","curator_id":"tlazar","start":1,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2M4V"}],"reference_id":"23548911","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":25,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Mycobacterium tuberculosis RNA polymerase-binding protein A (RbpA) and its interactions with sigma factors. <i> Bortoluzzi A, Muskett FW, Waters LC, Addis PW, Rieck B, Munder T, Schleier S, Forti F, Ghisotti D, Carr MD, O'Hare HM. </i> J Biol Chem, 2013","term_id":"GO:0005515","curator_id":"tlazar","start":1,"term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"23548911","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00791r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":26,"region_id":"DP00791r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural, functional, and genetic analyses of the actinobacterial transcription factor RbpA. <i> Hubin EA, Tabib-Salazar A, Humphrey LJ, Flack JE, Olinares PD, Darst SA, Campbell EA, Paget MS. </i> Proc Natl Acad Sci U S A, 2015","term_id":"IDPO:0000002","curator_id":"tlazar","start":1,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4X8K"}],"reference_id":"26040003","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":26,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural, functional, and genetic analyses of the actinobacterial transcription factor RbpA. <i> Hubin EA, Tabib-Salazar A, Humphrey LJ, Flack JE, Olinares PD, Darst SA, Campbell EA, Paget MS. </i> Proc Natl Acad Sci U S A, 2015","term_id":"GO:0003676","curator_id":"tlazar","start":1,"term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"26040003","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00791r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":79,"region_id":"DP00791r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Mycobacterium tuberculosis RNA polymerase-binding protein A (RbpA) and its interactions with sigma factors. <i> Bortoluzzi A, Muskett FW, Waters LC, Addis PW, Rieck B, Munder T, Schleier S, Forti F, Ghisotti D, Carr MD, O'Hare HM. </i> J Biol Chem, 2013","term_id":"IDPO:0000002","curator_id":"tlazar","start":69,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2M4V"}],"reference_id":"23548911","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P9WHJ4","date":"2016-08-18T17:18:23.000Z","acc":"P9WHJ5","name":"RNA polymerase-binding protein RbpA","length":111,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","dataset":[],"UniParc":"UPI00000317B5","genes":[{"name":{"value":"rbpA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01483","url":"https://hamap.expasy.org/unirule/MF_01483"}}]},"olnNames":[{"value":"Rv2050"}]}],"alphafold_very_low_content":0.009009009009009009,"disorder_content":0.3333333333333333,"disprot_consensus":{"full":[{"start":1,"end":26,"type":"D"},{"start":69,"end":79,"type":"D"}],"Structural state":[{"start":1,"end":26,"type":"D"},{"start":69,"end":79,"type":"D"}],"Molecular function":[{"start":1,"end":26,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01241","name":"Photosystem I psaG / psaK","start":48,"end":125}],"gene3D":[{"start":43,"end":131,"id":"1.10.286.40","name":"Chlorophyll a-b binding protein like"}]},"uniref50":"UniRef50_Q9SUI5","sequence":"MASQLSAMTSVPQFHGLRTYSSPRSMATLPSLRRRRSQGIRCDYIGSSTNLIMVTTTTLMLFAGRFGLAPSANRKATAGLKLEARESGLQTGDPAGFTLADTLACGAVGHIMGVGIVLGLKNTGVLDQIIG","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","BOP clade","Pooideae","Triticodae","Triticeae","Hordeinae","Hordeum"],"uniref90":"UniRef90_P36886","disprot_id":"DP00792","ncbi_taxon_id":4513,"regions_counter":2,"creator":"ameszaros","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":42,"region_id":"DP00792r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure determination and improved model of plant photosystem I. <i> Amunts A, Toporik H, Borovikova A, Nelson N. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"ameszaros","start":1,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"19923216","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2WSC"},{"db":"PDB","id":"2WSE"},{"db":"PDB","id":"2WSF"}],"term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P36886","date":"2016-08-18T19:05:20.000Z","acc":"P36886","name":"Photosystem I reaction center subunit psaK, chloroplastic","length":131,"organism":"Hordeum vulgare","dataset":[],"UniParc":"UPI000013256D","genes":[{"name":{"value":"PSAK"}}],"alphafold_very_low_content":0.22137404580152673,"disorder_content":0.32061068702290074,"disprot_consensus":{"full":[{"start":1,"end":42,"type":"D"}],"Structural state":[{"start":1,"end":42,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00428","name":"60s Acidic ribosomal protein","start":17,"end":114}],"gene3D":[{"start":1,"end":60,"id":"1.10.10.1410","name":"1.10.10.1410"}]},"uniref50":"UniRef50_P05387","sequence":"MRYVASYLLAALGGNSSPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGIGKLASVPAGGAVAVSAAPGSAAPAAGSAPAAAEEKKDEKKEESEESDDDMGFGLFD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P05387","disprot_id":"DP00793","ncbi_taxon_id":9606,"regions_counter":4,"creator":"ameszaros","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":115,"region_id":"DP00793r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of human P1•P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosome. <i> Lee KM, Yusa K, Chu LO, Yu CW, Oono M, Miyoshi T, Ito K, Shaw PC, Wong KB, Uchiumi T. </i> Nucleic Acids Res, 2013","term_id":"IDPO:0000002","curator_id":"ameszaros","start":63,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"23892290","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4BEH"}],"term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":115,"region_id":"DP00793r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Correlation between conformation and antibody binding: NMR structure of cross-reactive peptides from T. cruzi, human and L. braziliensis. <i> Soares MR, Bisch PM, Campos de Carvalho AC, Valente AP, Almeida FC. </i> FEBS Lett, 2004","term_id":"IDPO:0000002","curator_id":"ameszaros","start":102,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"14988012","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1S4J"}],"term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":115,"term_name":"order to disorder","start":102,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ameszaros","released":"2022_03","term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"14988012","version":2,"reference_html":"Correlation between conformation and antibody binding: NMR structure of cross-reactive peptides from T. cruzi, human and L. braziliensis. <i> Soares MR, Bisch PM, Campos de Carvalho AC, Valente AP, Almeida FC. </i> FEBS Lett, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000014","ec_id":"ECO:0006165","region_id":"DP00793r003","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":115,"term_name":"protein binding","start":102,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ameszaros","released":"2022_03","term_ontology":"GO","curator_name":"Attila Meszaros","reference_id":"14988012","version":3,"reference_html":"Correlation between conformation and antibody binding: NMR structure of cross-reactive peptides from T. cruzi, human and L. braziliensis. <i> Soares MR, Bisch PM, Campos de Carvalho AC, Valente AP, Almeida FC. </i> FEBS Lett, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00793r004","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P05387","date":"2016-08-18T19:48:09.000Z","acc":"P05387","name":"60S acidic ribosomal protein P2","length":115,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000134258","genes":[{"name":{"value":"RPLP2"},"synonyms":[{"value":"D11S2243E"},{"value":"RPP2"}]}],"alphafold_very_low_content":0.3217391304347826,"disorder_content":0.4608695652173913,"disprot_consensus":{"full":[{"start":63,"end":101,"type":"D"},{"start":102,"end":115,"type":"T"}],"Structural state":[{"start":63,"end":115,"type":"D"}],"Structural transition":[{"start":102,"end":115,"type":"T"}],"Molecular function":[{"start":102,"end":115,"type":"F"}]}},{"features":{"pfam":[{"id":"PF07742","name":"BTG family","start":1,"end":113}],"gene3D":[{"start":1,"end":122,"id":"1.20.120.1120","name":"Anti-proliferative protein, N-terminal domain"}]},"uniref50":"UniRef50_P50616","sequence":"MQLEIQVALNFIISYLYNKLPRRRVNIFGEELERLLKKKYEGHWYPEKPYKGSGFRCIHIGEKVDPVIEQASKESGLDIDDVRGNLPQDLSVWIDPFEVSYQIGEKGPVKVLYVDDNNENGCELDKEIKNSFNPEAQVFMPISDPASSVSSSPSPPFGHSAAVSPTFMPRSTQPLTFTTATFAATKFGSTKMKNSGRSNKVARTSPINLGLNVNDLLKQKAISSSMHSLYGLGLGSQQQPQQQQQPAQPPPPPPPPQQQQQQKTSALSPNAKEFIFPNMQGQGSSTNGMFPGDSPLNLSPLQYSNAFDVFAAYGGLNEKSFVDGLNFSLNNMQYSNQQFQPVMAN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P50616","disprot_id":"DP00794","ncbi_taxon_id":9606,"regions_counter":4,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":138,"region_id":"DP00794r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for the antiproliferative activity of the Tob-hCaf1 complex. <i> Horiuchi M, Takeuchi K, Noda N, Muroya N, Suzuki T, Nakamura T, Kawamura-Tsuzuku J, Takahasi K, Yamamoto T, Inagaki F. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"atantos","start":116,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2D5R"}],"reference_id":"19276069","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":285,"region_id":"DP00794r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Quantitative characterization of Tob interactions provides the thermodynamic basis for translation termination-coupled deadenylase regulation. <i> Ruan L, Osawa M, Hosoda N, Imai S, Machiyama A, Katada T, Hoshino S, Shimada I. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"atantos","start":147,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20595394","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":345,"region_id":"DP00794r003","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Quantitative characterization of Tob interactions provides the thermodynamic basis for translation termination-coupled deadenylase regulation. <i> Ruan L, Osawa M, Hosoda N, Imai S, Machiyama A, Katada T, Hoshino S, Shimada I. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"atantos","start":147,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20595394","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":345,"region_id":"DP00794r004","reference_id":"26518565","start":117,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"No density is visible for residues 117–345 of Vps36 crystals of Tob1","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structural basis for inhibition of the Tob-CNOT7 interaction by a fragment screening approach. <i> Bai Y, Tashiro S, Nagatoishi S, Suzuki T, Yan D, Liu R, Tsumoto K, Bartlam M, Yamamoto T. </i> Protein Cell, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5CI9"},{"db":"PDB","id":"5CI8"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P50616","date":"2016-08-18T22:54:56.000Z","acc":"P50616","name":"Protein Tob1","length":345,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00001370FB","genes":[{"name":{"value":"TOB1"},"synonyms":[{"value":"TOB"},{"value":"TROB1"}]}],"alphafold_very_low_content":0.4057971014492754,"disorder_content":0.6666666666666666,"disprot_consensus":{"full":[{"start":116,"end":345,"type":"D"}],"Structural state":[{"start":116,"end":345,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01290","name":"Thymosin beta-4 family","start":3,"end":41}],"gene3D":[{"start":2,"end":41,"id":"1.20.5.520","name":"Single helix bin"}]},"uniref50":"UniRef50_P62328","sequence":"MSDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P62328","disprot_id":"DP00795","ncbi_taxon_id":9913,"regions_counter":30,"creator":"tlazar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":44,"region_id":"DP00795r001","released":"2022_03","ec_id":"ECO:0006198","reference_html":"How a single residue in individual β-thymosin/WH2 domains controls their functions in actin assembly. <i> Didry D, Cantrelle FX, Husson C, Roblin P, Moorthy AM, Perez J, Le Clainche C, Hertzog M, Guittet E, Carlier MF, van Heijenoort C, Renault L. </i> EMBO J, 2012","term_id":"IDPO:0000002","curator_id":"tlazar","start":13,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22193718","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":44,"term_name":"protein sequestering activity","released":"2022_03","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","reference_html":"How a single residue in individual β-thymosin/WH2 domains controls their functions in actin assembly. <i> Didry D, Cantrelle FX, Husson C, Roblin P, Moorthy AM, Perez J, Le Clainche C, Hertzog M, Guittet E, Carlier MF, van Heijenoort C, Renault L. </i> EMBO J, 2012","term_id":"GO:0140311","curator_id":"tlazar","start":13,"term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"22193718","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006198","region_id":"DP00795r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a specific protein, to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:1493333]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":44,"term_name":"disorder to order","released":"2022_03","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","reference_html":"How a single residue in individual β-thymosin/WH2 domains controls their functions in actin assembly. <i> Didry D, Cantrelle FX, Husson C, Roblin P, Moorthy AM, Perez J, Le Clainche C, Hertzog M, Guittet E, Carlier MF, van Heijenoort C, Renault L. </i> EMBO J, 2012","term_id":"IDPO:0000011","curator_id":"tlazar","start":13,"term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"22193718","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006198","region_id":"DP00795r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":44,"term_name":"protein binding","released":"2022_03","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","reference_html":"How a single residue in individual β-thymosin/WH2 domains controls their functions in actin assembly. <i> Didry D, Cantrelle FX, Husson C, Roblin P, Moorthy AM, Perez J, Le Clainche C, Hertzog M, Guittet E, Carlier MF, van Heijenoort C, Renault L. </i> EMBO J, 2012","term_id":"GO:0005515","curator_id":"tlazar","start":13,"term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"22193718","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006198","region_id":"DP00795r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":44,"region_id":"DP00795r005","released":"2022_03","ec_id":"ECO:0006198","reference_html":"Solution conformation of thymosin beta 4: a nuclear magnetic resonance and simulated annealing study. <i> Zarbock J, Oschkinat H, Hannappel E, Kalbacher H, Voelter W, Holak TA. </i> Biochemistry, 1990","term_id":"IDPO:0000002","curator_id":"tlazar","start":1,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"2261438","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":44,"region_id":"DP00795r006","released":"2022_03","ec_id":"ECO:0006198","reference_html":"Conformation of thymosin beta 4 in water determined by NMR spectroscopy. <i> Czisch M, Schleicher M, Hörger S, Voelter W, Holak TA. </i> Eur J Biochem, 1993","term_id":"IDPO:0000002","curator_id":"tlazar","start":1,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"8269922","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":44,"term_name":"protein sequestering activity","released":"2022_03","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","reference_html":"Conformation of thymosin beta 4 in water determined by NMR spectroscopy. <i> Czisch M, Schleicher M, Hörger S, Voelter W, Holak TA. </i> Eur J Biochem, 1993","term_id":"GO:0140311","curator_id":"tlazar","start":1,"term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"8269922","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006198","region_id":"DP00795r007","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a specific protein, to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:1493333]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":44,"region_id":"DP00795r008","released":"2022_03","ec_id":"ECO:0006198","reference_html":"Coupling of folding and binding of thymosin beta4 upon interaction with monomeric actin monitored by nuclear magnetic resonance. <i> Domanski M, Hertzog M, Coutant J, Gutsche-Perelroizen I, Bontems F, Carlier MF, Guittet E, van Heijenoort C. </i> J Biol Chem, 2004","term_id":"IDPO:0000002","curator_id":"tlazar","start":1,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"15039431","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":44,"term_name":"protein sequestering activity","released":"2022_03","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","reference_html":"Coupling of folding and binding of thymosin beta4 upon interaction with monomeric actin monitored by nuclear magnetic resonance. <i> Domanski M, Hertzog M, Coutant J, Gutsche-Perelroizen I, Bontems F, Carlier MF, Guittet E, van Heijenoort C. </i> J Biol Chem, 2004","term_id":"GO:0140311","curator_id":"tlazar","start":1,"term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"15039431","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006198","region_id":"DP00795r009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a specific protein, to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:1493333]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":30,"region_id":"DP00795r015","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Coupling of folding and binding of thymosin beta4 upon interaction with monomeric actin monitored by nuclear magnetic resonance. <i> Domanski M, Hertzog M, Coutant J, Gutsche-Perelroizen I, Bontems F, Carlier MF, Guittet E, van Heijenoort C. </i> J Biol Chem, 2004","term_id":"IDPO:0000002","curator_id":"tlazar","start":14,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1UY5"}],"reference_id":"15039431","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":30,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Coupling of folding and binding of thymosin beta4 upon interaction with monomeric actin monitored by nuclear magnetic resonance. <i> Domanski M, Hertzog M, Coutant J, Gutsche-Perelroizen I, Bontems F, Carlier MF, Guittet E, van Heijenoort C. </i> J Biol Chem, 2004","term_id":"GO:0005515","curator_id":"tlazar","start":14,"term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"15039431","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00795r016","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":40,"region_id":"DP00795r017","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Coupling of folding and binding of thymosin beta4 upon interaction with monomeric actin monitored by nuclear magnetic resonance. <i> Domanski M, Hertzog M, Coutant J, Gutsche-Perelroizen I, Bontems F, Carlier MF, Guittet E, van Heijenoort C. </i> J Biol Chem, 2004","term_id":"IDPO:0000002","curator_id":"tlazar","start":31,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1UY5"}],"reference_id":"15039431","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":40,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Coupling of folding and binding of thymosin beta4 upon interaction with monomeric actin monitored by nuclear magnetic resonance. <i> Domanski M, Hertzog M, Coutant J, Gutsche-Perelroizen I, Bontems F, Carlier MF, Guittet E, van Heijenoort C. </i> J Biol Chem, 2004","term_id":"IDPO:0000011","curator_id":"tlazar","start":31,"term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"15039431","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00795r018","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":40,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Coupling of folding and binding of thymosin beta4 upon interaction with monomeric actin monitored by nuclear magnetic resonance. <i> Domanski M, Hertzog M, Coutant J, Gutsche-Perelroizen I, Bontems F, Carlier MF, Guittet E, van Heijenoort C. </i> J Biol Chem, 2004","term_id":"GO:0005515","curator_id":"tlazar","start":31,"term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"15039431","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00795r019","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":39,"region_id":"DP00795r022","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis of actin sequestration by thymosin-beta4: implications for WH2 proteins. <i> Irobi E, Aguda AH, Larsson M, Guerin C, Yin HL, Burtnick LD, Blanchoin L, Robinson RC. </i> EMBO J, 2004","term_id":"IDPO:0000002","curator_id":"tlazar","start":30,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1T44"}],"reference_id":"15329672","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":39,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural basis of actin sequestration by thymosin-beta4: implications for WH2 proteins. <i> Irobi E, Aguda AH, Larsson M, Guerin C, Yin HL, Burtnick LD, Blanchoin L, Robinson RC. </i> EMBO J, 2004","term_id":"IDPO:0000011","curator_id":"tlazar","start":30,"term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"15329672","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00795r023","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":39,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural basis of actin sequestration by thymosin-beta4: implications for WH2 proteins. <i> Irobi E, Aguda AH, Larsson M, Guerin C, Yin HL, Burtnick LD, Blanchoin L, Robinson RC. </i> EMBO J, 2004","term_id":"GO:0005515","curator_id":"tlazar","start":30,"term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"15329672","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00795r024","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":44,"region_id":"DP00795r025","released":"2022_03","ec_id":"ECO:0006220","reference_html":"How a single residue in individual β-thymosin/WH2 domains controls their functions in actin assembly. <i> Didry D, Cantrelle FX, Husson C, Roblin P, Moorthy AM, Perez J, Le Clainche C, Hertzog M, Guittet E, Carlier MF, van Heijenoort C, Renault L. </i> EMBO J, 2012","term_id":"IDPO:0000002","curator_id":"tlazar","start":22,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3SJH"}],"reference_id":"22193718","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":44,"term_name":"protein sequestering activity","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"How a single residue in individual β-thymosin/WH2 domains controls their functions in actin assembly. <i> Didry D, Cantrelle FX, Husson C, Roblin P, Moorthy AM, Perez J, Le Clainche C, Hertzog M, Guittet E, Carlier MF, van Heijenoort C, Renault L. </i> EMBO J, 2012","term_id":"GO:0140311","curator_id":"tlazar","start":22,"term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"22193718","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00795r026","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a specific protein, to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:1493333]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":44,"region_id":"DP00795r027","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Solution conformation of thymosin beta 4: a nuclear magnetic resonance and simulated annealing study. <i> Zarbock J, Oschkinat H, Hannappel E, Kalbacher H, Voelter W, Holak TA. </i> Biochemistry, 1990","term_id":"IDPO:0000002","curator_id":"tlazar","start":1,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"2261438","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":44,"term_name":"protein sequestering activity","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Solution conformation of thymosin beta 4: a nuclear magnetic resonance and simulated annealing study. <i> Zarbock J, Oschkinat H, Hannappel E, Kalbacher H, Voelter W, Holak TA. </i> Biochemistry, 1990","term_id":"GO:0140311","curator_id":"tlazar","start":1,"term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"2261438","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00795r028","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a specific protein, to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:1493333]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":44,"region_id":"DP00795r029","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Conformation of thymosin beta 4 in water determined by NMR spectroscopy. <i> Czisch M, Schleicher M, Hörger S, Voelter W, Holak TA. </i> Eur J Biochem, 1993","term_id":"IDPO:0000002","curator_id":"tlazar","start":1,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"8269922","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":44,"term_name":"protein sequestering activity","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Conformation of thymosin beta 4 in water determined by NMR spectroscopy. <i> Czisch M, Schleicher M, Hörger S, Voelter W, Holak TA. </i> Eur J Biochem, 1993","term_id":"GO:0140311","curator_id":"tlazar","start":1,"term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"8269922","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00795r030","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a specific protein, to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:1493333]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P62328","date":"2016-08-19T14:25:05.000Z","acc":"P62326","name":"Thymosin beta-4","length":44,"organism":"Bos taurus","dataset":[],"UniParc":"UPI000004613E","genes":[{"name":{"value":"TMSB4"},"synonyms":[{"value":"THYB4"}]}],"alphafold_very_low_content":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":12,"type":"D"},{"start":13,"end":44,"type":"T"}],"Structural state":[{"start":1,"end":44,"type":"D"}],"Molecular function":[{"start":1,"end":44,"type":"F"}],"Structural transition":[{"start":13,"end":44,"type":"T"}]}},{"features":{"pfam":[{"id":"PF02060","name":"Slow voltage-gated potassium channel","start":1,"end":126}]},"uniref50":"UniRef50_P15382","sequence":"MILSNTTAVTPFLTKLWQETVQQGGNMSGLARRSPRSSDGKLEALYVLMVLGFFGFFTLGIMLSYIRSKKLEHSNDPFNVYIESDAWQEKDKAYVQARVLESYRSCYVVENHLAIEQPNTHLPETKPSP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P15382","disprot_id":"DP00796","ncbi_taxon_id":9606,"regions_counter":6,"creator":"mmacossay","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":129,"region_id":"DP00796r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of KCNE1 and implications for how it modulates the KCNQ1 potassium channel. <i> Kang C, Tian C, Sönnichsen FD, Smith JA, Meiler J, George AL, Vanoye CG, Kim HJ, Sanders CR. </i> Biochemistry, 2008","term_id":"IDPO:0000002","curator_id":"mmacossay","start":107,"term_ontology":"IDPO","curator_name":"Mauricio Macossay-Castillo","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2K21"}],"reference_id":"18611041","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":129,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structure of KCNE1 and implications for how it modulates the KCNQ1 potassium channel. <i> Kang C, Tian C, Sönnichsen FD, Smith JA, Meiler J, George AL, Vanoye CG, Kim HJ, Sanders CR. </i> Biochemistry, 2008","term_id":"GO:0005515","curator_id":"mmacossay","start":107,"term_ontology":"GO","curator_name":"Mauricio Macossay-Castillo","reference_id":"18611041","version":3,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00796r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":45,"region_id":"DP00796r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of KCNE1 and implications for how it modulates the KCNQ1 potassium channel. <i> Kang C, Tian C, Sönnichsen FD, Smith JA, Meiler J, George AL, Vanoye CG, Kim HJ, Sanders CR. </i> Biochemistry, 2008","term_id":"IDPO:0000002","curator_id":"mmacossay","start":24,"term_ontology":"IDPO","curator_name":"Mauricio Macossay-Castillo","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2K21"}],"reference_id":"18611041","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":45,"term_name":"flexible linker","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structure of KCNE1 and implications for how it modulates the KCNQ1 potassium channel. <i> Kang C, Tian C, Sönnichsen FD, Smith JA, Meiler J, George AL, Vanoye CG, Kim HJ, Sanders CR. </i> Biochemistry, 2008","term_id":"IDPO:0000033","curator_id":"mmacossay","start":24,"term_ontology":"IDPO","curator_name":"Mauricio Macossay-Castillo","reference_id":"18611041","version":3,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00796r004","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":91,"region_id":"DP00796r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of KCNE1 and implications for how it modulates the KCNQ1 potassium channel. <i> Kang C, Tian C, Sönnichsen FD, Smith JA, Meiler J, George AL, Vanoye CG, Kim HJ, Sanders CR. </i> Biochemistry, 2008","term_id":"IDPO:0000002","curator_id":"mmacossay","start":72,"term_ontology":"IDPO","curator_name":"Mauricio Macossay-Castillo","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2K21"}],"reference_id":"18611041","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":91,"term_name":"flexible linker","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structure of KCNE1 and implications for how it modulates the KCNQ1 potassium channel. <i> Kang C, Tian C, Sönnichsen FD, Smith JA, Meiler J, George AL, Vanoye CG, Kim HJ, Sanders CR. </i> Biochemistry, 2008","term_id":"IDPO:0000033","curator_id":"mmacossay","start":72,"term_ontology":"IDPO","curator_name":"Mauricio Macossay-Castillo","reference_id":"18611041","version":3,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00796r006","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_P15382","date":"2016-08-20T16:33:18.000Z","acc":"P15382","name":"Potassium voltage-gated channel subfamily E member 1","length":129,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012F141","genes":[{"name":{"value":"KCNE1"}}],"alphafold_very_low_content":0.015503875968992248,"disorder_content":0.5038759689922481,"disprot_consensus":{"full":[{"start":24,"end":45,"type":"D"},{"start":72,"end":91,"type":"D"},{"start":107,"end":129,"type":"D"}],"Structural state":[{"start":24,"end":45,"type":"D"},{"start":72,"end":91,"type":"D"},{"start":107,"end":129,"type":"D"}],"Molecular function":[{"start":107,"end":129,"type":"F"}],"Disorder function":[{"start":24,"end":45,"type":"F"},{"start":72,"end":91,"type":"F"}]}},{"features":{"pfam":[{"id":"PF09470","name":"Telethonin protein","start":4,"end":167}],"gene3D":[{"start":1,"end":84,"id":"2.20.160.10","name":"titin domain like"}]},"uniref50":"UniRef50_O15273","sequence":"MATSELSCEVSEENCERREAFWAEWKDLTLSTRPEEGCSLHEEDTQRHETYHQQGQCQVLVQRSPWLMMRMGILGRGLQEYQLPYQRVLPLPIFTPAKMGATKEEREDTPIQLQELLALETALGGQCVDRQEVAEITKQLPPVVPVSKPGALRRSLSRSMSQEAQRG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O15273","disprot_id":"DP00797","ncbi_taxon_id":9606,"regions_counter":6,"creator":"mmacossay","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":167,"region_id":"DP00797r001","start":91,"ec_id":"ECO:0006220","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"While the N-terminal segment of telethonin in the current complex displays a virtually identical structure when being compared to the previously reported titin/telethonin (1–90) complex (RMSD, 0.826 Å), its C-terminus remained invisible, leading to the assumption that it is unstructured under the conditions used for crystallization.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16713295","version":3,"reference_html":"Evidence for a dimeric assembly of two titin/telethonin complexes induced by the telethonin C-terminus. <i> Pinotsis N, Petoukhov M, Lange S, Svergun D, Zou P, Gautel M, Wilmanns M. </i> J Struct Biol, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","cross_refs":[{"db":"PDB","id":"2F8V"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":167,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Evidence for a dimeric assembly of two titin/telethonin complexes induced by the telethonin C-terminus. <i> Pinotsis N, Petoukhov M, Lange S, Svergun D, Zou P, Gautel M, Wilmanns M. </i> J Struct Biol, 2006","term_id":"GO:0005515","curator_id":"mmacossay","start":91,"term_ontology":"GO","curator_name":"Mauricio Macossay-Castillo","reference_id":"16713295","version":3,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00797r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":167,"region_id":"DP00797r003","start":91,"ec_id":"ECO:0006204","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"From this comparison, we conclude that the C-terminus of telethonin indeed is unstructured in solution, in agreement with the observations in the crystal structure.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16713295","version":3,"reference_html":"Evidence for a dimeric assembly of two titin/telethonin complexes induced by the telethonin C-terminus. <i> Pinotsis N, Petoukhov M, Lange S, Svergun D, Zou P, Gautel M, Wilmanns M. </i> J Struct Biol, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":167,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Evidence for a dimeric assembly of two titin/telethonin complexes induced by the telethonin C-terminus. <i> Pinotsis N, Petoukhov M, Lange S, Svergun D, Zou P, Gautel M, Wilmanns M. </i> J Struct Biol, 2006","term_id":"GO:0005515","curator_id":"mmacossay","start":91,"term_ontology":"GO","curator_name":"Mauricio Macossay-Castillo","reference_id":"16713295","version":3,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00797r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":167,"region_id":"DP00797r005","reference_id":"16713295","start":91,"term_id":"GO:0060090","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Data derived from the crystal structure, the SAXS experiments as well as the in vivo experiments indicate that the presence of the telethonin C-terminus is required to trigger the formation of a dimeric assembly of titin/telethonin complexes.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":4,"reference_html":"Evidence for a dimeric assembly of two titin/telethonin complexes induced by the telethonin C-terminus. <i> Pinotsis N, Petoukhov M, Lange S, Svergun D, Zou P, Gautel M, Wilmanns M. </i> J Struct Biol, 2006","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","term_name":"molecular adaptor activity","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":167,"region_id":"DP00797r006","reference_id":"16713295","start":91,"term_id":"GO:0060090","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Data derived from the crystal structure, the SAXS experiments as well as the in vivo experiments indicate that the presence of the telethonin C-terminus is required to trigger the formation of a dimeric assembly of titin/telethonin complexes.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"x-ray crystallography evidence used in manual assertion","version":4,"reference_html":"Evidence for a dimeric assembly of two titin/telethonin complexes induced by the telethonin C-terminus. <i> Pinotsis N, Petoukhov M, Lange S, Svergun D, Zou P, Gautel M, Wilmanns M. </i> J Struct Biol, 2006","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","term_name":"molecular adaptor activity","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_O15273","date":"2016-08-20T18:18:39.000Z","acc":"O15273","name":"Telethonin","length":167,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000136BAD","genes":[{"name":{"value":"TCAP"}}],"alphafold_very_low_content":0.10778443113772455,"disorder_content":0.46107784431137727,"disprot_consensus":{"full":[{"start":91,"end":167,"type":"D"}],"Structural state":[{"start":91,"end":167,"type":"D"}],"Molecular function":[{"start":91,"end":167,"type":"F"}]}},{"features":{"pfam":[{"id":"PF27710","name":"tRNA (guanine(9)-N(1))-methyltransferase TRM10/TRM10A","start":32,"end":274}],"gene3D":[{"start":84,"end":272,"id":"3.40.1280.30","name":"3.40.1280.30"}]},"uniref50":"UniRef50_O14214","sequence":"MENKDALDIGKDDTNTSEADVSKNETQEQPVLSKSALKRLKRQQEWDAGREKRAEMRREKKRLRKEERKRKIEAGEVVKSQKKRIRLGKVVPSSIRIVLDCAFDDLMNDKEINSLCQQVTRCHSANRTALHPVELFATNFGGRLKTRQDFVLKGQQNNWKRYNPTTKSYLEEFESQKEKLVYLSADSDNTITELDEDKIYIIGAIVDKNRYKNLCQNKASEQGIKTAKLPIDEYIKITDRKILTVNQVFEILSLWLEYRDWEKAFMEVIPKRKGILLKSDESFDVSEDTRSQSNQSDSELEKEN","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"uniref90":"UniRef90_O14214","disprot_id":"DP00798","ncbi_taxon_id":284812,"regions_counter":2,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":304,"region_id":"DP00798r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of tRNA m1G9 methyltransferase Trm10: insight into the catalytic mechanism and recognition of tRNA substrate. <i> Shao Z, Yan W, Peng J, Zuo X, Zou Y, Li F, Gong D, Ma R, Wu J, Shi Y, Zhang Z, Teng M, Li X, Gong Q. </i> Nucleic Acids Res, 2014","term_id":"IDPO:0000002","curator_id":"nmurvai","start":271,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"24081582","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4JWH"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":83,"region_id":"DP00798r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of tRNA m1G9 methyltransferase Trm10: insight into the catalytic mechanism and recognition of tRNA substrate. <i> Shao Z, Yan W, Peng J, Zuo X, Zou Y, Li F, Gong D, Ma R, Wu J, Shi Y, Zhang Z, Teng M, Li X, Gong Q. </i> Nucleic Acids Res, 2014","term_id":"IDPO:0000002","curator_id":"nmurvai","start":1,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"24081582","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4JWH"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_O14214","date":"2016-08-21T20:05:29.000Z","acc":"O14214","name":"tRNA (guanine(9)-N1)-methyltransferase","length":304,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","dataset":[],"UniParc":"UPI000006A3A4","genes":[{"name":{"value":"trm10","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"24081582","url":"http://www.ncbi.nlm.nih.gov/pubmed/24081582","alternativeUrl":"https://europepmc.org/abstract/MED/24081582"}}]},"orfNames":[{"value":"SPAC6B12.09"}]}],"alphafold_very_low_content":0.17434210526315788,"disorder_content":0.3848684210526316,"disprot_consensus":{"full":[{"start":1,"end":83,"type":"D"},{"start":271,"end":304,"type":"D"}],"Structural state":[{"start":1,"end":83,"type":"D"},{"start":271,"end":304,"type":"D"}]}},{"features":{"pfam":[{"id":"PF06013","name":"Proteins of 100 residues with WXG","start":3,"end":87}],"gene3D":[{"start":1,"end":96,"id":"1.10.287.1060","name":"ESAT-6-like"}]},"uniref50":"UniRef50_P0A569","sequence":"MSQIMYNYPAMLGHAGDMAGYAGTLQSLGAEIAVEQAALQSAWQGDTGITYQAWQAQWNQAMEDLVRAYHAMSSTHEANTMAMMARDTAEAAKWGG","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"uniref90":"UniRef90_P0A569","disprot_id":"DP00799","ncbi_taxon_id":83332,"regions_counter":4,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":16,"region_id":"DP00799r001","released":"2025_06","ec_id":"ECO:0006165","reference_html":"Solution structure of the Mycobacterium tuberculosis EsxG·EsxH complex: functional implications and comparisons with other M. tuberculosis Esx family complexes. <i> Ilghari D, Lightbody KL, Veverka V, Waters LC, Muskett FW, Renshaw PS, Carr MD. </i> J Biol Chem, 2011","term_id":"IDPO:0000002","curator_id":"tcordero","start":1,"term_ontology":"IDPO","curator_name":"Trinidad Cordero","reference_id":"21730061","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2025-06-05T09:28:26.508Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2KG7"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0003-4991-7170","statement":[{"text":"The core of the complex is well defined (residues 15–79 in EsxG and 17–75 in EsxH), although there appears to be significant flexibility in the hairpin loop of EsxG (residues 40–47) as well as the N and C termini of EsxG and EsxH, which form flexible arms at both ends of the complex (Fig. 1).","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O53692"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T15:20:32.767Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":96,"region_id":"DP00799r002","released":"2025_06","ec_id":"ECO:0006165","reference_html":"Solution structure of the Mycobacterium tuberculosis EsxG·EsxH complex: functional implications and comparisons with other M. tuberculosis Esx family complexes. <i> Ilghari D, Lightbody KL, Veverka V, Waters LC, Muskett FW, Renshaw PS, Carr MD. </i> J Biol Chem, 2011","term_id":"IDPO:0000002","curator_id":"tcordero","start":76,"term_ontology":"IDPO","curator_name":"Trinidad Cordero","reference_id":"21730061","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2025-06-05T09:29:41.149Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2KG7"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0003-4991-7170","statement":[{"text":"The core of the complex is well defined (residues 15–79 in EsxG and 17–75 in EsxH), although there appears to be significant flexibility in the hairpin loop of EsxG (residues 40–47) as well as the N and C termini of EsxG and EsxH, which form flexible arms at both ends of the complex (Fig. 1).","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O53692"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T15:20:33.558Z"}},{"start":1,"end":16,"reference_id":"21730061","reference_source":"pmid","reference_html":"Solution structure of the Mycobacterium tuberculosis EsxG·EsxH complex: functional implications and comparisons with other M. tuberculosis Esx family complexes. <i> Ilghari D, Lightbody KL, Veverka V, Waters LC, Muskett FW, Renshaw PS, Carr MD. </i> J Biol Chem, 2011","date":"2025-06-04T16:57:34.502Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00799r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O53692"}],"statement":[{"text":"The core of the complex is well defined (residues 15–79 in EsxG and 17–75 in EsxH), although there appears to be significant flexibility in the hairpin loop of EsxG (residues 40–47) as well as the N and C termini of EsxG and EsxH, which form flexible arms at both ends of the complex (Fig. 1). ","type":"Results"}],"cross_refs":[{"db":"PDB","id":"2KG7"}]},{"start":76,"end":96,"reference_id":"21730061","reference_source":"pmid","reference_html":"Solution structure of the Mycobacterium tuberculosis EsxG·EsxH complex: functional implications and comparisons with other M. tuberculosis Esx family complexes. <i> Ilghari D, Lightbody KL, Veverka V, Waters LC, Muskett FW, Renshaw PS, Carr MD. </i> J Biol Chem, 2011","date":"2025-06-04T16:57:08.754Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00799r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O53692"}],"statement":[{"text":"The core of the complex is well defined (residues 15–79 in EsxG and 17–75 in EsxH), although there appears to be significant flexibility in the hairpin loop of EsxG (residues 40–47) as well as the N and C termini of EsxG and EsxH, which form flexible arms at both ends of the complex (Fig. 1). ","type":"Results"}],"cross_refs":[{"db":"PDB","id":"2KG7"}]}],"released":"2025_06","uniref100":"UniRef100_P0A569","date":"2016-08-21T20:26:40.000Z","acc":"P9WNK3","name":"ESAT-6-like protein EsxH","length":96,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","dataset":["Bacterial virulence-related proteins"],"UniParc":"UPI0000036DD4","genes":[{"name":{"value":"esxH","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15336430","url":"http://www.ncbi.nlm.nih.gov/pubmed/15336430","alternativeUrl":"https://europepmc.org/abstract/MED/15336430"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"19876390","url":"http://www.ncbi.nlm.nih.gov/pubmed/19876390","alternativeUrl":"https://europepmc.org/abstract/MED/19876390"}}]},"synonyms":[{"value":"cfp7"}],"orfNames":[{"value":"MTV035.16"}],"olnNames":[{"value":"Rv0288"}]}],"alphafold_very_low_content":0.03125,"disorder_content":0.3854166666666667,"disprot_consensus":{"full":[{"start":1,"end":16,"type":"D"},{"start":76,"end":96,"type":"D"}],"Structural state":[{"start":1,"end":16,"type":"D"},{"start":76,"end":96,"type":"D"}],"Disorder function":[{"start":1,"end":16,"type":"F"},{"start":76,"end":96,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04272","name":"Phospholamban","start":1,"end":52}],"gene3D":[{"start":1,"end":52,"id":"1.20.5.290","name":"Phospholamban"}]},"uniref50":"UniRef50_P26678","sequence":"MDKVQYLTRSAIRRASTIEMPQQARQNLQNLFINFCLILICLLLICIIVMLL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Carnivora","Caniformia","Canidae","Canis"],"uniref90":"UniRef90_P26678","disprot_id":"DP00801","ncbi_taxon_id":9615,"regions_counter":3,"creator":"droche","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":20,"region_id":"DP00801r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The structural basis for phospholamban inhibition of the calcium pump in sarcoplasmic reticulum. <i> Akin BL, Hurley TD, Chen Z, Jones LR. </i> J Biol Chem, 2013","term_id":"IDPO:0000002","curator_id":"droche","start":1,"term_ontology":"IDPO","curator_name":"Daniel Roche","reference_id":"23996003","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4KYT"},{"db":"PDB","id":"KY3U"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":20,"term_name":"phosphorylation display site","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"IDPO","curator_name":"Daniel Roche","reference_id":"23996003","version":2,"reference_html":"The structural basis for phospholamban inhibition of the calcium pump in sarcoplasmic reticulum. <i> Akin BL, Hurley TD, Chen Z, Jones LR. </i> J Biol Chem, 2013","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000045","ec_id":"ECO:0006220","region_id":"DP00801r002","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":20,"term_name":"protein binding","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"GO","curator_name":"Daniel Roche","reference_id":"23996003","version":3,"reference_html":"The structural basis for phospholamban inhibition of the calcium pump in sarcoplasmic reticulum. <i> Akin BL, Hurley TD, Chen Z, Jones LR. </i> J Biol Chem, 2013","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00801r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P61012","date":"2016-08-22T13:17:11.000Z","acc":"P61012","name":"Cardiac phospholamban","length":52,"organism":"Canis lupus familiaris","dataset":[],"UniParc":"UPI0000034315","genes":[{"name":{"value":"PLN"}}],"alphafold_very_low_content":0,"disorder_content":0.38461538461538464,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"D"}],"Structural state":[{"start":1,"end":20,"type":"D"}],"Disorder function":[{"start":1,"end":20,"type":"F"}],"Molecular function":[{"start":1,"end":20,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03244","name":"Photosystem I reaction centre subunit VI","start":7,"end":144}],"gene3D":[{"start":59,"end":127,"id":"1.20.5.220","name":"1.20.5.220"}]},"uniref50":"UniRef50_Q9SUI7","sequence":"MASLATLAAVQPTTLKGLAGSSIAGTKLHIKPARQSFKLNNVRSGAIVAKYGDKSVYFDLEDIANTTGQWDVYGSDAPSPYNSLQSKFFETFAAPFTKRGLLLKFLILGGGSLLTYVSANAPQDVLPITRGPQQPPKLGPRGKI","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","Caryophyllales","Chenopodiaceae","Chenopodioideae","Anserineae","Spinacia"],"uniref90":"UniRef90_P22179","disprot_id":"DP00803","ncbi_taxon_id":3562,"regions_counter":3,"creator":"droche","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":58,"region_id":"DP00803r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure determination and improved model of plant photosystem I. <i> Amunts A, Toporik H, Borovikova A, Nelson N. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"droche","start":1,"term_ontology":"IDPO","curator_name":"Daniel Roche","reference_id":"19923216","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2WSC"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":58,"term_name":"molecular adaptor activity","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"GO","curator_name":"Daniel Roche","reference_id":"19923216","version":3,"reference_html":"Structure determination and improved model of plant photosystem I. <i> Amunts A, Toporik H, Borovikova A, Nelson N. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006220","region_id":"DP00803r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":58,"term_name":"protein binding","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"GO","curator_name":"Daniel Roche","reference_id":"19923216","version":3,"reference_html":"Structure determination and improved model of plant photosystem I. <i> Amunts A, Toporik H, Borovikova A, Nelson N. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00803r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P22179","date":"2016-08-22T15:33:44.000Z","acc":"P22179","name":"Photosystem I reaction center subunit VI, chloroplastic","length":144,"organism":"Spinacia oleracea","dataset":[],"UniParc":"UPI000013252D","genes":[{"name":{"value":"PSAH"}}],"alphafold_very_low_content":0.09027777777777778,"disorder_content":0.4027777777777778,"disprot_consensus":{"full":[{"start":1,"end":58,"type":"D"}],"Structural state":[{"start":1,"end":58,"type":"D"}],"Molecular function":[{"start":1,"end":58,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00213","name":"ATP synthase delta (OSCP) subunit","start":13,"end":184}],"gene3D":[{"start":13,"end":106,"id":"1.10.520.20","name":"N-terminal domain of the delta subunit of the F1F0-ATP synthase"}]},"uniref50":"UniRef50_P72244","sequence":"MTVANSASISADIAGRYAQALFDLVRDSGGIDALSSQIDDLASAYDASQDLRDLTLSPLYDRQQQEAAVGALSERMGLSAELANTLRLLARNRRLFTLPQFVAKLRNLIADAKGEVTADVVSAQALTDEQKARLADTLAAKSGKTVKLNARVDESLIGGMIVKLGSQMIDSSIRSKLASLQNAMKEVG","taxonomy":["Bacteria","Proteobacteria","Alphaproteobacteria","Rhodobacterales","Rhodobacteraceae","Paracoccus"],"uniref90":"UniRef90_A1B8N7","disprot_id":"DP00806","ncbi_taxon_id":318586,"regions_counter":1,"creator":"droche","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":188,"region_id":"DP00806r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution. <i> Morales-Rios E, Montgomery MG, Leslie AG, Walker JE. </i> Proc Natl Acad Sci U S A, 2015","term_id":"IDPO:0000002","curator_id":"droche","start":116,"term_ontology":"IDPO","curator_name":"Daniel Roche","reference_id":"26460036","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5DN6"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_A1B8N7","date":"2016-08-22T16:09:37.000Z","acc":"A1B8N7","name":"ATP synthase subunit delta","length":188,"organism":"Paracoccus denitrificans (strain Pd 1222)","dataset":[],"UniParc":"UPI00019B22E8","genes":[{"name":{"value":"atpH","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01416","url":"https://hamap.expasy.org/unirule/MF_01416"}}]},"olnNames":[{"value":"Pden_3815"}]}],"alphafold_very_low_content":0.010638297872340425,"disorder_content":0.3882978723404255,"disprot_consensus":{"full":[{"start":116,"end":188,"type":"D"}],"Structural state":[{"start":116,"end":188,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00304","name":"Gamma-thionin family","start":28,"end":77}],"gene3D":[{"start":25,"end":77,"id":"3.30.30.10","name":"Knottin, scorpion toxin-like"}]},"uniref50":"UniRef50_Q84ZX5","sequence":"MAKCSYVFCAVLLIFIVAIGEMEAAGSKLCEKTSKTYSGKCDNKKCDKKCIEWEKAQHGACHKREAGKESCFCYFDCSKSPPGATPAPPGAAPPPAAGGSPSPPADGGSPPPPADGGSPPVDGGSPPPPSTH","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","campanulids","Asterales","Asteraceae","Asteroideae","Anthemideae","Artemisiinae","Artemisia"],"uniref90":"UniRef90_Q84ZX5","disprot_id":"DP00807","ncbi_taxon_id":4220,"regions_counter":3,"creator":"droche","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":132,"region_id":"DP00807r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Mapping the interactions between a major pollen allergen and human IgE antibodies. <i> Razzera G, Gadermaier G, de Paula V, Almeida MS, Egger M, Jahn-Schmid B, Almeida FC, Ferreira F, Valente AP. </i> Structure, 2010","term_id":"IDPO:0000002","curator_id":"droche","start":81,"term_ontology":"IDPO","curator_name":"Daniel Roche","reference_id":"20696401","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2KPY"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":132,"term_name":"molecular function activator activity","start":81,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"GO","curator_name":"Daniel Roche","reference_id":"20696401","version":3,"reference_html":"Mapping the interactions between a major pollen allergen and human IgE antibodies. <i> Razzera G, Gadermaier G, de Paula V, Almeida MS, Egger M, Jahn-Schmid B, Almeida FC, Ferreira F, Valente AP. </i> Structure, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140677","ec_id":"ECO:0006165","region_id":"DP00807r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":132,"term_name":"protein binding","start":81,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"GO","curator_name":"Daniel Roche","reference_id":"20696401","version":3,"reference_html":"Mapping the interactions between a major pollen allergen and human IgE antibodies. <i> Razzera G, Gadermaier G, de Paula V, Almeida MS, Egger M, Jahn-Schmid B, Almeida FC, Ferreira F, Valente AP. </i> Structure, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00807r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q84ZX5","date":"2016-08-22T16:19:40.000Z","acc":"Q84ZX5","name":"Major pollen allergen Art v 1","length":132,"organism":"Artemisia vulgaris","dataset":[],"UniParc":"UPI0000003738","genes":[],"alphafold_very_low_content":0.16666666666666666,"disorder_content":0.3939393939393939,"disprot_consensus":{"full":[{"start":81,"end":132,"type":"D"}],"Structural state":[{"start":81,"end":132,"type":"D"}],"Molecular function":[{"start":81,"end":132,"type":"F"}]}},{"acc":"P24937","sequence":"MEDINFASLAPRHGSRPFMGNWQDIGTSNMSGGAFSWGSLWSGIKNFGSTVKNYGSKAWNSSTGQMLRDKLKEQNFQQKVVDGLASGISGVVDLANQAVQNKINSKLDPRPPVEEPPPAVETVSPEGRGEKRPRPDREETLVTQIDEPPSYEEALKQGLPTTRPIAPMATGVLGQHTPVTLDLPPPADTQQKPVLPGPTAVVVTRPSRASLRRAASGPRSLRPVASGNWQSTLNSIVGLGVQSLKRRRCF","creator":"jbergier","dataset":["Viral proteins"],"date":"2016-08-22T16:27:38.000Z","disprot_id":"DP00808","features":{"pfam":[{"id":"PF02993","name":"Minor capsid protein VI","start":6,"end":250}]},"genes":[{"name":{"value":"L3","evidences":[{"source":{"id":"MF_04048","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04048","_id":"685af523b4ac24d5329d85cb"},"code":"ECO:0000255","_id":"685af523b4ac24d5329d85ca"}],"_id":"685af523b4ac24d5329d85cc"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d85c9"}],"length":250,"name":"Pre-protein VI","ncbi_taxon_id":28285,"organism":"Human adenovirus C serotype 5","regions_counter":17,"released":"2016_10","taxonomy":["Viruses","Varidnaviria","Bamfordvirae","Preplasmiviricota","Tectiliviricetes","Rowavirales","Adenoviridae","Mastadenovirus"],"UniParc":"UPI0000131B3C","uniref100":"UniRef100_P24937","uniref50":"UniRef50_P24937","uniref90":"UniRef90_P24937","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":158,"end":239,"interaction_partner":[],"reference_html":"Structures and organization of adenovirus cement proteins provide insights into the role of capsid maturation in virus entry and infection. <i> Reddy VS, Nemerow GR. </i> Proc Natl Acad Sci U S A, 2014","reference_id":"25071205","region_id":"DP00808r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"One copy of protein VI is found intimately associated with the base of each PPH on the capsid interior. We were able to resolve residues 6–31, 34–79, and 87–157 of protein VI, which interact primarily with the bases of PPHs; the remaining C-terminal residues (158–239) were disordered.","_id":"685af523b4ac24d5329d8598"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:08:21.515Z","_id":"685af523b4ac24d5329d8599"},"version":1,"_id":"685af523b4ac24d5329d8597","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6CGV","_id":"685af523b4ac24d5329d859d"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":25,"end":250,"interaction_partner":[],"reference_html":"Revised Crystal Structure of Human Adenovirus Reveals the Limits on Protein IX Quasi-Equivalence and on Analyzing Large Macromolecular Complexes. <i> Kundhavai Natchiar S, Venkataraman S, Mullen TM, Nemerow GR, Reddy VS. </i> J Mol Biol, 2018","reference_id":"30121295","region_id":"DP00808r007","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":" A segment of N-terminal pro-peptide of VI is found in the interior cavities of peripentonal hexons, and the rest of VI is disordered.","_id":"685af523b4ac24d5329d859b"},{"type":"Curator statement","text":"From Table 2, 1–24 corresponds to the ordered region of VI and 25–250 corresponds to the disordered region of VI.","_id":"685af523b4ac24d5329d859c"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:08:20.466Z","_id":"685af523b4ac24d5329d859e"},"version":1,"_id":"685af523b4ac24d5329d859a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6B1T","_id":"685af523b4ac24d5329d85a0"},{"db":"EMDB","id":"7034","_id":"685af523b4ac24d5329d85a1"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":240,"end":250,"interaction_partner":[],"reference_html":"Atomic Structures of Minor Proteins VI and VII in Human Adenovirus. <i> Dai X, Wu L, Sun R, Zhou ZH. </i> J Virol, 2017","reference_id":"28978703","region_id":"DP00808r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The protein VI density we modeled is only a small fraction of the full-length mature protein VI (aa 109 to 143 versus aa 34 to 239 as numbered in pVI), suggesting that both its N- and C-terminal regions are flexible. ","_id":"685af523b4ac24d5329d85a2"},{"type":"Curator statement","text":"The PDB show this bondaries disordered (240-250)","_id":"685af523b4ac24d5329d85a3"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:08:19.759Z","_id":"685af523b4ac24d5329d85a4"},"version":1,"_id":"685af523b4ac24d5329d859f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007040","ec_name":"plaque assay evidence used in manual assertion","ec_ontology":"ECO","start":25,"end":250,"interaction_partner":[],"reference_html":"Disulfide-bond formation by a single cysteine mutation in adenovirus protein VI impairs capsid release and membrane lysis. <i> Moyer CL, Nemerow GR. </i> Virology, 2012","reference_id":"22516138","region_id":"DP00808r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"We used the data from this experiment to calculate ID50 values for each virus and found that the G48C mutant required ∼3-fold higher p/c than wild type AdV to achieve the same level of infection. The decrease in infectivity for the G48C mutant was not as drastic as that of the AdV VI-L40Q virus, which was 12-fold reduced compared to wild type virus. Nonetheless, the phenotype of the G48C mutation is distinct from that of L40Q, as described below.","_id":"685af523b4ac24d5329d85ac"},{"type":"Results","text":"We further assayed infectivity of the G48C mutant in an AdV plaque assay that measures viral replication, and show that the mutant generated ∼3-fold less plaques than wild type AdV at 0.5 p/c (Fig. 2B), in good agreement with the data from the single-round infection (Fig. 2A). The L40Q virus was also reduced ∼13-fold in this assay. Taken together, the results of these assays clearly indicate that the AdV VI-G48C mutant impairs virus infectivity.","_id":"685af523b4ac24d5329d85ad"}],"states_connection":[],"term_comment":"","term_def":"\"A set of processes which all viruses follow to ensure survival; includes attachment and entry of the virus particle, decoding of genome information, translation of viral mRNA by host ribosomes, genome replication, and assembly and release of viral particles containing the genome.\" [ISBN:1555811272]","term_go_domain":"P","term_id":"GO:0019058","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral life cycle","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:45:12.092Z","_id":"685af523b4ac24d5329d85ae"},"version":1,"_id":"685af523b4ac24d5329d85ab","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":25,"end":250,"interaction_partner":[],"reference_html":"Disulfide-bond formation by a single cysteine mutation in adenovirus protein VI impairs capsid release and membrane lysis. <i> Moyer CL, Nemerow GR. </i> Virology, 2012","reference_id":"22516138","region_id":"DP00808r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Given the inherent decrease in membrane lytic activity of the disulfide bonded protein VI molecules, we next asked whether reduction of the disulfide bonds could restore membrane lytic activity to the G48C protein.","_id":"685af523b4ac24d5329d85b0"},{"type":"Results","text":"This small increase in membrane lytic activity was consistently observed in three independent experiments. Therefore, we conclude that disulfide bond formation not only restricts release of the membrane lytic protein from the viral capsid, but also impairs proper interaction with the host membrane that allows subsequent membrane lytic activity.","_id":"685af523b4ac24d5329d85b1"}],"states_connection":[],"term_comment":"","term_def":"\"The dissemination of mature viral particles from the host cell, e.g. by cell lysis or the budding of virus particles from the cell membrane.\" [GOC:jl]","term_go_domain":"P","term_id":"GO:0019076","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral release from host cell","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:45:01.756Z","_id":"685af523b4ac24d5329d85b2"},"version":1,"_id":"685af523b4ac24d5329d85af","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007040","ec_name":"plaque assay evidence used in manual assertion","ec_ontology":"ECO","start":147,"end":151,"interaction_partner":[],"reference_html":"A capsid-encoded PPxY-motif facilitates adenovirus entry. <i> Wodrich H, Henaff D, Jammart B, Segura-Morales C, Seelmeir S, Coux O, Ruzsics Z, Wiethoff CM, Kremer EJ. </i> PLoS Pathog, 2010","reference_id":"20333243","region_id":"DP00808r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"To identify possible trafficking determinants, we analyzed the sequences of protein VI from several Ad serotypes and identified a highly conserved ubiquitin-ligase interacting motif present in PPxY-type viral late domains (PPxY, Figure S2). To examine the role of this PPxY motif in Ad cell entry, we used an E1/E3-deleted Ad5 that had the protein VI PPSY motif mutated to PGAA (Ad5-VI-M1, detailed in Figure S3) [33],[34].","_id":"685af523b4ac24d5329d85b4"},{"type":"Results","text":"Plaques were significantly smaller for Ad5-VI-M1 versus Ad5-VI-wt (see below), suggesting that the altered PPxY domain affects some stages of virus propagation.","_id":"685af523b4ac24d5329d85b5"}],"states_connection":[],"term_comment":"","term_def":"\"A set of processes which all viruses follow to ensure survival; includes attachment and entry of the virus particle, decoding of genome information, translation of viral mRNA by host ribosomes, genome replication, and assembly and release of viral particles containing the genome.\" [ISBN:1555811272]","term_go_domain":"P","term_id":"GO:0019058","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral life cycle","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:35:23.546Z","_id":"685af523b4ac24d5329d85b6"},"version":1,"_id":"685af523b4ac24d5329d85b3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006323","ec_name":"fluorescence microscopy evidence used in manual assertion","ec_ontology":"ECO","start":147,"end":151,"interaction_partner":[],"reference_html":"Disulfide-bond formation by a single cysteine mutation in adenovirus protein VI impairs capsid release and membrane lysis. <i> Moyer CL, Nemerow GR. </i> Virology, 2012","reference_id":"22516138","region_id":"DP00808r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"To identify possible trafficking determinants, we analyzed the sequences of protein VI from several Ad serotypes and identified a highly conserved ubiquitin-ligase interacting motif present in PPxY-type viral late domains (PPxY, Figure S2). To examine the role of this PPxY motif in Ad cell entry, we used an E1/E3-deleted Ad5 that had the protein VI PPSY motif mutated to PGAA (Ad5-VI-M1, detailed in Figure S3) [33],[34].","_id":"685af523b4ac24d5329d85b8"},{"type":"Results","text":"To determine whether the M1 mutation influences Ad cell entry, we performed a fluorescent focus forming assay and stained cells at 8, 12 and 24 h post-infection for expression of the E2A protein, which marks the appearance of viral replication centers (Figure 2D and data not shown). Compared to Ad5-VI-wt, the Ad5-VI-M1 virus produced approximately 20-fold fewer fluorescent foci when equivalent numbers of viral particles were used for infections. This suggested that steps prior to replication (i.e. internalization) require an intact PPxY motif in protein VI.","_id":"685af523b4ac24d5329d85b9"}],"states_connection":[],"term_comment":"","term_def":"\"A set of processes which all viruses follow to ensure survival; includes attachment and entry of the virus particle, decoding of genome information, translation of viral mRNA by host ribosomes, genome replication, and assembly and release of viral particles containing the genome.\" [ISBN:1555811272]","term_go_domain":"P","term_id":"GO:0019058","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral life cycle","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:34:12.842Z","_id":"685af523b4ac24d5329d85ba"},"version":1,"_id":"685af523b4ac24d5329d85b7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IEP","ec_id":"ECO:0005636","ec_name":"green fluorescent protein reporter gene assay evidence used in manual assertion","ec_ontology":"ECO","start":147,"end":151,"interaction_partner":[],"reference_html":"Disulfide-bond formation by a single cysteine mutation in adenovirus protein VI impairs capsid release and membrane lysis. <i> Moyer CL, Nemerow GR. </i> Virology, 2012","reference_id":"22516138","region_id":"DP00808r014","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"To identify possible trafficking determinants, we analyzed the sequences of protein VI from several Ad serotypes and identified a highly conserved ubiquitin-ligase interacting motif present in PPxY-type viral late domains (PPxY, Figure S2). To examine the role of this PPxY motif in Ad cell entry, we used an E1/E3-deleted Ad5 that had the protein VI PPSY motif mutated to PGAA (Ad5-VI-M1, detailed in Figure S3) [33],[34].","_id":"685af523b4ac24d5329d85bc"},{"type":"Results","text":"We repeated plaque forming assays (Figure 2E) and single round infection assays (Figure 2F), this time using GFP expression as the quantification method in non-complementing U2OS cells. We observed a reduction in infectivity in the same order of magnitude as previously (compare Figures 2C with 2E and 2D with 2F). In addition the GFP expression allowed us to follow the plaque formation over time. As shown in Figure S4 the spread of the M1 mutant virus was significantly slower and led to fewer and much smaller plaques (Figure 2E and Figure S4).","_id":"685af523b4ac24d5329d85bd"}],"states_connection":[],"term_comment":"","term_def":"\"A set of processes which all viruses follow to ensure survival; includes attachment and entry of the virus particle, decoding of genome information, translation of viral mRNA by host ribosomes, genome replication, and assembly and release of viral particles containing the genome.\" [ISBN:1555811272]","term_go_domain":"P","term_id":"GO:0019058","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral life cycle","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:33:50.333Z","_id":"685af523b4ac24d5329d85be"},"version":1,"_id":"685af523b4ac24d5329d85bb","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007726","ec_name":"fusion protein localization evidence used in manual assertion","ec_ontology":"ECO","start":147,"end":151,"interaction_partner":[],"reference_html":"A capsid-encoded PPxY-motif facilitates adenovirus entry. <i> Wodrich H, Henaff D, Jammart B, Segura-Morales C, Seelmeir S, Coux O, Ruzsics Z, Wiethoff CM, Kremer EJ. </i> PLoS Pathog, 2010","reference_id":"20333243","region_id":"DP00808r015","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"To identify possible trafficking determinants, we analyzed the sequences of protein VI from several Ad serotypes and identified a highly conserved ubiquitin-ligase interacting motif present in PPxY-type viral late domains (PPxY, Figure S2). To examine the role of this PPxY motif in Ad cell entry, we used an E1/E3-deleted Ad5 that had the protein VI PPSY motif mutated to PGAA (Ad5-VI-M1, detailed in Figure S3) [33],[34].","_id":"685af523b4ac24d5329d85c0"},{"type":"Results","text":"Together these data suggested that protein VI is a highly mobile protein that moves along microtubules, presumably in association with vesicular structures whose motion depends on the PPxY motif.","_id":"685af523b4ac24d5329d85c1"}],"states_connection":[],"term_comment":"","term_def":"\"The directed movement of a protein along a microtubule, mediated by motor proteins.\" [PMID:25987607]","term_go_domain":"P","term_id":"GO:0098840","term_is_binding":false,"term_is_obsolete":false,"term_name":"protein transport along microtubule","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:33:37.267Z","_id":"685af523b4ac24d5329d85c2"},"version":1,"_id":"685af523b4ac24d5329d85bf","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IEP","ec_id":"ECO:0000279","ec_name":"qualitative western immunoblotting evidence used in manual assertion","ec_ontology":"ECO","start":147,"end":151,"interaction_partner":[],"reference_html":"Disulfide-bond formation by a single cysteine mutation in adenovirus protein VI impairs capsid release and membrane lysis. <i> Moyer CL, Nemerow GR. </i> Virology, 2012","reference_id":"22516138","region_id":"DP00808r016","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"To address the role of the PPxY motif in protein VI ubiquitylation, we repeated the in vitro ubiquitylation assay using wt or M1 mutant protein VI purified from E. coli followed by western blot analysis. We detected protein VI-reactive bands, consistent with protein VI modified with two to three ubiquitin (Figure 6B, lane 2). In contrast, no modification was observed when the PPxY motif was mutated (Figure 6B, lane 1) or in the absence of ATP (Figure 6B, lane 3 and 4).","_id":"685af523b4ac24d5329d85c4"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000046","term_name":"ubiquitination display site","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:33:11.671Z","_id":"685af523b4ac24d5329d85c5"},"version":1,"_id":"685af523b4ac24d5329d85c3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007106","ec_name":"green fluorescent protein fusion protein localization evidence used in manual assertion","ec_ontology":"ECO","start":147,"end":151,"interaction_partner":[],"reference_html":"Disulfide-bond formation by a single cysteine mutation in adenovirus protein VI impairs capsid release and membrane lysis. <i> Moyer CL, Nemerow GR. </i> Virology, 2012","reference_id":"22516138","region_id":"DP00808r017","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Two ligases, Nedd4.1 and Nedd4.2, were highly enriched on VI-wt beads while none of the other ligases showed strong binding to VI-wt- or to VI-M1-beads (Figure 7B). Taken together, these data suggest a preferential interaction between Nedd4.1 and Nedd4.2 and the PPxY motif in protein VI, which leads to relocalization of the ligases from the cytoplasm to a membrane compartment.","_id":"685af523b4ac24d5329d85c7"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:33:03.989Z","_id":"685af523b4ac24d5329d85c8"},"version":1,"_id":"685af523b4ac24d5329d85c6","reference_source":"pmid"}],"__v":0,"disorder_content":0.904,"disprot_consensus":{"full":[{"start":25,"end":250,"type":"D"}],"Structural state":[{"start":25,"end":250,"type":"D"}],"Biological process":[{"start":25,"end":250,"type":"F"}],"Disorder function":[{"start":147,"end":151,"type":"F"}],"Molecular function":[{"start":147,"end":151,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00575","name":"S1 RNA binding domain","start":4,"end":77}],"gene3D":[{"start":2,"end":88,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}]},"uniref50":"UniRef50_P80870","sequence":"MAAKFEVGSVYTGKVTGLQAYGAFVALDEETQGLVHISEVTHGFVKDINEHLSVGDEVQVKVLAVDEEKGKISLSIRATQAAPEKKESKPRKPKAAQVSEEASTPQGFNTLKDKLEEWIEMSNRKDLIKK","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Bacillus"],"uniref90":"UniRef90_P80870","disprot_id":"DP00809","ncbi_taxon_id":224308,"regions_counter":1,"creator":"droche","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":130,"region_id":"DP00809r001","released":"2025_12","ec_id":"ECO:0006165","reference_html":"Solution structure of GSP13 from Bacillus subtilis exhibits an S1 domain related to cold shock proteins. <i> Yu W, Hu J, Yu B, Xia W, Jin C, Xia B. </i> J Biomol NMR, 2009","term_id":"IDPO:0000002","curator_id":"vnugnes","start":81,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19152054","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2025-10-16T14:04:29.814Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2K4K"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The structure of GSP13 mainly consists of a typical S1 domain along with a C-terminal 50-residue flexible tail, different from the other known S1 domain containing proteins.","type":"Abstract"}]}],"released":"2016_10","uniref100":"UniRef100_P80870","date":"2016-08-22T16:37:32.000Z","acc":"P80870","name":"General stress protein 13","length":130,"organism":"Bacillus subtilis (strain 168)","dataset":["Stress response proteins"],"UniParc":"UPI0000060995","genes":[{"name":{"value":"yugI"},"olnNames":[{"value":"BSU31390"}]}],"alphafold_very_low_content":0.2153846153846154,"disorder_content":0.38461538461538464,"disprot_consensus":{"full":[{"start":81,"end":130,"type":"D"}],"Structural state":[{"start":81,"end":130,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01371","name":"Trp repressor protein","start":17,"end":103}],"gene3D":[{"start":8,"end":108,"id":"1.10.1270.10","name":"TrpR-like"}]},"uniref50":"UniRef50_A7MIH6","sequence":"MAQQSPYSAAMAEQRHQEWLRFVDLLKNAYQNDLHLPLLNLMLTPDEREALGTRVRIVEELLRGEMSQRELKNELGAGIATITRGSNSLKAAPVELRQWLEEVLLKSD","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_A7ZVT5","disprot_id":"DP00810","ncbi_taxon_id":83334,"regions_counter":4,"creator":"droche","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":92,"region_id":"DP00810r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Three-dimensional solution NMR structure of Apo-L75F-TrpR, a temperature-sensitive mutant of the tryptophan repressor protein. <i> Tyler R, Pelczer I, Carey J, Copié V. </i> Biochemistry, 2002","term_id":"IDPO:0000002","curator_id":"droche","start":63,"term_ontology":"IDPO","curator_name":"Daniel Roche","reference_id":"12356295","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2XDI"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":92,"term_name":"nucleic acid binding","start":63,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"GO","curator_name":"Daniel Roche","reference_id":"12356295","version":3,"reference_html":"Three-dimensional solution NMR structure of Apo-L75F-TrpR, a temperature-sensitive mutant of the tryptophan repressor protein. <i> Tyler R, Pelczer I, Carey J, Copié V. </i> Biochemistry, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006165","region_id":"DP00810r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":16,"region_id":"DP00810r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Three-dimensional solution NMR structure of Apo-L75F-TrpR, a temperature-sensitive mutant of the tryptophan repressor protein. <i> Tyler R, Pelczer I, Carey J, Copié V. </i> Biochemistry, 2002","term_id":"IDPO:0000002","curator_id":"droche","start":2,"term_ontology":"IDPO","curator_name":"Daniel Roche","reference_id":"12356295","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2XDI"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":16,"term_name":"nucleic acid binding","start":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"GO","curator_name":"Daniel Roche","reference_id":"12356295","version":3,"reference_html":"Three-dimensional solution NMR structure of Apo-L75F-TrpR, a temperature-sensitive mutant of the tryptophan repressor protein. <i> Tyler R, Pelczer I, Carey J, Copié V. </i> Biochemistry, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006165","region_id":"DP00810r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_A7ZVT5","date":"2016-08-22T16:45:33.000Z","acc":"P0A882","name":"Trp operon repressor","length":108,"organism":"Escherichia coli O157:H7","dataset":[],"UniParc":"UPI0000112F09","genes":[{"name":{"value":"trpR"},"olnNames":[{"value":"Z5995"},{"value":"ECs5351"}]}],"alphafold_very_low_content":0.027777777777777776,"disorder_content":0.4166666666666667,"disprot_consensus":{"full":[{"start":2,"end":16,"type":"D"},{"start":63,"end":92,"type":"D"}],"Structural state":[{"start":2,"end":16,"type":"D"},{"start":63,"end":92,"type":"D"}],"Molecular function":[{"start":2,"end":16,"type":"F"},{"start":63,"end":92,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00808","name":"Histone-like transcription factor (CBF/NF-Y) and archaeal histone","start":19,"end":83}],"gene3D":[{"start":5,"end":98,"id":"1.10.20.10","name":"Histone, subunit A"}]},"uniref50":"UniRef50_Q9V452","sequence":"MGEPRSQPPVERPPTAETFLPLSRVRTIMKSSMDTGLITNEVLFLMTKCTELFVRHLAGAAYTEEFGQRPGEALKYEHLSQVVNKNKNLEFLLQIVPQKIRVHQFQEMLRLNRSAGSDDDDDDDDDDDEEESESESESDE","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_Q9V452","disprot_id":"DP00811","ncbi_taxon_id":7227,"regions_counter":6,"creator":"droche","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":28,"region_id":"DP00811r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The histone fold subunits of Drosophila CHRAC facilitate nucleosome sliding through dynamic DNA interactions. <i> Hartlepp KF, Fernández-Tornero C, Eberharter A, Grüne T, Müller CW, Becker PB. </i> Mol Cell Biol, 2005","term_id":"IDPO:0000002","curator_id":"droche","start":1,"term_ontology":"IDPO","curator_name":"Daniel Roche","reference_id":"16260604","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":28,"term_name":"molecular adaptor activity","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"GO","curator_name":"Daniel Roche","reference_id":"16260604","version":3,"reference_html":"The histone fold subunits of Drosophila CHRAC facilitate nucleosome sliding through dynamic DNA interactions. <i> Hartlepp KF, Fernández-Tornero C, Eberharter A, Grüne T, Müller CW, Becker PB. </i> Mol Cell Biol, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006220","region_id":"DP00811r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":28,"term_name":"nucleic acid binding","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"GO","curator_name":"Daniel Roche","reference_id":"16260604","version":3,"reference_html":"The histone fold subunits of Drosophila CHRAC facilitate nucleosome sliding through dynamic DNA interactions. <i> Hartlepp KF, Fernández-Tornero C, Eberharter A, Grüne T, Müller CW, Becker PB. </i> Mol Cell Biol, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006220","region_id":"DP00811r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":140,"region_id":"DP00811r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The histone fold subunits of Drosophila CHRAC facilitate nucleosome sliding through dynamic DNA interactions. <i> Hartlepp KF, Fernández-Tornero C, Eberharter A, Grüne T, Müller CW, Becker PB. </i> Mol Cell Biol, 2005","term_id":"IDPO:0000002","curator_id":"droche","start":101,"term_ontology":"IDPO","curator_name":"Daniel Roche","reference_id":"16260604","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":140,"term_name":"molecular adaptor activity","start":101,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"GO","curator_name":"Daniel Roche","reference_id":"16260604","version":3,"reference_html":"The histone fold subunits of Drosophila CHRAC facilitate nucleosome sliding through dynamic DNA interactions. <i> Hartlepp KF, Fernández-Tornero C, Eberharter A, Grüne T, Müller CW, Becker PB. </i> Mol Cell Biol, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006220","region_id":"DP00811r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":140,"term_name":"nucleic acid binding","start":101,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"droche","released":"2022_03","term_ontology":"GO","curator_name":"Daniel Roche","reference_id":"16260604","version":3,"reference_html":"The histone fold subunits of Drosophila CHRAC facilitate nucleosome sliding through dynamic DNA interactions. <i> Hartlepp KF, Fernández-Tornero C, Eberharter A, Grüne T, Müller CW, Becker PB. </i> Mol Cell Biol, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006220","region_id":"DP00811r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q9V452","date":"2016-08-22T16:59:09.000Z","acc":"Q9V452","name":"Chromatin accessibility complex 16kD protein, isoform A","length":140,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI000007BB7D","genes":[{"name":{"value":"Chrac-16","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10856248","url":"http://www.ncbi.nlm.nih.gov/pubmed/10856248","alternativeUrl":"https://europepmc.org/abstract/MED/10856248"}},{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0043001","url":"http://flybase.org/reports/FBgn0043001.html"}}]},"synonyms":[{"value":"CHRAC","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0043001","url":"http://flybase.org/reports/FBgn0043001.html"}}]},{"value":"CHRAC16","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16260604","url":"http://www.ncbi.nlm.nih.gov/pubmed/16260604","alternativeUrl":"https://europepmc.org/abstract/MED/16260604"}},{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0043001","url":"http://flybase.org/reports/FBgn0043001.html"}}]},{"value":"joey","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0043001","url":"http://flybase.org/reports/FBgn0043001.html"}}]}],"orfNames":[{"value":"CG15736","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0043001","url":"http://flybase.org/reports/FBgn0043001.html"}}]}]}],"alphafold_very_low_content":0.02142857142857143,"disorder_content":0.4857142857142857,"disprot_consensus":{"full":[{"start":1,"end":28,"type":"D"},{"start":101,"end":140,"type":"D"}],"Structural state":[{"start":1,"end":28,"type":"D"},{"start":101,"end":140,"type":"D"}],"Molecular function":[{"start":1,"end":28,"type":"F"},{"start":101,"end":140,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03247","name":"Prothymosin/parathymosin family","start":2,"end":106}]},"uniref50":"UniRef50_P01252","sequence":"MSDAAVDTSSEITTKDLKEKKEVVEEAENGREAPANGNANEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAEAATGKRAAEDDEDDDVDTKKQKTDEDD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P01252","disprot_id":"DP00814","ncbi_taxon_id":9913,"regions_counter":5,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":110,"region_id":"DP00814r001","released":"2022_03","ec_id":"ECO:0007064","reference_html":"Prothymosin alpha: a biologically active protein with random coil conformation. <i> Gast K, Damaschun H, Eckert K, Schulze-Forster K, Maurer HR, Müller-Frohne M, Zirwer D, Czarnecki J, Damaschun G. </i> Biochemistry, 1995","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"7548085","version":3,"ec_name":"dynamic light scattering assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Measurements of the excess scattered intensity of protein solutions at finite concentrations yield apparent molar masses, Mapp. The molar mass can be estimated by a linear extrapolation to 0 protein concentration according to 1/Mapp=1/m + 2bC, where B is the second virial coefficient. The corresponding data for ProTα in PBS, pH 7.4, are shown in Figure 2. A linear least-squares fit yields M = (11700 ± 1200)g/mol and a second virial coefficient B=(2.84 ± 0.30)x10-3mol cm3/ g2. ","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":110,"region_id":"DP00814r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Prothymosin alpha: a biologically active protein with random coil conformation. <i> Gast K, Damaschun H, Eckert K, Schulze-Forster K, Maurer HR, Müller-Frohne M, Zirwer D, Czarnecki J, Damaschun G. </i> Biochemistry, 1995","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"7548085","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Prothymosin alpha: a biologically active protein with random coil conformation","type":"Abstract"},{"text":"Our results unequivocally demonstrate that prothymosin is a monomer under physiological conditions. The protein adopts a random coillike conformation but exhibits persistence of direction and curvature. No regular secondary structure is detectable by CD.","type":"Abstract"},{"text":"The CD spectrum of ProTα in PBS, pH7.4, is shown in Figure 1. It has a pattern typical of a protein lacking regular secondary structure as it is observed usually in solutions containing high concentrations of guanidinium chloride or urea.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":110,"region_id":"DP00814r003","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Prothymosin alpha: a biologically active protein with random coil conformation. <i> Gast K, Damaschun H, Eckert K, Schulze-Forster K, Maurer HR, Müller-Frohne M, Zirwer D, Czarnecki J, Damaschun G. </i> Biochemistry, 1995","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"7548085","version":3,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Furthermore, the scattering curve is shown in the form of a Kratky plot (Figure 5). This scattering curve exhibits the characteristics typical of random coil molecules with persistence of direction and persistence of curvature (Kirste & Oberthiir,1982).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":110,"reference_id":"7548085","reference_source":"pmid","reference_html":"Prothymosin alpha: a biologically active protein with random coil conformation. <i> Gast K, Damaschun H, Eckert K, Schulze-Forster K, Maurer HR, Müller-Frohne M, Zirwer D, Czarnecki J, Damaschun G. </i> Biochemistry, 1995","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007731","ec_ontology":"ECO","ec_name":"spectrometry evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00814r004","statement":[{"text":"Electrospray ionization mass spectrometry investigations yielded a single peak with an average molar mass of 11982.8 g/mol.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":110,"reference_id":"7548085","reference_source":"pmid","reference_html":"Prothymosin alpha: a biologically active protein with random coil conformation. <i> Gast K, Damaschun H, Eckert K, Schulze-Forster K, Maurer HR, Müller-Frohne M, Zirwer D, Czarnecki J, Damaschun G. </i> Biochemistry, 1995","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007066","ec_ontology":"ECO","ec_name":"static light scattering assay evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00814r005","statement":[{"text":"Measurements of the excess scattered intensity of protein solutions at finite concentrations yield apparent molar masses, Mapp. The molar mass can be estimated by a linear extrapolation to 0 protein concentration according to 1/Mapp=1/m + 2bC, where B is the second virial coefficient. The corresponding data for ProTα in PBS, pH 7.4, are shown in Figure 2. A linear least-squares fit yields M = (11700 ± 1200)g/mol and a second virial coefficient B=(2.84 ± 0.30)x10-3mol cm3/ g2. ","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P01252","date":"2016-08-23T11:10:10.000Z","acc":"P01252","name":"Prothymosin alpha","length":110,"organism":"Bos taurus","dataset":[],"UniParc":"UPI0000136F24","genes":[{"name":{"value":"PTMA"}}],"alphafold_very_low_content":0.00909090909090909,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":110,"type":"D"}],"Structural state":[{"start":1,"end":110,"type":"D"}]}},{"features":{"pfam":[{"id":"PF04979","name":"Protein phosphatase inhibitor 2 (IPP-2)","start":46,"end":174}]},"uniref50":"UniRef50_Q9DCL8","sequence":"MAASTASHRPIKGILKNKTSAASPPVVPSAEQPRPIVEEELSKKSQKWDEMNILATYHPADKDYGLMKIDEPNTPYHNMIGDDEDAYSDSEGNEVMTPDILAKKLAAAEGSEPKYRTREQESSGEEDNDLSPEEREKKRQFEMKRKLHYNEGLNIKLARQLISKDLHDDDEDEEMAETADGDSMNVEESSQGSTTSDHLQHKSQSS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q9DCL8","disprot_id":"DP00815","ncbi_taxon_id":10090,"regions_counter":20,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":206,"region_id":"DP00815r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structural basis for regulation of protein phosphatase 1 by inhibitor-2. <i> Hurley TD, Yang J, Zhang L, Goodwin KD, Zou Q, Cortese M, Dunker AK, DePaoli-Roach AA. </i> J Biol Chem, 2007","term_id":"IDPO:0000002","curator_id":"bszabo","start":1,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"17636256","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":206,"term_name":"molecular function inhibitor activity","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"17636256","version":3,"reference_html":"Structural basis for regulation of protein phosphatase 1 by inhibitor-2. <i> Hurley TD, Yang J, Zhang L, Goodwin KD, Zou Q, Cortese M, Dunker AK, DePaoli-Roach AA. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140678","ec_id":"ECO:0006204","region_id":"DP00815r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":206,"term_name":"disorder to order","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"17636256","version":2,"reference_html":"Structural basis for regulation of protein phosphatase 1 by inhibitor-2. <i> Hurley TD, Yang J, Zhang L, Goodwin KD, Zou Q, Cortese M, Dunker AK, DePaoli-Roach AA. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00815r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":206,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"17636256","version":3,"reference_html":"Structural basis for regulation of protein phosphatase 1 by inhibitor-2. <i> Hurley TD, Yang J, Zhang L, Goodwin KD, Zou Q, Cortese M, Dunker AK, DePaoli-Roach AA. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00815r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":42,"region_id":"DP00815r005","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for regulation of protein phosphatase 1 by inhibitor-2. <i> Hurley TD, Yang J, Zhang L, Goodwin KD, Zou Q, Cortese M, Dunker AK, DePaoli-Roach AA. </i> J Biol Chem, 2007","term_id":"IDPO:0000002","curator_id":"bszabo","start":17,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"17636256","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2O8G"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":42,"term_name":"molecular function inhibitor activity","start":17,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"17636256","version":3,"reference_html":"Structural basis for regulation of protein phosphatase 1 by inhibitor-2. <i> Hurley TD, Yang J, Zhang L, Goodwin KD, Zou Q, Cortese M, Dunker AK, DePaoli-Roach AA. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140678","ec_id":"ECO:0006220","region_id":"DP00815r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":42,"term_name":"disorder to order","start":17,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"17636256","version":2,"reference_html":"Structural basis for regulation of protein phosphatase 1 by inhibitor-2. <i> Hurley TD, Yang J, Zhang L, Goodwin KD, Zou Q, Cortese M, Dunker AK, DePaoli-Roach AA. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00815r007","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":42,"term_name":"protein binding","start":17,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"17636256","version":3,"reference_html":"Structural basis for regulation of protein phosphatase 1 by inhibitor-2. <i> Hurley TD, Yang J, Zhang L, Goodwin KD, Zou Q, Cortese M, Dunker AK, DePaoli-Roach AA. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00815r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":11,"region_id":"DP00815r009","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for regulation of protein phosphatase 1 by inhibitor-2. <i> Hurley TD, Yang J, Zhang L, Goodwin KD, Zou Q, Cortese M, Dunker AK, DePaoli-Roach AA. </i> J Biol Chem, 2007","term_id":"IDPO:0000002","curator_id":"bszabo","start":1,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"17636256","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2O8G"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":11,"term_name":"molecular function inhibitor activity","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"17636256","version":3,"reference_html":"Structural basis for regulation of protein phosphatase 1 by inhibitor-2. <i> Hurley TD, Yang J, Zhang L, Goodwin KD, Zou Q, Cortese M, Dunker AK, DePaoli-Roach AA. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140678","ec_id":"ECO:0006220","region_id":"DP00815r010","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":11,"term_name":"disorder to order","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"17636256","version":2,"reference_html":"Structural basis for regulation of protein phosphatase 1 by inhibitor-2. <i> Hurley TD, Yang J, Zhang L, Goodwin KD, Zou Q, Cortese M, Dunker AK, DePaoli-Roach AA. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00815r011","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":11,"term_name":"protein binding","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"17636256","version":3,"reference_html":"Structural basis for regulation of protein phosphatase 1 by inhibitor-2. <i> Hurley TD, Yang J, Zhang L, Goodwin KD, Zou Q, Cortese M, Dunker AK, DePaoli-Roach AA. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00815r012","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":129,"region_id":"DP00815r013","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for regulation of protein phosphatase 1 by inhibitor-2. <i> Hurley TD, Yang J, Zhang L, Goodwin KD, Zou Q, Cortese M, Dunker AK, DePaoli-Roach AA. </i> J Biol Chem, 2007","term_id":"IDPO:0000002","curator_id":"bszabo","start":57,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"17636256","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2O8G"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":129,"term_name":"molecular function inhibitor activity","start":57,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"17636256","version":3,"reference_html":"Structural basis for regulation of protein phosphatase 1 by inhibitor-2. <i> Hurley TD, Yang J, Zhang L, Goodwin KD, Zou Q, Cortese M, Dunker AK, DePaoli-Roach AA. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140678","ec_id":"ECO:0006220","region_id":"DP00815r014","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":129,"term_name":"disorder to order","start":57,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"17636256","version":2,"reference_html":"Structural basis for regulation of protein phosphatase 1 by inhibitor-2. <i> Hurley TD, Yang J, Zhang L, Goodwin KD, Zou Q, Cortese M, Dunker AK, DePaoli-Roach AA. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00815r015","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":129,"term_name":"protein binding","start":57,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"17636256","version":3,"reference_html":"Structural basis for regulation of protein phosphatase 1 by inhibitor-2. <i> Hurley TD, Yang J, Zhang L, Goodwin KD, Zou Q, Cortese M, Dunker AK, DePaoli-Roach AA. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00815r016","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":206,"region_id":"DP00815r017","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for regulation of protein phosphatase 1 by inhibitor-2. <i> Hurley TD, Yang J, Zhang L, Goodwin KD, Zou Q, Cortese M, Dunker AK, DePaoli-Roach AA. </i> J Biol Chem, 2007","term_id":"IDPO:0000002","curator_id":"bszabo","start":170,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"17636256","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2O8G"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":206,"term_name":"molecular function inhibitor activity","start":170,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"17636256","version":3,"reference_html":"Structural basis for regulation of protein phosphatase 1 by inhibitor-2. <i> Hurley TD, Yang J, Zhang L, Goodwin KD, Zou Q, Cortese M, Dunker AK, DePaoli-Roach AA. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140678","ec_id":"ECO:0006220","region_id":"DP00815r018","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":206,"term_name":"disorder to order","start":170,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"17636256","version":2,"reference_html":"Structural basis for regulation of protein phosphatase 1 by inhibitor-2. <i> Hurley TD, Yang J, Zhang L, Goodwin KD, Zou Q, Cortese M, Dunker AK, DePaoli-Roach AA. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00815r019","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":206,"term_name":"protein binding","start":170,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"17636256","version":3,"reference_html":"Structural basis for regulation of protein phosphatase 1 by inhibitor-2. <i> Hurley TD, Yang J, Zhang L, Goodwin KD, Zou Q, Cortese M, Dunker AK, DePaoli-Roach AA. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00815r020","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q9DCL8","date":"2016-08-23T11:29:06.000Z","acc":"Q9DCL8","name":"Protein phosphatase inhibitor 2","length":206,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000028607","genes":[{"name":{"value":"Ppp1r2"}}],"alphafold_very_low_content":0.13106796116504854,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":206,"type":"T"}],"Structural state":[{"start":1,"end":206,"type":"D"}],"Molecular function":[{"start":1,"end":206,"type":"F"}],"Structural transition":[{"start":1,"end":206,"type":"T"}]}},{"features":{"pfam":[{"id":"PF04979","name":"Protein phosphatase inhibitor 2 (IPP-2)","start":45,"end":173}]},"uniref50":"UniRef50_P41236","sequence":"MAASTASHRPIKGILKNKTSTTSSMVASAEQPRGNVDEELSKKSQKWDEMNILATYHPADKDYGLMKIDEPSTPYHSMMGDDEDACSDTEATEAMAPDILARKLAAAEGLEPKYRIQEQESSGEEDSDLSPEEREKKRQFEMKRKLHYNEGLNIKLARQLISKDLHDDDEDEEMLETADGESMNTEESNQGSTPSDQQQNKLRSS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P41236","disprot_id":"DP00816","ncbi_taxon_id":9606,"regions_counter":8,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":164,"region_id":"DP00816r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Detailed structural characterization of unbound protein phosphatase 1 inhibitors. <i> Dancheck B, Nairn AC, Peti W. </i> Biochemistry, 2008","term_id":"IDPO:0000002","curator_id":"bszabo","start":9,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"18954090","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"15179"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":164,"term_name":"molecular function inhibitor activity","start":9,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"18954090","version":3,"reference_html":"Detailed structural characterization of unbound protein phosphatase 1 inhibitors. <i> Dancheck B, Nairn AC, Peti W. </i> Biochemistry, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140678","ec_id":"ECO:0006165","region_id":"DP00816r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":164,"term_name":"disorder to order","start":9,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"18954090","version":2,"reference_html":"Detailed structural characterization of unbound protein phosphatase 1 inhibitors. <i> Dancheck B, Nairn AC, Peti W. </i> Biochemistry, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00816r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":164,"term_name":"protein binding","start":9,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"18954090","version":3,"reference_html":"Detailed structural characterization of unbound protein phosphatase 1 inhibitors. <i> Dancheck B, Nairn AC, Peti W. </i> Biochemistry, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00816r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":164,"region_id":"DP00816r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural diversity in free and bound states of intrinsically disordered protein phosphatase 1 regulators. <i> Marsh JA, Dancheck B, Ragusa MJ, Allaire M, Forman-Kay JD, Peti W. </i> Structure, 2010","term_id":"IDPO:0000002","curator_id":"bszabo","start":9,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"20826336","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":164,"term_name":"molecular function inhibitor activity","start":9,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"20826336","version":3,"reference_html":"Structural diversity in free and bound states of intrinsically disordered protein phosphatase 1 regulators. <i> Marsh JA, Dancheck B, Ragusa MJ, Allaire M, Forman-Kay JD, Peti W. </i> Structure, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140678","ec_id":"ECO:0006165","region_id":"DP00816r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":164,"term_name":"disorder to order","start":9,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"20826336","version":2,"reference_html":"Structural diversity in free and bound states of intrinsically disordered protein phosphatase 1 regulators. <i> Marsh JA, Dancheck B, Ragusa MJ, Allaire M, Forman-Kay JD, Peti W. </i> Structure, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00816r007","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":164,"term_name":"protein binding","start":9,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"20826336","version":3,"reference_html":"Structural diversity in free and bound states of intrinsically disordered protein phosphatase 1 regulators. <i> Marsh JA, Dancheck B, Ragusa MJ, Allaire M, Forman-Kay JD, Peti W. </i> Structure, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00816r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P41236","date":"2016-08-23T14:26:04.000Z","acc":"P41236","name":"Protein phosphatase inhibitor 2","length":205,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000049C96","genes":[{"name":{"value":"PPP1R2"},"synonyms":[{"value":"IPP2"}]}],"alphafold_very_low_content":0.2097560975609756,"disorder_content":0.7609756097560976,"disprot_consensus":{"full":[{"start":9,"end":164,"type":"T"}],"Structural state":[{"start":9,"end":164,"type":"D"}],"Molecular function":[{"start":9,"end":164,"type":"F"}],"Structural transition":[{"start":9,"end":164,"type":"T"}]}},{"features":{"pfam":[{"id":"PF03604","name":"DNA directed RNA polymerase, 7 kDa subunit","start":25,"end":63}],"gene3D":[{"start":15,"end":70,"id":"2.20.28.30","name":"RNA polymerase ii, chain L"}]},"uniref50":"UniRef50_P40422","sequence":"MSREGFQIPTNLDAAAAGTSQARTATLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRLVQFEAR","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P40422","disprot_id":"DP00818","ncbi_taxon_id":559292,"regions_counter":1,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":25,"region_id":"DP00818r001","released":"2023_12","ec_id":"ECO:0006224","reference_html":"Molecular structures of unbound and transcribing RNA polymerase III. <i> Hoffmann NA, Jakobi AJ, Moreno-Morcillo M, Moreno-Morcillo M, Glatt S, Kosinski J, Hagen WJ, Sachse C, Müller CW. </i> Nature, 2015","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"26605533","version":3,"ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","date":"2023-08-22T17:37:14.773Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5FJ8"}],"term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The Electron microscopy structure of the yeast RNA polymerase III elongation complex, shows this region of the subunit RPABC4 is disordered.","type":"Curator statement"}]}],"released":"2016_10","uniref100":"UniRef100_P40422","date":"2016-08-23T15:59:36.000Z","acc":"P40422","name":"DNA-directed RNA polymerases I, II, and III subunit RPABC4","length":70,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000013460F","genes":[{"name":{"value":"RPC10"},"synonyms":[{"value":"RPB12"}],"orfNames":[{"value":"YHR143BW"}],"olnNames":[{"value":"YHR143W-A"}]}],"alphafold_very_low_content":0,"disorder_content":0.35714285714285715,"disprot_consensus":{"full":[{"start":1,"end":25,"type":"D"}],"Structural state":[{"start":1,"end":25,"type":"D"}]}},{"acc":"O73557","sequence":"MGNKQAKAPESKDSPRASLIPDATHLGPQFCKSCWFENKGLVECNNHYLCLNCLTLLLSVSNRCPICKMPLPTKLRPSAAPTAPPTGAADSIRPPPYSP","creator":"jpujols","dataset":["Viral proteins"],"date":"2016-08-24T04:10:20.000Z","disprot_id":"DP00820","features":{"pfam":[{"id":"PF03854","name":"P-11 zinc finger","start":27,"end":76}],"gene3D":[{"start":39,"end":73,"id":"3.30.160.310","name":"3.30.160.310","_id":"685af523b4ac24d5329d85ce"}]},"genes":[{"name":{"value":"Z","evidences":[{"source":{"id":"MF_04087","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04087","_id":"685af523b4ac24d5329d8613"},"code":"ECO:0000255","_id":"685af523b4ac24d5329d8612"}],"_id":"685af523b4ac24d5329d8614"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d8611"}],"length":99,"name":"RING finger protein Z","ncbi_taxon_id":11622,"organism":"Lassa virus (strain Mouse/Sierra Leone/Josiah/1976)","regions_counter":14,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Polyploviricotina","Ellioviricetes","Bunyavirales","Arenaviridae","Mammarenavirus"],"UniParc":"UPI00000F4F33","uniref100":"UniRef100_O73557","uniref50":"UniRef50_O73557","uniref90":"UniRef90_O73557","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2M1S","_id":"685af523b4ac24d5329d85d0"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":29,"interaction_partner":[],"reference_html":"Structural characterization of the Z RING-eIF4E complex reveals a distinct mode of control for eIF4E. <i> Volpon L, Osborne MJ, Capul AA, de la Torre JC, Borden KL. </i> Proc Natl Acad Sci U S A, 2010","reference_id":"20212144","region_id":"DP00820r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In contrast, the N terminus (1–29) and C terminus (71–99) exhibit very low heteronuclear NOE values, consistent with these being disordered.","_id":"685af523b4ac24d5329d85d1"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T12:55:47.121Z","_id":"685af523b4ac24d5329d85d2"},"version":3,"_id":"685af523b4ac24d5329d85cf","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":29,"interaction_partner":[],"reference_html":"Structural characterization of the Z RING-eIF4E complex reveals a distinct mode of control for eIF4E. <i> Volpon L, Osborne MJ, Capul AA, de la Torre JC, Borden KL. </i> Proc Natl Acad Sci U S A, 2010","reference_id":"20212144","region_id":"DP00820r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In contrast, the N terminus (1–29) and C terminus (71–99) exhibit very low heteronuclear NOE values, consistent with these being disordered.","_id":"685af523b4ac24d5329d85d4"}],"states_connection":[],"term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T12:56:22.149Z","_id":"685af523b4ac24d5329d85d5"},"version":4,"_id":"685af523b4ac24d5329d85d3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5I72","_id":"685af523b4ac24d5329d85d7"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":25,"interaction_partner":[],"reference_html":"Crystal Structure of the Oligomeric Form of Lassa Virus Matrix Protein Z. <i> Hastie KM, Zandonatti M, Liu T, Li S, Woods VL, Saphire EO. </i> J Virol, 2016","reference_id":"26912609","region_id":"DP00820r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Although the construct used for crystallization encodes full-length Z, only residues 26 to 73 are ordered in monomer A and residues 26 to 75 are ordered in monomer B.","_id":"685af523b4ac24d5329d85d8"},{"type":"Results","text":"Indeed, residues 1 to 25 and 76 to 99 are disordered in the crystal structure and in solution studies by NMR.","_id":"685af523b4ac24d5329d85d9"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T12:55:34.490Z","_id":"685af523b4ac24d5329d85da"},"version":3,"_id":"685af523b4ac24d5329d85d6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5I72","_id":"685af523b4ac24d5329d85de"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":76,"end":99,"interaction_partner":[],"reference_html":"Crystal Structure of the Oligomeric Form of Lassa Virus Matrix Protein Z. <i> Hastie KM, Zandonatti M, Liu T, Li S, Woods VL, Saphire EO. </i> J Virol, 2016","reference_id":"26912609","region_id":"DP00820r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Although the construct used for crystallization encodes full-length Z, only residues 26 to 73 are ordered in monomer A and residues 26 to 75 are ordered in monomer B.","_id":"685af523b4ac24d5329d85df"},{"type":"Results","text":"Indeed, residues 1 to 25 and 76 to 99 are disordered in the crystal structure and in solution studies by NMR.","_id":"685af523b4ac24d5329d85e0"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T12:54:54.476Z","_id":"685af523b4ac24d5329d85e1"},"version":3,"_id":"685af523b4ac24d5329d85dd","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2M1S","_id":"685af523b4ac24d5329d85e5"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":71,"end":99,"interaction_partner":[],"reference_html":"Structural characterization of the Z RING-eIF4E complex reveals a distinct mode of control for eIF4E. <i> Volpon L, Osborne MJ, Capul AA, de la Torre JC, Borden KL. </i> Proc Natl Acad Sci U S A, 2010","reference_id":"20212144","region_id":"DP00820r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In contrast, the N terminus (1–29) and C terminus (71–99) exhibit very low heteronuclear NOE values, consistent with these being disordered.","_id":"685af523b4ac24d5329d85e6"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T12:55:25.662Z","_id":"685af523b4ac24d5329d85e7"},"version":3,"_id":"685af523b4ac24d5329d85e4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":71,"end":99,"interaction_partner":[],"reference_html":"Structural characterization of the Z RING-eIF4E complex reveals a distinct mode of control for eIF4E. <i> Volpon L, Osborne MJ, Capul AA, de la Torre JC, Borden KL. </i> Proc Natl Acad Sci U S A, 2010","reference_id":"20212144","region_id":"DP00820r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In contrast, the N terminus (1–29) and C terminus (71–99) exhibit very low heteronuclear NOE values, consistent with these being disordered.","_id":"685af523b4ac24d5329d85e9"}],"states_connection":[],"term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T12:55:53.786Z","_id":"685af523b4ac24d5329d85ea"},"version":4,"_id":"685af523b4ac24d5329d85e8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":25,"interaction_partner":[],"reference_html":"Crystal Structure of the Oligomeric Form of Lassa Virus Matrix Protein Z. <i> Hastie KM, Zandonatti M, Liu T, Li S, Woods VL, Saphire EO. </i> J Virol, 2016","reference_id":"26912609","region_id":"DP00820r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The extreme N and C termini of Z (residues 1 to 25 and residues 76 to 99) showed very high H/D exchange rates, indicating that these regions are highly flexible. Indeed, residues 1 to 25 and 76 to 99 are disordered in the crystal structure and in solution studies by NMR.","_id":"685af523b4ac24d5329d85ec"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T12:54:43.140Z","_id":"685af523b4ac24d5329d85ed"},"version":1,"_id":"685af523b4ac24d5329d85eb","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":76,"end":99,"interaction_partner":[],"reference_html":"Crystal Structure of the Oligomeric Form of Lassa Virus Matrix Protein Z. <i> Hastie KM, Zandonatti M, Liu T, Li S, Woods VL, Saphire EO. </i> J Virol, 2016","reference_id":"26912609","region_id":"DP00820r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The extreme N and C termini of Z (residues 1 to 25 and residues 76 to 99) showed very high H/D exchange rates, indicating that these regions are highly flexible. Indeed, residues 1 to 25 and 76 to 99 are disordered in the crystal structure and in solution studies by NMR.","_id":"685af523b4ac24d5329d85ef"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T12:53:51.791Z","_id":"685af523b4ac24d5329d85f0"},"version":1,"_id":"685af523b4ac24d5329d85ee","reference_source":"pmid"}],"__v":0,"disorder_content":0.5858585858585859,"disprot_consensus":{"full":[{"start":1,"end":29,"type":"D"},{"start":71,"end":99,"type":"D"}],"Structural state":[{"start":1,"end":29,"type":"D"},{"start":71,"end":99,"type":"D"}],"Disorder function":[{"start":1,"end":29,"type":"F"},{"start":71,"end":99,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00472","name":"RF-1 domain","start":7,"end":132}],"gene3D":[{"start":1,"end":136,"id":"3.30.160.20","name":"3.30.160.20"}]},"uniref50":"UniRef50_A0A653TMD7","sequence":"MLVISNNVHLPDAEIELTAIRAQGAGGQNVNKVSSAMHLRFDINASSLPPFYKERLLALNDSRITSDGVIVLKAQQYRTQEQNRADALLRLSELIVNAAKVEKKRRPTRPTLGSKTRRLESKSKRGSIKAGRGKVDF","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Pseudomonadales","Pseudomonadaceae","Pseudomonas"],"uniref90":"UniRef90_I4MWW5","disprot_id":"DP00822","ncbi_taxon_id":223283,"regions_counter":3,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":130,"region_id":"DP00822r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR structure of the peptidyl-tRNA hydrolase domain from Pseudomonas syringae expands the structural coverage of the hydrolysis domains of class 1 peptide chain release factors. <i> Singarapu KK, Xiao R, Acton T, Rost B, Montelione GT, Szyperski T. </i> Proteins, 2008","term_id":"IDPO:0000002","curator_id":"jpujols","start":100,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2JVA"}],"reference_id":"18247350","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":35,"region_id":"DP00822r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR structure of the peptidyl-tRNA hydrolase domain from Pseudomonas syringae expands the structural coverage of the hydrolysis domains of class 1 peptide chain release factors. <i> Singarapu KK, Xiao R, Acton T, Rost B, Montelione GT, Szyperski T. </i> Proteins, 2008","term_id":"IDPO:0000002","curator_id":"jpujols","start":21,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2JVA"}],"reference_id":"18247350","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":35,"term_name":"molecular recognition display site","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"NMR structure of the peptidyl-tRNA hydrolase domain from Pseudomonas syringae expands the structural coverage of the hydrolysis domains of class 1 peptide chain release factors. <i> Singarapu KK, Xiao R, Acton T, Rost B, Montelione GT, Szyperski T. </i> Proteins, 2008","term_id":"IDPO:0000037","curator_id":"jpujols","start":21,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","reference_id":"18247350","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00822r003","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_A0A0N0WM55","date":"2016-08-24T04:55:29.000Z","acc":"Q885L4","name":"Peptidyl-tRNA hydrolase domain protein","length":137,"organism":"Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)","dataset":[],"UniParc":"UPI0000008957","genes":[{"olnNames":[{"value":"PSPTO_1818","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAO55337.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAO55337.1"}}]}]}],"alphafold_very_low_content":0,"disorder_content":0.3357664233576642,"disprot_consensus":{"full":[{"start":21,"end":35,"type":"D"},{"start":100,"end":130,"type":"D"}],"Structural state":[{"start":21,"end":35,"type":"D"},{"start":100,"end":130,"type":"D"}],"Disorder function":[{"start":21,"end":35,"type":"F"}]}},{"features":{"pfam":[{"id":"PF08209","name":"Sgf11 (transcriptional regulation protein)","start":67,"end":99},{"id":"PF18519","name":"SAGA-associated factor 11 N-terminal domain","start":6,"end":44}],"gene3D":[{"start":69,"end":99,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":1,"end":42,"id":"1.10.287.210","name":"1.10.287.210"}]},"uniref50":"UniRef50_Q751G1","sequence":"MTEETITIDSISNGILNNLLTTLIQDIVARETTQQQLLKTRYPDLRSYYFDPNGSLDINGLQKQQESSQYIHCENCGRDVSANRLAAHLQRCLSRGARR","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_A6ZWK1","disprot_id":"DP00823","ncbi_taxon_id":889517,"regions_counter":2,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":99,"region_id":"DP00823r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Uncovering the role of Sgf73 in maintaining SAGA deubiquitinating module structure and activity. <i> Yan M, Wolberger C. </i> J Mol Biol, 2015","term_id":"IDPO:0000002","curator_id":"fquaglia","start":64,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"25526805","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4W4U"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":99,"term_name":"DNA binding, bending","start":64,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"25526805","version":4,"reference_html":"Uncovering the role of Sgf73 in maintaining SAGA deubiquitinating module structure and activity. <i> Yan M, Wolberger C. </i> J Mol Biol, 2015","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008301","ec_id":"ECO:0006220","region_id":"DP00823r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The activity of binding selectively and non-covalently to and distorting the original structure of DNA, typically a straight helix, into a bend, or increasing the bend if the original structure was intrinsically bent due to its sequence.\" [GOC:krc, GOC:vw, PMID:10710711, PMID:19037758]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_A6ZWK1","date":"2016-08-24T05:04:38.000Z","acc":"N1NXA6","name":"SAGA-associated factor 11","length":99,"organism":"Saccharomyces cerevisiae (strain CEN.PK113-7D)","dataset":[],"UniParc":"UPI0000036C9D","genes":[{"name":{"value":"SGF11","evidences":[{"code":"ECO:0000256","source":{"name":"HAMAP-Rule","id":"MF_03047","url":"https://hamap.expasy.org/unirule/MF_03047"}}]},"orfNames":[{"value":"CENPK1137D_1654","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EIW07067.1","url":"https://www.ebi.ac.uk/ena/browser/view/EIW07067.1"}}]}]}],"alphafold_very_low_content":0.020202020202020204,"disorder_content":0.36363636363636365,"disprot_consensus":{"full":[{"start":64,"end":99,"type":"D"}],"Structural state":[{"start":64,"end":99,"type":"D"}],"Molecular function":[{"start":64,"end":99,"type":"F"}]}},{"features":{"pfam":[{"id":"PF10731","name":"Thrombin inhibitor from mosquito","start":1,"end":54}]},"uniref50":"UniRef50_Q9NJS1","sequence":"MANKLVLISLLCVVLVAKITQAAPQYAPGDEPSYDEDTDDSDKLVENDTSITDEDYAAIEASLSETFNTAADPGRRLGEGSKP","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Nematocera","Culicoidea","Culicidae","Anophelinae","Anopheles"],"uniref90":"UniRef90_Q9NJS1","disprot_id":"DP00824","ncbi_taxon_id":7167,"regions_counter":13,"creator":"ppere","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":83,"region_id":"DP00824r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector. <i> Figueiredo AC, de Sanctis D, Gutiérrez-Gallego R, Cereija TB, Macedo-Ribeiro S, Fuentes-Prior P, Pereira PJ. </i> Proc Natl Acad Sci U S A, 2012","statement":[{"text":"Electron density maps were readily interpretable for mature anophelin residues AE32 to AP61 (Fig. 3A), but no significant\ndensity was detectable for the remaining N-terminal residues AA1 to AD31.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":54,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4E05"}],"reference_id":"23223529","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":83,"term_name":"molecular function inhibitor activity","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector. <i> Figueiredo AC, de Sanctis D, Gutiérrez-Gallego R, Cereija TB, Macedo-Ribeiro S, Fuentes-Prior P, Pereira PJ. </i> Proc Natl Acad Sci U S A, 2012","statement":[{"text":"...the inhibitor adopts a mostly extended conformation and binds to the proteinase in a reverse orientation (i.e., opposite to substrates) (Fig. S4).","type":"Results"}],"term_id":"GO:0140678","curator_id":"ppereira","start":54,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"23223529","version":4,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00824r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":83,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector. <i> Figueiredo AC, de Sanctis D, Gutiérrez-Gallego R, Cereija TB, Macedo-Ribeiro S, Fuentes-Prior P, Pereira PJ. </i> Proc Natl Acad Sci U S A, 2012","statement":[{"text":"In the two independent crystal structures of the human α-thrombin·anophelin complex, only the C-terminal portion of the inhibitor (...) was fully defined by electron density.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"ppereira","start":54,"term_ontology":"IDPO","curator_name":"Pedro Pereira","reference_id":"23223529","version":3,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00824r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":83,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector. <i> Figueiredo AC, de Sanctis D, Gutiérrez-Gallego R, Cereija TB, Macedo-Ribeiro S, Fuentes-Prior P, Pereira PJ. </i> Proc Natl Acad Sci U S A, 2012","statement":[{"text":"...the inhibitor adopts a mostly extended conformation and binds to the proteinase in a reverse orientation (i.e., opposite to substrates) (Fig. S4).","type":"Results"}],"term_id":"GO:0005515","curator_id":"ppereira","start":54,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"23223529","version":4,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00824r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":83,"region_id":"DP00824r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector. <i> Figueiredo AC, de Sanctis D, Gutiérrez-Gallego R, Cereija TB, Macedo-Ribeiro S, Fuentes-Prior P, Pereira PJ. </i> Proc Natl Acad Sci U S A, 2012","statement":[{"text":"In line with their lack of cysteines and the preponderance of polar residues, anophelins are predicted to be intrinsically disordered in solution (Fig. S1A). Indeed, the circular dichroism (CD) spectrum of anophelinAa is typical of random coils, and its deconvolution with different methods suggests a mostly disordered polypeptide (Fig. S1B).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"sventura","start":23,"term_ontology":"IDPO","curator_name":"Salvador Ventura","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4E05"}],"reference_id":"23223529","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":53,"region_id":"DP00824r006","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector. <i> Figueiredo AC, de Sanctis D, Gutiérrez-Gallego R, Cereija TB, Macedo-Ribeiro S, Fuentes-Prior P, Pereira PJ. </i> Proc Natl Acad Sci U S A, 2012","statement":[{"text":"In line with their lack of cysteines and the preponderance of polar residues, anophelins are predicted to be intrinsically disordered in solution (Fig. S1A). Indeed, the circular dichroism (CD) spectrum of anophelinAa is typical of random coils, and its deconvolution with different methods suggests a mostly disordered polypeptide (Fig. S1B).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":23,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23223529","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":83,"region_id":"DP00824r007","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector. <i> Figueiredo AC, de Sanctis D, Gutiérrez-Gallego R, Cereija TB, Macedo-Ribeiro S, Fuentes-Prior P, Pereira PJ. </i> Proc Natl Acad Sci U S A, 2012","statement":[{"text":"In line with their lack of cysteines and the preponderance of polar residues, anophelins are predicted to be intrinsically disordered in solution (Fig. S1A). Indeed, the circular dichroism (CD) spectrum of anophelinAa is typical of random coils, and its deconvolution with different methods suggests a mostly disordered polypeptide (Fig. S1B).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":54,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23223529","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":53,"region_id":"DP00824r008","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector. <i> Figueiredo AC, de Sanctis D, Gutiérrez-Gallego R, Cereija TB, Macedo-Ribeiro S, Fuentes-Prior P, Pereira PJ. </i> Proc Natl Acad Sci U S A, 2012","statement":[{"text":"...no significant density was detectable for the remaining N-terminal residues AA1 to AD31.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":23,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4E05"}],"reference_id":"23223529","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":83,"region_id":"DP00824r009","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector. <i> Figueiredo AC, de Sanctis D, Gutiérrez-Gallego R, Cereija TB, Macedo-Ribeiro S, Fuentes-Prior P, Pereira PJ. </i> Proc Natl Acad Sci U S A, 2012","statement":[{"text":"This N-terminal segment was similarly disordered in a second crystal form of the anophelin·thrombin complex solved at 3.2-Å resolution (space group H32; rmsd of 0.25 Å for 263 aligned Cα atoms) (Table 4) and also in this case, not constrained by crystal packing.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":56,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4E06"}],"reference_id":"23223529","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":83,"term_name":"molecular function inhibitor activity","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector. <i> Figueiredo AC, de Sanctis D, Gutiérrez-Gallego R, Cereija TB, Macedo-Ribeiro S, Fuentes-Prior P, Pereira PJ. </i> Proc Natl Acad Sci U S A, 2012","statement":[{"text":"...the inhibitor adopts a mostly extended conformation and binds to the proteinase in a reverse orientation (i.e., opposite to substrates) (Fig. S4).","type":"Results"}],"term_id":"GO:0140678","curator_id":"ppereira","start":56,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"23223529","version":3,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00824r010","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":83,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector. <i> Figueiredo AC, de Sanctis D, Gutiérrez-Gallego R, Cereija TB, Macedo-Ribeiro S, Fuentes-Prior P, Pereira PJ. </i> Proc Natl Acad Sci U S A, 2012","statement":[{"text":"...the inhibitor adopts a mostly extended conformation and binds to the proteinase in a reverse orientation (i.e., opposite to substrates) (Fig. S4).","type":"Results"}],"term_id":"GO:0005515","curator_id":"ppereira","start":56,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"23223529","version":3,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00824r011","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":83,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector. <i> Figueiredo AC, de Sanctis D, Gutiérrez-Gallego R, Cereija TB, Macedo-Ribeiro S, Fuentes-Prior P, Pereira PJ. </i> Proc Natl Acad Sci U S A, 2012","statement":[{"text":"In the two independent crystal structures of the human α-thrombin·anophelin complex, only the C-terminal portion of the inhibitor (...) was fully defined by electron density.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"ppereira","start":56,"term_ontology":"IDPO","curator_name":"Pedro Pereira","reference_id":"23223529","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00824r012","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":55,"region_id":"DP00824r013","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Unique thrombin inhibition mechanism by anophelin, an anticoagulant from the malaria vector. <i> Figueiredo AC, de Sanctis D, Gutiérrez-Gallego R, Cereija TB, Macedo-Ribeiro S, Fuentes-Prior P, Pereira PJ. </i> Proc Natl Acad Sci U S A, 2012","statement":[{"text":"Residues 23 to 55 are missing in PDB entry 4E06, being therefore disordered.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":23,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4E06"}],"reference_id":"23223529","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q9NJS1","date":"2016-08-24T05:18:17.000Z","acc":"Q9NJS1","name":"Salivary anti-thrombin peptide anophelin","length":83,"organism":"Anopheles albimanus","dataset":[],"UniParc":"UPI00000362D6","genes":[{"name":{"value":"AT","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF29443.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF29443.1"}}]}}],"alphafold_very_low_content":0,"disorder_content":0.7349397590361446,"disprot_consensus":{"full":[{"start":23,"end":53,"type":"D"},{"start":54,"end":83,"type":"T"}],"Structural state":[{"start":23,"end":83,"type":"D"}],"Molecular function":[{"start":54,"end":83,"type":"F"}],"Structural transition":[{"start":54,"end":83,"type":"T"}]}},{"features":{"pfam":[{"id":"PF02416","name":"mttA/Hcf106 family","start":4,"end":46}]},"uniref50":"UniRef50_O31467","sequence":"MFSNIGIPGLILIFVIALIIFGPSKLPEIGRAAGRTLLEFKSATKSLVSGDEKEEKSAELTAVKQDKNAG","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Bacillus"],"uniref90":"UniRef90_O31467","disprot_id":"DP00827","ncbi_taxon_id":224308,"regions_counter":4,"creator":"sventura","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":70,"region_id":"DP00827r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Solution NMR structure of the TatA component of the twin-arginine protein transport system from gram-positive bacterium Bacillus subtilis. <i> Hu Y, Zhao E, Li H, Xia B, Jin C. </i> J Am Chem Soc, 2010","term_id":"IDPO:0000002","curator_id":"sventura","start":49,"term_ontology":"IDPO","curator_name":"Salvador Ventura","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20726548","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":70,"region_id":"DP00827r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution NMR structure of the TatA component of the twin-arginine protein transport system from gram-positive bacterium Bacillus subtilis. <i> Hu Y, Zhao E, Li H, Xia B, Jin C. </i> J Am Chem Soc, 2010","term_id":"IDPO:0000002","curator_id":"sventura","start":49,"term_ontology":"IDPO","curator_name":"Salvador Ventura","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2L16"}],"reference_id":"20726548","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_O31467","date":"2016-08-24T05:44:48.000Z","acc":"O31467","name":"Sec-independent protein translocase protein TatAd","length":70,"organism":"Bacillus subtilis (strain 168)","dataset":[],"UniParc":"UPI00000540BD","genes":[{"name":{"value":"tatAd","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00236","url":"https://hamap.expasy.org/unirule/MF_00236"}}]},"synonyms":[{"value":"yczB"}],"olnNames":[{"value":"BSU02630"}]}],"alphafold_very_low_content":0,"disorder_content":0.3142857142857143,"disprot_consensus":{"full":[{"start":49,"end":70,"type":"D"}],"Structural state":[{"start":49,"end":70,"type":"D"}]}},{"features":{"pfam":[{"id":"PF05392","name":"Cytochrome C oxidase chain VIIB","start":1,"end":79}],"gene3D":[{"start":25,"end":80,"id":"4.10.51.10","name":"Cytochrome C Oxidase, chain K"}]},"uniref50":"UniRef50_P13183","sequence":"MFPLAKNALSRLRVQSIQQAVARQIHQKRAPDFHDKYGNAVLASGATFCVAVWVYMATQIGIEWNPSPVGRVTPKEWREQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P13183","disprot_id":"DP00828","ncbi_taxon_id":9913,"regions_counter":2,"creator":"sventura","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":56,"region_id":"DP00828r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A. <i> Tsukihara T, Aoyama H, Yamashita E, Tomizaki T, Yamaguchi H, Shinzawa-Itoh K, Nakashima R, Yaono R, Yoshikawa S. </i> Science, 1996","term_id":"IDPO:0000002","curator_id":"sventura","start":36,"term_ontology":"IDPO","curator_name":"Salvador Ventura","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1OCC"}],"reference_id":"8638158","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":56,"region_id":"DP00828r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"A combined quantum chemical and crystallographic study on the oxidized binuclear center of cytochrome c oxidase. <i> Kaila VR, Oksanen E, Goldman A, Bloch DA, Verkhovsky MI, Sundholm D, Wikström M. </i> Biochim Biophys Acta, 2011","term_id":"IDPO:0000002","curator_id":"sventura","start":36,"term_ontology":"IDPO","curator_name":"Salvador Ventura","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2Y69"}],"reference_id":"21211513","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P13183","date":"2016-08-24T05:53:12.000Z","acc":"P13183","name":"Cytochrome c oxidase subunit 7B, mitochondrial","length":80,"organism":"Bos taurus","dataset":[],"UniParc":"UPI0000128162","genes":[{"name":{"value":"COX7B"}}],"alphafold_very_low_content":0,"disorder_content":0.2625,"disprot_consensus":{"full":[{"start":36,"end":56,"type":"D"}],"Structural state":[{"start":36,"end":56,"type":"D"}]}},{"features":{"pfam":[{"id":"PF09386","name":"Antitoxin ParD","start":1,"end":77}],"gene3D":[{"start":1,"end":83,"id":"G3DSA:1.10.1220.50"}]},"uniref50":"UniRef50_P22995","sequence":"MSRLTIDMTDQQHQSLKALAALQGKTIKQYALERLFPGDADADQAWQELKTMLGNRINDGLAGKVSTKSVGEILDEELSGDRA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P22995","disprot_id":"DP00833","dataset":["Unicellular toxins and antitoxins"],"ncbi_taxon_id":562,"regions_counter":13,"creator":"bhajdu","regions":[{"region_id":"DP00833r001","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T13:52:51.171Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":83,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":58,"version":4,"statement":[{"text":"15N longitudinal (T1 ) and transverse (T2 ) relaxation measurements and heteronuclear NOEs showed that ParD is divided into two separate domains, a well-ordered N-terminal domain and a very flexible C-terminal domain. An increase in secondary structure was observed upon addition of trifluoroethanol, suggested to result from the formation of structured stretches in the C-terminal part of the protein","type":"Abstract"},{"text":"Consensus chemical shifts and NOE data (Figures 3B and 3C) indicate that the C-terminal region is less well ordered or undergoing rapid conformational change on the NMR timescale. However, \"13Cα chemical shifts show a tendency for the formation of further αhelices beyond the well-ordered N-terminal domain.[...] The negative NOE values for the C-terminal domain (Asp59–Ala83) indicate the presence of significant flexibility in this region. This is in excellent agreement with the \"15N-T1 and 15N-T2 relaxation times, which clearly show two structurally different moieties ranging from Leu4 to Ile57 for the well-structured N-terminus and from Asp59–Ala83 for the remaining flexible C-terminal region.[,,,] Cα chemical-shift data show a down-field shift from the random-coil values for residues in the C-terminus for residues 58–64, 66, 68–72, 74–81 and 83, indicating a tendency for the formation of helical structures. The deviations are, however, smaller than in the N-terminal region, which again supports the presence of a predominantly unstructured C-terminal domain.\n\n","type":"Results"}],"term_name":"disorder","reference_html":"The anti-toxin ParD of plasmid RK2 consists of two structurally distinct moieties and belongs to the ribbon-helix-helix family of DNA-binding proteins. <i> Oberer M, Zangger K, Prytulla S, Keller W. </i> Biochem J, 2002","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"11743881","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"4792"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"lchemes","curator_orcid":"0000-0003-0192-9906","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP00833r003","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T13:55:43.335Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":83,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":58,"version":4,"statement":[{"text":"Cα chemical-shift data show a down-field shift from the random-coil values for residues in the C-terminus for residues 58–64, 66, 68–72, 74–81 and 83, indicating a tendency for the formation of helical structures. The deviations are, however, smaller than in the N-terminal region, which again supports the presence of a predominantly unstructured C-terminal domain.\n\nAs can be seen from the combined chemical shift changes (Figure 7), addition of TFE influenced mainly the residues starting from Gly38), resulting in major chemical-shift differences. This indicates a transition from the more flexible and random-coil C-terminal moiety to an α-helical domain consistent with the CD experiment\n\nThe structural changes of ParD, which are induced by TFE addition as observed in the near-UV CD spectrum, indicate the formation of additional helical structure. As monitored by NMR spectroscopy, C-terminal residues appear to be involved mainly in these changes. \n","type":"Results"}],"term_name":"disorder to order","reference_html":"The anti-toxin ParD of plasmid RK2 consists of two structurally distinct moieties and belongs to the ribbon-helix-helix family of DNA-binding proteins. <i> Oberer M, Zangger K, Prytulla S, Keller W. </i> Biochem J, 2002","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"11743881","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"4792"}],"term_namespace":"Structural transition","ec_id":"ECO:0006165","curator_id":"lchemes","curator_orcid":"0000-0003-0192-9906","term_id":"IDPO:0000011","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00833r011","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T13:57:14.783Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":83,"term_id":"IDPO:0000011","start":58,"version":2,"statement":[{"text":"\nTFE was added to a ParD solution and changes in the secondary structure were monitored by CD spectroscopy. Upon an increase in the TFE concentration (from 0 to 5, 10, 20, 30, 40, 50, 60, 70 and 80%) the α-helical content rose gradually (from 37 to 44, 50, 53, 55, 62, 65, 68, 70 and 72%) with an isodichroic point at 200.4 nm (Figure 6).\nThe structural changes of ParD, which are induced by TFE addition as observed in the near-UV CD spectrum, indicate the formation of additional helical structure. As monitored by NMR spectroscopy, C-terminal residues appear to be involved mainly in these changes. ","type":"Results"},{"text":"Experimental 13Cα chemical-shift data, however, only indicate a propensity for α-helical regions in the C-terminus. We tried to induce this ‘missing’ helicity by the addition of TFE […] The structural changes of ParD, which are induced by TFE addition as observed in the near-UV CD spectrum, indicate the formation of additional helical structure","type":"Discussion"},{"text":"Near-UV CD is wrongly written by the authors, the spectrum shown in Figure 6 is a Far-UV CD spectrum","type":"Curator statement"}],"term_name":"disorder to order","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"11743881","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural transition","ec_id":"ECO:0006204","curator_id":"lchemes","reference_html":"The anti-toxin ParD of plasmid RK2 consists of two structurally distinct moieties and belongs to the ribbon-helix-helix family of DNA-binding proteins. <i> Oberer M, Zangger K, Prytulla S, Keller W. </i> Biochem J, 2002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00833r012","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T14:18:49.526Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":83,"term_id":"GO:0097351","start":50,"version":3,"statement":[{"text":"The mutations changed codons corresponding to Q51 and S53 of kis into the Ochre stop codon UAA. As this stop codon is not suppressed in the CSH16 (supE) background, the mutations should remove 35 and 33 residues, respectively, from the carboxyl terminus of the protein [...] Compared to the missense mutants, the nonsense mutants lose the antitoxin activity of the protein (Fig. 2). This suggests either that the deletions affect the region of Kis needed to inactivate Kid and to form with this protein an efficient repressor, or that these mutations severely affect the overall three-dimensional fold of Kis. However, since circular dichroism spectroscopy indicates that isolated Kis protein mainly has a flexible coil structure (our unpublished results), the latter hypothesis seems unlikely","type":"Results"}],"term_name":"toxin sequestering activity","ec_name":"mutant phenotype evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"11786266","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0000315","curator_id":"lchemes","reference_html":"Genetic identification of two functional regions in the antitoxin of the parD killer system of plasmid R1. <i> Santos-Sierra S, Pardo-Abarrio C, Giraldo R, Díaz-Orejas R. </i> FEMS Microbiol Lett, 2002","ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a toxic protein, disabling its function. There may be more than one antitoxin to a toxic protein. Instances of this activity are known only in prokaryotes, where the toxic protein may be a ribonuclease, a DNA gyrase, or other.\" [GOC:rs, PMID:19143615, PMID:19325885, PMID:21819231, PMID:22545240, PMID:24806488, Wikipedia:Toxin-antitoxin_system#Type_II]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00833r013","validated":{"curator_id":"fquaglia","timestamp":"2020-12-10T14:21:36.327Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":83,"term_id":"IDPO:0000002","start":38,"version":2,"statement":[{"text":"In this study, we show that the well-ordered N-terminal domain adopts the RHH fold whereas the C-terminal region is highly flexible in solution.","type":"Discussion"},{"text":"The lower number of NOEs found for the C-terminal portion of ParD is in agreement with the dynamic behavior already described for this protein, indicating an unstructured domain. Mainly intraresidual NOEs could be identified for the flexible C-terminal part of ParD.","type":"Results"},{"text":"The authors do not provide region boundaries. The region with high flexibility was determined based on the NMR structure PDB:2an7 using CYRANGE to include the bit that shows high RMSD between various models. This region however contains secondary structural elements and therefore isn't fully flexible.","type":"Curator statement"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"17656583","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2AN7"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"bmesza","reference_html":"The solution structure of ParD, the antidote of the ParDE toxin antitoxin module, provides the structural basis for DNA and toxin binding. <i> Oberer M, Zangger K, Gruber K, Keller W. </i> Protein Sci, 2007","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P22995","date":"2016-08-24T09:53:55.000Z","acc":"P22995","name":"Antitoxin ParD","length":83,"organism":"Escherichia coli","UniParc":"UPI000011F0B5","genes":[{"name":{"value":"parD"}}],"alphafold_very_low_content":0.024096385542168676,"disorder_content":0.5542168674698795,"disprot_consensus":{"full":[{"start":38,"end":57,"type":"D"},{"start":58,"end":83,"type":"T"}],"Structural state":[{"start":38,"end":83,"type":"D"}],"Structural transition":[{"start":58,"end":83,"type":"T"}],"Molecular function":[{"start":50,"end":83,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02416","name":"mttA/Hcf106 family","start":3,"end":45}]},"uniref50":"UniRef50_P69430","sequence":"MGGISIWQLLIIAVIVVLLFGTKKLGSIGSDLGASIKGFKKAMSDDEPKQDKTSQDADFTAKTIADKQADTNQEQAKTEDAKRHDKEQV","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P69430","disprot_id":"DP00834","ncbi_taxon_id":83333,"regions_counter":15,"creator":"tlazar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":89,"region_id":"DP00834r001","released":"2024_06","ec_id":"ECO:0006204","reference_html":"Characterization and membrane assembly of the TatA component of the Escherichia coli twin-arginine protein transport system. <i> Porcelli I, de Leeuw E, Wallis R, van den Brink-van der Laan E, de Kruijff B, Wallace BA, Palmer T, Berks BC. </i> Biochemistry, 2002","term_id":"IDPO:0000002","curator_id":"tlazar","start":21,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2023-09-28T17:29:31.726Z","reference_source":"pmid","term_name":"disorder","reference_id":"12427031","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Plasmid pFAT584 ( 12) was used for the overproduction of TatA with a carboxy-terminal hexahistidine tag, and plasmid pFAT587 ( 12) was used for the overproduction of a variant TatA protein (designated ΔTMS-TatA) in which the predicted amino-terminal transmembrane helix is replaced with a hexahistidine sequence."}]}],"statement":[{"text":"An expressed construct without the transmembrane segment is largely unstructured in aqueous solution but is able to insert into phospholipid monolayers and interacts with membrane bilayers.","type":"Abstract"},{"text":"Secondary structure analysis suggests that 80% of the polypeptide is in an “other” conformation which is usually indicative of an unfolded protein.","type":"Results"},{"text":"CD spectroscopy indicates that membrane association of the ΔTMS-TatA fragment induces some α-helix formation in this otherwise unstructured protein (Figure 5B).","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:31:02.821Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":89,"term_name":"lipid binding","released":"2024_06","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Characterization and membrane assembly of the TatA component of the Escherichia coli twin-arginine protein transport system. <i> Porcelli I, de Leeuw E, Wallis R, van den Brink-van der Laan E, de Kruijff B, Wallace BA, Palmer T, Berks BC. </i> Biochemistry, 2002","term_id":"GO:0008289","curator_id":"tlazar","start":21,"term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"12427031","version":4,"curator_orcid":"0000-0001-7496-6711","date":"2023-09-28T17:33:21.990Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00834r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Plasmid pFAT584 ( 12) was used for the overproduction of TatA with a carboxy-terminal hexahistidine tag, and plasmid pFAT587 ( 12) was used for the overproduction of a variant TatA protein (designated ΔTMS-TatA) in which the predicted amino-terminal transmembrane helix is replaced with a hexahistidine sequence."}]}],"statement":[{"text":"An expressed construct without the transmembrane segment is largely unstructured in aqueous solution but is able to insert into phospholipid monolayers and interacts with membrane bilayers.","type":"Abstract"},{"text":"The CD spectrum of ΔTMS-TatA in the presence of liposomes is clearly significantly changed from that of the protein alone, with the appearance of a peak at approximately 224 nm indicating helix formation (Figure 5B). This experiment demonstrates that ΔTMS-TatA interacts with membrane bilayers as well as monolayers. Secondary structure analysis shows that the liposomes increase the proportion of ΔTMS-TatA that is in an α-helical conformation and correspondingly reduce the number of “unfolded” residues (Table 1).","type":"Results"},{"text":"CD spectroscopy indicates that membrane association of the ΔTMS-TatA fragment induces some α-helix formation in this otherwise unstructured protein (Figure 5B).","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:30:18.396Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":44,"region_id":"DP00834r004","released":"2024_06","ec_id":"ECO:0006204","reference_html":"Towards understanding the Tat translocation mechanism through structural and biophysical studies of the amphipathic region of TatA from Escherichia coli. <i> Chan CS, Haney EF, Vogel HJ, Turner RJ. </i> Biochim Biophys Acta, 2011","term_id":"IDPO:0000002","curator_id":"tlazar","start":22,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2023-09-28T17:46:13.343Z","reference_source":"pmid","term_name":"disorder","reference_id":"21683683","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"A far-UV CD spectrum of TatAH2 showed that the peptide is relatively unstructured in aqueous buffer and with a low concentration (0.25 mM lipid) of small unilamellar vesicles (SUVs) made of E. coli polar lipids.","type":"Results"},{"text":"These observations suggest that the peptide is mostly unstructured in aqueous solution, but that it adopts a helical structure when placed in a membrane mimetic environment such as stable SUVs or detergent micelles.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:25:54.488Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":44,"term_name":"disorder to order","released":"2024_12","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Towards understanding the Tat translocation mechanism through structural and biophysical studies of the amphipathic region of TatA from Escherichia coli. <i> Chan CS, Haney EF, Vogel HJ, Turner RJ. </i> Biochim Biophys Acta, 2011","term_id":"IDPO:0000011","curator_id":"tlazar","start":22,"term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"21683683","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2023-09-28T17:45:33.585Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00834r005","ec_go":"EXP","disprot_namespace":"Structural transition","statement":[{"text":"A far-UV CD spectrum of TatAH2 showed that the peptide is relatively unstructured in aqueous buffer and with a low concentration (0.25 mM lipid) of small unilamellar vesicles (SUVs) made of E. coli polar lipids. However, the shape of the CD spectra in the presence of SUVs is not identical to that of the peptide in buffer, suggesting a slight difference in its secondary structure. In the presence of higher concentration E. coli SUVs, DPC and SDS micelles, and 50% trifluoroethanol, the CD spectra change to what is highly indicative of α-helical structure (Fig. 2). The vesicles generated at the low 0.25 mM lipid concentration are likely unstable and may contribute to the lack of secondary structure observed for TatAH2. These observations suggest that the peptide is mostly unstructured in aqueous solution, but that it adopts a helical structure when placed in a membrane mimetic environment such as stable SUVs or detergent micelles.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-31T16:24:22.341Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":44,"term_name":"lipid binding","released":"2024_06","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Towards understanding the Tat translocation mechanism through structural and biophysical studies of the amphipathic region of TatA from Escherichia coli. <i> Chan CS, Haney EF, Vogel HJ, Turner RJ. </i> Biochim Biophys Acta, 2011","term_id":"GO:0008289","curator_id":"tlazar","start":22,"term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"21683683","version":4,"curator_orcid":"0000-0001-7496-6711","date":"2023-09-28T17:45:05.820Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00834r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"statement":[{"text":"A far-UV CD spectrum of TatAH2 showed that the peptide is relatively unstructured in aqueous buffer and with a low concentration (0.25 mM lipid) of small unilamellar vesicles (SUVs) made of E. coli polar lipids. However, the shape of the CD spectra in the presence of SUVs is not identical to that of the peptide in buffer, suggesting a slight difference in its secondary structure. In the presence of higher concentration E. coli SUVs, DPC and SDS micelles, and 50% trifluoroethanol, the CD spectra change to what is highly indicative of α-helical structure (Fig. 2). The vesicles generated at the low 0.25 mM lipid concentration are likely unstable and may contribute to the lack of secondary structure observed for TatAH2. These observations suggest that the peptide is mostly unstructured in aqueous solution, but that it adopts a helical structure when placed in a membrane mimetic environment such as stable SUVs or detergent micelles.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:30:13.850Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":89,"region_id":"DP00834r010","released":"2024_06","ec_id":"ECO:0006204","reference_html":"Towards understanding the Tat translocation mechanism through structural and biophysical studies of the amphipathic region of TatA from Escherichia coli. <i> Chan CS, Haney EF, Vogel HJ, Turner RJ. </i> Biochim Biophys Acta, 2011","term_id":"IDPO:0000002","curator_id":"tlazar","start":44,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2023-09-28T17:48:05.424Z","reference_source":"pmid","term_name":"disorder","reference_id":"21683683","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"In contrast, a synthetic peptide representing the C-terminal region (residues 44 to 89 of TatA), displayed a lack of secondary structure with all these membrane mimetics except in the presence of SDS, which showed induction of some helical structure (Supplementary Fig. 1).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:25:40.577Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":89,"region_id":"DP00834r011","released":"2024_06","ec_id":"ECO:0006165","reference_html":"Structural basis for TatA oligomerization: an NMR study of Escherichia coli TatA dimeric structure. <i> Zhang Y, Hu Y, Li H, Jin C. </i> PLoS One, 2014","term_id":"IDPO:0000002","curator_id":"tlazar","start":47,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2023-09-28T18:02:45.809Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2MN6"},{"db":"PDB","id":"2MN7"}],"reference_id":"25090434","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Secondary structural analysis by consensus chemical shifts\nindex (CSI) demonstrates that the protein comprises two helices in\nthe N-terminal region and an unstructured C-terminus (Figure S2\nin File S1) [27,28], which is in accordance with previously\nreported TatA structures [10,12].","type":"Results"},{"text":"As shown in Figure 4A, the structure of the monomeric E. coli\nTatA consists of a 15-residue TMH (residues Ile6-Phe20), a 21-\nresidue APH (residues Lys24-Met43) and a mostly unstructured C-\nterminal region.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:36:19.759Z"}},{"start":22,"end":44,"reference_id":"21683683","reference_source":"pmid","reference_html":"Towards understanding the Tat translocation mechanism through structural and biophysical studies of the amphipathic region of TatA from Escherichia coli. <i> Chan CS, Haney EF, Vogel HJ, Turner RJ. </i> Biochim Biophys Acta, 2011","date":"2023-09-28T17:51:43.923Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP00834r012","statement":[{"text":"The two-dimensional NOESY spectrum of TatAH2 in aqueous\nsolution did not indicate the presence of a well defined peptide\nstructure due to the lack of observable inter-residue nOe cross peaks,\npoor peak dispersion, and a low number of peaks in general (not\nshown). This demonstrates that TatAH2 is essentially unstructured in\nwater, consistent with the results from the CD experiments in\naqueous buffer.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:25:20.356Z"}},{"start":22,"end":44,"reference_id":"21683683","reference_source":"pmid","reference_html":"Towards understanding the Tat translocation mechanism through structural and biophysical studies of the amphipathic region of TatA from Escherichia coli. <i> Chan CS, Haney EF, Vogel HJ, Turner RJ. </i> Biochim Biophys Acta, 2011","date":"2023-09-28T17:54:35.881Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP00834r013","statement":[{"text":"Spectra for the peptide in the presence of SDS micelles were\nacquired at 25, 30, and 37 °C on a 600 and 700 MHz spectrometer to\nobtain fully resolved cross-peaks. The final conditions yielding well\nresolved spectra were 1.43 mM peptide in 200 mM SDS, 100 mM NaCl\nat 37 °C (Fig. 5 and Supplementary Fig. 3). The solution structure of\nTatAH2 bound to SDS micelles at 37 °C is shown in Fig. 6. The peptide\nadopts a predominantly helical conformation consistent with the\nstructural motif suggested by CD spectroscopy.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-31T16:24:10.878Z"}},{"start":22,"end":44,"reference_id":"21683683","reference_source":"pmid","reference_html":"Towards understanding the Tat translocation mechanism through structural and biophysical studies of the amphipathic region of TatA from Escherichia coli. <i> Chan CS, Haney EF, Vogel HJ, Turner RJ. </i> Biochim Biophys Acta, 2011","date":"2023-09-28T17:55:49.078Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","region_id":"DP00834r014","statement":[{"text":"Spectra for the peptide in the presence of SDS micelles were\nacquired at 25, 30, and 37 °C on a 600 and 700 MHz spectrometer to\nobtain fully resolved cross-peaks. The final conditions yielding well\nresolved spectra were 1.43 mM peptide in 200 mM SDS, 100 mM NaCl\nat 37 °C (Fig. 5 and Supplementary Fig. 3). The solution structure of\nTatAH2 bound to SDS micelles at 37 °C is shown in Fig. 6. The peptide\nadopts a predominantly helical conformation consistent with the\nstructural motif suggested by CD spectroscopy.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:30:04.996Z"}}],"released":"2016_10","uniref100":"UniRef100_P69430","date":"2016-08-24T11:22:35.000Z","acc":"P69428","name":"Sec-independent protein translocase protein TatA","length":89,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI00000540BA","genes":[{"name":{"value":"tatA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00236","url":"https://hamap.expasy.org/unirule/MF_00236"}}]},"synonyms":[{"value":"mttA1"},{"value":"yigT"}],"olnNames":[{"value":"b3836"},{"value":"JW3813"}]}],"alphafold_very_low_content":0,"disorder_content":0.7752808988764045,"disprot_consensus":{"full":[{"start":21,"end":21,"type":"D"},{"start":22,"end":44,"type":"T"},{"start":45,"end":89,"type":"D"}],"Structural state":[{"start":21,"end":89,"type":"D"}],"Molecular function":[{"start":21,"end":89,"type":"F"}],"Structural transition":[{"start":22,"end":44,"type":"T"}]}},{"features":{"pfam":[{"id":"PF04051","name":"Transport protein particle (TRAPP) component","start":62,"end":271}],"gene3D":[{"start":144,"end":283,"id":"3.30.1380.20","name":"Trafficking protein particle complex subunit 3"},{"start":55,"end":121,"id":"3.30.1380.20","name":"Trafficking protein particle complex subunit 3"}]},"uniref50":"UniRef50_Q03337","sequence":"MSQRIIQPSASDQQFPGKSDGYEYTVGPKQAITSEASTTYIPSRIYSESLLFKRQEASLSAMAFLFQEMISQLHRTCKTAGDFETKLSDYGHNIGIRLLELLNFRASVSPSSLPRASAFLSQNESSSKLSNASNSPGMLANSSTATSASANERLQEKQTESLSNYITKMRRRDLKILDILQFIHGTLWSYLFNHVSDDLVKSSERDNEYMIVDNFPTLTQFIPGENVSCEYFVCGIIKGFLFNAGFPCGVTAHRMPQGGHSQRTVYLIQFDRQVLDREGLRFG","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q03337","disprot_id":"DP00835","ncbi_taxon_id":559292,"regions_counter":2,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":54,"region_id":"DP00835r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The structural basis for activation of the Rab Ypt1p by the TRAPP membrane-tethering complexes. <i> Cai Y, Chin HF, Lazarova D, Menon S, Fu C, Cai H, Sclafani A, Rodgers DW, De La Cruz EM, Ferro-Novick S, Reinisch KM. </i> Cell, 2008","term_id":"IDPO:0000002","curator_id":"nmurvai","start":1,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"18585354","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3CUE"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":164,"region_id":"DP00835r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The structural basis for activation of the Rab Ypt1p by the TRAPP membrane-tethering complexes. <i> Cai Y, Chin HF, Lazarova D, Menon S, Fu C, Cai H, Sclafani A, Rodgers DW, De La Cruz EM, Ferro-Novick S, Reinisch KM. </i> Cell, 2008","term_id":"IDPO:0000002","curator_id":"nmurvai","start":104,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"18585354","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3CUE"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q03337","date":"2016-08-24T20:07:08.000Z","acc":"Q03337","name":"Trafficking protein particle complex subunit 31","length":283,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000052E1B","genes":[{"name":{"value":"TRS31"},"olnNames":[{"value":"YDR472W"}]}],"alphafold_very_low_content":0.2756183745583039,"disorder_content":0.40636042402826855,"disprot_consensus":{"full":[{"start":1,"end":54,"type":"D"},{"start":104,"end":164,"type":"D"}],"Structural state":[{"start":1,"end":54,"type":"D"},{"start":104,"end":164,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00243","name":"Nerve growth factor family","start":132,"end":239}],"gene3D":[{"start":122,"end":241,"id":"2.10.90.10","name":"Cystine-knot cytokines"}]},"uniref50":"UniRef50_P01139","sequence":"MSMLFYTLITAFLIGVQAEPYTDSNVPEGDSVPEAHWTKLQHSLDTALRRARSAPTAPIAARVTGQTRNITVDPRLFKKRRLHSPRVLFSTQPPPTSSDTLDLDFQAHGTIPFNRTHRSKRSSTHPVFHMGEFSVCDSVSVWVGDKTTATDIKGKEVTVLAEVNINNSVFRQYFFETKCRASNPVESGCRGIDSKHWNSYCTTTHTFVKALTTDEKQAAWRFIRIDTACVCVLSRKATRRG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P01139","disprot_id":"DP00836","ncbi_taxon_id":10090,"regions_counter":1,"creator":"mmacossay","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":128,"region_id":"DP00836r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Molecular and structural insight into proNGF engagement of p75NTR and sortilin. <i> Feng D, Kim T, Ozkan E, Light M, Torkin R, Teng KK, Hempstead BL, Garcia KC. </i> J Mol Biol, 2010","term_id":"IDPO:0000002","curator_id":"mmacossay","start":19,"term_ontology":"IDPO","curator_name":"Mauricio Macossay-Castillo","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3IJ2"}],"reference_id":"20036257","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P01139","date":"2016-08-24T20:36:17.000Z","acc":"P01139","name":"Beta-nerve growth factor","length":241,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000022D09","genes":[{"name":{"value":"Ngf"},"synonyms":[{"value":"Ngfb"}]}],"alphafold_very_low_content":0.22406639004149378,"disorder_content":0.45643153526970953,"disprot_consensus":{"full":[{"start":19,"end":128,"type":"D"}],"Structural state":[{"start":19,"end":128,"type":"D"}]}},{"features":{"pfam":[{"id":"PF04683","name":"Proteasome complex subunit Rpn13, Pru domain","start":23,"end":121},{"id":"PF16550","name":"UCH-binding domain","start":268,"end":381}],"gene3D":[{"start":267,"end":387,"id":"3.40.190.140","name":"3.40.190.140"},{"start":22,"end":130,"id":"2.30.29.70","name":"Proteasomal ubiquitin receptor Rpn13/ADRM1"}]},"uniref50":"UniRef50_Q16186","sequence":"MTTSGALFPSLVPGSRGASNKYLVEFRAGKMSLKGTTVTPDKRKGLVYIQQTDDSLIHFCWKDRTSGNVEDDLIIFPDDCEFKRVPQCPSGRVYVLKFKAGSKRLFFWMQEPKTDQDEEHCRKVNEYLNNPPMPGALGASGSSGHELSALGGEGGLQSLLGNMSHSQLMQLIGPAGLGGLGGLGALTGPGLASLLGSSGPPGSSSSSSSRSQSAAVTPSSTTSSTRATPAPSAPAAASATSPSPAPSSGNGASTAASPTQPIQLSDLQSILATMNVPAGPAGGQQVDLASVLTPEIMAPILANADVQERLLPYLPSGESLPQTADEIQNTLTSPQFQQALGMFSAALASGQLGPLMCQFGLPAEAVEAANKGDVEAFAKAMQNNAKPEQKEGDTKDKKDEEEDMSLD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q16186","disprot_id":"DP00839","ncbi_taxon_id":9606,"regions_counter":8,"creator":"zdosztanyi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":21,"region_id":"DP00839r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2. <i> Chen X, Lee BH, Finley D, Walters KJ. </i> Mol Cell, 2010","term_id":"IDPO:0000002","curator_id":"zdosztanyi","start":1,"term_ontology":"IDPO","curator_name":"Zsuzsanna Dosztányi","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2KR0"}],"reference_id":"20471946","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":252,"region_id":"DP00839r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2. <i> Chen X, Lee BH, Finley D, Walters KJ. </i> Mol Cell, 2010","term_id":"IDPO:0000002","curator_id":"zdosztanyi","start":132,"term_ontology":"IDPO","curator_name":"Zsuzsanna Dosztányi","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2KR0"}],"reference_id":"20471946","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":252,"term_name":"flexible linker","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2. <i> Chen X, Lee BH, Finley D, Walters KJ. </i> Mol Cell, 2010","term_id":"IDPO:0000033","curator_id":"zdosztanyi","start":132,"term_ontology":"IDPO","curator_name":"Zsuzsanna Dosztányi","reference_id":"20471946","version":3,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00839r003","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":407,"region_id":"DP00839r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2. <i> Chen X, Lee BH, Finley D, Walters KJ. </i> Mol Cell, 2010","term_id":"IDPO:0000002","curator_id":"zdosztanyi","start":386,"term_ontology":"IDPO","curator_name":"Zsuzsanna Dosztányi","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2KR0"}],"reference_id":"20471946","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":285,"region_id":"DP00839r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2. <i> Chen X, Lee BH, Finley D, Walters KJ. </i> Mol Cell, 2010","term_id":"IDPO:0000002","curator_id":"zdosztanyi","start":253,"term_ontology":"IDPO","curator_name":"Zsuzsanna Dosztányi","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2KQZ"}],"reference_id":"20471946","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":285,"term_name":"molecular function inhibitor activity","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2. <i> Chen X, Lee BH, Finley D, Walters KJ. </i> Mol Cell, 2010","term_id":"GO:0140678","curator_id":"zdosztanyi","start":253,"term_ontology":"GO","curator_name":"Zsuzsanna Dosztányi","reference_id":"20471946","version":3,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00839r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":285,"term_name":"order to disorder","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2. <i> Chen X, Lee BH, Finley D, Walters KJ. </i> Mol Cell, 2010","term_id":"IDPO:0000014","curator_id":"zdosztanyi","start":253,"term_ontology":"IDPO","curator_name":"Zsuzsanna Dosztányi","reference_id":"20471946","version":2,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00839r007","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":285,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2. <i> Chen X, Lee BH, Finley D, Walters KJ. </i> Mol Cell, 2010","term_id":"GO:0005515","curator_id":"zdosztanyi","start":253,"term_ontology":"GO","curator_name":"Zsuzsanna Dosztányi","reference_id":"20471946","version":3,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00839r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q16186","date":"2016-08-25T12:04:02.000Z","acc":"Q16186","name":"Proteasomal ubiquitin receptor ADRM1","length":407,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000016A952","genes":[{"name":{"value":"ADRM1"},"synonyms":[{"value":"GP110"}]}],"alphafold_very_low_content":0.3488943488943489,"disorder_content":0.48402948402948404,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"},{"start":132,"end":252,"type":"D"},{"start":253,"end":285,"type":"T"},{"start":386,"end":407,"type":"D"}],"Structural state":[{"start":1,"end":21,"type":"D"},{"start":132,"end":285,"type":"D"},{"start":386,"end":407,"type":"D"}],"Disorder function":[{"start":132,"end":252,"type":"F"}],"Molecular function":[{"start":253,"end":285,"type":"F"}],"Structural transition":[{"start":253,"end":285,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00036","name":"EF hand domain","start":56,"end":81},{"id":"PF13499","name":"EF-hand domain pair","start":89,"end":160}],"gene3D":[{"start":86,"end":173,"id":"1.10.238.10","name":"EF-hand"},{"start":12,"end":177,"id":"1.10.238.10","name":"EF-hand"}]},"uniref50":"UniRef50_P43080","sequence":"MGNIMDGKSVEELSSTECHQWYKKFMTECPSGQLTLYEFRQFFGLKNLSPWASQYVEQMFETFDFNKDGYIDFMEYVAALSLVLKGKVEQKLRWYFKLYDVDGNGCIDRDELLTIIRAIRAINPCSDSTMTAEEFTDTVFSKIDVNGDGELSLEEFMEGVQKDQMLLDTLTRSLDLTRIVRRLQNGEQDEEGASGRETEAAEADG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P46065","disprot_id":"DP00840","ncbi_taxon_id":9913,"regions_counter":7,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":18,"region_id":"DP00840r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Backbone (1)H, (13)C, and (15)N resonance assignments of guanylyl cyclase activating protein-1, GCAP1. <i> Lim S, Peshenko IV, Dizhoor AM, Ames JB. </i> Biomol NMR Assign, 2013","term_id":"IDPO:0000002","curator_id":"bszabo","start":1,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"22392341","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"18026"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":205,"region_id":"DP00840r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Backbone (1)H, (13)C, and (15)N resonance assignments of guanylyl cyclase activating protein-1, GCAP1. <i> Lim S, Peshenko IV, Dizhoor AM, Ames JB. </i> Biomol NMR Assign, 2013","term_id":"IDPO:0000002","curator_id":"bszabo","start":187,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"22392341","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"18026"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":108,"region_id":"DP00840r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of Guanylyl Cyclase Activator Protein 1 (GCAP1) Mutant V77E in a Ca2+-free/Mg2+-bound Activator State. <i> Lim S, Peshenko IV, Olshevskaya EV, Dizhoor AM, Ames JB. </i> J Biol Chem, 2016","term_id":"IDPO:0000002","curator_id":"bszabo","start":74,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"26703466","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2NA0"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":129,"region_id":"DP00840r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of Guanylyl Cyclase Activator Protein 1 (GCAP1) Mutant V77E in a Ca2+-free/Mg2+-bound Activator State. <i> Lim S, Peshenko IV, Olshevskaya EV, Dizhoor AM, Ames JB. </i> J Biol Chem, 2016","term_id":"IDPO:0000002","curator_id":"bszabo","start":119,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"26703466","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2NA0"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P46065","date":"2016-08-25T14:00:11.000Z","acc":"P46065","name":"Guanylyl cyclase-activating protein 1","length":205,"organism":"Bos taurus","dataset":[],"UniParc":"UPI0000167C2B","genes":[{"name":{"value":"GUCA1A"},"synonyms":[{"value":"GCAP1"},{"value":"GUCA1"}]}],"alphafold_very_low_content":0.16585365853658537,"disorder_content":0.40487804878048783,"disprot_consensus":{"full":[{"start":1,"end":18,"type":"D"},{"start":74,"end":108,"type":"D"},{"start":119,"end":129,"type":"D"},{"start":187,"end":205,"type":"D"}],"Structural state":[{"start":1,"end":18,"type":"D"},{"start":74,"end":108,"type":"D"},{"start":119,"end":129,"type":"D"},{"start":187,"end":205,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":122,"end":380}],"gene3D":[{"start":200,"end":403,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"},{"start":102,"end":199,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"}]},"uniref50":"UniRef50_O14733","sequence":"MAASSLEQKLSRLEAKLKQENREARRRIDLNLDISPQRPRPTLQLPLANDGGSRSPSSESSPQHPTPPARPRHMLGLPSTLFTPRSMESIEIDQKLQEIMKQTGYLTIGGQRYQAEINDLENLGEMGSGTCGQVWKMRFRKTGHVIAVKQMRRSGNKEENKRILMDLDVVLKSHDCPYIVQCFGTFITNTDVFIAMELMGTCAEKLKKRMQGPIPERILGKMTVAIVKALYYLKEKHGVIHRDVKPSNILLDERGQIKLCDFGISGRLVDSKAKTRSAGCAAYMAPERIDPPDPTKPDYDIRADVWSLGISLVELATGQFPYKNCKTDFEVLTKVLQEEPPLLPGHMGFSGDFQSFVKDCLTKDHRKRPKYNKLLEHSFIKRYETLEVDVASWFKDVMAKTESPRTSGVLSQPHLPFFR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O14733","disprot_id":"DP00841","ncbi_taxon_id":9606,"regions_counter":8,"creator":"ameszaros","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":100,"region_id":"DP00841r001","released":"2025_12","ec_id":"ECO:0006165","reference_html":"Structure and dynamics of the MKK7-JNK signaling complex. <i> Kragelj J, Palencia A, Nanao MH, Maurin D, Bouvignies G, Blackledge M, Jensen MR. </i> Proc Natl Acad Sci U S A, 2015","term_id":"IDPO:0000002","curator_id":"vnugnes","start":30,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"25737554","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2025-10-16T14:08:47.573Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The 13Cα secondary chemical shifts reveal that MKK7 contains helical propensity at its N terminus (residues 5–30), whereas the remaining residues have secondary chemical shifts close to zero indicating a near random coil state (Fig. 1C).","type":"Results"}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":82,"term_name":"mitogen-activated protein kinase binding","start":70,"ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2025_12","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"25737554","version":4,"reference_html":"Structure and dynamics of the MKK7-JNK signaling complex. <i> Kragelj J, Palencia A, Nanao MH, Maurin D, Bouvignies G, Blackledge M, Jensen MR. </i> Proc Natl Acad Sci U S A, 2015","date":"2025-10-16T14:30:26.810Z","term_id":"GO:0051019","ec_id":"ECO:0005642","region_id":"DP00841r003","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a mitogen-activated protein kinase.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P45983","operator":null,"partner_start":null,"partner_end":null}],"statement":[{"text":"The intensity profile of MKK7 shows a decrease in signal intensities localized at the three JNK1 docking sites with D2 and D3 showing the clearest binding signatures (Fig. 4B).","type":"Results"},{"text":"The analysis gives an exchange rate of 707 ± 34 s−1 and a population of bound MKK7 of 0.8%. Clear dispersion profiles are observed for the residues T80, L81, and F82 that are located outside the canonical D3 docking site (R70-L77), confirming their involvement in the binding of JNK1.","type":"Results"}]},{"start":25,"end":34,"reference_id":"25737554","reference_source":"pmid","reference_html":"Structure and dynamics of the MKK7-JNK signaling complex. <i> Kragelj J, Palencia A, Nanao MH, Maurin D, Bouvignies G, Blackledge M, Jensen MR. </i> Proc Natl Acad Sci U S A, 2015","date":"2025-10-16T14:30:00.509Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051019","term_name":"mitogen-activated protein kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P45983","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00841r004","statement":[{"text":"NMR experiments carried out by using a shorter construct of the regulatory domain containing only the D1 docking site demonstrate that D1 binds JNK1 under these conditions (Fig. S7).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a mitogen-activated protein kinase.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":36,"end":47,"reference_id":"25737554","reference_source":"pmid","reference_html":"Structure and dynamics of the MKK7-JNK signaling complex. <i> Kragelj J, Palencia A, Nanao MH, Maurin D, Bouvignies G, Blackledge M, Jensen MR. </i> Proc Natl Acad Sci U S A, 2015","date":"2025-10-16T14:26:18.155Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051019","term_name":"mitogen-activated protein kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P45983","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00841r005","statement":[{"text":"The ITC measurements reveal that all docking sites bind with similar affinity in the low micromolar range with D2 (Kd = 7.9 μM) as the strongest binder followed by D3 (Kd = 11 μM) and D1 (Kd = 12 μM) (Fig. 3 A–C).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a mitogen-activated protein kinase.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":69,"end":78,"reference_id":"25737554","reference_source":"pmid","reference_html":"Structure and dynamics of the MKK7-JNK signaling complex. <i> Kragelj J, Palencia A, Nanao MH, Maurin D, Bouvignies G, Blackledge M, Jensen MR. </i> Proc Natl Acad Sci U S A, 2015","date":"2025-10-16T14:20:05.180Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051019","term_name":"mitogen-activated protein kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P45983","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00841r006","statement":[{"text":"The ITC measurements reveal that all docking sites bind with similar affinity in the low micromolar range with D2 (Kd = 7.9 μM) as the strongest binder followed by D3 (Kd = 11 μM) and D1 (Kd = 12 μM) (Fig. 3 A–C).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a mitogen-activated protein kinase.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":38,"end":47,"reference_id":"25737554","reference_source":"pmid","reference_html":"Structure and dynamics of the MKK7-JNK signaling complex. <i> Kragelj J, Palencia A, Nanao MH, Maurin D, Bouvignies G, Blackledge M, Jensen MR. </i> Proc Natl Acad Sci U S A, 2015","date":"2025-10-16T14:33:05.199Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051019","term_name":"mitogen-activated protein kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P45983","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00841r007","statement":[{"text":"The intensity profile of MKK7 shows a decrease in signal intensities localized at the three JNK1 docking sites with D2 and D3 showing the clearest binding signatures (Fig. 4B).","type":"Results"},{"text":"These observations suggest that the residues L43, L45, and L47 function as anchors of the docking site, whereas the charged residues R38 and R40 establish less well-defined contacts with the surface of JNK1.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a mitogen-activated protein kinase.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":37,"end":48,"reference_id":"25737554","reference_source":"pmid","reference_html":"Structure and dynamics of the MKK7-JNK signaling complex. <i> Kragelj J, Palencia A, Nanao MH, Maurin D, Bouvignies G, Blackledge M, Jensen MR. </i> Proc Natl Acad Sci U S A, 2015","date":"2025-10-16T14:41:49.475Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051019","term_name":"mitogen-activated protein kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P45983","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00841r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"33113"}],"statement":[{"text":"Interestingly, an alternative binding mode is observed in subunit D, where R40 contacts D326 and E329 on the surface of JNK1 and P41, L45, and L47 occupy the three pockets, resulting in increased flexibility at the level of T42 and L43 and consequently missing electron density for these two residues (Fig. 5 G and H).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a mitogen-activated protein kinase.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"cross_refs":[{"db":"PDB","id":"4UX9"}]}],"released":"2016_10","uniref100":"UniRef100_O14733","date":"2016-08-25T14:29:21.000Z","acc":"O14733","name":"Dual specificity mitogen-activated protein kinase kinase 7","length":419,"organism":"Homo sapiens","dataset":["Autophagy-related proteins","Stress response proteins"],"UniParc":"UPI0000169679","genes":[{"name":{"value":"MAP2K7"},"synonyms":[{"value":"JNKK2"},{"value":"MEK7"},{"value":"MKK7"},{"value":"PRKMK7"},{"value":"SKK4"}]}],"alphafold_very_low_content":0.20286396181384247,"disorder_content":0.16945107398568018,"disprot_consensus":{"full":[{"start":25,"end":29,"type":"F"},{"start":30,"end":100,"type":"D"}],"Structural state":[{"start":30,"end":100,"type":"D"}],"Molecular function":[{"start":25,"end":34,"type":"F"},{"start":36,"end":48,"type":"F"},{"start":69,"end":82,"type":"F"}]}},{"acc":"P12506","sequence":"MDPVDPNIEPWNHPGSQPKTACNRCHCKKCCYHCQVCFITKGLGISYGRKKRRQRRRPSQGGQTHQDPIPKQPSSQPRGDPTGPKE","creator":"bszabo","dataset":["Viral proteins","RNA-binding proteins"],"date":"2016-08-25T15:01:35.000Z","disprot_id":"DP00842","features":{"pfam":[{"id":"PF00539","name":"Transactivating regulatory protein (Tat)","start":3,"end":64}],"gene3D":[{"start":1,"end":86,"id":"4.10.20.10","name":"Tat domain","_id":"685af523b4ac24d5329d8616"}]},"genes":[{"name":{"value":"tat","evidences":[{"source":{"id":"MF_04079","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04079","_id":"685af523b4ac24d5329d863c"},"code":"ECO:0000255","_id":"685af523b4ac24d5329d863b"}],"_id":"685af523b4ac24d5329d863d"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d863a"}],"length":86,"name":"Protein Tat","ncbi_taxon_id":11683,"organism":"Human immunodeficiency virus type 1 group M subtype D (isolate Z2/CDC-Z34)","regions_counter":15,"released":"2016_10","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"UniParc":"UPI0000136938","uniref100":"UniRef100_P12506","uniref50":"UniRef50_P12506","uniref90":"UniRef90_P12506","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":86,"interaction_partner":[],"reference_html":"Full peptide synthesis, purification, and characterization of six Tat variants. Differences observed between HIV-1 isolates from Africa and other continents. <i> Péloponèse JM, Collette Y, Grégoire C, Bailly C, Campèse D, Meurs EF, Olive D, Loret EP. </i> J Biol Chem, 1999","reference_id":"10206951","region_id":"DP00842r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In aqueous buffer (Fig. 4 A), it can be deduced from the intensity of the negative 200 nm band that nonorganized structures are predominant (29). TableI reveals that there is no α helix in aqueous buffer excepted for Tat Mal and Tat Z2, which could have a short helix of eight to nine residues.","_id":"685af523b4ac24d5329d8630"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T12:58:29.734Z","_id":"685af523b4ac24d5329d8631"},"version":1,"_id":"685af523b4ac24d5329d862f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001807","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":86,"interaction_partner":[{"db":"RNAcentral","id":"URS000071DF2D_576904","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8633"}],"reference_html":"Full peptide synthesis, purification, and characterization of six Tat variants. Differences observed between HIV-1 isolates from Africa and other continents. <i> Péloponèse JM, Collette Y, Grégoire C, Bailly C, Campèse D, Meurs EF, Olive D, Loret EP. </i> J Biol Chem, 1999","reference_id":"10206951","region_id":"DP00842r014","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The six synthetic Tat proteins can bind to TAR RNA (Fig.3) and can inhibit PKR (data not shown).","_id":"685af523b4ac24d5329d8634"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a RNA region that regulates a nucleic acid-based process. Such processes include transcription, DNA replication, and DNA repair.\" [GOC:txnOH]","term_go_domain":"F","term_id":"GO:0001069","term_is_binding":true,"term_is_obsolete":false,"term_name":"regulatory region RNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T12:58:36.249Z","_id":"685af523b4ac24d5329d8635"},"version":1,"_id":"685af523b4ac24d5329d8632","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IEP","ec_id":"ECO:0005616","ec_name":"beta-galactosidase reporter gene assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":86,"interaction_partner":[],"reference_html":"Full peptide synthesis, purification, and characterization of six Tat variants. Differences observed between HIV-1 isolates from Africa and other continents. <i> Péloponèse JM, Collette Y, Grégoire C, Bailly C, Campèse D, Meurs EF, Olive D, Loret EP. </i> J Biol Chem, 1999","reference_id":"10206951","region_id":"DP00842r015","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In each case, Tat was added to the cell buffer, and therefore expression of β-gal up to the control means that the synthetic Tat was able to cross the cytoplasmic and nucleus membranes, bind TAR, and interact with cellular cofactors.","_id":"685af523b4ac24d5329d8637"},{"type":"Curator statement","text":"The authors show an increase in β-galactosidase expression through a transactivation assay with HeLa cells transfected with a LTR HIV-1 β-gal plasmid and purified TAT protein.","_id":"685af523b4ac24d5329d8638"}],"states_connection":[],"term_comment":"","term_def":"\"A process by which a viral gene is converted into a mature gene product or products (proteins or RNA). This includes viral transcription, processing to produce a mature RNA product, and viral translation.\" [GOC:bf, GOC:jl, ISBN:0121585336]","term_go_domain":"P","term_id":"GO:0019080","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral gene expression","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T12:58:45.356Z","_id":"685af523b4ac24d5329d8639"},"version":1,"_id":"685af523b4ac24d5329d8636","reference_source":"pmid"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":86,"type":"D"}],"Structural state":[{"start":1,"end":86,"type":"D"}],"Molecular function":[{"start":1,"end":86,"type":"F"}],"Biological process":[{"start":1,"end":86,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04568","name":"Mitochondrial ATPase inhibitor, IATP","start":21,"end":94}],"gene3D":[{"start":73,"end":109,"id":"1.20.5.500","name":"Single helix bin"},{"start":26,"end":72,"id":"1.20.5.500","name":"Single helix bin"}]},"uniref50":"UniRef50_P01096","sequence":"MAATALAARTRQAVWSVWAMQGRGFGSESGDNVRSSAGAVRDAGGAFGKREQAEEERYFRARAKEQLAALKKHHENEISHHAKEIERLQKEIERHKQSIKKLKQSEDDD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P01096","disprot_id":"DP00844","ncbi_taxon_id":9913,"regions_counter":1,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":18,"region_id":"DP00844r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The structure of bovine IF(1), the regulatory subunit of mitochondrial F-ATPase. <i> Cabezón E, Runswick MJ, Leslie AG, Walker JE. </i> EMBO J, 2001","term_id":"IDPO:0000002","curator_id":"eschad","start":1,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1GMJ"}],"reference_id":"11742976","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P01096","date":"2016-08-25T16:41:17.000Z","acc":"P01096","name":"ATPase inhibitor, mitochondrial","length":109,"organism":"Bos taurus","dataset":[],"UniParc":"UPI000017329D","genes":[{"name":{"value":"ATP5IF1","evidences":[{"code":"ECO:0000250","source":{"name":"UniProtKB","id":"Q9UII2","url":"https://www.uniprot.org/uniprot/Q9UII2"}}]},"synonyms":[{"value":"ATPI"},{"value":"ATPIF1"}]}],"alphafold_very_low_content":0.14678899082568808,"disorder_content":0.1651376146788991,"disprot_consensus":{"full":[{"start":1,"end":18,"type":"D"}],"Structural state":[{"start":1,"end":18,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00428","name":"60s Acidic ribosomal protein","start":17,"end":106}],"gene3D":[{"start":1,"end":58,"id":"1.10.10.1410","name":"1.10.10.1410"}]},"uniref50":"UniRef50_P23632","sequence":"MKYLAAYALVGLSGGTPSKSAVEAVLKAAGVPVDPSRVDALFAEFAGKDFDTVCTEGKSKLVGGVTRPNAATASAPTAAAAASSGAAAPAAAAEEEEDDDMGFGLFD","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Trypanosoma","Schizotrypanum"],"uniref90":"UniRef90_P23632","disprot_id":"DP00845","ncbi_taxon_id":5693,"regions_counter":2,"creator":"ameszaros","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":107,"region_id":"DP00845r001","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Correlation between conformation and antibody binding: NMR structure of cross-reactive peptides from T. cruzi, human and L. braziliensis. <i> Soares MR, Bisch PM, Campos de Carvalho AC, Valente AP, Almeida FC. </i> FEBS Lett, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":95,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14988012","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-09-16T14:44:49.039Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"EEEDDDMGFGLFD","statement":[{"text":"All peptides showed very poor NOESY spectra at 20°C (1-3).","type":"Results"},{"text":"Peptide R13 did not show any long-range NOE (more than four residues apart) and only two medium-range NOEs, suggesting that this peptide behaves as a random coil in solution, not showing any structural tendency.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:07:16.323Z"}}],"released":"2016_10","uniref100":"UniRef100_P23632","date":"2016-08-25T17:03:02.000Z","acc":"P23632","name":"60S acidic ribosomal protein P2-A","length":107,"organism":"Trypanosoma cruzi","dataset":["Neglected tropical diseases proteins"],"UniParc":"UPI0000134263","genes":[],"alphafold_very_low_content":0.308411214953271,"disorder_content":0.12149532710280374,"disprot_consensus":{"full":[{"start":95,"end":107,"type":"D"}],"Structural state":[{"start":95,"end":107,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03091","name":"CutA1 divalent ion tolerance protein","start":71,"end":166}],"gene3D":[{"start":63,"end":179,"id":"3.30.70.120","name":"3.30.70.120"}]},"uniref50":"UniRef50_O60888","sequence":"MSGGRAPAVLLGGVASLLLSFVWMPALLPVASRLLLLPRVLLTMASGSPPTQPSPASDSGSGYVPGSVSAAFVTCPNEKVAKEIARAVVEKRLAACVNLIPQITSIYEWKGKIEEDSEVLMMIKTQSSLVPALTDFVRSVHPYEVAEVIALPVEQGNFPYLQWVRQVTESVSDSITVLP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O60888","disprot_id":"DP00846","ncbi_taxon_id":9606,"regions_counter":2,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":60,"region_id":"DP00846r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of putative CutA1 from Homo sapiens determined at 2.05 A resolution. <i> Bagautdinov B, Matsuura Y, Bagautdinova S, Kunishima N, Yutani K. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2008","term_id":"IDPO:0000002","curator_id":"rdavidovic","start":45,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2ZFH"}],"reference_id":"18453701","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":179,"region_id":"DP00846r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of putative CutA1 from Homo sapiens determined at 2.05 A resolution. <i> Bagautdinov B, Matsuura Y, Bagautdinova S, Kunishima N, Yutani K. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2008","term_id":"IDPO:0000002","curator_id":"rdavidovic","start":170,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2ZFH"}],"reference_id":"18453701","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_O60888","date":"2016-08-26T09:05:38.000Z","acc":"O60888","name":"Protein CutA","length":179,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00004EAC91","genes":[{"name":{"value":"CUTA"},"synonyms":[{"value":"ACHAP"},{"value":"C6orf82"}]}],"alphafold_very_low_content":0.25139664804469275,"disorder_content":0.1452513966480447,"disprot_consensus":{"full":[{"start":45,"end":60,"type":"D"},{"start":170,"end":179,"type":"D"}],"Structural state":[{"start":45,"end":60,"type":"D"},{"start":170,"end":179,"type":"D"}]}},{"features":{"pfam":[{"id":"PF09645","name":"F-112 protein","start":3,"end":112}],"gene3D":[{"start":1,"end":73,"id":"1.10.10.1470","name":"F-112 protein-like"}]},"uniref50":"UniRef50_P20220","sequence":"MAQTLNSYKMAEIMYKILEKKGELTLEDILAQFEISVPSAYNIQRALKAICERHPDECEVQYKNRKTTFKWIKQEQKEEQKQEQTQDNIAKIFDAQPANFEQTDQGFIKAKQ","taxonomy":["Viruses","Fuselloviridae","Alphafusellovirus"],"uniref90":"UniRef90_P20220","disprot_id":"DP00847","ncbi_taxon_id":244589,"regions_counter":1,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":112,"region_id":"DP00847r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Cysteine usage in Sulfolobus spindle-shaped virus 1 and extension to hyperthermophilic viruses in general. <i> Menon SK, Maaty WS, Corn GJ, Kwok SC, Eilers BJ, Kraft P, Gillitzer E, Young MJ, Bothner B, Lawrence CM. </i> Virology, 2008","term_id":"IDPO:0000002","curator_id":"fquaglia","start":74,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2VQC"}],"reference_id":"18471851","statement":[{"text":"Interpretable electron density begins at the N-terminus with residue 4 of the native sequence and ends at residue 73. Residues 74 through 112 were not visible in the electron density, and accordingly not modelled.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-06T14:02:55.474Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P20220","date":"2016-08-26T09:51:26.000Z","acc":"P20220","name":"Protein F-112","length":112,"organism":"Sulfolobus spindle-shape virus 1","dataset":["Viral proteins"],"UniParc":"UPI000013934A","genes":[{"orfNames":[{"value":"f112"}]}],"disorder_content":0.3482142857142857,"disprot_consensus":{"full":[{"start":74,"end":112,"type":"D"}],"Structural state":[{"start":74,"end":112,"type":"D"}]}},{"features":{"pfam":[{"id":"PF05257","name":"CHAP domain","start":49,"end":128}],"gene3D":[{"start":42,"end":154,"id":"3.90.1720.10","name":"endopeptidase domain like (from Nostoc punctiforme)"}]},"uniref50":"UniRef50_A0A192F7U0","sequence":"MKKLVTATTLTAGIGAAIVGLDHGNEADAAEQTQPTNQSTTQSTSGSSANLYTAGQCTWYVYDKVGGNIGSTWGNANNWASAASSAGYTVNNSPEAGSILQSTAGGYGHVAYVENVNSDGSVEVSEMNYNGGPFSVSERTISAGEASSYNYIHLN","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Staphylococcaceae","Staphylococcus"],"uniref90":"UniRef90_A0A2C6U8Z0","disprot_id":"DP00848","ncbi_taxon_id":342451,"regions_counter":1,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":49,"region_id":"DP00848r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural elucidation of the Cys-His-Glu-Asn proteolytic relay in the secreted CHAP domain enzyme from the human pathogen Staphylococcus saprophyticus. <i> Rossi P, Aramini JM, Xiao R, Chen CX, Nwosu C, Owens LA, Maglaqui M, Nair R, Fischer M, Acton TB, Honig B, Rost B, Montelione GT. </i> Proteins, 2009","term_id":"IDPO:0000002","curator_id":"rdavidovic","start":1,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2K3A"}],"reference_id":"18951393","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_A0A380HKZ2","date":"2016-08-26T09:54:59.000Z","acc":"Q49ZM2","name":"Putative secretory antigen","length":155,"organism":"Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41)","dataset":[],"UniParc":"UPI0000589782","genes":[{"olnNames":[{"value":"SSP0609","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAE17754.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAE17754.1"}}]}]}],"alphafold_very_low_content":0.2903225806451613,"disorder_content":0.3161290322580645,"disprot_consensus":{"full":[{"start":1,"end":49,"type":"D"}],"Structural state":[{"start":1,"end":49,"type":"D"}]}},{"features":{"gene3D":[{"start":1,"end":102,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}],"pfam":[]},"uniref50":"UniRef50_A0A481NK40","sequence":"MTVIKPSSRPRPRKNKNIKVNTYRTSAMDLSPGSVHEGIVYFKDGIFKVRLLGYEGHECILLDYLNYRQDTLDRLKERLVGRVIKTRVVRADGLYVDLRRFF","taxonomy":["Viruses","Varidnaviria","Bamfordvirae","Nucleocytoviricota","Pokkesviricetes","Chitovirales","Poxviridae","Chordopoxvirinae","Leporipoxvirus"],"uniref90":"UniRef90_A0A481NK40","disprot_id":"DP00849","ncbi_taxon_id":31530,"regions_counter":3,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":32,"region_id":"DP00849r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Myxoma virus immunomodulatory protein M156R is a structural mimic of eukaryotic translation initiation factor eIF2alpha. <i> Ramelot TA, Cort JR, Yee AA, Liu F, Goshe MB, Edwards AM, Smith RD, Arrowsmith CH, Dever TE, Kennedy MA. </i> J Mol Biol, 2002","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1JJG"}],"reference_id":"12367520","statement":[{"text":"The structure contains 32 unstructured residues at the N terminus, one α-helix (residues 74–79) and five β-strands (residues 35–42, 47–50, 58–61, 83–91, and 95–99). The antiparallel β-strands are arranged in the order 3–2–1–4–5, with the first four strands in the Greek key topology.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-30T11:43:50.520Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":73,"region_id":"DP00849r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Myxoma virus immunomodulatory protein M156R is a structural mimic of eukaryotic translation initiation factor eIF2alpha. <i> Ramelot TA, Cort JR, Yee AA, Liu F, Goshe MB, Edwards AM, Smith RD, Arrowsmith CH, Dever TE, Kennedy MA. </i> J Mol Biol, 2002","term_id":"IDPO:0000002","curator_id":"fquaglia","start":62,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1JJG"}],"reference_id":"12367520","statement":[{"text":"Residues 62–73 of the loop preceding the α-helix had few structural restraints and this sequence therefore has a large variability in structural coordinates among the ensemble of structures.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-30T11:43:42.985Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":62,"end":73,"reference_id":"12367520","reference_source":"pmid","reference_html":"Myxoma virus immunomodulatory protein M156R is a structural mimic of eukaryotic translation initiation factor eIF2alpha. <i> Ramelot TA, Cort JR, Yee AA, Liu F, Goshe MB, Edwards AM, Smith RD, Arrowsmith CH, Dever TE, Kennedy MA. </i> J Mol Biol, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0001582","ec_ontology":"ECO","ec_name":"liquid chromatography coupled with tandem mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"1JJG"}],"region_id":"DP00849r003","statement":[{"text":"Liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis of in vitro phosphorylated M156R revealed that approximately 75% of the phosphorylation occurred in the peptide LLGYEGHECILLDYLNYR, which includes Y67. Fragmentation analysis indicated that Y54, Y64 or Y67 could be phosphorylated (data not shown).","type":"Results"}],"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":64,"end":64,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":67,"end":67,"position":"Specific residue"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-30T11:44:08.409Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_A0A481NK40","date":"2016-08-26T10:08:29.000Z","acc":"Q9Q8E9","name":"M156R","length":102,"organism":"Myxoma virus (strain Lausanne)","dataset":["Viral proteins"],"UniParc":"UPI00000F4C91","genes":[{"name":{"value":"m156R","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF15043.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF15043.1"}}]}}],"disorder_content":0.43137254901960786,"disprot_consensus":{"full":[{"start":1,"end":32,"type":"D"},{"start":62,"end":73,"type":"D"}],"Structural state":[{"start":1,"end":32,"type":"D"},{"start":62,"end":73,"type":"D"}],"Disorder function":[{"start":62,"end":73,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00589","name":"Phage integrase family","start":164,"end":308},{"id":"PF24624","name":"Phage integrase, N-terminal domain","start":57,"end":156}],"gene3D":[{"start":163,"end":337,"id":"1.10.443.10","name":"Intergrase catalytic core"}]},"uniref50":"UniRef50_P36932","sequence":"MAIKKLDDGRYEVDIRPTGRNGKRIRRKFDKKSEAVAFEKYTLYNHHNKEWLSKPTDKRRLSELTQIWWDLKGKHEEHGKSNLGKIEIFTKITNDPCAFQITKSLISQYCATRRSQGIKPSSINRDLTCISGMFTALIEAELFFGEHPIRGTKRLKEEKPETGYLTQEEIALLLAALDGDNKKIAILCLSTGARWGEAARLKAENIIHNRVTFVKTKTNKPRTVPISEAVAKMIADNKRGFLFPDADYPRFRRTMKAIKPDLPMGQATHALRHSFATHFMINGGSIITLQRILGHTRIEQTMVYAHFAPEYLQDAISLNPLRGGTEAESVHTVSTVE","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Uroviricota","Caudoviricetes","Caudovirales","Myoviridae","Peduovirinae","Peduovirus"],"uniref90":"UniRef90_P36932","disprot_id":"DP00850","ncbi_taxon_id":10679,"regions_counter":1,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":161,"region_id":"DP00850r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the bacteriophage P2 integrase catalytic domain. <i> Skaar K, Claesson M, Odegrip R, Högbom M, Haggård-Ljungquist E, Stenmark P. </i> FEBS Lett, 2015","term_id":"IDPO:0000002","curator_id":"fquaglia","start":46,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5C6K"}],"reference_id":"26453836","statement":[{"text":"The P2 Int45–337 construct used yielded crystals from which X-ray diffraction data to 1.9 Å was collected (see Table 1). However, the collected data only revealed electron density corresponding to the C-terminal catalytic domain of P2 Int.","type":"Results"},{"text":"The N-terminal arm-binding domain of λ is disordered in the crystal structure.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-15T12:04:36.230Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P36932","date":"2016-08-26T11:06:11.000Z","acc":"P36932","name":"Integrase","length":337,"organism":"Escherichia phage P2","dataset":["Viral proteins"],"UniParc":"UPI0000138837","genes":[{"name":{"value":"int"}}],"disorder_content":0.34421364985163205,"disprot_consensus":{"full":[{"start":46,"end":161,"type":"D"}],"Structural state":[{"start":46,"end":161,"type":"D"}]}},{"features":{"pfam":[{"id":"PF04896","name":"Ammonia monooxygenase/methane monooxygenase, subunit C","start":8,"end":248}],"gene3D":[{"start":1,"end":256,"id":"1.20.1050.50","name":"Particulate methane monooxygenase subunit c2. Chain: C"}]},"uniref50":"UniRef50_Q603F1","sequence":"MSVTTETTAGAAAGSDAIVDLRGMWVGVAGLNIFYLIVRIYEQIYGWRAGLDSFAPEFQTYWLSILWTEIPLELVSGLALAGWLWKTRDRNVDAVAPREELRRHVVLVEWLVVYAVAIYWGASFFTEQDGTWHMTVIRDTDFTPSHIIEFYMSYPIYSIMAVGAFFYAKTRIPYFAHGFSLAFLIVAIGPFMIIPNVGLNEWGHTFWFMEELFVAPLHWGFVFFGWMALGVFGVVLQILMGVKRLIGKDCVAALVG","taxonomy":["Bacteria","Proteobacteria","Alphaproteobacteria","Rhizobiales","Methylocystaceae","Methylosinus"],"uniref90":"UniRef90_A0A1A6FH42","disprot_id":"DP00851","ncbi_taxon_id":426,"regions_counter":2,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":256,"region_id":"DP00851r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The metal centers of particulate methane monooxygenase from Methylosinus trichosporium OB3b. <i> Hakemian AS, Kondapalli KC, Telser J, Hoffman BM, Stemmler TL, Rosenzweig AC. </i> Biochemistry, 2008","term_id":"IDPO:0000002","curator_id":"rdavidovic","start":177,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3CHX"}],"reference_id":"18540635","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":17,"region_id":"DP00851r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The metal centers of particulate methane monooxygenase from Methylosinus trichosporium OB3b. <i> Hakemian AS, Kondapalli KC, Telser J, Hoffman BM, Stemmler TL, Rosenzweig AC. </i> Biochemistry, 2008","term_id":"IDPO:0000002","curator_id":"rdavidovic","start":1,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3CHX"}],"reference_id":"18540635","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_A0A1A6FH42","date":"2016-08-26T11:56:53.000Z","acc":"Q9KX51","name":"PmoC","length":256,"organism":"Methylosinus trichosporium","dataset":[],"UniParc":"UPI00000BD6EE","genes":[{"name":{"value":"pmoC","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF37893.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF37893.1"}}]}}],"alphafold_very_low_content":0.0546875,"disorder_content":0.37890625,"disprot_consensus":{"full":[{"start":1,"end":17,"type":"D"},{"start":177,"end":256,"type":"D"}],"Structural state":[{"start":1,"end":17,"type":"D"},{"start":177,"end":256,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02320","name":"Ubiquinol-cytochrome C reductase hinge protein","start":76,"end":147}],"gene3D":[{"start":74,"end":147,"id":"1.10.287.20","name":"Ubiquinol-cytochrome C reductase hinge domain"}]},"uniref50":"UniRef50_P00127","sequence":"MGMLELVGEYWEQLKITVVPVVAAAEDDDNEQHEEKAAEGEEKEEENGDEDEDEDEDEDDDDDDDEDEEEEEEVTDQLEDLREHFKNTEEGKALVHHYEECAERVKIQQQQPGYADLEHKEDCVEEFFHLQHYLDTATAPRLFDKLK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P00127","disprot_id":"DP00853","ncbi_taxon_id":559292,"regions_counter":2,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":72,"region_id":"DP00853r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer. <i> Solmaz SR, Hunte C. </i> J Biol Chem, 2008","term_id":"IDPO:0000002","curator_id":"eschad","start":1,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3CX5"}],"reference_id":"18390544","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":72,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer. <i> Solmaz SR, Hunte C. </i> J Biol Chem, 2008","term_id":"GO:0005515","curator_id":"eschad","start":1,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"18390544","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00853r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P00127","date":"2016-08-26T18:38:59.000Z","acc":"P00127","name":"Cytochrome b-c1 complex subunit 6","length":147,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000168BA2","genes":[{"name":{"value":"QCR6"},"synonyms":[{"value":"UCR6"}],"olnNames":[{"value":"YFR033C"}]}],"alphafold_very_low_content":0.2925170068027211,"disorder_content":0.4897959183673469,"disprot_consensus":{"full":[{"start":1,"end":72,"type":"D"}],"Structural state":[{"start":1,"end":72,"type":"D"}],"Molecular function":[{"start":1,"end":72,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00436","name":"Single-strand binding protein family","start":7,"end":107}],"gene3D":[{"start":1,"end":120,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}]},"uniref50":"UniRef50_Q9X8U3","sequence":"MAGETVITVVGNLVDDPELRFTPSGAAVAKFRVASTPRTFDRQTNEWKDGESLFLTCSVWRQAAENVAESLQRGMRVIVQGRLKQRSYEDREGVKRTVYELDVDEVGASLRSATAKVTKTSGQGRGGQGGYGGGGGGQGGGGWGGGPGGGQQGGGAPADDPWATGGAPAGGQQGGGGQGGGGWGGGSGGGGGYSDEPPF","taxonomy":["Bacteria","Actinobacteria","Streptomycetales","Streptomycetaceae","Streptomyces","Streptomyces albidoflavus group"],"uniref90":"UniRef90_Q9X8U3","disprot_id":"DP00854","ncbi_taxon_id":100226,"regions_counter":1,"creator":"smribeiro","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":199,"region_id":"DP00854r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the single-stranded DNA-binding protein from Streptomyces coelicolor. <i> Stefanić Z, Vujaklija D, Luić M. </i> Acta Crystallogr D Biol Crystallogr, 2009","term_id":"IDPO:0000002","curator_id":"smribeiro","start":121,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3EIV"}],"reference_id":"19690375","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q9X8U3","date":"2016-08-26T19:03:04.000Z","acc":"Q9X8U3","name":"Single-stranded DNA-binding protein 2","length":199,"organism":"Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)","dataset":[],"UniParc":"UPI00000DB071","genes":[{"name":{"value":"ssb2"},"orfNames":[{"value":"SCH24.29"}],"olnNames":[{"value":"SCO3907"}]}],"alphafold_very_low_content":0.25125628140703515,"disorder_content":0.3969849246231156,"disprot_consensus":{"full":[{"start":121,"end":199,"type":"D"}],"Structural state":[{"start":121,"end":199,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01381","name":"Helix-turn-helix","start":82,"end":133}],"gene3D":[{"start":68,"end":165,"id":"1.10.260.40","name":"lambda repressor-like DNA-binding domains"}]},"uniref50":"UniRef50_C3NFW5","sequence":"MQANSEEYCELCGSQIRGKGITVSYEGSIITVCNSCYDRIRKHAVIVKADSKKSETRKKATLKPPKMENAELEIVTDYYKIIKTAREQLGISQQQLAQKLKVSENIVKRFESGKLKPTISQARQLEKILGIKLVTPLENNEESEKEFDDTGLTLGDVVNIKEGKK","taxonomy":["Archaea","Crenarchaeota","Thermoprotei","Sulfolobales","Sulfolobaceae","Saccharolobus"],"uniref90":"UniRef90_A0A5Q0TRX3","disprot_id":"DP00856","ncbi_taxon_id":273057,"regions_counter":3,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":79,"region_id":"DP00856r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Archaeal MBF1 binds to 30S and 70S ribosomes via its helix-turn-helix domain. <i> Blombach F, Launay H, Snijders AP, Zorraquino V, Wu H, de Koning B, Brouns SJ, Ettema TJ, Camilloni C, Cavalli A, Vendruscolo M, Dickman MJ, Cabrita LD, La Teana A, Benelli D, Londei P, Christodoulou J, van der Oost J. </i> Biochem J, 2014","term_id":"IDPO:0000002","curator_id":"eschad","start":68,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2MEZ"}],"reference_id":"24825021","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":79,"term_name":"flexible linker","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Archaeal MBF1 binds to 30S and 70S ribosomes via its helix-turn-helix domain. <i> Blombach F, Launay H, Snijders AP, Zorraquino V, Wu H, de Koning B, Brouns SJ, Ettema TJ, Camilloni C, Cavalli A, Vendruscolo M, Dickman MJ, Cabrita LD, La Teana A, Benelli D, Londei P, Christodoulou J, van der Oost J. </i> Biochem J, 2014","term_id":"IDPO:0000033","curator_id":"eschad","start":68,"term_ontology":"IDPO","curator_name":"Eva Schad","reference_id":"24825021","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00856r002","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":165,"region_id":"DP00856r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Archaeal MBF1 binds to 30S and 70S ribosomes via its helix-turn-helix domain. <i> Blombach F, Launay H, Snijders AP, Zorraquino V, Wu H, de Koning B, Brouns SJ, Ettema TJ, Camilloni C, Cavalli A, Vendruscolo M, Dickman MJ, Cabrita LD, La Teana A, Benelli D, Londei P, Christodoulou J, van der Oost J. </i> Biochem J, 2014","term_id":"IDPO:0000002","curator_id":"eschad","start":136,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2MEZ"}],"reference_id":"24825021","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_A0A0E3GWF4","date":"2016-08-26T19:59:46.000Z","acc":"Q980M2","name":"Multiprotein Bridging Factor (MBP-like), putative (MBP-like)","length":165,"organism":"Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)","dataset":[],"UniParc":"UPI00000669FD","genes":[{"name":{"value":"MBP-like","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAK40608.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAK40608.1"}}]},"olnNames":[{"value":"SSO0270","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAK40608.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAK40608.1"}}]}]}],"alphafold_very_low_content":0.2787878787878788,"disorder_content":0.2545454545454545,"disprot_consensus":{"full":[{"start":68,"end":79,"type":"D"},{"start":136,"end":165,"type":"D"}],"Structural state":[{"start":68,"end":79,"type":"D"},{"start":136,"end":165,"type":"D"}],"Disorder function":[{"start":68,"end":79,"type":"F"}]}},{"features":{"pfam":[{"id":"PF22224","name":"Amylase-binding protein AbpA","start":24,"end":195}]},"uniref50":"UniRef50_E8JW27","sequence":"MKKVLLSSVVALTLFAAAAPVFSADEATDAARNNDGAYYLQTQFTNADKVNEYLAQHDGEIRAEAAADPAVVAAKAALDAVEGGSHNYGEVKAAYEAAFNNAFNAVRNKYVQQFQATYNNATEQEGKTYIQGETPEQANARYLKRVGAANNQNPAAEDKGATTPASKEEAKKSEAAAKNAGKAAGKALPKTSAVK","taxonomy":["Bacteria","Firmicutes","Bacilli","Lactobacillales","Streptococcaceae","Streptococcus"],"uniref90":"UniRef90_A0A0M3SM72","disprot_id":"DP00858","ncbi_taxon_id":467705,"regions_counter":4,"creator":"mmacossay","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":134,"region_id":"DP00858r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of amylase-binding protein A of Streptococcus gordonii: a potential receptor for human salivary α-amylase enzyme. <i> Sethi A, Mohanty B, Ramasubbu N, Gooley PR. </i> Protein Sci, 2015","term_id":"IDPO:0000002","curator_id":"mmacossay","start":116,"term_ontology":"IDPO","curator_name":"Mauricio Macossay-Castillo","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2MXX"}],"reference_id":"25739638","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":195,"region_id":"DP00858r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of amylase-binding protein A of Streptococcus gordonii: a potential receptor for human salivary α-amylase enzyme. <i> Sethi A, Mohanty B, Ramasubbu N, Gooley PR. </i> Protein Sci, 2015","term_id":"IDPO:0000002","curator_id":"mmacossay","start":146,"term_ontology":"IDPO","curator_name":"Mauricio Macossay-Castillo","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2MXX"}],"reference_id":"25739638","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":44,"region_id":"DP00858r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of amylase-binding protein A of Streptococcus gordonii: a potential receptor for human salivary α-amylase enzyme. <i> Sethi A, Mohanty B, Ramasubbu N, Gooley PR. </i> Protein Sci, 2015","term_id":"IDPO:0000002","curator_id":"mmacossay","start":24,"term_ontology":"IDPO","curator_name":"Mauricio Macossay-Castillo","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2MXX"}],"reference_id":"25739638","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":44,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structure of amylase-binding protein A of Streptococcus gordonii: a potential receptor for human salivary α-amylase enzyme. <i> Sethi A, Mohanty B, Ramasubbu N, Gooley PR. </i> Protein Sci, 2015","term_id":"GO:0003676","curator_id":"mmacossay","start":24,"term_ontology":"GO","curator_name":"Mauricio Macossay-Castillo","reference_id":"25739638","version":3,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00858r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_A0A0M3SM72","date":"2016-08-27T16:07:12.000Z","acc":"A8AZZ3","name":"Amylase-binding protein AbpA","length":195,"organism":"Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288)","dataset":[],"UniParc":"UPI00015C4621","genes":[{"name":{"value":"abpA","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ABV10035.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABV10035.1"}}]},"olnNames":[{"value":"SGO_2105","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ABV10035.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABV10035.1"}}]}]}],"alphafold_very_low_content":0.5487179487179488,"disorder_content":0.46153846153846156,"disprot_consensus":{"full":[{"start":24,"end":44,"type":"D"},{"start":116,"end":134,"type":"D"},{"start":146,"end":195,"type":"D"}],"Structural state":[{"start":24,"end":44,"type":"D"},{"start":116,"end":134,"type":"D"},{"start":146,"end":195,"type":"D"}],"Molecular function":[{"start":24,"end":44,"type":"F"}]}},{"features":{"pfam":[{"id":"PF13801","name":"Heavy-metal resistance","start":8,"end":124}],"gene3D":[{"start":43,"end":123,"id":"1.20.120.1490","name":"1.20.120.1490"}]},"uniref50":"UniRef50_Q8Z331","sequence":"MKRNNKSAIALIALSLLALSSGAAFAGHHWGNNDGMWQQGGSPLTTEQQATAQKIYDDYYTQTSALRQQLISKRYEYNALLTASSPDTAKINAVAKEMESLGQKLDEQRVKRDVAMAQAGIPRGAGMGYGGCGGYGGGYHRGGGHMGMGNW","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"],"uniref90":"UniRef90_Q8Z331","disprot_id":"DP00861","ncbi_taxon_id":99287,"regions_counter":4,"creator":"sventura","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":151,"region_id":"DP00861r001","released":"2025_12","ec_id":"ECO:0006220","reference_html":"ZraP is a periplasmic molecular chaperone and a repressor of the zinc-responsive two-component regulator ZraSR. <i> Appia-Ayme C, Hall A, Patrick E, Rajadurai S, Clarke TA, Rowley G. </i> Biochem J, 2012","term_id":"IDPO:0000002","curator_id":"vnugnes","start":123,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2025-10-16T15:03:03.941Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3LAY"}],"reference_id":"22084975","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"ZraP is revealed as a decameric structure within which the  ZraP  monomer  is  composed  of  two α-helices  and  residues 123–151  are  disordered  (Figures  3A  and  3B).","type":"Results"}]},{"start":1,"end":42,"reference_id":"22084975","reference_source":"pmid","reference_html":"ZraP is a periplasmic molecular chaperone and a repressor of the zinc-responsive two-component regulator ZraSR. <i> Appia-Ayme C, Hall A, Patrick E, Rajadurai S, Clarke TA, Rowley G. </i> Biochem J, 2012","date":"2025-10-16T15:06:57.658Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_12","version":0,"region_id":"DP00861r004","statement":[{"text":"This region lacks electron density in the PDB structure, indicating it is disordered.","type":"Curator statement"}]}],"released":"2016_10","uniref100":"UniRef100_Q57H53","date":"2016-08-27T21:14:24.000Z","acc":"Q9L9I0","name":"Zinc resistance-associated protein","length":151,"organism":"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","dataset":["Stress response proteins"],"UniParc":"UPI000005A5D0","genes":[{"name":{"value":"zraP"},"orfNames":[{"value":"STMF1.61"}],"olnNames":[{"value":"STM4172"}]}],"alphafold_very_low_content":0.37748344370860926,"disorder_content":0.47019867549668876,"disprot_consensus":{"full":[{"start":1,"end":42,"type":"D"},{"start":123,"end":151,"type":"D"}],"Structural state":[{"start":1,"end":42,"type":"D"},{"start":123,"end":151,"type":"D"}]}},{"features":{"pfam":[{"id":"PF12685","name":"SpoIIIAH-like protein","start":5,"end":210}],"gene3D":[{"start":103,"end":218,"id":"3.30.300.270","name":"Stage III sporulation protein AH-like"}]},"uniref50":"UniRef50_P49785","sequence":"MLKKQTVWLLTMLSLVVVLSVYYIMSPESKNAVQMQSEKSASDSGEVATEKAPAKQDTKEKSGTETEKGKEDGTKGTKDSSADKETSAEASEKGTVVTETADDDLFTTYRLDLEDARSKEREELNAIVSSDDATAKEKSEAYDKMTALSEVEGTEKQLETLIKTQGYEDALVNAEGDKINITVKSDKHSKSKATAIIDLVAKEIKTMKDVAVTFEPSK","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Bacillus"],"uniref90":"UniRef90_P49785","disprot_id":"DP00862","ncbi_taxon_id":224308,"regions_counter":1,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":102,"region_id":"DP00862r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of components of an intercellular channel complex in sporulating Bacillus subtilis. <i> Levdikov VM, Blagova EV, McFeat A, Fogg MJ, Wilson KS, Wilkinson AJ. </i> Proc Natl Acad Sci U S A, 2012","term_id":"IDPO:0000002","curator_id":"rdavidovic","start":32,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3TUF"}],"reference_id":"22431604","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P49785","date":"2016-08-29T10:41:28.000Z","acc":"P49785","name":"Stage III sporulation protein AH","length":218,"organism":"Bacillus subtilis (strain 168)","dataset":[],"UniParc":"UPI00000606EC","genes":[{"name":{"value":"spoIIIAH"},"olnNames":[{"value":"BSU24360"}]}],"alphafold_very_low_content":0.3211009174311927,"disorder_content":0.3256880733944954,"disprot_consensus":{"full":[{"start":32,"end":102,"type":"D"}],"Structural state":[{"start":32,"end":102,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00027","name":"Cyclic nucleotide-binding domain","start":14,"end":101},{"id":"PF13545","name":"Crp-like helix-turn-helix domain","start":133,"end":192}],"gene3D":[{"start":1,"end":194,"id":"G3DSA:2.60.120.1460"}]},"uniref50":"UniRef50_Q9X0Q3","sequence":"MDLKKLLPCGKVIVFRKGEIVKHQDDPIEDVLILLEGTLKTEHVSENGKTLEIDEIKPVQIIASGFIFSSEPRFPVNVVAGENSKILSIPKEVFLDLLMKDRELLLFFLKDVSEHFRVVSEKLFFLTTKTLREKLMNFLVRHMNEKRELTLPVTLEELSRLFGCARPALSRVFQELEREGYIEKHGRRIKVLKNPFEHDRI","taxonomy":["Bacteria","Thermotogae","Thermotogales","Thermotogaceae","Thermotoga"],"uniref90":"UniRef90_Q9X0Q3","disprot_id":"DP00863","ncbi_taxon_id":243274,"regions_counter":1,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":201,"region_id":"DP00863r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"On the use of DXMS to produce more crystallizable proteins: structures of the T. maritima proteins TM0160 and TM1171. <i> Spraggon G, Pantazatos D, Klock HE, Wilson IA, Woods VL, Lesley SA. </i> Protein Sci, 2004","term_id":"IDPO:0000002","curator_id":"rdavidovic","start":130,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1O5L"}],"reference_id":"15557262","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q9X0Q3","date":"2016-08-29T12:32:43.000Z","acc":"Q9X0Q3","name":"Transcriptional regulator, crp family","length":201,"organism":"Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","dataset":[],"UniParc":"UPI00000D3911","genes":[{"olnNames":[{"value":"TM_1171","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAD36246.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD36246.1"}}]}]}],"alphafold_very_low_content":0.01990049751243781,"disorder_content":0.3582089552238806,"disprot_consensus":{"full":[{"start":130,"end":201,"type":"D"}],"Structural state":[{"start":130,"end":201,"type":"D"}]}},{"features":{"pfam":[{"id":"PF21473","name":"Single-stranded DNA binding protein Ssb-like, OB fold","start":11,"end":92}],"gene3D":[{"start":1,"end":111,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}]},"uniref50":"UniRef50_Q9BQ15","sequence":"MTTETFVKDIKPGLKNLNLIFIVLETGRVTKTKDGHEVRTCKVADKTGSINISVWDDVGNLIQPGDIIRLTKGYASVFKGCLTLYTGRGGDLQKIGEFCMVYSEVPNFSEPNPEYSTQQAPNKAVQNDSNPSASQPTTGPSAASPASENQNGNGLSAPPGPGGGPHPPHTPSHPPSTRITRSQPNHTPAGPPGPSSNPVSNGKETRRSSKR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9BQ15","disprot_id":"DP00864","ncbi_taxon_id":9606,"regions_counter":11,"creator":"ireményi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":37,"region_id":"DP00864r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis of SOSS1 complex assembly and recognition of ssDNA. <i> Ren W, Chen H, Sun Q, Tang X, Lim SC, Huang J, Song H. </i> Cell Rep, 2014","term_id":"IDPO:0000002","curator_id":"eschad","start":28,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4OWT"},{"db":"PDB","id":"4OWW"},{"db":"PDB","id":"4OWX"}],"reference_id":"24630995","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":81,"region_id":"DP00864r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis of SOSS1 complex assembly and recognition of ssDNA. <i> Ren W, Chen H, Sun Q, Tang X, Lim SC, Huang J, Song H. </i> Cell Rep, 2014","term_id":"IDPO:0000002","curator_id":"eschad","start":71,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4OWT"},{"db":"PDB","id":"4OWW"},{"db":"PDB","id":"4OWX"}],"reference_id":"24630995","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":211,"region_id":"DP00864r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis of SOSS1 complex assembly and recognition of ssDNA. <i> Ren W, Chen H, Sun Q, Tang X, Lim SC, Huang J, Song H. </i> Cell Rep, 2014","term_id":"IDPO:0000002","curator_id":"eschad","start":110,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4OWT"},{"db":"PDB","id":"4OWW"},{"db":"PDB","id":"4OWX"}],"reference_id":"24630995","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":211,"region_id":"DP00864r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"C-termini are essential and distinct for nucleic acid binding of human NABP1 and NABP2. <i> Vidhyasagar V, He Y, Guo M, Ding H, Talwar T, Nguyen V, Nwosu J, Katselis G, Wu Y. </i> Biochim Biophys Acta, 2016","term_id":"IDPO:0000002","curator_id":"eschad","start":122,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"26550690","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q9BQ15","date":"2016-08-29T15:42:26.000Z","acc":"Q9BQ15","name":"SOSS complex subunit B1","length":211,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000006DDFD","genes":[{"name":{"value":"NABP2"},"synonyms":[{"value":"OBFC2B"},{"value":"SSB1"}],"orfNames":[{"value":"LP3587"}]}],"alphafold_very_low_content":0.13744075829383887,"disorder_content":0.5829383886255924,"disprot_consensus":{"full":[{"start":28,"end":37,"type":"D"},{"start":71,"end":81,"type":"D"},{"start":110,"end":211,"type":"D"}],"Structural state":[{"start":28,"end":37,"type":"D"},{"start":71,"end":81,"type":"D"},{"start":110,"end":211,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00226","name":"DnaJ domain","start":11,"end":79},{"id":"PF05207","name":"CSL zinc finger","start":96,"end":146}],"gene3D":[{"start":91,"end":149,"id":"3.10.660.10","name":"DPH Zinc finger"},{"start":1,"end":90,"id":"1.10.287.110","name":"DnaJ domain"}]},"uniref50":"UniRef50_Q6P3W2","sequence":"MMAVEQMPKKDWYSILGADPSANISDLKQKYQKLILMYHPDKQSTDVPAGTVEECVQKFIEIDQAWKILGNEETKREYDLQRCEDDLRNVGPVDAQVYLEEMSWNEGDHSFYLSCRCGGKYSVSKDEAEEVSLISCDTCSLIIELLHYN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q6P3W2","disprot_id":"DP00865","ncbi_taxon_id":9606,"regions_counter":3,"creator":"zdosztanyi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":10,"region_id":"DP00865r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure and mechanistic insights into novel iron-mediated moonlighting functions of human J-protein cochaperone, Dph4. <i> Thakur A, Chitoor B, Goswami AV, Pareek G, Atreya HS, D'Silva P. </i> J Biol Chem, 2012","term_id":"IDPO:0000002","curator_id":"zdosztanyi","start":1,"term_ontology":"IDPO","curator_name":"Zsuzsanna Dosztányi","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2L6L"}],"reference_id":"22367199","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":92,"region_id":"DP00865r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure and mechanistic insights into novel iron-mediated moonlighting functions of human J-protein cochaperone, Dph4. <i> Thakur A, Chitoor B, Goswami AV, Pareek G, Atreya HS, D'Silva P. </i> J Biol Chem, 2012","term_id":"IDPO:0000002","curator_id":"zdosztanyi","start":77,"term_ontology":"IDPO","curator_name":"Zsuzsanna Dosztányi","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2L6L"}],"reference_id":"22367199","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":92,"term_name":"flexible linker","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structure and mechanistic insights into novel iron-mediated moonlighting functions of human J-protein cochaperone, Dph4. <i> Thakur A, Chitoor B, Goswami AV, Pareek G, Atreya HS, D'Silva P. </i> J Biol Chem, 2012","term_id":"IDPO:0000033","curator_id":"zdosztanyi","start":77,"term_ontology":"IDPO","curator_name":"Zsuzsanna Dosztányi","reference_id":"22367199","version":3,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00865r003","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_Q6P3W2","date":"2016-08-29T16:57:47.000Z","acc":"Q6P3W2","name":"DnaJ homolog subfamily C member 24","length":149,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00001F9F1F","genes":[{"name":{"value":"DNAJC24","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:26979","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:26979"}}]},"synonyms":[{"value":"DPH4"},{"value":"ZCSL3"}]}],"alphafold_very_low_content":0.04697986577181208,"disorder_content":0.174496644295302,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"},{"start":77,"end":92,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":77,"end":92,"type":"D"}],"Disorder function":[{"start":77,"end":92,"type":"F"}]}},{"features":{"pfam":[{"id":"PF16722","name":"Pathogenicity island protein gp6 in Staphylococcus","start":1,"end":72}],"gene3D":[{"start":2,"end":72,"id":"3.30.160.410","name":"3.30.160.410"}]},"uniref50":"UniRef50_K7ZN39","sequence":"METKYELNNTKKVANAFGLNEEDTNLLINAVDLDIKNNMQEISSELQQSEQSKQKQYGTTLQNLAKQNRIIK","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Staphylococcaceae","Staphylococcus"],"uniref90":"UniRef90_A0A0H2WYE1","disprot_id":"DP00866","ncbi_taxon_id":1280,"regions_counter":4,"creator":"zdosztanyi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":72,"region_id":"DP00866r001","released":"2023_12","ec_id":"ECO:0006165","reference_html":"The Staphylococcus aureus pathogenicity island 1 protein gp6 functions as an internal scaffold during capsid size determination. <i> Dearborn AD, Spilman MS, Damle PK, Chang JR, Monroe EB, Saad JS, Christie GE, Dokland T. </i> J Mol Biol, 2011","term_id":"IDPO:0000002","curator_id":"vnugnes","start":42,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-22T17:46:26.345Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2L8T"},{"db":"BMRB","id":"17425"}],"reference_id":"21821042","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Although secondary structure prediction indicates an additional C-terminal α-helical region between residues 40 and 72 (Fig. 3a), this sequence is flexible and does not adopt a unique structure in solution.","type":"Results"}]},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":72,"term_name":"disorder to order","released":"2023_12","ec_name":"cryogenic electron microscopy evidence used in manual assertion","reference_html":"The Staphylococcus aureus pathogenicity island 1 protein gp6 functions as an internal scaffold during capsid size determination. <i> Dearborn AD, Spilman MS, Damle PK, Chang JR, Monroe EB, Saad JS, Christie GE, Dokland T. </i> J Mol Biol, 2011","term_id":"IDPO:0000011","curator_id":"vnugnes","start":42,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"21821042","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-22T17:56:34.507Z","reference_source":"pmid","ec_id":"ECO:0006208","region_id":"DP00866r003","ec_go":"EXP","disprot_namespace":"Structural transition","cross_refs":[{"db":"EMDB","id":"1869"}],"statement":[{"text":"The N-terminal arms were disordered in 80α virions, but are ordered in both SaPI1 and 80α procapsids, suggesting that both gp6 and gp47 become ordered upon binding 21.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_A0A7U8XQV5","date":"2016-08-29T17:48:34.000Z","acc":"O54465","name":"Hypothetical mobile element-associated protein","length":72,"organism":"Staphylococcus aureus","dataset":[],"UniParc":"UPI0000529C97","genes":[{"orfNames":[{"value":"GO941_04055","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"MVL44662.1","url":"https://www.ebi.ac.uk/ena/browser/view/MVL44662.1"}}]},{"value":"GQX37_02380","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"NUY11407.1","url":"https://www.ebi.ac.uk/ena/browser/view/NUY11407.1"}}]},{"value":"NCTC7878_00451","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"SPZ97029.1","url":"https://www.ebi.ac.uk/ena/browser/view/SPZ97029.1"}}]},{"value":"SAGV69_01753","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AIU85401.1","url":"https://www.ebi.ac.uk/ena/browser/view/AIU85401.1"}}]},{"value":"SAHC1335_01735","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ALY20432.1","url":"https://www.ebi.ac.uk/ena/browser/view/ALY20432.1"}}]}]}],"alphafold_very_low_content":0.05555555555555555,"disorder_content":0.4305555555555556,"disprot_consensus":{"full":[{"start":42,"end":72,"type":"T"}],"Structural state":[{"start":42,"end":72,"type":"D"}],"Structural transition":[{"start":42,"end":72,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00017","name":"SH2 domain","start":14,"end":99},{"id":"PF00018","name":"SH3 domain","start":126,"end":168},{"id":"PF07653","name":"Variant SH3 domain","start":221,"end":273}],"gene3D":[{"start":1,"end":115,"id":"3.30.505.10","name":"SH2 domain"},{"start":202,"end":275,"id":"2.30.30.40","name":"SH3 Domains"},{"start":116,"end":174,"id":"2.30.30.40","name":"SH3 Domains"}]},"uniref50":"UniRef50_Q9NHC3","sequence":"MTTNGFDPFEWRSFYFPGMSREEAHKLLGEPQVSIGTFLMRDSSRPGEYSLTVREADEGNAVCHYLIERGEPKEDGTAAAGVKIANQSFPDIPALLNHFKMRVLTEASLLAAYKKPIIEVVVGTFKFTGERETDLPFEQGERLEILSKTNQDWWEARNALGTTGLVPANYVQIQMEFHNDRTSKGASQSSIGSSGGGAERFSSASTSSDNIELQPRLPAKAKVTFDRVPNAYDPTQLRVKKGQTVLVTQKMSNGMYKAELDGQIGSVPHTYLRFTAVSE","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"uniref90":"UniRef90_Q9NHC3","disprot_id":"DP00868","ncbi_taxon_id":6239,"regions_counter":2,"creator":"sventura","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":117,"region_id":"DP00868r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the cell corpse engulfment protein CED-2 in Caenorhabditis elegans. <i> Kang Y, Xu J, Liu Y, Sun J, Sun D, Hu Y, Liu Y. </i> Biochem Biophys Res Commun, 2011","term_id":"IDPO:0000002","curator_id":"sventura","start":102,"term_ontology":"IDPO","curator_name":"Salvador Ventura","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3QWY"}],"reference_id":"21616056","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":117,"term_name":"flexible linker","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of the cell corpse engulfment protein CED-2 in Caenorhabditis elegans. <i> Kang Y, Xu J, Liu Y, Sun J, Sun D, Hu Y, Liu Y. </i> Biochem Biophys Res Commun, 2011","term_id":"IDPO:0000033","curator_id":"sventura","start":102,"term_ontology":"IDPO","curator_name":"Salvador Ventura","reference_id":"21616056","version":3,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00868r002","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_Q9NHC3","date":"2016-08-29T18:12:11.000Z","acc":"Q9NHC3","name":"Cell death abnormality protein 2","length":279,"organism":"Caenorhabditis elegans","dataset":[],"UniParc":"UPI000007F7BE","genes":[{"name":{"value":"ced-2","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"Y41D4B.13a","url":"https://www.wormbase.org/db/seq/sequence?name=Y41D4B.13a;class=Transcript"}}]},"orfNames":[{"value":"Y41D4B.13","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"Y41D4B.13a","url":"https://www.wormbase.org/db/seq/sequence?name=Y41D4B.13a;class=Transcript"}}]}]}],"alphafold_very_low_content":0.14336917562724014,"disorder_content":0.05734767025089606,"disprot_consensus":{"full":[{"start":102,"end":117,"type":"D"}],"Structural state":[{"start":102,"end":117,"type":"D"}],"Disorder function":[{"start":102,"end":117,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00504","name":"Chlorophyll A-B binding protein","start":20,"end":215}],"gene3D":[{"start":88,"end":243,"id":"1.10.3460.10","name":"Chlorophyll a/b binding protein domain"}]},"uniref50":"UniRef50_G7JB75","sequence":"AQPKSGFSTDRPLWYPGAKAPEYLDGSLVGDYGFDPFGLGKPAEYLQYDYDGLDQNLAKNLAGDIIGTRTESADVKSTSLQPYSEVFGLQRFRECELIHGRWAMLATLGALTVEGLTGITWQDAGKVELIEGSSYLGQPLPFSMTTLIWIEVLVIGYIEFQRNAELDTEKRLYPGGTFDPLGLASDPEKKPILQLAEIKHARLAMVGFLGFAVQAAVTGKGPLNNWVTHLSDPLHTTILDRFL","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","Caryophyllales","Chenopodiaceae","Chenopodioideae","Anserineae","Spinacia"],"uniref90":"UniRef90_A0A0K9QLX6","disprot_id":"DP00869","ncbi_taxon_id":3562,"regions_counter":1,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":87,"region_id":"DP00869r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural insights into energy regulation of light-harvesting complex CP29 from spinach. <i> Pan X, Li M, Wan T, Wang L, Jia C, Hou Z, Zhao X, Zhang J, Chang W. </i> Nat Struct Mol Biol, 2011","term_id":"IDPO:0000002","curator_id":"rdavidovic","start":1,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3PL9"}],"reference_id":"21297637","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_A0A0K9QLX6","date":"2016-08-30T09:01:59.000Z","acc":"F2Z293","name":"Chlorophyll a-b binding protein, chloroplastic","length":243,"organism":"Spinacia oleracea","dataset":[],"UniParc":"UPI0001F84868","genes":[],"alphafold_very_low_content":0.03292181069958848,"disorder_content":0.35802469135802467,"disprot_consensus":{"full":[{"start":1,"end":87,"type":"D"}],"Structural state":[{"start":1,"end":87,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00710","name":"Asparaginase, N-terminal","start":11,"end":218},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":405,"end":493},{"id":"PF17763","name":"Glutaminase/Asparaginase C-terminal domain","start":237,"end":348}],"gene3D":[{"start":8,"end":235,"id":"3.40.50.1170","name":"L-asparaginase, N-terminal domain"},{"start":236,"end":361,"id":"3.40.50.40","name":"3.40.50.40"},{"start":400,"end":556,"id":"1.25.40.20","name":"Ankyrin repeat-containing domain"}]},"uniref50":"UniRef50_Q86U10","sequence":"MARASGSERHLLLIYTGGTLGMQSKGGVLVPGPGLVTLLRTLPMFHDKEFAQAQGLPDHALALPPASHGPRVLYTVLECQPLLDSSDMTIDDWIRIAKIIERHYEQYQGFVVIHGTDTMASGASMLSFMLENLHKPVILTGAQVPIRVLWNDARENLLGALLVAGQYIIPEVCLFMNSQLFRGNRVTKVDSQKFEAFCSPNLSPLATVGADVTIAWDLVRKVKWKDPLVVHSNMEHDVALLRLYPGIPASLVRAFLQPPLKGVVLETFGSGNGPSKPDLLQELRAAAQRGLIMVNCSQCLRGSVTPGYATSLAGANIVSGLDMTSEAALAKLSYVLGLPELSLERRQELLAKDLRGEMTLPTADLHQSSPPGSTLGQGVARLFSLFGCQEEDSVQDAVMPSLALALAHAGELEALQALMELGSDLRLKDSNGQTLLHVAARNGRDGVVTMLLHRGMDVNARDRDGLSPLLLAVQGRHRECIRLLRKAGACLSPQDLKDAGTELCRLASRADMEGLQAWGQAGADLQQPGYDGRSALCVAEAAGNQEVLALLRNLALVGPEVPPAI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Hystricomorpha","Caviidae","Cavia"],"uniref90":"UniRef90_H0W0T5","disprot_id":"DP00870","ncbi_taxon_id":10141,"regions_counter":2,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":565,"region_id":"DP00870r001","start":363,"ec_id":"ECO:0006220","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"25320094","version":3,"reference_html":"Identification and structural analysis of an L-asparaginase enzyme from guinea pig with putative tumor cell killing properties. <i> Schalk AM, Nguyen HA, Rigouin C, Lavie A. </i> J Biol Chem, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","cross_refs":[{"db":"PDB","id":"4R8K"},{"db":"PDB","id":"4R8L"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":565,"region_id":"DP00870r002","reference_id":"25320094","start":364,"term_id":"IDPO:0000048","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Although our results are consistent with the first cleavage site (residue 364), it is also possible that the residues were disordered up to the second cleavage site (residue 372), and no electron density was observed (34).","type":"Results"},{"text":"Apparently proteolysis occurring during the 2 weeks required for crystal growth released the catalytic domain, and it is only this that could form well ordered crystals. ","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cleavage assay evidence used in manual assertion","version":3,"reference_html":"Identification and structural analysis of an L-asparaginase enzyme from guinea pig with putative tumor cell killing properties. <i> Schalk AM, Nguyen HA, Rigouin C, Lavie A. </i> J Biol Chem, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","cross_refs":[{"db":"PDB","id":"4R8K"},{"db":"PDB","id":"4R8L"}],"term_name":"limited proteolysis display site","ec_go":"IDA","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_H0W0T5","date":"2016-08-30T10:31:55.000Z","acc":"H0W0T5","name":"ANK_REP_REGION domain-containing protein","length":565,"organism":"Cavia porcellus","dataset":[],"UniParc":"UPI000184C5C1","genes":[{"name":{"value":"ASPG","evidences":[{"code":"ECO:0000313","source":{"name":"Ensembl","id":"ENSCPOP00000016573","url":"https://www.ensembl.org/id/ENSCPOP00000016573"}}]}}],"alphafold_very_low_content":0.047787610619469026,"disorder_content":0.35929203539823007,"disprot_consensus":{"full":[{"start":363,"end":565,"type":"D"}],"Structural state":[{"start":363,"end":565,"type":"D"}],"Disorder function":[{"start":364,"end":565,"type":"F"}]}},{"acc":"A4ZNR2","sequence":"MDPNTVSSFQDILLRMSKMQLESSSEDLNGMITQFESLKLYRDSLGEAVMRMGDLHSLQNRNEKWREQLGQKFEEIRWLIEEVRHKLKITENSFEQITFMQALHLLLEVEQEIRTFSFQLI","creator":"aschramm","dataset":["Viral proteins"],"date":"2016-08-30T10:42:25.000Z","disprot_id":"DP00871","features":{"pfam":[{"id":"PF00601","name":"Influenza non-structural protein (NS2)","start":28,"end":121}],"gene3D":[{"start":59,"end":116,"id":"1.10.287.230","name":"1.10.287.230","_id":"685af523b4ac24d5329d863f"},{"start":1,"end":55,"id":"1.10.287.10","name":"S15/NS1, RNA-binding","_id":"685af523b4ac24d5329d8640"}]},"genes":[{"name":{"value":"NS2","evidences":[{"source":{"id":"ABP64737.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/ABP64737.1","_id":"685af523b4ac24d5329d8671"},"code":"ECO:0000313","_id":"685af523b4ac24d5329d8670"}],"_id":"685af523b4ac24d5329d8672"},"synonyms":[{"value":"NS","evidences":[{"source":{"id":"MF_04067","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04067","_id":"685af523b4ac24d5329d8675"},"code":"ECO:0000256","_id":"685af523b4ac24d5329d8674"},{"source":{"id":"RU362104","name":"RuleBase","url":"https://www.uniprot.org/unirule/RU362104","_id":"685af523b4ac24d5329d8677"},"code":"ECO:0000256","_id":"685af523b4ac24d5329d8676"}],"_id":"685af523b4ac24d5329d8673"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d866f"}],"length":121,"name":"Nuclear export protein","ncbi_taxon_id":437606,"organism":"Influenza A virus","regions_counter":8,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Polyploviricotina","Insthoviricetes","Articulavirales","Orthomyxoviridae","Alphainfluenzavirus"],"UniParc":"UPI0000000532","uniref100":"UniRef100_Q76MT9","uniref50":"UniRef50_P03506","uniref90":"UniRef90_P03506","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006206","ec_name":"near-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":121,"interaction_partner":[],"reference_html":"Structural plasticity in influenza virus protein NS2 (NEP). <i> Lommer BS, Luo M. </i> J Biol Chem, 2002","reference_id":"11751904","region_id":"DP00871r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Interestingly, the near-UV CD spectrum obtained at near physiological buffer conditions was virtually zero, and resembled the spectrum of the protein in the presence of 6m GdmCl (Fig. 3). These observations suggest that under native buffer conditions, the aromatic groups of NS2 are able to rotate freely and undergo no strong interactions with other groups within NS2 (48).","_id":"685af523b4ac24d5329d8644"},{"type":"Discussion","text":"While far-UV CD and FT-IR spectroscopy detected the presence of a significant amount of secondary structure in NS2, near-UV CD and fluorescence spectroscopy revealed that the aromatic residues of the protein were highly assessable to the solvent, and did not undergo strong interactions with neighboring groups.","_id":"685af523b4ac24d5329d8645"},{"type":"Discussion","text":"The flexibility observed in NS2 was intriguing, as with a length of 121 residues the protein is by far large enough to fold independently. The unusual set of characteristics found in the structure of NS2 (compactness, presence of a pronounced secondary structure, but absence of a tightly packed tertiary structure) are attributes typically connected with the molten globule state of proteins (52, 60).","_id":"685af523b4ac24d5329d8646"}],"states_connection":[],"term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T08:48:19.836Z","_id":"685af523b4ac24d5329d8647"},"version":3,"_id":"685af523b4ac24d5329d8643","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006232","ec_name":"differential scanning calorimetry evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":121,"interaction_partner":[],"reference_html":"Structural plasticity in influenza virus protein NS2 (NEP). <i> Lommer BS, Luo M. </i> J Biol Chem, 2002","reference_id":"11751904","region_id":"DP00871r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As expected, these results indicate that the unfolding of NS2 is dominated by the unfolding of its secondary structure. Assuming a two-state mechanism of unfolding, the conformational stability ΔG(H20) of NS2 was estimated as about 6 kcal/mol as described in Ref. 38 (TableII). This value is at the lower end of the range of stabilities commonly observed for solvent-induced unfolding of globular proteins (ΔG(H20) ≈ 5–10 kcal/mol) (55).","_id":"685af523b4ac24d5329d8649"},{"type":"Discussion","text":"The flexibility observed in NS2 was intriguing, as with a length of 121 residues the protein is by far large enough to fold independently. The unusual set of characteristics found in the structure of NS2 (compactness, presence of a pronounced secondary structure, but absence of a tightly packed tertiary structure) are attributes typically connected with the molten globule state of proteins (52, 60).","_id":"685af523b4ac24d5329d864a"}],"states_connection":[],"term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T08:48:17.615Z","_id":"685af523b4ac24d5329d864b"},"version":3,"_id":"685af523b4ac24d5329d8648","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":121,"interaction_partner":[],"reference_html":"Structural plasticity in influenza virus protein NS2 (NEP). <i> Lommer BS, Luo M. </i> J Biol Chem, 2002","reference_id":"11751904","region_id":"DP00871r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In contrast, if NS2 was added to ANS in the presence of 6 m GdmCl, no such interaction was observed. These results suggest that NS2 possesses a loosely packed hydrophobic core that is accessible to the solvent, as expected for a folded protein with a dynamic tertiary structure.","_id":"685af523b4ac24d5329d864d"},{"type":"Discussion","text":"Furthermore, isolated NS2 strongly interacted with the hydrophobic dye ANS suggesting that hydrophobic clusters within the structure of the protein were assessable to the solvent as well (51).","_id":"685af523b4ac24d5329d864e"},{"type":"Results","text":"Addition of acrylamide led to rapid quenching of the tryptophan fluorescence, comparable to tryptophan quenching under denaturing conditions (TableI). The Stern-Volmer plot of the quenching reaction showed upward curvature, indicating that both tryptophan residues of NS2 were nearly equally assessable to the solvent (Fig. 4) (34).","_id":"685af523b4ac24d5329d864f"},{"type":"Discussion","text":"While far-UV CD and FT-IR spectroscopy detected the presence of a significant amount of secondary structure in NS2, near-UV CD and fluorescence spectroscopy revealed that the aromatic residues of the protein were highly assessable to the solvent, and did not undergo strong interactions with neighboring groups.","_id":"685af523b4ac24d5329d8650"},{"type":"Discussion","text":"The flexibility observed in NS2 was intriguing, as with a length of 121 residues the protein is by far large enough to fold independently. The unusual set of characteristics found in the structure of NS2 (compactness, presence of a pronounced secondary structure, but absence of a tightly packed tertiary structure) are attributes typically connected with the molten globule state of proteins (52, 60).","_id":"685af523b4ac24d5329d8651"},{"type":"Curator statement","text":"There are two expermiments done with different fluorescence evidence: intrinsic florescence (tryptophan) and dye fluorescence (ANS).","_id":"685af523b4ac24d5329d8652"}],"states_connection":[],"term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T08:48:15.979Z","_id":"685af523b4ac24d5329d8653"},"version":3,"_id":"685af523b4ac24d5329d864c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IEP","ec_id":"ECO:0000279","ec_name":"qualitative western immunoblotting evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":121,"interaction_partner":[{"db":"UniProt","id":"A4ZNR1","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d865a"}],"reference_html":"Molecular assembly of influenza virus: association of the NS2 protein with virion matrix. <i> Yasuda J, Nakada S, Kato A, Toyoda T, Ishihama A. </i> Virology, 1993","reference_id":"8356796","region_id":"DP00871r006","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"These observations altogether indicate specific molecular association between M1 and NS2.","_id":"685af523b4ac24d5329d865b"},{"type":"Results","text":"Since the NS2 protein was not detected in the M1-free RNP peak (Figs. 3B and 3C; fractions 3-5), we concluded that NS2 is able to rebind RNP cores in vitro only in the simultaneous presence of M1.","_id":"685af523b4ac24d5329d865c"},{"type":"Results","text":"The above observation suggested direct physical association between M1 and NS2.","_id":"685af523b4ac24d5329d865d"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-08-12T15:14:15.264Z","_id":"685af523b4ac24d5329d865e"},"version":1,"_id":"685af523b4ac24d5329d8659","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-08T15:45:20.026Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005805","ec_name":"yeast 2-hybrid evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":121,"interaction_partner":[{"db":"UniProt","id":"P52594","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8663"},{"db":"UniProt","id":"P49686","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8664"},{"db":"UniProt","id":"Q02629","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8665"},{"db":"UniProt","id":"Q02630","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8666"}],"reference_html":"The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins. <i> O'Neill RE, Talon J, Palese P. </i> EMBO J, 1998","reference_id":"9427762","region_id":"DP00871r007","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"A functional domain on the NS2 with characteristics of a nuclear export signal was mapped: it interacts with cellular nucleoporins, can functionally replace the effector domain of the human immunodeficiency virus type 1 (HIV-1) Rev protein and mediates rapid nuclear export when cross-linked to a reporter protein.","_id":"685af523b4ac24d5329d8660"},{"type":"Introduction","text":"In the yeast two-hybrid system, only the viral NS2 protein was able to interact with different nucleoporins.","_id":"685af523b4ac24d5329d8661"},{"type":"Results","text":"The NEP of influenza virus was able to interact strongly with Rab/hRIP1 and yRip1, less strongly with yNup100 and yNup116, and not with yNup1.","_id":"685af523b4ac24d5329d8662"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-08-12T15:14:14.077Z","_id":"685af523b4ac24d5329d8667"},"version":2,"_id":"685af523b4ac24d5329d865f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Results","text":"A synthetic oligopeptide corresponding to NEP amino acids 11–23 (Figure 3C) was cross-linked to glutathione-S transferase (GST).","_id":"685af523b4ac24d5329d866a"}],"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","_id":"685af523b4ac24d5329d8669"}],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006031","ec_name":"immunolocalization evidence used in manual assertion","ec_ontology":"ECO","start":11,"end":23,"interaction_partner":[],"reference_html":"The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins. <i> O'Neill RE, Talon J, Palese P. </i> EMBO J, 1998","reference_id":"9427762","region_id":"DP00871r008","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"A functional domain on the NS2 with characteristics of a nuclear export signal was mapped: it interacts with cellular nucleoporins, can functionally replace the effector domain of the human immunodeficiency virus type 1 (HIV-1) Rev protein and mediates rapid nuclear export when cross-linked to a reporter protein.","_id":"685af523b4ac24d5329d866b"},{"type":"Results","text":"GST-x-NEP quickly migrated to the cytoplasm after microinjection into the nuclei of Madin–Darby bovine kidney (MDBK) cells (Figure 4A and C).","_id":"685af523b4ac24d5329d866c"},{"type":"Results","text":"Therefore, we conclude that the NEP protein contains an NES within amino acids 11– 23.","_id":"685af523b4ac24d5329d866d"}],"states_connection":[],"term_comment":"","term_def":"\"The directed movement of a protein from the nucleus into the cytoplasm.\" [GOC:jl]","term_go_domain":"P","term_id":"GO:0006611","term_is_binding":false,"term_is_obsolete":false,"term_name":"protein export from nucleus","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-08-12T15:14:13.553Z","_id":"685af523b4ac24d5329d866e"},"version":1,"_id":"685af523b4ac24d5329d8668","reference_source":"pmid"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":121,"type":"D"}],"Structural state":[{"start":1,"end":121,"type":"D"}],"Molecular function":[{"start":1,"end":121,"type":"F"}],"Biological process":[{"start":11,"end":23,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00022","name":"Actin","start":11,"end":481}],"gene3D":[{"start":371,"end":447,"id":"3.30.420.40","name":"3.30.420.40"},{"start":448,"end":488,"id":"3.30.420.40","name":"3.30.420.40"},{"start":186,"end":298,"id":"3.90.640.10","name":"Actin; Chain A, domain 4"},{"start":10,"end":151,"id":"3.30.420.40","name":"3.30.420.40"}]},"uniref50":"UniRef50_P80428","sequence":"MSNAALQVYGGDEVSAVVIDPGSYTTNIGYSGSDFPQSILPSVYGKYTADEGNKKIFSEQSIGIPRKDYELKPIIENGLVIDWDTAQEQWQWALQNELYLNSNSGIPALLTEPVWNSTENRKKSLEVLLEGMQFEACYLAPTSTCVSFAAGRPNCLVVDIGHDTCSVSPIVDGMTLSKSTRRNFIAGKFINHLIKKALEPKEIIPLFAIKQRKPEFIKKTFDYEVDKSLYDYANNRGFFQECKETLCHICPTKTLEETKTELSSTAKRSIESPWNEEIVFDNETRYGFAEELFLPKEDDIPANWPRSNSGVVKTWRNDYVPLKRTKPSGVNKSDKKVTPTEEKEQEAVSKSTSPAANSADTPNETGKRPLEEEKPPKENNELIGLADLVYSSIMSSDVDLRATLAHNVVLTGGTSSIPGLSDRLMTELNKILPSLKFRILTTGHTIERQYQSWLGGSILTSLGTFHQLWVGKKEYEEVGVERLLNDRFR","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P80428","disprot_id":"DP00872","ncbi_taxon_id":559292,"regions_counter":4,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":377,"region_id":"DP00872r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural biochemistry of nuclear actin-related proteins 4 and 8 reveals their interaction with actin. <i> Fenn S, Breitsprecher D, Gerhold CB, Witte G, Faix J, Hopfner KP. </i> EMBO J, 2011","term_id":"IDPO:0000002","curator_id":"bszabo","start":328,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"21499228","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3QB0"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":377,"term_name":"protein binding","start":328,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"21499228","version":3,"reference_html":"Structural biochemistry of nuclear actin-related proteins 4 and 8 reveals their interaction with actin. <i> Fenn S, Breitsprecher D, Gerhold CB, Witte G, Faix J, Hopfner KP. </i> EMBO J, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00872r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":226,"region_id":"DP00872r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural biochemistry of nuclear actin-related proteins 4 and 8 reveals their interaction with actin. <i> Fenn S, Breitsprecher D, Gerhold CB, Witte G, Faix J, Hopfner KP. </i> EMBO J, 2011","term_id":"IDPO:0000002","curator_id":"bszabo","start":199,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"21499228","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3QB0"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":226,"term_name":"protein binding","start":199,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"21499228","version":3,"reference_html":"Structural biochemistry of nuclear actin-related proteins 4 and 8 reveals their interaction with actin. <i> Fenn S, Breitsprecher D, Gerhold CB, Witte G, Faix J, Hopfner KP. </i> EMBO J, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00872r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P80428","date":"2016-08-30T11:30:58.000Z","acc":"P80428","name":"Actin-related protein 4","length":489,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000052F17","genes":[{"name":{"value":"ARP4"},"synonyms":[{"value":"ACT3"}],"orfNames":[{"value":"J1012"}],"olnNames":[{"value":"YJL081C"}]}],"alphafold_very_low_content":0.14314928425357873,"disorder_content":0.15950920245398773,"disprot_consensus":{"full":[{"start":199,"end":226,"type":"D"},{"start":328,"end":377,"type":"D"}],"Structural state":[{"start":199,"end":226,"type":"D"},{"start":328,"end":377,"type":"D"}],"Molecular function":[{"start":199,"end":226,"type":"F"},{"start":328,"end":377,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00022","name":"Actin","start":48,"end":325},{"id":"PF00022","name":"Actin","start":506,"end":619}],"gene3D":[{"start":121,"end":288,"id":"3.30.420.40","name":"3.30.420.40"},{"start":300,"end":398,"id":"3.90.640.10","name":"Actin; Chain A, domain 4"},{"start":32,"end":105,"id":"3.30.420.40","name":"3.30.420.40"},{"start":492,"end":619,"id":"3.30.420.40","name":"3.30.420.40"}]},"uniref50":"UniRef50_Q9H981","sequence":"MTQAEKGDTENGKEKGGEKEKEQRGVKRPIVPALVPESLQEQIQSNFIIVIHPGSTTLRIGRATDTLPASIPHVIARRHKQQGQPLYKDSWLLREGLNKPESNEQRQNGLKMVDQAIWSKKMSNGTRRIPVSPEQARSYNKQMRPAILDHCSGNKWTNTSHHPEYLVGEEALYVNPLDCYNIHWPIRRGQLNIHPGPGGSLTAVLADIEVIWSHAIQKYLEIPLKDLKYYRCILLIPDIYNKQHVKELVNMILMKMGFSGIVVHQESVCATYGSGLSSTCIVDVGDQKTSVCCVEDGVSHRNTRLCLAYGGSDVSRCFYWLMQRAGFPYRECQLTNKMDCLLLQHLKETFCHLDQDISGLQDHEFQIRHPDSPALLYQFRLGDEKLQAPMALFYPATFGIVGQKMTTLQHRSQGDPEDPHDEHYLLATQSKQEQSAKATADRKSASKPIGFEGDLRGQSSDLPERLHSQEVDLGSAQGDGLMAGNDSEEALTALMSRKTAISLFEGKALGLDKAILHSIDCCSSDDTKKKMYSSILVVGGGLMFHKAQEFLQHRILNKMPPSFRRIIENVDVITRPKDMDPRLIAWKGGAVLACLDTTQELWIYQREWQRFGVRMLRERAAFVW","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9H981","disprot_id":"DP00873","ncbi_taxon_id":9606,"regions_counter":2,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":507,"region_id":"DP00873r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of Actin-related protein 8 and its contribution to nucleosome binding. <i> Gerhold CB, Winkler DD, Lakomek K, Seifert FU, Fenn S, Kessler B, Witte G, Luger K, Hopfner KP. </i> Nucleic Acids Res, 2012","term_id":"IDPO:0000002","curator_id":"bszabo","start":401,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"22977180","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4FO0"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":507,"term_name":"protein binding","start":401,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"22977180","version":3,"reference_html":"Structure of Actin-related protein 8 and its contribution to nucleosome binding. <i> Gerhold CB, Winkler DD, Lakomek K, Seifert FU, Fenn S, Kessler B, Witte G, Luger K, Hopfner KP. </i> Nucleic Acids Res, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00873r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q9H981","date":"2016-08-30T12:18:18.000Z","acc":"Q9H981","name":"Actin-related protein 8","length":624,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000126064","genes":[{"name":{"value":"ACTR8"},"synonyms":[{"value":"ARP8"},{"value":"INO80N"}]}],"alphafold_very_low_content":0.1233974358974359,"disorder_content":0.17147435897435898,"disprot_consensus":{"full":[{"start":401,"end":507,"type":"D"}],"Structural state":[{"start":401,"end":507,"type":"D"}],"Molecular function":[{"start":401,"end":507,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00022","name":"Actin","start":6,"end":461}],"gene3D":[{"start":186,"end":326,"id":"3.90.640.10","name":"Actin; Chain A, domain 4"},{"start":144,"end":437,"id":"3.30.420.40","name":"3.30.420.40"},{"start":8,"end":461,"id":"3.30.420.40","name":"3.30.420.40"}]},"uniref50":"UniRef50_Q12406","sequence":"MTLNRKCVVIHNGSHRTVAGFSNVELPQCIIPSSYIKRTDEGGEAEFIFGTYNMIDAAAEKRNGDEVYTLVDSQGLPYNWDALEMQWRYLYDTQLKVSPEELPLVITMPATNGKPDMAILERYYELAFDKLNVPVFQIVIEPLAIALSMGKSSAFVIDIGASGCNVTPIIDGIVVKNAVVRSKFGGDFLDFQVHERLAPLIKEENDMENMADEQKRSTDVWYEASTWIQQFKSTMLQVSEKDLFELERYYKEQADIYAKQQEQLKQMDQQLQYTALTGSPNNPLVQKKNFLFKPLNKTLTLDLKECYQFAEYLFKPQLISDKFSPEDGLGPLMAKSVKKAGASINSMKANTSTNPNGLGTSHINTNVGDNNSTASSSNISPEQVYSLLLTNVIITGSTSLIEGMEQRIIKELSIRFPQYKLTTFANQVMMDRKIQGWLGALTMANLPSWSLGKWYSKEDYETLKRDRKQSQATNATN","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q12406","disprot_id":"DP00874","ncbi_taxon_id":559292,"regions_counter":3,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":214,"region_id":"DP00874r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the full-length yeast Arp7-Arp9 heterodimer. <i> Lobsiger J, Hunziker Y, Richmond TJ. </i> Acta Crystallogr D Biol Crystallogr, 2014","term_id":"IDPO:0000002","curator_id":"bszabo","start":204,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"24531465","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3WEE"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":276,"region_id":"DP00874r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the full-length yeast Arp7-Arp9 heterodimer. <i> Lobsiger J, Hunziker Y, Richmond TJ. </i> Acta Crystallogr D Biol Crystallogr, 2014","term_id":"IDPO:0000002","curator_id":"bszabo","start":262,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"24531465","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3WEE"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":379,"region_id":"DP00874r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the full-length yeast Arp7-Arp9 heterodimer. <i> Lobsiger J, Hunziker Y, Richmond TJ. </i> Acta Crystallogr D Biol Crystallogr, 2014","term_id":"IDPO:0000002","curator_id":"bszabo","start":353,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"24531465","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3WEE"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q12406","date":"2016-08-30T13:27:29.000Z","acc":"Q12406","name":"Actin-related protein 7","length":477,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000126063","genes":[{"name":{"value":"ARP7"},"synonyms":[{"value":"SWP61"}],"orfNames":[{"value":"YP9367.14"}],"olnNames":[{"value":"YPR034W"}]}],"alphafold_very_low_content":0.07127882599580712,"disorder_content":0.1111111111111111,"disprot_consensus":{"full":[{"start":204,"end":214,"type":"D"},{"start":262,"end":276,"type":"D"},{"start":353,"end":379,"type":"D"}],"Structural state":[{"start":204,"end":214,"type":"D"},{"start":262,"end":276,"type":"D"},{"start":353,"end":379,"type":"D"}]}},{"acc":"P69723","sequence":"MENRWQVMIVWQVDRMRIRTWKSLVKHHMYVSGKARGWFYRHHYESPHPRISSEVHIPLGDARLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPELADQLIHLYYFDCFSDSAIRKALLGHIVSPRCEYQAGHNKVGSLQYLALAALITPKKIKPPLPSVTKLTEDRWNKPQKTKGHRGSHTMNGH","creator":"esalladini","dataset":["Viral proteins","RNA-binding proteins"],"date":"2016-08-30T13:47:41.000Z","disprot_id":"DP00875","features":{"pfam":[{"id":"PF00559","name":"Retroviral Vif (Viral infectivity) protein","start":1,"end":192}]},"genes":[{"name":{"value":"vif","evidences":[{"source":{"id":"MF_04081","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04081","_id":"685af523b4ac24d5329d86b7"},"code":"ECO:0000255","_id":"685af523b4ac24d5329d86b6"}],"_id":"685af523b4ac24d5329d86b8"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d86b5"}],"length":192,"name":"Virion infectivity factor","ncbi_taxon_id":11706,"organism":"Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)","regions_counter":16,"released":"2016_10","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"UniParc":"UPI000000078E","uniref100":"UniRef100_P69720","uniref50":"UniRef50_P12504","uniref90":"UniRef90_P31820","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":141,"end":192,"interaction_partner":[],"reference_html":"The C-terminal domain of the HIV-1 Vif protein is natively unfolded in its unbound state. <i> Reingewertz TH, Benyamini H, Lebendiker M, Shalev DE, Friedler A. </i> Protein Eng Des Sel, 2009","reference_id":"19218568","region_id":"DP00875r001","released":"2022_03","sample":[],"sequence_construct":"KVXSLQYLALAALITPKKIKPPLPSVTKXTEDRWNKPQXTKGHRXSHTMNGH","statement":[{"type":"Results","text":"The far-UV CD spectrum of the CTD (Fig. 2A) lacked the typical signatures of secondary structure, exhibiting only a negative signal at 200 nm. This pattern implied a high content of unstructured regions in the CTD.","_id":"685af523b4ac24d5329d867a"},{"type":"Curator statement","text":"To avoid on-resin aggregation during the synthesis authors substituted the residues 185, 179, 169 and 143 with pseudoproline dipeptide.","_id":"685af523b4ac24d5329d867b"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T10:33:17.413Z","_id":"685af523b4ac24d5329d867c"},"version":3,"_id":"685af523b4ac24d5329d8679","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":141,"end":192,"interaction_partner":[],"reference_html":"The C-terminal domain of the HIV-1 Vif protein is natively unfolded in its unbound state. <i> Reingewertz TH, Benyamini H, Lebendiker M, Shalev DE, Friedler A. </i> Protein Eng Des Sel, 2009","reference_id":"19218568","region_id":"DP00875r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The CD spectrum of the CTD (Fig. 5A) in 5.4 mM DPC (green) and in 20 mM DPC (red), compared with the spectrum in buffer without DPC (blue), showed a red shift of ∼3 nm (from 199 to 202 nm). The minimum at 198 nm decreased, while the signal at 222 nm increased. The change in the CD spectrum indicates a structural change in the Vif CTD that was induced by the micellar environment.","_id":"685af523b4ac24d5329d867e"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_id":"GO:0008289","term_is_binding":true,"term_is_obsolete":false,"term_name":"lipid binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T10:36:47.556Z","_id":"685af523b4ac24d5329d867f"},"version":4,"_id":"685af523b4ac24d5329d867d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":141,"end":192,"interaction_partner":[],"reference_html":"The C-terminal domain of the HIV-1 Vif protein is natively unfolded in its unbound state. <i> Reingewertz TH, Benyamini H, Lebendiker M, Shalev DE, Friedler A. </i> Protein Eng Des Sel, 2009","reference_id":"19218568","region_id":"DP00875r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The CTD eluted from the column with an elution volume of 11.3 ml. This volume gave an apparent molecular weight of 14.0 kDa, a value 2.5 times higher than the calculated mass of 5.8 kDa according to the calibration curve of standard MW markers. This indicated an extended conformation of the Vif CTD.","_id":"685af523b4ac24d5329d8681"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T10:33:20.400Z","_id":"685af523b4ac24d5329d8682"},"version":3,"_id":"685af523b4ac24d5329d8680","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":145,"end":192,"interaction_partner":[],"reference_html":"The C-terminal domain of the HIV-1 Vif protein is natively unfolded in its unbound state. <i> Reingewertz TH, Benyamini H, Lebendiker M, Shalev DE, Friedler A. </i> Protein Eng Des Sel, 2009","reference_id":"19218568","region_id":"DP00875r009","released":"2022_03","sample":[],"sequence_construct":"KVXSLQYLALAALITPKKIKPPLPSVTKXTEDRWNKPQXTKGHRXSHTMNGH","statement":[{"type":"Results","text":"The 1H-NMR spectra of Vif145–192 showed a narrow dispersion of amide resonances, which is characteristic of a random coil (Fig. 4A). ","_id":"685af523b4ac24d5329d8690"},{"type":"Results","text":"The dispersion of the amide protons in the 15N-HSQC spectrum (Fig. 4B) was in a narrow range of 7.95–8.74 ppm, Δ = 0.79 ppm, characteristic of unfolded proteins and peptides.","_id":"685af523b4ac24d5329d8691"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T10:33:21.934Z","_id":"685af523b4ac24d5329d8692"},"version":1,"_id":"685af523b4ac24d5329d868f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":141,"end":192,"interaction_partner":[],"reference_html":"The C-terminal domain of the HIV-1 Vif protein is natively unfolded in its unbound state. <i> Reingewertz TH, Benyamini H, Lebendiker M, Shalev DE, Friedler A. </i> Protein Eng Des Sel, 2009","reference_id":"19218568","region_id":"DP00875r010","released":"2022_03","sample":[],"sequence_construct":"KVXSLQYLALAALITPKKIKPPLPSVTKXTEDRWNKPQXTKGHRXSHTMNGH","statement":[{"type":"Results","text":"The CD spectrum of the CTD (Fig. 5A) in 5.4 mM DPC (green) and in 20 mM DPC (red), compared with the spectrum in buffer without DPC (blue), showed a red shift of ∼3 nm (from 199 to 202 nm). The minimum at 198 nm decreased, while the signal at 222 nm increased. The change in the CD spectrum indicates a structural change in the Vif CTD that was induced by the micellar environment.","_id":"685af523b4ac24d5329d8694"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T10:36:52.184Z","_id":"685af523b4ac24d5329d8695"},"version":1,"_id":"685af523b4ac24d5329d8693","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":141,"end":192,"interaction_partner":[{"db":"UniProt","id":"Q15369","partner_start":76,"partner_end":111,"_id":"685af523b4ac24d5329d8697"}],"reference_html":"The C-terminal domain of the HIV-1 Vif protein is natively unfolded in its unbound state. <i> Reingewertz TH, Benyamini H, Lebendiker M, Shalev DE, Friedler A. </i> Protein Eng Des Sel, 2009","reference_id":"19218568","region_id":"DP00875r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Vif141–192 was titrated into fluorescein-labeled ElonginC76–111 and the resulting binding curve was fit to 1:1 binding model, resulting in Kd of 11.0 ± 0.6 µM (Fig. 5B).","_id":"685af523b4ac24d5329d8698"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T10:37:25.105Z","_id":"685af523b4ac24d5329d8699"},"version":1,"_id":"685af523b4ac24d5329d8696","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":145,"end":192,"interaction_partner":[{"db":"UniProt","id":"Q15369","partner_start":76,"partner_end":111,"_id":"685af523b4ac24d5329d869b"}],"reference_html":"The C-terminal domain of the HIV-1 Vif protein is natively unfolded in its unbound state. <i> Reingewertz TH, Benyamini H, Lebendiker M, Shalev DE, Friedler A. </i> Protein Eng Des Sel, 2009","reference_id":"19218568","region_id":"DP00875r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Vif145–192 bound the ElonginC peptide with similar affinity, Kd = 12.5 ± 0.3 µM.","_id":"685af523b4ac24d5329d869c"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T10:37:09.046Z","_id":"685af523b4ac24d5329d869d"},"version":1,"_id":"685af523b4ac24d5329d869a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":141,"end":192,"interaction_partner":[{"db":"UniProt","id":"Q15369","partner_start":76,"partner_end":111,"_id":"685af523b4ac24d5329d869f"}],"reference_html":"The C-terminal domain of the HIV-1 Vif protein is natively unfolded in its unbound state. <i> Reingewertz TH, Benyamini H, Lebendiker M, Shalev DE, Friedler A. </i> Protein Eng Des Sel, 2009","reference_id":"19218568","region_id":"DP00875r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The CD spectrum of Vif CTD—ElonginC76–111 mixture at 1:1 molar ratio (Fig. 5C) gave an average between the unbound spectra of the CTD and the free ElonginC76–111, indicating that there is no significant change in the CTD structure upon binding to ElonginC76–111 at this molar ratio.","_id":"685af523b4ac24d5329d86a0"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T10:37:05.896Z","_id":"685af523b4ac24d5329d86a1"},"version":1,"_id":"685af523b4ac24d5329d869e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005802","ec_name":"cell transfection experiment evidence used in manual assertion","ec_ontology":"ECO","start":157,"end":192,"interaction_partner":[],"reference_html":"Biological activity of human immunodeficiency virus type 1 Vif requires membrane targeting by C-terminal basic domains. <i> Goncalves J, Shi B, Yang X, Gabuzda D. </i> J Virol, 1995","reference_id":"7474141","region_id":"DP00875r014","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"Membrane localization is required for Vif function during HIV-1 replication. To provide a quantitative measure of the biological activity of the mutant Vif proteins, a transient complementation assay was used to examine the abilities of the mutant Vif proteins to complement a single round of HIV-1 replication in trans (Fig. 3) (5, 13). The expression of wild-type Vif in trans in this assay restores the replication of a  vif-defective virus to the wild-type level (5, 8). In the absence of Vif expressed in trans, replication of the vif-positive virus was approximately 10-fold greater than that of the vif-negative virus.","_id":"685af523b4ac24d5329d86a3"}],"states_connection":[],"term_comment":"","term_def":"\"Any process involved directly in viral genome replication, including viral nucleotide metabolism.\" [ISBN:0781702534]","term_go_domain":"P","term_id":"GO:0019079","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral genome replication","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-11T12:24:52.012Z","_id":"685af523b4ac24d5329d86a4"},"version":1,"_id":"685af523b4ac24d5329d86a2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"position":null,"statements":[{"type":"Article","text":"Site-directed mutagenesis was used to replace clusters of basic amino acids with uncharged alanine residues. A series of such Vif mutants was made (Fig. 1) and used for studies of membrane localization and Vif function.","_id":"685af523b4ac24d5329d86a7"},{"type":"Curator statement","text":"B1 has 3 mutations (Lys157Ala, Lys158Ala and Lys160Ala), B2 has 3 mutations (Arg173Ala, Lys175Ala and Lys177Ala) and B4 has the mutations of B1 and B2 combined.","_id":"685af523b4ac24d5329d86a8"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg173Ala","_id":"685af523b4ac24d5329d86a6"},{"start":null,"end":null,"position":null,"statements":[],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys175Ala","_id":"685af523b4ac24d5329d86a9"},{"start":null,"end":null,"position":null,"statements":[],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys177Ala","_id":"685af523b4ac24d5329d86aa"},{"start":null,"end":null,"position":null,"statements":[],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys157Ala","_id":"685af523b4ac24d5329d86ab"},{"start":null,"end":null,"position":null,"statements":[],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys158Ala","_id":"685af523b4ac24d5329d86ac"},{"start":null,"end":null,"position":null,"statements":[],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys160Ala","_id":"685af523b4ac24d5329d86ad"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-08-22T14:02:44.962Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005802","ec_name":"cell transfection experiment evidence used in manual assertion","ec_ontology":"ECO","start":157,"end":192,"interaction_partner":[],"reference_html":"Biological activity of human immunodeficiency virus type 1 Vif requires membrane targeting by C-terminal basic domains. <i> Goncalves J, Shi B, Yang X, Gabuzda D. </i> J Virol, 1995","reference_id":"7474141","region_id":"DP00875r015","released":"2023_12","sample":[],"sequence_construct":"AAIAPPLPSVTKLT EDAWNAPQATKGHRGSHTMNGH","statement":[{"type":"Article","text":"The biological activities of the mutant Vif proteins correlated directly with their membrane binding activities in vitro (Fig. 3), indicating that Vif function is likely to require membrane localization.","_id":"685af523b4ac24d5329d86ae"},{"type":"Article","text":"However, no virus replication was detected in H9 cultures transfected with the B1,  B2, or B4 HIV-1 mutant virus DNAs. These results confirm the absence or near absence of Vif function in the B1, B2, and B4 mutants during HIV-1 replication in nonpermissive cells. Moreover, the direct correlation between the loss of biological activity and the loss of membrane binding of Vif during HIV-1 replication in infected cells (Fig. 2B) indicates that membrane localization is likely to be required for Vif function in vivo.","_id":"685af523b4ac24d5329d86af"},{"type":"Article","text":"Virus replication was monitored by measuring the reverse transcriptase activity in the culture supernatant.","_id":"685af523b4ac24d5329d86b0"}],"states_connection":[],"term_comment":"","term_def":"\"The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.\" [ISBN:0716731363]","term_go_domain":"P","term_id":"GO:0005886","term_is_binding":false,"term_is_obsolete":false,"term_name":"plasma membrane","term_namespace":"Cellular component","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":2,"_id":"685af523b4ac24d5329d86a5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0007101","ec_name":"southern hybridization evidence used in manual assertion","ec_ontology":"ECO","start":157,"end":192,"interaction_partner":[],"reference_html":"Role of Vif in human immunodeficiency virus type 1 reverse transcription. <i> Goncalves J, Korin Y, Zack J, Gabuzda D. </i> J Virol, 1996","reference_id":"8970997","region_id":"DP00875r016","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"Full-genome-length minus-strand DNA was not detectable in vif mutant virions even when the blots were overexposed to visualize the short DNA products at an intensity similar to that of the wild type. The blots were rehybridized with the gag/pol(2) probe, which detects minus-strand DNA which has been reverse transcribed through the left half of the genome. Hybridization with the gag/pol(2) probe gave results similar to those obtained with the U3(2) probe, indicating that minus-strand synthesis was discontinuous with initiation at multiple sites.","_id":"685af523b4ac24d5329d86b2"},{"type":"Article","text":"The preceding experiment indicates that vif mutant virions are defective in their ability to synthesize minus-strand DNA. To determine the effect of Vif on synthesis of the plus strand, the blots from the preceding experiment were reprobed with U3 and gag/pol riboprobes of minus-strand polarity. The U3(1) probe detects initial plus-strand DNA products immediately adjacent to the 39 PPT. The gag/pol(1) probe detects plus-strand DNA products synthesized after the second template switch or initiated at the central PPT. In wild-type virions, the U3(1) and gag/pol(1) probes detected plus-strand DNA products of 0.5 to 9.7 kb (Fig. 3B). In contrast, plus-strand DNA products longer than 4 kb could not be detected in vif mutant virions even when the blots were overexposed to visualize the short DNA products at an intensity similar to that of the wild type.","_id":"685af523b4ac24d5329d86b3"}],"states_connection":[],"term_comment":"","term_def":"\"Any process involved directly in viral genome replication, including viral nucleotide metabolism.\" [ISBN:0781702534]","term_go_domain":"P","term_id":"GO:0019079","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral genome replication","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-11T12:04:18.714Z","_id":"685af523b4ac24d5329d86b4"},"version":1,"_id":"685af523b4ac24d5329d86b1","reference_source":"pmid"}],"__v":0,"disorder_content":0.2708333333333333,"disprot_consensus":{"full":[{"start":141,"end":192,"type":"T"}],"Structural state":[{"start":141,"end":192,"type":"D"}],"Molecular function":[{"start":141,"end":192,"type":"F"}],"Structural transition":[{"start":141,"end":192,"type":"T"}],"Biological process":[{"start":157,"end":192,"type":"F"}],"Cellular component":[{"start":157,"end":192,"type":"F"}]}},{"acc":"P14340","sequence":"MNNQRKKARNTPFNMLKRERNRVSTVQQLTKRFSLGMLQGRGPLKLFMALVAFLRFLTIPPTAGILKRWGTIKKSKAINVLRGFRKEIGRMLNILNRRRRTAGMIIMLIPTVMAFHLTTRNGEPHMIVSRQEKGKSLLFKTEDGVNMCTLMAMDLGELCEDTITYKCPFLKQNEPEDIDCWCNSTSTWVTYGTCTTTGEHRREKRSVALVPHVGMGLETRTETWMSSEGAWKHAQRIETWILRHPGFTIMAAILAYTIGTTHFQRALIFILLTAVAPSMTMRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPTLDFELIETEAKQPATLRKYCIEAKLTNTTTDSRCPTQGEPSLNEEQDKRFVCKHSMVDRGWGNGCGLFGKGGIVTCAMFTCKKNMKGKVVQPENLEYTIVITPHSGEEHAVGNDTGKHGKEIKITPQSSITEAELTGYGTVTMECSPRTGLDFNEMVLLQMENKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFTGHLKCRLRMDKLQLKGMSYSMCTGKFKVVKEIAETQHGTIVIRVQYEGDGSPCKIPFEIMDLEKRHVLGRLITVNPIVTEKDSPVNIEAEPPFGDSYIIIGVEPGQLKLNWFKKGSSIGQMIETTMRGAKRMAILGDTAWDFGSLGGVFTSIGKALHQVFGAIYGAAFSGVSWIMKILIGVIITWIGMNSRSTSLSVSLVLVGVVTLYLGVMVQADSGCVVSWKNKELKCGSGIFITDNVHTWTEQYKFQPESPSKLASAIQKAHEEGICGIRSVTRLENLMWKQITPELNHILSENEVKLTIMTGDIKGIMQAGKRSLQPQPTELKYSWKTWGKAKMLSTESHNQTFLIDGPETAECPNTNRAWNSLEVEDYGFGVFTTNIWLKLREKQDVFCDSKLMSAAIKDNRAVHADMGYWIESALNDTWKIEKASFIEVKSCHWPKSHTLWSNGVLESEMIIPKNFAGPVSQHNYRPGYHTQTAGPWHLGKLEMDFDFCEGTTVVVTEDCGNRGPSLRTTTASGKLITEWCCRSCTLPPLRYRGEDGCWYGMEIRPLKEKEENLVNSLVTAGHGQIDNFSLGVLGMALFLEEMLRTRVGTKHAILLVAVSFVTLITGNMSFRDLGRVMVMVGATMTDDIGMGVTYLALLAAFKVRPTFAAGLLLRKLTSKELMMTTIGIVLLSQSTIPETILELTDALALGMMVLKMVRKMEKYQLAVTIMAILCVPNAVILQNAWKVSCTILAVVSVSPLFLTSSQQKADWIPLALTIKGLNPTAIFLTTLSRTNKKRSWPLNEAIMAVGMVSILASSLLKNDIPMTGPLVAGGLLTVCYVLTGRSADLELERAADVKWEDQAEISGSSPILSITISEDGSMSIKNEEEEQTLTILIRTGLLVISGLFPVSIPITAAAWYLWEVKKQRAGVLWDVPSPPPVGKAELEDGAYRIKQKGILGYSQIGAGVYKEGTFHTMWHVTRGAVLMHKGKRIEPSWADVKKDLISYGGGWKLEGEWKEGEEVQVLALEPGKNPRAVQTKPGLFKTNAGTIGAVSLDFSPGTSGSPIIDKKGKVVGLYGNGVVTRSGAYVSAIAQTEKSIEDNPEIEDDIFRKRKLTIMDLHPGAGKTKRYLPAIVREAIKRGLRTLILAPTRVVAAEMEEALRGLPIRYQTPAIRAEHTGREIVDLMCHATFTMRLLSPVRVPNYNLIIMDEAHFTDPASIAARGYISTRVEMGEAAGIFMTATPPGSRDPFPQSNAPIMDEEREIPERSWSSGHEWVTDFKGKTVWFVPSIKAGNDIAACLRKNGKKVIQLSRKTFDSEYVKTRTNDWDFVVTTDISEMGANFKAERVIDPRRCMKPVILTDGEERVILAGPMPVTHSSAAQRRGRIGRNPKNENDQYIYMGEPLENDEDCAHWKEAKMLLDNINTPEGIIPSMFEPEREKVDAIDGEYRLRGEARKTFVDLMRRGDLPVWLAYRVAAEGINYADRRWCFDGIKNNQILEENVEVEIWTKEGERKKLKPRWLDAKIYSDPLALKEFKEFAAGRKSLTLNLITEMGRLPTFMTQKARDALDNLAVLHTAEAGGRAYNHALSELPETLETLLLLTLLATVTGGIFLFLMSGRGIGKMTLGMCCIITASILLWYAQIQPHWIAASIILEFFLIVLLIPEPEKQRTPQDNQLTYVVIAILTVVAATMANEMGFLEKTKKDLGLGSITTQQPESNILDIDLRPASAWTLYAVATTFVTPMLRHSIENSSVNVSLTAIANQATVLMGLGKGWPLSKMDIGVPLLAIGCYSQVNPITLTAALFLLVAHYAIIGPGLQAKATREAQKRAAAGIMKNPTVDGITVIDLDPIPYDPKFEKQLGQVMLLVLCVTQVLMMRTTWALCEALTLATGPISTLWEGNPGRFWNTTIAVSMANIFRGSYLAGAGLLFSIMKNTTNTRRGTGNIGETLGEKWKSRLNALGKSEFQIYKKSGIQEVDRTLAKEGIKRGETDHHAVSRGSAKLRWFVERNMVTPEGKVVDLGCGRGGWSYYCGGLKNVREVKGLTKGGPGHEEPIPMSTYGWNLVRLQSGVDVFFTPPEKCDTLLCDIGESSPNPTVEAGRTLRVLNLVENWLNNNTQFCIKVLNPYMPSVIEKMEALQRKYGGALVRNPLSRNSTHEMYWLSNASGNIVSSVNMISRMLINRFTMRHKKATYEPDVDLGSGTRNIGIESEIPNLDIIGKRIEKIKQEHETSWHYDQDHPYKTWAYHGSYETKQTGSASSMGNGVVRLLTKPWDVVPMVTQMAMTDTTPFGQQRVFKEKVDTRTQEPKEGTKKLMKITAEWLWKELGKKKTPRMCTREEFTRKVRSNAALGAIFTDENKWKSAREAVEDSRFWELVDKERNLHLEGKCETCVYNMMGKREKKLGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWFSRENSLSGVEGEGLHKLGYILRDVSKKEGGAMYADDTAGWDTRITLEDLKNEEMVTNHMEGEHKKLAEAIFKLTYQNKVVRVQRPTPRGTVMDIISRRDQRGSGQVGTYGLNTFTNMEAQLIRQMEGEGVFKSIQHLTVTEEIAVQNWLARVGRERLSRMAISGDDCVVKPLDDRFASALTALNDMGKVRKDIQQWEPSRGWNDWTQVPFCSHHFHELIMKDGRVLVVPCRNQDELIGRARISQGAGWSLRETACLGKSYAQMWSLMYFHRRDLRLAANAICSAVPSHWVPTSRTTWSIHAKHEWMTTEDMLTVWNRVWIQENPWMEDKTPVESWEEIPYLGKREDQWCGSLIGLTSRATWAKNIQTAINQVRSLIGNEEYTDYMPSMKRFRKEEEEAGVLW","creator":"esalladini","dataset":["Viral proteins","Neglected tropical diseases proteins","RNA-binding proteins"],"date":"2016-08-30T15:22:14.000Z","disprot_id":"DP00876","features":{"pfam":[{"id":"PF00869","name":"Flavivirus glycoprotein, central and dimerisation domains","start":282,"end":576},{"id":"PF00948","name":"Flavivirus non-structural Protein NS1","start":777,"end":1129},{"id":"PF00949","name":"Peptidase S7, Flavivirus NS3 serine protease","start":1492,"end":1643},{"id":"PF00972","name":"Flavivirus RNA-directed RNA polymerase, fingers and palm domains","start":2742,"end":3191},{"id":"PF01002","name":"Flavivirus non-structural protein NS2B","start":1349,"end":1475},{"id":"PF01003","name":"Flavivirus capsid protein C","start":5,"end":113},{"id":"PF01004","name":"Flavivirus envelope glycoprotein M","start":207,"end":279},{"id":"PF01005","name":"Flavivirus non-structural protein NS2A","start":1138,"end":1327},{"id":"PF01349","name":"Flavivirus non-structural protein NS4B","start":2244,"end":2484},{"id":"PF01350","name":"Flavivirus non-structural protein NS4A","start":2099,"end":2240},{"id":"PF01570","name":"Flavivirus polyprotein propeptide","start":120,"end":204},{"id":"PF01728","name":"FtsJ-like methyltransferase","start":2546,"end":2713},{"id":"PF02832","name":"Flavivirus glycoprotein, immunoglobulin-like domain","start":578,"end":673},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1658,"end":1805},{"id":"PF20483","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","start":3196,"end":3358},{"id":"PF20907","name":"Flavivirus NS3 helicase, C-terminal helical domain","start":1949,"end":2091},{"id":"PF21659","name":"Flavivirus envelope glycoprotein E, stem/anchor domain","start":676,"end":770}],"gene3D":[{"start":342,"end":535,"id":"3.30.387.10","name":"Viral Envelope Glycoprotein, domain 3","_id":"685af523b4ac24d5329d86c7"},{"start":679,"end":775,"id":"1.20.1280.260","name":"1.20.1280.260","_id":"685af523b4ac24d5329d86c8"},{"start":21,"end":100,"id":"1.10.10.930","name":"1.10.10.930","_id":"685af523b4ac24d5329d86c9"},{"start":206,"end":280,"id":"1.10.8.970","name":"Flavivirus envelope glycoprotein M-like","_id":"685af523b4ac24d5329d86ca"},{"start":572,"end":678,"id":"2.60.40.350","name":"2.60.40.350","_id":"685af523b4ac24d5329d86cb"},{"start":332,"end":554,"id":"3.30.67.10","name":"Viral Envelope Glycoprotein, domain 2","_id":"685af523b4ac24d5329d86cc"},{"start":115,"end":195,"id":"2.60.260.50","name":"Flavivirus polyprotein propeptide domain","_id":"685af523b4ac24d5329d86cd"},{"start":283,"end":571,"id":"2.60.98.10","name":"Tick-borne Encephalitis virus Glycoprotein, domain 1","_id":"685af523b4ac24d5329d86ce"},{"start":3019,"end":3087,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d86cf"},{"start":2885,"end":2980,"id":"1.10.260.90","name":"1.10.260.90","_id":"685af523b4ac24d5329d86d0"},{"start":2761,"end":2827,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d86d1"},{"start":2492,"end":2760,"id":"3.40.50.150","name":"Vaccinia Virus protein VP39","_id":"685af523b4ac24d5329d86d2"},{"start":1658,"end":1991,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d86d3"},{"start":2832,"end":2872,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d86d4"},{"start":1469,"end":1642,"id":"2.40.10.10","name":"Trypsin-like serine proteases","_id":"685af523b4ac24d5329d86d5"},{"start":1797,"end":1956,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d86d6"},{"start":1496,"end":1564,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d86d7"},{"start":1389,"end":1452,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d86d8"}]},"genes":[],"length":3391,"name":"Genome polyprotein","ncbi_taxon_id":11065,"organism":"Dengue virus type 2 (strain Thailand/NGS-C/1944)","regions_counter":9,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Flavivirus"],"UniParc":"UPI0000131DFA","uniref100":"UniRef100_P14340","uniref50":"UniRef50_P17763","uniref90":"UniRef90_P29990","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"4UIH","_id":"685af523b4ac24d5329d86e5"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006208","ec_name":"cryogenic electron microscopy evidence used in manual assertion","ec_ontology":"ECO","start":676,"end":775,"interaction_partner":[],"reference_html":"DENGUE VIRUS. Cryo-EM structure of an antibody that neutralizes dengue virus type 2 by locking E protein dimers. <i> Fibriansah G, Ibarra KD, Ng TS, Smith SA, Tan JL, Lim XN, Ooi JS, Kostyuchenko VA, Wang J, de Silva AM, Harris E, Crowe JE, Lok SM. </i> Science, 2015","reference_id":"26138979","region_id":"DP00876r006","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The PDB shows the disorder region from 676-775 (envelope protein E).","_id":"685af523b4ac24d5329d86e6"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-26T07:28:50.594Z","_id":"685af523b4ac24d5329d86e7"},"version":1,"_id":"685af523b4ac24d5329d86e4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6IZX","_id":"685af523b4ac24d5329d86e9"},{"db":"PDB","id":"6IZY","_id":"685af523b4ac24d5329d86ea"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":2742,"end":2761,"interaction_partner":[],"reference_html":"Discovery of a small molecule inhibitor targeting dengue virus NS5 RNA-dependent RNA polymerase. <i> Shimizu H, Saito A, Mikuni J, Nakayama EE, Koyama H, Honma T, Shirouzu M, Sekine SI, Shioda T. </i> PLoS Negl Trop Dis, 2019","reference_id":"31738758","region_id":"DP00876r007","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The PDB shows the disorder region from 2742-2761 (NS5 RNA-dependent RNA polymerase).","_id":"685af523b4ac24d5329d86eb"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-26T08:38:27.179Z","_id":"685af523b4ac24d5329d86ec"},"version":1,"_id":"685af523b4ac24d5329d86e8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6IZX","_id":"685af523b4ac24d5329d86ee"},{"db":"PDB","id":"6IZY","_id":"685af523b4ac24d5329d86ef"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":2947,"end":2963,"interaction_partner":[],"reference_html":"Discovery of a small molecule inhibitor targeting dengue virus NS5 RNA-dependent RNA polymerase. <i> Shimizu H, Saito A, Mikuni J, Nakayama EE, Koyama H, Honma T, Shirouzu M, Sekine SI, Shioda T. </i> PLoS Negl Trop Dis, 2019","reference_id":"31738758","region_id":"DP00876r008","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The PDB shows the disorder region from 2947-2963 (NS5 RNA-dependent RNA polymerase).","_id":"685af523b4ac24d5329d86f0"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-26T08:38:29.177Z","_id":"685af523b4ac24d5329d86f1"},"version":1,"_id":"685af523b4ac24d5329d86ed","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-21T19:18:28.690Z","disprot_namespace":"Structural state","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":22,"interaction_partner":[],"reference_html":"Fast NMR method to probe solvent accessibility and disordered regions in proteins. <i> Faustino AF, Barbosa GM, Silva M, Castanho MARB, Da Poian AT, Cabrita EJ, Santos NC, Almeida FCL, Martins IC. </i> Sci Rep, 2019","reference_id":"30733478","region_id":"DP00876r009","released":"2022_12","sample":[],"statement":[{"type":"Results","text":"The main structural regions are distinguished by their average backbone solvent accessibility (Fig. 3, left panel): the disordered N-terminal backbone is highly exposed, the flexible fold is partially accessible, and the conserved fold is mostly inaccessible to the solvent.","_id":"685af523b4ac24d5329d86f3"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-15T17:07:50.861Z","_id":"685af523b4ac24d5329d86f4"},"version":0,"_id":"685af523b4ac24d5329d86f2","reference_source":"pmid"}],"__v":0,"disorder_content":0.0468888233559422,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"},{"start":676,"end":775,"type":"D"},{"start":2742,"end":2761,"type":"D"},{"start":2947,"end":2963,"type":"D"}],"Structural state":[{"start":1,"end":22,"type":"D"},{"start":676,"end":775,"type":"D"},{"start":2742,"end":2761,"type":"D"},{"start":2947,"end":2963,"type":"D"}]}},{"acc":"P9WHN5","sequence":"MAQEQTKRGGGGGDDDDIAGSTAAGQERREKLTEETDDLLDEIDDVLEENAEDFVRAYVQKGGQ","alphafold_very_low_content":"0.0625","creator":"mnecci","dataset":[],"date":"2016-08-30T17:35:46.000Z","disprot_id":"DP00877","features":{"pfam":[{"id":"PF05639","name":"Pup-like protein","start":5,"end":64}]},"genes":[{"name":{"value":"pup","evidences":[],"_id":"685af523b4ac24d5329d8745"},"synonyms":[],"olnNames":[{"value":"Rv2111c","evidences":[],"_id":"685af523b4ac24d5329d8746"}],"orfNames":[],"_id":"685af523b4ac24d5329d8744"}],"length":64,"name":"Prokaryotic ubiquitin-like protein Pup","ncbi_taxon_id":83332,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","regions_counter":25,"released":"2016_10","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"UniParc":"UPI00000D107E","uniref100":"UniRef100_Q7TZ12","uniref50":"UniRef50_A0QFB4","uniref90":"UniRef90_Q7TZ12","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":64,"interaction_partner":[],"reference_html":"Prokaryotic ubiquitin-like protein pup is intrinsically disordered. <i> Chen X, Solomon WC, Kang Y, Cerda-Maira F, Darwin KH, Walters KJ. </i> J Mol Biol, 2009","reference_id":"19607839","region_id":"DP00877r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"We found that Pup runs at 14 kDa on an SDS gel as demonstrated previously.","_id":"685af523b4ac24d5329d86f7"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-30T10:46:39.922Z","_id":"685af523b4ac24d5329d86f8"},"version":3,"_id":"685af523b4ac24d5329d86f6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":64,"interaction_partner":[],"reference_html":"Pup, a prokaryotic ubiquitin-like protein, is an intrinsically disordered protein. <i> Liao S, Shang Q, Zhang X, Zhang J, Xu C, Tu X. </i> Biochem J, 2009","reference_id":"19580545","region_id":"DP00877r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Moreover, a CD spectrum of Pup under physiological condition displays a single minimum, at approx. 200 nm,\nwhich is the characteristic of unstructured proteins (Figure 2D).\nThis observation further strengthens the suggestion that Pup is an\nIDP. Meanwhile, there is a broad but weak negative ‘shoulder’\npeak between 218 nm and 230 nm, implying the existence of\na small proportion of residual secondary structure","_id":"685af523b4ac24d5329d86fa"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-30T10:46:17.133Z","_id":"685af523b4ac24d5329d86fb"},"version":3,"_id":"685af523b4ac24d5329d86f9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":64,"interaction_partner":[],"reference_html":"Pup, a prokaryotic ubiquitin-like protein, is an intrinsically disordered protein. <i> Liao S, Shang Q, Zhang X, Zhang J, Xu C, Tu X. </i> Biochem J, 2009","reference_id":"19580545","region_id":"DP00877r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Purified Pup displays an apparent molecular mass of 18 kDa\n(Figure 2C), in comparison to a theoretical molecular mass of\n8 kDa. The abnormal electrophoresis shift rate of Pup in SDS/PAGE might reflect its amino acid composition bias and extended\nconformation.","_id":"685af523b4ac24d5329d86fd"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-30T10:46:13.196Z","_id":"685af523b4ac24d5329d86fe"},"version":3,"_id":"685af523b4ac24d5329d86fc","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":64,"interaction_partner":[],"reference_html":"Prokaryotic ubiquitin-like protein pup is intrinsically disordered. <i> Chen X, Solomon WC, Kang Y, Cerda-Maira F, Darwin KH, Walters KJ. </i> J Mol Biol, 2009","reference_id":"19607839","region_id":"DP00877r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"A spectrum recorded on Pup reflects that\nof a disordered polypeptide with negative ellipticity near 200 nm and low ellipticity at 190 and\n222 nm (Figure 3a). Moreover, induced thermal melting did not produce the spectral transition\ncharacteristic of cooperative protein unfolding, thus providing further evidence for Pup being\nan intrinsically disordered protein (Figure 3b).","_id":"685af523b4ac24d5329d8700"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-30T10:43:37.778Z","_id":"685af523b4ac24d5329d8701"},"version":3,"_id":"685af523b4ac24d5329d86ff","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":64,"interaction_partner":[],"reference_html":"Prokaryotic ubiquitin-like protein pup is intrinsically disordered. <i> Chen X, Solomon WC, Kang Y, Cerda-Maira F, Darwin KH, Walters KJ. </i> J Mol Biol, 2009","reference_id":"19607839","region_id":"DP00877r005","released":"2022_03","sample":[],"statement":[{"type":"Figure","text":"Size exclusion chromatrography by FPLC reveals that 6.9 kDa Pup has a larger\nhydrodynamic radius than 8.6 kDa ubiquitin.","_id":"685af523b4ac24d5329d8703"},{"type":"Results","text":"Pup also elutes earlier than expected during size exclusion\nchromatography however. It directly follows the 16.7 kDa ubiquitin receptor Rpn13 and elutes\nsignificantly earlier than 8.6 kDa ubiquitin (Figure 1b), which forms a compact structure\n(Figure 1c)","_id":"685af523b4ac24d5329d8704"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-30T10:43:31.680Z","_id":"685af523b4ac24d5329d8705"},"version":3,"_id":"685af523b4ac24d5329d8702","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":64,"interaction_partner":[],"reference_html":"A distinct structural region of the prokaryotic ubiquitin-like protein (Pup) is recognized by the N-terminal domain of the proteasomal ATPase Mpa. <i> Sutter M, Striebel F, Damberger FF, Allain FH, Weber-Ban E. </i> FEBS Lett, 2009","reference_id":"19761766","region_id":"DP00877r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Even in the absence of denaturant, the CD spec-\ntrum of Pup displays a strongly negative mean molar ellipticity\nwith a minimum at slightly below 200 nm, a feature indicative of\npoorly structured proteins. However, a broad and low-amplitude negative band at around 225 nm predicts a low content of second-\nary structure.","_id":"685af523b4ac24d5329d8707"},{"type":"Discussion","text":"CD analysis of Pup indicates that Pup is mostly disordered and\ncontains only a small amount of secondary structure.","_id":"685af523b4ac24d5329d8708"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d8706","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3M91","_id":"685af523b4ac24d5329d8710"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":20,"interaction_partner":[],"reference_html":"Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation. <i> Wang T, Darwin KH, Li H. </i> Nat Struct Mol Biol, 2010","reference_id":"20953180","region_id":"DP00877r010","released":"2022_03","sample":[],"statement":[{"type":"Supplementary material","text":"Residues Mpa1-51, Pup1-20, Pup52-64 were also disordered in the crystal\nstructure of Pup:Mpa1-234 complex structure","_id":"685af523b4ac24d5329d8711"},{"type":"Supplementary material","text":"Mpa46-51, Pup52-64 residues are\ndisordered in Mpa46-96:Pup21-64 complex structure.","_id":"685af523b4ac24d5329d8712"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d870f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":51,"end":64,"interaction_partner":[],"reference_html":"Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation. <i> Wang T, Darwin KH, Li H. </i> Nat Struct Mol Biol, 2010","reference_id":"20953180","region_id":"DP00877r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":" The C-terminal 52-64 residues of Pup were also disordered in the crystal, similar to what we observed in the Pup21-64:Mpa46-96 crystal structure; this unstructured region might serve as a flexible linker between the induced α-helix and the C-terminus that forms an isopeptide bond with a substrate.","_id":"685af523b4ac24d5329d8717"}],"states_connection":[],"term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","version":4,"_id":"685af523b4ac24d5329d8716","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":21,"end":51,"interaction_partner":[],"reference_html":"Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation. <i> Wang T, Darwin KH, Li H. </i> Nat Struct Mol Biol, 2010","reference_id":"20953180","region_id":"DP00877r014","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"Full-length Pup alone is randomly coiled and extended under physiologically relevant conditions in vitro. The randomly coiled state of Pup may increase its target capture radius, allowing it to find the proteasomal ATPase more easily. Once the C-terminal part of Pup contacts the Mpa coiled-coil, the pupylated substrate is “reeled” into the proteasomal ATPase, and the Pup N-terminus is gradually forced towards the OB channel in Mpa. The pulling of Pup’s N-terminus into the OB channel might subsequently pull the Pup helix away from the Mpa coiled-coil, causing Pup to unfold and thread further into the channel to reach the Mpa AAA region. This notion is supported by our structure demonstrating the displacement of the N-terminal half of the Pup helix (residues 21-30) from the Mpa coiled-coil (Fig. 2a-b), and by the observation that this region of Pup interacts more weakly with Mpa than the C-terminal half.","_id":"685af523b4ac24d5329d871c"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","version":4,"_id":"685af523b4ac24d5329d871b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3M9D","_id":"685af523b4ac24d5329d871e"},{"db":"PDB","id":"3M91","_id":"685af523b4ac24d5329d871f"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":21,"end":51,"interaction_partner":[],"reference_html":"Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation. <i> Wang T, Darwin KH, Li H. </i> Nat Struct Mol Biol, 2010","reference_id":"20953180","region_id":"DP00877r015","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"Based on our crystal structures and the existing biochemical data, we propose the following\nmechanism of substrate recognition in the Pup-proteasome system (Fig. 3c): (I) Pup is\ninitially in an unfolded state when covalently linked to a protein substrate by its C-terminus via an isopeptide bond 15,16,18,21; (II) unstructured Pup folds into an α-helix, using the\nMpa coiled-coil as a template; and (III) the protein substrate, along with Pup, is pulled into\nthe central channel of the proteasomal ATPase at the expense of ATP hydrolysis 5,22. At the\ninterface between Mpa and the 20S core particle, Pup might either be removed by a\n“depupylase” 23, or be pushed by Mpa further into the 20S core and degraded along with the\nsubstrate.","_id":"685af523b4ac24d5329d8720"},{"type":"Discussion","text":"Full-length Pup alone is\nrandomly coiled and extended under physiologically relevant conditions in vitro. The\nrandomly coiled state of Pup may increase its target capture radius, allowing it to find the\nproteasomal ATPase more easily.","_id":"685af523b4ac24d5329d8721"},{"type":"Results","text":"The Pup region extending from Ser21 to Ala51 folded into an α-helix, apparently using the\nMpa coiled-coil as a template.","_id":"685af523b4ac24d5329d8722"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d871d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3M9D","_id":"685af523b4ac24d5329d8724"},{"db":"PDB","id":"3M91","_id":"685af523b4ac24d5329d8725"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":21,"end":51,"interaction_partner":[{"db":"UniProt","id":"P9WQN5","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8726"}],"reference_html":"Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation. <i> Wang T, Darwin KH, Li H. </i> Nat Struct Mol Biol, 2010","reference_id":"20953180","region_id":"DP00877r016","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The Pup region extending from Ser21 to Ala51 folded into an α-helix, apparently using the\nMpa coiled-coil as a template.","_id":"685af523b4ac24d5329d8727"},{"type":"Results","text":"The Pup helix interacted in an anti-parallel fashion with the lower half of the Mpa\ncoiled-coil (Fig. 1c). The Pup surface interacting with the Mpa coiled-coil was mainly\nhydrophobic and involved two patches of leucine zipper-like interactions: a smaller patch\nbetween Leu32 of Pup and Leu87 and Ala86 of Mpa-Ha; and an extensive patch formed by\nLeu39, Leu40, Ile43, Val46, and Leu47 of Pup, Ala80, Leu73 of Mpa Ha, and Leu85,\nLeu84, Ala80, and Leu77 of Mpa Hb (Fig. 1d).","_id":"685af523b4ac24d5329d8728"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","version":4,"_id":"685af523b4ac24d5329d8723","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006198","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":21,"end":61,"interaction_partner":[{"db":"UniProt","id":"P9WQN5","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d872e"}],"reference_html":"Prokaryotic ubiquitin-like protein pup is intrinsically disordered. <i> Chen X, Solomon WC, Kang Y, Cerda-Maira F, Darwin KH, Walters KJ. </i> J Mol Biol, 2009","reference_id":"19607839","region_id":"DP00877r019","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"We used 1 H, 15 N HSQC experiments to test whether our Pup sample was functional for Mpa binding. S21–K61 attenuated upon Mpa addition and new Mpa-bound Pup resonances appeared","_id":"685af523b4ac24d5329d872f"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","version":4,"_id":"685af523b4ac24d5329d872d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":61,"interaction_partner":[],"reference_html":"Pup, a prokaryotic ubiquitin-like protein, is an intrinsically disordered protein. <i> Liao S, Shang Q, Zhang X, Zhang J, Xu C, Tu X. </i> Biochem J, 2009","reference_id":"19580545","region_id":"DP00877r020","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As expected for a disordered protein, the chemical shift dispersion of 15 N is rather good, whereas amide 1 H chemical\nshifts were dispersed over a narrow range from 7.8 to 8.6 p.p.m.,\nwhich characterizes an unfolded protein.","_id":"685af523b4ac24d5329d8731"},{"type":"Results","text":"Almost all of the heteronuclear NOEs are negative, indicating that most of the polypeptide chain adopts large amplitude fluctuations on a subnanosecond time scale. This implies a highly flexible state of Pup.","_id":"685af523b4ac24d5329d8732"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":1,"_id":"685af523b4ac24d5329d8730","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0001238","ec_name":"nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":30,"end":59,"interaction_partner":[{"db":"UniProt","id":"P9WQN5","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8734"}],"reference_html":"Pup, a prokaryotic ubiquitin-like protein, is an intrinsically disordered protein. <i> Liao S, Shang Q, Zhang X, Zhang J, Xu C, Tu X. </i> Biochem J, 2009","reference_id":"19580545","region_id":"DP00877r021","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"In the present paper, SPR (surface plasmon resonance) and NMR perturbation studies imply that the C-terminus of Pup, ranging from residues 30 to 59, binds\nto Mpa probably through a hydrophobic interface.","_id":"685af523b4ac24d5329d8735"},{"type":"Results","text":"At the same time, the weakening of\nsome other cross-peaks from residues in the region 32–55 was\nobserved (Figures 6A and 6B). Most of these perturbed residues\nare hydrophobic, implying that Pup binds to Mpa via hydrophobic\ninteractions. This is consistent with the observations from the SPR\nexperiment.","_id":"685af523b4ac24d5329d8736"},{"type":"Discussion","text":"The perturbed residues, most of\nwhich are hydrophobic, are located in the region 30 to 59. These\nobservations suggest that Pup binds to Mpa via the last 30\namino acids, mainly through a hydrophobic interaction.","_id":"685af523b4ac24d5329d8737"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":1,"_id":"685af523b4ac24d5329d8733","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0001238","ec_name":"nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":64,"interaction_partner":[],"reference_html":"Prokaryotic ubiquitin-like protein pup is intrinsically disordered. <i> Chen X, Solomon WC, Kang Y, Cerda-Maira F, Darwin KH, Walters KJ. </i> J Mol Biol, 2009","reference_id":"19607839","region_id":"DP00877r022","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"We plotted the difference between the chemical shift values of Pup’s Cα and Hα atoms relative\nto those of randomly coiled values applying sequence-dependent corrections 21 to find very\nlittle deviation from the random coil values (Figure 2b). Only A51–A57 demonstrated a trend\ntowards helicity with slight, but consistent Cα downfield shifting and Hα upfield shifting","_id":"685af523b4ac24d5329d8739"},{"type":"Results","text":"Compared to ubiquitin 22 , Pup exhibits significantly smaller hetNOE\nvalues, with an average of 0.16 (at 800 MHz; Figure 4c) compared to ubiquitin’s average of\n0.75 (at 750 MHz) 22 , thus revealing an increase of high frequency motions. Pup’s last three\nC-terminal residues, its N-terminal end, and R29–K31 demonstrate enhanced flexible (Figure\n4c). R29–K31 and V55–V59 exhibit faster than average R N (N X ) values (Figure 4b), providing\nfurther evidence that these two regions undergo conformational exchange.","_id":"685af523b4ac24d5329d873a"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":1,"_id":"685af523b4ac24d5329d8738","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":52,"end":64,"interaction_partner":[],"reference_html":"Prokaryotic ubiquitin-like protein pup is intrinsically disordered. <i> Chen X, Solomon WC, Kang Y, Cerda-Maira F, Darwin KH, Walters KJ. </i> J Mol Biol, 2009","reference_id":"19607839","region_id":"DP00877r023","released":"2022_03","sample":[],"statement":[{"type":"Supplementary material","text":"Residues Mpa1-51, Pup1-20, Pup52-64 were also disordered in the crystal\nstructure of Pup:Mpa1-234 complex structure","_id":"685af523b4ac24d5329d873c"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":1,"_id":"685af523b4ac24d5329d873b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":64,"interaction_partner":[],"reference_html":"A distinct structural region of the prokaryotic ubiquitin-like protein (Pup) is recognized by the N-terminal domain of the proteasomal ATPase Mpa. <i> Sutter M, Striebel F, Damberger FF, Allain FH, Weber-Ban E. </i> FEBS Lett, 2009","reference_id":"19761766","region_id":"DP00877r024","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The [ 15 N, 1 H]-HSQC spectrum of Pup shows poor dispersion\nwhich is characteristic for an unfolded protein","_id":"685af523b4ac24d5329d873e"},{"type":"Results","text":"We characterized the degree of flexibility in the backbone of\nPup using the 15 N{ 1 H}-NOE experiment (Fig. 3b,c). Whereas the\nN- and C-terminal residues show negative NOE values indicating\nunrestricted motion of the N–H bond vector on the nanosecond\ntimescale, most residues of Pup have values between 0.2 and 0.4,\nshowing some degree of motional restriction of the backbone\n(Fig. 3b and c). This confirms that Pup is not entirely unstructured\nin its free form.","_id":"685af523b4ac24d5329d873f"},{"type":"Discussion","text":"15 N{ 1 H}-NOE experiment indicates that the protein\nis partially structured, although it does not appear to occupy one\nsingle favored conformation. Structure calculations using as input\nthe nearly complete resonance assignments and the NOESY spectra\ndo not converge to a single folded conformation. However, the res-\nidues 50–58 adopt a helical conformation. Although this region\nshows residual helical structure in these preliminary calculations,\nthe remainder of Pup occupies a range of conformations.","_id":"685af523b4ac24d5329d8740"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":1,"_id":"685af523b4ac24d5329d873d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":21,"end":58,"interaction_partner":[{"db":"UniProt","id":"P9WQN5","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8742"}],"reference_html":"A distinct structural region of the prokaryotic ubiquitin-like protein (Pup) is recognized by the N-terminal domain of the proteasomal ATPase Mpa. <i> Sutter M, Striebel F, Damberger FF, Allain FH, Weber-Ban E. </i> FEBS Lett, 2009","reference_id":"19761766","region_id":"DP00877r025","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The observed\nline-broadening clearly indicates interaction between Pup and\nMpa-CC. The most strongly affected 1 H– 15 N signals identify the\nMpa-CC binding region in Pup between residues 21 and 58.","_id":"685af523b4ac24d5329d8743"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":1,"_id":"685af523b4ac24d5329d8741","reference_source":"pmid"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"D"},{"start":21,"end":51,"type":"T"},{"start":52,"end":64,"type":"D"}],"Structural state":[{"start":1,"end":64,"type":"D"}],"Disorder function":[{"start":51,"end":64,"type":"F"}],"Molecular function":[{"start":21,"end":61,"type":"F"}],"Structural transition":[{"start":21,"end":51,"type":"T"}]}},{"features":{"pfam":[{"id":"PF18557","name":"Anti-sigma factor NepR","start":28,"end":55}]},"uniref50":"UniRef50_A0A2A2KBP6","sequence":"MLDLPGNKDKKASSKKSPAKVQSKDRDMGAALRSAYQKTIEEQVPDEMLDLLNKLA","taxonomy":["Bacteria","Proteobacteria","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"],"uniref90":"UniRef90_A0A2A2KBP6","disprot_id":"DP00878","ncbi_taxon_id":907061,"regions_counter":5,"creator":"mmacossay","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":56,"region_id":"DP00878r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis for sigma factor mimicry in the general stress response of Alphaproteobacteria. <i> Campagne S, Damberger FF, Kaczmarczyk A, Francez-Charlot A, Allain FH, Vorholt JA. </i> Proc Natl Acad Sci U S A, 2012","term_id":"IDPO:0000002","curator_id":"mmacossay","start":28,"term_ontology":"IDPO","curator_name":"Mauricio Macossay-Castillo","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2LFW"}],"reference_id":"22550171","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":56,"term_name":"molecular function inhibitor activity","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis for sigma factor mimicry in the general stress response of Alphaproteobacteria. <i> Campagne S, Damberger FF, Kaczmarczyk A, Francez-Charlot A, Allain FH, Vorholt JA. </i> Proc Natl Acad Sci U S A, 2012","term_id":"GO:0140678","curator_id":"mmacossay","start":28,"term_ontology":"GO","curator_name":"Mauricio Macossay-Castillo","reference_id":"22550171","version":3,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00878r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":56,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis for sigma factor mimicry in the general stress response of Alphaproteobacteria. <i> Campagne S, Damberger FF, Kaczmarczyk A, Francez-Charlot A, Allain FH, Vorholt JA. </i> Proc Natl Acad Sci U S A, 2012","term_id":"IDPO:0000011","curator_id":"mmacossay","start":28,"term_ontology":"IDPO","curator_name":"Mauricio Macossay-Castillo","reference_id":"22550171","version":2,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00878r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":56,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis for sigma factor mimicry in the general stress response of Alphaproteobacteria. <i> Campagne S, Damberger FF, Kaczmarczyk A, Francez-Charlot A, Allain FH, Vorholt JA. </i> Proc Natl Acad Sci U S A, 2012","term_id":"GO:0005515","curator_id":"mmacossay","start":28,"term_ontology":"GO","curator_name":"Mauricio Macossay-Castillo","reference_id":"22550171","version":3,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00878r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":27,"region_id":"DP00878r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis for sigma factor mimicry in the general stress response of Alphaproteobacteria. <i> Campagne S, Damberger FF, Kaczmarczyk A, Francez-Charlot A, Allain FH, Vorholt JA. </i> Proc Natl Acad Sci U S A, 2012","term_id":"IDPO:0000002","curator_id":"mmacossay","start":1,"term_ontology":"IDPO","curator_name":"Mauricio Macossay-Castillo","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2LFW"}],"reference_id":"22550171","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_A0A2A2KBP6","date":"2016-08-30T18:16:23.000Z","acc":"G8HXD9","name":"NepR","length":56,"organism":"Sphingomonas sp. Fr1","dataset":[],"UniParc":"UPI00023945A7","genes":[{"name":{"value":"nepR","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AET62590.1","url":"https://www.ebi.ac.uk/ena/browser/view/AET62590.1"}}]}}],"alphafold_very_low_content":0.14285714285714285,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":27,"type":"D"},{"start":28,"end":56,"type":"T"}],"Structural state":[{"start":1,"end":56,"type":"D"}],"Molecular function":[{"start":28,"end":56,"type":"F"}],"Structural transition":[{"start":28,"end":56,"type":"T"}]}},{"features":{"pfam":[{"id":"PF03297","name":"S25 ribosomal protein","start":12,"end":111}],"gene3D":[{"start":41,"end":125,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}]},"uniref50":"UniRef50_G1MYF9","sequence":"PPKDDKKKKDAGKSAKKDKDPVNKSGGKAKKKKWSKGKVRDKLNNLVLFDKATYDKLCKEVPNYKLITPAVVSERLKIRGSLARAALQELLSKGLIKLVSKHRAQVIYTRNTKGGDAPAAGEDA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Lagomorpha","Leporidae","Oryctolagus"],"uniref90":"UniRef90_G1TDB3","disprot_id":"DP00882","ncbi_taxon_id":9986,"regions_counter":2,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":39,"region_id":"DP00882r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The initiation of mammalian protein synthesis and mRNA scanning mechanism. <i> Lomakin IB, Steitz TA. </i> Nature, 2013","term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4KZX"},{"db":"PDB","id":"4KZY"}],"reference_id":"23873042","uniprot_changed":true,"statement":[{"text":"The N-terminal region (1-39) is missing but it was not mentioned in the article.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":124,"region_id":"DP00882r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The initiation of mammalian protein synthesis and mRNA scanning mechanism. <i> Lomakin IB, Steitz TA. </i> Nature, 2013","term_id":"IDPO:0000002","curator_id":"esalladini","start":115,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4KZX"},{"db":"PDB","id":"4KZY"}],"reference_id":"23873042","uniprot_changed":true,"statement":[{"text":"The C-terminal region (115-124) is missing but it was not mentioned in the article.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_G1TDB3","date":"2016-08-31T11:30:00.000Z","acc":"G1TDB3","name":"Uncharacterized protein","length":124,"organism":"Oryctolagus cuniculus","dataset":[],"uniparc":"UPI0000021166","genes":[],"alphafold_very_low_content":0.25,"disorder_content":0.3951612903225806,"disprot_consensus":{"full":[{"start":1,"end":39,"type":"D"},{"start":115,"end":124,"type":"D"}],"Structural state":[{"start":1,"end":39,"type":"D"},{"start":115,"end":124,"type":"D"}]}},{"features":{"pfam":[{"id":"PF08203","name":"Yeast RNA polymerase I subunit RPA14","start":15,"end":137}]},"uniref50":"UniRef50_P50106","sequence":"MMKGSRRTGNNTATTLNTPVVIHATQLPQHVSTDEVLQFLESFIDEKENIIDSTTMNTISGNAADADAAAVANTSLNIDTNLSSSISQLKRIQRDFKGLPPAQDFSAAPIQVSTTEKKETSIGVSATGGKKTTFADE","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P50106","disprot_id":"DP00884","ncbi_taxon_id":559292,"regions_counter":6,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":11,"region_id":"DP00884r001","released":"2022_12","ec_id":"ECO:0006220","reference_html":"RNA polymerase I structure and transcription regulation. <i> Engel C, Sainsbury S, Cheung AC, Kostrewa D, Cramer P. </i> Nature, 2013","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-22T18:57:19.729Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4C2M"}],"reference_id":"24153182","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The PDB corresponds to x-ray crystallographic evidence of the RNA polymerase I complex, form as a result of this protein interaction with multiple partners. The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":78,"region_id":"DP00884r002","released":"2022_12","ec_id":"ECO:0006220","reference_html":"RNA polymerase I structure and transcription regulation. <i> Engel C, Sainsbury S, Cheung AC, Kostrewa D, Cramer P. </i> Nature, 2013","term_id":"IDPO:0000002","curator_id":"vnugnes","start":49,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-22T18:57:05.136Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4C2M"}],"reference_id":"24153182","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The PDB corresponds to x-ray crystallographic evidence of the RNA polymerase I complex, form as a result of this protein interaction with multiple partners. The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":137,"region_id":"DP00884r003","released":"2022_12","ec_id":"ECO:0006220","reference_html":"RNA polymerase I structure and transcription regulation. <i> Engel C, Sainsbury S, Cheung AC, Kostrewa D, Cramer P. </i> Nature, 2013","term_id":"IDPO:0000002","curator_id":"vnugnes","start":101,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-22T18:56:37.202Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4C2M"}],"reference_id":"24153182","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The PDB corresponds to x-ray crystallographic evidence of the RNA polymerase I complex, form as a result of this protein interaction with multiple partners. The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":16,"region_id":"DP00884r004","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Functional architecture of RNA polymerase I. <i> Kuhn CD, Geiger SR, Baumli S, Gartmann M, Gerber J, Jennebach S, Mielke T, Tschochner H, Beckmann R, Cramer P. </i> Cell, 2007","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-22T18:58:03.967Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2RF4"}],"reference_id":"18160037","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P46669"}],"statement":[{"text":"The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ser55-Asn73del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ser113-Gle137del","start":null,"end":null,"position":null}],"sequence_construct":"MMKGSRRTGNNTATTLNTPVVIHATQLPQHVSTDEVLQFLESFIDEKENIIDIDTNLSSSISQLKRIQRDFKGLPPAQDFSAAPIQV"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":112,"region_id":"DP00884r006","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Functional architecture of RNA polymerase I. <i> Kuhn CD, Geiger SR, Baumli S, Gartmann M, Gerber J, Jennebach S, Mielke T, Tschochner H, Beckmann R, Cramer P. </i> Cell, 2007","term_id":"IDPO:0000002","curator_id":"vnugnes","start":103,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-22T18:58:13.988Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2RF4"}],"reference_id":"18160037","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":" P46669"}],"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ser55-Asn73del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ser113-Gle137del","start":null,"end":null,"position":null}],"sequence_construct":"MMKGSRRTGNNTATTLNTPVVIHATQLPQHVSTDEVLQFLESFIDEKENIIDIDTNLSSSISQLKRIQRDFKGLPPAQDFSAAPIQV"}],"released":"2016_10","uniref100":"UniRef100_P50106","date":"2016-09-01T10:30:55.000Z","acc":"P50106","name":"DNA-directed RNA polymerase I subunit RPA14","length":137,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI00001345BD","genes":[{"name":{"value":"RPA14"},"orfNames":[{"value":"YD8358.11"}],"olnNames":[{"value":"YDR156W"}]}],"alphafold_very_low_content":0.15328467153284672,"disorder_content":0.6058394160583942,"disprot_consensus":{"full":[{"start":1,"end":16,"type":"D"},{"start":49,"end":78,"type":"D"},{"start":101,"end":137,"type":"D"}],"Structural state":[{"start":1,"end":16,"type":"D"},{"start":49,"end":78,"type":"D"},{"start":101,"end":137,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01091","name":"PTN/MK heparin-binding protein family, C-terminal domain","start":82,"end":145},{"id":"PF05196","name":"PTN/MK heparin-binding protein family, N-terminal domain","start":25,"end":81}],"gene3D":[{"start":21,"end":77,"id":"2.20.60.10","name":"Pleiotrophin/Midkine, N-terminal domain"},{"start":78,"end":147,"id":"2.30.90.10","name":"Heparin-binding Growth Factor, Midkine; Chain A- C-terminal Domain"}]},"uniref50":"UniRef50_Q9DDG2","sequence":"MRSLFSIALVLVVVSMITVEASMKKKEKGKEPKADAECSEWQYGKCVPNSGDCGNGIREATCNEQTKKTKCKVPCNWKKDFGADCKYKFGRWAECDTTTGTRSRSGTLKKALFNAECQTTIKVSKPCTPKTPKPKGGEKKKGKGKEN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Actinopterygii","Neopterygii","Teleostei","Ostariophysi","Cypriniformes","Danionidae","Danioninae","Danio"],"uniref90":"UniRef90_Q9DDG2","disprot_id":"DP00885","ncbi_taxon_id":7955,"regions_counter":6,"creator":"smribeiro","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":36,"region_id":"DP00885r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure-function analysis of full-length midkine reveals novel residues important for heparin binding and zebrafish embryogenesis. <i> Lim J, Yao S, Graf M, Winkler C, Yang D. </i> Biochem J, 2013","term_id":"IDPO:0000002","curator_id":"smribeiro","start":20,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2LUU"}],"reference_id":"23418741","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":147,"region_id":"DP00885r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure-function analysis of full-length midkine reveals novel residues important for heparin binding and zebrafish embryogenesis. <i> Lim J, Yao S, Graf M, Winkler C, Yang D. </i> Biochem J, 2013","term_id":"IDPO:0000002","curator_id":"smribeiro","start":129,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2LUU"}],"reference_id":"23418741","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":147,"term_name":"flexible linker","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structure-function analysis of full-length midkine reveals novel residues important for heparin binding and zebrafish embryogenesis. <i> Lim J, Yao S, Graf M, Winkler C, Yang D. </i> Biochem J, 2013","term_id":"IDPO:0000033","curator_id":"smribeiro","start":129,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"23418741","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00885r006","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_Q9DDG2","date":"2016-09-01T12:21:13.000Z","acc":"Q9DDG2","name":"Midkine b","length":147,"organism":"Danio rerio","dataset":[],"UniParc":"UPI00000FC25C","genes":[{"name":{"value":"mdk2","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAG27035.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAG27035.1"}}]},"orfNames":[{"value":"SO:0001217","evidences":[{"code":"ECO:0000313","source":{"name":"ZFIN","id":"ZDB-GENE-010131-6","url":"http://zfin.org/cgi-bin/webdriver?MIval=aa-markerview.apg&OID=ZDB-GENE-010131-6"}}]}],"olnNames":[{"value":"mdkb","evidences":[{"code":"ECO:0000313","source":{"name":"Ensembl","id":"ENSDARP00000018513","url":"https://www.ensembl.org/id/ENSDARP00000018513"}},{"code":"ECO:0000313","source":{"name":"ZFIN","id":"ZDB-GENE-010131-6","url":"http://zfin.org/cgi-bin/webdriver?MIval=aa-markerview.apg&OID=ZDB-GENE-010131-6"}}]}]}],"alphafold_very_low_content":0.12244897959183673,"disorder_content":0.24489795918367346,"disprot_consensus":{"full":[{"start":20,"end":36,"type":"D"},{"start":129,"end":147,"type":"D"}],"Structural state":[{"start":20,"end":36,"type":"D"},{"start":129,"end":147,"type":"D"}],"Disorder function":[{"start":129,"end":147,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01016","name":"Ribosomal L27 protein","start":2,"end":80}],"gene3D":[{"start":21,"end":91,"id":"2.40.50.100","name":"2.40.50.100"}]},"uniref50":"UniRef50_Q9RY65","sequence":"MAHKKGVGSSKNGRDSNPKYLGVKKFGGEVVKAGNILVRQRGTKFKAGQGVGMGRDHTLFALSDGKVVFINKGKGARFISIEAAQTEVAAD","taxonomy":["Bacteria","Deinococcus-Thermus","Deinococci","Deinococcales","Deinococcaceae","Deinococcus"],"uniref90":"UniRef90_Q9RY65","disprot_id":"DP00886","ncbi_taxon_id":243230,"regions_counter":1,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":18,"region_id":"DP00886r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"High resolution structure of the large ribosomal subunit from a mesophilic eubacterium. <i> Harms J, Schluenzen F, Zarivach R, Bashan A, Gat S, Agmon I, Bartels H, Franceschi F, Yonath A. </i> Cell, 2001","term_id":"IDPO:0000002","curator_id":"atantos","start":1,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1KC9"}],"reference_id":"11733066","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q9RY65","date":"2016-09-01T12:51:55.000Z","acc":"Q9RY65","name":"50S ribosomal protein L27","length":91,"organism":"Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)","dataset":[],"UniParc":"UPI0000112804","genes":[{"name":{"value":"rpmA"},"olnNames":[{"value":"DR_0085"}]}],"alphafold_very_low_content":0.01098901098901099,"disorder_content":0.1978021978021978,"disprot_consensus":{"full":[{"start":1,"end":18,"type":"D"}],"Structural state":[{"start":1,"end":18,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01091","name":"PTN/MK heparin-binding protein family, C-terminal domain","start":96,"end":158},{"id":"PF05196","name":"PTN/MK heparin-binding protein family, N-terminal domain","start":34,"end":95}],"gene3D":[{"start":33,"end":94,"id":"2.20.60.10","name":"Pleiotrophin/Midkine, N-terminal domain"},{"start":95,"end":163,"id":"2.30.90.10","name":"Heparin-binding Growth Factor, Midkine; Chain A- C-terminal Domain"}]},"uniref50":"UniRef50_P21246","sequence":"MQAQQYQQQRRKFAAAFLAFIFILAAVDTAEAGKKEKPEKKVKKSDCGEWQWSVCVPTSGDCGLGTREGTRTGAECKQTMKTQRCKIPCNWKKQFGAECKYQFQAWGECDLNTALKTRTGSLKRALHNAECQKTVTISKPCGKLTKPKPQAESKKKKKEGKKQEKMLD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P21246","disprot_id":"DP00887","ncbi_taxon_id":9606,"regions_counter":14,"creator":"eschad","regions":[{"start":32,"end":46,"reference_id":"26896299","reference_source":"pmid","reference_html":"Structural studies reveal an important role for the pleiotrophin C-terminus in mediating interactions with chondroitin sulfate. <i> Ryan E, Shen D, Wang X. </i> FEBS J, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2N6F"}],"region_id":"DP00887r003","statement":[{"text":"In agreement with the previous study of PTN [27], we found that PTN is comprised of two TSR domains flanked by unstructured termini. Because no interdomain NOE was detected between the CTD and NTD, the two domains appear to be largely independent of each other and do not have a well-defined interdomain orientation.","type":"Results"},{"text":"The structured regions based on inspection of 2n6f are as follows: N-tail: 32-46; NTD (47-83), CTD (99-139), C-tail (140-168). The hinge region that is not constrained to the CTD corresponds to residues: 84-95. Numbering in the paper does not follow UNIPROT numbering. i.e. F63 corresponds to F95 and K60-K61 corresponds to UNIPROT: K92, K93.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T07:14:27.471Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":140,"end":168,"reference_id":"26896299","reference_source":"pmid","reference_html":"Structural studies reveal an important role for the pleiotrophin C-terminus in mediating interactions with chondroitin sulfate. <i> Ryan E, Shen D, Wang X. </i> FEBS J, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2N6F"}],"region_id":"DP00887r004","statement":[{"text":"In agreement with the previous study of PTN [27], we found that PTN is comprised of two TSR domains flanked by unstructured termini. Because no interdomain NOE was detected between the CTD and NTD, the two domains appear to be largely independent of each other and do not have a well-defined interdomain orientation.","type":"Results"},{"text":"The structured regions based on inspection of 2n6f are as follows: N-tail: 32-46; NTD (47-83), CTD (99-139), C-tail (140-168). The hinge region that is not constrained to the CTD corresponds to residues: 84-95. Numbering in the paper does not follow UNIPROT numbering. i.e. F63 corresponds to F95 and K60-K61 corresponds to UNIPROT: K92, K93.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T07:14:23.449Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":84,"end":95,"reference_id":"26896299","reference_source":"pmid","reference_html":"Structural studies reveal an important role for the pleiotrophin C-terminus in mediating interactions with chondroitin sulfate. <i> Ryan E, Shen D, Wang X. </i> FEBS J, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2N6F"}],"region_id":"DP00887r005","statement":[{"text":"In agreement with the previous study of PTN [27], we found that PTN is comprised of two TSR domains flanked by unstructured termini. Because no interdomain NOE was detected between the CTD and NTD, the two domains appear to be largely independent of each other and do not have a well-defined interdomain orientation.","type":"Results"},{"text":"Definitive NOE cross-peaks between CTD and residues in the hinge segment connecting the two TSR domains (residues 58–66) can be observed. Specifically, aromatic protons of F63 can be seen contacting side chains of Y69, V103 and I105 (Fig. 1D). Because F63 is the only residue with significant contacts with the CTD and the tolerance in these distance constraints is relatively large, the hinge shows larger positional variation than the TSR domains.","type":"Results"},{"text":"The structured regions based on inspection of 2n6f are as follows: N-tail: 32-46; NTD (47-83), CTD (99-139), C-tail (140-168). The hinge region that is not constrained to the CTD corresponds to residues: 84-95. Numbering in the paper does not follow UNIPROT numbering. i.e. F63 corresponds to F95 and K60-K61 corresponds to UNIPROT: K92, K93.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T07:13:04.016Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":84,"end":95,"reference_id":"26896299","reference_source":"pmid","reference_html":"Structural studies reveal an important role for the pleiotrophin C-terminus in mediating interactions with chondroitin sulfate. <i> Ryan E, Shen D, Wang X. </i> FEBS J, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"2N6F"}],"region_id":"DP00887r006","statement":[{"text":"Our structure shows that PTN possesses large basic surfaces on both of its structured domains and also that residues in the hinge segment connecting the domains have significant contacts with the C-terminal domain. Our analysis of PTN–CS interactions showed that the C-terminal tail of PTN is essential for maintaining stable interactions with chondroitin sulfate A, the type of CS commonly found on PTPRZ.","type":"Abstract"},{"text":"Definitive NOE cross-peaks between CTD and residues in the hinge segment connecting the two TSR domains (residues 58–66) can be observed. Specifically, aromatic protons of F63 can be seen contacting side chains of Y69, V103 and I105 (Fig. 1D). Because F63 is the only residue with significant contacts with the CTD and the tolerance in these distance constraints is relatively large, the hinge shows larger positional variation than the TSR domains.","type":"Results"},{"text":"The structured regions based on inspection of 2n6f are as follows: N-tail: 32-46; NTD (47-83), CTD (99-139), C-tail (140-168). The hinge region that is not constrained to the CTD corresponds to residues: 84-95. Numbering in the paper does not follow UNIPROT numbering. i.e. F63 corresponds to F95 and K60-K61 corresponds to UNIPROT: K92, K93.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T07:16:22.581Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":147,"end":168,"reference_id":"26896299","reference_source":"pmid","reference_html":"Structural studies reveal an important role for the pleiotrophin C-terminus in mediating interactions with chondroitin sulfate. <i> Ryan E, Shen D, Wang X. </i> FEBS J, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"GO:0030246","term_name":"carbohydrate binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005581","ec_ontology":"ECO","ec_name":"enzyme-linked immunoabsorbent assay evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00887r007","statement":[{"text":"Our analysis of PTN–CS interactions showed that the C-terminal tail of PTN is essential for maintaining stable interactions with chondroitin sulfate A, the type of CS commonly found on PTPRZ.","type":"Abstract"},{"text":"Furthermore, studies have also shown that truncated PTN missing the C-terminal tail (residues 115–136) can be found in vivo in significant quantities but is incapable of signaling through PTPRZ [35–37]. In addition, peptides derived from the C-terminal tail of PTN can inhibit PTPRZ-dependent cell migration [38]. This implies that the C-terminal tail, which does not contribute to heparin binding, plays an important role in interactions with PTPRZ.","type":"Introduction"},{"text":"However, truncated PTN failed to bind to CSA entirely, whereas wild-type PTN binds CSA with high affinity (Kd ~ 17 nM). These data indicate that the Cterminal tail of PTN is crucial for maintaining strong interactions with CSA, the type of CS commonly found on PTPRZ.","type":"Results"},{"text":"Work reported in the present study shows that, although the C-terminal tail plays a minimal role in binding the highly sulfated CSE, it is vital for maintaining stable interactions with CSA. Because more than 90% of disaccharides in the GAG chains of PTPRZ are CSA disaccharides [42], the Cterminal tail of PTN is demonstrated to be a crucial mediator of the interaction of PTN with PTPRZ. ","type":"Discussion"},{"text":"The C-terminal truncation: residues 115-136 discussed by the authors corresponds to residues 147-168 of the Uniprot entry","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T07:16:01.697Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.\" [GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":147,"end":168,"reference_id":"26896299","reference_source":"pmid","reference_html":"Structural studies reveal an important role for the pleiotrophin C-terminus in mediating interactions with chondroitin sulfate. <i> Ryan E, Shen D, Wang X. </i> FEBS J, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"GO:0030246","term_name":"carbohydrate binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00887r008","statement":[{"text":"Our analysis of PTN–CS interactions showed that the C-terminal tail of PTN is essential for maintaining stable interactions with chondroitin sulfate A, the type of CS commonly found on PTPRZ.","type":"Abstract"},{"text":"Furthermore, studies have also shown that truncated PTN missing the C-terminal tail (residues 115–136) can be found in vivo in significant quantities but is incapable of signaling through PTPRZ [35–37]. In addition, peptides derived from the C-terminal tail of PTN can inhibit PTPRZ-dependent cell migration [38]. This implies that the C-terminal tail, which does not contribute to heparin binding, plays an important role in interactions with PTPRZ.","type":"Introduction"},{"text":"In the absence of the Cterminal tail, CTD residues bound CSA dp8 with a Kd of only ~ 320 µM. Similarly, the CSA dp8 binding Kd of the NTD also doubled to 1.2 mM. This indicates that removal of the C-terminal tail has a significant effect on the affinity of PTN for CSA dp8 and is consistent with the results of the ELISA. It should be noted that the inability of truncated PTN to bind native CSA in ELISA does not contradict the results of the NMR titrations. The discrepancy can be explained by the successive washes required in ELISA, which prevents weak interactions ","type":"Results"},{"text":"Work reported in the present study shows that, although the C-terminal tail plays a minimal role in binding the highly sulfated CSE, it is vital for maintaining stable interactions with CSA. Because more than 90% of disaccharides in the GAG chains of PTPRZ are CSA disaccharides [42], the Cterminal tail of PTN is demonstrated to be a crucial mediator of the interaction of PTN with PTPRZ. ","type":"Discussion"},{"text":"The C-terminal truncation: residues 115-136 discussed by the authors corresponds to residues 147-168 of the Uniprot entry","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T07:16:00.121Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.\" [GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":144,"end":168,"reference_id":"21344482","reference_source":"pmid","reference_html":"A peptide corresponding to the C-terminal region of pleiotrophin inhibits angiogenesis in vivo and in vitro. <i> Mikelis C, Lamprou M, Koutsioumpa M, Koutsioubas AG, Spyranti Z, Zompra AA, Spiliopoulos N, Vradis AA, Katsoris P, Spyroulias GA, Cordopatis P, Courty J, Papadimitriou E. </i> J Cell Biochem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P05106","partner_start":null,"partner_end":null}],"region_id":"DP00887r009","statement":[{"text":"PTN112–136 inhibited binding of PTN to anb3 integrin, and as shown by surface plasmon resonance (SPR) measurements, specifically interacted with the specificity loop of the extracellular domain of b3. Moreover, it abolished PTN-induced FAK Y397 phosphorylation, similarly to the effect of a neutralizing anb3-selective antibody","type":"Abstract"},{"text":"PTN112_136 AFFECTED THE INTERACTION OF PTN WITH  anb3 INTEGRIN. Since both RPTPb/z and anb3 integrin are required for PTN-induced HUVEC migration [Polykratis et al., 2005; Mikelis et al., 2009], we studied whether PTN112–136 affects interaction of PTN with alphav b3, RPTPb/z, or both. Cells were grown in the presence or absence of PTN112–136 and in each case, 3mg of total protein from cell lysates were immunoprecipitated for anb3 or RPTPb/z and analyzed for the presence of PTN. PTN112–136 inhibited interaction of PTN with anb3 (Fig. 3A) but not RPTPb/z (Fig. 3B) in HUVEC.","type":"Results"},{"text":"The numbering by the authors differs from the uniprot numbering. Residue 112-136 correspond to 144-168 of the uniprot numbering.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T07:05:26.351Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":144,"end":168,"reference_id":"21344482","reference_source":"pmid","reference_html":"A peptide corresponding to the C-terminal region of pleiotrophin inhibits angiogenesis in vivo and in vitro. <i> Mikelis C, Lamprou M, Koutsioumpa M, Koutsioubas AG, Spyranti Z, Zompra AA, Spiliopoulos N, Vradis AA, Katsoris P, Spyroulias GA, Cordopatis P, Courty J, Papadimitriou E. </i> J Cell Biochem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P05106","partner_start":null,"partner_end":null}],"region_id":"DP00887r010","statement":[{"text":"PTN112–136 inhibited binding of PTN to anb3 integrin, and as shown by surface plasmon resonance (SPR) measurements, specifically interacted with the specificity loop of the extracellular domain of b3. Moreover, it abolished PTN-induced FAK Y397 phosphorylation, similarly to the effect of a neutralizing anb3-selective antibody","type":"Abstract"},{"text":"PTN112_136 SPECIFICALLY INTERACTED WITH THE CYSTEINE LOOP 177–184 OF THE b3 INTEGRIN EXTRACELLULAR DOMAIN. Since PTN interacts with anb3 through the specificity loop of the b3 integrin extracellular domain [Mikelis et al., 2009], we studied the interaction of PTN112–136 with a synthetic peptide that corresponds to aminoacids 177–184 and mimics the cysteine loop of b3 (B3 peptide) by using surface plasmon resonance (SPR)","type":"Results"},{"text":"Typical analyte–receptor binding kinetics are presented in Figure 4B. PTN112–136 and B3 peptide formed a relatively high affinity complex. The affinity of B3 peptide for PTN112–136 was much higher than the affinity of the B3 scrambled peptide.","type":"Results"},{"text":"In the present study, we show that the C-terminal region of PTN is responsible for binding to the Cys-loop of the b3 subunit, playing a major role in the interaction of PTN with anb3 and the resulting stimulation of cell migration.","type":"Discussion"},{"text":"The numbering by the authors differs from the uniprot numbering. Residue 112-136 correspond to 144-168 of the uniprot numbering.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T07:04:39.362Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":144,"end":168,"reference_id":"21344482","reference_source":"pmid","reference_html":"A peptide corresponding to the C-terminal region of pleiotrophin inhibits angiogenesis in vivo and in vitro. <i> Mikelis C, Lamprou M, Koutsioumpa M, Koutsioubas AG, Spyranti Z, Zompra AA, Spiliopoulos N, Vradis AA, Katsoris P, Spyroulias GA, Cordopatis P, Courty J, Papadimitriou E. </i> J Cell Biochem, 2011","date":"2024-05-14T16:39:47.321Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140677","term_name":"molecular function activator activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","released":"2024_06","version":5,"region_id":"DP00887r012","statement":[{"text":"PTN112–136 inhibited binding of PTN to anb3 integrin, and as shown by surface plasmon resonance (SPR) measurements, specifically interacted with the specificity loop of the extracellular domain of b3. Moreover, it abolished PTN-induced FAK Y397 phosphorylation, similarly to the effect of a neutralizing anb3-selective antibody","type":"Abstract"},{"text":"PTN112_136 AFFECTED THE INTERACTION OF PTN WITH  anb3 INTEGRIN. Since both RPTPb/z and anb3 integrin are required for PTN-induced HUVEC migration [Polykratis et al., 2005; Mikelis et al., 2009], we studied whether PTN112–136 affects interaction of PTN with alphav b3, RPTPb/z, or both. Cells were grown in the presence or absence of PTN112–136 and in each case, 3mg of total protein from cell lysates were immunoprecipitated for anb3 or RPTPb/z and analyzed for the presence of PTN. PTN112–136 inhibited interaction of PTN with anb3 (Fig. 3A) but not RPTPb/z (Fig. 3B) in HUVEC.","type":"Results"},{"text":"In the present study, we show that the C-terminal region of PTN is responsible for binding to the Cys-loop of the b3 subunit, playing a major role in the interaction of PTN with anb3 and the resulting stimulation of cell migration.","type":"Discussion"},{"text":"The numbering by the authors differs from the uniprot numbering. Residue 112-136 correspond to 144-168 of the uniprot numbering.","type":"Curator statement"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P05106","operator":"and","partner_start":null,"partner_end":null}]},{"start":144,"end":168,"reference_id":"21344482","reference_source":"pmid","reference_html":"A peptide corresponding to the C-terminal region of pleiotrophin inhibits angiogenesis in vivo and in vitro. <i> Mikelis C, Lamprou M, Koutsioumpa M, Koutsioubas AG, Spyranti Z, Zompra AA, Spiliopoulos N, Vradis AA, Katsoris P, Spyroulias GA, Cordopatis P, Courty J, Papadimitriou E. </i> J Cell Biochem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"IDPO:0000058","term_name":"self-activation","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005581","ec_ontology":"ECO","ec_name":"enzyme-linked immunoabsorbent assay evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00887r013","statement":[{"text":"PTN112–136 inhibited binding of PTN to anb3 integrin, and as shown by surface plasmon resonance (SPR) measurements, specifically interacted with the specificity loop of the extracellular domain of b3. Moreover, it abolished PTN-induced FAK Y397 phosphorylation, similarly to the effect of a neutralizing anb3-selective antibody","type":"Abstract"},{"text":"Collectively, our data suggest that although PTN112–136 induces some of the signaling pathways triggered by PTN, it inhibits PTN-induced angiogenic activities through inhibition of PTN binding to anb3 integrin. ","type":"Abstract"},{"text":"Based on the assumption that integrin-dependent Y397 autophosphorylation of FAK is the first step of its activation [Mitra and Schlaepfer, 2006], we studied whether PTN affects Y397 phosphorylation of FAK through anb3, as well as the effect of PTN112–136. As shown in Figure 5, PTN at the concentration of 100 ng/ml that causes the maximal effect on HUVEC migration [Polykratis et al., 2005], induced Y397 FAK auto-phosphorylation, an effect completely abolished by the anb3 neutralizing antibody LM609 or by PTN112–136","type":"Results"},{"text":"PTN induces Y397 FAK phosphorylation through anb3, an effect completely abolished by PTN112–136. FAK activation is required for integrin-mediated cell migration [Sieg et al., 1999] and the autophopshorylation on Y397 is prerequisite for the subsequent binding and activation from c-src [Mitra et al., 2005]. It seems that PTN binding to the cysteine loop 177–184 of anb3 leads to the initial activation of FAK, its interaction with the activated c-src and the induction of the migratory response, and PTN112–136 blocks this process (Fig. 8).","type":"Discussion"},{"text":"The numbering by the authors differs from the uniprot numbering. Residue 112-136 correspond to 144-168 of the uniprot numbering.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T07:06:56.624Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":144,"end":168,"reference_id":"21344482","reference_source":"pmid","reference_html":"A peptide corresponding to the C-terminal region of pleiotrophin inhibits angiogenesis in vivo and in vitro. <i> Mikelis C, Lamprou M, Koutsioumpa M, Koutsioubas AG, Spyranti Z, Zompra AA, Spiliopoulos N, Vradis AA, Katsoris P, Spyroulias GA, Cordopatis P, Courty J, Papadimitriou E. </i> J Cell Biochem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00887r014","statement":[{"text":"NMR spectroscopy studies showed that PTN112–136 was characterized by conformational flexibility and absence of any element of secondary structure at room temperature, although the biologically active peptide segment 123–132 may adopt a defined structure at lower temperature.","type":"Abstract"},{"text":"The NMR data for PTN112–136 suggest a conformation with no well-defined secondary structure elements for this peptide, due to the absence of any long-range and the limited number of medium-range (i,i.3) NOEs (Fig. 7B). However, a backbone bend is formed by residues Glu127–Gln131, indicating the formation of a segment with local folded structure in the conformational ensemble (Fig. 7C). As far as the nature of the peptide bond for both prolines is concerned, analysis of the proline 13C resonances observed for PTN112–136, demonstrate in both cases, Pro115 and Pro117, the existence of a dominant trans conformation. Cb of Pro115 is found to be at 33.172 ppm, while Cg is found at 29.632 ppm. The difference in ppm is 3.54, indicating that\nthe dominant conformation of the Lys114–Pro115 peptide bond of the model ensemble is trans and that cis–trans isomerization is not detectable in NMR time scale. The corresponding Dbg value for Pro117 is found to be 4.021, suggesting a trans conformation for the peptide bond between residues Lys116–Pro117\n","type":"Results"},{"text":"Based on the assumption that integrin-dependent Y397 autophosphorylation of FAK is the first step of its activation [Mitra and Schlaepfer, 2006], we studied whether PTN affects Y397 phosphorylation of FAK through anb3, as well as the effect of PTN112–136. As shown in Figure 5, PTN at the concentration of 100 ng/ml that causes the maximal effect on HUVEC migration [Polykratis et al., 2005], induced Y397 FAK auto-phosphorylation, an effect completely abolished by the anb3 neutralizing antibody LM609 or by PTN112–136","type":"Results"},{"text":"In an effort to better characterize PTN112–136 and to identify the\nlikely minimum amino acid sequence involved in its biological\nactivity, we elucidated the structural features of PTN112–136 by NMR\nspectroscopy. The peptide proved to be highly flexible in solution at\nroom temperature.","type":"Discussion"},{"text":"The numbering by the authors differs from the uniprot numbering. Residue 112-136 correspond to 144-168 of the uniprot numbering.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T07:03:58.320Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P21246","date":"2016-09-01T13:16:08.000Z","acc":"P21246","name":"Pleiotrophin","length":168,"organism":"Homo sapiens","dataset":["Extracellular matrix proteins"],"UniParc":"UPI000013297B","genes":[{"name":{"value":"PTN","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9630","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9630"}}]},"synonyms":[{"value":"HBNF1"},{"value":"NEGF1"}]}],"alphafold_very_low_content":0.16071428571428573,"disorder_content":0.3333333333333333,"disprot_consensus":{"full":[{"start":32,"end":46,"type":"D"},{"start":84,"end":95,"type":"D"},{"start":140,"end":168,"type":"D"}],"Structural state":[{"start":32,"end":46,"type":"D"},{"start":84,"end":95,"type":"D"},{"start":140,"end":168,"type":"D"}],"Disorder function":[{"start":84,"end":95,"type":"F"},{"start":144,"end":168,"type":"F"}],"Molecular function":[{"start":144,"end":168,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02604","name":"Antitoxin Phd_YefM, type II toxin-antitoxin system","start":1,"end":42}],"gene3D":[{"start":1,"end":39,"id":"3.40.1620.10","name":"YefM-like domain"}]},"uniref50":"UniRef50_P9WF18","sequence":"MSEVASRELRNDTAGVLRRVRAGEDVTITVSGRPVAVLTPVRPRRRRWLSKTEFLSRLRGAQADPGLRNDLAVLAGDTTEDLGPIR","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"uniref90":"UniRef90_P9WF18","disprot_id":"DP00889","dataset":["Unicellular toxins and antitoxins"],"ncbi_taxon_id":83332,"regions_counter":4,"creator":"atantos","regions":[{"region_id":"DP00889r004","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T09:59:35.712Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":45,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"Here we present the first crystal structure of a prokaryotic VapBC complex, VapBC-5 from M. tuberculosis. The toxin, VapC-5, contains 126 residues (Mr 14.0 kDa) and the antitoxin, VapB-5, contains 34 residues (Mr 3.8 kDa)","type":"Abstract"},{"text":"The structure of VapB-5 antitoxin shows clear electron density for 33 residues out of 93 (86 native and seven from the vector). The missing residues are part of the N-terminal region that is predicted to bind to DNA","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"18952600","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3DBO"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lchemes","reference_html":"Structure and proposed activity of a member of the VapBC family of toxin-antitoxin systems. VapBC-5 from Mycobacterium tuberculosis. <i> Miallau L, Faller M, Chiang J, Arbing M, Guo F, Cascio D, Eisenberg D. </i> J Biol Chem, 2009","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P9WF18","date":"2016-09-02T10:43:55.000Z","acc":"P9WF19","name":"Putative antitoxin VapB5","length":86,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","UniParc":"UPI00000D1041","genes":[{"name":{"value":"vapB5"},"olnNames":[{"value":"Rv0626"}]}],"alphafold_very_low_content":0,"disorder_content":0.5232558139534884,"disprot_consensus":{"full":[{"start":1,"end":45,"type":"D"}],"Structural state":[{"start":1,"end":45,"type":"D"}]}},{"features":{"pfam":[{"id":"PF05979","name":"Bacterial protein of unknown function (DUF896)","start":6,"end":68}],"gene3D":[{"start":1,"end":56,"id":"1.10.287.540","name":"Helix hairpin bin"}]},"uniref50":"UniRef50_O31818","sequence":"MISNAKIARINELAAKAKAGVITEEEKAEQQKLRQEYLKGFRSSMKNTLKSVKIIDPEGNDVTPEKLKREQRNNKLH","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Bacillus"],"uniref90":"UniRef90_O31818","disprot_id":"DP00892","ncbi_taxon_id":224308,"regions_counter":1,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":77,"region_id":"DP00892r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution NMR structure of the SOS response protein YnzC from Bacillus subtilis. <i> Aramini JM, Sharma S, Huang YJ, Swapna GV, Ho CK, Shetty K, Cunningham K, Ma LC, Zhao L, Owens LA, Jiang M, Xiao R, Liu J, Baran MC, Acton TB, Rost B, Montelione GT. </i> Proteins, 2008","term_id":"IDPO:0000002","curator_id":"nmurvai","start":41,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"18431750","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2HEP"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_O31818","date":"2016-09-02T14:02:23.000Z","acc":"O31818","name":"UPF0291 protein YnzC","length":77,"organism":"Bacillus subtilis (strain 168)","dataset":[],"UniParc":"UPI000006047C","genes":[{"name":{"value":"ynzC"},"olnNames":[{"value":"BSU17880"}]}],"alphafold_very_low_content":0.012987012987012988,"disorder_content":0.4805194805194805,"disprot_consensus":{"full":[{"start":41,"end":77,"type":"D"}],"Structural state":[{"start":41,"end":77,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00448","name":"SRP54-type protein, GTPase domain","start":419,"end":636},{"id":"PF02881","name":"SRP54-type protein, helical bundle domain","start":319,"end":389},{"id":"PF04086","name":"Signal recognition particle, alpha subunit, N-terminal","start":28,"end":128}],"gene3D":[{"start":299,"end":399,"id":"1.20.120.140","name":"Signal recognition particle SRP54, nucleotide-binding domain"},{"start":402,"end":638,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":1,"end":129,"id":"3.30.450.60","name":"3.30.450.60"}]},"uniref50":"UniRef50_P08240","sequence":"MLDFFTIFSKGGLVLWCFQGVSDSCTGPVNALIRSVLLQERGGNNSFTHEALTLKYKLDNQFELVFVVGFQKILTLTYVDKLIDDVHRLFRDKYRTEIQQQSALSLLNGTFDFQNDFLRLLREAEESSKIRAPTTMKKFEDSEKAKKPVRSMIETRGEKPKEKAKNSKKKGAKKEGSDGPLATSKPVPAEKSGLPVGPENGVELSKEELIRRKREEFIQKHGRGMEKSNKSTKSDAPKEKGKKAPRVWELGGCANKEVLDYSTPTTNGTPEAALSEDINLIRGTGSGGQLQDLDCSSSDDEGAAQNSTKPSATKGTLGGMFGMLKGLVGSKSLSREDMESVLDKMRDHLIAKNVAADIAVQLCESVANKLEGKVMGTFSTVTSTVKQALQESLVQILQPQRRVDMLRDIMDAQRRQRPYVVTFCGVNGVGKSTNLAKISFWLLENGFSVLIAACDTFRAGAVEQLRTHTRRLSALHPPEKHGGRTMVQLFEKGYGKDAAGIAMEAIAFARNQGFDVVLVDTAGRMQDNAPLMTALAKLITVNTPDLVLFVGEALVGNEAVDQLVKFNRALADHSMAQTPRLIDGIVLTKFDTIDDKVGAAISMTYITSKPIVFVGTGQTYCDLRSLNAKAVVAALMKA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P08240","disprot_id":"DP00893","ncbi_taxon_id":9606,"regions_counter":14,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":176,"region_id":"DP00893r004","released":"2023_06","ec_id":"ECO:0006220","reference_html":"The structure of the mammalian signal recognition particle (SRP) receptor as prototype for the interaction of small GTPases with Longin domains. <i> Schlenker O, Hendricks A, Sinning I, Wild K. </i> J Biol Chem, 2006","term_id":"IDPO:0000002","curator_id":"vnugnes","start":130,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16439358","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-05-09T19:42:58.814Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2FH5"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P47758"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:135398633"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"}],"statement":[{"text":"Disordered parts of the complex are indicated by dashed lines.","type":"Figure"},{"text":"Residues 41X-47X, 131X-176X, 208B-219B, and 248B-254B are not ordered and therefore missing in the model.","type":"Methods"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":176,"region_id":"DP00893r007","released":"2023_06","ec_id":"ECO:0006224","reference_html":"Signal recognition particle receptor exposes the ribosomal translocon binding site. <i> Halic M, Gartmann M, Schlenker O, Mielke T, Pool MR, Sinning I, Beckmann R. </i> Science, 2006","term_id":"IDPO:0000002","curator_id":"vnugnes","start":131,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16675701","version":3,"ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","date":"2023-05-09T15:50:04.228Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2GO5"},{"db":"EMDB","id":"1217"}],"term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"This region lacks electron density in the Electron Microscopy structure of the signal recognition particle receptor (SR) in complex with signal recognition particle (SRP) and ribosome nascent chain complex","type":"Curator statement"}]},{"start":130,"end":238,"reference_id":"34020957","reference_source":"pmid","reference_html":"Receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER.  <i> Lee JH, Jomaa A, Jomaa A, Chung S, Hwang Fu YH, Qian R, Sun X, Hsieh HH, Chandrasekar S, Bi X, Mattei S, Boehringer D, Weiss S, Ban N, Shan SO. </i> Sci Adv, 2021","date":"2023-05-09T15:48:15.659Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00893r014","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:135403657"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:135398633"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"}],"statement":[{"text":"This region lacks electron density in the Electron Microscopy structure of the Mammalian ribosome nascent chain complex with SRP and SRP receptor in early state A.","type":"Curator statement"}],"cross_refs":[{"db":"EMDB","id":"12303"},{"db":"PDB","id":"7NFX"}]}],"released":"2016_10","uniref100":"UniRef100_P08240","date":"2016-09-02T14:17:55.000Z","acc":"P08240","name":"Signal recognition particle receptor subunit alpha","length":638,"organism":"Homo sapiens","dataset":["NDDs-related proteins","RNA-binding proteins"],"UniParc":"UPI000016A84A","genes":[{"name":{"value":"SRPRA","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11307","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11307"}}]},"synonyms":[{"value":"SRPR"}]}],"alphafold_very_low_content":0.22413793103448276,"disorder_content":0.17084639498432602,"disprot_consensus":{"full":[{"start":130,"end":238,"type":"D"}],"Structural state":[{"start":130,"end":238,"type":"D"}]}},{"features":{"pfam":[{"id":"PF11511","name":"Intrinsic membrane protein PufX","start":1,"end":67}],"gene3D":[{"start":1,"end":56,"id":"1.20.5.920","name":"rhodobacter sphaeroides pufx membrane protein"}]},"uniref50":"UniRef50_P13402","sequence":"MADKTIFNDHLNTNPKTNLRLWVAFQMMKGAGWAGGVFFGTLLLIGFFRVVGRMLPIQENQAPAPNITGALETGIELIKHLV","taxonomy":["Bacteria","Proteobacteria","Alphaproteobacteria","Rhodobacterales","Rhodobacteraceae","Luteovulum"],"uniref90":"UniRef90_P13402","disprot_id":"DP00894","ncbi_taxon_id":1063,"regions_counter":4,"creator":"smribeiro","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":12,"region_id":"DP00894r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The solution structure of the PufX polypeptide from Rhodobacter sphaeroides. <i> Tunnicliffe RB, Ratcliffe EC, Hunter CN, Williamson MP. </i> FEBS Lett, 2006","term_id":"IDPO:0000002","curator_id":"smribeiro","start":1,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2RNG"}],"reference_id":"17161397","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":82,"region_id":"DP00894r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The solution structure of the PufX polypeptide from Rhodobacter sphaeroides. <i> Tunnicliffe RB, Ratcliffe EC, Hunter CN, Williamson MP. </i> FEBS Lett, 2006","term_id":"IDPO:0000002","curator_id":"smribeiro","start":54,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2RNG"}],"reference_id":"17161397","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":12,"region_id":"DP00894r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of the Rhodobacter sphaeroides PufX membrane protein: implications for the quinone exchange and protein-protein interactions. <i> Wang ZY, Suzuki H, Kobayashi M, Nozawa T. </i> Biochemistry, 2007","term_id":"IDPO:0000002","curator_id":"smribeiro","start":2,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2DW3"}],"reference_id":"17335288","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":72,"region_id":"DP00894r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of the Rhodobacter sphaeroides PufX membrane protein: implications for the quinone exchange and protein-protein interactions. <i> Wang ZY, Suzuki H, Kobayashi M, Nozawa T. </i> Biochemistry, 2007","term_id":"IDPO:0000002","curator_id":"smribeiro","start":54,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2DW3"}],"reference_id":"17335288","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P13402","date":"2016-09-02T15:20:02.000Z","acc":"Q7B2Z6","name":"Intrinsic membrane protein PufX","length":82,"organism":"Rhodobacter sphaeroides","dataset":[],"UniParc":"UPI0000000324","genes":[{"name":{"value":"pufX","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAB38756.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAB38756.1"}}]},"orfNames":[{"value":"EBL86_10045","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AZB68700.1","url":"https://www.ebi.ac.uk/ena/browser/view/AZB68700.1"}}]}]}],"alphafold_very_low_content":0.04878048780487805,"disorder_content":0.5,"disprot_consensus":{"full":[{"start":1,"end":12,"type":"D"},{"start":54,"end":82,"type":"D"}],"Structural state":[{"start":1,"end":12,"type":"D"},{"start":54,"end":82,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02478","name":"Pneumovirus phosphoprotein","start":65,"end":231}]},"uniref50":"UniRef50_P03421","sequence":"MEKFAPEFHGEDANNRATKFLESIKGKFTSPKDPKKKDSIISVNSIDIEVTKESPITSNSTIINPTNETDDTAGNKPNYQRKPLVSFKEDPTPSDNPFSKLYKETIETFDNNEEESSYSYEEINDQTNDNITARLDRIDEKLSEILGMLHTLVVASAGPTSARDGIRDAMIGLREEMIEKIRTEALMTNDRLEAMARLRNEESEKMAKDTSDEVSLNPTSEKLNNLLEGNDSDNDLSLEDF","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Pneumoviridae","Orthopneumovirus"],"uniref90":"UniRef90_P03421","disprot_id":"DP00895","ncbi_taxon_id":11259,"regions_counter":14,"creator":"zkalman","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":102,"region_id":"DP00895r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Intrinsic Disorder to Order Transitions in the Scaffold Phosphoprotein P from the Respiratory Syncytial Virus RNA Polymerase Complex. <i> Noval MG, Esperante SA, Molina IG, Chemes LB, Prat-Gay Gd. </i> Biochemistry, 2016","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"26901160","statement":[{"text":"The monomeric PN fragment displayed a CD spectrum at 25 °C typical of a disordered conformation with a predominant minimum at ∼200 nm, no components of regular secondary structure, and the expected increase in secondary structure content at high temperature due to strengthening of hydrophobic interactions, a typical feature of IDP regions (Figure 2C).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T10:32:27.868Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":102,"region_id":"DP00895r002","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Intrinsic Disorder to Order Transitions in the Scaffold Phosphoprotein P from the Respiratory Syncytial Virus RNA Polymerase Complex. <i> Noval MG, Esperante SA, Molina IG, Chemes LB, Prat-Gay Gd. </i> Biochemistry, 2016","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"chromatography evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"26901160","statement":[{"text":"The monomeric PN and PC fragments presented ratios (MWSEC/MWSLS) of 2.7 ± 0.1 and 3.1 ± 0.1, respectively, which can be explained by the extended conformation and low compactness of the polypeptide chain typical of IDPs.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T10:32:22.370Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":162,"end":241,"reference_id":"26901160","reference_source":"pmid","reference_html":"Intrinsic Disorder to Order Transitions in the Scaffold Phosphoprotein P from the Respiratory Syncytial Virus RNA Polymerase Complex. <i> Noval MG, Esperante SA, Molina IG, Chemes LB, Prat-Gay Gd. </i> Biochemistry, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00895r003","statement":[{"text":"The monomeric PN and PC fragments presented ratios (MWSEC/MWSLS) of 2.7 ± 0.1 and 3.1 ± 0.1, respectively, which can be explained by the extended conformation and low compactness of the polypeptide chain typical of IDPs.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T10:32:00.039Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":162,"end":241,"reference_id":"26901160","reference_source":"pmid","reference_html":"Intrinsic Disorder to Order Transitions in the Scaffold Phosphoprotein P from the Respiratory Syncytial Virus RNA Polymerase Complex. <i> Noval MG, Esperante SA, Molina IG, Chemes LB, Prat-Gay Gd. </i> Biochemistry, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00895r004","statement":[{"text":"The monomeric PC fragment presented a CD spectrum characterized by a small negative band at 220 nm indicative of some degree of α-helical content and a minimum centered at 204 nm, which indicates a mixture of contributions from disorder (200 nm) and α-helix (208 nm), showing that PC features both structured and disordered elements in contrast to the fully disordered conformation of the PN fragment (Figure 2F).","type":"Results"},{"text":"Thermal denaturation of full-length P revealed a structural transition between 5 and 60 °C, with some degree of cooperativity (Figure 4A, top panel). Within this temperature range, PTET, PNTET, and PN showed no thermal transition (Figure 4A, bottom panel) while PC and PTETC showed transitions similar to that of P (Figure 4B), in accordance with the results depicted in Figure 2.","type":"Results"},{"text":" In particular at pH 3.0, the PC fragment (pI = 4.34) presented an increase in α-helical content (Figure 8A), which resulted in substantial compaction of PC as determined by SEC, changing the MWSEC/MWSLS ratio from 3.1 ± 0.2 to 1.3 ± 0.1, similar to that of a globular protein (Figure 8B).","type":"Results"},{"text":"These findings supported the pre-molten globule-like nature of the PC module, whereas charge neutralization drives the extended structure to adopt a globular fold with a high degree of α-helical content.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T10:31:51.168Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":118,"reference_id":"22978633","reference_source":"pmid","reference_html":"Modular unfolding and dissociation of the human respiratory syncytial virus phosphoprotein p and its interaction with the m(2-1) antiterminator: a singular tetramer-tetramer interface arrangement. <i> Esperante SA, Paris G, de Prat-Gay G. </i> Biochemistry, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00895r006","statement":[{"text":"With the protein digestion protocol we used (see Experimental Procedures), we obtained a major species of fragment Y of 4959.6 Da determined by mass spectrometry, which fits well with a peptide containing three additional residues (Ser-Ala-Arg) in the carboxy terminal region (peptide starting at Ser 119 and ending at Arg 163 with a theoretical mass of 4958.4 Da).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T10:28:04.583Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":164,"end":241,"reference_id":"22978633","reference_source":"pmid","reference_html":"Modular unfolding and dissociation of the human respiratory syncytial virus phosphoprotein p and its interaction with the m(2-1) antiterminator: a singular tetramer-tetramer interface arrangement. <i> Esperante SA, Paris G, de Prat-Gay G. </i> Biochemistry, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00895r007","statement":[{"text":"With the protein digestion protocol we used (see Experimental Procedures), we obtained a major species of fragment Y of 4959.6 Da determined by mass spectrometry, which fits well with a peptide containing three additional residues (Ser-Ala-Arg) in the carboxy terminal region (peptide starting at Ser 119 and ending at Arg 163 with a theoretical mass of 4958.4 Da).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T10:28:03.027Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":161,"end":241,"reference_id":"18300250","reference_source":"pmid","reference_html":"Structural properties of the human respiratory syncytial virus P protein: evidence for an elongated homotetrameric molecule that is the smallest orthologue within the family of paramyxovirus polymerase cofactors. <i> Llorente MT, Taylor IA, López-Viñas E, Gomez-Puertas P, Calder LJ, García-Barreno B, Melero JA. </i> Proteins, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00895r008","statement":[{"text":"Therefore, P protein was doubly digested with a mixture of sequencing grade trypsin and chymotrypsin. This was followed by gel filtration chromatography, as described previously for fragment X. A peak eluting as a ∼120 kDa species showed a single band of ∼9 kDa in a SDS-PAGE gel [labeled Y* in Fig. 5(B)], that migrated faster than fragment X.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T10:24:07.233Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":1,"end":118,"reference_id":"18300250","reference_source":"pmid","reference_html":"Structural properties of the human respiratory syncytial virus P protein: evidence for an elongated homotetrameric molecule that is the smallest orthologue within the family of paramyxovirus polymerase cofactors. <i> Llorente MT, Taylor IA, López-Viñas E, Gomez-Puertas P, Calder LJ, García-Barreno B, Melero JA. </i> Proteins, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00895r009","statement":[{"text":"Therefore, P protein was doubly digested with a mixture of sequencing grade trypsin and chymotrypsin. This was followed by gel filtration chromatography, as described previously for fragment X. A peak eluting as a ∼120 kDa species showed a single band of ∼9 kDa in a SDS-PAGE gel [labeled Y* in Fig. 5(B)], that migrated faster than fragment X.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T10:24:02.463Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":234,"end":241,"reference_id":"18300250","reference_source":"pmid","reference_html":"Structural properties of the human respiratory syncytial virus P protein: evidence for an elongated homotetrameric molecule that is the smallest orthologue within the family of paramyxovirus polymerase cofactors. <i> Llorente MT, Taylor IA, López-Viñas E, Gomez-Puertas P, Calder LJ, García-Barreno B, Melero JA. </i> Proteins, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"P03418","partner_start":null,"partner_end":null}],"region_id":"DP00895r010","statement":[{"text":"We then shortened the P230–241 region at either end and produced the corresponding GST–P proteins in E. coli. Mutants PΔN231, PΔN232 and PΔN233 – the latter retaining only the nine most C-terminal amino acids of P – were still able to pull down N with the same efficiency as PΔN230 (Fig. 6c, dF6).","type":"Results"},{"text":"On the other hand, removal of the very C-terminal amino acid of P completely abolished its capacity to pull down N, just like the other mutants tested lacking 2 or 3 aa from the C terminus (Fig. 6c, dF6). Thus, the C-terminal P segment spanning aa 234–241 appears to contain the minimal region for efficient interaction with RNA–N in this system.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T10:34:23.935Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":161,"end":241,"reference_id":"18300250","reference_source":"pmid","reference_html":"Structural properties of the human respiratory syncytial virus P protein: evidence for an elongated homotetrameric molecule that is the smallest orthologue within the family of paramyxovirus polymerase cofactors. <i> Llorente MT, Taylor IA, López-Viñas E, Gomez-Puertas P, Calder LJ, García-Barreno B, Melero JA. </i> Proteins, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00895r011","statement":[{"text":"In order to characterize and compare the complexes co-purified by using either the oligomeric full-length P or the C-terminal fragment PΔN161, the samples were analysed by negative-staining electron microscopy (EM) after proteolytic separation from GST. Fig. 2F2(a, b) shows nucleocapsid-like structures eluted from GST beads for both P–N (a) and PΔN161–N (b).","type":"Results"}],"interaction_partner":[{"db":"UniProt","id":"P03418","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T10:34:22.610Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":161,"end":241,"reference_id":"18300250","reference_source":"pmid","reference_html":"Structural properties of the human respiratory syncytial virus P protein: evidence for an elongated homotetrameric molecule that is the smallest orthologue within the family of paramyxovirus polymerase cofactors. <i> Llorente MT, Taylor IA, López-Viñas E, Gomez-Puertas P, Calder LJ, García-Barreno B, Melero JA. </i> Proteins, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00895r012","statement":[{"text":"The second peak (P3), which eluted at 16.9 ml, only absorbed at 220 nm and contained the PΔN161 fragment. Its apparent mass was between 20.2 and 47.2 kDa, higher than its predicted mass of 10 kDa, presumably due to a markedly non-globular shape of the fragment (Tarbouriech et al., 2000).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T10:23:46.377Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":161,"end":241,"reference_id":"18300250","reference_source":"pmid","reference_html":"Structural properties of the human respiratory syncytial virus P protein: evidence for an elongated homotetrameric molecule that is the smallest orthologue within the family of paramyxovirus polymerase cofactors. <i> Llorente MT, Taylor IA, López-Viñas E, Gomez-Puertas P, Calder LJ, García-Barreno B, Melero JA. </i> Proteins, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019058","term_name":"viral life cycle","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00895r013","statement":[{"text":"In order to characterize and compare the complexes co-purified by using either the oligomeric full-length P or the C-terminal fragment PΔN161, the samples were analysed by negative-staining electron microscopy (EM) after proteolytic separation from GST. Fig. 2F2(a, b) shows nucleocapsid-like structures eluted from GST beads for both P–N (a) and PΔN161–N (b).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T10:34:29.458Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A set of processes which all viruses follow to ensure survival; includes attachment and entry of the virus particle, decoding of genome information, translation of viral mRNA by host ribosomes, genome replication, and assembly and release of viral particles containing the genome.\" [ISBN:1555811272]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":234,"end":241,"reference_id":"18300250","reference_source":"pmid","reference_html":"Structural properties of the human respiratory syncytial virus P protein: evidence for an elongated homotetrameric molecule that is the smallest orthologue within the family of paramyxovirus polymerase cofactors. <i> Llorente MT, Taylor IA, López-Viñas E, Gomez-Puertas P, Calder LJ, García-Barreno B, Melero JA. </i> Proteins, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019058","term_name":"viral life cycle","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00895r014","statement":[{"text":"We then shortened the P230–241 region at either end and produced the corresponding GST–P proteins in E. coli. Mutants PΔN231, PΔN232 and PΔN233 – the latter retaining only the nine most C-terminal amino acids of P – were still able to pull down N with the same efficiency as PΔN230 (Fig. 6c, dF6).","type":"Results"},{"text":"On the other hand, removal of the very C-terminal amino acid of P completely abolished its capacity to pull down N, just like the other mutants tested lacking 2 or 3 aa from the C terminus (Fig. 6c, dF6). Thus, the C-terminal P segment spanning aa 234–241 appears to contain the minimal region for efficient interaction with RNA–N in this system.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T10:34:27.883Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A set of processes which all viruses follow to ensure survival; includes attachment and entry of the virus particle, decoding of genome information, translation of viral mRNA by host ribosomes, genome replication, and assembly and release of viral particles containing the genome.\" [ISBN:1555811272]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2016_10","uniref100":"UniRef100_P03421","date":"2016-09-03T10:58:21.000Z","acc":"P03421","name":"Phosphoprotein","length":241,"organism":"Human respiratory syncytial virus A (strain A2)","dataset":["Viral proteins","Condensates-related proteins"],"UniParc":"UPI0000134B5D","genes":[{"name":{"value":"P"}}],"disorder_content":0.8257261410788381,"disprot_consensus":{"full":[{"start":1,"end":118,"type":"D"},{"start":161,"end":241,"type":"D"}],"Structural state":[{"start":1,"end":118,"type":"D"},{"start":161,"end":241,"type":"D"}],"Molecular function":[{"start":161,"end":241,"type":"F"}],"Biological process":[{"start":161,"end":241,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00448","name":"SRP54-type protein, GTPase domain","start":293,"end":493},{"id":"PF02881","name":"SRP54-type protein, helical bundle domain","start":210,"end":275}],"gene3D":[{"start":196,"end":492,"id":"1.20.120.140","name":"Signal recognition particle SRP54, nucleotide-binding domain"},{"start":290,"end":482,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_P10121","sequence":"MAKEKKRGFFSWLGFGQKEQTPEKETEVQNEQPVVEEIVQAQEPVKASEQAVEEQPQAHTEAEAETFAADVVEVTEQVAESEKAQPEAEVVAQPEPVVEETPEPVAIEREELPLPEDVNAEAVSPEEWQAEAETVEIVEAAEEEAAKEEITDEELETALAAEAAEEAVMVVPPAEEEQPVEEIAQEQEKPTKEGFFARLKRSLLKTKENLGSGFISLFRGKKIDDDLFEELEEQLLIADVGVETTRKIITNLTEGASRKQLRDAEALYGLLKEEMGEILAKVDEPLNVEGKAPFVILMVGVNGVGKTTTIGKLARQFEQQGKSVMLAAGDTFRAAAVEQLQVWGQRNNIPVIAQHTGADSASVIFDAIQAAKARNIDVLIADTAGRLQNKSHLMEELKKIVRVMKKLDVEAPHEVMLTIDASTGQNAVSQAKLFHEAVGLTGITLTKLDGTAKGGVIFSVADQFGIPIRYIGVGERIEDLRPFKADDFIEALFARED","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P10121","disprot_id":"DP00896","ncbi_taxon_id":83333,"regions_counter":4,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":187,"region_id":"DP00896r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Lipids trigger a conformational switch that regulates signal recognition particle (SRP)-mediated protein targeting. <i> Stjepanovic G, Kapp K, Bange G, Graf C, Parlitz R, Wild K, Mayer MP, Sinning I. </i> J Biol Chem, 2011","term_id":"IDPO:0000002","curator_id":"nmurvai","start":1,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"21543314","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":187,"term_name":"flexible N-terminal tail","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"21543314","version":3,"reference_html":"Lipids trigger a conformational switch that regulates signal recognition particle (SRP)-mediated protein targeting. <i> Stjepanovic G, Kapp K, Bange G, Graf C, Parlitz R, Wild K, Mayer MP, Sinning I. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000032","ec_id":"ECO:0006165","region_id":"DP00896r002","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":187,"region_id":"DP00896r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Lipids trigger a conformational switch that regulates signal recognition particle (SRP)-mediated protein targeting. <i> Stjepanovic G, Kapp K, Bange G, Graf C, Parlitz R, Wild K, Mayer MP, Sinning I. </i> J Biol Chem, 2011","term_id":"IDPO:0000002","curator_id":"nmurvai","start":1,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"21543314","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2YHS"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":187,"term_name":"flexible N-terminal tail","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"21543314","version":3,"reference_html":"Lipids trigger a conformational switch that regulates signal recognition particle (SRP)-mediated protein targeting. <i> Stjepanovic G, Kapp K, Bange G, Graf C, Parlitz R, Wild K, Mayer MP, Sinning I. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000032","ec_id":"ECO:0006220","region_id":"DP00896r004","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_P10121","date":"2016-09-03T17:57:10.000Z","acc":"P10121","name":"Signal recognition particle receptor FtsY","length":497,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI000012AD05","genes":[{"name":{"value":"ftsY","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00920","url":"https://hamap.expasy.org/unirule/MF_00920"}}]},"olnNames":[{"value":"b3464"},{"value":"JW3429"}]}],"alphafold_very_low_content":0.2635814889336016,"disorder_content":0.3762575452716298,"disprot_consensus":{"full":[{"start":1,"end":187,"type":"D"}],"Structural state":[{"start":1,"end":187,"type":"D"}],"Disorder function":[{"start":1,"end":187,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00448","name":"SRP54-type protein, GTPase domain","start":101,"end":295},{"id":"PF02881","name":"SRP54-type protein, helical bundle domain","start":5,"end":82},{"id":"PF02978","name":"Signal peptide binding domain","start":311,"end":431}],"gene3D":[{"start":5,"end":305,"id":"1.20.120.140","name":"Signal recognition particle SRP54, nucleotide-binding domain"},{"start":310,"end":433,"id":"1.10.260.30","name":"Signal recognition particle, SRP54 subunit, M-domain"},{"start":90,"end":284,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_Q57565","sequence":"MLDKLGENLNKALNKLKAAAFVDKKLIKEVIKDIQRALIQADVNVKLVLKMSKEIERRALEEKTPKGLSKKEHIIKIVYEELVKLLGEEAKKLELNPKKQNVILLVGIQGSGKTTTAAKLARYIQKRGLKPALIAADTYRPAAYEQLKQLAEKIHVPIYGDETRTKSPVDIVKEGMEKFKKADVLIIDTAGRHKEEKGLLEEMKQIKEITNPDEIILVIDGTIGQQAGIQAKAFKEAVGEIGSIIVTKLDGSAKGGGALSAVAETKAPIKFIGIGEGIDDLEPFDPKKFISRLLGMGDLESLLEKAEDMVDEKTEESIDAIMRGKFTLNELMTQLEAIENMGSMKKILSMIPGFGGAMPKELSHLTEAKIKKYKVIISSMTKEERENPKIIKASRIRRIARGSGTTENDVREVLRYYETTKNAIDKLRKGKMLRIGGPLGQIMRQLMFKEG","taxonomy":["Archaea","Euryarchaeota","Methanomada group","Methanococci","Methanococcales","Methanocaldococcaceae","Methanocaldococcus"],"uniref90":"UniRef90_Q57565","disprot_id":"DP00897","ncbi_taxon_id":243232,"regions_counter":13,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":318,"region_id":"DP00897r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Signal-sequence induced conformational changes in the signal recognition particle. <i> Hainzl T, Sauer-Eriksson AE. </i> Nat Commun, 2015","term_id":"IDPO:0000002","curator_id":"nmurvai","start":303,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"26051119","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4XCO"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":318,"term_name":"molecular adaptor activity","start":303,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"26051119","version":3,"reference_html":"Signal-sequence induced conformational changes in the signal recognition particle. <i> Hainzl T, Sauer-Eriksson AE. </i> Nat Commun, 2015","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006220","region_id":"DP00897r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":318,"term_name":"disorder to order","start":303,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"26051119","version":2,"reference_html":"Signal-sequence induced conformational changes in the signal recognition particle. <i> Hainzl T, Sauer-Eriksson AE. </i> Nat Commun, 2015","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00897r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":318,"term_name":"protein binding","start":303,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"26051119","version":3,"reference_html":"Signal-sequence induced conformational changes in the signal recognition particle. <i> Hainzl T, Sauer-Eriksson AE. </i> Nat Commun, 2015","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00897r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":364,"region_id":"DP00897r005","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Signal-sequence induced conformational changes in the signal recognition particle. <i> Hainzl T, Sauer-Eriksson AE. </i> Nat Commun, 2015","term_id":"IDPO:0000002","curator_id":"nmurvai","start":345,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"26051119","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4XCO"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":364,"term_name":"molecular adaptor activity","start":345,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"26051119","version":3,"reference_html":"Signal-sequence induced conformational changes in the signal recognition particle. <i> Hainzl T, Sauer-Eriksson AE. </i> Nat Commun, 2015","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006220","region_id":"DP00897r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":364,"term_name":"disorder to order","start":345,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"26051119","version":2,"reference_html":"Signal-sequence induced conformational changes in the signal recognition particle. <i> Hainzl T, Sauer-Eriksson AE. </i> Nat Commun, 2015","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00897r007","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":451,"region_id":"DP00897r008","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Signal-sequence induced conformational changes in the signal recognition particle. <i> Hainzl T, Sauer-Eriksson AE. </i> Nat Commun, 2015","term_id":"IDPO:0000002","curator_id":"nmurvai","start":430,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"26051119","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4XCO"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":451,"term_name":"molecular adaptor activity","start":430,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"26051119","version":3,"reference_html":"Signal-sequence induced conformational changes in the signal recognition particle. <i> Hainzl T, Sauer-Eriksson AE. </i> Nat Commun, 2015","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006220","region_id":"DP00897r009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":451,"term_name":"disorder to order","start":430,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"26051119","version":2,"reference_html":"Signal-sequence induced conformational changes in the signal recognition particle. <i> Hainzl T, Sauer-Eriksson AE. </i> Nat Commun, 2015","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00897r010","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":451,"term_name":"protein binding","start":430,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"26051119","version":3,"reference_html":"Signal-sequence induced conformational changes in the signal recognition particle. <i> Hainzl T, Sauer-Eriksson AE. </i> Nat Commun, 2015","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00897r011","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":364,"region_id":"DP00897r012","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Interaction of signal-recognition particle 54 GTPase domain and signal-recognition particle RNA in the free signal-recognition particle. <i> Hainzl T, Huang S, Sauer-Eriksson AE. </i> Proc Natl Acad Sci U S A, 2007","term_id":"IDPO:0000002","curator_id":"nmurvai","start":339,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"17846429","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2V3C"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":364,"region_id":"DP00897r013","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis of signal-sequence recognition by the signal recognition particle. <i> Hainzl T, Huang S, Meriläinen G, Brännström K, Sauer-Eriksson AE. </i> Nat Struct Mol Biol, 2011","term_id":"IDPO:0000002","curator_id":"nmurvai","start":341,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"21336278","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3NDB"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q57565","date":"2016-09-03T19:03:54.000Z","acc":"Q57565","name":"Signal recognition particle 54 kDa protein","length":451,"organism":"Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)","dataset":[],"UniParc":"UPI0000135EE2","genes":[{"name":{"value":"srp54","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00306","url":"https://hamap.expasy.org/unirule/MF_00306"}}]},"olnNames":[{"value":"MJ0101"}]}],"alphafold_very_low_content":0.07095343680709534,"disorder_content":0.1419068736141907,"disprot_consensus":{"full":[{"start":303,"end":318,"type":"T"},{"start":339,"end":344,"type":"D"},{"start":345,"end":364,"type":"T"},{"start":430,"end":451,"type":"T"}],"Structural state":[{"start":303,"end":318,"type":"D"},{"start":339,"end":364,"type":"D"},{"start":430,"end":451,"type":"D"}],"Molecular function":[{"start":303,"end":318,"type":"F"},{"start":345,"end":364,"type":"F"},{"start":430,"end":451,"type":"F"}],"Structural transition":[{"start":303,"end":318,"type":"T"},{"start":345,"end":364,"type":"T"},{"start":430,"end":451,"type":"T"}]}},{"features":{"pfam":[{"id":"PF16805","name":"Phage late-transcription coactivator","start":33,"end":109}],"gene3D":[{"start":32,"end":112,"id":"1.10.10.2850","name":"Phage late-transcription coactivator-like"}]},"uniref50":"UniRef50_P13338","sequence":"MTQFSLNDIRPVDETGLSEKELSIKKEKDEIAKLLDRQENGFIIEKMVEEFGMSYLEATTAFLEENSIPETQFAKFIPSGIIEKIQSEAIDENLLRPSVVRCEKTNTLDFLL","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Uroviricota","Caudoviricetes","Caudovirales","Myoviridae","Tevenvirinae","Tequatrovirus"],"uniref90":"UniRef90_P13338","disprot_id":"DP00898","ncbi_taxon_id":10665,"regions_counter":2,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":31,"region_id":"DP00898r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the bacteriophage T4 late-transcription coactivator gp33 with the β-subunit flap domain of Escherichia coli RNA polymerase. <i> Twist KA, Campbell EA, Deighan P, Nechaev S, Jain V, Geiduschek EP, Hochschild A, Darst SA. </i> Proc Natl Acad Sci U S A, 2011","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22135460","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3TBI"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The entire β-flap was built into the electron density map, but there was no clear density for two terminal segments of gp33, so only residues 32–102 (of the full 112) were modeled in the structure (Fig. 1). Analysis of the crystals indicated that they contained both proteins without proteolytic degradation (Fig. S1C), so the N-terminal 31 and C-terminal 10 residues of gp33 are presumed disordered in the crystals.","type":"Results"}],"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue","statements":[{"type":"Methods","text":"The structure was solved by a combination of molecular replacement and single-wavelength anomalous dispersion with data collected from selenomethionyl-substituted proteins."}]}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-15T11:24:16.367Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":112,"region_id":"DP00898r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the bacteriophage T4 late-transcription coactivator gp33 with the β-subunit flap domain of Escherichia coli RNA polymerase. <i> Twist KA, Campbell EA, Deighan P, Nechaev S, Jain V, Geiduschek EP, Hochschild A, Darst SA. </i> Proc Natl Acad Sci U S A, 2011","term_id":"IDPO:0000002","curator_id":"fquaglia","start":103,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22135460","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3TBI"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The entire β-flap was built into the electron density map, but there was no clear density for two terminal segments of gp33, so only residues 32–102 (of the full 112) were modeled in the structure (Fig. 1). Analysis of the crystals indicated that they contained both proteins without proteolytic degradation (Fig. S1C), so the N-terminal 31 and C-terminal 10 residues of gp33 are presumed disordered in the crystals.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-15T11:24:17.231Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P13338","date":"2016-09-04T01:06:45.000Z","acc":"P13338","name":"RNA polymerase-associated protein Gp33","length":112,"organism":"Enterobacteria phage T4","dataset":["Viral proteins"],"UniParc":"UPI000005CBE0","genes":[{"name":{"value":"33"}}],"disorder_content":0.36607142857142855,"disprot_consensus":{"full":[{"start":1,"end":31,"type":"D"},{"start":103,"end":112,"type":"D"}],"Structural state":[{"start":1,"end":31,"type":"D"},{"start":103,"end":112,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03892","name":"Nitrate reductase cytochrome c-type subunit (NapB)","start":36,"end":144}],"gene3D":[{"start":63,"end":130,"id":"1.10.1130.10","name":"Flavocytochrome C3; Chain A"}]},"uniref50":"UniRef50_P44654","sequence":"MINMTKQVSKILAGLFTALFAGSLMASDAPAVGKDLTQAAENIPPAFHNAPRQGELPALNYVNQPPMVPHSVANYQVTKNVNQCLNCHSPENSRLSGATRISPTHFMDRDGKVGSSSSPRRYFCLQCHVSQANVDPIVPNDFKPMKGYGN","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Pasteurellales","Pasteurellaceae","Haemophilus"],"uniref90":"UniRef90_P44654","disprot_id":"DP00899","ncbi_taxon_id":71421,"regions_counter":8,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":62,"region_id":"DP00899r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The 1.25 A resolution structure of the diheme NapB subunit of soluble nitrate reductase reveals a novel cytochrome c fold with a stacked heme arrangement. <i> Brigé A, Leys D, Meyer TE, Cusanovich MA, Van Beeumen JJ. </i> Biochemistry, 2002","term_id":"IDPO:0000002","curator_id":"nmurvai","start":28,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"11939777","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1JNI"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":150,"region_id":"DP00899r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The 1.25 A resolution structure of the diheme NapB subunit of soluble nitrate reductase reveals a novel cytochrome c fold with a stacked heme arrangement. <i> Brigé A, Leys D, Meyer TE, Cusanovich MA, Van Beeumen JJ. </i> Biochemistry, 2002","term_id":"IDPO:0000002","curator_id":"nmurvai","start":131,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"11939777","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1JNI"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":62,"region_id":"DP00899r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural and redox plasticity in the heterodimeric periplasmic nitrate reductase. <i> Arnoux P, Sabaty M, Alric J, Frangioni B, Guigliarelli B, Adriano JM, Pignol D. </i> Nat Struct Biol, 2003","term_id":"IDPO:0000002","curator_id":"nmurvai","start":28,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"14528294","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1JNI"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":62,"term_name":"molecular adaptor activity","start":28,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"14528294","version":3,"reference_html":"Structural and redox plasticity in the heterodimeric periplasmic nitrate reductase. <i> Arnoux P, Sabaty M, Alric J, Frangioni B, Guigliarelli B, Adriano JM, Pignol D. </i> Nat Struct Biol, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006220","region_id":"DP00899r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":62,"term_name":"disorder to order","start":28,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"14528294","version":2,"reference_html":"Structural and redox plasticity in the heterodimeric periplasmic nitrate reductase. <i> Arnoux P, Sabaty M, Alric J, Frangioni B, Guigliarelli B, Adriano JM, Pignol D. </i> Nat Struct Biol, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00899r005","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":150,"region_id":"DP00899r006","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural and redox plasticity in the heterodimeric periplasmic nitrate reductase. <i> Arnoux P, Sabaty M, Alric J, Frangioni B, Guigliarelli B, Adriano JM, Pignol D. </i> Nat Struct Biol, 2003","term_id":"IDPO:0000002","curator_id":"nmurvai","start":131,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"14528294","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1JNI"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":150,"term_name":"molecular adaptor activity","start":131,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"14528294","version":3,"reference_html":"Structural and redox plasticity in the heterodimeric periplasmic nitrate reductase. <i> Arnoux P, Sabaty M, Alric J, Frangioni B, Guigliarelli B, Adriano JM, Pignol D. </i> Nat Struct Biol, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006220","region_id":"DP00899r007","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":150,"term_name":"disorder to order","start":131,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"14528294","version":2,"reference_html":"Structural and redox plasticity in the heterodimeric periplasmic nitrate reductase. <i> Arnoux P, Sabaty M, Alric J, Frangioni B, Guigliarelli B, Adriano JM, Pignol D. </i> Nat Struct Biol, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00899r008","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2016_10","uniref100":"UniRef100_P44654","date":"2016-09-04T01:12:35.000Z","acc":"P44654","name":"Periplasmic nitrate reductase, electron transfer subunit","length":150,"organism":"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","dataset":[],"UniParc":"UPI000012FD63","genes":[{"name":{"value":"napB"},"olnNames":[{"value":"HI_0347"}]}],"alphafold_very_low_content":0,"disorder_content":0.36666666666666664,"disprot_consensus":{"full":[{"start":28,"end":62,"type":"T"},{"start":131,"end":150,"type":"T"}],"Structural state":[{"start":28,"end":62,"type":"D"},{"start":131,"end":150,"type":"D"}],"Molecular function":[{"start":28,"end":62,"type":"F"},{"start":131,"end":150,"type":"F"}],"Structural transition":[{"start":28,"end":62,"type":"T"},{"start":131,"end":150,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00400","name":"WD domain, G-beta repeat","start":429,"end":464},{"id":"PF00400","name":"WD domain, G-beta repeat","start":714,"end":750},{"id":"PF00400","name":"WD domain, G-beta repeat","start":766,"end":805},{"id":"PF08145","name":"BOP1NT (NUC169) domain","start":165,"end":426}]},"uniref50":"UniRef50_Q04660","sequence":"MMAKNNKTTEAKMSKKRAASEESDVEEDEDKLLSVDGLIDAEASESDEDDDEYESAVEEKESSSDKEAQDDSDDDSDAELNKLLAEEEGDGEEDYDSSEFSDDTTSLTDRLSGVKLQTIVDPNIYSKYADGSDRIIKPEINPVYDSDDSDAETQNTIGNIPLSAYDEMPHIGYDINGKRIMRPAKGSALDQLLDSIELPEGWTGLLDKNSGSSLNLTKEELELISKIQRNEQTDDSINPYEPLIDWFTRHEEVMPLTAVPEPKRRFVPSKNEAKRVMKIVRAIREGRIIPPKKLKEMKEKEKIENYQYDLWGDSTETNDHVMHLRAPKLPPPTNEESYNPPEEYLLSPEEKEAWENTEYSERERNFIPQKYSALRKVPGYGESIRERFERSLDLYLAPRVRKNKLNIDPNSLIPELPSPKDLRPFPIRCSTIYAGHKGKVRTLSIDPSGLWLATGSDDGTVRVWEILTGREVYRTTLIDDEENPDYHIECIEWNPDANNGILAVAVGENIHLIVPPIFGYDIENNGKTKIEDGFGYDTFGTVKKSNLEVNENGDGDEDGENESAKNAVKKQVAQWNKPSQKQLEKDICITISCKKTVKKLSWHRKGDYFVTVQPDSGNTSVLIHQVSKHLTQSPFKKSKGIIMDAKFHPFKPQLFVCSQRYVRIYDLSQQILVKKLLPGARWLSKIDIHPRGDNLIASSFDKRVLWHDLDLASTPYKTLRYHEKAVRSVNFHKKLPLFSSAADDGTIHVFHATVYDDMMKNPMIVPLKKLTGHKVINSLGVLDAIWHPREAWLFSAGADNTARLWTT","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q04660","disprot_id":"DP00900","ncbi_taxon_id":559292,"regions_counter":3,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":570,"region_id":"DP00900r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The carboxy-terminal domain of Erb1 is a seven-bladed ß-propeller that binds RNA. <i> Wegrecki M, Neira JL, Bravo J. </i> PLoS One, 2015","term_id":"IDPO:0000002","curator_id":"bszabo","start":535,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"25880847","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4U7A"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":570,"term_name":"disorder to order","start":535,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"25880847","version":2,"reference_html":"The carboxy-terminal domain of Erb1 is a seven-bladed ß-propeller that binds RNA. <i> Wegrecki M, Neira JL, Bravo J. </i> PLoS One, 2015","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP00900r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":570,"term_name":"DNA binding","start":535,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"25880847","version":3,"reference_html":"The carboxy-terminal domain of Erb1 is a seven-bladed ß-propeller that binds RNA. <i> Wegrecki M, Neira JL, Bravo J. </i> PLoS One, 2015","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003677","ec_id":"ECO:0006220","region_id":"DP00900r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q04660","date":"2016-09-05T11:09:27.000Z","acc":"Q04660","name":"Ribosome biogenesis protein ERB1","length":807,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI00000530E3","genes":[{"name":{"value":"ERB1","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03027","url":"https://hamap.expasy.org/unirule/MF_03027"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"11522832","url":"http://www.ncbi.nlm.nih.gov/pubmed/11522832","alternativeUrl":"https://europepmc.org/abstract/MED/11522832"}}]},"orfNames":[{"value":"YM9796.02C"}],"olnNames":[{"value":"YMR049C","evidences":[{"code":"ECO:0000312","source":{"name":"SGD","id":"S000004652","url":"https://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000004652"}}]}]}],"alphafold_very_low_content":0.18463444857496902,"disorder_content":0.04460966542750929,"disprot_consensus":{"full":[{"start":535,"end":570,"type":"T"}],"Structural state":[{"start":535,"end":570,"type":"D"}],"Structural transition":[{"start":535,"end":570,"type":"T"}],"Molecular function":[{"start":535,"end":570,"type":"F"}]}},{"features":{"pfam":[{"id":"PF07412","name":"Geminin","start":1,"end":184}],"gene3D":[{"start":83,"end":160,"id":"1.20.5.1180","name":"Geminin coiled-coil domain"}]},"uniref50":"UniRef50_O75496","sequence":"MNPSMKQKQEEIKENIKNSSVPRRTLKMIQPSASGSLVGRENELSAGLSKRKHRNDHLTSTTSSPGVIVPESSENKNLGGVTQESFDLMIKENPSSQYWKEVAEKRRKALYEALKENEKLHKEIEQKDNEIARLKKENKELAEVAEHVQYMAELIERLNGEPLDNFESLDNQEFDSEEETVEDSLVEDSEIGTCAEGTVSSSTDAKPCI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O75496","disprot_id":"DP00901","ncbi_taxon_id":9606,"regions_counter":3,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":91,"region_id":"DP00901r001","released":"2023_06","ec_id":"ECO:0006220","reference_html":"A dimerized coiled-coil domain and an adjoining part of geminin interact with two sites on Cdt1 for replication inhibition. <i> Saxena S, Yuan P, Dhar SK, Senga T, Takeda D, Robinson H, Kornbluth S, Swaminathan K, Dutta A. </i> Mol Cell, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":70,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15260975","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-05-23T17:33:47.608Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1UII"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"N-terminal residues 70-91 were not visible in the electron density maps using the experimental phases, calculated at different range of resolution. To determine whether these residues were lost by proteolysis, SDS-PAGE and Mass Spectroscopy were used to analyze the geminin 70-152 peptide in the crystals. The mass of the peptide in geminin 70-152 crystal was 13162.64 D and the peptide in Selenomethionine geminin 70-152 crystal was 13394.44 D, suggesting that the crystallized peptides were intact without any degradation. Therefore residues 70-91 of geminin are disordered and not observed in the electron density map.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_O75496","date":"2016-09-05T11:22:08.000Z","acc":"O75496","name":"Geminin","length":209,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI000012B3BB","genes":[{"name":{"value":"GMNN"}}],"alphafold_very_low_content":0.2583732057416268,"disorder_content":0.10526315789473684,"disprot_consensus":{"full":[{"start":70,"end":91,"type":"D"}],"Structural state":[{"start":70,"end":91,"type":"D"}]}},{"features":{"pfam":[{"id":"PF04539","name":"Sigma-70 region 3","start":115,"end":183},{"id":"PF04542","name":"Sigma-70 region 2","start":36,"end":102},{"id":"PF04545","name":"Sigma-70, region 4","start":197,"end":245}],"gene3D":[{"start":104,"end":158,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"start":177,"end":249,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"start":5,"end":103,"id":"1.10.601.10","name":"RNA Polymerase Primary Sigma Factor"}]},"uniref50":"UniRef50_P07860","sequence":"MDVDVKQGQSPIKDQEMKELIRRSQEGDQEARDEIIEKNMRLVWSVVQRFLNRGYEADDLFQIGCIGLLKSVDKFDLSYDVKFSTYAVPMIIGEIQRFLRDDGTVKVSRSLKEMGNKIRKAKDELSKTRGRSPTITEIADHLGISPEDVVLAQEAVRLPTSIHETVYENDGDPITLLDQIADADEASWFDKIALKKAIEELDERERLIVYLRYYRDRTQSEVASRLGISQVQVSRLEKKILQHIKDKMDG","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Geobacillus"],"uniref90":"UniRef90_O32728","disprot_id":"DP00902","ncbi_taxon_id":1422,"regions_counter":2,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":101,"region_id":"DP00902r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the Bacillus stearothermophilus anti-sigma factor SpoIIAB with the sporulation sigma factor sigmaF. <i> Campbell EA, Masuda S, Sun JL, Muzzin O, Olson CA, Wang S, Darst SA. </i> Cell, 2002","term_id":"IDPO:0000002","curator_id":"atantos","start":1,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1L0O"}],"reference_id":"11955433","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":250,"region_id":"DP00902r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the Bacillus stearothermophilus anti-sigma factor SpoIIAB with the sporulation sigma factor sigmaF. <i> Campbell EA, Masuda S, Sun JL, Muzzin O, Olson CA, Wang S, Darst SA. </i> Cell, 2002","term_id":"IDPO:0000002","curator_id":"atantos","start":159,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1L0O"}],"reference_id":"11955433","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_O32728","date":"2016-09-05T12:56:33.000Z","acc":"O32728","name":"RNA polymerase sigma factor","length":250,"organism":"Geobacillus stearothermophilus","dataset":[],"UniParc":"UPI00000B223F","genes":[],"alphafold_very_low_content":0.032,"disorder_content":0.772,"disprot_consensus":{"full":[{"start":1,"end":101,"type":"D"},{"start":159,"end":250,"type":"D"}],"Structural state":[{"start":1,"end":101,"type":"D"},{"start":159,"end":250,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01176","name":"Translation initiation factor 1A / IF-1","start":23,"end":117}],"gene3D":[{"start":2,"end":144,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}]},"uniref50":"UniRef50_P47813","sequence":"MPKNKGKGGKNRRRGKNENESEKRELVFKEDGQEYAQVIKMLGNGRLEAMCFDGVKRLCHIRGKLRKKVWINTSDIILVGLRDYQDNKADVILKYNADEARSLKAYGELPEHAKINETDTFGPGDDDEIQFDDIGDDDEDIDDI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P47813","disprot_id":"DP00903","ncbi_taxon_id":9606,"regions_counter":6,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":25,"region_id":"DP00903r001","released":"2022_12","ec_id":"ECO:0006165","reference_html":"The eIF1A solution structure reveals a large RNA-binding surface important for scanning function. <i> Battiste JL, Pestova TV, Hellen CU, Wagner G. </i> Mol Cell, 2000","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10678173","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-07-27T15:56:27.768Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1D7Q"},{"db":"BMRB","id":"4519"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Amino acids 1–24 and 118–143 at each terminus, as well as the His tag, do not have any observable long-range NOEs and have dynamics indicative of random coil conformations (data not shown).","type":"Results"},{"text":"Authors are not considering the first M residue, thus the disorder region is 1-25.","type":"Curator statement"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":144,"region_id":"DP00903r002","released":"2022_12","ec_id":"ECO:0006165","reference_html":"The eIF1A solution structure reveals a large RNA-binding surface important for scanning function. <i> Battiste JL, Pestova TV, Hellen CU, Wagner G. </i> Mol Cell, 2000","term_id":"IDPO:0000002","curator_id":"vnugnes","start":119,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10678173","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-07-27T15:58:01.198Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1D7Q"},{"db":"BMRB","id":"4519"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Amino acids 1–24 and 118–143 at each terminus, as well as the His tag, do not have any observable long-range NOEs and have dynamics indicative of random coil conformations (data not shown).","type":"Results"},{"text":"Authors are not considering the first Met residue, thus the disorder region is 119-144.","type":"Curator statement"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":27,"region_id":"DP00903r003","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Structural basis for the nuclear export activity of Importin13. <i> Grünwald M, Lazzaretti D, Bono F. </i> EMBO J, 2013","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"23435562","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-08-09T14:59:26.977Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3ZJY"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62826"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O94829 "},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:135398633"}],"statement":[{"text":"The NTT of eIF1A is not observed (residues 1–27) together with several loop regions (residues 54–56; 97–100; 109–112) (Figure 1A and B).","type":"Results"}]},{"start":129,"end":144,"reference_id":"27325746","reference_source":"pmid","reference_html":"eIF1A/eIF5B interaction network and its functions in translation initiation complex assembly and remodeling. <i> Nag N, Lin KY, Edmonds KA, Yu J, Nadkarni D, Marintcheva B, Marintchev A. </i> Nucleic Acids Res, 2016","date":"2022-07-27T17:18:19.017Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P47813","operator":null,"partner_start":25,"partner_end":117}],"region_id":"DP00903r004","statement":[{"text":"Deletion of eIF1A-CT16 affects a distinct surface on eIF1A-OB, which is a subset of that affected by deletion of eIF1A-CTT (compare Figure ​2B and Supplementary Figure S1A). Adding eIF1A-CT16 to 15N-labeled eIF1AΔC or eIF1AΔNC affects most of the same surfaces affected by the respective deletion (data not shown). Therefore, eIF1A-CT16 contacts the OB domain at a specific surface.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":138,"end":144,"reference_id":"27325746","reference_source":"pmid","reference_html":"eIF1A/eIF5B interaction network and its functions in translation initiation complex assembly and remodeling. <i> Nag N, Lin KY, Edmonds KA, Yu J, Nadkarni D, Marintcheva B, Marintchev A. </i> Nucleic Acids Res, 2016","date":"2022-07-27T17:24:23.235Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006309","ec_ontology":"ECO","ec_name":"competitive binding evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"O60841","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00903r006","statement":[{"text":"The affinity of Fl-eIF1A-CT7 for eIF5B-D4 was 12 μM. Competition FA assays using Fl-eIF1A-CT7 showed that the binding affinities of eIF1A-CT16 (12 μM) and of the full 26-residue eIF1A-CTT (12 μM) were similar (Figure ​3A and B, Table 1). In contrast, the affinity of full-length eIF1A for eIF5B-D4 was 39 μM, much weaker than that of eIF1A-CTT (Figure ​3B and Table ​1).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_P47813","date":"2016-09-05T13:14:00.000Z","acc":"P47813","name":"Eukaryotic translation initiation factor 1A, X-chromosomal","length":144,"organism":"Homo sapiens","dataset":["Cancer-related proteins","RNA-binding proteins"],"UniParc":"UPI0000110EFF","genes":[{"name":{"value":"EIF1AX"},"synonyms":[{"value":"EIF1A"},{"value":"EIF4C"}]}],"alphafold_very_low_content":0.10416666666666667,"disorder_content":0.3680555555555556,"disprot_consensus":{"full":[{"start":1,"end":27,"type":"D"},{"start":119,"end":144,"type":"D"}],"Structural state":[{"start":1,"end":27,"type":"D"},{"start":119,"end":144,"type":"D"}],"Molecular function":[{"start":129,"end":144,"type":"F"}]}},{"features":{"pfam":[{"id":"PF09873","name":"SepCysE-like","start":2,"end":212}]},"uniref50":"UniRef50_Q58876","sequence":"MRVEYSKDLIRKGISTISQLKKAKIRVEKDDKKISYKDAKPGKIDVNEFKKAIYLLIEADDFLYKKAPKHELNEEEAKEFCKLIIKCQEHLNKILANFGFEFEEKEIDEGALYIVSNKKLFKKLKNKNPNLKVVCTEGMLDIEDMRAIGVPEKALEGLKKKVEIARKNVERFIEKYKPEKIFVVVEDDKDELLYLRAKNLYNAEKLDADEILD","taxonomy":["Archaea","Euryarchaeota","Methanomada group","Methanococci","Methanococcales","Methanocaldococcaceae","Methanocaldococcus"],"uniref90":"UniRef90_Q58876","disprot_id":"DP00904","ncbi_taxon_id":243232,"regions_counter":1,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":213,"region_id":"DP00904r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Ancient translation factor is essential for tRNA-dependent cysteine biosynthesis in methanogenic archaea. <i> Liu Y, Nakamura A, Nakazawa Y, Asano N, Ford KA, Hohn MJ, Tanaka I, Yao M, Söll D. </i> Proc Natl Acad Sci U S A, 2014","term_id":"IDPO:0000002","curator_id":"atantos","start":104,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3WKR"}],"reference_id":"25002468","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q58876","date":"2016-09-05T13:19:48.000Z","acc":"Q58876","name":"Uncharacterized protein MJ1481","length":213,"organism":"Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)","dataset":[],"UniParc":"UPI000013AB45","genes":[{"olnNames":[{"value":"MJ1481"}]}],"alphafold_very_low_content":0.03755868544600939,"disorder_content":0.5164319248826291,"disprot_consensus":{"full":[{"start":104,"end":213,"type":"D"}],"Structural state":[{"start":104,"end":213,"type":"D"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MASEELQKDLEEVKVLLEKATRKRVRDALTAEKSKIETEIKNKMQQKSQKKAELLDNEKPAAVVAPITTGYTDGISQISL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"","disprot_id":"DP00907","ncbi_taxon_id":9606,"regions_counter":3,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":80,"region_id":"DP00907r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural analysis of Siah1-Siah-interacting protein interactions and insights into the assembly of an E3 ligase multiprotein complex. <i> Santelli E, Leone M, Li C, Fukushima T, Preece NE, Olson AJ, Ely KR, Reed JC, Pellecchia M, Liddington RC, Matsuzawa S. </i> J Biol Chem, 2005","term_id":"IDPO:0000002","curator_id":"atantos","start":48,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"16085652","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":80,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural analysis of Siah1-Siah-interacting protein interactions and insights into the assembly of an E3 ligase multiprotein complex. <i> Santelli E, Leone M, Li C, Fukushima T, Preece NE, Olson AJ, Ely KR, Reed JC, Pellecchia M, Liddington RC, Matsuzawa S. </i> J Biol Chem, 2005","term_id":"IDPO:0000011","curator_id":"atantos","start":48,"term_ontology":"IDPO","curator_name":"Agnes Tantos","reference_id":"16085652","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00907r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":80,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural analysis of Siah1-Siah-interacting protein interactions and insights into the assembly of an E3 ligase multiprotein complex. <i> Santelli E, Leone M, Li C, Fukushima T, Preece NE, Olson AJ, Ely KR, Reed JC, Pellecchia M, Liddington RC, Matsuzawa S. </i> J Biol Chem, 2005","term_id":"GO:0005515","curator_id":"atantos","start":48,"term_ontology":"GO","curator_name":"Agnes Tantos","reference_id":"16085652","version":3,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00907r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"","date":"2016-09-05T14:11:45.000Z","acc":"Q9HB71-2","name":"Isoform 2 of Calcyclin-binding protein","length":80,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000035D69","genes":[{"name":{"value":"CACYBP"},"synonyms":[{"value":"S100A6BP"},{"value":"SIP"}],"orfNames":[{"value":"PNAS-107"}]}],"disorder_content":0.4125,"disprot_consensus":{"full":[{"start":48,"end":80,"type":"T"}],"Structural state":[{"start":48,"end":80,"type":"D"}],"Structural transition":[{"start":48,"end":80,"type":"T"}],"Molecular function":[{"start":48,"end":80,"type":"F"}]}},{"features":{"pfam":[{"id":"PF07704","name":"Rv0623-like transcription factor","start":1,"end":83}]},"uniref50":"UniRef50_A0QRY5","sequence":"MALSIKHPEADRLARALAARTGETLTEAVVTALRERLARETGRARVVPLRDELAAIRHRCAALPVVDNRSAEAILGYDERGLPA","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"uniref90":"UniRef90_P9WJ34","disprot_id":"DP00908","dataset":["Unicellular toxins and antitoxins"],"ncbi_taxon_id":83332,"regions_counter":1,"creator":"atantos","regions":[{"region_id":"DP00908r001","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T11:04:15.519Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":46,"term_id":"IDPO:0000002","start":1,"version":4,"statement":[{"text":"For VapB30, we were unable to build the residues Met1–Val46 and residues Tyr77–Ala84 because of ambiguous or missing electron density in crystal form II. In crystal form I, the electron density of the residues Met1–Val46 was also absent; however, additional residues (Tyr77–Glu79) in chains B and H were visible in the electron density map.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26150422","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4XGQ"},{"db":"PDB","id":"4xgr"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structural and functional studies of the Mycobacterium tuberculosis VapBC30 toxin-antitoxin system: implications for the design of novel antimicrobial peptides. <i> Lee IG, Lee SJ, Chae S, Lee KY, Kim JH, Lee BJ. </i> Nucleic Acids Res, 2015","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P9WJ34","date":"2016-09-05T14:48:10.000Z","acc":"P9WJ35","name":"Antitoxin VapB30","length":84,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","UniParc":"UPI00000D119D","genes":[{"name":{"value":"vapB30"},"olnNames":[{"value":"Rv0623"}]}],"alphafold_very_low_content":0,"disorder_content":0.5476190476190477,"disprot_consensus":{"full":[{"start":1,"end":46,"type":"D"}],"Structural state":[{"start":1,"end":46,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01253","name":"Translation initiation factor SUI1","start":28,"end":101}],"gene3D":[{"start":1,"end":113,"id":"3.30.780.10","name":"SUI1-like domain"}]},"uniref50":"UniRef50_P41567","sequence":"MSAIQNLHSFDPFADASKGDDLLPAGTEDYIHIRIQQRNGRKTLTTVQGIADDYDKKKLVKAFKKKFACNGTVIEHPEYGEVIQLQGDQRKNICQFLVEIGLAKDDQLKVHGF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P41567","disprot_id":"DP00910","ncbi_taxon_id":9606,"regions_counter":1,"creator":"ameszaros","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":28,"region_id":"DP00910r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure and interactions of the translation initiation factor eIF1. <i> Fletcher CM, Pestova TV, Hellen CU, Wagner G. </i> EMBO J, 1999","term_id":"IDPO:0000002","curator_id":"ameszaros","start":1,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"10228174","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2IF1"}],"term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P41567","date":"2016-09-05T15:23:13.000Z","acc":"P41567","name":"Eukaryotic translation initiation factor 1","length":113,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000000DC99","genes":[{"name":{"value":"EIF1"},"synonyms":[{"value":"SUI1"}]}],"alphafold_very_low_content":0.07079646017699115,"disorder_content":0.24778761061946902,"disprot_consensus":{"full":[{"start":1,"end":28,"type":"D"}],"Structural state":[{"start":1,"end":28,"type":"D"}]}},{"features":{"pfam":[{"id":"PF06747","name":"CHCH domain","start":64,"end":100}]},"uniref50":"UniRef50_Q8N4Q1","sequence":"MSYCRQEGKDRIIFVTKEDHETPSSAELVADDPNDPYEEHGLILPNGNINWNCPCLGGMASGPCGEQFKSAFSCFHYSTEEIKGSDCVDQFRAMQECMQKYPDLYPQEDEDEEEEREKKPAEQAEETAPIEATATKEEEGSS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q8N4Q1","disprot_id":"DP00912","ncbi_taxon_id":9606,"regions_counter":1,"creator":"ahatos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":142,"region_id":"DP00912r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"MIA40 is an oxidoreductase that catalyzes oxidative protein folding in mitochondria. <i> Banci L, Bertini I, Cefaro C, Ciofi-Baffoni S, Gallo A, Martinelli M, Sideris DP, Katrakili N, Tokatlidis K. </i> Nat Struct Mol Biol, 2009","term_id":"IDPO:0000002","curator_id":"ahatos","start":107,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2K3J"}],"reference_id":"19182799","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q8N4Q1","date":"2016-09-05T15:49:42.000Z","acc":"Q8N4Q1","name":"Mitochondrial intermembrane space import and assembly protein 40","length":142,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000006E0C5","genes":[{"name":{"value":"CHCHD4"},"synonyms":[{"value":"MIA40"}]}],"alphafold_very_low_content":0.176056338028169,"disorder_content":0.2535211267605634,"disprot_consensus":{"full":[{"start":107,"end":142,"type":"D"}],"Structural state":[{"start":107,"end":142,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00202","name":"Aminotransferase class-III","start":420,"end":843}],"gene3D":[{"start":137,"end":275,"id":"3.40.50.720","name":"NAD(P)-binding Rossmann-like Domain"}]},"uniref50":"UniRef50_A0A0J9X1Q5","sequence":"MKFGFIAHPTSLGLKRYVKMLDLLQRNSTEQHSGYTRELWERQNLVPFMNFARITSATGATCEGVIKYMPLVADEMLADARGIAARVVQGIEELAGDGAELVGLGGFTSIVGRRGEATAEKSPVPVTSGNSLTTYAGYKALMQIQSWLEIRPEEEPVAIVGYPGSICLALSRLLLAHGFSLHLLHRAGNHDRSELLSHLPEEYHSRVTLTSDPEDLYPRCKLFAAATSAGGVIDPARLQPGSIFIDVALPRDIASETRPARDDILIIDGGCVTATDAVKLGGESLNVTIKQQLNGCMAETIVLALENRRENFSLGRYLAPEKVLEIGEIAERHGFFAYPLASYGERIDRQSVTNLKRYYHHDIYAGESADAALPASRLAFIDAVIAQTPAREDTLDRYHQYINPMMVDFLKLQRCDNVFRSAAGTQLYDDAGEAFLDMVAGYGCLNLGHNPQPVVNALKNYLDAQGPNFIQYISIPEQTAKLAEVLCRLAPGNMGRVFFSNSGTEAVEAAMKIAKASTGKPGIAYLRNSYHGKTLGALSITGRDKHRRYFTPLLDAMVEVPFGDLAALREALNREDVGALMIEPIQGEGGVHIPPAGYLQAVQQLCRETGVLLMVDEVQTGLGRTGKLFACEWDGIEPDVLMLSKSLSGGLIPIGATLCRADLWQKAYGTADRFLVHSSTYGGGNLASVVALSALREILAQDLVGHAERMGAYFKQALSEIAARYPFVSEVRGRGLMLGIQFDQAFTGAVNASAREFATRLPGDWHTTWKFLPDPVQAHLRAAMDRMEQALGEMFCMKFVTKLCQDHKILTFITANSSTVIRIQPPLIISKAEIDRFVGAFATVCEELSTFLD","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Serratia","unclassified Serratia"],"uniref90":"UniRef90_A0A0J9X1Q5","disprot_id":"DP00913","ncbi_taxon_id":1327989,"regions_counter":3,"creator":"ahatos","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":764,"region_id":"DP00913r001","start":746,"ec_id":"ECO:0006220","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"no electron density visible for residues from 745 to 765 of chain A and 743 to 765 of chain B, respectively","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24704447","version":3,"reference_html":"Crystal structure of the catalytic domain of PigE: a transaminase involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP) from Serratia sp. FS14. <i> Lou X, Ran T, Han N, Gao Y, He J, Tang L, Xu D, Wang W. </i> Biochem Biophys Res Commun, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","cross_refs":[{"db":"PDB","id":"4PPM"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":371,"region_id":"DP00913r003","reference_id":"24704447","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Surprisingly, the final model contains only 481 amino acids, including residues from Ala372 to Asp853, no electron density visible for the fragment from residues Met1 to Ala371.","type":"Results"},{"text":"In the final model, both monomers include the residues from 372 to 853, but no electron density visible for residues from 745 to 765 of chain A and 743 to 765 of chain B, respectively.","type":"Results"},{"text":"Sequence analysis showed that the C terminal of PigE (residue 372–853) is the putative catalytic domain, which shares some homology with the PLP-dependent aminotransferase family proteins, but the function for the N-terminal domain (residue 1–371) is unclear.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Crystal structure of the catalytic domain of PigE: a transaminase involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP) from Serratia sp. FS14. <i> Lou X, Ran T, Han N, Gao Y, He J, Tang L, Xu D, Wang W. </i> Biochem Biophys Res Commun, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4PPM"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_A0A0J9X1Q5","date":"2016-09-05T15:49:59.000Z","acc":"A0A0J9X1Q5","name":"Aminotransferase PigE","length":853,"organism":"Serratia sp. (strain FS14)","dataset":[],"UniParc":"UPI0002AF2381","genes":[{"name":{"value":"pigE","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"24704447","url":"http://www.ncbi.nlm.nih.gov/pubmed/24704447","alternativeUrl":"https://europepmc.org/abstract/MED/24704447"}}]},"orfNames":[{"value":"L085_23050","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AIA50007.1","url":"https://www.ebi.ac.uk/ena/browser/view/AIA50007.1"}}]}]}],"alphafold_very_low_content":0.01875732708089097,"disorder_content":0.45720984759671746,"disprot_consensus":{"full":[{"start":1,"end":371,"type":"D"},{"start":746,"end":764,"type":"D"}],"Structural state":[{"start":1,"end":371,"type":"D"},{"start":746,"end":764,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01176","name":"Translation initiation factor 1A / IF-1","start":22,"end":116}],"gene3D":[{"start":2,"end":146,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}]},"uniref50":"UniRef50_I7MK25","sequence":"MPKNKGRGGKNYRRGKNENETKRELVFKEEGMEYAQVIKMLGNGRLEVFCFDGKRRIGHICGRLKKKVWISMDDIVLVGLRDFQDDKCDILLKYLPDEVRNLKQYGEIDENIKINDKSGADQADVVFEDSDSDDKDDDDDDEDEQPTRQTNTRVNQMVESSDEEDNKETGNYEEQKYDQKHQNKKDDIDIDDI","taxonomy":["Eukaryota","Sar","Alveolata","Ciliophora","Intramacronucleata","Oligohymenophorea","Hymenostomatida","Tetrahymenina","Tetrahymenidae","Tetrahymena"],"uniref90":"UniRef90_I7MK25","disprot_id":"DP00914","ncbi_taxon_id":312017,"regions_counter":3,"creator":"ahatos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":17,"region_id":"DP00914r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The crystal structure of the eukaryotic 40S ribosomal subunit in complex with eIF1 and eIF1A. <i> Weisser M, Voigts-Hoffmann F, Rabl J, Leibundgut M, Ban N. </i> Nat Struct Mol Biol, 2013","term_id":"IDPO:0000002","curator_id":"ahatos","start":1,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2XZM"}],"reference_id":"23851459","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":17,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"The crystal structure of the eukaryotic 40S ribosomal subunit in complex with eIF1 and eIF1A. <i> Weisser M, Voigts-Hoffmann F, Rabl J, Leibundgut M, Ban N. </i> Nat Struct Mol Biol, 2013","term_id":"GO:0060090","curator_id":"ahatos","start":1,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"23851459","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00914r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":17,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"The crystal structure of the eukaryotic 40S ribosomal subunit in complex with eIF1 and eIF1A. <i> Weisser M, Voigts-Hoffmann F, Rabl J, Leibundgut M, Ban N. </i> Nat Struct Mol Biol, 2013","term_id":"GO:0005515","curator_id":"ahatos","start":1,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"23851459","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00914r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_I7MK25","date":"2016-09-05T15:50:11.000Z","acc":"I7MK25","name":"Eukaryotic translation initiation factor 1A","length":193,"organism":"Tetrahymena thermophila (strain SB210)","dataset":[],"UniParc":"UPI00006CA4A1","genes":[{"orfNames":[{"value":"TTHERM_00497990","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EAS07745.3","url":"https://www.ebi.ac.uk/ena/browser/view/EAS07745.3"}}]}]}],"alphafold_very_low_content":0.31088082901554404,"disorder_content":0.08808290155440414,"disprot_consensus":{"full":[{"start":1,"end":17,"type":"D"}],"Structural state":[{"start":1,"end":17,"type":"D"}],"Molecular function":[{"start":1,"end":17,"type":"F"}]}},{"features":{"pfam":[{"id":"PF28198","name":"PCNA-interacting regulator","start":1,"end":63}]},"uniref50":"UniRef50_Q5JH72","sequence":"MDRKLDEFIGDATPKKVSKEKPVRRKKRLKPTSLDSFLPEEHINYFRDLRIGSKKIRNAKIEEL","taxonomy":["Archaea","Euryarchaeota","Thermococci","Thermococcales","Thermococcaceae","Thermococcus"],"uniref90":"UniRef90_Q5JH72","disprot_id":"DP00915","ncbi_taxon_id":69014,"regions_counter":2,"creator":"ahatos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":27,"region_id":"DP00915r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"A small protein inhibits proliferating cell nuclear antigen by breaking the DNA clamp. <i> Altieri AS, Ladner JE, Li Z, Robinson H, Sallman ZF, Marino JP, Kelman Z. </i> Nucleic Acids Res, 2016","term_id":"IDPO:0000002","curator_id":"ahatos","start":1,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5DA7"}],"reference_id":"27141962","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":27,"region_id":"DP00915r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"A small protein inhibits proliferating cell nuclear antigen by breaking the DNA clamp. <i> Altieri AS, Ladner JE, Li Z, Robinson H, Sallman ZF, Marino JP, Kelman Z. </i> Nucleic Acids Res, 2016","term_id":"IDPO:0000002","curator_id":"ahatos","start":1,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27141962","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q5JH72","date":"2016-09-05T15:50:21.000Z","acc":"Q5JH72","name":"PCNA-inhibitor","length":64,"organism":"Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)","dataset":[],"UniParc":"UPI00004A3361","genes":[{"olnNames":[{"value":"TK0808","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"BAD84997.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAD84997.1"}}]}]}],"alphafold_very_low_content":0.015625,"disorder_content":0.421875,"disprot_consensus":{"full":[{"start":1,"end":27,"type":"D"}],"Structural state":[{"start":1,"end":27,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00581","name":"Rhodanese-like domain","start":31,"end":128}],"gene3D":[{"start":15,"end":146,"id":"3.40.250.10","name":"Rhodanese-like domain"}]},"uniref50":"UniRef50_Q8GY31","sequence":"MGRSIFSFFTKKKKMAMARSISYITSTQLLPLHRRPNIAIIDVRDEERNYDGHIAGSLHYASGSFDDKISHLVQNVKDKDTLVFHCALSQVRGPTCARRLVNYLDEKKEDTGIKNIMILERGFNGWEASGKPVCRCAEVPCKGDCA","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q8GY31","disprot_id":"DP00916","ncbi_taxon_id":3702,"regions_counter":3,"creator":"ahatos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":146,"region_id":"DP00916r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana. <i> Landrieu I, da Costa M, De Veylder L, Dewitte F, Vandepoele K, Hassan S, Wieruszeski JM, Corellou F, Faure JD, Van Montagu M, Inzé D, Lippens G. </i> Proc Natl Acad Sci U S A, 2004","term_id":"IDPO:0000002","curator_id":"ahatos","start":130,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1T3K"}],"reference_id":"15329414","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":146,"term_name":"ion binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana. <i> Landrieu I, da Costa M, De Veylder L, Dewitte F, Vandepoele K, Hassan S, Wieruszeski JM, Corellou F, Faure JD, Van Montagu M, Inzé D, Lippens G. </i> Proc Natl Acad Sci U S A, 2004","term_id":"GO:0043167","curator_id":"ahatos","start":130,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"15329414","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00916r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q8GY31","date":"2016-09-05T15:51:08.000Z","acc":"Q8GY31","name":"Dual specificity phosphatase Cdc25","length":146,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI000000C0E8","genes":[{"name":{"value":"CDC25","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15329414","url":"http://www.ncbi.nlm.nih.gov/pubmed/15329414","alternativeUrl":"https://europepmc.org/abstract/MED/15329414"}}]},"synonyms":[{"value":"ACR2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16567632","url":"http://www.ncbi.nlm.nih.gov/pubmed/16567632","alternativeUrl":"https://europepmc.org/abstract/MED/16567632"}}]},{"value":"ASR","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16507083","url":"http://www.ncbi.nlm.nih.gov/pubmed/16507083","alternativeUrl":"https://europepmc.org/abstract/MED/16507083"}}]},{"value":"STR5","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"17408957","url":"http://www.ncbi.nlm.nih.gov/pubmed/17408957","alternativeUrl":"https://europepmc.org/abstract/MED/17408957"}}]}],"orfNames":[{"value":"F12E4_220","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"CAB83305.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAB83305.1"}}]}],"olnNames":[{"value":"At5g03455","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT5G03455","url":""}}]}]}],"alphafold_very_low_content":0.0958904109589041,"disorder_content":0.11643835616438356,"disprot_consensus":{"full":[{"start":130,"end":146,"type":"D"}],"Structural state":[{"start":130,"end":146,"type":"D"}],"Molecular function":[{"start":130,"end":146,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02404","name":"Stem cell factor","start":1,"end":273}],"gene3D":[{"start":28,"end":171,"id":"1.20.1250.10","name":"1.20.1250.10"}]},"uniref50":"UniRef50_P21583","sequence":"MKKTQTWILTCIYLQLLLFNPLVKTEGICRNRVTNNVKDVTKLVANLPKDYMITLKYVPGMDVLPSHCWISEMVVQLSDSLTDLLDKFSNISEGLSNYSIIDKLVNIVDDLVECVKENSSKDLKKSFKSPEPRLFTPEEFFRIFNRSIDAFKDFVVASETSDCVVSSTLSPEKDSRVSVTKPFMLPPVAASSLRNDSSSSNRKAKNPPGDSSLHWAAMALPALFSLIIGFAFGALYWKKRQPSLTRAVENIQINEEDNEISMLQEKEREFQEV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P21583","disprot_id":"DP00917","ncbi_taxon_id":9606,"regions_counter":4,"creator":"ahatos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":103,"region_id":"DP00917r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the active core of human stem cell factor and analysis of binding to its receptor kit. <i> Jiang X, Gurel O, Mendiaz EA, Stearns GW, Clogston CL, Lu HS, Osslund TD, Syed RS, Langley KE, Hendrickson WA. </i> EMBO J, 2000","term_id":"IDPO:0000002","curator_id":"ahatos","start":92,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1SCF"}],"reference_id":"10880433","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":103,"term_name":"flexible linker","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of the active core of human stem cell factor and analysis of binding to its receptor kit. <i> Jiang X, Gurel O, Mendiaz EA, Stearns GW, Clogston CL, Lu HS, Osslund TD, Syed RS, Langley KE, Hendrickson WA. </i> EMBO J, 2000","term_id":"IDPO:0000033","curator_id":"ahatos","start":92,"term_ontology":"IDPO","curator_name":"András Hatos","reference_id":"10880433","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00917r002","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":141,"region_id":"DP00917r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the active core of human stem cell factor and analysis of binding to its receptor kit. <i> Jiang X, Gurel O, Mendiaz EA, Stearns GW, Clogston CL, Lu HS, Osslund TD, Syed RS, Langley KE, Hendrickson WA. </i> EMBO J, 2000","term_id":"IDPO:0000002","curator_id":"ahatos","start":127,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1SCF"}],"reference_id":"10880433","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":141,"term_name":"flexible linker","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of the active core of human stem cell factor and analysis of binding to its receptor kit. <i> Jiang X, Gurel O, Mendiaz EA, Stearns GW, Clogston CL, Lu HS, Osslund TD, Syed RS, Langley KE, Hendrickson WA. </i> EMBO J, 2000","term_id":"IDPO:0000033","curator_id":"ahatos","start":127,"term_ontology":"IDPO","curator_name":"András Hatos","reference_id":"10880433","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00917r004","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_P21583","date":"2016-09-05T15:51:25.000Z","acc":"P21583","name":"Kit ligand","length":273,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000002D482","genes":[{"name":{"value":"KITLG"},"synonyms":[{"value":"MGF"},{"value":"SCF"}]}],"alphafold_very_low_content":0.19047619047619047,"disorder_content":0.0989010989010989,"disprot_consensus":{"full":[{"start":92,"end":103,"type":"D"},{"start":127,"end":141,"type":"D"}],"Structural state":[{"start":92,"end":103,"type":"D"},{"start":127,"end":141,"type":"D"}],"Disorder function":[{"start":92,"end":103,"type":"F"},{"start":127,"end":141,"type":"F"}]}},{"features":{"pfam":[{"id":"PF19155","name":"Family of unknown function (DUF5837)","start":1,"end":70}]},"uniref50":"UniRef50_A0MHA3","sequence":"MNKKNILPQQGQPVIRLTAGQLSSQLAELSEEALGDAGLEASVTACITFCAYDGVEPSCTLCYTLCAYDGE","taxonomy":["Bacteria","Cyanobacteria","Synechococcales","Prochloraceae","Prochloron","environmental samples"],"uniref90":"UniRef90_A0MHA3","disprot_id":"DP00918","ncbi_taxon_id":259942,"regions_counter":1,"creator":"ahatos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":64,"region_id":"DP00918r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural analysis of leader peptide binding enables leader-free cyanobactin processing. <i> Koehnke J, Mann G, Bent AF, Ludewig H, Shirran S, Botting C, Lebl T, Houssen W, Jaspars M, Naismith JH. </i> Nat Chem Biol, 2015","term_id":"IDPO:0000002","curator_id":"ahatos","start":36,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4V1T"}],"reference_id":"26098679","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_A0MHA3","date":"2016-09-05T15:52:18.000Z","acc":"A0MHA3","name":"Patellamide protein","length":71,"organism":"uncultured Prochloron sp","dataset":[],"UniParc":"UPI0000E69AEC","genes":[{"name":{"value":"patE","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ABI99463.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABI99463.1"}}]}}],"alphafold_very_low_content":0.29577464788732394,"disorder_content":0.4084507042253521,"disprot_consensus":{"full":[{"start":36,"end":64,"type":"D"}],"Structural state":[{"start":36,"end":64,"type":"D"}]}},{"acc":"C6KEI3","sequence":"MGGKWSKSSIVGWPAIRERLRRAQPAAERRRAQPAAEGVGAASQDLGRHGALTSSNTDTTNADEEEEVGFPVRPQVPLRPMTYKGAVDLSFFLKEKGGLEGLVYSQKRKEILDLWVYHTQGYFPDWQCYTPGPGVRYPLTFGWCFKLVPVDPGEVEEATEGENNCLLHPICQHGMDDDHREVLKWKFDSHLAHTHMARELHPEFYKNC","creator":"jbergier","dataset":["Viral proteins"],"date":"2016-09-05T15:52:27.000Z","disprot_id":"DP00919","features":{"pfam":[{"id":"PF00469","name":"Negative factor, (F-Protein) or Nef","start":2,"end":207}]},"genes":[{"name":{"value":"nef","evidences":[{"source":{"id":"MF_04078","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04078","_id":"685af523b4ac24d5329d8759"},"code":"ECO:0000256","_id":"685af523b4ac24d5329d8758"},{"source":{"id":"ACS68799.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/ACS68799.1","_id":"685af523b4ac24d5329d875b"},"code":"ECO:0000313","_id":"685af523b4ac24d5329d875a"}],"_id":"685af523b4ac24d5329d875c"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d8757"}],"length":208,"name":"Protein Nef","ncbi_taxon_id":11676,"organism":"Human immunodeficiency virus 1","regions_counter":4,"released":"2016_10","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"UniParc":"UPI0001A94C43","uniref100":"UniRef100_C6KEI3","uniref50":"UniRef50_P03406","uniref90":"UniRef90_C6KEI3","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2XI1","_id":"685af523b4ac24d5329d8748"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":152,"end":180,"interaction_partner":[],"reference_html":"A novel dimer-tetramer transition captured by the crystal structure of the HIV-1 Nef. <i> Singh P, Yadav GP, Gupta S, Tripathi AK, Ramachandran R, Tripathi RK. </i> PLoS One, 2011","reference_id":"22073177","region_id":"DP00919r001","released":"2022_03","sample":[],"statement":[{"type":"Figure","text":"The PXXP motif in the present structure is from residues 74–80 while the 30-residue disordered loop distal to this motif ranges from residues 151–180.","_id":"685af523b4ac24d5329d8749"},{"type":"Curator statement","text":"There are two structural analysis in the PDB showing disorder regions:151-180 and 152-180. 152-180 comprises both structural analysis","_id":"685af523b4ac24d5329d874a"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T09:25:08.875Z","_id":"685af523b4ac24d5329d874b"},"version":3,"_id":"685af523b4ac24d5329d8747","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2XI1","_id":"685af523b4ac24d5329d874f"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":75,"interaction_partner":[],"reference_html":"A novel dimer-tetramer transition captured by the crystal structure of the HIV-1 Nef. <i> Singh P, Yadav GP, Gupta S, Tripathi AK, Ramachandran R, Tripathi RK. </i> PLoS One, 2011","reference_id":"22073177","region_id":"DP00919r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"On the other hand, the N-terminal anchor domain is disordered in the full-length structure.","_id":"685af523b4ac24d5329d8750"},{"type":"Methods","text":"Crystal diffraction and poor reproducibility were problems faced during the experiments and in hindsight were probably due to the disordered N-terminal domain as explained in ‘Results’.","_id":"685af523b4ac24d5329d8751"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T09:25:09.900Z","_id":"685af523b4ac24d5329d8752"},"version":3,"_id":"685af523b4ac24d5329d874e","reference_source":"pmid"}],"__v":0,"disorder_content":0.5,"disprot_consensus":{"full":[{"start":1,"end":75,"type":"D"},{"start":152,"end":180,"type":"D"}],"Structural state":[{"start":1,"end":75,"type":"D"},{"start":152,"end":180,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00412","name":"LIM domain","start":10,"end":65},{"id":"PF00412","name":"LIM domain","start":118,"end":174}],"gene3D":[{"start":108,"end":192,"id":"2.10.110.10","name":"Cysteine Rich Protein"},{"start":1,"end":81,"id":"2.10.110.10","name":"Cysteine Rich Protein"}]},"uniref50":"UniRef50_P67966","sequence":"MPNWGGGKKCGVCQKAVYFAEEVQCEGSSFHKSCFLCMVCKKNLDSTTVAVHGDEIYCKSCYGKKYGPKGYGYGMGAGTLSTDKGESLGIKYEEGQSHRPTNPNASRMAQKVGGSDGCPRCGQAVYAAEKVIGAGKSWHKSCFRCAKCGKSLESTTLADKDGEIYCKGCYAKNFGPKGFGFGQGAGALIHSQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Phasianinae","Gallus"],"uniref90":"UniRef90_P67966","disprot_id":"DP00922","ncbi_taxon_id":9031,"regions_counter":2,"creator":"ahatos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":115,"region_id":"DP00922r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of the chicken cysteine-rich protein, CRP1, a double-LIM protein implicated in muscle differentiation. <i> Yao X, Pérez-Alvarado GC, Louis HA, Pomiès P, Hatt C, Summers MF, Beckerle MC. </i> Biochemistry, 1999","term_id":"IDPO:0000002","curator_id":"ahatos","start":67,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1B8T"}],"reference_id":"10231520","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":115,"term_name":"flexible linker","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Solution structure of the chicken cysteine-rich protein, CRP1, a double-LIM protein implicated in muscle differentiation. <i> Yao X, Pérez-Alvarado GC, Louis HA, Pomiès P, Hatt C, Summers MF, Beckerle MC. </i> Biochemistry, 1999","term_id":"IDPO:0000033","curator_id":"ahatos","start":67,"term_ontology":"IDPO","curator_name":"András Hatos","reference_id":"10231520","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00922r002","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_P67966","date":"2016-09-05T15:52:55.000Z","acc":"P67966","name":"Cysteine and glycine-rich protein 1","length":192,"organism":"Gallus gallus","dataset":[],"UniParc":"UPI00001711EC","genes":[{"name":{"value":"CSRP1"},"synonyms":[{"value":"CSRP"}]}],"alphafold_very_low_content":0.0625,"disorder_content":0.2552083333333333,"disprot_consensus":{"full":[{"start":67,"end":115,"type":"D"}],"Structural state":[{"start":67,"end":115,"type":"D"}],"Disorder function":[{"start":67,"end":115,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00520","name":"Ion transport protein","start":17,"end":236}],"gene3D":[{"start":7,"end":122,"id":"1.20.120.350","name":"Voltage-gated potassium channels. Chain C"},{"start":124,"end":226,"id":"1.10.287.70","name":"1.10.287.70"}]},"uniref50":"UniRef50_W4QN78","sequence":"MQKQSLLIHFSKKIVSHRYFTRIIITLILFNALLVGLETYPALRHEYGSLFHVLDVILLWIFTLEILTRFLATTPKKDFFKGGWNWFDTIIVLSSHIFVGGHFITVLRILRVLRVLRAISVIPSLRRLVDALMLTIPALGNILILMSIIFYIFAVLGTMLFANVAPEYFANLQLSMLTLFQIVTLDSWGSGVMRPILVDIPWAWTYFIAFVLVGTFIIFNLFIGVIVNNVEKANEDEVKDKVKEKEEAAQKQMDSLHEELKEIKQYLKSIEKQNRSS","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Alkalihalobacillus"],"uniref90":"UniRef90_J8TM36","disprot_id":"DP00925","ncbi_taxon_id":1218173,"regions_counter":2,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":249,"region_id":"DP00925r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structure of the C-terminal domain of the prokaryotic sodium channel orthologue NsvBa. <i> Miller WC, Miles AJ, Wallace BA. </i> Eur Biophys J, 2016","term_id":"IDPO:0000002","curator_id":"atantos","start":236,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PCDDB","id":"CD0005306000"},{"db":"PCDDB","id":"CD0005333000"}],"reference_id":"27106836","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":249,"term_name":"flexible linker","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Structure of the C-terminal domain of the prokaryotic sodium channel orthologue NsvBa. <i> Miller WC, Miles AJ, Wallace BA. </i> Eur Biophys J, 2016","term_id":"IDPO:0000033","curator_id":"atantos","start":236,"term_ontology":"IDPO","curator_name":"Agnes Tantos","reference_id":"27106836","version":3,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00925r002","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_J8TM36","date":"2016-09-05T16:15:26.000Z","acc":"J8TM36","name":"Cation transporter","length":277,"organism":"Bacillus alcalophilus ATCC 27647 = CGMCC 1.3604","dataset":[],"UniParc":"UPI00027BB5D8","genes":[{"orfNames":[{"value":"AJ85_20185","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"THG88991.1","url":"https://www.ebi.ac.uk/ena/browser/view/THG88991.1"}}]},{"value":"BalcAV3624","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AFV25941.1","url":"https://www.ebi.ac.uk/ena/browser/view/AFV25941.1"}}]},{"value":"BALCAV_0212230","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"KGA97090.1","url":"https://www.ebi.ac.uk/ena/browser/view/KGA97090.1"}}]}]}],"alphafold_very_low_content":0.0036101083032490976,"disorder_content":0.05054151624548736,"disprot_consensus":{"full":[{"start":236,"end":249,"type":"D"}],"Structural state":[{"start":236,"end":249,"type":"D"}],"Disorder function":[{"start":236,"end":249,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05463","name":"Sclerostin (SOST)","start":1,"end":210}],"gene3D":[{"start":73,"end":169,"id":"2.10.90.10","name":"Cystine-knot cytokines"}]},"uniref50":"UniRef50_Q9BQB4","sequence":"MQLPLALCLVCLLVHTAFRVVEGQGWQAFKNDATEIIPELGEYPEPPPELENNKTMNRAENGGRPPHHPFETKDVSEYSCRELHFTRYVTDGPCRSAKPVTELVCSGQCGPARLLPNAIGRGKWWRPSGPDFRCIPDRYRAQRVQLLCPGGEAPRARKVRLVASCKCKRLTRFHNQSELKDFGTEAARPQKGRKPRPRARSAKANQAELENAY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9BQB4","disprot_id":"DP00926","ncbi_taxon_id":9606,"regions_counter":12,"creator":"zdosztanyi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":79,"region_id":"DP00926r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Characterization of the structural features and interactions of sclerostin: molecular insight into a key regulator of Wnt-mediated bone formation. <i> Veverka V, Henry AJ, Slocombe PM, Ventom A, Mulloy B, Muskett FW, Muzylak M, Greenslade K, Moore A, Zhang L, Gong J, Qian X, Paszty C, Taylor RJ, Robinson MK, Carr MD. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"esalladini","start":25,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2K8P"}],"reference_id":"19208630","statement":[{"text":"The NMR data clearly indicate that the fairly long N- and C-terminal regions (residues 1-55 and 145-189) of sclerostin are highly flexible and completely disordered (Fig. 2A).","type":"Results"},{"text":"The IDR characterized in the publication residues 1-55 corresponds to region 25-79 of the amino acid sequence.","type":"Curator statement"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-18T15:07:36.210Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":213,"region_id":"DP00926r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Characterization of the structural features and interactions of sclerostin: molecular insight into a key regulator of Wnt-mediated bone formation. <i> Veverka V, Henry AJ, Slocombe PM, Ventom A, Mulloy B, Muskett FW, Muzylak M, Greenslade K, Moore A, Zhang L, Gong J, Qian X, Paszty C, Taylor RJ, Robinson MK, Carr MD. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"esalladini","start":169,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2K8P"}],"reference_id":"19208630","statement":[{"text":"The NMR data clearly indicate that the fairly long N- and C-terminal regions (residues 1-55 and 145-189) of sclerostin are highly flexible and completely disordered (Fig. 2A).","type":"Results"},{"text":"The IDR characterized in the publication residues 145-189 corresponds to region 169-213 of the amino acid sequence.","type":"Curator statement"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-18T15:07:37.203Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":133,"region_id":"DP00926r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Characterization of the structural features and interactions of sclerostin: molecular insight into a key regulator of Wnt-mediated bone formation. <i> Veverka V, Henry AJ, Slocombe PM, Ventom A, Mulloy B, Muskett FW, Muzylak M, Greenslade K, Moore A, Zhang L, Gong J, Qian X, Paszty C, Taylor RJ, Robinson MK, Carr MD. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"esalladini","start":110,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2K8P"}],"reference_id":"19208630","statement":[{"text":"In common with the N- and C-terminal regions, loop 2 appears to be relatively flexible and adopts a diverse range of conformations within the family of converged structures.","type":"Results"},{"text":"The loop 2 corresponds to the region 110-133.","type":"Curator statement"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-18T15:17:48.958Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":133,"term_name":"molecular function inhibitor activity","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Characterization of the structural features and interactions of sclerostin: molecular insight into a key regulator of Wnt-mediated bone formation. <i> Veverka V, Henry AJ, Slocombe PM, Ventom A, Mulloy B, Muskett FW, Muzylak M, Greenslade K, Moore A, Zhang L, Gong J, Qian X, Paszty C, Taylor RJ, Robinson MK, Carr MD. </i> J Biol Chem, 2009","term_id":"GO:0140678","curator_id":"esalladini","start":110,"term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"19208630","version":4,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00926r004","statement":[{"text":"Identification of the Binding Site of an Antibody That Antagonizes the Inhibition of Wnt Signaling by Sclerostin","type":"Results"},{"text":"As described for heparin, the location of the inhibitory antibody binding site on sclerostin was mapped by following the changes in the positions of backbone amide NMR signals (15N and 1H) induced by the binding of the Fab fragment of the inhibitory antibody.","type":"Results"},{"text":"Examples of significantly affected amide signals of sclerostin are highlighted in the selected regions of 1H,15N HSQC spectra shown in Fig. 8A. The combined minimal shift values for the backbone amide signals versus protein sequence are shown in the histogram in Fig. 8B, which indicates that the majority of the perturbed residues are located within the flexible and solvent exposed loop 2 region of sclerostin (Fig. 8C).","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-21T15:32:49.744Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":110,"end":133,"reference_id":"19208630","reference_source":"pmid","reference_html":"Characterization of the structural features and interactions of sclerostin: molecular insight into a key regulator of Wnt-mediated bone formation. <i> Veverka V, Henry AJ, Slocombe PM, Ventom A, Mulloy B, Muskett FW, Muzylak M, Greenslade K, Moore A, Zhang L, Gong J, Qian X, Paszty C, Taylor RJ, Robinson MK, Carr MD. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0030246","term_name":"carbohydrate binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00926r006","statement":[{"text":"The predicted binding of heparin to sclerostin was confirmed by detecting changes in the positions of backbone amide NMR signals (15N and 1H) induced by binding of a dodecameric heparin fragment (Fig. 5A). The binding of the heparin fragment clearly results in very significant shifts in the positions of backbone amide signals from residues located mainly in loops 2 and 3, in particular, Glu-53, Ser-55, Arg-57, His-60, Ser-82, Gly-83, Leu-91, Trp-100, Trp-101, Arg-102, Ser-104, Asp-113, Arg-114, Tyr-115, Arg-116, Ala-117, Arg-119, Val-120, Gln-121, Leu-122, Leu-123, Glu-128, Ala-129, Arg-131, Ala-132, Val-135, Leu-137, Val-138, Cys-141, Lys-144, and Leu-146 (Fig. 5B).","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-22T07:09:04.636Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.\" [GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":115,"end":121,"reference_id":"21944579","reference_source":"pmid","reference_html":"Wnt antagonists bind through a short peptide to the first β-propeller domain of LRP5/6. <i> Bourhis E, Wang W, Tam C, Hwang J, Zhang Y, Spittler D, Huang OW, Gong Y, Estevez A, Zilberleyb I, Rouge L, Chiu C, Wu Y, Costa M, Hannoush RN, Franke Y, Cochran AG. </i> Structure, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"3SOV"}],"interaction_partner":[{"db":"UniProt","id":"O75581","partner_start":null,"partner_end":null}],"region_id":"DP00926r007","statement":[{"text":"To understand the interactions in detail, we determined high-resolution structures of DKK1 and SOST peptides in complex with LRP6 E1.","type":"Results"},{"text":"In the case of the SOST peptide, the Ile is followed by an intervening Gly before the basic Arg residue. This reorients the peptide backbone and places the Arg side chain in a more peripheral location on the acidic patch of LRP6 (Figure 4B).","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-21T13:05:05.457Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":115,"end":121,"reference_id":"21944579","reference_source":"pmid","reference_html":"Wnt antagonists bind through a short peptide to the first β-propeller domain of LRP5/6. <i> Bourhis E, Wang W, Tam C, Hwang J, Zhang Y, Spittler D, Huang OW, Gong Y, Estevez A, Zilberleyb I, Rouge L, Chiu C, Wu Y, Costa M, Hannoush RN, Franke Y, Cochran AG. </i> Structure, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"3SOV"}],"region_id":"DP00926r008","statement":[{"text":"To understand the interactions in detail, we determined high-resolution structures of DKK1 and SOST peptides in complex with LRP6 E1.","type":"Results"},{"text":"Taken together, the binding data and the effects on Wnt signaling confirm that the conserved “NXI” motif is functionally relevant for DKK1 and SOST inhibition of those Wnts signaling through binding to E1E2, and that the DKK1 CRD2 interaction with E3E4 is important only for inhibition of a different subset of Wnt ligands.","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-21T14:17:58.091Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":115,"end":121,"reference_id":"21944579","reference_source":"pmid","reference_html":"Wnt antagonists bind through a short peptide to the first β-propeller domain of LRP5/6. <i> Bourhis E, Wang W, Tam C, Hwang J, Zhang Y, Spittler D, Huang OW, Gong Y, Estevez A, Zilberleyb I, Rouge L, Chiu C, Wu Y, Costa M, Hannoush RN, Franke Y, Cochran AG. </i> Structure, 2011","date":"2022-03-09T08:07:03.730Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000353","ec_ontology":"ECO","ec_name":"physical interaction evidence used in manual assertion","released":"2022_03","version":4,"region_id":"DP00926r009","statement":[{"text":"For wild-type DKK1 and SOST, strong inhibition of WNT1-dependent signaling is observed.","type":"Results"},{"text":"Taken together, the binding data and the effects on Wnt signaling confirm that the conserved “NXI” motif is functionally relevant for DKK1 and SOST inhibition of those Wnts signaling through binding to E1E2, and that the DKK1 CRD2 interaction with E3E4 is important only for inhibition of a different subset of Wnt ligands.","type":"Results"},{"text":"The luciferase repoter assay was used to detect the interaction and DEXA scans measured the total bone marrow density.","type":"Curator statement"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"O75581","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T16:41:22.512Z"}},{"start":110,"end":133,"reference_id":"19208630","reference_source":"pmid","reference_html":"Characterization of the structural features and interactions of sclerostin: molecular insight into a key regulator of Wnt-mediated bone formation. <i> Veverka V, Henry AJ, Slocombe PM, Ventom A, Mulloy B, Muskett FW, Muzylak M, Greenslade K, Moore A, Zhang L, Gong J, Qian X, Paszty C, Taylor RJ, Robinson MK, Carr MD. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00926r012","statement":[{"text":"Heparin Mediates the Localization of Sclerostin at the Cell Surface","type":"Results"},{"text":" Additions of heparin to the cell culture for 3 h before the harvest of the supernatant resulted in a striking dose-dependent increase in the amount of sclerostin detected in the supernatant without affecting the total amount of sclerostin produced by the cells, as shown in Fig. 6A.","type":"Results"},{"text":"The experimental data reported here clearly indicates that the interaction between heparan sulfate and sclerostin will result in a significantly higher concentration of the protein at the surface of responsive cells, which may facilitate its regulation of the Wnt/β-catenin signaling pathway in a more spatially controlled and temporally dependent manner.","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-21T15:29:38.491Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2016_10","uniref100":"UniRef100_Q9BQB4","date":"2016-09-05T16:54:23.000Z","acc":"Q9BQB4","name":"Sclerostin","length":213,"organism":"Homo sapiens","dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000035BBE","genes":[{"name":{"value":"SOST","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:13771","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:13771"}}]},"orfNames":[{"value":"UNQ2976/PRO7455/PRO7476"}]}],"alphafold_very_low_content":0.03286384976525822,"disorder_content":0.5821596244131455,"disprot_consensus":{"full":[{"start":25,"end":79,"type":"D"},{"start":110,"end":133,"type":"D"},{"start":169,"end":213,"type":"D"}],"Structural state":[{"start":25,"end":79,"type":"D"},{"start":110,"end":133,"type":"D"},{"start":169,"end":213,"type":"D"}],"Molecular function":[{"start":110,"end":133,"type":"F"}],"Biological process":[{"start":110,"end":133,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00520","name":"Ion transport protein","start":12,"end":229}],"gene3D":[{"start":2,"end":115,"id":"1.20.120.350","name":"Voltage-gated potassium channels. Chain C"},{"start":127,"end":222,"id":"1.10.287.70","name":"1.10.287.70"}]},"uniref50":"UniRef50_A0A1Y2K2N9","sequence":"MSRKIRDLIESKRFQNVITAIIVLNGAVLGLLTDTTLSASSQNLLERVDQLCLTIFIVEISLKIYAYGVRGFFRSGWNLFDFVIVAIALMPAQGSLSVLRTFRIFRVMRLVSVIPTMRRVVQGMLLALPGVGSVAALLTVVFYIAAVMATNLYGATFPEWFGDLSKSLYTLFQVMTLESWSMGIVRPVMNVHPNAWVFFIPFIMLTTFTVLNLFIGIIVDAMAITKEQEEEAKTGHHQEPISQTLLHLGDRLDRIEKQLAQNNELLQRQQPQKK","taxonomy":["Bacteria","Proteobacteria","Alphaproteobacteria","Magnetococcales","Magnetococcaceae","Magnetococcus"],"uniref90":"UniRef90_A0L5S6","disprot_id":"DP00927","ncbi_taxon_id":156889,"regions_counter":1,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":239,"region_id":"DP00927r001","released":"2022_03","ec_id":"ECO:0006289","reference_html":"Role of the C-terminal domain in the structure and function of tetrameric sodium channels. <i> Bagnéris C, Decaen PG, Hall BA, Naylor CE, Clapham DE, Kay CW, Wallace BA. </i> Nat Commun, 2013","term_id":"IDPO:0000002","curator_id":"atantos","start":222,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24051986","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_A0L5S6","date":"2016-09-05T16:56:20.000Z","acc":"A0L5S6","name":"Ion transport protein","length":274,"organism":"Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1)","dataset":[],"UniParc":"UPI00003C5598","genes":[{"olnNames":[{"value":"Mmc1_0798","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ABK43319.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABK43319.1"}}]}]}],"alphafold_very_low_content":0.0036496350364963502,"disorder_content":0.06569343065693431,"disprot_consensus":{"full":[{"start":222,"end":239,"type":"D"}],"Structural state":[{"start":222,"end":239,"type":"D"}]}},{"features":{"pfam":[{"id":"PF07362","name":"Post-segregation antitoxin CcdA","start":2,"end":72}],"gene3D":[{"start":12,"end":41,"id":"1.10.1220.80","name":"1.10.1220.80"}]},"uniref50":"UniRef50_P62553","sequence":"MKQRITVTVDSDSYQLLKAYDVNISGLVSTTMQNEARRLRAERWKAENQEGMAEVARFIEMNGSFADENRDW","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P62553","disprot_id":"DP00928","dataset":["Unicellular toxins and antitoxins"],"ncbi_taxon_id":83333,"regions_counter":40,"creator":"ireményi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":72,"region_id":"DP00928r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Rejuvenation of CcdB-poisoned gyrase by an intrinsically disordered protein domain. <i> De Jonge N, Garcia-Pino A, Buts L, Haesaerts S, Charlier D, Zangger K, Wyns L, De Greve H, Loris R. </i> Mol Cell, 2009","statement":[{"text":"Far UV CD spectra of CcdA37-72 at 25 °C. The spectrum in blue is of unbound CcdA37-72 and has the typical shape of a random coil spectrum.","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":37,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":4,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T16:18:13.482Z","curator_name":"Bálint Mészáros"},"reference_id":"19647513","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":72,"term_name":"disorder to order","reference_html":"Rejuvenation of CcdB-poisoned gyrase by an intrinsically disordered protein domain. <i> De Jonge N, Garcia-Pino A, Buts L, Haesaerts S, Charlier D, Zangger K, Wyns L, De Greve H, Loris R. </i> Mol Cell, 2009","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":4,"term_id":"IDPO:0000011","curator_id":"rpancsa","start":37,"term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"19647513","statement":[{"text":"Far UV CD spectra of CcdA37-72 at 25 °C. The spectrum in blue is of unbound CcdA37-72 and has the typical shape of a random coil spectrum. The spectrum in green is the difference spectrum  between  the  CcdB2:CcdA37-72  complex  and  CcdB2,  thus  corresponding  to  that  of  CcdA37-72 in its bound state. Here the typical spectral shape corresponding to α-helix is clearly visible.","type":"Supplementary material"},{"text":"Upon  addition  of  CcdA37-72 to  CcdB2,  the  CD  spectrum  of  CcdA37-72  undergoes  significant  changes.  Figure  S1A  compares  the  far  UV  CD  spectrum  of  CcdA37-72  in  its  free  state  and  in  complex  with  a  CcdB  dimer  (CcdB2:CcdA37-72  ratio  1:1).  The  latter  indicates  that  upon  complex formation CcdA37-72 folds to a largely α-helical conformation, in agreement with our crystallographic studies.","type":"Supplementary material"}],"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T16:30:10.144Z","curator_name":"Bálint Mészáros"},"released":"2022_03","region_id":"DP00928r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00928r003","validated":{"curator_id":"bmesza","timestamp":"2020-12-16T11:00:26.283Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":72,"ec_name":"far-UV circular dichroism evidence used in manual assertion","start":37,"version":5,"statement":[{"text":"Upon addition of CcdA37-72 to CcdB2, the CD spectrum of CcdA37-72 undergoes significant changes. Figure S1A compares the far UV CD spectrum of CcdA37-72 in its free state and in complex with a CcdB dimer (CcdB2:CcdA37-72 ratio 1:1).","type":"Supplementary material"},{"text":"Binding studies using ITC, SPR, CD-, and fluorescence spectroscopy consistently yield a picture of the CcdB2 dimer possessing two binding sites for CcdA37-72, differing in affinity by a factor of at least 106 (Figure 2 and Figure S4). ","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P62554","partner_end":null}],"term_name":"protein binding","reference_html":"Rejuvenation of CcdB-poisoned gyrase by an intrinsically disordered protein domain. <i> De Jonge N, Garcia-Pino A, Buts L, Haesaerts S, Charlier D, Zangger K, Wyns L, De Greve H, Loris R. </i> Mol Cell, 2009","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"19647513","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006204","curator_id":"rpancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":72,"region_id":"DP00928r004","reference_html":"Rejuvenation of CcdB-poisoned gyrase by an intrinsically disordered protein domain. <i> De Jonge N, Garcia-Pino A, Buts L, Haesaerts S, Charlier D, Zangger K, Wyns L, De Greve H, Loris R. </i> Mol Cell, 2009","ec_id":"ECO:0006165","version":4,"term_id":"IDPO:0000002","curator_id":"rpancsa","start":37,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"The  fingerprint  region  of  the  TOCSY  spectrum  of  CcdA37-72  shows  poor  chemical  shift  dispersion.   They   all   fall   in   the   range   between   7.8-8.6   ppm,   typical   for   random   coil   conformations","type":"Supplementary material"}],"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T16:25:20.338Z","curator_name":"Bálint Mészáros"},"released":"2022_03","reference_id":"19647513","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":72,"region_id":"DP00928r005","released":"2022_03","ec_id":"ECO:0006206","reference_html":"Rejuvenation of CcdB-poisoned gyrase by an intrinsically disordered protein domain. <i> De Jonge N, Garcia-Pino A, Buts L, Haesaerts S, Charlier D, Zangger K, Wyns L, De Greve H, Loris R. </i> Mol Cell, 2009","statement":[{"text":"The near UV CD spectrum of CcdA37-72 lacks sharp peaks, which is an indication of disorder.","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":37,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"near-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T16:18:17.259Z","curator_name":"Bálint Mészáros"},"reference_id":"19647513","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":72,"region_id":"DP00928r008","released":"2022_03","ec_id":"ECO:0001249","reference_html":"Rejuvenation of CcdB-poisoned gyrase by an intrinsically disordered protein domain. <i> De Jonge N, Garcia-Pino A, Buts L, Haesaerts S, Charlier D, Zangger K, Wyns L, De Greve H, Loris R. </i> Mol Cell, 2009","statement":[{"text":"Fluorescence spectroscopy measurements of CcdA37-72 show a monotonic increase upon chemical unfolding with guanidinium chloride and the absence of a discrete folding/unfolding transition.","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":37,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"fluorescence evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"bmesza","timestamp":"2020-12-16T10:59:57.867Z","curator_name":"Bálint Mészáros"},"reference_id":"19647513","ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP00928r015","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T16:57:00.275Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":72,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":41,"version":3,"statement":[{"text":"Sequential backbone and side-chain assignments localized the well-dispersed signals to residues 3–40. Values closer to random coil shifts were\nobserved for the C-terminal 30 residues, together\nwith three different conformations (labeled “a”, “b” and “c” in Figure 1(b) and (c)). These provide evidence that CcdA consists of two domains, a structured N terminus (CcdAN; Gln3–Arg40) and a much more flexible C terminus (CcdAC; Ala41– Trp72) which adopts different, partially stable conformations.","type":"Results"},{"text":"The CcdA R70K mutant was used in the NMR measurement that showed increased stability against proteolytic cleavage.","type":"Curator statement"}],"term_name":"disorder","reference_html":"Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA. <i> Madl T, Van Melderen L, Mine N, Respondek M, Oberer M, Keller W, Khatai L, Zangger K. </i> J Mol Biol, 2006","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"17007877","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2ADL"},{"db":"PDB","id":"2H3A"},{"db":"PDB","id":"2H3C"},{"db":"PDB","id":"2ADN"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"rpancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":72,"region_id":"DP00928r019","released":"2022_03","ec_id":"ECO:0006204","reference_html":"ATP-dependent degradation of CcdA by Lon protease. Effects of secondary structure and heterologous subunit interactions. <i> Van Melderen L, Thi MH, Lecchi P, Gottesman S, Couturier M, Maurizi MR. </i> J Biol Chem, 1996","statement":[{"text":"Purified CcdA41, however, contained almost no α-helical or β-sheet structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":32,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T17:19:43.127Z","curator_name":"Bálint Mészáros"},"reference_id":"8910366","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":72,"region_id":"DP00928r022","released":"2022_03","ec_id":"ECO:0001249","reference_html":"ATP-dependent degradation of CcdA by Lon protease. Effects of secondary structure and heterologous subunit interactions. <i> Van Melderen L, Thi MH, Lecchi P, Gottesman S, Couturier M, Maurizi MR. </i> J Biol Chem, 1996","statement":[{"text":"The intrinsic fluorescence of CcdA had an emission maximum at 346 nm, suggesting that both tryptophan residues are highly solvent-exposed (Fig. 8). ","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":32,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"fluorescence evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T17:19:45.114Z","curator_name":"Bálint Mészáros"},"reference_id":"8910366","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":72,"term_name":"disorder to order","released":"2022_03","ec_name":"fluorescence evidence used in manual assertion","reference_html":"ATP-dependent degradation of CcdA by Lon protease. Effects of secondary structure and heterologous subunit interactions. <i> Van Melderen L, Thi MH, Lecchi P, Gottesman S, Couturier M, Maurizi MR. </i> J Biol Chem, 1996","statement":[{"text":"Changes in CcdA fluorescence also suggest a conformational change in CcdA upon binding CcdB. The intrinsic fluorescence of CcdA41 was similar to that of CcdA and was blue-shifted to a similar extent upon binding of CcdB. The intrinsic fluorescence of CcdA had an emission maximum at 346 nm, suggesting that both tryptophan residues are highly solvent-exposed (Fig. 8). Addition of CcdB results in a dramatic blue shift in the fluorescence emission which had a maximum near 330 nm (Fig. 8), indicating that both tryptophan residues are buried in the complex. The intrinsic fluorescence of CcdA41 was similar to that of CcdA and was blue-shifted to a similar extent upon binding of CcdB (data not shown). Burial of the tryptophan residues could indicate that those residues form part of the bonding domain between CcdA and CcdB or that CcdB binding induces a conformational change in CcdA that moves the tryptophan residues away from the solvent into closer contact with other residues in the terminal a-helix.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"rpancsa","start":32,"term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"8910366","version":3,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001249","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T17:20:27.567Z","curator_name":"Bálint Mészáros"},"region_id":"DP00928r023","ec_go":"IDA","disprot_namespace":"Structural transition"},{"region_id":"DP00928r024","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T16:31:33.067Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":72,"term_id":"IDPO:0000011","start":41,"version":2,"statement":[{"text":"In solution, CcdA37-72 behaves as a monomeric and intrinsically disordered protein and folds upon binding to CcdB. Electron density is observed for residues Ala41-Trp72, while residues Arg37-Arg40 remain disordered. Segment Arg40-Gly63 forms a long bent α-helix. Segment Ser64-Trp72, on the other hand, has a more irregular structure harboring just a single helical turn at its center.","type":"Results"}],"term_name":"disorder to order","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"19647513","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3G7Z"},{"db":"PDB","id":"3HPW"}],"term_namespace":"Structural transition","ec_id":"ECO:0005670","curator_id":"rpancsa","reference_html":"Rejuvenation of CcdB-poisoned gyrase by an intrinsically disordered protein domain. <i> De Jonge N, Garcia-Pino A, Buts L, Haesaerts S, Charlier D, Zangger K, Wyns L, De Greve H, Loris R. </i> Mol Cell, 2009","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00928r025","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T16:33:53.452Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":72,"term_id":"GO:0005515","start":37,"version":3,"statement":[{"text":"The crystal structure of the CcdB2:CcdA37-72 complex is asymmetric with a single CcdA37-72 domain wrapped around the CcdB2 dimer in a largely α-helical conformation, burying a total combined molecular surface of 2850 Å2 for CcdA37-72 and CcdB2.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P62554","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"19647513","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3G7Z"},{"db":"PDB","id":"3HPW"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"rpancsa","reference_html":"Rejuvenation of CcdB-poisoned gyrase by an intrinsically disordered protein domain. <i> De Jonge N, Garcia-Pino A, Buts L, Haesaerts S, Charlier D, Zangger K, Wyns L, De Greve H, Loris R. </i> Mol Cell, 2009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00928r026","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T16:38:52.776Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":72,"term_id":"GO:0097351","start":37,"version":3,"statement":[{"text":"We found that coexpression with CcdA37-72 is sufficient to protect E. coli cells from CcdB. The\ngrowth of cells cotransformed with plasmids coding for CcdB and CcdA37-72 (efficiency of plating [EOP] = 0.9 ± 0.2) is similar to the growth of cells transformed with plasmids coding for\nCcdB and full-length CcdA (EOP = 0.8 ± 0.3). Cells transformed with a plasmid coding only for CcdB produce very few colonies (EOP = 0.002 ± 0.002). ","type":"Results"}],"term_name":"toxin sequestering activity","ec_name":"experimental phenotypic evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"19647513","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0007634","curator_id":"rpancsa","reference_html":"Rejuvenation of CcdB-poisoned gyrase by an intrinsically disordered protein domain. <i> De Jonge N, Garcia-Pino A, Buts L, Haesaerts S, Charlier D, Zangger K, Wyns L, De Greve H, Loris R. </i> Mol Cell, 2009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a toxic protein, disabling its function. There may be more than one antitoxin to a toxic protein. Instances of this activity are known only in prokaryotes, where the toxic protein may be a ribonuclease, a DNA gyrase, or other.\" [GOC:rs, PMID:19143615, PMID:19325885, PMID:21819231, PMID:22545240, PMID:24806488, Wikipedia:Toxin-antitoxin_system#Type_II]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00928r027","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T16:34:19.897Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":72,"term_id":"GO:0005515","start":37,"version":3,"statement":[{"text":"Binding studies using ITC, SPR, CD-, and fluorescence spectroscopy consistently yield a picture of the CcdB2 dimer possessing two binding sites for CcdA37-72, differing in affinity by a factor of at least 106 (Figure 2 and Figure S4). ","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P62554","partner_end":null}],"term_name":"protein binding","ec_name":"isothermal titration calorimetry evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"19647513","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"rpancsa","reference_html":"Rejuvenation of CcdB-poisoned gyrase by an intrinsically disordered protein domain. <i> De Jonge N, Garcia-Pino A, Buts L, Haesaerts S, Charlier D, Zangger K, Wyns L, De Greve H, Loris R. </i> Mol Cell, 2009","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00928r028","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T16:34:21.054Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":72,"term_id":"GO:0005515","start":37,"version":3,"statement":[{"text":"Binding studies using ITC, SPR, CD-, and fluorescence spectroscopy consistently yield a picture of the CcdB2 dimer possessing two binding sites for CcdA37-72, differing in affinity by a factor of at least 106 (Figure 2 and Figure S4). ","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P62554","partner_end":null}],"term_name":"protein binding","ec_name":"surface plasmon resonance evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"19647513","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001269","curator_id":"rpancsa","reference_html":"Rejuvenation of CcdB-poisoned gyrase by an intrinsically disordered protein domain. <i> De Jonge N, Garcia-Pino A, Buts L, Haesaerts S, Charlier D, Zangger K, Wyns L, De Greve H, Loris R. </i> Mol Cell, 2009","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00928r029","validated":{"curator_id":"bmesza","timestamp":"2020-12-16T11:17:05.866Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":72,"term_id":"GO:0005515","start":37,"version":3,"statement":[{"text":"Binding studies using ITC, SPR, CD-, and fluorescence spectroscopy consistently yield a picture of the CcdB2 dimer possessing two binding sites for CcdA37-72, differing in affinity by a factor of at least 106 (Figure 2 and Figure S4). ","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P62554","partner_end":null}],"term_name":"protein binding","ec_name":"fluorescence evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"19647513","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001249","curator_id":"rpancsa","reference_html":"Rejuvenation of CcdB-poisoned gyrase by an intrinsically disordered protein domain. <i> De Jonge N, Garcia-Pino A, Buts L, Haesaerts S, Charlier D, Zangger K, Wyns L, De Greve H, Loris R. </i> Mol Cell, 2009","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00928r030","ec_ontology":"ECO","end":72,"term_id":"GO:0032984","start":37,"version":4,"statement":[{"text":"In order to determine how many molar equivalents of CcdA37-72 are required to disrupt the GyrA592:CcdB2 complex, we performed a series of analytical gel filtration experiments where GyrA592:CcdB2 was preincubated with different molar equivalents of CcdA37-72. Adding a single equivalent of monomeric CcdA37-72 to GyrA592:CcdB2 fully dissociated this complex, producing GyrA592 and CcdB2:CcdA37-72 (Figure 3C), confirming the functional relevance of our crystal structure. This result directly links the high-affinity interaction between CcdB and CcdA37-72 to the rejuvenation process.","type":"Results"}],"term_name":"protein-containing complex disassembly","ec_name":"gel-filtration evidence used in manual assertion","curator_orcid":"0000-0002-5152-5953","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"19647513","date":"2022-03-09T08:08:22.522Z","reference_source":"pmid","term_namespace":"Biological process","ec_id":"ECO:0001184","curator_id":"esalladini","reference_html":"Rejuvenation of CcdB-poisoned gyrase by an intrinsically disordered protein domain. <i> De Jonge N, Garcia-Pino A, Buts L, Haesaerts S, Charlier D, Zangger K, Wyns L, De Greve H, Loris R. </i> Mol Cell, 2009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The disaggregation of a protein-containing macromolecular complex into its constituent components.\" [GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T12:04:34.802Z"}},{"region_id":"DP00928r031","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T17:13:14.104Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":71,"term_id":"GO:0005515","start":46,"version":3,"statement":[{"text":"To map the regions of CcdA involved in the binding to the toxin CcdB a titration of unlabeled CcdB with increasing amounts of uniformly 13C/15N labeled CcdA was carried out. Significant chemical shift changes were observed for NH resonances of residues located within the C-terminal region of CcdA only (residues between Val46 and Asp71) and addition of CcdB had no effect on the N-terminal domain (Figure 4(a)). ","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P62554","partner_end":null}],"term_name":"protein binding","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"17007877","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"rpancsa","reference_html":"Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA. <i> Madl T, Van Melderen L, Mine N, Respondek M, Oberer M, Keller W, Khatai L, Zangger K. </i> J Mol Biol, 2006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00928r032","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T17:12:17.993Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":72,"term_id":"IDPO:0000011","start":46,"version":2,"statement":[{"text":"The residues located in CcdAC (green peaks; labels written in circles) were unaffected by residual proteases in the CcdB solution which successively digested CcdAN.","type":"Results"},{"text":"We observed that upon binding to CcdB, CcdAC becomes structured and that residues 46 to 72 are shielded in the complex.","type":"Discussion"}],"term_name":"disorder to order","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"17007877","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural transition","ec_id":"ECO:0006165","curator_id":"rpancsa","reference_html":"Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA. <i> Madl T, Van Melderen L, Mine N, Respondek M, Oberer M, Keller W, Khatai L, Zangger K. </i> J Mol Biol, 2006","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP00928r033","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T17:22:35.567Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":72,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"Complex of CcdA and CcdB—CcdA and CcdB interact to form a stable complex that can be isolated by gel filtration (Fig. 1A) or native gel electrophoresis (Fig. 2, A and C).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P62554","partner_end":null}],"term_name":"protein binding","ec_name":"native protein gel electrophoresis evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"8910366","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006305","curator_id":"rpancsa","reference_html":"ATP-dependent degradation of CcdA by Lon protease. Effects of secondary structure and heterologous subunit interactions. <i> Van Melderen L, Thi MH, Lecchi P, Gottesman S, Couturier M, Maurizi MR. </i> J Biol Chem, 1996","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00928r034","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T17:22:36.481Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":72,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"Complex of CcdA and CcdB—CcdA and CcdB interact to form a stable complex that can be isolated by gel filtration (Fig. 1A) or native gel electrophoresis (Fig. 2, A and C).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P62554","partner_end":null}],"term_name":"protein binding","ec_name":"chromatography evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"8910366","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0007680","curator_id":"rpancsa","reference_html":"ATP-dependent degradation of CcdA by Lon protease. Effects of secondary structure and heterologous subunit interactions. <i> Van Melderen L, Thi MH, Lecchi P, Gottesman S, Couturier M, Maurizi MR. </i> J Biol Chem, 1996","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP00928r035","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T17:19:46.324Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":72,"term_id":"IDPO:0000002","start":32,"version":2,"statement":[{"text":"CcdA41 was also degraded by Lon, but in this case similar degradation rates were observed with either ATP or AMPPNP.","type":"Results"},{"text":"While full length CcdA could only be degraded by Lon in the presence of ATP, CcdA41 was degraded by Lon independent of the presence of ATP.  This suggests that while full length CcdA has considerable amount of secondary structure, the C-terminal region (CcdA41) has not.","type":"Curator statement"}],"term_name":"disorder","ec_name":"cleavage assay evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"8910366","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0007691","curator_id":"rpancsa","reference_html":"ATP-dependent degradation of CcdA by Lon protease. Effects of secondary structure and heterologous subunit interactions. <i> Van Melderen L, Thi MH, Lecchi P, Gottesman S, Couturier M, Maurizi MR. </i> J Biol Chem, 1996","ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP00928r036","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T17:20:47.844Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":72,"term_id":"IDPO:0000011","start":32,"version":2,"statement":[{"text":"CcdB blocked activation of Lon ATPase activity by CcdA (Table IV), which suggests that CcdA can not interact with Lon when CcdA and CcdB are in a complex. Thus, CcdB protects CcdA probably by masking or making inaccessible those regions of CcdA normally recognized by Lon. CcdB also partially protects CcdA from degradation by proteases such as LysC and V8 protease.","type":"Results"}],"term_name":"disorder to order","ec_name":"cleavage assay evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"8910366","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural transition","ec_id":"ECO:0007691","curator_id":"rpancsa","reference_html":"ATP-dependent degradation of CcdA by Lon protease. Effects of secondary structure and heterologous subunit interactions. <i> Van Melderen L, Thi MH, Lecchi P, Gottesman S, Couturier M, Maurizi MR. </i> J Biol Chem, 1996","ec_go":"IDA","disprot_namespace":"Structural transition"},{"region_id":"DP00928r038","validated":{"curator_id":"bmesza","timestamp":"2020-12-16T11:17:09.803Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":72,"term_id":"GO:0005515","start":41,"version":3,"statement":[{"text":"Traces of proteases remaining in the CcdB solution digested CcdAN while CcdAC was protected against proteolysis even after weeks at room temperature.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P62554","partner_end":null}],"term_name":"protein binding","ec_name":"cleavage assay evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"17007877","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0007691","curator_id":"rpancsa","reference_html":"Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA. <i> Madl T, Van Melderen L, Mine N, Respondek M, Oberer M, Keller W, Khatai L, Zangger K. </i> J Mol Biol, 2006","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P62553","date":"2016-09-05T17:01:03.000Z","acc":"P62552","name":"Antitoxin CcdA","length":72,"organism":"Escherichia coli (strain K12)","UniParc":"UPI00001272A3","genes":[{"name":{"value":"ccdA"},"synonyms":[{"value":"H"},{"value":"letA"}],"olnNames":[{"value":"ECOK12F042"}]}],"alphafold_very_low_content":0.013888888888888888,"disorder_content":0.5694444444444444,"disprot_consensus":{"full":[{"start":1,"end":31,"type":"F"},{"start":32,"end":72,"type":"T"}],"Structural state":[{"start":32,"end":72,"type":"D"}],"Structural transition":[{"start":32,"end":72,"type":"T"}],"Molecular function":[{"start":1,"end":72,"type":"F"}],"Biological process":[{"start":37,"end":72,"type":"F"}]}},{"acc":"P04608","sequence":"MEPVDPRLEPWKHPGSQPKTACTNCYCKKCCFHCQVCFITKALGISYGRKKRRQRRRAHQNSQTHQASLSKQPTSQPRGDPTGPKE","creator":"zdosztanyi","dataset":["Viral proteins","RNA-binding proteins"],"date":"2016-09-05T17:14:04.000Z","disprot_id":"DP00929","features":{"pfam":[{"id":"PF00539","name":"Transactivating regulatory protein (Tat)","start":2,"end":64}],"gene3D":[{"start":1,"end":86,"id":"4.10.20.10","name":"Tat domain","_id":"685af523b4ac24d5329d875e"}]},"genes":[{"name":{"value":"tat","evidences":[{"source":{"id":"MF_04079","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04079","_id":"685af523b4ac24d5329d884f"},"code":"ECO:0000255","_id":"685af523b4ac24d5329d884e"}],"_id":"685af523b4ac24d5329d8850"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d884d"}],"length":86,"name":"Protein Tat","ncbi_taxon_id":11706,"organism":"Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)","regions_counter":46,"released":"2016_10","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"UniParc":"UPI000059C369","uniref100":"UniRef100_P04608","uniref50":"UniRef50_P04608","uniref90":"UniRef90_P04608","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3MI9","_id":"685af523b4ac24d5329d877e"},{"db":"PDB","id":"3MIA","_id":"685af523b4ac24d5329d877f"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":50,"end":86,"interaction_partner":[],"reference_html":"Crystal structure of HIV-1 Tat complexed with human P-TEFb. <i> Tahirov TH, Babayeva ND, Varzavand K, Cooper JJ, Sedore SC, Price DH. </i> Nature, 2010","reference_id":"20535204","region_id":"DP00929r012","released":"2022_03","sample":[],"statement":[{"type":"Methods","text":"Density was not observed for the amino acid residues 1-7, 89-96, 345 and the C-terminal His-tag of Cdk9, for the residues 1-6, 253-260 and 262-266 of Cyclin T1, and for the residues 50-86 of Tat.","_id":"685af523b4ac24d5329d877d"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-04T11:34:45.026Z","_id":"685af523b4ac24d5329d8780"},"version":3,"_id":"685af523b4ac24d5329d877c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3MI9","_id":"685af523b4ac24d5329d879f"},{"db":"PDB","id":"3MIA","_id":"685af523b4ac24d5329d87a0"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":49,"interaction_partner":[],"reference_html":"Crystal structure of HIV-1 Tat complexed with human P-TEFb. <i> Tahirov TH, Babayeva ND, Varzavand K, Cooper JJ, Sedore SC, Price DH. </i> Nature, 2010","reference_id":"20535204","region_id":"DP00929r020","released":"2022_03","sample":[{"db":"UniProt","deviation":null,"id":"P50750","statements":[{"type":"Methods","text":"C-terminally His tagged human Cdk9 (1-345), human Cyclin T1 (1-266), and HIV-1 Tat (1-86) were co-expressed in insect cells and purified by Ni-NTA and Mono S columns. The purified Tat•P-TEFb complex was crystallized using the sitting-drop vapor-diffusion method.","_id":"685af523b4ac24d5329d87a4"}],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d87a3"},{"db":"UniProt","deviation":null,"id":"O60563","statements":[{"type":"Methods","text":"C-terminally His tagged human Cdk9 (1-345), human Cyclin T1 (1-266), and HIV-1 Tat (1-86) were co-expressed in insect cells and purified by Ni-NTA and Mono S columns. The purified Tat•P-TEFb complex was crystallized using the sitting-drop vapor-diffusion method.","_id":"685af523b4ac24d5329d87a6"}],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d87a5"}],"statement":[{"type":"Results","text":"Indeed, the residues 1-49 are ordered in the crystal structure of Tat•P-TEFb, while the density for the rest of Tat (residues 50-86) is not defined.","_id":"685af523b4ac24d5329d87a1"},{"type":"Curator statement","text":"This region is ordered when bound to the positive transcription elongation factor, P-TEFb.","_id":"685af523b4ac24d5329d87a2"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T12:22:45.991Z","_id":"685af523b4ac24d5329d87a7"},"version":1,"_id":"685af523b4ac24d5329d879e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3MI9","_id":"685af523b4ac24d5329d87a9"},{"db":"PDB","id":"3MIA","_id":"685af523b4ac24d5329d87aa"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":49,"interaction_partner":[],"reference_html":"Crystal structure of HIV-1 Tat complexed with human P-TEFb. <i> Tahirov TH, Babayeva ND, Varzavand K, Cooper JJ, Sedore SC, Price DH. </i> Nature, 2010","reference_id":"20535204","region_id":"DP00929r021","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Indeed, the residues 1-49 are ordered in the crystal structure of Tat•P-TEFb, while the density for the rest of Tat (residues 50-86) is not defined.","_id":"685af523b4ac24d5329d87ab"},{"type":"Curator statement","text":"This region is ordered when bound to the positive transcription elongation factor, P-TEFb.","_id":"685af523b4ac24d5329d87ac"}],"states_connection":[{"source":"DP00929r025","target":"DP00929r020","_id":"685af523b4ac24d5329d87ad"}],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T12:22:54.918Z","_id":"685af523b4ac24d5329d87ae"},"version":1,"_id":"685af523b4ac24d5329d87a8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3MI9","_id":"685af523b4ac24d5329d87b0"},{"db":"PDB","id":"3MIA","_id":"685af523b4ac24d5329d87b1"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":49,"interaction_partner":[{"db":"UniProt","id":"O60563","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d87b2"},{"db":"UniProt","id":"P50750","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d87b3"}],"reference_html":"Crystal structure of HIV-1 Tat complexed with human P-TEFb. <i> Tahirov TH, Babayeva ND, Varzavand K, Cooper JJ, Sedore SC, Price DH. </i> Nature, 2010","reference_id":"20535204","region_id":"DP00929r022","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Indeed, the residues 1-49 are ordered in the crystal structure of Tat•P-TEFb, while the density for the rest of Tat (residues 50-86) is not defined.","_id":"685af523b4ac24d5329d87b4"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-04T11:34:54.172Z","_id":"685af523b4ac24d5329d87b5"},"version":1,"_id":"685af523b4ac24d5329d87af","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3MI9","_id":"685af523b4ac24d5329d87b7"},{"db":"PDB","id":"3MIA","_id":"685af523b4ac24d5329d87b8"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":49,"interaction_partner":[],"reference_html":"Crystal structure of HIV-1 Tat complexed with human P-TEFb. <i> Tahirov TH, Babayeva ND, Varzavand K, Cooper JJ, Sedore SC, Price DH. </i> Nature, 2010","reference_id":"20535204","region_id":"DP00929r023","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Indeed, the residues 1-49 are ordered in the crystal structure of Tat•P-TEFb, while the density for the rest of Tat (residues 50-86) is not defined.","_id":"685af523b4ac24d5329d87b9"}],"states_connection":[],"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","term_go_domain":"F","term_id":"GO:0140313","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular sequestering activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-04T11:34:58.743Z","_id":"685af523b4ac24d5329d87ba"},"version":1,"_id":"685af523b4ac24d5329d87b6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"DisProt","id":"DP03535","_id":"685af523b4ac24d5329d87bc"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IC","ec_id":"ECO:0007759","ec_name":"curator inference from database used in manual assertion","ec_ontology":"ECO","start":1,"end":57,"interaction_partner":[],"reference_html":"Conformational diversity in the intrinsically disordered HIV-1 Tat protein induced by zinc and pH. Kunihara T, Hayashi Y, Arai M. Biochem Biophys Res Commun, 2019","reference_id":"30600181","region_id":"DP00929r024","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"This region is 100% identical to that of Human immunodeficiency virus type 1 group M subtype B (isolate BH10) Tat protein, proved to be disordered.","_id":"685af523b4ac24d5329d87bd"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:58:19.774Z","_id":"685af523b4ac24d5329d87be"},"version":1,"_id":"685af523b4ac24d5329d87bb","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_id":"ECO:0000302","ec_name":"author statement used in manual assertion","ec_ontology":"ECO","start":1,"end":86,"interaction_partner":[],"reference_html":"Crystal structure of HIV-1 Tat complexed with human P-TEFb. <i> Tahirov TH, Babayeva ND, Varzavand K, Cooper JJ, Sedore SC, Price DH. </i> Nature, 2010","reference_id":"20535204","region_id":"DP00929r025","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"In the absence of interacting partners, Tat does not have prominent secondary structure elements, indicating the flexible nature of free Tat proteins.","_id":"685af523b4ac24d5329d87c0"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:58:15.203Z","_id":"685af523b4ac24d5329d87c1"},"version":1,"_id":"685af523b4ac24d5329d87bf","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_id":"ECO:0000302","ec_name":"author statement used in manual assertion","ec_ontology":"ECO","start":62,"end":68,"interaction_partner":[],"reference_html":"The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR. <i> Brand SR, Kobayashi R, Mathews MB. </i> J Biol Chem, 1997","reference_id":"9079663","region_id":"DP00929r026","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"The same material was subjected to sequential Edman degradation, and the release of radioactive derivatives was monitored. Peaks of radioactivity were observed at cycles 6, 8, and 12, indicative of phosphorylation sites at these distances following an arginine or lysine residue. The only place that such a pattern occurs in the Tat-72 molecule is at serine 62, threonine 64, and serine 68 (Fig. 5C).","_id":"685af523b4ac24d5329d87c3"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T12:24:21.727Z","_id":"685af523b4ac24d5329d87c4"},"version":1,"_id":"685af523b4ac24d5329d87c2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006076","ec_name":"protein binding evidence used in manual assertion","ec_ontology":"ECO","start":49,"end":72,"interaction_partner":[{"db":"UniProt","id":"P19525","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d87c6"}],"reference_html":"The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR. <i> Brand SR, Kobayashi R, Mathews MB. </i> J Biol Chem, 1997","reference_id":"9079663","region_id":"DP00929r027","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"GST-Tat 86, GST-Tat 72, and their mutant variants, p18IS and C22G, all bound PKR, whereas the 48Δ Tat truncation and its associated mutants failed to bind PKR. In addition the Tat construct Tat 86Δ2/36, an N-terminal deletion of residues 2-36 from GST-Tat 86, successfully bound activated PKR. These data suggest that the Tat sequence contained between amino acids 49 and 72 is important for binding PKR, but the N-terminal and C-terminal residues 2-36 and 73-86 are dispensable.","_id":"685af523b4ac24d5329d87c7"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T12:23:08.016Z","_id":"685af523b4ac24d5329d87c8"},"version":1,"_id":"685af523b4ac24d5329d87c5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0001202","ec_name":"in vitro protein kinase assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":72,"interaction_partner":[],"reference_html":"The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR. <i> Brand SR, Kobayashi R, Mathews MB. </i> J Biol Chem, 1997","reference_id":"9079663","region_id":"DP00929r028","released":"2022_03","sample":[{"db":"UniProt","deviation":null,"id":"P19525","statements":[{"type":"Methods","text":"Substrate competition assays containing eIF2 and Tat-72 were carried out by mixing 50 ng of purified eIF2 (a gift from J. Hershey) with increasing concentrations of purified Tat-72 (up to 500 ng). Concurrently, 50 ng of purified Tat was mixed with increasing concentrations of purified eIF2 (up to 500 ng). To each reaction 10 μl volumes from an kinase assay containing activated PKR was added.","_id":"685af523b4ac24d5329d87cb"}],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d87ca"},{"db":"UniProt","deviation":null,"id":"P05198","statements":[],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d87cc"}],"statement":[{"type":"Results","text":"Conversely, increasing the concentration of Tat protein, while maintaining a fixed concentration of eIF2, resulted in a marked reduction in eIF2 phosphorylation (lanes 5-8). These data suggest that Tat and eIF2 can compete as substrates for phosphorylation by autophosphorylated PKR. Considering the relative molecular masses of Tat and eIF2 (about 10 and 125 kDa, respectively), they appear to serve as substrates for PKR and as competitors on a comparable molar basis.","_id":"685af523b4ac24d5329d87cd"},{"type":"Curator statement","text":"Activation of PKR by dsRNA is accompanied by autophosphorylation. When activated PKR catalyzes the phosphorylation of the α subunit of eukaryotic initiation factor 2 (eIF2), which results in the sequestration of a second initiation factor, the guanosine nucleotide exchange factor eIF2B, leading to the inhibition of protein synthesis. This mode of translational shut down constitutes a host defense mechanism and, as such, is detrimental to the viral life cycle. The avoidance of the activation of PKR and/or eIF2 proteins serves as a viral strategy to circumvent this host response. ","_id":"685af523b4ac24d5329d87ce"}],"states_connection":[],"term_comment":"","term_def":"\"A process by which an organism avoids the effects of the host organism's immune response. The host is defined as the larger of the organisms involved in a symbiotic interaction.\" [GOC:mb, PMID:12439615]","term_go_domain":"P","term_id":"GO:0042783","term_is_binding":false,"term_is_obsolete":false,"term_name":"evasion of host immune response","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T12:24:18.673Z","_id":"685af523b4ac24d5329d87cf"},"version":1,"_id":"685af523b4ac24d5329d87c9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0001202","ec_name":"in vitro protein kinase assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":72,"interaction_partner":[],"reference_html":"The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR. <i> Brand SR, Kobayashi R, Mathews MB. </i> J Biol Chem, 1997","reference_id":"9079663","region_id":"DP00929r029","released":"2022_03","sample":[{"db":"UniProt","deviation":null,"id":"P19525","statements":[{"type":"Methods","text":"Reactions (20 μl) containing 2.5 μCi of [γ-32P]ATP (ICN Biomedical Inc., Costa Mesa, CA) and 0.5 μl of PKR (approximately 5 ng) purified to the mono-S stage (46) were conducted as described previously (47) in the presence of dsRNA derived from reovirus (a gift from A. Shatkin). Kinase reactions (20 μl total volume) containing PKC (10 ng) were carried out as described by the manufacturer (Upstate Biotechnology Inc., Lake Placid, NY).","_id":"685af523b4ac24d5329d87d2"}],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d87d1"},{"db":null,"deviation":null,"id":null,"statements":[],"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_id":"UO:0000023","unit_name":"µg","value":null,"_id":"685af523b4ac24d5329d87d3"}],"statement":[{"type":"Results","text":"In the absence of Tat, PKR was autophosphorylated in a dsRNA-dependent fashion (lanes 1 and 2). Preincubation of PKR with increasing concentrations of purified Tat-72 prior to the addition of dsRNA eliminated PKR autophosphorylation (lanes 3 and 4). As in previous experiments (Figs. 2, 3, 4, 5), when the addition of Tat was delayed until after PKR activation by dsRNA had occurred, both Tat and PKR were phosphorylated (lane 5). These observations indicate that Tat-72 can inhibit the activation of PKR by dsRNA in vitro, as well as its activity in phosphorylating eIF2.","_id":"685af523b4ac24d5329d87d4"},{"type":"Curator statement","text":"Activation of PKR by dsRNA is accompanied by autophosphorylation. When activated PKR catalyzes the phosphorylation of the α subunit of eukaryotic initiation factor 2 (eIF2), which results in the sequestration of a second initiation factor, the guanosine nucleotide exchange factor eIF2B, leading to the inhibition of protein synthesis. This mode of translational shut down constitutes a host defense mechanism and, as such, is detrimental to the viral life cycle. The avoidance of the activation of PKR and/or eIF2 proteins serves as a viral strategy to circumvent this host response. ","_id":"685af523b4ac24d5329d87d5"}],"states_connection":[],"term_comment":"","term_def":"\"A process by which an organism avoids the effects of the host organism's immune response. The host is defined as the larger of the organisms involved in a symbiotic interaction.\" [GOC:mb, PMID:12439615]","term_go_domain":"P","term_id":"GO:0042783","term_is_binding":false,"term_is_obsolete":false,"term_name":"evasion of host immune response","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T12:24:47.386Z","_id":"685af523b4ac24d5329d87d6"},"version":1,"_id":"685af523b4ac24d5329d87d0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","date":"2024-05-03T10:36:44.409Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001807","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","ec_ontology":"ECO","start":41,"end":54,"interaction_partner":[{"db":"RNAcentral","id":"URS00006B18E8_388826","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d87d8"}],"reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","reference_id":"11080476","region_id":"DP00929r030","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"The results of such an experiment are shown in Fig. 3A, where wild-type peptide 41-54 was capable of binding to TAR RNA (lane 3).","_id":"685af523b4ac24d5329d87d9"},{"type":"Curator statement","text":"The authors describe an HIV-1 subtype B Tat protein that is 101 residues long (UniProtKB:P20879; DisProt:DP03560). However, since the regions 41-54 are 100% identical, this IDR is considered to be involved in the same function.","_id":"685af523b4ac24d5329d87da"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a trans-activation response (TAR) element, a hairpin RNA structure located at the 5' end of all HIV-1 transcripts, and which is required for trans-activation of a viral promoter.\" [GOC:bf, GOC:PARL, PMID:25116364, Wikipedia:Trans-activation_response_element_(TAR)]","term_id":"GO:1990970","term_is_obsolete":false,"term_name":"trans-activation response element binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2024-05-06T12:58:01.737Z","_id":"685af523b4ac24d5329d87db"},"version":0,"_id":"685af523b4ac24d5329d87d7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-04-30T16:40:47.173Z","disprot_namespace":"Disorder function","ec_id":"ECO:0001254","ec_name":"radioisotope assay evidence used in manual assertion","ec_ontology":"ECO","start":41,"end":54,"interaction_partner":[],"reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","reference_id":"11080476","region_id":"DP00929r033","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"The results of such an experiment are shown in Fig. 1C, where Tat 41-54\npeptide, but not 41-50 peptide (lanes 7±10), was acetylated with GST-HAT.","_id":"685af523b4ac24d5329d87ec"}],"states_connection":[],"term_id":"IDPO:0000039","term_name":"acetylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d87eb","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":50,"end":50,"statements":[],"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d87ee"},{"start":51,"end":51,"statements":[],"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d87ef"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-04-30T16:40:36.965Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0007009","ec_name":"radioligand binding assay evidence used in manual assertion","ec_ontology":"ECO","start":41,"end":54,"interaction_partner":[{"db":"RNAcentral","id":"URS00006B18E8_388826","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d87f1"}],"reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","reference_id":"11080476","region_id":"DP00929r034","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"The results of such an experiment are shown in Fig. 3A, where wild-type peptide 41-54 was capable of binding to TAR RNA (lane 3). The TAR RNA binding is completely abolished when lysines 50 and 51 are acetylated (lanes 6 and 7). We observed no binding of double-acetylated 50 and 51 peptide to TAR RNA at any peptide concentration (data not shown). Similar results were also observed when Tat protein was acetylated with GST-HAT prior to TAR RNA binding (Fig. 3B, lanes 4 and 5).","_id":"685af523b4ac24d5329d87f0"}],"states_connection":[],"term_comment":"","term_def":"\"Any process that stops, prevents or reduces the frequency, rate or extent of RNA binding.\" [GO_REF:0000059, GOC:bf, GOC:PARL, GOC:TermGenie]","term_id":"GO:1905215","term_is_obsolete":false,"term_name":"negative regulation of RNA binding","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d87ed","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[],"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","_id":"685af523b4ac24d5329d87f3"},{"start":51,"end":51,"statements":[],"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d87f4"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-04-30T16:51:07.227Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0007009","ec_name":"radioligand binding assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":86,"interaction_partner":[{"db":"UniProt","id":"Q92793","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d87f5"}],"reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","reference_id":"11080476","region_id":"DP00929r035","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"The results of such an experiment are shown in Fig. 3C, where GST-Tat, but not GST, was able to bind to 35S-labeled CBP in vitro.","_id":"685af523b4ac24d5329d87f6"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d87f2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[],"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","_id":"685af523b4ac24d5329d87f8"},{"start":51,"end":51,"statements":[],"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d87f9"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-04-30T16:52:03.696Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0007009","ec_name":"radioligand binding assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":86,"interaction_partner":[{"db":"UniProt","id":"Q92793","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d87fa"}],"reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","reference_id":"11080476","region_id":"DP00929r036","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"The results of such an experiment are shown in Fig. 3C, where GST-Tat, but not GST, was able to bind to 35S-labeled CBP in vitro.","_id":"685af523b4ac24d5329d87fb"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a transcription coactivator, a protein involved in positive regulation of transcription via protein-protein interactions with transcription factors and other proteins that positively regulate transcription. Transcription coactivators do not bind DNA directly, but rather mediate protein-protein interactions between activating transcription factors and the basal transcription machinery.\" [GOC:krc]","term_id":"GO:0001223","term_is_obsolete":false,"term_name":"transcription coactivator binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d87f7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[],"term_id":"MI:0253","term_name":"other isotope label","term_namespace":"Labels and dyes","_id":"685af523b4ac24d5329d87fd"},{"start":51,"end":51,"statements":[],"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d87fe"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-04-30T17:12:38.094Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007632","ec_name":"transcriptional activation assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":86,"interaction_partner":[],"reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","reference_id":"11080476","region_id":"DP00929r037","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"Tat is one of the most powerful viral activators known to date. Tat could stimulate transcription of HIV-1 promoter anywhere from 100- to 1000-fold depending on the assay conditions used.","_id":"685af523b4ac24d5329d87ff"},{"type":"Results","text":"Taken together, the transient transfection results indicate that neither K50 nor K51 mutations alone are sufficient to completely lose the Tat transactivation on HIV-1 LTR.","_id":"685af523b4ac24d5329d8800"},{"type":"Curator statement","text":"Figure 5 shows the transcription activator activity of the wild-type TAT protein.","_id":"685af523b4ac24d5329d8801"}],"states_connection":[],"term_comment":"Usage guidance: transcription regulator activators bind to a transcription regulator to allow it to reach the chromatin or to contact other transcriptional regulators. This activity does not occur at the promoter. For activities that do occur at the promoter, consider GO:0001216 ; DNA-binding transcription activator activity or GO:0003713; transcription coactivator activity; those activities respectively bind DNA themselves or positively regulate a transcription regulator when it is located at the chromatin.","term_def":"\"A molecular function regulator that increases the activity of a transcription regulator via direct binding and/or post-translational modification.\" [PMID:9597751]","term_id":"GO:0140537","term_is_obsolete":false,"term_name":"transcription regulator activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d87fc","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[],"term_id":"MI:0253","term_name":"other isotope label","term_namespace":"Labels and dyes","_id":"685af523b4ac24d5329d8803"},{"start":51,"end":51,"statements":[],"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d8804"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-04-30T16:58:05.051Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0001254","ec_name":"radioisotope assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":86,"interaction_partner":[{"db":"UniProt","id":"Q09472","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8805"}],"reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","reference_id":"11080476","region_id":"DP00929r038","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"When binding 35S-labeled Tat to various GST-p300 domains, we found that Tat bound stably to all A, B, and C mutant domains under 0.1 M salt wash conditions (Fig. 4B, lanes 1-4).","_id":"685af523b4ac24d5329d8806"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d8802","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Results","text":"We decided to address this question by utilizing affinity pull-down experiments using wild-type or acetylated 42-54 peptides coupled to a biotin moiety.","_id":"685af523b4ac24d5329d8809"}],"term_id":"MI:0239","term_name":"biotin","term_namespace":"Tag","_id":"685af523b4ac24d5329d8808"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-04-30T17:39:41.495Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006077","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","ec_ontology":"ECO","start":42,"end":54,"interaction_partner":[{"db":"UniProt","id":"Q92793","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d880a"},{"db":"UniProt","id":"O60563","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d880b"},{"db":"UniProt","id":"P20226","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d880c"}],"reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","reference_id":"11080476","region_id":"DP00929r039","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"The results of such an experiment are shown in Fig. 7A, where 35Slabeled TBP, CBP, and cyclin T could efficiently bind to wild-type but not acetylated 42-50 peptide.","_id":"685af523b4ac24d5329d880d"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d8807","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Results","text":"We decided to address this question by utilizing affinity pull-down experiments using wild-type or acetylated 42-54 peptides coupled to a biotin moiety.","_id":"685af523b4ac24d5329d8810"}],"term_id":"MI:0239","term_name":"biotin","term_namespace":"Tag","_id":"685af523b4ac24d5329d880f"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-04-30T18:08:26.243Z","disprot_namespace":"Disorder function","ec_go":"IEP","ec_id":"ECO:0000279","ec_name":"qualitative western immunoblotting evidence used in manual assertion","ec_ontology":"ECO","start":42,"end":54,"interaction_partner":[{"db":"UniProt","id":"P24928","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8811"}],"reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","reference_id":"11080476","region_id":"DP00929r040","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"Results from Western blots indicated that wild-type and not acetylated peptide was capable of binding to core-Pol II.","_id":"685af523b4ac24d5329d8812"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA polymerase core enzyme, containing a specific subunit composition defined as the core enzyme.\" [GOC:jl, GOC:txnOH]","term_id":"GO:0043175","term_is_obsolete":false,"term_name":"RNA polymerase core enzyme binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d880e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Results","text":"We decided to address this question by utilizing affinity pull-down experiments using wild-type or acetylated 42-54 peptides coupled to a biotin moiety.","_id":"685af523b4ac24d5329d8815"}],"term_id":"MI:0239","term_name":"biotin","term_namespace":"Tag","_id":"685af523b4ac24d5329d8814"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-04-30T17:51:47.083Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006077","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","ec_ontology":"ECO","start":42,"end":54,"interaction_partner":[{"db":"UniProt","id":"O60563","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8816"}],"reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","reference_id":"11080476","region_id":"DP00929r041","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"The results of such an experiment are shown in Fig. 7A, where 35Slabeled TBP, CBP, and cyclin T could efficiently bind to wild-type but not acetylated 42-50 peptide.","_id":"685af523b4ac24d5329d8817"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to cyclins, proteins whose levels in a cell varies markedly during the cell cycle, rising steadily until mitosis, then falling abruptly to zero. As cyclins reach a threshold level, they are thought to drive cells into G2 phase and thus to mitosis.\" [GOC:ai]","term_id":"GO:0030332","term_is_obsolete":false,"term_name":"cyclin binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d8813","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Results","text":"We decided to address this question by utilizing affinity pull-down experiments using wild-type or acetylated 42-54 peptides coupled to a biotin moiety.","_id":"685af523b4ac24d5329d881a"}],"term_id":"MI:0239","term_name":"biotin","term_namespace":"Tag","_id":"685af523b4ac24d5329d8819"},{"start":50,"end":50,"statements":[{"type":"Figure","text":"The synthesized Tat peptides (42-54) with or without acetylated lysines at positions 50 and 51 were labeled with biotin at the N- terminus.","_id":"685af523b4ac24d5329d881c"}],"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d881b"},{"start":51,"end":51,"statements":[{"type":"Figure","text":"The synthesized Tat peptides (42-54) with or without acetylated lysines at positions 50 and 51 were labeled with biotin at the N- terminus.","_id":"685af523b4ac24d5329d881e"}],"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d881d"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-04-30T18:33:24.100Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006077","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","ec_ontology":"ECO","start":42,"end":54,"interaction_partner":[{"db":"UniProt","id":"P62805","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d881f"},{"db":"UniProt","id":"Q6NXT2","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8820"},{"db":"UniProt","id":"Q6FI13","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8821"},{"db":"UniProt","id":"P06899","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8822"}],"reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","reference_id":"11080476","region_id":"DP00929r042","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"The results of such an experiment are shown in Fig. 7B, where acetylated Tat peptide was able to bind to core histones. It is interesting to note that core histones in the absence of DNA did not bind to acetylated Tat, indicating that a fixed conformation of nucleosome is required for Tat to bind to core histones.","_id":"685af523b4ac24d5329d8823"},{"type":"Curator statement","text":"Experiments show that the wild-type not acetylated peptide also binds nucleosomes but in a lesser degree. ","_id":"685af523b4ac24d5329d8824"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a nucleosome, a complex comprised of DNA wound around a multisubunit core and associated proteins, which forms the primary packing unit of DNA into higher order structures.\" [GOC:mah]","term_id":"GO:0031491","term_is_obsolete":false,"term_name":"nucleosome binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d8818","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Methods","text":"Glutathione S-transferase (GST), GST-Tat, and GST-Tat mutants were prepared as already described (11).","_id":"685af523b4ac24d5329d8827"}],"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","_id":"685af523b4ac24d5329d8826"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-05-06T14:28:49.072Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005640","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":86,"interaction_partner":[{"db":"UniProt","id":"Q09472","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8828"},{"db":"UniProt","id":"Q92793","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8829"}],"reference_html":"HIV-1 tat transactivator recruits p300 and CREB-binding protein histone acetyltransferases to the viral promoter. <i> Marzio G, Tyagi M, Gutierrez MI, Giacca M. </i> Proc Natl Acad Sci U S A, 1998","reference_id":"9811832","region_id":"DP00929r043","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"As shown in Fig. ​1c, wild-type 101 and 86 Tat proteins bound the HAT activity present in the nuclear extract with similar efficiencies.","_id":"685af523b4ac24d5329d882a"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an histone acetyltransferase.\" [GOC:bf]","term_id":"GO:0035035","term_is_obsolete":false,"term_name":"histone acetyltransferase binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d8825","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Methods","text":"Glutathione S-transferase (GST), GST-Tat, and GST-Tat mutants were prepared as already described (11).","_id":"685af523b4ac24d5329d882d"}],"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","_id":"685af523b4ac24d5329d882c"},{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To determine the domains of Tat that are important for association with HAT activity, GST pull-down experiments were performed by using wt Tat 101 (present in several primary HIV isolates), wt Tat 86 (HXB2 clone), and some mutated derivatives of the latter [Tat 86 Δ(1–21), lacking the amino-terminal acidic domain; Tat 86R(49–57)A, with six arginines in the basic domain mutated to alanines; and Tat 86C(22–27)A, with three cysteines mutated to alanines in the cysteine-rich domain].","_id":"685af523b4ac24d5329d882f"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg49Ala","_id":"685af523b4ac24d5329d882e"},{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To determine the domains of Tat that are important for association with HAT activity, GST pull-down experiments were performed by using wt Tat 101 (present in several primary HIV isolates), wt Tat 86 (HXB2 clone), and some mutated derivatives of the latter [Tat 86 Δ(1–21), lacking the amino-terminal acidic domain; Tat 86R(49–57)A, with six arginines in the basic domain mutated to alanines; and Tat 86C(22–27)A, with three cysteines mutated to alanines in the cysteine-rich domain].","_id":"685af523b4ac24d5329d8831"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys50Ala","_id":"685af523b4ac24d5329d8830"},{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To determine the domains of Tat that are important for association with HAT activity, GST pull-down experiments were performed by using wt Tat 101 (present in several primary HIV isolates), wt Tat 86 (HXB2 clone), and some mutated derivatives of the latter [Tat 86 Δ(1–21), lacking the amino-terminal acidic domain; Tat 86R(49–57)A, with six arginines in the basic domain mutated to alanines; and Tat 86C(22–27)A, with three cysteines mutated to alanines in the cysteine-rich domain].","_id":"685af523b4ac24d5329d8833"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys51Ala","_id":"685af523b4ac24d5329d8832"},{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To determine the domains of Tat that are important for association with HAT activity, GST pull-down experiments were performed by using wt Tat 101 (present in several primary HIV isolates), wt Tat 86 (HXB2 clone), and some mutated derivatives of the latter [Tat 86 Δ(1–21), lacking the amino-terminal acidic domain; Tat 86R(49–57)A, with six arginines in the basic domain mutated to alanines; and Tat 86C(22–27)A, with three cysteines mutated to alanines in the cysteine-rich domain].","_id":"685af523b4ac24d5329d8835"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg52Ala","_id":"685af523b4ac24d5329d8834"},{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To determine the domains of Tat that are important for association with HAT activity, GST pull-down experiments were performed by using wt Tat 101 (present in several primary HIV isolates), wt Tat 86 (HXB2 clone), and some mutated derivatives of the latter [Tat 86 Δ(1–21), lacking the amino-terminal acidic domain; Tat 86R(49–57)A, with six arginines in the basic domain mutated to alanines; and Tat 86C(22–27)A, with three cysteines mutated to alanines in the cysteine-rich domain].","_id":"685af523b4ac24d5329d8837"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg53Ala","_id":"685af523b4ac24d5329d8836"},{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To determine the domains of Tat that are important for association with HAT activity, GST pull-down experiments were performed by using wt Tat 101 (present in several primary HIV isolates), wt Tat 86 (HXB2 clone), and some mutated derivatives of the latter [Tat 86 Δ(1–21), lacking the amino-terminal acidic domain; Tat 86R(49–57)A, with six arginines in the basic domain mutated to alanines; and Tat 86C(22–27)A, with three cysteines mutated to alanines in the cysteine-rich domain].","_id":"685af523b4ac24d5329d8839"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gln54Ala","_id":"685af523b4ac24d5329d8838"},{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To determine the domains of Tat that are important for association with HAT activity, GST pull-down experiments were performed by using wt Tat 101 (present in several primary HIV isolates), wt Tat 86 (HXB2 clone), and some mutated derivatives of the latter [Tat 86 Δ(1–21), lacking the amino-terminal acidic domain; Tat 86R(49–57)A, with six arginines in the basic domain mutated to alanines; and Tat 86C(22–27)A, with three cysteines mutated to alanines in the cysteine-rich domain].","_id":"685af523b4ac24d5329d883b"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg55Ala","_id":"685af523b4ac24d5329d883a"},{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To determine the domains of Tat that are important for association with HAT activity, GST pull-down experiments were performed by using wt Tat 101 (present in several primary HIV isolates), wt Tat 86 (HXB2 clone), and some mutated derivatives of the latter [Tat 86 Δ(1–21), lacking the amino-terminal acidic domain; Tat 86R(49–57)A, with six arginines in the basic domain mutated to alanines; and Tat 86C(22–27)A, with three cysteines mutated to alanines in the cysteine-rich domain].","_id":"685af523b4ac24d5329d883d"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg56Ala","_id":"685af523b4ac24d5329d883c"},{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To determine the domains of Tat that are important for association with HAT activity, GST pull-down experiments were performed by using wt Tat 101 (present in several primary HIV isolates), wt Tat 86 (HXB2 clone), and some mutated derivatives of the latter [Tat 86 Δ(1–21), lacking the amino-terminal acidic domain; Tat 86R(49–57)A, with six arginines in the basic domain mutated to alanines; and Tat 86C(22–27)A, with three cysteines mutated to alanines in the cysteine-rich domain].","_id":"685af523b4ac24d5329d883f"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg57Ala","_id":"685af523b4ac24d5329d883e"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-05-06T14:28:58.823Z","disprot_namespace":"Disorder function","ec_go":"IMP","ec_id":"ECO:0007089","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","ec_ontology":"ECO","start":49,"end":57,"interaction_partner":[{"db":"UniProt","id":"Q09472","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8840"},{"db":"UniProt","id":"Q92793","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8841"}],"reference_html":"HIV-1 tat transactivator recruits p300 and CREB-binding protein histone acetyltransferases to the viral promoter. <i> Marzio G, Tyagi M, Gutierrez MI, Giacca M. </i> Proc Natl Acad Sci U S A, 1998","reference_id":"9811832","region_id":"DP00929r044","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"As shown in Fig. 1c, wild-type 101 and 86 Tat proteins bound the HAT activity present in the nuclear extract with similar efficiencies. The affinity was only slightly decreased in mutants Tat 86 Δ(1–21) and Tat 86C(22–27)A. On the contrary, amino acid substitutions of the arginines in the arginine-rich domain almost abolished association of Tat with the HAT activity.","_id":"685af523b4ac24d5329d8842"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an histone acetyltransferase.\" [GOC:bf]","term_id":"GO:0035035","term_is_obsolete":false,"term_name":"histone acetyltransferase binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d882b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Methods","text":"Glutathione S-transferase (GST), GST-Tat, and GST-Tat mutants were prepared as already described (11).","_id":"685af523b4ac24d5329d8845"}],"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","_id":"685af523b4ac24d5329d8844"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-05-06T14:27:27.795Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005620","ec_name":"chromatin immunoprecipitation-PCR evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":86,"interaction_partner":[{"db":"ENA","id":"M69075","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8848"}],"reference_html":"HIV-1 tat transactivator recruits p300 and CREB-binding protein histone acetyltransferases to the viral promoter. <i> Marzio G, Tyagi M, Gutierrez MI, Giacca M. </i> Proc Natl Acad Sci U S A, 1998","reference_id":"9811832","region_id":"DP00929r045","released":"2024_06","sample":[{"db":"Cellosaurus","deviation":null,"entry_name":"HeLa-HL3T1","id":"CVCL_8232","statements":[],"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_id":"UO:0000201","unit_name":"cells/ml","value":null,"_id":"685af523b4ac24d5329d8846"}],"statement":[{"type":"Results","text":"After Tat treatment, a remarkable enrichment for this genomic region (10-fold for p300 and 33-fold for CBP) was observed (Fig. ​4e). These data demonstrate that Tat-mediated activation of the integrated LTR in vivo is concomitant with the recruitment of p300 and CBP specifically to the promoter region.","_id":"685af523b4ac24d5329d8847"}],"states_connection":[],"term_comment":"Usage guidance: transcription regulator activators bind to a transcription regulator to allow it to reach the chromatin or to contact other transcriptional regulators. This activity does not occur at the promoter. For activities that do occur at the promoter, consider GO:0001216 ; DNA-binding transcription activator activity or GO:0003713; transcription coactivator activity; those activities respectively bind DNA themselves or positively regulate a transcription regulator when it is located at the chromatin.","term_def":"\"A molecular function regulator that increases the activity of a transcription regulator via direct binding and/or post-translational modification.\" [PMID:9597751]","term_id":"GO:0140537","term_is_obsolete":false,"term_name":"transcription regulator activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d8843","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[],"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","_id":"685af523b4ac24d5329d884a"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-05-06T14:40:43.122Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005640","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","ec_ontology":"ECO","start":48,"end":57,"interaction_partner":[{"db":"UniProt","id":"Q09472","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d884b"}],"reference_html":"Interaction of human immunodeficiency virus type 1 Tat with the transcriptional coactivators p300 and CREB binding protein. <i> Hottiger MO, Nabel GJ. </i> J Virol, 1998","reference_id":"9733868","region_id":"DP00929r046","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"Only fusion proteins which contained the Tat basic domain (residues 48 to 57) bound p300, including a fusion protein that expressed only this basic domain region (Fig. 4A, top).","_id":"685af523b4ac24d5329d884c"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an histone acetyltransferase.\" [GOC:bf]","term_id":"GO:0035035","term_is_obsolete":false,"term_name":"histone acetyltransferase binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d8849","reference_source":"pmid"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":49,"type":"T"},{"start":50,"end":86,"type":"D"}],"Structural state":[{"start":1,"end":86,"type":"D"}],"Structural transition":[{"start":1,"end":49,"type":"T"}],"Molecular function":[{"start":1,"end":86,"type":"F"}],"Disorder function":[{"start":41,"end":54,"type":"F"},{"start":62,"end":68,"type":"F"}],"Biological process":[{"start":1,"end":72,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05466","name":"Brain acid soluble protein 1 (BASP1 protein)","start":1,"end":227}]},"uniref50":"UniRef50_P80723","sequence":"MGGKLSKKKKGYNVNDEKAKEKDKKAEGAATEEEGTPKESEPQAAAEPAEAKEGKEKPDQDAEGKAEEKEGEKDAAAAKEEAPKAEPEKTEGAAEAKAEPPKAPEQEQAAPGPAAGGEAPKAAEAAAAPAESAAPAAGEEPSKEEGEPKKTEAPAAPAAQETKSDGAPASDSKPGSSEAAPSSKETPAATEAPSSTPKAQGPAASAEEPKPVEAPAANSDQTVTVKE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P80723","disprot_id":"DP00930","ncbi_taxon_id":9606,"regions_counter":10,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":227,"region_id":"DP00930r001","released":"2023_12","ec_id":"ECO:0006165","reference_html":"¹H, ¹³C and ¹⁵N resonance assignments of human BASP1. <i> Geist L, Zawadzka-Kazimierczuk A, Saxena S, Żerko S, Koźmiński W, Konrat R. </i> Biomol NMR Assign, 2013","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-27T12:27:20.966Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"BMRB","id":"18417"}],"reference_id":"23179057","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Figure","text":"Assignments of backbone amides are labeled in single letter amino acid code and residue number (His6-tag: 1–26; hBASP1: 27–253"}]}],"sequence_construct":"MKHHHHHHPMSDYDIPTTENLYFQGAMGGKLSKKKKGYNVNDEKAKEKDKKAEGAATEEEGTPKESEPQAAAEPAEAKEGKEKPDQDAEGKAEEKEGEKDAAAAKEEAPKAEPEKTEGAAEAKAEPPKAPEQEQAAPGPAAGGEAPKAAEAAAAPAESAAPAAGEEPSKEEGEPKKTEAPAAPAAQETKSDGAPASDSKPGSSEAAPSSKETPAATEAPSSTPKAQGPAASAEEPKPVEAPAANSDQTVTVKE","statement":[{"text":"The 1H–15N HSQC spectrum of H6-hBASP1 shows a very narrow peak dispersion in the 1H dimension typical for intrinsically disordered proteins (Fig. 1).","type":"Results"},{"text":"Secondary chemical shifts for 13C′, 13Cα, 1Hα (Fig. 3) show only minor deviations from random coil chemical shift values.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:30:26.614Z"}},{"start":1,"end":227,"reference_id":"32750402","reference_source":"pmid","reference_html":"The effects of phospholipids and fatty acids on the oligomer formation of NAP-22. <i> Odagaki SI, Maekawa S, Hayashi F, Suzaki T, Morigaki K. </i> Neurosci Lett, 2020","date":"2023-11-27T12:33:40.180Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051260","term_name":"protein homooligomerization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP00930r005","statement":[{"text":" Under 150 mM NaCl and neutral pH conditions, NAP-22 samples showed two bands after SDS-PAGE. The lower band of ∼50 kDa was considered the monomer (Fig. 1A, white arrow). Another band that showed low mobility in the 10 % acrylamide gel was judged to be the oligomer (Fig. 1A, black arrow). Enlargement of the oligomer band showed that the band was composed of many bands of various number of monomers (Fig. 1B and C, Fig. 2A)","type":"Results"},{"text":"The dose-dependent effect of NaCl or MgCl2 on oligomerization was evident at 37℃ and pH 7.4 (Fig. 1B and C). ","type":"Results"}],"term_comment":"","term_def":"\"The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":150,"db":"ChEBI","id":"26710","entry_name":"sodium chloride"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:30:52.270Z"}},{"start":1,"end":227,"reference_id":"32750402","reference_source":"pmid","reference_html":"The effects of phospholipids and fatty acids on the oligomer formation of NAP-22. <i> Odagaki SI, Maekawa S, Hayashi F, Suzaki T, Morigaki K. </i> Neurosci Lett, 2020","date":"2023-11-27T13:10:39.656Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005516","term_name":"calmodulin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P0DP23","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00930r006","statement":[{"text":"Further addition of calmodulin (CaM) abolished oligomer formation and the formation of 1:1 complex of CaM and NAP-22 was observed (arrow in Fig. 1D) [11]. Addition of CaM after oligomerization also diminished oligomer.","type":"Results"}],"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:31:00.923Z"}},{"start":1,"end":67,"reference_id":"32750402","reference_source":"pmid","reference_html":"The effects of phospholipids and fatty acids on the oligomer formation of NAP-22. <i> Odagaki SI, Maekawa S, Hayashi F, Suzaki T, Morigaki K. </i> Neurosci Lett, 2020","date":"2023-11-27T14:15:26.850Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0379","term_name":"13C label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"N-terminal"}],"region_id":"DP00930r007","sequence_construct":"aaa","statement":[{"text":"Further addition of calmodulin (CaM) abolished oligomer formation and the formation of 1:1 complex of CaM and NAP-22 was observed (arrow in Fig. 1D) [11]. Addition of CaM after oligomerization also diminished oligomer.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:30:30.914Z"}},{"start":1,"end":227,"reference_id":"32750402","reference_source":"pmid","reference_html":"The effects of phospholipids and fatty acids on the oligomer formation of NAP-22. <i> Odagaki SI, Maekawa S, Hayashi F, Suzaki T, Morigaki K. </i> Neurosci Lett, 2020","date":"2023-11-27T13:58:04.815Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0097435","term_name":"supramolecular fiber organization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP00930r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"28494","entry_name":"cardiolipin"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"26208","entry_name":"polyunsaturated fatty acid"}],"statement":[{"text":"Observed NAP-22 oligomers are shown in Fig. 4. NAP-22 oligomers formed in HMEN buffer without lipid addition (CTL) showed a tangled rope-like filamentous structure.","type":"Results"},{"text":"Morphological analysis showed the formation of tangled rope-like filaments in the absence of lipid (Fig. 4). The presence of many annular structures in the filaments suggested that these rings could be the oligomer that assembled to make rope-like filaments.","type":"Discussion"},{"text":"The ring-structures observed on the NAP-22 aggregates observed in the presence of CL or PUFA were looked like ellipsoidal, and the size of the annular oligomers were slightly larger than that of oligomers formed in the absence of lipid (CTL). This suggests that CL and PUFA could increase the monomer number in the oligomer.","type":"Abstract"},{"text":"These results suggest the participation of NAP-22 to liquid-liquid phase separation through oligomerization.","type":"Abstract"}],"term_comment":"","term_def":"\"A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a supramolecular fiber, a polymer consisting of an indefinite number of protein or protein complex subunits that have polymerised to form a fiber-shaped structure.\" [GOC:pr]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:31:03.890Z"}},{"start":1,"end":60,"reference_id":"26411860","reference_source":"pmid","reference_html":"Detection of correlated conformational fluctuations in intrinsically disordered proteins through paramagnetic relaxation interference. <i> Kurzbach D, Vanas A, Flamm AG, Tarnoczi N, Kontaxis G, Maltar-Strmečki N, Widder K, Hinderberger D, Konrat R. </i> Phys Chem Chem Phys, 2016","date":"2023-11-30T20:42:07.297Z","curator_id":"atantos","curator_name":"Agnes Tantos","curator_orcid":"0000-0003-1273-9841","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP00930r009","statement":[{"text":"Our observations clearly indicate that the N-terminal region of BASP1 transiently samples compact substrates despite the lack of significant secondary 13C backbone chemical shifts for that regions.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:30:32.900Z"}},{"start":1,"end":227,"reference_id":"28397898","reference_source":"pmid","reference_html":"NMR probing and visualization of correlated structural fluctuations in intrinsically disordered proteins. <i> Kurzbach D, Beier A, Vanas A, Flamm AG, Platzer G, Schwarz TC, Konrat R. </i> Phys Chem Chem Phys, 2017","date":"2023-11-30T20:40:12.096Z","curator_id":"atantos","curator_name":"Agnes Tantos","curator_orcid":"0000-0003-1273-9841","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP00930r010","statement":[{"text":"The PRE correlation matrix points to the existence of partially folded structural segments comprising residues 1–70, 70–90, 90–140 and, 170–200 with the N-terminus being the most compact one. Inter-segmental couplings are weak or even anti-correlated. These findings are in very good agreement with earlier studies providing evidence for an N-terminal compaction of BASP1 in solution, while the rest of the polypeptide chain displays random coil characteristics.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:30:49.936Z"}}],"released":"2016_10","uniref100":"UniRef100_P80723","date":"2016-09-06T09:26:13.000Z","acc":"P80723","name":"Brain acid soluble protein 1","length":227,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI0000126798","genes":[{"name":{"value":"BASP1"},"synonyms":[{"value":"NAP22"}]}],"alphafold_very_low_content":0.4845814977973568,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":227,"type":"D"}],"Structural state":[{"start":1,"end":227,"type":"D"}],"Biological process":[{"start":1,"end":227,"type":"F"}],"Molecular function":[{"start":1,"end":227,"type":"F"}]}},{"features":{"pfam":[{"id":"PF20863","name":"IcmR, middle region","start":29,"end":86}]},"uniref50":"UniRef50_O54568","sequence":"MGNNTDDSARNPFGFYTPPRVKEIGEPDVTDATLGSVYSEIISPVKDCILTVAKAVSFNPGGKDNTDAVEVLTELNTKVERAALNQPILTTKTERMFGAAESEKSSEPPSHDERGFKLSS","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Legionellales","Legionellaceae","Legionella"],"uniref90":"UniRef90_O54568","disprot_id":"DP00931","ncbi_taxon_id":272624,"regions_counter":4,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":27,"region_id":"DP00931r001","released":"2022_12","ec_id":"ECO:0006204","reference_html":"Structure and function of interacting IcmR-IcmQ domains from a type IVb secretion system in Legionella pneumophila. <i> Raychaudhury S, Farelli JD, Montminy TP, Matthews M, Ménétret JF, Duménil G, Roy CR, Head JF, Isberg RR, Akey CW. </i> Structure, 2009","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-22T19:41:28.546Z","reference_source":"pmid","term_name":"disorder","reference_id":"19368892","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"During purification, IcmR is slowly digested by an endogenous bacterial protease to form a smaller fragment that can account for ∼30-40% of the sample (Experimental Procedures, Figure 1C, lane 1).","type":"Results"},{"text":"This complex was trypsinized to remove flexible residues from the two proteins. ","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":120,"region_id":"DP00931r002","released":"2022_12","ec_id":"ECO:0007691","reference_html":"Structure and function of interacting IcmR-IcmQ domains from a type IVb secretion system in Legionella pneumophila. <i> Raychaudhury S, Farelli JD, Montminy TP, Matthews M, Ménétret JF, Duménil G, Roy CR, Head JF, Isberg RR, Akey CW. </i> Structure, 2009","term_id":"IDPO:0000002","curator_id":"vnugnes","start":87,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-22T19:42:02.672Z","reference_source":"pmid","term_name":"disorder","reference_id":"19368892","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"This complex was trypsinized to remove flexible residues from the two proteins. ","type":"Results"},{"text":"During purification, IcmR is slowly digested by an endogenous bacterial protease to form a smaller fragment that can account for ∼30-40% of the sample (Experimental Procedures, Figure 1C, lane 1).","type":"Results"}]},{"start":1,"end":27,"reference_id":"23850453","reference_source":"pmid","reference_html":"IcmQ in the Type 4b secretion system contains an NAD+ binding domain. <i> Farelli JD, Gumbart JC, Akey IV, Hempstead A, Amyot W, Head JF, McKnight CJ, Isberg RR, Akey CW. </i> Structure, 2013","date":"2022-08-22T19:33:22.267Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"4EYY"}],"region_id":"DP00931r003","statement":[{"text":"After refinement, the final model consists of residues 28–86 of IcmR and residues 1–191 of IcmQ (see Table 1).","type":"Results"}]},{"start":87,"end":120,"reference_id":"23850453","reference_source":"pmid","reference_html":"IcmQ in the Type 4b secretion system contains an NAD+ binding domain. <i> Farelli JD, Gumbart JC, Akey IV, Hempstead A, Amyot W, Head JF, McKnight CJ, Isberg RR, Akey CW. </i> Structure, 2013","date":"2022-08-22T19:34:09.565Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"4EYY"}],"region_id":"DP00931r004","statement":[{"text":"After refinement, the final model consists of residues 28–86 of IcmR and residues 1–191 of IcmQ (see Table 1).","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_O54568","date":"2016-09-06T09:50:38.000Z","acc":"Q5ZYC9","name":"IcmR","length":120,"organism":"Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)","dataset":[],"UniParc":"UPI00000AF99B","genes":[{"name":{"value":"icmR","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAU26540.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAU26540.1"}}]},"olnNames":[{"value":"lpg0443","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAU26540.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAU26540.1"}}]}]}],"alphafold_very_low_content":0.35833333333333334,"disorder_content":0.5083333333333333,"disprot_consensus":{"full":[{"start":1,"end":27,"type":"D"},{"start":87,"end":120,"type":"D"}],"Structural state":[{"start":1,"end":27,"type":"D"},{"start":87,"end":120,"type":"D"}]}},{"acc":"P35926","sequence":"MKTIEQKIEQCRKWQKAARERAIARQREKLADPVWRESQYQKMRDTLDRRIAKQKERPPASKTRKSAVKIKSRGLKGRTPTAEERRIANALGALPCIACYMHGVISNEVSLHHIAGRTAPGCHKKQLPLCRWHHQHAAPAEVREKYPWLVPVHADGVVGGKKEFTLLNKSEMELLADAYEMANIMH","creator":"akajava","dataset":["Viral proteins"],"date":"2016-09-06T10:08:42.000Z","disprot_id":"DP00932","features":{"pfam":[{"id":"PF16786","name":"Recombination enhancement, RecA-dependent nuclease","start":80,"end":182}],"gene3D":[{"start":77,"end":186,"id":"3.30.40.190","name":"3.30.40.190","_id":"685af523b4ac24d5329d8852"}]},"genes":[{"name":{"value":"ref","evidences":[],"_id":"685af523b4ac24d5329d8861"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d8860"}],"length":186,"name":"Recombination enhancement function protein","ncbi_taxon_id":10678,"organism":"Escherichia phage P1","regions_counter":4,"released":"2016_10","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Uroviricota","Caudoviricetes","Caudovirales","Myoviridae","Punavirus"],"UniParc":"UPI000013362C","uniref100":"UniRef100_P35926","uniref50":"UniRef50_P35926","uniref90":"UniRef90_P35926","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3PLW","_id":"685af523b4ac24d5329d8854"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":76,"interaction_partner":[],"reference_html":"Creating directed double-strand breaks with the Ref protein: a novel RecA-dependent nuclease from bacteriophage P1. <i> Gruenig MC, Lu D, Won SJ, Dulberger CL, Manlick AJ, Keck JL, Cox MM. </i> J Biol Chem, 2011","reference_id":"21193392","region_id":"DP00932r001","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"The N-terminal 76 amino acid residues are disordered; this flexible region is required for optimal activity.","_id":"685af523b4ac24d5329d8855"},{"type":"Results","text":"Electron density for the N-terminal 76 residues was absent, indicating that it may be a flexible element.","_id":"685af523b4ac24d5329d8856"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T11:43:53.187Z","_id":"685af523b4ac24d5329d8857"},"version":3,"_id":"685af523b4ac24d5329d8853","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2023-02-16T19:55:40.002Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0001184","ec_name":"gel-filtration evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":76,"interaction_partner":[],"reference_html":"Creating directed double-strand breaks with the Ref protein: a novel RecA-dependent nuclease from bacteriophage P1. <i> Gruenig MC, Lu D, Won SJ, Dulberger CL, Manlick AJ, Keck JL, Cox MM. </i> J Biol Chem, 2011","reference_id":"21193392","region_id":"DP00932r003","released":"2023_06","sample":[],"statement":[{"type":"Results","text":"To test the functional importance of the N terminus, we constructed a deletion mutant of Ref that lacked the 76 N-terminal amino acids and purified it. It proved to be devoid of Ref-mediated nuclease activity on ssDNA under normal reaction conditions (Fig. 7, lanes 11–13). Some RecA-dependent ssDNA cleavage was seen at much higher concentrations of the mutant Ref protein (10× and 100×; Fig. 7, lanes 14–21). Ref ΔN76 was completely deficient in DNA binding to a 50-mer oligonucleotide up to a concentration of 2.4 μm using the assay shown in Fig. 1 (data not shown). This indicates that the disordered N-terminal domain plays an essential role the DNA binding activity of Ref and also enhances the RecA-dependent nuclease activity. We note that these N-terminal 76 amino acid residues represent a very highly charged part of the protein.","_id":"685af523b4ac24d5329d885b"}],"states_connection":[],"term_comment":"This term should only be used in cases when the regulator directly interacts with the enzyme.","term_def":"\"Binds to and increases the activity of an enzyme.\" [GOC:dph, GOC:mah, GOC:tb]","term_id":"GO:0008047","term_is_binding":false,"term_is_obsolete":false,"term_name":"enzyme activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-02-22T13:10:26.731Z","_id":"685af523b4ac24d5329d885c"},"version":2,"_id":"685af523b4ac24d5329d885a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001807","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":76,"interaction_partner":[],"reference_html":"Creating directed double-strand breaks with the Ref protein: a novel RecA-dependent nuclease from bacteriophage P1. <i> Gruenig MC, Lu D, Won SJ, Dulberger CL, Manlick AJ, Keck JL, Cox MM. </i> J Biol Chem, 2011","reference_id":"21193392","region_id":"DP00932r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"To test the functional importance of the N terminus, we constructed a deletion mutant of Ref that lacked the 76 N-terminal amino acids and purified it. It proved to be devoid of Ref-mediated nuclease activity on ssDNA under normal reaction conditions (Fig. 7, lanes 11–13). Some RecA-dependent ssDNA cleavage was seen at much higher concentrations of the mutant Ref protein (10× and 100×; Fig. 7, lanes 14–21). Ref ΔN76 was completely deficient in DNA binding to a 50-mer oligonucleotide up to a concentration of 2.4 μm using the assay shown in Fig. 1 (data not shown). This indicates that the disordered N-terminal domain plays an essential role the DNA binding activity of Ref and also enhances the RecA-dependent nuclease activity. We note that these N-terminal 76 amino acid residues represent a very highly charged part of the protein.","_id":"685af523b4ac24d5329d885e"}],"states_connection":[],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_id":"GO:0003677","term_is_binding":true,"term_is_obsolete":false,"term_name":"DNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T11:44:11.291Z","_id":"685af523b4ac24d5329d885f"},"version":1,"_id":"685af523b4ac24d5329d885d","reference_source":"pmid"}],"__v":0,"disorder_content":0.40860215053763443,"disprot_consensus":{"full":[{"start":1,"end":76,"type":"D"}],"Structural state":[{"start":1,"end":76,"type":"D"}],"Molecular function":[{"start":1,"end":76,"type":"F"}]}},{"features":{"pfam":[{"id":"PF16810","name":"RXLR phytopathogen effector protein, Avirulence activity","start":10,"end":103}],"gene3D":[{"start":41,"end":108,"id":"1.10.10.2460","name":"1.10.10.2460"}]},"uniref50":"UniRef50_B2C6F7","sequence":"GSSGSSGNVDSNQNKASMLQARLNDEAGGTRLLRVHHESDTEERGFLEKAAVKKMAKAIMADPNKADEVYKKWADKGYTLTQMSNFLKSKTAGKYDRVYNGYVIHLDY","taxonomy":["Eukaryota","Sar","Stramenopiles","Oomycota","Peronosporales","Peronosporaceae","Phytophthora"],"uniref90":"UniRef90_G1K3N3","disprot_id":"DP00933","ncbi_taxon_id":4784,"regions_counter":1,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":44,"region_id":"DP00933r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Phosphatidylinositol monophosphate-binding interface in the oomycete RXLR effector AVR3a is required for its stability in host cells to modulate plant immunity. <i> Yaeno T, Li H, Chaparro-Garcia A, Schornack S, Koshiba S, Watanabe S, Kigawa T, Kamoun S, Shirasu K. </i> Proc Natl Acad Sci U S A, 2011","term_id":"IDPO:0000002","curator_id":"akajava","start":1,"term_ontology":"IDPO","curator_name":"Andrey V Kajava","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-2342-6886","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2LC2"}],"reference_id":"21821794","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_G1K3N3","date":"2016-09-06T10:16:30.000Z","acc":"G1K3N3","name":"AVR3a4","length":108,"organism":"Phytophthora capsici","dataset":[],"UniParc":"UPI00021B6579","genes":[],"alphafold_very_low_content":0.3148148148148148,"disorder_content":0.4074074074074074,"disprot_consensus":{"full":[{"start":1,"end":44,"type":"D"}],"Structural state":[{"start":1,"end":44,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02827","name":"cAMP-dependent protein kinase inhibitor","start":2,"end":69}]},"uniref50":"UniRef50_P61925","sequence":"MTDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEEDAQRSSTEQSGEAQGEAAKSES","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P61925","disprot_id":"DP00934","ncbi_taxon_id":9606,"regions_counter":11,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":33,"region_id":"DP00934r009","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Two well-defined motifs in the cAMP-dependent protein kinase inhibitor (PKIalpha) correlate with inhibitory and nuclear export function. <i> Hauer JA, Barthe P, Taylor SS, Parello J, Padilla A. </i> Protein Sci, 1999","statement":[{"text":"The first a-helical region from residues 7 to 13 corresponds to the high affinity binding helix seen in the crystal structure. The second helix is from residue 34 to 43 of PKIa, and overlaps with the Nuclear Export Signal of PKIa. The remainder of PKIa is not structured. The experiments were done with the rabbit PKIa (Uniprot P61926), IDR is 100% identical.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":14,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-23T19:23:26.458Z","reference_source":"pmid","term_name":"disorder","reference_id":"10091657","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"GTDVETTYADFIASGRTGTTNAIHDMLVSSASGNSNELALKLAGLDINKTEGEEDAQRSSTEQSGEAQGEAAKSES"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":76,"region_id":"DP00934r010","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Two well-defined motifs in the cAMP-dependent protein kinase inhibitor (PKIalpha) correlate with inhibitory and nuclear export function. <i> Hauer JA, Barthe P, Taylor SS, Parello J, Padilla A. </i> Protein Sci, 1999","statement":[{"text":"The first a-helical region from residues 7 to 13 corresponds to the high affinity binding helix seen in the crystal structure. The second helix is from residue 34 to 43 of PKIa, and overlaps with the Nuclear Export Signal of PKIa. The remainder of PKIa is not structured. The experiments were done with the rabbit PKIa (Uniprot P61926), IDR is 100% identical.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":44,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-23T19:23:45.314Z","reference_source":"pmid","term_name":"disorder","reference_id":"10091657","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"GTDVETTYADFIASGRTGTTNAIHDMLVSSASGNSNELALKLAGLDINKTEGEEDAQRSSTEQSGEAQGEAAKSES"}],"released":"2016_10","uniref100":"UniRef100_P61925","date":"2016-09-06T10:33:22.000Z","acc":"P61925","name":"cAMP-dependent protein kinase inhibitor alpha","length":76,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012D7F3","genes":[{"name":{"value":"PKIA"},"synonyms":[{"value":"PRKACN1"}]}],"alphafold_very_low_content":0.14473684210526316,"disorder_content":0.6973684210526315,"disprot_consensus":{"full":[{"start":14,"end":33,"type":"D"},{"start":44,"end":76,"type":"D"}],"Structural state":[{"start":14,"end":33,"type":"D"},{"start":44,"end":76,"type":"D"}]}},{"features":{"pfam":[{"id":"PF12838","name":"4Fe-4S dicluster domain","start":10,"end":61}],"gene3D":[{"start":1,"end":81,"id":"3.30.70.20","name":"3.30.70.20"}]},"uniref50":"UniRef50_P31087","sequence":"MSHSVKIYDTCIGCTQCVRACPLDVLEMVPWDGCKAGQIASSPRTEDCVGCKRCETACPTDFLSIRVYLGAETTRSMGLAY","taxonomy":["Bacteria","Cyanobacteria","Synechococcales","Synechococcaceae","Synechococcus","unclassified Synechococcus"],"uniref90":"UniRef90_P31087","disprot_id":"DP00935","ncbi_taxon_id":32049,"regions_counter":11,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":58,"region_id":"DP00935r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of the unbound, oxidized Photosystem I subunit PsaC, containing [4Fe-4S] clusters F(A) and F(B): a conformational change occurs upon binding to photosystem I. <i> Antonkine ML, Liu G, Bentrop D, Bryant DA, Bertini I, Luchinat C, Golbeck JH, Stehlik D. </i> J Biol Inorg Chem, 2002","term_id":"IDPO:0000002","curator_id":"nmurvai","start":47,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"11941504","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1K0T"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":58,"term_name":"molecular adaptor activity","start":47,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"11941504","version":3,"reference_html":"Solution structure of the unbound, oxidized Photosystem I subunit PsaC, containing [4Fe-4S] clusters F(A) and F(B): a conformational change occurs upon binding to photosystem I. <i> Antonkine ML, Liu G, Bentrop D, Bryant DA, Bertini I, Luchinat C, Golbeck JH, Stehlik D. </i> J Biol Inorg Chem, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP00935r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":58,"term_name":"order to disorder","start":47,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"11941504","version":2,"reference_html":"Solution structure of the unbound, oxidized Photosystem I subunit PsaC, containing [4Fe-4S] clusters F(A) and F(B): a conformational change occurs upon binding to photosystem I. <i> Antonkine ML, Liu G, Bentrop D, Bryant DA, Bertini I, Luchinat C, Golbeck JH, Stehlik D. </i> J Biol Inorg Chem, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000014","ec_id":"ECO:0006165","region_id":"DP00935r007","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":58,"term_name":"protein binding","start":47,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"11941504","version":3,"reference_html":"Solution structure of the unbound, oxidized Photosystem I subunit PsaC, containing [4Fe-4S] clusters F(A) and F(B): a conformational change occurs upon binding to photosystem I. <i> Antonkine ML, Liu G, Bentrop D, Bryant DA, Bertini I, Luchinat C, Golbeck JH, Stehlik D. </i> J Biol Inorg Chem, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP00935r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":80,"region_id":"DP00935r009","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of the unbound, oxidized Photosystem I subunit PsaC, containing [4Fe-4S] clusters F(A) and F(B): a conformational change occurs upon binding to photosystem I. <i> Antonkine ML, Liu G, Bentrop D, Bryant DA, Bertini I, Luchinat C, Golbeck JH, Stehlik D. </i> J Biol Inorg Chem, 2002","term_id":"IDPO:0000002","curator_id":"nmurvai","start":68,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"11941504","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1K0T"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":80,"term_name":"molecular adaptor activity","start":68,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"11941504","version":3,"reference_html":"Solution structure of the unbound, oxidized Photosystem I subunit PsaC, containing [4Fe-4S] clusters F(A) and F(B): a conformational change occurs upon binding to photosystem I. <i> Antonkine ML, Liu G, Bentrop D, Bryant DA, Bertini I, Luchinat C, Golbeck JH, Stehlik D. </i> J Biol Inorg Chem, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP00935r010","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":80,"term_name":"ion binding","start":68,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"11941504","version":3,"reference_html":"Solution structure of the unbound, oxidized Photosystem I subunit PsaC, containing [4Fe-4S] clusters F(A) and F(B): a conformational change occurs upon binding to photosystem I. <i> Antonkine ML, Liu G, Bentrop D, Bryant DA, Bertini I, Luchinat C, Golbeck JH, Stehlik D. </i> J Biol Inorg Chem, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0043167","ec_id":"ECO:0006165","region_id":"DP00935r011","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P31087","date":"2016-09-06T10:39:58.000Z","acc":"P31087","name":"Photosystem I iron-sulfur center","length":81,"organism":"Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6)","dataset":[],"UniParc":"UPI000011323E","genes":[{"name":{"value":"psaC"},"olnNames":[{"value":"SYNPCC7002_A1589"}]}],"alphafold_very_low_content":0,"disorder_content":0.30864197530864196,"disprot_consensus":{"full":[{"start":47,"end":58,"type":"T"},{"start":68,"end":80,"type":"D"}],"Structural state":[{"start":47,"end":58,"type":"D"},{"start":68,"end":80,"type":"D"}],"Molecular function":[{"start":47,"end":58,"type":"F"},{"start":68,"end":80,"type":"F"}],"Structural transition":[{"start":47,"end":58,"type":"T"}]}},{"features":{"pfam":[{"id":"PF02191","name":"Olfactomedin-like domain","start":224,"end":477},{"id":"PF12308","name":"Neurogenesis glycoprotein","start":55,"end":152}]},"uniref50":"UniRef50_O88998","sequence":"MSVPLLKIGVVLSTMAMITNWMSQTLPSLVGLNTTRLSAASGGTLDRSTGVLPTNPEESWQVYSSAQDSEGRCICTVVAPQQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETKFKQVEESHKQHLARQFKAIKAKMDELRPLIPVLEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLACGKLTGISDPVTVKTSGSRFGSWMTDPLAPEGDNRVWYMDGYHNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQVVYNGSIYFNKFQSHIIIRFDLKTEAILKTRSLDYAGYNNMYHYAWGGHSDIDLMVDENGLWAVYATNQNAGNIVISKLDPVSLQILQTWNTSYPKRSAGEAFIICGTLYVTNGYSGGTKVHYAYQTNASTYEYIDIPFQNKYSHISMLDYNPKDRALYAWNNGHQTLYNVTLFHVIRSDEL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_O88998","disprot_id":"DP00936","ncbi_taxon_id":10090,"regions_counter":2,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":352,"region_id":"DP00936r001","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Olfactomedin-1 Has a V-shaped Disulfide-linked Tetrameric Structure. <i> Pronker MF, Bos TG, Sharp TH, Thies-Weesie DM, Janssen BJ. </i> J Biol Chem, 2015","term_id":"IDPO:0000002","curator_id":"vnugnes","start":339,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-22T20:29:09.273Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5AMO"}],"reference_id":"25903135","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"506227","entry_name":"N-acetyl-D-glucosamine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":"glycerol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":null}],"statement":[{"text":"A large portion, 209 residues of a total of 463 residues for the mature full-length protein, is missing in the electron density most likely due to α-chymotrypsin treatment of Olfm1. The final model consists of residues Val211–Phe477 and Arg210–Ala480 (the last two alanines Ala479 and Ala480 are from the NotI restriction site) for chains A and B, respectively, excluding loops Ala339–His352 in both chains.","type":"Methods"}]}],"released":"2016_10","uniref100":"UniRef100_O88998","date":"2016-09-06T11:30:08.000Z","acc":"O88998","name":"Noelin","length":485,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000029EA7","genes":[{"name":{"value":"Olfm1"},"synonyms":[{"value":"Noe1"},{"value":"Noel"},{"value":"Noel1"}]}],"alphafold_very_low_content":0.12783505154639174,"disorder_content":0.0288659793814433,"disprot_consensus":{"full":[{"start":339,"end":352,"type":"D"}],"Structural state":[{"start":339,"end":352,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00498","name":"FHA domain","start":49,"end":118}],"gene3D":[{"start":1,"end":132,"id":"2.60.200.20","name":"2.60.200.20"}]},"uniref50":"UniRef50_Q12972","sequence":"MAAAANSGSSLPLFDCPTWAGKPPPGLHLDVVKGDKLIEKLIIDEKKYYLFGRNPDLCDFTIDHQSCSRVHAALVYHKHLKRVFLIDLNSTHGTFLGHIRLEPHKPQQIPIDSTVSFGASTRAYTLREKPQTLPSAVKGDEKMGGEDDELKGLLGLPEEETELDNLTEFNTAHNKRISTLTIEEGNLDIQRPKRKRKNSRVTFSEDDEIINPEDVDPSVGRFRNMVQTAVVPVKKKRVEGPGSLGLEESGSRRMQNFAFSGGLYGGLPPTHSEAGSQPHGIHGTALIGGLPMPYPNLAPDVDLTPVVPSAVNMNPAPNPAVYNPEAVNEPKKKKYAKEAWPGKKPTPSLLI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q12972","disprot_id":"DP00937","ncbi_taxon_id":9606,"regions_counter":6,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":225,"region_id":"DP00937r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The molecular basis for substrate specificity of the nuclear NIPP1:PP1 holoenzyme. <i> O'Connell N, Nichols SR, Heroes E, Beullens M, Bollen M, Peti W, Page R. </i> Structure, 2012","term_id":"IDPO:0000002","curator_id":"eschad","start":144,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"BMRB","id":"18198"}],"reference_id":"22940584","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":225,"term_name":"molecular function inhibitor activity","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The molecular basis for substrate specificity of the nuclear NIPP1:PP1 holoenzyme. <i> O'Connell N, Nichols SR, Heroes E, Beullens M, Bollen M, Peti W, Page R. </i> Structure, 2012","term_id":"GO:0140678","curator_id":"eschad","start":144,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"22940584","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00937r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":225,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The molecular basis for substrate specificity of the nuclear NIPP1:PP1 holoenzyme. <i> O'Connell N, Nichols SR, Heroes E, Beullens M, Bollen M, Peti W, Page R. </i> Structure, 2012","term_id":"GO:0005515","curator_id":"eschad","start":144,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"22940584","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00937r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":198,"region_id":"DP00937r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The molecular basis for substrate specificity of the nuclear NIPP1:PP1 holoenzyme. <i> O'Connell N, Nichols SR, Heroes E, Beullens M, Bollen M, Peti W, Page R. </i> Structure, 2012","term_id":"IDPO:0000002","curator_id":"eschad","start":185,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3V4Y"}],"reference_id":"22940584","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":198,"term_name":"molecular function inhibitor activity","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"The molecular basis for substrate specificity of the nuclear NIPP1:PP1 holoenzyme. <i> O'Connell N, Nichols SR, Heroes E, Beullens M, Bollen M, Peti W, Page R. </i> Structure, 2012","term_id":"GO:0140678","curator_id":"eschad","start":185,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"22940584","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00937r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":198,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"The molecular basis for substrate specificity of the nuclear NIPP1:PP1 holoenzyme. <i> O'Connell N, Nichols SR, Heroes E, Beullens M, Bollen M, Peti W, Page R. </i> Structure, 2012","term_id":"GO:0005515","curator_id":"eschad","start":185,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"22940584","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00937r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q12972","date":"2016-09-06T12:32:12.000Z","acc":"Q12972","name":"Nuclear inhibitor of protein phosphatase 1","length":351,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000002B181","genes":[{"name":{"value":"PPP1R8"},"synonyms":[{"value":"ARD1"},{"value":"NIPP1"}]}],"alphafold_very_low_content":0.28774928774928776,"disorder_content":0.2336182336182336,"disprot_consensus":{"full":[{"start":144,"end":225,"type":"D"}],"Structural state":[{"start":144,"end":225,"type":"D"}],"Molecular function":[{"start":144,"end":225,"type":"F"}]}},{"acc":"P04859","sequence":"MDQDAFILKEDSEVEREAPGGRESLSDVIGFLDAVLSSEPTDIGGDRSWLHNTINTPQGPGSAHRAKSEGEGEVSTPSTQDNRSGEESRVSGRTSKPEAEAHAGNLDKQNIHRAFGGRTGTNSVSQDLGDGGDSGILENPPNERGYPRSGIEDENREMAAHPDKRGEDQAEGLPEEVRGGTSLPDEGEGGASNNGRSMEPGSSHSARVTGVLVIPSPELEEAVLRRNKRRPTNSGSKPLTPATVPGTRSPPLNRYNSTGSPPGKPPSTQDEHINSGDTPAVRVKDRKPPIGTRSVSDCPANGRPIHPGLESDSTKKGIGENTSSMKEMATLLTSLGVIQSAQEFESSRDASYVFARRALKSANYAEMTFNVCGLILSAEKSSARKVDENKQLLKQIQESVESFRDIYKRFSEYQKEQNSLLMSNLSTLHIITDRGGKTDNTDSLTRSPSVFAKSKENKTKATRFDPSMETLEDMKYKPDLIREDEFRDEIRNPVYQERDTEPRASNASRLLPSKEKPTMHSLRLVIESSPLSRAEKAAYVKSLSKCKTDQEVKAVMELVEEDIESLTN","creator":"slonghi","dataset":["Viral proteins"],"date":"2016-09-06T13:40:53.000Z","disprot_id":"DP00939","features":{"pfam":[{"id":"PF01806","name":"Paramyxovirinae P phosphoprotein C-terminal region","start":328,"end":564}],"gene3D":[{"start":382,"end":433,"id":"1.10.287.340","name":"1.10.287.340","_id":"685af523b4ac24d5329d8863"},{"start":319,"end":381,"id":"1.10.287.320","name":"Viral phosphoprotein oligmorisation site domain","_id":"685af523b4ac24d5329d8864"},{"start":516,"end":568,"id":"1.10.8.10","name":"DNA helicase RuvA subunit, C-terminal domain","_id":"685af523b4ac24d5329d8865"}]},"genes":[{"name":{"value":"P/V/C","evidences":[],"_id":"685af523b4ac24d5329d889c"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d889b"}],"length":568,"name":"Phosphoprotein","ncbi_taxon_id":11196,"organism":"Sendai virus (strain Harris)","regions_counter":14,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Paramyxoviridae","Orthoparamyxovirinae","Respirovirus"],"UniParc":"UPI0000134B7E","uniref100":"UniRef100_P04859","uniref50":"UniRef50_P04859","uniref90":"UniRef90_P04859","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1R4G","_id":"685af523b4ac24d5329d886c"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":474,"end":515,"interaction_partner":[],"reference_html":"Structure and dynamics of the nucleocapsid-binding domain of the Sendai virus phosphoprotein in solution. <i> Blanchard L, Tarbouriech N, Blackledge M, Timmins P, Burmeister WP, Ruigrok RW, Marion D. </i> Virology, 2004","reference_id":"14980481","region_id":"DP00939r003","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"We show that this small protein presents two subdomains linked by an 11-residue linker, with the N-subdomain lacking a well-defined conformation.","_id":"685af523b4ac24d5329d886d"},{"type":"Results","text":"To supplement the structural characterisation of PX, we measured heteronuclear relaxation at 600 MHz. Of the 95 amino acid residues (474–568), 68 {1H}-15N nOes (Fig. 3), 68 R1 and 68 R2 (data not shown) could be measured. The resulting data confirm that residues 474–515 indeed present differential dynamic behaviour compared to residues 516–568. In particular, the {1H}-15N nOe reveals a rigid domain (516–568) linked to a flexible domain (474–504) by an even more flexible linker (505–515).","_id":"685af523b4ac24d5329d886e"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-29T13:23:29.809Z","_id":"685af523b4ac24d5329d886f"},"version":3,"_id":"685af523b4ac24d5329d886b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":474,"end":515,"interaction_partner":[],"reference_html":"A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering. <i> Bernadó P, Blanchard L, Timmins P, Marion D, Ruigrok RW, Blackledge M. </i> Proc Natl Acad Sci U S A, 2005","reference_id":"16284250","region_id":"DP00939r005","released":"2022_03","sample":[],"statement":[{"type":"Conclusion","text":"This model is validated by experimental RDCs and SAXS data measured from PX from Sendai virus, a molecule containing folded and unfolded domains, confirming both local conformational sampling and the average size and shape of the ensemble. Despite the highly disperse ensemble, regions of preferential structuring along the flexible chain of PX are detected.","_id":"685af523b4ac24d5329d8874"},{"type":"Results","text":"In this study, experimental RDCs and SAXS data are combined with a conformational sampling algorithm to develop a structural model of the 57-aa unfolded domain of PX. Although they cover a smaller range than the RDCs measured in the folded domain, the N-NH and C′-NH RDC measured for PX aligned in 5% of C12E6/hexanol nevertheless present identifiable fine structure and values that are non-negligible compared with the folded domain.","_id":"685af523b4ac24d5329d8875"},{"type":"Curator statement","text":"57-aa including the 15 residues of the His-tag.","_id":"685af523b4ac24d5329d8876"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-29T13:16:25.707Z","_id":"685af523b4ac24d5329d8877"},"version":3,"_id":"685af523b4ac24d5329d8873","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"4999","_id":"685af523b4ac24d5329d8880"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":474,"end":517,"interaction_partner":[],"reference_html":"Assignment of the 1H, 15N and 13C resonances of the nucleocapsid-binding domain of the Sendai virus phosphoprotein. <i> Marion D, Tarbouriech N, Ruigrok RW, Burmeister WP, Blanchard L. </i> J Biomol NMR, 2001","reference_id":"11693574","region_id":"DP00939r009","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"The assignment of this small protein has been made difficult due to the limited amount of regular secondary structure (the N-terminus before Pro58 is disordered) shown by chemical shift data and the absence of medium and long-range NOEs.","_id":"685af523b4ac24d5329d8881"},{"type":"Methods","text":"An isotopically 15N/13C double-labelled sample of the X protein spanning amino acids 474 to 568 of the phosphoprotein (accession number swiss-prot P04859) (corresponding respectively to residue 15 and 109 in our numbering scheme) was obtained from 4 L E. coli BL21 (DE3) culture in M9 minimal medium containing 1 g/l 15NH4Cl and 1 g/l 13C6-glucose as sole nitrogen and carbon sources.","_id":"685af523b4ac24d5329d8882"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-29T13:16:07.498Z","_id":"685af523b4ac24d5329d8883"},"version":1,"_id":"685af523b4ac24d5329d887f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"4999","_id":"685af523b4ac24d5329d8885"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":474,"end":517,"interaction_partner":[],"reference_html":"Assignment of the 1H, 15N and 13C resonances of the nucleocapsid-binding domain of the Sendai virus phosphoprotein. <i> Marion D, Tarbouriech N, Ruigrok RW, Burmeister WP, Blanchard L. </i> J Biomol NMR, 2001","reference_id":"11693574","region_id":"DP00939r010","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"The assignment of this small protein has been made difficult due to the limited amount of regular secondary structure (the N-terminus before Pro58 is disordered) shown by chemical shift data and the absence of medium and long-range NOEs. This suggests that a flexible linker is needed between the oligomerisation domain/polymerase binding site and the N-RNA binding domain for biological activity.","_id":"685af523b4ac24d5329d8886"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-29T13:24:57.860Z","_id":"685af523b4ac24d5329d8887"},"version":1,"_id":"685af523b4ac24d5329d8884","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":474,"end":518,"interaction_partner":[],"reference_html":"Intrinsic dynamics of the partly unstructured PX domain from the Sendai virus RNA polymerase cofactor P. <i> Houben K, Blanchard L, Blackledge M, Marion D. </i> Biophys J, 2007","reference_id":"17586564","region_id":"DP00939r011","released":"2022_03","sample":[],"statement":[{"type":"Figure","text":" (A) Overall rotational correlation time τc. Isotropic rotational diffusion with a correlation time of 7.3 ns was assumed for the structured part (519–568), whereas a local diffusion model was used for residues in the unstructured part.","_id":"685af523b4ac24d5329d8889"},{"type":"Methods","text":"Isotope-labeled samples of the PX domain (474–568) of SeV phosphoprotein P, including an N-terminal His tag and a factor Xa cleavage site (MRGSHHHHHHIEGR), were prepared as described previously (30).","_id":"685af523b4ac24d5329d888a"},{"type":"Results","text":"All amide protons in the N-terminal part of PX exchanged within the dead time confirming the unstructured nature of this N-terminal subdomain.","_id":"685af523b4ac24d5329d888b"},{"type":"Curator statement","text":"From 474 to 518 is unstructured and from 519 to 568 structured.","_id":"685af523b4ac24d5329d888c"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-29T13:15:03.005Z","_id":"685af523b4ac24d5329d888d"},"version":1,"_id":"685af523b4ac24d5329d8888","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":504,"end":508,"interaction_partner":[],"reference_html":"Intrinsic dynamics of the partly unstructured PX domain from the Sendai virus RNA polymerase cofactor P. <i> Houben K, Blanchard L, Blackledge M, Marion D. </i> Biophys J, 2007","reference_id":"17586564","region_id":"DP00939r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The two alanines A-504 and A-507 both have high negative normalized order parameters. They are located in the stretch (504–508), which from the backbone 15N relaxation data was identified as a very flexible linker between the unstructured and structured domain; and this highly flexible character is clearly also sensed by the alanine Cα-Cβ axis. All other normalized order parameters in the unstructured part are also negative, meaning that the methyl groups are more flexible than on average in structured proteins.","_id":"685af523b4ac24d5329d888f"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-29T13:24:58.720Z","_id":"685af523b4ac24d5329d8890"},"version":1,"_id":"685af523b4ac24d5329d888e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1R4G","_id":"685af523b4ac24d5329d8892"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":505,"end":515,"interaction_partner":[],"reference_html":"Structure and dynamics of the nucleocapsid-binding domain of the Sendai virus phosphoprotein in solution. <i> Blanchard L, Tarbouriech N, Blackledge M, Timmins P, Burmeister WP, Ruigrok RW, Marion D. </i> Virology, 2004","reference_id":"14980481","region_id":"DP00939r013","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"We show that this small protein presents two subdomains linked by an 11-residue linker, with the N-subdomain lacking a well-defined conformation.","_id":"685af523b4ac24d5329d8893"},{"type":"Results","text":"To supplement the structural characterisation of PX, we measured heteronuclear relaxation at 600 MHz. Of the 95 amino acid residues (474–568), 68 {1H}-15N nOes (Fig. 3), 68 R1 and 68 R2 (data not shown) could be measured. The resulting data confirm that residues 474–515 indeed present differential dynamic behaviour compared to residues 516–568. In particular, the {1H}-15N nOe reveals a rigid domain (516–568) linked to a flexible domain (474–504) by an even more flexible linker (505–515).","_id":"685af523b4ac24d5329d8894"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-29T13:24:44.379Z","_id":"685af523b4ac24d5329d8895"},"version":1,"_id":"685af523b4ac24d5329d8891","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":474,"end":515,"interaction_partner":[],"reference_html":"A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering. <i> Bernadó P, Blanchard L, Timmins P, Marion D, Ruigrok RW, Blackledge M. </i> Proc Natl Acad Sci U S A, 2005","reference_id":"16284250","region_id":"DP00939r014","released":"2022_03","sample":[],"statement":[{"type":"Conclusion","text":"This model is validated by experimental RDCs and SAXS data measured from PX from Sendai virus, a molecule containing folded and unfolded domains, confirming both local conformational sampling and the average size and shape of the ensemble. Despite the highly disperse ensemble, regions of preferential structuring along the flexible chain of PX are detected.","_id":"685af523b4ac24d5329d8897"},{"type":"Results","text":"In this study, experimental RDCs and SAXS data are combined with a conformational sampling algorithm to develop a structural model of the 57-aa unfolded domain of PX. Although they cover a smaller range than the RDCs measured in the folded domain, the N-NH and C′-NH RDC measured for PX aligned in 5% of C12E6/hexanol nevertheless present identifiable fine structure and values that are non-negligible compared with the folded domain.","_id":"685af523b4ac24d5329d8898"},{"type":"Curator statement","text":"57-aa including the 15 residues of the His-tag.","_id":"685af523b4ac24d5329d8899"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-29T13:14:02.507Z","_id":"685af523b4ac24d5329d889a"},"version":1,"_id":"685af523b4ac24d5329d8896","reference_source":"pmid"}],"__v":0,"disorder_content":0.07922535211267606,"disprot_consensus":{"full":[{"start":474,"end":518,"type":"D"}],"Structural state":[{"start":474,"end":518,"type":"D"}],"Disorder function":[{"start":474,"end":517,"type":"F"}]}},{"features":{"pfam":[{"id":"PF30854","name":"Par-4 C-terminal domain","start":264,"end":332},{"id":"PF30855","name":"Par-4 SAC region","start":139,"end":198}]},"uniref50":"UniRef50_Q62627","sequence":"MATGGYRSSGSTTDFLEEWKAKREKMRAKQNPVGPGSSGGDPAAKSPAGPLAQTTAAGTSELNHGPAGAAAPAAPGPGALNCAHGSSALPRGAPGSRRPEDECPIAAGAAGAPASRGDEEEPDSAPEKGRSSGPSARKGKGQIEKRKLREKRRSTGVVNIPAAECLDEYEDDEAGQKERKREDAITQQNTIQNEAASLPDPGTSYLPQDPSRTVPGRYKSTISAPEEEILNRYPRTDRSGFSRHNRDTSAPANFASSSTLEKRIEDLEKEVLRERQENLRLTRLMQDKEEMIGKLKEEIDLLNRDLDDMEDENEQLKQENKTLLKVVGQLTR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_Q62627","disprot_id":"DP00940","ncbi_taxon_id":10116,"regions_counter":2,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":332,"region_id":"DP00940r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Intrinsic disorder and coiled-coil formation in prostate apoptosis response factor 4. <i> Libich DS, Schwalbe M, Kate S, Venugopal H, Claridge JK, Edwards PJ, Dutta K, Pascal SM. </i> FEBS J, 2009","term_id":"IDPO:0000002","curator_id":"eschad","start":1,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19490121","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":290,"region_id":"DP00940r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Intrinsic disorder and coiled-coil formation in prostate apoptosis response factor 4. <i> Libich DS, Schwalbe M, Kate S, Venugopal H, Claridge JK, Edwards PJ, Dutta K, Pascal SM. </i> FEBS J, 2009","term_id":"IDPO:0000002","curator_id":"eschad","start":1,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19490121","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q62627","date":"2016-09-06T15:23:43.000Z","acc":"Q62627","name":"PRKC apoptosis WT1 regulator protein","length":332,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI00000E5F94","genes":[{"name":{"value":"Pawr"},"synonyms":[{"value":"Par4"}]}],"alphafold_very_low_content":0.4427710843373494,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":332,"type":"D"}],"Structural state":[{"start":1,"end":332,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00443","name":"Ubiquitin carboxyl-terminal hydrolase","start":214,"end":518},{"id":"PF12436","name":"ICP0-binding domain of Ubiquitin-specific protease 7","start":620,"end":865},{"id":"PF14533","name":"Ubiquitin-specific protease C-terminal","start":875,"end":1086},{"id":"PF22486","name":"MATH domain","start":70,"end":194}],"gene3D":[{"start":63,"end":210,"id":"2.60.210.10","name":"Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A"},{"start":211,"end":523,"id":"3.90.70.10","name":"Cysteine proteinases"},{"start":677,"end":792,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"},{"start":535,"end":664,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"},{"start":793,"end":889,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"}]},"uniref50":"UniRef50_Q93009","sequence":"MNHQQQQQQQKAGEQQLSEPEDMEMEAGDTDDPPRITQNPVINGNVALSDGHNTAEEDMEDDTSWRSEATFQFTVERFSRLSESVLSPPCFVRNLPWKIMVMPRFYPDRPHQKSVGFFLQCNAESDSTSWSCHAQAVLKIINYRDDEKSFSRRISHLFFHKENDWGFSNFMAWSEVTDPEKGFIDDDKVTFEVFVQADAPHGVAWDSKKHTGYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPLALQRVFYELQHSDKPVGTKKLTKSFGWETLDSFMQHDVQELCRVLLDNVENKMKGTCVEGTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKGKKNIFESFVDYVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMYDPQTDQNIKINDRFEFPEQLPLDEFLQKTDPKDPANYILHAVLVHSGDNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHDDDLSVRHCTNAYMLVYIRESKLSEVLQAVTDHDIPQQLVERLQEEKRIEAQKRKERQEAHLYMQVQIVAEDQFCGHQGNDMYDEEKVKYTVFKVLKNSSLAEFVQSLSQTMGFPQDQIRLWPMQARSNGTKRPAMLDNEADGNKTMIELSDNENPWTIFLETVDPELAASGATLPKFDKDHDVMLFLKMYDPKTRSLNYCGHIYTPISCKIRDLLPVMCDRAGFIQDTSLILYEEVKPNLTERIQDYDVSLDKALDELMDGDIIVFQKDDPENDNSELPTAKEYFRDLYHRVDVIFCDKTIPNDPGFVVTLSNRMNYFQVAKTVAQRLNTDPMLLQFFKSQGYRDGPGNPLRHNYEGTLRDLLQFFKPRQPKKLYYQQLKMKITDFENRRSFKCIWLNSQFREEEITLYPDKHGCVRDLLEECKKAVELGEKASGKLRLLEIVSYKIIGVHQEDELLECLSPATSRTFRIEEIPLDQVDIDKENEMLVTVAHFHKEVFGTFGIPFLLRIHQGEHFREVMKRIQSLLDIQEKEFEKFKFAIVMMGRHQYINEDEYEVNLKDFEPQPGNMSHPRPWLGLDHFNKAPKRSRYTYLEKAIKIHN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q93009","disprot_id":"DP00941","ncbi_taxon_id":9606,"regions_counter":8,"creator":"aelofsson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":64,"region_id":"DP00941r003","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Structure of the p53 binding domain of HAUSP/USP7 bound to Epstein-Barr nuclear antigen 1 implications for EBV-mediated immortalization. <i> Saridakis V, Sheng Y, Sarkari F, Holowaty MN, Shire K, Nguyen T, Zhang RG, Liao J, Lee W, Edwards AM, Arrowsmith CH, Frappier L. </i> Mol Cell, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":54,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15808506","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-05-24T16:19:21.516Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1YZE"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The amino terminus and four loops are completely disordered.","type":"Methods"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":187,"region_id":"DP00941r004","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Structure of the p53 binding domain of HAUSP/USP7 bound to Epstein-Barr nuclear antigen 1 implications for EBV-mediated immortalization. <i> Saridakis V, Sheng Y, Sarkari F, Holowaty MN, Shire K, Nguyen T, Zhang RG, Liao J, Lee W, Edwards AM, Arrowsmith CH, Frappier L. </i> Mol Cell, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":174,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15808506","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-05-24T16:17:23.403Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1YZE"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The amino terminus and four loops are completely disordered.","type":"Methods"}]},{"start":105,"end":114,"reference_id":"15808506","reference_source":"pmid","reference_html":"Structure of the p53 binding domain of HAUSP/USP7 bound to Epstein-Barr nuclear antigen 1 implications for EBV-mediated immortalization. <i> Saridakis V, Sheng Y, Sarkari F, Holowaty MN, Shire K, Nguyen T, Zhang RG, Liao J, Lee W, Edwards AM, Arrowsmith CH, Frappier L. </i> Mol Cell, 2005","date":"2023-05-24T16:20:03.161Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1YZE"}],"region_id":"DP00941r005","statement":[{"text":"The amino terminus and four loops are completely disordered.","type":"Methods"}]},{"start":174,"end":187,"reference_id":"15808506","reference_source":"pmid","reference_html":"Structure of the p53 binding domain of HAUSP/USP7 bound to Epstein-Barr nuclear antigen 1 implications for EBV-mediated immortalization. <i> Saridakis V, Sheng Y, Sarkari F, Holowaty MN, Shire K, Nguyen T, Zhang RG, Liao J, Lee W, Edwards AM, Arrowsmith CH, Frappier L. </i> Mol Cell, 2005","date":"2023-05-24T16:24:52.663Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1YZE"},{"db":"PDB","id":"1YY6"}],"region_id":"DP00941r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P03211"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:923"}],"statement":[{"text":"In crystals generated by the USP7-EBNA1 complex, lattice contacts were not observed in the peptide binding region but were confined to the loops connecting the β strands (amino acids 77, 80, and 82 interacted with residues 178, 180, and 181).","type":"Methods"},{"text":"Upon USP7-EBNA1 complex formation this region becomes structures, as shown in the PDB 1YY6.","type":"Curator statement"}]},{"start":500,"end":509,"reference_id":"16402859","reference_source":"pmid","reference_html":"Structural basis of competitive recognition of p53 and MDM2 by HAUSP/USP7: implications for the regulation of the p53-MDM2 pathway. <i> Hu M, Gu L, Li M, Jeffrey PD, Gu W, Shi Y. </i> PLoS Biol, 2006","date":"2023-05-24T16:35:36.503Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2F1Z"}],"region_id":"DP00941r007","statement":[{"text":"PDB structure shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":1084,"end":1102,"reference_id":"26210801","reference_source":"pmid","reference_html":"Molecular mechanism for the substrate recognition of USP7. <i> Cheng J, Li Z, Gong R, Fang J, Yang Y, Sun C, Yang H, Xu Y. </i> Protein Cell, 2015","date":"2023-05-24T16:40:32.882Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5C56"}],"region_id":"DP00941r008","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08393"}],"statement":[{"text":"PDB structure of USP7/HAUSP in complex with ICP0 shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"released":"2016_10","uniref100":"UniRef100_Q93009","date":"2016-09-06T15:29:48.000Z","acc":"Q93009","name":"Ubiquitin carboxyl-terminal hydrolase 7","length":1102,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI000003AEBA","genes":[{"name":{"value":"USP7","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12093161","url":"http://www.ncbi.nlm.nih.gov/pubmed/12093161","alternativeUrl":"https://europepmc.org/abstract/MED/12093161"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:12630","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:12630"}}]},"synonyms":[{"value":"HAUSP","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9034339","url":"http://www.ncbi.nlm.nih.gov/pubmed/9034339","alternativeUrl":"https://europepmc.org/abstract/MED/9034339"}}]}]}],"alphafold_very_low_content":0.06987295825771325,"disorder_content":0.05807622504537205,"disprot_consensus":{"full":[{"start":54,"end":64,"type":"D"},{"start":105,"end":114,"type":"D"},{"start":174,"end":187,"type":"T"},{"start":500,"end":509,"type":"D"},{"start":1084,"end":1102,"type":"D"}],"Structural state":[{"start":54,"end":64,"type":"D"},{"start":105,"end":114,"type":"D"},{"start":174,"end":187,"type":"D"},{"start":500,"end":509,"type":"D"},{"start":1084,"end":1102,"type":"D"}],"Structural transition":[{"start":174,"end":187,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00234","name":"Protease inhibitor/seed storage/LTP family","start":47,"end":136}],"gene3D":[{"start":34,"end":145,"id":"1.10.110.10","name":"Plant lipid-transfer and hydrophobic proteins"}]},"uniref50":"UniRef50_Q6PSU2","sequence":"MAKSTILVALLALVLVAHASAMRRERGRQGDSSSCERQVDRVNLKPCEQHIMQRIMGEQEQYDSYDIRSTRSSDQQQRCCDELNEMENTQRCMCEALQQIMENQCDRLQDRQMVQQFKRELMNLPQQCNFRAPQRCDLDVSGGRC","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","fabids","Fabales","Fabaceae","Papilionoideae","50 kb inversion clade","dalbergioids sensu lato","Dalbergieae","Pterocarpus clade","Arachis"],"uniref90":"UniRef90_Q647G9","disprot_id":"DP00942","ncbi_taxon_id":3818,"regions_counter":5,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":34,"region_id":"DP00942r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions. <i> Lehmann K, Schweimer K, Reese G, Randow S, Suhr M, Becker WM, Vieths S, Rösch P. </i> Biochem J, 2006","term_id":"IDPO:0000002","curator_id":"nmurvai","start":22,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"16372900","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1W2Q"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":71,"region_id":"DP00942r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions. <i> Lehmann K, Schweimer K, Reese G, Randow S, Suhr M, Becker WM, Vieths S, Rösch P. </i> Biochem J, 2006","term_id":"IDPO:0000002","curator_id":"nmurvai","start":57,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"16372900","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1W2Q"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":145,"region_id":"DP00942r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions. <i> Lehmann K, Schweimer K, Reese G, Randow S, Suhr M, Becker WM, Vieths S, Rösch P. </i> Biochem J, 2006","term_id":"IDPO:0000002","curator_id":"nmurvai","start":129,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"16372900","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1W2Q"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q647G9","date":"2016-09-06T16:04:28.000Z","acc":"Q647G9","name":"Conglutin","length":145,"organism":"Arachis hypogaea","dataset":[],"UniParc":"UPI00004406A9","genes":[],"alphafold_very_low_content":0.0896551724137931,"disorder_content":0.3103448275862069,"disprot_consensus":{"full":[{"start":22,"end":34,"type":"D"},{"start":57,"end":71,"type":"D"},{"start":129,"end":145,"type":"D"}],"Structural state":[{"start":22,"end":34,"type":"D"},{"start":57,"end":71,"type":"D"},{"start":129,"end":145,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00595","name":"PDZ domain","start":498,"end":578},{"id":"PF17817","name":"PDZ domain","start":426,"end":489}],"gene3D":[{"start":475,"end":583,"id":"2.30.42.10","name":"2.30.42.10"}]},"uniref50":"UniRef50_O35274","sequence":"MMKTEPRGPGGPLRSASPHRSAYEAGIQALKPPDAPGPDEAPKAAHHKKYGSNVHRIKSMFLQMGTTTGPPGEAGGASGMAEAPRASDRGVRLSLPRASSLNENVDHSALLKLGTSVSERVSRFDSKPAPSAQPAPPPHPPSRLQETRKLFERSVPAASGGDKEAVARRLLRQERASLQDRKLDVVVRFNGSTEALDKLDADAVSPTVSQLSAVFEKADSRTGLHRAPGPPRAAGAPQVNSKLVTKRSRVFQPPPPPPAPSGDAATEKDRGPGGQQPPQHRVAPARPPPKPREVRKIKPVEVEESGESEAESAPGEVIQAEVTVHAALENGSTTATTASPAPEEPKAEAVPEEEASSSVATLERGVDNGRAPDMAPEEVDESKKEDFSEADLVDVSAYSGLGEDSGGSALEEDDEEDEEDGEPPYEPESGCVEIPGLSEEEDPAPSRKIHFSTAPIQVFSTYSNEDYDRRNEDVDPMAASAEYELEKRVERLELFPVELEKDSEGLGISIIGMGAGADMGLEKLGIFVKTVTEGGAAHRDGRIQVNDLLVEVDGTSLVGVTQSFAASVLRNTKGRVRFMIGRERPGEQSEVAQLIQQTLEQERWQREMMEQRYAQYGEDDEETGEYATDEDEELSPTFPGGEMAIEVFELAENEDALSPVEMEPEKLVHKFKELQIKHAVTEAEIQQLKRKLQSLEQEKGRWRVEKAQLEQSVEENKERMEKLEGYWGEAQSLCQAVDEHLRETQAQYQALERKYSKAKRLIKDYQQKEIEFLKKETAQRRVLEESELARKEEMDKLLDKISELEGNLQTLRNSNST","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_O35274","disprot_id":"DP00943","ncbi_taxon_id":10116,"regions_counter":8,"creator":"stama","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":494,"region_id":"DP00943r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites. <i> Ragusa MJ, Dancheck B, Critton DA, Nairn AC, Page R, Peti W. </i> Nat Struct Mol Biol, 2010","term_id":"IDPO:0000002","curator_id":"eschad","start":417,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"BMRB","id":"15180"}],"reference_id":"20305656","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":602,"region_id":"DP00943r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis for spinophilin-neurabin receptor interaction. <i> Kelker MS, Dancheck B, Ju T, Kessler RP, Hudak J, Nairn AC, Peti W. </i> Biochemistry, 2007","term_id":"IDPO:0000002","curator_id":"eschad","start":584,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2G5M"},{"db":"BMRB","id":"6927"}],"reference_id":"17279777","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":602,"term_name":"flexible linker","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis for spinophilin-neurabin receptor interaction. <i> Kelker MS, Dancheck B, Ju T, Kessler RP, Hudak J, Nairn AC, Peti W. </i> Biochemistry, 2007","term_id":"IDPO:0000033","curator_id":"eschad","start":584,"term_ontology":"IDPO","curator_name":"Eva Schad","reference_id":"17279777","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00943r003","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":154,"region_id":"DP00943r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure-function analysis of the filamentous actin binding domain of the neuronal scaffolding protein spinophilin. <i> Schüler H, Peti W. </i> FEBS J, 2008","term_id":"IDPO:0000002","curator_id":"ahatos","start":1,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18028445","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":154,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structure-function analysis of the filamentous actin binding domain of the neuronal scaffolding protein spinophilin. <i> Schüler H, Peti W. </i> FEBS J, 2008","term_id":"GO:0005515","curator_id":"ahatos","start":1,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"18028445","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00943r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":154,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structure-function analysis of the filamentous actin binding domain of the neuronal scaffolding protein spinophilin. <i> Schüler H, Peti W. </i> FEBS J, 2008","term_id":"GO:0003676","curator_id":"ahatos","start":1,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"18028445","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00943r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":154,"region_id":"DP00943r007","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structure-function analysis of the filamentous actin binding domain of the neuronal scaffolding protein spinophilin. <i> Schüler H, Peti W. </i> FEBS J, 2008","term_id":"IDPO:0000002","curator_id":"ahatos","start":1,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18028445","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":154,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Structure-function analysis of the filamentous actin binding domain of the neuronal scaffolding protein spinophilin. <i> Schüler H, Peti W. </i> FEBS J, 2008","term_id":"GO:0005515","curator_id":"ahatos","start":1,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"18028445","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00943r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_O35274","date":"2016-09-06T16:14:59.000Z","acc":"O35274","name":"Neurabin-2","length":817,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI000012FEE7","genes":[{"name":{"value":"Ppp1r9b","evidences":[{"code":"ECO:0000312","source":{"name":"RGD","id":"632281","url":"https://rgd.mcw.edu/tools/genes/genes_view.cgi?id=632281"}}]},"synonyms":[{"value":"Spino","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15743906","url":"http://www.ncbi.nlm.nih.gov/pubmed/15743906","alternativeUrl":"https://europepmc.org/abstract/MED/15743906"}}]}]}],"alphafold_very_low_content":0.5006119951040392,"disorder_content":0.3072215422276622,"disprot_consensus":{"full":[{"start":1,"end":154,"type":"D"},{"start":417,"end":494,"type":"D"},{"start":584,"end":602,"type":"D"}],"Structural state":[{"start":1,"end":154,"type":"D"},{"start":417,"end":494,"type":"D"},{"start":584,"end":602,"type":"D"}],"Disorder function":[{"start":584,"end":602,"type":"F"}],"Molecular function":[{"start":1,"end":154,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01655","name":"Ribosomal protein L32","start":126,"end":231},{"id":"PF14520","name":"SAM-like Helix-hairpin-helix tandem","start":15,"end":65}],"gene3D":[{"start":5,"end":69,"id":"1.10.150.20","name":"5' to 3' exonuclease, C-terminal subdomain"}]},"uniref50":"UniRef50_P12736","sequence":"MADNEEDVEAEEEYTELTDISGVGPSKAESLREAGFESVEDVRGADQSALADVSGIGNALAARIKADVGGLEVESETEAEVEEEGGEEAPDEDVETELQARGLTEKTPDLSDEDARLLTQRHRVGKPQFNRQDHHKKKRVSTSWRKPRGQLSKQRRGIKGKGDTVEAGFRSPTAVRGKHPSGFEEVRVHNVDDLEGVDGDTEAVRIASKVGARKRERIEEEAEDAGIRVLNPTYVEVEVSE","taxonomy":["Archaea","Euryarchaeota","Stenosarchaea group","Halobacteria","Halobacteriales","Haloarculaceae","Haloarcula"],"uniref90":"UniRef90_P12736","disprot_id":"DP00944","ncbi_taxon_id":272569,"regions_counter":4,"creator":"smribeiro","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":95,"region_id":"DP00944r001","released":"2023_12","ec_id":"ECO:0006220","reference_html":"A pre-translocational intermediate in protein synthesis observed in crystals of enzymatically active 50S subunits. <i> Schmeing TM, Seila AC, Hansen JL, Freeborn B, Soukup JK, Scaringe SA, Strobel SA, Moore PB, Steitz TA. </i> Nat Struct Biol, 2002","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-23T13:38:14.063Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1KQS"}],"reference_id":"11828326","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The PDB structure of the Haloarcula marismortui 50S complexed with a pretranslocational intermediate in protein synthesis shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":95,"region_id":"DP00944r002","released":"2023_12","ec_id":"ECO:0006220","reference_html":"The kink-turn: a new RNA secondary structure motif. <i> Klein DJ, Schmeing TM, Moore PB, Steitz TA. </i> EMBO J, 2001","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-23T13:36:30.687Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1JJ2"}],"reference_id":"11483524","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The fully refined crystal structure of the Haloarcula marismortui Large Ribosomal Subunit shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":95,"region_id":"DP00944r003","released":"2023_12","ec_id":"ECO:0006220","reference_html":"The structures of four macrolide antibiotics bound to the large ribosomal subunit. <i> Hansen JL, Ippolito JA, Ban N, Nissen P, Moore PB, Steitz TA. </i> Mol Cell, 2002","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-23T13:34:34.077Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1K8A"},{"db":"PDB","id":"1M1K"},{"db":"PDB","id":"1KD1"},{"db":"PDB","id":"1K9M"}],"reference_id":"12150912","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The PDB structure of the 50S ribosomal subunit of Haloarcula marismortui bound to Spiramycinazi, thromycin, Carbomycin or A tylosin; shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":95,"region_id":"DP00944r004","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Structural insights into peptide bond formation. <i> Hansen JL, Schmeing TM, Moore PB, Steitz TA. </i> Proc Natl Acad Sci U S A, 2002","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-23T13:33:46.178Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1Q82"}],"reference_id":"12185246","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The PDB structure of CC-Puromycin bound to the A-site of the 50S ribosomal subunit shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"released":"2016_10","uniref100":"UniRef100_P12736","date":"2016-09-06T16:27:57.000Z","acc":"P12736","name":"50S ribosomal protein L32e","length":241,"organism":"Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)","dataset":["RNA-binding proteins"],"UniParc":"UPI00001120D4","genes":[{"name":{"value":"rpl32e"},"olnNames":[{"value":"rrnAC1595"}]}],"alphafold_very_low_content":0.1037344398340249,"disorder_content":0.3941908713692946,"disprot_consensus":{"full":[{"start":1,"end":95,"type":"D"}],"Structural state":[{"start":1,"end":95,"type":"D"}]}},{"acc":"P59595","sequence":"MSDNGPQSNQRSAPRITFGGPTDSTDNNQNGGRNGARPKQRRPQGLPNNTASWFTALTQHGKEELRFPRGQGVPINTNSGPDDQIGYYRRATRRVRGGDGKMKELSPRWYFYYLGTGPEASLPYGANKEGIVWVATEGALNTPKDHIGTRNPNNNAATVLQLPQGTTLPKGFYAEGSRGGSQASSRSSSRSRGNSRNSTPGSSRGNSPARMASGGGETALALLLLDRLNQLESKVSGKGQQQQGQTVTKKSAAEASKKPRQKRTATKQYNVTQAFGRRGPEQTQGNFGDQDLIRQGTDYKHWPQIAQFAPSASAFFGMSRIGMEVTPSGTWLTYHGAIKLDDKDPQFKDNVILLNKHIDAYKTFPPTEPKKDKKKKTDEAQPLPQRQKKQPTVTLLPAADMDDFSRQLQNSMSGASADSTQA","creator":"jbergier","dataset":["Viral proteins","RNA-binding proteins"],"date":"2016-09-06T16:56:25.000Z","disprot_id":"DP00948","features":{"pfam":[{"id":"PF00937","name":"Coronavirus nucleocapsid","start":46,"end":391}]},"genes":[{"name":{"value":"N","evidences":[{"source":{"id":"MF_04096","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04096","_id":"685af523b4ac24d5329d8960"},"code":"ECO:0000255","_id":"685af523b4ac24d5329d895f"}],"_id":"685af523b4ac24d5329d8961"},"synonyms":[],"olnNames":[],"orfNames":[{"value":"9a","evidences":[],"_id":"685af523b4ac24d5329d8962"}],"_id":"685af523b4ac24d5329d895e"}],"length":422,"name":"Nucleoprotein","ncbi_taxon_id":694009,"organism":"Human SARS coronavirus","regions_counter":42,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Nidovirales","Cornidovirineae","Coronaviridae","Orthocoronavirinae","Betacoronavirus","Sarbecovirus"],"UniParc":"UPI000018DB79","uniref100":"UniRef100_P59595","uniref50":"UniRef50_P0DTC9","uniref90":"UniRef90_P59595","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":44,"interaction_partner":[],"reference_html":"Modular organization of SARS coronavirus nucleocapsid protein. <i> Chang CK, Sue SC, Yu TH, Hsieh CM, Tsai CK, Chiang YC, Lee SJ, Hsiao HH, Wu WJ, Chang WL, Lin CH, Huang TH. </i> J Biomed Sci, 2006","reference_id":"16228284","region_id":"DP00948r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"SARS-CoV N protein contains three intrinsically disordered regions","_id":"685af523b4ac24d5329d88b0"},{"type":"Results","text":"In conjunction with the observation that all additional resonances are observed in between 8.3±0.5 ppm in the proton dimension and PONDR results, we conclude that aminoacids 1–44, 182–247 and 366–422 are disordered.","_id":"685af523b4ac24d5329d88b1"},{"type":"Results","text":"The spectrum of N1-181 is a superposition of well-dispersed resonances and a cluster of overlapping resonances   around 8.3±0.4 ppm (Figure 2b).","_id":"685af523b4ac24d5329d88b2"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-15T08:46:15.235Z","_id":"685af523b4ac24d5329d88b3"},"version":3,"_id":"685af523b4ac24d5329d88af","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":182,"end":247,"interaction_partner":[],"reference_html":"Modular organization of SARS coronavirus nucleocapsid protein. <i> Chang CK, Sue SC, Yu TH, Hsieh CM, Tsai CK, Chiang YC, Lee SJ, Hsiao HH, Wu WJ, Chang WL, Lin CH, Huang TH. </i> J Biomed Sci, 2006","reference_id":"16228284","region_id":"DP00948r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"SARS-CoV N protein contains three intrinsically disordered regions","_id":"685af523b4ac24d5329d88bb"},{"type":"Results","text":" In conjunction with the observation that all additional resonances are observed in between 8.3±0.5 ppm in the proton dimension and PONDR results, we conclude that amino acids 1–44, 182–247 and 366–422 are disordered.","_id":"685af523b4ac24d5329d88bc"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-15T08:46:09.672Z","_id":"685af523b4ac24d5329d88bd"},"version":4,"_id":"685af523b4ac24d5329d88ba","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":366,"end":422,"interaction_partner":[],"reference_html":"Modular organization of SARS coronavirus nucleocapsid protein. <i> Chang CK, Sue SC, Yu TH, Hsieh CM, Tsai CK, Chiang YC, Lee SJ, Hsiao HH, Wu WJ, Chang WL, Lin CH, Huang TH. </i> J Biomed Sci, 2006","reference_id":"16228284","region_id":"DP00948r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"SARS-CoV N protein contains three intrinsically disordered regions","_id":"685af523b4ac24d5329d88c5"},{"type":"Results","text":"In conjunction with the observation that all additional resonances are observed in between 8.3±0.5 ppm in the proton dimension and PONDR results, we conclude that amino acids 1–44, 182–247 and 366–422 are disordered.","_id":"685af523b4ac24d5329d88c6"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-15T08:46:07.774Z","_id":"685af523b4ac24d5329d88c7"},"version":4,"_id":"685af523b4ac24d5329d88c4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":182,"end":247,"interaction_partner":[],"reference_html":"Multiple nucleic acid binding sites and intrinsic disorder of severe acute respiratory syndrome coronavirus nucleocapsid protein: implications for ribonucleocapsid protein packaging. <i> Chang CK, Hsu YL, Chang YH, Chao FA, Wu MC, Huang YS, Hu CK, Huang TH. </i> J Virol, 2009","reference_id":"19052082","region_id":"DP00948r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Furthermore, size exclusion chromatography of NP45-247 shows that the protein elutes out of the column with a Stokes radius corresponding to a globular protein of 41 kDa (Fig.5B). The theoretical molecular mass of the construct is 22.9 kDa, suggesting that the NP45-247 construct has an elongated shape. This is in contrast to the NTD, which is mainly globular (13). We attribute this to residues 182 to 247 forming an extraneous “tail” that affects the hydrodynamic properties of the molecule. ","_id":"685af523b4ac24d5329d88cf"},{"type":"Results","text":"Taken together, our results are compatible with previous reports from this lab where the didomain construct NP45-365 was shown to have resonances in the disordered region of the spectrum without affecting resonances belonging to either structural domain (2). We conclude that the flexible linker (residues 182 to 247) forms a bona fide ID domain not affected by either structural domain in the context of the whole protein.","_id":"685af523b4ac24d5329d88d0"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-15T08:38:56.588Z","_id":"685af523b4ac24d5329d88d1"},"version":4,"_id":"685af523b4ac24d5329d88ce","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":182,"end":247,"interaction_partner":[],"reference_html":"Multiple nucleic acid binding sites and intrinsic disorder of severe acute respiratory syndrome coronavirus nucleocapsid protein: implications for ribonucleocapsid protein packaging. <i> Chang CK, Hsu YL, Chang YH, Chao FA, Wu MC, Huang YS, Hu CK, Huang TH. </i> J Virol, 2009","reference_id":"19052082","region_id":"DP00948r013","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Small-angle X-ray scattering data show that the protein is in an extended conformation and that the two structural domains of the SARS-CoV N protein are far apart. Both the NTD and the CTD have been shown to bind RNA. Here we show that all disordered regions are also capable of binding to RNA.","_id":"685af523b4ac24d5329d88d9"},{"type":"Results","text":"Data analysis showed that the radius of gyration of the NP45-365 dimer is 61 Å, much larger than expected for a 72-kDa globular protein ​(Fig.7B). This is consistent with the model that the NTD and CTD do not interact, and the two NTDs in the dimer are likely to float freely in solution","_id":"685af523b4ac24d5329d88da"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-15T08:38:32.434Z","_id":"685af523b4ac24d5329d88db"},"version":4,"_id":"685af523b4ac24d5329d88d8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2JW8","_id":"685af523b4ac24d5329d88e4"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":248,"end":259,"interaction_partner":[],"reference_html":"Solution structure of the c-terminal dimerization domain of SARS coronavirus nucleocapsid protein solved by the SAIL-NMR method. <i> Takeda M, Chang CK, Ikeya T, Güntert P, Chang YH, Hsu YL, Huang TH, Kainosho M. </i> J Mol Biol, 2008","reference_id":"18561946","region_id":"DP00948r016","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Second, the two N-termini (residues 248–259) protruding from the dimer core are disordered in the NMR structure, whereas, in the crystal structure, they are involved in a number of intramonomer and intradimer contacts and are more rigid (Fig. 4a). The disorder of the N-termini in solution was further supported by the analysis of backbone amide-exchange rates (data not shown). ","_id":"685af523b4ac24d5329d88e3"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-21T13:58:12.232Z","_id":"685af523b4ac24d5329d88e5"},"version":3,"_id":"685af523b4ac24d5329d88e2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":248,"end":259,"interaction_partner":[],"reference_html":"Solution structure of the c-terminal dimerization domain of SARS coronavirus nucleocapsid protein solved by the SAIL-NMR method. <i> Takeda M, Chang CK, Ikeya T, Güntert P, Chang YH, Hsu YL, Huang TH, Kainosho M. </i> J Mol Biol, 2008","reference_id":"18561946","region_id":"DP00948r017","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"To identify these residues, we conducted chemical shift displacement (CSD) studies by titrating 10-mer (dT10) or 20-mer (dT20) poly-deoxythymine (poly-dT) single-stranded DNA (ssDNA) into the protein samples. ssDNA were used throughout this study as surrogates of single-stranded RNA. Titration of dT10 or dT20 into the protein sample caused a concentration-dependent gradual shift of some resonances, instead of the appearance of a new set of resonances, suggesting that the binding occurs in the fast-exchange regime, which is indicative of a low-affinity nucleic-acid-binding protein.13 For dT10, significant chemical shift changes were localized primarily in the N-terminal region, particularly K250, E253, A254, S256, K257, and K258 (Fig. 6a and b), while the majority of the other resonances were scarcely affected. This result suggests that dT10 binds to the SARS-CoV NP at the N-terminal flexible segment, without affecting the overall structure of the protein (Fig. 4). The binding constant estimated from the CSD studies at various dT10 concentrations is Kd ∼ 30 μM.","_id":"685af523b4ac24d5329d88e7"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-15T10:16:07.960Z","_id":"685af523b4ac24d5329d88e8"},"version":4,"_id":"685af523b4ac24d5329d88e6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":248,"end":259,"interaction_partner":[],"reference_html":"Solution structure of the c-terminal dimerization domain of SARS coronavirus nucleocapsid protein solved by the SAIL-NMR method. <i> Takeda M, Chang CK, Ikeya T, Güntert P, Chang YH, Hsu YL, Huang TH, Kainosho M. </i> J Mol Biol, 2008","reference_id":"18561946","region_id":"DP00948r018","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"To identify these residues, we conducted chemical shift displacement (CSD) studies by titrating 10-mer (dT10) or 20-mer (dT20) poly-deoxythymine (poly-dT) single-stranded DNA (ssDNA) into the protein samples. ssDNA were used throughout this study as surrogates of single-stranded RNA. Titration of dT10 or dT20 into the protein sample caused a concentration-dependent gradual shift of some resonances, instead of the appearance of a new set of resonances, suggesting that the binding occurs in the fast-exchange regime, which is indicative of a low-affinity nucleic-acid-binding protein.13 For dT10, significant chemical shift changes were localized primarily in the N-terminal region, particularly K250, E253, A254, S256, K257, and K258 (Fig. 6a and b), while the majority of the other resonances were scarcely affected. This result suggests that dT10 binds to the SARS-CoV NP at the N-terminal flexible segment, without affecting the overall structure of the protein (Fig. 4). The binding constant estimated from the CSD studies at various dT10 concentrations is Kd ∼ 30 μM.","_id":"685af523b4ac24d5329d88ea"}],"states_connection":[],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_id":"GO:0003677","term_is_binding":true,"term_is_obsolete":false,"term_name":"DNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-15T09:33:07.417Z","_id":"685af523b4ac24d5329d88eb"},"version":5,"_id":"685af523b4ac24d5329d88e9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":182,"end":247,"interaction_partner":[],"reference_html":"Modular organization of SARS coronavirus nucleocapsid protein. <i> Chang CK, Sue SC, Yu TH, Hsieh CM, Tsai CK, Chiang YC, Lee SJ, Hsiao HH, Wu WJ, Chang WL, Lin CH, Huang TH. </i> J Biomed Sci, 2006","reference_id":"16228284","region_id":"DP00948r019","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The  long  disordered  linker  between  the  two structural domains is consistent with the observation that there is little interaction between the two domains.","_id":"685af523b4ac24d5329d88ed"},{"type":"Results","text":"The two structural domains are connected by a disordered linker and capped by disordered N-terminal head and C-terminal tail.","_id":"685af523b4ac24d5329d88ee"},{"type":"Results","text":"The lack of resonance perturbation when the two domains are linked together suggests that interaction between these two domains is weak, if they interact at all. Our results conclude that SARS-CoV N protein contains two independent structural domains located at a.a. 45–181 and 248–365.","_id":"685af523b4ac24d5329d88ef"},{"type":"Discussion","text":"The flexible linker between the two structural domains is largely disordered. This disordered region may enable transient interactions with several structurally distinct partners. It has been shown that the M protein of SARS-CoV binds to this region between a.a. 168–208 [16]. Interestingly, human cellular hnRNP A1 has also been shown to bind to almost the same region between a.a. 161–210 [17]. The disordered state of this region potentially allows it to interact with different partners depending on context, e.g. with the M protein during virus assembly and with hnRNP A1 during host cell infection.","_id":"685af523b4ac24d5329d88f0"},{"type":"Curator statement","text":"Flexible linker connecting the N-terminal RNA-binding domain (RBD) (residues 45–181) and the C-terminal dimerization domain (residues 248–365) (DD) of SARS-CoV Nucleoprotein.","_id":"685af523b4ac24d5329d88f1"}],"states_connection":[],"term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-15T10:16:02.693Z","_id":"685af523b4ac24d5329d88f2"},"version":4,"_id":"685af523b4ac24d5329d88ec","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006077","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","ec_ontology":"ECO","start":184,"end":196,"interaction_partner":[],"reference_html":"Analysis of multimerization of the SARS coronavirus nucleocapsid protein. <i> He R, Dobie F, Ballantine M, Leeson A, Li Y, Bastien N, Cutts T, Andonov A, Cao J, Booth TF, Plummer FA, Tyler S, Baker L, Li X. </i> Biochem Biophys Res Commun, 2004","reference_id":"15020242","region_id":"DP00948r021","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Furthermore, mutational analyses characterized that a serine/arginine-rich motif (SSRSSSRSRGNSR) between amino acids 184 and 196 is crucial for N protein oligomerization, since deletion of this region completely abolished the N protein self-multimerization.","_id":"685af523b4ac24d5329d88f8"},{"type":"Results","text":"As shown in Fig. 4C, deletion of the serine/arginine-rich region (aa 184–196) resulted in a complete loss of SEAP activities, suggesting these amino acids are required for N self-interaction. Finally, consistent with results in Fig. 2, no self-interaction was observed in the viral M proteins. Taken together, these results suggest that amino acids 184–196 are indispensable for multimerization of SARS-CoV nucleocapsid protein.","_id":"685af523b4ac24d5329d88f9"}],"states_connection":[],"term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-15T10:15:58.386Z","_id":"685af523b4ac24d5329d88fa"},"version":5,"_id":"685af523b4ac24d5329d88f7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":182,"end":247,"interaction_partner":[],"reference_html":"Multiple nucleic acid binding sites and intrinsic disorder of severe acute respiratory syndrome coronavirus nucleocapsid protein: implications for ribonucleocapsid protein packaging. <i> Chang CK, Hsu YL, Chang YH, Chao FA, Wu MC, Huang YS, Hu CK, Huang TH. </i> J Virol, 2009","reference_id":"19052082","region_id":"DP00948r023","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Comparing the HSQC spectrum of NP45-247 with that of the NTD (NP45-181) in Fig.5A, we observed additional resonances in the spectrum of NP45-247 clustered in the 7.5- to 8.5-ppm range on the proton chemical shift. This strongly suggests that the additional residues from aa 182 to 247 of NP45-247 are disordered. ","_id":"685af523b4ac24d5329d8900"},{"type":"Results","text":"Taken together, our results are compatible with previous reports from this lab where the didomain construct NP45-365 was shown to have resonances in the disordered region of the spectrum without affecting resonances belonging to either structural domain (2). We conclude that the flexible linker (residues 182 to 247) forms a bona fide ID domain not affected by either structural domain in the context of the whole protein.","_id":"685af523b4ac24d5329d8901"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-15T08:34:30.081Z","_id":"685af523b4ac24d5329d8902"},"version":4,"_id":"685af523b4ac24d5329d88ff","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-09T08:12:00.729Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001807","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":44,"interaction_partner":[{"db":"ENA","id":"CS608005.1:1..21:misc_RNA.1","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d890c"}],"reference_html":"Multiple nucleic acid binding sites and intrinsic disorder of severe acute respiratory syndrome coronavirus nucleocapsid protein: implications for ribonucleocapsid protein packaging. <i> Chang CK, Hsu YL, Chang YH, Chao FA, Wu MC, Huang YS, Hu CK, Huang TH. </i> J Virol, 2009","reference_id":"19052082","region_id":"DP00948r025","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Both the NTD and the CTD have been shown to bind RNA. Here we show that all disordered regions are also capable of binding to RNA. Constructs containing multiple RNA-binding regions showed Hill coefficients greater than 1, suggesting that the N protein binds to RNA cooperatively. The current results underscore the important roles of multisite nucleic acid binding and intrinsic disorder in N protein function and RNP packaging.","_id":"685af523b4ac24d5329d8908"},{"type":"Introduction","text":"Here we tested all three disordered regions of the SARS-CoV N protein and found that they are all involved in RNA binding. The central region, in particular, had a large impact on binding behavior as monitored by electrophoretic mobility shift assays (EMSA).","_id":"685af523b4ac24d5329d8909"},{"type":"Results","text":"Figure 3 shows that inclusion of either the first 44 residues (aa 1 to 44) or the central flexible linker (residues 182 to 247) of the SARS-CoV N protein increases the apparent binding affinity for 20-mer poly(U) ssRNA three- to fourfold over that of the NTD (residues 45 to 181) alone. Inclusion of the flexible linker not only increases the apparent affinity; it also has a large effect on the apparent Hill coefficient. Similar results are obtained when either the central flexible linker or the C-terminal 54 residues (residues 366 to 422) are included in the construct of the CTD (residues 248 to 365), as shown in ​Fig.4. The increase in apparent binding affinity is even more pronounced (six- to eightfold), probably due to the dimeric nature of the CTD, which has two attached disordered regions, whereas the NTD has one.","_id":"685af523b4ac24d5329d890a"},{"type":"Results","text":"Taken together, a common trend is quickly apparent: inclusion of the disordered regions enhances the binding affinity of any particular construct. Of particular interest is the central flexible linker, which not only increases the binding affinity but also greatly enhances the Hill coefficients of the constructs.","_id":"685af523b4ac24d5329d890b"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_id":"GO:0003723","term_is_binding":true,"term_is_obsolete":false,"term_name":"RNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-08-12T14:48:25.586Z","_id":"685af523b4ac24d5329d890d"},"version":6,"_id":"685af523b4ac24d5329d8907","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-09T08:11:45.561Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001807","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","ec_ontology":"ECO","start":182,"end":247,"interaction_partner":[{"db":"ENA","id":"CS608005.1:1..21:misc_RNA.1","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8913"}],"reference_html":"Multiple nucleic acid binding sites and intrinsic disorder of severe acute respiratory syndrome coronavirus nucleocapsid protein: implications for ribonucleocapsid protein packaging. <i> Chang CK, Hsu YL, Chang YH, Chao FA, Wu MC, Huang YS, Hu CK, Huang TH. </i> J Virol, 2009","reference_id":"19052082","region_id":"DP00948r026","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Both the NTD and the CTD have been shown to bind RNA. Here we show that all disordered regions are also capable of binding to RNA. Constructs containing multiple RNA-binding regions showed Hill coefficients greater than 1, suggesting that the N protein binds to RNA cooperatively. The current results underscore the important roles of multisite nucleic acid binding and intrinsic disorder in N protein function and RNP packaging.","_id":"685af523b4ac24d5329d890f"},{"type":"Introduction","text":"Here we tested all three disordered regions of the SARS-CoV N protein and found that they are all involved in RNA binding. The central region, in particular, had a large impact on binding behavior as monitored by electrophoretic mobility shift assays (EMSA).","_id":"685af523b4ac24d5329d8910"},{"type":"Results","text":"Figure 3 shows that inclusion of either the first 44 residues (aa 1 to 44) or the central flexible linker (residues 182 to 247) of the SARS-CoV N protein increases the apparent binding affinity for 20-mer poly(U) ssRNA three- to fourfold over that of the NTD (residues 45 to 181) alone. Inclusion of the flexible linker not only increases the apparent affinity; it also has a large effect on the apparent Hill coefficient. Similar results are obtained when either the central flexible linker or the C-terminal 54 residues (residues 366 to 422) are included in the construct of the CTD (residues 248 to 365), as shown in ​Fig.4. The increase in apparent binding affinity is even more pronounced (six- to eightfold), probably due to the dimeric nature of the CTD, which has two attached disordered regions, whereas the NTD has one.","_id":"685af523b4ac24d5329d8911"},{"type":"Results","text":"Taken together, a common trend is quickly apparent: inclusion of the disordered regions enhances the binding affinity of any particular construct. Of particular interest is the central flexible linker, which not only increases the binding affinity but also greatly enhances the Hill coefficients of the constructs.","_id":"685af523b4ac24d5329d8912"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_id":"GO:0003723","term_is_binding":true,"term_is_obsolete":false,"term_name":"RNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-08-12T14:48:25.123Z","_id":"685af523b4ac24d5329d8914"},"version":6,"_id":"685af523b4ac24d5329d890e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-09T08:11:15.569Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001807","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","ec_ontology":"ECO","start":366,"end":422,"interaction_partner":[{"db":"ENA","id":"CS608005.1:1..21:misc_RNA.1","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d891a"}],"reference_html":"Multiple nucleic acid binding sites and intrinsic disorder of severe acute respiratory syndrome coronavirus nucleocapsid protein: implications for ribonucleocapsid protein packaging. <i> Chang CK, Hsu YL, Chang YH, Chao FA, Wu MC, Huang YS, Hu CK, Huang TH. </i> J Virol, 2009","reference_id":"19052082","region_id":"DP00948r027","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Both the NTD and the CTD have been shown to bind RNA. Here we show that all disordered regions are also capable of binding to RNA. Constructs containing multiple RNA-binding regions showed Hill coefficients greater than 1, suggesting that the N protein binds to RNA cooperatively. The current results underscore the important roles of multisite nucleic acid binding and intrinsic disorder in N protein function and RNP packaging.","_id":"685af523b4ac24d5329d8916"},{"type":"Introduction","text":"Here we tested all three disordered regions of the SARS-CoV N protein and found that they are all involved in RNA binding. The central region, in particular, had a large impact on binding behavior as monitored by electrophoretic mobility shift assays (EMSA)","_id":"685af523b4ac24d5329d8917"},{"type":"Results","text":"Figure 3 shows that inclusion of either the first 44 residues (aa 1 to 44) or the central flexible linker (residues 182 to 247) of the SARS-CoV N protein increases the apparent binding affinity for 20-mer poly(U) ssRNA three- to fourfold over that of the NTD (residues 45 to 181) alone. Inclusion of the flexible linker not only increases the apparent affinity; it also has a large effect on the apparent Hill coefficient. Similar results are obtained when either the central flexible linker or the C-terminal 54 residues (residues 366 to 422) are included in the construct of the CTD (residues 248 to 365), as shown in ​Fig.4. The increase in apparent binding affinity is even more pronounced (six- to eightfold), probably due to the dimeric nature of the CTD, which has two attached disordered regions, whereas the NTD has one. ","_id":"685af523b4ac24d5329d8918"},{"type":"Results","text":"Taken together, a common trend is quickly apparent: inclusion of the disordered regions enhances the binding affinity of any particular construct. Of particular interest is the central flexible linker, which not only increases the binding affinity but also greatly enhances the Hill coefficients of the constructs.","_id":"685af523b4ac24d5329d8919"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_id":"GO:0003723","term_is_binding":true,"term_is_obsolete":false,"term_name":"RNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-08-12T14:48:49.358Z","_id":"685af523b4ac24d5329d891b"},"version":6,"_id":"685af523b4ac24d5329d8915","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":46,"interaction_partner":[],"reference_html":"Ribonucleocapsid formation of severe acute respiratory syndrome coronavirus through molecular action of the N-terminal domain of N protein. <i> Saikatendu KS, Joseph JS, Subramanian V, Neuman BW, Buchmeier MJ, Stevens RC, Kuhn P. </i> J Virol, 2007","reference_id":"17229691","region_id":"DP00948r040","released":"2022_03","sample":[],"statement":[{"type":"Methods","text":"Multiple constructs were designed covering different regions of ORF9a from Tor2 strain of SARS-CoV as part of the structural and functional proteomics of SARS-CoV (FSPS) project. Domain boundaries were arrived at based on secondary structure predictions, earlier observations made in the literature regarding proteolytic susceptibility, and sequence conservation characteristics.","_id":"685af523b4ac24d5329d8954"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2020-12-02T15:01:26.479Z","_id":"685af523b4ac24d5329d8953"},"version":2,"_id":"685af523b4ac24d5329d8952","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001807","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","ec_ontology":"ECO","start":366,"end":382,"interaction_partner":[],"reference_html":"Carboxyl terminus of severe acute respiratory syndrome coronavirus nucleocapsid protein: self-association analysis and nucleic acid binding characterization. <i> Luo H, Chen J, Chen K, Shen X, Jiang H. </i> Biochemistry, 2006","reference_id":"17002283","region_id":"DP00948r041","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Gel shift assay results revealed that the SARS-CoV N protein C-terminus is also able to associate with nucleic acids and residues 363-382 are the responsible interaction partner, demonstrating that this fragment might involve genomic RNA binding sites.","_id":"685af523b4ac24d5329d8956"},{"type":"Results","text":"As shown in Figure 7, N303-422, N283-402, and N283-382 could associate with ssDNA and migrate into the gel; however, the removal of a further 20 and 40 amino acids, generating N263-362 and N243-343 (Figure 3A), caused the proteins to lose the capability of binding to ssDNA. The ability of interacting with ssDNA was restored for N343-422 (Figure 3A), as N283-422. These results thus indicated that residues 363-382 are responsible for nucleic acid binding of the SARS-CoV N protein carboxyl terminus.","_id":"685af523b4ac24d5329d8957"},{"type":"Curator statement","text":"Binding to DNA is used as a probe for nucleic acid binding, but the \"natural\" binder is RNA.","_id":"685af523b4ac24d5329d8958"}],"states_connection":[],"term_comment":"Note that this term is restricted to those cases where the binding is to a single-stranded DNA molecule, not to one of the stands of double-stranded DNA.","term_def":"\"Binding to single-stranded DNA.\" [GOC:elh, GOC:vw, PMID:22976174]","term_id":"GO:0003697","term_is_binding":true,"term_is_obsolete":false,"term_name":"single-stranded DNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-15T09:06:56.299Z","_id":"685af523b4ac24d5329d8959"},"version":1,"_id":"685af523b4ac24d5329d8955","reference_source":"pmid"}],"__v":0,"disorder_content":0.42890995260663506,"disprot_consensus":{"full":[{"start":1,"end":46,"type":"D"},{"start":182,"end":259,"type":"D"},{"start":366,"end":422,"type":"D"}],"Structural state":[{"start":1,"end":46,"type":"D"},{"start":182,"end":259,"type":"D"},{"start":366,"end":422,"type":"D"}],"Molecular function":[{"start":1,"end":44,"type":"F"},{"start":182,"end":259,"type":"F"},{"start":366,"end":422,"type":"F"}],"Disorder function":[{"start":182,"end":247,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02854","name":"MIF4G domain","start":168,"end":335},{"id":"PF02854","name":"MIF4G domain","start":571,"end":758},{"id":"PF02854","name":"MIF4G domain","start":777,"end":986},{"id":"PF04050","name":"Up-frameshift suppressor 2","start":1094,"end":1218}],"gene3D":[{"start":540,"end":757,"id":"1.25.40.180","name":"1.25.40.180"},{"start":117,"end":428,"id":"1.25.40.180","name":"1.25.40.180"},{"start":768,"end":1015,"id":"1.25.40.180","name":"1.25.40.180"}]},"uniref50":"UniRef50_Q9HAU5","sequence":"MPAERKKPASMEEKDSLPNNKEKDCSERRTVSSKERPKDDIKLTAKKEVSKAPEDKKKRLEDDKRKKEDKERKKKDEEKVKAEEESKKKEEEEKKKHQEEERKKQEEQAKRQQEEEAAAQMKEKEESIQLHQEAWERHHLRKELRSKNQNAPDSRPEENFFSRLDSSLKKNTAFVKKLKTITEQQRDSLSHDFNGLNLSKYIAEAVASIVEAKLKISDVNCAVHLCSLFHQRYADFAPSLLQVWKKHFEARKEEKTPNITKLRTDLRFIAELTIVGIFTDKEGLSLIYEQLKNIINADRESHTHVSVVISFCRHCGDDIAGLVPRKVKSAAEKFNLSFPPSEIISPEKQQPFQNLLKEYFTSLTKHLKRDHRELQNTERQNRRILHSKGELSEDRHKQYEEFAMSYQKLLANSQSLADLLDENMPDLPQDKPTPEEHGPGIDIFTPGKPGEYDLEGGIWEDEDARNFYENLIDLKAFVPAILFKDNEKSCQNKESNKDDTKEAKESKENKEVSSPDDLELELENLEINDDTLELEGGDEAEDLTKKLLDEQEQEDEEASTGSHLKLIVDAFLQQLPNCVNRDLIDKAAMDFCMNMNTKANRKKLVRALFIVPRQRLDLLPFYARLVATLHPCMSDVAEDLCSMLRGDFRFHVRKKDQINIETKNKTVRFIGELTKFKMFTKNDTLHCLKMLLSDFSHHHIEMACTLLETCGRFLFRSPESHLRTSVLLEQMMRKKQAMHLDARYVTMVENAYYYCNPPPAEKTVKKKRPPLQEYVRKLLYKDLSKVTTEKVLRQMRKLPWQDQEVKDYVICCMINIWNVKYNSIHCVANLLAGLVLYQEDVGIHVVDGVLEDIRLGMEVNQPKFNQRRISSAKFLGELYNYRMVESAVIFRTLYSFTSFGVNPDGSPSSLDPPEHLFRIRLVCTILDTCGQYFDRGSSKRKLDCFLVYFQRYVWWKKSLEVWTKDHPFPIDIDYMISDTLELLRPKIKLCNSLEESIRQVQDLEREFLIKLGLVNDKDSKDSMTEGENLEEDEEEEEGGAETEEQSGNESEVNEPEEEEGSDNDDDEGEEEEEENTDYLTDSNKENETDEENTEVMIKGGGLKHVPCVEDEDFIQALDKMMLENLQQRSGESVKVHQLDVAIPLHLKSQLRKGPPLGGGEGEAESADTMPFVMLTRKGNKQQFKILNVPMSSQLAANHWNQQQAEQEERMRMKKLTLDINERQEQEDYQEMLQSLAQRPAPANTNRERRPRYQHPKGAPNADLIFKTGGRRR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9HAU5","disprot_id":"DP00949","ncbi_taxon_id":9606,"regions_counter":26,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1129,"region_id":"DP00949r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Unusual bipartite mode of interaction between the nonsense-mediated decay factors, UPF1 and UPF2. <i> Clerici M, Mourão A, Gutsche I, Gehring NH, Hentze MW, Kulozik A, Kadlec J, Sattler M, Cusack S. </i> EMBO J, 2009","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1105,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-06-21T13:10:04.353Z","reference_source":"pmid","term_name":"disorder","reference_id":"19556969","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"To further characterize the bipartite binding region in UPF2, which interacts with UPF1, NMR spectra were recorded using two synthetic peptides, corresponding to the helical (residues 1105–1129) and β-hairpin (residues 1167–1207) motifs of UPF2, and to 15N-labelled UPF1 (115–287).","type":"Results"},{"text":"NMR measurements on the β-hairpin peptide show that it also unfolded in solution, whereas the helix peptide shows some NOEs that indicate a fractional population of helical conformation (data not shown).","type":"Results"}]},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":1129,"term_name":"disorder to order","released":"2023_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Unusual bipartite mode of interaction between the nonsense-mediated decay factors, UPF1 and UPF2. <i> Clerici M, Mourão A, Gutsche I, Gehring NH, Hentze MW, Kulozik A, Kadlec J, Sattler M, Cusack S. </i> EMBO J, 2009","term_id":"IDPO:0000011","curator_id":"vnugnes","start":1105,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19556969","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-06-21T13:30:34.076Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00949r003","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92900"}],"statement":[{"text":"Finally, the NMR spectrum of the free 15N-UPF2(1105–1207) shows that the protein is present in an almost completely unfolded state in solution and folding is observed on addition of UPF1(115–287) (Supplementary Figure S9D).","type":"Results"},{"text":"Altogether, these data confirm that UPF2 used a disordered bipartite motif that couples UPF1 binding to folding of the two interacting elements, with the β-hairpin element having the stronger interaction.","type":"Results"}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1129,"term_name":"protein binding","released":"2023_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Unusual bipartite mode of interaction between the nonsense-mediated decay factors, UPF1 and UPF2. <i> Clerici M, Mourão A, Gutsche I, Gehring NH, Hentze MW, Kulozik A, Kadlec J, Sattler M, Cusack S. </i> EMBO J, 2009","term_id":"GO:0005515","curator_id":"vnugnes","start":1105,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"19556969","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-06-21T13:14:46.332Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00949r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q92900","operator":"and","partner_start":115,"partner_end":287}],"statement":[{"text":"To further characterize the bipartite binding region in UPF2, which interacts with UPF1, NMR spectra were recorded using two synthetic peptides, corresponding to the helical (residues 1105–1129) and β-hairpin (residues 1167–1207) motifs of UPF2, and to 15N-labelled UPF1 (115–287). As expected, both peptides bind to different regions in UPF1 (Figure 4B and C).","type":"Results"},{"text":"On binding of the UPF2 helix peptide, residues Leu193, Ile233, Val161 and Val157 in UPF1 show large chemical-shift perturbations, consistent with the interactions seen in the crystal structure (Figure 4B).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1207,"region_id":"DP00949r005","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Unusual bipartite mode of interaction between the nonsense-mediated decay factors, UPF1 and UPF2. <i> Clerici M, Mourão A, Gutsche I, Gehring NH, Hentze MW, Kulozik A, Kadlec J, Sattler M, Cusack S. </i> EMBO J, 2009","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1167,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19556969","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-06-21T13:09:04.193Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"NMR spectra of the unbound peptide (residues 1167–1207) indicate that it is unstructured in solution (see below).","type":"Results"},{"text":"NMR measurements on the β-hairpin peptide show that it also unfolded in solution, whereas the helix peptide shows some NOEs that indicate a fractional population of helical conformation (data not shown).","type":"Results"}]},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":1207,"term_name":"disorder to order","start":1167,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19556969","version":3,"reference_html":"Unusual bipartite mode of interaction between the nonsense-mediated decay factors, UPF1 and UPF2. <i> Clerici M, Mourão A, Gutsche I, Gehring NH, Hentze MW, Kulozik A, Kadlec J, Sattler M, Cusack S. </i> EMBO J, 2009","date":"2023-06-21T13:35:16.395Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP00949r007","ec_go":"EXP","disprot_namespace":"Structural transition","curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92900"}],"statement":[{"text":"Finally, the NMR spectrum of the free 15N-UPF2(1105–1207) shows that the protein is present in an almost completely unfolded state in solution and folding is observed on addition of UPF1(115–287) (Supplementary Figure S9D).","type":"Results"},{"text":"Altogether, these data confirm that UPF2 used a disordered bipartite motif that couples UPF1 binding to folding of the two interacting elements, with the β-hairpin element having the stronger interaction.","type":"Results"}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":1207,"term_name":"protein binding","start":1167,"ec_name":"x-ray crystallography evidence used in manual assertion","curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"19556969","version":4,"reference_html":"Unusual bipartite mode of interaction between the nonsense-mediated decay factors, UPF1 and UPF2. <i> Clerici M, Mourão A, Gutsche I, Gehring NH, Hentze MW, Kulozik A, Kadlec J, Sattler M, Cusack S. </i> EMBO J, 2009","date":"2023-06-21T10:18:58.177Z","term_id":"GO:0005515","ec_id":"ECO:0005670","region_id":"DP00949r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"2WJV"}],"curator_orcid":"0000-0001-8399-7907","interaction_partner":[{"db":"UniProt","id":"Q92900","operator":"and","partner_start":115,"partner_end":925}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"}],"statement":[{"text":"On the other side of the CH-domain, the UPF2 β-hairpin is inserted between loops L10 and L7, which form another hydrophobic surface involving residues Leu176, Tyr184, Phe196, Trp241, Leu242 and the region 204-VVVL-207 (Figure 2D and Supplementary Figure S7B). The main interactions involve UPF2 residues from strand βA, including Leu1174, which contacts UPF1 residues Tyr184, Val204 and Val206, and Phe1171, which interacts with Val205. Met1173 is buried in the centre of the interface, notably contacting Phe196. Residues Leu1186, Val1188, Pro1189 and Leu1194, belonging to the UPF2 strand βB, contact Trp241 of UPF1 loop L10.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1166,"region_id":"DP00949r009","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Unusual bipartite mode of interaction between the nonsense-mediated decay factors, UPF1 and UPF2. <i> Clerici M, Mourão A, Gutsche I, Gehring NH, Hentze MW, Kulozik A, Kadlec J, Sattler M, Cusack S. </i> EMBO J, 2009","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1130,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-06-21T10:31:23.574Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2WJV"}],"reference_id":"19556969","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92900"}],"statement":[{"text":"In this structure, both the helical and β-hairpin segments of UPF2 have good and unambiguous electron density (Figure 1A, Supplementary Figure S1), although the linker between the two is only poorly defined.","type":"Results"},{"text":"Consistent with previous analyses (Meszaros et al, 2007), the disordered linker (residues 1130–1167) between the α-helical and β-hairpin of UPF2 is highly divergent in sequence and length compared with the interacting regions (Figure 2E).","type":"Discussion"}]},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":1166,"term_name":"flexible linker","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Unusual bipartite mode of interaction between the nonsense-mediated decay factors, UPF1 and UPF2. <i> Clerici M, Mourão A, Gutsche I, Gehring NH, Hentze MW, Kulozik A, Kadlec J, Sattler M, Cusack S. </i> EMBO J, 2009","term_id":"IDPO:0000033","curator_id":"vnugnes","start":1130,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19556969","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-06-21T10:31:10.236Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00949r010","ec_go":"EXP","disprot_namespace":"Disorder function","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92900"}],"statement":[{"text":"In this structure, both the helical and β-hairpin segments of UPF2 have good and unambiguous electron density (Figure 1A, Supplementary Figure S1), although the linker between the two is only poorly defined.","type":"Results"},{"text":"Consistent with previous analyses (Meszaros et al, 2007), the disordered linker (residues 1130–1167) between the α-helical and β-hairpin of UPF2 is highly divergent in sequence and length compared with the interacting regions (Figure 2E).","type":"Discussion"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":486,"region_id":"DP00949r012","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Structural and functional analysis of the three MIF4G domains of nonsense-mediated decay factor UPF2. <i> Clerici M, Deniaud A, Boehm V, Gehring NH, Schaffitzel C, Cusack S. </i> Nucleic Acids Res, 2014","term_id":"IDPO:0000002","curator_id":"vnugnes","start":430,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24271394","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-05-24T14:13:20.926Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4CEM"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":404,"end":404,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":424,"end":424,"position":"Specific residue"}],"curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Residues 430–486 at the C-terminus of the MIF4G-1 crystallization construct are disordered in the crystal structure.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":536,"region_id":"DP00949r013","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Structural and functional analysis of the three MIF4G domains of nonsense-mediated decay factor UPF2. <i> Clerici M, Deniaud A, Boehm V, Gehring NH, Schaffitzel C, Cusack S. </i> Nucleic Acids Res, 2014","term_id":"IDPO:0000002","curator_id":"vnugnes","start":481,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24271394","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-05-24T14:15:09.726Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4CEK"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Residues 481–558 following helix hB are largely disordered in the crystal structure (apart from the short helix hC) and indeed this region is highly variable between species (Supplementary Figure S2).","type":"Results"}]},{"start":1025,"end":1078,"reference_id":"https://mobidb.org/Q9HAU5","reference_source":"mobidb","reference_html":"An Entry Referenced from MobiDB","date":"2022-02-14T09:00:00.000Z","curator_id":"amonzon","curator_name":"Alex Monzon","curator_orcid":"0000-0003-0362-8218","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007759","ec_ontology":"ECO","ec_name":"curator inference from database used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP00949r014","statement":[{"text":"This poly-E region is inferred by the curator to be disordered, based on MobiDB-Lite and according to experimental evidence demonstrating that poly-E repeats display random-coil-like conformation (PMID:16949547)","type":"Curator statement"}],"ec_go":"IC","disprot_namespace":"Structural state"},{"start":757,"end":767,"reference_id":"24271394","reference_source":"pmid","reference_html":"Structural and functional analysis of the three MIF4G domains of nonsense-mediated decay factor UPF2. <i> Clerici M, Deniaud A, Boehm V, Gehring NH, Schaffitzel C, Cusack S. </i> Nucleic Acids Res, 2014","date":"2023-05-24T14:24:09.969Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00949r015","statement":[{"text":"The domains are connected via a short 11-amino acid-long linker (residues 757–767), which stretches the 23 Å distance between the C-terminus of MIF4G domain 2 and the N-terminus of MIF4G domain 3.","type":"Results"},{"text":"The dotted line represents the 10 residues linking h10 of MIF4G-2 to h1 of MIF4G-3.","type":"Figure"}]},{"start":757,"end":767,"reference_id":"24271394","reference_source":"pmid","reference_html":"Structural and functional analysis of the three MIF4G domains of nonsense-mediated decay factor UPF2. <i> Clerici M, Deniaud A, Boehm V, Gehring NH, Schaffitzel C, Cusack S. </i> Nucleic Acids Res, 2014","date":"2023-05-24T14:24:23.089Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00949r016","statement":[{"text":"The domains are connected via a short 11-amino acid-long linker (residues 757–767), which stretches the 23 Å distance between the C-terminus of MIF4G domain 2 and the N-terminus of MIF4G domain 3.","type":"Results"},{"text":"The dotted line represents the 10 residues linking h10 of MIF4G-2 to h1 of MIF4G-3.","type":"Figure"}]},{"start":1042,"end":1050,"reference_id":"24271394","reference_source":"pmid","reference_html":"Structural and functional analysis of the three MIF4G domains of nonsense-mediated decay factor UPF2. <i> Clerici M, Deniaud A, Boehm V, Gehring NH, Schaffitzel C, Cusack S. </i> Nucleic Acids Res, 2014","date":"2023-05-24T14:34:44.579Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00949r017","statement":[{"text":"Three SMG1 phosphorylation sites were identified (Supplementary Table S2): Ser886, Ser992 and Thr1042, Ser1046 or Ser1050.","type":"Results"},{"text":"Moreover, mutation of all five Ser/Thr led to a similar phosphorylation signal as the single S1046A mutant (Figure 6D), indicating that Ser1046 is the main phosphosite for SMG1 in the UPF2 MIF4G-3 construct (residues 761–1054), which we used as substrate in our assays.","type":"Results"}]},{"start":1207,"end":1227,"reference_id":"19556969","reference_source":"pmid","reference_html":"Unusual bipartite mode of interaction between the nonsense-mediated decay factors, UPF1 and UPF2. <i> Clerici M, Mourão A, Gutsche I, Gehring NH, Hentze MW, Kulozik A, Kadlec J, Sattler M, Cusack S. </i> EMBO J, 2009","date":"2023-05-24T15:21:41.903Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00949r018","statement":[{"text":"The additional NMR signals corresponding to the last 20 residues of the larger UPF2 construct have chemical shifts that are consistent with an unstructured peptide chain (Supplementary Figure S9C). ","type":"Results"}]},{"start":1167,"end":1207,"reference_id":"19556969","reference_source":"pmid","reference_html":"Unusual bipartite mode of interaction between the nonsense-mediated decay factors, UPF1 and UPF2. <i> Clerici M, Mourão A, Gutsche I, Gehring NH, Hentze MW, Kulozik A, Kadlec J, Sattler M, Cusack S. </i> EMBO J, 2009","date":"2023-05-24T15:30:18.530Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q92900","operator":null,"partner_start":115,"partner_end":287}],"region_id":"DP00949r019","statement":[{"text":"α-helix (1105–1129) shows the weaker binding with a Kd of 92 μM, whereas β-hairpin (1167–1207) has an ∼sixfold higher affinity with a Kd of 16 μM (Supplementary Figure S10).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1171,"end":1176,"reference_id":"19556969","reference_source":"pmid","reference_html":"Unusual bipartite mode of interaction between the nonsense-mediated decay factors, UPF1 and UPF2. <i> Clerici M, Mourão A, Gutsche I, Gehring NH, Hentze MW, Kulozik A, Kadlec J, Sattler M, Cusack S. </i> EMBO J, 2009","date":"2023-05-24T15:33:04.855Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe171Glu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met173Glu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu1174Glu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg1176Glu","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q92900","operator":null,"partner_start":115,"partner_end":287}],"region_id":"DP00949r020","statement":[{"text":"Mutations of β-hairpin hydrophobic residues Phe1171E, Met1173E and Leu1174E have very severe effects on the UPF1–UPF2 interaction, completely impairing UPF1 retention by UPF2. Mutation of Arg1176 (R1176E) also has an effect on complex formation. The Arg1176 side chain interacts with Tyr184 of UPF1, which, when mutated, also disrupts complex formation (Kadlec et al, 2006).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1171,"end":1176,"reference_id":"19556969","reference_source":"pmid","reference_html":"Unusual bipartite mode of interaction between the nonsense-mediated decay factors, UPF1 and UPF2. <i> Clerici M, Mourão A, Gutsche I, Gehring NH, Hentze MW, Kulozik A, Kadlec J, Sattler M, Cusack S. </i> EMBO J, 2009","date":"2023-05-24T15:50:03.620Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0000184","term_name":"nuclear-transcribed mRNA catabolic process, nonsense-mediated decay","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe171Glu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val172Arg","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met1173Glu","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP00949r021","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"statement":[{"text":"In the tethering assay, mutations of residues Phe1171 and Leu1174, located in the β-hairpin region, decrease NMD efficiency between 30 and 50%, reaching ∼80% for the triple mutant, FVM1173ERE.","type":"Results"},{"text":"In the rescue assay, in which native UPF2 is siRNA depleted and the function is rescued by a transfection of wild-type or mutant UPF2 that are RNAi insensitive, we observe very little effect on NMD efficiency compared with wild-type for the α-helix mutants and a significant effect among β-hairpin mutants only for the triple mutant, FVM1173ERE, which also has the biggest loss of function in the tethering assay (Figure 5D).","type":"Results"},{"text":"In conclusion, our in vitro binding studies and in vivo functional studies show that the β-hairpin region has the dominant function in making a functional UPF2–UPF1 interaction and that the complete disruption of this interaction severely impairs NMD.","type":"Results"}],"term_comment":"","term_def":"\"The nonsense-mediated decay pathway for nuclear-transcribed mRNAs degrades mRNAs in which an amino-acid codon has changed to a nonsense codon; this prevents the translation of such mRNAs into truncated, and potentially harmful, proteins.\" [GOC:krc, GOC:ma, PMID:10025395]","term_is_obsolete":false,"term_not_annotate":false},{"start":1015,"end":1054,"reference_id":"35640974","reference_source":"pmid","reference_html":"Structures of nonsense-mediated mRNA decay factors UPF3B and UPF3A in complex with UPF2 reveal molecular basis for competitive binding and for neurodevelopmental disorder-causing mutation. <i> Bufton JC, Powers KT, Szeto JA, Toelzer C, Berger I, Schaffitzel C. </i> Nucleic Acids Res, 2022","date":"2023-05-24T16:11:39.262Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7QG6"}],"region_id":"DP00949r022","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:8172"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9H1J1"}],"statement":[{"text":"The PDB structure of the protein complex with UPF3A, shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":1105,"end":1207,"reference_id":"19556969","reference_source":"pmid","reference_html":"Unusual bipartite mode of interaction between the nonsense-mediated decay factors, UPF1 and UPF2. <i> Clerici M, Mourão A, Gutsche I, Gehring NH, Hentze MW, Kulozik A, Kadlec J, Sattler M, Cusack S. </i> EMBO J, 2009","date":"2023-06-21T13:07:58.944Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP00949r023","statement":[{"text":"Finally, the NMR spectrum of the free 15N-UPF2(1105–1207) shows that the protein is present in an almost completely unfolded state in solution and folding is observed on addition of UPF1(115–287) (Supplementary Figure S9D).","type":"Results"}]},{"start":1167,"end":1207,"reference_id":"19556969","reference_source":"pmid","reference_html":"Unusual bipartite mode of interaction between the nonsense-mediated decay factors, UPF1 and UPF2. <i> Clerici M, Mourão A, Gutsche I, Gehring NH, Hentze MW, Kulozik A, Kadlec J, Sattler M, Cusack S. </i> EMBO J, 2009","date":"2023-06-21T13:15:05.870Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q92900","operator":null,"partner_start":115,"partner_end":287}],"region_id":"DP00949r024","statement":[{"text":"To further characterize the bipartite binding region in UPF2, which interacts with UPF1, NMR spectra were recorded using two synthetic peptides, corresponding to the helical (residues 1105–1129) and β-hairpin (residues 1167–1207) motifs of UPF2, and to 15N-labelled UPF1 (115–287). As expected, both peptides bind to different regions in UPF1 (Figure 4B and C).","type":"Results"},{"text":"For the UPF2 β-hairpin peptide, UPF1 residues Val206, Val205 and Trp241 show strong chemical-shift perturbations that cluster on the corresponding binding region seen in the crystal structure (Figure 4C).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1108,"end":1128,"reference_id":"19556969","reference_source":"pmid","reference_html":"Unusual bipartite mode of interaction between the nonsense-mediated decay factors, UPF1 and UPF2. <i> Clerici M, Mourão A, Gutsche I, Gehring NH, Hentze MW, Kulozik A, Kadlec J, Sattler M, Cusack S. </i> EMBO J, 2009","date":"2023-06-21T13:25:32.713Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2WJV"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q92900","operator":null,"partner_start":115,"partner_end":925}],"region_id":"DP00949r025","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"}],"statement":[{"text":"The crystal structure of the UPF1(115–914)–UPF2(1105–1198) complex in the monoclinic form allows the identification of two UPF1-interacting regions of UPF2, separated by a flexible linker, in agreement with what was originally proposed for yeast UPF2 (He et al, 1996). The N-terminal part of the UPF2 (residues 1108–1128) fragment forms a long, slightly curved, amphipathic α-helix (Figure 2A).","type":"Results"},{"text":"The binding site for the UPF2 α-helix is formed by the UPF1 residues, Val157, Val161, Phe192, Leu193 and Ile233 and the aliphatic part of Arg236 belonging to loops L6 and L10 and helix α1, which create a hydrophobic surface contacting UPF2 residues, Phe1113, Ile1114, Leu1117, Met1120, Met1121 and Leu1125 (Figure 2C and Supplementary Figure S7A).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1105,"end":1129,"reference_id":"19556969","reference_source":"pmid","reference_html":"Unusual bipartite mode of interaction between the nonsense-mediated decay factors, UPF1 and UPF2. <i> Clerici M, Mourão A, Gutsche I, Gehring NH, Hentze MW, Kulozik A, Kadlec J, Sattler M, Cusack S. </i> EMBO J, 2009","date":"2023-06-21T13:37:13.400Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q92900","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00949r026","statement":[{"text":"The separate helical and β-hairpin elements show different affinities for UPF1. α-helix (1105–1129) shows the weaker binding with a Kd of 92 μM, whereas β-hairpin (1167–1207) has an ∼sixfold higher affinity with a Kd of 16 μM (Supplementary Figure S10).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_Q9HAU5","date":"2016-09-06T17:58:47.000Z","acc":"Q9HAU5","name":"Regulator of nonsense transcripts 2","length":1272,"organism":"Homo sapiens","dataset":["NDDs-related proteins","RNA-binding proteins"],"UniParc":"UPI0000070D5E","genes":[{"name":{"value":"UPF2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:17854","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:17854"}}]},"synonyms":[{"value":"KIAA1408"},{"value":"RENT2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:17854","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:17854"}}]}]}],"alphafold_very_low_content":0.23270440251572327,"disorder_content":0.23977987421383648,"disprot_consensus":{"full":[{"start":430,"end":536,"type":"D"},{"start":757,"end":767,"type":"D"},{"start":1015,"end":1078,"type":"D"},{"start":1105,"end":1129,"type":"T"},{"start":1130,"end":1166,"type":"D"},{"start":1167,"end":1207,"type":"T"},{"start":1208,"end":1227,"type":"D"}],"Structural state":[{"start":430,"end":536,"type":"D"},{"start":757,"end":767,"type":"D"},{"start":1015,"end":1078,"type":"D"},{"start":1105,"end":1227,"type":"D"}],"Structural transition":[{"start":1105,"end":1129,"type":"T"},{"start":1167,"end":1207,"type":"T"}],"Molecular function":[{"start":1105,"end":1129,"type":"F"},{"start":1167,"end":1207,"type":"F"}],"Disorder function":[{"start":757,"end":767,"type":"F"},{"start":1042,"end":1050,"type":"F"},{"start":1130,"end":1166,"type":"F"}],"Biological process":[{"start":1171,"end":1176,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00612","name":"IQ calmodulin-binding motif","start":32,"end":52},{"id":"PF06614","name":"Neuromodulin","start":67,"end":238},{"id":"PF10580","name":"Gap junction protein N-terminal region","start":2,"end":31}],"gene3D":[{"start":4,"end":62,"id":"1.20.5.190","name":"1.20.5.190"}]},"uniref50":"UniRef50_P17677","sequence":"MLCCMRRTKQVEKNDDDQKIEQDGIKPEDKAHKAATKIQASFRGHITRKKLKGEKKDDVQAAEAEANKKDEAPVADGVEKKGEGTTTAEAAPATGSKPDEPGKAGETPSEEKKGEGDAATEQAAPQAPASSEEKAGSAETESATKASTDNSPSSKAEDAPAKEEPKQADVPAAVTAAAATTPAAEDAAAKATAQPPTETGESSQAEENIEAVDETKPKESARQDEGKEEEPEADQEHA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P17677","disprot_id":"DP00951","ncbi_taxon_id":9606,"regions_counter":4,"creator":"ldobson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":238,"region_id":"DP00951r001","released":"2022_03","ec_id":"ECO:0007680","reference_html":"High-order oligomers of intrinsically disordered brain proteins BASP1 and GAP-43 preserve the structural disorder. <i> Forsova OS, Zakharov VV. </i> FEBS J, 2016","term_id":"IDPO:0000002","curator_id":"atantos","start":1,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"chromatography evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"26918762","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":238,"region_id":"DP00951r002","released":"2022_03","ec_id":"ECO:0006202","reference_html":"High-order oligomers of intrinsically disordered brain proteins BASP1 and GAP-43 preserve the structural disorder. <i> Forsova OS, Zakharov VV. </i> FEBS J, 2016","term_id":"IDPO:0000002","curator_id":"atantos","start":1,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"synchrotron radiation circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"26918762","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":238,"region_id":"DP00951r003","released":"2022_03","ec_id":"ECO:0007691","reference_html":"High-order oligomers of intrinsically disordered brain proteins BASP1 and GAP-43 preserve the structural disorder. <i> Forsova OS, Zakharov VV. </i> FEBS J, 2016","term_id":"IDPO:0000002","curator_id":"atantos","start":1,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"26918762","ec_go":"IDA","disprot_namespace":"Structural state"},{"start":1,"end":238,"reference_id":"26748655","reference_source":"pmid","reference_html":"1H, 15N, 13C resonance assignment of human GAP-43. <i> Flamm AG, Żerko S, Zawadzka-Kazimierczuk A, Koźmiński W, Konrat R, Coudevylle N. </i> Biomol NMR Assign, 2016","date":"2024-11-21T11:21:38.929Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":6},{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":null,"value":273}],"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"BMRB","id":"19246"}],"region_id":"DP00951r004","sequence_construct":"MLGGMRRTKQVEKNDDDQKI EQDGIKPEDKAHKAATKIQA SFRGHITRKKLKGEKKDDVQ AAEAEANKKDEAPVADGVEK KGEGTTTAEAAPATGSKPDE PGKAGETPSEEKKGEGDAAT EQAAPQAPASSEEKAGSAET ESATKASTDNSPSSKAEDAP AKEEPKQADVPAAVTAAAAT TPAAEDAAAKATAQPPTETG ESSQAEENIEAVDETKPKES ARQDEGKEEEPEADQEHAAA LEHHHHHHH\n","statement":[{"text":"As can be clearly seen from the very narrow peak dispersion in the 1H dimension of the 1H–15N HSQC spectrum (Fig. 1), GAP-43 is an intrinsically disordered protein.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-21T14:43:11.274Z"}}],"released":"2016_10","uniref100":"UniRef100_P17677","date":"2016-09-07T09:17:43.000Z","acc":"P17677","name":"Neuromodulin","length":238,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012FF84","genes":[{"name":{"value":"GAP43"}}],"alphafold_very_low_content":0.4579831932773109,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":238,"type":"D"}],"Structural state":[{"start":1,"end":238,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00179","name":"Ubiquitin-conjugating enzyme","start":103,"end":226}],"gene3D":[{"start":83,"end":339,"id":"3.10.110.10","name":"Ubiquitin Conjugating Enzyme"}]},"uniref50":"UniRef50_Q9H832","sequence":"MAESPTEEAATAGAGAAGPGASSVAGVVGVSGSGGGFGPPFLPDVWAAAAAAGGAGGPGSGLAPLPGLPPSAAAHGAALLSHWDPTLSSDWDGERTAPQCLLRIKRDIMSIYKEPPPGMFVVPDTVDMTKIHALITGPFDTPYEGGFFLFVFRCPPDYPIHPPRVKLMTTGNNTVRFNPNFYRNGKVCLSILGTWTGPAWSPAQSISSVLISIQSLMTENPYHNEPGFEQERHPGDSKNYNECIRHETIRVAVCDMMEGKCPCPEPLRGVMEKSFLEYYDFYEVACKDRLHLQGQTMQDPFGEKRGHFDYQSLLMRLGLIRQKVLERLHNENAEMDSDSSSSGTETDLHGSLRV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9H832","disprot_id":"DP00953","ncbi_taxon_id":9606,"regions_counter":3,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":99,"region_id":"DP00953r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of UBE2Z Enzyme Provides Functional Insight into Specificity in the FAT10 Protein Conjugation Machinery. <i> Schelpe J, Monté D, Dewitte F, Sixma TK, Rucktooa P. </i> J Biol Chem, 2016","term_id":"IDPO:0000002","curator_id":"nmurvai","start":1,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"26555268","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5A4P"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":99,"term_name":"molecular adaptor activity","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"26555268","version":3,"reference_html":"Structure of UBE2Z Enzyme Provides Functional Insight into Specificity in the FAT10 Protein Conjugation Machinery. <i> Schelpe J, Monté D, Dewitte F, Sixma TK, Rucktooa P. </i> J Biol Chem, 2016","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006220","region_id":"DP00953r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":354,"region_id":"DP00953r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of UBE2Z Enzyme Provides Functional Insight into Specificity in the FAT10 Protein Conjugation Machinery. <i> Schelpe J, Monté D, Dewitte F, Sixma TK, Rucktooa P. </i> J Biol Chem, 2016","term_id":"IDPO:0000002","curator_id":"nmurvai","start":327,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"26555268","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5A4P"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q9H832","date":"2016-09-07T10:08:21.000Z","acc":"Q9H832","name":"Ubiquitin-conjugating enzyme E2 Z","length":354,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00005A774B","genes":[{"name":{"value":"UBE2Z"},"orfNames":[{"value":"HOYS7"}]}],"alphafold_very_low_content":0.2457627118644068,"disorder_content":0.3587570621468927,"disprot_consensus":{"full":[{"start":1,"end":99,"type":"D"},{"start":327,"end":354,"type":"D"}],"Structural state":[{"start":1,"end":99,"type":"D"},{"start":327,"end":354,"type":"D"}],"Molecular function":[{"start":1,"end":99,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00615","name":"Regulator of G protein signaling domain","start":88,"end":210},{"id":"PF00778","name":"DIX domain","start":763,"end":838},{"id":"PF08833","name":"Axin beta-catenin binding motif","start":467,"end":502},{"id":"PF16646","name":"Axin-1 tankyrase binding domain","start":9,"end":82}],"gene3D":[{"start":759,"end":842,"id":"3.10.20.380","name":"3.10.20.380"},{"start":193,"end":212,"id":"1.10.196.10","name":"1.10.196.10"},{"start":80,"end":114,"id":"1.10.196.10","name":"1.10.196.10"},{"start":115,"end":192,"id":"1.10.167.10","name":"Regulator of G-protein Signalling 4, domain 2"}]},"uniref50":"UniRef50_P57094","sequence":"MSVKGKGFPLDLGGSFTEDAPRPPVPGEEGELITTDQRPFSHTYYSLKNDGIKNETSTATPRRPDLDLGYEPEGSASPTPPYLKWAESLHSLLDDQDGIHLFRTFLQQENCADLLDFWFACSGFRKLEPNDSKVEKRLKLAKAIYKKYVLDSNGIVSRQIKPATKSFIKDCVLRQQIDPAMFDQAQMEIQSMMEDNTYPVFLKSDIYLEYTTIGGESPKNYSDQSSGSGTGKGPSGYLPTLNEDEEWRCDQGGEHERERECIPSSLFSQKLALDSSSHCAGSNRRLSDGREFRPGTWREPVNPYYVNTGYAGAPVTSANDSEQQSMSSDADTMSLTDSSVDGIPPYRLRKHYRREMQESANANGRGPLPHIPRTYHMPKDIHVDPEKFAAELISRLEGVLRDREAEQKLEERLKRVRAEEEGDDGDVSSGPSVISHKLPSGPPMHHFNSRYSETGCVGMQIRDAHEENPESILDEHVQRVMKTPGCQSPGTGRHSPKSRSPDGHLSKTLPGSLGTMQTGHGKHSSKSTAKVDSGNLHHHKHVYHHVHHHGGVKPKEQIDGESTQRVQTNFPWNVESHNYATKSRNYAESMGMAPNPMDSLAYSGKVSMLSKRNAKKADLGKSESASHEMPVVPEDSERHQKILQWIMEGEKEIIRHKKSNHSSSSAKKQPPTELARPLSIERPGAVHPWVSAQLRNVVQPSHPFIQDPTMPPNPAPNPLTQLVSKPGARLEEEEKKAAKMPQKQRLKPQKKNVSAPSQPCDNIVVAYYFCGEPIPYRTMVKGRVVTLGQFKELLTKKGNYRYYFKKVSDEFDCGVVFEEVREDDMILPIYEEKIIGQVEKID","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Amphibia","Batrachia","Anura","Pipoidea","Pipidae","Xenopodinae","Xenopus","Xenopus"],"uniref90":"UniRef90_Q9YGY0","disprot_id":"DP00954","ncbi_taxon_id":8355,"regions_counter":3,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":465,"region_id":"DP00954r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of a beta-catenin/axin complex suggests a mechanism for the beta-catenin destruction complex. <i> Xing Y, Clements WK, Kimelman D, Xu W. </i> Genes Dev, 2003","term_id":"IDPO:0000002","curator_id":"eschad","start":435,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1QZ7"}],"reference_id":"14600025","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":465,"term_name":"flexible linker","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of a beta-catenin/axin complex suggests a mechanism for the beta-catenin destruction complex. <i> Xing Y, Clements WK, Kimelman D, Xu W. </i> Genes Dev, 2003","term_id":"IDPO:0000033","curator_id":"eschad","start":435,"term_ontology":"IDPO","curator_name":"Eva Schad","reference_id":"14600025","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00954r002","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":504,"region_id":"DP00954r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of a beta-catenin/axin complex suggests a mechanism for the beta-catenin destruction complex. <i> Xing Y, Clements WK, Kimelman D, Xu W. </i> Genes Dev, 2003","term_id":"IDPO:0000002","curator_id":"eschad","start":483,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1QZ7"}],"reference_id":"14600025","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q9YGY0","date":"2016-09-07T11:26:43.000Z","acc":"Q9YGY0","name":"Axin-1","length":842,"organism":"Xenopus laevis","dataset":[],"UniParc":"UPI00001266A3","genes":[{"name":{"value":"axin1"},"synonyms":[{"value":"axin"},{"value":"axn"}]}],"alphafold_very_low_content":0.5273159144893111,"disorder_content":0.06294536817102138,"disprot_consensus":{"full":[{"start":435,"end":465,"type":"D"},{"start":483,"end":504,"type":"D"}],"Structural state":[{"start":435,"end":465,"type":"D"},{"start":483,"end":504,"type":"D"}],"Disorder function":[{"start":435,"end":465,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00612","name":"IQ calmodulin-binding motif","start":32,"end":52},{"id":"PF06614","name":"Neuromodulin","start":68,"end":242},{"id":"PF10580","name":"Gap junction protein N-terminal region","start":2,"end":31}],"gene3D":[{"start":4,"end":62,"id":"1.20.5.190","name":"1.20.5.190"}]},"uniref50":"UniRef50_P06836","sequence":"MLCCMRRTKQVEKNDEDQKIEQDGIKPEDKAHKAATKIQASFRGHITRKKLKGEKKGDAPAAEAEANEKDEAAVAEGTEKKEGEGSTPAEAAPGAGPKPEEKTGKAGETPSEEKKGEGAPDAATEQAAPQAPAPSEEKAGSAETESATKASTDNSPSSKAEDAPAKEEPKQADVPAAVTAAAATAPAAEDAAAMATAQPPTETAESSQAEEKIEAVDETKPKDSARQDEGKGEEREADQEHA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P06836","disprot_id":"DP00955","ncbi_taxon_id":9913,"regions_counter":6,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":242,"region_id":"DP00955r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Nuclear magnetic resonance studies of the structure of B50/neuromodulin and its interaction with calmodulin. <i> Zhang M, Vogel HJ, Zwiers H. </i> Biochem Cell Biol, 1994","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"7818844","statement":[{"text":"B50/neuromodulin is a neuronal phosphoprotein that is found in association with the inner membrane of nerve cells. In this work, we have studied the structure of bovine B50 in aqueous solution (pH 7.5) by 1H nuclear magnetic resonance (NMR) spectroscopy and our results indicate that B50 is an unstructured protein under these conditions.","type":"Abstract"},{"text":"In agreement with a previous study (Masure et al. 1986), B50 appears to be a largely unstructured protein without any significant amount of regular secondary structure, as indicated by NMR and CD spectroscopy.","type":"Results"},{"text":"It is obvious that there is very little chemical shift dispersion in the aliphatic region of the NMR spectrum. A two-dimensional NOESY spectrum of B50 in H20 showed that no dNN(i,i+ 1) NOE cross-peaks could be observed, indicating that B50 does not have any regular α-helical structure.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-09T12:16:23.299Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":242,"reference_id":"7818844","reference_source":"pmid","reference_html":"Nuclear magnetic resonance studies of the structure of B50/neuromodulin and its interaction with calmodulin. <i> Zhang M, Vogel HJ, Zwiers H. </i> Biochem Cell Biol, 1994","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00955r002","statement":[{"text":"In agreement with a previous study (Masure et al. 1986), B50 appears to be a largely unstructured protein without any significant amount of regular secondary structure, as indicated by NMR and CD spectroscopy.","type":"Results"},{"text":"The CD spectrum of B50 in 5 rnM Tris buffer gave a typical random coil spectrum for the protein (data not shown).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-09T12:12:51.905Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":38,"end":51,"reference_id":"7818844","reference_source":"pmid","reference_html":"Nuclear magnetic resonance studies of the structure of B50/neuromodulin and its interaction with calmodulin. <i> Zhang M, Vogel HJ, Zwiers H. </i> Biochem Cell Biol, 1994","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00955r003","statement":[{"text":"The interaction of a 14-residue peptide (I38-L51) encompassing the CaM-binding domain of B50 with CaM was also studied by NMR. We have found from two-dimensional transferred nuclear Overhauser enhancement experiments that the B50 peptide binds weakly to apo-CaM in an α-helical conformation; the α-helix appears to be induced by the binding of the peptide to apo-CaM.","type":"Abstract"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-09T12:16:28.665Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":38,"end":51,"reference_id":"7818844","reference_source":"pmid","reference_html":"Nuclear magnetic resonance studies of the structure of B50/neuromodulin and its interaction with calmodulin. <i> Zhang M, Vogel HJ, Zwiers H. </i> Biochem Cell Biol, 1994","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP00955r004","statement":[{"text":"The interaction of a 14-residue peptide (I38-L51) encompassing the CaM-binding domain of B50 with CaM was also studied by NMR. We have found from two-dimensional transferred nuclear Overhauser enhancement experiments that the B50 peptide binds weakly to apo-CaM in an α-helical conformation; the α-helix appears to be induced by the binding of the peptide to apo-CaM.","type":"Abstract"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-09T12:16:25.982Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":1,"end":242,"reference_id":"1826685","reference_source":"pmid","reference_html":"The interactions of the brain-specific calmodulin-binding protein kinase C substrate, neuromodulin (GAP 43), with membrane phospholipids. <i> Houbre D, Duportail G, Deloulme JC, Baudier J. </i> J Biol Chem, 1991","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00955r005","statement":[{"text":"We used Western blot analysis to investigate the distribution of neuromodulin and neurogranin in membrane and cytosolic extracts of adult rat brain (Fig. 1). Neuromodulin immunoreactivity was found mainly associated with the membrane fractions, but a cytosolic form of the protein also existed (Fig. 1a).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-09T08:08:24.637Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":242,"reference_id":"1826685","reference_source":"pmid","reference_html":"The interactions of the brain-specific calmodulin-binding protein kinase C substrate, neuromodulin (GAP 43), with membrane phospholipids. <i> Houbre D, Duportail G, Deloulme JC, Baudier J. </i> J Biol Chem, 1991","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP00955r006","statement":[{"text":"We used Western blot analysis to investigate the distribution of neuromodulin and neurogranin in membrane and cytosolic extracts of adult rat brain (Fig. 1). Neuromodulin immunoreactivity was found mainly associated with the membrane fractions, but a cytosolic form of the protein also existed (Fig. 1a).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-09T08:08:28.754Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P06836","date":"2016-09-07T11:34:21.000Z","acc":"P06836","name":"Neuromodulin","length":242,"organism":"Bos taurus","dataset":[],"UniParc":"UPI000012FF80","genes":[{"name":{"value":"GAP43"}}],"alphafold_very_low_content":0.5041322314049587,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":37,"type":"D"},{"start":38,"end":51,"type":"T"},{"start":52,"end":242,"type":"D"}],"Structural state":[{"start":1,"end":242,"type":"D"}],"Molecular function":[{"start":1,"end":242,"type":"F"}],"Structural transition":[{"start":38,"end":51,"type":"T"}],"Biological process":[{"start":1,"end":242,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01172","name":"Shwachman-Bodian-Diamond syndrome (SBDS) N-terminal domain","start":16,"end":103},{"id":"PF09377","name":"SBDS protein, domain II","start":113,"end":175}],"gene3D":[{"start":101,"end":175,"id":"1.10.10.900","name":"SBDS protein C-terminal domain, subdomain 1"},{"start":1,"end":97,"id":"3.30.1250.10","name":"Ribosome maturation protein SBDS, N-terminal domain"}]},"uniref50":"UniRef50_Q583Z1","sequence":"MSARIQVPLSQRRHTNVAVVRYTKNGVRLEIACYKNKVISYRGGIETRMDEVLQVERVFTNVSRGLYSSEKEIEAVFGKGTSEKEALQYILDHGELQVAQQERAAEIDQMFIDIAVIISQKCVNEVTQRPFPSQVIEQALHSIGAAVKLDQPVKKQALAFIHQLIDAKTIPIARARMKLRCVVPDEPSLEKLVEWCETNGTSILQKVVEAGGSDAALQIHSLLILLQPHLFRDIERFVKTEMPPGGSVHVIENAAMDVGEGDVMDAELIARANAHMTGASGVGNADKSHCTGSSSNPHAESNRGRRKGKGGSRKPQGVQRVLGKDDGTDQQTVTTAELSSTPAVVGENDDELKVALSKLVLDETNGSRDEDYDGKGRRGKKKAKRRQGEPHQKQQQQPATPQKTVEVDEQQGSDEEVLVNRKQRKQAAARVRVKDDKRNEYWNDADDDDYDYGYEDEDAGEVRD","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Trypanosoma","Schizotrypanum"],"uniref90":"UniRef90_K2N684","disprot_id":"DP00957","ncbi_taxon_id":5693,"regions_counter":10,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":464,"region_id":"DP00957r001","released":"2022_12","ec_id":"ECO:0006204","reference_html":"Characterization of the Trypanosoma cruzi ortholog of the SBDS protein reveals an intrinsically disordered extended C-terminal region showing RNA-interacting activity. <i> de Oliveira JF, Castilho BA, Sforça ML, Krieger MA, Zeri AC, Guimarães BG, Zanchin NI. </i> Biochimie, 2009","term_id":"IDPO:0000002","curator_id":"vnugnes","start":264,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19121363","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-09-16T13:03:48.319Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Consistent with this finding, the CD spectrum of the C-terminal region contains a negative peak near the 200 nm region, which is representative of unfolded proteins (Fig. 3D).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:08:24.505Z"}},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":464,"term_name":"disorder to order","start":264,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"vnugnes","released":"2022_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19121363","version":3,"reference_html":"Characterization of the Trypanosoma cruzi ortholog of the SBDS protein reveals an intrinsically disordered extended C-terminal region showing RNA-interacting activity. <i> de Oliveira JF, Castilho BA, Sforça ML, Krieger MA, Zeri AC, Guimarães BG, Zanchin NI. </i> Biochimie, 2009","date":"2022-09-16T13:12:22.493Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00957r002","ec_go":"EXP","disprot_namespace":"Structural transition","curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting poly-A(25) RNA."}]}],"statement":[{"text":" The resulting spectrum of the mix C-TcSBDS and RNA differs slightly in the 200 and 220 nm regions from the theoretical sum of the spectra from C-TcSBDS and the RNA poly-A measured separately (Fig. 7A).","type":"Results"},{"text":"A comparison of the CD spectra of the C-TcSBDS–RNA interaction with the spectrum of C-TcSBDS with 5% TFE indicates similar changes in the 200 nm region that might be due to conformation changes of C-TcSBDS following interaction with RNA.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:08:49.218Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":464,"region_id":"DP00957r004","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Characterization of the Trypanosoma cruzi ortholog of the SBDS protein reveals an intrinsically disordered extended C-terminal region showing RNA-interacting activity. <i> de Oliveira JF, Castilho BA, Sforça ML, Krieger MA, Zeri AC, Guimarães BG, Zanchin NI. </i> Biochimie, 2009","term_id":"IDPO:0000002","curator_id":"vnugnes","start":264,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19121363","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-09-16T13:04:17.308Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The conformation of the C-terminal domain was also analyzed qualitatively by NMR. As shown in Fig. 5, the 15N-HSQC NMR spectrum revealed that the majority of the resonance peaks are clustered between 8.0 ppm and 8.8 ppm in the 1H dimension, and this low dispersion is characteristic of unfolded structures [21].","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:08:29.215Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":464,"region_id":"DP00957r007","released":"2022_12","ec_id":"ECO:0007691","reference_html":"Characterization of the Trypanosoma cruzi ortholog of the SBDS protein reveals an intrinsically disordered extended C-terminal region showing RNA-interacting activity. <i> de Oliveira JF, Castilho BA, Sforça ML, Krieger MA, Zeri AC, Guimarães BG, Zanchin NI. </i> Biochimie, 2009","term_id":"IDPO:0000002","curator_id":"vnugnes","start":264,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19121363","version":3,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-09-16T13:04:53.354Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"High susceptibility to proteolysis is also an indication of unfolded protein regions. Therefore, the recombinant full-length TcSBDS, N-TcSBDS and the C-terminal region C-TcSBDS were submitted to limited proteolysis. As expected, C-TcSBDS was readily digested by trypsin (Fig. 4).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:08:38.368Z"}},{"start":264,"end":464,"reference_id":"19121363","reference_source":"pmid","reference_html":"Characterization of the Trypanosoma cruzi ortholog of the SBDS protein reveals an intrinsically disordered extended C-terminal region showing RNA-interacting activity. <i> de Oliveira JF, Castilho BA, Sforça ML, Krieger MA, Zeri AC, Guimarães BG, Zanchin NI. </i> Biochimie, 2009","date":"2022-09-16T13:08:34.560Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","region_id":"DP00957r010","statement":[{"text":"Interestingly, we found that the interaction of TcSBDS with RNA is mediated by the C-terminal natively unfolded region (Fig. 6A, lanes 2, 3, 6, 7).","type":"Results"},{"text":"Band shifts were observed only for the EMSA performed with the RNA poly-A probe (Fig. 6B, lanes 2 and 4) both for the full-length TcSBDS and the C-terminal natively unfolded region, C-TcSBDS, indicating that TcSBDS shows higher affinity to RNA than to DNA. EMSA assays were also performed with C-TcSBDS using synthetic RNA (Fig. 6C, lanes 1, 2–5, 6) and DNA (Fig. 6C, lanes 3, 4–7, 8) sequences, which showed results similar to those obtained with the homopolymers RNA poly-A and DNA poly-A. These data indicate that TcSBDS shows a much higher affinity to RNA than to DNA.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:08:54.773Z"}}],"released":"2016_10","uniref100":"UniRef100_C0J347","date":"2016-09-07T13:11:03.000Z","acc":"C0J347","name":"SBDS-like protein","length":464,"organism":"Trypanosoma cruzi","dataset":["Neglected tropical diseases proteins","RNA-binding proteins"],"UniParc":"UPI00019637FE","genes":[],"alphafold_very_low_content":0.3728448275862069,"disorder_content":0.4331896551724138,"disprot_consensus":{"full":[{"start":264,"end":464,"type":"T"}],"Structural state":[{"start":264,"end":464,"type":"D"}],"Structural transition":[{"start":264,"end":464,"type":"T"}],"Molecular function":[{"start":264,"end":464,"type":"F"}]}},{"features":{"pfam":[{"id":"PF08738","name":"Gon7 family","start":4,"end":110}]},"uniref50":"UniRef50_P46984","sequence":"MKLPVAQYSAPDGVEKSFAPIRDDPRYMTTEGRTTGPSDHVLNAGQIDRDKPSEPERTKDGSQLTYLGQLRTQLTGLQDDINEFLTGRMELAKNKKKAGADEKRIQEEINQLLDGGDGDEDAV","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P46984","disprot_id":"DP00958","ncbi_taxon_id":559292,"regions_counter":9,"creator":"smribeiro","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":123,"region_id":"DP00958r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Crystal structures of the Gon7/Pcc1 and Bud32/Cgi121 complexes provide a model for the complete yeast KEOPS complex. <i> Zhang W, Collinet B, Graille M, Daugeron MC, Lazar N, Libri D, Durand D, van Tilbeurgh H. </i> Nucleic Acids Res, 2015","term_id":"IDPO:0000002","curator_id":"smribeiro","start":1,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"25735745","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":21,"region_id":"DP00958r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structures of the Gon7/Pcc1 and Bud32/Cgi121 complexes provide a model for the complete yeast KEOPS complex. <i> Zhang W, Collinet B, Graille M, Daugeron MC, Lazar N, Libri D, Durand D, van Tilbeurgh H. </i> Nucleic Acids Res, 2015","term_id":"IDPO:0000002","curator_id":"smribeiro","start":2,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4WXA"}],"reference_id":"25735745","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":21,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structures of the Gon7/Pcc1 and Bud32/Cgi121 complexes provide a model for the complete yeast KEOPS complex. <i> Zhang W, Collinet B, Graille M, Daugeron MC, Lazar N, Libri D, Durand D, van Tilbeurgh H. </i> Nucleic Acids Res, 2015","term_id":"GO:0060090","curator_id":"smribeiro","start":2,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"25735745","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00958r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":21,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structures of the Gon7/Pcc1 and Bud32/Cgi121 complexes provide a model for the complete yeast KEOPS complex. <i> Zhang W, Collinet B, Graille M, Daugeron MC, Lazar N, Libri D, Durand D, van Tilbeurgh H. </i> Nucleic Acids Res, 2015","term_id":"IDPO:0000011","curator_id":"smribeiro","start":2,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"25735745","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00958r004","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":21,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structures of the Gon7/Pcc1 and Bud32/Cgi121 complexes provide a model for the complete yeast KEOPS complex. <i> Zhang W, Collinet B, Graille M, Daugeron MC, Lazar N, Libri D, Durand D, van Tilbeurgh H. </i> Nucleic Acids Res, 2015","term_id":"GO:0005515","curator_id":"smribeiro","start":2,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"25735745","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00958r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":113,"region_id":"DP00958r006","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structures of the Gon7/Pcc1 and Bud32/Cgi121 complexes provide a model for the complete yeast KEOPS complex. <i> Zhang W, Collinet B, Graille M, Daugeron MC, Lazar N, Libri D, Durand D, van Tilbeurgh H. </i> Nucleic Acids Res, 2015","term_id":"IDPO:0000002","curator_id":"smribeiro","start":65,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4WXA"}],"reference_id":"25735745","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":113,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structures of the Gon7/Pcc1 and Bud32/Cgi121 complexes provide a model for the complete yeast KEOPS complex. <i> Zhang W, Collinet B, Graille M, Daugeron MC, Lazar N, Libri D, Durand D, van Tilbeurgh H. </i> Nucleic Acids Res, 2015","term_id":"GO:0060090","curator_id":"smribeiro","start":65,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"25735745","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00958r007","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":113,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structures of the Gon7/Pcc1 and Bud32/Cgi121 complexes provide a model for the complete yeast KEOPS complex. <i> Zhang W, Collinet B, Graille M, Daugeron MC, Lazar N, Libri D, Durand D, van Tilbeurgh H. </i> Nucleic Acids Res, 2015","term_id":"IDPO:0000011","curator_id":"smribeiro","start":65,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"25735745","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00958r008","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":113,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structures of the Gon7/Pcc1 and Bud32/Cgi121 complexes provide a model for the complete yeast KEOPS complex. <i> Zhang W, Collinet B, Graille M, Daugeron MC, Lazar N, Libri D, Durand D, van Tilbeurgh H. </i> Nucleic Acids Res, 2015","term_id":"GO:0005515","curator_id":"smribeiro","start":65,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"25735745","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00958r009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P46984","date":"2016-09-07T13:26:22.000Z","acc":"P46984","name":"EKC/KEOPS complex subunit GON7","length":123,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000013B601","genes":[{"name":{"value":"GON7"},"synonyms":[{"value":"LDB6"},{"value":"PCC2"}],"orfNames":[{"value":"J0420"}],"olnNames":[{"value":"YJL184W"}]}],"alphafold_very_low_content":0.04065040650406504,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":1,"type":"D"},{"start":2,"end":21,"type":"T"},{"start":22,"end":64,"type":"D"},{"start":65,"end":113,"type":"T"},{"start":114,"end":123,"type":"D"}],"Structural state":[{"start":1,"end":123,"type":"D"}],"Molecular function":[{"start":2,"end":21,"type":"F"},{"start":65,"end":113,"type":"F"}],"Structural transition":[{"start":2,"end":21,"type":"T"},{"start":65,"end":113,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00615","name":"Regulator of G protein signaling domain","start":88,"end":210},{"id":"PF00778","name":"DIX domain","start":783,"end":858},{"id":"PF08833","name":"Axin beta-catenin binding motif","start":465,"end":496},{"id":"PF16646","name":"Axin-1 tankyrase binding domain","start":9,"end":82}],"gene3D":[{"start":779,"end":862,"id":"3.10.20.380","name":"3.10.20.380"},{"start":193,"end":212,"id":"1.10.196.10","name":"1.10.196.10"},{"start":80,"end":114,"id":"1.10.196.10","name":"1.10.196.10"},{"start":115,"end":192,"id":"1.10.167.10","name":"Regulator of G-protein Signalling 4, domain 2"}]},"uniref50":"UniRef50_O35625","sequence":"MNIQEQGFPLDLGASFTEDAPRPPVPGEEGELVSTDPRPASYSFCSGKGVGIKGETSTATPRRSDLDLGYEPEGSASPTPPYLKWAESLHSLLDDQDGISLFRTFLKQEGCADLLDFWFACTGFRKLEPCDSNEEKRLKLARAIYRKYILDNNGIVSRQTKPATKSFIKGCIMKQLIDPAMFDQAQTEIQATMEENTYPSFLKSDIYLEYTRTGSESPKVCSDQSSGSGTGKGISGYLPTLNEDEEWKCDQDMDEDDGRDAAPPGRLPQKLLLETAAPRVSSSRRYSEGREFRYGSWREPVNPYYVNAGYALAPATSANDSEQQSLSSDADTLSLTDSSVDGIPPYRIRKQHRREMQESVQVNGRVPLPHIPRTYRVPKEVRVEPQKFAEELIHRLEAVQRTREAEEKLEERLKRVRMEEEGEDGDPSSGPPGPCHKLPPAPAWHHFPPRCVDMGCAGLRDAHEENPESILDEHVQRVLRTPGRQSPGPGHRSPDSGHVAKMPVALGGAASGHGKHVPKSGAKLDAAGLHHHRHVHHHVHHSTARPKEQVEAEATRRAQSSFAWGLEPHSHGARSRGYSESVGAAPNASDGLAHSGKVGVACKRNAKKAESGKSASTEVPGASEDAEKNQKIMQWIIEGEKEISRHRRTGHGSSGTRKPQPHENSRPLSLEHPWAGPQLRTSVQPSHLFIQDPTMPPHPAPNPLTQLEEARRRLEEEEKRASRAPSKQRYVQEVMRRGRACVRPACAPVLHVVPAVSDMELSETETRSQRKVGGGSAQPCDSIVVAYYFCGEPIPYRTLVRGRAVTLGQFKELLTKKGSYRYYFKKVSDEFDCGVVFEEVREDEAVLPVFEEKIIGKVEKVD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O15169","disprot_id":"DP00959","ncbi_taxon_id":9606,"regions_counter":12,"creator":"ireményi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":500,"region_id":"DP00959r001","released":"2023_12","ec_id":"ECO:0001184","reference_html":"Critical scaffolding regions of the tumor suppressor Axin1 are natively unfolded. <i> Noutsou M, Duarte AM, Anvarian Z, Didenko T, Minde DP, Minde DP, Kuper I, de Ridder I, Oikonomou C, Friedler A, Boelens R, Rüdiger SG, Maurice MM. </i> J Mol Biol, 2011","term_id":"IDPO:0000002","curator_id":"vnugnes","start":295,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"gel-filtration evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-27T14:30:33.129Z","reference_source":"pmid","term_name":"disorder","reference_id":"21087614","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The large apparent size of AxinCRG295-A500 during size-exclusion chromatography could be attributed to either an unfolded extended shape or oligomerization.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:31:31.887Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":500,"region_id":"DP00959r003","released":"2023_12","ec_id":"ECO:0001249","reference_html":"Critical scaffolding regions of the tumor suppressor Axin1 are natively unfolded. <i> Noutsou M, Duarte AM, Anvarian Z, Didenko T, Minde DP, Minde DP, Kuper I, de Ridder I, Oikonomou C, Friedler A, Boelens R, Rüdiger SG, Maurice MM. </i> J Mol Biol, 2011","term_id":"IDPO:0000002","curator_id":"vnugnes","start":295,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"fluorescence evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-27T14:30:16.555Z","reference_source":"pmid","term_name":"disorder","reference_id":"21087614","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"We monitored the fluorescence spectrum of AxinCRG295-A500 while raising the temperature from 20 °C to 80 °C (Fig. 3a and b). The fluorescence intensity of AxinCRG295-A500 peaked at similar wavelengths at minimal and maximal temperatures (Fig. 3a). In concordance, the thermal denaturation curve of AxinCRG295-A500 did not reveal a transition in fluorescence intensity (Fig. 3b).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:31:33.965Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":500,"region_id":"DP00959r005","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Critical scaffolding regions of the tumor suppressor Axin1 are natively unfolded. <i> Noutsou M, Duarte AM, Anvarian Z, Didenko T, Minde DP, Minde DP, Kuper I, de Ridder I, Oikonomou C, Friedler A, Boelens R, Rüdiger SG, Maurice MM. </i> J Mol Biol, 2011","term_id":"IDPO:0000002","curator_id":"vnugnes","start":295,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-27T14:31:22.656Z","reference_source":"pmid","term_name":"disorder","reference_id":"21087614","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The far-UV CD spectrum yielded a negative peak of ellipticity at 201 nm, a typical feature of random-coil structures35 (Fig. 5).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:31:36.439Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":500,"region_id":"DP00959r007","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Critical scaffolding regions of the tumor suppressor Axin1 are natively unfolded. <i> Noutsou M, Duarte AM, Anvarian Z, Didenko T, Minde DP, Minde DP, Kuper I, de Ridder I, Oikonomou C, Friedler A, Boelens R, Rüdiger SG, Maurice MM. </i> J Mol Biol, 2011","term_id":"IDPO:0000002","curator_id":"vnugnes","start":295,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-27T14:32:23.880Z","reference_source":"pmid","term_name":"disorder","reference_id":"21087614","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The resulting HSQC spectrum showed strongly clustered resonances in a narrow range of 7.6–8.6 ppm, which is characteristic of unfolded proteins.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:31:39.954Z"}},{"start":295,"end":500,"reference_id":"21087614","reference_source":"pmid","reference_html":"Critical scaffolding regions of the tumor suppressor Axin1 are natively unfolded. <i> Noutsou M, Duarte AM, Anvarian Z, Didenko T, Minde DP, Minde DP, Kuper I, de Ridder I, Oikonomou C, Friedler A, Boelens R, Rüdiger SG, Maurice MM. </i> J Mol Biol, 2011","date":"2023-11-27T15:01:19.200Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001254","ec_ontology":"ECO","ec_name":"radioisotope assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P49841","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P35222","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP00959r009","statement":[{"text":"Titration of AxinCRG295-A500 strongly enhanced the efficiency of GSK3β in phosphorylating β-catenin in vitro (Fig. 8a), whereas no effect was observed on AxinCR variants lacking either the β-catenin binding site (AxinCRΔβcat) or the GSK3β binding site (AxinCRΔGSK3β), suggesting that Axin binding of both GSK3β and β-catenin is required for its scaffolding function (Fig. 8b and c).","type":"Results"},{"text":"We conclude that the highly flexible AxinCRG295-A500 fragment scaffolds and targets GSK3β kinase activity towards its substrate, β-catenin.","type":"Results"}],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:31:41.739Z"}},{"start":295,"end":500,"reference_id":"21087614","reference_source":"pmid","reference_html":"Critical scaffolding regions of the tumor suppressor Axin1 are natively unfolded. <i> Noutsou M, Duarte AM, Anvarian Z, Didenko T, Minde DP, Minde DP, Kuper I, de Ridder I, Oikonomou C, Friedler A, Boelens R, Rüdiger SG, Maurice MM. </i> J Mol Biol, 2011","date":"2023-11-27T14:52:16.814Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008013","term_name":"beta-catenin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P35222","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00959r010","statement":[{"text":"We recombinantly produced GSK3β as His-tagged NusA fusion protein (to increase solubility) and His-tagged β-catenin. Both His-NusA-tagged GSK3β and His-tagged β-catenin, but not control His-NusA protein, were able to bind AxinCRG295-A500 in a pull-down approach (Fig. 2a–c).","type":"Results"},{"text":"To verify that this interaction also takes place in vivo, we expressed glutathione S-transferase (GST)-tagged AxinCRG295-A500 in HEK293T cells and confirmed its binding to endogenous GSK3β and β-catenin (Fig. 2d).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a catenin beta subunit.\" [GOC:bf]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:31:44.284Z"}},{"start":295,"end":500,"reference_id":"21087614","reference_source":"pmid","reference_html":"Critical scaffolding regions of the tumor suppressor Axin1 are natively unfolded. <i> Noutsou M, Duarte AM, Anvarian Z, Didenko T, Minde DP, Minde DP, Kuper I, de Ridder I, Oikonomou C, Friedler A, Boelens R, Rüdiger SG, Maurice MM. </i> J Mol Biol, 2011","date":"2023-11-27T14:52:42.808Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P49841","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP00959r011","statement":[{"text":"We recombinantly produced GSK3β as His-tagged NusA fusion protein (to increase solubility) and His-tagged β-catenin. Both His-NusA-tagged GSK3β and His-tagged β-catenin, but not control His-NusA protein, were able to bind AxinCRG295-A500 in a pull-down approach (Fig. 2a–c).","type":"Results"},{"text":"To verify that this interaction also takes place in vivo, we expressed glutathione S-transferase (GST)-tagged AxinCRG295-A500 in HEK293T cells and confirmed its binding to endogenous GSK3β and β-catenin (Fig. 2d).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:31:47.252Z"}}],"released":"2016_10","uniref100":"UniRef100_O15169","date":"2016-09-07T14:00:20.000Z","acc":"O15169","name":"Axin-1","length":862,"organism":"Homo sapiens","dataset":["Cancer-related proteins","Condensates-related proteins","NDDs-related proteins"],"UniParc":"UPI0000043C29","genes":[{"name":{"value":"AXIN1"},"synonyms":[{"value":"AXIN"}]}],"alphafold_very_low_content":0.48839907192575405,"disorder_content":0.23897911832946636,"disprot_consensus":{"full":[{"start":295,"end":500,"type":"D"}],"Structural state":[{"start":295,"end":500,"type":"D"}],"Molecular function":[{"start":295,"end":500,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00017","name":"SH2 domain","start":578,"end":648},{"id":"PF01017","name":"STAT transcription factor, coiled-coil domain","start":146,"end":308},{"id":"PF02864","name":"STAT protein, DNA binding domain","start":321,"end":456},{"id":"PF02865","name":"STAT protein, protein interaction domain","start":2,"end":122},{"id":"PF12188","name":"Signal transducer and activator of transcription 2 C terminal","start":783,"end":838},{"id":"PF21354","name":"Signal transducer and activator of transcription, linker domain","start":482,"end":557}],"gene3D":[{"start":1,"end":130,"id":"1.10.532.10","name":"STAT transcription factor, N-terminal domain"},{"start":317,"end":458,"id":"2.60.40.630","name":"STAT transcription factor, DNA-binding domain"},{"start":581,"end":699,"id":"3.30.505.10","name":"SH2 domain"},{"start":459,"end":580,"id":"1.10.238.10","name":"EF-hand"},{"start":138,"end":314,"id":"1.20.1050.20","name":"STAT transcription factor, all-alpha domain"}]},"uniref50":"UniRef50_P52630","sequence":"MAQWEMLQNLDSPFQDQLHQLYSHSLLPVDIRQYLAVWIEDQNWQEAALGSDDSKATMLFFHFLDQLNYECGRCSQDPESLLLQHNLRKFCRDIQPFSQDPTQLAEMIFNLLLEEKRILIQAQRAQLEQGEPVLETPVESQQHEIESRILDLRAMMEKLVKSISQLKDQQDVFCFRYKIQAKGKTPSLDPHQTKEQKILQETLNELDKRRKEVLDASKALLGRLTTLIELLLPKLEEWKAQQQKACIRAPIDHGLEQLETWFTAGAKLLFHLRQLLKELKGLSCLVSYQDDPLTKGVDLRNAQVTELLQRLLHRAFVVETQPCMPQTPHRPLILKTGSKFTVRTRLLVRLQEGNESLTVEVSIDRNPPQLQGFRKFNILTSNQKTLTPEKGQSQGLIWDFGYLTLVEQRSGGSGKGSNKGPLGVTEELHIISFTVKYTYQGLKQELKTDTLPVVIISNMNQLSIAWASVLWFNLLSPNLQNQQFFSNPPKAPWSLLGPALSWQFSSYVGRGLNSDQLSMLRNKLFGQNCRTEDPLLSWADFTKRESPPGKLPFWTWLDKILELVHDHLKDLWNDGRIMGFVSRSQERRLLKKTMSGTFLLRFSESSEGGITCSWVEHQDDDKVLIYSVQPYTKEVLQSLPLTEIIRHYQLLTEENIPENPLRFLYPRIPRDEAFGCYYQEKVNLQERRKYLKHRLIVVSNRQVDELQQPLELKPEPELESLELELGLVPEPELSLDLEPLLKAGLDLGPELESVLESTLEPVIEPTLCMVSQTVPEPDQGPVSQPVPEPDLPCDLRHLNTEPMEIFRNCVKIEEIMPNGDPLLAGQNTVDEVYVSRPSHFYTDGPLMPSDF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P52630","disprot_id":"DP00961","ncbi_taxon_id":9606,"regions_counter":5,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":816,"region_id":"DP00961r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domains. <i> Wojciak JM, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> EMBO J, 2009","term_id":"IDPO:0000002","curator_id":"eschad","start":786,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2KA4"},{"db":"BMRB","id":"16014"}],"reference_id":"19214187","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":816,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domains. <i> Wojciak JM, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> EMBO J, 2009","term_id":"IDPO:0000011","curator_id":"eschad","start":786,"term_ontology":"IDPO","curator_name":"Eva Schad","reference_id":"19214187","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00961r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":816,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domains. <i> Wojciak JM, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> EMBO J, 2009","term_id":"GO:0005515","curator_id":"eschad","start":786,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"19214187","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00961r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":838,"region_id":"DP00961r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domains. <i> Wojciak JM, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> EMBO J, 2009","term_id":"IDPO:0000002","curator_id":"eschad","start":817,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2KA4"},{"db":"BMRB","id":"16014"}],"reference_id":"19214187","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":838,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domains. <i> Wojciak JM, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> EMBO J, 2009","term_id":"GO:0005515","curator_id":"eschad","start":817,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"19214187","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00961r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P52630","date":"2016-09-07T15:01:17.000Z","acc":"P52630","name":"Signal transducer and activator of transcription 2","length":851,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000473FC","genes":[{"name":{"value":"STAT2"}}],"alphafold_very_low_content":0.19623971797884843,"disorder_content":0.06227967097532315,"disprot_consensus":{"full":[{"start":786,"end":816,"type":"T"},{"start":817,"end":838,"type":"D"}],"Structural state":[{"start":786,"end":838,"type":"D"}],"Structural transition":[{"start":786,"end":816,"type":"T"}],"Molecular function":[{"start":786,"end":838,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00017","name":"SH2 domain","start":578,"end":622},{"id":"PF01017","name":"STAT transcription factor, coiled-coil domain","start":144,"end":308},{"id":"PF02864","name":"STAT protein, DNA binding domain","start":322,"end":458},{"id":"PF02865","name":"STAT protein, protein interaction domain","start":2,"end":119},{"id":"PF12162","name":"STAT1 TAZ2 binding domain","start":715,"end":738},{"id":"PF21354","name":"Signal transducer and activator of transcription, linker domain","start":481,"end":558}],"gene3D":[{"start":1,"end":126,"id":"1.10.532.10","name":"STAT transcription factor, N-terminal domain"},{"start":582,"end":708,"id":"3.30.505.10","name":"SH2 domain"},{"start":316,"end":460,"id":"2.60.40.630","name":"STAT transcription factor, DNA-binding domain"},{"start":709,"end":750,"id":"1.10.8.1200","name":"signal transducer and activator of transcription 1"},{"start":461,"end":581,"id":"1.10.238.10","name":"EF-hand"},{"start":133,"end":315,"id":"1.20.1050.20","name":"STAT transcription factor, all-alpha domain"}]},"uniref50":"UniRef50_P42224","sequence":"MSQWYELQQLDSKFLEQVHQLYDDSFPMEIRQYLAQWLEKQDWEHAANDVSFATIRFHDLLSQLDDQYSRFSLENNFLLQHNIRKSKRNLQDNFQEDPIQMSMIIYSCLKEERKILENAQRFNQAQSGNIQSTVMLDKQKELDSKVRNVKDKVMCIEHEIKSLEDLQDEYDFKCKTLQNREHETNGVAKSDQKQEQLLLKKMYLMLDNKRKEVVHKIIELLNVTELTQNALINDELVEWKRRQQSACIGGPPNACLDQLQNWFTIVAESLQQVRQQLKKLEELEQKYTYEHDPITKNKQVLWDRTFSLFQQLIQSSFVVERQPCMPTHPQRPLVLKTGVQFTVKLRLLVKLQELNYNLKVKVLFDKDVNERNTVKGFRKFNILGTHTKVMNMEESTNGSLAAEFRHLQLKEQKNAGTRTNEGPLIVTEELHSLSFETQLCQPGLVIDLETTSLPVVVISNVSQLPSGWASILWYNMLVAEPRNLSFFLTPPCARWAQLSEVLSWQFSSVTKRGLNVDQLNMLGEKLLGPNASPDGLIPWTRFCKENINDKNFPFWLWIESILELIKKHLLPLWNDGCIMGFISKERERALLKDQQPGTFLLRFSESSREGAITFTWVERSQNGGEPDFHAVEPYTKKELSAVTFPDIIRNYKVMAAENIPENPLKYLYPNIDKDHAFGKYYSRPKEAPEPMELDGPKGTGYIKTELISVSEVHPSRLQTTDNLLPMSPEEFDEVSRIVGSVEFDSMMNTV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P42224","disprot_id":"DP00962","ncbi_taxon_id":9606,"regions_counter":4,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":719,"region_id":"DP00962r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domains. <i> Wojciak JM, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> EMBO J, 2009","term_id":"IDPO:0000002","curator_id":"eschad","start":710,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2KA6"},{"db":"BMRB","id":"16015"}],"reference_id":"19214187","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":750,"region_id":"DP00962r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domains. <i> Wojciak JM, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> EMBO J, 2009","term_id":"IDPO:0000002","curator_id":"eschad","start":720,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2KA6"},{"db":"BMRB","id":"16015"}],"reference_id":"19214187","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":750,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domains. <i> Wojciak JM, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> EMBO J, 2009","term_id":"IDPO:0000011","curator_id":"eschad","start":720,"term_ontology":"IDPO","curator_name":"Eva Schad","reference_id":"19214187","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00962r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":750,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domains. <i> Wojciak JM, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> EMBO J, 2009","term_id":"GO:0005515","curator_id":"eschad","start":720,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"19214187","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00962r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P42224","date":"2016-09-07T15:24:09.000Z","acc":"P42224","name":"Signal transducer and activator of transcription 1-alpha/beta","length":750,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000179512","genes":[{"name":{"value":"STAT1"}}],"alphafold_very_low_content":0.06666666666666667,"disorder_content":0.05466666666666667,"disprot_consensus":{"full":[{"start":710,"end":719,"type":"D"},{"start":720,"end":750,"type":"T"}],"Structural state":[{"start":710,"end":750,"type":"D"}],"Structural transition":[{"start":720,"end":750,"type":"T"}],"Molecular function":[{"start":720,"end":750,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04806","name":"EspF protein repeat","start":79,"end":95},{"id":"PF04806","name":"EspF protein repeat","start":96,"end":142},{"id":"PF04806","name":"EspF protein repeat","start":143,"end":189},{"id":"PF04806","name":"EspF protein repeat","start":190,"end":236},{"id":"PF04806","name":"EspF protein repeat","start":237,"end":283},{"id":"PF04806","name":"EspF protein repeat","start":284,"end":330}],"gene3D":[{"start":174,"end":220,"id":"1.10.8.830","name":"TccP2/EspF(U)-like"},{"start":268,"end":314,"id":"1.10.8.830","name":"TccP2/EspF(U)-like"},{"start":127,"end":173,"id":"1.10.8.830","name":"TccP2/EspF(U)-like"},{"start":315,"end":337,"id":"1.10.8.830","name":"TccP2/EspF(U)-like"},{"start":79,"end":126,"id":"1.10.8.830","name":"TccP2/EspF(U)-like"},{"start":221,"end":267,"id":"1.10.8.830","name":"TccP2/EspF(U)-like"}]},"uniref50":"UniRef50_P0DJ88","sequence":"MINNVSSLFPTVNRNITAVYKKSSFSVSPQKITLNPVKISSPFSPSSSSISATTLFRAPNAHSASFHRQSTAESSLHQQLPNVRQRLIQHLAEHGIKPARSMAEHIPPAPNWPAPPPPVQNEQSRPLPDVAQRLVQHLAEHGIQPARNMAEHIPPAPNWPAPPLPVQNEQSRPLPDVAQRLVQHLAEHGIQPARSMAEHIPPAPNWPAPPPPVQNEQSRPLPDVAQRLMQHLAEHGIQPARNMAEHIPPAPNWPAPTPPVQNEQSRPLPDVAQRLMQHLAEHGIQPARNMAEHIPPAPNWPAPTPPVQNEQSRPLPDVAQRLMQHLAEHGINTSKRS","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0DJ88","disprot_id":"DP00963","ncbi_taxon_id":83334,"regions_counter":21,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":314,"region_id":"DP00963r004","released":"2025_06","ec_id":"ECO:0006165","reference_html":"Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. <i> Aitio O, Hellman M, Skehan B, Kesti T, Leong JM, Saksela K, Permi P. </i> Structure, 2012","term_id":"IDPO:0000002","curator_id":"vnugnes","start":293,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2025-02-04T14:15:24.704Z","reference_source":"pmid","term_name":"disorder","reference_id":"22921828","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"In contrast, the C-terminal part (residues 17–47), which includes the proline-rich segment 27IPPAPNWPAPTPP39 that harbors the tandem PxxP motifs responsible IRTKS SH3 binding, is highly disordered.","type":"Results"}]},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":306,"term_name":"disorder to order","released":"2025_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. <i> Aitio O, Hellman M, Skehan B, Kesti T, Leong JM, Saksela K, Permi P. </i> Structure, 2012","term_id":"IDPO:0000011","curator_id":"vnugnes","start":294,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"22921828","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2025-02-04T14:22:01.702Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00963r005","ec_go":"EXP","disprot_namespace":"Structural transition","statement":[{"text":"Clearly, the N-WASP GBD binding epitope, encompassing residues 3Asp-Arg21, became more rigid upon binding to N-WASP as reported by increased heteronuclear NOEs > 0.7), whereas extensive disorder-to-order transition, which translates into substantial increase of heteronuclear NOEs from negative to large positive values, could be observed for the IRTKS SH3 binding region (27IPPAPNWPAPTPP39).","type":"Results"},{"text":" It contains two protein recognition motifs, which undergo disorder-to-order transition upon binding.","type":"Discussion"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UHR4"}],"cross_refs":[{"db":"BMRB","id":"18165"},{"db":"PDB","id":"2LNH"}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":306,"term_name":"SH3 domain binding","released":"2025_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. <i> Aitio O, Hellman M, Skehan B, Kesti T, Leong JM, Saksela K, Permi P. </i> Structure, 2012","term_id":"GO:0017124","curator_id":"vnugnes","start":294,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"22921828","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2025-02-04T14:31:03.230Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00963r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins.\" [GOC:go_curators, Pfam:PF00018]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"BMRB","id":"18165"},{"db":"PDB","id":"2LNH"}],"interaction_partner":[{"db":"UniProt","id":"Q9UHR4","operator":null,"partner_start":339,"partner_end":402}],"statement":[{"text":"Clearly, the N-WASP GBD binding epitope, encompassing residues 3Asp-Arg21, became more rigid upon binding to N-WASP as reported by increased heteronuclear NOEs > 0.7), whereas extensive disorder-to-order transition, which translates into substantial increase of heteronuclear NOEs from negative to large positive values, could be observed for the IRTKS SH3 binding region (27IPPAPNWPAPTPP39)","type":"Results"}]},{"start":268,"end":314,"reference_id":"22921828","reference_source":"pmid","reference_html":"Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. <i> Aitio O, Hellman M, Skehan B, Kesti T, Leong JM, Saksela K, Permi P. </i> Structure, 2012","date":"2025-02-03T10:20:27.808Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00963r008","statement":[{"text":"Instead of well-dispersed 15N-1H correlation spectrum of folded proteins, the 15N-HSQC spectrum of EspFU R475 displayed a poorly dispersed correlation map reminiscent of disordered polypeptide chain (Fig. 1C).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-03T13:08:36.686Z"}},{"start":294,"end":306,"reference_id":"22921828","reference_source":"pmid","reference_html":"Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. <i> Aitio O, Hellman M, Skehan B, Kesti T, Leong JM, Saksela K, Permi P. </i> Structure, 2012","date":"2025-02-05T13:28:00.635Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140272","term_name":"exogenous protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp300Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To this end, we made two peptides that carry mutations in position 33 according to EspFU R475 numbering: An EspFU peptide in which the tryptophan in 32NWP34 was replaced by alanine (yielding 32NAP34) and an Eps8 peptide in which the linker alanine in 32RAP34 was replaced by tryptophan (yielding 32RWP34)."}]},{"term_id":"MI:0693","term_name":"Gal4 DNA-binding domain tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q9UHR4","operator":null,"partner_start":339,"partner_end":402}],"region_id":"DP00963r009","statement":[{"text":"W to A replacement in EspFU peptide reduced the affinity substantially, Kd (EspFUW33A) = 22.3 μM, and strikingly, the A to W replacement converted the Eps8 peptide into a strong binder Kd (Eps8A33W) = 2.4 μM. This clearly pinpointed the critical role of the linker tryptophan for high affinity, thus explaining the higher affinity of EspFU as compared to the cellular Eps8 ligand.","type":"Results"},{"text":"Next, we tested alanine substitution of residue W33 in a yeast two-hybrid assay, and found that W to A mutation in “PW33A” construct disrupted binding to IRTKS-SH3, and completely abrogated any activity in this assay (Fig. 4C).","type":"Results"}],"term_comment":"Note that as GO captures normal processes, it may be that exogenous proteins interactions are normal for one of the participating species but not the other. Therefore reciprocal annotations should not be made without confirming that it is physiological relevant.","term_def":"\"Binding to a protein or protein complex from a different species, for example a pathogen molecule binding to a host protein.\" [PMID:28861068]","term_is_obsolete":false,"term_not_annotate":false},{"start":294,"end":306,"reference_id":"22921828","reference_source":"pmid","reference_html":"Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. <i> Aitio O, Hellman M, Skehan B, Kesti T, Leong JM, Saksela K, Permi P. </i> Structure, 2012","date":"2025-02-03T14:42:37.161Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0044650","term_name":"adhesion of symbiont to host cell","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp300Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To this end, we made two peptides that carry mutations in position 33 according to EspFU R475 numbering: An EspFU peptide in which the tryptophan in 32NWP34 was replaced by alanine (yielding 32NAP34) and an Eps8 peptide in which the linker alanine in 32RAP34 was replaced by tryptophan (yielding 32RWP34)."}]}],"ec_go":"IMP","region_id":"DP00963r010","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_C1M8"}],"statement":[{"text":"When MEFs expressing wild type GFP-HPHP fusion construct were infected with KC12, a modified E. coli capable of translocating Tir but not expressing EspFU, the ectopically expressed GFP-HPHP was recruited to the sites of bacterial attachment, as shown by immunostaining the myc-tagged GFP-HPHP fusion, and induced actin pedestal formation (Fig. 4D). In contrast, the IRTKS binding-deficient mutant GFP-HP*HP* failed to be recruited to the sites of bacterial attachments, and consequently no actin assembly was observed, suggesting that IRTKS binding was an essential activity for EspFU recruitment to sites of clustered Tir.","type":"Results"},{"text":"Thus, we conclude that the enhanced IRTKS binding affinity provided by W33 plays a critical role in pedestal formation.","type":"Results"}],"term_comment":"","term_def":"\"The attachment of a symbiont to a host cell via adhesion molecules, general stickiness etc., either directly or indirectly.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":294,"end":306,"reference_id":"22921828","reference_source":"pmid","reference_html":"Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. <i> Aitio O, Hellman M, Skehan B, Kesti T, Leong JM, Saksela K, Permi P. </i> Structure, 2012","date":"2025-02-03T14:55:22.092Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051127","term_name":"positive regulation of actin nucleation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp300Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To this end, we made two peptides that carry mutations in position 33 according to EspFU R475 numbering: An EspFU peptide in which the tryptophan in 32NWP34 was replaced by alanine (yielding 32NAP34) and an Eps8 peptide in which the linker alanine in 32RAP34 was replaced by tryptophan (yielding 32RWP34)."}]}],"ec_go":"IMP","region_id":"DP00963r011","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_C1M8"}],"statement":[{"text":"When MEFs expressing wild type GFP-HPHP fusion construct were infected with KC12, a modified E. coli capable of translocating Tir but not expressing EspFU, the ectopically expressed GFP-HPHP was recruited to the sites of bacterial attachment, as shown by immunostaining the myc-tagged GFP-HPHP fusion, and induced actin pedestal formation (Fig. 4D). In contrast, the IRTKS binding-deficient mutant GFP-HP*HP* failed to be recruited to the sites of bacterial attachments, and consequently no actin assembly was observed, suggesting that IRTKS binding was an essential activity for EspFU recruitment to sites of clustered Tir.","type":"Results"},{"text":"Thus, we conclude that the enhanced IRTKS binding affinity provided by W33 plays a critical role in pedestal formation.","type":"Results"}],"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of actin nucleation, the initial step in the formation of an actin filament in which actin monomers combine to form a new filament.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":268,"end":314,"reference_id":"22921828","reference_source":"pmid","reference_html":"Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. <i> Aitio O, Hellman M, Skehan B, Kesti T, Leong JM, Saksela K, Permi P. </i> Structure, 2012","date":"2025-02-04T14:17:28.197Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0044003","term_name":"modulation by symbiont of host process","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00963r012","statement":[{"text":"Most importantly, we reveal the underlying structural mechanism by which EspFU outcompetes cellular IRTKS SH3 binding ligands and firmly interconnects actin polymerization and membrane regulation machineries.","type":"Introduction"},{"text":"These data showed that the pathogenic EspFU is able to usurp this host cell signaling pathway by superseding the cellular ligand with approximately 60 times higher affinity against its target.","type":"Results"},{"text":"When MEFs expressing wild type GFP-HPHP fusion construct were infected with KC12, a modified E. coli capable of translocating Tir but not expressing EspFU, the ectopically expressed GFP-HPHP was recruited to the sites of bacterial attachment, as shown by immunostaining the myc-tagged GFP-HPHP fusion, and induced actin pedestal formation (Fig. 4D).","type":"Results"},{"text":"Thus, we conclude that the enhanced IRTKS binding affinity provided by W33 plays a critical role in pedestal formation.","type":"Results"}],"term_comment":"","term_def":"\"The process in which a symbiont organism effects a change in the structure or processes of its host organism.\" [GOC:cc]","term_is_obsolete":false,"term_not_annotate":false},{"start":268,"end":314,"reference_id":"22921828","reference_source":"pmid","reference_html":"Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. <i> Aitio O, Hellman M, Skehan B, Kesti T, Leong JM, Saksela K, Permi P. </i> Structure, 2012","date":"2025-02-03T14:59:57.040Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"18165"},{"db":"PDB","id":"2LNH"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9UHR4","operator":null,"partner_start":339,"partner_end":402},{"db":"UniProt","id":"O00401","operator":"and","partner_start":207,"partner_end":270}],"region_id":"DP00963r013","statement":[{"text":"Despite subtle chemical shift perturbations observed in 15N-HSQC spectra of EspFU R475 between binary and ternary complexes (Fig. 2D), the structure suggests that the N- and C-terminal regions of EspFU function as independent units.","type":"Results"},{"text":"Thus, EspFU binding of the IRTKS/IRSp53 SH3 domain results in recruitment of the EspFU:N-WASP:Arp2/3 complex and localized actin assembly.","type":"Results"}],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false},{"start":270,"end":288,"reference_id":"22921828","reference_source":"pmid","reference_html":"Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. <i> Aitio O, Hellman M, Skehan B, Kesti T, Leong JM, Saksela K, Permi P. </i> Structure, 2012","date":"2025-02-04T14:24:02.201Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"18165 "},{"db":"PDB","id":"2LNH"}],"region_id":"DP00963r014","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O00401"}],"statement":[{"text":"Clearly, the N-WASP GBD binding epitope, encompassing residues 3Asp-Arg21, became more rigid upon binding to N-WASP as reported by increased heteronuclear NOEs > 0.7), whereas extensive disorder-to-order transition, which translates into substantial increase of heteronuclear NOEs from negative to large positive values, could be observed for the IRTKS SH3 binding region (27IPPAPNWPAPTPP39).","type":"Results"},{"text":" It contains two protein recognition motifs, which undergo disorder-to-order transition upon binding.","type":"Discussion"}]},{"start":270,"end":288,"reference_id":"22921828","reference_source":"pmid","reference_html":"Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. <i> Aitio O, Hellman M, Skehan B, Kesti T, Leong JM, Saksela K, Permi P. </i> Structure, 2012","date":"2025-02-04T14:34:10.277Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140272","term_name":"exogenous protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"18165 "},{"db":"PDB","id":"2LNH"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"O00401","operator":null,"partner_start":207,"partner_end":270}],"region_id":"DP00963r015","statement":[{"text":"Clearly, the N-WASP GBD binding epitope, encompassing residues 3Asp-Arg21, became more rigid upon binding to N-WASP as reported by increased heteronuclear NOEs > 0.7), whereas extensive disorder-to-order transition, which translates into substantial increase of heteronuclear NOEs from negative to large positive values, could be observed for the IRTKS SH3 binding region (27IPPAPNWPAPTPP39).","type":"Results"}],"term_comment":"Note that as GO captures normal processes, it may be that exogenous proteins interactions are normal for one of the participating species but not the other. Therefore reciprocal annotations should not be made without confirming that it is physiological relevant.","term_def":"\"Binding to a protein or protein complex from a different species, for example a pathogen molecule binding to a host protein.\" [PMID:28861068]","term_is_obsolete":false,"term_not_annotate":false},{"start":221,"end":267,"reference_id":"22921828","reference_source":"pmid","reference_html":"Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. <i> Aitio O, Hellman M, Skehan B, Kesti T, Leong JM, Saksela K, Permi P. </i> Structure, 2012","date":"2025-02-05T09:38:05.353Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00963r016","statement":[{"text":"Instead of well-dispersed 15N-1H correlation spectrum of folded proteins, the 15N-HSQC spectrum of EspFU R475 displayed a poorly dispersed correlation map reminiscent of disordered polypeptide chain (Fig. 1C).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-05T13:20:16.824Z"}},{"start":246,"end":267,"reference_id":"22921828","reference_source":"pmid","reference_html":"Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. <i> Aitio O, Hellman M, Skehan B, Kesti T, Leong JM, Saksela K, Permi P. </i> Structure, 2012","date":"2025-02-05T09:41:35.443Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP00963r017","statement":[{"text":"In contrast, the C-terminal part (residues 17–47), which includes the proline-rich segment 27IPPAPNWPAPTPP39 that harbors the tandem PxxP motifs responsible IRTKS SH3 binding, is highly disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-05T13:20:57.281Z"}},{"start":223,"end":241,"reference_id":"22921828","reference_source":"pmid","reference_html":"Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. <i> Aitio O, Hellman M, Skehan B, Kesti T, Leong JM, Saksela K, Permi P. </i> Structure, 2012","date":"2025-02-05T10:17:37.848Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"GO:0140272","term_name":"exogenous protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"18165"},{"db":"PDB","id":"2LNH"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"O00401","operator":null,"partner_start":207,"partner_end":270}],"region_id":"DP00963r018","statement":[{"text":"Clearly, the N-WASP GBD binding epitope, encompassing residues 3Asp-Arg21, became more rigid upon binding to N-WASP as reported by increased heteronuclear NOEs > 0.7), whereas extensive disorder-to-order transition, which translates into substantial increase of heteronuclear NOEs from negative to large positive values, could be observed for the IRTKS SH3 binding region (27IPPAPNWPAPTPP39).","type":"Results"}],"term_comment":"Note that as GO captures normal processes, it may be that exogenous proteins interactions are normal for one of the participating species but not the other. Therefore reciprocal annotations should not be made without confirming that it is physiological relevant.","term_def":"\"Binding to a protein or protein complex from a different species, for example a pathogen molecule binding to a host protein.\" [PMID:28861068]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-05T13:27:16.016Z"}},{"start":247,"end":259,"reference_id":"22921828","reference_source":"pmid","reference_html":"Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. <i> Aitio O, Hellman M, Skehan B, Kesti T, Leong JM, Saksela K, Permi P. </i> Structure, 2012","date":"2025-02-05T15:24:02.828Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"GO:0140272","term_name":"exogenous protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0693","term_name":"Gal4 DNA-binding domain tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp300Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To this end, we made two peptides that carry mutations in position 33 according to EspFU R475 numbering: An EspFU peptide in which the tryptophan in 32NWP34 was replaced by alanine (yielding 32NAP34) and an Eps8 peptide in which the linker alanine in 32RAP34 was replaced by tryptophan (yielding 32RWP34)."}]}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q9UHR4","operator":null,"partner_start":339,"partner_end":402}],"region_id":"DP00963r019","statement":[{"text":"W to A replacement in EspFU peptide reduced the affinity substantially, Kd (EspFUW33A) = 22.3 μM, and strikingly, the A to W replacement converted the Eps8 peptide into a strong binder Kd (Eps8A33W) = 2.4 μM. This clearly pinpointed the critical role of the linker tryptophan for high affinity, thus explaining the higher affinity of EspFU as compared to the cellular Eps8 ligand.","type":"Results"},{"text":"Next, we tested alanine substitution of residue W33 in a yeast two-hybrid assay, and found that W to A mutation in “PW33A” construct disrupted binding to IRTKS-SH3, and completely abrogated any activity in this assay (Fig. 4C).","type":"Results"}],"term_comment":"Note that as GO captures normal processes, it may be that exogenous proteins interactions are normal for one of the participating species but not the other. Therefore reciprocal annotations should not be made without confirming that it is physiological relevant.","term_def":"\"Binding to a protein or protein complex from a different species, for example a pathogen molecule binding to a host protein.\" [PMID:28861068]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-05T17:11:00.913Z"}},{"start":223,"end":241,"reference_id":"22921828","reference_source":"pmid","reference_html":"Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. <i> Aitio O, Hellman M, Skehan B, Kesti T, Leong JM, Saksela K, Permi P. </i> Structure, 2012","date":"2025-02-06T08:33:37.798Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"18165"},{"db":"PDB","id":"2LNH"}],"region_id":"DP00963r020","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O00401"}],"statement":[{"text":"Clearly, the N-WASP GBD binding epitope, encompassing residues 3Asp-Arg21, became more rigid upon binding to N-WASP as reported by increased heteronuclear NOEs > 0.7), whereas extensive disorder-to-order transition, which translates into substantial increase of heteronuclear NOEs from negative to large positive values, could be observed for the IRTKS SH3 binding region (27IPPAPNWPAPTPP39).","type":"Results"},{"text":"It contains two protein recognition motifs, which undergo disorder-to-order transition upon binding.","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-06T13:36:48.076Z"}},{"start":247,"end":259,"reference_id":"22921828","reference_source":"pmid","reference_html":"Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly. <i> Aitio O, Hellman M, Skehan B, Kesti T, Leong JM, Saksela K, Permi P. </i> Structure, 2012","date":"2025-02-06T08:38:04.723Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"18165"},{"db":"PDB","id":"2LNH"}],"region_id":"DP00963r021","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UHR4"}],"statement":[{"text":"Clearly, the N-WASP GBD binding epitope, encompassing residues 3Asp-Arg21, became more rigid upon binding to N-WASP as reported by increased heteronuclear NOEs > 0.7), whereas extensive disorder-to-order transition, which translates into substantial increase of heteronuclear NOEs from negative to large positive values, could be observed for the IRTKS SH3 binding region (27IPPAPNWPAPTPP39).","type":"Results"},{"text":"It contains two protein recognition motifs, which undergo disorder-to-order transition upon binding.","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-06T13:36:47.312Z"}}],"released":"2016_10","uniref100":"UniRef100_P0DJ88","date":"2016-09-07T16:24:03.000Z","acc":"P0DJ89","name":"Secreted effector protein EspF(U)","length":337,"organism":"Escherichia coli O157:H7","dataset":["Bacterial virulence-related proteins"],"UniParc":"UPI00000D2AF1","genes":[{"name":{"value":"espF(U)"},"synonyms":[{"value":"tccP"}]}],"alphafold_very_low_content":0.42136498516320475,"disorder_content":0.2789317507418398,"disprot_consensus":{"full":[{"start":221,"end":222,"type":"D"},{"start":223,"end":241,"type":"T"},{"start":242,"end":246,"type":"D"},{"start":247,"end":259,"type":"T"},{"start":260,"end":269,"type":"D"},{"start":270,"end":288,"type":"T"},{"start":289,"end":293,"type":"D"},{"start":294,"end":306,"type":"T"},{"start":307,"end":314,"type":"D"}],"Structural state":[{"start":221,"end":314,"type":"D"}],"Structural transition":[{"start":223,"end":241,"type":"T"},{"start":247,"end":259,"type":"T"},{"start":270,"end":288,"type":"T"},{"start":294,"end":306,"type":"T"}],"Molecular function":[{"start":223,"end":241,"type":"F"},{"start":247,"end":259,"type":"F"},{"start":268,"end":314,"type":"F"}],"Biological process":[{"start":268,"end":314,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03911","name":"Sec61beta family","start":11,"end":49}]},"uniref50":"UniRef50_P60460","sequence":"MSKREETGLATSAGLIRYMDETFSKIRVKPEHVIGVTVAFVIIEAILTYGRFL","taxonomy":["Archaea","Euryarchaeota","Methanomada group","Methanococci","Methanococcales","Methanocaldococcaceae","Methanocaldococcus"],"uniref90":"UniRef90_P60460","disprot_id":"DP00964","ncbi_taxon_id":243232,"regions_counter":2,"creator":"smribeiro","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":20,"region_id":"DP00964r001","released":"2023_12","ec_id":"ECO:0006220","reference_html":"X-ray structure of a protein-conducting channel. <i> Van den Berg B, Clemons WM, Collinson I, Modis Y, Hartmann E, Harrison SC, Rapoport TA. </i> Nature, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-23T13:53:50.006Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1RH5"},{"db":"PDB","id":"1RHZ"}],"reference_id":"14661030","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q57817"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q60175"}],"statement":[{"text":"The PDB structure of the SecYEβ complexes shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":20,"region_id":"DP00964r002","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Puzzle plugged by protein pore plasticity. <i> Minor DL. </i> Mol Cell, 2007","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-23T13:51:16.598Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2YXQ"},{"db":"PDB","id":"2YXR"}],"reference_id":"17531803","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q60175"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q57817"}],"statement":[{"text":"The PDB structure of the SecYEβ complexes shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"released":"2016_10","uniref100":"UniRef100_P60460","date":"2016-09-07T17:06:26.000Z","acc":"P60460","name":"Preprotein translocase subunit SecG","length":53,"organism":"Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)","dataset":[],"UniParc":"UPI00002326C4","genes":[{"name":{"value":"secG"},"olnNames":[{"value":"MJ0912.1"}]}],"alphafold_very_low_content":0.018867924528301886,"disorder_content":0.37735849056603776,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"D"}],"Structural state":[{"start":1,"end":20,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00861","name":"Ribosomal L18 of archaea, bacteria, mitoch. and chloroplast","start":6,"end":120}],"gene3D":[{"start":5,"end":120,"id":"3.30.420.100","name":"3.30.420.100"}]},"uniref50":"UniRef50_P09415","sequence":"MITKVDRNAVRKKRHARIRKKIFGTTERPRLSVFRSNKHIYAQIIDDTKSATIVSASTLDKEFGLDSTNNIEAAKKVGELVAKRALEKGIKQVVFDRGGYLYHGRVKALADAAREAGLEF","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Geobacillus"],"uniref90":"UniRef90_P09415","disprot_id":"DP00966","ncbi_taxon_id":1422,"regions_counter":1,"creator":"smribeiro","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":23,"region_id":"DP00966r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The solution structure of ribosomal protein L18 from Bacillus stearothermophilus. <i> Turner CF, Moore PB. </i> J Mol Biol, 2004","term_id":"IDPO:0000002","curator_id":"smribeiro","start":1,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1OVY"}],"reference_id":"14687565","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P09415","date":"2016-09-07T19:00:34.000Z","acc":"P09415","name":"50S ribosomal protein L18","length":120,"organism":"Geobacillus stearothermophilus","dataset":[],"UniParc":"UPI0000133C65","genes":[{"name":{"value":"rplR"}}],"alphafold_very_low_content":0,"disorder_content":0.19166666666666668,"disprot_consensus":{"full":[{"start":1,"end":23,"type":"D"}],"Structural state":[{"start":1,"end":23,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03131","name":"bZIP Maf transcription factor","start":461,"end":551}],"gene3D":[{"start":426,"end":515,"id":"1.10.880.10","name":"Transcription factor, Skn-1-like, DNA-binding domain"}]},"uniref50":"UniRef50_Q16236","sequence":"MMDLELPPPGLQSQQDMDLIDILWRQDIDLGVSREVFDFSQRQKDYELEKQKKLEKERQEQLQKEQEKAFFAQFQLDEETGEFLPIQPAQHIQTDTSGSASYSQVAHIPKQDALYFEDCMQLLAETFPFVDDHESLALDIPSHAESSVFTAPHQAQSLNSSLEAAMTDLSSIEQDMEQVWQELFSIPELQCLNTENKQLADTTAVPSPEATLTEMDSNYHFYSSISSLEKEVGNCGPHFLHGFEDSFSSILSTDDASQLTSLDSNPTLNTDFGDEFYSAFIAEPSDGGSMPSSAAISQSLSELLDGTIEGCDLSLCKAFNPKHAEGTMEFNDSDSGISLNTSPSRASPEHSVESSIYGDPPPGFSDSEMEELDSAPGSVKQNGPKAQPAHSPGDTVQPLSPAQGHSAPMRESQCENTTKKEVPVSPGHQKAPFTKDKHSSRLEAHLTRDELRAKALHIPFPVEKIINLPVDDFNEMMSKEQFNEAQLALIRDIRRRGKNKVAAQNCRKRKLENIVELEQDLGHLKDEREKLLREKGENDRNLHLLKRRLSTLYLEVFSMLRDEDGKPYSPSEYSLQQTRDGNVFLVPKSKKPDTKKN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q60795","disprot_id":"DP00968","ncbi_taxon_id":10090,"regions_counter":4,"creator":"zdosztanyi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":98,"region_id":"DP00968r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Keap1 recruits Neh2 through binding to ETGE and DLG motifs: characterization of the two-site molecular recognition model. <i> Tong KI, Katoh Y, Kusunoki H, Itoh K, Tanaka T, Yamamoto M. </i> Mol Cell Biol, 2006","term_id":"IDPO:0000002","curator_id":"zdosztanyi","start":1,"term_ontology":"IDPO","curator_name":"Zsuzsanna Dosztányi","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"16581765","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":98,"term_name":"molecular function regulator","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Keap1 recruits Neh2 through binding to ETGE and DLG motifs: characterization of the two-site molecular recognition model. <i> Tong KI, Katoh Y, Kusunoki H, Itoh K, Tanaka T, Yamamoto M. </i> Mol Cell Biol, 2006","term_id":"GO:0098772","curator_id":"zdosztanyi","start":1,"term_ontology":"GO","curator_name":"Zsuzsanna Dosztányi","reference_id":"16581765","version":3,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00968r002","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":98,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Keap1 recruits Neh2 through binding to ETGE and DLG motifs: characterization of the two-site molecular recognition model. <i> Tong KI, Katoh Y, Kusunoki H, Itoh K, Tanaka T, Yamamoto M. </i> Mol Cell Biol, 2006","term_id":"IDPO:0000011","curator_id":"zdosztanyi","start":1,"term_ontology":"IDPO","curator_name":"Zsuzsanna Dosztányi","reference_id":"16581765","version":2,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00968r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":98,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Keap1 recruits Neh2 through binding to ETGE and DLG motifs: characterization of the two-site molecular recognition model. <i> Tong KI, Katoh Y, Kusunoki H, Itoh K, Tanaka T, Yamamoto M. </i> Mol Cell Biol, 2006","term_id":"GO:0005515","curator_id":"zdosztanyi","start":1,"term_ontology":"GO","curator_name":"Zsuzsanna Dosztányi","reference_id":"16581765","version":3,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00968r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q60795","date":"2016-09-07T20:50:27.000Z","acc":"Q60795","name":"Nuclear factor erythroid 2-related factor 2","length":597,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000054C7F","genes":[{"name":{"value":"Nfe2l2","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:108420","url":"http://www.informatics.jax.org/marker/MGI:108420"}}]},"synonyms":[{"value":"Nrf2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8943040","url":"http://www.ncbi.nlm.nih.gov/pubmed/8943040","alternativeUrl":"https://europepmc.org/abstract/MED/8943040"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"9240432","url":"http://www.ncbi.nlm.nih.gov/pubmed/9240432","alternativeUrl":"https://europepmc.org/abstract/MED/9240432"}}]}]}],"alphafold_very_low_content":0.48743718592964824,"disorder_content":0.16415410385259632,"disprot_consensus":{"full":[{"start":1,"end":98,"type":"T"}],"Structural state":[{"start":1,"end":98,"type":"D"}],"Molecular function":[{"start":1,"end":98,"type":"F"}],"Structural transition":[{"start":1,"end":98,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00292","name":"'Paired box' domain","start":16,"end":140},{"id":"PF12403","name":"Paired-box protein 2 C terminal","start":283,"end":390}],"gene3D":[{"start":85,"end":149,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"start":9,"end":84,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}]},"uniref50":"UniRef50_P32114-2","sequence":"MDLEKNYPTPRTSRTGHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIKPGVIGGSKPKVATPKVVEKIAEYKRQNPTMFAWEIRDRLLAERVCDNDTVPSVSSINRIIRTKVQQPPNQPVPASSHSIVSTGSVTQVSSVSTDSAGSSYSISGILGITSPSADTNKRKRDEGIQESPVPNGHSLPGRDFLRKQMRGDLFTQQQLEVLDRVFERQHYSDIFTTTEPIKPEQTTEYSAMASLAGGLDDMKANLASPTPADIGSSVPGPQSYPIVTGRDLASTTLPGYPPHVPPAGQGSYSAPTLTGMVPGSEFSGSPYSHPQYSSYNDSWRFPNPGLLGSPYYYSAAARGAAPPAAATAYDRH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q02548","disprot_id":"DP00969","ncbi_taxon_id":9606,"regions_counter":16,"creator":"zdosztanyi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":30,"region_id":"DP00969r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Structural and Dynamics Studies of Pax5 Reveal Asymmetry in Stability and DNA Binding by the Paired Domain. <i> Perez-Borrajero C, Okon M, McIntosh LP. </i> J Mol Biol, 2016","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-05T15:54:08.419Z","reference_source":"pmid","term_name":"disorder","reference_id":"27067111","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"However, the N-terminal ~ 30 residues of Pax51-92 and Pax51-149 lacked any persistent secondary structure and exhibited low RCI-S2 values, indicative of conformational flexibility.","type":"Results"}],"cross_refs":[{"db":"BMRB","id":"26730"}]},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":30,"term_name":"disorder to order","released":"2023_06","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","reference_html":"Structural and Dynamics Studies of Pax5 Reveal Asymmetry in Stability and DNA Binding by the Paired Domain. <i> Perez-Borrajero C, Okon M, McIntosh LP. </i> J Mol Biol, 2016","term_id":"IDPO:0000011","curator_id":"vnugnes","start":19,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27067111","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-05T15:57:59.559Z","reference_source":"pmid","ec_id":"ECO:0006196","region_id":"DP00969r007","ec_go":"EXP","disprot_namespace":"Structural transition","cross_refs":[{"db":"BMRB","id":"26730"},{"db":"BMRB","id":"26731"}],"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Results","text":"To characterize the potential changes in structure and dynamics that occur upon DNA binding by the PD, we assigned the backbone chemical shifts of amide-protonated 2H/15N/13C-labeled Pax51-149 in complex with a 25 bp DNA duplex corresponding to the high affinity variant of the CD19 promoter, CD19-2_Ains (Table 1, Fig. 3a and Supplementary Fig. S1) [23]."}]}],"statement":[{"text":"In contrast, the RCI-S2 values of the linker and the N-terminal residues increased to match those in the helical bundles. This indicates that the protein backbone in these regions becomes more ordered when bound to DNA (Fig. 3b).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":92,"region_id":"DP00969r009","released":"2023_06","ec_id":"ECO:0006196","reference_html":"Structural and Dynamics Studies of Pax5 Reveal Asymmetry in Stability and DNA Binding by the Paired Domain. <i> Perez-Borrajero C, Okon M, McIntosh LP. </i> J Mol Biol, 2016","term_id":"IDPO:0000002","curator_id":"vnugnes","start":76,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-05T15:53:59.717Z","reference_source":"pmid","term_name":"disorder","reference_id":"27067111","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The linker residues in all three fragments were also found to be disordered, exhibiting random coil chemical shifts and hence low RCI-S2 parameters.","type":"Results"}],"cross_refs":[{"db":"BMRB","id":"26730"}]},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":92,"term_name":"flexible linker","released":"2023_06","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","reference_html":"Structural and Dynamics Studies of Pax5 Reveal Asymmetry in Stability and DNA Binding by the Paired Domain. <i> Perez-Borrajero C, Okon M, McIntosh LP. </i> J Mol Biol, 2016","term_id":"IDPO:0000033","curator_id":"vnugnes","start":76,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27067111","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-05T15:46:00.090Z","reference_source":"pmid","ec_id":"ECO:0006196","region_id":"DP00969r011","ec_go":"EXP","disprot_namespace":"Disorder function","statement":[{"text":"The linker residues in all three fragments were also found to be disordered, exhibiting random coil chemical shifts and hence low RCI-S2 parameters.","type":"Results"}]},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":92,"term_name":"disorder to order","released":"2023_06","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","reference_html":"Structural and Dynamics Studies of Pax5 Reveal Asymmetry in Stability and DNA Binding by the Paired Domain. <i> Perez-Borrajero C, Okon M, McIntosh LP. </i> J Mol Biol, 2016","term_id":"IDPO:0000011","curator_id":"vnugnes","start":76,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27067111","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-05T15:53:39.288Z","reference_source":"pmid","ec_id":"ECO:0006196","region_id":"DP00969r012","ec_go":"EXP","disprot_namespace":"Structural transition","cross_refs":[{"db":"BMRB","id":"26730"},{"db":"BMRB","id":"26731"}],"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Results","text":"To characterize the potential changes in structure and dynamics that occur upon DNA binding by the PD, we assigned the backbone chemical shifts of amide-protonated 2H/15N/13C-labeled Pax51-149 in complex with a 25 bp DNA duplex corresponding to the high affinity variant of the CD19 promoter, CD19-2_Ains (Table 1, Fig. 3a and Supplementary Fig. S1) [23]. "}]}],"statement":[{"text":"In contrast, the RCI-S2 values of the linker and the N-terminal residues increased to match those in the helical bundles. This indicates that the protein backbone in these regions becomes more ordered when bound to DNA (Fig. 3b).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":18,"region_id":"DP00969r014","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Structural analysis of the autoinhibition of Ets-1 and its role in protein partnerships. <i> Garvie CW, Pufall MA, Graves BJ, Wolberger C. </i> J Biol Chem, 2002","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-05T15:39:51.652Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1MDM"}],"reference_id":"12221090","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P27577","statements":[{"type":"Methods","text":"The Pax-5-(1–149)·Ets-1ΔN280·DNA complex was prepared for crystallization by mixing equimolar amounts of protein and DNA, followed by dialysis into 10 mm Tris (pH 8.0), 1 mm DTT."}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"ENA","id":"S59359","statements":[{"type":"Methods","text":"The ternary complex was crystallized using a duplex formed by annealing 5′-TTGCCGGAGATGGGCTCCAGTGGCCT-3′ and 5′-AAGGCCACTGGAGCCCATCTCCGGCA-3′, at a concentration of 0.32 mm."}]}],"statement":[{"text":"The final model had all the DNA, Pax-5 residues 19–142, and Ets-1 residues 309–437.","type":"Methods"}]}],"released":"2016_10","uniref100":"UniRef100_Q02548","date":"2016-09-07T21:27:27.000Z","acc":"Q02548","name":"Paired box protein Pax-5","length":391,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI000013136C","genes":[{"name":{"value":"PAX5"}}],"alphafold_very_low_content":0.5063938618925832,"disorder_content":0.12020460358056266,"disprot_consensus":{"full":[{"start":1,"end":18,"type":"D"},{"start":19,"end":30,"type":"T"},{"start":76,"end":92,"type":"T"}],"Structural state":[{"start":1,"end":30,"type":"D"},{"start":76,"end":92,"type":"D"}],"Structural transition":[{"start":19,"end":30,"type":"T"},{"start":76,"end":92,"type":"T"}],"Disorder function":[{"start":76,"end":92,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00364","name":"Biotin-requiring enzyme","start":83,"end":155},{"id":"PF30639","name":"Domain of unknown function (DUF8684)","start":4,"end":33}],"gene3D":[{"start":77,"end":156,"id":"2.40.50.100","name":"2.40.50.100"}]},"uniref50":"UniRef50_P37799","sequence":"MDIRKIKKLIELVEESGISELEISEGEESVRISRAAPAASFPVMQQAYAAPMMQQPAQSNAAAPATVPSMEAPAAAEISGHIVRSPMVGTFYRTPSPDAKAFIEVGQKVNVGDTLCIVEAMKMMNQIEADKSGTVKAILVESGQPVEFDEPLVVIE","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0ABE0","disprot_id":"DP00970","ncbi_taxon_id":83333,"regions_counter":3,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":77,"region_id":"DP00970r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The three-dimensional structure of the biotin carboxylase-biotin carboxyl carrier protein complex of E. coli acetyl-CoA carboxylase. <i> Broussard TC, Kobe MJ, Pakhomova S, Neau DB, Price AE, Champion TS, Waldrop GL. </i> Structure, 2013","term_id":"IDPO:0000002","curator_id":"nmurvai","start":1,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"23499019","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4HR7"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":77,"term_name":"molecular adaptor activity","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"23499019","version":3,"reference_html":"The three-dimensional structure of the biotin carboxylase-biotin carboxyl carrier protein complex of E. coli acetyl-CoA carboxylase. <i> Broussard TC, Kobe MJ, Pakhomova S, Neau DB, Price AE, Champion TS, Waldrop GL. </i> Structure, 2013","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006220","region_id":"DP00970r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":77,"term_name":"protein binding","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"23499019","version":3,"reference_html":"The three-dimensional structure of the biotin carboxylase-biotin carboxyl carrier protein complex of E. coli acetyl-CoA carboxylase. <i> Broussard TC, Kobe MJ, Pakhomova S, Neau DB, Price AE, Champion TS, Waldrop GL. </i> Structure, 2013","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP00970r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P0ABE0","date":"2016-09-07T23:32:59.000Z","acc":"P0ABD8","name":"Biotin carboxyl carrier protein of acetyl-CoA carboxylase","length":156,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI00000480B6","genes":[{"name":{"value":"accB"},"synonyms":[{"value":"fabE"}],"olnNames":[{"value":"b3255"},{"value":"JW3223"}]}],"alphafold_very_low_content":0.14743589743589744,"disorder_content":0.4935897435897436,"disprot_consensus":{"full":[{"start":1,"end":77,"type":"D"}],"Structural state":[{"start":1,"end":77,"type":"D"}],"Molecular function":[{"start":1,"end":77,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MAGNFDSEERSSWYWGRLSRQEAVALLQGQRHGVFLVRDSSTSPGDYVLSVSENSRVSHYIINSSGPRPPVPPSPAQPPPGVSPSRLRIGDQEFDSLPALLEFYKIHYLDTTTLIEPVSRSRQGSGVILRQEEAEYVRALFDFNGNDEEDLPFKKGDILRIRDKPEEQWWNAEDSEGKRGMIPVPYVEKYRPASASVSALIGGR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"","disprot_id":"DP00973","ncbi_taxon_id":9606,"regions_counter":4,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":133,"region_id":"DP00973r003","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK. <i> Kobashigawa Y, Sakai M, Naito M, Yokochi M, Kumeta H, Makino Y, Ogura K, Tanaka S, Inagaki F. </i> Nat Struct Mol Biol, 2007","term_id":"IDPO:0000002","curator_id":"vnugnes","start":121,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-09-01T17:42:13.329Z","reference_source":"pmid","term_name":"disorder","reference_id":"17515907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"CRKI (residues 1–204) showed well-dispersed, sharp signals, which we did not expect, given its molecular weight. Thus, CRKI was considered to have well-defined SH2 and SH3 domains that were connected by a flexible linker.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"2EYY"}]},{"start":121,"end":133,"reference_id":"17515907","reference_source":"pmid","reference_html":"Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK. <i> Kobashigawa Y, Sakai M, Naito M, Yokochi M, Kumeta H, Makino Y, Ogura K, Tanaka S, Inagaki F. </i> Nat Struct Mol Biol, 2007","date":"2024-09-16T08:38:26.696Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":1,"cross_refs":[{"db":"PDB","id":"2EYY"}],"region_id":"DP00973r004","statement":[{"text":"CRKI (residues 1–204) showed well-dispersed, sharp signals, which we did not expect, given its molecular weight. Thus, CRKI was considered to have well-defined SH2 and SH3 domains that were connected by a flexible linker.","type":"Results"}]}],"released":"2016_10","uniref100":"","date":"2016-09-08T11:51:48.000Z","acc":"P46108-2","name":"Isoform Crk-I of Adapter molecule crk","length":204,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000002A725","genes":[{"name":{"value":"CRK"}}],"disorder_content":0.06372549019607843,"disprot_consensus":{"full":[{"start":121,"end":133,"type":"D"}],"Structural state":[{"start":121,"end":133,"type":"D"}],"Disorder function":[{"start":121,"end":133,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00001","name":"7 transmembrane receptor (rhodopsin family)","start":85,"end":336}],"gene3D":[{"start":52,"end":347,"id":"1.20.1070.10","name":"Rhodopsin 7-helix transmembrane proteins"}]},"uniref50":"UniRef50_P35372","sequence":"MDSSAGPGNISDCSDPLAPASCSPAPGSWLNLSHVDGNQSDPCGPNRTGLGGSHSLCPQTGSPSMVTAITIMALYSIVCVVGLFGNFLVMYVIVRYTKMKTATNIYIFNLALADALATSTLPFQSVNYLMGTWPFGNILCKIVISIDYYNMFTSIFTLCTMSVDRYIAVCHPVKALDFRTPRNAKIVNVCNWILSSAIGLPVMFMATTKYRQGSIDCTLTFSHPTWYWENLLKICVFIFAFIMPVLIITVCYGLMILRLKSVRMLSGSKEKDRNLRRITRMVLVVVAVFIVCWTPIHIYVIIKALITIPETTFQTVSWHFCIALGYTNSCLNPVLYAFLDENFKRCFREFCIPTSSTIEQQNSARIRQNTREHPSTANTVDRTNHQLENLEAETAPLP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P33535-5","disprot_id":"DP00974","ncbi_taxon_id":10090,"regions_counter":2,"creator":"ameszaros","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":51,"region_id":"DP00974r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the µ-opioid receptor bound to a morphinan antagonist. <i> Manglik A, Kruse AC, Kobilka TS, Thian FS, Mathiesen JM, Sunahara RK, Pardo L, Weis WI, Kobilka BK, Granier S. </i> Nature, 2012","statement":[{"text":"Previously crystallized GPCRs show little density for the poorly ordered amino and carboxy terminal domains. Although these domains are not critical for maintaining high ligand affinity, these flexible regions may inhibit crystallogenesis","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22437502","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4DKL"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":398,"region_id":"DP00974r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the µ-opioid receptor bound to a morphinan antagonist. <i> Manglik A, Kruse AC, Kobilka TS, Thian FS, Mathiesen JM, Sunahara RK, Pardo L, Weis WI, Kobilka BK, Granier S. </i> Nature, 2012","statement":[{"text":"Previously crystallized GPCRs show little density for the poorly ordered amino and carboxy terminal domains. Although these domains are not critical for maintaining high ligand affinity, these flexible regions may inhibit crystallogenesis","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":361,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22437502","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4DKL"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P42866","date":"2016-09-08T12:44:33.000Z","acc":"P42866","name":"Mu-type opioid receptor","length":398,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000000B28","genes":[{"name":{"value":"Oprm1"},"synonyms":[{"value":"Mor"},{"value":"Oprm"}]}],"alphafold_very_low_content":0.16834170854271358,"disorder_content":0.2236180904522613,"disprot_consensus":{"full":[{"start":1,"end":51,"type":"D"},{"start":361,"end":398,"type":"D"}],"Structural state":[{"start":1,"end":51,"type":"D"},{"start":361,"end":398,"type":"D"}]}},{"features":{"pfam":[{"id":"PF11714","name":"Thrombin inhibitor Madanin","start":1,"end":78}]},"uniref50":"UniRef50_Q4R1A5","sequence":"MKHFAILILAVVASAVVMAYPERDSAKEGNQEQERALHVKVQKRTDGDADYDEYEEDGTTPTPDPTAPTAKPRLRGNKP","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Chelicerata","Arachnida","Acari","Parasitiformes","Ixodida","Ixodoidea","Ixodidae","Haemaphysalinae","Haemaphysalis"],"uniref90":"UniRef90_Q86FP9","disprot_id":"DP00975","ncbi_taxon_id":44386,"regions_counter":9,"creator":"ppere","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":79,"region_id":"DP00975r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The tick-derived anticoagulant madanin is processed by thrombin and factor Xa. <i> Figueiredo AC, de Sanctis D, Pereira PJ. </i> PLoS One, 2013","term_id":"IDPO:0000002","curator_id":"smribeiro","start":20,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23951260","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":73,"region_id":"DP00975r006","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Tyrosine sulfation modulates activity of tick-derived thrombin inhibitors. <i> Thompson RE, Liu X, Ripoll-Rozada J, Alonso-García N, Parker BL, Pereira PJB, Payne RJ. </i> Nat Chem, 2017","statement":[{"text":"The electron density maps were readily interpretable for madanin-1 residues M D31 to M R54 (Fig. 5a)...","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":50,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5L6N"}],"reference_id":"28837178","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":73,"term_name":"molecular function inhibitor activity","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Tyrosine sulfation modulates activity of tick-derived thrombin inhibitors. <i> Thompson RE, Liu X, Ripoll-Rozada J, Alonso-García N, Parker BL, Pereira PJB, Payne RJ. </i> Nat Chem, 2017","statement":[{"text":"Madanin-1 exhibits a novel mechanism of thrombin inhibition.","type":"Results"}],"term_id":"GO:0140678","curator_id":"ppereira","start":50,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"28837178","version":3,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00975r007","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":73,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Tyrosine sulfation modulates activity of tick-derived thrombin inhibitors. <i> Thompson RE, Liu X, Ripoll-Rozada J, Alonso-García N, Parker BL, Pereira PJB, Payne RJ. </i> Nat Chem, 2017","statement":[{"text":"Remarkably, madanin-1 runs along the surface of thrombin in an extended conformation, with its C-terminal region blocking the active site of the enzyme, while the sulfotyrosine-containing region of the inhibitor establishes specific interactions with the exosite II of thrombin (Fig. 5a).","type":"Results"}],"term_id":"GO:0005515","curator_id":"ppereira","start":50,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"28837178","version":3,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00975r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":73,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Tyrosine sulfation modulates activity of tick-derived thrombin inhibitors. <i> Thompson RE, Liu X, Ripoll-Rozada J, Alonso-García N, Parker BL, Pereira PJB, Payne RJ. </i> Nat Chem, 2017","statement":[{"text":"Remarkably, madanin-1 runs along the surface of thrombin in an extended conformation, with its C-terminal region blocking the active site of the enzyme, while the sulfotyrosine-containing region of the inhibitor establishes specific interactions with the exosite II of thrombin (Fig. 5a).","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"ppereira","start":50,"term_ontology":"IDPO","curator_name":"Pedro Pereira","reference_id":"28837178","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00975r009","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2016_10","uniref100":"UniRef100_Q86FP9","date":"2016-09-08T13:43:41.000Z","acc":"Q86FP9","name":"Thrombin inhibitor madanin 1","length":79,"organism":"Haemaphysalis longicornis","dataset":[],"UniParc":"UPI000018F2B5","genes":[],"alphafold_very_low_content":0.08860759493670886,"disorder_content":0.759493670886076,"disprot_consensus":{"full":[{"start":20,"end":49,"type":"D"},{"start":50,"end":73,"type":"T"},{"start":74,"end":79,"type":"D"}],"Structural state":[{"start":20,"end":79,"type":"D"}],"Molecular function":[{"start":50,"end":73,"type":"F"}],"Structural transition":[{"start":50,"end":73,"type":"T"}]}},{"acc":"P04578","sequence":"MRVKEKYQHLWRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTRPNNNTRKRIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLREQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQIINMWQKVGKAMYAPPISGQIRCSSNITGLLLTRDGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEGIEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQGLERILL","creator":"esalladini","dataset":["Viral proteins"],"date":"2016-09-08T13:48:41.000Z","disprot_id":"DP00976","features":{"pfam":[{"id":"PF00516","name":"Envelope glycoprotein GP120","start":34,"end":511},{"id":"PF00517","name":"Retroviral envelope protein","start":530,"end":719}],"gene3D":[{"start":40,"end":165,"id":"2.170.40.20","name":"Human immunodeficiency virus 1, Gp160, envelope glycoprotein","_id":"685af523b4ac24d5329d896e"},{"start":167,"end":499,"id":"2.170.40.20","name":"Human immunodeficiency virus 1, Gp160, envelope glycoprotein","_id":"685af523b4ac24d5329d896f"},{"start":539,"end":663,"id":"1.10.287.210","name":"1.10.287.210","_id":"685af523b4ac24d5329d8970"},{"start":664,"end":688,"id":"1.20.5.490","name":"Single helix bin","_id":"685af523b4ac24d5329d8971"}]},"genes":[{"name":{"value":"env","evidences":[{"source":{"id":"MF_04083","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04083","_id":"685af523b4ac24d5329d899a"},"code":"ECO:0000255","_id":"685af523b4ac24d5329d8999"}],"_id":"685af523b4ac24d5329d899b"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d8998"}],"length":856,"name":"Envelope glycoprotein gp160","ncbi_taxon_id":11706,"organism":"Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)","regions_counter":13,"released":"2016_10","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"UniParc":"UPI000059C27B","uniref100":"UniRef100_P04578","uniref50":"UniRef50_P04578","uniref90":"UniRef90_P04578","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006222","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","ec_ontology":"ECO","start":127,"end":196,"interaction_partner":[],"reference_html":"Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates. <i> Kwong PD, Wyatt R, Majeed S, Robinson J, Sweet RW, Sodroski J, Hendrickson WA. </i> Structure, 2000","reference_id":"11188697","region_id":"DP00976r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In addition, several of the biologically important loops displayed high atomic-mobility (B) factors and were not accurately modeled.","_id":"685af523b4ac24d5329d8985"},{"type":"Curator statement","text":"The region from 127 to 196 (V1-V2 loops) was not modeled.","_id":"685af523b4ac24d5329d8986"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-09-15T14:54:19.389Z","_id":"685af523b4ac24d5329d8987"},"version":1,"_id":"685af523b4ac24d5329d8984","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006222","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","ec_ontology":"ECO","start":127,"end":196,"interaction_partner":[{"db":"UniProt","id":"P01730","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8989"}],"reference_html":"Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates. <i> Kwong PD, Wyatt R, Majeed S, Robinson J, Sweet RW, Sodroski J, Hendrickson WA. </i> Structure, 2000","reference_id":"11188697","region_id":"DP00976r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"For the bridging sheet, the flexibility in the V1/V2 stem in conjunction with a lattice contact with the second domain of CD4 results in a different orientation of the V1/V2 stem and a high overall rmsd.","_id":"685af523b4ac24d5329d898a"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-09-15T14:54:24.892Z","_id":"685af523b4ac24d5329d898b"},"version":1,"_id":"685af523b4ac24d5329d8988","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":127,"end":196,"interaction_partner":[],"reference_html":"Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates. <i> Kwong PD, Wyatt R, Majeed S, Robinson J, Sweet RW, Sodroski J, Hendrickson WA. </i> Structure, 2000","reference_id":"11188697","region_id":"DP00976r011","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"The structure of the HIV gp120 envelope glycoprotein allows direct visualization of two overlapping sets of machinery. One, involved in entry, binds to both CD4 and a chemokine receptor and transmits a signal to gp41 to initiate membrane fusion. The other uses loop variation, steric occlusion, conformational change and a carbohydrate cloak to evade the immune system.","_id":"685af523b4ac24d5329d898d"}],"states_connection":[],"term_comment":"","term_def":"\"A process by which an organism avoids the effects of the host organism's immune response. The host is defined as the larger of the organisms involved in a symbiotic interaction.\" [GOC:mb, PMID:12439615]","term_id":"GO:0042783","term_is_binding":false,"term_is_obsolete":false,"term_name":"evasion of host immune response","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-09-15T14:54:27.569Z","_id":"685af523b4ac24d5329d898e"},"version":1,"_id":"685af523b4ac24d5329d898c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1G9M","_id":"685af523b4ac24d5329d8990"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":398,"end":409,"interaction_partner":[],"reference_html":"Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates. <i> Kwong PD, Wyatt R, Majeed S, Robinson J, Sweet RW, Sodroski J, Hendrickson WA. </i> Structure, 2000","reference_id":"11188697","region_id":"DP00976r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"These include a single addition to the mostly disordered V4 loop (at 397) and four additional N-acetylglucosamine glycans at asparagines 88, 230, 241, and 463.","_id":"685af523b4ac24d5329d8991"},{"type":"Results","text":"Still others, such as the V4 loop, are divergent in both sequence and structure.","_id":"685af523b4ac24d5329d8992"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-09-15T14:54:21.422Z","_id":"685af523b4ac24d5329d8993"},"version":1,"_id":"685af523b4ac24d5329d898f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":127,"end":196,"interaction_partner":[],"reference_html":"Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates. <i> Kwong PD, Wyatt R, Majeed S, Robinson J, Sweet RW, Sodroski J, Hendrickson WA. </i> Structure, 2000","reference_id":"11188697","region_id":"DP00976r013","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"The structure of the HIV gp120 envelope glycoprotein allows direct visualization of two overlapping sets of machinery. One, involved in entry, binds to both CD4 and a chemokine receptor and transmits a signal to gp41 to initiate membrane fusion. The other uses loop variation, steric occlusion, conformational change and a carbohydrate cloak to evade the immune system.","_id":"685af523b4ac24d5329d8995"},{"type":"Results","text":"For the bridging sheet, the flexibility in the V1/V2 stem in conjunction with a lattice contact with the second domain of CD4 results in a different orientation of the V1/V2 stem and a high overall rmsd.","_id":"685af523b4ac24d5329d8996"}],"states_connection":[],"term_comment":"Viral attachment to the host cell is not part of viral entry in GO because virus attachment does not always lead to viral entry: attachment can also result in the virion being carried by the host cell to another location.","term_def":"\"The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm.\" [GOC:jl]","term_go_domain":"P","term_id":"GO:0046718","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral entry into host cell","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-11T11:37:48.254Z","_id":"685af523b4ac24d5329d8997"},"version":1,"_id":"685af523b4ac24d5329d8994","reference_source":"pmid"}],"__v":0,"disorder_content":0.09579439252336448,"disprot_consensus":{"full":[{"start":127,"end":196,"type":"D"},{"start":398,"end":409,"type":"D"}],"Structural state":[{"start":127,"end":196,"type":"D"},{"start":398,"end":409,"type":"D"}],"Molecular function":[{"start":127,"end":196,"type":"F"}],"Biological process":[{"start":127,"end":196,"type":"F"}]}},{"features":{"pfam":[{"id":"PF11714","name":"Thrombin inhibitor Madanin","start":1,"end":79}]},"uniref50":"UniRef50_Q4R1A5","sequence":"MKHFVILILAVVASAVVMAYPERDSAKDGNQEKERALLVKVQERYQGNQGDYDEYDQDETTPPPDPTAQTARPRLRQNQD","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Chelicerata","Arachnida","Acari","Parasitiformes","Ixodida","Ixodoidea","Ixodidae","Haemaphysalinae","Haemaphysalis"],"uniref90":"UniRef90_Q86FP8","disprot_id":"DP00977","ncbi_taxon_id":44386,"regions_counter":3,"creator":"smribeiro","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":80,"region_id":"DP00977r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The tick-derived anticoagulant madanin is processed by thrombin and factor Xa. <i> Figueiredo AC, de Sanctis D, Pereira PJ. </i> PLoS One, 2013","term_id":"IDPO:0000002","curator_id":"smribeiro","start":20,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23951260","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":80,"term_name":"molecular function inhibitor activity","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"The tick-derived anticoagulant madanin is processed by thrombin and factor Xa. <i> Figueiredo AC, de Sanctis D, Pereira PJ. </i> PLoS One, 2013","term_id":"GO:0140678","curator_id":"smribeiro","start":20,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"23951260","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00977r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":80,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"The tick-derived anticoagulant madanin is processed by thrombin and factor Xa. <i> Figueiredo AC, de Sanctis D, Pereira PJ. </i> PLoS One, 2013","term_id":"GO:0005515","curator_id":"smribeiro","start":20,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"23951260","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP00977r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q86FP8","date":"2016-09-08T13:54:58.000Z","acc":"Q86FP8","name":"Thrombin inhibitor madanin 2","length":80,"organism":"Haemaphysalis longicornis","dataset":[],"UniParc":"UPI000018F2B6","genes":[],"alphafold_very_low_content":0.0625,"disorder_content":0.7625,"disprot_consensus":{"full":[{"start":20,"end":80,"type":"D"}],"Structural state":[{"start":20,"end":80,"type":"D"}],"Molecular function":[{"start":20,"end":80,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01192","name":"RNA polymerase Rpb6","start":71,"end":121}],"gene3D":[{"start":2,"end":142,"id":"3.90.940.10","name":"3.90.940.10"}]},"uniref50":"UniRef50_P36595","sequence":"MSDYEEDEAFGMDGAVMEEEVDELEMIDENGQSQQGVSHPGEPSTTVITEDVASSKTAQSGKAVAKEDRTTTPYMTKYERARILGTRALQISMNAPVLVDLEGETDPLQIAMKELAQKKIPLLVRRYLPDGSYEDWSVAELI","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"uniref90":"UniRef90_P36595","disprot_id":"DP00980","ncbi_taxon_id":284812,"regions_counter":5,"creator":"akajava","regions":[{"start":1,"end":59,"reference_id":"19458260","reference_source":"pmid","reference_html":"Schizosacharomyces pombe RNA polymerase II at 3.6-A resolution. <i> Spåhr H, Calero G, Bushnell DA, Kornberg RD. </i> Proc Natl Acad Sci U S A, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3H0G"}],"region_id":"DP00980r005","statement":[{"text":"The N-terminal of the sequence is missing from the pdb, even if not mention in the paper.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-23T14:58:38.560Z"}}],"released":"2016_10","uniref100":"UniRef100_P36595","date":"2016-09-09T10:03:54.000Z","acc":"P36595","name":"DNA-directed RNA polymerases I, II, and III subunit RPABC2","length":142,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","dataset":[],"UniParc":"UPI00001345E1","genes":[{"name":{"value":"rpb6"},"synonyms":[{"value":"rpo15"}],"orfNames":[{"value":"SPCC1020.04c"}]}],"alphafold_very_low_content":0.19014084507042253,"disorder_content":0.4154929577464789,"disprot_consensus":{"full":[{"start":1,"end":59,"type":"D"}],"Structural state":[{"start":1,"end":59,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01241","name":"Photosystem I psaG / psaK","start":72,"end":162}],"gene3D":[{"start":73,"end":167,"id":"1.10.286.40","name":"Chlorophyll a-b binding protein like"}]},"uniref50":"UniRef50_Q9S7N7","sequence":"MAAATASLSSTLLAPCSSKQPQPQQQHQHQQLKCKSFSGLRPLKLNISSNNSSSSLSMSSARRSMTCRAELSPSLVISLSTGLSLFLGRFVFFNFQRENMAKQVPEQNGMSHFEAGDTRAKEYVSLLKSNDPVGFNIVDVLAWGSIGHIVAYYILATASNGYDPSFF","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","Caryophyllales","Chenopodiaceae","Chenopodioideae","Anserineae","Spinacia"],"uniref90":"UniRef90_P12357","disprot_id":"DP00984","ncbi_taxon_id":3562,"regions_counter":2,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":167,"region_id":"DP00984r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure determination and improved model of plant photosystem I. <i> Amunts A, Toporik H, Borovikova A, Nelson N. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"akajava","start":73,"term_ontology":"IDPO","curator_name":"Andrey V Kajava","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2342-6886","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2WSC:G"}],"reference_id":"19923216","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":164,"region_id":"DP00984r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Photosynthesis. Structural basis for energy transfer pathways in the plant PSI-LHCI supercomplex. <i> Qin X, Suga M, Kuang T, Shen JR. </i> Science, 2015","term_id":"IDPO:0000002","curator_id":"akajava","start":70,"term_ontology":"IDPO","curator_name":"Andrey V Kajava","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2342-6886","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4XK8:G"}],"reference_id":"26023133","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P12357","date":"2016-09-09T10:50:47.000Z","acc":"P12357","name":"Photosystem I reaction center subunit V, chloroplastic","length":167,"organism":"Spinacia oleracea","dataset":[],"UniParc":"UPI0000132524","genes":[{"name":{"value":"PSAG"}}],"alphafold_very_low_content":0.3772455089820359,"disorder_content":0.5868263473053892,"disprot_consensus":{"full":[{"start":70,"end":167,"type":"D"}],"Structural state":[{"start":70,"end":167,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01507","name":"Phosphoadenosine phosphosulfate reductase domain","start":28,"end":259}],"gene3D":[{"start":6,"end":211,"id":"3.40.50.620","name":"HUPs"}]},"uniref50":"UniRef50_P72338","sequence":"MVDKLTHLKQLEAESIHIIREVAAEFDNPVMLYSIGKDSAVMLHLARKAFFPGKLPFPVMHVDTRWKFQEMYRFRDQMVEEMGLDLITHINPDGVAQGINPFTHGSAKHTDIMKTEGLKQALDKHGFDAAFGGARRDEEKSRAKERVYSFRDSKHRWDPKNQRPELWNVYNGNVNKGESIRVFPLSNWTELDIWQYIYLEGIPIVPLYFAAERDVIEKNGTLIMIDDERILEHLTDEEKSRIVKKKVRFRTLGCYPLTGAVESEATSLTDIIQEMLLTRTSERQGRVIDHDGAGSMEEKKRQGYF","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Pseudomonadales","Pseudomonadaceae","Pseudomonas"],"uniref90":"UniRef90_Q87WW0","disprot_id":"DP00985","ncbi_taxon_id":223283,"regions_counter":3,"creator":"ameszaros","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":305,"region_id":"DP00985r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Molecular basis for G protein control of the prokaryotic ATP sulfurylase. <i> Mougous JD, Lee DH, Hubbard SC, Schelle MW, Vocadlo DJ, Berger JM, Bertozzi CR. </i> Mol Cell, 2006","term_id":"IDPO:0000002","curator_id":"ameszaros","start":217,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"16387658","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1ZUN"}],"term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":305,"term_name":"entropic chain","start":217,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ameszaros","released":"2022_03","term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"16387658","version":3,"reference_html":"Molecular basis for G protein control of the prokaryotic ATP sulfurylase. <i> Mougous JD, Lee DH, Hubbard SC, Schelle MW, Vocadlo DJ, Berger JM, Bertozzi CR. </i> Mol Cell, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0006220","region_id":"DP00985r002","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":305,"term_name":"small molecule binding","start":217,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"ameszaros","released":"2022_03","term_ontology":"GO","curator_name":"Attila Meszaros","reference_id":"16387658","version":3,"reference_html":"Molecular basis for G protein control of the prokaryotic ATP sulfurylase. <i> Mougous JD, Lee DH, Hubbard SC, Schelle MW, Vocadlo DJ, Berger JM, Bertozzi CR. </i> Mol Cell, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0036094","ec_id":"ECO:0006220","region_id":"DP00985r003","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q87WW0","date":"2016-09-09T10:57:26.000Z","acc":"Q87WW0","name":"Sulfate adenylyltransferase subunit 2","length":305,"organism":"Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)","dataset":[],"UniParc":"UPI00000092F8","genes":[{"name":{"value":"cysD","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00064","url":"https://hamap.expasy.org/unirule/MF_00064"}}]},"olnNames":[{"value":"PSPTO_4433"}]}],"alphafold_very_low_content":0.009836065573770493,"disorder_content":0.29180327868852457,"disprot_consensus":{"full":[{"start":217,"end":305,"type":"D"}],"Structural state":[{"start":217,"end":305,"type":"D"}],"Disorder function":[{"start":217,"end":305,"type":"F"}],"Molecular function":[{"start":217,"end":305,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02226","name":"Picornavirus coat protein (VP4)","start":2,"end":69}],"gene3D":[{"start":1,"end":69,"id":"4.10.80.10","name":"Picornavirus coat protein VP4"}]},"uniref50":"UniRef50_P03303","sequence":"MGAQVTRQQTGTHENANIATNGSHITYNQINFYKDSYAASASKQDFSQDPSKFTEPVVEGLKAGAPVLK","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Picornavirales","Picornaviridae","Enterovirus","Enterovirus D"],"uniref90":"UniRef90_Q68T42","disprot_id":"DP00986","ncbi_taxon_id":42789,"regions_counter":1,"creator":"jbergier","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":29,"region_id":"DP00986r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure and inhibition of EV-D68, a virus that causes respiratory illness in children. <i> Liu Y, Sheng J, Fokine A, Meng G, Shin WH, Long F, Kuhn RJ, Kihara D, Rossmann MG. </i> Science, 2015","term_id":"IDPO:0000002","curator_id":"jbergier","start":2,"term_ontology":"IDPO","curator_name":"Julian Bergier","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4WM7"},{"db":"PDB","id":"4WM8"}],"reference_id":"25554786","statement":[{"text":"According to the PDB structures, the region within the boundaries is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-30T10:39:44.193Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_A0A6B7FJM4","date":"2016-09-09T11:13:56.000Z","acc":"Q8QWD4","name":"VP4","length":69,"organism":"Enterovirus D68","dataset":["Viral proteins"],"UniParc":"UPI0000001F2C","genes":[],"disorder_content":0.4057971014492754,"disprot_consensus":{"full":[{"start":2,"end":29,"type":"D"}],"Structural state":[{"start":2,"end":29,"type":"D"}]}},{"features":{"pfam":[{"id":"PF18557","name":"Anti-sigma factor NepR","start":24,"end":56}]},"uniref50":"UniRef50_B4WE61","sequence":"MIEHVPMEDKRKGAAALDEARLRQQAIGVKLRQMFDEVVNEPVPDEFLAILRKAERPAGGE","taxonomy":["Bacteria","Proteobacteria","Alphaproteobacteria","Caulobacterales","Caulobacteraceae","Caulobacter"],"uniref90":"UniRef90_Q9A2T0","disprot_id":"DP00987","ncbi_taxon_id":565050,"regions_counter":2,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":22,"region_id":"DP00987r001","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Structural basis of a protein partner switch that regulates the general stress response of α-proteobacteria. <i> Herrou J, Rotskoff G, Luo Y, Roux B, Crosson S. </i> Proc Natl Acad Sci U S A, 2012","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-23T19:39:48.151Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3T0Y"}],"reference_id":"22550172","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":15,"end":15,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":91,"end":91,"position":"Specific residue"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A0H3CBZ6"}],"statement":[{"text":"The anti-σ factor, NepR, contains 68 amino acids; electron density for the first 29 N-terminal residues and the last 6 residues of the C terminus is not visible in our maps.","type":"Results"},{"text":"The region the authors mention corresponds to the 1-22 region of this Uniprot.","type":"Curator statement"}]}],"released":"2016_10","uniref100":"UniRef100_Q9A2T0","date":"2016-09-09T11:40:33.000Z","acc":"A0A0H3CFC9","name":"Anti-sigma factor NepR","length":61,"organism":"Caulobacter vibrioides (strain NA1000 / CB15N)","dataset":[],"UniParc":"UPI0003ED1FAC","genes":[{"name":{"value":"nepR","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ACL97055.2","url":"https://www.ebi.ac.uk/ena/browser/view/ACL97055.2"}}]},"olnNames":[{"value":"CCNA_03590","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ACL97055.2","url":"https://www.ebi.ac.uk/ena/browser/view/ACL97055.2"}}]}]}],"alphafold_very_low_content":0.04918032786885246,"disorder_content":0.36065573770491804,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"}],"Structural state":[{"start":1,"end":22,"type":"D"}]}},{"features":{"pfam":[{"id":"PF10636","name":"Hemin uptake protein hemP","start":27,"end":63}],"gene3D":[{"start":22,"end":63,"id":"2.10.70.10","name":"Complement Module, domain 1"}]},"uniref50":"UniRef50_P0ACY0","sequence":"MRYTDSRKLTPETDANHKTASPQPIRRISSQTLLGPDGKLIIDHDGQEYLLRKTQAGKLLLTK","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0ACY0","disprot_id":"DP00989","ncbi_taxon_id":83333,"regions_counter":1,"creator":"ameszaros","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":20,"region_id":"DP00989r001","reference_id":"26144239","start":1,"ec_id":"ECO:0006220","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In this paper, we have shown that YdiE from E. coli has a highly similar structure, with a relatively large, unfolded N-terminal region and a C-terminal region that dimerizes through a highly hydrophobic interface.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"The crystal and solution structure of YdiE from Escherichia coli. <i> Nishimura K, Addy C, Shrestha R, Voet AR, Zhang KY, Ito Y, Tame JR. </i> Acta Crystallogr F Struct Biol Commun, 2015","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","cross_refs":[{"db":"PDB","id":"4YNX"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P0ACY0","date":"2016-09-09T12:41:24.000Z","acc":"P0ACX9","name":"Uncharacterized protein YdiE","length":63,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI000013A9D0","genes":[{"name":{"value":"ydiE"},"olnNames":[{"value":"b1705"},{"value":"JW1695"}]}],"alphafold_very_low_content":0.015873015873015872,"disorder_content":0.31746031746031744,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"D"}],"Structural state":[{"start":1,"end":20,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02507","name":"Photosystem I reaction centre subunit III","start":62,"end":229}],"gene3D":[{"start":78,"end":230,"id":"1.10.8.110","name":"Photosystem I PsaF, reaction centre subunit III"}]},"uniref50":"UniRef50_Q9SHE8","sequence":"MSFTIPTNLYKPLATKPKHLSSSSFAPRSKIVCQQENDQQQPKKLELAKVGANAAAALALSSVLLSSWSVAPDAAMADIAGLTPCKESKQFAKREKQALKKLQASLKLYADDSAPALAIKATMEKTKKRFDNYGKYGLLCGSDGLPHLIVSGDQRHWGEFITPGILFLYIAGWIGWVGRSYLIAIRDEKKPTQKEIIIDVPLASSLLFRGFSWPVAAYRELLNGELVDNNF","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","Caryophyllales","Chenopodiaceae","Chenopodioideae","Anserineae","Spinacia"],"uniref90":"UniRef90_P12355","disprot_id":"DP00990","ncbi_taxon_id":3562,"regions_counter":1,"creator":"ameszaros","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":77,"region_id":"DP00990r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure determination and improved model of plant photosystem I. <i> Amunts A, Toporik H, Borovikova A, Nelson N. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"ameszaros","start":1,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"19923216","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2WSC"},{"db":"PDB","id":"2WSE"},{"db":"PDB","id":"2WSF"}],"term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P12355","date":"2016-09-09T12:54:17.000Z","acc":"P12355","name":"Photosystem I reaction center subunit III, chloroplastic","length":231,"organism":"Spinacia oleracea","dataset":[],"UniParc":"UPI000013251A","genes":[{"name":{"value":"PSAF"}}],"alphafold_very_low_content":0.2683982683982684,"disorder_content":0.3333333333333333,"disprot_consensus":{"full":[{"start":1,"end":77,"type":"D"}],"Structural state":[{"start":1,"end":77,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00582","name":"Universal stress protein family","start":3,"end":146},{"id":"PF00582","name":"Universal stress protein family","start":173,"end":300}],"gene3D":[{"start":1,"end":315,"id":"3.40.50.12370","name":"3.40.50.12370"}]},"uniref50":"UniRef50_Q8ZP84","sequence":"MAMYQNMLVVIDPNQDDQPALRRAVYLHQRIGGKIKAFLPIYDFSYEMTTLLSPDERTAMRQGVISQRTAWIHEQAKYYLNAGVPIEIKVVWHNRPFEAIIQEVISGGHDLVLKMAHQHDRLEAVIFTPTDWHLLRKCPSPVWMVKDQPWPEGGKALVAVNLASEEPYHNALNEKLVKETIELAEQVNHTEVHLVGAYPVTPINIAIELPEFDPSVYNDAIRGQHLLAMKALRQKFGINENMTHVEKGLPEEVIPDLAEHLQAGIVVLGTVGRTGISAAFLGNTAEQVIDHLRCDLLVIKPDQYQTPVELDDEEDD","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0AAC2","disprot_id":"DP00991","ncbi_taxon_id":83333,"regions_counter":3,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":282,"region_id":"DP00991r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure and functional implications of the tandem-type universal stress protein UspE from Escherichia coli. <i> Xu Y, Guo J, Jin X, Kim JS, Ji Y, Fan S, Ha NC, Quan CS. </i> BMC Struct Biol, 2016","term_id":"IDPO:0000002","curator_id":"atantos","start":269,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5CB0"}],"reference_id":"26865045","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":282,"term_name":"entropic chain","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure and functional implications of the tandem-type universal stress protein UspE from Escherichia coli. <i> Xu Y, Guo J, Jin X, Kim JS, Ji Y, Fan S, Ha NC, Quan CS. </i> BMC Struct Biol, 2016","term_id":"IDPO:0000030","curator_id":"atantos","start":269,"term_ontology":"IDPO","curator_name":"Agnes Tantos","reference_id":"26865045","version":3,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00991r002","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":282,"term_name":"small molecule binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure and functional implications of the tandem-type universal stress protein UspE from Escherichia coli. <i> Xu Y, Guo J, Jin X, Kim JS, Ji Y, Fan S, Ha NC, Quan CS. </i> BMC Struct Biol, 2016","term_id":"GO:0036094","curator_id":"atantos","start":269,"term_ontology":"GO","curator_name":"Agnes Tantos","reference_id":"26865045","version":3,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP00991r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P0AAC2","date":"2016-09-09T13:07:46.000Z","acc":"P0AAC0","name":"Universal stress protein E","length":316,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI0000165443","genes":[{"name":{"value":"uspE"},"synonyms":[{"value":"ydaA"}],"olnNames":[{"value":"b1333"},{"value":"JW1327"}]}],"alphafold_very_low_content":0.022151898734177215,"disorder_content":0.04430379746835443,"disprot_consensus":{"full":[{"start":269,"end":282,"type":"D"}],"Structural state":[{"start":269,"end":282,"type":"D"}],"Disorder function":[{"start":269,"end":282,"type":"F"}],"Molecular function":[{"start":269,"end":282,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02406","name":"MmoB/DmpM family","start":36,"end":124}],"gene3D":[{"start":1,"end":138,"id":"3.90.56.10","name":"Monooxygenase component MmoB/DmpM"}]},"uniref50":"UniRef50_P27356","sequence":"MSSAHNAYNAGIMQKTGKAFADEFFAEENQVVHESNAVVLVLMKSDEIDAIIEDIVLKGGKAKNPSIVVEDKAGFWWIKADGAIEIDAAEAGELLGKPFSVYDLLINVSSTVGRAYTLGTKFTITSELMGLDRALTDI","taxonomy":["Bacteria","Proteobacteria","Alphaproteobacteria","Rhizobiales","Methylocystaceae","Methylosinus"],"uniref90":"UniRef90_P27356","disprot_id":"DP00992","ncbi_taxon_id":426,"regions_counter":3,"creator":"ameszaros","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":35,"region_id":"DP00992r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of component B from methane monooxygenase derived through heteronuclear NMR and molecular modeling. <i> Chang SL, Wallar BJ, Lipscomb JD, Mayo KH. </i> Biochemistry, 1999","term_id":"IDPO:0000002","curator_id":"ameszaros","start":1,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"10231531","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2MOB"}],"term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":35,"term_name":"molecular function regulator","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ameszaros","released":"2022_03","term_ontology":"GO","curator_name":"Attila Meszaros","reference_id":"10231531","version":3,"reference_html":"Solution structure of component B from methane monooxygenase derived through heteronuclear NMR and molecular modeling. <i> Chang SL, Wallar BJ, Lipscomb JD, Mayo KH. </i> Biochemistry, 1999","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006165","region_id":"DP00992r002","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":138,"region_id":"DP00992r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of component B from methane monooxygenase derived through heteronuclear NMR and molecular modeling. <i> Chang SL, Wallar BJ, Lipscomb JD, Mayo KH. </i> Biochemistry, 1999","term_id":"IDPO:0000002","curator_id":"ameszaros","start":127,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"10231531","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2MOB"}],"term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P27356","date":"2016-09-09T13:14:14.000Z","acc":"P27356","name":"Methane monooxygenase regulatory protein B","length":138,"organism":"Methylosinus trichosporium","dataset":[],"UniParc":"UPI000011269A","genes":[{"name":{"value":"mmoB"}}],"alphafold_very_low_content":0.028985507246376812,"disorder_content":0.34057971014492755,"disprot_consensus":{"full":[{"start":1,"end":35,"type":"D"},{"start":127,"end":138,"type":"D"}],"Structural state":[{"start":1,"end":35,"type":"D"},{"start":127,"end":138,"type":"D"}],"Molecular function":[{"start":1,"end":35,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02120","name":"Flagellar hook-length control protein FliK","start":273,"end":354}]},"uniref50":"UniRef50_Q9I332","sequence":"MLKLNAVDTAPLVSSDTLAPLPPLRAQQIAFEQALPAHRPPAPRPPFDKGDETTEAAATADAPTSTPLADQPAAPAADRPPTIRQPPMPVAADATPTPTPTPTPTPTPTPTPTPTPTVSPSGSVARQAPAVSARVAASTQAREPASVSAPPVDEPPLVPVSSHPQIAGRTHERPQPGPGFPAKTAAEVAPTAQASVQASPPAPTAGGEGRGEERRQPGETDPSALPPDDQAPVPLPAMQTPGDRLLARLLASSGSRPLPLADLARLLDAVQGRIQVASAAESHAARLQVRLPQLGAVEVQVLHGHGQLQIEISASPGSLALLQQARGELLERLQRLHPEQPVQLTFNQQQDSGQRSRQRRYLHEEWQAE","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Pseudomonadales","Pseudomonadaceae","Pseudomonas"],"uniref90":"UniRef90_Q9I332","disprot_id":"DP00993","ncbi_taxon_id":208964,"regions_counter":5,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":253,"region_id":"DP00993r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The Structure of a Type 3 Secretion System (T3SS) Ruler Protein Suggests a Molecular Mechanism for Needle Length Sensing. <i> Bergeron JRC, Fernández L, Wasney GA, Vuckovic M, Reffuveille F, Hancock REW, Strynadka NCJ. </i> J Biol Chem, 2016","term_id":"IDPO:0000002","curator_id":"atantos","start":1,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"26589798","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":253,"term_name":"flexible N-terminal tail","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The Structure of a Type 3 Secretion System (T3SS) Ruler Protein Suggests a Molecular Mechanism for Needle Length Sensing. <i> Bergeron JRC, Fernández L, Wasney GA, Vuckovic M, Reffuveille F, Hancock REW, Strynadka NCJ. </i> J Biol Chem, 2016","term_id":"IDPO:0000032","curator_id":"atantos","start":1,"term_ontology":"IDPO","curator_name":"Agnes Tantos","reference_id":"26589798","version":3,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00993r002","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":40,"region_id":"DP00993r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The Structure of a Type 3 Secretion System (T3SS) Ruler Protein Suggests a Molecular Mechanism for Needle Length Sensing. <i> Bergeron JRC, Fernández L, Wasney GA, Vuckovic M, Reffuveille F, Hancock REW, Strynadka NCJ. </i> J Biol Chem, 2016","term_id":"IDPO:0000002","curator_id":"atantos","start":20,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"26589798","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Biological process","ec_ontology":"ECO","end":40,"term_name":"localization","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The Structure of a Type 3 Secretion System (T3SS) Ruler Protein Suggests a Molecular Mechanism for Needle Length Sensing. <i> Bergeron JRC, Fernández L, Wasney GA, Vuckovic M, Reffuveille F, Hancock REW, Strynadka NCJ. </i> J Biol Chem, 2016","term_id":"GO:0051179","curator_id":"atantos","start":20,"term_ontology":"GO","curator_name":"Agnes Tantos","reference_id":"26589798","version":3,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00993r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":40,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The Structure of a Type 3 Secretion System (T3SS) Ruler Protein Suggests a Molecular Mechanism for Needle Length Sensing. <i> Bergeron JRC, Fernández L, Wasney GA, Vuckovic M, Reffuveille F, Hancock REW, Strynadka NCJ. </i> J Biol Chem, 2016","term_id":"GO:0005515","curator_id":"atantos","start":20,"term_ontology":"GO","curator_name":"Agnes Tantos","reference_id":"26589798","version":3,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00993r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q9I332","date":"2016-09-09T13:25:50.000Z","acc":"Q9I332","name":"Translocation protein in type III secretion","length":369,"organism":"Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)","dataset":[],"UniParc":"UPI00000C544E","genes":[{"name":{"value":"pscP","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAG05084.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAG05084.1"}}]},"olnNames":[{"value":"PA1695","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAG05084.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAG05084.1"}}]}]}],"alphafold_very_low_content":0.33875338753387535,"disorder_content":0.6856368563685636,"disprot_consensus":{"full":[{"start":1,"end":253,"type":"D"}],"Structural state":[{"start":1,"end":253,"type":"D"}],"Disorder function":[{"start":1,"end":253,"type":"F"}],"Biological process":[{"start":20,"end":40,"type":"F"}],"Molecular function":[{"start":20,"end":40,"type":"F"}]}},{"features":{"pfam":[{"id":"PF09598","name":"Stm1","start":2,"end":53}]},"uniref50":"UniRef50_P39015","sequence":"MSNPFDLLGNDVEDADVVVLPPKEIVKSNTSSKKADVPPPSADPSKARKNRPRPSGNEGAIRDKTAGRRNNRSKDVTDSATTKKSNTRRATDRHSRTGKTDTKKKVNQGWGDDKKELSAEKEAQADAAAEIAEDAAEAEDAGKPKTAQLSLQDYLNQQANNQFNKVPEAKKVELDAERIETAEKEAYVPATKVKNVKSKQLKTKEYLEFDATFVESNTRKNFGDRNNNSRNNFNNRRGGRGARKGNNTANATNSANTVQKNRNIDVSNLPSLA","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P39015","disprot_id":"DP00994","ncbi_taxon_id":559292,"regions_counter":8,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":117,"region_id":"DP00994r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for the inhibition of the eukaryotic ribosome. <i> Garreau de Loubresse N, Prokhorova I, Holtkamp W, Rodnina MV, Yusupova G, Yusupov M. </i> Nature, 2014","term_id":"IDPO:0000002","curator_id":"nmurvai","start":85,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"25209664","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4U3M"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":273,"region_id":"DP00994r005","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for the inhibition of the eukaryotic ribosome. <i> Garreau de Loubresse N, Prokhorova I, Holtkamp W, Rodnina MV, Yusupova G, Yusupov M. </i> Nature, 2014","term_id":"IDPO:0000002","curator_id":"nmurvai","start":177,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"25209664","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4U3M"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":273,"region_id":"DP00994r006","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal Structure of Hypusine-Containing Translation Factor eIF5A Bound to a Rotated Eukaryotic Ribosome. <i> Melnikov S, Mailliot J, Shin BS, Rigger L, Yusupova G, Micura R, Dever TE, Yusupov M. </i> J Mol Biol, 2016","term_id":"IDPO:0000002","curator_id":"nmurvai","start":195,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"27196944","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5DC3"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":121,"region_id":"DP00994r007","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal Structure of Hypusine-Containing Translation Factor eIF5A Bound to a Rotated Eukaryotic Ribosome. <i> Melnikov S, Mailliot J, Shin BS, Rigger L, Yusupova G, Micura R, Dever TE, Yusupov M. </i> J Mol Biol, 2016","term_id":"IDPO:0000002","curator_id":"nmurvai","start":85,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"27196944","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5DC3"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":168,"region_id":"DP00994r008","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal Structure of Hypusine-Containing Translation Factor eIF5A Bound to a Rotated Eukaryotic Ribosome. <i> Melnikov S, Mailliot J, Shin BS, Rigger L, Yusupova G, Micura R, Dever TE, Yusupov M. </i> J Mol Biol, 2016","term_id":"IDPO:0000002","curator_id":"nmurvai","start":142,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"27196944","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5DC3"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P39015","date":"2016-09-09T14:35:54.000Z","acc":"P39015","name":"Suppressor protein STM1","length":273,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI00005EE2F1","genes":[{"name":{"value":"STM1"},"synonyms":[{"value":"MPT4"},{"value":"STO1"}],"orfNames":[{"value":"L9634.1"}],"olnNames":[{"value":"YLR150W"}]}],"alphafold_very_low_content":0.1391941391941392,"disorder_content":0.5897435897435898,"disprot_consensus":{"full":[{"start":85,"end":121,"type":"D"},{"start":142,"end":168,"type":"D"},{"start":177,"end":273,"type":"D"}],"Structural state":[{"start":85,"end":121,"type":"D"},{"start":142,"end":168,"type":"D"},{"start":177,"end":273,"type":"D"}]}},{"features":{"pfam":[{"id":"PF04568","name":"Mitochondrial ATPase inhibitor, IATP","start":16,"end":85}],"gene3D":[{"start":22,"end":82,"id":"1.20.5.500","name":"Single helix bin"}]},"uniref50":"UniRef50_P01097","sequence":"MLPRSALARSLQLQRGVAARFYSEGSTGTPRGSGSEDSFVKRERATEDFFVRQREKEQLRHLKEQLEKQRKKIDSLENKIDSMTK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P01097","disprot_id":"DP00995","ncbi_taxon_id":559292,"regions_counter":4,"creator":"lkalmar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":50,"region_id":"DP00995r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The region from phenylalanine-28 to lysine-50 of a yeast mitochondrial ATPase inhibitor (IF1) forms an α-helix in solution. <i> Sun L, Nakamae N, Ichikawa N. </i> J Bioenerg Biomembr, 2015","term_id":"IDPO:0000002","curator_id":"lkalmar","start":28,"term_ontology":"IDPO","curator_name":"Lajos Kalmár","reference_id":"26420258","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":50,"term_name":"molecular function inhibitor activity","start":28,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"lkalmar","released":"2022_03","term_ontology":"GO","curator_name":"Lajos Kalmár","reference_id":"26420258","version":3,"reference_html":"The region from phenylalanine-28 to lysine-50 of a yeast mitochondrial ATPase inhibitor (IF1) forms an α-helix in solution. <i> Sun L, Nakamae N, Ichikawa N. </i> J Bioenerg Biomembr, 2015","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140678","ec_id":"ECO:0006204","region_id":"DP00995r002","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":50,"term_name":"disorder to order","start":28,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"lkalmar","released":"2022_03","term_ontology":"IDPO","curator_name":"Lajos Kalmár","reference_id":"26420258","version":2,"reference_html":"The region from phenylalanine-28 to lysine-50 of a yeast mitochondrial ATPase inhibitor (IF1) forms an α-helix in solution. <i> Sun L, Nakamae N, Ichikawa N. </i> J Bioenerg Biomembr, 2015","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP00995r003","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":50,"term_name":"protein binding","start":28,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"lkalmar","released":"2022_03","term_ontology":"GO","curator_name":"Lajos Kalmár","reference_id":"26420258","version":3,"reference_html":"The region from phenylalanine-28 to lysine-50 of a yeast mitochondrial ATPase inhibitor (IF1) forms an α-helix in solution. <i> Sun L, Nakamae N, Ichikawa N. </i> J Bioenerg Biomembr, 2015","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP00995r004","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P01097","date":"2016-09-09T15:56:27.000Z","acc":"P01097","name":"ATPase inhibitor, mitochondrial","length":85,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000017329E","genes":[{"name":{"value":"INH1"},"orfNames":[{"value":"D1305"}],"olnNames":[{"value":"YDL181W"}]}],"alphafold_very_low_content":0,"disorder_content":0.27058823529411763,"disprot_consensus":{"full":[{"start":28,"end":50,"type":"T"}],"Structural state":[{"start":28,"end":50,"type":"D"}],"Molecular function":[{"start":28,"end":50,"type":"F"}],"Structural transition":[{"start":28,"end":50,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00436","name":"Single-strand binding protein family","start":4,"end":107}],"gene3D":[{"start":1,"end":117,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}]},"uniref50":"UniRef50_Q9WZ73","sequence":"MSFFNKIILIGRLVRDPEERYTLSGTPVTTFTIAVDRVPRKNAPDDAQTTDFFRIVTFGRLAEFARTYLTKGRLVLVEGEMRMRRWETPTGEKRVSPEVVANVVRFMDRKPAETVSETEEELEIPEEDFSSDTFSEDEPPF","taxonomy":["Bacteria","Thermotogae","Thermotogales","Thermotogaceae","Thermotoga"],"uniref90":"UniRef90_Q9WZ73","disprot_id":"DP00996","ncbi_taxon_id":243274,"regions_counter":9,"creator":"lkalmar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":48,"region_id":"DP00996r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of a single-stranded DNA-binding protein (TM0604) from Thermotoga maritima at 2.60 A resolution. <i> DiDonato M, Krishna SS, Schwarzenbacher R, McMullan D, Jaroszewski L, Miller MD, Abdubek P, Agarwalla S, Ambing E, Axelrod H, Biorac T, Chiu HJ, Deacon AM, Elsliger MA, Feuerhelm J, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Haugen J, Hornsby M, Klock HE, Knuth MW, Koesema E, Kreusch A, Kuhn P, Lesley SA, Moy K, Nigoghossian E, Okach L, Paulsen J, Quijano K, Reyes R, Rife C, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Wilson IA. </i> Proteins, 2006","term_id":"IDPO:0000002","curator_id":"lkalmar","start":38,"term_ontology":"IDPO","curator_name":"Lajos Kalmár","reference_id":"16435371","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1Z9F"}],"term_name":"disorder","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":48,"term_name":"molecular function regulator","start":38,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"lkalmar","released":"2022_03","term_ontology":"GO","curator_name":"Lajos Kalmár","reference_id":"16435371","version":3,"reference_html":"Crystal structure of a single-stranded DNA-binding protein (TM0604) from Thermotoga maritima at 2.60 A resolution. <i> DiDonato M, Krishna SS, Schwarzenbacher R, McMullan D, Jaroszewski L, Miller MD, Abdubek P, Agarwalla S, Ambing E, Axelrod H, Biorac T, Chiu HJ, Deacon AM, Elsliger MA, Feuerhelm J, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Haugen J, Hornsby M, Klock HE, Knuth MW, Koesema E, Kreusch A, Kuhn P, Lesley SA, Moy K, Nigoghossian E, Okach L, Paulsen J, Quijano K, Reyes R, Rife C, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Wilson IA. </i> Proteins, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006220","region_id":"DP00996r002","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":48,"term_name":"nucleic acid binding","start":38,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"lkalmar","released":"2022_03","term_ontology":"GO","curator_name":"Lajos Kalmár","reference_id":"16435371","version":3,"reference_html":"Crystal structure of a single-stranded DNA-binding protein (TM0604) from Thermotoga maritima at 2.60 A resolution. <i> DiDonato M, Krishna SS, Schwarzenbacher R, McMullan D, Jaroszewski L, Miller MD, Abdubek P, Agarwalla S, Ambing E, Axelrod H, Biorac T, Chiu HJ, Deacon AM, Elsliger MA, Feuerhelm J, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Haugen J, Hornsby M, Klock HE, Knuth MW, Koesema E, Kreusch A, Kuhn P, Lesley SA, Moy K, Nigoghossian E, Okach L, Paulsen J, Quijano K, Reyes R, Rife C, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Wilson IA. </i> Proteins, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006220","region_id":"DP00996r003","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":141,"region_id":"DP00996r007","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of a single-stranded DNA-binding protein (TM0604) from Thermotoga maritima at 2.60 A resolution. <i> DiDonato M, Krishna SS, Schwarzenbacher R, McMullan D, Jaroszewski L, Miller MD, Abdubek P, Agarwalla S, Ambing E, Axelrod H, Biorac T, Chiu HJ, Deacon AM, Elsliger MA, Feuerhelm J, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Haugen J, Hornsby M, Klock HE, Knuth MW, Koesema E, Kreusch A, Kuhn P, Lesley SA, Moy K, Nigoghossian E, Okach L, Paulsen J, Quijano K, Reyes R, Rife C, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Wilson IA. </i> Proteins, 2006","term_id":"IDPO:0000002","curator_id":"lkalmar","start":109,"term_ontology":"IDPO","curator_name":"Lajos Kalmár","reference_id":"16435371","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1Z9F"}],"term_name":"disorder","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":141,"term_name":"molecular function regulator","start":109,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"lkalmar","released":"2022_03","term_ontology":"GO","curator_name":"Lajos Kalmár","reference_id":"16435371","version":3,"reference_html":"Crystal structure of a single-stranded DNA-binding protein (TM0604) from Thermotoga maritima at 2.60 A resolution. <i> DiDonato M, Krishna SS, Schwarzenbacher R, McMullan D, Jaroszewski L, Miller MD, Abdubek P, Agarwalla S, Ambing E, Axelrod H, Biorac T, Chiu HJ, Deacon AM, Elsliger MA, Feuerhelm J, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Haugen J, Hornsby M, Klock HE, Knuth MW, Koesema E, Kreusch A, Kuhn P, Lesley SA, Moy K, Nigoghossian E, Okach L, Paulsen J, Quijano K, Reyes R, Rife C, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Wilson IA. </i> Proteins, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0098772","ec_id":"ECO:0006220","region_id":"DP00996r008","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":141,"term_name":"nucleic acid binding","start":109,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"lkalmar","released":"2022_03","term_ontology":"GO","curator_name":"Lajos Kalmár","reference_id":"16435371","version":3,"reference_html":"Crystal structure of a single-stranded DNA-binding protein (TM0604) from Thermotoga maritima at 2.60 A resolution. <i> DiDonato M, Krishna SS, Schwarzenbacher R, McMullan D, Jaroszewski L, Miller MD, Abdubek P, Agarwalla S, Ambing E, Axelrod H, Biorac T, Chiu HJ, Deacon AM, Elsliger MA, Feuerhelm J, Godzik A, Grittini C, Grzechnik SK, Hale J, Hampton E, Haugen J, Hornsby M, Klock HE, Knuth MW, Koesema E, Kreusch A, Kuhn P, Lesley SA, Moy K, Nigoghossian E, Okach L, Paulsen J, Quijano K, Reyes R, Rife C, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, White A, Wolf G, Xu Q, Hodgson KO, Wooley J, Wilson IA. </i> Proteins, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006220","region_id":"DP00996r009","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q9WZ73","date":"2016-09-09T16:43:33.000Z","acc":"Q9WZ73","name":"Single-stranded DNA-binding protein","length":141,"organism":"Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","dataset":[],"UniParc":"UPI00000D39C6","genes":[{"name":{"value":"ssb"},"olnNames":[{"value":"TM_0604"}]}],"alphafold_very_low_content":0.03546099290780142,"disorder_content":0.3120567375886525,"disprot_consensus":{"full":[{"start":38,"end":48,"type":"D"},{"start":109,"end":141,"type":"D"}],"Structural state":[{"start":38,"end":48,"type":"D"},{"start":109,"end":141,"type":"D"}],"Molecular function":[{"start":38,"end":48,"type":"F"},{"start":109,"end":141,"type":"F"}]}},{"features":{"pfam":[{"id":"PF07739","name":"TipAS antibiotic-recognition domain","start":131,"end":247},{"id":"PF13411","name":"MerR HTH family regulatory protein","start":3,"end":70}],"gene3D":[{"start":160,"end":253,"id":"1.10.490.50","name":"Antibiotic binding domain of TipA-like multidrug resistance regulators"},{"start":1,"end":140,"id":"1.10.1660.10","name":"1.10.1660.10"}]},"uniref50":"UniRef50_P0A4T9-2","sequence":"MSYSVGQVAGFAGVTVRTLHHYDDIGLLVPSERSHAGHRRYSDADLDRLQQILFYRELGFPLDEVAALLDDPAADPRAHLRRQHELLSARIGKLQKMAAAVEQAMEARSMGINLTPEEKFEVFGDFDPDQYEEEVRERWGNTDAYRQSKEKTASYTKEDWQRIQDEADELTRRFVALMDAGEPADSEGAMDAAEDHRQGIARNHYDCGYEMHTCLGEMYVSDERFTRNIDAAKPGLAAYMRDAILANAVRHTP","taxonomy":["Bacteria","Actinobacteria","Streptomycetales","Streptomycetaceae","Streptomyces"],"uniref90":"UniRef90_P0A4T9-2","disprot_id":"DP00997","ncbi_taxon_id":1916,"regions_counter":6,"creator":"ahatos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":159,"region_id":"DP00997r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis for antibiotic recognition by the TipA class of multidrug-resistance transcriptional regulators. <i> Kahmann JD, Sass HJ, Allan MG, Seto H, Thompson CJ, Grzesiek S. </i> EMBO J, 2003","term_id":"IDPO:0000002","curator_id":"ahatos","start":111,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1NY9"}],"reference_id":"12682015","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":159,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis for antibiotic recognition by the TipA class of multidrug-resistance transcriptional regulators. <i> Kahmann JD, Sass HJ, Allan MG, Seto H, Thompson CJ, Grzesiek S. </i> EMBO J, 2003","term_id":"GO:0005515","curator_id":"ahatos","start":111,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"12682015","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00997r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":159,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis for antibiotic recognition by the TipA class of multidrug-resistance transcriptional regulators. <i> Kahmann JD, Sass HJ, Allan MG, Seto H, Thompson CJ, Grzesiek S. </i> EMBO J, 2003","term_id":"IDPO:0000011","curator_id":"ahatos","start":111,"term_ontology":"IDPO","curator_name":"András Hatos","reference_id":"12682015","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP00997r006","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2016_10","uniref100":"UniRef100_P0A4T8","date":"2016-09-09T16:45:43.000Z","acc":"P0A4T9","name":"HTH-type transcriptional activator TipA","length":253,"organism":"Streptomyces lividans","dataset":[],"UniParc":"UPI0000136FB3","genes":[{"name":{"value":"tipA"}}],"alphafold_very_low_content":0.011857707509881422,"disorder_content":0.19367588932806323,"disprot_consensus":{"full":[{"start":111,"end":159,"type":"T"}],"Structural state":[{"start":111,"end":159,"type":"D"}],"Molecular function":[{"start":111,"end":159,"type":"F"}],"Structural transition":[{"start":111,"end":159,"type":"T"}]}},{"acc":"Q05127","sequence":"MTTRTKGRGHTAATTQNDRMPGPELSGWISEQLMTGRIPVSDIFCDIENNPGLCYASQMQQTKPNPKTRNSQTQTDPICNHSFEEVVQTLASLATVVQQQTIASESLEQRITSLENGLKPVYDMAKTISSLNRVCAEMVAKYDLLVMTTGRATATAAATEAYWAEHGQPPPGPSLYEESAIRGKIESRDETVPQSVREAFNNLNSTTSLTEENFGKPDISAKDLRNIMYDHLPGFGTAFHQLVQVICKLGKDSNSLDIIHAEFQASLAEGDSPQCALIQITKRVPIFQDAAPPVIHIRSRGDIPRACQKSLRPVPPSPKIDRGWVCVFQLQDGKTLGLKI","creator":"aschramm","dataset":["Viral proteins","RNA-binding proteins"],"date":"2016-09-09T16:49:56.000Z","disprot_id":"DP00998","features":{"pfam":[{"id":"PF02097","name":"Filoviridae VP35","start":20,"end":340}],"gene3D":[{"start":212,"end":288,"id":"1.10.8.950","name":"Filoviridae VP35, C-terminal inhibitory domain, helical subdomain","_id":"685af523b4ac24d5329d89c4"},{"start":289,"end":340,"id":"2.10.10.70","name":"Filoviridae VP35, C-terminal inhibitory domain, beta-sheet subdomain","_id":"685af523b4ac24d5329d89c5"}]},"genes":[{"name":{"value":"VP35","evidences":[],"_id":"685af523b4ac24d5329d8a02"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d8a01"}],"length":340,"name":"Polymerase cofactor VP35","ncbi_taxon_id":128952,"organism":"Zaire ebolavirus (strain Mayinga-76)","regions_counter":16,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Filoviridae","Ebolavirus"],"UniParc":"UPI000000135E","uniref100":"UniRef100_Q05127","uniref50":"UniRef50_Q05127","uniref90":"UniRef90_Q05127","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":20,"end":48,"interaction_partner":[],"reference_html":"An Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral RNA Synthesis by Modulating Nucleoprotein-RNA Interactions. <i> Leung DW, Borek D, Luthra P, Binning JM, Anantpadma M, Liu G, Harvey IB, Su Z, Endlich-Frazier A, Pan J, Shabman RS, Chiu W, Davey RA, Otwinowski Z, Basler CF, Amarasinghe GK. </i> Cell Rep, 2015","reference_id":"25865894","region_id":"DP00998r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"We also assessed the secondary structure of the NPBP peptide by circular dichroism (CD) spectroscopy, which revealed that NPBP and truncations of NPBP are intrinsically disordered in solution.","_id":"685af523b4ac24d5329d89c7"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-21T14:33:20.948Z","_id":"685af523b4ac24d5329d89c8"},"version":3,"_id":"685af523b4ac24d5329d89c6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"4YPI","_id":"685af523b4ac24d5329d89d2"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":20,"end":48,"interaction_partner":[{"db":"UniProt","id":"P18272","partner_start":244,"partner_end":383,"_id":"685af523b4ac24d5329d89d3"}],"reference_html":"An Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral RNA Synthesis by Modulating Nucleoprotein-RNA Interactions. <i> Leung DW, Borek D, Luthra P, Binning JM, Anantpadma M, Liu G, Harvey IB, Su Z, Endlich-Frazier A, Pan J, Shabman RS, Chiu W, Davey RA, Otwinowski Z, Basler CF, Amarasinghe GK. </i> Cell Rep, 2015","reference_id":"25865894","region_id":"DP00998r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"We solved the crystal structure of the VP35 NPBP/ΔNPNTD complex to 3.7 Å resolution by selenomethionine single wavelength anomalous dispersion (Se-SAD) and observed four NPBP/ΔNPNTD heterodimers in the asymmetric unit (termed molA, molB, molC, and molD for ΔNPNTD and molE, molF, molG, and molH for NPBP) (Figure 2D, Figure S3A and Table S1).","_id":"685af523b4ac24d5329d89d4"},{"type":"Results","text":"In the structure of molG/molC, NPBP interacts exclusively with the foot lobe of ΔNPNTD. NPBP forms two orthogonal helices (VP35 residues 26–36 form an alpha helix and residues 40–42 form a turn of a 310 helix) and makes multiple hydrogen bonds and non-bonded contacts with NP (Figure 3B–E).","_id":"685af523b4ac24d5329d89d5"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-21T14:45:08.284Z","_id":"685af523b4ac24d5329d89d6"},"version":4,"_id":"685af523b4ac24d5329d89d1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005647","ec_name":"isothermal titration calorimetry evidence used in manual assertion","ec_ontology":"ECO","start":20,"end":48,"interaction_partner":[{"db":"UniProt","id":"P18272","partner_start":25,"partner_end":457,"_id":"685af523b4ac24d5329d89d8"}],"reference_html":"An Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral RNA Synthesis by Modulating Nucleoprotein-RNA Interactions. <i> Leung DW, Borek D, Luthra P, Binning JM, Anantpadma M, Liu G, Harvey IB, Su Z, Endlich-Frazier A, Pan J, Shabman RS, Chiu W, Davey RA, Otwinowski Z, Basler CF, Amarasinghe GK. </i> Cell Rep, 2015","reference_id":"25865894","region_id":"DP00998r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"These results revealed that VP35 residues 20–48 (i.e. NPBP) comprise the most critical region for high affinity ΔNPNTD binding (KD=18.0 ± 6.0 nM at 500 mM NaCl, Figure 2C and S2B; and KD=28.9 ± 6.4 nM at 150 mM NaCl, Figure S2C).","_id":"685af523b4ac24d5329d89d9"},{"type":"Results","text":"Further analysis of the ITC data and MALS results indicates that NPBP binds to ΔNPNTD with a 1:1 stoichiometry (Figure S2B) with a complex molecular weight corresponding to one molecule of ΔNPNTD and one molecule of NPBP (Figure S2D).","_id":"685af523b4ac24d5329d89da"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-21T14:45:09.602Z","_id":"685af523b4ac24d5329d89db"},"version":1,"_id":"685af523b4ac24d5329d89d7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":20,"end":48,"interaction_partner":[{"db":"UniProt","id":"P18272","partner_start":25,"partner_end":457,"_id":"685af523b4ac24d5329d89dd"}],"reference_html":"An Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral RNA Synthesis by Modulating Nucleoprotein-RNA Interactions. <i> Leung DW, Borek D, Luthra P, Binning JM, Anantpadma M, Liu G, Harvey IB, Su Z, Endlich-Frazier A, Pan J, Shabman RS, Chiu W, Davey RA, Otwinowski Z, Basler CF, Amarasinghe GK. </i> Cell Rep, 2015","reference_id":"25865894","region_id":"DP00998r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Further analysis of the ITC data and MALS results indicates that NPBP binds to ΔNPNTD with a 1:1 stoichiometry (Figure S2B) with a complex molecular weight corresponding to one molecule of ΔNPNTD and one molecule of NPBP (Figure S2D).","_id":"685af523b4ac24d5329d89de"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-21T14:44:46.409Z","_id":"685af523b4ac24d5329d89df"},"version":1,"_id":"685af523b4ac24d5329d89dc","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0001220","ec_name":"in vivo transcription assay evidence used in manual assertion","ec_ontology":"ECO","start":20,"end":48,"interaction_partner":[],"reference_html":"An Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral RNA Synthesis by Modulating Nucleoprotein-RNA Interactions. <i> Leung DW, Borek D, Luthra P, Binning JM, Anantpadma M, Liu G, Harvey IB, Su Z, Endlich-Frazier A, Pan J, Shabman RS, Chiu W, Davey RA, Otwinowski Z, Basler CF, Amarasinghe GK. </i> Cell Rep, 2015","reference_id":"25865894","region_id":"DP00998r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In contrast, residues 20–52 are critical for EBOV MG activity as N-terminal truncations that extend into this conserved region, including truncations such as in the 30–340 construct, resulted in >60% loss of activity relative to WT VP35 (residues 1–340). Deletion of the entire NPBP region plus the first 19 amino acids results in near-complete loss of MG activity, suggesting that the entire NPBP is required for activity.","_id":"685af523b4ac24d5329d89e1"}],"states_connection":[],"term_comment":"","term_def":"\"The process by which a viral genome, or part of a viral genome, is transcribed within the host cell.\" [GOC:jl, ISBN:0781702534]","term_id":"GO:0019083","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral transcription","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-21T14:45:22.326Z","_id":"685af523b4ac24d5329d89e2"},"version":1,"_id":"685af523b4ac24d5329d89e0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"4YPI","_id":"685af523b4ac24d5329d89e4"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":26,"end":36,"interaction_partner":[],"reference_html":"An Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral RNA Synthesis by Modulating Nucleoprotein-RNA Interactions. <i> Leung DW, Borek D, Luthra P, Binning JM, Anantpadma M, Liu G, Harvey IB, Su Z, Endlich-Frazier A, Pan J, Shabman RS, Chiu W, Davey RA, Otwinowski Z, Basler CF, Amarasinghe GK. </i> Cell Rep, 2015","reference_id":"25865894","region_id":"DP00998r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"NPBP forms two orthogonal helices (VP35 residues 26–36 form an alpha helix and residues 40–42 form a turn of a 310 helix) and makes multiple hydrogen bonds and non-bonded contacts with NP (Figure 3B–E).","_id":"685af523b4ac24d5329d89e5"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-21T14:34:54.459Z","_id":"685af523b4ac24d5329d89e6"},"version":1,"_id":"685af523b4ac24d5329d89e3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006309","ec_name":"competitive binding evidence used in manual assertion","ec_ontology":"ECO","start":20,"end":48,"interaction_partner":[],"reference_html":"An Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral RNA Synthesis by Modulating Nucleoprotein-RNA Interactions. <i> Leung DW, Borek D, Luthra P, Binning JM, Anantpadma M, Liu G, Harvey IB, Su Z, Endlich-Frazier A, Pan J, Shabman RS, Chiu W, Davey RA, Otwinowski Z, Basler CF, Amarasinghe GK. </i> Cell Rep, 2015","reference_id":"25865894","region_id":"DP00998r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In these experiments, NPBP was titrated into the reaction while ssRNA and ΔNPNTD concentrations were held constant. Increasing NPBP concentration resulted in a proportional loss of ssRNA from the ssRNA-NP complex (Figure 5D), yielding an IC50 of 4 μM. These results indicate that ssRNA and NPBP binding to NP are mutually exclusive.","_id":"685af523b4ac24d5329d89e8"},{"type":"Results","text":"ΔNPNTD binds ssRNA and the ssRNA binding is inhibited by NPBP","_id":"685af523b4ac24d5329d89e9"}],"states_connection":[],"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","term_id":"GO:0140313","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular sequestering activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-21T14:45:34.823Z","_id":"685af523b4ac24d5329d89ea"},"version":1,"_id":"685af523b4ac24d5329d89e7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006309","ec_name":"competitive binding evidence used in manual assertion","ec_ontology":"ECO","start":20,"end":48,"interaction_partner":[{"db":"UniProt","id":"P18272","partner_start":25,"partner_end":457,"_id":"685af523b4ac24d5329d89ec"}],"reference_html":"An Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral RNA Synthesis by Modulating Nucleoprotein-RNA Interactions. <i> Leung DW, Borek D, Luthra P, Binning JM, Anantpadma M, Liu G, Harvey IB, Su Z, Endlich-Frazier A, Pan J, Shabman RS, Chiu W, Davey RA, Otwinowski Z, Basler CF, Amarasinghe GK. </i> Cell Rep, 2015","reference_id":"25865894","region_id":"DP00998r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In these experiments, NPBP was titrated into the reaction while ssRNA and ΔNPNTD concentrations were held constant. Increasing NPBP concentration resulted in a proportional loss of ssRNA from the ssRNA-NP complex (Figure 5D), yielding an IC50 of 4 μM. These results indicate that ssRNA and NPBP binding to NP are mutually exclusive.","_id":"685af523b4ac24d5329d89ed"},{"type":"Results","text":"ΔNPNTD binds ssRNA and the ssRNA binding is inhibited by NPBP","_id":"685af523b4ac24d5329d89ee"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-21T14:43:45.120Z","_id":"685af523b4ac24d5329d89ef"},"version":1,"_id":"685af523b4ac24d5329d89eb","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":20,"end":48,"interaction_partner":[],"reference_html":"An Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral RNA Synthesis by Modulating Nucleoprotein-RNA Interactions. <i> Leung DW, Borek D, Luthra P, Binning JM, Anantpadma M, Liu G, Harvey IB, Su Z, Endlich-Frazier A, Pan J, Shabman RS, Chiu W, Davey RA, Otwinowski Z, Basler CF, Amarasinghe GK. </i> Cell Rep, 2015","reference_id":"25865894","region_id":"DP00998r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In contrast to previous results for the peptide-free NP proteins (Figure 1B–C), which eluted at the V0, all NPBP-bound NP proteins eluted at a volume consistent with a well-behaved heterodimer (one molecule of NP and one NPBP molecule) (Figure 6C), indicating that NPBP interaction also prevents oligomerization.","_id":"685af523b4ac24d5329d89f1"}],"states_connection":[],"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","term_id":"GO:0140313","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular sequestering activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-21T14:45:19.170Z","_id":"685af523b4ac24d5329d89f2"},"version":1,"_id":"685af523b4ac24d5329d89f0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-09T08:14:00.480Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005647","ec_name":"isothermal titration calorimetry evidence used in manual assertion","ec_ontology":"ECO","start":20,"end":48,"interaction_partner":[{"db":"UniProt","id":"P18272","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d89f6"}],"reference_html":"An Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral RNA Synthesis by Modulating Nucleoprotein-RNA Interactions. <i> Leung DW, Borek D, Luthra P, Binning JM, Anantpadma M, Liu G, Harvey IB, Su Z, Endlich-Frazier A, Pan J, Shabman RS, Chiu W, Davey RA, Otwinowski Z, Basler CF, Amarasinghe GK. </i> Cell Rep, 2015","reference_id":"25865894","region_id":"DP00998r014","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"These results revealed that VP35 residues 20–48 (i.e. NPBP) comprise the most critical region for high affinity ΔNPNTD binding (KD=18.0 ± 6.0 nM at 500 mM NaCl, Figure 2C and S2B; and KD=28.9 ± 6.4 nM at 150 mM NaCl, Figure S2C).","_id":"685af523b4ac24d5329d89f4"},{"type":"Results","text":"Further analysis of the ITC data and MALS results indicates that NPBP binds to ΔNPNTD with a 1:1 stoichiometry (Figure S2B) with a complex molecular weight corresponding to one molecule of ΔNPNTD and one molecule of NPBP (Figure S2D).","_id":"685af523b4ac24d5329d89f5"}],"states_connection":[],"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","term_id":"GO:0140313","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular sequestering activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-30T19:47:45.701Z","_id":"685af523b4ac24d5329d89f7"},"version":2,"_id":"685af523b4ac24d5329d89f3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"4YPI","_id":"685af523b4ac24d5329d89f9"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":20,"end":48,"interaction_partner":[],"reference_html":"An Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral RNA Synthesis by Modulating Nucleoprotein-RNA Interactions. <i> Leung DW, Borek D, Luthra P, Binning JM, Anantpadma M, Liu G, Harvey IB, Su Z, Endlich-Frazier A, Pan J, Shabman RS, Chiu W, Davey RA, Otwinowski Z, Basler CF, Amarasinghe GK. </i> Cell Rep, 2015","reference_id":"25865894","region_id":"DP00998r015","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"We solved the crystal structure of the VP35 NPBP/ΔNPNTD complex to 3.7 Å resolution by selenomethionine single wavelength anomalous dispersion (Se-SAD) and observed four NPBP/ΔNPNTD heterodimers in the asymmetric unit (termed molA, molB, molC, and molD for ΔNPNTD and molE, molF, molG, and molH for NPBP) (Figure 2D, Figure S3A and Table S1).","_id":"685af523b4ac24d5329d89fa"},{"type":"Results","text":"In the structure of molG/molC, NPBP interacts exclusively with the foot lobe of ΔNPNTD. NPBP forms two orthogonal helices (VP35 residues 26–36 form an alpha helix and residues 40–42 form a turn of a 310 helix) and makes multiple hydrogen bonds and non-bonded contacts with NP (Figure 3B–E).","_id":"685af523b4ac24d5329d89fb"}],"states_connection":[],"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","term_id":"GO:0140313","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular sequestering activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-21T14:45:14.183Z","_id":"685af523b4ac24d5329d89fc"},"version":1,"_id":"685af523b4ac24d5329d89f8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-09T08:15:16.391Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006323","ec_name":"fluorescence microscopy evidence used in manual assertion","ec_ontology":"ECO","start":20,"end":48,"interaction_partner":[],"reference_html":"An Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral RNA Synthesis by Modulating Nucleoprotein-RNA Interactions. <i> Leung DW, Borek D, Luthra P, Binning JM, Anantpadma M, Liu G, Harvey IB, Su Z, Endlich-Frazier A, Pan J, Shabman RS, Chiu W, Davey RA, Otwinowski Z, Basler CF, Amarasinghe GK. </i> Cell Rep, 2015","reference_id":"25865894","region_id":"DP00998r016","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"VP35 NPBP inhibits Ebola RNA synthesis","_id":"685af523b4ac24d5329d89fe"},{"type":"Results","text":"To further test activity of NPBP in the context of EBOV infections, HeLa cells were pretransfected with the GFP-NPBP or GFP-control peptide constructs and then challenged with EBOV. Representative images of these infections show that GFP-NPBP, but not the GFP control plasmid was able to inhibit EBOV replication (Figure 7D). Consistent with the immunofluorescence results and with the MG assays, quantitative reverse transcription-PCR (qRT-PCR) results show that the presence of GFP-VP35 NPBP, but not the GFP-control, results in lower viral RNA in the cell supernatants (Figure 7E). Collectively, these results suggest that NPBP can functionally interact with the NP in the viral RDRP complex and has the potential to inhibit viral RNA synthesis.","_id":"685af523b4ac24d5329d89ff"}],"states_connection":[],"term_comment":"","term_def":"\"Any process involved directly in viral genome replication, including viral nucleotide metabolism.\" [ISBN:0781702534]","term_go_domain":"P","term_id":"GO:0019079","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral genome replication","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-30T19:45:06.023Z","_id":"685af523b4ac24d5329d8a00"},"version":2,"_id":"685af523b4ac24d5329d89fd","reference_source":"pmid"}],"__v":0,"disorder_content":0.08529411764705883,"disprot_consensus":{"full":[{"start":20,"end":25,"type":"D"},{"start":26,"end":36,"type":"T"},{"start":37,"end":48,"type":"D"}],"Structural state":[{"start":20,"end":48,"type":"D"}],"Molecular function":[{"start":20,"end":48,"type":"F"}],"Biological process":[{"start":20,"end":48,"type":"F"}],"Structural transition":[{"start":26,"end":36,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00943","name":"Alphavirus E2 glycoprotein","start":347,"end":749},{"id":"PF00944","name":"Alphavirus core protein","start":112,"end":268},{"id":"PF01563","name":"Alphavirus E3 glycoprotein","start":275,"end":333},{"id":"PF01589","name":"Alphavirus E1 glycoprotein","start":751,"end":1253}],"gene3D":[{"start":339,"end":600,"id":"2.60.40.3200","name":"Alphavirus E2 glycoprotein, A domain"},{"start":1042,"end":1106,"id":"2.60.98.10","name":"Tick-borne Encephalitis virus Glycoprotein, domain 1"},{"start":931,"end":993,"id":"2.60.98.10","name":"Tick-borne Encephalitis virus Glycoprotein, domain 1"},{"start":509,"end":563,"id":"3.30.1490.280","name":"Alphavirus E2 glycoprotein, domain B"},{"start":602,"end":689,"id":"2.60.40.2400","name":"Alphavirus E2 glycoprotein, domain C"},{"start":1107,"end":1206,"id":"2.60.40.350","name":"2.60.40.350"},{"start":816,"end":890,"id":"2.60.98.10","name":"Tick-borne Encephalitis virus Glycoprotein, domain 1"},{"start":119,"end":182,"id":"2.40.10.10","name":"Trypsin-like serine proteases"},{"start":183,"end":267,"id":"2.40.10.10","name":"Trypsin-like serine proteases"}]},"uniref50":"UniRef50_P03315","sequence":"MNYIPTQTFYGRRWRPRPAARPWPLQATPVAPVVPDFQAQQMQQLISAVNALTMRQNAIAPARPPKPKKKKTTKPKPKTQPKKINGKTQQQKKKDKQADKKKKKPGKRERMCMKIENDCIFEVKHEGKVTGYACLVGDKVMKPAHVKGVIDNADLAKLAFKKSSKYDLECAQIPVHMRSDASKYTHEKPEGHYNWHHGAVQYSGGRFTIPTGAGKPGDSGRPIFDNKGRVVAIVLGGANEGSRTALSVVTWNKDMVTRVTPEGSEEWSAPLITAMCVLANATFPCFQPPCVPCCYENNAEATLRMLEDNVDRPGYYDLLQAALTCRNGTRHRRSVSQHFNVYKATRPYIAYCADCGAGHSCHSPVAIEAVRSEATDGMLKIQFSAQIGIDKSDNHDYTKIRYADGHAIENAVRSSLKVATSGDCFVHGTMGHFILAKCPPGEFLQVSIQDTRNAVRACRIQYHHDPQPVGREKFTIRPHYGKEIPCTTYQQTTAETVEEIDMHMPPDTPDRTLLSQQSGNVKITVGGKKVKYNCTCGTGNVGTTNSDMTINTCLIEQCHVSVTDHKKWQFNSPFVPRADEPARKGKVHIPFPLDNITCRVPMAREPTVIHGKREVTLHLHPDHPTLFSYRTLGEDPQYHEEWVTAAVERTIPVPVDGMEYHWGNNDPVRLWSQLTTEGKPHGWPHQIVQYYYGLYPAATVSAVVGMSLLALISIFASCYMLVAARSKCLTPYALTPGAAVPWTLGILCCAPRAHAASVAETMAYLWDQNQALFWLEFAAPVACILIITYCLRNVLCCCKSLSFLVLLSLGATARAYEHSTVMPNVVGFPYKAHIERPGYSPLTLQMQVVETSLEPTLNLEYITCEYKTVVPSPYVKCCGASECSTKEKPDYQCKVYTGVYPFMWGGAYCFCDSENTQLSEAYVDRSDVCRHDHASAYKAHTASLKAKVRVMYGNVNQTVDVYVNGDHAVTIGGTQFIFGPLSSAWTPFDNKIVVYKDEVFNQDFPPYGSGQPGRFGDIQSRTVESNDLYANTALKLARPSPGMVHVPYTQTPSGFKYWLKEKGTALNTKAPFGCQIKTNPVRAMNCAVGNIPVSMNLPDSAFTRIVEAPTIIDLTCTVATCTHSSDFGGVLTLTYKTNKNGDCSVHSHSNVATLQEATAKVKTAGKVTLHFSTASASPSFVVSLCSARATCSASCEPPKDHIVPYAASHSNVVFPDMSGTALSWVQKISGGLGAFAIGAILVLVVVTCIGLRR","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Alsuviricetes","Martellivirales","Togaviridae","Alphavirus"],"uniref90":"UniRef90_P03315","disprot_id":"DP00999","ncbi_taxon_id":11033,"regions_counter":6,"creator":"aschramm","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":260,"region_id":"DP00999r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Novel enzymatic activity derived from the Semliki Forest virus capsid protein. <i> Morillas M, Eberl H, Allain FH, Glockshuber R, Kuennemann E. </i> J Mol Biol, 2008","term_id":"IDPO:0000003","curator_id":"aschramm","start":119,"term_ontology":"IDPO","curator_name":"Antoine Schramm","reference_id":"18177892","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"molten globule","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":260,"term_name":"small molecule binding","start":119,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"aschramm","released":"2022_03","term_ontology":"GO","curator_name":"Antoine Schramm","reference_id":"18177892","version":3,"reference_html":"Novel enzymatic activity derived from the Semliki Forest virus capsid protein. <i> Morillas M, Eberl H, Allain FH, Glockshuber R, Kuennemann E. </i> J Mol Biol, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0036094","ec_id":"ECO:0006165","region_id":"DP00999r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":260,"region_id":"DP00999r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Novel enzymatic activity derived from the Semliki Forest virus capsid protein. <i> Morillas M, Eberl H, Allain FH, Glockshuber R, Kuennemann E. </i> J Mol Biol, 2008","term_id":"IDPO:0000003","curator_id":"aschramm","start":119,"term_ontology":"IDPO","curator_name":"Antoine Schramm","reference_id":"18177892","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"molten globule","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":260,"term_name":"small molecule binding","start":119,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"aschramm","released":"2022_03","term_ontology":"GO","curator_name":"Antoine Schramm","reference_id":"18177892","version":3,"reference_html":"Novel enzymatic activity derived from the Semliki Forest virus capsid protein. <i> Morillas M, Eberl H, Allain FH, Glockshuber R, Kuennemann E. </i> J Mol Biol, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0036094","ec_id":"ECO:0006204","region_id":"DP00999r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":260,"region_id":"DP00999r005","released":"2022_03","ec_id":"ECO:0006206","reference_html":"Novel enzymatic activity derived from the Semliki Forest virus capsid protein. <i> Morillas M, Eberl H, Allain FH, Glockshuber R, Kuennemann E. </i> J Mol Biol, 2008","term_id":"IDPO:0000003","curator_id":"aschramm","start":119,"term_ontology":"IDPO","curator_name":"Antoine Schramm","reference_id":"18177892","version":2,"ec_name":"near-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"molten globule","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":260,"term_name":"small molecule binding","start":119,"ec_name":"near-UV circular dichroism evidence used in manual assertion","curator_id":"aschramm","released":"2022_03","term_ontology":"GO","curator_name":"Antoine Schramm","reference_id":"18177892","version":3,"reference_html":"Novel enzymatic activity derived from the Semliki Forest virus capsid protein. <i> Morillas M, Eberl H, Allain FH, Glockshuber R, Kuennemann E. </i> J Mol Biol, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0036094","ec_id":"ECO:0006206","region_id":"DP00999r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P03315","date":"2016-09-09T17:13:03.000Z","acc":"P03315","name":"Structural polyprotein","length":1253,"organism":"Semliki forest virus","dataset":["Viral proteins"],"UniParc":"UPI0000131EBF","genes":[],"disorder_content":0.11332801276935354,"disprot_consensus":{"full":[{"start":119,"end":260,"type":"D"}],"Structural state":[{"start":119,"end":260,"type":"D"}],"Molecular function":[{"start":119,"end":260,"type":"F"}]}},{"features":{"pfam":[{"id":"PF12136","name":"RNA polymerase Rpo13 subunit HTH domain","start":21,"end":59}]},"uniref50":"UniRef50_B8YB65","sequence":"MVSGMSTEEEKEGTNDEEVSEEREVEETSEEEFPKLSIQDIELLMKNTEIWDNLLNGKISVDEAKRLFEDNYKDYEKRDSRRKAKKAASKKVKKTKKKEKSVEG","taxonomy":["Archaea","Crenarchaeota","Thermoprotei","Sulfolobales","Sulfolobaceae","Saccharolobus"],"uniref90":"UniRef90_B8YB65","disprot_id":"DP01001","ncbi_taxon_id":523848,"regions_counter":11,"creator":"zdosztanyi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":32,"region_id":"DP01001r001","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Structural and functional analyses of the interaction of archaeal RNA polymerase with DNA. <i> Wojtas MN, Mogni M, Millet O, Bell SD, Abrescia NG. </i> Nucleic Acids Res, 2012","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-23T14:47:08.666Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4AYB"}],"reference_id":"22848102","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The core of Rpo13 forms a HTH comprising helix-1 (α1; residues 38–56) and helix-2 (α2; residues 61–82) with the first visible Cα N-terminal residue (F33) facing the DNA-binding cleft (Figure 4B).","type":"Results"},{"text":"The PDB structure is about the archaeal RNA polymerase complex and involve many other proteins.","type":"Curator statement"}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":104,"term_name":"double-stranded DNA binding","released":"2023_12","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","reference_html":"Structural and functional analyses of the interaction of archaeal RNA polymerase with DNA. <i> Wojtas MN, Mogni M, Millet O, Bell SD, Abrescia NG. </i> Nucleic Acids Res, 2012","term_id":"GO:0003690","curator_id":"vnugnes","start":85,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"22848102","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-23T15:32:57.185Z","reference_source":"pmid","ec_id":"ECO:0001807","region_id":"DP01001r004","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to double-stranded DNA.\" [GOC:elh, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"statement":[{"text":"Finally, using EMSAs (Figure 6) we could readily detect interaction between purified recombinant Rpo13 and dsDNA with an apparent Kd of ∼2 µM, consistent with our NMR data (Figure 5B). We could not detect any significant single stranded DNA (ssDNA) binding activity (Figure 6A, left).","type":"Results"},{"text":"Deletion of the N-terminal tail rendered the protein prone to aggregation, but DNA binding was still detectable at low concentrations (Figure 6C, top). Importantly, however, deletion of the C-terminal tail (amino acids 85–104) had no detectable effect on protein stability or solubility but abrogated DNA binding (Figure 6C, below).","type":"Results"}],"interaction_partner":[{"db":"ENA","id":"CP033241","operator":"and","partner_start":null,"partner_end":null}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":104,"region_id":"DP01001r005","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Structural and functional analyses of the interaction of archaeal RNA polymerase with DNA. <i> Wojtas MN, Mogni M, Millet O, Bell SD, Abrescia NG. </i> Nucleic Acids Res, 2012","term_id":"IDPO:0000002","curator_id":"vnugnes","start":83,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-23T14:47:16.305Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4AYB"}],"reference_id":"22848102","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The core of Rpo13 forms a HTH comprising helix-1 (α1; residues 38–56) and helix-2 (α2; residues 61–82) with the first visible Cα N-terminal residue (F33) facing the DNA-binding cleft (Figure 4B).","type":"Results"},{"text":"The PDB structure is about the archaeal RNA polymerase complex and involve many other proteins.","type":"Curator statement"}]},{"term_namespace":"Cellular component","ec_ontology":"ECO","end":104,"term_name":"DNA-directed RNA polymerase complex","released":"2023_12","ec_name":"chromatin immunoprecipitation-chip evidence used in manual assertion","reference_html":"Structural and functional analyses of the interaction of archaeal RNA polymerase with DNA. <i> Wojtas MN, Mogni M, Millet O, Bell SD, Abrescia NG. </i> Nucleic Acids Res, 2012","term_id":"GO:0000428","curator_id":"vnugnes","start":1,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"22848102","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-23T15:29:04.752Z","reference_source":"pmid","ec_id":"ECO:0006007","region_id":"DP01001r006","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A protein complex that possesses DNA-directed RNA polymerase activity.\" [GOC:krc]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"B8YB53","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"B8YB54","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"B8YB56","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"B8YB57","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"B8YB58","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"B8YB59","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"B8YB60","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"B8YB61","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"B8YB62","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"B8YB63","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"B8YB64","operator":"and","partner_start":null,"partner_end":null}],"statement":[{"text":"We also detect elevated signals of both proteins in some intragenic regions, perhaps indicative of polymerase pausing [an extensive genome-wide analysis will be published elsewhere (M.M. and S.D.B., unpublished data)]. Taken together, these data indicate that Rpo13 co-localizes with elongating RNAP.","type":"Results"},{"text":"The co-purification and crystallization of Rpo13 with RNAP clearly indicates a stable association in solution.","type":"Results"}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":52,"term_name":"RNA polymerase binding","released":"2023_12","ec_name":"x-ray crystallography evidence used in manual assertion","reference_html":"Structural and functional analyses of the interaction of archaeal RNA polymerase with DNA. <i> Wojtas MN, Mogni M, Millet O, Bell SD, Abrescia NG. </i> Nucleic Acids Res, 2012","term_id":"GO:0070063","curator_id":"vnugnes","start":47,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"22848102","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-23T15:22:22.039Z","reference_source":"pmid","ec_id":"ECO:0005670","region_id":"DP01001r007","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA polymerase molecule or complex.\" [GOC:BHF, GOC:mah, GOC:txnOH]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"4AYB"}],"statement":[{"text":"Residues N47 and W51 with T48 and D52 of Rpo13’s α1 confer specificity for binding to the RNAP. The former amino acids bind to the Rpo5 subunit and the latter two to the clamp-head domain of Rpo1N. Two tryptophan residues, one from Rpo13 (W51) and the other from the clamp-head (W125) reciprocally dock via hydrogen bonds onto G60 of Rpo5 and T48 of Rpo13, respectively (Figure 4B). Further hydrogen bonds between Rpo13 N47 and P58 of Rpo5 and Rpo13 D52 and R124 of the clamp-head domain strengthen the binding of Rpo13 to the crevice formed by Rpo5 and the clamp head (Figure 4B).","type":"Results"}]},{"start":1,"end":32,"reference_id":"22848102","reference_source":"pmid","reference_html":"Structural and functional analyses of the interaction of archaeal RNA polymerase with DNA. <i> Wojtas MN, Mogni M, Millet O, Bell SD, Abrescia NG. </i> Nucleic Acids Res, 2012","date":"2023-08-23T14:51:23.341Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01001r009","statement":[{"text":"CD spectroscopy in the far UV region on Rpo13 reveals a protein with ∼35% α-helical, 48% random coil and 17% beta-sheet content (Figure 5A, left; Supplementary Methods). This secondary structure assignment of Rpo13 in solution fits the X-ray secondary structural description of Rpo13 bound to the entire enzyme where only 39 residues out of 104 are ordered.","type":"Results"}]},{"start":83,"end":104,"reference_id":"22848102","reference_source":"pmid","reference_html":"Structural and functional analyses of the interaction of archaeal RNA polymerase with DNA. <i> Wojtas MN, Mogni M, Millet O, Bell SD, Abrescia NG. </i> Nucleic Acids Res, 2012","date":"2023-08-23T14:51:32.174Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01001r010","statement":[{"text":"CD spectroscopy in the far UV region on Rpo13 reveals a protein with ∼35% α-helical, 48% random coil and 17% beta-sheet content (Figure 5A, left; Supplementary Methods). This secondary structure assignment of Rpo13 in solution fits the X-ray secondary structural description of Rpo13 bound to the entire enzyme where only 39 residues out of 104 are ordered.","type":"Results"}]},{"start":1,"end":104,"reference_id":"22848102","reference_source":"pmid","reference_html":"Structural and functional analyses of the interaction of archaeal RNA polymerase with DNA. <i> Wojtas MN, Mogni M, Millet O, Bell SD, Abrescia NG. </i> Nucleic Acids Res, 2012","date":"2023-08-23T14:54:55.477Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01001r011","statement":[{"text":"Full-length Rpo13 was also studied by NMR spectroscopy (Supplemental Methods). The 1H–15N–HSQC spectrum (Figure 5B) shows a poor dispersion in the proton chemical shift, indicating a loss in both secondary and tertiary structure. Interestingly, the analysis of the peaks cannot account for all residues (even considering signal overlap) and the spectrum is showing resonances for a subset of residues only. The missing peaks that include the tryptophan residue used for the specific interaction with Rpo1N, may have disappeared because of conformational exchange in the microsecond–millisecond timescale or because of segmental aggregation. This complex behaviour implies a molten globular structure that undergoes exchange between several conformations.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_B8YB65","date":"2016-09-09T17:40:40.000Z","acc":"B8YB65","name":"RNA polymerase subunit 13","length":104,"organism":"Saccharolobus shibatae B12","dataset":[],"UniParc":"UPI00019220B8","genes":[{"name":{"value":"rpo13","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"19419240","url":"http://www.ncbi.nlm.nih.gov/pubmed/19419240","alternativeUrl":"https://europepmc.org/abstract/MED/19419240"}}]}}],"alphafold_very_low_content":0.2403846153846154,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":104,"type":"D"}],"Structural state":[{"start":1,"end":104,"type":"D"}],"Molecular function":[{"start":47,"end":52,"type":"F"},{"start":85,"end":104,"type":"F"}],"Cellular component":[{"start":1,"end":104,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03498","name":"Cytolethal distending toxin A/C domain","start":76,"end":219}],"gene3D":[{"start":57,"end":222,"id":"2.80.10.50","name":"2.80.10.50"}]},"uniref50":"UniRef50_O06522","sequence":"MKKFLPGLLLMGLVACSSNQRMSDYSQPESQSDLAPKSSTTQFQPQPLLSKASSMPLNLLSSSKNGQVSPSEPSNFMTLMGQNGALLTVWALAKRNWLWAYPNIYSQDFGNIRNWKIEPGKHREYFRFVNQSLGTCIEAYGNGLIHDTCSLDKLAQEFELLPTDSGAVVIKSVSQGRCVTYNPVSPTYYSTVTLSTCDGATEPLRDQTWYLAPPVLEATAVN","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Pasteurellales","Pasteurellaceae","Aggregatibacter"],"uniref90":"UniRef90_O06522","disprot_id":"DP01002","dataset":["Unicellular toxins and antitoxins","Bacterial virulence-related proteins"],"ncbi_taxon_id":714,"regions_counter":3,"creator":"lkalmar","regions":[{"region_id":"DP01002r003","validated":{"curator_id":"bmesza","timestamp":"2020-12-15T11:23:39.549Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":70,"term_id":"IDPO:0000002","start":53,"version":3,"statement":[{"text":"(2Fo − Fc) and (Fo − Fc) maps showed that the N-termini of CdtA, CdtB, and CdtC started at residues 71, 23, and 25, respectively, indicating that the residues 53–70 of CdtA and residues 21–24 of CdtC are disordered in the crystal structure.","type":"Methods"},{"text":"The most variable region is from residue 63 to 70 (63SKNGQVSP70 vs. 63SGPNRQVLP70) (A1 in Fig. 3​3).). The N terminus of aCdtA is disordered up to residue 70 (i.e., residues 53–70 are disordered), indicating that these residues are not strongly associated with the main body.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"16434747","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2F2F"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"rpancsa","reference_html":"Variation of loop sequence alters stability of cytolethal distending toxin (CDT): crystal structure of CDT from Actinobacillus actinomycetemcomitans. <i> Yamada T, Komoto J, Saiki K, Konishi K, Takusagawa F. </i> Protein Sci, 2006","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_O87120","date":"2016-09-09T17:49:27.000Z","acc":"O87120","name":"Cytolethal distending toxin subunit A","length":222,"organism":"Aggregatibacter actinomycetemcomitans","UniParc":"UPI000012746A","genes":[{"name":{"value":"cdtA"}}],"alphafold_very_low_content":0.18468468468468469,"disorder_content":0.08108108108108109,"disprot_consensus":{"full":[{"start":53,"end":70,"type":"D"}],"Structural state":[{"start":53,"end":70,"type":"D"}]}},{"features":{"pfam":[{"id":"PF09274","name":"ParG","start":1,"end":76}],"gene3D":[{"start":1,"end":76,"id":"1.10.1220.10","name":"Met repressor-like"}]},"uniref50":"UniRef50_Q70W75","sequence":"MSLEKAHTSVKKMTFGENRDLERVVTAPVSSGKIKRVNVNFDEEKHTRFKAACARKGTSITDVVNQLVDNWLKENE","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"],"uniref90":"UniRef90_B0EYM2","disprot_id":"DP01004","ncbi_taxon_id":108619,"regions_counter":4,"creator":"zdosztanyi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":32,"region_id":"DP01004r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"ParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structure. <i> Golovanov AP, Barillà D, Golovanova M, Hayes F, Lian LY. </i> Mol Microbiol, 2003","term_id":"IDPO:0000002","curator_id":"zdosztanyi","start":1,"term_ontology":"IDPO","curator_name":"Zsuzsanna Dosztányi","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1P94"}],"reference_id":"14622405","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":32,"term_name":"molecular function regulator","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"ParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structure. <i> Golovanov AP, Barillà D, Golovanova M, Hayes F, Lian LY. </i> Mol Microbiol, 2003","term_id":"GO:0098772","curator_id":"zdosztanyi","start":1,"term_ontology":"GO","curator_name":"Zsuzsanna Dosztányi","reference_id":"14622405","version":3,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01004r002","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":32,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"ParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structure. <i> Golovanov AP, Barillà D, Golovanova M, Hayes F, Lian LY. </i> Mol Microbiol, 2003","term_id":"GO:0005515","curator_id":"zdosztanyi","start":1,"term_ontology":"GO","curator_name":"Zsuzsanna Dosztányi","reference_id":"14622405","version":3,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01004r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":32,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"ParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structure. <i> Golovanov AP, Barillà D, Golovanova M, Hayes F, Lian LY. </i> Mol Microbiol, 2003","term_id":"GO:0003676","curator_id":"zdosztanyi","start":1,"term_ontology":"GO","curator_name":"Zsuzsanna Dosztányi","reference_id":"14622405","version":3,"curator_orcid":"0000-0002-3624-5937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01004r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_B0ZE05","date":"2016-09-09T19:01:08.000Z","acc":"Q9KJ82","name":"Plasmid partition protein ParG","length":76,"organism":"Salmonella newport","dataset":[],"UniParc":"UPI00000B6707","genes":[{"name":{"value":"parG","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF74218.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF74218.1"}}]}}],"alphafold_very_low_content":0.02631578947368421,"disorder_content":0.42105263157894735,"disprot_consensus":{"full":[{"start":1,"end":32,"type":"D"}],"Structural state":[{"start":1,"end":32,"type":"D"}],"Molecular function":[{"start":1,"end":32,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00651","name":"BTB/POZ domain","start":27,"end":132},{"id":"PF03131","name":"bZIP Maf transcription factor","start":617,"end":694}],"gene3D":[{"start":585,"end":672,"id":"1.10.880.10","name":"Transcription factor, Skn-1-like, DNA-binding domain"},{"start":9,"end":137,"id":"3.30.710.10","name":"Potassium Channel Kv1.1; Chain A"}]},"uniref50":"UniRef50_Q9BYV9","sequence":"MSVDEKPGSPMYVYESTVHCANILLGLNDQRKKDILCDVTLIVERKEFRAHRAVLAACSEYFWQALVGQTKDDLVVSLPEEVTARGFGPLLQFAYTAKLLLSRENIREVIRCAEFLRMHNLEDSCFSFLQTQLLNREDGLFVCRKDSACQRPQEDHGNSAGEEEEEEETMDSETARMACATDQMLPDPISFEATAIPVAEKEEALLPESEVPTDTKENSEKGALTQYPRYKKYQLACTKNVYSAPSHGTSGFASTFSEDSPGNSLKPGLPMGQIKSEPPSEETEEESITLCLSGDETDIKDRPGDVEMDRKQPSPAPTPSTPTGAACLDRSRSVSSPSCLRSLFGITKGVESTGLPSTSQQPLVRSSACPFNKGISQGDLKTDYTPLAGNYGQPHVGQKDVSNFAMGSPLRGPGPETLCKQEGELDRRSVIFSASACDQPNTPVHSYSAVSNLDKDLSEPVPKSLWVGAGQSLPSSQAYSHSGLMADHLPGRIRPNTSCPVPIKVCPRSPPLETRTRTSSSCSSYSYAEDGSGGSPCSLPLCEFSSSPCSQGARFLATEHQEPGLMGDGMYNQVRPQIKCEQSYGTNSSDESGSFSEADSESCPVQDRGQEVKLPFPVDQITDLPRNDFQMMIKMHKLTSEQLEFIHDIRRRSKNRIAAQRCRKRKLDCIQNLECEIRKLVCEKEKLLSERNHLKACMGELLDNFSCLSQEVCRDIQSPEQIQALHRYCPVLIPMDLPGASVNPPPVGVEQSLAPSPCAVGGSVPCCLEPGAAPPGLPWVPSNTSENCTSGRRLEGSDPGTFSERGPPLEARSQSVTVDFCQEMTEKCTTDEQPRKDYA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P97303","disprot_id":"DP01009","ncbi_taxon_id":10090,"regions_counter":4,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":520,"region_id":"DP01009r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Heme binds to an intrinsically disordered region of Bach2 and alters its conformation. <i> Watanabe-Matsui M, Matsumoto T, Matsui T, Ikeda-Saito M, Muto A, Murayama K, Igarashi K. </i> Arch Biochem Biophys, 2015","term_id":"IDPO:0000002","curator_id":"eschad","start":331,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"25444856","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":520,"term_name":"ion binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Heme binds to an intrinsically disordered region of Bach2 and alters its conformation. <i> Watanabe-Matsui M, Matsumoto T, Matsui T, Ikeda-Saito M, Muto A, Murayama K, Igarashi K. </i> Arch Biochem Biophys, 2015","term_id":"GO:0043167","curator_id":"eschad","start":331,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"25444856","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01009r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":520,"region_id":"DP01009r003","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Heme binds to an intrinsically disordered region of Bach2 and alters its conformation. <i> Watanabe-Matsui M, Matsumoto T, Matsui T, Ikeda-Saito M, Muto A, Murayama K, Igarashi K. </i> Arch Biochem Biophys, 2015","term_id":"IDPO:0000002","curator_id":"eschad","start":331,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"25444856","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":520,"term_name":"ion binding","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","reference_html":"Heme binds to an intrinsically disordered region of Bach2 and alters its conformation. <i> Watanabe-Matsui M, Matsumoto T, Matsui T, Ikeda-Saito M, Muto A, Murayama K, Igarashi K. </i> Arch Biochem Biophys, 2015","term_id":"GO:0043167","curator_id":"eschad","start":331,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"25444856","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","region_id":"DP01009r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P97303","date":"2016-09-09T23:42:38.000Z","acc":"P97303","name":"Transcription regulator protein BACH2","length":839,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000028CA4","genes":[{"name":{"value":"Bach2"}}],"alphafold_very_low_content":0.66388557806913,"disorder_content":0.22646007151370678,"disprot_consensus":{"full":[{"start":331,"end":520,"type":"D"}],"Structural state":[{"start":331,"end":520,"type":"D"}],"Molecular function":[{"start":331,"end":520,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00036","name":"EF hand domain","start":61,"end":86},{"id":"PF13499","name":"EF-hand domain pair","start":96,"end":174}],"gene3D":[{"start":91,"end":187,"id":"1.10.238.10","name":"EF-hand"},{"start":20,"end":188,"id":"1.10.238.10","name":"EF-hand"}]},"uniref50":"UniRef50_Q8VBV8","sequence":"MGQQFSWEEAEENGAVGAADAAQLQEWYKKFLEECPSGTLFMHEFKRFFKVPDNEEATQYVEAMFRAFDTNGDNTIDFLEYVAALNLVLRGTLEHKLKWTFKIYDKDRNGCIDRQELLDIVESIYKLKKACSVEVEAEQQGKLLTPEEVVDRIFLLVDENGDGQLSLNEFVEGARRDKWVMKMLQMDLNPSSWISQQRRKSAMF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P51177","disprot_id":"DP01010","ncbi_taxon_id":9913,"regions_counter":3,"creator":"lkalmar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":18,"region_id":"DP01010r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Three-dimensional structure of guanylyl cyclase activating protein-2, a calcium-sensitive modulator of photoreceptor guanylyl cyclases. <i> Ames JB, Dizhoor AM, Ikura M, Palczewski K, Stryer L. </i> J Biol Chem, 1999","term_id":"IDPO:0000002","curator_id":"lkalmar","start":2,"term_ontology":"IDPO","curator_name":"Lajos Kalmár","reference_id":"10383444","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1JBA"}],"term_name":"disorder","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":144,"region_id":"DP01010r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Three-dimensional structure of guanylyl cyclase activating protein-2, a calcium-sensitive modulator of photoreceptor guanylyl cyclases. <i> Ames JB, Dizhoor AM, Ikura M, Palczewski K, Stryer L. </i> J Biol Chem, 1999","term_id":"IDPO:0000002","curator_id":"lkalmar","start":132,"term_ontology":"IDPO","curator_name":"Lajos Kalmár","reference_id":"10383444","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1JBA"}],"term_name":"disorder","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":204,"region_id":"DP01010r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Three-dimensional structure of guanylyl cyclase activating protein-2, a calcium-sensitive modulator of photoreceptor guanylyl cyclases. <i> Ames JB, Dizhoor AM, Ikura M, Palczewski K, Stryer L. </i> J Biol Chem, 1999","term_id":"IDPO:0000002","curator_id":"lkalmar","start":191,"term_ontology":"IDPO","curator_name":"Lajos Kalmár","reference_id":"10383444","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1JBA"}],"term_name":"disorder","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P51177","date":"2016-09-10T11:58:31.000Z","acc":"P51177","name":"Guanylyl cyclase-activating protein 2","length":204,"organism":"Bos taurus","dataset":[],"UniParc":"UPI0000111EC4","genes":[{"name":{"value":"GUCA1B"},"synonyms":[{"value":"GCAP-2"},{"value":"GCAP2"}]}],"alphafold_very_low_content":0.19117647058823528,"disorder_content":0.21568627450980393,"disprot_consensus":{"full":[{"start":2,"end":18,"type":"D"},{"start":132,"end":144,"type":"D"},{"start":191,"end":204,"type":"D"}],"Structural state":[{"start":2,"end":18,"type":"D"},{"start":132,"end":144,"type":"D"},{"start":191,"end":204,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00050","name":"Kazal-type serine protease inhibitor domain","start":5,"end":61},{"id":"PF00050","name":"Kazal-type serine protease inhibitor domain","start":69,"end":126},{"id":"PF00050","name":"Kazal-type serine protease inhibitor domain","start":137,"end":185}],"gene3D":[{"start":1,"end":61,"id":"3.30.60.30","name":"3.30.60.30"},{"start":65,"end":126,"id":"3.30.60.30","name":"3.30.60.30"},{"start":130,"end":185,"id":"3.30.60.30","name":"3.30.60.30"}]},"uniref50":"UniRef50_P01005","sequence":"VEVDCSRFPNTTNEEGKDVLVCTEDLRPICGTDGVTHSECLLCAYNIEYGTNISKEHDGECREAVPMDCSRYPNTTSEEGKVMILCNKALNPVCGTDGVTYDNECVLCAHNLEQGTSVGKKHDGECRKELAAVSVDCSEYPKPACTLEYRPLCGSDNKTYGNKCNFCNAVVESNGTLTLSHFGKC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Meleagridinae","Meleagris"],"uniref90":"UniRef90_P68390","disprot_id":"DP01011","ncbi_taxon_id":9103,"regions_counter":3,"creator":"lkalmar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":65,"region_id":"DP01011r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of trypsin-turkey egg white inhibitor complex. <i> Ibrahim BS, Pattabhi V. </i> Biochem Biophys Res Commun, 2004","term_id":"IDPO:0000002","curator_id":"lkalmar","start":1,"term_ontology":"IDPO","curator_name":"Lajos Kalmár","reference_id":"14672690","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1Z7K"}],"term_name":"disorder","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":65,"term_name":"molecular function inhibitor activity","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"lkalmar","released":"2022_03","term_ontology":"GO","curator_name":"Lajos Kalmár","reference_id":"14672690","version":3,"reference_html":"Crystal structure of trypsin-turkey egg white inhibitor complex. <i> Ibrahim BS, Pattabhi V. </i> Biochem Biophys Res Commun, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140678","ec_id":"ECO:0006220","region_id":"DP01011r002","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":65,"term_name":"protein binding","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"lkalmar","released":"2022_03","term_ontology":"GO","curator_name":"Lajos Kalmár","reference_id":"14672690","version":3,"reference_html":"Crystal structure of trypsin-turkey egg white inhibitor complex. <i> Ibrahim BS, Pattabhi V. </i> Biochem Biophys Res Commun, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP01011r003","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P68390","date":"2016-09-10T12:56:28.000Z","acc":"P68390","name":"Ovomucoid","length":185,"organism":"Meleagris gallopavo","dataset":[],"UniParc":"UPI000012D795","genes":[],"alphafold_very_low_content":0.010810810810810811,"disorder_content":0.35135135135135137,"disprot_consensus":{"full":[{"start":1,"end":65,"type":"D"}],"Structural state":[{"start":1,"end":65,"type":"D"}],"Molecular function":[{"start":1,"end":65,"type":"F"}]}},{"features":{"pfam":[{"id":"PF09301","name":"Domain of unknown function (DUF1970)","start":2,"end":113}]},"uniref50":"UniRef50_P27392","sequence":"MDKKKLLYWVGGGLVLILIWLWFRNRPAAQVASNWEGPPYMTYNQPQAGSVTLPVAGYTSPSPTLPNRNRSCGCNPAVSAAMAQGADLASKLTDSITSQLNDYASSLNDYLASQAGV","taxonomy":["Viruses","Varidnaviria","Bamfordvirae","Preplasmiviricota","Tectiliviricetes","Kalamavirales","Tectiviridae","Alphatectivirus"],"uniref90":"UniRef90_P27392","disprot_id":"DP01012","ncbi_taxon_id":10658,"regions_counter":3,"creator":"gbalatti","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":93,"region_id":"DP01012r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Insights into assembly from structural analysis of bacteriophage PRD1. <i> Abrescia NG, Cockburn JJ, Grimes JM, Sutton GC, Diprose JM, Butcher SJ, Fuller SD, San Martín C, Burnett RM, Stuart DI, Bamford DH, Bamford JK. </i> Nature, 2004","term_id":"IDPO:0000002","curator_id":"gbalatti","start":57,"term_ontology":"IDPO","curator_name":"Galo Balatti","reference_id":"15525981","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1W8X"}],"term_name":"disorder","curator_orcid":"0000-0003-1900-1188","statement":[{"text":"There is no electron density for residues 57–93, indicating that\nthis portion (denoted loop 57–93 ) does not obey icosahedral symmetry.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-29T13:39:49.460Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":93,"term_name":"flexible linker","start":57,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"gbalatti","released":"2022_03","term_ontology":"IDPO","curator_name":"Galo Balatti","reference_id":"15525981","version":4,"reference_html":"Insights into assembly from structural analysis of bacteriophage PRD1. <i> Abrescia NG, Cockburn JJ, Grimes JM, Sutton GC, Diprose JM, Butcher SJ, Fuller SD, San Martín C, Burnett RM, Stuart DI, Bamford DH, Bamford JK. </i> Nature, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006220","region_id":"DP01012r002","curator_orcid":"0000-0003-1900-1188","statement":[{"text":"The bulk of the capsid is cemented together by protein P30, and the vertex is stabilized by the integral membrane protein P16. The latter seems to act as a metastable sensor, linking the symmetry-mismatched vertex base and receptor-binding spike shaft with the membrane and providing a mechanism for the \ncontrolled extrusion of a membrane–protein–DNA tube to initiate host entry\nanalysis","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-29T13:40:22.757Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":57,"end":93,"reference_id":"15525981","reference_source":"pmid","reference_html":"Insights into assembly from structural analysis of bacteriophage PRD1. <i> Abrescia NG, Cockburn JJ, Grimes JM, Sutton GC, Diprose JM, Butcher SJ, Fuller SD, San Martín C, Burnett RM, Stuart DI, Bamford DH, Bamford JK. </i> Nature, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"P27384","partner_start":null,"partner_end":null}],"region_id":"DP01012r003","statement":[{"text":"The disordered loop 57–93 probably forms non-icosahedrally symmetric interactions with the vertex base, presumably explaining arms of electron density seen connecting the P16 region and capsid vertex in the cryo-EM.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-29T13:40:18.173Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P27392","date":"2016-09-10T13:02:22.000Z","acc":"P27392","name":"Protein P16","length":117,"organism":"Enterobacteria phage PRD1","dataset":["Viral proteins"],"UniParc":"UPI0000138D29","genes":[{"name":{"value":"XVI"},"synonyms":[{"value":"S"}]}],"disorder_content":0.3162393162393162,"disprot_consensus":{"full":[{"start":57,"end":93,"type":"D"}],"Structural state":[{"start":57,"end":93,"type":"D"}],"Disorder function":[{"start":57,"end":93,"type":"F"}],"Molecular function":[{"start":57,"end":93,"type":"F"}]}},{"acc":"P68927","sequence":"MYLTLQEWNARQRRPRSLETVRRWVRECRIFPPPVKDGREYLFHESAVKVDLNRPVTGSLLKRIRNGKKAKS","creator":"lkalmar","dataset":["Viral proteins"],"date":"2016-09-10T13:48:14.000Z","disprot_id":"DP01013","features":{"pfam":[{"id":"PF07825","name":"Excisionase-like protein","start":1,"end":72}],"gene3D":[{"start":1,"end":72,"id":"1.10.1660.20","name":"1.10.1660.20","_id":"685af523b4ac24d5329d8a04"}]},"genes":[{"name":{"value":"xis","evidences":[],"_id":"685af523b4ac24d5329d8a1a"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d8a19"}],"length":72,"name":"Excisionase","ncbi_taxon_id":10742,"organism":"Escherichia phage HK022","regions_counter":5,"released":"2016_10","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Uroviricota","Caudoviricetes","Caudovirales","Siphoviridae","Hendrixvirus"],"UniParc":"UPI0000000908","uniref100":"UniRef100_P68927","uniref50":"UniRef50_P68927","uniref90":"UniRef90_P68927","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1PM6","_id":"685af523b4ac24d5329d8a06"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":51,"end":72,"interaction_partner":[],"reference_html":"Solution structure and stability of the full-length excisionase from bacteriophage HK022. <i> Rogov VV, Lücke C, Muresanu L, Wienk H, Kleinhaus I, Werner K, Löhr F, Pristovsek P, Rüterjans H. </i> Eur J Biochem, 2003","reference_id":"14653811","region_id":"DP01013r001","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Residues 51–72, which were not\nresolved in the k Xis, do not show any regular structure in\nHK022 Xis and thus appear to be completely disordered in\nsolution.","_id":"685af523b4ac24d5329d8a07"},{"type":"Results","text":"The residues from Asp51 to Ser72 are not included in any\nregular structure element in HK022 Xis, as indicated by the\nlack of any medium- or long-range NOEs. Hence, the\nC terminus is largely disordered and displays very high local\nRMSD values.","_id":"685af523b4ac24d5329d8a08"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-07T08:17:17.953Z","_id":"685af523b4ac24d5329d8a09"},"version":3,"_id":"685af523b4ac24d5329d8a05","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IMP","ec_id":"ECO:0001175","ec_name":"deletion mutation phenotypic evidence used in manual assertion","ec_ontology":"ECO","start":53,"end":72,"interaction_partner":[{"db":"UniProt","id":"P16407","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8a11"}],"reference_html":"Characterization of the bacteriophage lambda excisionase (Xis) protein: the C-terminus is required for Xis-integrase cooperativity but not for DNA binding. <i> Numrych TE, Gumport RI, Gardner JF. </i> EMBO J, 1992","reference_id":"1396573","region_id":"DP01013r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"This finding shows\nthat\nthe\nC-\nterminal\nregion\nof\nXis\nis\nrequired\nfor\nXis\n-Int\nDNA\nbinding\ncooperativity.\nThe\nobservation\nthat\nthese\nmutants\nare\ndeficient\nin\nexcisive\nrecombination\nin\nvivo\nindicates\nthat\nthis\ncooperativity\nis\nimportant\nfor\nexcision.","_id":"685af523b4ac24d5329d8a12"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-07T10:00:48.296Z","_id":"685af523b4ac24d5329d8a13"},"version":1,"_id":"685af523b4ac24d5329d8a10","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001807","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","ec_ontology":"ECO","start":53,"end":72,"interaction_partner":[{"db":"UniProt","id":"P16407","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8a15"}],"reference_html":"Characterization of the bacteriophage lambda excisionase (Xis) protein: the C-terminus is required for Xis-integrase cooperativity but not for DNA binding. <i> Numrych TE, Gumport RI, Gardner JF. </i> EMBO J, 1992","reference_id":"1396573","region_id":"DP01013r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Taken\ntogether,\nthese\nresults\nprovide\nthe\nfirst\nevidence\nthat\nXis-Int\ncooperativity\nprobably\ntakes\nplace\nthrough\ndirect\nprotein\n-protein\ninteractions\nbetween\nInt\nand\nthe\nC-terminal\nregion\nof\nXis,\nand\nnot\nthrough\nXis-induced\nalterations\nin\nDNA\nstructure\nthat\nin\nturn\npromote\nInt\nbinding.","_id":"685af523b4ac24d5329d8a16"},{"type":"Discussion","text":"The\nproperties\nof\nthe\nmutant\nXis\n(Xis-54)\nlacking\nthe\nC-terminal\n19\namino\nacids\nin\nthe\nexcision,\nchallenge\nphage\nand\ngel\nretardation\nassays\ndemonstrate\nthat\nthe\nN-terminal\n53\namino\nacids\nof\nXis\nare\nsufficient\nto\npromote\nX\nexcision,\nbind\nthe\nDNA\nand\ninteract\ncooperatively\nwith\nFIS.","_id":"685af523b4ac24d5329d8a17"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-07T10:00:47.268Z","_id":"685af523b4ac24d5329d8a18"},"version":1,"_id":"685af523b4ac24d5329d8a14","reference_source":"pmid"}],"__v":0,"disorder_content":0.3055555555555556,"disprot_consensus":{"full":[{"start":51,"end":72,"type":"D"}],"Structural state":[{"start":51,"end":72,"type":"D"}],"Molecular function":[{"start":53,"end":72,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05160","name":"DSS1/SEM1 family","start":22,"end":82}]},"uniref50":"UniRef50_O94742","sequence":"MSTDVAAAQAQSKIDLTKKKNEEINKKSLEEDDEFEDFPIDTWANGETIKSNAVTQTNIWEENWDDVEVDDDFTNELKAELDRYKRENQ","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_O94742","disprot_id":"DP01014","ncbi_taxon_id":559292,"regions_counter":11,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":89,"region_id":"DP01014r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex. <i> Ellisdon AM, Dimitrova L, Hurt E, Stewart M. </i> Nat Struct Mol Biol, 2012","term_id":"IDPO:0000002","curator_id":"lkalmar","start":1,"term_ontology":"IDPO","curator_name":"Lajos Kalmár","reference_id":"22343721","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3T5V"}],"term_name":"disorder","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":89,"term_name":"molecular adaptor activity","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"lkalmar","released":"2022_03","term_ontology":"GO","curator_name":"Lajos Kalmár","reference_id":"22343721","version":3,"reference_html":"Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex. <i> Ellisdon AM, Dimitrova L, Hurt E, Stewart M. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006220","region_id":"DP01014r002","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":89,"term_name":"protein binding","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"lkalmar","released":"2022_03","term_ontology":"GO","curator_name":"Lajos Kalmár","reference_id":"22343721","version":3,"reference_html":"Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex. <i> Ellisdon AM, Dimitrova L, Hurt E, Stewart M. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP01014r003","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":89,"region_id":"DP01014r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Dss1 is a 26S proteasome ubiquitin receptor. <i> Paraskevopoulos K, Kriegenburg F, Tatham MH, Rösner HI, Medina B, Larsen IB, Brandstrup R, Hardwick KG, Hay RT, Kragelund BB, Hartmann-Petersen R, Gordon C. </i> Mol Cell, 2014","term_id":"IDPO:0000002","curator_id":"lkalmar","start":1,"term_ontology":"IDPO","curator_name":"Lajos Kalmár","reference_id":"25306921","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":89,"term_name":"molecular adaptor activity","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"lkalmar","released":"2022_03","term_ontology":"GO","curator_name":"Lajos Kalmár","reference_id":"25306921","version":3,"reference_html":"Dss1 is a 26S proteasome ubiquitin receptor. <i> Paraskevopoulos K, Kriegenburg F, Tatham MH, Rösner HI, Medina B, Larsen IB, Brandstrup R, Hardwick KG, Hay RT, Kragelund BB, Hartmann-Petersen R, Gordon C. </i> Mol Cell, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP01014r005","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":89,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"lkalmar","released":"2022_03","term_ontology":"GO","curator_name":"Lajos Kalmár","reference_id":"25306921","version":3,"reference_html":"Dss1 is a 26S proteasome ubiquitin receptor. <i> Paraskevopoulos K, Kriegenburg F, Tatham MH, Rösner HI, Medina B, Larsen IB, Brandstrup R, Hardwick KG, Hay RT, Kragelund BB, Hartmann-Petersen R, Gordon C. </i> Mol Cell, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP01014r006","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":70,"reference_id":"22343721","reference_source":"pmid","reference_html":"Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex. <i> Ellisdon AM, Dimitrova L, Hurt E, Stewart M. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3T5V"}],"region_id":"DP01014r007","statement":[{"text":"Curator statement: This entry corresponds to the bound state of Sem1 to Sac3 and Thp1. The crystal structure shows that Sem1 interacts in a mostly extended conformation, with the exception of the C-terminal helix. Several amino acids from the N-terminus and the central region do not possess electron density. ","type":"Curator statement"},{"text":"No electron density was observed for the poorly-conserved residues (1-22) at the Sem1 N-terminus, and between the N and C-terminal binding sites (residues 42-52).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":70,"reference_id":"22343721","reference_source":"pmid","reference_html":"Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex. <i> Ellisdon AM, Dimitrova L, Hurt E, Stewart M. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3T5V"}],"interaction_partner":[{"db":"UniProt","id":"Q08231","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P46674","partner_start":null,"partner_end":null}],"region_id":"DP01014r008","statement":[{"text":"Sem1 residues 23-41 bind in a positively charged cleft formed by the TPR-like helices of the Thp1 superhelical domain (Fig. 2c,d). In this cleft, aspartates and glutamates from Sem1 form extensive ionic interactions and hydrogen bonds with several Thp1 helices (Fig 2c).","type":"Results"},{"text":"A single Sem1 chain wraps intimately around Thp1, but makes little contact with Sac3, demonstrating that Sem1 is a stoichiometric component of the TREX-2 complex. Sem1 makes extensive contacts with Thp1, burying 2741 Å2 of surface area, but makes only minor contact to Sac3, burying 293 Å2 (Supplementary Movie 2). Sem1 residues 53-89 make extensive interactions across the surface of the Thp1 superhelical domain and form a strongly conserved C-terminal helix (Supplementary Fig. 1) that binds in the cleft formed between helices α16 and α17 of the winged helix domain (Fig. 2a,b).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":70,"reference_id":"22343721","reference_source":"pmid","reference_html":"Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex. <i> Ellisdon AM, Dimitrova L, Hurt E, Stewart M. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0044183","term_name":"protein folding chaperone","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000282","ec_ontology":"ECO","ec_name":"heterologous protein expression evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3T5V"}],"region_id":"DP01014r009","statement":[{"text":"When expressed alone, Thp1 remained insoluble irrespective of the use of a range of solubilizing tags (Fig. 1a, lane 1), but its solubility improved dramatically when coexpressed with Sem1 (Fig. 1a, lane 2).Furthermore, Sem1 was not pulled down by Sac3 unless Thp1 was present (Fig. 1a, lanes 4 and 5), indicating that Sem1 stabilizes Thp1 and in turn facilitates formation of a stoichiometric Sac3–Thp1–Sem1 complex in vitro.","type":"Results"},{"text":"Although Sem1 has been proposed to function as the “molecular glue” that holds Sac3 and Thp1 together32, in TREX-2 Sem1 makes few contacts with Sac3 and instead appears to facilitate complex formation by stabilizing Thp1.","type":"Discussion"}],"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":70,"reference_id":"24412063","reference_source":"pmid","reference_html":"The intrinsically disordered Sem1 protein functions as a molecular tether during proteasome lid biogenesis. <i> Tomko RJ, Hochstrasser M. </i> Mol Cell, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3T5V"}],"region_id":"DP01014r010","statement":[{"text":"Yeast expressing sem1-Δ5link displayed levels of proteasomes and lid subcomplexes equivalent to cells expressing WT SEM1, and they incorporated Rpn3 into the lid and LP3 (Figure 5B). However, yeast expressing sem1-Δ11link or sem1-Δ15link had decreased levels of proteasomes compared to yeast with WT SEM1, and they did not accumulate detectable levels of LP3. Yeast expressing sem1-Δ19link were severely depleted for 26S proteasomes and free lid and had no detectable LP3 (Figure 5B)”.","type":"Results"},{"text":"The variability of the linker sequence, together with the requirement for a minimal length for efficient LP3 assembly, lead us to conclude that the linker functions primarily as a flexible spacer between Sem1 site 1 and site 2 that permits their optimal binding to Rpn3 and Rpn7","type":"Results"},{"text":"The two conserved acidic sites at opposing ends of a poorly conserved linker sequence allow Sem1 to tether Rpn3 and Rpn7 to one another until their interface can be reinforced or remodeled via docking to other lid subunits”, “Rpn3-Rpn7 tethering by Sem1 requires physical linkage between Sem1 site 1 and site 2, and the linker must be ≥10 residues in length to function normally in proteasome biogenesis (Figure 4A)","type":"Discussion"}],"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":70,"reference_id":"24412063","reference_source":"pmid","reference_html":"The intrinsically disordered Sem1 protein functions as a molecular tether during proteasome lid biogenesis. <i> Tomko RJ, Hochstrasser M. </i> Mol Cell, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"P40016","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q06103","partner_start":null,"partner_end":null}],"region_id":"DP01014r011","statement":[{"text":"Human Rpn3 contacts Sem1 site 1 (Wei et al., 2008). The site of interaction between Rpn7 and Sem1 is poorly defined, although EM analysis suggests that Rpn7 binds the C-terminal region of Sem1 (Bohn et al., 2013). We confirmed that mutation of the eight residues of site 1 (Figure 1A) to alanines disrupted Sem1 interaction with yeast Rpn3 (Figure 3A, left panel); in contrast, this had no effect on binding to Rpn7 (Figure 3A, right panel). Conversely, mutation of the absolutely conserved Trp60 and Trp64 residues in Site 2 disrupted Sem1 binding to Rpn7 while leaving binding to Rpn3 intact (Figure 3A). These data indicate that Sem1 site 1 and site 2 contribute to independent binding sites for Rpn3 and Rpn7.","type":"Results"},{"text":"The authors use a set of Rpn3, Rpn7 and Sem1 mutants, expressed in yeast, and tag-based purifications of the macro-complex to decipher the role of Sem1 in the formation of the proteosomal lid. They demonstrate that two separate motifs, enriched in charged residues, are responsible of the interaction. As well, the length of the linker also determines the efficient tethering effect of Sem1.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-07T12:17:04.535Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_O94742","date":"2016-09-10T16:25:11.000Z","acc":"O94742","name":"26S proteasome complex subunit SEM1","length":89,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000069DCA","genes":[{"name":{"value":"SEM1"},"synonyms":[{"value":"DSH1"}],"olnNames":[{"value":"YDR363W-A"}]}],"alphafold_very_low_content":0.011235955056179775,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":89,"type":"D"}],"Structural state":[{"start":1,"end":89,"type":"D"}],"Molecular function":[{"start":1,"end":89,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01132","name":"Elongation factor P (EF-P) OB domain","start":68,"end":125},{"id":"PF08207","name":"Elongation factor P (EF-P) KOW-like domain","start":5,"end":62},{"id":"PF09285","name":"Elongation factor P, C-terminal","start":131,"end":186}],"gene3D":[{"start":1,"end":65,"id":"2.30.30.30","name":"2.30.30.30"},{"start":130,"end":187,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"},{"start":66,"end":127,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}]},"uniref50":"UniRef50_Q6LM11","sequence":"MATHSTNEFRGGLKVMVDGDPCSIIDNEFVKPGKGQAFNRVKFRNLKTGRVLERTFKSGETLPAADVVEVEMQYLYNDGEFWHFMTSENYEQHAASKEAVAEAKQWLKEEALCMVTMWNGVPLSVEPPNFVELKITETEPGVRGDTATGGTKRAKLETGAVVRVPLFLNEGEIIKVDTRRGEYVSRAK","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Legionellales","Coxiellaceae","Coxiella"],"uniref90":"UniRef90_B6J307","disprot_id":"DP01015","ncbi_taxon_id":227377,"regions_counter":1,"creator":"lkalmar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":188,"region_id":"DP01015r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural genomics for drug design against the pathogen Coxiella burnetii. <i> Franklin MC, Cheung J, Rudolph MJ, Burshteyn F, Cassidy M, Gary E, Hillerich B, Yao ZK, Carlier PR, Totrov M, Love JD. </i> Proteins, 2015","term_id":"IDPO:0000002","curator_id":"lkalmar","start":132,"term_ontology":"IDPO","curator_name":"Lajos Kalmár","reference_id":"26033498","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3TRE"}],"term_name":"disorder","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_B6J307","date":"2016-09-10T16:38:24.000Z","acc":"Q83AR4","name":"Elongation factor P","length":188,"organism":"Coxiella burnetii (strain RSA 493 / Nine Mile phase I)","dataset":[],"UniParc":"UPI0000183B4E","genes":[{"name":{"value":"efp","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00141","url":"https://hamap.expasy.org/unirule/MF_00141"}}]},"olnNames":[{"value":"CBU_1816"}]}],"alphafold_very_low_content":0,"disorder_content":0.30319148936170215,"disprot_consensus":{"full":[{"start":132,"end":188,"type":"D"}],"Structural state":[{"start":132,"end":188,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03784","name":"Cyclotide family","start":89,"end":117}]},"uniref50":"UniRef50_P56254","sequence":"MAKFTVCLLLCLLLAAFVGAFGSELSDSHKTTLVNEIAEKMLQRKILDGVEATLVTDVAEKMFLRKMKAEAKTSETADQVFLKQLQLKGLPVCGETCVGGTCNTPGCTCSWPVCTRNGLPSLAA","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","lamiids","Gentianales","Rubiaceae","Rubioideae","Spermacoceae","Hedyotis-Oldenlandia complex","Oldenlandia"],"uniref90":"UniRef90_P56254","disprot_id":"DP01017","ncbi_taxon_id":60225,"regions_counter":1,"creator":"lkalmar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":88,"region_id":"DP01017r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The N-terminal pro-domain of the kalata B1 cyclotide precursor is intrinsically unstructured. <i> Daly NL, Gunasekera S, Clark RJ, Lin F, Wade JD, Anderson MA, Craik DJ. </i> Biopolymers, 2016","term_id":"IDPO:0000002","curator_id":"lkalmar","start":72,"term_ontology":"IDPO","curator_name":"Lajos Kalmár","reference_id":"27564841","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0003-3691-8350","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P56254","date":"2016-09-10T18:32:15.000Z","acc":"P56254","name":"Kalata-B1","length":124,"organism":"Oldenlandia affinis","dataset":[],"UniParc":"UPI000012DB78","genes":[{"name":{"value":"OAK1"}}],"alphafold_very_low_content":0.12903225806451613,"disorder_content":0.13709677419354838,"disprot_consensus":{"full":[{"start":72,"end":88,"type":"D"}],"Structural state":[{"start":72,"end":88,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00063","name":"Myosin head (motor domain)","start":104,"end":792},{"id":"PF01576","name":"Myosin tail","start":869,"end":1949},{"id":"PF02736","name":"Myosin N-terminal SH3-like domain","start":43,"end":96}],"gene3D":[{"start":806,"end":863,"id":"4.10.270.10","name":"Myosin, subunit A"},{"start":55,"end":95,"id":"2.30.30.360","name":"Myosin S1 fragment, N-terminal"},{"start":96,"end":733,"id":"3.40.850.10","name":"Kinesin motor domain"},{"start":486,"end":691,"id":"1.20.58.530","name":"1.20.58.530"},{"start":361,"end":664,"id":"1.20.120.720","name":"Myosin VI head, motor domain, U50 subdomain"},{"start":986,"end":1097,"id":"1.20.5.340","name":"1.20.5.340"}]},"uniref50":"UniRef50_Q7Z406-4","sequence":"MAAVTMSVSGRKVASRPGPVPEAAQSFLYAPRTPNVGGPGGPQVEWTARRMVWVPSELHGFEAAALRDEGEEEAEVELAESGRRLRLPRDQIQRMNPPKFSKAEDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVSTMSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFRAGVLAQLEEERDLKVTDIIVSFQAAARGYLARRAFQRRQQQQSALRVMQRNCAAYLKLRNWQWWRLFIKVKPLLQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEDAGARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRRGPLTFTTRTVRQVFRLEEGVASDEEEAEGAEPGSAPGQEPEAPPPATPQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q6URW6","disprot_id":"DP01022","ncbi_taxon_id":10090,"regions_counter":4,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":2000,"region_id":"DP01022r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The positively charged region of the myosin IIC non-helical tailpiece promotes filament assembly. <i> Ronen D, Rosenberg MM, Shalev DE, Rosenberg M, Rotem S, Friedler A, Ravid S. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"bszabo","start":1954,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"19959848","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":2000,"term_name":"molecular adaptor activity","start":1954,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"19959848","version":3,"reference_html":"The positively charged region of the myosin IIC non-helical tailpiece promotes filament assembly. <i> Ronen D, Rosenberg MM, Shalev DE, Rosenberg M, Rotem S, Friedler A, Ravid S. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006204","region_id":"DP01022r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":2000,"term_name":"protein binding","start":1954,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"19959848","version":3,"reference_html":"The positively charged region of the myosin IIC non-helical tailpiece promotes filament assembly. <i> Ronen D, Rosenberg MM, Shalev DE, Rosenberg M, Rotem S, Friedler A, Ravid S. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP01022r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":2000,"region_id":"DP01022r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The positively charged region of the myosin IIC non-helical tailpiece promotes filament assembly. <i> Ronen D, Rosenberg MM, Shalev DE, Rosenberg M, Rotem S, Friedler A, Ravid S. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"bszabo","start":1954,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"19959848","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q6URW6","date":"2016-09-12T14:55:23.000Z","acc":"Q6URW6","name":"Myosin-14","length":2000,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00001BD7B7","genes":[{"name":{"value":"Myh14"}}],"alphafold_very_low_content":0.0625,"disorder_content":0.0235,"disprot_consensus":{"full":[{"start":1954,"end":2000,"type":"D"}],"Structural state":[{"start":1954,"end":2000,"type":"D"}],"Molecular function":[{"start":1954,"end":2000,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00096","name":"Zinc finger, C2H2 type","start":295,"end":317},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":367,"end":389},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":443,"end":464},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":469,"end":492}],"gene3D":[{"start":357,"end":401,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":264,"end":322,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":416,"end":497,"id":"3.30.160.60","name":"Classic Zinc Finger"}]},"uniref50":"UniRef50_Q63ZV0","sequence":"MPRGFLVKRSKKSTPVSYRVRGGEDGDRALLLSPSCGGARAEPPAPSPVPGPLPPPPPAERAHAALAAALACAPGPQPPPQGPRAAHFGNPEAAHPAPLYSPTRPVSREHEKHKYFERSFNLGSPVSAESFPTPAALLGGGGGGGASGAGGGGTCGGDPLLFAPAELKMGTAFSAGAEAARGPGPGPPLPPAAALRPPGKRPPPPTAAEPPAKAVKAPGAKKPKAIRKLHFEDEVTTSPVLGLKIKEGPVEAPRGRAGGAARPLGEFICQLCKEEYADPFALAQHKCSRIVRVEYRCPECAKVFSCPANLASHRRWHKPRPAPAAARAPEPEAAARAEAREAPGGGSDRDTPSPGGVSESGSEDGLYECHHCAKKFRRQAYLRKHLLAHHQALQAKGAPLAPPAEDLLALYPGPDEKAPQEAAGDGEGAGVLGLSASAECHLCPVCGESFASKGAQERHLRLLHAAQVFPCKYCPATFYSSPGLTRHINKCHPSENRQVILLQVPVRPAC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q01101","disprot_id":"DP01023","ncbi_taxon_id":9606,"regions_counter":4,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":20,"region_id":"DP01023r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Protein recognition by short peptide reversible inhibitors of the chromatin-modifying LSD1/CoREST lysine demethylase. <i> Tortorici M, Borrello MT, Tardugno M, Chiarelli LR, Pilotto S, Ciossani G, Vellore NA, Bailey SG, Cowan J, O'Connell M, Crabb SJ, Packham G, Mai A, Baron R, Ganesan A, Mattevi A. </i> ACS Chem Biol, 2013","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"23721412","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3ZMS"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":20,"term_name":"molecular adaptor activity","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"23721412","version":3,"reference_html":"Protein recognition by short peptide reversible inhibitors of the chromatin-modifying LSD1/CoREST lysine demethylase. <i> Tortorici M, Borrello MT, Tardugno M, Chiarelli LR, Pilotto S, Ciossani G, Vellore NA, Bailey SG, Cowan J, O'Connell M, Crabb SJ, Packham G, Mai A, Baron R, Ganesan A, Mattevi A. </i> ACS Chem Biol, 2013","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006220","region_id":"DP01023r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":20,"term_name":"disorder to order","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"23721412","version":2,"reference_html":"Protein recognition by short peptide reversible inhibitors of the chromatin-modifying LSD1/CoREST lysine demethylase. <i> Tortorici M, Borrello MT, Tardugno M, Chiarelli LR, Pilotto S, Ciossani G, Vellore NA, Bailey SG, Cowan J, O'Connell M, Crabb SJ, Packham G, Mai A, Baron R, Ganesan A, Mattevi A. </i> ACS Chem Biol, 2013","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP01023r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":20,"term_name":"protein binding","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"23721412","version":3,"reference_html":"Protein recognition by short peptide reversible inhibitors of the chromatin-modifying LSD1/CoREST lysine demethylase. <i> Tortorici M, Borrello MT, Tardugno M, Chiarelli LR, Pilotto S, Ciossani G, Vellore NA, Bailey SG, Cowan J, O'Connell M, Crabb SJ, Packham G, Mai A, Baron R, Ganesan A, Mattevi A. </i> ACS Chem Biol, 2013","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP01023r004","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q01101","date":"2016-09-12T15:19:10.000Z","acc":"Q01101","name":"Insulinoma-associated protein 1","length":510,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000046C2F","genes":[{"name":{"value":"INSM1"},"synonyms":[{"value":"IA1"}]}],"alphafold_very_low_content":0.4764705882352941,"disorder_content":0.0392156862745098,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"T"}],"Structural state":[{"start":1,"end":20,"type":"D"}],"Molecular function":[{"start":1,"end":20,"type":"F"}],"Structural transition":[{"start":1,"end":20,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00117","name":"Glutamine amidotransferase class-I","start":180,"end":355},{"id":"PF00185","name":"Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain","start":2072,"end":2220},{"id":"PF00988","name":"Carbamoyl-phosphate synthase small chain, CPSase domain","start":4,"end":137},{"id":"PF01979","name":"Amidohydrolase family","start":1464,"end":1522},{"id":"PF02142","name":"MGS-like domain","start":1327,"end":1427},{"id":"PF02729","name":"Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain","start":1924,"end":2065},{"id":"PF02786","name":"Carbamoyl-phosphate synthase L chain, ATP binding domain","start":514,"end":717},{"id":"PF02786","name":"Carbamoyl-phosphate synthase L chain, ATP binding domain","start":1050,"end":1247},{"id":"PF02787","name":"Carbamoyl-phosphate synthetase large chain, oligomerisation domain","start":764,"end":895},{"id":"PF25596","name":"Carbamoyl phosphate synthase preATP-grasp domain","start":394,"end":510},{"id":"PF25596","name":"Carbamoyl phosphate synthase preATP-grasp domain","start":933,"end":1043}],"gene3D":[{"start":2052,"end":2209,"id":"3.40.50.1370","name":"Aspartate/ornithine carbamoyltransferase"},{"start":1925,"end":2220,"id":"3.40.50.1370","name":"Aspartate/ornithine carbamoyltransferase"},{"start":1060,"end":1129,"id":"3.30.1490.20","name":"ATP-grasp fold, A domain"},{"start":784,"end":926,"id":"1.10.1030.10","name":"Carbamoyl-phosphate synthetase, large subunit oligomerisation domain"},{"start":1,"end":149,"id":"3.50.30.20","name":"Carbamoyl-phosphate synthase small subunit, N-terminal domain"},{"start":1310,"end":1449,"id":"3.40.50.1380","name":"Methylglyoxal synthase-like domain"},{"start":154,"end":361,"id":"3.40.50.880","name":"3.40.50.880"},{"start":506,"end":783,"id":"3.30.470.20","name":"ATP-grasp fold, B domain"},{"start":929,"end":1036,"id":"3.40.50.20","name":"3.40.50.20"},{"start":1454,"end":1823,"id":"3.20.20.140","name":"Metal-dependent hydrolases"},{"start":391,"end":502,"id":"3.40.50.20","name":"3.40.50.20"},{"start":1040,"end":1302,"id":"3.30.470.20","name":"ATP-grasp fold, B domain"}]},"uniref50":"UniRef50_P27708","sequence":"MAALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNYGIPPDEMDEFGLCKWFESSGIHVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVDTRELTKKLREQGSLLGKLVQNGTEPSSLPFLDPNARPLVPEVSIKTPRVFNTGGAPRILALDCGLKYNQIRCLCQRGAEVTVVPWDHALDSQEYEGLFLSNGPGDPASYPSVVSTLSRVLSEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVETDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVKEATAGNPGGQTVRERLTERLCPPGIPTPGSGLPPPRKVLILGSGGLSIGQAGEFDYSGSQAIKALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVLLTFGGQTALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQAQAAAERLGYPVLVRAAFALGGLGSGFASNREELSALVAPAFAHTSQVLVDKSLKGWKEIEYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAPSQTLNDREYQLLRQTAIKVTQHLGIVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPELRNSVTGGTAAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKALRMVDENCVGFDHTVKPVSDMELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRMKRIIAHAQLLEQHRGQPLPPDLLQQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAVKQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLGSGVYRIGSSVEFDWCAVGCIQQLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLPNNMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQTVGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAVASDGVVAAIAISEHVENAGVHSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVGLMTGSGVVGVKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIGSYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGECPPQRSILEQLAEKNFELVINLSMRGAGGRRLSSFVTKGYRTRRLAADFSVPLIIDIKCTKLFVEALGQIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMVCAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENAGTLGTVAGSAAGLKLYLNETFSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKEEILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPGKGEVRPELGSRQDVEALWENMAVIDCFASDHAPHTLEEKCGSRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIFHLPPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVLVPPGYGQDVRKWPQGAVPQLPPSAPATSEMTTTPERPRRGIPGLPDGRFHLPPRIHRASDPGLPAEEPKEKSSRKVAEPELMGTPDGTCYPPPPVPRQASPQNLGTPGLLHPQTSPLLHSLVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSFAAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVSLRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEACFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLATVLGRF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P27708","disprot_id":"DP01024","ncbi_taxon_id":9606,"regions_counter":10,"creator":"ameszaros","regions":[{"start":1822,"end":1846,"reference_id":"24332717","reference_source":"pmid","reference_html":"Structure, functional characterization, and evolution of the dihydroorotase domain of human CAD. <i> Grande-García A, Lallous N, Díaz-Tejada C, Ramón-Maiques S. </i> Structure, 2014","date":"2022-10-27T09:43:41.806Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu1637Thr","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"The crystal structures of two mutants, E1637T and C1617S, were also determined."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys1617Ser","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"The crystal structures of two mutants, E1637T and C1617S, were also determined."}]}],"cross_refs":[{"db":"PDB","id":"4C6J"},{"db":"PDB","id":"4C6C"},{"db":"PDB","id":"4C6F"},{"db":"PDB","id":"4BY3"},{"db":"PDB","id":"4C6I"},{"db":"PDB","id":"4C6M"},{"db":"PDB","id":"4C6B"},{"db":"PDB","id":"4C6Q"},{"db":"PDB","id":"4C6O"},{"db":"PDB","id":"4C6N"},{"db":"PDB","id":"4C6L"},{"db":"PDB","id":"4C6P"},{"db":"PDB","id":"4C6D"},{"db":"PDB","id":"4C6K"},{"db":"PDB","id":"4C6E"}],"region_id":"DP01024r009","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":4,"db":"PubChem","id":"CID:439216","statements":[{"type":"Methods","text":"Crystals of wild-type or mutant huDHOase, alone or in the presence of 4 mM L-dihydroorotate (Sigma) or 5 mM 5-fluoroorotic acid (Ecogen), were obtained as previously described (Lallous et al., 2012). "}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":5,"db":"PubChem","id":"CID:69711","statements":[{"type":"Methods","text":"Crystals of wild-type or mutant huDHOase, alone or in the presence of 4 mM L-dihydroorotate (Sigma) or 5 mM 5-fluoroorotic acid (Ecogen), were obtained as previously described (Lallous et al., 2012). "}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30751","entry_name":"formic acid"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15859","entry_name":"N-carbamoyl-L-aspartic acid"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16742 ","entry_name":"orotic acid"}],"statement":[{"text":"The last 25 amino acids of the C-terminal extension (residues 1822–1846) are not seen in the electron density maps, and likely belong to the linker sequence connecting with the ATCase domain of CAD.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-27T13:02:14.505Z"}},{"start":1822,"end":1846,"reference_id":"24332717","reference_source":"pmid","reference_html":"Structure, functional characterization, and evolution of the dihydroorotase domain of human CAD. <i> Grande-García A, Lallous N, Díaz-Tejada C, Ramón-Maiques S. </i> Structure, 2014","date":"2022-10-27T09:48:47.509Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys1613Ser","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"The crystal structures of two mutants, E1637T and C1617S, were also determined."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu1637Thr","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"The crystal structures of two mutants, E1637T and C1617S, were also determined."}]}],"cross_refs":[{"db":"PDB","id":"4C6J"},{"db":"PDB","id":"4C6C"},{"db":"PDB","id":"4C6F"},{"db":"PDB","id":"4BY3"},{"db":"PDB","id":"4C6I"},{"db":"PDB","id":"4C6M"},{"db":"PDB","id":"4C6B"},{"db":"PDB","id":"4C6Q"},{"db":"PDB","id":"4C6O"},{"db":"PDB","id":"4C6N"},{"db":"PDB","id":"4C6L"},{"db":"PDB","id":"4C6P"},{"db":"PDB","id":"4C6D"},{"db":"PDB","id":"4C6K"},{"db":"PDB","id":"4C6E"}],"region_id":"DP01024r010","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":4,"db":"PubChem","id":"CID:439216","statements":[{"type":"Methods","text":"Crystals of wild-type or mutant huDHOase, alone or in the presence of 4 mM L-dihydroorotate (Sigma) or 5 mM 5-fluoroorotic acid (Ecogen), were obtained as previously described (Lallous et al., 2012). "}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":5,"db":"PubChem","id":"CID:69711","statements":[{"type":"Methods","text":"Crystals of wild-type or mutant huDHOase, alone or in the presence of 4 mM L-dihydroorotate (Sigma) or 5 mM 5-fluoroorotic acid (Ecogen), were obtained as previously described (Lallous et al., 2012). "}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30751","entry_name":"formic acid"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15859","entry_name":"N-carbamoyl-L-aspartic acid"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16742 ","entry_name":"orotic acid"}],"statement":[{"text":"The last 25 amino acids of the C-terminal extension (residues 1822–1846) are not seen in the electron density maps, and likely belong to the linker sequence connecting with the ATCase domain of CAD.","type":"Results"},{"text":"This extension is an important structural component that fastens the bottom elements of the catalytic barrel and fixes the exit point of the linker that connects with the ATCase domain.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-27T13:02:15.073Z"}}],"released":"2016_10","uniref100":"UniRef100_P27708","date":"2016-09-12T23:17:51.000Z","acc":"P27708","name":"CAD protein","length":2225,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI000016A64E","genes":[{"name":{"value":"CAD","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:1424","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:1424"}}]}}],"alphafold_very_low_content":0.05528089887640449,"disorder_content":0.011235955056179775,"disprot_consensus":{"full":[{"start":1822,"end":1846,"type":"D"}],"Structural state":[{"start":1822,"end":1846,"type":"D"}],"Disorder function":[{"start":1822,"end":1846,"type":"F"}]}},{"features":{"pfam":[{"id":"PF13499","name":"EF-hand domain pair","start":41,"end":105}],"gene3D":[{"start":1,"end":107,"id":"1.10.238.10","name":"EF-hand"}]},"uniref50":"UniRef50_P02619","sequence":"SFAGLKDADVAAALAACSAADSFKHKEFFAKVGLASKSLDDVKKAFYVIDQDKSGFIEEDELKLFLQNFSPSARALTDAETKAFLADGDKDGDGMIGVDEFAAMIKA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Actinopterygii","Neopterygii","Teleostei","Protacanthopterygii","Esociformes","Esocidae","Esox"],"uniref90":"UniRef90_P02619","disprot_id":"DP01025","ncbi_taxon_id":8010,"regions_counter":6,"creator":"wvranken","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":107,"region_id":"DP01025r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Apo-parvalbumin as an intrinsically disordered protein. <i> Permyakov SE, Bakunts AG, Denesyuk AI, Knyazeva EL, Uversky VN, Permyakov EA. </i> Proteins, 2008","term_id":"IDPO:0000002","curator_id":"wvranken","start":1,"term_ontology":"IDPO","curator_name":"Wim Vranken","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18260106","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":107,"term_name":"ion binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Apo-parvalbumin as an intrinsically disordered protein. <i> Permyakov SE, Bakunts AG, Denesyuk AI, Knyazeva EL, Uversky VN, Permyakov EA. </i> Proteins, 2008","term_id":"GO:0043167","curator_id":"wvranken","start":1,"term_ontology":"GO","curator_name":"Wim Vranken","reference_id":"18260106","version":3,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01025r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":107,"region_id":"DP01025r003","released":"2022_03","ec_id":"ECO:0006206","reference_html":"Apo-parvalbumin as an intrinsically disordered protein. <i> Permyakov SE, Bakunts AG, Denesyuk AI, Knyazeva EL, Uversky VN, Permyakov EA. </i> Proteins, 2008","term_id":"IDPO:0000002","curator_id":"wvranken","start":1,"term_ontology":"IDPO","curator_name":"Wim Vranken","ec_name":"near-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18260106","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":107,"term_name":"ion binding","released":"2022_03","ec_name":"near-UV circular dichroism evidence used in manual assertion","reference_html":"Apo-parvalbumin as an intrinsically disordered protein. <i> Permyakov SE, Bakunts AG, Denesyuk AI, Knyazeva EL, Uversky VN, Permyakov EA. </i> Proteins, 2008","term_id":"GO:0043167","curator_id":"wvranken","start":1,"term_ontology":"GO","curator_name":"Wim Vranken","reference_id":"18260106","version":3,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006206","region_id":"DP01025r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":107,"region_id":"DP01025r005","released":"2022_03","ec_id":"ECO:0006232","reference_html":"Apo-parvalbumin as an intrinsically disordered protein. <i> Permyakov SE, Bakunts AG, Denesyuk AI, Knyazeva EL, Uversky VN, Permyakov EA. </i> Proteins, 2008","term_id":"IDPO:0000002","curator_id":"wvranken","start":1,"term_ontology":"IDPO","curator_name":"Wim Vranken","ec_name":"differential scanning calorimetry evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18260106","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":107,"term_name":"ion binding","released":"2022_03","ec_name":"differential scanning calorimetry evidence used in manual assertion","reference_html":"Apo-parvalbumin as an intrinsically disordered protein. <i> Permyakov SE, Bakunts AG, Denesyuk AI, Knyazeva EL, Uversky VN, Permyakov EA. </i> Proteins, 2008","term_id":"GO:0043167","curator_id":"wvranken","start":1,"term_ontology":"GO","curator_name":"Wim Vranken","reference_id":"18260106","version":3,"curator_orcid":"0000-0001-7470-4324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006232","region_id":"DP01025r006","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P02619","date":"2016-09-13T14:19:38.000Z","acc":"P02619","name":"Parvalbumin beta","length":107,"organism":"Esox lucius","dataset":[],"UniParc":"UPI0000112A01","genes":[],"alphafold_very_low_content":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":107,"type":"D"}],"Structural state":[{"start":1,"end":107,"type":"D"}],"Molecular function":[{"start":1,"end":107,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00109","name":"Beta-ketoacyl synthase, N-terminal domain","start":1,"end":237},{"id":"PF00550","name":"Phosphopantetheine attachment site","start":2127,"end":2188},{"id":"PF00698","name":"Acyl transferase domain","start":493,"end":809},{"id":"PF00975","name":"Thioesterase domain","start":2243,"end":2500},{"id":"PF02801","name":"Beta-ketoacyl synthase, C-terminal domain","start":243,"end":359},{"id":"PF08242","name":"Methyltransferase domain","start":1246,"end":1344},{"id":"PF08659","name":"KR domain","start":1886,"end":2064},{"id":"PF13602","name":"Zinc-binding dehydrogenase","start":1721,"end":1854},{"id":"PF16197","name":"Ketoacyl-synthetase C-terminal extension","start":362,"end":472},{"id":"PF21089","name":"Polyketide synthase dehydratase domain","start":872,"end":946},{"id":"PF21149","name":"Fatty acid synthase, pseudo-KR domain","start":1422,"end":1519}],"gene3D":[{"start":2242,"end":2491,"id":"3.40.50.1820","name":"alpha/beta hydrolase"},{"start":1,"end":406,"id":"3.40.47.10","name":"3.40.47.10"},{"start":857,"end":1110,"id":"3.10.129.110","name":"Polyketide synthase dehydratase"},{"start":2119,"end":2208,"id":"1.10.1200.10","name":"ACP-like"},{"start":488,"end":807,"id":"3.40.366.10","name":"Malonyl-Coenzyme A Acyl Carrier Protein, domain 2"},{"start":2345,"end":2434,"id":"1.10.1470.20","name":"Fatty acid synthase; domain 2"},{"start":1111,"end":1407,"id":"3.40.50.150","name":"Vaccinia Virus protein VP39"},{"start":420,"end":844,"id":"3.30.70.3290","name":"3.30.70.3290"},{"start":1521,"end":1879,"id":"3.90.180.10","name":"Medium-chain alcohol dehydrogenases, catalytic domain"},{"start":1420,"end":2111,"id":"3.40.50.720","name":"NAD(P)-binding Rossmann-like Domain"}]},"uniref50":"UniRef50_A0A4X2LHN4","sequence":"MEEVVIAGMSGKLPESENLEEFWANLIGGVDMVTADDRRWKAGLYGLPRRMGKLKDLSRFDASFFGVHSKQANTMDPQLRMLLEVTYEAIVDGGINPASLRGTSTGVWVGVSSSDASEALSRDPETLVGYSMIGCQRAMMANRLSFFFDFKGPSITIDTACSSSLLALQSAYQAIRGGECSAAVVGGLNVLLKPNSSLQFMKLGMLSQDGTCRSFDAEGTGYCRAEAVVAVLLTKKSLARRVYATILNAGTNTDGSKEQGVTFPSGDVQEQLIRSLYAPAGPDPESLEYIEAHGTGTKVGDPQELNGIVNALCATRREPLLIGSTKSNMGHPEPASGVAALIKVLLSLEHGVWAPNLHYHTPNPEIPALQDGRLQVVDRPLPIRGGNVGINSFGFGGSNVHVILQPNSRPAPPPAQHAALPRLLQASGRTLEAVQTLLEQGLRHSRDLAFVGMLNEIAAVSPVAMPFRGYAVLGGEAGSQEVQQVPGSKRPVWFICSGMGAQWQGMGLSLMRLDRFRDSILRSDQALKPLGLRVSDLLLSTDEAVLDDIVSSFVSLTSIQIALIDLLTSLGLQPDGIIGHSLGEVACGYADGCLTQEEAVLSSYWRGYCIKEANVLPGAMAAVGLSWEECKQRCPPGIVPACHNSKDTVTISGPQAAMSEFLQQLKREDVFVKEVRTGGIAFHSYFMESIAPTLLRQLRKVILDPKPRSKRWLSTSIPEAQWQGSLARTFSAEYSVNNLVSPVLFQEALQHVPAHAVVVEIAPHALLQAVLKRSLESSCTIIPLMKKDHRDNLEFFLSNVGRLHLAGVSVNPNGLFPPVEFPAPRGTPLISPHXKWDHSQAWDVPSAADFPSGSSCSSVAVYKFDVSPESPDHYLVDHCIDGRVLFPGTGYLWLTWKTLARALSQNLEETPVVFEDVTLHQATILPKTGTVSLEVRLLEASHAFEVSDSNGSLIASGKVYQWESPDPKLFDTRAAVDPADSTAEFRLSQGDVYKDLRLRGYDYGPFFQLVLESDLEGNRGRLQWNDSWVSFLDAMLHMSILAPGQLGLYLPTRFTSIRIDPVTHRQKLYTLQDTTQAADVVVDRNLNTVVAGGALFLGAHSSVAPRRPQEHLKPILEKFCFTPHVESGCLAGNTALQEELQLCRGLAQALQTKVAQQGLKMVVPGLDGAQAPREAPQQSLPRLLAAACQLQLNGNLQLELGQVLAQERPLLCDDPLLSGLLDAPALKACVDTALENMASPKMKVVEVLAGDGQLYSRIPALLNTQPVMDLDYTATDRNPQALEAAQAKLEQLHVTQGQWDPANPAPGSLGKADLLVCNCALATLGDPAVAVGNMAATLKEGGFLLLHTLLAGHPLGEMVGFLTSPEQGGRHLLSQDQWESLFAGASLHLVALKRSFYGSVLFLCRQQTPQDSPVFLSVEDTSFRWVDSLKDILADASSRPVWLMAVGCSTSGVVGMVNCLRKEPGGHRIRCVLVSNLSSTSPAPEMHPSSSELQKVLQGDLVMNVYRDGAWGAFRHFPLEQDRPEKQTEHAFVNVLSRGDLSSIRWVCSPLHYALPASCQDRLCSVYYTSLNFRDVMLATGKLSPDSIPGKWLTRDCMLGMEFSGRDASGRRVMGMVPAEGLATSVLLLQHATWEVPSTWTLEEAASVPIVYTTAYYSLVVRGRMQPGESVLIHSGSGGVGQAAIAIALSRGCRVFTTVGSAEKRAYLQARFPQLDETCFANSRDTSFEQHVLRHTAGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNHALGMAVFLKNVTFHGILLDSLFEEGGATWQEVSELLKAGIQEGVVQPLKCTVFPRTKVEAAFRYMAQGKHIGKVVIQVREEEQGPAPRGLPPIALTGLSKTFCPPHKSYVITGGLGGFGLQLAQWLRLRGAQKLVLTSRSGIRTGYQARQVREWRRQGVQVLVSTSNASSLDGARSLITEATQLGPVGGVFNLAMVLRDAVLENQTPEFFQDVSKPKYSGTANLDRVTREACPELDYFVIFSSVSCGRGNAGQANYGFANSAMERICEKRRHDGLPGLAVQWGAIGDVGVVLETMGTNDTVIGGTLPQRIASCLEVLDLFLSQPHPVLSSFVLAEKKAAAPRDGSSQKDLVKAVAHILGIRDVASINPDSTLVDLGLDSLMGVEVRQILEREHDLVLSMREVRQLSLRKLQELSSKTSTDADPATPTSHEDSPVRQQATLNLSTLLVNPEGPTLTRLNSVQSAERPLFLVHPIEGSITVFHGLAAKLSIPTYGLQCTGAAPLDSIQSLASYYIECIRQVQPEGPYRIAGYSYGACVAFEMCSQLQAQQSATPGNHSLFLFDGSHTFVLAYTQSVRAKMTPGCEAEAEAKAMYFFVQQFTDMEQGKVLEALIPLQGLEARVAATVDLITQSHAGLDRHALSFAARSFYQKLRAAENYWPQATYHGNVTLLRAKTGGAYGEDLGADYNLSQVCDGKVSVHVIEGDHRTLLEGSGLESILSIIHSCLAEPRVSVREG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Suina","Suidae","Sus"],"uniref90":"UniRef90_A5YV76","disprot_id":"DP01026","ncbi_taxon_id":9823,"regions_counter":6,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1990,"region_id":"DP01026r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The crystal structure of a mammalian fatty acid synthase. <i> Maier T, Leibundgut M, Ban N. </i> Science, 2008","term_id":"IDPO:0000002","curator_id":"mnecci","start":1975,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"18772430","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2VZ8"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":1990,"term_name":"disorder to order","start":1975,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Loops in the vicinity of the active site cleft are disordered in the apo form of mFAS and become stabilized upon cofactor binding. This includes residues 1975 to 1990, corresponding to the β4/α4 loop in FabG, that are presumably stabilized by interactions of Met1973 with the active site Lys1995, and part of the substrate binding extension (residues 2072 to 2075)","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18772430","version":3,"reference_html":"The crystal structure of a mammalian fatty acid synthase. <i> Maier T, Leibundgut M, Ban N. </i> Science, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2VZ9"},{"db":"PDB","id":"2VZ8"}],"region_id":"DP01026r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":1990,"term_name":"small molecule binding","start":1975,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"18772430","version":3,"reference_html":"The crystal structure of a mammalian fatty acid synthase. <i> Maier T, Leibundgut M, Ban N. </i> Science, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0036094","ec_id":"ECO:0006220","region_id":"DP01026r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":2212,"region_id":"DP01026r004","released":"2022_03","ec_id":"ECO:0000269","reference_html":"Effect of modification of the length and flexibility of the acyl carrier protein-thioesterase interdomain linker on functionality of the animal fatty acid synthase. <i> Joshi AK, Witkowski A, Berman HA, Zhang L, Smith S. </i> Biochemistry, 2005","term_id":"IDPO:0000002","curator_id":"mnecci","start":2188,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15751987","version":2,"ec_name":"experimental evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":2212,"term_name":"entropic chain","start":2188,"ec_name":"experimental evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15751987","version":3,"reference_html":"Effect of modification of the length and flexibility of the acyl carrier protein-thioesterase interdomain linker on functionality of the animal fatty acid synthase. <i> Joshi AK, Witkowski A, Berman HA, Zhang L, Smith S. </i> Biochemistry, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0000269","region_id":"DP01026r005","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":2512,"region_id":"DP01026r006","reference_id":"18772430","start":2112,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Bound NADP+ cofactors and the attachment sites for the disordered C-terminal ACP/TE domains","type":"Figure"},{"text":"The flexibly tethered ACP and the following TE domains are not visualized in the structure.","type":"Article"},{"text":"Here, we present the crystal structure of mFAS in its free and NADP+-bound states, in which the flexibly tethered C-terminal ACP/TE domains (23) remain unresolved.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"The crystal structure of a mammalian fatty acid synthase. <i> Maier T, Leibundgut M, Ban N. </i> Science, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2VZ9"},{"db":"PDB","id":"2VZ8"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_A5YV76","date":"2016-09-13T15:35:29.000Z","acc":"A5YV76","name":"Fatty acid synthase","length":2512,"organism":"Sus scrofa","dataset":[],"UniParc":"UPI0001565ED4","genes":[{"name":{"value":"FASN","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ABR09275.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABR09275.1"}}]}}],"disorder_content":0.1660031847133758,"disprot_consensus":{"full":[{"start":1975,"end":1990,"type":"T"},{"start":2112,"end":2512,"type":"D"}],"Structural state":[{"start":1975,"end":1990,"type":"D"},{"start":2112,"end":2512,"type":"D"}],"Structural transition":[{"start":1975,"end":1990,"type":"T"}],"Molecular function":[{"start":1975,"end":1990,"type":"F"}],"Disorder function":[{"start":2188,"end":2212,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00156","name":"Phosphoribosyl transferase domain","start":40,"end":192}],"gene3D":[{"start":15,"end":228,"id":"3.40.50.2020","name":"3.40.50.2020"}]},"uniref50":"UniRef50_Q4DRC4","sequence":"MFIRLFAREEEGEKEGKICHMPREYEFAEKILFTEEEIRTRIKEVAKRIADDYKGKGLRPYVNPLVLISVLKGSFMFTADLCRALCDFNVPVRMEFICVSSYGEGLTSSGQVRMLLDTRHSIEGHHVLIVEDIVDTALTLNYLYHMYFTRRPASLKTVVLLDKREGRRVPFSADYVVANIPNAFVIGYGLDYDDTYRELRDIVVLRPEVYAEREAARQKKQRAIGSADTDRDAKREFHSKY","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Trypanosoma","Schizotrypanum"],"uniref90":"UniRef90_Q4DRC4","disprot_id":"DP01027","ncbi_taxon_id":353153,"regions_counter":2,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":241,"region_id":"DP01027r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"A 1.4 A crystal structure for the hypoxanthine phosphoribosyltransferase of Trypanosoma cruzi. <i> Focia PJ, Craig SP, Nieves-Alicea R, Fletterick RJ, Eakin AE. </i> Biochemistry, 1998","term_id":"IDPO:0000002","curator_id":"fquaglia","start":210,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9790669","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1TC1"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Both subunits have disordered C-termini and the lack of clear density prohibits tracing the chain further, thus the proposed cleavage site for this fragment of the enzyme cannot be visualized in this structure.","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-07T10:27:28.723Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":220,"end":241,"reference_id":"9858784","reference_source":"pmid","reference_html":"Limited proteolysis of a trypanosomal hypoxanthine phosphoribosyltransferase yields crystals that diffract X-rays to near atomic resolution. <i> Nieves-Alicea R, Focia PJ, Craig SP, Eakin AE. </i> Biochim Biophys Acta, 1998","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01027r002","statement":[{"text":"Herein, we describe how limited proteolysis of the recombinant trypanosomal HPRT provided a new crystal form that yielded very high resolution X-ray diffraction data and permitted the solution of the crystal structure and refinement to 1.4 Å resolution [13]. ","type":"Article"},{"text":" In addition to indicating that the start methionine had been removed from the recombinant enzyme, the data shows that the smaller molecular mass polypeptide observed in the SDS-PAGE was likely to be a product of cleavage by an endo-peptidase near the C-terminus of the recombinant HPRT.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-07T10:39:46.501Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q4DRC4","date":"2016-09-14T11:44:34.000Z","acc":"Q4DRC4","name":"Hypoxanthine phosphoribosyltransferase","length":241,"organism":"Trypanosoma cruzi (strain CL Brener)","dataset":["Neglected tropical diseases proteins"],"UniParc":"UPI000055D4E6","genes":[{"orfNames":[{"value":"Tc00.1047053509693.70","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EAN95065.1","url":"https://www.ebi.ac.uk/ena/browser/view/EAN95065.1"}}]}]}],"alphafold_very_low_content":0.0954356846473029,"disorder_content":0.13278008298755187,"disprot_consensus":{"full":[{"start":210,"end":241,"type":"D"}],"Structural state":[{"start":210,"end":241,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02288","name":"Dehydratase medium subunit","start":69,"end":181}],"gene3D":[{"start":46,"end":224,"id":"3.40.50.10150","name":"B12-dependent dehydatase associated subunit"}]},"uniref50":"UniRef50_O31041","sequence":"MEINEKLLRQIIEDVLSEMKGSDKPVSFNAPAASAAPQATPPAGDGFLTEVGEARQGTQQDEVIIAVGPAFGLAQTVNIVGIPHKSILREVIAGIEEEGIKARVIRCFKSSDVAFVAVEGNRLSGSGISIGIQSKGTTVIHQQGLPPLSNLELFPQAPLLTLETYRQIGKNAARYAKRESPQPVPTLNDQMARPKYQAKSAILHIKETKYVVTGKNPQELRVAL","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Klebsiella"],"uniref90":"UniRef90_O31041","disprot_id":"DP01028","ncbi_taxon_id":571,"regions_counter":1,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":45,"region_id":"DP01028r001","released":"2023_12","ec_id":"ECO:0007691","reference_html":"A new mode of B12 binding and the direct participation of a potassium ion in enzyme catalysis: X-ray structure of diol dehydratase. <i> Shibata N, Masuda J, Tobimatsu T, Toraya T, Suto K, Morimoto Y, Yasuoka N. </i> Structure, 1999","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10467140","version":3,"ec_name":"cleavage assay evidence used in manual assertion","date":"2023-08-23T16:57:29.216Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"The initial model including cobalamin was built with XFIT [[41]] to the experimental electron-density map at 2.5 Å resolution, except for residues as follows: residues 1–4 of the α subunit, residues 1–46 of the β subunit, residues 1–37 of the γ subunit, and a few residues located in the C terminus in all subunits.","type":"Methods"},{"text":"The missing region in the β or γ subunits is shown in gray.","type":"Figure"},{"text":"The N-terminal region up to Aspβ45 could not be located in the electron-density map. It was confirmed that this region had also been eliminated by limited proteolysis during crystallization.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_Q59471","date":"2016-09-14T13:27:40.000Z","acc":"Q59471","name":"Diol dehydrase beta subunit","length":224,"organism":"Klebsiella oxytoca","dataset":[],"UniParc":"UPI00000B76C2","genes":[{"name":{"value":"pddB","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAA08100.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAA08100.1"}}]}}],"alphafold_very_low_content":0.09375,"disorder_content":0.20089285714285715,"disprot_consensus":{"full":[{"start":1,"end":45,"type":"D"}],"Structural state":[{"start":1,"end":45,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02287","name":"Dehydratase small subunit","start":40,"end":170}],"gene3D":[{"start":81,"end":173,"id":"1.10.1510.20","name":"Propanediol/glycerol dehydratase, small subunit"}]},"uniref50":"UniRef50_O31042","sequence":"MNTDAIESMVRDVLSRMNSLQGEAPAAAPAAGGASRSARVSDYPLANKHPEWVKTATNKTLDDFTLENVLSNKVTAQDMRITPETLRLQASIAKDAGRDRLAMNFERAAELTAVPDDRILEIYNALRPYRSTKEELLAIADDLESRYQAKICAAFVREAATLYVERKKLKGDD","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Klebsiella"],"uniref90":"UniRef90_O31042","disprot_id":"DP01029","ncbi_taxon_id":571,"regions_counter":1,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":36,"region_id":"DP01029r001","released":"2023_12","ec_id":"ECO:0007691","reference_html":"A new mode of B12 binding and the direct participation of a potassium ion in enzyme catalysis: X-ray structure of diol dehydratase. <i> Shibata N, Masuda J, Tobimatsu T, Toraya T, Suto K, Morimoto Y, Yasuoka N. </i> Structure, 1999","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10467140","version":3,"ec_name":"cleavage assay evidence used in manual assertion","date":"2023-08-23T16:59:01.830Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"The initial model including cobalamin was built with XFIT [[41]] to the experimental electron-density map at 2.5 Å resolution, except for residues as follows: residues 1–4 of the α subunit, residues 1–46 of the β subunit, residues 1–37 of the γ subunit, and a few residues located in the C terminus in all subunits. ","type":"Methods"},{"text":"The missing region in the β or γ subunits is shown in gray.","type":"Figure"},{"text":"In the γ subunit, the N-terminal region up to Argγ36 could not be located on the electron-density map. It was confirmed by SDS (sodium dodecyl sulfate)–polyacrylamide gel electrophoresis that this region had been removed by limited proteolysis during crystallization.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_Q59472","date":"2016-09-14T13:57:08.000Z","acc":"Q59472","name":"Diol dehydrase gamma subunit","length":173,"organism":"Klebsiella oxytoca","dataset":[],"UniParc":"UPI00000BCF16","genes":[{"name":{"value":"pddC","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAA08101.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAA08101.1"}}]},"orfNames":[{"value":"DVB85_01585","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"RDB01945.1","url":"https://www.ebi.ac.uk/ena/browser/view/RDB01945.1"}}]}]}],"alphafold_very_low_content":0.07514450867052024,"disorder_content":0.20809248554913296,"disprot_consensus":{"full":[{"start":1,"end":36,"type":"D"}],"Structural state":[{"start":1,"end":36,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00746","name":"LPXTG cell wall anchor motif","start":680,"end":719},{"id":"PF02246","name":"Protein L b1 domain","start":104,"end":174},{"id":"PF02246","name":"Protein L b1 domain","start":177,"end":246},{"id":"PF02246","name":"Protein L b1 domain","start":249,"end":318},{"id":"PF02246","name":"Protein L b1 domain","start":321,"end":390},{"id":"PF02246","name":"Protein L b1 domain","start":395,"end":463},{"id":"PF18656","name":"Family of unknown function (DUF5633)","start":478,"end":517},{"id":"PF18656","name":"Family of unknown function (DUF5633)","start":530,"end":570}],"gene3D":[{"start":245,"end":317,"id":"3.10.20.10","name":"3.10.20.10"},{"start":318,"end":390,"id":"3.10.20.10","name":"3.10.20.10"},{"start":172,"end":244,"id":"3.10.20.10","name":"3.10.20.10"},{"start":96,"end":171,"id":"3.10.20.10","name":"3.10.20.10"},{"start":391,"end":462,"id":"3.10.20.10","name":"3.10.20.10"}]},"uniref50":"UniRef50_A0A233V257","sequence":"MAALAGAIVVTGGVGSYAADEPIDLEKLEEKRDKENVGNLPKFDNEVKDGSENPMAKYPDFDDEASTRFETENNEFEEKKVVSDNFFDQSEHPFVENKEETPETPETDSEEEVTIKANLIFANGSTQTAEFKGTFEKATSEAYAYADTLKKDNGEYTVDVADKGYTLNIKFAGKEKTPEEPKEEVTIKANLIYADGKTQTAEFKGTFEEATAEAYRYADALKKDNGEYTVDVADKGYTLNIKFAGKEKTPEEPKEEVTIKANLIYADGKTQTAEFKGTFEEATAEAYRYADLLAKENGKYTVDVADKGYTLNIKFAGKEKTPEEPKEEVTIKANLIYADGKTQTAEFKGTFAEATAEAYRYADLLAKENGKYTADLEDGGYTINIRFAGKKVDEKPEEKEQVTIKENIYFEDGTVQTATFKGTFAEATAEAYRYADLLSKEHGKYTADLEDGGYTINIRFAGKEEPEETPEKPEVQDGYASYEEAEAAAKEALKNDDVNKSYTIRQGADGRYYYVLSPVEAEEEKPEAQNGYATYEEAEAAAKKALENDPINKSYSIRQGADGRYYYVLSPVEAETPEKPVEPSEPSTPDVPSNPSNPSTPDVPSTPDVPSNPSTPEVPSNPSTPGNEEKPGNEQKPGNEQKPGNEQKPGNEQKPGNEQKPDQPSKPEKEENGKGGVDSPKKKEKAALPKAGSEAEILTLAAASLSSVAGAFISLKKRK","taxonomy":["Bacteria","Firmicutes","Tissierellia","Tissierellales","Peptoniphilaceae","Finegoldia"],"uniref90":"UniRef90_D6S9W1","disprot_id":"DP01030","ncbi_taxon_id":1260,"regions_counter":8,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":155,"region_id":"DP01030r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: secondary structure propensities are not conserved in proteins with the same fold. <i> Ramírez-Alvarado M, Serrano L, Blanco FJ. </i> Protein Sci, 1997","term_id":"IDPO:0000002","curator_id":"mnecci","start":136,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"9007989","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":155,"term_name":"molecular adaptor activity","start":136,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"9007989","version":3,"reference_html":"Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: secondary structure propensities are not conserved in proteins with the same fold. <i> Ramírez-Alvarado M, Serrano L, Blanco FJ. </i> Protein Sci, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP01030r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":155,"term_name":"disorder to order","start":136,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"9007989","version":2,"reference_html":"Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: secondary structure propensities are not conserved in proteins with the same fold. <i> Ramírez-Alvarado M, Serrano L, Blanco FJ. </i> Protein Sci, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP01030r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":155,"term_name":"protein binding","start":136,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"9007989","version":3,"reference_html":"Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: secondary structure propensities are not conserved in proteins with the same fold. <i> Ramírez-Alvarado M, Serrano L, Blanco FJ. </i> Protein Sci, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP01030r004","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":155,"region_id":"DP01030r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: secondary structure propensities are not conserved in proteins with the same fold. <i> Ramírez-Alvarado M, Serrano L, Blanco FJ. </i> Protein Sci, 1997","term_id":"IDPO:0000002","curator_id":"mnecci","start":136,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"9007989","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":155,"term_name":"molecular adaptor activity","start":136,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"9007989","version":3,"reference_html":"Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: secondary structure propensities are not conserved in proteins with the same fold. <i> Ramírez-Alvarado M, Serrano L, Blanco FJ. </i> Protein Sci, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006204","region_id":"DP01030r006","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":155,"term_name":"disorder to order","start":136,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"9007989","version":2,"reference_html":"Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: secondary structure propensities are not conserved in proteins with the same fold. <i> Ramírez-Alvarado M, Serrano L, Blanco FJ. </i> Protein Sci, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP01030r007","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":155,"term_name":"protein binding","start":136,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"9007989","version":3,"reference_html":"Conformational analysis of peptides corresponding to all the secondary structure elements of protein L B1 domain: secondary structure propensities are not conserved in proteins with the same fold. <i> Ramírez-Alvarado M, Serrano L, Blanco FJ. </i> Protein Sci, 1997","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP01030r008","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_D6S9W1","date":"2016-09-14T14:24:21.000Z","acc":"Q51912","name":"GRAM_POS_ANCHORING domain-containing protein","length":719,"organism":"Finegoldia magna","dataset":[],"UniParc":"UPI00000B533A","genes":[],"alphafold_very_low_content":0.3852573018080668,"disorder_content":0.027816411682892908,"disprot_consensus":{"full":[{"start":136,"end":155,"type":"T"}],"Structural state":[{"start":136,"end":155,"type":"D"}],"Molecular function":[{"start":136,"end":155,"type":"F"}],"Structural transition":[{"start":136,"end":155,"type":"T"}]}},{"acc":"Q99IB8","sequence":"MSTNPKPQRKTKRNTNRRPEDVKFPGGGQIVGGVYLLPRRGPRLGVRTTRKTSERSQPRGRRQPIPKDRRSTGKAWGKPGRPWPLYGNEGLGWAGWLLSPRGSRPSWGPTDPRHRSRNVGKVIDTLTCGFADLMGYIPVVGAPLSGAARAVAHGVRVLEDGVNYATGNLPGFPFSIFLLALLSCITVPVSAAQVKNTSSSYMVTNDCSNDSITWQLEAAVLHVPGCVPCERVGNTSRCWVPVSPNMAVRQPGALTQGLRTHIDMVVMSATFCSALYVGDLCGGVMLAAQVFIVSPQYHWFVQECNCSIYPGTITGHRMAWDMMMNWSPTATMILAYVMRVPEVIIDIVSGAHWGVMFGLAYFSMQGAWAKVIVILLLAAGVDAGTTTVGGAVARSTNVIAGVFSHGPQQNIQLINTNGSWHINRTALNCNDSLNTGFLAALFYTNRFNSSGCPGRLSACRNIEAFRIGWGTLQYEDNVTNPEDMRPYCWHYPPKPCGVVPARSVCGPVYCFTPSPVVVGTTDRRGVPTYTWGENETDVFLLNSTRPPQGSWFGCTWMNSTGFTKTCGAPPCRTRADFNASTDLLCPTDCFRKHPDATYIKCGSGPWLTPKCLVHYPYRLWHYPCTVNFTIFKIRMYVGGVEHRLTAACNFTRGDRCDLEDRDRSQLSPLLHSTTEWAILPCTYSDLPALSTGLLHLHQNIVDVQYMYGLSPAITKYVVRWEWVVLLFLLLADARVCACLWMLILLGQAEAALEKLVVLHAASAANCHGLLYFAIFFVAAWHIRGRVVPLTTYCLTGLWPFCLLLMALPRQAYAYDAPVHGQIGVGLLILITLFTLTPGYKTLLGQCLWWLCYLLTLGEAMIQEWVPPMQVRGGRDGIAWAVTIFCPGVVFDITKWLLALLGPAYLLRAALTHVPYFVRAHALIRVCALVKQLAGGRYVQVALLALGRWTGTYIYDHLTPMSDWAASGLRDLAVAVEPIIFSPMEKKVIVWGAETAACGDILHGLPVSARLGQEILLGPADGYTSKGWKLLAPITAYAQQTRGLLGAIVVSMTGRDRTEQAGEVQILSTVSQSFLGTTISGVLWTVYHGAGNKTLAGLRGPVTQMYSSAEGDLVGWPSPPGTKSLEPCKCGAVDLYLVTRNADVIPARRRGDKRGALLSPRPISTLKGSSGGPVLCPRGHVVGLFRAAVCSRGVAKSIDFIPVETLDVVTRSPTFSDNSTPPAVPQTYQVGYLHAPTGSGKSTKVPVAYAAQGYKVLVLNPSVAATLGFGAYLSKAHGINPNIRTGVRTVMTGEAITYSTYGKFLADGGCASGAYDIIICDECHAVDATSILGIGTVLDQAETAGVRLTVLATATPPGSVTTPHPDIEEVGLGREGEIPFYGRAIPLSCIKGGRHLIFCHSKKKCDELAAALRGMGLNAVAYYRGLDVSIIPAQGDVVVVATDALMTGYTGDFDSVIDCNVAVTQAVDFSLDPTFTITTQTVPQDAVSRSQRRGRTGRGRQGTYRYVSTGERASGMFDSVVLCECYDAGAAWYDLTPAETTVRLRAYFNTPGLPVCQDHLEFWEAVFTGLTHIDAHFLSQTKQAGENFAYLVAYQATVCARAKAPPPSWDAMWKCLARLKPTLAGPTPLLYRLGPITNEVTLTHPGTKYIATCMQADLEVMTSTWVLAGGVLAAVAAYCLATGCVSIIGRLHVNQRVVVAPDKEVLYEAFDEMEECASRAALIEEGQRIAEMLKSKIQGLLQQASKQAQDIQPAMQASWPKVEQFWARHMWNFISGIQYLAGLSTLPGNPAVASMMAFSAALTSPLSTSTTILLNIMGGWLASQIAPPAGATGFVVSGLVGAAVGSIGLGKVLVDILAGYGAGISGALVAFKIMSGEKPSMEDVINLLPGILSPGALVVGVICAAILRRHVGPGEGAVQWMNRLIAFASRGNHVAPTHYVTESDASQRVTQLLGSLTITSLLRRLHNWITEDCPIPCSGSWLRDVWDWVCTILTDFKNWLTSKLFPKLPGLPFISCQKGYKGVWAGTGIMTTRCPCGANISGNVRLGSMRITGPKTCMNTWQGTFPINCYTEGQCAPKPPTNYKTAIWRVAASEYAEVTQHGSYSYVTGLTTDNLKIPCQLPSPEFFSWVDGVQIHRFAPTPKPFFRDEVSFCVGLNSYAVGSQLPCEPEPDADVLRSMLTDPPHITAETAARRLARGSPPSEASSSVSQLSAPSLRATCTTHSNTYDVDMVDANLLMEGGVAQTEPESRVPVLDFLEPMAEEESDLEPSIPSECMLPRSGFPRALPAWARPDYNPPLVESWRRPDYQPPTVAGCALPPPKKAPTPPPRRRRTVGLSESTISEALQQLAIKTFGQPPSSGDAGSSTGAGAAESGGPTSPGEPAPSETGSASSMPPLEGEPGDPDLESDQVELQPPPQGGGVAPGSGSGSWSTCSEEDDTTVCCSMSYSWTGALITPCSPEEEKLPINPLSNSLLRYHNKVYCTTSKSASQRAKKVTFDRTQVLDAHYDSVLKDIKLAASKVSARLLTLEEACQLTPPHSARSKYGFGAKEVRSLSGRAVNHIKSVWKDLLEDPQTPIPTTIMAKNEVFCVDPAKGGKKPARLIVYPDLGVRVCEKMALYDITQKLPQAVMGASYGFQYSPAQRVEYLLKAWAEKKDPMGFSYDTRCFDSTVTERDIRTEESIYQACSLPEEARTAIHSLTERLYVGGPMFNSKGQTCGYRRCRASGVLTTSMGNTITCYVKALAACKAAGIVAPTMLVCGDDLVVISESQGTEEDERNLRAFTEAMTRYSAPPGDPPRPEYDLELITSCSSNVSVALGPRGRRRYYLTRDPTTPLARAAWETVRHSPINSWLGNIIQYAPTIWVRMVLMTHFFSILMVQDTLDQNLNFEMYGSVYSVNPLDLPAIIERLHGLDAFSMHTYSHHELTRVASALRKLGAPPLRVWKSRARAVRASLISRGGKAAVCGRYLFNWAVKTKLKLTPLPEARLLDLSSWFTVGAGGGDIFHSVSRARPRSLLFGLLLLFVGVGLFLLPAR","creator":"bszabo","dataset":["Viral proteins","RNA-binding proteins"],"date":"2016-09-14T15:15:21.000Z","disprot_id":"DP01031","features":{"pfam":[{"id":"PF00998","name":"Viral RNA dependent RNA polymerase","start":2445,"end":2955},{"id":"PF01001","name":"Hepatitis C virus non-structural protein NS4b","start":1733,"end":1925},{"id":"PF01006","name":"Hepatitis C virus non-structural protein NS4a","start":1662,"end":1715},{"id":"PF01506","name":"Hepatitis C virus non-structural 5a protein membrane anchor","start":1978,"end":1999},{"id":"PF01538","name":"Hepatitis C virus non-structural protein NS2","start":818,"end":1009},{"id":"PF01539","name":"Hepatitis C virus envelope glycoprotein E1","start":193,"end":382},{"id":"PF01542","name":"Hepatitis C virus core protein","start":116,"end":190},{"id":"PF01543","name":"Hepatitis C virus capsid protein","start":2,"end":115},{"id":"PF01560","name":"Hepatitis C virus non-structural protein E2/NS1","start":387,"end":733},{"id":"PF02907","name":"Hepatitis C virus NS3 protease","start":1060,"end":1206},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1295,"end":1359},{"id":"PF08300","name":"Hepatitis C virus non-structural 5a zinc finger domain","start":2010,"end":2070},{"id":"PF08301","name":"Hepatitis C virus non-structural 5a domain 1b","start":2072,"end":2172},{"id":"PF12941","name":"HCV NS5a protein C-terminal region","start":2184,"end":2406},{"id":"PF22027","name":"NS3 RNA helicase, C-terminal helical domain","start":1520,"end":1659}],"gene3D":[{"start":903,"end":981,"id":"1.20.1280.150","name":"Hepatitis C virus non-structural protein NS2, N-terminal domain","_id":"685af523b4ac24d5329d8a29"},{"start":2018,"end":2078,"id":"2.20.25.210","name":"Hepatitis C NS5A, domain 1B","_id":"685af523b4ac24d5329d8a2a"},{"start":998,"end":1025,"id":"2.30.30.710","name":"Hepatitis C virus non-structural protein NS2, C-terminal domain","_id":"685af523b4ac24d5329d8a2b"},{"start":2079,"end":2164,"id":"2.20.25.220","name":"Hepatitis C virus NS5A, 1B domain","_id":"685af523b4ac24d5329d8a2c"},{"start":2,"end":45,"id":"4.10.710.10","name":"Hepatitis C Virus Capsid Protein; Chain A","_id":"685af523b4ac24d5329d8a2d"},{"start":2630,"end":2693,"id":"3.30.70.270","name":"3.30.70.270","_id":"685af523b4ac24d5329d8a2e"},{"start":1359,"end":1516,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d8a2f"},{"start":1126,"end":1209,"id":"2.40.10.10","name":"Trypsin-like serine proteases","_id":"685af523b4ac24d5329d8a30"},{"start":206,"end":276,"id":"2.30.30.1080","name":"Hepatitis C virus envelope glycoprotein E1, chain C","_id":"685af523b4ac24d5329d8a31"},{"start":1210,"end":1358,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d8a32"},{"start":1026,"end":1124,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d8a33"},{"start":1517,"end":1644,"id":"1.10.820.10","name":"RNA Helicase Chain A , domain 3","_id":"685af523b4ac24d5329d8a34"},{"start":2700,"end":2810,"id":"3.30.70.270","name":"3.30.70.270","_id":"685af523b4ac24d5329d8a35"}]},"genes":[],"length":3033,"name":"Genome polyprotein","ncbi_taxon_id":356411,"organism":"Hepatitis C virus genotype 2a (isolate JFH-1)","regions_counter":23,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Hepacivirus"],"UniParc":"UPI00000EE4B6","uniref100":"UniRef100_Q99IB8","uniref50":"UniRef50_P27958","uniref90":"UniRef90_Q99IB8","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"16165","_id":"685af523b4ac24d5329d8a38"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2224,"end":2317,"interaction_partner":[],"reference_html":"Hepatitis C virus NS5A protein is a substrate for the peptidyl-prolyl cis/trans isomerase activity of cyclophilins A and B. <i> Hanoulle X, Badillo A, Wieruszeski JM, Verdegem D, Landrieu I, Bartenschlager R, Penin F, Lippens G. </i> J Biol Chem, 2009","reference_id":"19297321","region_id":"DP01031r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The 1H,15N HSQC of NS5A-D2 (Fig. 2A) displays a narrow proton chemical shift range, limited to 1 ppm excluding three outlying peaks (Trp312, Ala313, and Arg326; see below). This low level of dispersion again points to the nonstructured nature of the polypeptide, at least when isolated in solution.","_id":"685af523b4ac24d5329d8a37"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T12:16:15.809Z","_id":"685af523b4ac24d5329d8a39"},"version":3,"_id":"685af523b4ac24d5329d8a36","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":2224,"end":2317,"interaction_partner":[],"reference_html":"Hepatitis C virus NS5A protein is a substrate for the peptidyl-prolyl cis/trans isomerase activity of cyclophilins A and B. <i> Hanoulle X, Badillo A, Wieruszeski JM, Verdegem D, Landrieu I, Bartenschlager R, Penin F, Lippens G. </i> J Biol Chem, 2009","reference_id":"19297321","region_id":"DP01031r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In gel filtration chromatography, the protein elutes at a volume corresponding to a ∼30-kDa globular protein, (Fig. 1B). Such a large apparent molecular weight in a gel filtration assay is commonly associated with natively unfolded proteins devoid of globular domain (52).","_id":"685af523b4ac24d5329d8a3b"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T12:15:16.498Z","_id":"685af523b4ac24d5329d8a3c"},"version":3,"_id":"685af523b4ac24d5329d8a3a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":2224,"end":2317,"interaction_partner":[],"reference_html":"Hepatitis C virus NS5A protein is a substrate for the peptidyl-prolyl cis/trans isomerase activity of cyclophilins A and B. <i> Hanoulle X, Badillo A, Wieruszeski JM, Verdegem D, Landrieu I, Bartenschlager R, Penin F, Lippens G. </i> J Biol Chem, 2009","reference_id":"19297321","region_id":"DP01031r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In aqueous buffer, NS5A-D2 gave a complex spectrum with a large negative band around 198 nm and a shoulder in the 220–240 nm range, indicating a mixture of random coil structure with the presence of some poorly defined structures.","_id":"685af523b4ac24d5329d8a3e"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T12:14:38.072Z","_id":"685af523b4ac24d5329d8a3f"},"version":3,"_id":"685af523b4ac24d5329d8a3d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":2224,"end":2317,"interaction_partner":[],"reference_html":"Hepatitis C virus NS5A protein is a substrate for the peptidyl-prolyl cis/trans isomerase activity of cyclophilins A and B. <i> Hanoulle X, Badillo A, Wieruszeski JM, Verdegem D, Landrieu I, Bartenschlager R, Penin F, Lippens G. </i> J Biol Chem, 2009","reference_id":"19297321","region_id":"DP01031r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Despite an excellent agreement between expected (11,639 Da) and experimental mass as determined by mass spectroscopy, NS5A-D2 has an apparent molecular weight of ∼18 kDa by SDS-PAGE. This discrepancy is probably due to the primary aa sequence of NS5A-D2, which includes many acidic residues and prolines (50, 51).","_id":"685af523b4ac24d5329d8a41"},{"type":"Curator statement","text":"This abnormal behavior is observed in intrinsically disordered regions or IDPs.","_id":"685af523b4ac24d5329d8a42"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T12:14:29.059Z","_id":"685af523b4ac24d5329d8a43"},"version":1,"_id":"685af523b4ac24d5329d8a40","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2224,"end":2317,"interaction_partner":[{"db":"UniProt","id":"P62937","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8a45"},{"db":"UniProt","id":"P23284","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8a46"}],"reference_html":"Hepatitis C virus NS5A protein is a substrate for the peptidyl-prolyl cis/trans isomerase activity of cyclophilins A and B. <i> Hanoulle X, Badillo A, Wieruszeski JM, Verdegem D, Landrieu I, Bartenschlager R, Penin F, Lippens G. </i> J Biol Chem, 2009","reference_id":"19297321","region_id":"DP01031r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"To quantify the interaction strength between both partners, we titrated increasing amounts of unlabeled NS5A-D2 into samples of 15N-labeled CypA or CypB. Chemical shift changes of residues at the periphery of the binding site varied in a monotonous way from their free position toward the ligand saturated value, allowing the determination of KD values of 64 and 90 μm for CypA and CypB, respectively (Fig. 4, A–C).","_id":"685af523b4ac24d5329d8a47"},{"type":"Discussion","text":"Chemical shift perturbation experiments on both NS5A-D2·CypA and NS5A-D2·CypB complexes gave evidence for a direct physical interaction that is localized to the active site on the cyclophilins (Fig. 3). ","_id":"685af523b4ac24d5329d8a48"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T12:57:55.571Z","_id":"685af523b4ac24d5329d8a49"},"version":1,"_id":"685af523b4ac24d5329d8a44","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":2331,"end":2440,"interaction_partner":[],"reference_html":"Domain 3 of NS5A protein from the hepatitis C virus has intrinsic alpha-helical propensity and is a substrate of cyclophilin A. <i> Verdegem D, Badillo A, Wieruszeski JM, Landrieu I, Leroy A, Bartenschlager R, Penin F, Lippens G, Hanoulle X. </i> J Biol Chem, 2011","reference_id":"21489988","region_id":"DP01031r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Although the molecular mass of NS5A-D3 (JFH-1) was 11,837 Da, as determined by mass spectroscopy, the purified protein migrates as a ∼27-kDa protein by SDS-PAGE (Fig. 2A).","_id":"685af523b4ac24d5329d8a4b"},{"type":"Curator statement","text":"This abnormal behavior is observed in intrinsically disordered regions or IDPs.","_id":"685af523b4ac24d5329d8a4c"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T12:13:20.610Z","_id":"685af523b4ac24d5329d8a4d"},"version":1,"_id":"685af523b4ac24d5329d8a4a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"16798","_id":"685af523b4ac24d5329d8a51"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2331,"end":2440,"interaction_partner":[],"reference_html":"Domain 3 of NS5A protein from the hepatitis C virus has intrinsic alpha-helical propensity and is a substrate of cyclophilin A. <i> Verdegem D, Badillo A, Wieruszeski JM, Landrieu I, Leroy A, Bartenschlager R, Penin F, Lippens G, Hanoulle X. </i> J Biol Chem, 2011","reference_id":"21489988","region_id":"DP01031r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In conclusion, in aqueous buffer, NS5A-D3 (JFH-1) is mostly unfolded but has a short and stable α-helical secondary structure element centered around the N-terminal Ala367.","_id":"685af523b4ac24d5329d8a4f"},{"type":"Results","text":"Both the narrow amide proton dispersion and the clustering of glycine and serine/threonine resonances confirm the non-structured nature of NS5A-D3 (JFH-1).","_id":"685af523b4ac24d5329d8a50"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T12:15:46.067Z","_id":"685af523b4ac24d5329d8a52"},"version":1,"_id":"685af523b4ac24d5329d8a4e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":2331,"end":2440,"interaction_partner":[],"reference_html":"Domain 3 of NS5A protein from the hepatitis C virus has intrinsic alpha-helical propensity and is a substrate of cyclophilin A. <i> Verdegem D, Badillo A, Wieruszeski JM, Landrieu I, Leroy A, Bartenschlager R, Penin F, Lippens G, Hanoulle X. </i> J Biol Chem, 2011","reference_id":"21489988","region_id":"DP01031r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The CD spectrum of NS5A-D3 is typical for a poorly folded protein with a large negative peak centered at 198 nm.","_id":"685af523b4ac24d5329d8a54"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T12:10:47.663Z","_id":"685af523b4ac24d5329d8a55"},"version":1,"_id":"685af523b4ac24d5329d8a53","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2331,"end":2440,"interaction_partner":[{"db":"UniProt","id":"P62937","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8a57"}],"reference_html":"Domain 3 of NS5A protein from the hepatitis C virus has intrinsic alpha-helical propensity and is a substrate of cyclophilin A. <i> Verdegem D, Badillo A, Wieruszeski JM, Landrieu I, Leroy A, Bartenschlager R, Penin F, Lippens G, Hanoulle X. </i> J Biol Chem, 2011","reference_id":"21489988","region_id":"DP01031r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":" By comparison with the NS5A-D3 spectra recorded alone, we identified the residues involved in interaction with CypA based on chemical shift perturbations and/or peak broadening. Most of the perturbed resonances belong to residues in the C-terminal half of NS5A-D3 (from Ser415 to Asp461 for JFH-1 and from Ser414 to Val445 for Con1) (Fig. 1). ","_id":"685af523b4ac24d5329d8a58"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T12:57:54.563Z","_id":"685af523b4ac24d5329d8a59"},"version":1,"_id":"685af523b4ac24d5329d8a56","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2226,"end":2238,"interaction_partner":[{"db":"UniProt","id":"Q99IB8","partner_start":2464,"partner_end":3033,"_id":"685af523b4ac24d5329d8a62"}],"reference_html":"Hepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5A. <i> Rosnoblet C, Fritzinger B, Legrand D, Launay H, Wieruszeski JM, Lippens G, Hanoulle X. </i> J Biol Chem, 2012","reference_id":"23152499","region_id":"DP01031r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Based on our previous assignment of the NS5A-D2 spectrum, we could plot on a per residue basis the ratio of the peak intensities in the absence or presence of NS5BΔ21, and as such identified three different regions of NS5A-D2 that interact with the polymerase (Fig. 1, A and C, and supplemental Fig. 5). Two peptides of roughly 10 residues form the first anchoring points (residues 250–262 (region A) and residues 274–287 (region B)). A larger zone of interaction spanning residues 306–333 forms the third zone of interaction (region C).","_id":"685af523b4ac24d5329d8a63"},{"type":"Curator statement","text":"The 250-262 residues from NS5A protein corresponds to the 2226-2238 region of the Hepatitis C virus genotype 2a (isolate JFH-1) genome polyprotein. The binding partner, NS5BΔ21, is also encoded in the polyprotein within the residues 2464-3033","_id":"685af523b4ac24d5329d8a64"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T12:04:07.975Z","_id":"685af523b4ac24d5329d8a65"},"version":1,"_id":"685af523b4ac24d5329d8a61","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2250,"end":2263,"interaction_partner":[{"db":"UniProt","id":"Q99IB8","partner_start":2464,"partner_end":3033,"_id":"685af523b4ac24d5329d8a67"}],"reference_html":"Hepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5A. <i> Rosnoblet C, Fritzinger B, Legrand D, Launay H, Wieruszeski JM, Lippens G, Hanoulle X. </i> J Biol Chem, 2012","reference_id":"23152499","region_id":"DP01031r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Based on our previous assignment of the NS5A-D2 spectrum, we could plot on a per residue basis the ratio of the peak intensities in the absence or presence of NS5BΔ21, and as such identified three different regions of NS5A-D2 that interact with the polymerase (Fig. 1, A and C, and supplemental Fig. 5). Two peptides of roughly 10 residues form the first anchoring points (residues 250–262 (region A) and residues 274–287 (region B)). A larger zone of interaction spanning residues 306–333 forms the third zone of interaction (region C).","_id":"685af523b4ac24d5329d8a68"},{"type":"Curator statement","text":"The 274-287 residues from NS5A protein corresponds to the 2250-2263 region of the Hepatitis C virus genotype 2a (isolate JFH-1) genome polyprotein. The binding partner, NS5BΔ21, is also encoded in the polyprotein within the residues 2464-3033","_id":"685af523b4ac24d5329d8a69"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T12:04:00.056Z","_id":"685af523b4ac24d5329d8a6a"},"version":1,"_id":"685af523b4ac24d5329d8a66","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2282,"end":2309,"interaction_partner":[{"db":"UniProt","id":"Q99IB8","partner_start":2464,"partner_end":3033,"_id":"685af523b4ac24d5329d8a6c"}],"reference_html":"Hepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5A. <i> Rosnoblet C, Fritzinger B, Legrand D, Launay H, Wieruszeski JM, Lippens G, Hanoulle X. </i> J Biol Chem, 2012","reference_id":"23152499","region_id":"DP01031r014","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Based on our previous assignment of the NS5A-D2 spectrum, we could plot on a per residue basis the ratio of the peak intensities in the absence or presence of NS5BΔ21, and as such identified three different regions of NS5A-D2 that interact with the polymerase (Fig. 1, A and C, and supplemental Fig. 5). Two peptides of roughly 10 residues form the first anchoring points (residues 250–262 (region A) and residues 274–287 (region B)). A larger zone of interaction spanning residues 306–333 forms the third zone of interaction (region C).","_id":"685af523b4ac24d5329d8a6d"},{"type":"Curator statement","text":"The 306-333 residues from NS5A protein corresponds to the 2282-2309 region of the Hepatitis C virus genotype 2a (isolate JFH-1) genome polyprotein. The binding partner, NS5BΔ21, is also encoded in the polyprotein within the residues 2464-3033","_id":"685af523b4ac24d5329d8a6e"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T12:03:54.731Z","_id":"685af523b4ac24d5329d8a6f"},"version":1,"_id":"685af523b4ac24d5329d8a6b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001269","ec_name":"surface plasmon resonance evidence used in manual assertion","ec_ontology":"ECO","start":2224,"end":2317,"interaction_partner":[{"db":"UniProt","id":"Q99IB8","partner_start":2464,"partner_end":3033,"_id":"685af523b4ac24d5329d8a80"}],"reference_html":"Hepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5A. <i> Rosnoblet C, Fritzinger B, Legrand D, Launay H, Wieruszeski JM, Lippens G, Hanoulle X. </i> J Biol Chem, 2012","reference_id":"23152499","region_id":"DP01031r019","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Analysis of the corresponding sensorgrams showed that the signal response at equilibrium was initially dose-dependent and then saturated, which corresponds to a specific interaction between NS5A-D2 and NS5BΔ21. The Scatchard plot of these data is linear, and thus data are consistent with the Langmuir model (see supplemental Fig. 3). The measured association (ka) and dissociation (kd) rate constants allowed the determination of an equilibrium dissociation constant (KD) of 21 × 10−6 m (see Fig. 2) for the interaction between NS5BΔ21 and NS5A-D2.","_id":"685af523b4ac24d5329d8a81"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T12:03:52.318Z","_id":"685af523b4ac24d5329d8a82"},"version":1,"_id":"685af523b4ac24d5329d8a7f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2280,"end":2299,"interaction_partner":[{"db":"UniProt","id":"P62937","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8a84"}],"reference_html":"Hepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5A. <i> Rosnoblet C, Fritzinger B, Legrand D, Launay H, Wieruszeski JM, Lippens G, Hanoulle X. </i> J Biol Chem, 2012","reference_id":"23152499","region_id":"DP01031r020","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In agreement with our previous findings (53) and confirmed very recently with a peptide-immobilized spot assay (69), two different regions of NS5A-D2 were broadened in the presence of CypA (Fig. 1D). The first comprises residues Gly-304–Pro-323, whereas the second corresponds to residues Gly-337–Pro-341 located at the C-terminal end.","_id":"685af523b4ac24d5329d8a85"},{"type":"Curator statement","text":"The 304-323 residues from NS5A protein corresponds to the 2280-2299 region of the Hepatitis C virus genotype 2a (isolate JFH-1) genome polyprotein.","_id":"685af523b4ac24d5329d8a86"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T12:03:31.572Z","_id":"685af523b4ac24d5329d8a87"},"version":1,"_id":"685af523b4ac24d5329d8a83","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2313,"end":2317,"interaction_partner":[{"db":"UniProt","id":"P62937","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8a89"}],"reference_html":"Hepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5A. <i> Rosnoblet C, Fritzinger B, Legrand D, Launay H, Wieruszeski JM, Lippens G, Hanoulle X. </i> J Biol Chem, 2012","reference_id":"23152499","region_id":"DP01031r021","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In agreement with our previous findings (53) and confirmed very recently with a peptide-immobilized spot assay (69), two different regions of NS5A-D2 were broadened in the presence of CypA (Fig. 1D). The first comprises residues Gly-304–Pro-323, whereas the second corresponds to residues Gly-337–Pro-341 located at the C-terminal end.","_id":"685af523b4ac24d5329d8a8a"},{"type":"Curator statement","text":"The 337-341 residues from NS5A protein corresponds to the 2313-2317 region of the Hepatitis C virus genotype 2a (isolate JFH-1) genome polyprotein.","_id":"685af523b4ac24d5329d8a8b"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T12:03:23.132Z","_id":"685af523b4ac24d5329d8a8c"},"version":1,"_id":"685af523b4ac24d5329d8a88","reference_source":"pmid"}],"__v":0,"disorder_content":0.06726013847675569,"disprot_consensus":{"full":[{"start":2224,"end":2317,"type":"D"},{"start":2331,"end":2440,"type":"D"}],"Structural state":[{"start":2224,"end":2317,"type":"D"},{"start":2331,"end":2440,"type":"D"}],"Molecular function":[{"start":2224,"end":2317,"type":"F"},{"start":2331,"end":2440,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00092","name":"von Willebrand factor type A domain","start":212,"end":350},{"id":"PF00746","name":"LPXTG cell wall anchor motif","start":1047,"end":1088},{"id":"PF02986","name":"Fibronectin binding repeat","start":824,"end":864},{"id":"PF02986","name":"Fibronectin binding repeat","start":866,"end":903},{"id":"PF02986","name":"Fibronectin binding repeat","start":905,"end":946},{"id":"PF02986","name":"Fibronectin binding repeat","start":948,"end":985},{"id":"PF02986","name":"Fibronectin binding repeat","start":988,"end":1023}],"gene3D":[{"start":206,"end":361,"id":"3.40.50.410","name":"von Willebrand factor, type A domain"}]},"uniref50":"UniRef50_Q06556","sequence":"MTNCKYKLRKLSIGLVSVGTMFMAAPVMGEDASQPTASVTTESPAIQTEEDQGSQAEALEEPTPAPQTSPSTVSAVPAEAAAMADEKGIAEAPAHEPAPKASVQAEAASPAGKAEATTNTGQPTNTEQARSRSKRAAEIAPQTIEVEKLEVDKENSSLTVKDGEKDKQLIKHRDGNQRDIFDISRDVKVNQDGTMDVTLTVKPKQIDEGAEVIVLLDTSQKMTETDFNTAKENIKKLVTTLTGTTDKEGKNVSHYNNRNSVRLIDFYRKVGESTDLSGWDAKKIDEKLNEVWKKAKDDYNGWGVDLQGAIHKAREIFNLDKEKRSGKRQHIVLFSQGESTFSYDIKDKSKMDKVAVEEPVTYSNPLFPWPFYFDTTTRTHNVVNDAKKLIDFLNKLGISQFNGAVDNVATVGNTLLGLGSFFGLKNPLDYISLADLETSKLNSEKFDYSRRVGEGYNFRSYFDREVDKVGFKKILVEKIKGNLKKFQPKQTDTWLSSLGLNSIKEKIQDWMIDKALDNLFYRRQYQFYNHNLSAQAEARMAREEGIKFYAVDVTEPERIAKEINSQKYSEAYTNHLKKKAEEARELAKKRNEKFDKYLKEMSESQKFFKDVEDPEKFKDILTELKVTETFEEKVSVNNSEQRKSNKEVEYKKASSNSSFLSFIFSSSTNESITWTLSKDKLQKALQSGETLTLEYKLKIHKDKFKLAPQTRSKRSLDTSENKKSVTEKVITSDVKYKINDKEVKGKELDDVSLTYSKETVRKPQVEPNVPDTPQEKPLTPLAPSEPSQPSIPETPLIPSEPSVPETSTPEGPTEGENNLGGQSEEITITEDSQSGMSGQNPGSGNETVVEDTQTSQEDIVLGGPGQVIDFTEDSQPGMSGNNSHTITEDSKPSQEDEVIIGGQGQVIDFTEDTQSGMSGDNSHTDGTVLEEDSKPSQEDEVIIGGQGQVIDFTEDTQTGMSGAGQVESPTITEETHKPEIIMGGQSDPIDMVEDTLPGMSGSNEATVVEEDTRPKLQFHFDNEEPVPATVPTVSQTPIAQVESKVPHAKAESALPQTGDTNKLETFFTITALTVIGAAGLLGKKRRNNQTD","taxonomy":["Bacteria","Firmicutes","Bacilli","Lactobacillales","Streptococcaceae","Streptococcus"],"uniref90":"UniRef90_Q06556","disprot_id":"DP01032","ncbi_taxon_id":1334,"regions_counter":6,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":969,"region_id":"DP01032r001","released":"2023_12","ec_id":"ECO:0007680","reference_html":"Conformational changes in the fibronectin binding MSCRAMMs are induced by ligand binding. <i> House-Pompeo K, Xu Y, Joh D, Speziale P, Höök M. </i> J Biol Chem, 1996","term_id":"IDPO:0000002","curator_id":"vnugnes","start":848,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"8576127","version":3,"ec_name":"chromatography evidence used in manual assertion","date":"2023-08-23T17:41:46.348Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The absence of fixed long-distance intramolecular interactions is confirmed by the results of unfolding experiments monitored by gel-permeation chromatography. ","type":"Discussion"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":969,"region_id":"DP01032r003","released":"2023_12","ec_id":"ECO:0005632","reference_html":"Conformational changes in the fibronectin binding MSCRAMMs are induced by ligand binding. <i> House-Pompeo K, Xu Y, Joh D, Speziale P, Höök M. </i> J Biol Chem, 1996","term_id":"IDPO:0000002","curator_id":"vnugnes","start":848,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"8576127","version":3,"ec_name":"fluorescence anisotropy evidence used in manual assertion","date":"2023-08-23T17:41:40.165Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"It was determined that ANS did not bind to rFNBD-A or rFNBD-B under any conditions tested, indicating that the proteins do not appear to be capable of forming localized, stable regions of hydrophobic side chains (data not shown). From the experimental evidence presented above we conclude that the rFNBDs do not have the characteristics of folded or partially folded (i.e. a molten globule) proteins, instead the structure of the repeat regions is highly dynamic and appears to be thermodynamically indistinct from the denatured state.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":969,"region_id":"DP01032r005","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Conformational changes in the fibronectin binding MSCRAMMs are induced by ligand binding. <i> House-Pompeo K, Xu Y, Joh D, Speziale P, Höök M. </i> J Biol Chem, 1996","term_id":"IDPO:0000002","curator_id":"vnugnes","start":806,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"8576127","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-08-23T17:24:08.623Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"This type of spectra is characteristic of proteins that are predominately composed of random coil and γ-turns and contain a minimum amount of α-helix or β-sheet conformation(15., 16.). A larger version of the FnbA Fn binding segment, PAQ8(9.), contains A1, A2, and A3 as well as an upstream sequence designated Au (Fig. 1A). This sequence is similar to the other Fn binding motifs (Fig. 1B) and has been shown to have Fn binding activity. PAQ8, when analyzed by far-UV CD, appears to have no significant increase in secondary structure over the smaller proteins (Fig. 2).","type":"Results"}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":969,"term_name":"fibronectin binding","start":848,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"vnugnes","released":"2023_12","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"8576127","version":4,"reference_html":"Conformational changes in the fibronectin binding MSCRAMMs are induced by ligand binding. <i> House-Pompeo K, Xu Y, Joh D, Speziale P, Höök M. </i> J Biol Chem, 1996","date":"2023-08-23T17:41:53.442Z","term_id":"GO:0001968","ec_id":"ECO:0006204","region_id":"DP01032r006","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a fibronectin, a group of related adhesive glycoproteins of high molecular weight found on the surface of animal cells, connective tissue matrices, and in extracellular fluids.\" [GOC:hjd]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P07589","operator":null,"partner_start":null,"partner_end":null}],"statement":[{"text":"On addition of N29 to rFNBD-A at ratios ranging from 0:1 to 4.9:1 there is a marked change in the appearance of the far-UV CD spectra.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_Q06556","date":"2016-09-14T15:34:30.000Z","acc":"Q06556","name":"Fibronectin binding protein","length":1091,"organism":"Streptococcus dysgalactiae","dataset":[],"UniParc":"UPI00000B92C0","genes":[{"name":{"value":"fnbA","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAA80121.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA80121.1"}}]}}],"alphafold_very_low_content":0.44362969752520626,"disorder_content":0.15032080659945005,"disprot_consensus":{"full":[{"start":806,"end":969,"type":"D"}],"Structural state":[{"start":806,"end":969,"type":"D"}],"Molecular function":[{"start":848,"end":969,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03250","name":"Tropomodulin","start":3,"end":143},{"id":"PF27087","name":"TMOD/LMOD Leucine-rich domain","start":179,"end":338}],"gene3D":[{"start":179,"end":349,"id":"3.80.10.10","name":"Ribonuclease Inhibitor"}]},"uniref50":"UniRef50_F1NY71","sequence":"MSYRKELEKYRDLDEDKILGALTEEELRKLENELEELDPDNALLPAGLRQRDQTQKPPTGPFKREELMAHLEQQAKDIKDREDLVPFTGEKRGKAWIPKQKPMDPVLESVTLEPELEEALANASDAELCDIAAILGMHTLMSNQQYYEALGSSTIVNKEGLNSVIKPTKYKPVPDEEPNSTDVEETLKRIQNNDPDLEEVNLNNIMNIPVPTLKALAEALKTNTYVKKFSIVGTRSNDPVAFALAEMLKVNNTLKSLNVESNFISGSGILALVEALQSNTSLIELRIDNQSQPLGNNVEMEIANMLEKNTTLLKFGYHFTQQGPRLRASNAMMNNNDLVRKRRLAELNGPIFPKCRTGV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Phasianinae","Gallus"],"uniref90":"UniRef90_F1NY71","disprot_id":"DP01033","ncbi_taxon_id":9031,"regions_counter":10,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":92,"region_id":"DP01033r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structure and tropomyosin binding properties of the N-terminal capping domain of tropomodulin 1. <i> Greenfield NJ, Kostyukova AS, Hitchcock-DeGregori SE. </i> Biophys J, 2005","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15475586","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":92,"term_name":"molecular adaptor activity","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"15475586","version":3,"reference_html":"Structure and tropomyosin binding properties of the N-terminal capping domain of tropomodulin 1. <i> Greenfield NJ, Kostyukova AS, Hitchcock-DeGregori SE. </i> Biophys J, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006204","region_id":"DP01033r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":92,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"15475586","version":3,"reference_html":"Structure and tropomyosin binding properties of the N-terminal capping domain of tropomodulin 1. <i> Greenfield NJ, Kostyukova AS, Hitchcock-DeGregori SE. </i> Biophys J, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP01033r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":92,"region_id":"DP01033r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure and tropomyosin binding properties of the N-terminal capping domain of tropomodulin 1. <i> Greenfield NJ, Kostyukova AS, Hitchcock-DeGregori SE. </i> Biophys J, 2005","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15475586","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":92,"term_name":"molecular adaptor activity","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"15475586","version":3,"reference_html":"Structure and tropomyosin binding properties of the N-terminal capping domain of tropomodulin 1. <i> Greenfield NJ, Kostyukova AS, Hitchcock-DeGregori SE. </i> Biophys J, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP01033r005","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":92,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"15475586","version":3,"reference_html":"Structure and tropomyosin binding properties of the N-terminal capping domain of tropomodulin 1. <i> Greenfield NJ, Kostyukova AS, Hitchcock-DeGregori SE. </i> Biophys J, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP01033r006","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":35,"region_id":"DP01033r007","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure and tropomyosin binding properties of the N-terminal capping domain of tropomodulin 1. <i> Greenfield NJ, Kostyukova AS, Hitchcock-DeGregori SE. </i> Biophys J, 2005","term_id":"IDPO:0000002","curator_id":"mnecci","start":24,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15475586","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":35,"term_name":"molecular adaptor activity","start":24,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"15475586","version":3,"reference_html":"Structure and tropomyosin binding properties of the N-terminal capping domain of tropomodulin 1. <i> Greenfield NJ, Kostyukova AS, Hitchcock-DeGregori SE. </i> Biophys J, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP01033r008","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":35,"term_name":"disorder to order","start":24,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15475586","version":2,"reference_html":"Structure and tropomyosin binding properties of the N-terminal capping domain of tropomodulin 1. <i> Greenfield NJ, Kostyukova AS, Hitchcock-DeGregori SE. </i> Biophys J, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP01033r009","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":35,"term_name":"protein binding","start":24,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"15475586","version":3,"reference_html":"Structure and tropomyosin binding properties of the N-terminal capping domain of tropomodulin 1. <i> Greenfield NJ, Kostyukova AS, Hitchcock-DeGregori SE. </i> Biophys J, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP01033r010","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q91006","date":"2016-09-14T16:27:53.000Z","acc":"Q91006","name":"Tropomodulin","length":359,"organism":"Gallus gallus","dataset":[],"UniParc":"UPI00000FCF56","genes":[],"alphafold_very_low_content":0.016713091922005572,"disorder_content":0.2562674094707521,"disprot_consensus":{"full":[{"start":1,"end":23,"type":"D"},{"start":24,"end":35,"type":"T"},{"start":36,"end":92,"type":"D"}],"Structural state":[{"start":1,"end":92,"type":"D"}],"Molecular function":[{"start":1,"end":92,"type":"F"}],"Structural transition":[{"start":24,"end":35,"type":"T"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_P73124","sequence":"MSTQQQARALMMRHHQFIKNRQQSMLSRAAAEIGVEAEKDFWTTVQGKPQSSFRTTYDRSNASLS","taxonomy":["Bacteria","Cyanobacteria","Synechococcales","Merismopediaceae","Synechocystis","unclassified Synechocystis"],"uniref90":"UniRef90_P73124","disprot_id":"DP01034","ncbi_taxon_id":1111708,"regions_counter":21,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":65,"region_id":"DP01034r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The inactivating factor of glutamine synthetase, IF7, is a \"natively unfolded\" protein. <i> Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL. </i> Protein Sci, 2003","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12824490","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":65,"term_name":"molecular adaptor activity","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"12824490","version":3,"reference_html":"The inactivating factor of glutamine synthetase, IF7, is a \"natively unfolded\" protein. <i> Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL. </i> Protein Sci, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP01034r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":65,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"12824490","version":3,"reference_html":"The inactivating factor of glutamine synthetase, IF7, is a \"natively unfolded\" protein. <i> Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL. </i> Protein Sci, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP01034r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":65,"region_id":"DP01034r004","released":"2022_03","ec_id":"ECO:0006228","reference_html":"The inactivating factor of glutamine synthetase, IF7, is a \"natively unfolded\" protein. <i> Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL. </i> Protein Sci, 2003","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12824490","version":2,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":65,"term_name":"molecular adaptor activity","start":1,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"12824490","version":3,"reference_html":"The inactivating factor of glutamine synthetase, IF7, is a \"natively unfolded\" protein. <i> Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL. </i> Protein Sci, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006228","region_id":"DP01034r005","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":65,"term_name":"protein binding","start":1,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"12824490","version":3,"reference_html":"The inactivating factor of glutamine synthetase, IF7, is a \"natively unfolded\" protein. <i> Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL. </i> Protein Sci, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006228","region_id":"DP01034r006","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":65,"region_id":"DP01034r007","released":"2022_03","ec_id":"ECO:0007680","reference_html":"The inactivating factor of glutamine synthetase, IF7, is a \"natively unfolded\" protein. <i> Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL. </i> Protein Sci, 2003","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12824490","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":65,"term_name":"molecular adaptor activity","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"12824490","version":3,"reference_html":"The inactivating factor of glutamine synthetase, IF7, is a \"natively unfolded\" protein. <i> Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL. </i> Protein Sci, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0007680","region_id":"DP01034r008","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":65,"term_name":"protein binding","start":1,"ec_name":"chromatography evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"12824490","version":3,"reference_html":"The inactivating factor of glutamine synthetase, IF7, is a \"natively unfolded\" protein. <i> Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL. </i> Protein Sci, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007680","region_id":"DP01034r009","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":65,"region_id":"DP01034r010","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The inactivating factor of glutamine synthetase, IF7, is a \"natively unfolded\" protein. <i> Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL. </i> Protein Sci, 2003","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12824490","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":65,"term_name":"molecular adaptor activity","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"12824490","version":3,"reference_html":"The inactivating factor of glutamine synthetase, IF7, is a \"natively unfolded\" protein. <i> Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL. </i> Protein Sci, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006204","region_id":"DP01034r011","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":65,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"12824490","version":3,"reference_html":"The inactivating factor of glutamine synthetase, IF7, is a \"natively unfolded\" protein. <i> Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL. </i> Protein Sci, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP01034r012","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":65,"region_id":"DP01034r013","released":"2022_03","ec_id":"ECO:0006206","reference_html":"The inactivating factor of glutamine synthetase, IF7, is a \"natively unfolded\" protein. <i> Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL. </i> Protein Sci, 2003","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12824490","version":2,"ec_name":"near-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":65,"term_name":"molecular adaptor activity","start":1,"ec_name":"near-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"12824490","version":3,"reference_html":"The inactivating factor of glutamine synthetase, IF7, is a \"natively unfolded\" protein. <i> Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL. </i> Protein Sci, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006206","region_id":"DP01034r014","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":65,"term_name":"protein binding","start":1,"ec_name":"near-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"12824490","version":3,"reference_html":"The inactivating factor of glutamine synthetase, IF7, is a \"natively unfolded\" protein. <i> Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL. </i> Protein Sci, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006206","region_id":"DP01034r015","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":65,"region_id":"DP01034r016","released":"2022_03","ec_id":"ECO:0006317","reference_html":"The inactivating factor of glutamine synthetase, IF7, is a \"natively unfolded\" protein. <i> Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL. </i> Protein Sci, 2003","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12824490","version":2,"ec_name":"temperature-induced protein unfolding evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":65,"term_name":"molecular adaptor activity","start":1,"ec_name":"temperature-induced protein unfolding evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"12824490","version":3,"reference_html":"The inactivating factor of glutamine synthetase, IF7, is a \"natively unfolded\" protein. <i> Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL. </i> Protein Sci, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006317","region_id":"DP01034r017","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":65,"term_name":"protein binding","start":1,"ec_name":"temperature-induced protein unfolding evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"12824490","version":3,"reference_html":"The inactivating factor of glutamine synthetase, IF7, is a \"natively unfolded\" protein. <i> Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL. </i> Protein Sci, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006317","region_id":"DP01034r018","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":65,"region_id":"DP01034r019","released":"2022_03","ec_id":"ECO:0001249","reference_html":"The inactivating factor of glutamine synthetase, IF7, is a \"natively unfolded\" protein. <i> Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL. </i> Protein Sci, 2003","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12824490","version":2,"ec_name":"fluorescence evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":65,"term_name":"molecular adaptor activity","start":1,"ec_name":"fluorescence evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"12824490","version":3,"reference_html":"The inactivating factor of glutamine synthetase, IF7, is a \"natively unfolded\" protein. <i> Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL. </i> Protein Sci, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0001249","region_id":"DP01034r020","curator_orcid":"0000-0001-9377-482X","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":65,"term_name":"protein binding","start":1,"ec_name":"fluorescence evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"12824490","version":3,"reference_html":"The inactivating factor of glutamine synthetase, IF7, is a \"natively unfolded\" protein. <i> Muro-Pastor MI, Barrera FN, Reyes JC, Florencio FJ, Neira JL. </i> Protein Sci, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0001249","region_id":"DP01034r021","curator_orcid":"0000-0001-9377-482X","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P73124","date":"2016-09-14T16:55:10.000Z","acc":"P73124","name":"Ssl1911 protein","length":65,"organism":"Synechocystis sp. (strain PCC 6803 / Kazusa)","dataset":[],"UniParc":"UPI00000C0CA4","genes":[{"olnNames":[{"value":"ssl1911","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAA17150.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAA17150.1"}}]}]}],"alphafold_very_low_content":0.03076923076923077,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":65,"type":"D"}],"Structural state":[{"start":1,"end":65,"type":"D"}],"Molecular function":[{"start":1,"end":65,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_Q42447","sequence":"MASYQKHYDDQGRKVDEYGNVEKQTDEYGNPVHAASVTYVATRTAAGGYSDDINKQHDTTNAYGVDTGRQHSSGGYDGDTNKHHGTTGGYNDDTNRHHGTTGVYGIDTDRQQHGTTGGYAGDTGRQHGNIGGPYYGTNTADTGTGPRSGTTGGTGYGGTGGTDYGTTGGTGYGSGTGYGVNTGGAHTEAGYRKEHRQHDQSHGDQNEKKGIMDKIKEKLPGGHSDK","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","fabids","Fabales","Fabaceae","Papilionoideae","50 kb inversion clade","NPAAA clade","indigoferoid/millettioid clade","Phaseoleae","Glycine","Glycine subgen. Soja"],"uniref90":"UniRef90_Q70EM0","disprot_id":"DP01035","ncbi_taxon_id":3847,"regions_counter":2,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":226,"region_id":"DP01035r001","released":"2022_03","ec_id":"ECO:0006317","reference_html":"Conformation of a group 2 late embryogenesis abundant protein from soybean. Evidence of poly (L-proline)-type II structure. <i> Soulages JL, Kim K, Arrese EL, Walters C, Cushman JC. </i> Plant Physiol, 2003","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12644649","version":2,"ec_name":"temperature-induced protein unfolding evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":226,"region_id":"DP01035r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Conformation of a group 2 late embryogenesis abundant protein from soybean. Evidence of poly (L-proline)-type II structure. <i> Soulages JL, Kim K, Arrese EL, Walters C, Cushman JC. </i> Plant Physiol, 2003","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12644649","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_K7LEQ5","date":"2016-09-14T17:05:07.000Z","acc":"Q39805","name":"Dehydrin-like protein","length":226,"organism":"Glycine max","dataset":[],"UniParc":"UPI00000AB57A","genes":[],"alphafold_very_low_content":0.7876106194690266,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":226,"type":"D"}],"Structural state":[{"start":1,"end":226,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00477","name":"Small hydrophilic plant seed protein","start":1,"end":60}]},"uniref50":"UniRef50_I1JLC8","sequence":"MASRQNNKQELDERARQGETVVPGGTGGKSLEAQQHLAEGRSKGGQTRKEQLGTEGYQEMGRKGGLSTVEKSGEERAQEEGIGIDESKFRTGNNKNQNQNEDQDK","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","fabids","Fabales","Fabaceae","Papilionoideae","50 kb inversion clade","NPAAA clade","indigoferoid/millettioid clade","Phaseoleae","Glycine","Glycine subgen. Soja"],"uniref90":"UniRef90_I1JLC8","disprot_id":"DP01036","ncbi_taxon_id":3847,"regions_counter":1,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":105,"region_id":"DP01036r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Temperature-induced extended helix/random coil transitions in a group 1 late embryogenesis-abundant protein from soybean. <i> Soulages JL, Kim K, Walters C, Cushman JC. </i> Plant Physiol, 2002","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"11891239","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_I1JLC8","date":"2016-09-14T18:01:53.000Z","acc":"I1JLC8","name":"Protein SLE2","length":105,"organism":"Glycine max","dataset":[],"UniParc":"UPI00023BC1B6","genes":[{"name":{"value":"SLE2"},"synonyms":[{"value":"GmD-19","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11891239","url":"http://www.ncbi.nlm.nih.gov/pubmed/11891239","alternativeUrl":"https://europepmc.org/abstract/MED/11891239"}}]},{"value":"GmPM11","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"23017910","url":"http://www.ncbi.nlm.nih.gov/pubmed/23017910","alternativeUrl":"https://europepmc.org/abstract/MED/23017910"}}]}],"olnNames":[{"value":"Glyma03g07470.1"}]}],"alphafold_very_low_content":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":105,"type":"D"}],"Structural state":[{"start":1,"end":105,"type":"D"}]}},{"features":{"pfam":[{"id":"PF04203","name":"Sortase domain","start":76,"end":204}],"gene3D":[{"start":62,"end":206,"id":"2.40.260.10","name":"Sortase"}]},"uniref50":"UniRef50_Q2FV99","sequence":"MKKWTNRLMTIAGVVLILVAAYLFAKPHIDNYLHDKDKDEKIEQYDKNVKEQASKDKKQQAKPQIPKDKSKVAGYIEIPDADIKEPVYPGPATPEQLNRGVSFAEENESLDDQNISIAGHTFIDRPNYQFTNLKAAKKGSMVYFKVGNETRKYKMTSIRDVKPTDVGVLDEQKGKDKQLTLITCDDYNEKTGVWEKRKIFVATEVK","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Staphylococcaceae","Staphylococcus"],"uniref90":"UniRef90_Q2FV99","disprot_id":"DP01037","ncbi_taxon_id":1280,"regions_counter":6,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":174,"region_id":"DP01037r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus. <i> Ilangovan U, Ton-That H, Iwahara J, Schneewind O, Clubb RT. </i> Proc Natl Acad Sci U S A, 2001","term_id":"IDPO:0000002","curator_id":"mnecci","start":162,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"11371637","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1IJA"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":174,"term_name":"entropic chain","start":162,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"11371637","version":3,"reference_html":"Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus. <i> Ilangovan U, Ton-That H, Iwahara J, Schneewind O, Clubb RT. </i> Proc Natl Acad Sci U S A, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0006165","region_id":"DP01037r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":174,"term_name":"ion binding","start":162,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"11371637","version":3,"reference_html":"Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus. <i> Ilangovan U, Ton-That H, Iwahara J, Schneewind O, Clubb RT. </i> Proc Natl Acad Sci U S A, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0043167","ec_id":"ECO:0006165","region_id":"DP01037r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":176,"region_id":"DP01037r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structures of Staphylococcus aureus sortase A and its substrate complex. <i> Zong Y, Bice TW, Ton-That H, Schneewind O, Narayana SV. </i> J Biol Chem, 2004","term_id":"IDPO:0000002","curator_id":"mnecci","start":164,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15117963","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"12TW"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":176,"term_name":"entropic chain","start":164,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15117963","version":3,"reference_html":"Crystal structures of Staphylococcus aureus sortase A and its substrate complex. <i> Zong Y, Bice TW, Ton-That H, Schneewind O, Narayana SV. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000030","ec_id":"ECO:0006220","region_id":"DP01037r005","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":176,"term_name":"ion binding","start":164,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"15117963","version":3,"reference_html":"Crystal structures of Staphylococcus aureus sortase A and its substrate complex. <i> Zong Y, Bice TW, Ton-That H, Schneewind O, Narayana SV. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0043167","ec_id":"ECO:0006220","region_id":"DP01037r006","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q2FV99","date":"2016-09-15T10:29:19.000Z","acc":"Q9S446","name":"Class A sortase SrtA","length":206,"organism":"Staphylococcus aureus","dataset":[],"UniParc":"UPI00000B26CB","genes":[{"name":{"value":"srtA","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAD48437.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD48437.1"}}]},"orfNames":[{"value":"BTN44_15220","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AUS76496.1","url":"https://www.ebi.ac.uk/ena/browser/view/AUS76496.1"}}]},{"value":"DD547_02559","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AXP72369.1","url":"https://www.ebi.ac.uk/ena/browser/view/AXP72369.1"}}]},{"value":"EDCC5055_02506","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"SIN31549.1","url":"https://www.ebi.ac.uk/ena/browser/view/SIN31549.1"}}]},{"value":"EP54_00580","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"KMR58640.1","url":"https://www.ebi.ac.uk/ena/browser/view/KMR58640.1"}}]},{"value":"EQ90_03180","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"KMR37796.1","url":"https://www.ebi.ac.uk/ena/browser/view/KMR37796.1"}}]},{"value":"FA040_11075","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TKC08455.1","url":"https://www.ebi.ac.uk/ena/browser/view/TKC08455.1"}}]},{"value":"GO814_08865","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"MVK35245.1","url":"https://www.ebi.ac.uk/ena/browser/view/MVK35245.1"}}]},{"value":"GO942_11165","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"MVM11223.1","url":"https://www.ebi.ac.uk/ena/browser/view/MVM11223.1"}}]},{"value":"GQX37_12930","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"NUY13409.1","url":"https://www.ebi.ac.uk/ena/browser/view/NUY13409.1"}}]},{"value":"HMPREF3211_00152","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"KXA40421.1","url":"https://www.ebi.ac.uk/ena/browser/view/KXA40421.1"}}]},{"value":"SAGV69_03019","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AIU86445.1","url":"https://www.ebi.ac.uk/ena/browser/view/AIU86445.1"}}]},{"value":"SAHC1335_00526","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ALY19449.1","url":"https://www.ebi.ac.uk/ena/browser/view/ALY19449.1"}}]},{"value":"SAMEA2077334_00652","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAA6491759.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA6491759.1"}}]},{"value":"SAMEA2078260_01136","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAA4368165.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA4368165.1"}}]},{"value":"SAMEA2078588_01162","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAA6071387.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA6071387.1"}}]},{"value":"SAMEA2080344_00650","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAA6320315.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA6320315.1"}}]},{"value":"SAMEA2081063_00930","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAA4677845.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA4677845.1"}}]},{"value":"SAMEA2081470_00875","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAA5245134.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA5245134.1"}}]},{"value":"SAMEA70146418_00206","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAC8191385.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAC8191385.1"}}]}]}],"alphafold_very_low_content":0.009708737864077669,"disorder_content":0.07281553398058252,"disprot_consensus":{"full":[{"start":162,"end":176,"type":"D"}],"Structural state":[{"start":162,"end":176,"type":"D"}],"Disorder function":[{"start":162,"end":176,"type":"F"}],"Molecular function":[{"start":162,"end":176,"type":"F"}]}},{"features":{"pfam":[],"gene3D":[{"start":541,"end":593,"id":"2.40.10.10","name":"Trypsin-like serine proteases"}]},"uniref50":"UniRef50_B3V833","sequence":"RLGRVGRFKKGVALRIGHTEKGIIEIPSMIATEAALACFAYNLPVMTGGVSTSLIGNCTVRQVKTMQQFELSPFFIQNFVAHDGSMHPVIHDILKKYKLRDCMTPLCDQSIPYRASSTWLSVSEYERLGVALEIPKQVKIAFHIKEIPPKLHEMLWETVVKYKDVCLFPSIRASSISKIAYTLRTDLFAIPRTLILVERLLEEERVKQSQFRSLIDEGCSSMFSIVNLTNTLRARYAKDYTADNIQKLEKVRSQLKEFSNLDGSACEENLIKRYESLQFVHHQAATSLAKDLKLKGTWKKSLVAKDLIIAGAVAIGGIGLIYSWFTQSVETVSHQGKNKSKRIQALKFRHARDKRAGFEIDNNDDTIEEFFGSAYRKKGKGKGTTVGMGKSSRRFINMYGFDPTEYSFIQFVDPLTGAQIEENVYADIRDIQERFSEVRKKMVENDDIEMQALGSNTTIHAYFRKDWSDKALKIDLMPHNPLKVCDKTNGIAKFPERELELRQTGPAVEVDVKDIPAQEVEHEAKSLMRGLRDFNPIAQTVCRLKVSVEYGTSEMYGFGFGAYIIANHHLFRSYNGSMEVRSMHGTFRVKNLHS","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Stelpaviricetes","Patatavirales","Potyviridae","Potyvirus"],"uniref90":"UniRef90_Q85258","disprot_id":"DP01039","ncbi_taxon_id":12216,"regions_counter":6,"creator":"wvranken","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":523,"region_id":"DP01039r001","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Virulence factor of potato virus Y, genome-attached terminal protein VPg, is a highly disordered protein. <i> Grzela R, Szolajska E, Ebel C, Madern D, Favier A, Wojtal I, Zagorski W, Chroboczek J. </i> J Biol Chem, 2008","term_id":"IDPO:0000002","curator_id":"vnugnes","start":336,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-23T18:39:53.883Z","reference_source":"pmid","term_name":"disorder","reference_id":"17971447","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"GKNKSKRIQALKFRHARDKRAGFEIDNNDDTIEEFFGSAYRKKGKGKGTTVGMGKSSRRFINMYGFDPTEYSFIQFVDPLTGAQIEENVYADIRDIQERFSEVRKKMVENDDIEMQALGSNTTIHAYFRKDWSDKALKIDLMPHNPLKVCDKTNGIAKFPERELELRQTGPAVEVDVKDIPAQEVEHE","statement":[{"text":"The 1H NMR spectra recorded under these different conditions were quite similar and showed a relatively poor dispersion of the amide protons in the 6–9 ppm region (Fig. 6A), characteristic of a rather unfolded protein. However, several aliphatic peaks were observed at ∼0 ppm, located away from the random coil frequency at ∼0.7 ppm of the main peak.","type":"Results"},{"text":"These values of λNOE are characteristic of partially unfolded or degraded proteins (32). Because the VPg samples were found not to be degraded after the NMR experiment (data not shown), these data confirm that VPg is in an unfolded state.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":523,"region_id":"DP01039r002","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Virulence factor of potato virus Y, genome-attached terminal protein VPg, is a highly disordered protein. <i> Grzela R, Szolajska E, Ebel C, Madern D, Favier A, Wojtal I, Zagorski W, Chroboczek J. </i> J Biol Chem, 2008","term_id":"IDPO:0000002","curator_id":"vnugnes","start":336,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-23T18:38:02.636Z","reference_source":"pmid","term_name":"disorder","reference_id":"17971447","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"GKNKSKRIQALKFRHARDKRAGFEIDNNDDTIEEFFGSAYRKKGKGKGTTVGMGKSSRRFINMYGFDPTEYSFIQFVDPLTGAQIEENVYADIRDIQERFSEVRKKMVENDDIEMQALGSNTTIHAYFRKDWSDKALKIDLMPHNPLKVCDKTNGIAKFPERELELRQTGPAVEVDVKDIPAQEVEHE","statement":[{"text":"The CD spectra of monomeric and dimeric VPg (Fig. 5A) are identical and exhibit negative ellipticity near 205 nm, a shoulder at 220 nm, and a weak positive maximum of ∼190 nm.","type":"Results"},{"text":"The effect of temperature was tested (Fig. 5B), and in common with other unfolded proteins (43), no cooperative transition of the molar ellipticity was observed. Our data show that VPg does not have a compact structure, nor does it contain significant secondary elements. ","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":523,"region_id":"DP01039r003","released":"2023_12","ec_id":"ECO:0006275","reference_html":"Virulence factor of potato virus Y, genome-attached terminal protein VPg, is a highly disordered protein. <i> Grzela R, Szolajska E, Ebel C, Madern D, Favier A, Wojtal I, Zagorski W, Chroboczek J. </i> J Biol Chem, 2008","term_id":"IDPO:0000002","curator_id":"vnugnes","start":336,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"analytical ultracentrifugation evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-23T18:32:18.340Z","reference_source":"pmid","term_name":"disorder","reference_id":"17971447","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The results thus imply an elongated structure for both monomeric and dimeric VPg.","type":"Results"}],"sequence_construct":"GKNKSKRIQALKFRHARDKRAGFEIDNNDDTIEEFFGSAYRKKGKGKGTTVGMGKSSRRFINMYGFDPTEYSFIQFVDPLTGAQIEENVYADIRDIQERFSEVRKKMVENDDIEMQALGSNTTIHAYFRKDWSDKALKIDLMPHNPLKVCDKTNGIAKFPERELELRQTGPAVEVDVKDIPAQEVEHE"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":523,"region_id":"DP01039r004","released":"2023_12","ec_id":"ECO:0007064","reference_html":"Virulence factor of potato virus Y, genome-attached terminal protein VPg, is a highly disordered protein. <i> Grzela R, Szolajska E, Ebel C, Madern D, Favier A, Wojtal I, Zagorski W, Chroboczek J. </i> J Biol Chem, 2008","term_id":"IDPO:0000002","curator_id":"vnugnes","start":336,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"dynamic light scattering assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-23T18:32:06.763Z","reference_source":"pmid","term_name":"disorder","reference_id":"17971447","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The dynamic light scattering technique makes it possible to monitor unfolding or denaturation caused by changes in pH or temperature. The protein melting point temperature Tm obtained from dynamic light scattering analysis is indicative of thermal stability.","type":"Results"}],"sequence_construct":"GKNKSKRIQALKFRHARDKRAGFEIDNNDDTIEEFFGSAYRKKGKGKGTTVGMGKSSRRFINMYGFDPTEYSFIQFVDPLTGAQIEENVYADIRDIQERFSEVRKKMVENDDIEMQALGSNTTIHAYFRKDWSDKALKIDLMPHNPLKVCDKTNGIAKFPERELELRQTGPAVEVDVKDIPAQEVEHE"},{"start":336,"end":523,"reference_id":"17971447","reference_source":"pmid","reference_html":"Virulence factor of potato virus Y, genome-attached terminal protein VPg, is a highly disordered protein. <i> Grzela R, Szolajska E, Ebel C, Madern D, Favier A, Wojtal I, Zagorski W, Chroboczek J. </i> J Biol Chem, 2008","date":"2023-08-23T18:31:46.881Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"Q85258","operator":null,"partner_start":336,"partner_end":523}],"region_id":"DP01039r005","sequence_construct":"GKNKSKRIQALKFRHARDKRAGFEIDNNDDTIEEFFGSAYRKKGKGKGTTVGMGKSSRRFINMYGFDPTEYSFIQFVDPLTGAQIEENVYADIRDIQERFSEVRKKMVENDDIEMQALGSNTTIHAYFRKDWSDKALKIDLMPHNPLKVCDKTNGIAKFPERELELRQTGPAVEVDVKDIPAQEVEHE","statement":[{"text":"When VPg was prepared under nonreducing conditions and run on semi-denaturing SDS-PAGE, a slowly migrating band of 44 kDa, consistent with the molecular weight calculated for VPg dimer (21) was observed in addition to a major band (22kDa) corresponding to the monomeric protein (Fig. 3A, lane 1).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":336,"end":523,"reference_id":"17971447","reference_source":"pmid","reference_html":"Virulence factor of potato virus Y, genome-attached terminal protein VPg, is a highly disordered protein. <i> Grzela R, Szolajska E, Ebel C, Madern D, Favier A, Wojtal I, Zagorski W, Chroboczek J. </i> J Biol Chem, 2008","date":"2023-08-23T18:35:13.512Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q85258","operator":null,"partner_start":336,"partner_end":523}],"region_id":"DP01039r006","sequence_construct":"GKNKSKRIQALKFRHARDKRAGFEIDNNDDTIEEFFGSAYRKKGKGKGTTVGMGKSSRRFINMYGFDPTEYSFIQFVDPLTGAQIEENVYADIRDIQERFSEVRKKMVENDDIEMQALGSNTTIHAYFRKDWSDKALKIDLMPHNPLKVCDKTNGIAKFPERELELRQTGPAVEVDVKDIPAQEVEHE","statement":[{"text":"The results of the monomer/dimer mixture analysis gives the s20,w values 1.7 and 3.0 S for VPg monomer and dimer, respectively.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_Q85258","date":"2016-09-15T11:18:06.000Z","acc":"Q85258","name":"Polyprotein","length":594,"organism":"Potato virus Y","dataset":["Viral proteins"],"UniParc":"UPI00000F87AC","genes":[],"disorder_content":0.3164983164983165,"disprot_consensus":{"full":[{"start":336,"end":523,"type":"D"}],"Structural state":[{"start":336,"end":523,"type":"D"}],"Molecular function":[{"start":336,"end":523,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_Q9FUW7","sequence":"MKTFLIFVLLAMAMKIATAARELNPSNKELQSPQQSFSYQQQPFPQQPYPQQPYPSQQPYPSQQPFPTPQQQFPEQSQQPFTQPQQPTPIQPQQPFPQQPQQPQQPFPQPQQPFPWQPQQPFPQTQQSFPLQPQQPFPQQPQQPFPQPQLPFPQQSEQIIPQQLQQPFPLQPQQPFPQQPQQPFPQPQQPIPVQPQQSFPQQSQQSQQPFAQPQQLFPELQQPIPQQPQQPFPLQPQQPFPQQPQQPFPQQPQQSFPQQPQQPYPQQQPYGSSLTSIGGQ","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","BOP clade","Pooideae","Triticodae","Triticeae","Triticinae","Triticum"],"uniref90":"UniRef90_Q9FUW7","disprot_id":"DP01040","ncbi_taxon_id":4565,"regions_counter":1,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":280,"region_id":"DP01040r001","released":"2022_03","ec_id":"ECO:0006299","reference_html":"New insight into the solution structures of wheat gluten proteins from Raman optical activity. <i> Blanch EW, Kasarda DD, Hecht L, Nielsen K, Barron LD. </i> Biochemistry, 2003","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12741823","version":2,"ec_name":"Raman spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q9FUW7","date":"2016-09-15T11:27:41.000Z","acc":"Q9FUW7","name":"Omega gliadin storage protein","length":280,"organism":"Triticum aestivum","dataset":[],"UniParc":"UPI00000A7502","genes":[],"alphafold_very_low_content":0.6142857142857143,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":280,"type":"D"}],"Structural state":[{"start":1,"end":280,"type":"D"}]}},{"acc":"Q80FJ1","sequence":"MGSGPSNFVNHAPGEAIVTGLEKGADKVAGTISHTIWEVIAGLVALLTFLAFGFWLFKYLQKRRERRRQLTEFQKRYLRNSYRLSEIQRPISQHEYEDPYEPPSRRKPPPPPYSTYVNIDNVSAI","creator":"mnecci","dataset":["Viral proteins"],"date":"2016-09-15T16:20:48.000Z","disprot_id":"DP01043","features":{"pfam":[]},"genes":[],"length":125,"name":"Membrane fusion protein p14","ncbi_taxon_id":226613,"organism":"Reptilian orthoreovirus","regions_counter":6,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Duplornaviricota","Resentoviricetes","Reovirales","Reoviridae","Spinareovirinae","Orthoreovirus"],"UniParc":"UPI000004B7E5","uniref100":"UniRef100_Q80FJ1","uniref50":"UniRef50_Q80FJ1","uniref90":"UniRef90_Q80FJ1","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":31,"interaction_partner":[],"reference_html":"Myristoylation, a protruding loop, and structural plasticity are essential features of a nonenveloped virus fusion peptide motif. <i> Corcoran JA, Syvitski R, Top D, Epand RM, Epand RF, Jakeman D, Duncan R. </i> J Biol Chem, 2004","reference_id":"15448165","region_id":"DP01043r001","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"From NMR spectroscopic data and simulated annealing, the soluble nonmyristoylated p14 ectodomain peptide consists of an N-proximal extended loop flanked by two proline hinges. The remaining two-thirds of the ectodomain peptide structure is disordered, consistent with predictions based on CD spectra of the myristoylated peptide","_id":"685af523b4ac24d5329d8a96"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-15T08:31:53.262Z","_id":"685af523b4ac24d5329d8a97"},"version":3,"_id":"685af523b4ac24d5329d8a95","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":31,"interaction_partner":[],"reference_html":"Myristoylation, a protruding loop, and structural plasticity are essential features of a nonenveloped virus fusion peptide motif. <i> Corcoran JA, Syvitski R, Top D, Epand RM, Epand RF, Jakeman D, Duncan R. </i> J Biol Chem, 2004","reference_id":"15448165","region_id":"DP01043r002","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"The C-terminal disordered region (residues 15–31) may act as a flexible linker, facilitating conformational changes in either the structure or spatial arrangement of the p14 HP, similar to the proposed role of the\nlinker region that connects the influenza HA fusion peptide to the remainder of the HA2 polypeptide ","_id":"685af523b4ac24d5329d8a99"}],"states_connection":[],"term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-15T08:31:49.957Z","_id":"685af523b4ac24d5329d8a9a"},"version":4,"_id":"685af523b4ac24d5329d8a98","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":31,"interaction_partner":[],"reference_html":"Myristoylation, a protruding loop, and structural plasticity are essential features of a nonenveloped virus fusion peptide motif. <i> Corcoran JA, Syvitski R, Top D, Epand RM, Epand RF, Jakeman D, Duncan R. </i> J Biol Chem, 2004","reference_id":"15448165","region_id":"DP01043r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Solution NMR spectroscopy was used to provide additional insight into why residues clustered near the central portion of the p14 HP exert a sequence-specific effect on p14 fusion activity, while at the same time CD analysis predicts the p14 ectodomain is mostly disordered","_id":"685af523b4ac24d5329d8a9c"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-15T08:31:54.411Z","_id":"685af523b4ac24d5329d8a9d"},"version":3,"_id":"685af523b4ac24d5329d8a9b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":31,"interaction_partner":[],"reference_html":"Myristoylation, a protruding loop, and structural plasticity are essential features of a nonenveloped virus fusion peptide motif. <i> Corcoran JA, Syvitski R, Top D, Epand RM, Epand RF, Jakeman D, Duncan R. </i> J Biol Chem, 2004","reference_id":"15448165","region_id":"DP01043r005","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Circular dichroism (CD) of a myristoylated peptide representing the majority of the p14 ectodomain suggested this region is mostly disordered in solution but assumes increased structure in an apolar environment","_id":"685af523b4ac24d5329d8aa1"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-15T08:31:52.047Z","_id":"685af523b4ac24d5329d8aa2"},"version":1,"_id":"685af523b4ac24d5329d8aa0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":31,"interaction_partner":[],"reference_html":"Myristoylation, a protruding loop, and structural plasticity are essential features of a nonenveloped virus fusion peptide motif. <i> Corcoran JA, Syvitski R, Top D, Epand RM, Epand RF, Jakeman D, Duncan R. </i> J Biol Chem, 2004","reference_id":"15448165","region_id":"DP01043r006","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"The inherent structural plasticity of many fusion peptides is likely essential for their role as membrane destabilizing modules. We propose that the p14 HP is no exception, requiring a dynamic structure in addition to a potential membrane-embedding loop in order to achieve maximal function as a membrane-\ndestabilizing module.","_id":"685af523b4ac24d5329d8aa4"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_go_domain":"F","term_id":"GO:0008289","term_is_binding":true,"term_is_obsolete":false,"term_name":"lipid binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-15T08:31:50.864Z","_id":"685af523b4ac24d5329d8aa5"},"version":1,"_id":"685af523b4ac24d5329d8aa3","reference_source":"pmid"}],"__v":0,"disorder_content":0.24,"disprot_consensus":{"full":[{"start":2,"end":31,"type":"T"}],"Structural state":[{"start":2,"end":31,"type":"D"}],"Disorder function":[{"start":2,"end":31,"type":"F"}],"Structural transition":[{"start":2,"end":31,"type":"T"}],"Molecular function":[{"start":2,"end":31,"type":"F"}]}},{"features":{"pfam":[{"id":"PF08951","name":"Bacteriocin immunity protein family","start":3,"end":84}],"gene3D":[{"start":1,"end":85,"id":"1.20.1440.50","name":"Ta0600-like"}]},"uniref50":"UniRef50_C7DQC5","sequence":"MKKNAKQIVHELYNDISISKDPKYSDILEVLQKVYLKLEKQKYELDPSPLINRLVNYLYFTAYTNKIRFTEYQEELIRNLSEIGRTAGINGLYRADYGDKSQF","taxonomy":["Bacteria","Firmicutes","Bacilli","Lactobacillales","Enterococcaceae","Enterococcus"],"uniref90":"UniRef90_C7DQC5","disprot_id":"DP01044","dataset":["Unicellular toxins and antitoxins"],"ncbi_taxon_id":1352,"regions_counter":3,"creator":"mnecci","regions":[{"region_id":"DP01044r003","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T11:05:09.710Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":103,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":82,"version":3,"statement":[{"text":"However, the absence of a single main chain conformation of the C-terminal part inthe structure of Se-Met-EntA-im-(L31M+L80M) and that of molecule B points to a flexible C terminus.","type":"Results"}],"term_name":"disorder","reference_html":"1.6-Angstroms crystal structure of EntA-im. A bacterial immunity protein conferring immunity to the antimicrobial activity of the pediocin-like bacteriocin enterocin A. <i> Johnsen L, Dalhus B, Leiros I, Nissen-Meyer J. </i> J Biol Chem, 2005","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15753083","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2BL8"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_C7DQC5","date":"2016-09-15T17:13:36.000Z","acc":"Q47785","name":"Bacteriocin immunity protein","length":103,"organism":"Enterococcus faecium","UniParc":"UPI00000B84A6","genes":[{"name":{"value":"orf2","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAA63891.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA63891.1"}}]},"synonyms":[{"value":"entI","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAF74791.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAF74791.1"}}]}],"orfNames":[{"value":"CUM68_01155","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"PQD93390.1","url":"https://www.ebi.ac.uk/ena/browser/view/PQD93390.1"}}]},{"value":"CUN04_07130","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"PQC75887.1","url":"https://www.ebi.ac.uk/ena/browser/view/PQC75887.1"}}]},{"value":"CUS10_04885","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"PQE63740.1","url":"https://www.ebi.ac.uk/ena/browser/view/PQE63740.1"}}]},{"value":"CWC53_09520","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TEA56375.1","url":"https://www.ebi.ac.uk/ena/browser/view/TEA56375.1"}}]},{"value":"DKP91_10665","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"PZM55231.1","url":"https://www.ebi.ac.uk/ena/browser/view/PZM55231.1"}}]},{"value":"DPX29_12575","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"RAQ33134.1","url":"https://www.ebi.ac.uk/ena/browser/view/RAQ33134.1"}}]},{"value":"DSH71_04730","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EGP5687390.1","url":"https://www.ebi.ac.uk/ena/browser/view/EGP5687390.1"}}]},{"value":"DTX73_06505","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"KAA0691158.1","url":"https://www.ebi.ac.uk/ena/browser/view/KAA0691158.1"}}]},{"value":"GBM44_11695","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"KAB7618578.1","url":"https://www.ebi.ac.uk/ena/browser/view/KAB7618578.1"}}]},{"value":"GBM73_12235","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"KAB7578303.1","url":"https://www.ebi.ac.uk/ena/browser/view/KAB7578303.1"}}]},{"value":"SAP083A_011","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ADA62232.1","url":"https://www.ebi.ac.uk/ena/browser/view/ADA62232.1"}}]}]}],"alphafold_very_low_content":0.07766990291262135,"disorder_content":0.21359223300970873,"disprot_consensus":{"full":[{"start":82,"end":103,"type":"D"}],"Structural state":[{"start":82,"end":103,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01514","name":"Secretory protein of YscJ/FliF RBM domain","start":90,"end":181}],"gene3D":[{"start":20,"end":91,"id":"3.30.70.1530","name":"Hypothetical protein rpa1041"},{"start":98,"end":190,"id":"3.30.300.30","name":"3.30.300.30"}]},"uniref50":"UniRef50_Q9AJ19","sequence":"MKKHIKNLFLLAAICLTVACKEQLYTGLTEKEANQMQALLLSNDVNVSKEMDKSGNMTLSVEKEDFVRAITILNNNGFPKKKFADIEVIFPPSQLVASPSQENAKINYLKEQDIERLLSKIPGVIDCSVSLNVNNNESQPSSAAVLVISSPEVNLAPSVIQIKNLVKNSVDDLKLENISVVIKSSSGQDG","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_Q9AJ19","disprot_id":"DP01045","ncbi_taxon_id":83334,"regions_counter":2,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":85,"region_id":"DP01045r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural and functional studies of the enteropathogenic Escherichia coli type III needle complex protein EscJ. <i> Crepin VF, Prasannan S, Shaw RK, Wilson RK, Creasey E, Abe CM, Knutton S, Frankel G, Matthews S. </i> Mol Microbiol, 2005","term_id":"IDPO:0000002","curator_id":"mnecci","start":60,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15752191","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":85,"term_name":"flexible linker","start":60,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15752191","version":3,"reference_html":"Structural and functional studies of the enteropathogenic Escherichia coli type III needle complex protein EscJ. <i> Crepin VF, Prasannan S, Shaw RK, Wilson RK, Creasey E, Abe CM, Knutton S, Frankel G, Matthews S. </i> Mol Microbiol, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006165","region_id":"DP01045r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_O52136","date":"2016-09-15T17:29:28.000Z","acc":"Q7DB66","name":"Lipoprotein","length":190,"organism":"Escherichia coli O157:H7","dataset":[],"UniParc":"UPI00000D00A7","genes":[{"name":{"value":"escJ","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAB37996.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAB37996.1"}}]},"orfNames":[{"value":"ECs_4573","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAB37996.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAB37996.1"}}]}]}],"alphafold_very_low_content":0.010526315789473684,"disorder_content":0.1368421052631579,"disprot_consensus":{"full":[{"start":60,"end":85,"type":"D"}],"Structural state":[{"start":60,"end":85,"type":"D"}],"Disorder function":[{"start":60,"end":85,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_Q5XZ32","sequence":"MKKVKSKYLALGLLFGFISCDLFIRYEMKEESPGLFDKGNSILETSEESIKKPMNKKGKGKIARKKGKSKVSRKEPYIHSLKRDSANKSNFLQKNVILEEESLKTELLKEQSETRKEKIQKQQDEYKGMTQGSLNSLSGESGELEEPIESNEIDLTIDSDLRPKSSLQGIAGSNSISYTDEIEEEDYDQYYLDEYDEEDEEEIRLSNRYQSYLEGVKYNVDSAIQTITKIYNTYTLFSTKLTQMYSTRLDNFAKAKAKEEAAKFTKEDLEKNFKTLLNYIQVSVKTAANFVYINDTHAKRKLENIEAEIKTLIAKIKEQSNLYEAYKAIVTSILLMRDSLKEVQGIIDKNGVWY","taxonomy":["Bacteria","Spirochaetes","Spirochaetales","Borreliaceae","Borreliella"],"uniref90":"UniRef90_Q8RNW3","disprot_id":"DP01047","ncbi_taxon_id":224326,"regions_counter":8,"creator":"gerdos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":205,"region_id":"DP01047r001","released":"2022_03","ec_id":"ECO:0007680","reference_html":"BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorferi, contains a disordered region that undergoes a conformational change on ligand binding. <i> Kim JH, Singvall J, Schwarz-Linek U, Johnson BJ, Potts JR, Höök M. </i> J Biol Chem, 2004","term_id":"IDPO:0000002","curator_id":"mnecci","start":56,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15292204","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":205,"term_name":"molecular adaptor activity","start":56,"ec_name":"chromatography evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"15292204","version":3,"reference_html":"BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorferi, contains a disordered region that undergoes a conformational change on ligand binding. <i> Kim JH, Singvall J, Schwarz-Linek U, Johnson BJ, Potts JR, Höök M. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0007680","region_id":"DP01047r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":205,"term_name":"disorder to order","start":56,"ec_name":"chromatography evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15292204","version":2,"reference_html":"BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorferi, contains a disordered region that undergoes a conformational change on ligand binding. <i> Kim JH, Singvall J, Schwarz-Linek U, Johnson BJ, Potts JR, Höök M. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0007680","region_id":"DP01047r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":205,"region_id":"DP01047r004","released":"2022_03","ec_id":"ECO:0006325","reference_html":"BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorferi, contains a disordered region that undergoes a conformational change on ligand binding. <i> Kim JH, Singvall J, Schwarz-Linek U, Johnson BJ, Potts JR, Höök M. </i> J Biol Chem, 2004","term_id":"IDPO:0000002","curator_id":"mnecci","start":56,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15292204","version":2,"ec_name":"viscosity measurement evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":205,"term_name":"molecular adaptor activity","start":56,"ec_name":"viscosity measurement evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"15292204","version":3,"reference_html":"BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorferi, contains a disordered region that undergoes a conformational change on ligand binding. <i> Kim JH, Singvall J, Schwarz-Linek U, Johnson BJ, Potts JR, Höök M. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006325","region_id":"DP01047r005","curator_orcid":"0000-0001-9377-482X","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":205,"region_id":"DP01047r006","released":"2022_03","ec_id":"ECO:0006204","reference_html":"BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorferi, contains a disordered region that undergoes a conformational change on ligand binding. <i> Kim JH, Singvall J, Schwarz-Linek U, Johnson BJ, Potts JR, Höök M. </i> J Biol Chem, 2004","term_id":"IDPO:0000002","curator_id":"mnecci","start":56,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15292204","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":205,"term_name":"molecular adaptor activity","start":56,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"15292204","version":3,"reference_html":"BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorferi, contains a disordered region that undergoes a conformational change on ligand binding. <i> Kim JH, Singvall J, Schwarz-Linek U, Johnson BJ, Potts JR, Höök M. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006204","region_id":"DP01047r007","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":205,"term_name":"disorder to order","start":56,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15292204","version":2,"reference_html":"BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorferi, contains a disordered region that undergoes a conformational change on ligand binding. <i> Kim JH, Singvall J, Schwarz-Linek U, Johnson BJ, Potts JR, Höök M. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP01047r008","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2016_10","uniref100":"UniRef100_C5J482","date":"2016-09-16T12:34:51.000Z","acc":"O50835","name":"Fibronectin-binding protein BBK32","length":354,"organism":"Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)","dataset":[],"UniParc":"UPI00000568BD","genes":[{"name":{"value":"bbk32","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAC66134.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAC66134.1"}}]},"olnNames":[{"value":"BB_K32","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAC66134.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAC66134.1"}}]}]}],"alphafold_very_low_content":0.4632768361581921,"disorder_content":0.423728813559322,"disprot_consensus":{"full":[{"start":56,"end":205,"type":"T"}],"Structural state":[{"start":56,"end":205,"type":"D"}],"Molecular function":[{"start":56,"end":205,"type":"F"}],"Structural transition":[{"start":56,"end":205,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00170","name":"bZIP transcription factor","start":216,"end":268},{"id":"PF12498","name":"Basic leucine-zipper C terminal","start":283,"end":376}],"gene3D":[{"start":216,"end":270,"id":"1.20.5.170","name":"1.20.5.170"}]},"uniref50":"UniRef50_P12959","sequence":"MEHVISMEEILGPFWDLPPSPPPLPLPEQQPLVTDTGSVVIDGVVTQGGGDGEGGDMMGQNTTEWTFERLLEEEILINKTTLVTNSSCSTLNIDPVVEVDQGTMASGAVSAVGDPMEYNAILKRKLEVDLVAFKMWRASSVVNSERSQDSNNHNGGSKNVVQNKLNGEDPINNHAQNVDLRVRLATSSSSRDPSPSDEDMDGEVEILGFKMPTEERVRKRKESNRESARRSRYRKAAHLKELEDQVEQLKAENSCLLRRLAALNQKYNEANVDNRVLRADMETLRAKVKMGEDSLKRVMEMSSLPPSMPIPALPSSSDASVPIQDDIINYFSTTPAADEDAPVDNNSFIIMPMADPLQLVQAEDQPTMGAMELIQKTMGAMPTSPGSALQESQLLGLGPDETINMDMY","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","PACMAD clade","Panicoideae","Andropogonodae","Andropogoneae","Coicinae","Coix"],"uniref90":"UniRef90_Q39532","disprot_id":"DP01048","ncbi_taxon_id":4505,"regions_counter":6,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":276,"region_id":"DP01048r001","released":"2022_03","ec_id":"ECO:0007680","reference_html":"The bZIP region of the plant transcription factor opaque-2 forms stable homodimers in solution and retains its helical structure upon subunit dissociation. <i> Moreau VH, da Silva AC, Siloto RM, Valente AP, Leite A, Almeida FC. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"mnecci","start":224,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15096055","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":276,"term_name":"molecular adaptor activity","start":224,"ec_name":"chromatography evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"15096055","version":3,"reference_html":"The bZIP region of the plant transcription factor opaque-2 forms stable homodimers in solution and retains its helical structure upon subunit dissociation. <i> Moreau VH, da Silva AC, Siloto RM, Valente AP, Leite A, Almeida FC. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0007680","region_id":"DP01048r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":276,"term_name":"nucleic acid binding","start":224,"ec_name":"chromatography evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"15096055","version":3,"reference_html":"The bZIP region of the plant transcription factor opaque-2 forms stable homodimers in solution and retains its helical structure upon subunit dissociation. <i> Moreau VH, da Silva AC, Siloto RM, Valente AP, Leite A, Almeida FC. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0007680","region_id":"DP01048r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":276,"region_id":"DP01048r004","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The bZIP region of the plant transcription factor opaque-2 forms stable homodimers in solution and retains its helical structure upon subunit dissociation. <i> Moreau VH, da Silva AC, Siloto RM, Valente AP, Leite A, Almeida FC. </i> Biochemistry, 2004","term_id":"IDPO:0000002","curator_id":"mnecci","start":224,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15096055","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":276,"term_name":"molecular adaptor activity","start":224,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"15096055","version":3,"reference_html":"The bZIP region of the plant transcription factor opaque-2 forms stable homodimers in solution and retains its helical structure upon subunit dissociation. <i> Moreau VH, da Silva AC, Siloto RM, Valente AP, Leite A, Almeida FC. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006204","region_id":"DP01048r005","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":276,"term_name":"nucleic acid binding","start":224,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"15096055","version":3,"reference_html":"The bZIP region of the plant transcription factor opaque-2 forms stable homodimers in solution and retains its helical structure upon subunit dissociation. <i> Moreau VH, da Silva AC, Siloto RM, Valente AP, Leite A, Almeida FC. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006204","region_id":"DP01048r006","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q39532","date":"2016-09-16T13:21:24.000Z","acc":"Q39532","name":"Opaque 2","length":408,"organism":"Coix lacryma-jobi","dataset":[],"UniParc":"UPI00000A6AD6","genes":[],"alphafold_very_low_content":0.5514705882352942,"disorder_content":0.12990196078431374,"disprot_consensus":{"full":[{"start":224,"end":276,"type":"D"}],"Structural state":[{"start":224,"end":276,"type":"D"}],"Molecular function":[{"start":224,"end":276,"type":"F"}]}},{"acc":"Q6QCC2","sequence":"MNRTAFCCLSLTTALILTACSSGGGGVAADIGAGLADALTAPLDHKDKGLQSLTLDQSVRKNEKLKLAAQGAEKTYGNGDSLNTGKLKNDKVSRFDFIRQIEVDGQLITLESGEFQVYKQSHSALTAFQTEQIQDSEHSGKMVAKRQFRIGDIAGEHTSFDKLPEGGRATYRGTAFGSDDAGGKLTYTIDFAAKQGNGKIEHLKSPELNVDLAAADIKPDGKRHAVISGSVLYNQAEKGSYSLGIFGGKAQEVAGSAEVKTVNGIRHIGLAAKQ","alphafold_very_low_content":"0.10218978102189781","creator":"mnecci","dataset":[],"date":"2016-09-16T13:34:35.000Z","disprot_id":"DP01049","features":{"pfam":[{"id":"PF08794","name":"Factor H binding protein, C-terminal","start":161,"end":257},{"id":"PF20937","name":"Factor H binding protein, N-terminal","start":8,"end":93}],"gene3D":[{"start":159,"end":274,"id":"2.40.160.90","name":"2.40.160.90","_id":"685af523b4ac24d5329d8aa7"},{"start":16,"end":158,"id":"2.60.40.1980","name":"2.60.40.1980","_id":"685af523b4ac24d5329d8aa8"}]},"genes":[{"name":{"value":"gna1870","evidences":[{"source":{"id":"AAT01290.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/AAT01290.1","_id":"685af523b4ac24d5329d8ab5"},"code":"ECO:0000313","_id":"685af523b4ac24d5329d8ab4"}],"_id":"685af523b4ac24d5329d8ab6"},"synonyms":[{"value":"fhbp","evidences":[{"source":{"id":"AHY94658.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/AHY94658.1","_id":"685af523b4ac24d5329d8ab9"},"code":"ECO:0000313","_id":"685af523b4ac24d5329d8ab8"}],"_id":"685af523b4ac24d5329d8ab7"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d8ab3"}],"length":274,"name":"Factor H-binding protein","ncbi_taxon_id":487,"organism":"Neisseria meningitidis","regions_counter":2,"released":"2016_10","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"UniParc":"UPI000025440C","uniref100":"UniRef100_Q6QCC2","uniref50":"UniRef50_L0GCN6","uniref90":"UniRef90_Q6QCC2","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[],"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","_id":"685af523b4ac24d5329d8aad"}],"cross_refs":[{"db":"BMRB","id":"16058","_id":"685af523b4ac24d5329d8aae"},{"db":"PDB","id":"2KC0","_id":"685af523b4ac24d5329d8aaf"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-16T10:24:07.135Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":41,"end":51,"interaction_partner":[],"reference_html":"Solution structure of the factor H-binding protein, a survival factor and protective antigen of Neisseria meningitidis. <i> Cantini F, Veggi D, Dragonetti S, Savino S, Scarselli M, Romagnoli G, Pizza M, Banci L, Rappuoli R. </i> J Biol Chem, 2009","reference_id":"19196709","region_id":"DP01049r002","released":"2022_03","sample":[],"sequence_construct":"MVAADIGAGLADALTAPLDHKDKGLQSLTLDQSVRKNEKLKLAAQGAEKTYGNGDSLNTGKLKNDKVSRFDFIRQIEVDGQLITLESGEFQVYKQSHSALTAFQTEQIQDSEHSGKMVAKRQFRIGDIAGEHTSFDKLPEGGRATYRGTAFGSDDAGGKLTYTIDFAAKQGNGKIEHLKSPELNVDLAAADIKPDGKRHAVISGSVLYNQAEKGSYSLGIFGGKAQEVAGSAEVKTVNGIRHIGLAAKQHHHHHH","statement":[{"type":"Results","text":"The latter interactions define the conformation of a long loop (segment 22–32), which is completely solvent-exposed and rich in charged residues.","_id":"685af523b4ac24d5329d8ab0"},{"type":"Curator statement","text":"The segment 22-32 is corresponding to 41-51 in UniProt.","_id":"685af523b4ac24d5329d8ab1"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-10-13T20:26:49.924Z","_id":"685af523b4ac24d5329d8ab2"},"version":0,"_id":"685af523b4ac24d5329d8aac","reference_source":"pmid"}],"__v":0,"disorder_content":0.040145985401459854,"disprot_consensus":{"full":[{"start":41,"end":51,"type":"D"}],"Structural state":[{"start":41,"end":51,"type":"D"}]}},{"features":{"pfam":[{"id":"PF17209","name":"Hfq protein","start":7,"end":69}],"gene3D":[{"start":1,"end":72,"id":"2.30.30.100","name":"2.30.30.100"}]},"uniref50":"UniRef50_Q9ZI76","sequence":"MAKGQSLQDPFLNALRRERVPVSIYLVNGIKLQGQIESFDQFVILLKNTVSQMVYKHAISTVVPSRPVSHHSNNAGGGTSSNYHHGSSAQNTSAQQDSEETE","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_A4W5R3","disprot_id":"DP01050","ncbi_taxon_id":83333,"regions_counter":5,"creator":"eschad","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":102,"region_id":"DP01050r001","start":75,"ec_id":"ECO:0006165","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21330354","version":4,"reference_html":"Structural insights into the dynamics and function of the C-terminus of the E. coli RNA chaperone Hfq. <i> Beich-Frandsen M, Vecerek B, Konarev PV, Sjöblom B, Kloiber K, Hämmerle H, Rajkowitsch L, Miles AJ, Kontaxis G, Wallace BA, Svergun DI, Konrat R, Bläsi U, Djinovic-Carugo K. </i> Nucleic Acids Res, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":102,"region_id":"DP01050r002","start":75,"ec_id":"ECO:0006202","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","ec_name":"synchrotron radiation circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21330354","version":4,"reference_html":"Structural insights into the dynamics and function of the C-terminus of the E. coli RNA chaperone Hfq. <i> Beich-Frandsen M, Vecerek B, Konarev PV, Sjöblom B, Kloiber K, Hämmerle H, Rajkowitsch L, Miles AJ, Kontaxis G, Wallace BA, Svergun DI, Konrat R, Bläsi U, Djinovic-Carugo K. </i> Nucleic Acids Res, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":102,"term_name":"RNA folding chaperone","start":75,"ec_name":"synchrotron radiation circular dichroism evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"21330354","version":5,"reference_html":"Structural insights into the dynamics and function of the C-terminus of the E. coli RNA chaperone Hfq. <i> Beich-Frandsen M, Vecerek B, Konarev PV, Sjöblom B, Kloiber K, Hämmerle H, Rajkowitsch L, Miles AJ, Kontaxis G, Wallace BA, Svergun DI, Konrat R, Bläsi U, Djinovic-Carugo K. </i> Nucleic Acids Res, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140691","ec_id":"ECO:0006202","region_id":"DP01050r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA or an RNA-containing complex to assist the folding process.\" [PMID:31165735]","disprot_namespace":"Disorder function","term_is_binding":false},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":102,"term_name":"disorder to order","start":75,"ec_name":"synchrotron radiation circular dichroism evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21330354","version":4,"reference_html":"Structural insights into the dynamics and function of the C-terminus of the E. coli RNA chaperone Hfq. <i> Beich-Frandsen M, Vecerek B, Konarev PV, Sjöblom B, Kloiber K, Hämmerle H, Rajkowitsch L, Miles AJ, Kontaxis G, Wallace BA, Svergun DI, Konrat R, Bläsi U, Djinovic-Carugo K. </i> Nucleic Acids Res, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006202","region_id":"DP01050r004","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":102,"term_name":"DNA binding","start":75,"ec_name":"synchrotron radiation circular dichroism evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"21330354","version":5,"reference_html":"Structural insights into the dynamics and function of the C-terminus of the E. coli RNA chaperone Hfq. <i> Beich-Frandsen M, Vecerek B, Konarev PV, Sjöblom B, Kloiber K, Hämmerle H, Rajkowitsch L, Miles AJ, Kontaxis G, Wallace BA, Svergun DI, Konrat R, Bläsi U, Djinovic-Carugo K. </i> Nucleic Acids Res, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003677","ec_id":"ECO:0006202","region_id":"DP01050r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_A7ZV41","date":"2016-09-16T13:54:34.000Z","acc":"P0A6X3","name":"RNA-binding protein Hfq","length":102,"organism":"Escherichia coli (strain K12)","dataset":["Stress response proteins"],"UniParc":"UPI00001562A2","genes":[{"name":{"value":"hfq","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00436","url":"https://hamap.expasy.org/unirule/MF_00436"}}]},"olnNames":[{"value":"b4172"},{"value":"JW4130"}]}],"alphafold_very_low_content":0.13725490196078433,"disorder_content":0.27450980392156865,"disprot_consensus":{"full":[{"start":75,"end":102,"type":"T"}],"Structural state":[{"start":75,"end":102,"type":"D"}],"Molecular function":[{"start":75,"end":102,"type":"F"}],"Structural transition":[{"start":75,"end":102,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00009","name":"Elongation factor Tu GTP binding domain","start":258,"end":478},{"id":"PF03144","name":"Elongation factor Tu domain 2","start":502,"end":570},{"id":"PF22594","name":"GTP-eEF1A C-terminal domain-like","start":581,"end":680}],"gene3D":[{"start":485,"end":574,"id":"2.40.30.10","name":"Translation factors"},{"start":577,"end":684,"id":"2.40.30.10","name":"Translation factors"},{"start":238,"end":484,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_P05453","sequence":"MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVDTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVNDMFGGKDHVSLIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREAKDAGRQGWYLSWVMDTNKEERNDGKTIEVGKAYFETEKRRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYETGFERGGQTREHALLAKTQGVNKMVVVVNKMDDPTVNWSKERYDQCVSNVSNFLRAIGYNIKTDVVFMPVSGYSGANLKDHVDPKECPWYTGPTLLEYLDTMNHVDRHINAPFMLPIAAKMKDLGTIVEGKIESGHIKKGQSTLLMPNKTAVEIQNIYNETENEVDMAMCGEQVKLRIKGVEEEDISPGFVLTSPKNPIKSVTKFVAQIAIVELKSIIAAGFSCVMHVHTAIEEVHIVKLLHKLEKGTNRKSKKPPAFAKKGMKVIAVLETEAPVCVETYQDYPQLGRFTLRDQGTTIAIGKIVKIAE","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P05453","disprot_id":"DP01051","ncbi_taxon_id":4932,"regions_counter":2,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":253,"region_id":"DP01051r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The role of conformational flexibility in prion propagation and maintenance for Sup35p. <i> Scheibel T, Lindquist SL. </i> Nat Struct Biol, 2001","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"11685242","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":253,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"11685242","version":3,"reference_html":"The role of conformational flexibility in prion propagation and maintenance for Sup35p. <i> Scheibel T, Lindquist SL. </i> Nat Struct Biol, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP01051r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q7LKB1","date":"2016-09-16T15:59:27.000Z","acc":"Q7LKB1","name":"Prion protein","length":685,"organism":"Saccharomyces cerevisiae","dataset":[],"UniParc":"UPI000006A2A9","genes":[{"name":{"value":"SUP35","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAK26176.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAK26176.1"}}]}}],"alphafold_very_low_content":0.34744525547445254,"disorder_content":0.36934306569343067,"disprot_consensus":{"full":[{"start":1,"end":253,"type":"D"}],"Structural state":[{"start":1,"end":253,"type":"D"}],"Molecular function":[{"start":1,"end":253,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":386,"end":439},{"id":"PF01585","name":"G-patch domain","start":297,"end":337}],"gene3D":[{"start":360,"end":443,"id":"3.30.70.330","name":"3.30.70.330"}]},"uniref50":"UniRef50_Q8MWS6","sequence":"MLDSLYGDLPPPSKDEGCPPKPTSLLGSLYDDLDDTPDTSSSSSASSSSSSSSALFASSSWTAERLQMLTPAVVRKQTLKSASGLGAASSQTAGQASSSKPPLDVAAVAAAASAAAAAVAAQLKAVKSEAFGDRARSLFGRGEREKAEALGASDEAASAPGVAGGVKRDESEKGESLRALGRLGVETAEGRRGHQGGDKETESSGFVSIGQMKDEYDPGTPNDYSAIYREKIRKQQREELERLRQQELDKQRRDRELPGSGSSLSGVAFGDSPSTPSPPAAPPAPPVLPSYIDPAKKSFAARMMEKMGWKHGEGLGVNKQGITAPLVAKKTAMSSGVIVQGAEVVQAAAQVWAQFNRPPTRVLLLLNMVGRGEVDEDLKEETEEEAAKFGNLLQVKIVEAAEAPDDEAVRIFCEYERKEEATRAFMTMNGRVFGGRTVKGRFYCEERWGKDDLMPNPEEEADKPLD","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Conoidasida","Coccidia","Eucoccidiorida","Eimeriorina","Sarcocystidae","Toxoplasma"],"uniref90":"UniRef90_Q8MWS6","disprot_id":"DP01052","ncbi_taxon_id":5811,"regions_counter":3,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":343,"region_id":"DP01052r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structural and functional characterization of the TgDRE multidomain protein, a DNA repair enzyme from Toxoplasma gondii. <i> Frénal K, Callebaut I, Wecker K, Prochnicka-Chalufour A, Dendouga N, Zinn-Justin S, Delepierre M, Tomavo S, Wolff N. </i> Biochemistry, 2006","term_id":"IDPO:0000002","curator_id":"mnecci","start":283,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"16605254","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":343,"term_name":"molecular adaptor activity","start":283,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"16605254","version":3,"reference_html":"Structural and functional characterization of the TgDRE multidomain protein, a DNA repair enzyme from Toxoplasma gondii. <i> Frénal K, Callebaut I, Wecker K, Prochnicka-Chalufour A, Dendouga N, Zinn-Justin S, Delepierre M, Tomavo S, Wolff N. </i> Biochemistry, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006204","region_id":"DP01052r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":343,"term_name":"DNA binding","start":283,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"16605254","version":3,"reference_html":"Structural and functional characterization of the TgDRE multidomain protein, a DNA repair enzyme from Toxoplasma gondii. <i> Frénal K, Callebaut I, Wecker K, Prochnicka-Chalufour A, Dendouga N, Zinn-Justin S, Delepierre M, Tomavo S, Wolff N. </i> Biochemistry, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003677","ec_id":"ECO:0006204","region_id":"DP01052r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q8MWS6","date":"2016-09-16T16:11:45.000Z","acc":"Q8MWS6","name":"DNA repair enzyme","length":466,"organism":"Toxoplasma gondii","dataset":["Stress response proteins"],"UniParc":"UPI00000802B2","genes":[],"alphafold_very_low_content":0.48068669527896996,"disorder_content":0.13090128755364808,"disprot_consensus":{"full":[{"start":283,"end":343,"type":"D"}],"Structural state":[{"start":283,"end":343,"type":"D"}],"Molecular function":[{"start":283,"end":343,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00031","name":"Cystatin domain","start":4,"end":91}],"gene3D":[{"start":1,"end":98,"id":"3.10.450.10","name":"3.10.450.10"}]},"uniref50":"UniRef50_P04080","sequence":"MMCGAPSATQPATAETQHIADQVRSQLEEKENKKFPVFKAVSFKSQVVAGTNYFIKVHVGDEDFVHLRVFQSLPHENKPLTLSNYQTNKAKHDELTYF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P04080","disprot_id":"DP01054","ncbi_taxon_id":9606,"regions_counter":5,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":67,"region_id":"DP01054r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"In vitro study of stability and amyloid-fibril formation of two mutants of human stefin B (cystatin B) occurring in patients with EPM1. <i> Rabzelj S, Turk V, Zerovnik E. </i> Protein Sci, 2005","term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"16155205","version":4,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"The R68X mutant (Arg68Stop) is a peptide of 67 amino acids from the N terminus of stefin B. CD spectra have shown that the R68X peptide is not folded, in contrast to the G4R mutant, which folds like wild type.","type":"Abstract"},{"text":"Far-UV CD spectra (Fig. 1A) for the wt stefin B and the G4R mutant are very similar; both proteins give characteristic CD spectra for α/β secondary structure with minima at 222 nm, while the R68X mutant gives a CD spectrum characteristic of unfolded proteins with a minimum at 200 nm and low ellipticity in the 210–230 nm region.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-09T14:43:20.307Z"}},{"start":1,"end":67,"reference_id":"16155205","reference_source":"pmid","reference_html":"In vitro study of stability and amyloid-fibril formation of two mutants of human stefin B (cystatin B) occurring in patients with EPM1. <i> Rabzelj S, Turk V, Zerovnik E. </i> Protein Sci, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01054r004","statement":[{"text":"The R68X mutant showed a very high tendency to fibrillate (Fig. 8 [triangle]). Fibrils formed in 1 h without the addition of TFE (Fig. 8A1,A2 [triangle]). However, these fibrils were shorter from those grown in the presence of TFE, as judged from TEM images (Fig. 8B1,B2,C [triangle]).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-15T10:36:14.463Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":67,"reference_id":"16155205","reference_source":"pmid","reference_html":"In vitro study of stability and amyloid-fibril formation of two mutants of human stefin B (cystatin B) occurring in patients with EPM1. <i> Rabzelj S, Turk V, Zerovnik E. </i> Protein Sci, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01054r005","statement":[{"text":"For the R68X mutant, in the absence of TFE and in 3% TFE, fibril formation was very much faster (Fig. 6). No distinct lag phase could be observed, and in a few hours the whole reaction reached the plateau phase.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-09T14:43:23.278Z"}}],"released":"2016_10","uniref100":"UniRef100_P04080","date":"2016-09-16T16:52:17.000Z","acc":"Q76LA1","name":"CSTB protein","length":98,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI0000001F9C","genes":[{"name":{"value":"CSTB","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAC20304.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAC20304.1"}}]},"orfNames":[{"value":"hCG_401291","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EAX09473.1","url":"https://www.ebi.ac.uk/ena/browser/view/EAX09473.1"}}]}]}],"alphafold_very_low_content":0,"disorder_content":0.6836734693877551,"disprot_consensus":{"full":[{"start":1,"end":67,"type":"D"}],"Structural state":[{"start":1,"end":67,"type":"D"}],"Biological process":[{"start":1,"end":67,"type":"F"}]}},{"features":{"pfam":[{"id":"PF11493","name":"Thylakoid soluble phosphoprotein TSP9","start":21,"end":101}]},"uniref50":"UniRef50_Q8GT36","sequence":"MSSLPFVFGAAASSRVVTAAAAKGTAETKQEKSFVDWLLGKITKEDQFYETDPILRGGDVKSSGSTSGKKGGTTSGKKGTVSIPSKKKNGNGGVFGGLFAKKD","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","Caryophyllales","Chenopodiaceae","Chenopodioideae","Anserineae","Spinacia"],"uniref90":"UniRef90_Q8GT36","disprot_id":"DP01055","ncbi_taxon_id":3562,"regions_counter":3,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":103,"region_id":"DP01055r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Micelle-induced folding of spinach thylakoid soluble phosphoprotein of 9 kDa and its functional implications. <i> Song J, Lee MS, Carlberg I, Vener AV, Markley JL. </i> Biochemistry, 2006","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"17176085","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Biological process","reference_source":"pmid","ec_ontology":"ECO","end":103,"term_name":"localization","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"17176085","version":3,"reference_html":"Micelle-induced folding of spinach thylakoid soluble phosphoprotein of 9 kDa and its functional implications. <i> Song J, Lee MS, Carlberg I, Vener AV, Markley JL. </i> Biochemistry, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0051179","ec_id":"ECO:0006165","region_id":"DP01055r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":103,"term_name":"lipid binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"17176085","version":3,"reference_html":"Micelle-induced folding of spinach thylakoid soluble phosphoprotein of 9 kDa and its functional implications. <i> Song J, Lee MS, Carlberg I, Vener AV, Markley JL. </i> Biochemistry, 2006","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008289","ec_id":"ECO:0006165","region_id":"DP01055r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q8GT36","date":"2016-09-16T17:21:51.000Z","acc":"Q8GT36","name":"Thylakoid soluble phosphoprotein","length":103,"organism":"Spinacia oleracea","dataset":[],"UniParc":"UPI00000AE3B9","genes":[{"name":{"value":"tsp9","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAD45559.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAD45559.1"}}]},"orfNames":[{"value":"SOVF_029300","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"KNA22939.1","url":"https://www.ebi.ac.uk/ena/browser/view/KNA22939.1"}}]}]}],"alphafold_very_low_content":0.11650485436893204,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":103,"type":"D"}],"Structural state":[{"start":1,"end":103,"type":"D"}],"Biological process":[{"start":1,"end":103,"type":"F"}],"Molecular function":[{"start":1,"end":103,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_A7UMX5","sequence":"MIQSAAPSIPRVEVILDCSDREKEAPKSLAERGCVDSQVEGGQSEAPPSLPSFAISSEGTEQGEDNQHSEKDHRPLKHRARHARLRRSESLSEKQVKEAKSKCKSIALLLTAAPNPNSKGVLMFKKRRQRARKYTLVSYGTGELERDEDEGEEGEVEEGDKENTFEVSLLATSESEIDEDFFSDIDNDKKIVTFDWDSGLLEVEKKTKSGDEMQTLPETTGKGALMFARRRQRMDQITAEQEEMKARTAHAEEQREVTVSENFQKVSSSAYQTKEEEMLRQQPCISKSYADVSQNDGKIVQQNGFGVAPDTSLSFQSSEAQKAASLNRTAKPFPFGVQNRAAAPFSPTRNVTSPLSDLPAPPPYCSISPPPEALYRPLSAPAASKAAPILWSHTEPTERIASRDERIAVPAKRTGILQEAKRRSTSKPMFSFKEAPKVSPNPALLSLVHNAEGKKGSGAGFESGPEEDYLSLGAEACNFMQSQASKQKAPPPTAPKPSLKVSPAAGTPVSPVWSPAVASNKAPSFPAPASPQAAYPAPLKSPQYPHSPSANPPNTLNLSGPFKGPQATLASPNHPAKTPTTPSAGETKPFEMPPEMRGKGAQLFARRHSRMEKYVVDSETVQANMARASSPTPSLPASWKYSSNVRAPPPVAYNPIHSPSYPPAATKPFPKSTAATKNTKRKPKKGLNALDIMKHQPYQLDASLFTFQPPSNKESLGIKQIPKLPTSKQATSLRLPGSASPTNVRASSVYSVPAYSSQPSFQSNASTPVNESYTPTGYSAFSKPESTTSSLFTAPRPKFSAKKAGVIAQERSSGRSLSLPGKPSFISRATSPTSPLIFQPAPDYFSKPDTAADKPGKRLTPWEAAAKSPLGLVDEAFRPQNMQESIAANVVSAAHRKTLPEPPDEWKQKVSYEPPGPSASLALLGGKQPGVTSARKSSLSVSNATTQAGSQQQYAYCSQRSQTDPDIMSMDSRSDYGLSTADSNYNPQPRGWRRPT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Meleagridinae","Meleagris"],"uniref90":"UniRef90_A7UMX5","disprot_id":"DP01056","ncbi_taxon_id":9103,"regions_counter":4,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":996,"region_id":"DP01056r001","released":"2022_03","ec_id":"ECO:0007064","reference_html":"Fesselin is a natively unfolded protein. <i> Khaymina SS, Kenney JM, Schroeter MM, Chalovich JM. </i> J Proteome Res, 2007","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"17676886","version":2,"ec_name":"dynamic light scattering assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":996,"region_id":"DP01056r002","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Fesselin is a natively unfolded protein. <i> Khaymina SS, Kenney JM, Schroeter MM, Chalovich JM. </i> J Proteome Res, 2007","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"17676886","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":996,"region_id":"DP01056r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Fesselin is a natively unfolded protein. <i> Khaymina SS, Kenney JM, Schroeter MM, Chalovich JM. </i> J Proteome Res, 2007","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"17676886","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":996,"region_id":"DP01056r004","released":"2022_03","ec_id":"ECO:0001249","reference_html":"Fesselin is a natively unfolded protein. <i> Khaymina SS, Kenney JM, Schroeter MM, Chalovich JM. </i> J Proteome Res, 2007","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"17676886","version":2,"ec_name":"fluorescence evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_A7UMX5","date":"2016-09-16T17:48:25.000Z","acc":"A7UMX5","name":"Synaptopodin 2 variant","length":996,"organism":"Meleagris gallopavo","dataset":[],"UniParc":"UPI00015C3184","genes":[],"alphafold_very_low_content":0.7228915662650602,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":996,"type":"D"}],"Structural state":[{"start":1,"end":996,"type":"D"}]}},{"features":{"pfam":[{"id":"PF28971","name":"Cold-regulated 15 domain","start":3,"end":139}]},"uniref50":"UniRef50_Q42512","sequence":"MAMSFSGAVLTGMASSFHSGAKQSSFGAVRVGQKTQFVVVSQRKKSLIYAAKGDGNILDDLNEATKKASDFVTDKTKEALADGEKAKDYVVEKNSETADTLGKEAEKAAAYVEEKGKEAANKAAEFAEGKAGEAKDATK","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q42512","disprot_id":"DP01057","ncbi_taxon_id":3702,"regions_counter":14,"creator":"eficho","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":139,"region_id":"DP01057r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Interaction of two intrinsically disordered plant stress proteins (COR15A and COR15B) with lipid membranes in the dry state. <i> Thalhammer A, Hundertmark M, Popova AV, Seckler R, Hincha DK. </i> Biochim Biophys Acta, 2010","term_id":"IDPO:0000002","curator_id":"mnecci","start":41,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"20510170","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":139,"term_name":"disorder to order","start":41,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"20510170","version":2,"reference_html":"Interaction of two intrinsically disordered plant stress proteins (COR15A and COR15B) with lipid membranes in the dry state. <i> Thalhammer A, Hundertmark M, Popova AV, Seckler R, Hincha DK. </i> Biochim Biophys Acta, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP01057r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":139,"term_name":"protein binding","start":41,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"20510170","version":3,"reference_html":"Interaction of two intrinsically disordered plant stress proteins (COR15A and COR15B) with lipid membranes in the dry state. <i> Thalhammer A, Hundertmark M, Popova AV, Seckler R, Hincha DK. </i> Biochim Biophys Acta, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP01057r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":139,"term_name":"lipid binding","start":41,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"20510170","version":3,"reference_html":"Interaction of two intrinsically disordered plant stress proteins (COR15A and COR15B) with lipid membranes in the dry state. <i> Thalhammer A, Hundertmark M, Popova AV, Seckler R, Hincha DK. </i> Biochim Biophys Acta, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008289","ec_id":"ECO:0006204","region_id":"DP01057r004","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":139,"region_id":"DP01057r005","released":"2022_03","ec_id":"ECO:0007689","reference_html":"Interaction of two intrinsically disordered plant stress proteins (COR15A and COR15B) with lipid membranes in the dry state. <i> Thalhammer A, Hundertmark M, Popova AV, Seckler R, Hincha DK. </i> Biochim Biophys Acta, 2010","term_id":"IDPO:0000002","curator_id":"mnecci","start":41,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"20510170","version":2,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":139,"term_name":"protein binding","start":41,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"20510170","version":3,"reference_html":"Interaction of two intrinsically disordered plant stress proteins (COR15A and COR15B) with lipid membranes in the dry state. <i> Thalhammer A, Hundertmark M, Popova AV, Seckler R, Hincha DK. </i> Biochim Biophys Acta, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007689","region_id":"DP01057r006","curator_orcid":"0000-0001-9377-482X","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":139,"term_name":"lipid binding","start":41,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"20510170","version":3,"reference_html":"Interaction of two intrinsically disordered plant stress proteins (COR15A and COR15B) with lipid membranes in the dry state. <i> Thalhammer A, Hundertmark M, Popova AV, Seckler R, Hincha DK. </i> Biochim Biophys Acta, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008289","ec_id":"ECO:0007689","region_id":"DP01057r007","curator_orcid":"0000-0001-9377-482X","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":41,"end":139,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins.  <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2024-08-26T14:48:38.781Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP01057r008","statement":[{"text":"Figure S5 shows FTIR spectra of the six LEA_4 proteins in EG concentrations ranging from 0 to 12 osM. Similar to decreasing RH, increasing osmolarity induces coil-helix transitions, indicated by a shift of the Amide I maxima to higher wavenumbers.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":"ethylene glycol"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-16T10:25:22.758Z"}},{"start":41,"end":139,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins.  <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2024-08-26T14:49:18.488Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP01057r009","statement":[{"text":"All proteins showed typical random coil spectra in dilute solution. With increasing concentrations of each of the co-solvents, the changes in the spectral shape report on the formation of ordered secondary structure. In EG (Figure S6), four out of the six proteins showed a two-state transition, indicated by the isodichroic points and the typical α-helical spectral shape with two negative maxima at 208 and 222 nm at high EG concentrations.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":"ethylene glycol"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-16T10:25:20.806Z"}},{"start":41,"end":139,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins.  <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2024-08-26T14:45:56.748Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":1,"region_id":"DP01057r010","statement":[{"text":"Simultaneous static and dynamic light scattering (SLS/DLS) measurements were conducted to determine the apparent average single particle mass (Mapp) and the apparent average hydrodynamic radius (RS) of the proteins in solution as a function of concentration (Figure S4, [30]). Absolute molecular mass and RS were obtained by extrapolation of apparent molecular mass and RS to infinite dilution. All investigated LEA proteins are essentially monomeric under fully hydrated conditions. Compared to globular proteins, RS of all investigated LEA proteins was rather large, indicating their expanded, non-compact nature.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-16T10:25:03.430Z"}},{"start":41,"end":139,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among <i>Arabidopsis thaliana</i> LEA_4 Proteins. <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2024-08-28T09:33:09.198Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP01057r012","statement":[{"text":"All proteins showed typical random coil spectra in dilute solution.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-16T10:26:32.142Z"}},{"start":41,"end":139,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among <i>Arabidopsis thaliana</i> LEA_4 Proteins. <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2024-08-28T11:26:01.584Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0009409","term_name":"response to cold","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IDA","region_id":"DP01057r014","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":" 39073","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}],"entry_name":"6-carboxyfluorescein"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"170453367","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"10724471 ","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"56842030  ","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"45109789","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]}],"statement":[{"text":"Therefore, we analyzed the stability of liposomes modeling the lipid composition of inner chloroplast membranes (ICMM) after a freeze/thaw cycle and a dehydration/rehydration cycle in the ethylene glycolpresence of all six LEA_4 proteins at different LEA protein: lipid mass ratios (Figure 13).","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cold stimulus, a temperature stimulus below the optimal temperature for that organism.\" [GOC:lr]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T08:41:47.661Z"}}],"released":"2016_10","uniref100":"UniRef100_Q42512","date":"2016-09-16T18:09:32.000Z","acc":"Q42512","name":"Protein COLD-REGULATED 15A, chloroplastic","length":139,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI00000ACCE1","genes":[{"name":{"value":"COR15A","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16668917","url":"http://www.ncbi.nlm.nih.gov/pubmed/16668917","alternativeUrl":"https://europepmc.org/abstract/MED/16668917"}}]},"orfNames":[{"value":"F14N22.19","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAD22999.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD22999.1"}}]}],"olnNames":[{"value":"At2g42540","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT2G42540","url":""}}]}]}],"alphafold_very_low_content":0.7050359712230215,"disorder_content":0.7122302158273381,"disprot_consensus":{"full":[{"start":41,"end":139,"type":"T"}],"Structural state":[{"start":41,"end":139,"type":"D"}],"Structural transition":[{"start":41,"end":139,"type":"T"}],"Molecular function":[{"start":41,"end":139,"type":"F"}],"Biological process":[{"start":41,"end":139,"type":"F"}]}},{"features":{"pfam":[{"id":"PF28971","name":"Cold-regulated 15 domain","start":3,"end":140}]},"uniref50":"UniRef50_Q42512","sequence":"MAMSLSGAVLSGMGSSFHNVGAKQSGVGTVRVGRKSELVVVAQRKKSLIYAVKSDGNILDDLNEATKKASDFVTDKTKEALADGEKTKDYIVEKTIEANETATEEAKKALDYVTEKGKEAGNKAAEFVEGKAEEAKNATKS","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q9SIN5","disprot_id":"DP01058","ncbi_taxon_id":3702,"regions_counter":7,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":139,"region_id":"DP01058r001","released":"2022_03","ec_id":"ECO:0007689","reference_html":"Interaction of two intrinsically disordered plant stress proteins (COR15A and COR15B) with lipid membranes in the dry state. <i> Thalhammer A, Hundertmark M, Popova AV, Seckler R, Hincha DK. </i> Biochim Biophys Acta, 2010","term_id":"IDPO:0000002","curator_id":"mnecci","start":41,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"20510170","version":2,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":139,"term_name":"protein binding","start":41,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"20510170","version":3,"reference_html":"Interaction of two intrinsically disordered plant stress proteins (COR15A and COR15B) with lipid membranes in the dry state. <i> Thalhammer A, Hundertmark M, Popova AV, Seckler R, Hincha DK. </i> Biochim Biophys Acta, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007689","region_id":"DP01058r002","curator_orcid":"0000-0001-9377-482X","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":139,"term_name":"lipid binding","start":41,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"20510170","version":3,"reference_html":"Interaction of two intrinsically disordered plant stress proteins (COR15A and COR15B) with lipid membranes in the dry state. <i> Thalhammer A, Hundertmark M, Popova AV, Seckler R, Hincha DK. </i> Biochim Biophys Acta, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008289","ec_id":"ECO:0007689","region_id":"DP01058r003","curator_orcid":"0000-0001-9377-482X","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":139,"region_id":"DP01058r004","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Interaction of two intrinsically disordered plant stress proteins (COR15A and COR15B) with lipid membranes in the dry state. <i> Thalhammer A, Hundertmark M, Popova AV, Seckler R, Hincha DK. </i> Biochim Biophys Acta, 2010","term_id":"IDPO:0000002","curator_id":"mnecci","start":41,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"20510170","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":139,"term_name":"disorder to order","start":41,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"20510170","version":2,"reference_html":"Interaction of two intrinsically disordered plant stress proteins (COR15A and COR15B) with lipid membranes in the dry state. <i> Thalhammer A, Hundertmark M, Popova AV, Seckler R, Hincha DK. </i> Biochim Biophys Acta, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP01058r005","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":139,"term_name":"protein binding","start":41,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"20510170","version":3,"reference_html":"Interaction of two intrinsically disordered plant stress proteins (COR15A and COR15B) with lipid membranes in the dry state. <i> Thalhammer A, Hundertmark M, Popova AV, Seckler R, Hincha DK. </i> Biochim Biophys Acta, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP01058r006","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":139,"term_name":"lipid binding","start":41,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"20510170","version":3,"reference_html":"Interaction of two intrinsically disordered plant stress proteins (COR15A and COR15B) with lipid membranes in the dry state. <i> Thalhammer A, Hundertmark M, Popova AV, Seckler R, Hincha DK. </i> Biochim Biophys Acta, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008289","ec_id":"ECO:0006204","region_id":"DP01058r007","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q9SIN5","date":"2016-09-16T18:10:44.000Z","acc":"Q9SIN5","name":"Protein COLD-REGULATED 15B, chloroplastic","length":141,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI000009C928","genes":[{"name":{"value":"COR15B","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8260628","url":"http://www.ncbi.nlm.nih.gov/pubmed/8260628","alternativeUrl":"https://europepmc.org/abstract/MED/8260628"}}]},"orfNames":[{"value":"F14N22","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAD23000.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD23000.1"}}]}],"olnNames":[{"value":"At2g42530","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT2G42530","url":""}}]}]}],"alphafold_very_low_content":0.5957446808510638,"disorder_content":0.7021276595744681,"disprot_consensus":{"full":[{"start":41,"end":139,"type":"T"}],"Structural state":[{"start":41,"end":139,"type":"D"}],"Molecular function":[{"start":41,"end":139,"type":"F"}],"Structural transition":[{"start":41,"end":139,"type":"T"}]}},{"acc":"Q71FK2","sequence":"MPDTTPVAATSSAPPTAKDAGAKAPSDFSNPNTAPSLSDLKKVKYVSTVTSVATPAEIEALGKIFTAMGLAANETGPAMWDLARAYADVQSSKSAQLIGATPSNPALSRRALAAQFDRINITPRQFCMYFAKVVWNILLDSNIPPANWAKLGYQEDTKFAAFDFFDGVTNPASLQPADGLIRQPNEKELAAHSVAKYGALARQKISTGNYITTLGEVTRGHMGGANTMYAIDAPPEL","creator":"ahatos","dataset":["Viral proteins"],"date":"2016-09-16T22:38:44.000Z","disprot_id":"DP01059","features":{"pfam":[{"id":"PF00286","name":"Viral coat protein","start":50,"end":188}]},"genes":[],"length":237,"name":"Coat protein","ncbi_taxon_id":112229,"organism":"Pepino mosaic virus","regions_counter":3,"released":"2016_10","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Alsuviricetes","Tymovirales","Alphaflexiviridae","Potexvirus"],"UniParc":"UPI00000FA19E","uniref100":"UniRef100_Q8JJF2","uniref50":"UniRef50_P15100","uniref90":"UniRef90_T2KEI6","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5FN1","_id":"685af523b4ac24d5329d8ac3"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006224","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":20,"interaction_partner":[],"reference_html":"The near-atomic cryoEM structure of a flexible filamentous plant virus shows homology of its coat protein with nucleoproteins of animal viruses. <i> Agirrezabala X, Méndez-López E, Lasso G, Sánchez-Pina MA, Aranda M, Valle M. </i> Elife, 2015","reference_id":"26673077","region_id":"DP01059r003","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"The first 20 amino acids in the N-terminal side are not included in the atomic model because the region projects outwards, and its density vanishes due to high flexibility.","_id":"685af523b4ac24d5329d8ac4"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":1,"_id":"685af523b4ac24d5329d8ac2","reference_source":"pmid"}],"__v":0,"disorder_content":0.08438818565400844,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"D"}],"Structural state":[{"start":1,"end":20,"type":"D"}]}},{"acc":"Q9Y6C2","sequence":"MAPRTLWSCYLCCLLTAAAGAASYPPRGFSLYTGSSGALSPGGPQAQIAPRPASRHRNWCAYVVTRTVSCVLEDGVETYVKYQPCAWGQPQCPQSIMYRRFLRPRYRVAYKTVTDMEWRCCQGYGGDDCAESPAPALGPASSTPRPLARPARPNLSGSSAGSPLSGLGGEGPGESEKVQQLEEQVQSLTKELQGLRGVLQGLSGRLAEDVQRAVETAFNGRQQPADAAARPGVHETLNEIQHQLQLLDTRVSTHDQELGHLNNHHGGSSSSGGSRAPAPASAPPGPSEELLRQLEQRLQESCSVCLAGLDGFRRQQQEDRERLRAMEKLLASVEERQRHLAGLAVGRRPPQECCSPELGRRLAELERRLDVVAGSVTVLSGRRGTELGGAAGQGGHPPGYTSLASRLSRLEDRFNSTLGPSEEQEESWPGAPGGLSHWLPAARGRLEQLGGLLANVSGELGGRLDLLEEQVAGAMQACGQLCSGAPGEQDSQVSEILSALERRVLDSEGQLRLVGSGLHTVEAAGEARQATLEGLQEVVGRLQDRVDAQDETAAEFTLRLNLTAARLGQLEGLLQAHGDEGCGACGGVQEELGRLRDGVERCSCPLLPPRGPGAGPGVGGPSRGPLDGFSVFGGSSGSALQALQGELSEVILSFSSLNDSLNELQTTVEGQGADLADLGATKDRIISEINRLQQEATEHATESEERFRGLEEGQAQAGQCPSLEGRLGRLEGVCERLDTVAGGLQGLREGLSRHVAGLWAGLRETNTTSQMQAALLEKLVGGQAGLGRRLGALNSSLQLLEDRLHQLSLKDLTGPAGEAGPPGPPGLQGPPGPAGPPGSPGKDGQEGPIGPPGPQGEQGVEGAPAAPVPQVAFSAALSLPRSEPGTVPFDRVLLNDGGYYDPETGVFTAPLAGRYLLSAVLTGHRHEKVEAVLSRSNQGVARVDSGGYEPEGLENKPVAESQPSPGTLGVFSLILPLQAGDTVCVDLVMGQLAHSEEPLTIFSGALLYGDPELEHA","alphafold_very_low_content":"0.30118110236220474","creator":"mnecci","dataset":["Extracellular matrix proteins"],"date":"2016-09-17T10:02:48.000Z","disprot_id":"DP01063","features":{"pfam":[{"id":"PF00386","name":"C1q domain","start":872,"end":1007},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":814,"end":867},{"id":"PF07546","name":"EMI domain","start":57,"end":126}],"gene3D":[{"start":859,"end":1016,"id":"2.60.120.40","name":"2.60.120.40","_id":"685af523b4ac24d5329d8ac8"}]},"genes":[{"name":{"value":"EMILIN1","evidences":[],"_id":"685af523b4ac24d5329d8af4"},"synonyms":[{"value":"EMI","evidences":[],"_id":"685af523b4ac24d5329d8af5"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d8af3"}],"length":1016,"name":"EMILIN-1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":8,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI000013D0F3","uniref100":"UniRef100_Q9Y6C2","uniref50":"UniRef50_Q9Y6C2","uniref90":"UniRef90_Q9Y6C2","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2KA3","_id":"685af523b4ac24d5329d8ad0"},{"db":"PDB","id":"2OII","_id":"685af523b4ac24d5329d8ad1"}],"curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":948,"end":966,"interaction_partner":[],"reference_html":"The solution structure of EMILIN1 globular C1q domain reveals a disordered insertion necessary for interaction with the alpha4beta1 integrin. <i> Verdone G, Doliana R, Corazza A, Colebrooke SA, Spessotto P, Bot S, Bucciotti F, Capuano A, Silvestri A, Viglino P, Campbell ID, Colombatti A, Esposito G. </i> J Biol Chem, 2008","reference_id":"18463100","region_id":"DP01063r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Following the secondary structure numbering of homologous proteins (10), the latter unstructured stretch reads Tyr927–Gly945","_id":"685af523b4ac24d5329d8ad2"},{"type":"Results","text":"The flexible character of the unstructured segment Tyr927–Gly945, suggested by the sharpness of the corresponding NMR signals, was confirmed by 15N{1H} NOE measurements, which exhibited local enhancements ranging between -90 and -110%, as opposed to an average value of -15% observed for all the other residues but the N- and C-terminal ones (not shown).","_id":"685af523b4ac24d5329d8ad3"},{"type":"Results","text":"The region Tyr927–Gly945 was classified as flexible and disordered in every analysis performed, according to 15N{1H} NOE evidence.","_id":"685af523b4ac24d5329d8ad4"},{"type":"Curator statement","text":"The published residue boundaries needed to be shifted by +21 to confirm to the current UniProt sequence.","_id":"685af523b4ac24d5329d8ad5"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-05-17T15:02:50.846Z","_id":"685af523b4ac24d5329d8ad6"},"version":2,"_id":"685af523b4ac24d5329d8acf","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IMP","ec_id":"ECO:0001175","ec_name":"deletion mutation phenotypic evidence used in manual assertion","ec_ontology":"ECO","start":953,"end":966,"interaction_partner":[{"db":"UniProt","id":"P13612","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8ad8"},{"db":"UniProt","id":"P05556","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8ad9"}],"reference_html":"The solution structure of EMILIN1 globular C1q domain reveals a disordered insertion necessary for interaction with the alpha4beta1 integrin. <i> Verdone G, Doliana R, Corazza A, Colebrooke SA, Spessotto P, Bot S, Bucciotti F, Capuano A, Silvestri A, Viglino P, Campbell ID, Colombatti A, Esposito G. </i> J Biol Chem, 2008","reference_id":"18463100","region_id":"DP01063r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The different point-mutated proteins and the shortest deletion mutant del(Leu932–Gly945) were then assayed in standard cell adhesion assays. Jurkat cells that express high levels of the α4β1 integrin attached in a dose-response assay very efficiently to wild type and mutated EMILIN1 gC1q except del(Gly932–Gly945), E933A, L932A/E933A, and wild type EMILIN1 gC1q denatured in 8 m urea.","_id":"685af523b4ac24d5329d8ada"},{"type":"Curator statement","text":"The published residue boundaries needed to be shifted by +21 to confirm to the current UniProt sequence.","_id":"685af523b4ac24d5329d8adb"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-05-17T15:04:48.828Z","_id":"685af523b4ac24d5329d8adc"},"version":3,"_id":"685af523b4ac24d5329d8ad7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IMP","ec_id":"ECO:0000315","ec_name":"mutant phenotype evidence used in manual assertion","ec_ontology":"ECO","start":951,"end":956,"interaction_partner":[{"db":"UniProt","id":"P13612","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8ade"},{"db":"UniProt","id":"P05556","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8adf"}],"reference_html":"The solution structure of EMILIN1 globular C1q domain reveals a disordered insertion necessary for interaction with the alpha4beta1 integrin. <i> Verdone G, Doliana R, Corazza A, Colebrooke SA, Spessotto P, Bot S, Bucciotti F, Capuano A, Silvestri A, Viglino P, Campbell ID, Colombatti A, Esposito G. </i> J Biol Chem, 2008","reference_id":"18463100","region_id":"DP01063r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The different point-mutated proteins and the shortest deletion mutant del(Leu932–Gly945) were then assayed in standard cell adhesion assays. Jurkat cells that express high levels of the α4β1 integrin attached in a dose-response assay very efficiently to wild type and mutated EMILIN1 gC1q except del(Gly932–Gly945), E933A, L932A/E933A, and wild type EMILIN1 gC1q denatured in 8 m urea.","_id":"685af523b4ac24d5329d8ae0"},{"type":"Curator statement","text":"The published residue boundaries needed to be shifted by +21 to confirm to the current UniProt sequence.","_id":"685af523b4ac24d5329d8ae1"},{"type":"Results","text":"Thus, amino acid substitution mutants revealed that the conserved residue Glu933 is essential for binding of EMILIN1 gC1q to integrin α4β1, whereas single mutations of several residues close to Glu933, do not affect the interaction between the two molecules.","_id":"685af523b4ac24d5329d8ae2"},{"type":"Results","text":"Because static adhesion and haptotaxis experiments showed that cells are highly dependent on Glu933 for full functionality, we next mimicked cell flow in blood vessels to determine whether firm arrest of Jurkat T cells mediated by α4β1 was also related to residue Glu933. Under flow conditions at a shear rate of 20 s-1 almost no Jurkat cells had arrested on E933A-gC1q-coated surfaces up to 4 min of flow. In marked contrast up to 160 cells/mm2 were firmly arrested on coated wt gC1q-coated surfaces.","_id":"685af523b4ac24d5329d8ae3"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-05-17T15:04:55.156Z","_id":"685af523b4ac24d5329d8ae4"},"version":3,"_id":"685af523b4ac24d5329d8add","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IMP","ec_id":"ECO:0000315","ec_name":"mutant phenotype evidence used in manual assertion","ec_ontology":"ECO","start":951,"end":956,"interaction_partner":[],"reference_html":"The solution structure of EMILIN1 globular C1q domain reveals a disordered insertion necessary for interaction with the alpha4beta1 integrin. <i> Verdone G, Doliana R, Corazza A, Colebrooke SA, Spessotto P, Bot S, Bucciotti F, Capuano A, Silvestri A, Viglino P, Campbell ID, Colombatti A, Esposito G. </i> J Biol Chem, 2008","reference_id":"18463100","region_id":"DP01063r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The different point-mutated proteins and the shortest deletion mutant del(Leu932–Gly945) were then assayed in standard cell adhesion assays. Jurkat cells that express high levels of the α4β1 integrin attached in a dose-response assay very efficiently to wild type and mutated EMILIN1 gC1q except del(Gly932–Gly945), E933A, L932A/E933A, and wild type EMILIN1 gC1q denatured in 8 m urea.","_id":"685af523b4ac24d5329d8ae6"},{"type":"Results","text":"Thus, amino acid substitution mutants revealed that the conserved residue Glu933 is essential for binding of EMILIN1 gC1q to integrin α4β1, whereas single mutations of several residues close to Glu933, do not affect the interaction between the two molecules.","_id":"685af523b4ac24d5329d8ae7"},{"type":"Results","text":"Because static adhesion and haptotaxis experiments showed that cells are highly dependent on Glu933 for full functionality, we next mimicked cell flow in blood vessels to determine whether firm arrest of Jurkat T cells mediated by α4β1 was also related to residue Glu933. Under flow conditions at a shear rate of 20 s-1 almost no Jurkat cells had arrested on E933A-gC1q-coated surfaces up to 4 min of flow. In marked contrast up to 160 cells/mm2 were firmly arrested on coated wt gC1q-coated surfaces.","_id":"685af523b4ac24d5329d8ae8"},{"type":"Curator statement","text":"The published residue boundaries needed to be shifted by +21 to confirm to the current UniProt sequence.","_id":"685af523b4ac24d5329d8ae9"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-05-17T15:04:57.405Z","_id":"685af523b4ac24d5329d8aea"},"version":3,"_id":"685af523b4ac24d5329d8ae5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2KA3","_id":"685af523b4ac24d5329d8aec"}],"curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":948,"end":966,"interaction_partner":[],"reference_html":"NMR-based homology model for the solution structure of the C-terminal globular domain of EMILIN1. <i> Verdone G, Corazza A, Colebrooke SA, Cicero D, Eliseo T, Boyd J, Doliana R, Fogolari F, Viglino P, Colombatti A, Campbell ID, Esposito G. </i> J Biomol NMR, 2009","reference_id":"19023665","region_id":"DP01063r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"One difficulty encountered with the resonance assignment of gC1q arose from the identification of residues belonging to the segment Tyr927-Gly945, which contains four proline residues. Detection and recognition of resonances for this proved difficult due to a relatively poor signal-to-noise ratio of the nitrogen correlation spectra and was only accomplished when the majority of other peaks had already been classified. Line broadening due to slow conformational averaging of this region of EMILIN1 gC1q could be a reason for the lack of detectable amide resonances. Noticeably, this segment has very low sequence homology with other proteins of the family because it includes part of a 12-residue insertion (from Ser940 to Ser951) that is unique to EMILIN1 and EMILIN2 gC1q domains. Two amino acids in the segment 927–945, i.e. Asn934 and Ser940, still have unassigned HN groups and nine amino acids have typical 1H and 15N random coil chemical shifts","_id":"685af523b4ac24d5329d8aed"},{"type":"Curator statement","text":"The published residue boundaries needed to be shifted by +21 to confirm to the current UniProt sequence.","_id":"685af523b4ac24d5329d8aee"},{"type":"Results","text":"According to our data the secondary structure of the EMILIN1 gC1q domain is composed of nine β-strands and one unstructured region including residues 927–945.","_id":"685af523b4ac24d5329d8aef"},{"type":"Results","text":"15N{1H} NOE measurements were run at 11.4 T and 310 K, using two different relaxation/saturation delays, 3 and 5 s. As seen from the histogram in Fig. 4, the results indicate that, besides the N-terminal and C-terminal regions, the highest mobility is observed at segment 927–945.","_id":"685af523b4ac24d5329d8af0"},{"type":"Results","text":"Some residues belong to portions of the polypeptide chain with high mobility, according to 15 N{1H} NOE data (Fig. 4), i.e. the C-terminal segment including residues Glu991-Ala995, Val949, Ala958 and the unstructured region previously identified in fragment Tyr927-Gly945. This supports the hypothesis of the existence of a flexible loop (927–945) and a five-residue C-terminal segment that are separate from the main protein fold. It is worth noting that the segment Tyr927-Gly945 and the C-terminal pentapeptide showed typical random-coil chemical shifts and no TALOS prediction output nor slow-exchanging amide protons were available or detected for those amino acids.","_id":"685af523b4ac24d5329d8af1"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-05-17T15:02:52.631Z","_id":"685af523b4ac24d5329d8af2"},"version":2,"_id":"685af523b4ac24d5329d8aeb","reference_source":"pmid"}],"__v":0,"disorder_content":0.018700787401574805,"disprot_consensus":{"full":[{"start":948,"end":966,"type":"D"}],"Structural state":[{"start":948,"end":966,"type":"D"}],"Molecular function":[{"start":951,"end":966,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":312,"end":490},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":527,"end":635}],"gene3D":[{"start":505,"end":679,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":252,"end":504,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_Q61496","sequence":"MGDEDWEAEINPHMSSYVPIFEKDRYSGENGDNFNRTPASSSEMDDGPSRRDHFMKSGFASGRNFGNRDAGECNKRDNTSTMGGFGVGKSFGNRGFSNSRFEDGDSSGFWRESSNDCEDNPTRNRGFSKRGGYRDGNNSEASGPYRRGGRGSFRGCRGGFGLGSPNNDLDPDECMQRTGGLFGSRRPVLSGTGNGDTSQSRSGSGSERGGYKGLNEEVITGSGKNSWKSEAEGGESSDTQGPKVTYIPPPPPEDEDSIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITASRFKELQEPECIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLMFSATFPEEIQRLAAEFLKSNYLFVAVGQVGGACRDVQQTVLQVGQFSKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDLESDNHLAQPLVKVLTDAQQDVPAWLEEIAFSTYIPGFSGSTRGNVFASVDTRKGKSTLNTAGFSSSQAPNPVDDESWD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q61496","disprot_id":"DP01065","ncbi_taxon_id":9606,"regions_counter":5,"creator":"ndavey","regions":[{"start":1,"end":236,"reference_id":"25747659","reference_source":"pmid","reference_html":"Phase transition of a disordered nuage protein generates environmentally responsive membraneless organelles. <i> Nott TJ, Petsalaki E, Farber P, Jervis D, Fussner E, Plochowietz A, Craggs TD, Bazett-Jones DP, Pawson T, Forman-Kay JD, Baldwin AJ. </i> Mol Cell, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01065r004","statement":[{"text":"The narrow range of amide proton chemical shifts observed in a 1H/15N HSQC spectra of the two proteins (Figure S5A) confirmed that they are intrinsically disordered.","type":"Results"},{"text":"Here, we demonstrate that human Ddx4 and its isolated disordered N terminus spontaneously self-associate both in cells and in vitro into structures that are indistinguishable from the cellular Ddx4-organelles.","type":"Introduction"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-09-25T14:49:53.017Z"}},{"start":1,"end":236,"reference_id":"25747659","reference_source":"pmid","reference_html":"Phase transition of a disordered nuage protein generates environmentally responsive membraneless organelles. <i> Nott TJ, Petsalaki E, Farber P, Jervis D, Fussner E, Plochowietz A, Craggs TD, Bazett-Jones DP, Pawson T, Forman-Kay JD, Baldwin AJ. </i> Mol Cell, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007731","ec_ontology":"ECO","ec_name":"spectrometry evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01065r005","statement":[{"text":"Here, we demonstrate that human Ddx4 and its isolated disordered N terminus spontaneously self-associate both in cells and in vitro into structures that are indistinguishable from the cellular Ddx4-organelles.","type":"Introduction"},{"text":"The organelles are clearly partitioned from surrounding nuclear structures including chromatin domains and other native nuclear bodies (Figures 1C and S2B), a finding consistent with the liquid droplet-like nature suggested by FRAP measurements (Figure 2A).","type":"Results"},{"text":"These data reveal that the disordered termini of Ddx4 mediate self-organization into macroscopic fluxional spherical structures in live cells that can be classified as organelles, which can respond rapidly to changes in the cellular environment.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-17T16:37:12.429Z"}}],"released":"2016_10","uniref100":"UniRef100_Q9NQI0","date":"2016-09-17T19:09:50.000Z","acc":"Q9NQI0","name":"Probable ATP-dependent RNA helicase DDX4","length":724,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI0000169D64","genes":[{"name":{"value":"DDX4"},"synonyms":[{"value":"VASA"}]}],"alphafold_very_low_content":0.3825966850828729,"disorder_content":0.3259668508287293,"disprot_consensus":{"full":[{"start":1,"end":236,"type":"D"}],"Structural state":[{"start":1,"end":236,"type":"D"}],"Molecular function":[{"start":1,"end":236,"type":"F"}]}},{"acc":"Q9NQI0-2","sequence":"MGDEDWEAEINPHMSSYVPIFEKDRYSGENGDNFNRTPASSSEMDDGPSRRDHFMKSGFASGRNFGNRDAGECNKRDNTSTMGGFGVGKSFGNRGFSNSRFEDGDSSGFWRESSNDCEDNPTRNRGFSKRGDNDLDPDECMQRTGGLFGSRRPVLSGTGNGDTSQSRSGSGSERGGYKGLNEEVITGSGKNSWKSEAEGGESSDTQGPKVTYIPPPPPEDEDSIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITASRFKELQEPECIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLMFSATFPEEIQRLAAEFLKSNYLFVAVGQVGGACRDVQQTVLQVGQFSKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDLESDNHLAQPLVKVLTDAQQDVPAWLEEIAFSTYIPGFSGSTRGNVFASVDTRKGKSTLNTAGFSSSQAPNPVDDESWD","creator":"ndavey","dataset":[],"date":"2016-09-17T19:17:25.000Z","disprot_id":"DP01066","features":{"pfam":[]},"genes":[{"name":{"value":"DDX4","evidences":[],"_id":"685af523b4ac24d5329d8afe"},"synonyms":[{"value":"VASA","evidences":[],"_id":"685af523b4ac24d5329d8aff"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d8afd"}],"length":690,"name":"Isoform 2 of Probable ATP-dependent RNA helicase DDX4","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":3,"released":"2016_10","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI000020C786","uniref100":"","uniref50":"","uniref90":"","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006198","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":204,"interaction_partner":[],"reference_html":"Phase transition of a disordered nuage protein generates environmentally responsive membraneless organelles. <i> Nott TJ, Petsalaki E, Farber P, Jervis D, Fussner E, Plochowietz A, Craggs TD, Bazett-Jones DP, Pawson T, Forman-Kay JD, Baldwin AJ. </i> Mol Cell, 2015","reference_id":"25747659","region_id":"DP01066r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The narrow range of amide proton chemical shifts observed in a 1H/15N HSQC spectra of the two proteins (Figure S5A) confirmed that they are intrinsically disordered.","_id":"685af523b4ac24d5329d8af7"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-23T19:48:40.257Z","_id":"685af523b4ac24d5329d8af8"},"version":3,"_id":"685af523b4ac24d5329d8af6","reference_source":"pmid"}],"__v":0,"disorder_content":0.2956521739130435,"disprot_consensus":{"full":[{"start":1,"end":204,"type":"D"}],"Structural state":[{"start":1,"end":204,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00985","name":"Merozoite Surface Antigen 2 (MSA-2) family","start":105,"end":264}]},"uniref50":"UniRef50_P19599","sequence":"MKVIKTLSIINFFIFVTFNIKNESKYSNTFINNAYNMSIRRSMANEGSNTNSVGANAPNADTIASGSQRSTNSASTSTTNNGESQTTTPTAADTIASGSQRSTNSASTSTTNNGESQTTTPTAADTPTATESISPSPPITTTESSKFWQCTNKTDGKGEESEKQNELNESTEEGPKAPQEPQTAENENPAAPENKGTGQHGHMHGSRNNHPQNTSDSQKECTDGNKENCGAATSLLSNSSNIASINKFVVLISATLVLSFAIFI","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"uniref90":"UniRef90_P19599","disprot_id":"DP01067","ncbi_taxon_id":5837,"regions_counter":1,"creator":"ldobson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":238,"region_id":"DP01067r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Solution conformation, backbone dynamics and lipid interactions of the intrinsically unstructured malaria surface protein MSP2. <i> Zhang X, Perugini MA, Yao S, Adda CG, Murphy VJ, Low A, Anders RF, Norton RS. </i> J Mol Biol, 2008","term_id":"IDPO:0000004","curator_id":"ndavey","start":21,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"pre-molten globule","reference_id":"18440022","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P19599","date":"2016-09-18T00:01:05.000Z","acc":"P19599","name":"Merozoite surface antigen 2","length":264,"organism":"Plasmodium falciparum (isolate FC27 / Papua New Guinea)","dataset":[],"UniParc":"UPI000000071B","genes":[{"name":{"value":"MSA2"}}],"alphafold_very_low_content":0.7045454545454546,"disorder_content":0.8257575757575758,"disprot_consensus":{"full":[{"start":21,"end":238,"type":"D"}],"Structural state":[{"start":21,"end":238,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01429","name":"Methyl-CpG binding domain","start":148,"end":214},{"id":"PF14048","name":"C-terminal domain of methyl-CpG binding protein 2 and 3","start":298,"end":387},{"id":"PF16564","name":"p55-binding region of Methyl-CpG-binding domain proteins MBD","start":223,"end":292}],"gene3D":[{"start":144,"end":214,"id":"3.30.890.10","name":"Methyl-cpg-binding Protein 2; Chain A"}]},"uniref50":"UniRef50_Q9UBB5","sequence":"MRAHPGGGRCCPEQEEGESAAGGSGAGGDSAIEQGGQGSALAPSPVSGVRREGARGGGRGRGRWKQAGRGGGVCGRGRGRGRGRGRGRGRGRGRGRPPSGGSGLGGDGGGCGGGGSGGGGAPRREPVPFPSGSAGPGPRGPRATESGKRMDCPALPPGWKKEEVIRKSGLSAGKSDVYYFSPSGKKFRSKPQLARYLGNTVDLSSFDFRTGKMMPSKLQKNKQRLRNDPLNQNKGKPDLNTTLPIRQTASIFKQPVTKVTNHPSNKVKSDPQRMNEQPRQLFWEKRLQGLSASDVTEQIIKTMELPKGLQGVGPGSNDETLLSAVASALHTSSAPITGQVSAAVEKNPAVWLNTSQPLCKAFIVTDEDIRKQEERVQQVRKKLEEALMADILSRAADTEEMDIEMDSGDEA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UBB5","disprot_id":"DP01068","ncbi_taxon_id":9606,"regions_counter":3,"creator":"aghosh","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":356,"region_id":"DP01068r001","released":"2022_03","ec_id":"ECO:0006198","reference_html":"An intrinsically disordered region of methyl-CpG binding domain protein 2 (MBD2) recruits the histone deacetylase core of the NuRD complex. <i> Desai MA, Webb HD, Sinanan LM, Scarsdale JN, Walavalkar NM, Ginder GD, Williams DC. </i> Nucleic Acids Res, 2015","term_id":"IDPO:0000002","curator_id":"ndavey","start":238,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"25753662","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":356,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","reference_html":"An intrinsically disordered region of methyl-CpG binding domain protein 2 (MBD2) recruits the histone deacetylase core of the NuRD complex. <i> Desai MA, Webb HD, Sinanan LM, Scarsdale JN, Walavalkar NM, Ginder GD, Williams DC. </i> Nucleic Acids Res, 2015","term_id":"GO:0060090","curator_id":"ndavey","start":238,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"25753662","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006198","region_id":"DP01068r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":356,"term_name":"protein binding","released":"2022_03","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","reference_html":"An intrinsically disordered region of methyl-CpG binding domain protein 2 (MBD2) recruits the histone deacetylase core of the NuRD complex. <i> Desai MA, Webb HD, Sinanan LM, Scarsdale JN, Walavalkar NM, Ginder GD, Williams DC. </i> Nucleic Acids Res, 2015","term_id":"GO:0005515","curator_id":"ndavey","start":238,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"25753662","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006198","region_id":"DP01068r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q9UBB5","date":"2016-09-18T00:20:01.000Z","acc":"Q9UBB5","name":"Methyl-CpG-binding domain protein 2","length":411,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000003166A","genes":[{"name":{"value":"MBD2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6917","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6917"}}]}}],"alphafold_very_low_content":0.3771289537712895,"disorder_content":0.2895377128953771,"disprot_consensus":{"full":[{"start":238,"end":356,"type":"D"}],"Structural state":[{"start":238,"end":356,"type":"D"}],"Molecular function":[{"start":238,"end":356,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_K7YJH2","sequence":"MKRLLVLSILLTLGFSFAGTASADENANRPVNPGEDPNEAFRSTPFEATTSALGDCRECIAYRTGATTGKGSRRHDDTVSREIKGSSATPGGSEKAGTGRQ","taxonomy":["Bacteria","Proteobacteria","Oligoflexia","Bdellovibrionales","Bdellovibrionaceae","Bdellovibrio"],"uniref90":"UniRef90_K7YJH2","disprot_id":"DP01069","ncbi_taxon_id":264462,"regions_counter":6,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":101,"region_id":"DP01069r001","released":"2022_03","ec_id":"ECO:0006198","reference_html":"The lifestyle switch protein Bd0108 of Bdellovibrio bacteriovorus is an intrinsically disordered protein. <i> Prehna G, Ramirez BE, Lovering AL. </i> PLoS One, 2014","term_id":"IDPO:0000002","curator_id":"ndavey","start":1,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"25514156","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":101,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","reference_html":"The lifestyle switch protein Bd0108 of Bdellovibrio bacteriovorus is an intrinsically disordered protein. <i> Prehna G, Ramirez BE, Lovering AL. </i> PLoS One, 2014","term_id":"GO:0060090","curator_id":"ndavey","start":1,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"25514156","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006198","region_id":"DP01069r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":101,"term_name":"protein binding","released":"2022_03","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","reference_html":"The lifestyle switch protein Bd0108 of Bdellovibrio bacteriovorus is an intrinsically disordered protein. <i> Prehna G, Ramirez BE, Lovering AL. </i> PLoS One, 2014","term_id":"GO:0005515","curator_id":"ndavey","start":1,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"25514156","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006198","region_id":"DP01069r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":101,"region_id":"DP01069r004","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The lifestyle switch protein Bd0108 of Bdellovibrio bacteriovorus is an intrinsically disordered protein. <i> Prehna G, Ramirez BE, Lovering AL. </i> PLoS One, 2014","term_id":"IDPO:0000002","curator_id":"ndavey","start":1,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"25514156","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":101,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"The lifestyle switch protein Bd0108 of Bdellovibrio bacteriovorus is an intrinsically disordered protein. <i> Prehna G, Ramirez BE, Lovering AL. </i> PLoS One, 2014","term_id":"GO:0060090","curator_id":"ndavey","start":1,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"25514156","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01069r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":101,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"The lifestyle switch protein Bd0108 of Bdellovibrio bacteriovorus is an intrinsically disordered protein. <i> Prehna G, Ramirez BE, Lovering AL. </i> PLoS One, 2014","term_id":"GO:0005515","curator_id":"ndavey","start":1,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"25514156","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01069r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q9ETD9","date":"2016-09-18T06:38:11.000Z","acc":"Q6MRH6","name":"Hit locus orf4","length":101,"organism":"Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100)","dataset":[],"UniParc":"UPI00000BB893","genes":[{"olnNames":[{"value":"Bd0108","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAE77782.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAE77782.1"}}]}]}],"alphafold_very_low_content":0.33663366336633666,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":101,"type":"D"}],"Structural state":[{"start":1,"end":101,"type":"D"}],"Molecular function":[{"start":1,"end":101,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03366","name":"YEATS family","start":28,"end":107},{"id":"PF17793","name":"ANC1 homology domain (AHD)","start":503,"end":563}],"gene3D":[{"start":1,"end":138,"id":"2.60.40.1970","name":"YEATS domain"},{"start":472,"end":563,"id":"1.20.1270.290","name":"1.20.1270.290"}]},"uniref50":"UniRef50_P42568","sequence":"MASSCAVQVKLELGHRAQVRKKPTVEGFTHDWMVFVRGPEHSNIQHFVEKVVFHLHESFPRPKRVCKDPPYKVEESGYAGFILPIEVYFKNKEEPRKVRFDYDLFLHLEGHPPVNHLRCEKLTFNNPTEDFRRKLLKAGGDPNRSIHTSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSTSFSKPHKLMKEHKEKPSKDSREHKSAFKEPSRDHNKSSKESSKKPKENKPLKEEKIVPKMAFKEPKPMSKEPKPDSNLLTITSGQDKKAPSKRPPISDSEELSAKKRKKSSSEALFKSFSSAPPLILTCSADKKQIKDKSHVKMGKVKIESETSEKKKSTLPPFDDIVDPNDSDVEENISSKSDSEQPSPASSSSSSSSSFTPSQTRQQGPLRSIMKDLHSDDNEEESDEVEDNDNDSEMERPVNRGGSRSRRVSLSDGSDSESSSASSPLHHEPPPPLLKTNNNQILEVKSPIKQSKSDKQIKNGECDKAYLDELVELHRRLMTLRERHILQQIVNLIEETGHFHITNTTFDFDLCSLDKTTVRKLQSYLETSGTS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P42568","disprot_id":"DP01070","ncbi_taxon_id":9606,"regions_counter":12,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":568,"region_id":"DP01070r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Leukemia fusion target AF9 is an intrinsically disordered transcriptional regulator that recruits multiple partners via coupled folding and binding. <i> Leach BI, Kuntimaddi A, Schmidt CR, Cierpicki T, Johnson SA, Bushweller JH. </i> Structure, 2013","term_id":"IDPO:0000002","curator_id":"fquaglia","start":490,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23260655","statement":[{"text":"We show that the ANC1 homology domain (AHD) of AF9, one of the most common MLL translocation partners, is intrinsically disordered and recruits multiple transcription factors through coupled folding and binding.","type":"Abstract"},{"text":"15N-1H HSQC spectra showed extreme broadening, with only a small number of peaks with narrow 1H chemical shift dispersion and an insufficient number of peaks for the amino acids in the domain (Figure 1a). Since the interacting regions between AF4 and AF9 had been finely mapped (Srinivasan et al., 2004), we titrated a peptide derived from the AF9 interaction motif of AF4 (residues 761 to 774) into the AF9 AHD. This resulted in dramatically improved chemical shift dispersion and an increased number of observable peaks in the HSQC spectrum (Figure 1b).","type":"Results"},{"text":"These data show that the AF9 AHD is intrinsically disordered, and recruits AF4 through mutual synergistic folding (Demarest et al., 2002).","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:26:19.567Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":568,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Leukemia fusion target AF9 is an intrinsically disordered transcriptional regulator that recruits multiple partners via coupled folding and binding. <i> Leach BI, Kuntimaddi A, Schmidt CR, Cierpicki T, Johnson SA, Bushweller JH. </i> Structure, 2013","term_id":"GO:0060090","curator_id":"fquaglia","start":490,"term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"23260655","version":4,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01070r002","statement":[{"text":"Leukemia fusion target AF9 is an intrinsically disordered transcriptional regulator that recruits multiple partners via coupled folding and binding.","type":"Abstract"},{"text":"We show that the ANC1 homology domain (AHD) of AF9, one of the most common MLL translocation partners, is intrinsically disordered and recruits multiple transcription factors through coupled folding and binding.","type":"Abstract"},{"text":"We propose that AF9 functions as a signaling hub that regulates transcription through dynamic recruitment of cofactors in normal hematopoiesis and in acute leukemia.","type":"Abstract"},{"text":"In addition to AF4 family members, the AF9 AHD has previously been shown to interact with hPC3, BCoR and Dot1L. Having established that AF4 and AF9 interact through mutual synergistic folding, we hypothesized that other binding partners may interact with AF9 in a similar manner.","type":"Results"},{"text":"In order to investigate the other interactions with the AF9 AHD, we cloned DNA coding for the sequences derived from hPC3, Dot1L and BCoR into our coexpression vector and found that all of these co-purified with AF9. Using triple resonance based backbone assignments and 1H 15N heteronuclear NOE experiments, we were able to map the residues of these proteins involved in the interaction with the AF9 AHD. Immediately apparent is the similarity in the chemical shifts of the AF9 NH moieties observed in the HSQC spectra of these complexes. As chemical shifts are highly sensitive to structure, this similarity indicates that AF9 retains a similar fold in all of the complexes (Figure 3a-d).","type":"Results"},{"text":"Together, these data strongly suggest that AF9 retains a similar fold in each of the complexes, and that each of its binding partners share a common binding site on AF9. This is consistent with previous data showing that AF9 binding partners interact with the AF9 AHD in a mutually exclusive manner (Srinivasan et al., 2003; Yokoyama et al., 2010). It was previously proposed that where IDPs compete for binding to a common site, coupled folding and binding may allow one IDP to displace another without its prior dissociation, facilitating rapid exchange between high affinity partners (De Guzman et al., 2004). The differing functions of the AF9 binding partners suggest that the function of the AHD may be to regulate gene expression through alternate binding to its partners, and intrinsic disorder may facilitate their exchange as a function of local concentration and affinity.","type":"Results"},{"text":"The AHD recruits AF4, BCoR, Dot1L and hPC3 by coupled folding and binding","type":"Article"},{"text":"AF9 binding partners compete for binding to a common site","type":"Article"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:26:28.795Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":568,"term_name":"disorder to order","released":"2022_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Leukemia fusion target AF9 is an intrinsically disordered transcriptional regulator that recruits multiple partners via coupled folding and binding. <i> Leach BI, Kuntimaddi A, Schmidt CR, Cierpicki T, Johnson SA, Bushweller JH. </i> Structure, 2013","term_id":"IDPO:0000011","curator_id":"vnugnes","start":490,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"23260655","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-14T21:54:19.050Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01070r003","statement":[{"text":"15N-1H HSQC spectra showed extreme broadening, with only a small number of peaks with narrow 1H chemical shift dispersion and an insufficient number of peaks for the amino acids in the domain (Figure 1a). Since the interacting regions between AF4 and AF9 had been finely mapped (Srinivasan et al., 2004), we titrated a peptide derived from the AF9 interaction motif of AF4 (residues 761 to 774) into the AF9 AHD. This resulted in dramatically improved chemical shift dispersion and an increased number of observable peaks in the HSQC spectrum (Figure 1b).","type":"Results"},{"text":"These data show that the AF9 AHD is intrinsically disordered, and recruits AF4 through mutual synergistic folding (Demarest et al., 2002).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P51825"}]},{"region_id":"DP01070r004","ec_ontology":"ECO","end":568,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":490,"version":5,"statement":[{"text":"Leukemia fusion target AF9 is an intrinsically disordered transcriptional regulator that recruits multiple partners via coupled folding and binding.","type":"Abstract"},{"text":"We show that the ANC1 homology domain (AHD) of AF9, one of the most common MLL translocation partners, is intrinsically disordered and recruits multiple transcription factors through coupled folding and binding.","type":"Abstract"},{"text":"We propose that AF9 functions as a signaling hub that regulates transcription through dynamic recruitment of cofactors in normal hematopoiesis and in acute leukemia.","type":"Abstract"},{"text":"In addition to AF4 family members, the AF9 AHD has previously been shown to interact with hPC3, BCoR and Dot1L. Having established that AF4 and AF9 interact through mutual synergistic folding, we hypothesized that other binding partners may interact with AF9 in a similar manner.","type":"Results"},{"text":"In order to investigate the other interactions with the AF9 AHD, we cloned DNA coding for the sequences derived from hPC3, Dot1L and BCoR into our coexpression vector and found that all of these co-purified with AF9. Using triple resonance based backbone assignments and 1H 15N heteronuclear NOE experiments, we were able to map the residues of these proteins involved in the interaction with the AF9 AHD. Immediately apparent is the similarity in the chemical shifts of the AF9 NH moieties observed in the HSQC spectra of these complexes. As chemical shifts are highly sensitive to structure, this similarity indicates that AF9 retains a similar fold in all of the complexes (Figure 3a-d).","type":"Results"},{"text":"Together, these data strongly suggest that AF9 retains a similar fold in each of the complexes, and that each of its binding partners share a common binding site on AF9. This is consistent with previous data showing that AF9 binding partners interact with the AF9 AHD in a mutually exclusive manner (Srinivasan et al., 2003; Yokoyama et al., 2010). It was previously proposed that where IDPs compete for binding to a common site, coupled folding and binding may allow one IDP to displace another without its prior dissociation, facilitating rapid exchange between high affinity partners (De Guzman et al., 2004). The differing functions of the AF9 binding partners suggest that the function of the AHD may be to regulate gene expression through alternate binding to its partners, and intrinsic disorder may facilitate their exchange as a function of local concentration and affinity.","type":"Results"},{"text":"The AHD recruits AF4, BCoR, Dot1L and hPC3 by coupled folding and binding","type":"Article"},{"text":"AF9 binding partners compete for binding to a common site","type":"Article"}],"term_name":"protein binding","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"23260655","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"fquaglia","reference_html":"Leukemia fusion target AF9 is an intrinsically disordered transcriptional regulator that recruits multiple partners via coupled folding and binding. <i> Leach BI, Kuntimaddi A, Schmidt CR, Cierpicki T, Johnson SA, Bushweller JH. </i> Structure, 2013","term_id":"GO:0005515","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:26:25.698Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":568,"region_id":"DP01070r008","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Leukemia fusion target AF9 is an intrinsically disordered transcriptional regulator that recruits multiple partners via coupled folding and binding. <i> Leach BI, Kuntimaddi A, Schmidt CR, Cierpicki T, Johnson SA, Bushweller JH. </i> Structure, 2013","term_id":"IDPO:0000002","curator_id":"fquaglia","start":490,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23260655","statement":[{"text":"We show that the ANC1 homology domain (AHD) of AF9, one of the most common MLL translocation partners, is intrinsically disordered and recruits multiple transcription factors through coupled folding and binding.","type":"Abstract"},{"text":"In order to understand the structural changes induced by peptide binding, we conducted circular dichroism (CD) experiments on the AF9 AHD alone and in complex with the AF4 peptide. Surprisingly, these showed that in isolation the AHD is almost entirely random coil with only a small amount of beta structure predicted using K2D (Andrade et al., 1993)(Figure 1c). Upon addition of the AF4 peptide, the domain undergoes a structural rearrangement to form a mixed alpha-beta structure consistent with the dramatic change in the HSQC spectrum (Figure 1b).","type":"Results"},{"text":"These data show that the AF9 AHD is intrinsically disordered, and recruits AF4 through mutual synergistic folding (Demarest et al., 2002).","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:26:21.295Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":568,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Leukemia fusion target AF9 is an intrinsically disordered transcriptional regulator that recruits multiple partners via coupled folding and binding. <i> Leach BI, Kuntimaddi A, Schmidt CR, Cierpicki T, Johnson SA, Bushweller JH. </i> Structure, 2013","term_id":"GO:0060090","curator_id":"fquaglia","start":490,"term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"23260655","version":4,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01070r009","statement":[{"text":"In order to understand the structural changes induced by peptide binding, we conducted circular dichroism (CD) experiments on the AF9 AHD alone and in complex with the AF4 peptide. Surprisingly, these showed that in isolation the AHD is almost entirely random coil with only a small amount of beta structure predicted using K2D (Andrade et al., 1993)(Figure 1c). Upon addition of the AF4 peptide, the domain undergoes a structural rearrangement to form a mixed alpha-beta structure consistent with the dramatic change in the HSQC spectrum (Figure 1b).\" Results \"These data show that the AF9 AHD is intrinsically disordered, and recruits AF4 through mutual synergistic folding (Demarest et al., 2002).","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:26:30.547Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01070r010","ec_ontology":"ECO","end":568,"ec_name":"far-UV circular dichroism evidence used in manual assertion","start":490,"version":5,"statement":[{"text":"In order to understand the structural changes induced by peptide binding, we conducted circular dichroism (CD) experiments on the AF9 AHD alone and in complex with the AF4 peptide. Surprisingly, these showed that in isolation the AHD is almost entirely random coil with only a small amount of beta structure predicted using K2D (Andrade et al., 1993)(Figure 1c). Upon addition of the AF4 peptide, the domain undergoes a structural rearrangement to form a mixed alpha-beta structure consistent with the dramatic change in the HSQC spectrum (Figure 1b).\" Results \"These data show that the AF9 AHD is intrinsically disordered, and recruits AF4 through mutual synergistic folding (Demarest et al., 2002).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P51825","partner_end":null}],"term_name":"protein binding","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"23260655","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006204","curator_id":"fquaglia","reference_html":"Leukemia fusion target AF9 is an intrinsically disordered transcriptional regulator that recruits multiple partners via coupled folding and binding. <i> Leach BI, Kuntimaddi A, Schmidt CR, Cierpicki T, Johnson SA, Bushweller JH. </i> Structure, 2013","term_id":"GO:0005515","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:26:27.091Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":490,"end":568,"reference_id":"23260655","reference_source":"pmid","reference_html":"Leukemia fusion target AF9 is an intrinsically disordered transcriptional regulator that recruits multiple partners via coupled folding and binding. <i> Leach BI, Kuntimaddi A, Schmidt CR, Cierpicki T, Johnson SA, Bushweller JH. </i> Structure, 2013","date":"2022-06-14T21:54:02.963Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_06","version":3,"region_id":"DP01070r011","statement":[{"text":"In order to understand the structural changes induced by peptide binding, we conducted circular dichroism (CD) experiments on the AF9 AHD alone and in complex with the AF4 peptide. Surprisingly, these showed that in isolation the AHD is almost entirely random coil with only a small amount of beta structure predicted using K2D (Andrade et al., 1993)(Figure 1c). Upon addition of the AF4 peptide, the domain undergoes a structural rearrangement to form a mixed alpha-beta structure consistent with the dramatic change in the HSQC spectrum (Figure 1b).","type":"Results"},{"text":"These data show that the AF9 AHD is intrinsically disordered, and recruits AF4 through mutual synergistic folding (Demarest et al., 2002).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P51825 "}]},{"start":490,"end":568,"reference_id":"23260655","reference_source":"pmid","reference_html":"Leukemia fusion target AF9 is an intrinsically disordered transcriptional regulator that recruits multiple partners via coupled folding and binding. <i> Leach BI, Kuntimaddi A, Schmidt CR, Cierpicki T, Johnson SA, Bushweller JH. </i> Structure, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01070r012","statement":[{"text":"We expressed the C-terminal 79 amino acids of AF9, which includes the minimal portion of AF9 required for oncogenic activity of an MLL-AF9 fusion protein in colony forming assays (Prasad et al., 1995) and roughly corresponds to the minimal domain observed in a clinical case of leukemia with an MLL-AF9 translocation (Mitterbauer et al., 1999). During initial efforts to express and purify the AHD, we found that it had limited solubility and that the domain was prone to proteolytic degradation.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:26:18.566Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_P42568","date":"2016-09-18T07:13:30.000Z","acc":"P42568","name":"Protein AF-9","length":568,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI000012565A","genes":[{"name":{"value":"MLLT3","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16001262","url":"http://www.ncbi.nlm.nih.gov/pubmed/16001262","alternativeUrl":"https://europepmc.org/abstract/MED/16001262"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:7136","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:7136"}}]},"synonyms":[{"value":"AF9","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10861294","url":"http://www.ncbi.nlm.nih.gov/pubmed/10861294","alternativeUrl":"https://europepmc.org/abstract/MED/10861294"}}]},{"value":"YEATS3"}]}],"alphafold_very_low_content":0.5352112676056338,"disorder_content":0.13908450704225353,"disprot_consensus":{"full":[{"start":490,"end":568,"type":"T"}],"Structural state":[{"start":490,"end":568,"type":"D"}],"Molecular function":[{"start":490,"end":568,"type":"F"}],"Structural transition":[{"start":490,"end":568,"type":"T"}]}},{"features":{"pfam":[{"id":"PF07918","name":"CAP160 repeat","start":227,"end":252},{"id":"PF23399","name":"LTI65/LTI78 PGEED repeat","start":332,"end":361},{"id":"PF23403","name":"LTI65/LTI78 CAP160 N-terminal","start":21,"end":70}]},"uniref50":"UniRef50_O23764","sequence":"MESQLHRPTEQEVMEGQTADHGEKKSMLAKVKEKAKKLKGSINKKHGSSQDDDADNDEEINTSPAVHGAPGTSPPPPTQGGEYGGLSERDVNIPHPLASTQANLDKPADVTDASRELQVPPPVPETTPEVSDKGLTEDLGSNAGQGVKESDVDSLTQGLKGVNYGGDDSNPLSGQEHQTISDEPKSLPGQGNDLPQSHPSSEDEPKKFDANDQPQSMPQDTITGKLSSVPAVIIDRAAAAKNVVASKLGYGGSQAQESAADAGAAQQKKPLTETAAEYKNLVAEKLTPVYEKVAGAGSTVTSKVWGSGGTTAGEQTQGGEGVVDGGGAASNKGVFTKDYLSEKLKPGDEDKALSQAIMEKLQLSKKPAVEGGAGDETKASESSPGVVGTIKGAVGSLIGGGNKSSGAESAAAADEQTQALGE","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","lamiids","Lamiales","Linderniaceae","Craterostigma"],"uniref90":"UniRef90_O23764","disprot_id":"DP01071","ncbi_taxon_id":4153,"regions_counter":7,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":422,"region_id":"DP01071r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The lysine-rich motif of intrinsically disordered stress protein CDeT11-24 from Craterostigma plantagineum is responsible for phosphatidic acid binding and protection of enzymes from damaging effects caused by desiccation. <i> Petersen J, Eriksson SK, Harryson P, Pierog S, Colby T, Bartels D, Röhrig H. </i> J Exp Bot, 2012","term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22791833","statement":[{"text":"Recombinant protein overexpressed and purified from E. coli displayed an ellipticity minimum at 200nm and a value near zero at 220nm in physiological buffers, which supports an overall disordered structure.","type":"Results"},{"text":"CDeT11-24 protein extracted from plant cells showed a CD spectrum similar to the spectrum of recombinant protein (Fig. 1C), indicating that there was no significant difference between native and recombinant proteins with regard to this property.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":422,"term_name":"small molecule binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"The lysine-rich motif of intrinsically disordered stress protein CDeT11-24 from Craterostigma plantagineum is responsible for phosphatidic acid binding and protection of enzymes from damaging effects caused by desiccation. <i> Petersen J, Eriksson SK, Harryson P, Pierog S, Colby T, Bartels D, Röhrig H. </i> J Exp Bot, 2012","term_id":"GO:0036094","curator_id":"ndavey","start":1,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"22791833","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01071r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":422,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"The lysine-rich motif of intrinsically disordered stress protein CDeT11-24 from Craterostigma plantagineum is responsible for phosphatidic acid binding and protection of enzymes from damaging effects caused by desiccation. <i> Petersen J, Eriksson SK, Harryson P, Pierog S, Colby T, Bartels D, Röhrig H. </i> J Exp Bot, 2012","term_id":"GO:0005515","curator_id":"ndavey","start":1,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"22791833","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01071r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":422,"reference_id":"22791833","reference_source":"pmid","reference_html":"The lysine-rich motif of intrinsically disordered stress protein CDeT11-24 from Craterostigma plantagineum is responsible for phosphatidic acid binding and protection of enzymes from damaging effects caused by desiccation. <i> Petersen J, Eriksson SK, Harryson P, Pierog S, Colby T, Bartels D, Röhrig H. </i> J Exp Bot, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006317","ec_ontology":"ECO","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01071r005","statement":[{"text":"The CDeT11-24 protein remained soluble in heat-treated protein extracts of dried C. plantagineum tissues (Fig. 1A).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":422,"reference_id":"22791833","reference_source":"pmid","reference_html":"The lysine-rich motif of intrinsically disordered stress protein CDeT11-24 from Craterostigma plantagineum is responsible for phosphatidic acid binding and protection of enzymes from damaging effects caused by desiccation. <i> Petersen J, Eriksson SK, Harryson P, Pierog S, Colby T, Bartels D, Röhrig H. </i> J Exp Bot, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0044183","term_name":"protein folding chaperone","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01071r006","statement":[{"text":"In the presence of recombinant CDeT11-24 proteins, CS activity remained at more than 80% for 6His-CDeT11-24 and at 70% for CDeT11-24, even after three cycles of dehydration and rehydration. The protective effect slightly exceeded the effect caused by the disaccharide trehalose, which was used as a reference (Crowe et al., 2001).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":422,"reference_id":"22791833","reference_source":"pmid","reference_html":"The lysine-rich motif of intrinsically disordered stress protein CDeT11-24 from Craterostigma plantagineum is responsible for phosphatidic acid binding and protection of enzymes from damaging effects caused by desiccation. <i> Petersen J, Eriksson SK, Harryson P, Pierog S, Colby T, Bartels D, Röhrig H. </i> J Exp Bot, 2012","date":"2022-03-09T08:15:54.776Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006077","ec_ontology":"ECO","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","released":"2022_03","version":4,"region_id":"DP01071r007","statement":[{"text":"Lipid-binding assays revealed that CDeT11-24 is able to interact with phosphatidic acid, although electrostatic repulsion was expected due to the overall negative net charge of the protein under the tested physiological conditions.","type":"Abstract"},{"text":"Analysis of the truncated CDeT11-24 protein identified this region to be responsible for both activities: enzyme protection and phosphatidic acid interaction.","type":"Abstract"},{"text":"However, CDeT11-24 bound to the phospholipid monoester PA. Weak binding was also observed with cardiolipin, which is a phospholipid containing two phosphodiester groups.","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"ChEBI","id":"89530","operator":"and","partner_start":null,"partner_end":null}]}],"released":"2016_10","uniref100":"UniRef100_O23764","date":"2016-09-18T09:51:25.000Z","acc":"O23764","name":"CDet11-24 protein","length":422,"organism":"Craterostigma plantagineum","dataset":[],"UniParc":"UPI000009CE8C","genes":[{"name":{"value":"CDet11-24","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAA05780.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA05780.1"}}]}}],"alphafold_very_low_content":0.6137440758293838,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":422,"type":"D"}],"Structural state":[{"start":1,"end":422,"type":"D"}],"Molecular function":[{"start":1,"end":422,"type":"F"}]}},{"features":{"pfam":[{"id":"PF07651","name":"ANTH domain","start":22,"end":283}],"gene3D":[{"start":147,"end":294,"id":"1.20.58.150","name":"ANTH domain"},{"start":1,"end":146,"id":"1.25.40.90","name":"1.25.40.90"}]},"uniref50":"UniRef50_Q05140","sequence":"MSGQTLTDRIAAAQYSVTGSAVARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFDFARVKKGADGVMRTMVPEKLLKSMPILQGQIDALLEFDVHPNELTNGVINAAFMLLFKDLIKLFACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSEFLKVAEQVGIDKGDIPDLTQAPSSLMETLEQHLNTLEGKKPGNNEGSGAPSPLSKSSPATTVTSPNSTPAKTIDTSPPVDIFATASAAAPVSSAKPSSDLLDLQPDFSGAAAGAAAPVVPPSGGATAWGDLLGEDSLAALSSVPCEAPISDPFAPEPSPPTTTTEPASASASTTTAVTAVTTEVDLFGDAFAASPGEAPAASEGATAPATPAPVAAALDACSGNDPFAPSEGSAEAAPELDLFAMKPPETSAPVVTPTASTAPPVPATAPSPAPTAVAATAATTTAAAAATTTATTSAAAATTAAAPPALDIFGDLFDSAPEVAAAPKPDAAPSIDLFGTDAFSSPPRGASPVPESSLTADLLSVDAFAAPSPASTASPAKAESSGVIDLFGDAFGSGASETQPAPQAVSSSSASADLLAGFGGSFMAPSTTPVTPAQNNLLQPSFEAAFGTTPSTSSSSSFDPSVFDGLGDLLMPTMAPSGQPAPVSMVPPSPAMAASKGLGSDLDSSLASLVGNLGISGTTSKKGDLQWNAGEKKLTGGANWQPKVTPATWSAGVPPQGTVPPTSSVPPGAGAPSVGQPGAGFGMPPSGTGMTMMSQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPATQSPKKPPAKDPLADLNIKDFL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q61548","disprot_id":"DP01073","ncbi_taxon_id":10090,"regions_counter":3,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":680,"region_id":"DP01073r001","released":"2022_03","ec_id":"ECO:0006198","reference_html":"Dynamic interactions between clathrin and locally structured elements in a disordered protein mediate clathrin lattice assembly. <i> Zhuo Y, Ilangovan U, Schirf V, Demeler B, Sousa R, Hinck AP, Lafer EM. </i> J Mol Biol, 2010","term_id":"IDPO:0000002","curator_id":"ndavey","start":623,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20875424","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":680,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","reference_html":"Dynamic interactions between clathrin and locally structured elements in a disordered protein mediate clathrin lattice assembly. <i> Zhuo Y, Ilangovan U, Schirf V, Demeler B, Sousa R, Hinck AP, Lafer EM. </i> J Mol Biol, 2010","term_id":"GO:0060090","curator_id":"ndavey","start":623,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"20875424","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006198","region_id":"DP01073r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":680,"term_name":"protein binding","released":"2022_03","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","reference_html":"Dynamic interactions between clathrin and locally structured elements in a disordered protein mediate clathrin lattice assembly. <i> Zhuo Y, Ilangovan U, Schirf V, Demeler B, Sousa R, Hinck AP, Lafer EM. </i> J Mol Biol, 2010","term_id":"GO:0005515","curator_id":"ndavey","start":623,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"20875424","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006198","region_id":"DP01073r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q61548","date":"2016-09-18T10:13:53.000Z","acc":"Q61548","name":"Clathrin coat assembly protein AP180","length":901,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000289A5","genes":[{"name":{"value":"Snap91"}}],"alphafold_very_low_content":0.6470588235294118,"disorder_content":0.06437291897891231,"disprot_consensus":{"full":[{"start":623,"end":680,"type":"D"}],"Structural state":[{"start":623,"end":680,"type":"D"}],"Molecular function":[{"start":623,"end":680,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_Q7YUB9","sequence":"MPPIATRRGQYEPKVQQAKLSPDTIPLNPADKTKDPLARADSLHHHVESDSQEDDKAAEEPPLSRKRWQNRTFRRKGRRQAPYKHK","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Tylenchina","Tylenchomorpha","Aphelenchoidea","Aphelenchidae","Aphelenchus"],"uniref90":"UniRef90_Q7YUB9","disprot_id":"DP01074","ncbi_taxon_id":70226,"regions_counter":8,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":86,"region_id":"DP01074r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Catalytic and chaperone-like functions in an intrinsically disordered protein associated with desiccation tolerance. <i> Chakrabortee S, Meersman F, Kaminski Schierle GS, Bertoncini CW, McGee B, Kaminski CF, Tunnacliffe A. </i> Proc Natl Acad Sci U S A, 2010","term_id":"IDPO:0000002","curator_id":"ndavey","start":1,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20805515","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":86,"term_name":"protein folding chaperone","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Catalytic and chaperone-like functions in an intrinsically disordered protein associated with desiccation tolerance. <i> Chakrabortee S, Meersman F, Kaminski Schierle GS, Bertoncini CW, McGee B, Kaminski CF, Tunnacliffe A. </i> Proc Natl Acad Sci U S A, 2010","term_id":"GO:0044183","curator_id":"ndavey","start":1,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"20805515","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01074r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":86,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Catalytic and chaperone-like functions in an intrinsically disordered protein associated with desiccation tolerance. <i> Chakrabortee S, Meersman F, Kaminski Schierle GS, Bertoncini CW, McGee B, Kaminski CF, Tunnacliffe A. </i> Proc Natl Acad Sci U S A, 2010","term_id":"GO:0005515","curator_id":"ndavey","start":1,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"20805515","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01074r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":86,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Catalytic and chaperone-like functions in an intrinsically disordered protein associated with desiccation tolerance. <i> Chakrabortee S, Meersman F, Kaminski Schierle GS, Bertoncini CW, McGee B, Kaminski CF, Tunnacliffe A. </i> Proc Natl Acad Sci U S A, 2010","term_id":"GO:0003676","curator_id":"ndavey","start":1,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"20805515","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01074r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":86,"region_id":"DP01074r005","released":"2022_03","ec_id":"ECO:0006228","reference_html":"Catalytic and chaperone-like functions in an intrinsically disordered protein associated with desiccation tolerance. <i> Chakrabortee S, Meersman F, Kaminski Schierle GS, Bertoncini CW, McGee B, Kaminski CF, Tunnacliffe A. </i> Proc Natl Acad Sci U S A, 2010","term_id":"IDPO:0000002","curator_id":"ndavey","start":1,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20805515","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":86,"term_name":"protein folding chaperone","released":"2022_03","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","reference_html":"Catalytic and chaperone-like functions in an intrinsically disordered protein associated with desiccation tolerance. <i> Chakrabortee S, Meersman F, Kaminski Schierle GS, Bertoncini CW, McGee B, Kaminski CF, Tunnacliffe A. </i> Proc Natl Acad Sci U S A, 2010","term_id":"GO:0044183","curator_id":"ndavey","start":1,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"20805515","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006228","region_id":"DP01074r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":86,"term_name":"protein binding","released":"2022_03","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","reference_html":"Catalytic and chaperone-like functions in an intrinsically disordered protein associated with desiccation tolerance. <i> Chakrabortee S, Meersman F, Kaminski Schierle GS, Bertoncini CW, McGee B, Kaminski CF, Tunnacliffe A. </i> Proc Natl Acad Sci U S A, 2010","term_id":"GO:0005515","curator_id":"ndavey","start":1,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"20805515","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006228","region_id":"DP01074r007","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":86,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","reference_html":"Catalytic and chaperone-like functions in an intrinsically disordered protein associated with desiccation tolerance. <i> Chakrabortee S, Meersman F, Kaminski Schierle GS, Bertoncini CW, McGee B, Kaminski CF, Tunnacliffe A. </i> Proc Natl Acad Sci U S A, 2010","term_id":"GO:0003676","curator_id":"ndavey","start":1,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"20805515","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006228","region_id":"DP01074r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q7YUB9","date":"2016-09-18T10:23:35.000Z","acc":"Q7YUB9","name":"Anhydrin-1","length":86,"organism":"Aphelenchus avenae","dataset":[],"UniParc":"UPI00001B97B3","genes":[{"name":{"value":"Ahn-1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAQ20894.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAQ20894.1"}}]}}],"alphafold_very_low_content":0.06976744186046512,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":86,"type":"D"}],"Structural state":[{"start":1,"end":86,"type":"D"}],"Molecular function":[{"start":1,"end":86,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_P20676","sequence":"MSSNTSSVMSSPRVEKRSFSSTLKSFFTNPNKKRPSSKKVFSSNLSYANHLEESDVEDTLHVNKRKRVSGTSQHSDSLTQNNNNAPIIIYGTENTERPPLLPILPIQRLRLLREKQRVRNMRELGLIQSTEFPSITSSVILGSQSKSDEGGSYLCTSSTPSPIKNGSCTRQLAGKSGEDTNVGLPILKSLKNRSNRKRFHSQSKGTVWSANFEYDLSEYDAIQKKDNKDKEGNAGGDQKTSENRNNIKSSISNGNLATGPNLTSEIEDLRADINSNRLSNPQKNLLLKGPASTVAKTAPIQESFVPNSERSGTPTLKKNIEPKKDKESIVLPTVGFDFIKDNETPSKKTSPKATSSAGAVFKSSVEMGKTDKSTKTAEAPTLSFNFSQKANKTKAVDNTVPSTTLFNFGGKSDTVTSASQPFKFGKTSEKSENHTESDAPPKSTAPIFSFGKQEENGDEGDDENEPKRKRRLPVSEDTNTKPLFDFGKTGDQKETKKGESEKDASGKPSFVFGASDKQAEGTPLFTFGKKADVTSNIDSSAQFTFGKAATAKETHTKPSETPATIVKKPTFTFGQSTSENKISEGSAKPTFSFSKSEEERKSSPISNEAAKPSFSFPGKPVDVQAPTDDKTLKPTFSFTEPAQKDSSVVSEPKKPSFTFASSKTSQPKPLFSFGKSDAAKEPPGSNTSFSFTKPPANETDKRPTPPSFTFGGSTTNNTTTTSTKPSFSFGAPESMKSTASTAAANTEKLSNGFSFTKFNHNKEKSNSPTSFFDGSASSTPIPVLGKPTDATGNTTSKSAFSFGTANTNGTNASANSTSFSFNAPATGNGTTTTSNTSGTNIAGTFNVGKPDQSIASGNTNGAGSAFGFSSSGTAATGAASNQSSFNFGNNGAGGLNPFTSATSSTNANAGLFNKPPSTNAQNVNVPSAFNFTGNNSTPGGGSVFNMNGNTNANTVFAGSNNQPHQSQTPSFNTNSSFTPSTVPNINFSGLNGGITNTATNALRPSDIFGANAASGSNSNVTNPSSIFGGAGGVPTTSFGQPQSAPNQMGMGTNNGMSMGGGVMANRKIARMRHSKR","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P20676","disprot_id":"DP01075","ncbi_taxon_id":559292,"regions_counter":12,"creator":"gerdos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1076,"region_id":"DP01075r001","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. <i> Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. </i> Proc Natl Acad Sci U S A, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":300,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T10:08:07.491Z","reference_source":"pmid","term_name":"disorder","reference_id":"12604785","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Far-UV CD measurements of purified FG Nups produce spectra characteristic of unfolded proteins (Fig. ​3A). Each FG Nup has an intensive minimum near 200 nm and low ellipticity at 222 nm that reflect extensive contributions of unstructured coil and a lack of α-helical structure.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1076,"region_id":"DP01075r004","released":"2023_12","ec_id":"ECO:0006228","reference_html":"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. <i> Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. </i> Proc Natl Acad Sci U S A, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":300,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T10:08:40.601Z","reference_source":"pmid","term_name":"disorder","reference_id":"12604785","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Because FTIR spectroscopy is more sensitive to β-sheet structure than CD, we also generated FTIR spectra (amide I region) for each FG Nup. These spectra show broad absorbance bands near 1,655 cm−1 corresponding to disordered conformations (Table 3 and Fig. 5, which is published as supporting information on the PNAS web site). Deconvolution (Fourier self-deconvolution and second derivative) and curve fitting of the FTIR spectra permitted quantitative analyses of secondary structure content, confirming that purified FG Nups are composed mostly (≈80%) of disordered structure (Table ​3; Fig. ​3B).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1076,"region_id":"DP01075r007","released":"2023_12","ec_id":"ECO:0007691","reference_html":"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. <i> Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. </i> Proc Natl Acad Sci U S A, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":300,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T10:13:11.327Z","reference_source":"pmid","term_name":"disorder","reference_id":"12604785","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"In contrast, most FG Nups in nuclei are fully proteolysed within 60 min (category III) or 15 min (category IV) (Fig. ​4A). Nups localized to the nuclear basket structure of the NPC (Nup60p, Nup1p, and Nup2p) and to cytoplasmic fibrils (Nup159p and Nup42p) (30–32) are the most sensitive to proteinase K (Fig. ​4A). Some FG Nups located at the center of the NPC (Nup57p, Nup53p, and nNup145p) (30) degrade after a lag period of 10 min (category II), suggesting that these Nups also contain highly flexible structures but are not immediately accessible to the protease (Fig. ​4A).","type":"Results"}]},{"start":300,"end":1076,"reference_id":"12604785","reference_source":"pmid","reference_html":"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. <i> Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. </i> Proc Natl Acad Sci U S A, 2003","date":"2023-11-22T10:00:43.230Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01075r010","statement":[{"text":"Instead, the experimentally determined RS values for the FG Nups compare favorably to theoretical RS values predicted for monomeric proteins in natively unfolded conformations (Table 4, which is published as supporting information on the PNAS web site, www.pnas.org) (17).","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P20676","date":"2016-09-18T15:45:26.000Z","acc":"P20676","name":"Nucleoporin NUP1","length":1076,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000130A2B","genes":[{"name":{"value":"NUP1"},"orfNames":[{"value":"YOR3182C"}],"olnNames":[{"value":"YOR098C"}]}],"alphafold_very_low_content":0.8587360594795539,"disorder_content":0.7221189591078067,"disprot_consensus":{"full":[{"start":300,"end":1076,"type":"D"}],"Structural state":[{"start":300,"end":1076,"type":"D"}]}},{"features":{"pfam":[{"id":"PF04096","name":"Nup98-96 autopeptidase S59","start":815,"end":955},{"id":"PF13634","name":"Nucleoporin FG repeat region","start":6,"end":75},{"id":"PF13634","name":"Nucleoporin FG repeat region","start":287,"end":373},{"id":"PF13634","name":"Nucleoporin FG repeat region","start":429,"end":509}],"gene3D":[{"start":805,"end":958,"id":"3.30.1610.10","name":"Peptidase S59, nucleoporin"}]},"uniref50":"UniRef50_Q02629","sequence":"MFGNNRPMFGGSNLSFGSNTSSFGGQQSQQPNSLFGNSNNNNNSTSNNAQSGFGGFTSAAGSNSNSLFGNNNTQNNGAFGQSMGATQNSPFGSLNSSNASNGNTFGGSSSMGSFGGNTNNAFNNNSNSTNSPFGFNKPNTGGTLFGSQNNNSAGTSSLFGGQSTSTTGTFGNTGSSFGTGLNGNGSNIFGAGNNSQSNTTGSLFGNQQSSAFGTNNQQGSLFGQQSQNTNNAFGNQNQLGGSSFGSKPVGSGSLFGQSNNTLGNTTNNRNGLFGQMNSSNQGSSNSGLFGQNSMNSSTQGVFGQNNNQMQINGNNNNSLFGKANTFSNSASGGLFGQNNQQQGSGLFGQNSQTSGSSGLFGQNNQKQPNTFTQSNTGIGLFGQNNNQQQQSTGLFGAKPAGTTGSLFGGNSSTQPNSLFGTTNVPTSNTQSQQGNSLFGATKLTNMPFGGNPTANQSGSGNSLFGTKPASTTGSLFGNNTASTTVPSTNGLFGNNANNSTSTTNTGLFGAKPDSQSKPALGGGLFGNSNSNSSTIGQNKPVFGGTTQNTGLFGATGTNSSAVGSTGKLFGQNNNTLNVGTQNVPPVNNTTQNALLGTTAVPSLQQAPVTNEQLFSKISIPNSITNPVKATTSKVNADMKRNSSLTSAYRLAPKPLFAPSSNGDAKFQKWGKTLERSDRGSSTSNSITDPESSYLNSNDLLFDPDRRYLKHLVIKNNKNLNVINHNDDEASKVKLVTFTTESASKDDQASSSIAASKLTEKAHSPQTDLKDDHDESTPDPQSKSPNGSTSIPMIENEKISSKVPGLLSNDVTFFKNNYYISPSIETLGNKSLIELRKINNLVIGHRNYGKVEFLEPVDLLNTPLDTLCGDLVTFGPKSCSIYENCSIKPEKGEGINVRCRVTLYSCFPIDKETRKPIKNITHPLLKRSIAKLKENPVYKFESYDPVTGTYSYTIDHPVLT","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q02629","disprot_id":"DP01076","ncbi_taxon_id":559292,"regions_counter":15,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":640,"region_id":"DP01076r001","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. <i> Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. </i> Proc Natl Acad Sci U S A, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T10:09:15.046Z","reference_source":"pmid","term_name":"disorder","reference_id":"12604785","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Far-UV CD measurements of purified FG Nups produce spectra characteristic of unfolded proteins (Fig. ​3A). Each FG Nup has an intensive minimum near 200 nm and low ellipticity at 222 nm that reflect extensive contributions of unstructured coil and a lack of α-helical structure.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:32:25.592Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":640,"region_id":"DP01076r004","released":"2023_12","ec_id":"ECO:0006228","reference_html":"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. <i> Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. </i> Proc Natl Acad Sci U S A, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T10:09:06.512Z","reference_source":"pmid","term_name":"disorder","reference_id":"12604785","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Because FTIR spectroscopy is more sensitive to β-sheet structure than CD, we also generated FTIR spectra (amide I region) for each FG Nup. These spectra show broad absorbance bands near 1,655 cm−1 corresponding to disordered conformations (Table 3 and Fig. 5, which is published as supporting information on the PNAS web site). Deconvolution (Fourier self-deconvolution and second derivative) and curve fitting of the FTIR spectra permitted quantitative analyses of secondary structure content, confirming that purified FG Nups are composed mostly (≈80%) of disordered structure (Table ​3; Fig. ​3B).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:32:28.283Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":640,"region_id":"DP01076r007","released":"2023_12","ec_id":"ECO:0007691","reference_html":"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. <i> Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. </i> Proc Natl Acad Sci U S A, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T10:13:20.402Z","reference_source":"pmid","term_name":"disorder","reference_id":"12604785","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"In contrast, most FG Nups in nuclei are fully proteolysed within 60 min (category III) or 15 min (category IV) (Fig. ​4A). Nups localized to the nuclear basket structure of the NPC (Nup60p, Nup1p, and Nup2p) and to cytoplasmic fibrils (Nup159p and Nup42p) (30–32) are the most sensitive to proteinase K (Fig. ​4A). Some FG Nups located at the center of the NPC (Nup57p, Nup53p, and nNup145p) (30) degrade after a lag period of 10 min (category II), suggesting that these Nups also contain highly flexible structures but are not immediately accessible to the protease (Fig. ​4A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:32:30.671Z"}},{"start":1,"end":640,"reference_id":"12604785","reference_source":"pmid","reference_html":"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. <i> Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. </i> Proc Natl Acad Sci U S A, 2003","date":"2023-11-22T10:01:12.505Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01076r010","statement":[{"text":"Instead, the experimentally determined RS values for the FG Nups compare favorably to theoretical RS values predicted for monomeric proteins in natively unfolded conformations (Table 4, which is published as supporting information on the PNAS web site, www.pnas.org) (17).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:32:32.669Z"}},{"start":2,"end":580,"reference_id":"25562883","reference_source":"pmid","reference_html":"Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity.  <i> Schmidt HB, Görlich D. </i> Elife, 2015","date":"2023-11-22T10:44:19.438Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007122","ec_ontology":"ECO","ec_name":"in vitro assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP01076r011","statement":[{"text":"Remarkably, the Nup100 FG domain solution turned instantaneously turbid, pointing to a very rapid phase-separation and formation of small particles or liquid droplets, which can be easily recovered by centrifugation (Figure 1B). We tried to record a time course of this reaction (by static light scattering) but had to realise that the reaction had already reached its endpoint before we could place samples into the instrument and start the measurement (after 10–30 s).","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:32:40.171Z"}},{"start":2,"end":580,"reference_id":"25562883","reference_source":"pmid","reference_html":"Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity.  <i> Schmidt HB, Görlich D. </i> Elife, 2015","date":"2023-11-22T10:47:58.410Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","region_id":"DP01076r012","statement":[{"text":"When applying dynamic light scattering (DLS) to the 10 µM Nup100 FG domain sample, we observed a very prominent particle population with diameters ranging mostly between 2 and 8 µm (Figure 1C). At a lower concentration (0.625 µM), we observed a broader main peak with 0.4–4 µm particles (accounting for ≈60% by mass), another peak with 25 nm assembly intermediates (10%) and residual monomers (30%). The remaining monomer concentration can be taken as an estimate for the critical concentration for this phase-separation, which hence should be in the range of ≈200 nM FG domain or ≈10 µM FG repeat units.","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:32:45.661Z"}},{"start":2,"end":580,"reference_id":"25562883","reference_source":"pmid","reference_html":"Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity.  <i> Schmidt HB, Görlich D. </i> Elife, 2015","date":"2023-11-22T10:48:53.659Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007060","ec_ontology":"ECO","ec_name":"confocal laser scanning microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP01076r013","statement":[{"text":"Confocal laser-scanning microscopy (CLSM) of Nup100 FG particles, formed in the presence of 5% (vol/vol) Atto390-labeled FG domain tracers, indicated that the particle size increased with higher initial concentration (not shown). Most particles were of nearly spherical shape, whereby the evident deviations from perfect spheres indicated that the phase-separated objects represent solids rather than liquids (Figure 1D; further evidence for this assumption is provided below).","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:32:47.564Z"}},{"start":2,"end":580,"reference_id":"25562883","reference_source":"pmid","reference_html":"Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity.  <i> Schmidt HB, Görlich D. </i> Elife, 2015","date":"2023-11-22T10:52:01.391Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP01076r014","statement":[{"text":"For that we recorded the local fluorescent intensity of the added Alexa488 FG domain tracer, determined absolute fluorophore concentrations by calibration with a series of internal Alexa488-MBP standards (Figure 1E,F), and used this number to derive an average intra-particle concentration of the Nup100 FG domain of 275 mg/ml (corresponding to 4.7 mM FG domain or 200 mM FG motifs). Further assuming a specific partial volume for the protein part of 0.73 ml/g, one can estimate that the polypeptide accounts for 20% and water (respectively buffer) for the remaining 80% of the particle volume. These numbers are well in line with the assumption that these particles indeed represent hydrogels.","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:32:49.359Z"}},{"start":2,"end":580,"reference_id":"25562883","reference_source":"pmid","reference_html":"Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity.  <i> Schmidt HB, Görlich D. </i> Elife, 2015","date":"2023-11-22T10:59:41.215Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140694","term_name":"non-membrane-bounded organelle assembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP01076r015","statement":[{"text":"Following recombinant expression (after modest induction), we resuspended the bacteria in a physiological buffer, gently disrupted the cells by lysozyme treatment, and subjected the lysate to a 10,000×g centrifugation step. We observed that the FG domains from Nup100 and Nup116 (the second S.c. Nup98 paralog) pelleted under these conditions (Figure 4A,B). ","type":"Results"},{"text":"Microscopic analysis revealed that the Nup100 and Nup116 ‘FG bodies’ were 10 µm-sized irregularly shaped particles that probably had been ‘glued’ together from smaller species during the centrifugation steps. They nearly perfectly excluded our passive permeation marker MBP-Cherry and yet allowed a very efficient intra-particle accumulation of the NTR⋅cargo complex Impβ⋅IBB-GFP, reaching again a particle:buffer partition coefficient of around 200 (Figure 4A,B).","type":"Results"}],"term_comment":"","term_def":"\"The aggregation, arrangement and bonding together of a set of components to form a non-membrane-bounded organelle.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:32:51.199Z"}}],"released":"2016_10","uniref100":"UniRef100_Q02629","date":"2016-09-18T15:55:07.000Z","acc":"Q02629","name":"Nucleoporin NUP100/NSP100","length":959,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":["Condensates-related proteins"],"UniParc":"UPI000012FC09","genes":[{"name":{"value":"NUP100"},"synonyms":[{"value":"NSP100"}],"orfNames":[{"value":"YKL336"}],"olnNames":[{"value":"YKL068W"}]}],"alphafold_very_low_content":0.7570385818561001,"disorder_content":0.6673618352450469,"disprot_consensus":{"full":[{"start":1,"end":640,"type":"D"}],"Structural state":[{"start":1,"end":640,"type":"D"}],"Molecular function":[{"start":2,"end":580,"type":"F"}],"Biological process":[{"start":2,"end":580,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05064","name":"Nsp1-like C-terminal region","start":621,"end":730}],"gene3D":[{"start":663,"end":723,"id":"1.20.5.170","name":"1.20.5.170"}]},"uniref50":"UniRef50_P14907","sequence":"MNFNTPQQNKTPFSFGTANNNSNTTNQNSSTGAGAFGTGQSTFGFNNSAPNNTNNANSSITPAFGSNNTGNTAFGNSNPTSNVFGSNNSTTNTFGSNSAGTSLFGSSSAQQTKSNGTAGGNTFGSSSLFNNSTNSNTTKPAFGGLNFGGGNNTTPSSTGNANTSNNLFGATANANKPAFSFGATTNDDKKTEPDKPAFSFNSSVGNKTDAQAPTTGFSFGSQLGGNKTVNEAAKPSLSFGSGSAGANPAGASQPEPTTNEPAKPALSFGTATSDNKTTNTTPSFSFGAKSDENKAGATSKPAFSFGAKPEEKKDDNSSKPAFSFGAKSNEDKQDGTAKPAFSFGAKPAEKNNNETSKPAFSFGAKSDEKKDGDASKPAFSFGAKPDENKASATSKPAFSFGAKPEEKKDDNSSKPAFSFGAKSNEDKQDGTAKPAFSFGAKPAEKNNNETSKPAFSFGAKSDEKKDGDASKPAFSFGAKSDEKKDSDSSKPAFSFGTKSNEKKDSGSSKPAFSFGAKPDEKKNDEVSKPAFSFGAKANEKKESDESKSAFSFGSKPTGKEEGDGAKAAISFGAKPEEQKSSDTSKPAFTFGAQKDNEKKTEESSTGKSTADVKSSDSLKLNSKPVELKPVSLDNKTLDDLVTKWTNQLTESASHFEQYTKKINSWDQVLVKGGEQISQLYSDAVMAEHSQNKIDQSLQYIERQQDELENFLDNFETKTEALLSDVVSTSSGAAANNNDQKRQQAYKTAQTLDENLNSLSSNLSSLIVEINNVSNTFNKTTNIDINNEDENIQLIKILNSHFDALRSLDDNSTSLEKQINSIKK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P14907","disprot_id":"DP01077","ncbi_taxon_id":559292,"regions_counter":17,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":603,"region_id":"DP01077r001","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. <i> Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. </i> Proc Natl Acad Sci U S A, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T10:09:23.848Z","reference_source":"pmid","term_name":"disorder","reference_id":"12604785","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Far-UV CD measurements of purified FG Nups produce spectra characteristic of unfolded proteins (Fig. ​3A). Each FG Nup has an intensive minimum near 200 nm and low ellipticity at 222 nm that reflect extensive contributions of unstructured coil and a lack of α-helical structure.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-14T15:12:07.417Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":603,"region_id":"DP01077r004","released":"2023_12","ec_id":"ECO:0007691","reference_html":"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. <i> Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. </i> Proc Natl Acad Sci U S A, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T10:13:28.865Z","reference_source":"pmid","term_name":"disorder","reference_id":"12604785","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"In contrast, most FG Nups in nuclei are fully proteolysed within 60 min (category III) or 15 min (category IV) (Fig. ​4A). Nups localized to the nuclear basket structure of the NPC (Nup60p, Nup1p, and Nup2p) and to cytoplasmic fibrils (Nup159p and Nup42p) (30–32) are the most sensitive to proteinase K (Fig. ​4A). Some FG Nups located at the center of the NPC (Nup57p, Nup53p, and nNup145p) (30) degrade after a lag period of 10 min (category II), suggesting that these Nups also contain highly flexible structures but are not immediately accessible to the protease (Fig. ​4A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-14T15:12:08.999Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":603,"region_id":"DP01077r007","released":"2023_12","ec_id":"ECO:0006228","reference_html":"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. <i> Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. </i> Proc Natl Acad Sci U S A, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T10:09:32.736Z","reference_source":"pmid","term_name":"disorder","reference_id":"12604785","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Because FTIR spectroscopy is more sensitive to β-sheet structure than CD, we also generated FTIR spectra (amide I region) for each FG Nup. These spectra show broad absorbance bands near 1,655 cm−1 corresponding to disordered conformations (Table 3 and Fig. 5, which is published as supporting information on the PNAS web site). Deconvolution (Fourier self-deconvolution and second derivative) and curve fitting of the FTIR spectra permitted quantitative analyses of secondary structure content, confirming that purified FG Nups are composed mostly (≈80%) of disordered structure (Table ​3; Fig. ​3B).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-14T15:12:11.148Z"}},{"start":1,"end":603,"reference_id":"12604785","reference_source":"pmid","reference_html":"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. <i> Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. </i> Proc Natl Acad Sci U S A, 2003","date":"2023-11-22T10:02:03.715Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01077r014","statement":[{"text":"Instead, the experimentally determined RS values for the FG Nups compare favorably to theoretical RS values predicted for monomeric proteins in natively unfolded conformations (Table 4, which is published as supporting information on the PNAS web site, www.pnas.org) (17).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-14T15:12:13.194Z"}},{"start":262,"end":603,"reference_id":"12372823","reference_source":"pmid","reference_html":"GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta. <i> Bayliss R, Littlewood T, Strawn LA, Wente SR, Stewart M. </i> J Biol Chem, 2002","date":"2023-11-22T12:56:16.362Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q14974","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01077r015","statement":[{"text":"Both GLFG domains (Nup100 and Nup116) and a control FxFG-containing protein (GST-Nup1, residues 423–816), bound wild-type importin-β effectively (Fig. 3,lanes 1, 5, and 9).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-14T15:12:18.280Z"}},{"start":496,"end":607,"reference_id":"12372823","reference_source":"pmid","reference_html":"GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta. <i> Bayliss R, Littlewood T, Strawn LA, Wente SR, Stewart M. </i> J Biol Chem, 2002","date":"2023-11-22T13:09:03.620Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1O6O"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q14974","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01077r016","statement":[{"text":"Although the coordinates of Ib442 when bound to FF5, in the original Ib442-FF5 crystal form, was a more similar starting model than the IBB-bound structure, we thought it prudent to avoid the possibility of introducing bias arising from a Nup-bound Ib442 as a model. ","type":"Methods"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-14T15:12:21.222Z"}},{"start":496,"end":607,"reference_id":"12372823","reference_source":"pmid","reference_html":"GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta. <i> Bayliss R, Littlewood T, Strawn LA, Wente SR, Stewart M. </i> J Biol Chem, 2002","date":"2023-11-22T13:10:07.915Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1O6O"}],"region_id":"DP01077r017","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q14974"}],"statement":[{"text":"PDB structure shows this region remains disordered even in complex with Importin subunit beta-1.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-14T15:12:16.142Z"}}],"released":"2016_10","uniref100":"UniRef100_P14907","date":"2016-09-18T15:58:40.000Z","acc":"P14907","name":"Nucleoporin NSP1","length":823,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":["Condensates-related proteins"],"UniParc":"UPI0000053064","genes":[{"name":{"value":"NSP1"},"orfNames":[{"value":"J1207"}],"olnNames":[{"value":"YJL041W"}]}],"alphafold_very_low_content":0.7521263669501823,"disorder_content":0.7375455650060754,"disprot_consensus":{"full":[{"start":1,"end":607,"type":"D"}],"Structural state":[{"start":1,"end":607,"type":"D"}],"Molecular function":[{"start":262,"end":607,"type":"F"}]}},{"features":{"pfam":[{"id":"PF16755","name":"NUP159/214 beta propeller","start":35,"end":374}],"gene3D":[{"start":1,"end":387,"id":"2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"}]},"uniref50":"UniRef50_P40477","sequence":"MSSLKDEVPTETSEDFGFKFLGQKQILPSFNEKLPFASLQNLDISNSKSLFVAASGSKAVVGELQLLRDHITSDSTPLTFKWEKEIPDVIFVCFHGDQVLVSTRNALYSLDLEELSEFRTVTSFEKPVFQLKNVNNTLVILNSVNDLSALDLRTKSTKQLAQNVTSFDVTNSQLAVLLKDRSFQSFAWRNGEMEKQFEFSLPSELEELPVEEYSPLSVTILSPQDFLAVFGNVISETDDEVSYDQKMYIIKHIDGSASFQETFDITPPFGQIVRFPYMYKVTLSGLIEPDANVNVLASSCSSEVSIWDSKQVIEPSQDSERAVLPISEETDKDTNPIGVAVDVVTSGTILEPCSGVDTIERLPLVYILNNEGSLQIVGLFHVAAIKSGHYSINLESLEHEKSLSPTSEKIPIAGQEQEEKKKNNESSKALSENPFTSANTSGFTFLKTQPAAANSLQSQSSSTFGAPSFGSSAFKIDLPSVSSTSTGVASSEQDATDPASAKPVFGKPAFGAIAKEPSTSEYAFGKPSFGAPSFGSGKSSVESPASGSAFGKPSFGTPSFGSGNSSVEPPASGSAFGKPSFGTPSFGSGNSSAEPPASGSAFGKPSFGTSAFGTASSNETNSGSIFGKAAFGSSSFAPANNELFGSNFTISKPTVDSPKEVDSTSPFPSSGDQSEDESKSDVDSSSTPFGTKPNTSTKPKTNAFDFGSSSFGSGFSKALESVGSDTTFKFGTQASPFSSQLGNKSPFSSFTKDDTENGSLSKGSTSEINDDNEEHESNGPNVSGNDLTDSTVEQTSSTRLPETPSDEDGEVVEEEAQKSPIGKLTETIKKSANIDMAGLKNPVFGNHVKAKSESPFSAFATNITKPSSTTPAFSFGNSTMNKSNTSTVSPMEEADTKETSEKGPITLKSVENPFLPAKEERTGESSKKDHNDDPKDGYVSGSEISVRTSESAFDTTANEEIPKSQDVNNHEKSETDPKYSQHAVVDHDNKSKEMNETSKNNERSGQPNHGVQGDGIALKKDNEKENFDSNMAIKQFEDHQSSEEDASEKDSRQSSEVKESDDNMSLNSDRDESISESYDKLEDINTDELPHGGEAFKAREVSASADFDVQTSLEDNYAESGIQTDLSESSKENEVQTDAIPVKHNSTQTVKKEAVDNGLQTEPVETCNFSVQTFEGDENYLAEQCKPKQLKEYYTSAKVSNIPFVSQNSTLRLIESTFQTVEAEFTVLMENIRNMDTFFTDQSSIPLVKRTVRSINNLYTWRIPEAEILLNIQNNIKCEQMQITNANIQDLKEKVTDYVRKDIAQITEDVANAKEEYLFLMHFDDASSGYVKDLSTHQFRMQKTLRQKLFDVSAKINHTEELLNILKLFTVKNKRLDDNPLVAKLAKESLARDGLLKEIKLLREQVSRLQLEEKGKKASSFDASSSITKDMKGFKVVEVGLAMNTKKQIGDFFKNLNMAK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P40477","disprot_id":"DP01078","ncbi_taxon_id":559292,"regions_counter":10,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":881,"region_id":"DP01078r001","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. <i> Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. </i> Proc Natl Acad Sci U S A, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":441,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T10:09:40.090Z","reference_source":"pmid","term_name":"disorder","reference_id":"12604785","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Far-UV CD measurements of purified FG Nups produce spectra characteristic of unfolded proteins (Fig. ​3A). Each FG Nup has an intensive minimum near 200 nm and low ellipticity at 222 nm that reflect extensive contributions of unstructured coil and a lack of α-helical structure.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":881,"region_id":"DP01078r004","released":"2023_12","ec_id":"ECO:0006228","reference_html":"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. <i> Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. </i> Proc Natl Acad Sci U S A, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":441,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T10:09:47.452Z","reference_source":"pmid","term_name":"disorder","reference_id":"12604785","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Because FTIR spectroscopy is more sensitive to β-sheet structure than CD, we also generated FTIR spectra (amide I region) for each FG Nup. These spectra show broad absorbance bands near 1,655 cm−1 corresponding to disordered conformations (Table 3 and Fig. 5, which is published as supporting information on the PNAS web site). Deconvolution (Fourier self-deconvolution and second derivative) and curve fitting of the FTIR spectra permitted quantitative analyses of secondary structure content, confirming that purified FG Nups are composed mostly (≈80%) of disordered structure (Table ​3; Fig. ​3B).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":881,"region_id":"DP01078r007","released":"2023_12","ec_id":"ECO:0007691","reference_html":"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. <i> Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. </i> Proc Natl Acad Sci U S A, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":441,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T10:13:34.519Z","reference_source":"pmid","term_name":"disorder","reference_id":"12604785","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"In contrast, most FG Nups in nuclei are fully proteolysed within 60 min (category III) or 15 min (category IV) (Fig. ​4A). Nups localized to the nuclear basket structure of the NPC (Nup60p, Nup1p, and Nup2p) and to cytoplasmic fibrils (Nup159p and Nup42p) (30–32) are the most sensitive to proteinase K (Fig. ​4A). Some FG Nups located at the center of the NPC (Nup57p, Nup53p, and nNup145p) (30) degrade after a lag period of 10 min (category II), suggesting that these Nups also contain highly flexible structures but are not immediately accessible to the protease (Fig. ​4A).","type":"Results"}]},{"start":441,"end":881,"reference_id":"12604785","reference_source":"pmid","reference_html":"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. <i> Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. </i> Proc Natl Acad Sci U S A, 2003","date":"2023-11-22T10:02:29.008Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01078r010","statement":[{"text":"Instead, the experimentally determined RS values for the FG Nups compare favorably to theoretical RS values predicted for monomeric proteins in natively unfolded conformations (Table 4, which is published as supporting information on the PNAS web site, www.pnas.org) (17).","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P40477","date":"2016-09-18T16:05:05.000Z","acc":"P40477","name":"Nucleoporin NUP159","length":1460,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000036C5D","genes":[{"name":{"value":"NUP159"},"synonyms":[{"value":"NUP158"},{"value":"RAT7"}],"olnNames":[{"value":"YIL115C"}]}],"alphafold_very_low_content":0.5397260273972603,"disorder_content":0.30205479452054795,"disprot_consensus":{"full":[{"start":441,"end":881,"type":"D"}],"Structural state":[{"start":441,"end":881,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00638","name":"RanBP1 domain","start":204,"end":325}],"gene3D":[{"start":134,"end":327,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"}]},"uniref50":"UniRef50_P40517","sequence":"MSETNGGNAARENSEVKQTAVENPIDKLDGTPKRPREKDQDEQAEETSDKSEAPNKNDEEKKEEGKKDQEPSHKKIKVDDGKTVESGIVEDDKKEDKFVFGAASKFGTGFGVAKKDTKDGDATTSTESLPASDSKTKKPFAFGSGLSFGSGFNILKNKTENNSESEKKATDVDKDKVHSGSEQLANASEDTKDKPKPLKLQKQEVKSGEESEECIYQVNAKLYQLSNIKEGWKERGVGIIKINKSKDDVEKTRIVMRSRGILKVILNIQLVKGFTVQKGFTGSLQSEKFIRLLAVDDNGDPAQYAIKTGKKETTDELYNIIVKSVPK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P40517","disprot_id":"DP01079","ncbi_taxon_id":559292,"regions_counter":10,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":203,"region_id":"DP01079r001","released":"2023_12","ec_id":"ECO:0007691","reference_html":"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. <i> Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. </i> Proc Natl Acad Sci U S A, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T10:13:42.179Z","reference_source":"pmid","term_name":"disorder","reference_id":"12604785","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"In contrast, most FG Nups in nuclei are fully proteolysed within 60 min (category III) or 15 min (category IV) (Fig. ​4A). Nups localized to the nuclear basket structure of the NPC (Nup60p, Nup1p, and Nup2p) and to cytoplasmic fibrils (Nup159p and Nup42p) (30–32) are the most sensitive to proteinase K (Fig. ​4A). Some FG Nups located at the center of the NPC (Nup57p, Nup53p, and nNup145p) (30) degrade after a lag period of 10 min (category II), suggesting that these Nups also contain highly flexible structures but are not immediately accessible to the protease (Fig. ​4A).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":203,"region_id":"DP01079r004","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. <i> Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. </i> Proc Natl Acad Sci U S A, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T10:09:55.603Z","reference_source":"pmid","term_name":"disorder","reference_id":"12604785","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Far-UV CD measurements of purified FG Nups produce spectra characteristic of unfolded proteins (Fig. ​3A). Each FG Nup has an intensive minimum near 200 nm and low ellipticity at 222 nm that reflect extensive contributions of unstructured coil and a lack of α-helical structure.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":203,"region_id":"DP01079r007","released":"2023_12","ec_id":"ECO:0006228","reference_html":"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. <i> Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. </i> Proc Natl Acad Sci U S A, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T10:10:11.306Z","reference_source":"pmid","term_name":"disorder","reference_id":"12604785","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Because FTIR spectroscopy is more sensitive to β-sheet structure than CD, we also generated FTIR spectra (amide I region) for each FG Nup. These spectra show broad absorbance bands near 1,655 cm−1 corresponding to disordered conformations (Table 3 and Fig. 5, which is published as supporting information on the PNAS web site). Deconvolution (Fourier self-deconvolution and second derivative) and curve fitting of the FTIR spectra permitted quantitative analyses of secondary structure content, confirming that purified FG Nups are composed mostly (≈80%) of disordered structure (Table ​3; Fig. ​3B).","type":"Results"}]},{"start":1,"end":203,"reference_id":"12604785","reference_source":"pmid","reference_html":"Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. <i> Denning DP, Patel SS, Uversky V, Fink AL, Rexach M. </i> Proc Natl Acad Sci U S A, 2003","date":"2023-11-22T10:02:57.646Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01079r010","statement":[{"text":"Instead, the experimentally determined RS values for the FG Nups compare favorably to theoretical RS values predicted for monomeric proteins in natively unfolded conformations (Table 4, which is published as supporting information on the PNAS web site, www.pnas.org) (17).","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P40517","date":"2016-09-18T16:15:15.000Z","acc":"P40517","name":"Ran-specific GTPase-activating protein 2","length":327,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000013BFA4","genes":[{"name":{"value":"YRB2"},"olnNames":[{"value":"YIL063C"}]}],"alphafold_very_low_content":0.42813455657492355,"disorder_content":0.6207951070336392,"disprot_consensus":{"full":[{"start":1,"end":203,"type":"D"}],"Structural state":[{"start":1,"end":203,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00734","name":"Fungal cellulose binding domain","start":30,"end":57},{"id":"PF01341","name":"Glycosyl hydrolases family 6","start":120,"end":472}],"gene3D":[{"start":113,"end":476,"id":"3.20.20.40","name":"1, 4-beta cellobiohydrolase"}]},"uniref50":"UniRef50_Q9C1S9","sequence":"MAKFFLTAAFAAAALAAPVVEERQNCAPTWGQCGGIGFNGPTCCQSGSTCVKQNDWYSQCLPGSQVTTTSTTSTSSSSTTSRATSTTRTGGVTSITTAPTRTVTIPGGATTTASYNGNPFEGVQLWANNYYRSEVHTLAIPQITDPALRAAASAVAEVPSFQWLDRNVTVDTLLVETLSEIRAANQAGANPPYAAQIVVYDLPDRDCAAAASNGEWAIANNGANNYKGYINRIREILISFSDVRTILVIEPDSLANMVTNMNVAKCSGAASTYRELTIYALKQLDLPHVAMYMDAGHAGWLGWPANIQPAAELFAKIYEDAGKPRAVRGLATNVANYNAWSISSPPPYTSPNPNYDEKHYIEAFRPLLEARGFPAQFIVDQGRSGKQPTGQKEWGHWCNAIGTGFGMRPTANTGHQYVDAFVWVKPGGECDGTSDTTAARYDYHCGLEDALKPAPEAGQWFQAYFEQLLRNANPPF","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Sordariomycetidae","Sordariales","Chaetomiaceae","Humicola"],"uniref90":"UniRef90_Q9C1S9","disprot_id":"DP01080","ncbi_taxon_id":34413,"regions_counter":2,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":96,"region_id":"DP01080r001","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Protein disorder: conformational distribution of the flexible linker in a chimeric double cellulase. <i> von Ossowski I, Eaton JT, Czjzek M, Perkins SJ, Frandsen TP, Schülein M, Panine P, Henrissat B, Receveur-Bréchot V. </i> Biophys J, 2005","term_id":"IDPO:0000002","curator_id":"ndavey","start":44,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"15653742","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":96,"term_name":"flexible linker","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","reference_html":"Protein disorder: conformational distribution of the flexible linker in a chimeric double cellulase. <i> von Ossowski I, Eaton JT, Czjzek M, Perkins SJ, Frandsen TP, Schülein M, Panine P, Henrissat B, Receveur-Bréchot V. </i> Biophys J, 2005","term_id":"IDPO:0000033","curator_id":"ndavey","start":44,"term_ontology":"IDPO","curator_name":"Norman Davey","reference_id":"15653742","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","region_id":"DP01080r002","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_Q9C1S9","date":"2016-09-18T17:12:56.000Z","acc":"Q9C1S9","name":"Exoglucanase-6A","length":476,"organism":"Humicola insolens","dataset":[],"UniParc":"UPI0000069E91","genes":[{"name":{"value":"cel6A","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10413461","url":"http://www.ncbi.nlm.nih.gov/pubmed/10413461","alternativeUrl":"https://europepmc.org/abstract/MED/10413461"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"12842048","url":"http://www.ncbi.nlm.nih.gov/pubmed/12842048","alternativeUrl":"https://europepmc.org/abstract/MED/12842048"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"9335167","url":"http://www.ncbi.nlm.nih.gov/pubmed/9335167","alternativeUrl":"https://europepmc.org/abstract/MED/9335167"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"9882628","url":"http://www.ncbi.nlm.nih.gov/pubmed/9882628","alternativeUrl":"https://europepmc.org/abstract/MED/9882628"}}]},"synonyms":[{"value":"avi2","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"BAB39154.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAB39154.1"}}]}]}],"alphafold_very_low_content":0.08823529411764706,"disorder_content":0.11134453781512606,"disprot_consensus":{"full":[{"start":44,"end":96,"type":"D"}],"Structural state":[{"start":44,"end":96,"type":"D"}],"Disorder function":[{"start":44,"end":96,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02368","name":"Bacterial Ig-like domain (group 2)","start":229,"end":297},{"id":"PF02368","name":"Bacterial Ig-like domain (group 2)","start":315,"end":386},{"id":"PF02368","name":"Bacterial Ig-like domain (group 2)","start":404,"end":487},{"id":"PF02368","name":"Bacterial Ig-like domain (group 2)","start":493,"end":571},{"id":"PF02368","name":"Bacterial Ig-like domain (group 2)","start":586,"end":659},{"id":"PF02368","name":"Bacterial Ig-like domain (group 2)","start":676,"end":747},{"id":"PF02368","name":"Bacterial Ig-like domain (group 2)","start":762,"end":837},{"id":"PF02368","name":"Bacterial Ig-like domain (group 2)","start":853,"end":928},{"id":"PF02368","name":"Bacterial Ig-like domain (group 2)","start":944,"end":1022},{"id":"PF02368","name":"Bacterial Ig-like domain (group 2)","start":1035,"end":1118}],"gene3D":[{"start":226,"end":310,"id":"2.60.40.1080","name":"2.60.40.1080"},{"start":490,"end":581,"id":"2.60.40.1080","name":"2.60.40.1080"},{"start":51,"end":135,"id":"2.60.40.1080","name":"2.60.40.1080"},{"start":851,"end":940,"id":"2.60.40.1080","name":"2.60.40.1080"},{"start":402,"end":489,"id":"2.60.40.1080","name":"2.60.40.1080"},{"start":941,"end":1029,"id":"2.60.40.1080","name":"2.60.40.1080"},{"start":1030,"end":1123,"id":"2.60.40.1080","name":"2.60.40.1080"},{"start":672,"end":758,"id":"2.60.40.1080","name":"2.60.40.1080"},{"start":136,"end":225,"id":"2.60.40.1080","name":"2.60.40.1080"},{"start":311,"end":401,"id":"2.60.40.1080","name":"2.60.40.1080"},{"start":759,"end":850,"id":"2.60.40.1080","name":"2.60.40.1080"},{"start":582,"end":671,"id":"2.60.40.1080","name":"2.60.40.1080"}]},"uniref50":"UniRef50_A0A418AC61","sequence":"MKKIFCISIFLSMFFQSCMSWPLLTSLAGLAAGKRGGDSSFFHLLLGNSNPTITRIELSYQDSSIANGTSTALEVTAIFDNGTNQNITDSTYIVPDSQSVVTIQGNRVRGITSGSSIIKAEYNGLYSEQKITVTPAILNSIQVTSLESGILPKGTNRQLSAIGIFSDGSHQDISNDPLIVWSSSNPDLVQVDDSGLASGINLGTAHIRASFQSKQGAEEMTVGDAVLSQIQVTSNNLNIPLGKKQKLTATGIYSDNSNRDISSSVIWNSSNSTIANIQNNGILETADTGIVTVSASTENIIGSVKLIVTPAALVSISVSPTNSTVAKGLQENFKATGIFTDNSNSDITDQVTWDSSNTDILSISNASDSHGLASTLNQGNVKVTASIGGIQGSTDFKVTQEVLTSIEVSPTRTSIAKGLTQKFTAIGIFTDNSKKDITDQVTWNSSSAIVSVSNLDDNKGLGKAHAVGDTTITATLGKVAGKTWLTVVPAVLTSIQINPVNPSLAKGLTQKFTATGIYSDNSNKDITSAVTWFSSDSSIATISNAQKNQGNAYGAATGTTDIKATFGKVSSPVSTLSVTAAKLVEIQITPAAASKAKGLTERFKATGIFTDNSNSDITNQVTWNSSNTDIAEIKNTSGSKGITNTLTPGSSEISAALGSIKSSKVILKVTPAQLISIAVTPINPSVAKGLIRQFKATGTYTDHSVQDVTALATWSSSNPGKAMVNNVTGSVTTVATGNTNIKATIDSISGSSVLNVTPALLTSIEITPTINSITHGLTKQFKATGIFSDKSTQNLTQLVTWISSDPSKIEIENTSGKKGIATASKLGSSNIKAVYKFVQSSPIPITVTDLKLKSITISPSSSSIAKGLTQQFKAIGTFIDGSEQEITNLVTWYSSKSDVAPINNAANAKGLATALSIGSSNISAIYNSISSNKINFNVSAATLDSIKINPVNNNIAKGLTQQYTALGVYSDSTIQDISDSVTWSSSNSSSISISNSTETKGKATALQIGKSKITATYNSISENIDITVSAATLSSISISPINTNINATVSKQFFAMGTYSDGTKADLTSSVTWSSSNKSQSKVSNASKTKGLVTGIASGNSIITATYGSVSGNTILTVNKTDTIAPTVQSVVSLSPTTIQVVYSESINNKEALDLSNYKIINSSNFIGHCSDNTDFNSNSQTADFSLSSIKGSKNTFTITLSHSQILNKSYTLVVNKQGIHDLSSIPNSLSCPNNSDFIGKEQLKLTSAVCNSLNQVIVSFSKPLYSGKEATKSVECSNPSQCESRYKFAGVSSLGSITSVRILDGKVCGGAPADSSKICLTHSLLQSGGQYTIIAANDLNGDGFDNKSWGAIRDSFDQENLQSSPKDRINFIGCGNSPLNFMDGPIVSDPFGDGSDFGFLVDYNNQIYLGPNVKGNQAARFNYDGTFPESIFFSFTQDINATNRASSRDGGIPVPNYVTIGHTGCTLNSADITTGCGPDNEDGRGVFATGSLDKKSHIFIAGSKPKSFNYLYYSSDTDTNLNFKYISMGKITGLATAGTSSIAVLDDRIHVGFAKKNQNLNAPDFGKITFNTSEHNRCAIVNNCEASDGYRGNRFRIDRMPYFGGGSVDVVNYRSYKSDNSSINWGYYVGIDSLFVFKEKLYAANGGFPNSLHNGSIIHSTSANPSPCEGINRCSSWKDTAPRSNPKWHNSPHNNWFSLELTKYRNLIPADKAFSQFAEFNGRLYVTRTICVTKEDHSGLRQSLQTVKGCTDGSYTNRRPQLWKCDPTLTGDTTTCEAEDWSLVGDNGTGFTNFGDNSNHSMTMMVASGSYLYIGFDNENGIQIWRTNLENPGSSSHNWEPIGIGGLRDVTNRQIYSAISGMNFGVNFVYISVGNKNKPVKIYRQQNQ","taxonomy":["Bacteria","Spirochaetes","Leptospirales","Leptospiraceae","Leptospira"],"uniref90":"UniRef90_Q72V39","disprot_id":"DP01082","ncbi_taxon_id":44276,"regions_counter":12,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1165,"region_id":"DP01082r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Fibronectin binds to and induces conformational change in a disordered region of leptospiral immunoglobulin-like protein B. <i> Lin YP, Greenwood A, Nicholson LK, Sharma Y, McDonough SP, Chang YF. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"ndavey","start":1119,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19581300","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1165,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Fibronectin binds to and induces conformational change in a disordered region of leptospiral immunoglobulin-like protein B. <i> Lin YP, Greenwood A, Nicholson LK, Sharma Y, McDonough SP, Chang YF. </i> J Biol Chem, 2009","term_id":"GO:0060090","curator_id":"ndavey","start":1119,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"19581300","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01082r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1165,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Fibronectin binds to and induces conformational change in a disordered region of leptospiral immunoglobulin-like protein B. <i> Lin YP, Greenwood A, Nicholson LK, Sharma Y, McDonough SP, Chang YF. </i> J Biol Chem, 2009","term_id":"GO:0005515","curator_id":"ndavey","start":1119,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"19581300","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01082r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1165,"region_id":"DP01082r004","released":"2022_03","ec_id":"ECO:0006232","reference_html":"Fibronectin binds to and induces conformational change in a disordered region of leptospiral immunoglobulin-like protein B. <i> Lin YP, Greenwood A, Nicholson LK, Sharma Y, McDonough SP, Chang YF. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"ndavey","start":1119,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"differential scanning calorimetry evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19581300","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1165,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"differential scanning calorimetry evidence used in manual assertion","reference_html":"Fibronectin binds to and induces conformational change in a disordered region of leptospiral immunoglobulin-like protein B. <i> Lin YP, Greenwood A, Nicholson LK, Sharma Y, McDonough SP, Chang YF. </i> J Biol Chem, 2009","term_id":"GO:0060090","curator_id":"ndavey","start":1119,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"19581300","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006232","region_id":"DP01082r005","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1165,"term_name":"protein binding","released":"2022_03","ec_name":"differential scanning calorimetry evidence used in manual assertion","reference_html":"Fibronectin binds to and induces conformational change in a disordered region of leptospiral immunoglobulin-like protein B. <i> Lin YP, Greenwood A, Nicholson LK, Sharma Y, McDonough SP, Chang YF. </i> J Biol Chem, 2009","term_id":"GO:0005515","curator_id":"ndavey","start":1119,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"19581300","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006232","region_id":"DP01082r006","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1165,"region_id":"DP01082r007","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Fibronectin binds to and induces conformational change in a disordered region of leptospiral immunoglobulin-like protein B. <i> Lin YP, Greenwood A, Nicholson LK, Sharma Y, McDonough SP, Chang YF. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"ndavey","start":1119,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"chromatography evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19581300","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1165,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"chromatography evidence used in manual assertion","reference_html":"Fibronectin binds to and induces conformational change in a disordered region of leptospiral immunoglobulin-like protein B. <i> Lin YP, Greenwood A, Nicholson LK, Sharma Y, McDonough SP, Chang YF. </i> J Biol Chem, 2009","term_id":"GO:0060090","curator_id":"ndavey","start":1119,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"19581300","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","region_id":"DP01082r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1165,"term_name":"protein binding","released":"2022_03","ec_name":"chromatography evidence used in manual assertion","reference_html":"Fibronectin binds to and induces conformational change in a disordered region of leptospiral immunoglobulin-like protein B. <i> Lin YP, Greenwood A, Nicholson LK, Sharma Y, McDonough SP, Chang YF. </i> J Biol Chem, 2009","term_id":"GO:0005515","curator_id":"ndavey","start":1119,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"19581300","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","region_id":"DP01082r009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1165,"region_id":"DP01082r010","released":"2022_03","ec_id":"ECO:0007064","reference_html":"Fibronectin binds to and induces conformational change in a disordered region of leptospiral immunoglobulin-like protein B. <i> Lin YP, Greenwood A, Nicholson LK, Sharma Y, McDonough SP, Chang YF. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"ndavey","start":1119,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"dynamic light scattering assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19581300","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1165,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"dynamic light scattering assay evidence used in manual assertion","reference_html":"Fibronectin binds to and induces conformational change in a disordered region of leptospiral immunoglobulin-like protein B. <i> Lin YP, Greenwood A, Nicholson LK, Sharma Y, McDonough SP, Chang YF. </i> J Biol Chem, 2009","term_id":"GO:0060090","curator_id":"ndavey","start":1119,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"19581300","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007064","region_id":"DP01082r011","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1165,"term_name":"protein binding","released":"2022_03","ec_name":"dynamic light scattering assay evidence used in manual assertion","reference_html":"Fibronectin binds to and induces conformational change in a disordered region of leptospiral immunoglobulin-like protein B. <i> Lin YP, Greenwood A, Nicholson LK, Sharma Y, McDonough SP, Chang YF. </i> J Biol Chem, 2009","term_id":"GO:0005515","curator_id":"ndavey","start":1119,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"19581300","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007064","region_id":"DP01082r012","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_M3HD70","date":"2016-09-18T17:30:05.000Z","acc":"Q7X2A1","name":"Immunoglobulin-like B protein","length":1889,"organism":"Leptospira interrogans serovar Pomona","dataset":[],"UniParc":"UPI00001AA790","genes":[],"disorder_content":0.024880889359449446,"disprot_consensus":{"full":[{"start":1119,"end":1165,"type":"D"}],"Structural state":[{"start":1119,"end":1165,"type":"D"}],"Molecular function":[{"start":1119,"end":1165,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01336","name":"OB-fold nucleic acid binding domain","start":184,"end":265},{"id":"PF04057","name":"Replication factor-A protein 1, N-terminal domain","start":2,"end":91},{"id":"PF08646","name":"Replication factor-A C terminal domain","start":519,"end":672},{"id":"PF16900","name":"Replication protein A OB domain","start":292,"end":389}],"gene3D":[{"start":481,"end":679,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"},{"start":170,"end":279,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"},{"start":284,"end":406,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"},{"start":1,"end":107,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}]},"uniref50":"UniRef50_P27694","sequence":"MQQGDTSIKPVLQVINIRPITTGNSPPRYRLLMSDGLNTLSSFMLATQLNALVEGGQLASNCVCQVHRFIVNTLKDGRRVVILMDLEVVKSAGEVGVKIGNPVPYNEGHAQQQAVSAPASAATPPASKPQPQNGSLGVGSTVAKAYGASKPFGKPAGTGLLQPTSGTQSKVVPIASLTPYQSKWTICARVTNKSQIRTWSNSRGEGKLFSIELVDESGEIRATAFNEQVDKFFPLIEVNKVYYFSKGTLKIANKQFSAVKNDYEMTFNNETSVLPCEDGHHLPTVQFDFTGIGDLESKSKDSLVDIIGICKSYEDATKITVKSNNREVAKRNICLMDMSGKVVTATLWGEDADKFDGSRQPVMAIKGARVSDFGGRSLSVLSSSTVLVNPDIPEAYKLRGWHYVFGDGGLKALLHRQAHDPLMNLESQRKQLELKCCVLTLIPPGRQGFNSCVLESSAESISGLRCGQLMWGFDSEGQALDGVSISDLRSGGTGGSNTNWKTLYEAKSENLGQGDKADYFSTVATVVFLRKENCMYQACPTQDCNKKVIDQQNGLYRCEKCDREFPNFKYRMILSVNIADFQENQWVTCFQESAEAILGQNTVYLGELKEKVGCVFVSMNEQAFEEVFQNANFRSFTFRIRVKLETYNDESRIKATVIDVKPVDYRDYSKRLIMNIRKNI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_Q7TP21","disprot_id":"DP01083","ncbi_taxon_id":10116,"regions_counter":4,"creator":"ndavey","regions":[{"start":91,"end":167,"reference_id":"17721672","reference_source":"pmid","reference_html":"Dynamic behavior of an intrinsically unstructured linker domain is conserved in the face of negligible amino acid sequence conservation. <i> Daughdrill GW, Narayanaswami P, Gilmore SH, Belczyk A, Brown CJ. </i> J Mol Evol, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01083r003","statement":[{"text":"Dynamic Behavior of an Intrinsically Unstructured Linker Domain Is Conserved in the Face of Negligible Amino Acid Sequence Conservation","type":"Title"},{"text":"The IULD functions to tether two high affinity single stranded DNA binding domains (DBD A and B) to an N-terminal single stranded DNA (ssDNA) binding and protein interaction domain (DBD F; see Fig. 1 for domain structure of RPA70) (Daughdrill et al. 2001).","type":"Introduction"},{"text":"Plot showing the values for the reduced spectral density function at 0 frequency, J(0). J(0) values are plotted on the vertical axis and residue number is plotted on the horizontal axis.","type":"Figure"},{"text":"Unstructured linker domain (IULD) connecting two compact globular regions - the N-terminal DBD F domain and the ss-DNA binding DBD A domain - in the 70 kDa subunit of replication protein A (RPA70).","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":91,"end":167,"reference_id":"17721672","reference_source":"pmid","reference_html":"Dynamic behavior of an intrinsically unstructured linker domain is conserved in the face of negligible amino acid sequence conservation. <i> Daughdrill GW, Narayanaswami P, Gilmore SH, Belczyk A, Brown CJ. </i> J Mol Evol, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01083r004","statement":[{"text":"Dynamic Behavior of an Intrinsically Unstructured Linker Domain Is Conserved in the Face of Negligible Amino Acid Sequence Conservation","type":"Title"},{"text":"The IULD functions to tether two high affinity single stranded DNA binding domains (DBD A and B) to an N-terminal single stranded DNA (ssDNA) binding and protein interaction domain (DBD F; see Fig. 1 for domain structure of RPA70) (Daughdrill et al. 2001).","type":"Introduction"},{"text":"Plot showing the values for the reduced spectral density function at 0 frequency, J(0). J(0) values are plotted on the vertical axis and residue number is plotted on the horizontal axis.","type":"Figure"},{"text":"Unstructured linker domain (IULD) connecting two compact globular regions - the N-terminal DBD F domain and the ss-DNA binding DBD A domain - in the 70 kDa subunit of replication protein A (RPA70).","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_Q7TP21","date":"2016-09-18T19:03:03.000Z","acc":"Q7TP21","name":"Replication protein A subunit","length":680,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI00001B48AB","genes":[{"name":{"value":"Rpa1","evidences":[{"code":"ECO:0000313","source":{"name":"Ensembl","id":"ENSRNOP00000079958","url":"https://www.ensembl.org/id/ENSRNOP00000079958"}},{"code":"ECO:0000313","source":{"name":"RGD","id":"1307376","url":"https://rgd.mcw.edu/tools/genes/genes_view.cgi?id=1307376"}}]}}],"alphafold_very_low_content":0.2,"disorder_content":0.11323529411764706,"disprot_consensus":{"full":[{"start":91,"end":167,"type":"D"}],"Structural state":[{"start":91,"end":167,"type":"D"}],"Disorder function":[{"start":91,"end":167,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01336","name":"OB-fold nucleic acid binding domain","start":187,"end":269},{"id":"PF04057","name":"Replication factor-A protein 1, N-terminal domain","start":5,"end":110},{"id":"PF08646","name":"Replication factor-A C terminal domain","start":453,"end":598},{"id":"PF16900","name":"Replication protein A OB domain","start":296,"end":393}],"gene3D":[{"start":3,"end":124,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"},{"start":284,"end":419,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"},{"start":173,"end":283,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"},{"start":420,"end":606,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}]},"uniref50":"UniRef50_C8VB95","sequence":"MAGQITQGALDAMFNDPDRAQQQFPVPILQCLQIKTLDSKNGGAGATERFRIVLSDLKNYVQCMMATQTNHLVHDGLLQRGCIVRLKQYQAQCLKGKNILIVLDLEVIQSLGCPEKMGDPQPLGPRSAEPQQNPNLGSTGFYGVKSEPTQDTKPQFPRQMPSRNASGGQGSSTIYPIEGLSPFSHKWTIKARVTSKSDIKTWHKASGEGKLFSVNFLDESGEIRATGFNDQVDQFYDLLQEGQVYYISTPCRVQLAKKQWSNLPNDYELTFERDTVIEKAEDQTSVPQVRFNFVNIQELQDVERDATVDIIGVLKEVQEVTQIVSKTTQKPYDKRELTLVDNTGYSVRCTIWGKTATNFDAQPESIVAFKGTKVSDFGGRSLSLLSSGTMAIDPDIPEAHHLKGWYDSSGRNNTFATHNNMQTLGGATGRKDDAKTISQVKEENLGTNEAPDYFALKATVVFIKQDNFAYPGCRSEGCNRKVTDMGDGTWRCEKCQINHDRPQYRYIMSVNVNDHTGQLWLSCFDDTARVIMGKSADELMEIRETDETRLPAEFEQANCRKLNFRCRAKMDTFGEQQRIRYQVMSVAPLDYKMEGNKLNELINSYNQMSM","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Sordariomycetidae","Sordariales","Sordariaceae","Neurospora"],"uniref90":"UniRef90_F7VU70","disprot_id":"DP01084","ncbi_taxon_id":367110,"regions_counter":2,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":173,"region_id":"DP01084r001","released":"2022_03","ec_id":"ECO:0006198","reference_html":"Dynamic behavior of an intrinsically unstructured linker domain is conserved in the face of negligible amino acid sequence conservation. <i> Daughdrill GW, Narayanaswami P, Gilmore SH, Belczyk A, Brown CJ. </i> J Mol Evol, 2007","term_id":"IDPO:0000002","curator_id":"fquaglia","start":111,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17721672","statement":[{"text":"Dynamic Behavior of an Intrinsically Unstructured Linker Domain Is Conserved in the Face of Negligible Amino Acid Sequence Conservation","type":"Title"},{"text":"The IULD functions to tether two high affinity single stranded DNA binding domains (DBD A and B) to an N-terminal single stranded DNA (ssDNA) binding and protein interaction domain (DBD F; see Fig. 1 for domain structure of RPA70) (Daughdrill et al. 2001).","type":"Introduction"},{"text":"Plot showing the values for the reduced spectral density function at 0 frequency, J(0). J(0) values are plotted on the vertical axis and residue number is plotted on the horizontal axis.","type":"Figure"},{"text":"Unstructured linker domain (IULD) connecting two compact globular regions - the N-terminal DBD F domain and the ss-DNA binding DBD A domain - in the 70 kDa subunit of replication protein A (RPA70).","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":173,"term_name":"flexible linker","released":"2022_03","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","reference_html":"Dynamic behavior of an intrinsically unstructured linker domain is conserved in the face of negligible amino acid sequence conservation. <i> Daughdrill GW, Narayanaswami P, Gilmore SH, Belczyk A, Brown CJ. </i> J Mol Evol, 2007","term_id":"IDPO:0000033","curator_id":"fquaglia","start":111,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17721672","version":4,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006198","region_id":"DP01084r002","statement":[{"text":"Dynamic Behavior of an Intrinsically Unstructured Linker Domain Is Conserved in the Face of Negligible Amino Acid Sequence Conservation","type":"Title"},{"text":"The IULD functions to tether two high affinity single stranded DNA binding domains (DBD A and B) to an N-terminal single stranded DNA (ssDNA) binding and protein interaction domain (DBD F; see Fig. 1 for domain structure of RPA70) (Daughdrill et al. 2001).","type":"Introduction"},{"text":"Plot showing the values for the reduced spectral density function at 0 frequency, J(0). J(0) values are plotted on the vertical axis and residue number is plotted on the horizontal axis.","type":"Figure"},{"text":"Unstructured linker domain (IULD) connecting two compact globular regions - the N-terminal DBD F domain and the ss-DNA binding DBD A domain - in the 70 kDa subunit of replication protein A (RPA70).","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_Q8X0J1","date":"2016-09-18T19:04:21.000Z","acc":"Q1K7R9","name":"Replication protein A subunit","length":610,"organism":"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)","dataset":[],"UniParc":"UPI00000698C0","genes":[{"name":{"value":"rpa-1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EAA32097.1","url":"https://www.ebi.ac.uk/ena/browser/view/EAA32097.1"}}]},"orfNames":[{"value":"NCU03606","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EAA32097.1","url":"https://www.ebi.ac.uk/ena/browser/view/EAA32097.1"}}]}]}],"alphafold_very_low_content":0.10491803278688525,"disorder_content":0.10327868852459017,"disprot_consensus":{"full":[{"start":111,"end":173,"type":"D"}],"Structural state":[{"start":111,"end":173,"type":"D"}],"Disorder function":[{"start":111,"end":173,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01336","name":"OB-fold nucleic acid binding domain","start":216,"end":294},{"id":"PF04057","name":"Replication factor-A protein 1, N-terminal domain","start":5,"end":103},{"id":"PF08646","name":"Replication factor-A C terminal domain","start":483,"end":634},{"id":"PF16900","name":"Replication protein A OB domain","start":320,"end":424}],"gene3D":[{"start":449,"end":639,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"},{"start":308,"end":448,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"},{"start":195,"end":303,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"},{"start":3,"end":115,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}]},"uniref50":"UniRef50_Q9SKI4","sequence":"MPVSLTPNAITAIHDGDVNLKPLLQVLEIKMIGRSQERSQERYRFLISDGVSAQHAMVAVQLNDRVKSGQFEKGSIVQLIDYICSDVKGRKLIVVLNMETIVQQSETIGNPTIFGETDTEAQKTFSGTGNIPPPNRVVFNEPMVQHSVNRAPPRGVNIQNQANNTPSFRPSVQPSYQPPASYRNHGPIMKNEAPARVIPIAALNPYQGRWAIKARVTAKGDIRRYNNAKGDGKVFSFDLLDYDGGEIRVTCFNALVDRFYDVTEVGKVYLISKGSLKPAQKNFNHLKNEWEIFLESTSTVELCPDEDGSIPKQQFSFRPISDIENAENNTILDVIGVVTSVNPSVPILRKNGMETHRRILNLKDESGKAVEVTLWGEFCNRDGRQLEEMVDSAFHPVLAIKAGKVSDFSGKSVGTISSTQLFINPDFPEAHKLRTWFDYGGKDTASFSISRDTMPGGVSRNEIRKNVSQIKEEGLGRSDKPDWITVKATISFIKTDSFCYTACPLMIGDKQCNKKVTRSGTNRWLCDRCNQESDECDYRYLLQVQIQDHTGLTWITAFQETGEEIMGCPAKKLYAMKYELEKEEEFAEIVRDRLFHQYMLKLKIKEESYGDEQRVKMTVVKVDKVNYTSESKYMLDLLVR","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q9SKI4","disprot_id":"DP01085","ncbi_taxon_id":3702,"regions_counter":2,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":193,"region_id":"DP01085r001","released":"2022_03","ec_id":"ECO:0006198","reference_html":"Dynamic behavior of an intrinsically unstructured linker domain is conserved in the face of negligible amino acid sequence conservation. <i> Daughdrill GW, Narayanaswami P, Gilmore SH, Belczyk A, Brown CJ. </i> J Mol Evol, 2007","term_id":"IDPO:0000002","curator_id":"fquaglia","start":106,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17721672","statement":[{"text":"Dynamic Behavior of an Intrinsically Unstructured Linker Domain Is Conserved in the Face of Negligible Amino Acid Sequence Conservation","type":"Title"},{"text":"The IULD functions to tether two high affinity single stranded DNA binding domains (DBD A and B) to an N-terminal single stranded DNA (ssDNA) binding and protein interaction domain (DBD F; see Fig. 1 for domain structure of RPA70) (Daughdrill et al. 2001).","type":"Introduction"},{"text":"Plot showing the values for the reduced spectral density function at 0 frequency, J(0). J(0) values are plotted on the vertical axis and residue number is plotted on the horizontal axis.","type":"Figure"},{"text":"Unstructured linker domain (IULD) connecting two compact globular regions - the N-terminal DBD F domain and the ss-DNA binding DBD A domain - in the 70 kDa subunit of replication protein A (RPA70).","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":193,"term_name":"flexible linker","released":"2022_03","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","reference_html":"Dynamic behavior of an intrinsically unstructured linker domain is conserved in the face of negligible amino acid sequence conservation. <i> Daughdrill GW, Narayanaswami P, Gilmore SH, Belczyk A, Brown CJ. </i> J Mol Evol, 2007","term_id":"IDPO:0000033","curator_id":"fquaglia","start":106,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17721672","version":4,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006198","region_id":"DP01085r002","statement":[{"text":"Dynamic Behavior of an Intrinsically Unstructured Linker Domain Is Conserved in the Face of Negligible Amino Acid Sequence Conservation","type":"Title"},{"text":"The IULD functions to tether two high affinity single stranded DNA binding domains (DBD A and B) to an N-terminal single stranded DNA (ssDNA) binding and protein interaction domain (DBD F; see Fig. 1 for domain structure of RPA70) (Daughdrill et al. 2001).","type":"Introduction"},{"text":"Plot showing the values for the reduced spectral density function at 0 frequency, J(0). J(0) values are plotted on the vertical axis and residue number is plotted on the horizontal axis.","type":"Figure"},{"text":"Unstructured linker domain (IULD) connecting two compact globular regions - the N-terminal DBD F domain and the ss-DNA binding DBD A domain - in the 70 kDa subunit of replication protein A (RPA70).","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_Q9SKI4","date":"2016-09-18T19:05:03.000Z","acc":"Q9SKI4","name":"Replication protein A 70 kDa DNA-binding subunit A","length":640,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI0000060DC6","genes":[{"name":{"value":"RPA1A"},"synonyms":[{"value":"RPA70A"}],"orfNames":[{"value":"T12H3.6"}],"olnNames":[{"value":"At2g06510"}]}],"alphafold_very_low_content":0.1390625,"disorder_content":0.1375,"disprot_consensus":{"full":[{"start":106,"end":193,"type":"D"}],"Structural state":[{"start":106,"end":193,"type":"D"}],"Disorder function":[{"start":106,"end":193,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02721","name":"Domain of unknown function DUF223","start":191,"end":309},{"id":"PF04057","name":"Replication factor-A protein 1, N-terminal domain","start":9,"end":109},{"id":"PF08646","name":"Replication factor-A C terminal domain","start":475,"end":620},{"id":"PF16900","name":"Replication protein A OB domain","start":319,"end":412}],"gene3D":[{"start":8,"end":119,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"},{"start":438,"end":627,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"},{"start":183,"end":292,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"},{"start":297,"end":437,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}]},"uniref50":"UniRef50_Q10Q08","sequence":"MDSDAAPSVTPGAVAFVLENASPDAATGVPVPEIVLQVVDLKPIGTRFTFLASDGKDKIKTMLLTQLAPEVRSGNIQNLGVIRVLDYTCNTIGEKQEKVLIITKLEVVFKALDSEIKCEAEKQEEKPAILLSPKEESVVLSKPTNAPPLPPVVLKPKQEVKSASQIVNEQRGNAAPAARLAMTRRVHPLISLNPYQGNWIIKVRVTSKGNLRTYKNARGEGCVFNVELTDVDGTQIQATMFNEAAKKFYPMFELGKVYYISKGSLRVANKQFKTVHNDYEMTLNENAVVEEAEGETFIPQIQYNFVKIDQLGPYVGGRELVDVIGVVQSVSPTLSVRRKIDNETIPKRDIVVADDSSKTVTISLWNDLATTTGQELLDMVDSAPIIAIKSLKVSDFQGLSLSTVGRSTIVVNPDLPEAEQLRAWYDSEGKGTSMASIGSDMGASRVGGARSMYSDRVFLSHITSDPNLGQDKPVFFSLNAYISLIKPDQTMWYRACKTCNKKVTEAIGSGYWCEGCQKNDAECSLRYIMVIKVSDPTGEAWLSLFNDQAERIVGCSADELDRIRKEEGDDSYLLKLKEATWVPHLFRVSVTQNEYMNEKRQRITVRSEAPVDHAAEAKYMLEEIAKLTGC","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","BOP clade","Oryzoideae","Oryzeae","Oryzinae","Oryza","Oryza sativa"],"uniref90":"UniRef90_Q10Q08","disprot_id":"DP01086","ncbi_taxon_id":39947,"regions_counter":2,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":180,"region_id":"DP01086r001","released":"2022_03","ec_id":"ECO:0006198","reference_html":"Dynamic behavior of an intrinsically unstructured linker domain is conserved in the face of negligible amino acid sequence conservation. <i> Daughdrill GW, Narayanaswami P, Gilmore SH, Belczyk A, Brown CJ. </i> J Mol Evol, 2007","term_id":"IDPO:0000002","curator_id":"fquaglia","start":105,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17721672","statement":[{"text":"Dynamic Behavior of an Intrinsically Unstructured Linker Domain Is Conserved in the Face of Negligible Amino Acid Sequence Conservation","type":"Title"},{"text":"The IULD functions to tether two high affinity single stranded DNA binding domains (DBD A and B) to an N-terminal single stranded DNA (ssDNA) binding and protein interaction domain (DBD F; see Fig. 1 for domain structure of RPA70) (Daughdrill et al. 2001). ","type":"Introduction"},{"text":"Plot showing the values for the reduced spectral density function at 0 frequency, J(0). J(0) values are plotted on the vertical axis and residue number is plotted on the horizontal axis.","type":"Figure"},{"text":"Unstructured linker domain (IULD) connecting two compact globular regions - the N-terminal DBD F domain and the ss-DNA binding DBD A domain - in the 70 kDa subunit of replication protein A (RPA70).","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":180,"term_name":"flexible linker","released":"2022_03","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","reference_html":"Dynamic behavior of an intrinsically unstructured linker domain is conserved in the face of negligible amino acid sequence conservation. <i> Daughdrill GW, Narayanaswami P, Gilmore SH, Belczyk A, Brown CJ. </i> J Mol Evol, 2007","term_id":"IDPO:0000033","curator_id":"fquaglia","start":105,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17721672","version":4,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006198","region_id":"DP01086r002","statement":[{"text":"Dynamic Behavior of an Intrinsically Unstructured Linker Domain Is Conserved in the Face of Negligible Amino Acid Sequence Conservation","type":"Title"},{"text":"The IULD functions to tether two high affinity single stranded DNA binding domains (DBD A and B) to an N-terminal single stranded DNA (ssDNA) binding and protein interaction domain (DBD F; see Fig. 1 for domain structure of RPA70) (Daughdrill et al. 2001).","type":"Introduction"},{"text":"Plot showing the values for the reduced spectral density function at 0 frequency, J(0). J(0) values are plotted on the vertical axis and residue number is plotted on the horizontal axis.","type":"Figure"},{"text":"Unstructured linker domain (IULD) connecting two compact globular regions - the N-terminal DBD F domain and the ss-DNA binding DBD A domain - in the 70 kDa subunit of replication protein A (RPA70).","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_Q10Q08","date":"2016-09-18T19:06:11.000Z","acc":"Q10Q08","name":"Replication protein A 70 kDa DNA-binding subunit B","length":630,"organism":"Oryza sativa subsp. japonica","dataset":[],"UniParc":"UPI0000DB4529","genes":[{"name":{"value":"RPA1B"},"synonyms":[{"value":"RPA70B"}],"orfNames":[{"value":"OsJ_09906"}],"olnNames":[{"value":"Os03g0214100"},{"value":"LOC_Os03g11540"}]}],"alphafold_very_low_content":0.1253968253968254,"disorder_content":0.12063492063492064,"disprot_consensus":{"full":[{"start":105,"end":180,"type":"D"}],"Structural state":[{"start":105,"end":180,"type":"D"}],"Disorder function":[{"start":105,"end":180,"type":"F"}]}},{"acc":"Q1PAB4","sequence":"MEPVDPRLEPWKHPGSQPRTACTNCYCKKCCFHCQVCFIRKALGISYGRKKRRQRRRAPQDSETHQVSPPKQPASQPRGDPTGPKESKKKVERETETHPVN","creator":"jbergier","dataset":["Viral proteins","RNA-binding proteins"],"date":"2016-09-19T09:31:17.000Z","disprot_id":"DP01087","features":{"pfam":[{"id":"PF00539","name":"Transactivating regulatory protein (Tat)","start":2,"end":64}],"gene3D":[{"start":1,"end":86,"id":"4.10.20.10","name":"Tat domain","_id":"685af523b4ac24d5329d8b01"}]},"genes":[{"name":{"value":"tat","evidences":[{"source":{"id":"MF_04079","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04079","_id":"685af523b4ac24d5329d8bb0"},"code":"ECO:0000256","_id":"685af523b4ac24d5329d8baf"},{"source":{"id":"ABE73045.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/ABE73045.1","_id":"685af523b4ac24d5329d8bb2"},"code":"ECO:0000313","_id":"685af523b4ac24d5329d8bb1"}],"_id":"685af523b4ac24d5329d8bb3"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d8bae"}],"length":101,"name":"Protein Tat","ncbi_taxon_id":11676,"organism":"Human immunodeficiency virus 1","regions_counter":40,"released":"2016_10","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"UniParc":"UPI0000D5C32B","uniref100":"UniRef100_Q1PAB4","uniref50":"UniRef50_P04608","uniref90":"UniRef90_Q1PAB4","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":101,"interaction_partner":[],"reference_html":"UV and X-ray structural studies of a 101-residue long Tat protein from a HIV-1 primary isolate and of its mutated, detoxified, vaccine candidate. <i> Foucault M, Mayol K, Receveur-Bréchot V, Bussat MC, Klinguer-Hamour C, Verrier B, Beck A, Haser R, Gouet P, Guillon C. </i> Proteins, 2010","reference_id":"20034112","region_id":"DP01087r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In line with data in the literature concerning other Tat variants, the CD spectra demonstrated the absence of any significant ordered secondary structure for these proteins, as seen from the intensive minimum at 198 nm and an ellipticity close to zero in the vicinity of 185 and 222 nm (see Fig. 2).","_id":"685af523b4ac24d5329d8b03"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T09:37:16.927Z","_id":"685af523b4ac24d5329d8b04"},"version":3,"_id":"685af523b4ac24d5329d8b02","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006206","ec_name":"near-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":101,"interaction_partner":[],"reference_html":"UV and X-ray structural studies of a 101-residue long Tat protein from a HIV-1 primary isolate and of its mutated, detoxified, vaccine candidate. <i> Foucault M, Mayol K, Receveur-Bréchot V, Bussat MC, Klinguer-Hamour C, Verrier B, Beck A, Haser R, Gouet P, Guillon C. </i> Proteins, 2010","reference_id":"20034112","region_id":"DP01087r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":" As expected, the CD spectrum of wt-Tat133 alone or in the presence of 6M urea was characteristic of a fully unfolded protein.","_id":"685af523b4ac24d5329d8b0d"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T09:37:10.902Z","_id":"685af523b4ac24d5329d8b0e"},"version":3,"_id":"685af523b4ac24d5329d8b0c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007064","ec_name":"dynamic light scattering assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":101,"interaction_partner":[],"reference_html":"UV and X-ray structural studies of a 101-residue long Tat protein from a HIV-1 primary isolate and of its mutated, detoxified, vaccine candidate. <i> Foucault M, Mayol K, Receveur-Bréchot V, Bussat MC, Klinguer-Hamour C, Verrier B, Beck A, Haser R, Gouet P, Guillon C. </i> Proteins, 2010","reference_id":"20034112","region_id":"DP01087r014","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Thus, the Stokes radii measured by DLS and gel filtration for Tat proteins are not compatible with a globular protein, but with a disordered state.","_id":"685af523b4ac24d5329d8b20"},{"type":"Results","text":"The hydrodynamic radii measured for wt-Tat133 and STLA-Tat133 by DLS analysis at a concentration of 1 mg/mL were RS = 30 ± 3 Å (data not shown), which is coherent with a fully unfolded protein.","_id":"685af523b4ac24d5329d8b21"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T09:36:32.605Z","_id":"685af523b4ac24d5329d8b22"},"version":3,"_id":"685af523b4ac24d5329d8b1f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":101,"interaction_partner":[],"reference_html":"UV and X-ray structural studies of a 101-residue long Tat protein from a HIV-1 primary isolate and of its mutated, detoxified, vaccine candidate. <i> Foucault M, Mayol K, Receveur-Bréchot V, Bussat MC, Klinguer-Hamour C, Verrier B, Beck A, Haser R, Gouet P, Guillon C. </i> Proteins, 2010","reference_id":"20034112","region_id":"DP01087r018","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"For wt-Tat133, this ratio Rg/Rs is between 1.1 and 1.4 depending if we use the Rs value measured by DLS or gel filtration, respectively, and is thus coherent with a fully unfolded protein.","_id":"685af523b4ac24d5329d8b2a"},{"type":"Results","text":"In the case of wt-Tat133, the Kratky plot is typical of a fully unfolded protein without significant residual structure [Fig. 4(B)].","_id":"685af523b4ac24d5329d8b2b"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T09:36:53.848Z","_id":"685af523b4ac24d5329d8b2c"},"version":3,"_id":"685af523b4ac24d5329d8b29","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0001184","ec_name":"gel-filtration evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":101,"interaction_partner":[],"reference_html":"UV and X-ray structural studies of a 101-residue long Tat protein from a HIV-1 primary isolate and of its mutated, detoxified, vaccine candidate. <i> Foucault M, Mayol K, Receveur-Bréchot V, Bussat MC, Klinguer-Hamour C, Verrier B, Beck A, Haser R, Gouet P, Guillon C. </i> Proteins, 2010","reference_id":"20034112","region_id":"DP01087r022","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Thus, the Stokes radii measured by DLS and gel filtration for Tat proteins are not compatible with a globular protein, but with a disordered state.","_id":"685af523b4ac24d5329d8b34"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T09:36:34.715Z","_id":"685af523b4ac24d5329d8b35"},"version":1,"_id":"685af523b4ac24d5329d8b33","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":101,"interaction_partner":[],"reference_html":"UV and X-ray structural studies of a 101-residue long Tat protein from a HIV-1 primary isolate and of its mutated, detoxified, vaccine candidate. <i> Foucault M, Mayol K, Receveur-Bréchot V, Bussat MC, Klinguer-Hamour C, Verrier B, Beck A, Haser R, Gouet P, Guillon C. </i> Proteins, 2010","reference_id":"20034112","region_id":"DP01087r023","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"An α-helix transition was observed for the wt-Tat133/14C12B5 Fab′ complexes, as indicated by the more pronounced minimum between 210 and 220 nm and by the shifting of the maximum toward 195 nm of the experimentally observed spectrum compared with the corresponding theoretical average curve [Fig. 7(A)].","_id":"685af523b4ac24d5329d8b37"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T10:39:05.325Z","_id":"685af523b4ac24d5329d8b38"},"version":5,"_id":"685af523b4ac24d5329d8b36","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":101,"interaction_partner":[],"reference_html":"UV and X-ray structural studies of a 101-residue long Tat protein from a HIV-1 primary isolate and of its mutated, detoxified, vaccine candidate. <i> Foucault M, Mayol K, Receveur-Bréchot V, Bussat MC, Klinguer-Hamour C, Verrier B, Beck A, Haser R, Gouet P, Guillon C. </i> Proteins, 2010","reference_id":"20034112","region_id":"DP01087r024","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As shown in Figure 6(B), the emission spectra of WT-Tat in water or in 6M urea are identical, with a maximal emission wavelength at ∼347 nm characteristic of a tryptophan in an aqueous environment,63 confirming that the region around Trp11 is natively unfolded.","_id":"685af523b4ac24d5329d8b3a"},{"type":"Discussion","text":"Our fluorescence emission experiments showed that the peak of fluorescence of Tat alone at ∼347 nm is close to the location of the peak of a fully accessible tryptophan.63 Moreover, the fluorescence did not display any shift when Tat was placed in a denaturing environment (6M urea). This confirms that Tat is natively unfolded and suggests that, in the native conformation of Tat, the only tryptophan of Tat (Trp11) is not involved in a putative hydrophobic pocket contrarily to what has been suggested by others studies.","_id":"685af523b4ac24d5329d8b3b"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T09:31:52.652Z","_id":"685af523b4ac24d5329d8b3c"},"version":1,"_id":"685af523b4ac24d5329d8b39","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"The results of such an experiment are shown in Fig. 5A,\nwhere upon electroporation of K50A or K51A with reporter\nHIV-LTR CAT, we observed a slight drop in transcriptional\nactivity (less than 50%, compare lanes 3±6).","_id":"685af523b4ac24d5329d8b57"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys50Ala","_id":"685af523b4ac24d5329d8b56"},{"start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"The results of such an experiment are shown in Fig. 5A,\nwhere upon electroporation of K50A or K51A with reporter\nHIV-LTR CAT, we observed a slight drop in transcriptional\nactivity (less than 50%, compare lanes 3±6).","_id":"685af523b4ac24d5329d8b59"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys51Ala","_id":"685af523b4ac24d5329d8b58"}],"cross_refs":[],"curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","date":"2024-02-12T14:47:30.071Z","disprot_namespace":"Disorder function","ec_id":"ECO:0007014","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","ec_ontology":"ECO","start":48,"end":52,"interaction_partner":[],"reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","reference_id":"11080476","region_id":"DP01087r028","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"The results of such an experiment are shown in Fig. 5A, where upon electroporation of K50A or K51A with reporter HIV-LTR CAT, we observed a slight drop in transcriptional activity (less than 50%, compare lanes 3±6).","_id":"685af523b4ac24d5329d8b5a"},{"type":"Results","text":"However, a more pronounced drop in transactivation was observed with the double-mutant 50 and 51 (~5-fold, lanes 7 and 8).","_id":"685af523b4ac24d5329d8b5b"},{"type":"Results","text":"The results in Fig. 5C indicate that only lysine residues and not alanine or\narginine substitutions at positions 50 and 51 are critical for the observed acetylation effect. Taken together, the transient transfection results indicate that neither K50 nor K51 mutations alone are sufficient to completely lose the Tat transactivation on HIV-1 LTR.","_id":"685af523b4ac24d5329d8b5c"},{"type":"Curator statement","text":"The authors describe an HIV-1 subtype B Tat protein that is 101 residues long (UniProtKB:P20879; DisProt:DP03560). However, since the residues Lys50 and Lys51 is in the identical IDR (100%), it is considered to be involved in the same function.","_id":"685af523b4ac24d5329d8b5d"}],"states_connection":[],"term_comment":"Usage guidance: transcription regulator activators bind to a transcription regulator to allow it to reach the chromatin or to contact other transcriptional regulators. This activity does not occur at the promoter. For activities that do occur at the promoter, consider GO:0001216 ; DNA-binding transcription activator activity or GO:0003713; transcription coactivator activity; those activities respectively bind DNA themselves or positively regulate a transcription regulator when it is located at the chromatin.","term_def":"\"A molecular function regulator that increases the activity of a transcription regulator via direct binding and/or post-translational modification.\" [PMID:9597751]","term_id":"GO:0140537","term_is_obsolete":false,"term_name":"transcription regulator activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2024-04-30T15:14:08.599Z","_id":"685af523b4ac24d5329d8b5e"},"version":0,"_id":"685af523b4ac24d5329d8b55","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-04-30T15:40:25.584Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001807","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","ec_ontology":"ECO","start":41,"end":54,"interaction_partner":[{"db":"RNAcentral","id":"URS00006B18E8_388826","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8b66"}],"reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","reference_id":"11080476","region_id":"DP01087r030","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"The results of such an experiment are shown in Fig. 3A, where wild-type peptide 41-54 was capable of binding to TAR RNA (lane 3).","_id":"685af523b4ac24d5329d8b67"},{"type":"Curator statement","text":"While the authors describe a different HIV-1 Tat protein (subtype B), this region is considered to be involved in the same function, since the region sequence is identical.","_id":"685af523b4ac24d5329d8b68"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a trans-activation response (TAR) element, a hairpin RNA structure located at the 5' end of all HIV-1 transcripts, and which is required for trans-activation of a viral promoter.\" [GOC:bf, GOC:PARL, PMID:25116364, Wikipedia:Trans-activation_response_element_(TAR)]","term_id":"GO:1990970","term_is_obsolete":false,"term_name":"trans-activation response element binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d8b65","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-04-30T15:49:03.390Z","disprot_namespace":"Disorder function","ec_id":"ECO:0001254","ec_name":"radioisotope assay evidence used in manual assertion","ec_ontology":"ECO","start":41,"end":54,"interaction_partner":[],"reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","reference_id":"11080476","region_id":"DP01087r031","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"The results of such an experiment are shown in Fig. 1C, where Tat 41-54\npeptide, but not 41-50 peptide (lanes 7±10), was acetylated with GST-HAT.","_id":"685af523b4ac24d5329d8b6a"},{"type":"Curator statement","text":"While the authors describe a different HIV-1 Tat protein (subtype B), this region is considered to be involved in the same function, since the region sequence is identical.","_id":"685af523b4ac24d5329d8b6b"}],"states_connection":[],"term_id":"IDPO:0000039","term_name":"acetylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d8b69","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":50,"end":50,"statements":[],"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d8b6d"},{"start":51,"end":51,"statements":[],"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d8b6e"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-04-30T16:09:18.486Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0007009","ec_name":"radioligand binding assay evidence used in manual assertion","ec_ontology":"ECO","start":41,"end":54,"interaction_partner":[{"db":"RNAcentral","id":"URS00006B18E8_388826","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8b71"}],"reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","reference_id":"11080476","region_id":"DP01087r032","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"The results of such an experiment are shown in Fig. 3A, where wild-type peptide 41-54 was capable of binding to TAR RNA (lane 3). The TAR RNA binding is completely abolished when lysines 50 and 51 are acetylated (lanes 6 and 7). We observed no binding of double-acetylated 50 and 51 peptide to TAR RNA at any peptide concentration (data not shown). Similar results were also observed when Tat protein was acetylated with GST-HAT prior to TAR RNA binding (Fig. 3B, lanes 4 and 5).","_id":"685af523b4ac24d5329d8b6f"},{"type":"Curator statement","text":"While the authors describe a different HIV-1 Tat protein (subtype B), this region is considered to be involved in the same function, since the region sequence is identical.","_id":"685af523b4ac24d5329d8b70"}],"states_connection":[],"term_comment":"","term_def":"\"Any process that stops, prevents or reduces the frequency, rate or extent of RNA binding.\" [GO_REF:0000059, GOC:bf, GOC:PARL, GOC:TermGenie]","term_id":"GO:1905215","term_is_obsolete":false,"term_name":"negative regulation of RNA binding","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d8b6c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Results","text":"We decided to address this question by utilizing affinity pull-down experiments using wild-type or acetylated 42-54 peptides coupled to a biotin moiety.","_id":"685af523b4ac24d5329d8b74"}],"term_id":"MI:0239","term_name":"biotin","term_namespace":"Tag","_id":"685af523b4ac24d5329d8b73"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-04-30T17:55:09.498Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006077","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","ec_ontology":"ECO","start":42,"end":54,"interaction_partner":[{"db":"UniProt","id":"Q92793","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8b75"}],"reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","reference_id":"11080476","region_id":"DP01087r033","released":"2024_06","sample":[],"statement":[{"type":"Curator statement","text":"While the authors describe a different HIV-1 Tat protein (subtype B), this region is considered to be involved in the same function, since the region sequence is identical.","_id":"685af523b4ac24d5329d8b76"},{"type":"Results","text":"The results of such an experiment are shown in Fig. 7A, where 35Slabeled TBP, CBP, and cyclin T could efficiently bind to wild-type but not acetylated 42-50 peptide.","_id":"685af523b4ac24d5329d8b77"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a transcription coactivator, a protein involved in positive regulation of transcription via protein-protein interactions with transcription factors and other proteins that positively regulate transcription. Transcription coactivators do not bind DNA directly, but rather mediate protein-protein interactions between activating transcription factors and the basal transcription machinery.\" [GOC:krc]","term_id":"GO:0001223","term_is_obsolete":false,"term_name":"transcription coactivator binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d8b72","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Results","text":"We decided to address this question by utilizing affinity pull-down experiments using wild-type or acetylated 42-54 peptides coupled to a biotin moiety.","_id":"685af523b4ac24d5329d8b7a"}],"term_id":"MI:0239","term_name":"biotin","term_namespace":"Tag","_id":"685af523b4ac24d5329d8b79"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-04-30T17:54:41.764Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006077","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","ec_ontology":"ECO","start":42,"end":54,"interaction_partner":[{"db":"UniProt","id":"O60563","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8b7b"},{"db":"UniProt","id":"Q92793","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8b7c"},{"db":"UniProt","id":"P20226","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8b7d"}],"reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","reference_id":"11080476","region_id":"DP01087r034","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"The results of such an experiment are shown in Fig. 7A, where 35Slabeled TBP, CBP, and cyclin T could efficiently bind to wild-type but not acetylated 42-50 peptide.","_id":"685af523b4ac24d5329d8b7e"},{"type":"Curator statement","text":"While the authors describe a different HIV-1 Tat protein (subtype B), this region is considered to be involved in the same function, since the region sequence is identical.","_id":"685af523b4ac24d5329d8b7f"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d8b78","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Results","text":"We decided to address this question by utilizing affinity pull-down experiments using wild-type or acetylated 42-54 peptides coupled to a biotin moiety.","_id":"685af523b4ac24d5329d8b82"}],"term_id":"MI:0239","term_name":"biotin","term_namespace":"Tag","_id":"685af523b4ac24d5329d8b81"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-04-30T17:56:24.744Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006077","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","ec_ontology":"ECO","start":42,"end":54,"interaction_partner":[{"db":"UniProt","id":"O60563","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8b83"}],"reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","reference_id":"11080476","region_id":"DP01087r035","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"The results of such an experiment are shown in Fig. 7A, where 35Slabeled TBP, CBP, and cyclin T could efficiently bind to wild-type but not acetylated 42-50 peptide.","_id":"685af523b4ac24d5329d8b84"},{"type":"Curator statement","text":"While the authors describe a different HIV-1 Tat protein (subtype B), this region is considered to be involved in the same function, since the region sequence is identical.","_id":"685af523b4ac24d5329d8b85"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to cyclins, proteins whose levels in a cell varies markedly during the cell cycle, rising steadily until mitosis, then falling abruptly to zero. As cyclins reach a threshold level, they are thought to drive cells into G2 phase and thus to mitosis.\" [GOC:ai]","term_id":"GO:0030332","term_is_obsolete":false,"term_name":"cyclin binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d8b80","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Results","text":"We decided to address this question by utilizing affinity pull-down experiments using wild-type or acetylated 42-54 peptides coupled to a biotin moiety.","_id":"685af523b4ac24d5329d8b88"}],"term_id":"MI:0239","term_name":"biotin","term_namespace":"Tag","_id":"685af523b4ac24d5329d8b87"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-04-30T18:09:19.906Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006077","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","ec_ontology":"ECO","start":42,"end":54,"interaction_partner":[{"db":"UniProt","id":"P24928","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8b89"}],"reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","reference_id":"11080476","region_id":"DP01087r036","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"Results from Western blots indicated that wild-type and not acetylated peptide was capable of binding to core-Pol II.","_id":"685af523b4ac24d5329d8b8a"},{"type":"Curator statement","text":"While the authors describe a different HIV-1 Tat protein (subtype B), this region is considered to be involved in the same function, since the region sequence is identical.","_id":"685af523b4ac24d5329d8b8b"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA polymerase core enzyme, containing a specific subunit composition defined as the core enzyme.\" [GOC:jl, GOC:txnOH]","term_id":"GO:0043175","term_is_obsolete":false,"term_name":"RNA polymerase core enzyme binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d8b86","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Results","text":"We decided to address this question by utilizing affinity pull-down experiments using wild-type or acetylated 42-54 peptides coupled to a biotin moiety.","_id":"685af523b4ac24d5329d8b8e"}],"term_id":"MI:0239","term_name":"biotin","term_namespace":"Tag","_id":"685af523b4ac24d5329d8b8d"},{"start":50,"end":50,"statements":[{"type":"Figure","text":"The synthesized Tat peptides (42-54) with or without acetylated lysines at positions 50 and 51 were labeled with biotin at the N- terminus.","_id":"685af523b4ac24d5329d8b90"}],"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d8b8f"},{"start":51,"end":51,"statements":[{"type":"Figure","text":"The synthesized Tat peptides (42-54) with or without acetylated lysines at positions 50 and 51 were labeled with biotin at the N- terminus.","_id":"685af523b4ac24d5329d8b92"}],"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d8b91"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-04-30T18:32:33.198Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006077","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","ec_ontology":"ECO","start":42,"end":54,"interaction_partner":[{"db":"UniProt","id":"P62805","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8b93"},{"db":"UniProt","id":"Q6NXT2","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8b94"},{"db":"UniProt","id":"Q6FI13","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8b95"},{"db":"UniProt","id":"P06899","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8b96"}],"reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","reference_id":"11080476","region_id":"DP01087r037","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"The results of such an experiment are shown in Fig. 7B, where acetylated Tat peptide was able to bind to core histones. It is interesting to note that core histones in the absence of DNA did not bind to acetylated Tat, indicating that a fixed conformation of nucleosome is required for Tat to bind to core histones.","_id":"685af523b4ac24d5329d8b97"},{"type":"Curator statement","text":"While the authors describe a different HIV-1 Tat protein (subtype B), this region is considered to be involved in the same function, since the region sequence is identical.","_id":"685af523b4ac24d5329d8b98"},{"type":"Curator statement","text":"Experiments show that the wild-type not acetylated peptide also binds nucleosomes but in a lesser degree.","_id":"685af523b4ac24d5329d8b99"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a nucleosome, a complex comprised of DNA wound around a multisubunit core and associated proteins, which forms the primary packing unit of DNA into higher order structures.\" [GOC:mah]","term_id":"GO:0031491","term_is_obsolete":false,"term_name":"nucleosome binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d8b8c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Methods","text":"Glutathione S-transferase (GST), GST-Tat, and GST-Tat mutants were prepared as already described (11).","_id":"685af523b4ac24d5329d8ba0"}],"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","_id":"685af523b4ac24d5329d8b9f"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-05-06T13:54:31.910Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006030","ec_name":"co-immunoprecipitation evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":101,"interaction_partner":[{"db":"UniProt","id":"Q09472","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8b9b"},{"db":"UniProt","id":"Q92793","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8b9c"}],"reference_html":"HIV-1 tat transactivator recruits p300 and CREB-binding protein histone acetyltransferases to the viral promoter. <i> Marzio G, Tyagi M, Gutierrez MI, Giacca M. </i> Proc Natl Acad Sci U S A, 1998","reference_id":"9811832","region_id":"DP01087r038","released":"2024_06","sample":[{"db":"Cellosaurus","deviation":null,"entry_name":"HeLa-HL3T1","id":"CVCL_8232","statements":[],"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_id":"UO:0000201","unit_name":"cells/ml","value":null,"_id":"685af523b4ac24d5329d8b9d"}],"statement":[{"type":"Results","text":"Immunoprecipitation with an anti-CBP or an anti-p300 antibody resulted in the coimmunoprecipitation of CBP or p300 as well as Tat in Tat- but not GST-treated cells. Accordingly, immunoprecipitation with an anti-Tat antibody recovered Tat as well as CBP and p300.","_id":"685af523b4ac24d5329d8b9e"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an histone acetyltransferase.\" [GOC:bf]","term_id":"GO:0035035","term_is_obsolete":false,"term_name":"histone acetyltransferase binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d8b9a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Methods","text":"Glutathione S-transferase (GST), GST-Tat, and GST-Tat mutants were prepared as already described (11).","_id":"685af523b4ac24d5329d8ba7"}],"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","_id":"685af523b4ac24d5329d8ba6"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-05-06T13:54:13.423Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006030","ec_name":"co-immunoprecipitation evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":101,"interaction_partner":[{"db":"UniProt","id":"Q09472","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8ba2"},{"db":"UniProt","id":"Q92793","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8ba3"}],"reference_html":"HIV-1 tat transactivator recruits p300 and CREB-binding protein histone acetyltransferases to the viral promoter. <i> Marzio G, Tyagi M, Gutierrez MI, Giacca M. </i> Proc Natl Acad Sci U S A, 1998","reference_id":"9811832","region_id":"DP01087r039","released":"2024_06","sample":[{"db":"Cellosaurus","deviation":null,"entry_name":"HeLa-HL3T1","id":"CVCL_8232","statements":[],"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_id":"UO:0000201","unit_name":"cells/ml","value":null,"_id":"685af523b4ac24d5329d8ba4"}],"statement":[{"type":"Results","text":"Immunoprecipitation with an anti-CBP or an anti-p300 antibody resulted in the coimmunoprecipitation of CBP or p300 as well as Tat in Tat- but not GST-treated cells. Accordingly, immunoprecipitation with an anti-Tat antibody recovered Tat as well as CBP and p300.","_id":"685af523b4ac24d5329d8ba5"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a transcription coactivator, a protein involved in positive regulation of transcription via protein-protein interactions with transcription factors and other proteins that positively regulate transcription. Transcription coactivators do not bind DNA directly, but rather mediate protein-protein interactions between activating transcription factors and the basal transcription machinery.\" [GOC:krc]","term_id":"GO:0001223","term_is_obsolete":false,"term_name":"transcription coactivator binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d8ba1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Methods","text":"Glutathione S-transferase (GST), GST-Tat, and GST-Tat mutants were prepared as already described (11).","_id":"685af523b4ac24d5329d8bad"}],"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","_id":"685af523b4ac24d5329d8bac"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-05-06T14:29:19.321Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005640","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":101,"interaction_partner":[{"db":"UniProt","id":"Q09472","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8baa"},{"db":"UniProt","id":"Q92793","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8bab"}],"reference_html":"HIV-1 tat transactivator recruits p300 and CREB-binding protein histone acetyltransferases to the viral promoter. <i> Marzio G, Tyagi M, Gutierrez MI, Giacca M. </i> Proc Natl Acad Sci U S A, 1998","reference_id":"9811832","region_id":"DP01087r040","released":"2024_06","sample":[],"statement":[{"type":"Results","text":"As shown in Fig. ​1c, wild-type 101 and 86 Tat proteins bound the HAT activity present in the nuclear extract with similar efficiencies.","_id":"685af523b4ac24d5329d8ba9"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an histone acetyltransferase.\" [GOC:bf]","term_id":"GO:0035035","term_is_obsolete":false,"term_name":"histone acetyltransferase binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d8ba8","reference_source":"pmid"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":101,"type":"T"}],"Structural state":[{"start":1,"end":101,"type":"D"}],"Structural transition":[{"start":1,"end":101,"type":"T"}],"Molecular function":[{"start":1,"end":101,"type":"F"}],"Disorder function":[{"start":41,"end":54,"type":"F"}],"Biological process":[{"start":41,"end":54,"type":"F"}]}},{"features":{"pfam":[{"id":"PF27999","name":"SEED MATURATION PROTEIN 1","start":1,"end":60}]},"uniref50":"UniRef50_A0A6J1C618","sequence":"MAKSKEDITYATSQARLSEDEAVRVAYEHGSPLEGGKIADSQPVDLFSSAHNMPKSGQTTMDSNTSDQSQMQRDTQEGGSKEFTTGAPG","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","fabids","Fabales","Fabaceae","Papilionoideae","50 kb inversion clade","NPAAA clade","indigoferoid/millettioid clade","Phaseoleae","Glycine","Glycine subgen. Soja"],"uniref90":"UniRef90_Q2XSH9","disprot_id":"DP01088","ncbi_taxon_id":3847,"regions_counter":7,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":89,"region_id":"DP01088r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Characterization of two soybean (Glycine max L.) LEA IV proteins by circular dichroism and Fourier transform infrared spectrometry. <i> Shih MD, Hsieh TY, Lin TP, Hsing YI, Hoekstra FA. </i> Plant Cell Physiol, 2010","term_id":"IDPO:0000004","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"20071374","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"pre-molten globule","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":89,"term_name":"protein folding chaperone","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"20071374","version":3,"reference_html":"Characterization of two soybean (Glycine max L.) LEA IV proteins by circular dichroism and Fourier transform infrared spectrometry. <i> Shih MD, Hsieh TY, Lin TP, Hsing YI, Hoekstra FA. </i> Plant Cell Physiol, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0044183","ec_id":"ECO:0006204","region_id":"DP01088r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":89,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"20071374","version":3,"reference_html":"Characterization of two soybean (Glycine max L.) LEA IV proteins by circular dichroism and Fourier transform infrared spectrometry. <i> Shih MD, Hsieh TY, Lin TP, Hsing YI, Hoekstra FA. </i> Plant Cell Physiol, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP01088r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":89,"region_id":"DP01088r004","released":"2022_03","ec_id":"ECO:0006228","reference_html":"Characterization of two soybean (Glycine max L.) LEA IV proteins by circular dichroism and Fourier transform infrared spectrometry. <i> Shih MD, Hsieh TY, Lin TP, Hsing YI, Hoekstra FA. </i> Plant Cell Physiol, 2010","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"20071374","version":2,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":89,"term_name":"protein folding chaperone","start":1,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"20071374","version":3,"reference_html":"Characterization of two soybean (Glycine max L.) LEA IV proteins by circular dichroism and Fourier transform infrared spectrometry. <i> Shih MD, Hsieh TY, Lin TP, Hsing YI, Hoekstra FA. </i> Plant Cell Physiol, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0044183","ec_id":"ECO:0006228","region_id":"DP01088r005","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":89,"term_name":"pre-molten globule to order","start":1,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"20071374","version":2,"reference_html":"Characterization of two soybean (Glycine max L.) LEA IV proteins by circular dichroism and Fourier transform infrared spectrometry. <i> Shih MD, Hsieh TY, Lin TP, Hsing YI, Hoekstra FA. </i> Plant Cell Physiol, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000013","ec_id":"ECO:0006228","region_id":"DP01088r006","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":89,"term_name":"protein binding","start":1,"ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"20071374","version":3,"reference_html":"Characterization of two soybean (Glycine max L.) LEA IV proteins by circular dichroism and Fourier transform infrared spectrometry. <i> Shih MD, Hsieh TY, Lin TP, Hsing YI, Hoekstra FA. </i> Plant Cell Physiol, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006228","region_id":"DP01088r007","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q2XSH9","date":"2016-09-19T09:45:23.000Z","acc":"Q9XES8","name":"Seed maturation protein PM28","length":89,"organism":"Glycine max","dataset":[],"UniParc":"UPI00000AAA2E","genes":[{"name":{"value":"PM28","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAD30427.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD30427.1"}}]},"synonyms":[{"value":"547536","evidences":[{"code":"ECO:0000313","source":{"name":"EnsemblPlants","id":"KRH43801","url":"http://www.ensemblgenomes.org/id/KRH43801"}}]}],"orfNames":[{"value":"GLYMA_08G172800","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"KRH43801.1","url":"https://www.ebi.ac.uk/ena/browser/view/KRH43801.1"}}]}]}],"alphafold_very_low_content":0.20224719101123595,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":89,"type":"T"}],"Structural state":[{"start":1,"end":89,"type":"D"}],"Molecular function":[{"start":1,"end":89,"type":"F"}],"Structural transition":[{"start":1,"end":89,"type":"T"}]}},{"features":{"pfam":[{"id":"PF02237","name":"Biotin protein ligase C terminal domain","start":218,"end":264},{"id":"PF03099","name":"Biotin/lipoate A/B protein ligase family","start":55,"end":147}],"gene3D":[{"start":219,"end":266,"id":"2.30.30.100","name":"2.30.30.100"},{"start":1,"end":218,"id":"3.30.930.10","name":"Bira Bifunctional Protein; Domain 2"}]},"uniref50":"UniRef50_I6YFP0","sequence":"MTDRDRLRPPLDERSLRDQLIGAGSGWRQLDVVAQTGSTNADLLARAASGADIDGVVLIAEHQTAGRGRHGRGWAATARAQIILSVGVRVVDVPVQAWGWLSLAAGLAVLDSVAPLIAVPPAETGLKWPNDVLARGGKLAGILAEVAQPFVVLGVGLNVTQAPEEVDPDATSLLDLGVAAPDRNRIASRLLRELEARIIQWRNANPQLAADYRARSLTIGSRVRVELPGGQDVVGIARDIDDQGRLCLDVGGRTVVVSAGDVVHLR","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"uniref90":"UniRef90_I6YFP0","disprot_id":"DP01091","ncbi_taxon_id":83331,"regions_counter":4,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":81,"region_id":"DP01091r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural ordering of disordered ligand-binding loops of biotin protein ligase into active conformations as a consequence of dehydration. <i> Gupta V, Gupta RK, Khare G, Salunke DM, Surolia A, Tyagi AK. </i> PLoS One, 2010","term_id":"IDPO:0000002","curator_id":"mnecci","start":60,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"20169168","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3L2Z"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":81,"term_name":"small molecule binding","start":60,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"20169168","version":3,"reference_html":"Structural ordering of disordered ligand-binding loops of biotin protein ligase into active conformations as a consequence of dehydration. <i> Gupta V, Gupta RK, Khare G, Salunke DM, Surolia A, Tyagi AK. </i> PLoS One, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0036094","ec_id":"ECO:0006220","region_id":"DP01091r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":172,"region_id":"DP01091r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural ordering of disordered ligand-binding loops of biotin protein ligase into active conformations as a consequence of dehydration. <i> Gupta V, Gupta RK, Khare G, Salunke DM, Surolia A, Tyagi AK. </i> PLoS One, 2010","term_id":"IDPO:0000002","curator_id":"mnecci","start":159,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"20169168","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3L2Z"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":172,"term_name":"small molecule binding","start":159,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"20169168","version":3,"reference_html":"Structural ordering of disordered ligand-binding loops of biotin protein ligase into active conformations as a consequence of dehydration. <i> Gupta V, Gupta RK, Khare G, Salunke DM, Surolia A, Tyagi AK. </i> PLoS One, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0036094","ec_id":"ECO:0006220","region_id":"DP01091r004","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_I6YFP0","date":"2016-09-19T10:43:25.000Z","acc":"P96884","name":"BirA bifunctional protein","length":266,"organism":"Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)","dataset":[],"UniParc":"UPI00000D0FC3","genes":[{"name":{"value":"birA","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAK47721.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAK47721.1"}}]},"olnNames":[{"value":"MT3379","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAK47721.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAK47721.1"}}]}]}],"alphafold_very_low_content":0,"disorder_content":0.13533834586466165,"disprot_consensus":{"full":[{"start":60,"end":81,"type":"D"},{"start":159,"end":172,"type":"D"}],"Structural state":[{"start":60,"end":81,"type":"D"},{"start":159,"end":172,"type":"D"}],"Molecular function":[{"start":60,"end":81,"type":"F"},{"start":159,"end":172,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04316","name":"Anti-sigma-28 factor, FlgM","start":35,"end":85}],"gene3D":[{"start":52,"end":88,"id":"G3DSA:1.10.287.1160"}]},"uniref50":"UniRef50_O66683","sequence":"MVNRIELSRLIGLLLETEKRKNTEQKESGTNKIEDKVTLSKIAQELSKNDVEEKDLEKKVKELKEKIEKGEYEVSDEKVVKGLIEFFT","taxonomy":["Bacteria","Aquificae","Aquificales","Aquificaceae","Aquifex"],"uniref90":"UniRef90_O66683","disprot_id":"DP01092","ncbi_taxon_id":224324,"regions_counter":6,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":88,"region_id":"DP01092r001","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Aquifex aeolicus FlgM protein exhibits a temperature-dependent disordered nature. <i> Molloy RG, Ma WK, Allen AC, Greenwood K, Bryan L, Sacora R, Williams L, Gage MJ. </i> Biochim Biophys Acta, 2010","term_id":"IDPO:0000003","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"20298817","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-08-23T19:25:41.137Z","reference_source":"pmid","term_name":"molten globule","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":20}],"statement":[{"text":"CD spectra were measured at 20 °C for both the S. typhimurium and A. aeolicus FlgM proteins in 10 mM sodium phosphate (pH 7.4). While the S. typhimurium FlgM protein exhibits disordered character, the A. aeolicus FlgM protein exhibits minima at 220 and 207 (Fig. 3A), consistent with significant α-helical character. ","type":"Results"},{"text":"The results presented thus far demonstrate that the A. aeolicus FlgM protein forms a molten-globule like structure with significant α-helical character at room temperature.","type":"Results"}]},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":17,"term_name":"disorder to order","start":1,"ec_name":"x-ray crystallography evidence used in manual assertion","curator_id":"vnugnes","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15068809","version":4,"reference_html":"Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation. <i> Sorenson MK, Ray SS, Darst SA. </i> Mol Cell, 2004","date":"2023-08-23T19:31:46.269Z","term_id":"IDPO:0000011","ec_id":"ECO:0005670","region_id":"DP01092r002","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Structural transition","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"1SC5"},{"db":"PDB","id":"1RP3"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O67268"}],"statement":[{"text":"In the A. aeolicus σ28/FlgM complex, most of the FlgM polypeptide is structured.","type":"Results"}]},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":88,"term_name":"protein binding","start":1,"ec_name":"x-ray crystallography evidence used in manual assertion","curator_id":"vnugnes","released":"2023_12","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"15068809","version":4,"reference_html":"Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation. <i> Sorenson MK, Ray SS, Darst SA. </i> Mol Cell, 2004","date":"2023-08-23T19:30:06.949Z","term_id":"GO:0005515","ec_id":"ECO:0005670","region_id":"DP01092r003","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"1SC5"},{"db":"PDB","id":"1RP3"}],"interaction_partner":[{"db":"UniProt","id":"O67268","operator":"and","partner_start":null,"partner_end":null}],"statement":[{"text":"In the packed conformation of σ28, the β′ coiled-coil binding determinant in σ282 is facing outwards but is directly occluded by H1′-H2′ of FlgM (Figure 4A).","type":"Results"}]},{"start":1,"end":88,"reference_id":"20298817","reference_source":"pmid","reference_html":"Aquifex aeolicus FlgM protein exhibits a temperature-dependent disordered nature. <i> Molloy RG, Ma WK, Allen AC, Greenwood K, Bryan L, Sacora R, Williams L, Gage MJ. </i> Biochim Biophys Acta, 2010","date":"2023-08-23T19:25:33.075Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000018","term_name":"disorder to molten globule","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01092r004","statement":[{"text":"The results presented thus far demonstrate that the A. aeolicus FlgM protein forms a molten-globule like structure with significant α-helical character at room temperature. However, there is a 23% decrease in α-helical character upon heating the sample to physiological temperature for A. aeolicus (85 °C), suggesting that some regions of the protein become more disordered at higher temperature.","type":"Results"},{"text":"Taken together, our results demonstrate that the A. aeolicus FlgM exhibits a molten globular-like state at lower temperatures, in contrast to the extended-disordered nature observed for the S. typhimurium FlgM, consistent with disorder predictions. However, the A. aeolicus FlgM converts to an extended-disordered structure as the temperature approaches physiological temperature for A. aeolicus. ","type":"Results"}],"states_connection":[{"source":"DP01092r005","target":"DP01092r001"}]},{"start":1,"end":88,"reference_id":"20298817","reference_source":"pmid","reference_html":"Aquifex aeolicus FlgM protein exhibits a temperature-dependent disordered nature. <i> Molloy RG, Ma WK, Allen AC, Greenwood K, Bryan L, Sacora R, Williams L, Gage MJ. </i> Biochim Biophys Acta, 2010","date":"2023-08-23T19:25:26.471Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":85}],"region_id":"DP01092r005","statement":[{"text":"However, there is a 23% decrease in α-helical character upon heating the sample to physiological temperature for A. aeolicus (85 °C), suggesting that some regions of the protein become more disordered at higher temperature.","type":"Results"},{"text":"However, the A. aeolicus FlgM converts to an extended-disordered structure as the temperature approaches physiological temperature for A. aeolicus. ","type":"Results"}]},{"start":30,"end":88,"reference_id":"15068809","reference_source":"pmid","reference_html":"Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation. <i> Sorenson MK, Ray SS, Darst SA. </i> Mol Cell, 2004","date":"2023-08-23T19:33:38.866Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1SC5"},{"db":"PDB","id":"1RP3"}],"region_id":"DP01092r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O67268"}],"statement":[{"text":"In the A. aeolicus σ28/FlgM complex, most of the FlgM polypeptide is structured.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_O66683","date":"2016-09-19T11:01:41.000Z","acc":"O66683","name":"Anti sigma factor FlgM","length":88,"organism":"Aquifex aeolicus (strain VF5)","dataset":[],"UniParc":"UPI0000056326","genes":[{"name":{"value":"flgM","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAC06641.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAC06641.1"}}]},"orfNames":[{"value":"aq_357a","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAC06641.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAC06641.1"}}]}]}],"alphafold_very_low_content":0.06818181818181818,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":88,"type":"T"}],"Structural state":[{"start":1,"end":88,"type":"D"}],"Structural transition":[{"start":1,"end":88,"type":"T"}],"Molecular function":[{"start":1,"end":88,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00685","name":"Sulfotransferase domain","start":6,"end":218}],"gene3D":[{"start":91,"end":284,"id":"1.25.40.460","name":"1.25.40.460"}]},"uniref50":"UniRef50_Q8KLM3","sequence":"MNGIRWIASYPKAGNTWVRCMLAAYITGKAPQVWNDIDAESLTLEAMLRFGDLPPAEPMEPVLVKTHLKADVPVLGLYGEATAKVLYLVRNPRDMLLSSMRMASISRDDVEKSRDFARKFIANEGLGWNALGAGGGVGLGSWPENVRSWTESSSDRFPNADVLTMRYEDLKGDPVARFSEIVEFLDLGGPVDIEDIRRAVAASTLERMRELEKRSEQQGGGSPIRHGDARMMKGGPGGARPQFVGEGRYDQSLSFLGEDIESDYQELLHGDSGFALYAKQYGYAG","taxonomy":["Bacteria","environmental samples"],"uniref90":"UniRef90_B7T1D7","disprot_id":"DP01093","ncbi_taxon_id":164851,"regions_counter":6,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":137,"region_id":"DP01093r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structures of the glycopeptide sulfotransferase Teg12 in a complex with the teicoplanin aglycone. <i> Bick MJ, Banik JJ, Darst SA, Brady SF. </i> Biochemistry, 2010","term_id":"IDPO:0000002","curator_id":"mnecci","start":127,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"20361791","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3MG9"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":137,"term_name":"flexible linker","start":127,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"20361791","version":3,"reference_html":"Crystal structures of the glycopeptide sulfotransferase Teg12 in a complex with the teicoplanin aglycone. <i> Bick MJ, Banik JJ, Darst SA, Brady SF. </i> Biochemistry, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006220","region_id":"DP01093r004","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":250,"region_id":"DP01093r005","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structures of the glycopeptide sulfotransferase Teg12 in a complex with the teicoplanin aglycone. <i> Bick MJ, Banik JJ, Darst SA, Brady SF. </i> Biochemistry, 2010","term_id":"IDPO:0000002","curator_id":"mnecci","start":216,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"20361791","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3MG9"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":250,"term_name":"flexible linker","start":216,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"20361791","version":3,"reference_html":"Crystal structures of the glycopeptide sulfotransferase Teg12 in a complex with the teicoplanin aglycone. <i> Bick MJ, Banik JJ, Darst SA, Brady SF. </i> Biochemistry, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006220","region_id":"DP01093r006","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_B7T1D7","date":"2016-09-19T11:31:04.000Z","acc":"B7T1D7","name":"Teg12","length":285,"organism":"uncultured soil bacterium","dataset":[],"UniParc":"UPI000188D9A3","genes":[{"name":{"value":"teg12","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ACJ60995.1","url":"https://www.ebi.ac.uk/ena/browser/view/ACJ60995.1"}}]}}],"alphafold_very_low_content":0.05964912280701754,"disorder_content":0.16140350877192983,"disprot_consensus":{"full":[{"start":127,"end":137,"type":"D"},{"start":216,"end":250,"type":"D"}],"Structural state":[{"start":127,"end":137,"type":"D"},{"start":216,"end":250,"type":"D"}],"Disorder function":[{"start":127,"end":137,"type":"F"},{"start":216,"end":250,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_Q9BP37","sequence":"MTYMCSILICLVLILCARGAEADDNGNYGNGMASVRTQGNTYDDLASLISYLTRHSFRRPFHECALCYSITDPGERQRCIDMYCSYTN","taxonomy":["Eukaryota","Metazoa","Spiralia","Lophotrochozoa","Mollusca","Gastropoda","Vetigastropoda","Lepetellida","Haliotoidea","Haliotidae","Haliotis"],"uniref90":"UniRef90_Q9BP37","disprot_id":"DP01094","ncbi_taxon_id":6454,"regions_counter":14,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":52,"region_id":"DP01094r001","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Characterization of two molluscan crystal-modulating biomineralization proteins and identification of putative mineral binding domains. <i> Michenfelder M, Fu G, Lawrence C, Weaver JC, Wustman BA, Taranto L, Evans JS, Morse DE. </i> Biopolymers, 2003","term_id":"IDPO:0000002","curator_id":"vnugnes","start":23,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"14648763","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-11-22T13:36:43.118Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"These results indicate that both the AP7-1 and AP24-1 model polypeptides do not possess significant percentages of either α-helix or β-strand secondary structure, but adopt random coil or extended conformations in solution, consistent with the structural features observed for other calcium carbonate mineral binding sequences.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":52,"region_id":"DP01094r004","released":"2023_12","ec_id":"ECO:0006198","reference_html":"Structural characterization of the N-terminal mineral modification domains from the molluscan crystal-modulating biomineralization proteins, AP7 and AP24. <i> Wustman BA, Morse DE, Evans JS. </i> Biopolymers, 2004","term_id":"IDPO:0000002","curator_id":"vnugnes","start":23,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15222016","version":3,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2023-11-22T13:42:16.899Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"This suggests that AP7-1 adopts a open, unfolded conformation that features largely random coil-like and/or extended structure.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":88,"region_id":"DP01094r007","released":"2023_12","ec_id":"ECO:0006198","reference_html":"Identification and structural characterization of an unusual RING-like sequence within an extracellular biomineralization protein, AP7. <i> Collino S, Kim IW, Evans JS. </i> Biochemistry, 2008","term_id":"IDPO:0000002","curator_id":"vnugnes","start":53,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18298090","version":3,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2023-11-22T14:24:33.704Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The 11H PFG-NOESY spectra of this region suggest its disordered nature. 1H chemical shifts are confined in the region 8.0 to 8.6 ppm while for globular proteins, 1H chemical shifts usually spread out in the region 9.5 to 6.0 ppm.","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"2JYP"}]},{"start":53,"end":88,"reference_id":"18298090","reference_source":"pmid","reference_html":"Identification and structural characterization of an unusual RING-like sequence within an extracellular biomineralization protein, AP7. <i> Collino S, Kim IW, Evans JS. </i> Biochemistry, 2008","date":"2023-11-22T14:24:47.196Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008270","term_name":"zinc ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001588","ec_ontology":"ECO","ec_name":"ion trap mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"29105","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01094r012","statement":[{"text":"This C-terminal sequence can bind Zn (II), Co (II), and other multivalent metal ions (Figures 2 and3, and Table 1) in 1:1 and 2:1 metal ion:peptide stoichiometries, and the ligand coordination number for polypeptide:Zn (II) interaction is either mono, bi, or tridentate in nature.","type":"Discussion"}],"term_comment":"","term_def":"\"Binding to a zinc ion (Zn).\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":53,"end":88,"reference_id":"18298090","reference_source":"pmid","reference_html":"Identification and structural characterization of an unusual RING-like sequence within an extracellular biomineralization protein, AP7. <i> Collino S, Kim IW, Evans JS. </i> Biochemistry, 2008","date":"2023-11-22T14:24:41.806Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001588","ec_ontology":"ECO","ec_name":"ion trap mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"48828","operator":null,"partner_start":null,"partner_end":null},{"db":"ChEBI","id":"49701","operator":"or","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"29108","operator":"or","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"49591","operator":"or","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"48775","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP01094r013","statement":[{"text":"This C-terminal sequence can bind Zn (II), Co (II), and other multivalent metal ions (Figures 2 and3, and Table 1) in 1:1 and 2:1 metal ion:peptide stoichiometries, and the ligand coordination number for polypeptide:Zn (II) interaction is either mono, bi, or tridentate in nature.","type":"Discussion"}],"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":23,"end":88,"reference_id":"18298090","reference_source":"pmid","reference_html":"Identification and structural characterization of an unusual RING-like sequence within an extracellular biomineralization protein, AP7. <i> Collino S, Kim IW, Evans JS. </i> Biochemistry, 2008","date":"2023-11-22T14:42:59.034Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051260","term_name":"protein homooligomerization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":4},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":5},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":6},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":8},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":9}],"ec_go":"EXP","region_id":"DP01094r014","statement":[{"text":"In summary, we find that under nonreducing conditions, AP7 is monomeric at pH 10 and exists as a high-molecular mass oligomer from pH 4 to 9 in solution.","type":"Results"}],"term_comment":"","term_def":"\"The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_Q9BP37","date":"2016-09-19T12:00:11.000Z","acc":"Q9BP37","name":"Aragonite protein AP7","length":88,"organism":"Haliotis rufescens","dataset":["Extracellular matrix proteins","Condensates-related proteins"],"UniParc":"UPI000007D9A1","genes":[],"alphafold_very_low_content":0.3068181818181818,"disorder_content":0.75,"disprot_consensus":{"full":[{"start":23,"end":88,"type":"D"}],"Structural state":[{"start":23,"end":88,"type":"D"}],"Molecular function":[{"start":53,"end":88,"type":"F"}],"Biological process":[{"start":23,"end":88,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_Q9BP38","sequence":"MTWMKMFYLTLAVTAAVLLVTVAAADDDEDASSGLCNQYNQNVTTRPNNKPKMFLRKNINFEIISVHNIWRDPNTVYWCDFSLEEEDGIKHWRHYDFNATHWWVEKGCSGTFVVEECNTKDITNPGPRSTAGKSPMQGTLAAPKPVANWMSIMSRSRFDMGTWDKEGFNML","taxonomy":["Eukaryota","Metazoa","Spiralia","Lophotrochozoa","Mollusca","Gastropoda","Vetigastropoda","Lepetellida","Haliotoidea","Haliotidae","Haliotis"],"uniref90":"UniRef90_Q9BP38","disprot_id":"DP01095","ncbi_taxon_id":6454,"regions_counter":6,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":54,"region_id":"DP01095r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Characterization of two molluscan crystal-modulating biomineralization proteins and identification of putative mineral binding domains. <i> Michenfelder M, Fu G, Lawrence C, Weaver JC, Wustman BA, Taranto L, Evans JS, Morse DE. </i> Biopolymers, 2003","term_id":"IDPO:0000002","curator_id":"mnecci","start":25,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"14648763","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":54,"term_name":"glycosylation display site","start":25,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"14648763","version":2,"reference_html":"Characterization of two molluscan crystal-modulating biomineralization proteins and identification of putative mineral binding domains. <i> Michenfelder M, Fu G, Lawrence C, Weaver JC, Wustman BA, Taranto L, Evans JS, Morse DE. </i> Biopolymers, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000041","ec_id":"ECO:0006204","region_id":"DP01095r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":54,"term_name":"ion binding","start":25,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"14648763","version":3,"reference_html":"Characterization of two molluscan crystal-modulating biomineralization proteins and identification of putative mineral binding domains. <i> Michenfelder M, Fu G, Lawrence C, Weaver JC, Wustman BA, Taranto L, Evans JS, Morse DE. </i> Biopolymers, 2003","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0043167","ec_id":"ECO:0006204","region_id":"DP01095r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":54,"region_id":"DP01095r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural characterization of the N-terminal mineral modification domains from the molluscan crystal-modulating biomineralization proteins, AP7 and AP24. <i> Wustman BA, Morse DE, Evans JS. </i> Biopolymers, 2004","term_id":"IDPO:0000003","curator_id":"mnecci","start":25,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15222016","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"molten globule","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":54,"term_name":"glycosylation display site","start":25,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"15222016","version":2,"reference_html":"Structural characterization of the N-terminal mineral modification domains from the molluscan crystal-modulating biomineralization proteins, AP7 and AP24. <i> Wustman BA, Morse DE, Evans JS. </i> Biopolymers, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000041","ec_id":"ECO:0006165","region_id":"DP01095r005","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":54,"term_name":"ion binding","start":25,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"15222016","version":3,"reference_html":"Structural characterization of the N-terminal mineral modification domains from the molluscan crystal-modulating biomineralization proteins, AP7 and AP24. <i> Wustman BA, Morse DE, Evans JS. </i> Biopolymers, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0043167","ec_id":"ECO:0006165","region_id":"DP01095r006","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q9BP38","date":"2016-09-19T14:26:05.000Z","acc":"Q9BP38","name":"Aragonite protein AP24","length":171,"organism":"Haliotis rufescens","dataset":[],"UniParc":"UPI000007F864","genes":[],"alphafold_very_low_content":0.4678362573099415,"disorder_content":0.17543859649122806,"disprot_consensus":{"full":[{"start":25,"end":54,"type":"D"}],"Structural state":[{"start":25,"end":54,"type":"D"}],"Disorder function":[{"start":25,"end":54,"type":"F"}],"Molecular function":[{"start":25,"end":54,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03011","name":"PFEMP1 DBL domain","start":585,"end":741},{"id":"PF03011","name":"PFEMP1 DBL domain","start":1460,"end":1610},{"id":"PF05424","name":"Duffy binding domain","start":112,"end":309},{"id":"PF05424","name":"Duffy binding domain","start":897,"end":1126},{"id":"PF05424","name":"Duffy binding domain","start":1749,"end":1936},{"id":"PF05424","name":"Duffy binding domain","start":2137,"end":2295},{"id":"PF15445","name":"acidic terminal segments, variant surface antigen of PfEMP1","start":2458,"end":2924},{"id":"PF15447","name":"N-terminal segments of PfEMP1","start":14,"end":50},{"id":"PF18562","name":"Cysteine-Rich Interdomain Region 1 gamma","start":1386,"end":1444},{"id":"PF22672","name":"Duffy-binding-like domain, C-terminal subdomain","start":313,"end":472},{"id":"PF22672","name":"Duffy-binding-like domain, C-terminal subdomain","start":1191,"end":1342},{"id":"PF22672","name":"Duffy-binding-like domain, C-terminal subdomain","start":1940,"end":2078}],"gene3D":[{"start":2101,"end":2278,"id":"1.20.1310.20","name":"Duffy-antigen binding domain"},{"start":1008,"end":1362,"id":"1.20.1310.20","name":"Duffy-antigen binding domain"},{"start":1657,"end":2100,"id":"1.20.1310.20","name":"Duffy-antigen binding domain"},{"start":6,"end":494,"id":"1.20.1310.20","name":"Duffy-antigen binding domain"},{"start":2279,"end":2406,"id":"1.20.58.830","name":"1.20.58.830"},{"start":1367,"end":1609,"id":"1.20.58.1930","name":"1.20.58.1930"},{"start":576,"end":754,"id":"1.20.58.830","name":"1.20.58.830"},{"start":2606,"end":2652,"id":"1.10.1900.40","name":"Acidic terminal segments, variant surface antigen of PfEMP1"},{"start":2708,"end":2784,"id":"1.10.1900.40","name":"Acidic terminal segments, variant surface antigen of PfEMP1"}]},"uniref50":"UniRef50_Q25733","sequence":"MGGGNGGGGTKDKDAKHALDRIGEEVYKEKVENDAEKYKKALKGNLQEAKGIGELASSPNPCKLVEDYYNNRLKRKRYPCANRQTVRFSDEYGGQCTFNRIKDSENNDNSIGACAPYRRLHLCDYNLEKMGKTSTTKHDLLLDVCMAAKYEGDSIKTHYTKHELTNPDTKSQLCTILARSFADIGDIVRGKDLYLGYDDKEKDERKKLENNLIEIFKKIHENLGTQDAKDHYKKDEENYYQLREDWWTANRSTVWKAITCHAGESDKYFRKTCCSGEWTDDKCRCKDEEGKNETNEVPTYFDYVPQYLRWFEEWAEDFCRKRKKKIENAIKNCRGEKGNERYCDLNGYNCEETARGAEIFVKGDDCHKCSVACDRFVKWIDNQRKEFDKQKKKYDEEINKTHGTTITTGNGKINNLYVGHFYKILKKYYPTVDKSLQKLNDEAICKKPPNVGNEKASTVDFNNEVNTTFSHTTYCEACPWCGAQKEKNGGGWKAKEKSCAKKKERIFNKENSTDIKILTPEKGRSKTLEKLKTFCKDGQKIKNDIWKCHYDDNGTDDQTDDSNDCVLGDWGNLTKEDKIMSYNAFFWMWVHDMLIDSIKWRDEHGRCINKDKGKTCIKGCNKKCICFQKWVEQKKTEWGKIKDHFRKQKDIPKDWTHDDFLQTLLMKDLLLEIIQDTYGDANEIKRIEALLEQAGVGGIDFAALAGLYTKGFVAEKDTTIDKLLQHEQKEADKCLKTHTDDTCPPQEDRSVARSESATVPSPPADPKATEEVDANASSDDEDDFEEEEEEEEDEGEEEAEEVQEEKTDESATEAVAPSPPGTTQDGVKPASQEDDVKVCSIVDKALKGKLDDACTLKYGKTAPTSWKCIPSGNNTTTESTTKPGAAGTPSGKDTGSICVPPRRRKLYVGKLHDWAGGETTEAKSQETSGGQKTPSGNESSPSEKLPQGPTPETTKETPESSLLHAFVSPPRLRRFLPWHKFKEQWKAQHGAGATGQQTIIGTLDGGGEETPDKLLKTGHIPPDFLRQMFYTLGDYRDILVGNTDIVVHTSGNKEDMQIMEAIQKKIEQILPTSGSSPSPPRVTQTQHSVENPRKTWWNENGKKIWEGMVCALTYNTDTPSGTAPTQIQEVRTKLRDENSKNPKIPQYKYDQVKLDDTSDAKTTGSPVPSGEKITPLTDFISRPPYFRYLEEWGETFCKERKKRLEKIKEECRGDRTGHEHCSGDGYDCTRTDADRNDKFVDLNCRDCHIQCRKYRKWIDIKFDEYHKQEKKYQGEYDKLTKDKSSGGDNNCCKDIEKHKSAAVFLKELKHCKNGQTSENKGNQEDQLNKLDFDKIPQTFSPSTYCKACPVYGVNCNGNKRGRGGTNGCTTNNEPENKENDKGAASTISILINDGSTNGATNGTTGTTDETLKECSDKYAFFKGLRKQEWTCQKKYGVNQCNLTNRVNDTYFDKDIVFNEFFQRWLRYFVHDYNILKHKIDPCIKKEKQDKTEHKCINGCNIKCECVRKWLEIKGNEWGNIKKHYNINSNDDKETIAYNVKSYFVDQGLFDTDYKKAQKVVEDEKERKKIWGCTGHDECSEKEKEENKNFITNLISELQDKITSCQNKHNPNGKTACDPFPSPTPEETDPLDDDTPDPLDDDQHTEQPKFCPPPPPPMTCVEKIAKELRVEAEGKINNELKGNGKDFNGKCNNVKKKNGAVIGEESCKFEQTYENSVNNINNKCKDNQNERFKIGQKWNFKYIGTIRKDLCIPPRREHMCLDDLSMLGRTTISDSSALLKKIQEAAKSERDDIIRKLLEQNSCDEHRICDAMKYSFADLGDIIRGRDLWNKNSKQKGLQKRLEYAFINIYNKLQNDKNKYEKDRPKYLQLRSDWWDANRKHIWNAMTCNAPDDAKFLKKNPNDTSGSSSSKGIMTTHSNCGYDKEPPDYDYIPQPFRWMQEWSESFCKLLNEEMEQFEKTCGECKKNSITCEDDRNGTNCENCKNQCEKYKKLIHNWKLGFDKYKEIYNEIYNNKDSKINSNEYFKKFLEKLKDKCKELNSSDKCIDEATHCTKYKFSNSENKNHNNYAFKNPPKEYEKACKCDAPDPLDNCPKDSATYEKACNTLLPTKLCESKTFNNDDDSWDTSFVQTSPRDNTGVLVPPRRRQICLKNITTKLRSIEKIDDFKAELMTSAYNEGKLLCELYKKDRDVTLQAMKYSFYDYGDIVKGTDLISTAPLDKLKTKLNVLLKGDGTNEIKEDRGKWWTENRTRVWHAMLCGYKAAGGKIEERDCSLPDDNTHQFLRWFREWSEHFCAKRQKLFNEVKRECASAQCIIEYGTIDPPVCEEACTQYRDYITRKIQEYRLLNYQYNTNFNEKKAEVTKAPEYFNDKCNDKCNCLSKYIDIEKKWKNMYDSFDDNDLKNKCICRQIKPKRPPKKVKPEEEHTPSEQDTPPPLPPKPDDLPPPAEEPFNRDILEKTIPFGIALALGSIAFLFLKKKTKSSVGNLFQILHIPKSDYDIPTKLSPNRYIPYTSGKYRGKRYIYLEGDSGTDSGYTDHYSDITSSSESEYEELDINDIYVPGSPKYKTLIEVVLEPSGNNTTASGKNTPSDTQNDIQNDGIPSSKITDNEWNTLKDEFISNMLQNEPNTEPNMLGYNVDNNTHPTTSRHNVEEKPFIMSIHDRDLYSGEEYSYNVNMVNNDIPISARNGNYSGIDLINDSLNSNKVDIYDELLKRKENELFGTNHTKKNTSTNSVAKNTNTDPIHNQLNLFHTWLDRHRDMCEKWDTNNKKEELLDKLKEEWNKDNNSGNINPSGNTPPTSDIPSGKQSDIPSDNNIHSDIPYVLNTDVSIQIHMDNPKPINEFSNMDTYPNNSSMDTILEDLDKPFNEPYYYDVQDDIYYDVHDHDTSTVDTNAMDEPSKVQIEMDVNTKLVKEKYPIADLWDI","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"uniref90":"UniRef90_Q25733","disprot_id":"DP01096","ncbi_taxon_id":5833,"regions_counter":3,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":618,"region_id":"DP01096r003","start":605,"term_id":"IDPO:0000002","statement":[{"text":"The first helix (H1) of the bundle is joined to the second helix (H2) through a disordered fourteen-residue loop.","type":"Results"},{"text":"The function of the disordered loop cannot be inferred from the experiments; however, deleting the loop and at least one adjacent helix abolished binding to the human CD36 receptor. The length of the loop is variable between various homologoues.","type":"Curator statement"}],"curator_id":"bmesza","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"18773118","version":2,"reference_html":"The cysteine-rich interdomain region from the highly variable plasmodium falciparum erythrocyte membrane protein-1 exhibits a conserved structure. <i> Klein MM, Gittis AG, Su HP, Makobongo MO, Moore JM, Singh S, Miller LH, Garboczi DN. </i> PLoS Pathog, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3C64"}],"term_name":"disorder","curator_orcid":"0000-0003-0919-4449","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"UniRef100_Q25733","date":"2016-09-19T15:06:02.000Z","acc":"Q25733","name":"PfEMP1 variant 1 of strain MC","length":2924,"organism":"Plasmodium falciparum","dataset":[],"UniParc":"UPI0000079077","genes":[{"name":{"value":"MCvar-1 PfEMP1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAB60251.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAB60251.1"}}]}}],"disorder_content":0.0047879616963064295,"disprot_consensus":{"full":[{"start":605,"end":618,"type":"D"}],"Structural state":[{"start":605,"end":618,"type":"D"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MSDNDDIEVESDADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"","disprot_id":"DP01097","ncbi_taxon_id":9606,"regions_counter":13,"creator":"mnecci","regions":[{"start":84,"end":151,"reference_id":"9115440","reference_source":"pmid","reference_html":"The crystal structure of an intact human Max-DNA complex: new insights into mechanisms of transcriptional control. <i> Brownlie P, Ceska T, Lamers M, Romier C, Stier G, Teo H, Suck D. </i> Structure, 1997","date":"2023-01-18T10:45:19.091Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2023_06","version":3,"region_id":"DP01097r013","statement":[{"text":"The X-ray crystal structure of the intact human Max protein homodimer in complex with a 13-mer DNA duplex was determined to 2.8 A resolution and refined to an R factor of 0.213. The C-terminal domains in both chains of the Max dimer are disordered.","type":"Abstract"},{"text":"The C-terminal domains in both chains of the Max dimer are disordered.","type":"Abstract"},{"text":"The disorder observed in the C-terminal domain suggests that contacts with additional protein components of the transcription machinery are necessary for ordering the secondary structure.","type":"Abstract"},{"text":"Although p21 Max is present in the crystals in its entirety, together with the 13 base pair duplex of DNA, in our crystals a large part of the C terminus is disordered. The present model includes residues 3–82 and 10–82 in monomers A and B, respectively.","type":"Results"},{"text":"Finally, regarding the C-terminal domain comprising residues 93–150, this entire region is disordered in the Max structure reported here.","type":"Results"},{"text":"The C-terminal domain following the leucine zipper is disordered in the crystal structure, suggesting that it is intrinsically flexible and that other components of the transcriptional machinery may be required for secondary structure formation.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-18T15:54:37.289Z"}}],"released":"2016_10","uniref100":"","date":"2016-09-20T11:12:12.000Z","acc":"P61244-2","name":"Isoform 2 of Protein max","length":151,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000012AF","genes":[{"name":{"value":"MAX","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6913","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6913"}}]},"synonyms":[{"value":"BHLHD4"}]}],"disorder_content":0.4503311258278146,"disprot_consensus":{"full":[{"start":84,"end":151,"type":"D"}],"Structural state":[{"start":84,"end":151,"type":"D"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MNINDLKLTLSKAGQEHLLRFWNELEEAQQVELYAELQAMNFEELNFFFQKAIEGFNQSSHQKNVDARMEPVPREVLGSATRDQDQLQAWESEGLFQISQNKVAVLLLAGGQGTRLGVAYPKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYYGNKCIIPWYIMTSGRTMESTKEFFTKHKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDMEQRGIWSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQVVEYSEISLATAQKRSSDGRLLFNAGNIANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPYVDTQGQLIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLKNADSQNGKDNPTTARHALMSLHHCWVLNAGGHFIDENGSRLPAIPRLKDANDVPIQCEISPLISYAGEGLESYVADKEFHAPLIIDENGVHELVKNGI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"","disprot_id":"DP01098","ncbi_taxon_id":9606,"regions_counter":2,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":68,"region_id":"DP01098r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture. <i> Peneff C, Ferrari P, Charrier V, Taburet Y, Monnier C, Zamboni V, Winter J, Harnois M, Fassy F, Bourne Y. </i> EMBO J, 2001","term_id":"IDPO:0000002","curator_id":"mnecci","start":54,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"11707391","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1JVD"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":68,"term_name":"flexible linker","start":54,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"11707391","version":3,"reference_html":"Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture. <i> Peneff C, Ferrari P, Charrier V, Taburet Y, Monnier C, Zamboni V, Winter J, Harnois M, Fassy F, Bourne Y. </i> EMBO J, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006220","region_id":"DP01098r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"","date":"2016-09-20T12:04:30.000Z","acc":"Q16222-2","name":"Isoform AGX1 of UDP-N-acetylhexosamine pyrophosphorylase","length":505,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000002B673","genes":[{"name":{"value":"UAP1"},"synonyms":[{"value":"SPAG2"}]}],"disorder_content":0.0297029702970297,"disprot_consensus":{"full":[{"start":54,"end":68,"type":"D"}],"Structural state":[{"start":54,"end":68,"type":"D"}],"Disorder function":[{"start":54,"end":68,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MASPPPFHSQKLPGEYFRYKGVPFPVGLYSLESISLAENTQDVRDDDIFIITYPKSGTTWMIEIICLILKEGDPSWIRSVPIWERAPWCETIVGAFSLPDQYSPRLMSSHLPIQIFTKAFFSSKAKVIYMGRNPRDVVVSLYHYSKIAGQLKDPGTPDQFLRDFLKGEVQFGSWFDHIKGWLRMKGKDNFLFITYEELQQDLQGSVERICGFLGRPLGKEALGSVVAHSTFSAMKANTMSNYTLLPPSLLDHRRGAFLRKGVCGDWKNHFTVAQSEAFDRAYRKQMRGMPTFPWDEDPEEDGSPDPEPSPEPEPKPSLEPNTSLEREPRPNSSPSPSPGQASETPHPRPS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"","disprot_id":"DP01099","ncbi_taxon_id":9606,"regions_counter":2,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":10,"region_id":"DP01099r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms. <i> Lee KA, Fuda H, Lee YC, Negishi M, Strott CA, Pedersen LC. </i> J Biol Chem, 2003","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12923182","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1Q20"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":350,"region_id":"DP01099r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms. <i> Lee KA, Fuda H, Lee YC, Negishi M, Strott CA, Pedersen LC. </i> J Biol Chem, 2003","term_id":"IDPO:0000002","curator_id":"mnecci","start":339,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12923182","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1Q20"}],"term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2016_10","uniref100":"","date":"2016-09-20T12:22:26.000Z","acc":"O00204-2","name":"Isoform 2 of Sulfotransferase 2B1","length":350,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000006DFE7","genes":[{"name":{"value":"SULT2B1"},"synonyms":[{"value":"HSST2"}]}],"disorder_content":0.06285714285714286,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"},{"start":339,"end":350,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":339,"end":350,"type":"D"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"","disprot_id":"DP01100","ncbi_taxon_id":9606,"regions_counter":53,"creator":"grivas","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":441,"region_id":"DP01100r001","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure. <i> Schweers O, Schönbrunn-Hanebeck E, Marx A, Mandelkow E. </i> J Biol Chem, 1994","term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"7929085","version":3,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"Again tau is clearly different from a globular protein (Fig. 3b, bottom), it has the characteristics of a denatured protein.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-11T19:58:55.601Z"}},{"start":1,"end":441,"reference_id":"14769047","reference_source":"pmid","reference_html":"Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on beta-structure in the core domain. <i> Barghorn S, Davies P, Mandelkow E. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01100r027","statement":[{"text":"Soluble proteins K19, K18-ΔK280, and full-length htau40-ΔK280 exhibit FTIR maxima around 1645−1646 cm-1, consistent with the CD experiments and the dominance of the random coil conformation [Figure 6A−C (dashed lines)].","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-22T14:50:59.519Z"}},{"start":1,"end":441,"reference_id":"14769047","reference_source":"pmid","reference_html":"Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on beta-structure in the core domain. <i> Barghorn S, Davies P, Mandelkow E. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01100r028","statement":[{"text":"The CD spectra change when tau is induced to aggregate into PHFs. Figure 4A−C (solid lines) shows the PHF spectra after separation from soluble tau by a clearing spin. For three-repeat construct K19, the minimum shifts toward a higher wavelength, indicating a transition to a higher β-sheet content (Figure 4A). This change is even more pronounced for the FTDP-17 mutant of four-repeat construct K18 (K18-ΔK280, Figure 4B), consistent with the strong tendency of this mutant to form PHFs due to an increased propensity for β-sheet formation (20, 23).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-22T14:51:30.014Z"}},{"start":1,"end":441,"reference_id":"14769047","reference_source":"pmid","reference_html":"Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on beta-structure in the core domain. <i> Barghorn S, Davies P, Mandelkow E. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01100r029","statement":[{"text":"Upon PHF polymerization, the spectra of the repeat constructs shift the maximum to ∼1629 and 1626 cm-1 [Figure 6A,B (solid lines)], indicating a shift toward a high β-structure content (55, 56).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-22T14:51:29.416Z"}},{"start":1,"end":441,"reference_id":"14769047","reference_source":"pmid","reference_html":"Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on beta-structure in the core domain. <i> Barghorn S, Davies P, Mandelkow E. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01100r032","statement":[{"text":"In all cases, the filaments were mainly of the paired helical type, had a typical length of 100−500 nm, were 10−25 nm wide, and had a crossover repeat of ∼80 nm (Figure 2, top panel). Thus, they showed all characteristics of “Alzheimer PHFs” (39, 40).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-22T14:51:28.060Z"}},{"start":1,"end":441,"reference_id":"14769047","reference_source":"pmid","reference_html":"Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on beta-structure in the core domain. <i> Barghorn S, Davies P, Mandelkow E. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01100r033","statement":[{"text":"In a Western blot analysis, the samples were probed with the polyclonal antibody K9JA that recognizes the repeat region and the C-terminus of tau. The pattern was comparable to that of the Coomassie-stained gel with regard to the three- to four-band pattern and the high- and low-Mr smear, showing that most of the protein (∼75% as measured by densitometric methods) in the Alzheimer PHF preparations was indeed tau (Figure 3B).","type":"Results"}],"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-22T14:51:21.280Z"}},{"start":1,"end":441,"reference_id":"14769047","reference_source":"pmid","reference_html":"Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on beta-structure in the core domain. <i> Barghorn S, Davies P, Mandelkow E. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01100r034","statement":[{"text":"In the SDS gel, the three individual Alzheimer PHFs all exhibited the typical three- to four-band appearance [bands at 55, 64, and 69 kDa and a minor fourth band (72−74 kDa) which contain the six human tau isoforms in a highly phosphorylated form (43−45)] (Figure 3A).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-22T14:51:14.696Z"}},{"start":1,"end":441,"reference_id":"7929085","reference_source":"pmid","reference_html":"Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure. <i> Schweers O, Schönbrunn-Hanebeck E, Marx A, Mandelkow E. </i> J Biol Chem, 1994","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000269","ec_ontology":"ECO","ec_name":"experimental evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01100r035","statement":[{"text":"Tau can be boiled and dissolved in dilute acids, and yet it does not lose its microtubule-assembly promoting activity (Fellous et al., 1977); this argues that overall chain folding is not very important for the interaction of tau with microtubules (although other less obvious functions may be affected by this treatment).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-11T19:31:14.625Z"}},{"start":1,"end":441,"reference_id":"7929085","reference_source":"pmid","reference_html":"Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure. <i> Schweers O, Schönbrunn-Hanebeck E, Marx A, Mandelkow E. </i> J Biol Chem, 1994","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006317","ec_ontology":"ECO","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01100r036","statement":[{"text":"Tau can be boiled and dissolved in dilute acids, and yet it does not lose its microtubule-assembly promoting activity (Fellous et al., 1977); this argues that overall chain folding is not very important for the interaction of tau with microtubules (although other less obvious functions may be affected by this treatment).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-11T19:31:14.364Z"}},{"start":1,"end":441,"reference_id":"7929085","reference_source":"pmid","reference_html":"Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure. <i> Schweers O, Schönbrunn-Hanebeck E, Marx A, Mandelkow E. </i> J Biol Chem, 1994","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007731","ec_ontology":"ECO","ec_name":"spectrometry evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01100r037","statement":[{"text":"Additional evidence for the apparent \"denatured\" state of tau comes from absorption spectroscopy (data not  shown). ","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-11T18:56:16.332Z"}},{"start":1,"end":441,"reference_id":"7929085","reference_source":"pmid","reference_html":"Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure. <i> Schweers O, Schönbrunn-Hanebeck E, Marx A, Mandelkow E. </i> J Biol Chem, 1994","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01100r038","statement":[{"text":"Tau is difficult to visualize in the electron microscope because of its low contrast (Zingsheim et al., 1979), but the glycerol-spray technique reveals the structure of an elongated and flexible rod, about 35 nm in length (Fig. 2, Wille et al. (1992)).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-11T19:59:07.901Z"}},{"start":1,"end":441,"reference_id":"7929085","reference_source":"pmid","reference_html":"Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure. <i> Schweers O, Schönbrunn-Hanebeck E, Marx A, Mandelkow E. </i> J Biol Chem, 1994","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0007062","ec_ontology":"ECO","ec_name":"light scattering evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01100r039","statement":[{"text":"Fig. 6, a and b, shows the wide and small angle pattern of pelleted microtubules. These structures can be oriented quite well by either of the above methods, but here we have chosen an example of rather poor orientation in order to facilitate the comparison with the PHF  pattern below (for an example of good orientation and its interpretation see Mandelkow et al. (1977) and Mandelkow (1986)).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-11T19:59:04.913Z"}},{"start":1,"end":441,"reference_id":"7929085","reference_source":"pmid","reference_html":"Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure. <i> Schweers O, Schönbrunn-Hanebeck E, Marx A, Mandelkow E. </i> J Biol Chem, 1994","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01100r040","statement":[{"text":"The amide I maxima between 1600 and 1700 cm\" arise from stretch vibrations of the amide carbonyl groups and vary depending on how the carbonyls are hydrogen bonded. Thus absorption maxima between 1617 and 1634 cm\" are characteristic for β-sheets while α-helices, turns, or random coils have maxima between 1645 and 1663 cm\" (Susi  and Byler,  1986).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-11T19:59:01.741Z"}},{"start":1,"end":441,"reference_id":"10805776","reference_source":"pmid","reference_html":"Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure. <i> von Bergen M, Friedhoff P, Biernat J, Heberle J, Mandelkow EM, Mandelkow E. </i> Proc Natl Acad Sci U S A, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01100r041","statement":[{"text":"All curves obtained for hτ23 show a minimum of around 200 nm, characteristic of largely random coil structures, which confirms our earlier observations (25).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-11T18:56:13.248Z"}},{"start":1,"end":441,"reference_id":"18771286","reference_source":"pmid","reference_html":"Domain conformation of tau protein studied by solution small-angle X-ray scattering. <i> Mylonas E, Hascher A, Bernadó P, Blackledge M, Mandelkow E, Svergun DI. </i> Biochemistry, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01100r042","statement":[{"text":"All the profiles are featureless, and the Kratky plots [s2I(s) vs s] are without apparent peaks (Supporting Information Figure 3), which is typical for unfolded proteins.","type":"Results"},{"text":"Table 1 indicates that the larger constructs (ht23 and ht40) have Rg values close to or smaller than the predicted random coil values, which are shown by ref 29 to agree well with the experimental data from chemically unfolded proteins (note that as tau constructs are not denatured using chemicals the random coil estimations cannot be considered ideal predictions, but they do provide a useful guidance).","type":"Results"},{"text":"For full length constructs (ht40 and ht23), little difference from the pool distribution was observed (typical models of ht40 selected from the random pools are displayed in Figure 4 to demonstrate that the protein is indeed rather unstructured).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-10T20:46:03.515Z"}}],"released":"2016_10","uniref100":"","date":"2016-09-20T12:39:36.000Z","acc":"P10636-8","name":"Isoform Tau-F of Microtubule-associated protein tau","length":441,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI000002D754","genes":[{"name":{"value":"MAPT","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6893","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6893"}}]},"synonyms":[{"value":"MAPTL"},{"value":"MTBT1"},{"value":"TAU"}]}],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":441,"type":"D"}],"Structural state":[{"start":1,"end":441,"type":"D"}],"Biological process":[{"start":1,"end":441,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MASQKRPSQRSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFSGDRGAPKRGSGKDSHTRTTHYGSLPQKSQHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKLGGRDSRSGSPMARR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"","disprot_id":"DP01101","ncbi_taxon_id":10090,"regions_counter":17,"creator":"ldobson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":169,"region_id":"DP01101r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Effects of the osmolyte trimethylamine-N-oxide on conformation, self-association, and two-dimensional crystallization of myelin basic protein. <i> Hill CM, Bates IR, White GF, Hallett FR, Harauz G. </i> J Struct Biol, 2002","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"12372316","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":169,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"12372316","version":3,"reference_html":"Effects of the osmolyte trimethylamine-N-oxide on conformation, self-association, and two-dimensional crystallization of myelin basic protein. <i> Hill CM, Bates IR, White GF, Hallett FR, Harauz G. </i> J Struct Biol, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP01101r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":169,"reference_id":"19636827","reference_source":"pmid","reference_html":"NMR assignment of an intrinsically disordered protein under physiological conditions: the 18.5 kDa isoform of murine myelin basic protein. <i> Libich DS, Monette MM, Robertson VJ, Harauz G. </i> Biomol NMR Assign, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01101r003","statement":[{"text":"NMR assignment of an intrinsically disordered protein under physiological conditions: the 18.5 kDa isoform of murine myelin basic protein","type":"Title"},{"text":"The high degree of spin system overlap and chemical shift degeneracy inherent to intrinsically disordered proteins hinders resonance assignment. The 1H, 15N, and 13C backbone assignments were over 93% complete, excluding the carbonyl carbons, and residues Q3, L27, V91, and T92 for which no sequential crosspeaks were observed. Further, no resonances could be assigned for P96 and P97, which were part of a proline-rich domain.","type":"Article"},{"text":"Notably, an amphipathic α-helix (V83-T92) present in the protein under membrane-mimetic conditions appears disordered under these solution conditions.","type":"Article"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-21T15:39:39.173Z"}},{"start":82,"end":93,"reference_id":"22947219","reference_source":"pmid","reference_html":"Solution nuclear magnetic resonance structure and molecular dynamics simulations of a murine 18.5 kDa myelin basic protein segment (S72-S107) in association with dodecylphosphocholine micelles. <i> Ahmed MA, De Avila M, Polverini E, Bessonov K, Bamm VV, Harauz G. </i> Biochemistry, 2012","date":"2024-05-07T08:40:05.396Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"2LUG"}],"region_id":"DP01101r004","statement":[{"text":"Here, we have extended these MD studies to determine experimentally the conformation of the considerably larger α2- peptide comprising residues S72−S107 of this region of the protein, in association with DPC micelles, using solution NMR spectroscopy.","type":"Results"}],"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":6.5},{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":null,"value":285}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:644308"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-21T15:38:53.547Z"}},{"start":82,"end":93,"reference_id":"22947219","reference_source":"pmid","reference_html":"Solution nuclear magnetic resonance structure and molecular dynamics simulations of a murine 18.5 kDa myelin basic protein segment (S72-S107) in association with dodecylphosphocholine micelles. <i> Ahmed MA, De Avila M, Polverini E, Bessonov K, Bamm VV, Harauz G. </i> Biochemistry, 2012","date":"2024-05-07T08:43:11.875Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"2LUG"}],"ec_go":"EXP","region_id":"DP01101r005","statement":[{"text":"\"The α2-peptide (S72−S107) from the 18.5 kDa murine MBP amino acid sequence was designed initially to include one region of three (specifically V83−T92) that are known to adopt a strongly amphipathic α-helical structure in association with detergent micelles and phospholipid\nbilayers.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-21T15:39:08.007Z"}},{"start":79,"end":96,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T15:01:55.855Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP01101r006","statement":[{"text":"In aqueous solution (pure water, and 100 mm KCl, pH 6.5), the spectra indicated that the polypeptide had little or no regular secondary structure. In organic and membrane-mimetic conditions (30% TFE and 20 mm DPC, respectively), the spectra clearly indicated an α-helical conformation.","type":"Results"}]},{"start":79,"end":96,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T15:02:37.695Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP01101r007","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:162343649"}],"statement":[{"text":"In aqueous solution (pure water, and 100 mm KCl, pH 6.5), the spectra indicated that the polypeptide had little or no regular secondary structure. In organic and membrane-mimetic conditions (30% TFE and 20 mm DPC, respectively), the spectra clearly indicated an α-helical conformation.","type":"Results"}]},{"start":79,"end":96,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T15:15:21.962Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP01101r008","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:162343649"}],"statement":[{"text":"In aqueous solution (pure water, and 100 mm KCl, pH 6.5), the spectra indicated that the polypeptide had little or no regular secondary structure. In organic and membrane-mimetic conditions (30% TFE and 20 mm DPC, respectively), the spectra clearly indicated an α-helical conformation.","type":"Results"}],"states_connection":[{"source":"DP01101r006","target":"DP01101r007"}]},{"start":79,"end":96,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T15:05:23.394Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"78018","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01101r009","statement":[{"text":"In aqueous solution (pure water, and 100 mm KCl, pH 6.5), the spectra indicated that the polypeptide had little or no regular secondary structure. In organic and membrane-mimetic conditions (30% TFE and 20 mm DPC, respectively), the spectra clearly indicated an α-helical conformation.","type":"Results"},{"text":"Here, we focused on a conserved segment of MBP which is known to be a-helical when bound to a membrane, is a potential calmodulin-binding site, and also a primary immunodominant epitope in multiple sclerosis.","type":"Discussion"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":83,"end":93,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T15:06:07.422Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"78018","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01101r010","statement":[{"text":"The CSI analyses of our assignments, shown in Fig. 3, indicate a noticeable tendency of a central 10-residue segment of the polypeptide to adopt a helical conformation from residues 5′ to 14′, for samples in TFE-d2 (Fig. 3B) and in DPC-d38 (Fig. 3C), but not in KCl (Fig. 3A).","type":"Results"},{"text":"Here, we focused on a conserved segment of MBP which is known to be a-helical when bound to a membrane, is a potential calmodulin-binding site, and also a primary immunodominant epitope in multiple sclerosis.","type":"Discussion"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":79,"end":96,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T15:08:19.718Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP01101r011","statement":[{"text":"The CSI analyses of our assignments, shown in Fig. 3, indicate a noticeable tendency of a central 10-residue segment of the polypeptide to adopt a helical conformation from residues 5′ to 14′, for samples in TFE-d2 (Fig. 3B) and in DPC-d38 (Fig. 3C), but not in KCl (Fig. 3A).","type":"Results"}],"cross_refs":[{"db":"BMRB","id":"6857"}]},{"start":83,"end":93,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T15:14:36.309Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP01101r012","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:162343649"}],"statement":[{"text":"The CSI analyses of our assignments, shown in Fig. 3, indicate a noticeable tendency of a central 10-residue segment of the polypeptide to adopt a helical conformation from residues 5′ to 14′, for samples in TFE-d2 (Fig. 3B) and in DPC-d38 (Fig. 3C), but not in KCl (Fig. 3A).","type":"Results"}],"cross_refs":[{"db":"BMRB","id":"6857"}]},{"start":83,"end":93,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T15:15:55.404Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"6857"}],"region_id":"DP01101r013","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:162343649"}],"statement":[{"text":"The CSI analyses of our assignments, shown in Fig. 3, indicate a noticeable tendency of a central 10-residue segment of the polypeptide to adopt a helical conformation from residues 5′ to 14′, for samples in TFE-d2 (Fig. 3B) and in DPC-d38 (Fig. 3C), but not in KCl (Fig. 3A).","type":"Results"}],"states_connection":[{"source":"DP01101r011","target":"DP01101r012"}]},{"start":83,"end":93,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T15:17:19.929Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006287","ec_ontology":"ECO","ec_name":"electron paramagnetic resonance evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"78018","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01101r014","statement":[{"text":"These results demonstrate that the polypeptide α helix forms distinct hydrophobic and electrostatic contacts with the DPC micelles, and are in agreement with the SDSL/EPR mapping and positioning of the α-helical model of this epitope of MBP on the surface of a lipid bilayer [6,7].","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":73,"end":108,"reference_id":"22947219","reference_source":"pmid","reference_html":"Solution nuclear magnetic resonance structure and molecular dynamics simulations of a murine 18.5 kDa myelin basic protein segment (S72-S107) in association with dodecylphosphocholine micelles. <i> Ahmed MA, De Avila M, Polverini E, Bessonov K, Bamm VV, Harauz G. </i> Biochemistry, 2012","date":"2025-03-21T15:27:53.742Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP01101r015","statement":[{"text":"The central region of the α2-peptide (P82–V91) shows a strong tendency to form an α-helix, as fully expected, whereas the rest of the α2-peptide remains in a predominantly random coil conformation.","type":"Results"}]},{"start":92,"end":101,"reference_id":"22947219","reference_source":"pmid","reference_html":"Solution nuclear magnetic resonance structure and molecular dynamics simulations of a murine 18.5 kDa myelin basic protein segment (S72-S107) in association with dodecylphosphocholine micelles. <i> Ahmed MA, De Avila M, Polverini E, Bessonov K, Bamm VV, Harauz G. </i> Biochemistry, 2012","date":"2025-03-21T15:34:31.683Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0017124","term_name":"SH3 domain binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q05876","operator":null,"partner_start":82,"partner_end":143}],"region_id":"DP01101r016","statement":[{"text":"The titration of Fyn-SH3 into a solution of fully 13C- and 15N-labeled α2-peptide showed chemical shift perturbations of several assigned regions (Figure 9).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins.\" [GOC:go_curators, Pfam:PF00018]","term_is_obsolete":false,"term_not_annotate":false},{"start":82,"end":93,"reference_id":"22947219","reference_source":"pmid","reference_html":"Solution nuclear magnetic resonance structure and molecular dynamics simulations of a murine 18.5 kDa myelin basic protein segment (S72-S107) in association with dodecylphosphocholine micelles. <i> Ahmed MA, De Avila M, Polverini E, Bessonov K, Bamm VV, Harauz G. </i> Biochemistry, 2012","date":"2025-03-21T15:44:30.009Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"2LUG"},{"db":"BMRB","id":"18520"}],"region_id":"DP01101r017","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:644308"}],"statement":[{"text":"The central region of the α2-peptide (P82–V91) shows a strong tendency to form an α-helix, as fully expected, whereas the rest of the α2-peptide remains in a predominantly random coil conformation","type":"Results"},{"text":"Here, we have extended these MD studies to determine experimentally the conformation of the considerably larger α2- peptide comprising residues S72−S107 of this region of the protein, in association with DPC micelles, using solution NMR spectroscopy.","type":"Results"}],"states_connection":[{"source":"DP01101r015","target":"DP01101r004"}]}],"released":"2016_10","uniref100":"","date":"2016-09-20T16:09:03.000Z","acc":"P04370-5","name":"Isoform 5 of Myelin basic protein","length":169,"organism":"Mus musculus","dataset":[],"UniParc":"UPI000002ADAA","genes":[{"name":{"value":"Mbp"},"synonyms":[{"value":"Shi"}]}],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":78,"type":"D"},{"start":79,"end":96,"type":"T"},{"start":97,"end":169,"type":"D"}],"Structural state":[{"start":1,"end":169,"type":"D"}],"Molecular function":[{"start":1,"end":169,"type":"F"}],"Structural transition":[{"start":79,"end":96,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":287,"end":365},{"id":"PF00641","name":"Zn-finger in Ran binding protein and others","start":422,"end":453}],"gene3D":[{"start":284,"end":369,"id":"3.30.70.330","name":"3.30.70.330"},{"start":418,"end":455,"id":"4.10.1060.10","name":"Zinc finger, RanBP2-type"}]},"uniref50":"UniRef50_P35637","sequence":"MASNDYTQQATQSYGAYPTQPGQGYSQQSSQPYGQQSYSGYSQSTDTSGYGQSSYSSYGQSQNTGYGTQSTPQGYGSTGGYGSSQSSQSSYGQQSSYPGYGQQPAPSSTSGSYGSSSQSSSYGQPQSGSYSQQPSYGGQQQSYGQQQSYNPPQGYGQQNQYNSSSGGGGGGGGGGNYGQDQSSMSSGGGSGGGYGNQDQSGGGGSGGYGQQDRGGRGRGGSGGGGGGGGGGYNRSSGGYEPRGRGGGRGGRGGMGGSDRGGFNKFGGPRDQGSRHDSEQDNSDNNTIFVQGLGENVTIESVADYFKQIGIIKTNKKTGQPMINLYTDRETGKLKGEATVSFDDPPSAKAAIDWFDGKEFSGNPIKVSFATRRADFNRGGGNGRGGRGRGGPMGRGGYGGGGSGGGGRGGFPSGGGGGGGQQRAGDWKCPNPTCENMNFSWRNECNQCKAPKPDGPGGGPGGSHMGGNYGDDRRGGRGGYDRGGYRGRGGDRGGFRGGRGGGDRGGFGPGKMDSRGEHRQDRRERPY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P35637","disprot_id":"DP01102","ncbi_taxon_id":9606,"regions_counter":46,"creator":"mmarengo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":507,"region_id":"DP01102r004","reference_id":"29677513","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The lack of stable Kapβ2•FUS contacts outside the PY-NLS is consistent with observations that only the PY-NLS is observed in crystal structures of Kapβ2 bound to FUS (full-length), FUS(371–526) and FUS(456–526)","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple Sites. <i> Yoshizawa T, Ali R, Jiou J, Fung HYJ, Burke KA, Kim SJ, Lin Y, Peeples WB, Saltzberg D, Soniat M, Baumhardt JM, Oldenbourg R, Sali A, Fawzi NL, Rosen MK, Chook YM. </i> Cell, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5YVG"},{"db":"PDB","id":"5YVH"},{"db":"PDB","id":"5YVI"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-30T11:33:18.220Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP01102r005","ec_ontology":"ECO","end":526,"term_id":"GO:0005515","start":508,"version":4,"statement":[{"text":"The RNA-binding protein Fused in Sarcoma (FUS) undergoes LLPS in vitro and associates with condensates in cells. We show that the Importin Karyopherin-β2/Transportin-1 inhibits LLPS of FUS. This activity depends on tight binding of Karyopherin-β2 to the C-terminal proline-tyrosine nuclear localization signal (PY-NLS) of FUS.","type":"Abstract"},{"text":"Kapβ2 inhibits FUS turbidity and phase separation in a PY-NLS- and RanGTP-dependent manner","type":"Figure"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q92973","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"29677513","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5YVG"},{"db":"PDB","id":"5YVH"},{"db":"PDB","id":"5YVI"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"fquaglia","reference_html":"Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple Sites. <i> Yoshizawa T, Ali R, Jiou J, Fung HYJ, Burke KA, Kim SJ, Lin Y, Peeples WB, Saltzberg D, Soniat M, Baumhardt JM, Oldenbourg R, Sali A, Fawzi NL, Rosen MK, Chook YM. </i> Cell, 2018","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-30T12:01:13.045Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q92973","partner_end":null}],"ec_ontology":"ECO","end":41,"region_id":"DP01102r006","reference_id":"29677513","start":37,"term_id":"GO:0005515","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The largest perturbations are observed for resonances from the segments 37SYSGY41, 97YPGY100 and 149YSPPSG154, suggesting relatively stronger binding to these elements","type":"Results"},{"text":"Amide resonances change similarly upon addition of Kapβ2 alone or Kapβ2•PY-NLS, indicating contacts outside the PY-NLS binding site of the karyopherin","type":"Results"},{"text":"Kapβ2 inhibits FUS turbidity and phase separation in a PY-NLS- and RanGTP-dependent manner","type":"Figure"},{"text":"NMR analyses reveal multiple weak interactions of Kapβ2 with both folded and disordered regions across FUS.","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":4,"reference_html":"Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple Sites. <i> Yoshizawa T, Ali R, Jiou J, Fung HYJ, Burke KA, Kim SJ, Lin Y, Peeples WB, Saltzberg D, Soniat M, Baumhardt JM, Oldenbourg R, Sali A, Fawzi NL, Rosen MK, Chook YM. </i> Cell, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"protein binding","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-30T12:01:11.544Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q92973","partner_end":null}],"ec_ontology":"ECO","end":154,"region_id":"DP01102r007","reference_id":"29677513","start":149,"term_id":"GO:0005515","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The largest perturbations are observed for resonances from the segments 37SYSGY41, 97YPGY100 and 149YSPPSG154, suggesting relatively stronger binding to these elements","type":"Results"},{"text":"Amide resonances change similarly upon addition of Kapβ2 alone or Kapβ2•PY-NLS, indicating contacts outside the PY-NLS binding site of the karyopherin","type":"Results"},{"text":"Kapβ2 inhibits FUS turbidity and phase separation in a PY-NLS- and RanGTP-dependent manner","type":"Figure"},{"text":"NMR analyses reveal multiple weak interactions of Kapβ2 with both folded and disordered regions across FUS.","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":4,"reference_html":"Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple Sites. <i> Yoshizawa T, Ali R, Jiou J, Fung HYJ, Burke KA, Kim SJ, Lin Y, Peeples WB, Saltzberg D, Soniat M, Baumhardt JM, Oldenbourg R, Sali A, Fawzi NL, Rosen MK, Chook YM. </i> Cell, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"protein binding","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-30T12:01:07.047Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Cellular component","ec_ontology":"ECO","end":163,"region_id":"DP01102r008","reference_id":"22579281","start":1,"term_id":"GO:0043232","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Phase-Transition of the LC Sequence Domain of FUS into a Hydrogel","type":"Results"},{"text":"By contrast, N-terminal truncations lacking the LC sequence were incapable of phase transitioning into a hydrogel-like state.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"fluorescence evidence used in manual assertion","version":4,"reference_html":"Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels. <i> Kato M, Han TW, Xie S, Shi K, Du X, Wu LC, Mirzaei H, Goldsmith EJ, Longgood J, Pei J, Grishin NV, Frantz DE, Schneider JW, Chen S, Li L, Sawaya MR, Eisenberg D, Tycko R, McKnight SL. </i> Cell, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001249","term_name":"intracellular non-membrane-bounded organelle","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-30T12:01:21.231Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Organized structure of distinctive morphology and function, not bounded by a lipid bilayer membrane and occurring within the cell. Includes ribosomes, the cytoskeleton and chromosomes.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":false},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":526,"region_id":"DP01102r009","reference_id":"22579281","start":1,"term_id":"GO:0140693","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"Full-length FUS also undergoes LLPS, but at much lower concentrations, consistent with previous reports that the RGG regions can contribute to self-association of the protein","type":"Introduction"}],"curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","version":5,"reference_html":"Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels. <i> Kato M, Han TW, Xie S, Shi K, Du X, Wu LC, Mirzaei H, Goldsmith EJ, Longgood J, Pei J, Grishin NV, Frantz DE, Schneider JW, Chen S, Li L, Sawaya MR, Eisenberg D, Tycko R, McKnight SL. </i> Cell, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"molecular condensate scaffold activity","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-30T19:48:23.045Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":370,"region_id":"DP01102r010","reference_id":"29677513","start":285,"term_id":"GO:0003723","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The 1H/15N HSQC spectrum of 17 μM 15N-FUS(164–500) shows many strong resonances with 1H chemical shifts between ~7.5 ppm and 8.5 ppm, mostly representing residues in unstructured regions of the protein, as well as numerous resonances outside of this window, which represent the folded RRM (residues 285–370) and Cys4-type ZnF (residues 421–455) domains.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":4,"reference_html":"Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple Sites. <i> Yoshizawa T, Ali R, Jiou J, Fung HYJ, Burke KA, Kim SJ, Lin Y, Peeples WB, Saltzberg D, Soniat M, Baumhardt JM, Oldenbourg R, Sali A, Fawzi NL, Rosen MK, Chook YM. </i> Cell, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"RNA binding","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-30T12:01:03.792Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":370,"region_id":"DP01102r011","reference_id":"29677513","start":285,"term_id":"IDPO:0000011","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The 1H/15N HSQC spectrum of 17 μM 15N-FUS(164–500) shows many strong resonances with 1H chemical shifts between ~7.5 ppm and 8.5 ppm, mostly representing residues in unstructured regions of the protein, as well as numerous resonances outside of this window, which represent the folded RRM (residues 285–370) and Cys4-type ZnF (residues 421–455) domains.","type":"Results"}],"curator_id":"vnugnes","released":"2022_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":4,"reference_html":"Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple Sites. <i> Yoshizawa T, Ali R, Jiou J, Fung HYJ, Burke KA, Kim SJ, Lin Y, Peeples WB, Saltzberg D, Soniat M, Baumhardt JM, Oldenbourg R, Sali A, Fawzi NL, Rosen MK, Chook YM. </i> Cell, 2018","date":"2022-06-15T14:03:51.313Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder to order","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92973","statements":[{"type":"Results","text":"Addition of Kapβ2 to 15N-FUS(164–526) harboring the PY-NLS causes severe line-broadening of most resonances in 1H/15N HSQC spectra, including all of those representing the folded domains and much of the disordered regions thus precluding analysis (Figure S4A)."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-15T10:15:10.415Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":455,"region_id":"DP01102r012","reference_id":"29677513","start":421,"term_id":"IDPO:0000011","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The 1H/15N HSQC spectrum of 17 μM 15N-FUS(164–500) shows many strong resonances with 1H chemical shifts between ~7.5 ppm and 8.5 ppm, mostly representing residues in unstructured regions of the protein, as well as numerous resonances outside of this window, which represent the folded RRM (residues 285–370) and Cys4-type ZnF (residues 421–455) domains.","type":"Results"}],"curator_id":"vnugnes","released":"2022_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":4,"reference_html":"Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple Sites. <i> Yoshizawa T, Ali R, Jiou J, Fung HYJ, Burke KA, Kim SJ, Lin Y, Peeples WB, Saltzberg D, Soniat M, Baumhardt JM, Oldenbourg R, Sali A, Fawzi NL, Rosen MK, Chook YM. </i> Cell, 2018","date":"2022-06-15T14:03:12.639Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder to order","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92973","statements":[{"type":"Results","text":"Addition of Kapβ2 to 15N-FUS(164–526) harboring the PY-NLS causes severe line-broadening of most resonances in 1H/15N HSQC spectra, including all of those representing the folded domains and much of the disordered regions thus precluding analysis (Figure S4A)."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-15T10:15:12.154Z"}},{"start":1,"end":526,"reference_id":"29677513","reference_source":"pmid","reference_html":"Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple Sites. <i> Yoshizawa T, Ali R, Jiou J, Fung HYJ, Burke KA, Kim SJ, Lin Y, Peeples WB, Saltzberg D, Soniat M, Baumhardt JM, Oldenbourg R, Sali A, Fawzi NL, Rosen MK, Chook YM. </i> Cell, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006307","ec_ontology":"ECO","ec_name":"turbidity measurement evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01102r013","statement":[{"text":"Removal of MBP from MBP-FUS with the Tev protease causes FUS to self-associate, producing a turbid solution (Figure 1B and S1D, E).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-09T14:32:16.515Z"}},{"start":1,"end":163,"reference_id":"26455390","reference_source":"pmid","reference_html":"Residue-by-Residue View of In Vitro FUS Granules that Bind the C-Terminal Domain of RNA Polymerase II. <i> Burke KA, Janke AM, Rhine CL, Fawzi NL. </i> Mol Cell, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01102r014","statement":[{"text":"The lack of significant deviation between the observed shifts and those of a random coil reference demonstrate that the monomeric FUS LC domain is highly disordered, lacking significant population of α helices or β sheets (Figure S1A).","type":"Results"},{"text":"These data support our conclusion that the domain is predominantly disordered.","type":"Results"},{"text":"Because NMR chemical shifts are sensitive reporters of structure, we conclude that the LC domain retains the same disordered structure in the monomeric full-length protein as in the isolated FUS LC domain.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-30T14:48:34.138Z"}},{"start":1,"end":163,"reference_id":"26455390","reference_source":"pmid","reference_html":"Residue-by-Residue View of In Vitro FUS Granules that Bind the C-Terminal Domain of RNA Polymerase II. <i> Burke KA, Janke AM, Rhine CL, Fawzi NL. </i> Mol Cell, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006307","ec_ontology":"ECO","ec_name":"turbidity measurement evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01102r015","statement":[{"text":"While measuring the structural properties of the monomeric FUS LC, we noticed that our solutions of FUS turned opalescent or cloudy when placed on ice.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-09T14:32:15.568Z"}},{"start":1,"end":526,"reference_id":"26455390","reference_source":"pmid","reference_html":"Residue-by-Residue View of In Vitro FUS Granules that Bind the C-Terminal Domain of RNA Polymerase II. <i> Burke KA, Janke AM, Rhine CL, Fawzi NL. </i> Mol Cell, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006307","ec_ontology":"ECO","ec_name":"turbidity measurement evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01102r016","statement":[{"text":"Upon release of MBP by TEV cleavage leaving the native protein, samples as low as 1 μM full-length FUS assemble into an opalescent, phase-separated liquid (Figure 2B) resembling that formed by FUS LC. Phase separation proceeds rapidly after addition of TEV, and the extent of phase-separation is greater at higher concentrations of full-length FUS (Figure S2A).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-30T19:48:19.686Z"}},{"start":1,"end":163,"reference_id":"26455390","reference_source":"pmid","reference_html":"Residue-by-Residue View of In Vitro FUS Granules that Bind the C-Terminal Domain of RNA Polymerase II. <i> Burke KA, Janke AM, Rhine CL, Fawzi NL. </i> Mol Cell, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01102r017","statement":[{"text":"We used differential interference contrast microscopy to visualize the formation of liquid phase-separated FUS LC (Figure 2A), which resemble FUS-containing RNP granules previously observed in cells (Bentmann et al., 2012).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-30T19:48:27.157Z"}},{"start":1,"end":526,"reference_id":"22579281","reference_source":"pmid","reference_html":"Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels. <i> Kato M, Han TW, Xie S, Shi K, Du X, Wu LC, Mirzaei H, Goldsmith EJ, Longgood J, Pei J, Grishin NV, Frantz DE, Schneider JW, Chen S, Li L, Sawaya MR, Eisenberg D, Tycko R, McKnight SL. </i> Cell, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0043232","term_name":"intracellular non-membrane-bounded organelle","term_namespace":"Cellular component","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01102r018","statement":[{"text":"While working with concentrated forms of the recombinant, full length FUS protein linked to a GST tag (∼10mg/ml), it was noted that the protein adopted a gel-like state when stored at low temperature.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Organized structure of distinctive morphology and function, not bounded by a lipid bilayer membrane and occurring within the cell. Includes ribosomes, the cytoskeleton and chromosomes.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-30T19:48:16.976Z"}},{"start":1,"end":214,"reference_id":"22579281","reference_source":"pmid","reference_html":"Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels. <i> Kato M, Han TW, Xie S, Shi K, Du X, Wu LC, Mirzaei H, Goldsmith EJ, Longgood J, Pei J, Grishin NV, Frantz DE, Schneider JW, Chen S, Li L, Sawaya MR, Eisenberg D, Tycko R, McKnight SL. </i> Cell, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0043232","term_name":"intracellular non-membrane-bounded organelle","term_namespace":"Cellular component","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01102r019","statement":[{"text":"When produced as chimeric proteins with GST, mCherry or GFP, the FUS LC domain (residues 2-214, ∼50mg/ml) yielded clear, red and green colored hydrogels respectively (Figure 3A).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Organized structure of distinctive morphology and function, not bounded by a lipid bilayer membrane and occurring within the cell. Includes ribosomes, the cytoskeleton and chromosomes.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-30T19:48:30.628Z"}},{"start":1,"end":214,"reference_id":"22579281","reference_source":"pmid","reference_html":"Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels. <i> Kato M, Han TW, Xie S, Shi K, Du X, Wu LC, Mirzaei H, Goldsmith EJ, Longgood J, Pei J, Grishin NV, Frantz DE, Schneider JW, Chen S, Li L, Sawaya MR, Eisenberg D, Tycko R, McKnight SL. </i> Cell, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01102r020","statement":[{"text":"To initiate morphological and structural studies of the nature of the mCherry:FUS LC hydrogel, we first gathered transmission electron microscope (TEM) images of a pre-formed hydrogel composed of either mCherry:FUS LC or a His6-tag version of the FUS LC domain (Figure 5A and 5B). Both the mCherry:FUS and His:FUS preparations revealed morphologically uniform amyloid-like fibers.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-30T19:48:15.848Z"}},{"start":1,"end":214,"reference_id":"22579281","reference_source":"pmid","reference_html":"Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels. <i> Kato M, Han TW, Xie S, Shi K, Du X, Wu LC, Mirzaei H, Goldsmith EJ, Longgood J, Pei J, Grishin NV, Frantz DE, Schneider JW, Chen S, Li L, Sawaya MR, Eisenberg D, Tycko R, McKnight SL. </i> Cell, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0043232","term_name":"intracellular non-membrane-bounded organelle","term_namespace":"Cellular component","term_ontology":"GO","ec_id":"ECO:0006307","ec_ontology":"ECO","ec_name":"turbidity measurement evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01102r021","statement":[{"text":"When produced as chimeric proteins with GST, mCherry or GFP, the FUS LC domain (residues 2-214, ∼50mg/ml) yielded clear, red and green colored hydrogels respectively (Figure 3A).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Organized structure of distinctive morphology and function, not bounded by a lipid bilayer membrane and occurring within the cell. Includes ribosomes, the cytoskeleton and chromosomes.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-30T19:48:15.472Z"}},{"start":1,"end":526,"reference_id":"21541367","reference_source":"pmid","reference_html":"Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS. <i> Sun Z, Diaz Z, Fang X, Hart MP, Chesi A, Shorter J, Gitler AD. </i> PLoS Biol, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0043232","term_name":"intracellular non-membrane-bounded organelle","term_namespace":"Cellular component","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01102r022","statement":[{"text":"Whereas the control, YFP alone, was localized diffusely throughout the cytoplasm and nucleus, FUS-YFP localized to the cytoplasm where it formed numerous foci (Figure 1C).","type":"Results"},{"text":"However, FUS expression induced the formation of P-bodies and stress granules and FUS-YFP colocalized with both of these structures (Figure 2A,B).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Organized structure of distinctive morphology and function, not bounded by a lipid bilayer membrane and occurring within the cell. Includes ribosomes, the cytoskeleton and chromosomes.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-30T18:07:12.970Z"}},{"start":1,"end":526,"reference_id":"21541367","reference_source":"pmid","reference_html":"Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS. <i> Sun Z, Diaz Z, Fang X, Hart MP, Chesi A, Shorter J, Gitler AD. </i> PLoS Biol, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0043232","term_name":"intracellular non-membrane-bounded organelle","term_namespace":"Cellular component","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01102r023","statement":[{"text":"Upon addition of TEV protease, FUS aggregated extremely rapidly (Figure 5C). By contrast, GST-FUS remained predominantly soluble (Figure 5C). Under identical conditions neither GST nor TEV protease aggregated (Figure 5C).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Organized structure of distinctive morphology and function, not bounded by a lipid bilayer membrane and occurring within the cell. Includes ribosomes, the cytoskeleton and chromosomes.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-30T18:07:11.732Z"}},{"start":1,"end":422,"reference_id":"21541367","reference_source":"pmid","reference_html":"Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS. <i> Sun Z, Diaz Z, Fang X, Hart MP, Chesi A, Shorter J, Gitler AD. </i> PLoS Biol, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0043232","term_name":"intracellular non-membrane-bounded organelle","term_namespace":"Cellular component","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01102r024","statement":[{"text":"Adding back the first RGG domain (amino acids 371–422) was sufficient to restore cytoplasmic aggregation (Figure 3B, construct 1–422).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Organized structure of distinctive morphology and function, not bounded by a lipid bilayer membrane and occurring within the cell. Includes ribosomes, the cytoskeleton and chromosomes.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-30T18:07:11.328Z"}},{"start":1,"end":526,"reference_id":"26317470","reference_source":"pmid","reference_html":"A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation. <i> Patel A, Lee HO, Jawerth L, Maharana S, Jahnel M, Hein MY, Stoynov S, Mahamid J, Saha S, Franzmann TM, Pozniakovski A, Poser I, Maghelli N, Royer LA, Weigert M, Myers EW, Grill S, Drechsel D, Hyman AA, Alberti S. </i> Cell, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0043232","term_name":"intracellular non-membrane-bounded organelle","term_namespace":"Cellular component","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01102r025","statement":[{"text":"We also noticed that FUS formed small foci in the nucleoplasm (Figure 1B).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Organized structure of distinctive morphology and function, not bounded by a lipid bilayer membrane and occurring within the cell. Includes ribosomes, the cytoskeleton and chromosomes.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-30T15:43:59.828Z"}},{"start":1,"end":526,"reference_id":"26317470","reference_source":"pmid","reference_html":"A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation. <i> Patel A, Lee HO, Jawerth L, Maharana S, Jahnel M, Hein MY, Stoynov S, Mahamid J, Saha S, Franzmann TM, Pozniakovski A, Poser I, Maghelli N, Royer LA, Weigert M, Myers EW, Grill S, Drechsel D, Hyman AA, Alberti S. </i> Cell, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006067","ec_ontology":"ECO","ec_name":"fluorescence recovery after photobleaching evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01102r026","statement":[{"text":"The spatiotemporal analysis of such half-bleach events showed that FUS was redistributed rapidly within stress granules and nuclear FUS assemblies, from the unbleached area to the bleached area (Figures 2A and 2B; Figure S2A; Movie S2). Thus, we conclude that FUS molecules can diffuse freely in stress granules and nuclear assemblies, in agreement with a liquid material state.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-30T15:43:41.486Z"}},{"start":1,"end":526,"reference_id":"26317470","reference_source":"pmid","reference_html":"A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation. <i> Patel A, Lee HO, Jawerth L, Maharana S, Jahnel M, Hein MY, Stoynov S, Mahamid J, Saha S, Franzmann TM, Pozniakovski A, Poser I, Maghelli N, Royer LA, Weigert M, Myers EW, Grill S, Drechsel D, Hyman AA, Alberti S. </i> Cell, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01102r027","statement":[{"text":"Therefore, FUS assemblies have all the hallmarks of a liquid state: they turn over quickly; are spherical; and when they fuse, they relax into one spherical assembly (Hyman et al., 2014). Taken together, these experiments show that FUS assemblies are liquid droplets, which probably form by liquid-liquid demixing in the cytoplasm or nucleoplasm.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-30T15:43:36.896Z"}},{"start":2,"end":36,"reference_id":"28942918","reference_source":"pmid","reference_html":"Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains. <i> Murray DT, Kato M, Lin Y, Thurber KR, Hung I, McKnight SL, Tycko R. </i> Cell, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5W3N"}],"region_id":"DP01102r028","statement":[{"text":"Despite the repetitive nature of the FUS-LC sequence, we find that the structured core of FUS-LC fibrils is formed reproducibly by a specific 57-residue segment in the N-terminal half. Other segments, especially in the C-terminal half, remain dynamically disordered.","type":"Introduction"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-30T13:50:22.969Z"}},{"start":98,"end":214,"reference_id":"28942918","reference_source":"pmid","reference_html":"Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains. <i> Murray DT, Kato M, Lin Y, Thurber KR, Hung I, McKnight SL, Tycko R. </i> Cell, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5W3N"}],"region_id":"DP01102r029","statement":[{"text":"Despite the repetitive nature of the FUS-LC sequence, we find that the structured core of FUS-LC fibrils is formed reproducibly by a specific 57-residue segment in the N-terminal half. Other segments, especially in the C-terminal half, remain dynamically disordered.","type":"Introduction"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-30T13:50:02.310Z"}},{"start":39,"end":95,"reference_id":"28942918","reference_source":"pmid","reference_html":"Structure of FUS Protein Fibrils and Its Relevance to Self-Assembly and Phase Separation of Low-Complexity Domains. <i> Murray DT, Kato M, Lin Y, Thurber KR, Hung I, McKnight SL, Tycko R. </i> Cell, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"5W3N"}],"region_id":"DP01102r030","statement":[{"text":"Despite the repetitive nature of the FUS-LC sequence, we find that the structured core of FUS-LC fibrils is formed reproducibly by a specific 57-residue segment in the N-terminal half. Other segments, especially in the C-terminal half, remain dynamically disordered.","type":"Introduction"},{"text":"We therefore conclude that residues 39–95 constitute the structurally ordered core of FUS-LC fibrils, with partial disorder or enhanced dynamics in residues 55–62 that precludes detection or unambiguous assignment of solid state NMR signals to these sites.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-30T14:48:39.132Z"}},{"start":1,"end":211,"reference_id":"38070499","reference_source":"pmid","reference_html":"The roles of FUS-RNA binding domain and low complexity domain in RNA-dependent phase separation. <i> Ganser LR, Niaki AG, Yuan X, Huang E, Deng D, Djaja NA, Ge Y, Craig A, Langlois O, Myong S. </i> Structure, 2024","date":"2024-05-08T08:35:09.232Z","curator_id":"mmarengo","curator_name":"Mauro Marengo","curator_orcid":"0000-0002-5389-3979","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","region_id":"DP01102r032","statement":[{"text":"Although it was expected that RBD would bind RNA, it was surprising that the\nLCD domain also bound RNA given that prion-like domains are not typically thought to have RNA-binding activity.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"ChEBI","id":"CHEBI:8758","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-13T13:20:24.223Z"}},{"start":305,"end":368,"reference_id":"38070499","reference_source":"pmid","reference_html":"The roles of FUS-RNA binding domain and low complexity domain in RNA-dependent phase separation. <i> Ganser LR, Niaki AG, Yuan X, Huang E, Deng D, Djaja NA, Ge Y, Craig A, Langlois O, Myong S. </i> Structure, 2024","date":"2024-05-08T09:02:22.357Z","curator_id":"mmarengo","curator_name":"Mauro Marengo","curator_orcid":"0000-0002-5389-3979","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe305Leu","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test the role of the RRM, we used a FUS mutant with an RNA-binding deficient RRM, 4FL (F305L/F341L/F359L/F368L), and with four phenylalanine to leucine point mutations in the RRM (Figure 6A)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe341Leu","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test the role of the RRM, we used a FUS mutant with an RNA-binding deficient RRM, 4FL (F305L/F341L/F359L/F368L), and with four phenylalanine to leucine point mutations in the RRM (Figure 6A)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe359Leu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe368Leu","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test the role of the RRM, we used a FUS mutant with an RNA-binding deficient RRM, 4FL (F305L/F341L/F359L/F368L), and with four phenylalanine to leucine point mutations in the RRM (Figure 6A)."}]}],"region_id":"DP01102r035","statement":[{"text":"We found that FUS 4FL forms aberrant droplets that are substantially smaller than full-length FUS droplets, suggesting that FUS with a dysfunctional RRM cannot form proper condensates (Figure 6B). In the EMSA, 4FL still binds RNA and forms C1and C2, but not higher-order complex, similar to LCD and LCD-RGG1 (Figures 6C and S5). This suggests that the RRM is responsible for the high-order complex formation, while other regions of FUS, such as the RGG motifs or zinc finger domain, are responsible for the C1 and C2 complex formation. ","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"ec_go":"IMP","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-13T17:58:46.919Z"}},{"start":1,"end":526,"reference_id":"38070499","reference_source":"pmid","reference_html":"The roles of FUS-RNA binding domain and low complexity domain in RNA-dependent phase separation. <i> Ganser LR, Niaki AG, Yuan X, Huang E, Deng D, Djaja NA, Ge Y, Craig A, Langlois O, Myong S. </i> Structure, 2024","date":"2024-05-08T08:59:58.462Z","curator_id":"mmarengo","curator_name":"Mauro Marengo","curator_orcid":"0000-0002-5389-3979","term_id":"GO:0005654","term_name":"nucleoplasm","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005589","ec_ontology":"ECO","ec_name":"confocal microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","region_id":"DP01102r036","statement":[{"text":"Full-length FUS remains soluble in nucleoplasm as expected from the RNA buffering phase separation of FUS (Figures 7A and S7A)","type":"Results"}],"term_comment":"","term_def":"\"That part of the nuclear content other than the chromosomes or the nucleolus.\" [GOC:ma, ISBN:0124325653]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"We expressed GFP-tagged full-length FUS, LCD, RBD, and 4FL in HeLa cells to examine the cellular localization and condensation behavior"},{"type":"Methods","text":"Cells were transfected with 0.1 ug of GFP tagged FUS constructs (LCD, RBD and 4FL), unless otherwise specified."}]}],"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-13T13:20:45.459Z"}},{"start":1,"end":526,"reference_id":"38070499","reference_source":"pmid","reference_html":"The roles of FUS-RNA binding domain and low complexity domain in RNA-dependent phase separation. <i> Ganser LR, Niaki AG, Yuan X, Huang E, Deng D, Djaja NA, Ge Y, Craig A, Langlois O, Myong S. </i> Structure, 2024","date":"2024-05-07T14:35:56.833Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005590","ec_ontology":"ECO","ec_name":"wide-field microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","region_id":"DP01102r038","statement":[{"text":"We find that in the absence of RNA, neither LCD nor RBD form droplets up to 15 μM while full-length FUS forms droplets by at least 2.5 μM (Figures 1B and S1A).","type":"Results"},{"text":"These results agree with previous results in the absence of RNA showing that LCD and RBD alone do not phase separate up to 30 μM while RBD+LCD in trans does not phase separate until ~25 μM compared to 5 μM for full-length FUS.","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false},{"start":221,"end":526,"reference_id":"38070499","reference_source":"pmid","reference_html":"The roles of FUS-RNA binding domain and low complexity domain in RNA-dependent phase separation. <i> Ganser LR, Niaki AG, Yuan X, Huang E, Deng D, Djaja NA, Ge Y, Craig A, Langlois O, Myong S. </i> Structure, 2024","date":"2024-05-07T14:18:06.745Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006062","ec_ontology":"ECO","ec_name":"wide-field fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","region_id":"DP01102r039","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting single stranded RNA molecule U40 with sequence:  5'-UUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUU/3AmMO/-3"}]}],"statement":[{"text":"Strikingly, we find that RBD phase separates in the presence of RNA as readily as full-length FUS, whereas LCD does not form droplets in any conditions tested with RNA (Figures 1B and ​1C).","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false},{"start":221,"end":526,"reference_id":"38070499","reference_source":"pmid","reference_html":"The roles of FUS-RNA binding domain and low complexity domain in RNA-dependent phase separation. <i> Ganser LR, Niaki AG, Yuan X, Huang E, Deng D, Djaja NA, Ge Y, Craig A, Langlois O, Myong S. </i> Structure, 2024","date":"2024-05-07T14:23:52.948Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","region_id":"DP01102r040","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting single stranded RNA molecule U40 with sequence:  5'-UUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUU/3AmMO/-3"}]}],"statement":[{"text":"Dynamic light scattering (DLS), which is sensitive to very small cluster (1–100 nm diameter) and droplet (1–10 μm) formation, further confirmed our results that FUS and RBD form micron-scale condensates (both ~100 nm clusters and ~1000 nm droplets were observed) while LCD remains dilute (10 nm diameter) in the presence of RNA (Figure S1B).","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false},{"start":221,"end":526,"reference_id":"38070499","reference_source":"pmid","reference_html":"The roles of FUS-RNA binding domain and low complexity domain in RNA-dependent phase separation. <i> Ganser LR, Niaki AG, Yuan X, Huang E, Deng D, Djaja NA, Ge Y, Craig A, Langlois O, Myong S. </i> Structure, 2024","date":"2024-05-07T14:37:44.959Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006067","ec_ontology":"ECO","ec_name":"fluorescence recovery after photobleaching evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"When required, proteins were labeled at free amine groups (lysine side chains and N-terminal amine) using Cy3-NHS ester dye."}]}],"ec_go":"IDA","region_id":"DP01102r041","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting single stranded RNA molecule U40 with sequence:  5'-UUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUUU/3AmMO/-3"}]}],"statement":[{"text":"Similar FRAP results were observed for RBD with and without LCD after bleaching the full droplet, bleaching partial droplets to observe only intra-droplet dynamics, and when the RBD was fluorescently labeled instead of the RNA molecule (Figure S2).","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false},{"start":221,"end":526,"reference_id":"38070499","reference_source":"pmid","reference_html":"The roles of FUS-RNA binding domain and low complexity domain in RNA-dependent phase separation. <i> Ganser LR, Niaki AG, Yuan X, Huang E, Deng D, Djaja NA, Ge Y, Craig A, Langlois O, Myong S. </i> Structure, 2024","date":"2024-05-07T14:45:56.537Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"8758","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01102r042","statement":[{"text":"First, we demonstrate that both RBD and LCD truncations bind RNA using an Electrophoretic mobility shift assay (EMSA) gel (Figure 3).","type":"Results"},{"text":"Together, the EMSA suggests that although both FUS domains can bind U50 RNA as monomers and dimers, the ability to form high-order complexes, presumably through multivalent interactions, is driven by the RBD and may be critical for droplet formation.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":526,"reference_id":"38070499","reference_source":"pmid","reference_html":"The roles of FUS-RNA binding domain and low complexity domain in RNA-dependent phase separation. <i> Ganser LR, Niaki AG, Yuan X, Huang E, Deng D, Djaja NA, Ge Y, Craig A, Langlois O, Myong S. </i> Structure, 2024","date":"2024-05-07T14:54:48.339Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"8758","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01102r043","statement":[{"text":"In agreement with these previous results, we find that full-length FUS forms a highly dynamic complex with RNA at high concentration (500 nM) at which multimer binding is favored (Figure 4B). RBD, LCD, and R + L also yield a mix of static high-FRET and dynamic mid-FRET signal (Figure 4).","type":"Results"},{"text":"These data show that both domains are critical for maintaining a dynamic FUS-RNA interaction.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":221,"end":526,"reference_id":"38070499","reference_source":"pmid","reference_html":"The roles of FUS-RNA binding domain and low complexity domain in RNA-dependent phase separation. <i> Ganser LR, Niaki AG, Yuan X, Huang E, Deng D, Djaja NA, Ge Y, Craig A, Langlois O, Myong S. </i> Structure, 2024","date":"2024-05-07T14:56:19.029Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"8758","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01102r044","statement":[{"text":"Furthermore, at 10 nM concentration, RBD binding shows FRET fluctuations in the intermediate state that suggest the protein is not as stably bound prior to reaching the high-FRET state (Figure 5B, left).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":211,"reference_id":"38070499","reference_source":"pmid","reference_html":"The roles of FUS-RNA binding domain and low complexity domain in RNA-dependent phase separation. <i> Ganser LR, Niaki AG, Yuan X, Huang E, Deng D, Djaja NA, Ge Y, Craig A, Langlois O, Myong S. </i> Structure, 2024","date":"2024-05-07T14:57:03.054Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"8758","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01102r045","statement":[{"text":"The LCD also binds RNA, as was in the EMSA, but instead of undergoing a two-state process, it transitions directly to the high-FRET state (Figure 5C).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":221,"end":526,"reference_id":"38070499","reference_source":"pmid","reference_html":"The roles of FUS-RNA binding domain and low complexity domain in RNA-dependent phase separation. <i> Ganser LR, Niaki AG, Yuan X, Huang E, Deng D, Djaja NA, Ge Y, Craig A, Langlois O, Myong S. </i> Structure, 2024","date":"2024-05-07T15:15:40.829Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140694","term_name":"non-membrane-bounded organelle assembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Figure","text":"(A–D) N-terminally GFP tagged full-length FUS (A), LCD (B), RBD (C), and 4FL (D) are expressed in HeLa cells."}]}],"ec_go":"IDA","region_id":"DP01102r046","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","statements":[{"type":"Figure","text":"(A–D) N-terminally GFP tagged full-length FUS (A), LCD (B), RBD (C), and 4FL (D) are expressed in HeLa cells."}],"entry_name":"Henrietta Lacks cells"}],"statement":[{"text":"Interestingly, RBD-FUS, which drives phase separation into large condensates in vitro, co-condenses into the nucleolus which is highly enriched with RNA (Figures 7C and S7C).","type":"Results"}],"term_comment":"","term_def":"\"The aggregation, arrangement and bonding together of a set of components to form a non-membrane-bounded organelle.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2016_10","uniref100":"UniRef100_P35637","date":"2016-09-22T14:44:02.000Z","acc":"P35637","name":"RNA-binding protein FUS","length":526,"organism":"Homo sapiens","dataset":["Condensates-related proteins","Cancer-related proteins","RNA-binding proteins","Age-related disorders proteins"],"UniParc":"UPI000012AD9A","genes":[{"name":{"value":"FUS"},"synonyms":[{"value":"TLS"}]}],"alphafold_very_low_content":0.6920152091254753,"disorder_content":0.9638783269961977,"disprot_consensus":{"full":[{"start":1,"end":284,"type":"D"},{"start":285,"end":370,"type":"T"},{"start":371,"end":420,"type":"D"},{"start":421,"end":455,"type":"T"},{"start":456,"end":507,"type":"D"},{"start":508,"end":526,"type":"F"}],"Structural state":[{"start":1,"end":507,"type":"D"}],"Molecular function":[{"start":1,"end":526,"type":"F"}],"Cellular component":[{"start":1,"end":526,"type":"F"}],"Structural transition":[{"start":285,"end":370,"type":"T"},{"start":421,"end":455,"type":"T"}],"Biological process":[{"start":1,"end":214,"type":"F"},{"start":221,"end":526,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00520","name":"Ion transport protein","start":51,"end":344},{"id":"PF00520","name":"Ion transport protein","start":432,"end":669},{"id":"PF00520","name":"Ion transport protein","start":799,"end":1074},{"id":"PF00520","name":"Ion transport protein","start":1118,"end":1391},{"id":"PF08763","name":"Voltage gated calcium channel IQ domain","start":1464,"end":1536},{"id":"PF16905","name":"Voltage-dependent L-type calcium channel, IQ-associated","start":1401,"end":1454}],"gene3D":[{"start":789,"end":908,"id":"1.20.120.350","name":"Voltage-gated potassium channels. Chain C"},{"start":1107,"end":1252,"id":"1.20.120.350","name":"Voltage-gated potassium channels. Chain C"},{"start":41,"end":180,"id":"1.20.120.350","name":"Voltage-gated potassium channels. Chain C"},{"start":422,"end":544,"id":"1.20.120.350","name":"Voltage-gated potassium channels. Chain C"},{"start":1253,"end":1384,"id":"1.10.287.70","name":"1.10.287.70"},{"start":545,"end":669,"id":"1.10.287.70","name":"1.10.287.70"},{"start":913,"end":1073,"id":"1.10.287.70","name":"1.10.287.70"},{"start":1385,"end":1506,"id":"1.10.238.10","name":"EF-hand"}]},"uniref50":"UniRef50_Q13698","sequence":"MEPSSPQDEGLRKKQPKKPVPEILPRPPRALFCLTLENPLRKACISIVEWKPFETIILLTIFANCVALAVYLPMPEDDNNSLNLGLEKLEYFFLIVFSIEAAMKIIAYGFLFHQDAYLRSGWNVLDFTIVFLGVFTVILEQVNVIQSHTAPMSSKGAGLDVKALRAFRVLRPLRLVSGVPSLQVVLNSIFKAMLPLFHIALLVLFMVIIYAIIGLELFKGKMHKTCYFIGTDIVATVENEEPSPCARTGSGRRCTINGSECRGGWPGPNHGITHFDNFGFSMLTVYQCITMEGWTDVLYWVNDAIGNEWPWIYFVTLILLGSFFILNLVLGVLSGEFTKEREKAKSRGTFQKLREKQQLDEDLRGYMSWITQGEVMDVEDFREGKLSLDEGGSDTESLYEIAGLNKIIQFIRHWRQWNRIFRWKCHDIVKSKVFYWLVILIVALNTLSIASEHHNQPLWLTRLQDIANRVLLSLFTTEMLMKMYGLGLRQYFMSIFNRFDCFVVCSGILEILLVESGAMTPLGISVLRCIRLLRIFKITKYWTSLSNLVASLLNSIRSIASLLLLLFLFIVIFALLGMQLFGGRYDFEDTEVRRSNFDNFPQALISVFQVLTGEDWTSMMYNGIMAYGGPSYPGMLVCIYFIILFVCGNYILLNVFLAIAVDNLAEAESLTSAQKAKAEEKKRRKMSKGLPDKSEEEKSTMAKKLEQKPKGEGIPTTAKLKIDEFESNVNEVKDPYPSADFPGDDEEDEPEIPLSPRPRPLAELQLKEKAVPIPEASSFFIFSPTNKIRVLCHRIVNATWFTNFILLFILLSSAALAAEDPIRADSMRNQILKHFDIGFTSVFTVEIVLKMTTYGAFLHKGSFCRNYFNMLDLLVVAVSLISMGLESSAISVVKILRVLRVLRPLRAINRAKGLKHVVQCMFVAISTIGNIVLVTTLLQFMFACIGVQLFKGKFFRCTDLSKMTEEECRGYYYVYKDGDPMQIELRHREWVHSDFHFDNVLSAMMSLFTVSTFEGWPQLLYKAIDSNAEDVGPIYNNRVEMAIFFIIYIILIAFFMMNIFVGFVIVTFQEQGETEYKNCELDKNQRQCVQYALKARPLRCYIPKNPYQYQVWYIVTSSYFEYLMFALIMLNTICLGMQHYNQSEQMNHISDILNVAFTIIFTLEMILKLMAFKARGYFGDPWNVFDFLIVIGSIIDVILSEIDTFLASSGGLYCLGGGCGNVDPDESARISSAFFRLFRVMRLIKLLSRAEGVRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQMFGKIALVDGTQINRNNNFQTFPQAVLLLFRCATGEAWQEILLACSYGKLCDPESDYAPGEEYTCGTNFAYYYFISFYMLCAFLVINLFVAVIMDNFDYLTRDWSILGPHHLDEFKAIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKFCPHRVACKRLVGMNMPLNSDGTVTFNATLFALVRTALKIKTEGNFEQANEELRAIIKKIWKRTSMKLLDQVIPPIGDDEVTVGKFYATFLIQEHFRKFMKRQEEYYGYRPKKDIVQIQAGLRTIEEEAAPEICRTVSGDLAAEEELERAMVEAAMEEGIFRRTGGLFGQVDNFLERTNSLPPVMANQRPLQFAEIEMEEMESPVFLEDFPQDPRTNPLARANTNNANANVAYGNSNHSNSHVFSSVHYEREFPEETETPATRGRALGQPCRVLGPHSKPCVEMLKGLLTQRAMPRGQAPPAPCQCPRVESSMPEDRKSSTPGSLHEETPHSRSTRENTSRCSAPATALLIQKALVRGGLGTLAADANFIMATGQALADACQMEPEEVEIMATELLKGREAPEGMASSLGCLNLGSSLGSLDQHQGSQETLIPPRL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q13698","disprot_id":"DP01103","ncbi_taxon_id":9606,"regions_counter":9,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":785,"region_id":"DP01103r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"A dihydropyridine receptor alpha1s loop region critical for skeletal muscle contraction is intrinsically unstructured and binds to a SPRY domain of the type 1 ryanodine receptor. <i> Cui Y, Tae HS, Norris NC, Karunasekara Y, Pouliquin P, Board PG, Dulhunty AF, Casarotto MG. </i> Int J Biochem Cell Biol, 2009","term_id":"IDPO:0000002","curator_id":"mnecci","start":665,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"18761102","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":785,"term_name":"molecular function activator activity","start":665,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"18761102","version":3,"reference_html":"A dihydropyridine receptor alpha1s loop region critical for skeletal muscle contraction is intrinsically unstructured and binds to a SPRY domain of the type 1 ryanodine receptor. <i> Cui Y, Tae HS, Norris NC, Karunasekara Y, Pouliquin P, Board PG, Dulhunty AF, Casarotto MG. </i> Int J Biochem Cell Biol, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140677","ec_id":"ECO:0006204","region_id":"DP01103r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":785,"term_name":"small molecule binding","start":665,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"18761102","version":3,"reference_html":"A dihydropyridine receptor alpha1s loop region critical for skeletal muscle contraction is intrinsically unstructured and binds to a SPRY domain of the type 1 ryanodine receptor. <i> Cui Y, Tae HS, Norris NC, Karunasekara Y, Pouliquin P, Board PG, Dulhunty AF, Casarotto MG. </i> Int J Biochem Cell Biol, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0036094","ec_id":"ECO:0006204","region_id":"DP01103r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":785,"region_id":"DP01103r004","released":"2022_03","ec_id":"ECO:0006198","reference_html":"A dihydropyridine receptor alpha1s loop region critical for skeletal muscle contraction is intrinsically unstructured and binds to a SPRY domain of the type 1 ryanodine receptor. <i> Cui Y, Tae HS, Norris NC, Karunasekara Y, Pouliquin P, Board PG, Dulhunty AF, Casarotto MG. </i> Int J Biochem Cell Biol, 2009","term_id":"IDPO:0000002","curator_id":"mnecci","start":665,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"18761102","version":2,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":785,"term_name":"molecular function activator activity","start":665,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"18761102","version":3,"reference_html":"A dihydropyridine receptor alpha1s loop region critical for skeletal muscle contraction is intrinsically unstructured and binds to a SPRY domain of the type 1 ryanodine receptor. <i> Cui Y, Tae HS, Norris NC, Karunasekara Y, Pouliquin P, Board PG, Dulhunty AF, Casarotto MG. </i> Int J Biochem Cell Biol, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140677","ec_id":"ECO:0006198","region_id":"DP01103r005","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":785,"term_name":"small molecule binding","start":665,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"18761102","version":3,"reference_html":"A dihydropyridine receptor alpha1s loop region critical for skeletal muscle contraction is intrinsically unstructured and binds to a SPRY domain of the type 1 ryanodine receptor. <i> Cui Y, Tae HS, Norris NC, Karunasekara Y, Pouliquin P, Board PG, Dulhunty AF, Casarotto MG. </i> Int J Biochem Cell Biol, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0036094","ec_id":"ECO:0006198","region_id":"DP01103r006","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":791,"region_id":"DP01103r007","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Cyclization of the intrinsically disordered α1S dihydropyridine receptor II-III loop enhances secondary structure and in vitro function. <i> Tae HS, Cui Y, Karunasekara Y, Board PG, Dulhunty AF, Casarotto MG. </i> J Biol Chem, 2011","term_id":"IDPO:0000002","curator_id":"mnecci","start":666,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"21525002","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":791,"term_name":"molecular function activator activity","start":666,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"21525002","version":3,"reference_html":"Cyclization of the intrinsically disordered α1S dihydropyridine receptor II-III loop enhances secondary structure and in vitro function. <i> Tae HS, Cui Y, Karunasekara Y, Board PG, Dulhunty AF, Casarotto MG. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140677","ec_id":"ECO:0006204","region_id":"DP01103r008","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":791,"term_name":"small molecule binding","start":666,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"21525002","version":3,"reference_html":"Cyclization of the intrinsically disordered α1S dihydropyridine receptor II-III loop enhances secondary structure and in vitro function. <i> Tae HS, Cui Y, Karunasekara Y, Board PG, Dulhunty AF, Casarotto MG. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0036094","ec_id":"ECO:0006204","region_id":"DP01103r009","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_Q13698","date":"2016-09-22T16:35:44.000Z","acc":"Q13698","name":"Voltage-dependent L-type calcium channel subunit alpha-1S","length":1873,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000016A484","genes":[{"name":{"value":"CACNA1S"},"synonyms":[{"value":"CACH1"},{"value":"CACN1"},{"value":"CACNL1A3","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"7713519","url":"http://www.ncbi.nlm.nih.gov/pubmed/7713519","alternativeUrl":"https://europepmc.org/abstract/MED/7713519"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"8838325","url":"http://www.ncbi.nlm.nih.gov/pubmed/8838325","alternativeUrl":"https://europepmc.org/abstract/MED/8838325"}}]}]}],"alphafold_very_low_content":0.22637479978643887,"disorder_content":0.06780565936999466,"disprot_consensus":{"full":[{"start":665,"end":791,"type":"D"}],"Structural state":[{"start":665,"end":791,"type":"D"}],"Molecular function":[{"start":665,"end":791,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00008","name":"EGF-like domain","start":106,"end":136},{"id":"PF00008","name":"EGF-like domain","start":144,"end":174},{"id":"PF00008","name":"EGF-like domain","start":222,"end":252},{"id":"PF00008","name":"EGF-like domain","start":261,"end":291},{"id":"PF00008","name":"EGF-like domain","start":339,"end":367},{"id":"PF00008","name":"EGF-like domain","start":456,"end":485},{"id":"PF00008","name":"EGF-like domain","start":494,"end":523},{"id":"PF00008","name":"EGF-like domain","start":532,"end":561},{"id":"PF00008","name":"EGF-like domain","start":607,"end":637},{"id":"PF00008","name":"EGF-like domain","start":645,"end":672},{"id":"PF00008","name":"EGF-like domain","start":720,"end":748},{"id":"PF00008","name":"EGF-like domain","start":795,"end":824},{"id":"PF00008","name":"EGF-like domain","start":833,"end":864},{"id":"PF00008","name":"EGF-like domain","start":911,"end":939},{"id":"PF00008","name":"EGF-like domain","start":1025,"end":1055},{"id":"PF00008","name":"EGF-like domain","start":1063,"end":1093},{"id":"PF00008","name":"EGF-like domain","start":1116,"end":1141},{"id":"PF00008","name":"EGF-like domain","start":1149,"end":1178},{"id":"PF00008","name":"EGF-like domain","start":1187,"end":1216},{"id":"PF00008","name":"EGF-like domain","start":1236,"end":1263},{"id":"PF00008","name":"EGF-like domain","start":1311,"end":1343},{"id":"PF00023","name":"Ankyrin repeat","start":1994,"end":2026},{"id":"PF00066","name":"LNR domain","start":1447,"end":1480},{"id":"PF00066","name":"LNR domain","start":1487,"end":1522},{"id":"PF00066","name":"LNR domain","start":1527,"end":1561},{"id":"PF06816","name":"NOTCH protein","start":1566,"end":1621},{"id":"PF07645","name":"Calcium-binding EGF domain","start":178,"end":211},{"id":"PF07645","name":"Calcium-binding EGF domain","start":295,"end":329},{"id":"PF07645","name":"Calcium-binding EGF domain","start":412,"end":445},{"id":"PF07645","name":"Calcium-binding EGF domain","start":869,"end":900},{"id":"PF07684","name":"NOTCH protein","start":1672,"end":1729},{"id":"PF12661","name":"Human growth factor-like EGF","start":575,"end":595},{"id":"PF12661","name":"Human growth factor-like EGF","start":687,"end":708},{"id":"PF12661","name":"Human growth factor-like EGF","start":762,"end":783},{"id":"PF12661","name":"Human growth factor-like EGF","start":954,"end":975},{"id":"PF12661","name":"Human growth factor-like EGF","start":992,"end":1013},{"id":"PF12661","name":"Human growth factor-like EGF","start":1357,"end":1374},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":1913,"end":1989},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":2046,"end":2113}],"gene3D":[{"start":1871,"end":2126,"id":"1.25.40.20","name":"Ankyrin repeat-containing domain"},{"start":103,"end":142,"id":"2.10.25.10","name":"Laminin"},{"start":1351,"end":1386,"id":"2.10.25.10","name":"Laminin"},{"start":1184,"end":1223,"id":"2.10.25.10","name":"Laminin"},{"start":1387,"end":1429,"id":"2.10.25.10","name":"Laminin"},{"start":604,"end":643,"id":"2.10.25.10","name":"Laminin"},{"start":415,"end":453,"id":"2.10.25.10","name":"Laminin"},{"start":792,"end":828,"id":"2.10.25.10","name":"Laminin"},{"start":58,"end":100,"id":"2.10.25.10","name":"Laminin"},{"start":1147,"end":1183,"id":"2.10.25.10","name":"Laminin"},{"start":754,"end":791,"id":"2.10.25.10","name":"Laminin"},{"start":374,"end":414,"id":"2.10.25.10","name":"Laminin"},{"start":829,"end":871,"id":"2.10.25.10","name":"Laminin"},{"start":1445,"end":1566,"id":"3.30.300.320","name":"3.30.300.320"},{"start":1023,"end":1058,"id":"2.10.25.10","name":"Laminin"},{"start":337,"end":373,"id":"2.10.25.10","name":"Laminin"},{"start":260,"end":297,"id":"2.10.25.10","name":"Laminin"},{"start":531,"end":567,"id":"2.10.25.10","name":"Laminin"},{"start":221,"end":259,"id":"2.10.25.10","name":"Laminin"},{"start":1567,"end":1740,"id":"3.30.70.3310","name":"3.30.70.3310"},{"start":454,"end":491,"id":"2.10.25.10","name":"Laminin"},{"start":1309,"end":1350,"id":"2.10.25.10","name":"Laminin"},{"start":872,"end":907,"id":"2.10.25.10","name":"Laminin"},{"start":908,"end":944,"id":"2.10.25.10","name":"Laminin"},{"start":568,"end":603,"id":"2.10.25.10","name":"Laminin"},{"start":1113,"end":1146,"id":"2.10.25.10","name":"Laminin"},{"start":492,"end":530,"id":"2.10.25.10","name":"Laminin"},{"start":986,"end":1022,"id":"2.10.25.10","name":"Laminin"},{"start":1269,"end":1308,"id":"2.10.25.10","name":"Laminin"},{"start":644,"end":680,"id":"2.10.25.10","name":"Laminin"},{"start":298,"end":336,"id":"2.10.25.10","name":"Laminin"},{"start":181,"end":217,"id":"2.10.25.10","name":"Laminin"},{"start":1227,"end":1268,"id":"2.10.25.10","name":"Laminin"},{"start":717,"end":753,"id":"2.10.25.10","name":"Laminin"},{"start":1061,"end":1106,"id":"2.10.25.10","name":"Laminin"},{"start":681,"end":716,"id":"2.10.25.10","name":"Laminin"},{"start":143,"end":180,"id":"2.10.25.10","name":"Laminin"},{"start":945,"end":985,"id":"2.10.25.10","name":"Laminin"}]},"uniref50":"UniRef50_P46531","sequence":"MPPLLAPLLCLALLPALAARGPRCSQPGETCLNGGKCEAANGTEACVCGGAFVGPRCQDPNPCLSTPCKNAGTCHVVDRRGVADYACSCALGFSGPLCLTPLDNACLTNPCRNGGTCDLLTLTEYKCRCPPGWSGKSCQQADPCASNPCANGGQCLPFEASYICHCPPSFHGPTCRQDVNECGQKPGLCRHGGTCHNEVGSYRCVCRATHTGPNCERPYVPCSPSPCQNGGTCRPTGDVTHECACLPGFTGQNCEENIDDCPGNNCKNGGACVDGVNTYNCRCPPEWTGQYCTEDVDECQLMPNACQNGGTCHNTHGGYNCVCVNGWTGEDCSENIDDCASAACFHGATCHDRVASFYCECPHGRTGLLCHLNDACISNPCNEGSNCDTNPVNGKAICTCPSGYTGPACSQDVDECSLGANPCEHAGKCINTLGSFECQCLQGYTGPRCEIDVNECVSNPCQNDATCLDQIGEFQCICMPGYEGVHCEVNTDECASSPCLHNGRCLDKINEFQCECPTGFTGHLCQYDVDECASTPCKNGAKCLDGPNTYTCVCTEGYTGTHCEVDIDECDPDPCHYGSCKDGVATFTCLCRPGYTGHHCETNINECSSQPCRHGGTCQDRDNAYLCFCLKGTTGPNCEINLDDCASSPCDSGTCLDKIDGYECACEPGYTGSMCNINIDECAGNPCHNGGTCEDGINGFTCRCPEGYHDPTCLSEVNECNSNPCVHGACRDSLNGYKCDCDPGWSGTNCDINNNECESNPCVNGGTCKDMTSGYVCTCREGFSGPNCQTNINECASNPCLNQGTCIDDVAGYKCNCLLPYTGATCEVVLAPCAPSPCRNGGECRQSEDYESFSCVCPTGWQGQTCEVDINECVLSPCRHGASCQNTHGGYRCHCQAGYSGRNCETDIDDCRPNPCHNGGSCTDGINTAFCDCLPGFRGTFCEEDINECASDPCRNGANCTDCVDSYTCTCPAGFSGIHCENNTPDCTESSCFNGGTCVDGINSFTCLCPPGFTGSYCQHDVNECDSQPCLHGGTCQDGCGSYRCTCPQGYTGPNCQNLVHWCDSSPCKNGGKCWQTHTQYRCECPSGWTGLYCDVPSVSCEVAAQRQGVDVARLCQHGGLCVDAGNTHHCRCQAGYTGSYCEDLVDECSPSPCQNGATCTDYLGGYSCKCVAGYHGVNCSEEIDECLSHPCQNGGTCLDLPNTYKCSCPRGTQGVHCEINVDDCNPPVDPVSRSPKCFNNGTCVDQVGGYSCTCPPGFVGERCEGDVNECLSNPCDARGTQNCVQRVNDFHCECRAGHTGRRCESVINGCKGKPCKNGGTCAVASNTARGFICKCPAGFEGATCENDARTCGSLRCLNGGTCISGPRSPTCLCLGPFTGPECQFPASSPCLGGNPCYNQGTCEPTSESPFYRCLCPAKFNGLLCHILDYSFGGGAGRDIPPPLIEEACELPECQEDAGNKVCSLQCNNHACGWDGGDCSLNFNDPWKNCTQSLQCWKYFSDGHCDSQCNSAGCLFDGFDCQRAEGQCNPLYDQYCKDHFSDGHCDQGCNSAECEWDGLDCAEHVPERLAAGTLVVVVLMPPEQLRNSSFHFLRELSRVLHTNVVFKRDAHGQQMIFPYYGREEELRKHPIKRAAEGWAAPDALLGQVKASLLPGGSEGGRRRRELDPMDVRGSIVYLEIDNRQCVQASSQCFQSATDVAAFLGALASLGSLNIPYKIEAVQSETVEPPPPAQLHFMYVAAAAFVLLFFVGCGVLLSRKRRRQHGQLWFPEGFKVSEASKKKRREPLGEDSVGLKPLKNASDGALMDDNQNEWGDEDLETKKFRFEEPVVLPDLDDQTDHRQWTQQHLDAADLRMSAMAPTPPQGEVDADCMDVNVRGPDGFTPLMIASCSGGGLETGNSEEEEDAPAVISDFIYQGASLHNQTDRTGETALHLAARYSRSDAAKRLLEASADANIQDNMGRTPLHAAVSADAQGVFQILIRNRATDLDARMHDGTTPLILAARLAVEGMLEDLINSHADVNAVDDLGKSALHWAAAVNNVDAAVVLLKNGANKDMQNNREETPLFLAAREGSYETAKVLLDHFANRDITDHMDRLPRDIAQERMHHDIVRLLDEYNLVRSPQLHGAPLGGTPTLSPPLCSPNGYLGSLKPGVQGKKVRKPSSKGLACGSKEAKDLKARRKKSQDGKGCLLDSSGMLSPVDSLESPHGYLSDVASPPLLPSPFQQSPSVPLNHLPGMPDTHLGIGHLNVAAKPEMAALGGGGRLAFETGPPRLSHLPVASGTSTVLGSSSGGALNFTVGGSTSLNGQCEWLSRLQSGMVPNQYNPLRGSVAPGPLSTQAPSLQHGMVGPLHSSLAASALSQMMSYQGLPSTRLATQPHLVQTQQVQPQNLQMQQQNLQPANIQQQQSLQPPPPPPQPHLGVSSAASGHLGRSFLSGEPSQADVQPLGPSSLAVHTILPQESPALPTSLPSSLVPPVTAAQFLTPPSQHSYSSPVDNTPSHQLQVPEHPFLTPSPESPDQWSSSSPHSNVSDWSEGVSSPPTSMQSQIARIPEAFK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P46531","disprot_id":"DP01104","ncbi_taxon_id":9606,"regions_counter":2,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1888,"region_id":"DP01104r001","released":"2022_03","ec_id":"ECO:0006198","reference_html":"Effects of Linker Length and Transient Secondary Structure Elements in the Intrinsically Disordered Notch RAM Region on Notch Signaling. <i> Sherry KP, Johnson SE, Hatem CL, Majumdar A, Barrick D. </i> J Mol Biol, 2015","term_id":"IDPO:0000002","curator_id":"mnecci","start":1758,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"26344835","version":2,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":1888,"term_name":"ADP-ribosylation display site","start":1758,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"26344835","version":2,"reference_html":"Effects of Linker Length and Transient Secondary Structure Elements in the Intrinsically Disordered Notch RAM Region on Notch Signaling. <i> Sherry KP, Johnson SE, Hatem CL, Majumdar A, Barrick D. </i> J Mol Biol, 2015","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000038","ec_id":"ECO:0006198","region_id":"DP01104r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2016_10","uniref100":"UniRef100_P46531","date":"2016-09-22T17:03:02.000Z","acc":"P46531","name":"Neurogenic locus notch homolog protein 1","length":2555,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI0000E8261B","genes":[{"name":{"value":"NOTCH1"},"synonyms":[{"value":"TAN1"}]}],"alphafold_very_low_content":0.2731898238747554,"disorder_content":0.0512720156555773,"disprot_consensus":{"full":[{"start":1758,"end":1888,"type":"D"}],"Structural state":[{"start":1758,"end":1888,"type":"D"}],"Disorder function":[{"start":1758,"end":1888,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":340,"end":583},{"id":"PF00130","name":"Phorbol esters/diacylglycerol binding domain (C1 domain)","start":37,"end":87},{"id":"PF00130","name":"Phorbol esters/diacylglycerol binding domain (C1 domain)","start":102,"end":153},{"id":"PF00168","name":"C2 domain","start":172,"end":276},{"id":"PF00433","name":"Protein kinase C terminal domain","start":624,"end":658}],"gene3D":[{"start":156,"end":292,"id":"2.60.40.150","name":"C2 domain"},{"start":21,"end":89,"id":"3.30.60.20","name":"3.30.60.20"},{"start":424,"end":616,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"},{"start":94,"end":151,"id":"3.30.60.20","name":"3.30.60.20"},{"start":336,"end":423,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":617,"end":670,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"}]},"uniref50":"UniRef50_P17252","sequence":"MADVYPANDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINDPSLCGMDHTEKRGRIYLKAEVTDEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSNLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKAHNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPVGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLNNVMLNSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLMTKQPAKRLGCGPEGERDVREHAFFRRIDWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVNPQFVHPILQSAV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P17252","disprot_id":"DP01105","ncbi_taxon_id":10090,"regions_counter":7,"creator":"mnecci","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":672,"region_id":"DP01105r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The C-terminal V5 domain of Protein Kinase Cα is intrinsically disordered, with propensity to associate with a membrane mimetic. <i> Yang Y, Igumenova TI. </i> PLoS One, 2013","term_id":"IDPO:0000002","curator_id":"mnecci","start":606,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"23762412","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":672,"term_name":"limited proteolysis display site","start":606,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"23762412","version":2,"reference_html":"The C-terminal V5 domain of Protein Kinase Cα is intrinsically disordered, with propensity to associate with a membrane mimetic. <i> Yang Y, Igumenova TI. </i> PLoS One, 2013","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000048","ec_id":"ECO:0006204","region_id":"DP01105r002","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":672,"term_name":"lipid binding","start":606,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"23762412","version":3,"reference_html":"The C-terminal V5 domain of Protein Kinase Cα is intrinsically disordered, with propensity to associate with a membrane mimetic. <i> Yang Y, Igumenova TI. </i> PLoS One, 2013","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008289","ec_id":"ECO:0006204","region_id":"DP01105r003","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":672,"region_id":"DP01105r004","released":"2022_03","ec_id":"ECO:0006198","reference_html":"The C-terminal V5 domain of Protein Kinase Cα is intrinsically disordered, with propensity to associate with a membrane mimetic. <i> Yang Y, Igumenova TI. </i> PLoS One, 2013","term_id":"IDPO:0000002","curator_id":"mnecci","start":606,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"23762412","version":2,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":672,"term_name":"limited proteolysis display site","start":606,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"23762412","version":2,"reference_html":"The C-terminal V5 domain of Protein Kinase Cα is intrinsically disordered, with propensity to associate with a membrane mimetic. <i> Yang Y, Igumenova TI. </i> PLoS One, 2013","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000048","ec_id":"ECO:0006198","region_id":"DP01105r005","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":672,"term_name":"disorder to order","start":606,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"23762412","version":2,"reference_html":"The C-terminal V5 domain of Protein Kinase Cα is intrinsically disordered, with propensity to associate with a membrane mimetic. <i> Yang Y, Igumenova TI. </i> PLoS One, 2013","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006198","region_id":"DP01105r006","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":672,"term_name":"lipid binding","start":606,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","curator_id":"mnecci","released":"2022_03","term_ontology":"GO","curator_name":"Marco Necci","reference_id":"23762412","version":3,"reference_html":"The C-terminal V5 domain of Protein Kinase Cα is intrinsically disordered, with propensity to associate with a membrane mimetic. <i> Yang Y, Igumenova TI. </i> PLoS One, 2013","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008289","ec_id":"ECO:0006198","region_id":"DP01105r007","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2016_10","uniref100":"UniRef100_P20444","date":"2016-09-23T12:05:41.000Z","acc":"P20444","name":"Protein kinase C alpha type","length":672,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000281FB","genes":[{"name":{"value":"Prkca"},"synonyms":[{"value":"Pkca"}]}],"alphafold_very_low_content":0.09672619047619048,"disorder_content":0.09970238095238096,"disprot_consensus":{"full":[{"start":606,"end":672,"type":"T"}],"Structural state":[{"start":606,"end":672,"type":"D"}],"Disorder function":[{"start":606,"end":672,"type":"F"}],"Molecular function":[{"start":606,"end":672,"type":"F"}],"Structural transition":[{"start":606,"end":672,"type":"T"}]}},{"features":{"pfam":[{"id":"PF09067","name":"Erythropoietin receptor, ligand binding","start":25,"end":120}],"gene3D":[{"start":126,"end":234,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":25,"end":125,"id":"2.60.40.10","name":"Immunoglobulins"}]},"uniref50":"UniRef50_P16471","sequence":"MKENVASATVFTLLLFLNTCLLNGQLPPGKPEIFKCRSPNKETFTCWWRPGTDGGLPTNYSLTYHREGETLMHECPDYITGGPNSCHFGKQYTSMWRTYIMMVNATNQMGSSFSDELYVDVTYIVQPDPPLELAVEVKQPEDRKPYLWIKWSPPTLIDLKTGWFTLLYEIRLKPEKAAEWEIHFAGQQTEFKILSLHPGQKYLVQVRCKPDHGYWSAWSPATFIQIPSDFTMNDTTVWISVAVLSAVICLIIVWAVALKGYSMVTCIFPPVPGPKIKGFDAHLLEKGKSEELLSALGCQDFPPTSDYEDLLVEYLEVDDSEDQHLMSVHSKEHPSQGMKPTYLDPDTDSGRGSCDSPSLLSEKCEEPQANPSTFYDPEVIEKPENPETTHTWDPQCISMEGKIPYFHAGGSKCSTWPLPQPSQHNPRSSYHNITDVCELAVGPAGAPATLLNEAGKDALKSSQTIKSREEGKATQQREVESFHSETDQDTPWLLPQEKTPFGSAKPLDYVEIHKVNKDGALSLLPKQRENSGKPKKPGTPENNKEYAKVSGVMDNNILVLVPDPHAKNVACFEESAKEAPPSLEQNQAEKALANFTATSSKCRLQLGGLDYLDPACFTHSFH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P16471","disprot_id":"DP01106","ncbi_taxon_id":9606,"regions_counter":18,"creator":"epapa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":598,"region_id":"DP01106r001","released":"2022_12","ec_id":"ECO:0006210","reference_html":"Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes. <i> Haxholm GW, Nikolajsen LF, Olsen JG, Fredsted J, Larsen FH, Goffin V, Pedersen SF, Brooks AJ, Waters MJ, Kragelund BB. </i> Biochem J, 2015","term_id":"IDPO:0000002","curator_id":"vnugnes","start":236,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"25846210","version":3,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","date":"2022-09-06T13:47:56.408Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"To improve our understanding of signalling, we aimed at providing an in-depth characterization and focused on the full-length recombinantly expressed long isoform of the human PRLR-ICD (Gly236–His598) with an N-terminal His6-tag (PRLRICDFL,His; Figure 1B)."}]}],"statement":[{"text":"A large negative minimum at 200 nm in the far-UV CD spectrum (Figure 1C) together with a linearly increasing Kratky plot obtained by SAXS (Figure 1D) collectively suggested that PRLR-ICDFL,His was highly disordered with a low content of secondary structure.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":598,"region_id":"DP01106r005","released":"2022_12","ec_id":"ECO:0006204","reference_html":"Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes. <i> Haxholm GW, Nikolajsen LF, Olsen JG, Fredsted J, Larsen FH, Goffin V, Pedersen SF, Brooks AJ, Waters MJ, Kragelund BB. </i> Biochem J, 2015","term_id":"IDPO:0000002","curator_id":"vnugnes","start":236,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"25846210","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-09-06T13:44:52.034Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"To improve our understanding of signalling, we aimed at providing an in-depth characterization and focused on the full-length recombinantly expressed long isoform of the human PRLR-ICD (Gly236–His598) with an N-terminal His6-tag (PRLRICDFL,His; Figure 1B)."}]}],"statement":[{"text":"A large negative minimum at 200 nm in the far-UV CD spectrum (Figure 1C) together with a linearly increasing Kratky plot obtained by SAXS (Figure 1D) collectively suggested that PRLR-ICDFL,His was highly disordered with a low\ncontent of secondary structure.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":598,"region_id":"DP01106r009","released":"2022_12","ec_id":"ECO:0005642","reference_html":"Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes. <i> Haxholm GW, Nikolajsen LF, Olsen JG, Fredsted J, Larsen FH, Goffin V, Pedersen SF, Brooks AJ, Waters MJ, Kragelund BB. </i> Biochem J, 2015","term_id":"IDPO:0000002","curator_id":"vnugnes","start":236,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"25846210","version":3,"ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","date":"2022-09-06T13:47:22.372Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"To improve our understanding of signalling, we aimed at providing an in-depth characterization and focused on the full-length recombinantly expressed long isoform of the human PRLR-ICD (Gly236–His598) with an N-terminal His6-tag (PRLRICDFL,His; Figure 1B)."}]}],"statement":[{"text":"Furthermore, the 1 H-15N-HSQC spectrum of PRLR-ICDFL,His obtained by NMR spectroscopy (Figure 1E) showed low dispersion of signals in the proton dimension, characteristic of IDPs [39] and similar to data obtained for gp130 [10].","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":396,"region_id":"DP01106r013","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A combined computational and structural model of the full-length human prolactin receptor. <i> Bugge K, Papaleo E, Haxholm GW, Hopper JT, Robinson CV, Olsen JG, Lindorff-Larsen K, Kragelund BB. </i> Nat Commun, 2016","statement":[{"text":"NMR diffusion experiments were applied to measure the hydrodynamic radius (RH) of hPRLR-ICD to 74 ű1 Å.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"epapa","start":236,"term_ontology":"IDPO","curator_name":"Elena Papaleo","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27174498","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":236,"end":396,"reference_id":"25846210","reference_source":"pmid","reference_html":"Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes. <i> Haxholm GW, Nikolajsen LF, Olsen JG, Fredsted J, Larsen FH, Goffin V, Pedersen SF, Brooks AJ, Waters MJ, Kragelund BB. </i> Biochem J, 2015","date":"2022-09-06T14:20:49.102Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001226","ec_ontology":"ECO","ec_name":"lipid binding assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"18303","operator":null,"partner_start":null,"partner_end":null},{"db":"ChEBI","id":"16038","operator":"or","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"28874","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP01106r014","statement":[{"text":"First, lipid-binding specificity was assessed using lipid strips pre-dotted with different phospholipids and PRLR-ICDmp specifically recognized only negatively charged phospholipids [phosphatidylserine (PS), phosphatidylethanolamine (PE) and\nphosphatidylinositol phosphates (PIPs)] (Supplementary Figure S2). These lipids are hallmarks of the inner plasma membrane leaflet [46] and, importantly, PRLR-ICDmp did not recognize phosphatidylcholine (PC; Supplementary Figure S2), which is an outer leaflet constituent [46].","type":"Results"},{"text":"As seen from Figure 2(C), addition of POPC/POPS SUV to the PRLRICDFL resulted in chemical shift changes in all three identified LIDs and thus confirmed the results obtained using the truncated variants. Moreover, since the chemical shift changes of the resolved residues of the truncated and full-length PRLR-ICD variants were similar, each LID of the PRLR-ICD appeared to associate with the lipids independently most probably due to the long disordered regions separating them.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":236,"end":300,"reference_id":"25846210","reference_source":"pmid","reference_html":"Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes. <i> Haxholm GW, Nikolajsen LF, Olsen JG, Fredsted J, Larsen FH, Goffin V, Pedersen SF, Brooks AJ, Waters MJ, Kragelund BB. </i> Biochem J, 2015","date":"2022-09-06T14:21:02.785Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"73001","operator":null,"partner_start":null,"partner_end":null},{"db":"ChEBI","id":"74909","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP01106r015","statement":[{"text":"Large confined chemical shift changes were observed for residues Glu245–His300 and the majority of signals from Gly236–Phe244 disappeared as a result of binding, thus identifying a LID1 comprising residues Gly236– His300 (Figure 2B). The chemical shifts of residues Phe350– His383 were also affected by the presence of POPC/POPS SUVs thereby defining a second LID, LID2 (Figure 2B).","type":"Results"},{"text":"As seen from Figure 2(C), addition of POPC/POPS SUV to the PRLRICDFL resulted in chemical shift changes in all three identified LIDs and thus confirmed the results obtained using the truncated variants. Moreover, since the chemical shift changes of the resolved residues of the truncated and full-length PRLR-ICD variants were similar, each LID of the PRLR-ICD appeared to associate with the lipids independently most probably due to the long disordered regions separating them.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":350,"end":383,"reference_id":"25846210","reference_source":"pmid","reference_html":"Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes. <i> Haxholm GW, Nikolajsen LF, Olsen JG, Fredsted J, Larsen FH, Goffin V, Pedersen SF, Brooks AJ, Waters MJ, Kragelund BB. </i> Biochem J, 2015","date":"2022-09-06T14:14:44.113Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"73001","operator":null,"partner_start":null,"partner_end":null},{"db":"ChEBI","id":"74909","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP01106r016","statement":[{"text":"Large confined chemical shift changes were observed for residues Glu245–His300 and the majority of signals from Gly236–Phe244 disappeared as a result of binding, thus identifying a LID1 comprising residues Gly236– His300 (Figure 2B). The chemical shifts of residues Phe350– His383 were also affected by the presence of POPC/POPS SUVs thereby defining a second LID, LID2 (Figure 2B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":547,"end":598,"reference_id":"25846210","reference_source":"pmid","reference_html":"Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes. <i> Haxholm GW, Nikolajsen LF, Olsen JG, Fredsted J, Larsen FH, Goffin V, Pedersen SF, Brooks AJ, Waters MJ, Kragelund BB. </i> Biochem J, 2015","date":"2022-09-06T14:20:37.125Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"73001","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01106r017","statement":[{"text":"Following the same strategy as for PRLR-ICDmp, POPS specificity was observed for PRLR-ICDmd using 31P-NMR (Figure 2A) and chemical shift changes obtained from 1 H-15NHSQC spectra identified an additional LID3 in PRLR-ICDmd comprising residues Cys547-His598 (Figure 2B).","type":"Results"},{"text":"As seen from Figure 2(C), addition of POPC/POPS SUV to the PRLRICDFL resulted in chemical shift changes in all three identified LIDs and thus confirmed the results obtained using the truncated variants. Moreover, since the chemical shift changes of the resolved residues of the truncated and full-length PRLR-ICD variants were similar, each LID of the PRLR-ICD appeared to associate with the lipids independently most probably due to the long disordered regions separating them.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":281,"end":285,"reference_id":"25846210","reference_source":"pmid","reference_html":"Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes. <i> Haxholm GW, Nikolajsen LF, Olsen JG, Fredsted J, Larsen FH, Goffin V, Pedersen SF, Brooks AJ, Waters MJ, Kragelund BB. </i> Biochem J, 2015","date":"2022-09-06T14:46:55.053Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP01106r018","statement":[{"text":"Using in vitro kinase assays, we investigated whether incubation with these active kinases could phosphorylate PRLR-ICDmp and showed that Lyn, Fyn and c-Src resulted in tyrosine phosphorylation (Figure 5A, lanes 3–5), whereas Jak2 and Fgr\ndid not (Figure 5A, lanes 2 and 6).","type":"Results"},{"text":"By reassigning the phosphorylated state, phosphorylation-induced chemical shift changes were seen to locate to residues Thr280– Tyr290 and most pronounced around residues Thr280–Glu284, thereby strongly indicating Tyr283 to be phosphorylated by Fyn.","type":"Results"}]}],"released":"2016_10","uniref100":"UniRef100_P16471","date":"2016-09-23T14:34:32.000Z","acc":"P16471","name":"Prolactin receptor","length":622,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000132234","genes":[{"name":{"value":"PRLR"}}],"alphafold_very_low_content":0.4630225080385852,"disorder_content":0.5836012861736335,"disprot_consensus":{"full":[{"start":236,"end":598,"type":"D"}],"Structural state":[{"start":236,"end":598,"type":"D"}],"Molecular function":[{"start":236,"end":396,"type":"F"},{"start":547,"end":598,"type":"F"}],"Disorder function":[{"start":281,"end":285,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":106,"end":164},{"id":"PF00076","name":"RNA recognition motif","start":193,"end":241},{"id":"PF18694","name":"TAR DNA-binding protein 43, N-terminal domain","start":4,"end":76},{"id":"PF20910","name":"TAR DNA-binding protein 43, C-terminal","start":262,"end":371}],"gene3D":[{"start":189,"end":269,"id":"3.30.70.330","name":"3.30.70.330"},{"start":92,"end":188,"id":"3.30.70.330","name":"3.30.70.330"}]},"uniref50":"UniRef50_Q13148","sequence":"MSEYIRVTEDENDEPIEIPSEDDGTVLLSTVTAQFPGACGLRYRNPVSQCMRGVRLVEGILHAPDAGWGNLVYVVNYPKDNKRKMDETDASSAVKVKRAVQKTSDLIVLGLPWKTTEQDLKEYFSTFGEVLMVQVKKDLKTGHSKGFGFVRFTEYETQVKVMSQRHMIDGRWCDCKLPNSKQSQDEPLRSRKVFVGRCTEDMTEDELREFFSQYGDVMDVFIPKPFRAFAFVTFADDQIAQSLCGEDLIIKGISVHISNAEPKHNSNRQLERSGRFGGNPGGFGNQGGFGNSRGGGAGLGNNQGSNMGGGMNFGAFSINPAMMAAAQAALQSSWGMMGMLASQQNQSGPSGNNQNQGNMQREPNQAFGSGNNSYSGSNSGAAIGWGSASNAGSGSGFNGGFGSSMDSKSSGWGM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q13148","disprot_id":"DP01108","ncbi_taxon_id":9606,"regions_counter":40,"creator":"bjuhasz","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":414,"region_id":"DP01108r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"TAR DNA-binding protein 43 (TDP-43) liquid-liquid phase separation is mediated by just a few aromatic residues. <i> Li HR, Chiang WC, Chou PC, Wang WJ, Huang JR. </i> J Biol Chem, 2018","statement":[{"text":"Furthermore, the fact that the LLPS of this intrinsically disordered domain is controlled by just a few residues may explain the unusual droplet form of TDP-43 (9).","type":"Figure"},{"text":"The HSQC showed in the article is a typical IDP spectra, but it was taken for granted and not specified.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":266,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29511089","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:01:57.798Z"}},{"start":266,"end":414,"reference_id":"29511089","reference_source":"pmid","reference_html":"TAR DNA-binding protein 43 (TDP-43) liquid-liquid phase separation is mediated by just a few aromatic residues. <i> Li HR, Chiang WC, Chou PC, Wang WJ, Huang JR. </i> J Biol Chem, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01108r003","statement":[{"text":"We also collected time-lapse micrographs from low to high and then back to low temperatures to confirm the reversibility of the process (Fig. 2C, and supporting Movie S1).","type":"Results"},{"text":"At 5 °C and a protein concentration of 20 μm, clear evidence of LLPS was only observed for the WT sample (Fig. 3A).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:02:57.644Z"}},{"start":266,"end":414,"reference_id":"29511089","reference_source":"pmid","reference_html":"TAR DNA-binding protein 43 (TDP-43) liquid-liquid phase separation is mediated by just a few aromatic residues. <i> Li HR, Chiang WC, Chou PC, Wang WJ, Huang JR. </i> J Biol Chem, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006307","ec_ontology":"ECO","ec_name":"turbidity measurement evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01108r004","statement":[{"text":"We measured the turbidity of the WT sample (the optical density at 600 nm, OD600 nm, Fig. 2A) and recorded micrographs of the condensates at different static temperatures (Fig. 2B) to confirm the occurrence of LLPS.","type":"Results"},{"text":"At 5 °C and a protein concentration of 20 μm, clear evidence of LLPS was only observed for the WT sample (Fig. 3A).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:02:56.907Z"}},{"start":267,"end":414,"reference_id":"27545621","reference_source":"pmid","reference_html":"ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain. <i> Conicella AE, Zerze GH, Mittal J, Fawzi NL. </i> Structure, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01108r005","statement":[{"text":"The two dimensional NMR spectrum of the TDP-43 C-terminal domain serves as a fingerprint of protein structure, with a narrow range of 1H chemical shifts consistent with predominant disorder (Figure 1A).","type":"Results"},{"text":"For the majority of the domain, the difference between the observed Cα and Cβ chemical shift values and those predicted for an entirely disordered protein, δΔCα-δΔCβ, do not exceed ±0.75 ppm, consistent with intrinsic disorder.","type":"Results"},{"text":"The narrow assigned 1H-15N HSQC of TDP-43267–414 suggests the domain is primarily intrinsically disordered.","type":"Figure"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:01:56.505Z"}},{"start":267,"end":414,"reference_id":"27545621","reference_source":"pmid","reference_html":"ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain. <i> Conicella AE, Zerze GH, Mittal J, Fawzi NL. </i> Structure, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01108r006","statement":[{"text":"However, upon addition of 150 mM NaCl, the domain rapidly undergoes LLPS (Figure 3A top). These assemblies appear as dynamic, high protein concentration liquid droplets that flow and fuse and show effectively complete fluorescence recovery after photobleaching (FRAP), highlighting their liquid-like character (Figure 3C and Movie S1).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:02:55.404Z"}},{"start":267,"end":414,"reference_id":"27545621","reference_source":"pmid","reference_html":"ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain. <i> Conicella AE, Zerze GH, Mittal J, Fawzi NL. </i> Structure, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006067","ec_ontology":"ECO","ec_name":"fluorescence recovery after photobleaching evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01108r007","statement":[{"text":"However, upon addition of 150 mM NaCl, the domain rapidly undergoes LLPS (Figure 3A top). These assemblies appear as dynamic, high protein concentration liquid droplets that flow and fuse and show effectively complete fluorescence recovery after photobleaching (FRAP), highlighting their liquid-like character (Figure 3C and Movie S1).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:03:02.054Z"}},{"start":267,"end":414,"reference_id":"27545621","reference_source":"pmid","reference_html":"ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain. <i> Conicella AE, Zerze GH, Mittal J, Fawzi NL. </i> Structure, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006307","ec_ontology":"ECO","ec_name":"turbidity measurement evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01108r008","statement":[{"text":"The extent of phase separation increases with increasing salt concentration as monitored by turbidity.","type":"Figure"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:02:53.935Z"}},{"start":321,"end":343,"reference_id":"27545621","reference_source":"pmid","reference_html":"ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain. <i> Conicella AE, Zerze GH, Mittal J, Fawzi NL. </i> Structure, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006307","ec_ontology":"ECO","ec_name":"turbidity measurement evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01108r009","statement":[{"text":"Interestingly, both removal of the region harboring the α-helical structure and these mutations (Δ321–343) as well as introduction of the helix-breaking A326P resulted in loss of phase separation, suggesting that the helical region is important for LLPS. ","type":"Figure"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:02:52.289Z"}},{"start":266,"end":414,"reference_id":"28988034","reference_source":"pmid","reference_html":"The physical forces mediating self-association and phase-separation in the C-terminal domain of TDP-43. <i> Li HR, Chen TC, Hsiao CL, Shi L, Chou CY, Huang JR. </i> Biochim Biophys Acta Proteins Proteom, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01108r010","statement":[{"text":"The TDP-43266–414 variants undergo LLPS at different temperatures and have different NMR signal intensity profiles.","type":"Results"},{"text":"We observed that wild-type TDP-43266–414 showed reversible LLPS when we lowered the temperature (Fig. 2 a and b; all samples returned to the original transparency either from observing the microscope image or from its turbidity).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:02:51.251Z"}},{"start":266,"end":414,"reference_id":"28988034","reference_source":"pmid","reference_html":"The physical forces mediating self-association and phase-separation in the C-terminal domain of TDP-43. <i> Li HR, Chen TC, Hsiao CL, Shi L, Chou CY, Huang JR. </i> Biochim Biophys Acta Proteins Proteom, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006307","ec_ontology":"ECO","ec_name":"turbidity measurement evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01108r011","statement":[{"text":"The TDP-43266–414 variants undergo LLPS at different temperatures and have different NMR signal intensity profiles.","type":"Results"},{"text":"We observed that wild-type TDP-43266–414 showed reversible LLPS when we lowered the temperature (Fig. 2 a and b; all samples returned to the original transparency either from observing the microscope image or from its turbidity).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:02:50.659Z"}},{"start":266,"end":414,"reference_id":"28988034","reference_source":"pmid","reference_html":"The physical forces mediating self-association and phase-separation in the C-terminal domain of TDP-43. <i> Li HR, Chen TC, Hsiao CL, Shi L, Chou CY, Huang JR. </i> Biochim Biophys Acta Proteins Proteom, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0043232","term_name":"intracellular non-membrane-bounded organelle","term_namespace":"Cellular component","term_ontology":"GO","ec_id":"ECO:0006307","ec_ontology":"ECO","ec_name":"turbidity measurement evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01108r012","statement":[{"text":"We found that TDP-43266–414 turned into hydrogel even in 8 M urea when the protein concentration is high (above 500 μM).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Organized structure of distinctive morphology and function, not bounded by a lipid bilayer membrane and occurring within the cell. Includes ribosomes, the cytoskeleton and chromosomes.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:02:48.753Z"}},{"start":263,"end":414,"reference_id":"26735904","reference_source":"pmid","reference_html":"ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43. <i> Lim L, Wei Y, Lu Y, Song J. </i> PLoS Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01108r013","statement":[{"text":"As judged by its far-ultraviolet (UV) CD spectrum with the maximal negative signal at 199 nm and no positive signal at 190 nm (Fig 1B), it appears to be highly disordered without any stable secondary structure.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:01:55.021Z"}},{"start":263,"end":414,"reference_id":"26735904","reference_source":"pmid","reference_html":"ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43. <i> Lim L, Wei Y, Lu Y, Song J. </i> PLoS Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01108r014","statement":[{"text":"Moreover, it has a 1H-15N heteronuclear single quantum coherence spectroscopy (HSQC) spectrum with very narrow 1H (0.86 ppm) and 15N (17.84 ppm) spectral dispersions in which three Trp residues have their sidechain HSQC peaks largely overlapped (Fig 1C). These observations indicate that it also has no tight tertiary packing.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:01:54.722Z"}},{"start":263,"end":414,"reference_id":"26735904","reference_source":"pmid","reference_html":"ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43. <i> Lim L, Wei Y, Lu Y, Song J. </i> PLoS Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0043232","term_name":"intracellular non-membrane-bounded organelle","term_namespace":"Cellular component","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01108r015","statement":[{"text":"Interestingly, the sample, even at a concentration of 20 μM, started to self-associate in pH 6.8 buffer, as monitored by CD (Fig 1B). After 1 d, the CD signal intensity showed a slight reduction, while after 4 d, the CD spectrum changed dramatically which is similar to what have been observed on the soluble β-stranded oligomers formed by the peptides derived from the TDP-43 prion-like domain [43–45]. After 8 d, no further changes were detected and also no visible aggregate was formed. This implies that the wild-type prion-like domain is able to progressively assemble into larger but soluble oligomers at neutral pH. The deconvolution analysis of the CD spectra revealed that the soluble oligomer formed at 8 d contains ~3% helical but ~72% β-sheet and β-turn, as well as ~25% random coil conformations.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Organized structure of distinctive morphology and function, not bounded by a lipid bilayer membrane and occurring within the cell. Includes ribosomes, the cytoskeleton and chromosomes.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:02:48.060Z"}},{"start":263,"end":414,"reference_id":"26735904","reference_source":"pmid","reference_html":"ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43. <i> Lim L, Wei Y, Lu Y, Song J. </i> PLoS Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0043232","term_name":"intracellular non-membrane-bounded organelle","term_namespace":"Cellular component","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01108r016","statement":[{"text":"Even after 15 min, many HSQC peaks became broadened (Fig 1D), implying the occurrence of dynamic oligomerization. After 4 hr (Fig 1E) and 9 hr (Fig 1F), most peaks became very broad and consequently the intensity became weak. After 1 d, most peaks became too broad to be detectable (Fig 1G). Furthermore, the NMR sample in pH 6.8 buffer formed hydrogels after 1 d, which could change back to solution upon shaking, similar to what was also observed on the fused in sarcoma (FUS) prion-like domain [30,49]. However, higher protein concentrations such as at 200 μM would result in the rapid precipitation with white aggregates upon dilution into the buffer at pH 6.8.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Organized structure of distinctive morphology and function, not bounded by a lipid bilayer membrane and occurring within the cell. Includes ribosomes, the cytoskeleton and chromosomes.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:02:46.875Z"}},{"start":263,"end":414,"reference_id":"26735904","reference_source":"pmid","reference_html":"ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43. <i> Lim L, Wei Y, Lu Y, Song J. </i> PLoS Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01108r017","statement":[{"text":"Interestingly, as seen in S3E Fig, immediately upon dilution into the 1 mM phosphate buffer (pH 6.8), the wild type showed a large intensity of the ThT-binding induced fluorescence with the emission maximum at ~488 nm, implying its fast formation of the β-rich amyloid-like structure. After 1 d, the intensity was further increased and then reached the highest point after 2 d, followed by the reduction of the intensity afterward.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:02:45.711Z"}},{"start":263,"end":414,"reference_id":"26735904","reference_source":"pmid","reference_html":"ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43. <i> Lim L, Wei Y, Lu Y, Song J. </i> PLoS Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01108r018","statement":[{"text":"As seen in Fig 4A–4D, after one week, the wild type and three mutants were all able to form amyloid fibrillar structures, with the widths of fibrils ranging from 15 to 30 nm, similar to the fine structures that were detected in the neuronal TDP-43 inclusions in patients’ brain tissues [57].","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:02:44.296Z"}},{"start":263,"end":414,"reference_id":"26735904","reference_source":"pmid","reference_html":"ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43. <i> Lim L, Wei Y, Lu Y, Song J. </i> PLoS Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0043232","term_name":"intracellular non-membrane-bounded organelle","term_namespace":"Cellular component","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01108r019","statement":[{"text":"On the other hand, amorphous structures of diverse sizes were observed for the aggregates rapidly formed by diluting the wild type into 1 mM phosphate buffer at pH 6.8 to reach a concentration of 200 μM (Fig 4E).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Organized structure of distinctive morphology and function, not bounded by a lipid bilayer membrane and occurring within the cell. Includes ribosomes, the cytoskeleton and chromosomes.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:02:38.704Z"}},{"start":263,"end":414,"reference_id":"26735904","reference_source":"pmid","reference_html":"ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43. <i> Lim L, Wei Y, Lu Y, Song J. </i> PLoS Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01108r020","statement":[{"text":"Indeed, as characterized by CD spectroscopy, ssDNA was able to bind and trigger the significant conformational changes for the wild-type prion-like domain (S7A Fig).","type":"Results"},{"text":"As judged from CD spectra in the presence of DPC at different ratios (Fig 7C), gradual addition of DPC induces progressive increase of the helical conformation, with the significant transition occurring over the ratios 50–100 (prion:DPC).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:02:10.898Z"}},{"start":263,"end":414,"reference_id":"26735904","reference_source":"pmid","reference_html":"ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43. <i> Lim L, Wei Y, Lu Y, Song J. </i> PLoS Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01108r021","statement":[{"text":"Indeed, as characterized by CD spectroscopy, ssDNA was able to bind and trigger the significant conformational changes for the wild-type prion-like domain (S7A Fig).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:02:18.841Z"}},{"start":263,"end":414,"reference_id":"26735904","reference_source":"pmid","reference_html":"ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43. <i> Lim L, Wei Y, Lu Y, Song J. </i> PLoS Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01108r022","statement":[{"text":"However, upon addition of ssDNA at a ratio of 1:0.5 (protein:ssDNA), two very up-field peaks started to manifest and their intensity become much higher at a ratio of 1:1 (Fig 6A).","type":"Results"},{"text":"Very interestingly, for the wild type, although at a ratio of 1:0.5 many peaks became too broad to be detected mostly due to the involvement in forming the large oligomer, a set of HSQC peaks is still detectable and mostly superimposable to those in the free state (Fig 6B).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:02:17.966Z"}},{"start":263,"end":414,"reference_id":"26735904","reference_source":"pmid","reference_html":"ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43. <i> Lim L, Wei Y, Lu Y, Song J. </i> PLoS Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01108r023","statement":[{"text":"However, upon addition of ssDNA at a ratio of 1:0.5 (protein:ssDNA), two very up-field peaks started to manifest and their intensity become much higher at a ratio of 1:1 (Fig 6A).","type":"Results"},{"text":"Very interestingly, for the wild type, although at a ratio of 1:0.5 many peaks became too broad to be detected mostly due to the involvement in forming the large oligomer, a set of HSQC peaks is still detectable and mostly superimposable to those in the free state (Fig 6B).","type":"Results"},{"text":"SSP analysis and manifestation of a large amount of NOEs indicate that the membrane-interacting subdomain transforms into a well-folded structure in the membrane environment.","type":"Results"},{"text":"Furthermore, consistent with the CD results, HSQC titrations also showed that the prion-like domain underwent conformational changes with gradual addition of DPC, as indicated by the significant shifts of some HSQC peaks (Fig 7D and 7E).","type":"Results"}],"cross_refs":[{"db":"PDB","id":"2N2C"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:02:08.644Z"}},{"start":263,"end":414,"reference_id":"26735904","reference_source":"pmid","reference_html":"ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43. <i> Lim L, Wei Y, Lu Y, Song J. </i> PLoS Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01108r024","statement":[{"text":"As seen in Fig 7A, in the presence of bicelle at a ratio of 1:200 (prion:bicelle), the prion-like domain has a far-UV CD spectrum very different from that in aqueous solution, with the maximal negative signal shifted from 198 to 203 nm; and a new negative signal at 222 nm, implying that the prion-like domain indeed has the subdomain which can interact with membranes to form helical conformation.","type":"Results"},{"text":"As judged from CD spectra in the presence of DPC at different ratios (Fig 7C), gradual addition of DPC induces progressive increase of the helical conformation, with the significant transition occurring over the ratios 50–100 (prion:DPC).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:02:16.063Z"}},{"start":263,"end":414,"reference_id":"26735904","reference_source":"pmid","reference_html":"ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43. <i> Lim L, Wei Y, Lu Y, Song J. </i> PLoS Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"2N2C"}],"region_id":"DP01108r025","statement":[{"text":"Furthermore, in the presence of bicelle, many HSQC peaks underwent shifts and some even completely disappeared, as well as the peaks of three Trp side chains became well-separated (Fig 7B). This observation suggests that upon interacting with bicelle, each of Trp side chains has different chemical environment. Strikingly, the disappeared peaks were identified to be from residues Met307-Gln344, indicating that these residues became tightly associated with the large bicelle, consequently their HSQC peaks became too broad to be detected due to shortening of their T2 values [79].","type":"Results"},{"text":"Furthermore, consistent with the CD results, HSQC titrations also showed that the prion-like domain underwent conformational changes with gradual addition of DPC, as indicated by the significant shifts of some HSQC peaks (Fig 7D and 7E).","type":"Results"},{"text":"SSP analysis and manifestation of a large amount of NOEs indicate that the membrane-interacting subdomain transforms into a well-folded structure in the membrane environment.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:02:14.565Z"}}],"released":"2018_11","uniref100":"UniRef100_Q13148","date":"2018-06-18T15:36:33.000Z","acc":"Q13148","name":"TAR DNA-binding protein 43","length":414,"organism":"Homo sapiens","dataset":["Condensates-related proteins","RNA-binding proteins","Stress response proteins"],"UniParc":"UPI0000136B42","genes":[{"name":{"value":"TARDBP","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"18396105","url":"http://www.ncbi.nlm.nih.gov/pubmed/18396105","alternativeUrl":"https://europepmc.org/abstract/MED/18396105"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11571","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11571"}}]},"synonyms":[{"value":"TDP43","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"7745706","url":"http://www.ncbi.nlm.nih.gov/pubmed/7745706","alternativeUrl":"https://europepmc.org/abstract/MED/7745706"}}]}]}],"alphafold_very_low_content":0.3961352657004831,"disorder_content":0.3671497584541063,"disprot_consensus":{"full":[{"start":263,"end":414,"type":"T"}],"Structural state":[{"start":263,"end":414,"type":"D"}],"Molecular function":[{"start":263,"end":414,"type":"F"}],"Cellular component":[{"start":263,"end":414,"type":"F"}],"Biological process":[{"start":263,"end":414,"type":"F"}],"Structural transition":[{"start":263,"end":414,"type":"T"}]}},{"acc":"P22626","sequence":"MEKTLETVPLERKKREKEQFRKLFIGGLSFETTEESLRNYYEQWGKLTDCVVMRDPASKRSRGFGFVTFSSMAEVDAAMAARPHSIDGRVVEPKRAVAREESGKPGAHVTVKKLFVGGIKEDTEEHHLRDYFEEYGKIDTIEIITDRQSGKKRGFGFVTFDDHDPVDKIVLQKYHTINGHNAEVRKALSRQEMQEVQSSRSGRGGNFGFGDSRGGGGNFGPGPGSNFRGGSDGYGSGRGFGDGYNGYGGGPGGGNFGGSPGYGGGRGGYGGGGPGYGNQGGGYGGGYDNYGGGNYGSGNYNDFGNYNQQPSNYGPMKSGNFGGSRNMGGPYGGGNYGPGGSGGSGGYGGRSRY","alphafold_very_low_content":"0.4164305949008499","creator":"tlazar","dataset":["Condensates-related proteins","Cancer-related proteins","RNA-binding proteins"],"date":"2018-06-18T15:48:48.000Z","disprot_id":"DP01109","features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":23,"end":88},{"id":"PF00076","name":"RNA recognition motif","start":114,"end":172},{"id":"PF11627","name":"Heterogeneous nuclear ribonucleoprotein A1, LC domain","start":296,"end":334}],"gene3D":[{"start":107,"end":187,"id":"3.30.70.330","name":"3.30.70.330","_id":"685af523b4ac24d5329d8bb6"},{"start":15,"end":96,"id":"3.30.70.330","name":"3.30.70.330","_id":"685af523b4ac24d5329d8bb7"}]},"genes":[{"name":{"value":"HNRNPA2B1","evidences":[],"_id":"685af523b4ac24d5329d8bc8"},"synonyms":[{"value":"HNRPA2B1","evidences":[],"_id":"685af523b4ac24d5329d8bc9"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d8bc7"}],"length":353,"name":"Heterogeneous nuclear ribonucleoproteins A2/B1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":5,"released":"2018_11","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI000002B298","uniref100":"UniRef100_P22626","uniref50":"UniRef50_P22626","uniref90":"UniRef90_P22626","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":190,"end":341,"interaction_partner":[],"reference_html":"Mechanistic View of hnRNPA2 Low-Complexity Domain Structure, Interactions, and Phase Separation Altered by Mutation and Arginine Methylation. <i> Ryan VH, Dignon GL, Zerze GH, Chabata CV, Silva R, Conicella AE, Amaya J, Burke KA, Mittal J, Fawzi NL. </i> Mol Cell, 2018","reference_id":"29358076","region_id":"DP01109r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The two-dimensional 1H-15N NMR correlation spectra (heteronuclear single quantum coherence, HSQC) of wild type (WT), D290V, and P298L hnRNPA2 LC have a narrow chemical shift range, characteristic of a disordered protein (Figure 1A).","_id":"685af523b4ac24d5329d8bb9"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-06-22T15:07:45.770Z","_id":"685af523b4ac24d5329d8bba"},"version":3,"_id":"685af523b4ac24d5329d8bb8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006307","ec_name":"turbidity measurement evidence used in manual assertion","ec_ontology":"ECO","start":190,"end":341,"interaction_partner":[],"reference_html":"Mechanistic View of hnRNPA2 Low-Complexity Domain Structure, Interactions, and Phase Separation Altered by Mutation and Arginine Methylation. <i> Ryan VH, Dignon GL, Zerze GH, Chabata CV, Silva R, Conicella AE, Amaya J, Burke KA, Mittal J, Fawzi NL. </i> Mol Cell, 2018","reference_id":"29358076","region_id":"DP01109r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In addition, all hnRNPA2 LC variants show initial turbidity consistent with liquid-liquid phase separation but only D290V and P298L show turbidity at time points longer than 3 hours (Figure S4A), suggesting formation of static aggregates.","_id":"685af523b4ac24d5329d8bbf"}],"states_connection":[],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_id":"GO:0140693","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-06-22T15:07:49.051Z","_id":"685af523b4ac24d5329d8bc0"},"version":1,"_id":"685af523b4ac24d5329d8bbe","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006067","ec_name":"fluorescence recovery after photobleaching evidence used in manual assertion","ec_ontology":"ECO","start":190,"end":341,"interaction_partner":[],"reference_html":"Mechanistic View of hnRNPA2 Low-Complexity Domain Structure, Interactions, and Phase Separation Altered by Mutation and Arginine Methylation. <i> Ryan VH, Dignon GL, Zerze GH, Chabata CV, Silva R, Conicella AE, Amaya J, Burke KA, Mittal J, Fawzi NL. </i> Mol Cell, 2018","reference_id":"29358076","region_id":"DP01109r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"At 50 mM NaCl, FRAP experiments indicate that droplets of WT, D290V, P298L are liquid at early time points, as the fluorescent signal redistributes after bleaching part of individual droplets (Figure 3D).","_id":"685af523b4ac24d5329d8bc2"}],"states_connection":[],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_id":"GO:0140693","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-06-22T15:07:47.894Z","_id":"685af523b4ac24d5329d8bc3"},"version":1,"_id":"685af523b4ac24d5329d8bc1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0001232","ec_name":"microscopy evidence used in manual assertion","ec_ontology":"ECO","start":190,"end":341,"interaction_partner":[],"reference_html":"Mechanistic View of hnRNPA2 Low-Complexity Domain Structure, Interactions, and Phase Separation Altered by Mutation and Arginine Methylation. <i> Ryan VH, Dignon GL, Zerze GH, Chabata CV, Silva R, Conicella AE, Amaya J, Burke KA, Mittal J, Fawzi NL. </i> Mol Cell, 2018","reference_id":"29358076","region_id":"DP01109r005","released":"2022_03","sample":[],"statement":[{"type":"Figure","text":"DIC micrographs show hnRNPA2 LC WT, D290V, and P298L form liquid droplets. Over time, D290V droplets seed persistent aggregates with fibrous structure. P298L forms non-spherical clusters consistent with aggregation.","_id":"685af523b4ac24d5329d8bc5"}],"states_connection":[],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_id":"GO:0140693","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-06-22T15:07:46.953Z","_id":"685af523b4ac24d5329d8bc6"},"version":1,"_id":"685af523b4ac24d5329d8bc4","reference_source":"pmid"}],"__v":0,"disorder_content":0.43059490084985835,"disprot_consensus":{"full":[{"start":190,"end":341,"type":"D"}],"Structural state":[{"start":190,"end":341,"type":"D"}],"Molecular function":[{"start":190,"end":341,"type":"F"}]}},{"acc":"Q9UHD9","sequence":"MAENGESSGPPRPSRGPAAAQGSAAAPAEPKIIKVTVKTPKEKEEFAVPENSSVQQFKEAISKRFKSQTDQLVLIFAGKILKDQDTLIQHGIHDGLTVHLVIKSQNRPQGQSTQPSNAAGTNTTSASTPRSNSTPISTNSNPFGLGSLGGLAGLSSLGLSSTNFSELQSQMQQQLMASPEMMIQIMENPFVQSMLSNPDLMRQLIMANPQMQQLIQRNPEISHLLNNPDIMRQTLEIARNPAMMQEMMRNQDLALSNLESIPGGYNALRRMYTDIQEPMLNAAQEQFGGNPFASVGSSSSSGEGTQPSRTENRDPLPNPWAPPPATQSSATTSTTTSTGSGSGNSSSNATGNTVAAANYVASIFSTPGMQSLLQQITENPQLIQNMLSAPYMRSMMQSLSQNPDLAAQMMLNSPLFTANPQLQEQMRPQLPAFLQQMQNPDTLSAMSNPRAMQALMQIQQGLQTLATEAPGLIPSFTPGVGVGVLGTAIGPVGPVTPIGPIGPIVPFTPIGPIGPIGPTGPAAPPGSTGSGGPTGPTVSSAAPSETTSPTSESGPNQQFIQQMVQALAGANAPQLPNPEVRFQQQLEQLNAMGFLNREANLQALIATGGDINAAIERLLGSQPS","alphafold_very_low_content":"0.32211538461538464","creator":"tlazar","dataset":["Condensates-related proteins"],"date":"2018-06-18T15:53:32.000Z","disprot_id":"DP01110","features":{"pfam":[{"id":"PF00240","name":"Ubiquitin family","start":35,"end":104},{"id":"PF00627","name":"UBA/TS-N domain","start":583,"end":618},{"id":"PF23195","name":"Ubiquilin-1-like domain","start":174,"end":293}],"gene3D":[{"start":211,"end":264,"id":"1.10.260.100","name":"1.10.260.100","_id":"685af523b4ac24d5329d8bcd"},{"start":1,"end":103,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1","_id":"685af523b4ac24d5329d8bce"},{"start":358,"end":418,"id":"1.10.260.100","name":"1.10.260.100","_id":"685af523b4ac24d5329d8bcf"},{"start":572,"end":624,"id":"1.10.8.10","name":"DNA helicase RuvA subunit, C-terminal domain","_id":"685af523b4ac24d5329d8bd0"}]},"genes":[{"name":{"value":"UBQLN2","evidences":[],"_id":"685af523b4ac24d5329d8be1"},"synonyms":[{"value":"N4BP4","evidences":[],"_id":"685af523b4ac24d5329d8be2"},{"value":"PLIC2","evidences":[],"_id":"685af523b4ac24d5329d8be3"}],"olnNames":[],"orfNames":[{"value":"HRIHFB2157","evidences":[],"_id":"685af523b4ac24d5329d8be4"}],"_id":"685af523b4ac24d5329d8be0"}],"length":624,"name":"Ubiquilin-2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":4,"released":"2018_11","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000038C53","uniref100":"UniRef100_Q9UHD9","uniref50":"UniRef50_Q9UHD9","uniref90":"UniRef90_Q9UHD9","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":450,"end":576,"interaction_partner":[],"reference_html":"Ubiquitin Modulates Liquid-Liquid Phase Separation of UBQLN2 via Disruption of Multivalent Interactions. <i> Dao TP, Kolaitis RM, Kim HJ, O'Donovan K, Martyniak B, Colicino E, Hehnly H, Taylor JP, Castañeda CA. </i> Mol Cell, 2018","reference_id":"29526694","region_id":"DP01110r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"1H-15N spectra of UBQLN2 450–624 revealed a concentration of amide resonances between 8.0 – 8.5 ppm in 1H dimension, consistent with a largely disordered construct (Figure 3A).","_id":"685af523b4ac24d5329d8bd8"},{"type":"Results","text":"These data demonstrate that much of UBQLN2 450–624 is disordered. However, the UBA domain exhibits significant α-helical propensity, consistent with its known structure. Residues 450–460, located in the STI1-II domain, exhibit slight α-helical propensity and are predicted to be somewhat ordered according to PONDR-FIT calculations (Figure S1A).","_id":"685af523b4ac24d5329d8bd9"},{"type":"Results","text":"Using a combination of backbone amide, Cα, Cβ, and CO chemical shifts, we predicted secondary structure population using the δ2D algorithm (Figure 3D) (Camilloni et al., 2012). These calculations confirmed the UBA domain to be α-helical.","_id":"685af523b4ac24d5329d8bda"},{"type":"Results","text":"Backbone R2 relaxation rates for UBQLN2 487–624 reinforced the notion that residues 487–580 were generally intrinsically disordered; R2 rates were 2–4 s-1, similar to the intrinsically disordered region in FUS in the non-phase separated state (Burke et al., 2015).","_id":"685af523b4ac24d5329d8bdb"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-23T18:59:01.892Z","_id":"685af523b4ac24d5329d8bdc"},"version":1,"_id":"685af523b4ac24d5329d8bd7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006323","ec_name":"fluorescence microscopy evidence used in manual assertion","ec_ontology":"ECO","start":450,"end":576,"interaction_partner":[],"reference_html":"Ubiquitin Modulates Liquid-Liquid Phase Separation of UBQLN2 via Disruption of Multivalent Interactions. <i> Dao TP, Kolaitis RM, Kim HJ, O'Donovan K, Martyniak B, Colicino E, Hehnly H, Taylor JP, Castañeda CA. </i> Mol Cell, 2018","reference_id":"29526694","region_id":"DP01110r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"When cells were exposed to arsensite stress, only FL UBQLN2 and UBQLN2 450–624 formed cytoplasmic puncta (Figure 2E). Moreover, even at slightly higher expression level than FL UBQLN2 (Figure 2F), UBQLN2 450–624 formed less puncta (Figures (Figures2E,2E, ,2G),2G), consistent with its reduced propensity to undergo LLPS in vitro. We noted that a portion of exogenously-introduced UBQLN2 colocalized with SG markers, whereas some exogenous UBQLN2 formed puncta that did not colocalize with SG marker.","_id":"685af523b4ac24d5329d8bde"}],"states_connection":[],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_id":"GO:0140693","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-23T18:59:05.731Z","_id":"685af523b4ac24d5329d8bdf"},"version":1,"_id":"685af523b4ac24d5329d8bdd","reference_source":"pmid"}],"__v":0,"disorder_content":0.20352564102564102,"disprot_consensus":{"full":[{"start":450,"end":576,"type":"D"}],"Structural state":[{"start":450,"end":576,"type":"D"}],"Molecular function":[{"start":450,"end":576,"type":"F"}]}},{"acc":"Q13501","sequence":"MASLTVKAYLLGKEDAAREIRRFSFCCSPEPEAEAEAAAGPGPCERLLSRVAALFPALRPGGFQAHYRDEDGDLVAFSSDEELTMAMSYVKDDIFRIYIKEKKECRRDHRPPCAQEAPRNMVHPNVICDGCNGPVVGTRYKCSVCPDYDLCSVCEGKGLHRGHTKLAFPSPFGHLSEGFSHSRWLRKVKHGHFGWPGWEMGPPGNWSPRPPRAGEARPGPTAESASGPSEDPSVNFLKNVGESVAAALSPLGIEVDIDVEHGGKRSRLTPVSPESSSTEEKSSSQPSSCCSDPSKPGGNVEGATQSLAEQMRKIALESEGRPEEQMESDNCSGGDDDWTHLSSKEVDPSTGELQSLQMPESEGPSSLDPSQEGPTGLKEAALYPHLPPEADPRLIESLSQMLSMGFSDEGGWLTRLLQTKNYDIGAALDTIQYSKHPPPL","alphafold_very_low_content":"0.3659090909090909","creator":"vsagris","dataset":["Autophagy-related proteins","NDDs-related proteins","Condensates-related proteins","Age-related disorders proteins"],"date":"2018-06-18T16:06:11.000Z","disprot_id":"DP01111","features":{"pfam":[{"id":"PF00564","name":"PB1 domain","start":41,"end":101},{"id":"PF00569","name":"Zinc finger, ZZ type","start":123,"end":159},{"id":"PF16577","name":"UBA domain","start":379,"end":440}],"gene3D":[{"start":115,"end":169,"id":"3.30.60.90","name":"3.30.60.90","_id":"685af523b4ac24d5329d8be8"},{"start":1,"end":102,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1","_id":"685af523b4ac24d5329d8be9"},{"start":386,"end":436,"id":"1.10.8.10","name":"DNA helicase RuvA subunit, C-terminal domain","_id":"685af523b4ac24d5329d8bea"}]},"genes":[{"name":{"value":"SQSTM1","evidences":[],"_id":"685af523b4ac24d5329d8bf7"},"synonyms":[{"value":"ORCA","evidences":[],"_id":"685af523b4ac24d5329d8bf8"},{"value":"OSIL","evidences":[],"_id":"685af523b4ac24d5329d8bf9"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d8bf6"}],"length":440,"name":"Sequestosome-1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":3,"released":"2018_11","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000071099","uniref100":"UniRef100_Q13501","uniref50":"UniRef50_Q13501","uniref90":"UniRef90_Q13501","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":341,"end":386,"interaction_partner":[],"reference_html":"Characterization of a non-UBA domain missense mutation of sequestosome 1 (SQSTM1) in Paget's disease of bone. <i> Najat D, Garner T, Hagen T, Shaw B, Sheppard PW, Falchetti A, Marini F, Brandi ML, Long JE, Cavey JR, Searle MS, Layfield R. </i> J Bone Miner Res, 2009","reference_id":"19049332","region_id":"DP01111r001","released":"2022_03","sample":[],"statement":[{"type":"Figure","text":"The additional N-terminal residues in the longer construct (341–386) are largely clustered in a small group with a narrow range of 1H chemical shifts indicative of unstructured polypeptide chain (shown in box).","_id":"685af523b4ac24d5329d8bec"},{"type":"Results","text":"Thus, the NMR and CD data are in good agreement and suggest that the N-terminal extension in the 341–440 UBA construct is not significantly structured.","_id":"685af523b4ac24d5329d8bed"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-05-31T10:13:12.099Z","_id":"685af523b4ac24d5329d8bee"},"version":3,"_id":"685af523b4ac24d5329d8beb","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":341,"end":386,"interaction_partner":[],"reference_html":"Characterization of a non-UBA domain missense mutation of sequestosome 1 (SQSTM1) in Paget's disease of bone. <i> Najat D, Garner T, Hagen T, Shaw B, Sheppard PW, Falchetti A, Marini F, Brandi ML, Long JE, Cavey JR, Searle MS, Layfield R. </i> J Bone Miner Res, 2009","reference_id":"19049332","region_id":"DP01111r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The spectrum of the longer construct has a more pronounced minimum at 205 nm, which indicates a significant contribution to the spectrum from a disordered random coil part of the polypeptide.","_id":"685af523b4ac24d5329d8bf3"},{"type":"Results","text":"Thus, the NMR and CD data are in good agreement and suggest that the N-terminal extension in the 341–440 UBA construct is not significantly structured.","_id":"685af523b4ac24d5329d8bf4"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-05-31T10:13:11.402Z","_id":"685af523b4ac24d5329d8bf5"},"version":1,"_id":"685af523b4ac24d5329d8bf2","reference_source":"pmid"}],"__v":0,"disorder_content":0.10454545454545454,"disprot_consensus":{"full":[{"start":341,"end":386,"type":"D"}],"Structural state":[{"start":341,"end":386,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00017","name":"SH2 domain","start":333,"end":408},{"id":"PF00017","name":"SH2 domain","start":624,"end":698},{"id":"PF00620","name":"RhoGAP domain","start":129,"end":274},{"id":"PF16454","name":"Phosphatidylinositol 3-kinase regulatory subunit P85 inter-SH2 domain","start":431,"end":599}],"gene3D":[{"start":104,"end":316,"id":"1.10.555.10","name":"Rho GTPase activation protein"},{"start":317,"end":443,"id":"3.30.505.10","name":"SH2 domain"},{"start":613,"end":724,"id":"3.30.505.10","name":"SH2 domain"},{"start":1,"end":83,"id":"2.30.30.40","name":"SH3 Domains"}]},"uniref50":"UniRef50_P27986","sequence":"MSAEGYQYRALYDYKKEREEDIDLHLGDILTVNKGSLVALGFSDGQEARPEEIGWLNGYNETTGERGDFPGTYVEYIGRKKISPPTPKPRPPRPLPVAPGSSKTEADVEQQALTLPDLAEQFAPPDIAPPLLIKLVEAIEKKGLECSTLYRTQSSSNLAELRQLLDCDTPSVDLEMIDVHVLADAFKRYLLDLPNPVIPAAVYSEMISLAPEVQSSEEYIQLLKKLIRSPSIPHQYWLTLQYLLKHFFKLSQTSSKNLLNARVLSEIFSPMLFRFSAASSDNTENLIKVIEILISTEWNERQPAPALPPKPPKPTTVANNGMNNNMSLQDAEWYWGDISREEVNEKLRDTADGTFLVRDASTKMHGDYTLTLRKGGNNKLIKIFHRDGKYGFSDPLTFSSVVELINHYRNESLAQYNPKLDVKLLYPVSKYQQDQVVKEDNIEAVGKKLHEYNTQFQEKSREYDRLYEEYTRTSQEIQMKRTAIEAFNETIKIFEEQCQTQERYSKEYIEKFKREGNEKEIQRIMHNYDKLKSRISEIIDSRRRLEEDLKKQAAEYREIDKRMNSIKPDLIQLRKTRDQYLMWLTQKGVRQKKLNEWLGNENTEDQYSLVEDDEDLPHHDEKTWNVGSSNRNKAENLLRGKRDGTFLVRESSKQGCYACSVVVDGEVKHCVINKTATGYGFAEPYNLYSSLKELVLHYQHTSLVQHNDSLNVTLAYPVYAQQRR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P27986","disprot_id":"DP01112","ncbi_taxon_id":9606,"regions_counter":5,"creator":"tlazar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":104,"region_id":"DP01112r001","released":"2022_06","ec_id":"ECO:0006165","reference_html":"Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase. <i> Renzoni DA, Pugh DJ, Siligardi G, Das P, Morton CJ, Rossi C, Waterfield MD, Campbell ID, Ladbury JE. </i> Biochemistry, 1996","statement":[{"text":"NMR analysis provides no evidence of short- or long-range NOE interactions in the free peptide.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":91,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-15T15:06:17.126Z","reference_source":"pmid","term_name":"disorder","reference_id":"8961927","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":104,"term_name":"protein binding","released":"2022_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase. <i> Renzoni DA, Pugh DJ, Siligardi G, Das P, Morton CJ, Rossi C, Waterfield MD, Campbell ID, Ladbury JE. </i> Biochemistry, 1996","statement":[{"text":" The binding of the peptide to the SH3 domain was investigated using NMR, CD, and ITC at 30 °C (Table 2). Despite the quite different methods the binding data are in good agreement. Using these very different probes of binding the average KD is found to be of the order of 31 μM, giving a free energy ΔG° for the interaction of −26 kJ·mol-1.","type":"Results"}],"term_id":"GO:0005515","curator_id":"vnugnes","start":91,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"8961927","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-15T15:04:40.052Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01112r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"1A0N"},{"db":"PDB","id":"1AZG"}],"interaction_partner":[{"db":"UniProt","id":"P06241","operator":"and","partner_start":null,"partner_end":null}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":104,"region_id":"DP01112r003","released":"2022_06","ec_id":"ECO:0006204","reference_html":"Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase. <i> Renzoni DA, Pugh DJ, Siligardi G, Das P, Morton CJ, Rossi C, Waterfield MD, Campbell ID, Ladbury JE. </i> Biochemistry, 1996","statement":[{"text":"The featureless CD spectrum is consistent with the free peptide being nonstructured.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":91,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-15T15:06:33.445Z","reference_source":"pmid","term_name":"disorder","reference_id":"8961927","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":104,"term_name":"protein binding","released":"2022_06","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase. <i> Renzoni DA, Pugh DJ, Siligardi G, Das P, Morton CJ, Rossi C, Waterfield MD, Campbell ID, Ladbury JE. </i> Biochemistry, 1996","statement":[{"text":"The figure shows three independently determined spectra:  the spectrum for the free peptide at 22 °C suggesting that there is no secondary structure present; the spectrum of P2L peptide bound to the Fyn SH3 domain in a 1:1 concentration ratio with the spectrum of the free SH3 domain subtracted; the spectrum of free P2L peptide at −104 °C showing PPII helical conformation.","type":"Figure"}],"term_id":"GO:0005515","curator_id":"vnugnes","start":91,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"8961927","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-15T15:05:31.014Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01112r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P06241","operator":"and","partner_start":null,"partner_end":null}]},{"start":91,"end":104,"reference_id":"8961927","reference_source":"pmid","reference_html":"Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase. <i> Renzoni DA, Pugh DJ, Siligardi G, Das P, Morton CJ, Rossi C, Waterfield MD, Campbell ID, Ladbury JE. </i> Biochemistry, 1996","date":"2022-06-15T15:05:45.044Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P06241","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01112r005","statement":[{"text":"The binding of the peptide to the SH3 domain was investigated using NMR, CD, and ITC at 30 °C (Table 2). Despite the quite different methods the binding data are in good agreement. Using these very different probes of binding the average KD is found to be of the order of 31 μM, giving a free energy ΔG° for the interaction of −26 kJ·mol-1.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_P27986","date":"2018-06-19T07:50:00.000Z","acc":"P27986","name":"Phosphatidylinositol 3-kinase regulatory subunit alpha","length":724,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins","Stress response proteins"],"UniParc":"UPI0000054C77","genes":[{"name":{"value":"PIK3R1"},"synonyms":[{"value":"GRB1"}]}],"alphafold_very_low_content":0.08701657458563536,"disorder_content":0.019337016574585635,"disprot_consensus":{"full":[{"start":91,"end":104,"type":"D"}],"Structural state":[{"start":91,"end":104,"type":"D"}],"Molecular function":[{"start":91,"end":104,"type":"F"}]}},{"acc":"D0PV95","sequence":"MESNQSNNGGSGNAALNRGGRYVPPHLRGGDGGAAAAASAGGDDRRGGAGGGGYRRGGGNSGGGGGGGYDRGYNDNRDDRDNRGGSGGYGRDRNYEDRGYNGGGGGGGNRGYNNNRGGGGGGYNRQDRGDGGSSNFSRGGYNNRDEGSDNRGSGRSYNNDRRDNGGDGQNTRWNNLDAPPSRGTSKWENRGARDERIEQELFSGQLSGINFDKYEEIPVEATGDDVPQPISLFSDLSLHEWIEENIKTAGYDRPTPVQKYSIPALQGGRDLMSCAQTGSGKTAAFLVPLVNAILQDGPDAVHRSVTSSGGRKKQYPSALVLSPTRELSLQIFNESRKFAYRTPITSALLYGGRENYKDQIHKLRLGCHILIATPGRLIDVMDQGLIGMEGCRYLVLDEADRMLDMGFEPQIRQIVECNRMPSKEERITAMFSATFPKEIQLLAQDFLKENYVFLAVGRVGSTSENIMQKIVWVEEDEKRSYLMDLLDATGDSSLTLVFVETKRGASDLAYYLNRQNYEVVTIHGDLKQFEREKHLDLFRTGTAPILVATAVAARGLDIPNVKHVINYDLPSDVDEYVHRIGRTGRVGNVGLATSFFNDKNRNIARELMDLIVEANQELPDWLEGMSGDMRSGGGYRGRGGRGNGQRFGGRDHRYQGGSGNGGGGNGGGGGFGGGGQRSGGGGGFQSGGGGGRQQQQQQRAQPQQDWWS","alphafold_very_low_content":"0.3474576271186441","creator":"tlazar","dataset":["Condensates-related proteins","RNA-binding proteins"],"date":"2018-06-19T08:31:26.000Z","disprot_id":"DP01113","features":{"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":255,"end":440},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":478,"end":587}],"gene3D":[{"start":182,"end":455,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d8bfc"},{"start":456,"end":630,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d8bfd"}]},"genes":[{"name":{"value":"laf-1","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/19361491","id":"19361491","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/19361491","_id":"685af523b4ac24d5329d8c0c"},"code":"ECO:0000303","_id":"685af523b4ac24d5329d8c0b"},{"source":{"id":"Y71H2AM.19b","name":"WormBase","url":"https://www.wormbase.org/db/seq/sequence?name=Y71H2AM.19b;class=Transcript","_id":"685af523b4ac24d5329d8c0e"},"code":"ECO:0000312","_id":"685af523b4ac24d5329d8c0d"}],"_id":"685af523b4ac24d5329d8c0f"},"synonyms":[],"olnNames":[],"orfNames":[{"value":"Y71H2AM.19","evidences":[{"source":{"id":"Y71H2AM.19b","name":"WormBase","url":"https://www.wormbase.org/db/seq/sequence?name=Y71H2AM.19b;class=Transcript","_id":"685af523b4ac24d5329d8c12"},"code":"ECO:0000312","_id":"685af523b4ac24d5329d8c11"}],"_id":"685af523b4ac24d5329d8c10"}],"_id":"685af523b4ac24d5329d8c0a"}],"length":708,"name":"ATP-dependent RNA helicase laf-1","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions_counter":4,"released":"2018_11","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"UniParc":"UPI0001BB3642","uniref100":"UniRef100_D0PV95","uniref50":"UniRef50_D0PV95","uniref90":"UniRef90_D0PV95","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":168,"interaction_partner":[],"reference_html":"The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics. <i> Elbaum-Garfinkle S, Kim Y, Szczepaniak K, Chen CC, Eckmann CR, Myong S, Brangwynne CP. </i> Proc Natl Acad Sci U S A, 2015","reference_id":"26015579","region_id":"DP01113r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"To test the disorder prediction of this important domain, we performed circular dichroism (CD) measurements, which demonstrate a random coil signature (32) for the isolated RGG domain compared with the predominantly alpha-helical secondary structure of the FL and terminal deletions (Fig. 5B).","_id":"685af523b4ac24d5329d8bff"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-01-10T17:59:16.472Z","_id":"685af523b4ac24d5329d8c00"},"version":3,"_id":"685af523b4ac24d5329d8bfe","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006323","ec_name":"fluorescence microscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":168,"interaction_partner":[],"reference_html":"The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics. <i> Elbaum-Garfinkle S, Kim Y, Szczepaniak K, Chen CC, Eckmann CR, Myong S, Brangwynne CP. </i> Proc Natl Acad Sci U S A, 2015","reference_id":"26015579","region_id":"DP01113r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In contrast, deletion of the RGG-rich N terminus (ΔRGG) results in no observable droplets, even up to concentrations as high as 250 μM, revealing the N-terminal RGG domain as essential for phase separation. Moreover, the isolated N-terminal RGG domain was alone sufficient for forming droplets (Fig. 5C).","_id":"685af523b4ac24d5329d8c05"}],"states_connection":[],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_id":"GO:0140693","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-01-10T17:59:25.900Z","_id":"685af523b4ac24d5329d8c06"},"version":1,"_id":"685af523b4ac24d5329d8c04","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001183","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":168,"interaction_partner":[],"reference_html":"The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics. <i> Elbaum-Garfinkle S, Kim Y, Szczepaniak K, Chen CC, Eckmann CR, Myong S, Brangwynne CP. </i> Proc Natl Acad Sci U S A, 2015","reference_id":"26015579","region_id":"DP01113r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Because the RGG domain is sufficient for RNA binding (Fig. S8), we asked whether the disordered RGG domain could be responsible for the observed dynamic binding to RNA. Applying our FRET assay to the truncation mutants, we find that both ΔC and the RGG domain alone exhibit highly dynamic FRET traces, similar to that seen in the full-length construct (Fig. 5D). However, ΔRGG gives rise to a static, tightly wrapped conformation of bound RNA, similar to that observed in non–droplet-forming conditions (Fig. 4 B and C).","_id":"685af523b4ac24d5329d8c08"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_id":"GO:0003723","term_is_binding":true,"term_is_obsolete":false,"term_name":"RNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-01-10T17:59:33.421Z","_id":"685af523b4ac24d5329d8c09"},"version":1,"_id":"685af523b4ac24d5329d8c07","reference_source":"pmid"}],"__v":0,"disorder_content":0.23728813559322035,"disprot_consensus":{"full":[{"start":1,"end":168,"type":"D"}],"Structural state":[{"start":1,"end":168,"type":"D"}],"Molecular function":[{"start":1,"end":168,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00017","name":"SH2 domain","start":282,"end":356},{"id":"PF00018","name":"SH3 domain","start":8,"end":53},{"id":"PF00018","name":"SH3 domain","start":113,"end":157},{"id":"PF00018","name":"SH3 domain","start":196,"end":244}],"gene3D":[{"start":336,"end":377,"id":"3.30.505.10","name":"SH2 domain"},{"start":1,"end":61,"id":"2.30.30.40","name":"SH3 Domains"},{"start":93,"end":178,"id":"2.30.30.40","name":"SH3 Domains"},{"start":190,"end":254,"id":"2.30.30.40","name":"SH3 Domains"}]},"uniref50":"UniRef50_P16333","sequence":"MAEEVVVVAKFDYVAQQEQELDIKKNERLWLLDDSKSWWRVRNSMNKTGFVPSNYVERKNSARKASIVKNLKDTLGIGKVKRKPSVPDSASPADDSFVDPGERLYDLNMPAYVKFNYMAEREDELSLIKGTKVIVMEKCSDGWWRGSYNGQVGWFPSNYVTEEGDSPLGDHVGSLSEKLAAVVNNLNTGQVLHVVQALYPFSSSNDEELNFEKGDVMDVIEKPENDPEWWKCRKINGMVGLVPKNYVTVMQNNPLTSGLEPSPPQCDYIRPSLTGKFAGNPWYYGKVTRHQAEMALNERGHEGDFLIRDSESSPNDFSVSLKAQGKNKHFKVQLKETVYCIGQRKFSTMEELVEHYKKAPIFTSEQGEKLYLVKHLS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P16333","disprot_id":"DP01114","ncbi_taxon_id":9606,"regions_counter":4,"creator":"tlazar","regions":[{"start":59,"end":108,"reference_id":"26553976","reference_source":"pmid","reference_html":"Conserved interdomain linker promotes phase separation of the multivalent adaptor protein Nck. <i> Banjade S, Wu Q, Mittal A, Peeples WB, Pappu RV, Rosen MK. </i> Proc Natl Acad Sci U S A, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01114r003","statement":[{"text":"L1 is partially disordered, and also binds the second SH3 domain.","type":"Figure"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-23T17:59:43.015Z"}},{"start":59,"end":108,"reference_id":"26553976","reference_source":"pmid","reference_html":"Conserved interdomain linker promotes phase separation of the multivalent adaptor protein Nck. <i> Banjade S, Wu Q, Mittal A, Peeples WB, Pappu RV, Rosen MK. </i> Proc Natl Acad Sci U S A, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01114r004","statement":[{"text":"Our studies demonstrate that linker regions between modular domains can contribute to the driving forces for self-assembly and phase separation of multivalent proteins.","type":"Results"},{"text":"Conserved interdomain linker promotes phase separation of the multivalent adaptor protein Nck.","type":"Title"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-23T17:59:43.016Z"}}],"released":"2018_11","uniref100":"UniRef100_P16333","date":"2018-06-19T08:43:03.000Z","acc":"P16333","name":"Cytoplasmic protein NCK1","length":377,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI000012FE3E","genes":[{"name":{"value":"NCK1"},"synonyms":[{"value":"NCK"}]}],"alphafold_very_low_content":0.23607427055702918,"disorder_content":0.13262599469496023,"disprot_consensus":{"full":[{"start":59,"end":108,"type":"D"}],"Structural state":[{"start":59,"end":108,"type":"D"}],"Molecular function":[{"start":59,"end":108,"type":"F"}]}},{"acc":"Q16236","sequence":"MMDLELPPPGLPSQQDMDLIDILWRQDIDLGVSREVFDFSQRRKEYELEKQKKLEKERQEQLQKEQEKAFFAQLQLDEETGEFLPIQPAQHIQSETSGSANYSQVAHIPKSDALYFDDCMQLLAQTFPFVDDNEVSSATFQSLVPDIPGHIESPVFIATNQAQSPETSVAQVAPVDLDGMQQDIEQVWEELLSIPELQCLNIENDKLVETTMVPSPEAKLTEVDNYHFYSSIPSMEKEVGNCSPHFLNAFEDSFSSILSTEDPNQLTVNSLNSDATVNTDFGDEFYSAFIAEPSISNSMPSPATLSHSLSELLNGPIDVSDLSLCKAFNQNHPESTAEFNDSDSGISLNTSPSVASPEHSVESSSYGDTLLGLSDSEVEELDSAPGSVKQNGPKTPVHSSGDMVQPLSPSQGQSTHVHDAQCENTPEKELPVSPGHRKTPFTKDKHSSRLEAHLTRDELRAKALHIPFPVEKIINLPVVDFNEMMSKEQFNEAQLALIRDIRRRGKNKVAAQNCRKRKLENIVELEQDLDHLKDEKEKLLKEKGENDKSLHLLKKQLSTLYLEVFSMLRDEDGKPYSPSEYSLQQTRDGNVFLVPKSKKPDVKKN","alphafold_very_low_content":"0.4826446280991736","creator":"tlazar","dataset":["Autophagy-related proteins","Cancer-related proteins","Condensates-related proteins"],"date":"2018-06-19T08:52:06.000Z","disprot_id":"DP01115","features":{"pfam":[{"id":"PF03131","name":"bZIP Maf transcription factor","start":469,"end":559}],"gene3D":[{"start":434,"end":523,"id":"1.10.880.10","name":"Transcription factor, Skn-1-like, DNA-binding domain","_id":"685af523b4ac24d5329d8c14"}]},"genes":[{"name":{"value":"NFE2L2","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/29018201","id":"29018201","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/29018201","_id":"685af523b4ac24d5329d8c7d"},"code":"ECO:0000303","_id":"685af523b4ac24d5329d8c7c"},{"source":{"id":"HGNC:7782","name":"HGNC","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:7782","_id":"685af523b4ac24d5329d8c7f"},"code":"ECO:0000312","_id":"685af523b4ac24d5329d8c7e"}],"_id":"685af523b4ac24d5329d8c80"},"synonyms":[{"value":"NRF2","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/33009401","id":"33009401","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/33009401","_id":"685af523b4ac24d5329d8c83"},"code":"ECO:0000303","_id":"685af523b4ac24d5329d8c82"},{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/7937919","id":"7937919","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/7937919","_id":"685af523b4ac24d5329d8c85"},"code":"ECO:0000303","_id":"685af523b4ac24d5329d8c84"}],"_id":"685af523b4ac24d5329d8c81"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d8c7b"}],"length":605,"name":"Nuclear factor erythroid 2-related factor 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":22,"released":"2018_11","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000054C80","uniref100":"UniRef100_Q16236","uniref50":"UniRef50_Q16236","uniref90":"UniRef90_Q16236","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2FLU","_id":"685af523b4ac24d5329d8c1b"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":69,"end":84,"interaction_partner":[],"reference_html":"Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling. <i> Lo SC, Li X, Henzl MT, Beamer LJ, Hannink M. </i> EMBO J, 2006","reference_id":"16888629","region_id":"DP01115r002","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Keap1 is a BTB-Kelch substrate adaptor protein that regulates steady-state levels of Nrf2, a bZIP transcription factor, in response to oxidative stress. We have determined the structure of the Kelch domain of Keap1 bound to a 16-mer peptide from Nrf2 containing a highly conserved DxETGE motif. The Nrf2 peptide contains two short antiparallel β-strands connected by two overlapping type I β-turns stabilized by the aspartate and threonine residues. The β-turn region fits into a binding pocket on the top face of the Kelch domain and the glutamate residues form multiple hydrogen bonds with highly conserved residues in Keap1.","_id":"685af523b4ac24d5329d8c1a"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"mpajkos","curator_name":"Mátyás Pajkos","timestamp":"2021-09-23T12:56:48.359Z","_id":"685af523b4ac24d5329d8c1c"},"version":4,"_id":"685af523b4ac24d5329d8c19","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":605,"interaction_partner":[],"reference_html":"Nrf2, the Major Regulator of the Cellular Oxidative Stress Response, is Partially Disordered. <i> Karunatilleke NC, Fast CS, Ngo V, Brickenden A, Duennwald ML, Konermann L, Choy WY. </i> Int J Mol Sci, 2021","reference_id":"34299054","region_id":"DP01115r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Intriguingly, although the molecular weight of FL-Nrf2 is only 70.4 kDa (including the His-tag), it runs with an apparent MW of ~110 kDa on SDS-PAGE gels as already reported previously [44] (Figure S1). The high net charge and aberrant SDS-PAGE migration behavior suggest that FL-Nrf2 may be partially disordered","_id":"685af523b4ac24d5329d8c1e"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"mpajkos","curator_name":"Mátyás Pajkos","timestamp":"2021-09-23T12:56:55.489Z","_id":"685af523b4ac24d5329d8c1f"},"version":1,"_id":"685af523b4ac24d5329d8c1d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":605,"interaction_partner":[],"reference_html":"Nrf2, the Major Regulator of the Cellular Oxidative Stress Response, is Partially Disordered. <i> Karunatilleke NC, Fast CS, Ngo V, Brickenden A, Duennwald ML, Konermann L, Choy WY. </i> Int J Mol Sci, 2021","reference_id":"34299054","region_id":"DP01115r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"CD spectropolarimetry was applied for assessing the secondary structure of FL-Nrf2 at 5, 10, 25, and 35 °C. The negative bands at 208 and 222 nm indicate the presence of α-helical structural elements (Figure 1A). Spectral deconvolution indicates that at 25 °C, there are around 27% α-helical, 21% β-strand and 52% disordered/turn structures, implying that Nrf2 is indeed partially disordered (Figure 1B; Table S1).","_id":"685af523b4ac24d5329d8c21"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"mpajkos","curator_name":"Mátyás Pajkos","timestamp":"2021-09-23T12:56:56.809Z","_id":"685af523b4ac24d5329d8c22"},"version":1,"_id":"685af523b4ac24d5329d8c20","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":605,"interaction_partner":[],"reference_html":"Nrf2, the Major Regulator of the Cellular Oxidative Stress Response, is Partially Disordered. <i> Karunatilleke NC, Fast CS, Ngo V, Brickenden A, Duennwald ML, Konermann L, Choy WY. </i> Int J Mol Sci, 2021","reference_id":"34299054","region_id":"DP01115r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"We used NMR spectroscopy to further verify the disordered nature of FL-Nrf2. Figure 2 shows the 1H-15N HSQC spectra of FL-Nrf2 acquired at 5, 10, 25, and 35 °C. At all four temperatures, despite the presence of some well-dispersed peaks with relatively weak intensities, most of the observed backbone amide signals are crowded in a narrow region between 7.8 and 8.7 ppm in the 1H dimension. This lack of 1H resonance dispersion indicates that many parts of FL-Nrf2 do not adopt stable structures and undergo rapid conformational interconversion [51,52,53,54]. In addition, the disordered nature of FL-Nrf2 does not change significantly at lower temperatures. For comparison, we also acquired the HSQC spectrum of FL-Nrf2 at 35 °C in the presence of 6 M urea, under which conditions the protein was expected to be largely unfolded (Figure S3). The similarity of all these spectra therefore suggest that FL-Nrf2 is already extensively unfolded even in the absence of urea.","_id":"685af523b4ac24d5329d8c24"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"mpajkos","curator_name":"Mátyás Pajkos","timestamp":"2021-09-23T12:56:58.462Z","_id":"685af523b4ac24d5329d8c25"},"version":1,"_id":"685af523b4ac24d5329d8c23","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006236","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":605,"interaction_partner":[],"reference_html":"Nrf2, the Major Regulator of the Cellular Oxidative Stress Response, is Partially Disordered. <i> Karunatilleke NC, Fast CS, Ngo V, Brickenden A, Duennwald ML, Konermann L, Choy WY. </i> Int J Mol Sci, 2021","reference_id":"34299054","region_id":"DP01115r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Fast HDX kinetics were observed throughout the entire protein, where the majority of the peptides exhibit ~100% deuteration after 12 s. This lack of protection indicates that FL-Nrf2 is significantly disordered (Figure S6). Notably, several peptides in distinct parts of the protein showed somewhat slower deuteration. For instance, the peptide covering residues 54–74 in the Neh2 domain only displayed complete deuteration after >24 s. This observation is consistent with earlier findings that even though the Neh2 domain is disordered, helical propensity exists between residues 39 and 71 [22]. Other regions that showed somewhat slower exchange are 235–249, 417–434, and 512–537. They are located in the Neh7 domain, the linker between the Neh6 and Neh1 domains, and the Neh1 domain, respectively.","_id":"685af523b4ac24d5329d8c27"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"mpajkos","curator_name":"Mátyás Pajkos","timestamp":"2021-09-23T12:57:00.459Z","_id":"685af523b4ac24d5329d8c28"},"version":1,"_id":"685af523b4ac24d5329d8c26","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-15T17:22:57.325Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006236","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","ec_ontology":"ECO","start":17,"end":46,"interaction_partner":[],"reference_html":"Nrf2, the Major Regulator of the Cellular Oxidative Stress Response, is Partially Disordered. <i> Karunatilleke NC, Fast CS, Ngo V, Brickenden A, Duennwald ML, Konermann L, Choy WY. </i> Int J Mol Sci, 2021","reference_id":"34299054","region_id":"DP01115r007","released":"2022_06","sample":[{"db":"UniProt","deviation":null,"id":"Q14145","statements":[],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d8c2c"}],"statement":[{"type":"Results","text":"We also investigated how FL-Nrf2 interacts with Kelch, which is part of the negative regulator Keap1. Previous studies showed that the isolated Neh2 domain of FL-Nrf2 binds Kelch at two sites: the high- affinity ETGE motif (around residues 76–84; Kd ~5 nM) and the low-affinity DLG motif (around residues 17–46; Kd ~1 μM) [22]. Here we used HDX-MS to further dissect the effects of Kelch-binding on the conformational dynamics of FL-Nrf2. In these experiments, the FL-Nrf2 concentration was held constant at 2 μM, while the Kelch concentration varied from 2 to 4 and 6 μM, which corresponded to FL-Nrf2:Kelch ratios of 1:1, 1:2, and 1:3, respectively (Figure 4).","_id":"685af523b4ac24d5329d8c2a"},{"type":"Results","text":"Significant changes in deuterium uptake were observed in the Neh2 domain upon the addition of Kelch. In the presence of 1:1 Kelch, a considerable reduction in FL-Nrf2 deuterium uptake was displayed around the ETGE binding motif and a small reduction in deuterium uptake around the DLG motif, consistent with the binding affinities of the two sites. For a 1:2 ratio, a substantial reduction in deuterium uptake was observed around the DLG binding site and an even more significant reduction in HDX close to the ETGE motif. Further reduction in deuterium uptake around both sites was noted at a 1:3 ratio. Notably, the addition of Kelch did not slow down the deuterium uptake in any other domains of FL-Nrf2.","_id":"685af523b4ac24d5329d8c2b"}],"states_connection":[],"term_id":"IDPO:0000013","term_name":"pre-molten globule to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-12-07T09:17:40.088Z","_id":"685af523b4ac24d5329d8c2d"},"version":2,"_id":"685af523b4ac24d5329d8c29","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006236","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","ec_ontology":"ECO","start":17,"end":46,"interaction_partner":[{"db":"UniProt","id":"Q14145","partner_start":321,"partner_end":609,"_id":"685af523b4ac24d5329d8c31"}],"reference_html":"Nrf2, the Major Regulator of the Cellular Oxidative Stress Response, is Partially Disordered. <i> Karunatilleke NC, Fast CS, Ngo V, Brickenden A, Duennwald ML, Konermann L, Choy WY. </i> Int J Mol Sci, 2021","reference_id":"34299054","region_id":"DP01115r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"We also investigated how FL-Nrf2 interacts with Kelch, which is part of the negative regulator Keap1. Previous studies showed that the isolated Neh2 domain of FL-Nrf2 binds Kelch at two sites: the high- affinity ETGE motif (around residues 76–84; Kd ~5 nM) and the low-affinity DLG motif (around residues 17–46; Kd ~1 μM) [22]. Here we used HDX-MS to further dissect the effects of Kelch-binding on the conformational dynamics of FL-Nrf2. In these experiments, the FL-Nrf2 concentration was held constant at 2 μM, while the Kelch concentration varied from 2 to 4 and 6 μM, which corresponded to FL-Nrf2:Kelch ratios of 1:1, 1:2, and 1:3, respectively (Figure 4).","_id":"685af523b4ac24d5329d8c2f"},{"type":"Results","text":"Significant changes in deuterium uptake were observed in the Neh2 domain upon the addition of Kelch. In the presence of 1:1 Kelch, a considerable reduction in FL-Nrf2 deuterium uptake was displayed around the ETGE binding motif and a small reduction in deuterium uptake around the DLG motif, consistent with the binding affinities of the two sites. For a 1:2 ratio, a substantial reduction in deuterium uptake was observed around the DLG binding site and an even more significant reduction in HDX close to the ETGE motif. Further reduction in deuterium uptake around both sites was noted at a 1:3 ratio. Notably, the addition of Kelch did not slow down the deuterium uptake in any other domains of FL-Nrf2.","_id":"685af523b4ac24d5329d8c30"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"mpajkos","curator_name":"Mátyás Pajkos","timestamp":"2021-09-23T12:56:49.884Z","_id":"685af523b4ac24d5329d8c32"},"version":1,"_id":"685af523b4ac24d5329d8c2e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006236","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","ec_ontology":"ECO","start":76,"end":84,"interaction_partner":[{"db":"UniProt","id":"Q14145","partner_start":321,"partner_end":609,"_id":"685af523b4ac24d5329d8c36"}],"reference_html":"Nrf2, the Major Regulator of the Cellular Oxidative Stress Response, is Partially Disordered. <i> Karunatilleke NC, Fast CS, Ngo V, Brickenden A, Duennwald ML, Konermann L, Choy WY. </i> Int J Mol Sci, 2021","reference_id":"34299054","region_id":"DP01115r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"We also investigated how FL-Nrf2 interacts with Kelch, which is part of the negative regulator Keap1. Previous studies showed that the isolated Neh2 domain of FL-Nrf2 binds Kelch at two sites: the high- affinity ETGE motif (around residues 76–84; Kd ~5 nM) and the low-affinity DLG motif (around residues 17–46; Kd ~1 μM) [22]. Here we used HDX-MS to further dissect the effects of Kelch-binding on the conformational dynamics of FL-Nrf2. In these experiments, the FL-Nrf2 concentration was held constant at 2 μM, while the Kelch concentration varied from 2 to 4 and 6 μM, which corresponded to FL-Nrf2:Kelch ratios of 1:1, 1:2, and 1:3, respectively (Figure 4).","_id":"685af523b4ac24d5329d8c34"},{"type":"Results","text":"Significant changes in deuterium uptake were observed in the Neh2 domain upon the addition of Kelch. In the presence of 1:1 Kelch, a considerable reduction in FL-Nrf2 deuterium uptake was displayed around the ETGE binding motif and a small reduction in deuterium uptake around the DLG motif, consistent with the binding affinities of the two sites. For a 1:2 ratio, a substantial reduction in deuterium uptake was observed around the DLG binding site and an even more significant reduction in HDX close to the ETGE motif. Further reduction in deuterium uptake around both sites was noted at a 1:3 ratio. Notably, the addition of Kelch did not slow down the deuterium uptake in any other domains of FL-Nrf2.","_id":"685af523b4ac24d5329d8c35"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"mpajkos","curator_name":"Mátyás Pajkos","timestamp":"2021-09-23T12:56:51.560Z","_id":"685af523b4ac24d5329d8c37"},"version":1,"_id":"685af523b4ac24d5329d8c33","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-15T17:32:40.355Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006236","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","ec_ontology":"ECO","start":76,"end":84,"interaction_partner":[],"reference_html":"Nrf2, the Major Regulator of the Cellular Oxidative Stress Response, is Partially Disordered. <i> Karunatilleke NC, Fast CS, Ngo V, Brickenden A, Duennwald ML, Konermann L, Choy WY. </i> Int J Mol Sci, 2021","reference_id":"34299054","region_id":"DP01115r010","released":"2022_06","sample":[],"statement":[{"type":"Abstract","text":"Nuclear factor erythroid 2-related factor 2 (Nrf2) is a transcription regulator that plays a pivotal role in coordinating the cellular response to oxidative stress. Through interactions with other proteins, such as Kelch-like ECH-associated protein 1 (Keap1), CREB-binding protein (CBP), and retinoid X receptor alpha (RXRα), Nrf2 mediates the transcription of cytoprotective genes critical for removing toxicants and preventing DNA damage, thereby playing a significant role in chemoprevention.","_id":"685af523b4ac24d5329d8c39"}],"states_connection":[],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of cellular response to oxidative stress.\" [GOC:mah, GOC:TermGenie]","term_id":"GO:1900407","term_is_binding":true,"term_is_obsolete":false,"term_name":"regulation of cellular response to oxidative stress","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-12-07T09:17:45.698Z","_id":"685af523b4ac24d5329d8c3a"},"version":2,"_id":"685af523b4ac24d5329d8c38","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-15T17:32:13.607Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006236","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","ec_ontology":"ECO","start":17,"end":46,"interaction_partner":[],"reference_html":"Nrf2, the Major Regulator of the Cellular Oxidative Stress Response, is Partially Disordered. <i> Karunatilleke NC, Fast CS, Ngo V, Brickenden A, Duennwald ML, Konermann L, Choy WY. </i> Int J Mol Sci, 2021","reference_id":"34299054","region_id":"DP01115r011","released":"2022_06","sample":[],"statement":[{"type":"Abstract","text":"Nuclear factor erythroid 2-related factor 2 (Nrf2) is a transcription regulator that plays a pivotal role in coordinating the cellular response to oxidative stress. Through interactions with other proteins, such as Kelch-like ECH-associated protein 1 (Keap1), CREB-binding protein (CBP), and retinoid X receptor alpha (RXRα), Nrf2 mediates the transcription of cytoprotective genes critical for removing toxicants and preventing DNA damage, thereby playing a significant role in chemoprevention.","_id":"685af523b4ac24d5329d8c3c"}],"states_connection":[],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of cellular response to oxidative stress.\" [GOC:mah, GOC:TermGenie]","term_id":"GO:1900407","term_is_binding":true,"term_is_obsolete":false,"term_name":"regulation of cellular response to oxidative stress","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-12-07T09:17:47.868Z","_id":"685af523b4ac24d5329d8c3d"},"version":2,"_id":"685af523b4ac24d5329d8c3b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"position":null,"statements":[],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr80Ala","_id":"685af523b4ac24d5329d8c42"},{"start":80,"end":80,"statements":[],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d8c43"}],"cross_refs":[{"db":"ELM","id":"DEG_Kelch_Keap1_1","_id":"685af523b4ac24d5329d8c44"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-08-08T19:53:13.278Z","disprot_namespace":"Disorder function","ec_go":"IEP","ec_id":"ECO:0000279","ec_name":"qualitative western immunoblotting evidence used in manual assertion","ec_ontology":"ECO","start":74,"end":87,"interaction_partner":[{"db":"UniProt","id":"Q14145","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8c3f"}],"reference_html":"Structure of the Keap1:Nrf2 interface provides mechanistic insight into Nrf2 signaling. <i> Lo SC, Li X, Henzl MT, Beamer LJ, Hannink M. </i> EMBO J, 2006","reference_id":"16888629","region_id":"DP01115r012","released":"2022_12","sample":[],"statement":[{"type":"Results","text":"Peptide competition experiments were carried out using 14-mer peptides that contained either an alanine or phosphothreonine in place of T80. A 14-mer peptide corresponding to amino acids 74–87 of Nrf2 that contained an alanine in place of T80 was unable to displace HA-Nrf2 from Keap1-CBD even at input peptide levels 100-fold higher than that needed for the wild-type peptide to displace Nrf2 from Keap1 (Figure 7A, compare lanes 3–6 with lanes 7–10). Likewise, a 14-mer peptide that contained a phosphothreonine residue in place of T80 was also unable to displace Nrf2 from Keap1 (Figure 7A, lanes 11–14).","_id":"685af523b4ac24d5329d8c40"},{"type":"Curator statement","text":"KEAP1 is a substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex.","_id":"685af523b4ac24d5329d8c41"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.\" [GOC:vp]","term_id":"GO:0031625","term_is_binding":true,"term_is_obsolete":false,"term_name":"ubiquitin protein ligase binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-12-07T09:17:53.807Z","_id":"685af523b4ac24d5329d8c45"},"version":3,"_id":"685af523b4ac24d5329d8c3e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-07-29T19:44:14.120Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005640","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":56,"interaction_partner":[{"db":"UniProt","id":"Q9Z2X8","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8c4c"}],"reference_html":"Kinetic, thermodynamic, and structural characterizations of the association between Nrf2-DLGex degron and Keap1. <i> Fukutomi T, Takagi K, Mizushima T, Ohuchi N, Yamamoto M. </i> Mol Cell Biol, 2014","reference_id":"24366543","region_id":"DP01115r014","released":"2022_12","sample":[],"statement":[{"type":"Results","text":"We found that wild-type (WT) Neh2(1-56) nicely interacted with Keap1 (WT in Fig. 2B). The D38H and Q43G mutant forms retained the same binding activity as the WT, and the S33R and Q43R mutant forms exhibited slightly stronger binding activity than the WT (Fig. 2C, right panel).","_id":"685af523b4ac24d5329d8c4d"},{"type":"Curator statement","text":"The peptide used in this assessment derives from the mouse form. The Q43R mutant corresponds to the human protein sequence.","_id":"685af523b4ac24d5329d8c4e"},{"type":"Curator statement","text":"KEAP1 is a substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex.","_id":"685af523b4ac24d5329d8c4f"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.\" [GOC:vp]","term_id":"GO:0031625","term_is_obsolete":false,"term_name":"ubiquitin protein ligase binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-12-07T09:17:56.775Z","_id":"685af523b4ac24d5329d8c50"},"version":0,"_id":"685af523b4ac24d5329d8c4b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[],"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","_id":"685af523b4ac24d5329d8c52"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T15:20:09.994Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0005601","ec_name":"immunofluorescence confocal microscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":605,"interaction_partner":[],"reference_html":"p62-Dependent Phase Separation of Patient-Derived KEAP1 Mutations and NRF2.  <i> Cloer EW, Siesser PF, Cousins EM, Goldfarb D, Mowrey DD, Harrison JS, Weir SJ, Dokholyan NV, Major MB. </i> Mol Cell Biol, 2018","reference_id":"30126895","region_id":"DP01115r015","released":"2023_12","sample":[{"db":"Cellosaurus","deviation":null,"entry_name":"NCIH1299","id":"CVCL_0060","statements":[],"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_id":"UO:0000201","unit_name":"cells/ml","value":null,"_id":"685af523b4ac24d5329d8c53"}],"statement":[{"type":"Results","text":"To identify the proteins contained in the biomolecular condensates, IF analysis of mKeap1-mCh and mEGFP-Nrf2 in H1299 cells was performed, and results confirmed that Keap1 and Nrf2 colocalize in the clusters (Fig. 8A).","_id":"685af523b4ac24d5329d8c54"},{"type":"Discussion","text":"Fourth, the ANCHOR mutants form p62-dependent biomolecular condensates that are spherical and contain p62, p62 pS351, polyUb, and NRF2; these clusters are not delivered to the autophagy pathway for clearance and are formed by phase separation.","_id":"685af523b4ac24d5329d8c55"},{"type":"Discussion","text":"Furthermore, NRF2 was detected in the biomolecular condensates only in the presence of KEAP1 ANCHOR mutants.","_id":"685af523b4ac24d5329d8c56"}],"states_connection":[],"term_comment":"","term_def":"\"Organized structure of distinctive morphology and function, not bounded by a lipid bilayer membrane. Includes ribosomes, the cytoskeleton and chromosomes.\" [GOC:go_curators]","term_id":"GO:0043228","term_is_obsolete":false,"term_name":"non-membrane-bounded organelle","term_namespace":"Cellular component","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-12-07T09:17:58.980Z","_id":"685af523b4ac24d5329d8c57"},"version":0,"_id":"685af523b4ac24d5329d8c51","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Results","text":"o investigate whether these IDRs form phase-separated droplets in vitro, we purified a peptide containing the first IDR (NRF21-208) and a peptide containing the second and third IDRs (NRF2209-605), each tagged with mEGFP (monomeric enhanced green fluorescent protein) (Fig. 7B).","_id":"685af523b4ac24d5329d8c5a"}],"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","_id":"685af523b4ac24d5329d8c59"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T15:34:10.614Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006323","ec_name":"fluorescence microscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":208,"interaction_partner":[],"reference_html":"Activation of NRF2 ameliorates oxidative stress and cystogenesis in autosomal dominant polycystic kidney disease. <i> Lu Y, Sun Y, Liu Z, Lu Y, Zhu X, Lan B, Mi Z, Dang L, Li N, Zhan W, Tan L, Pi J, Xiong H, Zhang L, Chen Y. </i> Sci Transl Med, 2020","reference_id":"32727915","region_id":"DP01115r016","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"Droplet formation assays revealed that both NRF21-208-mEGFP and NRF2209-605-mEGFP formed phase-separated droplets in a concentration-dependent manner (Fig. 7C). NRF21-208-mEGFP also contains the AD of NRF2 and formed markedly larger droplets than NRF2209-605-mEGFP at the same concentration","_id":"685af523b4ac24d5329d8c5b"}],"states_connection":[],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_id":"GO:0140693","term_is_obsolete":false,"term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-12-07T09:18:00.858Z","_id":"685af523b4ac24d5329d8c5c"},"version":0,"_id":"685af523b4ac24d5329d8c58","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Results","text":"o investigate whether these IDRs form phase-separated droplets in vitro, we purified a peptide containing the first IDR (NRF21-208) and a peptide containing the second and third IDRs (NRF2209-605), each tagged with mEGFP (monomeric enhanced green fluorescent protein) (Fig. 7B).","_id":"685af523b4ac24d5329d8c5f"}],"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","_id":"685af523b4ac24d5329d8c5e"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T15:34:40.029Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006323","ec_name":"fluorescence microscopy evidence used in manual assertion","ec_ontology":"ECO","start":209,"end":605,"interaction_partner":[],"reference_html":"Activation of NRF2 ameliorates oxidative stress and cystogenesis in autosomal dominant polycystic kidney disease. <i> Lu Y, Sun Y, Liu Z, Lu Y, Zhu X, Lan B, Mi Z, Dang L, Li N, Zhan W, Tan L, Pi J, Xiong H, Zhang L, Chen Y. </i> Sci Transl Med, 2020","reference_id":"32727915","region_id":"DP01115r017","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"Droplet formation assays revealed that both NRF21-208-mEGFP and NRF2209-605-mEGFP formed phase-separated droplets in a concentration-dependent manner (Fig. 7C).","_id":"685af523b4ac24d5329d8c60"}],"states_connection":[],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_id":"GO:0140693","term_is_obsolete":false,"term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-12-07T09:18:02.668Z","_id":"685af523b4ac24d5329d8c61"},"version":0,"_id":"685af523b4ac24d5329d8c5d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Results","text":"o investigate whether these IDRs form phase-separated droplets in vitro, we purified a peptide containing the first IDR (NRF21-208) and a peptide containing the second and third IDRs (NRF2209-605), each tagged with mEGFP (monomeric enhanced green fluorescent protein) (Fig. 7B).","_id":"685af523b4ac24d5329d8c64"}],"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","_id":"685af523b4ac24d5329d8c63"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T15:36:43.885Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006067","ec_name":"fluorescence recovery after photobleaching evidence used in manual assertion","ec_ontology":"ECO","start":209,"end":605,"interaction_partner":[],"reference_html":"Activation of NRF2 ameliorates oxidative stress and cystogenesis in autosomal dominant polycystic kidney disease. <i> Lu Y, Sun Y, Liu Z, Lu Y, Zhu X, Lan B, Mi Z, Dang L, Li N, Zhan W, Tan L, Pi J, Xiong H, Zhang L, Chen Y. </i> Sci Transl Med, 2020","reference_id":"32727915","region_id":"DP01115r018","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"Consistent with the FRAP analysis, fusion analysis showed that NRF21-208 droplets fused into one droplet within seconds (Fig. 7E). These results indicated that NRF21-208-mEGFP droplets are dynamic and liquid-like, whereas NRF2209-605-mEGFP droplets had relatively poor dynamics and droplet formation.","_id":"685af523b4ac24d5329d8c65"}],"states_connection":[],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_id":"GO:0140693","term_is_obsolete":false,"term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-12-07T09:18:04.550Z","_id":"685af523b4ac24d5329d8c66"},"version":0,"_id":"685af523b4ac24d5329d8c62","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Results","text":"o investigate whether these IDRs form phase-separated droplets in vitro, we purified a peptide containing the first IDR (NRF21-208) and a peptide containing the second and third IDRs (NRF2209-605), each tagged with mEGFP (monomeric enhanced green fluorescent protein) (Fig. 7B).","_id":"685af523b4ac24d5329d8c69"}],"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","_id":"685af523b4ac24d5329d8c68"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T15:36:49.900Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006067","ec_name":"fluorescence recovery after photobleaching evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":208,"interaction_partner":[],"reference_html":"Activation of NRF2 ameliorates oxidative stress and cystogenesis in autosomal dominant polycystic kidney disease. <i> Lu Y, Sun Y, Liu Z, Lu Y, Zhu X, Lan B, Mi Z, Dang L, Li N, Zhan W, Tan L, Pi J, Xiong H, Zhang L, Chen Y. </i> Sci Transl Med, 2020","reference_id":"32727915","region_id":"DP01115r019","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"Consistent with the FRAP analysis, fusion analysis showed that NRF21-208 droplets fused into one droplet within seconds (Fig. 7E). These results indicated that NRF21-208-mEGFP droplets are dynamic and liquid-like, whereas NRF2209-605-mEGFP droplets had relatively poor dynamics and droplet formation.","_id":"685af523b4ac24d5329d8c6a"}],"states_connection":[],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_id":"GO:0140693","term_is_obsolete":false,"term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-12-07T09:18:06.793Z","_id":"685af523b4ac24d5329d8c6b"},"version":0,"_id":"685af523b4ac24d5329d8c67","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"statements":[{"type":"Results","text":"o investigate whether these IDRs form phase-separated droplets in vitro, we purified a peptide containing the first IDR (NRF21-208) and a peptide containing the second and third IDRs (NRF2209-605), each tagged with mEGFP (monomeric enhanced green fluorescent protein) (Fig. 7B).","_id":"685af523b4ac24d5329d8c6e"}],"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","_id":"685af523b4ac24d5329d8c6d"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T15:44:10.309Z","disprot_namespace":"Disorder function","ec_go":"IMP","ec_id":"ECO:0007089","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":208,"interaction_partner":[],"reference_html":"Activation of NRF2 ameliorates oxidative stress and cystogenesis in autosomal dominant polycystic kidney disease. <i> Lu Y, Sun Y, Liu Z, Lu Y, Zhu X, Lan B, Mi Z, Dang L, Li N, Zhan W, Tan L, Pi J, Xiong H, Zhang L, Chen Y. </i> Sci Transl Med, 2020","reference_id":"32727915","region_id":"DP01115r020","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"We expressed either full-length NRF2 fused to EGFP or the NRF2 peptide lacking the first IDR (EGFP-NRF2209-605) in NRF2 knockout cells (fig. S7C). Only full-length NRF2 increases the expression of NRF2 target genes (Fig. 7G), suggesting that the first IDR is required for NRF2 transactivation.","_id":"685af523b4ac24d5329d8c6f"}],"states_connection":[],"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription.\" [GOC:go_curators, GOC:txnOH]","term_id":"GO:0045893","term_is_obsolete":false,"term_name":"positive regulation of transcription, DNA-templated","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-12-07T09:18:09.375Z","_id":"685af523b4ac24d5329d8c70"},"version":0,"_id":"685af523b4ac24d5329d8c6c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T15:55:17.209Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005804","ec_name":"immunofluorescence evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":605,"interaction_partner":[],"reference_html":"Activation of NRF2 ameliorates oxidative stress and cystogenesis in autosomal dominant polycystic kidney disease. <i> Lu Y, Sun Y, Liu Z, Lu Y, Zhu X, Lan B, Mi Z, Dang L, Li N, Zhan W, Tan L, Pi J, Xiong H, Zhang L, Chen Y. </i> Sci Transl Med, 2020","reference_id":"32727915","region_id":"DP01115r021","released":"2023_12","sample":[{"db":"Cellosaurus","deviation":null,"id":"CVCL_K230","statements":[],"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_id":"UO:0000201","unit_name":"cells/ml","value":null,"_id":"685af523b4ac24d5329d8c72"}],"statement":[{"type":"Results","text":"We detected NRF2-positive nuclear puncta in WT 9-12 ADPKD cells, and the size and the number of NRF2-positive puncta increased upon SFN treatment (Fig. 8A). Costaining for NRF2 and MED1 showed that they partially colocalized at puncta in the nuclei of cells (Fig. 8B), suggesting that NRF2 associates with Mediator condensates in vivo.","_id":"685af523b4ac24d5329d8c73"},{"type":"Results","text":"Together, these results showed that NRF2 and the Mediator complex form phase-separated condensates at superenhancers to regulate NRF2 target gene expression, including cytoprotective genes.","_id":"685af523b4ac24d5329d8c74"}],"states_connection":[],"term_comment":"","term_def":"\"A protein complex that interacts with the carboxy-terminal domain of the largest subunit of RNA polymerase II and plays an active role in transducing the signal from a transcription factor to the transcriptional machinery. The mediator complex is required for activation of transcription of most protein-coding genes, but can also act as a transcriptional corepressor. The Saccharomyces complex contains several identifiable subcomplexes: a head domain comprising Srb2, -4, and -5, Med6, -8, and -11, and Rox3 proteins; a middle domain comprising Med1, -4, and -7, Nut1 and -2, Cse2, Rgr1, Soh1, and Srb7 proteins; a tail consisting of Gal11p, Med2p, Pgd1p, and Sin4p; and a regulatory subcomplex comprising Ssn2, -3, and -8, and Srb8 proteins. Metazoan mediator complexes have similar modular structures and include homologs of yeast Srb and Med proteins.\" [PMID:11454195, PMID:16168358, PMID:17870225]","term_id":"GO:0016592","term_is_obsolete":false,"term_name":"mediator complex","term_namespace":"Cellular component","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-12-07T09:18:11.608Z","_id":"685af523b4ac24d5329d8c75"},"version":0,"_id":"685af523b4ac24d5329d8c71","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-11-22T15:55:09.314Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005804","ec_name":"immunofluorescence evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":605,"interaction_partner":[],"reference_html":"Activation of NRF2 ameliorates oxidative stress and cystogenesis in autosomal dominant polycystic kidney disease. <i> Lu Y, Sun Y, Liu Z, Lu Y, Zhu X, Lan B, Mi Z, Dang L, Li N, Zhan W, Tan L, Pi J, Xiong H, Zhang L, Chen Y. </i> Sci Transl Med, 2020","reference_id":"32727915","region_id":"DP01115r022","released":"2023_12","sample":[{"db":"Cellosaurus","deviation":null,"id":"CVCL_K230","statements":[],"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_id":"UO:0000201","unit_name":"cells/ml","value":null,"_id":"685af523b4ac24d5329d8c77"}],"statement":[{"type":"Results","text":"We detected NRF2-positive nuclear puncta in WT 9-12 ADPKD cells, and the size and the number of NRF2-positive puncta increased upon SFN treatment (Fig. 8A). Costaining for NRF2 and MED1 showed that they partially colocalized at puncta in the nuclei of cells (Fig. 8B), suggesting that NRF2 associates with Mediator condensates in vivo.","_id":"685af523b4ac24d5329d8c78"},{"type":"Results","text":"Together, these results showed that NRF2 and the Mediator complex form phase-separated condensates at superenhancers to regulate NRF2 target gene expression, including cytoprotective genes.","_id":"685af523b4ac24d5329d8c79"}],"states_connection":[],"term_comment":"","term_def":"\"Organized structure of distinctive morphology and function, not bounded by a lipid bilayer membrane. Includes ribosomes, the cytoskeleton and chromosomes.\" [GOC:go_curators]","term_id":"GO:0043228","term_is_obsolete":false,"term_name":"non-membrane-bounded organelle","term_namespace":"Cellular component","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-12-07T09:18:14.468Z","_id":"685af523b4ac24d5329d8c7a"},"version":0,"_id":"685af523b4ac24d5329d8c76","reference_source":"pmid"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":16,"type":"D"},{"start":17,"end":46,"type":"T"},{"start":47,"end":605,"type":"D"}],"Structural state":[{"start":1,"end":605,"type":"D"}],"Molecular function":[{"start":1,"end":605,"type":"F"}],"Structural transition":[{"start":17,"end":46,"type":"T"}],"Biological process":[{"start":1,"end":208,"type":"F"}],"Cellular component":[{"start":1,"end":605,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00628","name":"PHD-finger","start":1482,"end":1530},{"id":"PF00628","name":"PHD-finger","start":1569,"end":1624},{"id":"PF00856","name":"SET domain","start":3840,"end":3945},{"id":"PF02008","name":"CXXC zinc finger domain","start":1148,"end":1194},{"id":"PF05964","name":"F/Y-rich N-terminus","start":2019,"end":2074},{"id":"PF05965","name":"F/Y rich C-terminus","start":3669,"end":3748},{"id":"PF13771","name":"PHD-like zinc-binding domain","start":1900,"end":1978}],"gene3D":[{"start":1563,"end":1628,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":1429,"end":1540,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":1866,"end":1980,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":2020,"end":2136,"id":"3.30.160.360","name":"3.30.160.360"},{"start":3813,"end":3969,"id":"2.170.270.10","name":"SET domain"}]},"uniref50":"UniRef50_Q03164","sequence":"MAHSCRWRFPARPGTTGGGGGGGRRGLGGAPRQRVPALLLPPGPPVGGGGPGAPPSPPAVAAAAAAAGSSGAGVPGGAAAASAASSSSASSSSSSSSSASSGPALLRVGPGFDAALQVSAAIGTNLRRFRAVFGESGGGGGSGEDEQFLGFGSDEEVRVRSPTRSPSVKTSPRKPRGRPRSGSDRNSAILSDPSVFSPLNKSETKSGDKIKKKDSKSIEKKRGRPPTFPGVKIKITHGKDISELPKGNKEDSLKKIKRTPSATFQQATKIKKLRAGKLSPLKSKFKTGKLQIGRKGVQIVRRRGRPPSTERIKTPSGLLINSELEKPQKVRKDKEGTPPLTKEDKTVVRQSPRRIKPVRIIPSSKRTDATIAKQLLQRAKKGAQKKIEKEAAQLQGRKVKTQVKNIRQFIMPVVSAISSRIIKTPRRFIEDEDYDPPIKIARLESTPNSRFSAPSCGSSEKSSAASQHSSQMSSDSSRSSSPSVDTSTDSQASEEIQVLPEERSDTPEVHPPLPISQSPENESNDRRSRRYSVSERSFGSRTTKKLSTLQSAPQQQTSSSPPPPLLTPPPPLQPASSISDHTPWLMPPTIPLASPFLPASTAPMQGKRKSILREPTFRWTSLKHSRSEPQYFSSAKYAKEGLIRKPIFDNFRPPPLTPEDVGFASGFSASGTAASARLFSPLHSGTRFDMHKRSPLLRAPRFTPSEAHSRIFESVTLPSNRTSAGTSSSGVSNRKRKRKVFSPIRSEPRSPSHSMRTRSGRLSSSELSPLTPPSSVSSSLSISVSPLATSALNPTFTFPSHSLTQSGESAEKNQRPRKQTSAPAEPFSSSSPTPLFPWFTPGSQTERGRNKDKAPEELSKDRDADKSVEKDKSRERDREREKENKRESRKEKRKKGSEIQSSSALYPVGRVSKEKVVGEDVATSSSAKKATGRKKSSSHDSGTDITSVTLGDTTAVKTKILIKKGRGNLEKTNLDLGPTAPSLEKEKTLCLSTPSSSTVKHSTSSIGSMLAQADKLPMTDKRVASLLKKAKAQLCKIEKSKSLKQTDQPKAQGQESDSSETSVRGPRIKHVCRRAAVALGRKRAVFPDDMPTLSALPWEEREKILSSMGNDDKSSIAGSEDAEPLAPPIKPIKPVTRNKAPQEPPVKKGRRSRRCGQCPGCQVPEDCGVCTNCLDKPKFGGRNIKKQCCKMRKCQNLQWMPSKAYLQKQAKAVKKKEKKSKTSEKKDSKESSVVKNVVDSSQKPTPSAREDPAPKKSSSEPPPRKPVEEKSEEGNVSAPGPESKQATTPASRKSSKQVSQPALVIPPQPPTTGPPRKEVPKTTPSEPKKKQPPPPESGPEQSKQKKVAPRPSIPVKQKPKEKEKPPPVNKQENAGTLNILSTLSNGNSSKQKIPADGVHRIRVDFKEDCEAENVWEMGGLGILTSVPITPRVVCFLCASSGHVEFVYCQVCCEPFHKFCLEENERPLEDQLENWCCRRCKFCHVCGRQHQATKQLLECNKCRNSYHPECLGPNYPTKPTKKKKVWICTKCVRCKSCGSTTPGKGWDAQWSHDFSLCHDCAKLFAKGNFCPLCDKCYDDDDYESKMMQCGKCDRWVHSKCENLSDEMYEILSNLPESVAYTCVNCTERHPAEWRLALEKELQISLKQVLTALLNSRTTSHLLRYRQAAKPPDLNPETEESIPSRSSPEGPDPPVLTEVSKQDDQQPLDLEGVKRKMDQGNYTSVLEFSDDIVKIIQAAINSDGGQPEIKKANSMVKSFFIRQMERVFPWFSVKKSRFWEPNKVSSNSGMLPNAVLPPSLDHNYAQWQEREENSHTEQPPLMKKIIPAPKPKGPGEPDSPTPLHPPTPPILSTDRSREDSPELNPPPGIEDNRQCALCLTYGDDSANDAGRLLYIGQNEWTHVNCALWSAEVFEDDDGSLKNVHMAVIRGKQLRCEFCQKPGATVGCCLTSCTSNYHFMCSRAKNCVFLDDKKVYCQRHRDLIKGEVVPENGFEVFRRVFVDFEGISLRRKFLNGLEPENIHMMIGSMTIDCLGILNDLSDCEDKLFPIGYQCSRVYWSTTDARKRCVYTCKIVECRPPVVEPDINSTVEHDENRTIAHSPTSFTESSSKESQNTAEIISPPSPDRPPHSQTSGSCYYHVISKVPRIRTPSYSPTQRSPGCRPLPSAGSPTPTTHEIVTVGDPLLSSGLRSIGSRRHSTSSLSPQRSKLRIMSPMRTGNTYSRNNVSSVSTTGTATDLESSAKVVDHVLGPLNSSTSLGQNTSTSSNLQRTVVTVGNKNSHLDGSSSSEMKQSSASDLVSKSSSLKGEKTKVLSSKSSEGSAHNVAYPGIPKLAPQVHNTTSRELNVSKIGSFAEPSSVSFSSKEALSFPHLHLRGQRNDRDQHTDSTQSANSSPDEDTEVKTLKLSGMSNRSSIINEHMGSSSRDRRQKGKKSCKETFKEKHSSKSFLEPGQVTTGEEGNLKPEFMDEVLTPEYMGQRPCNNVSSDKIGDKGLSMPGVPKAPPMQVEGSAKELQAPRKRTVKVTLTPLKMENESQSKNALKESSPASPLQIESTSPTEPISASENPGDGPVAQPSPNNTSCQDSQSNNYQNLPVQDRNLMLPDGPKPQEDGSFKRRYPRRSARARSNMFFGLTPLYGVRSYGEEDIPFYSSSTGKKRGKRSAEGQVDGADDLSTSDEDDLYYYNFTRTVISSGGEERLASHNLFREEEQCDLPKISQLDGVDDGTESDTSVTATTRKSSQIPKRNGKENGTENLKIDRPEDAGEKEHVTKSSVGHKNEPKMDNCHSVSRVKTQGQDSLEAQLSSLESSRRVHTSTPSDKNLLDTYNTELLKSDSDNNNSDDCGNILPSDIMDFVLKNTPSMQALGESPESSSSELLNLGEGLGLDSNREKDMGLFEVFSQQLPTTEPVDSSVSSSISAEEQFELPLELPSDLSVLTTRSPTVPSQNPSRLAVISDSGEKRVTITEKSVASSESDPALLSPGVDPTPEGHMTPDHFIQGHMDADHISSPPCGSVEQGHGNNQDLTRNSSTPGLQVPVSPTVPIQNQKYVPNSTDSPGPSQISNAAVQTTPPHLKPATEKLIVVNQNMQPLYVLQTLPNGVTQKIQLTSSVSSTPSVMETNTSVLGPMGGGLTLTTGLNPSLPTSQSLFPSASKGLLPMSHHQHLHSFPAATQSSFPPNISNPPSGLLIGVQPPPDPQLLVSESSQRTDLSTTVATPSSGLKKRPISRLQTRKNKKLAPSSTPSNIAPSDVVSNMTLINFTPSQLPNHPSLLDLGSLNTSSHRTVPNIIKRSKSSIMYFEPAPLLPQSVGGTAATAAGTSTISQDTSHLTSGSVSGLASSSSVLNVVSMQTTTTPTSSASVPGHVTLTNPRLLGTPDIGSISNLLIKASQQSLGIQDQPVALPPSSGMFPQLGTSQTPSTAAITAASSICVLPSTQTTGITAASPSGEADEHYQLQHVNQLLASKTGIHSSQRDLDSASGPQVSNFTQTVDAPNSMGLEQNKALSSAVQASPTSPGGSPSSPSSGQRSASPSVPGPTKPKPKTKRFQLPLDKGNGKKHKVSHLRTSSSEAHIPDQETTSLTSGTGTPGAEAEQQDTASVEQSSQKECGQPAGQVAVLPEVQVTQNPANEQESAEPKTVEEEESNFSSPLMLWLQQEQKRKESITEKKPKKGLVFEISSDDGFQICAESIEDAWKSLTDKVQEARSNARLKQLSFAGVNGLRMLGILHDAVVFLIEQLSGAKHCRNYKFRFHKPEEANEPPLNPHGSARAEVHLRKSAFDMFNFLASKHRQPPEYNPNDEEEEEVQLKSARRATSMDLPMPMRFRHLKKTSKEAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGNVIRSIQTDKREKYYDSKGIGCYMFRIDDSEVVDATMHGNAARFINHSCEPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDASNKLPCNCGAKKCRKFLN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q03164","disprot_id":"DP01116","ncbi_taxon_id":9606,"regions_counter":3,"creator":"tlazar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":160,"region_id":"DP01116r001","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Validation and structural characterization of the LEDGF/p75-MLL interface as a new target for the treatment of MLL-dependent leukemia. <i> Cermáková K, Tesina P, Demeulemeester J, El Ashkar S, Méreau H, Schwaller J, Rezáčová P, Veverka V, De Rijck J. </i> Cancer Res, 2014","statement":[{"text":"In addition, the lack of a defined conformation in the backbone region of bound MLL140–160 between anchored residues F148 and F151 is in agreement with the absence of amide proton signals for G150 and F151 in NMR spectra due to exchange-related signal broadening.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"tlazar","start":140,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2022-08-03T16:15:04.881Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2MSR"},{"db":"BMRB","id":"25130"}],"reference_id":"25082813","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-03T18:27:43.195Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":160,"term_name":"protein binding","released":"2022_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Validation and structural characterization of the LEDGF/p75-MLL interface as a new target for the treatment of MLL-dependent leukemia. <i> Cermáková K, Tesina P, Demeulemeester J, El Ashkar S, Méreau H, Schwaller J, Rezáčová P, Veverka V, De Rijck J. </i> Cancer Res, 2014","statement":[{"text":"MLL forms a ternary complex with the lens epithelium–derived growth factor (LEDGF/p75) and MENIN.","type":"Abstract"},{"text":"MLL140–160 is anchored between the two interhelical loops of LEDGF/p75 IBD (aa I359 to D369 and K402 to M413) via F148 and F151 (Fig. 3B).","type":"Results"}],"term_id":"GO:0005515","curator_id":"tlazar","start":140,"term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"25082813","version":4,"curator_orcid":"0000-0001-7496-6711","date":"2022-08-03T16:19:29.532Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01116r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"BMRB","id":"25130"},{"db":"PDB","id":"2MSR"}],"interaction_partner":[{"db":"UniProt","id":"O75475","operator":"and","partner_start":344,"partner_end":426}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-03T18:27:41.309Z"}},{"start":140,"end":160,"reference_id":"25082813","reference_source":"pmid","reference_html":"Validation and structural characterization of the LEDGF/p75-MLL interface as a new target for the treatment of MLL-dependent leukemia. <i> Cermáková K, Tesina P, Demeulemeester J, El Ashkar S, Méreau H, Schwaller J, Rezáčová P, Veverka V, De Rijck J. </i> Cancer Res, 2014","date":"2022-08-03T16:27:46.630Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"O75475","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01116r003","statement":[{"text":"Binding of MLL140–160 to the IBD was further investigated using ITC. The ITC results corresponded with a stoichiometry close to 1:1 (n = 1.15). They were fitted by a single-site binding model, which provided the dissociation constant (Kd) of 86.3 ± 21.3 μmol/L (Fig. 2E). These results confirmed the existence of an additional interface between LEDGF/p75 and MLL.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-03T18:27:42.255Z"}}],"released":"2018_11","uniref100":"UniRef100_Q03164","date":"2018-06-19T11:36:02.000Z","acc":"Q03164","name":"Histone-lysine N-methyltransferase 2A","length":3969,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI0000161C5A","genes":[{"name":{"value":"KMT2A"},"synonyms":[{"value":"ALL1"},{"value":"CXXC7"},{"value":"HRX"},{"value":"HTRX"},{"value":"MLL"},{"value":"MLL1"},{"value":"TRX1"}]}],"disorder_content":0.005291005291005291,"disprot_consensus":{"full":[{"start":140,"end":160,"type":"D"}],"Structural state":[{"start":140,"end":160,"type":"D"}],"Molecular function":[{"start":140,"end":160,"type":"F"}]}},{"features":{"pfam":[{"id":"PF08311","name":"Mad3/BUB1 homology region 1","start":57,"end":179}],"gene3D":[{"start":782,"end":1042,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"},{"start":57,"end":220,"id":"1.25.40.430","name":"1.25.40.430"}]},"uniref50":"UniRef50_O60566","sequence":"MAAVKKEGGALSEAMSLEGDEWELSKENVQPLRQGRIMSTLQGALAQESACNNTLQQQKRAFEYEIRFYTGNDPLDVWDRYISWTEQNYPQGGKESNMSTLLERAVEALQGEKRYYSDPRFLNLWLKLGRLCNEPLDMYSYLHNQGIGVSLAQFYISWAEEYEARENFRKADAIFQEGIQQKAEPLERLQSQHRQFQARVSRQTLLALEKEEEEEVFESSVPQRSTLAELKSKGKKTARAPIIRVGGALKAPSQNRGLQNPFPQQMQNNSRITVFDENADEASTAELSKPTVQPWIAPPMPRAKENELQAGPWNTGRSLEHRPRGNTASLIAVPAVLPSFTPYVEETARQPVMTPCKIEPSINHILSTRKPGKEEGDPLQRVQSHQQASEEKKEKMMYCKEKIYAGVGEFSFEEIRAEVFRKKLKEQREAELLTSAEKRAEMQKQIEEMEKKLKEIQTTQQERTGDQQEETMPTKETTKLQIASESQKIPGMTLSSSVCQVNCCARETSLAENIWQEQPHSKGPSVPFSIFDEFLLSEKKNKSPPADPPRVLAQRRPLAVLKTSESITSNEDVSPDVCDEFTGIEPLSEDAIITGFRNVTICPNPEDTCDFARAARFVSTPFHEIMSLKDLPSDPERLLPEEDLDVKTSEDQQTACGTIYSQTLSIKKLSPIIEDSREATHSSGFSGSSASVASTSSIKCLQIPEKLELTNETSENPTQSPWCSQYRRQLLKSLPELSASAELCIEDRPMPKLEIEKEIELGNEDYCIKREYLICEDYKLFWVAPRNSAELTVIKVSSQPVPWDFYINLKLKERLNEDFDHFCSCYQYQDGCIVWHQYINCFTLQDLLQHSEYITHEITVLIIYNLLTIVEMLHKAEIVHGDLSPRCLILRNRIHDPYDCNKNNQALKIVDFSYSVDLRVQLDVFTLSGFRTVQILEGQKILANCSSPYQVDLFGIADLAHLLLFKEHLQVFWDGSFWKLSQNISELKDGELWNKFFVRILNANDEATVSVLGELAAEMNGVFDTTFQSHLNKALWKVGKLTSPGALLFQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O60566","disprot_id":"DP01117","ncbi_taxon_id":9606,"regions_counter":3,"creator":"tlazar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":42,"region_id":"DP01117r001","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Structural analysis of human Cdc20 supports multisite degron recognition by APC/C. <i> Tian W, Li B, Warrington R, Tomchick DR, Yu H, Luo X. </i> Proc Natl Acad Sci U S A, 2012","statement":[{"text":"The region represents a linear degradation motif [degron]: DEG_APCC_KENBOX_2","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"tlazar","start":20,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2022-08-03T16:36:36.351Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4GGD"},{"db":"ELM","id":"DEG_APCC_KENBOX_2"},{"db":"ELM","id":"ELMI002601"}],"reference_id":"23091007","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-03T18:28:26.491Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":42,"term_name":"protein binding","released":"2022_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural analysis of human Cdc20 supports multisite degron recognition by APC/C. <i> Tian W, Li B, Warrington R, Tomchick DR, Yu H, Luo X. </i> Proc Natl Acad Sci U S A, 2012","statement":[{"text":"Checkpoint inhibition of APC/CCdc20 requires the binding of a BubR1 KEN box to Cdc20.","type":"Abstract"}],"term_id":"GO:0005515","curator_id":"tlazar","start":20,"term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"23091007","version":4,"curator_orcid":"0000-0001-7496-6711","date":"2022-08-03T16:59:10.877Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01117r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"ELM","id":"DEG_APCC_KENBOX_2"},{"db":"ELM","id":"ELMI002601"},{"db":"PDB","id":"4GGD"}],"interaction_partner":[{"db":"UniProt","id":"Q12834","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-03T18:28:46.376Z"}},{"start":20,"end":42,"reference_id":"23091007","reference_source":"pmid","reference_html":"Structural analysis of human Cdc20 supports multisite degron recognition by APC/C. <i> Tian W, Li B, Warrington R, Tomchick DR, Yu H, Luo X. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-08-03T16:58:44.299Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001254","ec_ontology":"ECO","ec_name":"radioisotope assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"Q12834","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01117r003","statement":[{"text":"Addition of the synthetic BubR1 KEN1 peptide reduced, but did not abolish, Cdc20 binding to BubR1N, indicating that other regions of BubR1N contributed to Cdc20 binding (Fig. S2B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"cross_refs":[{"db":"ELM","id":"DEG_APCC_KENBOX_2"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-03T18:28:45.808Z"}}],"released":"2018_11","uniref100":"UniRef100_O60566","date":"2018-06-19T11:56:26.000Z","acc":"O60566","name":"Mitotic checkpoint serine/threonine-protein kinase BUB1 beta","length":1050,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI0000529D35","genes":[{"name":{"value":"BUB1B"},"synonyms":[{"value":"BUBR1"},{"value":"MAD3L"},{"value":"SSK1"}]}],"alphafold_very_low_content":0.35904761904761906,"disorder_content":0.021904761904761906,"disprot_consensus":{"full":[{"start":20,"end":42,"type":"D"}],"Structural state":[{"start":20,"end":42,"type":"D"}],"Molecular function":[{"start":20,"end":42,"type":"F"}]}},{"features":{"pfam":[{"id":"PF24807","name":"CDC20/Fizzy WD40 domain","start":176,"end":470}],"gene3D":[{"start":160,"end":477,"id":"2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"}]},"uniref50":"UniRef50_Q12834","sequence":"MAQFAFESDLHSLLQLDAPIPNAPPARWQRKAKEAAGPAPSPMRAANRSHSAGRTPGRTPGKSSSKVQTTPSKPGGDRYIPHRSAAQMEVASFLLSKENQPENSQTPTKKEHQKAWALNLNGFDVEEAKILRLSGKPQNAPEGYQNRLKVLYSQKATPGSSRKTCRYIPSLPDRILDAPEIRNDYYLNLVDWSSGNVLAVALDNSVYLWSASSGDILQLLQMEQPGEYISSVAWIKEGNYLAVGTSSAEVQLWDVQQQKRLRNMTSHSARVGSLSWNSYILSSGSRSGHIHHHDVRVAEHHVATLSGHSQEVCGLRWAPDGRHLASGGNDNLVNVWPSAPGEGGWVPLQTFTQHQGAVKAVAWCPWQSNVLATGGGTSDRHIRIWNVCSGACLSAVDAHSQVCSILWSPHYKELISGHGFAQNQLVIWKYPTMAKVAELKGHTSRVLSLTMSPDGATVASAAADETLRLWRCFELDPARRREREKASAAKSSLIHQGIR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q12834","disprot_id":"DP01118","ncbi_taxon_id":9606,"regions_counter":2,"creator":"tlazar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":164,"region_id":"DP01118r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural analysis of human Cdc20 supports multisite degron recognition by APC/C. <i> Tian W, Li B, Warrington R, Tomchick DR, Yu H, Luo X. </i> Proc Natl Acad Sci U S A, 2012","statement":[{"text":"Both the N-terminal region (residues 81–164) and the C-terminal region (residues 477–499; including the IR motif) of Cdc20ΔN80 were disordered and not visible in the structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"tlazar","start":81,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4GGD"}],"reference_id":"23091007","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-22T17:50:20.770Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":499,"region_id":"DP01118r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural analysis of human Cdc20 supports multisite degron recognition by APC/C. <i> Tian W, Li B, Warrington R, Tomchick DR, Yu H, Luo X. </i> Proc Natl Acad Sci U S A, 2012","statement":[{"text":"Both the N-terminal region (residues 81–164) and the C-terminal region (residues 477–499; including the IR motif) of Cdc20ΔN80 were disordered and not visible in the structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"tlazar","start":477,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4GGD"}],"reference_id":"23091007","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-22T17:50:21.720Z"}}],"released":"2018_11","uniref100":"UniRef100_Q12834","date":"2018-06-19T12:04:51.000Z","acc":"Q12834","name":"Cell division cycle protein 20 homolog","length":499,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000048D5D","genes":[{"name":{"value":"CDC20"}}],"alphafold_very_low_content":0.09619238476953908,"disorder_content":0.21442885771543085,"disprot_consensus":{"full":[{"start":81,"end":164,"type":"D"},{"start":477,"end":499,"type":"D"}],"Structural state":[{"start":81,"end":164,"type":"D"},{"start":477,"end":499,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":229,"end":262},{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":351,"end":390},{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":432,"end":473},{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":584,"end":622}],"gene3D":[{"start":133,"end":686,"id":"1.25.10.10","name":"Leucine-rich Repeat Variant"}]},"uniref50":"UniRef50_Q02248","sequence":"MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEPLGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q02248","disprot_id":"DP01119","ncbi_taxon_id":9606,"regions_counter":25,"creator":"bmesza","regions":[{"region_id":"DP01119r001","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T10:29:45.497Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":44,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":19,"version":2,"statement":[{"text":"In the case of the β-catenin substrate, the segment between the destruction motif and the lysine is unstructured","type":"Results"}],"term_name":"disorder","reference_html":"Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase. <i> Wu G, Xu G, Schulman BA, Jeffrey PD, Harper JW, Pavletich NP. </i> Mol Cell, 2003","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"12820959","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1P22"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"tlazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP01119r002","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T10:29:46.602Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":781,"term_id":"IDPO:0000002","start":692,"version":4,"statement":[{"text":"Only residues 665–691 of β-catenin C-terminal domain, which were also identified by MR method, were visible in the electron density maps before and after density modification.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"18334222","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2Z6H"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"bmesza","reference_html":"Crystal structure of a full-length beta-catenin. <i> Xing Y, Takemaru K, Liu J, Berndt JD, Zheng JJ, Moon RT, Xu W. </i> Structure, 2008","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":781,"region_id":"DP01119r003","reference_id":"18334222","start":687,"term_id":"IDPO:0000002","curator_orcid":"0000-0003-0919-4449","statement":[{"text":"The 15N-TROSY spectrum of 15N-labeled β-catenin C-terminal tail alone shows poor dispersion of the resonance, indicating that the C-terminal tail per se does not have any folded structure.","type":"Results"}],"curator_id":"bmesza","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":4,"reference_html":"Crystal structure of a full-length beta-catenin. <i> Xing Y, Takemaru K, Liu J, Berndt JD, Zheng JJ, Moon RT, Xu W. </i> Structure, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T10:29:47.886Z","curator_name":"Federica Quaglia"},"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":137,"region_id":"DP01119r004","reference_id":"18334222","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0003-0919-4449","statement":[{"text":"The N-terminal domain of β-catenin has a poor expression yield and tends to be degraded during purification.","type":"Results"}],"curator_id":"bmesza","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"cleavage assay evidence used in manual assertion","version":4,"reference_html":"Crystal structure of a full-length beta-catenin. <i> Xing Y, Takemaru K, Liu J, Berndt JD, Zheng JJ, Moon RT, Xu W. </i> Structure, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T10:29:48.554Z","curator_name":"Federica Quaglia"},"term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP01119r005","ec_ontology":"ECO","end":781,"term_id":"IDPO:0000011","start":772,"version":6,"statement":[{"text":"The high-resolution crystal structure of TIP-1 in complex with the C-terminal peptide of β-catenin provides molecular details for the recognition of β-catenin by TIP-1.","type":"Abstract"}],"term_name":"disorder to order","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0001-8399-7907","released":"2022_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18835279","date":"2022-08-08T18:52:52.961Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3DIW"},{"db":"ELM","id":"LIG_PDZ_Class_1"}],"term_namespace":"Structural transition","ec_id":"ECO:0005670","curator_id":"vnugnes","reference_html":"Structural basis of beta-catenin recognition by Tax-interacting protein-1. <i> Zhang J, Yan X, Shi C, Yang X, Guo Y, Tian C, Long J, Shen Y. </i> J Mol Biol, 2008","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9DBG9 "}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-15T21:22:31.536Z"}},{"region_id":"DP01119r006","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T10:29:52.020Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":781,"term_id":"GO:0005515","start":772,"version":5,"statement":[{"text":"The high-resolution crystal structure of TIP-1 in complex with the C-terminal peptide of β-catenin provides molecular details for the recognition of β-catenin by TIP-1.","type":"Abstract"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9DBG9","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","reference_html":"Structural basis of beta-catenin recognition by Tax-interacting protein-1. <i> Zhang J, Yan X, Shi C, Yang X, Guo Y, Tian C, Long J, Shen Y. </i> J Mol Biol, 2008","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"18835279","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3DIW"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"bmesza","curator_orcid":"0000-0003-0919-4449","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01119r007","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T10:29:52.736Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":44,"term_id":"GO:0005515","start":19,"version":5,"statement":[{"text":"The 3.0 Å structure of a β-TrCP1-Skp1-β-catenin complex reveals the basis of substrate recognition by the β-TrCP1 WD40 domain.","type":"Abstract"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9Y297","partner_end":null},{"partner_start":null,"db":"UniProt","id":"P63208","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","reference_html":"Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase. <i> Wu G, Xu G, Schulman BA, Jeffrey PD, Harper JW, Pavletich NP. </i> Mol Cell, 2003","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"12820959","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1P22"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"bmesza","curator_orcid":"0000-0003-0919-4449","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01119r008","ec_ontology":"ECO","end":44,"term_id":"IDPO:0000011","start":19,"version":5,"statement":[{"text":"The 3.0 Å structure of a β-TrCP1-Skp1-β-catenin complex reveals the basis of substrate recognition by the β-TrCP1 WD40 domain.","type":"Abstract"}],"term_name":"disorder to order","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0001-8399-7907","released":"2022_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12820959","date":"2022-06-15T17:58:46.504Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1P22"}],"term_namespace":"Structural transition","ec_id":"ECO:0005670","curator_id":"vnugnes","reference_html":"Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase. <i> Wu G, Xu G, Schulman BA, Jeffrey PD, Harper JW, Pavletich NP. </i> Mol Cell, 2003","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":" P63208 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y297"}],"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":33,"end":33,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":37,"end":37,"position":"Specific residue"}],"sequence_construct":"KAAVSHWQQQSYLDSGIHSGATTTAP","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T09:47:38.484Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":47,"region_id":"DP01119r009","reference_id":"12051714","start":43,"term_id":"IDPO:0000045","curator_orcid":"0000-0003-0919-4449","statement":[{"text":"In this study, the phosphorylation of b-catenin at Ser45 was characterised using a phospho-specific antibody.","type":"Abstract"}],"curator_id":"bmesza","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"immunodetection assay evidence used in manual assertion","version":4,"reference_html":"Characterisation of the phosphorylation of beta-catenin at the GSK-3 priming site Ser45. <i> Hagen T, Vidal-Puig A. </i> Biochem Biophys Res Commun, 2002","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T10:29:56.420Z","curator_name":"Federica Quaglia"},"term_name":"phosphorylation display site","ec_go":"IDA","disprot_namespace":"Disorder function"},{"region_id":"DP01119r010","ec_ontology":"ECO","end":21,"term_id":"IDPO:0000046","start":17,"version":5,"statement":[{"text":"These findings, together with the conservation of this lysine among β-catenin orthologs and paralogues (Table 1), suggest that Lys19 is a ubiquitination site of β-catenin in vivo.","type":"Results"}],"term_name":"ubiquitination display site","ec_name":"enzymatic activity assay evidence used in manual assertion","curator_orcid":"0000-0001-8399-7907","released":"2022_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12820959","date":"2022-06-15T18:05:32.350Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1P22"}],"term_namespace":"Disorder function","ec_id":"ECO:0005801","curator_id":"vnugnes","reference_html":"Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase. <i> Wu G, Xu G, Schulman BA, Jeffrey PD, Harper JW, Pavletich NP. </i> Mol Cell, 2003","ec_go":"IDA","disprot_namespace":"Disorder function","construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":33,"end":33,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":37,"end":37,"position":"Specific residue"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T09:48:48.400Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":25,"region_id":"DP01119r011","reference_id":"24342833","start":21,"term_id":"IDPO:0000041","curator_orcid":"0000-0003-0919-4449","statement":[{"text":"Serine 23 of β-catenin was determined as a site for O-GlcNAc modification which regulated its subcellular distribution, its interactions with cellular partners and consequently its transcriptional activity.","type":"Abstract"}],"curator_id":"bmesza","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"immunodetection assay evidence used in manual assertion","version":4,"reference_html":"β-catenin is O-GlcNAc glycosylated at Serine 23: implications for β-catenin's subcellular localization and transactivator function. <i> Ha JR, Hao L, Venkateswaran G, Huang YH, Garcia E, Persad S. </i> Exp Cell Res, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T10:29:58.452Z","curator_name":"Federica Quaglia"},"term_name":"glycosylation display site","ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":43,"region_id":"DP01119r012","reference_id":"11955436","start":39,"term_id":"IDPO:0000045","curator_orcid":"0000-0003-0919-4449","statement":[{"text":"LiCl is a potent GSK-3 inhibitor (Stambolic et al. 1996, Hedgepeth et al. 1997) and indeed suppressed T41/S37/S33 but not S45 phosphorylation (Figure 2B).","type":"Results"}],"curator_id":"bmesza","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"immunodetection assay evidence used in manual assertion","version":4,"reference_html":"Control of beta-catenin phosphorylation/degradation by a dual-kinase mechanism. <i> Liu C, Li Y, Semenov M, Han C, Baeg GH, Tan Y, Zhang Z, Lin X, He X. </i> Cell, 2002","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T10:29:59.568Z","curator_name":"Federica Quaglia"},"term_name":"phosphorylation display site","ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":39,"region_id":"DP01119r013","reference_id":"11955436","start":35,"term_id":"IDPO:0000045","curator_orcid":"0000-0003-0919-4449","statement":[{"text":"LiCl is a potent GSK-3 inhibitor (Stambolic et al. 1996, Hedgepeth et al. 1997) and indeed suppressed T41/S37/S33 but not S45 phosphorylation (Figure 2B).","type":"Results"}],"curator_id":"bmesza","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"immunodetection assay evidence used in manual assertion","version":4,"reference_html":"Control of beta-catenin phosphorylation/degradation by a dual-kinase mechanism. <i> Liu C, Li Y, Semenov M, Han C, Baeg GH, Tan Y, Zhang Z, Lin X, He X. </i> Cell, 2002","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T10:30:00.150Z","curator_name":"Federica Quaglia"},"term_name":"phosphorylation display site","ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":35,"region_id":"DP01119r014","reference_id":"11955436","start":31,"term_id":"IDPO:0000045","curator_orcid":"0000-0003-0919-4449","statement":[{"text":"LiCl is a potent GSK-3 inhibitor (Stambolic et al. 1996, Hedgepeth et al. 1997) and indeed suppressed T41/S37/S33 but not S45 phosphorylation (Figure 2B).","type":"Results"}],"curator_id":"bmesza","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"immunodetection assay evidence used in manual assertion","version":4,"reference_html":"Control of beta-catenin phosphorylation/degradation by a dual-kinase mechanism. <i> Liu C, Li Y, Semenov M, Han C, Baeg GH, Tan Y, Zhang Z, Lin X, He X. </i> Cell, 2002","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T10:30:01.020Z","curator_name":"Federica Quaglia"},"term_name":"phosphorylation display site","ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":25,"region_id":"DP01119r015","reference_id":"12027456","start":21,"term_id":"IDPO:0000045","curator_orcid":"0000-0003-0919-4449","statement":[{"text":"These data indicate that the S23 and S29 residues are indeed phosphorylated in vivo.","type":"Results"}],"curator_id":"bmesza","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"immunodetection assay evidence used in manual assertion","version":4,"reference_html":"Identification of two novel regulated serines in the N terminus of beta-catenin. <i> van Noort M, van de Wetering M, Clevers H. </i> Exp Cell Res, 2002","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T10:30:02.451Z","curator_name":"Federica Quaglia"},"term_name":"phosphorylation display site","ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":31,"region_id":"DP01119r016","reference_id":"12027456","start":27,"term_id":"IDPO:0000045","curator_orcid":"0000-0003-0919-4449","statement":[{"text":"These data indicate that the S23 and S29 residues are indeed phosphorylated in vivo.","type":"Results"}],"curator_id":"bmesza","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"immunodetection assay evidence used in manual assertion","version":4,"reference_html":"Identification of two novel regulated serines in the N terminus of beta-catenin. <i> van Noort M, van de Wetering M, Clevers H. </i> Exp Cell Res, 2002","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T10:30:03.252Z","curator_name":"Federica Quaglia"},"term_name":"phosphorylation display site","ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":51,"region_id":"DP01119r017","reference_id":"24824780","start":47,"term_id":"IDPO:0000039","curator_orcid":"0000-0003-0919-4449","statement":[{"text":"In line with loss of SIRT1 repression, expression of wild type MCC but not MCC‐R506Q mutant resulted in β‐cat‐K49 deacetylation (Fig. 6c).","type":"Results"}],"curator_id":"bmesza","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"immunodetection assay evidence used in manual assertion","version":4,"reference_html":"MCC inhibits beta-catenin transcriptional activity by sequestering DBC1 in the cytoplasm. <i> Pangon L, Mladenova D, Watkins L, Van Kralingen C, Currey N, Al-Sohaily S, Lecine P, Borg JP, Kohonen-Corish MR. </i> Int J Cancer, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T10:30:04.751Z","curator_name":"Federica Quaglia"},"term_name":"acetylation display site","ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":66,"region_id":"DP01119r018","reference_id":"20026641","start":62,"term_id":"IDPO:0000045","curator_orcid":"0000-0003-0919-4449","statement":[{"text":"PTK6 directly phosphorylates beta-catenin on Tyr64, Tyr142, Tyr331 and/or Tyr333, with the predominant site being Tyr64.","type":"Results"}],"curator_id":"bmesza","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"immunodetection assay evidence used in manual assertion","version":4,"reference_html":"Identification of beta-catenin as a target of the intracellular tyrosine kinase PTK6. <i> Palka-Hamblin HL, Gierut JJ, Bie W, Brauer PM, Zheng Y, Asara JM, Tyner AL. </i> J Cell Sci, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T10:30:05.419Z","curator_name":"Federica Quaglia"},"term_name":"phosphorylation display site","ec_go":"IDA","disprot_namespace":"Disorder function"},{"region_id":"DP01119r019","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T10:29:54.185Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":781,"term_id":"GO:0005515","start":772,"version":5,"statement":[{"text":"ITC experimentsusing our present system show weak binding of Lin-7 to the C-terminal of β-catenin (SupplementaryData Fig. 5).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9DBG9","partner_end":null}],"term_name":"protein binding","ec_name":"isothermal titration calorimetry evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"18835279","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"bmesza","reference_html":"Structural basis of beta-catenin recognition by Tax-interacting protein-1. <i> Zhang J, Yan X, Shi C, Yang X, Guo Y, Tian C, Long J, Shen Y. </i> J Mol Biol, 2008","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01119r020","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T10:29:54.968Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":781,"term_id":"GO:0005515","start":683,"version":5,"statement":[{"text":"To test whether Fhit directly interacts with LEF-1 or β-catenin, in vitro pull-down experiments with purified recombinant fusion proteins were performed. In contrast to Hint1, Fhit directly associates with β-catenin.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P49789","partner_end":null}],"term_name":"protein binding","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"18077326","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006077","curator_id":"bmesza","reference_html":"The tumor suppressor Fhit acts as a repressor of beta-catenin transcriptional activity. <i> Weiske J, Albring KF, Huber O. </i> Proc Natl Acad Sci U S A, 2007","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":31,"end":35,"reference_id":"15829978","reference_source":"pmid","reference_html":"Functional correlates of mutation of the Asp32 and Gly34 residues of beta-catenin. <i> Provost E, McCabe A, Stern J, Lizardi I, D'Aquila TG, Rimm DL. </i> Oncogene, 2005","date":"2022-07-06T18:21:34.468Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031396","term_name":"regulation of protein ubiquitination","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp32Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly34Ala","start":null,"end":null,"position":null}],"region_id":"DP01119r021","statement":[{"text":"We demonstrate that the mutants D32A and G34A exhibit no change in phosphorylation by GSK3β, but display reduced ubiquitination compared to wild-type and S33A mutant β-catenin.","type":"Abstract"},{"text":"D32A and G34A were greatly reduced compared to WT β-catenin in their degree of ubiquitination.","type":"Results"},{"text":"Since the phosphorylation status of D32A and G34A is normal, we concluded that alterations to the ubiquitination status of β-catenin are due to its interaction with the ubiquitin machinery and its function as a ubiquitin substrate.","type":"Results"}],"ec_go":"IMP","term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of the addition of ubiquitin groups to a protein.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-11T13:12:56.344Z"}},{"start":33,"end":37,"reference_id":"15829978","reference_source":"pmid","reference_html":"Functional correlates of mutation of the Asp32 and Gly34 residues of beta-catenin. <i> Provost E, McCabe A, Stern J, Lizardi I, D'Aquila TG, Rimm DL. </i> Oncogene, 2005","date":"2022-07-04T14:50:37.607Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser33Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser37Ala","start":null,"end":null,"position":null}],"region_id":"DP01119r022","statement":[{"text":"A greater than 50% reduction in phosphorylation was seen in the QUAD (S33AS37AT41AS45A) and S33AS37A mutants, as expected for partial serine/threonine mutants of β-catenin. Since there are multiple kinase sites that are substrates for GSK3β, no β-catenin mutants showed complete loss of phosphorylation similar to the α-catenin control. ","type":"Results"},{"text":"The double serine mutant S33S37A served as a negative control, since β-TrCP-mediated ubiquitination of β-catenin is phosphorylation dependent.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T09:48:11.909Z"}},{"start":32,"end":37,"reference_id":"12820959","reference_source":"pmid","reference_html":"Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase. <i> Wu G, Xu G, Schulman BA, Jeffrey PD, Harper JW, Pavletich NP. </i> Mol Cell, 2003","date":"2022-08-08T18:47:08.441Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031625","term_name":"ubiquitin protein ligase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":33,"end":33,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":37,"end":37,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"1P22"},{"db":"ELM","id":"deg_scf_trcp1_1"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9Y297","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01119r023","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63208"}],"statement":[{"text":"The phosphoserine, aspartic acid, and hydrophobic residues of the destruction motif are recognized directly by contacts from β-TrCP1.","type":"Results"},{"text":"The destruction motif comprises the 32-37 region. ","type":"Curator statement"},{"text":"These findings support the structure-based conclusion that Asp32, pSer33, pSer37, and Gly34 are critical for β-TrCP1-β-catenin binding and specificity, while Ile35, which makes fewer contacts, plays a smaller role.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.\" [GOC:vp]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-03-15T09:07:03.686Z"}},{"start":30,"end":40,"reference_id":"12820959","reference_source":"pmid","reference_html":"Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase. <i> Wu G, Xu G, Schulman BA, Jeffrey PD, Harper JW, Pavletich NP. </i> Mol Cell, 2003","date":"2022-07-04T18:13:09.735Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":33,"end":33,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":37,"end":37,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"1P22"}],"region_id":"DP01119r024","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63208"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y297"}],"statement":[{"text":"Of the 26 β-catenin residues in the crystals, only an 11 residue segment (residues 30 to 40), centered on the doubly phosphorylated destruction motif (residues 32 to 37), is ordered in the structure.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T09:47:27.371Z"}},{"start":17,"end":21,"reference_id":"12820959","reference_source":"pmid","reference_html":"Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase. <i> Wu G, Xu G, Schulman BA, Jeffrey PD, Harper JW, Pavletich NP. </i> Mol Cell, 2003","date":"2022-07-04T18:34:48.797Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000046","term_name":"ubiquitination display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":33,"end":33,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":37,"end":37,"position":"Specific residue"}],"region_id":"DP01119r025","statement":[{"text":"When the R7 mutant of ubiquitin is used, the SCFβ-TrCP1 monoubiquitinates the doubly phosphorylated β-catenin (lane 3) and IκBα (lane 6) peptides at comparable rates. The reaction is dependent on Lys19 in the β-catenin peptide (lane 5) and is specific for β-TrCP1 because Cul1-Rbx1 (lane 7) or SCFSkp2-Cks1 (lane 8) cannot substitute for SCFβ-TrCP1. ","type":"Figure"},{"text":"These findings, together with the conservation of this lysine among β-catenin orthologs and paralogues (Table 1), suggest that Lys19 is a ubiquitination site of β-catenin in vivo.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-06T09:48:05.737Z"}}],"released":"2018_11","uniref100":"UniRef100_P35222","date":"2018-06-19T12:11:02.000Z","acc":"P35222","name":"Catenin beta-1","length":781,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins","Condensates-related proteins"],"UniParc":"UPI000012862F","genes":[{"name":{"value":"CTNNB1"},"synonyms":[{"value":"CTNNB"}],"orfNames":[{"value":"OK/SW-cl.35"},{"value":"PRO2286"}]}],"alphafold_very_low_content":0.21510883482714468,"disorder_content":0.2970550576184379,"disprot_consensus":{"full":[{"start":1,"end":18,"type":"D"},{"start":19,"end":44,"type":"T"},{"start":45,"end":137,"type":"D"},{"start":683,"end":686,"type":"F"},{"start":687,"end":771,"type":"D"},{"start":772,"end":781,"type":"T"}],"Structural state":[{"start":1,"end":137,"type":"D"},{"start":687,"end":781,"type":"D"}],"Structural transition":[{"start":19,"end":44,"type":"T"},{"start":772,"end":781,"type":"T"}],"Molecular function":[{"start":19,"end":44,"type":"F"},{"start":683,"end":781,"type":"F"}],"Disorder function":[{"start":17,"end":25,"type":"F"},{"start":27,"end":51,"type":"F"},{"start":62,"end":66,"type":"F"}],"Biological process":[{"start":31,"end":35,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00134","name":"Cyclin, N-terminal domain","start":115,"end":242},{"id":"PF02984","name":"Cyclin, C-terminal domain","start":245,"end":364}],"gene3D":[{"start":129,"end":242,"id":"1.10.472.10","name":"Cyclin-like"},{"start":115,"end":370,"id":"1.10.472.10","name":"Cyclin-like"}]},"uniref50":"UniRef50_P24864","sequence":"MPRERRERDAKERDTMKEDGGAEFSARSRKRKANVTVFLQDPDEEMAKIDRTARDQCGSQPWDNNAVCADPCSLIPTPDKEDDDRVYPNSTCKPRIIAPSRGSPLPVLSWANREEVWKIMLNKEKTYLRDQHFLEQHPLLQPKMRAILLDWLMEVCEVYKLHRETFYLAQDFFDRYMATQENVVKTLLQLIGISSLFIAAKLEEIYPPKLHQFAYVTDGACSGDEILTMELMIMKALKWRLSPLTIVSWLNVYMQVAYLNDLHEVLLPQYPQQIFIQIAELLDLCVLDVDCLEFPYGILAASALYHFSSSELMQKVSGYQWCDIENCVKWMVPFAMVIRETGSSKLKHFRGVADEDAHNIQTHRDSLDLLDKARAKKAMLSEQNRASPLPSGLLTPPQSGKKQSSGPEMA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P24864","disprot_id":"DP01120","ncbi_taxon_id":9606,"regions_counter":1,"creator":"tlazar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":373,"region_id":"DP01120r001","released":"2022_06","ec_id":"ECO:0006220","reference_html":"Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases. <i> Hao B, Oehlmann S, Sowa ME, Harper JW, Pavletich NP. </i> Mol Cell, 2007","statement":[{"text":"The N-terminal 14 residues, which contain the phosphorylated Ser372 (pSer372), and the C-terminal five residues are not visible in the electron density maps and are presumably disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":360,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-15T17:50:52.307Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2OVQ"}],"reference_id":"17434132","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":395,"end":395,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":372,"end":372,"position":"Specific residue"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q969H0"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63208 "}]}],"released":"2018_11","uniref100":"UniRef100_P24864","date":"2018-06-19T13:17:03.000Z","acc":"P24864","name":"G1/S-specific cyclin-E1","length":410,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI0000001C33","genes":[{"name":{"value":"CCNE1"},"synonyms":[{"value":"CCNE"}]}],"alphafold_very_low_content":0.24390243902439024,"disorder_content":0.03414634146341464,"disprot_consensus":{"full":[{"start":360,"end":373,"type":"D"}],"Structural state":[{"start":360,"end":373,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02309","name":"AUX/IAA family","start":10,"end":233}],"gene3D":[{"start":120,"end":237,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"}]},"uniref50":"UniRef50_Q38825","sequence":"MIGQLMNLKATELCLGLPGGAEAVESPAKSAVGSKRGFSETVDLMLNLQSNKEGSVDLKNVSAVPKEKTTLKDPSKPPAKAQVVGWPPVRNYRKNMMTQQKTSSGAEEASSEKAGNFGGGAAGAGLVKVSMDGAPYLRKVDLKMYKSYQDLSDALAKMFSSFTMGNYGAQGMIDFMNESKLMNLLNSSEYVPSYEDKDGDWMLVGDVPWEMFVESCKRLRIMKGSEAVGLAPRAMEKYCKNRS","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q38825","disprot_id":"DP01121","ncbi_taxon_id":3702,"regions_counter":2,"creator":"tlazar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":94,"region_id":"DP01121r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Mechanism of auxin perception by the TIR1 ubiquitin ligase. <i> Tan X, Calderon-Villalobos LI, Sharon M, Zheng C, Robinson CV, Estelle M, Zheng N. </i> Nature, 2007","statement":[{"text":"above the auxin-binding site, the highly coiled IAA7 peptide is docked to the upper part of the surface pocket","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"tlazar","start":82,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2P1Q"}],"reference_id":"17410169","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":94,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Mechanism of auxin perception by the TIR1 ubiquitin ligase. <i> Tan X, Calderon-Villalobos LI, Sharon M, Zheng C, Robinson CV, Estelle M, Zheng N. </i> Nature, 2007","statement":[{"text":"peptide adopts a highly coiled conformation and fills the TIR1 pocket with the central hydrophobic consensus motif","type":"Results"}],"term_id":"GO:0005515","curator_id":"tlazar","start":82,"term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"17410169","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01121r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q38825","date":"2018-06-19T13:25:12.000Z","acc":"Q38825","name":"Auxin-responsive protein IAA7","length":243,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI0000000E29","genes":[{"name":{"value":"IAA7"},"synonyms":[{"value":"AXR2"}],"orfNames":[{"value":"MXC7.8"}],"olnNames":[{"value":"At3g23050"}]}],"alphafold_very_low_content":0.3333333333333333,"disorder_content":0.053497942386831275,"disprot_consensus":{"full":[{"start":82,"end":94,"type":"D"}],"Structural state":[{"start":82,"end":94,"type":"D"}],"Molecular function":[{"start":82,"end":94,"type":"F"}]}},{"features":{"pfam":[{"id":"PF07776","name":"Zinc-finger associated domain (zf-AD)","start":28,"end":96}]},"uniref50":"UniRef50_Q27934","sequence":"MSTNQQQQANPSAAVAAPAASSEYLKRTCLICGCHTNQTINIYEPRSGPNIVQLIQAKFKFQPLNEDKFLCFSCNNWLINWHSLQAVNSNEAESQSQSPSHMGNSVLQQERTKLRPVAMVRPTVRVQPQSQPQLQPQVPINPTPAPIVYSKRRASRRSASVSRMSRVLRQCCVESLRRSPKKRNQQSVFVCLRPQGQKRSNAICKVECVAPRRKPVERLVKDVAATATPTPVLNTQSTPTYQRFPQPSVDGKVVAMFRRLGTTLSREEPAAYSAESNPACSKLPQIMSPLKEAPRWTRDLDDDEILLEFDTAISEVLPTARYQVTHEENKENQQAQEMELELEEEEEVDGRAELEVVQEAEAPLEPQSHHKQGNSHQNSHQASIQLAGLRLPMGLSISLV","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_Q27934","disprot_id":"DP01122","ncbi_taxon_id":7227,"regions_counter":2,"creator":"tlazar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":130,"region_id":"DP01122r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Elucidation of the substrate binding site of Siah ubiquitin ligase. <i> House CM, Hancock NC, Möller A, Cromer BA, Fedorov V, Bowtell DD, Parker MW, Polekhina G. </i> Structure, 2006","statement":[{"text":"[degron DEG_SIAH_1] peptide used in the crystallization included residues 107–130. Thus, residues 108–113 and 125–130 were flexible and could not be modeled.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"tlazar","start":107,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"16615911","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":130,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Elucidation of the substrate binding site of Siah ubiquitin ligase. <i> House CM, Hancock NC, Möller A, Cromer BA, Fedorov V, Bowtell DD, Parker MW, Polekhina G. </i> Structure, 2006","statement":[{"text":"degron motif (PXAXVXP) (as defined by House et al., 2003) that do interact with Siah include Arg115 and Thr123","type":"Results"}],"term_id":"GO:0005515","curator_id":"tlazar","start":107,"term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"16615911","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01122r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q27934","date":"2018-06-19T13:42:25.000Z","acc":"Q27934","name":"Protein phyllopod","length":400,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI0000083F72","genes":[{"name":{"value":"phyl"},"orfNames":[{"value":"CG10108"}]}],"alphafold_very_low_content":0.445,"disorder_content":0.06,"disprot_consensus":{"full":[{"start":107,"end":130,"type":"D"}],"Structural state":[{"start":107,"end":130,"type":"D"}],"Molecular function":[{"start":107,"end":130,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00017","name":"SH2 domain","start":10,"end":87},{"id":"PF00017","name":"SH2 domain","start":163,"end":238},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":342,"end":592}],"gene3D":[{"start":113,"end":154,"id":"1.10.930.10","name":"Syk Kinase; Chain A, domain 2"},{"start":155,"end":264,"id":"3.30.505.10","name":"SH2 domain"},{"start":2,"end":112,"id":"3.30.505.10","name":"SH2 domain"},{"start":417,"end":607,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"},{"start":327,"end":416,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"}]},"uniref50":"UniRef50_P43403","sequence":"MPDPAAHLPFFYGSISRAEAEEHLKLAGMADGLFLLRQCLRSLGGYVLSLVHDVRFHHFPIERQLNGTYAIAGGKAHCGPAELCEFYSRDPDGLPCNLRKPCNRPSGLEPQPGVFDCLRDAMVRDYVRQTWKLEGEALEQAIISQAPQVEKLIATTAHERMPWYHSSLTREEAERKLYSGAQTDGKFLLRPRKEQGTYALSLIYGKTVYHYLISQDKAGKYCIPEGTKFDTLWQLVEYLKLKADGLIYCLKEACPNSSASNASGAAAPTLPAHPSTLTHPQRRIDTLNSDGYTPEPARITSPDKPRPMPMDTSVYESPYSDPEELKDKKLFLKRDNLLIADIELGCGNFGSVRQGVYRMRKKQIDVAIKVLKQGTEKADTEEMMREAQIMHQLDNPYIVRLIGVCQAEALMLVMEMAGGGPLHKFLVGKREEIPVSNVAELLHQVSMGMKYLEEKNFVHRDLAARNVLLVNRHYAKISDFGLSKALGADDSYYTARSAGKWPLKWYAPECINFRKFSSRSDVWSYGVTMWEALSYGQKPYKKMKGPEVMAFIEQGKRMECPPECPPELYALMSDCWIYKWEDRPDFLTVEQRMRACYYSLASKVEGPPGSTQKAEAACA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P43403","disprot_id":"DP01123","ncbi_taxon_id":9606,"regions_counter":3,"creator":"mguha","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":302,"region_id":"DP01123r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for activation of ZAP-70 by phosphorylation of the SH2-kinase linker. <i> Yan Q, Barros T, Visperas PR, Deindl S, Kadlecek TA, Weiss A, Kuriyan J. </i> Mol Cell Biol, 2013","statement":[{"text":"Two regions of the molecule appeared to be disordered and were not modeled. These were the N-terminal portion of the SH2-kinase linker (residues 258 to 302) and a portion of the activation loop of the kinase domain (residues 484 to 500).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mguha","start":258,"term_ontology":"IDPO","curator_name":"Mainak Guharoy","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4K2R"}],"reference_id":"23530057","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":500,"region_id":"DP01123r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for activation of ZAP-70 by phosphorylation of the SH2-kinase linker. <i> Yan Q, Barros T, Visperas PR, Deindl S, Kadlecek TA, Weiss A, Kuriyan J. </i> Mol Cell Biol, 2013","term_id":"IDPO:0000002","curator_id":"mguha","start":484,"term_ontology":"IDPO","curator_name":"Mainak Guharoy","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4K2R"}],"reference_id":"23530057","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":500,"term_name":"phosphorylation display site","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural basis for activation of ZAP-70 by phosphorylation of the SH2-kinase linker. <i> Yan Q, Barros T, Visperas PR, Deindl S, Kadlecek TA, Weiss A, Kuriyan J. </i> Mol Cell Biol, 2013","statement":[{"text":"Tyr493 located in the disordered part of the ZAP70 activation loop is phosphorylated","type":"Results"}],"term_id":"IDPO:0000045","curator_id":"mguha","start":484,"term_ontology":"IDPO","curator_name":"Mainak Guharoy","reference_id":"23530057","version":2,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01123r003","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_P43403","date":"2018-06-20T09:15:48.000Z","acc":"P43403","name":"Tyrosine-protein kinase ZAP-70","length":619,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000013C370","genes":[{"name":{"value":"ZAP70"},"synonyms":[{"value":"SRK"}]}],"alphafold_very_low_content":0.11308562197092084,"disorder_content":0.10016155088852989,"disprot_consensus":{"full":[{"start":258,"end":302,"type":"D"},{"start":484,"end":500,"type":"D"}],"Structural state":[{"start":258,"end":302,"type":"D"},{"start":484,"end":500,"type":"D"}],"Disorder function":[{"start":484,"end":500,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00250","name":"Forkhead domain","start":159,"end":244},{"id":"PF08430","name":"Forkhead N-terminal region","start":17,"end":158},{"id":"PF09354","name":"HNF3 C-terminal domain","start":373,"end":446}],"gene3D":[{"start":157,"end":258,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}]},"uniref50":"UniRef50_P35583","sequence":"MLGAVKMEGHEPSDWSSYYAEPEGYSSVSNMNAGLGMNGMNTYMSMSAAAMGSGSGNMSAGSMNMSSYVGAGMSPSLAGMSPGAGAMAGMGGSAGAAGVAGMGPHLSPSLSPLGGQAAGAMGGLAPYANMNSMSPMYGQAGLSRARDPKTYRRSYTHAKPPYSYISLITMAIQQSPNKMLTLSEIYQWIMDLFPFYRQNQQRWQNSIRHSLSFNDCFLKVPRSPDKPGKGSFWTLHPDSGNMFENGCYLRRQKRFKCEKQLALKEAAGAAGSGKKAAAGAQASQAQLGEAAGPASETPAGTESPHSSASPCQEHKRGGLGELKGTPAAALSPPEPAPSPGQQQQAAAHLLGPPHHPGLPPEAHLKPEHHYAFNHPFSINNLMSSEQQHHHSHHHHQPHKMDLKAYEQVMHYPGYGSPMPGSLAMGPVTNKTGLDASPLAADTSYYQGVYSRPIMNSS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P32182","disprot_id":"DP01124","ncbi_taxon_id":9606,"regions_counter":2,"creator":"mpajkos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":258,"region_id":"DP01124r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the Forkhead Domain of FOXA2 Bound to a Complete DNA Consensus Site. <i> Li J, Dantas Machado AC, Guo M, Sagendorf JM, Zhou Z, Jiang L, Chen X, Wu D, Qu L, Chen Z, Chen L, Rohs R, Chen Y. </i> Biochemistry, 2017","statement":[{"text":"\"the electron density of wing 2 (residues 240–258) in the FOXA2-DBD/DBE2 structure could not be observed. This result suggested that wing 2 was flexible and disordered in the crystal.\"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":240,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5X07"}],"reference_id":"28644006","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":258,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of the Forkhead Domain of FOXA2 Bound to a Complete DNA Consensus Site. <i> Li J, Dantas Machado AC, Guo M, Sagendorf JM, Zhou Z, Jiang L, Chen X, Wu D, Qu L, Chen Z, Chen L, Rohs R, Chen Y. </i> Biochemistry, 2017","statement":[{"text":"\"To test whether wing 2 contributes to FOXA2-DBD/DNA binding, we constructed a truncated fragment of FOXA2 without wing 2 and measured the DNA binding ability using ITC. The binding affinity of FOXA2 was reduced by ∼30-fold when the C-terminal wing 2 region was removed. These results suggested that wing 2 of FOXA2 was important for optimal DNA binding.\"","type":"Results"}],"term_id":"GO:0003676","curator_id":"mpajkos","start":240,"term_ontology":"GO","curator_name":"Mátyás Pajkos","reference_id":"28644006","version":3,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01124r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q9Y261","date":"2018-06-20T13:32:42.000Z","acc":"Q9Y261","name":"Hepatocyte nuclear factor 3-beta","length":457,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012CA87","genes":[{"name":{"value":"FOXA2"},"synonyms":[{"value":"HNF3B"},{"value":"TCF3B"}]}],"alphafold_very_low_content":0.5645514223194749,"disorder_content":0.04157549234135667,"disprot_consensus":{"full":[{"start":240,"end":258,"type":"D"}],"Structural state":[{"start":240,"end":258,"type":"D"}],"Molecular function":[{"start":240,"end":258,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00536","name":"SAM domain (Sterile alpha motif)","start":473,"end":534},{"id":"PF00536","name":"SAM domain (Sterile alpha motif)","start":549,"end":604},{"id":"PF07653","name":"Variant SH3 domain","start":286,"end":340},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":9,"end":110},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":172,"end":250},{"id":"PF13637","name":"Ankyrin repeats (many copies)","start":119,"end":168},{"id":"PF16600","name":"Caskin1 CASK-interaction domain","start":373,"end":421},{"id":"PF16632","name":"C-terminal region of Caskin","start":1368,"end":1430},{"id":"PF16907","name":"Proline rich region of Caskin proteins","start":877,"end":962}],"gene3D":[{"start":540,"end":615,"id":"1.10.150.50","name":"Transcription Factor, Ets-1"},{"start":2,"end":182,"id":"1.25.40.20","name":"Ankyrin repeat-containing domain"},{"start":468,"end":539,"id":"1.10.150.50","name":"Transcription Factor, Ets-1"},{"start":283,"end":348,"id":"2.30.30.40","name":"SH3 Domains"}]},"uniref50":"UniRef50_Q8VHK2","sequence":"MGKEQELVQAVKAEDVGTAQRLLQRPRPGKAKLLGSTKKINVNFQDPDGFSALHHAALNGNTELISLLLEAQAAVDIKDNKGMRPLHYAAWQGRKEPMKLVLKAGSAVNVPSDEGHIPLHLAAQHGHYDVSEMLLQHQSNPCIVDNSGKTPLDLACEFGRVGVVQLLLSSNMCAALLEPRPGDTTDPNGTSPLHLAAKNGHIDIIRLLLQAGIDINRQTKSGTALHEAALCGKTEVVRLLLDSGINAQVRNTYSQTALDIVHQFTTSQASKEIKQLLREASAALQVRATKDYCNNYDLTSLNVKAGDIITVLEQHPDGRWKGCIHDNRTGNDRVGYFPSSLGEAIVKRAGSRTGSEPSPPQGGGSLGPSAPPEEIWVLRKPFAGGDRSGSLSNVAGGRSTGGHALHAGAEGVKLLATVLSQKSVSESSPGDSPVKPPEGSSGAARSQPPAAHAGQVYGEQPPKKLESSSASEGKSAEAVSQWLATFQLQLYAPNFTSAGYDLPTISRMTPEDLTAIGVTKPGHRKKITAEISGLNIPDCLPEHKPANLAVWLSMIGLAQYYKVLVDNGYENIDFITDITWEDLQEIGITKLGHQKKLMLAVRKLAELQKAEYSKYEGGPLRRKAPQSLEMMAIESPPPSEPAAAECQSPKMTTFQDSELSGELQAALSGPAEAGAAAAEKSSNHLPATPRTTSRQESSLSGRARHMSSSQELLGDGPQGPGSPMSRSQEYLLDEGPAPGTPPKEVRSSRHGHSVKRASVPPVPGKPRQVLPSGVSHFTPPQTPTKAQPGSPQALGGPHGPATAKVKPTPQLLPPTDRPMSPRSLPQSPTHRGFAYVLPQPVEGEAGPPAPGPVPPPVPAAVPTLCLPPEADVEPRRPKKRAHSLNRYAASDSEPERDELLVPAAAGPYATVQRRVGRSHSVRAPAGTDKNVNRSQSFAVRPRKKGPPPPPPKRSSSAMASANLADEPSPDVETEDGRLGVRAQRRRASDLAGSVDTGSAGSVKSIAAMLELSSIGGGGRAIRRPPEGHPTPRPASPDPGRVATVLASVKHKEAIGPDGEVVNRRRTLSGPVTGLLATARRGPGEPAEQSHFMEDGTARQRLRGPAKGEAGVEGPPLARVEASATLKRRIRAKQSQQENVKFILTESDTVKRRPKAKEPDIGPEPPPPLSVYQNGTATIRRRPASEQAGPPELPPPPPPAEPPPTDLMPLPPLPLPDGSARKPVKPPVSPKPILAQPVSKIQGSPTPASKKVPLPGPGSPEVKRAHGTPPPVSPKPPPPPTAPKPAKALAGLQSSSATPSPVPSPARQPPAALIKPASSPPSQSASPAKPPSPGAPALQVPTKPPRAAASVVSGPPVASDCASPGDSARQKLEETSACLAAALQAVEEKIRQEDGQGPRPSSIEEKSTGSILEDIGSMFDDLADQLDAMLE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_Q8VHK2","disprot_id":"DP01127","ncbi_taxon_id":10116,"regions_counter":5,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1430,"region_id":"DP01127r001","released":"2022_03","ec_id":"ECO:0006198","reference_html":"High levels of structural disorder in scaffold proteins as exemplified by a novel neuronal protein, CASK-interactive protein1. <i> Balázs A, Csizmok V, Buday L, Rakács M, Kiss R, Bokor M, Udupa R, Tompa K, Tompa P. </i> FEBS J, 2009","statement":[{"text":"The one-dimensional 1H-NMR spectra of the PRD-His fragments (prolin rich domains) also underscores a largely disordered conformational state. Chemical shifts show a poor dispersion, i.e. amide proton signals are clustered within a half-p.p.m. range centred at 8 p.p.m., whereas the methyl group protons are clustered at around 1 p.p.m. Such a limited dispersion and signal overlap in 1H chemical shifts are typical of IDPs.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":603,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"19523119","version":2,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":1430,"term_name":"protein binding","start":603,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","statement":[{"text":"The molecular mechanism of the function of Caskins is not known at present. As a result of their large size, the capacity to bind multiple partners and the lack of catalytic domains, they probably fall into the class of scaffold proteins, which bind components of a signal transduction pathway simultaneously and ensure the specificity and efficiency of signal propagation. As the long regions of these proteins often lack any sequence similarity to other proteins and appear to lack folded structural domains, we anticipated that structural disorder may be a general feature of scaffold proteins. The first and second proline-rich regions of Caskin1 (PRD1-GST and PRD2-GST were able to interact with the GFP-Abi2 protein.","type":"Introduction"}],"curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"19523119","version":3,"reference_html":"High levels of structural disorder in scaffold proteins as exemplified by a novel neuronal protein, CASK-interactive protein1. <i> Balázs A, Csizmok V, Buday L, Rakács M, Kiss R, Bokor M, Udupa R, Tompa K, Tompa P. </i> FEBS J, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006198","region_id":"DP01127r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1430,"region_id":"DP01127r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"High levels of structural disorder in scaffold proteins as exemplified by a novel neuronal protein, CASK-interactive protein1. <i> Balázs A, Csizmok V, Buday L, Rakács M, Kiss R, Bokor M, Udupa R, Tompa K, Tompa P. </i> FEBS J, 2009","statement":[{"text":"The CD spectrum of PRD-His shows a minimum at 202 nm, which is characteristic of a protein in a largely disordered conformation. The CD spectra of the separate PRDs also show characteristic minima around 200 nm, which underscores the unstructured nature of these regions.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":603,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"19523119","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1430,"region_id":"DP01127r004","released":"2022_03","ec_id":"ECO:0007691","reference_html":"High levels of structural disorder in scaffold proteins as exemplified by a novel neuronal protein, CASK-interactive protein1. <i> Balázs A, Csizmok V, Buday L, Rakács M, Kiss R, Bokor M, Udupa R, Tompa K, Tompa P. </i> FEBS J, 2009","statement":[{"text":"PRD-His shows a greater sensitivity to proteolysis with a protease of wide substrate specificity, subtilisin, than does the globular control protein BSA; this provides an indication of its disordered conformation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":603,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"19523119","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1430,"region_id":"DP01127r005","released":"2022_03","ec_id":"ECO:0007680","reference_html":"High levels of structural disorder in scaffold proteins as exemplified by a novel neuronal protein, CASK-interactive protein1. <i> Balázs A, Csizmok V, Buday L, Rakács M, Kiss R, Bokor M, Udupa R, Tompa K, Tompa P. </i> FEBS J, 2009","statement":[{"text":"Gel filtration data also verify the disordered nature of the proline-rich region, as the apparent molecular mass (mapp) of PRD-His (334.5 kDa) is 3.9 times higher than the real value (85.9 kDa).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":603,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"19523119","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q8VHK2","date":"2018-06-21T10:12:07.000Z","acc":"Q8VHK2","name":"Caskin-1","length":1430,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI00000E71EE","genes":[{"name":{"value":"Caskin1"}}],"alphafold_very_low_content":0.6195804195804195,"disorder_content":0.579020979020979,"disprot_consensus":{"full":[{"start":603,"end":1430,"type":"D"}],"Structural state":[{"start":603,"end":1430,"type":"D"}],"Molecular function":[{"start":603,"end":1430,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02234","name":"Cyclin-dependent kinase inhibitor","start":31,"end":79}],"gene3D":[{"start":23,"end":106,"id":"4.10.365.10","name":"p27"}]},"uniref50":"UniRef50_P46527","sequence":"MSNVRVSNGSPSLERMDARQAEHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQESQDGSGSRPAAPLIGAPANSEDTHLVDPKTDPSDSQTGLAEQCAGIRKRPATD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O43806","disprot_id":"DP01128","ncbi_taxon_id":9606,"regions_counter":9,"creator":"tlazar","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":93,"region_id":"DP01128r001","released":"2025_12","ec_id":"ECO:0006165","reference_html":"Disordered p27Kip1 exhibits intrinsic structure resembling the Cdk2/cyclin A-bound conformation. <i> Sivakolundu SG, Bashford D, Kriwacki RW. </i> J Mol Biol, 2005","statement":[{"text":"Before binding, p27 is at least partially disordered and folds upon binding its Cdk/cyclin targets.","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":25,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2025-12-03T20:38:41.490Z","reference_source":"pmid","term_name":"disorder","reference_id":"16214166","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":93,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Disordered p27Kip1 exhibits intrinsic structure resembling the Cdk2/cyclin A-bound conformation. <i> Sivakolundu SG, Bashford D, Kriwacki RW. </i> J Mol Biol, 2005","statement":[{"text":"Before binding, p27 is at least partially disordered and folds upon binding its Cdk/cyclin targets.","type":"Abstract"}],"term_id":"GO:0005515","curator_id":"tlazar","start":25,"term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"16214166","version":3,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01128r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":93,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Disordered p27Kip1 exhibits intrinsic structure resembling the Cdk2/cyclin A-bound conformation. <i> Sivakolundu SG, Bashford D, Kriwacki RW. </i> J Mol Biol, 2005","statement":[{"text":"Before binding, p27 is at least partially disordered and folds upon binding its Cdk/cyclin targets.","type":"Abstract"}],"term_id":"IDPO:0000011","curator_id":"tlazar","start":25,"term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"16214166","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01128r003","ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:17:54.905Z"}},{"start":22,"end":97,"reference_id":"11749217","reference_source":"pmid","reference_html":"Effects of macromolecular crowding on the intrinsically disordered proteins c-Fos and p27(Kip1). <i> Flaugh SL, Lumb KJ. </i> Biomacromolecules, 2001","date":"2023-07-17T16:54:45.053Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01128r004","statement":[{"text":"In the presence of macromolecular crowding agents, neither the intrinsically disordered C-terminal activation domain of c-Fos nor the kinase-inhibition domain of p27Kip1 undergoes any significant conformational change that is detected by changes in either circular dichroism or fluorescence spectra.","type":"Abstract"},{"text":"While intrinsically disordered at physiological temperatures, marginally stable helix is present in p27ID at 5 °C (Figure 2A).8 Addition of TFE to p27ID induced a marked change in the CD spectrum indicative of a large increase in helix content (Figure 2A). However addition of several crowding agents did not induce any significant change in the CD spectrum of p27ID above 212 nm that reflects formation of helical or strand secondary structure (Figure 2B).","type":"Results"},{"text":"A decrease in the intensity of the CD signal of p27ID at 204 nm was observed in the presence of the 37.5 and 77 kDa dextrans, and the fluorescence emission intensity of p27ID at 350 nm was reduced in the presence of 77 kDa dextran and Ficoll 70 (as observed for FosAD).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:22:38.574Z"}},{"start":22,"end":97,"reference_id":"11749217","reference_source":"pmid","reference_html":"Effects of macromolecular crowding on the intrinsically disordered proteins c-Fos and p27(Kip1). <i> Flaugh SL, Lumb KJ. </i> Biomacromolecules, 2001","date":"2023-07-17T16:56:14.658Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006336","ec_ontology":"ECO","ec_name":"intrinsic fluorescence-based protein conformation evidence","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01128r005","statement":[{"text":"In the presence of macromolecular crowding agents, neither the intrinsically disordered C-terminal activation domain of c-Fos nor the kinase-inhibition domain of p27Kip1 undergoes any significant conformational change that is detected by changes in either circular dichroism or fluorescence spectra.","type":"Abstract"},{"text":"Crowding agents did not affect the p27ID fluorescence emission maximum of 350 nm (Figure 2C) or did not affect significantly the fluorescence spectrum of ANS in the presence of p27ID (data not shown).","type":"Results"},{"text":"A decrease in the intensity of the CD signal of p27ID at 204 nm was observed in the presence of the 37.5 and 77 kDa dextrans, and the fluorescence emission intensity of p27ID at 350 nm was reduced in the presence of 77 kDa dextran and Ficoll 70 (as observed for FosAD).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:22:28.650Z"}},{"start":1,"end":158,"reference_id":"11790096","reference_source":"pmid","reference_html":"Functional consequences of preorganized helical structure in the intrinsically disordered cell-cycle inhibitor p27(Kip1). <i> Bienkiewicz EA, Adkins JN, Lumb KJ. </i> Biochemistry, 2002","date":"2023-07-17T17:09:30.085Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01128r006","statement":[{"text":"The CD spectrum of full-length human p27 is characteristic of an unfolded protein (Figure 3). The minimum at 200 nm is indicative of an unfolded conformation, and the weak negative shoulder at 222 nm suggests the absence of significant amounts of helix or β-strand. The helix content is estimated at 2 or 6% from [θ]222 or CDPro, respectively. The results indicate that full-length p27, while active as a Cdk inhibitor, is largely unfolded.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:15:28.695Z"}},{"start":22,"end":97,"reference_id":"11790096","reference_source":"pmid","reference_html":"Functional consequences of preorganized helical structure in the intrinsically disordered cell-cycle inhibitor p27(Kip1). <i> Bienkiewicz EA, Adkins JN, Lumb KJ. </i> Biochemistry, 2002","date":"2023-07-17T17:08:03.843Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01128r007","statement":[{"text":"We report here a study of the functional consequences of conformational preferences in the intrinsically disordered human p27 Cdk-inhibition domain. Rather than existing as a random coil, the p27 Cdk-inhibition domain exhibits a propensity to form preexisting helical structure that corresponds to the α-helix, but not the 310 helix, that forms upon binding cyclin A-Cdk2.","type":"Introduction"},{"text":"The CD spectra of p27ID in kinase-assay buffer at 30 and 60 °C are also characteristic of an unfolded protein (Figure 5). The minimum at 204 nm is indicative of an unfolded conformation, and the weak negative shoulder at 222 nm suggests the absence of significant amounts of helix or β-strand.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:13:18.389Z"}},{"start":22,"end":97,"reference_id":"11790096","reference_source":"pmid","reference_html":"Functional consequences of preorganized helical structure in the intrinsically disordered cell-cycle inhibitor p27(Kip1). <i> Bienkiewicz EA, Adkins JN, Lumb KJ. </i> Biochemistry, 2002","date":"2023-07-17T17:11:28.838Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01128r008","statement":[{"text":"The NMR properties of p27ID at 30 °C are characteristic of an unfolded protein. 1H chemical-shift ranges were obtained from DQF COSY (pH 4.4) or TOCSY−HSQC (pH 7.0) spectra using gradients for solvent suppression. The Hα and HN chemical shifts at pH 4.4 span 3.9−4.6 and 7.8−8.6 ppm, respectively, and at pH 7.0 span 4.05−4.59 and 7.77−8.58 ppm, respectively (data not shown). These chemical-shift ranges are typical of those observed in unfolded proteins ( 28). The amide 1H−15N NOE is negative (approximately −1 to −3.9) for each of 64 resolved mainchain amide cross-peaks at pH 4.4 (from an expected total of 70; data not shown), indicating that the p27ID main chain is highly flexible with motion on a time scale characteristic of unfolded proteins ( 29, 30).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:12:37.220Z"}},{"start":22,"end":97,"reference_id":"11790096","reference_source":"pmid","reference_html":"Functional consequences of preorganized helical structure in the intrinsically disordered cell-cycle inhibitor p27(Kip1). <i> Bienkiewicz EA, Adkins JN, Lumb KJ. </i> Biochemistry, 2002","date":"2023-07-17T17:17:57.176Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007123","ec_ontology":"ECO","ec_name":"enzyme inhibition evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P20248","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P24941","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01128r009","statement":[{"text":"p27ID binds cyclin A-Cdk2 with a Kd of 8 ± 2 nM at 30 °C (Figure 9).","type":"Results"},{"text":"Figure 9 Kd determinations from cyclin A-Cdk2 inhibition assays (50 nM cyclin A-Cdk2, 25 mM HEPES, 50 mM NaCl, and 5 mM MgCl2, pH 7.5, 30 °C).","type":"Figure"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:15:55.950Z"}}],"released":"2018_11","uniref100":"UniRef100_O43806","date":"2018-06-21T11:42:30.000Z","acc":"O43806","name":"p27 kip1 protein","length":158,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI000006FD53","genes":[{"name":{"value":"p27 kip1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAA59284.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA59284.1"}}]}}],"alphafold_very_low_content":0.3291139240506329,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":24,"type":"D"},{"start":25,"end":93,"type":"T"},{"start":94,"end":158,"type":"D"}],"Structural state":[{"start":1,"end":158,"type":"D"}],"Molecular function":[{"start":22,"end":97,"type":"F"}],"Structural transition":[{"start":25,"end":93,"type":"T"}]}},{"acc":"P12296","sequence":"MATTMEQEICAHSMTFEECPKCSALQYRNGFYLLKYDEEWYPEELLTDGEDDVFDPDLDMEVVFETQGNSTSSDKNNSSSEGNEGVIINNFYSNQYQNSIDLSANATGSDPPKTYGQFSNLLSGAVNAFSNMLPLLADQNTEEMENLSDRVSQDTAGNTVTNTQSTVGRLVGYGTVHDGEHPASCADTASEKILAVERYYTFKVNDWTSTQKPFEYIRIPLPHVLSGEDGGVFGATLRRHYLVKTGWRVQVQCNASQFHAGSLLVFMAPEYPTLDVFAMDNRWSKDNLPNGTRTQTNRKGPFAMDHQNFWQWTLYPHQFLNLRTNTTVDLEVPYVNIAPTSSWTQHASWTLVIAVVAPLTYSTGASTSLDITASIQPVRPVFNGLRHEVLSRQSPIPVTIREHAGTWYSTLPDSTVPIYGKTPVAPANYMVGEYKDFLEIAQIPTFIGNKVPNAVPYIEASNTAVKTQPLAVYQVTLSCSCLANTFLAALSRNFAQYRGSLVYTFVFTGTAMMKGKFLIAYTPPGAGKPTSRDQAMQATYAIWDLGLNSSYSFTVPFISPTHFRMVGTDQANITNVDGWVTVWQLTPLTYPPGCPTSAKILTMVSAGKDFSLKMPISPAPWSPQGVENAEKGVTENTDATADFVAQPVYLPENQTKVAFFYDRSSPIGAFAVKSGSLESGFAPFSNKACPNSVILTPGPQFDPAYDQLRPQRLTEIWGNGNEETSEVFPLKTKQDYSFCLFSPFVYYKCDLEVTLSPHTSGAHGLLVRWCPTGTPTKPTTQVLHEVSSLSEGRTPQVYSAGPGTSNQISFVVPYNSPLSVLPAVWYNGHKRFDNTGDLGIAPNSDFGTLFFAGTKPDIKFTVYLRYKNMRVFCPRPTVFFPWPTSGDKIDMTPRAGVLMLESPNPLDVSKTYPTLHILLQFNHRGLEARIFRHGQLWAETHAEVVLRSKTKQISFLSNGSYPSMDATTPLNPWKSTYQAVLRAEPHRVTMDVYHKRIRPFRLPLVQKEWRTCEENVFGLYHVFETHYAGYFSDLLIHDVETNPGPFTFKPRQRPVFQTQGAAVSSMAQTLLPNDLASKAMGSAFTALLDANEDAQKAMKIIKTLSSLSDAWENVKGTLNNPEFWKQLLSRCVQLIAGMTIAVMHPDPLTLLCLGVLTAAEITSQTSLCEEIAAKFKTIFTTPPPRFPVISLFQQQSPLKQVNDVFSLAKNLDWAVKTVEKVVDWFGTWVAQEEREQTLDQLLQRFPEHAKRISDLRNGMAAYVECKESFDFFEKLYNQAVKEKRTGIAAVCEKFRQKHDHATARCEPVVIVLRGDAGQGKSLSSQIIAQAVSKTIFGRQSVYSLPPDSDFFDGYENQFAAIMDDLGQNPDGSDFTTFCQMVSTTNLLPNMASLERKGTPFTSQLVVATTNLPEFRPVTIAHYPAVERRITFDYSVSAGPVCSKTEAGCKVLDVERAFRPTGDAPLPCFQNNCLFLEKAGLQFRDNRSKEILSLVDVIERAVTRIERKKKVLTAVQTLVAQGPVDEVSFYSVVQQLKARQEATDEQLEELQEAFARVQERSSVFSDWMKISAMLCAATLALTQVVKMAKAVKQMVRPDLVRVQLDEQEQGPYNETTRIKPKTLQLLDVQGPNPTMDFEKFVAKFVTAPIGFVYPTGVSTQTCLLVKGRTLAVNRHMAESDWTSIVVRGVSHTRSSVKIIAIAKAGKETDVSFIRLSSGPLFRDNTSKFVKASDVLPHSSSPLIGIMNVDIPMMYTGTFLKAGVSVPVETGQTFNHCIHYKANTRKGWCGSAILADLGGSKKILGFHSAGSMGVAAASIISQEMIDAVVQAFEPQGALERLPDGPRIHVPRKTALRPTVARQVFQPAFAPAVLSKFDPRTDADVDEVAFSKHTSNQETLPPVFRMVAREYANRVFALLGRDNGRLSVKQALDGLEGMDPMDKNTSPGLPYTTLGMRRTDVVDWETATLIPFAAERLEKMNNKDFSDIVYQTFLKDELRPIEKVQAAKTRIVDVPPFEHCILGRQLLGKFASKFQTQPGLELGSAIGCDPDVHWTAFGVAMQGFERVYDVDYSNFDSTHSVAVFRLLAEEFFSEENGFDPLVKDYLESLAISKHAYEEKRYLITGGLPSGCAATSMLNTIMNNIIIRAGLYLTYKNFEFDDVKVLSYGDDLLVATNYQLNFDRVRTSLAKTGYKITPANKTSTFPLESTLEDVVFLKRKFKKEGPLYRPVMNREALEAMLSYYRPGTLSEKLTSITMLAVHSGKQEYDRLFAPFREVGVIVPTFESVEYRWRSLFW","creator":"tlazar","dataset":["Viral proteins","RNA-binding proteins"],"date":"2018-06-21T11:58:06.000Z","disprot_id":"DP01129","features":{"pfam":[{"id":"PF00073","name":"picornavirus capsid protein","start":163,"end":361},{"id":"PF00073","name":"picornavirus capsid protein","start":424,"end":583},{"id":"PF00548","name":"3C cysteine protease (picornain 3C)","start":1659,"end":1808},{"id":"PF00680","name":"Viral RNA-dependent RNA polymerase","start":1855,"end":2273},{"id":"PF00910","name":"RNA helicase","start":1310,"end":1411},{"id":"PF11475","name":"Virion protein N terminal domain","start":1,"end":32},{"id":"PF22663","name":"Picornavirus coat protein","start":628,"end":876}],"gene3D":[{"start":394,"end":624,"id":"2.60.120.20","name":"2.60.120.20","_id":"685af523b4ac24d5329d8c8d"},{"start":68,"end":137,"id":"4.10.90.10","name":"Capsid protein VP4 superfamily, Picornavirus","_id":"685af523b4ac24d5329d8c8e"},{"start":625,"end":901,"id":"2.60.120.20","name":"2.60.120.20","_id":"685af523b4ac24d5329d8c8f"},{"start":138,"end":393,"id":"2.60.120.20","name":"2.60.120.20","_id":"685af523b4ac24d5329d8c90"},{"start":2229,"end":2293,"id":"1.20.960.20","name":"1.20.960.20","_id":"685af523b4ac24d5329d8c91"},{"start":1726,"end":1831,"id":"2.40.10.10","name":"Trypsin-like serine proteases","_id":"685af523b4ac24d5329d8c92"},{"start":2104,"end":2228,"id":"3.30.70.270","name":"3.30.70.270","_id":"685af523b4ac24d5329d8c93"},{"start":2036,"end":2091,"id":"3.30.70.270","name":"3.30.70.270","_id":"685af523b4ac24d5329d8c94"}]},"genes":[],"length":2293,"name":"Genome polyprotein","ncbi_taxon_id":12107,"organism":"Mengo encephalomyocarditis virus","regions_counter":14,"released":"2018_11","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Picornavirales","Picornaviridae","Cardiovirus"],"UniParc":"UPI0000661828","uniref100":"UniRef100_P12296","uniref50":"UniRef50_P12296","uniref90":"UniRef90_P12296","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2MMH","_id":"685af523b4ac24d5329d8c9d"},{"db":"PDB","id":"2MMI","_id":"685af523b4ac24d5329d8c9e"},{"db":"PDB","id":"2MML","_id":"685af523b4ac24d5329d8c9f"},{"db":"PDB","id":"2MMK","_id":"685af523b4ac24d5329d8ca0"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0001238","ec_name":"nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":19,"interaction_partner":[],"reference_html":"Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase. <i> Bacot-Davis VR, Ciomperlik JJ, Basta HA, Cornilescu CC, Palmenberg AC. </i> Proc Natl Acad Sci U S A, 2014","reference_id":"25331866","region_id":"DP01129r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The majority of LM0P was random coil, interspersed with four short helical segments (Figs. 1 and 2 A and B). As defined by TALOS+ algorithms (17), the α1 and α2 segments (aa 23–26 and 29–31) spanned the COOH-half of the zinc finger. The α3 and α4 motifs, in the hinge region (aa 45–49) and near the COOH tail (aa 63–66), were less well defined.","_id":"685af523b4ac24d5329d8ca1"},{"type":"Curator statement","text":"The sequence of LM is 4 aa longer at the N-terminal.","_id":"685af523b4ac24d5329d8ca2"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-04T09:03:57.375Z","_id":"685af523b4ac24d5329d8ca3"},"version":1,"_id":"685af523b4ac24d5329d8c9c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2MMH","_id":"685af523b4ac24d5329d8ca5"},{"db":"PDB","id":"2MMI","_id":"685af523b4ac24d5329d8ca6"},{"db":"PDB","id":"2MML","_id":"685af523b4ac24d5329d8ca7"},{"db":"PDB","id":"2MMK","_id":"685af523b4ac24d5329d8ca8"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0001238","ec_name":"nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":27,"end":41,"interaction_partner":[],"reference_html":"Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase. <i> Bacot-Davis VR, Ciomperlik JJ, Basta HA, Cornilescu CC, Palmenberg AC. </i> Proc Natl Acad Sci U S A, 2014","reference_id":"25331866","region_id":"DP01129r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The majority of LM0P was random coil, interspersed with four short helical segments (Figs. 1 and 2 A and B). As defined by TALOS+ algorithms (17), the α1 and α2 segments (aa 23–26 and 29–31) spanned the COOH-half of the zinc finger. The α3 and α4 motifs, in the hinge region (aa 45–49) and near the COOH tail (aa 63–66), were less well defined.","_id":"685af523b4ac24d5329d8ca9"},{"type":"Curator statement","text":"The sequence of LM is 4 aa longer at the N-terminal.","_id":"685af523b4ac24d5329d8caa"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-04T09:03:56.029Z","_id":"685af523b4ac24d5329d8cab"},"version":1,"_id":"685af523b4ac24d5329d8ca4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2MMH","_id":"685af523b4ac24d5329d8cad"},{"db":"PDB","id":"2MMI","_id":"685af523b4ac24d5329d8cae"},{"db":"PDB","id":"2MML","_id":"685af523b4ac24d5329d8caf"},{"db":"PDB","id":"2MMK","_id":"685af523b4ac24d5329d8cb0"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0001238","ec_name":"nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":45,"end":59,"interaction_partner":[],"reference_html":"Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase. <i> Bacot-Davis VR, Ciomperlik JJ, Basta HA, Cornilescu CC, Palmenberg AC. </i> Proc Natl Acad Sci U S A, 2014","reference_id":"25331866","region_id":"DP01129r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The majority of LM0P was random coil, interspersed with four short helical segments (Figs. 1 and 2 A and B). As defined by TALOS+ algorithms (17), the α1 and α2 segments (aa 23–26 and 29–31) spanned the COOH-half of the zinc finger. The α3 and α4 motifs, in the hinge region (aa 45–49) and near the COOH tail (aa 63–66), were less well defined.","_id":"685af523b4ac24d5329d8cb1"},{"type":"Curator statement","text":"The sequence of LM is 4 aa longer at the N-terminal.","_id":"685af523b4ac24d5329d8cb2"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-04T09:03:52.454Z","_id":"685af523b4ac24d5329d8cb3"},"version":1,"_id":"685af523b4ac24d5329d8cac","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":47,"end":47,"statements":[{"type":"Results","text":"Accordingly, we carried out, matched NMR studies on the unphosphorylated (LM0P), singly phosphorylated (LM1P, T47), and doubly phosphorylated (LM2P, Y41/T47) variants of recombinant LM. ","_id":"685af523b4ac24d5329d8cb6"}],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d8cb5"}],"cross_refs":[{"db":"PDB","id":"2MMH","_id":"685af523b4ac24d5329d8cb7"},{"db":"PDB","id":"2MMI","_id":"685af523b4ac24d5329d8cb8"},{"db":"PDB","id":"2MML","_id":"685af523b4ac24d5329d8cb9"},{"db":"PDB","id":"2MMK","_id":"685af523b4ac24d5329d8cba"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0001238","ec_name":"nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":19,"interaction_partner":[],"reference_html":"Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase. <i> Bacot-Davis VR, Ciomperlik JJ, Basta HA, Cornilescu CC, Palmenberg AC. </i> Proc Natl Acad Sci U S A, 2014","reference_id":"25331866","region_id":"DP01129r006","released":"2022_03","sample":[],"sequence_construct":"MATTMEQEICAHSMTFEECPKCSALQYRNGFYLLKYDEEWYPEELLTDGEDDVFDPDLDMEVVFETQ","statement":[{"type":"Results","text":"Surprisingly, when one or two phosphates were added, the overall proteins still configured largely as random coil (Fig. 1 and Fig. S6 B–D).","_id":"685af523b4ac24d5329d8cbb"},{"type":"Figure","text":"The remainder of each protein is random coil.","_id":"685af523b4ac24d5329d8cbc"},{"type":"Curator statement","text":"The figure 1 shows the secondary when the protein is without PTMs, phosphorilated or binding protein Ran. The secondary structure along the sequence is shown and the rest of the protein is random coil.","_id":"685af523b4ac24d5329d8cbd"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000030","term_name":"entropic chain","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-04T09:05:38.018Z","_id":"685af523b4ac24d5329d8cbe"},"version":1,"_id":"685af523b4ac24d5329d8cb4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":47,"end":47,"statements":[{"type":"Results","text":"Accordingly, we carried out, matched NMR studies on the unphosphorylated (LM0P), singly phosphorylated (LM1P, T47), and doubly phosphorylated (LM2P, Y41/T47) variants of recombinant LM. ","_id":"685af523b4ac24d5329d8cc1"}],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d8cc0"}],"cross_refs":[{"db":"PDB","id":"2MMH","_id":"685af523b4ac24d5329d8cc2"},{"db":"PDB","id":"2MMI","_id":"685af523b4ac24d5329d8cc3"},{"db":"PDB","id":"2MML","_id":"685af523b4ac24d5329d8cc4"},{"db":"PDB","id":"2MMK","_id":"685af523b4ac24d5329d8cc5"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0001238","ec_name":"nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":37,"end":67,"interaction_partner":[],"reference_html":"Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase. <i> Bacot-Davis VR, Ciomperlik JJ, Basta HA, Cornilescu CC, Palmenberg AC. </i> Proc Natl Acad Sci U S A, 2014","reference_id":"25331866","region_id":"DP01129r007","released":"2022_03","sample":[],"sequence_construct":"MATTMEQEICAHSMTFEECPKCSALQYRNGFYLLKYDEEWYPEELLTDGEDDVFDPDLDMEVVFETQ","statement":[{"type":"Results","text":"Surprisingly, when one or two phosphates were added, the overall proteins still configured largely as random coil (Fig. 1 and Fig. S6 B–D).","_id":"685af523b4ac24d5329d8cc6"},{"type":"Figure","text":"The remainder of each protein is random coil.","_id":"685af523b4ac24d5329d8cc7"},{"type":"Curator statement","text":"The figure 1 shows the secondary when the protein is without PTMs, phosphorilated or binding protein Ran. The secondary structure along the sequence is shown and the rest of the protein is random coil.","_id":"685af523b4ac24d5329d8cc8"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-04T09:03:51.143Z","_id":"685af523b4ac24d5329d8cc9"},"version":1,"_id":"685af523b4ac24d5329d8cbf","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":47,"end":47,"statements":[{"type":"Results","text":"Accordingly, we carried out, matched NMR studies on the unphosphorylated (LM0P), singly phosphorylated (LM1P, T47), and doubly phosphorylated (LM2P, Y41/T47) variants of recombinant LM. ","_id":"685af523b4ac24d5329d8ccc"}],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d8ccb"},{"start":41,"end":41,"statements":[{"type":"Results","text":"Accordingly, we carried out, matched NMR studies on the unphosphorylated (LM0P), singly phosphorylated (LM1P, T47), and doubly phosphorylated (LM2P, Y41/T47) variants of recombinant LM. ","_id":"685af523b4ac24d5329d8cce"}],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d8ccd"}],"cross_refs":[{"db":"PDB","id":"2MMH","_id":"685af523b4ac24d5329d8ccf"},{"db":"PDB","id":"2MMI","_id":"685af523b4ac24d5329d8cd0"},{"db":"PDB","id":"2MML","_id":"685af523b4ac24d5329d8cd1"},{"db":"PDB","id":"2MMK","_id":"685af523b4ac24d5329d8cd2"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0001238","ec_name":"nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":15,"interaction_partner":[],"reference_html":"Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase. <i> Bacot-Davis VR, Ciomperlik JJ, Basta HA, Cornilescu CC, Palmenberg AC. </i> Proc Natl Acad Sci U S A, 2014","reference_id":"25331866","region_id":"DP01129r008","released":"2022_03","sample":[],"sequence_construct":"MATTMEQEICAHSMTFEECPKCSALQYRNGFYLLKYDEEWYPEELLTDGEDDVFDPDLDMEVVFETQ","statement":[{"type":"Results","text":"Surprisingly, when one or two phosphates were added, the overall proteins still configured largely as random coil (Fig. 1 and Fig. S6 B–D).","_id":"685af523b4ac24d5329d8cd3"},{"type":"Figure","text":"The remainder of each protein is random coil.","_id":"685af523b4ac24d5329d8cd4"},{"type":"Curator statement","text":"The figure 1 shows the secondary when the protein is without PTMs, phosphorilated or binding protein Ran. The secondary structure along the sequence is shown and the rest of the protein is random coil.","_id":"685af523b4ac24d5329d8cd5"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-04T09:03:50.249Z","_id":"685af523b4ac24d5329d8cd6"},"version":1,"_id":"685af523b4ac24d5329d8cca","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":47,"end":47,"statements":[{"type":"Results","text":"Accordingly, we carried out, matched NMR studies on the unphosphorylated (LM0P), singly phosphorylated (LM1P, T47), and doubly phosphorylated (LM2P, Y41/T47) variants of recombinant LM. ","_id":"685af523b4ac24d5329d8cd9"}],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d8cd8"},{"start":41,"end":41,"statements":[{"type":"Results","text":"Accordingly, we carried out, matched NMR studies on the unphosphorylated (LM0P), singly phosphorylated (LM1P, T47), and doubly phosphorylated (LM2P, Y41/T47) variants of recombinant LM. ","_id":"685af523b4ac24d5329d8cdb"}],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d8cda"}],"cross_refs":[{"db":"PDB","id":"2MMH","_id":"685af523b4ac24d5329d8cdc"},{"db":"PDB","id":"2MMI","_id":"685af523b4ac24d5329d8cdd"},{"db":"PDB","id":"2MML","_id":"685af523b4ac24d5329d8cde"},{"db":"PDB","id":"2MMK","_id":"685af523b4ac24d5329d8cdf"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0001238","ec_name":"nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":22,"end":43,"interaction_partner":[],"reference_html":"Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase. <i> Bacot-Davis VR, Ciomperlik JJ, Basta HA, Cornilescu CC, Palmenberg AC. </i> Proc Natl Acad Sci U S A, 2014","reference_id":"25331866","region_id":"DP01129r009","released":"2022_03","sample":[],"sequence_construct":"MATTMEQEICAHSMTFEECPKCSALQYRNGFYLLKYDEEWYPEELLTDGEDDVFDPDLDMEVVFETQ","statement":[{"type":"Results","text":"Surprisingly, when one or two phosphates were added, the overall proteins still configured largely as random coil (Fig. 1 and Fig. S6 B–D).","_id":"685af523b4ac24d5329d8ce0"},{"type":"Figure","text":"The remainder of each protein is random coil.","_id":"685af523b4ac24d5329d8ce1"},{"type":"Curator statement","text":"The figure 1 shows the secondary when the protein is without PTMs, phosphorilated or binding protein Ran. The secondary structure along the sequence is shown and the rest of the protein is random coil.","_id":"685af523b4ac24d5329d8ce2"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-04T09:03:48.527Z","_id":"685af523b4ac24d5329d8ce3"},"version":1,"_id":"685af523b4ac24d5329d8cd7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":47,"end":47,"statements":[{"type":"Results","text":"Accordingly, we carried out, matched NMR studies on the unphosphorylated (LM0P), singly phosphorylated (LM1P, T47), and doubly phosphorylated (LM2P, Y41/T47) variants of recombinant LM. ","_id":"685af523b4ac24d5329d8ce6"}],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d8ce5"},{"start":41,"end":41,"statements":[{"type":"Results","text":"Accordingly, we carried out, matched NMR studies on the unphosphorylated (LM0P), singly phosphorylated (LM1P, T47), and doubly phosphorylated (LM2P, Y41/T47) variants of recombinant LM. ","_id":"685af523b4ac24d5329d8ce8"}],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d8ce7"}],"cross_refs":[{"db":"PDB","id":"2MMH","_id":"685af523b4ac24d5329d8ce9"},{"db":"PDB","id":"2MMI","_id":"685af523b4ac24d5329d8cea"},{"db":"PDB","id":"2MML","_id":"685af523b4ac24d5329d8ceb"},{"db":"PDB","id":"2MMK","_id":"685af523b4ac24d5329d8cec"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0001238","ec_name":"nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":46,"end":67,"interaction_partner":[],"reference_html":"Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase. <i> Bacot-Davis VR, Ciomperlik JJ, Basta HA, Cornilescu CC, Palmenberg AC. </i> Proc Natl Acad Sci U S A, 2014","reference_id":"25331866","region_id":"DP01129r010","released":"2022_03","sample":[],"sequence_construct":"MATTMEQEICAHSMTFEECPKCSALQYRNGFYLLKYDEEWYPEELLTDGEDDVFDPDLDMEVVFETQ","statement":[{"type":"Results","text":"Surprisingly, when one or two phosphates were added, the overall proteins still configured largely as random coil (Fig. 1 and Fig. S6 B–D).","_id":"685af523b4ac24d5329d8ced"},{"type":"Figure","text":"The remainder of each protein is random coil.","_id":"685af523b4ac24d5329d8cee"},{"type":"Curator statement","text":"The figure 1 shows the secondary when the protein is without PTMs, phosphorilated or binding protein Ran. The secondary structure along the sequence is shown and the rest of the protein is random coil.","_id":"685af523b4ac24d5329d8cef"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-04T09:03:47.225Z","_id":"685af523b4ac24d5329d8cf0"},"version":1,"_id":"685af523b4ac24d5329d8ce4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2MMH","_id":"685af523b4ac24d5329d8cf2"},{"db":"PDB","id":"2MMI","_id":"685af523b4ac24d5329d8cf3"},{"db":"PDB","id":"2MML","_id":"685af523b4ac24d5329d8cf4"},{"db":"PDB","id":"2MMK","_id":"685af523b4ac24d5329d8cf5"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0001238","ec_name":"nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":29,"end":60,"interaction_partner":[],"reference_html":"Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase. <i> Bacot-Davis VR, Ciomperlik JJ, Basta HA, Cornilescu CC, Palmenberg AC. </i> Proc Natl Acad Sci U S A, 2014","reference_id":"25331866","region_id":"DP01129r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"When the 15N/13C protein labels were switched in Ran:LM0P complexes, the states of LM0P as influenced by Ran showed multiple peak shifts relative to free LM0P (Fig. 1 and Fig. S3A). The shifts included all residues in the hinge region, as had been anticipated from mutagenesis mapping (15). Also involved were regions from the carboxyl third of the protein. The zinc finger region did not change, maintaining the α1 and α2 helices. However, as with both phosphorylation datasets, the rest of (Ran):LM0P now became more compact (Fig. 4B).","_id":"685af523b4ac24d5329d8cf6"},{"type":"Curator statement","text":"Region disordered when it's bound to Ran","_id":"685af523b4ac24d5329d8cf7"},{"type":"Curator statement","text":"The figure 1 shows the secondary when the protein is without PTMs, phosphorilated or binding protein Ran. The secondary structure along the sequence is shown and the rest of the protein is random coil.","_id":"685af523b4ac24d5329d8cf8"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-04T09:03:46.160Z","_id":"685af523b4ac24d5329d8cf9"},"version":1,"_id":"685af523b4ac24d5329d8cf1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"19852","_id":"685af523b4ac24d5329d8cfb"},{"db":"PDB","id":"2MMH","_id":"685af523b4ac24d5329d8cfc"},{"db":"PDB","id":"2MMI","_id":"685af523b4ac24d5329d8cfd"},{"db":"PDB","id":"2MML","_id":"685af523b4ac24d5329d8cfe"},{"db":"PDB","id":"2MMK","_id":"685af523b4ac24d5329d8cff"},{"db":"BMRB","id":"19854","_id":"685af523b4ac24d5329d8d00"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0001238","ec_name":"nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":29,"end":41,"interaction_partner":[{"db":"UniProt","id":"P62826","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8d01"}],"reference_html":"Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase. <i> Bacot-Davis VR, Ciomperlik JJ, Basta HA, Cornilescu CC, Palmenberg AC. </i> Proc Natl Acad Sci U S A, 2014","reference_id":"25331866","region_id":"DP01129r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"When the 15N/13C protein labels were switched in Ran:LM0P complexes, the states of LM0P as influenced by Ran showed multiple peak shifts relative to free LM0P (Fig. 1 and Fig. S3A). The shifts included all residues in the hinge region, as had been anticipated from mutagenesis mapping (15). Also involved were regions from the carboxyl third of the protein. The zinc finger region did not change, maintaining the α1 and α2 helices. However, as with both phosphorylation datasets, the rest of (Ran):LM0P now became more compact (Fig. 4B).","_id":"685af523b4ac24d5329d8d02"},{"type":"Results","text":"The LM0P hinge and acidic domains interact significantly with the proximal tip of the Ran COOH tail (aa 203–210), but the remainder of this segment is free to arch without steric hindrance, morphing and encircling central interaction residues of LM0P (Fig. 4D). ","_id":"685af523b4ac24d5329d8d03"},{"type":"Results","text":"Important Ran:LM0P contacts include T32:L37, A183:D41, P184:Y45, P185:E42, Q196:Y36, Y197:Y40; Y197:W44, A204:G34, A204:L38, and T207:N33 (Fig. 4E).","_id":"685af523b4ac24d5329d8d04"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-04T09:05:36.299Z","_id":"685af523b4ac24d5329d8d05"},"version":1,"_id":"685af523b4ac24d5329d8cfa","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"19852","_id":"685af523b4ac24d5329d8d07"},{"db":"PDB","id":"2MMH","_id":"685af523b4ac24d5329d8d08"},{"db":"PDB","id":"2MMI","_id":"685af523b4ac24d5329d8d09"},{"db":"PDB","id":"2MML","_id":"685af523b4ac24d5329d8d0a"},{"db":"PDB","id":"2MMK","_id":"685af523b4ac24d5329d8d0b"},{"db":"BMRB","id":"19854","_id":"685af523b4ac24d5329d8d0c"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0001238","ec_name":"nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":47,"end":53,"interaction_partner":[{"db":"UniProt","id":"P62826","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8d0d"}],"reference_html":"Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase. <i> Bacot-Davis VR, Ciomperlik JJ, Basta HA, Cornilescu CC, Palmenberg AC. </i> Proc Natl Acad Sci U S A, 2014","reference_id":"25331866","region_id":"DP01129r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"When the 15N/13C protein labels were switched in Ran:LM0P complexes, the states of LM0P as influenced by Ran showed multiple peak shifts relative to free LM0P (Fig. 1 and Fig. S3A). The shifts included all residues in the hinge region, as had been anticipated from mutagenesis mapping (15). Also involved were regions from the carboxyl third of the protein. The zinc finger region did not change, maintaining the α1 and α2 helices. However, as with both phosphorylation datasets, the rest of (Ran):LM0P now became more compact (Fig. 4B).","_id":"685af523b4ac24d5329d8d0e"},{"type":"Results","text":"The LM0P hinge and acidic domains interact significantly with the proximal tip of the Ran COOH tail (aa 203–210), but the remainder of this segment is free to arch without steric hindrance, morphing and encircling central interaction residues of LM0P (Fig. 4D). ","_id":"685af523b4ac24d5329d8d0f"},{"type":"Results","text":"Important Ran:LM0P contacts include T32:L37, A183:D41, P184:Y45, P185:E42, Q196:Y36, Y197:Y40; Y197:W44, A204:G34, A204:L38, and T207:N33 (Fig. 4E).","_id":"685af523b4ac24d5329d8d10"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-04T09:05:18.615Z","_id":"685af523b4ac24d5329d8d11"},"version":1,"_id":"685af523b4ac24d5329d8d06","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"19852","_id":"685af523b4ac24d5329d8d13"},{"db":"PDB","id":"2MMH","_id":"685af523b4ac24d5329d8d14"},{"db":"PDB","id":"2MMI","_id":"685af523b4ac24d5329d8d15"},{"db":"PDB","id":"2MML","_id":"685af523b4ac24d5329d8d16"},{"db":"PDB","id":"2MMK","_id":"685af523b4ac24d5329d8d17"},{"db":"BMRB","id":"19854","_id":"685af523b4ac24d5329d8d18"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0001238","ec_name":"nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":56,"end":67,"interaction_partner":[{"db":"UniProt","id":"P62826","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8d19"}],"reference_html":"Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase. <i> Bacot-Davis VR, Ciomperlik JJ, Basta HA, Cornilescu CC, Palmenberg AC. </i> Proc Natl Acad Sci U S A, 2014","reference_id":"25331866","region_id":"DP01129r014","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"When the 15N/13C protein labels were switched in Ran:LM0P complexes, the states of LM0P as influenced by Ran showed multiple peak shifts relative to free LM0P (Fig. 1 and Fig. S3A). The shifts included all residues in the hinge region, as had been anticipated from mutagenesis mapping (15). Also involved were regions from the carboxyl third of the protein. The zinc finger region did not change, maintaining the α1 and α2 helices. However, as with both phosphorylation datasets, the rest of (Ran):LM0P now became more compact (Fig. 4B).","_id":"685af523b4ac24d5329d8d1a"},{"type":"Results","text":"The LM0P hinge and acidic domains interact significantly with the proximal tip of the Ran COOH tail (aa 203–210), but the remainder of this segment is free to arch without steric hindrance, morphing and encircling central interaction residues of LM0P (Fig. 4D). ","_id":"685af523b4ac24d5329d8d1b"},{"type":"Results","text":"Important Ran:LM0P contacts include T32:L37, A183:D41, P184:Y45, P185:E42, Q196:Y36, Y197:Y40; Y197:W44, A204:G34, A204:L38, and T207:N33 (Fig. 4E).","_id":"685af523b4ac24d5329d8d1c"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-04T09:05:16.800Z","_id":"685af523b4ac24d5329d8d1d"},"version":1,"_id":"685af523b4ac24d5329d8d12","reference_source":"pmid"}],"__v":0,"disorder_content":0.028347143480157,"disprot_consensus":{"full":[{"start":1,"end":19,"type":"D"},{"start":22,"end":67,"type":"D"}],"Structural state":[{"start":1,"end":19,"type":"D"},{"start":22,"end":67,"type":"D"}],"Disorder function":[{"start":1,"end":19,"type":"F"}],"Molecular function":[{"start":29,"end":41,"type":"F"},{"start":47,"end":53,"type":"F"},{"start":56,"end":67,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00640","name":"Phosphotyrosine interaction domain (PTB/PID)","start":39,"end":171},{"id":"PF06311","name":"NUMB domain","start":258,"end":338}],"gene3D":[{"start":23,"end":171,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"}]},"uniref50":"UniRef50_Q9QZS3","sequence":"MNKLRQSFRRKKDVYVPEASRPHQWQTDEEGVRTGKCSFPVKYLGHVEVDESRGMHICEDAVKRLKAERKFFKGFFGKTGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLERKQKREKECGVTATFDASRTTFTREGSFRVTTATEQAEREEIMKQMQDAKKAETDKIVVGSSVAPGNTAPSPSSPTSPTSDATTSLEMNNPHAIPRRHAPIEQLARQGSFRGFPALSQKMSPFKRQLSLRINELPSTMQRKTDFPIKNAVPEVEGEAESISSLCSQITNAFSTPEDPFSSAPMTKPVTVVAPQSPTFQANGTDSAFHVLAKPAHTALAPVAMPVRETNPWAHAPDAANKEIAATCSGTEWGQSSGAASPGLFQAGHRRTPSEADRWLEEVSKSVRAQQPQASAAPLQPVLQPPPPTAISQPASPFQGNAFLTSQPVPVGVVPALQPAFVPAQSYPVANGMPYPAPNVPVVGITPSQMVANVFGTAGHPQAAHPHQSPSLVRQQTFPHYEASSATTSPFFKPPAQHLNGSAAFNGVDDGRLASADRHTEVPTGTCPVDPFEAQWAALENKSKQRTNPSPTNPFSSDLQKTFEIEL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9QZS3","disprot_id":"DP01130","ncbi_taxon_id":9606,"regions_counter":2,"creator":"mguha","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":78,"region_id":"DP01130r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A Numb-Mdm2 fuzzy complex reveals an isoform-specific involvement of Numb in breast cancer. <i> Colaluca IN, Basile A, Freiburger L, D'Uva V, Disalvatore D, Vecchi M, Confalonieri S, Tosoni D, Cecatiello V, Malabarba MG, Yang CJ, Kainosho M, Sattler M, Mapelli M, Pece S, Di Fiore PP. </i> J Cell Biol, 2018","statement":[{"text":"NMR data demonstrate that Ex3 in the free PTBi is intrinsically disordered","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"mguha","start":68,"term_ontology":"IDPO","curator_name":"Mainak Guharoy","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29269425","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":78,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"A Numb-Mdm2 fuzzy complex reveals an isoform-specific involvement of Numb in breast cancer. <i> Colaluca IN, Basile A, Freiburger L, D'Uva V, Disalvatore D, Vecchi M, Confalonieri S, Tosoni D, Cecatiello V, Malabarba MG, Yang CJ, Kainosho M, Sattler M, Mapelli M, Pece S, Di Fiore PP. </i> J Cell Biol, 2018","statement":[{"text":"The Ex3-encoded sequence of Numb PTB is necessary for interaction with Mdm2","type":"Results"}],"term_id":"GO:0005515","curator_id":"mguha","start":68,"term_ontology":"GO","curator_name":"Mainak Guharoy","reference_id":"29269425","version":3,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01130r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P49757","date":"2018-06-21T12:07:34.000Z","acc":"P49757","name":"Protein numb homolog","length":651,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000000163C","genes":[{"name":{"value":"NUMB","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:8060","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8060"}}]},"synonyms":[{"value":"C14orf41","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:8060","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8060"}}]}]}],"alphafold_very_low_content":0.4608294930875576,"disorder_content":0.016897081413210446,"disprot_consensus":{"full":[{"start":68,"end":78,"type":"D"}],"Structural state":[{"start":68,"end":78,"type":"D"}],"Molecular function":[{"start":68,"end":78,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00011","name":"Hsp20/alpha crystallin family","start":70,"end":153},{"id":"PF00525","name":"Alpha crystallin A chain, N terminal","start":3,"end":61}],"gene3D":[{"start":56,"end":160,"id":"2.60.40.790","name":"2.60.40.790"}]},"uniref50":"UniRef50_O14558","sequence":"MEIPVPVQPSWLRRASAPLPGLSAPGRLFDQRFGEGLLEAELAALCPTTLAPYYLRAPSVALPVAQVPTDPGHFSVLLDVKHFSPEEIAVKVVGEHVEVHARHEERPDEHGFVAREFHRRYRLPPGVDPAAVTSALSPEGVLSIQAAPASAQAPPPAAAK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O14558","disprot_id":"DP01131","ncbi_taxon_id":9606,"regions_counter":12,"creator":"grivas","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":56,"region_id":"DP01131r001","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Molecular structure and dynamics of the dimeric human small heat shock protein HSPB6. <i> Weeks SD, Baranova EV, Heirbaut M, Beelen S, Shkumatov AV, Gusev NB, Strelkov SV. </i> J Struct Biol, 2014","statement":[{"text":"Since extensive crystallization efforts with the full-length human HSPB6 failed, we employed limited proteolysis to remove poorly ordered regions of this protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"tlazar","start":1,"term_ontology":"IDPO","curator_name":"Tamas Lazar","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24382496","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-12-03T15:21:01.689Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":39,"term_name":"protein folding chaperone","released":"2025_12","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","reference_html":"Molecular structure and dynamics of the dimeric human small heat shock protein HSPB6. <i> Weeks SD, Baranova EV, Heirbaut M, Beelen S, Shkumatov AV, Gusev NB, Strelkov SV. </i> J Struct Biol, 2014","statement":[{"text":"The ΔN23 truncation showed approximately 60% of the chaperoning activity of the FL protein with 1:0.2 ratio insulin:sHSP, and was almost as efficient as the FL at higher ratios (Fig. 6A). In contrast, both ΔN56 and ΔN39 showed minimal chaperone activity for all concentrations tested.","type":"Results"},{"text":"In addition, we found that ΔN23 retained most of the chaperoning activity for reduced insulin when compared to the full-length HSPB6, but the ΔN39 truncation was a poor chaperone (Figs. 6A and S8). Altogether, the correlating self-association properties and the chaperoning capacity of truncated variants clearly suggest that the conserved region of HSPB6 plays an important functional role, although more structural data are required towards a complete mechanistic model.","type":"Discussion"},{"text":"Both ΔN39 and ΔN56 remove the conserved N-terminal region, and both lose chaperone activity completely. This indicates that the sequence between residues ~24–39 (and extending to ~56) is crucial for chaperone-like function.","type":"Curator statement"}],"term_id":"GO:0044183","curator_id":"vnugnes","start":24,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"24382496","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2025-12-03T15:32:15.635Z","reference_source":"pmid","ec_id":"ECO:0007089","region_id":"DP01131r002","ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":56,"region_id":"DP01131r003","released":"2025_12","ec_id":"ECO:0006210","reference_html":"Molecular structure and dynamics of the dimeric human small heat shock protein HSPB6. <i> Weeks SD, Baranova EV, Heirbaut M, Beelen S, Shkumatov AV, Gusev NB, Strelkov SV. </i> J Struct Biol, 2014","statement":[{"text":"In addition the HSPB6 peaks are asymmetric, with the scattering tailing upwards at higher qRg values, suggesting that at all concentrations the protein is partially disordered. The combined evidence supports the hypothesis that in dilute solution the HSPB6 structure is based on the ACD dimer, having an oblate shape, flanked by N- and C- regions that are disordered.","type":"Results"},{"text":"The SAXS data confirm that the N-terminal domains of HSPB6 are poorly ordered, appearing as a ‘cloud’ of possible conformations in the final model (Fig. 5I).","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2025-12-03T15:20:49.388Z","reference_source":"pmid","term_name":"disorder","reference_id":"24382496","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":39,"end":69,"reference_id":"28089448","reference_source":"pmid","reference_html":"Structural Basis for the Interaction of a Human Small Heat Shock Protein with the 14-3-3 Universal Signaling Regulator. <i> Sluchanko NN, Beelen S, Kulikova AA, Weeks SD, Antson AA, Gusev NB, Strelkov SV. </i> Structure, 2017","date":"2025-12-04T08:22:02.318Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"PDB","id":"5LTW"}],"region_id":"DP01131r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P31947","statements":[{"type":"Methods","text":"The complexes of 14-3-3 proteins and phosphorylated HSPB6 variants were prepared and purified using size-exclusion chromatography (SEC) immediately before crystallization, essentially as described by Chernik et al. (2007)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"934"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"6503"}],"statement":[{"text":"The proximal half of the NTD (residues 39–69) is disordered in all chains, leaving an ambiguity in the interconnection of the N-terminal parts and the ACDs (see Figure 3B for details).","type":"Results"}],"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":16,"end":16,"position":"Specific residue"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-12-04T13:00:18.870Z"}},{"start":27,"end":38,"reference_id":"28089448","reference_source":"pmid","reference_html":"Structural Basis for the Interaction of a Human Small Heat Shock Protein with the 14-3-3 Universal Signaling Regulator. <i> Sluchanko NN, Beelen S, Kulikova AA, Weeks SD, Antson AA, Gusev NB, Strelkov SV. </i> Structure, 2017","date":"2025-12-04T08:23:01.980Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"PDB","id":"5LTW"}],"region_id":"DP01131r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P31947","statements":[{"type":"Methods","text":"The complexes of 14-3-3 proteins and phosphorylated HSPB6 variants were prepared and purified using size-exclusion chromatography (SEC) immediately before crystallization, essentially as described by Chernik et al. (2007)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"934"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"6503"}],"statement":[{"text":"In each of three complexes found in the crystallographic asymmetric unit, residues 1–20 of both NTDs, as well as residues 27–38 of one of the NTDs, could be traced. In addition, in one of the six NTDs, residues 21–26 were also traced, so that the structure of the entire region encompassing residues 1–38 could be established.","type":"Results"}],"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":16,"end":16,"position":"Specific residue"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-12-04T13:00:33.936Z"}},{"start":27,"end":38,"reference_id":"28089448","reference_source":"pmid","reference_html":"Structural Basis for the Interaction of a Human Small Heat Shock Protein with the 14-3-3 Universal Signaling Regulator. <i> Sluchanko NN, Beelen S, Kulikova AA, Weeks SD, Antson AA, Gusev NB, Strelkov SV. </i> Structure, 2017","date":"2025-12-04T08:25:31.586Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"PDB","id":"5LTW"}],"region_id":"DP01131r007","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P31947","statements":[{"type":"Methods","text":"The complexes of 14-3-3 proteins and phosphorylated HSPB6 variants were prepared and purified using size-exclusion chromatography (SEC) immediately before crystallization, essentially as described by Chernik et al. (2007)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"934"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"6503"}],"statement":[{"text":"Most interestingly, the crystal structure of the 14-3-3σ/pHSPB6 complex also reveals the RLFDQxFG motif (HSPB6 residues 27–34), which is the sole highly conserved region within the NTD of vertebrate sHSPs (Heirbaut et al., 2014). We have found that in the type I chain this motif becomes ordered upon its insertion into the distinct shared groove of the ACD dimer formed by the two β3 strands (Bagneris et al., 2009) (Figures 3B and 3D).","type":"Results"},{"text":"Ordering of the NTDs within the 14-3-3/pHSPB6 complex follows the principle of induced folding, which appears to be a general feature observed upon the interaction of IDR-containing proteins with their partners (Wright and Dyson, 2009).","type":"Discussion"}],"states_connection":[{"source":"DP01131r001","target":"DP01131r006"}],"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":16,"end":16,"position":"Specific residue"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-12-04T13:00:47.309Z"}},{"start":2,"end":10,"reference_id":"28089448","reference_source":"pmid","reference_html":"Structural Basis for the Interaction of a Human Small Heat Shock Protein with the 14-3-3 Universal Signaling Regulator. <i> Sluchanko NN, Beelen S, Kulikova AA, Weeks SD, Antson AA, Gusev NB, Strelkov SV. </i> Structure, 2017","date":"2025-12-04T08:29:18.744Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000056","term_name":"self-interaction","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"PDB","id":"5LUM"}],"region_id":"DP01131r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1117"}],"statement":[{"text":"Interestingly, we have found that the type I N terminus “patches” the β4/β8 groove on the side of the nearest ACD within one heterotetramer, whereas the type II chain engages in a similar patching across a crystal lattice contact (Figures 3A and S2). In each case, residues V5 and V7 insert into the hydrophobic core of the ACD (Figure 3C). Moreover, we could obtain an independent insight into this phenomenon by co-crystallizing the isolated ACD domain of HSPB6 (residues 72–149) with an N-terminal peptide of HSPB6, which corresponds to residues 2–10 (EIPVPVQPS, N-peptide). The resulting crystal structure at 2.6 Å resolution readily reveals the patching of the β4/β8 grooves at either side of the ACD dimer by well-ordered peptides (Figure 3C), fully confirming the patching mechanism observed in the 14-3-3σ/pHSPB6 complex (Figure S2C).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-12-04T13:01:43.454Z"}},{"start":13,"end":20,"reference_id":"28089448","reference_source":"pmid","reference_html":"Structural Basis for the Interaction of a Human Small Heat Shock Protein with the 14-3-3 Universal Signaling Regulator. <i> Sluchanko NN, Beelen S, Kulikova AA, Weeks SD, Antson AA, Gusev NB, Strelkov SV. </i> Structure, 2017","date":"2025-12-04T08:32:24.183Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"GO:0071889","term_name":"14-3-3 protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"PDB","id":"5LTW"}],"ec_go":"EXP","region_id":"DP01131r009","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"934"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"6503"}],"statement":[{"text":"First, both phosphoserine-containing regions of the HSPB6 dimer were found to bind in the corresponding 14-3-3 grooves (Figure 3A), in a conformation virtually identical to that observed in the 14-3-3/phosphopeptide 13–20 complex (Cα RMSD of 0.15 Å for residues 14–19). The observed structure thus confirms the hypothesis that HSPB6 fully sequesters the 14-3-3 dimer, making it unavailable for interaction with other phosphorylated partners.","type":"Results"},{"text":"Figure 6. Proposed Mechanism of the 14-3-3/pHSPB6 Regulatory Complex Formation\n\nKey regions of the HSPB6 NTD are labeled as follows: N, the N-terminal region (residues 1–10); P, the 14-3-3-binding region (residues 13–20) including the phosphoserine 16; C, the “central” conserved region (residues 27–34).","type":"Figure"}],"term_comment":"","term_def":"\"Binding to a 14-3-3 protein. A 14-3-3 protein is any of a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells, and have been implicated in the modulation of distinct biological processes by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. Each 14-3-3 protein sequence can be roughly divided into three sections: a divergent amino terminus, the conserved core region and a divergent carboxy-terminus. The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain, a cradle for interacting with client proteins.\" [GOC:cna, GOC:mah, PMID:15167810, PMID:19575580]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":16,"end":16,"position":"Specific residue"}],"interaction_partner":[{"db":"UniProt","id":"P31947","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-12-04T13:01:25.220Z"}},{"start":27,"end":34,"reference_id":"28089448","reference_source":"pmid","reference_html":"Structural Basis for the Interaction of a Human Small Heat Shock Protein with the 14-3-3 Universal Signaling Regulator. <i> Sluchanko NN, Beelen S, Kulikova AA, Weeks SD, Antson AA, Gusev NB, Strelkov SV. </i> Structure, 2017","date":"2025-12-04T12:55:49.361Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000056","term_name":"self-interaction","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"PDB","id":"5LTW"}],"region_id":"DP01131r010","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P31947"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"934"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"6503"}],"statement":[{"text":"Most interestingly, the crystal structure of the 14-3-3σ/pHSPB6 complex also reveals the RLFDQxFG motif (HSPB6 residues 27–34), which is the sole highly conserved region within the NTD of vertebrate sHSPs (Heirbaut et al., 2014). We have found that in the type I chain this motif becomes ordered upon its insertion into the distinct shared groove of the ACD dimer formed by the two β3 strands (Bagneris et al., 2009) (Figures 3B and 3D).","type":"Results"},{"text":"Figure 6. Proposed Mechanism of the 14-3-3/pHSPB6 Regulatory Complex Formation\n\nKey regions of the HSPB6 NTD are labeled as follows: N, the N-terminal region (residues 1–10); P, the 14-3-3-binding region (residues 13–20) including the phosphoserine 16; C, the “central” conserved region (residues 27–34). One of the two central regions may occupy the shared β3/β3 groove of the ACD dimer already in the free state.\nKey regions of the HSPB6 NTD are labeled as follows: N, the N-terminal region (residues 1–10); P, the 14-3-3-binding region (residues 13–20) including the phosphoserine 16; C, the “central” conserved region (residues 27–34).","type":"Figure"}],"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":16,"end":16,"position":"Specific residue"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-12-04T13:01:09.511Z"}}],"released":"2018_11","uniref100":"UniRef100_O14558","date":"2018-06-21T12:25:51.000Z","acc":"O14558","name":"Heat shock protein beta-6","length":160,"organism":"Homo sapiens","dataset":["Stress response proteins"],"UniParc":"UPI000016955A","genes":[{"name":{"value":"HSPB6"}}],"alphafold_very_low_content":0.11875,"disorder_content":0.43125,"disprot_consensus":{"full":[{"start":1,"end":26,"type":"D"},{"start":27,"end":38,"type":"T"},{"start":39,"end":69,"type":"D"}],"Structural state":[{"start":1,"end":69,"type":"D"}],"Molecular function":[{"start":13,"end":20,"type":"F"},{"start":24,"end":39,"type":"F"}],"Structural transition":[{"start":27,"end":38,"type":"T"}],"Disorder function":[{"start":2,"end":10,"type":"F"},{"start":27,"end":34,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00250","name":"Forkhead domain","start":162,"end":243},{"id":"PF16675","name":"KIX-binding domain of forkhead box O, CR2","start":423,"end":504},{"id":"PF16676","name":"Transactivation domain of FOXO protein family","start":595,"end":634}],"gene3D":[{"start":150,"end":249,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}]},"uniref50":"UniRef50_Q9R1E0","sequence":"MAEAPQVVEIDPDFEPLPRPRSCTWPLPRPEFSQSNSATSSPAPSGSAAANPDAAAGLPSASAAAVSADFMSNLSLLEESEDFPQAPGSVAAAVAAAAAAAATGGLCGDFQGPEAGCLHPAPPQPPPPGPLSQHPPVPPAAAGPLAGQPRKSSSSRRNAWGNLSYADLITKAIESSAEKRLTLSQIYEWMVKSVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIRVQNEGTGKSSWWMLNPEGGKSGKSPRRRAASMDNNSKFAKSRSRAAKKKASLQSGQEGAGDSPGSQFSKWPASPGSHSNDDFDNWSTFRPRTSSNASTISGRLSPIMTEQDDLGEGDVHSMVYPPSAAKMASTLPSLSEISNPENMENLLDNLNLLSSPTSLTVSTQSSPGTMMQQTPCYSFAPPNTSLNSPSPNYQKYTYGQSSMSPLPQMPIQTLQDNKSSYGGMSQYNCAPGLLKELLTSDSPPHNDIMTPVDPGVAQPNSRVLGQNVMMGPNSVMSTYGSQASHNKMMNPSSHTHPGHAQQTSAVNGRPLPHTVSTMPHTSGMNRLTQVKTPVQVPLPHPMQMSALGGYSSVSSCNGYGRMGLLHQEKLPSDLDGMFIERLDCDMESIIRNDLMDGDTLDFNFDNVLPNQSFPHSVKTTTHSWVSG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9R1E0","disprot_id":"DP01132","ncbi_taxon_id":9606,"regions_counter":3,"creator":"mpajkos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":266,"region_id":"DP01132r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for DNA recognition by FoxO1 and its regulation by posttranslational modification. <i> Brent MM, Anand R, Marmorstein R. </i> Structure, 2008","statement":[{"text":"\"electron density was not observed for the C-terminal wing 2 region of the FoxO1 DBD suggesting that it is flexible and disordered in the crystals.\"\n\"we crystallized and determined the structure of FoxO1 151–266 bound to the IRE and DBE2 sequences, but electron density was not observed for residues 242–266.\"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":242,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3CO6"}],"reference_id":"18786403","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":266,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural basis for DNA recognition by FoxO1 and its regulation by posttranslational modification. <i> Brent MM, Anand R, Marmorstein R. </i> Structure, 2008","statement":[{"text":"\"wing 2 enhances affinity through forming transient and/or multiple nonspecific electrostatic interactions with the phosphate backbone of the DNA. This hypothesis is supported by the observation that acetylation of Lys245 and Lys248 in wing 2 by CBP/p300 reduces DNA binding affinity\"","type":"Discussion"}],"term_id":"GO:0003676","curator_id":"mpajkos","start":242,"term_ontology":"GO","curator_name":"Mátyás Pajkos","reference_id":"18786403","version":3,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01132r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":262,"region_id":"DP01132r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structures reveal a new and novel FoxO1 binding site within the human glucose-6-phosphatase catalytic subunit 1 gene promoter. <i> Singh P, Han EH, Endrizzi JA, O'Brien RM, Chi YI. </i> J Struct Biol, 2017","statement":[{"text":"\"the lack of electron density at the C-terminal second wing (W2) indicates its flexibility and disorderness in FoxO1. Although we used the entire FoxO1-DBD (amino acids 154–262) in crystallization, the final electron density was only visible for the regions between amino acid 160 and 245 for both monomers.\"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":246,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5DUI"}],"reference_id":"28223045","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q12778","date":"2018-06-21T13:17:36.000Z","acc":"Q12778","name":"Forkhead box protein O1","length":655,"organism":"Homo sapiens","dataset":["Autophagy-related proteins","Cancer-related proteins"],"UniParc":"UPI000012ADE9","genes":[{"name":{"value":"FOXO1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12228231","url":"http://www.ncbi.nlm.nih.gov/pubmed/12228231","alternativeUrl":"https://europepmc.org/abstract/MED/12228231"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:3819","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:3819"}}]},"synonyms":[{"value":"FKHR","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9479491","url":"http://www.ncbi.nlm.nih.gov/pubmed/9479491","alternativeUrl":"https://europepmc.org/abstract/MED/9479491"}}]},{"value":"FOXO1A"}]}],"alphafold_very_low_content":0.7007633587786259,"disorder_content":0.03816793893129771,"disprot_consensus":{"full":[{"start":242,"end":266,"type":"D"}],"Structural state":[{"start":242,"end":266,"type":"D"}],"Molecular function":[{"start":242,"end":266,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MVRSRQMCNTNMSVPTDGAVTTSQIPASEQETLVRPKPLLLKLLKSVGAQKDTYTMKEVLFYLGQYIMTKRLYDEKQQHIVYCSNDLLGDLFGVPSFSVKEHRKIYTMIYRNLVVVNQQESSDSGTSVSENRCHLEGGSDQKDLVQELQEEKPSSSHLVSRPSTSSRRRAISETEENSDELSGERQRKRHKSDSISLSFDESLALCVIREICCERSSSSESTGTPSNPDLDAGVSEHSGDWLDQDSVSDQFSVEFEVESLDSEDYSLSEEGQELSDEDDEVYQVTVYQAGESDTDSFEEDPEISLADYWKCTSCNEMNPPLPSHCNRCWALRENWLPEDKGKDKGEISEKAKLENSTQAEEGFDVPDCKKTIVNDSRESCVEENDDKITQASQSQESEDYSQPSTSSSIIYSSQEDVKEFEREETQDKEESVESSLPLNAIEPCVICQGRPKNGCIVHGKTGHLMACFTCAKKLKKRNKPCPVCRQPIQMIVLTYFP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"","disprot_id":"DP01133","ncbi_taxon_id":9606,"regions_counter":3,"creator":"mguha","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":302,"region_id":"DP01133r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A Numb-Mdm2 fuzzy complex reveals an isoform-specific involvement of Numb in breast cancer. <i> Colaluca IN, Basile A, Freiburger L, D'Uva V, Disalvatore D, Vecchi M, Confalonieri S, Tosoni D, Cecatiello V, Malabarba MG, Yang CJ, Kainosho M, Sattler M, Mapelli M, Pece S, Di Fiore PP. </i> J Cell Biol, 2018","statement":[{"text":"Experimental NMR chemical shifts and 15N relaxation data demonstrate that Mdm2(216-302) is an intrinsically unstructured and highly flexible monomeric protein in solution, as confirmed by static light scattering analysis.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mguha","start":216,"term_ontology":"IDPO","curator_name":"Mainak Guharoy","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29269425","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":302,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"A Numb-Mdm2 fuzzy complex reveals an isoform-specific involvement of Numb in breast cancer. <i> Colaluca IN, Basile A, Freiburger L, D'Uva V, Disalvatore D, Vecchi M, Confalonieri S, Tosoni D, Cecatiello V, Malabarba MG, Yang CJ, Kainosho M, Sattler M, Mapelli M, Pece S, Di Fiore PP. </i> J Cell Biol, 2018","statement":[{"text":"This acidic region of Mdm2 forms a fuzzy complex with a short sequence encompassing the alternatively spliced exon 3 (Ex3) of Numb.","type":"Curator statement"}],"term_id":"GO:0005515","curator_id":"mguha","start":216,"term_ontology":"GO","curator_name":"Mainak Guharoy","reference_id":"29269425","version":3,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01133r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":302,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"A Numb-Mdm2 fuzzy complex reveals an isoform-specific involvement of Numb in breast cancer. <i> Colaluca IN, Basile A, Freiburger L, D'Uva V, Disalvatore D, Vecchi M, Confalonieri S, Tosoni D, Cecatiello V, Malabarba MG, Yang CJ, Kainosho M, Sattler M, Mapelli M, Pece S, Di Fiore PP. </i> J Cell Biol, 2018","statement":[{"text":"Our NMR data demonstrate that the Numb-Mdm2 binding interface comprises residues 216-302 of the Mdm2 acidic domain.","type":"Discussion"}],"term_id":"GO:0005515","curator_id":"mguha","start":216,"term_ontology":"GO","curator_name":"Mainak Guharoy","reference_id":"29269425","version":3,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01133r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"","date":"2018-06-21T13:56:43.000Z","acc":"Q00987-11","name":"Isoform 11 of E3 ubiquitin-protein ligase Mdm2","length":497,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00006CA35C","genes":[{"name":{"value":"MDM2"}}],"disorder_content":0.1750503018108652,"disprot_consensus":{"full":[{"start":216,"end":302,"type":"D"}],"Structural state":[{"start":216,"end":302,"type":"D"}],"Molecular function":[{"start":216,"end":302,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00096","name":"Zinc finger, C2H2 type","start":546,"end":570},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":607,"end":632},{"id":"PF23561","name":"C2H2 zinc finger","start":515,"end":544}],"gene3D":[{"start":544,"end":574,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":575,"end":604,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":605,"end":633,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":479,"end":511,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":512,"end":543,"id":"3.30.160.60","name":"Classic Zinc Finger"}]},"uniref50":"UniRef50_Q61602","sequence":"MEAQSHSSTTTEKKKVENSIVKCSTRTDVSEKAVASSTTSNEDESPGQTYHRERRNAITMQPQNVQGLSKVSEEPSTSSDERASLIKKEIHGSLPHVAEPSVPYRGTVFAMDPRNGYMEPHYHPPHLFPAFHPPVPIDARHHEGRYHYDPSPIPPLHMTSALSSSPTYPDLPFIRISPHRNPTAASESPFSPPHPYINPYMDYIRSLHSSPSLSMISATRGLSPTDAPHAGVSPAEYYHQMALLTGQRSPYADIIPSAATAGTGAIHMEYLHAMDSTRFSSPRLSARPSRKRTLSISPLSDHSFDLQTMIRTSPNSLVTILNNSRSSSSASGSYGHLSASAISPALSFTYSSAPVSLHMHQQILSRQQSLGSAFGHSPPLIHPAPTFPTQRPIPGIPTVLNPVQVSSGPSESSQNKPTSESAVSSTGDPMHNKRSKIKPDEDLPSPGARGQQEQPEGTTLVKEEGDKDESKQEPEVIYETNCHWEGCAREFDTQEQLVHHINNDHIHGEKKEFVCRWLDCSREQKPFKAQYMLVVHMRRHTGEKPHKCTFEGCTKAYSRLENLKTHLRSHTGEKPYVCEHEGCNKAFSNASDRAKHQNRTHSNEKPYVCKIPGCTKRYTDPSSLRKHVKTVHGPEAHVTKKQRGDIHPRPPPPRDSGSHSQSRSPGRPTQGALGEQQDLSNTTSKREECLQVKTVKAEKPMTSQPSPGGQSSCSSQQSPISNYSNSGLELPLTDGGSIGDLSAIDETPIMDSTISTATTALALQARRNPAGTKWMEHVKLERLKQVNGMFPRLNPILPPKAPAVSPLIGNGTQSNNTCSLGGPMTLLPGRSDLSGVDVTMLNMLNRRDSSASTISSAYLSSRRSSGISPCFSSRRSSEASQAEGRPQNVSVADSYDPISTDASRRSSEASQSDGLPSLLSLTPAQQYRLKAKYAAATGGPPPTPLPNMERMSLKTRLALLGDALEPGVALPPVHAPRRCSDGGAHGYGRRHLQPHDAPGHGVRRASDPVRTGSEGLALPRVPRFSSLSSCNPPAMATSAEKRSLVLQNYTRPEGGQSRNFHSSPCPPSITENVTLESLTMDADANLNDEDFLPDDVVQYLNSQNQAGYEQHFPSALPDDSKVPHGPGDFDAPGLPDSHAGQQFHALEQPCPEGSKTDLPIQWNEVSSGSADLSSSKLKCGPRPAVPQTRAFGFCNGMVVHPQNPLRSGPAGGYQTLGENSNPYGGPEHLMLHNSPGSGTSGNAFHEQPCKAPQYGNCLNRQPVAPGALDGACGAGIQASKLKSTPMQGSGGQLNFGLPVAPNESAGSMVNGMQNQDPVGQGYLAHQLLGDSMQHPGAGRPGQQMLGQISATSHINIYQGPESCLPGAHGMGSQPSSLAVVRGYQPCASFGGSRRQAMPRDSLALQSGQLSDTSQTCRVNGIKMEMKGQPHPLCSNLQNYSGQFYDQTVGFSQQDTKAGSFSISDASCLLQGTSAKNSELLSPGANQVTSTVDSLDSHDLEGVQIDFDAIIDDGDHSSLMSGALSPSIIQNLSHSSSRLTTPRASLPFPALSMSTTNMAIGDMSSLLTSLAEESKFLAVMQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P10071","disprot_id":"DP01134","ncbi_taxon_id":9606,"regions_counter":4,"creator":"fkordevani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":236,"region_id":"DP01134r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"The transcriptional repressor domain of Gli3 is intrinsically disordered. <i> Tsanev R, Vanatalu K, Jarvet J, Tanner R, Laur K, Tiigimägi P, Kragelund BB, Østerlund T, Kogerman P. </i> PLoS One, 2013","statement":[{"text":"The NMR spectrum of Gli3RD expressing cells (Fig. 2A) is qualitatively similar to that of the purified protein, measured at pH 7.4 (Fig. 2B). All of the proton peaks lie within a narrow window of 8 ppm that is typical for unfolded peptides.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":106,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24146948","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-05-04T17:35:43.596Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907"}],"released":"2018_11","uniref100":"UniRef100_P10071","date":"2018-06-22T06:25:18.000Z","acc":"P10071","name":"Transcriptional activator GLI3","length":1580,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI000012B60B","genes":[{"name":{"value":"GLI3"}}],"alphafold_very_low_content":0.8316455696202532,"disorder_content":0.08291139240506329,"disprot_consensus":{"full":[{"start":106,"end":236,"type":"D"}],"Structural state":[{"start":106,"end":236,"type":"D"}]}},{"features":{"pfam":[{"id":"PF09649","name":"Histone chaperone domain CHZ","start":87,"end":120}]},"uniref50":"UniRef50_P40019","sequence":"MSDEAKEKRELESQKESSHNKSEKSVEPKPKRRRRRNYDDYDAEVAKEETKAKNGLTKSENNGTVEDSESDMDDAKLDALMGNEGEEEEDDLAEIDTSNIITSGRRTRGKVIDYKKTAEELDKKEPSTGSKDDVGYGEKEEDDEDEEDDDFKE","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P40019","disprot_id":"DP01135","ncbi_taxon_id":559292,"regions_counter":2,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":153,"region_id":"DP01135r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Chz1, a nuclear chaperone for histone H2AZ. <i> Luk E, Vu ND, Patteson K, Mizuguchi G, Wu WH, Ranjan A, Backus J, Sen S, Lewis M, Bai Y, Wu C. </i> Mol Cell, 2007","statement":[{"text":"Chz1 alone yielded a typical CD spectrum characteristic of an unfolded polypeptide chain, suggesting that Chz1 is unfolded in physiological conditions.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":1,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"17289584","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":153,"term_name":"disorder to order","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"17289584","version":2,"reference_html":"Chz1, a nuclear chaperone for histone H2AZ. <i> Luk E, Vu ND, Patteson K, Mizuguchi G, Wu WH, Ranjan A, Backus J, Sen S, Lewis M, Bai Y, Wu C. </i> Mol Cell, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP01135r002","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_P40019","date":"2018-06-22T11:11:31.000Z","acc":"P40019","name":"Histone H2A.Z-specific chaperone CHZ1","length":153,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000013AC8E","genes":[{"name":{"value":"CHZ1"},"olnNames":[{"value":"YER030W"}]}],"alphafold_very_low_content":0.3006535947712418,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":153,"type":"T"}],"Structural state":[{"start":1,"end":153,"type":"D"}],"Structural transition":[{"start":1,"end":153,"type":"T"}]}},{"features":{"pfam":[{"id":"PF13639","name":"Ring finger domain","start":250,"end":280}]},"uniref50":"UniRef50_P22470","sequence":"MSESGQEQNRGTNTSPNNAENNNNSNAASGPLNGGAEQTRNITVSIQYSYFTPERLAHLSNISNNDNNENNSAASGSTIANGTGPSFGIGNGGHQPDGALVLSFRDVPASTPQDRLNSFISVAAQLAMERFNRLLNRPKGISKDEFDKLPVLQVSDLPKAEGPLCSICYDEYEDEVDSTKAKRKRDSENEEESEGTKKRKDNEGAPLRTTADNDSNPSITNATVVEPPSIPLTEQQRTLNDEETNPSYKHSPIKLPCGHIFGRECIYKWSRLENSCPLCRQKISESVGVQRAAQQDTDEVAANEAAFERIRRVLYDPTAVNSTNENSSAPSENTSNTTVPTIGNASSGEQMLSRTGFFLVPQNGQPLHNPVRLPPNDSDRNGVNGPSSTTQNPPSNSGGSNNNQSPRWVPIPLTLFQFHSPNPNPSASDSSASPSAANGPNSNNTSSDATDPHHNRLRAVLDHIFNVAQRGTSDTSATTAPGAQTVHNQGRNDSSSSDTTQGSSFLENISRLTGHFTNGSRDNNNDNNHSNDQQRGGSTGENNRNNLFSSGVASYRNQNGDVTTVELRNNNSAAFPPTDENPSQGQGSSSSDTTIHNDVPNDNNEQRSSQ","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P22470","disprot_id":"DP01136","ncbi_taxon_id":559292,"regions_counter":10,"creator":"mguha","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":610,"region_id":"DP01136r002","released":"2023_12","ec_id":"ECO:0007688","reference_html":"Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates. <i> Rosenbaum JC, Fredrickson EK, Oeser ML, Garrett-Engele CM, Locke MN, Richardson LA, Nelson ZW, Hetrick ED, Milac TI, Gottschling DE, Gardner RG. </i> Mol Cell, 2011","statement":[{"text":"We also observed that intact San1 migrated at ~100 kDa, larger than its calculated ~66 kDa mass. Intrinsically disordered proteins often show this behavior due to a low content of hydrophobic residues (Tompa, 2002).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"gel electrophoresis evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-24T12:58:30.842Z","reference_source":"pmid","term_name":"disorder","reference_id":"21211726","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":610,"region_id":"DP01136r003","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates. <i> Rosenbaum JC, Fredrickson EK, Oeser ML, Garrett-Engele CM, Locke MN, Richardson LA, Nelson ZW, Hetrick ED, Milac TI, Gottschling DE, Gardner RG. </i> Mol Cell, 2011","statement":[{"text":"The CD spectrum of San1 had a minimum close to 200 nm (Figure 2E), which is characteristic of a protein with mostly random coil content and is typical for intrinsically disordered proteins (Receveur-Brechot et al., 2006). ","type":"Results"},{"text":"The San1 spectrum had a small valley at ~224 nm indicating San1 possesses some α-helical content.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-24T13:00:37.323Z","reference_source":"pmid","term_name":"disorder","reference_id":"21211726","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":610,"region_id":"DP01136r004","released":"2023_12","ec_id":"ECO:0001184","reference_html":"Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates. <i> Rosenbaum JC, Fredrickson EK, Oeser ML, Garrett-Engele CM, Locke MN, Richardson LA, Nelson ZW, Hetrick ED, Milac TI, Gottschling DE, Gardner RG. </i> Mol Cell, 2011","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"gel-filtration evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-24T12:59:05.546Z","reference_source":"pmid","term_name":"disorder","reference_id":"21211726","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"In light of the disorder predictions, we repeated the gel filtration assay using San1 purified from E. coli and found that San1 migrated at ~500 kDa despite the absence of any yeast proteins (Figure 2C), indicating that San1 is either disordered and/or forms multimers with itself. To examine if San1 forms multimers, we coexpressed differently tagged versions of San1 in E. coli and found that neither version copurified with the other (E.K.F. and R.G.G., unpublished data), indicating that San1 does not self-associate.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":610,"region_id":"DP01136r005","released":"2023_12","ec_id":"ECO:0007691","reference_html":"Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates. <i> Rosenbaum JC, Fredrickson EK, Oeser ML, Garrett-Engele CM, Locke MN, Richardson LA, Nelson ZW, Hetrick ED, Milac TI, Gottschling DE, Gardner RG. </i> Mol Cell, 2011","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-24T12:55:57.177Z","reference_source":"pmid","term_name":"disorder","reference_id":"21211726","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"We found San1 was completely digested at the earliest time points whereas BSA resisted digestion throughout the time course of protease treatment (Figure 2D).","type":"Results"}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":610,"region_id":"DP01136r006","released":"2023_12","ec_id":"ECO:0006030","reference_html":"Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates. <i> Rosenbaum JC, Fredrickson EK, Oeser ML, Garrett-Engele CM, Locke MN, Richardson LA, Nelson ZW, Hetrick ED, Milac TI, Gottschling DE, Gardner RG. </i> Mol Cell, 2011","term_id":"GO:0051787","curator_id":"vnugnes","start":1,"term_ontology":"GO","curator_name":"Victoria Nugnes","ec_name":"co-immunoprecipitation evidence used in manual assertion","version":5,"curator_orcid":"0000-0001-8399-7907","date":"2026-06-26T14:57:46.683Z","reference_source":"pmid","term_name":"misfolded protein binding","reference_id":"21211726","ec_go":"IPI","disprot_namespace":"Disorder function","construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"We previously appended a 3xHSV epitope tag to natively expressed San1 in a sir4-9 strain and found it was functional for Sir4-9 degradation (Gardner et al., 2005)."}]}],"statement":[{"text":"The San1 substrate Sir4-9 had the greatest number of spectral counts in the tagged coIP replicates and showed the greatest enrichment over the untagged replicates.","type":"Results"},{"text":"Authors shows SAN1 only binds to Sir4, when the latter is mutated to a temperature-sensitive version and is induced to unfold, and not to the native wildtype protein.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a misfolded protein.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","interaction_partner":[{"db":"UniProt","id":"P11978","operator":"and","partner_start":null,"partner_end":null}]},{"start":1,"end":164,"reference_id":"21211726","reference_source":"pmid","reference_html":"Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates. <i> Rosenbaum JC, Fredrickson EK, Oeser ML, Garrett-Engele CM, Locke MN, Richardson LA, Nelson ZW, Hetrick ED, Milac TI, Gottschling DE, Gardner RG. </i> Mol Cell, 2011","date":"2026-06-26T14:57:54.689Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051787","term_name":"misfolded protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005805","ec_ontology":"ECO","ec_name":"yeast 2-hybrid evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"construct_alterations":[{"term_id":"MI:0693","term_name":"Gal4 DNA-binding domain tag","term_namespace":"Tag","start":null,"end":null,"position":"unspecified"},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Cys165_Glu285del","start":null,"end":null,"position":null}],"ec_go":"IPI","region_id":"DP01136r007","statement":[{"text":"To test this, we fused to the Gal4 DNA-binding domain (GBD) a ubiquitination-deficient version of San1, which contains the C279S substitution in the RING domain (Gardner et al., 2005). We also fused the Gal4 activation domain (GAD) to either normal or mutant Sir4, Cdc68, and Cdc13.","type":"Results"},{"text":"As anticipated, we observed an interaction between San1 and mutant Sir4-9, Cdc68-1, and Cdc13-1 but not with normal Sir4, Cdc68, and Cdc13 (Figure 1A).","type":"Results"},{"text":"Authors shows SAN1 only binds to Sir4, when the latter is mutated to a temperature-sensitive version and is induced to unfold, and not to the native wildtype protein.","type":"Curator statement"},{"text":"As expected, the RING domain deletion (residues 165-285) had little effect on substrate interactions consistent with its primary function in ubiquitin conjugase recruitment. In agreement with the second model, no single interaction profile emerged for San1-substrate interactions; multiple deletions in the N- and C-terminal disordered regions differentially affected each substrate interaction with San1 having a distinct interaction profile with each substrate.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a misfolded protein.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","interaction_partner":[{"db":"UniProt","id":"P11978","operator":"and","partner_start":null,"partner_end":null}]},{"start":286,"end":610,"reference_id":"21211726","reference_source":"pmid","reference_html":"Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates. <i> Rosenbaum JC, Fredrickson EK, Oeser ML, Garrett-Engele CM, Locke MN, Richardson LA, Nelson ZW, Hetrick ED, Milac TI, Gottschling DE, Gardner RG. </i> Mol Cell, 2011","date":"2026-06-26T14:58:05.563Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051787","term_name":"misfolded protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005805","ec_ontology":"ECO","ec_name":"yeast 2-hybrid evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Cys165_Glu285del","start":null,"end":null,"position":"unspecified"},{"term_id":"MI:0693","term_name":"Gal4 DNA-binding domain tag","term_namespace":"Tag","start":null,"end":null,"position":"unspecified"}],"ec_go":"IPI","region_id":"DP01136r008","statement":[{"text":"To test this, we fused to the Gal4 DNA-binding domain (GBD) a ubiquitination-deficient version of San1, which contains the C279S substitution in the RING domain (Gardner et al., 2005). We also fused the Gal4 activation domain (GAD) to either normal or mutant Sir4, Cdc68, and Cdc13.","type":"Results"},{"text":"As anticipated, we observed an interaction between San1 and mutant Sir4-9, Cdc68-1, and Cdc13-1 but not with normal Sir4, Cdc68, and Cdc13 (Figure 1A).","type":"Results"},{"text":"Authors shows SAN1 only binds to Sir4, when the latter is mutated to a temperature-sensitive version and is induced to unfold, and not to the native wildtype protein.","type":"Curator statement"},{"text":"As expected, the RING domain deletion (residues 165-285) had little effect on substrate interactions consistent with its primary function in ubiquitin conjugase recruitment. In agreement with the second model, no single interaction profile emerged for San1-substrate interactions; multiple deletions in the N- and C-terminal disordered regions differentially affected each substrate interaction with San1 having a distinct interaction profile with each substrate.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a misfolded protein.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","interaction_partner":[{"db":"UniProt","id":"P11978","operator":"and","partner_start":null,"partner_end":null}]},{"start":1,"end":610,"reference_id":"21211726","reference_source":"pmid","reference_html":"Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates. <i> Rosenbaum JC, Fredrickson EK, Oeser ML, Garrett-Engele CM, Locke MN, Richardson LA, Nelson ZW, Hetrick ED, Milac TI, Gottschling DE, Gardner RG. </i> Mol Cell, 2011","date":"2023-08-24T15:01:06.980Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0004842","term_name":"ubiquitin-protein transferase activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001222","ec_ontology":"ECO","ec_name":"in vivo ubiquitination assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP01136r009","statement":[{"text":"We also examined San1-dependent ubiquitination of select GAD-fusion substrates using the in coli assay and found they were ubiquitinated in a San1-dependent manner (Figure 5D), indicating San1 directly targets these substrates as well.","type":"Results"}],"term_comment":"","term_def":"\"Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages.\" [GOC:BioGRID, GOC:jh2, PMID:9635407]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":610,"reference_id":"21211726","reference_source":"pmid","reference_html":"Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates. <i> Rosenbaum JC, Fredrickson EK, Oeser ML, Garrett-Engele CM, Locke MN, Richardson LA, Nelson ZW, Hetrick ED, Milac TI, Gottschling DE, Gardner RG. </i> Mol Cell, 2011","date":"2025-12-23T12:42:05.520Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0045732","term_name":"positive regulation of protein catabolic process","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"ec_go":"IEP","region_id":"DP01136r010","statement":[{"text":"We analyzed the degradation of each GAD fusion and found 25 of 28 required San1 to be fully degraded: 14 underwent primarily San1-dependent degradation (Figures 5A and S4A), 11 were subject to degradation that was partially dependent on San1 (Figures 5B and S4A), and 3 were stable when San1 was present (Figure 5C).","type":"Results"}],"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"}],"released":"2018_11","uniref100":"UniRef100_P22470","date":"2018-06-22T17:40:22.000Z","acc":"P22470","name":"Protein SAN1","length":610,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000135539","genes":[{"name":{"value":"SAN1"},"orfNames":[{"value":"YD2943.02C"}],"olnNames":[{"value":"YDR143C"}]}],"alphafold_very_low_content":0.6491803278688525,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":610,"type":"D"}],"Structural state":[{"start":1,"end":610,"type":"D"}],"Molecular function":[{"start":1,"end":610,"type":"F"}],"Biological process":[{"start":1,"end":610,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05093","name":"Cytokine-induced anti-apoptosis inhibitor 1, Fe-S biogenesis","start":236,"end":268},{"id":"PF05093","name":"Cytokine-induced anti-apoptosis inhibitor 1, Fe-S biogenesis","start":270,"end":303},{"id":"PF20922","name":"Anamorsin, N-terminal","start":9,"end":171}],"gene3D":[{"start":1,"end":173,"id":"3.40.50.150","name":"Vaccinia Virus protein VP39"}]},"uniref50":"UniRef50_Q6FI81","sequence":"MADFGISAGQFVAVVWDKSSPVEALKGLVDKLQALTGNEGRVSVENIKQLLQSAHKESSFDIILSGLVPGSTTLHSAEILAEIARILRPGGCLFLKEPVETAVDNNSKVKTASKLCSALTLSGLVEVKELQREPLTPEEVQSVREHLGHESDNLLFVQITGKKPNFEVGSSRQLKLSITKKSSPSVKPAVDPAAAKLWTLSANDMEDDSMDLIDSDELLDPEDLKKPDPASLRAASCGEGKKRKACKNCTCGLAEELEKEKSREQMSSQPKSACGNCYLGDAFRCASCPYLGMPAFKPGEKVLLSDSNLHDA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q6FI81","disprot_id":"DP01137","ncbi_taxon_id":9606,"regions_counter":2,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":266,"region_id":"DP01137r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Anamorsin is a [2Fe-2S] cluster-containing substrate of the Mia40-dependent mitochondrial protein trapping machinery. <i> Banci L, Bertini I, Ciofi-Baffoni S, Boscaro F, Chatzi A, Mikolajczyk M, Tokatlidis K, Winkelmann J. </i> Chem Biol, 2011","statement":[{"text":"The 1H-15N HSQC spectra of the full-length protein shows highly crowded cross-peaks in the spectral region between 8 and 8.5 ppm indicating that the protein contains an unstructured region, in addition to several signals spread over a larger spectral range, indicative of folded conformations. After degradation, the 1H-15N HSQC spectrum of the resulting fragment shows the disappearance of many of the signals in the crowded, central region, whereas the well-resolved resonances are still present and do not show significant chemical shift changes. 15N{1H} NOEs experiments on the full-length anamorsin showed that the residues not belonging to the N-terminal domain (that are all in the highly crowded spectral region between 8 and 8.5 ppm) exhibited negative or very low NOEs, indicative of a high degree of flexibility in the C-terminal part of the protein. We can conclude that the N-terminal part is well-folded whereas the C-terminal part, comprising both the linker and CIAPIN1 domain, is largely unstructured and flexible and therefore, highly prone to degradation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":173,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"21700214","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":266,"term_name":"iron ion binding","start":173,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Anamorsin contains a well-folded N-terminal domain and a largely unstructured, flexible C-terminal part, containing a CIAPIN1 domain with highly conserved cysteine pattern. Secondary structure and folding predictions reveal that these two domains in anamorsin are separated by an unstructured amino acid linker of ∼50 residues and that a large part of the CIAPIN1 domain, in particular its initial segment (residues 222–266), is structurally highly disordered, whereas the final segment is predicted to be more structured. The latter region of the CIAPIN1 domain contains a twin CX2C motif whereas the initial segment of the CIAPIN1 domain contains the four additional cysteines of the highly conserved cysteine pattern. It is likely that cysteines of the highly conserved cysteine pattern in anamorsin are involved in iron binding. Mass spectrometry analysis revealed that the stable fragment is constituted by the N-terminal part spanning aa 1–172 of the protein. During degradation, the color of the anamorsin solution is lost, indicating that iron is released. Because the remaining stable fragment does not contain cysteines of the CIAPIN1 domain, at least one of the latter cysteines is essential for iron binding.","type":"Results"}],"curator_id":"fquaglia","released":"2022_12","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"21700214","version":4,"reference_html":"Anamorsin is a [2Fe-2S] cluster-containing substrate of the Mia40-dependent mitochondrial protein trapping machinery. <i> Banci L, Bertini I, Ciofi-Baffoni S, Boscaro F, Chatzi A, Mikolajczyk M, Tokatlidis K, Winkelmann J. </i> Chem Biol, 2011","date":"2022-12-06T11:26:46.488Z","term_id":"GO:0005506","ec_id":"ECO:0006165","region_id":"DP01137r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an iron (Fe) ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":false,"curator_orcid":"0000-0002-0341-4888"}],"released":"2018_11","uniref100":"UniRef100_Q6FI81","date":"2018-06-25T10:53:32.000Z","acc":"Q6FI81","name":"Anamorsin","length":312,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00003B116F","genes":[{"name":{"value":"CIAPIN1","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03115","url":"https://hamap.expasy.org/unirule/MF_03115"}}]},"orfNames":[{"value":"CUA001"},{"value":"PRO0915"}]}],"alphafold_very_low_content":0.03205128205128205,"disorder_content":0.30128205128205127,"disprot_consensus":{"full":[{"start":173,"end":266,"type":"D"}],"Structural state":[{"start":173,"end":266,"type":"D"}],"Molecular function":[{"start":173,"end":266,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02037","name":"SAP domain","start":460,"end":493},{"id":"PF02755","name":"RPEL repeat","start":92,"end":113},{"id":"PF02755","name":"RPEL repeat","start":136,"end":158},{"id":"PF02755","name":"RPEL repeat","start":180,"end":200}],"gene3D":[{"start":441,"end":509,"id":"1.10.720.30","name":"SAP domain"}]},"uniref50":"UniRef50_Q8K4J6","sequence":"MGGVTITKAKVDFSSVVCLPPSVIAVNGLDGGGAGENDEEPVLLSLSAAPSPQSEAVANELQELSLQPELTLGLHPGRNPNLPPLSERKNVLQLKLQQRRTREELVSQGIMPPLKSPAAFHEQRRSLERARTEDYLKRKIRSRPERSELVRMHILEETSAEPSLQAKQLKLKRARLADDLNEKIAQRPGPMELVEKNILPVESSLKEALIVGQVNYPKVADSSSFDEDSSDALSPEQPASHESQGSVPSPLESRASDLLPSATSISPTQVLSQLPMAPDPGETLFLAEQPPLPPPPLLPPSLTSGSIVPTAKPAPTLIKQSQPKSASEKSQRSKKAKELKPKVKKLKYHQYIPPDQKQDKGAPAMDSSYAKILQQQQLFLQLQILNQQQQQQQQQHYNYQAILPAPPKPSGETPGSSAPTPSRSLSTSSSSSSGTPGPGGLARQNSTALAGKPGALPANLDDMKVAELKQELKLRSLPVSGTKTELIERLRAYQDQVSPAPGAPKAPATTSVLSKAGEVVVAFPAALLSTGSALVTAGLAPAEMVVATVTSNGMVKFGSTGSTPPVSPTPSERSLLSTGDENSTPGDAFGEMVTSPLTQLTLQASPLQIVKEEGARAASCCLSPGARAELEGLDKDQMLQEKDKQIEELTRMLQQKQQLVELLRLQLEQQKRAQQPAPASSPVKRESSFSSCQLSCQPQGAARAFGPGLVVPTTNHGDAQAPAPESPPVVVKQEAGPPEPDLAPASQLLLGSQGTSFLKKVSPPTLVTDSTGTHLILTVTNKSADGPGLPTGSPQQPLSQPGSPAPGPPAQMDLEHPPQPSFATPTSLLKKEPPGYEETVTQQPKQQENGSSSQHMDDLFDILIQSGEISADFKEPPSLPGKEKSPPAEAYGPPLTPQPSPLSELPQAAPPPGSPTLPGRLEDFLESSTGLPLLTSGHEGPEPLSLIDDLHSQMLSSSAILDHPPSPMDTSELHFAPEPSSGMGLDLAVGHLDSMDWLELSSGGPVLSLAPLSTTAPSLFSMDFLDGHDLQLHWDSCL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_Q8K4J6","disprot_id":"DP01139","ncbi_taxon_id":10116,"regions_counter":18,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":160,"region_id":"DP01139r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","statement":[{"text":"The CD spectra of RPELs exhibited a strong negative band near 200 nm and a weak negative shoulder at 220 nm, which is characteristic of unfolded polypeptides. This is supported by the prediction of structural disorder by IUPred, which indicates that RPEL1(85-116), RPEL2(129-160), and RPEL3 (173-204) are disordered. The negative band near 200 nm is stronger in the order of RPEL3 > RPEL2 > RPEL1.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":129,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"24909411","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":160,"term_name":"protein binding","start":129,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"Mouilleron et al. have shown that RPEL1 and RPEL2 bind to G-actin tightly, with dissociation constants (Kd) of 1.0 and 1.9 μM, respectively. They also showed that RPEL3 binds weakly to G-actin with a Kd value of 28.9 μM, although the essential residues for the interaction with G-actin are conserved in RPEL3. From these Kd values, the Gibbs free energy changes (ΔG0) of binding are −8.2 kcal/mol, −7.8 kcal/mol, and −6.2 kcal/mol for RPEL1, RPEL2, and RPEL3, respectively. The helical propensity is higher in the order of RPEL1, RPEL2, and RPEL3. These results suggest that the amount of preformed structure may correlate with the ΔG0 value of binding. It is conceivable that the binding strength between IDP and the target molecule is modulated by the preformed structural elements in free IDP.","type":"Discussion"}],"curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"24909411","version":3,"reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","cross_refs":[{"db":"PMID","id":"19008859"}],"region_id":"DP01139r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":160,"term_name":"disorder to order","start":129,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"According to the crystal structures of RPEL1 and RPEL2 in complex with G-actin, the RPEL motif adopts two α-helices and binds to the hydrophobic cleft and the hydrophobic ledge of G-actin. The essential residues for actin binding are completely conserved between RPEL2 and RPEL3, while the essential residues are partially different between RPEL1 and RPEL2: Ile140 and Leu155 of RPEL2 are substituted with Leu and Met in RPEL1, although Leu136, Lys139, Arg143, Leu149, and Ile154 of RPEL2 are conserved in RPEL1.","type":"Discussion"}],"curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"24909411","version":2,"reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP01139r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":160,"region_id":"DP01139r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","term_id":"IDPO:0000002","curator_id":"bszabo","start":129,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"24909411","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":160,"term_name":"disorder to order","start":129,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"According to the crystal structures of RPEL1 and RPEL2 in complex with G-actin, the RPEL motif adopts two α-helices and binds to the hydrophobic cleft and the hydrophobic ledge of G-actin. The essential residues for actin binding are completely conserved between RPEL2 and RPEL3, while the essential residues are partially different between RPEL1 and RPEL2: Ile140 and Leu155 of RPEL2 are substituted with Leu and Met in RPEL1, although Leu136, Lys139, Arg143, Leu149, and Ile154 of RPEL2 are conserved in RPEL1.","type":"Discussion"}],"curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"24909411","version":2,"reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP01139r005","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":160,"term_name":"protein binding","start":129,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Mouilleron et al. have shown that RPEL1 and RPEL2 bind to G-actin tightly, with dissociation constants (Kd) of 1.0 and 1.9 μM, respectively. They also showed that RPEL3 binds weakly to G-actin with a Kd value of 28.9 μM, although the essential residues for the interaction with G-actin are conserved in RPEL3. From these Kd values, the Gibbs free energy changes (ΔG0) of binding are −8.2 kcal/mol, −7.8 kcal/mol, and −6.2 kcal/mol for RPEL1, RPEL2, and RPEL3, respectively. The helical propensity is higher in the order of RPEL1, RPEL2, and RPEL3. These results suggest that the amount of preformed structure may correlate with the ΔG0 value of binding. It is conceivable that the binding strength between IDP and the target molecule is modulated by the preformed structural elements in free IDP.","type":"Discussion"}],"curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"24909411","version":3,"reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","cross_refs":[{"db":"PMID","id":"19008859"}],"region_id":"DP01139r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":204,"region_id":"DP01139r007","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","statement":[{"text":"The CD spectra of RPELs exhibited a strong negative band near 200 nm and a weak negative shoulder at 220 nm, which is characteristic of unfolded polypeptides. This is supported by the prediction of structural disorder by IUPred, which indicates that RPEL1(85-116), RPEL2(129-160), and RPEL3 (173-204) are disordered. The negative band near 200 nm is stronger in the order of RPEL3 > RPEL2 > RPEL1.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":173,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"24909411","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":204,"term_name":"protein binding","start":173,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"Mouilleron et al. have shown that RPEL1 and RPEL2 bind to G-actin tightly, with dissociation constants (Kd) of 1.0 and 1.9 μM, respectively. They also showed that RPEL3 binds weakly to G-actin with a Kd value of 28.9 μM, although the essential residues for the interaction with G-actin are conserved in RPEL3. From these Kd values, the Gibbs free energy changes (ΔG0) of binding are −8.2 kcal/mol, −7.8 kcal/mol, and −6.2 kcal/mol for RPEL1, RPEL2, and RPEL3, respectively. The helical propensity is higher in the order of RPEL1, RPEL2, and RPEL3. These results suggest that the amount of preformed structure may correlate with the ΔG0 value of binding. It is conceivable that the binding strength between IDP and the target molecule is modulated by the preformed structural elements in free IDP.","type":"Discussion"}],"curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"24909411","version":3,"reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","cross_refs":[{"db":"PMID","id":"19008859"}],"region_id":"DP01139r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":204,"term_name":"disorder to order","start":173,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"According to the crystal structures of RPEL1 and RPEL2 in complex with G-actin, the RPEL motif adopts two α-helices and binds to the hydrophobic cleft and the hydrophobic ledge of G-actin. The essential residues for actin binding are completely conserved between RPEL2 and RPEL3, while the essential residues are partially different between RPEL1 and RPEL2: Ile140 and Leu155 of RPEL2 are substituted with Leu and Met in RPEL1, although Leu136, Lys139, Arg143, Leu149, and Ile154 of RPEL2 are conserved in RPEL1.","type":"Discussion"}],"curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"24909411","version":2,"reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP01139r009","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":204,"region_id":"DP01139r010","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","term_id":"IDPO:0000002","curator_id":"bszabo","start":173,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"24909411","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":204,"term_name":"disorder to order","start":173,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"According to the crystal structures of RPEL1 and RPEL2 in complex with G-actin, the RPEL motif adopts two α-helices and binds to the hydrophobic cleft and the hydrophobic ledge of G-actin. The essential residues for actin binding are completely conserved between RPEL2 and RPEL3, while the essential residues are partially different between RPEL1 and RPEL2: Ile140 and Leu155 of RPEL2 are substituted with Leu and Met in RPEL1, although Leu136, Lys139, Arg143, Leu149, and Ile154 of RPEL2 are conserved in RPEL1.","type":"Discussion"}],"curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"24909411","version":2,"reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP01139r011","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":204,"term_name":"protein binding","start":173,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Mouilleron et al. have shown that RPEL1 and RPEL2 bind to G-actin tightly, with dissociation constants (Kd) of 1.0 and 1.9 μM, respectively. They also showed that RPEL3 binds weakly to G-actin with a Kd value of 28.9 μM, although the essential residues for the interaction with G-actin are conserved in RPEL3. From these Kd values, the Gibbs free energy changes (ΔG0) of binding are −8.2 kcal/mol, −7.8 kcal/mol, and −6.2 kcal/mol for RPEL1, RPEL2, and RPEL3, respectively. The helical propensity is higher in the order of RPEL1, RPEL2, and RPEL3. These results suggest that the amount of preformed structure may correlate with the ΔG0 value of binding. It is conceivable that the binding strength between IDP and the target molecule is modulated by the preformed structural elements in free IDP.","type":"Discussion"}],"curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"24909411","version":3,"reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","cross_refs":[{"db":"PMID","id":"19008859"}],"region_id":"DP01139r012","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":116,"region_id":"DP01139r013","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","statement":[{"text":"The 1H-15N HSQC spectrum of RPEL1 (85-116) shows the backbone amide resonances within 8.0–8.6 ppm in the 1H dimension. The narrow chemical shift dispersion in the 1H dimension is characteristic of intrinsically disordered proteins (IDPs).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":85,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"24909411","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":116,"term_name":"disorder to order","start":85,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"According to the crystal structures of RPEL1 and RPEL2 in complex with G-actin, the RPEL motif adopts two α-helices and binds to the hydrophobic cleft and the hydrophobic ledge of G-actin. The essential residues for actin binding are completely conserved between RPEL2 and RPEL3, while the essential residues are partially different between RPEL1 and RPEL2: Ile140 and Leu155 of RPEL2 are substituted with Leu and Met in RPEL1, although Leu136, Lys139, Arg143, Leu149, and Ile154 of RPEL2 are conserved in RPEL1.","type":"Discussion"}],"curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"24909411","version":2,"reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP01139r014","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":116,"term_name":"protein binding","start":85,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Mouilleron et al. have shown that RPEL1 and RPEL2 bind to G-actin tightly, with dissociation constants (Kd) of 1.0 and 1.9 μM, respectively. They also showed that RPEL3 binds weakly to G-actin with a Kd value of 28.9 μM, although the essential residues for the interaction with G-actin are conserved in RPEL3. From these Kd values, the Gibbs free energy changes (ΔG0) of binding are −8.2 kcal/mol, −7.8 kcal/mol, and −6.2 kcal/mol for RPEL1, RPEL2, and RPEL3, respectively. The helical propensity is higher in the order of RPEL1, RPEL2, and RPEL3. These results suggest that the amount of preformed structure may correlate with the ΔG0 value of binding. It is conceivable that the binding strength between IDP and the target molecule is modulated by the preformed structural elements in free IDP.","type":"Discussion"}],"curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"24909411","version":3,"reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","cross_refs":[{"db":"PMID","id":"19008859"}],"region_id":"DP01139r015","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":116,"region_id":"DP01139r016","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","statement":[{"text":"The CD spectra of RPELs exhibited a strong negative band near 200 nm and a weak negative shoulder at 220 nm, which is characteristic of unfolded polypeptides. This is supported by the prediction of structural disorder by IUPred, which indicates that RPEL1(85-116), RPEL2(129-160), and RPEL3 (173-204) are disordered. The negative band near 200 nm is stronger in the order of RPEL3 > RPEL2 > RPEL1.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":85,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"24909411","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":116,"term_name":"disorder to order","start":85,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"According to the crystal structures of RPEL1 and RPEL2 in complex with G-actin, the RPEL motif adopts two α-helices and binds to the hydrophobic cleft and the hydrophobic ledge of G-actin. The essential residues for actin binding are completely conserved between RPEL2 and RPEL3, while the essential residues are partially different between RPEL1 and RPEL2: Ile140 and Leu155 of RPEL2 are substituted with Leu and Met in RPEL1, although Leu136, Lys139, Arg143, Leu149, and Ile154 of RPEL2 are conserved in RPEL1.","type":"Discussion"}],"curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"24909411","version":2,"reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP01139r017","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":116,"term_name":"protein binding","start":85,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"Mouilleron et al. have shown that RPEL1 and RPEL2 bind to G-actin tightly, with dissociation constants (Kd) of 1.0 and 1.9 μM, respectively. They also showed that RPEL3 binds weakly to G-actin with a Kd value of 28.9 μM, although the essential residues for the interaction with G-actin are conserved in RPEL3. From these Kd values, the Gibbs free energy changes (ΔG0) of binding are −8.2 kcal/mol, −7.8 kcal/mol, and −6.2 kcal/mol for RPEL1, RPEL2, and RPEL3, respectively. The helical propensity is higher in the order of RPEL1, RPEL2, and RPEL3. These results suggest that the amount of preformed structure may correlate with the ΔG0 value of binding. It is conceivable that the binding strength between IDP and the target molecule is modulated by the preformed structural elements in free IDP.","type":"Discussion"}],"curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"24909411","version":3,"reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","cross_refs":[{"db":"PMID","id":"19008859"}],"region_id":"DP01139r018","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_A0A0G2JXC5","date":"2018-06-25T13:24:38.000Z","acc":"A0A0G2JXC5","name":"Myocardin-related transcription factor A","length":1038,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI0003D0C60C","genes":[{"name":{"value":"Mrtfa","evidences":[{"code":"ECO:0000313","source":{"name":"Ensembl","id":"ENSRNOP00000070219","url":"https://www.ensembl.org/id/ENSRNOP00000070219"}},{"code":"ECO:0000313","source":{"name":"RGD","id":"1304873","url":"https://rgd.mcw.edu/tools/genes/genes_view.cgi?id=1304873"}}]},"synonyms":[{"value":"Mkl1","evidences":[{"code":"ECO:0000313","source":{"name":"RGD","id":"1304873","url":"https://rgd.mcw.edu/tools/genes/genes_view.cgi?id=1304873"}}]}]}],"alphafold_very_low_content":0.6483622350674374,"disorder_content":0.09248554913294797,"disprot_consensus":{"full":[{"start":85,"end":116,"type":"T"},{"start":129,"end":160,"type":"T"},{"start":173,"end":204,"type":"T"}],"Structural state":[{"start":85,"end":116,"type":"D"},{"start":129,"end":160,"type":"D"},{"start":173,"end":204,"type":"D"}],"Molecular function":[{"start":85,"end":116,"type":"F"},{"start":129,"end":160,"type":"F"},{"start":173,"end":204,"type":"F"}],"Structural transition":[{"start":85,"end":116,"type":"T"},{"start":129,"end":160,"type":"T"},{"start":173,"end":204,"type":"T"}]}},{"features":{"pfam":[{"id":"PF05348","name":"Proteasome maturation factor UMP1","start":25,"end":146}]},"uniref50":"UniRef50_P38293","sequence":"MNIVPQDTFKSQVSTDQDKSVLSSAVPSLPDTLRQQEGGAVPLSTQLNDRHPLESTLKNWETTQRQRQMEQYRQIFGIAEPMKRTMEMEIVNRTDFNPLSTNGSIHRDILLNKECSIDWEDVYPGTGLQASTMVGDDVHSKIEKQLGI","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P38293","disprot_id":"DP01140","ncbi_taxon_id":559292,"regions_counter":5,"creator":"smribeiro","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":148,"region_id":"DP01140r001","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Biochemical and biophysical characterization of recombinant yeast proteasome maturation factor ump1. <i> Sá-Moura B, Simões AM, Fraga J, Fernandes H, Abreu IA, Botelho HM, Gomes CM, Marques AJ, Dohmen RJ, Ramos PC, Macedo-Ribeiro S. </i> Comput Struct Biotechnol J, 2013","statement":[{"text":"The logarithmic plot of these calculated Rs values versus the molecular masses of the corresponding monomeric and dimeric Ump1 variants indicates that these proteins do not behave as natively folded globular proteins in solution, and fall very close to the plot representing the behaviour of molecules with a natively unfolded molten globule conformation","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"smribeiro","start":1,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"chromatography evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24688736","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":148,"region_id":"DP01140r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Biochemical and biophysical characterization of recombinant yeast proteasome maturation factor ump1. <i> Sá-Moura B, Simões AM, Fraga J, Fernandes H, Abreu IA, Botelho HM, Gomes CM, Marques AJ, Dohmen RJ, Ramos PC, Macedo-Ribeiro S. </i> Comput Struct Biotechnol J, 2013","statement":[{"text":"The CD spectra for all proteins (monomeric and dimeric wild-type Ump1, as well as Ump1-C115S mutant) exhibit isodichroic curves, with a minimum at 201 nm and a shoulder around 222 nm.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"smribeiro","start":1,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24688736","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":148,"region_id":"DP01140r003","released":"2022_03","ec_id":"ECO:0006317","reference_html":"Biochemical and biophysical characterization of recombinant yeast proteasome maturation factor ump1. <i> Sá-Moura B, Simões AM, Fraga J, Fernandes H, Abreu IA, Botelho HM, Gomes CM, Marques AJ, Dohmen RJ, Ramos PC, Macedo-Ribeiro S. </i> Comput Struct Biotechnol J, 2013","statement":[{"text":"all preparations of wild-type Ump1 exhibit a very gradual – and almost constant – CD signal variation with temperature, from 25 to 90°C. This is unlike the typical behaviour of small, single domain folded globular proteins, where the unfolding is highly cooperative and occurs in a very narrow temperature range. Also, even at 90°C, Ump1 does not seem to be fully denatured...","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"smribeiro","start":1,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24688736","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":84,"region_id":"DP01140r004","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Biochemical and biophysical characterization of recombinant yeast proteasome maturation factor ump1. <i> Sá-Moura B, Simões AM, Fraga J, Fernandes H, Abreu IA, Botelho HM, Gomes CM, Marques AJ, Dohmen RJ, Ramos PC, Macedo-Ribeiro S. </i> Comput Struct Biotechnol J, 2013","statement":[{"text":"The CD spectra from this Ump1 N-terminal proteolytic fragment confirm that, in accordance with the theoretical disorder predictions (Figure 2 and S2), the N-terminal region is largely unstructured (Figure 5).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"smribeiro","start":1,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24688736","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":148,"region_id":"DP01140r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Backbone ¹H, ¹³C and ¹⁵N assignments of yeast Ump1, an intrinsically disordered protein that functions as a proteasome assembly chaperone. <i> Uekusa Y, Okawa K, Yagi-Utsumi M, Serve O, Nakagawa Y, Mizushima T, Yagi H, Saeki Y, Tanaka K, Kato K. </i> Biomol NMR Assign, 2014","statement":[{"text":"Backbone chemical shift data indicated that Ump1 is an intrinsically unstructured protein and largely devoid of secondary structural elements.","type":"Abstract"},{"text":"Figure 1 shows the 1H–15N HSQC spectrum of Ump1 recorded at 30 °C. The HSQC peaks were observed within a narrow spectral region (7.3–8.5 ppm for the 1H chemical shifts), which indicated that Ump1 was largely unstructured in solution.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24065419","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P38293","date":"2018-06-25T13:40:57.000Z","acc":"P38293","name":"Proteasome maturation factor UMP1","length":148,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000137C2C","genes":[{"name":{"value":"UMP1"},"orfNames":[{"value":"YBR1234"}],"olnNames":[{"value":"YBR173C"}]}],"alphafold_very_low_content":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":148,"type":"D"}],"Structural state":[{"start":1,"end":148,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02888","name":"Calmodulin binding domain","start":403,"end":518},{"id":"PF03530","name":"Calcium-activated SK potassium channel","start":122,"end":236},{"id":"PF07885","name":"Ion channel","start":320,"end":398}],"gene3D":[{"start":299,"end":398,"id":"1.10.287.70","name":"1.10.287.70"},{"start":399,"end":494,"id":"1.10.287.70","name":"1.10.287.70"}]},"uniref50":"UniRef50_P70604","sequence":"MSSCRYNGGVMRPLSNLSSSRRNLHEMDSEAQPLQPPASVVGGGGGASSPSAAAAASSSAPEIVVSKPEHNNSNNLALYGTGGGGSTGGGGGGGGGGGGSGHGSSSGTKSSKKKNQNIGYKLGHRRALFEKRKRLSDYALIFGMFGIVVMVIETELSWGAYDKASLYSLALKCLISLSTIILLGLIIVYHAREIQLFMVDNGADDWRIAMTYERIFFICLEILVCAIHPIPGNYTFTWTARLAFSYAPSTTTADVDIILSIPMFLRLYLIARVMLLHSKLFTDASSRSIGALNKINFNTRFVMKTLMTICPGTVLLVFSISLWIIAAWTVRACERYHDQQDVTSNFLGAMWLISITFLSIGYGDMVPNTYCGKGVCLLTGIMGAGCTALVVAVVARKLELTKAEKHVHNFMMDTQLTKRVKNAAANVLRETWLIYKNTKLVKKIDHAKVRKHQRKFLQAIHQLRSVKMEQRKLNDQANTLVDLAKTQNIMYDMISDLNERSEDFEKRIVTLETKLETLIGSIHALPGLISQTIRQQQRDFIETQMENYDKHVTYNAERSRSSSRRRRSSSTAPPTSSESS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_P70604","disprot_id":"DP01141","ncbi_taxon_id":10116,"regions_counter":4,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":424,"region_id":"DP01141r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A helical region in the C terminus of small-conductance Ca2+-activated K+ channels controls assembly with apo-calmodulin. <i> Wissmann R, Bildl W, Neumann H, Rivard AF, Klöcker N, Weitz D, Schulte U, Adelman JP, Bentrop D, Fakler B. </i> J Biol Chem, 2002","statement":[{"text":"Positive NOE values indicative for increased rigidity were observed for residues between Ala-425 and Tyr-435, while negative values were obtained outside this region. Together, the NOE pattern and the results from dynamic measurements suggested that CaMBD consists of an ordered most likely helical core region flanked by flexible N and C termini.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":396,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1KKD"}],"reference_id":"11723128","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P0DP29","partner_end":null}],"ec_ontology":"ECO","end":424,"term_name":"protein binding","start":396,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11723128","statement":[{"text":"Both types of interactions with CaM require a domain of about 90 amino acids in the proximal C terminus of the channel subunit, the calmodulin binding domain (CaMBD). As long as the CaMBD is present at the C terminus of the SK α-subunit, channels exhibit regular Ca2+-gating; deletions of more than 10 residues resulted in channels that were no longer gated by intracellular Ca2+.","type":"Introduction"}],"reference_html":"A helical region in the C terminus of small-conductance Ca2+-activated K+ channels controls assembly with apo-calmodulin. <i> Wissmann R, Bildl W, Neumann H, Rivard AF, Klöcker N, Weitz D, Schulte U, Adelman JP, Bentrop D, Fakler B. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","version":4,"region_id":"DP01141r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":487,"region_id":"DP01141r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A helical region in the C terminus of small-conductance Ca2+-activated K+ channels controls assembly with apo-calmodulin. <i> Wissmann R, Bildl W, Neumann H, Rivard AF, Klöcker N, Weitz D, Schulte U, Adelman JP, Bentrop D, Fakler B. </i> J Biol Chem, 2002","statement":[{"text":"Positive NOE values indicative for increased rigidity were observed for residues between Ala-30 and Tyr-40, while negative values were obtained outside this region. Together, the NOE pattern and the results from dynamic measurements suggested that CaMBD consists of an ordered most likely helical core region flanked by flexible N and C termini.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":436,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1KKD"}],"reference_id":"11723128","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P0DP29","partner_end":null}],"ec_ontology":"ECO","end":487,"term_name":"protein binding","start":436,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11723128","statement":[{"text":"Both types of interactions with CaM require a domain of about 90 amino acids in the proximal C terminus of the channel subunit, the calmodulin binding domain (CaMBD). As long as the CaMBD is present at the C terminus of the SK α-subunit, channels exhibit regular Ca2+-gating; deletions of more than 10 residues resulted in channels that were no longer gated by intracellular Ca2+.","type":"Introduction"}],"reference_html":"A helical region in the C terminus of small-conductance Ca2+-activated K+ channels controls assembly with apo-calmodulin. <i> Wissmann R, Bildl W, Neumann H, Rivard AF, Klöcker N, Weitz D, Schulte U, Adelman JP, Bentrop D, Fakler B. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","version":4,"region_id":"DP01141r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P70604","date":"2018-06-25T14:38:26.000Z","acc":"P70604","name":"Small conductance calcium-activated potassium channel protein 2","length":580,"organism":"Rattus norvegicus","dataset":["Autophagy-related proteins"],"UniParc":"UPI0000049EE4","genes":[{"name":{"value":"Kcnn2"}}],"alphafold_very_low_content":0.22241379310344828,"disorder_content":0.1396551724137931,"disprot_consensus":{"full":[{"start":396,"end":424,"type":"D"},{"start":436,"end":487,"type":"D"}],"Structural state":[{"start":396,"end":424,"type":"D"},{"start":436,"end":487,"type":"D"}],"Molecular function":[{"start":396,"end":424,"type":"F"},{"start":436,"end":487,"type":"F"}]}},{"acc":"O92972","sequence":"MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKASERSQPRGRRQPIPKARRPEGRAWAQPGYPWPLYGNEGLGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLALLSCLTIPASAYEVRNVSGIYHVTNDCSNSSIVYEAADVIMHTPGCVPCVREGNSSRCWVALTPTLAARNASVPTTTIRRHVDLLVGTAAFCSAMYVGDLCGSIFLVSQLFTFSPRRHETVQDCNCSIYPGHVSGHRMAWDMMMNWSPTTALVVSQLLRIPQAVVDMVAGAHWGVLAGLAYYSMVGNWAKVLIVALLFAGVDGETHTTGRVAGHTTSGFTSLFSSGASQKIQLVNTNGSWHINRTALNCNDSLQTGFFAALFYAHKFNSSGCPERMASCRPIDWFAQGWGPITYTKPNSSDQRPYCWHYAPRPCGVVPASQVCGPVYCFTPSPVVVGTTDRSGVPTYSWGENETDVMLLNNTRPPQGNWFGCTWMNSTGFTKTCGGPPCNIGGVGNRTLICPTDCFRKHPEATYTKCGSGPWLTPRCLVDYPYRLWHYPCTLNFSIFKVRMYVGGVEHRLNAACNWTRGERCNLEDRDRSELSPLLLSTTEWQILPCAFTTLPALSTGLIHLHQNIVDVQYLYGVGSAFVSFAIKWEYILLLFLLLADARVCACLWMMLLIAQAEAALENLVVLNAASVAGAHGILSFLVFFCAAWYIKGRLAPGAAYAFYGVWPLLLLLLALPPRAYALDREMAASCGGAVLVGLVFLTLSPYYKVFLTRLIWWLQYFITRAEAHMQVWVPPLNVRGGRDAIILLTCAVHPELIFDITKLLLAILGPLMVLQAGITRVPYFVRAQGLIRACMLVRKVAGGHYVQMAFMKLGALTGTYVYNHLTPLRDWAHAGLRDLAVAVEPVVFSAMETKVITWGADTAACGDIILGLPVSARRGKEIFLGPADSLEGQGWRLLAPITAYSQQTRGVLGCIITSLTGRDKNQVEGEVQVVSTATQSFLATCINGVCWTVYHGAGSKTLAGPKGPITQMYTNVDLDLVGWQAPPGARSMTPCSCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPVSYLKGSSGGPLLCPSGHVVGVFRAAVCTRGVAKAVDFIPVESMETTMRSPVFTDNSSPPAVPQTFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIDPNIRTGVRTITTGGSITYSTYGKFLADGGCSGGAYDIIICDECHSTDSTTILGIGTVLDQAETAGARLVVLATATPPGSVTVPHPNIEEIGLSNNGEIPFYGKAIPIEAIKGGRHLIFCHSKKKCDELAAKLTGLGLNAVAYYRGLDVSVIPPIGDVVVVATDALMTGFTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTVPQDAVSRSQRRGRTGRGRSGIYRFVTPGERPSGMFDSSVLCECYDAGCAWYELTPAETSVRLRAYLNTPGLPVCQDHLEFWESVFTGLTHIDAHFLSQTKQAGDNFPYLVAYQATVCARAQAPPPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEVILTHPITKYIMACMSADLEVVTSTWVLVGGVLAALAAYCLTTGSVVIVGRIILSGKPAVVPDREVLYQEFDEMEECASQLPYIEQGMQLAEQFKQKALGLLQTATKQAEAAAPVVESKWRALETFWAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTASITSPLTTQNTLLFNILGGWVAAQLAPPSAASAFVGAGIAGAAVGSIGLGKVLVDILAGYGAGVAGALVAFKVMSGEVPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLIAFASRGNHVSPTHYVPESDAAARVTQILSSLTITQLLKRLHQWINEDCSTPCSGSWLRDVWDWICTVLTDFKTWLQSKLLPRLPGVPFLSCQRGYKGVWRGDGIMQTTCPCGAQIAGHVKNGSMRIVGPRTCSNTWHGTFPINAYTTGPCTPSPAPNYSRALWRVAAEEYVEVTRVGDFHYVTGMTTDNVKCPCQVPAPEFFTEVDGVRLHRYAPACKPLLREDVTFQVGLNQYLVGSQLPCEPEPDVTVLTSMLTDPSHITAETAKRRLARGSPPSLASSSASQLSAPSLKATCTTHHDSPDADLIEANLLWRQEMGGNITRVESENKVVILDSFEPLHAEGDEREISVAAEILRKSRKFPSALPIWARPDYNPPLLESWKDPDYVPPVVHGCPLPPTKAPPIPPPRRKRTVVLTESNVSSALAELATKTFGSSGSSAVDSGTATALPDLASDDGDKGSDVESYSSMPPLEGEPGDPDLSDGSWSTVSEEASEDVVCCSMSYTWTGALITPCAAEESKLPINPLSNSLLRHHNMVYATTSRSASLRQKKVTFDRLQVLDDHYRDVLKEMKAKASTVKAKLLSIEEACKLTPPHSAKSKFGYGAKDVRNLSSRAVNHIRSVWEDLLEDTETPIDTTIMAKSEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVSTLPQAVMGSSYGFQYSPKQRVEFLVNTWKSKKCPMGFSYDTRCFDSTVTESDIRVEESIYQCCDLAPEARQAIRSLTERLYIGGPLTNSKGQNCGYRRCRASGVLTTSCGNTLTCYLKATAACRAAKLQDCTMLVNGDDLVVICESAGTQEDAAALRAFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDASGKRVYYLTRDPTTPLARAAWETARHTPINSWLGNIIMYAPTLWARMILMTHFFSILLAQEQLEKALDCQIYGACYSIEPLDLPQIIERLHGLSAFTLHSYSPGEINRVASCLRKLGVPPLRTWRHRARSVRAKLLSQGGRAATCGRYLFNWAVRTKLKLTPIPAASQLDLSGWFVAGYSGGDIYHSLSRARPRWFPLCLLLLSVGVGIYLLPNR","creator":"jmanso","dataset":["Viral proteins","RNA-binding proteins"],"date":"2018-06-25T16:54:12.000Z","disprot_id":"DP01142","features":{"pfam":[{"id":"PF00998","name":"Viral RNA dependent RNA polymerase","start":2422,"end":2932},{"id":"PF01001","name":"Hepatitis C virus non-structural protein NS4b","start":1728,"end":1921},{"id":"PF01006","name":"Hepatitis C virus non-structural protein NS4a","start":1658,"end":1711},{"id":"PF01506","name":"Hepatitis C virus non-structural 5a protein membrane anchor","start":1974,"end":1996},{"id":"PF01538","name":"Hepatitis C virus non-structural protein NS2","start":811,"end":1005},{"id":"PF01539","name":"Hepatitis C virus envelope glycoprotein E1","start":193,"end":382},{"id":"PF01542","name":"Hepatitis C virus core protein","start":116,"end":190},{"id":"PF01543","name":"Hepatitis C virus capsid protein","start":2,"end":115},{"id":"PF01560","name":"Hepatitis C virus non-structural protein E2/NS1","start":386,"end":729},{"id":"PF02907","name":"Hepatitis C virus NS3 protease","start":1056,"end":1203},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1294,"end":1355},{"id":"PF08300","name":"Hepatitis C virus non-structural 5a zinc finger domain","start":2006,"end":2067},{"id":"PF08301","name":"Hepatitis C virus non-structural 5a domain 1b","start":2068,"end":2168},{"id":"PF12941","name":"HCV NS5a protein C-terminal region","start":2179,"end":2419},{"id":"PF22027","name":"NS3 RNA helicase, C-terminal helical domain","start":1516,"end":1656}],"gene3D":[{"start":994,"end":1021,"id":"2.30.30.710","name":"Hepatitis C virus non-structural protein NS2, C-terminal domain","_id":"685af523b4ac24d5329d8d2c"},{"start":2014,"end":2074,"id":"2.20.25.210","name":"Hepatitis C NS5A, domain 1B","_id":"685af523b4ac24d5329d8d2d"},{"start":2075,"end":2160,"id":"2.20.25.220","name":"Hepatitis C virus NS5A, 1B domain","_id":"685af523b4ac24d5329d8d2e"},{"start":900,"end":977,"id":"1.20.1280.150","name":"Hepatitis C virus non-structural protein NS2, N-terminal domain","_id":"685af523b4ac24d5329d8d2f"},{"start":1513,"end":1641,"id":"1.10.820.10","name":"RNA Helicase Chain A , domain 3","_id":"685af523b4ac24d5329d8d30"},{"start":206,"end":275,"id":"2.30.30.1080","name":"Hepatitis C virus envelope glycoprotein E1, chain C","_id":"685af523b4ac24d5329d8d31"},{"start":2607,"end":2663,"id":"3.30.70.270","name":"3.30.70.270","_id":"685af523b4ac24d5329d8d32"},{"start":2,"end":45,"id":"4.10.710.10","name":"Hepatitis C Virus Capsid Protein; Chain A","_id":"685af523b4ac24d5329d8d33"},{"start":1122,"end":1205,"id":"2.40.10.10","name":"Trypsin-like serine proteases","_id":"685af523b4ac24d5329d8d34"},{"start":1022,"end":1120,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d8d35"},{"start":1355,"end":1512,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d8d36"},{"start":1206,"end":1354,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d8d37"}]},"genes":[],"length":3010,"name":"Genome polyprotein","ncbi_taxon_id":420174,"organism":"Hepatitis C virus genotype 1b (strain HC-J4)","regions_counter":27,"released":"2018_11","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Hepacivirus"],"UniParc":"UPI0000F0A5B5","uniref100":"UniRef100_O92972","uniref50":"UniRef50_P27958","uniref90":"UniRef90_P26662","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2314,"end":2338,"interaction_partner":[{"db":"UniProt","id":"O00499","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8d44"}],"reference_html":"Transient structure and SH3 interaction sites in an intrinsically disordered fragment of the hepatitis C virus protein NS5A. <i> Feuerstein S, Solyom Z, Aladag A, Favier A, Schwarten M, Hoffmann S, Willbold D, Brutscher B. </i> J Mol Biol, 2012","reference_id":"22543239","region_id":"DP01142r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Adding a small amount of Bin1–SH3 (molar ratio of 5:1) only affects the line widths and chemical shifts of amide resonances in the region 342 to 366 (Fig. 4a) comprising three canonical SH3 binding sites (PPII helix motifs): one of class I [PP1.2 (348–354)] and two of class II [PP2.1 (343–348) and PP2.2 (351–356)] (Fig. 4c).","_id":"685af523b4ac24d5329d8d42"},{"type":"Curator statement","text":"Residues 342-366 of the nonstructural protein 5A (NS5A) from Hepatitis C virus genotype 1b (strain HC-J4) corresponds to 2314-2338 residues of the polyprotein.","_id":"685af523b4ac24d5329d8d43"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T14:15:10.360Z","_id":"685af523b4ac24d5329d8d45"},"version":1,"_id":"685af523b4ac24d5329d8d41","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":2163,"end":2341,"interaction_partner":[],"reference_html":"Transient structure and SH3 interaction sites in an intrinsically disordered fragment of the hepatitis C virus protein NS5A. <i> Feuerstein S, Solyom Z, Aladag A, Favier A, Schwarten M, Hoffmann S, Willbold D, Brutscher B. </i> J Mol Biol, 2012","reference_id":"22543239","region_id":"DP01142r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The Kratky representation of these data, shown in Fig. 3d, is characteristic of a highly disordered protein. Nevertheless, a small bump observed in this scattering curve (at s ≈ 0.7) is indicative of a certain degree of compactness.","_id":"685af523b4ac24d5329d8d47"},{"type":"Results","text":"For most residues, the absolute values of these secondary chemical shifts are below 1.0 to 1.5 ppm, indicating the absence of any persistent secondary structure in this protein fragment consistent with an IDP.","_id":"685af523b4ac24d5329d8d48"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T14:06:41.224Z","_id":"685af523b4ac24d5329d8d49"},"version":1,"_id":"685af523b4ac24d5329d8d46","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001269","ec_name":"surface plasmon resonance evidence used in manual assertion","ec_ontology":"ECO","start":2305,"end":2341,"interaction_partner":[{"db":"UniProt","id":"O00499","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8d4b"}],"reference_html":"Transient structure and SH3 interaction sites in an intrinsically disordered fragment of the hepatitis C virus protein NS5A. <i> Feuerstein S, Solyom Z, Aladag A, Favier A, Schwarten M, Hoffmann S, Willbold D, Brutscher B. </i> J Mol Biol, 2012","reference_id":"22543239","region_id":"DP01142r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"This refers to a macroscopic system with a high binding affinity of the two proteins, consistent with a Kd of 0.1 μM measured by surface plasmon resonance for a short NS5A(333–369) fragment that comprises the entire poly-proline rich region (Fig. S6).","_id":"685af523b4ac24d5329d8d4c"},{"type":"Curator statement","text":"Residues 333-369 of the nonstructural protein 5A (NS5A) from Hepatitis C virus genotype 1b (strain HC-J4) corresponds to 2305-2341 residues of the polyprotein.","_id":"685af523b4ac24d5329d8d4d"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T14:15:08.284Z","_id":"685af523b4ac24d5329d8d4e"},"version":1,"_id":"685af523b4ac24d5329d8d4a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2172,"end":2200,"interaction_partner":[{"db":"UniProt","id":"O00499","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8d57"}],"reference_html":"Interaction of nonstructural protein 5A of the hepatitis C virus with Src homology 3 domains using noncanonical binding sites. <i> Schwarten M, Sólyom Z, Feuerstein S, Aladağ A, Hoffmann S, Willbold D, Brutscher B. </i> Biochemistry, 2013","reference_id":"23947833","region_id":"DP01142r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Upon addition of SH3 at concentrations higher than the equimolar concentration, chemical shift changes were observed for NS5A residues 200–228 (binding site B1) and 295–320 (binding site B2).","_id":"685af523b4ac24d5329d8d58"},{"type":"Curator statement","text":"Residues 200-228 (B1) of the nonstructural protein 5A (NS5A) from Hepatitis C virus genotype 1b (strain HC-J4) corresponds to 2172-2200 residues of the polyprotein.","_id":"685af523b4ac24d5329d8d59"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T14:15:02.784Z","_id":"685af523b4ac24d5329d8d5a"},"version":1,"_id":"685af523b4ac24d5329d8d56","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2267,"end":2292,"interaction_partner":[{"db":"UniProt","id":"O00499","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8d5c"}],"reference_html":"Interaction of nonstructural protein 5A of the hepatitis C virus with Src homology 3 domains using noncanonical binding sites. <i> Schwarten M, Sólyom Z, Feuerstein S, Aladağ A, Hoffmann S, Willbold D, Brutscher B. </i> Biochemistry, 2013","reference_id":"23947833","region_id":"DP01142r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Upon addition of SH3 at concentrations higher than the equimolar concentration, chemical shift changes were observed for NS5A residues 200–228 (binding site B1) and 295–320 (binding site B2).","_id":"685af523b4ac24d5329d8d5d"},{"type":"Discussion","text":"Here we have shown that NS5A interacts with SH3 domains via three distinct binding regions, with one (B3) corresponding to the canonical PxxP motif and the other two (B1 and B2) not containing such a canonical SH3 recognition element.","_id":"685af523b4ac24d5329d8d5e"},{"type":"Curator statement","text":"Residues 295-320 (B2) of the nonstructural protein 5A (NS5A) from Hepatitis C virus genotype 1b (strain HC-J4) corresponds to 2267-2292 residues of the polyprotein.","_id":"685af523b4ac24d5329d8d5f"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T14:14:59.719Z","_id":"685af523b4ac24d5329d8d60"},"version":1,"_id":"685af523b4ac24d5329d8d5b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2163,"end":2312,"interaction_partner":[{"db":"UniProt","id":"O00499","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8d70"}],"reference_html":"Interaction of nonstructural protein 5A of the hepatitis C virus with Src homology 3 domains using noncanonical binding sites. <i> Schwarten M, Sólyom Z, Feuerstein S, Aladağ A, Hoffmann S, Willbold D, Brutscher B. </i> Biochemistry, 2013","reference_id":"23947833","region_id":"DP01142r014","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In the following, we will focus on the interaction of NS5A(191–340) with the Bin1-SH3 domain that induces the largest chemical shift changes in the NS5A spectrum. A very similar pattern of chemical shift changes and line broadening was observed in NMR titration experiments (Figure 3B) as shown in Figure 2B for the longer NS5A construct, indicating that the observed perturbation is due to direct SH3 binding events, and not to conformational changes induced by the high-affinity interaction of the SH3 domain with the PxxP motif of NS5A.","_id":"685af523b4ac24d5329d8d71"},{"type":"Curator statement","text":"Residues 191-340 of the truncated nonstructural protein 5A (NS5A) from Hepatitis C virus genotype 1b (strain HC-J4) corresponds to 2163-2312 residues of the polyprotein.","_id":"685af523b4ac24d5329d8d72"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T14:08:40.537Z","_id":"685af523b4ac24d5329d8d73"},"version":1,"_id":"685af523b4ac24d5329d8d6f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2314,"end":2340,"interaction_partner":[{"db":"UniProt","id":"O00499","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8d75"}],"reference_html":"Interaction of nonstructural protein 5A of the hepatitis C virus with Src homology 3 domains using noncanonical binding sites. <i> Schwarten M, Sólyom Z, Feuerstein S, Aladağ A, Hoffmann S, Willbold D, Brutscher B. </i> Biochemistry, 2013","reference_id":"23947833","region_id":"DP01142r015","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Besides the interaction with SH3 domains mediated by a canonical PxxP motif located in the LCS-2 region of NS5A (binding site B3), we were able to identify two additional peptide regions in NS5A that interact with the four SH3 domains mentioned above (Figure 2B).","_id":"685af523b4ac24d5329d8d76"},{"type":"Figure","text":"For a NS5A:SH3 ratio of 1:1 (yellow), chemical shift changes can mainly be detected close to the PxxP motifs.","_id":"685af523b4ac24d5329d8d77"},{"type":"Discussion","text":"Here we have shown that NS5A interacts with SH3 domains via three distinct binding regions, with one (B3) corresponding to the canonical PxxP motif and the other two (B1 and B2) not containing such a canonical SH3 recognition element.","_id":"685af523b4ac24d5329d8d78"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T14:08:11.067Z","_id":"685af523b4ac24d5329d8d79"},"version":1,"_id":"685af523b4ac24d5329d8d74","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2163,"end":2341,"interaction_partner":[],"reference_html":"Interaction of nonstructural protein 5A of the hepatitis C virus with Src homology 3 domains using noncanonical binding sites. <i> Schwarten M, Sólyom Z, Feuerstein S, Aladağ A, Hoffmann S, Willbold D, Brutscher B. </i> Biochemistry, 2013","reference_id":"23947833","region_id":"DP01142r019","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"More surprisingly, the hetNOE values of NS5A residues in the binding regions decrease upon interaction with SH3, in agreement with a more flexible structural ensemble. The interaction of NS5A with Bin1-SH3 via low-affinity binding sites B1 and B2 thus adds another example of a “fuzzy” complex(34-36) formed between a globular protein domain and an intrinsically disordered protein (IDP).","_id":"685af523b4ac24d5329d8d84"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T14:06:40.141Z","_id":"685af523b4ac24d5329d8d85"},"version":1,"_id":"685af523b4ac24d5329d8d83","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2163,"end":2341,"interaction_partner":[{"db":"UniProt","id":"O00499","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8d87"}],"reference_html":"Transient structure and SH3 interaction sites in an intrinsically disordered fragment of the hepatitis C virus protein NS5A. <i> Feuerstein S, Solyom Z, Aladag A, Favier A, Schwarten M, Hoffmann S, Willbold D, Brutscher B. </i> J Mol Biol, 2012","reference_id":"22543239","region_id":"DP01142r020","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Consequently, at an equimolar mixture of the two proteins at 100 μM concentration, this high-affinity NS5A(191–369) binding site is saturated, and only peaks from the bound state were observable in the NMR spectra.","_id":"685af523b4ac24d5329d8d88"},{"type":"Curator statement","text":"Residues 191-369 of the nonstructural protein 5A (NS5A) from Hepatitis C virus genotype 1b (strain HC-J4) corresponds to 2163-2341 residues of the polyprotein.","_id":"685af523b4ac24d5329d8d89"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T14:08:04.553Z","_id":"685af523b4ac24d5329d8d8a"},"version":1,"_id":"685af523b4ac24d5329d8d86","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2314,"end":2340,"interaction_partner":[],"reference_html":"Interaction of nonstructural protein 5A of the hepatitis C virus with Src homology 3 domains using noncanonical binding sites. <i> Schwarten M, Sólyom Z, Feuerstein S, Aladağ A, Hoffmann S, Willbold D, Brutscher B. </i> Biochemistry, 2013","reference_id":"23947833","region_id":"DP01142r021","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Besides the interaction with SH3 domains mediated by a canonical PxxP motif located in the LCS-2 region of NS5A (binding site B3), we were able to identify two additional peptide regions in NS5A that interact with the four SH3 domains mentioned above (Figure 2B).","_id":"685af523b4ac24d5329d8d8c"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T14:20:09.993Z","_id":"685af523b4ac24d5329d8d8d"},"version":1,"_id":"685af523b4ac24d5329d8d8b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2163,"end":2312,"interaction_partner":[],"reference_html":"Interaction of nonstructural protein 5A of the hepatitis C virus with Src homology 3 domains using noncanonical binding sites. <i> Schwarten M, Sólyom Z, Feuerstein S, Aladağ A, Hoffmann S, Willbold D, Brutscher B. </i> Biochemistry, 2013","reference_id":"23947833","region_id":"DP01142r022","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In the following, we will focus on the interaction of NS5A(191–340) with the Bin1-SH3 domain that induces the largest chemical shift changes in the NS5A spectrum. A very similar pattern of chemical shift changes and line broadening was observed in NMR titration experiments (Figure 3B) as shown in Figure 2B for the longer NS5A construct, indicating that the observed perturbation is due to direct SH3 binding events, and not to conformational changes induced by the high-affinity interaction of the SH3 domain with the PxxP motif of NS5A.","_id":"685af523b4ac24d5329d8d8f"},{"type":"Curator statement","text":"Residues 191-340 of the truncated nonstructural protein 5A (NS5A) from Hepatitis C virus genotype 1b (strain HC-J4) corresponds to 2163-2312 residues of the polyprotein.","_id":"685af523b4ac24d5329d8d90"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T14:20:11.098Z","_id":"685af523b4ac24d5329d8d91"},"version":1,"_id":"685af523b4ac24d5329d8d8e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2267,"end":2292,"interaction_partner":[],"reference_html":"Interaction of nonstructural protein 5A of the hepatitis C virus with Src homology 3 domains using noncanonical binding sites. <i> Schwarten M, Sólyom Z, Feuerstein S, Aladağ A, Hoffmann S, Willbold D, Brutscher B. </i> Biochemistry, 2013","reference_id":"23947833","region_id":"DP01142r023","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"Here we have shown that NS5A interacts with SH3 domains via three distinct binding regions, with one (B3) corresponding to the canonical PxxP motif and the other two (B1 and B2) not containing such a canonical SH3 recognition element.","_id":"685af523b4ac24d5329d8d93"},{"type":"Curator statement","text":"Residues 295-320 (B2) of the nonstructural protein 5A (NS5A) from Hepatitis C virus genotype 1b (strain HC-J4) corresponds to 2267-2292 residues of the polyprotein.","_id":"685af523b4ac24d5329d8d94"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T14:20:12.808Z","_id":"685af523b4ac24d5329d8d95"},"version":1,"_id":"685af523b4ac24d5329d8d92","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2172,"end":2200,"interaction_partner":[],"reference_html":"Interaction of nonstructural protein 5A of the hepatitis C virus with Src homology 3 domains using noncanonical binding sites. <i> Schwarten M, Sólyom Z, Feuerstein S, Aladağ A, Hoffmann S, Willbold D, Brutscher B. </i> Biochemistry, 2013","reference_id":"23947833","region_id":"DP01142r024","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Upon addition of SH3 at concentrations higher than the equimolar concentration, chemical shift changes were observed for NS5A residues 200–228 (binding site B1) and 295–320 (binding site B2).","_id":"685af523b4ac24d5329d8d97"},{"type":"Curator statement","text":"Residues 200-228 (B1) of the nonstructural protein 5A (NS5A) from Hepatitis C virus genotype 1b (strain HC-J4) corresponds to 2172-2200 residues of the polyprotein.","_id":"685af523b4ac24d5329d8d98"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T14:20:14.296Z","_id":"685af523b4ac24d5329d8d99"},"version":1,"_id":"685af523b4ac24d5329d8d96","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-09T08:16:37.293Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001269","ec_name":"surface plasmon resonance evidence used in manual assertion","ec_ontology":"ECO","start":2305,"end":2341,"interaction_partner":[{"db":"UniProt","id":"O00499","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8d9d"}],"reference_html":"Transient structure and SH3 interaction sites in an intrinsically disordered fragment of the hepatitis C virus protein NS5A. <i> Feuerstein S, Solyom Z, Aladag A, Favier A, Schwarten M, Hoffmann S, Willbold D, Brutscher B. </i> J Mol Biol, 2012","reference_id":"22543239","region_id":"DP01142r025","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"This refers to a macroscopic system with a high binding affinity of the two proteins, consistent with a Kd of 0.1 μM measured by surface plasmon resonance for a short NS5A(333–369) fragment that comprises the entire poly-proline rich region (Fig. S6).","_id":"685af523b4ac24d5329d8d9b"},{"type":"Curator statement","text":"Residues 333-369 of the nonstructural protein 5A (NS5A) from Hepatitis C virus genotype 1b (strain HC-J4) corresponds to 2305-2341 residues of the polyprotein.","_id":"685af523b4ac24d5329d8d9c"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-30T19:44:40.979Z","_id":"685af523b4ac24d5329d8d9e"},"version":2,"_id":"685af523b4ac24d5329d8d9a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2314,"end":2338,"interaction_partner":[],"reference_html":"Transient structure and SH3 interaction sites in an intrinsically disordered fragment of the hepatitis C virus protein NS5A. <i> Feuerstein S, Solyom Z, Aladag A, Favier A, Schwarten M, Hoffmann S, Willbold D, Brutscher B. </i> J Mol Biol, 2012","reference_id":"22543239","region_id":"DP01142r026","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Adding a small amount of Bin1–SH3 (molar ratio of 5:1) only affects the line widths and chemical shifts of amide resonances in the region 342 to 366 (Fig. 4a) comprising three canonical SH3 binding sites (PPII helix motifs): one of class I [PP1.2 (348–354)] and two of class II [PP2.1 (343–348) and PP2.2 (351–356)] (Fig. 4c).","_id":"685af523b4ac24d5329d8da0"},{"type":"Curator statement","text":"Residues 342-366 of the nonstructural protein 5A (NS5A) from Hepatitis C virus genotype 1b (strain HC-J4) corresponds to 2314-2338 residues of the polyprotein.","_id":"685af523b4ac24d5329d8da1"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T14:20:17.156Z","_id":"685af523b4ac24d5329d8da2"},"version":1,"_id":"685af523b4ac24d5329d8d9f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":2163,"end":2341,"interaction_partner":[],"reference_html":"Transient structure and SH3 interaction sites in an intrinsically disordered fragment of the hepatitis C virus protein NS5A. <i> Feuerstein S, Solyom Z, Aladag A, Favier A, Schwarten M, Hoffmann S, Willbold D, Brutscher B. </i> J Mol Biol, 2012","reference_id":"22543239","region_id":"DP01142r027","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Consequently, at an equimolar mixture of the two proteins at 100 μM concentration, this high-affinity NS5A(191–369) binding site is saturated, and only peaks from the bound state were observable in the NMR spectra.","_id":"685af523b4ac24d5329d8da4"},{"type":"Curator statement","text":"Residues 191-369 of the nonstructural protein 5A (NS5A) from Hepatitis C virus genotype 1b (strain HC-J4) corresponds to 2163-2341 residues of the polyprotein.","_id":"685af523b4ac24d5329d8da5"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T14:20:26.878Z","_id":"685af523b4ac24d5329d8da6"},"version":1,"_id":"685af523b4ac24d5329d8da3","reference_source":"pmid"}],"__v":0,"disorder_content":0.05946843853820598,"disprot_consensus":{"full":[{"start":2163,"end":2341,"type":"D"}],"Structural state":[{"start":2163,"end":2341,"type":"D"}],"Molecular function":[{"start":2163,"end":2341,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03545","name":"Yersinia virulence determinant (YopE)","start":127,"end":195},{"id":"PF09020","name":"YopE, N terminal","start":1,"end":126}],"gene3D":[{"start":90,"end":219,"id":"1.20.120.260","name":"Virulence factor YopE uncharacterised domain"}]},"uniref50":"UniRef50_P31493","sequence":"MKISSFISTSLPLPTSVSGSSSVGEMSGRSVSQQTSDQYANNLAGRTESPQGSSLASRIIERLSSVAHSVIGFIQRMFSEGSHKPVVTPAPTPAQMPSPTSFSDSIKQLAAETLPKYMQQLNSLDAEMLQKNHDQFATGSGPLRGSITQCQGLMQFCGGELQAEASAILNTPVCGIPFSQWGTIGGAASAYVASGVDLTQAANEIKGLAQQMQKLLSLM","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"],"uniref90":"UniRef90_P31493","disprot_id":"DP01144","ncbi_taxon_id":273123,"regions_counter":6,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":100,"region_id":"DP01144r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The type III secretion chaperone SycE promotes a localized disorder-to-order transition in the natively unfolded effector YopE. <i> Rodgers L, Gamez A, Riek R, Ghosh P. </i> J Biol Chem, 2008","statement":[{"text":"Backbone chemical shifts of free YopE were compared with those expected for a random coil state. The deviations from random coil values of secondary chemical shifts (Δδ) in 15N, 1H, and 13C dimensions of the chaperone binding (Cb) region of free YopE were found to be close to zero, indicating that this region was in a random coil state.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":1,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18502763","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-10T15:55:20.121Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":78,"term_name":"disorder to order","released":"2025_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The type III secretion chaperone SycE promotes a localized disorder-to-order transition in the natively unfolded effector YopE. <i> Rodgers L, Gamez A, Riek R, Ghosh P. </i> J Biol Chem, 2008","statement":[{"text":"Backbone chemical shifts of free YopE were compared with those expected for a random coil state. The deviations from random coil values of secondary chemical shifts (Δδ) in 15N, 1H, and 13C dimensions of the chaperone binding (Cb) region of free YopE were found to be close to zero, indicating that this region was in a random coil state. In contrast, when SycE was bound, these same residues of YopE had values significantly different from those typical for a random coil state. These results provide evidence for SycE promoting a transition in the Cb region from an unstructured state to a structured conformation.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"vnugnes","start":23,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18502763","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2025-06-05T13:21:53.606Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01144r002","ec_go":"EXP","disprot_namespace":"Structural transition","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"BMRB","id":"15878"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q663P0"}]},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q663P0","partner_end":null}],"ec_ontology":"ECO","end":78,"term_name":"protein binding","start":23,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0001-8399-7907","curator_id":"vnugnes","released":"2025_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"18502763","statement":[{"text":" Comparison of dually assigned residues also revealed that SycE binding had no effect on the S1 region and likewise no effect on residues 81–100 connecting the Cb region to the RhoGAP domain. These results provide direct evidence for the effect of SycE binding being strictly localized to the Cb region of YopE and not extending outside the Cb region.","type":"Results"},{"text":"The Cb region spans residues 23-78 of YopE.","type":"Curator statement"}],"reference_html":"The type III secretion chaperone SycE promotes a localized disorder-to-order transition in the natively unfolded effector YopE. <i> Rodgers L, Gamez A, Riek R, Ghosh P. </i> J Biol Chem, 2008","date":"2025-06-03T14:09:56.147Z","term_id":"GO:0005515","ec_id":"ECO:0006165","version":5,"region_id":"DP01144r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"BMRB","id":"15878"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"sequence_construct":"MKISSFISTSLPLPTSVSGSSSVGEMSGRSVSQQTSDQYANNLAGRTESPQGSSLASRIIERLSSVAHSVIGFIQRMFSEGSHKPVVTPAPTPAQMPSPTSFSDSIKQLAAETLPKYMQQLNSLDAEMLQKNHAQFATGSGPLRGSITQCQGLMQFCGGELQAEASAILNTPVCGIPFSQWGTIGGVASAYVASGVDLTQAANEIKGLAQQMQKLLSLMLEHHHHHH"},{"start":1,"end":100,"reference_id":"18502763","reference_source":"pmid","reference_html":"The type III secretion chaperone SycE promotes a localized disorder-to-order transition in the natively unfolded effector YopE. <i> Rodgers L, Gamez A, Riek R, Ghosh P. </i> J Biol Chem, 2008","date":"2025-04-25T12:42:49.519Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP01144r005","statement":[{"text":"Backbone chemical shifts of free YopE were compared with those expected for a random coil state. The deviations from random coil values of secondary chemical shifts (Δδ) in 15N, 1H, and 13C dimensions of the chaperone binding (Cb) region of free YopE were found to be close to zero, indicating that this region was in a random coil state.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-03T14:13:50.099Z"}},{"start":79,"end":100,"reference_id":"18502763","reference_source":"pmid","reference_html":"The type III secretion chaperone SycE promotes a localized disorder-to-order transition in the natively unfolded effector YopE. <i> Rodgers L, Gamez A, Riek R, Ghosh P. </i> J Biol Chem, 2008","date":"2025-06-03T14:14:59.105Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":null}],"cross_refs":[{"db":"BMRB","id":"7426"}],"region_id":"DP01144r006","sequence_construct":"MKISSFISTSLPLPTSVSGSSSVGEMSGRSVSQQTSDQYANNLAGRTESPQGSSLASRIIERLSSVAHSVIGFIQRMFSEGSHKPVVTPAPTPAQMPSPTSFSDSIKQLAAETLPKYMQQLNSLDAEMLQKNHAQFATGSGPLRGSITQCQGLMQFCGGELQAEASAILNTPVCGIPFSQWGTIGGVASAYVASGVDLTQAANEIKGLAQQMQKLLSLMLEHHHHHH","statement":[{"text":"Residues 79–101 connecting the Cb region to the RhoGAP domain lacked detectable secondary structure regardless of SycE binding (Fig. 2), indicating that these residues likely serve as an unstructured linker.","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_P31493","date":"2018-06-25T17:57:04.000Z","acc":"P08008","name":"Outer membrane virulence protein YopE","length":219,"organism":"Yersinia pseudotuberculosis serotype I (strain IP32953)","dataset":["Bacterial virulence-related proteins"],"UniParc":"UPI000013BCAE","genes":[{"name":{"value":"yopE"},"synonyms":[{"value":"yop25"}],"olnNames":[{"value":"pYV0025"}]}],"alphafold_very_low_content":0.2694063926940639,"disorder_content":0.45662100456621,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"},{"start":23,"end":78,"type":"T"},{"start":79,"end":100,"type":"D"}],"Structural state":[{"start":1,"end":100,"type":"D"}],"Structural transition":[{"start":23,"end":78,"type":"T"}],"Molecular function":[{"start":23,"end":78,"type":"F"}],"Disorder function":[{"start":1,"end":100,"type":"F"}]}},{"features":{"pfam":[{"id":"PF14185","name":"Antitoxin SpoIISB, type II toxin-antitoxin system","start":1,"end":56}],"gene3D":[{"start":34,"end":56,"id":"1.20.5.740","name":"Single helix  bin"}]},"uniref50":"UniRef50_O34800","sequence":"MERAFQNRCEPRAAKPFKILKKRSTTSVASYQVSPHTARIFKENERLIDEYKRKKA","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Bacillus"],"uniref90":"UniRef90_O34800","disprot_id":"DP01146","dataset":["Unicellular toxins and antitoxins"],"ncbi_taxon_id":224308,"regions_counter":11,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":56,"region_id":"DP01146r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The structure and interactions of SpoIISA and SpoIISB, a toxin-antitoxin system in Bacillus subtilis. <i> Florek P, Levdikov VM, Blagova E, Lebedev AA, Škrabana R, Resetárová S, Pavelcíková P, Barak I, Wilkinson AJ. </i> J Biol Chem, 2011","statement":[{"text":"By contrast the far-UV CD spectrum of SpoIISB has less pronounced features with a shallow minimum at 200 nm. This spectrum is barely distinct from the CD spectrum of a control sample containing buffer alone. We deduce from this spectrum that SpoIISB is natively disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":1,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"fquaglia","timestamp":"2020-12-10T17:52:44.914Z","curator_name":"Federica Quaglia"},"reference_id":"21147767","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP01146r003","validated":{"curator_id":"fquaglia","timestamp":"2020-12-10T17:52:50.389Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":56,"ec_name":"far-UV circular dichroism evidence used in manual assertion","start":1,"version":5,"statement":[{"text":"The addition of SpoIISB leads to an increase in the molar ellipticity of the sample at 190–200 nm and a decrease in the molar ellipticity over the wavelength range 205–225 nm. This indicates that the addition of SpoIISB to His6-CSpoIISA leads to an increase in the amount of protein that has secondary structure. Because the CD spectrum of SpoIISB alone indicates that this protein is unstructured, we conclude that CSpoIISA induces structure in SpoIISB as the two proteins form a complex.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"O34853","partner_end":null}],"term_name":"protein binding","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"21147767","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006204","curator_id":"rpancsa","reference_html":"The structure and interactions of SpoIISA and SpoIISB, a toxin-antitoxin system in Bacillus subtilis. <i> Florek P, Levdikov VM, Blagova E, Lebedev AA, Škrabana R, Resetárová S, Pavelcíková P, Barak I, Wilkinson AJ. </i> J Biol Chem, 2011","term_id":"GO:0005515","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":56,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"The structure and interactions of SpoIISA and SpoIISB, a toxin-antitoxin system in Bacillus subtilis. <i> Florek P, Levdikov VM, Blagova E, Lebedev AA, Škrabana R, Resetárová S, Pavelcíková P, Barak I, Wilkinson AJ. </i> J Biol Chem, 2011","statement":[{"text":"The addition of SpoIISB leads to an increase in the molar ellipticity of the sample at 190–200 nm and a decrease in the molar ellipticity over the wavelength range 205–225 nm. This indicates that the addition of SpoIISB to His6-CSpoIISA leads to an increase in the amount of protein that has secondary structure. Because the CD spectrum of SpoIISB alone indicates that this protein is unstructured, we conclude that CSpoIISA induces structure in SpoIISB as the two proteins form a complex. These observations are consistent with the crystal structure, which shows that SpoIISB exhibits secondary structure in the complex that is dependent on extensive packing against SpoIISA.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"rpancsa","start":1,"term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"21147767","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","validated":{"curator_id":"fquaglia","timestamp":"2020-12-10T16:29:45.835Z","curator_name":"Federica Quaglia"},"region_id":"DP01146r004","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP01146r005","validated":{"curator_id":"fquaglia","timestamp":"2020-12-10T17:52:52.224Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":56,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"Surface plasmon resonance experiments revealed that the CSpoIISA·SpoIISB complex is stable with a dissociation constant in the nanomolar range.","type":"Abstract"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"O34853","partner_end":null}],"term_name":"protein binding","ec_name":"surface plasmon resonance evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"21147767","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001269","curator_id":"rpancsa","reference_html":"The structure and interactions of SpoIISA and SpoIISB, a toxin-antitoxin system in Bacillus subtilis. <i> Florek P, Levdikov VM, Blagova E, Lebedev AA, Škrabana R, Resetárová S, Pavelcíková P, Barak I, Wilkinson AJ. </i> J Biol Chem, 2011","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01146r006","validated":{"curator_id":"fquaglia","timestamp":"2020-12-10T17:53:07.526Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":56,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"Here, the crystal structure of a cytoplasmic fragment of SpoIISA (CSpoIISA) in complex with SpoIISB has been determined by selenomethionine-multiwavelength anomalous dispersion phasing to 2.5 Å spacing, revealing a CSpoIISA2·SpoIISB2 heterotetramer. CSpoIISA has a single domain α/β structure resembling a GAF domain with an extended α-helix at its N terminus. The two CSpoIISA protomers form extensive interactions through an intermolecular four-helix bundle. Each SpoIISB chain is highly extended and lacking tertiary structure. The SpoIISB chains wrap around the CSpoIISA dimer, forming extensive interactions with both CSpoIISA protomers.","type":"Abstract"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"O34853","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"21147767","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3O6Q"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"rpancsa","reference_html":"The structure and interactions of SpoIISA and SpoIISB, a toxin-antitoxin system in Bacillus subtilis. <i> Florek P, Levdikov VM, Blagova E, Lebedev AA, Škrabana R, Resetárová S, Pavelcíková P, Barak I, Wilkinson AJ. </i> J Biol Chem, 2011","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01146r007","validated":{"curator_id":"fquaglia","timestamp":"2020-12-10T17:52:47.993Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":52,"term_id":"IDPO:0000011","start":9,"version":2,"statement":[{"text":"Here, the crystal structure of a cytoplasmic fragment of SpoIISA (CSpoIISA) in complex with SpoIISB has been determined by selenomethionine-multiwavelength anomalous dispersion phasing to 2.5 Å spacing, revealing a CSpoIISA2·SpoIISB2 heterotetramer. CSpoIISA has a single domain α/β structure resembling a GAF domain with an extended α-helix at its N terminus. The two CSpoIISA protomers form extensive interactions through an intermolecular four-helix bundle. Each SpoIISB chain is highly extended and lacking tertiary structure. The SpoIISB chains wrap around the CSpoIISA dimer, forming extensive interactions with both CSpoIISA protomers.","type":"Abstract"}],"term_name":"disorder to order","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"21147767","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3O6Q"}],"term_namespace":"Structural transition","ec_id":"ECO:0005670","curator_id":"rpancsa","reference_html":"The structure and interactions of SpoIISA and SpoIISB, a toxin-antitoxin system in Bacillus subtilis. <i> Florek P, Levdikov VM, Blagova E, Lebedev AA, Škrabana R, Resetárová S, Pavelcíková P, Barak I, Wilkinson AJ. </i> J Biol Chem, 2011","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP01146r008","ec_ontology":"ECO","end":56,"term_id":"GO:0097351","start":1,"version":4,"statement":[{"text":"Surface plasmon resonance experiments revealed that the CSpoIISA·SpoIISB complex is stable with a dissociation constant in the nanomolar range.","type":"Abstract"},{"text":"High affinity binding of CSpoIISA to SpoIISB is largely conferred by the low rate of complex dissociation, reflected in the slow release of bound SpoIISB from the sensor chip after the end of the injection (Fig. 2B). This could have biological implications in effective blocking of SpoIISA by SpoIISB in vivo under conditions of limited renewal of the available SpoIISB pool in the cell.","type":"Results"}],"term_name":"toxin sequestering activity","ec_name":"surface plasmon resonance evidence used in manual assertion","curator_orcid":"0000-0002-5152-5953","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"21147767","date":"2022-03-09T08:17:06.156Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001269","curator_id":"esalladini","reference_html":"The structure and interactions of SpoIISA and SpoIISB, a toxin-antitoxin system in Bacillus subtilis. <i> Florek P, Levdikov VM, Blagova E, Lebedev AA, Škrabana R, Resetárová S, Pavelcíková P, Barak I, Wilkinson AJ. </i> J Biol Chem, 2011","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a toxic protein, disabling its function. There may be more than one antitoxin to a toxic protein. Instances of this activity are known only in prokaryotes, where the toxic protein may be a ribonuclease, a DNA gyrase, or other.\" [GOC:rs, PMID:19143615, PMID:19325885, PMID:21819231, PMID:22545240, PMID:24806488, Wikipedia:Toxin-antitoxin_system#Type_II]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"O34853","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-26T18:38:20.884Z"}},{"region_id":"DP01146r009","validated":{"curator_id":"fquaglia","timestamp":"2020-12-10T17:53:42.172Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":56,"term_id":"GO:0097351","start":1,"version":3,"statement":[{"text":"Here, the crystal structure of a cytoplasmic fragment of SpoIISA (CSpoIISA) in complex with SpoIISB has been determined by selenomethionine-multiwavelength anomalous dispersion phasing to 2.5 Å spacing, revealing a CSpoIISA2·SpoIISB2 heterotetramer. CSpoIISA has a single domain α/β structure resembling a GAF domain with an extended α-helix at its N terminus. The two CSpoIISA protomers form extensive interactions through an intermolecular four-helix bundle. Each SpoIISB chain is highly extended and lacking tertiary structure. The SpoIISB chains wrap around the CSpoIISA dimer, forming extensive interactions with both CSpoIISA protomers.","type":"Abstract"}],"term_name":"toxin sequestering activity","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"21147767","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"rpancsa","reference_html":"The structure and interactions of SpoIISA and SpoIISB, a toxin-antitoxin system in Bacillus subtilis. <i> Florek P, Levdikov VM, Blagova E, Lebedev AA, Škrabana R, Resetárová S, Pavelcíková P, Barak I, Wilkinson AJ. </i> J Biol Chem, 2011","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a toxic protein, disabling its function. There may be more than one antitoxin to a toxic protein. Instances of this activity are known only in prokaryotes, where the toxic protein may be a ribonuclease, a DNA gyrase, or other.\" [GOC:rs, PMID:19143615, PMID:19325885, PMID:21819231, PMID:22545240, PMID:24806488, Wikipedia:Toxin-antitoxin_system#Type_II]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01146r010","validated":{"curator_id":"fquaglia","timestamp":"2020-12-10T17:53:41.272Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":56,"term_id":"GO:0097351","start":1,"version":3,"statement":[{"text":"Inappropriate spoIISA expression causes lysis of vegetatively growing B. subtilis cells and Escherichia coli cells when expressed heterologously, effects that are countered by co-expression of spoIISB, identifying SpoIISA-SpoIISB as a toxin-antitoxin system.","type":"Abstract"}],"term_name":"toxin sequestering activity","ec_name":"experimental phenotypic evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"21147767","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0007634","curator_id":"rpancsa","reference_html":"The structure and interactions of SpoIISA and SpoIISB, a toxin-antitoxin system in Bacillus subtilis. <i> Florek P, Levdikov VM, Blagova E, Lebedev AA, Škrabana R, Resetárová S, Pavelcíková P, Barak I, Wilkinson AJ. </i> J Biol Chem, 2011","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a toxic protein, disabling its function. There may be more than one antitoxin to a toxic protein. Instances of this activity are known only in prokaryotes, where the toxic protein may be a ribonuclease, a DNA gyrase, or other.\" [GOC:rs, PMID:19143615, PMID:19325885, PMID:21819231, PMID:22545240, PMID:24806488, Wikipedia:Toxin-antitoxin_system#Type_II]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01146r011","validated":{"curator_id":"fquaglia","timestamp":"2020-12-10T17:53:38.910Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":53,"term_id":"GO:0097351","start":13,"version":3,"statement":[{"text":"However, when spoIISA was co-expressed with spoIISB deletants encoding proteins in which 3 or 12 N-terminal residues were replaced by Met-Ala and Met-Ala-Ala, respectively, the sporulation efficiencies of the strains were similar to the wild type strain (2.9 × 108 and 8.4 × 108 spores/ml; Fig. 4A). These results suggest that the N-terminal 12 residues are dispensable for the antitoxin activity of SpoIISB in vivo. Because the missing residues include Cys9′, the disulfide bridge is probably not critical for the antidote function. The sporulation efficiencies of strains encoding SpoIISB proteins with C-terminal deletions of 16, 12, 8, and 4 residues were 9.5 × 103, 5.7 × 103, 6.6 × 103, and 4.8 × 103 spores/ml, respectively. These are similar to the sporulation efficiency of cells in which the entire spoIISB gene has been deleted. Thus, C-terminal deletion of four or more residues leads to a loss of the capacity of SpoIISB to overcome SpoIISA toxicity.","type":"Results"}],"term_name":"toxin sequestering activity","ec_name":"deletion mutation phenotypic evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"21147767","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001175","curator_id":"rpancsa","reference_html":"The structure and interactions of SpoIISA and SpoIISB, a toxin-antitoxin system in Bacillus subtilis. <i> Florek P, Levdikov VM, Blagova E, Lebedev AA, Škrabana R, Resetárová S, Pavelcíková P, Barak I, Wilkinson AJ. </i> J Biol Chem, 2011","ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a toxic protein, disabling its function. There may be more than one antitoxin to a toxic protein. Instances of this activity are known only in prokaryotes, where the toxic protein may be a ribonuclease, a DNA gyrase, or other.\" [GOC:rs, PMID:19143615, PMID:19325885, PMID:21819231, PMID:22545240, PMID:24806488, Wikipedia:Toxin-antitoxin_system#Type_II]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_O34800","date":"2018-06-25T20:12:59.000Z","acc":"O34800","name":"Stage II sporulation protein SB","length":56,"organism":"Bacillus subtilis (strain 168)","UniParc":"UPI0000060292","genes":[{"name":{"value":"spoIISB"},"olnNames":[{"value":"BSU12820"}]}],"alphafold_very_low_content":0.03571428571428571,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":56,"type":"T"}],"Structural state":[{"start":1,"end":56,"type":"D"}],"Molecular function":[{"start":1,"end":56,"type":"F"}],"Structural transition":[{"start":1,"end":56,"type":"T"}]}},{"features":{"pfam":[{"id":"PF18286","name":"Type III secretion system ExsE","start":33,"end":78}],"gene3D":[{"start":16,"end":81,"id":"G3DSA:3.30.1490.370"}]},"uniref50":"UniRef50_Q9I322","sequence":"MKIESISPVQPSQDAGAEAVGHFEGRSVTRAAVRGEDRSSVAGLARWLARNVAGDPRSEQALQRLADGDGTPLEARTVRRR","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Pseudomonadales","Pseudomonadaceae","Pseudomonas"],"uniref90":"UniRef90_Q9I322","disprot_id":"DP01147","ncbi_taxon_id":208964,"regions_counter":6,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":81,"region_id":"DP01147r001","released":"2022_03","ec_id":"ECO:0007691","reference_html":"The transiently ordered regions in intrinsically disordered ExsE are correlated with structural elements involved in chaperone binding. <i> Zheng Z, Ma D, Yahr TL, Chen L. </i> Biochem Biophys Res Commun, 2012","statement":[{"text":"Whereas ExsE is rapidly degraded to small undetectable peptides by SDS-PAGE following a brief treatment with subtilisin. The limited stability of ExsE towards proteolytic digestion suggests that it either lacks of stable tertiary fold or adopts a highly dynamic structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":1,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22138394","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":81,"region_id":"DP01147r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The transiently ordered regions in intrinsically disordered ExsE are correlated with structural elements involved in chaperone binding. <i> Zheng Z, Ma D, Yahr TL, Chen L. </i> Biochem Biophys Res Commun, 2012","statement":[{"text":"ExsE lacks stable secondary structures, and resembles random coil conformations in solution based on circular dichroism.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":1,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22138394","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":81,"term_name":"molecular function regulator","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"The transiently ordered regions in intrinsically disordered ExsE are correlated with structural elements involved in chaperone binding. <i> Zheng Z, Ma D, Yahr TL, Chen L. </i> Biochem Biophys Res Commun, 2012","statement":[{"text":"ExsE interacts with the secretion chaperone ExsC.","type":"Introduction"}],"term_id":"GO:0098772","curator_id":"rpancsa","start":1,"term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"22138394","version":3,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01147r003","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P26995","partner_end":null}],"ec_ontology":"ECO","end":81,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"22138394","statement":[{"text":"ExsE interacts with the secretion chaperone ExsC.","type":"Introduction"}],"reference_html":"The transiently ordered regions in intrinsically disordered ExsE are correlated with structural elements involved in chaperone binding. <i> Zheng Z, Ma D, Yahr TL, Chen L. </i> Biochem Biophys Res Commun, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","version":4,"region_id":"DP01147r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":81,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"The transiently ordered regions in intrinsically disordered ExsE are correlated with structural elements involved in chaperone binding. <i> Zheng Z, Ma D, Yahr TL, Chen L. </i> Biochem Biophys Res Commun, 2012","statement":[{"text":"We identified regions that are partially ordered in the largely unstructured ExsE polypeptide. We found that these regions are correlated with those that adopt secondary structures when ExsE binds to ExsC. In the stable ExsE-ExsC interface, ExsE is in the fully extended conformation, and two signature β strands at both the N- and C-termini of the ExsE polypeptide pair with two symmetry-related five-stranded β sheets of dimeric ExsC. These findings suggest the importance of pre-existing ordered structured in binding of intrinsically disordered proteins to their targets.","type":"Introduction"}],"term_id":"IDPO:0000011","curator_id":"rpancsa","start":1,"term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"22138394","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01147r005","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":81,"region_id":"DP01147r006","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The transiently ordered regions in intrinsically disordered ExsE are correlated with structural elements involved in chaperone binding. <i> Zheng Z, Ma D, Yahr TL, Chen L. </i> Biochem Biophys Res Commun, 2012","statement":[{"text":"The 1H-15N HSQC NMR spectra showed that the amide proton chemical shifts of ExsE collapse in a narrow range of 7.8-8.6 ppm, consistent with the absence of secondary structures in ExsE. ExsE is highly dynamic throughout the polypeptide chain, as indicated by backbone dynamic analysis on relaxation times T1 and T2 of 15N and the {1H}-15N heteronuclear NOEs. Some local regions in the globally unstructured ExsE may possess residual or transient structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":1,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22138394","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9I322","date":"2018-06-25T20:33:49.000Z","acc":"Q9I322","name":"ExsE","length":81,"organism":"Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)","dataset":[],"UniParc":"UPI00000C5458","genes":[{"name":{"value":"exsE"},"olnNames":[{"value":"PA1711"}]}],"alphafold_very_low_content":0.012345679012345678,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":81,"type":"T"}],"Structural state":[{"start":1,"end":81,"type":"D"}],"Molecular function":[{"start":1,"end":81,"type":"F"}],"Structural transition":[{"start":1,"end":81,"type":"T"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_P73124","sequence":"MSTQQQARALMMRHHQFIKNRQQSLLSRAAAEIGVQAEKDFWTTVQGKPQSSFRETYDRSSASLS","taxonomy":["Bacteria","Cyanobacteria","Synechococcales","Merismopediaceae","Synechocystis","unclassified Synechocystis"],"uniref90":"UniRef90_P73124","disprot_id":"DP01148","ncbi_taxon_id":1147,"regions_counter":7,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":65,"region_id":"DP01148r001","released":"2025_06","ec_id":"ECO:0006165","reference_html":"Dissecting the Binding between Glutamine Synthetase and Its Two Natively Unfolded Protein Inhibitors. <i> Pantoja-Uceda D, Neira JL, Saelices L, Robles-Rengel R, Florencio FJ, Muro-Pastor MI, Santoro J. </i> Biochemistry, 2016","statement":[{"text":"The 1H–15N HSQC spectrum showed signals with narrow lines and limited dispersion. In total, the δ2D prediction suggests that 29% of the residues in IF7 adopt helical conformations (helical percentages of >10%) and 71% of them populate random-coil conformations.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":1,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0849-9312","date":"2025-04-30T08:56:44.027Z","reference_source":"pmid","term_name":"disorder","reference_id":"27232663","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"BMRB","id":"25921"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T22:32:09.470Z"}},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"A0A068N015","partner_end":null}],"ec_ontology":"ECO","end":65,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"27232663","statement":[{"text":"Glutamine synthetase (GS) is controlled by a post-translational regulatory mechanism involving protein–protein interactions with 65-residue (IF7) and 149-residue (IF17) inactivating proteins.","type":"Introduction"}],"reference_html":"Dissecting the Binding between Glutamine Synthetase and Its Two Natively Unfolded Protein Inhibitors. <i> Pantoja-Uceda D, Neira JL, Saelices L, Robles-Rengel R, Florencio FJ, Muro-Pastor MI, Santoro J. </i> Biochemistry, 2016","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","version":4,"region_id":"DP01148r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":65,"reference_id":"32074499","reference_source":"pmid","reference_html":"Dynamics of the intrinsically disordered inhibitor IF7 of glutamine synthetase in isolation and in complex with its partner. <i> Neira JL, Ortore MG, Florencio FJ, Muro-Pastor MI, Rizzuti B. </i> Arch Biochem Biophys, 2020","date":"2025-04-30T09:02:41.371Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP01148r004","statement":[{"text":"The NOE values of residues of the isolated IF7 were below 0.52 (the value observed for Ala29) (Fig. 1 D). Keeping in mind that at 11.7 T the maximum value for the NOE is 0.70 [52] in an isotropically tumbling molecule without internal motions, we must conclude that isolated IF7 had a highly flexible backbone.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T22:32:07.559Z"}},{"start":1,"end":65,"reference_id":"32074499","reference_source":"pmid","reference_html":"Dynamics of the intrinsically disordered inhibitor IF7 of glutamine synthetase in isolation and in complex with its partner. <i> Neira JL, Ortore MG, Florencio FJ, Muro-Pastor MI, Rizzuti B. </i> Arch Biochem Biophys, 2020","date":"2025-04-30T09:07:04.206Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP01148r005","statement":[{"text":"We did not observe a well-defined peak in the Kratky plot of isolated IF7 data, proving that the protein did not have a globular shape. In a first approximation, SAXS data for IF7 were fitted by using either the Guinier or Debye equation (Fig. S2). The two approaches provided a radius of gyration Rg = 24.2 ± 0.2 Å (in the Guinier approach) and Rg = 26.95 ± 0.05 Å (in the Debye approach). The Debye equation is more appropriate for disordered chains than the Guinier one, and accurately fitted our experimental data, as shown by the continuous line (Fig. 3).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T22:31:56.049Z"}},{"start":1,"end":65,"reference_id":"32074499","reference_source":"pmid","reference_html":"Dynamics of the intrinsically disordered inhibitor IF7 of glutamine synthetase in isolation and in complex with its partner. <i> Neira JL, Ortore MG, Florencio FJ, Muro-Pastor MI, Rizzuti B. </i> Arch Biochem Biophys, 2020","date":"2025-04-30T09:17:11.036Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P77961","operator":null,"partner_start":1,"partner_end":473}],"region_id":"DP01148r006","statement":[{"text":"Because GS and IF7 sizes are very different, it is clear that GS scattering contribution dominates SAXS data. However, the fact that the experimental curve, corresponding to the simultaneous presence of GS and IF7 in solution, was different from the sum of the single scattering contributions of the two isolated proteins, confirms the presence of a well defined assembly arrangement between IF7 and GS. Although the presence of the IF7/GS complex in solution is well-documented [6,9,25], our SAXS results provide a direct estimation of some of its structural features at a low resolution.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T22:32:18.336Z"}},{"start":1,"end":65,"reference_id":"32074499","reference_source":"pmid","reference_html":"Dynamics of the intrinsically disordered inhibitor IF7 of glutamine synthetase in isolation and in complex with its partner. <i> Neira JL, Ortore MG, Florencio FJ, Muro-Pastor MI, Rizzuti B. </i> Arch Biochem Biophys, 2020","date":"2025-04-30T09:21:43.411Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P77961","operator":null,"partner_start":1,"partner_end":473}],"region_id":"DP01148r007","statement":[{"text":"The addition of GS in submicromolar concentrations to IF7 did not change the chemical shifts of the cross-peaks in the HSQC spectrum of IF7 (Fig. S1, Table ST2), although it induced signal broadening as it happened in the cross-peaks of other IDPs when bound to their partners [22,57, and references therein]. In general, we observed an increase in all the relaxation rates of IF7, when compared to those measured in the absence of GS (Fig. 2).","type":"Results"},{"text":"All the NOE values showed the same tendency described in the absence of GS, indicating that IF7 kept its disordered state when it is bound.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T22:32:14.748Z"}}],"released":"2018_11","uniref100":"UniRef100_A0A068MVV3","date":"2018-06-25T21:07:20.000Z","acc":"A0A068MVV3","name":"Glutamine synthetase inactivating factor IF7","length":65,"organism":"Synechocystis sp. (strain PCC 6714)","dataset":[],"UniParc":"UPI00048AF037","genes":[{"name":{"value":"gifA","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AIE74196.1","url":"https://www.ebi.ac.uk/ena/browser/view/AIE74196.1"}}]},"orfNames":[{"value":"D082_16680","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AIE74196.1","url":"https://www.ebi.ac.uk/ena/browser/view/AIE74196.1"}}]}]}],"alphafold_very_low_content":0.03076923076923077,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":65,"type":"D"}],"Structural state":[{"start":1,"end":65,"type":"D"}],"Molecular function":[{"start":1,"end":65,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04111","name":"Apg6 BARA domain","start":264,"end":445},{"id":"PF15285","name":"Beclin-1 BH3 domain, Bcl-2-interacting","start":105,"end":129},{"id":"PF17675","name":"Apg6 coiled-coil region","start":135,"end":261}],"gene3D":[{"start":241,"end":450,"id":"1.10.418.40","name":"Autophagy protein 6/Beclin 1"}]},"uniref50":"UniRef50_Q14457","sequence":"MEGSKTSNNSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEETNSGEEPFIETPRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEILEQMNEDDSEQLQMELKELALEEERLIQELEDVEKNRKIVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQMRYAQTQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q14457","disprot_id":"DP01149","ncbi_taxon_id":9606,"regions_counter":37,"creator":"zkalman","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":150,"region_id":"DP01149r001","released":"2022_06","ec_id":"ECO:0006204","reference_html":"The BECN1 N-terminal domain is intrinsically disordered. <i> Lee EF, Perugini MA, Pettikiriarachchi A, Evangelista M, Keizer DW, Yao S, Fairlie WD. </i> Autophagy, 2016","statement":[{"text":"The CD spectrum showed a single minimum at approximately 200 nm (Fig. 2A) that is indicative of random or disordered secondary structure. ","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-05-16T20:04:48.123Z","reference_source":"pmid","term_name":"disorder","reference_id":"27046249","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:27:26.049Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":150,"region_id":"DP01149r002","released":"2022_06","ec_id":"ECO:0006165","reference_html":"The BECN1 N-terminal domain is intrinsically disordered. <i> Lee EF, Perugini MA, Pettikiriarachchi A, Evangelista M, Keizer DW, Yao S, Fairlie WD. </i> Autophagy, 2016","statement":[{"text":"The 1H-15N HSQC spectrum of BECN1(1–150)[4CS]Y (Fig. 2B) displayed very narrow chemical shift dispersion (between 7.7 and 8.7 ppm) on the 1H dimension that is a characteristic feature of intrinsically disordered proteins.","type":"Results"},{"text":"Experimentally observed backbone chemical shifts of BECN1(1–150)[4CS]Y were then used to evaluate its secondary structure with the improved version of Chemical Shift Index software (CSI 2.0)34 which makes use of all 6 backbone chemical shifts (13Cα, 13Cβ, 13C, 15N, 1HN, and 1Hα), along with sequence-derived features. This analysis confirmed that BECN1 is disordered throughout its entire N terminus (1 to 150) except for a potential half-helical turn involving residues A44 and P45 (Fig. 2C).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-05-16T20:40:45.672Z","reference_source":"pmid","term_name":"disorder","reference_id":"27046249","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys18Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The human BECN1 DNA encoding residues 1 to 150 was codon-optimized for expression in E. coli and cloned into the pET DUET-1 vector (Site I) (Novagen, 71146–3) at the BamHI/NotI sites, which fuses it to a hexahistdidine purification tag followed by a short linker sequence (MGSSHHHHHHSQDP). This served as a base construct for a subsequent construct in which all cysteines (i.e., residues 18, 21, 137, 140) were mutated to serine plus a C-terminal tyrosine was added to facilitate quantification by UV spectroscopy (called “BECN1(1–150)[4CS]Y”)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys21Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The human BECN1 DNA encoding residues 1 to 150 was codon-optimized for expression in E. coli and cloned into the pET DUET-1 vector (Site I) (Novagen, 71146–3) at the BamHI/NotI sites, which fuses it to a hexahistdidine purification tag followed by a short linker sequence (MGSSHHHHHHSQDP). This served as a base construct for a subsequent construct in which all cysteines (i.e., residues 18, 21, 137, 140) were mutated to serine plus a C-terminal tyrosine was added to facilitate quantification by UV spectroscopy (called “BECN1(1–150)[4CS]Y”)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys137Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The human BECN1 DNA encoding residues 1 to 150 was codon-optimized for expression in E. coli and cloned into the pET DUET-1 vector (Site I) (Novagen, 71146–3) at the BamHI/NotI sites, which fuses it to a hexahistdidine purification tag followed by a short linker sequence (MGSSHHHHHHSQDP). This served as a base construct for a subsequent construct in which all cysteines (i.e., residues 18, 21, 137, 140) were mutated to serine plus a C-terminal tyrosine was added to facilitate quantification by UV spectroscopy (called “BECN1(1–150)[4CS]Y”)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys140Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The human BECN1 DNA encoding residues 1 to 150 was codon-optimized for expression in E. coli and cloned into the pET DUET-1 vector (Site I) (Novagen, 71146–3) at the BamHI/NotI sites, which fuses it to a hexahistdidine purification tag followed by a short linker sequence (MGSSHHHHHHSQDP). This served as a base construct for a subsequent construct in which all cysteines (i.e., residues 18, 21, 137, 140) were mutated to serine plus a C-terminal tyrosine was added to facilitate quantification by UV spectroscopy (called “BECN1(1–150)[4CS]Y”)."}]}],"cross_refs":[{"db":"BMRB","id":"25384"}],"sequence_construct":"MGSSHHHHHHSQDPMEGSKTSNNSTMQVSFVSQRSSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEETNSGEEPFIETPRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLSEESTDTLLDQLDTY","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:27:27.937Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":150,"region_id":"DP01149r005","released":"2022_06","ec_id":"ECO:0006165","reference_html":"Characterisation of the conformational preference and dynamics of the intrinsically disordered N-terminal region of Beclin 1 by NMR spectroscopy. <i> Yao S, Lee EF, Pettikiriarachchi A, Evangelista M, Keizer DW, Fairlie WD. </i> Biochim Biophys Acta, 2016","statement":[{"text":"Previously reported backbone chemical shifts of BecN-150CSY (http://www.bmrb.wisc.edu, Accession code: 25384) [16] were further analysed using the δ2D method [30] and the results are summarized in Figure 2. As expected, BecN-150CSY is predominantly random coil (Fig. 2A) which is consistent with results from Chemical Shift Index analysis using CSI 2.0 [15] as reported previously [16], though a slightly higher propensity of α-helical conformation was observed for residues adjacent to the BH3 domain (Fig. 2B) when compared with the rest of BecN-150CSY.","type":"Results"},{"text":"Using dioxane with a hydrodynamic radius of 2.12 Å as an internal reference (Eq. 2 [29]), Rh values for BecN-150CSY were calculated to range from 29.5 to 31.4 Å across the temperature range studied, with a mean value of 30.54 ± 0.68 Å. This Rh value of BecN-150CSY is in very good agreement with those reported previously for IDPs of approximately the same size, such as α-synuclein (140 amino acid residues, Rh ~ 29 Å [36]) and MSP2 (229 amino acid residues, Rh ~ 34 -39 Å [37]). Similarly, using the relationship between Rh and the number of residues, N, for IDPs, Rh IDP = 2.49 N 0.509 as reported by Marsh and Forman-Kay [38], an expected value of 32.3 Å for BecN-150CSY was obtained which again is in excellent agreement with Rh values derived from the PFG-NMR measurements.","type":"Results"},{"text":"As the temperature coefficients of backbone amide protons over the entire BecN-150CSY were well below -4.5 ppb K -1, this indicates that the backbone amide protons are not involved in any stable hydrogen bonds [40-42] and is in agreement with the characteristics of an intrinsically disordered protein","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-05-16T20:18:49.710Z","reference_source":"pmid","term_name":"disorder","reference_id":"27288992","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys18Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The 15N-labelled Beclin 1 N-terminal domain (residues 1-150) with all cysteines mutated to serines and a tyrosine included at the C-terminal of the construct for quantitation by UV spectroscopy (BecN-150CSY), was identical to the material used for the assignment of backbone chemical shifts"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys21Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The 15N-labelled Beclin 1 N-terminal domain (residues 1-150) with all cysteines mutated to serines and a tyrosine included at the C-terminal of the construct for quantitation by UV spectroscopy (BecN-150CSY), was identical to the material used for the assignment of backbone chemical shifts"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys137Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The 15N-labelled Beclin 1 N-terminal domain (residues 1-150) with all cysteines mutated to serines and a tyrosine included at the C-terminal of the construct for quantitation by UV spectroscopy (BecN-150CSY), was identical to the material used for the assignment of backbone chemical shifts"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys140Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The 15N-labelled Beclin 1 N-terminal domain (residues 1-150) with all cysteines mutated to serines and a tyrosine included at the C-terminal of the construct for quantitation by UV spectroscopy (BecN-150CSY), was identical to the material used for the assignment of backbone chemical shifts"}]}],"sequence_construct":"MGSSHHHHHHSQDPMEGSKTSNNSTMQVSFVSQRSSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEETNSGEEPFIETPRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLSEESTDTLLDQLDTY","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:27:29.737Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":150,"region_id":"DP01149r006","released":"2022_06","ec_id":"ECO:0006196","reference_html":"Characterisation of the conformational preference and dynamics of the intrinsically disordered N-terminal region of Beclin 1 by NMR spectroscopy. <i> Yao S, Lee EF, Pettikiriarachchi A, Evangelista M, Keizer DW, Fairlie WD. </i> Biochim Biophys Acta, 2016","statement":[{"text":"Unlike globular proteins, where amide protons involved in hydrogen bonding will display slow solvent exchange with the solvent (in the order of minutes or slower) and typically have a temperature coefficient more positive than -4.5 ppb/K, [41], no simple correlation between relatively rapid solvent exchange rates (Fig. 5B) and the measured temperature coefficients (Fig. 3C) were observed in the present study. Even in the presence of a 14 amino acids N-terminal purification tag, the residues that undergo the most significant exchange with the solvent water are near the N-terminus of BecN-150CSY. Notably, no significant difference in solvent exchange was observed for residues within the BH3 domain, hence, the degree of surface exposure, compared to the rest of the N-terminal domain.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-05-16T18:10:13.320Z","reference_source":"pmid","term_name":"disorder","reference_id":"27288992","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys18Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The 15N-labelled Beclin 1 N-terminal domain (residues 1-150) with all cysteines mutated to serines and a tyrosine included at the C-terminal of the construct for quantitation by UV spectroscopy (BecN-150CSY), was identical to the material used for the assignment of backbone chemical shifts."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys21Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The 15N-labelled Beclin 1 N-terminal domain (residues 1-150) with all cysteines mutated to serines and a tyrosine included at the C-terminal of the construct for quantitation by UV spectroscopy (BecN-150CSY), was identical to the material used for the assignment of backbone chemical shifts"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys137Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The 15N-labelled Beclin 1 N-terminal domain (residues 1-150) with all cysteines mutated to serines and a tyrosine included at the C-terminal of the construct for quantitation by UV spectroscopy (BecN-150CSY), was identical to the material used for the assignment of backbone chemical shifts"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys140Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The 15N-labelled Beclin 1 N-terminal domain (residues 1-150) with all cysteines mutated to serines and a tyrosine included at the C-terminal of the construct for quantitation by UV spectroscopy (BecN-150CSY), was identical to the material used for the assignment of backbone chemical shifts"}]}],"sequence_construct":"MGSSHHHHHHSQDPMEGSKTSNNSTMQVSFVSQRSSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEETNSGE EPFIETPRQDGVSRRFIPPA RMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLSEESTDTLLDQLDTY","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:27:31.238Z"}},{"start":1,"end":150,"reference_id":"27046249","reference_source":"pmid","reference_html":"The BECN1 N-terminal domain is intrinsically disordered. <i> Lee EF, Perugini MA, Pettikiriarachchi A, Evangelista M, Keizer DW, Yao S, Fairlie WD. </i> Autophagy, 2016","date":"2022-05-16T18:48:10.198Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP01149r007","statement":[{"text":"Upon gel-filtration chromatography, the major protein-containing peak eluted at an earlier retention time than expected for a protein of the calculated molecular mass based on the amino acid sequence (Fig. 1B). ","type":"Results"},{"text":"These data demonstrated that the protein exists as a 1.2S monomer (Fig. 1C), hence the behavior on gel-filtration is indicative of the protein being intrinsically disordered rather than oligomeric.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:27:32.939Z"}},{"start":1,"end":150,"reference_id":"27046249","reference_source":"pmid","reference_html":"The BECN1 N-terminal domain is intrinsically disordered. <i> Lee EF, Perugini MA, Pettikiriarachchi A, Evangelista M, Keizer DW, Yao S, Fairlie WD. </i> Autophagy, 2016","date":"2022-05-16T18:50:07.694Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP01149r008","statement":[{"text":"The highly elongated shape of the molecule, as determined by its high frictional ratio in the sedimentation velocity experiment (f/f0: 2.2), is also a characteristic of an intrinsically disordered protein.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:27:34.643Z"}},{"start":1,"end":150,"reference_id":"27046249","reference_source":"pmid","reference_html":"The BECN1 N-terminal domain is intrinsically disordered. <i> Lee EF, Perugini MA, Pettikiriarachchi A, Evangelista M, Keizer DW, Yao S, Fairlie WD. </i> Autophagy, 2016","date":"2022-05-16T18:51:02.416Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP01149r009","statement":[{"text":"The slightly anomalous migration on SDS-PAGE is likely due to the high positive charge content of the molecule, another characteristic of an intrinsically disordered protein.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:27:35.890Z"}},{"start":105,"end":130,"reference_id":"27046249","reference_source":"pmid","reference_html":"The BECN1 N-terminal domain is intrinsically disordered. <i> Lee EF, Perugini MA, Pettikiriarachchi A, Evangelista M, Keizer DW, Yao S, Fairlie WD. </i> Autophagy, 2016","date":"2022-05-17T14:09:08.857Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","region_id":"DP01149r010","statement":[{"text":"In solution competition assays, the IC50 (2.0 μM) value of BECN1(1–150)[4CS]Y was similar to that of a synthetic peptide whose sequence overlaps with the BECN1(BH3) domain (IC50 2.9 μM) and consistent with previously published binding data on BECN1(BH3) domain peptides.10,12,16 The similarity in the values between the BECN1(BH3) peptide and the entire N-terminal domain suggests the protein produced is fully functional and that regions outside of the BH3 domain are not involved in interactions with BCL2 family members.","type":"Results"},{"text":"BH3 domain of Beclin-1 corresponds to the region 105-130","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"Q07817","operator":null,"partner_start":1,"partner_end":218}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:27:50.305Z"}},{"start":98,"end":132,"reference_id":"27046249","reference_source":"pmid","reference_html":"The BECN1 N-terminal domain is intrinsically disordered. <i> Lee EF, Perugini MA, Pettikiriarachchi A, Evangelista M, Keizer DW, Yao S, Fairlie WD. </i> Autophagy, 2016","date":"2022-06-03T17:19:34.065Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys18Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The human BECN1 DNA encoding residues 1 to 150 was codon-optimized for expression in E. coli and cloned into the pET DUET-1 vector (Site I) (Novagen, 71146–3) at the BamHI/NotI sites, which fuses it to a hexahistdidine purification tag followed by a short linker sequence (MGSSHHHHHHSQDP). This served as a base construct for a subsequent construct in which all cysteines (i.e., residues 18, 21, 137, 140) were mutated to serine plus a C-terminal tyrosine was added to facilitate quantification by UV spectroscopy (called “BECN1(1–150)[4CS]Y”)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys21Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The human BECN1 DNA encoding residues 1 to 150 was codon-optimized for expression in E. coli and cloned into the pET DUET-1 vector (Site I) (Novagen, 71146–3) at the BamHI/NotI sites, which fuses it to a hexahistdidine purification tag followed by a short linker sequence (MGSSHHHHHHSQDP). This served as a base construct for a subsequent construct in which all cysteines (i.e., residues 18, 21, 137, 140) were mutated to serine plus a C-terminal tyrosine was added to facilitate quantification by UV spectroscopy (called “BECN1(1–150)[4CS]Y”)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys137Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The human BECN1 DNA encoding residues 1 to 150 was codon-optimized for expression in E. coli and cloned into the pET DUET-1 vector (Site I) (Novagen, 71146–3) at the BamHI/NotI sites, which fuses it to a hexahistdidine purification tag followed by a short linker sequence (MGSSHHHHHHSQDP). This served as a base construct for a subsequent construct in which all cysteines (i.e., residues 18, 21, 137, 140) were mutated to serine plus a C-terminal tyrosine was added to facilitate quantification by UV spectroscopy (called “BECN1(1–150)[4CS]Y”)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys140Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The human BECN1 DNA encoding residues 1 to 150 was codon-optimized for expression in E. coli and cloned into the pET DUET-1 vector (Site I) (Novagen, 71146–3) at the BamHI/NotI sites, which fuses it to a hexahistdidine purification tag followed by a short linker sequence (MGSSHHHHHHSQDP). This served as a base construct for a subsequent construct in which all cysteines (i.e., residues 18, 21, 137, 140) were mutated to serine plus a C-terminal tyrosine was added to facilitate quantification by UV spectroscopy (called “BECN1(1–150)[4CS]Y”)."}]}],"region_id":"DP01149r011","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":0.46,"db":"UniProt","id":"Q07817","statements":[{"type":"Methods","text":"To validate the interaction between BECN1(1–150)[4CS]Y and BCL2L1ΔC25, BCL2L1ΔC25 (0.46 mM) was titrated into the 13C/15N BECN1(1–150)[4CS]Y solution (0.145 mM) with the course of interaction monitored by 1H-15N HSQC spectra. "}]}],"sequence_construct":"MGSSHHHHHHSQDPMEGSKTSNNSTMQVSFVSQRSSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEETNSGEEPFIETPRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLSEESTDTLLDQLDTY","statement":[{"text":"When BCL2L1ΔC25 was titrated into the BECN1(1–150)[4CS]Y sample, only resonances located within or adjacent to the BH3 domain (residues 98 to 132) were significantly perturbed (Fig. 3A to H) with only a small number of new resonances detected in the BCL2L1ΔC25-bound form (highlighted in cyan circles in Fig. 3A). This indicates the exchange between the free and bound conformations of BECN1(1–150)[4CS]Y is intermediate (in the millisecond range) on the NMR chemical shift timescale.","type":"Results"},{"text":"BH3 domain of Beclin-1 corresponds to the region 105-130","type":"Curator statement"},{"text":"Interestingly, the large majority of resonances of BECN1(1–150)[4CS]Y were completely unaffected (both peak intensity and linewidth) by the binding of its BH3 domain with BCL2L1ΔC25 (except for a small loss in intensity in residues adjacent to Q40, Fig. 3B), indicating that nearly all residues outside of the BH3 domain are tumbling as freely when bound to BCL2L1 as in the unbound form, and do not adopt any secondary or tertiary structure elements that are not present in the free form.","type":"Results"},{"text":"In addition, the BH3 domain α-helix induced upon interaction with BCL2L1 reverts to a disordered state when the complex is dissociated by exposure to a competitive inhibitor.","type":"Abstract"},{"text":"More importantly, our NMR analysis showed that upon binding to BCL2L1, the whole of the N-terminal region except the BH3 domain remains unstructured, suggesting that this interaction does not “nucleate” additional structural transitions beyond the formation of the α-helical BH3 domain.","type":"Discussion"}],"states_connection":[{"source":"DP01149r002","target":"DP01149r012"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:27:46.981Z"}},{"start":105,"end":130,"reference_id":"27046249","reference_source":"pmid","reference_html":"The BECN1 N-terminal domain is intrinsically disordered. <i> Lee EF, Perugini MA, Pettikiriarachchi A, Evangelista M, Keizer DW, Yao S, Fairlie WD. </i> Autophagy, 2016","date":"2022-05-17T14:10:49.407Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys18Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The human BECN1 DNA encoding residues 1 to 150 was codon-optimized for expression in E. coli and cloned into the pET DUET-1 vector (Site I) (Novagen, 71146–3) at the BamHI/NotI sites, which fuses it to a hexahistdidine purification tag followed by a short linker sequence (MGSSHHHHHHSQDP). This served as a base construct for a subsequent construct in which all cysteines (i.e., residues 18, 21, 137, 140) were mutated to serine plus a C-terminal tyrosine was added to facilitate quantification by UV spectroscopy (called “BECN1(1–150)[4CS]Y”)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys21Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The human BECN1 DNA encoding residues 1 to 150 was codon-optimized for expression in E. coli and cloned into the pET DUET-1 vector (Site I) (Novagen, 71146–3) at the BamHI/NotI sites, which fuses it to a hexahistdidine purification tag followed by a short linker sequence (MGSSHHHHHHSQDP). This served as a base construct for a subsequent construct in which all cysteines (i.e., residues 18, 21, 137, 140) were mutated to serine plus a C-terminal tyrosine was added to facilitate quantification by UV spectroscopy (called “BECN1(1–150)[4CS]Y”)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys137Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The human BECN1 DNA encoding residues 1 to 150 was codon-optimized for expression in E. coli and cloned into the pET DUET-1 vector (Site I) (Novagen, 71146–3) at the BamHI/NotI sites, which fuses it to a hexahistdidine purification tag followed by a short linker sequence (MGSSHHHHHHSQDP). This served as a base construct for a subsequent construct in which all cysteines (i.e., residues 18, 21, 137, 140) were mutated to serine plus a C-terminal tyrosine was added to facilitate quantification by UV spectroscopy (called “BECN1(1–150)[4CS]Y”)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys140Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The human BECN1 DNA encoding residues 1 to 150 was codon-optimized for expression in E. coli and cloned into the pET DUET-1 vector (Site I) (Novagen, 71146–3) at the BamHI/NotI sites, which fuses it to a hexahistdidine purification tag followed by a short linker sequence (MGSSHHHHHHSQDP). This served as a base construct for a subsequent construct in which all cysteines (i.e., residues 18, 21, 137, 140) were mutated to serine plus a C-terminal tyrosine was added to facilitate quantification by UV spectroscopy (called “BECN1(1–150)[4CS]Y”)."}]}],"region_id":"DP01149r012","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":0.46,"db":"UniProt","id":"Q07817","statements":[{"type":"Methods","text":"To validate the interaction between BECN1(1–150)[4CS]Y and BCL2L1ΔC25, BCL2L1ΔC25 (0.46 mM) was titrated into the 13C/15N BECN1(1–150)[4CS]Y solution (0.145 mM) with the course of interaction monitored by 1H-15N HSQC spectra. "}]}],"sequence_construct":"MGSSHHHHHHSQDPMEGSKTSNNSTMQVSFVSQRSSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEETNSGEEPFIETPRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLSEESTDTLLDQLDTY","statement":[{"text":"In addition, the BH3 domain α-helix induced upon interaction with BCL2L1 reverts to a disordered state when the complex is dissociated by exposure to a competitive inhibitor.","type":"Abstract"},{"text":"BH3 domain of Beclin-1 corresponds to the region 105-130 ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:27:37.245Z"}},{"start":105,"end":130,"reference_id":"27046249","reference_source":"pmid","reference_html":"The BECN1 N-terminal domain is intrinsically disordered. <i> Lee EF, Perugini MA, Pettikiriarachchi A, Evangelista M, Keizer DW, Yao S, Fairlie WD. </i> Autophagy, 2016","date":"2022-05-17T14:09:29.939Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys18Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The human BECN1 DNA encoding residues 1 to 150 was codon-optimized for expression in E. coli and cloned into the pET DUET-1 vector (Site I) (Novagen, 71146–3) at the BamHI/NotI sites, which fuses it to a hexahistdidine purification tag followed by a short linker sequence (MGSSHHHHHHSQDP). This served as a base construct for a subsequent construct in which all cysteines (i.e., residues 18, 21, 137, 140) were mutated to serine plus a C-terminal tyrosine was added to facilitate quantification by UV spectroscopy (called “BECN1(1–150)[4CS]Y”)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys21Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The human BECN1 DNA encoding residues 1 to 150 was codon-optimized for expression in E. coli and cloned into the pET DUET-1 vector (Site I) (Novagen, 71146–3) at the BamHI/NotI sites, which fuses it to a hexahistdidine purification tag followed by a short linker sequence (MGSSHHHHHHSQDP). This served as a base construct for a subsequent construct in which all cysteines (i.e., residues 18, 21, 137, 140) were mutated to serine plus a C-terminal tyrosine was added to facilitate quantification by UV spectroscopy (called “BECN1(1–150)[4CS]Y”)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys137Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The human BECN1 DNA encoding residues 1 to 150 was codon-optimized for expression in E. coli and cloned into the pET DUET-1 vector (Site I) (Novagen, 71146–3) at the BamHI/NotI sites, which fuses it to a hexahistdidine purification tag followed by a short linker sequence (MGSSHHHHHHSQDP). This served as a base construct for a subsequent construct in which all cysteines (i.e., residues 18, 21, 137, 140) were mutated to serine plus a C-terminal tyrosine was added to facilitate quantification by UV spectroscopy (called “BECN1(1–150)[4CS]Y”)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys140Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The human BECN1 DNA encoding residues 1 to 150 was codon-optimized for expression in E. coli and cloned into the pET DUET-1 vector (Site I) (Novagen, 71146–3) at the BamHI/NotI sites, which fuses it to a hexahistdidine purification tag followed by a short linker sequence (MGSSHHHHHHSQDP). This served as a base construct for a subsequent construct in which all cysteines (i.e., residues 18, 21, 137, 140) were mutated to serine plus a C-terminal tyrosine was added to facilitate quantification by UV spectroscopy (called “BECN1(1–150)[4CS]Y”)."}]}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q07817","operator":null,"partner_start":1,"partner_end":218}],"region_id":"DP01149r013","sequence_construct":"MGSSHHHHHHSQDPMEGSKTSNNSTMQVSFVSQRSSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEETNSGEEPFIETPRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLSEESTDTLLDQLDTY","statement":[{"text":"When BCL2L1ΔC25 was titrated into the BECN1(1–150)[4CS]Y sample, only resonances located within or adjacent to the BH3 domain (residues 98 to 132) were significantly perturbed (Fig. 3A to H) with only a small number of new resonances detected in the BCL2L1ΔC25-bound form (highlighted in cyan circles in Fig. 3A). This indicates the exchange between the free and bound conformations of BECN1(1–150)[4CS]Y is intermediate (in the millisecond range) on the NMR chemical shift timescale.","type":"Results"},{"text":"BH3 domain of Beclin-1 corresponds to the region 105-130","type":"Curator statement"},{"text":"Interestingly, the large majority of resonances of BECN1(1–150)[4CS]Y were completely unaffected (both peak intensity and linewidth) by the binding of its BH3 domain with BCL2L1ΔC25 (except for a small loss in intensity in residues adjacent to Q40, Fig. 3B), indicating that nearly all residues outside of the BH3 domain are tumbling as freely when bound to BCL2L1 as in the unbound form, and do not adopt any secondary or tertiary structure elements that are not present in the free form.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:27:54.118Z"}},{"start":105,"end":130,"reference_id":"24115198","reference_source":"pmid","reference_html":"Intrinsically disordered regions in autophagy proteins. <i> Mei Y, Su M, Soni G, Salem S, Colbert CL, Sinha SC. </i> Proteins, 2014","date":"2022-05-17T13:20:28.068Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP01149r014","statement":[{"text":"As expected for disordered peptides,23, 24 the 1D-1H NMR spectra (Figure 3A) measured for the BH3D lacked peaks upfield of the strong methyl peaks at 0.8 ppm; contained broad peaks at about 8.3 ppm, the region characteristic for amide groups in random-coil conformation; and had little signal dispersion visible downfield of ~8.5 ppm, with the few peaks visible below 8.5 ppm being attributable to Trp sidechains.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:27:38.183Z"}},{"start":105,"end":130,"reference_id":"24115198","reference_source":"pmid","reference_html":"Intrinsically disordered regions in autophagy proteins. <i> Mei Y, Su M, Soni G, Salem S, Colbert CL, Sinha SC. </i> Proteins, 2014","date":"2022-05-17T13:21:45.421Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006200","ec_ontology":"ECO","ec_name":"circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP01149r015","statement":[{"text":"The BECN1 BH3D CD spectra showed a large single negative transition at ~195 nm, indicative of a random coil conformation (Figure 3B); compared to the CD spectra of α-helical polypeptides which are expected to display a positive band at ~192 nm and a large negative split transition at 208 nm and 222 nm; and of β-strand polypeptides which would show a positive band at 195 nm and a negative band at 218 nm.","type":"Results"},{"text":"In contrast to the isolated BH3D, the molar ellipticity at 222 nm indicated that a BECN1 BH3D+HD+CCD construct has a much higher helical content, although not as high as that observed for a HD+CCD construct. This reduction in helical content suggests that the BH3D is disordered even when attached to the helical domains that follow it.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:27:39.571Z"}},{"start":105,"end":130,"reference_id":"24115198","reference_source":"pmid","reference_html":"Intrinsically disordered regions in autophagy proteins. <i> Mei Y, Su M, Soni G, Salem S, Colbert CL, Sinha SC. </i> Proteins, 2014","date":"2022-05-17T14:51:13.579Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P10415","operator":null,"partner_start":1,"partner_end":218}],"region_id":"DP01149r016","statement":[{"text":"ITC measurements indicate that the BECN1 BH3D binds to BCL2 with a Kd of 10.4 μM (Table IV). Binding is abolished by Ala substitutions of the single residues L112, L116, or F123, as well as the double G120E+D121A substitution (DS).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:27:56.043Z"}},{"start":105,"end":130,"reference_id":"24115198","reference_source":"pmid","reference_html":"Intrinsically disordered regions in autophagy proteins. <i> Mei Y, Su M, Soni G, Salem S, Colbert CL, Sinha SC. </i> Proteins, 2014","date":"2022-05-17T13:44:52.977Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006200","ec_ontology":"ECO","ec_name":"circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP01149r017","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":0.001,"db":"UniProt","id":"P10415","statements":[{"type":"Methods","text":"BECN1 constructs were diluted to 10–100 μM in a “CD buffer” comprising 10 mM potassium phosphate, pH 7.6, with 100 mM (NH4)2SO4. For experiments involving complexes of BCL2 and BECN1 BH3D-derived peptides, the BCL2 and peptides were mixed in 1:1, 1:10 or 2:1 molar ratios, then dialyzed against and diluted in the CD buffer. "}]}],"statement":[{"text":"This secondary structure content is unchanged upon addition of equimolar or 0.5-fold molar BECN1 BH3D, suggesting that the BH3D folds into a helix upon binding (Table III).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:27:40.885Z"}},{"start":105,"end":130,"reference_id":"24115198","reference_source":"pmid","reference_html":"Intrinsically disordered regions in autophagy proteins. <i> Mei Y, Su M, Soni G, Salem S, Colbert CL, Sinha SC. </i> Proteins, 2014","date":"2022-06-03T17:19:13.371Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006200","ec_ontology":"ECO","ec_name":"circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP01149r018","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":0.001,"db":"UniProt","id":"P10415","statements":[{"type":"Methods","text":"BECN1 constructs were diluted to 10–100 μM in a “CD buffer” comprising 10 mM potassium phosphate, pH 7.6, with 100 mM (NH4)2SO4. For experiments involving complexes of BCL2 and BECN1 BH3D-derived peptides, the BCL2 and peptides were mixed in 1:1, 1:10 or 2:1 molar ratios, then dialyzed against and diluted in the CD buffer."}]}],"statement":[{"text":"This secondary structure content is unchanged upon addition of equimolar or 0.5-fold molar BECN1 BH3D, suggesting that the BH3D folds into a helix upon binding (Table III). However, addition of a 10-fold molar excess of the BH3D reduces the helical content of the sample to 76%, consistent with a significant population of BH3D molecules being in a random coil conformation. In contrast to the BH3D, addition of equimolar or 10-fold excess molar DS BH3D peptide dramatically reduces the helical content of the sample to ~67% and ~45% respectively, indicating that there is no change in the secondary structure of the DS BH3D peptide, consistent with lack of binding to BCL2s.","type":"Results"},{"text":"Thus, the combined information from IDR predictions, CD, NMR and co-complex crystal structures indicates that the BECN1 BH3D undergoes a disorder to αhelix transition upon binding.","type":"Results"}],"states_connection":[{"source":"DP01149r015","target":"DP01149r017"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:27:48.400Z"}},{"start":141,"end":156,"reference_id":"26937551","reference_source":"pmid","reference_html":"Conformational Flexibility Enables the Function of a BECN1 Region Essential for Starvation-Mediated Autophagy. <i> Mei Y, Ramanathan A, Glover K, Stanley C, Sanishvili R, Chakravarthy S, Yang Z, Colbert CL, Sinha SC. </i> Biochemistry, 2016","date":"2022-05-17T14:28:08.687Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":20,"statements":[{"type":"Methods","text":"BECN1 FHD crystals were grown at 20 °C by sitting drop vapor diffusion from a drop consisting of 1 µl of 10 mg/m1FHDin 25 mM HEPES, pH 7.5; 250 mM NaCl; 2 mM b-mercaptoethanol and 1 µl of reservoir solution, comprising 100 mM sodium citrate tribasic dihydrate, pH 5.6; 250 mM potassium sodium tartrate tetrahydrate; and 2.2 M ammonium sulfate."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7.5,"statements":[{"type":"Methods","text":"BECN1 FHD crystals were grown at 20 °C by sitting drop vapor diffusion from a drop consisting of 1 µl of 10 mg/m1FHDin 25 mM HEPES, pH 7.5; 250 mM NaCl; 2 mM b-mercaptoethanol and 1 µl of reservoir solution, comprising 100 mM sodium citrate tribasic dihydrate, pH 5.6; 250 mM potassium sodium tartrate tetrahydrate; and 2.2 M ammonium sulfate."}]}],"cross_refs":[{"db":"PDB","id":"5EFM"}],"region_id":"DP01149r019","statement":[{"text":"Electron density corresponding to residues 141–156 is missing, suggesting that similar to the BH3D preceding it (16), this region may be unstructured in certain physiological contexts.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T11:14:55.964Z"}},{"start":104,"end":131,"reference_id":"17659302","reference_source":"pmid","reference_html":"Molecular basis of Bcl-xL's target recognition versatility revealed by the structure of Bcl-xL in complex with the BH3 domain of Beclin-1. <i> Feng W, Huang S, Wu H, Zhang M. </i> J Mol Biol, 2007","date":"2022-05-17T15:05:54.380Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q07817","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01149r020","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q07817","statements":[{"type":"Methods","text":"The Bcl-xL constructs used in this study lacked amino acid residues 45–84 and 197–233."}]}],"statement":[{"text":"A 72 residue fragment (residues 104–175) in the N-terminal region of Beclin-1 was found to bind robustly to Bcl-xL in a pull down assay (Figure 1(a)). Deletion of residues 104–131 eliminated interaction between Beclin-1 and Bcl-xL (Figure 1(a)), indicating that this 28 residue fragment of Beclin-1 is required for the protein to interact with Bcl-xL.","type":"Results"},{"text":"We further noted that Trx-Beclin-1 (104-131) binds to GST-Bcl-xL in a similar manner when compared to Trx-Beclin-1 (104-175), suggesting that the 28 residue fragment of Beclin-1 (residues 104–131) is likely to be sufficient for binding to Bcl-xL.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:27:56.906Z"}},{"start":104,"end":131,"reference_id":"17659302","reference_source":"pmid","reference_html":"Molecular basis of Bcl-xL's target recognition versatility revealed by the structure of Bcl-xL in complex with the BH3 domain of Beclin-1. <i> Feng W, Huang S, Wu H, Zhang M. </i> J Mol Biol, 2007","date":"2022-05-17T15:07:54.270Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"2PON"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q07817","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01149r021","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q07817","statements":[{"type":"Methods","text":"The Bcl-xL constructs used in this study lacked amino acid residues 45–84 and 197–233."}]}],"statement":[{"text":"Mixing a peptide fragment encompassing Beclin-1 (104-131) (Figure 1(d) and (e)), but not its immediate C-terminal fragment (residues 132–175, data not shown), with Bcl-xL induced large chemical shift changes to a subset of resonances in the 1H-15N heteronuclear single quantum coherence (HSQC) spectrum of 15N-labeled Bcl-xL, further supporting that the 28 residue fragment of Beclin-1 (residues 104–131) binds to Bcl-xL specifically. ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:27:58.455Z"}},{"start":104,"end":131,"reference_id":"17659302","reference_source":"pmid","reference_html":"Molecular basis of Bcl-xL's target recognition versatility revealed by the structure of Bcl-xL in complex with the BH3 domain of Beclin-1. <i> Feng W, Huang S, Wu H, Zhang M. </i> J Mol Biol, 2007","date":"2022-05-17T15:15:08.309Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006277","ec_ontology":"ECO","ec_name":"fluorescence polarization evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q07817","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01149r022","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q07817","statements":[{"type":"Methods","text":"The Bcl-xL constructs used in this study lacked amino acid residues 45–84 and 197–233."}]}],"statement":[{"text":"We found that Bcl-xL binds to Beclin-1 (104-131) with a relatively high affinity (Kd ∼1.4 μM) (Figure 1(c)). Longer Beclin-1 fragments with extensions in both the N and C termini of this 28 residue peptide did not increase the binding affinity of Beclin-1 to Bcl-xL (data not shown), further demonstrating that the 28 residue peptide fragment identified here represents the complete Bcl-xL-binding domain of Beclin-1.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:28:00.275Z"}},{"start":105,"end":130,"reference_id":"18797192","reference_source":"pmid","reference_html":"Molecular basis of the regulation of Beclin 1-dependent autophagy by the gamma-herpesvirus 68 Bcl-2 homolog M11. <i> Sinha S, Colbert CL, Becker N, Wei Y, Levine B. </i> Autophagy, 2008","date":"2022-05-17T19:48:09.749Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q07817","operator":null,"partner_start":2,"partner_end":136}],"region_id":"DP01149r023","statement":[{"text":"Analysis of these NMR spectra showed that binding of the Beclin 1 BH3 domain affects extensive regions of M11, including not only residues of the hydrophobic groove and those that undergo conformational changes, but also residues from other regions of M11 (Fig. 2A). ","type":"Abstract"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:28:01.844Z"}},{"start":105,"end":130,"reference_id":"18797192","reference_source":"pmid","reference_html":"Molecular basis of the regulation of Beclin 1-dependent autophagy by the gamma-herpesvirus 68 Bcl-2 homolog M11. <i> Sinha S, Colbert CL, Becker N, Wei Y, Levine B. </i> Autophagy, 2008","date":"2022-05-17T19:48:30.614Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"3DVU"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q07817","operator":null,"partner_start":2,"partner_end":136}],"region_id":"DP01149r024","statement":[{"text":"Our 2.5 Å crystal structure of the M11-Beclin 1 BH3 domain complex (Fig. 1) shows that the Beclin 1 BH3 domain binds to a hydrophobic surface groove on M11, similar to the binding of BH3 domains of proapoptotic proteins to other antiapoptotic Bcl-2s.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:28:03.075Z"}},{"start":1,"end":135,"reference_id":"18797192","reference_source":"pmid","reference_html":"Molecular basis of the regulation of Beclin 1-dependent autophagy by the gamma-herpesvirus 68 Bcl-2 homolog M11. <i> Sinha S, Colbert CL, Becker N, Wei Y, Levine B. </i> Autophagy, 2008","date":"2022-05-18T15:16:29.546Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q07817","operator":null,"partner_start":1,"partner_end":136}],"region_id":"DP01149r025","statement":[{"text":"The Beclin 1 (1–135) fragment binds to γHV68 M11 with approximately 40-fold higher affinity than cBcl-2 and 65-fold higher affinity than KSHV Bcl-2 (Table 1).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:28:04.369Z"}},{"start":105,"end":130,"reference_id":"18797192","reference_source":"pmid","reference_html":"Molecular basis of the regulation of Beclin 1-dependent autophagy by the gamma-herpesvirus 68 Bcl-2 homolog M11. <i> Sinha S, Colbert CL, Becker N, Wei Y, Levine B. </i> Autophagy, 2008","date":"2022-05-18T16:22:15.251Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P10415","operator":null,"partner_start":1,"partner_end":218}],"region_id":"DP01149r026","statement":[{"text":"The Beclin 1 (1–135) fragment binds to γHV68 M11 with approximately 40-fold higher affinity than cBcl-2 and 65-fold higher affinity than KSHV Bcl-2 (Table 1).","type":"Results"},{"text":"Thus, compared to the Beclin 1 BH3 domain, the 1–135 fragment binds approximately five-fold more strongly to M11, but does not bind significantly better to either cBcl-2 or KSHV Bcl-2.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:28:05.855Z"}},{"start":105,"end":130,"reference_id":"18797192","reference_source":"pmid","reference_html":"Molecular basis of the regulation of Beclin 1-dependent autophagy by the gamma-herpesvirus 68 Bcl-2 homolog M11. <i> Sinha S, Colbert CL, Becker N, Wei Y, Levine B. </i> Autophagy, 2008","date":"2022-05-18T16:40:34.898Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0010506","term_name":"regulation of autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007106","ec_ontology":"ECO","ec_name":"green fluorescent protein fusion protein localization evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IDA","region_id":"DP01149r027","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P10415"}],"statement":[{"text":"Beclin 1-dependent, starvation-induced autophagy levels are downregulated by cBcl-2 (p < 0.001 for cBcl-2 versus empty vector), and even more potently by KSHV Bcl-2 (p < 0.0003 for KSHV Bcl-2 versus empty vector).","type":"Results"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.\" [GOC:dph, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:28:11.280Z"}},{"start":105,"end":130,"reference_id":"30626284","reference_source":"pmid","reference_html":"Structural insights into BCL2 pro-survival protein interactions with the key autophagy regulator BECN1 following phosphorylation by STK4/MST1. <i> Lee EF, Smith NA, Soares da Costa TP, Meftahi N, Yao S, Harris TJ, Tran S, Pettikiriarachchi A, Perugini MA, Keizer DW, Evangelista M, Smith BJ, Fairlie WD. </i> Autophagy, 2019","date":"2022-05-18T19:56:16.133Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5VAU"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P10415","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01149r029","statement":[{"text":"We first solved a structure of BCL2 bound to wild-type BECN1 BH3 (PDB code 5VAU, Table 2). This structure has four molecules in the asu, affording four views of the interaction (Figure 3(a)).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-24T13:29:00.911Z"}},{"start":105,"end":130,"reference_id":"30626284","reference_source":"pmid","reference_html":"Structural insights into BCL2 pro-survival protein interactions with the key autophagy regulator BECN1 following phosphorylation by STK4/MST1. <i> Lee EF, Smith NA, Soares da Costa TP, Meftahi N, Yao S, Harris TJ, Tran S, Pettikiriarachchi A, Perugini MA, Keizer DW, Evangelista M, Smith BJ, Fairlie WD. </i> Autophagy, 2019","date":"2022-05-18T20:28:21.486Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q07817","operator":null,"partner_start":1,"partner_end":218}],"region_id":"DP01149r030","statement":[{"text":"The wild-type BECN1 BH3 yielded IC50 values consistent with what we and others have reported previously for binding to BCL2L1 [3,4,18–20], while the p-T108 peptide bound slightly, though significantly, tighter (2.0 μM versus 1.2 μM, p < 0.0001) (Table 1, Figure S1(a,b)).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-24T13:24:54.643Z"}},{"start":96,"end":102,"reference_id":"30767700","reference_source":"pmid","reference_html":"Members of the autophagy class III phosphatidylinositol 3-kinase complex I interact with GABARAP and GABARAPL1 via LIR motifs. <i> Birgisdottir ÅB, Mouilleron S, Bhujabal Z, Wirth M, Sjøttem E, Evjen G, Zhang W, Lee R, O'Reilly N, Tooze SA, Lamark T, Johansen T. </i> Autophagy, 2019","date":"2022-05-19T13:40:18.598Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"6HOI"},{"db":"PDB","id":"6HOJ"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9H0R8","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01149r031","statement":[{"text":"PIK3C3, BECN1 and ATG14 WT LIR motifs bound to GABARAPL1 in and extended conformation with the two core hydrophobic residues in position 0 and +3 deeply bound to the hydrophobic pockets HP1 and HP2.","type":"Results"},{"text":"The specific interactions observed in WT BECN1 structures were: 1) Hydrophobic contact between L99 (BECN1) in position +2 and the edge of HP2; 2) two hydrogen bonds between the guanidine of R28 (GABARAPL1) and the carbonyls of G101 (BECN1)-L100 (BECN1), as well as a third one between the carbonyl of N95 (BECN1) (or the side chain of S96 for the peptide structure) and the side chain of K48 (GABARAPL1) (Figure 5(a,b)).","type":"Results"},{"text":"BECN1 LIR motif coresponds to the 97-100 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-24T14:01:34.557Z"}},{"start":76,"end":105,"reference_id":"27179590","reference_source":"pmid","reference_html":"Identifying intrinsically disordered protein regions likely to undergo binding-induced helical transitions. <i> Glover K, Mei Y, Sinha SC. </i> Biochim Biophys Acta, 2016","date":"2022-05-19T14:36:33.227Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP01149r032","statement":[{"text":"Authors show the region is intrinsically unstructured by itslarge negative ellipticity at 200 nm and moderate ellipticity at 190 nm, typical of IDR","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:27:43.612Z"}},{"start":50,"end":78,"reference_id":"27179590","reference_source":"pmid","reference_html":"Identifying intrinsically disordered protein regions likely to undergo binding-induced helical transitions. <i> Glover K, Mei Y, Sinha SC. </i> Biochim Biophys Acta, 2016","date":"2022-05-19T14:37:02.451Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP01149r033","statement":[{"text":"Authors show the region is intrinsically unstructured by itslarge negative ellipticity at 200 nm and moderate ellipticity at 190 nm, typical of IDR","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:27:44.909Z"}},{"start":105,"end":130,"reference_id":"27179590","reference_source":"pmid","reference_html":"Identifying intrinsically disordered protein regions likely to undergo binding-induced helical transitions. <i> Glover K, Mei Y, Sinha SC. </i> Biochim Biophys Acta, 2016","date":"2022-05-19T14:44:09.842Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP01149r034","statement":[{"text":"Authors show the region is intrinsically unstructured by itslarge negative ellipticity at 200 nm and moderate ellipticity at 190 nm, typical of IDR","type":"Curator statement"},{"text":"Although none of these IDRs have a helical content sufficient for formation of a stable helix in the absence of TFE, addition of TFE induces a significant disorder-to-helix transition in all three IDRs (Table 4).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:27:45.529Z"}},{"start":96,"end":101,"reference_id":"30767700","reference_source":"pmid","reference_html":"Members of the autophagy class III phosphatidylinositol 3-kinase complex I interact with GABARAP and GABARAPL1 via LIR motifs. <i> Birgisdottir ÅB, Mouilleron S, Bhujabal Z, Wirth M, Sjøttem E, Evjen G, Zhang W, Lee R, O'Reilly N, Tooze SA, Lamark T, Johansen T. </i> Autophagy, 2019","date":"2022-05-26T14:05:40.709Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q9H0R8","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"O95166","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP01149r035","statement":[{"text":"The putative core motif of BECN1 (FTLI amino acids F97-I100) was also mutated (F97A, I100A) and tested for interaction with the recombinant GST-Atg8 homologs. The mutations significantly reduced binding and confirmed a functional LIR motif in BECN1 (Figure 2).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe97Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile100Ala","start":null,"end":null,"position":null}],"sequence_construct":"MEGSKTSNNSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEETNSGEEPFIETPRQDGVSRRFIPPARMMSTESANSATLAGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEILEQMNEDDSEQLQMELKELALEEERLIQELEDVEKNRKIVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQMRYAQTQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:29:12.076Z"}},{"start":97,"end":100,"reference_id":"30767700","reference_source":"pmid","reference_html":"Members of the autophagy class III phosphatidylinositol 3-kinase complex I interact with GABARAP and GABARAPL1 via LIR motifs. <i> Birgisdottir ÅB, Mouilleron S, Bhujabal Z, Wirth M, Sjøttem E, Evjen G, Zhang W, Lee R, O'Reilly N, Tooze SA, Lamark T, Johansen T. </i> Autophagy, 2019","date":"2022-06-28T10:46:34.614Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":1,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser90Glu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser93Glu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser96Glu","start":null,"end":null,"position":null}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9H0R8","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"O95166","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP01149r036","sequence_construct":"MEGSKTSNNSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEETNSGEEPFIETPRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEILEQMNEDDSEQLQMELKELALEEERLIQELEDVEKNRKIVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQMRYAQTQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK","statement":[{"text":"BECN1 only bound with significant affinity to GABARAP and GABARAPL1.","type":"Results"},{"text":"The region includes the canonical LIR motif \"FTLI\"","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T12:29:04.666Z"}},{"start":97,"end":100,"reference_id":"30767700","reference_source":"pmid","reference_html":"Members of the autophagy class III phosphatidylinositol 3-kinase complex I interact with GABARAP and GABARAPL1 via LIR motifs. <i> Birgisdottir ÅB, Mouilleron S, Bhujabal Z, Wirth M, Sjøttem E, Evjen G, Zhang W, Lee R, O'Reilly N, Tooze SA, Lamark T, Johansen T. </i> Autophagy, 2019","date":"2022-06-28T10:47:07.928Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe97Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile100Ala","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP01149r037","statement":[{"text":"The putative core motif of BECN1 (FTLI amino acids F97-I100) was also mutated (F97A, I100A) and tested for interaction with the recombinant GST-Atg8 homologs. The mutations significantly reduced binding and confirmed a functional LIR motif in BECN1 (Figure 2).","type":"Results"},{"text":"The region includes the canonical LIR motif \"FTLI\"","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T12:29:22.145Z"}}],"released":"2018_11","uniref100":"UniRef100_Q14457","date":"2018-06-25T21:24:43.000Z","acc":"Q14457","name":"Beclin-1","length":450,"organism":"Homo sapiens","dataset":["Autophagy-related proteins"],"UniParc":"UPI000016A9FF","genes":[{"name":{"value":"BECN1"},"synonyms":[{"value":"GT197"}]}],"alphafold_very_low_content":0.17555555555555555,"disorder_content":0.3466666666666667,"disprot_consensus":{"full":[{"start":1,"end":97,"type":"D"},{"start":98,"end":132,"type":"T"},{"start":133,"end":156,"type":"D"}],"Structural state":[{"start":1,"end":156,"type":"D"}],"Molecular function":[{"start":1,"end":135,"type":"F"}],"Structural transition":[{"start":98,"end":132,"type":"T"}],"Biological process":[{"start":97,"end":100,"type":"F"},{"start":105,"end":130,"type":"F"}]}},{"acc":"P03255","sequence":"MRHIICHGGVITEEMAASLLDQLIEEVLADNLPPPSHFEPPTLHELYDLDVTAPEDPNEEAVSQIFPDSVMLAVQEGIDLLTFPPAPGSPEPPHLSRQPEQPEQRALGPVSMPNLVPEVIDLTCHEAGFPPSDDEDEEGEEFVLDYVEHPGHGCRSCHYHRRNTGDPDIMCSLCYMRTCGMFVYSPVSEPEPEPEPEPEPARPTRRPKMAPAILRRPTSPVSRECNSSTDSCDSGPSNTPPEIHPVVPLCPIKPVAVRVGGRRQAVECIEDLLNEPGQPLDLSCKRPRP","creator":"jbergier","dataset":["Viral proteins"],"date":"2018-06-25T22:16:38.000Z","disprot_id":"DP01150","features":{"pfam":[{"id":"PF02703","name":"Early E1A protein","start":1,"end":163}]},"genes":[],"length":289,"name":"Early E1A protein","ncbi_taxon_id":28285,"organism":"Human adenovirus C serotype 5","regions_counter":25,"released":"2018_11","taxonomy":["Viruses","Varidnaviria","Bamfordvirae","Preplasmiviricota","Tectiliviricetes","Rowavirales","Adenoviridae","Mastadenovirus"],"UniParc":"UPI0000001815","uniref100":"UniRef100_P03255","uniref50":"UniRef50_P03255","uniref90":"UniRef90_P03255","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":53,"end":91,"interaction_partner":[],"reference_html":"Mapping the interactions of adenoviral E1A proteins with the p160 nuclear receptor coactivator binding domain of CBP. <i> Haberz P, Arai M, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> Protein Sci, 2016","reference_id":"27699893","region_id":"DP01150r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Binding of the NCBD to 15N‐labeled AdV5 E1A(53–91) leads to large, fast exchange shifts of E1A cross peaks (Supporting Information Fig. S11); the chemical shift changes are considerably larger than for the corresponding AdV12 E1A(52–81) construct [Fig.3(C)]. This may reflect local sequence differences or, more likely, the presence of additional hydrophobic residues beyond the C‐terminus of the AdV5 CR1 motif that are absent from AdV12[Fig.1(A)].","_id":"685af523b4ac24d5329d8db5"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T13:42:40.592Z","_id":"685af523b4ac24d5329d8db6"},"version":3,"_id":"685af523b4ac24d5329d8db4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":91,"interaction_partner":[],"reference_html":"Mapping the interactions of adenoviral E1A proteins with the p160 nuclear receptor coactivator binding domain of CBP. <i> Haberz P, Arai M, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> Protein Sci, 2016","reference_id":"27699893","region_id":"DP01150r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The AdV5 E1A constructs are intrinsically disordered, with chemical shifts that deviate little from random coil values except for residues E13‐D21, which have a small propensity to form helical structure (∼30% population)","_id":"685af523b4ac24d5329d8dbe"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T13:50:26.023Z","_id":"685af523b4ac24d5329d8dbf"},"version":2,"_id":"685af523b4ac24d5329d8dbd","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":91,"interaction_partner":[{"db":"UniProt","id":"Q92793","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8dc7"},{"db":"UniProt","id":"Q09472","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8dc8"}],"reference_html":"Mapping the interactions of adenoviral E1A proteins with the p160 nuclear receptor coactivator binding domain of CBP. <i> Haberz P, Arai M, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> Protein Sci, 2016","reference_id":"27699893","region_id":"DP01150r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Titrations were performed in which aliquots of the unlabeled NCBD were added to 15N‐labeled AdV5 E1A(1‐91) and AdV12 E1A(1‐81) in order to map the NCBD binding sites (Supporting Information Figs. S13 and S17).","_id":"685af523b4ac24d5329d8dc3"},{"type":"Results","text":"The chemical shift perturbations reveal three NCBD binding sites in homologous regions of AdV5 and AdV12 E1A; for AdV12, the NCBD binding sites are located between residues L10‐V30, S40‐L47, and V61‐F78 ​[Fig.3(B)].","_id":"685af523b4ac24d5329d8dc4"},{"type":"Discussion","text":"Thus the interaction between E1A and TAZ2 can be characterized as a partly “fuzzy” complex, with one portion of the E1A sequence participating in a strong interaction with TAZ2, while the other portion, corresponding to the N‐terminal region, participating in an interaction characterized by multiple states in intermediate exchange on the NMR time scale.","_id":"685af523b4ac24d5329d8dc5"},{"type":"Discussion","text":"For AdV5 E1A, the precise boundaries of the NCBD binding sites were more difficult to identify due to cross peak overlap and because of differences in the exchange regime, with many AdV5 E1A residues exchange broadened or in slow exchange on the chemical shift time scale.","_id":"685af523b4ac24d5329d8dc6"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T13:51:59.445Z","_id":"685af523b4ac24d5329d8dc9"},"version":4,"_id":"685af523b4ac24d5329d8dc2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":139,"interaction_partner":[],"reference_html":"Structural basis for subversion of cellular control mechanisms by the adenoviral E1A oncoprotein. <i> Ferreon JC, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> Proc Natl Acad Sci U S A, 2009","reference_id":"19651603","region_id":"DP01150r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"More dramatic differences are observed between\nthe HSQC spectra of free and bound E1A (Fig. 2B). E1A is\nlargely unstructured in the free state as seen by the limited\nchemical shift dispersion in the 1H dimension; backbone resonances\nof both E1A(53–91) and E1A(1–139) show little deviation\nof chemical shifts from random coil values (Fig. S2 A and\nB)","_id":"685af523b4ac24d5329d8dcb"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T13:50:16.711Z","_id":"685af523b4ac24d5329d8dcc"},"version":2,"_id":"685af523b4ac24d5329d8dca","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":53,"end":91,"interaction_partner":[],"reference_html":"Structural basis for subversion of cellular control mechanisms by the adenoviral E1A oncoprotein. <i> Ferreon JC, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> Proc Natl Acad Sci U S A, 2009","reference_id":"19651603","region_id":"DP01150r014","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"More dramatic differences are observed between\nthe HSQC spectra of free and bound E1A (Fig. 2B). E1A is\nlargely unstructured in the free state as seen by the limited\nchemical shift dispersion in the 1H dimension; backbone resonances\nof both E1A(53–91) and E1A(1–139) show little deviation\nof chemical shifts from random coil values (Fig. S2 A and\nB)","_id":"685af523b4ac24d5329d8dd4"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T13:50:11.052Z","_id":"685af523b4ac24d5329d8dd5"},"version":2,"_id":"685af523b4ac24d5329d8dd3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":27,"end":91,"interaction_partner":[{"db":"UniProt","id":"P06400","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8ddb"}],"reference_html":"Structural basis for subversion of cellular control mechanisms by the adenoviral E1A oncoprotein. <i> Ferreon JC, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> Proc Natl Acad Sci U S A, 2009","reference_id":"19651603","region_id":"DP01150r016","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"HSQC cross peaks associated with these residues are broadened and/or shifted upon binding of pRb to E1A(27–91) or E1A(53–91) (Fig. S4C).","_id":"685af523b4ac24d5329d8dda"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T13:51:57.979Z","_id":"685af523b4ac24d5329d8ddc"},"version":4,"_id":"685af523b4ac24d5329d8dd9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":106,"end":139,"interaction_partner":[],"reference_html":"Structural basis for subversion of cellular control mechanisms by the adenoviral E1A oncoprotein. <i> Ferreon JC, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> Proc Natl Acad Sci U S A, 2009","reference_id":"19651603","region_id":"DP01150r017","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As expected (16), the LXCXE motif\nin CR2 binds with high affinity to pRb; there is a large increase\nin dispersion of the HSQC spectrum of E1A(106–139) in the\npresence of pRb and exchange is slow on the chemical shift\ntimescale (Fig. S4A).","_id":"685af523b4ac24d5329d8dde"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T13:50:07.212Z","_id":"685af523b4ac24d5329d8ddf"},"version":2,"_id":"685af523b4ac24d5329d8ddd","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":106,"end":139,"interaction_partner":[{"db":"UniProt","id":"P06400","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8de2"}],"reference_html":"Structural basis for subversion of cellular control mechanisms by the adenoviral E1A oncoprotein. <i> Ferreon JC, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> Proc Natl Acad Sci U S A, 2009","reference_id":"19651603","region_id":"DP01150r018","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Interactions between the pRb pocket domain and 15N-labeled E1A peptides were examined using HSQC titrations (Fig. S4). As expected (16), the LXCXE motif in CR2 binds with high affinity to pRb; there is a large increase in dispersion of the HSQC spectrum of E1A(106–139) in the presence of pRb and exchange is slow on the chemical shift timescale (Fig. S4A).","_id":"685af523b4ac24d5329d8de1"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T13:51:56.517Z","_id":"685af523b4ac24d5329d8de3"},"version":4,"_id":"685af523b4ac24d5329d8de0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":91,"interaction_partner":[],"reference_html":"Mapping the interactions of adenoviral E1A proteins with the p160 nuclear receptor coactivator binding domain of CBP. <i> Haberz P, Arai M, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> Protein Sci, 2016","reference_id":"27699893","region_id":"DP01150r020","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"Efficient displacement of p53 likely requires E1A to compete with both the AD1 and AD2 motifs for binding to NCBD, which would be favored in E1A constructs containing two or three NCBD binding sites. By competing for binding of p53, E1A may interfere with p53‐activated transcriptional programs that are mediated through interactions with the NCBD (also called IBiD) domain of CBP/p300,25 providing a plausible structural insight into the means whereby E1A might repress p53‐mediated apoptosis by inhibiting binding of p53 to both the NCBD and TAZ2 domains of CBP/p300.","_id":"685af523b4ac24d5329d8de8"},{"type":"Results","text":"Increased competition efficiency was observed for the longer CR1 constructs (AdV5 E1A(36–91) and AdV12 E1A(35–81)), which contain two NCBD binding sites, and the highest efficiency was observed for AdV5 E1A(1–91) and AdV12 E1A(1–81), an indication that both the N‐terminal and CR1 regions are required for efficient competition with p53 for the NCBD.","_id":"685af523b4ac24d5329d8de9"}],"states_connection":[],"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","term_id":"GO:0140313","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular sequestering activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T13:55:43.121Z","_id":"685af523b4ac24d5329d8dea"},"version":1,"_id":"685af523b4ac24d5329d8de7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2KJE","_id":"685af523b4ac24d5329d8dec"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":53,"end":91,"interaction_partner":[],"reference_html":"Structural basis for subversion of cellular control mechanisms by the adenoviral E1A oncoprotein. <i> Ferreon JC, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> Proc Natl Acad Sci U S A, 2009","reference_id":"19651603","region_id":"DP01150r021","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"To test the hypothesis that E1A and p53 compete directly for TAZ2, p53(13–61) and E1A(53–91) were titrated into 15N-labeled TAZ2 and HSQC spectra were recorded.","_id":"685af523b4ac24d5329d8ded"},{"type":"Results","text":"Addition of equimolar E1A to the TAZ:p53 complex causes all TAZ2 cross peaks to shift to their characteristic positions in the HSQC spectrum of the binary TAZ2:E1A complex (Fig. 4A, Fig. S3C), indicating that E1A displaces the p53 TAD from TAZ2.","_id":"685af523b4ac24d5329d8dee"}],"states_connection":[],"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","term_id":"GO:0140313","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular sequestering activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T13:55:41.788Z","_id":"685af523b4ac24d5329d8def"},"version":1,"_id":"685af523b4ac24d5329d8deb","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2KJE","_id":"685af523b4ac24d5329d8df1"},{"db":"BMRB","id":"16318","_id":"685af523b4ac24d5329d8df2"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":59,"end":82,"interaction_partner":[],"reference_html":"Structural basis for subversion of cellular control mechanisms by the adenoviral E1A oncoprotein. <i> Ferreon JC, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> Proc Natl Acad Sci U S A, 2009","reference_id":"19651603","region_id":"DP01150r022","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"A well-defined α-helix is formed by residues E59–I65, with shorter helical turns between L72–V74 and L80–T82, and a compact loop between F66–A73.","_id":"685af523b4ac24d5329d8df3"},{"type":"Results","text":"Upon interaction with TAZ2, there are large changes in the E1A chemical shifts (Fig. S2C) indicative of coupled folding and binding.","_id":"685af523b4ac24d5329d8df4"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T13:51:49.788Z","_id":"685af523b4ac24d5329d8df5"},"version":1,"_id":"685af523b4ac24d5329d8df0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2KJE","_id":"685af523b4ac24d5329d8df7"},{"db":"BMRB","id":"16318","_id":"685af523b4ac24d5329d8df8"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":53,"end":91,"interaction_partner":[{"db":"UniProt","id":"Q92793","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8df9"}],"reference_html":"Structural basis for subversion of cellular control mechanisms by the adenoviral E1A oncoprotein. <i> Ferreon JC, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> Proc Natl Acad Sci U S A, 2009","reference_id":"19651603","region_id":"DP01150r023","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"E1A binds in a deep hydrophobic groove in the surface of TAZ2, formed at the interfaces between helices α1/α2 and α1/α3, and buries ≈1400 Å2 of the TAZ2 surface (Fig. 3 B and C).","_id":"685af523b4ac24d5329d8dfa"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T13:51:53.765Z","_id":"685af523b4ac24d5329d8dfb"},"version":1,"_id":"685af523b4ac24d5329d8df6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":27,"end":91,"interaction_partner":[],"reference_html":"Structural basis for subversion of cellular control mechanisms by the adenoviral E1A oncoprotein. <i> Ferreon JC, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> Proc Natl Acad Sci U S A, 2009","reference_id":"19651603","region_id":"DP01150r024","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Upon titration with pRb, the A53 cross peak shifts in slow exchange from its position in the spectrum of the TAZ2 binary complex to its position in the binary E1A(27–91):pRb complex (Fig. 5B) while the cross peaks of many residues in the region 39–51 are broadened (Fig. S5), confirming binding of pRb to its cognate site. Thus, despite the close proximity of the pRb and CBP/p300 binding sites in the E1A CR1 region, the NMR data provide unequivocal evidence that both TAZ2 and the pRb pocket domain can bind simultaneously to form a ternary TAZ2-E1A-pRb complex.","_id":"685af523b4ac24d5329d8dfd"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T13:55:39.113Z","_id":"685af523b4ac24d5329d8dfe"},"version":1,"_id":"685af523b4ac24d5329d8dfc","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"position":null,"statements":[],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu115Ala","_id":"685af523b4ac24d5329d8e00"}],"cross_refs":[{"db":"ELM","id":"ELME000145","_id":"685af523b4ac24d5329d8e03"}],"curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","date":"2024-08-08T09:25:01.343Z","disprot_namespace":"Disorder function","ec_go":"IMP","ec_id":"ECO:0007089","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","ec_ontology":"ECO","start":113,"end":117,"interaction_partner":[{"db":"UniProt","id":"Q15326","operator":null,"partner_start":563,"partner_end":598,"_id":"685af523b4ac24d5329d8e04"}],"reference_html":"The conserved Mynd domain of BS69 binds cellular and oncoviral proteins through a common PXLXP motif. <i> Ansieau S, Leutz A. </i> J Biol Chem, 2002","reference_id":"11733528","region_id":"DP01150r025","released":"2024_12","sample":[],"statement":[{"type":"Results","text":"To determine whether this motif is involved in binding to BS69, the central invariable leucine residue was mutated into an alanine in E1A. As shown in Fig. 3A, the resulting 12S and 13S E1A (E1A,L115A) mutant proteins failed to interact with BS69.","_id":"685af523b4ac24d5329d8e01"},{"type":"Discussion","text":"We found that BS69-type Mynd domains interact through conserved PXLXP peptide motifs with the oncoviral proteins E1A and EBNA2 and with the cellular MGA protein.","_id":"685af523b4ac24d5329d8e02"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2024-09-18T11:23:15.589Z","_id":"685af523b4ac24d5329d8e05"},"version":0,"_id":"685af523b4ac24d5329d8dff","reference_source":"pmid"}],"__v":0,"disorder_content":0.4809688581314879,"disprot_consensus":{"full":[{"start":1,"end":52,"type":"D"},{"start":53,"end":91,"type":"T"},{"start":92,"end":139,"type":"D"}],"Structural state":[{"start":1,"end":139,"type":"D"}],"Structural transition":[{"start":53,"end":91,"type":"T"}],"Molecular function":[{"start":1,"end":91,"type":"F"},{"start":106,"end":139,"type":"F"}]}},{"acc":"P03259","sequence":"MRTEMTPLVLSYQEADDILEHLVDNFFNEVPSDDDLYVPSLYELYDLDVESAGEDNNEQAVNEFFPESLILAASEGLFLPEPPVLSPVCEPIGGECMPQLHPEDMDLLCYEMGFPCSDSEDEQDENGMAHVSASAAAAAADREREEFQLDHPELPGHNCKSCEHHRNSTGNTDLMCSLCYLRAYNMFIYSPVSDNEPEPNSTLDGDERPSPPKLGSAVPEGVIKPVPQRVTGRRRCAVESILDLIQEEEREQTVPVDLSVKRPRCN","creator":"jbergier","dataset":["Viral proteins"],"date":"2018-06-25T22:30:28.000Z","disprot_id":"DP01151","features":{"pfam":[{"id":"PF02703","name":"Early E1A protein","start":1,"end":167}]},"genes":[],"length":266,"name":"Early E1A protein","ncbi_taxon_id":28282,"organism":"Human adenovirus A serotype 12","regions_counter":6,"released":"2018_11","taxonomy":["Viruses","Varidnaviria","Bamfordvirae","Preplasmiviricota","Tectiliviricetes","Rowavirales","Adenoviridae","Mastadenovirus","Human mastadenovirus A"],"UniParc":"UPI0000129A80","uniref100":"UniRef100_P03259","uniref50":"UniRef50_P03259","uniref90":"UniRef90_P03259","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":266,"interaction_partner":[],"reference_html":"Mapping the interactions of adenoviral E1A proteins with the p160 nuclear receptor coactivator binding domain of CBP. <i> Haberz P, Arai M, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> Protein Sci, 2016","reference_id":"27699893","region_id":"DP01151r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The 1H‐15N heteronuclear single‐quantum coherence (HSQC) spectra of the unbound 15N‐labeled NCBD and 15N‐labeled E1A constructs are poorly dispersed​(Fig.2,2, black), especially in the 1H dimension, since both proteins are intrinsically disordered.","_id":"685af523b4ac24d5329d8e09"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-05T10:02:04.161Z","_id":"685af523b4ac24d5329d8e0a"},"version":3,"_id":"685af523b4ac24d5329d8e08","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":81,"interaction_partner":[{"db":"UniProt","id":"Q92793","partner_start":10,"partner_end":30,"_id":"685af523b4ac24d5329d8e15"},{"db":"UniProt","id":"Q92793","partner_start":40,"partner_end":47,"_id":"685af523b4ac24d5329d8e16"},{"db":"UniProt","id":"Q92793","partner_start":61,"partner_end":78,"_id":"685af523b4ac24d5329d8e17"},{"db":"UniProt","id":"Q92793","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8e18"},{"db":"UniProt","id":"Q09472","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8e19"}],"reference_html":"Mapping the interactions of adenoviral E1A proteins with the p160 nuclear receptor coactivator binding domain of CBP. <i> Haberz P, Arai M, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> Protein Sci, 2016","reference_id":"27699893","region_id":"DP01151r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Titrations were performed in which aliquots of the unlabeled NCBD were added to 15N‐labeled AdV5 E1A(1‐91) and AdV12 E1A(1‐81) in order to map the NCBD binding sites (Supporting Information Figs. S13 and S17).","_id":"685af523b4ac24d5329d8e1a"},{"type":"Results","text":"The chemical shift perturbations reveal three NCBD binding sites in homologous regions of AdV5 and AdV12 E1A; for AdV12, the NCBD binding sites are located between residues L10‐V30, S40‐L47, and V61‐F78 [Fig.3(B)].","_id":"685af523b4ac24d5329d8e1b"},{"type":"Discussion","text":"Thus the interaction between E1A and TAZ2 can be characterized as a partly “fuzzy” complex, with one portion of the E1A sequence participating in a strong interaction with TAZ2, while the other portion, corresponding to the N‐terminal region, participating in an interaction characterized by multiple states in intermediate exchange on the NMR time scale.","_id":"685af523b4ac24d5329d8e1c"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-05T10:02:06.356Z","_id":"685af523b4ac24d5329d8e1d"},"version":1,"_id":"685af523b4ac24d5329d8e14","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":13,"end":27,"interaction_partner":[],"reference_html":"Mapping the interactions of adenoviral E1A proteins with the p160 nuclear receptor coactivator binding domain of CBP. <i> Haberz P, Arai M, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> Protein Sci, 2016","reference_id":"27699893","region_id":"DP01151r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The large shifts of E1A HSQC cross peaks upon binding to the NCBD reflect formation of structure in the bound state. The secondary structure of AdV12 E1A in complex with the NCBD was predicted from the bound E1A 1H, 13Cα and 15N chemical shifts using the program TALOS+.33 The results ​[Fig.3(D)] show that, upon binding to the NCBD, AdV12 E1A folds to form local helical structure between residues Q13 and F27 in the N‐terminal region and between residues E67 and A73 in the C‐terminal part of the CR1 region.","_id":"685af523b4ac24d5329d8e1f"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-05T10:02:05.190Z","_id":"685af523b4ac24d5329d8e20"},"version":1,"_id":"685af523b4ac24d5329d8e1e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":81,"interaction_partner":[],"reference_html":"Mapping the interactions of adenoviral E1A proteins with the p160 nuclear receptor coactivator binding domain of CBP. <i> Haberz P, Arai M, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> Protein Sci, 2016","reference_id":"27699893","region_id":"DP01151r006","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"Efficient displacement of p53 likely requires E1A to compete with both the AD1 and AD2 motifs for binding to NCBD, which would be favored in E1A constructs containing two or three NCBD binding sites. By competing for binding of p53, E1A may interfere with p53‐activated transcriptional programs that are mediated through interactions with the NCBD (also called IBiD) domain of CBP/p300,25 providing a plausible structural insight into the means whereby E1A might repress p53‐mediated apoptosis by inhibiting binding of p53 to both the NCBD and TAZ2 domains of CBP/p300.","_id":"685af523b4ac24d5329d8e22"},{"type":"Results","text":"Increased competition efficiency was observed for the longer CR1 constructs (AdV5 E1A(36–91) and AdV12 E1A(35–81)), which contain two NCBD binding sites, and the highest efficiency was observed for AdV5 E1A(1–91) and AdV12 E1A(1–81), an indication that both the N‐terminal and CR1 regions are required for efficient competition with p53 for the NCBD.","_id":"685af523b4ac24d5329d8e23"}],"states_connection":[],"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","term_id":"GO:0140313","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular sequestering activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-05T10:02:07.699Z","_id":"685af523b4ac24d5329d8e24"},"version":1,"_id":"685af523b4ac24d5329d8e21","reference_source":"pmid"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":12,"type":"D"},{"start":13,"end":27,"type":"T"},{"start":28,"end":266,"type":"D"}],"Structural state":[{"start":1,"end":266,"type":"D"}],"Molecular function":[{"start":1,"end":81,"type":"F"}],"Structural transition":[{"start":13,"end":27,"type":"T"}]}},{"features":{"pfam":[{"id":"PF02453","name":"Reticulon","start":976,"end":1138}]},"uniref50":"UniRef50_Q9NQC3-4","sequence":"MEDIDQSSLVSSSTDSPPRPPPAFKYQFVTEPEDEEDEEEEEDEEEDDEDLEELEVLERKPAAGLSAAAVPPAAAAPLLDFSSDSVPPAPRGPLPAAPPAAPERQPSWERSPAAPAPSLPPAAAVLPSKLPEDDEPPARPPPPPPAGASPLAEPAAPPSTPAAPKRRGSGSVDETLFALPAASEPVIPSSAEKIMDLMEQPGNTVSSGQEDFPSVLLETAASLPSLSPLSTVSFKEHGYLGNLSAVSSSEGTIEETLNEASKELPERATNPFVNRDLAEFSELEYSEMGSSFKGSPKGESAILVENTKEEVIVRSKDKEDLVCSAALHSPQESPVGKEDRVVSPEKTMDIFNEMQMSVVAPVREEYADFKPFEQAWEVKDTYEGSRDVLAARANVESKVDRKCLEDSLEQKSLGKDSEGRNEDASFPSTPEPVKDSSRAYITCASFTSATESTTANTFPLLEDHTSENKTDEKKIEERKAQIITEKTSPKTSNPFLVAVQDSEADYVTTDTLSKVTEAAVSNMPEGLTPDLVQEACESELNEATGTKIAYETKVDLVQTSEAIQESLYPTAQLCPSFEEAEATPSPVLPDIVMEAPLNSLLPSAGASVVQPSVSPLEAPPPVSYDSIKLEPENPPPYEEAMNVALKALGTKEGIKEPESFNAAVQETEAPYISIACDLIKETKLSTEPSPDFSNYSEIAKFEKSVPEHAELVEDSSPESEPVDLFSDDSIPEVPQTQEEAVMLMKESLTEVSETVAQHKEERLSASPQELGKPYLESFQPNLHSTKDAASNDIPTLTKKEKISLQMEEFNTAIYSNDDLLSSKEDKIKESETFSDSSPIEIIDEFPTFVSAKDDSPKLAKEYTDLEVSDKSEIANIQSGADSLPCLELPCDLSFKNIYPKDEVHVSDEFSENRSSVSKASISPSNVSALEPQTEMGSIVKSKSLTKEAEKKLPSDTEKEDRSLSAVLSAELSKTSVVDLLYWRDIKKTGVVFGASLFLLLSLTVFSIVSVTAYIALALLSVTISFRIYKGVIQAIQKSDEGHPFRAYLESEVAISEELVQKYSNSALGHVNSTIKELRRLFLVDDLVDSLKFAVLMWVFTYVGALFNGLTLLILALISLFSIPVIYERHQVQIDHYLGLANKSVKDAMAKIQAKIPGLKRKAD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_Q99P72","disprot_id":"DP01152","ncbi_taxon_id":10116,"regions_counter":4,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":725,"region_id":"DP01152r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The Neurite Outgrowth Inhibitory Nogo-A-Δ20 Region Is an Intrinsically Disordered Segment Harbouring Three Stretches with Helical Propensity. <i> Zelenay V, Arzt ME, Bibow S, Schwab ME, Riek R. </i> PLoS One, 2016","statement":[{"text":"A 2D-NMR [15N,1H]-HSQC spectrum confirmed the intrinsically disordered character of Nogo-A-Δ20, as deduced from the low chemical shift dispersion in the 1H dimension. Using triple resonance experiments, 94% of the non-proline backbone residues were assigned. While secondary structure analysis and relaxation measurements highlighted the intrinsically disordered character of Nogo-A-Δ20, three stretches comprising residues 561-EAIQESL-567, 639-EAMNVALKALGT-650, and 693-SNYSEIAK-700 form transient α-helical structures.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":544,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27611089","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P47752","partner_end":null},{"partner_start":null,"db":"UniProt","id":"Q66H06","partner_end":null}],"ec_ontology":"ECO","end":725,"term_name":"protein binding","start":544,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"27611089","statement":[{"text":"Nogo-A-Δ20 interacts with sphingosine 1-phosphate receptor 2 (S1PR2) and tetraspanin-3. Extracellular loops 2 and 3 of S1PR2 were concluded to be the primary binding sites for Nogo-A-Δ20, binding occurred with affinities in the nanomolar range.","type":"Results"}],"reference_html":"The Neurite Outgrowth Inhibitory Nogo-A-Δ20 Region Is an Intrinsically Disordered Segment Harbouring Three Stretches with Helical Propensity. <i> Zelenay V, Arzt ME, Bibow S, Schwab ME, Riek R. </i> PLoS One, 2016","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","version":4,"region_id":"DP01152r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":725,"region_id":"DP01152r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The Neurite Outgrowth Inhibitory Nogo-A-Δ20 Region Is an Intrinsically Disordered Segment Harbouring Three Stretches with Helical Propensity. <i> Zelenay V, Arzt ME, Bibow S, Schwab ME, Riek R. </i> PLoS One, 2016","statement":[{"text":"The CD spectrum of Nogo-A-Δ20 with its minimum at around 200 nm suggests a high proportion of unstructured regions, with some residual secondary structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":544,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27611089","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":31,"end":54,"reference_id":"https://mobidb.org/Q9JK11","reference_source":"mobidb","reference_html":"An Entry Referenced from MobiDB","date":"2022-02-14T09:00:00.000Z","curator_id":"amonzon","curator_name":"Alex Monzon","curator_orcid":"0000-0003-0362-8218","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007759","ec_ontology":"ECO","ec_name":"curator inference from database used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01152r004","statement":[{"text":"This poly-E region is inferred by the curator to be disordered, based on MobiDB-Lite and according to experimental evidence demonstrating that poly-E repeats display random-coil-like conformation (PMID:16949547)","type":"Curator statement"}],"ec_go":"IC","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9JK11","date":"2018-06-25T22:45:13.000Z","acc":"Q9JK11","name":"Reticulon-4","length":1163,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI00001352DD","genes":[{"name":{"value":"Rtn4"},"synonyms":[{"value":"Nogo"}]}],"alphafold_very_low_content":0.822871883061049,"disorder_content":0.177128116938951,"disprot_consensus":{"full":[{"start":31,"end":54,"type":"D"},{"start":544,"end":725,"type":"D"}],"Structural state":[{"start":31,"end":54,"type":"D"},{"start":544,"end":725,"type":"D"}],"Molecular function":[{"start":544,"end":725,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":151,"end":345},{"id":"PF16918","name":"Protein kinase G tetratricopeptide repeat","start":409,"end":748},{"id":"PF16919","name":"Protein kinase G rubredoxin domain","start":69,"end":141}],"gene3D":[{"start":412,"end":594,"id":"1.25.40.10","name":"Tetratricopeptide repeat domain"},{"start":421,"end":745,"id":"1.25.40.10","name":"Tetratricopeptide repeat domain"},{"start":103,"end":237,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":238,"end":394,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"}]},"uniref50":"UniRef50_A0QQK3","sequence":"MAKASETERSGPGTQPADAQTATSATVRPLSTQAVFRPDFGDEDNFPHPTLGPDTEPQDRMATTSRVRPPVRRLGGGLVEIPRAPDIDPLEALMTNPVVPESKRFCWNCGRPVGRSDSETKGASEGWCPYCGSPYSFLPQLNPGDIVAGQYEVKGCIAHGGLGWIYLALDRNVNGRPVVLKGLVHSGDAEAQAMAMAERQFLAEVVHPSIVQIFNFVEHTDRHGDPVGYIVMEYVGGQSLKRSKGQKLPVAEAIAYLLEILPALSYLHSIGLVYNDLKPENIMLTEEQLKLIDLGAVSRINSFGYLYGTPGFQAPEIVRTGPTVATDIYTVGRTLAALTLDLPTRNGRYVDGLPEDDPVLKTYDSYGRLLRRAIDPDPRQRFTTAEEMSAQLTGVLREVVAQDTGVPRPGLSTIFSPSRSTFGVDLLVAHTDVYLDGQVHAEKLTANEIVTALSVPLVDPTDVAASVLQATVLSQPVQTLDSLRAARHGALDADGVDFSESVELPLMEVRALLDLGDVAKATRKLDDLAERVGWRWRLVWYRAVAELLTGDYDSATKHFTEVLDTFPGELAPKLALAATAELAGNTDEHKFYQTVWSTNDGVISAAFGLARARSAEGDRVGAVRTLDEVPPTSRHFTTARLTSAVTLLSGRSTSEVTEEQIRDAARRVEALPPTEPRVLQIRALVLGGALDWLKDNKASTNHILGFPFTSHGLRLGVEASLRSLARVAPTQRHRYTLVDMANKVRPTSTF","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"uniref90":"UniRef90_P65729","disprot_id":"DP01153","ncbi_taxon_id":83332,"regions_counter":12,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":75,"region_id":"DP01153r001","start":1,"ec_id":"ECO:0006165","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The low signal dispersion of the NORS region indicates already that it is indeed a natively disordered protein (IDP) region. ","type":"Results"},{"text":"The NORS region (approximately residues 1–75) shows strongly negative 13Cα secondary shifts for residues preceding a proline.","type":"Results"},{"text":"Overall, the NORS region appears, as predicted, natively disordered.","type":"Results"},{"text":"The presented NMR structural and dynamic data for the NORS region (His-PknG1–75; Fig. 1, C and D, and supplemental Figs. S2 and S3A) demonstrate that the NORS region is indeed rather unstructured and dynamic.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27810897","version":3,"reference_html":"Oxidative Unfolding of the Rubredoxin Domain and the Natively Disordered N-terminal Region Regulate the Catalytic Activity of Mycobacterium tuberculosis Protein Kinase G. <i> Wittwer M, Luo Q, Kaila VR, Dames SA. </i> J Biol Chem, 2016","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-03T14:24:12.068Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":65,"term_name":"phosphorylation display site","released":"2025_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Oxidative Unfolding of the Rubredoxin Domain and the Natively Disordered N-terminal Region Regulate the Catalytic Activity of Mycobacterium tuberculosis Protein Kinase G. <i> Wittwer M, Luo Q, Kaila VR, Dames SA. </i> J Biol Chem, 2016","statement":[{"text":"Based on the available assignments, this includes residues near the known in vivo phosphorylation site Thr63 (11) as well as residues near other threonine residues know to be phosphorylated in vitro (Thr23, Thr32, and Thr64) (10).","type":"Introduction"}],"term_id":"IDPO:0000045","curator_id":"vnugnes","start":61,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27810897","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2025-06-03T15:56:37.678Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01153r002","ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":1,"end":75,"reference_id":"27810897","reference_source":"pmid","reference_html":"Oxidative Unfolding of the Rubredoxin Domain and the Natively Disordered N-terminal Region Regulate the Catalytic Activity of Mycobacterium tuberculosis Protein Kinase G. <i> Wittwer M, Luo Q, Kaila VR, Dames SA. </i> J Biol Chem, 2016","date":"2025-04-25T12:57:11.571Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP01153r003","statement":[{"text":"The presented NMR structural and dynamic data for the NORS region (His-PknG1–75; Fig. 1, C and D, and supplemental Figs. S2 and S3A) demonstrate that the NORS region is indeed rather unstructured and dynamic.","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-03T14:24:14.833Z"}},{"start":1,"end":73,"reference_id":"27810897","reference_source":"pmid","reference_html":"Oxidative Unfolding of the Rubredoxin Domain and the Natively Disordered N-terminal Region Regulate the Catalytic Activity of Mycobacterium tuberculosis Protein Kinase G. <i> Wittwer M, Luo Q, Kaila VR, Dames SA. </i> J Biol Chem, 2016","date":"2025-06-03T15:34:43.238Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0046777","term_name":"protein autophosphorylation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1Arg73del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP01153r004","statement":[{"text":"Compared with the wild type (Fig. 2A, blue columns), deletion of the N-terminal NORS region reduces PknG catalytic activity significantly (Fig. 2A, green columns), and additional removal of the C-terminal TPRD results in a further reduction (Fig. 2A, red columns). This is consistent with published results (10, 11, 14).","type":"Results"},{"text":"Compared with the wild type (Fig. 2A, blue columns), deletion of the N-terminal NORS region reduces PknG catalytic activity significantly (Fig. 2A, green columns), and additional removal of the C-terminal TPRD results in a further reduction (Fig. 2A, red columns). This is consistent with published results (10, 11, 14).","type":"Results"}],"term_comment":"","term_def":"\"The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation).\" [ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false},{"start":21,"end":25,"reference_id":"19447903","reference_source":"pmid","reference_html":"Survival of pathogenic mycobacteria in macrophages is mediated through autophosphorylation of protein kinase G. <i> Scherr N, Müller P, Perisa D, Combaluzier B, Jenö P, Pieters J. </i> J Bacteriol, 2009","date":"2025-06-03T15:52:46.859Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr23Ala","start":null,"end":null,"position":null}],"region_id":"DP01153r005","statement":[{"text":"As shown in Fig. ​3C, PknG autophosphorylation was reduced when a threonine residue at either position 32 or position 63/64 is mutated into alanine. Autophosphorylation was further reduced when a second threonine residue was mutated into an alanine as demonstrated for construct T32/63/64. ","type":"Results"},{"text":"These results demonstrate that the major autophosphorylation sites of PknG are T23, T32, and T63/64, which are located close to the N terminus (Fig. 3D).","type":"Results"}]},{"start":30,"end":34,"reference_id":"19447903","reference_source":"pmid","reference_html":"Survival of pathogenic mycobacteria in macrophages is mediated through autophosphorylation of protein kinase G. <i> Scherr N, Müller P, Perisa D, Combaluzier B, Jenö P, Pieters J. </i> J Bacteriol, 2009","date":"2025-06-03T15:53:00.499Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr32Ala","start":null,"end":null,"position":null}],"region_id":"DP01153r006","statement":[{"text":"As shown in Fig. ​3C, PknG autophosphorylation was reduced when a threonine residue at either position 32 or position 63/64 is mutated into alanine. Autophosphorylation was further reduced when a second threonine residue was mutated into an alanine as demonstrated for construct T32/63/64. ","type":"Results"},{"text":"These results demonstrate that the major autophosphorylation sites of PknG are T23, T32, and T63/64, which are located close to the N terminus (Fig. 3D).","type":"Results"}]},{"start":61,"end":65,"reference_id":"19447903","reference_source":"pmid","reference_html":"Survival of pathogenic mycobacteria in macrophages is mediated through autophosphorylation of protein kinase G. <i> Scherr N, Müller P, Perisa D, Combaluzier B, Jenö P, Pieters J. </i> J Bacteriol, 2009","date":"2025-06-03T15:53:48.188Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr63Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr64Ala","start":null,"end":null,"position":null}],"region_id":"DP01153r007","statement":[{"text":"As shown in Fig. ​3C, PknG autophosphorylation was reduced when a threonine residue at either position 32 or position 63/64 is mutated into alanine. Autophosphorylation was further reduced when a second threonine residue was mutated into an alanine as demonstrated for construct T32/63/64. ","type":"Results"},{"text":"These results demonstrate that the major autophosphorylation sites of PknG are T23, T32, and T63/64, which are located close to the N terminus (Fig. 3D).","type":"Results"}]},{"start":75,"end":147,"reference_id":"27810897","reference_source":"pmid","reference_html":"Oxidative Unfolding of the Rubredoxin Domain and the Natively Disordered N-terminal Region Regulate the Catalytic Activity of Mycobacterium tuberculosis Protein Kinase G. <i> Wittwer M, Luo Q, Kaila VR, Dames SA. </i> J Biol Chem, 2016","date":"2025-06-03T16:05:39.064Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP01153r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"Thus, it appears to be present in a folded metal-bound state.","type":"Results"},{"text":"Altogether, the data indicate that the RD can switch between a reduced, metal-bound folded state and an oxidized, metal-free unfolded state (Fig. 3B).","type":"Results"}]},{"start":75,"end":147,"reference_id":"27810897","reference_source":"pmid","reference_html":"Oxidative Unfolding of the Rubredoxin Domain and the Natively Disordered N-terminal Region Regulate the Catalytic Activity of Mycobacterium tuberculosis Protein Kinase G. <i> Wittwer M, Luo Q, Kaila VR, Dames SA. </i> J Biol Chem, 2016","date":"2025-06-03T16:08:42.835Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP01153r009","statement":[{"text":"Indicated by the low signal dispersion, the RD in the oxidized, metal-free form is, as the NORS, largely unfolded.","type":"Results"},{"text":"Altogether, the data indicate that the RD can switch between a reduced, metal-bound folded state and an oxidized, metal-free unfolded state (Fig. 3B).","type":"Results"}]},{"start":75,"end":147,"reference_id":"27810897","reference_source":"pmid","reference_html":"Oxidative Unfolding of the Rubredoxin Domain and the Natively Disordered N-terminal Region Regulate the Catalytic Activity of Mycobacterium tuberculosis Protein Kinase G. <i> Wittwer M, Luo Q, Kaila VR, Dames SA. </i> J Biol Chem, 2016","date":"2025-06-03T16:09:54.550Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP01153r010","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"Indicated by the low signal dispersion, the RD in the oxidized, metal-free form is, as the NORS, largely unfolded.","type":"Results"},{"text":"Altogether, the data indicate that the RD can switch between a reduced, metal-bound folded state and an oxidized, metal-free unfolded state (Fig. 3B). Thus, a change of the redox conditions may regulate the catalytic kinase domain by controlled un- and refolding of the RD, which is expected to influence the substrate access.","type":"Results"}],"states_connection":[{"source":"DP01153r008","target":"DP01153r009"}]},{"start":21,"end":64,"reference_id":"19447903","reference_source":"pmid","reference_html":"Survival of pathogenic mycobacteria in macrophages is mediated through autophosphorylation of protein kinase G. <i> Scherr N, Müller P, Perisa D, Combaluzier B, Jenö P, Pieters J. </i> J Bacteriol, 2009","date":"2025-06-03T16:31:39.541Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0044068","term_name":"modulation by symbiont of host cellular process","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr21Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"For in vivo studies, pknG-ΔN and pknG-Pmut (in which T21, T23, T26, T32, T63, and T64 were mutated to alanines) were inserted into the mycobacterial vector pMV361 using EcoRV and HindIII restriction sites."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr23Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"For in vivo studies, pknG-ΔN and pknG-Pmut (in which T21, T23, T26, T32, T63, and T64 were mutated to alanines) were inserted into the mycobacterial vector pMV361 using EcoRV and HindIII restriction sites."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr26Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"For in vivo studies, pknG-ΔN and pknG-Pmut (in which T21, T23, T26, T32, T63, and T64 were mutated to alanines) were inserted into the mycobacterial vector pMV361 using EcoRV and HindIII restriction sites."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr32Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"For in vivo studies, pknG-ΔN and pknG-Pmut (in which T21, T23, T26, T32, T63, and T64 were mutated to alanines) were inserted into the mycobacterial vector pMV361 using EcoRV and HindIII restriction sites."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr63Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"For in vivo studies, pknG-ΔN and pknG-Pmut (in which T21, T23, T26, T32, T63, and T64 were mutated to alanines) were inserted into the mycobacterial vector pMV361 using EcoRV and HindIII restriction sites."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr64Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"For in vivo studies, pknG-ΔN and pknG-Pmut (in which T21, T23, T26, T32, T63, and T64 were mutated to alanines) were inserted into the mycobacterial vector pMV361 using EcoRV and HindIII restriction sites."}]}],"ec_go":"IMP","region_id":"DP01153r011","statement":[{"text":"The results, shown in Fig. ​Fig.5B,5B, show that for mycobacteria expressing PknG-Pmut as well as PknG-ΔN, lysosomal delivery was significantly increased compared to wild-type mycobacteria, suggesting that autophosphorylation is essential for the prevention of mycobacterial trafficking to lysosomes.","type":"Results"}],"term_comment":"","term_def":"\"Any process in which a symbiont organism modulates the frequency, rate or extent of a cellular process, any process that is carried out at the cellular level, but not necessarily restricted to a single cell, in its host organism.\" [MITRE:tk]","term_is_obsolete":false,"term_not_annotate":false},{"start":21,"end":64,"reference_id":"19447903","reference_source":"pmid","reference_html":"Survival of pathogenic mycobacteria in macrophages is mediated through autophosphorylation of protein kinase G. <i> Scherr N, Müller P, Perisa D, Combaluzier B, Jenö P, Pieters J. </i> J Bacteriol, 2009","date":"2025-06-03T16:34:55.599Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0052067","term_name":"antiphagocytosis","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr21Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"For in vivo studies, pknG-ΔN and pknG-Pmut (in which T21, T23, T26, T32, T63, and T64 were mutated to alanines) were inserted into the mycobacterial vector pMV361 using EcoRV and HindIII restriction sites."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr23Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"For in vivo studies, pknG-ΔN and pknG-Pmut (in which T21, T23, T26, T32, T63, and T64 were mutated to alanines) were inserted into the mycobacterial vector pMV361 using EcoRV and HindIII restriction sites."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr26Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"For in vivo studies, pknG-ΔN and pknG-Pmut (in which T21, T23, T26, T32, T63, and T64 were mutated to alanines) were inserted into the mycobacterial vector pMV361 using EcoRV and HindIII restriction sites."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr32Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"For in vivo studies, pknG-ΔN and pknG-Pmut (in which T21, T23, T26, T32, T63, and T64 were mutated to alanines) were inserted into the mycobacterial vector pMV361 using EcoRV and HindIII restriction sites."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr63Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"For in vivo studies, pknG-ΔN and pknG-Pmut (in which T21, T23, T26, T32, T63, and T64 were mutated to alanines) were inserted into the mycobacterial vector pMV361 using EcoRV and HindIII restriction sites."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr64Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"For in vivo studies, pknG-ΔN and pknG-Pmut (in which T21, T23, T26, T32, T63, and T64 were mutated to alanines) were inserted into the mycobacterial vector pMV361 using EcoRV and HindIII restriction sites."}]}],"ec_go":"IMP","region_id":"DP01153r012","statement":[{"text":"The lysosomal transfer of the mycobacterial strains expressing PknG lacking the autophosphorylation sites suggests that autophosphorylation is required for intracellular survival.","type":"Results"},{"text":"While as expected wild-type mycobacteria were able to survive as indicated by the incorporation of [3H]uracil, none of the PknG mutant strains proliferated, as evidenced by the lack of tritium incorporation (Fig. ​5D). We conclude, based upon uracil incorporation, that autophosphorylation of PknG is essential for the intracellular survival of mycobacteria within macrophages.","type":"Results"},{"text":"The virulence of pathogenic mycobacteria is dependent on their capacity to survive within macrophages by preventing phagosome-lysosome fusion (21, 22).","type":"Discussion"}],"term_comment":"","term_def":"\"Any process in which a symbiont avoids phagocytosis by a host cell, for example a phagocyte or a macrophage. The host is defined as the larger of the organisms involved in a symbiotic interaction.\" [GOC:mtg_pamgo_17jul06, PMID:23084912, PMID:29114249]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_P65729","date":"2018-06-25T23:10:06.000Z","acc":"P9WI73","name":"Serine/threonine-protein kinase PknG","length":750,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","dataset":["Bacterial virulence-related proteins"],"UniParc":"UPI0000131B7D","genes":[{"name":{"value":"pknG"},"orfNames":[{"value":"MTCY22G10.06c"}],"olnNames":[{"value":"Rv0410c"}]}],"alphafold_very_low_content":0.09066666666666667,"disorder_content":0.196,"disprot_consensus":{"full":[{"start":1,"end":74,"type":"D"},{"start":75,"end":147,"type":"T"}],"Structural state":[{"start":1,"end":147,"type":"D"}],"Disorder function":[{"start":1,"end":75,"type":"F"}],"Biological process":[{"start":1,"end":73,"type":"F"}],"Structural transition":[{"start":75,"end":147,"type":"T"}]}},{"features":{"pfam":[],"gene3D":[{"start":30,"end":158,"id":"1.10.110.10","name":"Plant lipid-transfer and hydrophobic proteins"}]},"uniref50":"UniRef50_P19594","sequence":"MTKFTILLISLLFCIAHTCSASKWQHQQDSCRKQLQGVNLTPCEKHIMEKIQGRGDDDDDDDDDNHILRTMRGRINYIRRNEGKDEDEEEEGHMQKCCTEMSELRSPKCQCKALQKIMENQSEELEEKQKKKMEKELINLATMCRFGPMIQCDLSSDD","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","fabids","Fabales","Fabaceae","Papilionoideae","50 kb inversion clade","NPAAA clade","indigoferoid/millettioid clade","Phaseoleae","Glycine","Glycine subgen. Soja"],"uniref90":"UniRef90_P19594","disprot_id":"DP01154","ncbi_taxon_id":3847,"regions_counter":2,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":64,"region_id":"DP01154r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Lunasin is a redox sensitive intrinsically disordered peptide with two transiently populated α-helical regions. <i> Aleksis R, Jaudzems K, Muceniece R, Liepinsh E. </i> Peptides, 2016","statement":[{"text":"The obtained 13Cα,β chemical shifts were then compared with random-coil values in order to estimate secondary structure propensities. The reduced lunasin form shows some residual secondary structure. The calculated Δδi values are small, as compared to the characteristic values for structured regions in proteins (|Δδi| > 1 ppm), indicating that there is a reduced population of the secondary structures in solution because of an equilibrium with unstructured conformations.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":22,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27639324","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P0CG89","partner_end":null}],"ec_ontology":"ECO","end":64,"term_name":"protein binding","start":22,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"27639324","statement":[{"text":"Both, the helical region (Glu23-Ile30) as well as the 22 residues of the N-terminus were found to facilitate the binding to deacetylated N-terminal tail of histone H4.","type":"Introduction"}],"reference_html":"Lunasin is a redox sensitive intrinsically disordered peptide with two transiently populated α-helical regions. <i> Aleksis R, Jaudzems K, Muceniece R, Liepinsh E. </i> Peptides, 2016","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","version":4,"region_id":"DP01154r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P19594","date":"2018-06-25T23:49:51.000Z","acc":"P19594","name":"2S albumin","length":158,"organism":"Glycine max","dataset":[],"UniParc":"UPI000003C545","genes":[],"alphafold_very_low_content":0.20253164556962025,"disorder_content":0.2721518987341772,"disprot_consensus":{"full":[{"start":22,"end":64,"type":"D"}],"Structural state":[{"start":22,"end":64,"type":"D"}],"Molecular function":[{"start":22,"end":64,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00309","name":"Sigma-54 factor, Activator interacting domain (AID)","start":3,"end":46},{"id":"PF04552","name":"Sigma-54, DNA binding domain","start":245,"end":397},{"id":"PF04963","name":"Sigma-54 factor, core binding domain","start":74,"end":175}],"gene3D":[{"start":69,"end":198,"id":"1.10.10.1330","name":"RNA polymerase sigma-54 factor, core-binding domain"},{"start":339,"end":398,"id":"1.10.10.60","name":"Homeodomain-like"}]},"uniref50":"UniRef50_O66858","sequence":"MLNQRLEVRQKLNLKLLLKQDLELLTYQTQELEKLIHEEVLVNPLIKGVFKKIPKSFEVKETVPYQIPYTPSELEELQQNIKLELEGKEQELALELLNYLNEKGFLSKSVEEISDVLRCSVEELEKVRQKVLRLEPLGVCSKDVWEFLELQIEEIYPEEEEILKKALRDLKRGKKLKPEIKGKLSRLRLFPLSSSAEKVYTFAKVDAIIEEENGEFFIYLYEDFIDIDLNEEYWELYKKSRNLQKELKEAFERYESIRKVLDIRRRNLRKVLEKIVERQKDFLTGKGSLKPLTLREVSSEIGIHESTLSRIVNSKYVKTPVGTYSLRTFFVRESAEGLTQGELMKLIKEIVENEDKRKPYSDQEIANILKEKGFKVARRTVAKYREMLGIPSSRERRI","taxonomy":["Bacteria","Aquificae","Aquificales","Aquificaceae","Aquifex"],"uniref90":"UniRef90_O66858","disprot_id":"DP01155","ncbi_taxon_id":224324,"regions_counter":4,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":60,"region_id":"DP01155r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Role of the σ<sup>54</sup> Activator Interacting Domain in Bacterial Transcription Initiation. <i> Siegel AR, Wemmer DE. </i> J Mol Biol, 2016","statement":[{"text":"Nearly all of the amide peaks in the previously assigned σ54(60-135) spectrum perfectly match the peaks in the σ54(1-135) spectrum. Almost all of the additional peaks in the σ54(1-135) spectrum have low dispersion of chemical shifts in the 1H dimension. These peaks correspond to the first 60 residues of σ54 and the low shift dispersion is characteristic of an unfolded protein segment.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":1,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27732872","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"O67198","partner_end":null}],"ec_ontology":"ECO","end":60,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"27732872","statement":[{"text":"The N-terminal activator interacting domain (AID) of σ54/rpoN binds the transcriptional activator NtrC1. σ54 only binds the transcriptional activators with significant affinity when the activator subunits are primarily in the ATP state.","type":"Introduction"}],"reference_html":"Role of the σ<sup>54</sup> Activator Interacting Domain in Bacterial Transcription Initiation. <i> Siegel AR, Wemmer DE. </i> J Mol Biol, 2016","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","version":4,"region_id":"DP01155r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":60,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Role of the σ<sup>54</sup> Activator Interacting Domain in Bacterial Transcription Initiation. <i> Siegel AR, Wemmer DE. </i> J Mol Biol, 2016","statement":[{"text":"The σ54 AID becomes structured after associating with the core loops of the transcriptional activator NtrC1C in its ATP state and the primary site of the interaction is the first predicted helix (residues 6-12).","type":"Abstract"}],"term_id":"IDPO:0000011","curator_id":"rpancsa","start":1,"term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"27732872","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01155r003","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_O66858","date":"2018-06-26T00:19:01.000Z","acc":"O66858","name":"RNA polymerase sigma factor RpoN","length":398,"organism":"Aquifex aeolicus (strain VF5)","dataset":[],"UniParc":"UPI00000563D4","genes":[{"name":{"value":"rpoN","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAC06814.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAC06814.1"}}]},"olnNames":[{"value":"aq_599","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAC06814.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAC06814.1"}}]}]}],"alphafold_very_low_content":0.10050251256281408,"disorder_content":0.1507537688442211,"disprot_consensus":{"full":[{"start":1,"end":60,"type":"T"}],"Structural state":[{"start":1,"end":60,"type":"D"}],"Molecular function":[{"start":1,"end":60,"type":"F"}],"Structural transition":[{"start":1,"end":60,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00538","name":"linker histone H1 and H5 family","start":25,"end":96}],"gene3D":[{"start":19,"end":109,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}]},"uniref50":"UniRef50_P07305","sequence":"MTENSTSAPAAKPKRAKASKKSTDHPKYSDMIVAAIQAEKNRAGSSRQSIQKYIKSHYKVGENADSQIKLSIKRLVTTGVLKQTKGVGASGSFRLAKSDEPKKSVAFKKTKKEIKKVATPKKASKPKKAASKAPTKKPKATPVKKAKKKLAATPKKAKKPKTVKAKPVKASKPKKAKPVKPKAKSSAKRAGKKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P07305","disprot_id":"DP01156","ncbi_taxon_id":9606,"regions_counter":10,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":194,"region_id":"DP01156r001","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Extreme disorder in an ultrahigh-affinity protein complex. <i> Borgia A, Borgia MB, Bugge K, Kissling VM, Heidarsson PO, Fernandes CB, Sottini A, Soranno A, Buholzer KJ, Nettels D, Kragelund BB, Best RB, Schuler B. </i> Nature, 2018","statement":[{"text":"The CD spectra of unbound ProTα and H1 reflect the low secondary structure content of the individual IDPs, except for the small helix-turn-helix domain of H113,19,20 (Fig. 1c).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":98,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"29466338","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-11-23T15:47:13.068Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:07:05.046Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":194,"term_name":"protein binding","start":98,"ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Extreme disorder in an ultrahigh-affinity protein complex. <i> Borgia A, Borgia MB, Bugge K, Kissling VM, Heidarsson PO, Fernandes CB, Sottini A, Soranno A, Buholzer KJ, Nettels D, Kragelund BB, Best RB, Schuler B. </i> Nature, 2018","statement":[{"text":"Surprisingly, the CD spectrum of an equimolar mixture of the two proteins can be explained by the simple sum of the individual spectra, indicating that complex formation entails minimal changes in average secondary structure content.","type":"Results"},{"text":"Note, however, that the globular domain is dispensable for complex formation (Fig. 2b, cf. High-affinity binding in spite of disorder).","type":"Results"}],"curator_id":"vnugnes","released":"2023_12","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"29466338","version":5,"term_id":"GO:0005515","date":"2023-11-23T15:47:46.627Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01156r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"curator_orcid":"0000-0001-8399-7907","interaction_partner":[{"db":"UniProt","id":"P06454","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:07:14.716Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":22,"region_id":"DP01156r003","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Extreme disorder in an ultrahigh-affinity protein complex. <i> Borgia A, Borgia MB, Bugge K, Kissling VM, Heidarsson PO, Fernandes CB, Sottini A, Soranno A, Buholzer KJ, Nettels D, Kragelund BB, Best RB, Schuler B. </i> Nature, 2018","statement":[{"text":"The CD spectra of unbound ProTα and H1 reflect the low secondary structure content of the individual IDPs, except for the small helix-turn-helix domain of H113,19,20 (Fig. 1c).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"29466338","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-11-23T14:49:04.551Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:07:06.857Z"}},{"term_namespace":"Molecular function","interaction_partner":[{"db":"UniProt","id":"P06454"}],"ec_ontology":"ECO","end":22,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Extreme disorder in an ultrahigh-affinity protein complex. <i> Borgia A, Borgia MB, Bugge K, Kissling VM, Heidarsson PO, Fernandes CB, Sottini A, Soranno A, Buholzer KJ, Nettels D, Kragelund BB, Best RB, Schuler B. </i> Nature, 2018","statement":[{"text":"Surprisingly, the CD spectrum of an equimolar mixture of the two proteins can be explained by the simple sum of the individual spectra, indicating that complex formation entails minimal changes in average secondary structure content.","type":"Results"},{"text":"Note, however, that the globular domain is dispensable for complex formation (Fig. 2b, cf. High-affinity binding in spite of disorder).","type":"Results"}],"curator_id":"vnugnes","released":"2023_12","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"29466338","version":5,"term_id":"GO:0005515","date":"2023-11-23T14:52:32.145Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01156r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"curator_orcid":"0000-0001-8399-7907","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:07:17.228Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":194,"region_id":"DP01156r005","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Extreme disorder in an ultrahigh-affinity protein complex. <i> Borgia A, Borgia MB, Bugge K, Kissling VM, Heidarsson PO, Fernandes CB, Sottini A, Soranno A, Buholzer KJ, Nettels D, Kragelund BB, Best RB, Schuler B. </i> Nature, 2018","statement":[{"text":"1H,15N heteronuclear single quantum coherence (HSQC) spectra of the individual proteins exhibit low dispersion of the 1H chemical shifts, as expected for IDPs14,21-23 (Fig. 1e,f). Only the globular domain of H1, which is stably folded even in isolation (Extended Data Fig. 1), shows the large dispersion of resonances characteristic of tertiary structure23,24 (Fig. 1g).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":98,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"29466338","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-11-23T15:46:59.912Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:07:11.339Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":194,"term_name":"protein binding","start":98,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Extreme disorder in an ultrahigh-affinity protein complex. <i> Borgia A, Borgia MB, Bugge K, Kissling VM, Heidarsson PO, Fernandes CB, Sottini A, Soranno A, Buholzer KJ, Nettels D, Kragelund BB, Best RB, Schuler B. </i> Nature, 2018","statement":[{"text":"Remarkably, the overall peak dispersion remains unchanged upon complex formation, confirming that no pronounced tertiary structure is formed upon binding. Nevertheless, small but clearly detectable peak shifts observed for ProTα and H1 indicate significant changes in the average chemical environment of the corresponding residues, as expected upon interaction with the large opposite charge of the other IDP.","type":"Results"},{"text":"Note, however, that the globular domain is dispensable for complex formation (Fig. 2b, cf. High-affinity binding in spite of disorder).","type":"Results"}],"curator_id":"vnugnes","released":"2023_12","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"29466338","version":5,"term_id":"GO:0005515","date":"2023-11-23T15:47:39.288Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01156r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"BMRB","id":"27216"}],"curator_orcid":"0000-0001-8399-7907","interaction_partner":[{"db":"UniProt","id":"P06454","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:07:18.611Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":22,"region_id":"DP01156r007","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Extreme disorder in an ultrahigh-affinity protein complex. <i> Borgia A, Borgia MB, Bugge K, Kissling VM, Heidarsson PO, Fernandes CB, Sottini A, Soranno A, Buholzer KJ, Nettels D, Kragelund BB, Best RB, Schuler B. </i> Nature, 2018","statement":[{"text":"1H,15N heteronuclear single quantum coherence (HSQC) spectra of the individual proteins exhibit low dispersion of the 1H chemical shifts, as expected for IDPs14,21-23 (Fig. 1e,f). Only the globular domain of H1, which is stably folded even in isolation (Extended Data Fig. 1), shows the large dispersion of resonances characteristic of tertiary structure23,24 (Fig. 1g).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"29466338","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-11-23T14:43:22.988Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:07:13.376Z"}},{"term_namespace":"Molecular function","interaction_partner":[{"db":"UniProt","id":"P06454"}],"ec_ontology":"ECO","end":22,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Extreme disorder in an ultrahigh-affinity protein complex. <i> Borgia A, Borgia MB, Bugge K, Kissling VM, Heidarsson PO, Fernandes CB, Sottini A, Soranno A, Buholzer KJ, Nettels D, Kragelund BB, Best RB, Schuler B. </i> Nature, 2018","statement":[{"text":"Remarkably, the overall peak dispersion remains unchanged upon complex formation, confirming that no pronounced tertiary structure is formed upon binding. Nevertheless, small but clearly detectable peak shifts observed for ProTα and H1 indicate significant changes in the average chemical environment of the corresponding residues, as expected upon interaction with the large opposite charge of the other IDP.","type":"Results"},{"text":"Note, however, that the globular domain is dispensable for complex formation (Fig. 2b, cf. High-affinity binding in spite of disorder).","type":"Results"}],"curator_id":"vnugnes","released":"2023_12","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"29466338","version":5,"term_id":"GO:0005515","date":"2023-11-23T14:51:20.706Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01156r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"BMRB","id":"27216"}],"curator_orcid":"0000-0001-8399-7907","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:07:20.717Z"}},{"start":104,"end":194,"reference_id":"29466338","reference_source":"pmid","reference_html":"Extreme disorder in an ultrahigh-affinity protein complex. <i> Borgia A, Borgia MB, Bugge K, Kissling VM, Heidarsson PO, Fernandes CB, Sottini A, Soranno A, Buholzer KJ, Nettels D, Kragelund BB, Best RB, Schuler B. </i> Nature, 2018","date":"2023-11-23T15:10:06.582Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P06454","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01156r009","statement":[{"text":"The dominant contribution to the interaction with ProTα stems from the unstructured C-terminal part of H1, which alone binds with picomolar affinity. The N-terminal half and the isolated globular domain of H1 also bind ProTα, but with much lower affinity (Fig. 2b).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:07:22.904Z"}},{"start":101,"end":194,"reference_id":"35377618","reference_source":"pmid","reference_html":"H1.0 C Terminal Domain Is Integral for Altering Transcription Factor Binding within Nucleosomes. <i> Burge NL, Thuma JL, Hong ZZ, Jamison KB, Ottesen JJ, Poirier MG. </i> Biochemistry, 2022","date":"2023-11-23T16:15:41.221Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031491","term_name":"nucleosome binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","region_id":"DP01156r010","statement":[{"text":"Both H1.0ΔC and H1.0 ΔCpartial bind nucleosomes at a concentration of about 30 nM (Figure 4B,C), while full length H1.0 binds nucleosomes at about 3 nM (Figure 2A). This implies that both deletion mutants have about a 10-fold lower affinity to nucleosomes than full length H1.0. ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a nucleosome, a complex comprised of DNA wound around a multisubunit core and associated proteins, which forms the primary packing unit of DNA into higher order structures.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"P06899","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P68431","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P62805","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P04908","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:07:25.449Z"}}],"released":"2018_11","uniref100":"UniRef100_P07305","date":"2018-06-26T08:07:22.000Z","acc":"P07305","name":"Histone H1.0","length":194,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI000012BEED","genes":[{"name":{"value":"H1-0","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4714","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4714"}}]},"synonyms":[{"value":"H1F0","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4714","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4714"}}]},{"value":"H1FV"}]}],"alphafold_very_low_content":0.24742268041237114,"disorder_content":0.6134020618556701,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"},{"start":98,"end":194,"type":"D"}],"Structural state":[{"start":1,"end":22,"type":"D"},{"start":98,"end":194,"type":"D"}],"Molecular function":[{"start":1,"end":22,"type":"F"},{"start":98,"end":194,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00125","name":"Core histone H2A/H2B/H3/H4 domain","start":7,"end":89},{"id":"PF16211","name":"C-terminus of histone H2A","start":92,"end":126}],"gene3D":[{"start":1,"end":129,"id":"1.10.20.10","name":"Histone, subunit A"}]},"uniref50":"UniRef50_P04908","sequence":"MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P04908","disprot_id":"DP01157","ncbi_taxon_id":9606,"regions_counter":6,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":27,"region_id":"DP01157r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of the isolated histone H2A-H2B heterodimer. <i> Moriwaki Y, Yamane T, Ohtomo H, Ikeguchi M, Kurita J, Sato M, Nagadoi A, Shimojo H, Nishimura Y. </i> Sci Rep, 2016","statement":[{"text":"We examined the secondary structures of the isolated H2A-H2B heterodimer by TROSY-NMR. Almost all of the main-chain signals (i.e., HN, N, Cα, Cβ and C’ signals) could be assigned (96% for H2A; 95% for H2B). As shown in the experimental chemical shift indices obtained from the Cα and Cβ chemical shift values, both H2A and H2B contain a core histone fold comprising four α-helices together with two β-strands—namely, α1–β1–α2–β2–α3–αC, much as is observed for their counterparts in the nucleosome. Outside the histone fold of H2A, however, the N-terminal αN helix and the C-terminal β3 strand and 310 helix observed in the nucleosome are entirely disordered in the isolated H2A-H2B heterodimer.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":1,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"27181506","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"11609"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":27,"term_name":"acetylation display site","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Histone proteins have N-terminal and/or C-terminal flexible tails, which are modified by methylation and acetylation, and influence chromatin remodeling.","type":"Discussion"}],"curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"27181506","version":2,"reference_html":"Solution structure of the isolated histone H2A-H2B heterodimer. <i> Moriwaki Y, Yamane T, Ohtomo H, Ikeguchi M, Kurita J, Sato M, Nagadoi A, Shimojo H, Nishimura Y. </i> Sci Rep, 2016","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000039","ec_id":"ECO:0006165","region_id":"DP01157r002","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":27,"term_name":"methylation display site","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Histone tails play important roles in the dynamic functions of chromatin through posttranslational modifications such as acetylation, phosphorylation and methylation.","type":"Introduction"}],"curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"27181506","version":2,"reference_html":"Solution structure of the isolated histone H2A-H2B heterodimer. <i> Moriwaki Y, Yamane T, Ohtomo H, Ikeguchi M, Kurita J, Sato M, Nagadoi A, Shimojo H, Nishimura Y. </i> Sci Rep, 2016","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000042","ec_id":"ECO:0006165","region_id":"DP01157r003","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":130,"region_id":"DP01157r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of the isolated histone H2A-H2B heterodimer. <i> Moriwaki Y, Yamane T, Ohtomo H, Ikeguchi M, Kurita J, Sato M, Nagadoi A, Shimojo H, Nishimura Y. </i> Sci Rep, 2016","statement":[{"text":"We examined the secondary structures of the isolated H2A-H2B heterodimer by TROSY-NMR. Almost all of the main-chain signals (i.e., HN, N, Cα, Cβ and C’ signals) could be assigned (96% for H2A; 95% for H2B). As shown in the experimental chemical shift indices obtained from the Cα and Cβ chemical shift values, both H2A and H2B contain a core histone fold comprising four α-helices together with two β-strands—namely, α1–β1–α2–β2–α3–αC, much as is observed for their counterparts in the nucleosome. Outside the histone fold of H2A, however, the N-terminal αN helix and the C-terminal β3 strand and 310 helix observed in the nucleosome are entirely disordered in the isolated H2A-H2B heterodimer.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":98,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"27181506","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"11609"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":130,"term_name":"acetylation display site","start":98,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Histone proteins have N-terminal and/or C-terminal flexible tails, which are modified by methylation and acetylation, and influence chromatin remodeling.","type":"Discussion"}],"curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"27181506","version":2,"reference_html":"Solution structure of the isolated histone H2A-H2B heterodimer. <i> Moriwaki Y, Yamane T, Ohtomo H, Ikeguchi M, Kurita J, Sato M, Nagadoi A, Shimojo H, Nishimura Y. </i> Sci Rep, 2016","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000039","ec_id":"ECO:0006165","region_id":"DP01157r005","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":130,"term_name":"methylation display site","start":98,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Histone tails play important roles in the dynamic functions of chromatin through posttranslational modifications such as acetylation, phosphorylation and methylation.","type":"Introduction"}],"curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"27181506","version":2,"reference_html":"Solution structure of the isolated histone H2A-H2B heterodimer. <i> Moriwaki Y, Yamane T, Ohtomo H, Ikeguchi M, Kurita J, Sato M, Nagadoi A, Shimojo H, Nishimura Y. </i> Sci Rep, 2016","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000042","ec_id":"ECO:0006165","region_id":"DP01157r006","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_P04908","date":"2018-06-26T09:11:41.000Z","acc":"P04908","name":"Histone H2A type 1-B/E","length":130,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012BF64","genes":[{"name":{"value":"H2AC4","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4734","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4734"}}]},"synonyms":[{"value":"H2AFM","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4734","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4734"}}]},{"value":"HIST1H2AB","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4734","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4734"}}]}]},{"name":{"value":"H2AC8","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4724","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4724"}}]},"synonyms":[{"value":"H2AFA","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4724","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4724"}}]},{"value":"HIST1H2AE","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4724","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4724"}}]}]}],"alphafold_very_low_content":0,"disorder_content":0.46153846153846156,"disprot_consensus":{"full":[{"start":1,"end":27,"type":"D"},{"start":98,"end":130,"type":"D"}],"Structural state":[{"start":1,"end":27,"type":"D"},{"start":98,"end":130,"type":"D"}],"Disorder function":[{"start":1,"end":27,"type":"F"},{"start":98,"end":130,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00125","name":"Core histone H2A/H2B/H3/H4 domain","start":20,"end":101}],"gene3D":[{"start":1,"end":126,"id":"1.10.20.10","name":"Histone, subunit A"}]},"uniref50":"UniRef50_P06899","sequence":"MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P06899","disprot_id":"DP01158","ncbi_taxon_id":9606,"regions_counter":3,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":38,"region_id":"DP01158r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Solution structure of the isolated histone H2A-H2B heterodimer. <i> Moriwaki Y, Yamane T, Ohtomo H, Ikeguchi M, Kurita J, Sato M, Nagadoi A, Shimojo H, Nishimura Y. </i> Sci Rep, 2016","statement":[{"text":"H2A and H2B each contain a histone fold, comprising four α-helices and two β-strands (α1-β1-α2-β2-α3-αC), together with the long disordered N- and C-terminal H2A tails and the long N-terminal H2B tail.","type":"Introduction"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27181506","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-05-04T17:51:18.919Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"11609"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04908"}]}],"released":"2018_11","uniref100":"UniRef100_P06899","date":"2018-06-26T09:14:42.000Z","acc":"P06899","name":"Histone H2B type 1-J","length":126,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI0000001BD5","genes":[{"name":{"value":"H2BC11","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4761","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4761"}}]},"synonyms":[{"value":"H2BFR","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4761","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4761"}}]},{"value":"HIST1H2BJ","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4761","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4761"}}]}]}],"alphafold_very_low_content":0.0873015873015873,"disorder_content":0.30158730158730157,"disprot_consensus":{"full":[{"start":1,"end":38,"type":"D"}],"Structural state":[{"start":1,"end":38,"type":"D"}]}},{"features":{"pfam":[{"id":"PF10195","name":"DNA-binding nuclear phosphoprotein p8","start":26,"end":83}]},"uniref50":"UniRef50_A6NF83","sequence":"MEAPAERALPRLQALARPPPPISYEEELYDCLDYYYLRDFPACGAGRSKGRTRREQALRTNWPAPGGHERKVAQKLLNGQRKRRQRQLHPKMRTRLT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_A6NF83","disprot_id":"DP01159","ncbi_taxon_id":9606,"regions_counter":6,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":97,"region_id":"DP01159r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The chromatin nuclear protein NUPR1L is intrinsically disordered and binds to the same proteins as its paralogue. <i> Neira JL, López MB, Sevilla P, Rizzuti B, Cámara-Artigas A, Vidal M, Iovanna JL. </i> Biochem J, 2018","statement":[{"text":"The far-UV CD spectrum of NUPR1L at pH 7.5 had minima at 210 nm, and a wide shoulder around 222 nm, which suggest the presence of helix- or turn-like conformations. This spectrum is different to that observed for NUPR1, with a minimum at around 205 nm, which was characteristic of random-coil conformations. However, as NUPR1L has one Trp, five Tyr, one Phe and two His, we cannot rule out the absorbance of aromatic residues, which also occur at these wavelengths. As it happened with the thermal denaturations followed by fluorescence, the transitions followed by the ellipticity at 222 nm did not show any sigmoidal behaviour, suggesting that possible helical or turn-like conformations were not rigid. We conclude that NUPR1L was an IDP on the basis of two pieces of evidence. The absence of sigmoidal transitions in fluorescence and CD thermal and in the fluorescence chemical denaturations indicates the lack of secondary and tertiary structures. Although such absence is one of the features to assess protein disorder, it could be argued that non- sigmoidal denaturation curves are also due to non-cooperative transitions. However, it would be highly unlikely that non-cooperative transitions for the same protein were observed in chemical and thermal denaturations.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":1,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"29925531","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":97,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"29925531","version":3,"reference_html":"The chromatin nuclear protein NUPR1L is intrinsically disordered and binds to the same proteins as its paralogue. <i> Neira JL, López MB, Sevilla P, Rizzuti B, Cámara-Artigas A, Vidal M, Iovanna JL. </i> Biochem J, 2018","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP01159r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":97,"region_id":"DP01159r003","released":"2022_03","ec_id":"ECO:0001249","reference_html":"The chromatin nuclear protein NUPR1L is intrinsically disordered and binds to the same proteins as its paralogue. <i> Neira JL, López MB, Sevilla P, Rizzuti B, Cámara-Artigas A, Vidal M, Iovanna JL. </i> Biochem J, 2018","statement":[{"text":"Thermal denaturations of NUPR1L at several pH values (3.0, 5.5, 7.0, 8.4 and 13.0) were carried out by following the changes in the intrinsic fluorescence. At all pH values explored, we did not observe any sigmoidal transition, and protein precipitation was observed at acidic pH. Thermal denaturations of isolated NUPR1 do not show any sigmoidal transition. We also tried to follow the denaturation of NUPR1L in the presence of urea by excitation either at 280 or 295 nm. However, as it happened with the thermal denaturations, no sigmoidal curves were observed at any of the two excitation wavelengths. A similar behaviour has been reported in the chemical denaturations of isolated NUPR.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":1,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"29925531","version":2,"ec_name":"fluorescence evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":97,"term_name":"protein binding","start":1,"ec_name":"fluorescence evidence used in manual assertion","curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"29925531","version":3,"reference_html":"The chromatin nuclear protein NUPR1L is intrinsically disordered and binds to the same proteins as its paralogue. <i> Neira JL, López MB, Sevilla P, Rizzuti B, Cámara-Artigas A, Vidal M, Iovanna JL. </i> Biochem J, 2018","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0001249","region_id":"DP01159r004","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":97,"region_id":"DP01159r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The chromatin nuclear protein NUPR1L is intrinsically disordered and binds to the same proteins as its paralogue. <i> Neira JL, López MB, Sevilla P, Rizzuti B, Cámara-Artigas A, Vidal M, Iovanna JL. </i> Biochem J, 2018","statement":[{"text":"We acquired a 1D 1H NMR spectrum at very low NUPR1L concentration (9 μM, in protomer units) at pH 8.0, in the presence of 500 mM NaCl and 1 mM β-ME. In the up-field region of the spectrum, all the methyl protons appeared clustered around 0.9 ppm, as they are expected in a polypeptide chain devoid of rigid secondary and tertiary structures. On the other hand, in the amide region a very low signal intensity was observed and very broad peaks were detected (the sharp peaks are due to the aromatic protons of the His-tail (around 8.5 ppm) and the presence of protons of the bases of deoxy-oligonucleotides); furthermore, no signal, around 10.20 ppm, was observed for the indole moiety of Trp62, where it should be observed for a disordered polypeptide chain [61]. These results can be explained as due to: (i) the presence of slow-to-intermediate conformational exchange in NUPR1L involving such aromatic ring, which broadens the signal; or alternatively, (ii) signal broadening due to presence of large molecular weight species. The latter explanation agrees with the experimental observation that Trp62 was involved in the self-association equilibrium of NUPR1L as shown by the quenching results. Then, the NMR indicates that NUPR1L was a disordered protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":1,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"29925531","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":97,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"We have shown that NUPR1L was capable of interacting with the same partners of NUPR1, namely, prothymosin α and C-RING1B. However, while the affinity for prothymosin α was the same, within the uncertainty, for both protein isoforms, in the case of C-RING1B the apparent affinity of NUPR1L was smaller (i.e., larger Kd) compared to that of NUPR1: 60 μM versus 10 μM. This difference is due to the self-association of NUPR1L, since the reported constants should include the dissociation of both C-RING1B and NUPR1L, unless the complex involves the formation of a higher-order state between the oligomeric species of both proteins, in which case the real affinity between the two proteins must be lower.","type":"Discussion"}],"curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"29925531","version":3,"reference_html":"The chromatin nuclear protein NUPR1L is intrinsically disordered and binds to the same proteins as its paralogue. <i> Neira JL, López MB, Sevilla P, Rizzuti B, Cámara-Artigas A, Vidal M, Iovanna JL. </i> Biochem J, 2018","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP01159r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_A6NF83","date":"2018-06-26T11:40:38.000Z","acc":"A6NF83","name":"Nuclear protein 2","length":97,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00001D751D","genes":[{"name":{"value":"NUPR2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:44164","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:44164"}}]},"synonyms":[{"value":"NUPR1L","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"25899918","url":"http://www.ncbi.nlm.nih.gov/pubmed/25899918","alternativeUrl":"https://europepmc.org/abstract/MED/25899918"}}]}]}],"alphafold_very_low_content":0.030927835051546393,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":97,"type":"D"}],"Structural state":[{"start":1,"end":97,"type":"D"}],"Molecular function":[{"start":1,"end":97,"type":"F"}]}},{"features":{"pfam":[{"id":"PF13419","name":"Haloacid dehalogenase-like hydrolase","start":82,"end":258}],"gene3D":[{"start":93,"end":157,"id":"1.10.150.240","name":"Putative phosphatase; domain 2"},{"start":82,"end":276,"id":"3.40.50.1000","name":"HAD superfamily/HAD-like"}]},"uniref50":"UniRef50_P68910","sequence":"MSSPRERRPASQAPRLSRRPPAHQTSRSSPDTTAPTGSGLSNRFVNDNGIVTDTTASGTNCPPPPRAAARRASSPGESPQLVIFDLDGTLTDSARGIVSSFRHALNHIGAPVPEGDLATHIVGPPMHETLRAMGLGESAEEAIVAYRADYSARGWAMNSLFDGIGPLLADLRTAGVRLAVATSKAEPTARRILRHFGIEQHFEVIAGASTDGSRGSKVDVLAHALAQLRPLPERLVMVGDRSHDVDGAAAHGIDTVVVGWGYGRADFIDKTSTTVVTHAATIDELREALGV","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"uniref90":"UniRef90_P68910","disprot_id":"DP01160","ncbi_taxon_id":83332,"regions_counter":2,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":81,"region_id":"DP01160r001","released":"2025_06","ec_id":"ECO:0006165","reference_html":"The domain architecture of PtkA, the first tyrosine kinase from <i>Mycobacterium tuberculosis</i>, differs from the conventional kinase architecture. <i> Niesteruk A, Jonker HRA, Richter C, Linhard V, Sreeramulu S, Schwalbe H. </i> J Biol Chem, 2018","statement":[{"text":"The sequence-based analysis of PtkA (30.6 kDa, 291 amino acids) predicts a high disorder tendency for the N-terminal part comprising 80 amino acids (Fig. S1). Our NMR data confirm the prediction, showing that PtkA consists of a well-folded KCD and an unstructured IDD. The 2D 1H,15N TROSY spectrum of the full-length PtkA shows in total 231 of 270 expected amide resonances (Fig. 1A). Two subsets of signals can be clearly observed: (i) a set of well-dispersed peaks, typical for a well-folded structure, and (ii) another set of signals with high intensity, which are clustered in the center of the spectrum (1H: 7.6–8.6 ppm), indicative of unstructured regions within the full-length PtkA. The 2D 1H,15N HSQC spectrum of PtkA shows only minor changes of the chemical shift in the presence of ATP (Fig. S8).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"29884774","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2025-01-22T19:42:07.100Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":81,"term_name":"self-inhibition","start":1,"ec_name":"in vitro protein kinase assay evidence used in manual assertion","statement":[{"text":"The results thus obtained suggest that the KCDPtkA is 5 times more active than the full-length PtkA. Activity of the KCDPtkA measured together with isolated IDD (IDDPtkA) shows a decrease compared with the KCDPtkA alone, suggesting that the IDD has an inhibitory effect on the kinase activity.","type":"Results"},{"text":" The decrease of the PtkA activity in the presence of IDD suggests an inhibitory effect of the disordered domain during the autophosphorylation. Spin label studies indicated the existence of residual long-range transient interactions of the IDD with the KCD.","type":"Discussion"},{"text":"These results strongly suggest that the IDD transiently binds to the KCD and masks the substrate-binding site and inhibits the kinase activity.","type":"Results"}],"curator_id":"vnugnes","released":"2025_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"29884774","version":4,"reference_html":"The domain architecture of PtkA, the first tyrosine kinase from <i>Mycobacterium tuberculosis</i>, differs from the conventional kinase architecture. <i> Niesteruk A, Jonker HRA, Richter C, Linhard V, Sreeramulu S, Schwalbe H. </i> J Biol Chem, 2018","date":"2025-01-22T19:50:52.860Z","term_id":"IDPO:0000059","ec_id":"ECO:0001202","region_id":"DP01160r002","ec_go":"EXP","disprot_namespace":"Disorder function","curator_orcid":"0000-0001-8399-7907"}],"released":"2025_06","uniref100":"UniRef100_P68910","date":"2018-06-26T12:34:21.000Z","acc":"P9WPI9","name":"Uncharacterized protein Rv2232","length":291,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","dataset":["Bacterial virulence-related proteins"],"UniParc":"UPI000013B8E5","genes":[{"name":{"value":"ptkA","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"19366344","url":"http://www.ncbi.nlm.nih.gov/pubmed/19366344","alternativeUrl":"https://europepmc.org/abstract/MED/19366344"}}]},"orfNames":[{"value":"MTCY427.13/MTCY427.14"}],"olnNames":[{"value":"Rv2232"}]}],"alphafold_very_low_content":0.20962199312714777,"disorder_content":0.27835051546391754,"disprot_consensus":{"full":[{"start":1,"end":81,"type":"D"}],"Structural state":[{"start":1,"end":81,"type":"D"}],"Disorder function":[{"start":1,"end":81,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04564","name":"U-box domain","start":3,"end":54},{"id":"PF08606","name":"Prp19/Pso4-like","start":68,"end":134},{"id":"PF24814","name":"Prp19 WD40 domain","start":216,"end":496}],"gene3D":[{"start":2,"end":58,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":195,"end":504,"id":"2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"}]},"uniref50":"UniRef50_Q9UMS4","sequence":"MSLICSISNEVPEHPCVSPVSNHVYERRLIEKYIAENGTDPINNQPLSEEQLIDIKVAHPIRPKPPSATSIPAILKALQDEWDAVMLHSFTLRQQLQTTRQELSHALYQHDAACRVIARLTKEVTAAREALATLKPQAGLIVPQAVPSSQPSVVGAGEPMDLGELVGMTPEIIQKLQDKATVLTTERKKRGKTVPEELVKPEELSKYRQVASHVGLHSASIPGILALDLCPSDTNKILTGGADKNVVVFDKSSEQILATLKGHTKKVTSVVFHPSQDLVFSASPDATIRIWSVPNASCVQVVRAHESAVTGLSLHATGDYLLSSSDDQYWAFSDIQTGRVLTKVTDETSGCSLTCAQFHPDGLIFGTGTMDSQIKIWDLKERTNVANFPGHSGPITSIAFSENGYYLATAADDSSVKLWDLRKLKNFKTLQLDNNFEVKSLIFDQSGTYLALGGTDVQIYICKQWTEILHFTEHSGLTTGVAFGHHAKFIASTGMDRSLKFYSL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UMS4","disprot_id":"DP01161","ncbi_taxon_id":9606,"regions_counter":1,"creator":"mpajkos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":194,"region_id":"DP01161r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the WD40 domain of human PRPF19. <i> Zhang Y, Li Y, Liang X, Zhu Z, Sun H, He H, Min J, Liao S, Liu Y. </i> Biochem Biophys Res Commun, 2017","statement":[{"text":"The structure covering the WD40 domain part of human PRFP19 (residues 169–504 ) has been solved. Residues 169-194 was invisible in the structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":169,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4LG8"}],"reference_id":"28962858","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9UMS4","date":"2018-06-26T13:01:08.000Z","acc":"Q9UMS4","name":"Pre-mRNA-processing factor 19","length":504,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000003F659","genes":[{"name":{"value":"PRPF19","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:17896","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:17896"}}]},"synonyms":[{"value":"NMP200","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11082287","url":"http://www.ncbi.nlm.nih.gov/pubmed/11082287","alternativeUrl":"https://europepmc.org/abstract/MED/11082287"}}]},{"value":"PRP19","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11435423","url":"http://www.ncbi.nlm.nih.gov/pubmed/11435423","alternativeUrl":"https://europepmc.org/abstract/MED/11435423"}}]},{"value":"SNEV","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16332694","url":"http://www.ncbi.nlm.nih.gov/pubmed/16332694","alternativeUrl":"https://europepmc.org/abstract/MED/16332694"}}]}]}],"alphafold_very_low_content":0.06349206349206349,"disorder_content":0.051587301587301584,"disprot_consensus":{"full":[{"start":169,"end":194,"type":"D"}],"Structural state":[{"start":169,"end":194,"type":"D"}]}},{"features":{"pfam":[{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":46,"end":134},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":188,"end":259},{"id":"PF15898","name":"cGMP-dependent protein kinase interacting domain","start":931,"end":1030}],"gene3D":[{"start":163,"end":299,"id":"1.25.40.20","name":"Ankyrin repeat-containing domain"},{"start":1,"end":162,"id":"1.25.40.20","name":"Ankyrin repeat-containing domain"}]},"uniref50":"UniRef50_O14974","sequence":"MKMADAKQKRNEQLKRWIGSETDLEPPVVKRQKTKVKFDDGAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIEAARKEEERIMLRDARQWLNSGHINDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVADEDILGYLEELQKKQNLLHSEKRDKKSPLIESTANMDNNQSQKTFKNKETLIIEPEKNASRIESLEQEKVDEEEEGKKDESSCSSEEDEEDDSESEAETDKTKPLASVTNANTSSTQAAPVAVTTPTVSSGQATPTSPIKKFPTTATKISPKEEERKDESPATWRLGLRKTGSYGALAEITASKEGQKEKDTAGVTRSASSPRLSSSLDNKEKEKDSKGTRLAYVAPTIPRRLASTSDIEEKENRDSSSLRTSSSYTRRKWEDDLKKNSSVNEGSTYHKSCSFGRRQDDLISSSVPSTTSTPTVTSAAGLQKSLLSSTSTTTKITTGSSSAGTQSSTSNRLWAEDSTEKEKDSVPTAVTIPVAPTVVNAAASTTTLTTTTAGTVSSTTEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRSRSTRTREQENEEKEKEEKEKQDKEKQEEKKESETSREDEYKQKYSRTYDETYQRYRPVSTSSSTTPSSSLSTMSSSLYASSQLNRPNSLVGITSAYSRGITKENEREGEKREEEKEGEDKSQPKSIRERRRPREKRRSTGVSFWTQDSDENEQEQQSDTEEGSNKKETQTDSISRYETSSTSAGDRYDSLLGRSGSYSYLEERKPYSSRLEKDDSTDFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKATQRQERFADRSLLEMEKRERRALERRISEMEEELKMLPDLKADNQRLKDENGALIRVISKLSK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O14974","disprot_id":"DP01163","ncbi_taxon_id":9606,"regions_counter":2,"creator":"jmanso","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":40,"region_id":"DP01163r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Structural signature of the MYPT1-PP1 interaction. <i> Pinheiro AS, Marsh JA, Forman-Kay JD, Peti W. </i> J Am Chem Soc, 2011","statement":[{"text":"MYPT1 residues 1-40 form the disordered region, while MYPT1 residues 41-98 form the folded ankyrin-repeat region.","type":"Results"},{"text":"Furthermore, while i,i+1 1HN-1HN NOE cross-peaks, typical for α-helical secondary structure elements, can be detected in the well-folded ankyrin-repeat region (residues 41-98) of MYPT11-98, no significant i,i+1 1HN-1HN NOE cross-peaks are identified in the disordered region (residues 1-40).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-16T16:33:21.109Z","reference_source":"pmid","term_name":"disorder","reference_id":"21142030","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_O14974","date":"2018-06-26T14:44:54.000Z","acc":"O14974","name":"Protein phosphatase 1 regulatory subunit 12A","length":1030,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI0000073E69","genes":[{"name":{"value":"PPP1R12A","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:7618","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:7618"}}]},"synonyms":[{"value":"MBS"},{"value":"MYPT1","evidences":[{"code":"ECO:0000305"}]}]}],"alphafold_very_low_content":0.5300970873786408,"disorder_content":0.038834951456310676,"disprot_consensus":{"full":[{"start":1,"end":40,"type":"D"}],"Structural state":[{"start":1,"end":40,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00018","name":"SH3 domain","start":1064,"end":1110},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":936,"end":1018},{"id":"PF21801","name":"Apoptosis-stimulating of p53 protein 2-like, N-terminal RA domain","start":3,"end":82}],"gene3D":[{"start":904,"end":1128,"id":"1.25.40.20","name":"Ankyrin repeat-containing domain"},{"start":1,"end":83,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"}]},"uniref50":"UniRef50_Q13625","sequence":"MMPMFLTVYLSNNEQHFTEVPVTPETICRDVVDLCKEPGESDCHLAEVWCGSERPVADNERMFDVLQRFGSQRNEVRFFLRHERPPGRDIVSGPRSQDPSLKRNGVKVPGEYRRKENGVNSPRMDLTLAELQEMASRQQQQIEAQQQLLATKEQRLKFLKQQDQRQQQQVAEQEKLKRLKEIAENQEAKLKKVRALKGHVEQKRLSNGKLVEEIEQMNNLFQQKQRELVLAVSKVEELTRQLEMLKNGRIDSHHDNQSAVAELDRLYKELQLRNKLNQEQNAKLQQQRECLNKRNSEVAVMDKRVNELRDRLWKKKAALQQKENLPVSSDGNLPQQAASAPSRVAAVGPYIQSSTMPRMPSRPELLVKPALPDGSLVIQASEGPMKIQTLPNMRSGAASQTKGSKIHPVGPDWSPSNADLFPSQGSASVPQSTGNALDQVDDGEVPLREKEKKVRPFSMFDAVDQSNAPPSFGTLRKNQSSEDILRDAQVANKNVAKVPPPVPTKPKQINLPYFGQTNQPPSDIKPDGSSQQLSTVVPSMGTKPKPAGQQPRVLLSPSIPSVGQDQTLSPGSKQESPPAAAVRPFTPQPSKDTLLPPFRKPQTVAASSIYSMYTQQQAPGKNFQQAVQSALTKTHTRGPHFSSVYGKPVIAAAQNQQQHPENIYSNSQGKPGSPEPETEPVSSVQENHENERIPRPLSPTKLLPFLSNPYRNQSDADLEALRKKLSNAPRPLKKRSSITEPEGPNGPNIQKLLYQRTTIAAMETISVPSYPSKSASVTASSESPVEIQNPYLHVEPEKEVVSLVPESLSPEDVGNASTENSDMPAPSPGLDYEPEGVPDNSPNLQNNPEEPNPEAPHVLDVYLEEYPPYPPPPYPSGEPEGPGEDSVSMRPPEITGQVSLPPGKRTNLRKTGSERIAHGMRVKFNPLALLLDSSLEGEFDLVQRIIYEVDDPSLPNDEGITALHNAVCAGHTEIVKFLVQFGVNVNAADSDGWTPLHCAASCNNVQVCKFLVESGAAVFAMTYSDMQTAADKCEEMEEGYTQCSQFLYGVQEKMGIMNKGVIYALWDYEPQNDDELPMKEGDCMTIIHREDEDEIEWWWARLNDKEGYVPRNLLGLYPRIKPRQRSLA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q13625","disprot_id":"DP01164","ncbi_taxon_id":9606,"regions_counter":18,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":692,"region_id":"DP01164r001","released":"2023_12","ec_id":"ECO:0007680","reference_html":"An Intrinsically Disordered Region in the Proapoptotic ASPP2 Protein Binds to the Helicobacter pylori Oncoprotein CagA. <i> Reingewertz TH, Iosub-Amir A, Bonsor DA, Mayer G, Amartely H, Friedler A, Sundberg EJ. </i> Biochemistry, 2015","statement":[{"text":"Using size exclusion chromatography, we observed a low level of compactness for ASPP2331–692, indicative of an extended conformation of this domain, typical of intrinsically disordered proteins.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":331,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"chromatography evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-24T15:41:49.908Z","reference_source":"pmid","term_name":"disorder","reference_id":"25963096","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":692,"region_id":"DP01164r002","released":"2023_12","ec_id":"ECO:0006204","reference_html":"An Intrinsically Disordered Region in the Proapoptotic ASPP2 Protein Binds to the Helicobacter pylori Oncoprotein CagA. <i> Reingewertz TH, Iosub-Amir A, Bonsor DA, Mayer G, Amartely H, Friedler A, Sundberg EJ. </i> Biochemistry, 2015","statement":[{"text":"We also analyzed ASPP2331–692 by far-UV CD and observed a spectrum that consisted mainly of a minimum at 200 nm, indicative of a high content of unstructured protein (Figure 2C). We calculated the secondary structure content (47, 48) of ASPP2331–692 to be 56% disordered, 2% helix, 28% strand, and 14% turn conformations.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":331,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-24T16:18:32.056Z","reference_source":"pmid","term_name":"disorder","reference_id":"25963096","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":692,"region_id":"DP01164r004","released":"2023_12","ec_id":"ECO:0006165","reference_html":"An Intrinsically Disordered Region in the Proapoptotic ASPP2 Protein Binds to the Helicobacter pylori Oncoprotein CagA. <i> Reingewertz TH, Iosub-Amir A, Bonsor DA, Mayer G, Amartely H, Friedler A, Sundberg EJ. </i> Biochemistry, 2015","statement":[{"text":"The HSQC-TROSY spectrum of 15N-labeled ASPP2331–692 exhibited a pattern typical for disordered proteins (Figure 2E), in which the observed resonances of the amide protons are dispersed in a narrow cluster ranged from δ1H 7.7 to 8.5 ppm (Δ = 0.8 ppm), unlike wider distributions typical for structured proteins.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":331,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-24T15:43:50.687Z","reference_source":"pmid","term_name":"disorder","reference_id":"25963096","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":918,"region_id":"DP01164r006","released":"2023_12","ec_id":"ECO:0007680","reference_html":"The structure and interactions of the proline-rich domain of ASPP2. <i> Rotem S, Katz C, Benyamini H, Lebendiker M, Veprintsev D, Rüdiger S, Danieli T, Friedler A. </i> J Biol Chem, 2008","statement":[{"text":"The ASPP2 Pro domain eluted earlier than predicted from its molecular mass, and its apparent molecular mass estimated from the calibration curve was ∼130,000 Da (Fig. 2A), a value five times higher than the theoretical value of 24,500 Da. This early elution in the gel filtration may be attributed to an extended or unfolded native structure of the protein (39) or to putative oligomerization.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":693,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"chromatography evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-24T16:22:36.936Z","reference_source":"pmid","term_name":"disorder","reference_id":"18448430","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":918,"region_id":"DP01164r007","released":"2023_12","ec_id":"ECO:0006204","reference_html":"The structure and interactions of the proline-rich domain of ASPP2. <i> Rotem S, Katz C, Benyamini H, Lebendiker M, Veprintsev D, Rüdiger S, Danieli T, Friedler A. </i> J Biol Chem, 2008","statement":[{"text":"The far-UV CD spectrum of the recombinant purified protein exhibited a minimum at only ∼200 nm (Fig. 3A), suggesting a highly unstructured conformation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":693,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-24T16:23:02.920Z","reference_source":"pmid","term_name":"disorder","reference_id":"18448430","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":484,"end":692,"reference_id":"25963096","reference_source":"pmid","reference_html":"An Intrinsically Disordered Region in the Proapoptotic ASPP2 Protein Binds to the Helicobacter pylori Oncoprotein CagA. <i> Reingewertz TH, Iosub-Amir A, Bonsor DA, Mayer G, Amartely H, Friedler A, Sundberg EJ. </i> Biochemistry, 2015","date":"2023-08-24T16:08:42.317Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P80200","operator":null,"partner_start":1,"partner_end":256}],"region_id":"DP01164r008","statement":[{"text":"By further dissecting ASPP2331–692 into two nonoverlapping parts, we observed that this interaction is mediated solely through residues 484–692, as ASPP2484–692 bound CagA with a KD of 13 μM (Figure 4B), with no contribution to binding from the N-terminal part, ASPP2331–484 (Figure 4C).","type":"Results"},{"text":"Conversely, we observed no binding between ASPP2484–692 and CagA256–885 by both ITC (Figure 4H and Table 1) and SPR (Figure 4I). These data indicate that ASPP2484–692 interacts with the extreme N-terminal domain of CagA, inclusive of residues 1–256, which also contains the binding site for ASPP2746–765.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":331,"end":692,"reference_id":"25963096","reference_source":"pmid","reference_html":"An Intrinsically Disordered Region in the Proapoptotic ASPP2 Protein Binds to the Helicobacter pylori Oncoprotein CagA. <i> Reingewertz TH, Iosub-Amir A, Bonsor DA, Mayer G, Amartely H, Friedler A, Sundberg EJ. </i> Biochemistry, 2015","date":"2023-08-24T16:02:41.740Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001245","ec_ontology":"ECO","ec_name":"peptide array evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P80200","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01164r009","statement":[{"text":"Although CagA1–885 bound several peptides (I24-ASPP2386–400, J1-ASPP2397–411, and J6-ASPP2440–454) within the ASPP2331–484 region that did not bind as a contiguous protein fragment in our SPR experiments, peptides derived from the ASPP2484–692 region that confers CagA binding were both more numerous and prominent (Figure 4F). In particular, peptides centered within a set of binding peptides (J12-ASPP2494–508 and J17-ASPP2541–555) and peptides of the highest intensity (J21-ASPP2577–591 and K6-ASPP2656–670) are likely to comprise the noncontiguous binding determinants of the ASPP2484–692 protein fragment.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":484,"end":692,"reference_id":"25963096","reference_source":"pmid","reference_html":"An Intrinsically Disordered Region in the Proapoptotic ASPP2 Protein Binds to the Helicobacter pylori Oncoprotein CagA. <i> Reingewertz TH, Iosub-Amir A, Bonsor DA, Mayer G, Amartely H, Friedler A, Sundberg EJ. </i> Biochemistry, 2015","date":"2023-08-24T16:08:52.532Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P80200","operator":null,"partner_start":1,"partner_end":256}],"region_id":"DP01164r010","statement":[{"text":"When we measured the thermodynamic parameters of binding between ASPP2484–692 and CagA1–885 (Figure 4G and Table 1), we observed binding with similar affinity (KD = 4.9 ± 0.5 μM) to that from the analogous experiment carried out by SPR. Conversely, we observed no binding between ASPP2484–692 and CagA256–885 by both ITC (Figure 4H and Table 1) and SPR (Figure 4I). These data indicate that ASPP2484–692 interacts with the extreme N-terminal domain of CagA, inclusive of residues 1–256, which also contains the binding site for ASPP2746–765.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":693,"end":918,"reference_id":"25963096","reference_source":"pmid","reference_html":"An Intrinsically Disordered Region in the Proapoptotic ASPP2 Protein Binds to the Helicobacter pylori Oncoprotein CagA. <i> Reingewertz TH, Iosub-Amir A, Bonsor DA, Mayer G, Amartely H, Friedler A, Sundberg EJ. </i> Biochemistry, 2015","date":"2023-08-24T16:14:52.857Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P80200","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01164r011","statement":[{"text":"To quantify and analyze the thermodynamic profile of the CagA interactions with the Pro-rich and Ank-SH3 domains of ASPP2, we performed isothermal titration calorimetry using CagA1–885 and the ASPP2 Pro-rich and Ank-SH3 domains either alone (ASPP2693–918 and ASPP2893–1128, respectively) or together (as a single fused fragment, ASPP2693–1128). We found that CagA1–885 bound ASPP2693–1128, inclusive of both Pro-rich and Ank-SH3 domains, as a 1:1 complex with an affinity of 62 nM (Figure 5A). This interaction is entirely dependent on the presence of the Pro-rich domain, as we detected no binding between CagA and the ASPP2 Ank-SH3 domain (Figure 5B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":710,"end":904,"reference_id":"25963096","reference_source":"pmid","reference_html":"An Intrinsically Disordered Region in the Proapoptotic ASPP2 Protein Binds to the Helicobacter pylori Oncoprotein CagA. <i> Reingewertz TH, Iosub-Amir A, Bonsor DA, Mayer G, Amartely H, Friedler A, Sundberg EJ. </i> Biochemistry, 2015","date":"2023-08-24T16:14:42.513Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001245","ec_ontology":"ECO","ec_name":"peptide array evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P80200","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01164r012","statement":[{"text":"In the ASPP2 Pro-rich domain, three sets of binding peptides included (i) K12-ASPP2710–724/K13-ASPP2721–735, (ii) K15-ASPP2739–753/K16-ASPP2746–760, and (iii) L8-ASPP2890–904/L9-ASPP2901–915/L10-ASPP2908–922.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":693,"end":918,"reference_id":"25963096","reference_source":"pmid","reference_html":"An Intrinsically Disordered Region in the Proapoptotic ASPP2 Protein Binds to the Helicobacter pylori Oncoprotein CagA. <i> Reingewertz TH, Iosub-Amir A, Bonsor DA, Mayer G, Amartely H, Friedler A, Sundberg EJ. </i> Biochemistry, 2015","date":"2023-08-24T16:28:22.530Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006077","ec_ontology":"ECO","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"region_id":"DP01164r013","statement":[{"text":"We performed a nickel-affinity pulldown experiment to test whether the two domains interact with each other. ASPP2 Ank-SH3 was retrieved by nickel beads following its incubation with His-tagged ASPP2 Pro but not when incubated with the nickel beads alone (Fig. 4A).","type":"Results"}]},{"start":693,"end":918,"reference_id":"25963096","reference_source":"pmid","reference_html":"An Intrinsically Disordered Region in the Proapoptotic ASPP2 Protein Binds to the Helicobacter pylori Oncoprotein CagA. <i> Reingewertz TH, Iosub-Amir A, Bonsor DA, Mayer G, Amartely H, Friedler A, Sundberg EJ. </i> Biochemistry, 2015","date":"2023-08-24T16:33:06.042Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006077","ec_ontology":"ECO","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q13625","operator":null,"partner_start":893,"partner_end":1128}],"region_id":"DP01164r014","statement":[{"text":"We performed a nickel-affinity pulldown experiment to test whether the two domains interact with each other. ASPP2 Ank-SH3 was retrieved by nickel beads following its incubation with His-tagged ASPP2 Pro but not when incubated with the nickel beads alone (Fig. 4A).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":693,"end":752,"reference_id":"25963096","reference_source":"pmid","reference_html":"An Intrinsically Disordered Region in the Proapoptotic ASPP2 Protein Binds to the Helicobacter pylori Oncoprotein CagA. <i> Reingewertz TH, Iosub-Amir A, Bonsor DA, Mayer G, Amartely H, Friedler A, Sundberg EJ. </i> Biochemistry, 2015","date":"2023-08-24T16:35:01.768Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001245","ec_ontology":"ECO","ec_name":"peptide array evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q13625","operator":null,"partner_start":931,"partner_end":961},{"db":"UniProt","id":"Q13625","operator":"and","partner_start":1083,"partner_end":1096}],"region_id":"DP01164r015","statement":[{"text":"ASPP2 Pro-bound peptides from the first Ank repeat (aa 931–961) and from the SH3 domain (aa 1083–1096) (Table 1 and Fig. 5, A, B, and D). Screening a second peptide array revealed that ASPP2 Ank-SH3 bound several peptides derived from ASPP2 Pro (Table 2 and Fig. 5, C and D). These peptides are located between residues 693 and 752 at the N-terminal region of the ASPP2 Pro domain, and between residues 893 and 912 at its C terminus.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":893,"end":912,"reference_id":"25963096","reference_source":"pmid","reference_html":"An Intrinsically Disordered Region in the Proapoptotic ASPP2 Protein Binds to the Helicobacter pylori Oncoprotein CagA. <i> Reingewertz TH, Iosub-Amir A, Bonsor DA, Mayer G, Amartely H, Friedler A, Sundberg EJ. </i> Biochemistry, 2015","date":"2023-08-24T16:35:11.116Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001245","ec_ontology":"ECO","ec_name":"peptide array evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q13625","operator":null,"partner_start":931,"partner_end":961},{"db":"UniProt","id":"Q13625","operator":"and","partner_start":1083,"partner_end":1096}],"region_id":"DP01164r016","statement":[{"text":"ASPP2 Pro-bound peptides from the first Ank repeat (aa 931–961) and from the SH3 domain (aa 1083–1096) (Table 1 and Fig. 5, A, B, and D). Screening a second peptide array revealed that ASPP2 Ank-SH3 bound several peptides derived from ASPP2 Pro (Table 2 and Fig. 5, C and D). These peptides are located between residues 693 and 752 at the N-terminal region of the ASPP2 Pro domain, and between residues 893 and 912 at its C terminus.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":693,"end":918,"reference_id":"25963096","reference_source":"pmid","reference_html":"An Intrinsically Disordered Region in the Proapoptotic ASPP2 Protein Binds to the Helicobacter pylori Oncoprotein CagA. <i> Reingewertz TH, Iosub-Amir A, Bonsor DA, Mayer G, Amartely H, Friedler A, Sundberg EJ. </i> Biochemistry, 2015","date":"2023-08-24T16:51:03.770Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000059","term_name":"self-inhibition","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005632","ec_ontology":"ECO","ec_name":"fluorescence anisotropy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01164r017","statement":[{"text":"We used fluorescence anisotropy to test the affinity of ASPP2 Ank-SH3 and ASPP2 Pro-Ank-SH3 to this peptide. ASPP2 Ank-SH3 bound NFκB 303–332 with Kd = 0.27 μm, whereas ASPP2 Pro-Ank-SH3 bound this peptide with Kd = 1.2 μm, an order of magnitude weaker (Fig. 7A). This shows that the presence of the proline-rich domain inhibits the interaction of ASPP2 Ank-SH3 with the NFκB peptide.","type":"Results"},{"text":"In summary, our results show that the interaction between ASPP2 Pro and ASPP2 Ank-SH3 inhibits the intermolecular interaction of the latter with the NFκB peptide.","type":"Results"}]},{"start":693,"end":918,"reference_id":"25963096","reference_source":"pmid","reference_html":"An Intrinsically Disordered Region in the Proapoptotic ASPP2 Protein Binds to the Helicobacter pylori Oncoprotein CagA. <i> Reingewertz TH, Iosub-Amir A, Bonsor DA, Mayer G, Amartely H, Friedler A, Sundberg EJ. </i> Biochemistry, 2015","date":"2023-08-24T16:50:45.036Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000059","term_name":"self-inhibition","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006309","ec_ontology":"ECO","ec_name":"competitive binding evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01164r018","statement":[{"text":"Next, we tested by competition fluorescence anisotropy whether NFκB 303–332 and the ASPP2 Pro-derived peptide ASPP2 723–737 compete on the same binding site in ASPP2 Ank-SH3. When unlabeled ASPP2 723–737 was added to a pre-formed complex of ASPP2 Ank-SH3 and fluorescently labeled NFκB 303–332 at IS = 50 mm, competition took place and the anisotropy decreased almost completely back to the initial values (Fig. 7B). The same trend was observed when the competition was performed in the opposite way: Unlabeled NFκB 303–332 displaced fluorescently labeled ASPP2 723–737 even quicker (Fig. 7C), because its affinity to ASPP2 Ank-SH3 was much tighter.","type":"Results"},{"text":"In summary, our results show that the interaction between ASPP2 Pro and ASPP2 Ank-SH3 inhibits the intermolecular interaction of the latter with the NFκB peptide.","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_Q13625","date":"2018-06-26T14:45:13.000Z","acc":"Q13625","name":"Apoptosis-stimulating of p53 protein 2","length":1128,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000131032","genes":[{"name":{"value":"TP53BP2"},"synonyms":[{"value":"ASPP2"},{"value":"BBP"}]}],"alphafold_very_low_content":0.5186170212765957,"disorder_content":0.5212765957446809,"disprot_consensus":{"full":[{"start":331,"end":918,"type":"D"}],"Structural state":[{"start":331,"end":918,"type":"D"}],"Molecular function":[{"start":331,"end":918,"type":"F"}],"Disorder function":[{"start":693,"end":918,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01467","name":"Cytidylyltransferase-like","start":12,"end":228}]},"uniref50":"UniRef50_Q9HAN9","sequence":"MENSEKTEVVLLACGSFNPITNMHLRLFELAKDYMNGTGRYTVVKGIISPVGDAYKKKGLIPAYHRVIMAELATKNSKWVEVDTWESLQKEWKETLKVLRHHQEKLEASDCDHQQNSPTLERPGRKRKWTETQDSSQKKSLEPKTKAVPKVKLLCGADLLESFAVPNLWKSEDITQIVANYGLICVTRAGNDAQKFIYESDVLWKHRSNIHVVNEWIANDISSTKIRRALRRGQSIRYLVPDLVQEYIEKHNLYSSESEDRNAGVILAPLQRNTAEAKT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9HAN9","disprot_id":"DP01165","ncbi_taxon_id":9606,"regions_counter":1,"creator":"jmanso","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":146,"region_id":"DP01165r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of human nicotinamide/nicotinic acid mononucleotide adenylyltransferase. Basis for the dual substrate specificity and activation of the oncolytic agent tiazofurin. <i> Zhou T, Kurnasov O, Tomchick DR, Binns DD, Grishin NV, Marquez VE, Osterman AL, Zhang H. </i> J Biol Chem, 2002","statement":[{"text":"Additionally, a stretch of\n37 residues between helix C and strand d (from 109 to 146) is\nalso disordered in the crystal. This region contains the predicted\nnuclear localization signal (NLS) sequence PGRKRKW\nand two putative phosphorylation site serine residues (Ser-109\nand Ser-136)","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jmanso","start":109,"term_ontology":"IDPO","curator_name":"Jose A Manso","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1KQN"}],"reference_id":"11788603","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-16T16:24:18.101Z"}}],"released":"2018_11","uniref100":"UniRef100_Q9HAN9","date":"2018-06-26T14:45:36.000Z","acc":"Q9HAN9","name":"Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1","length":279,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI0000041261","genes":[{"name":{"value":"NMNAT1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:17877","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:17877"}}]},"synonyms":[{"value":"NMNAT"}]}],"alphafold_very_low_content":0.1039426523297491,"disorder_content":0.13620071684587814,"disprot_consensus":{"full":[{"start":109,"end":146,"type":"D"}],"Structural state":[{"start":109,"end":146,"type":"D"}]}},{"features":{"pfam":[{"id":"PF05925","name":"Enterobacterial virulence protein IpgD","start":1,"end":559}],"gene3D":[{"start":58,"end":181,"id":"1.20.58.450","name":"Cell division control protein 42 homolog"}]},"uniref50":"UniRef50_O30916","sequence":"MQIQSFYHSASLKTQEAFKSLQKTLYNGMQILSGQGKAPAKAPDARPEIIVLREPGATWGNYLQHQKASNHSLHNLYNLQRDLLTVAATVLGKQDPVLTSMANQMELAKVKADRPATKQEEAAAKALKKNLIELIAARTQQQDGLPAKEAHRFAAVAFRDAQVKQLNNQPWQTIKNTLTHNGHHYTNTQLPAAEMKIGAKDIFPSAYEGKGVCSWDTKNIHHANNLWMSTVSVHEDGKDKTLFCGIRHGVLSPYHEKDPLLRHVGAENKAKEVLTAALFSKPELLNKALAGEAVSLKLVSVGLLTASNIFGKEGTMVEDQMRAWQSLTQPGKMIHLKIRNKDGDLQTVKIKPDVAAFNVGVNELALKLGFGLKASDSYNAEALHQLLGNDLRPEARPGGWVGEWLAQYPDNYEVVNTLARQIKDIWKNNQHHKDGGEPYKLAQRLAMLAHEIDAVPAWNCKSGKDRTGMMDSEIKREIISLHQTHMLSAPGSLPDSGGQKIFQKVLLNSGNLEIQKQNTGGAGNKVMKNLSPEVLNLSYQKRVGDENIWQSVKGISSLITS","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"],"uniref90":"UniRef90_O30916","disprot_id":"DP01166","ncbi_taxon_id":99287,"regions_counter":7,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":148,"region_id":"DP01166r001","released":"2025_06","ec_id":"ECO:0007691","reference_html":"The structural organization of the N-terminus domain of SopB, a virulence factor of Salmonella, depends on the nature of its protein partners. <i> Roblin P, Lebrun P, Rucktooa P, Dewitte F, Lens Z, Receveur-Brechot V, Raussens V, Villeret V, Bompard C. </i> Biochim Biophys Acta, 2013","statement":[{"text":"This complex was subjected to further analysis by limited proteolysis. The chaperone SigE was resistant to digestion but SopB was quickly digested to a 40 KDa protease-resistant fragment (Fig. 1A). This resistant fragment was identified by N-terminal sequencing and mass spectroscopy. It starts at residue E149 and the last amino acid residue identified by trypsin digestion followed by mass spectroscopy was R476. This result suggests that the 150 first residues of SopB are accessible to protease and may contain the CBD of SopB and the 40 KDa C-terminal region is very stable and may correspond to the Inositol-phosphatase domain of the effector.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":1,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0849-9312","date":"2025-06-05T07:57:16.352Z","reference_source":"pmid","term_name":"disorder","reference_id":"24075929","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T13:23:20.599Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":45,"region_id":"DP01166r005","released":"2025_06","ec_id":"ECO:0006220","reference_html":"The structural organization of the N-terminus domain of SopB, a virulence factor of Salmonella, depends on the nature of its protein partners. <i> Roblin P, Lebrun P, Rucktooa P, Dewitte F, Lens Z, Receveur-Brechot V, Raussens V, Villeret V, Bompard C. </i> Biochim Biophys Acta, 2013","statement":[{"text":" The structure of the N-terminal domain of SopB (residues 29–181) in complex with Cdc42 has recently been solved [35]. Analysis of this structure shows no electronic density for residues from 29 to 45 and 171 to 181 suggesting that these fragments don't have a stable conformation in the complex.","type":"Introduction"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":29,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0003-0849-9312","date":"2025-06-05T08:03:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4DID"}],"reference_id":"24075929","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P60953"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17552","entry_name":"GDP"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T13:23:33.367Z"}}],"released":"2025_06","uniref100":"UniRef100_O30916","date":"2018-06-26T14:45:40.000Z","acc":"O30916","name":"Inositol phosphate phosphatase SopB","length":561,"organism":"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","dataset":["Bacterial virulence-related proteins"],"UniParc":"UPI00000BCCCE","genes":[{"name":{"value":"sopB"},"synonyms":[{"value":"sigD"}],"olnNames":[{"value":"STM1091"}]}],"alphafold_very_low_content":0.062388591800356503,"disorder_content":0.2638146167557932,"disprot_consensus":{"full":[{"start":1,"end":148,"type":"D"}],"Structural state":[{"start":1,"end":148,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00955","name":"HCO3- transporter integral membrane domain","start":378,"end":554},{"id":"PF00955","name":"HCO3- transporter integral membrane domain","start":565,"end":889},{"id":"PF07565","name":"Band 3 cytoplasmic domain","start":55,"end":328}],"gene3D":[{"start":51,"end":356,"id":"3.40.930.10","name":"Mannitol-specific EII; Chain A"},{"start":388,"end":430,"id":"1.10.287.570","name":"Helical hairpin bin"}]},"uniref50":"UniRef50_P02730","sequence":"MEELQDDYEDMMEENLEQEEYEDPDIPESQMEEPAAHDTEATATDYHTTSHPGTHKVYVELQELVMDEKNQELRWMEAARWVQLEENLGENGAWGRPHLSHLTFWSLLELRRVFTKGTVLLDLQETSLAGVANQLLDRFIFEDQIRPQDREELLRALLLKHSHAGELEALGGVKPAVLTRSGDPSQPLLPQHSSLETQLFCEQGDGGTEGHSPSGILEKIPPDSEATLVLVGRADFLEQPVLGFVRLQEAAELEAVELPVPIRFLFVLLGPEAPHIDYTQLGRAAATLMSERVFRIDAYMAQSRGELLHSLEGFLDCSLVLPPTDAPSEQALLSLVPVQRELLRRRYQSSPAKPDSSFYKGLDLNGGPDDPLQQTGQLFGGLVRDIRRRYPYYLSDITDAFSPQVLAAVIFIYFAALSPAITFGGLLGEKTRNQMGVSELLISTAVQGILFALLGAQPLLVVGFSGPLLVFEEAFFSFCETNGLEYIVGRVWIGFWLILLVVLVVAFEGSFLVRFISRYTQEIFSFLISLIFIYETFSKLIKIFQDHPLQKTYNYNVLMVPKPQGPLPNTALLSLVLMAGTFFFAMMLRKFKNSSYFPGKLRRVIGDFGVPISILIMVLVDFFIQDTYTQKLSVPDGFKVSNSSARGWVIHPLGLRSEFPIWMMFASALPALLVFILIFLESQITTLIVSKPERKMVKGSGFHLDLLLVVGMGGVAALFGMPWLSATTVRSVTHANALTVMGKASTPGAAAQIQEVKEQRISGLLVAVLVGLSILMEPILSRIPLAVLFGIFLYMGVTSLSGIQLFDRILLLFKPPKYHPDVPYVKRVKTWRMHLFTGIQIICLAVLWVVKSTPASLALPFVLILTVPLRRVLLPLIFRNVELQCLDADDAKATFDEEEGRDEYDEVAMPV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P02730","disprot_id":"DP01167","ncbi_taxon_id":9606,"regions_counter":1,"creator":"jmanso","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":54,"region_id":"DP01167r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3. <i> Zhang D, Kiyatkin A, Bolin JT, Low PS. </i> Blood, 2000","statement":[{"text":"Residues 1-54, 202-211, and 357-379 were not observed or were poorly defined by the electron density.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jmanso","start":1,"term_ontology":"IDPO","curator_name":"Jose A Manso","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"11049968","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P02730","date":"2018-06-26T14:45:54.000Z","acc":"P02730","name":"Band 3 anion transport protein","length":911,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000375B8","genes":[{"name":{"value":"SLC4A1"},"synonyms":[{"value":"AE1"},{"value":"DI"},{"value":"EPB3"}]}],"alphafold_very_low_content":0.10428100987925357,"disorder_content":0.059275521405049394,"disprot_consensus":{"full":[{"start":1,"end":54,"type":"D"}],"Structural state":[{"start":1,"end":54,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02540","name":"NAD synthase","start":18,"end":84}],"gene3D":[{"start":5,"end":170,"id":"3.40.50.620","name":"HUPs"}]},"uniref50":"UniRef50_F9UST4","sequence":"MATLATKKATLVAALKDLQRVTVAFSGGIDSTLVLKMALDVLGRDNVTAVVANSELFTDEEFDKAMSLAEELGANVQGTTLDYLSDDHIKNNTPDSWYYAKKMFYSRLNDIAANNGSAAVLDGMIKNDENDYRPGLKARSEAGARSLLQEADFFKTDVRALAQELGLTNWNKVASCSVSSRFPYGTTLTHDNIAQVMAAEKYLRSLGFPTVRVRFHNDIARIELPEARIGDFLVFNDRVNRQLQSLGFRYVTLDLGGFRSGRMNDTLTKAQLATFA","taxonomy":["Bacteria","Firmicutes","Bacilli","Lactobacillales","Lactobacillaceae","Lactiplantibacillus"],"uniref90":"UniRef90_F9UST4","disprot_id":"DP01168","ncbi_taxon_id":220668,"regions_counter":1,"creator":"jmanso","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":147,"region_id":"DP01168r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural insights into the catalytic mechanism of a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family, LarE. <i> Fellner M, Desguin B, Hausinger RP, Hu J. </i> Proc Natl Acad Sci U S A, 2017","statement":[{"text":"A fragment (residues 126–147, including several highly conserved residues) is severely disordered, except for in chain B of an alternative substrate-free structure (PDB ID code 5UNM), where it folds into an extended loop","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jmanso","start":126,"term_ontology":"IDPO","curator_name":"Jose A Manso","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28784764","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_F9UST4","date":"2018-06-26T14:46:10.000Z","acc":"F9UST4","name":"Pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase","length":276,"organism":"Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)","dataset":[],"UniParc":"UPI00000107E8","genes":[{"name":{"value":"larE","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16166538","url":"http://www.ncbi.nlm.nih.gov/pubmed/16166538","alternativeUrl":"https://europepmc.org/abstract/MED/16166538"}},{"code":"ECO:0000312","source":{"name":"EMBL","id":"CCC77665.1","url":"https://www.ebi.ac.uk/ena/browser/view/CCC77665.1"}}]},"olnNames":[{"value":"lp_0109","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"CCC77665.1","url":"https://www.ebi.ac.uk/ena/browser/view/CCC77665.1"}}]}]}],"alphafold_very_low_content":0,"disorder_content":0.07971014492753623,"disprot_consensus":{"full":[{"start":126,"end":147,"type":"D"}],"Structural state":[{"start":126,"end":147,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00309","name":"Sigma-54 factor, Activator interacting domain (AID)","start":5,"end":48},{"id":"PF04552","name":"Sigma-54, DNA binding domain","start":317,"end":475},{"id":"PF04963","name":"Sigma-54 factor, core binding domain","start":116,"end":303}],"gene3D":[{"start":116,"end":252,"id":"1.10.10.1330","name":"RNA polymerase sigma-54 factor, core-binding domain"},{"start":417,"end":474,"id":"1.10.10.60","name":"Homeodomain-like"}]},"uniref50":"UniRef50_P24255","sequence":"MKQGLQLRLSQQLAMTPQLQQAIRLLQLSTLELQQELQQALESNPLLEQIDTHEEIDTRETQDSETLDTADALEQKEMPEELPLDASWDTIYTAGTPSGTSGDYIDDELPVYQGETTQTLQDYLMWQVELTPFSDTDRAIATSIVDAVDETGYLTVPLEDILESIGDEEIDIDEVEAVLKRIQRFDPVGVAAKDLRDCLLIQLSQFDKTTPWLEEARLIISDHLDLLANHDFRTLMRVTRLKEDVLKEAVNLIQSLDPRPGQSIQTGEPEYVIPDVLVRKHNGHWTVELNSDSIPRLQINQHYASMCNNARNDGDSQFIRSNLQDAKWLIKSLESRNDTLLRVSRCIVEQQQAFFEQGEEYMKPMVLADIAQAVEMHESTISRVTTQKYLHSPRGIFELKYFFSSHVNTEGGGEASSTAIRALVKKLIAAENPAKPLSDSKLTSLLSEQGIMVARRTVAKYRESLSIPPSNQRKQLV","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P24255","disprot_id":"DP01169","ncbi_taxon_id":83333,"regions_counter":3,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":105,"region_id":"DP01169r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Role of the σ<sup>54</sup> Activator Interacting Domain in Bacterial Transcription Initiation. <i> Siegel AR, Wemmer DE. </i> J Mol Biol, 2016","statement":[{"text":"The σ54(106-269) peaks are well-dispersed and nearly all of them overlay with a peak in the σ54(1-269) spectrum. The extra peaks in the σ54(1-269) construct, which must correspond to the first 105 residues of E.c. σ54, are poorly dispersed and in the region of the spectrum that corresponds to unfolded residues. Other constructs of E.c. σ54 were also studied, including the full length protein (residues 1-477), the AID-linker-4 helix bundle σ54(1-186), the AID alone σ54(1-62), and a segment of the AID alone σ54(11-48). In all of these the pattern of poorly dispersed peaks associated with the AID, with 1H shifts between 8 and 9 ppm, occurs.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":1,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27732872","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P0AFB8","partner_end":null}],"ec_ontology":"ECO","end":105,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"27732872","statement":[{"text":"A segment of the AID drives complex formation with the activator ATPase domain NtrC1C in its ATP state.","type":"Results"}],"reference_html":"Role of the σ<sup>54</sup> Activator Interacting Domain in Bacterial Transcription Initiation. <i> Siegel AR, Wemmer DE. </i> J Mol Biol, 2016","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","version":4,"region_id":"DP01169r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":105,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Role of the σ<sup>54</sup> Activator Interacting Domain in Bacterial Transcription Initiation. <i> Siegel AR, Wemmer DE. </i> J Mol Biol, 2016","statement":[{"text":"We performed similar experiments with full length 15N-labeled E.coli σ54 and RNA polymerase. With excess core RNAP present most of the peaks corresponding to the AID and linker are broadened. The ~10 remaining peaks likely correspond to the N-terminal residues before the start of, and possibly including, the N-terminal helix of the AID. So the σ54 AID is an unstructured, intrinsically disordered domain in σ54 alone, with most of it becoming ordered when in complex with core polymerase.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"rpancsa","start":1,"term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"27732872","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01169r003","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_P24255","date":"2018-06-26T15:37:42.000Z","acc":"P24255","name":"RNA polymerase sigma-54 factor","length":477,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI000016F4B6","genes":[{"name":{"value":"rpoN"},"synonyms":[{"value":"glnF"},{"value":"ntrA"}],"olnNames":[{"value":"b3202"},{"value":"JW3169"}]}],"alphafold_very_low_content":0.09224318658280922,"disorder_content":0.22012578616352202,"disprot_consensus":{"full":[{"start":1,"end":105,"type":"T"}],"Structural state":[{"start":1,"end":105,"type":"D"}],"Molecular function":[{"start":1,"end":105,"type":"F"}],"Structural transition":[{"start":1,"end":105,"type":"T"}]}},{"features":{"pfam":[{"id":"PF05236","name":"Transcription initiation factor TFIID component TAF4 family","start":834,"end":1082},{"id":"PF07531","name":"NHR1 homology to TAF","start":592,"end":682}],"gene3D":[{"start":575,"end":688,"id":"1.20.120.1110","name":"TAFH/NHR1 domain"},{"start":871,"end":920,"id":"1.10.20.10","name":"Histone, subunit A"}]},"uniref50":"UniRef50_O00268","sequence":"MAAGSDLLDEVFFNSEVDEKVVSDLVGSLESQLAASAAHHHHLAPRTPEVRAAAAGALGNHVVSGSPAGAAGAGPAAPAEGAPGAAPEPPPAGRARPGGGGPQRPGPPSPRRPLVPAGPAPPAAKLRPPPEGSAGSCAPVPAAAAVAAGPEPAPAGPAKPAGPAALAARAGPGPGPGPGPGPGPGPGKPAGPGAAQTLNGSAALLNSHHAAAPAVSLVNNGPAALLPLPKPAAPGTVIQTPPFVGAAAPPAPAAPSPPAAPAPAAPAAAPPPPPPAPATLARPPGHPAGPPTAAPAVPPPAAAQNGGSAGAAPAPAPAAGGPAGVSGQPGPGAAAAAPAPGVKAESPKRVVQAAPPAAQTLAASGPASTAASMVIGPTMQGALPSPAAVPPPAPGTPTGLPKGAAGAVTQSLSRTPTATTSGIRATLTPTVLAPRLPQPPQNPTNIQNFQLPPGMVLVRSENGQLLMIPQQALAQMQAQAHAQPQTTMAPRPATPTSAPPVQISTVQAPGTPIIARQVTPTTIIKQVSQAQTTVQPSATLQRSPGVQPQLVLGGAAQTASLGTATAVQTGTPQRTVPGATTTSSAATETMENVKKCKNFLSTLIKLASSGKQSTETAANVKELVQNLLDGKIEAEDFTSRLYRELNSSPQPYLVPFLKRSLPALRQLTPDSAAFIQQSQQQPPPPTSQATTALTAVVLSSSVQRTAGKTAATVTSALQPPVLSLTQPTQVGVGKQGQPTPLVIQQPPKPGALIRPPQVTLTQTPMVALRQPHNRIMLTTPQQIQLNPLQPVPVVKPAVLPGTKALSAVSAQAAAAQKNKLKEPGGGSFRDDDDINDVASMAGVNLSEESARILATNSELVGTLTRSCKDETFLLQAPLQRRILEIGKKHGITELHPDVVSYVSHATQQRLQNLVEKISETAQQKNFSYKDDDRYEQASDVRAQLKFFEQLDQIEKQRKDEQEREILMRAAKSRSRQEDPEQLRLKQKAKEMQQQELAQMRQRDANLTALAAIGPRKKRKVDCPGPGSGAEGSGPGSVVPGSSGVGTPRQFTRQRITRVNLRDLIFCLENERETSHSLLLYKAFLK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O00268","disprot_id":"DP01170","ncbi_taxon_id":9606,"regions_counter":5,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":838,"region_id":"DP01170r001","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Interaction between intrinsically disordered regions in transcription factors Sp1 and TAF4. <i> Hibino E, Inoue R, Sugiyama M, Kuwahara J, Matsuzaki K, Hoshino M. </i> Protein Sci, 2016","statement":[{"text":" The spectrum of TAF4N/C was also represented by a large minimum at 205 nm, suggesting that the molecule was largely disordered. However, a careful observation revealed that the negative minimum in the spectrum of TAF4N/C was broader and shallower than that of Sp1‐QB.","type":"Results"},{"text":"These results suggest that some part of TAF4N/C may adopt an α‐helical conformation. Nevertheless, the spectra of both proteins indicated that most of the molecule was largely disordered, consistent with NMR observations.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":408,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-06-21T10:09:52.350Z","reference_source":"pmid","term_name":"disorder","reference_id":"27515574","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":838,"region_id":"DP01170r002","released":"2023_06","ec_id":"ECO:0006210","reference_html":"Interaction between intrinsically disordered regions in transcription factors Sp1 and TAF4. <i> Hibino E, Inoue R, Sugiyama M, Kuwahara J, Matsuzaki K, Hoshino M. </i> Protein Sci, 2016","statement":[{"text":"On the other hand, the R g value of TAF4N/C was significantly smaller than that is expected for the urea‐denatured state of protein with 431 amino acid residues (∼70 Å).32 The result is consistent with that of CD spectrum, suggesting possible formation of α‐helical structure in some part of TAF4N/C.","type":"Results"},{"text":"None of the plot for Sp1‐QA, Sp1‐QB, and TAF4N/C showed any clear peaks, suggesting that these proteins are largely disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":408,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-06-21T10:11:11.260Z","reference_source":"pmid","term_name":"disorder","reference_id":"27515574","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":838,"region_id":"DP01170r003","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Interaction between intrinsically disordered regions in transcription factors Sp1 and TAF4. <i> Hibino E, Inoue R, Sugiyama M, Kuwahara J, Matsuzaki K, Hoshino M. </i> Protein Sci, 2016","statement":[{"text":"All resonance peaks were poorly dispersed along the 1H chemical shift axis and appeared within the range of 8.5 and 7.5 ppm, indicating that the protein had neither secondary nor tertiary structures that were stabilized by regular hydrogen bonds and the rigid packing of side chains (Fig. ​(Fig.2).2). This result suggests that the central region of TAF4, which contains all the Q‐domains, is intrinsically disordered under physiological conditions.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":408,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-06-21T10:11:41.342Z","reference_source":"pmid","term_name":"disorder","reference_id":"27515574","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":349,"db":"UniProt","id":"P08047","partner_end":495}],"ec_ontology":"ECO","end":838,"term_name":"protein binding","start":408,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0001-8399-7907","curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"27515574","statement":[{"text":"We found that it was possible to classify the residues of Sp1‐QB into two groups: one independent of the concentrations of TAF4N/C and the other showing a significant decrease in intensity. The results for several representative residues are shown in Figure ​Figure3(D).3(D). These plots corresponded well among residues belonging to the same group, suggesting that the interaction between Sp1‐QB and TAF4N/C is consistent to the two‐state binding model.","type":"Results"}],"reference_html":"Interaction between intrinsically disordered regions in transcription factors Sp1 and TAF4. <i> Hibino E, Inoue R, Sugiyama M, Kuwahara J, Matsuzaki K, Hoshino M. </i> Protein Sci, 2016","date":"2023-05-31T15:24:51.075Z","term_id":"GO:0005515","ec_id":"ECO:0006165","version":5,"region_id":"DP01170r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":408,"end":838,"reference_id":"27515574","reference_source":"pmid","reference_html":"Interaction between intrinsically disordered regions in transcription factors Sp1 and TAF4. <i> Hibino E, Inoue R, Sugiyama M, Kuwahara J, Matsuzaki K, Hoshino M. </i> Protein Sci, 2016","date":"2023-05-31T15:23:54.591Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P08047","operator":null,"partner_start":349,"partner_end":495}],"region_id":"DP01170r005","statement":[{"text":"The fit converged well, and single association and dissociation rate constants were estimated to be 4.40 ± 0.08 M−1 s−1 and (3.03 ± 0.06) × 10−4 s−1, respectively. The equilibrium association constant between Sp1‐QB and TAF4N/C was estimated to be (1.45 ± 0.04) × 104 M−1 from these association and dissociation rate constants. These results suggest a significant interaction between Sp1‐QB and TAF4N/C.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_O00268","date":"2018-06-26T18:19:02.000Z","acc":"O00268","name":"Transcription initiation factor TFIID subunit 4","length":1085,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI00001367E2","genes":[{"name":{"value":"TAF4"},"synonyms":[{"value":"TAF2C"},{"value":"TAF2C1"},{"value":"TAF4A"},{"value":"TAFII130"},{"value":"TAFII135"}]}],"alphafold_very_low_content":0.6331797235023041,"disorder_content":0.3972350230414747,"disprot_consensus":{"full":[{"start":408,"end":838,"type":"D"}],"Structural state":[{"start":408,"end":838,"type":"D"}],"Molecular function":[{"start":408,"end":838,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00568","name":"WH1 domain","start":36,"end":144},{"id":"PF00786","name":"P21-Rho-binding domain","start":237,"end":294},{"id":"PF02205","name":"WH2 motif","start":427,"end":453}],"gene3D":[{"start":242,"end":321,"id":"3.90.810.10","name":"CRIB domain"},{"start":15,"end":157,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":431,"end":492,"id":"3.90.810.10","name":"CRIB domain"}]},"uniref50":"UniRef50_P42768","sequence":"MSGGPMGGRPGGRGAPAVQQNIPSTLLQDHENQRLFEMLGRKCLTLATAVVQLYLALPPGAEHWTKEHCGAVCFVKDNPQKSYFIRLYGLQAGRLLWEQELYSQLVYSTPTPFFHTFAGDDCQAGLNFADEDEAQAFRALVQEKIQKRNQRQSGDRRQLPPPPTPANEERRGGLPPLPLHPGGDQGGPPVGPLSLGLATVDIQNPDITSSRYRGLPAPGPSPADKKRSGKKKISKADIGAPSGFKHVSHVGWDPQNGFDVNNLDPDLRSLFSRAGISEAQLTDAETSKLIYDFIEDQGGLEAVRQEMRRQEPLPPPPPPSRGGNQLPRPPIVGGNKGRSGPLPPVPLGIAPPPPTPRGPPPPGRGGPPPPPPPATGRSGPLPPPPPGAGGPPMPPPPPPPPPPPSSGNGPAPPPLPPALVPAGGLAPGGGRGALLDQIRQGIQLNKTPGAPESSALQPPPQSSEGLVGALMHVMQKRSRAIHSSDEGEDQAGDEDEDDEWDD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P42768","disprot_id":"DP01171","ncbi_taxon_id":9606,"regions_counter":6,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":268,"region_id":"DP01171r001","released":"2023_12","ec_id":"ECO:0006204","reference_html":"The Cdc42/Rac interactive binding region motif of the Wiskott Aldrich syndrome protein (WASP) is necessary but not sufficient for tight binding to Cdc42 and structure formation. <i> Rudolph MG, Bayer P, Abo A, Kuhlmann J, Vetter IR, Wittinghofer A. </i> J Biol Chem, 1998","statement":[{"text":"SDS-polyacrylamide gel electrophoresis analysis of the purified fragments (Fig. 1B) and mass spectroscopy show that the WASP fragments of 4 kDa (residues 221–257), 7 kDa (201–268), and 13 kDa (201–321) molecular mass, termed W4, W7, and W13, respectively, can be isolated as soluble non-GST fusion proteins without degradation and in reasonable quantities.","type":"Results"},{"text":"It can be seen from Fig. 5D that the spectra of W4 and W7 in the <210 nm range resemble those expected for a random coil conformation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":201,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0849-9312","date":"2023-12-07T10:34:49.667Z","reference_source":"pmid","term_name":"disorder","reference_id":"9660763","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T11:40:58.875Z"}},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P60953","partner_end":null}],"ec_ontology":"ECO","end":268,"term_name":"protein binding","start":201,"ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"9660763","statement":[{"text":"The CRIB/GBD motif of WASP mediated binding to Cdc42.","type":"Curator statement"}],"reference_html":"The Cdc42/Rac interactive binding region motif of the Wiskott Aldrich syndrome protein (WASP) is necessary but not sufficient for tight binding to Cdc42 and structure formation. <i> Rudolph MG, Bayer P, Abo A, Kuhlmann J, Vetter IR, Wittinghofer A. </i> J Biol Chem, 1998","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","version":4,"region_id":"DP01171r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-27T15:32:35.917Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":268,"term_name":"disorder to order","released":"2022_06","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"The Cdc42/Rac interactive binding region motif of the Wiskott Aldrich syndrome protein (WASP) is necessary but not sufficient for tight binding to Cdc42 and structure formation. <i> Rudolph MG, Bayer P, Abo A, Kuhlmann J, Vetter IR, Wittinghofer A. </i> J Biol Chem, 1998","statement":[{"text":"The binding of Cdc42 induces a structural rearrangement of residues in the GBD/CRIB motif, or alternatively, the Wiskott Aldrich syndrome protein fragments have an ensemble of conformations, one of which is stabilized by Cdc42 binding.","type":"Abstract"}],"term_id":"IDPO:0000011","curator_id":"vnugnes","start":201,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"9660763","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-15T18:14:22.026Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01171r003","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P60953"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T16:11:42.603Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":268,"region_id":"DP01171r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The Cdc42/Rac interactive binding region motif of the Wiskott Aldrich syndrome protein (WASP) is necessary but not sufficient for tight binding to Cdc42 and structure formation. <i> Rudolph MG, Bayer P, Abo A, Kuhlmann J, Vetter IR, Wittinghofer A. </i> J Biol Chem, 1998","statement":[{"text":"Short and medium range NOEs were analyzed to characterize the secondary structure of W7. Surprisingly, considering the tight binding of W7 to Cdc42, amino acid regions in the N-terminal part of W7 including the GBD/CRIB motif itself do not show any obvious secondary structure. Only the region from Trp-252 to Asp-264 shows NOEs typical of an α-helical conformation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":201,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"9660763","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T16:11:24.083Z"}}],"released":"2018_11","uniref100":"UniRef100_P42768","date":"2018-06-26T18:41:58.000Z","acc":"P42768","name":"Wiskott-Aldrich syndrome protein","length":502,"organism":"Homo sapiens","dataset":["Cancer-related proteins","Condensates-related proteins"],"UniParc":"UPI000003CA0A","genes":[{"name":{"value":"WAS"},"synonyms":[{"value":"IMD2"}]}],"alphafold_very_low_content":0.26095617529880477,"disorder_content":0.13545816733067728,"disprot_consensus":{"full":[{"start":201,"end":268,"type":"T"}],"Structural state":[{"start":201,"end":268,"type":"D"}],"Molecular function":[{"start":201,"end":268,"type":"F"}],"Structural transition":[{"start":201,"end":268,"type":"T"}]}},{"features":{"pfam":[{"id":"PF02205","name":"WH2 motif","start":30,"end":56}],"gene3D":[{"start":461,"end":494,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"}]},"uniref50":"UniRef50_O43516","sequence":"MPVPPPPAPPPPPTFALANTEKPTLNKTEQAGRNALLSDISKGKKLKKTVTNDRSAPILDKPKGAGAGGGGGGFGGGGGFGGGGGGGGGGSFGGGGPPGLGGLFQAGMPKLRSTANRDNDSGGSRPPLLPPGGRSTSAKPFSPPSGPGRFPVPSPGHRSGPPEPQRNRMPPPRPDVGSKPDSIPPPVPSTPRPIQSSPHNRGSPPVPGGPRQPSPGPTPPPFPGNRGTALGGGSIRQSPLSSSSPFSNRPPLPPTPSRALDDKPPPPPPPVGNRPSIHREAVPPPPPQNNKPPVPSTPRPSASSQAPPPPPPPSRPGPPPLPPSSSGNDETPRLPQRNLSLSSSTPPLPSPGRSGPLPPPPSERPPPPVRDPPGRSGPLPPPPPVSRNGSTSRALPATPQLPSRSGVDSPRSGPRPPLPPDRPSAGAPPPPPPSTSIRNGFQDSPCEDEWESRFYFHPISDLPPPEPYVQTTKSYPSKLARNESRSGSNRRERGAPPLPPIPR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O43516","disprot_id":"DP01172","ncbi_taxon_id":9606,"regions_counter":12,"creator":"zkalman","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":101,"region_id":"DP01172r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"New insights into the role of the disordered WIP N-terminal domain revealed by NMR structural characterization. <i> Elazari-Shalom H, Shaked H, Esteban-Martin S, Salvatella X, Barda-Saad M, Chill JH. </i> FEBS J, 2015","statement":[{"text":"The CD curve of WIP-N (res2-101) exhibits a minimum at 195 nm and a weak shoulder at 220 nm, characteristic features of an unstructured protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":2,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"25495558","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":101,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"New insights into the role of the disordered WIP N-terminal domain revealed by NMR structural characterization. <i> Elazari-Shalom H, Shaked H, Esteban-Martin S, Salvatella X, Barda-Saad M, Chill JH. </i> FEBS J, 2015","statement":[{"text":"WIP interacts with actin through its N‐terminal domain that contains two canonical actin binding motifs (ABMs).","type":"Introduction"}],"term_id":"GO:0005515","curator_id":"rpancsa","start":2,"term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"25495558","version":3,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01172r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":101,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"New insights into the role of the disordered WIP N-terminal domain revealed by NMR structural characterization. <i> Elazari-Shalom H, Shaked H, Esteban-Martin S, Salvatella X, Barda-Saad M, Chill JH. </i> FEBS J, 2015","statement":[{"text":"For the ABM the disordered to folded transition involves a gain of stabilizing interactions with actin at the price of a decrease in its entropy; by partially mirroring the future bound state the ABM can limit this entropic loss and increase its binding affinity.","type":"Discussion"}],"term_id":"IDPO:0000011","curator_id":"rpancsa","start":2,"term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"25495558","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01172r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":65,"region_id":"DP01172r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A J-modulated protonless NMR experiment characterizes the conformational ensemble of the intrinsically disordered protein WIP. <i> Rozentur-Shkop E, Goobes G, Chill JH. </i> J Biomol NMR, 2016","statement":[{"text":"One- and two-bond J(15N,13Cα) couplings were acquired for WIP residues 2-65 at various temperatures, and in denaturing and crowding environments. Under native conditions fitted J-couplings identified in the WIP conformational ensemble a propensity for extended conformation at residues 16-23 and 45-60, and a helical tendency at residues 28-42. These findings are consistent with a previous study of the based upon chemical shift and RDC data and confirm that the WIP2-65 conformational ensemble is biased towards the structure assumed by this fragment in its actin-bound form.","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":2,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27844185","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":101,"region_id":"DP01172r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"New insights into the role of the disordered WIP N-terminal domain revealed by NMR structural characterization. <i> Elazari-Shalom H, Shaked H, Esteban-Martin S, Salvatella X, Barda-Saad M, Chill JH. </i> FEBS J, 2015","statement":[{"text":"The comparison between the 2D 1H‐15N heteronuclear single quantum coherence (HSQC) spectrum and the 2D in‐phase anti‐phase (IPAP) 13C‐15N (CON) spectrum of WIP-N further corroborates our identification of WIP-N as a disordered domain. The CON spectrum displays significantly advantageous spectral dispersion which is characteristic of disordered proteins. As expected, secondary chemical shifts in WIP-N are generally small, in the ±0.5 p.p.m. range. However, they are revealing in that they identify structural tendencies in the disordered state of WIP-N or regions for which the multi‐conformational average differs from random coil. In both prediction methods residues 30–42 exhibit a helical propensity, and residues 45–62 demonstrate a β‐strand propensity. Furthermore, a third region with β‐strand structural propensity, albeit lower than that of residues 45–62, is clearly revealed for residues 17–25. The ensemble‐based analysis of RDCs confirms our previous results, finding that in WIPN the multi‐conformational average for the N‐terminal ABM exhibits the characteristic helix‐β‐strand motif, and that it is preceded by an additional segment with β‐strand structural propensity. In addition, it shows that the ABM does not exhibit tertiary structure or even partial long‐range order and should be considered as an array of independent structural elements.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":2,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"25495558","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":503,"region_id":"DP01172r006","released":"2022_03","ec_id":"ECO:0006196","reference_html":"NMR determines transient structure and dynamics in the disordered C-terminal domain of WASp interacting protein. <i> Haba NY, Gross R, Novacek J, Shaked H, Zidek L, Barda-Saad M, Chill JH. </i> Biophys J, 2013","statement":[{"text":"Regions that were most protected from solvent exchange, exhibiting negligible recovery after 20 ms, included residues 440–468, spanning the rigid VCR domain, and residues 475–479, both consistent with structural elements delineated by chemical-shift data. Low protection factors identified increased flexibility in two regions of WIPC, residues 470–474 and 481–490, which exhibited recovery rates of 5–10% and 10–25%, respectively.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":407,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23870269","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":503,"region_id":"DP01172r007","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR determines transient structure and dynamics in the disordered C-terminal domain of WASp interacting protein. <i> Haba NY, Gross R, Novacek J, Shaked H, Zidek L, Barda-Saad M, Chill JH. </i> Biophys J, 2013","statement":[{"text":"The transiently structured regions are connected by unstructured linker segments, as could be deduced from minimal secondary structure, low transverse relaxation and hetNOE rates, minimal IRCS values, and exposure to solvent exchange.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":407,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23870269","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P42768","partner_end":null}],"ec_ontology":"ECO","end":503,"term_name":"protein binding","start":407,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"23870269","statement":[{"text":"WASp-interacting protein (WIP) acts as the cellular chaperone of WASp, conveys WASp to areas of active actin assembly after antigen-receptor and chemokine receptor signaling (3,4), and stabilizes WASp by shielding it from cellular degradation systems. The C-terminal segment of WIP contains the verprolin conserved region (VCR; residues 444–478) that is capable of binding the N-terminal EVH1 domain of WASp.","type":"Introduction"}],"reference_html":"NMR determines transient structure and dynamics in the disordered C-terminal domain of WASp interacting protein. <i> Haba NY, Gross R, Novacek J, Shaked H, Zidek L, Barda-Saad M, Chill JH. </i> Biophys J, 2013","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","version":4,"region_id":"DP01172r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":503,"term_name":"protein folding chaperone","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"NMR determines transient structure and dynamics in the disordered C-terminal domain of WASp interacting protein. <i> Haba NY, Gross R, Novacek J, Shaked H, Zidek L, Barda-Saad M, Chill JH. </i> Biophys J, 2013","statement":[{"text":"WASp-interacting protein (WIP) acts as the cellular chaperone of WASp, conveys WASp to areas of active actin assembly after antigen-receptor and chemokine receptor signaling (3,4), and stabilizes WASp by shielding it from cellular degradation systems. The C-terminal segment of WIP is capable of binding  and chaperoning the N-terminal EVH1 domain of WASp.","type":"Introduction"}],"term_id":"GO:0044183","curator_id":"rpancsa","start":407,"term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"23870269","version":3,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01172r009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":503,"term_name":"phosphorylation display site","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"NMR determines transient structure and dynamics in the disordered C-terminal domain of WASp interacting protein. <i> Haba NY, Gross R, Novacek J, Shaked H, Zidek L, Barda-Saad M, Chill JH. </i> Biophys J, 2013","statement":[{"text":"One such region of interest is the phosphorylation site of residues 484–492, whose flexibility is consistent with its need to be sufficiently exposed to allow access to the phosphorylating enzyme PKCθ.","type":"Discussion"}],"term_id":"IDPO:0000045","curator_id":"rpancsa","start":407,"term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"23870269","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01172r010","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":503,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"NMR determines transient structure and dynamics in the disordered C-terminal domain of WASp interacting protein. <i> Haba NY, Gross R, Novacek J, Shaked H, Zidek L, Barda-Saad M, Chill JH. </i> Biophys J, 2013","statement":[{"text":"Thus, contributing to the formation of the WIP/WASp complex are preformed motifs at residues 462–465 and 474–478, and a third motif (residues 457–461) whose structure is formed only in the presence of WASp.","type":"Discussion"}],"term_id":"IDPO:0000011","curator_id":"rpancsa","start":407,"term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"23870269","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01172r011","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_O43516","date":"2018-06-26T19:40:44.000Z","acc":"O43516","name":"WAS/WASL-interacting protein family member 1","length":503,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000138EAA","genes":[{"name":{"value":"WIPF1"},"synonyms":[{"value":"WASPIP"},{"value":"WIP"}]}],"alphafold_very_low_content":0.44532803180914515,"disorder_content":0.39165009940357853,"disprot_consensus":{"full":[{"start":2,"end":101,"type":"T"},{"start":407,"end":503,"type":"T"}],"Structural state":[{"start":2,"end":101,"type":"D"},{"start":407,"end":503,"type":"D"}],"Molecular function":[{"start":2,"end":101,"type":"F"},{"start":407,"end":503,"type":"F"}],"Structural transition":[{"start":2,"end":101,"type":"T"},{"start":407,"end":503,"type":"T"}],"Disorder function":[{"start":407,"end":503,"type":"F"}]}},{"features":{"pfam":[{"id":"PF15152","name":"Kisspeptin","start":48,"end":122}]},"uniref50":"UniRef50_Q15726","sequence":"MNSLVSWQLLLFLCATHFGEPLEKVASVGNSRPTGQQLESLGLLAPGEQSLPCTERKPAATARLSRRGTSLSPPPESSGSPQQPGLSAPHSRQIPAPQGAVLVQREKDLPNYNWNSFGLRFGKREAAPGNHGRSAGRG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q15726","disprot_id":"DP01173","ncbi_taxon_id":9606,"regions_counter":9,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":138,"region_id":"DP01173r001","released":"2022_03","ec_id":"ECO:0007680","reference_html":"The metastasis suppressor KISS1 is an intrinsically disordered protein slightly more extended than a random coil. <i> Ibáñez de Opakua A, Merino N, Villate M, Cordeiro TN, Ormaza G, Sánchez-Carbayo M, Diercks T, Bernadó P, Blanco FJ. </i> PLoS One, 2017","statement":[{"text":"The protein eluted from the SEC column at a volume corresponding to an apparent molar mass of 28 kDa. The mass derived from MALS data is 11.7 kDa, however, demonstrating that Kiss1 is monomeric. These inconsistent results indicate that Kiss1 is either folded with an elongated shape, or flexible and disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":20,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"chromatography evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28207895","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":138,"region_id":"DP01173r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The metastasis suppressor KISS1 is an intrinsically disordered protein slightly more extended than a random coil. <i> Ibáñez de Opakua A, Merino N, Villate M, Cordeiro TN, Ormaza G, Sánchez-Carbayo M, Diercks T, Bernadó P, Blanco FJ. </i> PLoS One, 2017","statement":[{"text":"The low dispersion of the backbone 1HN chemical shifts observed in the HSQC spectrum indicates that KISS1 is largely disordered and flexible under native conditions. Analysis of chemical shift deviations and 15N T2 relaxation times does not provide clear evidence for any conformational preference, suggesting that KISS1 behaves as a random coil polypeptide.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":20,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28207895","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":138,"term_name":"limited proteolysis display site","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The metastasis suppressor KISS1 is an intrinsically disordered protein slightly more extended than a random coil. <i> Ibáñez de Opakua A, Merino N, Villate M, Cordeiro TN, Ormaza G, Sánchez-Carbayo M, Diercks T, Bernadó P, Blanco FJ. </i> PLoS One, 2017","statement":[{"text":"After secretion KISS is processed by the furin endoprotease. This enzyme recognizes dibasic cleavage sites on the amino acid sequence and, after the action of carboxypeptidases and peptidyl-glycine-α-amidating monooxygenase (PAM), generates a fragment of 54 residues known as Kisspeptin54 (KISS1 residues 68–121). Kisspeptin54 can be further cleaved into smaller 14, 13 and 10 residue fragments, or kisspeptins, which are ligands of the seven-transmembrane helix G protein-coupled receptor GPR54, also named KISS1R.","type":"Introduction"}],"term_id":"IDPO:0000048","curator_id":"rpancsa","start":20,"term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"28207895","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01173r003","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":138,"term_name":"phosphorylation display site","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The metastasis suppressor KISS1 is an intrinsically disordered protein slightly more extended than a random coil. <i> Ibáñez de Opakua A, Merino N, Villate M, Cordeiro TN, Ormaza G, Sánchez-Carbayo M, Diercks T, Bernadó P, Blanco FJ. </i> PLoS One, 2017","statement":[{"text":"Phosphorylated at residue Y110.","type":"Discussion"}],"term_id":"IDPO:0000045","curator_id":"rpancsa","start":20,"term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"28207895","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01173r004","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":138,"term_name":"molecular recognition display site","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The metastasis suppressor KISS1 is an intrinsically disordered protein slightly more extended than a random coil. <i> Ibáñez de Opakua A, Merino N, Villate M, Cordeiro TN, Ormaza G, Sánchez-Carbayo M, Diercks T, Bernadó P, Blanco FJ. </i> PLoS One, 2017","statement":[{"text":"C-terminal amidation by peptidyl-glycine-α-amidating monooxygenase.","type":"Discussion"}],"term_id":"IDPO:0000037","curator_id":"rpancsa","start":20,"term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"28207895","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01173r005","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q969F8","partner_end":null}],"ec_ontology":"ECO","end":138,"term_name":"protein binding","start":20,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"28207895","statement":[{"text":"KISS1 and its fragments interact with KISS1R, their GPCR receptor.","type":"Discussion"}],"reference_html":"The metastasis suppressor KISS1 is an intrinsically disordered protein slightly more extended than a random coil. <i> Ibáñez de Opakua A, Merino N, Villate M, Cordeiro TN, Ormaza G, Sánchez-Carbayo M, Diercks T, Bernadó P, Blanco FJ. </i> PLoS One, 2017","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","version":4,"region_id":"DP01173r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":138,"region_id":"DP01173r007","released":"2022_03","ec_id":"ECO:0006317","reference_html":"The metastasis suppressor KISS1 is an intrinsically disordered protein slightly more extended than a random coil. <i> Ibáñez de Opakua A, Merino N, Villate M, Cordeiro TN, Ormaza G, Sánchez-Carbayo M, Diercks T, Bernadó P, Blanco FJ. </i> PLoS One, 2017","statement":[{"text":"The thermal denaturation curve of Kiss1 followed by the changes in the CD signal at 222 nm does not show any cooperative folding-unfolding transition, indicating that KISS1 lacks a defined tertiary structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":20,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28207895","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":138,"region_id":"DP01173r008","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The metastasis suppressor KISS1 is an intrinsically disordered protein slightly more extended than a random coil. <i> Ibáñez de Opakua A, Merino N, Villate M, Cordeiro TN, Ormaza G, Sánchez-Carbayo M, Diercks T, Bernadó P, Blanco FJ. </i> PLoS One, 2017","statement":[{"text":"The far-UV CD spectrum of Kiss1 shows a minimum at 198 nm and a shoulder at 226 nm, consistent with a predominantly random-coil protein with little secondary structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":20,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28207895","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":138,"region_id":"DP01173r009","released":"2022_03","ec_id":"ECO:0006210","reference_html":"The metastasis suppressor KISS1 is an intrinsically disordered protein slightly more extended than a random coil. <i> Ibáñez de Opakua A, Merino N, Villate M, Cordeiro TN, Ormaza G, Sánchez-Carbayo M, Diercks T, Bernadó P, Blanco FJ. </i> PLoS One, 2017","statement":[{"text":"The Kratky representation is typical for a disordered protein, with a monotonic increase of I(s)s2 with the momentum transfer s. An analysis of the smallest angle data by Guinier’s approach for a momentum transfer range s·Rg < 1.3 (where Rg is the radius of gyration) indicates that KISS1 has an average radius of gyration of 34.7 ± 0.5 Å. This value is slightly larger than expected for an IDP of 120 residues (RgRC = 30.1 Å), suggesting that KISS1 could transiently adopt more extended structures.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":20,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28207895","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q15726","date":"2018-06-26T20:43:18.000Z","acc":"Q15726","name":"Metastasis-suppressor KiSS-1","length":138,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012DE77","genes":[{"name":{"value":"KISS1"},"orfNames":[{"value":"PP5098"}]}],"alphafold_very_low_content":0.39855072463768115,"disorder_content":0.8623188405797102,"disprot_consensus":{"full":[{"start":20,"end":138,"type":"D"}],"Structural state":[{"start":20,"end":138,"type":"D"}],"Disorder function":[{"start":20,"end":138,"type":"F"}],"Molecular function":[{"start":20,"end":138,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00096","name":"Zinc finger, C2H2 type","start":430,"end":454},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":460,"end":484},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":490,"end":512}],"gene3D":[{"start":455,"end":486,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":487,"end":513,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":431,"end":454,"id":"3.30.160.60","name":"Classic Zinc Finger"}]},"uniref50":"UniRef50_Q60793","sequence":"MRQPPGESDMAVSDALLPSFSTFASGPAGREKTLRQAGAPNNRWREELSHMKRLPPVLPGRPYDLAAATVATDLESGGAGAACGGSNLAPLPRRETEEFNDLLDLDFILSNSLTHPPESVAATVSSSASASSSSSPSSSGPASAPSTCSFTYPIRAGNDPGVAPGGTGGGLLYGRESAPPPTAPFNLADINDVSPSGGFVAELLRPELDPVYIPPQQPQPPGGGLMGKFVLKASLSAPGSEYGSPSVISVSKGSPDGSHPVVVAPYNGGPPRTCPKIKQEAVSSCTHLGAGPPLSNGHRPAAHDFPLGRQLPSRTTPTLGLEEVLSSRDCHPALPLPPGFHPHPGPNYPSFLPDQMQPQVPPLHYQGQSRGFVARAGEPCVCWPHFGTHGMMLTPPSSPLELMPPGSCMPEEPKPKRGRRSWPRKRTATHTCDYAGCGKTYTKSSHLKAHLRTHTGEKPYHCDWDGCGWKFARSDELTRHYRKHTGHRPFQCQKCDRAFSRSDHLALHMKRHF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O43474","disprot_id":"DP01174","ncbi_taxon_id":9606,"regions_counter":3,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":130,"region_id":"DP01174r001","released":"2022_06","ec_id":"ECO:0006165","reference_html":"Backbone <sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N NMR resonance assignments of the Krüppel-like factor 4 activation domain. <i> Conroy BS, Weiss ER, Smith SP, Langelaan DN. </i> Biomol NMR Assign, 2017","statement":[{"text":"The narrow chemical shift dispersion in the 1H dimension of the 1H-15N HSQC spectrum, suggests that the KLF41–130 fragment is intrinsically disordered. Analysis using the secondary structure propensity (SSP) algorithm (Marsh et al. 2006) indicates that most of KLF41–130 is disordered, however there are two continuous regions with >20% helical propensity spanning residues Asn42-Met51 and Asp104-His115 (Fig. 2). ","type":"Article"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":1,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0849-9312","date":"2022-06-23T10:57:15.136Z","reference_source":"pmid","term_name":"disorder","reference_id":"28247282","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"BMRB","id":"26953"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-23T13:57:54.914Z"}}],"released":"2018_11","uniref100":"UniRef100_O43474","date":"2018-06-26T21:12:32.000Z","acc":"O43474","name":"Krueppel-like factor 4","length":513,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI000014D66E","genes":[{"name":{"value":"KLF4","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6348","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6348"}}]},"synonyms":[{"value":"EZF"},{"value":"GKLF"}]}],"alphafold_very_low_content":0.7192982456140351,"disorder_content":0.253411306042885,"disprot_consensus":{"full":[{"start":1,"end":130,"type":"D"}],"Structural state":[{"start":1,"end":130,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00029","name":"Connexin","start":3,"end":233}],"gene3D":[{"start":2,"end":244,"id":"1.20.1440.80","name":"Gap junction channel protein cysteine-rich domain"}]},"uniref50":"UniRef50_Q03190","sequence":"MGDWGFLEKLLDQVQEHSTVVGKIWLTVLFIFRILILGLAGESVWGDEQSDFECNTAQPGCTNVCYDQAFPISHIRYWVLQFLFVSTPTLIYLGHVIYLSRREERLRQKEGELRALPSKDLHVERALAAIEHQMAKISVAEDGRLRIRGALMGTYVVSVLCKSVLEAGFLYGQWRLYGWTMEPVFVCQRAPCPHIVDCYVSRPTEKTIFIIFMLVVGVISLVLNLLELVHLLCRCVSREIKARRDHDARPAQGSASDPYPEQVFFYLPMGEGPSSPPCPTYNGLSSTEQNWANLTTEERLTSSRPPPFVNTAPQGGRKSPSRPNSSASKKQYV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q03190","disprot_id":"DP01175","ncbi_taxon_id":10090,"regions_counter":4,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":333,"region_id":"DP01175r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Chemical shift assignments of the connexin37 carboxyl terminal domain. <i> Li H, Spagnol G, Pontifex TK, Burt JM, Sorgen PL. </i> Biomol NMR Assign, 2017","statement":[{"text":"Chemical shift index predictions of secondary structure and the lack of medium- and long-range NOE connectivities observed in the 1H–15N NOESY-HSQC and 1H-13C-NOESY spectra are consistent with the prediction of an intrinsically disordered structure for the Cx37CT.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":233,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28251507","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":333,"term_name":"molecular recognition display site","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Chemical shift assignments of the connexin37 carboxyl terminal domain. <i> Li H, Spagnol G, Pontifex TK, Burt JM, Sorgen PL. </i> Biomol NMR Assign, 2017","statement":[{"text":"The CT plays a role in the trafficking, localization, and turnover of gap junction channels, as well as the level of gap junction intercellular communication via numerous post-translational modifications and protein-protein interactions.","type":"Introduction"}],"term_id":"IDPO:0000037","curator_id":"rpancsa","start":233,"term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"28251507","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01175r002","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":333,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Chemical shift assignments of the connexin37 carboxyl terminal domain. <i> Li H, Spagnol G, Pontifex TK, Burt JM, Sorgen PL. </i> Biomol NMR Assign, 2017","statement":[{"text":"The CT plays a role in the trafficking, localization, and turnover of gap junction channels, as well as the level of gap junction intercellular communication via numerous post-translational modifications and protein-protein interactions.","type":"Introduction"}],"term_id":"GO:0005515","curator_id":"rpancsa","start":233,"term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"28251507","version":3,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01175r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P28235","date":"2018-06-26T21:27:19.000Z","acc":"P28235","name":"Gap junction alpha-4 protein","length":333,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000264A8","genes":[{"name":{"value":"Gja4"},"synonyms":[{"value":"Cxn-37"}]}],"alphafold_very_low_content":0.19519519519519518,"disorder_content":0.3033033033033033,"disprot_consensus":{"full":[{"start":233,"end":333,"type":"D"}],"Structural state":[{"start":233,"end":333,"type":"D"}],"Disorder function":[{"start":233,"end":333,"type":"F"}],"Molecular function":[{"start":233,"end":333,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00029","name":"Connexin","start":2,"end":213}],"gene3D":[{"start":1,"end":225,"id":"1.20.1440.80","name":"Gap junction channel protein cysteine-rich domain"}]},"uniref50":"UniRef50_P08034","sequence":"MNWTGLYTLLSGVNRHSTAIGRVWLSVIFIFRIMVLVVAAESVWGDEKSSFICNTLQPGCNSVCYDHFFPISHVRLWSLQLILVSTPALLVAMHVAHQQHIEKKMLRLEGHGDPLHLEEVKRHKVHISGTLWWTYVISVVFRLLFEAVFMYVFYLLYPGYAMVRLVKCEAFPCPNTVDCFVSRPTEKTVFTVFMLAASGICIILNVAEVVYLIIRACARRAQRRSNPPSRKGSGFGHRLSPEYKQNEINKLLSEQDGSLKDILRRSPGTGAGLAEKSDRCSAC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_P08034","disprot_id":"DP01176","ncbi_taxon_id":10116,"regions_counter":4,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":283,"region_id":"DP01176r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Characterization of the structure and intermolecular interactions between the connexin 32 carboxyl-terminal domain and the protein partners synapse-associated protein 97 and calmodulin. <i> Stauch K, Kieken F, Sorgen P. </i> J Biol Chem, 2012","statement":[{"text":"Analysis of the 15N-NOESY spectra did not produce NOEs consistent with any secondary structure. The intrinsically disordered structure for the soluble Cx32CT domain as determined by CD is consistent with the narrow 1H chemical shift dispersions (<1 ppm) observed in the 15N-HSQC.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":217,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22718765","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T22:28:44.065Z"}},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q62696","partner_end":null},{"partner_start":null,"db":"UniProt","id":"P0DP29","partner_end":null}],"ec_ontology":"ECO","end":283,"term_name":"protein binding","start":217,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"22718765","statement":[{"text":"Cx32CT domain interacts with the protein partners synapse-associated protein 97 (SAP97) and calmodulin (CaM).","type":"Abstract"}],"reference_html":"Characterization of the structure and intermolecular interactions between the connexin 32 carboxyl-terminal domain and the protein partners synapse-associated protein 97 and calmodulin. <i> Stauch K, Kieken F, Sorgen P. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","version":4,"region_id":"DP01176r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":283,"region_id":"DP01176r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Characterization of the structure and intermolecular interactions between the connexin 32 carboxyl-terminal domain and the protein partners synapse-associated protein 97 and calmodulin. <i> Stauch K, Kieken F, Sorgen P. </i> J Biol Chem, 2012","statement":[{"text":"The soluble Cx32CT showed a peak minimum near 198 nm and little ellipticity at 222 nm, characteristic of a flexible, intrinsically disordered protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":217,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22718765","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T22:28:34.329Z"}},{"start":217,"end":283,"reference_id":"22718765","reference_source":"pmid","reference_html":"Characterization of the structure and intermolecular interactions between the connexin 32 carboxyl-terminal domain and the protein partners synapse-associated protein 97 and calmodulin. <i> Stauch K, Kieken F, Sorgen P. </i> J Biol Chem, 2012","date":"2025-04-25T21:55:50.846Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP01176r004","statement":[{"text":"Analysis of the 15N-NOESY spectra did not produce NOEs consistent with any secondary structure. The intrinsically disordered structure for the soluble Cx32CT domain as determined by CD is consistent with the narrow 1H chemical shift dispersions (<1 ppm) observed in the 15N-HSQC.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T22:28:47.266Z"}}],"released":"2018_11","uniref100":"UniRef100_P28230","date":"2018-06-26T21:34:55.000Z","acc":"P08033","name":"Gap junction beta-1 protein","length":283,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI000000094F","genes":[{"name":{"value":"Gjb1"},"synonyms":[{"value":"Cxn-32"}]}],"alphafold_very_low_content":0.10247349823321555,"disorder_content":0.23674911660777384,"disprot_consensus":{"full":[{"start":217,"end":283,"type":"D"}],"Structural state":[{"start":217,"end":283,"type":"D"}],"Molecular function":[{"start":217,"end":283,"type":"F"}],"Disorder function":[{"start":217,"end":283,"type":"F"}]}},{"features":{"pfam":[{"id":"PF10614","name":"Type VIII secretion system (T8SS), CsgF protein","start":5,"end":129}]},"uniref50":"UniRef50_P0AEA4","sequence":"MRVKHAVVLLMLISPLSWAGTMTFQFRNPNFGGNPNNGAFLLNSAQAQNSYKDPSYNDDFGIETPSALDNFTQAIQSQILGGLLSNINTGKPGRMVTNDYIVDIANRDGQLQLNVTDRKTGQTSTIQVSGLQNNSTDF","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0AEA4","disprot_id":"DP01177","ncbi_taxon_id":83333,"regions_counter":1,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":49,"region_id":"DP01177r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural and functional characterization of the Curli adaptor protein CsgF. <i> Schubeis T, Spehr J, Viereck J, Köpping L, Nagaraj M, Ahmed M, Ritter C. </i> FEBS Lett, 2018","statement":[{"text":"The backbone and sidechain resonances were assigned using three-dimensional NMR spectra of the monomer, following standard procedures. Solely, the prolines, the C-terminal His6-tag and three residues at the N terminus remained unassigned. Eventually, 79% of protons and more than 69% of heteroatoms could be assigned. The structure was calculated with a total number of 1027 NOE restraints out of which 12% could be assigned to long range distance restraints. The structure of CsgF consists of three independent elements: An N-terminal unstructured region, a 21-residue a-Helix and a C-terminal antiparallel b-sheet made of four strands. Almost all long range restraints were found to define the b-sheet. The bundle of the lowest energy structures demonstrates that no unique arrangement between the three regions could be determined due to the absence of interdomain NOE restraints.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":19,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"29427517","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"34052"},{"db":"PDB","id":"5m1u"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P0AEA4","date":"2018-06-27T09:08:04.000Z","acc":"P0AE98","name":"Curli production assembly/transport component CsgF","length":138,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI0000128532","genes":[{"name":{"value":"csgF"},"olnNames":[{"value":"b1038"},{"value":"JW1021"}]}],"alphafold_very_low_content":0.057971014492753624,"disorder_content":0.2246376811594203,"disprot_consensus":{"full":[{"start":19,"end":49,"type":"D"}],"Structural state":[{"start":19,"end":49,"type":"D"}]}},{"features":{"pfam":[{"id":"PF05022","name":"SRP40, C-terminal domain","start":624,"end":696}]},"uniref50":"UniRef50_Q14978","sequence":"MADAGIRRVVPSDLYPLVLGFLRDNQLSEVANKFAKATGATQQDANASSLLDIYSFWLKSAKVPERKLQANGPVAKKAKKKASSSDSEDSSEEEEEVQGPPAKKAAVPAKRVGLPPGKAAAKASESSSSEESSDDDDEEDQKKQPVQKGVKPQAKAAKAPPKKAKSSDSDSDSSSEDEPPKNQKPKITPVTVKAQTKAPPKPARAAPKIANGKAASSSSSSSSSSSSDDSEEEKAAATPKKTVPKKQVVAKAPVKAATTPTRKSSSSEDSSSDEEEEQKKPMKNKPGPYSSVPPPSAPPPKKSLGTQPPKKAVEKQQPVESSEDSSDESDSSSEEEKKPPTKAVVSKATTKPPPAKKAAESSSDSSDSDSSEDDEAPSKPAGTTKNSSNKPAVTTKSPAVKPAAAPKQPVGGGQKLLTRKADSSSSEEESSSSEEEKTKKMVATTKPKATAKAALSLPAKQAPQGSRDSSSDSDSSSSEEEEEKTSKSAVKKKPQKVAGGAAPSKPASAKKGKAESSNSSSSDDSSEEEEEKLKGKGSPRPQAPKANGTSALTAQNGKAAKNSEEEEEEKKKAAVVVSKSGSLKKRKQNEAAKEAETPQAKKIKLQTPNTFPKRKKGEKRASSPFRRVREEEIEVDSRVADNSFDAKRGAAGDWGERANQVLKFTKGKSFRHEKTKKKRGSYRGGSISVQVNSIKFDSE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q14978","disprot_id":"DP01178","ncbi_taxon_id":9606,"regions_counter":7,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":699,"region_id":"DP01178r001","released":"2022_03","ec_id":"ECO:0006317","reference_html":"Structural disorder and local order of hNopp140. <i> Tantos A, Szrnka K, Szabo B, Bokor M, Kamasa P, Matus P, Bekesi A, Tompa K, Han KH, Tompa P. </i> Biochim Biophys Acta, 2013","statement":[{"text":"Thermal stability is a key feature of mostly disordered proteins. Due to their specific amino acid composition and their inherent lack of structure, no aggregation occurs at high temperatures. According to our expectations, the level of intact hNopp140 has not changed after 10 min of boiling, while the globular control BSA aggregated and\nprecipitated.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":1,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"22906532","version":2,"ec_name":"temperature-induced protein unfolding evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":699,"region_id":"DP01178r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structural disorder and local order of hNopp140. <i> Tantos A, Szrnka K, Szabo B, Bokor M, Kamasa P, Matus P, Bekesi A, Tompa K, Han KH, Tompa P. </i> Biochim Biophys Acta, 2013","statement":[{"text":"The spectrum of hNopp140 has a characteristic peak with a minimum at 203 nm tending to disappear at 220 nm. This resembles the CD spectrum of IDPs that are characterized with a minimum at 200 nm, and an approximately zero value at 220 nm.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":1,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"22906532","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":699,"term_name":"molecular function inhibitor activity","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"Previously it was shown that the phosphorylated form of hNopp140 preferentially binds to CK2, suppressing the catalytic activity of the enzyme. This enzyme is highly conserved in eukaryotes and is implicated in cell proliferation, apoptosis and differentiation. In fact, CK2 was found to be primarily responsible for extensive phosphorylation of hNopp140.","type":"Introduction"}],"curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"22906532","version":3,"reference_html":"Structural disorder and local order of hNopp140. <i> Tantos A, Szrnka K, Szabo B, Bokor M, Kamasa P, Matus P, Bekesi A, Tompa K, Han KH, Tompa P. </i> Biochim Biophys Acta, 2013","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140678","ec_id":"ECO:0006204","region_id":"DP01178r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":699,"region_id":"DP01178r004","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Structural disorder and local order of hNopp140. <i> Tantos A, Szrnka K, Szabo B, Bokor M, Kamasa P, Matus P, Bekesi A, Tompa K, Han KH, Tompa P. </i> Biochim Biophys Acta, 2013","statement":[{"text":"Protease sensitivity is another important marker of disordered proteins, because their extended structure makes them fully accessible to the action of proteases. In accord, hNopp140 proved to be highly sensitive to proteolysis which is another piece of evidence underlining its disordered status. The level of intact BSA has hardly changed in the\ntime-scale used in our experiment, while hNopp140 was degraded promptly by both proteinase K and trypsin. After only 30 s there was practically no detectable hNopp140 left,while the level of BSA stayed stable even after 1 min","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":1,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"22906532","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":699,"region_id":"DP01178r005","released":"2022_03","ec_id":"ECO:0006198","reference_html":"Structural disorder and local order of hNopp140. <i> Tantos A, Szrnka K, Szabo B, Bokor M, Kamasa P, Matus P, Bekesi A, Tompa K, Han KH, Tompa P. </i> Biochim Biophys Acta, 2013","statement":[{"text":"As further evidence for the absence of folded structure, the proton 1D spectrum is concentrated to a relatively narrow ppm region. The reason for this is that the similar chemical environment of the protons in the same chemical group results in very similar chemical shifts. The proton 1D spectrum of globular proteins spreads over a much wider\nrange due to the very big differences in the local magnetic environments. 1H-NMR spectra of hNopp140 is characterized by line narrowing and lack of resonance dispersion typical of a disordered protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":1,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"22906532","version":2,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":699,"term_name":"phosphorylation display site","start":1,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","statement":[{"text":"Most serine residues are phosphorylated by casein kinase 2 (CK2), which makes hNopp140 one of the most highly phosphorylated proteins in the cell with approximately 80 phosphates per molecule. Several other kinases such as PKA, PKC and cdc2 kinase, are able to phosphorylate Nopp140 underlining the importance of the phosphorylation in the regulation of the function of the protein and it was also shown that PKA and not CK2 phosphorylation was necessary for the rat Nopp140 to be able to activate agp gene expression.","type":"Introduction"}],"curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"22906532","version":2,"reference_html":"Structural disorder and local order of hNopp140. <i> Tantos A, Szrnka K, Szabo B, Bokor M, Kamasa P, Matus P, Bekesi A, Tompa K, Han KH, Tompa P. </i> Biochim Biophys Acta, 2013","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000045","ec_id":"ECO:0006198","region_id":"DP01178r006","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":699,"region_id":"DP01178r007","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Structural disorder and local order of hNopp140. <i> Tantos A, Szrnka K, Szabo B, Bokor M, Kamasa P, Matus P, Bekesi A, Tompa K, Han KH, Tompa P. </i> Biochim Biophys Acta, 2013","statement":[{"text":"Protein disorder also manifests itself in other physical characteristics, such as aberrant mobility in gel filtration. Most IDPs elute at two to six times higher molecular weight than their actual size. The apparent molecular weight of hNopp140 extrapolated from the data of four protein standards is 511.0 kDa in contrast to the 75.58 kDa\ncalculated from its amino acid sequence, resulting in an apparent molar weight 7 times higher than the actual size of the molecule.\nThe hydrodynamic radius of hNopp140 was also determined in this\nexperiment and gave a result of 5.7 nm. Based on the classification of\nunfolded proteins according to their compactness [42], hNopp140 falls\nsomewhere between random coil and premolten globule, but it is closer\nto the latter category (Fig. 3B).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":1,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"22906532","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q14978","date":"2018-06-27T10:47:11.000Z","acc":"Q14978","name":"Nucleolar and coiled-body phosphoprotein 1","length":699,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00001303C3","genes":[{"name":{"value":"NOLC1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:15608","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:15608"}}]},"synonyms":[{"value":"KIAA0035","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"7584026","url":"http://www.ncbi.nlm.nih.gov/pubmed/7584026","alternativeUrl":"https://europepmc.org/abstract/MED/7584026"}}]},{"value":"NS5ATP13"}]}],"alphafold_very_low_content":0.6738197424892703,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":699,"type":"D"}],"Structural state":[{"start":1,"end":699,"type":"D"}],"Molecular function":[{"start":1,"end":699,"type":"F"}],"Disorder function":[{"start":1,"end":699,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00644","name":"Poly(ADP-ribose) polymerase catalytic domain","start":320,"end":421},{"id":"PF12174","name":"RCD1-SRO-TAF4 (RST) plant domain","start":502,"end":568},{"id":"PF23467","name":"WWE domain","start":83,"end":162}],"gene3D":[{"start":273,"end":451,"id":"3.90.228.10","name":"3.90.228.10"}]},"uniref50":"UniRef50_Q8RY59","sequence":"MEAKIVKVLDSSRCEDGFGKKRKRAASYAAYVTGVSCAKLQNVPPPNGQCQIPDKRRRLEGENKLSAYENRSGKALVRYYTYFKKTGIAKRVMMYENGEWNDLPEHVICAIQNELEEKSAAIEFKLCGHSFILDFLHMQRLDMETGAKTPLAWIDNAGKCFFPEIYESDERTNYCHHKCVEDPKQNAPHDIKLRLEIDVNGGETPRLNLEECSDESGDNMMDDVPLAQRSSNEHYDEATEDSCSRKLEAAVSKWDETDAIVVSGAKLTGSEVLDKDAVKKMFAVGTASLGHVPVLDVGRFSSEIAEARLALFQKQVEITKKHRGDANVRYAWLPAKREVLSAVMMQGLGVGGAFIRKSIYGVGIHLTAADCPYFSARYCDVDENGVRYMVLCRVIMGNMELLRGDKAQFFSGGEEYDNGVDDIESPKNYIVWNINMNTHIFPEFVVRFKLSNLPNAEGNLIAKRDNSGVTLEGPKDLPPQLESNQGARGSGSANSVGSSTTRPKSPWMPFPTLFAAISHKVAENDMLLINADYQQLRDKKMTRAEFVRKLRVIVGDDLLRSTITTLQNQPKSKEIPGSIRDHEEGAGGL","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q8RY59","disprot_id":"DP01180","ncbi_taxon_id":3702,"regions_counter":4,"creator":"vnugnes","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":509,"region_id":"DP01180r001","released":"2025_12","ec_id":"ECO:0006165","reference_html":"<sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N NMR chemical shift assignments of A. thaliana RCD1 RST. <i> Tossavainen H, Hellman M, Vainonen JP, Kangasjärvi J, Permi P. </i> Biomol NMR Assign, 2017","term_id":"IDPO:0000002","curator_id":"vnugnes","start":468,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"28593560","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2025-10-14T18:55:40.902Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"27034"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The 1H, 15N HSQC spectrum of RCD1 (468–589) is shown in Fig. 1b, in which the labels are colored according to this structure prediction. In agreement with the prediction, about half of the amide peaks, originating from the structured segment, are widely dispersed (green labels) and have uniform peak intensities while the other half are clustered in a narrow region of the 1HN axis and show great variance in peak intensities, ranging from very weak (e.g. V469–L471 and G491–S495) to very high (e.g. D476–L481).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":589,"region_id":"DP01180r002","released":"2025_12","ec_id":"ECO:0006165","reference_html":"<sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N NMR chemical shift assignments of A. thaliana RCD1 RST. <i> Tossavainen H, Hellman M, Vainonen JP, Kangasjärvi J, Permi P. </i> Biomol NMR Assign, 2017","term_id":"IDPO:0000002","curator_id":"vnugnes","start":568,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"28593560","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2025-10-14T18:55:26.019Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"27034"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The 1H, 15N HSQC spectrum of RCD1 (468–589) is shown in Fig. 1b, in which the labels are colored according to this structure prediction. In agreement with the prediction, about half of the amide peaks, originating from the structured segment, are widely dispersed (green labels) and have uniform peak intensities while the other half are clustered in a narrow region of the 1HN axis and show great variance in peak intensities, ranging from very weak (e.g. V469–L471 and G491–S495) to very high (e.g. D476–L481).","type":"Results"}]},{"start":500,"end":511,"reference_id":"29657132","reference_source":"pmid","reference_html":"Structure of Radical-Induced Cell Death1 Hub Domain Reveals a Common αα-Scaffold for Disorder in Transcriptional Networks. <i> Bugge K, Staby L, Kemplen KR, O'Shea C, Bendsen SK, Jensen MK, Olsen JG, Skriver K, Kragelund BB. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"5OAO"},{"db":"BMRB","id":"27302"}],"region_id":"DP01180r003","statement":[{"text":"Triple-resonance NMR spectra showed significant peak-broadening in the N-terminal region of both variants, as also reported in a recent NMR analysis of RCD1-RST468-589 (Tossavainen et al., 2017).","type":"Results"},{"text":"Although sequential assignment was possible in the free state, structure elucidation was impeded by general peak-broadening, particularly in the N-terminal region.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-15T12:57:40.447Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":573,"end":589,"reference_id":"34687712","reference_source":"pmid","reference_html":"Flanking Disorder of the Folded αα-Hub Domain from Radical Induced Cell Death1 Affects Transcription Factor Binding by Ensemble Redistribution. <i> Staby L, Due AD, Kunze MBA, Jørgensen MLM, Skriver K, Kragelund BB. </i> J Mol Biol, 2021","date":"2025-10-14T19:05:21.361Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000056","term_name":"self-interaction","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_12","version":2,"cross_refs":[{"db":"BMRB","id":"50545"}],"region_id":"DP01180r004","statement":[{"text":"This  suggests  that  the  flanking  regions induce  a  conformational  state  mimicking  the  bound  state.  In  support  of  this,  amide  CSPs  of  RCD1-RST487-589 correlated well with those of DREB2A-bound RCD1-RST499-572, when using unbound RCD1-RST499-572 as reference (Fig. 1D, top, S1A, Pearson’s r = 0.84).","type":"Results"},{"text":"The amide resonances of this variant overlapped with those of RCD1-RST487-589 confirming the C-terminal tail as the source of the induced changes (Fig. 1C).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_Q8RY59","date":"2018-06-27T12:13:59.000Z","acc":"Q8RY59","name":"Inactive poly [ADP-ribose] polymerase RCD1","length":589,"organism":"Arabidopsis thaliana","dataset":["Stress response proteins"],"UniParc":"UPI00000A133F","genes":[{"name":{"value":"RCD1"},"synonyms":[{"value":"ATP8"},{"value":"CEO1"}],"orfNames":[{"value":"F3C3.1"}],"olnNames":[{"value":"At1g32230"}]}],"alphafold_very_low_content":0.41935483870967744,"disorder_content":0.11205432937181664,"disprot_consensus":{"full":[{"start":468,"end":511,"type":"D"},{"start":568,"end":589,"type":"D"}],"Structural state":[{"start":468,"end":511,"type":"D"},{"start":568,"end":589,"type":"D"}],"Disorder function":[{"start":573,"end":589,"type":"F"}]}},{"features":{"pfam":[{"id":"PF17524","name":"Anti-sigma factor CnrY","start":1,"end":95}]},"uniref50":"UniRef50_P56621","sequence":"MADVEEWLTHARKVTQEASIGVDVTSIQECISAEPAQRVLVARRDAWRAICCAAFAALVAFAAINRVATIMLEKPAPTWVATPSAASPFGLLIGK","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Cupriavidus"],"uniref90":"UniRef90_P56621","disprot_id":"DP01181","ncbi_taxon_id":266264,"regions_counter":5,"creator":"mpajkos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":30,"region_id":"DP01181r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The crystal structure of the anti-σ factor CnrY in complex with the σ factor CnrH shows a new structural class of anti-σ factors targeting extracytoplasmic function σ factors. <i> Maillard AP, Girard E, Ziani W, Petit-Härtlein I, Kahn R, Covès J. </i> J Mol Biol, 2014","statement":[{"text":"The crystall structure of CnrH ( residues 5–91 and 123–189) and CnrYc (residues 2–30) has been solved.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":2,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4CXF"}],"reference_id":"24727125","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":30,"term_name":"molecular function inhibitor activity","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"The crystal structure of the anti-σ factor CnrY in complex with the σ factor CnrH shows a new structural class of anti-σ factors targeting extracytoplasmic function σ factors. <i> Maillard AP, Girard E, Ziani W, Petit-Härtlein I, Kahn R, Covès J. </i> J Mol Biol, 2014","statement":[{"text":"CnrH inhibition by CnrYc.\n\"CnrYc stabilizes a conformation of CnrH that cannot bind the promoter − 10 element and it occludes the RP core-binding determinants on σ2 and σ4.\"","type":"Discussion"}],"term_id":"GO:0140678","curator_id":"mpajkos","start":2,"term_ontology":"GO","curator_name":"Mátyás Pajkos","reference_id":"24727125","version":3,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01181r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":30,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"The crystal structure of the anti-σ factor CnrY in complex with the σ factor CnrH shows a new structural class of anti-σ factors targeting extracytoplasmic function σ factors. <i> Maillard AP, Girard E, Ziani W, Petit-Härtlein I, Kahn R, Covès J. </i> J Mol Biol, 2014","statement":[{"text":"\"The final 1.75-Å-resolution model consists of residues 5–91 and 123–189 of CnrH, and in residues 2–30 of CnrY\"","type":"Methods"}],"term_id":"GO:0005515","curator_id":"mpajkos","start":2,"term_ontology":"GO","curator_name":"Mátyás Pajkos","reference_id":"24727125","version":3,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01181r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":30,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"The crystal structure of the anti-σ factor CnrY in complex with the σ factor CnrH shows a new structural class of anti-σ factors targeting extracytoplasmic function σ factors. <i> Maillard AP, Girard E, Ziani W, Petit-Härtlein I, Kahn R, Covès J. </i> J Mol Biol, 2014","term_id":"IDPO:0000011","curator_id":"mpajkos","start":2,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","reference_id":"24727125","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01181r005","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_P56621","date":"2018-06-27T14:41:13.000Z","acc":"P56621","name":"Nickel and cobalt resistance protein CnrY","length":95,"organism":"Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)","dataset":[],"UniParc":"UPI0000127C3A","genes":[{"name":{"value":"cnrY"},"synonyms":[{"value":"ORF0b"}],"orfNames":[{"value":"RMe0088"}],"olnNames":[{"value":"Rmet_6205"}]}],"alphafold_very_low_content":0.010526315789473684,"disorder_content":0.30526315789473685,"disprot_consensus":{"full":[{"start":2,"end":30,"type":"T"}],"Structural state":[{"start":2,"end":30,"type":"D"}],"Molecular function":[{"start":2,"end":30,"type":"F"}],"Structural transition":[{"start":2,"end":30,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":201,"end":466},{"id":"PF00498","name":"FHA domain","start":66,"end":133},{"id":"PF00498","name":"FHA domain","start":602,"end":680}],"gene3D":[{"start":573,"end":730,"id":"2.60.200.20","name":"2.60.200.20"},{"start":191,"end":275,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":1,"end":164,"id":"2.60.200.20","name":"2.60.200.20"},{"start":276,"end":496,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"}]},"uniref50":"UniRef50_P22216","sequence":"MENITQPTQQSTQATQRFLIEKFSQEQIGENIVCRVICTTGQIPIRDLSADISQVLKEKRSIKKVWTFGRNPACDYHLGNISRLSNKHFQILLGEDGNLLLNDISTNGTWLNGQKVEKNSNQLLSQGDEITVGVGVESDILSLVIFINDKFKQCLEQNKVDRIRSNLKNTSKIASPGLTSSTASSMVANKTGIFKDFSIIDEVVGQGAFATVKKAIERTTGKTFAVKIISKRKVIGNMDGVTRELEVLQKLNHPRIVRLKGFYEDTESYYMVMEFVSGGDLMDFVAAHGAVGEDAGREISRQILTAIKYIHSMGISHRDLKPDNILIEQDDPVLVKITDFGLAKVQGNGSFMKTFCGTLAYVAPEVIRGKDTSVSPDEYEERNEYSSLVDMWSMGCLVYVILTGHLPFSGSTQDQLYKQIGRGSYHEGPLKDFRISEEARDFIDSLLQVDPNNRSTAAKALNHPWIKMSPLGSQSYGDFSQISLSQSLSQQKLLENMDDAQYEFVKAQRKLQMEQQLQEQDQEDQDGKIQGFKIPAHAPIRYTQPKSIEAETREQKLLHSNNTENVKSSKKKGNGRFLTLKPLPDSIIQESLEIQQGVNPFFIGRSEDCNCKIEDNRLSRVHCFIFKKRHAVGKSMYESPAQGLDDIWYCHTGTNVSYLNNNRMIQGTKFLLQDGDEIKIIWDKNNKFVIGFKVEINDTTGLFNEGLGMLQEQRVVLKQTAEEKDLVKKLTQMMAAQRANQPSASSSSMSAKKPPVSDTNNNGNNSVLNDLVESPINANTGNILKRIHSVSLSQSQIDPSKKVKRAKLDQTSKGPENLQFS","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P22216","disprot_id":"DP01182","ncbi_taxon_id":559292,"regions_counter":10,"creator":"gerdos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":190,"region_id":"DP01182r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Phospho-Priming Confers Functionally Relevant Specificities for Rad53 Kinase Autophosphorylation. <i> Chen ES, Weng JH, Chen YH, Wang SC, Liu XX, Huang WC, Matsui T, Kawano Y, Liao JH, Lim LH, Bessho Y, Huang KF, Wu WJ, Tsai MD. </i> Biochemistry, 2017","statement":[{"text":"Electron density is not discernible for part of the SCD1 domain (residues\n1−14), part of the loops of the FHA1 domain (residues 79−86 and 135−137), the linker region between the FHA1 and kinase domains (residues 165−190), part of the activation segment (residues 344−356)","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jmanso","start":165,"term_ontology":"IDPO","curator_name":"Jose A Manso","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28858528","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":14,"region_id":"DP01182r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Phospho-Priming Confers Functionally Relevant Specificities for Rad53 Kinase Autophosphorylation. <i> Chen ES, Weng JH, Chen YH, Wang SC, Liu XX, Huang WC, Matsui T, Kawano Y, Liao JH, Lim LH, Bessho Y, Huang KF, Wu WJ, Tsai MD. </i> Biochemistry, 2017","statement":[{"text":"Electron density is not discernible for part of the SCD1 domain (residues\n1−14), part of the loops of the FHA1 domain (residues 79−86 and 135−137), the linker region between the FHA1 and kinase domains (residues 165−190), part of the activation segment (residues 344−356)","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jmanso","start":1,"term_ontology":"IDPO","curator_name":"Jose A Manso","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28858528","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP01182r003","ec_ontology":"ECO","end":190,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":170,"version":3,"statement":[{"text":"No discernable electron density was observed for a number of loop regions, including the N-terminal 21 residues preceding the kinase domain (170 to 190), residues 207 to 209 of the glycine-rich loop β1–β2 in molecule B (201 to 209 in molecule A), residues 234 to 237 of loop β3–αC (232 to 238 in molecule B), residues 347 to 357 of the activation segment, residues 369 to 381 of loop αEF–αF, residues 472 to 474, and the C-terminal 16 residues (497 to 512).","type":"Results"}],"term_name":"disorder","reference_html":"Structural basis of Rad53 kinase activation by dimerization and activation segment exchange. <i> Wybenga-Groot LE, Ho CS, Sweeney FD, Ceccarelli DF, McGlade CJ, Durocher D, Sicheri F. </i> Cell Signal, 2014","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24815189","date":"2023-08-24T17:03:22.545Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4PDP"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"GAMATSKIASPGLTSSTASSMVANKTGIFKDFSIIDEVVGQGAFATVKKAIERTTGKTFSVKIISKRKVIGNMDGVTRELEVLQKLNHPRIVRLKGFYEDTESYYMVMEFVSGGDLMDFVAAHGAVGEDAGREISRQILTAIKYIHSMGISHRDLKPDNILIEQDDPVLVKITAFGLAKVQGNGSFMKTFCGTLAYVAPEVIRGKDTSVSPDEYEERNEYSSLVDMWSMGCLVYVILTGHLPFSGSTQDQLYKQIGRGSYHEGPLKDFRISEEARDFIDSLLQVDPNNRSTAAKALNHPWIKMSPLGSQSYGDFSQISLSQSLSQQKLLENMDDAQYEFVKAQRKLQ"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":356,"region_id":"DP01182r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Phospho-Priming Confers Functionally Relevant Specificities for Rad53 Kinase Autophosphorylation. <i> Chen ES, Weng JH, Chen YH, Wang SC, Liu XX, Huang WC, Matsui T, Kawano Y, Liao JH, Lim LH, Bessho Y, Huang KF, Wu WJ, Tsai MD. </i> Biochemistry, 2017","statement":[{"text":"Electron density is not discernible for part of the SCD1 domain (residues\n1−14), part of the loops of the FHA1 domain (residues 79−86 and 135−137), the linker region between the FHA1 and kinase domains (residues 165−190), part of the activation segment (residues 344−356)","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jmanso","start":344,"term_ontology":"IDPO","curator_name":"Jose A Manso","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28858528","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP01182r005","ec_ontology":"ECO","end":357,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":347,"version":3,"statement":[{"text":"No discernable electron density was observed for a number of loop regions, including the N-terminal 21 residues preceding the kinase domain (170 to 190), residues 207 to 209 of the glycine-rich loop β1–β2 in molecule B (201 to 209 in molecule A), residues 234 to 237 of loop β3–αC (232 to 238 in molecule B), residues 347 to 357 of the activation segment, residues 369 to 381 of loop αEF–αF, residues 472 to 474, and the C-terminal 16 residues (497 to 512).","type":"Results"}],"term_name":"disorder","reference_html":"Structural basis of Rad53 kinase activation by dimerization and activation segment exchange. <i> Wybenga-Groot LE, Ho CS, Sweeney FD, Ceccarelli DF, McGlade CJ, Durocher D, Sicheri F. </i> Cell Signal, 2014","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24815189","date":"2023-08-24T17:02:44.582Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4PDP"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"GAMATSKIASPGLTSSTASSMVANKTGIFKDFSIIDEVVGQGAFATVKKAIERTTGKTFSVKIISKRKVIGNMDGVTRELEVLQKLNHPRIVRLKGFYEDTESYYMVMEFVSGGDLMDFVAAHGAVGEDAGREISRQILTAIKYIHSMGISHRDLKPDNILIEQDDPVLVKITAFGLAKVQGNGSFMKTFCGTLAYVAPEVIRGKDTSVSPDEYEERNEYSSLVDMWSMGCLVYVILTGHLPFSGSTQDQLYKQIGRGSYHEGPLKDFRISEEARDFIDSLLQVDPNNRSTAAKALNHPWIKMSPLGSQSYGDFSQISLSQSLSQQKLLENMDDAQYEFVKAQRKLQ"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":357,"term_name":"phosphorylation display site","released":"2023_12","ec_name":"immunodetection assay evidence used in manual assertion","reference_html":"Structural basis of Rad53 kinase activation by dimerization and activation segment exchange. <i> Wybenga-Groot LE, Ho CS, Sweeney FD, Ceccarelli DF, McGlade CJ, Durocher D, Sicheri F. </i> Cell Signal, 2014","statement":[{"text":" Phosphorylation was assessed by immunoblot using a Thr354 phospho-specific antibody (α-Rad53pT354).","type":"Introduction"}],"term_id":"IDPO:0000045","curator_id":"vnugnes","start":352,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24815189","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-24T17:08:24.908Z","reference_source":"pmid","ec_id":"ECO:0007719","region_id":"DP01182r006","ec_go":"EXP","disprot_namespace":"Disorder function"},{"region_id":"DP01182r007","ec_ontology":"ECO","end":382,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":368,"version":3,"statement":[{"text":"No discernable electron density was observed for a number of loop regions, including the N-terminal 21 residues preceding the kinase domain (170 to 190), residues 207 to 209 of the glycine-rich loop β1–β2 in molecule B (201 to 209 in molecule A), residues 234 to 237 of loop β3–αC (232 to 238 in molecule B), residues 347 to 357 of the activation segment, residues 369 to 381 of loop αEF–αF, residues 472 to 474, and the C-terminal 16 residues (497 to 512)","type":"Results"}],"term_name":"disorder","reference_html":"Structural basis of Rad53 kinase activation by dimerization and activation segment exchange. <i> Wybenga-Groot LE, Ho CS, Sweeney FD, Ceccarelli DF, McGlade CJ, Durocher D, Sicheri F. </i> Cell Signal, 2014","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24815189","date":"2023-08-24T17:02:13.748Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4PDP"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"GAMATSKIASPGLTSSTASSMVANKTGIFKDFSIIDEVVGQGAFATVKKAIERTTGKTFSVKIISKRKVIGNMDGVTRELEVLQKLNHPRIVRLKGFYEDTESYYMVMEFVSGGDLMDFVAAHGAVGEDAGREISRQILTAIKYIHSMGISHRDLKPDNILIEQDDPVLVKITAFGLAKVQGNGSFMKTFCGTLAYVAPEVIRGKDTSVSPDEYEERNEYSSLVDMWSMGCLVYVILTGHLPFSGSTQDQLYKQIGRGSYHEGPLKDFRISEEARDFIDSLLQVDPNNRSTAAKALNHPWIKMSPLGSQSYGDFSQISLSQSLSQQKLLENMDDAQYEFVKAQRKLQ"},{"region_id":"DP01182r008","ec_ontology":"ECO","end":512,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":497,"version":3,"statement":[{"text":"No discernable electron density was observed for a number of loop regions, including the N-terminal 21 residues preceding the kinase domain (170 to 190), residues 207 to 209 of the glycine-rich loop β1–β2 in molecule B (201 to 209 in molecule A), residues 234 to 237 of loop β3–αC (232 to 238 in molecule B), residues 347 to 357 of the activation segment, residues 369 to 381 of loop αEF–αF, residues 472 to 474, and the C-terminal 16 residues (497 to 512).","type":"Results"}],"term_name":"disorder","reference_html":"Structural basis of Rad53 kinase activation by dimerization and activation segment exchange. <i> Wybenga-Groot LE, Ho CS, Sweeney FD, Ceccarelli DF, McGlade CJ, Durocher D, Sicheri F. </i> Cell Signal, 2014","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24815189","date":"2023-08-24T17:01:31.401Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4PDP"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"GAMATSKIASPGLTSSTASSMVANKTGIFKDFSIIDEVVGQGAFATVKKAIERTTGKTFSVKIISKRKVIGNMDGVTRELEVLQKLNHPRIVRLKGFYEDTESYYMVMEFVSGGDLMDFVAAHGAVGEDAGREISRQILTAIKYIHSMGISHRDLKPDNILIEQDDPVLVKITAFGLAKVQGNGSFMKTFCGTLAYVAPEVIRGKDTSVSPDEYEERNEYSSLVDMWSMGCLVYVILTGHLPFSGSTQDQLYKQIGRGSYHEGPLKDFRISEEARDFIDSLLQVDPNNRSTAAKALNHPWIKMSPLGSQSYGDFSQISLSQSLSQQKLLENMDDAQYEFVKAQRKLQ"}],"released":"2018_11","uniref100":"UniRef100_P22216","date":"2018-06-27T14:55:50.000Z","acc":"P22216","name":"Serine/threonine-protein kinase RAD53","length":821,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000005328E","genes":[{"name":{"value":"RAD53"},"synonyms":[{"value":"MEC2"},{"value":"SAD1"},{"value":"SPK1"}],"orfNames":[{"value":"P2588"}],"olnNames":[{"value":"YPL153C"}]}],"alphafold_very_low_content":0.24238733252131547,"disorder_content":0.10353227771010962,"disprot_consensus":{"full":[{"start":1,"end":14,"type":"D"},{"start":165,"end":190,"type":"D"},{"start":344,"end":357,"type":"D"},{"start":368,"end":382,"type":"D"},{"start":497,"end":512,"type":"D"}],"Structural state":[{"start":1,"end":14,"type":"D"},{"start":165,"end":190,"type":"D"},{"start":344,"end":357,"type":"D"},{"start":368,"end":382,"type":"D"},{"start":497,"end":512,"type":"D"}],"Disorder function":[{"start":352,"end":357,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04538","name":"Brain expressed X-linked like family","start":13,"end":124}]},"uniref50":"UniRef50_Q3MKQ2","sequence":"MESKDQGVKNLNMENDHQKKEEKEEKPQDTIRREPAVALTSEAGKNCAPRGGRRRFRVRQPIAHYRWDLMQRVGEPQGRMREENVQRFGGDVRQLMEKLRERQLSHSLRAVSTDPPHHDHHDEFCLMP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q9R224","disprot_id":"DP01183","ncbi_taxon_id":10090,"regions_counter":2,"creator":"mguha","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":128,"region_id":"DP01183r002","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Brain expressed and X-linked (Bex) proteins are intrinsically disordered proteins (IDPs) and form new signaling hubs. <i> Fernandez EM, Díaz-Ceso MD, Vilar M. </i> PLoS One, 2015","statement":[{"text":"As shown in Fig. 6B, the CD spectrum of Bex1 in solution revealed a high level of disorder, although the observed spectrum did not exhibit a completely random coil conformation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-24T17:20:19.540Z","reference_source":"pmid","term_name":"disorder","reference_id":"25612294","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9R224","date":"2018-06-27T18:58:06.000Z","acc":"Q9R224","name":"Protein BEX1","length":128,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000294F8","genes":[{"name":{"value":"Bex1"},"synonyms":[{"value":"Rex3"}]}],"alphafold_very_low_content":0.21875,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":128,"type":"D"}],"Structural state":[{"start":1,"end":128,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":326,"end":572},{"id":"PF00786","name":"P21-Rho-binding domain","start":10,"end":63}],"gene3D":[{"start":4,"end":47,"id":"3.90.810.10","name":"CRIB domain"},{"start":398,"end":591,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"},{"start":261,"end":397,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"}]},"uniref50":"UniRef50_O96013","sequence":"MFGKRKKRVEISAPSNFEHRVHTGFDQHEQKFTGLPRQWQSLIEESARRPKPLVDPACITSIQPGAPKTIVRGSKGAKDGALTLLLDEFENMSVTRSNSLRRDSPPPPARARQENGMPEEPATTARGGPGKAGSRGRFAGHSEAGGGSGDRRRAGPEKRPKSSREGSGGPQESSRDKRPLSGPDVGTPQPAGLASGAKLAAGRPFNTYPRADTDHPSRGAQGEPHDVAPNGPSAGGLAIPQSSSSSSRPPTRARGAPSPGVLGPHASEPQLAPPACTPAAPAVPGPPGPRSPQREPQRVSHEQFRAALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNRTR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O96013","disprot_id":"DP01184","ncbi_taxon_id":9606,"regions_counter":3,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":68,"region_id":"DP01184r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR binding and crystal structure reveal that intrinsically-unstructured regulatory domain auto-inhibits PAK4 by a mechanism different from that of PAK1. <i> Wang W, Lim L, Baskaran Y, Manser E, Song J. </i> Biochem Biophys Res Commun, 2013","statement":[{"text":"Furthermore, it is also lacking of any tight\ntertiary packing as evident from its HSQC spectrum which has\nnarrow spectral dispersions on both 1H and 15N dimensions","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":9,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23876315","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":68,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"NMR binding and crystal structure reveal that intrinsically-unstructured regulatory domain auto-inhibits PAK4 by a mechanism different from that of PAK1. <i> Wang W, Lim L, Baskaran Y, Manser E, Song J. </i> Biochem Biophys Res Commun, 2013","statement":[{"text":"In the present study, we first experimentally demonstrate that\nthe N-terminal regulatory domain sufficient for auto-inhibiting\nPAK4 and binding Cdc42 isintrinsically unstructured.","type":"Discussion"}],"term_id":"GO:0005515","curator_id":"eschad","start":9,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"23876315","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01184r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":68,"region_id":"DP01184r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"NMR binding and crystal structure reveal that intrinsically-unstructured regulatory domain auto-inhibits PAK4 by a mechanism different from that of PAK1. <i> Wang W, Lim L, Baskaran Y, Manser E, Song J. </i> Biochem Biophys Res Commun, 2013","statement":[{"text":"As judged from its far-UV spectrum with the maximal negative\nsignal at 201 nm (Fig. 1B), the domain is predominantly\nunstructured in the free state, without any stable secondary\nstructures","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":9,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23876315","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_O96013","date":"2018-06-28T14:45:40.000Z","acc":"O96013","name":"Serine/threonine-protein kinase PAK 4","length":591,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000001281","genes":[{"name":{"value":"PAK4"},"synonyms":[{"value":"KIAA1142"}]}],"alphafold_very_low_content":0.38578680203045684,"disorder_content":0.10152284263959391,"disprot_consensus":{"full":[{"start":9,"end":68,"type":"D"}],"Structural state":[{"start":9,"end":68,"type":"D"}],"Molecular function":[{"start":9,"end":68,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03876","name":"SHS2 domain found in N terminus of Rpb7p/Rpc25p/MJ0397","start":45,"end":111},{"id":"PF17875","name":"RPA43 OB domain in RNA Pol I","start":127,"end":250}],"gene3D":[{"start":21,"end":130,"id":"3.30.1490.120","name":"RNA polymerase Rpb7-like, N-terminal domain"}]},"uniref50":"UniRef50_P46669","sequence":"MSQVKRANENRETARFIKKHKKQVTNPIDEKNGTSNCIVRVPIALYVSLAPMYLENPLQGVMKQHLNPLVMKYNNKVGGVVLGYEGLKILDADPLSKEDTSEKLIKITPDTPFGFTWCHVNLYVWQPQVGDVLEGYIFIQSASHIGLLIHDAFNASIKKNNIPVDWTFVHNDVEEDADVINTDENNGNNNNEDNKDSNGGSNSLGKFSFGNRSLGHWVDSNGEPIDGKLRFTVRNVHTTGRVVSVDGTLISDADEEGNGYNSSRSQAESLPIVSNKKIVFDDEVSIENKESHKELDLPEVKEDNGSEIVYEENTSESNDGESSDSD","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P46669","disprot_id":"DP01185","ncbi_taxon_id":559292,"regions_counter":3,"creator":"jmanso","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":111,"region_id":"DP01185r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Functional architecture of RNA polymerase I. <i> Kuhn CD, Geiger SR, Baumli S, Gartmann M, Gerber J, Jennebach S, Mielke T, Tschochner H, Beckmann R, Cramer P. </i> Cell, 2007","statement":[{"text":"The A43 tip loop is flexible in the crystal structure (Figures 3B and S4), but is likely folded upon binding to the Pol I core.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jmanso","start":95,"term_ontology":"IDPO","curator_name":"Jose A Manso","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18160037","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":111,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Functional architecture of RNA polymerase I. <i> Kuhn CD, Geiger SR, Baumli S, Gartmann M, Gerber J, Jennebach S, Mielke T, Tschochner H, Beckmann R, Cramer P. </i> Cell, 2007","term_id":"GO:0005515","curator_id":"jmanso","start":95,"term_ontology":"GO","curator_name":"Jose A Manso","reference_id":"18160037","version":3,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01185r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":111,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Functional architecture of RNA polymerase I. <i> Kuhn CD, Geiger SR, Baumli S, Gartmann M, Gerber J, Jennebach S, Mielke T, Tschochner H, Beckmann R, Cramer P. </i> Cell, 2007","term_id":"IDPO:0000011","curator_id":"jmanso","start":95,"term_ontology":"IDPO","curator_name":"Jose A Manso","reference_id":"18160037","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01185r003","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_P46669","date":"2018-06-28T18:36:07.000Z","acc":"P46669","name":"DNA-directed RNA polymerase I subunit RPA43","length":326,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI00000531DF","genes":[{"name":{"value":"RPA43"},"synonyms":[{"value":"RRN12"}],"orfNames":[{"value":"O6271"}],"olnNames":[{"value":"YOR340C"}]}],"alphafold_very_low_content":0.254601226993865,"disorder_content":0.05214723926380368,"disprot_consensus":{"full":[{"start":95,"end":111,"type":"T"}],"Structural state":[{"start":95,"end":111,"type":"D"}],"Molecular function":[{"start":95,"end":111,"type":"F"}],"Structural transition":[{"start":95,"end":111,"type":"T"}]}},{"acc":"P03086","sequence":"MVLRQLSRKASVKVSKTWSGTKKRAQRILIFLLEFLLDFCTGEDSVDGKKRQRHSGLTEQTYSALPEPKAT","creator":"bszabo","dataset":["Viral proteins"],"date":"2018-06-29T10:49:27.000Z","disprot_id":"DP01186","features":{"pfam":[{"id":"PF01736","name":"Polyomavirus agnoprotein","start":1,"end":63}]},"genes":[],"length":71,"name":"Agnoprotein","ncbi_taxon_id":10632,"organism":"JC polyomavirus","regions_counter":5,"released":"2018_11","taxonomy":["Viruses","Monodnaviria","Shotokuvirae","Cossaviricota","Papovaviricetes","Sepolyvirales","Polyomaviridae","Betapolyomavirus"],"UniParc":"UPI00000000EC","uniref100":"UniRef100_P03086","uniref50":"UniRef50_P03086","uniref90":"UniRef90_P03086","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5NHQ","_id":"685af523b4ac24d5329d8e29"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":14,"end":23,"interaction_partner":[],"reference_html":"Nuclear Magnetic Resonance Structure of the Human Polyoma JC Virus Agnoprotein. <i> Coric P, Saribas AS, Abou-Gharbia M, Childers W, Condra JH, White MK, Safak M, Bouaziz S. </i> J Cell Biochem, 2017","reference_id":"28295503","region_id":"DP01186r002","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Here, we report the resolution of the 3D structure of full-length JCV agnoprotein by NMR, which not only confirmed the existence of the previously reported major α-helix domain at the same position but also revealed the presence of an additional minor α-helix region spanning amino acid residues Leu6 to Ala10. The remaining regions of the protein adopt an intrinsically unstructured conformation.","_id":"685af523b4ac24d5329d8e2a"},{"type":"Figure","text":"Average structure of agnoprotein contains two α-helical structures Leu6- Lsy13 and Arg24-Phe39 (colored green) and two principal unstructured regions spanning residues Val14-Lys23 and Cys40-Thr71 (colored red).","_id":"685af523b4ac24d5329d8e2b"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-15T11:59:10.101Z","_id":"685af523b4ac24d5329d8e2c"},"version":1,"_id":"685af523b4ac24d5329d8e28","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5NHQ","_id":"685af523b4ac24d5329d8e2e"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":40,"end":71,"interaction_partner":[],"reference_html":"Nuclear Magnetic Resonance Structure of the Human Polyoma JC Virus Agnoprotein. <i> Coric P, Saribas AS, Abou-Gharbia M, Childers W, Condra JH, White MK, Safak M, Bouaziz S. </i> J Cell Biochem, 2017","reference_id":"28295503","region_id":"DP01186r003","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Here, we report the resolution of the 3D structure of full-length JCV agnoprotein by NMR, which not only confirmed the existence of the previously reported major α-helix domain at the same position but also revealed the presence of an additional minor α-helix region spanning amino acid residues Leu6 to Ala10. The remaining regions of the protein adopt an intrinsically unstructured conformation.","_id":"685af523b4ac24d5329d8e2f"},{"type":"Figure","text":"Average structure of agnoprotein contains two α-helical structures Leu6- Lsy13 and Arg24-Phe39 (colored green) and two principal unstructured regions spanning residues Val14-Lys23 and Cys40-Thr71 (colored red).","_id":"685af523b4ac24d5329d8e30"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-15T11:59:08.236Z","_id":"685af523b4ac24d5329d8e31"},"version":1,"_id":"685af523b4ac24d5329d8e2d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005644","ec_name":"immunoprecipitation evidence used in manual assertion","ec_ontology":"ECO","start":19,"end":23,"interaction_partner":[],"reference_html":"Phosphorylation mutants of JC virus agnoprotein are unable to sustain the viral infection cycle. <i> Sariyer IK, Akan I, Palermo V, Gordon J, Khalili K, Safak M. </i> J Virol, 2006","reference_id":"16571806","region_id":"DP01186r004","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Agnoprotein contains several potential phosphorylation sites, including Ser7, Ser11, and Thr21, which are potential targets for the serine/threonine-specific protein kinase C (PKC). In this study, we investigated the functional significance of these phosphorylation sites for the activity of agnoprotein. In vitro and in vivo kinase assays demonstrated that agnoprotein is a target for phosphorylation by PKC. In addition, each of the PKC phosphorylation sites was mutated to Ala singly and in combination, and the effects of these mutations on the JCV life cycle were analyzed.","_id":"685af523b4ac24d5329d8e33"},{"type":"Curator statement","text":"Evidence corresponding to Thr21.","_id":"685af523b4ac24d5329d8e34"}],"states_connection":[],"term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T14:37:23.781Z","_id":"685af523b4ac24d5329d8e35"},"version":2,"_id":"685af523b4ac24d5329d8e32","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IEP","ec_id":"ECO:0000279","ec_name":"qualitative western immunoblotting evidence used in manual assertion","ec_ontology":"ECO","start":19,"end":23,"interaction_partner":[],"reference_html":"Phosphorylation mutants of JC virus agnoprotein are unable to sustain the viral infection cycle. <i> Sariyer IK, Akan I, Palermo V, Gordon J, Khalili K, Safak M. </i> J Virol, 2006","reference_id":"16571806","region_id":"DP01186r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Agnoprotein phosphorylation mutants were unable to sustain infection cycle.","_id":"685af523b4ac24d5329d8e37"},{"type":"Results","text":"As shown in Fig. ​Fig.3A,3A, as expected, WT virus replicated efficiently during the infection cycle, and its level of replication increased gradually but significantly toward 21 day posttransfection (lanes 2 to 4). However, it was surprising that all three phosphorylation mutants of agnoprotein showed replication only during the early phases of infection cycle (lanes 5, 8, and 11) and were unable to sustain replication cycles at later time points. It was also evident from our results that mutation at Thr21 alone or those at Ser7 and Ser11 were sufficient to cause this effect.","_id":"685af523b4ac24d5329d8e38"},{"type":"Discussion","text":"In the present study, we investigated the functional importance of phosphorylation sites of agnoprotein (Ser7, Ser11, and Thr21) by genetic and biochemical approaches and demonstrated that the phosphorylation of respective target sites on agnoprotein by PKC (Ser7, Ser11, and Thr21) is critical for virus propagation.","_id":"685af523b4ac24d5329d8e39"},{"type":"Discussion","text":"In conclusion, we have demonstrated that agnoprotein is phosphorylated by PKC and viruses containing phosphorylation mutants of agnoprotein do not propagate after the first round of the infection cycle.","_id":"685af523b4ac24d5329d8e3a"},{"type":"Curator statement","text":"Evidence corresponding to Thr21.","_id":"685af523b4ac24d5329d8e3b"}],"states_connection":[],"term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T14:37:22.081Z","_id":"685af523b4ac24d5329d8e3c"},"version":2,"_id":"685af523b4ac24d5329d8e36","reference_source":"pmid"}],"__v":0,"disorder_content":0.5915492957746479,"disprot_consensus":{"full":[{"start":14,"end":23,"type":"D"},{"start":40,"end":71,"type":"D"}],"Structural state":[{"start":14,"end":23,"type":"D"},{"start":40,"end":71,"type":"D"}],"Disorder function":[{"start":19,"end":23,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00575","name":"S1 RNA binding domain","start":80,"end":157},{"id":"PF03876","name":"SHS2 domain found in N terminus of Rpb7p/Rpc25p/MJ0397","start":8,"end":66}],"gene3D":[{"start":1,"end":83,"id":"3.30.1490.120","name":"RNA polymerase Rpb7-like, N-terminal domain"},{"start":84,"end":171,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}]},"uniref50":"UniRef50_P34087","sequence":"MFFIKDLSLNITLHPSFFGPRMKQYLKTKLLEEVEGSCTGKFGYILCVLDYDNIDIQRGRILPTDGSAEFNVKYRAVVFKPFKGEVVDGTVVSCSQHGFEVQVGPMKVFVTKHLMPQDLTFNAGSNPPSYQSSEDVITIKSRIRVKIEGCISQVSSIHAIGSIKEDYLGAI","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P34087","disprot_id":"DP01187","ncbi_taxon_id":559292,"regions_counter":3,"creator":"jmanso","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":68,"region_id":"DP01187r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structures of complete RNA polymerase II and its subcomplex, Rpb4/7. <i> Armache KJ, Mitterweger S, Meinhart A, Cramer P. </i> J Biol Chem, 2005","statement":[{"text":"Disordered in the Rpb4/7 structure are the Rpb7 tip loop (residues 57– 68)","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jmanso","start":57,"term_ontology":"IDPO","curator_name":"Jose A Manso","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"15591044","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":68,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structures of complete RNA polymerase II and its subcomplex, Rpb4/7. <i> Armache KJ, Mitterweger S, Meinhart A, Cramer P. </i> J Biol Chem, 2005","statement":[{"text":"The Rpb7 tip domain binds to the Pol II core with the helical turn K1 and with the highly conserved “tip loop,” which is disordered in the free Rpb4/7 structure but folds upon core binding.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"jmanso","start":57,"term_ontology":"IDPO","curator_name":"Jose A Manso","reference_id":"15591044","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01187r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":68,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structures of complete RNA polymerase II and its subcomplex, Rpb4/7. <i> Armache KJ, Mitterweger S, Meinhart A, Cramer P. </i> J Biol Chem, 2005","term_id":"GO:0005515","curator_id":"jmanso","start":57,"term_ontology":"GO","curator_name":"Jose A Manso","reference_id":"15591044","version":3,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01187r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P34087","date":"2018-06-29T11:23:52.000Z","acc":"P34087","name":"DNA-directed RNA polymerase II subunit RPB7","length":171,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000053195","genes":[{"name":{"value":"RPB7"},"orfNames":[{"value":"D9509.22"}],"olnNames":[{"value":"YDR404C"}]}],"alphafold_very_low_content":0,"disorder_content":0.07017543859649122,"disprot_consensus":{"full":[{"start":57,"end":68,"type":"T"}],"Structural state":[{"start":57,"end":68,"type":"D"}],"Structural transition":[{"start":57,"end":68,"type":"T"}],"Molecular function":[{"start":57,"end":68,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00443","name":"Ubiquitin carboxyl-terminal hydrolase","start":362,"end":730}],"gene3D":[{"start":357,"end":734,"id":"3.90.70.10","name":"Cysteine proteinases"}]},"uniref50":"UniRef50_P53874","sequence":"MTTQESIKPLVDRILSNPLQFNAAMISNKSNNNDTSAAPENSSYIVIGKQHNNNSNSTAIAATAESKQIKENNLIDRPNGKKTNTVPKSMAEALLLYTSKNDKDAADATGAKKSAELSTELSTEPPSSSSEDDKVGKEEEEEGEIFHEARDYVEPRKASLKERDNADKGDGEDIGEDIGEDIGEDIGEDIGEDIGENLGSPLATIDDSSNENEKEKRKELSTSISSDDEIEDDEDEDDMDYDSSAMEKELPEEEENDSSSKISEGEKKSLYQDLMENSTVEVNRYEPVNNTKENGNRNPKGEEEEEEEEELKHKSRSITPPVTISNLSNFYQFNENINDRGSLNSTRIVKNWGDKFTNLKPRGLLNHGVTCYTNAAVQAMLHIPSIQHYLFDILMGKYDSTISKNSVSYTLAETSKKMWLPVSKNPRKNVSASYINPKHLISRLDDINCMMSEWQQEDSHEYFMSLMSRLQEDSVPKGHKLIESIIYDIFGGLLKQIVTCKSCGSISKTEQPFYDLSLHLKGKKKLDPNSDLSSDSINGTSATTSTTTSNAATKPSLSSSSSVNLNNGSPFAAASDLSSANRRFSIEKSIKDFFNPELIKVDKEQKGYVCEKCHKTTNAVKHSSILRAPETLLVHLKKFRFNGTSSSKMKQAVSYPMFLDLTEYCESKELPVKYQLLSVVVHEGRSLSSGHYIAHCKQPDGSWATYDDEYINIISERDVLKEPNAYYLLYTRLTPKSVPLPLAKSAMATGNVTSKSKQEQAVNEPNNRPLKINSKKNNRKKWKKNKKRKFTK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P53874","disprot_id":"DP01189","ncbi_taxon_id":559292,"regions_counter":13,"creator":"mguha","regions":[{"start":1,"end":359,"reference_id":"26149687","reference_source":"pmid","reference_html":"A Conserved Deubiquitinating Enzyme Uses Intrinsically Disordered Regions to Scaffold Multiple Protein Interaction Sites. <i> Reed BJ, Locke MN, Gardner RG. </i> J Biol Chem, 2015","date":"2024-02-08T14:06:02.892Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01189r005","statement":[{"text":"Purified Ubp10's spectrum (Fig. 3C, black line) contains minima at 204 and 218 nm, indicative of the known α-helical structure in its DUB catalytic domain (26) (Fig. 1A). However, when compared with the highly structured α-helical protein BSA (Fig. 3C, gray line), the shift of Ubp10's spectrum downwards and toward 200 nm is characteristic of a protein with a high degree of random coil (31).","type":"Results"},{"text":"Purified Ubp10 or BSA was exposed to trypsin over a time course of 45 min. Ubp10 was rapidly degraded with almost no visible full-length protein after 2 min of exposure to trypsin (Fig. 3D).","type":"Results"},{"text":"The CD and limited proteolysis results in combination with different disorder predictors used in the publication allow us to define this region as disordered.","type":"Curator statement"}]},{"start":730,"end":792,"reference_id":"26149687","reference_source":"pmid","reference_html":"A Conserved Deubiquitinating Enzyme Uses Intrinsically Disordered Regions to Scaffold Multiple Protein Interaction Sites. <i> Reed BJ, Locke MN, Gardner RG. </i> J Biol Chem, 2015","date":"2024-02-08T14:06:32.646Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01189r006","statement":[{"text":"Purified Ubp10's spectrum (Fig. 3C, black line) contains minima at 204 and 218 nm, indicative of the known α-helical structure in its DUB catalytic domain (26) (Fig. 1A). However, when compared with the highly structured α-helical protein BSA (Fig. 3C, gray line), the shift of Ubp10's spectrum downwards and toward 200 nm is characteristic of a protein with a high degree of random coil (31).","type":"Results"},{"text":"Purified Ubp10 or BSA was exposed to trypsin over a time course of 45 min. Ubp10 was rapidly degraded with almost no visible full-length protein after 2 min of exposure to trypsin (Fig. 3D).","type":"Results"},{"text":"The CD and limited proteolysis results in combination with different disorder predictors used in the publication allow us to define this region as disordered.","type":"Curator statement"}]},{"start":2,"end":27,"reference_id":"26149687","reference_source":"pmid","reference_html":"A Conserved Deubiquitinating Enzyme Uses Intrinsically Disordered Regions to Scaffold Multiple Protein Interaction Sites. <i> Reed BJ, Locke MN, Gardner RG. </i> J Biol Chem, 2015","date":"2024-02-08T14:12:56.271Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005805","ec_ontology":"ECO","ec_name":"yeast 2-hybrid evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0693","term_name":"Gal4 DNA-binding domain tag","term_namespace":"Tag","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"Yeast cells expressing fusions of the Gal4-binding domain (GBD) with Ubp10 or USP36 containing the indicated mutations and the appropriate protein fusions to the Gal4 activation domain (GAD) were spotted onto selective (synthetic medium minus histidine) and nonselective (synthetic medium plus histidine) media to assess interactions and spotting efficiency, respectively."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P36009","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01189r007","statement":[{"text":"We found that regions of Ubp10 required to interact with each protein were also sufficient for that interaction (Fig. 4C). Residues 2–27 of Ubp10 solely interacted with Dhr2. Residues 109–145 of Ubp10 solely interacted with Sir4. Residues 167–208 of Ubp10 solely interacted with Utp22.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":109,"end":145,"reference_id":"26149687","reference_source":"pmid","reference_html":"A Conserved Deubiquitinating Enzyme Uses Intrinsically Disordered Regions to Scaffold Multiple Protein Interaction Sites. <i> Reed BJ, Locke MN, Gardner RG. </i> J Biol Chem, 2015","date":"2024-02-08T14:13:24.639Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005805","ec_ontology":"ECO","ec_name":"yeast 2-hybrid evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0693","term_name":"Gal4 DNA-binding domain tag","term_namespace":"Tag","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"Yeast cells expressing fusions of the Gal4-binding domain (GBD) with Ubp10 or USP36 containing the indicated mutations and the appropriate protein fusions to the Gal4 activation domain (GAD) were spotted onto selective (synthetic medium minus histidine) and nonselective (synthetic medium plus histidine) media to assess interactions and spotting efficiency, respectively."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P11978","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01189r008","statement":[{"text":"We found that regions of Ubp10 required to interact with each protein were also sufficient for that interaction (Fig. 4C). Residues 2–27 of Ubp10 solely interacted with Dhr2. Residues 109–145 of Ubp10 solely interacted with Sir4. Residues 167–208 of Ubp10 solely interacted with Utp22.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":167,"end":208,"reference_id":"26149687","reference_source":"pmid","reference_html":"A Conserved Deubiquitinating Enzyme Uses Intrinsically Disordered Regions to Scaffold Multiple Protein Interaction Sites. <i> Reed BJ, Locke MN, Gardner RG. </i> J Biol Chem, 2015","date":"2024-02-08T14:13:53.118Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005805","ec_ontology":"ECO","ec_name":"yeast 2-hybrid evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0693","term_name":"Gal4 DNA-binding domain tag","term_namespace":"Tag","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"Yeast cells expressing fusions of the Gal4-binding domain (GBD) with Ubp10 or USP36 containing the indicated mutations and the appropriate protein fusions to the Gal4 activation domain (GAD) were spotted onto selective (synthetic medium minus histidine) and nonselective (synthetic medium plus histidine) media to assess interactions and spotting efficiency, respectively."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P53254","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01189r009","statement":[{"text":"We found that regions of Ubp10 required to interact with each protein were also sufficient for that interaction (Fig. 4C). Residues 2–27 of Ubp10 solely interacted with Dhr2. Residues 109–145 of Ubp10 solely interacted with Sir4. Residues 167–208 of Ubp10 solely interacted with Utp22.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":171,"end":208,"reference_id":"26149687","reference_source":"pmid","reference_html":"A Conserved Deubiquitinating Enzyme Uses Intrinsically Disordered Regions to Scaffold Multiple Protein Interaction Sites. <i> Reed BJ, Locke MN, Gardner RG. </i> J Biol Chem, 2015","date":"2024-02-08T14:16:33.359Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0693","term_name":"Gal4 DNA-binding domain tag","term_namespace":"Tag","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"Yeast cells expressing fusions of the Gal4-binding domain (GBD) with Ubp10 or USP36 containing the indicated mutations and the appropriate protein fusions to the Gal4 activation domain (GAD) were spotted onto selective (synthetic medium minus histidine) and nonselective (synthetic medium plus histidine) media to assess interactions and spotting efficiency, respectively."}]},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Glu171Ser208del","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P53254","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01189r010","statement":[{"text":"Residues 2–27 in Ubp10 were required to interact with Dhr2, and loss of these residues did not affect the interaction with Sir4 or Utp22. Likewise, Ubp10 required residues 109–122 and 123–141 to interact with Sir4, and loss of these residues had no effect on interaction with Dhr2 and Utp22. Finally, Ubp10 required residues 171–208 to interact with Utp22, and loss of these residues had no effect on interaction with Dhr2 and Sir4. Thus, each of the three representative Ubp10 interactions is defined by its own unique binding module within Ubp10's N-terminal IDR.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":109,"end":141,"reference_id":"26149687","reference_source":"pmid","reference_html":"A Conserved Deubiquitinating Enzyme Uses Intrinsically Disordered Regions to Scaffold Multiple Protein Interaction Sites. <i> Reed BJ, Locke MN, Gardner RG. </i> J Biol Chem, 2015","date":"2024-02-08T14:18:36.134Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0693","term_name":"Gal4 DNA-binding domain tag","term_namespace":"Tag","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"Yeast cells expressing fusions of the Gal4-binding domain (GBD) with Ubp10 or USP36 containing the indicated mutations and the appropriate protein fusions to the Gal4 activation domain (GAD) were spotted onto selective (synthetic medium minus histidine) and nonselective (synthetic medium plus histidine) media to assess interactions and spotting efficiency, respectively."}]},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ile109Ser122del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Thr123Gln141del","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P11978","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01189r011","statement":[{"text":"Residues 2–27 in Ubp10 were required to interact with Dhr2, and loss of these residues did not affect the interaction with Sir4 or Utp22. Likewise, Ubp10 required residues 109–122 and 123–141 to interact with Sir4, and loss of these residues had no effect on interaction with Dhr2 and Utp22. Finally, Ubp10 required residues 171–208 to interact with Utp22, and loss of these residues had no effect on interaction with Dhr2 and Sir4. Thus, each of the three representative Ubp10 interactions is defined by its own unique binding module within Ubp10's N-terminal IDR.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":2,"end":27,"reference_id":"26149687","reference_source":"pmid","reference_html":"A Conserved Deubiquitinating Enzyme Uses Intrinsically Disordered Regions to Scaffold Multiple Protein Interaction Sites. <i> Reed BJ, Locke MN, Gardner RG. </i> J Biol Chem, 2015","date":"2024-02-08T14:19:11.965Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0693","term_name":"Gal4 DNA-binding domain tag","term_namespace":"Tag","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"Yeast cells expressing fusions of the Gal4-binding domain (GBD) with Ubp10 or USP36 containing the indicated mutations and the appropriate protein fusions to the Gal4 activation domain (GAD) were spotted onto selective (synthetic medium minus histidine) and nonselective (synthetic medium plus histidine) media to assess interactions and spotting efficiency, respectively."}]},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Thr2Ser27del","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P36009","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01189r012","statement":[{"text":"Residues 2–27 in Ubp10 were required to interact with Dhr2, and loss of these residues did not affect the interaction with Sir4 or Utp22. Likewise, Ubp10 required residues 109–122 and 123–141 to interact with Sir4, and loss of these residues had no effect on interaction with Dhr2 and Utp22. Finally, Ubp10 required residues 171–208 to interact with Utp22, and loss of these residues had no effect on interaction with Dhr2 and Sir4. Thus, each of the three representative Ubp10 interactions is defined by its own unique binding module within Ubp10's N-terminal IDR.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":109,"end":141,"reference_id":"26149687","reference_source":"pmid","reference_html":"A Conserved Deubiquitinating Enzyme Uses Intrinsically Disordered Regions to Scaffold Multiple Protein Interaction Sites. <i> Reed BJ, Locke MN, Gardner RG. </i> J Biol Chem, 2015","date":"2024-02-08T14:32:08.870Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031509","term_name":"subtelomeric heterochromatin assembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ile109Gln141del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP01189r013","statement":[{"text":"Only the Ubp10 mutant lacking the residues required for Sir4 interaction resulted in loss of telomere chromatin silencing equivalent to the loss of silencing resulting from deletion of UBP10 (ubp10Δ) (Fig. 4D). Thus, the Ubp10-binding module for Sir4 is not only required to coordinate the Ubp10-Sir4 interaction, but is also required to direct Ubp10's functional role in telomere chromatin silencing.","type":"Results"}],"term_comment":"","term_def":"\"The assembly of chromatin into heterochromatin at the subtelomeric region, resulting in a chromatin conformation refractory to transcription.\" [GOC:mah, PMID:10219245, PMID:26205977]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_P53874","date":"2018-06-29T14:56:53.000Z","acc":"P53874","name":"Ubiquitin carboxyl-terminal hydrolase 10","length":792,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000005309D","genes":[{"name":{"value":"UBP10"},"synonyms":[{"value":"DOT4","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9755194","url":"http://www.ncbi.nlm.nih.gov/pubmed/9755194","alternativeUrl":"https://europepmc.org/abstract/MED/9755194"}}]}],"orfNames":[{"value":"N1619"}],"olnNames":[{"value":"YNL186W"}]}],"alphafold_very_low_content":0.48484848484848486,"disorder_content":0.5328282828282829,"disprot_consensus":{"full":[{"start":1,"end":359,"type":"D"},{"start":730,"end":792,"type":"D"}],"Structural state":[{"start":1,"end":359,"type":"D"},{"start":730,"end":792,"type":"D"}],"Molecular function":[{"start":2,"end":27,"type":"F"},{"start":109,"end":145,"type":"F"},{"start":167,"end":208,"type":"F"}],"Biological process":[{"start":109,"end":141,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MSSNAGEWCLMESDPGVFTELIKGFGCRGAQVEEIWSLEPESFEKLKPVHGLIFLFKWQPGEEPAGSVVQDSRLETIFFAKQVINNACATQAIVSVLLNCTHQDVHLGETLSEFKEFSQSFDAAMKGLALSNSDVIRQVHNSFARQQMFEFDTKTPAKEEDAFHFVSYVPVNGRLYELDGLREGPIDLGACNQDDWITAVRPVIEKRIQKYSEGEIRFNLMAIVSDRKMIYEQKIAELQRQLAEEPMDTDQGSTVLSAIQSEVARNQMLIEEEVQKLKRYKIENIRRKHNYLPFIMELLKTLAEHQQLIPLVEKAKEKQNAKKAQETK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"","disprot_id":"DP01190","ncbi_taxon_id":10090,"regions_counter":1,"creator":"mguha","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":160,"region_id":"DP01190r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for the activation and inhibition of the UCH37 deubiquitylase. <i> Vander Linden RT, Hemmis CW, Schmitt B, Ndoja A, Whitby FG, Robinson H, Cohen RE, Yao T, Hill CP. </i> Mol Cell, 2015","term_id":"IDPO:0000002","curator_id":"mguha","start":151,"term_ontology":"IDPO","curator_name":"Mainak Guharoy","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4WLR"}],"reference_id":"25702872","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"","date":"2018-06-29T15:26:40.000Z","acc":"Q9WUP7-2","name":"Isoform 2 of Ubiquitin carboxyl-terminal hydrolase isozyme L5","length":328,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000018AF","genes":[{"name":{"value":"Uchl5"},"synonyms":[{"value":"Uch37"}]}],"disorder_content":0.03048780487804878,"disprot_consensus":{"full":[{"start":151,"end":160,"type":"D"}],"Structural state":[{"start":151,"end":160,"type":"D"}]}},{"features":{"pfam":[{"id":"PF05160","name":"DSS1/SEM1 family","start":7,"end":65}]},"uniref50":"UniRef50_O14140","sequence":"MSRAALPSLENLEDDDEFEDFATENWPMKDTELDTGDDTLWENNWDDEDIGDDDFSVQLQAELKKKGVAAN","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"uniref90":"UniRef90_O14140","disprot_id":"DP01191","ncbi_taxon_id":284812,"regions_counter":8,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":54,"region_id":"DP01191r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Dss1 is a 26S proteasome ubiquitin receptor. <i> Paraskevopoulos K, Kriegenburg F, Tatham MH, Rösner HI, Medina B, Larsen IB, Brandstrup R, Hardwick KG, Hay RT, Kragelund BB, Hartmann-Petersen R, Gordon C. </i> Mol Cell, 2014","statement":[{"text":"Figure 2D. Calpha secondary chemical shifts of Dss1 confirm the predominantly disordered structure.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"mguha","start":1,"term_ontology":"IDPO","curator_name":"Mainak Guharoy","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"25306921","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":54,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Dss1 is a 26S proteasome ubiquitin receptor. <i> Paraskevopoulos K, Kriegenburg F, Tatham MH, Rösner HI, Medina B, Larsen IB, Brandstrup R, Hardwick KG, Hay RT, Kragelund BB, Hartmann-Petersen R, Gordon C. </i> Mol Cell, 2014","statement":[{"text":"Dss1 is intrinsically disordered with a single, transiently populated alpha helix from F55 through K66.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"mguha","start":1,"term_ontology":"IDPO","curator_name":"Mainak Guharoy","reference_id":"25306921","version":2,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01191r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":54,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Dss1 is a 26S proteasome ubiquitin receptor. <i> Paraskevopoulos K, Kriegenburg F, Tatham MH, Rösner HI, Medina B, Larsen IB, Brandstrup R, Hardwick KG, Hay RT, Kragelund BB, Hartmann-Petersen R, Gordon C. </i> Mol Cell, 2014","statement":[{"text":"Titration analyses with increasing amounts of ubiquitin disclosed the strongest binding to ubiquitin by binding site I (UBS-I), which is located at D38-D49 and disclosed the second and weakest site, UBS-II, located at D16-N25.","type":"Results"}],"term_id":"GO:0005515","curator_id":"mguha","start":1,"term_ontology":"GO","curator_name":"Mainak Guharoy","reference_id":"25306921","version":3,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01191r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":54,"reference_id":"30355493","reference_source":"pmid","reference_html":"Expanded Interactome of the Intrinsically Disordered Protein Dss1. <i> Schenstrøm SM, Rebula CA, Tatham MH, Hendus-Altenburger R, Jourdain I, Hay RT, Kragelund BB, Hartmann-Petersen R. </i> Cell Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01191r004","statement":[{"text":"Comparison of the NMR peak intensities of 15N-Dss1-N71C with and without MTSL indicated transient long-range effects from the C-terminal spin label (N71C) to regions >30 residues away. Thus, the C terminus was observed to be close to binding site I (BS-I) as well as to the linker between BS-I and BS-II (Figures 1C and S1C).","type":"Results"},{"text":"Because the PREs, the chemical shifts effects, and the population of the helix are all less than maximal, the helix of Dss1 is not tightly anchored but rather forms a “cloud” that dynamically shields access to the helix itself and to BS-I (Figure 1E). Such equilibrium between open and closed conformations may have consequences for how, and to which extent, the binding sites in Dss1 are available.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":54,"reference_id":"30355493","reference_source":"pmid","reference_html":"Expanded Interactome of the Intrinsically Disordered Protein Dss1. <i> Schenstrøm SM, Rebula CA, Tatham MH, Hendus-Altenburger R, Jourdain I, Hay RT, Kragelund BB, Hartmann-Petersen R. </i> Cell Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001582","ec_ontology":"ECO","ec_name":"liquid chromatography coupled with tandem mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01191r005","statement":[{"text":"For wild-type Dss1, GFP-Dss1 preparations were enriched in 263 proteins (Figure S3B).","type":"Results"},{"text":"Comparison of the GFP-Dss1 and GFP-Dss1Δhelix interactomes revealed that most interactions (Figures S3D–S3F) occurred independently of the helix (Figure 2D, green points). This agrees with previous reports that most binding to Dss1 is confined to the disordered region (Kragelund et al., 2016).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-07T12:58:49.450Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":54,"reference_id":"34439840","reference_source":"pmid","reference_html":"Insight into Calcium-Binding Motifs of Intrinsically Disordered Proteins. <i> Newcombe EA, Fernandes CB, Lundsgaard JE, Brakti I, Lindorff-Larsen K, Langkilde AE, Skriver K, Kragelund BB. </i> Biomolecules, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"ChEBI","id":"3312","partner_start":null,"partner_end":null}],"region_id":"DP01191r006","statement":[{"text":"We included the highly multispecific yeast protein DSS1wt, which has a high κ-value, indicating regions of repetitive charged residues of the same charge. In this case, we found two regions of higher CSPs, one between residues S8 to D14, and one between residues T39 to N43 (Figure 1D). Although these regions had the highest CSP, we observed generally high CSPs throughout the protein, i.e., S8–D14, D18–E32, and T39–N43. ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-07T13:11:26.933Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":54,"reference_id":"34439840","reference_source":"pmid","reference_html":"Insight into Calcium-Binding Motifs of Intrinsically Disordered Proteins. <i> Newcombe EA, Fernandes CB, Lundsgaard JE, Brakti I, Lindorff-Larsen K, Langkilde AE, Skriver K, Kragelund BB. </i> Biomolecules, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007740","ec_ontology":"ECO","ec_name":"small molecule detection assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"ChEBI","id":"3312","partner_start":null,"partner_end":null}],"region_id":"DP01191r007","statement":[{"text":"DSS1wt binds calcium at a higher ratio of 1:4 (Figure 1G,I), which may cause overlap within the regions with high CSPs. The overall affinity of DSS1wt for calcium was measured to be ~70 μM (Figure 1H). ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-07T13:11:23.767Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":54,"reference_id":"34439840","reference_source":"pmid","reference_html":"Insight into Calcium-Binding Motifs of Intrinsically Disordered Proteins. <i> Newcombe EA, Fernandes CB, Lundsgaard JE, Brakti I, Lindorff-Larsen K, Langkilde AE, Skriver K, Kragelund BB. </i> Biomolecules, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"IDPO:0000019","term_name":"disorder to pre-molten globule","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01191r008","statement":[{"text":"We next acquired DOSY spectra for DSS1wt and its mutants, finding that both DSS1wt and DSS1D became more compact upon calcium binding (25.7% and 17.6%, respectively).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-07T13:10:48.005Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_O14140","date":"2018-06-29T15:44:48.000Z","acc":"O14140","name":"26S proteasome complex subunit rpn15","length":71,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","dataset":[],"UniParc":"UPI000006B2C1","genes":[{"name":{"value":"rpn15"},"synonyms":[{"value":"dss1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15990877","url":"http://www.ncbi.nlm.nih.gov/pubmed/15990877","alternativeUrl":"https://europepmc.org/abstract/MED/15990877"}}]},{"value":"sem1"}],"orfNames":[{"value":"SPAC3G6.02","evidences":[{"code":"ECO:0000312","source":{"name":"PomBase","id":"SPAC3G6.02","url":""}}]}]}],"alphafold_very_low_content":0.056338028169014086,"disorder_content":0.7605633802816901,"disprot_consensus":{"full":[{"start":1,"end":54,"type":"T"}],"Structural state":[{"start":1,"end":54,"type":"D"}],"Structural transition":[{"start":1,"end":54,"type":"T"}],"Molecular function":[{"start":1,"end":54,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02809","name":"Ubiquitin interaction motif","start":212,"end":227},{"id":"PF02809","name":"Ubiquitin interaction motif","start":282,"end":297},{"id":"PF13519","name":"von Willebrand factor type A domain","start":6,"end":114}],"gene3D":[{"start":3,"end":185,"id":"3.40.50.410","name":"von Willebrand factor, type A domain"},{"start":261,"end":307,"id":"1.10.10.890","name":"1.10.10.890"}]},"uniref50":"UniRef50_P55036","sequence":"MVLESTMVCVDNSEYMRNGDFLPTRLQAQQDAVNIVCHSKTRSNPENNVGLITLANDCEVLTTLTPDTGRILSKLHTVQPKGKITFCTGIRVAHLALKHRQGKNHKMRIIAFVGSPVEDNEKDLVKLAKRLKKEKVNVDIINFGEEEVNTEKLTAFVNTLNGKDGTGSHLVTVPPGPSLADALISSPILAGEGGAMLGLGASDFEFGVDPSADPELALALRVSMEEQRQRQEEEARRAAAASAAEAGIATTGTEDSDDALLKMTISQQEFGRTGLPDLSSMTEEEQIAYAMQMSLQGAEFGQAESADIDASSAMDTSEPAKEEDDYDVMQDPEFLQSVLENLPGVDPNNEAIRNAMGSLASQATKDGKKDKKEEDKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P55036","disprot_id":"DP01192","ncbi_taxon_id":9606,"regions_counter":19,"creator":"mpajkos","regions":[{"region_id":"DP01192r001","validated":{"curator_id":"ahatos","timestamp":"2020-11-30T16:23:20.100Z","curator_name":"András Hatos"},"ec_ontology":"ECO","end":256,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":246,"version":3,"statement":[{"text":"S5a (196-306) contains three a-helices that are connected by flexible regions.","type":"Figure"},{"text":"S5a (196-306) contains three well-structured regions spanning residues P214-E245, D257-E269, and L278-Q296 (Figure 1(b)–(e)). Flexible, randomly coiled linker regions connect the structured elements and prevent them from being defined relative to each other. This lack of higher-order structure within these regions is supported by their chemical-shift assignments,26 lack of long-range nuclear Overhauser effect (NOE) interactions, and NMR relaxation data (data not shown).","type":"Results"},{"text":"Between the UIMs of S5a is a second α-helix with flexible linker regions at either end (Figure 1).","type":"Discussion"}],"term_name":"disorder","reference_html":"Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition. <i> Wang Q, Young P, Walters KJ. </i> J Mol Biol, 2005","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15826667","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1YX4"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"fquaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":256,"term_name":"flexible linker","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structure of S5a bound to monoubiquitin provides a model for polyubiquitin recognition. <i> Wang Q, Young P, Walters KJ. </i> J Mol Biol, 2005","statement":[{"text":"S5a (196-306) contains three well-structured regions spanning residues P214-E245, D257-E269, and L278-Q296 (Figure 1(b)–(e)). Flexible, randomly coiled linker regions connect the structured elements and prevent them from being defined relative to each other. This lack of higher-order structure within these regions is supported by their chemical-shift assignments,26 lack of long-range nuclear Overhauser effect (NOE) interactions, and NMR relaxation data (data not shown).","type":"Results"},{"text":"Between the UIMs of S5a is a second α-helix with flexible linker regions at either end (Figure 1).","type":"Discussion"}],"term_id":"IDPO:0000033","curator_id":"fquaglia","start":246,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15826667","version":4,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","validated":{"curator_id":"ahatos","timestamp":"2020-11-30T16:23:25.122Z","curator_name":"András Hatos"},"region_id":"DP01192r002","ec_go":"EXP","disprot_namespace":"Disorder function"},{"region_id":"DP01192r005","validated":{"curator_id":"fquaglia","timestamp":"2020-11-27T14:55:18.568Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":377,"term_id":"IDPO:0000002","start":305,"version":2,"statement":[{"text":"Here, we identify a region at the C-terminal end of hRpn10 that forms a binding site in the proteasome for E6AP. By using biophysical techniques including NMR spectroscopy, we find this region to be disordered when unbound","type":"Introduction"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0001-5791-9825","released":"2022_03","term_ontology":"IDPO","curator_name":"Mátyás Pajkos","reference_id":"32157086","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6U19"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"mpajkos","reference_html":"Structure of E3 ligase E6AP with a proteasome-binding site provided by substrate receptor hRpn10. <i> Buel GR, Chen X, Chari R, O'Neill MJ, Ebelle DL, Jenkins C, Sridharan V, Tarasov SG, Tarasova NI, Andresson T, Walters KJ. </i> Nat Commun, 2020","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP01192r006","validated":{"curator_id":"fquaglia","timestamp":"2020-11-30T09:50:38.383Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":341,"term_id":"IDPO:0000011","start":332,"version":3,"statement":[{"text":"Comparisons of our NMR data acquired on free and AZUL-bound RAZUL indicate that RAZUL acquires helicity upon binding to AZUL. Carbonyl and Cα values when compared with random coil taking into account amino acid type yields a chemical shift index (CSI) that informs on secondary structure; these values shift to reflect greater helicity for RAZUL when bound to AZUL (Fig. 5c and Supplementary Fig. 6b). Moreover, intramolecular interactions characteristic of helicity were observed following AZUL addition, but not for free RAZUL (Supplementary Fig. 6c, d). Overall, our NMR data indicate that RAZUL switches from a poorly ordered state to a well-defined helical state following AZUL binding.","type":"Results"}],"term_name":"disorder to order","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0001-5791-9825","released":"2022_03","term_ontology":"IDPO","curator_name":"Mátyás Pajkos","reference_id":"32157086","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6U19"}],"term_namespace":"Structural transition","ec_id":"ECO:0006165","curator_id":"mpajkos","reference_html":"Structure of E3 ligase E6AP with a proteasome-binding site provided by substrate receptor hRpn10. <i> Buel GR, Chen X, Chari R, O'Neill MJ, Ebelle DL, Jenkins C, Sridharan V, Tarasov SG, Tarasova NI, Andresson T, Walters KJ. </i> Nat Commun, 2020","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP01192r007","validated":{"curator_id":"fquaglia","timestamp":"2020-11-27T14:55:45.803Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":361,"term_id":"GO:0060090","start":328,"version":3,"statement":[{"text":"RAZUL binds the AZUL helices from the opposite direction compared with the Zn finger. In this complex, two α-helices are formed in RAZUL that span P332–N341 (α1) and E350–S361 (α2). Directly N-terminal to RAZUL α1 is a single turn of a 3 10 -helix that spans V328-Q330.\nRAZUL α1 is centered between the two AZUL helices by hydrophobic interactions involving F334, L335, V338, and L339 as well as L342 and V345 from the RAZUL α1/ α2 loop. From the 3 10 -helix, V328 and M329 form hydrophobic interactions. RAZUL α2 is more peripheral compared with α1, with A351, I352, A355, M356, and L359.","type":"Results"}],"term_name":"molecular adaptor activity","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0001-5791-9825","released":"2022_03","term_ontology":"GO","curator_name":"Mátyás Pajkos","reference_id":"32157086","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6U19"}],"term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"mpajkos","reference_html":"Structure of E3 ligase E6AP with a proteasome-binding site provided by substrate receptor hRpn10. <i> Buel GR, Chen X, Chari R, O'Neill MJ, Ebelle DL, Jenkins C, Sridharan V, Tarasov SG, Tarasova NI, Andresson T, Walters KJ. </i> Nat Commun, 2020","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01192r008","validated":{"curator_id":"fquaglia","timestamp":"2020-11-30T11:31:48.095Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":361,"term_id":"GO:0005515","start":328,"version":3,"statement":[{"text":"E6AP AZUL binds to hRpn10 RAZUL at the proteasome.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q05086","partner_end":null}],"term_name":"protein binding","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0001-5791-9825","released":"2022_03","term_ontology":"GO","curator_name":"Mátyás Pajkos","reference_id":"32157086","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6U19"}],"term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"mpajkos","reference_html":"Structure of E3 ligase E6AP with a proteasome-binding site provided by substrate receptor hRpn10. <i> Buel GR, Chen X, Chari R, O'Neill MJ, Ebelle DL, Jenkins C, Sridharan V, Tarasov SG, Tarasova NI, Andresson T, Walters KJ. </i> Nat Commun, 2020","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01192r009","validated":{"curator_id":"fquaglia","timestamp":"2020-11-30T09:47:50.546Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":361,"term_id":"IDPO:0000011","start":350,"version":2,"statement":[{"text":"Comparisons of our NMR data acquired on free and AZUL-bound RAZUL indicate that RAZUL acquires helicity upon binding to AZUL. Carbonyl and Cα values when compared with random coil taking into account amino acid type yields a chemical shift index (CSI) that informs on secondary structure; these values shift to reflect greater helicity for RAZUL when bound to AZUL (Fig. 5c and Supplementary Fig. 6b). Moreover, intramolecular interactions characteristic of helicity were observed following AZUL addition, but not for free RAZUL (Supplementary Fig. 6c, d). Overall, our NMR data indicate that RAZUL switches from a poorly ordered state to a well-defined helical state following AZUL binding.","type":"Results"}],"term_name":"disorder to order","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0001-5791-9825","released":"2022_03","term_ontology":"IDPO","curator_name":"Mátyás Pajkos","reference_id":"32157086","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6U19"}],"term_namespace":"Structural transition","ec_id":"ECO:0006165","curator_id":"mpajkos","reference_html":"Structure of E3 ligase E6AP with a proteasome-binding site provided by substrate receptor hRpn10. <i> Buel GR, Chen X, Chari R, O'Neill MJ, Ebelle DL, Jenkins C, Sridharan V, Tarasov SG, Tarasova NI, Andresson T, Walters KJ. </i> Nat Commun, 2020","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP01192r010","validated":{"curator_id":"fquaglia","timestamp":"2020-11-30T09:57:39.618Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":377,"term_id":"IDPO:0000011","start":305,"version":2,"statement":[{"text":"CD measurements indicated 7% and 46% helicity, respectively, for unbound RAZUL (blue) and AZUL (green), and a theoretical spectrum (gray dashed line) for the mixture with markedly less spectral features of helicity compared with the recorded experimental spectrum (orange, Fig. 5d). Overall, 35% helicity is indicated from the experimental CD data recorded on the complex, consistent with the 36% helicity determined by NMR (Fig. 5b). The AZUL secondary structure is unaltered by binding to RAZUL (Supplementary Fig. 6a), leading us to conclude that the observed difference between the theoretical and experimental CD spectra reflects increased helicity for RAZUL, consistent with the NMR data (for example, Fig. 5c).","type":"Results"}],"term_name":"disorder to order","ec_name":"circular dichroism evidence used in manual assertion","curator_orcid":"0000-0001-5791-9825","released":"2022_03","term_ontology":"IDPO","curator_name":"Mátyás Pajkos","reference_id":"32157086","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural transition","ec_id":"ECO:0006200","curator_id":"mpajkos","reference_html":"Structure of E3 ligase E6AP with a proteasome-binding site provided by substrate receptor hRpn10. <i> Buel GR, Chen X, Chari R, O'Neill MJ, Ebelle DL, Jenkins C, Sridharan V, Tarasov SG, Tarasova NI, Andresson T, Walters KJ. </i> Nat Commun, 2020","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP01192r011","validated":{"curator_id":"fquaglia","timestamp":"2020-11-30T10:08:50.897Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":377,"term_id":"IDPO:0000002","start":305,"version":2,"statement":[{"text":"CD measurements indicated 7% and 46% helicity, respectively, for unbound RAZUL (blue) and AZUL (green), and a theoretical spectrum (gray dashed line) for the mixture with markedly less spectral features of helicity compared with the recorded experimental spectrum (orange, Fig. 5d). Overall, 35% helicity is indicated from the experimental CD data recorded on the complex, consistent with the 36% helicity determined by NMR (Fig. 5b). The AZUL secondary structure is unaltered by binding to RAZUL (Supplementary Fig. 6a), leading us to conclude that the observed difference between the theoretical and experimental CD spectra reflects increased helicity for RAZUL, consistent with the NMR data (for example, Fig. 5c).","type":"Results"}],"term_name":"disorder","ec_name":"circular dichroism evidence used in manual assertion","curator_orcid":"0000-0001-5791-9825","released":"2022_03","term_ontology":"IDPO","curator_name":"Mátyás Pajkos","reference_id":"32157086","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006200","curator_id":"mpajkos","reference_html":"Structure of E3 ligase E6AP with a proteasome-binding site provided by substrate receptor hRpn10. <i> Buel GR, Chen X, Chari R, O'Neill MJ, Ebelle DL, Jenkins C, Sridharan V, Tarasov SG, Tarasova NI, Andresson T, Walters KJ. </i> Nat Commun, 2020","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP01192r012","validated":{"curator_id":"fquaglia","timestamp":"2020-11-30T10:27:00.484Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":377,"term_id":"GO:0060090","start":305,"version":3,"statement":[{"text":"CD measurements indicated 7% and 46% helicity, respectively, for unbound RAZUL (blue) and AZUL (green), and a theoretical spectrum (gray dashed line) for the mixture with markedly less spectral features of helicity compared with the recorded experimental spectrum (orange, Fig. 5d). Overall, 35% helicity is indicated from the experimental CD data recorded on the complex, consistent with the 36% helicity determined by NMR (Fig. 5b). The AZUL secondary structure is unaltered by binding to RAZUL (Supplementary Fig. 6a), leading us to conclude that the observed difference between the theoretical and experimental CD spectra reflects increased helicity for RAZUL, consistent with the NMR data (for example, Fig. 5c).","type":"Results"}],"term_name":"molecular adaptor activity","ec_name":"circular dichroism evidence used in manual assertion","curator_orcid":"0000-0001-5791-9825","released":"2022_03","term_ontology":"GO","curator_name":"Mátyás Pajkos","reference_id":"32157086","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006200","curator_id":"mpajkos","reference_html":"Structure of E3 ligase E6AP with a proteasome-binding site provided by substrate receptor hRpn10. <i> Buel GR, Chen X, Chari R, O'Neill MJ, Ebelle DL, Jenkins C, Sridharan V, Tarasov SG, Tarasova NI, Andresson T, Walters KJ. </i> Nat Commun, 2020","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01192r016","validated":{"curator_id":"fquaglia","timestamp":"2020-11-30T11:31:48.955Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":377,"term_id":"GO:0005515","start":305,"version":3,"statement":[{"text":"Expression of full-length (lane 7) but not RAZUL-truncated hRpn10 (lane 6) resulted in observable E6AP co-immunoprecipitation with proteasomes isolated from ΔRAZUL cells (Fig. 4a); we attribute the lower amounts of E6AP co-immunoprecipitated with proteasomes of hRpn10full-length-expressing ΔRAZUL cells to the reduced abundance of endogenous E6AP in this cell line, as described above (Fig. 2b). This experiment indicates that the hRpn10 RAZUL recruits E6AP to the proteasome.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q05086","partner_end":null}],"term_name":"protein binding","ec_name":"co-immunoprecipitation evidence used in manual assertion","curator_orcid":"0000-0001-5791-9825","released":"2022_03","term_ontology":"GO","curator_name":"Mátyás Pajkos","reference_id":"32157086","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006030","curator_id":"mpajkos","reference_html":"Structure of E3 ligase E6AP with a proteasome-binding site provided by substrate receptor hRpn10. <i> Buel GR, Chen X, Chari R, O'Neill MJ, Ebelle DL, Jenkins C, Sridharan V, Tarasov SG, Tarasova NI, Andresson T, Walters KJ. </i> Nat Commun, 2020","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01192r017","validated":{"curator_id":"fquaglia","timestamp":"2020-11-30T11:31:51.690Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":377,"term_id":"GO:0005515","start":305,"version":3,"statement":[{"text":"To assess the strength of hRpn10(305–377):AZUL interaction, we used isothermal titration calorimetry (ITC) with the AZUL added incrementally to hRpn10(305–377); a Kd value of 11.6 + 3.3 nM was measured (Fig. 1d and Supplementary Fig. 2f), indicating similar strength to hRpn13 interaction with the proteasome.\n","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q05086","partner_end":null}],"term_name":"protein binding","ec_name":"isothermal titration calorimetry evidence used in manual assertion","curator_orcid":"0000-0001-5791-9825","released":"2022_03","term_ontology":"GO","curator_name":"Mátyás Pajkos","reference_id":"32157086","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"mpajkos","reference_html":"Structure of E3 ligase E6AP with a proteasome-binding site provided by substrate receptor hRpn10. <i> Buel GR, Chen X, Chari R, O'Neill MJ, Ebelle DL, Jenkins C, Sridharan V, Tarasov SG, Tarasova NI, Andresson T, Walters KJ. </i> Nat Commun, 2020","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01192r018","validated":{"curator_id":"fquaglia","timestamp":"2020-11-30T11:31:53.565Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":377,"term_id":"GO:0005515","start":305,"version":3,"statement":[{"text":"Surface plasmon resonance (SPR) similarly revealed a Kd value of 8.1 + 1.4 nM for GST-hRpn10(305–377) binding to AZUL (Fig. 1d and Supplementary Fig. 2g).\n","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q05086","partner_end":null}],"term_name":"protein binding","ec_name":"surface plasmon resonance evidence used in manual assertion","curator_orcid":"0000-0001-5791-9825","released":"2022_03","term_ontology":"GO","curator_name":"Mátyás Pajkos","reference_id":"32157086","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001269","curator_id":"mpajkos","reference_html":"Structure of E3 ligase E6AP with a proteasome-binding site provided by substrate receptor hRpn10. <i> Buel GR, Chen X, Chari R, O'Neill MJ, Ebelle DL, Jenkins C, Sridharan V, Tarasov SG, Tarasova NI, Andresson T, Walters KJ. </i> Nat Commun, 2020","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01192r019","validated":{"curator_id":"fquaglia","timestamp":"2020-11-30T11:37:31.737Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":377,"term_id":"GO:0005515","start":305,"version":3,"statement":[{"text":"The AZUL secondary structure is unaltered by binding to RAZUL (Supplementary Fig. 6a), leading us to conclude that the observed difference between the theoretical and experimental CD spectra reflects increased helicity for RAZUL, consistent with the NMR data (for example, Fig. 5c).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q05086","partner_end":null}],"term_name":"protein binding","ec_name":"circular dichroism evidence used in manual assertion","curator_orcid":"0000-0001-5791-9825","released":"2022_03","term_ontology":"GO","curator_name":"Mátyás Pajkos","reference_id":"32157086","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006200","curator_id":"mpajkos","reference_html":"Structure of E3 ligase E6AP with a proteasome-binding site provided by substrate receptor hRpn10. <i> Buel GR, Chen X, Chari R, O'Neill MJ, Ebelle DL, Jenkins C, Sridharan V, Tarasov SG, Tarasova NI, Andresson T, Walters KJ. </i> Nat Commun, 2020","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P55036","date":"2018-06-29T16:53:48.000Z","acc":"P55036","name":"26S proteasome non-ATPase regulatory subunit 4","length":377,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000038DA5","genes":[{"name":{"value":"PSMD4"},"synonyms":[{"value":"MCB1"}]}],"alphafold_very_low_content":0.1883289124668435,"disorder_content":0.22281167108753316,"disprot_consensus":{"full":[{"start":246,"end":256,"type":"D"},{"start":305,"end":377,"type":"T"}],"Structural state":[{"start":246,"end":256,"type":"D"},{"start":305,"end":377,"type":"D"}],"Disorder function":[{"start":246,"end":256,"type":"F"}],"Structural transition":[{"start":305,"end":377,"type":"T"}],"Molecular function":[{"start":305,"end":377,"type":"F"}]}},{"features":{"pfam":[{"id":"PF08839","name":"DNA replication factor CDT1 like","start":186,"end":349},{"id":"PF16679","name":"DNA replication factor Cdt1 C-terminal domain","start":421,"end":516}],"gene3D":[{"start":408,"end":545,"id":"1.10.10.1420","name":"DNA replication factor Cdt1, C-terminal WH domain"}]},"uniref50":"UniRef50_Q9H211","sequence":"MEQRRVTDFFARRRPGPPRIAPPKLACRTPSPARPALRAPASATSGSRKRARPPAAPGRDQARPPARRRLRLSVDEVSSPSTPEAPDIPACPSPGQKIKKSTPAAGQPPHLTSAQDQDTISELASCLQRARELGARVRALKASAQDAGESCTPEAEGRPEEPCGEKAPAYQRFHALAQPGLPGLVLPYKYQVLAEMFRSMDTIVGMLHNRSETPTFAKVQRGVQDMMRRRFEECNVGQIKTVYPASYRFRQERSVPTFKDGTRRSDYQLTIEPLLEQEADGAAPQLTASRLLQRRQIFSQKLVEHVKEHHKAFLASLSPAMVVPEDQLTRWHPRFNVDEVPDIEPAALPQPPATEKLTTAQEVLARARNLISPRMEKALSQLALRSAAPSSPGSPRPALPATPPATPPAASPSALKGVSQDLLERIRAKEAQKQLAQMTRCPEQEQRLQRLERLPELARVLRSVFVSERKPALSMEVACARMVGSCCTIMSPGEMEKHLLLLSELLPDWLSLHRIRTDTYVKLDKAADLAHITARLAHQTRAEEGL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9H211","disprot_id":"DP01193","ncbi_taxon_id":9606,"regions_counter":10,"creator":"eficho","regions":[{"start":92,"end":159,"reference_id":"38260441","reference_source":"pmid","reference_html":"SAXS/MC studies of the mixed-folded protein Cdt1 reveal monomeric, folded over conformations. <i> Smith KP, Chakravarthy S, Rahi A, Chakraborty M, Vosberg KM, Tonelli M, Plach MG, Grigorescu AA, Curtis JE, Varma D. </i> bioRxiv, 2024","date":"2024-10-09T08:30:56.952Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP01193r008","statement":[{"text":"We used Dynamic Light Scattering (DLS) to estimate the radius of hydration (R(h)) as well as polydispersity of Cdt1 in solution. Ovalbumin showed similar R(h) values in our system as with published results (60). For Cdt1, DLS demonstrated the protein was 99% monomeric, had a calculated R(h) of 3.7 nm, and was 40% polydisperse (Figure 3A). This relatively high level of polydispersity is consistent with a mixed-folded protein with many different conformations and also is consistent with thermally instability at relatively low temperatures (61).","type":"Results"},{"text":"We used both circular dichroism (CD) and intrinsic fluorescence (Ex280, Em330/350) to measure the changes in secondary and tertiary elements, respectively. Our thermal stability data for ovalbumin (Figure 2B & 2C) was similar to previously published data (48) given the difference in buffers (Table 1 & 2). For both DSF and DSCD, Cdt1 followed a simple two-state unfolding process. In fluorescence detection, we observed a melting temperature (Tm) of 43 °C (Figure 2B). In CD, we calculated a Tm of 42 °C (Figure 2C).","type":"Results"},{"text":"We also performed 1H/15N HSQC NMR to validate our CD results. The number of peaks, their broadness and their location similarly demonstrate a high disorder content (56). This data confirms all but the WH domains are disordered in human Cdt1.","type":"Results"},{"text":"Using our experimental secondary structure content analysis, we defined the N-terminal and linker regions as entirely flexible.","type":"Results"},{"text":"The authors define the WH domains as those spanning the residues 159-356 and 410-546.","type":"Curator statement"}]},{"start":356,"end":410,"reference_id":"38260441","reference_source":"pmid","reference_html":"SAXS/MC studies of the mixed-folded protein Cdt1 reveal monomeric, folded over conformations. <i> Smith KP, Chakravarthy S, Rahi A, Chakraborty M, Vosberg KM, Tonelli M, Plach MG, Grigorescu AA, Curtis JE, Varma D. </i> bioRxiv, 2024","date":"2024-10-09T08:31:20.177Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP01193r009","statement":[{"text":"We used Dynamic Light Scattering (DLS) to estimate the radius of hydration (R(h)) as well as polydispersity of Cdt1 in solution. Ovalbumin showed similar R(h) values in our system as with published results (60). For Cdt1, DLS demonstrated the protein was 99% monomeric, had a calculated R(h) of 3.7 nm, and was 40% polydisperse (Figure 3A). This relatively high level of polydispersity is consistent with a mixed-folded protein with many different conformations and also is consistent with thermally instability at relatively low temperatures (61).","type":"Results"},{"text":"We used both circular dichroism (CD) and intrinsic fluorescence (Ex280, Em330/350) to measure the changes in secondary and tertiary elements, respectively. Our thermal stability data for ovalbumin (Figure 2B & 2C) was similar to previously published data (48) given the difference in buffers (Table 1 & 2). For both DSF and DSCD, Cdt1 followed a simple two-state unfolding process. In fluorescence detection, we observed a melting temperature (Tm) of 43 °C (Figure 2B). In CD, we calculated a Tm of 42 °C (Figure 2C).","type":"Results"},{"text":"We also performed 1H/15N HSQC NMR to validate our CD results. The number of peaks, their broadness and their location similarly demonstrate a high disorder content (56). This data confirms all but the WH domains are disordered in human Cdt1.","type":"Results"},{"text":"Using our experimental secondary structure content analysis, we defined the N-terminal and linker regions as entirely flexible.","type":"Results"},{"text":"The authors define the WH domains as those spanning the residues 159-356 and 410-546.","type":"Curator statement"}]},{"start":356,"end":410,"reference_id":"38260441","reference_source":"pmid","reference_html":"SAXS/MC studies of the mixed-folded protein Cdt1 reveal monomeric, folded over conformations. <i> Smith KP, Chakravarthy S, Rahi A, Chakraborty M, Vosberg KM, Tonelli M, Plach MG, Grigorescu AA, Curtis JE, Varma D. </i> bioRxiv, 2024","date":"2024-10-09T08:32:07.376Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP01193r010","statement":[{"text":"We used Dynamic Light Scattering (DLS) to estimate the radius of hydration (R(h)) as well as polydispersity of Cdt1 in solution. Ovalbumin showed similar R(h) values in our system as with published results (60). For Cdt1, DLS demonstrated the protein was 99% monomeric, had a calculated R(h) of 3.7 nm, and was 40% polydisperse (Figure 3A). This relatively high level of polydispersity is consistent with a mixed-folded protein with many different conformations and also is consistent with thermally instability at relatively low temperatures (61).","type":"Results"},{"text":"We used both circular dichroism (CD) and intrinsic fluorescence (Ex280, Em330/350) to measure the changes in secondary and tertiary elements, respectively. Our thermal stability data for ovalbumin (Figure 2B & 2C) was similar to previously published data (48) given the difference in buffers (Table 1 & 2). For both DSF and DSCD, Cdt1 followed a simple two-state unfolding process. In fluorescence detection, we observed a melting temperature (Tm) of 43 °C (Figure 2B). In CD, we calculated a Tm of 42 °C (Figure 2C).","type":"Results"},{"text":"We also performed 1H/15N HSQC NMR to validate our CD results. The number of peaks, their broadness and their location similarly demonstrate a high disorder content (56). This data confirms all but the WH domains are disordered in human Cdt1.","type":"Results"},{"text":"Using our experimental secondary structure content analysis, we defined the N-terminal and linker regions as entirely flexible.","type":"Results"},{"text":"The authors define the WH domains as those spanning the residues 159-356 and 410-546.","type":"Curator statement"}]}],"released":"2018_11","uniref100":"UniRef100_Q9H211","date":"2018-07-01T09:52:51.000Z","acc":"Q9H211","name":"DNA replication factor Cdt1","length":546,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI0000070A16","genes":[{"name":{"value":"CDT1","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAG45181.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAG45181.1"}}]}}],"alphafold_very_low_content":0.2600732600732601,"disorder_content":0.22527472527472528,"disprot_consensus":{"full":[{"start":92,"end":159,"type":"D"},{"start":356,"end":410,"type":"D"}],"Structural state":[{"start":92,"end":159,"type":"D"},{"start":356,"end":410,"type":"D"}],"Disorder function":[{"start":356,"end":410,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02516","name":"Oligosaccharyl transferase STT3, N-terminal","start":15,"end":417},{"id":"PF21436","name":"STT3/PglB/AglB core domain","start":511,"end":562}],"gene3D":[{"start":492,"end":641,"id":"3.40.50.12610","name":"3.40.50.12610"}]},"uniref50":"UniRef50_P39007","sequence":"MGSDRSCVLSVFQTILKLVIFVAIFGAAISSRLFAVIKFESIIHEFDPWFNYRATKYLVNNSFYKFLNWFDDRTWYPLGRVTGGTLYPGLMTTSAFIWHALRNWLGLPIDIRNVCVLFAPLFSGVTAWATYEFTKEIKDASAGLLAAGFIAIVPGYISRSVAGSYDNEAIAITLLMVTFMFWIKAQKTGSIMHATCAALFYFYMVSAWGGYVFITNLIPLHVFLLILMGRYSSKLYSAYTTWYAIGTVASMQIPFVGFLPIRSNDHMAALGVFGLIQIVAFGDFVKGQISTAKFKVIMMVSLFLILVLGVVGLSALTYMGLIAPWTGRFYSLWDTNYAKIHIPIIASVSEHQPVSWPAFFFDTHFLIWLFPAGVFLLFLDLKDEHVFVIAYSVLCSYFAGVMVRLMLTLTPVICVSAAVALSKIFDIYLDFKTSDRKYAIKPAALLAKLIVSGSFIFYLYLFVFHSTWVTRTAYSSPSVVLPSQTPDGKLALIDDFREAYYWLRMNSDEDSKVAAWWDYGYQIGGMADRTTLVDNNTWNNTHIAIVGKAMASPEEKSYEILKEHDVDYVLVIFGGLIGFGGDDINKFLWMIRISEGIWPEEIKERDFYTAEGEYRVDARASETMRNSLLYKMSYKDFPQLFNGGQATDRVRQQMITPLDVPPLDYFDEVFTSENWMVRIYQLKKDDAQGRTLRDVGELTRSSTKTRRSIKRPELGLRV","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P39007","disprot_id":"DP01195","ncbi_taxon_id":559292,"regions_counter":3,"creator":"stama","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":351,"region_id":"DP01195r001","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Structure of the yeast oligosaccharyltransferase complex gives insight into eukaryotic N-glycosylation. <i> Wild R, Kowal J, Eyring J, Ngwa EM, Aebi M, Locher KP. </i> Science, 2018","term_id":"IDPO:0000002","curator_id":"stama","start":299,"term_ontology":"IDPO","curator_name":"Stella Tamana","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29301962","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":351,"term_name":"disorder to order","released":"2022_03","ec_name":"cryogenic electron microscopy evidence used in manual assertion","reference_html":"Structure of the yeast oligosaccharyltransferase complex gives insight into eukaryotic N-glycosylation. <i> Wild R, Kowal J, Eyring J, Ngwa EM, Aebi M, Locher KP. </i> Science, 2018","term_id":"IDPO:0000011","curator_id":"stama","start":299,"term_ontology":"IDPO","curator_name":"Stella Tamana","reference_id":"29301962","version":2,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","region_id":"DP01195r002","ec_go":"IDA","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":351,"region_id":"DP01195r003","released":"2022_03","ec_id":"ECO:0006224","reference_html":"The atomic structure of a eukaryotic oligosaccharyltransferase complex. <i> Bai L, Wang T, Zhao G, Kovach A, Li H. </i> Nature, 2018","term_id":"IDPO:0000002","curator_id":"stama","start":299,"term_ontology":"IDPO","curator_name":"Stella Tamana","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29466327","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P39007","date":"2018-07-02T08:23:37.000Z","acc":"P39007","name":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3","length":718,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000168E6F","genes":[{"name":{"value":"STT3"},"olnNames":[{"value":"YGL022W"}]}],"alphafold_very_low_content":0.025069637883008356,"disorder_content":0.07381615598885793,"disprot_consensus":{"full":[{"start":299,"end":351,"type":"T"}],"Structural state":[{"start":299,"end":351,"type":"D"}],"Structural transition":[{"start":299,"end":351,"type":"T"}]}},{"features":{"pfam":[{"id":"PF04756","name":"OST3 / OST6 family, transporter family","start":27,"end":340}],"gene3D":[{"start":23,"end":191,"id":"3.40.30.10","name":"Glutaredoxin"}]},"uniref50":"UniRef50_P48439","sequence":"MNWLFLVSLVFFCGVSTHPALAMSSNRLLKLANKSPKKIIPLKDSSFENILAPPHENAYIVALFTATAPEIGCSLCLELESEYDTIVASWFDDHPDAKSSNSDTSIFFTKVNLEDPSKTIPKAFQFFQLNNVPRLFIFKPNSPSILDHSVISISTDTGSERMKQIIQAIKQFSQVNDFSLHLPMDWTPIITSTIITFITVLLFKKQSKLMFSIISSRIIWATLSTFFIICMISAYMFNQIRNTQLAGVGPKGEVMYFLPNEFQHQFAIETQVMVLIYGTLAALVVVLVKGIQFLRSHLYPETKKAYFIDAILASFCALFIYVFFAALTTVFTIKSPAYPFPLLRLSAPFK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P48439","disprot_id":"DP01196","ncbi_taxon_id":559292,"regions_counter":4,"creator":"stama","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":215,"region_id":"DP01196r001","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Structure of the yeast oligosaccharyltransferase complex gives insight into eukaryotic N-glycosylation. <i> Wild R, Kowal J, Eyring J, Ngwa EM, Aebi M, Locher KP. </i> Science, 2018","term_id":"IDPO:0000002","curator_id":"stama","start":23,"term_ontology":"IDPO","curator_name":"Stella Tamana","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29301962","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":215,"term_name":"disorder to order","released":"2022_03","ec_name":"cryogenic electron microscopy evidence used in manual assertion","reference_html":"Structure of the yeast oligosaccharyltransferase complex gives insight into eukaryotic N-glycosylation. <i> Wild R, Kowal J, Eyring J, Ngwa EM, Aebi M, Locher KP. </i> Science, 2018","term_id":"IDPO:0000011","curator_id":"stama","start":23,"term_ontology":"IDPO","curator_name":"Stella Tamana","reference_id":"29301962","version":2,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","region_id":"DP01196r002","ec_go":"IDA","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":215,"region_id":"DP01196r003","released":"2022_03","ec_id":"ECO:0006224","reference_html":"The atomic structure of a eukaryotic oligosaccharyltransferase complex. <i> Bai L, Wang T, Zhao G, Kovach A, Li H. </i> Nature, 2018","term_id":"IDPO:0000002","curator_id":"stama","start":23,"term_ontology":"IDPO","curator_name":"Stella Tamana","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29466327","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":215,"term_name":"disorder to order","released":"2022_03","ec_name":"cryogenic electron microscopy evidence used in manual assertion","reference_html":"The atomic structure of a eukaryotic oligosaccharyltransferase complex. <i> Bai L, Wang T, Zhao G, Kovach A, Li H. </i> Nature, 2018","term_id":"IDPO:0000011","curator_id":"stama","start":23,"term_ontology":"IDPO","curator_name":"Stella Tamana","reference_id":"29466327","version":2,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","region_id":"DP01196r004","ec_go":"IDA","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_P48439","date":"2018-07-02T09:17:13.000Z","acc":"P48439","name":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3","length":350,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000130EE9","genes":[{"name":{"value":"OST3"},"orfNames":[{"value":"YOR3124W"}],"olnNames":[{"value":"YOR085W"}]}],"alphafold_very_low_content":0.04,"disorder_content":0.5514285714285714,"disprot_consensus":{"full":[{"start":23,"end":215,"type":"T"}],"Structural state":[{"start":23,"end":215,"type":"D"}],"Structural transition":[{"start":23,"end":215,"type":"T"}]}},{"features":{"pfam":[{"id":"PF02516","name":"Oligosaccharyl transferase STT3, N-terminal","start":19,"end":429},{"id":"PF18527","name":"STT3/PglB C-terminal beta-barrel domain","start":594,"end":673},{"id":"PF21436","name":"STT3/PglB/AglB core domain","start":456,"end":583}],"gene3D":[{"start":429,"end":581,"id":"3.40.1380.40","name":"3.40.1380.40"}]},"uniref50":"UniRef50_B9KDD4","sequence":"MKLQQNFTDNNSIKYTCILILIAFAFSVLCRLYWVAWASEFYEFFFNDQLMITTNDGYAFAEGARDMIAGFHQPNDLSYFGSSLSTLTYWLYSILPFSFESIILYMSAFFASLIVVPIILIAREYKLTTYGFIAALLGSIANSYYNRTMSGYYDTDMLVLVLPMLILLTFIRLTINKDIFTLLLSPVFIMIYLWWYPSSYSLNFAMIGLFGLYTLVFHRKEKIFYLTIALMIIALSMLAWQYKLALIVLLFAIFAFKEEKINFYMIWALIFISILILHLSGGLDPVLYQLKFYVFKASDVQNLKDAAFMYFNVNETIMEVNTIDPEVFMQRISSSVLVFILSFIGFILLCKDHKSMLLALPMLALGFMALRAGLRFTIYAVPVMALGFGYFLYAFFNFLEKKQIKLSLRNKNILLILIAFFSISPALMHIYYYKSSTVFTSYEASILNDLKNKAQREDYVVAWWDYGYPIRYYSDVKTLIDGGKHLGKDNFFSSFVLSKEQIPAANMARLSVEYTEKSFKENYPDVLKAMVKDYNKTSAKDFLESLNDKDFKFDTNKTRDVYIYMPYRMLRIMPVVAQFANTNPDNGEQEKSLFFSQANAIAQDKTTGSVMLDNGVEIINDFRALKVEGASIPLKAFVDIESITNGKFYYNEIDSKAQIYLLFLREYKSFVILDESLYNSSYIQMFLLNQYDQDLFEQITNDTRAKIYRLKR","taxonomy":["Bacteria","Proteobacteria","Epsilonproteobacteria","Campylobacterales","Campylobacteraceae","Campylobacter"],"uniref90":"UniRef90_B9KDD4","disprot_id":"DP01199","ncbi_taxon_id":306263,"regions_counter":3,"creator":"stama","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":327,"region_id":"DP01199r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Molecular basis of lipid-linked oligosaccharide recognition and processing by bacterial oligosaccharyltransferase. <i> Napiórkowska M, Boilevin J, Sovdat T, Darbre T, Reymond JL, Aebi M, Locher KP. </i> Nat Struct Mol Biol, 2017","term_id":"IDPO:0000002","curator_id":"ahatos","start":281,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29058712","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":327,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Molecular basis of lipid-linked oligosaccharide recognition and processing by bacterial oligosaccharyltransferase. <i> Napiórkowska M, Boilevin J, Sovdat T, Darbre T, Reymond JL, Aebi M, Locher KP. </i> Nat Struct Mol Biol, 2017","term_id":"IDPO:0000011","curator_id":"ahatos","start":281,"term_ontology":"IDPO","curator_name":"András Hatos","reference_id":"29058712","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01199r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":327,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Molecular basis of lipid-linked oligosaccharide recognition and processing by bacterial oligosaccharyltransferase. <i> Napiórkowska M, Boilevin J, Sovdat T, Darbre T, Reymond JL, Aebi M, Locher KP. </i> Nat Struct Mol Biol, 2017","term_id":"GO:0005515","curator_id":"ahatos","start":281,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"29058712","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01199r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_B9KDD4","date":"2018-07-02T11:27:30.000Z","acc":"B9KDD4","name":"Undecaprenyl-diphosphooligosaccharide--protein glycotransferase","length":712,"organism":"Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060)","dataset":[],"UniParc":"UPI00004B333F","genes":[{"name":{"value":"pglB"},"olnNames":[{"value":"Cla_1253"}]}],"alphafold_very_low_content":0,"disorder_content":0.06601123595505617,"disprot_consensus":{"full":[{"start":281,"end":327,"type":"T"}],"Structural state":[{"start":281,"end":327,"type":"D"}],"Structural transition":[{"start":281,"end":327,"type":"T"}],"Molecular function":[{"start":281,"end":327,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02516","name":"Oligosaccharyl transferase STT3, N-terminal","start":18,"end":418},{"id":"PF18079","name":"Archaeal glycosylation protein B long peripheral domain","start":779,"end":864},{"id":"PF22627","name":"AglB core domain","start":501,"end":614}],"gene3D":[{"start":499,"end":699,"id":"3.40.50.12610","name":"3.40.50.12610"},{"start":640,"end":770,"id":"1.20.58.1650","name":"1.20.58.1650"},{"start":780,"end":867,"id":"2.60.40.3390","name":"2.60.40.3390"}]},"uniref50":"UniRef50_O29867","sequence":"MQNAESWFKKYWHLSVLVIAALISVKLRILNPWNSVFTWTVRLGGNDPWYYYRLIENTIHNFPHRIWFDPFTYYPYGSYTHFGPFLVYLGSIAGIIFSATSGESLRAVLAFIPAIGGVLAILPVYLLTREVFDKRAAVIAAFLIAIVPGQFLQRSILGFNDHHIWEAFWQVSALGTFLLAYNRWKGHDLSHNLTARQMAYPVIAGITIGLYVLSWGAGFIIAPIILAFMFFAFVLAGFVNADRKNLSLVAVVTFAVSALIYLPFAFNYPGFSTIFYSPFQLLVLLGSAVIAAAFYQIEKWNDVGFFERVGLGRKGMPLAVIVLTALIMGLFFVISPDFARNLLSVVRVVQPKGGALTIAEVYPFFFTHNGEFTLTNAVLHFGALFFFGMAGILYSAYRFLKRRSFPEMALLIWAIAMFIALWGQNRFAYYFAAVSAVYSALALSVVFDKLHLYRALENAIGARNKLSYFRVAFALLIALAAIYPTYILADAQSSYAGGPNKQWYDALTWMRENTPDGEKYDEYYLQLYPTPQSNKEPFSYPFETYGVISWWDYGHWIEAVAHRMPIANPFQAGIGNKYNNVPGASSFFTAENESYAEFVAEKLNVKYVVSDIEMETGKYYAMAVWAEGDLPLAEKYYGGYFYYSPTGTFGYANSQWDIPLNSIIIPLRIPSELYYSTMEAKLHLFDGSGLSHYRMIYESDYPAEWKSYSSQVNLNNESQVLQTALYEAVMRARYGVSPTMGTQEVLYKYAYTQLYEKKMGIPVKIAPSGYVKIFERVKGAVVTGKVSANVTEVSVNATIKTNQNRTFEYWQTVEVKNGTYTVVLPYSHNSDYPVKPITPYHIKAGNVVKEITIYESQVQNGEIIQLDL","taxonomy":["Archaea","Euryarchaeota","Archaeoglobi","Archaeoglobales","Archaeoglobaceae","Archaeoglobus"],"uniref90":"UniRef90_O29867","disprot_id":"DP01200","ncbi_taxon_id":224325,"regions_counter":1,"creator":"stama","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":373,"region_id":"DP01200r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structures of an archaeal oligosaccharyltransferase provide insights into the catalytic cycle of N-linked protein glycosylation. <i> Matsumoto S, Shimada A, Nyirenda J, Igura M, Kawano Y, Kohda D. </i> Proc Natl Acad Sci U S A, 2013","term_id":"IDPO:0000002","curator_id":"stama","start":336,"term_ontology":"IDPO","curator_name":"Stella Tamana","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24127570","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_O29867","date":"2018-07-02T11:41:52.000Z","acc":"O29867","name":"Dolichyl-phosphooligosaccharide-protein glycotransferase 3","length":868,"organism":"Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)","dataset":[],"UniParc":"UPI0000057125","genes":[{"name":{"value":"aglB3"},"olnNames":[{"value":"AF_0380"}]}],"alphafold_very_low_content":0,"disorder_content":0.04377880184331797,"disprot_consensus":{"full":[{"start":336,"end":373,"type":"D"}],"Structural state":[{"start":336,"end":373,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03433","name":"EspA-like secreted protein","start":36,"end":179}],"gene3D":[{"start":31,"end":102,"id":"1.10.287.1140","name":"EspA/CesA-like"},{"start":134,"end":192,"id":"1.10.287.1140","name":"EspA/CesA-like"}]},"uniref50":"UniRef50_Q5K5Q4","sequence":"MDTSTTASVASANASTSTSMAYDLGSMSKDDVIDLFNKLGVFQAAILMFAYMYQAQSDLSIAKFADMNEASKESTTAQKMANLVDAKIADVQSSSDKNAKAQLPDEVISYINDPRNDITISGIDNINAQLGAGDLQTVKAAISAKANNLTTTVNNSQLEIQQMSNTLNLLTSARSDMQSLQYRTISGISLGK","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_Q47184","disprot_id":"DP01201","ncbi_taxon_id":562,"regions_counter":12,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":30,"region_id":"DP01201r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"A pH-dependent conformational change in EspA, a component of the Escherichia coli O157:H7 type III secretion system. <i> Kato T, Hamada D, Fukui T, Hayashi M, Honda T, Murooka Y, Yanagihara I. </i> FEBS J, 2005","statement":[{"text":"If the unsolved regions in the EspA–CesA complex structure are disordered, the a-helical content of EspA should be 37.5%. This value is highly consistent with the a-helical content estimated here from far-UV CD spectra of EspA at pH 7.0 (39.6%). It is generally considered that the native-like secondary structures are present in the partially folded state of a protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":1,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"15943811","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":30,"term_name":"order to disorder","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"A pH-dependent conformational change in EspA, a component of the Escherichia coli O157:H7 type III secretion system. <i> Kato T, Hamada D, Fukui T, Hayashi M, Honda T, Murooka Y, Yanagihara I. </i> FEBS J, 2005","statement":[{"text":"EspA is shown to spontaneously associate into oligomeric structures at neutral pH. However, two distinctive partially unfolded species occur at lower pH. Based on these results, a phase diagram, illustrating potential EspA conformational transitions, was constructed.","type":"Discussion"}],"term_id":"IDPO:0000014","curator_id":"amonzon","start":1,"term_ontology":"IDPO","curator_name":"Alex Monzon","reference_id":"15943811","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01201r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":30,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"A pH-dependent conformational change in EspA, a component of the Escherichia coli O157:H7 type III secretion system. <i> Kato T, Hamada D, Fukui T, Hayashi M, Honda T, Murooka Y, Yanagihara I. </i> FEBS J, 2005","term_id":"GO:0005515","curator_id":"amonzon","start":1,"term_ontology":"GO","curator_name":"Alex Monzon","reference_id":"15943811","version":3,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01201r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":30,"region_id":"DP01201r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural characterization of a type III secretion system filament protein in complex with its chaperone. <i> Yip CK, Finlay BB, Strynadka NC. </i> Nat Struct Mol Biol, 2005","statement":[{"text":"The experimental electron density map only showed clear density for the N-terminal region (Asp31–Leu59) and the C-terminal region (Leu148–Leu190) of EspA.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":1,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1XOU"}],"reference_id":"15619638","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":30,"term_name":"order to disorder","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural characterization of a type III secretion system filament protein in complex with its chaperone. <i> Yip CK, Finlay BB, Strynadka NC. </i> Nat Struct Mol Biol, 2005","term_id":"IDPO:0000014","curator_id":"amonzon","start":1,"term_ontology":"IDPO","curator_name":"Alex Monzon","reference_id":"15619638","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01201r005","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":30,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural characterization of a type III secretion system filament protein in complex with its chaperone. <i> Yip CK, Finlay BB, Strynadka NC. </i> Nat Struct Mol Biol, 2005","statement":[{"text":"CesA is the recently proposed chaperone of EspA,\nand we demonstrate that CesA traps EspA in a monomeric state and inhibits its polymerization. Crystallographic analysis of the\nheterodimeric CesA–EspA complex at a resolution of 2.8 Å reveals that EspA contains two long \u0001-helices, which are involved in\nextensive coiled-coil interactions with CesA.","type":"Abstract"}],"term_id":"GO:0005515","curator_id":"amonzon","start":1,"term_ontology":"GO","curator_name":"Alex Monzon","reference_id":"15619638","version":3,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01201r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":147,"region_id":"DP01201r007","released":"2022_03","ec_id":"ECO:0006204","reference_html":"A pH-dependent conformational change in EspA, a component of the Escherichia coli O157:H7 type III secretion system. <i> Kato T, Hamada D, Fukui T, Hayashi M, Honda T, Murooka Y, Yanagihara I. </i> FEBS J, 2005","statement":[{"text":"If the unsolved regions in the EspA–CesA complex structure are disordered, the a-helical content of EspA should be 37.5%. This value is highly consistent with the a-helical content estimated here from far-UV CD spectra of EspA at pH 7.0 (39.6%). It is generally considered that the native-like secondary structures are present in the partially folded state of a protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":60,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"15943811","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":147,"term_name":"order to disorder","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"A pH-dependent conformational change in EspA, a component of the Escherichia coli O157:H7 type III secretion system. <i> Kato T, Hamada D, Fukui T, Hayashi M, Honda T, Murooka Y, Yanagihara I. </i> FEBS J, 2005","statement":[{"text":"EspA is shown to spontaneously associate into oligomeric structures at neutral pH. However, two distinctive partially unfolded species occur at lower pH. Based on these results, a phase diagram, illustrating potential EspA conformational transitions, was constructed.","type":"Discussion"}],"term_id":"IDPO:0000014","curator_id":"amonzon","start":60,"term_ontology":"IDPO","curator_name":"Alex Monzon","reference_id":"15943811","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01201r008","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":147,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"A pH-dependent conformational change in EspA, a component of the Escherichia coli O157:H7 type III secretion system. <i> Kato T, Hamada D, Fukui T, Hayashi M, Honda T, Murooka Y, Yanagihara I. </i> FEBS J, 2005","term_id":"GO:0005515","curator_id":"amonzon","start":60,"term_ontology":"GO","curator_name":"Alex Monzon","reference_id":"15943811","version":3,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01201r009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":147,"region_id":"DP01201r010","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural characterization of a type III secretion system filament protein in complex with its chaperone. <i> Yip CK, Finlay BB, Strynadka NC. </i> Nat Struct Mol Biol, 2005","statement":[{"text":"The experimental electron density map only showed clear density for the N-terminal region (Asp31–Leu59) and the C-terminal region (Leu148–Leu190) of EspA.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":60,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1XOU"}],"reference_id":"15619638","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":147,"term_name":"order to disorder","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural characterization of a type III secretion system filament protein in complex with its chaperone. <i> Yip CK, Finlay BB, Strynadka NC. </i> Nat Struct Mol Biol, 2005","term_id":"IDPO:0000014","curator_id":"amonzon","start":60,"term_ontology":"IDPO","curator_name":"Alex Monzon","reference_id":"15619638","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01201r011","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":147,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural characterization of a type III secretion system filament protein in complex with its chaperone. <i> Yip CK, Finlay BB, Strynadka NC. </i> Nat Struct Mol Biol, 2005","term_id":"GO:0005515","curator_id":"amonzon","start":60,"term_ontology":"GO","curator_name":"Alex Monzon","reference_id":"15619638","version":3,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01201r012","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q47184","date":"2018-07-02T11:50:58.000Z","acc":"Q47184","name":"EspA","length":192,"organism":"Escherichia coli","dataset":[],"UniParc":"UPI0000033222","genes":[{"name":{"value":"espA","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAA91163.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA91163.1"}}]},"orfNames":[{"value":"D3G36_09190","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EFA4418039.1","url":"https://www.ebi.ac.uk/ena/browser/view/EFA4418039.1"}}]},{"value":"NCTC10089_00097","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"VTR11369.1","url":"https://www.ebi.ac.uk/ena/browser/view/VTR11369.1"}}]}]}],"alphafold_very_low_content":0.11458333333333333,"disorder_content":0.6145833333333334,"disprot_consensus":{"full":[{"start":1,"end":30,"type":"T"},{"start":60,"end":147,"type":"T"}],"Structural state":[{"start":1,"end":30,"type":"D"},{"start":60,"end":147,"type":"D"}],"Structural transition":[{"start":1,"end":30,"type":"T"},{"start":60,"end":147,"type":"T"}],"Molecular function":[{"start":1,"end":30,"type":"F"},{"start":60,"end":147,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00642","name":"Zinc finger C-x8-C-x5-C-x3-H type (and similar)","start":841,"end":864},{"id":"PF08711","name":"TFIIS helical bundle-like domain","start":93,"end":144}],"gene3D":[{"start":74,"end":160,"id":"1.20.930.10","name":"Conserved domain common to transcription factors TFIIS, elongin A, CRSP70"}]},"uniref50":"UniRef50_Q96QC0","sequence":"MGSGPIDPKELLKGLDSFLTRDGEVKSVDGIAKIFSLMKEARKMVSRCTYLNIILQTRAPEVLVKFIDVGGYKLLNSWLTYSKTTNNIPLLQQILLTLQHLPLTVDHLKQNNTAKLVKQLSKSSEDEELRKLASVLVSDWMAVIRSQSSTQPAEKDKKKRKEEGKSRTTLPERPLTEVKAETRAEEAPEKKKEKPKSLRTTAPSHAKFRSTGLELDTPSLVPVKKNSSTVVVSDKYNLKPIPLKRQSATAAPGDAAPPAEKKYKPLNTTPNTTKEIKVKIIPPQPMEGLGFLDALNSAPVPGIKIKKKKKVLSPTAAKPSPFEGKTSTEPSTAKPSSPEPAAPAEPMDTDRPGTPVPAVEVPELMDAASSEPGALDAKPVESPGDPNQLTRKGRKRKTVTWPEEGKLREYFYFELDETERVNVNKIKDFGEAAKREILSDRHAFETARRLSHDNMEEKVPWVCPRPLVLPSPLVIPGSNSQERYIQAEREKGILQELFLNKESPHEPDPEPYEPIPPKLIPLDEECAMDETPYVETLEPGGSGGSPDGAGGSKLPPVLANLMGSMGAGKSPQGPGGGGINVQEILTSIMGSPNNHPSEELLKQPDYSDKLKQMLVPHGLLGPGPVANGFPPGGPGGPKGMQHFPPGPGGPMPGPHGGPGGPVGPRLLGPPPPSRGGDPFWDGPGDPMRGGPMRGGPGPGPGPYHRGRGGRGGNEPPPPPPFRGARGGRSGGGPPNGRGGPGGGGMVGGGGHRPHEGPGGSMGSGHRSHEGPGGSMGSGHRSHEGPGHGGPHGHRPHDVPSHRGHDHRGPPPHEHRGHDGHGGGGHRGHDGGHSHGGDMSNRPVCRHFMMKGNCRYENNCAFYHPGVNGPPLP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_Q96QC0","disprot_id":"DP01202","ncbi_taxon_id":10116,"regions_counter":3,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":433,"region_id":"DP01202r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Understanding the antagonism of retinoblastoma protein dephosphorylation by PNUTS provides insights into the PP1 regulatory code. <i> Choy MS, Hieke M, Kumar GS, Lewis GR, Gonzalez-DeWhitt KR, Kessler RP, Stein BJ, Hessenberger M, Nairn AC, Peti W, Page R. </i> Proc Natl Acad Sci U S A, 2014","statement":[{"text":"A 2D [1H,15N] heteronuclear single\nquantum coherence (HSQC) spectrum showed that PNUTS, like most PP1 regulatory proteins, is an\nIDP, based on the significantly limited chemical-shift dispersion","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":309,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24591642","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":433,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Understanding the antagonism of retinoblastoma protein dephosphorylation by PNUTS provides insights into the PP1 regulatory code. <i> Choy MS, Hieke M, Kumar GS, Lewis GR, Gonzalez-DeWhitt KR, Kessler RP, Stein BJ, Hessenberger M, Nairn AC, Peti W, Page R. </i> Proc Natl Acad Sci U S A, 2014","statement":[{"text":"Isothermal titration\ncalorimetry of PNUTS394–433 and PP1α7–330,\nconfirming that the intrinsically unstructured PNUTS\nPP1 binding domain is functional and interacts\nstrongly with PP1.","type":"Figure"}],"term_id":"GO:0005515","curator_id":"eschad","start":309,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"24591642","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"4MOY"}],"region_id":"DP01202r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":433,"region_id":"DP01202r003","released":"2022_03","ec_id":"ECO:0006317","reference_html":"Understanding the antagonism of retinoblastoma protein dephosphorylation by PNUTS provides insights into the PP1 regulatory code. <i> Choy MS, Hieke M, Kumar GS, Lewis GR, Gonzalez-DeWhitt KR, Kessler RP, Stein BJ, Hessenberger M, Nairn AC, Peti W, Page R. </i> Proc Natl Acad Sci U S A, 2014","statement":[{"text":"PNUTS’s high temperature stability (80 °C).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":309,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24591642","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_O55000","date":"2018-07-02T12:58:08.000Z","acc":"O55000","name":"Serine/threonine-protein phosphatase 1 regulatory subunit 10","length":872,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI00000E78A0","genes":[{"name":{"value":"Ppp1r10"},"synonyms":[{"value":"Cat53"},{"value":"Pnuts"}]}],"alphafold_very_low_content":0.5458715596330275,"disorder_content":0.143348623853211,"disprot_consensus":{"full":[{"start":309,"end":433,"type":"D"}],"Structural state":[{"start":309,"end":433,"type":"D"}],"Molecular function":[{"start":309,"end":433,"type":"F"}]}},{"features":{"pfam":[{"id":"PF10488","name":"Phosphatase-1 catalytic subunit binding region","start":549,"end":619}]},"uniref50":"UniRef50_O75807","sequence":"MAPGQAPHQATPWRDAHPFFLLSPVMGLLSRAWSRLRGLGPLEPWLVEAVKGAALVEAGLEGEARTPLAIPHTPWGRRPEEEAEDSGGPGEDRETLGLKTSSSLPEAWGLLDDDDGMYGEREATSVPRGQGSQFADGQRAPLSPSLLIRTLQGSDKNPGEEKAEEEGVAEEEGVNKFSYPPSHRECCPAVEEEDDEEAVKKEAHRTSTSALSPGSKPSTWVSCPGEEENQATEDKRTERSKGARKTSVSPRSSGSDPRSWEYRSGEASEEKEEKAHKETGKGEAAPGPQSSAPAQRPQLKSWWCQPSDEEEGEVKALGAAEKDGEAECPPCIPPPSAFLKAWVYWPGEDTEEEEDEEEDEDSDSGSDEEEGEAEASSSTPATGVFLKSWVYQPGEDTEEEEDEDSDTGSAEDEREAETSASTPPASAFLKAWVYRPGEDTEEEEDEDVDSEDKEDDSEAALGEAESDPHPSHPDQRAHFRGWGYRPGKETEEEEAAEDWGEAEPCPFRVAIYVPGEKPPPPWAPPRLPLRLQRRLKRPETPTHDPDPETPLKARKVRFSEKVTVHFLAVWAGPAQAARQGPWEQLARDRSRFARRITQAQEELSPCLTPAARARAWARLRNPPLAPIPALTQTLPSSSVPSSPVQTTPLSQAVATPSRSSAAAAAALDLSGRRG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O75807","disprot_id":"DP01203","ncbi_taxon_id":9606,"regions_counter":14,"creator":"grivas","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":631,"region_id":"DP01203r001","released":"2024_12","ec_id":"ECO:0006165","reference_html":"Structural and Functional Analysis of the GADD34:PP1 eIF2α Phosphatase. <i> Choy MS, Yusoff P, Lee IC, Newton JC, Goh CW, Page R, Shenolikar S, Peti W. </i> Cell Rep, 2015","statement":[{"text":"Our studies showed that GADD34513-631 is heat stable (80°C, 15 min; Fig. S1) and that its 2D [1H,15N] HSQC spectrum lacked chemical shift dispersion in the 1HN dimension, confirming that the GADD34 PP1-binding domain is an intrinsically disordered protein (IDP).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":513,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2024-11-12T16:09:33.576Z","reference_source":"pmid","term_name":"disorder","reference_id":"26095357","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":631,"region_id":"DP01203r003","released":"2022_03","ec_id":"ECO:0006317","reference_html":"Structural and Functional Analysis of the GADD34:PP1 eIF2α Phosphatase. <i> Choy MS, Yusoff P, Lee IC, Newton JC, Goh CW, Page R, Shenolikar S, Peti W. </i> Cell Rep, 2015","statement":[{"text":"GADD34 (513–631) is heat stable.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":513,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"26095357","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-05-13T15:54:54.161Z"}},{"start":1,"end":674,"reference_id":"28759048","reference_source":"pmid","reference_html":"Decoding the selectivity of eIF2α holophosphatases and PPP1R15A inhibitors. <i> Carrara M, Sigurdardottir A, Bertolotti A. </i> Nat Struct Mol Biol, 2017","date":"2024-11-12T15:47:35.295Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001191","ec_ontology":"ECO","ec_name":"in vitro cleavage assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"region_id":"DP01203r004","statement":[{"text":"As expected for natively unstructured proteins41, R15A and R15B were sensitive to a limited trypsin proteolysis (Fig. 4c).","type":"Results"}]},{"start":554,"end":674,"reference_id":"34847777","reference_source":"pmid","reference_html":"Substrate recognition determinants of human eIF2α phosphatases. <i> Hodgson G, Andreeva A, Bertolotti A. </i> Open Biol, 2021","date":"2024-11-12T15:53:03.203Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008157","term_name":"protein phosphatase 1 binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"To identify functional regions in R15s, we generated a series of truncation mutants that were FLAG-tagged on their amino-termini."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P62136","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01203r005","statement":[{"text":"PP1 was found to interact with the R15A derivatives that encompassed residues 554–674, which contains the RVxF motif (figure 1a; electronic supplementary material, figure S2).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein phosphatase 1.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":325,"end":554,"reference_id":"34847777","reference_source":"pmid","reference_html":"Substrate recognition determinants of human eIF2α phosphatases. <i> Hodgson G, Andreeva A, Bertolotti A. </i> Open Biol, 2021","date":"2024-11-12T15:54:02.997Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0071074","term_name":"eukaryotic initiation factor eIF2 binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"To identify functional regions in R15s, we generated a series of truncation mutants that were FLAG-tagged on their amino-termini."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9BY44","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01203r006","statement":[{"text":" eIF2α was enriched in the R15A325–554 and R15A325–674 pulldowns as well as in the pulldown of the full-length R15A1–674, albeit to a lesser extent (figure 1a; electronic supplementary material, figure S2). We found no enrichment of eIF2α upon immunoprecipitation of R15A1–325 or R15A554–674 (figure 1a; electronic supplementary material, figure S2). This reveals that R15A325–554 encodes the substrate recruitment region.","type":"Results"}],"term_comment":"","term_def":"\"Binding to eukaryotic initiation factor eIF2, a protein complex involved in the initiation of ribosome-mediated translation.\" [GOC:hjd]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":674,"reference_id":"34847777","reference_source":"pmid","reference_html":"Substrate recognition determinants of human eIF2α phosphatases. <i> Hodgson G, Andreeva A, Bertolotti A. </i> Open Biol, 2021","date":"2024-11-12T15:54:55.360Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0000164","term_name":"protein phosphatase type 1 complex","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"To identify functional regions in R15s, we generated a series of truncation mutants that were FLAG-tagged on their amino-termini."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9BY44","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P62136","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01203r007","statement":[{"text":" eIF2α was enriched in the R15A325–554 and R15A325–674 pulldowns as well as in the pulldown of the full-length R15A1–674, albeit to a lesser extent (figure 1a; electronic supplementary material, figure S2). We found no enrichment of eIF2α upon immunoprecipitation of R15A1–325 or R15A554–674 (figure 1a; electronic supplementary material, figure S2). This reveals that R15A325–554 encodes the substrate recruitment region.","type":"Results"},{"text":"PP1 was found to interact with the R15A derivatives that encompassed residues 554–674, which contains the RVxF motif (figure 1a; electronic supplementary material, figure S2).","type":"Results"}],"term_comment":"","term_def":"\"A protein complex that possesses magnesium-dependent protein serine/threonine phosphatase (AMD phosphatase) activity, and consists of a catalytic subunit and one or more regulatory subunits that dictates the phosphatase's substrate specificity, function, and activity.\" [GOC:mah, GOC:ssd]","term_is_obsolete":false,"term_not_annotate":false},{"start":355,"end":674,"reference_id":"34847777","reference_source":"pmid","reference_html":"Substrate recognition determinants of human eIF2α phosphatases. <i> Hodgson G, Andreeva A, Bertolotti A. </i> Open Biol, 2021","date":"2024-11-12T16:05:08.505Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019888","term_name":"protein phosphatase regulator activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006170","ec_ontology":"ECO","ec_name":"quantitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IEP","interaction_partner":[{"db":"UniProt","id":"P62136","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01203r008","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","statements":[{"type":"Figure","text":"(a,b) R15 constructs were transfected into HEK 293T cells, such that cells were overconfluent before lysis, providing high basal eIF2α phosphorylation to asses R15 construct activity."}],"entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"Overexpression of full-length R15A1–674 led to a robust decrease in the levels of phosphorylated eIF2α (figure 3a). Overexpression of R15A325–674 also led to nearly complete dephosphorylation of eIF2α (figure 3a).","type":"Results"},{"text":"The amino-terminal regions of R15s, which do not bind the substrate nor PP1, as well as R15A325–554 and R15B340–639, which bind the substrate but not PP1, did not decrease phosphorylation of eIF2α (figure 3a,b). ","type":"Results"}],"term_comment":"","term_def":"\"Binds to and modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_O75807","date":"2018-07-02T13:31:19.000Z","acc":"O75807","name":"Protein phosphatase 1 regulatory subunit 15A","length":674,"organism":"Homo sapiens","dataset":["Autophagy-related proteins","Stress response proteins"],"UniParc":"UPI000006F652","genes":[{"name":{"value":"PPP1R15A"},"synonyms":[{"value":"GADD34"}]}],"alphafold_very_low_content":0.6735905044510386,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":674,"type":"D"}],"Structural state":[{"start":1,"end":674,"type":"D"}],"Molecular function":[{"start":325,"end":674,"type":"F"}],"Cellular component":[{"start":1,"end":674,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00125","name":"Core histone H2A/H2B/H3/H4 domain","start":7,"end":89},{"id":"PF16211","name":"C-terminus of histone H2A","start":92,"end":125}],"gene3D":[{"start":1,"end":129,"id":"1.10.20.10","name":"Histone, subunit A"}]},"uniref50":"UniRef50_Q99878","sequence":"MSGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTDSHKAKAK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Phasianinae","Gallus"],"uniref90":"UniRef90_Q99878","disprot_id":"DP01205","ncbi_taxon_id":9031,"regions_counter":2,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":13,"region_id":"DP01205r001","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Structure of the histone-core octamer in KCl/phosphate crystals at 2.15 A resolution. <i> Chantalat L, Nicholson JM, Lambert SJ, Reid AJ, Donovan MJ, Reynolds CD, Wood CM, Baldwin JP. </i> Acta Crystallogr D Biol Crystallogr, 2003","statement":[{"text":"Histone N-terminal tail regions extend to Lys15 on the H2As, Ser36 on the H2Bs, Tyr41 on the H3s and Arg23 on the H4s. The C-terminal tails of the H2As extend from Pro117. Most of the amino-acid residues in the tails in our structure are disordered.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-24T17:42:03.605Z","reference_source":"pmid","term_name":"disorder","reference_id":"12876341","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"1HQ3"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62801"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84229"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0C1H5"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1061"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":129,"region_id":"DP01205r002","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Structure of the histone-core octamer in KCl/phosphate crystals at 2.15 A resolution. <i> Chantalat L, Nicholson JM, Lambert SJ, Reid AJ, Donovan MJ, Reynolds CD, Wood CM, Baldwin JP. </i> Acta Crystallogr D Biol Crystallogr, 2003","statement":[{"text":"Histone N-terminal tail regions extend to Lys15 on the H2As, Ser36 on the H2Bs, Tyr41 on the H3s and Arg23 on the H4s. The C-terminal tails of the H2As extend from Pro117. Most of the amino-acid residues in the tails in our structure are disordered.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":120,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-24T17:40:55.736Z","reference_source":"pmid","term_name":"disorder","reference_id":"12876341","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0C1H5"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84229"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62801"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1061"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"}],"cross_refs":[{"db":"PDB","id":"1HQ3"}]}],"released":"2018_11","uniref100":"UniRef100_P02263","date":"2018-07-03T02:20:46.000Z","acc":"P02263","name":"Histone H2A-IV","length":129,"organism":"Gallus gallus","dataset":[],"UniParc":"UPI0000111B88","genes":[],"alphafold_very_low_content":0.007751937984496124,"disorder_content":0.17829457364341086,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"D"},{"start":120,"end":129,"type":"D"}],"Structural state":[{"start":1,"end":13,"type":"D"},{"start":120,"end":129,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03165","name":"MH1 domain","start":31,"end":131},{"id":"PF03166","name":"MH2 domain","start":269,"end":441}],"gene3D":[{"start":268,"end":465,"id":"2.60.200.10","name":"2.60.200.10"},{"start":3,"end":144,"id":"3.90.520.10","name":"SMAD MH1 domain"}]},"uniref50":"UniRef50_Q15797","sequence":"MNVTSLFSFTSPAVKRLLGWKQGDEEEKWAEKAVDALVKKLKKKKGAMEELEKALSCPGQPSNCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLECCEFPFGSKQKEVCINPYHYKRVESPVLPPVLVPRHSEYNPQHSLLAQFRNLGQNEPHMPLNATFPDSFQQPNSHPFPHSPNSSYPNSPGSSSSTYPHSPTSSDPGSPFQMPADTPPPAYLPPEDPMTQDGSQPMDTNMMAPPLPSEINRGDVQAVAYEEPKHWCSIVYYELNNRVGEAFHASSTSVLVDGFTDPSNNKNRFCLGLLSNVNRNSTIENTRRHIGKGVHLYYVGGEVYAECLSDSSIFVQSRNCNYHHGFHPTTVCKIPSGCSLKIFNNQEFAQLLAQSVNHGFETVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNPISSVS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q15797","disprot_id":"DP01206","ncbi_taxon_id":9606,"regions_counter":4,"creator":"gerdos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":267,"region_id":"DP01206r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis of Smad1 activation by receptor kinase phosphorylation. <i> Qin BY, Chacko BM, Lam SS, de Caestecker MP, Correia JJ, Lin K. </i> Mol Cell, 2001","statement":[{"text":"The linker region (residues 217 to 267) is not visible due to structural disordering.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":217,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"11779505","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":267,"term_name":"flexible linker","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural basis of Smad1 activation by receptor kinase phosphorylation. <i> Qin BY, Chacko BM, Lam SS, de Caestecker MP, Correia JJ, Lin K. </i> Mol Cell, 2001","term_id":"IDPO:0000033","curator_id":"rdavidovic","start":217,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","reference_id":"11779505","version":3,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01206r002","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_Q15797","date":"2018-07-03T06:53:37.000Z","acc":"Q15797","name":"Mothers against decapentaplegic homolog 1","length":465,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000135A76","genes":[{"name":{"value":"SMAD1"},"synonyms":[{"value":"BSP1"},{"value":"MADH1"},{"value":"MADR1"}]}],"alphafold_very_low_content":0.18924731182795698,"disorder_content":0.10967741935483871,"disprot_consensus":{"full":[{"start":217,"end":267,"type":"D"}],"Structural state":[{"start":217,"end":267,"type":"D"}],"Disorder function":[{"start":217,"end":267,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02205","name":"WH2 motif","start":725,"end":751},{"id":"PF08397","name":"IRSp53/MIM homology domain","start":16,"end":237}],"gene3D":[{"start":1,"end":246,"id":"1.20.1270.60","name":"Arfaptin homology (AH) domain/BAR domain"}]},"uniref50":"UniRef50_Q8R1S4","sequence":"MEAVIEKECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRHRSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKKKSSDTLKLQKKAKKGRGDIQPQLDSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTISEDLKSLTMDPHKLPSSSEQVILDLKGSDYSWSYQTPPSSPSTTMSRKSSVCSSLNSVNSSDSRSSGSHSHSPSSHYRYRSSNLAQQAPVRLSSVSSHDSGFISQDAFQSKSPSPMPPEAPNQLSNGFSHYSLSSESHVGPTGAGLFPHCLPASRLLPRVTSVHLPDYAHYYTIGPGMFPSSQIPSWKDWAKPGPYDQPLVNTLQRRKEKREPDPNGGGPTTASGPPAAAEEAQRPRSMTVSAATRPGEEMEACEELALALSRGLQLDTQRSSRDSLQCSSGYSTQTTTPCCSEDTIPSQVSDYDYFSVSGDQEADQQEFDKSSTIPRNSDISQSYRRMFQAKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKTPTVPDLPGVLPAPPDGPEERGEHSPESPSVGEGPQGVTSMPSSMWSGQASVNPPLPGPKPSIPEEHRQAIPESEAEDQEREPPSATVSPGQIPESDPADLSPRDTPQGEDMLNAIRRGVKLKKTTTNDRSAPRFS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O43312","disprot_id":"DP01224","ncbi_taxon_id":9606,"regions_counter":2,"creator":"lpaladin","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":753,"region_id":"DP01224r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for the actin-binding function of missing-in-metastasis. <i> Lee SH, Kerff F, Chereau D, Ferron F, Klug A, Dominguez R. </i> Structure, 2007","statement":[{"text":"We made a synthetic peptide corresponding to this WH2, comprising amino acids Asp 724 to the C-terminus (Ser 755) of human MIM. The structure of the WH2 of MIM can be conceptually subdivided into two parts, an N-terminal amphiphilic α-helix, comprising amino acids Gly 728 to Gly 738, and a C-terminal extended region from Val 739 to Arg 753.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bhajdu","start":739,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2D1K"}],"reference_id":"17292833","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":753,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural basis for the actin-binding function of missing-in-metastasis. <i> Lee SH, Kerff F, Chereau D, Ferron F, Klug A, Dominguez R. </i> Structure, 2007","statement":[{"text":"The crystal structure of this WH2 was determined as a ternary complex with actin-DNase I.","type":"Results"}],"term_id":"GO:0005515","curator_id":"bhajdu","start":739,"term_ontology":"GO","curator_name":"Borbála Hajdu-Soltész","reference_id":"17292833","version":3,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01224r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_O43312","date":"2018-07-03T08:30:33.000Z","acc":"O43312","name":"Protein MTSS 1","length":755,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000019B3D8","genes":[{"name":{"value":"MTSS1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:20443","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:20443"}}]},"synonyms":[{"value":"KIAA0429"},{"value":"MIM"}]}],"alphafold_very_low_content":0.5298013245033113,"disorder_content":0.019867549668874173,"disprot_consensus":{"full":[{"start":739,"end":753,"type":"D"}],"Structural state":[{"start":739,"end":753,"type":"D"}],"Molecular function":[{"start":739,"end":753,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03247","name":"Prothymosin/parathymosin family","start":2,"end":97}]},"uniref50":"UniRef50_Q9NYD3","sequence":"MSDAAVDTSSEITTEDLKEKKEVVEEAENGRDAPADEENGEQEADNEVDEEQEEGGEEEGDGEEEDGDEDEGAESATDKRAAEDDEDNDVDTKKQKTDEDD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9NYD3","disprot_id":"DP01228","ncbi_taxon_id":9606,"regions_counter":11,"creator":"stama","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":101,"region_id":"DP01228r001","released":"2022_03","ec_id":"ECO:0006283","reference_html":"Prothymosin alpha: a biologically active protein with random coil conformation. <i> Gast K, Damaschun H, Eckert K, Schulze-Forster K, Maurer HR, Müller-Frohne M, Zirwer D, Czarnecki J, Damaschun G. </i> Biochemistry, 1995","term_id":"IDPO:0000002","curator_id":"stama","start":1,"term_ontology":"IDPO","curator_name":"Stella Tamana","ec_name":"electrospray ionization fourier transform ion cyclotron resonance mass spectrometry evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"7548085","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":101,"term_name":"protein folding chaperone","released":"2022_03","ec_name":"electrospray ionization fourier transform ion cyclotron resonance mass spectrometry evidence used in manual assertion","reference_html":"Prothymosin alpha: a biologically active protein with random coil conformation. <i> Gast K, Damaschun H, Eckert K, Schulze-Forster K, Maurer HR, Müller-Frohne M, Zirwer D, Czarnecki J, Damaschun G. </i> Biochemistry, 1995","term_id":"GO:0044183","curator_id":"stama","start":1,"term_ontology":"GO","curator_name":"Stella Tamana","reference_id":"7548085","version":3,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006283","region_id":"DP01228r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":101,"region_id":"DP01228r003","released":"2022_03","ec_id":"ECO:0007064","reference_html":"Prothymosin alpha: a biologically active protein with random coil conformation. <i> Gast K, Damaschun H, Eckert K, Schulze-Forster K, Maurer HR, Müller-Frohne M, Zirwer D, Czarnecki J, Damaschun G. </i> Biochemistry, 1995","term_id":"IDPO:0000002","curator_id":"stama","start":1,"term_ontology":"IDPO","curator_name":"Stella Tamana","ec_name":"dynamic light scattering assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"7548085","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":101,"term_name":"protein folding chaperone","released":"2022_03","ec_name":"dynamic light scattering assay evidence used in manual assertion","reference_html":"Prothymosin alpha: a biologically active protein with random coil conformation. <i> Gast K, Damaschun H, Eckert K, Schulze-Forster K, Maurer HR, Müller-Frohne M, Zirwer D, Czarnecki J, Damaschun G. </i> Biochemistry, 1995","term_id":"GO:0044183","curator_id":"stama","start":1,"term_ontology":"GO","curator_name":"Stella Tamana","reference_id":"7548085","version":3,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007064","region_id":"DP01228r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":101,"region_id":"DP01228r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Extreme disorder in an ultrahigh-affinity protein complex. <i> Borgia A, Borgia MB, Bugge K, Kissling VM, Heidarsson PO, Fernandes CB, Sottini A, Soranno A, Buholzer KJ, Nettels D, Kragelund BB, Best RB, Schuler B. </i> Nature, 2018","term_id":"IDPO:0000002","curator_id":"stama","start":1,"term_ontology":"IDPO","curator_name":"Stella Tamana","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29466338","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":101,"term_name":"protein folding chaperone","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Extreme disorder in an ultrahigh-affinity protein complex. <i> Borgia A, Borgia MB, Bugge K, Kissling VM, Heidarsson PO, Fernandes CB, Sottini A, Soranno A, Buholzer KJ, Nettels D, Kragelund BB, Best RB, Schuler B. </i> Nature, 2018","term_id":"GO:0044183","curator_id":"stama","start":1,"term_ontology":"GO","curator_name":"Stella Tamana","reference_id":"29466338","version":3,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01228r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":101,"region_id":"DP01228r007","released":"2022_03","ec_id":"ECO:0006206","reference_html":"Extreme disorder in an ultrahigh-affinity protein complex. <i> Borgia A, Borgia MB, Bugge K, Kissling VM, Heidarsson PO, Fernandes CB, Sottini A, Soranno A, Buholzer KJ, Nettels D, Kragelund BB, Best RB, Schuler B. </i> Nature, 2018","term_id":"IDPO:0000002","curator_id":"stama","start":1,"term_ontology":"IDPO","curator_name":"Stella Tamana","ec_name":"near-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29466338","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":101,"term_name":"protein folding chaperone","released":"2022_03","ec_name":"near-UV circular dichroism evidence used in manual assertion","reference_html":"Extreme disorder in an ultrahigh-affinity protein complex. <i> Borgia A, Borgia MB, Bugge K, Kissling VM, Heidarsson PO, Fernandes CB, Sottini A, Soranno A, Buholzer KJ, Nettels D, Kragelund BB, Best RB, Schuler B. </i> Nature, 2018","term_id":"GO:0044183","curator_id":"stama","start":1,"term_ontology":"GO","curator_name":"Stella Tamana","reference_id":"29466338","version":3,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006206","region_id":"DP01228r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":101,"region_id":"DP01228r009","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Prothymosin alpha: a biologically active protein with random coil conformation. <i> Gast K, Damaschun H, Eckert K, Schulze-Forster K, Maurer HR, Müller-Frohne M, Zirwer D, Czarnecki J, Damaschun G. </i> Biochemistry, 1995","term_id":"IDPO:0000002","curator_id":"stama","start":1,"term_ontology":"IDPO","curator_name":"Stella Tamana","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"7548085","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":101,"term_name":"protein folding chaperone","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","reference_html":"Prothymosin alpha: a biologically active protein with random coil conformation. <i> Gast K, Damaschun H, Eckert K, Schulze-Forster K, Maurer HR, Müller-Frohne M, Zirwer D, Czarnecki J, Damaschun G. </i> Biochemistry, 1995","term_id":"GO:0044183","curator_id":"stama","start":1,"term_ontology":"GO","curator_name":"Stella Tamana","reference_id":"7548085","version":3,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","region_id":"DP01228r010","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":101,"region_id":"DP01228r011","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Natively unfolded human prothymosin alpha adopts partially folded collapsed conformation at acidic pH. <i> Uversky VN, Gillespie JR, Millett IS, Khodyakova AV, Vasiliev AM, Chernovskaya TV, Vasilenko RN, Kozlovskaya GD, Dolgikh DA, Fink AL, Doniach S, Abramov VM. </i> Biochemistry, 1999","term_id":"IDPO:0000002","curator_id":"stama","start":1,"term_ontology":"IDPO","curator_name":"Stella Tamana","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"10555983","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9UMZ1","date":"2018-07-03T09:23:17.000Z","acc":"Q9UMZ1","name":"Prothymosin a14","length":101,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000006F864","genes":[],"alphafold_very_low_content":0.009900990099009901,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":101,"type":"D"}],"Structural state":[{"start":1,"end":101,"type":"D"}],"Molecular function":[{"start":1,"end":101,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00400","name":"WD domain, G-beta repeat","start":10,"end":41},{"id":"PF00400","name":"WD domain, G-beta repeat","start":50,"end":86},{"id":"PF00400","name":"WD domain, G-beta repeat","start":96,"end":130},{"id":"PF00400","name":"WD domain, G-beta repeat","start":203,"end":243},{"id":"PF00400","name":"WD domain, G-beta repeat","start":260,"end":289}],"gene3D":[{"start":1,"end":316,"id":"2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"}]},"uniref50":"UniRef50_P55735","sequence":"MVSVINTVDTSHEDMIHDAQMDYYGTRLATCSSDRSVKIFDVRNGGQILIADLRGHEGPVWQVAWAHPMYGNILASCSYDRKVIIWREENGTWEKSHEHAGHDSSVNSVCWAPHDYGLILACGSSDGAISLLTYTGEGQWEVKKINNAHTIGCNAVSWAPAVVPGSLIDHPSGQKPNYIKRFASGGCDNLIKLWKEEEDGQWKEEQKLEAHSDWVRDVAWAPSIGLPTSTIASCSQDGRVFIWTCDDASSNTWSPKLLHKFNDVVWHVSWSITANILAVSGGDNKVTLWKESVDGQWVCISDVNKGQGSVSASVTEGQQNEQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P55735","disprot_id":"DP01236","ncbi_taxon_id":9606,"regions_counter":2,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":316,"region_id":"DP01236r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Architecture of a coat for the nuclear pore membrane. <i> Hsia KC, Stavropoulos P, Blobel G, Hoelz A. </i> Cell, 2007","statement":[{"text":"No electron density was\nobserved for the N-terminal 14 and C-terminal 12 residues, the residues 165 to 172 in Sec13,\nand the N-terminal 6 residues of Nup145C. These residues are presumed to be disordered and\ntherefore have been omitted from the final model","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":305,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18160040","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":14,"region_id":"DP01236r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Architecture of a coat for the nuclear pore membrane. <i> Hsia KC, Stavropoulos P, Blobel G, Hoelz A. </i> Cell, 2007","statement":[{"text":"No electron density was\nobserved for the N-terminal 14 and C-terminal 12 residues, the residues 165 to 172 in Sec13,\nand the N-terminal 6 residues of Nup145C. These residues are presumed to be disordered and\ntherefore have been omitted from the final model","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":1,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18160040","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P55735","date":"2018-07-03T09:48:27.000Z","acc":"P55735","name":"Protein SEC13 homolog","length":322,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000013DEC3","genes":[{"name":{"value":"SEC13"},"synonyms":[{"value":"D3S1231E"},{"value":"SEC13A","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"25201882","url":"http://www.ncbi.nlm.nih.gov/pubmed/25201882","alternativeUrl":"https://europepmc.org/abstract/MED/25201882"}}]},{"value":"SEC13L1"},{"value":"SEC13R"}]}],"alphafold_very_low_content":0.043478260869565216,"disorder_content":0.08074534161490683,"disprot_consensus":{"full":[{"start":1,"end":14,"type":"D"},{"start":305,"end":316,"type":"D"}],"Structural state":[{"start":1,"end":14,"type":"D"},{"start":305,"end":316,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02002","name":"TFIIE alpha subunit","start":11,"end":118}],"gene3D":[{"start":108,"end":169,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"}]},"uniref50":"UniRef50_P36100","sequence":"MDRPIDDIVKNLLKFVVRGFYGGSFVLVLDAILFHSVLAEDDLKQLLSINKTELGPLIARLRSDRLISIHKQREYPPNSKSVERVYYYVKYPHAIDAIKWKVHQVVQRLKDDLDKNSEPNGYMCPICLTKYTQLEAVQLLNFDRTEFLCSLCDEPLVEDDSGKKNKEKQDKLNRLMDQIQPIIDSLKKIDDSRIEENTFEIALARLIPPQNQSHAAYTYNPKKGSTMFRPGDSAPLPNLMGTALGNDSSRRAGANSQATLHINITTASDEVAQRELQERQAEEKRKQNAVPEWHKQSTIGKTALGRLDNEEEFDPVVTASAMDSINPDNEPAQETSYQNNRTLTEQEMEERENEKTLNDYYAALAKKQAKLNKEEEEEEEEEEDEEEEEEEEMEDVMDDNDETARENALEDEFEDVTDTAGTAKTESNTSNDVKQESINDKTEDAVNATATASGPSANAKPNDGDDDDDDDDDEMDIEFEDV","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P36100","disprot_id":"DP01237","ncbi_taxon_id":559292,"regions_counter":1,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":482,"region_id":"DP01237r001","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Transcription initiation complex structures elucidate DNA opening. <i> Plaschka C, Hantsche M, Dienemann C, Burzinski C, Plitzko J, Cramer P. </i> Nature, 2016","term_id":"IDPO:0000002","curator_id":"rdavidovic","start":195,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5FYW"}],"reference_id":"27193681","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P36100","date":"2018-07-03T10:14:00.000Z","acc":"P36100","name":"Transcription initiation factor IIE subunit alpha","length":482,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000005304A","genes":[{"name":{"value":"TFA1"},"olnNames":[{"value":"YKL028W"}]}],"alphafold_very_low_content":0.2883817427385892,"disorder_content":0.5975103734439834,"disprot_consensus":{"full":[{"start":195,"end":482,"type":"D"}],"Structural state":[{"start":195,"end":482,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00350","name":"Dynamin family","start":73,"end":248},{"id":"PF01031","name":"Dynamin central region","start":259,"end":546},{"id":"PF02212","name":"Dynamin GTPase effector domain","start":571,"end":660}],"gene3D":[{"start":366,"end":630,"id":"1.20.120.1240","name":"Dynamin, middle domain"},{"start":59,"end":355,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_P20591","sequence":"MVVSEVDIAKADPAAASHPLLLNGDATVAQKNPGSVAENNLCSQYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKLVNEDKWRGKVSYQDYEIEISDASEVEKEINKAQNAIAGEGMGISHELITLEISSRDVPDLTLIDLPGITRVAVGNQPADIGYKIKTLIKKYIQRQETISLVVVPSNVDIATTEALSMAQEVDPEGDRTIGILTKPDLVDKGTEDKVVDVVRNLVFHLKKGYMIVKCRGQQEIQDQLSLSEALQREKIFFENHPYFRDLLEEGKATVPCLAEKLTSELITHICKSLPLLENQIKETHQRITEELQKYGVDIPEDENEKMFFLIDKVNAFNQDITALMQGEETVGEEDIRLFTRLRHEFHKWSTIIENNFQEGHKILSRKIQKFENQYRGRELPGFVNYRTFETIVKQQIKALEEPAVDMLHTVTDMVRLAFTDVSIKNFEEFFNLHRTAKSKIEDIRAEQEREGEKLIRLHFQMEQIVYCQDQVYRGALQKVREKELEEEKKKKSWDFGAFQSSSATDSSMEEIFQHLMAYHQEASKRISSHIPLIIQFFMLQTYGQQLQKAMLQLLQDKDTYSWLLKERSDTSDKRKFLKERLARLTQARRRLAQFPG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P20591","disprot_id":"DP01239","ncbi_taxon_id":9606,"regions_counter":2,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":447,"region_id":"DP01239r001","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Structural basis of oligomerization in the stalk region of dynamin-like MxA. <i> Gao S, von der Malsburg A, Paeschke S, Behlke J, Haller O, Kochs G, Daumke O. </i> Nature, 2010","statement":[{"text":"A putative loop L2 (amino acids 438–447) opposite the deduced position of the G domain is not visible in our structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":438,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-24T14:48:50.680Z","reference_source":"pmid","term_name":"disorder","reference_id":"20428112","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"3LJB"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:07:59.857Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":572,"region_id":"DP01239r002","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Structural basis of oligomerization in the stalk region of dynamin-like MxA. <i> Gao S, von der Malsburg A, Paeschke S, Behlke J, Haller O, Kochs G, Daumke O. </i> Nature, 2010","statement":[{"text":"The 40-amino-acid-long loop L4 (residues 532–572) is at the equivalent sequence position as the pleckstrin homology (PH) domain of dynamin (Fig. 1a and Supplementary Fig. 3) and is absent in our model.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":532,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-24T14:47:35.937Z","reference_source":"pmid","term_name":"disorder","reference_id":"20428112","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"3LJB"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:08:01.697Z"}}],"released":"2018_11","uniref100":"UniRef100_P20591","date":"2018-07-03T11:15:52.000Z","acc":"P20591","name":"Interferon-induced GTP-binding protein Mx1","length":662,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI000012FAA0","genes":[{"name":{"value":"MX1"}}],"alphafold_very_low_content":0.08610271903323263,"disorder_content":0.0770392749244713,"disprot_consensus":{"full":[{"start":438,"end":447,"type":"D"},{"start":532,"end":572,"type":"D"}],"Structural state":[{"start":438,"end":447,"type":"D"},{"start":532,"end":572,"type":"D"}]}},{"features":{"pfam":[{"id":"PF04049","name":"Anaphase promoting complex subunit 8 / Cdc23","start":32,"end":270},{"id":"PF13181","name":"Tetratricopeptide repeat","start":332,"end":363},{"id":"PF13414","name":"TPR repeat","start":372,"end":409}],"gene3D":[{"start":26,"end":327,"id":"1.25.40.10","name":"Tetratricopeptide repeat domain"},{"start":328,"end":538,"id":"1.25.40.10","name":"Tetratricopeptide repeat domain"}]},"uniref50":"UniRef50_Q9UJX2","sequence":"MAASTSMVPVAVTAAVAPVLSINSDFSDLREIKKQLLLIAGLTRERGLLHSSKWSAELAFSLPALPLAELQPPPPITEEDAQDMDAYTLAKAYFDVKEYDRAAHFLHGCNSKKAYFLYMYSRYLSGEKKKDDETVDSLGPLEKGQVKNEALRELRVELSKKHQARELDGFGLYLYGVVLRKLDLVKEAIDVFVEATHVLPLHWGAWLELCNLITDKEMLKFLSLPDTWMKEFFLAHIYTELQLIEEALQKYQNLIDVGFSKSSYIVSQIAVAYHNIRDIDKALSIFNELRKQDPYRIENMDTFSNLLYVRSMKSELSYLAHNLCEIDKYRVETCCVIGNYYSLRSQHEKAALYFQRALKLNPRYLGAWTLMGHEYMEMKNTSAAIQAYRHAIEVNKRDYRAWYGLGQTYEILKMPFYCLYYYRRAHQLRPNDSRMLVALGECYEKLNQLVEAKKCYWRAYAVGDVEKMALVKLAKLHEQLTESEQAAQCYIKYIQDIYSCGEIVEHLEESTAFRYLAQYYFKCKLWDEASTCAQKCCAFNDTREEGKALLRQILQLRNQGETPTTEVPAPFFLPASLSANNTPTRRVSPLNLSSVTP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UJX2","disprot_id":"DP01240","ncbi_taxon_id":9606,"regions_counter":2,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":25,"region_id":"DP01240r001","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"However, the \nintrinsically disordered regions of some APC/C subunits were not visible in the EM map \n(defined in Extended Data Table 2).","type":"Table"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":1,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":597,"region_id":"DP01240r002","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"However, the \nintrinsically disordered regions of some APC/C subunits were not visible in the EM map \n(defined in Extended Data Table 2).","type":"Table"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":558,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9UJX2","date":"2018-07-03T12:34:55.000Z","acc":"Q9UJX2","name":"Cell division cycle protein 23 homolog","length":597,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000006CC86","genes":[{"name":{"value":"CDC23"},"synonyms":[{"value":"ANAPC8"}]}],"alphafold_very_low_content":0.08710217755443886,"disorder_content":0.10887772194304858,"disprot_consensus":{"full":[{"start":1,"end":25,"type":"D"},{"start":558,"end":597,"type":"D"}],"Structural state":[{"start":1,"end":25,"type":"D"},{"start":558,"end":597,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00999","name":"Sodium/hydrogen exchanger, transmembrane","start":110,"end":503},{"id":"PF16644","name":"Regulatory region of Na+/H+ exchanger NHE binds to calmodulin","start":600,"end":685}]},"uniref50":"UniRef50_P19634","sequence":"MVLRSGICGLSPHRIFPSLLVVVALVGLLPVLRSHGLQLSPTASTIRSSEPPRERSIGDVTTAPPEVTPESRPVNHSVTDHGMKPRKAFPVLGIDYTHVRTPFEISLWILLACLMKIGFHVIPTISSIVPESCLLIVVGLLVGGLIKGVGETPPFLQSDVFFLFLLPPIILDAGYFLPLRQFTENLGTILIFAVVGTLWNAFFLGGLMYAVCLVGGEQINNIGLLDNLLFGSIISAVDPVAVLAVFEEIHINELLHILVFGESLLNDAVTVVLYHLFEEFANYEHVGIVDIFLGFLSFFVVALGGVLVGVVYGVIAAFTSRFTSHIRVIEPLFVFLYSYMAYLSAELFHLSGIMALIASGVVMRPYVEANISHKSHTTIKYFLKMWSSVSETLIFIFLGVSTVAGSHHWNWTFVISTLLFCLIARVLGVLGLTWFINKFRIVKLTPKDQFIIAYGGLRGAIAFSLGYLLDKKHFPMCDLFLTAIITVIFFTVFVQGMTIRPLVDLLAVKKKQETKRSINEEIHTQFLDHLLTGIEDICGHYGHHHWKDKLNRFNKKYVKKCLIAGERSKEPQLIAFYHKMEMKQAIELVESGGMGKIPSAVSTVSMQNIHPKSLPSERILPALSKDKEEEIRKILRNNLQKTRQRLRSYNRHTLVADPYEEAWNQMLLRRQKARQLEQKINNYLTVPAHKLDSPTMSRARIGSDPLAYEPKEDLPVITIDPASPQSPESVDLVNEELKGKVLGLSRDPAKVAEEDEDDDGGIMMRSKETSSPGTDDVFTPAPSDSPSSQRIQRCLSDPGPHPEPGEGEPFFPKGQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P19634","disprot_id":"DP01241","ncbi_taxon_id":9606,"regions_counter":13,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":815,"region_id":"DP01241r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A phosphorylation-motif for tuneable helix stabilisation in intrinsically disordered proteins - Lessons from the sodium proton exchanger 1 (NHE1). <i> Hendus-Altenburger R, Lambrughi M, Terkelsen T, Pedersen SF, Papaleo E, Lindorff-Larsen K, Kragelund BB. </i> Cell Signal, 2017","statement":[{"text":"Secondary structure analysis by NMR spectroscopy revealed severaltransient helices (THs) in the intrinsically disordered NHE1cdt\nThesewere located at P694-R700 (TH1), P727-G743 (TH2), D758-S766 (TH3), andP786-L795 (TH4), where TH1 and TH4 were rather short and lowly populated.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"epapa","start":680,"term_ontology":"IDPO","curator_name":"Elena Papaleo","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28554535","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":815,"region_id":"DP01241r002","released":"2022_03","ec_id":"ECO:0006210","reference_html":"The intracellular distal tail of the Na+/H+ exchanger NHE1 is intrinsically disordered: implications for NHE1 trafficking. <i> Nørholm AB, Hendus-Altenburger R, Bjerre G, Kjaergaard M, Pedersen SF, Kragelund BB. </i> Biochemistry, 2011","statement":[{"text":"When presented as a Kratky plot, the SAXS profile of hNHE1 cdt increased throughout its range (Figure 2C), a pattern characteristic for unfolded proteins.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mguha","start":686,"term_ontology":"IDPO","curator_name":"Mainak Guharoy","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21425832","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":815,"region_id":"DP01241r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The intracellular distal tail of the Na+/H+ exchanger NHE1 is intrinsically disordered: implications for NHE1 trafficking. <i> Nørholm AB, Hendus-Altenburger R, Bjerre G, Kjaergaard M, Pedersen SF, Kragelund BB. </i> Biochemistry, 2011","statement":[{"text":"The secondary structure and overall fold analyses of hNHE1 cdt by far-UV CD spectroscopy showed a distinct minimum at ~200 nm and a shoulder at 220-230 nm, indicating the absence of regular secondary structures (Figure 2B).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mguha","start":686,"term_ontology":"IDPO","curator_name":"Mainak Guharoy","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21425832","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":795,"region_id":"DP01241r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A phosphorylation-motif for tuneable helix stabilisation in intrinsically disordered proteins - Lessons from the sodium proton exchanger 1 (NHE1). <i> Hendus-Altenburger R, Lambrughi M, Terkelsen T, Pedersen SF, Papaleo E, Lindorff-Larsen K, Kragelund BB. </i> Cell Signal, 2017","statement":[{"text":"The Δδircfor the phosphorylated state showed similar profile as for the unphosphorylated state,but with increased helicity for TH4.\nTo assess whether the local sequence is responsible for the stabilizing effect of phosphorylation and whether it is independent of the nearby T779 phosphorylation we next assigned the NMR chemical shifts of the TH4pepWTwith and without phosphorylation by natural abundance NMR spectroscopy.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"epapa","start":786,"term_ontology":"IDPO","curator_name":"Elena Papaleo","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28554535","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":795,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"A phosphorylation-motif for tuneable helix stabilisation in intrinsically disordered proteins - Lessons from the sodium proton exchanger 1 (NHE1). <i> Hendus-Altenburger R, Lambrughi M, Terkelsen T, Pedersen SF, Papaleo E, Lindorff-Larsen K, Kragelund BB. </i> Cell Signal, 2017","term_id":"IDPO:0000011","curator_id":"epapa","start":786,"term_ontology":"IDPO","curator_name":"Elena Papaleo","reference_id":"28554535","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01241r005","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":795,"term_name":"phosphorylation display site","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"A phosphorylation-motif for tuneable helix stabilisation in intrinsically disordered proteins - Lessons from the sodium proton exchanger 1 (NHE1). <i> Hendus-Altenburger R, Lambrughi M, Terkelsen T, Pedersen SF, Papaleo E, Lindorff-Larsen K, Kragelund BB. </i> Cell Signal, 2017","term_id":"IDPO:0000045","curator_id":"epapa","start":786,"term_ontology":"IDPO","curator_name":"Elena Papaleo","reference_id":"28554535","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01241r006","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":815,"region_id":"DP01241r007","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The intracellular distal tail of the Na+/H+ exchanger NHE1 is intrinsically disordered: implications for NHE1 trafficking. <i> Nørholm AB, Hendus-Altenburger R, Bjerre G, Kjaergaard M, Pedersen SF, Kragelund BB. </i> Biochemistry, 2011","statement":[{"text":"Finally, the [1H, 15N]-HSQC NMR spectrum of hNHE1 cdt showed a significant lack of dispersion in the proton dimension (Figure 2D), demonstrating in unison with the other data that the regulatory distal domain of NHE1 is intrinsically disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mguha","start":686,"term_ontology":"IDPO","curator_name":"Mainak Guharoy","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21425832","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":795,"region_id":"DP01241r008","released":"2022_03","ec_id":"ECO:0006204","reference_html":"A phosphorylation-motif for tuneable helix stabilisation in intrinsically disordered proteins - Lessons from the sodium proton exchanger 1 (NHE1). <i> Hendus-Altenburger R, Lambrughi M, Terkelsen T, Pedersen SF, Papaleo E, Lindorff-Larsen K, Kragelund BB. </i> Cell Signal, 2017","statement":[{"text":"While for all variants, including the WT peptide, the ellipticity at 190 nm increased uponphosphorylation, indicating less disorder, the negative ellipticity at 222 nm,indicating an increase in helicity, was only increased for the WT and theD784A variants. \nchange at 222 nm clearly indicated R790 to be important for conferring the phosphorylation-induced helix stabilisation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"epapa","start":786,"term_ontology":"IDPO","curator_name":"Elena Papaleo","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28554535","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":795,"term_name":"phosphorylation display site","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"A phosphorylation-motif for tuneable helix stabilisation in intrinsically disordered proteins - Lessons from the sodium proton exchanger 1 (NHE1). <i> Hendus-Altenburger R, Lambrughi M, Terkelsen T, Pedersen SF, Papaleo E, Lindorff-Larsen K, Kragelund BB. </i> Cell Signal, 2017","term_id":"IDPO:0000045","curator_id":"epapa","start":786,"term_ontology":"IDPO","curator_name":"Elena Papaleo","reference_id":"28554535","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01241r009","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":795,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"A phosphorylation-motif for tuneable helix stabilisation in intrinsically disordered proteins - Lessons from the sodium proton exchanger 1 (NHE1). <i> Hendus-Altenburger R, Lambrughi M, Terkelsen T, Pedersen SF, Papaleo E, Lindorff-Larsen K, Kragelund BB. </i> Cell Signal, 2017","term_id":"IDPO:0000011","curator_id":"epapa","start":786,"term_ontology":"IDPO","curator_name":"Elena Papaleo","reference_id":"28554535","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01241r010","ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":680,"end":815,"reference_id":"34439840","reference_source":"pmid","reference_html":"Insight into Calcium-Binding Motifs of Intrinsically Disordered Proteins. <i> Newcombe EA, Fernandes CB, Lundsgaard JE, Brakti I, Lindorff-Larsen K, Langkilde AE, Skriver K, Kragelund BB. </i> Biomolecules, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"IDPO:0000019","term_name":"disorder to pre-molten globule","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01241r011","statement":[{"text":"We found that the Rh of NHE1 reduced more severely by ~8 Å (25.6%) upon calcium addition (Figure 4C), again related to the position of the binding site at mid-sequence.","type":"Results"},{"text":"These data suggest that in some cases, the position of the Ca2+-binding site can affect the extension of the IDP by inducing a conformational shift, seen here for both NHE1 and ANAC046","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-07T13:13:45.917Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":745,"end":766,"reference_id":"34439840","reference_source":"pmid","reference_html":"Insight into Calcium-Binding Motifs of Intrinsically Disordered Proteins. <i> Newcombe EA, Fernandes CB, Lundsgaard JE, Brakti I, Lindorff-Larsen K, Langkilde AE, Skriver K, Kragelund BB. </i> Biomolecules, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007740","ec_ontology":"ECO","ec_name":"small molecule detection assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"ChEBI","id":"3312","partner_start":null,"partner_end":null}],"region_id":"DP01241r012","statement":[{"text":"NHE1680-815 similarly bound calcium at a 1:1 ratio (Figure 1G,I), again with micromolar affinity (~130 μM; Figure 1H).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-07T13:13:58.115Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":745,"end":766,"reference_id":"34439840","reference_source":"pmid","reference_html":"Insight into Calcium-Binding Motifs of Intrinsically Disordered Proteins. <i> Newcombe EA, Fernandes CB, Lundsgaard JE, Brakti I, Lindorff-Larsen K, Langkilde AE, Skriver K, Kragelund BB. </i> Biomolecules, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"ChEBI","id":"3312","partner_start":null,"partner_end":null}],"region_id":"DP01241r013","statement":[{"text":"Subsequently, we used the C-terminal disordered tail of the sodium-proton exchanger 1 (NHE1680-815) to address the interaction between calcium and a protein with high negative charge at the center of the sequence, finding that this was indeed the region (S745–S766) with the highest CSPs (Figure 1C).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-07T13:13:53.452Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P19634","date":"2018-07-03T13:35:21.000Z","acc":"P19634","name":"Sodium/hydrogen exchanger 1","length":815,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012FD1B","genes":[{"name":{"value":"SLC9A1"},"synonyms":[{"value":"APNH1"},{"value":"NHE1"}]}],"alphafold_very_low_content":0.2969325153374233,"disorder_content":0.1668711656441718,"disprot_consensus":{"full":[{"start":680,"end":815,"type":"T"}],"Structural state":[{"start":680,"end":815,"type":"D"}],"Structural transition":[{"start":680,"end":815,"type":"T"}],"Disorder function":[{"start":786,"end":795,"type":"F"}],"Molecular function":[{"start":745,"end":766,"type":"F"}]}},{"features":{"pfam":[{"id":"PF14559","name":"Tetratricopeptide repeat","start":14,"end":75}],"gene3D":[{"start":1,"end":111,"id":"1.25.40.10","name":"Tetratricopeptide repeat domain"}]},"uniref50":"UniRef50_P25638","sequence":"MSQFEKQKEQGNSLFKQGLYREAVHCYDQLITAQPQNPVGYSNKAMALIKLGEYTQAIQMCQQGLRYTSTAEHVAIRSKLQYRLELAQGAVGSVQIPVVEVDELPEGYDRS","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P25638","disprot_id":"DP01243","ncbi_taxon_id":559292,"regions_counter":4,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":111,"region_id":"DP01243r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of minimal tetratricopeptide repeat domain protein Tah1 reveals mechanism of its interaction with Pih1 and Hsp90. <i> Jiménez B, Ugwu F, Zhao R, Ortí L, Makhnevych T, Pineda-Lucena A, Houry WA. </i> J Biol Chem, 2012","statement":[{"text":"The last 20 C-terminal\nresidues of Tah1 (residues 92–111) are unstructured","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":92,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22179618","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":111,"region_id":"DP01243r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"High-resolution structural analysis shows how Tah1 tethers Hsp90 to the R2TP complex. <i> Back R, Dominguez C, Rothé B, Bobo C, Beaufils C, Moréra S, Meyer P, Charpentier B, Branlant C, Allain FH, Manival X. </i> Structure, 2013","statement":[{"text":"The 19-amino acid C-terminal region (positions 93–111)\nlocated immediately downstream from helix C displays the\ncharacteristic features of an unstructured region","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":93,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24012479","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":111,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"High-resolution structural analysis shows how Tah1 tethers Hsp90 to the R2TP complex. <i> Back R, Dominguez C, Rothé B, Bobo C, Beaufils C, Moréra S, Meyer P, Charpentier B, Branlant C, Allain FH, Manival X. </i> Structure, 2013","statement":[{"text":"Our NMR spectrum of the Tah1:Pih1(257–\n344) complex strongly suggests that the C-terminal part of\nTah1 folds upon interaction with Pih1.","type":"Discussion"}],"term_id":"IDPO:0000011","curator_id":"eschad","start":93,"term_ontology":"IDPO","curator_name":"Eva Schad","reference_id":"24012479","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01243r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":111,"term_name":"protein binding","released":"2025_12","ec_name":"yeast 2-hybrid evidence used in manual assertion","reference_html":"High-resolution structural analysis shows how Tah1 tethers Hsp90 to the R2TP complex. <i> Back R, Dominguez C, Rothé B, Bobo C, Beaufils C, Moréra S, Meyer P, Charpentier B, Branlant C, Allain FH, Manival X. </i> Structure, 2013","statement":[{"text":"Therefore, in Y2H assays, the short unstructured C-terminal region of Tah1 was sufficient to bind Pih1 and the strength of the interaction was similar to that for full-length Tah1.","type":"Results"}],"term_id":"GO:0005515","curator_id":"vnugnes","start":93,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"24012479","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2025-10-22T13:41:22.762Z","reference_source":"pmid","ec_id":"ECO:0005805","region_id":"DP01243r004","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P38768","operator":"and","partner_start":null,"partner_end":null}]}],"released":"2018_11","uniref100":"UniRef100_P25638","date":"2018-07-03T14:22:06.000Z","acc":"P25638","name":"TPR repeat-containing protein associated with Hsp90","length":111,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000013A726","genes":[{"name":{"value":"TAH1"},"orfNames":[{"value":"YCR60W"}],"olnNames":[{"value":"YCR060W"}]}],"alphafold_very_low_content":0.04504504504504504,"disorder_content":0.18018018018018017,"disprot_consensus":{"full":[{"start":92,"end":92,"type":"D"},{"start":93,"end":111,"type":"T"}],"Structural state":[{"start":92,"end":111,"type":"D"}],"Structural transition":[{"start":93,"end":111,"type":"T"}],"Molecular function":[{"start":93,"end":111,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00233","name":"3'5'-cyclic nucleotide phosphodiesterase","start":612,"end":845},{"id":"PF01590","name":"GAF domain","start":164,"end":312},{"id":"PF01590","name":"GAF domain","start":347,"end":501}],"gene3D":[{"start":130,"end":343,"id":"3.30.450.40","name":"3.30.450.40"},{"start":98,"end":519,"id":"3.30.450.40","name":"3.30.450.40"},{"start":535,"end":860,"id":"1.10.1300.10","name":"3'5'-cyclic nucleotide phosphodiesterase, catalytic domain"}]},"uniref50":"UniRef50_O76074","sequence":"MERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFTFSYFVRKATREMVNAWFAERVHTIPVCKEGIRGHTESCSCPLQQSPRADNSAPGTPTRKISASEFDRPLRPIVVKDSEGTVSFLSDSEKKEQMPLTPPRFDHDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSNDKFLISRLFDVAEGSTLEEVSNNCIRLEWNKGIVGHVAALGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIISFMQVQKCTIFIVDEDCSDSFSSVFHMECEELEKSSDTLTREHDANKINYMYAQYVKNTMEPLNIPDVSKDKRFPWTTENTGNVNQQCIRSLLCTPIKNGKKNKVIGVCQLVNKMEENTGKVKPFNRNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETRELQSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAELVATEFFDQGDRERKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCFPLLDGCRKNRQKWQALAEQQEKMLINGESGQAKRN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O76074","disprot_id":"DP01244","ncbi_taxon_id":9606,"regions_counter":3,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":145,"region_id":"DP01244r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Conformation changes, N-terminal involvement, and cGMP signal relay in the phosphodiesterase-5 GAF domain. <i> Wang H, Robinson H, Ke H. </i> J Biol Chem, 2010","statement":[{"text":"Most residues in the structures have a good electron density and are traced without ambiguity, except for disordered residues 128–145, 395–406, and 436–445 in subunit A and residues 131–146, 209–217, 395–408, and 435–446 in subunit B in both structures. In addition, residues 89–100 in the PDE5A89 structure are disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"gminervini","start":128,"term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"20861010","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3LFV"}],"term_name":"disorder","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":406,"region_id":"DP01244r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Conformation changes, N-terminal involvement, and cGMP signal relay in the phosphodiesterase-5 GAF domain. <i> Wang H, Robinson H, Ke H. </i> J Biol Chem, 2010","statement":[{"text":"Most residues in the structures have a good electron density and are traced without ambiguity, except for disordered residues 128–145, 395–406, and 436–445 in subunit A and residues 131–146, 209–217, 395–408, and 435–446 in subunit B in both structures. In addition, residues 89–100 in the PDE5A89 structure are disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"gminervini","start":395,"term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"20861010","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3LFV"}],"term_name":"disorder","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":850,"region_id":"DP01244r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Mechanism for the allosteric regulation of phosphodiesterase 2A deduced from the X-ray structure of a near full-length construct. <i> Pandit J, Forman MD, Fennell KF, Dillman KS, Menniti FS. </i> Proc Natl Acad Sci U S A, 2009","statement":[{"text":"Residues 840–850 of the M-loop have not been modeled due to disorder and are indicated by a dotted line","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"gminervini","start":840,"term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"19828435","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_O76074","date":"2018-07-03T14:56:32.000Z","acc":"O76074","name":"cGMP-specific 3',5'-cyclic phosphodiesterase","length":875,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000013D571","genes":[{"name":{"value":"PDE5A","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:8784","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8784"}}]},"synonyms":[{"value":"PDE5"}]}],"alphafold_very_low_content":0.10628571428571429,"disorder_content":0.046857142857142854,"disprot_consensus":{"full":[{"start":128,"end":145,"type":"D"},{"start":395,"end":406,"type":"D"},{"start":840,"end":850,"type":"D"}],"Structural state":[{"start":128,"end":145,"type":"D"},{"start":395,"end":406,"type":"D"},{"start":840,"end":850,"type":"D"}]}},{"acc":"P12823","sequence":"MNDQRKKARNTPFNMLKRERNRVSTVQQLTKRFSLGMLQGRGPLKLFMALVAFLRFLTIPPTAGILKRWGTIKKSKAINVLRGFRKEIGRMLNILNRRRRTAGMIIMLIPTVMAFHLTTRNGEPHMIVSRQEKGKSLLFKTKDGTNMCTLMAMDLGELCEDTITYKCPFLKQNEPEDIDCWCNSTSTWVTYGTCTTTGEHRREKRSVALVPHVGMGLETRTETWMSSEGAWKHAQRIETWILRHPGFTIMAAILAYTIGTTHFQRVLIFILLTAIAPSMTMRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPTLDFELIKTEAKQPATLRKYCIEAKLTNTTTDSRCPTQGEPTLNEEQDKRFVCKHSMVDRGWGNGCGLFGKGGIVTCAMFTCKKNMEGKIVQPENLEYTVVITPHSGEEHAVGNDTGKHGKEVKITPQSSITEAELTGYGTVTMECSPRTGLDFNEMVLLQMKDKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFTGHLKCRLRMDKLQLKGMSYSMCTGKFKVVKEIAETQHGTIVIRVQYEGDGSPCKTPFEIMDLEKRHVLGRLTTVNPIVTEKDSPVNIEAEPPFGDSYIIIGVEPGQLKLDWFKKGSSIGQMFETTMRGAKRMAILGDTAWDFGSLGGVFTSIGKALHQVFGAIYGAAFSGVSWTMKILIGVIITWIGMNSRSTSLSVSLVLVGIVTLYLGVMVQADSGCVVSWKNKELKCGSGIFVTDNVHTWTEQYKFQPESPSKLASAIQKAHEEGICGIRSVTRLENLMWKQITSELNHILSENEVKLTIMTGDIKGIMQVGKRSLRPQPTELRYSWKTWGKAKMLSTELHNQTFLIDGPETAECPNTNRAWNSLEVEDYGFGVFTTNIWLRLREKQDAFCDSKLMSAAIKDNRAVHADMGYWIESALNDTWKIEKASFIEVKSCHWPKSHTLWSNGVLESEMVIPKNFAGPVSQHNNRPGYHTQTAGPWHLGKLEMDFDFCEGTTVVVTEDCGNRGPSLRTTTASGKLITEWCCRSCTLPPLRYRGEDGCWYGMEIRPLKEKEENLVSSLVTAGHGQIDNFSLGILGMALFLEEMLRTRVGTKHAILLVAVSFVTLITGNMSFRDLGRVMVMVGATMTDDIGMGVTYLALLAAFKVRPTFAAGLLLRKLTSKELMMTTIGIVLLSQSSIPETILELTDALALGMMVLKMVRNMEKYQLAVTIMAILCVPNAVILQNAWKVSCTILAVVSVSPLFLTSSQQKADWIPLALTIKGLNPTAIFLTTLSRTSKKRSWPLNEAIMAVGMVSILASSLLKNDTPMTGPLVAGGLLTVCYVLTGRSADLELERATDVKWDDQAEISGSSPILSITISEDGSMSIKNEEEEQTLTILIRTGLLVISGLFPVSIPITAAAWYLWEVKKQRAGVLWDVPSPPPVGKAELEDGAYRIKQKGILGYSQIGAGVYKEGTFHTMWHVTRGAVLMHKGKRIEPSWADVKKDLISYGGGWKLEGEWKEGEEVQVLALEPGKNPRAVQTKPGLFRTNTGTIGAVSLDFSPGTSGSPIVDKKGKVVGLYGNGVVTRSGAYVSAIAQTEKSIEDNPEIEDDIFRKRRLTIMDLHPGAGKTKRYLPAIVREAIKRGLRTLILAPTRVVAAEMEEALRGLPIRYQTPAIRAEHTGREIVDLMCHATFTMRLLSPIRVPNYNLIIMDEAHFTDPASIAARGYISTRVEMGEAAGIFMTATPPGSRDPFPQSNAPIMDEEREIPERSWNSGHEWVTDFKGKTVWFVPSIKTGNDIAACLRKNGKRVIQLSRKTFDSEYVKTRTNDWDFVVTTDISEMGANFKAERVIDPRRCMKPVILTDGEERVILAGPMPVTHSSAAQRRGRIGRNPRNENDQYIYMGEPLENDEDCAHWKEAKMLLDNINTPEGIIPSMFEPEREKVDAIDGEYRLRGEARKTFVDLMRRGDLPVWLAYKVAAEGINYADRRWCFDGTRNNQILEENVEVEIWTKEGERKKLKPRWLDARIYSDPLALKEFAAGRKSLTLNLITEMGRLPTFMTQKARDALDNLAVLHTAEAGGKAYNHALSELPETLETLLLLTLLATVTGGIFLFLMSGRGIGKMTLGMCCIITASILLWYAQIQPHWIAASIILEFFLIVLLIPEPEKQRTPQDNQLTYVIIAILTVVAATMANEMGFLEKTKKDLGLGNIATQQPESNILDIDLRPASAWTLYAVATTFITPMLRHSIENSSVNVSLTAIANQATVLMGLGKGWPLSKMDIGVPLLAIGCYSQVNPITLTAALLLLVAHYAIIGPGLQAKATREAQKRAAAGIMKNPTVDGITVIDLDPIPYDPKFEKQLGQVMLLVLCVTQVLMMRTTWALCEALTLATGPVSTLWEGNPGRFWNTTIAVSMANIFRGSYLAGAGLLFSIMKNTTSTRRGTGNIGETLGEKWKSRLNALGKSEFQIYKKSGIQEVDRTLAKEGIKRGETDHHAVSRGSAKLRWFVERNLVTPEGKVVDLGCGRGGWSYYCGGLKNVREVKGLTKGGPGHEEPIPMSTYGWNLVRLQSGVDVFFVPPEKCDTLLCDIGESSPNPTVEAGRTLRVLNLVENWLNNNTQFCVKVLNPYMPSVIERMETLQRKYGGALVRNPLSRNSTHEMYWVSNASGNIVSSVNMISRMLINRFTMRHKKATYEPDVDLGSGTRNIGIESETPNLDIIGKRIEKIKQEHETSWHYDQDHPYKTWAYHGSYETKQTGSASSMVNGVVRLLTKPWDVVPMVTQMAMTDTTPFGQQRVFKEKVDTRTQEPKEGTKKLMKITAEWLWKELGKKKTPRMCTREEFTKKVRSNAALGAIFTDENKWKSAREAVEDSRFWELVDKERNLHLEGKCETCVYNMMGKREKKLGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWFSRENSLSGVEGEGLHKLGYILREVSKKEGGAMYADDTAGWDTRITIEDLKNEEMITNHMAGEHKKLAEAIFKLTYQNKVVRVQRPTPRGTVMDIISRRDQRGSGQVGTYGLNTFTNMEAQLIRQMEGEGIFKSIQHLTASEEIAVQDWLARVGRERLSRMAISGDDCVVKPLDDRFARALTALNDMGKVRKDIQQWEPSRGWNDWTQVPFCSHHFHELIMKDGRTLVVPCRNQDELIGRARISQGAGWSLRETACLGKSYAQMWSLMYFHRRDLRLAANAICSAVPSHWVPTSRTTWSIHASHEWMTTEDMLTVWNKVWILENPWMEDKTPVESWEEIPYLGKREDQWCGSLIGLTSRATWAKNIQTAINQVRSLIGNEEYTDYMPSMKRFRREEEEAGVLW","creator":"gbalatti","dataset":["Viral proteins","Neglected tropical diseases proteins","RNA-binding proteins"],"date":"2018-07-03T15:12:27.000Z","disprot_id":"DP01245","features":{"pfam":[{"id":"PF00869","name":"Flavivirus glycoprotein, central and dimerisation domains","start":282,"end":576},{"id":"PF00948","name":"Flavivirus non-structural Protein NS1","start":777,"end":1129},{"id":"PF00949","name":"Peptidase S7, Flavivirus NS3 serine protease","start":1492,"end":1643},{"id":"PF00972","name":"Flavivirus RNA-directed RNA polymerase, fingers and palm domains","start":2739,"end":3188},{"id":"PF01002","name":"Flavivirus non-structural protein NS2B","start":1349,"end":1475},{"id":"PF01003","name":"Flavivirus capsid protein C","start":5,"end":113},{"id":"PF01004","name":"Flavivirus envelope glycoprotein M","start":207,"end":279},{"id":"PF01005","name":"Flavivirus non-structural protein NS2A","start":1138,"end":1328},{"id":"PF01349","name":"Flavivirus non-structural protein NS4B","start":2241,"end":2481},{"id":"PF01350","name":"Flavivirus non-structural protein NS4A","start":2096,"end":2237},{"id":"PF01570","name":"Flavivirus polyprotein propeptide","start":120,"end":204},{"id":"PF01728","name":"FtsJ-like methyltransferase","start":2543,"end":2710},{"id":"PF02832","name":"Flavivirus glycoprotein, immunoglobulin-like domain","start":578,"end":673},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1658,"end":1805},{"id":"PF20483","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","start":3193,"end":3355},{"id":"PF20907","name":"Flavivirus NS3 helicase, C-terminal helical domain","start":1949,"end":2086},{"id":"PF21659","name":"Flavivirus envelope glycoprotein E, stem/anchor domain","start":676,"end":770}],"gene3D":[{"start":206,"end":280,"id":"1.10.8.970","name":"Flavivirus envelope glycoprotein M-like","_id":"685af523b4ac24d5329d8e58"},{"start":678,"end":775,"id":"1.20.1280.260","name":"1.20.1280.260","_id":"685af523b4ac24d5329d8e59"},{"start":115,"end":195,"id":"2.60.260.50","name":"Flavivirus polyprotein propeptide domain","_id":"685af523b4ac24d5329d8e5a"},{"start":574,"end":677,"id":"2.60.40.350","name":"2.60.40.350","_id":"685af523b4ac24d5329d8e5b"},{"start":21,"end":100,"id":"1.10.10.930","name":"1.10.10.930","_id":"685af523b4ac24d5329d8e5c"},{"start":342,"end":535,"id":"3.30.387.10","name":"Viral Envelope Glycoprotein, domain 3","_id":"685af523b4ac24d5329d8e5d"},{"start":283,"end":573,"id":"2.60.98.10","name":"Tick-borne Encephalitis virus Glycoprotein, domain 1","_id":"685af523b4ac24d5329d8e5e"},{"start":332,"end":554,"id":"3.30.67.10","name":"Viral Envelope Glycoprotein, domain 2","_id":"685af523b4ac24d5329d8e5f"},{"start":2759,"end":2823,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d8e60"},{"start":1496,"end":1564,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d8e61"},{"start":2489,"end":2758,"id":"3.40.50.150","name":"Vaccinia Virus protein VP39","_id":"685af523b4ac24d5329d8e62"},{"start":1658,"end":1991,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d8e63"},{"start":1469,"end":1642,"id":"2.40.10.10","name":"Trypsin-like serine proteases","_id":"685af523b4ac24d5329d8e64"},{"start":1389,"end":1452,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d8e65"},{"start":3017,"end":3084,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d8e66"},{"start":2882,"end":2977,"id":"1.10.260.90","name":"1.10.260.90","_id":"685af523b4ac24d5329d8e67"},{"start":1797,"end":1956,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d8e68"},{"start":2828,"end":2869,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d8e69"}]},"genes":[],"length":3388,"name":"Genome polyprotein","ncbi_taxon_id":11066,"organism":"Dengue virus type 2 (strain Puerto Rico/PR159-S1/1969)","regions_counter":17,"released":"2018_11","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Flavivirus"],"UniParc":"UPI0000131DFB","uniref100":"UniRef100_P12823","uniref50":"UniRef50_P17763","uniref90":"UniRef90_P29990","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1R6R","_id":"685af523b4ac24d5329d8e6c"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":20,"interaction_partner":[],"reference_html":"Partial Intrinsic Disorder Governs the Dengue Capsid Protein Conformational Ensemble. <i> Boon PLS, Saw WG, Lim XX, Raghuvamsi PV, Huber RG, Marzinek JK, Holdbrook DA, Anand GS, Grüber G, Bond PJ. </i> ACS Chem Biol, 2018","reference_id":"29792674","region_id":"DP01245r001","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"The NMR structure of DENV-2 C protein (PDB ID: 1R6R) reveals a homodimer that contains a well-folded core domain (residues 21–100) and a conformationally labile N-terminal region (residues 1–20), which is absent from the reported coordinates.","_id":"685af523b4ac24d5329d8e6b"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-07T08:15:22.803Z","_id":"685af523b4ac24d5329d8e6d"},"version":2,"_id":"685af523b4ac24d5329d8e6a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":20,"interaction_partner":[],"reference_html":"Partial Intrinsic Disorder Governs the Dengue Capsid Protein Conformational Ensemble. <i> Boon PLS, Saw WG, Lim XX, Raghuvamsi PV, Huber RG, Marzinek JK, Holdbrook DA, Anand GS, Grüber G, Bond PJ. </i> ACS Chem Biol, 2018","reference_id":"29792674","region_id":"DP01245r002","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"The N-terminal tails of the DENV C protein are essential for efficient viral particle formation as well as for recognition of different ligands during the life cycle of the virus","_id":"685af523b4ac24d5329d8e6f"}],"states_connection":[],"term_id":"IDPO:0000030","term_name":"entropic chain","term_namespace":"Disorder function","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-07T08:10:45.767Z","_id":"685af523b4ac24d5329d8e70"},"version":3,"_id":"685af523b4ac24d5329d8e6e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1R6R","_id":"685af523b4ac24d5329d8e72"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":21,"interaction_partner":[],"reference_html":"Flavivirus capsid is a dimeric alpha-helical protein. <i> Jones CT, Ma L, Burgner JW, Groesch TD, Post CB, Kuhn RJ. </i> J Virol, 2003","reference_id":"12768036","region_id":"DP01245r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The secondary structure of DEN2C is composed of four alpha helices. The most N-terminal helix (helix I, amino acids 26 to 31) is followed by a 14-residue loop and a second helix (helix II, amino acids 45 to 55). Helix II contains the start of an internal hydrophobic region that has been previously implicated in membrane association (underlined residues of DEN2C sequence in Fig. ​Fig.4B).4B). Following helix II is a loop region (amino acids 56 to 62) that is followed by helix III (amino acids 63 to 69) and then a fourth short loop region (amino acids 70 to 73). The longest helix in DEN2C (helix IV) occurs at the C terminus of the protein (amino acids 74 to 96). The N terminus of DEN2C (amino acids 1 to 21) does not appear to possess secondary structure.","_id":"685af523b4ac24d5329d8e73"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T13:14:20.335Z","_id":"685af523b4ac24d5329d8e74"},"version":1,"_id":"685af523b4ac24d5329d8e71","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":13,"interaction_partner":[],"reference_html":"Flavivirus capsid is a dimeric alpha-helical protein. <i> Jones CT, Ma L, Burgner JW, Groesch TD, Post CB, Kuhn RJ. </i> J Virol, 2003","reference_id":"12768036","region_id":"DP01245r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The alpha-helical nature of the C protein was confirmed experimentally by far-UV circular dichroism (CD). The far-UV CD spectra of both YFC and DEN2C demonstrated characteristics of alpha-helical proteins with local minima at 222 and 208 and a maximum at 190 nm (data not shown). In addition, the far-UV CD spectra for DEN2CΔ1-13 was essentially identical to that for DEN2C, indicating that removal of the first 13 residues did not significantly perturb the secondary structure of DEN2C (data not shown).","_id":"685af523b4ac24d5329d8e76"}],"states_connection":[],"term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T13:16:07.003Z","_id":"685af523b4ac24d5329d8e77"},"version":1,"_id":"685af523b4ac24d5329d8e75","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-11-24T12:19:10.685Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":14,"end":23,"interaction_partner":[],"reference_html":"The disordered N-terminal region of dengue virus capsid protein contains a lipid-droplet-binding motif. <i> Martins IC, Gomes-Neto F, Faustino AF, Carvalho FA, Carneiro FA, Bozza PT, Mohana-Borges R, Castanho MA, Almeida FC, Santos NC, Da Poian AT. </i> Biochem J, 2012","reference_id":"22428600","region_id":"DP01245r007","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"The Hα chemical shift changes promoted by the presence of LDs were quantified, showing that the highest changes occurred for the resonances of Asn1, Met2 and Leu3.","_id":"685af523b4ac24d5329d8e80"},{"type":"Results","text":"To evaluate whether binding of pep14–23 to LDs was also dependent on a surface protein, LD limited proteolysis was performed before zeta potential measurements. As previously observed for C protein, LD trypsinization eliminated the ability of pep14–23 to interact with LDs (Figure 4).","_id":"685af523b4ac24d5329d8e81"},{"type":"Curator statement","text":"Authors show this fragment binds to an unidentified  protein present in lipid droplets from BHK cells.","_id":"685af523b4ac24d5329d8e82"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-11-24T12:37:34.579Z","_id":"685af523b4ac24d5329d8e83"},"version":3,"_id":"685af523b4ac24d5329d8e7f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1L9K","_id":"685af523b4ac24d5329d8e85"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":2756,"end":2784,"interaction_partner":[],"reference_html":"An RNA cap (nucleoside-2'-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization. <i> Egloff MP, Benarroch D, Selisko B, Romette JL, Canard B. </i> EMBO J, 2002","reference_id":"12032088","region_id":"DP01245r008","released":"2022_03","sample":[{"db":"ENA","deviation":null,"id":"1963","statements":[{"type":"Curator statement","text":"Crystals were soaked in a solution containing β,γ-methylene GTP (GDPMP), a non-hydrolysable GTP analogue.","_id":"685af523b4ac24d5329d8e87"}],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":2,"_id":"685af523b4ac24d5329d8e86"}],"sequence_construct":"GTGNIGETLGEKWKSRLNALGKSEFQIYKKSGIQEVDRTLAKEGIKRGETDHHAVSRGSAKLRWFVERNLVTPEGKVVDLGCGRGGWSYYCGGLKNVREVKGLTKGGPGHEEPIPMSTYGWNLVRLQSGVDVFFVPPEKCDTLLCDIGESSPNPTVEAGRTLRVLNLVENWLNNNTQFCVKVLNPYMPSVIERMETLQRKYGGALVRNPLSRNSTHEMYWVS NASGNIVSSVNMISRMLINRFTMRHKKATYEPDVDLGSGTRNIGIESETPNLDIIGKRIEKIKQEHETSWHYDQ","statement":[{"type":"Results","text":"Mass spectrometry analysis of dissolved NS5MTaseDV crystals showed that the C-terminus missing in the structure is present in the crystallized protein. Thus, the C-terminal part appears to be flexible, probably due to the absence of the polymerase domain of NS5.","_id":"685af523b4ac24d5329d8e88"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-07T08:12:50.368Z","_id":"685af523b4ac24d5329d8e89"},"version":1,"_id":"685af523b4ac24d5329d8e84","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-20T15:36:40.414Z","disprot_namespace":"Structural state","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1489,"end":1660,"interaction_partner":[],"reference_html":"NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics. <i> Gupta G, Lim L, Song J. </i> PLoS One, 2015","reference_id":"26258523","region_id":"DP01245r009","released":"2022_12","sample":[],"statement":[{"type":"Results","text":"As shown in Fig 1A, NS3pro has very similar far-UV CD spectra in Milli-Q water (pH 4.0) and 5 mM phosphate buffer (pH 7.0), with the maximal negative signal at 200 nm and no positive signal below 200 nm, which is typical of a predominantly disordered protein without any stable secondary structure.","_id":"685af523b4ac24d5329d8e8b"},{"type":"Curator statement","text":"The NS3pro 14-185 region corresponds to the 1489-1660 region of the polyprotein.","_id":"685af523b4ac24d5329d8e8c"},{"type":"Results","text":"Taken together, CD and NMR results define the 172-residue NS3pro domain to be an intrinsically disordered protein which is lacking of both stable secondary and tertiary structures in the absence of the NS2B cofactor [22,31–36].","_id":"685af523b4ac24d5329d8e8d"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-15T17:10:11.105Z","_id":"685af523b4ac24d5329d8e8e"},"version":0,"_id":"685af523b4ac24d5329d8e8a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-20T15:36:23.120Z","disprot_namespace":"Structural state","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1489,"end":1660,"interaction_partner":[],"reference_html":"NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics. <i> Gupta G, Lim L, Song J. </i> PLoS One, 2015","reference_id":"26258523","region_id":"DP01245r010","released":"2022_12","sample":[],"statement":[{"type":"Results","text":"Moreover, it has a HSQC spectrum with very narrow spectral dispersions at both 1H (~0.9 ppm) and 15N (~19 ppm) dimensions (Fig 1B), further indicating the absence of tight tertiary packing.","_id":"685af523b4ac24d5329d8e90"},{"type":"Results","text":"Taken together, CD and NMR results define the 172-residue NS3pro domain to be an intrinsically disordered protein which is lacking of both stable secondary and tertiary structures in the absence of the NS2B cofactor [22,31–36].","_id":"685af523b4ac24d5329d8e91"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-15T17:10:13.938Z","_id":"685af523b4ac24d5329d8e92"},"version":0,"_id":"685af523b4ac24d5329d8e8f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-20T15:37:24.952Z","disprot_namespace":"Structural transition","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1489,"end":1660,"interaction_partner":[],"reference_html":"NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics. <i> Gupta G, Lim L, Song J. </i> PLoS One, 2015","reference_id":"26258523","region_id":"DP01245r011","released":"2022_12","sample":[{"db":"UniProt","deviation":null,"id":"P12823","statements":[{"type":"Curator statement","text":"The NS2B protein corresponds to the \t1346-1475 region of the Dengue virus type 2 (strain Puerto Rico/PR159-S1/1969).","_id":"685af523b4ac24d5329d8e95"}],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d8e94"}],"statement":[{"type":"Results","text":"The NS3pro domain in complex with NS2B has very large (ΔCα-ΔCβ) deviations characteristic of a well-folded protein.","_id":"685af523b4ac24d5329d8e96"},{"type":"Results","text":"Taken together, CD and NMR results define the 172-residue NS3pro domain to be an intrinsically disordered protein which is lacking of both stable secondary and tertiary structures in the absence of the NS2B cofactor [22,31–36].","_id":"685af523b4ac24d5329d8e97"},{"type":"Curator statement","text":"The NS3pro 14-185 region corresponds to the 1489-1660 region of the polyprotein.","_id":"685af523b4ac24d5329d8e98"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-15T17:10:17.047Z","_id":"685af523b4ac24d5329d8e99"},"version":0,"_id":"685af523b4ac24d5329d8e93","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-20T15:38:13.178Z","disprot_namespace":"Structural transition","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1489,"end":1660,"interaction_partner":[],"reference_html":"NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics. <i> Gupta G, Lim L, Song J. </i> PLoS One, 2015","reference_id":"26258523","region_id":"DP01245r012","released":"2022_12","sample":[{"db":"UniProt","deviation":null,"id":"P12823","statements":[{"type":"Curator statement","text":"The NS2B protein corresponds to the \t1346-1475 region of the Dengue virus type 2 (strain Puerto Rico/PR159-S1/1969).","_id":"685af523b4ac24d5329d8e9c"}],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d8e9b"}],"statement":[{"type":"Results","text":"The isolated NS3pro (14–185) and NS2B (48–100) are largely disordered in solution (Fig 3A) and the NS3pro alone showed no detectable catalytic activity even with a protease concentration up to 5 μM in buffers at pH 7.5 (Fig 3B). However, upon mixing them at an equal molar ratio in Milli-Q water at pH 4.0, the mixture has a CD spectrum for a protein with a substantial amount of secondary structures, which has a large positive signal at 190 nm and the maximal negative signal at 208 nm (Fig 3A).","_id":"685af523b4ac24d5329d8e9d"},{"type":"Curator statement","text":"The NS3pro 14-185 region corresponds to the 1489-1660 region of the polyprotein.","_id":"685af523b4ac24d5329d8e9e"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-15T17:10:25.502Z","_id":"685af523b4ac24d5329d8e9f"},"version":0,"_id":"685af523b4ac24d5329d8e9a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-20T15:42:56.461Z","disprot_namespace":"Structural state","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1393,"end":1445,"interaction_partner":[],"reference_html":"NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics. <i> Gupta G, Lim L, Song J. </i> PLoS One, 2015","reference_id":"26258523","region_id":"DP01245r013","released":"2022_12","sample":[],"statement":[{"type":"Results","text":"Unfortunately, HSQC peaks of the NS2B (48–100) are much more broadened than those of NS3pro, implying that the isolated NS2B (48–100) has dynamic aggregation or/and conformational exchanges on the μs-ms time scale, thus preventing from further high-resolution NMR studies","_id":"685af523b4ac24d5329d8ea1"},{"type":"Curator statement","text":"The NS2B 48-100 region corresponds to the 1393-1445 region of the polyprotein.","_id":"685af523b4ac24d5329d8ea2"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-15T17:10:14.619Z","_id":"685af523b4ac24d5329d8ea3"},"version":0,"_id":"685af523b4ac24d5329d8ea0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-20T15:44:13.893Z","disprot_namespace":"Structural state","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1393,"end":1445,"interaction_partner":[],"reference_html":"NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics. <i> Gupta G, Lim L, Song J. </i> PLoS One, 2015","reference_id":"26258523","region_id":"DP01245r014","released":"2022_12","sample":[],"statement":[{"type":"Results","text":"Interestingly, on the other hand, NS2B (48–100) has a CD spectrum with the maximal negative signal at 206 nm and positive signal at 190 nm, as well as an additional negative signal at 222 nm.","_id":"685af523b4ac24d5329d8ea5"},{"type":"Curator statement","text":"The NS2B 48-100 region corresponds to the 1393-1445 region of the polyprotein.","_id":"685af523b4ac24d5329d8ea6"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d8ea4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-20T15:47:52.292Z","disprot_namespace":"Structural transition","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1393,"end":1445,"interaction_partner":[],"reference_html":"NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics. <i> Gupta G, Lim L, Song J. </i> PLoS One, 2015","reference_id":"26258523","region_id":"DP01245r015","released":"2022_12","sample":[{"db":"UniProt","deviation":null,"id":"P12823","statements":[{"type":"Curator statement","text":"The NS3pro 14-185 region corresponds to the 1489-1660 region of the Dengue virus type 2 (strain Puerto Rico/PR159-S1/1969) polyprotein.","_id":"685af523b4ac24d5329d8ea9"}],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d8ea8"}],"statement":[{"type":"Results","text":"The isolated NS3pro (14–185) and NS2B (48–100) are largely disordered in solution (Fig 3A) and the NS3pro alone showed no detectable catalytic activity even with a protease concentration up to 5 μM in buffers at pH 7.5 (Fig 3B). However, upon mixing them at an equal molar ratio in Milli-Q water at pH 4.0, the mixture has a CD spectrum for a protein with a substantial amount of secondary structures, which has a large positive signal at 190 nm and the maximal negative signal at 208 nm (Fig 3A).","_id":"685af523b4ac24d5329d8eaa"},{"type":"Curator statement","text":"The NS2B 48-100 region corresponds to the 1393-1445 region of the polyprotein.","_id":"685af523b4ac24d5329d8eab"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-15T17:10:26.688Z","_id":"685af523b4ac24d5329d8eac"},"version":0,"_id":"685af523b4ac24d5329d8ea7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-20T19:02:49.837Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1393,"end":1445,"interaction_partner":[{"db":"UniProt","id":"P12823","operator":null,"partner_start":1489,"partner_end":1660,"_id":"685af523b4ac24d5329d8eae"}],"reference_html":"NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics. <i> Gupta G, Lim L, Song J. </i> PLoS One, 2015","reference_id":"26258523","region_id":"DP01245r016","released":"2022_12","sample":[],"statement":[{"type":"Results","text":"The NS3pro domain in complex with NS2B has very large (ΔCα-ΔCβ) deviations characteristic of a well-folded protein.","_id":"685af523b4ac24d5329d8eaf"},{"type":"Curator statement","text":"The NS3pro 14-185 region corresponds to the 1489-1660 region of the polyprotein. while the NS2B 48-100 region corresponds to the 1393-1445 region of the polyprotein.","_id":"685af523b4ac24d5329d8eb0"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-15T17:10:33.976Z","_id":"685af523b4ac24d5329d8eb1"},"version":0,"_id":"685af523b4ac24d5329d8ead","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-20T19:03:24.631Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1489,"end":1660,"interaction_partner":[{"db":"UniProt","id":"P12823","operator":null,"partner_start":1393,"partner_end":1445,"_id":"685af523b4ac24d5329d8eb3"}],"reference_html":"NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics. <i> Gupta G, Lim L, Song J. </i> PLoS One, 2015","reference_id":"26258523","region_id":"DP01245r017","released":"2022_12","sample":[],"statement":[{"type":"Results","text":"The NS3pro domain in complex with NS2B has very large (ΔCα-ΔCβ) deviations characteristic of a well-folded protein.","_id":"685af523b4ac24d5329d8eb4"},{"type":"Curator statement","text":"The NS3pro 14-185 region corresponds to the 1489-1660 region of the polyprotein. while the NS2B 48-100 region corresponds to the 1393-1445 region of the polyprotein.","_id":"685af523b4ac24d5329d8eb5"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-15T17:10:36.406Z","_id":"685af523b4ac24d5329d8eb6"},"version":0,"_id":"685af523b4ac24d5329d8eb2","reference_source":"pmid"}],"__v":0,"disorder_content":0.08116883116883117,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"},{"start":22,"end":23,"type":"F"},{"start":1393,"end":1445,"type":"T"},{"start":1489,"end":1660,"type":"T"},{"start":2756,"end":2784,"type":"D"}],"Structural state":[{"start":1,"end":21,"type":"D"},{"start":1393,"end":1445,"type":"D"},{"start":1489,"end":1660,"type":"D"},{"start":2756,"end":2784,"type":"D"}],"Disorder function":[{"start":1,"end":20,"type":"F"}],"Molecular function":[{"start":14,"end":23,"type":"F"},{"start":1393,"end":1445,"type":"F"},{"start":1489,"end":1660,"type":"F"}],"Structural transition":[{"start":1393,"end":1445,"type":"T"},{"start":1489,"end":1660,"type":"T"}]}},{"features":{"pfam":[{"id":"PF10471","name":"Anaphase-promoting complex APC subunit CDC26","start":1,"end":45}]},"uniref50":"UniRef50_O13916","sequence":"MLRRNPTAIQITAEDVLAYDEEKLRQTLDSESTTEEALQKNEESTRLSPEKKKIIRERRIGITQIFDSSMHPSQGGAAQS","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"uniref90":"UniRef90_O13916","disprot_id":"DP01246","ncbi_taxon_id":284812,"regions_counter":1,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":80,"region_id":"DP01246r001","released":"2026_06","ec_id":"ECO:0006220","reference_html":"The APC/C subunit Cdc16/Cut9 is a contiguous tetratricopeptide repeat superhelix with a homo-dimer interface similar to Cdc27. <i> Zhang Z, Kulkarni K, Hanrahan SJ, Thompson AJ, Barford D. </i> EMBO J, 2010","statement":[{"text":"Full-length Hcn1 was co-crystallized with Cut9; however, only residues 1–24 are clearly visible in the electron density map, and thus the lack of density for residues 25–80 indicates structural disorder.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":25,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"20924356","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2025-12-15T18:22:11.450Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"2XPI"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"}],"released":"2018_11","uniref100":"UniRef100_O13916","date":"2018-07-03T15:22:54.000Z","acc":"O13916","name":"Anaphase-promoting complex subunit hcn1","length":80,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","dataset":[],"UniParc":"UPI000013AA40","genes":[{"name":{"value":"hcn1"},"orfNames":[{"value":"SPAC23C11.12"}]}],"alphafold_very_low_content":0.1125,"disorder_content":0.7,"disprot_consensus":{"full":[{"start":25,"end":80,"type":"D"}],"Structural state":[{"start":25,"end":80,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00635","name":"MSP (Major sperm protein) domain","start":8,"end":110}],"gene3D":[{"start":1,"end":125,"id":"2.60.40.10","name":"Immunoglobulins"}]},"uniref50":"UniRef50_O95292","sequence":"MAKVEQVLSLEPQHELKFRGPFTDVVTTNLKLGNPTDRNVCFKVKTTAPRRYCVRPNSGIIDAGASINVSVMLQPFDYDPNEKSKHKFMVQSMFAPTDTSDMEAVWKEAKPEDLMDSKLRCVFELPAENDKPHDVEINKIISTTASKTETPIVSKSLSSSLDDTEVKKVMEECKRLQGEVQRLREENKQFKEEDGLRMRKTVQSNSPISALAPTGKEEGLSTRLLALVVLFFIVGVIIGKIAL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O95292","disprot_id":"DP01248","ncbi_taxon_id":9606,"regions_counter":8,"creator":"jmanso","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":125,"region_id":"DP01248r001","released":"2024_12","ec_id":"ECO:0006204","reference_html":"Elimination of the native structure and solubility of the hVAPB MSP domain by the Pro56Ser mutation that causes amyotrophic lateral sclerosis. <i> Shi J, Lua S, Tong JS, Song J. </i> Biochemistry, 2010","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-12-09T15:09:23.174Z","reference_source":"pmid","term_name":"disorder","reference_id":"20377183","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro56Ser","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To address the consequence of the ALS-causing Pro56Ser mutation, we generated the Pro56Ser mutant of the hVAPB MSP domain by using site-directed mutagenesis."}]}],"statement":[{"text":"The Pro56Ser mutated version of this peptide, associated with Amyotrophic Lateral Sclerosis (ALS), is intrinsically disordered in solution at pH 3.5–5.5, and aggregates at pH 6.5 due to a loss of stability.","type":"Curator statement"},{"text":"As shown in Figure 4a, at pH 3.5 the Pro56Ser MSP domain has a far-UV CD spectrum characteristic of a predominantly unstructured protein, with its maximal negative signal at ∼199 nm and without any positive signal (30). Interestingly, the overall shapes of the CD curves are very similar at pH 3.5, 4.5, and 5.5, indicating that the mutant remains highly unstructured even at pH 5.5.","type":"Results"}],"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":3.5},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":4.5},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":5.5}]},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":125,"term_name":"order to disorder","released":"2024_12","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Elimination of the native structure and solubility of the hVAPB MSP domain by the Pro56Ser mutation that causes amyotrophic lateral sclerosis. <i> Shi J, Lua S, Tong JS, Song J. </i> Biochemistry, 2010","statement":[{"text":"When the Proline 56 residue is mutated to Serine, variant associated with Amyotrophic Lateral Sclerosis (ALS), the MSP domain loses its native structure and stability, becoming disodered.","type":"Curator statement"},{"text":"As shown in Figure 4a, at pH 3.5 the Pro56Ser MSP domain has a far-UV CD spectrum characteristic of a predominantly unstructured protein, with its maximal negative signal at ∼199 nm and without any positive signal (30). Interestingly, the overall shapes of the CD curves are very similar at pH 3.5, 4.5, and 5.5, indicating that the mutant remains highly unstructured even at pH 5.5.","type":"Results"},{"text":"As shown in Figure 4b, the overall shapes of the CD spectra are still similar at various pH values and salt concentrations up to 10 mM, indicating that the mutant remains similarly disordered under these conditions. However, when the pH value reached 6.5 for the sample containing 10 mM salt, the protein precipitated immediately, and consequently, the CD signal disappeared (Figure 4b).","type":"Results"}],"term_id":"IDPO:0000014","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"20377183","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-12-09T15:25:10.905Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01248r002","ec_go":"EXP","disprot_namespace":"Structural transition","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro56Ser","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To address the consequence of the ALS-causing Pro56Ser mutation, we generated the Pro56Ser mutant of the hVAPB MSP domain by using site-directed mutagenesis."}]}],"states_connection":[{"source":"DP01248r007","target":"DP01248r001"}]},{"start":125,"end":150,"reference_id":"22720086","reference_source":"pmid","reference_html":"Intrinsically unstructured domain 3 of hepatitis C Virus NS5A forms a \"fuzzy complex\" with VAPB-MSP domain which carries ALS-causing mutations. <i> Gupta G, Qin H, Song J. </i> PLoS One, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01248r003","statement":[{"text":"On the other hand, VAPB(1–150) has a far-UV CD spectrum similar to that of VAPB(1–125) which was previously characterized to adopt a β-dominant MSP fold [46]. This observation implies that the extra C-terminal 25 residues in VAPB(1–150) is largely unstructured and its presence does not alter the MSP-fold.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":125,"end":150,"reference_id":"22720086","reference_source":"pmid","reference_html":"Intrinsically unstructured domain 3 of hepatitis C Virus NS5A forms a \"fuzzy complex\" with VAPB-MSP domain which carries ALS-causing mutations. <i> Gupta G, Qin H, Song J. </i> PLoS One, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01248r004","statement":[{"text":"Furthermore, as shown in Figure 1d, most HSQC peaks of VAPB(1–125) are also superimposable to those of VAPB(1–150), indicating that the C-terminal 25 residues of VAPB(1–150) have no significant packing with the MSP fold assumed by the N-terminal 125 residues [46]. Taken together, CD and NMR results demonstrate that VAPB(1–195) is composed two structural domains, namely the well-folded β-dominant MSP fold and helical VAPB-CC linked by the flexible loop.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":1,"end":125,"reference_id":"20377183","reference_source":"pmid","reference_html":"Elimination of the native structure and solubility of the hVAPB MSP domain by the Pro56Ser mutation that causes amyotrophic lateral sclerosis. <i> Shi J, Lua S, Tong JS, Song J. </i> Biochemistry, 2010","date":"2024-12-09T15:10:15.948Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":5.5},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":4.5},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":3.5}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro56Ser","start":null,"end":null,"position":null}],"region_id":"DP01248r005","statement":[{"text":"The Pro56Ser mutated version of this peptide, associated with Amyotrophic Lateral Sclerosis (ALS), is intrinsically disordered in solution at pH 3.5–5.5, and aggregates at pH 6.5 due to a loss of stability.","type":"Curator statement"},{"text":"As one can see in Figure 4c, at pH 3.5, the mutant has a HSQC spectrum characteristic of an unfolded protein without any tight tertiary packing, with only 0.8 and 11 ppm dispersions over the 1H and 15N dimensions, respectively (43-46), consistent with the CD results.","type":"Results"},{"text":"It is thus interesting to investigate whether the mutant might have a conformational ensemble similar to that of the unfolded population of the wild type at pH 3.5. However, unlike the wild-type MSP domain which could reversibly fold back at pH >4.5, the Pro56Ser mutant at pH 4.5 and 5.5 still remains highly unstructured as no significant dispersion change is observed for their HSQC spectra (Figure 4d,e). At pH 6.5, the protein completely aggregated, and consequently, no HSQC peaks could be detected (data not shown).","type":"Results"}]},{"start":1,"end":125,"reference_id":"20377183","reference_source":"pmid","reference_html":"Elimination of the native structure and solubility of the hVAPB MSP domain by the Pro56Ser mutation that causes amyotrophic lateral sclerosis. <i> Shi J, Lua S, Tong JS, Song J. </i> Biochemistry, 2010","date":"2024-12-09T15:24:53.877Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro56Ser","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To address the consequence of the ALS-causing Pro56Ser mutation, we generated the Pro56Ser mutant of the hVAPB MSP domain by using site-directed mutagenesis."}]}],"region_id":"DP01248r006","statement":[{"text":"When the Proline 56 residue is mutated to Serine, variant associated with Amyotrophic Lateral Sclerosis (ALS), the MSP domain loses its native structure and stability, becoming disodered.","type":"Curator statement"},{"text":"As one can see in Figure 4c, at pH 3.5, the mutant has a HSQC spectrum characteristic of an unfolded protein without any tight tertiary packing, with only 0.8 and 11 ppm dispersions over the 1H and 15N dimensions, respectively (43-46), consistent with the CD results.","type":"Results"},{"text":"It is thus interesting to investigate whether the mutant might have a conformational ensemble similar to that of the unfolded population of the wild type at pH 3.5. However, unlike the wild-type MSP domain which could reversibly fold back at pH >4.5, the Pro56Ser mutant at pH 4.5 and 5.5 still remains highly unstructured as no significant dispersion change is observed for their HSQC spectra (Figure 4d,e). At pH 6.5, the protein completely aggregated, and consequently, no HSQC peaks could be detected (data not shown).","type":"Results"}],"states_connection":[{"source":"DP01248r008","target":"DP01248r005"}]},{"start":1,"end":125,"reference_id":"20377183","reference_source":"pmid","reference_html":"Elimination of the native structure and solubility of the hVAPB MSP domain by the Pro56Ser mutation that causes amyotrophic lateral sclerosis. <i> Shi J, Lua S, Tong JS, Song J. </i> Biochemistry, 2010","date":"2024-12-09T15:23:31.156Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP01248r007","statement":[{"text":"As shown in Figure 1b, at pH 6.5, the wild-type MSP domain has a far-UV CD spectrum typical of β-dominant secondary structure, with the maximal negative signal at ∼218 nm and the positive signal at ∼199 nm (32).","type":"Results"}]},{"start":1,"end":125,"reference_id":"20377183","reference_source":"pmid","reference_html":"Elimination of the native structure and solubility of the hVAPB MSP domain by the Pro56Ser mutation that causes amyotrophic lateral sclerosis. <i> Shi J, Lua S, Tong JS, Song J. </i> Biochemistry, 2010","date":"2024-12-09T15:24:15.855Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP01248r008","statement":[{"text":"Consistent with the CD results, at neutral pH the wild-type MSP domain has a HSQC spectrum typical of a well-folded protein (Figure 1c), with 3.2 and 26 ppm spectral dispersions over the 1H and 15N dimensions, respectively.","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_O95292","date":"2018-07-03T18:06:30.000Z","acc":"O95292","name":"Vesicle-associated membrane protein-associated protein B/C","length":243,"organism":"Homo sapiens","dataset":["Age-related disorders proteins"],"UniParc":"UPI0000048ED2","genes":[{"name":{"value":"VAPB"},"orfNames":[{"value":"UNQ484/PRO983"}]}],"alphafold_very_low_content":0.205761316872428,"disorder_content":0.6172839506172839,"disprot_consensus":{"full":[{"start":1,"end":125,"type":"T"},{"start":126,"end":150,"type":"D"}],"Structural state":[{"start":1,"end":150,"type":"D"}],"Structural transition":[{"start":1,"end":125,"type":"T"}],"Disorder function":[{"start":125,"end":150,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00001","name":"7 transmembrane receptor (rhodopsin family)","start":55,"end":302},{"id":"PF12109","name":"CXCR4 Chemokine receptor N terminal","start":6,"end":37}],"gene3D":[{"start":28,"end":303,"id":"1.20.1070.10","name":"Rhodopsin 7-helix transmembrane proteins"}]},"uniref50":"UniRef50_P61073","sequence":"MEGISIYTSDNYTEEMGSGDYDSMKEPCFREENANFNKIFLPTIYSIIFLTGIVGNGLVILVMGYQKKLRSMTDKYRLHLSVADLLFVITLPFWAVDAVANWYFGNFLCKAVHVIYTVNLYSSVLILAFISLDRYLAIVHATNSQRPRKLLAEKVVYVGVWIPALLLTIPDFIFANVSEADDRYICDRFYPNDLWVVVFQFQHIMVGLILPGIVILSCYCIIISKLSHSKGHQKRKALKTTVILILAFFACWLPYYIGISIDSFILLEIIKQGCEFENTVHKWISITEALAFFHCCLNPILYAFLGAKFKTSAQHALTSVSRGSSLKILSKGKRGGHSSVSTESESSSFHSS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P61073","disprot_id":"DP01249","ncbi_taxon_id":9606,"regions_counter":7,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":26,"region_id":"DP01249r001","released":"2022_06","ec_id":"ECO:0006220","reference_html":"Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists. <i> Wu B, Chien EY, Mol CD, Fenalti G, Liu W, Katritch V, Abagyan R, Brooun A, Wells P, Bi FC, Hamel DJ, Kuhn P, Handel TM, Cherezov V, Stevens RC. </i> Science, 2010","statement":[{"text":"The 26 N-terminal residues of CXCR4 did not have interpretable density and are presumed to be disordered","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-15T18:45:13.954Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3OE8"},{"db":"PDB","id":"3ODU"}],"reference_id":"20929726","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":24,"reference_id":"20929726","reference_source":"pmid","reference_html":"Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists. <i> Wu B, Chien EY, Mol CD, Fenalti G, Liu W, Katritch V, Abagyan R, Brooun A, Wells P, Bi FC, Hamel DJ, Kuhn P, Handel TM, Cherezov V, Stevens RC. </i> Science, 2010","date":"2022-06-15T18:31:34.024Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP01249r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting CXC chemokine receptor antagonist peptide with sequence RRACYQKPPYRRCRGP."}]}],"sequence_construct":"DYKDDDDAGAPEGISIYTSDNYTEEMGSGDYDSMKEPCFREENANFNKIFLPTIYSIIFLTGIVGNGLVILVMGYQKKLRSMTDKYRLHLSVADLLFVITLPFWAVDAVANWYFGNFLCKAVHVIYTVNLYSSVWILAFISLDRYLAIVHATNSQRPRKLLAEKVVYVGVWIPALLLTIPDFIFANVSEADDRYICDRFYPNDLWVVVFQFQHIMVGLILPGIVILSCYCIIISKLSHNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYSGSGHQKRKALKPTVILILAFFACWLPYYIGISIDSFILLEIIKQGCEFENTVHKWISITEALAFFHCCLNPILYAFLGAKFKTSAQHALTSGRPLEVLFQ","statement":[{"text":"The lack of electron density in this region indicates disorder. ","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"3OE0"}]},{"start":304,"end":319,"reference_id":"20929726","reference_source":"pmid","reference_html":"Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists. <i> Wu B, Chien EY, Mol CD, Fenalti G, Liu W, Katritch V, Abagyan R, Brooun A, Wells P, Bi FC, Hamel DJ, Kuhn P, Handel TM, Cherezov V, Stevens RC. </i> Science, 2010","date":"2022-06-15T18:34:56.288Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP01249r004","sequence_construct":"DYKDDDDAGAPEGISIYTSDNYTEEMGSGDYDSMKEPCFREENANFNKIFLPTIYSIIFLTGIVGNGLVILVMGYQKKLRSMTDKYRLHLSVADLLFVITLPFWAVDAVANWYFGNFLCKAVHVIYTVNLYSSVWILAFISLDRYLAIVHATNSQRPRKLLAEKVVYVGVWIPALLLTIPDFIFANVSEADDRYICDRFYPNDLWVVVFQFQHIMVGLILPGIVILSCYCIIISKLSHNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYSGSGHQKRKALKPTVILILAFFACWLPYYIGISIDSFILLEIIKQGCEFENTVHKWISITEALAFFHCCLNPILYAFLGAKFKTSAQHALTSGRPLEVLFQ","statement":[{"text":"The lack of electron density in this region indicates disorder. ","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"3OE0"},{"db":"PDB","id":"3OE9"}]},{"start":1,"end":27,"reference_id":"20929726","reference_source":"pmid","reference_html":"Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists. <i> Wu B, Chien EY, Mol CD, Fenalti G, Liu W, Katritch V, Abagyan R, Brooun A, Wells P, Bi FC, Hamel DJ, Kuhn P, Handel TM, Cherezov V, Stevens RC. </i> Science, 2010","date":"2022-06-15T18:33:18.300Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"3OE9"}],"region_id":"DP01249r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting CXC chemokine receptor antagonist peptide with sequence RRACYQKPPYRRCRGP."}]}],"sequence_construct":"DYKDDDDAGAPEGISIYTSDNYTEEMGSGDYDSMKEPCFREENANFNKIFLPTIYSIIFLTGIVGNGLVILVMGYQKKLRSMTDKYRLHLSVADLLFVITLPFWAVDAVANWYFGNFLCKAVHVIYTVNLYSSVWILAFISLDRYLAIVHATNSQRPRKLLAEKVVYVGVWIPALLLTIPDFIFANVSEADDRYICDRFYPNDLWVVVFQFQHIMVGLILPGIVILSCYCIIISKLSHNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYSGSGHQKRKALKPTVILILAFFACWLPYYIGISIDSFILLEIIKQGCEFENTVHKWISITEALAFFHCCLNPILYAFLGAKFKTSAQHALTSGRPLEVLFQ","statement":[{"text":"The lack of electron density in this region indicates disorder. ","type":"Curator statement"}]},{"start":1,"end":34,"reference_id":"20929726","reference_source":"pmid","reference_html":"Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists. <i> Wu B, Chien EY, Mol CD, Fenalti G, Liu W, Katritch V, Abagyan R, Brooun A, Wells P, Bi FC, Hamel DJ, Kuhn P, Handel TM, Cherezov V, Stevens RC. </i> Science, 2010","date":"2022-06-15T18:39:23.225Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"3OE6"}],"region_id":"DP01249r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting CXC chemokine receptor antagonist peptide with sequence RRACYQKPPYRRCRGP."}]}],"sequence_construct":"DYKDDDDAGAPEGISIYTSDNYTEEMGSGDYDSMKEPCFREENANFNKIFLPTIYSIIFLTGIVGNGLVILVMGYQKKLRSMTDKYRLHLSVADLLFVITLPFWAVDAVANWYFGNFLCKAVHVIYTVNLYSSVWILAFISLDRYLAIVHATNSQRPRKLLAEKVVYVGVWIPALLLTIPDFIFANVSEADDRYICDRFYPNDLWVVVFQFQHIMVGLILPGIVILSCYCIIISKLSHNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYSGSGHQKRKALKPTVILILAFFACWLPYYIGISIDSFILLEIIKQGCEFENTVHKWISITEALAFFHCCLNPILYAFLGAKFKTSAQHALTSGRPLEVLFQ","statement":[{"text":"The lack of electron density in this region indicates disorder. ","type":"Curator statement"}]},{"start":313,"end":325,"reference_id":"20929726","reference_source":"pmid","reference_html":"Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists. <i> Wu B, Chien EY, Mol CD, Fenalti G, Liu W, Katritch V, Abagyan R, Brooun A, Wells P, Bi FC, Hamel DJ, Kuhn P, Handel TM, Cherezov V, Stevens RC. </i> Science, 2010","date":"2022-06-15T18:41:00.748Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"3OE6"}],"region_id":"DP01249r007","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting CXC chemokine receptor antagonist peptide with sequence RRACYQKPPYRRCRGP."}]}],"sequence_construct":"DYKDDDDAGAPEGISIYTSDNYTEEMGSGDYDSMKEPCFREENANFNKIFLPTIYSIIFLTGIVGNGLVILVMGYQKKLRSMTDKYRLHLSVADLLFVITLPFWAVDAVANWYFGNFLCKAVHVIYTVNLYSSVWILAFISLDRYLAIVHATNSQRPRKLLAEKVVYVGVWIPALLLTIPDFIFANVSEADDRYICDRFYPNDLWVVVFQFQHIMVGLILPGIVILSCYCIIISKLSHNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYSGSGHQKRKALKPTVILILAFFACWLPYYIGISIDSFILLEIIKQGCEFENTVHKWISITEALAFFHCCLNPILYAFLGAKFKTSAQHALTSGRPLEVLFQ","statement":[{"text":"The lack of electron density in this region indicates disorder. ","type":"Curator statement"}]}],"released":"2018_11","uniref100":"UniRef100_P61073","date":"2018-07-04T01:23:10.000Z","acc":"P61073","name":"C-X-C chemokine receptor type 4","length":352,"organism":"Homo sapiens","dataset":["Autophagy-related proteins","Cancer-related proteins"],"UniParc":"UPI000000106C","genes":[{"name":{"value":"CXCR4"}}],"alphafold_very_low_content":0.13068181818181818,"disorder_content":0.1590909090909091,"disprot_consensus":{"full":[{"start":1,"end":34,"type":"D"},{"start":304,"end":325,"type":"D"}],"Structural state":[{"start":1,"end":34,"type":"D"},{"start":304,"end":325,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00125","name":"Core histone H2A/H2B/H3/H4 domain","start":18,"end":98}],"gene3D":[{"start":1,"end":123,"id":"1.10.20.10","name":"Histone, subunit A"}]},"uniref50":"UniRef50_P02283","sequence":"MPPKTSGKAAKKAGKAQKNITKTDKKKKRKRKESYAIYIYKVLKQVHPDTGISSKAMSIMNSFVNDIFERIAAEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_P02283","disprot_id":"DP01250","ncbi_taxon_id":7227,"regions_counter":3,"creator":"zskalman","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":27,"region_id":"DP01250r001","released":"2025_06","ec_id":"ECO:0006220","reference_html":"Structure of the Drosophila nucleosome core particle highlights evolutionary constraints on the H2A-H2B histone dimer. <i> Clapier CR, Chakravarthy S, Petosa C, Fernández-Tornero C, Luger K, Müller CW. </i> Proteins, 2008","statement":[{"text":"Unstructured residues are indicated in lower case.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":2,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2025-02-03T19:45:34.817Z","reference_source":"pmid","term_name":"disorder","reference_id":"17957772","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"2PYO"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84051"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84040"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02299"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"DNA fragment derived from human α-satellite DNA with sequence 5'-ATCAATATCCACCTGCAGATACTACCAAAAGTGTATTTGGAAACTGCTCCATCAAAAGGCATGTTCAGCTGGAATCCAGCTGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTGGTAGTATCTGCAGGTGGATATTGAT"}]}]},{"start":2,"end":34,"reference_id":"34837025","reference_source":"pmid","reference_html":"Mapping the electrostatic potential of the nucleosome acidic patch. <i> Zhang H, Eerland J, Horn V, Schellevis R, van Ingen H. </i> Sci Rep, 2021","date":"2024-11-20T08:51:23.770Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7PJ1"}],"region_id":"DP01250r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84051 "}],"statement":[{"text":"Chemical shift indices obtained from the experimental Cα and Cβ chemical shifts confirm the presence of the histone fold core secondary structure elements with disordered tails for both histones, similar to the human dimer (Fig. 1a).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-03T19:12:38.001Z"}},{"start":2,"end":34,"reference_id":"34837025","reference_source":"pmid","reference_html":"Mapping the electrostatic potential of the nucleosome acidic patch. <i> Zhang H, Eerland J, Horn V, Schellevis R, van Ingen H. </i> Sci Rep, 2021","date":"2025-02-03T19:24:51.911Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7PJ1"}],"region_id":"DP01250r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84051"}],"statement":[{"text":"Chemical shift indices obtained from the experimental Cα and Cβ chemical shifts confirm the presence of the histone fold core secondary structure elements with disordered tails for both histones, similar to the human dimer (Fig. 1a).","type":"Results"}]}],"released":"2025_06","uniref100":"UniRef100_P02283","date":"2018-07-04T06:32:43.000Z","acc":"P02283","name":"Histone H2B","length":123,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI000012BFC6","genes":[{"name":{"value":"His2B"}},{"name":{"value":"His2B:CG17949"},"orfNames":[{"value":"CG17949"}]},{"name":{"value":"His2B:CG33868"},"orfNames":[{"value":"CG33868"}]},{"name":{"value":"His2B:CG33870"},"orfNames":[{"value":"CG33870"}]},{"name":{"value":"His2B:CG33872"},"orfNames":[{"value":"CG33872"}]},{"name":{"value":"His2B:CG33874"},"orfNames":[{"value":"CG33874"}]},{"name":{"value":"His2B:CG33876"},"orfNames":[{"value":"CG33876"}]},{"name":{"value":"His2B:CG33878"},"orfNames":[{"value":"CG33878"}]},{"name":{"value":"His2B:CG33880"},"orfNames":[{"value":"CG33880"}]},{"name":{"value":"His2B:CG33882"},"orfNames":[{"value":"CG33882"}]},{"name":{"value":"His2B:CG33884"},"orfNames":[{"value":"CG33884"}]},{"name":{"value":"His2B:CG33886"},"orfNames":[{"value":"CG33886"}]},{"name":{"value":"His2B:CG33888"},"orfNames":[{"value":"CG33888"}]},{"name":{"value":"His2B:CG33890"},"orfNames":[{"value":"CG33890"}]},{"name":{"value":"His2B:CG33892"},"orfNames":[{"value":"CG33892"}]},{"name":{"value":"His2B:CG33894"},"orfNames":[{"value":"CG33894"}]},{"name":{"value":"His2B:CG33896"},"orfNames":[{"value":"CG33896"}]},{"name":{"value":"His2B:CG33898"},"orfNames":[{"value":"CG33898"}]},{"name":{"value":"His2B:CG33900"},"orfNames":[{"value":"CG33900"}]},{"name":{"value":"His2B:CG33902"},"orfNames":[{"value":"CG33902"}]},{"name":{"value":"His2B:CG33904"},"orfNames":[{"value":"CG33904"}]},{"name":{"value":"His2B:CG33906"},"orfNames":[{"value":"CG33906"}]},{"name":{"value":"His2B:CG33908"},"orfNames":[{"value":"CG33908"}]},{"name":{"value":"His2B:CG33910"},"orfNames":[{"value":"CG33910"}]}],"alphafold_very_low_content":0.07317073170731707,"disorder_content":0.2682926829268293,"disprot_consensus":{"full":[{"start":2,"end":34,"type":"D"}],"Structural state":[{"start":2,"end":34,"type":"D"}],"Disorder function":[{"start":2,"end":34,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00019","name":"Transforming growth factor beta like domain","start":292,"end":389},{"id":"PF00688","name":"TGF-beta propeptide","start":31,"end":261}],"gene3D":[{"start":279,"end":390,"id":"2.10.90.10","name":"Cystine-knot cytokines"},{"start":28,"end":269,"id":"2.60.120.970","name":"2.60.120.970"}]},"uniref50":"UniRef50_P01137","sequence":"MPPSGLRLLPLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESAEPEPEPEADYYAKEVTRVLMVETHNEIYDKFKQSTHSIYMFFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLSRGGEIEGFRLSAHCSCDSRDNTLQVDINGFTTGRRGDLATIHGMNRPFLLLMATPLERAQHLQSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQALEPLPIVYYVGRKPKVEQLSNMIVRSCKCS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P01137","disprot_id":"DP01252","ncbi_taxon_id":9606,"regions_counter":3,"creator":"vsagris","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":261,"region_id":"DP01252r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Prodomain-growth factor swapping in the structure of pro-TGF-β1. <i> Zhao B, Xu S, Dong X, Lu C, Springer TA. </i> J Biol Chem, 2018","statement":[{"text":"In chains G and H, residues 241–258 and 241–249, respectively, are disordered, compared with residues 243–250 in chain A of pro-TGF-β1 alone (Fig. 3A). However, the positions of ordered residues 240 and 251–261 also differ markedly. Thus, residues 240–261 (22 residues) are capable of remodeling to extend away from pro-TGF-β1 and fit into the PC cleavage site.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"gminervini","start":240,"term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"29109152","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-25T07:52:14.685Z"}},{"start":257,"end":260,"reference_id":"30979895","reference_source":"pmid","reference_html":"Transcriptional regulation of autophagy-lysosomal function in BRAF-driven melanoma progression and chemoresistance. <i> Li S, Song Y, Quach C, Guo H, Jang GB, Maazi H, Zhao S, Sands NA, Liu Q, In GK, Peng D, Yuan W, Machida K, Yu M, Akbari O, Hagiya A, Yang Y, Punj V, Tang L, Liang C. </i> Nat Commun, 2019","date":"2022-06-24T20:24:24.390Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","region_id":"DP01252r002","statement":[{"text":"To determine whether the two xLIR of TGF-β mediate LC3 interaction, we generated the W17A/V20A, F257A/L260A, and W17A/V20A/F257A/L260A mutants of TGF-β (Supplementary Fig. 7g). TGF-β interaction with recombinant LC3 (His-LC3) was reduced by W17A/V20A or F257A/L260A, and further decreased by W17A/V20A/F257A/L260A (Supplementary Fig. 7g), suggesting that both xLIR motifs are required for efficient LC3 interaction. In vitro experiments using recombinant GST-pro-TGF-β and His-LC3 confirmed their direct interaction, which was disrupted by W17A/V20A/F257A/L260A (Supplementary Fig. 7h).","type":"Results"},{"text":"The annotated region includes the LIR motif (FLLL) at positions 257-260.","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-25T07:52:23.811Z"}},{"start":257,"end":260,"reference_id":"30979895","reference_source":"pmid","reference_html":"Transcriptional regulation of autophagy-lysosomal function in BRAF-driven melanoma progression and chemoresistance. <i> Li S, Song Y, Quach C, Guo H, Jang GB, Maazi H, Zhao S, Sands NA, Liu Q, In GK, Peng D, Yuan W, Machida K, Yu M, Akbari O, Hagiya A, Yang Y, Punj V, Tang L, Liang C. </i> Nat Commun, 2019","date":"2022-06-24T20:23:45.792Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","region_id":"DP01252r003","statement":[{"text":"To determine whether the two xLIR of TGF-β mediate LC3 interaction, we generated the W17A/V20A, F257A/L260A, and W17A/V20A/F257A/L260A mutants of TGF-β (Supplementary Fig. 7g). TGF-β interaction with recombinant LC3 (His-LC3) was reduced by W17A/V20A or F257A/L260A, and further decreased by W17A/V20A/F257A/L260A (Supplementary Fig. 7g), suggesting that both xLIR motifs are required for efficient LC3 interaction. In vitro experiments using recombinant GST-pro-TGF-β and His-LC3 confirmed their direct interaction, which was disrupted by W17A/V20A/F257A/L260A (Supplementary Fig. 7h).","type":"Results"},{"text":"The annotated region includes the LIR motif (FLLL) at positions 257-260.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-25T07:52:27.279Z"}}],"released":"2018_11","uniref100":"UniRef100_P01137","date":"2018-07-04T07:53:15.000Z","acc":"P01137","name":"Transforming growth factor beta-1 proprotein","length":390,"organism":"Homo sapiens","dataset":["Autophagy-related proteins","Extracellular matrix proteins"],"UniParc":"UPI000002C691","genes":[{"name":{"value":"TGFB1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11766","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11766"}}]},"synonyms":[{"value":"TGFB"}]}],"alphafold_very_low_content":0.08461538461538462,"disorder_content":0.05641025641025641,"disprot_consensus":{"full":[{"start":240,"end":261,"type":"D"}],"Structural state":[{"start":240,"end":261,"type":"D"}],"Biological process":[{"start":257,"end":260,"type":"F"}],"Molecular function":[{"start":257,"end":260,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00428","name":"60s Acidic ribosomal protein","start":23,"end":113}],"gene3D":[{"start":1,"end":64,"id":"1.10.10.1410","name":"1.10.10.1410"}]},"uniref50":"UniRef50_P05386","sequence":"MASVSELACIYSALILHDDEVTVTEDKINALIKAAGVNVEPFWPGLFAKALANVNIGSLICNVGAGGPAPAAGAAPAGGPAPSTAAAPAEEKKVEAKKEESEESDDDMGFGLFD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P05386","disprot_id":"DP01253","ncbi_taxon_id":9606,"regions_counter":2,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":114,"region_id":"DP01253r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of human P1•P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosome. <i> Lee KM, Yusa K, Chu LO, Yu CW, Oono M, Miyoshi T, Ito K, Shaw PC, Wong KB, Uchiumi T. </i> Nucleic Acids Res, 2013","statement":[{"text":"The structure of HsP1•HsP2 heterodimer can mainly be divided into two domains–a N-terminal dimerization domain (residue 1–62 of HsP1 and HsP2) and a flexible C-terminal tail, which is composed of the hinge and the highly conserved C-terminal regions (residue 63–114 of HsP1 and 63–115 of HsP2). As a result, the flexible tails of P1•P2 can extend up to ~125 Å away from the N-terminal dimerization domain (Figure 1A).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"gminervini","start":63,"term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"23892290","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":114,"term_name":"protein binding","start":63,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"we propose a model that recruitment of TCS to the sarcin-ricin loop required the flexible C-terminal tail, and the proline-alanine rich hinge region lengthens this C-terminal tail, allowing the tail to sweep around the ribosome to recruit TCS.","type":"Abstract"}],"curator_id":"gminervini","released":"2022_03","term_ontology":"GO","curator_name":"Giovanni Minervini","reference_id":"23892290","version":3,"reference_html":"Solution structure of human P1•P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosome. <i> Lee KM, Yusa K, Chu LO, Yu CW, Oono M, Miyoshi T, Ito K, Shaw PC, Wong KB, Uchiumi T. </i> Nucleic Acids Res, 2013","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","cross_refs":[{"db":"PMCID","id":"PMC3794596"}],"region_id":"DP01253r002","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P05386","date":"2018-07-04T08:01:30.000Z","acc":"P05386","name":"60S acidic ribosomal protein P1","length":114,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000134244","genes":[{"name":{"value":"RPLP1"},"synonyms":[{"value":"RRP1"}]}],"alphafold_very_low_content":0.30701754385964913,"disorder_content":0.45614035087719296,"disprot_consensus":{"full":[{"start":63,"end":114,"type":"D"}],"Structural state":[{"start":63,"end":114,"type":"D"}],"Molecular function":[{"start":63,"end":114,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02037","name":"SAP domain","start":573,"end":607},{"id":"PF02735","name":"Ku70/Ku80 beta-barrel domain","start":265,"end":459},{"id":"PF03730","name":"Ku70/Ku80 C-terminal arm","start":472,"end":556},{"id":"PF03731","name":"Ku70/Ku80 N-terminal alpha/beta domain","start":37,"end":255}],"gene3D":[{"start":35,"end":250,"id":"3.40.50.410","name":"von Willebrand factor, type A domain"},{"start":279,"end":341,"id":"4.10.970.10","name":"Ku70, bridge and pillars"},{"start":559,"end":609,"id":"1.10.720.30","name":"SAP domain"},{"start":254,"end":439,"id":"2.40.290.10","name":"2.40.290.10"},{"start":440,"end":533,"id":"1.10.1600.10","name":"1.10.1600.10"}]},"uniref50":"UniRef50_P12956","sequence":"MSGWESYYKTEGDEEAEEEQEENLEASGDYKYSGRDSLIFLVDASKAMFESQSEDELTPFDMSIQCIQSVYISKIISSDRDLLAVVFYGTEKDKNSVNFKNIYVLQELDNPGAKRILELDQFKGQQGQKRFQDMMGHGSDYSLSEVLWVCANLFSDVQFKMSHKRIMLFTNEDNPHGNDSAKASRARTKAGDLRDTGIFLDLMHLKKPGGFDISLFYRDIISIAEDEDLRVHFEESSKLEDLLRKVRAKETRKRALSRLKLKLNKDIVISVGIYNLVQKALKPPPIKLYRETNEPVKTKTRTFNTSTGGLLLPSDTKRSQIYGSRQIILEKEETEELKRFDDPGLMLMGFKPLVLLKKHHYLRPSLFVYPEESLVIGSSTLFSALLIKCLEKEVAALCRYTPRRNIPPYFVALVPQEEELDDQKIQVTPPGFQLVFLPFADDKRKMPFTEKIMATPEQVGKMKAIVEKLRFTYRSDSFENPVLQQHFRNLEALALDLMEPEQAVDLTLPKVEAMNKRLGSLVDEFKELVYPPDYNPEGKVTKRKHDNEGSGSKRPKVEYSEEELKTHISKGTLGKFTVPMLKEACRAYGLKSGLKKQELLEALTKHFQD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P12956","disprot_id":"DP01254","ncbi_taxon_id":9606,"regions_counter":1,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":609,"region_id":"DP01254r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair. <i> Walker JR, Corpina RA, Goldberg J. </i> Nature, 2001","statement":[{"text":"The final model is complete with the exception of the disordered Ku70 residues 1–33, 223–230, 533–609 (including the SAP domain), and Ku80 residues 1–5, 171–180, 546–565, plus the disordered final 3 bp of the G-rich stem that occupy a solvent space in the crystal","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"gminervini","start":533,"term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"11493912","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P12956","date":"2018-07-04T08:26:32.000Z","acc":"P12956","name":"X-ray repair cross-complementing protein 6","length":609,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012E125","genes":[{"name":{"value":"XRCC6"},"synonyms":[{"value":"G22P1"}]}],"alphafold_very_low_content":0.08538587848932677,"disorder_content":0.12643678160919541,"disprot_consensus":{"full":[{"start":533,"end":609,"type":"D"}],"Structural state":[{"start":533,"end":609,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02735","name":"Ku70/Ku80 beta-barrel domain","start":253,"end":453},{"id":"PF03730","name":"Ku70/Ku80 C-terminal arm","start":477,"end":568},{"id":"PF03731","name":"Ku70/Ku80 N-terminal alpha/beta domain","start":9,"end":243},{"id":"PF08785","name":"Ku C terminal domain like","start":593,"end":705}],"gene3D":[{"start":561,"end":710,"id":"1.25.40.240","name":"Ku, C-terminal domain"},{"start":243,"end":443,"id":"2.40.290.10","name":"2.40.290.10"},{"start":1,"end":242,"id":"3.40.50.410","name":"von Willebrand factor, type A domain"},{"start":444,"end":545,"id":"1.10.1600.10","name":"1.10.1600.10"}]},"uniref50":"UniRef50_P13010","sequence":"MVRSGNKAAVVLCMDVGFTMSNSIPGIESPFEQAKKVITMFVQRQVFAENKDEIALVLFGTDGTDNPLSGGDQYQNITVHRHLMLPDFDLLEDIESKIQPGSQQADFLDALIVSMDVIQHETIGKKFEKRHIEIFTDLSSRFSKSQLDIIIHSLKKCDISLQFFLPFSLGKEDGSGDRGDGPFRLGGHGPSFPLKGITEQQKEGLEIVKMVMISLEGEDGLDEIYSFSESLRKLCVFKKIERHSIHWPCRLTIGSNLSIRIAAYKSILQERVKKTWTVVDAKTLKKEDIQKETVYCLNDDDETEVLKEDIIQGFRYGSDIVPFSKVDEEQMKYKSEGKCFSVLGFCKSSQVQRRFFMGNQVLKVFAARDDEAAAVALSSLIHALDDLDMVAIVRYAYDKRANPQVGVAFPHIKHNYECLVYVQLPFMEDLRQYMFSSLKNSKKYAPTEAQLNAVDALIDSMSLAKKDEKTDTLEDLFPTTKIPNPRFQRLFQCLLHRALHPREPLPPIQQHIWNMLNPPAEVTTKSQIPLSKIKTLFPLIEAKKKDQVTAQEIFQDNHEDGPTAKKLKTEQGGAHFSVSSLAEGSVTSVGSVNPAENFRVLVKQKKASFEEASNQLINHIEQFLDTNETPYFMKSIDCIRAFREEAIKFSEEQRFNNFLKALQEKVEIKQLNHFWEIVVQDGITLITKEEASGSSVTAEEAKKFLAPKDKPSGDTAAVFEEGGDVDDLLDMI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P13010","disprot_id":"DP01255","ncbi_taxon_id":9606,"regions_counter":1,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":565,"region_id":"DP01255r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair. <i> Walker JR, Corpina RA, Goldberg J. </i> Nature, 2001","statement":[{"text":"The final model is complete with the exception of the disordered Ku70 residues 1–33, 223–230, 533–609 (including the SAP domain), and Ku80 residues 1–5, 171–180, 546–565, plus the disordered final 3 bp of the G-rich stem that occupy a solvent space in the crystal","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"gminervini","start":546,"term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"11493912","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P13010","date":"2018-07-04T08:32:39.000Z","acc":"P13010","name":"X-ray repair cross-complementing protein 5","length":732,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012E126","genes":[{"name":{"value":"XRCC5"},"synonyms":[{"value":"G22P2"}]}],"alphafold_very_low_content":0.10109289617486339,"disorder_content":0.0273224043715847,"disprot_consensus":{"full":[{"start":546,"end":565,"type":"D"}],"Structural state":[{"start":546,"end":565,"type":"D"}]}},{"acc":"Q32ZE1","sequence":"MKNPKEEIRRIRIVNMLKRGVARVNPLGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEIIKKFKKDLAAMLRIINARKERKRRGADTSIGIIGLLLTTAMAAEITRRGSAYYMYLDRSDAGKAISFATTLGVNKCHVQIMDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREYTKHLIKVENWIFRNPGFALVAVAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGCVTVMAQDKPTVDIELVTTTVSNMAEVRSYCYEASISDMASDSRCPTQGEAYLDKQSDTQYVCKRTLVDRGWGNGCGLFGKGSLVTCAKFTCSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIGYETDEDRAKVEVTPNSPRAEATLGGFGSLGLDCEPRTGLDFSDLYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKEALVEFKDAHAKRQTVVVLGSQEGAVHTALAGALEAEMDGAKGRLFSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKVPAETLHGTVTVEVQYAGTDGPCKIPVQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGDKKITHHWHRSGSTIGKAFEATVRGAKRMAVLGDTAWDFGSVGGVFNSLGKGIHQIFGAAFKSLFGGMSWFSQILIGTLLVWLGLNTKNGSISLTCLALGGVMIFLSTAVSADVGCSVDFSKKETRCGTGVFIYNDVEAWRDRYKYHPDSPRRLAAAVKQAWEEGICGISSVSRMENIMWKSVEGELNAILEENGVQLTVVVGSVKNPMWRGPQRLPVPVNELPHGWKAWGKSYFVRAAKTNNSFVVDGDTLKECPLEHRAWNSFLVEDHGFGVFHTSVWLKVREDYSLECDPAVIGTAVKGREAAHSDLGYWIESEKNDTWRLKRAHLIEMKTCEWPKSHTLWTDGVEESDLIIPKSLAGPLSHHNTREGYRTQVKGPWHSEELEIRFEECPGTKVYVEETCGTRGPSLRSTTASGRVIEEWCCRECTMPPLSFRAKDGCWYGMEIRPRKEPESNLVRSMVTAGSTDHMDHFSLGVLVILLMVQEGLKKRMTTKIIMSTSMAVLVVMILGGFSMSDLAKLVILMGATFAEMNTGGDVAHLALVAAFKVRPALLVSFIFRANWTPRESMLLALASCLLQTAISALEGDLMVLINGFALAWLAIRAMAVPRTDNIALPILAALTPLARGTLLVAWRAGLATCGGIMLLSLKGKGSVKKNLPFVMALGLTAVRVVDPINVVGLLLLTRSGKRSWPPSEVLTAVGLICALAGGFAKADIEMAGPMAAVGLLIVSYVVSGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEEDGPPMREIILKVVLMAICGMNPIAIPFAAGAWYVYVKTGKRSGALWDVPAPKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGAALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWDGLSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGKREEETPVECFEPSMLKKKQLTVLDLHPGAGKTRRVLPEIVREAIKKRLRTVILAPTRVVAAEMEEALRGLPVRYMTTAVNVTHSGTEIVDLMCHATFTSRLLQPIRVPNYNLNIMDEAHFTDPSSIAARGYISTRVEMGEAAAIFMTATPPGTRDAFPDSNSPIMDTEVEVPERAWSSGFDWVTDHSGKTVWFVPSVRNGNEIAACLTKAGKRVIQLSRKTFETEFQKTKNQEWDFVITTDISEMGANFKADRVIDSRRCLKPVILDGERVILAGPMPVTHASAAQRRGRIGRNPNKPGDEYMYGGGCAETDEGHAHWLEARMLLDNIYLQDGLIASLYRPEADKVAAIEGEFKLRTEQRKTFVELMKRGDLPVWLAYQVASAGITYTDRRWCFDGTTNNTIMEDSVPAEVWTKYGEKRVLKPRWMDARVCSDHAALKSFKEFAAGKRGAALGVMEALGTLPGHMTERFQEAIDNLAVLMRAETGSRPYKAAAAQLPETLETIMLLGLLGTVSLGIFFVLMRNKGIGKMGFGMVTLGASAWLMWLSEIEPARIACVLIVVFLLLVVLIPEPEKQRSPQDNQMAIIIMVAVGLLGLITANELGWLERTKNDIAHLMGRREEGATMGFSMDIDLRPASAWAIYAALTTLITPAVQHAVTTSYNNYSLMAMATQAGVLFGMGKGMPFMHGDLGVPLLMMGCYSQLTPLTLIVAIILLVAHYMYLIPGLQAAAARAAQKRTAAGIMKNPVVDGIVVTDIDTMTIDPQVEKKMGQVLLIAVAISSAVLLRTAWGWGEAGALITAATSTLWEGSPNKYWNSSTATSLCNIFRGSYLAGASLIYTVTRNAGLVKRRGGGTGETLGEKWKARLNQMSALEFYSYKKSGITEVCREEARRALKDGVATGGHAVSRGSAKIRWLEERGYLQPYGKVVDLGCGRGGWSYYAATIRKVQEVRGYTKGGPGHEEPMLVQSYGWNIVRLKSGVDVFHMAAEPCDTLLCDIGESSSSPEVEETRTLRVLSMVGDWLEKRPGAFCIKVLCPYTSTMMETMERLQRRHGGGLVRVPLCRNSTHEMYWVSGAKSNIIKSVSTTSQLLLGRMDGPRRPVKYEEDVNLGSGTRAVASCAEAPNMKIIGRRIERIRNEHAETWFLDENHPYRTWAYHGSYEAPTQGSASSLVNGVVRLLSKPWDVVTGVTGIAMTDTTPYGQQRVFKEKVDTRVPDPQEGTRQVMNIVSSWLWKELGKRKRPRVCTKEEFINKVRSNAALGAIFEEEKEWKTAVEAVNDPRFWALVDREREHHLRGECHSCVYNMMGKREKKQGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMGRENSGGGVEGLGLQRLGYILEEMNRAPGGKMYADDTAGWDTRISKFDLENEALITNQMEEGHRTLALAVIKYTYQNKVVKVLRPAEGGKTVMDIISRQDQRGSGQVVTYALNTFTNLVVQLIRNMEAEEVLEMQDLWLLRKPEKVTRWLQSNGWDRLKRMAVSGDDCVVKPIDDRFAHALRFLNDMGKVRKDTQEWKPSTGWSNWEEVPFCSHHFNKLYLKDGRSIVVPCRHQDELIGRARVSPGAGWSIRETACLAKSYAQMWQLLYFHRRDLRLMANAICSAVPVDWVPTGRTTWSIHGKGEWMTTEDMLMVWNRVWIEENDHMEDKTPVTKWTDIPYLGKREDLWCGSLIGHRPRTTWAENIKDTVNMVRRIIGDEEKYMDYLSTQVRYLGEEGSTPGVL","creator":"lchemes","dataset":["Viral proteins","Neglected tropical diseases proteins","RNA-binding proteins"],"date":"2018-07-04T08:46:04.000Z","disprot_id":"DP01256","features":{"pfam":[{"id":"PF00869","name":"Flavivirus glycoprotein, central and dimerisation domains","start":292,"end":588},{"id":"PF00948","name":"Flavivirus non-structural Protein NS1","start":793,"end":1144},{"id":"PF00949","name":"Peptidase S7, Flavivirus NS3 serine protease","start":1515,"end":1665},{"id":"PF00972","name":"Flavivirus RNA-directed RNA polymerase, fingers and palm domains","start":2768,"end":3218},{"id":"PF01002","name":"Flavivirus non-structural protein NS2B","start":1374,"end":1498},{"id":"PF01003","name":"Flavivirus capsid protein C","start":11,"end":122},{"id":"PF01004","name":"Flavivirus envelope glycoprotein M","start":217,"end":290},{"id":"PF01005","name":"Flavivirus non-structural protein NS2A","start":1154,"end":1258},{"id":"PF01349","name":"Flavivirus non-structural protein NS4B","start":2266,"end":2506},{"id":"PF01350","name":"Flavivirus non-structural protein NS4A","start":2122,"end":2264},{"id":"PF01570","name":"Flavivirus polyprotein propeptide","start":130,"end":214},{"id":"PF01728","name":"FtsJ-like methyltransferase","start":2571,"end":2740},{"id":"PF02832","name":"Flavivirus glycoprotein, immunoglobulin-like domain","start":590,"end":688},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1683,"end":1829},{"id":"PF20483","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","start":3222,"end":3385},{"id":"PF20907","name":"Flavivirus NS3 helicase, C-terminal helical domain","start":1970,"end":2113},{"id":"PF21659","name":"Flavivirus envelope glycoprotein E, stem/anchor domain","start":691,"end":785}],"gene3D":[{"start":352,"end":545,"id":"3.30.387.10","name":"Viral Envelope Glycoprotein, domain 3","_id":"685af523b4ac24d5329d8ec5"},{"start":342,"end":564,"id":"3.30.67.10","name":"Viral Envelope Glycoprotein, domain 2","_id":"685af523b4ac24d5329d8ec6"},{"start":23,"end":98,"id":"1.10.10.930","name":"1.10.10.930","_id":"685af523b4ac24d5329d8ec7"},{"start":123,"end":204,"id":"2.60.260.50","name":"Flavivirus polyprotein propeptide domain","_id":"685af523b4ac24d5329d8ec8"},{"start":587,"end":695,"id":"2.60.40.350","name":"2.60.40.350","_id":"685af523b4ac24d5329d8ec9"},{"start":292,"end":586,"id":"2.60.98.10","name":"Tick-borne Encephalitis virus Glycoprotein, domain 1","_id":"685af523b4ac24d5329d8eca"},{"start":696,"end":790,"id":"1.20.1280.260","name":"1.20.1280.260","_id":"685af523b4ac24d5329d8ecb"},{"start":216,"end":290,"id":"1.10.8.970","name":"Flavivirus envelope glycoprotein M-like","_id":"685af523b4ac24d5329d8ecc"},{"start":1821,"end":1978,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d8ecd"},{"start":1412,"end":1464,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d8ece"},{"start":2853,"end":2898,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d8ecf"},{"start":1682,"end":2012,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d8ed0"},{"start":1492,"end":1583,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d8ed1"},{"start":3047,"end":3114,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d8ed2"},{"start":2788,"end":2852,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d8ed3"},{"start":1584,"end":1675,"id":"2.40.10.10","name":"Trypsin-like serine proteases","_id":"685af523b4ac24d5329d8ed4"},{"start":2516,"end":2787,"id":"3.40.50.150","name":"Vaccinia Virus protein VP39","_id":"685af523b4ac24d5329d8ed5"},{"start":2911,"end":3006,"id":"1.10.260.90","name":"1.10.260.90","_id":"685af523b4ac24d5329d8ed6"}]},"genes":[],"length":3419,"name":"Genome polyprotein","ncbi_taxon_id":64320,"organism":"Zika virus","regions_counter":22,"released":"2018_11","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Flavivirus"],"UniParc":"UPI00005D6997","uniref100":"UniRef100_Q32ZE1","uniref50":"UniRef50_P06935","uniref90":"UniRef90_Q32ZE1","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5GJ4","_id":"685af523b4ac24d5329d8ee1"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006198","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":1450,"end":1470,"interaction_partner":[],"reference_html":"Structure of the NS2B-NS3 protease from Zika virus after self-cleavage. <i> Phoo WW, Li Y, Zhang Z, Lee MY, Loh YR, Tan YB, Ng EY, Lescar J, Kang C, Luo D. </i> Nat Commun, 2016","reference_id":"27845325","region_id":"DP01256r003","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The C-terminal cytosolic region of NS2B is flexible and disordered as shown by the low NOE values (Figure 2A) of NMR experiments, which corresponds to residues 76-96 of NS2B. Only residues 45-76 are well ordered.","_id":"685af523b4ac24d5329d8edf"},{"type":"Results","text":"Conversely, residues S48 to D75 of NS2B appear stable in solution, as demonstrated by hetNOE values larger than 0.6 (Fig. 2a).","_id":"685af523b4ac24d5329d8ee0"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T10:40:22.221Z","_id":"685af523b4ac24d5329d8ee2"},"version":3,"_id":"685af523b4ac24d5329d8ede","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5GJ4","_id":"685af523b4ac24d5329d8eed"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":1499,"end":1516,"interaction_partner":[],"reference_html":"Structure of the NS2B-NS3 protease from Zika virus after self-cleavage. <i> Phoo WW, Li Y, Zhang Z, Lee MY, Loh YR, Tan YB, Ng EY, Lescar J, Kang C, Luo D. </i> Nat Commun, 2016","reference_id":"27845325","region_id":"DP01256r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"No electron density is visible for the first 18 amino acids of NS3 protease, indicating that after cleavage the N-terminal region of NS3 protease falls off from its own S′ pocket. Overall, the structure of eZiPro captures the post cleavage state of NS2B-NS3 protease.","_id":"685af523b4ac24d5329d8eee"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T10:40:14.595Z","_id":"685af523b4ac24d5329d8eef"},"version":1,"_id":"685af523b4ac24d5329d8eec","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5GJ4","_id":"685af523b4ac24d5329d8ef1"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1499,"end":1515,"interaction_partner":[],"reference_html":"Structure of the NS2B-NS3 protease from Zika virus after self-cleavage. <i> Phoo WW, Li Y, Zhang Z, Lee MY, Loh YR, Tan YB, Ng EY, Lescar J, Kang C, Luo D. </i> Nat Commun, 2016","reference_id":"27845325","region_id":"DP01256r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"We then collected the 15N T1, T2, hetNOE parameters and found that residues including S1-E17 and R170 to E177 of the N- and C-termini of NS3pro are highly dynamic in solution, characterized by low T1 and hetNOE values (<0.6) (Fig. 2a).","_id":"685af523b4ac24d5329d8ef2"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-29T13:49:46.866Z","_id":"685af523b4ac24d5329d8ef3"},"version":1,"_id":"685af523b4ac24d5329d8ef0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5GJ4","_id":"685af523b4ac24d5329d8ef5"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1444,"end":1455,"interaction_partner":[],"reference_html":"Structure of the NS2B-NS3 protease from Zika virus after self-cleavage. <i> Phoo WW, Li Y, Zhang Z, Lee MY, Loh YR, Tan YB, Ng EY, Lescar J, Kang C, Luo D. </i> Nat Commun, 2016","reference_id":"27845325","region_id":"DP01256r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Residues V76-V87 of NS2B which form a β-hairpin in the crystal structure, are relatively flexible in solution and exhibit relatively broaden peaks, suggesting a dynamic sampling process of the NS2B cofactor binding to NS3 and forming the P2 pocket (Fig. 1b; Supplementary Fig. 6).","_id":"685af523b4ac24d5329d8ef6"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-29T13:49:37.455Z","_id":"685af523b4ac24d5329d8ef7"},"version":1,"_id":"685af523b4ac24d5329d8ef4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5GJ4","_id":"685af523b4ac24d5329d8ef9"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1444,"end":1455,"interaction_partner":[],"reference_html":"Structure of the NS2B-NS3 protease from Zika virus after self-cleavage. <i> Phoo WW, Li Y, Zhang Z, Lee MY, Loh YR, Tan YB, Ng EY, Lescar J, Kang C, Luo D. </i> Nat Commun, 2016","reference_id":"27845325","region_id":"DP01256r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Residues V76-V87 of NS2B which form a β-hairpin in the crystal structure, are relatively flexible in solution and exhibit relatively broaden peaks, suggesting a dynamic sampling process of the NS2B cofactor binding to NS3 and forming the P2 pocket (Fig. 1b; Supplementary Fig. 6).","_id":"685af523b4ac24d5329d8efa"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T10:41:14.502Z","_id":"685af523b4ac24d5329d8efb"},"version":1,"_id":"685af523b4ac24d5329d8ef8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5GJ4","_id":"685af523b4ac24d5329d8efd"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1444,"end":1455,"interaction_partner":[],"reference_html":"Structure of the NS2B-NS3 protease from Zika virus after self-cleavage. <i> Phoo WW, Li Y, Zhang Z, Lee MY, Loh YR, Tan YB, Ng EY, Lescar J, Kang C, Luo D. </i> Nat Commun, 2016","reference_id":"27845325","region_id":"DP01256r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Residues V76-V87 of NS2B which form a β-hairpin in the crystal structure, are relatively flexible in solution and exhibit relatively broaden peaks, suggesting a dynamic sampling process of the NS2B cofactor binding to NS3 and forming the P2 pocket (Fig. 1b; Supplementary Fig. 6).","_id":"685af523b4ac24d5329d8efe"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-15T17:11:49.853Z","_id":"685af523b4ac24d5329d8eff"},"version":1,"_id":"685af523b4ac24d5329d8efc","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5GJ4","_id":"685af523b4ac24d5329d8f01"},{"db":"DisProt","id":"DP03524","_id":"685af523b4ac24d5329d8f02"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1499,"end":1512,"interaction_partner":[],"reference_html":"Crystal structure of Zika virus NS2B-NS3 protease in complex with a boronate inhibitor. <i> Lei J, Hansen G, Nitsche C, Klein CD, Zhang L, Hilgenfeld R. </i> Science, 2016","reference_id":"27386922","region_id":"DP01256r012","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The PDB corresponds to the Uniprot A0A140DLX4 and shows disorder in the region 1503-1516. IDR is 100% identical to this Uniprot and comprises the residues 1499-1512.","_id":"685af523b4ac24d5329d8f03"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-29T13:49:24.003Z","_id":"685af523b4ac24d5329d8f04"},"version":1,"_id":"685af523b4ac24d5329d8f00","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5U04","_id":"685af523b4ac24d5329d8f06"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-15T16:17:28.591Z","disprot_namespace":"Structural state","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":2822,"end":2836,"interaction_partner":[],"reference_html":"Crystal structure of Zika virus NS5 RNA-dependent RNA polymerase. <i> Godoy AS, Lima GM, Oliveira KI, Torres NU, Maluf FV, Guido RV, Oliva G. </i> Nat Commun, 2017","reference_id":"28345596","region_id":"DP01256r013","released":"2022_12","sample":[{"db":"ChEBI","deviation":null,"entry_name":"zinc(2+)","id":"29105","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d8f07"},{"db":"ChEBI","deviation":null,"entry_name":"phosphate(3-)","id":"18367","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d8f08"}],"statement":[{"type":"Results","text":"The first 15 N-terminal and last 16 C-terminal residues are not visible in the electron density. Due to disorder, parts of loops 1 (residues 340–363), 3 (residues 408–417), 4 (residues 454–471), 5 (residues 533–542) and 6 (residues 576–606) are also missing in the model.","_id":"685af523b4ac24d5329d8f09"},{"type":"Curator statement","text":"The 15 N-terminal region of the Zika virus RNA-dependent RNA polymerase corresponds to the 2822-2836 region of the polyprotein.","_id":"685af523b4ac24d5329d8f0a"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-15T17:11:18.124Z","_id":"685af523b4ac24d5329d8f0b"},"version":0,"_id":"685af523b4ac24d5329d8f05","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5U04","_id":"685af523b4ac24d5329d8f0d"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-15T16:33:16.019Z","disprot_namespace":"Structural state","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":2857,"end":2879,"interaction_partner":[],"reference_html":"Crystal structure of Zika virus NS5 RNA-dependent RNA polymerase. <i> Godoy AS, Lima GM, Oliveira KI, Torres NU, Maluf FV, Guido RV, Oliva G. </i> Nat Commun, 2017","reference_id":"28345596","region_id":"DP01256r014","released":"2022_12","sample":[{"db":"ChEBI","deviation":null,"entry_name":"zinc(2+)","id":"29105","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d8f0e"},{"db":"ChEBI","deviation":null,"entry_name":"phosphate(3-)","id":"18367","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d8f0f"}],"statement":[{"type":"Results","text":"The first 15 N-terminal and last 16 C-terminal residues are not visible in the electron density. Due to disorder, parts of loops 1 (residues 340–363), 3 (residues 408–417), 4 (residues 454–471), 5 (residues 533–542) and 6 (residues 576–606) are also missing in the model.","_id":"685af523b4ac24d5329d8f10"},{"type":"Curator statement","text":"The 340-363 region of the Zika virus RNA-dependent RNA polymerase corresponds to the 2857-2879 region of the polyprotein.","_id":"685af523b4ac24d5329d8f11"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-15T17:11:20.527Z","_id":"685af523b4ac24d5329d8f12"},"version":0,"_id":"685af523b4ac24d5329d8f0c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5U04","_id":"685af523b4ac24d5329d8f14"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-15T16:35:08.148Z","disprot_namespace":"Structural state","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":2971,"end":2986,"interaction_partner":[],"reference_html":"Crystal structure of Zika virus NS5 RNA-dependent RNA polymerase. <i> Godoy AS, Lima GM, Oliveira KI, Torres NU, Maluf FV, Guido RV, Oliva G. </i> Nat Commun, 2017","reference_id":"28345596","region_id":"DP01256r015","released":"2022_12","sample":[{"db":"ChEBI","deviation":null,"entry_name":"zinc(2+)","id":"29105","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d8f15"},{"db":"ChEBI","deviation":null,"entry_name":"phosphate(3-)","id":"18367","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d8f16"}],"statement":[{"type":"Results","text":"The first 15 N-terminal and last 16 C-terminal residues are not visible in the electron density. Due to disorder, parts of loops 1 (residues 340–363), 3 (residues 408–417), 4 (residues 454–471), 5 (residues 533–542) and 6 (residues 576–606) are also missing in the model.","_id":"685af523b4ac24d5329d8f17"},{"type":"Curator statement","text":"The 454-471 region of the Zika virus RNA-dependent RNA polymerase corresponds to the 2971-2986 region of the polyprotein.","_id":"685af523b4ac24d5329d8f18"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-15T17:11:23.096Z","_id":"685af523b4ac24d5329d8f19"},"version":0,"_id":"685af523b4ac24d5329d8f13","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5U04","_id":"685af523b4ac24d5329d8f1b"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-15T16:37:23.741Z","disprot_namespace":"Structural state","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":3093,"end":3121,"interaction_partner":[],"reference_html":"Crystal structure of Zika virus NS5 RNA-dependent RNA polymerase. <i> Godoy AS, Lima GM, Oliveira KI, Torres NU, Maluf FV, Guido RV, Oliva G. </i> Nat Commun, 2017","reference_id":"28345596","region_id":"DP01256r016","released":"2022_12","sample":[{"db":"ChEBI","deviation":null,"entry_name":"zinc(2+)","id":"29105","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d8f1c"},{"db":"ChEBI","deviation":null,"entry_name":"phosphate(3-)","id":"18367","statements":[],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d8f1d"}],"statement":[{"type":"Results","text":"The first 15 N-terminal and last 16 C-terminal residues are not visible in the electron density. Due to disorder, parts of loops 1 (residues 340–363), 3 (residues 408–417), 4 (residues 454–471), 5 (residues 533–542) and 6 (residues 576–606) are also missing in the model.","_id":"685af523b4ac24d5329d8f1e"},{"type":"Curator statement","text":"The C-terminal region of the Zika virus RNA-dependent RNA polymerase corresponds to the 3404-3419 region of the polyprotein.","_id":"685af523b4ac24d5329d8f1f"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-15T17:11:26.007Z","_id":"685af523b4ac24d5329d8f20"},"version":0,"_id":"685af523b4ac24d5329d8f1a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-20T13:47:20.788Z","disprot_namespace":"Structural state","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":2116,"end":2163,"interaction_partner":[],"reference_html":"Use of massively multiple merged data for low-resolution S-SAD phasing and refinement of flavivirus NS1. <i> Akey DL, Brown WC, Konwerski JR, Ogata CM, Smith JL. </i> Acta Crystallogr D Biol Crystallogr, 2014","reference_id":"25286855","region_id":"DP01256r017","released":"2022_12","sample":[],"statement":[{"type":"Results","text":"The CD spectrum of NS4A (1–48) is showing a minimum (negative peak) at 199 nm (Fig. 2), and the ellipticity value beyond 199 nm showing no signature peak that suggests missing helices and beta-strands. Shape of the spectrum and signature minima indicating the Far-UV CD spectrum of typically disordered (unstructured or natively unfolded) protein.","_id":"685af523b4ac24d5329d8f22"},{"type":"Curator statement","text":"The 1-48 region of the NS4A protein corresponds to the 2116-2163 region of the Zika virus polyprotein.","_id":"685af523b4ac24d5329d8f23"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-15T17:11:37.665Z","_id":"685af523b4ac24d5329d8f24"},"version":0,"_id":"685af523b4ac24d5329d8f21","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-20T13:57:15.073Z","disprot_namespace":"Structural transition","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":2116,"end":2163,"interaction_partner":[],"reference_html":"Use of massively multiple merged data for low-resolution S-SAD phasing and refinement of flavivirus NS1. <i> Akey DL, Brown WC, Konwerski JR, Ogata CM, Smith JL. </i> Acta Crystallogr D Biol Crystallogr, 2014","reference_id":"25286855","region_id":"DP01256r018","released":"2022_12","sample":[{"db":"ChEBI","deviation":null,"entry_name":"1,2-dioleoyl-sn-glycero-3-phosphocholine(1+)","id":"52360","statements":[],"term_id":"IDPO:00488","term_name":"interacting lipid","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d8f26"},{"db":"ChEBI","deviation":null,"entry_name":"1,2-dioleoyl-sn-glycero-3-phospho-L-serine","id":"60568","statements":[],"term_id":"IDPO:00488","term_name":"interacting lipid","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d8f27"},{"db":"ChEBI","deviation":null,"entry_name":"sodium dodecyl sulfate","id":"8984","statements":[],"term_id":"IDPO:00488","term_name":"interacting lipid","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d8f28"}],"statement":[{"type":"Results","text":"The CD spectrum of NS4A (1–48) peptide is of disordered type as observed in the previous section, but when this peptide is mixed with lipid vesicles (DOPC or DOPS), it displays spectra of a helix (Fig. 5A and B).","_id":"685af523b4ac24d5329d8f29"},{"type":"Curator statement","text":"While increasing SDS concentration up to 0.5 mM and beyond, a spectral shift was observed at 199 nm and 222 nm, indicating a transition from disordered to α-helix (Fig. 5D).","_id":"685af523b4ac24d5329d8f2a"},{"type":"Curator statement","text":"The 1-48 region of the NS4A protein corresponds to the 2116-2163 region of the Zika virus polyprotein.","_id":"685af523b4ac24d5329d8f2b"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-15T17:11:55.930Z","_id":"685af523b4ac24d5329d8f2c"},"version":0,"_id":"685af523b4ac24d5329d8f25","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-20T13:56:21.370Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":2116,"end":2163,"interaction_partner":[{"db":"ChEBI","id":"52360","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8f2e"},{"db":"ChEBI","id":"60568","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8f2f"},{"db":"ChEBI","id":"8984","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8f30"}],"reference_html":"Use of massively multiple merged data for low-resolution S-SAD phasing and refinement of flavivirus NS1. <i> Akey DL, Brown WC, Konwerski JR, Ogata CM, Smith JL. </i> Acta Crystallogr D Biol Crystallogr, 2014","reference_id":"25286855","region_id":"DP01256r019","released":"2022_12","sample":[],"statement":[{"type":"Results","text":"The CD spectrum of NS4A (1–48) peptide is of disordered type as observed in the previous section, but when this peptide is mixed with lipid vesicles (DOPC or DOPS), it displays spectra of a helix (Fig. 5A and B).","_id":"685af523b4ac24d5329d8f31"},{"type":"Results","text":"The SDS micelles further probed the structural transition in NS4A (1–48). SDS is an anionic detergent that, upon interaction, causes a conformational change in many proteins (Blinkhorn and Jones, 1973; Moriyama et al., 2008; Singh et al., 2008).","_id":"685af523b4ac24d5329d8f32"},{"type":"Curator statement","text":"The 1-48 region of the NS4A protein corresponds to the 2116-2163 region of the Zika virus polyprotein.","_id":"685af523b4ac24d5329d8f33"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_id":"GO:0008289","term_is_obsolete":false,"term_name":"lipid binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-15T17:12:02.051Z","_id":"685af523b4ac24d5329d8f34"},"version":0,"_id":"685af523b4ac24d5329d8f2d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-21T19:54:58.001Z","disprot_namespace":"Structural state","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1441,"end":1468,"interaction_partner":[],"reference_html":"Solution conformations of Zika NS2B-NS3pro and its inhibition by natural products from edible plants. <i> Roy A, Lim L, Srivastava S, Lu Y, Song J. </i> PLoS One, 2017","reference_id":"28700665","region_id":"DP01256r020","released":"2022_12","sample":[{"db":"UniProt","deviation":null,"id":"Q32ZE1","statements":[{"type":"Curator statement","text":"The NS3pro protein corresponds to the 1476-2093 residues of the Zika virus genome polyprotein.","_id":"685af523b4ac24d5329d8f37"}],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d8f36"}],"statement":[{"type":"Results","text":"While 15N-labeled ZIKV NS2B in complex with unlabeled ZIKV NS3pro had a narrowly-dispersed HSQC spectrum with only ~29 peaks detectable (S2B Fig), Dengue NS2B in complex with Dengue NS3pro domain has a well-dispersed HSQC spectrum (S2C Fig) [21,30,31] which unambiguously indicates Dengue NS2B has a tight tertiary packing unlike the Zika one.","_id":"685af523b4ac24d5329d8f38"},{"type":"Curator statement","text":"The NS2B peptide used corresponds to the 1416-1468 residues of the Zika virus genome polyprotein.","_id":"685af523b4ac24d5329d8f39"},{"type":"Results","text":"Our NMR results here indicated that only C-terminal residues of ZIKV NS2B remained disordered both in the complex form (Arg73-Lys100; Fig 2E) and in presence of BPTI (Leu86-Lys100; Fig 2F), and the conformation of these C-terminal residues in ZIKV NS2B in these two forms are similar to the uncomplexed form as their HSQC peaks are superimposable (Fig 2C).","_id":"685af523b4ac24d5329d8f3a"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-15T17:11:41.808Z","_id":"685af523b4ac24d5329d8f3b"},"version":0,"_id":"685af523b4ac24d5329d8f35","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-21T19:59:19.322Z","disprot_namespace":"Structural state","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1416,"end":1468,"interaction_partner":[],"reference_html":"Solution conformations of Zika NS2B-NS3pro and its inhibition by natural products from edible plants. <i> Roy A, Lim L, Srivastava S, Lu Y, Song J. </i> PLoS One, 2017","reference_id":"28700665","region_id":"DP01256r021","released":"2022_12","sample":[],"statement":[{"type":"Results","text":"The small absolute values of (ΔCα-ΔCβ) chemical shifts over the whole sequence clearly indicate that the isolated Zika NS2B (48–100) lacks stable secondary structure.","_id":"685af523b4ac24d5329d8f3d"},{"type":"Curator statement","text":"The NS2B peptide used corresponds to the 1416-1468 residues of the Zika virus genome polyprotein.","_id":"685af523b4ac24d5329d8f3e"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-15T17:11:45.263Z","_id":"685af523b4ac24d5329d8f3f"},"version":0,"_id":"685af523b4ac24d5329d8f3c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-21T19:59:51.404Z","disprot_namespace":"Structural transition","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1416,"end":1440,"interaction_partner":[],"reference_html":"Solution conformations of Zika NS2B-NS3pro and its inhibition by natural products from edible plants. <i> Roy A, Lim L, Srivastava S, Lu Y, Song J. </i> PLoS One, 2017","reference_id":"28700665","region_id":"DP01256r022","released":"2022_12","sample":[{"db":"UniProt","deviation":null,"id":"Q32ZE1","statements":[{"type":"Curator statement","text":"The NS3pro protein corresponds to the 1476-2093 residues of the Zika virus genome polyprotein","_id":"685af523b4ac24d5329d8f42"}],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d8f41"}],"statement":[{"type":"Results","text":"The small absolute values of (ΔCα-ΔCβ) chemical shifts over the whole sequence clearly indicate that the isolated Zika NS2B (48–100) lacks stable secondary structure.","_id":"685af523b4ac24d5329d8f43"},{"type":"Curator statement","text":"The NS2B peptide used corresponds to the 1416-1468 residues of the Zika virus genome polyprotein.","_id":"685af523b4ac24d5329d8f44"},{"type":"Results","text":"Our NMR results here indicated that only C-terminal residues of ZIKV NS2B remained disordered both in the complex form (Arg73-Lys100; Fig 2E) and in presence of BPTI (Leu86-Lys100; Fig 2F), and the conformation of these C-terminal residues in ZIKV NS2B in these two forms are similar to the uncomplexed form as their HSQC peaks are superimposable (Fig 2C).","_id":"685af523b4ac24d5329d8f45"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-15T17:11:57.705Z","_id":"685af523b4ac24d5329d8f46"},"version":0,"_id":"685af523b4ac24d5329d8f40","reference_source":"pmid"}],"__v":0,"disorder_content":0.059666569172272595,"disprot_consensus":{"full":[{"start":1416,"end":1440,"type":"T"},{"start":1441,"end":1443,"type":"D"},{"start":1444,"end":1455,"type":"T"},{"start":1456,"end":1470,"type":"D"},{"start":1499,"end":1516,"type":"D"},{"start":2116,"end":2163,"type":"T"},{"start":2822,"end":2836,"type":"D"},{"start":2857,"end":2879,"type":"D"},{"start":2971,"end":2986,"type":"D"},{"start":3093,"end":3121,"type":"D"}],"Structural state":[{"start":1416,"end":1470,"type":"D"},{"start":1499,"end":1516,"type":"D"},{"start":2116,"end":2163,"type":"D"},{"start":2822,"end":2836,"type":"D"},{"start":2857,"end":2879,"type":"D"},{"start":2971,"end":2986,"type":"D"},{"start":3093,"end":3121,"type":"D"}],"Molecular function":[{"start":1444,"end":1455,"type":"F"},{"start":2116,"end":2163,"type":"F"}],"Structural transition":[{"start":1416,"end":1440,"type":"T"},{"start":1444,"end":1455,"type":"T"},{"start":2116,"end":2163,"type":"T"}]}},{"features":{"pfam":[{"id":"PF13499","name":"EF-hand domain pair","start":31,"end":94},{"id":"PF13499","name":"EF-hand domain pair","start":103,"end":167}],"gene3D":[{"start":143,"end":171,"id":"1.10.238.10","name":"EF-hand"},{"start":3,"end":95,"id":"1.10.238.10","name":"EF-hand"},{"start":96,"end":142,"id":"1.10.238.10","name":"EF-hand"}]},"uniref50":"UniRef50_P41208","sequence":"MASNFKKANMASSSQRKRMSPKPELTEEQKQEIREAFDLFDADGTGTIDVKELKVAMRALGFEPKKEEIKKMISEIDKEGTGKMNFGDFLTVMTQKMSEKDTKEEILKAFKLFDDDETGKISFKNLKRVAKELGENLTDEELQEMIDEADRDGDGEVSEQEFLRIMKKTSLY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P41208","disprot_id":"DP01259","ncbi_taxon_id":9606,"regions_counter":1,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":22,"region_id":"DP01259r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The structure of the human centrin 2-xeroderma pigmentosum group C protein complex. <i> Thompson JR, Ryan ZC, Salisbury JL, Kumar R. </i> J Biol Chem, 2006","statement":[{"text":"Disordered HsCen-2 N-terminal Residues—One aspect missing from the HsCen-2 structure is the sequence of amino acids numbered 1-22 from the N-terminal domain, which were determined to be disordered.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"gminervini","start":1,"term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"16627479","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P41208","date":"2018-07-04T09:49:20.000Z","acc":"P41208","name":"Centrin-2","length":172,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012751A","genes":[{"name":{"value":"CETN2"},"synonyms":[{"value":"CALT"},{"value":"CEN2"}]}],"alphafold_very_low_content":0.11627906976744186,"disorder_content":0.12790697674418605,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"}],"Structural state":[{"start":1,"end":22,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01423","name":"LSM domain","start":29,"end":102}],"gene3D":[{"start":1,"end":115,"id":"2.30.30.100","name":"2.30.30.100"}]},"uniref50":"UniRef50_P53905","sequence":"MHQQHSKSENKPQQQRKKFEGPKREAILDLAKYKDSKIRVKLMGGKLVIGVLKGYDQLMNLVLDDTVEYMSNPDDENNTELISKNARKLGLTVIRGTILVSLSSAEGSDVLYMQK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P53905","disprot_id":"DP01261","ncbi_taxon_id":559292,"regions_counter":2,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":26,"region_id":"DP01261r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structures of the Lsm complex bound to the 3' end sequence of U6 small nuclear RNA. <i> Zhou L, Hang J, Zhou Y, Wan R, Lu G, Yin P, Yan C, Shi Y. </i> Nature, 2014","statement":[{"text":"For both the RNA-free and RNA-bound Lsm complexes, the following regions have no clear electron density and are absent in the final atomic models: residues 1–26 and 106–115 of Lsm7. These sequences are all located on the surface and presumably highly flexible.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24240276","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4M7A"},{"db":"PDB","id":"4M7D"},{"db":"PDB","id":"4M75"},{"db":"PDB","id":"4M78"},{"db":"PDB","id":"4M77"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":115,"region_id":"DP01261r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structures of the Lsm complex bound to the 3' end sequence of U6 small nuclear RNA. <i> Zhou L, Hang J, Zhou Y, Wan R, Lu G, Yin P, Yan C, Shi Y. </i> Nature, 2014","statement":[{"text":"For both the RNA-free and RNA-bound Lsm complexes, the following regions have no clear electron density and are absent in the final atomic models: residues 1–26 and 106–115 of Lsm7. These sequences are all located on the surface and presumably highly flexible.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":105,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24240276","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4M7A"},{"db":"PDB","id":"4M7D"},{"db":"PDB","id":"4M75"},{"db":"PDB","id":"4M78"},{"db":"PDB","id":"4M77"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P53905","date":"2018-07-04T10:11:15.000Z","acc":"P53905","name":"U6 snRNA-associated Sm-like protein LSm7","length":115,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI00000530D5","genes":[{"name":{"value":"LSM7"},"orfNames":[{"value":"N1202"},{"value":"N1780"}],"olnNames":[{"value":"YNL147W"}]}],"alphafold_very_low_content":0.008695652173913044,"disorder_content":0.3217391304347826,"disprot_consensus":{"full":[{"start":1,"end":26,"type":"D"},{"start":105,"end":115,"type":"D"}],"Structural state":[{"start":1,"end":26,"type":"D"},{"start":105,"end":115,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02969","name":"TATA box binding protein associated factor (TAF)","start":12,"end":76},{"id":"PF07571","name":"TAF6 C-terminal HEAT repeat domain","start":214,"end":397}],"gene3D":[{"start":9,"end":77,"id":"1.10.20.10","name":"Histone, subunit A"},{"start":213,"end":416,"id":"1.25.40.770","name":"TAF6, C-terminal HEAT repeat domain"}]},"uniref50":"UniRef50_P49848","sequence":"MAEEKKLKLSNTVLPSESMKVVAESMGIAQIQEETCQLLTDEVSYRIKEIAQDALKFMHMGKRQKLTTSDIDYALKLKNVEPLYGFHAQEFIPFRFASGGGRELYFYEEKEVDLSDIINTPLPRVPLDVCLKAHWLSIEGCQPAIPENPPPAPKEQQKAEATEPLKSAKPGQEEDGPLKGKGQGATTADGKGKEKKAPPLLEGAPLRLKPRSIHELSVEQQLYYKEITEACVGSCEAKRAEALQSIATDPGLYQMLPRFSTFISEGVRVNVVQNNLALLIYLMRMVKALMDNPTLYLEKYVHELIPAVMTCIVSRQLCLRPDVDNHWALRDFAARLVAQICKHFSTTTNNIQSRITKTFTKSWVDEKTPWTTRYGSIAGLAELGHDVIKTLILPRLQQEGERIRSVLDGPVLSNIDRIGADHVQSLLLKHCAPVLAKLRPPPDNQDAYRAEFGSLGPLLCSQVVKARAQAALQAQQVNRTTLTITQPRPTLTLSQAPQPGPRTPGLLKVPGSIALPVQTLVSARAAAPPQPSPPPTKFIVMSSSSSAPSTQQVLSLSTSAPGSGSTTTSPVTTTVPSVQPIVKLVSTATTAPPSTAPSGPGSVQKYIVVSLPPTGEGKGGPTSHPSPVPPPASSPSPLSGSALCGGKQEAGDSPPPAPGTPKANGSQPNSGSPQPAP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P49848","disprot_id":"DP01262","ncbi_taxon_id":9606,"regions_counter":3,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":216,"region_id":"DP01262r001","released":"2023_06","ec_id":"ECO:0006224","reference_html":"Structure of promoter-bound TFIID and model of human pre-initiation complex assembly. <i> Louder RK, He Y, López-Blanco JR, Fang J, Chacón P, Nogales E. </i> Nature, 2016","statement":[{"text":"We were unable to detect density near either copy of the TAF6C homodimer for the N-terminal histone fold domain of TAF6, which forms a heterodimer with the histone fold domain of TAF915.","type":"Article"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27007846","version":3,"ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","date":"2023-06-14T09:26:12.342Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5FUR"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":677,"region_id":"DP01262r003","released":"2023_06","ec_id":"ECO:0006224","reference_html":"Structure of promoter-bound TFIID and model of human pre-initiation complex assembly. <i> Louder RK, He Y, López-Blanco JR, Fang J, Chacón P, Nogales E. </i> Nature, 2016","term_id":"IDPO:0000002","curator_id":"vnugnes","start":437,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27007846","version":3,"ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","date":"2023-05-31T13:43:26.268Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5FUR"},{"db":"EMDB","id":"3305"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","disprot_namespace":"Structural state","statement":[{"text":"This region lacks electron density, indicating it is disordered in the Cryo-EM structure of the human TFIID-IIA bound to core promoter DNA.","type":"Curator statement"}]}],"released":"2018_11","uniref100":"UniRef100_P49848","date":"2018-07-04T10:11:35.000Z","acc":"P49848","name":"Transcription initiation factor TFIID subunit 6","length":677,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI0000044681","genes":[{"name":{"value":"TAF6"},"synonyms":[{"value":"TAF2E"},{"value":"TAFII70"}]}],"alphafold_very_low_content":0.3707533234859675,"disorder_content":0.6750369276218612,"disprot_consensus":{"full":[{"start":1,"end":216,"type":"D"},{"start":437,"end":677,"type":"D"}],"Structural state":[{"start":1,"end":216,"type":"D"},{"start":437,"end":677,"type":"D"}]}},{"features":{"pfam":[{"id":"PF07522","name":"DNA repair metallo-beta-lactamase","start":219,"end":299}],"gene3D":[{"start":7,"end":298,"id":"3.60.15.10","name":"Ribonuclease Z/Hydroxyacylglutathione hydrolase-like"},{"start":154,"end":276,"id":"3.40.50.12650","name":"3.40.50.12650"}]},"uniref50":"UniRef50_Q9H816","sequence":"MNGVLIPHTPIAVDFWSLRRAGTARLFFLSHMHSDHTVGLSSTWARPLYCSPITAHLLHRHLQVSKQWIQALEVGESHVLPLDEIGQETMTVTLLDANHCPGSVMFLFEGYFGTILYTGDFRYTPSMLKEPALTLGKQIHTLYLDNTNCNPALVLPSRQEAAHQIVQLIRKHPQHNIKIGLYSLGKESLLEQLALEFQTWVVLSPRRLELVQLLGLADVFTVEEKAGRIHAVDHMEICHSNMLRWNQTHPTIAILPTSRKIHSSHPDIHVIPYSDHSSYSELRAFVAALKPCQVVPIVSRRPCGGFQDSLSPRISVPLIPDSVQQYMSSSSRKPSLLWLLERRLKRPRTQGVVFESPEESADQSQADRDSKKAKKEKLSPWPADLEKQPSHHPLRIKKQLFPDLYSKEWNKAVPFCESQKRVTMLTAPLGFSVHLRSTDEEFISQKTREEIGLGSPLVPMGDDDGGPEATGNQSAWMGHGSPLSHSSKGTPLLATEFRGLALKYLLTPVNFFQAGYSSRRFDQQVEKYHKPC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9H816","disprot_id":"DP01268","ncbi_taxon_id":9606,"regions_counter":1,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":335,"region_id":"DP01268r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The structures of the SNM1A and SNM1B/Apollo nuclease domains reveal a potential basis for their distinct DNA processing activities. <i> Allerston CK, Lee SY, Newman JA, Schofield CJ, McHugh PJ, Gileadi O. </i> Nucleic Acids Res, 2015","statement":[{"text":"the C-terminal peptide (314–335) is not visible in the structure and is assumed to be disordered.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":314,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26582912","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5AHO"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9H816","date":"2018-07-04T10:12:40.000Z","acc":"Q9H816","name":"5' exonuclease Apollo","length":532,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000006FBBC","genes":[{"name":{"value":"DCLRE1B"},"synonyms":[{"value":"SNM1B"}]}],"alphafold_very_low_content":0.34398496240601506,"disorder_content":0.041353383458646614,"disprot_consensus":{"full":[{"start":314,"end":335,"type":"D"}],"Structural state":[{"start":314,"end":335,"type":"D"}]}},{"features":{"pfam":[{"id":"PF18210","name":"Knl1 RWD C-terminal domain","start":2087,"end":2240},{"id":"PF19221","name":"MELT motif","start":165,"end":187},{"id":"PF19221","name":"MELT motif","start":294,"end":317},{"id":"PF19221","name":"MELT motif","start":452,"end":468},{"id":"PF19221","name":"MELT motif","start":500,"end":520},{"id":"PF19221","name":"MELT motif","start":589,"end":607},{"id":"PF19221","name":"MELT motif","start":774,"end":798},{"id":"PF19221","name":"MELT motif","start":884,"end":908},{"id":"PF19221","name":"MELT motif","start":929,"end":949},{"id":"PF19221","name":"MELT motif","start":964,"end":988},{"id":"PF19221","name":"MELT motif","start":1097,"end":1122},{"id":"PF19221","name":"MELT motif","start":1140,"end":1161},{"id":"PF19221","name":"MELT motif","start":1176,"end":1200}]},"uniref50":"UniRef50_Q8NG31","sequence":"MDGVSSEANEENDNIERPVRRRHSSILKPPRSPLQDLRGGNERVQESNALRNKKNSRRVSFADTIKVFQTESHMKIVRKSEMEGCSAMVPSQLQLLPPGFKRFSCLSLPETETGENLLLIQNKKLEDNYCEITGMNTLLSAPIHTQMQQKEFSIIEHTRERKHANDQTVIFSDENQMDLTSSHTVMITKGLLDNPISEKSTKIDTTSFLANLKLHTEDSRMKKEVNFSVDQNTSSENKIDFNDFIKRLKTGKCSAFPDVPDKENFEIPIYSKEPNSASSTHQMHVSLKEDENNSNITRLFREKDDGMNFTQCHTANIQTLIPTSSETNSRESKGNDITIYGNDFMDLTFNHTLQILPATGNFSEIENQTQNAMDVTTGYGTKASGNKTVFKSKQNTAFQDLSINSADKIHITRSHIMGAETHIVSQTCNQDARILAMTPESIYSNPSIQGCKTVFYSSCNDAMEMTKCLSNMREEKNLLKHDSNYAKMYCNPDAMSSLTEKTIYSGEENMDITKSHTVAIDNQIFKQDQSNVQIAAAPTPEKEMMLQNLMTTSEDGKMNVNCNSVPHVSKERIQQSLSNPLSISLTDRKTELLSGENMDLTESHTSNLGSQVPLAAYNLAPESTSESHSQSKSSSDECEEITKSRNEPFQRSDIIAKNSLTDTWNKDKDWVLKILPYLDKDSPQSADCNQEIATSHNIVYCGGVLDKQITNRNTVSWEQSLFSTTKPLFSSGQFSMKNHDTAISSHTVKSVLGQNSKLAEPLRKSLSNPTPDYCHDKMIICSEEEQNMDLTKSHTVVIGFGPSELQELGKTNLEHTTGQLTTMNRQIAVKVEKCGKSPIEKSGVLKSNCIMDVLEDESVQKPKFPKEKQNVKIWGRKSVGGPKIDKTIVFSEDDKNDMDITKSYTIEINHRPLLEKRDCHLVPLAGTSETILYTCRQDDMEITRSHTTALECKTVSPDEITTRPMDKTVVFVDNHVELEMTESHTVFIDYQEKERTDRPNFELSQRKSLGTPTVICTPTEESVFFPGNGESDRLVANDSQLTPLEEWSNNRGPVEVADNMELSKSATCKNIKDVQSPGFLNEPLSSKSQRRKSLKLKNDKTIVFSENHKNDMDITQSCMVEIDNESALEDKEDFHLAGASKTILYSCGQDDMEITRSHTTALECKTLLPNEIAIRPMDKTVLFTDNYSDLEVTDSHTVFIDCQATEKILEENPKFGIGKGKNLGVSFPKDNSCVQEIAEKQALAVGNKIVLHTEQKQQLFAATNRTTNEIIKFHSAAMDEKVIGKVVDQACTLEKAQVESCQLNNRDRRNVDFTSSHATAVCGSSDNYSCLPNVISCTDNLEGSAMLLCDKDEEKANYCPVQNDLAYANDFASEYYLESEGQPLSAPCPLLEKEEVIQTSTKGQLDCVITLHKDQDLIKDPRNLLANQTLVYSQDLGEMTKLNSKRVSFKLPKDQMKVYVDDIYVIPQPHFSTDQPPLPKKGQSSINKEEVILSKAGNKSLNIIENSSAPICENKPKILNSEEWFAAACKKELKENIQTTNYNTALDFHSNSDVTKQVIQTHVNAGEAPDPVITSNVPCFHSIKPNLNNLNGKTGEFLAFQTVHLPPLPEQLLELGNKAHNDMHIVQATEIHNINIISSNAKDSRDEENKKSHNGAETTSLPPKTVFKDKVRRCSLGIFLPRLPNKRNCSVTGIDDLEQIPADTTDINHLETQPVSSKDSGIGSVAGKLNLSPSQYINEENLPVYPDEINSSDSINIETEEKALIETYQKEISPYENKMGKTCNSQKRTWVQEEEDIHKEKKIRKNEIKFSDTTQDREIFDHHTEEDIDKSANSVLIKNLSRTPSSCSSSLDSIKADGTSLDFSTYRSSQMESQFLRDTICEESLREKLQDGRITIREFFILLQVHILIQKPRQSNLPGNFTVNTPPTPEDLMLSQYVYRPKIQIYREDCEARRQKIEELKLSASNQDKLLVDINKNLWEKMRHCSDKELKAFGIYLNKIKSCFTKMTKVFTHQGKVALYGKLVQSAQNEREKLQIKIDEMDKILKKIDNCLTEMETETKNLEDEEKNNPVEEWDSEMRAAEKELEQLKTEEEELQRNLLELEVQKEQTLAQIDFMQKQRNRTEELLDQLSLSEWDVVEWSDDQAVFTFVYDTIQLTITFEESVVGFPFLDKRYRKIVDVNFQSLLDEDQAPPSSLLVHKLIFQYVEEKESWKKTCTTQHQLPKMLEEFSLVVHHCRLLGEEIEYLKRWGPNYNLMNIDINNNELRLLFSSSAAFAKFEITLFLSAYYPSVPLPSTIQNHVGNTSQDDIATILSKVPLENNYLKNVVKQIYQDLFQDCHFYH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q8NG31","disprot_id":"DP01269","ncbi_taxon_id":9606,"regions_counter":7,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":200,"region_id":"DP01269r001","released":"2022_06","ec_id":"ECO:0006220","reference_html":"Structural analysis reveals features of the spindle checkpoint kinase Bub1-kinetochore subunit Knl1 interaction. <i> Krenn V, Wehenkel A, Li X, Santaguida S, Musacchio A. </i> J Cell Biol, 2012","statement":[{"text":"There is interpretable electron density for residues 175–189 of Knl1, whereas the rest of the polypeptide chain is presumably disordered in solvent and therefore invisible in the electron density.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":176,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22331848","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-06-26T18:20:15.627Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4A1G"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T12:37:38.118Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":226,"region_id":"DP01269r002","released":"2022_06","ec_id":"ECO:0006220","reference_html":"Structural analysis reveals features of the spindle checkpoint kinase Bub1-kinetochore subunit Knl1 interaction. <i> Krenn V, Wehenkel A, Li X, Santaguida S, Musacchio A. </i> J Cell Biol, 2012","statement":[{"text":"There is interpretable electron density for residues 175–189 of Knl1, whereas the rest of the polypeptide chain is presumably disordered in solvent and therefore invisible in the electron density.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":217,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22331848","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-06-26T18:21:32.543Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4A1G"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T12:37:35.395Z"}},{"region_id":"DP01269r003","ec_ontology":"ECO","end":252,"ec_name":"far-UV circular dichroism evidence used in manual assertion","start":234,"version":3,"statement":[{"text":"Far-UV circular dichroism spectra reveal a predominantly disorder structure of Blinkin peptide S208-K226 in aqueous solutions.","type":"Figure"},{"text":"Region 208-226 of the Isoform 2 (identifier: Q8NG31-2), used in this study, corresponds to the 234-252 region of the Isoform 1.","type":"Curator statement"}],"term_name":"disorder","reference_html":"Structure of a Blinkin-BUBR1 complex reveals an interaction crucial for kinetochore-mitotic checkpoint regulation via an unanticipated binding Site. <i> Bolanos-Garcia VM, Lischetti T, Matak-Vinković D, Cota E, Simpson PJ, Chirgadze DY, Spring DR, Robinson CV, Nilsson J, Blundell TL. </i> Structure, 2011","released":"2022_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"22000412","date":"2022-06-22T20:09:03.425Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006204","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"SSENKIDFNDFIKRLKTGK","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-26T18:21:50.334Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":251,"term_name":"disorder to order","released":"2022_06","ec_name":"x-ray crystallography evidence used in manual assertion","reference_html":"Structure of a Blinkin-BUBR1 complex reveals an interaction crucial for kinetochore-mitotic checkpoint regulation via an unanticipated binding Site. <i> Bolanos-Garcia VM, Lischetti T, Matak-Vinković D, Cota E, Simpson PJ, Chirgadze DY, Spring DR, Robinson CV, Nilsson J, Blundell TL. </i> Structure, 2011","statement":[{"text":"However, the structure reveals that this Blinkin region undergoes a dramatic disorder-to-order transition upon BUBR1 binding, a feature also observed in TFE-titration experiments of Blinkin mimic peptides monitored by circular dichroism (Figure 3C and inset).","type":"Results"},{"text":"Electron density of the Blinkin residues N211-G225 was clearly visible and unequivocally shows that the side chains of Blinkin residues I213, F215, F218, and I219 form part of a short α helix defined by residues F215-T224 (Figure 2D) that runs parallel to the long axis of BUBR1 TPR1 and TPR2.","type":"Results"},{"text":"Region 208-226 of the Isoform 2 (identifier: Q8NG31-2), used in this study, corresponds to the 234-252 region of the Isoform 1. The residues the authors are referring as visible are N237-251.","type":"Curator statement"}],"term_id":"IDPO:0000011","curator_id":"vnugnes","start":237,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"22000412","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-22T20:36:38.363Z","reference_source":"pmid","ec_id":"ECO:0005670","region_id":"DP01269r004","ec_go":"EXP","disprot_namespace":"Structural transition","cross_refs":[{"db":"PDB","id":"3si5"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8NG31"}],"sequence_construct":"SSENKIDFNDFIKRLKTGK","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-26T18:21:56.373Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":252,"term_name":"protein binding","released":"2022_06","ec_name":"electrospray ionization fourier transform ion cyclotron resonance mass spectrometry evidence used in manual assertion","reference_html":"Structure of a Blinkin-BUBR1 complex reveals an interaction crucial for kinetochore-mitotic checkpoint regulation via an unanticipated binding Site. <i> Bolanos-Garcia VM, Lischetti T, Matak-Vinković D, Cota E, Simpson PJ, Chirgadze DY, Spring DR, Robinson CV, Nilsson J, Blundell TL. </i> Structure, 2011","statement":[{"text":"Nano-ESI MS of synthetic peptides that mimic Blinkin S208-K226 confirm the interaction while peptides harbouring site-specific substitutions indicate the hydrophobic residues I213, F215, F218 and I219 are critical for binding BUBR1.","type":"Results"},{"text":"Region 208-226 of the Isoform 2 (identifier: Q8NG31-2), used in this study, corresponds to the 234-252 region of the Isoform 1. In this sense, residues critical for the interaction are I239, F241, F244 and I245.","type":"Curator statement"}],"term_id":"GO:0005515","curator_id":"vnugnes","start":234,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"22000412","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-22T20:30:02.916Z","reference_source":"pmid","ec_id":"ECO:0006283","region_id":"DP01269r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q8NG31","operator":"and","partner_start":null,"partner_end":null}],"sequence_construct":"SSENKIDFNDFIKRLKTGK","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-26T18:21:57.565Z"}},{"start":234,"end":252,"reference_id":"22331848","reference_source":"pmid","reference_html":"Structural analysis reveals features of the spindle checkpoint kinase Bub1-kinetochore subunit Knl1 interaction. <i> Krenn V, Wehenkel A, Li X, Santaguida S, Musacchio A. </i> J Cell Biol, 2012","date":"2022-06-22T20:59:15.706Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"BMRB","id":"17960"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q8NG31","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01269r006","statement":[{"text":"The micromolar binding affinity of Blinkin S208-K226 peptide for BUBR157-220 (9.3 μM ± 0.4 in 1:1 stoichiometry) reflects a relatively moderate interaction. Nano-ESI MS and 2D NMR titration data confirmed the 1:1 stoichiometry of the interaction.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"sequence_construct":"SSENKIDFNDFIKRLKTG","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-26T18:22:02.623Z"}},{"start":234,"end":252,"reference_id":"22331848","reference_source":"pmid","reference_html":"Structural analysis reveals features of the spindle checkpoint kinase Bub1-kinetochore subunit Knl1 interaction. <i> Krenn V, Wehenkel A, Li X, Santaguida S, Musacchio A. </i> J Cell Biol, 2012","date":"2022-06-22T20:39:41.530Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"3SI5"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q8NG31","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01269r007","statement":[{"text":"The 2.2 Å Crystal Structure of the BUBR1-Blinkin Complex Reveals an Unexpected Mode of Binding","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-26T18:22:04.082Z"}}],"released":"2018_11","uniref100":"UniRef100_Q8NG31","date":"2018-07-04T10:12:50.000Z","acc":"Q8NG31","name":"Kinetochore scaffold 1","length":2342,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI0000E59BD3","genes":[{"name":{"value":"KNL1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:24054","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:24054"}}]},"synonyms":[{"value":"CASC5"},{"value":"KIAA1570"}]}],"alphafold_very_low_content":0.8151152860802733,"disorder_content":0.02305721605465414,"disprot_consensus":{"full":[{"start":176,"end":200,"type":"D"},{"start":217,"end":226,"type":"D"},{"start":234,"end":236,"type":"D"},{"start":237,"end":251,"type":"T"},{"start":252,"end":252,"type":"D"}],"Structural state":[{"start":176,"end":200,"type":"D"},{"start":217,"end":226,"type":"D"},{"start":234,"end":252,"type":"D"}],"Structural transition":[{"start":237,"end":251,"type":"T"}],"Molecular function":[{"start":234,"end":252,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00307","name":"Calponin homology (CH) domain","start":17,"end":117},{"id":"PF03271","name":"EB1-like C-terminal motif","start":210,"end":248}],"gene3D":[{"start":198,"end":230,"id":"1.20.5.1160","name":"Vasodilator-stimulated phosphoprotein"},{"start":1,"end":130,"id":"1.10.418.10","name":"Calponin-like domain"}]},"uniref50":"UniRef50_Q15691","sequence":"MAVNVYSTSVTSDNLSRHDMLAWINESLQLNLTKIEQLCSGAAYCQFMDMLFPGSIALKKVKFQAKLEHEYIQNFKILQAGFKRMGVDKIIPVDKLVKGKFQDNFEFVQWFKKFFDANYDGKDYDPVAARQGQETAVAPSLVAPALNKPKKPLTSSSAAPQRPISTQRTAAAPKAGPGVVRKNPGVGNGDDEAAELMQQVNVLKLTVEDLEKERDFYFGKLRNIELICQENEGENDPVLQRIVDILYATDEGFVIPDEGGPQEEQEEY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q15691","disprot_id":"DP01271","ncbi_taxon_id":9606,"regions_counter":5,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":268,"region_id":"DP01271r001","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Key interaction modes of dynamic +TIP networks. <i> Honnappa S, Okhrimenko O, Jaussi R, Jawhari H, Jelesarov I, Winkler FK, Steinmetz MO. </i> Mol Cell, 2006","statement":[{"text":"The carboxy-terminal acidic sequence segment of EB1c is disordered beyond Thr249 in both copies, and the interaction of residues 249–255 with p150n seen in the contact A mode of EB1c-p150n (Figure 2B) is not present.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":256,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16949363","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-11-24T15:12:52.615Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2HKQ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q14203"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-24T15:13:18.435Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":268,"region_id":"DP01271r002","reference_id":"19632184","start":252,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In free EB1c, the polypeptide segment 194–250 is predominantly structured in solution, whereas the segment 252–268 appears to be flexibly disordered. In complex with APCp1, residues 250–257 of EB1c become ordered (Figure 6B), and chemical shift changes indicate that these residues together with residues 213–225 and 247–249 of the hydrophobic cavity and the polar rim are the major interaction sites (Figure 6C; Figure S7).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"reference_html":"An EB1-binding motif acts as a microtubule tip localization signal. <i> Honnappa S, Gouveia SM, Weisbrich A, Damberger FF, Bhavesh NS, Jawhari H, Grigoriev I, van Rijssel FJ, Buey RM, Lawera A, Jelesarov I, Winkler FK, Wüthrich K, Akhmanova A, Steinmetz MO. </i> Cell, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-24T14:53:09.855Z"}},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P25054","partner_end":null}],"ec_ontology":"ECO","end":257,"region_id":"DP01271r003","reference_id":"19632184","start":250,"term_id":"GO:0005515","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In free EB1c, the polypeptide segment 194–250 is predominantly structured in solution, whereas the segment 252–268 appears to be flexibly disordered. In complex with APCp1, residues 250–257 of EB1c become ordered (Figure 6B), and chemical shift changes indicate that these residues together with residues 213–225 and 247–249 of the hydrophobic cavity and the polar rim are the major interaction sites (Figure 6C; Figure S7).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":4,"reference_html":"An EB1-binding motif acts as a microtubule tip localization signal. <i> Honnappa S, Gouveia SM, Weisbrich A, Damberger FF, Bhavesh NS, Jawhari H, Grigoriev I, van Rijssel FJ, Buey RM, Lawera A, Jelesarov I, Winkler FK, Wüthrich K, Akhmanova A, Steinmetz MO. </i> Cell, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"protein binding","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-24T15:07:16.586Z"}}],"released":"2018_11","uniref100":"UniRef100_Q15691","date":"2018-07-04T10:13:07.000Z","acc":"Q15691","name":"Microtubule-associated protein RP/EB family member 1","length":268,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI000012EB1B","genes":[{"name":{"value":"MAPRE1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6890","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6890"}}]}}],"alphafold_very_low_content":0.16791044776119404,"disorder_content":0.06343283582089553,"disprot_consensus":{"full":[{"start":250,"end":251,"type":"F"},{"start":252,"end":268,"type":"D"}],"Structural state":[{"start":252,"end":268,"type":"D"}],"Molecular function":[{"start":250,"end":257,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00109","name":"Beta-ketoacyl synthase, N-terminal domain","start":31,"end":280},{"id":"PF00109","name":"Beta-ketoacyl synthase, N-terminal domain","start":1489,"end":1739},{"id":"PF00550","name":"Phosphopantetheine attachment site","start":1400,"end":1466},{"id":"PF00550","name":"Phosphopantetheine attachment site","start":3419,"end":3484},{"id":"PF00698","name":"Acyl transferase domain","start":560,"end":880},{"id":"PF00698","name":"Acyl transferase domain","start":2015,"end":2331},{"id":"PF02801","name":"Beta-ketoacyl synthase, C-terminal domain","start":288,"end":406},{"id":"PF02801","name":"Beta-ketoacyl synthase, C-terminal domain","start":1747,"end":1862},{"id":"PF08240","name":"Alcohol dehydrogenase GroES-like domain","start":2850,"end":2927},{"id":"PF08659","name":"KR domain","start":1132,"end":1297},{"id":"PF08659","name":"KR domain","start":3141,"end":3317},{"id":"PF08990","name":"Erythronolide synthase docking domain","start":2,"end":30},{"id":"PF09277","name":"Erythronolide synthase, docking","start":3491,"end":3545},{"id":"PF13602","name":"Zinc-binding dehydrogenase","start":3005,"end":3131},{"id":"PF14765","name":"Polyketide synthase dehydratase N-terminal domain","start":2503,"end":2645},{"id":"PF16197","name":"Ketoacyl-synthetase C-terminal extension","start":408,"end":523},{"id":"PF16197","name":"Ketoacyl-synthetase C-terminal extension","start":1867,"end":1977},{"id":"PF21089","name":"Polyketide synthase dehydratase domain","start":2377,"end":2475},{"id":"PF22953","name":"Polyketide synthase extender module SpnB, Rossmann fold domain","start":949,"end":1114},{"id":"PF22953","name":"Polyketide synthase extender module SpnB, Rossmann fold domain","start":2661,"end":2809}],"gene3D":[{"start":1480,"end":1932,"id":"3.40.47.10","name":"3.40.47.10"},{"start":2366,"end":2649,"id":"3.10.129.110","name":"Polyketide synthase dehydratase"},{"start":27,"end":467,"id":"3.40.47.10","name":"3.40.47.10"},{"start":2014,"end":2316,"id":"3.40.366.10","name":"Malonyl-Coenzyme A Acyl Carrier Protein, domain 2"},{"start":560,"end":864,"id":"3.40.366.10","name":"Malonyl-Coenzyme A Acyl Carrier Protein, domain 2"},{"start":1381,"end":1473,"id":"1.10.1200.10","name":"ACP-like"},{"start":3399,"end":3491,"id":"1.10.1200.10","name":"ACP-like"},{"start":473,"end":902,"id":"3.30.70.3290","name":"3.30.70.3290"},{"start":903,"end":1365,"id":"3.40.50.720","name":"NAD(P)-binding Rossmann-like Domain"},{"start":2821,"end":3135,"id":"3.90.180.10","name":"Medium-chain alcohol dehydrogenases, catalytic domain"},{"start":3136,"end":3380,"id":"3.40.50.720","name":"NAD(P)-binding Rossmann-like Domain"},{"start":2650,"end":2812,"id":"3.40.50.11460","name":"3.40.50.11460"},{"start":3497,"end":3537,"id":"1.20.5.1140","name":"Docking domain of the erythromycin polyketide synthase (DEBS)"},{"start":1933,"end":2358,"id":"3.30.70.3290","name":"3.30.70.3290"}]},"uniref50":"UniRef50_Q03132","sequence":"MTDSEKVAEYLRRATLDLRAARQRIRELESDPIAIVSMACRLPGGVNTPQRLWELLREGGETLSGFPTDRGWDLARLHHPDPDNPGTSYVDKGGFLDDAAGFDAEFFGVSPREAAAMDPQQRLLLETSWELVENAGIDPHSLRGTATGVFLGVAKFGYGEDTAAAEDVEGYSVTGVAPAVASGRISYTMGLEGPSISVDTACSSSLVALHLAVESLRKGESSMAVVGGAAVMATPGVFVDFSRQRALAADGRSKAFGAGADGFGFSEGVTLVLLERLSEARRNGHEVLAVVRGSALNQDGASNGLSAPSGPAQRRVIRQALESCGLEPGDVDAVEAHGTGTALGDPIEANALLDTYGRDRDADRPLWLGSVKSNIGHTQAAAGVTGLLKVVLALRNGELPATLHVEEPTPHVDWSSGGVALLAGNQPWRRGERTRRARVSAFGISGTNAHVIVEEAPEREHRETTAHDGRPVPLVVSARTTAALRAQAAQIAELLERPDADLAGVGLGLATTRARHEHRAAVVASTREEAVRGLREIAAGAATADAVVEGVTEVDGRNVVFLFPGQGSQWAGMGAELLSSSPVFAGKIRACDESMAPMQDWKVSDVLRQAPGAPGLDRVDVVQPVLFAVMVSLAELWRSYGVEPAAVVGHSQGEIAAAHVAGALTLEDAAKLVVGRSRLMRSLSGEGGMAAVALGEAAVRERLRPWQDRLSVAAVNGPRSVVVSGEPGALRAFSEDCAAEGIRVRDIDVDYASHSPQIERVREELLETTGDIAPRPARVTFHSTVESRSMDGTELDARYWYRNLRETVRFADAVTRLAESGYDAFIEVSPHPVVVQAVEEAVEEADGAEDAVVVGSLHRDGGDLSAFLRSMATAHVSGVDIRWDVALPGAAPFALPTYPFQRKRYWLQPAAPAAASDELAYRVSWTPIEKPESGNLDGDWLVVTPLISPEWTEMLCEAINANGGRALRCEVDTSASRTEMAQAVAQAGTGFRGVLSLLSSDESACRPGVPAGAVGLLTLVQALGDAGVDAPVWCLTQGAVRTPADDDLARPAQTTAHGFAQVAGLELPGRWGGVVDLPESVDDAALRLLVAVLRGGGRAEDHLAVRDGRLHGRRVVRASLPQSGSRSWTPHGTVLVTGAASPVGDQLVRWLADRGAERLVLAGACPGDDLLAAVEEAGASAVVCAQDAAALREALGDEPVTALVHAGTLTNFGSISEVAPEEFAETIAAKTALLAVLDEVLGDRAVEREVYCSSVAGIWGGAGMAAYAAGSAYLDALAEHHRARGRSCTSVAWTPWALPGGAVDDGYLRERGLRSLSADRAMRTWERVLAAGPVSVAVADVDWPVLSEGFAATRPTALFAELAGRGGQAEAEPDSGPTGEPAQRLAGLSPDEQQENLLELVANAVAEVLGHESAAEINVRRAFSELGLDSLNAMALRKRLSASTGLRLPASLVFDHPTVTALAQHLRARLVGDADQAAVRVVGAADESEPIAIVGIGCRFPGGIGSPEQLWRVLAEGANLTTGFPADRGWDIGRLYHPDPDNPGTSYVDKGGFLTDAADFDPGFFGITPREALAMDPQQRLMLETAWEAVERAGIDPDALRGTDTGVFVGMNGQSYMQLLAGEAERVDGYQGLGNSASVLSGRIAYTFGWEGPALTVDTACSSSLVGIHLAMQALRRGECSLALAGGVTVMSDPYTFVDFSTQRGLASDGRCKAFSARADGFALSEGVAALVLEPLSRARANGHQVLAVLRGSAVNQDGASNGLAAPNGPSQERVIRQALAASGVPAADVDVVEAHGTGTELGDPIEAGALIATYGQDRDRPLRLGSVKTNIGHTQAAAGAAGVIKVVLAMRHGMLPRSLHADELSPHIDWESGAVEVLREEVPWPAGERPRRAGVSSFGVSGTNAHVIVEEAPAEQEAARTERGPLPFVLSGRSEAVVAAQARALAEHLRDTPELGLTDAAWTLATGRARFDVRAAVLGDDRAGVCAELDALAEGRPSADAVAPVTSAPRKPVLVFPGQGAQWVGMARDLLESSEVFAESMSRCAEALSPHTDWKLLDVVRGDGGPDPHERVDVLQPVLFSIMVSLAELWRAHGVTPAAVVGHSQGEIAAAHVAGALSLEAAAKVVALRSQVLRELDDQGGMVSVGASRDELETVLARWDGRVAVAAVNGPGTSVVAGPTAELDEFFAEAEAREMKPRRIAVRYASHSPEVARIEDRLAAELGTITAVRGSVPLHSTVTGEVIDTSAMDASYWYRNLRRPVLFEQAVRGLVEQGFDTFVEVSPHPVLLMAVEETAEHAGAEVTCVPTLRREQSGPHEFLRNLLRAHVHGVGADLRPAVAGGRPAELPTYPFEHQRFWPRPHRPADVSALGVRGAEHPLLLAAVDVPGHGGAVFTGRLSTDEQPWLAEHVVGGRTLVPGSVLVDLALAAGEDVGLPVLEELVLQRPLVLAGAGALLRMSVGAPDESGRRTIDVHAAEDVADLADAQWSQHATGTLAQGVAAGPRDTEQWPPEDAVRIPLDDHYDGLAEQGYEYGPSFQALRAAWRKDDSVYAEVSIAADEEGYAFHPVLLDAVAQTLSLGALGEPGGGKLPFAWNTVTLHASGATSVRVVATPAGADAMALRVTDPAGHLVATVDSLVVRSTGEKWEQPEPRGGEGELHALDWGRLAEPGSTGRVVAADASDLDAVLRSGEPEPDAVLVRYEPEGDDPRAAARHGVLWAAALVRRWLEQEELPGATLVIATSGAVTVSDDDSVPEPGAAAMWGVIRCAQAESPDRFVLLDTDAEPGMLPAVPDNPQLALRGDDVFVPRLSPLAPSALTLPAGTQRLVPGDGAIDSVAFEPAPDVEQPLRAGEVRVDVRATGVNFRDVLLALGMYPQKADMGTEAAGVVTAVGPDVDAFAPGDRVLGLFQGAFAPIAVTDHRLLARVPDGWSDADAAAVPIAYTTAHYALHDLAGLRAGQSVLIHAAAGGVGMAAVALARRAGAEVLATAGPAKHGTLRALGLDDEHIASSRETGFARKFRERTGGRGVDVVLNSLTGELLDESADLLAEDGVFVEMGKTDLRDAGDFRGRYAPFDLGEAGDDRLGEILREVVGLLGAGELDRLPVSAWELGSAPAALQHMSRGRHVGKLVLTQPAPVDPDGTVLITGGTGTLGRLLARHLVTEHGVRHLLLVSRRGADAPGSDELRAEIEDLGASAEIAACDTADRDALSALLDGLPRPLTGVVHAAGVLADGLVTSIDEPAVEQVLRAKVDAAWNLHELTANTGLSFFVLFSSAASVLAGPGQGVYAAANESLNALAALRRTRGLPAKALGWGLWAQASEMTSGLGDRIARTGVAALPTERALALFDSALRRGGEVVFPLSINRSALRRAEFVPEVLRGMVRAKLRAAGQAEAAGPNVVDRLAGRSESDQVAGLAELVRSHAAAVSGYGSADQLPERKAFKDLGFDSLAAVELRNRLGTATGVRLPSTLVFDHPTPLAVAEHLRDRLFAASPAVDIGDRLDELEKALEALSAEDGHDDVGQRLESLLRRWNSRRADAPSTSAISEDASDDELFSMLDQRFGGGEDL","taxonomy":["Bacteria","Actinobacteria","Pseudonocardiales","Pseudonocardiaceae","Saccharopolyspora"],"uniref90":"UniRef90_Q03132","disprot_id":"DP01272","ncbi_taxon_id":1836,"regions_counter":2,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":922,"region_id":"DP01272r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural and mechanistic analysis of protein interactions in module 3 of the 6-deoxyerythronolide B synthase. <i> Tang Y, Chen AY, Kim CY, Cane DE, Khosla C. </i> Chem Biol, 2007","statement":[{"text":"no electron density was observed for two N-terminal residues, fourteen C-terminal residues, and eleven residues from two internal disordered regions.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":908,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17719492","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2QO3"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":2653,"region_id":"DP01272r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the erythromycin polyketide synthase dehydratase. <i> Keatinge-Clay A. </i> J Mol Biol, 2008","statement":[{"text":"Three regions of the constructed DH fragment were unobservable in the electron density maps: 1) the N-terminal histidine tag and H2362-A2365, (2) the C-terminal residues S2641-G2653, and 3) the loop P2582-G2585.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":2641,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18952099","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3EL6"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q03132","date":"2018-07-04T10:13:12.000Z","acc":"Q03132","name":"6-deoxyerythronolide-B synthase EryA2, modules 3 and 4","length":3567,"organism":"Saccharopolyspora erythraea","dataset":[],"UniParc":"UPI000012A187","genes":[{"name":{"value":"eryA","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"1740151","url":"http://www.ncbi.nlm.nih.gov/pubmed/1740151","alternativeUrl":"https://europepmc.org/abstract/MED/1740151"}}]}}],"disorder_content":0.00784973366975049,"disprot_consensus":{"full":[{"start":908,"end":922,"type":"D"},{"start":2641,"end":2653,"type":"D"}],"Structural state":[{"start":908,"end":922,"type":"D"},{"start":2641,"end":2653,"type":"D"}]}},{"features":{"pfam":[{"id":"PF16788","name":"ATF-interacting protein binding domain","start":564,"end":775},{"id":"PF16794","name":"Fibronectin-III type domain","start":1160,"end":1260}],"gene3D":[{"start":1154,"end":1269,"id":"2.60.40.10","name":"Immunoglobulins"}]},"uniref50":"UniRef50_Q6VMQ6","sequence":"MDSLEEPQKKVFKARKTMRVSDRQQLEAVYKVKEELLKTDVKLLNGNHENGDLDPTSPLENMDYIKDKEEVNGIEEICFDPEGSKAEWKETPCILSVNVKNKQDDDLNCEPLSPHNITPEPVSKLPAEPVSGDPAPGDLDAGDPASGVLASGDSTSGDPTSSEPSSSDAASGDATSGDAPSGDVSPGDATSGDATADDLSSGDPTSSDPIPGEPVPVEPISGDCAADDIASSEITSVDLASGAPASTDPASDDLASGDLSSSELASDDLATGELASDELTSESTFDRTFEPKSVPVCEPVPEIDNIEPSSNKDDDFLEKNGADEKLEQIQSKDSLDEKNKADNNIDANEETLETDDTTICSDRPPENEKKVEEDIITELALGEDAISSSMEIDQGEKNEDETSADLVETINENVIEDNKSENILENTDSMETDEIIPILEKLAPSEDELTCFSKTSLLPIDETNPDLEEKMESSFGSPSKQESSESLPKEAFLVLSDEEDISGEKDESEVISQNETCSPAEVESNEKDNKPEEEEQVIHEDDERPSEKNEFSRRKRSKSEDMDNVQSKRRRYMEEEYEAEFQVKITAKGDINQKLQKVIQWLLEEKLCALQCAVFDKTLAELKTRVEKIECNKRHKTVLTELQAKIARLTKRFEAAKEDLKKRHEHPPNPPVSPGKTVNDVNSNNNMSYRNAGTVRQMLESKRNVSESAPPSFQTPVNTVSSTNLVTPPAVVSSQPKLQTPVTSGSLTATSVLPAPNTATVVATTQVPSGNPQPTISLQPLPVILHVPVAVSSQPQLLQSHPGTLVTNQPSGNVEFISVQSPPTVSGLTKNPVSLPSLPNPTKPNNVPSVPSPSIQRNPTASAAPLGTTLAVQAVPTAHSIVQATRTSLPTVGPSGLYSPSTNRGPIQMKIPISAFSTSSAAEQNSNTTPRIENQTNKTIDASVSKKAADSTSQCGKATGSDSSGVIDLTMDDEESGASQDPKKLNHTPVSTMSSSQPVSRPLQPIQPAPPLQPSGVPTSGPSQTTIHLLPTAPTTVNVTHRPVTQVTTRLPVPRAPANHQVVYTTLPAPPAQAPLRGTVMQAPAVRQVNPQNSVTVRVPQTTTYVVNNGLTLGSTGPQLTVHHRPPQVHTEPPRPVHPAPLPEAPQPQRLPPEAASTSLPQKPHLKLARVQSQNGIVLSWSVLEVDRSCATVDSYHLYAYHEEPSATVPSQWKKIGEVKALPLPMACTLTQFVSGSKYYFAVRAKDIYGRFGPFCDPQSTDVISSTQSS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q6VMQ6","disprot_id":"DP01277","ncbi_taxon_id":9606,"regions_counter":1,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":964,"region_id":"DP01277r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of the small ubiquitin-like modifier (SUMO)-interacting motif of MBD1-containing chromatin-associated factor 1 bound to SUMO-3. <i> Sekiyama N, Ikegami T, Yamane T, Ikeguchi M, Uchimura Y, Baba D, Ariyoshi M, Tochio H, Saitoh H, Shirakawa M. </i> J Biol Chem, 2008","statement":[{"text":"The disordered 32 N-terminal (five amino acids (GSPEF) from the vector and residues 938 –964 of\nMCAF1), the 6 C-terminal residues of SIM MCAF1 , and the 15 N-terminal residues of SUMO-3 are omitted from all\nfigures for clarity","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"gminervini","start":938,"term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"18842587","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q6VMQ6","date":"2018-07-04T11:09:47.000Z","acc":"Q6VMQ6","name":"Activating transcription factor 7-interacting protein 1","length":1270,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00001D6EB8","genes":[{"name":{"value":"ATF7IP","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:20092","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:20092"}}]},"synonyms":[{"value":"MCAF"},{"value":"MCAF1"}]}],"alphafold_very_low_content":0.7661417322834646,"disorder_content":0.02125984251968504,"disprot_consensus":{"full":[{"start":938,"end":964,"type":"D"}],"Structural state":[{"start":938,"end":964,"type":"D"}]}},{"features":{"pfam":[{"id":"PF15275","name":"PEHE domain","start":474,"end":591},{"id":"PF16801","name":"Dimerisation domain of Male-specific-Lethal 1","start":215,"end":250}],"gene3D":[{"start":209,"end":267,"id":"1.20.5.170","name":"1.20.5.170"}]},"uniref50":"UniRef50_Q6PDM1","sequence":"MTMRSAVFKAAAAPAGGNPEQRLDYERAAALGGPEDEPGAAEAHFLPRHRKLKEPGPPLASSQGGSPAPSPAGCGGKGRGLLLPAGAAPGQQEESWGGSVPLPCPPPATKQAGIGGEPAAAGAGCSPRPKYQAVLPIQTGSLVAAAKEPTPWAGDKGGAASPAATASDPAGPPPLPLPGPPPLAPTATAGTLAASEGRWKSMRKSPLGGGGGSGASSQAACLKQILLLQLDLIEQQQQQLQAKEKEIEELKSERDTLLARIERMERRMQLVKKDNEKERHKLFQGYETEEREETELSEKIKLECQPELSETSQTLPPKPFSCGRSGKGHKRKSPFGSTERKTPVKKLAPEFSKVKTKTPKHSPIKEEPCGSLSETVCKRELRSQETPEKPRSSVDTPPRLSTPQKGPSTHPKEKAFSSEIEDLPYLSTTEMYLCRWHQPPPSPLPLRESSPKKEETVARCLMPSSVAGETSVLAVPSWRDHSVEPLRDPNPSDLLENLDDSVFSKRHAKLELDEKRRKRWDIQRIREQRILQRLQLRMYKKKGIQESEPEVTSFFPEPDDVESLMITPFLPVVAFGRPLPKLTPQNFELPWLDERSRCRLEIQKKQTPHRTCRK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q6PDM1","disprot_id":"DP01278","ncbi_taxon_id":9606,"regions_counter":1,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":568,"region_id":"DP01278r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1. <i> Kadlec J, Hallacli E, Lipp M, Holz H, Sanchez-Weatherby J, Cusack S, Akhtar A. </i> Nat Struct Mol Biol, 2011","statement":[{"text":"The disordered regions in MSL1 and MSL3 are shown as dots.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"gminervini","start":558,"term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"21217699","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q68DK7","date":"2018-07-04T12:47:00.000Z","acc":"Q68DK7","name":"Male-specific lethal 1 homolog","length":614,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000041A0E7","genes":[{"name":{"value":"MSL1"},"synonyms":[{"value":"MSL1L1"}]}],"alphafold_very_low_content":0.5456026058631922,"disorder_content":0.017915309446254073,"disprot_consensus":{"full":[{"start":558,"end":568,"type":"D"}],"Structural state":[{"start":558,"end":568,"type":"D"}]}},{"features":{"pfam":[{"id":"PF05712","name":"MRG","start":160,"end":505},{"id":"PF22732","name":"MSL3 chromodomain-like","start":11,"end":87}],"gene3D":[{"start":165,"end":312,"id":"1.10.274.30","name":"MRG domain"},{"start":417,"end":518,"id":"1.10.274.30","name":"MRG domain"},{"start":1,"end":91,"id":"2.30.30.140","name":"2.30.30.140"}]},"uniref50":"UniRef50_Q8N5Y2","sequence":"MSASEGMKFKFHSGEKVLCFEPDPTKARVLYDAKIVDVIVGKDEKGRKIPEYLIHFNGWNRSWDRWAAEDHVLRDTDENRRLQRKLARKAVARLRSTGRKKKRCRLPGVDSVLKGLPTEEKDENDENSLSSSSDCSENKDEEISEESDIEEKTEVKEEPELQTRREMEERTITIEIPEVLKKQLEDDCYYINRRKRLVKLPCQTNIITILESYVKHFAINAAFSANERPRHHHVMPHANMNVHYIPAEKNVDLCKEMVDGLRITFDYTLPLVLLYPYEQAQYKKVTSSKFFLPIKESATSTNRSQEELSPSPPLLNPSTPQSTESQPTTGEPATPKRRKAEPEALQSLRRSTRHSANCDRLSESSASPQPKRRQQDTSASMPKLFLHLEKKTPVHSRSSSPIPLTPSKEGSAVFAGFEGRRTNEINEVLSWKLVPDNYPPGDQPPPPSYIYGAQHLLRLFVKLPEILGKMSFSEKNLKALLKHFDLFLRFLAEYHDDFFPESAYVAACEAHYSTKNPRAIY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q8N5Y2","disprot_id":"DP01279","ncbi_taxon_id":9606,"regions_counter":2,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":246,"region_id":"DP01279r001","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1. <i> Kadlec J, Hallacli E, Lipp M, Holz H, Sanchez-Weatherby J, Cusack S, Akhtar A. </i> Nat Struct Mol Biol, 2011","statement":[{"text":"The disordered regions in MSL1 and MSL3 are shown as dots.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":226,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"21217699","version":4,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-11-24T12:32:15.220Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"2Y0N"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6PDM1"}]},{"start":508,"end":518,"reference_id":"21217699","reference_source":"pmid","reference_html":"Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1. <i> Kadlec J, Hallacli E, Lipp M, Holz H, Sanchez-Weatherby J, Cusack S, Akhtar A. </i> Nat Struct Mol Biol, 2011","date":"2023-05-04T17:56:33.126Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP01279r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6PDM1"}],"statement":[{"text":"The disordered regions in MSL1 and MSL3 are shown as dots.","type":"Figure"}]}],"released":"2018_11","uniref100":"UniRef100_Q8N5Y2","date":"2018-07-04T12:50:22.000Z","acc":"Q8N5Y2","name":"Male-specific lethal 3 homolog","length":521,"organism":"Homo sapiens","dataset":["NDDs-related proteins","RNA-binding proteins"],"UniParc":"UPI000006E6B7","genes":[{"name":{"value":"MSL3"},"synonyms":[{"value":"MSL3L1"}]}],"alphafold_very_low_content":0.39539347408829173,"disorder_content":0.061420345489443376,"disprot_consensus":{"full":[{"start":226,"end":246,"type":"D"},{"start":508,"end":518,"type":"D"}],"Structural state":[{"start":226,"end":246,"type":"D"},{"start":508,"end":518,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00014","name":"Kunitz/Bovine pancreatic trypsin inhibitor domain","start":290,"end":341},{"id":"PF02177","name":"Amyloid A4 N-terminal heparin-binding","start":31,"end":131},{"id":"PF03494","name":"Beta-amyloid peptide (beta-APP)","start":676,"end":713},{"id":"PF10515","name":"Beta-amyloid precursor protein C-terminus","start":716,"end":766},{"id":"PF12924","name":"Copper-binding of amyloid precursor, CuBD","start":132,"end":188},{"id":"PF12925","name":"E2 domain of amyloid precursor protein","start":367,"end":548}],"gene3D":[{"start":131,"end":189,"id":"3.30.1490.140","name":"Amyloidogenic glycoprotein, copper-binding domain"},{"start":363,"end":580,"id":"1.20.120.770","name":"Amyloid precursor protein, E2 domain"},{"start":17,"end":123,"id":"3.90.570.10","name":"Amyloidogenic glycoprotein, heparin-binding domain"},{"start":742,"end":770,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":672,"end":711,"id":"4.10.230.10","name":"Amyloidogenic glycoprotein, amyloid-beta peptide"},{"start":278,"end":354,"id":"4.10.410.10","name":"Pancreatic trypsin inhibitor Kunitz domain"}]},"uniref50":"UniRef50_P05067","sequence":"MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSAMSQSLLKTTQEPLARDPVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHSFGADSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P05067","disprot_id":"DP01280","ncbi_taxon_id":9606,"regions_counter":11,"creator":"eficho","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":711,"region_id":"DP01280r001","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Solution structure of methionine-oxidized amyloid beta-peptide (1-40). Does oxidation affect conformational switching? <i> Watson AA, Fairlie DP, Craik DJ. </i> Biochemistry, 1998","statement":[{"text":"On the other hand, the unoxidized Aβ(1−40) initially produces a CD spectrum characteristic of a random coil, but this changes over several days (Figure 1b) to that of a β-sheet structure that is associated with aggregation and fibril formation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":672,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-12-15T14:10:37.756Z","reference_source":"pmid","term_name":"disorder","reference_id":"9737846","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Biological process","ec_ontology":"ECO","end":711,"term_name":"amyloid fibril formation","released":"2023_12","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Solution structure of methionine-oxidized amyloid beta-peptide (1-40). Does oxidation affect conformational switching? <i> Watson AA, Fairlie DP, Craik DJ. </i> Biochemistry, 1998","statement":[{"text":"On the other hand, the unoxidized Aβ(1−40) initially produces a CD spectrum characteristic of a random coil, but this changes over several days (Figure 1b) to that of a β-sheet structure that is associated with aggregation and fibril formation.","type":"Results"}],"term_id":"GO:1990000","curator_id":"vnugnes","start":672,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"9737846","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-12-15T14:28:35.047Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01280r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":711,"term_name":"disorder to order","released":"2023_12","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Solution structure of methionine-oxidized amyloid beta-peptide (1-40). Does oxidation affect conformational switching? <i> Watson AA, Fairlie DP, Craik DJ. </i> Biochemistry, 1998","statement":[{"text":"On the other hand, the unoxidized Aβ(1−40) initially produces a CD spectrum characteristic of a random coil, but this changes over several days (Figure 1b) to that of a β-sheet structure that is associated with aggregation and fibril formation.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"vnugnes","start":672,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"9737846","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-12-15T14:27:43.539Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01280r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":686,"region_id":"DP01280r004","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Solution structure of methionine-oxidized amyloid beta-peptide (1-40). Does oxidation affect conformational switching? <i> Watson AA, Fairlie DP, Craik DJ. </i> Biochemistry, 1998","statement":[{"text":"The main structural feature is an α-helix spanning residues 16−24. The rest of the peptide appears to be disordered with poor superimposition in other regions, including the second helical region (residues 28−36, rmsd of 2.2 Å) found for Aβ(1−40).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":672,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-12-15T14:22:15.992Z","reference_source":"pmid","term_name":"disorder","reference_id":"9737846","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":711,"region_id":"DP01280r005","released":"2023_12","ec_id":"ECO:0006204","reference_html":"High-resolution NMR characterization of low abundance oligomers of amyloid-β without purification. <i> Kotler SA, Brender JR, Vivekanandan S, Suzuki Y, Yamamoto K, Monette M, Krishnamoorthy J, Walsh P, Cauble M, Holl MM, Marsh EN, Ramamoorthy A. </i> Sci Rep, 2015","statement":[{"text":"A noticeably different CD spectrum is apparent in the filtrate, which shows a strong minimum near 198 nm indicative of a predominantly disordered structure (Fig. 1a, blue) very similar to that of early aggregation states of Aβ (Fig. 1a, red).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":672,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-12-15T13:48:59.648Z","reference_source":"pmid","term_name":"disorder","reference_id":"26138908","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":711,"region_id":"DP01280r009","released":"2023_12","ec_id":"ECO:0006165","reference_html":"High-resolution NMR characterization of low abundance oligomers of amyloid-β without purification. <i> Kotler SA, Brender JR, Vivekanandan S, Suzuki Y, Yamamoto K, Monette M, Krishnamoorthy J, Walsh P, Cauble M, Holl MM, Marsh EN, Ramamoorthy A. </i> Sci Rep, 2015","statement":[{"text":"Taken together, this finding suggests a dynamic and disordered structure with a high degree of turns and twists but without a well-defined secondary structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":672,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-12-15T13:47:56.428Z","reference_source":"pmid","term_name":"disorder","reference_id":"26138908","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":672,"end":711,"reference_id":"26138908","reference_source":"pmid","reference_html":"High-resolution NMR characterization of low abundance oligomers of amyloid-β without purification. <i> Kotler SA, Brender JR, Vivekanandan S, Suzuki Y, Yamamoto K, Monette M, Krishnamoorthy J, Walsh P, Cauble M, Holl MM, Marsh EN, Ramamoorthy A. </i> Sci Rep, 2015","date":"2023-12-15T14:01:42.257Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006333","ec_ontology":"ECO","ec_name":"thioflavin T based fluorescence spectroscopy evidence","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01280r010","statement":[{"text":"Conversely, an intense ThT signal is present in the isolated fibril fraction. Measuring the concentration of the spin-X filtrate by the bicinchoninic acid (BCA) protein concentration assay (Thermo Scientific) revealed 17.0 ± 6.0 μM or only 7.3 + 2.6% of the total Aβ1-40 concentration (231 μM) was not fibrillar. Together, the ThT, CD, and BCA results confirm the sample primarily consists of amyloid fibrils with a minority population of a largely disordered, relatively low MW species.","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false},{"start":672,"end":711,"reference_id":"26138908","reference_source":"pmid","reference_html":"High-resolution NMR characterization of low abundance oligomers of amyloid-β without purification. <i> Kotler SA, Brender JR, Vivekanandan S, Suzuki Y, Yamamoto K, Monette M, Krishnamoorthy J, Walsh P, Cauble M, Holl MM, Marsh EN, Ramamoorthy A. </i> Sci Rep, 2015","date":"2023-12-15T14:04:10.478Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","region_id":"DP01280r011","statement":[{"text":"In contrast to the sparse spectra obtained from unaggregated Aβ1-40, the RFDR-based 2D 1H/1H spectra of the aggregated sample showed multiple cross-peaks consistent with the presence of the disordered oligomer suggested by the CD, fluorescence, and AFM experiments (Fig.1).","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_P05067","date":"2018-07-04T13:28:57.000Z","acc":"P05067","name":"Amyloid-beta precursor protein","length":770,"organism":"Homo sapiens","dataset":["Condensates-related proteins","Age-related disorders proteins"],"UniParc":"UPI000002A2F6","genes":[{"name":{"value":"APP","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:620","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:620"}}]},"synonyms":[{"value":"A4","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"2881207","url":"http://www.ncbi.nlm.nih.gov/pubmed/2881207","alternativeUrl":"https://europepmc.org/abstract/MED/2881207"}}]},{"value":"AD1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:620","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:620"}}]}]}],"alphafold_very_low_content":0.35194805194805195,"disorder_content":0.05194805194805195,"disprot_consensus":{"full":[{"start":672,"end":711,"type":"T"}],"Structural state":[{"start":672,"end":711,"type":"D"}],"Biological process":[{"start":672,"end":711,"type":"F"}],"Structural transition":[{"start":672,"end":711,"type":"T"}]}},{"features":{"pfam":[{"id":"PF15150","name":"Phorbol-12-myristate-13-acetate-induced","start":1,"end":34},{"id":"PF15150","name":"Phorbol-12-myristate-13-acetate-induced","start":50,"end":103}]},"uniref50":"UniRef50_Q9JM54","sequence":"MPGRKARRNAPVNPTRAELPPEFAAQLRKIGDKVYCTWSAPDITVVLAQMPGKSQKSRMRSPSPTRVPADLKDECAQLRRIGDKVNLRQKLLNLISKLFNLVT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q9JM54","disprot_id":"DP01281","ncbi_taxon_id":10090,"regions_counter":5,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":42,"region_id":"DP01281r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structure of the BH3 domains from the p53-inducible BH3-only proteins Noxa and Puma in complex with Mcl-1. <i> Day CL, Smits C, Fan FC, Lee EF, Fairlie WD, Hinds MG. </i> J Mol Biol, 2008","statement":[{"text":"NoxaA, Puma, NoxaB and\nBim BH3 domains have CD spectra typical for unstructured\npeptides","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":16,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18589438","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":42,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Structure of the BH3 domains from the p53-inducible BH3-only proteins Noxa and Puma in complex with Mcl-1. <i> Day CL, Smits C, Fan FC, Lee EF, Fairlie WD, Hinds MG. </i> J Mol Biol, 2008","statement":[{"text":"Although in isolation the Puma and NoxaA BH3\npeptides are unstructured in solution, when bound\nto Mcl-1, they form well-ordered α-helices","type":"Discussion"}],"term_id":"GO:0005515","curator_id":"eschad","start":16,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"18589438","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","cross_refs":[{"db":"PDB","id":"2ROD"}],"region_id":"DP01281r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":42,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Structure of the BH3 domains from the p53-inducible BH3-only proteins Noxa and Puma in complex with Mcl-1. <i> Day CL, Smits C, Fan FC, Lee EF, Fairlie WD, Hinds MG. </i> J Mol Biol, 2008","statement":[{"text":"Although in isolation the Puma and NoxaA BH3\npeptides are unstructured in solution, when bound\nto Mcl-1, they form well-ordered α-helices","type":"Discussion"}],"term_id":"IDPO:0000011","curator_id":"eschad","start":16,"term_ontology":"IDPO","curator_name":"Eva Schad","reference_id":"18589438","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01281r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":93,"region_id":"DP01281r004","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structure of the BH3 domains from the p53-inducible BH3-only proteins Noxa and Puma in complex with Mcl-1. <i> Day CL, Smits C, Fan FC, Lee EF, Fairlie WD, Hinds MG. </i> J Mol Biol, 2008","statement":[{"text":"NoxaA, Puma, NoxaB and\nBim BH3 domains have CD spectra typical for unstructured\npeptides","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":73,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18589438","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":93,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Structure of the BH3 domains from the p53-inducible BH3-only proteins Noxa and Puma in complex with Mcl-1. <i> Day CL, Smits C, Fan FC, Lee EF, Fairlie WD, Hinds MG. </i> J Mol Biol, 2008","statement":[{"text":"Mcl-1 binds both NoxaA and NoxaB","type":"Results"}],"term_id":"GO:0005515","curator_id":"eschad","start":73,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"18589438","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","cross_refs":[{"db":"PDB","id":"2NL9"}],"region_id":"DP01281r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q9JM54","date":"2018-07-04T14:08:32.000Z","acc":"Q9JM54","name":"Phorbol-12-myristate-13-acetate-induced protein 1","length":103,"organism":"Mus musculus","dataset":[],"UniParc":"UPI000002238B","genes":[{"name":{"value":"Pmaip1"},"synonyms":[{"value":"Noxa"}]}],"alphafold_very_low_content":0.17475728155339806,"disorder_content":0.46601941747572817,"disprot_consensus":{"full":[{"start":16,"end":42,"type":"T"},{"start":73,"end":93,"type":"D"}],"Structural state":[{"start":16,"end":42,"type":"D"},{"start":73,"end":93,"type":"D"}],"Molecular function":[{"start":16,"end":42,"type":"F"},{"start":73,"end":93,"type":"F"}],"Structural transition":[{"start":16,"end":42,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00400","name":"WD domain, G-beta repeat","start":172,"end":205},{"id":"PF00400","name":"WD domain, G-beta repeat","start":220,"end":255},{"id":"PF00400","name":"WD domain, G-beta repeat","start":263,"end":301},{"id":"PF00400","name":"WD domain, G-beta repeat","start":309,"end":345},{"id":"PF00400","name":"WD domain, G-beta repeat","start":366,"end":401},{"id":"PF12265","name":"Histone-binding protein RBBP4 or subunit C of CAF1 complex","start":18,"end":87}],"gene3D":[{"start":2,"end":423,"id":"2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"}]},"uniref50":"UniRef50_Q16576","sequence":"MASKEMFEDTVEERVINEEYKIWKKNTPFLYDLVMTHALQWPSLTVQWLPEVTKPEGKDYALHWLVLGTHTSDEQNHLVVARVHIPNDDAQFDASHCDSDKGEFGGFGSVTGKIECEIKINHEGEVNRARYMPQNPHIIATKTPSSDVLVFDYTKHPAKPDPSGECNPDLRLRGHQKEGYGLSWNSNLSGHLLSASDDHTVCLWDINAGPKEGKIVDAKAIFTGHSAVVEDVAWHLLHESLFGSVADDQKLMIWDTRSNTTSKPSHLVDAHTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKLHTFESHKDEIFQVHWSPHNETILASSGTDRRLNVWDLSKIGEEQSAEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVICSVSEDNIMQIWQMAENIYNDEESDVTTSELEGQGS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q16576","disprot_id":"DP01282","ncbi_taxon_id":9606,"regions_counter":2,"creator":"jmanso","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":110,"region_id":"DP01282r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for the recognition of histone H4 by the histone-chaperone RbAp46. <i> Murzina NV, Pei XY, Zhang W, Sparkes M, Vicente-Garcia J, Pratap JV, McLaughlin SH, Ben-Shahar TR, Verreault A, Luisi BF, Laue ED. </i> Structure, 2008","statement":[{"text":"The structure is well defined, except for the N terminus (residues 2–8), a segment comprising residues 90–109, and the C terminus (residues 409–425), for which the electron density is unclear due to structural disorder","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jmanso","start":90,"term_ontology":"IDPO","curator_name":"Jose A Manso","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18571423","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":425,"region_id":"DP01282r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for the recognition of histone H4 by the histone-chaperone RbAp46. <i> Murzina NV, Pei XY, Zhang W, Sparkes M, Vicente-Garcia J, Pratap JV, McLaughlin SH, Ben-Shahar TR, Verreault A, Luisi BF, Laue ED. </i> Structure, 2008","statement":[{"text":"The structure is well defined, except for the N terminus (residues 2–8), a segment comprising residues 90–109, and the C terminus (residues 409–425), for which the electron density is unclear due to structural disorder","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jmanso","start":409,"term_ontology":"IDPO","curator_name":"Jose A Manso","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18571423","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q16576","date":"2018-07-04T14:50:34.000Z","acc":"Q16576","name":"Histone-binding protein RBBP7","length":425,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000001ED","genes":[{"name":{"value":"RBBP7"},"synonyms":[{"value":"RBAP46"}]}],"alphafold_very_low_content":0.07764705882352942,"disorder_content":0.08941176470588236,"disprot_consensus":{"full":[{"start":90,"end":110,"type":"D"},{"start":409,"end":425,"type":"D"}],"Structural state":[{"start":90,"end":110,"type":"D"},{"start":409,"end":425,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03357","name":"Snf7","start":18,"end":187}]},"uniref50":"UniRef50_Q9Y3E7","sequence":"MGLFGKTQEKPPKELVNEWSLKIRKEMRVVDRQIRDIQREEEKVKRSVKDAAKKGQKDVCIVLAKEMIRSRKAVSKLYASKAHMNSVLMGMKNQLAVLRVAGSLQKSTEVMKAMQSLVKIPEIQATMRELSKEMMKAGIIEEMLEDTFESMDDQEEMEEEAEMEIDRILFEITAGALGKAPSKVTDALPEPEPPGAMAASEDEEEEEEALEAMQSRLATLRS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9Y3E7","disprot_id":"DP01283","ncbi_taxon_id":9606,"regions_counter":2,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":199,"region_id":"DP01283r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for ESCRT-III CHMP3 recruitment of AMSH. <i> Solomons J, Sabin C, Poudevigne E, Usami Y, Hulsik DL, Macheboeuf P, Hartlieb B, Göttlinger H, Weissenhorn W. </i> Structure, 2011","statement":[{"text":"residues 184–199 do not contribute to the interaction and are disordered in the structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"gminervini","start":184,"term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"21827950","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":199,"term_name":"molecular function inhibitor activity","start":184,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","statement":[{"text":"Here we present structural evidence for a closed and open conformation of full length CHMP3, which confirms the activated state represented by the CHMP3 crystal structure. Both conformations do not reveal any changes in their secondary structure content or in their overall thermal stability, indicating that a first step in activation entails detachment of the C-terminal module from the N-terminal core.","type":"Introduction"}],"curator_id":"gminervini","released":"2022_03","term_ontology":"GO","curator_name":"Giovanni Minervini","reference_id":"21827950","version":3,"reference_html":"Structural basis for ESCRT-III CHMP3 recruitment of AMSH. <i> Solomons J, Sabin C, Poudevigne E, Usami Y, Hulsik DL, Macheboeuf P, Hartlieb B, Göttlinger H, Weissenhorn W. </i> Structure, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140678","ec_id":"ECO:0006220","cross_refs":[{"db":"PMC2756293","id":""}],"region_id":"DP01283r002","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q9Y3E7","date":"2018-07-04T15:00:51.000Z","acc":"Q9Y3E7","name":"Charged multivesicular body protein 3","length":222,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000006E953","genes":[{"name":{"value":"CHMP3"},"synonyms":[{"value":"CGI149"},{"value":"NEDF"},{"value":"VPS24"}],"orfNames":[{"value":"CGI-149"}]}],"alphafold_very_low_content":0.11261261261261261,"disorder_content":0.07207207207207207,"disprot_consensus":{"full":[{"start":184,"end":199,"type":"D"}],"Structural state":[{"start":184,"end":199,"type":"D"}],"Molecular function":[{"start":184,"end":199,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00623","name":"RNA polymerase Rpb1, domain 2","start":356,"end":521},{"id":"PF04983","name":"RNA polymerase Rpb1, domain 3","start":525,"end":691},{"id":"PF04990","name":"RNA polymerase Rpb1, domain 7","start":1164,"end":1299},{"id":"PF04992","name":"RNA polymerase Rpb1, domain 6","start":896,"end":1079},{"id":"PF04997","name":"RNA polymerase Rpb1, domain 1","start":16,"end":354},{"id":"PF04998","name":"RNA polymerase Rpb1, domain 5","start":830,"end":895},{"id":"PF04998","name":"RNA polymerase Rpb1, domain 5","start":1080,"end":1163},{"id":"PF04998","name":"RNA polymerase Rpb1, domain 5","start":1300,"end":1425},{"id":"PF05000","name":"RNA polymerase Rpb1, domain 4","start":718,"end":823},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1589,"end":1600},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1616,"end":1629},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1630,"end":1643},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1644,"end":1657},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1658,"end":1671},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1672,"end":1685},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1686,"end":1699},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1700,"end":1713},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1714,"end":1727},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1728,"end":1741},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1742,"end":1755},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1757,"end":1769},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1770,"end":1783},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1784,"end":1797},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1798,"end":1811},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1833,"end":1846},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1847,"end":1860},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1861,"end":1874},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1875,"end":1888},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1896,"end":1909},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1917,"end":1930},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1941,"end":1954}],"gene3D":[{"start":1164,"end":1300,"id":"3.30.1360.140","name":"3.30.1360.140"},{"start":525,"end":686,"id":"1.10.274.100","name":"RNA polymerase Rpb1, domain 3"},{"start":687,"end":832,"id":"1.10.132.30","name":"1.10.132.30"},{"start":269,"end":319,"id":"1.20.120.1280","name":"RNA polymerase II, clamp domain"},{"start":1427,"end":1471,"id":"1.10.150.390","name":"1.10.150.390"},{"start":346,"end":516,"id":"2.40.40.20","name":"2.40.40.20"},{"start":389,"end":452,"id":"3.30.1490.180","name":"RNA polymerase ii"},{"start":9,"end":122,"id":"1.20.120.1280","name":"RNA polymerase II, clamp domain"}]},"uniref50":"UniRef50_P24928","sequence":"MHGGGPPSGDSACPLRTIKRVQFGVLSPDELKRMSVTEGGIKYPETTEGGRPKLGGLMDPRQGVIERTGRCQTCAGNMTECPGHFGHIELAKPVFHVGFLVKTMKVLRCVCFFCSKLLVDSNNPKIKDILAKSKGQPKKRLTHVYDLCKGKNICEGGEEMDNKFGVEQPEGDEDLTKEKGHGGCGRYQPRIRRSGLELYAEWKHVNEDSQEKKILLSPERVHEIFKRISDEECFVLGMEPRYARPEWMIVTVLPVPPLSVRPAVVMQGSARNQDDLTHKLADIVKINNQLRRNEQNGAAAHVIAEDVKLLQFHVATMVDNELPGLPRAMQKSGRPLKSLKQRLKGKEGRVRGNLMGKRVDFSARTVITPDPNLSIDQVGVPRSIAANMTFAEIVTPFNIDRLQELVRRGNSQYPGAKYIIRDNGDRIDLRFHPKPSDLHLQTGYKVERHMCDGDIVIFNRQPTLHKMSMMGHRVRILPWSTFRLNLSVTTPYNADFDGDEMNLHLPQSLETRAEIQELAMVPRMIVTPQSNRPVMGIVQDTLTAVRKFTKRDVFLERGEVMNLLMFLSTWDGKVPQPAILKPRPLWTGKQIFSLIIPGHINCIRTHSTHPDDEDSGPYKHISPGDTKVVVENGELIMGILCKKSLGTSAGSLVHISYLEMGHDITRLFYSNIQTVINNWLLIEGHTIGIGDSIADSKTYQDIQNTIKKAKQDVIEVIEKAHNNELEPTPGNTLRQTFENQVNRILNDARDKTGSSAQKSLSEYNNFKSMVVSGAKGSKINISQVIAVVGQQNVEGKRIPFGFKHRTLPHFIKDDYGPESRGFVENSYLAGLTPTEFFFHAMGGREGLIDTAVKTAETGYIQRRLIKSMESVMVKYDATVRNSINQVVQLRYGEDGLAGESVEFQNLATLKPSNKAFEKKFRFDYTNERALRRTLQEDLVKDVLSNAHIQNELEREFERMREDREVLRVIFPTGDSKVVLPCNLLRMIWNAQKIFHINPRLPSDLHPIKVVEGVKELSKKLVIVNGDDPLSRQAQENATLLFNIHLRSTLCSRRMAEEFRLSGEAFDWLLGEIESKFNQAIAHPGEMVGALAAQSLGEPATQMTLNTFHYAGVSAKNVTLGVPRLKELINISKKPKTPSLTVFLLGQSARDAERAKDILCRLEHTTLRKVTANTAIYYDPNPQSTVVAEDQEWVNVYYEMPDFDVARISPWLLRVELDRKHMTDRKLTMEQIAEKINAGFGDDLNCIFNDDNAEKLVLRIRIMNSDENKMQEEEEVVDKMDDDVFLRCIESNMLTDMTLQGIEQISKVYMHLPQTDNKKKIIITEDGEFKALQEWILETDGVSLMRVLSEKDVDPVRTTSNDIVEIFTVLGIEAVRKALERELYHVISFDGSYVNYRHLALLCDTMTCRGHLMAITRHGVNRQDTGPLMKCSFEETVDVLMEAAAHGESDPMKGVSENIMLGQLAPAGTGCFDLLLDAEKCKYGMEIPTNIPGLGAAGPTGMFFGSAPSPMGGISPAMTPWNQGATPAYGAWSPSVGSGMTPGAAGFSPSAASDASGFSPGYSPAWSPTPGSPGSPGPSSPYIPSPGGAMSPSYSPTSPAYEPRSPGGYTPQSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPNYTPTSPSYSPTSPSYSPTSPNYTPTSPNYSPTSPSYSPTSPSYSPTSPSYSPSSPRYTPQSPTYTPSSPSYSPSSPSYSPTSPKYTPTSPSYSPSSPEYTPTSPKYSPTSPKYSPTSPKYSPTSPTYSPTTPKYSPTSPTYSPTSPVYTPTSPKYSPTSPTYSPTSPKYSPTSPTYSPTSPKGSTYSPTSPGYSPTSPTYSLTSPAISPDDSDEEN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P24928","disprot_id":"DP01284","ncbi_taxon_id":9606,"regions_counter":3,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1970,"region_id":"DP01284r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Lysines in the RNA Polymerase II C-Terminal Domain Contribute to TAF15 Fibril Recruitment. <i> Janke AM, Seo DH, Rahmanian V, Conicella AE, Mathews KL, Burke KA, Mittal J, Fawzi NL. </i> Biochemistry, 2018","statement":[{"text":"Human RNA polymerase II CTD heptads 27-52 is predominantly disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":1773,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28945358","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-16T16:03:10.458Z"}},{"start":1773,"end":1970,"reference_id":"28945358","reference_source":"pmid","reference_html":"Lysines in the RNA Polymerase II C-Terminal Domain Contribute to TAF15 Fibril Recruitment. <i> Janke AM, Seo DH, Rahmanian V, Conicella AE, Mathews KL, Burke KA, Mittal J, Fawzi NL. </i> Biochemistry, 2018","date":"2023-05-16T16:16:46.154Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0050436","term_name":"microfibril binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q92804","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01284r002","statement":[{"text":"Dark-state exchange saturation transfer (DEST) NMR probes the binding of CTD27-52 WT to sonicated TAF15 fibrils","type":"Figure"},{"text":"However, in the presence of sonicated fibrils we reliably observe decreased peak intensity and increased transverse relaxation, ΔR2, of CTD27-52 which can be explained by transient binding of CTD27-52 to the high molecular weight fibrillar segments25.","type":"Results"}],"term_comment":"See also the cellular component term 'microfibril ; GO:0001527'.","term_def":"\"Binding to a microfibril, any small fibril occurring in biological material.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:10:50.994Z"}},{"start":1773,"end":1960,"reference_id":"28945358","reference_source":"pmid","reference_html":"Lysines in the RNA Polymerase II C-Terminal Domain Contribute to TAF15 Fibril Recruitment. <i> Janke AM, Seo DH, Rahmanian V, Conicella AE, Mathews KL, Burke KA, Mittal J, Fawzi NL. </i> Biochemistry, 2018","date":"2023-05-16T16:21:52.547Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0050436","term_name":"microfibril binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"Q92804","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01284r003","statement":[{"text":"As previously observed5, high avidity binding of the CTD27-52 in solution corresponds to CTD27-52 fluorescence localization around the outer ring of each mCherry-TAF15 LC hydrogel.","type":"Results"},{"text":"However, when dilute CTD Δ1961-1970 is incubated with intact TAF15 hydrogels, CTD Δ1961-1970 fluorescence localization and recovery after photobleaching are almost identical to that of WT (the half life and diffusion rate of CTD Δ1961-1970 were 56.6 ± 7.1 seconds and 0.096 ± 0.012 μm2/s, respectively, compared to 58.0 ± 0.3 seconds and 0.094 ± 0.001 μm2/s for WT) (Figure S8D–E).","type":"Results"}],"term_comment":"See also the cellular component term 'microfibril ; GO:0001527'.","term_def":"\"Binding to a microfibril, any small fibril occurring in biological material.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:10:57.442Z"}}],"released":"2018_11","uniref100":"UniRef100_P24928","date":"2018-07-04T15:01:57.000Z","acc":"P24928","name":"DNA-directed RNA polymerase II subunit RPB1","length":1970,"organism":"Homo sapiens","dataset":["NDDs-related proteins","Condensates-related proteins","RNA-binding proteins"],"UniParc":"UPI0000140EB9","genes":[{"name":{"value":"POLR2A","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9187","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9187"}}]},"synonyms":[{"value":"POLR2"}]}],"alphafold_very_low_content":0.24974619289340103,"disorder_content":0.10050761421319797,"disprot_consensus":{"full":[{"start":1773,"end":1970,"type":"D"}],"Structural state":[{"start":1773,"end":1970,"type":"D"}],"Molecular function":[{"start":1773,"end":1970,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01873","name":"Domain found in IF2B/IF5","start":24,"end":133}],"gene3D":[{"start":34,"end":106,"id":"3.30.70.3150","name":"3.30.70.3150"}]},"uniref50":"UniRef50_Q97W59","sequence":"MSSEKEYVEMLDRLYSKLPEKGRKEGTQSLPNMIILNIGNTTIIRNFAEYCDRIRREDKICMKYLLKELAAPGNVDDKGELVIQGKFSSQVINTLMERFLKAYVECSTCKSLDTILKKEKKSWYIVCLACGAQTPVKPL","taxonomy":["Archaea","Crenarchaeota","Thermoprotei","Sulfolobales","Sulfolobaceae","Saccharolobus"],"uniref90":"UniRef90_Q97W59","disprot_id":"DP01285","ncbi_taxon_id":273057,"regions_counter":1,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":139,"region_id":"DP01285r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the intact archaeal translation initiation factor 2 demonstrates very high conformational flexibility in the alpha- and beta-subunits. <i> Stolboushkina E, Nikonov S, Nikulin A, Bläsi U, Manstein DJ, Fedorov R, Garber M, Nikonov O. </i> J Mol Biol, 2008","statement":[{"text":"Figure 6 clearly shows that only the N-terminal α-helical parts of aIF2β (residues 5–17) retain their positions in all known structures. The conformations of the central parts and zinc-binding domains of aIF2β vary in each structure","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"gminervini","start":18,"term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"18675278","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q97W59","date":"2018-07-04T15:31:30.000Z","acc":"Q97W59","name":"Translation initiation factor 2 subunit beta","length":139,"organism":"Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)","dataset":[],"UniParc":"UPI000012D29C","genes":[{"name":{"value":"eif2b","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00232","url":"https://hamap.expasy.org/unirule/MF_00232"}}]},"synonyms":[{"value":"aif2b"}],"olnNames":[{"value":"SSO2381"}]}],"alphafold_very_low_content":0.02877697841726619,"disorder_content":0.8776978417266187,"disprot_consensus":{"full":[{"start":18,"end":139,"type":"D"}],"Structural state":[{"start":18,"end":139,"type":"D"}]}},{"features":{"pfam":[{"id":"PF08088","name":"Conotoxin I-superfamily","start":1,"end":42}]},"uniref50":"UniRef50_Q7Z094","sequence":"GPSFCKADEKPCEYHADCCNCCLSGICAPSTNWILPGCSTSSFFKI","taxonomy":["Eukaryota","Metazoa","Spiralia","Lophotrochozoa","Mollusca","Gastropoda","Caenogastropoda","Neogastropoda","Conoidea","Conidae","Conus","Phasmoconus"],"uniref90":"UniRef90_Q7Z094","disprot_id":"DP01286","dataset":[],"ncbi_taxon_id":61198,"regions_counter":2,"creator":"gminervini","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":46,"region_id":"DP01286r001","reference_id":"17696362","start":36,"ec_id":"ECO:0006165","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Indeed, apart from the first few residues, the structure is well defined up to around residue 35 and does adopt an ICK structure.","type":"Abstract"},{"text":"The C-terminal region, including Phe44, is disordered.","type":"Abstract"},{"text":"Thus, even though the regions of conformational space sampled by the families of structures of ι-RXIA and ι-RXIA[l-Phe44] differ slightly in Figure 6, no conclusions can be drawn about the solution conformations of the C-terminal tail containing Phe44 other than that they are disordered in both cases.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"reference_html":"Structure and sodium channel activity of an excitatory I1-superfamily conotoxin. <i> Buczek O, Wei D, Babon JJ, Yang X, Fiedler B, Chen P, Yoshikami D, Olivera BM, Bulaj G, Norton RS. </i> Biochemistry, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q7Z094","date":"2018-07-04T16:03:59.000Z","acc":"Q7Z094","name":"Iota-conotoxin RXIA","length":46,"organism":"Conus radiatus","UniParc":"UPI00001AE1E1","genes":[],"alphafold_very_low_content":0.17391304347826086,"disorder_content":0.2391304347826087,"disprot_consensus":{"full":[{"start":36,"end":46,"type":"D"}],"Structural state":[{"start":36,"end":46,"type":"D"}]}},{"features":{"gene3D":[{"start":74,"end":143,"id":"3.30.160.60","name":"Classic Zinc Finger"}],"pfam":[]},"uniref50":"UniRef50_Q9VZU1","sequence":"MHSEKHTPDIRELMPVREHRCERCPSLVFGNLSHYQLHLRRRHQEVIPPSVIGPIVAFHCPVEKCIYHVATKGARSFTSLRLLRQHYQKSHLDKNYKCLACGGKFLLQHHLEKHQCSKHKCPVCELTYNSKAGLRTHMRRKNHLVHHESDKVPIPSLATWKRLNPQPIPVSADSLTAHSLKTGSDLHPSEEYINNLPSNLAGVTELYAEIPNPEANMPSTLELDTNLPAAEEHILCFLPIMDVSYALEMSSQKLDMETQTEEDDLNEIRNEVLAPLLRDIETQTPDTRGDIGTMTDDFPEEQEPVAVGSHFHAYSETEPMFDLQTSAHMYTQTCDDLFEELGLSHIQTQTHWPDGLYNTQHTQTCDEIMDELFPDNFQSTCTQTRWLD","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_Q9VZU1","disprot_id":"DP01287","ncbi_taxon_id":7227,"regions_counter":3,"creator":"mguha","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":388,"region_id":"DP01287r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Multivalency regulates activity in an intrinsically disordered transcription factor. <i> Clark S, Myers JB, King A, Fiala R, Novacek J, Pearce G, Heierhorst J, Reichow SL, Barbar EJ. </i> Elife, 2018","statement":[{"text":"A high level of disorder in dLBD is revealed by the limited amide proton chemical shift dispersion in 15N HSQC spectra.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mguha","start":241,"term_ontology":"IDPO","curator_name":"Mainak Guharoy","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29714690","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":388,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Multivalency regulates activity in an intrinsically disordered transcription factor. <i> Clark S, Myers JB, King A, Fiala R, Novacek J, Pearce G, Heierhorst J, Reichow SL, Barbar EJ. </i> Elife, 2018","statement":[{"text":"We demonstrate that the long intrinsically disordered C-terminal domain of ASCIZ binds LC8 to form a dynamic ensemble of complexes.","type":"Abstract"}],"term_id":"GO:0005515","curator_id":"mguha","start":241,"term_ontology":"GO","curator_name":"Mainak Guharoy","reference_id":"29714690","version":3,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01287r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":388,"region_id":"DP01287r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Multivalency regulates activity in an intrinsically disordered transcription factor. <i> Clark S, Myers JB, King A, Fiala R, Novacek J, Pearce G, Heierhorst J, Reichow SL, Barbar EJ. </i> Elife, 2018","statement":[{"text":"The dLBD CD spectrum has a large negative ellipticity at 200 nm, indicating that it is primarily disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mguha","start":241,"term_ontology":"IDPO","curator_name":"Mainak Guharoy","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29714690","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9VZU1","date":"2018-07-04T20:30:27.000Z","acc":"Q9VZU1","name":"ASCIZ zinc finger protein, isoform A","length":388,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI0000076FA3","genes":[{"name":{"value":"Asciz","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47726.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47726.1"}},{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0035407","url":"http://flybase.org/reports/FBgn0035407.html"}}]},"synonyms":[{"value":"CC15","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47726.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47726.1"}}]},{"value":"dASCIZ","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47726.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47726.1"}}]},{"value":"Digitor","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47726.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47726.1"}}]},{"value":"Dmel\\CG14962","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47726.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47726.1"}}]}],"orfNames":[{"value":"CG14962","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47726.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47726.1"}},{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0035407","url":"http://flybase.org/reports/FBgn0035407.html"}}]},{"value":"Dmel_CG14962","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47726.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47726.1"}}]}]}],"alphafold_very_low_content":0.5592783505154639,"disorder_content":0.38144329896907214,"disprot_consensus":{"full":[{"start":241,"end":388,"type":"D"}],"Structural state":[{"start":241,"end":388,"type":"D"}],"Molecular function":[{"start":241,"end":388,"type":"F"}]}},{"features":{"gene3D":[{"start":80,"end":187,"id":"3.30.160.60","name":"Classic Zinc Finger"}],"pfam":[{"id":"PF24757","name":"ASCIZ first and second C2H2 zinc finger domains","start":83,"end":112},{"id":"PF24757","name":"ASCIZ first and second C2H2 zinc finger domains","start":130,"end":163},{"id":"PF24759","name":"ASCIZ third C2HC zinc finger domain","start":164,"end":188},{"id":"PF24761","name":"ASCIZ forth C2H2 zinc finger domain","start":190,"end":220}]},"uniref50":"UniRef50_O43313","sequence":"MAASEAAAAAGSAALAAGARAVPAATTGAAAAASGPWVPPGPRLRGSRPRPAGATQQPAVPAPPAGELIQPSVSELSRAVRTNILCTVRGCGKILPNSPALNMHLVKSHRLQDGIVNPTIRKDLKTGPKFYCCPIEGCPRGPERPFSQFSLVKQHFMKMHAEKKHKCSKCSNSYGTEWDLKRHAEDCGKTFRCTCGCPYASRTALQSHIYRTGHEIPAEHRDPPSKKRKMENCAQNQKLSNKTIESLNNQPIPRPDTQELEASEIKLEPSFEDSCGSNTDKQTLTTPPRYPQKLLLPKPKVALVKLPVMQFSVMPVFVPTADSSAQPVVLGVDQGSATGAVHLMPLSVGTLILGLDSEACSLKESLPLFKIANPIAGEPISTGVQVNFGKSPSNPLQELGNTCQKNSISSINVQTDLSYASQNFIPSAQWATADSSVSSCSQTDLSFDSQVSLPISVHTQTFLPSSKVTSSIAAQTDAFMDTCFQSGGVSRETQTSGIESPTDDHVQMDQAGMCGDIFESVHSSYNVATGNIISNSLVAETVTHSLLPQNEPKTLNQDIEKSAPIINFSAQNSMLPSQNMTDNQTQTIDLLSDLENILSSNLPAQTLDHRSLLSDTNPGPDTQLPSGPAQNPGIDFDIEEFFSASNIQTQTEESELSTMTTEPVLESLDIETQTDFLLADTSAQSYGCRGNSNFLGLEMFDTQTQTDLNFFLDSSPHLPLGSILKHSSFSVSTDSSDTETQTEGVSTAKNIPALESKVQLNSTETQTMSSGFETLGSLFFTSNETQTAMDDFLLADLAWNTMESQFSSVETQTSAEPHTVSNF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O43313","disprot_id":"DP01288","ncbi_taxon_id":9606,"regions_counter":2,"creator":"mguha","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":823,"region_id":"DP01288r001","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Multivalency regulates activity in an intrinsically disordered transcription factor. <i> Clark S, Myers JB, King A, Fiala R, Novacek J, Pearce G, Heierhorst J, Reichow SL, Barbar EJ. </i> Elife, 2018","statement":[{"text":"We similarly assessed the gel mobility of complexes formed by LC8 and the LC8-binding domain of human ASCIZ (hLBD).\nMolecular sieving is the dominate effect on hLBD mobility as both hLBD and dLBD are disordered and highly extended.\nhLBD:LC8 complexes form a dynamic ensemble....Titration of the hLBD with LC8 by size-exclusion chromatography (Fig 4d) supports our interpretation of the native gel experiments in Fig 4c.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mguha","start":362,"term_ontology":"IDPO","curator_name":"Mainak Guharoy","ec_name":"chromatography evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29714690","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":823,"term_name":"protein binding","released":"2022_03","ec_name":"chromatography evidence used in manual assertion","reference_html":"Multivalency regulates activity in an intrinsically disordered transcription factor. <i> Clark S, Myers JB, King A, Fiala R, Novacek J, Pearce G, Heierhorst J, Reichow SL, Barbar EJ. </i> Elife, 2018","term_id":"GO:0005515","curator_id":"mguha","start":362,"term_ontology":"GO","curator_name":"Mainak Guharoy","reference_id":"29714690","version":3,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","region_id":"DP01288r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_O43313","date":"2018-07-04T20:46:46.000Z","acc":"O43313","name":"ATM interactor","length":823,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00001397CC","genes":[{"name":{"value":"ATMIN"},"synonyms":[{"value":"KIAA0431"},{"value":"ZNF822"}]}],"alphafold_very_low_content":0.7424058323207776,"disorder_content":0.5613608748481167,"disprot_consensus":{"full":[{"start":362,"end":823,"type":"D"}],"Structural state":[{"start":362,"end":823,"type":"D"}],"Molecular function":[{"start":362,"end":823,"type":"F"}]}},{"features":{"pfam":[{"id":"PF15731","name":"Antitoxin component of bacterial toxin-antitoxin system, MqsA","start":28,"end":101}],"gene3D":[{"start":4,"end":101,"id":"1.10.260.40","name":"lambda repressor-like DNA-binding domains"}]},"uniref50":"UniRef50_Q9KMA5","sequence":"MSNRDLFAELSSALVEAKQHSEGKLTLKTHHVNDVGELNISPDEIVSIREQFNMSRGVFARLLHTSSRTLENWEQGRSVPNGQAVTLLKLVQRHPETLSHIAEL","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Vibrionales","Vibrionaceae","Vibrio"],"uniref90":"UniRef90_Q9KMA5","disprot_id":"DP01289","dataset":["Unicellular toxins and antitoxins"],"ncbi_taxon_id":243277,"regions_counter":26,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":36,"region_id":"DP01289r001","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Ribosome-dependent Vibrio cholerae mRNAse HigB2 is regulated by a β-strand sliding mechanism. <i> Hadži S, Garcia-Pino A, Haesaerts S, Jurenas D, Gerdes K, Lah J, Loris R. </i> Nucleic Acids Res, 2017","statement":[{"text":"Together with the CD data, this thus agrees with a model in which the VcHigA2 antitoxin has a well-structured dimeric C-terminal domain, as seen in the crystal structure, and ~36 amino acids long disordered N-terminal segment.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mguha","start":1,"term_ontology":"IDPO","curator_name":"Mainak Guharoy","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T17:21:45.014Z","curator_name":"Bálint Mészáros"},"reference_id":"28334932","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":36,"region_id":"DP01289r002","reference_html":"Ribosome-dependent Vibrio cholerae mRNAse HigB2 is regulated by a β-strand sliding mechanism. <i> Hadži S, Garcia-Pino A, Haesaerts S, Jurenas D, Gerdes K, Lah J, Loris R. </i> Nucleic Acids Res, 2017","ec_id":"ECO:0006204","version":3,"term_id":"IDPO:0000002","curator_id":"rpancsa","start":1,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"The CD spectrum of the N-terminal region in its native state (attached to the C-terminal domain) was estimated by calculating the difference spectrum between full length VcHigA2 and a truncate (VcHigA2ΔN) consisting of amino acid residues 37–104. The latter protein, which mirrors the residues seen in the crystal structure, is thermodynamically stable and shows a CD spectrum with essentially the same α-helical content as the full length protein (Figure ​(Figure2B). The difference spectrum is similar to the spectrum of the isolated peptide and suggests presence of the random coil structure (gray and blue curves, Figure2B).","type":"Results"}],"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T17:22:38.904Z","curator_name":"Bálint Mészáros"},"released":"2022_03","reference_id":"28334932","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":36,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Ribosome-dependent Vibrio cholerae mRNAse HigB2 is regulated by a β-strand sliding mechanism. <i> Hadži S, Garcia-Pino A, Haesaerts S, Jurenas D, Gerdes K, Lah J, Loris R. </i> Nucleic Acids Res, 2017","statement":[{"text":"The interaction between VcHigA2 and VcHigB2 is characterised by a very high affinity and by structuring of the antitoxin N-terminal domain. Coupled folding and binding is evident from the comparison of the CD spectra from free and the VcHigB2-bound VcHigA2.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"mguha","start":1,"term_ontology":"IDPO","curator_name":"Mainak Guharoy","reference_id":"28334932","version":2,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T17:25:58.198Z","curator_name":"Bálint Mészáros"},"region_id":"DP01289r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP01289r004","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T10:00:26.616Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":36,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":1,"version":3,"statement":[{"text":"Several lines of evidence suggest that the VcHigA2 N-terminal region (residues 1–36), which was not observed in the crystal structure of the free antitoxin, is intrinsically disordered in solution.","type":"Results"}],"term_name":"disorder","reference_html":"Ribosome-dependent Vibrio cholerae mRNAse HigB2 is regulated by a β-strand sliding mechanism. <i> Hadži S, Garcia-Pino A, Haesaerts S, Jurenas D, Gerdes K, Lah J, Loris R. </i> Nucleic Acids Res, 2017","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"28334932","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5J9I"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"rpancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":33,"region_id":"DP01289r006","reference_html":"Ribosome-dependent Vibrio cholerae mRNAse HigB2 is regulated by a β-strand sliding mechanism. <i> Hadži S, Garcia-Pino A, Haesaerts S, Jurenas D, Gerdes K, Lah J, Loris R. </i> Nucleic Acids Res, 2017","ec_id":"ECO:0006204","version":3,"term_id":"IDPO:0000002","curator_id":"rpancsa","start":3,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"The CD spectrum of a peptide encompassing residues Asn3 to Asn33 is typical for a random coil polypeptide with a minimum below 200 nm and a very weak ellipticity above 210 nm.","type":"Results"}],"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T17:23:11.186Z","curator_name":"Bálint Mészáros"},"released":"2022_03","reference_id":"28334932","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP01289r007","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T17:28:49.634Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":22,"term_id":"GO:0097351","start":3,"version":3,"statement":[{"text":"The minimal element for toxin inhibition is the VcHigA2 peptide encompassing residues Asn3-Glu22, which corresponds to the segment that folds into an α-helix upon toxin binding (see below). Using an in vitro ribosome binding assay we also observe that the VcHigA23-22 peptide prevents VcHigB2 binding to the ribosomes (Figure ​(Figure3B).3B). Thus the intrinsically disordered N-terminal domain is sufficient for VcHigB2 toxin regulation.","type":"Results"}],"term_name":"toxin sequestering activity","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"28334932","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5JAA"}],"term_namespace":"Molecular function","ec_id":"ECO:0006218","curator_id":"rpancsa","reference_html":"Ribosome-dependent Vibrio cholerae mRNAse HigB2 is regulated by a β-strand sliding mechanism. <i> Hadži S, Garcia-Pino A, Haesaerts S, Jurenas D, Gerdes K, Lah J, Loris R. </i> Nucleic Acids Res, 2017","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a toxic protein, disabling its function. There may be more than one antitoxin to a toxic protein. Instances of this activity are known only in prokaryotes, where the toxic protein may be a ribonuclease, a DNA gyrase, or other.\" [GOC:rs, PMID:19143615, PMID:19325885, PMID:21819231, PMID:22545240, PMID:24806488, Wikipedia:Toxin-antitoxin_system#Type_II]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01289r008","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T17:28:05.205Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":36,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"The dissociation constant of the VcHigB2–VcHigA2 complex is 50 pM.","type":"Results"},{"text":"The negative enthalpy change likely originates from the folding of the N-terminal domain (in particular the formation of an α-helix) and from specific interactions between VcHigB2 and VcHigA2.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9KMA6","partner_end":null}],"term_name":"protein binding","ec_name":"isothermal titration calorimetry evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"28334932","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"rpancsa","reference_html":"Ribosome-dependent Vibrio cholerae mRNAse HigB2 is regulated by a β-strand sliding mechanism. <i> Hadži S, Garcia-Pino A, Haesaerts S, Jurenas D, Gerdes K, Lah J, Loris R. </i> Nucleic Acids Res, 2017","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01289r009","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T10:00:53.188Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":36,"term_id":"IDPO:0000011","start":3,"version":2,"statement":[{"text":"The N-terminal region of VcHigA2 folds into an N-terminal α-helix (residues 3–22) followed by a short β-strand (residues 28–37).","type":"Results"}],"term_name":"disorder to order","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"28334932","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5JAA"}],"term_namespace":"Structural transition","ec_id":"ECO:0005670","curator_id":"rpancsa","reference_html":"Ribosome-dependent Vibrio cholerae mRNAse HigB2 is regulated by a β-strand sliding mechanism. <i> Hadži S, Garcia-Pino A, Haesaerts S, Jurenas D, Gerdes K, Lah J, Loris R. </i> Nucleic Acids Res, 2017","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP01289r010","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T10:01:09.118Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":36,"term_id":"GO:0005515","start":3,"version":3,"statement":[{"text":"The minimal element for toxin inhibition is the VcHigA2 peptide encompassing residues Asn3-Glu22, which corresponds to the segment that folds into an alpha-helix upon toxin binding.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9KMA6","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"28334932","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5JAA"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"rpancsa","reference_html":"Ribosome-dependent Vibrio cholerae mRNAse HigB2 is regulated by a β-strand sliding mechanism. <i> Hadži S, Garcia-Pino A, Haesaerts S, Jurenas D, Gerdes K, Lah J, Loris R. </i> Nucleic Acids Res, 2017","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q9KMA5","date":"2018-07-04T20:58:29.000Z","acc":"Q9KMA5","name":"Antitoxin HigA-2","length":104,"organism":"Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)","UniParc":"UPI00000C3536","genes":[{"name":{"value":"higA-2"},"olnNames":[{"value":"VC_A0469"}]}],"alphafold_very_low_content":0,"disorder_content":0.34615384615384615,"disprot_consensus":{"full":[{"start":1,"end":36,"type":"T"}],"Structural state":[{"start":1,"end":36,"type":"D"}],"Structural transition":[{"start":1,"end":36,"type":"T"}],"Molecular function":[{"start":1,"end":36,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04014","name":"Antidote-toxin recognition MazE, bacterial antitoxin","start":6,"end":51}],"gene3D":[{"start":1,"end":82,"id":"2.10.260.10","name":"2.10.260.10"}]},"uniref50":"UniRef50_P0AE73","sequence":"MIHSSVKRWGNSPAVRIPATLMQALNLNIDDEVKIDLVDGKLIIEPVRKEPVFTLAELVNDITPENLHENIDWGEPKDKEVW","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0AE73","disprot_id":"DP01291","dataset":["Unicellular toxins and antitoxins"],"ncbi_taxon_id":83333,"regions_counter":16,"creator":"mguha","regions":[{"region_id":"DP01291r001","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T10:17:01.232Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":82,"term_id":"IDPO:0000002","start":48,"version":3,"statement":[{"text":"MazE  is  an  82-amino  acid  protein  (98amino acids in the used His-tagged construct), but in our crystal structure only 44 residues located in the N-terminal half of the sequence are found ordered. SDS-gel analysis of redissolved crystals nevertheless indicated that in the crystal the protein is intact. Lack of structure of the C-terminal half is thus not a consequence  of  proteolytic  degradation  of  the  sample.  This makes  MazE  a  member  of  the  growing  class  of  intrinsicallyunstructured  proteins  that  become  structured  upon  binding their natural partners. ","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12743116","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1MVF"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Crystal structure of the intrinsically flexible addiction antidote MazE. <i> Loris R, Marianovsky I, Lah J, Laeremans T, Engelberg-Kulka H, Glaser G, Muyldermans S, Wyns L. </i> J Biol Chem, 2003","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP01291r002","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T10:22:12.120Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":82,"term_id":"IDPO:0000002","start":51,"version":4,"statement":[{"text":"Information about the dynamical behavior of both full-length and truncated EcMazEs in their free form was obtained by measuring {1H}-15N steady state NOEs (Supplementary Figure S2). Small and negative {1H}-15N NOEs are indicative of higher flexibility and they are observed mainly for the N-terminal residues (His-tag) and in the disordered C-terminal domain, in agreement with the lack of density in the crystal for the C-terminal tails of full-length EcMazE. Moreover, lack of chemical shift dispersion and high intensity peaks of the C-terminal domain in full-length EcMazE (Figure ​(Figure1B,1B, inset) confirms the high flexibility of this region.","type":"Results"},{"text":"Multiple complementary techniques including\nNMR, SAXS and ITC show that the long intrinsically\ndisordered C-termini in MazE, required for MazF neutralization, does not affect the interactions between\nthe antitoxin and its operator. Rather, the MazE Cterminus plays an important role in the MazF binding,\nwhich was found to increase the MazE affinity for the\npalindromic single site operator","type":"Abstract"},{"text":"Structures 2MRU and 2MRN are of the MazE 1-50 structured region in isolation and bound to DNA, and were used to derive the disordered state of the C terminal tail in the NMR and SAXS experiments","type":"Curator statement"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"25564525","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"25093"},{"db":"PDB","id":"2MRU"},{"db":"PDB","id":"2MRN"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"lchemes","reference_html":"Escherichia coli antitoxin MazE as transcription factor: insights into MazE-DNA binding. <i> Zorzini V, Buts L, Schrank E, Sterckx YG, Respondek M, Engelberg-Kulka H, Loris R, Zangger K, van Nuland NA. </i> Nucleic Acids Res, 2015","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":82,"region_id":"DP01291r003","start":51,"ec_id":"ECO:0006210","curator_orcid":"0000-0003-0192-9906","statement":[{"text":"The major source of variability required for a good agreement with the SAXS data is likely attributed to the flexible C-terminus.","type":"Results"},{"text":"None of the two normalized Kratky return to zero, indicating the presence of highly flexible regions in the scattering particle mainly due to the His-tag in both complexes and increased flexibility is even more present in the full-length EcMazE–DNA ‘a’ complex due to the extended disordered C-terminal tails, missing in the EcMazE1–50–DNA ‘a’ complex.","type":"Results"},{"text":"We determined an accurate structural model of the EcMazE–DNA complex using a combination of NMR and SAXS. This structure is in agreement with previous mutagenesis data and confirms that the C-terminal tail of EcMazE remains disordered and is not directly involved in DNA-binding upon interaction between the N-terminal EcMazE domain with DNA.","type":"Discussion"},{"text":"Complementary to validating our NMR EcMazE1–50-DNA structure, we aimed to investigate the structural dynamics of the DNA-binding domain and the extended toxin-neutralizing domain in the full-length protein (...) Furthermore, a comparison between the normalized Kratky plots of both EcMazE–DNA complexes (Figure\n7D) reveals that the EcMazE1–50-DNA shows diminished internal flexibility compared to full-length EcMazE-DNA. This is in perfect agreement with our NMR relaxation data (Supplementary Figure S2), and can be explained by the absence of the long disordered C-terminal tail in the truncated EcMazE1–50.(....) None of the two normalized Kratky return to zero, indicating the presence of highly flexible regions in the scattering particle mainly due to the His-tag in both complexes and increased flexibility is even more present in the full-length EcMazE–DNA ‘a’ complex due to the extended disordered C-terminal tails, missing in the EcMazE1–50– DNA ‘a’ complex","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"25564525","version":4,"reference_html":"Escherichia coli antitoxin MazE as transcription factor: insights into MazE-DNA binding. <i> Zorzini V, Buts L, Schrank E, Sterckx YG, Respondek M, Engelberg-Kulka H, Loris R, Zangger K, van Nuland NA. </i> Nucleic Acids Res, 2015","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T10:22:32.633Z","curator_name":"Bálint Mészáros"},"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP01291r005","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T13:20:12.991Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":76,"term_id":"IDPO:0000011","start":48,"version":2,"statement":[{"text":"The C-terminal region, unstructured in the free form of MazE, becomes structured in complex with toxin MazF.","type":"Curator statement"},{"text":"Interactions between MazE and MazF are primarily mediated by the C \nterminus of MazE, which wraps around the MazF homodimer crossing the edge of the MazF dimer interface and draping primarily over the medial MazF protomer (Figure 2).","type":"Results"}],"term_name":"disorder to order","ec_name":"x-ray crystallography evidence used in manual assertion","reference_html":"Crystal structure of the MazE/MazF complex: molecular bases of antidote-toxin recognition. <i> Kamada K, Hanaoka F, Burley SK. </i> Mol Cell, 2003","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12718874","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1UB4"}],"term_namespace":"Structural transition","ec_id":"ECO:0005670","curator_id":"fquaglia","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP01291r007","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:52:29.421Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":76,"term_id":"GO:0005515","start":48,"version":3,"statement":[{"text":"MazE (antidote) and MazF (toxin) form a linear heterohexamer composed of alternating toxin and antidote homodimers (MazF(2)-MazE(2)-MazF(2)). The MazE homodimer contains a beta barrel from which two extended C termini project, making interactions with flanking MazF homodimers that resemble the plasmid-encoded toxins CcdB and Kid. The MazE/MazF heterohexamer structure documents that the mechanism of antidote-toxin recognition is common to both chromosomal and plasmid-borne addiction modules, and provides general molecular insights into toxin function, antidote degradation in the absence of toxin, and promoter DNA binding by antidote/toxin complexes.","type":"Abstract"},{"text":"Numerous van der Waals, polar, and salt-bridge interactions among conserved residues stabilize the conformation of residues 68–76 of MazE as it meanders across the basic underside of the MazF homodimer (Figure 5A).","type":"Results"},{"text":"Site 2 is almost exclusively hydrophobic in nature and represents the most extensive contact interface between MazE and MazF (buried solvent accessible surface area = 1170 Å2, Figure 5B). Residues 54–67 of MazE and three segments of the MazF polypeptide chain support interactions within site 2, including the S3-S4 loop, α helix H1# (# denotes the lateral MazF protomer), and the C terminus of α helix H3 (Figure 1B).","type":"Results"},{"text":"Site 3 interactions between MazE and MazF bury approximately 410 Å2 of solvent-accessible surface areas, and involve residues 48–53 of MazE plus the medial monomer of MazF. Within the site 3 segment of MazE (residues 51–54), Pro 51 and a conserved aromatic residue (Phe53) make van der Waals interactions with α helix H3 (residues Gln100, Leu101, and Ala104) of the medial MazF protomer as the polypeptide chain of the antidote meanders across the hydrophobic surface of the toxin homodimer Figure 4, Figure 5.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P0AE70","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","reference_html":"Crystal structure of the MazE/MazF complex: molecular bases of antidote-toxin recognition. <i> Kamada K, Hanaoka F, Burley SK. </i> Mol Cell, 2003","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"12718874","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1UB4"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"fquaglia","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01291r012","ec_ontology":"ECO","end":82,"term_id":"GO:0003677","start":51,"version":5,"statement":[{"text":"However, addition of a variable amount of EcMazF to a lower concentration of EcMazE (1 μM), which is not sufficient to cause a shift of the DNA band by itself, results in an increase in affinity for EcMazE to DNA (Figure ​3B). At very high EcMazF:EcMazE ratios, this effect is abolished and coincides with a reduced shift of the band corresponding to the complex. Thus, EcMazF enhances the binding of EcMazE to their DNA operator fragment ‘a’ though its interaction with the C-terminal region of EcMazE.","type":"Results"},{"text":"Superposition of our EcMazE–DNA complex on the crystal structure of the EcMazE–EcMazF complex (32) (Supplementary Figure S8C) indicates additional protein–DNA interaction via the flanking basic regions of the EcMazF homodimer. This favors a model where the enhancement in DNA binding by EcMazF is caused by co-operative binding of the antitoxin and toxin to the DNA instead of an allosteric effect.","type":"Discussion"}],"term_name":"DNA binding","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","curator_orcid":"0000-0001-8399-7907","released":"2024_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"25564525","date":"2024-05-16T17:46:14.192Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001807","curator_id":"vnugnes","reference_html":"Escherichia coli antitoxin MazE as transcription factor: insights into MazE-DNA binding. <i> Zorzini V, Buts L, Schrank E, Sterckx YG, Respondek M, Engelberg-Kulka H, Loris R, Zangger K, van Nuland NA. </i> Nucleic Acids Res, 2015","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01291r013","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T10:56:48.265Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":82,"term_id":"IDPO:0000011","start":68,"version":2,"statement":[{"text":"Central in this regulation is an EcMazE-induced double conformational change as follows: a rearrangement of a crucial active site loop and a relative rotation of the two monomers in the EcMazF dimer. Both are induced by the C-terminal residues Asp-78–Trp-82 of EcMazE, which are also responsible for strong negative cooperativity in EcMazE-EcMazF binding","type":"Abstract"},{"text":"To investigate the interaction between EcMazF and residues Asp-78–Trp-82 of EcMazE, we determined the crystal structure of EcMazFE24A in complex with EcMazE(68– 82). In our structures, Pro-76–Trp-82 forms a -hairpin, the presence of which prevents loop 1-2 of both EcMazF monomers to adopt the catalytically competent conformation and simultaneously blocks both substrate-binding sites on the EcMazF dimer\n","type":"Results"}],"term_name":"disorder to order","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"27026704","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5CQY"},{"db":"PDB","id":"5CQX"}],"term_namespace":"Structural transition","ec_id":"ECO:0005670","curator_id":"lchemes","reference_html":"Substrate Recognition and Activity Regulation of the Escherichia coli mRNA Endonuclease MazF. <i> Zorzini V, Mernik A, Lah J, Sterckx YG, De Jonge N, Garcia-Pino A, De Greve H, Versées W, Loris R. </i> J Biol Chem, 2016","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP01291r014","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T10:57:17.609Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":82,"term_id":"GO:0005515","start":68,"version":3,"statement":[{"text":"Central in this regulation is an EcMazE-induced double conformational change as follows: a rearrangement of a crucial active site loop and a relative rotation of the two monomers in the EcMazF dimer. Both are induced by the C-terminal residues Asp-78–Trp-82 of EcMazE, which are also responsible for strong negative cooperativity in EcMazE-EcMazF binding","type":"Abstract"},{"text":"To investigate the interaction between EcMazF and residues Asp-78–Trp-82 of EcMazE, we determined the crystal structure of EcMazFE24A in complex with EcMazE(68– 82). In our structures, Pro-76–Trp-82 forms a -hairpin, the presence of which prevents loop 1-2 of both EcMazF monomers to adopt the catalytically competent conformation and simultaneously blocks both substrate-binding sites on the EcMazF dimer\n","type":"Results"}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"27026704","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5CQY"},{"db":"PDB","id":"5CQX"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"lchemes","reference_html":"Substrate Recognition and Activity Regulation of the Escherichia coli mRNA Endonuclease MazF. <i> Zorzini V, Mernik A, Lah J, Sterckx YG, De Jonge N, Garcia-Pino A, De Greve H, Versées W, Loris R. </i> J Biol Chem, 2016","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01291r015","validated":{"curator_id":"bmesza","timestamp":"2020-12-09T10:57:43.943Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":82,"term_id":"GO:0097351","start":68,"version":3,"statement":[{"text":"Central in this regulation is an EcMazE-induced double conformational change as follows: a rearrangement of a crucial active site loop and a relative rotation of the two monomers in the EcMazF dimer. Both are induced by the C-terminal residues Asp-78–Trp-82 of EcMazE, which are also responsible for strong negative cooperativity in EcMazE-EcMazF binding","type":"Abstract"},{"text":"To investigate the interaction between EcMazF and residues Asp-78–Trp-82 of EcMazE, we determined the crystal structure of EcMazFE24A in complex with EcMazE(68– 82). In our structures, Pro-76–Trp-82 forms a -hairpin, the presence of which prevents loop 1-2 of both EcMazF monomers to adopt the catalytically competent conformation and simultaneously blocks both substrate-binding sites on the EcMazF dimer\n","type":"Results"}],"term_name":"toxin sequestering activity","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"27026704","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5CQY"},{"db":"PDB","id":"5CQX"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"lchemes","reference_html":"Substrate Recognition and Activity Regulation of the Escherichia coli mRNA Endonuclease MazF. <i> Zorzini V, Mernik A, Lah J, Sterckx YG, De Jonge N, Garcia-Pino A, De Greve H, Versées W, Loris R. </i> J Biol Chem, 2016","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a toxic protein, disabling its function. There may be more than one antitoxin to a toxic protein. Instances of this activity are known only in prokaryotes, where the toxic protein may be a ribonuclease, a DNA gyrase, or other.\" [GOC:rs, PMID:19143615, PMID:19325885, PMID:21819231, PMID:22545240, PMID:24806488, Wikipedia:Toxin-antitoxin_system#Type_II]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01291r016","ec_ontology":"ECO","end":82,"term_id":"GO:0005515","start":50,"version":4,"statement":[{"text":"Central in this regulation is an EcMazE-induced double conformational change as follows: a rearrangement of a crucial active site loop and a relative rotation of the two monomers in the EcMazF dimer. Both are induced by the C-terminal residues Asp-78–Trp-82 of EcMazE, which are also responsible for strong negative cooperativity in EcMazE-EcMazF binding","type":"Abstract"},{"text":"E24A Mutation Does Not Affect Antitoxin Recognition—We next compared the binding of the intrinsically disordered domain of EcMazE (EcMazE(50– 82)) to EcMazF and EcMazFE24A using ITC (Table 2 and Fig. 6). We find that both EcMazF and EcMazFE24A possess two binding sites for EcMazE(50– 82). Binding is sequential and with strong negative cooperativity. The first EcMazE(50– 82) molecule binds with an affinity around 10 nM, although subsequent binding of the second EcMazE(50– 82) is 3 orders of magnitude weaker. This cooperativity is largely due to the C-terminal EcMazE residues Asp-78–Trp-82 (Table 2 and Fig. 6).","type":"Results"}],"term_name":"protein binding","ec_name":"isothermal titration calorimetry evidence used in manual assertion","curator_orcid":"0000-0002-5152-5953","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"27026704","date":"2022-03-09T08:17:55.047Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"esalladini","reference_html":"Substrate Recognition and Activity Regulation of the Escherichia coli mRNA Endonuclease MazF. <i> Zorzini V, Mernik A, Lah J, Sterckx YG, De Jonge N, Garcia-Pino A, De Greve H, Versées W, Loris R. </i> J Biol Chem, 2016","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P0AE70","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-30T12:55:57.657Z"}}],"released":"2018_11","uniref100":"UniRef100_P0AE73","date":"2018-07-04T21:15:22.000Z","acc":"P0AE72","name":"Antitoxin MazE","length":82,"organism":"Escherichia coli (strain K12)","UniParc":"UPI00001278B4","genes":[{"name":{"value":"mazE"},"synonyms":[{"value":"chpAI"},{"value":"chpR"}],"olnNames":[{"value":"b2783"},{"value":"JW2754"}]}],"alphafold_very_low_content":0,"disorder_content":0.4268292682926829,"disprot_consensus":{"full":[{"start":48,"end":82,"type":"T"}],"Structural state":[{"start":48,"end":82,"type":"D"}],"Structural transition":[{"start":48,"end":82,"type":"T"}],"Molecular function":[{"start":48,"end":82,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01080","name":"Presenilin","start":76,"end":457}],"gene3D":[{"start":354,"end":459,"id":"1.10.472.100","name":"Presenilin"}]},"uniref50":"UniRef50_P49768","sequence":"MTELPAPLSYFQNAQMSEDNHLSNTVRSQNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFIYLGEVFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAESTERESQDTVAENDDGGFSEEWEAQRDSHLGPHRSTPESRAAVQELSSSILAGEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDYLVQPFMDQLAFHQFYI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P49768","disprot_id":"DP01292","ncbi_taxon_id":9606,"regions_counter":2,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":77,"region_id":"DP01292r001","released":"2023_12","ec_id":"ECO:0006224","reference_html":"An atomic structure of human γ-secretase. <i> Bai XC, Yan C, Yang G, Lu P, Ma D, Sun L, Zhou R, Scheres SHW, Shi Y. </i> Nature, 2015","statement":[{"text":"The N-terminal 77 residues have no EM density and are presumably disordered, likely due to their intrinsic flexibility.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-28T14:42:49.974Z","reference_source":"pmid","term_name":"disorder","reference_id":"26280335","ec_go":"IDA","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NZ42"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q96BI3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92542"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5287971"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"}],"cross_refs":[{"db":"EMDB","id":"3061"},{"db":"PDB","id":"5A63"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":378,"region_id":"DP01292r002","released":"2023_12","ec_id":"ECO:0006224","reference_html":"An atomic structure of human γ-secretase. <i> Bai XC, Yan C, Yang G, Lu P, Ma D, Sun L, Zhou R, Scheres SHW, Shi Y. </i> Nature, 2015","statement":[{"text":"The extended sequences between TM6 and TM7 harbor the site of autocatalytic cleavage; but these sequences are hydrophilic and mostly disordered (Fig. 2b).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":262,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-28T14:42:37.507Z","reference_source":"pmid","term_name":"disorder","reference_id":"26280335","ec_go":"IDA","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"5A63"},{"db":"EMDB","id":"3061"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92542"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q96BI3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NZ42"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5287971"}]}],"released":"2018_11","uniref100":"UniRef100_P49768","date":"2018-07-05T06:31:44.000Z","acc":"P49768","name":"Presenilin-1","length":467,"organism":"Homo sapiens","dataset":["Age-related disorders proteins"],"UniParc":"UPI000003F05F","genes":[{"name":{"value":"PSEN1"},"synonyms":[{"value":"AD3"},{"value":"PS1"},{"value":"PSNL1"}]}],"alphafold_very_low_content":0.2633832976445396,"disorder_content":0.41541755888650966,"disprot_consensus":{"full":[{"start":1,"end":77,"type":"D"},{"start":262,"end":378,"type":"D"}],"Structural state":[{"start":1,"end":77,"type":"D"},{"start":262,"end":378,"type":"D"}]}},{"acc":"Q13542","sequence":"MSSSAGSGHQPSQSRAIPTRTVAISDAAQLPHDYCTTPGGTLFSTTPGGTRIIYDRKFLLDRRNSPMAQTPPCHLPNIPGVTSPGTLIEDSKVEVNNLNNLNNHDRKHAVGDDAQFEMDI","alphafold_very_low_content":"0.18333333333333332","creator":"gminervini","dataset":[],"date":"2018-07-05T08:01:34.000Z","disprot_id":"DP01293","features":{"pfam":[{"id":"PF05456","name":"Eukaryotic translation initiation factor 4E binding protein (EIF4EBP)","start":7,"end":120}]},"genes":[{"name":{"value":"EIF4EBP2","evidences":[{"source":{"id":"HGNC:3289","name":"HGNC","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:3289","_id":"685af523b4ac24d5329d8f75"},"code":"ECO:0000312","_id":"685af523b4ac24d5329d8f74"}],"_id":"685af523b4ac24d5329d8f76"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d8f73"}],"length":120,"name":"Eukaryotic translation initiation factor 4E-binding protein 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":8,"released":"2018_11","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000073D8C","uniref100":"UniRef100_Q13542","uniref50":"UniRef50_Q13542","uniref90":"UniRef90_Q13542","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":120,"interaction_partner":[],"reference_html":"Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch. <i> Bah A, Vernon RM, Siddiqui Z, Krzeminski M, Muhandiram R, Zhao C, Sonenberg N, Kay LE, Forman-Kay JD. </i> Nature, 2015","reference_id":"25533957","region_id":"DP01293r001","released":"2022_03","sample":[],"statement":[{"type":"Title","text":"Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch","_id":"685af523b4ac24d5329d8f49"},{"type":"Article","text":"IDPs such as non-phosphorylated 4E-BP2 have intense peaks with narrow 1HN chemical shift dispersion26.","_id":"685af523b4ac24d5329d8f4a"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-12-07T13:51:20.121Z","_id":"685af523b4ac24d5329d8f4b"},"version":3,"_id":"685af523b4ac24d5329d8f48","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"IntAct","id":"EBI-16080855","_id":"685af523b4ac24d5329d8f51"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":120,"interaction_partner":[{"db":"UniProt","id":"P06730","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8f52"}],"reference_html":"Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch. <i> Bah A, Vernon RM, Siddiqui Z, Krzeminski M, Muhandiram R, Zhao C, Sonenberg N, Kay LE, Forman-Kay JD. </i> Nature, 2015","reference_id":"25533957","region_id":"DP01293r003","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Here we show that multisite phosphorylation induces folding of the intrinsically disordered 4E-BP2, the major neural isoform of the family of three mammalian proteins that bind eIF4E and suppress cap-dependent translation initiation.","_id":"685af523b4ac24d5329d8f50"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-12-07T13:51:35.933Z","_id":"685af523b4ac24d5329d8f53"},"version":4,"_id":"685af523b4ac24d5329d8f4f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":18,"end":62,"interaction_partner":[],"reference_html":"Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch. <i> Bah A, Vernon RM, Siddiqui Z, Krzeminski M, Muhandiram R, Zhao C, Sonenberg N, Kay LE, Forman-Kay JD. </i> Nature, 2015","reference_id":"25533957","region_id":"DP01293r005","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"We demonstrate that phosphorylation at T37 and T46 induces folding of residues P18–R62 of 4E-BP2 into a four-stranded β-domain that sequesters the helical YXXXXLΦ motif into a partly buried β-strand, blocking its accessibility to eIF4E","_id":"685af523b4ac24d5329d8f5e"}],"states_connection":[],"term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-12-07T13:51:43.416Z","_id":"685af523b4ac24d5329d8f5f"},"version":3,"_id":"685af523b4ac24d5329d8f5d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":18,"end":62,"interaction_partner":[],"reference_html":"Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch. <i> Bah A, Vernon RM, Siddiqui Z, Krzeminski M, Muhandiram R, Zhao C, Sonenberg N, Kay LE, Forman-Kay JD. </i> Nature, 2015","reference_id":"25533957","region_id":"DP01293r006","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"We demonstrate that phosphorylation at T37 and T46 induces folding of residues P18–R62 of 4E-BP2 into a four-stranded β-domain that sequesters the helical YXXXXLΦ motif into a partly buried β-strand, blocking its accessibility to eIF4E.","_id":"685af523b4ac24d5329d8f61"},{"type":"Article","text":"Unlike other IDPs for which phosphorylation only causes downfield chemical shifts of phosphorylated residues27, 4E-BP2 phosphorylation induces widespread downfield and upfield chemical shifts for residues spanning T19–R62, suggesting folding upon phosphorylation (Fig. 1b).","_id":"685af523b4ac24d5329d8f62"}],"states_connection":[{"source":"DP01293r001","target":"DP01293r007","_id":"685af523b4ac24d5329d8f63"}],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-12-07T13:51:25.535Z","_id":"685af523b4ac24d5329d8f64"},"version":3,"_id":"685af523b4ac24d5329d8f60","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":37,"end":37,"statements":[],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d8f66"},{"start":46,"end":46,"statements":[],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d8f67"},{"start":65,"end":65,"statements":[],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d8f68"},{"start":70,"end":70,"statements":[],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d8f69"},{"start":83,"end":83,"statements":[],"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","_id":"685af523b4ac24d5329d8f6a"}],"cross_refs":[{"db":"PDB","id":"2MX4","_id":"685af523b4ac24d5329d8f6b"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":18,"end":62,"interaction_partner":[],"reference_html":"Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch. <i> Bah A, Vernon RM, Siddiqui Z, Krzeminski M, Muhandiram R, Zhao C, Sonenberg N, Kay LE, Forman-Kay JD. </i> Nature, 2015","reference_id":"25533957","region_id":"DP01293r007","released":"2022_03","sample":[],"sequence_construct":"MSSSAGSGHQPSQSRAIPTRTVAISDAAQLPHDYCTTPGGTLFSTTPGGTRIIYDRKFLLDRRNSPMAQTPPCHLPNIPGVTSPGTLIEDSKVEVNNLNNLNNHDRKHAVGDDAQFEMDI","statement":[{"type":"Article","text":"Unlike other IDPs for which phosphorylation only causes downfield chemical shifts of phosphorylated residues27, 4E-BP2 phosphorylation induces widespread downfield and upfield chemical shifts for residues spanning T19–R62, suggesting folding upon phosphorylation (Fig. 1b).","_id":"685af523b4ac24d5329d8f6c"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-12-07T13:51:24.412Z","_id":"685af523b4ac24d5329d8f6d"},"version":1,"_id":"685af523b4ac24d5329d8f65","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005647","ec_name":"isothermal titration calorimetry evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":120,"interaction_partner":[{"db":"UniProt","id":"P06730","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8f6f"}],"reference_html":"Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch. <i> Bah A, Vernon RM, Siddiqui Z, Krzeminski M, Muhandiram R, Zhao C, Sonenberg N, Kay LE, Forman-Kay JD. </i> Nature, 2015","reference_id":"25533957","region_id":"DP01293r008","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":" In its non-phosphorylated state, 4E-BP2 interacts tightly with eIF4E using both a canonical YXXXXLW motif (starting at Y54) that undergoes a disorder-to-helix transition upon binding and a dyna- mic secondary binding site7–11.","_id":"685af523b4ac24d5329d8f70"},{"type":"Article","text":"ITC (Extended Data Table 2 and Extended Data Fig. 7) and NMR data were obtained on 4E-BP2 variants to probe the role of electrostatics in folding and reducing eIF4E affinity.","_id":"685af523b4ac24d5329d8f71"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-12-07T13:51:40.969Z","_id":"685af523b4ac24d5329d8f72"},"version":1,"_id":"685af523b4ac24d5329d8f6e","reference_source":"pmid"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":17,"type":"D"},{"start":18,"end":62,"type":"T"},{"start":63,"end":120,"type":"D"}],"Structural state":[{"start":1,"end":120,"type":"D"}],"Molecular function":[{"start":1,"end":120,"type":"F"}],"Disorder function":[{"start":18,"end":62,"type":"F"}],"Structural transition":[{"start":18,"end":62,"type":"T"}]}},{"acc":"Q98XH7","sequence":"MEPVDPKLEPWKHPGSQPKTACNNCYCKRCCLHCQVCFMTKGLGIYYGRKKRRQRRRASQDRQTHQDSLSEQ","creator":"jbergier","dataset":["Viral proteins","RNA-binding proteins"],"date":"2018-07-05T08:23:22.000Z","disprot_id":"DP01295","features":{"pfam":[{"id":"PF00539","name":"Transactivating regulatory protein (Tat)","start":2,"end":64}],"gene3D":[{"start":1,"end":72,"id":"4.10.20.10","name":"Tat domain","_id":"685af523b4ac24d5329d8f78"}]},"genes":[{"name":{"value":"tat","evidences":[{"source":{"id":"AAG32882.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/AAG32882.1","_id":"685af523b4ac24d5329d8f96"},"code":"ECO:0000313","_id":"685af523b4ac24d5329d8f95"}],"_id":"685af523b4ac24d5329d8f97"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d8f94"}],"length":72,"name":"Protein Tat","ncbi_taxon_id":11676,"organism":"Human immunodeficiency virus 1","regions_counter":8,"released":"2018_11","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"UniParc":"UPI0000103A33","uniref100":"UniRef100_Q98XH7","uniref50":"UniRef50_H9CD48","uniref90":"UniRef90_Q98XH7","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3O6M","_id":"685af523b4ac24d5329d8f7f"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":6,"end":14,"interaction_partner":[],"reference_html":"Fab'-induced folding of antigenic N-terminal peptides from intrinsically disordered HIV-1 Tat revealed by X-ray crystallography. <i> Serrière J, Dugua JM, Bossus M, Verrier B, Haser R, Gouet P, Guillon C. </i> J Mol Biol, 2011","reference_id":"21035463","region_id":"DP01295r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"2Fo − Fc and Fo − Fc difference electron density maps showed that Tat-1 and Tat-3 peptides were well lodged in the antigen-binding site of Fab′ (Fig. 2c).","_id":"685af523b4ac24d5329d8f80"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T14:21:02.981Z","_id":"685af523b4ac24d5329d8f81"},"version":1,"_id":"685af523b4ac24d5329d8f7e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3O6L","_id":"685af523b4ac24d5329d8f83"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":16,"interaction_partner":[],"reference_html":"Fab'-induced folding of antigenic N-terminal peptides from intrinsically disordered HIV-1 Tat revealed by X-ray crystallography. <i> Serrière J, Dugua JM, Bossus M, Verrier B, Haser R, Gouet P, Guillon C. </i> J Mol Biol, 2011","reference_id":"21035463","region_id":"DP01295r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"2Fo − Fc and Fo − Fc difference electron density maps showed that Tat-1 and Tat-3 peptides were well lodged in the antigen-binding site of Fab′ (Fig. 2c).","_id":"685af523b4ac24d5329d8f84"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T14:20:56.546Z","_id":"685af523b4ac24d5329d8f85"},"version":1,"_id":"685af523b4ac24d5329d8f82","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005581","ec_name":"enzyme-linked immunoabsorbent assay evidence used in manual assertion","ec_ontology":"ECO","start":6,"end":14,"interaction_partner":[],"reference_html":"Fab'-induced folding of antigenic N-terminal peptides from intrinsically disordered HIV-1 Tat revealed by X-ray crystallography. <i> Serrière J, Dugua JM, Bossus M, Verrier B, Haser R, Gouet P, Guillon C. </i> J Mol Biol, 2011","reference_id":"21035463","region_id":"DP01295r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Thus, mAb 11H6H1 recognizes the full-length active Tat and the smaller 15-mer peptide (Tat-1) and 9-mer minimal epitope (Tat-3) with similar affinities, suggesting that the antibody/peptide interaction is close to that observed with the full-length protein. Moreover, the fact that the 9-mer peptide is recognized with the same affinity as the 15-mer peptide suggests that it indeed contains all the residues necessary for the recognition of Tat by 11H6H1. ","_id":"685af523b4ac24d5329d8f87"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T14:20:55.138Z","_id":"685af523b4ac24d5329d8f88"},"version":1,"_id":"685af523b4ac24d5329d8f86","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3O6M","_id":"685af523b4ac24d5329d8f8a"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":6,"end":14,"interaction_partner":[],"reference_html":"Fab'-induced folding of antigenic N-terminal peptides from intrinsically disordered HIV-1 Tat revealed by X-ray crystallography. <i> Serrière J, Dugua JM, Bossus M, Verrier B, Haser R, Gouet P, Guillon C. </i> J Mol Biol, 2011","reference_id":"21035463","region_id":"DP01295r006","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"The crystal structures of this 9-mer peptide and of an overlapping 15-mer peptide were determined in complex with Fab′ 11H6H1 at 2.4 Å and 2.1 Å resolution, respectively.","_id":"685af523b4ac24d5329d8f8b"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T14:21:07.561Z","_id":"685af523b4ac24d5329d8f8c"},"version":1,"_id":"685af523b4ac24d5329d8f89","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3O6L","_id":"685af523b4ac24d5329d8f8e"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005581","ec_name":"enzyme-linked immunoabsorbent assay evidence used in manual assertion","ec_ontology":"ECO","start":2,"end":16,"interaction_partner":[],"reference_html":"Fab'-induced folding of antigenic N-terminal peptides from intrinsically disordered HIV-1 Tat revealed by X-ray crystallography. <i> Serrière J, Dugua JM, Bossus M, Verrier B, Haser R, Gouet P, Guillon C. </i> J Mol Biol, 2011","reference_id":"21035463","region_id":"DP01295r007","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"The crystal structures of this 9-mer peptide and of an overlapping 15-mer peptide were determined in complex with Fab′ 11H6H1 at 2.4 Å and 2.1 Å resolution, respectively.","_id":"685af523b4ac24d5329d8f8f"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T14:21:05.551Z","_id":"685af523b4ac24d5329d8f90"},"version":1,"_id":"685af523b4ac24d5329d8f8d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_id":"ECO:0000302","ec_name":"author statement used in manual assertion","ec_ontology":"ECO","start":2,"end":16,"interaction_partner":[],"reference_html":"Fab'-induced folding of antigenic N-terminal peptides from intrinsically disordered HIV-1 Tat revealed by X-ray crystallography. <i> Serrière J, Dugua JM, Bossus M, Verrier B, Haser R, Gouet P, Guillon C. </i> J Mol Biol, 2011","reference_id":"21035463","region_id":"DP01295r008","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"Although early NMR structural studies of Tat suggested that Tat was a globular protein devoid of secondary structural elements,19, 20, 21, 22 recent publications have demonstrated that Tat is in fact an intrinsically disordered protein in solution that is able to bind a wide variety of structurally distinct cellular and/or viral biological partners responsible for several biological functions.23, 24 This was further demonstrated by a recent crystallographic study of Tat in complex with the nuclear transcription factor p-TEFb, in which Tat appears elongated, except for short helices around its cysteine-rich domain.","_id":"685af523b4ac24d5329d8f92"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T14:20:52.815Z","_id":"685af523b4ac24d5329d8f93"},"version":1,"_id":"685af523b4ac24d5329d8f91","reference_source":"pmid"}],"__v":0,"disorder_content":0.20833333333333334,"disprot_consensus":{"full":[{"start":2,"end":16,"type":"D"}],"Structural state":[{"start":2,"end":16,"type":"D"}],"Molecular function":[{"start":2,"end":16,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02672","name":"CP12 domain","start":4,"end":74}]},"uniref50":"UniRef50_Q6BBK3","sequence":"MSDIQEKIEQARQEAHAISEEKGATSPDAAAAWDAVEELQAEAAHQRQQKSETEPFFGDYCSENPDAAECLIYDD","taxonomy":["Bacteria","Cyanobacteria","Synechococcales","Synechococcaceae","Synechococcus"],"uniref90":"UniRef90_Q6BBK3","disprot_id":"DP01296","ncbi_taxon_id":1140,"regions_counter":3,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":52,"region_id":"DP01296r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure basis for the regulation of glyceraldehyde-3-phosphate dehydrogenase activity via the intrinsically disordered protein CP12. <i> Matsumura H, Kai A, Maeda T, Tamoi M, Satoh A, Tamura H, Hirose M, Ogawa T, Kizu N, Wadano A, Inoue T, Shigeoka S. </i> Structure, 2011","statement":[{"text":"Mass spectroscopy of dissolved crystals confirmed that only the full-length CP12 is contained in the crystals (H.M. and A.K., unpublished observation); therefore, the N-terminal region is largely disordered in the crystal","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"gminervini","start":1,"term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"22153507","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":52,"term_name":"disorder to order","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"gminervini","released":"2022_03","term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"22153507","version":2,"reference_html":"Structure basis for the regulation of glyceraldehyde-3-phosphate dehydrogenase activity via the intrinsically disordered protein CP12. <i> Matsumura H, Kai A, Maeda T, Tamoi M, Satoh A, Tamura H, Hirose M, Ogawa T, Kizu N, Wadano A, Inoue T, Shigeoka S. </i> Structure, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP01296r002","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":52,"term_name":"protein binding","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","statement":[{"text":"The GAPDH-CP12 complex structure reveals that the oxidized CP12 becomes partially structured upon GAPDH binding","type":"Abstract"}],"curator_id":"gminervini","released":"2022_03","term_ontology":"GO","curator_name":"Giovanni Minervini","reference_id":"22153507","version":3,"reference_html":"Structure basis for the regulation of glyceraldehyde-3-phosphate dehydrogenase activity via the intrinsically disordered protein CP12. <i> Matsumura H, Kai A, Maeda T, Tamoi M, Satoh A, Tamura H, Hirose M, Ogawa T, Kizu N, Wadano A, Inoue T, Shigeoka S. </i> Structure, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","cross_refs":[{"db":"imex","id":"DIP-59423N"}],"region_id":"DP01296r003","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q6BBK3","date":"2018-07-05T08:35:39.000Z","acc":"Q6BBK3","name":"CP12","length":75,"organism":"Synechococcus elongatus (strain PCC 7942)","dataset":[],"UniParc":"UPI00003A0656","genes":[{"name":{"value":"cp12","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAD34549.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAD34549.1"}}]},"olnNames":[{"value":"Synpcc7942_0361","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ABB56393.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABB56393.1"}}]}]}],"alphafold_very_low_content":0,"disorder_content":0.6933333333333334,"disprot_consensus":{"full":[{"start":1,"end":52,"type":"T"}],"Structural state":[{"start":1,"end":52,"type":"D"}],"Structural transition":[{"start":1,"end":52,"type":"T"}],"Molecular function":[{"start":1,"end":52,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03760","name":"Late embryogenesis abundant (LEA) group 1","start":1,"end":75}]},"uniref50":"UniRef50_Q96273","sequence":"MQSAKEKISDMASTAKEKLNIGGAKAQGHAEKTMARTKKEKKLAQEREKSKEAQAKADLHQSKAEHAADAQVHGHHLPGHSTYPTRATGANYPPGQI","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q96273","disprot_id":"DP01299","ncbi_taxon_id":3702,"regions_counter":4,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":97,"region_id":"DP01299r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The Unstructured N-terminal Region of Arabidopsis Group 4 Late Embryogenesis Abundant (LEA) Proteins Is Required for Folding and for Chaperone-like Activity under Water Deficit. <i> Cuevas-Velazquez CL, Saab-Rincón G, Reyes JL, Covarrubias AA. </i> J Biol Chem, 2016","statement":[{"text":"The results obtained corroborated that both proteins are mostly disordered in solution over a wide range of temperatures (Fig. 2, A and B) and pH (data not shown), with the characteristic negative band for random coil structures around 198 nm.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"gminervini","start":1,"term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"27006402","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-11-25T15:54:58.720Z"}},{"start":1,"end":97,"reference_id":"27006402","reference_source":"pmid","reference_html":"The Unstructured N-terminal Region of Arabidopsis Group 4 Late Embryogenesis Abundant (LEA) Proteins Is Required for Folding and for Chaperone-like Activity under Water Deficit. <i> Cuevas-Velazquez CL, Saab-Rincón G, Reyes JL, Covarrubias AA. </i> J Biol Chem, 2016","date":"2025-11-25T16:22:02.470Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0050821","term_name":"protein stabilization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"IDA","region_id":"DP01299r003","statement":[{"text":"For this purpose, LDH in the presence or absence of AtLEA4-5, AtLEA4-2, AtLEA4-51–77, or AtLEA4-578–158 was subjected to in vitro freeze-thaw cycles and partial dehydration treatments.","type":"Results"},{"text":"AtLEA4-2, the smallest protein of this group, mostly consisting of the N-terminal region (Fig. 1A), showed a similar protective effect on LDH activity as AtLEA4-5 after partial dehydration (Fig. 5A).","type":"Results"}],"term_comment":"","term_def":"\"Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":97,"reference_id":"27006402","reference_source":"pmid","reference_html":"The Unstructured N-terminal Region of Arabidopsis Group 4 Late Embryogenesis Abundant (LEA) Proteins Is Required for Folding and for Chaperone-like Activity under Water Deficit. <i> Cuevas-Velazquez CL, Saab-Rincón G, Reyes JL, Covarrubias AA. </i> J Biol Chem, 2016","date":"2025-11-25T16:23:06.920Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0009631","term_name":"cold acclimation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"IDA","region_id":"DP01299r004","statement":[{"text":"For this purpose, LDH in the presence or absence of AtLEA4-5, AtLEA4-2, AtLEA4-51–77, or AtLEA4-578–158 was subjected to in vitro freeze-thaw cycles and partial dehydration treatments.","type":"Results"},{"text":"AtLEA4-2, the smallest protein of this group, mostly consisting of the N-terminal region (Fig. 1A), showed a similar protective effect on LDH activity as AtLEA4-5 after partial dehydration (Fig. 5A).","type":"Results"}],"term_comment":"","term_def":"\"Any process that increases freezing tolerance of an organism in response to low, nonfreezing temperatures.\" [GOC:syr]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_Q96273","date":"2018-07-05T08:57:03.000Z","acc":"Q96273","name":"Late embryogenesis abundant protein 18","length":97,"organism":"Arabidopsis thaliana","dataset":["Stress response proteins"],"UniParc":"UPI00000AC93B","genes":[{"name":{"value":"LEA18","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"18318901","url":"http://www.ncbi.nlm.nih.gov/pubmed/18318901","alternativeUrl":"https://europepmc.org/abstract/MED/18318901"}}]},"synonyms":[{"value":"LEA4-2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"20668063","url":"http://www.ncbi.nlm.nih.gov/pubmed/20668063","alternativeUrl":"https://europepmc.org/abstract/MED/20668063"}}]}],"olnNames":[{"value":"At2g35300","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT2G35300","url":""}}]}]}],"alphafold_very_low_content":0.16494845360824742,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":97,"type":"D"}],"Structural state":[{"start":1,"end":97,"type":"D"}],"Biological process":[{"start":1,"end":97,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_Q9SLJ2","sequence":"MAGLINKIGDALHIGGGNKEGEHKKEEEHKKHVDEHKSGEHKEGIVDKIKDKIHGGEGKSHDGEGKSHDGEKKKKKDKKEKKHHDDGHHSSSSDSDSD","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q9SLJ2","disprot_id":"DP01300","ncbi_taxon_id":3702,"regions_counter":1,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":98,"region_id":"DP01300r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Biochemical Characterization Of The Arabidopsis Ks-Type Dehydrin Protein, Whose Gene Expression Is Constitutively Abundant Rather Than Stress Dependent <i> Hara, Masakazu; Shinoda, Yuri; Kubo, Masayuki; Kashima, Daiju; Takahashi, Ikuo; Kato, Takanari; Horiike, Tokumasa; Kuboi, Toru <i> Acta Physiologiae Plantarum 2011","statement":[{"text":"the CD analysis indicated that the recombinant AtHIRD11 was disordered because the large negative peak around 200 nm occurred","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"gminervini","start":1,"term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"10.1007/s11738-011-0749-1","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"doi","term_name":"disorder","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9SLJ2","date":"2018-07-05T09:05:36.000Z","acc":"Q9SLJ2","name":"Dehydrin HIRD11","length":98,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI000009F87D","genes":[{"name":{"value":"HIRD11","evidences":[{"code":"ECO:0000303","source":{"name":"Citation","id":"Ref.8","url":"https://www.uniprot.org/uniprot/null#ref8"}}]},"synonyms":[{"value":"SRC1","evidences":[{"code":"ECO:0000305"}]}],"orfNames":[{"value":"F20D21.23","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAD25619.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD25619.1"}}]}],"olnNames":[{"value":"At1g54410","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT1G54410","url":""}}]}]}],"alphafold_very_low_content":0.24489795918367346,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":98,"type":"D"}],"Structural state":[{"start":1,"end":98,"type":"D"}]}},{"features":{"pfam":[{"id":"PF09806","name":"Cyclin-dependent kinase 2-associated protein","start":42,"end":114}]},"uniref50":"UniRef50_O14519","sequence":"MSYKPNLAAHMPAAALNAAGSVHSPSTSMATSSQYRQLLSDYGPPSLGYTQGTGNSQVPQSKYAELLAIIEELGKEIRPTYAGSKSAMERLKRGIIHARGLVRECLAETERNARS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O14519","disprot_id":"DP01303","ncbi_taxon_id":9606,"regions_counter":1,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":60,"region_id":"DP01303r001","released":"2022_03","ec_id":"ECO:0006236","reference_html":"Human cyclin-dependent kinase 2-associated protein 1 (CDK2AP1) is dimeric in its disulfide-reduced state, with natively disordered N-terminal region. <i> Ertekin A, Aramini JM, Rossi P, Leonard PG, Janjua H, Xiao R, Maglaqui M, Lee HW, Prestegard JH, Montelione GT. </i> J Biol Chem, 2012","statement":[{"text":"Full-length CDK2AP1 was analyzed by HDX-MS. The backbone amide groups in the entire N-terminal 60 residues of the protein exhibit rapid HDX rates characteristic of intrinsically disordered polypeptide segments","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"gminervini","start":1,"term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"22427660","version":2,"ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_O14519","date":"2018-07-05T09:26:05.000Z","acc":"O14519","name":"Cyclin-dependent kinase 2-associated protein 1","length":115,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000000164E","genes":[{"name":{"value":"CDK2AP1"},"synonyms":[{"value":"CDKAP1"},{"value":"DOC1"}]}],"alphafold_very_low_content":0.13043478260869565,"disorder_content":0.5217391304347826,"disprot_consensus":{"full":[{"start":1,"end":60,"type":"D"}],"Structural state":[{"start":1,"end":60,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01255","name":"Putative undecaprenyl diphosphate synthase","start":194,"end":296}],"gene3D":[{"start":104,"end":297,"id":"3.40.1180.10","name":"Decaprenyl diphosphate synthase-like"}]},"uniref50":"UniRef50_Q96E22","sequence":"MTGLYELVWRVLHALLCLHLTLTSWLRVRFGTWNWIWRRCCRAASAAVLAPLGFTLRKPRAVGRNRRHHRHPHGGPGPGPGPAATHPRLRWRADVRSLQKLPVHMGLLVTEEVQEPSFSDIASLVVWCMAVGISYISVYDHQGIFKRNNSRLMDEILKQQQELLGQDCSKYSAEFANSNDKDDQDLNCPSAVKVLSPEDGKADIVRAAQDFCQLVAQQQRKPTDLDVDLLGSLLSSHGFPDPDLVLKFGPVDSTLGFLPWQIRLTEIVSLPSHLNISYEDFFSALRQYAACEQRLGK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q99LJ8","disprot_id":"DP01304","ncbi_taxon_id":10090,"regions_counter":6,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":120,"region_id":"DP01304r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Nogo-B receptor possesses an intrinsically unstructured ectodomain and a partially folded cytoplasmic domain. <i> Li M, Song J. </i> Biochem Biophys Res Commun, 2007","statement":[{"text":"The far-UV CD spectrum of the NgBR ectodomain owned the largest negative signal at 198 nm and had no positive signal at 190 nm, indicating that it was predominantly unstructured.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":47,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17585875","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":120,"term_name":"disorder to order","start":47,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"It is highly possible that the NgBR cytoplasmic domain becomes well-folded upon binding isoprenyl lipids and/or prenylated proteins.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17585875","version":2,"reference_html":"Nogo-B receptor possesses an intrinsically unstructured ectodomain and a partially folded cytoplasmic domain. <i> Li M, Song J. </i> Biochem Biophys Res Commun, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP01304r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":120,"region_id":"DP01304r003","released":"2022_03","ec_id":"ECO:0006206","reference_html":"Nogo-B receptor possesses an intrinsically unstructured ectodomain and a partially folded cytoplasmic domain. <i> Li M, Song J. </i> Biochem Biophys Res Commun, 2007","statement":[{"text":"No significant difference was detected for its near-UV CD spectra in the absence and presence of 8 M urea , suggesting that the no tight tertiary packing existed in the NgBR ectodomain.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":47,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17585875","version":2,"ec_name":"near-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":120,"term_name":"disorder to order","start":47,"ec_name":"near-UV circular dichroism evidence used in manual assertion","statement":[{"text":"It is highly possible that the NgBR cytoplasmic domain becomes well-folded upon binding isoprenyl lipids and/or prenylated proteins.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17585875","version":2,"reference_html":"Nogo-B receptor possesses an intrinsically unstructured ectodomain and a partially folded cytoplasmic domain. <i> Li M, Song J. </i> Biochem Biophys Res Commun, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006206","region_id":"DP01304r004","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":120,"region_id":"DP01304r005","released":"2022_03","ec_id":"ECO:0006198","reference_html":"Nogo-B receptor possesses an intrinsically unstructured ectodomain and a partially folded cytoplasmic domain. <i> Li M, Song J. </i> Biochem Biophys Res Commun, 2007","statement":[{"text":"1H–15N NMR HSQC spectrum of the NgBR ectodomain displayed very narrow spectral dispersions over both dimensions (∼0.75 ppm for 1H and ∼20 ppm for 15N) as well as NMR resonance peaks could be observed for almost all residues. These characteristics indicated that the NgBR ectodomain is highly disordered in the free state","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":47,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17585875","version":2,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":120,"term_name":"disorder to order","start":47,"ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","statement":[{"text":"It is highly possible that the NgBR cytoplasmic domain becomes well-folded upon binding isoprenyl lipids and/or prenylated proteins.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17585875","version":2,"reference_html":"Nogo-B receptor possesses an intrinsically unstructured ectodomain and a partially folded cytoplasmic domain. <i> Li M, Song J. </i> Biochem Biophys Res Commun, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006198","region_id":"DP01304r006","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_Q99LJ8","date":"2018-07-05T09:26:23.000Z","acc":"Q99LJ8","name":"Dehydrodolichyl diphosphate synthase complex subunit Nus1","length":297,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000220C3","genes":[{"name":{"value":"Nus1","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:1196365","url":"http://www.informatics.jax.org/marker/MGI:1196365"}}]},"synonyms":[{"value":"D10Ertd438e"},{"value":"Ngbr"}]}],"alphafold_very_low_content":0.1447811447811448,"disorder_content":0.24915824915824916,"disprot_consensus":{"full":[{"start":47,"end":120,"type":"T"}],"Structural state":[{"start":47,"end":120,"type":"D"}],"Structural transition":[{"start":47,"end":120,"type":"T"}]}},{"acc":"P08392","sequence":"MASENKQRPGSPGPTDGPPPTPSPDRDERGALGWGAETEEGGDDPDHDPDHPHDLDDARRDGRAPAAGTDAGEDAGDAVSPRQLALLASMVEEAVRTIPTPDPAASPPRTPAFRADDDDGDEYDDAADAAGDRAPARGREREAPLRGAYPDPTDRLSPRPPAQPPRRRRHGRWRPSASSTSSDSGSSSSSSASSSSSSSDEDEDDDGNDAADHAREARAVGRGPSSAAPAAPGRTPPPPGPPPLSEAAPKPRAAARTPAASAGRIERRRARAAVAGRDATGRFTAGQPRRVELDADATSGAFYARYRDGYVSGEPWPGAGPPPPGRVLYGGLGDSRPGLWGAPEAEEARRRFEASGAPAAVWAPELGDAAQQYALITRLLYTPDAEAMGWLQNPRVVPGDVALDQACFRISGAARNSSSFITGSVARAVPHLGYAMAAGRFGWGLAHAAAAVAMSRRYDRAQKGFLLTSLRRAYAPLLARENAALTGAAGSPGAGADDEGVAAVAAAAPGERAVPAGYGAAGILAALGRLSAAPASPAGGDDPDAARHADADDDAGRRAQAGRVAVECLAACRGILEALAEGFDGDLAAVPGLAGARPASPPRPEGPAGPASPPPPHADAPRLRAWLRELRFVRDALVLMRLRGDLRVAGGSEAAVAAVRAVSLVAGALGPALPRDPRLPSSAAAAAADLLFDNQSLRPLLAAAASAPDAADALAAAAASAAPREGRKRKSPGPARPPGGGGPRPPKTKKSGADAPGSDARAPLPAPAPPSTPPGPEPAPAQPAAPRAAAAQARPRPVAVSRRPAEGPDPLGGWRRQPPGPSHTAAPAAAALEAYCSPRAVAELTDHPLFPVPWRPALMFDPRALASIAARCAGPAPAAQAACGGGDDDDNPHPHGAAGGRLFGPLRASGPLRRMAAWMRQIPDPEDVRVVVLYSPLPGEDLAGGGASGGPPEWSAERGGLSCLLAALANRLCGPDTAAWAGNWTGAPDVSALGAQGVLLLSTRDLAFAGAVEFLGLLASAGDRRLIVVNTVRACDWPADGPAVSRQHAYLACELLPAVQCAVRWPAARDLRRTVLASGRVFGPGVFARVEAAHARLYPDAPPLRLCRGGNVRYRVRTRFGPDTPVPMSPREYRRAVLPALDGRAAASGTTDAMAPGAPDFCEEEAHSHAACARWGLGAPLRPVYVALGREAVRAGPARWRGPRRDFCARALLEPDDDAPPLVLRGDDDGPGALPPAPPGIRWASATGRSGTVLAAAGAVEVLGAEAGLATPPRREVVDWEGAWDEDDGGAFEGDGVL","creator":"gbalatti","dataset":["Viral proteins"],"date":"2018-07-05T09:37:23.000Z","disprot_id":"DP01305","features":{"pfam":[{"id":"PF03584","name":"Herpesvirus ICP4-like protein N-terminal region","start":311,"end":483},{"id":"PF03585","name":"Herpesvirus ICP4-like protein C-terminal region","start":812,"end":1252}]},"genes":[{"name":{"value":"ICP4","evidences":[],"_id":"685af523b4ac24d5329d8fad"},"synonyms":[{"value":"IE175","evidences":[],"_id":"685af523b4ac24d5329d8fae"}],"olnNames":[],"orfNames":[{"value":"RS1","evidences":[],"_id":"685af523b4ac24d5329d8faf"}],"_id":"685af523b4ac24d5329d8fac"}],"length":1298,"name":"Major viral transcription factor ICP4","ncbi_taxon_id":10299,"organism":"Human herpesvirus 1 (strain 17)","regions_counter":5,"released":"2018_11","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Peploviricota","Herviviricetes","Herpesvirales","Herpesviridae","Alphaherpesvirinae","Simplexvirus"],"UniParc":"UPI000012D182","uniref100":"UniRef100_P08392","uniref50":"UniRef50_P08392","uniref90":"UniRef90_P08392","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5MHK","_id":"685af523b4ac24d5329d8f9c"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":258,"end":286,"interaction_partner":[],"reference_html":"The herpes viral transcription factor ICP4 forms a novel DNA recognition complex. <i> Tunnicliffe RB, Lockhart-Cairns MP, Levy C, Mould AP, Jowitt TA, Sito H, Baldock C, Sandri-Goldin RM, Golovanov AP. </i> Nucleic Acids Res, 2017","reference_id":"28505309","region_id":"DP01305r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Within the X-ray crystallography derived maps, electron\ndensity was not observed for ICP4 residues 258–286, a region\npreviously predicted to be disordered, with the possible\nexception of F283 and T284 in chain","_id":"685af523b4ac24d5329d8f9b"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-29T11:42:26.911Z","_id":"685af523b4ac24d5329d8f9d"},"version":3,"_id":"685af523b4ac24d5329d8f9a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"26957","_id":"685af523b4ac24d5329d8fa2"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":258,"end":289,"interaction_partner":[],"reference_html":"The herpes viral transcription factor ICP4 forms a novel DNA recognition complex. <i> Tunnicliffe RB, Lockhart-Cairns MP, Levy C, Mould AP, Jowitt TA, Sito H, Baldock C, Sandri-Goldin RM, Golovanov AP. </i> Nucleic Acids Res, 2017","reference_id":"28505309","region_id":"DP01305r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Analysis of 3D TOCSY-HSQC and NOESY-HSQC spectra allowed the amino acid type of 34 sharp backbone amide signals to be determined based on comparison with typical random coil chemical shifts. It was also possible to assign backbone amides to 21 residues within the N-terminal region 259–289, plus the C-terminal residues 485–487 (Figure 4E). While the remaining 10 peaks could not be attributed to specific sequence positions, their sidechain chemical shifts in the TOCSY spectra were characteristic of five arginines and five alanines, which matched the numbers of remaining unassigned residues scattered within regions 258–289 and 482–487.","_id":"685af523b4ac24d5329d8fa3"},{"type":"Results","text":"1H-15N correlation NMR spectra acquired on ICP4NΔIDR contained broad and dispersed amide signals characteristic for a large globular protein, whereas in the longer ICP4N construct, we observed additional prominent sharp, poorly dispersed amide signals characteristic of the presence of an IDR","_id":"685af523b4ac24d5329d8fa4"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T10:42:13.284Z","_id":"685af523b4ac24d5329d8fa5"},"version":1,"_id":"685af523b4ac24d5329d8fa1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006287","ec_name":"electron paramagnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":258,"end":287,"interaction_partner":[],"reference_html":"The herpes viral transcription factor ICP4 forms a novel DNA recognition complex. <i> Tunnicliffe RB, Lockhart-Cairns MP, Levy C, Mould AP, Jowitt TA, Sito H, Baldock C, Sandri-Goldin RM, Golovanov AP. </i> Nucleic Acids Res, 2017","reference_id":"28505309","region_id":"DP01305r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"These results suggest that an absolute requirement for tight specific binding is the presence of the intrinsically disordered N-terminal region, whereas if this region is deleted, the affinity for DNA consensus sequence is not only reduced, but approximately half of this consensus sequence is no longer recognized.","_id":"685af523b4ac24d5329d8fa7"}],"states_connection":[],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_id":"GO:0003677","term_is_binding":true,"term_is_obsolete":false,"term_name":"DNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T10:45:35.112Z","_id":"685af523b4ac24d5329d8fa8"},"version":1,"_id":"685af523b4ac24d5329d8fa6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006287","ec_name":"electron paramagnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":258,"end":289,"interaction_partner":[],"reference_html":"The herpes viral transcription factor ICP4 forms a novel DNA recognition complex. <i> Tunnicliffe RB, Lockhart-Cairns MP, Levy C, Mould AP, Jowitt TA, Sito H, Baldock C, Sandri-Goldin RM, Golovanov AP. </i> Nucleic Acids Res, 2017","reference_id":"28505309","region_id":"DP01305r005","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"The combination of the ICP4N globular homo-dimer and IDRs tune the specificity and maximize affinity for a DNA motif. Conversely, the combination of the IDRs with the apparent conformational plasticity of the S-loop and R-turn likely allows non-consensus DNA interactions with ICP4. The flexibility of these regions may facilitate the linear movement of ICP4 along a DNA duplex in search of high affinity consensus sites, or hopping along longer distances mediated by the IDRs. ","_id":"685af523b4ac24d5329d8faa"}],"states_connection":[],"term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-12T10:47:59.162Z","_id":"685af523b4ac24d5329d8fab"},"version":1,"_id":"685af523b4ac24d5329d8fa9","reference_source":"pmid"}],"__v":0,"disorder_content":0.02465331278890601,"disprot_consensus":{"full":[{"start":258,"end":289,"type":"D"}],"Structural state":[{"start":258,"end":289,"type":"D"}],"Molecular function":[{"start":258,"end":287,"type":"F"}],"Disorder function":[{"start":258,"end":289,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00005","name":"ABC transporter","start":521,"end":671},{"id":"PF00664","name":"ABC transporter transmembrane region","start":189,"end":458}],"gene3D":[{"start":229,"end":552,"id":"1.20.1560.10","name":"ABC transporter type 1, transmembrane domain"},{"start":555,"end":806,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_Q03518","sequence":"MASSRCPAPRGCRCLPGASLAWLGTVLLLLADWVLLRTALPRIFSLLVPTALPLLRVWAVGLSRWAVLWLGACGVLRATVGSKSENAGAQGWLAALKPLAAALGLALPGLALFRELISWGAPGSADSTRLLHWGSHPTAFVVSYAAALPAAALWHKLGSLWVPGGQGGSGNPVRRLLGCLGSETRRLSLFLVLVVLSSLGEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPERYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMVQAPADAPE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q03518","disprot_id":"DP01306","ncbi_taxon_id":9606,"regions_counter":1,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":112,"region_id":"DP01306r001","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Structure of the transporter associated with antigen processing trapped by herpes simplex virus. <i> Oldham ML, Grigorieff N, Chen J. </i> Elife, 2016","statement":[{"text":"No density was observed for either the C-terminal 33 residues of ICP47 or the two TMD0s, indicating these regions are flexible in this conformation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":1,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5U1D"}],"reference_id":"27935481","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q03518","date":"2018-07-05T09:43:28.000Z","acc":"Q03518","name":"Antigen peptide transporter 1","length":748,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00001368D6","genes":[{"name":{"value":"TAP1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10605026","url":"http://www.ncbi.nlm.nih.gov/pubmed/10605026","alternativeUrl":"https://europepmc.org/abstract/MED/10605026"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:43","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:43"}}]},"synonyms":[{"value":"ABCB2"},{"value":"PSF1"},{"value":"RING4"},{"value":"Y3"}]}],"alphafold_very_low_content":0.14356435643564355,"disorder_content":0.1497326203208556,"disprot_consensus":{"full":[{"start":1,"end":112,"type":"D"}],"Structural state":[{"start":1,"end":112,"type":"D"}]}},{"acc":"O60828","sequence":"MPLPVALQTRLAKRGILKHLEPEPEEEIIAEDYDDDPVDYEATRLEGLPPSWYKVFDPSCGLPYYWNADTDLVSWLSPHDPNSVVTKSAKKLRSSNADAEEKLDRSHDKSDRGHDKSDRSHEKLDRGHDKSDRGHDKSDRDRERGYDKVDRERERDRERDRDRGYDKADREEGKERRHHRREELAPYPKSKKAVSRKDEELDPMDPSSYSDAPRGTWSTGLPKRNEAKTGADTTAAGPLFQQRPYPSPGAVLRANAEASRTKQQD","alphafold_very_low_content":"0.09056603773584905","creator":"eleonardi","dataset":["NDDs-related proteins"],"date":"2018-07-05T09:56:13.000Z","disprot_id":"DP01308","features":{"gene3D":[{"start":44,"end":102,"id":"2.20.70.10","name":"2.20.70.10","_id":"685af523b4ac24d5329d8fb0"},{"start":175,"end":265,"id":"3.40.30.10","name":"Glutaredoxin","_id":"685af523b4ac24d5329d8fb1"}],"pfam":[{"id":"PF28767","name":"PQBP1 helical domain","start":129,"end":186}]},"genes":[{"name":{"value":"PQBP1","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/10332029","id":"10332029","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/10332029","_id":"685af523b4ac24d5329d901a"},"code":"ECO:0000303","_id":"685af523b4ac24d5329d9019"},{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/11163963","id":"11163963","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/11163963","_id":"685af523b4ac24d5329d901c"},"code":"ECO:0000303","_id":"685af523b4ac24d5329d901b"},{"source":{"id":"HGNC:9330","name":"HGNC","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9330","_id":"685af523b4ac24d5329d901e"},"code":"ECO:0000312","_id":"685af523b4ac24d5329d901d"}],"_id":"685af523b4ac24d5329d901f"},"synonyms":[{"value":"NPW38","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/10198427","id":"10198427","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/10198427","_id":"685af523b4ac24d5329d9022"},"code":"ECO:0000303","_id":"685af523b4ac24d5329d9021"}],"_id":"685af523b4ac24d5329d9020"}],"olnNames":[],"orfNames":[{"value":"JM26","evidences":[],"_id":"685af523b4ac24d5329d9023"}],"_id":"685af523b4ac24d5329d9018"}],"length":265,"name":"Polyglutamine-binding protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":24,"released":"2018_11","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000073DB7","uniref100":"UniRef100_O60828","uniref50":"UniRef50_O60828","uniref90":"UniRef90_O60828","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0001591","ec_name":"atomic force microscopy evidence used in manual assertion","ec_ontology":"ECO","start":82,"end":265,"interaction_partner":[],"reference_html":"Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy. <i> Kodera N, Noshiro D, Dora SK, Mori T, Habchi J, Blocquel D, Gruet A, Dosnon M, Salladini E, Bignon C, Fujioka Y, Oda T, Noda NN, Sato M, Lotti M, Mizuguchi M, Longhi S, Ando T. </i> Nat Nanotechnol, 2021","reference_id":"33230318","region_id":"DP01308r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In the five constructs, the IDRs with average diameter 0.5 ± 0.1–0.3 nm (mean ± s.d.) appeared constantly disordered.","_id":"685af523b4ac24d5329d8fbb"},{"type":"Results","text":"This Flory exponent ν is close to 0.5, which holds for 2D and three-dimensional (3D) ideal and Gaussian chains, indicating that these constantly disordered segments have similar values of persistence length (Lp)","_id":"685af523b4ac24d5329d8fbc"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-08-03T09:08:38.323Z","_id":"685af523b4ac24d5329d8fbd"},"version":2,"_id":"685af523b4ac24d5329d8fba","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":265,"interaction_partner":[],"reference_html":"Solution model of the intrinsically disordered polyglutamine tract-binding protein-1. <i> Rees M, Gorba C, de Chiara C, Bui TT, Garcia-Maya M, Drake AF, Okazawa H, Pastore A, Svergun D, Chen YW. </i> Biophys J, 2012","reference_id":"22500761","region_id":"DP01308r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Incubation of PQBP-1 with ANS in the native condition (PBS) results in a blue shift of the fluorescence spectral peak from 510 nm to 475 nm accompanied by a threefold increase in quantum yield (Fig. 4 a). These effects are characteristic of ANS binding to a species adopting a premolten or molten-globule conformation. The relatively small increase in quantum yield suggested that ANS binding to PQBP-1 is not hydrophobic but instead is electrostatic in nature (43).","_id":"685af523b4ac24d5329d8fbf"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-08-03T09:09:17.090Z","_id":"685af523b4ac24d5329d8fc0"},"version":2,"_id":"685af523b4ac24d5329d8fbe","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":265,"interaction_partner":[],"reference_html":"Solution model of the intrinsically disordered polyglutamine tract-binding protein-1. <i> Rees M, Gorba C, de Chiara C, Bui TT, Garcia-Maya M, Drake AF, Okazawa H, Pastore A, Svergun D, Chen YW. </i> Biophys J, 2012","reference_id":"22500761","region_id":"DP01308r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The RS of PQBP-1 obtained from gel filtration (3.50 nm) agrees well with that determined from sedimentation velocity experiments (3.67 nm), and that predicted for a natively disordered premolten globule protein (3.70 ± 0.41 nm).","_id":"685af523b4ac24d5329d8fc2"},{"type":"Results","text":"The major peak has an elution volume that corresponds to two times the molecular mass of PQBP-1 (30.6 kDa), suggesting that the protein is dimeric if it adopts a compact, globular conformation. However, it is well established that elongated or unfolded proteins elute at a volume corresponding to a higher apparent molecular mass (40).","_id":"685af523b4ac24d5329d8fc3"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-08-03T09:09:15.104Z","_id":"685af523b4ac24d5329d8fc4"},"version":2,"_id":"685af523b4ac24d5329d8fc1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006275","ec_name":"analytical ultracentrifugation evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":265,"interaction_partner":[],"reference_html":"Solution model of the intrinsically disordered polyglutamine tract-binding protein-1. <i> Rees M, Gorba C, de Chiara C, Bui TT, Garcia-Maya M, Drake AF, Okazawa H, Pastore A, Svergun D, Chen YW. </i> Biophys J, 2012","reference_id":"22500761","region_id":"DP01308r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The RS of PQBP-1 obtained from gel filtration (3.50 nm) agrees well with that determined from sedimentation velocity experiments (3.67 nm), and that predicted for a natively disordered premolten globule protein (3.70 ± 0.41 nm).","_id":"685af523b4ac24d5329d8fc6"},{"type":"Results","text":"The frictional coefficient ratio (f/f0) has a value of 1.74 (±0.09), which suggests that PQBP-1 is highly elongated. The Stokes radius of PQBP-1 calculated from these experiments is 3.67 (±0.02) nm.","_id":"685af523b4ac24d5329d8fc7"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-08-03T09:09:13.135Z","_id":"685af523b4ac24d5329d8fc8"},"version":2,"_id":"685af523b4ac24d5329d8fc5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":265,"interaction_partner":[],"reference_html":"Solution model of the intrinsically disordered polyglutamine tract-binding protein-1. <i> Rees M, Gorba C, de Chiara C, Bui TT, Garcia-Maya M, Drake AF, Okazawa H, Pastore A, Svergun D, Chen YW. </i> Biophys J, 2012","reference_id":"22500761","region_id":"DP01308r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The CD spectrum of PQBP-1 (Fig. 3 a) is typical of a protein or peptide without regular conformation: it lacks spectral features or any positive signals in the far-UV range, and has a characteristic negative maximum at 200 nm (41, 42). The absence of a positive CD signal below 200 nm indicates that there is very little or no helical structure.","_id":"685af523b4ac24d5329d8fca"},{"type":"Results","text":"From the top 20 solutions (data not shown), the spectrum is found to consist of a significant amount of β-strand structure (∼20–50%) and turns (∼15–40%), but little helical content (∼5–10%). The remaining regions of the protein (∼25–55%) are irregular structures. The variable temperature CD results are also typical of a disordered protein, with a broad melting profile (Fig. 3 b).","_id":"685af523b4ac24d5329d8fcb"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-08-03T09:09:12.157Z","_id":"685af523b4ac24d5329d8fcc"},"version":2,"_id":"685af523b4ac24d5329d8fc9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":265,"interaction_partner":[],"reference_html":"Solution model of the intrinsically disordered polyglutamine tract-binding protein-1. <i> Rees M, Gorba C, de Chiara C, Bui TT, Garcia-Maya M, Drake AF, Okazawa H, Pastore A, Svergun D, Chen YW. </i> Biophys J, 2012","reference_id":"22500761","region_id":"DP01308r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The processed scattering pattern of PQBP-1 (Fig. 5 a) yields an Rg of 3.8 (±0.2) nm, with a molecular mass of 30 (±3) kDa, suggesting that the protein remains monomeric in solution. The ratio of the Rg to the hydrodynamics radius (determined by AUC and SEC) is an indicator of the compactness of a protein. PQBP-1 has an Rg/RS ratio of 1.0, which is intermediate between the value of a spherical species (0.8) and that of an unstructured random coil (1.5) (47). ","_id":"685af523b4ac24d5329d8fce"},{"type":"Results","text":"Instead, this plot shows a peak at approximately q = 1 nm−1 followed by a shallow downward slope, suggesting that PQBP-1 is partially unfolded. The p(r) function of PQBP-1 has an asymmetric shape (Fig. 5 c), with its maximum at low r followed by a long tail. This is again consistent with an extended, perhaps partially unfolded molecule with the maximum dimension (Dmax) equal to 13 nm.","_id":"685af523b4ac24d5329d8fcf"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-08-03T09:09:20.875Z","_id":"685af523b4ac24d5329d8fd0"},"version":2,"_id":"685af523b4ac24d5329d8fcd","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006077","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","ec_ontology":"ECO","start":223,"end":265,"interaction_partner":[{"db":"UniProt","id":"P83876","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8fd2"}],"reference_html":"Polyglutamine tract-binding protein-1 binds to U5-15kD via a continuous 23-residue segment of the C-terminal domain. <i> Takahashi M, Mizuguchi M, Shinoda H, Aizawa T, Demura M, Okazawa H, Kawano K. </i> Biochim Biophys Acta, 2010","reference_id":"20307692","region_id":"DP01308r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The N-terminal deletion mutants used were PQBP-1(179–265), PQBP-1(193–265) and PQBP-1(223–265). Fig. 2 shows that all of the deletion mutants bound to U5-15kD, and thus the residues 223 to 265 of PQBP-1 appear to be sufficient for the interaction with U5-15kD. The fragment PQBP-1(223–265) is called PQBP-1-CT43 in the following.","_id":"685af523b4ac24d5329d8fd3"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-08-03T09:32:56.419Z","_id":"685af523b4ac24d5329d8fd4"},"version":3,"_id":"685af523b4ac24d5329d8fd1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":223,"end":265,"interaction_partner":[{"db":"UniProt","id":"P83876","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8fd6"}],"reference_html":"Polyglutamine tract-binding protein-1 binds to U5-15kD via a continuous 23-residue segment of the C-terminal domain. <i> Takahashi M, Mizuguchi M, Shinoda H, Aizawa T, Demura M, Okazawa H, Kawano K. </i> Biochim Biophys Acta, 2010","reference_id":"20307692","region_id":"DP01308r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The attenuated resonances upon binding of PQBP-1-CT43 originate from residues in the α1 helix, the loop β2–β3, the strand β3, the loop β3–β4, and the strand β4 (Fig. 5A). These residues are located on one face of U5-15kD (Fig. 5B).","_id":"685af523b4ac24d5329d8fd7"},{"type":"Results","text":"The HSQC spectrum of PQBP-1-CT43 in the free form is typical of an unstructured protein (Fig. 6A), since the backbone resonances are clustered together in a limited frequency range, spanning less than 0.7 ppm in the 1H dimension [23].","_id":"685af523b4ac24d5329d8fd8"},{"type":"Discussion","text":"The binding of U5-15kD results in strong attenuation of the resonances originating from residues 241 to 263 of PQBP-1-CT43. From this, we conclude that the binding site is a continuous segment of residues 241–263 within the C-terminal domain, and that this segment undergoes some conformational and dynamical changes upon binding to U5-15kD.","_id":"685af523b4ac24d5329d8fd9"},{"type":"Discussion","text":"On the other hand, there was no significant chemical shift change in residues 193–240 of PQBP-1 following the binding to U5-15kD [12]. This means that the residues 193–240, that is, the C-terminal domain except for the binding segment, remains unstructured even in the bound state.","_id":"685af523b4ac24d5329d8fda"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-08-03T09:32:55.214Z","_id":"685af523b4ac24d5329d8fdb"},"version":3,"_id":"685af523b4ac24d5329d8fd5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IMP","ec_id":"ECO:0000315","ec_name":"mutant phenotype evidence used in manual assertion","ec_ontology":"ECO","start":223,"end":265,"interaction_partner":[{"db":"UniProt","id":"P83876","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8fdd"}],"reference_html":"Polyglutamine tract-binding protein-1 binds to U5-15kD via a continuous 23-residue segment of the C-terminal domain. <i> Takahashi M, Mizuguchi M, Shinoda H, Aizawa T, Demura M, Okazawa H, Kawano K. </i> Biochim Biophys Acta, 2010","reference_id":"20307692","region_id":"DP01308r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The alanine substitutions markedly reduced the binding activity in the case of Y245A, V251A and L252A (Fig. 7). On the other hand, the N255A and R260A mutations slightly reduced the binding activity, although the effect of R260A was very small. ","_id":"685af523b4ac24d5329d8fde"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-08-03T09:32:54.362Z","_id":"685af523b4ac24d5329d8fdf"},"version":3,"_id":"685af523b4ac24d5329d8fdc","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":220,"end":265,"interaction_partner":[],"reference_html":"Segmental isotope-labeling of the intrinsically disordered protein PQBP1. <i> Nabeshima Y, Mizuguchi M, Kajiyama A, Okazawa H. </i> FEBS Lett, 2014","reference_id":"25447530","region_id":"DP01308r014","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Next, we compared the 1H–15N HSQC spectra of the segmentally isotope-labeled PQBP1 and the isolated C-fragment of residues 220–265. The 1H–15N HSQC spectrum of the C-fragment shows the backbone amide resonances within 8.0–8.6 ppm in the 1H dimension (Fig. 3c). The narrow chemical shift dispersion in the 1H dimension is characteristic of IDPs","_id":"685af523b4ac24d5329d8fe1"},{"type":"Results","text":"The 1H–15N HSQC spectrum of the segmentally isotope-labeled PQBP1 is similar to that of the C-fragment, and thus the C-segment (residues 220–265) within full-length PQBP1 is disordered like the isolated C-fragment (Fig. 3).","_id":"685af523b4ac24d5329d8fe2"},{"type":"Discussion","text":"We concluded that the C-segment (residues 220–265) interacts very weakly with the N-segment (residues 1–220) within the context of full-length PQBP1. This is compatible with the solution model of PQBP1 reported by Ree et al. [42].","_id":"685af523b4ac24d5329d8fe3"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-08-05T07:13:51.684Z","_id":"685af523b4ac24d5329d8fe4"},"version":2,"_id":"685af523b4ac24d5329d8fe0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"4BWS","_id":"685af523b4ac24d5329d8fe6"},{"db":"PDB","id":"4BWQ","_id":"685af523b4ac24d5329d8fe7"},{"db":"PDB","id":"4CDO","_id":"685af523b4ac24d5329d8fe8"}],"curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":238,"end":260,"interaction_partner":[],"reference_html":"Mutations in the PQBP1 gene prevent its interaction with the spliceosomal protein U5-15 kD. <i> Mizuguchi M, Obita T, Serita T, Kojima R, Nabeshima Y, Okazawa H. </i> Nat Commun, 2014","reference_id":"24781215","region_id":"DP01308r015","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The refined model of the PQBP1-CT43 in the complex consists of the residues 238–260: it lacks the 15 N-terminal residues (residues 223–237; KRNEAKTGADTTAAG) and the 5 C-terminal residues (residues 261–265; TKQQD) owing to conformational flexibility (Fig. 2a). PQBP1-CT43 in the complex adopts an L-shaped structure with an extended conformation (residues 238–247) followed by an α-helix conformation (residues 248–259). The α-helix starts at Pro248, which generates the bend of the L-shaped structure.","_id":"685af523b4ac24d5329d8fe9"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-08-02T14:32:25.337Z","_id":"685af523b4ac24d5329d8fea"},"version":2,"_id":"685af523b4ac24d5329d8fe5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"4BWS","_id":"685af523b4ac24d5329d8fec"},{"db":"PDB","id":"4BWQ","_id":"685af523b4ac24d5329d8fed"},{"db":"PDB","id":"4CDO","_id":"685af523b4ac24d5329d8fee"}],"curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":223,"end":243,"interaction_partner":[],"reference_html":"Mutations in the PQBP1 gene prevent its interaction with the spliceosomal protein U5-15 kD. <i> Mizuguchi M, Obita T, Serita T, Kojima R, Nabeshima Y, Okazawa H. </i> Nat Commun, 2014","reference_id":"24781215","region_id":"DP01308r016","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The crystal structure of the fusion protein was refined to a resolution of 2.5 Å with an Rwork/Rfree value of 19/24% (Table 1). The refined model of the fusion protein is missing the residues 223–243 and 260–265 of PQBP1, presumably owing to conformational flexibility.","_id":"685af523b4ac24d5329d8fef"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-08-02T14:24:31.767Z","_id":"685af523b4ac24d5329d8ff0"},"version":2,"_id":"685af523b4ac24d5329d8feb","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"4BWS","_id":"685af523b4ac24d5329d8ff2"},{"db":"PDB","id":"4BWQ","_id":"685af523b4ac24d5329d8ff3"},{"db":"PDB","id":"4CDO","_id":"685af523b4ac24d5329d8ff4"}],"curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":238,"end":260,"interaction_partner":[{"db":"UniProt","id":"P83876\t","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d8ff5"}],"reference_html":"Mutations in the PQBP1 gene prevent its interaction with the spliceosomal protein U5-15 kD. <i> Mizuguchi M, Obita T, Serita T, Kojima R, Nabeshima Y, Okazawa H. </i> Nat Commun, 2014","reference_id":"24781215","region_id":"DP01308r017","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The binary complex of PQBP1-CT43 and U5–15kD was obtained by mixing the proteins at a 1:5 molar ratio (U5–15kD to PQBP1-CT43). The crystals belong to space group P2 and contain four heterodimeric complexes in the asymmetric unit. The crystal structure of the binary complex was refined to a resolution of 2.1 Å with an Rwork/Rfree value of 19/25% (Table 1). The refined model of the PQBP1-CT43 in the complex consists of the residues 238–260: it lacks the 15 N-terminal residues (residues 223–237; KRNEAKTGADTTAAG) and the 5 C-terminal residues (residues 261–265; TKQQD) owing to conformational flexibility (Fig. 2a).","_id":"685af523b4ac24d5329d8ff6"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-08-02T14:32:26.334Z","_id":"685af523b4ac24d5329d8ff7"},"version":3,"_id":"685af523b4ac24d5329d8ff1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":265,"interaction_partner":[],"reference_html":"Polyglutamine tract binding protein-1 is an intrinsically unstructured protein. <i> Takahashi M, Mizuguchi M, Shinoda H, Aizawa T, Demura M, Okazawa H, Kawano K. </i> Biochim Biophys Acta, 2009","reference_id":"19303059","region_id":"DP01308r018","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"In the present study, we demonstrate that PQBP-1 is composed of a large unstructured region and a small folded core. Intriguingly, the large unstructured region encompasses two functional domains: a polar amino acid rich domain and a C-terminal domain. These findings suggest that PQBP-1 belongs to the family of intrinsically unstructured/disordered proteins.","_id":"685af523b4ac24d5329d8ff9"},{"type":"Introduction","text":"We demonstrate that PQBP-1 is composed of a large unstructured region and a small folded core. The large unstructured region encompasses two functional domains, the PRD and the CTD.","_id":"685af523b4ac24d5329d8ffa"},{"type":"Results","text":"To determine the secondary structure of the full-length PQBP-1, we recorded the far-UV CD spectrum (Fig. 3A). The CD spectrum displays a minimum at 204 nm with negative ellipticity of − 4700 deg cm2 dmol− 1, which is characteristic of a protein in largely unfolded conformations, whereas the spectral features indicative of α-helices or β-sheets are absent (Fig. 3A).","_id":"685af523b4ac24d5329d8ffb"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-22T15:29:20.953Z","_id":"685af523b4ac24d5329d8ffc"},"version":1,"_id":"685af523b4ac24d5329d8ff8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":265,"interaction_partner":[],"reference_html":"Polyglutamine tract binding protein-1 is an intrinsically unstructured protein. <i> Takahashi M, Mizuguchi M, Shinoda H, Aizawa T, Demura M, Okazawa H, Kawano K. </i> Biochim Biophys Acta, 2009","reference_id":"19303059","region_id":"DP01308r019","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"In the present study, we demonstrate that PQBP-1 is composed of a large unstructured region and a small folded core. Intriguingly, the large unstructured region encompasses two functional domains: a polar amino acid rich domain and a C-terminal domain. These findings suggest that PQBP-1 belongs to the family of intrinsically unstructured/disordered proteins.","_id":"685af523b4ac24d5329d8ffe"},{"type":"Introduction","text":"We demonstrate that PQBP-1 is composed of a large unstructured region and a small folded core. The large unstructured region encompasses two functional domains, the PRD and the CTD.","_id":"685af523b4ac24d5329d8fff"},{"type":"Results","text":"The 1H–15N HSQC spectrum also revealed the largely unfolded conformation of full-length PQBP-1, as judged by the numerous sharp resonances of backbone amides which overlap within a narrow 1H chemical shift range from 7.8 to 8.8 ppm (Fig. 4A). In addition to the sharp resonances, however, the HSQC spectrum for the full-length PQBP-1 showed several well-dispersed peaks typical of a folded conformation. The HSQC thus indicates that the full-length PQBP-1 contains a small structured region as well as a large unstructured region.","_id":"685af523b4ac24d5329d9000"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-22T15:29:23.445Z","_id":"685af523b4ac24d5329d9001"},"version":1,"_id":"685af523b4ac24d5329d8ffd","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":94,"end":265,"interaction_partner":[],"reference_html":"Polyglutamine tract binding protein-1 is an intrinsically unstructured protein. <i> Takahashi M, Mizuguchi M, Shinoda H, Aizawa T, Demura M, Okazawa H, Kawano K. </i> Biochim Biophys Acta, 2009","reference_id":"19303059","region_id":"DP01308r020","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The 1H–15N HSQC spectra of PQBP-1-PR and PQBP-1-CT showed the sharp resonances of backbone amides clustered within 7.8–8.8 ppm (1H dimension), indicating highly flexible, unfolded conformations (Fig. 4C and D). In contrast, the backbone amide resonances of PQBP-1-WW are dispersed from 7.0 to 9.8 ppm, which is characteristic of folded proteins (Fig. 4B).","_id":"685af523b4ac24d5329d9003"},{"type":"Results","text":"Therefore, the comparison of the HSQC spectra of full-length PQBP-1 and its fragments revealed that the PRD and CTD are largely unstructured in PQBP-1, and the WWD is involved in the structured region of PQBP-1.","_id":"685af523b4ac24d5329d9004"},{"type":"Curator statement","text":"Region corresponding to fragments PQBP-1-PR (94–176) and PQBP-1-CT (193–265).","_id":"685af523b4ac24d5329d9005"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-22T15:24:01.413Z","_id":"685af523b4ac24d5329d9006"},"version":1,"_id":"685af523b4ac24d5329d9002","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":94,"end":265,"interaction_partner":[],"reference_html":"Polyglutamine tract binding protein-1 is an intrinsically unstructured protein. <i> Takahashi M, Mizuguchi M, Shinoda H, Aizawa T, Demura M, Okazawa H, Kawano K. </i> Biochim Biophys Acta, 2009","reference_id":"19303059","region_id":"DP01308r021","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The far-UV CD spectrum of PQBP-1-PR and -CT lacked the typical signature of secondary structure, exhibiting instead only a negative signal at 200 nm (Fig. 3C and D). ","_id":"685af523b4ac24d5329d9008"},{"type":"Results","text":"These CD data support the conclusion derived from NMR that PQBP-1 comprises the folded region in the WWD and the large unstructured regions in the PRD and CTD.","_id":"685af523b4ac24d5329d9009"},{"type":"Curator statement","text":"Region corresponding to fragments PQBP-1-PR (94–176) and PQBP-1-CT (193–265).","_id":"685af523b4ac24d5329d900a"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-22T15:23:27.281Z","_id":"685af523b4ac24d5329d900b"},"version":1,"_id":"685af523b4ac24d5329d9007","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-09T08:26:04.717Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001269","ec_name":"surface plasmon resonance evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":265,"interaction_partner":[{"db":"UniProt","id":"P83876","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d900e"}],"reference_html":"Polyglutamine tract binding protein-1 is an intrinsically unstructured protein. <i> Takahashi M, Mizuguchi M, Shinoda H, Aizawa T, Demura M, Okazawa H, Kawano K. </i> Biochim Biophys Acta, 2009","reference_id":"19303059","region_id":"DP01308r022","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Binding of U5-15kD is one of the functions of PQBP-1. To determine the affinity of PQBP-1 to U5-15kD, we decided to analyze this interaction by surface plasmon resonance (Fig. 6A). We determined the apparent association rate constant and dissociation rate constant for the complex between PQBP-1 and U5-15kD. PQBP-1 exhibited a fast association rate with U5-15kD (ka = 4.1 × 103 M− 1 s− 1) and a slow dissociation rate (kd = 2.5 × 10− 3 s− 1). Hence, the dissociation constant (KD = kd / ka) was calculated to be 0.6 μM.","_id":"685af523b4ac24d5329d900d"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-29T21:19:21.903Z","_id":"685af523b4ac24d5329d900f"},"version":2,"_id":"685af523b4ac24d5329d900c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-09T08:25:54.674Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006077","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","ec_ontology":"ECO","start":193,"end":265,"interaction_partner":[{"db":"UniProt","id":"P83876","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9012"}],"reference_html":"Polyglutamine tract binding protein-1 is an intrinsically unstructured protein. <i> Takahashi M, Mizuguchi M, Shinoda H, Aizawa T, Demura M, Okazawa H, Kawano K. </i> Biochim Biophys Acta, 2009","reference_id":"19303059","region_id":"DP01308r023","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The binding was confirmed by GST pull-down assay and gel-filtration chromatography. The GST pull-down assay shows that either GST-PQBP-1 or GST-PQBP-1-CT binds to U5-15kD (Fig. 6B).","_id":"685af523b4ac24d5329d9011"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-29T21:19:20.051Z","_id":"685af523b4ac24d5329d9013"},"version":2,"_id":"685af523b4ac24d5329d9010","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-09T08:25:40.888Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0001184","ec_name":"gel-filtration evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":265,"interaction_partner":[{"db":"UniProt","id":"P83876","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9016"}],"reference_html":"Polyglutamine tract binding protein-1 is an intrinsically unstructured protein. <i> Takahashi M, Mizuguchi M, Shinoda H, Aizawa T, Demura M, Okazawa H, Kawano K. </i> Biochim Biophys Acta, 2009","reference_id":"19303059","region_id":"DP01308r024","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The binding was confirmed by GST pull-down assay and gel-filtration chromatography. The GST pull-down assay shows that either GST-PQBP-1 or GST-PQBP-1-CT binds to U5-15kD (Fig. 6B).","_id":"685af523b4ac24d5329d9015"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-29T21:19:14.600Z","_id":"685af523b4ac24d5329d9017"},"version":2,"_id":"685af523b4ac24d5329d9014","reference_source":"pmid"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":237,"type":"D"},{"start":238,"end":260,"type":"T"},{"start":261,"end":265,"type":"D"}],"Structural state":[{"start":1,"end":265,"type":"D"}],"Molecular function":[{"start":1,"end":265,"type":"F"}],"Structural transition":[{"start":238,"end":260,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":19,"end":315}],"gene3D":[{"start":108,"end":330,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"},{"start":1,"end":107,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"}]},"uniref50":"UniRef50_P50750","sequence":"MAKQYDSVECPFCDEVSKYEKLAKIGQGTFGEVFKARHRKTGQKVALKKVLMENEKEGFPITALREIKILQLLKHENVVNLIEICRTKASPYNRCKGSIYLVFDFCEHDLAGLLSNVLVKFTLSEIKRVMQMLLNGLYYIHRNKILHRDMKAANVLITRDGVLKLADFGLARAFSLAKNSQPNRYTNRVVTLWYRPPELLLGERDYGPPIDLWGAGCIMAEMWTRSPIMQGNTEQHQLALISQLCGSITPEVWPNVDNYELYEKLELVKGQKRKVKDRLKAYVRDPYALDLIDKLLVLDPAQRIDSDDALNHDFFWSDPMPSDLKGMLSTHLTSMFEYLAPPRRKGSQITQQSTNQSRNPATTNQTEFERVF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P50750","disprot_id":"DP01309","ncbi_taxon_id":9606,"regions_counter":8,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":98,"region_id":"DP01309r001","released":"2023_06","ec_id":"ECO:0006220","reference_html":"The structure of P-TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation. <i> Baumli S, Lolli G, Lowe ED, Troiani S, Rusconi L, Bullock AN, Debreczeni JE, Knapp S, Johnson LN. </i> EMBO J, 2008","statement":[{"text":"The loops between residues 50-55, 87-98 and 259-267 are missing in the 2.5A structure as well as a part of the activation segment residues 176-182.  ","type":"Supplementary material"},{"text":"The major differences occur in loop regions and include the loop before the αC helix, corresponding to a CycA contact region in the CDK2/CycA complex, the\nloop between β4 and β5 where CDK9 has an insertion compared with CDK2 (not defined by electron density (residues 87–98)), the loop between the  αD and  αE helices (residues 114–121), part of the activation segment (where additional residues 179–182 are not defined) and the loop between  αG and  αH residues 259–267.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"maspromonte","start":87,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"curator_orcid":"0000-0002-4937-6952","date":"2023-06-21T14:12:58.606Z","reference_source":"pmid","term_name":"disorder","reference_id":"18566585","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"3BLR"},{"db":"PDB","id":"3BLH"},{"db":"PDB","id":"3BLQ"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18367","entry_name":"phosphate(3-)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"47344","entry_name":"alvocidib"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":" O60563"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46097","entry_name":"Htris"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15422","entry_name":"ATP"}],"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":186,"end":186,"position":"Specific residue","statements":[{"type":"Results","text":"To explore the role of Thr186 phosphorylation in catalysis,\nwe generated the T186A mutant. "}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T14:31:07.867Z"}},{"start":328,"end":372,"reference_id":"22959624","reference_source":"pmid","reference_html":"The CDK9 tail determines the reaction pathway of positive transcription elongation factor b. <i> Baumli S, Hole AJ, Wang LZ, Noble ME, Endicott JA. </i> Structure, 2012","date":"2022-10-28T09:18:42.688Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"4EC9"}],"region_id":"DP01309r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60563 "}],"statement":[{"text":"In these structures, electron density for the C-terminal sequence of CDK9 is either missing after residue 325 (Baumli et al., 2008) or extends away from the CDK9 fold and adopts a structure that is determined by crystal contacts (Tahirov et al., 2010; Figure S4).","type":"Results"},{"text":"The electron density gradually weakens after residue 327, and further residues could not be built with confidence. This result indicates that the CDK9 C-terminal tail is inherently flexible.","type":"Results"},{"text":"(I) Apo CDK9 has a flexible C-terminal tail.","type":"Figure"},{"text":"(V) ADP is released and the kinase returns to its apo state with a flexible C-terminal tail.","type":"Figure"}],"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":186,"end":186,"position":"Specific residue"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-28T18:13:43.164Z"}},{"start":328,"end":338,"reference_id":"22959624","reference_source":"pmid","reference_html":"The CDK9 tail determines the reaction pathway of positive transcription elongation factor b. <i> Baumli S, Hole AJ, Wang LZ, Noble ME, Endicott JA. </i> Structure, 2012","date":"2023-06-21T14:18:00.752Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":1,"cross_refs":[{"db":"PDB","id":"4EC8"},{"db":"PDB","id":"4EC9"}],"region_id":"DP01309r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60563 "},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:135398514"}],"statement":[{"text":"The CDK9 C-Terminal Tail Becomes Structured upon Binding to an Active Kinase Conformation.","type":"Results"},{"text":"The resulting crystal structure, solved at 3.6 Å resolution, shows unambiguous electron density for the inhibitor and 11 additional CDK9 C-terminal residues as compared with the structure of CDK9FL/cyclin T259 (Table 2; Figures 3B–3D).","type":"Results"},{"text":"CDK9 adopts a closed state upon DRB binding in which the N-terminal lobe is rotated by 8° with respect to the apo or ATP-bound structure.","type":"Results"},{"text":"This closed state is stabilized in the context of CDK9FL by folding of the C-terminal tail over the ATP binding site (Figures 3B and 3D).","type":"Results"}],"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":186,"end":186,"position":"Specific residue"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T14:32:06.879Z"}},{"start":345,"end":357,"reference_id":"12942536","reference_source":"pmid","reference_html":"Catalytic activity of Cdk9 is required for nuclear co-localization of the Cdk9/cyclin T1 (P-TEFb) complex. <i> Napolitano G, Majello B, Lania L. </i> J Cell Physiol, 2003","date":"2022-10-28T09:48:35.036Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"GO:0051647","term_name":"nucleus localization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007849","ec_ontology":"ECO","ec_name":"fluorescence quantification assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Lys345_Ser357del","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The resulting GAL4-Cdk9ΔST construct contains the deletion of the aa 345-357. All constructs were verified by sequencing."},{"type":"Results","text":"As shown in Figure 1, unlike the Cdk9wt GFP-fusion protein, both GFP-Cdk9Δ337 and GFP-Cdk9ΔST fusions failed to accumulate to the nucleus and the majority of transfected cells showed a fluorescence signal in both nuclear and cytoplasmic compartments."}]}],"ec_go":"IDA","region_id":"DP01309r005","term_comment":"","term_def":"\"Any process in which the nucleus is transported to, and/or maintained in, a specific location within the cell.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"statement":[{"text":" In addition to the catalityc activity, nuclear localization of Cdk9 protein requires the presence of the phospho-acceptor sites at the C-terminus tail.","type":"Abstract"},{"text":"To test this hypothesis, we constructed two C-terminal mutants Cdk9Δ337 and Cdk9ΔST both lacking the Ser/Thr residues previously shown to represent the major phospho-acceptor sites of auto-phosphorylation. As shown in Figure 1, unlike the Cdk9wt GFP-fusion protein, both GFP-Cdk9Δ337 and GFP-Cdk9ΔST fusions failed to accumulate to the nucleus and the majority of transfected cells showed a fluorescence signal in both nuclear and cytoplasmic compartments. These results provide evidences that Cdk9 nuclear localization is dependent upon the catalytic activity of the kinase and the presence of the major phospho-acceptor residues required for auto-phosphorylation.","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"060563"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-28T18:41:57.136Z"}},{"start":259,"end":273,"reference_id":"22292676","reference_source":"pmid","reference_html":"The CDK9 C-helix exhibits conformational plasticity that may explain the selectivity of CAN508. <i> Baumli S, Hole AJ, Noble ME, Endicott JA. </i> ACS Chem Biol, 2012","date":"2022-10-28T08:59:18.151Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"3TNH"}],"region_id":"DP01309r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"060563"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"42356","entry_name":"CAN-508"}],"statement":[{"text":"The PDB evidence shows this region lacks electron density, indicating it is disordered","type":"Curator statement"}],"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":186,"end":186,"position":"Specific residue"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-28T18:12:57.445Z"}},{"start":88,"end":97,"reference_id":"12942536","reference_source":"pmid","reference_html":"Catalytic activity of Cdk9 is required for nuclear co-localization of the Cdk9/cyclin T1 (P-TEFb) complex. <i> Napolitano G, Majello B, Lania L. </i> J Cell Physiol, 2003","date":"2022-10-28T09:09:27.463Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"3TNI "},{"db":"PDB","id":"3TNH"}],"region_id":"DP01309r007","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60563"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15961","entry_name":"O-phospho-L-homoserine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"42356","entry_name":"CAN-508"}],"statement":[{"text":"The PDB evidence shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":186,"end":186,"position":"Specific residue"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-28T18:12:57.954Z"}},{"start":330,"end":372,"reference_id":"22959624","reference_source":"pmid","reference_html":"The CDK9 tail determines the reaction pathway of positive transcription elongation factor b. <i> Baumli S, Hole AJ, Wang LZ, Noble ME, Endicott JA. </i> Structure, 2012","date":"2022-10-28T09:26:35.570Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"GO:0016301","term_name":"kinase activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001202","ec_ontology":"ECO","ec_name":"in vitro protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","region_id":"DP01309r008","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60563","statements":[{"type":"Methods","text":"CDK9/cyclin T activity was measured by incorporating radiolabeled phosphate into substrate GST-CTD containing 52 heptad repeats."}]}],"statement":[{"text":"At an ATP concentration of 100 μM, CDK9330 has only 30% of the kinase activity of the full-length protein (Figure S1A available online). Further enzymatic analysis revealed that this difference in activity does not result from differences in affinity toward GST-CTD, because both CDK9330 and CDK9FL have very similar KM,app (apparent KM value at a fixed concentration of the second substrate) values for this substrate (21.3 ± 3.7 μM versus 24.3 ± 2.7 μM, respectively; Figure S1B).","type":"Results"},{"text":"Furthermore, the dependence of KM as well as Vmax with respect to the ATP substrate indicates that the C-terminal tail influences ATP binding and catalysis (Cornish-Bowden, 2004).","type":"Results"}],"term_comment":"Note that this term encompasses all activities that transfer a single phosphate group; although ATP is by far the most common phosphate donor, reactions using other phosphate donors are included in this term.","term_def":"\"Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.\" [ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-28T18:32:09.275Z"}}],"released":"2018_11","uniref100":"UniRef100_P50750","date":"2018-07-05T11:11:32.000Z","acc":"P50750","name":"Cyclin-dependent kinase 9","length":372,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI0000127435","genes":[{"name":{"value":"CDK9","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10903437","url":"http://www.ncbi.nlm.nih.gov/pubmed/10903437","alternativeUrl":"https://europepmc.org/abstract/MED/10903437"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:1780","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:1780"}}]},"synonyms":[{"value":"CDC2L4"},{"value":"TAK"}]}],"alphafold_very_low_content":0.08602150537634409,"disorder_content":0.1935483870967742,"disprot_consensus":{"full":[{"start":87,"end":98,"type":"D"},{"start":259,"end":273,"type":"D"},{"start":328,"end":338,"type":"T"},{"start":339,"end":372,"type":"D"}],"Structural state":[{"start":87,"end":98,"type":"D"},{"start":259,"end":273,"type":"D"},{"start":328,"end":372,"type":"D"}],"Structural transition":[{"start":328,"end":338,"type":"T"}],"Biological process":[{"start":345,"end":357,"type":"F"}],"Molecular function":[{"start":330,"end":372,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00412","name":"LIM domain","start":183,"end":238},{"id":"PF00412","name":"LIM domain","start":243,"end":299},{"id":"PF00412","name":"LIM domain","start":303,"end":367}],"gene3D":[{"start":300,"end":372,"id":"2.10.110.10","name":"Cysteine Rich Protein"},{"start":177,"end":239,"id":"2.10.110.10","name":"Cysteine Rich Protein"},{"start":240,"end":299,"id":"2.10.110.10","name":"Cysteine Rich Protein"}]},"uniref50":"UniRef50_Q8WUP2","sequence":"MASKPEKRVASSVFITLAPPRRDVAVAEEVRQAVCEARRGRPWEAPAPMKTPEAGLAGRPSPWTTPGRAAATVPAAPMQLFNGGCPPPPPVLDGEDVLPDLDLLPPPPPPPPVLLPSEEEAPAPMGASLIADLEQLHLSPPPPPPQAPAEGPSVQPGPLRPMEEELPPPPAEPVEKGASTDICAFCHKTVSPRELAVEAMKRQYHAQCFTCRTCRRQLAGQSFYQKDGRPLCEPCYQDTLERCGKCGEVVRDHIIRALGQAFHPSCFTCVTCARCIGDESFALGSQNEVYCLDDFYRKFAPVCSICENPIIPRDGKDAFKIECMGRNFHENCYRCEDCRILLSVEPTDQGCYPLNNHLFCKPCHVKRSAAGCC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q8WUP2","disprot_id":"DP01310","ncbi_taxon_id":9606,"regions_counter":3,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":19,"region_id":"DP01310r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis of the migfilin-filamin interaction and competition with integrin beta tails. <i> Lad Y, Jiang P, Ruskamo S, Harburger DS, Ylänne J, Campbell ID, Calderwood DA. </i> J Biol Chem, 2008","term_id":"IDPO:0000002","curator_id":"gminervini","start":5,"term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"18829455","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":19,"term_name":"protein binding","start":5,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","statement":[{"text":"Migfilin Residues 5-19 Mediate Binding to FLNa","type":"Results"}],"curator_id":"gminervini","released":"2022_03","term_ontology":"GO","curator_name":"Giovanni Minervini","reference_id":"18829455","version":3,"reference_html":"Structural basis of the migfilin-filamin interaction and competition with integrin beta tails. <i> Lad Y, Jiang P, Ruskamo S, Harburger DS, Ylänne J, Campbell ID, Calderwood DA. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP01310r002","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":85,"region_id":"DP01310r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis of the migfilin-filamin interaction and competition with integrin beta tails. <i> Lad Y, Jiang P, Ruskamo S, Harburger DS, Ylänne J, Campbell ID, Calderwood DA. </i> J Biol Chem, 2008","statement":[{"text":"The 1H-15N-HSQC spectrum of migfilin-(1-85) (supplemental Fig. S1) has chemical shifts typical of an unstructured species (30). Moreover, heteronuclear 1H-(15N)-NOE experiments showed complete peak inversion for nearly all the N-H cross-peaks, which implies that the protein chain is extremely flexible (31).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"gminervini","start":1,"term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"18829455","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q8WUP2","date":"2018-07-05T11:14:03.000Z","acc":"Q8WUP2","name":"Filamin-binding LIM protein 1","length":373,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000013E169","genes":[{"name":{"value":"FBLIM1"},"synonyms":[{"value":"FBLP1"}]}],"alphafold_very_low_content":0.3699731903485255,"disorder_content":0.22788203753351208,"disprot_consensus":{"full":[{"start":1,"end":85,"type":"D"}],"Structural state":[{"start":1,"end":85,"type":"D"}],"Molecular function":[{"start":5,"end":19,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00153","name":"Mitochondrial carrier protein","start":193,"end":281},{"id":"PF00153","name":"Mitochondrial carrier protein","start":287,"end":374},{"id":"PF00153","name":"Mitochondrial carrier protein","start":387,"end":472},{"id":"PF13499","name":"EF-hand domain pair","start":25,"end":84},{"id":"PF13499","name":"EF-hand domain pair","start":88,"end":148}],"gene3D":[{"start":187,"end":476,"id":"1.50.40.10","name":"Mitochondrial carrier domain"},{"start":22,"end":100,"id":"1.10.238.10","name":"EF-hand"},{"start":102,"end":176,"id":"1.10.238.10","name":"EF-hand"}]},"uniref50":"UniRef50_Q6NUK1","sequence":"MLRWLRDFVLPTAACQDAEQPTRYETLFQALDRNGDGVVDIGELQEGLRNLGIPLGQDAEEKIFTTGDVNKDGKLDFEEFMKYLKDHEKKMKLAFKSLDKNNDGKIEASEIVQSLQTLGLTISEQQAELILQSIDVDGTMTVDWNEWRDYFLFNPVTDIEEIIRFWKHSTGIDIGDSLTIPDEFTEDEKKSGQWWRQLLAGGIAGAVSRTSTAPLDRLKIMMQVHGSKSDKMNIFGGFRQMVKEGGIRSLWRGNGTNVIKIAPETAVKFWAYEQYKKLLTEEGQKIGTFERFISGSMAGATAQTFIYPMEVMKTRLAVGKTGQYSGIYDCAKKILKHEGLGAFYKGYVPNLLGIIPYAGIDLAVYELLKSYWLDNFAKDSVNPGVMVLLGCGALSSTCGQLASYPLALVRTRMQAQAMLEGSPQLNMVGLFRRIISKEGIPGLYRGITPNFMKVLPAVGISYVVYENMKQTLGVTQK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q6NUK1","disprot_id":"DP01311","ncbi_taxon_id":9606,"regions_counter":11,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":78,"region_id":"DP01311r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"A self-sequestered calmodulin-like Ca²⁺ sensor of mitochondrial SCaMC carrier and its implication to Ca²⁺-dependent ATP-Mg/P(i) transport. <i> Yang Q, Brüschweiler S, Chou JJ. </i> Structure, 2014","statement":[{"text":"Regions that have low heteronuclear NOE values include H3 and adjacent loops (residues 50–78), the Ca2+-binding loop of EF-hand III (residues 99–109), as well as the C-terminal H9 (residues 159–170) (Fig. 3B and 3G).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":50,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24332718","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-01-30T14:24:33.304Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-31T14:18:13.181Z"}},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":78,"term_name":"disorder to order","start":50,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"We attempted to crystallize the apo NTD but were not successful. We then found, during measurements of NMR relaxation rates, that the apo NTD has very substantial internal dynamics, which explains the unsuccessful crystallization trials. The 1H-15N TROSY-HSQC spectra of the apo and Ca2+-bound NTD are completely different (Fig. S4A), indicating that the structural and/or dynamic properties of the two states are very different and that Ca2+ binding clearly triggers a major conformational switch in the protein.","type":"Results"},{"text":"The relaxation data for the Ca2+-bound NTD is very uniform (except for N- and C-terminus) (Fig. 3A, 3C and 3E), which is indicative of a rigid and compact structure where the structured segments of the protein tumble together in solution.","type":"Results"},{"text":"Regions that have low heteronuclear NOE values include H3 and adjacent loops (residues 50–78), the Ca2+-binding loop of EF-hand III (residues 99–109), as well as the C-terminal H9 (residues 159–170) (Fig. 3B and 3G).","type":"Results"}],"curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24332718","version":3,"reference_html":"A self-sequestered calmodulin-like Ca²⁺ sensor of mitochondrial SCaMC carrier and its implication to Ca²⁺-dependent ATP-Mg/P(i) transport. <i> Yang Q, Brüschweiler S, Chou JJ. </i> Structure, 2014","date":"2023-01-30T14:29:00.543Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP01311r002","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-31T14:18:24.623Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":109,"region_id":"DP01311r003","released":"2023_06","ec_id":"ECO:0006165","reference_html":"A self-sequestered calmodulin-like Ca²⁺ sensor of mitochondrial SCaMC carrier and its implication to Ca²⁺-dependent ATP-Mg/P(i) transport. <i> Yang Q, Brüschweiler S, Chou JJ. </i> Structure, 2014","statement":[{"text":"Regions that have low heteronuclear NOE values include H3 and adjacent loops (residues 50–78), the Ca2+-binding loop of EF-hand III (residues 99–109), as well as the C-terminal H9 (residues 159–170) (Fig. 3B and 3G).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":99,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24332718","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-01-30T14:24:54.906Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-31T14:18:14.104Z"}},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":109,"term_name":"calcium ion binding","start":99,"ec_name":"x-ray crystallography evidence used in manual assertion","statement":[{"text":"The crystal structure of the Ca2-bound NTD shows a rigid and elongated architecture that contains three main structured regions: the N-terminal lobe (residues 22–87) and the C-terminal lobe (residues 88–152), each consisting of two Ca2+-bound EF hands, and a C-terminal helix (residues 159–170) (Fig. 1A).","type":"Results"},{"text":"Regions that have low heteronuclear NOE values include H3 and adjacent loops (residues 50–78), the Ca2+-binding loop of EF-hand III (residues 99–109), as well as the C-terminal H9 (residues 159–170) (Fig. 3B and 3G).","type":"Results"}],"curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"24332718","version":4,"reference_html":"A self-sequestered calmodulin-like Ca²⁺ sensor of mitochondrial SCaMC carrier and its implication to Ca²⁺-dependent ATP-Mg/P(i) transport. <i> Yang Q, Brüschweiler S, Chou JJ. </i> Structure, 2014","date":"2023-01-30T14:46:12.402Z","term_id":"GO:0005509","ec_id":"ECO:0005670","region_id":"DP01311r004","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a calcium ion (Ca2+).\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys15Ser","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"4N5X"}],"interaction_partner":[{"db":"ChEBI","id":"29108","operator":null,"partner_start":null,"partner_end":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46807","entry_name":"diethylene glycol"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-31T14:18:42.858Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":170,"region_id":"DP01311r005","released":"2023_06","ec_id":"ECO:0006165","reference_html":"A self-sequestered calmodulin-like Ca²⁺ sensor of mitochondrial SCaMC carrier and its implication to Ca²⁺-dependent ATP-Mg/P(i) transport. <i> Yang Q, Brüschweiler S, Chou JJ. </i> Structure, 2014","term_id":"IDPO:0000002","curator_id":"vnugnes","start":159,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24332718","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-01-30T14:25:06.746Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Regions that have low heteronuclear NOE values include H3 and adjacent loops (residues 50–78), the Ca2+-binding loop of EF-hand III (residues 99–109), as well as the C-terminal H9 (residues 159–170) (Fig. 3B and 3G).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-31T14:18:15.371Z"}},{"start":1,"end":21,"reference_id":"24332718","reference_source":"pmid","reference_html":"A self-sequestered calmodulin-like Ca²⁺ sensor of mitochondrial SCaMC carrier and its implication to Ca²⁺-dependent ATP-Mg/P(i) transport. <i> Yang Q, Brüschweiler S, Chou JJ. </i> Structure, 2014","date":"2023-01-30T14:06:51.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys15Ser","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"4N5X"}],"region_id":"DP01311r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46807","entry_name":"diethylene glycol"}],"statement":[{"text":"The structure of the Ca2+-bound NTD in the P3121 crystal was subsequently refined to 2.1 Å with good statistics (R = 17.67%, Rfree = 22.53%; full statistics in Table 1).","type":"Results"},{"text":"In the electron density map, however, only residues 22–176 were visible.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-31T14:18:16.523Z"}},{"start":177,"end":193,"reference_id":"24332718","reference_source":"pmid","reference_html":"A self-sequestered calmodulin-like Ca²⁺ sensor of mitochondrial SCaMC carrier and its implication to Ca²⁺-dependent ATP-Mg/P(i) transport. <i> Yang Q, Brüschweiler S, Chou JJ. </i> Structure, 2014","date":"2023-01-30T14:07:05.218Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys15Ser","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"4N5X"}],"region_id":"DP01311r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46807","entry_name":"diethylene glycol"}],"statement":[{"text":"The structure of the Ca2+-bound NTD in the P3121 crystal was subsequently refined to 2.1 Å with good statistics (R = 17.67%, Rfree = 22.53%; full statistics in Table 1).","type":"Results"},{"text":"In the electron density map, however, only residues 22–176 were visible.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-31T14:18:20.790Z"}},{"start":99,"end":109,"reference_id":"24332718","reference_source":"pmid","reference_html":"A self-sequestered calmodulin-like Ca²⁺ sensor of mitochondrial SCaMC carrier and its implication to Ca²⁺-dependent ATP-Mg/P(i) transport. <i> Yang Q, Brüschweiler S, Chou JJ. </i> Structure, 2014","date":"2023-01-30T14:27:55.394Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP01311r009","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"We attempted to crystallize the apo NTD but were not successful. We then found, during measurements of NMR relaxation rates, that the apo NTD has very substantial internal dynamics, which explains the unsuccessful crystallization trials. The 1H-15N TROSY-HSQC spectra of the apo and Ca2+-bound NTD are completely different (Fig. S4A), indicating that the structural and/or dynamic properties of the two states are very different and that Ca2+ binding clearly triggers a major conformational switch in the protein.","type":"Results"},{"text":"The relaxation data for the Ca2+-bound NTD is very uniform (except for N- and C-terminus) (Fig. 3A, 3C and 3E), which is indicative of a rigid and compact structure where the structured segments of the protein tumble together in solution.","type":"Results"},{"text":"Regions that have low heteronuclear NOE values include H3 and adjacent loops (residues 50–78), the Ca2+-binding loop of EF-hand III (residues 99–109), as well as the C-terminal H9 (residues 159–170) (Fig. 3B and 3G).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-31T14:18:26.429Z"}},{"start":159,"end":170,"reference_id":"24332718","reference_source":"pmid","reference_html":"A self-sequestered calmodulin-like Ca²⁺ sensor of mitochondrial SCaMC carrier and its implication to Ca²⁺-dependent ATP-Mg/P(i) transport. <i> Yang Q, Brüschweiler S, Chou JJ. </i> Structure, 2014","date":"2023-01-30T14:28:07.822Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP01311r010","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"We attempted to crystallize the apo NTD but were not successful. We then found, during measurements of NMR relaxation rates, that the apo NTD has very substantial internal dynamics, which explains the unsuccessful crystallization trials. The 1H-15N TROSY-HSQC spectra of the apo and Ca2+-bound NTD are completely different (Fig. S4A), indicating that the structural and/or dynamic properties of the two states are very different and that Ca2+ binding clearly triggers a major conformational switch in the protein.","type":"Results"},{"text":"The relaxation data for the Ca2+-bound NTD is very uniform (except for N- and C-terminus) (Fig. 3A, 3C and 3E), which is indicative of a rigid and compact structure where the structured segments of the protein tumble together in solution.","type":"Results"},{"text":"Regions that have low heteronuclear NOE values include H3 and adjacent loops (residues 50–78), the Ca2+-binding loop of EF-hand III (residues 99–109), as well as the C-terminal H9 (residues 159–170) (Fig. 3B and 3G).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-31T14:18:37.321Z"}},{"start":68,"end":79,"reference_id":"24332718","reference_source":"pmid","reference_html":"A self-sequestered calmodulin-like Ca²⁺ sensor of mitochondrial SCaMC carrier and its implication to Ca²⁺-dependent ATP-Mg/P(i) transport. <i> Yang Q, Brüschweiler S, Chou JJ. </i> Structure, 2014","date":"2023-01-30T14:50:35.896Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys15Ser","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"4N5X"}],"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"29108","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01311r011","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46807","entry_name":"diethylene glycol"}],"statement":[{"text":"The crystal structure of the Ca2-bound NTD shows a rigid and elongated architecture that contains three main structured regions: the N-terminal lobe (residues 22–87) and the C-terminal lobe (residues 88–152), each consisting of two Ca2+-bound EF hands, and a C-terminal helix (residues 159–170) (Fig. 1A).","type":"Results"},{"text":"The supplementary Figure S2 shows this region, define as EF-hand II, coordinates Ca+2 ion.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a calcium ion (Ca2+).\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-31T14:18:44.819Z"}}],"released":"2018_11","uniref100":"UniRef100_Q6NUK1","date":"2018-07-05T12:26:35.000Z","acc":"Q6NUK1","name":"Calcium-binding mitochondrial carrier protein SCaMC-1","length":477,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000352C31","genes":[{"name":{"value":"SLC25A24"},"synonyms":[{"value":"APC1"},{"value":"MCSC1"},{"value":"SCAMC1"}]}],"alphafold_very_low_content":0.06079664570230608,"disorder_content":0.18867924528301888,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"},{"start":50,"end":78,"type":"T"},{"start":79,"end":79,"type":"F"},{"start":99,"end":109,"type":"T"},{"start":159,"end":170,"type":"T"},{"start":177,"end":193,"type":"D"}],"Structural state":[{"start":1,"end":21,"type":"D"},{"start":50,"end":78,"type":"D"},{"start":99,"end":109,"type":"D"},{"start":159,"end":170,"type":"D"},{"start":177,"end":193,"type":"D"}],"Structural transition":[{"start":50,"end":78,"type":"T"},{"start":99,"end":109,"type":"T"},{"start":159,"end":170,"type":"T"}],"Molecular function":[{"start":68,"end":79,"type":"F"},{"start":99,"end":109,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05076","name":"Suppressor of fused protein (SUFU)","start":64,"end":240},{"id":"PF12470","name":"Suppressor of Fused Gli/Ci N terminal binding domain","start":253,"end":473}],"gene3D":[{"start":355,"end":484,"id":"3.30.1360.230","name":"Sufu, C-terminal domain"}]},"uniref50":"UniRef50_Q9UMX1","sequence":"MAELRPSGAPGPTAPPAPGPTAPPAFASLFPPGLHAIYGECRRLYPDQPNPLQVTAIVKYWLGGPDPLDYVSMYRNVGSPSANIPEHWHYISFGLSDLYGDNRVHEFTGTDGPSGFGFELTFRLKRETGESAPPTWPAELMQGLARYVFQSENTFCSGDHVSWHSPLDNSESRIQHMLLTEDPQMQPVQTPFGVVTFLQIVGVCTEELHSAQQWNGQGILELLRTVPIAGGPWLITDMRRGETIFEIDPHLQERVDKGIETDGSNLSGVSAKCAWDDLSRPPEDDEDSRSICIGTQPRRLSGKDTEQIRETLRRGLEINSKPVLPPINPQRQNGLAHDRAPSRKDSLESDSSTAIIPHELIRTRQLESVHLKFNQESGALIPLCLRGRLLHGRHFTYKSITGDMAITFVSTGVEGAFATEEHPYAAHGPWLQILLTEEFVEKMLEDLEDLTSPEEFKLPKEYSWPEKKLKVSILPDVVFDSPLH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UMX1","disprot_id":"DP01312","ncbi_taxon_id":9606,"regions_counter":2,"creator":"gminervini","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":360,"region_id":"DP01312r001","reference_id":"24311597","start":279,"ec_id":"ECO:0006220","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Topology scheme, with the intrinsically disordered region (IDR) represented by a dashed line.","type":"Figure"},{"text":"Although the crystallized protein was intact (Supplementary Fig. S2a), both SUFU molecules in the orthorhombic asymmetric unit show no apparent density for the C-terminal domain residues 279–360, suggesting that this region of the molecule is highly mobile.","type":"Results"},{"text":"Collectively, these data suggest that residues 279–360 constitute an intrinsically disordered region (IDR) that is an inherent feature of native human SUFU.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":5,"reference_html":"Structural basis of SUFU-GLI interaction in human Hedgehog signalling regulation. <i> Cherry AL, Finta C, Karlström M, Jin Q, Schwend T, Astorga-Wells J, Zubarev RA, Del Campo M, Criswell AR, de Sanctis D, Jovine L, Toftgård R. </i> Acta Crystallogr D Biol Crystallogr, 2013","date":"2023-11-24T12:38:46.766Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"4BL8"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P11831"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-24T12:39:26.832Z"}}],"released":"2018_11","uniref100":"UniRef100_Q9UMX1","date":"2018-07-05T12:53:32.000Z","acc":"Q9UMX1","name":"Suppressor of fused homolog","length":484,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI0000073118","genes":[{"name":{"value":"SUFU","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12068298","url":"http://www.ncbi.nlm.nih.gov/pubmed/12068298","alternativeUrl":"https://europepmc.org/abstract/MED/12068298"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:16466","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:16466"}}]},"orfNames":[{"value":"UNQ650/PRO1280","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12975309","url":"http://www.ncbi.nlm.nih.gov/pubmed/12975309","alternativeUrl":"https://europepmc.org/abstract/MED/12975309"}}]}]}],"alphafold_very_low_content":0.17768595041322313,"disorder_content":0.16942148760330578,"disprot_consensus":{"full":[{"start":279,"end":360,"type":"D"}],"Structural state":[{"start":279,"end":360,"type":"D"}]}},{"features":{"pfam":[{"id":"PF07807","name":"RED-like protein C-terminal region","start":428,"end":537},{"id":"PF07808","name":"RED-like protein N-terminal region","start":66,"end":295}]},"uniref50":"UniRef50_Q9N4U5","sequence":"MADNPTNLRNADFRKLLTSARSDRPAVSAFAKPADPKTGDDKPASFKHKHLKPAKFKKPQAAAHGKAKKEKTEADEDEAALKNILKNYRDRAAERRKQGDEKEDPSKLTAAYRAVPGDARSAQDQADLRKQAILESKYLGGDLEHTHLVKGLDYSLLNKVRSEIDKSDDDDDDDIDTAFDEKVTSSSSSSKPSEASLLAQELAQSHSENRMVRSLHRVLFKNEVPLHNQLFAKGRMAYVVELEDEETDIPTTLLRSLHDLPRAESAQSIQANNLIILKLSHVLSHLRAEPKKKKKEEFRVQLGSRDAPGAAAAAPGAKGDSIYDDLDDYVPSRKSRDSRDAGRRGSRRDRSRDRSRDRDRDRDRDNRDRYFEKSANSRREEEQNRREQQRERERAEQERRREREKEREQEKAKEREKKRKELEESSGYDECYPGGLVEMGGAWDSDEEADYSKMDAGPKKNQAVNRWDFDTEEEYASYMEGREALPKAAYQYGVKNGEGGRKNKKQSAVSDAKRLDRELNEINKIMDKRKAGGDGAGGGGDYKKPKY","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"uniref90":"UniRef90_Q9N4U5","disprot_id":"DP01313","ncbi_taxon_id":6239,"regions_counter":3,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":223,"region_id":"DP01313r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structural Basis for the Functional Coupling of the Alternative Splicing Factors Smu1 and RED. <i> Ulrich AKC, Schulz JF, Kamprad A, Schütze T, Wahl MC. </i> Structure, 2016","statement":[{"text":"These observations suggest that ceRED163−223 is unstructured in isolation and that its ceSmu1NTR-interacting α helices are induced upon complex formation","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"gminervini","start":163,"term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"27150041","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":223,"term_name":"disorder to order","start":163,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"These observations suggest that ceRED163−223 is unstructured in isolation and that its ceSmu1NTR-interacting α helices are induced upon complex formation","type":"Results"}],"curator_id":"gminervini","released":"2022_03","term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"27150041","version":2,"reference_html":"Structural Basis for the Functional Coupling of the Alternative Splicing Factors Smu1 and RED. <i> Ulrich AKC, Schulz JF, Kamprad A, Schütze T, Wahl MC. </i> Structure, 2016","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP01313r002","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":223,"term_name":"protein binding","start":163,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"These observations suggest that ceRED163−223 is unstructured in isolation and that its ceSmu1NTR-interacting α helices are induced upon complex formation","type":"Results"}],"curator_id":"gminervini","released":"2022_03","term_ontology":"GO","curator_name":"Giovanni Minervini","reference_id":"27150041","version":3,"reference_html":"Structural Basis for the Functional Coupling of the Alternative Splicing Factors Smu1 and RED. <i> Ulrich AKC, Schulz JF, Kamprad A, Schütze T, Wahl MC. </i> Structure, 2016","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","cross_refs":[{"db":"IntAct","id":"EBI-2415311"},{"db":"IntAct","id":"EBI-2411547"}],"region_id":"DP01313r003","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q9N4U5","date":"2018-07-05T13:01:25.000Z","acc":"Q9N4U5","name":"Smu-2 suppressor of mec-8 and unc-52 protein","length":547,"organism":"Caenorhabditis elegans","dataset":[],"UniParc":"UPI000007AF8F","genes":[{"name":{"value":"smu-2","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"Y49F6B.4","url":"https://www.wormbase.org/db/seq/sequence?name=Y49F6B.4;class=Transcript"}}]},"orfNames":[{"value":"Y49F6B.4","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"Y49F6B.4","url":"https://www.wormbase.org/db/seq/sequence?name=Y49F6B.4;class=Transcript"}}]}]}],"alphafold_very_low_content":0.23948811700182815,"disorder_content":0.11151736745886655,"disprot_consensus":{"full":[{"start":163,"end":223,"type":"T"}],"Structural state":[{"start":163,"end":223,"type":"D"}],"Structural transition":[{"start":163,"end":223,"type":"T"}],"Molecular function":[{"start":163,"end":223,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00536","name":"SAM domain (Sterile alpha motif)","start":785,"end":848},{"id":"PF16616","name":"Unstructured region on Polyhomeotic-like protein 1 and 2","start":662,"end":781},{"id":"PF21319","name":"Zinc finger, FCS-type","start":632,"end":661}],"gene3D":[{"start":775,"end":850,"id":"1.10.150.50","name":"Transcription Factor, Ets-1"},{"start":612,"end":662,"id":"3.30.60.160","name":"3.30.60.160"}]},"uniref50":"UniRef50_Q8IXK0","sequence":"MENELPVPHTSNRASVTTNTSGTNSSSGCISSSGGGGGSGGRPTAPQISVYSGIPDRQTVQVIQQALHRQPSTAAQYLQQMYAAQQQHLMLQTAALQQQHLSSAQLQSLAAVQQASLVANRQGSTPGSSVSSQAPAQSSSLNLAASPAAAQLINRAQSVNSAAASGLAQQAVLLGNTSSPALTASQAQMYLRAQMLIFTPTATVATVQPELCTGSPARPPTPAQVQNLTLRTQQTPAAAASGPPPTQPVLPSLALKPTPSSSQPLPAPPQGRTMAQGSPAGAKPSGTDNAPETLKAGDGNCNMEGRPGPGRAVPAVATHPLIAPAYAHLQSHQLLPQPPAKHPQPQFVAQQQPQPPRPAPQVQSQPQLASVSPSLALQSSPEDHALPLGSVTQALPLQCSTTHVHKPGNSQQCHLPTLDTGSQNGHPEGGSHPPQRRFQHTSAVILQVQPASPVTPQQCAPDDWKEVVPAEKSVPVARPGPSPHQQAIIPAIPGGLPGPKSPNIQQCPAHETGQGIVHALTDLSSPGMTSGNGNSASSIAGTAPQNGENKPPQAIVKPQILTHVIEGFVIQEGAEPFPVGRSSLLVGNLKKKYAQGFLPEKPPQQDHTTTTDSEMEEPYLQESKEEGTPLKLKCELCGRVDFAYKFKRSKRFCSMACAKRYNVGCTKRVGLFHSDRSKLQKAGTTTHNRRRASKASLPTLTKDTKKQPSGTVPLSVTAALQLAHSQEDSSRCSDNSSYEEPLSPISASSSTSRRRQGQRDLDLPDMHMRDLVGVGHHFLPSEPTKWNVEDVYEFIRSLPGCQEIAEEFRAQEIDGQALLLLKEDHLMSAMNIKLGPALKIYARISMLKDS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q9QWH1","disprot_id":"DP01315","ncbi_taxon_id":10090,"regions_counter":2,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":79,"region_id":"DP01315r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization. <i> Gray F, Cho HJ, Shukla S, He S, Harris A, Boytsov B, Jaremko Ł, Jaremko M, Demeler B, Lawlor ER, Grembecka J, Cierpicki T. </i> Nat Commun, 2016","statement":[{"text":"e found that PHC21–79 is disordered in solution as judged by poor peak dispersion on the 1H–15N HSQC spectra (Supplementary Fig. 3).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"gminervini","start":1,"term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"27827373","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":79,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"We found that the most significantly perturbed signals correspond to PHC2 residues 33–59 indicating that this represents the BMI1-binding motif in the PHC2 (Fig. 1f).","type":"Results"}],"curator_id":"gminervini","released":"2022_03","term_ontology":"GO","curator_name":"Giovanni Minervini","reference_id":"27827373","version":3,"reference_html":"BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization. <i> Gray F, Cho HJ, Shukla S, He S, Harris A, Boytsov B, Jaremko Ł, Jaremko M, Demeler B, Lawlor ER, Grembecka J, Cierpicki T. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","cross_refs":[{"db":"IntAct","id":"EBI-927401"}],"region_id":"DP01315r002","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q9QWH1","date":"2018-07-05T14:00:26.000Z","acc":"Q9QWH1","name":"Polyhomeotic-like protein 2","length":850,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000022FD4","genes":[{"name":{"value":"Phc2"},"synonyms":[{"value":"Edr2"},{"value":"Ph2"}]}],"alphafold_very_low_content":0.7211764705882353,"disorder_content":0.09294117647058824,"disprot_consensus":{"full":[{"start":1,"end":79,"type":"D"}],"Structural state":[{"start":1,"end":79,"type":"D"}],"Molecular function":[{"start":1,"end":79,"type":"F"}]}},{"features":{"pfam":[{"id":"PF13923","name":"Zinc finger, C3HC4 type (RING finger)","start":17,"end":56},{"id":"PF16207","name":"RAWUL domain RING finger- and WD40-associated ubiquitin-like","start":160,"end":224}],"gene3D":[{"start":1,"end":108,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":121,"end":233,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"}]},"uniref50":"UniRef50_P25916","sequence":"MHRTTRIKITELNPHLMCVLCGGYFIDATTIIECLHSFCKTCIVRYLETSKYCPICDVQVHKTRPLLNIRSDKTLQDIVYKLVPGLFKNEMKRRRDFYAAHPSADAANGSNEDRGEVADEEKRIITDDEIISLSIEFFDQSRLDRKVNKEKPKEEVNDKRYLRCPAAMTVMHLRKFLRSKMDIPNTFQIDVMYEEEPLKDYYTLMDIAYIYTWRRNGPLPLKYRVRPTCKRMKMSHQRDGLTNAGELESDSGSDKANSPAGGVPSTSSCLPSPSTPVQSPHPQFPHISSTMNGTSNSPSANHQSSFASRPRKSSLNGSSATSSG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P25916","disprot_id":"DP01316","ncbi_taxon_id":10090,"regions_counter":1,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":240,"region_id":"DP01316r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Detection of disordered regions in globular proteins using ¹³C-detected NMR. <i> Gray FL, Murai MJ, Grembecka J, Cierpicki T. </i> Protein Sci, 2012","statement":[{"text":"We assigned disordered fragments in BMI1106-240 by employing a combination of 13C-detected 2D CACO, CBCACO and CANCO experiments using a previously published protocol","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"gminervini","start":106,"term_ontology":"IDPO","curator_name":"Giovanni Minervini","reference_id":"23047544","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-7013-5785","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P25916","date":"2018-07-05T14:09:45.000Z","acc":"P25916","name":"Polycomb complex protein BMI-1","length":324,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000229C6","genes":[{"name":{"value":"Bmi1"},"synonyms":[{"value":"Bmi-1"},{"value":"Pcgf4"}]}],"alphafold_very_low_content":0.24691358024691357,"disorder_content":0.4166666666666667,"disprot_consensus":{"full":[{"start":106,"end":240,"type":"D"}],"Structural state":[{"start":106,"end":240,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00027","name":"Cyclic nucleotide-binding domain","start":494,"end":576},{"id":"PF00520","name":"Ion transport protein","start":143,"end":403},{"id":"PF08412","name":"Ion transport protein N-terminal","start":98,"end":141}],"gene3D":[{"start":463,"end":587,"id":"2.60.120.10","name":"Jelly Rolls"},{"start":398,"end":462,"id":"1.10.287.630","name":"Helix hairpin bin"},{"start":144,"end":397,"id":"1.10.287.70","name":"1.10.287.70"}]},"uniref50":"UniRef50_O60741","sequence":"MEGGGKPNSSSNSRDDGNSVFPAKASATGAGPAAAEKRLGTPPGGGGAGAKEHGNSVCFKVDGGGGGGGGGGGGEEPAGGFEDAEGPRRQYGFMQRQFTSMLQPGVNKFSLRMFGSQKAVEKEQERVKTAGFWIIHPYSDFRFYWDLIMLIMMVGNLVIIPVGITFFTEQTTTPWIIFNVASDTVFLLDLIMNFRTGTVNEDSSEIILDPKVIKMNYLKSWFVVDFISSIPVDYIFLIVEKGMDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIFNLIGMMLLLCHWDGCLQFLVPLLQDFPPDCWVSLNEMVNDSWGKQYSYALFKAMSHMLCIGYGAQAPVSMSDLWITMLSMIVGATCYAMFVGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADMRQKIHDYYEHRYQGKIFDEENILNELNDPLREEIVNFNCRKLVATMPLFANADPNFVTAMLSKLRFEVFQPGDYIIREGAVGKKMYFIQHGVAGVITKSSKEMKLTDGSYFGEICLLTKGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLQKFQKDLNTGVFNNQENEILKQIVKHDREMVQAIAPINYPQMTTLNSTSSTTTPTSRMRTQSPPVYTATSLSHSNLHSPSPSTQTPQPSAILSPCSYTTAVCSPPVQSPLAARTFHYASPTASQLSLMQQQPQQQVQQSQPPQTQPQQPSPQPQTPGSSTPKNEVHKSTQALHNTNLTREVRPLSASQPSLPHEVSTLISRPHPTVGESLASIPQPVTAVPGTGLQAGGRSTVPQRVTLFRQMSSGAIPPNRGVPPAPPPPAAALPRESSSVLNTDPDAEKPRFASNL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O60741","disprot_id":"DP01317","ncbi_taxon_id":9606,"regions_counter":1,"creator":"gminervini","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":93,"region_id":"DP01317r001","released":"2023_06","ec_id":"ECO:0006224","reference_html":"Structures of the Human HCN1 Hyperpolarization-Activated Channel. <i> Lee CH, MacKinnon R. </i> Cell, 2017","statement":[{"text":"Density for N-terminal residues 1 to 93 was not visible because these residues are most likely unstructured and disordered (nearly 30% are glycines).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"maspromonte","start":1,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","reference_id":"28086084","version":4,"ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","date":"2023-05-17T10:23:13.486Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-4937-6952","ec_go":"IDA","disprot_namespace":"Structural state","cross_refs":[{"db":"EMDB","id":"EMD-8511"},{"db":"PDB","id":"5U6O"},{"db":"PDB","id":"5U6P"},{"db":"EMDB","id":"EMD-8512"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17489","entry_name":"3',5'-cyclic AMP"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-17T13:13:11.560Z"}}],"released":"2018_11","uniref100":"UniRef100_O60741","date":"2018-07-05T14:22:00.000Z","acc":"O60741","name":"Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1","length":890,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI00001AED69","genes":[{"name":{"value":"HCN1"},"synonyms":[{"value":"BCNG1"}]}],"alphafold_very_low_content":0.3775280898876405,"disorder_content":0.10449438202247191,"disprot_consensus":{"full":[{"start":1,"end":93,"type":"D"}],"Structural state":[{"start":1,"end":93,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03165","name":"MH1 domain","start":41,"end":171},{"id":"PF03166","name":"MH2 domain","start":273,"end":443}],"gene3D":[{"start":265,"end":467,"id":"2.60.200.10","name":"2.60.200.10"}]},"uniref50":"UniRef50_Q15796","sequence":"MSSILPFTPPVVKRLLGWKKSAGGSGGAGGGEQNGQEEKWCEKAVKSLVKKLKKTGRLDELEKAITTQNCNTKCVTIPSTCSEIWGLSTPNTIDQWDTTGLYSFSEQTRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELKAIENCEYAFNLKKDEVCVNPYHYQRVETPVLPPVLVPRHTEILTELPPLDDYTHSIPENTNFPAGIEPQSNYIPETPPPGYISEDGETSDQQLNQSMDTGSPAELSPTTLSPVNHSLDLQPVTYSEPAFWCSIAYYELNQRVGETFHASQPSLTVDGFTDPSNSERFCLGLLSNVNRNATVEMTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSVRCSSMS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q15796","disprot_id":"DP01319","ncbi_taxon_id":9606,"regions_counter":10,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":264,"region_id":"DP01319r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of a phosphorylated Smad2. Recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-beta signaling. <i> Wu JW, Hu M, Chai J, Seoane J, Huse M, Li C, Rigotti DJ, Kyin S, Muir TW, Fairman R, Massagué J, Shi Y. </i> Mol Cell, 2001","statement":[{"text":"The N-terminal 24 residues are disordered in the crystals.","type":"Methods"},{"text":"The N-terminal 24 residues are disordered in the crystals correspond to the UniProt region 241-264.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":241,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1KHX"}],"reference_id":"11779503","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T16:28:12.694Z"}},{"start":457,"end":467,"reference_id":"10615055","reference_source":"pmid","reference_html":"Structural basis of Smad2 recognition by the Smad anchor for receptor activation. <i> Wu G, Chen YG, Ozdamar B, Gyuricza CA, Chong PA, Wrana JL, Massagué J, Shi Y. </i> Science, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"region_id":"DP01319r004","statement":[{"text":"The final refined model contains two complexes of Smad2 (residues 263–456) and SARA (residues 669–709), and 243 water molecules. The NH2- and COOH-terminal residues in Smad2 have no electron density, and we presume that these regions are disordered in the crystals.","type":"Methods"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T16:25:27.087Z"}},{"start":457,"end":467,"reference_id":"10615055","reference_source":"pmid","reference_html":"Structural basis of Smad2 recognition by the Smad anchor for receptor activation. <i> Wu G, Chen YG, Ozdamar B, Gyuricza CA, Chong PA, Wrana JL, Massagué J, Shi Y. </i> Science, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01319r005","statement":[{"text":"Compared to the unphosphorylated Smad2 (Wu et al., 2000), the N-terminal extension adopts a different conformation and is more than 12 Å away, whereas the previously flexible C terminus becomes well ordered after phosphorylation (Figure 2B).","type":"Results"},{"text":"Structural comparison of the phosphorylated (green) and unphosphorylated (gold) Smad2-MH2 (PDB code 1DEV). The differences are apparent in two locations; the N-terminal extensions are more than 12 Å apart, and the flexible C terminus in the unphosphorylated Smad2 becomes rigid and ordered upon phosphorylation.","type":"Figure"}],"cross_refs":[{"db":"PDB","id":"1DEV"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T16:25:37.698Z"}},{"start":463,"end":467,"reference_id":"10615055","reference_source":"pmid","reference_html":"Structural basis of Smad2 recognition by the Smad anchor for receptor activation. <i> Wu G, Chen YG, Ozdamar B, Gyuricza CA, Chong PA, Wrana JL, Massagué J, Shi Y. </i> Science, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1DEV"}],"region_id":"DP01319r006","statement":[{"text":"To reveal the structural basis of phosphorylation-induced homotrimerization, we crystallized a Smad2-MH2 fragment (residues 241–467) with Ser465 and Ser467 homogeneously phosphorylated.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T16:13:35.652Z"}},{"start":463,"end":467,"reference_id":"10615055","reference_source":"pmid","reference_html":"Structural basis of Smad2 recognition by the Smad anchor for receptor activation. <i> Wu G, Chen YG, Ozdamar B, Gyuricza CA, Chong PA, Wrana JL, Massagué J, Shi Y. </i> Science, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"1DEV"}],"region_id":"DP01319r007","statement":[{"text":"The phosphorylated Smad2 forms a symmetric homotrimer, with both the phosphorylated C terminus and the N-terminal extension from one MH2 domain reaching out to interact with an adjacent domain (Figure 2C).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T16:25:48.131Z"}},{"start":18,"end":33,"reference_id":"31582430","reference_source":"pmid","reference_html":"Structural basis for distinct roles of SMAD2 and SMAD3 in FOXH1 pioneer-directed TGF-β signaling. <i> Aragón E, Wang Q, Zou Y, Morgani SM, Ruiz L, Kaczmarska Z, Su J, Torner C, Tian L, Hu J, Shu W, Agrawal S, Gomes T, Márquez JA, Hadjantonakis AK, Macias MJ, Massagué J. </i> Genes Dev, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"BMRB","id":"27742"}],"region_id":"DP01319r008","statement":[{"text":"The flexibility of this loop was confirmed by low 1H,15N heteronuclear NOE values (Supplemental Fig. S3A) and by the presence of partially overlapped amides as indicated in the 1H-15N HSQC (Fig. 1D; Supplemental Fig. S1D).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T16:27:18.520Z"}},{"start":18,"end":33,"reference_id":"31582430","reference_source":"pmid","reference_html":"Structural basis for distinct roles of SMAD2 and SMAD3 in FOXH1 pioneer-directed TGF-β signaling. <i> Aragón E, Wang Q, Zou Y, Morgani SM, Ruiz L, Kaczmarska Z, Su J, Torner C, Tian L, Hu J, Shu W, Agrawal S, Gomes T, Márquez JA, Hadjantonakis AK, Macias MJ, Massagué J. </i> Genes Dev, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"region_id":"DP01319r009","statement":[{"text":"The loop connecting the α1 and α2 helices (G-loop, Supplemental Fig. S1A), was excluded in the refined model because it is not well defined in the electron density map.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T16:27:28.263Z"}},{"start":18,"end":33,"reference_id":"31582430","reference_source":"pmid","reference_html":"Structural basis for distinct roles of SMAD2 and SMAD3 in FOXH1 pioneer-directed TGF-β signaling. <i> Aragón E, Wang Q, Zou Y, Morgani SM, Ruiz L, Kaczmarska Z, Su J, Torner C, Tian L, Hu J, Shu W, Agrawal S, Gomes T, Márquez JA, Hadjantonakis AK, Macias MJ, Massagué J. </i> Genes Dev, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01319r010","statement":[{"text":"The SAXS data also supports the conformational variability sampled by the G-loop, in agreement with the faster motions detected by NMR, with heteronuclear NOE values below 0.3 (Fig. 3B; Supplemental Fig. S3B).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T16:27:25.066Z"}}],"released":"2018_11","uniref100":"UniRef100_Q15796","date":"2018-07-05T21:39:21.000Z","acc":"Q15796","name":"Mothers against decapentaplegic homolog 2","length":467,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI0000032EE7","genes":[{"name":{"value":"SMAD2"},"synonyms":[{"value":"MADH2"},{"value":"MADR2"}]}],"alphafold_very_low_content":0.25267665952890794,"disorder_content":0.10920770877944326,"disprot_consensus":{"full":[{"start":18,"end":33,"type":"D"},{"start":241,"end":264,"type":"D"},{"start":457,"end":467,"type":"T"}],"Structural state":[{"start":18,"end":33,"type":"D"},{"start":241,"end":264,"type":"D"},{"start":457,"end":467,"type":"D"}],"Structural transition":[{"start":457,"end":467,"type":"T"}],"Disorder function":[{"start":463,"end":467,"type":"F"}],"Molecular function":[{"start":463,"end":467,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05093","name":"Cytokine-induced anti-apoptosis inhibitor 1, Fe-S biogenesis","start":247,"end":341},{"id":"PF16803","name":"Fe-S cluster assembly protein DRE2 N-terminus","start":6,"end":131}],"gene3D":[{"start":1,"end":133,"id":"3.40.50.11000","name":"Fe-S cluster assembly protein Dre2, N-terminal domain"}]},"uniref50":"UniRef50_Q6CJS8","sequence":"MSQYKTGLLLIHPAVTTTPELVENTKAQAASKKVKFVDQFLINKLNDGSITLENAKYETVHYLTPEAQTDIKFPKKLISVLADSLKPNGSLIGLSDIYKVDALINGFEIINEPDYCWIKMDSSKLNQTVSIPLKKKKTNNTKLQSGSKLPTFKKASSSTSNLPSFKKADHSRQPIVKETDSFKPPSFKMTTEPKVYRVVDDLIEDSDDDDFSSDSSKAQYFDQVDTSDDSIEEEELIDEDGSGKSMITMITCGKSKTKKKKACKDCTCGMKEQEENEINDIRSQQDKVVKFTEDELTEIDFTIDGKKVGGCGSCSLGDAFRCSGCPYLGLPAFKPGQPINLDSISDDL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_B3LRE5","disprot_id":"DP01320","ncbi_taxon_id":559292,"regions_counter":2,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":348,"region_id":"DP01320r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"A S-adenosylmethionine methyltransferase-like domain within the essential, Fe-S-containing yeast protein Dre2. <i> Soler N, Craescu CT, Gallay J, Frapart YM, Mansuy D, Raynal B, Baldacci G, Pastore A, Huang ME, Vernis L. </i> FEBS J, 2012","statement":[{"text":"CD, NMR and fluorescence data confirm the in silico predictions and show that the N-terminus of Dre2 [Dre2 (1–133)] is a stably-folded domain, whereas the C-terminus is intrinsically unstructured, and contains eight cysteines that coordinate the Fe-S clusters.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":234,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22487307","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":348,"term_name":"molecular adaptor activity","start":234,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"A tight interaction between the Fe-S-containing Dre2-C-terminus and the two FMN-binding and FAD-binding domains from the reductase Tah18 is essential for yeast viability.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"22487307","version":3,"reference_html":"A S-adenosylmethionine methyltransferase-like domain within the essential, Fe-S-containing yeast protein Dre2. <i> Soler N, Craescu CT, Gallay J, Frapart YM, Mansuy D, Raynal B, Baldacci G, Pastore A, Huang ME, Vernis L. </i> FEBS J, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006204","region_id":"DP01320r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_C7GX69","date":"2018-07-06T08:38:10.000Z","acc":"P36152","name":"Fe-S cluster assembly protein DRE2","length":348,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000052EB8","genes":[{"name":{"value":"DRE2","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03115","url":"https://hamap.expasy.org/unirule/MF_03115"}}]},"olnNames":[{"value":"YKR071C"}]}],"alphafold_very_low_content":0.1235632183908046,"disorder_content":0.33045977011494254,"disprot_consensus":{"full":[{"start":234,"end":348,"type":"D"}],"Structural state":[{"start":234,"end":348,"type":"D"}],"Molecular function":[{"start":234,"end":348,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02986","name":"Fibronectin binding repeat","start":403,"end":437},{"id":"PF02986","name":"Fibronectin binding repeat","start":439,"end":474},{"id":"PF02986","name":"Fibronectin binding repeat","start":476,"end":511},{"id":"PF02986","name":"Fibronectin binding repeat","start":513,"end":548},{"id":"PF02986","name":"Fibronectin binding repeat","start":550,"end":585},{"id":"PF08341","name":"Thioester domain","start":95,"end":200}],"gene3D":[{"start":55,"end":262,"id":"2.30.30.670","name":"Thioester domain"},{"start":131,"end":234,"id":"1.10.150.480","name":"1.10.150.480"}]},"uniref50":"UniRef50_A0A7G7GPD4","sequence":"MNNKMFLNKEAGFLAHTKRKRRFAVTLVGVFFMLLASAGAIGFGQVAYAADEKTVPHRVSQNPEFPWYGYDFYKGPYTRYHNLQLNLNGSKTYQAYCFNLKRFEPKKEGSYFPNWYKRWDGSEETFVKYADNPRKDNESSRVIDVELEKNILRVLYNGYPNNGNGIMEGLEPLNAILVTQNAVWYYSDNSSIFNTDNFFTTEAKDLNIKPEQLSLMRVALKKLIDPKLSEESLKPVPSTFRLNIFESQDKLYQNLLSAEFVPENPPKPGETPEHGPKTPELDGTPIPEGPQRPNESLEPTLPPVMLDGQEVPEVPSESLEPALPPLMPELDGQEVPEVPSESLEPALPPLMPELDGQEVPEKPSVDLPIEDPRYEFNNKDQSPLAGESGETEYITEVYGNQQNPVDIDKKLPNETGFSGNMVETEDTKEPGVLMGGQSESVEFTKDTQTGMSGQTTPQVETEDTKEPGVLMGGQSESVEFTKDTQTGMSGQTASQVETEDTKEPGVLMGGQSESVEFTKDTQTGMSGQTTPQVETEDTKEPGVLMGGQSESVEFTKDTQTGMSGFSETVTIVEDTRPKLVFHFDNNEPKVEENREKPTKNITPILPATGDIENVLAFLGILILSVLPIFSLLKKQTKQ","taxonomy":["Bacteria","Firmicutes","Bacilli","Lactobacillales","Streptococcaceae","Streptococcus"],"uniref90":"UniRef90_Q01924","disprot_id":"DP01322","ncbi_taxon_id":1314,"regions_counter":2,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":591,"region_id":"DP01322r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Pathogenic bacteria attach to human fibronectin through a tandem beta-zipper. <i> Schwarz-Linek U, Werner JM, Pickford AR, Gurusiddappa S, Kim JH, Pilka ES, Briggs JA, Gough TS, Höök M, Campbell ID, Potts JR. </i> Nature, 2003","statement":[{"text":"Fibronectin-binding proteins (FnBPs), anchored in the bacterial cell wall, have multiple Fn-binding repeats in an unfolded region of the protein","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":396,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"12736686","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":591,"term_name":"order to disorder","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Pathogenic bacteria attach to human fibronectin through a tandem beta-zipper. <i> Schwarz-Linek U, Werner JM, Pickford AR, Gurusiddappa S, Kim JH, Pilka ES, Briggs JA, Gough TS, Höök M, Campbell ID, Potts JR. </i> Nature, 2003","statement":[{"text":"As well as showing how pathogenic bacteria can adhere to F1 modules in 1–5 F1 of Fn, the consequences of the mechanism, namely the high affinity and specificity of the binding, the significant conformational change undergone by the unfolded region of the FnBP and the presence of multiple Fn-binding sites, are all likely to have a role in bacterial invasion","type":"Results"}],"term_id":"IDPO:0000014","curator_id":"amonzon","start":396,"term_ontology":"IDPO","curator_name":"Alex Monzon","reference_id":"12736686","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01322r002","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_Q01924","date":"2018-07-06T20:34:22.000Z","acc":"Q01924","name":"Fibronectin-binding protein","length":638,"organism":"Streptococcus pyogenes","dataset":[],"UniParc":"UPI00000B9D5E","genes":[{"name":{"value":"Sfb","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAA48133.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA48133.1"}}]}}],"alphafold_very_low_content":0.6520376175548589,"disorder_content":0.3072100313479624,"disprot_consensus":{"full":[{"start":396,"end":591,"type":"T"}],"Structural state":[{"start":396,"end":591,"type":"D"}],"Structural transition":[{"start":396,"end":591,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00505","name":"HMG (high mobility group) box","start":437,"end":500},{"id":"PF08517","name":"Ataxin-1 and HBP1 module (AXH)","start":215,"end":339}],"gene3D":[{"start":420,"end":505,"id":"1.10.30.10","name":"High mobility group box domain"}]},"uniref50":"UniRef50_Q8R316","sequence":"MVWEVKTNQMPNAVQKLLLVMDKRAPGMSDSLELLQCNENLPSSPGYNSCDEHMELDDLPELQAVQSDPTQSAIYQLSSDVSHQEYPRSSWSQNTSDIPENTHREDEVDWLTELANIATSPQSPLMQCSFYNRSSPVHIIATSKSLHSYARPPPVSSSSKSGPAFPHDHWKEETPVRHERANSESESGIFCMSSLSDDDDLGWCNSWPSTIWHCFLKGTRLCFHKESNKEWQDVEDFARAASCDNEEEIQMGTHKGYGSDGLKLLSHEESVSFGESVLKLTFDPGTVEDGLLTVECKLDHPFYVKNKGWSSFYPSLTVVQHGIPCCEIHIGDVCLPPGHPDAINFDDSGVFDTFKSYDFTPMDSSAVYVLSSMARQRRASLSCGGGPGTGQEFSGSEFSKSCGSPGSSQLSSSSLYAKAVKSHSSGTVSATSPNKCKRPMNAFMLFAKKYRVEYTQMYPGKDNRAISVILGDRWKKMKNEERRMYTLEAKALAEEQKRLNPDCWKRKRTNSGSQQH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q8R316","disprot_id":"DP01323","ncbi_taxon_id":10090,"regions_counter":8,"creator":"amonzon","regions":[{"region_id":"DP01323r001","ec_ontology":"ECO","end":255,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":242,"version":3,"statement":[{"text":"An additional triple-stranded β sheet is made of two antiparallel strands (β6 and β7), and a third strand (β8) that runs parallel to β7. α1 packs against β1 and β2 and is followed by a long unstructured region of 13 amino acids (residues 242–255), whereas α2 packs against β7 and β8.","type":"Results"},{"text":"An additional triple-stranded β sheet is made of two antiparallel strands (β6 and β7), and a third strand (β8) that runs parallel to β7. α1 packs against β1 and β2 and is followed by a long unstructured region of 13 amino acids (residues 242–255), whereas α2 packs against β7 and β8.","type":"Results"}],"term_name":"disorder","reference_html":"The AXH domain adopts alternative folds the solution structure of HBP1 AXH. <i> de Chiara C, Menon RP, Adinolfi S, de Boer J, Ktistaki E, Kelly G, Calder L, Kioussis D, Pastore A. </i> Structure, 2005","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15893665","date":"2023-08-28T15:02:19.918Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1V06"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":358,"end":380,"reference_id":"15235594","reference_source":"pmid","reference_html":"HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations. <i> Swanson KA, Knoepfler PS, Huang K, Kang RS, Cowley SM, Laherty CD, Eisenman RN, Radhakrishnan I. </i> Nat Struct Mol Biol, 2004","date":"2023-08-28T14:51:09.052Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006200","ec_ontology":"ECO","ec_name":"circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01323r004","statement":[{"text":"Like Mad1 SID, the circular dichroism spectrum of unbound HBP1 SID is characterized by the absence of stable secondary structure (data not shown).","type":"Results"}]},{"start":366,"end":376,"reference_id":"15235594","reference_source":"pmid","reference_html":"HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations. <i> Swanson KA, Knoepfler PS, Huang K, Kang RS, Cowley SM, Laherty CD, Eisenman RN, Radhakrishnan I. </i> Nat Struct Mol Biol, 2004","date":"2023-08-28T14:53:47.347Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01323r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q60520"}],"statement":[{"text":"In the complex, however, HBP1 SID forms an amphipathic helix (αA) that extends from Ala366 to Gln376. The regions preceding and following the helix in the NMR structure are poorly defined, most likely owing to a lack of experimental restraints and/or enhanced flexibility (Fig. 4a).","type":"Results"}],"cross_refs":[{"db":"PDB","id":"1S5R"}],"states_connection":[{"source":"DP01323r004","target":"DP01323r006"}]},{"start":366,"end":376,"reference_id":"15235594","reference_source":"pmid","reference_html":"HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations. <i> Swanson KA, Knoepfler PS, Huang K, Kang RS, Cowley SM, Laherty CD, Eisenman RN, Radhakrishnan I. </i> Nat Struct Mol Biol, 2004","date":"2023-08-28T14:53:57.294Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01323r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q60520"}],"statement":[{"text":"In the complex, however, HBP1 SID forms an amphipathic helix (αA) that extends from Ala366 to Gln376. The regions preceding and following the helix in the NMR structure are poorly defined, most likely owing to a lack of experimental restraints and/or enhanced flexibility (Fig. 4a).","type":"Results"}],"cross_refs":[{"db":"PDB","id":"1S5R"}]},{"start":366,"end":376,"reference_id":"15235594","reference_source":"pmid","reference_html":"HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations. <i> Swanson KA, Knoepfler PS, Huang K, Kang RS, Cowley SM, Laherty CD, Eisenman RN, Radhakrishnan I. </i> Nat Struct Mol Biol, 2004","date":"2023-08-28T14:55:19.703Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1S5R"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q60520","operator":null,"partner_start":295,"partner_end":383}],"region_id":"DP01323r007","statement":[{"text":"In the complex, however, HBP1 SID forms an amphipathic helix (αA) that extends from Ala366 to Gln376. The regions preceding and following the helix in the NMR structure are poorly defined, most likely owing to a lack of experimental restraints and/or enhanced flexibility (Fig. 4a).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":358,"end":380,"reference_id":"15235594","reference_source":"pmid","reference_html":"HBP1 and Mad1 repressors bind the Sin3 corepressor PAH2 domain with opposite helical orientations. <i> Swanson KA, Knoepfler PS, Huang K, Kang RS, Cowley SM, Laherty CD, Eisenman RN, Radhakrishnan I. </i> Nat Struct Mol Biol, 2004","date":"2023-08-28T14:58:48.624Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q60520","operator":null,"partner_start":295,"partner_end":383}],"region_id":"DP01323r008","statement":[{"text":"We therefore synthesized a peptide corresponding to HBP1 residues 358–380 (henceforth designated HBP1 SID) and assayed for binding to mSin3A PAH2 using isothermal titration calorimetry (ITC). The HBP1 SID peptide bound mSin3A PAH2 with moderate affinity (Kd = 5.2 ± 1.0 μM) and 1:1 stoichiometry (Supplementary Fig. 1 online). A His6-tagged HBP1 construct spanning residues 342–398 also bound mSin3A PAH2 with a similar affinity, implying that the principal affinity determinants for the Sin3 interaction resided within HBP1 residues 358–380.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_Q8R316","date":"2018-07-07T20:58:48.000Z","acc":"Q8R316","name":"HMG box-containing protein 1","length":516,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000280FB","genes":[{"name":{"value":"Hbp1"}}],"alphafold_very_low_content":0.4786821705426357,"disorder_content":0.07170542635658915,"disprot_consensus":{"full":[{"start":242,"end":255,"type":"D"},{"start":358,"end":365,"type":"D"},{"start":366,"end":376,"type":"T"},{"start":377,"end":380,"type":"D"}],"Structural state":[{"start":242,"end":255,"type":"D"},{"start":358,"end":380,"type":"D"}],"Structural transition":[{"start":366,"end":376,"type":"T"}],"Molecular function":[{"start":358,"end":380,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":1762,"end":1825},{"id":"PF00627","name":"UBA/TS-N domain","start":1151,"end":1180},{"id":"PF10427","name":"Argonaute hook","start":1035,"end":1148},{"id":"PF12938","name":"M domain of GW182","start":1227,"end":1455},{"id":"PF16608","name":"TNRC6-PABC binding domain","start":1465,"end":1758}],"gene3D":[{"start":1508,"end":1595,"id":"3.30.70.330","name":"3.30.70.330"},{"start":921,"end":1000,"id":"1.10.8.10","name":"DNA helicase RuvA subunit, C-terminal domain"}]},"uniref50":"UniRef50_Q9HCJ0","sequence":"MEEKKKKKQEEKKKKEGAQKKAADQKTKVPEPTKTCSSQPQPAGTSTSTSTSTISSSNNGKRASASGQQPAASRYLPREVPPRFRQQEQKQLLKRGQPLPTGTLTSVSPTQGAGPAGVSPPPLPGAGTQHHPSKLQPDLSHSGLADHYENSHWGQQPTYRSEANCSWDKVIIDRTDKEAWPSITGTETESASECTTDTDSASNCGSENSSMATGSAQGNFTGHTKKTNGNNGTNGALVQSPSNQSALGAGGANSNGSAARVWGVATGSSSGLAHCSVSGGDGKMDTMIGDGRSQNCWGASNSNAGINLNLNPNANPAAWPVLGHEGTVATGNPSSICSPVSAIGQNMGNQNGNPTGTLGAWGNLLPQESTEPQTSTSQNVSFSAQPQNLNTDGPNNTNPMNSSPNPINAMQTNGLPNWGMAVGMGAIIPPHLQGLPGANGSSVSQVSGGSAEGISNSVWGLSPGNPATGNSNSGFSQGNGDTVNSALSAKQNGSSSAVQKEGSGGNAWDSGPPAGPGILAWGRGSGNNGVGNIHSGAWGHPSRSTSNGVNGEWGKPPNQHSNSDINGKGSTGWESPSVTSQNPTVQPGGEHMNSWAKAASSGTTASEGSSDGSGNHNEGSTGREGTGEGRRRDKGIIDQGHIQLPRNDLDPRVLSNTGWGQTPVKQNTAWEFEESPRSERKNDNGTEAWGCAATQASNSGGKNDGSIMNSTNTSSVSGWVNAPPAAVPANTGWGDSNNKAPSGPGVWGDSISSTAVSTAAAAKSGHAWSGAANQEDKSPTWGEPPKPKSQHWGDGQRSNPAWSAGGGDWADSSSVLGHLGDGKKNGSGWDADSNRSGSGWNDTTRSGNSGWGNSTNTKANPGTNWGETLKPGPQQNWASKPQDNNVSNWGGAASVKQTGTGWIGGPVPVKQKDSSEATGWEEPSPPSIRRKMEIDDGTSAWGDPSNYNNKTVNMWDRNNPVIQSSTTTNTTTTTTTTTSNTTHRVETPPPHQAGTQLNRSPLLGPVSSGWGEMPNVHSKTENSWGEPSSPSTLVDNGTAAWGKPPSSGSGWGDHPAEPPVAFGRAGAPVAASALCKPASKSMQEGWGSGGDEMNLSTSQWEDEEGDVWNNAASQESTSSCSSWGNAPKKGLQKGMKTSGKQDEAWIMSRLIKQLTDMGFPREPAEEALKSNNMNLDQAMSALLEKKVDVDKRGLGVTDHNGMAAKPLGCRPPISKESSVDRPTFLDKDGGLVEEPTPSPFLPSPSLKLPLSHSALPSQALGGIASGLGMQNLNSSRQIPSGNLGMFGNSGAAQARTMQQPPQPPVQPLNSSQPSLRAQVPQFLSPQVQAQLLQFAAKNIGLNPALLTSPINPQHMTMLNQLYQLQLAYQRLQIQQQMLQAQRNVSGSMRQQEQQVARTITNLQQQIQQHQRQLAQALLVKQPPPPPPPPHLSLHPSAGKSAMDSFPSHPQTPGLPDLQTKEQQSSPNTFAPYPLAGLNPNMNVNSMDMTGGLSVKDPSQSQSRLPQWTHPNSMDNLPSAASPLEQNPSKHGAIPGGLSIGPPGKSSIDDSYGRYDLIQNSESPASPPVAVPHSWSRAKSDSDKISNGSSINWPPEFHPGVPWKGLQNIDPENDPDVTPGSVPTGPTINTTIQDVNRYLLKSGGSSPPSSQNATLPSSSAWPLSASGYSSSFSSIASAPSVAGKLSDIKSTWSSGPTSHTQASLSHELWKVPRNSTAPTRPPPGLTNPKPSSTWGASPLGWTSSYSSGSAWSTDTSGRTSSWLVLRNLTPQIDGSTLRTLCLQHGPLITFHLNLTQGNAVVRYSSKEEAAKAQKSLHMCVLGNTTILAEFAGEEEVNRFLAQGQALPPTSSWQSSSASSQPRLSAAGSSHGLVRSDAGHWNAPCLGGKGSSELLWGGVPQYSSSLWGPPSADDSRVIGSPTPLTTLLPGDLLSGESL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9HCJ0","disprot_id":"DP01324","ncbi_taxon_id":9606,"regions_counter":8,"creator":"amonzon","regions":[{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1606,"term_name":"protein binding","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural insights into the human GW182-PABC interaction in microRNA-mediated deadenylation. <i> Jinek M, Fabian MR, Coyle SM, Sonenberg N, Doudna JA. </i> Nat Struct Mol Biol, 2010","term_id":"GO:0005515","curator_id":"vnugnes","start":1592,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"20098421","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-04T18:14:24.994Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01324r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P11940","operator":"and","partner_start":null,"partner_end":null}],"statement":[{"text":"Here we show that a conserved motif in the human GW182 paralog TNRC6C interacts with the C-terminal domain of polyadenylate binding protein 1 (PABC) and present the crystal structure of the complex.","type":"Abstract"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1608,"region_id":"DP01324r003","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Structural basis of binding of P-body-associated proteins GW182 and ataxin-2 by the Mlle domain of poly(A)-binding protein. <i> Kozlov G, Safaee N, Rosenauer A, Gehring K. </i> J Biol Chem, 2010","statement":[{"text":"1H-15N heteronuclear single quantum correlation spectra of the DUF region showed limited dispersion of signals, which confirms that the peptide is unfolded prior to Mlle binding (supplemental Fig. S1).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1587,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-04T18:06:07.155Z","reference_source":"pmid","term_name":"disorder","reference_id":"20181956","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1606,"term_name":"protein binding","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural basis of binding of P-body-associated proteins GW182 and ataxin-2 by the Mlle domain of poly(A)-binding protein. <i> Kozlov G, Safaee N, Rosenauer A, Gehring K. </i> J Biol Chem, 2010","term_id":"GO:0005515","curator_id":"vnugnes","start":1591,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"20181956","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-04T18:09:17.904Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01324r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"3KTP"}],"interaction_partner":[{"db":"UniProt","id":"P11940","operator":"and","partner_start":null,"partner_end":null}],"statement":[{"text":"Helices α2 and α3 and a small part of helix α5 participate in peptide binding. The electron density map showed the GW182 peptide from residues Asn1384 to Gln1399.","type":"Results"}]},{"start":1591,"end":1606,"reference_id":"20181956","reference_source":"pmid","reference_html":"Structural basis of binding of P-body-associated proteins GW182 and ataxin-2 by the Mlle domain of poly(A)-binding protein. <i> Kozlov G, Safaee N, Rosenauer A, Gehring K. </i> J Biol Chem, 2010","date":"2023-05-04T18:09:11.732Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P11940","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01324r005","statement":[{"text":"Titration of the 15N-labeled peptide with the Mlle domain produced large chemical shift changes, indicating that the peptide becomes structured upon Mlle binding.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1591,"end":1606,"reference_id":"20181956","reference_source":"pmid","reference_html":"Structural basis of binding of P-body-associated proteins GW182 and ataxin-2 by the Mlle domain of poly(A)-binding protein. <i> Kozlov G, Safaee N, Rosenauer A, Gehring K. </i> J Biol Chem, 2010","date":"2023-05-04T18:08:38.455Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP01324r006","statement":[{"text":" Titration of the 15N-labeled peptide with the Mlle domain produced large chemical shift changes, indicating that the peptide becomes structured upon Mlle binding.","type":"Results"}]},{"start":1591,"end":1606,"reference_id":"20181956","reference_source":"pmid","reference_html":"Structural basis of binding of P-body-associated proteins GW182 and ataxin-2 by the Mlle domain of poly(A)-binding protein. <i> Kozlov G, Safaee N, Rosenauer A, Gehring K. </i> J Biol Chem, 2010","date":"2023-05-04T18:09:05.136Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3KTP"}],"region_id":"DP01324r007","statement":[{"text":"Helices α2 and α3 and a small part of helix α5 participate in peptide binding. The electron density map showed the GW182 peptide from residues Asn1384 to Gln1399.","type":"Results"}]},{"start":1591,"end":1606,"reference_id":"20181956","reference_source":"pmid","reference_html":"Structural basis of binding of P-body-associated proteins GW182 and ataxin-2 by the Mlle domain of poly(A)-binding protein. <i> Kozlov G, Safaee N, Rosenauer A, Gehring K. </i> J Biol Chem, 2010","date":"2023-05-04T18:10:56.597Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P11940","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01324r008","statement":[{"text":"The affinity of the wild-type GW182-(1380–1401) peptide measured by ITC was 6 μm (Fig. 2a). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_Q9HCJ0","date":"2018-07-07T22:53:23.000Z","acc":"Q9HCJ0","name":"Trinucleotide repeat-containing gene 6C protein","length":1936,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI000052BFDB","genes":[{"name":{"value":"TNRC6C"},"synonyms":[{"value":"KIAA1582"}]}],"alphafold_very_low_content":0.8579881656804734,"disorder_content":0.011363636363636364,"disprot_consensus":{"full":[{"start":1587,"end":1590,"type":"D"},{"start":1591,"end":1606,"type":"T"},{"start":1607,"end":1608,"type":"D"}],"Structural state":[{"start":1587,"end":1608,"type":"D"}],"Molecular function":[{"start":1591,"end":1606,"type":"F"}],"Structural transition":[{"start":1591,"end":1606,"type":"T"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MIKRFLEDTTDDGELSKFVKDFSGNASCHPPEAKTWASRPQVPEPRPQAPDLYDDDLEFRPPSRPQSSDNQQYFCAPAPLSPSARPRSPWGKLDPYDSSEDDKEYVGFATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVNSLFLTDLYRDRKLLGAEERIMQTVEITKHAVDIEEKGVRLRLTIVDTPGFGDAVNNTECWKPVAEYIDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGYGPSLRLLAPPGAVKGTGQEHQGQGCH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"","disprot_id":"DP01325","ncbi_taxon_id":9606,"regions_counter":4,"creator":"mguha","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":274,"region_id":"DP01325r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Mechanism of the interaction between the intrinsically disordered C-terminus of the pro-apoptotic ARTS protein and the Bir3 domain of XIAP. <i> Reingewertz TH, Shalev DE, Sukenik S, Blatt O, Rotem-Bamberger S, Lebendiker M, Larisch S, Friedler A. </i> PLoS One, 2011","statement":[{"text":"The 1H-NMR spectra of ARTS CTD showed a narrow dispersion of amide resonances. This pattern implies a random coil conformation and is characteristic of disordered regions and peptides.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mguha","start":248,"term_ontology":"IDPO","curator_name":"Mainak Guharoy","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21949740","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":274,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Mechanism of the interaction between the intrinsically disordered C-terminus of the pro-apoptotic ARTS protein and the Bir3 domain of XIAP. <i> Reingewertz TH, Shalev DE, Sukenik S, Blatt O, Rotem-Bamberger S, Lebendiker M, Larisch S, Friedler A. </i> PLoS One, 2011","statement":[{"text":"We showed that the nine C-terminal residues (266-274) of the proapoptotic ARTS protein mediate its interaction with the Bir3 domain of XIAP.","type":"Discussion"}],"term_id":"GO:0005515","curator_id":"mguha","start":248,"term_ontology":"GO","curator_name":"Mainak Guharoy","reference_id":"21949740","version":3,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01325r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":274,"region_id":"DP01325r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Mechanism of the interaction between the intrinsically disordered C-terminus of the pro-apoptotic ARTS protein and the Bir3 domain of XIAP. <i> Reingewertz TH, Shalev DE, Sukenik S, Blatt O, Rotem-Bamberger S, Lebendiker M, Larisch S, Friedler A. </i> PLoS One, 2011","statement":[{"text":"The far-UV CD spectrum of ARTS C-terminal domain (CTD) is composed largely of a minimum at 200 nm and is missing the typical signatures of secondary structures, indicating mainly a random coil. This is a characteristic pattern for disordered regions.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mguha","start":248,"term_ontology":"IDPO","curator_name":"Mainak Guharoy","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21949740","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":274,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Mechanism of the interaction between the intrinsically disordered C-terminus of the pro-apoptotic ARTS protein and the Bir3 domain of XIAP. <i> Reingewertz TH, Shalev DE, Sukenik S, Blatt O, Rotem-Bamberger S, Lebendiker M, Larisch S, Friedler A. </i> PLoS One, 2011","statement":[{"text":"We showed that the nine C-terminal residues (266-274) of the proapoptotic ARTS protein mediate its interaction with the Bir3 domain of XIAP.","type":"Discussion"}],"term_id":"GO:0005515","curator_id":"mguha","start":248,"term_ontology":"GO","curator_name":"Mainak Guharoy","reference_id":"21949740","version":3,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01325r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"","date":"2018-07-08T13:57:34.000Z","acc":"O43236-6","name":"Isoform ARTS of Septin-4","length":274,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000003FD93","genes":[{"name":{"value":"SEPTIN4","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9165","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9165"}}]},"synonyms":[{"value":"C17orf47","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9165","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9165"}}]},{"value":"PNUTL2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9889007","url":"http://www.ncbi.nlm.nih.gov/pubmed/9889007","alternativeUrl":"https://europepmc.org/abstract/MED/9889007"}}]},{"value":"SEP4","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9165","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9165"}}]},{"value":"SEPT4","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9165","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9165"}}]}],"orfNames":[{"value":"hucep-7"}]}],"disorder_content":0.09854014598540146,"disprot_consensus":{"full":[{"start":248,"end":274,"type":"D"}],"Structural state":[{"start":248,"end":274,"type":"D"}],"Molecular function":[{"start":248,"end":274,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03416","name":"Peptidase C54 catalytic domain","start":40,"end":335},{"id":"PF20166","name":"ATG4, F-type LIR motif","start":363,"end":391}]},"uniref50":"UniRef50_Q9Y4P1","sequence":"MDAATLTYDTLRFAEFEDFPETSEPVWILGRKYSIFTEKDEILSDVASRLWFTYRKNFPAIGGTGPTSDTGWGCMLRCGQMIFAQALVCRHLGRDWRWTQRKRQPDSYFSVLNAFIDRKDSYYSIHQIAQMGVGEGKSIGQWYGPNTVAQVLKKLAVFDTWSSLAVHIAMDNTVVMEEIRRLCRTSVPCAGATAFPADSDRHCNGFPAGAEVTNRPSPWRPLVLLIPLRLGLTDINEAYVETLKHCFMMPQSLGVIGGKPNSAHYFIGYVGEELIYLDPHTTQPAVEPTDGCFIPDESFHCQHPPCRMSIAELDPSIAVGFFCKTEDDFNDWCQQVKKLSLLGGALPMFELVELQPSHLACPDVLNLSLDSSDVERLERFFDSEDEDFEILSL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9Y4P1","disprot_id":"DP01326","ncbi_taxon_id":9606,"regions_counter":10,"creator":"vsagris","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":216,"region_id":"DP01326r001","released":"2022_06","ec_id":"ECO:0006220","reference_html":"Structural basis for the specificity and catalysis of human Atg4B responsible for mammalian autophagy. <i> Sugawara K, Suzuki NN, Fujioka Y, Mizushima N, Ohsumi Y, Inagaki F. </i> J Biol Chem, 2005","statement":[{"text":"The four N-terminal residues, 16 C-terminal residues, and four loop regions corresponding to residues 190 –216, 288 –290, 343–346, and 356 –361 lacked defined electron density and were omitted from the model (Fig. 1).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":190,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-05-16T08:04:41.170Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2CY7"}],"reference_id":"16183633","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T12:25:57.243Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":392,"term_name":"protein binding","released":"2022_06","ec_name":"mutant phenotype evidence used in manual assertion","reference_html":"ATG4B contains a C-terminal LIR motif important for binding and efficient cleavage of mammalian orthologs of yeast Atg8. <i> Skytte Rasmussen M, Mouilleron S, Kumar Shrestha B, Wirth M, Lee R, Bowitz Larsen K, Abudu Princely Y, O'Reilly N, Sjøttem E, Tooze SA, Lamark T, Johansen T. </i> Autophagy, 2017","term_id":"GO:0005515","curator_id":"fquaglia","start":387,"term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"28287329","version":4,"curator_orcid":"0000-0002-0341-4888","date":"2022-05-16T08:23:43.583Z","reference_source":"pmid","ec_id":"ECO:0000315","region_id":"DP01326r003","ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"statement":[{"text":"ATG4B contains a C-terminal LIR motif important for binding and efficient cleavage of mammalian orthologs of yeast Atg8.","type":"Title"},{"text":"ATG4B contains a C-terminal LIR motif important for a strong interaction with Atg8-family orthologs","type":"Results"},{"text":"C-terminal sequences of ATG4B constructs carrying mutations affecting the C-terminal LIR motif.","type":"Figure"},{"text":"Next, a series of mutant ATG4B constructs, either deleted for the C-terminal LIR region (ΔLIRC) or carrying 2 (2mLIR) or 5 (5mLIR) point mutations affecting the motif (Fig. 1D), were in vitro translated and tested for interaction with Atg8-family orthologs fused to GST. Mutation of 2 residues in the core LIRC motif (F388A and L391A) reduced the interaction of ATG4B with LC3A, LC3B, LC3C and GABARAPL2 to 25% residual binding, and the interactions with GABARAP or GABARAPL1 to 60% (Fig. 1E and F). However, mutation of 5 residues in the LIRC region, or deletion of the LIRC motif, reduced the interactions with GABARAP and GABARAPL1 to 10% to 15% (Fig. 1E and F). The 5 point-mutations included the 3 negatively charged residues located immediately N-terminal to the core LIRC motif (Fig. 1D), in addition to the F388A and L391A mutations. In contrast to mutation of the C-terminal LIR, mutation or deletion of the N-terminal YDTL LIR (LIRN) had only a very minor effect on the interaction with LC3B or GABARAPL1 (Fig. 1G and H). Thus, we identified a LIR motif in the C terminus of ATG4B that contributed strongly to the interaction between ATG4B and Atg8-family proteins.","type":"Results"},{"text":"The C-terminal LIR motif corresponds to residues 388-391 (FEIL).","type":"Curator statement"}],"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T12:23:36.439Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":215,"region_id":"DP01326r004","released":"2022_06","ec_id":"ECO:0006220","reference_html":"The crystal structure of human Atg4b, a processing and de-conjugating enzyme for autophagosome-forming modifiers. <i> Kumanomidou T, Mizushima T, Komatsu M, Suzuki A, Tanida I, Sou YS, Ueno T, Kominami E, Tanaka K, Yamane T. </i> J Mol Biol, 2006","statement":[{"text":"The structure from residues 191 to 215, which links the auxiliary domain and protease domain, could not be constructed because of the weak electron density.","type":"Article"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":191,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-05-16T10:18:19.214Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2D1I"}],"reference_id":"16325851","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T12:25:49.820Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":217,"region_id":"DP01326r005","released":"2022_06","ec_id":"ECO:0006220","reference_html":"The structure of Atg4B-LC3 complex reveals the mechanism of LC3 processing and delipidation during autophagy. <i> Satoo K, Noda NN, Kumeta H, Fujioka Y, Mizushima N, Ohsumi Y, Inagaki F. </i> EMBO J, 2009","term_id":"IDPO:0000002","curator_id":"fquaglia","start":187,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-05-16T10:22:01.746Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2Z0E"},{"db":"PDB","id":"2ZZP"},{"db":"PDB","id":"2Z0D"}],"reference_id":"19322194","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Disordered region in ATG4B.","type":"Curator statement"}],"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T12:25:42.040Z"}},{"start":378,"end":393,"reference_id":"16183633","reference_source":"pmid","reference_html":"Structural basis for the specificity and catalysis of human Atg4B responsible for mammalian autophagy. <i> Sugawara K, Suzuki NN, Fujioka Y, Mizushima N, Ohsumi Y, Inagaki F. </i> J Biol Chem, 2005","date":"2022-05-16T08:06:20.618Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"2CY7"}],"region_id":"DP01326r006","statement":[{"text":"The four N-terminal residues, 16 C-terminal residues, and four loop regions corresponding to residues 190 –216, 288 –290, 343–346, and 356 –361 lacked defined electron density and were omitted from the model (Fig. 1).","type":"Results"}],"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T12:25:38.617Z"}},{"start":388,"end":391,"reference_id":"28287329","reference_source":"pmid","reference_html":"ATG4B contains a C-terminal LIR motif important for binding and efficient cleavage of mammalian orthologs of yeast Atg8. <i> Skytte Rasmussen M, Mouilleron S, Kumar Shrestha B, Wirth M, Lee R, Bowitz Larsen K, Abudu Princely Y, O'Reilly N, Sjøttem E, Tooze SA, Lamark T, Johansen T. </i> Autophagy, 2017","date":"2022-06-28T10:42:27.473Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007716","ec_ontology":"ECO","ec_name":"staining evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IDA","region_id":"DP01326r007","statement":[{"text":"ATG4B contains a C-terminal LIR motif important for binding and efficient cleavage of mammalian orthologs of yeast Atg8. ","type":"Title"},{"text":"ATG4B contains a C-terminal LIR motif important for a strong interaction with Atg8-family orthologs","type":"Results"},{"text":"The C-terminal LIR motif is important for the interaction of full-length ATG4B with Atg8-family orthologs. Myc-tagged ATG4B constructs were in vitro translated in the presence of [35S]methionine, and tested in GST affinity isolation experiments for binding to the indicated Atg8-family orthologs fused to GST. Bound proteins were detected by autoradiography (AR), and immobilized GST or GST-tagged proteins by Coomassie brilliant blue staining (CBB).","type":"Figure"},{"text":"The C-terminal LIR motif corresponds to residues 388-391 (FEIL).","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T12:23:10.244Z"}},{"start":388,"end":391,"reference_id":"28287329","reference_source":"pmid","reference_html":"ATG4B contains a C-terminal LIR motif important for binding and efficient cleavage of mammalian orthologs of yeast Atg8. <i> Skytte Rasmussen M, Mouilleron S, Kumar Shrestha B, Wirth M, Lee R, Bowitz Larsen K, Abudu Princely Y, O'Reilly N, Sjøttem E, Tooze SA, Lamark T, Johansen T. </i> Autophagy, 2017","date":"2022-06-28T10:42:01.521Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006170","ec_ontology":"ECO","ec_name":"quantitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IEP","region_id":"DP01326r008","statement":[{"text":"ATG4B contains a C-terminal LIR motif important for binding and efficient cleavage of mammalian orthologs of yeast Atg8. ","type":"Title"},{"text":"Strikingly, the LIR motif of ATG4B was required for stabilization of the unlipidated forms of GABARAP and GABARAPL1 in cells.","type":"Abstract"},{"text":"The LIRC motif of ATG4B is required for stabilization of GABARAP and GABARAPL1. (A) The endogenous level of GABARAP is severely diminished in cells that do not express ATG4B. Extracts of atg4b KO cells reconstituted with the indicated GFP-ATG4 constructs were analyzed by western blotting.","type":"Figure"},{"text":"Intriguingly, we observed that GABARAP and GABARAPL1 were degraded and virtually absent in cells lacking ATG4B. Consistently, the levels of these 2 proteins were highly elevated in cells overexpressing WT ATG4B. We propose that binding to ATG4B stabilizes these proteins. Without this stabilization they are rapidly degraded by the proteasome and unavailable for autophagosome formation.","type":"Discussion"},{"text":"The C-terminal LIR motif corresponds to residues 388-391 (FEIL).","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T12:22:48.687Z"}},{"start":388,"end":391,"reference_id":"28287329","reference_source":"pmid","reference_html":"ATG4B contains a C-terminal LIR motif important for binding and efficient cleavage of mammalian orthologs of yeast Atg8. <i> Skytte Rasmussen M, Mouilleron S, Kumar Shrestha B, Wirth M, Lee R, Bowitz Larsen K, Abudu Princely Y, O'Reilly N, Sjøttem E, Tooze SA, Lamark T, Johansen T. </i> Autophagy, 2017","date":"2022-06-28T10:42:14.275Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5LXI"},{"db":"PDB","id":"5LXH"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9H0R8","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01326r009","statement":[{"text":"ATG4B contains a C-terminal LIR motif important for binding and efficient cleavage of mammalian orthologs of yeast Atg8.","type":"Title"},{"text":"We solved the crystal structures of the GABARAPL1-ATG4B C-terminal LIR complex.","type":"Abstract"},{"text":"Crystal structures of the complex of GABARAPL1 with 2 LIR peptides at 1.55- and 1.75-Å resolution reveal canonical LIR-LDS interactions with important contributions from electrostatic interactions involving residues both N-terminal to, and within, the core LIR.","type":"Introduction"},{"text":"To evaluate the interaction between the C-terminal LIR-motif of ATG4B with Atg8-family proteins in more detail, we determined the X-ray structure of GABARAPL1 in complex with a peptide containing the C-terminal 10-amino acid LIRC motif of ATG4B (Fig. S1A).","type":"Results"},{"text":"The structure displays 4 additional interactions: 1) Electrostatic interactions between the acidic N-terminal LIRC residues 384Glu-Asp-Glu-Asp387 of ATG4B and the basic residues GABARAPL1 (K46), GABARAPL1 (K24), GABARAPL1 (K20) and GABARAPL1 (K48), respectively; 2) a salt bridge between ATG4B (E389) and GABARAPL1 (R67); 3) some hydrophobic interactions between ATG4B (I390) in position +2 and GABARAPL1 (L50) as well as GABARAPL1 (Y25); 4) 3 hydrogen bonds between the carbonyls of ATG4B (L391), ATG4B (S392) and the guanidinium group of GABARAPL1 (R28). Except for the C-terminal ATG4B (L393), all residues in the LIRC are contributing to the interaction.","type":"Results"},{"text":"The C-terminal LIR motif corresponds to residues 388-391 (FEIL).","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T12:22:11.676Z"}},{"start":191,"end":215,"reference_id":"16325851","reference_source":"pmid","reference_html":"The crystal structure of human Atg4b, a processing and de-conjugating enzyme for autophagosome-forming modifiers. <i> Kumanomidou T, Mizushima T, Komatsu M, Suzuki A, Tanida I, Sou YS, Ueno T, Kominami E, Tanaka K, Yamane T. </i> J Mol Biol, 2006","date":"2022-05-16T10:18:36.736Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP01326r010","statement":[{"text":"The structure from residues 191 to 215, which links the auxiliary domain and protease domain, could not be constructed because of the weak electron density.","type":"Article"}],"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T12:20:50.448Z"}}],"released":"2018_11","uniref100":"UniRef100_Q9Y4P1","date":"2018-07-09T03:24:04.000Z","acc":"Q9Y4P1","name":"Cysteine protease ATG4B","length":393,"organism":"Homo sapiens","dataset":["Autophagy-related proteins"],"UniParc":"UPI00001AF16F","genes":[{"name":{"value":"ATG4B","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15187094","url":"http://www.ncbi.nlm.nih.gov/pubmed/15187094","alternativeUrl":"https://europepmc.org/abstract/MED/15187094"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:20790","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:20790"}}]},"synonyms":[{"value":"APG4B","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15187094","url":"http://www.ncbi.nlm.nih.gov/pubmed/15187094","alternativeUrl":"https://europepmc.org/abstract/MED/15187094"}}]},{"value":"AUTL1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:20790","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:20790"}}]},{"value":"KIAA0943","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10231032","url":"http://www.ncbi.nlm.nih.gov/pubmed/10231032","alternativeUrl":"https://europepmc.org/abstract/MED/10231032"}}]}]}],"alphafold_very_low_content":0.09923664122137404,"disorder_content":0.11959287531806616,"disprot_consensus":{"full":[{"start":187,"end":217,"type":"D"},{"start":378,"end":393,"type":"D"}],"Structural state":[{"start":187,"end":217,"type":"D"},{"start":378,"end":393,"type":"D"}],"Molecular function":[{"start":387,"end":392,"type":"F"}],"Biological process":[{"start":388,"end":391,"type":"F"}],"Disorder function":[{"start":191,"end":215,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00087","name":"Snake toxin and toxin-like protein","start":63,"end":137}],"gene3D":[{"start":62,"end":139,"id":"2.10.60.10","name":"CD59"}]},"uniref50":"UniRef50_Q8IV16","sequence":"MKALGAVLLALLLFGRPGRGQTQQEEEEEDEDHGPDDYDEEDEDEVEEEETNRLPGGRSRVLLRCYTCKSLPRDERCNLTQNCSHGQTCTTLIAHGNTESGLLTTHSTWCTDSCQPITKTVEGTQVTMTCCQSSLCNVPPWQSSRVQDPTGKGAGGPRGSSETVGAALLLNLLAGLGAMGARRP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q8IV16","disprot_id":"DP01327","ncbi_taxon_id":9606,"regions_counter":7,"creator":"eficho","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":54,"region_id":"DP01327r001","released":"2022_03","ec_id":"ECO:0007680","reference_html":"The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain. <i> Mysling S, Kristensen KK, Larsson M, Beigneux AP, Gårdsvoll H, Fong LG, Bensadouen A, Jørgensen TJ, Young SG, Ploug M. </i> Elife, 2016","term_id":"IDPO:0000002","curator_id":"mguha","start":21,"term_ontology":"IDPO","curator_name":"Mainak Guharoy","ec_name":"chromatography evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"26725083","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":54,"region_id":"DP01327r002","start":21,"ec_id":"ECO:0006210","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"GPIHBP1 is highly asymmetrical with an N-terminal intrinsically disordered region (IDR) rich in acidic residues","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29899144","version":3,"reference_html":"A disordered acidic domain in GPIHBP1 harboring a sulfated tyrosine regulates lipoprotein lipase. <i> Kristensen KK, Midtgaard SR, Mysling S, Kovrov O, Hansen LB, Skar-Gislinge N, Beigneux AP, Kragelund BB, Olivecrona G, Young SG, Jørgensen TJD, Fong LG, Ploug M. </i> Proc Natl Acad Sci U S A, 2018","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","cross_refs":[{"db":"SASBDB","id":"SASDHF4"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":54,"region_id":"DP01327r003","released":"2022_03","ec_id":"ECO:0007691","reference_html":"The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain. <i> Mysling S, Kristensen KK, Larsson M, Beigneux AP, Gårdsvoll H, Fong LG, Bensadouen A, Jørgensen TJ, Young SG, Ploug M. </i> Elife, 2016","term_id":"IDPO:0000002","curator_id":"mguha","start":21,"term_ontology":"IDPO","curator_name":"Mainak Guharoy","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"26725083","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":54,"region_id":"DP01327r004","released":"2022_03","ec_id":"ECO:0006196","reference_html":"The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain. <i> Mysling S, Kristensen KK, Larsson M, Beigneux AP, Gårdsvoll H, Fong LG, Bensadouen A, Jørgensen TJ, Young SG, Ploug M. </i> Elife, 2016","term_id":"IDPO:0000002","curator_id":"mguha","start":21,"term_ontology":"IDPO","curator_name":"Mainak Guharoy","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1354-2872","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"26725083","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q8IV16","date":"2018-07-09T06:46:27.000Z","acc":"Q8IV16","name":"Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1","length":184,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000746BF","genes":[{"name":{"value":"GPIHBP1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:24945","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:24945"}}]},"synonyms":[{"value":"HBP1"}]}],"alphafold_very_low_content":0.1956521739130435,"disorder_content":0.18478260869565216,"disprot_consensus":{"full":[{"start":21,"end":54,"type":"D"}],"Structural state":[{"start":21,"end":54,"type":"D"}]}},{"features":{"gene3D":[{"start":37,"end":213,"id":"2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"}],"pfam":[{"id":"PF00400","name":"WD domain, G-beta repeat","start":85,"end":124}]},"uniref50":"UniRef50_Q9C0C7","sequence":"MKVVPEKNAVRILWGRERGARAMGAQRLLQELVEDKTRWMKWEGKRVELPDSPRSTFLLAFSPDRTLLASTHVNHNIYITEVKTGKCVHSLIGHRRTPWCVTFHPTISGLIASGCLDGEVRIWDLHGGSESWFTDSNNAIASLAFHPTAQLLLIATANEIHFWDWSRREPFAVVKTASEMERVRLVRFDPLGHYLLTAIVNPSNQQGDDEPEIPIDGTELSHYRQRALLQSQPVRRTPLLHNFLHMLSSRSSGIQVGEQSTVQDSATPSPPPPPPQPSTERPRTSAYIRLRQRVSYPTAECCQHLGILCLCSRCSGTRVPSLLPHQDSVPPASARATTPSFSFVQTEPFHPPEQASSTQQDQGLLNRPSAFSTVQSSTAGNTLRNLSLGPTRRSLGGPLSSHPSRYHREIAPGLTGSEWTRTVLSLNSRSEAESMPPPRTSASSVSLLSVLRQQEGGSQASVYTSATEGRGFPASGLATESDGGNGSSQNNSGSIRHELQCDLRRFFLEYDRLQELDQSLSGEAPQTQQAQEMLNNNIESERPGPSHQPTPHSSENNSNLSRGHLNRCRACHNLLTFNNDTLRWERTTPNYSSGEASSSWQVPSSFESVPSSGSQLPPLERTEGQTPSSSRLELSSSASPQEERTVGVAFNQETGHWERIYTQSSRSGTVSQEALHQDMPEESSEEDSLRRRLLESSLISLSRYDGAGSREHPIYPDPARLSPAAYYAQRMIQYLSRRDSIRQRSMRYQQNRLRSSTSSSSSDNQGPSVEGTDLEFEDFEDNGDRSRHRAPRNARMSAPSLGRFVPRRFLLPEYLPYAGIFHERGQPGLATHSSVNRVLAGAVIGDGQSAVASNIANTTYRLQWWDFTKFDLPEISNASVNVLVQNCKIYNDASCDISADGQLLAAFIPSSQRGFPDEGILAVYSLAPHNLGEMLYTKRFGPNAISVSLSPMGRYVMVGLASRRILLHPSTEHMVAQVFRLQQAHGGETSMRRVFNVLYPMPADQRRHVSINSARWLPEPGLGLAYGTNKGDLVICRPEALNSGVEYYWDQLNETVFTVHSNSRSSERPGTSRATWRTDRDMGLMNAIGLQPRNPATSVTSQGTQTLALQLQNAETQTEREVPEPGTAASGPGEGEGSEYGASGEDALSRIQRLMAEGGMTAVVQREQSTTMASMGGFGNNIIVSHRIHRSSQTGTEPGAAHTSSPQPSTSRGLLPEAGQLAERGLSPRTASWDQPGTPGREPTQPTLPSSSPVPIPVSLPSAEGPTLHCELTNNNHLLDGGSSRGDAAGPRGEPRNR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9C0C7","disprot_id":"DP01328","ncbi_taxon_id":9606,"regions_counter":3,"creator":"oantonescu","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":541,"region_id":"DP01328r001","released":"2022_06","ec_id":"ECO:0006204","reference_html":"Identifying intrinsically disordered protein regions likely to undergo binding-induced helical transitions. <i> Glover K, Mei Y, Sinha SC. </i> Biochim Biophys Acta, 2016","term_id":"IDPO:0000002","curator_id":"vnugnes","start":527,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-05-23T19:55:13.806Z","reference_source":"pmid","term_name":"disorder","reference_id":"27179590","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Authors show the region is intrinsically unstructured by its large negative ellipticity at 200 nm and moderate ellipticity at 190 nm, typical of IDR.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-12T11:08:51.690Z"}}],"released":"2018_11","uniref100":"UniRef100_Q9C0C7","date":"2018-07-09T07:41:29.000Z","acc":"Q9C0C7","name":"Activating molecule in BECN1-regulated autophagy protein 1","length":1298,"organism":"Homo sapiens","dataset":["Autophagy-related proteins","NDDs-related proteins"],"UniParc":"UPI000007141C","genes":[{"name":{"value":"AMBRA1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"17589504","url":"http://www.ncbi.nlm.nih.gov/pubmed/17589504","alternativeUrl":"https://europepmc.org/abstract/MED/17589504"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:25990","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:25990"}}]},"synonyms":[{"value":"DCAF3","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16949367","url":"http://www.ncbi.nlm.nih.gov/pubmed/16949367","alternativeUrl":"https://europepmc.org/abstract/MED/16949367"}}]},{"value":"KIAA1736","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11214970","url":"http://www.ncbi.nlm.nih.gov/pubmed/11214970","alternativeUrl":"https://europepmc.org/abstract/MED/11214970"}}]}]}],"alphafold_very_low_content":0.6810477657935285,"disorder_content":0.011556240369799691,"disprot_consensus":{"full":[{"start":527,"end":541,"type":"D"}],"Structural state":[{"start":527,"end":541,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00178","name":"Ets-domain","start":5,"end":85}],"gene3D":[{"start":1,"end":102,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}]},"uniref50":"UniRef50_P28324","sequence":"MDSAITLWQFLLQLLQKPQNKHMICWTSNDGQFKLLQAEEVARLWGIRKNKPNMNYDKLSRALRYYYVKNIIKKVNGQKFVYKFVSYPEILNMDPMTVGRIEGDCESLNFSEVSSSSKDVENGGKDKPPQPGAKTSSRNDYIHSGLYSSFTLNSLNSSNVKLFKLIKTENPAEKLAEKKSPQEPTPSVIKFVTTPSKKPPVEPVAATISIGPSISPSSEETIQALETLVSPKLPSLEAPTSASNVMTAFATTPPISSIPPLQEPPRTPSPPLSSHPDIDTDIDSVASQPMELPENLSLEPKDQDSVLLEKDKVNNSSRSKKPKGLELAPTLVITSSDPSPLGILSPSLPTASLTPAFFSQTPIILTPSPLLSSIHFWSTLSPVAPLSPARLQGANTLFQFPSVLNSHGPFTLSGLDGPSTPGPFSPDLQKT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P28324","disprot_id":"DP01329","ncbi_taxon_id":9606,"regions_counter":3,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":136,"region_id":"DP01329r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The B-box dominates SAP-1-SRF interactions in the structure of the ternary complex. <i> Hassler M, Richmond TJ. </i> EMBO J, 2001","statement":[{"text":"The 43 amino acids (94–136) linking the B-box to the ETS domain of SAP-1 are unobserved in the electron density map and are therefore likely to be highly disordered.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":94,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11406578","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1HBX"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T12:39:07.705Z"}},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":136,"term_name":"flexible linker","start":94,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","statement":[{"text":"This linker region must be flexible as it accommodates cooperative binding of SAP-1 and SRF on sites disposed with virtually any spacing of up to 10 bp as well as direction reversal of the EBS with respect to the CArG-box","type":"Discussion"},{"text":"The terminal amino acids and the SAP-1 linker region disordered in the structure are printed in gray.","type":"Figure"}],"curator_id":"fquaglia","released":"2022_06","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11406578","version":4,"reference_html":"The B-box dominates SAP-1-SRF interactions in the structure of the ternary complex. <i> Hassler M, Richmond TJ. </i> EMBO J, 2001","date":"2022-06-25T20:27:27.043Z","term_id":"IDPO:0000033","ec_id":"ECO:0006220","region_id":"DP01329r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T12:39:10.577Z"}}],"released":"2018_11","uniref100":"UniRef100_P28324","date":"2018-07-09T14:08:17.000Z","acc":"P28324","name":"ETS domain-containing protein Elk-4","length":431,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI000017640E","genes":[{"name":{"value":"ELK4"},"synonyms":[{"value":"SAP1"}]}],"alphafold_very_low_content":0.5406032482598608,"disorder_content":0.09976798143851508,"disprot_consensus":{"full":[{"start":94,"end":136,"type":"D"}],"Structural state":[{"start":94,"end":136,"type":"D"}],"Disorder function":[{"start":94,"end":136,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":500,"end":679},{"id":"PF00270","name":"DEAD/DEAH box helicase","start":1349,"end":1518},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":772,"end":878},{"id":"PF02889","name":"Sec63 Brl domain","start":999,"end":1307},{"id":"PF02889","name":"Sec63 Brl domain","start":1848,"end":2158},{"id":"PF18149","name":"N-terminal helicase PWI domain","start":281,"end":389},{"id":"PF21188","name":"Pre-mRNA-splicing helicase BRR2 plug domain","start":116,"end":188},{"id":"PF23445","name":"Winged Helix-turn-helix domain","start":909,"end":982},{"id":"PF23445","name":"Winged Helix-turn-helix domain","start":1743,"end":1824}],"gene3D":[{"start":1199,"end":1311,"id":"2.60.40.150","name":"C2 domain"},{"start":2049,"end":2163,"id":"2.60.40.150","name":"C2 domain"},{"start":999,"end":1140,"id":"1.10.3380.10","name":"Sec63 N-terminal domain-like domain"},{"start":703,"end":902,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":491,"end":702,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":1141,"end":1198,"id":"1.10.150.20","name":"5' to 3' exonuclease, C-terminal subdomain"},{"start":1312,"end":1540,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":1541,"end":1743,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":1850,"end":1990,"id":"1.10.3380.10","name":"Sec63 N-terminal domain-like domain"},{"start":1991,"end":2048,"id":"1.10.150.20","name":"5' to 3' exonuclease, C-terminal subdomain"}]},"uniref50":"UniRef50_P32639","sequence":"MTEHETKDKAKKIREIYRYDEMSNKVLKVDKRFMNTSQNPQRDAEISQPKSMSGRISAKDMGQGLCNNINKGLKENDVAVEKTGKSASLKKIQQHNTILNSSSDFRLHYYPKDPSNVETYEQILQWVTEVLGNDIPHDLIIGTADIFIRQLKENEENEDGNIEERKEKIQHELGINIDSLKFNELVKLMKNITDYETHPDNSNKQAVAILADDEKSDEEEVTEMSNNANVLGGEINDNEDDDEEYDYNDVEVNSKKKNKRALPNIENDIIKLSDSKTSNIESVPIYSIDEFFLQRKLRSELGYKDTSVIQDLSEKILNDIETLEHNPVALEQKLVDLLKFENISLAEFILKNRSTIFWGIRLAKSTENEIPNLIEKMVAKGLNDLVEQYKFRETTHSKRELDSGDDQPQSSEAKRTKFSNPAIPPVIDLEKIKFDESSKLMTVTKVSLPEGSFKRVKPQYDEIHIPAPSKPVIDYELKEITSLPDWCQEAFPSSETTSLNPIQSKVFHAAFEGDSNMLICAPTGSGKTNIALLTVLKALSHHYNPKTKKLNLSAFKIVYIAPLKALVQEQVREFQRRLAFLGIKVAELTGDSRLSRKQIDETQVLVSTPEKWDITTRNSNNLAIVELVRLLIIDEIHLLHDDRGPVLESIVARTFWASKYGQEYPRIIGLSATLPNYEDVGRFLRVPKEGLFYFDSSFRPCPLSQQFCGIKERNSLKKLKAMNDACYEKVLESINEGNQIIVFVHSRKETSRTATWLKNKFAEENITHKLTKNDAGSKQILKTEAANVLDPSLRKLIESGIGTHHAGLTRSDRSLSEDLFADGLLQVLVCTATLAWGVNLPAHTVIIKGTDVYSPEKGSWEQLSPQDVLQMLGRAGRPRYDTFGEGIIITDQSNVQYYLSVLNQQLPIESQFVSKLVDNLNAEVVAGNIKCRNDAVNWLAYTYLYVRMLASPMLYKVPDISSDGQLKKFRESLVHSALCILKEQELVLYDAENDVIEATDLGNIASSFYINHASMDVYNRELDEHTTQIDLFRIFSMSEEFKYVSVRYEEKRELKQLLEKAPIPIREDIDDPLAKVNVLLQSYFSQLKFEGFALNSDIVFIHQNAGRLLRAMFEICLKRGWGHPTRMLLNLCKSATTKMWPTNCPLRQFKTCPVEVIKRLEASTVPWGDYLQLETPAEVGRAIRSEKYGKQVYDLLKRFPKMSVTCNAQPITRSVMRFNIEIIADWIWDMNVHGSLEPFLLMLEDTDGDSILYYDVLFITPDIVGHEFTLSFTYELKQHNQNNLPPNFFLTLISENWWHSEFEIPVSFNGFKLPKKFPPPTPLLENISISTSELGNDDFSEVFEFKTFNKIQSQVFESLYNSNDSVFVGSGKGTGKTAMAELALLNHWRQNKGRAVYINPSGEKIDFLLSDWNKRFSHLAGGKIINKLGNDPSLNLKLLAKSHVLLATPVQFELLSRRWRQRKNIQSLELMIYDDAHEISQGVYGAVYETLISRMIFIATQLEKKIRFVCLSNCLANARDFGEWAGMTKSNIYNFSPSERIEPLEINIQSFKDVEHISFNFSMLQMAFEASAAAAGNRNSSSVFLPSRKDCMEVASAFMKFSKAIEWDMLNVEEEQIVPYIEKLTDGHLRAPLKHGVGILYKGMASNDERIVKRLYEYGAVSVLLISKDCSAFACKTDEVIILGTNLYDGAEHKYMPYTINELLEMVGLASGNDSMAGKVLILTSHNMKAYYKKFLIEPLPTESYLQYIIHDTLNNEIANSIIQSKQDCVDWFTYSYFYRRIHVNPSYYGVRDTSPHGISVFLSNLVETCLNDLVESSFIEIDDTEAEVTAEVNGGDDEATEIISTLSNGLIASHYGVSFFTIQSFVSSLSNTSTLKNMLYVLSTAVEFESVPLRKGDRALLVKLSKRLPLRFPEHTSSGSVSFKVFLLLQAYFSRLELPVDFQNDLKDILEKVVPLINVVVDILSANGYLNATTAMDLAQMLIQGVWDVDNPLRQIPHFNNKILEKCKEINVETVYDIMALEDEERDEILTLTDSQLAQVAAFVNNYPNVELTYSLNNSDSLISGVKQKITIQLTRDVEPENLQVTSEKYPFDKLESWWLVLGEVSKKELYAIKKVTLNKETQQYELEFDTPTSGKHNLTIWCVCDSYLDADKELSFEINVK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P32639","disprot_id":"DP01330","ncbi_taxon_id":559292,"regions_counter":3,"creator":"mpajkos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":112,"region_id":"DP01330r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The large N-terminal region of the Brr2 RNA helicase guides productive spliceosome activation. <i> Absmeier E, Wollenhaupt J, Mozaffari-Jovin S, Becke C, Lee CT, Preussner M, Heyd F, Urlaub H, Lührmann R, Santos KF, Wahl MC. </i> Genes Dev, 2015","statement":[{"text":"Region could not be traced in the electron density of the present FL Brr2-Jab1 crystals.","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":1,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5DCA"}],"reference_id":"26637280","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":257,"region_id":"DP01330r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The large N-terminal region of the Brr2 RNA helicase guides productive spliceosome activation. <i> Absmeier E, Wollenhaupt J, Mozaffari-Jovin S, Becke C, Lee CT, Preussner M, Heyd F, Urlaub H, Lührmann R, Santos KF, Wahl MC. </i> Genes Dev, 2015","statement":[{"text":"Region could not be traced in the electron density of the present FL Brr2-Jab1 crystals.","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":193,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5DCA"}],"reference_id":"26637280","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":419,"region_id":"DP01330r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The large N-terminal region of the Brr2 RNA helicase guides productive spliceosome activation. <i> Absmeier E, Wollenhaupt J, Mozaffari-Jovin S, Becke C, Lee CT, Preussner M, Heyd F, Urlaub H, Lührmann R, Santos KF, Wahl MC. </i> Genes Dev, 2015","statement":[{"text":"Region could not be traced in the electron density of the present FL Brr2-Jab1 crystals.","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":394,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5DCA"}],"reference_id":"26637280","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P32639","date":"2018-07-10T16:01:06.000Z","acc":"P32639","name":"Pre-mRNA-splicing helicase BRR2","length":2163,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000126AE4","genes":[{"name":{"value":"BRR2"},"synonyms":[{"value":"RSS1"},{"value":"SNU246"}],"orfNames":[{"value":"SYGP-ORF66"}],"olnNames":[{"value":"YER172C"}]}],"alphafold_very_low_content":0.09153952843273232,"disorder_content":0.09385113268608414,"disprot_consensus":{"full":[{"start":1,"end":112,"type":"D"},{"start":193,"end":257,"type":"D"},{"start":394,"end":419,"type":"D"}],"Structural state":[{"start":1,"end":112,"type":"D"},{"start":193,"end":257,"type":"D"},{"start":394,"end":419,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00337","name":"Galactoside-binding lectin","start":117,"end":246}],"gene3D":[{"start":113,"end":250,"id":"2.60.120.200","name":"2.60.120.200"}]},"uniref50":"UniRef50_P17931","sequence":"MADNFSLHDALSGSGNPNPQGWPGAWGNQPAGAGGYPGASYPGAYPGQAPPGAYPGQAPPGAYPGAPGAYPGAPAPGVYPGPPSGPGAYPSSGQPSATGAYPATGPYGAPAGPLIVPYNLPLPGGVVPRMLITILGTVKPNANRIALDFQRGNDVAFHFNPRFNENNRRVIVCNTKLDNNWGREERQSVFPFESGKPFKIQVLVEPDHFKVAVNDAHLLQYNHRVKKLNEISKLGISGDIDLTSASYTMI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P17931","disprot_id":"DP01332","ncbi_taxon_id":9606,"regions_counter":11,"creator":"ireményi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":100,"region_id":"DP01332r001","released":"2022_03","ec_id":"ECO:0006210","reference_html":"The intrinsically disordered N-terminal domain of galectin-3 dynamically mediates multisite self-association of the protein through fuzzy interactions. <i> Lin YH, Qiu DC, Chang WH, Yeh YQ, Jeng US, Liu FT, Huang JR. </i> J Biol Chem, 2017","term_id":"IDPO:0000002","curator_id":"rpancsa","start":20,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28893908","statement":[{"text":"Small-angle X-ray scattering studies. A, SAXS intensities of galectin-3 as a function of the scattering vector q (Å−1). B, the Kratky plot is typical of that of a partially folded protein.","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T15:03:57.484Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":115,"region_id":"DP01332r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"(1)H, (13)C, and (15)N backbone and side-chain chemical shift assignments for the 36 proline-containing, full length 29 kDa human chimera-type galectin-3. <i> Ippel H, Miller MC, Berbís MA, Suylen D, André S, Hackeng TM, Cañada FJ, Weber C, Gabius HJ, Jiménez-Barbero J, Mayo KH. </i> Biomol NMR Assign, 2015","statement":[{"text":"Resonances from the CRD are relatively well dispersed for the canonical β-sheet structure as previously reported for truncated Gal-3 CRD (Umemoto and Leffler 2001), whereas those arising from the N-terminal tail exhibit rather narrow line widths, reflecting comparatively increased internal mobility. In addition, resonances arising from the N-terminal tail are minimally dispersed and fall within the spectral region associated with random coil conformation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24504927","cross_refs":[{"db":"BMRB","id":"19491"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T13:58:07.351Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":20,"end":100,"reference_id":"28893908","reference_source":"pmid","reference_html":"The intrinsically disordered N-terminal domain of galectin-3 dynamically mediates multisite self-association of the protein through fuzzy interactions. <i> Lin YH, Qiu DC, Chang WH, Yeh YQ, Jeng US, Liu FT, Huang JR. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01332r004","statement":[{"text":"The low sequence complexity of the structurally disordered NTD is reminiscent of those recently reported proteins whose low-complexity domains mediate their liquid–liquid phase separation behavior in various cellular functions. Indeed, we found that the NTD (as does a phosphomimetic mutant S6E) undergoes temperature-dependent phase separation.","type":"Discussion"},{"text":"The text is in the discussion, but the figure showing LLPS is in the supplementary.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T15:04:10.426Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":20,"end":100,"reference_id":"28893908","reference_source":"pmid","reference_html":"The intrinsically disordered N-terminal domain of galectin-3 dynamically mediates multisite self-association of the protein through fuzzy interactions. <i> Lin YH, Qiu DC, Chang WH, Yeh YQ, Jeng US, Liu FT, Huang JR. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01332r005","statement":[{"text":"The MTSL label on the CRD (I250C; the β-strand 11) bleaches a broad range of intensity in the NTD, consistent with the model that the NTD contacts with the CRD fuzzily and that the first ∼20 residues have less contact with this domain","type":"Results"},{"text":"The authors report an intra-protein interaction between the disordered N-terminal domain and the folded C-terminal domain.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T15:04:02.437Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":40,"reference_id":"28973299","reference_source":"pmid","reference_html":"Novel polysaccharide binding to the N-terminal tail of galectin-3 is likely modulated by proline isomerization. <i> Miller MC, Zheng Y, Yan J, Zhou Y, Tai G, Mayo KH. </i> Glycobiology, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0030246","term_name":"carbohydrate binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01332r006","statement":[{"text":"The present study is focused on human galectin-3 (Gal-3) interactions with a 60 kDa rhamnogalacturonan RG-I-4 that we use as a model to garner information as to how galectins interact with large polysaccharides, as well as to develop this agent as a therapeutic against human disease. Gal-3 is unique among galectins, because as the only chimera-type, it has a long N-terminal tail (NT) that has long puzzled investigators due to its dynamic, disordered nature and presence of numerous prolines. Here, we use 15N-1H heteronuclear single quantum coherence NMR spectroscopy to demonstrate that multiple sites on RG-I-4 provide epitopes for binding to three sites on 15N-labeled Gal-3, two within its carbohydrate recognition domain (CRD) and one at a novel site within the NT encompassing the first 40 residues that are highly conserved among all species of Gal-3.","type":"Abstract"},{"text":"A number of NT resonances are chemically shifted by the presence of RG-I-4, with the most perturbed ones belonging to residues within the N-terminal part of the NT as observed with the NT in full length Gal-3. These data indicate that the Gal-3 NT (independent of the presence of the CRD) binds to one or more sites within the RG-I-4 polysaccharide.","type":"Results"},{"text":"Although there are some changes that occur within the C-terminal part of the NT (residues ~75–100), the most perturbed resonances belong to residues within the N-terminal part of the NT (residues 1–40). Likewise, seven of the nine Asn/Gln residues in the NT (i.e., N4, N16, N18, Q20, N28, Q29, Q48) perturbed by interactions with RG-I-4.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T15:04:06.060Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.\" [GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":112,"reference_id":"32144274","reference_source":"pmid","reference_html":"Liquid-liquid phase separation and extracellular multivalent interactions in the tale of galectin-3. <i> Chiu YP, Sun YC, Qiu DC, Lin YH, Chen YQ, Kuo JC, Huang JR. </i> Nat Commun, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01332r007","statement":[{"text":"Indeed, a 1 mM NTD sample with 150 mM NaCl condenses at higher temperatures and dissolves at lower ones in a reversible manner.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T15:04:11.410Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":112,"reference_id":"28893908","reference_source":"pmid","reference_html":"The intrinsically disordered N-terminal domain of galectin-3 dynamically mediates multisite self-association of the protein through fuzzy interactions. <i> Lin YH, Qiu DC, Chang WH, Yeh YQ, Jeng US, Liu FT, Huang JR. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01332r008","statement":[{"text":"We collected the longitudinal relaxation rates (R1), transverse relaxation rates (R2), and heteronuclear NOEs (hetNOEs) at different protein concentrations. The residues in the NTD have higher R1 values, lower R2 values, and lower hetNOEs than those in the CRD because the intrinsically disordered region is more dynamic.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T15:04:00.075Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P17931","date":"2018-07-11T13:26:15.000Z","acc":"P17931","name":"Galectin-3","length":250,"organism":"Homo sapiens","dataset":["Extracellular matrix proteins","Condensates-related proteins"],"UniParc":"UPI000012E42A","genes":[{"name":{"value":"LGALS3","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6563","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6563"}}]},"synonyms":[{"value":"MAC2"}]}],"alphafold_very_low_content":0.392,"disorder_content":0.46,"disprot_consensus":{"full":[{"start":1,"end":115,"type":"D"}],"Structural state":[{"start":1,"end":115,"type":"D"}],"Molecular function":[{"start":1,"end":112,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00373","name":"FERM central domain","start":518,"end":640},{"id":"PF16705","name":"NUDIX, or N-terminal NPxY motif-rich, region of KRIT","start":22,"end":198},{"id":"PF24521","name":"KRIT1 ankyrin-repeats domain","start":273,"end":419},{"id":"PF24522","name":"KRIT1/FRMD8, FERM domain C-lobe","start":656,"end":721}],"gene3D":[{"start":271,"end":416,"id":"1.25.40.20","name":"Ankyrin repeat-containing domain"},{"start":516,"end":634,"id":"1.20.80.10","name":"1.20.80.10"},{"start":635,"end":736,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":1,"end":41,"id":"3.30.70.2240","name":"KRIT, N-terminal Nudix domain, NPxY motif-rich region"},{"start":417,"end":515,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"},{"start":48,"end":185,"id":"3.30.70.2240","name":"KRIT, N-terminal Nudix domain, NPxY motif-rich region"}]},"uniref50":"UniRef50_O00522","sequence":"MGNPENIEDAYVAVIRPKNTASLNSREYRAKSYEILLHEVPIEGQKKKRKKVLLETKLQGNSEITQGILDYVVETTKPISPANQGIRGKRVVLMKKFPLDGEKMGREASLFIVPSVVKDNTKYTYTPGCPIFYCLQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTNVINPAYATESGQTENSLHMGYSALEIKSKMLALEKADTCIYNPLFGSDLQYTNRVDKVVINPYFGLGAPDYSKIQIPKQEKWQRSMSSVTEDKERQWVDDFPLHRSACEGDSELLSRLLSERFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKCNPNLLNGQLSSPLHFAAGGGHAEIVQILLNHPETDRHITDQQGRSPLNICEENKQNNWEEAAKLLKEAINKPYEKVRIYRMDGSYRSVELKHGNNTTVQQIMEGMRLSQETQQYFTIWICSENLSLQLKPYHKPLQHVRDWPEILAELTNLDPQRETPQLFLRRDVRLPLEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLNEENLKSIVPVTKLKSKAPHWTNRILHEYKNLSTSEGVSKEMHHLQRMFLQNCWEIPTYGAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQAGLVVKLLMKLNGQLMPTERNS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O00522","disprot_id":"DP01333","ncbi_taxon_id":9606,"regions_counter":1,"creator":"akajava","regions":[{"region_id":"DP01333r001","ec_ontology":"ECO","end":128,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":118,"version":3,"statement":[{"text":"The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}],"term_name":"disorder","reference_html":"Mechanism for KRIT1 release of ICAP1-mediated suppression of integrin activation. <i> Liu W, Draheim KM, Zhang R, Calderwood DA, Boggon TJ. </i> Mol Cell, 2013","released":"2022_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"23317506","date":"2022-08-23T19:43:27.887Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4DX8"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O14713"}]}],"released":"2018_11","uniref100":"UniRef100_O00522","date":"2018-07-11T15:14:49.000Z","acc":"O00522","name":"Krev interaction trapped protein 1","length":736,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012E078","genes":[{"name":{"value":"KRIT1"},"synonyms":[{"value":"CCM1"}]}],"alphafold_very_low_content":0.12228260869565218,"disorder_content":0.014945652173913044,"disprot_consensus":{"full":[{"start":118,"end":128,"type":"D"}],"Structural state":[{"start":118,"end":128,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00685","name":"Sulfotransferase domain","start":6,"end":232}],"gene3D":[{"start":91,"end":274,"id":"1.25.40.460","name":"1.25.40.460"}]},"uniref50":"UniRef50_Q8KLM3","sequence":"MNGIRWIASYPKAGNTWLRCMLAAYITGKAPQTWKDMETVSLELEGMLHLGDMPPTEPTKPVLVKTHLKADVPVLGLYSEATAKVLYLVRNPRDILLSAMRMTAISRDDMESSRTFARDFIANEGLRMRGRGGGAGLGSWPENVRIWTESSRDRFPNADVLTMRYEDLKGDPVARFSEIVEFLDLGDPVDIEDIRRAVAACTLERMRELEKRSQQQGQWASMTGGRGGEKHPFVGEGRYDQSLSFLGEDIESAYQELLHGDSEFAHYAKQYGYAG","taxonomy":["Bacteria","environmental samples"],"uniref90":"UniRef90_B7T1D9","disprot_id":"DP01334","ncbi_taxon_id":164851,"regions_counter":2,"creator":"jmanso","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":240,"region_id":"DP01334r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The 2.7 Å resolution structure of the glycopeptide sulfotransferase Teg14. <i> Bick MJ, Banik JJ, Darst SA, Brady SF. </i> Acta Crystallogr D Biol Crystallogr, 2010","statement":[{"text":"V3, which is encompassed by the 26-amino-acid disordered region, was not visible\nin the structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jmanso","start":215,"term_ontology":"IDPO","curator_name":"Jose A Manso","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3NIB"}],"reference_id":"21123867","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":240,"term_name":"small molecule binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"The 2.7 Å resolution structure of the glycopeptide sulfotransferase Teg14. <i> Bick MJ, Banik JJ, Darst SA, Brady SF. </i> Acta Crystallogr D Biol Crystallogr, 2010","statement":[{"text":"V3 could not be modeled in the electron-density map. The V3 loop is\npart of a larger motif that we have termed the GHL (glycopeptide\nhelix loop) and is believed to interact extensively with the glycopeptide.","type":"Results"}],"term_id":"GO:0036094","curator_id":"jmanso","start":215,"term_ontology":"GO","curator_name":"Jose A Manso","reference_id":"21123867","version":3,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01334r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_B7T1D9","date":"2018-07-11T15:22:18.000Z","acc":"B7T1D9","name":"Teg14","length":275,"organism":"uncultured soil bacterium","dataset":[],"UniParc":"UPI000188D9A5","genes":[{"name":{"value":"teg14","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ACJ60997.1","url":"https://www.ebi.ac.uk/ena/browser/view/ACJ60997.1"}}]}}],"alphafold_very_low_content":0.04727272727272727,"disorder_content":0.09454545454545454,"disprot_consensus":{"full":[{"start":215,"end":240,"type":"D"}],"Structural state":[{"start":215,"end":240,"type":"D"}],"Molecular function":[{"start":215,"end":240,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04706","name":"Dickkopf N-terminal cysteine-rich region","start":85,"end":139},{"id":"PF21479","name":"Dickkopf-related protein 1/2/4, C-terminal subdomain 2","start":217,"end":266},{"id":"PF21481","name":"Dickkopf-related protein 1/2/4, C-terminal subdomain 1","start":185,"end":214}],"gene3D":[{"start":175,"end":266,"id":"2.10.80.10","name":"Lipase, subunit A"}]},"uniref50":"UniRef50_O94907","sequence":"MMALGAAGATRVFVAMVAAALGGHPLLGVSATLNSVLNSNAIKNLPPPLGGAAGHPGSAVSAAPGILYPGGNKYQTIDNYQPYPCAEDEECGTDEYCASPTRGGDAGVQICLACRKRRKRCMRHAMCCPGNYCKNGICVSSDQNHFRGEIEETITESFGNDHSTLDGYSRRTTLSSKMYHTKGQEGSVCLRSSDCASGLCCARHFWSKICKPVLKEGQVCTKHRRKGSHGLEIFQRCYCGEGLSCRIQKDHHQASNSSRLHTCQRH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O94907","disprot_id":"DP01335","ncbi_taxon_id":9606,"regions_counter":1,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":260,"region_id":"DP01335r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis of Wnt signaling inhibition by Dickkopf binding to LRP5/6. <i> Ahn VE, Chu ML, Choi HJ, Tran D, Abo A, Weis WI. </i> Dev Cell, 2011","statement":[{"text":"All residues of LRP6(3-4) are visible in both copies in the crystal, except for the loop comprising residues 1006–1012. In both copies, at least one sugar is visible at each of the five predicted N-linked glycosylation sites (Figure S1). The model of Dkk1_C comprises residues 182–264, except that the loop spanning residues 250–258 is disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ahatos","start":250,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3S2K"}],"reference_id":"22000856","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_O94907","date":"2018-07-11T15:41:52.000Z","acc":"O94907","name":"Dickkopf-related protein 1","length":266,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000004C65E","genes":[{"name":{"value":"DKK1"},"orfNames":[{"value":"UNQ492/PRO1008"}]}],"alphafold_very_low_content":0.34210526315789475,"disorder_content":0.041353383458646614,"disprot_consensus":{"full":[{"start":250,"end":260,"type":"D"}],"Structural state":[{"start":250,"end":260,"type":"D"}]}},{"features":{"pfam":[{"id":"PF14000","name":"DNA packaging protein FI","start":2,"end":129}],"gene3D":[{"start":72,"end":132,"id":"3.40.5.70","name":"DNA packaging chaperone protein FI, C-terminal beta-strand domain"}]},"uniref50":"UniRef50_P03709","sequence":"MTKDELIARLRSLGEQLNRDVSLTGTKEELALRVAELKEELDDTDETAGQDTPLSRENVLTGHENEVGSAQPDTVILDTSELVTVVALVKLHTDALHATRDEPVAFVLPGTAFRVSAGVAAEMTERGLARMQ","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Uroviricota","Caudoviricetes","Caudovirales","Siphoviridae","Lambdavirus"],"uniref90":"UniRef90_P03709","disprot_id":"DP01336","ncbi_taxon_id":10710,"regions_counter":3,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":80,"region_id":"DP01336r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural and biochemical characterization of phage λ FI protein (gpFI) reveals a novel mechanism of DNA packaging chaperone activity. <i> Popovic A, Wu B, Arrowsmith CH, Edwards AM, Davidson AR, Maxwell KL. </i> J Biol Chem, 2012","statement":[{"text":"Amide proton chemical shift values consistent with unstructured protein and a lack of medium and long range NOEs indicated that residues 42–80 were unstructured.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jbergier","start":42,"term_ontology":"IDPO","curator_name":"Julian Bergier","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2LSM"}],"reference_id":"22801427","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-29T13:34:41.849Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":80,"term_name":"flexible linker","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural and biochemical characterization of phage λ FI protein (gpFI) reveals a novel mechanism of DNA packaging chaperone activity. <i> Popovic A, Wu B, Arrowsmith CH, Edwards AM, Davidson AR, Maxwell KL. </i> J Biol Chem, 2012","statement":[{"text":"A partial trypsin digestion reaction of full-length gpFI by SDS-PAGE revealed the presence of a single band of ∼10 kDa that was resolved as two protein fragments by native PAGE. This further supports the presence of two independently folded domains in this protein with cleavage likely taking place at the single Arg residue present at position 56 in the unstructured loop between the two domains.","type":"Results"}],"term_id":"IDPO:0000033","curator_id":"jbergier","start":42,"term_ontology":"IDPO","curator_name":"Julian Bergier","reference_id":"22801427","version":4,"curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01336r002","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-29T13:34:51.135Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":42,"end":80,"reference_id":"22801427","reference_source":"pmid","reference_html":"Structural and biochemical characterization of phage λ FI protein (gpFI) reveals a novel mechanism of DNA packaging chaperone activity. <i> Popovic A, Wu B, Arrowsmith CH, Edwards AM, Davidson AR, Maxwell KL. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01336r003","statement":[{"text":"A partial trypsin digestion reaction of full-length gpFI by SDS-PAGE revealed the presence of a single band of ∼10 kDa that was resolved as two protein fragments by native PAGE. This further supports the presence of two independently folded domains in this protein with cleavage likely taking place at the single Arg residue present at position 56 in the unstructured loop between the two domains.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-29T13:34:40.902Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P03709","date":"2018-07-11T16:16:59.000Z","acc":"P03709","name":"DNA-packaging protein FI","length":132,"organism":"Escherichia phage lambda","dataset":["Viral proteins"],"UniParc":"UPI0000138CC0","genes":[{"name":{"value":"Fi"},"olnNames":[{"value":"lambdap09"}]}],"disorder_content":0.29545454545454547,"disprot_consensus":{"full":[{"start":42,"end":80,"type":"D"}],"Structural state":[{"start":42,"end":80,"type":"D"}],"Disorder function":[{"start":42,"end":80,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00179","name":"Ubiquitin-conjugating enzyme","start":7,"end":141}],"gene3D":[{"start":1,"end":151,"id":"3.10.110.10","name":"Ubiquitin Conjugating Enzyme"}]},"uniref50":"UniRef50_Q96B02","sequence":"MASMQKRLQKELLALQNDPPPGMTLNEKSVQNSITQWIVDMEGAPGTLYEGEKFQLLFKFSSRYPFDSPQVMFTGENIPVHPHVYSNGHICLSILTEDWSPALSVQSVCLSIISMLSSCKEKRRPPDNSFYVRTCNKNPKKTKWWYHDDTC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q96B02","disprot_id":"DP01337","ncbi_taxon_id":9606,"regions_counter":1,"creator":"jmanso","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":145,"region_id":"DP01337r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Intrinsic disorder drives N-terminal ubiquitination by Ube2w. <i> Vittal V, Shi L, Wenzel DM, Scaglione KM, Duncan ED, Basrur V, Elenitoba-Johnson KS, Baker D, Paulson HL, Brzovic PS, Klevit RE. </i> Nat Chem Biol, 2015","statement":[{"text":"In place of the final\nC-terminal helix present in canonical UBC\nfolds, residues N136–W145 form a disordered\nregion that occupies positions directly beneath\nthe active site in all states of the ensemble, as\nrevealed by the spin label attached to active site\nC91.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jmanso","start":136,"term_ontology":"IDPO","curator_name":"Jose A Manso","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2MT6"}],"reference_id":"25436519","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q96B02","date":"2018-07-11T16:45:00.000Z","acc":"Q96B02","name":"Ubiquitin-conjugating enzyme E2 W","length":151,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000037726","genes":[{"name":{"value":"UBE2W"},"synonyms":[{"value":"UBC16"}]}],"alphafold_very_low_content":0.013245033112582781,"disorder_content":0.06622516556291391,"disprot_consensus":{"full":[{"start":136,"end":145,"type":"D"}],"Structural state":[{"start":136,"end":145,"type":"D"}]}},{"features":{"pfam":[{"id":"PF06804","name":"Outer membrane protein assembly factor BamC-like C-terminal domain","start":230,"end":342},{"id":"PF29358","name":"Outer membrane protein assembly factor BamC-like N-terminal domain","start":41,"end":223}],"gene3D":[{"start":226,"end":344,"id":"3.30.310.170","name":"Outer membrane protein assembly factor BamC"},{"start":101,"end":212,"id":"3.30.530.50","name":"3.30.530.50"}]},"uniref50":"UniRef50_P0A903","sequence":"MAYSVQKSRLAKVAGVSLVLLLAACSSDSRYKRQVSGDEAYLEAAPLAELHAPAGMILPVTSGDYAIPVTNGSGAVGKALDIRPPAQPLALVSGARTQFTGDTASLLVENGRGNTLWPQVVSVLQAKNYTITQRDDAGQTLTTDWVQWNRLDEDEQYRGRYQISVKPQGYQQAVTVKLLNLEQAGKPVADAASMQRYSTEMMNVISAGLDKSATDAANAAQNRASTTMDVQSAADDTGLPMLVVRGPFNVVWQRLPAALEKVGMKVTDSTRSQGNMAVTYKPLSDSDWQELGASDPGLASGDYKLQVGDLDNRSSLQFIDPKGHTLTQSQNDALVAVFQAAFSK","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0A903","disprot_id":"DP01339","ncbi_taxon_id":83333,"regions_counter":8,"creator":"akajava","regions":[{"term_namespace":"Molecular function","ec_ontology":"ECO","end":98,"term_name":"protein binding","released":"2022_12","ec_name":"x-ray crystallography evidence used in manual assertion","reference_html":"Crystal structure of β-barrel assembly machinery BamCD protein complex. <i> Kim KH, Aulakh S, Paetzel M. </i> J Biol Chem, 2011","statement":[{"text":"The most outstanding structural feature of the BamCD complex is the 73-residue-long unstructured N terminus of BamC that has not been observed in previously reported structures (11, 23, 39); it folds into an elongated U-shaped loop structure that interacts extensively with BamD by fitting into a trail of crevices that run along the longitudinal axis of BamD (Fig. 2b and supplemental Fig. 3).","type":"Results"},{"text":" In this study, we crystallized BamD in a heterodimeric complex with BamCUN, and its structure was solved and refined to 2.9 Å resolution (supplemental Table 2).","type":"Results"}],"term_id":"GO:0005515","curator_id":"vnugnes","start":26,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"21937441","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-23T20:32:45.220Z","reference_source":"pmid","ec_id":"ECO:0005670","region_id":"DP01339r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"3TGO"}],"interaction_partner":[{"db":"UniProt","id":"P0AC02","operator":"and","partner_start":null,"partner_end":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":"glycerol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18367","entry_name":"phosphate(3-)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEMBL","id":"29103"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29101","entry_name":"sodium(1+)"}]},{"start":1,"end":100,"reference_id":"21624375","reference_source":"pmid","reference_html":"Structure of the BamC two-domain protein obtained by Rosetta with a limited NMR data set. <i> Warner LR, Varga K, Lange OF, Baker SL, Baker D, Sousa MC, Pardi A. </i> J Mol Biol, 2011","date":"2022-08-23T19:57:05.944Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP01339r003","statement":[{"text":"The first 100 N-terminal residues are not structured in BamC","type":"Results"}]},{"start":214,"end":227,"reference_id":"21624375","reference_source":"pmid","reference_html":"Structure of the BamC two-domain protein obtained by Rosetta with a limited NMR data set. <i> Warner LR, Varga K, Lange OF, Baker SL, Baker D, Sousa MC, Pardi A. </i> J Mol Biol, 2011","date":"2022-08-23T20:00:03.511Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"2LAE"}],"region_id":"DP01339r004","statement":[{"text":"Heteronuclear 15N{1H} NOEs were measured for the backbone amides in BamC101-344 and as seen in Fig. 2a, residues in the N- and C-terminal domains generally had NOE values above 0.7, whereas residues 214 to 227 in the linker had significantly lower 15N{1H} NOE values (0.13 to 0.42), indicating a flexible linker.","type":"Results"}]},{"start":214,"end":227,"reference_id":"21624375","reference_source":"pmid","reference_html":"Structure of the BamC two-domain protein obtained by Rosetta with a limited NMR data set. <i> Warner LR, Varga K, Lange OF, Baker SL, Baker D, Sousa MC, Pardi A. </i> J Mol Biol, 2011","date":"2022-08-23T19:59:46.192Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"2LAE"}],"region_id":"DP01339r005","statement":[{"text":"Heteronuclear 15N{1H} NOEs were measured for the backbone amides in BamC101-344 and as seen in Fig. 2a, residues in the N- and C-terminal domains generally had NOE values above 0.7, whereas residues 214 to 227 in the linker had significantly lower 15N{1H} NOE values (0.13 to 0.42), indicating a flexible linker.","type":"Results"}]},{"start":26,"end":98,"reference_id":"21937441","reference_source":"pmid","reference_html":"Crystal structure of β-barrel assembly machinery BamCD protein complex. <i> Kim KH, Aulakh S, Paetzel M. </i> J Biol Chem, 2011","date":"2022-08-23T20:11:31.222Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P0AC02","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01339r006","statement":[{"text":"Size exclusion chromatography analysis showed that any truncated form of BamC missing the unstructured N terminus (i.e. BamCN, BamCC, and BamCNC) was unable to form the BamCD complex (Fig. 1b and supplemental Fig. 1). On the other hand, BamCUN co-purified with BamD throughout the entire purification process despite missing the C-terminal domain (Fig. 1, c and d).","type":"Results"},{"text":"Together, these results show that the unstructured N terminus of BamC is required for the formation of the BamCD complex.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":26,"end":98,"reference_id":"21937441","reference_source":"pmid","reference_html":"Crystal structure of β-barrel assembly machinery BamCD protein complex. <i> Kim KH, Aulakh S, Paetzel M. </i> J Biol Chem, 2011","date":"2022-08-23T20:38:39.024Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"3TGO"}],"region_id":"DP01339r007","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0AC02"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":"glycerol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18367","entry_name":"phosphate(3-)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29103","entry_name":"potassium(1+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29101","entry_name":"sodium(1+)"}],"statement":[{"text":"The most outstanding structural feature of the BamCD complex is the 73-residue-long unstructured N terminus of BamC that has not been observed in previously reported structures (11, 23, 39); it folds into an elongated U-shaped loop structure that interacts extensively with BamD by fitting into a trail of crevices that run along the longitudinal axis of BamD (Fig. 2b and supplemental Fig. 3).","type":"Results"}]},{"start":26,"end":98,"reference_id":"21937441","reference_source":"pmid","reference_html":"Crystal structure of β-barrel assembly machinery BamCD protein complex. <i> Kim KH, Aulakh S, Paetzel M. </i> J Biol Chem, 2011","date":"2022-08-23T20:23:13.367Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP01339r008","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0AC02"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":"glycerol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18367","entry_name":"phosphate(3-)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29103","entry_name":"potassium(1+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29101","entry_name":"sodium(1+)"}],"statement":[{"text":"The most outstanding structural feature of the BamCD complex is the 73-residue-long unstructured N terminus of BamC that has not been observed in previously reported structures (11, 23, 39); it folds into an elongated U-shaped loop structure that interacts extensively with BamD by fitting into a trail of crevices that run along the longitudinal axis of BamD (Fig. 2b and supplemental Fig. 3).","type":"Results"}],"states_connection":[{"source":"DP01339r003","target":"DP01339r007"}]}],"released":"2018_11","uniref100":"UniRef100_P0A903","date":"2018-07-12T11:29:09.000Z","acc":"P0A903","name":"Outer membrane protein assembly factor BamC","length":344,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI000013021C","genes":[{"name":{"value":"bamC","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00924","url":"https://hamap.expasy.org/unirule/MF_00924"}}]},"synonyms":[{"value":"dapX"},{"value":"nlpB"}],"olnNames":[{"value":"b2477"},{"value":"JW2462"}]}],"alphafold_very_low_content":0.00872093023255814,"disorder_content":0.3313953488372093,"disprot_consensus":{"full":[{"start":1,"end":25,"type":"D"},{"start":26,"end":98,"type":"T"},{"start":99,"end":100,"type":"D"},{"start":214,"end":227,"type":"D"}],"Structural state":[{"start":1,"end":100,"type":"D"},{"start":214,"end":227,"type":"D"}],"Molecular function":[{"start":26,"end":98,"type":"F"}],"Disorder function":[{"start":214,"end":227,"type":"F"}],"Structural transition":[{"start":26,"end":98,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":56,"end":314}],"gene3D":[{"start":44,"end":131,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":133,"end":334,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"}]},"uniref50":"UniRef50_P52564","sequence":"MSQSKGKKRNPGLKIPKEAFEQPQTSSTPPRDLDSKACISIGNQNFEVKADDLEPIMELGRGAYGVVEKMRHVPSGQIMAVKRIRATVNSQEQKRLLMDLDISMRTVDCPFTVTFYGALFREGDVWICMELMDTSLDKFYKQVIDKGQTIPEDILGKIAVSIVKALEHLHSKLSVIHRDVKPSNVLINALGQVKMCDFGISGYLVDSVAKTIDAGCKPYMAPERINPELNQKGYSVKSDIWSLGITMIELAILRFPYDSWGTPFQQLKQVVEEPSPQLPADKFSAEFVDFTSQCLKKNSKERPTYPELMQHPFFTLHESKGTDVASFVKLILGD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P52564","disprot_id":"DP01342","ncbi_taxon_id":9606,"regions_counter":10,"creator":"xcastro","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":43,"region_id":"DP01342r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of non-phosphorylated MAP2K6 in a putative auto-inhibition state. <i> Matsumoto T, Kinoshita T, Matsuzaka H, Nakai R, Kirii Y, Yokota K, Tada T. </i> J Biochem, 2012","statement":[{"text":"It was likely that the R-factor and R-free values were rather high owing to the highest disordered rate. The npMAP2K6 is composed of 340 residues, with 49 residues disordered in the crystal. Although the N-terminal\nregion (residues 1-43) and the His 6 -tag were disordered, the kinase domain (residues 44-334) was ordered (Fig. 2A).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"akajava","start":1,"term_ontology":"IDPO","curator_name":"Andrey V Kajava","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2342-6886","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3VN9"}],"reference_id":"22383536","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-24T14:52:41.801Z"}},{"start":15,"end":37,"reference_id":"37708276","reference_source":"pmid","reference_html":"Architecture of the MKK6-p38α complex defines the basis of MAPK specificity and activation. <i> Juyoux P, Galdadas I, Gobbo D, von Velsen J, Pelosse M, Tully M, Vadas O, Gervasio FL, Pellegrini E, Bowler MW. </i> Science, 2023","date":"2025-10-22T13:54:25.530Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0988","term_name":"STREP","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Supplementary material","text":"For recombinant protein expression, human p38α sequences (WT, T180V, Y182F, and K53A mutants) were fused to a His6 tag with a 3C protease cleavage site and cloned into a pET-28b vector; MKK6DDGRA sequence (constitutively active S207D T211D mutant of human MKK6 with GRA24 KIM) was fused to a twin StrepII tag with a 3C cleavage site and cloned into a pFastBac1 vector."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser207Asp","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr211Asp","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"8A8M"}],"region_id":"DP01342r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q16539","statements":[{"type":"Supplementary material","text":"Purified MKK6DDGRA-p38αT180V was complemented with 250 µM AMP-CP, 250 µM NH4F and 25 µM AlCl3, and incubated on ice for 30 minutes before proceeding."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"92199"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"}],"sequence_construct":"MGSQLLERRGVSELPPLYIPKEAFEQPQTSSTPPRDLDSKACISIGNQNFEVKADDLEPIMELGRGAYGVVEKMRHVPSGQIMAVKRIRATVNSQEQKRLLMDLDISMRTVDCPFTVTFYGALFREGDVWICMELMDTSLDKFYKQVIDKGQTIPEDILGKIAVSIVKALEHLHSKLSVIHRDVKPSNVLINALGQVKMCDFGISGYLVDDVAKDIDAGCKPYMAPERINPELNQKGYSVKSDIWSLGITMIELAILRFPYDSWGTPFQQLKQVVEEPSPQLPADKFSAEFVDFTSQCLKKNSKERPTYPELMQHPFFTLHESKGTDVASFVKLILGDLEVLFQGPWSHPQFEKGGGSGGGSGGSAWSHPQFEK","statement":[{"text":"The MKK6 linker and A loop are disordered and respectively shown as a full black line and an orange dashed line.","type":"Figure"},{"text":"Most of the linker between the KIM and the MKK6 kinase core, as well as the MKK6 A loop, remains disordered and, therefore, unresolved.","type":"Results"},{"text":"Although most of the MKK6 N-terminal linker remains disordered, its length seems to be tightly linked to the substrate MAPK, and the presence of some secondary structural elements differs between MAP2Ks, contributing to specificity (Fig. 5C).","type":"Discussion"},{"text":"Manual inspection of the cryo-EM structure indicates missing residues in regions 15–37 (linker) and 205–217 (A loop).","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-06T16:58:29.122Z"}},{"start":205,"end":217,"reference_id":"37708276","reference_source":"pmid","reference_html":"Architecture of the MKK6-p38α complex defines the basis of MAPK specificity and activation. <i> Juyoux P, Galdadas I, Gobbo D, von Velsen J, Pelosse M, Tully M, Vadas O, Gervasio FL, Pellegrini E, Bowler MW. </i> Science, 2023","date":"2025-10-22T13:54:35.487Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0988","term_name":"STREP","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Supplementary material","text":"For recombinant protein expression, human p38α sequences (WT, T180V, Y182F, and K53A mutants) were fused to a His6 tag with a 3C protease cleavage site and cloned into a pET-28b vector; MKK6DDGRA sequence (constitutively active S207D T211D mutant of human MKK6 with GRA24 KIM) was fused to a twin StrepII tag with a 3C cleavage site and cloned into a pFastBac1 vector."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser207Asp","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr211Asp","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"8A8M"}],"region_id":"DP01342r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q16539","statements":[{"type":"Supplementary material","text":"Purified MKK6DDGRA-p38αT180V was complemented with 250 µM AMP-CP, 250 µM NH4F and 25 µM AlCl3, and incubated on ice for 30 minutes before proceeding."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"92199"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"}],"sequence_construct":"MGSQLLERRGVSELPPLYIPKEAFEQPQTSSTPPRDLDSKACISIGNQNFEVKADDLEPIMELGRGAYGVVEKMRHVPSGQIMAVKRIRATVNSQEQKRLLMDLDISMRTVDCPFTVTFYGALFREGDVWICMELMDTSLDKFYKQVIDKGQTIPEDILGKIAVSIVKALEHLHSKLSVIHRDVKPSNVLINALGQVKMCDFGISGYLVDDVAKDIDAGCKPYMAPERINPELNQKGYSVKSDIWSLGITMIELAILRFPYDSWGTPFQQLKQVVEEPSPQLPADKFSAEFVDFTSQCLKKNSKERPTYPELMQHPFFTLHESKGTDVASFVKLILGDLEVLFQGPWSHPQFEKGGGSGGGSGGSAWSHPQFEK","statement":[{"text":"The MKK6 linker and A loop are disordered and respectively shown as a full black line and an orange dashed line.","type":"Figure"},{"text":"Most of the linker between the KIM and the MKK6 kinase core, as well as the MKK6 A loop, remains disordered and, therefore, unresolved.","type":"Results"},{"text":"Although most of the MKK6 N-terminal linker remains disordered, its length seems to be tightly linked to the substrate MAPK, and the presence of some secondary structural elements differs between MAP2Ks, contributing to specificity (Fig. 5C).","type":"Discussion"},{"text":"Manual inspection of the cryo-EM structure indicates missing residues in regions 15–37 (linker) and 205–217 (A loop).","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-06T16:58:43.892Z"}},{"start":18,"end":37,"reference_id":"37708276","reference_source":"pmid","reference_html":"Architecture of the MKK6-p38α complex defines the basis of MAPK specificity and activation. <i> Juyoux P, Galdadas I, Gobbo D, von Velsen J, Pelosse M, Tully M, Vadas O, Gervasio FL, Pellegrini E, Bowler MW. </i> Science, 2023","date":"2026-06-19T07:10:36.613Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IMP","region_id":"DP01342r004","statement":[{"text":"Our results show that the sequence of the middle region (MKK6DD Ala scan 28 to 39) of the N-terminal linker has no effect on p38α signaling in cellulo. However, the sequence of the linker close to the KIM (MKK6DD Ala scan 18 to 29) and the region close to the kinase core, which comprises the predicted β strands (MKK6DD Ala scan 38 to 49) (Fig. 5) seem to have some importance because their mutation to alanine reduced p38α signaling by 27 and 58%, respectively.","type":"Results"},{"text":"By removing or adding 10 residues to the linker region, activity is reduced by ~50%. This implies that the length of the linker, controlled by the number of amino acids and/or by secondary-structure elements, is important in the positioning of the MAP2K for engagement with the MAPK and is finely tuned for MAP kinase pairs.","type":"Results"}],"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of MAP kinase activity.\" [GOC:dph, GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"xcastro","last_modified_name":"Ximena Aixa Castro","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-24T17:56:45.425Z"}},{"start":15,"end":37,"reference_id":"37708276","reference_source":"pmid","reference_html":"Architecture of the MKK6-p38α complex defines the basis of MAPK specificity and activation. <i> Juyoux P, Galdadas I, Gobbo D, von Velsen J, Pelosse M, Tully M, Vadas O, Gervasio FL, Pellegrini E, Bowler MW. </i> Science, 2023","date":"2025-10-22T14:16:48.142Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0988","term_name":"STREP","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Supplementary material","text":"For recombinant protein expression, human p38α sequences (WT, T180V, Y182F, and K53A mutants) were fused to a His6 tag with a 3C protease cleavage site and cloned into a pET-28b vector; MKK6DDGRA sequence (constitutively active S207D T211D mutant of human MKK6 with GRA24 KIM) was fused to a twin StrepII tag with a 3C cleavage site and cloned into a pFastBac1 vector."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser207Asp","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr211Asp","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"8A8M"}],"region_id":"DP01342r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q16539","statements":[{"type":"Supplementary material","text":"Purified MKK6DDGRA-p38αT180V was complemented with 250 µM AMP-CP, 250 µM NH4F and 25 µM AlCl3, and incubated on ice for 30 minutes before proceeding."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"92199"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"}],"sequence_construct":"MGSQLLERRGVSELPPLYIPKEAFEQPQTSSTPPRDLDSKACISIGNQNFEVKADDLEPIMELGRGAYGVVEKMRHVPSGQIMAVKRIRATVNSQEQKRLLMDLDISMRTVDCPFTVTFYGALFREGDVWICMELMDTSLDKFYKQVIDKGQTIPEDILGKIAVSIVKALEHLHSKLSVIHRDVKPSNVLINALGQVKMCDFGISGYLVDDVAKDIDAGCKPYMAPERINPELNQKGYSVKSDIWSLGITMIELAILRFPYDSWGTPFQQLKQVVEEPSPQLPADKFSAEFVDFTSQCLKKNSKERPTYPELMQHPFFTLHESKGTDVASFVKLILGDLEVLFQGPWSHPQFEKGGGSGGGSGGSAWSHPQFEK","statement":[{"text":"The MKK6 linker and A loop are disordered and respectively shown as a full black line and an orange dashed line.","type":"Figure"},{"text":"Most of the linker between the KIM and the MKK6 kinase core, as well as the MKK6 A loop, remains disordered and, therefore, unresolved.","type":"Results"},{"text":"Manual inspection of the cryo-EM structure indicates missing residues in region 15–37 (linker).","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-06T17:08:51.575Z"}},{"start":207,"end":211,"reference_id":"8622669","reference_source":"pmid","reference_html":"MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-activated protein kinase signal transduction pathway. <i> Raingeaud J, Whitmarsh AJ, Barrett T, Dérijard B, Davis RJ. </i> Mol Cell Biol, 1996","date":"2025-10-23T09:05:13.341Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001247","ec_ontology":"ECO","ec_name":"point mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":207,"end":207,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":211,"end":211,"position":"Specific residue"}],"region_id":"DP01342r006","statement":[{"text":"The mechanism of MKK6 activation may therefore be mediated by increased negative charge on Ser-207 and Thr-211. To test this hypothesis, we examined the effect of introducing a constitutive negative charge by replacing Ser-207 and Thr-211 with Glu.","type":"Results"},{"text":"Similarly, MKK6 is activated by dual phosphorylation on Ser-207 and Thr-211 (Fig. 5).","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-06T17:10:51.063Z"}},{"start":207,"end":211,"reference_id":"8622669","reference_source":"pmid","reference_html":"MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-activated protein kinase signal transduction pathway. <i> Raingeaud J, Whitmarsh AJ, Barrett T, Dérijard B, Davis RJ. </i> Mol Cell Biol, 1996","date":"2026-05-15T10:59:36.407Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"GO:0004708","term_name":"MAP kinase kinase activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001247","ec_ontology":"ECO","ec_name":"point mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser207Glu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr211Glu","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP01342r007","statement":[{"text":"The mechanism of MKK6 activation may therefore be mediated by increased negative charge on Ser-207 and Thr-211. To test this hypothesis, we examined the effect of introducing a constitutive negative charge by replacing Ser-207 and Thr-211 with Glu. MKK6(Glu) caused activation of wild-type (Thr-Gly-Tyr) p38 MAP kinase but not activation of the phosphorylation-defective (Ala-Gly-Phe) mutant (Fig. 7B). In contrast, kinase-negative MKK6 did not activate p38 MAP kinase (Fig. 7B). Together, these data demonstrate that MKK6(Glu) is an activator of p38 MAP kinase in vivo.","type":"Results"},{"text":"Similarly, MKK6 is activated by dual phosphorylation on Ser-207 and Thr-211 (Fig. 5).","type":"Discussion"}],"term_comment":"","term_def":"\"Catalysis of the concomitant phosphorylation of threonine (T) and tyrosine (Y) residues in a Thr-Glu-Tyr (TEY) thiolester sequence in a MAP kinase (MAPK) substrate.\" [ISBN:0198547684]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"xcastro","last_modified_name":"Ximena Aixa Castro","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T15:50:00.849Z"}},{"start":207,"end":211,"reference_id":"16728640","reference_source":"pmid","reference_html":"Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation. <i> Mukherjee S, Keitany G, Li Y, Wang Y, Ball HL, Goldsmith EJ, Orth K. </i> Science, 2006","date":"2025-10-23T10:11:58.746Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000039","term_name":"acetylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007713","ec_ontology":"ECO","ec_name":"acetylation assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","start":207,"end":207,"position":"Specific residue"},{"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","start":211,"end":211,"position":"Specific residue"}],"region_id":"DP01342r009","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"73755097","statements":[{"type":"Results","text":"rMAPKK6 was modified with the 14C-labeled acetyl moiety only in the presence of recombinant YopJ expressed as a glutathione S-transferase fusion protein (GST-YopJ) and the labeled acetyl donor [14C]acetyl-CoA (Fig. 3A)."}]}],"statement":[{"text":"rMAPKK6, coexpressed with YopJ and shown to be acetylated at Ser207 and Thr211 (Fig. 2, B and C), was not phosphorylated by upstream signaling machinery (Fig. 1D).","type":"Results"},{"text":"To determine whether YopJ directly functions as an acetyltransferase, we performed a transferase reaction in the presence of 14C-labeled acetyl–coenzyme A (CoA) (12). rMAPKK6 was modified with the 14C-labeled acetyl moiety only in the presence of recombinant YopJ expressed as a glutathione S-transferase fusion protein (GST-YopJ) and the labeled acetyl donor [14C]acetyl-CoA (Fig. 3A).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-06T17:22:13.918Z"}}],"released":"2018_11","uniref100":"UniRef100_P52564","date":"2018-07-12T13:01:52.000Z","acc":"P52564","name":"Dual specificity mitogen-activated protein kinase kinase 6","length":334,"organism":"Homo sapiens","dataset":["Stress response proteins"],"UniParc":"UPI000012F492","genes":[{"name":{"value":"MAP2K6"},"synonyms":[{"value":"MEK6"},{"value":"MKK6"},{"value":"PRKMK6"},{"value":"SKK3"}]}],"alphafold_very_low_content":0.10778443113772455,"disorder_content":0.16766467065868262,"disprot_consensus":{"full":[{"start":1,"end":43,"type":"D"},{"start":205,"end":217,"type":"D"}],"Structural state":[{"start":1,"end":43,"type":"D"},{"start":205,"end":217,"type":"D"}],"Disorder function":[{"start":15,"end":37,"type":"F"},{"start":207,"end":211,"type":"F"}],"Molecular function":[{"start":207,"end":211,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00554","name":"Rel homology DNA-binding domain","start":410,"end":570},{"id":"PF16179","name":"Rel homology dimerisation domain","start":580,"end":678}],"gene3D":[{"start":397,"end":571,"id":"2.60.40.340","name":"Rel homology domain (RHD), DNA-binding domain"},{"start":572,"end":676,"id":"2.60.40.10","name":"Immunoglobulins"}]},"uniref50":"UniRef50_Q13469","sequence":"MNAPERQPQPDGGDAPGHEPGGSPQDELDFSILFDYEYLNPNEEEPNAHKVASPPSGPAYPDDVLDYGLKPYSPLASLSGEPPGRFGEPDRVGPQKFLSAAKPAGASGLSPRIEITPSHELIQAVGPLRMRDAGLLVEQPPLAGVAASPRFTLPVPGFEGYREPLCLSPASSGSSASFISDTFSPYTSPCVSPNNGGPDDLCPQFQNIPAHYSPRTSPIMSPRTSLAEDSCLGRHSPVPRPASRSSSPGAKRRHSCAEALVALPPGASPQRSRSPSPQPSSHVAPQDHGSPAGYPPVAGSAVIMDALNSLATDSPCGIPPKMWKTSPDPSPVSAAPSKAGLPRHIYPAVEFLGPCEQGERRNSAPESILLVPPTWPKPLVPAIPICSIPVTASLPPLEWPLSSQSGSYELRIEVQPKPHHRAHYETEGSRGAVKAPTGGHPVVQLHGYMENKPLGLQIFIGTADERILKPHAFYQVHRITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRNADIELRKGETDIGRKNTRVRLVFRVHIPESSGRIVSLQTASNPIECSQRSAHELPMVERQDTDSCLVYGGQQMILTGQNFTSESKVVFTEKTTDGQQIWEMEATVDKDKSQPNMLFVEIPEYRNKHIRTPVKVNFYVINGKRKRSQPQHFTYHPVPAIKTEPTDEYDPTLICSPTHGGLGSQPYYPQHPMVAESPSCLVATMAPCQQFRTGLSSPDARYQQQNPAAVLYQRSKSLSPSLLGYQQPALMAAPLSLADAHRSVLVHAGSQGQSSALLHPSPTNQQASPVIHYSPTNQQLRCGSHQEFQHIMYCENFAPGTTRPGPPPVSQGQRLSPGSYPTVIQQQNATSQRAAKNGPPVSDQKEVLPAGVTIKQEQNLDQTYLDDVNEIIRKEFSGPPARNQT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q13469","disprot_id":"DP01344","ncbi_taxon_id":9606,"regions_counter":4,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":294,"region_id":"DP01344r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"<sup>15</sup>N detection harnesses the slow relaxation property of nitrogen: Delivering enhanced resolution for intrinsically disordered proteins. <i> Chhabra S, Fischer P, Takeuchi K, Dubey A, Ziarek JJ, Boeszoermenyi A, Mathieu D, Bermel W, Davey NE, Wagner G, Arthanari H. </i> Proc Natl Acad Sci U S A, 2018","statement":[{"text":"These 15N-detected experiments were used to assign the backbone resonances of human transcription factor nuclear factor of activated T cells (NFATC2) (residues 131–294). This portion of NFAT is disordered.","type":"Introduction"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":131,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29432148","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":294,"term_name":"molecular adaptor activity","released":"2022_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"<sup>15</sup>N detection harnesses the slow relaxation property of nitrogen: Delivering enhanced resolution for intrinsically disordered proteins. <i> Chhabra S, Fischer P, Takeuchi K, Dubey A, Ziarek JJ, Boeszoermenyi A, Mathieu D, Bermel W, Davey NE, Wagner G, Arthanari H. </i> Proc Natl Acad Sci U S A, 2018","statement":[{"text":"Our data demonstrate that, upon PKA phosphorylation, 14-3-3 binds to NFAT and blocks access to the nuclear localization sequence (NLS), which may prevent the nuclear transport protein importin from translocating NFAT to the nucleus, thus preventing transcriptional activation","type":"Introduction"}],"term_id":"GO:0060090","curator_id":"vnugnes","start":131,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"29432148","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-15T19:05:42.358Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01344r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":225,"end":225,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":255,"end":255,"position":"Specific residue"}]},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":294,"term_name":"phosphorylation display site","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"<sup>15</sup>N detection harnesses the slow relaxation property of nitrogen: Delivering enhanced resolution for intrinsically disordered proteins. <i> Chhabra S, Fischer P, Takeuchi K, Dubey A, Ziarek JJ, Boeszoermenyi A, Mathieu D, Bermel W, Davey NE, Wagner G, Arthanari H. </i> Proc Natl Acad Sci U S A, 2018","statement":[{"text":"PKA phosphorylation resulted in downfield shifts of the 1H resonances of two serine residues that are assigned to S-225 and S-255.","type":"Results"}],"term_id":"IDPO:0000045","curator_id":"ndavey","start":131,"term_ontology":"IDPO","curator_name":"Norman Davey","reference_id":"29432148","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01344r003","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":294,"term_name":"14-3-3 protein binding","released":"2022_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"<sup>15</sup>N detection harnesses the slow relaxation property of nitrogen: Delivering enhanced resolution for intrinsically disordered proteins. <i> Chhabra S, Fischer P, Takeuchi K, Dubey A, Ziarek JJ, Boeszoermenyi A, Mathieu D, Bermel W, Davey NE, Wagner G, Arthanari H. </i> Proc Natl Acad Sci U S A, 2018","statement":[{"text":"PKA phosphorylation of NFAT promotes its association with the 14-3-3 chaperone protein, which results in the inhibition of NFAT transcriptional activity (26).","type":"Results"}],"term_id":"GO:0071889","curator_id":"vnugnes","start":131,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"29432148","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-15T19:06:21.823Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01344r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a 14-3-3 protein. A 14-3-3 protein is any of a large family of approximately 30kDa acidic proteins which exist primarily as homo- and heterodimers within all eukaryotic cells, and have been implicated in the modulation of distinct biological processes by binding to specific phosphorylated sites on diverse target proteins, thereby forcing conformational changes or influencing interactions between their targets and other molecules. Each 14-3-3 protein sequence can be roughly divided into three sections: a divergent amino terminus, the conserved core region and a divergent carboxy-terminus. The conserved middle core region of the 14-3-3s encodes an amphipathic groove that forms the main functional domain, a cradle for interacting with client proteins.\" [GOC:cna, GOC:mah, PMID:15167810, PMID:19575580]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":225,"end":225,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":255,"end":255,"position":"Specific residue"}],"interaction_partner":[{"db":"UniProt","id":"P27348","operator":"and","partner_start":null,"partner_end":null}]}],"released":"2018_11","uniref100":"UniRef100_Q13469","date":"2018-07-13T07:56:41.000Z","acc":"Q13469","name":"Nuclear factor of activated T-cells, cytoplasmic 2","length":925,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI000012FFB7","genes":[{"name":{"value":"NFATC2"},"synonyms":[{"value":"NFAT1"},{"value":"NFATP"}]}],"alphafold_very_low_content":0.6410810810810811,"disorder_content":0.1772972972972973,"disprot_consensus":{"full":[{"start":131,"end":294,"type":"D"}],"Structural state":[{"start":131,"end":294,"type":"D"}],"Molecular function":[{"start":131,"end":294,"type":"F"}],"Disorder function":[{"start":131,"end":294,"type":"F"}]}},{"features":{"pfam":[{"id":"PF12998","name":"Inhibitor of growth proteins N-terminal histone-binding","start":6,"end":107}],"gene3D":[{"start":189,"end":246,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"}]},"uniref50":"UniRef50_Q9UNL4","sequence":"MAAGMYLEHYLDSIENLPFELQRNFQLMRDLDQRTEDLKAEIDKLATEYMSSARSLSSEEKLALLKQIQEAYGKCKEFGDDKVQLAMQTYEMVDKHIRRLDTDLARFEADLKEKQIESSDYDSSSSKGKKKGRTQKEKKAARARSKGKNSDEEAPKTAQKKLKLVRTSPEYGMPSVTFGSVHPSDVLDMPVDPNEPTYCLCHQVSYGEMIGCDNPDCSIEWFHFACVGLTTKPRGKWFCPRCSQERKKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UNL4","disprot_id":"DP01347","ncbi_taxon_id":9606,"regions_counter":2,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":188,"region_id":"DP01347r001","released":"2022_12","ec_id":"ECO:0006204","reference_html":"The dimeric structure and the bivalent recognition of H3K4me3 by the tumor suppressor ING4 suggests a mechanism for enhanced targeting of the HBO1 complex to chromatin. <i> Palacios A, Moreno A, Oliveira BL, Rivera T, Prieto J, García P, Fernández-Fernández MR, Bernadó P, Palmero I, Blanco FJ. </i> J Mol Biol, 2010","statement":[{"text":"The shape of the spectra of Nt_NLS and NLS_PHD can be explained by the combination of the spectra of Nt\nor PHD, respectively, and the spectrum of a random-coil chain: less negative ellipticity at 222 nm, less positive ellipticity at 190 nm, and a shift to lower wavelengths of the Nt minimum at 208 nm and the PHD minimum at 202 nm. These results suggest that NLS behaves as a disordered random coil.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":119,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-24T15:06:58.998Z","reference_source":"pmid","term_name":"disorder","reference_id":"20053357","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9UNL4","date":"2018-07-13T08:13:47.000Z","acc":"Q9UNL4","name":"Inhibitor of growth protein 4","length":249,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000006EFE0","genes":[{"name":{"value":"ING4"},"orfNames":[{"value":"My036"}]}],"alphafold_very_low_content":0.20883534136546184,"disorder_content":0.28112449799196787,"disprot_consensus":{"full":[{"start":119,"end":188,"type":"D"}],"Structural state":[{"start":119,"end":188,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01789","name":"PsbP","start":98,"end":266}],"gene3D":[{"start":82,"end":267,"id":"3.40.1000.10","name":"Mog1/PsbP, alpha/beta/alpha sandwich"}]},"uniref50":"UniRef50_P12302","sequence":"MASTACFLHHHAAISSPAAGRGSAAQRYQAVSIKPNQIVCKAQKQDDNEANVLNSGVSRRLALTVLIGAAAVGSKVSPADAAYGEAANVFGKPKKNTEFMPYNGDGFKLLVPSKWNPSKEKEFPGQVLRYEDNFDATSNLSVLVQPTDKKSITDFGSPEDFLSQVDYLLGKQAYFGKTDSEGGFDSGVVASANVLESSTPVVDGKQYYSITVLTRTADGDEGGKHQVIAATVKDGKLYICKAQAGDKRWFKGAKKFVESATSSFSVA","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","Caryophyllales","Chenopodiaceae","Chenopodioideae","Anserineae","Spinacia"],"uniref90":"UniRef90_P12302","disprot_id":"DP01351","ncbi_taxon_id":3562,"regions_counter":7,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":188,"region_id":"DP01351r001","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Raman spectroscopy adds complementary detail to the high-resolution x-ray crystal structure of photosynthetic PsbP from Spinacia oleracea. <i> Kopecky V, Kohoutova J, Lapkouski M, Hofbauerova K, Sovova Z, Ettrichova O, González-Pérez S, Dulebo A, Kaftan D, Smatanova IK, Revuelta JL, Arellano JB, Carey J, Ettrich R. </i> PLoS One, 2012","statement":[{"text":"Although purified spinach PsbP protein shows no degradation products by analytical SDS gel electrophoresis and full-length protein is recovered from dissolved crystals as reported already [35], the electron density is not resolved in the N-terminal region (residues 1–15) and in two internal regions (residues 90–107 and 135–139), as in the structure of tobacco PsbP (PDB ID 1V2B [33]; Figure 1).","type":"Results"},{"text":"Unresolved residues (90-107) correspond to residues 171-188 in Uniprot","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":171,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-24T15:31:55.622Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2VU4"}],"reference_id":"23071614","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":92,"region_id":"DP01351r002","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Crystal structure analysis of extrinsic PsbP protein of photosystem II reveals a manganese-induced conformational change. <i> Cao P, Xie Y, Li M, Pan X, Zhang H, Zhao X, Su X, Cheng T, Chang W. </i> Mol Plant, 2015","statement":[{"text":" Except for the N-terminal 11 residues, we constructed the structure of spinach PsbP in its entirety for the first time (P12 to A186) (Figure 1A).","type":"Article"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":82,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-24T15:32:32.971Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4RTI"}],"reference_id":"25704164","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29035","entry_name":"manganese(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":188,"term_name":"manganese ion binding","released":"2024_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure analysis of extrinsic PsbP protein of photosystem II reveals a manganese-induced conformational change. <i> Cao P, Xie Y, Li M, Pan X, Zhang H, Zhao X, Su X, Cheng T, Chang W. </i> Mol Plant, 2015","statement":[{"text":"Our structures add crucial structural information for PsbP, with two Mn ions identified inside PsbP for the first time. We propose that one of the ions is responsible for a dramatic conformational change (with a maximum move of 20 Å) that is revealed here within the long region (aa 90–107).","type":"Article"},{"text":"We propose that the observed conformational change in the loop90–107 region is induced by binding of Mn2.","type":"Article"}],"term_id":"GO:0030145","curator_id":"vnugnes","start":171,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"25704164","version":5,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-01T14:51:30.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01351r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a manganese ion (Mn).\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"4RTI"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29035","entry_name":"manganese(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"}],"interaction_partner":[{"db":"ChEBI","id":"29035","operator":"and","partner_start":null,"partner_end":null}]},{"start":82,"end":96,"reference_id":"23071614","reference_source":"pmid","reference_html":"Raman spectroscopy adds complementary detail to the high-resolution x-ray crystal structure of photosynthetic PsbP from Spinacia oleracea. <i> Kopecky V, Kohoutova J, Lapkouski M, Hofbauerova K, Sovova Z, Ettrichova O, González-Pérez S, Dulebo A, Kaftan D, Smatanova IK, Revuelta JL, Arellano JB, Carey J, Ettrich R. </i> PLoS One, 2012","date":"2022-08-24T15:31:43.046Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"2VU4"}],"region_id":"DP01351r004","statement":[{"text":"Although purified spinach PsbP protein shows no degradation products by analytical SDS gel electrophoresis and full-length protein is recovered from dissolved crystals as reported already [35], the electron density is not resolved in the N-terminal region (residues 1–15) and in two internal regions (residues 90–107 and 135–139), as in the structure of tobacco PsbP (PDB ID 1V2B [33]; Figure 1).","type":"Results"},{"text":"Unresolved residues (1-15) correspond to residues 82-96 in Uniprot.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}]},{"start":117,"end":188,"reference_id":"25704164","reference_source":"pmid","reference_html":"Crystal structure analysis of extrinsic PsbP protein of photosystem II reveals a manganese-induced conformational change. <i> Cao P, Xie Y, Li M, Pan X, Zhang H, Zhao X, Su X, Cheng T, Chang W. </i> Mol Plant, 2015","date":"2022-08-24T15:35:02.011Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"4RTI"}],"region_id":"DP01351r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29035","entry_name":"manganese(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"}],"statement":[{"text":"The two internal segments (aa 90–107 and aa 134–139), unresolved in the previous structures, were unambiguously defined in our structure based on their electron density maps (Supplemental Figure 2), with both segments exhibiting a loop conformation.","type":"Article"},{"text":"We propose that the observed conformational change in the loop90–107 region is induced by binding of Mn2.","type":"Article"}]},{"start":117,"end":188,"reference_id":"25704164","reference_source":"pmid","reference_html":"Crystal structure analysis of extrinsic PsbP protein of photosystem II reveals a manganese-induced conformational change. <i> Cao P, Xie Y, Li M, Pan X, Zhang H, Zhao X, Su X, Cheng T, Chang W. </i> Mol Plant, 2015","date":"2022-08-24T15:36:28.444Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"4RTI"}],"region_id":"DP01351r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29035","entry_name":"manganese(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"}],"statement":[{"text":"The two internal segments (aa 90–107 and aa 134–139), unresolved in the previous structures, were unambiguously defined in our structure based on their electron density maps (Supplemental Figure 2), with both segments exhibiting a loop conformation.","type":"Article"},{"text":"We propose that the observed conformational change in the loop90–107 region is induced by binding of Mn2.","type":"Article"}],"states_connection":[{"source":"DP01351r001","target":"DP01351r005"}]},{"start":1,"end":95,"reference_id":"27251276","reference_source":"pmid","reference_html":"Structure of spinach photosystem II-LHCII supercomplex at 3.2 Å resolution. <i> Wei X, Su X, Cao P, Liu X, Chang W, Li M, Zhang X, Liu Z. </i> Nature, 2016","date":"2022-08-24T18:29:07.218Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"3JCU"},{"db":"EMDB","id":"EMD-6617"}],"region_id":"DP01351r007","statement":[{"text":"In the Cryo-EM structure of spinach PSII-LHCII supercomplex portrayed in the PDB this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"released":"2018_11","uniref100":"UniRef100_P12302","date":"2018-07-13T08:24:42.000Z","acc":"P12302","name":"Oxygen-evolving enhancer protein 2, chloroplastic","length":267,"organism":"Spinacia oleracea","dataset":[],"UniParc":"UPI0000132735","genes":[{"name":{"value":"PSBP"}}],"alphafold_very_low_content":0.2546816479400749,"disorder_content":0.6292134831460674,"disprot_consensus":{"full":[{"start":1,"end":96,"type":"D"},{"start":117,"end":188,"type":"T"}],"Structural state":[{"start":1,"end":96,"type":"D"},{"start":117,"end":170,"type":"S"},{"start":171,"end":188,"type":"D"}],"Molecular function":[{"start":171,"end":188,"type":"F"}],"Structural transition":[{"start":117,"end":188,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00481","name":"Protein phosphatase 2C","start":311,"end":570},{"id":"PF00498","name":"FHA domain","start":208,"end":284}],"gene3D":[{"start":311,"end":580,"id":"3.60.40.10","name":"PPM-type phosphatase domain"},{"start":176,"end":310,"id":"2.60.200.20","name":"2.60.200.20"}]},"uniref50":"UniRef50_P46014","sequence":"MAMIGMNIIGLFMVLMLLLISLIILFACKPWRYFSRFRSSSRFSSTFKVGDLQRPLISDDGNLIQGQTSEVTREYDLEGACYQNDGLLHSSLTEGRFYKQRLPSSSPHFSQGESFVLEVISEPSDNALVGQTLKLPAEKGSLAEVQTYDWQNNRNENLQYNLEKDRLINLSPRLVEDQRSWLFLEVIAGPAIGLQHAVNSTSSSKLPVKLGRVSPSDLALKDSEVSGKHAQITWNSTKFKWELVDMGSLNGTLVNSHSISHPDLGSRKWGNPVELASDDIITLGTTTKVYVRISSQNEFQIPFKIGVASDPMAMRRGGRKLPMEDVCHYKWPLPGANKFGLFCVCDGHGGSGAAQSAIKIIPEVLANILSDSLRKEKVLSKRDASDVLRDMFAKTEARLEEHQYEGCTATVLLVWKDNEENFFAQCANLGDSACVIHLGGRYIQMTEDHRVVSLSERKRFQEAGLALRDGETRLFGINLARMLGDKFPKQQDSRFSAEPYISEPLRIDQSSKDVFAVLASDGLWDVVSPKKAVQLVLQMRDKERGRESSAEKIANGLLNEARAMRTKDNTSIIYLDFDTSL","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_P46014","disprot_id":"DP01355","ncbi_taxon_id":3702,"regions_counter":1,"creator":"jmanso","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":313,"region_id":"DP01355r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase. <i> Lee GI, Ding Z, Walker JC, Van Doren SR. </i> Proc Natl Acad Sci U S A, 2003","statement":[{"text":"C-terminal residues 299–313 appear to be unstructured","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jmanso","start":299,"term_ontology":"IDPO","curator_name":"Jose A Manso","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1MZK"}],"reference_id":"14500786","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P46014","date":"2018-07-13T14:56:37.000Z","acc":"P46014","name":"Protein phosphatase 2C 70","length":581,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI00001797A0","genes":[{"name":{"value":"KAPP","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"7973632","url":"http://www.ncbi.nlm.nih.gov/pubmed/7973632","alternativeUrl":"https://europepmc.org/abstract/MED/7973632"}}]},"synonyms":[{"value":"RAG1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"18162596","url":"http://www.ncbi.nlm.nih.gov/pubmed/18162596","alternativeUrl":"https://europepmc.org/abstract/MED/18162596"}}]}],"orfNames":[{"value":"F7K24.30"},{"value":"T24G5.3"}],"olnNames":[{"value":"At5g19280"}]}],"alphafold_very_low_content":0.25989672977624784,"disorder_content":0.025817555938037865,"disprot_consensus":{"full":[{"start":299,"end":313,"type":"D"}],"Structural state":[{"start":299,"end":313,"type":"D"}]}},{"features":{"pfam":[{"id":"PF05711","name":"Macrocin-O-methyltransferase (TylF)","start":21,"end":252}],"gene3D":[{"start":6,"end":253,"id":"3.40.50.150","name":"Vaccinia Virus protein VP39"}]},"uniref50":"UniRef50_Q9S4D5","sequence":"MSPSTGVELYLDLLKRTVSNFIYQDATHVAGLITEAAFVEEARESGEDYPTVAHTMIGMKRLNNLQHCVESALRDGVPGDVLETGVWRGGACIFARGILKAYDVRDRTVWVADSFQGFPKITDDDHPMDAEMNLHQYNEAVDLPTSLATVQRNFSRYGLLDDQVRFLPGWFKDTMPTAPFERLAVLRMDGDSYGATMDVLTHAYPRLSPGGFAIIDDYCIPACREAVHEYRDRHGISDEIVEIDRQGVYWRRSA","taxonomy":["Bacteria","Actinobacteria","Micromonosporales","Micromonosporaceae","Micromonospora"],"uniref90":"UniRef90_Q49492","disprot_id":"DP01356","ncbi_taxon_id":28040,"regions_counter":3,"creator":"jmanso","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":144,"region_id":"DP01356r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis of substrate specificity and regiochemistry in the MycF/TylF family of sugar O-methyltransferases. <i> Bernard SM, Akey DL, Tripathi A, Park SR, Konwerski JR, Anzai Y, Li S, Kato F, Sherman DH, Smith JL. </i> ACS Chem Biol, 2015","statement":[{"text":"MycF WT crystal contents Mg-disordered lid. The active site of MycF becomes progressively more ordered as the cosubstrate and substrate bind. SAM/SAH binding to MycF closes the helical lid domain over the cosubstrate, partially orders the lid loop, and forms the binding site for the substrate mycinamicin III, which orders the remainder of the lid loop.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jmanso","start":116,"term_ontology":"IDPO","curator_name":"Jose A Manso","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4XVZ"}],"reference_id":"25692963","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":144,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural basis of substrate specificity and regiochemistry in the MycF/TylF family of sugar O-methyltransferases. <i> Bernard SM, Akey DL, Tripathi A, Park SR, Konwerski JR, Anzai Y, Li S, Kato F, Sherman DH, Smith JL. </i> ACS Chem Biol, 2015","term_id":"IDPO:0000011","curator_id":"jmanso","start":116,"term_ontology":"IDPO","curator_name":"Jose A Manso","reference_id":"25692963","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01356r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":144,"term_name":"small molecule binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural basis of substrate specificity and regiochemistry in the MycF/TylF family of sugar O-methyltransferases. <i> Bernard SM, Akey DL, Tripathi A, Park SR, Konwerski JR, Anzai Y, Li S, Kato F, Sherman DH, Smith JL. </i> ACS Chem Biol, 2015","term_id":"GO:0036094","curator_id":"jmanso","start":116,"term_ontology":"GO","curator_name":"Jose A Manso","reference_id":"25692963","version":3,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01356r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q49492","date":"2018-07-13T16:36:56.000Z","acc":"Q49492","name":"Mycinamicin III 3''-O-methyltransferase","length":254,"organism":"Micromonospora griseorubida","dataset":[],"UniParc":"UPI00000BD58F","genes":[{"name":{"value":"mycF"}}],"alphafold_very_low_content":0,"disorder_content":0.1141732283464567,"disprot_consensus":{"full":[{"start":116,"end":144,"type":"T"}],"Structural state":[{"start":116,"end":144,"type":"D"}],"Structural transition":[{"start":116,"end":144,"type":"T"}],"Molecular function":[{"start":116,"end":144,"type":"F"}]}},{"features":{"pfam":[{"id":"PF08784","name":"Replication protein A C terminal","start":166,"end":262}],"gene3D":[{"start":200,"end":270,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"start":41,"end":172,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}]},"uniref50":"UniRef50_P15927","sequence":"MWNSGFESYGSSSYGGAGGYTQSPGGFGSPAPSQAEKKSRARAQHIVPCTISQLLSATLVDEVFRIGNVEISQVTIVGIIRHAEKAPTNIVYKIDDMTAAPMDVRQWVDTDDTSSENTVVPPETYVKVAGHLRSFQNKKSLVAFKIMPLEDMNEFTTHILEVINAHMVLSKANSQPSAGRAPISNPGMSEAGNFGGNSFMPANGLTVAQNQVLNLIKACPRPEGLNFQDLKNQLKHMSVSSIKQAVDFLSNEGHIYSTVDDDHFKSTDAE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P15927","disprot_id":"DP01361","ncbi_taxon_id":9606,"regions_counter":2,"creator":"baykac","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":42,"region_id":"DP01361r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the full-length human RPA14/32 complex gives insights into the mechanism of DNA binding and complex formation. <i> Deng X, Habel JE, Kabaleeswaran V, Snell EH, Wold MS, Borgstahl GE. </i> J Mol Biol, 2007","term_id":"IDPO:0000002","curator_id":"baykac","start":1,"term_ontology":"IDPO","curator_name":"Burcu Aykac-Fas","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-3842-731X","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2PI2"}],"reference_id":"17976647","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":270,"region_id":"DP01361r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the full-length human RPA14/32 complex gives insights into the mechanism of DNA binding and complex formation. <i> Deng X, Habel JE, Kabaleeswaran V, Snell EH, Wold MS, Borgstahl GE. </i> J Mol Biol, 2007","term_id":"IDPO:0000002","curator_id":"baykac","start":175,"term_ontology":"IDPO","curator_name":"Burcu Aykac-Fas","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-3842-731X","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2PI2"}],"reference_id":"17976647","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P15927","date":"2018-07-13T18:36:28.000Z","acc":"P15927","name":"Replication protein A 32 kDa subunit","length":270,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000013379F","genes":[{"name":{"value":"RPA2"},"synonyms":[{"value":"REPA2"},{"value":"RPA32"},{"value":"RPA34"}]}],"alphafold_very_low_content":0.2037037037037037,"disorder_content":0.5111111111111111,"disprot_consensus":{"full":[{"start":1,"end":42,"type":"D"},{"start":175,"end":270,"type":"D"}],"Structural state":[{"start":1,"end":42,"type":"D"},{"start":175,"end":270,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00071","name":"Ras family","start":12,"end":168}],"gene3D":[{"start":1,"end":216,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_P62826","sequence":"MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P62826","disprot_id":"DP01364","ncbi_taxon_id":9606,"regions_counter":3,"creator":"baykac","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":44,"region_id":"DP01364r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Next-generation XPO1 inhibitor shows improved efficacy and in vivo tolerability in hematological malignancies. <i> Hing ZA, Fung HY, Ranganathan P, Mitchell S, El-Gamal D, Woyach JA, Williams K, Goettl VM, Smith J, Yu X, Meng X, Sun Q, Cagatay T, Lehman AM, Lucas DM, Baloglu E, Shacham S, Kauffman MG, Byrd JC, Chook YM, Garzon R, Lapalombella R. </i> Leukemia, 2016","term_id":"IDPO:0000002","curator_id":"baykac","start":33,"term_ontology":"IDPO","curator_name":"Burcu Aykac-Fas","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-3842-731X","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5JLJ"}],"reference_id":"27323910","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":144,"region_id":"DP01364r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Next-generation XPO1 inhibitor shows improved efficacy and in vivo tolerability in hematological malignancies. <i> Hing ZA, Fung HY, Ranganathan P, Mitchell S, El-Gamal D, Woyach JA, Williams K, Goettl VM, Smith J, Yu X, Meng X, Sun Q, Cagatay T, Lehman AM, Lucas DM, Baloglu E, Shacham S, Kauffman MG, Byrd JC, Chook YM, Garzon R, Lapalombella R. </i> Leukemia, 2016","term_id":"IDPO:0000002","curator_id":"baykac","start":123,"term_ontology":"IDPO","curator_name":"Burcu Aykac-Fas","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-3842-731X","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5JLJ"}],"reference_id":"27323910","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":198,"region_id":"DP01364r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Next-generation XPO1 inhibitor shows improved efficacy and in vivo tolerability in hematological malignancies. <i> Hing ZA, Fung HY, Ranganathan P, Mitchell S, El-Gamal D, Woyach JA, Williams K, Goettl VM, Smith J, Yu X, Meng X, Sun Q, Cagatay T, Lehman AM, Lucas DM, Baloglu E, Shacham S, Kauffman MG, Byrd JC, Chook YM, Garzon R, Lapalombella R. </i> Leukemia, 2016","term_id":"IDPO:0000002","curator_id":"baykac","start":170,"term_ontology":"IDPO","curator_name":"Burcu Aykac-Fas","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-3842-731X","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5JLJ"}],"reference_id":"27323910","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P62826","date":"2018-07-13T18:36:55.000Z","acc":"P62826","name":"GTP-binding nuclear protein Ran","length":216,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000000DE2","genes":[{"name":{"value":"RAN"},"synonyms":[{"value":"ARA24","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10400640","url":"http://www.ncbi.nlm.nih.gov/pubmed/10400640","alternativeUrl":"https://europepmc.org/abstract/MED/10400640"}}]}],"orfNames":[{"value":"OK/SW-cl.81"}]}],"alphafold_very_low_content":0.037037037037037035,"disorder_content":0.2916666666666667,"disprot_consensus":{"full":[{"start":33,"end":44,"type":"D"},{"start":123,"end":144,"type":"D"},{"start":170,"end":198,"type":"D"}],"Structural state":[{"start":33,"end":44,"type":"D"},{"start":123,"end":144,"type":"D"},{"start":170,"end":198,"type":"D"}]}},{"features":{"pfam":[{"id":"PF15957","name":"Commissureless","start":129,"end":262}]},"uniref50":"UniRef50_Q24139","sequence":"MISTTDYPTVETTTTAEELYAEYISAPASSMSPAAIAEHLQQNQITFEIPSAHDLRHIDALNSFNALLQRIGNAAVSYDPAPPSGWSPDGSISTEQLSKSVVLDLADLRDRSEESGESSWWSQIFGDADMHVIINYLWIGVVSSLVILSLVFILFSCYFYRKFRTWKKCNKDIRAQIHAASDSYSSHLVGCDASRLLLHQQMQHPHHRSSEAGFYQIESPPCYTIATGLPSYDEALHHQPRHFAYGMKFVYPSLAAVHHHHHCISNWEKQEPLNKLQKCKLSAAAAVEEDKADSSSSTSASASPSSSESSNLATATPAICINMPSGRQDEEVDNSDSDSAIAVAVAVAQSLQPAAPADDDCASLVVVVAA","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_Q24139","disprot_id":"DP01366","ncbi_taxon_id":7227,"regions_counter":2,"creator":"baykac","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":237,"region_id":"DP01366r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural determinants for high-affinity binding in a Nedd4 WW3* domain-Comm PY motif complex. <i> Kanelis V, Bruce MC, Skrynnikov NR, Rotin D, Forman-Kay JD. </i> Structure, 2006","term_id":"IDPO:0000002","curator_id":"baykac","start":227,"term_ontology":"IDPO","curator_name":"Burcu Aykac-Fas","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-3842-731X","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2EZ5"}],"reference_id":"16531238","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":237,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural determinants for high-affinity binding in a Nedd4 WW3* domain-Comm PY motif complex. <i> Kanelis V, Bruce MC, Skrynnikov NR, Rotin D, Forman-Kay JD. </i> Structure, 2006","statement":[{"text":"\"Interactions between the WW domains of Drosophila Nedd4 (dNedd4) and Commissureless (Comm) PY motifs promote axon crossing at the CNS midline and muscle synaptogenesis. Here we report the solution structure of the dNedd4 WW3* domain complexed to the second PY motif (227'TGLPSYDEALH237') of Comm. ... Residues Y232'-L236' form a helical turn, following the PPII helical PY motif.\"","type":"Abstract"}],"term_id":"GO:0005515","curator_id":"baykac","start":227,"term_ontology":"GO","curator_name":"Burcu Aykac-Fas","reference_id":"16531238","version":3,"curator_orcid":"0000-0003-3842-731X","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01366r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q24139","date":"2018-07-13T18:37:08.000Z","acc":"Q24139","name":"Protein commissureless 1","length":370,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI00001246FD","genes":[{"name":{"value":"comm","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0010105","url":"http://flybase.org/reports/FBgn0010105.html"}}]},"orfNames":[{"value":"CG17943","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0010105","url":"http://flybase.org/reports/FBgn0010105.html"}}]}]}],"alphafold_very_low_content":0.518918918918919,"disorder_content":0.02972972972972973,"disprot_consensus":{"full":[{"start":227,"end":237,"type":"D"}],"Structural state":[{"start":227,"end":237,"type":"D"}],"Molecular function":[{"start":227,"end":237,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00928","name":"Adaptor complexes medium subunit family","start":560,"end":872},{"id":"PF12016","name":"Stonin 2","start":1,"end":340}],"gene3D":[{"start":837,"end":867,"id":"2.60.40.1170","name":"Mu homology domain, subdomain B"},{"start":561,"end":714,"id":"2.60.40.1170","name":"Mu homology domain, subdomain B"},{"start":774,"end":836,"id":"2.60.40.1170","name":"Mu homology domain, subdomain B"}]},"uniref50":"UniRef50_Q8WXE9","sequence":"MTTLDHVIATHQSEWVSFNEEPPFPAHSQGGTEEHLPGLSSSPDQSESSSGENHVVDGGSQDHSHSEQDDSSEKMGLISEAASPPGSPEQPPPDLASAISNWVQFEDDTPWASTSPPHQETAETALPLTMPCWTCPSFDSLGRCPLTSESSWTTHSEDTSSPSFGCSYTDLQLINAEEQTSGQASGADSTDNSSSLQEDEEVEMEAISWQASSPAMNGHPAPPVTSARFPSWVTFDDNEVSCPLPPVTSPLKPNTPPSASVIPDVPYNSMGSFKKRDRPKSTLMNFSKVQKLDISSLNRTPSVTEASPWRATNPFLNETLQDVQPSPINPFSAFFEEQERRSQNSSISSTTGKSQRDSLIVIYQDAISFDDSSKTQSHSDAVEKLKQLQIDDPDHFGSATLPDDDPVAWIELDAHPPGSARSQPRDGWPMMLRIPEKKNIMSSRHWGPIFVKLTDTGYLQLYYEQGLEKPFREFKLEICHEISEPRLQNYDENGRIHSLRIDRVTYKEKKKYQPKPAVAHTAEREQVIKLGTTNYDDFLSFIHAVQDRLMDLPVLSMDLSTVGLNYLEEEITVDVRDEFSGIVSKGDNQILQHHVLTRIHILSFLSGLAECRLGLNDILVKGNEIVLRQDIMPTTTTKWIKLHECRFHGCVDEDVFHNSRVILFNPLDACRFELMRFRTVFAEKTLPFTLRTATSVNGAEVEVQSWLRMSTGFSANRDPLTQVPCENVMIRYPVPSEWVKNFRRESVLGEKSLKAKVNRGASFGSTSVSGSEPVMRVTLGTAKYEHAFNSIVWRINRLPDKNSASGHPHCFFCHLELGSDREVPSRFANHVNVEFSMPTTSASKASVRSISVEDKTDVRKWVNYSAHYSYQVALGSIWLMLPTPFVHPTTLPLLFLLAMLTMFAW","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q8WXE9","disprot_id":"DP01368","ncbi_taxon_id":9606,"regions_counter":3,"creator":"baykac","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":340,"region_id":"DP01368r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of the Eps15-stonin2 complex provides a molecular explanation for EH-domain ligand specificity. <i> Rumpf J, Simon B, Jung N, Maritzen T, Haucke V, Sattler M, Groemping Y. </i> EMBO J, 2008","statement":[{"text":"This article and the region was mentioned to be an IDR in the article with Pubmed ID 23874186. In this article Figure 4 shows the IDR and cites the PDB: 2JXC structure article as: \"In panel D, a relatively long disordered segment of human stonin-2 interacts with one folded EF-hand domain of human EPS15 (PDB: 2JXC).\"","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"baykac","start":301,"term_ontology":"IDPO","curator_name":"Burcu Aykac-Fas","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-3842-731X","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2JXC"}],"reference_id":"18200045","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":340,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structure of the Eps15-stonin2 complex provides a molecular explanation for EH-domain ligand specificity. <i> Rumpf J, Simon B, Jung N, Maritzen T, Haucke V, Sattler M, Groemping Y. </i> EMBO J, 2008","statement":[{"text":"Stonin-2 NMR structure in complex with Eps15 (UniProt ID: P42566 \"EPS15_HUMAN\")","type":"Curator statement"}],"term_id":"GO:0005515","curator_id":"baykac","start":301,"term_ontology":"GO","curator_name":"Burcu Aykac-Fas","reference_id":"18200045","version":3,"curator_orcid":"0000-0003-3842-731X","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01368r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":331,"region_id":"DP01368r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"1H, 13C, and 15N chemical shift assignments for the Eps15-EH2-stonin 2 complex. <i> Rumpf J, Simon B, Groemping Y, Sattler M. </i> Biomol NMR Assign, 2008","statement":[{"text":"\"Figure 2b: Secondary chemical shifts Δδ(Cα–Cβ) of the stonin 2 peptide bound to Eps15 EH2.\"","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"baykac","start":301,"term_ontology":"IDPO","curator_name":"Burcu Aykac-Fas","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-3842-731X","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19636924","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q8WXE9","date":"2018-07-13T18:37:41.000Z","acc":"Q8WXE9","name":"Stonin-2","length":905,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000007259C","genes":[{"name":{"value":"STON2"},"synonyms":[{"value":"STN2"},{"value":"STNB"}]}],"alphafold_very_low_content":0.47624309392265196,"disorder_content":0.04419889502762431,"disprot_consensus":{"full":[{"start":301,"end":340,"type":"D"}],"Structural state":[{"start":301,"end":340,"type":"D"}],"Molecular function":[{"start":301,"end":340,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_P0CU46","sequence":"MPYEKHVEQTVVEKTEQPGHSSTHHAPAQRTVAREQEEVVHKEFTHTDIRVPHIDAPPPIIAASAVGLAEEIVSHGFQASAARISGASTEVDMRPSPKLAEEARRDAERYQKEHEMINRQAEATLQKKAEEYRHQTEAEAEKIRRELEKQHERDIQFRKDLIDQTIEKQKREVDLEAKMAKRELDREAQLAKEALERSRMATNVEVTLDTAAGHTVSGGTTVSSVDKVETVRERKHH","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Tardigrada","Eutardigrada","Parachela","Hypsibioidea","Ramazzottiidae","Ramazzottius"],"uniref90":"UniRef90_J7M799","disprot_id":"DP01377","ncbi_taxon_id":947166,"regions_counter":1,"creator":"mmacossay","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":237,"region_id":"DP01377r001","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Two novel heat-soluble protein families abundantly expressed in an anhydrobiotic tardigrade. <i> Yamaguchi A, Tanaka S, Yamaguchi S, Kuwahara H, Takamura C, Imajoh-Ohmi S, Horikawa DD, Toyoda A, Katayama T, Arakawa K, Fujiyama A, Kubo T, Kunieda T. </i> PLoS One, 2012","statement":[{"text":"In contrast, the CD spectrum of CAHS1 had a single deep minimum around 200 nm, similar to that of hydrated LEA proteins [31], suggesting that these proteins are unstructured in hydrated conditions (Fig. 4B).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-28T15:43:28.982Z","reference_source":"pmid","term_name":"disorder","reference_id":"22937162","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_J7M799","date":"2018-07-16T08:11:53.000Z","acc":"J7M799","name":"Cytosolic-abundant heat soluble protein 1","length":237,"organism":"Ramazzottius varieornatus","dataset":["Stress response proteins"],"UniParc":"UPI00027DB7F7","genes":[{"name":{"value":"CAHS1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"22937162","url":"http://www.ncbi.nlm.nih.gov/pubmed/22937162","alternativeUrl":"https://europepmc.org/abstract/MED/22937162"}}]},"orfNames":[{"value":"RvY_00944"}]}],"alphafold_very_low_content":0.37130801687763715,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":237,"type":"D"}],"Structural state":[{"start":1,"end":237,"type":"D"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_P0CU43","sequence":"MSNYQQESSYQYSDRSNNGQQQEQQEKKEVEHSSYTHTDVKVNMPNLIAPFISSSAGLAQELVGEGFQASVSRITGASGELTVIDTEAETEEARRDMEAKAREQELLSRQFEKELERKTEAYRKQQEVETEKIRKELEKQHLRDVEFRKELMEQTIENQKRQIDLEARYAKKELERERNKVKRVLERSKFHTDIQVNMEAAAGSTHSGSSSVAVSESEKFQTNN","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Tardigrada","Eutardigrada","Parachela","Hypsibioidea","Hypsibiidae","Hypsibius"],"uniref90":"UniRef90_P0CU43","disprot_id":"DP01378","ncbi_taxon_id":232323,"regions_counter":3,"creator":"mmacossay","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":224,"region_id":"DP01378r001","released":"2024_06","ec_id":"ECO:0006165","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","statement":[{"text":"IDPs lack persistent secondary structure (Theillet et al., 2014; Yamaguchi et al., 2012), which we confirmed for CAHS proteins using nuclear magnetic resonance spectroscopy (NMR).","type":"Results"},{"text":"For α-synuclein, a known disordered protein, and for CAHS proteins, the crosspeaks occur over a narrower window (Figure 2, top), from ~8.0 to ~8.6 ppm, which coincides with the range for amide protons in the central residue of unstructured tripeptides (Schwarzinger et al., 2000).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2024-03-22T15:17:37.412Z","reference_source":"pmid","term_name":"disorder","reference_id":"28306513","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":224,"region_id":"DP01378r002","released":"2023_12","ec_id":"ECO:0006196","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","statement":[{"text":"For the disordered proteins tested (α-synuclein and CAHS proteins), nearly all the amide protons were exchanged for deuterons within 20 min, as shown by the decrease in intensity of the one-dimensional proton spectrum (Figure 2).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-28T15:45:14.488Z","reference_source":"pmid","term_name":"disorder","reference_id":"28306513","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":3,"end":222,"reference_id":"28306513","reference_source":"pmid","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","date":"2024-03-22T15:55:22.601Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0009269","term_name":"response to desiccation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001585","ec_ontology":"ECO","ec_name":"small interfering RNA knockdown evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IMP","region_id":"DP01378r003","statement":[{"text":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation.","type":"Title"},{"text":"Tardigrade-Specific IDPs Are Required for Desiccation Tolerance","type":"Results"},{"text":"However, targeting two of four highly induced (13- to 22-fold) CAHS genes significantly (p < 0.01) reduced survival after desiccation compared with a control treatment, GFP RNAi (Figure 4B).","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a desiccation stimulus, extreme dryness resulting from the prolonged deprivation of water.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_P0CU43","date":"2018-07-16T10:58:29.000Z","acc":"P0CU43","name":"Cytosolic-abundant heat soluble protein 77580","length":224,"organism":"Hypsibius dujardini","dataset":["Stress response proteins"],"UniParc":"UPI0009F0F06B","genes":[{"name":{"value":"CAHS 77580","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"28306513","url":"http://www.ncbi.nlm.nih.gov/pubmed/28306513","alternativeUrl":"https://europepmc.org/abstract/MED/28306513"}}]}}],"alphafold_very_low_content":0.3080357142857143,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":224,"type":"D"}],"Structural state":[{"start":1,"end":224,"type":"D"}],"Biological process":[{"start":3,"end":222,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_P0CU43","sequence":"MSNYQQESSYQYSDRSNNGQQQEQQEKKEVEHSSYTHTDVKVNMPNLIAPFISSSAGLAQELVGEGFQASVSRITGASGELTVIDTEAETEEARRDLEAKAREQELLSRQFEKELERKTEAYRKQQEVETEKIRKELEKQHLRDVEFRKELMEQTIENQKRQIDLEARYAKKELERERNKVKRVLERSKFHTDIQVNMEAAAGSTHSGSSSVAVSESEKFQTNN","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Tardigrada","Eutardigrada","Parachela","Hypsibioidea","Hypsibiidae","Hypsibius"],"uniref90":"UniRef90_P0CU43","disprot_id":"DP01379","ncbi_taxon_id":232323,"regions_counter":3,"creator":"mmacossay","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":224,"region_id":"DP01379r001","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","statement":[{"text":"IDPs lack persistent secondary structure (Theillet et al., 2014; Yamaguchi et al., 2012), which we confirmed for CAHS proteins using nuclear magnetic resonance spectroscopy (NMR).","type":"Results"},{"text":"For α-synuclein, a known disordered protein, and for CAHS proteins, the crosspeaks occur over a narrower window (Figure 2, top), from ~8.0 to ~8.6 ppm, which coincides with the range for amide protons in the central residue of unstructured tripeptides (Schwarzinger et al., 2000).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-28T15:45:54.132Z","reference_source":"pmid","term_name":"disorder","reference_id":"28306513","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":224,"region_id":"DP01379r002","released":"2023_12","ec_id":"ECO:0006196","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","statement":[{"text":"For the disordered proteins tested (α-synuclein and CAHS proteins), nearly all the amide protons were exchanged for deuterons within 20 min, as shown by the decrease in intensity of the one-dimensional proton spectrum (Figure 2).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-28T15:45:07.594Z","reference_source":"pmid","term_name":"disorder","reference_id":"28306513","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":224,"reference_id":"28306513","reference_source":"pmid","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","date":"2024-03-22T15:54:29.576Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0009269","term_name":"response to desiccation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001585","ec_ontology":"ECO","ec_name":"small interfering RNA knockdown evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IMP","region_id":"DP01379r003","statement":[{"text":"Tardigrade-Specific IDPs Are Required for Desiccation Tolerance","type":"Results"},{"text":"However, targeting two of four highly induced (13- to 22-fold) CAHS genes significantly (p < 0.01) reduced survival after desiccation compared with a control treatment, GFP RNAi (Figure 4B). ","type":"Results"},{"text":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation.","type":"Title"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a desiccation stimulus, extreme dryness resulting from the prolonged deprivation of water.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_P0CU44","date":"2018-07-16T11:07:26.000Z","acc":"P0CU44","name":"Cytosolic-abundant heat soluble protein 77611","length":224,"organism":"Hypsibius dujardini","dataset":["Stress response proteins"],"UniParc":"UPI000A27FC20","genes":[{"name":{"value":"CAHS 77611","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"28306513","url":"http://www.ncbi.nlm.nih.gov/pubmed/28306513","alternativeUrl":"https://europepmc.org/abstract/MED/28306513"}}]}}],"alphafold_very_low_content":0.3080357142857143,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":224,"type":"D"}],"Structural state":[{"start":1,"end":224,"type":"D"}],"Biological process":[{"start":1,"end":224,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_P0CU45","sequence":"MSGRNVESHMERNEKVVVNNSGHADVKKHQQQVEHTEFTHTEVKAPLIHPAPPIISTGAAGLAEEIVGQGFTASAARISGGTAEVHLQPSAAMTEEARRDQERYRQEQESIAKQQEREMEKKTEAYRKTAEAEAEKIRKELEKQHARDVEFRKDLIESTIDRQKREVDLEAKMAKRELDREGQLAKEALERSRLATNVEVNFDSAAGHTVSGGTTISSSDKMEIKRN","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Tardigrada","Eutardigrada","Parachela","Hypsibioidea","Hypsibiidae","Hypsibius"],"uniref90":"UniRef90_P0CU45","disprot_id":"DP01380","ncbi_taxon_id":232323,"regions_counter":3,"creator":"mmacossay","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":227,"region_id":"DP01380r001","released":"2023_12","ec_id":"ECO:0006196","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","statement":[{"text":"For the disordered proteins tested (α-synuclein and CAHS proteins), nearly all the amide protons were exchanged for deuterons within 20 min, as shown by the decrease in intensity of the one-dimensional proton spectrum (Figure 2).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-28T15:49:08.175Z","reference_source":"pmid","term_name":"disorder","reference_id":"28306513","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":227,"region_id":"DP01380r002","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","statement":[{"text":"IDPs lack persistent secondary structure (Theillet et al., 2014; Yamaguchi et al., 2012), which we confirmed for CAHS proteins using nuclear magnetic resonance spectroscopy (NMR).","type":"Results"},{"text":"For α-synuclein, a known disordered protein, and for CAHS proteins, the crosspeaks occur over a narrower window (Figure 2, top), from ~8.0 to ~8.6 ppm, which coincides with the range for amide protons in the central residue of unstructured tripeptides (Schwarzinger et al., 2000).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-28T15:52:03.943Z","reference_source":"pmid","term_name":"disorder","reference_id":"28306513","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":3,"end":227,"reference_id":"28306513","reference_source":"pmid","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","date":"2024-03-22T15:56:16.474Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0009269","term_name":"response to desiccation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001585","ec_ontology":"ECO","ec_name":"small interfering RNA knockdown evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IMP","region_id":"DP01380r003","statement":[{"text":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation.","type":"Title"},{"text":"Tardigrade-Specific IDPs Are Required for Desiccation Tolerance","type":"Results"},{"text":"However, targeting two of four highly induced (13- to 22-fold) CAHS genes significantly (p < 0.01) reduced survival after desiccation compared with a control treatment, GFP RNAi (Figure 4B).","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a desiccation stimulus, extreme dryness resulting from the prolonged deprivation of water.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_P0CU45","date":"2018-07-16T11:10:21.000Z","acc":"P0CU45","name":"Cytosolic-abundant heat soluble protein 94205","length":227,"organism":"Hypsibius dujardini","dataset":["Stress response proteins"],"UniParc":"UPI000A27FC1F","genes":[{"name":{"value":"CAHS 94205","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"28306513","url":"http://www.ncbi.nlm.nih.gov/pubmed/28306513","alternativeUrl":"https://europepmc.org/abstract/MED/28306513"}}]},"synonyms":[{"value":"CAHS-a","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"22937162","url":"http://www.ncbi.nlm.nih.gov/pubmed/22937162","alternativeUrl":"https://europepmc.org/abstract/MED/22937162"}}]}]}],"alphafold_very_low_content":0.28634361233480177,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":227,"type":"D"}],"Structural state":[{"start":1,"end":227,"type":"D"}],"Biological process":[{"start":3,"end":227,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_P0CU46","sequence":"MSQQYEKKVERTEVVYGGDRRVEGSASASAEKTTNYTHTEIRAPMVNPLPPIISTGAAGLAQEIVGEGFTASATRISGAAATTQVLESQASREQAFKDQEKYSREQASIARAHDKDLEKKTEEYRKTAEAEAEKIRKELEKQHARDVEFRKDLVESAIDRQKREVDLEAKYAKKELEHERELAMNALEQSKMATNVQVQMDTAAGTTVSGGTTVSEHTEVHDGKEKKSLGEKIKSLF","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Tardigrada","Eutardigrada","Parachela","Hypsibioidea","Hypsibiidae","Hypsibius"],"uniref90":"UniRef90_P0CU46","disprot_id":"DP01381","ncbi_taxon_id":232323,"regions_counter":3,"creator":"mmacossay","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":237,"region_id":"DP01381r001","released":"2024_06","ec_id":"ECO:0006165","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","statement":[{"text":"IDPs lack persistent secondary structure (Theillet et al., 2014; Yamaguchi et al., 2012), which we confirmed for CAHS proteins using nuclear magnetic resonance spectroscopy (NMR)","type":"Results"},{"text":"For α-synuclein, a known disordered protein, and for CAHS proteins, the crosspeaks occur over a narrower window (Figure 2, top), from ~8.0 to ~8.6 ppm, which coincides with the range for amide protons in the central residue of unstructured tripeptides (Schwarzinger et al., 2000).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-03-22T15:17:33.181Z","reference_source":"pmid","term_name":"disorder","reference_id":"28306513","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":237,"region_id":"DP01381r002","released":"2024_06","ec_id":"ECO:0006196","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","statement":[{"text":"For the disordered proteins tested (α-synuclein and CAHS proteins), nearly all the amide protons were exchanged for deuterons within 20 min, as shown by the decrease in intensity of the one-dimensional proton spectrum (Figure 2).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-03-22T15:17:04.809Z","reference_source":"pmid","term_name":"disorder","reference_id":"28306513","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":237,"reference_id":"28306513","reference_source":"pmid","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","date":"2024-03-22T15:57:02.056Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0009269","term_name":"response to desiccation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001585","ec_ontology":"ECO","ec_name":"small interfering RNA knockdown evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IMP","region_id":"DP01381r003","statement":[{"text":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation.","type":"Title"},{"text":"Tardigrade-Specific IDPs Are Required for Desiccation Tolerance","type":"Results"},{"text":"However, targeting two of four highly induced (13- to 22-fold) CAHS genes significantly (p < 0.01) reduced survival after desiccation compared with a control treatment, GFP RNAi (Figure 4B).","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a desiccation stimulus, extreme dryness resulting from the prolonged deprivation of water.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_P0CU46","date":"2018-07-16T11:14:11.000Z","acc":"P0CU46","name":"Cytosolic-abundant heat soluble protein 86272","length":237,"organism":"Hypsibius dujardini","dataset":["Stress response proteins"],"UniParc":"UPI000A27FC27","genes":[{"name":{"value":"CAHS 86272","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"28306513","url":"http://www.ncbi.nlm.nih.gov/pubmed/28306513","alternativeUrl":"https://europepmc.org/abstract/MED/28306513"}}]},"synonyms":[{"value":"CAHS-b","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"22937162","url":"http://www.ncbi.nlm.nih.gov/pubmed/22937162","alternativeUrl":"https://europepmc.org/abstract/MED/22937162"}}]}]}],"alphafold_very_low_content":0.3206751054852321,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":237,"type":"D"}],"Structural state":[{"start":1,"end":237,"type":"D"}],"Biological process":[{"start":1,"end":237,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_P0CU47","sequence":"MATKESKYERVEKVNVDADGATLVKNIGEDRGKEDPGMNYQDKRPANLVPGAPAGVIPNRIESLPTDRAGQRLREHLSESERLRGSRSSTSSKSSSFVEPSLKYRGEIGPIGKNGEFVASSNRQNSSSNVSSSDNSERASPASRNSNPGMNNGMTTQRTTVITESSVQGLGAQRTVPIQPHQQREDHEVITHESHARAPETTVVTIPTTRFESAQLESRRDGRTYTEDKELTIPAPVVAPQIHAHQQVNMSGGTSATIHATTDLHLASEAQINDMGPEEYERYRAKVEALARIHEDETSRKAAAYRNAVEADAELIRQTLERQHMRDIEFRKDLVESSVDRQQQEIRLEAEYAMRALEQERVNARAALDQAMASTNIDVNIDSAIGTTHSQGRVTTTSESRTSQARGPATAAVI","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Tardigrada","Eutardigrada","Parachela","Hypsibioidea","Hypsibiidae","Hypsibius"],"uniref90":"UniRef90_P0CU47","disprot_id":"DP01382","ncbi_taxon_id":232323,"regions_counter":2,"creator":"mmacossay","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":414,"region_id":"DP01382r001","released":"2024_06","ec_id":"ECO:0006165","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","statement":[{"text":"IDPs lack persistent secondary structure (Theillet et al., 2014; Yamaguchi et al., 2012), which we confirmed for CAHS proteins using nuclear magnetic resonance spectroscopy (NMR).","type":"Results"},{"text":"For α-synuclein, a known disordered protein, and for CAHS proteins, the crosspeaks occur over a narrower window (Figure 2, top), from ~8.0 to ~8.6 ppm, which coincides with the range for amide protons in the central residue of unstructured tripeptides (Schwarzinger et al., 2000).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-03-22T15:21:28.980Z","reference_source":"pmid","term_name":"disorder","reference_id":"28306513","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":414,"region_id":"DP01382r002","released":"2024_06","ec_id":"ECO:0006196","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","statement":[{"text":"For the disordered proteins tested (α-synuclein and CAHS proteins), nearly all the amide protons were exchanged for deuterons within 20 min, as shown by the decrease in intensity of the one-dimensional proton spectrum (Figure 2).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-03-22T15:21:09.796Z","reference_source":"pmid","term_name":"disorder","reference_id":"28306513","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P0CU47","date":"2018-07-16T11:16:28.000Z","acc":"P0CU47","name":"Cytosolic-abundant heat soluble protein 89226","length":414,"organism":"Hypsibius dujardini","dataset":["Stress response proteins"],"UniParc":"UPI000A27FC4D","genes":[{"name":{"value":"CAHS 89226","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"28306513","url":"http://www.ncbi.nlm.nih.gov/pubmed/28306513","alternativeUrl":"https://europepmc.org/abstract/MED/28306513"}}]}}],"alphafold_very_low_content":0.46859903381642515,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":414,"type":"D"}],"Structural state":[{"start":1,"end":414,"type":"D"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_P0CU43","sequence":"MSAEAMNMNMNQDAVFIPPPEGEQYERKEKQEIQQTSYLQSQVKVPLVNLPAPFFSTSFSAQEILGEGFQASISRISAVSEELSSIEIPELAEEARRDFAAKTREQEMLSANYQKEVERKTEAYRKQQEVEADKIRKELEKQHLRDVEFRKDIVEMAIENQKKMIDVESRYAKKDMDRERVKVRMMLEQQKFHSDIQVNLDSSAAGTETGGQVVSESQKFTERNRQIKQ","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Tardigrada","Eutardigrada","Parachela","Macrobiotoidea","Macrobiotidae","Paramacrobiotus","Paramacrobiotus richtersi group"],"uniref90":"UniRef90_P0CU51","disprot_id":"DP01383","ncbi_taxon_id":697321,"regions_counter":3,"creator":"mmacossay","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":229,"region_id":"DP01383r001","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","statement":[{"text":"IDPs lack persistent secondary structure (Theillet et al., 2014; Yamaguchi et al., 2012), which we confirmed for CAHS proteins using nuclear magnetic resonance spectroscopy (NMR).","type":"Results"},{"text":"For α-synuclein, a known disordered protein, and for CAHS proteins, the crosspeaks occur over a narrower window (Figure 2, top), from ~8.0 to ~8.6 ppm, which coincides with the range for amide protons in the central residue of unstructured tripeptides (Schwarzinger et al., 2000).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-28T15:52:20.220Z","reference_source":"pmid","term_name":"disorder","reference_id":"28306513","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":229,"region_id":"DP01383r002","released":"2023_12","ec_id":"ECO:0006196","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","statement":[{"text":"For the disordered proteins tested (α-synuclein and CAHS proteins), nearly all the amide protons were exchanged for deuterons within 20 min, as shown by the decrease in intensity of the one-dimensional proton spectrum (Figure 2).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-28T15:49:21.101Z","reference_source":"pmid","term_name":"disorder","reference_id":"28306513","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":229,"reference_id":"28306513","reference_source":"pmid","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","date":"2024-03-22T16:11:47.672Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0009269","term_name":"response to desiccation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007117","ec_ontology":"ECO","ec_name":"mutant physiological response evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IMP","region_id":"DP01383r003","statement":[{"text":"Similar results were obtained in bacteria, with exogenous expression of some CAHS proteins resulting in increases of more than 2 orders of magnitude in desiccation tolerance (Figure 6B). Importantly, α-synuclein, a protein that exists as a disordered monomer in cells (Fauvet et al., 2012; Theillet et al., 2016) and has no known connection to stress tolerance (Drescher et al., 2012; Theillet et al., 2014), did not increase survival under drying conditions (Figure 6B), demonstrating that something beyond intrinsic disorder of TDPs is essential for their protective capabilities.","type":"Results"},{"text":"Tardigrade-Specific IDPs Increase Desiccation Tolerance in Heterologous Systems and In Vitro","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a desiccation stimulus, extreme dryness resulting from the prolonged deprivation of water.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_P0CU51","date":"2018-07-16T11:20:40.000Z","acc":"P0CU51","name":"Cytosolic-abundant heat soluble protein 107838","length":229,"organism":"Paramacrobiotus richtersi","dataset":["Stress response proteins"],"UniParc":"UPI000A27FC3A","genes":[{"name":{"value":"CAHS 107838","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"28306513","url":"http://www.ncbi.nlm.nih.gov/pubmed/28306513","alternativeUrl":"https://europepmc.org/abstract/MED/28306513"}}]}}],"alphafold_very_low_content":0.20087336244541484,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":229,"type":"D"}],"Structural state":[{"start":1,"end":229,"type":"D"}],"Biological process":[{"start":1,"end":229,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_P0CU45","sequence":"MSGRNVESHMERNEKVVVNNSGHADVKKQQQQVEHTEFTHTEVKAPLIHPAPPIISTGAAGLAEEIVGQGFTASAARISGGTAEIHLQPSAAMTEEARRDQERYRQEQESIAKQQEREMEKKTEAYRKTAEAEAEKIRKELEKQHARDVEFRKDLIESTIDRQKREVDLEAKMAKRELDREGQLAKEALERSRLATNVEVNFDSAAGHTVSGGTTVSTSDKMEIKRN","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Tardigrada","Eutardigrada","Parachela","Hypsibioidea","Hypsibiidae","Hypsibius"],"uniref90":"UniRef90_P0CU45","disprot_id":"DP01384","ncbi_taxon_id":232323,"regions_counter":16,"creator":"mmacossay","regions":[{"start":1,"end":94,"reference_id":"34750927","reference_source":"pmid","reference_html":"Intrinsically Disordered Tardigrade Proteins Self-Assemble into Fibrous Gels in Response to Environmental Stress. <i> Malki A, Teulon JM, Camacho-Zarco AR, Chen SW, Adamski W, Maurin D, Salvi N, Pellequer JL, Blackledge M. </i> Angew Chem Int Ed Engl, 2022","date":"2023-02-13T13:54:21.994Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP01384r003","statement":[{"text":"Here, we characterize the conformational and physical behaviour of CAHS‐8 from Hypsibius exemplaris. NMR spectroscopy reveals that the protein comprises an extended central helical domain flanked by disordered termini.","type":"Abstract"},{"text":"By using high‐field NMR spectroscopy, we reveal that the protein comprises an extended central helical domain, with apparent coiled‐coil propensity, flanked by long, highly disordered N‐ and C‐terminal domains.","type":"Article"},{"text":"The 15N‐1H HSQC spectrum of CAHS‐8 (Figure 1 A) is typical of an intrinsically disordered protein, with low dispersion in the 1HN dimension.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-13T16:50:55.450Z"}},{"start":195,"end":227,"reference_id":"34750927","reference_source":"pmid","reference_html":"Intrinsically Disordered Tardigrade Proteins Self-Assemble into Fibrous Gels in Response to Environmental Stress. <i> Malki A, Teulon JM, Camacho-Zarco AR, Chen SW, Adamski W, Maurin D, Salvi N, Pellequer JL, Blackledge M. </i> Angew Chem Int Ed Engl, 2022","date":"2023-02-13T13:54:42.454Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP01384r004","statement":[{"text":"Here, we characterize the conformational and physical behaviour of CAHS‐8 from Hypsibius exemplaris. NMR spectroscopy reveals that the protein comprises an extended central helical domain flanked by disordered termini.","type":"Abstract"},{"text":"By using high‐field NMR spectroscopy, we reveal that the protein comprises an extended central helical domain, with apparent coiled‐coil propensity, flanked by long, highly disordered N‐ and C‐terminal domains.","type":"Article"},{"text":"The 15N‐1H HSQC spectrum of CAHS‐8 (Figure 1 A) is typical of an intrinsically disordered protein, with low dispersion in the 1HN dimension.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-13T16:50:56.917Z"}},{"start":1,"end":227,"reference_id":"28306513","reference_source":"pmid","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","date":"2024-03-22T15:14:11.510Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01384r006","statement":[{"text":"For α-synuclein, a known disordered protein, and for CAHS proteins, the crosspeaks occur over a narrower window (Figure 2, top), from ~8.0 to ~8.6 ppm, which coincides with the range for amide protons in the central residue of unstructured tripeptides (Schwarzinger et al., 2000).","type":"Results"}]},{"start":1,"end":227,"reference_id":"28306513","reference_source":"pmid","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","date":"2024-03-22T16:12:31.181Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0009269","term_name":"response to desiccation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007117","ec_ontology":"ECO","ec_name":"mutant physiological response evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IMP","region_id":"DP01384r007","statement":[{"text":"Several CAHS proteins were sufficient to increase the desiccation tolerance of yeast nearly 100-fold (Figure 6A). Similar results were obtained in bacteria, with exogenous expression of some CAHS proteins resulting in increases of more than 2 orders of magnitude in desiccation tolerance (Figure 6B). Importantly, α-synuclein, a protein that exists as a disordered monomer in cells (Fauvet et al., 2012; Theillet et al., 2016) and has no known connection to stress tolerance (Drescher et al., 2012; Theillet et al., 2014), did not increase survival under drying conditions (Figure 6B), demonstrating that something beyond intrinsic disorder of TDPs is essential for their protective capabilities.","type":"Results"},{"text":"Tardigrade-Specific IDPs Increase Desiccation Tolerance in Heterologous Systems and In Vitro","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a desiccation stimulus, extreme dryness resulting from the prolonged deprivation of water.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":227,"reference_id":"34750927","reference_source":"pmid","reference_html":"Intrinsically Disordered Tardigrade Proteins Self-Assemble into Fibrous Gels in Response to Environmental Stress. <i> Malki A, Teulon JM, Camacho-Zarco AR, Chen SW, Adamski W, Maurin D, Salvi N, Pellequer JL, Blackledge M. </i> Angew Chem Int Ed Engl, 2022","date":"2022-06-13T13:34:43.125Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"51115"}],"region_id":"DP01384r008","statement":[{"text":"NMR spectroscopy reveals that the protein comprises an extended central helical domain flanked by disordered termini.","type":"Abstract"},{"text":"By using high-field NMR spectroscopy, we reveal that the protein comprises an extended central helical domain, with apparent coiled-coil propensity, flanked by long, highly disordered N- and C-terminal domains.","type":"Results"},{"text":"The 15N-1H HSQC spectrum of CAHS-8 (Figure 1 A) is typical of an intrinsically disordered protein, with low dispersion in the 1HN dimension.","type":"Results"},{"text":"A) The 15N-1H correlation spectrum is characteristic of an intrinsically disordered protein. B, C) Secondary 13Ca and 13C’ chemical shifts showing strong a-helical propensities from 95– 195, divided into two distinct helices, a1 (E95-F150) and a2 (V167- L194). 15N relaxation (D; 850 MHz, E; 600 MHz), 15N-1H RDCs (F), and PREs (see Figure S1) suggest the protein acts as a disordered chain comprising two highly populated a-helices (303 K) and no persistent tertiary structure.","type":"Figure"},{"text":"The tertiary folding of CAHS-8 was probed using paramagnetic relaxation enhancements, with TEMPO-maleimide labelling of positions A134C and A185C. The absence of significant enhancements beyond immediate neighbours indicates an absence of persistent long-range structure (see Figure S1).","type":"Results"},{"text":"The presence of two helices connected by a more flexible linker is supported by the measurement of 15N-1H residual dipolar couplings (RDCs; see Methods in the Supporting Information). The RDCs show a profile typical of IDPs with helical elements that do not specifically interact with each other, as predicted by simulation and experimentally validated in numerous systems. The RDCs exhibit positive values in the helical regions and lower or negative values in the unstructured parts of the chain (Figure 1 f).","type":"Results"},{"text":"We describe the monomeric behaviour of the protein as partially disordered, with a long two-helical domain flanked by long flexible tails.","type":"Conclusion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-11T14:55:29.825Z"}},{"start":1,"end":227,"reference_id":"34750927","reference_source":"pmid","reference_html":"Intrinsically Disordered Tardigrade Proteins Self-Assemble into Fibrous Gels in Response to Environmental Stress. <i> Malki A, Teulon JM, Camacho-Zarco AR, Chen SW, Adamski W, Maurin D, Salvi N, Pellequer JL, Blackledge M. </i> Angew Chem Int Ed Engl, 2022","date":"2022-06-13T13:35:29.394Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP01384r009","statement":[{"text":"SAXS measured at 2 mg mL-1 (blue)","type":"Figure"},{"text":"The average radius of gyration Rg,av of an ensemble of fully disordered conformers is 47 +/- 10 A, while an ensemble of conformers containing the helical elements (Rg,av = 59 +/- 11 A; see Figure S2) coincides with the experimental radius of gyration, thereby supporting the nature of the ensemble of unfolded chains comprising significant populations of helices a1 and a2.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-11T14:55:31.427Z"}},{"start":95,"end":195,"reference_id":"34750927","reference_source":"pmid","reference_html":"Intrinsically Disordered Tardigrade Proteins Self-Assemble into Fibrous Gels in Response to Environmental Stress. <i> Malki A, Teulon JM, Camacho-Zarco AR, Chen SW, Adamski W, Maurin D, Salvi N, Pellequer JL, Blackledge M. </i> Angew Chem Int Ed Engl, 2022","date":"2022-06-13T13:36:06.492Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0097435","term_name":"supramolecular fiber organization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP01384r010","statement":[{"text":"CAHS-8 shows a strongly concentration-dependent propensity to oligomerize, as illustrated by SAXS, where scattering curves that are characteristic of fibril formation are observed at higher concentrations (Figure 2 A).","type":"Results"},{"text":"Figure 2. Monomeric CAHS-8 forms higher order oligomers as a function of concentration and temperature. A) SAXS measured at\n2 mg mL-1 (blue) and 5 mg mL-1 (red). At the higher concentration, the curve shows characteristics associated with fibril formation.","type":"Figure"}],"term_comment":"","term_def":"\"A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a supramolecular fiber, a polymer consisting of an indefinite number of protein or protein complex subunits that have polymerised to form a fiber-shaped structure.\" [GOC:pr]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-11T14:55:48.913Z"}},{"start":95,"end":195,"reference_id":"34750927","reference_source":"pmid","reference_html":"Intrinsically Disordered Tardigrade Proteins Self-Assemble into Fibrous Gels in Response to Environmental Stress. <i> Malki A, Teulon JM, Camacho-Zarco AR, Chen SW, Adamski W, Maurin D, Salvi N, Pellequer JL, Blackledge M. </i> Angew Chem Int Ed Engl, 2022","date":"2022-06-13T13:36:25.008Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0097435","term_name":"supramolecular fiber organization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006196","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP01384r011","statement":[{"text":"The 13C chemical shifts show strong temperature dependence, revealing a significantly higher helical content at 278 K for helix a2 (see FigureS3). The 15N relaxation is also temperature dependent (Figure 2 C and see also Figure S4), notably higher than that normally observed in intrinsically disordered proteins containing helical elements[21, 22] (see Figure S2), thus supporting the formation of higher order oligomers at lower temperature.","type":"Results"},{"text":"No signals from helix a1 were detected in the 15N-1H HSQC spectrum of a gel formed from 15N-labelled CAHS-8","type":"Results"},{"text":"These observations are compatible with the involvement of a1 in the formation of fibrils that constitute the gel","type":"Results"},{"text":"On the basis of these observations, we propose that the long helical domains of the partially disordered protein associate through coiled-coil-like interactions under certain environmental conditions (low temperature, high concentration) to form oligomers, then fibrils (Figure 5 C), which eventually form a gel-like matrix. Both charged and hydrophobic amino acids in this region are strongly conserved over CAHS proteins from different species. NMR relaxation data also show strong evidence that this region is central to the intermolecular interaction, with signals in this region disappearing at lower temperatures, where higher order oligomerization is favoured, and relaxation rates increasing more in this region than elsewhere.","type":"Discussion"},{"text":"We propose that this domain mediates homo-dimerization through a coiled-coil interaction, and have experimentally observed the successive formation of oligomers, fibrils, and eventually gels in response to concentration and temperature change.","type":"Conclusion"}],"term_comment":"","term_def":"\"A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a supramolecular fiber, a polymer consisting of an indefinite number of protein or protein complex subunits that have polymerised to form a fiber-shaped structure.\" [GOC:pr]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-11T14:55:45.097Z"}},{"start":95,"end":195,"reference_id":"34750927","reference_source":"pmid","reference_html":"Intrinsically Disordered Tardigrade Proteins Self-Assemble into Fibrous Gels in Response to Environmental Stress. <i> Malki A, Teulon JM, Camacho-Zarco AR, Chen SW, Adamski W, Maurin D, Salvi N, Pellequer JL, Blackledge M. </i> Angew Chem Int Ed Engl, 2022","date":"2022-06-13T13:36:38.956Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0097435","term_name":"supramolecular fiber organization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP01384r012","statement":[{"text":"Dynamic light scattering (DLS) measurements were used to map the phase diagram of CAHS-8 by observing the dependence of the decay in the autocorrelation of scattered intensity as a function of temperature and concentration (Figure 2 B). We observe the formation of an apparent physical hydrogel phase at low temperatures and higher concentration, in qualitative agreement with observations from the NMR and SAXS studies.","type":"Results"},{"text":"Phase diagram derived from DLS. Orange represents the isotropic phase, red represents increased oligomerization associated with slight gel formation, and blue represents gel formation.","type":"Figure"}],"term_comment":"","term_def":"\"A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a supramolecular fiber, a polymer consisting of an indefinite number of protein or protein complex subunits that have polymerised to form a fiber-shaped structure.\" [GOC:pr]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-11T14:55:51.706Z"}},{"start":95,"end":195,"reference_id":"34750927","reference_source":"pmid","reference_html":"Intrinsically Disordered Tardigrade Proteins Self-Assemble into Fibrous Gels in Response to Environmental Stress. <i> Malki A, Teulon JM, Camacho-Zarco AR, Chen SW, Adamski W, Maurin D, Salvi N, Pellequer JL, Blackledge M. </i> Angew Chem Int Ed Engl, 2022","date":"2022-06-13T13:38:12.200Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0097435","term_name":"supramolecular fiber organization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001591","ec_ontology":"ECO","ec_name":"atomic force microscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","region_id":"DP01384r013","statement":[{"text":"We used atomic force microscopy (AFM) in liquid and air modes to observe the apparent formation of fibrils that eventually form a dense mesh that resembles a gel and to investigate the nature of these gels. Extension often follows a twisted helix structure comprising paired filaments, exhibiting a pitch of approximately 600 nm (Figure 3 A). AFM was used to follow gel formation, and revealed the generation of fibrillar structures as a function of time (Figure 3 B, see also Figure S3), eventually leading to a dense mesh of fibres (Figure 3 C).","type":"Results"},{"text":"B) Allowing fibrillation to continue whilst the sample is drying shows an increasingly dense matrix of fibrils. C) After the kinetic series from (A) was recorded and the sample fully dehydrated, air imaging displays the entanglement of the fibrils forming a gel. D) Placing a 30 mg mL-1 gel on glass reveals porous structures, comprising cavities with diameters of tens of nanometers.","type":"Figure"}],"term_comment":"","term_def":"\"A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a supramolecular fiber, a polymer consisting of an indefinite number of protein or protein complex subunits that have polymerised to form a fiber-shaped structure.\" [GOC:pr]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-11T14:55:39.836Z"}},{"start":1,"end":94,"reference_id":"34750927","reference_source":"pmid","reference_html":"Intrinsically Disordered Tardigrade Proteins Self-Assemble into Fibrous Gels in Response to Environmental Stress. <i> Malki A, Teulon JM, Camacho-Zarco AR, Chen SW, Adamski W, Maurin D, Salvi N, Pellequer JL, Blackledge M. </i> Angew Chem Int Ed Engl, 2022","date":"2022-06-13T13:37:30.399Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP01384r014","statement":[{"text":"NMR spectroscopy reveals that the protein comprises an extended central helical domain flanked by disordered termini.","type":"Abstract"},{"text":"By using high-field NMR spectroscopy, we reveal that the protein comprises an extended central helical domain, with apparent coiled-coil propensity, flanked by long, highly disordered N- and C-terminal domains.","type":"Results"},{"text":"NMR spectroscopic analysis of the gels formed from 15N-labelled CAHS-8 demonstrates that the intrinsically disordered domains (excluding helix a1) remain flexible in the context of the fibrillar gel (Figure 4 A).","type":"Results"},{"text":"15N spin relaxation rates reveal an overall similar dynamic behaviour of the N- terminal intrinsically disordered region at 303K as the protein in free solution. The 62–72 strand, comprising both hydrophobic and acidic residues, shows elevated R2 values, which suggests increased correlation times, possibly arising from interaction with more rigid elements of the gel.","type":"Results"},{"text":"We describe the monomeric behaviour of the protein as partially disordered, with a long two-helical domain flanked by long flexible tails.","type":"Conclusion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-11T14:55:36.951Z"}},{"start":196,"end":227,"reference_id":"34750927","reference_source":"pmid","reference_html":"Intrinsically Disordered Tardigrade Proteins Self-Assemble into Fibrous Gels in Response to Environmental Stress. <i> Malki A, Teulon JM, Camacho-Zarco AR, Chen SW, Adamski W, Maurin D, Salvi N, Pellequer JL, Blackledge M. </i> Angew Chem Int Ed Engl, 2022","date":"2022-06-13T13:34:31.076Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP01384r015","statement":[{"text":"NMR spectroscopy reveals that the protein comprises an extended central helical domain flanked by disordered termini.","type":"Abstract"},{"text":"By using high-field NMR spectroscopy, we reveal that the protein comprises an extended central helical domain, with apparent coiled-coil propensity, flanked by long, highly disordered N- and C-terminal domains.","type":"Results"},{"text":"NMR spectroscopic analysis of the gels formed from 15N-labelled CAHS-8 demonstrates that the intrinsically disordered domains (excluding helix a1) remain flexible in the context of the fibrillar gel (Figure 4 A).","type":"Results"},{"text":"The C-terminal domain shows a similar dynamic behaviour to the monomeric phase","type":"Results"},{"text":"We describe the monomeric behaviour of the protein as partially disordered, with a long two-helical domain flanked by long flexible tails.","type":"Conclusion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-11T14:55:33.318Z"}},{"start":95,"end":195,"reference_id":"34750927","reference_source":"pmid","reference_html":"Intrinsically Disordered Tardigrade Proteins Self-Assemble into Fibrous Gels in Response to Environmental Stress. <i> Malki A, Teulon JM, Camacho-Zarco AR, Chen SW, Adamski W, Maurin D, Salvi N, Pellequer JL, Blackledge M. </i> Angew Chem Int Ed Engl, 2022","date":"2022-06-13T13:46:33.393Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000013","term_name":"pre-molten globule to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP01384r016","statement":[{"text":"NMR spectroscopy reveals that the protein comprises an extended central helical domain flanked by disordered termini. Upon concentration, the protein is shown to successively form oligomers, long fibres, and finally gels constituted of fibres in a strongly temperature-dependent manner. The helical domain forms the core of the fibrillar structure","type":"Abstract"},{"text":"By using high-field NMR spectroscopy, we reveal that the protein comprises an extended central helical domain, with apparent coiled-coil propensity","type":"Results"},{"text":"The 13C chemical shifts show strong temperature dependence, reveal- ing a significantly higher helical content at 278 K for helix a2 (see FigureS3). The 15N relaxation is also temperature dependent (Figure 2 C and see also Figure S4), notably higher than that normally observed in intrinsically disordered proteins containing helical elements[21, 22] (see Figure S2), thus supporting the formation of higher order oligomers at lower temperature.","type":"Results"},{"text":"No signals from helix a1 were detected in the 15N-1H HSQC spectrum of a gel formed from 15N-labelled CAHS-8","type":"Results"},{"text":"Signals from helix a2 are visible in the spectrum, but show considerably higher relaxation rates than those in free solution (25 s-1 compared to 10 s-1), which suggests that this domain is tethered to a much larger, or immobile, object.","type":"Results"},{"text":"On the basis of these observations, we propose that the long helical domains of the partially disordered protein associate through coiled-coil-like interactions under certain environmental conditions (low temperature, high concentration) to form oligomers, then fibrils (Figure 5 C), which eventually form a gel-like matrix.","type":"Discussion"},{"text":"We describe the monomeric behaviour of the protein as partially disordered, with a long two-helical domain flanked by long flexible tails. We propose that this domain mediates homo-dimerization through a coiled-coil interaction, and have experimentally observed the successive formation of oligomers, fibrils, and eventually gels in response to concentration and temperature change.","type":"Conclusion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-11T14:55:29.370Z"}}],"released":"2018_11","uniref100":"UniRef100_P0CU48","date":"2018-07-16T11:22:06.000Z","acc":"P0CU50","name":"Cytosolic-abundant heat soluble protein 94063","length":227,"organism":"Hypsibius dujardini","dataset":["Stress response proteins"],"UniParc":"UPI000A27FC39","genes":[{"name":{"value":"CAHS 94063","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"28306513","url":"http://www.ncbi.nlm.nih.gov/pubmed/28306513","alternativeUrl":"https://europepmc.org/abstract/MED/28306513"}}]}}],"alphafold_very_low_content":0.31277533039647576,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":94,"type":"D"},{"start":95,"end":195,"type":"T"},{"start":196,"end":227,"type":"D"}],"Structural state":[{"start":1,"end":227,"type":"D"}],"Biological process":[{"start":1,"end":227,"type":"F"}],"Disorder function":[{"start":1,"end":94,"type":"F"},{"start":196,"end":227,"type":"F"}],"Structural transition":[{"start":95,"end":195,"type":"T"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_P0CU49","sequence":"MFLARNVSRVALRSASLSPAAIPQQQHAGVAAVYAVRFASSSGSGRPADNWAESQKEKAKAGLKDAQAEVGKVAREVKDKAAGGIEQAKDAVKQGANDLKRSGSRTFENAKDDIQAKAQHAKSDLKGAKHQAEGVVENVKEAAENAWEKTKDVAENLKDKVQSPGGLADKAANAWETVKDRAQDAASEVKHKAGDLKDKAQQVIHDATTQSGDNRKQDQQQRRDSQGSQSGQNSRSRN","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Tardigrada","Eutardigrada","Parachela","Hypsibioidea","Hypsibiidae","Hypsibius"],"uniref90":"UniRef90_P0CU49","disprot_id":"DP01386","ncbi_taxon_id":232323,"regions_counter":3,"creator":"mmacossay","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":238,"region_id":"DP01386r001","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","statement":[{"text":"For α-synuclein, a known disordered protein, and for CAHS proteins, the crosspeaks occur over a narrower window (Figure 2, top), from ~8.0 to ~8.6 ppm, which coincides with the range for amide protons in the central residue of unstructured tripeptides (Schwarzinger et al., 2000).","type":"Results"},{"text":"IDPs lack persistent secondary structure (Theillet et al., 2014; Yamaguchi et al., 2012), which we confirmed for CAHS proteins using nuclear magnetic resonance spectroscopy (NMR).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-28T15:52:53.356Z","reference_source":"pmid","term_name":"disorder","reference_id":"28306513","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":238,"region_id":"DP01386r002","released":"2023_12","ec_id":"ECO:0006196","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","statement":[{"text":"For the disordered proteins tested (α-synuclein and CAHS proteins), nearly all the amide protons were exchanged for deuterons within 20 min, as shown by the decrease in intensity of the one-dimensional proton spectrum (Figure 2).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-28T15:50:34.397Z","reference_source":"pmid","term_name":"disorder","reference_id":"28306513","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":238,"reference_id":"28306513","reference_source":"pmid","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","date":"2024-03-22T16:09:20.461Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0009269","term_name":"response to desiccation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007117","ec_ontology":"ECO","ec_name":"mutant physiological response evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IMP","region_id":"DP01386r003","statement":[{"text":"Several CAHS proteins were sufficient to increase the desiccation tolerance of yeast nearly 100-fold (Figure 6A). ","type":"Results"},{"text":"Tardigrade-Specific IDPs Increase Desiccation Tolerance in Heterologous Systems and In Vitro","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a desiccation stimulus, extreme dryness resulting from the prolonged deprivation of water.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_P0CU49","date":"2018-07-16T11:24:45.000Z","acc":"P0CU49","name":"Cytosolic-abundant heat soluble protein 68135","length":238,"organism":"Hypsibius dujardini","dataset":["Stress response proteins"],"UniParc":"UPI0009F0E043","genes":[],"alphafold_very_low_content":0.42436974789915966,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":238,"type":"D"}],"Structural state":[{"start":1,"end":238,"type":"D"}],"Biological process":[{"start":1,"end":238,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_P0CU43","sequence":"MEAMNMNIPRDAMFVPPPESEQNGYHEKSEVQQTSYMQSQVKVPHYNFPTPYFTTSFSAQELLGEGFQASISRISAVTEDMQSMEIPEFVEEARRDYAAKTRENEMLGQQYEKELERKSEAYRKHQEVEADKIRKELEKQHMRDIEFRKEIAELAIENQKRMIDLECRYAKKDMDRERTKVRMMLEQQKFHSDIQVNLDSSAAGTESGGHVVSQSEKFTERNREMKR","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Tardigrada","Eutardigrada","Parachela","Macrobiotoidea","Macrobiotidae","Paramacrobiotus","Paramacrobiotus richtersi group"],"uniref90":"UniRef90_P0CU52","disprot_id":"DP01388","ncbi_taxon_id":697321,"regions_counter":3,"creator":"mmacossay","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":227,"region_id":"DP01388r001","released":"2023_12","ec_id":"ECO:0006196","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","statement":[{"text":"For the disordered proteins tested (α-synuclein and CAHS proteins), nearly all the amide protons were exchanged for deuterons within 20 min, as shown by the decrease in intensity of the one-dimensional proton spectrum (Figure 2).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-28T15:50:52.139Z","reference_source":"pmid","term_name":"disorder","reference_id":"28306513","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":227,"region_id":"DP01388r002","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","statement":[{"text":"IDPs lack persistent secondary structure (Theillet et al., 2014; Yamaguchi et al., 2012), which we confirmed for CAHS proteins using nuclear magnetic resonance spectroscopy (NMR).","type":"Results"},{"text":"For α-synuclein, a known disordered protein, and for CAHS proteins, the crosspeaks occur over a narrower window (Figure 2, top), from ~8.0 to ~8.6 ppm, which coincides with the range for amide protons in the central residue of unstructured tripeptides (Schwarzinger et al., 2000).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-28T15:53:06.848Z","reference_source":"pmid","term_name":"disorder","reference_id":"28306513","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":227,"reference_id":"28306513","reference_source":"pmid","reference_html":"Tardigrades Use Intrinsically Disordered Proteins to Survive Desiccation. <i> Boothby TC, Tapia H, Brozena AH, Piszkiewicz S, Smith AE, Giovannini I, Rebecchi L, Pielak GJ, Koshland D, Goldstein B. </i> Mol Cell, 2017","date":"2024-03-22T16:12:22.710Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0009269","term_name":"response to desiccation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007117","ec_ontology":"ECO","ec_name":"mutant physiological response evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IMP","region_id":"DP01388r003","statement":[{"text":"Several CAHS proteins were sufficient to increase the desiccation tolerance of yeast nearly 100-fold (Figure 6A). Similar results were obtained in bacteria, with exogenous expression of some CAHS proteins resulting in increases of more than 2 orders of magnitude in desiccation tolerance (Figure 6B). Importantly, α-synuclein, a protein that exists as a disordered monomer in cells (Fauvet et al., 2012; Theillet et al., 2016) and has no known connection to stress tolerance (Drescher et al., 2012; Theillet et al., 2014), did not increase survival under drying conditions (Figure 6B), demonstrating that something beyond intrinsic disorder of TDPs is essential for their protective capabilities.","type":"Results"},{"text":"Tardigrade-Specific IDPs Increase Desiccation Tolerance in Heterologous Systems and In Vitro","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a desiccation stimulus, extreme dryness resulting from the prolonged deprivation of water.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_P0CU52","date":"2018-07-16T11:36:55.000Z","acc":"P0CU52","name":"Cytosolic-abundant heat soluble protein 106094","length":227,"organism":"Paramacrobiotus richtersi","dataset":["Stress response proteins"],"UniParc":"UPI000A27FC3C","genes":[{"name":{"value":"CAHS 106094","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"28306513","url":"http://www.ncbi.nlm.nih.gov/pubmed/28306513","alternativeUrl":"https://europepmc.org/abstract/MED/28306513"}}]}}],"alphafold_very_low_content":0.2907488986784141,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":227,"type":"D"}],"Structural state":[{"start":1,"end":227,"type":"D"}],"Biological process":[{"start":1,"end":227,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00125","name":"Core histone H2A/H2B/H3/H4 domain","start":44,"end":131}],"gene3D":[{"start":2,"end":136,"id":"1.10.20.10","name":"Histone, subunit A"}]},"uniref50":"UniRef50_Q71DI3","sequence":"MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Amphibia","Batrachia","Anura","Pipoidea","Pipidae","Xenopodinae","Xenopus","Xenopus"],"uniref90":"UniRef90_Q71DI3","disprot_id":"DP01389","ncbi_taxon_id":8355,"regions_counter":3,"creator":"ldobson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":35,"region_id":"DP01389r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Histone H3 and H4 N-terminal tails in nucleosome arrays at cellular concentrations probed by magic angle spinning NMR spectroscopy. <i> Gao M, Nadaud PS, Bernier MW, North JA, Hammel PC, Poirier MG, Jaroniec CP. </i> J Am Chem Soc, 2013","statement":[{"text":"A strong correlation exists between the most dynamic histone residues identified in the current study, amino acids 1–35 in H3 and 1–21 in H4, and the crystal structure of the nucleosome core particle which reveals the same residues as being largely unstructured.","type":"Conclusion"}],"term_id":"IDPO:0000002","curator_id":"jlamb","start":1,"term_ontology":"IDPO","curator_name":"John Lamb","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0568-8281","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1KX5"}],"reference_id":"24088044","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-21T16:01:23.541Z"}},{"start":1,"end":37,"reference_id":"37551430","reference_source":"pmid","reference_html":"A dual role for the chromatin reader ORCA/LRWD1 in targeting the origin recognition complex to chromatin. <i> Sahu S, Ekundayo BE, Kumar A, Bleichert F. </i> EMBO J, 2023","date":"2026-05-13T15:44:19.533Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":1,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly103Ala","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"8SIY"}],"region_id":"DP01389r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A140UHX1"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62799"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06897"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02281"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q75PQ8"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null}],"sequence_construct":"ARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA","statement":[{"text":"This region is not visible in the structure.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-13T15:44:22.075Z"}},{"start":1,"end":37,"reference_id":"37551430","reference_source":"pmid","reference_html":"A dual role for the chromatin reader ORCA/LRWD1 in targeting the origin recognition complex to chromatin. <i> Sahu S, Ekundayo BE, Kumar A, Bleichert F. </i> EMBO J, 2023","date":"2025-03-21T16:00:29.803Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly103Ala","start":null,"end":null,"position":null}],"region_id":"DP01389r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A140UHX1"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62799"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06897"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02281"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q75PQ8"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":"Widom 601 DNA is part of the complex, with sequence: ATCCTGGAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGACAGCTCTAGCACCGCTTAAACGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGGATTACTCCCTAGTCTCCAGGCACGTGTCAGATATATACATCCTGTGAT"}],"sequence_construct":"ARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA","statement":[{"text":"This region is not visible in the structure indicating it is disordered. ","type":"Curator statement"}]}],"released":"2018_11","uniref100":"UniRef100_Q71DI3","date":"2018-07-16T11:54:20.000Z","acc":"P84233","name":"Histone H3.2","length":136,"organism":"Xenopus laevis","dataset":[],"UniParc":"UPI000001C8EC","genes":[],"alphafold_very_low_content":0.022058823529411766,"disorder_content":0.27205882352941174,"disprot_consensus":{"full":[{"start":1,"end":37,"type":"D"}],"Structural state":[{"start":1,"end":37,"type":"D"}],"Disorder function":[{"start":1,"end":37,"type":"F"}]}},{"features":{"pfam":[{"id":"PF15511","name":"Centromere kinetochore component CENP-T histone fold","start":44,"end":96}],"gene3D":[{"start":2,"end":103,"id":"1.10.20.10","name":"Histone, subunit A"}]},"uniref50":"UniRef50_P62805","sequence":"MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Amphibia","Batrachia","Anura","Pipoidea","Pipidae","Xenopodinae","Xenopus","Xenopus"],"uniref90":"UniRef90_P62805","disprot_id":"DP01390","ncbi_taxon_id":8355,"regions_counter":3,"creator":"ldobson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":21,"region_id":"DP01390r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Histone H3 and H4 N-terminal tails in nucleosome arrays at cellular concentrations probed by magic angle spinning NMR spectroscopy. <i> Gao M, Nadaud PS, Bernier MW, North JA, Hammel PC, Poirier MG, Jaroniec CP. </i> J Am Chem Soc, 2013","statement":[{"text":"A strong correlation exists between the most dynamic histone residues identified in the current study, amino acids 1–35 in H3 and 1–21 in H4, and the crystal structure of the nucleosome core particle which reveals the same residues as being largely unstructured.","type":"Conclusion"}],"term_id":"IDPO:0000002","curator_id":"jlamb","start":1,"term_ontology":"IDPO","curator_name":"John Lamb","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0568-8281","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1KX5"}],"reference_id":"24088044","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-21T16:03:03.637Z"}},{"start":1,"end":24,"reference_id":"37551430","reference_source":"pmid","reference_html":"A dual role for the chromatin reader ORCA/LRWD1 in targeting the origin recognition complex to chromatin. <i> Sahu S, Ekundayo BE, Kumar A, Bleichert F. </i> EMBO J, 2023","date":"2026-05-13T15:46:55.635Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":3,"cross_refs":[{"db":"PDB","id":"8SIY"}],"region_id":"DP01390r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A140UHX1"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06897"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02281"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q75PQ8"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84233"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null}],"statement":[{"text":"This region is not visible in the structure.","type":"Curator statement"}],"sequence_construct":"SGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-13T15:47:12.439Z"}},{"start":1,"end":24,"reference_id":"37551430","reference_source":"pmid","reference_html":"A dual role for the chromatin reader ORCA/LRWD1 in targeting the origin recognition complex to chromatin. <i> Sahu S, Ekundayo BE, Kumar A, Bleichert F. </i> EMBO J, 2023","date":"2026-05-13T15:46:50.016Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"8SIY"}],"region_id":"DP01390r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A140UHX1"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06897"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02281"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q75PQ8"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting Widom 601 dsDNA with sequence: ATCCTGGAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGACAGCTCTAGCACCGCTTAAACGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGGATTACTCCCTAGTCTCCAGGCACGTGTCAGATATATACATCCTGTGAT"}]}],"statement":[{"text":"The PDB-deposited data indicate that this region lacks electron density. As it appears to be part of the analyzed sample, the absence of electron density is likely due to its disordered nature, consistent with predicted data.","type":"Curator statement"}]}],"released":"2018_11","uniref100":"UniRef100_P62805","date":"2018-07-16T11:56:40.000Z","acc":"P62799","name":"Histone H4","length":103,"organism":"Xenopus laevis","dataset":[],"UniParc":"UPI0000027039","genes":[],"alphafold_very_low_content":0.009708737864077669,"disorder_content":0.23300970873786409,"disprot_consensus":{"full":[{"start":1,"end":24,"type":"D"}],"Structural state":[{"start":1,"end":24,"type":"D"}],"Disorder function":[{"start":1,"end":24,"type":"F"}]}},{"acc":"P03520","sequence":"MDNLTKVREYLKSYSRLDQAVGEIDEIEAQRAEKSNYELFQEDGVEEHTKPSYFQAADDSDTESEPEIEDNQGLYAQDPEAEQVEGFIQGPLDDYADEEVDVVFTSDWKPPELESDEHGKTLRLTSPEGLSGEQKSQWLSTIKAVVQSAKYWNLAECTFEASGEGVIMKERQITPDVYKVTPVMNTHPSQSEAVSDVWSLSKTSMTFQPKKASLQPLTISLDELFSSRGEFISVGGDGRMSHKEAILLGLRYKKLYNQARVKYSL","creator":"jlamb","dataset":["Viral proteins","Condensates-related proteins","RNA-binding proteins"],"date":"2018-07-16T12:02:02.000Z","disprot_id":"DP01391","features":{"pfam":[{"id":"PF00922","name":"Vesiculovirus phosphoprotein","start":4,"end":263}],"gene3D":[{"start":180,"end":265,"id":"1.10.8.440","name":"Vesicular stomatitis virus phosphoprotein C-terminal domain","_id":"685af523b4ac24d5329d9025"}]},"genes":[{"name":{"value":"P","evidences":[],"_id":"685af523b4ac24d5329d9058"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d9057"}],"length":265,"name":"Phosphoprotein","ncbi_taxon_id":11285,"organism":"Vesicular stomatitis Indiana virus (strain San Juan)","regions_counter":10,"released":"2018_11","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Rhabdoviridae","Vesiculovirus"],"UniParc":"UPI0000038D14","uniref100":"UniRef100_P03520","uniref50":"UniRef50_P03520","uniref90":"UniRef90_P03520","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":60,"interaction_partner":[],"reference_html":"The N(0)-binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient α-helices. <i> Leyrat C, Jensen MR, Ribeiro EA, Gérard FC, Ruigrok RW, Blackledge M, Jamin M. </i> Protein Sci, 2011","reference_id":"21207454","region_id":"DP01391r001","released":"2022_03","sample":[],"statement":[{"type":"Title","text":"The N(0)-binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient α-helices.","_id":"685af523b4ac24d5329d9027"},{"type":"Abstract","text":"Here, using nuclear magnetic resonance (NMR) spectroscopy and small-angle X-ray scattering (SAXS), we show that an isolated peptide corresponding to the 60 first N-terminal residues of VSV P (P(60)) and encompassing P(NTR) has overall molecular dimensions and a dynamic behavior characteristic of a disordered protein but transiently populates conformers containing α-helices.","_id":"685af523b4ac24d5329d9028"},{"type":"Results","text":"Isolated VSV P60 is intrinsically disordered but exhibits transient secondary structures","_id":"685af523b4ac24d5329d9029"},{"type":"Results","text":"The 2D 1H-15N-HSQC NMR spectrum of P60 exhibited narrow line widths and poor dispersion of the amide proton chemical shifts (Fig. 3), in agreement with structural disorder in solution. These results indicate that VSV P60 has overall molecular dimensions and NMR spectroscopic properties of a disordered protein, as shown previously for RV P68.","_id":"685af523b4ac24d5329d902a"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-11T14:46:34.025Z","_id":"685af523b4ac24d5329d902b"},"version":3,"_id":"685af523b4ac24d5329d9026","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":60,"interaction_partner":[],"reference_html":"The N(0)-binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient α-helices. <i> Leyrat C, Jensen MR, Ribeiro EA, Gérard FC, Ruigrok RW, Blackledge M, Jamin M. </i> Protein Sci, 2011","reference_id":"21207454","region_id":"DP01391r003","released":"2022_03","sample":[],"statement":[{"type":"Title","text":"The N(0)-binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient α-helices.","_id":"685af523b4ac24d5329d9031"},{"type":"Abstract","text":"Here, using nuclear magnetic resonance (NMR) spectroscopy and small-angle X-ray scattering (SAXS), we show that an isolated peptide corresponding to the 60 first N-terminal residues of VSV P (P(60)) and encompassing P(NTR) has overall molecular dimensions and a dynamic behavior characteristic of a disordered protein but transiently populates conformers containing α-helices.","_id":"685af523b4ac24d5329d9032"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-11T14:46:35.452Z","_id":"685af523b4ac24d5329d9033"},"version":3,"_id":"685af523b4ac24d5329d9030","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":60,"interaction_partner":[],"reference_html":"The N(0)-binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient α-helices. <i> Leyrat C, Jensen MR, Ribeiro EA, Gérard FC, Ruigrok RW, Blackledge M, Jamin M. </i> Protein Sci, 2011","reference_id":"21207454","region_id":"DP01391r005","released":"2022_03","sample":[],"statement":[{"type":"Title","text":"The N(0)-binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient α-helices.","_id":"685af523b4ac24d5329d9039"},{"type":"Abstract","text":"Here, using nuclear magnetic resonance (NMR) spectroscopy and small-angle X-ray scattering (SAXS), we show that an isolated peptide corresponding to the 60 first N-terminal residues of VSV P (P(60)) and encompassing P(NTR) has overall molecular dimensions and a dynamic behavior characteristic of a disordered protein but transiently populates conformers containing α-helices.","_id":"685af523b4ac24d5329d903a"},{"type":"Results","text":"Isolated VSV P60 is intrinsically disordered but exhibits transient secondary structures","_id":"685af523b4ac24d5329d903b"},{"type":"Results","text":"The far-UV CD spectrum exhibited a prominent shoulder near 222 nm and a minimum near 205 nm, suggesting the presence of α-helical structure (Fig. 4). Assuming that the molar ellipticity value at 222 nm reports only on the presence of α-helix, the average helical content of P60 was estimated to be 7%.12,42 NMR spectroscopy is highly sensitive to local structure and therefore provides information about the location and population of fluctuating secondary structures within an otherwise flexible protein.","_id":"685af523b4ac24d5329d903c"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-11T14:46:36.849Z","_id":"685af523b4ac24d5329d903d"},"version":1,"_id":"685af523b4ac24d5329d9038","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007062","ec_name":"light scattering evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":60,"interaction_partner":[],"reference_html":"The N(0)-binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient α-helices. <i> Leyrat C, Jensen MR, Ribeiro EA, Gérard FC, Ruigrok RW, Blackledge M, Jamin M. </i> Protein Sci, 2011","reference_id":"21207454","region_id":"DP01391r006","released":"2022_03","sample":[],"statement":[{"type":"Title","text":"The N(0)-binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient α-helices.","_id":"685af523b4ac24d5329d903f"},{"type":"Abstract","text":"Here, using nuclear magnetic resonance (NMR) spectroscopy and small-angle X-ray scattering (SAXS), we show that an isolated peptide corresponding to the 60 first N-terminal residues of VSV P (P(60)) and encompassing P(NTR) has overall molecular dimensions and a dynamic behavior characteristic of a disordered protein but transiently populates conformers containing α-helices.","_id":"685af523b4ac24d5329d9040"},{"type":"Results","text":"Isolated VSV P60 is intrinsically disordered but exhibits transient secondary structures","_id":"685af523b4ac24d5329d9041"},{"type":"Results","text":"The N-terminal domain of VSV P (P60, aa 1–60) was produced in Escherichia coli as a recombinant protein containing a C-terminal His-tag (8 aa). The long-term stability of P60 was significantly improved in the presence of a mixture of 50 mMl-Arg and 50 mMl-Glu.39 Under these conditions, an average molecular mass of 7.2 ± 0.7 kDa was determined by SEC combined with detection by multiangle laser light scattering and refractometry (SEC/MALLS/RI), indicating that P60 was monomeric (MM calculated from the sequence = 8054 Da) and well behaved in solution up to concentrations of 2 mM (Fig. 1). Its Stokes' radius of 2.3 ± 0.1 nm indicated an extended conformation, closer to that expected for an unfolded protein of the same molecular mass (RS = 2.5 nm) than to that expected for a globular protein (RS = 1.5 nm).","_id":"685af523b4ac24d5329d9042"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-11T14:46:38.416Z","_id":"685af523b4ac24d5329d9043"},"version":1,"_id":"685af523b4ac24d5329d903e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3PMK","_id":"685af523b4ac24d5329d9045"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":6,"end":33,"interaction_partner":[],"reference_html":"Structure of the vesicular stomatitis virus N⁰-P complex. <i> Leyrat C, Yabukarski F, Tarbouriech N, Ribeiro EA, Jensen MR, Blackledge M, Ruigrok RW, Jamin M. </i> PLoS Pathog, 2011","reference_id":"21960769","region_id":"DP01391r007","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Replication of non-segmented negative-strand RNA viruses requires the continuous supply of the nucleoprotein (N) in the form of a complex with the phosphoprotein (P). Here, we present the structural characterization of a soluble, heterodimeric complex between a variant of vesicular stomatitis virus N lacking its 21 N-terminal residues (NΔ21) and a peptide of 60 amino acids (P60) encompassing the molecular recognition element (MoRE) of P that binds RNA-free N (N0). The complex crystallized in a decameric circular form, which was solved at 3.0 Å resolution, reveals how the MoRE folds upon binding to N and competes with RNA binding and N polymerization.","_id":"685af523b4ac24d5329d9046"},{"type":"Curator statement","text":"The authors describe a structure of the vesicular stomatitis virus N⁰-P complex (PDB:3PMK), using a recombinant phosphoprotein (UniProt ACC: B7UCZ3) whose N-terminal region is identical to the phosphoprotein here annotated.","_id":"685af523b4ac24d5329d9047"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-11T14:46:32.569Z","_id":"685af523b4ac24d5329d9048"},"version":1,"_id":"685af523b4ac24d5329d9044","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3PMK","_id":"685af523b4ac24d5329d904a"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":6,"end":33,"interaction_partner":[{"db":"UniProt","id":"B7UCZ2","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d904b"}],"reference_html":"Structure of the vesicular stomatitis virus N⁰-P complex. <i> Leyrat C, Yabukarski F, Tarbouriech N, Ribeiro EA, Jensen MR, Blackledge M, Ruigrok RW, Jamin M. </i> PLoS Pathog, 2011","reference_id":"21960769","region_id":"DP01391r008","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Replication of non-segmented negative-strand RNA viruses requires the continuous supply of the nucleoprotein (N) in the form of a complex with the phosphoprotein (P). Here, we present the structural characterization of a soluble, heterodimeric complex between a variant of vesicular stomatitis virus N lacking its 21 N-terminal residues (NΔ21) and a peptide of 60 amino acids (P60) encompassing the molecular recognition element (MoRE) of P that binds RNA-free N (N0). The complex crystallized in a decameric circular form, which was solved at 3.0 Å resolution, reveals how the MoRE folds upon binding to N and competes with RNA binding and N polymerization.","_id":"685af523b4ac24d5329d904c"},{"type":"Curator statement","text":"The authors describe a structure of the vesicular stomatitis virus N⁰-P complex (PDB:3PMK), using a recombinant phosphoprotein (UniProt ACC: B7UCZ3) whose N-terminal region is identical to the phosphoprotein here annotated.","_id":"685af523b4ac24d5329d904d"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-11T14:46:31.110Z","_id":"685af523b4ac24d5329d904e"},"version":1,"_id":"685af523b4ac24d5329d9049","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":6,"end":33,"interaction_partner":[],"reference_html":"Structure of the vesicular stomatitis virus N⁰-P complex. <i> Leyrat C, Yabukarski F, Tarbouriech N, Ribeiro EA, Jensen MR, Blackledge M, Ruigrok RW, Jamin M. </i> PLoS Pathog, 2011","reference_id":"21960769","region_id":"DP01391r009","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Replication of non-segmented negative-strand RNA viruses requires the continuous supply of the nucleoprotein (N) in the form of a complex with the phosphoprotein (P). Here, we present the structural characterization of a soluble, heterodimeric complex between a variant of vesicular stomatitis virus N lacking its 21 N-terminal residues (NΔ21) and a peptide of 60 amino acids (P60) encompassing the molecular recognition element (MoRE) of P that binds RNA-free N (N0). The complex crystallized in a decameric circular form, which was solved at 3.0 Å resolution, reveals how the MoRE folds upon binding to N and competes with RNA binding and N polymerization.","_id":"685af523b4ac24d5329d9050"},{"type":"Curator statement","text":"The authors describe a structure of the vesicular stomatitis virus N⁰-P complex (PDB:3PMK), using a recombinant phosphoprotein (UniProt ACC: B7UCZ3) whose N-terminal region is identical to the phosphoprotein here annotated.","_id":"685af523b4ac24d5329d9051"}],"states_connection":[],"term_comment":"","term_def":"\"Any process involved directly in viral genome replication, including viral nucleotide metabolism.\" [ISBN:0781702534]","term_go_domain":"P","term_id":"GO:0019079","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral genome replication","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-11T14:46:28.329Z","_id":"685af523b4ac24d5329d9052"},"version":1,"_id":"685af523b4ac24d5329d904f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0007066","ec_name":"static light scattering assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":60,"interaction_partner":[],"reference_html":"Structure of the vesicular stomatitis virus N⁰-P complex. <i> Leyrat C, Yabukarski F, Tarbouriech N, Ribeiro EA, Jensen MR, Blackledge M, Ruigrok RW, Jamin M. </i> PLoS Pathog, 2011","reference_id":"21960769","region_id":"DP01391r010","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"The characterization by absorbance spectroscopy and size-exclusion chromatography (SEC) combined with static light scattering (MALLS) demonstrates that both NΔ210-P60 and NΔ210-P dimer complexes are free of RNA in solution, forming soluble heterodimers or heterotrimers, respectively. Therefore, P60 fulfills both chaperone activities of full-length P.","_id":"685af523b4ac24d5329d9054"},{"type":"Curator statement","text":"The authors use a recombinant phosphoprotein (UniProt ACC: B7UCZ3) whose N-terminal region (1-60) is identical to the phosphoprotein here annotated.","_id":"685af523b4ac24d5329d9055"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA or an RNA-containing complex to assist the folding process.\" [PMID:31165735]","term_go_domain":"F","term_id":"GO:0140691","term_is_binding":false,"term_is_obsolete":false,"term_name":"RNA folding chaperone","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-11T14:46:26.852Z","_id":"685af523b4ac24d5329d9056"},"version":1,"_id":"685af523b4ac24d5329d9053","reference_source":"pmid"}],"__v":0,"disorder_content":0.22641509433962265,"disprot_consensus":{"full":[{"start":1,"end":5,"type":"D"},{"start":6,"end":33,"type":"T"},{"start":34,"end":60,"type":"D"}],"Structural state":[{"start":1,"end":60,"type":"D"}],"Structural transition":[{"start":6,"end":33,"type":"T"}],"Molecular function":[{"start":1,"end":60,"type":"F"}],"Biological process":[{"start":6,"end":33,"type":"F"}]}},{"features":{"pfam":[{"id":"PF09510","name":"Rtt102p-like transcription regulator protein","start":6,"end":140}]},"uniref50":"UniRef50_P53330","sequence":"MDPQTLITKANKVSYYGNPTSKESWRYDWYQPSKVSSNVQQPQQQLGDMENNLEKYPFRYKTWLRNQEDEKNLQRESCEDILDLKEFDRRILKKSLMTSHTKGDTSKATGAPSANQGDEALSVDDIRGAVGNSEAIPGLSAGVNNDNTKESKDVKMN","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P53330","disprot_id":"DP01392","ncbi_taxon_id":559292,"regions_counter":6,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":53,"region_id":"DP01392r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of an actin-related subcomplex of the SWI/SNF chromatin remodeler. <i> Schubert HL, Wittmeyer J, Kasten MM, Hinata K, Rawling DC, Héroux A, Cairns BR, Hill CP. </i> Proc Natl Acad Sci U S A, 2013","statement":[{"text":"Missing electron density.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":35,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4I6M"}],"reference_id":"23401505","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-02-05T14:40:45.185Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":53,"region_id":"DP01392r002","released":"2024_06","ec_id":"ECO:0006220","reference_html":"Actin-related proteins regulate the RSC chromatin remodeler by weakening intramolecular interactions of the Sth1 ATPase. <i> Turegun B, Baker RW, Leschziner AE, Dominguez R. </i> Commun Biol, 2018","statement":[{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":36,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-05T15:35:52.359Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5TGC"}],"reference_id":"29809203","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q05123 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q12406"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5957"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":157,"region_id":"DP01392r003","released":"2024_06","ec_id":"ECO:0006220","reference_html":"Actin-related proteins regulate the RSC chromatin remodeler by weakening intramolecular interactions of the Sth1 ATPase. <i> Turegun B, Baker RW, Leschziner AE, Dominguez R. </i> Commun Biol, 2018","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":91,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-05T15:35:23.593Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5TGC"}],"reference_id":"29809203","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q05123 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q12406"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5957"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":157,"region_id":"DP01392r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of an actin-related subcomplex of the SWI/SNF chromatin remodeler. <i> Schubert HL, Wittmeyer J, Kasten MM, Hinata K, Rawling DC, Héroux A, Cairns BR, Hill CP. </i> Proc Natl Acad Sci U S A, 2013","statement":[{"text":"Missing electron density.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":91,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4I6M"}],"reference_id":"23401505","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-02-05T14:40:28.651Z"}}],"released":"2018_11","uniref100":"UniRef100_P53330","date":"2018-07-16T12:16:04.000Z","acc":"P53330","name":"Regulator of Ty1 transposition protein 102","length":157,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000013AFCE","genes":[{"name":{"value":"RTT102"},"orfNames":[{"value":"G9378"}],"olnNames":[{"value":"YGR275W"}]}],"alphafold_very_low_content":0.2929936305732484,"disorder_content":0.5477707006369427,"disprot_consensus":{"full":[{"start":35,"end":53,"type":"D"},{"start":91,"end":157,"type":"D"}],"Structural state":[{"start":35,"end":53,"type":"D"},{"start":91,"end":157,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00057","name":"Low-density lipoprotein receptor domain class A","start":26,"end":63},{"id":"PF00057","name":"Low-density lipoprotein receptor domain class A","start":67,"end":104},{"id":"PF00057","name":"Low-density lipoprotein receptor domain class A","start":107,"end":143},{"id":"PF00057","name":"Low-density lipoprotein receptor domain class A","start":147,"end":184},{"id":"PF00057","name":"Low-density lipoprotein receptor domain class A","start":196,"end":231},{"id":"PF00057","name":"Low-density lipoprotein receptor domain class A","start":235,"end":270},{"id":"PF00057","name":"Low-density lipoprotein receptor domain class A","start":276,"end":313},{"id":"PF00058","name":"Low-density lipoprotein receptor repeat class B","start":439,"end":483},{"id":"PF00058","name":"Low-density lipoprotein receptor repeat class B","start":487,"end":526},{"id":"PF00058","name":"Low-density lipoprotein receptor repeat class B","start":529,"end":569},{"id":"PF00058","name":"Low-density lipoprotein receptor repeat class B","start":573,"end":614},{"id":"PF00058","name":"Low-density lipoprotein receptor repeat class B","start":616,"end":656},{"id":"PF07645","name":"Calcium-binding EGF domain","start":354,"end":392},{"id":"PF14670","name":"Coagulation Factor Xa inhibitory site","start":318,"end":348},{"id":"PF14670","name":"Coagulation Factor Xa inhibitory site","start":673,"end":711}],"gene3D":[{"start":66,"end":104,"id":"4.10.400.10","name":"Low-density Lipoprotein Receptor"},{"start":234,"end":273,"id":"4.10.400.10","name":"Low-density Lipoprotein Receptor"},{"start":399,"end":659,"id":"2.120.10.30","name":"TolB, C-terminal domain"},{"start":274,"end":308,"id":"4.10.400.10","name":"Low-density Lipoprotein Receptor"},{"start":20,"end":65,"id":"4.10.400.10","name":"Low-density Lipoprotein Receptor"},{"start":192,"end":233,"id":"4.10.400.10","name":"Low-density Lipoprotein Receptor"},{"start":148,"end":186,"id":"4.10.400.10","name":"Low-density Lipoprotein Receptor"},{"start":660,"end":713,"id":"2.10.25.10","name":"Laminin"},{"start":354,"end":398,"id":"2.10.25.10","name":"Laminin"},{"start":118,"end":147,"id":"4.10.1220.10","name":"EGF-type module"},{"start":311,"end":353,"id":"2.10.25.10","name":"Laminin"}]},"uniref50":"UniRef50_P01130","sequence":"MGPWGWKLRWTVALLLAAAGTAVGDRCERNEFQCQDGKCISYKWVCDGSAECQDGSDESQETCLSVTCKSGDFSCGGRVNRCIPQFWRCDGQVDCDNGSDEQGCPPKTCSQDEFRCHDGKCISRQFVCDSDRDCLDGSDEASCPVLTCGPASFQCNSSTCIPQLWACDNDPDCEDGSDEWPQRCRGLYVFQGDSSPCSAFEFHCLSGECIHSSWRCDGGPDCKDKSDEENCAVATCRPDEFQCSDGNCIHGSRQCDREYDCKDMSDEVGCVNVTLCEGPNKFKCHSGECITLDKVCNMARDCRDWSDEPIKECGTNECLDNNGGCSHVCNDLKIGYECLCPDGFQLVAQRRCEDIDECQDPDTCSQLCVNLEGGYKCQCEEGFQLDPHTKACKAVGSIAYLFFTNRHEVRKMTLDRSEYTSLIPNLRNVVALDTEVASNRIYWSDLSQRMICSTQLDRAHGVSSYDTVISRDIQAPDGLAVDWIHSNIYWTDSVLGTVSVADTKGVKRKTLFRENGSKPRAIVVDPVHGFMYWTDWGTPAKIKKGGLNGVDIYSLVTENIQWPNGITLDLLSGRLYWVDSKLHSISSIDVNGGNRKTILEDEKRLAHPFSLAVFEDKVFWTDIINEAIFSANRLTGSDVNLLAENLLSPEDMVLFHNLTQPRGVNWCERTTLSNGGCQYLCLPAPQINPHSPKFTCACPDGMLLARDMRSCLTEAEAAVATQETSTVRLKVSSTAVRTQHTTTRPVPDTSRLPGATPGLTTVEIVTMSHQALGDVAGRGNEKKPSSVRALSIVLPIVLLVFLCLGVFLLWKNWRLKNINSINFDNPVYQKTTEDEVHICHNQDGYSYPSRQMVSLEDDVA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P01130","disprot_id":"DP01396","ncbi_taxon_id":9606,"regions_counter":4,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":175,"region_id":"DP01396r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The structure, dynamics, and binding of the LA45 module pair of the low-density lipoprotein receptor suggest an important role for LA4 in ligand release. <i> Guttman M, Komives EA. </i> Biochemistry, 2011","statement":[{"text":"The 12 residue linker connecting the modules, though slightly structured through an interaction with LA4, is highly flexible.","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":163,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22091758","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2LGP"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":175,"term_name":"flexible linker","start":163,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Across species, evolution has conserved the length (12–14 residues) of the linker between LA4 and LA5 without conservation of any specific residues, which is typically seen for flexible linkers.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22091758","version":3,"reference_html":"The structure, dynamics, and binding of the LA45 module pair of the low-density lipoprotein receptor suggest an important role for LA4 in ligand release. <i> Guttman M, Komives EA. </i> Biochemistry, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006165","region_id":"DP01396r002","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":175,"term_name":"molecular adaptor activity","start":163,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Truncation of this linker significantly alters the interaction with LDL particles hinting that it may be required for the two modules to access distant epitopes on ligands such as multiple copies of ApoE on a lipoprotein surface.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"22091758","version":3,"reference_html":"The structure, dynamics, and binding of the LA45 module pair of the low-density lipoprotein receptor suggest an important role for LA4 in ligand release. <i> Guttman M, Komives EA. </i> Biochemistry, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0060090","ec_id":"ECO:0006165","region_id":"DP01396r003","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":393,"region_id":"DP01396r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural and biochemical characterization of the wild type PCSK9-EGF(AB) complex and natural familial hypercholesterolemia mutants. <i> Bottomley MJ, Cirillo A, Orsatti L, Ruggeri L, Fisher TS, Santoro JC, Cummings RT, Cubbon RM, Lo Surdo P, Calzetta A, Noto A, Baysarowich J, Mattu M, Talamo F, De Francesco R, Sparrow CP, Sitlani A, Carfí A. </i> J Biol Chem, 2009","statement":[{"text":"No interpretable electron density was observed for the EGF(B) domain, suggesting that it is disordered in the crystals","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":354,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19001363","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2W2Q"},{"db":"PDB","id":"2W2P"},{"db":"PDB","id":"2W2O"},{"db":"PDB","id":"2W2N"},{"db":"PDB","id":"2W2M"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P01130","date":"2018-07-16T12:34:41.000Z","acc":"P01130","name":"Low-density lipoprotein receptor","length":860,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000015DF","genes":[{"name":{"value":"LDLR"}}],"alphafold_very_low_content":0.15465116279069768,"disorder_content":0.06162790697674419,"disprot_consensus":{"full":[{"start":163,"end":175,"type":"D"},{"start":354,"end":393,"type":"D"}],"Structural state":[{"start":163,"end":175,"type":"D"},{"start":354,"end":393,"type":"D"}],"Disorder function":[{"start":163,"end":175,"type":"F"}],"Molecular function":[{"start":163,"end":175,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05076","name":"Suppressor of fused protein (SUFU)","start":64,"end":240},{"id":"PF12470","name":"Suppressor of Fused Gli/Ci N terminal binding domain","start":253,"end":473}],"gene3D":[{"start":355,"end":484,"id":"3.30.1360.230","name":"Sufu, C-terminal domain"}]},"uniref50":"UniRef50_Q9Z0P7","sequence":"MAELRPSVAPGPAAPPASGPSAPPAFASLFPPGLHAIYGECRRLYPDQPNPLQVTAIVKYWLGGPDPLDYVSMYRNMGSPSANIPEHWHYISFGLSDLYGDNRVHEFTGTDGPSGFGFELTFRLKRETGESAPPTWPAELMQGLARYVFQSENTFCSGDHVSWHSPLDNSESRIQHMLLTEDPQMQPVRTPFGVVTFLQIVGVCTEELHSAQQWNGQGILELLRTVPIAGGPWLITDMRRGETIFEIDPHLQERVDKGIETDGSNLSGVSAKCAWDDLSRPPEDEEDSRSICLGTQPRRLSGKDTEQIRETLRRGLEINSKPVLPPINSQRQNGLTHDRAPSRKDSLGSDSSTAIIPHELIRTRQLESVHLKFNQESGALIPLCLRGRLLHGRHFTYKSITGDMAITFVSTGVEGAFATEEHPYAAHGPWLQILLTEEFVEKMLEDLEDLTSPEEFKLPKEYSWPEKKLKVSILPDVVFDSPLH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q9Z0P7","disprot_id":"DP01397","ncbi_taxon_id":10090,"regions_counter":1,"creator":"jlamb","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":359,"region_id":"DP01397r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis of SUFU-GLI interaction in human Hedgehog signalling regulation. <i> Cherry AL, Finta C, Karlström M, Jin Q, Schwend T, Astorga-Wells J, Zubarev RA, Del Campo M, Criswell AR, de Sanctis D, Jovine L, Toftgård R. </i> Acta Crystallogr D Biol Crystallogr, 2013","statement":[{"text":"3.2. SUFU contains an intrinsically disordered region","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jlamb","start":279,"term_ontology":"IDPO","curator_name":"John Lamb","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0568-8281","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24311597","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9Z0P7","date":"2018-07-16T13:05:43.000Z","acc":"Q9Z0P7","name":"Suppressor of fused homolog","length":484,"organism":"Mus musculus","dataset":[],"UniParc":"UPI000005FB6A","genes":[{"name":{"value":"Sufu","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"23034632","url":"http://www.ncbi.nlm.nih.gov/pubmed/23034632","alternativeUrl":"https://europepmc.org/abstract/MED/23034632"}},{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:1345643","url":"http://www.informatics.jax.org/marker/MGI:1345643"}}]}}],"alphafold_very_low_content":0.17768595041322313,"disorder_content":0.16735537190082644,"disprot_consensus":{"full":[{"start":279,"end":359,"type":"D"}],"Structural state":[{"start":279,"end":359,"type":"D"}]}},{"features":{"pfam":[{"id":"PF19026","name":"HYPK UBA domain","start":82,"end":122}]},"uniref50":"UniRef50_K1XJR2","sequence":"MAAEDRQPADIVEGATAGDVEEEVAPAAKSAEDRKAAAALSKLDAHADEDMAPAREVDQEAVKNAMSALSGASTEKKEVKKVKVDPADVNLLVEELELSKAKATELLKAHDGDAIKAMKAYIQPAF","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Sordariomycetidae","Sordariales","Chaetomiaceae","Chaetomium"],"uniref90":"UniRef90_G0SCY6","disprot_id":"DP01398","ncbi_taxon_id":759272,"regions_counter":3,"creator":"jmanso","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":25,"region_id":"DP01398r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis of HypK regulating N-terminal acetylation by the NatA complex. <i> Weyer FA, Gumiero A, Lapouge K, Bange G, Kopp J, Sinning I. </i> Nat Commun, 2017","statement":[{"text":"Only small parts of the structure are disordered. HypK: residues 1–25, 43–56","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jmanso","start":1,"term_ontology":"IDPO","curator_name":"Jose A Manso","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5NNR"}],"reference_id":"28585574","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":25,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural basis of HypK regulating N-terminal acetylation by the NatA complex. <i> Weyer FA, Gumiero A, Lapouge K, Bange G, Kopp J, Sinning I. </i> Nat Commun, 2017","statement":[{"text":"Our study also shows that the regulatory function of HypK resides in its N-terminal region comprising the first 50 residues (disordered N terminus and helix α1), which bind at the entrance of the Naa10 active site and seem to block access to the active site.","type":"Discussion"}],"term_id":"GO:0005515","curator_id":"jmanso","start":1,"term_ontology":"GO","curator_name":"Jose A Manso","reference_id":"28585574","version":3,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01398r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":56,"region_id":"DP01398r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis of HypK regulating N-terminal acetylation by the NatA complex. <i> Weyer FA, Gumiero A, Lapouge K, Bange G, Kopp J, Sinning I. </i> Nat Commun, 2017","term_id":"IDPO:0000002","curator_id":"jmanso","start":43,"term_ontology":"IDPO","curator_name":"Jose A Manso","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5NNR"}],"reference_id":"28585574","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_G0SCY6","date":"2018-07-16T13:15:32.000Z","acc":"G0SCY6","name":"Uncharacterized protein","length":126,"organism":"Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)","dataset":[],"UniParc":"UPI0002280524","genes":[{"orfNames":[{"value":"CTHT_0058830","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EGS19257.1","url":"https://www.ebi.ac.uk/ena/browser/view/EGS19257.1"}}]}]}],"alphafold_very_low_content":0.10317460317460317,"disorder_content":0.30952380952380953,"disprot_consensus":{"full":[{"start":1,"end":25,"type":"D"},{"start":43,"end":56,"type":"D"}],"Structural state":[{"start":1,"end":25,"type":"D"},{"start":43,"end":56,"type":"D"}],"Molecular function":[{"start":1,"end":25,"type":"F"}]}},{"features":{"pfam":[{"id":"PF12569","name":"N-terminal acetyltransferase A, auxiliary subunit","start":184,"end":698},{"id":"PF13432","name":"Tetratricopeptide repeat","start":19,"end":75},{"id":"PF13432","name":"Tetratricopeptide repeat","start":85,"end":128}],"gene3D":[{"start":501,"end":727,"id":"1.25.40.1010","name":"1.25.40.1010"},{"start":2,"end":499,"id":"1.25.40.1040","name":"1.25.40.1040"}]},"uniref50":"UniRef50_G3J5S8","sequence":"MPQPLSTREANLFRTVIRHYEDKQYKRGLKAAEQILKKNPKHGDTMSMKALILNAQGKTEEAFALAKEALTIDMKSYICWHVYGILYRTNKNFDEAIKAYKFALKLEPESHQIQRDLAVLQIQMRDYAGYVQSRLNMLKARPQIRQNWTALAIAYHLEGNLEKAEHILTTYEKSLTTPPPKTDLEHSEALLYKNTIIAERGDIERALQHLETDCKHCLDRLAVMELRASYLSKLARKDEAAKAYRALLDRNPEHMDYYKGLISALDISADDEEAQKAVYDEYAAKYPRSDAAKRLPLNFLSGERFRTTAKAYLTLMFDKGVPSTFANLKHLYSDSFKKETLASLAEEYLNEYVNARPSDNQADGDGSKGKGAALYYLAQHYNYYMSRDLTRALEYVEKAIELDPKNVDFHMTKARIFKHQGDLAKAAETMDYARSLDPKDRYINSKAAKYQLRNNENEKALATMGLFTRAETAGGPLADLTDMQCIWFLTEDGEAWQRRGNTALALKRYHTVFSIFDTWQEDQFDFHSFSLRKGQIRAYVDMVRWEDRLREHPFYFRAALDAVNLYLSMYDKPQSANGANGTEAANPNGEDAAEKKKAAKKARKEAQKAEREAAERAAKQDPNKPGAQKGKEEDIKKKDDDPNGEKLAATKDPLGDAMKFLNYILQFSPKNIDGQIAGFEVYIRKKKYLLALRCLKAASAIDKNHPNVLEQAAKLRKIVSSALGSMAPKLREVIQAELVGVPGA","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Sordariomycetidae","Sordariales","Chaetomiaceae","Chaetomium"],"uniref90":"UniRef90_G0S4M4","disprot_id":"DP01399","ncbi_taxon_id":759272,"regions_counter":1,"creator":"jmanso","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":637,"region_id":"DP01399r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis of HypK regulating N-terminal acetylation by the NatA complex. <i> Weyer FA, Gumiero A, Lapouge K, Bange G, Kopp J, Sinning I. </i> Nat Commun, 2017","statement":[{"text":"Small parts of the structure are disordered: the lysine-rich region (charged helix) 573–637.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jmanso","start":573,"term_ontology":"IDPO","curator_name":"Jose A Manso","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5NNP"}],"reference_id":"28585574","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_G0S4M4","date":"2018-07-16T13:26:48.000Z","acc":"G0S4M4","name":"N-terminal acetyltransferase-like protein","length":744,"organism":"Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)","dataset":[],"UniParc":"UPI000227ED51","genes":[{"orfNames":[{"value":"CTHT_0031530","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EGS21299.1","url":"https://www.ebi.ac.uk/ena/browser/view/EGS21299.1"}}]}]}],"alphafold_very_low_content":0.06182795698924731,"disorder_content":0.08736559139784947,"disprot_consensus":{"full":[{"start":573,"end":637,"type":"D"}],"Structural state":[{"start":573,"end":637,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":104,"end":367}],"gene3D":[{"start":79,"end":181,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":182,"end":389,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"}]},"uniref50":"UniRef50_P45985","sequence":"MAAPSPSGGGGSGGGSGSGTPGPVGSPAPGHPAVSSMQGKRKALKLNFANPPFKSTARFTLNPNPTGVQNPHIERLRTHSIESSGKLKISPEQHWDFTAEDLKDLGEIGRGAYGSVNKMVHKPSGQIMAVKRIRSTVDEKEQKQLLMDLDVVMRSSDCPYIVQFYGALFREGDCWICMELMSTSFDKFYKYVYSVLDDVIPEEILGKITLATVKALNHLKENLKIIHRDIKPSNILLDRSGNIKLCDFGISGQLVDSIAKTRDAGCRPYMAPERIDPSASRQGYDVRSDVWSLGITLYELATGRFPYPKWNSVFDQLTQVVKGDPPQLSNSEEREFSPSFINFVNLCLTKDESKRPKYKELLKHPFILMYEERAVEVACYVCKILDQMPATPSSPMYVD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P45985","disprot_id":"DP01400","ncbi_taxon_id":9606,"regions_counter":9,"creator":"jpujols","regions":[{"term_namespace":"Molecular function","ec_ontology":"ECO","end":62,"term_name":"mitogen-activated protein kinase p38 binding","released":"2025_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Deciphering the Dynamic Interaction Profile of an Intrinsically Disordered Protein by NMR Exchange Spectroscopy. <i> Delaforge E, Kragelj J, Tengo L, Palencia A, Milles S, Bouvignies G, Salvi N, Blackledge M, Jensen MR. </i> J Am Chem Soc, 2018","statement":[{"text":"Large increases in the 15N R2 rates are observed even for small molar ratios of p38α for all residues of the docking site motif and the KIS domain, as well as for residues immediately adjacent to these regions. These results confirm the extended nature of the MKK4 interaction site with p38α.","type":"Results"}],"term_id":"GO:0048273","curator_id":"vnugnes","start":49,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"29276882","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2025-11-25T14:40:39.192Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01400r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to mitogen-activated protein kinase p38, an enzyme that catalyzes the transfer of phosphate from ATP to hydroxyl side chains on proteins in response to mitogen activation.\" [GOC:curators, PMID:17827184]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q16539","operator":null,"partner_start":null,"partner_end":null}],"cross_refs":[{"db":"ELM","id":"DOC_MAPK_MEF2A_6"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":86,"region_id":"DP01400r003","released":"2025_12","ec_id":"ECO:0006165","reference_html":"Deciphering the Dynamic Interaction Profile of an Intrinsically Disordered Protein by NMR Exchange Spectroscopy. <i> Delaforge E, Kragelj J, Tengo L, Palencia A, Milles S, Bouvignies G, Salvi N, Blackledge M, Jensen MR. </i> J Am Chem Soc, 2018","statement":[{"text":"The secondary 13Cα chemical shifts show that this domain is devoid of transiently populated secondary structures (Figure 2C). Nuclear relaxation rates can be used to probe the dynamics of IDPs on the pico- to nanosecond time scale including correlated motions.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2025-11-25T14:30:23.965Z","reference_source":"pmid","term_name":"disorder","reference_id":"29276882","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":12,"end":86,"reference_id":"34439869","reference_source":"pmid","reference_html":"Enthalpy-Entropy Compensation in the Promiscuous Interaction of an Intrinsically Disordered Protein with Homologous Protein Partners. <i> Kragelj J, Orand T, Delaforge E, Tengo L, Blackledge M, Palencia A, Jensen MR. </i> Biomolecules, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01400r004","statement":[{"text":"Line broadening is observed for multiple residues upon addition of JNK1 demonstrating a clear interaction, while chemical shift changes are negligible (Figure 1). We quantified the intensities of the resonances as a function of the molar ratio of JNK1 showing that the interacting region extends over a large part of the MKK4 sequence with the docking site motif (40KRKALKLNF48) experiencing the most pronounced line broadening (Figure 2).","type":"Results"}],"interaction_partner":[{"db":"UniProt","id":"P45983","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-07T13:25:34.528Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":12,"end":86,"reference_id":"34439869","reference_source":"pmid","reference_html":"Enthalpy-Entropy Compensation in the Promiscuous Interaction of an Intrinsically Disordered Protein with Homologous Protein Partners. <i> Kragelj J, Orand T, Delaforge E, Tengo L, Blackledge M, Palencia A, Jensen MR. </i> Biomolecules, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01400r005","statement":[{"text":"We compared the thermodynamic profiles of the MKK4:JNK1 and MKK4:p38α complexes by using ITC (Figure 4). Both complexes show a 1:1 stoichiometry with the JNK1 complex displaying an approximately three times higher binding affinity (KD = 1.3 μM) than the p38α complex (KD = 4.1 μM).","type":"Results"},{"text":"This entry corresponds to the experimental evidences of two independent heterodimers MKK4:JNK1 and MKK4:p38α. Binding free energies reveal that JNK1 and p38α binding to MKK4 are governed by different thermodynamic contributions. p38α ruled by a clear entropic contribution, while the enthalpy compensates the lack of entropic contribution for the JNK1 interaction.","type":"Curator statement"}],"interaction_partner":[{"db":"UniProt","id":"P45983","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q16539","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-07T13:25:28.909Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":38,"end":49,"reference_id":"34439869","reference_source":"pmid","reference_html":"Enthalpy-Entropy Compensation in the Promiscuous Interaction of an Intrinsically Disordered Protein with Homologous Protein Partners. <i> Kragelj J, Orand T, Delaforge E, Tengo L, Blackledge M, Palencia A, Jensen MR. </i> Biomolecules, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01400r006","statement":[{"text":"The results show that MKK4 folds into two different conformations upon binding to JNK1 and p38α. While MKK4 shows poor helical propensity in complex with p38α, it folds into a helix encompassing residues K40-K45 upon binding to JNK1 (Figure 6a). We note that a conformational selection mechanism can be ruled out in the case of the JNK1 complex, as MKK4 does not show any helical propensity in its free state (Figure 6a) [35]. ","type":"Results"},{"text":"Despite prominent helix is comprised between residues 40 and 45, the region between residue 28 and 49 shows significant population of α-helix as calculated from the experimental chemical shifts.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-07T13:25:06.782Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":41,"end":48,"reference_id":"29276882","reference_source":"pmid","reference_html":"Deciphering the Dynamic Interaction Profile of an Intrinsically Disordered Protein by NMR Exchange Spectroscopy. <i> Delaforge E, Kragelj J, Tengo L, Palencia A, Milles S, Bouvignies G, Salvi N, Blackledge M, Jensen MR. </i> J Am Chem Soc, 2018","date":"2025-11-25T14:48:33.659Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0048273","term_name":"mitogen-activated protein kinase p38 binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"ELM","id":"DOC_MAPK_MEF2A_6"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q16539","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01400r008","statement":[{"text":"Addition of the canonical docking site peptide of MKK4 (residues 39–50) leads to CSPs primarily in three different regions of p38α involving residues 110–129, 160–164, and 304–320 that are all located at or in close proximity to the docking groove.","type":"Results"}],"term_comment":"","term_def":"\"Binding to mitogen-activated protein kinase p38, an enzyme that catalyzes the transfer of phosphate from ATP to hydroxyl side chains on proteins in response to mitogen activation.\" [GOC:curators, PMID:17827184]","term_is_obsolete":false,"term_not_annotate":false},{"start":40,"end":48,"reference_id":"34439869","reference_source":"pmid","reference_html":"Enthalpy-Entropy Compensation in the Promiscuous Interaction of an Intrinsically Disordered Protein with Homologous Protein Partners. <i> Kragelj J, Orand T, Delaforge E, Tengo L, Blackledge M, Palencia A, Jensen MR. </i> Biomolecules, 2021","date":"2025-11-25T15:42:46.039Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051019","term_name":"mitogen-activated protein kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"ELM","id":"DOC_MAPK_NFAT4_5"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P45983","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01400r009","statement":[{"text":"We quantified the intensities of the resonances as a function of the molar ratio of JNK1 showing that the interacting region extends over a large part of the MKK4 sequence with the docking site motif (40KRKALKLNF48) experiencing the most pronounced line broadening (Figure 2).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a mitogen-activated protein kinase.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_P45985","date":"2018-07-16T13:36:52.000Z","acc":"P45985","name":"Dual specificity mitogen-activated protein kinase kinase 4","length":399,"organism":"Homo sapiens","dataset":["Cancer-related proteins","Stress response proteins"],"UniParc":"UPI000012F48E","genes":[{"name":{"value":"MAP2K4"},"synonyms":[{"value":"JNKK1"},{"value":"MEK4"},{"value":"MKK4"},{"value":"PRKMK4"},{"value":"SEK1"},{"value":"SERK1"},{"value":"SKK1"}]}],"alphafold_very_low_content":0.21553884711779447,"disorder_content":0.21553884711779447,"disprot_consensus":{"full":[{"start":1,"end":37,"type":"D"},{"start":38,"end":49,"type":"T"},{"start":50,"end":86,"type":"D"}],"Structural state":[{"start":1,"end":86,"type":"D"}],"Molecular function":[{"start":12,"end":86,"type":"F"}],"Structural transition":[{"start":38,"end":49,"type":"T"}]}},{"features":{"pfam":[{"id":"PF01423","name":"LSM domain","start":4,"end":65}],"gene3D":[{"start":1,"end":109,"id":"2.30.30.100","name":"2.30.30.100"}]},"uniref50":"UniRef50_P47093","sequence":"MSATLKDYLNKRVVIIKVDGECLIASLNGFDKNTNLFITNVFNRISKEFICKAQLLRGSEIALVGLIDAENDDSLAPIDEKKVPMLKDTKNKIENEHVIWEKVYESKTK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P47093","disprot_id":"DP01401","ncbi_taxon_id":559292,"regions_counter":1,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":109,"region_id":"DP01401r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structures of the Lsm complex bound to the 3' end sequence of U6 small nuclear RNA. <i> Zhou L, Hang J, Zhou Y, Wan R, Lu G, Yin P, Yan C, Shi Y. </i> Nature, 2014","statement":[{"text":"For both the RNA-free and RNA-bound Lsm complexes, the following regions have no clear electron density and are absent in the final atomic models: residues 90–95 of Lsm2, residues 80–89 of Lsm3, residues 87–93 of Lsm4, residues 1–5 and 85–93 of Lsm5, residues 1–10 of Lsm6, residues 1–26 and 106–115 of Lsm7, residues 68–109 of Lsm8. These sequences are all located on the surface and presumably highly flexible.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":68,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24240276","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4M7A"},{"db":"PDB","id":"4M7D"},{"db":"PDB","id":"4M78"},{"db":"PDB","id":"4M77"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P47093","date":"2018-07-16T13:56:16.000Z","acc":"P47093","name":"U6 snRNA-associated Sm-like protein LSm8","length":109,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000013B61D","genes":[{"name":{"value":"LSM8"},"orfNames":[{"value":"J1464"},{"value":"YJR83.16"}],"olnNames":[{"value":"YJR022W"}]}],"alphafold_very_low_content":0.01834862385321101,"disorder_content":0.3853211009174312,"disprot_consensus":{"full":[{"start":68,"end":109,"type":"D"}],"Structural state":[{"start":68,"end":109,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01423","name":"LSM domain","start":15,"end":82}],"gene3D":[{"start":1,"end":86,"id":"2.30.30.100","name":"2.30.30.100"}]},"uniref50":"UniRef50_A6ZYX7","sequence":"MSGKASTEGSVTTEFLSDIIGKTVNVKLASGLLYSGRLESIDGFMNVALSSATEHYESNNNKLLNKFNSDVFLRGTQVMYISEQKI","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_A6ZYX7","disprot_id":"DP01402","ncbi_taxon_id":559292,"regions_counter":1,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":10,"region_id":"DP01402r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structures of the Lsm complex bound to the 3' end sequence of U6 small nuclear RNA. <i> Zhou L, Hang J, Zhou Y, Wan R, Lu G, Yin P, Yan C, Shi Y. </i> Nature, 2014","statement":[{"text":"For both the RNA-free and RNA-bound Lsm complexes, the following regions have no clear electron density and are absent in the final atomic models: residues 90–95 of Lsm2, residues 80–89 of Lsm3, residues 87–93 of Lsm4, residues 1–5 and 85–93 of Lsm5, residues 1–10 of Lsm6, residues 1–26 and 106–115 of Lsm7, residues 68–109 of Lsm8. These sequences are all located on the surface and presumably highly flexible.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24240276","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4M7A"},{"db":"PDB","id":"4M7D"},{"db":"PDB","id":"4M75"},{"db":"PDB","id":"4M78"},{"db":"PDB","id":"4M77"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_A6ZYX7","date":"2018-07-16T13:59:05.000Z","acc":"Q06406","name":"U6 snRNA-associated Sm-like protein LSm6","length":86,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI00000530D4","genes":[{"name":{"value":"LSM6"},"orfNames":[{"value":"D9481.18"}],"olnNames":[{"value":"YDR378C"}]}],"alphafold_very_low_content":0.023255813953488372,"disorder_content":0.11627906976744186,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00167","name":"Fibroblast growth factor","start":70,"end":195}],"gene3D":[{"start":53,"end":212,"id":"2.80.10.50","name":"2.80.10.50"}]},"uniref50":"UniRef50_P70377","sequence":"MAAAIASSLIRQKRQAREREKSNACKCVSSPSKGKTSCDKNKLNVFSRVKLFGSKKRRRRRPEPQLKGIVTKLYSRQGYHLQLQADGTIDGTKDEDSTYTLFNLIPVGLRVVAIQGVQTKLYLAMNSEGYLYTSELFTPECKFKESVFENYYVTYSSMIYRQQQSGRGWYLGLNKEGEIMKGNHVKKNKPAAHFLPKPLKVAMYKEPSLHDLTEFSRSGSGTPTKSRSVSGVLNGGKSMSHNEST","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P70377","disprot_id":"DP01404","ncbi_taxon_id":9606,"regions_counter":2,"creator":"maspromonte","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":237,"region_id":"DP01404r001","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Crystal structure of a fibroblast growth factor homologous factor (FHF) defines a conserved surface on FHFs for binding and modulation of voltage-gated sodium channels. <i> Goetz R, Dover K, Laezza F, Shtraizent N, Huang X, Tchetchik D, Eliseenkova AV, Xu CF, Neubert TA, Ornitz DM, Goldfarb M, Mohammadi M. </i> J Biol Chem, 2009","statement":[{"text":"After completion of diffraction data collection, the crystal was analyzed by mass spectrometry, which indicated that FHF2A residues 60–237 are within the boundaries of the crystallized FHF2A protein.","type":"Results"},{"text":"The final model for the FHF2A structure contains residues 64–212 of two FHF2A molecules; residues 60–63 at the N terminus and 213–237 at the C terminus are disordered in each of the two molecules.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"maspromonte","start":213,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2023-06-21T14:26:13.156Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3HBW"}],"reference_id":"19406745","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T14:33:46.375Z"}}],"released":"2018_11","uniref100":"UniRef100_Q92913","date":"2018-07-17T08:24:39.000Z","acc":"Q92913","name":"Fibroblast growth factor 13","length":245,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI00000359FC","genes":[{"name":{"value":"FGF13","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:3670","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:3670"}}]},"synonyms":[{"value":"FHF2"}]}],"alphafold_very_low_content":0.17551020408163265,"disorder_content":0.10204081632653061,"disprot_consensus":{"full":[{"start":213,"end":237,"type":"D"}],"Structural state":[{"start":213,"end":237,"type":"D"}]}},{"features":{"pfam":[{"id":"PF11430","name":"Programmed cell death activator EGL-1","start":67,"end":86}]},"uniref50":"UniRef50_O61667","sequence":"MLMLTFASTSSDLLPMSNVFDVQSSVFYNEKNMFYSSSQDFSSCEDSSQFADDSGFFDDSEISSIGYEIGSKLAAMCDDFDAQMMSYSAHASDRSLFHRLLDFFAF","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"uniref90":"UniRef90_O61667","disprot_id":"DP01407","ncbi_taxon_id":6239,"regions_counter":1,"creator":"achasapi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":106,"region_id":"DP01407r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural, biochemical, and functional analyses of CED-9 recognition by the proapoptotic proteins EGL-1 and CED-4. <i> Yan N, Gu L, Kokel D, Chai J, Li W, Han A, Chen L, Xue D, Shi Y. </i> Mol Cell, 2004","statement":[{"text":"The N-terminal 2 residues and the C-terminal 14 residues in EGL-1 have no electron density in the maps, and we presume that these regions are disordered in the crystals.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"achasapi","start":93,"term_ontology":"IDPO","curator_name":"Anastasia Chasapi","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-1986-5007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1TY4"}],"reference_id":"15383288","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_O61667","date":"2018-07-17T10:57:56.000Z","acc":"O61667","name":"Programmed cell death activator egl-1","length":106,"organism":"Caenorhabditis elegans","dataset":[],"UniParc":"UPI000007AC22","genes":[{"name":{"value":"egl-1","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAC39023.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAC39023.1"}},{"code":"ECO:0000312","source":{"name":"WormBase","id":"F23B12.9","url":"https://www.wormbase.org/db/seq/sequence?name=F23B12.9;class=Transcript"}}]},"orfNames":[{"value":"F23B12.9"}]}],"alphafold_very_low_content":0.32075471698113206,"disorder_content":0.1320754716981132,"disprot_consensus":{"full":[{"start":93,"end":106,"type":"D"}],"Structural state":[{"start":93,"end":106,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03234","name":"Cdc37 N terminal kinase binding","start":1,"end":109},{"id":"PF08564","name":"Cdc37 C terminal domain","start":292,"end":355},{"id":"PF08565","name":"Cdc37 Hsp90 binding domain","start":167,"end":269}],"gene3D":[{"start":148,"end":276,"id":"1.20.58.610","name":"Cdc37, Hsp90 binding domain"}]},"uniref50":"UniRef50_Q16543","sequence":"MVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECKRKVAECQRKLKELEVAEGGKAELERLQAEAQQLRKEERSWEQKLEEMRKKEKSMPWNVDTLSKDGFSKSMVNTKPEKTEEDSEEVREQKHKTFVEKYEKQIKHFGMLRRWDDSQKYLSDNVHLVCEETANYLVIWCIDLEVEEKCALMEQVAHQTIVMQFILELAKSLKVDPRACFRQFFTKIKTADRQYMEGFNDELEAFKERVRGRAKLRIEKAMKEYEEEERKKRLGPGGLDPVEVYESLPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKASEAKEGEEAGPGDPLLEAVPKTGDEKDVSV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q16543","disprot_id":"DP01420","ncbi_taxon_id":9606,"regions_counter":3,"creator":"achasapi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":25,"region_id":"DP01420r001","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Molecular Mechanism of Protein Kinase Recognition and Sorting by the Hsp90 Kinome-Specific Cochaperone Cdc37. <i> Keramisanou D, Aboalroub A, Zhang Z, Liu W, Marshall D, Diviney A, Larsen RW, Landgraf R, Gelis I. </i> Mol Cell, 2016","statement":[{"text":"N-Cdc37 secondary structure: straight and zigzag lines illustrate unstructured and helical regions, respectively.","type":"Figure"},{"text":"In summary, N-Cdc37 forms an independently folded domain that adopts a two-helix bundle conformation and displays differential dynamics containing long N- and C-terminal flexible tails.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-28T16:05:36.767Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2NCA"}],"reference_id":"27105117","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"GHMVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECKRKVAECQRKLKELEVAEGGKAELERLQAEAQQLRKEERSWEQKLEEMRKKEKSMPWNVDTLSKDGFSK"},{"region_id":"DP01420r002","ec_ontology":"ECO","end":126,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":112,"version":3,"statement":[{"text":"N-Cdc37 secondary structure: straight and zigzag lines illustrate unstructured and helical regions, respectively.","type":"Figure"},{"text":"In summary, N-Cdc37 forms an independently folded domain that adopts a two-helix bundle conformation and displays differential dynamics containing long N- and C-terminal flexible tails","type":"Results"}],"term_name":"disorder","reference_html":"Molecular Mechanism of Protein Kinase Recognition and Sorting by the Hsp90 Kinome-Specific Cochaperone Cdc37. <i> Keramisanou D, Aboalroub A, Zhang Z, Liu W, Marshall D, Diviney A, Larsen RW, Landgraf R, Gelis I. </i> Mol Cell, 2016","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27105117","date":"2023-08-28T16:05:05.368Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2NCA"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"GHMVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECKRKVAECQRKLKELEVAEGGKAELERLQAEAQQLRKEERSWEQKLEEMRKKEKSMPWNVDTLSKDGFSK"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":378,"region_id":"DP01420r003","released":"2024_12","ec_id":"ECO:0006165","reference_html":"The C-terminal domain of human Cdc37 studied by solution NMR. <i> Zhang Z, Keramisanou D, Dudhat A, Paré M, Gelis I. </i> J Biomol NMR, 2015","statement":[{"text":"On the other hand, residues in the segment 345–378 exhibit low (<0.3) or even negative values suggesting that this is an inherently flexible region, where ps–ns dynamics are operative and ample backbone conformational heterogeneity is present","type":"Results"},{"text":"In contrast, for the 35 C-terminal residues that are predicted disordered and have low {1H}–15N NOEs, this drops to 2.9 s−1.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":344,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-12-04T18:46:12.752Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2N5X"}],"reference_id":"26400850","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q16543","date":"2018-07-17T11:00:40.000Z","acc":"Q16543","name":"Hsp90 co-chaperone Cdc37","length":378,"organism":"Homo sapiens","dataset":["Age-related disorders proteins"],"UniParc":"UPI000012723D","genes":[{"name":{"value":"CDC37"},"synonyms":[{"value":"CDC37A"}]}],"alphafold_very_low_content":0.09523809523809523,"disorder_content":0.1984126984126984,"disprot_consensus":{"full":[{"start":1,"end":25,"type":"D"},{"start":112,"end":126,"type":"D"},{"start":344,"end":378,"type":"D"}],"Structural state":[{"start":1,"end":25,"type":"D"},{"start":112,"end":126,"type":"D"},{"start":344,"end":378,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00246","name":"Zinc carboxypeptidase","start":129,"end":409},{"id":"PF02244","name":"Carboxypeptidase activation peptide","start":30,"end":105}],"gene3D":[{"start":23,"end":114,"id":"3.30.70.340","name":"Metallocarboxypeptidase-like"},{"start":115,"end":423,"id":"3.40.630.10","name":"Zn peptidases"}]},"uniref50":"UniRef50_Q96IY4","sequence":"MKLYSLGVLVATVLFCGEHAFAFQRGQVLSALPRTSRQVQILQNVTTTYKIVLWQPVAAEYIVKGYEVHFFVNASDVSNVKAHLNASRIPFRVLVENVEDLIRQQTSNDTISPRASSSYYEQYHSLNEIYSWIEVMTERYPDMVEKIHIGSSYEKYPLYVLKVSKKEQRAKNAMWIDCGIHAREWISPAFCLWFVGSVTYYYGKEKMHTNLLKHMDFYIMPVVNVDGYDYTWKKDRMWRKNRSLHEKNACVGTDLNRNFASKHWCGEGASSSSCSEIYCGTYPESEPEVKAVADFLRRNIKHIKAYISMHSYSQKIVFPYSYSRSRSKDHEELSLVAREAVFAMENIHRNIRYTHGSGSESLYLAPGGSDDWIYDLGIKYSFTFELRDKGKYGFLLPESYIRPTCSEALVAVAKIASHVVKNV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_Q2KIG3","disprot_id":"DP01424","ncbi_taxon_id":9913,"regions_counter":1,"creator":"achasapi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":117,"region_id":"DP01424r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Flexibility of the thrombin-activatable fibrinolysis inhibitor pro-domain enables productive binding of protein substrates. <i> Valnickova Z, Sanglas L, Arolas JL, Petersen SV, Schar C, Otzen D, Aviles FX, Gomis-Rüth FX, Enghild JJ. </i> J Biol Chem, 2010","term_id":"IDPO:0000002","curator_id":"ahatos","start":1,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3OSL"}],"reference_id":"20880845","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q2KIG3","date":"2018-07-17T11:01:32.000Z","acc":"Q2KIG3","name":"Carboxypeptidase B2","length":423,"organism":"Bos taurus","dataset":[],"UniParc":"UPI00005BDD34","genes":[{"name":{"value":"CPB2"}}],"alphafold_very_low_content":0.04728132387706856,"disorder_content":0.2765957446808511,"disprot_consensus":{"full":[{"start":1,"end":117,"type":"D"}],"Structural state":[{"start":1,"end":117,"type":"D"}]}},{"acc":"Q15004","sequence":"MVRTKADSVPGTYRKVVAARAPRKVLGSSTSATNSTSVSSRKAENKYAGGNPVCVRPTPKWQKGIGEFFRLSPKDSEKENQIPEEAGSSGLGKAKRKACPLQPDHTNDEKE","alphafold_very_low_content":"0.10810810810810811","creator":"tszani","dataset":["Cancer-related proteins","NDDs-related proteins"],"date":"2018-07-17T11:47:08.000Z","disprot_id":"DP01425","features":{"pfam":[{"id":"PF15715","name":"PCNA-associated factor histone like domain","start":1,"end":109}]},"genes":[{"name":{"value":"PCLAF","evidences":[{"source":{"id":"HGNC:28961","name":"HGNC","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:28961","_id":"685af523b4ac24d5329d909e"},"code":"ECO:0000312","_id":"685af523b4ac24d5329d909d"}],"_id":"685af523b4ac24d5329d909f"},"synonyms":[{"value":"KIAA0101","evidences":[],"_id":"685af523b4ac24d5329d90a0"},{"value":"NS5ATP9","evidences":[],"_id":"685af523b4ac24d5329d90a1"},{"value":"PAF","evidences":[],"_id":"685af523b4ac24d5329d90a2"}],"olnNames":[],"orfNames":[{"value":"L5","evidences":[],"_id":"685af523b4ac24d5329d90a3"}],"_id":"685af523b4ac24d5329d909c"}],"length":111,"name":"PCNA-associated factor","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":17,"released":"2018_11","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI000003ABC6","uniref100":"UniRef100_Q15004","uniref50":"UniRef50_Q15004","uniref90":"UniRef90_Q15004","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"19332","_id":"685af523b4ac24d5329d905e"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":111,"interaction_partner":[],"reference_html":"p15PAF is an intrinsically disordered protein with nonrandom structural preferences at sites of interaction with other proteins. <i> De Biasio A, Ibáñez de Opakua A, Cordeiro TN, Cordeiro TN, Villate M, Merino N, Sibille N, Lelli M, Diercks T, Bernadó P, Blanco FJ. </i> Biophys J, 2014","reference_id":"24559989","region_id":"DP01425r001","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"We present to our knowledge the first structural characterization of the proliferating-cell-nuclear-antigen-associated factor p15(PAF), showing that it is monomeric and intrinsically disordered in solution but has nonrandom conformational preferences at sites of protein-protein interactions.","_id":"685af523b4ac24d5329d905b"},{"type":"Results","text":"The lack of dispersion in the backbone amide 1H chemical shifts as seen in the 1H-15N HSQC spectrum gives evidence of the largely disordered and flexible nature of p15PAF under native conditions.","_id":"685af523b4ac24d5329d905c"},{"type":"Results","text":"1H-15N RDCs of p15PAF measured in a stretched polyacrylamide gel aligning medium are mainly negative (Fig. 4, black circles), as observed in disordered proteins (16,47).","_id":"685af523b4ac24d5329d905d"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T14:52:19.941Z","_id":"685af523b4ac24d5329d905f"},"version":3,"_id":"685af523b4ac24d5329d905a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":111,"interaction_partner":[],"reference_html":"p15PAF is an intrinsically disordered protein with nonrandom structural preferences at sites of interaction with other proteins. <i> De Biasio A, Ibáñez de Opakua A, Cordeiro TN, Cordeiro TN, Villate M, Merino N, Sibille N, Lelli M, Diercks T, Bernadó P, Blanco FJ. </i> Biophys J, 2014","reference_id":"24559989","region_id":"DP01425r002","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"We present to our knowledge the first structural characterization of the proliferating-cell-nuclear-antigen-associated factor p15(PAF), showing that it is monomeric and intrinsically disordered in solution but has nonrandom conformational preferences at sites of protein-protein interactions.","_id":"685af523b4ac24d5329d9061"},{"type":"Results","text":"The far-UV CD spectrum of p15PAF shows a minimum at 198 nm and a shoulder at 222 nm, consistent with a predominantly random-coil protein with little secondary structure (Fig. 2 B). The thermal denaturation curve of p15PAF followed by the changes in the CD signal at 222 nm (see Fig. 2 B, inset) does not show any cooperative folding-unfolding transition, indicating that p15PAF lacks a defined tertiary structure.","_id":"685af523b4ac24d5329d9062"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T11:37:30.106Z","_id":"685af523b4ac24d5329d9063"},"version":3,"_id":"685af523b4ac24d5329d9060","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":111,"interaction_partner":[],"reference_html":"p15PAF is an intrinsically disordered protein with nonrandom structural preferences at sites of interaction with other proteins. <i> De Biasio A, Ibáñez de Opakua A, Cordeiro TN, Cordeiro TN, Villate M, Merino N, Sibille N, Lelli M, Diercks T, Bernadó P, Blanco FJ. </i> Biophys J, 2014","reference_id":"24559989","region_id":"DP01425r006","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"We present to our knowledge the first structural characterization of the proliferating-cell-nuclear-antigen-associated factor p15(PAF), showing that it is monomeric and intrinsically disordered in solution but has nonrandom conformational preferences at sites of protein-protein interactions.","_id":"685af523b4ac24d5329d906c"},{"type":"Results","text":"We used SAXS to characterize the conformational space sampled by p15PAF in solution and to validate the structure ensemble derived from the RDC data. As shown in Fig. 5, the SAXS profile of p15PAF and its Kratky representation are typical for a disordered protein. The SAXS curve shows no features (Fig. 5 A) and the Kratky plot does not show a maximum, with a monotonic increase at large momentum transfer values (Fig. 5 B).","_id":"685af523b4ac24d5329d906d"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T11:36:58.557Z","_id":"685af523b4ac24d5329d906e"},"version":1,"_id":"685af523b4ac24d5329d906b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007064","ec_name":"dynamic light scattering assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":111,"interaction_partner":[],"reference_html":"p15PAF is an intrinsically disordered protein with nonrandom structural preferences at sites of interaction with other proteins. <i> De Biasio A, Ibáñez de Opakua A, Cordeiro TN, Cordeiro TN, Villate M, Merino N, Sibille N, Lelli M, Diercks T, Bernadó P, Blanco FJ. </i> Biophys J, 2014","reference_id":"24559989","region_id":"DP01425r007","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"We present to our knowledge the first structural characterization of the proliferating-cell-nuclear-antigen-associated factor p15(PAF), showing that it is monomeric and intrinsically disordered in solution but has nonrandom conformational preferences at sites of protein-protein interactions.","_id":"685af523b4ac24d5329d9070"},{"type":"Results","text":"The protein eluted from the SEC column at a volume that, according to the calibration with molecular weight standards, corresponds to an apparent molar mass of 25 kDa. However, the mass derived from the MALLS data is 11.5 kDa (Fig. 2 A), demonstrating that p15PAF is monomeric. These inconsistent results suggest that p15PAF is either folded with an elongated shape or is flexible and disordered (39). In both instances, it would elute at a smaller volume than a globular protein of the same mass.","_id":"685af523b4ac24d5329d9071"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T10:04:43.817Z","_id":"685af523b4ac24d5329d9072"},"version":1,"_id":"685af523b4ac24d5329d906f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":62,"end":69,"interaction_partner":[{"db":"UniProt","id":"P12004","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9074"}],"reference_html":"Structure of p15(PAF)-PCNA complex and implications for clamp sliding during DNA replication and repair. <i> De Biasio A, de Opakua AI, Mortuza GB, Molina R, Cordeiro TN, Castillo F, Villate M, Merino N, Delgado S, Gil-Cartón D, Luque I, Diercks T, Bernadó P, Montoya G, Blanco FJ. </i> Nat Commun, 2015","reference_id":"25762514","region_id":"DP01425r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As a disordered protein, p15 yields NMR spectra with sharp signals and poor dispersion in the proton frequency. On addition of excess PCNA, signal intensities decrease generally and most notably for the central residues V53-D75 that even disappear (Fig. 1d). This observation highlights the central region of p15 as the principal binding site for PCNA, which includes the PIP-box motif (62QKGIGEFF69, conserved residues underlined).","_id":"685af523b4ac24d5329d9075"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T14:52:33.171Z","_id":"685af523b4ac24d5329d9076"},"version":1,"_id":"685af523b4ac24d5329d9073","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005647","ec_name":"isothermal titration calorimetry evidence used in manual assertion","ec_ontology":"ECO","start":50,"end":77,"interaction_partner":[{"db":"UniProt","id":"P12004","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9078"}],"reference_html":"Structure of p15(PAF)-PCNA complex and implications for clamp sliding during DNA replication and repair. <i> De Biasio A, de Opakua AI, Mortuza GB, Molina R, Cordeiro TN, Castillo F, Villate M, Merino N, Delgado S, Gil-Cartón D, Luque I, Diercks T, Bernadó P, Montoya G, Blanco FJ. </i> Nat Commun, 2015","reference_id":"25762514","region_id":"DP01425r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Isothermal titration calorimetry (ITC) measurements could be fitted very well to a model assuming independent p15 binding to equivalent sites in the PCNA trimer, with a dissociation constant of 1.1 μM at 25 °C (Fig. 1c).","_id":"685af523b4ac24d5329d9079"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T14:52:31.135Z","_id":"685af523b4ac24d5329d907a"},"version":1,"_id":"685af523b4ac24d5329d9077","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005647","ec_name":"isothermal titration calorimetry evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":31,"interaction_partner":[{"db":"UniProt","id":"P12004","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d907c"}],"reference_html":"Structure of p15(PAF)-PCNA complex and implications for clamp sliding during DNA replication and repair. <i> De Biasio A, de Opakua AI, Mortuza GB, Molina R, Cordeiro TN, Castillo F, Villate M, Merino N, Delgado S, Gil-Cartón D, Luque I, Diercks T, Bernadó P, Montoya G, Blanco FJ. </i> Nat Commun, 2015","reference_id":"25762514","region_id":"DP01425r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"All three p15 fragments bind PCNA, but with decreasing affinity (Supplementary Fig. 1 and Supplementary Table 1). The N-terminal deletion mutant binds PCNA with only slightly lower affinity than p15, implying that any transient interactions of the N-terminal V2-S31 residues stabilize the complex only marginally. The affinity of p1550–77, however, is reduced by a factor of 5 and the shortest core fragment p1559–70 even by a factor of 33. These results indicate that residues G50-T58 and/or L71-E77 strongly contribute to PCNA binding, which is further enhanced by residues A32-G49.","_id":"685af523b4ac24d5329d907d"},{"type":"Supplementary material","text":"Isothermal titration calorimetry measurements and analysis of p15 and fragments binding to PCNA in PBS, pH 7.0 at 35 °C.","_id":"685af523b4ac24d5329d907e"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T14:52:28.642Z","_id":"685af523b4ac24d5329d907f"},"version":1,"_id":"685af523b4ac24d5329d907b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"4D2G","_id":"685af523b4ac24d5329d9083"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":51,"end":71,"interaction_partner":[{"db":"UniProt","id":"P12004","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9081"}],"reference_html":"Structure of p15(PAF)-PCNA complex and implications for clamp sliding during DNA replication and repair. <i> De Biasio A, de Opakua AI, Mortuza GB, Molina R, Cordeiro TN, Castillo F, Villate M, Merino N, Delgado S, Gil-Cartón D, Luque I, Diercks T, Bernadó P, Montoya G, Blanco FJ. </i> Nat Commun, 2015","reference_id":"25762514","region_id":"DP01425r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Residues N51-L71 of p1550–77 are well defined in the crystal structure (Supplementary Fig. 6), although the side chains of N51, R70 and L71 could not be reliably modelled (Fig. 2b).","_id":"685af523b4ac24d5329d9082"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T14:52:26.348Z","_id":"685af523b4ac24d5329d9084"},"version":1,"_id":"685af523b4ac24d5329d9080","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006277","ec_name":"fluorescence polarization evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":31,"interaction_partner":[],"reference_html":"Structure of p15(PAF)-PCNA complex and implications for clamp sliding during DNA replication and repair. <i> De Biasio A, de Opakua AI, Mortuza GB, Molina R, Cordeiro TN, Castillo F, Villate M, Merino N, Delgado S, Gil-Cartón D, Luque I, Diercks T, Bernadó P, Montoya G, Blanco FJ. </i> Nat Commun, 2015","reference_id":"25762514","region_id":"DP01425r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The p15–DNA interaction is unspecific since any of the DNA molecules tested (single-stranded DNA, primed DNA and flapped DNA) are bound by p15 with similar affinity (Supplementary Fig. 11a). The binding isotherms could be fitted to a 1:1 interaction model, with apparent dissociation constants between 0.2 and 0.4 μM at 25 °C.","_id":"685af523b4ac24d5329d9086"},{"type":"Results","text":"The affinity of p15ΔN is reduced by two orders of magnitude, indicating that the basic N-terminal region of p15 contributes most to the DNA affinity (Fig. 5a).","_id":"685af523b4ac24d5329d9087"}],"states_connection":[],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_id":"GO:0003677","term_is_binding":true,"term_is_obsolete":false,"term_name":"DNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T14:52:23.104Z","_id":"685af523b4ac24d5329d9088"},"version":1,"_id":"685af523b4ac24d5329d9085","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006277","ec_name":"fluorescence polarization evidence used in manual assertion","ec_ontology":"ECO","start":50,"end":77,"interaction_partner":[],"reference_html":"Structure of p15(PAF)-PCNA complex and implications for clamp sliding during DNA replication and repair. <i> De Biasio A, de Opakua AI, Mortuza GB, Molina R, Cordeiro TN, Castillo F, Villate M, Merino N, Delgado S, Gil-Cartón D, Luque I, Diercks T, Bernadó P, Montoya G, Blanco FJ. </i> Nat Commun, 2015","reference_id":"25762514","region_id":"DP01425r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The p15–DNA interaction is unspecific since any of the DNA molecules tested (single-stranded DNA, primed DNA and flapped DNA) are bound by p15 with similar affinity (Supplementary Fig. 11a). The binding isotherms could be fitted to a 1:1 interaction model, with apparent dissociation constants between 0.2 and 0.4 μM at 25 °C.","_id":"685af523b4ac24d5329d908a"},{"type":"Results","text":"The central fragment p1550–77 binds DNA with even lower affinity, and no DNA binding was observed with the core PIP-box fragment p1559–70. When DNA was titrated with PCNA-bound p15, the increase in fluorescence polarization was larger (Fig. 5a), indicating that a ternary complex forms (since the larger the size of the complex the larger the polarization). The slightly reduced DNA affinity shows that PCNA interferes only weakly with p15 binding to DNA. Similarly, when DNA-bound p15 was titrated with PCNA (Fig. 5b) the PCNA affinity was comparable to that of isolated p15 (or p1550–77). Thus, a ternary p15–PCNA–DNA complex forms in solution in which the direct p15–PCNA and p15–DNA interactions are largely independent of each other.","_id":"685af523b4ac24d5329d908b"}],"states_connection":[],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_id":"GO:0003677","term_is_binding":true,"term_is_obsolete":false,"term_name":"DNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T14:52:21.996Z","_id":"685af523b4ac24d5329d908c"},"version":1,"_id":"685af523b4ac24d5329d9089","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-15T20:01:25.851Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006277","ec_name":"fluorescence polarization evidence used in manual assertion","ec_ontology":"ECO","start":50,"end":77,"interaction_partner":[{"db":"UniProt","id":"P12004","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d908f"}],"reference_html":"Structure of p15(PAF)-PCNA complex and implications for clamp sliding during DNA replication and repair. <i> De Biasio A, de Opakua AI, Mortuza GB, Molina R, Cordeiro TN, Castillo F, Villate M, Merino N, Delgado S, Gil-Cartón D, Luque I, Diercks T, Bernadó P, Montoya G, Blanco FJ. </i> Nat Commun, 2015","reference_id":"25762514","region_id":"DP01425r014","released":"2022_06","sample":[{"db":null,"deviation":null,"id":null,"statements":[],"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_id":"UO:0000023","unit_name":"µg","value":null,"_id":"685af523b4ac24d5329d9090"}],"statement":[{"type":"Results","text":"The central fragment p1550–77 binds DNA with even lower affinity, and no DNA binding was observed with the core PIP-box fragment p1559–70. When DNA was titrated with PCNA-bound p15, the increase in fluorescence polarization was larger (Fig. 5a), indicating that a ternary complex forms (since the larger the size of the complex the larger the polarization). The slightly reduced DNA affinity shows that PCNA interferes only weakly with p15 binding to DNA. Similarly, when DNA-bound p15 was titrated with PCNA (Fig. 5b) the PCNA affinity was comparable to that of isolated p15 (or p1550–77). Thus, a ternary p15–PCNA–DNA complex forms in solution in which the direct p15–PCNA and p15–DNA interactions are largely independent of each other.","_id":"685af523b4ac24d5329d908e"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":2,"_id":"685af523b4ac24d5329d908d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-15T20:00:59.387Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006277","ec_name":"fluorescence polarization evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":31,"interaction_partner":[{"db":"UniProt","id":"P12004","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9094"}],"reference_html":"Structure of p15(PAF)-PCNA complex and implications for clamp sliding during DNA replication and repair. <i> De Biasio A, de Opakua AI, Mortuza GB, Molina R, Cordeiro TN, Castillo F, Villate M, Merino N, Delgado S, Gil-Cartón D, Luque I, Diercks T, Bernadó P, Montoya G, Blanco FJ. </i> Nat Commun, 2015","reference_id":"25762514","region_id":"DP01425r015","released":"2022_06","sample":[{"db":null,"deviation":null,"id":null,"statements":[],"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_id":"UO:0000023","unit_name":"µg","value":null,"_id":"685af523b4ac24d5329d9095"}],"statement":[{"type":"Results","text":"The affinity of p15ΔN is reduced by two orders of magnitude, indicating that the basic N-terminal region of p15 contributes most to the DNA affinity (Fig. 5a).","_id":"685af523b4ac24d5329d9092"},{"type":"Results","text":"The central fragment p1550–77 binds DNA with even lower affinity, and no DNA binding was observed with the core PIP-box fragment p1559–70. When DNA was titrated with PCNA-bound p15, the increase in fluorescence polarization was larger (Fig. 5a), indicating that a ternary complex forms (since the larger the size of the complex the larger the polarization). The slightly reduced DNA affinity shows that PCNA interferes only weakly with p15 binding to DNA. Similarly, when DNA-bound p15 was titrated with PCNA (Fig. 5b) the PCNA affinity was comparable to that of isolated p15 (or p1550–77). Thus, a ternary p15–PCNA–DNA complex forms in solution in which the direct p15–PCNA and p15–DNA interactions are largely independent of each other.","_id":"685af523b4ac24d5329d9093"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":2,"_id":"685af523b4ac24d5329d9091","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":50,"end":77,"interaction_partner":[],"reference_html":"Structure of p15(PAF)-PCNA complex and implications for clamp sliding during DNA replication and repair. <i> De Biasio A, de Opakua AI, Mortuza GB, Molina R, Cordeiro TN, Castillo F, Villate M, Merino N, Delgado S, Gil-Cartón D, Luque I, Diercks T, Bernadó P, Montoya G, Blanco FJ. </i> Nat Commun, 2015","reference_id":"25762514","region_id":"DP01425r016","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The poor HN signal dispersion and only minor changes in Cα chemical shifts (Supplementary Fig. 13) indicate that p15 does not acquire a defined structure on binding to the DNA; rather, its backbone remains flexible and disordered. In the presence of PCNA, DNA-bound p15 shows a similar pattern of NMR signal attenuation as in the absence of DNA (Fig. 5c), in line with a ternary complex where the central region of p15 is tightly bound to PCNA.","_id":"685af523b4ac24d5329d9097"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T14:52:36.480Z","_id":"685af523b4ac24d5329d9098"},"version":1,"_id":"685af523b4ac24d5329d9096","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007044","ec_name":"transmission electron microscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":111,"interaction_partner":[],"reference_html":"Structure of p15(PAF)-PCNA complex and implications for clamp sliding during DNA replication and repair. <i> De Biasio A, de Opakua AI, Mortuza GB, Molina R, Cordeiro TN, Castillo F, Villate M, Merino N, Delgado S, Gil-Cartón D, Luque I, Diercks T, Bernadó P, Montoya G, Blanco FJ. </i> Nat Commun, 2015","reference_id":"25762514","region_id":"DP01425r017","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"For an experimental verification of this possibility, PCNA in the presence of p15, DNA or both was stained with uranyl acetate and observed by transmission electron microscopy (Fig. 6b). Two-dimensional analysis of single particle projections yielded class averages for top-, side-, and tilted-views of the PCNA ring, with a larger proportion of tilted-view classes for the ternary p15–DNA–PCNA complex (Supplementary Fig. 15). Most remarkably, many of the top- and tilted-views of the ternary complex show increased density within the PCNA ring compared to both binary mixtures (where only the p15–PCNA mixture, however, is expected to form a complex). The same result is obtained when the rotational power spectra of individual particles in the three data sets are calculated and classified (Supplementary Fig. 16). These observations indicate that p15-bound DNA in the ternary complex is (at least transiently) located within the PCNA ring.","_id":"685af523b4ac24d5329d909a"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T14:52:34.896Z","_id":"685af523b4ac24d5329d909b"},"version":1,"_id":"685af523b4ac24d5329d9099","reference_source":"pmid"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":111,"type":"D"}],"Structural state":[{"start":1,"end":111,"type":"D"}],"Molecular function":[{"start":1,"end":111,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01857","name":"Retinoblastoma-associated protein B domain","start":646,"end":765},{"id":"PF01858","name":"Retinoblastoma-associated protein A domain","start":373,"end":573},{"id":"PF08934","name":"Rb C-terminal domain","start":768,"end":925},{"id":"PF11934","name":"Domain of unknown function (DUF3452)","start":113,"end":226}],"gene3D":[{"start":371,"end":608,"id":"1.10.472.10","name":"Cyclin-like"},{"start":623,"end":787,"id":"1.10.472.10","name":"Cyclin-like"},{"start":52,"end":127,"id":"1.10.472.10","name":"Cyclin-like"},{"start":188,"end":338,"id":"1.10.472.140","name":"1.10.472.140"}]},"uniref50":"UniRef50_P06400","sequence":"MPPKTPRKTAATAAAAAAEPPAPPPPPPPEEDPEQDSGPEDLPLVRLEFEETEEPDFTALCQKLKIPDHVRERAWLTWEKVSSVDGVLGGYIQKKKELWGICIFIAAVDLDEMSFTFTELQKNIEISVHKFFNLLKEIDTSTKVDNAMSRLLKKYDVLFALFSKLERTCELIYLTQPSSSISTEINSALVLKVSWITFLLAKGEVLQMEDDLVISFQLMLCVLDYFIKLSPPMLLKEPYKTAVIPINGSPRTPRRGQNRSARIAKQLENDTRIIEVLCKEHECNIDEVKNVYFKNFIPFMNSLGLVTSNGLPEVENLSKRYEEIYLKNKDLDARLFLDHDKTLQTDSIDSFETQRTPRKSNLDEEVNVIPPHTPVRTVMNTIQQLMMILNSASDQPSENLISYFNNCTVNPKESILKRVKDIGYIFKEKFAKAVGQGCVEIGSQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYSRSTSQNLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKAEGNLTREMIKHLERCEHRIMESLAWLSDSPLFDLIKQSKDREGPTDHLESACPLNLPLQNNHTAADMYLSPVRSPKKKGSTTRVNSTANAETQATSAFQTQKPLKSTSLSLFYKKVYRLAYLRLNTLCERLLSEHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAVQETFKRVLIKEEEYDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHIPRSPYKFPSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGSNPPKPLKKLRFDIEGSDEADGSKHLPGESKFQQKLAEMTSTRTRMQKQKMNDSMDTSNKEEK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P06400","disprot_id":"DP01426","ncbi_taxon_id":9606,"regions_counter":22,"creator":"lchemes","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":93,"region_id":"DP01426r001","released":"2022_06","ec_id":"ECO:0006220","reference_html":"Crystal structure of the retinoblastoma protein N domain provides insight into tumor suppression, ligand interaction, and holoprotein architecture. <i> Hassler M, Singh S, Yue WW, Luczynski M, Lakbir R, Sanchez-Sanchez F, Bader T, Pearl LH, Mittnacht S. </i> Mol Cell, 2007","statement":[{"text":"Disordered loop in the RbN domain","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":84,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"17996702","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-06-15T19:30:48.520Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2QDJ"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":114,"end":114,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":149,"end":149,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":209,"end":209,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":220,"end":220,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":234,"end":234,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":301,"end":301,"position":"Specific residue"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":635,"region_id":"DP01426r002","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Structure of the retinoblastoma tumour-suppressor pocket domain bound to a peptide from HPV E7. <i> Lee JO, Russo AA, Pavletich NP. </i> Nature, 1998","statement":[{"text":"The spacer, which is the least conserved region of Rb (Fig. 1a), and is different in the related p107 and p130 pocket proteins, appears to be unstructured or loosely folded based on proteolytic digestion (data not shown).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"lchemes","start":590,"term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"9495340","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1GUX"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":635,"term_name":"flexible linker","start":590,"ec_name":"cleavage assay evidence used in manual assertion","statement":[{"text":"This is the spacer joining the A and B subdomains of RbAB (RbPL)","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"9495340","version":3,"reference_html":"Structure of the retinoblastoma tumour-suppressor pocket domain bound to a peptide from HPV E7. <i> Lee JO, Russo AA, Pavletich NP. </i> Nature, 1998","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0007691","region_id":"DP01426r003","curator_orcid":"0000-0003-0192-9906","ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":513,"region_id":"DP01426r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the retinoblastoma tumour-suppressor pocket domain bound to a peptide from HPV E7. <i> Lee JO, Russo AA, Pavletich NP. </i> Nature, 1998","statement":[{"text":"This is a Flexible region in the RbA subdomain that appears disordered in most RbAB structures","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"lchemes","start":500,"term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"9495340","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1GUX"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":370,"region_id":"DP01426r005","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Structures of inactive retinoblastoma protein reveal multiple mechanisms for cell cycle control. <i> Burke JR, Hura GL, Rubin SM. </i> Genes Dev, 2012","statement":[{"text":"The work provides evidence that phosphorylation of RbIDL produces a transition from unassociated to self-associated Rb: \"This analysis suggests an equilibrium between associated and dissociated RbN and pocket domains, in which phos- phorylation of RbIDL shifts the equilibrium toward the associated conformation. \"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"lchemes","start":346,"term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"22569856","version":2,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"undefined","id":"undefined"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":370,"term_name":"flexible linker","start":346,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","curator_id":"lchemes","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"22569856","version":3,"reference_html":"Structures of inactive retinoblastoma protein reveal multiple mechanisms for cell cycle control. <i> Burke JR, Hura GL, Rubin SM. </i> Genes Dev, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006210","region_id":"DP01426r006","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":370,"region_id":"DP01426r007","released":"2022_06","ec_id":"ECO:0006220","reference_html":"Structures of inactive retinoblastoma protein reveal multiple mechanisms for cell cycle control. <i> Burke JR, Hura GL, Rubin SM. </i> Genes Dev, 2012","statement":[{"text":"This region corresponds to the linker joining the RbN and RbAB domains. T373 phosphorylation induces conformational transitions in the linker region. The larger interface (2277 A ̊ 2 buried surface area) is formed between pocket subdomain A and RbN subdomain B and is mediated by T373 phosphorylation (Fig. 4B)","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":346,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"22569856","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-06-15T19:32:40.302Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4ELJ"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":373,"end":373,"position":"Specific residue"}]},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":370,"term_name":"flexible linker","start":346,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","statement":[{"text":"This is the RbIDL linker region joining the RbN and the RbAB domains (the two main structured domains in Rb).","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"22569856","version":3,"reference_html":"Structures of inactive retinoblastoma protein reveal multiple mechanisms for cell cycle control. <i> Burke JR, Hura GL, Rubin SM. </i> Genes Dev, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006220","region_id":"DP01426r008","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":370,"term_name":"protein binding","start":346,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","statement":[{"text":"373 phosphorylation induces interactions of RbIDL with the RbAB domain that also block E2F binding, favouring the autoinhibited conformation. \"\"","type":"Results"}],"curator_id":"lchemes","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"22569856","version":3,"reference_html":"Structures of inactive retinoblastoma protein reveal multiple mechanisms for cell cycle control. <i> Burke JR, Hura GL, Rubin SM. </i> Genes Dev, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP01426r009","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":370,"term_name":"order to disorder","start":346,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","statement":[{"text":"Here we observe that T356 phosphorylation disorders a helix in RbN.","type":"Results"}],"curator_id":"vnugnes","released":"2022_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"22569856","version":3,"reference_html":"Structures of inactive retinoblastoma protein reveal multiple mechanisms for cell cycle control. <i> Burke JR, Hura GL, Rubin SM. </i> Genes Dev, 2012","date":"2022-06-15T19:39:20.264Z","term_id":"IDPO:0000014","ec_id":"ECO:0006220","region_id":"DP01426r010","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural transition","construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":356,"end":356,"position":"Specific residue"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":370,"region_id":"DP01426r011","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Crystal structure of the retinoblastoma protein N domain provides insight into tumor suppression, ligand interaction, and holoprotein architecture. <i> Hassler M, Singh S, Yue WW, Luczynski M, Lakbir R, Sanchez-Sanchez F, Bader T, Pearl LH, Mittnacht S. </i> Mol Cell, 2007","statement":[{"text":"limited tryptic digestion of Rb residues 1-370 generated two fragments with approximate size of 24.7 and 10.9 kDa (Supplement; Fig S-1A). Mass spectrometry and N-terminal sequencing of these identified three polypeptides encompassing residues 46-251, 263-355 and 266-355 (not shown), indicating trimming from both termini","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"lchemes","start":355,"term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"17996702","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":269,"region_id":"DP01426r012","released":"2022_06","ec_id":"ECO:0006220","reference_html":"Crystal structure of the retinoblastoma protein N domain provides insight into tumor suppression, ligand interaction, and holoprotein architecture. <i> Hassler M, Singh S, Yue WW, Luczynski M, Lakbir R, Sanchez-Sanchez F, Bader T, Pearl LH, Mittnacht S. </i> Mol Cell, 2007","statement":[{"text":"Disordered loop in the RbN domain joining helices alpha 9 and alpha 10 (R-Linker) \" limited tryptic digestion of Rb residues 1-370 generated two fragments [...] indicating trimming from both termini and removal of an internal arginine (Arg)-rich linker (aa 251-266)\"","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":245,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"17996702","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-06-15T19:27:13.159Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2QDJ"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":114,"end":114,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":149,"end":149,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":209,"end":209,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":220,"end":220,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":234,"end":234,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":301,"end":301,"position":"Specific residue"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":511,"region_id":"DP01426r013","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structures of inactive retinoblastoma protein reveal multiple mechanisms for cell cycle control. <i> Burke JR, Hura GL, Rubin SM. </i> Genes Dev, 2012","statement":[{"text":"This is a Flexible region in the RbA subdomain that appears disordered in most RbAB structures","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"lchemes","start":500,"term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"22569856","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4ELL"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":615,"region_id":"DP01426r014","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structures of inactive retinoblastoma protein reveal multiple mechanisms for cell cycle control. <i> Burke JR, Hura GL, Rubin SM. </i> Genes Dev, 2012","statement":[{"text":"Region is part of the RbPL, a flexible loop connecting the A and B subdomains of the central RbAB domain. This loop can be phosphorylated, inducing a closed conformation that has decreased ability to bind the E2F transcription factor","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"lchemes","start":577,"term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"22569856","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4ELL"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":615,"term_name":"flexible linker","start":577,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"lchemes","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"22569856","version":3,"reference_html":"Structures of inactive retinoblastoma protein reveal multiple mechanisms for cell cycle control. <i> Burke JR, Hura GL, Rubin SM. </i> Genes Dev, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006220","region_id":"DP01426r015","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":615,"term_name":"protein binding","start":577,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","statement":[{"text":"Phosphorylation of S608 in the flexible RbPL loop induces binding to RbAB (residues 600-609) favouring a \"closed\" autoinhibited conformation which inhibits binding of the E2F transactivation domain to pRb. \"In sum, the RbPL–P structure demonstrates that S608 phosphorylation results in a bound and inhibitory conformation of RbPL that directly blocks the E2FTD-binding site.\"","type":"Results"}],"curator_id":"lchemes","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"22569856","version":3,"reference_html":"Structures of inactive retinoblastoma protein reveal multiple mechanisms for cell cycle control. <i> Burke JR, Hura GL, Rubin SM. </i> Genes Dev, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP01426r016","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":589,"region_id":"DP01426r017","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the retinoblastoma tumour-suppressor pocket domain bound to a peptide from HPV E7. <i> Lee JO, Russo AA, Pavletich NP. </i> Nature, 1998","statement":[{"text":"This region of the RbPL linker appears disordered in the crystal structure","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"lchemes","start":578,"term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"9495340","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1GUX"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":928,"region_id":"DP01426r018","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release. <i> Rubin SM, Gall AL, Zheng N, Pavletich NP. </i> Cell, 2005","statement":[{"text":"Limited proteolysis of an Rb protein containing the pocket and RbC domains (771-928) suggested that RbC does not contain stable structural domains. However, the region 771-785 is part of the ordered Rb pocket domain and hence not included in the annotation.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":786,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"16360038","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":928,"region_id":"DP01426r019","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release. <i> Rubin SM, Gall AL, Zheng N, Pavletich NP. </i> Cell, 2005","statement":[{"text":"NMR data indicate that the isolated RbC (786-928) is unstructured in solution.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":786,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"16360038","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":873,"region_id":"DP01426r020","reference_id":"16360038","start":829,"term_id":"IDPO:0000011","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Here, we demonstrate an interaction between RbC and the CC-MB domains of E2F-DP heterodimers and present the crystal structure of an RbC-E2F1-DP1 complex.","type":"Introduction"}],"curator_id":"vnugnes","released":"2022_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"x-ray crystallography evidence used in manual assertion","version":4,"reference_html":"Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release. <i> Rubin SM, Gall AL, Zheng N, Pavletich NP. </i> Cell, 2005","date":"2022-06-15T19:38:49.385Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"2AZE"}],"term_name":"disorder to order","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q01094 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q14186 "}]},{"region_id":"DP01426r021","ec_ontology":"ECO","end":873,"term_id":"GO:0005515","start":829,"version":4,"statement":[{"text":"Here, we demonstrate an interaction between RbC and the CC-MB domains of E2F-DP heterodimers and present the crystal structure of an RbC-E2F1-DP1 complex.","type":"Introduction"},{"text":"RbC Binds to E2FCM-DPCM through a Bipartite Interaction","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q01094","partner_end":null},{"partner_start":null,"db":"UniProt","id":"Q14186","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16360038","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2AZE"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"fquaglia","reference_html":"Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release. <i> Rubin SM, Gall AL, Zheng N, Pavletich NP. </i> Cell, 2005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":873,"region_id":"DP01426r022","reference_id":"16360038","start":829,"term_id":"GO:0060090","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Here, we demonstrate an interaction between RbC and the CC-MB domains of E2F-DP heterodimers and present the crystal structure of an RbC-E2F1-DP1 complex.","type":"Introduction"},{"text":"RbC Binds to E2FCM-DPCM through a Bipartite Interaction","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"x-ray crystallography evidence used in manual assertion","version":4,"reference_html":"Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release. <i> Rubin SM, Gall AL, Zheng N, Pavletich NP. </i> Cell, 2005","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"2AZE"}],"term_name":"molecular adaptor activity","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P06400","date":"2018-07-17T11:59:30.000Z","acc":"P06400","name":"Retinoblastoma-associated protein","length":928,"organism":"Homo sapiens","dataset":["Autophagy-related proteins","Cancer-related proteins"],"UniParc":"UPI00001740DB","genes":[{"name":{"value":"RB1"}}],"alphafold_very_low_content":0.21120689655172414,"disorder_content":0.2974137931034483,"disprot_consensus":{"full":[{"start":84,"end":93,"type":"D"},{"start":245,"end":269,"type":"D"},{"start":346,"end":370,"type":"T"},{"start":500,"end":513,"type":"D"},{"start":577,"end":635,"type":"D"},{"start":786,"end":828,"type":"D"},{"start":829,"end":873,"type":"T"},{"start":874,"end":928,"type":"D"}],"Structural state":[{"start":84,"end":93,"type":"D"},{"start":245,"end":269,"type":"D"},{"start":346,"end":370,"type":"D"},{"start":500,"end":513,"type":"D"},{"start":577,"end":635,"type":"D"},{"start":786,"end":928,"type":"D"}],"Disorder function":[{"start":346,"end":370,"type":"F"},{"start":577,"end":635,"type":"F"}],"Molecular function":[{"start":346,"end":370,"type":"F"},{"start":577,"end":615,"type":"F"},{"start":829,"end":873,"type":"F"}],"Structural transition":[{"start":346,"end":370,"type":"T"},{"start":829,"end":873,"type":"T"}]}},{"features":{"pfam":[{"id":"PF02319","name":"E2F/DP family winged-helix DNA-binding domain","start":129,"end":192},{"id":"PF16421","name":"E2F transcription factor CC-MB domain","start":206,"end":299}],"gene3D":[{"start":121,"end":194,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}]},"uniref50":"UniRef50_Q01094","sequence":"MALAGAPAGGPCAPALEALLGAGALRLLDSSQIVIISAAQDASAPPAPTGPAAPAAGPCDPDLLLFATPQAPRPTPSAPRPALGRPPVKRRLDLETDHQYLAESSGPARGRGRHPGKGVKSPGEKSRYETSLNLTTKRFLELLSHSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLGSHTTVGVGGRLEGLTQDLRQLQESEQQLDHLMNICTTQLRLLSEDTDSQRLAYVTCQDLRSIADPAEQMVMVIKAPPETQLQAVDSSENFQISLKSKQGPIDVFLCPEETVGGISPGKTPSQEVTSEEENRATDSATIVSPPPSSPPSSLTTDPSQSLLSLEQEPLLSRMGSLRAPVDEDRLSPLVAADSLLEHVREDFSGLLPEEFISLSPPHEALDYHFGLEEGEGIRDLFDCDFGDLTPLDF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q01094","disprot_id":"DP01427","ncbi_taxon_id":9606,"regions_counter":4,"creator":"bmesza","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":301,"region_id":"DP01427r001","start":200,"ec_id":"ECO:0006165","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The lack of 15N and particularly 1H chemical shift dispersion in (A) and (B) are consistent with polypeptides lacking significant structure (Dyson and Wright, 2004). The fact that the NMR data suggests that E2F1CM is unstructured in the absence of DP1CM is consistent with the structural and biochemical studies presented in this study, which indicate that the stability of E2F1CM requires heterodimerization. ","type":"Supplementary material"},{"text":"In addition, NMR data suggest that E2F1CM is unstructured in the absence of DP1 (Supplemental Data, Section 2). These results confirm the structure-based prediction that the E2F1CM homodimer is less stable than the E2F1CM-DP1CM heterodimer, and they provide an explanation for the observation that the DNA binding and transactivation activities of E2F1 are reduced in the absence of a DP partner","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16360038","version":4,"reference_html":"Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release. <i> Rubin SM, Gall AL, Zheng N, Pavletich NP. </i> Cell, 2005","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-07-01T13:55:57.144Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":301,"region_id":"DP01427r002","reference_id":"16360038","start":200,"term_id":"IDPO:0000011","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Intermolecular interactions are distributed throughout the E2F1 and DP1 polypeptides and involve the coiled coil, the β sandwich, and essentially all of the additional secondary-structure elements (Figures 2A and 2B).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"x-ray crystallography evidence used in manual assertion","version":4,"reference_html":"Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release. <i> Rubin SM, Gall AL, Zheng N, Pavletich NP. </i> Cell, 2005","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"2AZE"}],"term_name":"disorder to order","validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-07-01T13:55:34.345Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP01427r003","ec_ontology":"ECO","end":301,"term_id":"GO:0005515","start":200,"version":4,"statement":[{"text":"Here, we demonstrate an interaction between RbC and the CC-MB domains of E2F-DP heterodimers and present the crystal structure of an RbC-E2F1-DP1 complex. ","type":"Introduction"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P06400","partner_end":null},{"partner_start":null,"db":"UniProt","id":"Q14186","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16360038","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2AZE"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"fquaglia","reference_html":"Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release. <i> Rubin SM, Gall AL, Zheng N, Pavletich NP. </i> Cell, 2005","validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-07-01T09:56:06.077Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":301,"region_id":"DP01427r004","reference_id":"16360038","start":200,"term_id":"GO:0060090","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Here, we demonstrate an interaction between RbC and the CC-MB domains of E2F-DP heterodimers and present the crystal structure of an RbC-E2F1-DP1 complex. ","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"x-ray crystallography evidence used in manual assertion","version":4,"reference_html":"Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release. <i> Rubin SM, Gall AL, Zheng N, Pavletich NP. </i> Cell, 2005","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"2AZE"}],"term_name":"molecular adaptor activity","validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-07-01T09:57:04.915Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q01094","date":"2018-07-17T12:08:10.000Z","acc":"Q01094","name":"Transcription factor E2F1","length":437,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000002EDEC","genes":[{"name":{"value":"E2F1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8964493","url":"http://www.ncbi.nlm.nih.gov/pubmed/8964493","alternativeUrl":"https://europepmc.org/abstract/MED/8964493"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:3113","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:3113"}}]},"synonyms":[{"value":"RBBP3","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"1638634","url":"http://www.ncbi.nlm.nih.gov/pubmed/1638634","alternativeUrl":"https://europepmc.org/abstract/MED/1638634"}}]}]}],"alphafold_very_low_content":0.41876430205949655,"disorder_content":0.2334096109839817,"disprot_consensus":{"full":[{"start":200,"end":301,"type":"T"}],"Structural state":[{"start":200,"end":301,"type":"D"}],"Structural transition":[{"start":200,"end":301,"type":"T"}],"Molecular function":[{"start":200,"end":301,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00005","name":"ABC transporter","start":696,"end":857},{"id":"PF00005","name":"ABC transporter","start":1362,"end":1510},{"id":"PF00664","name":"ABC transporter transmembrane region","start":300,"end":590},{"id":"PF00664","name":"ABC transporter transmembrane region","start":1015,"end":1293}],"gene3D":[{"start":290,"end":617,"id":"1.20.1560.10","name":"ABC transporter type 1, transmembrane domain"},{"start":979,"end":1326,"id":"1.20.1560.10","name":"ABC transporter type 1, transmembrane domain"},{"start":1332,"end":1580,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":675,"end":953,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_Q09428","sequence":"MPLAFCGTENHSAAYRVDQGVLNNGCFVDALNVVPHVFLLFITFPILFIGWGSQSSKVHIHHSTWLHFPGHNLRWILTFILLFVLVCEIAEGILSDGVTESRHLHLYMPAGMAFMAAITSVVYYHNIETSNFPKLLIALLIYWTLAFITKTIKFVKFYDHAIGFSQLRFCLTGLLVILYGMLLLVEVNVIRVRRYIFFKTPREVKPPEDLQDLGVRFLQPFVNLLSKGTYWWMNAFIKTAHKKPIDLRAIAKLPIAMRALTNYQRLCVAFDAQARKDTQSPQGARAIWRALCHAFGRRLILSSTFRILADLLGFAGPLCIFGIVDHLGKENHVFQPKTQFLGVYFVSSQEFLGNAYVLAVLLFLALLLQRTFLQASYYVAIETGINLRGAIQTKIYNKIMHMSTSNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWTMPVQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRTTLEHSNERLKQTNEMLRGMKLLKLYAWESIFCSRVEVTRRKEMTSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKESDLSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKLSEFLSSAEIREEQCAPREPAPQGQAGKYQAVPLKVVNRKRPAREEVRDLLGPLQRLAPSMDGDADNFCVQIIGGFFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSNLPDSEGEDPSSPERETAAGSDIRSRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQQTNVVFLDDPFSALDVHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSECQLFEHWKTLMNRQDQELEKETVMERKASEPSQGLPRAMSSRDGLLLDEEEEEEEAAESEEDDNLSSVLHQRAKIPWRACTKYLSSAGILLLSLLVFSQLLKHMVLVAIDYWLAKWTDSALVLSPAARNCSLSQECDLDQSVYAMVFTLLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLVSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVCMEYIGACVVLIAAATSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIHALLKTEAESYEGLLAPSLIPKNWPDQGKIQIQNLSVRYDSSLKPVLKHVNTLISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPETLLSQKDSVFASFVRADK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Cricetidae","Cricetinae","Cricetus"],"uniref90":"UniRef90_Q09427","disprot_id":"DP01429","ncbi_taxon_id":10034,"regions_counter":5,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1000,"region_id":"DP01429r001","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Cryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating. <i> Martin GM, Yoshioka C, Rex EA, Fay JF, Xie Q, Whorton MR, Chen JZ, Shyng SL. </i> Elife, 2017","statement":[{"text":"SUR1 had some disordered regions (744-770, 928-1000, 1319-1343), particularly in the linkers\nbetween TMDs and NBDs, and in NBD1, that were not seen in our map.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":928,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5TWV"}],"reference_id":"28092267","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1343,"region_id":"DP01429r002","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Cryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating. <i> Martin GM, Yoshioka C, Rex EA, Fay JF, Xie Q, Whorton MR, Chen JZ, Shyng SL. </i> Elife, 2017","statement":[{"text":"SUR1 had some disordered regions (744-770, 928-1000, 1319-1343), particularly in the linkers\nbetween TMDs and NBDs, and in NBD1, that were not seen in our map.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":1319,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5TWV"}],"reference_id":"28092267","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":770,"region_id":"DP01429r003","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Cryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating. <i> Martin GM, Yoshioka C, Rex EA, Fay JF, Xie Q, Whorton MR, Chen JZ, Shyng SL. </i> Elife, 2017","statement":[{"text":"SUR1 had some disordered regions (744-770, 928-1000, 1319-1343), particularly in the linkers\nbetween TMDs and NBDs, and in NBD1, that were not seen in our map.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":747,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5TWV"}],"reference_id":"28092267","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":1000,"region_id":"DP01429r004","reference_id":"28092267","start":928,"term_id":"IDPO:0000033","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"SUR1 had some disordered regions (744–770, 928–1000, 1319–1343), particularly in the linkers between TMDs and NBDs, and in NBD1, that were not seen in our map.","type":"Methods"},{"text":"Flexible linker connecting ABC transporter 1 domain and ABC transmembrane type-1 2 domain.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy evidence used in manual assertion","version":4,"reference_html":"Cryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating. <i> Martin GM, Yoshioka C, Rex EA, Fay JF, Xie Q, Whorton MR, Chen JZ, Shyng SL. </i> Elife, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","cross_refs":[{"db":"PDB","id":"5TWV"}],"term_name":"flexible linker","ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":1343,"region_id":"DP01429r005","reference_id":"28092267","start":1319,"term_id":"IDPO:0000033","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"SUR1 had some disordered regions (744–770, 928–1000, 1319–1343), particularly in the linkers between TMDs and NBDs, and in NBD1, that were not seen in our map.","type":"Methods"},{"text":"Flexible linker connecting ABC transmembrane type-1 2 and ABC transporter 2 domain.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy evidence used in manual assertion","version":4,"reference_html":"Cryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating. <i> Martin GM, Yoshioka C, Rex EA, Fay JF, Xie Q, Whorton MR, Chen JZ, Shyng SL. </i> Elife, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","cross_refs":[{"db":"PDB","id":"5TWV"}],"term_name":"flexible linker","ec_go":"IDA","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_Q09427","date":"2018-07-17T12:49:35.000Z","acc":"Q09427","name":"ATP-binding cassette sub-family C member 8","length":1582,"organism":"Cricetus cricetus","dataset":[],"UniParc":"UPI000017071E","genes":[{"name":{"value":"ABCC8"},"synonyms":[{"value":"SUR"}]}],"alphafold_very_low_content":0.09671302149178256,"disorder_content":0.07711757269279393,"disprot_consensus":{"full":[{"start":747,"end":770,"type":"D"},{"start":928,"end":1000,"type":"D"},{"start":1319,"end":1343,"type":"D"}],"Structural state":[{"start":747,"end":770,"type":"D"},{"start":928,"end":1000,"type":"D"},{"start":1319,"end":1343,"type":"D"}],"Disorder function":[{"start":928,"end":1000,"type":"F"},{"start":1319,"end":1343,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03931","name":"Skp1 family, tetramerisation domain","start":5,"end":65}],"gene3D":[{"start":1,"end":99,"id":"3.30.710.10","name":"Potassium Channel Kv1.1; Chain A"}]},"uniref50":"UniRef50_Q03071","sequence":"MSQDFVTLVSKDDKEYEISRSAAMISPTLKAMIEGPFRESKGRIELKQFDSHILEKAVEYLNYNLKYSGVSEDDDEIPEFEIPTEMSLELLLAADYLSI","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q03071","disprot_id":"DP01430","ncbi_taxon_id":559292,"regions_counter":1,"creator":"bmesza","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":99,"region_id":"DP01430r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Binding of elongin A or a von Hippel-Lindau peptide stabilizes the structure of yeast elongin C. <i> Botuyan MV, Koth CM, Mer G, Chakrabartty A, Conaway JW, Conaway RC, Edwards AM, Arrowsmith CH, Chazin WJ. </i> Proc Natl Acad Sci U S A, 1999","statement":[{"text":"15N HSQC NMR spectra indicate that Elc1 has regions of dynamic instability and/or flexibility. Most peaks missing from the HSQC spectrum and those lacking correlations in triple-resonance and NOESY spectra are from residues at the C terminus of Elc1. Thus, the dynamic instability of Elc1 appears to be most prominent at the C terminus.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":77,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"10430890","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q03071","date":"2018-07-17T13:57:57.000Z","acc":"Q03071","name":"Elongin-C","length":99,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000069742","genes":[{"name":{"value":"ELC1"},"olnNames":[{"value":"YPL046C"}]}],"alphafold_very_low_content":0.010101010101010102,"disorder_content":0.23232323232323232,"disprot_consensus":{"full":[{"start":77,"end":99,"type":"D"}],"Structural state":[{"start":77,"end":99,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03242","name":"Late embryogenesis abundant protein (LEA_3a subfamily)","start":1,"end":93}]},"uniref50":"UniRef50_C6SZ33","sequence":"MARSFTNIKAISALVAEEFSNSLARRGYAATAQSAGRVGASMSGKMGSTKSGEEKAAAREKVSWVPDPVTGYYKPENIKEIDVAELRSAVLGKN","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","fabids","Fabales","Fabaceae","Papilionoideae","50 kb inversion clade","NPAAA clade","Hologalegina","robinioid clade","Loteae","Lotus"],"uniref90":"UniRef90_C6ZFX3","disprot_id":"DP01431","ncbi_taxon_id":34305,"regions_counter":3,"creator":"achasapi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":94,"region_id":"DP01431r002","released":"2022_03","ec_id":"ECO:0007691","reference_html":"An unusual intrinsically disordered protein from the model legume Lotus japonicus stabilizes proteins in vitro. <i> Haaning S, Radutoiu S, Hoffmann SV, Dittmer J, Giehm L, Otzen DE, Stougaard J. </i> J Biol Chem, 2008","statement":[{"text":"LjIDP1 protease sensitivity is comparable with the intrinsically disordered α-synuclein, whereas the globular protein lysozyme remains intact under the same conditions. This suggests that the amino acid backbone of LjIDP1 is largely accessible to proteolytic attack and in combination with the spectroscopic data unequivocally shows that LjIDP1 is largely disordered along the entire length.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"achasapi","start":1,"term_ontology":"IDPO","curator_name":"Anastasia Chasapi","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1986-5007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18779323","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":94,"region_id":"DP01431r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"An unusual intrinsically disordered protein from the model legume Lotus japonicus stabilizes proteins in vitro. <i> Haaning S, Radutoiu S, Hoffmann SV, Dittmer J, Giehm L, Otzen DE, Stougaard J. </i> J Biol Chem, 2008","statement":[{"text":"The 1H spectrum of LjIDP1 shows no signal dispersion typical of globular proteins, and the similarity of the spectra in the aliphatic region with and without urea indicates that no major structural transitions occurred and supports the notion that LjIDP1 is intrinsically disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"achasapi","start":1,"term_ontology":"IDPO","curator_name":"Anastasia Chasapi","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1986-5007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18779323","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_C6ZFX3","date":"2018-07-17T13:58:30.000Z","acc":"C6ZFX3","name":"Intrinsically disordered protein 1","length":94,"organism":"Lotus japonicus","dataset":[],"UniParc":"UPI0001B0671B","genes":[],"alphafold_very_low_content":0.2553191489361702,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":94,"type":"D"}],"Structural state":[{"start":1,"end":94,"type":"D"}]}},{"features":{"pfam":[{"id":"PF13499","name":"EF-hand domain pair","start":43,"end":104}],"gene3D":[{"start":1,"end":108,"id":"1.10.238.10","name":"EF-hand"}]},"uniref50":"UniRef50_Q91482","sequence":"MACAHLCKEADIKAALEACKAADTFNFKTFFHTIGFASKSADDVKKAFKVIDQDASGFIEVEELKLFLQNFCPNARVLTDAETKAFLKAGDADGDGMIGIDEFAVLVKQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Actinopterygii","Neopterygii","Teleostei","Protacanthopterygii","Salmoniformes","Salmonidae","Salmoninae","Oncorhynchus"],"uniref90":"UniRef90_Q91482","disprot_id":"DP01432","ncbi_taxon_id":8019,"regions_counter":4,"creator":"bmesza","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":109,"region_id":"DP01432r001","released":"2022_03","ec_id":"ECO:0007691","reference_html":"In search for globally disordered apo-parvalbumins: Case of parvalbumin β-1 from coho salmon. <i> Vologzhannikova AA, Khorn PA, Kazakov AS, Ismailov RG, Sokolov AS, Uversky VN, Permyakov EA, Permyakov SE. </i> Cell Calcium, 2017","statement":[{"text":"Ca2+ depletion from csPA makes it susceptible to the limited proteolysis by bovine α-chymotrypsin at 37 °C.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":2,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29029791","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":109,"term_name":"molten globule to order","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","reference_html":"In search for globally disordered apo-parvalbumins: Case of parvalbumin β-1 from coho salmon. <i> Vologzhannikova AA, Khorn PA, Kazakov AS, Ismailov RG, Sokolov AS, Uversky VN, Permyakov EA, Permyakov SE. </i> Cell Calcium, 2017","statement":[{"text":"Apo-PA is destabilized due to the highly unfavorable electrostatic repulsion of the nearby carboxylates within Ca2+-binding loops of PA, which turns into favorable electrostatic attraction upon the metal association.","type":"Results"}],"term_id":"IDPO:0000012","curator_id":"bmesza","start":2,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"29029791","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","region_id":"DP01432r002","ec_go":"IDA","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":109,"region_id":"DP01432r003","released":"2022_03","ec_id":"ECO:0006232","reference_html":"In search for globally disordered apo-parvalbumins: Case of parvalbumin β-1 from coho salmon. <i> Vologzhannikova AA, Khorn PA, Kazakov AS, Ismailov RG, Sokolov AS, Uversky VN, Permyakov EA, Permyakov SE. </i> Cell Calcium, 2017","statement":[{"text":"The DSC data strongly evidence the absence of rigid tertiary structure in apo-csPA. This conclusion is further supported by the data on GdmCl-induced unfolding of apo-csPA at 20 °C, monitored by its molar ellipticity at 222 nm.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":2,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"differential scanning calorimetry evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29029791","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":109,"region_id":"DP01432r004","released":"2022_03","ec_id":"ECO:0001249","reference_html":"In search for globally disordered apo-parvalbumins: Case of parvalbumin β-1 from coho salmon. <i> Vologzhannikova AA, Khorn PA, Kazakov AS, Ismailov RG, Sokolov AS, Uversky VN, Permyakov EA, Permyakov SE. </i> Cell Calcium, 2017","statement":[{"text":"Maximum intensity of bis-ANS fluorescence in the presence of apo-csPA exceeds that value for the Ca2+-loaded protein by a factor of 8, while bis-ANS emission spectrum maximum position (λmax) for apo-csPA is blue shifted by 2 nm with respect to the λmax value for the Ca2+-bound protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":2,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"fluorescence evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29029791","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_E1UJ20","date":"2018-07-17T14:20:44.000Z","acc":"E1UJ20","name":"Parvalbumin beta-1","length":109,"organism":"Oncorhynchus kisutch","dataset":[],"UniParc":"UPI0001E5AE45","genes":[{"name":{"value":"pvalb1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CBG76586.1","url":"https://www.ebi.ac.uk/ena/browser/view/CBG76586.1"}}]},"synonyms":[{"value":"LOC109886728","evidences":[{"code":"ECO:0000313","source":{"name":"Ensembl","id":"ENSOKIP00005100409","url":"https://www.ensembl.org/id/ENSOKIP00005100409"}}]}]}],"alphafold_very_low_content":0,"disorder_content":0.9908256880733946,"disprot_consensus":{"full":[{"start":2,"end":109,"type":"T"}],"Structural state":[{"start":2,"end":109,"type":"D"}],"Structural transition":[{"start":2,"end":109,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00623","name":"RNA polymerase Rpb1, domain 2","start":348,"end":511},{"id":"PF04983","name":"RNA polymerase Rpb1, domain 3","start":516,"end":684},{"id":"PF04990","name":"RNA polymerase Rpb1, domain 7","start":1156,"end":1291},{"id":"PF04992","name":"RNA polymerase Rpb1, domain 6","start":890,"end":1071},{"id":"PF04997","name":"RNA polymerase Rpb1, domain 1","start":12,"end":346},{"id":"PF04998","name":"RNA polymerase Rpb1, domain 5","start":822,"end":889},{"id":"PF04998","name":"RNA polymerase Rpb1, domain 5","start":1072,"end":1155},{"id":"PF04998","name":"RNA polymerase Rpb1, domain 5","start":1292,"end":1418},{"id":"PF05000","name":"RNA polymerase Rpb1, domain 4","start":711,"end":815}],"gene3D":[{"start":517,"end":678,"id":"1.10.274.100","name":"RNA polymerase Rpb1, domain 3"},{"start":679,"end":824,"id":"1.10.132.30","name":"1.10.132.30"},{"start":1156,"end":1292,"id":"3.30.1360.140","name":"3.30.1360.140"},{"start":338,"end":508,"id":"2.40.40.20","name":"2.40.40.20"},{"start":1418,"end":1463,"id":"1.10.150.390","name":"1.10.150.390"},{"start":381,"end":444,"id":"3.30.1490.180","name":"RNA polymerase ii"},{"start":258,"end":311,"id":"1.20.120.1280","name":"RNA polymerase II, clamp domain"},{"start":3,"end":119,"id":"1.20.120.1280","name":"RNA polymerase II, clamp domain"}]},"uniref50":"UniRef50_P04052","sequence":"MSTPTDSKAPLRQVKRVQFGILSPDEIRRMSVTEGGVQFAETMEGGRPKLGGLMDPRQGVIDRTSRCQTCAGNMTECPGHFGHIDLAKPVFHIGFITKTIKILRCVCFYCSKMLVSPHNPKIKEIVMKSRGQPRKRLAYVYDLCKGKTICEGGEDMDLTKENQQPDPNKKPGHGGCGHYQPSIRRTGLDLTAEWKHQNEDSQEKKIVVSAERVWEILKHITDEECFILGMDPKYARPDWMIVTVLPVPPLAVRPAVVMFGAAKNQDDLTHKLSDIIKANNELRKNEASGAAAHVIQENIKMLQFHVATLVDNDMPGMPRAMQKSGKPLKAIKARLKGKEGRIRGNLMGKRVDFSARTVITPDPNLRIDQVGVPRSIAQNLTFPELVTPFNIDRMQELVRRGNSQYPGAKYIVRDNGERIDLRFHPKSSDLHLQCGYKVERHLRDDDLVIFNRQPTLHKMSMMGHRVKVLPWSTFRMNLSCTSPYNADFDGDEMNLHVPQSMETRAEVENIHITPRQIITPQANKPVMGIVQDTLTAVRKMTKRDVFITREQVMNLLMFLPTWDAKMPQPCILKPRPLWTGKQIFSLIIPGNVNMIRTHSTHPDEEDEGPYKWISPGDTKVMVEHGELIMGILCKKSLGTSAGSLLHICFLELGHDIAGRFYGNIQTVINNWLLFEGHSIGIGDTIADPQTYNEIQQAIKKAKDDVINVIQKAHNMELEPTPGNTLRQTFENKVNRILNDARDKTGGSAKKSLTEYNNLKAMVVSGSKGSNINISQVIACVGQQNVEGKRIPYGFRKRTLPHFIKDDYGPESRGFVENSYLAGLTPSEFYFHAMGGREGLIDTAVKTAETGYIQRRLIKAMESVMVNYDGTVRNSVGQLIQLRYGEDGLCGELVEFQNMPTVKLSNKSFEKRFKFDWSNERLMKKVFTDDVIKEMTDSSEAIQELEAEWDRLVSDRDSLRQIFPNGESKVVLPCNLQRMIWNVQKIFHINKRLPTDLSPIRVIKGVKTLLERCVIVTGNDRISKQANENATLLFQCLIRSTLCTKYVSEEFRLSTEAFEWLVGEIETRFQQAQANPGEMVGALAAQSLGEPATQMTLNTFHFAGVSSKNVTLGVPRLKEIINISKKPKAPSLTVFLTGGAARDAEKAKNVLCRLEHTTLRKVTANTAIYYDPDPQRTVISEDQEFVNVYYEMPDFDPTRISPWLLRIELDRKRMTDKKLTMEQIAEKINVGFGEDLNCIFNDDNADKLVLRIRIMNNEENKFQDEDEAVDKMEDDMFLRCIEANMLSDMTLQGIEAIGKVYMHLPQTDSKKRIVITETGEFKAIGEWLLETDGTSMMKVLSERDVDPIRTSSNDICEIFQVLGIEAVRKSVEKEMNAVLQFYGLYVNYRHLALLCDVMTAKGHLMAITRHGINRQDTGALMRCSFEETVDVLMDAAAHAETDPMRGVSENIIMGQLPKMGTGCFDLLLDAEKCRFGIEIPNTLGNSMLGGAAMFIGGGSTPSMTPPMTPWANCNTPRYFSPPGHVSAMTPGGPSFSPSAASDASGMSPSWSPAHPGSSPSSPGPSMSPYFPASPSVSPSYSPTSPNYTASSPGGASPNYSPSSPNYSPTSPLYASPRYASTTPNFNPQSTGYSPSSSGYSPTSPVYSPTVQFQSSPSFAGSGSNIYSPGNAYSPSSSNYSPNSPSYSPTSPSYSPSSPSYSPTSPCYSPTSPSYSPTSPNYTPVTPSYSPTSPNYSASPQYSPASPAYSQTGVKYSPTSPTYSPPSPSYDGSPGSPQYTPGSPQYSPASPKYSPTSPLYSPSSPQHSPSNQYSPTGSTYSATSPRYSPNMSIYSPSSTKYSPTSPTYTPTARNYSPTSPMYSPTAPSHYSPTSPAYSPSSPTFEESED","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_P04052","disprot_id":"DP01433","ncbi_taxon_id":7227,"regions_counter":1,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1739,"region_id":"DP01433r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Phosphorylation induces sequence-specific conformational switches in the RNA polymerase II C-terminal domain. <i> Gibbs EB, Lu F, Portz B, Fisher MJ, Medellin BP, Laremore TN, Zhang YJ, Gilmour DS, Showalter SA. </i> Nat Commun, 2017","statement":[{"text":"In summary, the\nunphosphorylated state CTD2' is highly disordered, temporally\ndynamic and contains nearly all trans-proline.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":1657,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28497798","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P04052","date":"2018-07-17T14:34:24.000Z","acc":"P04052","name":"DNA-directed RNA polymerase II subunit RPB1","length":1887,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI000016BD40","genes":[{"name":{"value":"RpII215"},"orfNames":[{"value":"CG1554"}]}],"alphafold_very_low_content":0.23264440911499734,"disorder_content":0.04398516163222046,"disprot_consensus":{"full":[{"start":1657,"end":1739,"type":"D"}],"Structural state":[{"start":1657,"end":1739,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01034","name":"Syndecan domain","start":139,"end":196}]},"uniref50":"UniRef50_P31431","sequence":"MAPARLFALLLFFVGGVAESIRETEVIDPQDLLEGRYFSGALPDDEDVVGPGQESDDFELSGSGDLDDLEDSMIGPEVVHPLVPLDNHIPERAGSGSQVPTEPKKLEENEVIPKRISPVEESEDVSNKVSMSSTVQGSNIFERTEVLAALIVGGIVGILFAVFLILLLMYRMKKKDEGSYDLGKKPIYKKAPTNEFYA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P31431","disprot_id":"DP01434","ncbi_taxon_id":9606,"regions_counter":1,"creator":"bmesza","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":198,"region_id":"DP01434r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of the dimeric cytoplasmic domain of syndecan-4. <i> Shin J, Lee W, Lee D, Koo BK, Han I, Lim Y, Woods A, Couchman JR, Oh ES. </i> Biochemistry, 2001","statement":[{"text":"Two-dimensional NOESY proton spectrum shows that the intracellular regions of syndecan-4 exhibit extensive flexibility.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":171,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"11456484","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-09T15:26:46.379Z"}}],"released":"2018_11","uniref100":"UniRef100_P31431","date":"2018-07-17T15:36:21.000Z","acc":"P31431","name":"Syndecan-4","length":198,"organism":"Homo sapiens","dataset":["Cancer-related proteins","Extracellular matrix proteins"],"UniParc":"UPI000003EE91","genes":[{"name":{"value":"SDC4"}}],"alphafold_very_low_content":0.16161616161616163,"disorder_content":0.1414141414141414,"disprot_consensus":{"full":[{"start":171,"end":198,"type":"D"}],"Structural state":[{"start":171,"end":198,"type":"D"}]}},{"features":{"pfam":[{"id":"PF05831","name":"GAGE protein","start":1,"end":101}]},"uniref50":"UniRef50_O60829","sequence":"MSARVRSRSRGRGDGQEAPDVVAFVAPGESQQEEPPTDNQDIEPGQEREGTPPIEERKVEGDCQEMDLEKTRSERGDGSDVKEKTPPNPKHAKTKEAGDGQP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O60829","disprot_id":"DP01435","ncbi_taxon_id":9606,"regions_counter":11,"creator":"mmacossay","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":102,"region_id":"DP01435r001","released":"2022_03","ec_id":"ECO:0006198","reference_html":"The cancer/testis antigen prostate-associated gene 4 (PAGE4) is a highly intrinsically disordered protein. <i> Zeng Y, He Y, Yang F, Mooney SM, Getzenberg RH, Orban J, Kulkarni P. </i> J Biol Chem, 2011","statement":[{"text":"1) Thus, the lack of signal dispersion is strongly indicative of a polypeptide chain with little or no defined tertiary structure\n2) Taken together, the CD and NMR data show that PAGE4 does not have detectable secondary and tertiary structure, consistent with an IDP","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mmacossay","start":1,"term_ontology":"IDPO","curator_name":"Mauricio Macossay-Castillo","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21357425","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":102,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","reference_html":"The cancer/testis antigen prostate-associated gene 4 (PAGE4) is a highly intrinsically disordered protein. <i> Zeng Y, He Y, Yang F, Mooney SM, Getzenberg RH, Orban J, Kulkarni P. </i> J Biol Chem, 2011","statement":[{"text":"PAGE4 preferential binding sites when the PAGE4-FLAG protein was present (lane 3) as well as FLAG-p53, which was used as a positive control. DNA sequence analysis revealed that PAGE4 preferentially binds to a GC-rich sequence, 5'-GCCGCGGGG-3' (Fig. 4)","type":"Results"}],"term_id":"GO:0003676","curator_id":"mmacossay","start":1,"term_ontology":"GO","curator_name":"Mauricio Macossay-Castillo","reference_id":"21357425","version":3,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006198","region_id":"DP01435r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":102,"region_id":"DP01435r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The cancer/testis antigen prostate-associated gene 4 (PAGE4) is a highly intrinsically disordered protein. <i> Zeng Y, He Y, Yang F, Mooney SM, Getzenberg RH, Orban J, Kulkarni P. </i> J Biol Chem, 2011","statement":[{"text":"1) These spectra showed that the PAGE4 polypeptide chain contains no significant alpha-helical or beta-strand secondary structural elements over this temperature range as evidenced by low ellipticity values in the 215–230 nm region\n2) Taken together, the CD and NMR data show that PAGE4 does not have detectable secondary and tertiary structure, consistent with an IDP","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mmacossay","start":1,"term_ontology":"IDPO","curator_name":"Mauricio Macossay-Castillo","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21357425","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":102,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"The cancer/testis antigen prostate-associated gene 4 (PAGE4) is a highly intrinsically disordered protein. <i> Zeng Y, He Y, Yang F, Mooney SM, Getzenberg RH, Orban J, Kulkarni P. </i> J Biol Chem, 2011","statement":[{"text":"PAGE4 preferential binding sites when the PAGE4-FLAG protein was present (lane 3) as well as FLAG-p53, which was used as a positive control. DNA sequence analysis revealed that PAGE4 preferentially binds to a GC-rich sequence, 5'-GCCGCGGGG-3' (Fig. 4)","type":"Results"}],"term_id":"GO:0003676","curator_id":"mmacossay","start":1,"term_ontology":"GO","curator_name":"Mauricio Macossay-Castillo","reference_id":"21357425","version":3,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01435r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":102,"region_id":"DP01435r005","released":"2024_06","ec_id":"ECO:0006165","reference_html":"Phosphorylation-induced Conformational Ensemble Switching in an Intrinsically Disordered Cancer/Testis Antigen. <i> He Y, Chen Y, Mooney SM, Rajagopalan K, Bhargava A, Sacho E, Weninger K, Bryan PN, Kulkarni P, Orban J. </i> J Biol Chem, 2015","statement":[{"text":"These data show that WT PAGE4 is highly flexible, with average heteronuclear NOE values (∼0.1–0.2) similar to those of comparable molecular weight IDPs (53).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-08T15:24:49.446Z","reference_source":"pmid","term_name":"disorder","reference_id":"26242913","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"BMRB","id":"26544"}]},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":70,"term_name":"disorder to order","released":"2024_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Phosphorylation-induced Conformational Ensemble Switching in an Intrinsically Disordered Cancer/Testis Antigen. <i> He Y, Chen Y, Mooney SM, Rajagopalan K, Bhargava A, Sacho E, Weninger K, Bryan PN, Kulkarni P, Orban J. </i> J Biol Chem, 2015","statement":[{"text":"As expected, the largest effects for 15N, HN, and CO shifts were seen at Thr-51 itself, with relatively smaller changes for the nearest neighbors. In contrast to these localized effects, significant differences were detected for Cα chemical shifts over a region extending from residues 40–70 (Fig. 4C).","type":"Results"},{"text":"Phosphorylation on Thr-51 decreases picosecond-nanosecond timescale motions in the immediate vicinity, with higher heteronuclear NOE values for Thr-51, Ile-54, and Glu-55 and smaller changes in other parts of the chain.","type":"Results"},{"text":"Therefore, phosphorylation switches the conformational ensemble to a more compact but still flexible state.","type":"Discussion"}],"term_id":"IDPO:0000011","curator_id":"vnugnes","start":40,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"26242913","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-08T15:36:48.020Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01435r006","ec_go":"EXP","disprot_namespace":"Structural transition","construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":51,"end":51,"position":"Specific residue"}],"cross_refs":[{"db":"BMRB","id":"26545"},{"db":"BMRB","id":"26544"}]},{"start":49,"end":53,"reference_id":"26242913","reference_source":"pmid","reference_html":"Phosphorylation-induced Conformational Ensemble Switching in an Intrinsically Disordered Cancer/Testis Antigen. <i> He Y, Chen Y, Mooney SM, Rajagopalan K, Bhargava A, Sacho E, Weninger K, Bryan PN, Kulkarni P, Orban J. </i> J Biol Chem, 2015","date":"2024-02-08T15:34:06.313Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":51,"end":51,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":9,"end":9,"position":"Specific residue"}],"cross_refs":[{"db":"BMRB","id":"26545"}],"region_id":"DP01435r007","statement":[{"text":"NMR assignment of phospho-PAGE4 using the above methods revealed complete phosphorylation at Thr-51 and partial (∼30–40%) phosphorylation at Ser-9.","type":"Results"}]},{"start":7,"end":11,"reference_id":"26242913","reference_source":"pmid","reference_html":"Phosphorylation-induced Conformational Ensemble Switching in an Intrinsically Disordered Cancer/Testis Antigen. <i> He Y, Chen Y, Mooney SM, Rajagopalan K, Bhargava A, Sacho E, Weninger K, Bryan PN, Kulkarni P, Orban J. </i> J Biol Chem, 2015","date":"2024-02-08T15:34:30.871Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":51,"end":51,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":9,"end":9,"position":"Specific residue"}],"cross_refs":[{"db":"BMRB","id":"26545"}],"region_id":"DP01435r008","statement":[{"text":"NMR assignment of phospho-PAGE4 using the above methods revealed complete phosphorylation at Thr-51 and partial (∼30–40%) phosphorylation at Ser-9.","type":"Results"}]},{"start":7,"end":11,"reference_id":"26242913","reference_source":"pmid","reference_html":"Phosphorylation-induced Conformational Ensemble Switching in an Intrinsically Disordered Cancer/Testis Antigen. <i> He Y, Chen Y, Mooney SM, Rajagopalan K, Bhargava A, Sacho E, Weninger K, Bryan PN, Kulkarni P, Orban J. </i> J Biol Chem, 2015","date":"2024-02-08T15:35:13.143Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":51,"end":51,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":9,"end":9,"position":"Specific residue"}],"region_id":"DP01435r009","statement":[{"text":"The original HIPK1 kinase study suggested single-site specificity of phosphorylation at Thr-51, but the coexpression experiments carried out here on a larger scale for NMR analysis produced an ∼2:1 mixture of singly and doubly phosphorylated PAGE4, evident from both NMR analysis (Fig. 2, B and D) and mass spectrometry (Fig. 3).","type":"Results"}]},{"start":49,"end":53,"reference_id":"26242913","reference_source":"pmid","reference_html":"Phosphorylation-induced Conformational Ensemble Switching in an Intrinsically Disordered Cancer/Testis Antigen. <i> He Y, Chen Y, Mooney SM, Rajagopalan K, Bhargava A, Sacho E, Weninger K, Bryan PN, Kulkarni P, Orban J. </i> J Biol Chem, 2015","date":"2024-02-08T15:35:28.806Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":51,"end":51,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":9,"end":9,"position":"Specific residue"}],"region_id":"DP01435r010","statement":[{"text":"The original HIPK1 kinase study suggested single-site specificity of phosphorylation at Thr-51, but the coexpression experiments carried out here on a larger scale for NMR analysis produced an ∼2:1 mixture of singly and doubly phosphorylated PAGE4, evident from both NMR analysis (Fig. 2, B and D) and mass spectrometry (Fig. 3).","type":"Results"}]},{"start":69,"end":73,"reference_id":"26242913","reference_source":"pmid","reference_html":"Phosphorylation-induced Conformational Ensemble Switching in an Intrinsically Disordered Cancer/Testis Antigen. <i> He Y, Chen Y, Mooney SM, Rajagopalan K, Bhargava A, Sacho E, Weninger K, Bryan PN, Kulkarni P, Orban J. </i> J Biol Chem, 2015","date":"2024-02-08T15:42:02.717Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P05412","operator":null,"partner_start":1,"partner_end":223}],"region_id":"DP01435r011","statement":[{"text":"In contrast, addition of either unlabeled full-length c-Jun or c-Jun (1–223) perturbed a specific set of WT PAGE4 residues in a similar way, albeit weakly (Fig. 10A). The largest chemical shift changes occurred in the transient helix region of PAGE4 from residues 69–73 (Fig. 10, A and C). The binding interaction between WT PAGE4 and c-Jun was estimated at a KD of >50 μm from the NMR titration data, with precipitation of c-Jun at higher concentrations preventing a more accurate determination.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_O60829","date":"2018-07-17T15:54:21.000Z","acc":"O60829","name":"P antigen family member 4","length":102,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012B3E1","genes":[{"name":{"value":"PAGE4"},"synonyms":[{"value":"GAGEC1"}],"orfNames":[{"value":"JM27"}]}],"alphafold_very_low_content":0.058823529411764705,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":39,"type":"D"},{"start":40,"end":70,"type":"T"},{"start":71,"end":102,"type":"D"}],"Structural state":[{"start":1,"end":102,"type":"D"}],"Molecular function":[{"start":1,"end":102,"type":"F"}],"Structural transition":[{"start":40,"end":70,"type":"T"}],"Disorder function":[{"start":7,"end":11,"type":"F"},{"start":49,"end":53,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00018","name":"SH3 domain","start":639,"end":682},{"id":"PF00069","name":"Protein kinase domain","start":22,"end":281},{"id":"PF00595","name":"PDZ domain","start":547,"end":623},{"id":"PF00625","name":"Guanylate kinase","start":774,"end":947},{"id":"PF02828","name":"L27 domain","start":374,"end":423},{"id":"PF02828","name":"L27 domain","start":430,"end":478}],"gene3D":[{"start":631,"end":742,"id":"2.30.30.40","name":"SH3 Domains"},{"start":19,"end":101,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":764,"end":961,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":286,"end":319,"id":"1.10.238.10","name":"EF-hand"},{"start":541,"end":630,"id":"2.30.42.10","name":"2.30.42.10"},{"start":102,"end":285,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"}]},"uniref50":"UniRef50_P54936","sequence":"MRELDPDESNLLLDEQLSIRDVIEQGPFSNVYRILHGPSNRKFLLRSINLNLFRQHTGLGFEEIDEEIRICQNLQHPYICRLEKTINSVHYRHIIFENMEGNDICFEIVQRASNGFVFSEYVVSHYTRQLLDALDYCHTRKIVHRDVRPHNLVLASKDTSAPLKLCGFGVAKDLSEIGGSMACGRVGVPQFMAPEIVRKDRVSCSSDIWSSGVVLFLLLAGRLPFSGSTSDIYERIMQTDVDVDGYMPNISESARNLVRRMLNADPSKRISAKEALNHEWIRDKEHMASRKHMNDVIDQMRRYNESRKLKSNVLSAVNSGRFDETTPRQDTPQTAFVDGSSPGGDCCHRGESSSNDAAEPPADKDLSGAYKVLGSLDAINSLLDPNSYKPGSTTFQKIHDDGSVRNLLRLYDKIKALPCEPVVTEVDTSTLRKETLNQIDGLLGPSPEALELRQLLNSPHLASCVQALDVVVCEIRDPKNEASGSGDKEGNCVSSDPAPAYLNGGVLPLGAQRAGTSFEHFNQSAVHTSYDEEEEELYDCMSRLRLVQFQKDTQEPMGITLKVNEDGRCFVARIMHGGMIHRQATLHVGDEIREINGMSVANRSVESLQEMLRDARGQVTFKIIPSYRSAPPACEIFVRAQFDYEPSQDDLIPCPQAGIPFKTGDILQVISKDDHNWWQARFVSSFPSIGNSSNAQRSNQQQVAGLIPSPELQEWRTACLAMERSKNTCNTHCMWFNKKKKYYTTKYLQKHSALFDQLDLVTYEEVMRLSQYRRKTLVLLGAHGVGRRHIKNTLIHRHPNRFAYPIPHTTRPPRKDEVDGKHYYFVTNEQMMADIQNNEYLEYGTHEESMYGTKLETIRNIHKSGKIAILDVEPQALKVLRTAEYSPFVVFIAAPNLQGMQDPDGSLEKLLNESDVLRQAFGHLFDFIITNSDIDDTIAQLERLVEKLPAYPQWLPVTWVY","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"uniref90":"UniRef90_P54936","disprot_id":"DP01436","ncbi_taxon_id":6239,"regions_counter":3,"creator":"bmesza","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":487,"region_id":"DP01436r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Coordinated folding and association of the LIN-2, -7 (L27) domain. An obligate heterodimerization involved in assembly of signaling and cell polarity complexes. <i> Harris BZ, Venkatasubrahmanyam S, Lim WA. </i> J Biol Chem, 2002","statement":[{"text":"Spectra for L27 monomers (Lin-2 and Lin-7 proteins) show little ellipticity at 222 nm, indicating that the individual monomers are largely unfolded.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":423,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"12110687","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":487,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Coordinated folding and association of the LIN-2, -7 (L27) domain. An obligate heterodimerization involved in assembly of signaling and cell polarity complexes. <i> Harris BZ, Venkatasubrahmanyam S, Lim WA. </i> J Biol Chem, 2002","statement":[{"text":"There is a striking increase of ellipticity at 222 nm upon mixing of the monomers. The individual unfolded monomers become a stable, helical, folded unit upon association.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"bmesza","start":423,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"12110687","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01436r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":487,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Coordinated folding and association of the LIN-2, -7 (L27) domain. An obligate heterodimerization involved in assembly of signaling and cell polarity complexes. <i> Harris BZ, Venkatasubrahmanyam S, Lim WA. </i> J Biol Chem, 2002","statement":[{"text":"Difference CD spectra for the interacting pair of proteins (C.e. LIN-7:C.e. LIN-2C) show minima at 222 nm, indicative of a significant increase in α-helical content upon association.","type":"Results"}],"term_id":"GO:0005515","curator_id":"bmesza","start":423,"term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"12110687","version":3,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01436r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P54936","date":"2018-07-17T16:23:02.000Z","acc":"P54936","name":"Protein lin-2","length":961,"organism":"Caenorhabditis elegans","dataset":[],"UniParc":"UPI000012E69E","genes":[{"name":{"value":"lin-2"},"orfNames":[{"value":"F17E5.1"}]}],"alphafold_very_low_content":0.15816857440166493,"disorder_content":0.06763787721123829,"disprot_consensus":{"full":[{"start":423,"end":487,"type":"T"}],"Structural state":[{"start":423,"end":487,"type":"D"}],"Structural transition":[{"start":423,"end":487,"type":"T"}],"Molecular function":[{"start":423,"end":487,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00595","name":"PDZ domain","start":202,"end":278},{"id":"PF02828","name":"L27 domain","start":121,"end":174}],"gene3D":[{"start":178,"end":284,"id":"2.30.42.10","name":"2.30.42.10"},{"start":116,"end":170,"id":"1.10.287.650","name":"L27 domain"}]},"uniref50":"UniRef50_A8XCE8","sequence":"MGLKGFTGSFQQIRGLLRPPKNLPFRGIFRKDGEVVRKDDLLVNQFKMNYHPGLNVYYENDRGERLLRAHCDGIVRISQEKCDPDYEIEEMKGYEYRKDVDLYKMTFNMDNPDGPNLERDVQRILELMEHVQKTGEVNNAKLASLQQVLQSEFFGAVREVYETVYESIDADTTPEIKAAATAKATVAAFAAAEGHAHPRIVELPKTDQGLGFNVMGGKEQNSPIYISRIIPGGVADRHGGLKRGDQLIAVNGNVEAECHEKAVDLLKSAVGSVKLVIRYMPKLLDEMERRFERQRIP","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"uniref90":"UniRef90_A8XCE8","disprot_id":"DP01437","ncbi_taxon_id":6239,"regions_counter":3,"creator":"bmesza","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":180,"region_id":"DP01437r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Coordinated folding and association of the LIN-2, -7 (L27) domain. An obligate heterodimerization involved in assembly of signaling and cell polarity complexes. <i> Harris BZ, Venkatasubrahmanyam S, Lim WA. </i> J Biol Chem, 2002","statement":[{"text":"Spectra for L27 monomers (Lin-2 and Lin-7 proteins) show little ellipticity at 222 nm, indicating that the individual monomers are largely unfolded.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":115,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"12110687","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":180,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Coordinated folding and association of the LIN-2, -7 (L27) domain. An obligate heterodimerization involved in assembly of signaling and cell polarity complexes. <i> Harris BZ, Venkatasubrahmanyam S, Lim WA. </i> J Biol Chem, 2002","statement":[{"text":"There is a striking increase of ellipticity at 222 nm upon mixing of the monomers. The individual unfolded monomers become a stable, helical, folded unit upon association.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"bmesza","start":115,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"12110687","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01437r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":180,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Coordinated folding and association of the LIN-2, -7 (L27) domain. An obligate heterodimerization involved in assembly of signaling and cell polarity complexes. <i> Harris BZ, Venkatasubrahmanyam S, Lim WA. </i> J Biol Chem, 2002","statement":[{"text":"Difference CD spectra for the interacting pair of proteins (C.e. LIN-7:C.e. LIN-2C) show minima at 222 nm, indicative of a significant increase in α-helical content upon association.","type":"Results"}],"term_id":"GO:0005515","curator_id":"bmesza","start":115,"term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"12110687","version":3,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","cross_refs":[{"db":"PDB","id":"1zl8"}],"region_id":"DP01437r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P90976","date":"2018-07-17T16:30:45.000Z","acc":"P90976","name":"LIN-7","length":297,"organism":"Caenorhabditis elegans","dataset":[],"UniParc":"UPI000007C31E","genes":[],"alphafold_very_low_content":0.07744107744107744,"disorder_content":0.2222222222222222,"disprot_consensus":{"full":[{"start":115,"end":180,"type":"T"}],"Structural state":[{"start":115,"end":180,"type":"D"}],"Structural transition":[{"start":115,"end":180,"type":"T"}],"Molecular function":[{"start":115,"end":180,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":12,"end":276},{"id":"PF00595","name":"PDZ domain","start":491,"end":567},{"id":"PF00625","name":"Guanylate kinase","start":738,"end":911},{"id":"PF02828","name":"L27 domain","start":347,"end":395},{"id":"PF02828","name":"L27 domain","start":406,"end":455},{"id":"PF07653","name":"Variant SH3 domain","start":629,"end":674}],"gene3D":[{"start":403,"end":456,"id":"1.10.287.650","name":"L27 domain"},{"start":94,"end":303,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"},{"start":485,"end":576,"id":"2.30.42.10","name":"2.30.42.10"},{"start":593,"end":730,"id":"2.30.30.40","name":"SH3 Domains"},{"start":339,"end":394,"id":"1.10.287.650","name":"L27 domain"},{"start":5,"end":93,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":731,"end":926,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_O14936","sequence":"MADDDVLFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQLRKFNARRKLKGAVLAAVSSHKFNSFYGDPPEELPDFSEDPTSSGLLAAERAVSQVLDSLEEIHALTDCSEKDLDFLHSVFQDQHLHTLLDLYDKINTKSSPQIRNPPSDAVQRAKEVLEEISCYPENNDAKELKRILTQPHFMALLQTHDVVAHEVYSDEALRVTPPPTSPYLNGDSPESANGDMDMENVTRVRLVQFQKNTDEPMGITLKMNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIVPSYRTQSSSCERDSPSTSRQSPANGHSSTNNSVSDLPSTTQPKGRQIYVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPELQEWRVACIAMEKTKQEQQASCTWFGKKKKQYKDKYLAKHNAVFDQLDLVTYEEVVKLPAFKRKTLVLLGAHGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLETIRKIHEQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPTITPGLNEDESLQRLQKESDILQRTYAHYFDLTIINNEIDETIRHLEEAVELVCTAPQWVPVSWVY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O14936","disprot_id":"DP01438","ncbi_taxon_id":9606,"regions_counter":10,"creator":"bmesza","regions":[{"term_namespace":"Molecular function","ec_ontology":"ECO","end":401,"term_name":"protein binding","released":"2022_12","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Coordinated folding and association of the LIN-2, -7 (L27) domain. An obligate heterodimerization involved in assembly of signaling and cell polarity complexes. <i> Harris BZ, Venkatasubrahmanyam S, Lim WA. </i> J Biol Chem, 2002","statement":[{"text":"The binding and folding events are linked for the LIN-2C:LIN-7 L27 pair; the individual monomers are largely unfolded but become a stable, helical, folded unit upon association.","type":"Results"}],"term_id":"GO:0005515","curator_id":"maspromonte","start":335,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"12110687","version":4,"curator_orcid":"0000-0002-4937-6952","date":"2022-10-27T10:24:57.311Z","reference_source":"pmid","ec_id":"ECO:0006204","cross_refs":[{"db":"PDB","id":"1zl8"}],"region_id":"DP01438r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":460,"region_id":"DP01438r004","released":"2022_12","ec_id":"ECO:0006204","reference_html":"Coordinated folding and association of the LIN-2, -7 (L27) domain. An obligate heterodimerization involved in assembly of signaling and cell polarity complexes. <i> Harris BZ, Venkatasubrahmanyam S, Lim WA. </i> J Biol Chem, 2002","statement":[{"text":"Spectra for L27 monomers (CASK/Lin-2) show little ellipticity at 222 nm, indicating that the individual monomers are largely unfolded.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"maspromonte","start":394,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-4937-6952","date":"2022-10-27T09:21:11.096Z","reference_source":"pmid","term_name":"disorder","reference_id":"12110687","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":460,"term_name":"protein binding","released":"2022_12","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Coordinated folding and association of the LIN-2, -7 (L27) domain. An obligate heterodimerization involved in assembly of signaling and cell polarity complexes. <i> Harris BZ, Venkatasubrahmanyam S, Lim WA. </i> J Biol Chem, 2002","statement":[{"text":"The binding and folding events are linked for the LIN-2C:LIN-7 L27 pair; the individual monomers are largely unfolded but become a stable, helical, folded unit upon association.","type":"Results"}],"term_id":"GO:0005515","curator_id":"maspromonte","start":394,"term_ontology":"GO","curator_name":"Maria Cristina Aspromonte","reference_id":"12110687","version":4,"curator_orcid":"0000-0002-4937-6952","date":"2022-10-27T10:25:18.686Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01438r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":304,"end":337,"reference_id":"34543009","reference_source":"pmid","reference_html":"Design and Development of a Chemical Probe for Pseudokinase Ca<sup>2+</sup>/calmodulin-Dependent Ser/Thr Kinase. <i> Russ N, Schröder M, Berger BT, Mandel S, Aydogan Y, Mauer S, Pohl C, Drewry DH, Chaikuad A, Müller S, Knapp S. </i> J Med Chem, 2021","date":"2023-06-21T13:43:25.569Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":1,"cross_refs":[{"db":"PDB","id":"7OAI"},{"db":"PDB","id":"7OAJ"},{"db":"PDB","id":"7OAK"},{"db":"PDB","id":"7OAL"}],"region_id":"DP01438r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:174"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:155908702"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:155908701"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:71552942"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:155908699"}],"statement":[{"text":"The PDB evidence shows this region lacks electron density, indicating it is disordered","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T13:58:09.122Z"}},{"start":307,"end":337,"reference_id":"20424264","reference_source":"pmid","reference_html":"Evolution of CASK into a Mg2+-sensitive kinase. <i> Mukherjee K, Sharma M, Jahn R, Wahl MC, Südhof TC. </i> Sci Signal, 2010","date":"2023-06-21T13:36:33.702Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000269","ec_ontology":"ECO","ec_name":"experimental evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro22Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To examine whether these additional changes in conserved residues contribute to the loss of Mg2+-coordination in CASK, we reverted Pro22 and His145 to the canonical Ala and Glu residues, respectively, in addition to the initial Gly162Asp and Cys146Asn mutations."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.His145Glu","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To examine whether these additional changes in conserved residues contribute to the loss of Mg2+-coordination in CASK, we reverted Pro22 and His145 to the canonical Ala and Glu residues, respectively, in addition to the initial Gly162Asp and Cys146Asn mutations."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly162Asp","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To examine whether these additional changes in conserved residues contribute to the loss of Mg2+-coordination in CASK, we reverted Pro22 and His145 to the canonical Ala and Glu residues, respectively, in addition to the initial Gly162Asp and Cys146Asn mutations."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys146Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To examine whether these additional changes in conserved residues contribute to the loss of Mg2+-coordination in CASK, we reverted Pro22 and His145 to the canonical Ala and Glu residues, respectively, in addition to the initial Gly162Asp and Cys146Asn mutations."}]}],"cross_refs":[{"db":"PDB","id":"3MFU"},{"db":"PDB","id":"3MFT"},{"db":"PDB","id":"3MFS"},{"db":"PDB","id":"3MFR"}],"region_id":"DP01438r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"47785 ","entry_name":"AMP-PNP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29035","entry_name":"manganese(2+)"}],"statement":[{"text":"The PDB evidence shows this region lacks amminoacid residues 307-337, indicating it is disordered","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T13:56:54.794Z"}},{"start":317,"end":345,"reference_id":"21855798","reference_source":"pmid","reference_html":"Liprin-mediated large signaling complex organization revealed by the liprin-α/CASK and liprin-α/liprin-β complex structures. <i> Wei Z, Zheng S, Spangler SA, Yu C, Hoogenraad CC, Zhang M. </i> Mol Cell, 2011","date":"2022-10-12T13:07:06.312Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":16}],"cross_refs":[{"db":"PDB","id":"3TAC"}],"region_id":"DP01438r009","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75334 "},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"The PDB evidence shows this region lacks electron density, indicating it is disordered","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-27T13:26:56.411Z"}},{"start":305,"end":337,"reference_id":"18423203","reference_source":"pmid","reference_html":"CASK Functions as a Mg2+-independent neurexin kinase. <i> Mukherjee K, Sharma M, Urlaub H, Bourenkov GP, Jahn R, Südhof TC, Wahl MC. </i> Cell, 2008","date":"2023-06-21T13:31:24.467Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":1,"cross_refs":[{"db":"PDB","id":"3C0H"},{"db":"PDB","id":"3C0I"}],"region_id":"DP01438r010","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16027","entry_name":"adenosine 5'-monophosphate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"28931","entry_name":"3'-AMP"}],"statement":[{"text":"Both the P1 and P212121 structures exhibited uninterrupted backbone electron densities throughout the entire domain from residues 5 to 304.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T13:54:55.783Z"}}],"released":"2018_11","uniref100":"UniRef100_O14936","date":"2018-07-17T16:33:20.000Z","acc":"O14936","name":"Peripheral plasma membrane protein CASK","length":926,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI000012853E","genes":[{"name":{"value":"CASK","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:1497","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:1497"}}]},"synonyms":[{"value":"LIN2"}]}],"alphafold_very_low_content":0.15334773218142547,"disorder_content":0.11771058315334773,"disprot_consensus":{"full":[{"start":304,"end":345,"type":"D"},{"start":346,"end":393,"type":"F"},{"start":394,"end":460,"type":"D"}],"Structural state":[{"start":304,"end":345,"type":"D"},{"start":394,"end":460,"type":"D"}],"Molecular function":[{"start":335,"end":460,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00165","name":"Bacterial regulatory helix-turn-helix proteins, AraC family","start":229,"end":267},{"id":"PF22404","name":"ToxT, N-terminal cupin-like domain","start":5,"end":162}],"gene3D":[{"start":212,"end":276,"id":"1.10.10.60","name":"Homeodomain-like"},{"start":165,"end":211,"id":"1.10.10.1310","name":"ToxT, HTH1 motif"},{"start":1,"end":164,"id":"2.60.120.810","name":"2.60.120.810"}]},"uniref50":"UniRef50_A5F384","sequence":"MIGKKSFQTNVYRMSKFDTYIFNNLYINDYKMFWIDSGIAKLIDKNCLVSYEINSSSIILLKKNSIQRFSLTSLSDENINVSVITISDSFIRSLKSYILGDLMIRNLYSENKDLLLWNCEHNDIAVLSEVVNGFREINYSDEFLKVFFSGFFSKVEKKYNSIFITDDLDAMEKISCLVKSDITRNWRWADICGELRTNRMILKKELESRGVKFRELINSIRISYSISLMKTGEFKIKQIAYQSGFASVSYFSTVFKSTMNVAPSEYLFMLTGVAEK","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Vibrionales","Vibrionaceae","Vibrio"],"uniref90":"UniRef90_A5F384","disprot_id":"DP01439","ncbi_taxon_id":345073,"regions_counter":3,"creator":"nfarahi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":110,"region_id":"DP01439r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of Vibrio cholerae ToxT reveals a mechanism for fatty acid regulation of virulence genes. <i> Lowden MJ, Skorupski K, Pellegrini M, Chiorazzo MG, Taylor RK, Kull FJ. </i> Proc Natl Acad Sci U S A, 2010","statement":[{"text":"Helix α1 and sheet β9 are linked by a disordered region between residues 101 and 110","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jmanso","start":101,"term_ontology":"IDPO","curator_name":"Jose A Manso","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3GBG"}],"reference_id":"20133655","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-12T11:24:31.554Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":101,"end":109,"reference_id":"25422303","reference_source":"pmid","reference_html":"A small unstructured region in Vibrio cholerae ToxT mediates the response to positive and negative effectors and ToxT proteolysis. <i> Thomson JJ, Plecha SC, Withey JH. </i> J Bacteriol, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000048","term_name":"limited proteolysis display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01439r002","statement":[{"text":"The solved crystal structure of ToxT revealed an unstructured region in the N-terminal domain between residues 100 and 110. This region and the surrounding amino acids have been previously implicated in ToxT proteolysis, resistance to inhibition by negative effectors, and ToxT dimerization. To better characterize this region, site-directed mutagenesis was performed to assess the effects on ToxT proteolysis and bile sensitivity. This analysis identified specific mutations within this unstructured region that prevent ToxT proteolysis and other mutations that reduce inhibition by bile and unsaturated fatty acids.","type":"Abstract"},{"text":"To further characterize this region in regard to these roles, we performed site-directed alanine mutagenesis of ToxT amino acids 100 to 109, shown in Fig. 1.","type":"Results"},{"text":"The previously described degradation intermediate of ToxT (24) was present in cell extracts from strains carrying each of the mutations in the unstructured region between amino acids 100 and 109 except for the G100A and M103A mutant strains (Fig. 2A). Densitometry was performed using ImageJ software (Fig. 2B) and revealed that the L107A and S109A mutants also had decreased levels of degradation compared to the results for the WT. Mutations I104A and R105A resulted in increased degradation of ToxT, possibly due to decreased ToxT stability. The identification of mutations in this region affecting ToxT proteolysis both confirms previous work demonstrating the importance of amino acids 100 to 109 and pinpoints amino acids 100 and 103 as crucial for ToxT proteolysis.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:04:59.313Z"},"ec_go":"IMP","disprot_namespace":"Disorder function"},{"start":101,"end":110,"reference_id":"25422303","reference_source":"pmid","reference_html":"A small unstructured region in Vibrio cholerae ToxT mediates the response to positive and negative effectors and ToxT proteolysis. <i> Thomson JJ, Plecha SC, Withey JH. </i> J Bacteriol, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01439r003","statement":[{"text":"The solved crystal structure of ToxT revealed an unstructured region in the N-terminal domain between residues 100 and 110. This region and the surrounding amino acids have been previously implicated in ToxT proteolysis, resistance to inhibition by negative effectors, and ToxT dimerization. To better characterize this region, site-directed mutagenesis was performed to assess the effects on ToxT proteolysis and bile sensitivity. This analysis identified specific mutations within this unstructured region that prevent ToxT proteolysis and other mutations that reduce inhibition by bile and unsaturated fatty acids.","type":"Abstract"},{"text":"As was observed in the bile experiments, mutation of residues 100 to 104, 107, and 108 caused decreased overall transcriptional activity with and without added effector. Also, the D101A, I104A, and Y108A mutants had increased sensitivity to linoleic acid, as we had observed with bile. ","type":"Results"},{"text":"This analysis revealed ToxT mutations (G100A, D101A, I104A, Y108A, and E110A) that caused greater sensitivity to the negative effect of bile.","type":"Results"},{"text":"ToxT alanine substitutions at amino acids 100 to 104, 107, and 108 caused decreased overall ToxT activity, as we observed in the bile/UFA experiments described above. Additionally, mutation of S109 and E110 caused slight decreases in overall activity compared to that of the WT. The L107A mutant was completely inactive, and bicarbonate had no activating effect on this variant of ToxT. Bicarbonate increased the activity of WT MBP-ToxT 2.6-fold in these experiments (Fig. 5). ToxT G100A, D101A, M103A, I104A, and Y108A mutants all had an increased response to the activating effect of bicarbonate. ","type":"Results"},{"text":"These results suggest that the same ToxT residues within the unstructured region from amino acid 100 to 109 may be involved in the response to both positive and negative effectors.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:04:57.181Z"},"ec_go":"IMP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_A5F384","date":"2018-07-17T17:24:28.000Z","acc":"A5F384","name":"TCP pilus virulence regulatory protein","length":276,"organism":"Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)","dataset":["Bacterial virulence-related proteins"],"UniParc":"UPI0000000A93","genes":[{"name":{"value":"tcpN"},"synonyms":[{"value":"toxT"}],"olnNames":[{"value":"VC0395_A0363"},{"value":"VC395_0854"}]}],"alphafold_very_low_content":0.014492753623188406,"disorder_content":0.036231884057971016,"disprot_consensus":{"full":[{"start":101,"end":110,"type":"D"}],"Structural state":[{"start":101,"end":110,"type":"D"}],"Disorder function":[{"start":101,"end":109,"type":"F"}],"Molecular function":[{"start":101,"end":110,"type":"F"}]}},{"features":{"pfam":[{"id":"PF12949","name":"HeH/LEM domain","start":86,"end":118},{"id":"PF17891","name":"Mu-like prophage FluMu N-terminal domain","start":7,"end":54}],"gene3D":[{"start":1,"end":54,"id":"3.40.5.80","name":"3.40.5.80"}]},"uniref50":"UniRef50_P44228","sequence":"MDKTFCVVVQNRIKEGYRRAGFSFHLGDNSLAAVSESQLAQLKADPRLVVQITETGSQEGGEGLSKEPAGSDEQKQLRADPPSTDLNTFTVEQLKAQLTERGITFKQSATKAELIALFAPADGEKSEA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Pasteurellales","Pasteurellaceae","Haemophilus"],"uniref90":"UniRef90_P44228","disprot_id":"DP01440","ncbi_taxon_id":71421,"regions_counter":4,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":28,"region_id":"DP01440r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of HI1506, a novel two-domain protein from Haemophilus influenzae. <i> Sari N, He Y, Doseeva V, Surabian K, Ramprakash J, Schwarz F, Herzberg O, Orban J. </i> Protein Sci, 2007","statement":[{"text":"\"Residues at the N terminus (residues 1–7) and at the C terminus (residues 121–131) are unstructured, as evidenced by a low number of inter-residue NOEs.\"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":12,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2OUT"}],"reference_id":"17400915","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":28,"term_name":"DNA binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Solution structure of HI1506, a novel two-domain protein from Haemophilus influenzae. <i> Sari N, He Y, Doseeva V, Surabian K, Ramprakash J, Schwarz F, Herzberg O, Orban J. </i> Protein Sci, 2007","statement":[{"text":"\"In conclusion, the structure of HI1506 reveals a novel two-domain conformation, in which each domain contains a significant contiguous area of positively charged surface. For both the N- and C-domains, some of the more closely related structures are associated with an RNA binding function.\"","type":"Results"}],"term_id":"GO:0003677","curator_id":"amonzon","start":12,"term_ontology":"GO","curator_name":"Alex Monzon","reference_id":"17400915","version":3,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01440r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":84,"region_id":"DP01440r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of HI1506, a novel two-domain protein from Haemophilus influenzae. <i> Sari N, He Y, Doseeva V, Surabian K, Ramprakash J, Schwarz F, Herzberg O, Orban J. </i> Protein Sci, 2007","statement":[{"text":"\"The solution structure of HI1506 consists of two structured domains connected by an unstructured 30 amino acid loop\"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":54,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2OUT"}],"reference_id":"17400915","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":84,"term_name":"DNA binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Solution structure of HI1506, a novel two-domain protein from Haemophilus influenzae. <i> Sari N, He Y, Doseeva V, Surabian K, Ramprakash J, Schwarz F, Herzberg O, Orban J. </i> Protein Sci, 2007","statement":[{"text":"\"In conclusion, the structure of HI1506 reveals a novel two-domain conformation, in which each domain contains a significant contiguous area of positively charged surface. For both the N- and C-domains, some of the more closely related structures are associated with an RNA binding function.\"","type":"Results"}],"term_id":"GO:0003677","curator_id":"amonzon","start":54,"term_ontology":"GO","curator_name":"Alex Monzon","reference_id":"17400915","version":3,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01440r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P44228","date":"2018-07-17T17:41:36.000Z","acc":"P44228","name":"Mu-like prophage FluMu protein gp35","length":128,"organism":"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","dataset":[],"UniParc":"UPI0000138559","genes":[{"olnNames":[{"value":"HI_1506/HI_1507"}]}],"alphafold_very_low_content":0.2734375,"disorder_content":0.375,"disprot_consensus":{"full":[{"start":12,"end":28,"type":"D"},{"start":54,"end":84,"type":"D"}],"Structural state":[{"start":12,"end":28,"type":"D"},{"start":54,"end":84,"type":"D"}],"Molecular function":[{"start":12,"end":28,"type":"F"},{"start":54,"end":84,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00178","name":"Ets-domain","start":335,"end":415},{"id":"PF02198","name":"Sterile alpha motif (SAM)/Pointed domain","start":54,"end":135},{"id":"PF19525","name":"Ets1 N-terminal flanking region of Ets domain","start":148,"end":332}],"gene3D":[{"start":42,"end":138,"id":"1.10.150.50","name":"Transcription Factor, Ets-1"},{"start":297,"end":436,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}]},"uniref50":"UniRef50_P14921","sequence":"MKAAVDLKPTLTIIKTEKVDLELFPSPDMECADVPLLTPSSKEMMSQALKATFSGFTKEQQRLGIPKDPRQWTETHVRDWVMWAVNEFSLKGVDFQKFCMNGAALCALGKDCFLELAPDFVGDILWEHLEILQKEDVKPYQVNGVNPAYPESRYTSDYFISYGIEHAQCVPPSEFSEPSFITESYQTLHPISSEELLSLKYENDYPSVILRDPLQTDTLQNDYFAIKQEVVTPDNMCMGRTSRGKLGGQDSFESIESYDSCDRLTQSWSSQSSFNSLQRVPSYDSFDSEDYPAALPNHKPKGTFKDYVRDRADLNKDKPVIPAAALAGYTGSGPIQLWQFLLELLTDKSCQSFISWTGDGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTAGKRYVYRFVCDLQSLLGYTPEELHAMLDVKPDADE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P14921","disprot_id":"DP01441","ncbi_taxon_id":9606,"regions_counter":2,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":318,"region_id":"DP01441r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"A novel allosteric mechanism on protein-DNA interactions underlying the phosphorylation-dependent regulation of Ets1 target gene expressions. <i> Shiina M, Hamada K, Inoue-Bungo T, Shimamura M, Uchiyama A, Baba S, Sato K, Yamamoto M, Ogata K. </i> J Mol Biol, 2015","statement":[{"text":"The conformation of the inhibitory module of Ets1 in (Ets1)2–DNA and Ets1–Pax5–DNA complexes, which do not contain Runx1, resembled that of free Ets1, although HI-1 was disordered","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jmanso","start":276,"term_ontology":"IDPO","curator_name":"Jose A Manso","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3WTS"}],"reference_id":"25083921","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":318,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"A novel allosteric mechanism on protein-DNA interactions underlying the phosphorylation-dependent regulation of Ets1 target gene expressions. <i> Shiina M, Hamada K, Inoue-Bungo T, Shimamura M, Uchiyama A, Baba S, Sato K, Yamamoto M, Ogata K. </i> J Mol Biol, 2015","statement":[{"text":"CaMKII-catalyzed phosphorylation of Ets1 in a\nserine-rich region of the N-terminal extension of HI-1\nis known to stabilize the inhibitory hydrophobic core\n(Fig. 1b, f, and j), resulting in a 50- to 1000-fold\nreduction in its affinity for DNA","type":"Results"}],"term_id":"GO:0003676","curator_id":"jmanso","start":276,"term_ontology":"GO","curator_name":"Jose A Manso","reference_id":"25083921","version":3,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01441r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P14921","date":"2018-07-17T19:01:48.000Z","acc":"P14921","name":"Protein C-ets-1","length":441,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012A268","genes":[{"name":{"value":"ETS1"},"synonyms":[{"value":"EWSR2"}]}],"alphafold_very_low_content":0.45351473922902497,"disorder_content":0.09750566893424037,"disprot_consensus":{"full":[{"start":276,"end":318,"type":"D"}],"Structural state":[{"start":276,"end":318,"type":"D"}],"Molecular function":[{"start":276,"end":318,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04927","name":"Seed maturation protein","start":16,"end":70},{"id":"PF04927","name":"Seed maturation protein","start":133,"end":189},{"id":"PF04927","name":"Seed maturation protein","start":197,"end":255}]},"uniref50":"UniRef50_P09444","sequence":"MSQEQPRRPQAGQDPIKYGDVLPVSGDLSQKPITPEDAAMMQSAESRVLGQTQPGGVASVMQSAATRNEQAGIVGHKDVTDVTGDRGVTVTETQVPGRRIITETVGGQVVGQFVEPTPVQVGLTGAVRESALTIGEALEATAHTVGDKPVEQSDASAIQAAEVRATGSNVITPGGLASMAQSAAAFNAECQREEEKIKMGNVLTGATAKLPADKAATRQDAAGVASAEMRNNPDATATPGGVAASVAAAARLNENVGNVM","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","fabids","Fabales","Fabaceae","Papilionoideae","50 kb inversion clade","NPAAA clade","Hologalegina","IRL clade","Trifolieae","Medicago"],"uniref90":"UniRef90_A0A1S2XYX3","disprot_id":"DP01442","ncbi_taxon_id":3880,"regions_counter":8,"creator":"achasapi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":260,"region_id":"DP01442r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"MtPM25 is an atypical hydrophobic late embryogenesis-abundant protein that dissociates cold and desiccation-aggregated proteins. <i> Boucher V, Buitink J, Lin X, Boudet J, Hoekstra FA, Hundertmark M, Renard D, Leprince O. </i> Plant Cell Environ, 2010","statement":[{"text":"Inspection of the spectrum (Fig. 1a) shows a negative peak at 200 nm, which is indicative of a highly unfolded protein in a random coil structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"achasapi","start":1,"term_ontology":"IDPO","curator_name":"Anastasia Chasapi","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1986-5007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20002332","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-02-05T16:05:12.802Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":260,"region_id":"DP01442r002","released":"2024_06","ec_id":"ECO:0006228","reference_html":"Comparative analysis of the heat stable proteome of radicles of Medicago truncatula seeds during germination identifies late embryogenesis abundant proteins associated with desiccation tolerance. <i> Boudet J, Buitink J, Hoekstra FA, Rogniaux H, Larré C, Satour P, Leprince O. </i> Plant Physiol, 2006","statement":[{"text":"Superficial inspection of the IR spectrum in the amide-I region (Fig. 9) revealed that in D2O the proteins displayed a broadened band at a wavenumber position (1,460 cm−1) that was lower than in the case of the fast-dried proteins (1,550 cm−1). This behavior in D2O may be partly due to 2H exchange with protons in the protein backbone, which is particularly likely in unordered structures (Raussens et al., 1997).","type":"Results"},{"text":"Apparently, the amide protons (N-H) were, to a considerable extent, open for 2H exchange from D2O, which is interpreted to mean that both proteins have a fairly unordered structure in water (Haris et al., 1989).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-05T15:59:56.929Z","reference_source":"pmid","term_name":"disorder","reference_id":"16461389","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"41981","entry_name":"dideuterium oxide"}]},{"start":1,"end":260,"reference_id":"16461389","reference_source":"pmid","reference_html":"Comparative analysis of the heat stable proteome of radicles of Medicago truncatula seeds during germination identifies late embryogenesis abundant proteins associated with desiccation tolerance. <i> Boudet J, Buitink J, Hoekstra FA, Rogniaux H, Larré C, Satour P, Leprince O. </i> Plant Physiol, 2006","date":"2024-02-05T16:01:47.652Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01442r003","statement":[{"text":" In contrast to MtEm6, MtPM25 tended to form extended β sheets upon slow drying, which appeared to be reversible upon rehydration. When indicated as percentages of α helix, β sheet, and unordered structures, MtEm6 consisted of 57%, 12%, and 31%, and 60%, 8%, and 32%, after fast and slow drying, respectively. Data for MtPM25 were 54%, 17%, and 29%, and 56%, 25%, and 19%, respectively.","type":"Results"},{"text":"The removal of the water induced a transition from a fairly disordered conformation to the formation of a considerable amount of ordered structures (Table IV).","type":"Discussion"}]},{"start":1,"end":260,"reference_id":"20002332","reference_source":"pmid","reference_html":"MtPM25 is an atypical hydrophobic late embryogenesis-abundant protein that dissociates cold and desiccation-aggregated proteins. <i> Boucher V, Buitink J, Lin X, Boudet J, Hoekstra FA, Hundertmark M, Renard D, Leprince O. </i> Plant Cell Environ, 2010","date":"2024-02-05T16:41:18.094Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0050821","term_name":"protein stabilization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","region_id":"DP01442r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P13491"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P13490"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P00889"}],"statement":[{"text":"Figure 3a shows that PM25 is a potent stabilizer of LDH during three cycles of freezing/thawing in a concentration dependent fashion. The enzyme activity is completely recovered at a mass ratio (PM25 : enzyme) of 6:1. In contrast, EM6 was mildly efficient regardless as to whether data were expressed on mass ratio (Fig. 3a) or molar ratio (EM6 being ca. half the weight of PM25) whereas lyzozyme is almost ineffective.","type":"Results"},{"text":"PM25 stabilizes proteins in aggregation assays more efficiently than EM6","type":"Results"},{"text":"Figure 3e shows that both PM25 and EM6 could offer a partial protection to CS against drying in a concentration dependent manner, as previously described for other LEA proteins (Goyal et al. 2005; Gilles et al. 2007). Again, PM25 was more efficient at protecting CS from drying than EM6.","type":"Results"}],"term_comment":"","term_def":"\"Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":260,"reference_id":"20002332","reference_source":"pmid","reference_html":"MtPM25 is an atypical hydrophobic late embryogenesis-abundant protein that dissociates cold and desiccation-aggregated proteins. <i> Boucher V, Buitink J, Lin X, Boudet J, Hoekstra FA, Hundertmark M, Renard D, Leprince O. </i> Plant Cell Environ, 2010","date":"2024-02-05T16:34:20.814Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0035617","term_name":"stress granule disassembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006307","ec_ontology":"ECO","ec_name":"turbidity measurement evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","region_id":"DP01442r005","statement":[{"text":"Figure 5a shows that the addition of PM25 to the water SP after thawing leads to a significant decrease in turbidity compared with water controls, suggesting that PM25 is able to dissolve aggregates formed after two successive freeze–thawing cycles.","type":"Results"}],"term_comment":"","term_def":"\"The disaggregation of a stress granule into its constituent protein and RNA parts.\" [GOC:BHF, PMID:19825938]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":260,"reference_id":"20002332","reference_source":"pmid","reference_html":"MtPM25 is an atypical hydrophobic late embryogenesis-abundant protein that dissociates cold and desiccation-aggregated proteins. <i> Boucher V, Buitink J, Lin X, Boudet J, Hoekstra FA, Hundertmark M, Renard D, Leprince O. </i> Plant Cell Environ, 2010","date":"2024-02-05T16:38:16.728Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0035617","term_name":"stress granule disassembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007684","ec_ontology":"ECO","ec_name":"protein separation evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","region_id":"DP01442r006","statement":[{"text":"Figure 5a shows that the addition of PM25 to the water SP after thawing leads to a significant decrease in turbidity compared with water controls, suggesting that PM25 is able to dissolve aggregates formed after two successive freeze–thawing cycles.","type":"Results"},{"text":"PM25 dissolves stress-induced aggregates of water-soluble proteins upon thawing and rehydration","type":"Results"}],"term_comment":"","term_def":"\"The disaggregation of a stress granule into its constituent protein and RNA parts.\" [GOC:BHF, PMID:19825938]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":260,"reference_id":"20002332","reference_source":"pmid","reference_html":"MtPM25 is an atypical hydrophobic late embryogenesis-abundant protein that dissociates cold and desiccation-aggregated proteins. <i> Boucher V, Buitink J, Lin X, Boudet J, Hoekstra FA, Hundertmark M, Renard D, Leprince O. </i> Plant Cell Environ, 2010","date":"2024-02-05T16:40:37.869Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0050821","term_name":"protein stabilization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006317","ec_ontology":"ECO","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","region_id":"DP01442r007","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P00889"}],"statement":[{"text":"Next, we assessed whether PM25 behaved like a chaperone using a standard thermally-induced unfolding assay with CS. The inactivation kinetics experiment shows that during heating at 43 °C, CS lost virtually all activity within 20 min, whereas the presence of PM25 significantly retarded the loss of the activity early during heating (Fig. 3b).","type":"Results"},{"text":"This suggests that PM25 stabilizes CS against heating by acting on certain intermediates that are transiently formed during heating, but not on the denatured enzyme.","type":"Results"}],"term_comment":"","term_def":"\"Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":260,"reference_id":"20002332","reference_source":"pmid","reference_html":"MtPM25 is an atypical hydrophobic late embryogenesis-abundant protein that dissociates cold and desiccation-aggregated proteins. <i> Boucher V, Buitink J, Lin X, Boudet J, Hoekstra FA, Hundertmark M, Renard D, Leprince O. </i> Plant Cell Environ, 2010","date":"2024-02-05T16:44:44.775Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0035617","term_name":"stress granule disassembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","region_id":"DP01442r008","statement":[{"text":" Adding PM25 upon thawing resulted in the disappearance of the aggregates, with those remaining being much smaller and of different morphology (Fig. 6d). Also, no coacervate was observed in the thawed solution in the presence of PM25. We assayed the effect of PM25 on the size distribution of the aggregates using light microscopy because they were too large to be analysed by light scattering. Figure 6e confirms that PM25 is able to reduce both the average surface area and the size distribution by one and seven orders of magnitude, respectively.","type":"Results"}],"term_comment":"","term_def":"\"The disaggregation of a stress granule into its constituent protein and RNA parts.\" [GOC:BHF, PMID:19825938]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_Q2Q4X9","date":"2018-07-17T21:17:27.000Z","acc":"Q2Q4X9","name":"Seed maturation protein","length":260,"organism":"Medicago truncatula","dataset":[],"UniParc":"UPI000067B2DF","genes":[{"name":{"value":"PM25","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ABB16353.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABB16353.1"}}]}}],"alphafold_very_low_content":0.11923076923076924,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":260,"type":"T"}],"Structural state":[{"start":1,"end":260,"type":"D"}],"Structural transition":[{"start":1,"end":260,"type":"T"}],"Biological process":[{"start":1,"end":260,"type":"F"}]}},{"features":{"pfam":[{"id":"PF12862","name":"Anaphase-promoting complex subunit 5","start":254,"end":353},{"id":"PF12862","name":"Anaphase-promoting complex subunit 5","start":458,"end":490},{"id":"PF21371","name":"Anaphase-promoting complex subunit 5, N-terminal domain","start":23,"end":169},{"id":"PF29127","name":"Suppressor of spindle checkpoint defect 1 C-terminal domain","start":547,"end":746}],"gene3D":[{"start":514,"end":741,"id":"1.25.40.10","name":"Tetratricopeptide repeat domain"}]},"uniref50":"UniRef50_Q9UJX4","sequence":"MASVHESLYFNPMMTNGVVHANVFGIKDWVTPYKIAVLVLLNEMSRTGEGAVSLMERRRLNQLLLPLLQGPDITLSKLYKLIEESCPQLANSVQIRIKLMAEGELKDMEQFFDDLSDSFSGTEPEVHKTSVVGLFLRHMILAYSKLSFSQVFKLYTALQQYFQNGEKKTVEDADMELTSRDEGERKMEKEELDVSVREEEVSCSGPLSQKQAEFFLSQQASLLKNDETKALTPASLQKELNNLLKFNPDFAEAHYLSYLNNLRVQDVFSSTHSLLHYFDRLILTGAESKSNGEEGYGRSLRYAALNLAALHCRFGHYQQAELALQEAIRIAQESNDHVCLQHCLSWLYVLGQKRSDSYVLLEHSVKKAVHFGLPYLASLGIQSLVQQRAFAGKTANKLMDALKDSDLLHWKHSLSELIDISIAQKTAIWRLYGRSTMALQQAQMLLSMNSLEAVNAGVQQNNTESFAVALCHLAELHAEQGCFAAASEVLKHLKERFPPNSQHAQLWMLCDQKIQFDRAMNDGKYHLADSLVTGITALNSIEGVYRKAVVLQAQNQMSEAHKLLQKLLVHCQKLKNTEMVISVLLSVAELYWRSSSPTIALPMLLQALALSKEYRLQYLASETVLNLAFAQLILGIPEQALSLLHMAIEPILADGAILDKGRAMFLVAKCQVASAASYDQPKKAEALEAAIENLNEAKNYFAKVDCKERIRDVVYFQARLYHTLGKTQERNRCAMLFRQLHQELPSHGVPLINHL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UJX4","disprot_id":"DP01443","ncbi_taxon_id":9606,"regions_counter":5,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":26,"region_id":"DP01443r001","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The regions are detailed in the Extended Data Table 2.","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":1,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":24,"region_id":"DP01443r002","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Molecular mechanism of APC/C activation by mitotic phosphorylation. <i> Zhang S, Chang L, Alfieri C, Zhang Z, Yang J, Maslen S, Skehel M, Barford D. </i> Nature, 2016","term_id":"IDPO:0000002","curator_id":"amonzon","start":1,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5G05"},{"db":"PDB","id":"5G04"}],"reference_id":"27120157","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":205,"region_id":"DP01443r003","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","term_id":"IDPO:0000002","curator_id":"amonzon","start":168,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5G05"},{"db":"PDB","id":"5G04"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":205,"region_id":"DP01443r004","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The regions are detailed in the Extended Data Table 2.","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":170,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":413,"region_id":"DP01443r005","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Cryo-EM of Mitotic Checkpoint Complex-Bound APC/C Reveals Reciprocal and Conformational Regulation of Ubiquitin Ligation. <i> Yamaguchi M, VanderLinden R, Weissmann F, Qiao R, Dube P, Brown NG, Haselbach D, Zhang W, Sidhu SS, Peters JM, Stark H, Schulman BA. </i> Mol Cell, 2016","statement":[{"text":"Figure S5. Missing electron density, conformational flexibility.","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":353,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5KHU"},{"db":"PDB","id":"5KHR"}],"reference_id":"27522463","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9UJX4","date":"2018-07-17T21:27:10.000Z","acc":"Q9UJX4","name":"Anaphase-promoting complex subunit 5","length":755,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000716C8","genes":[{"name":{"value":"ANAPC5"},"synonyms":[{"value":"APC5"}]}],"alphafold_very_low_content":0.09668874172185431,"disorder_content":0.16556291390728478,"disprot_consensus":{"full":[{"start":1,"end":26,"type":"D"},{"start":168,"end":205,"type":"D"},{"start":353,"end":413,"type":"D"}],"Structural state":[{"start":1,"end":26,"type":"D"},{"start":168,"end":205,"type":"D"},{"start":353,"end":413,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00515","name":"Tetratricopeptide repeat","start":567,"end":600},{"id":"PF00515","name":"Tetratricopeptide repeat","start":636,"end":667},{"id":"PF12895","name":"Anaphase-promoting complex, cyclosome, subunit 3","start":17,"end":93},{"id":"PF13181","name":"Tetratricopeptide repeat","start":601,"end":634},{"id":"PF13181","name":"Tetratricopeptide repeat","start":672,"end":702}],"gene3D":[{"start":455,"end":531,"id":"1.25.40.10","name":"Tetratricopeptide repeat domain"},{"start":1,"end":171,"id":"1.25.40.10","name":"Tetratricopeptide repeat domain"},{"start":532,"end":664,"id":"1.25.40.10","name":"Tetratricopeptide repeat domain"},{"start":665,"end":768,"id":"1.25.40.10","name":"Tetratricopeptide repeat domain"}]},"uniref50":"UniRef50_P30260","sequence":"MTVLQEPVQAAIWQALNHYAYRDAVFLAERLYAEVHSEEALFLLATCYYRSGKAYKAYRLLKGHSCTTPQCKYLLAKCCVDLSKLAEGEQILSGGVFNKQKSHDDIVTEFGDSACFTLSLLGHVYCKTDRLAKGSECYQKSLSLNPFLWSPFESLCEIGEKPDPDQTFKFTSLQNFSNCLPNSCTTQVPNHSLSHRQPETVLTETPQDTIELNRLNLESSNSKYSLNTDSSVSYIDSAVISPDTVPLGTGTSILSKQVQNKPKTGRSLLGGPAALSPLTPSFGILPLETPSPGDGSYLQNYTNTPPVIDVPSTGAPSKKSVARIGQTGTKSVFSQSGNSREVTPILAQTQSSGPQTSTTPQVLSPTITSPPNALPRRSSRLFTSDSSTTKENSKKLKMKFPPKIPNRKTKSKTNKGGITQPNINDSLEITKLDSSIISEGKISTITPQIQAFNLQKAAAEGLMSLLREMGKGYLALCSYNCKEAINILSHLPSHHYNTGWVLCQIGRAYFELSEYMQAERIFSEVRRIENYRVEGMEIYSTTLWHLQKDVALSVLSKDLTDMDKNSPEAWCAAGNCFSLQREHDIAIKFFQRAIQVDPNYAYAYTLLGHEFVLTEELDKALACFRNAIRVNPRHYNAWYGLGMIYYKQEKFSLAEMHFQKALDINPQSSVLLCHIGVVQHALKKSEKALDTLNKAIVIDPKNPLCKFHRASVLFANEKYKSALQELEELKQIVPKESLVYFLIGKVYKKLGQTHLALMNFSWAMDLDPKGANNQIKEAIDKRYLPDDEEPITQEEQIMGTDESQESSMTDADDTQLHAAESDEF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P30260","disprot_id":"DP01445","ncbi_taxon_id":9606,"regions_counter":4,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":450,"region_id":"DP01445r001","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The regions are detailed in the Extended Data Table 2","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":171,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"},{"db":"PDB","id":"5A31"},{"db":"PDB","id":"5G05"},{"db":"PDB","id":"5G04"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":824,"region_id":"DP01445r002","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The regions are detailed in the Extended Data Table 2","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":767,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"},{"db":"PDB","id":"5A31"},{"db":"PDB","id":"5G05"},{"db":"PDB","id":"5G04"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":447,"region_id":"DP01445r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of an APC3-APC16 complex: insights into assembly of the anaphase-promoting complex/cyclosome. <i> Yamaguchi M, Yu S, Qiao R, Weissmann F, Miller DJ, VanderLinden R, Brown NG, Frye JJ, Peters JM, Schulman BA. </i> J Mol Biol, 2015","statement":[{"text":"\"Several  lines of evidence suggested that residues 182-453 are mobile and/or disordered, and not part of the signature TPR folded region of human APC3\"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":180,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4RG6"},{"db":"PDB","id":"4RG7"},{"db":"PDB","id":"4RG9"}],"reference_id":"25490258","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":824,"region_id":"DP01445r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of an APC3-APC16 complex: insights into assembly of the anaphase-promoting complex/cyclosome. <i> Yamaguchi M, Yu S, Qiao R, Weissmann F, Miller DJ, VanderLinden R, Brown NG, Frye JJ, Peters JM, Schulman BA. </i> J Mol Biol, 2015","statement":[{"text":"\"...the subsequent residues 775-830 are not visible in the electron density and are presumably disordered\"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":769,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4RG6"},{"db":"PDB","id":"4RG7"},{"db":"PDB","id":"4RG9"}],"reference_id":"25490258","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P30260","date":"2018-07-17T21:51:12.000Z","acc":"P30260","name":"Cell division cycle protein 27 homolog","length":824,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000016AE00","genes":[{"name":{"value":"CDC27"},"synonyms":[{"value":"ANAPC3"},{"value":"D0S1430E"},{"value":"D17S978E"}]}],"alphafold_very_low_content":0.37985436893203883,"disorder_content":0.41019417475728154,"disprot_consensus":{"full":[{"start":171,"end":450,"type":"D"},{"start":767,"end":824,"type":"D"}],"Structural state":[{"start":171,"end":450,"type":"D"},{"start":767,"end":824,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00619","name":"Caspase recruitment domain","start":21,"end":98},{"id":"PF05729","name":"NACHT domain","start":197,"end":367},{"id":"PF13516","name":"Leucine Rich repeat","start":730,"end":749},{"id":"PF13516","name":"Leucine Rich repeat","start":786,"end":805},{"id":"PF13516","name":"Leucine Rich repeat","start":821,"end":833},{"id":"PF13516","name":"Leucine Rich repeat","start":839,"end":861},{"id":"PF17776","name":"NLRC4 helical domain HD2","start":517,"end":666},{"id":"PF17779","name":"NOD2 winged helix domain","start":458,"end":515}],"gene3D":[{"start":675,"end":860,"id":"3.80.10.10","name":"Ribonuclease Inhibitor"},{"start":861,"end":946,"id":"3.80.10.10","name":"Ribonuclease Inhibitor"},{"start":9,"end":106,"id":"1.10.533.10","name":"Death Domain, Fas"},{"start":122,"end":302,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_Q9Y239","sequence":"MEEQGHSEMEIIPSESHPHIQLLKSNRELLVTHIRNTQCLVDNLLKNDYFSAEDAEIVCACPTQPDKVRKILDLVQSKGEEVSEFFLYLLQQLADAYVDLRPWLLEIGFSPSLLTQSKVVVNTDPVSRYTQQLRHHLGRDSKFVLCYAQKEELLLEEIYMDTIMELVGFSNESLGSLNSLACLLDHTTGILNEQGETIFILGDAGVGKSMLLQRLQSLWATGRLDAGVKFFFHFRCRMFSCFKESDRLCLQDLLFKHYCYPERDPEEVFAFLLRFPHVALFTFDGLDELHSDLDLSRVPDSSCPWEPAHPLVLLANLLSGKLLKGASKLLTARTGIEVPRQFLRKKVLLRGFSPSHLRAYARRMFPERALQDRLLSQLEANPNLCSLCSVPLFCWIIFRCFQHFRAAFEGSPQLPDCTMTLTDVFLLVTEVHLNRMQPSSLVQRNTRSPVETLHAGRDTLCSLGQVAHRGMEKSLFVFTQEEVQASGLQERDMQLGFLRALPELGPGGDQQSYEFFHLTLQAFFTAFFLVLDDRVGTQELLRFFQEWMPPAGAATTSCYPPFLPFQCLQGSGPAREDLFKNKDHFQFTNLFLCGLLSKAKQKLLRHLVPAAALRRKRKALWAHLFSSLRGYLKSLPRVQVESFNQVQAMPTFIWMLRCIYETQSQKVGQLAARGICANYLKLTYCNACSADCSALSFVLHHFPKRLALDLDNNNLNDYGVRELQPCFSRLTVLRLSVNQITDGGVKVLSEELTKYKIVTYLGLYNNQITDVGARYVTKILDECKGLTHLKLGKNKITSEGGKYLALAVKNSKSISEVGMWGNQVGDEGAKAFAEALRNHPSLTTLSLASNGISTEGGKSLARALQQNTSLEILWLTQNELNDEVAESLAEMLKVNQTLKHLWLIQNQITAKGTAQLADALQSNTGITEICLNGNLIKPEEAKVYEDEKRIICF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9Y239","disprot_id":"DP01446","ncbi_taxon_id":9606,"regions_counter":1,"creator":"bmesza","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":138,"region_id":"DP01446r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of NOD1 CARD and mutational analysis of its interaction with the CARD of downstream kinase RICK. <i> Manon F, Favier A, Núñez G, Simorre JP, Cusack S. </i> J Mol Biol, 2007","statement":[{"text":"Residues 111–138 of NOD1 are located in an unstructured carboxy-terminal extension where unfavourable dynamic properties resulted in a low signal to noise in the NMR spectra.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":111,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2B1W"}],"reference_id":"17054981","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9Y239","date":"2018-07-17T21:51:31.000Z","acc":"Q9Y239","name":"Nucleotide-binding oligomerization domain-containing protein 1","length":953,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000375EE","genes":[{"name":{"value":"NOD1"},"synonyms":[{"value":"CARD4"}]}],"alphafold_very_low_content":0.07555089192025184,"disorder_content":0.02938090241343127,"disprot_consensus":{"full":[{"start":111,"end":138,"type":"D"}],"Structural state":[{"start":111,"end":138,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00134","name":"Cyclin, N-terminal domain","start":27,"end":152},{"id":"PF02984","name":"Cyclin, C-terminal domain","start":157,"end":255}],"gene3D":[{"start":26,"end":247,"id":"1.10.472.10","name":"Cyclin-like"},{"start":41,"end":153,"id":"1.10.472.10","name":"Cyclin-like"}]},"uniref50":"UniRef50_P30281","sequence":"MELLCCEGTRHAPRAGPDPRLLGDQRVLQSLLRLEERYVPRASYFQCVQREIKPHMRKMLAYWMLEVCEEQRCEEEVFPLAMNYLDRYLSCVPTRKAQLQLLGAVCMLLASKLRETTPLTIEKLCIYTDHAVSPRQLRDWEVLVLGKLKWDLAAVIAHDFLAFILHRLSLPRDRQALVKKHAQTFLALCATDYTFAMYPPSMIATGSIGAAVQGLGACSMSGDELTELLAGITGTEVDCLRACQEQIEAALRESLREASQTSSSPAPKAPRGSSSQGPSQTSTPTDVTAIHL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P30281","disprot_id":"DP01447","ncbi_taxon_id":9606,"regions_counter":3,"creator":"bmesza","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":292,"region_id":"DP01447r001","released":"2022_06","ec_id":"ECO:0006220","reference_html":"The structure of CDK4/cyclin D3 has implications for models of CDK activation. <i> Takaki T, Echalier A, Brown NR, Hunt T, Endicott JA, Noble ME. </i> Proc Natl Acad Sci U S A, 2009","statement":[{"text":"The equivalent protein sequence of cyclin D3 (residues 255–C terminus) is not apparent in the electron density, presumably because of disorder.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":255,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"curator_orcid":"0000-0002-0341-4888","date":"2022-06-25T20:30:15.746Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3G33"}],"reference_id":"19237555","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P11802"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T12:40:09.898Z"}},{"start":1,"end":22,"reference_id":"19237555","reference_source":"pmid","reference_html":"The structure of CDK4/cyclin D3 has implications for models of CDK activation. <i> Takaki T, Echalier A, Brown NR, Hunt T, Endicott JA, Noble ME. </i> Proc Natl Acad Sci U S A, 2009","date":"2022-06-25T20:31:53.093Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"3G33"}],"region_id":"DP01447r002","statement":[{"text":"N-terminal region characterized by missing electron density in the crystal structure.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T12:40:11.834Z"}},{"start":281,"end":285,"reference_id":"15252116","reference_source":"pmid","reference_html":"cAMP-induced degradation of cyclin D3 through association with GSK-3beta. <i> Naderi S, Gutzkow KB, Låhne HU, Lefdal S, Ryves WJ, Harwood AJ, Blomhoff HK. </i> J Cell Sci, 2004","date":"2022-07-29T12:08:22.137Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001202","ec_ontology":"ECO","ec_name":"in vitro protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP01447r003","statement":[{"text":"We found that phosphorylation of His-cyclin D3 (wt) in vitro by GSK-3β reached a stoichiometry of approximately 0.6 mol phosphate per mol of His-cyclin D3 (wt) (data not shown), indicating that GSK-3β effectively phosphorylates cyclin D3 in vitro. To determine whether Thr-283 in cyclin D3 is phosphorylated by GSK-3β, a bacterially produced His-tagged cyclin D3 mutant containing an Ala for Thr-283 substitution [His-cyclin D3 (T283A)] was used as a substrate in an in vitro kinase reaction with purified GSK-3β. Fig. 6B shows that GSK-3β phosphorylated His-cyclin D3 (wt) but not His-cyclin D3 (T283A).","type":"Results"},{"text":"Taken together, these results indicate that cyclin D3 is a specific substrate for GSK-3β, and map the site of GSK-3β phosphorylation to Thr-283 in cyclin D3.","type":"Results"}],"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":283,"end":283,"position":"Specific residue"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-29T12:09:34.517Z"}}],"released":"2018_11","uniref100":"UniRef100_P30281","date":"2018-07-17T22:06:26.000Z","acc":"P30281","name":"G1/S-specific cyclin-D3","length":292,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI0000149774","genes":[{"name":{"value":"CCND3","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"1386336","url":"http://www.ncbi.nlm.nih.gov/pubmed/1386336","alternativeUrl":"https://europepmc.org/abstract/MED/1386336"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:1585","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:1585"}}]}}],"alphafold_very_low_content":0.10273972602739725,"disorder_content":0.2054794520547945,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"},{"start":255,"end":292,"type":"D"}],"Structural state":[{"start":1,"end":22,"type":"D"},{"start":255,"end":292,"type":"D"}],"Disorder function":[{"start":281,"end":285,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00865","name":"Osteopontin","start":22,"end":294}]},"uniref50":"UniRef50_P10923","sequence":"MRLAVICFCLFGIASSLPVKVTDSGSSEEKLYSLHPDPIATWLVPDPSQKQNLLAPQNAVSSEEKDDFKQETLPSNSNESHDHMDDDDDDDDDDGDHAESEDSVDSDESDESHHSDESDETVTASTQADTFTPIVPTVDVPNGRGDSLAYGLRSKSRSFQVSDEQYPDATDEDLTSHMKSGESKESLDVIPVAQLLSMPSDQDNNGKGSHESSQLDEPSLETHRLEHSKESQESADQSDVIDSQASSKASLEHQSHKFHSHKDKLVLDPKSKEDDRYLKFRISHELESSSSEVN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P10923","disprot_id":"DP01448","ncbi_taxon_id":10090,"regions_counter":2,"creator":"bmesza","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":294,"region_id":"DP01448r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"NMR characterization of intramolecular interaction of osteopontin, an intrinsically disordered protein with cryptic integrin-binding motifs. <i> Yamaguchi Y, Hanashima S, Yagi H, Takahashi Y, Sasakawa H, Kurimoto E, Iguchi T, Kon S, Uede T, Kato K. </i> Biochem Biophys Res Commun, 2010","statement":[{"text":"The far-ultraviolet CD spectral data indicated that mouse OPN largely lacks secondary structures.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":17,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20152802","validated":{"curator_name":"Rita Pancsa","curator_id":"rpancsa","timestamp":"2021-06-18T11:48:06.166Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":294,"region_id":"DP01448r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR characterization of intramolecular interaction of osteopontin, an intrinsically disordered protein with cryptic integrin-binding motifs. <i> Yamaguchi Y, Hanashima S, Yagi H, Takahashi Y, Sasakawa H, Kurimoto E, Iguchi T, Kon S, Uede T, Kato K. </i> Biochem Biophys Res Commun, 2010","statement":[{"text":"The HSQC peaks of OPN were observed within narrow spectral region (7.5–8.5 ppm of the 1H chemical shifts), confirming that they are largely unstructured in solution.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":17,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20152802","validated":{"curator_name":"Rita Pancsa","curator_id":"rpancsa","timestamp":"2021-06-18T11:48:08.124Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P10923","date":"2018-07-18T08:51:48.000Z","acc":"P10923","name":"Osteopontin","length":294,"organism":"Mus musculus","dataset":["Extracellular matrix proteins"],"UniParc":"UPI000000139D","genes":[{"name":{"value":"Spp1"},"synonyms":[{"value":"Eta-1"},{"value":"Op"},{"value":"Spp-1"}]}],"alphafold_very_low_content":0.41496598639455784,"disorder_content":0.9455782312925171,"disprot_consensus":{"full":[{"start":17,"end":294,"type":"D"}],"Structural state":[{"start":17,"end":294,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00098","name":"Zinc knuckle","start":278,"end":293},{"id":"PF16275","name":"Splicing factor 1 helix-hairpin domain","start":18,"end":130},{"id":"PF22675","name":"KHDC4/BBP-like, KH-domain type I","start":146,"end":227}],"gene3D":[{"start":76,"end":262,"id":"3.30.1370.10","name":"K Homology domain, type 1"}]},"uniref50":"UniRef50_Q15637","sequence":"MATGANATPLDFPSKKRKRSRWNQDTMEQKTVIPGMPTVIPPGLTREQERAYIVQLQIEDLTRKLRTGDLGIPPNPEDRSPSPEPIYNSEGKRLNTREFRTRKKLEEERHNLITEMVALNPDFKPPADYKPPATRVSDKVMIPQDEYPEINFVGLLIGPRGNTLKNIEKECNAKIMIRGKGSVKEGKVGRKDGQMLPGEDEPLHALVTANTMENVKKAVEQIRNILKQGIETPEDQNDLRKMQLRELARLNGTLREDDNRILRPWQSSETRSITNTTVCTKCGGAGHIASDCKFQRPGDPQSAQDKARMDKEYLSLMAELGEAPVPASVGSTSGPATTPLASAPRPAAPANNPPPPSLMSTTQSRPPWMNSGPSESRPYHGMHGGGPGGPGGGPHSFPHPLPSLTGGHGGHPMQHNPNGPPPPWMQPPPPPMNQGPHPPGHHGPPPMDQYLGSTPVGSGVYRLHQGKGMMPPPPMGMMPPPPPPPSGQPPPPPSGPLPPWQQQQQQPPPPPPPSSSMASSTPLPWQQNTTTTTTSAGTGSIPPWQQQQAAAAASPGAPQMQGNPTMVPLPPGVQPPLPPGAPPPPPPPPPGSAGMMYAPPPPPPPPMDPSNFVTMMGMGVAGMPPFGMPPAPPPPPPQN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q15637","disprot_id":"DP01449","ncbi_taxon_id":9606,"regions_counter":4,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":25,"region_id":"DP01449r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP. <i> Selenko P, Gregorovic G, Sprangers R, Stier G, Rhani Z, Krämer A, Sattler M. </i> Mol Cell, 2003","statement":[{"text":"NMR spectra of free SF1(1-25) display characteristics of a random coil conformation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":1,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"12718882","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":25,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP. <i> Selenko P, Gregorovic G, Sprangers R, Stier G, Rhani Z, Krämer A, Sattler M. </i> Mol Cell, 2003","statement":[{"text":"Upon addition of unlabeled U2AF65-RRM3 to 15N-labeled SF1(1-25), tight binding is observed.","type":"Results"}],"term_id":"GO:0005515","curator_id":"eschad","start":1,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"12718882","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01449r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":95,"region_id":"DP01449r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure, phosphorylation and U2AF65 binding of the N-terminal domain of splicing factor 1 during 3'-splice site recognition. <i> Zhang Y, Madl T, Bagdiul I, Kern T, Kang HS, Zou P, Mäusbacher N, Sieber SA, Krämer A, Sattler M. </i> Nucleic Acids Res, 2013","statement":[{"text":"NMR data demonstrate that\nSF1NTD comprises a structured domain consisting of\ntwo a-helical regions that are interrupted by a long disordered\nlinker (residues 69–95)","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":69,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23175611","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":95,"term_name":"phosphorylation display site","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structure, phosphorylation and U2AF65 binding of the N-terminal domain of splicing factor 1 during 3'-splice site recognition. <i> Zhang Y, Madl T, Bagdiul I, Kern T, Kang HS, Zou P, Mäusbacher N, Sieber SA, Krämer A, Sattler M. </i> Nucleic Acids Res, 2013","statement":[{"text":"SF1HH comprises\na helix-hairpin motif with two a-helices in an anti-parallel\narrangement that are connected by a flexible linker\n(Figure 2), which contains the SPSP tandem phosphorylation\nmotif.","type":"Results"}],"term_id":"IDPO:0000045","curator_id":"eschad","start":69,"term_ontology":"IDPO","curator_name":"Eva Schad","reference_id":"23175611","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01449r004","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_Q15637","date":"2018-07-18T11:16:33.000Z","acc":"Q15637","name":"Splicing factor 1","length":639,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000072211","genes":[{"name":{"value":"SF1"},"synonyms":[{"value":"ZFM1"},{"value":"ZNF162"}]}],"alphafold_very_low_content":0.3208137715179969,"disorder_content":0.081377151799687,"disprot_consensus":{"full":[{"start":1,"end":25,"type":"D"},{"start":69,"end":95,"type":"D"}],"Structural state":[{"start":1,"end":25,"type":"D"},{"start":69,"end":95,"type":"D"}],"Molecular function":[{"start":1,"end":25,"type":"F"}],"Disorder function":[{"start":69,"end":95,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00646","name":"F-box domain","start":257,"end":288},{"id":"PF22191","name":"IBR domain","start":373,"end":420}],"gene3D":[{"start":362,"end":419,"id":"2.20.25.20","name":"2.20.25.20"},{"start":244,"end":340,"id":"1.20.1280.50","name":"1.20.1280.50"}]},"uniref50":"UniRef50_Q9UKT4","sequence":"MSRRPCSCALRPPRCSCSASPSAVTAAGRPRPSDSCKEESSTLSVKMKCDFNCNHVHSGLKLVKPDDIGRLVSYTPAYLEGSCKDCIKDYERLSCIGSPIVSPRIVQLETESKRLHNKENQHVQQTLNSTNEIEALETSRLYEDSGYSSFSLQSGLSEHEEGSLLEENFGDSLQSCLLQIQSPDQYPNKNLLPVLHFEKVVCSTLKKNAKRNPKVDREMLKEIIARGNFRLQNIIGRKMGLECVDILSELFRRGLRHVLATILAQLSDMDLINVSKVSTTWKKILEDDKGAFQLYSKAIQRVTENNNKFSPHASTREYVMFRTPLASVQKSAAQTSLKKDAQTKLSNQGDQKGSTYSRHNEFSEVAKTLKKNESLKACIRCNSPAKYDCYLQRATCKREGCGFDYCTKCLCNYHTTKDCSDGKLLKASCKIGPLPGTKKSKKNLRRL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UKT4","disprot_id":"DP01450","ncbi_taxon_id":9606,"regions_counter":14,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":318,"region_id":"DP01450r001","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"Region 1-318 is described as disordered in Extended Data Table 2.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":355,"region_id":"DP01450r002","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"Region 336-355 is described as disordered in Extended Data Table 2, although upon examination of the associated cryo-EM PDB structure it appears that the region is invisible starting from Ala332.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":332,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":447,"region_id":"DP01450r003","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"Region 437-447 in the LR tail appears to be disordered.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":437,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"},{"start":305,"end":374,"reference_id":"23708605","reference_source":"pmid","reference_html":"Electron microscopy structure of human APC/C(CDH1)-EMI1 reveals multimodal mechanism of E3 ligase shutdown. <i> Frye JJ, Brown NG, Petzold G, Watson ER, Grace CR, Nourse A, Jarvis MA, Kriwacki RW, Peters JM, Stark H, Schulman BA. </i> Nat Struct Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01450r004","statement":[{"text":"NMR studies indicate that other than the 45-residue ZBR, the 143-residue C-terminal EMI1 inhibitory region lacks fixed tertiary structure.","type":"Introduction"},{"text":"The APC/C inhibitory domain of EMI1 contains two intrinsically disordered segments separated by a zinc-dependent folded domain","type":"Figure"},{"text":"Overall, the data suggest that EMI1DLZT is substantially intrinsically unfolded, with predominantly disordered D-box, Linker, and Tail regions separated by a folded ZBR.","type":"Results"},{"text":"Backbone resonance assignments revealed that the chemical shifts were consistently dispersed for the ZBR residues in EMI1DLZT, EMI1ZT, and EMI1Z constructs, indicating that the ZBR is an autonomously folded domain (Fig. 1b). Notably, the remaining resonances in EMI1DLZT displayed poor dispersion, low or negative {1H}-15N heteronuclear NOE (HetNOE) values, and relatively lower differences in Cα chemical shifts compared to values predicted for a random coil (Fig. 1c).","type":"Results"}],"cross_refs":[{"db":"PDB","id":"2M6N"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":421,"end":447,"reference_id":"23708605","reference_source":"pmid","reference_html":"Electron microscopy structure of human APC/C(CDH1)-EMI1 reveals multimodal mechanism of E3 ligase shutdown. <i> Frye JJ, Brown NG, Petzold G, Watson ER, Grace CR, Nourse A, Jarvis MA, Kriwacki RW, Peters JM, Stark H, Schulman BA. </i> Nat Struct Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01450r005","statement":[{"text":"NMR studies indicate that other than the 45-residue ZBR, the 143-residue C-terminal EMI1 inhibitory region lacks fixed tertiary structure.","type":"Introduction"},{"text":"The APC/C inhibitory domain of EMI1 contains two intrinsically disordered segments separated by a zinc-dependent folded domain","type":"Figure"},{"text":"Overall, the data suggest that EMI1DLZT is substantially intrinsically unfolded, with predominantly disordered D-box, Linker, and Tail regions separated by a folded ZBR.","type":"Results"},{"text":"Backbone resonance assignments revealed that the chemical shifts were consistently dispersed for the ZBR residues in EMI1DLZT, EMI1ZT, and EMI1Z constructs, indicating that the ZBR is an autonomously folded domain (Fig. 1b). Notably, the remaining resonances in EMI1DLZT displayed poor dispersion, low or negative {1H}-15N heteronuclear NOE (HetNOE) values, and relatively lower differences in Cα chemical shifts compared to values predicted for a random coil (Fig. 1c).","type":"Results"}],"cross_refs":[{"db":"PDB","id":"2M6N"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":421,"end":447,"reference_id":"23708605","reference_source":"pmid","reference_html":"Electron microscopy structure of human APC/C(CDH1)-EMI1 reveals multimodal mechanism of E3 ligase shutdown. <i> Frye JJ, Brown NG, Petzold G, Watson ER, Grace CR, Nourse A, Jarvis MA, Kriwacki RW, Peters JM, Stark H, Schulman BA. </i> Nat Struct Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01450r006","statement":[{"text":"To further characterize the biophysical properties of EMI1DLZT, we measured the hydrodynamic radius (Rh) to be 3.1 nm and 2.9 nm by dynamic light scattering (DLS) and analytical ultracentrifugation, respectively (Fig. 1f, g). A globular protein would have to be ~46 kDa, rather than the 16.0 kDa of EMI1DLZT to yield an Rh value of 3.1 nm by DLS. The best-fit weight-average anhydrous frictional ratio (f/f0)w values of 1.73 and 1.85 obtained from two analytical ultracentrifugation experiments indicate that EMI1DLZT is elongated in solution (Supplementary Fig. 1). Overall, the data suggest that EMI1DLZT is substantially intrinsically unfolded, with predominantly disordered D-box, Linker, and Tail regions separated by a folded ZBR.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":305,"end":374,"reference_id":"23708605","reference_source":"pmid","reference_html":"Electron microscopy structure of human APC/C(CDH1)-EMI1 reveals multimodal mechanism of E3 ligase shutdown. <i> Frye JJ, Brown NG, Petzold G, Watson ER, Grace CR, Nourse A, Jarvis MA, Kriwacki RW, Peters JM, Stark H, Schulman BA. </i> Nat Struct Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01450r007","statement":[{"text":"To further characterize the biophysical properties of EMI1DLZT, we measured the hydrodynamic radius (Rh) to be 3.1 nm and 2.9 nm by dynamic light scattering (DLS) and analytical ultracentrifugation, respectively (Fig. 1f, g). A globular protein would have to be ~46 kDa, rather than the 16.0 kDa of EMI1DLZT to yield an Rh value of 3.1 nm by DLS. The best-fit weight-average anhydrous frictional ratio (f/f0)w values of 1.73 and 1.85 obtained from two analytical ultracentrifugation experiments indicate that EMI1DLZT is elongated in solution (Supplementary Fig. 1). Overall, the data suggest that EMI1DLZT is substantially intrinsically unfolded, with predominantly disordered D-box, Linker, and Tail regions separated by a folded ZBR.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":321,"end":330,"reference_id":"23708605","reference_source":"pmid","reference_html":"Electron microscopy structure of human APC/C(CDH1)-EMI1 reveals multimodal mechanism of E3 ligase shutdown. <i> Frye JJ, Brown NG, Petzold G, Watson ER, Grace CR, Nourse A, Jarvis MA, Kriwacki RW, Peters JM, Stark H, Schulman BA. </i> Nat Struct Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01450r008","statement":[{"text":"An obvious key functional element is EMI1’s D-box. In examining the EM data, there are differences between APC/CCDH1 and the EMI1–SKP1- and EMI1DLZT-bound complexes in the vicinity of CDH1 and APC10, consistent with EMI1’s D-box binding the coreceptors (Supplemental Fig. 2). We were unable to generate stoichiometric complexes for mutants lacking EMI1’s D-box. Furthermore, alanine substitutions in place of Arg322 and Leu325 in EMI1DLZT’s D-box “RxxL” motif decreased inhibition of cycB-NT* in reactions with UBCH10 to the point that we could not measure a Ki under the initial rate conditions (Table 1). The apparent Ki increased by over two orders-of-magnitude for UbcycB-NT* ubiquitination by APC/CCDH1 and UBE2S.","type":"Results"},{"text":"The intrinsically disordered D-box, linker and tail elements, together with a structured zinc-binding domain, bind distinct regions of APC/C(CDH1) to synergistically both block the substrate-binding site and inhibit ubiquitin-chain elongation. ","type":"Abstract"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":321,"end":330,"reference_id":"23708605","reference_source":"pmid","reference_html":"Electron microscopy structure of human APC/C(CDH1)-EMI1 reveals multimodal mechanism of E3 ligase shutdown. <i> Frye JJ, Brown NG, Petzold G, Watson ER, Grace CR, Nourse A, Jarvis MA, Kriwacki RW, Peters JM, Stark H, Schulman BA. </i> Nat Struct Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01450r009","statement":[{"text":"Furthermore, alanine substitutions in place of Arg322 and Leu325 in EMI1DLZT’s D-box “RxxL” motif decreased inhibition of cycB-NT* in reactions with UBCH10 to the point that we could not measure a Ki under the initial rate conditions (Table 1). The apparent Ki increased by over two orders-of-magnitude for UbcycB-NT* ubiquitination by APC/CCDH1 and UBE2S.","type":"Results"},{"text":"The functional importance of intrinsic structural disorder is explained by the D-box, Linker, ZBR, and Tail synergistically blocking both Ub ligation to a substrate and Ub chain elongation by APC/C.","type":"Introduction"},{"text":"The intrinsically disordered D-box, linker and tail elements, together with a structured zinc-binding domain, bind distinct regions of APC/C(CDH1) to synergistically both block the substrate-binding site and inhibit ubiquitin-chain elongation. ","type":"Abstract"},{"text":"The functional importance of intrinsic structural disorder is explained by enabling a small inhibitory domain to bind multiple sites to shut down multiple functions of a “molecular machine” nearly 100 times its size.","type":"Abstract"}],"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":421,"end":447,"reference_id":"23708605","reference_source":"pmid","reference_html":"Electron microscopy structure of human APC/C(CDH1)-EMI1 reveals multimodal mechanism of E3 ligase shutdown. <i> Frye JJ, Brown NG, Petzold G, Watson ER, Grace CR, Nourse A, Jarvis MA, Kriwacki RW, Peters JM, Stark H, Schulman BA. </i> Nat Struct Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01450r010","statement":[{"text":"Although the Ki for full-length EMI1 increased substantially, presumably due to lack of its D-box recruitment by CDH1, the isolated EMI1 Tail inhibited APC/C-UBE2S-mediated ubiquitination of UbcycB-NT* equally well in the presence or absence of CDH1 (Table 1, Fig. 6a, b).","type":"Results"},{"text":"The functional importance of intrinsic structural disorder is explained by enabling a small inhibitory domain to bind multiple sites to shut down multiple functions of a “molecular machine” nearly 100 times its size.","type":"Abstract"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":421,"end":447,"reference_id":"23708605","reference_source":"pmid","reference_html":"Electron microscopy structure of human APC/C(CDH1)-EMI1 reveals multimodal mechanism of E3 ligase shutdown. <i> Frye JJ, Brown NG, Petzold G, Watson ER, Grace CR, Nourse A, Jarvis MA, Kriwacki RW, Peters JM, Stark H, Schulman BA. </i> Nat Struct Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01450r011","statement":[{"text":"The indifference to CDH1 implied that the isolated EMI1 Tail targets a catalytic function of APC/C-UBE2S independently of blocking APC/C binding to a D-box substrate.","type":"Results"},{"text":"Furthermore, between the EM data showing EMI1 contacting the APC/C Catalytic core and biochemical data analyzing reactions inhibited by EMI1, we also uncovered a function for the unstructured C-terminal tail of EMI1 in blocking catalysis of Ub chain elongation by UBE2S","type":"Discussion"}],"ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":338,"end":359,"reference_id":"23708605","reference_source":"pmid","reference_html":"Electron microscopy structure of human APC/C(CDH1)-EMI1 reveals multimodal mechanism of E3 ligase shutdown. <i> Frye JJ, Brown NG, Petzold G, Watson ER, Grace CR, Nourse A, Jarvis MA, Kriwacki RW, Peters JM, Stark H, Schulman BA. </i> Nat Struct Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01450r012","statement":[{"text":"Prompted by the structural data showing that an insertion maps to the central location between the D-box coreceptor APC10, the Arc lamp, and the Platform (Fig. 4a), we considered that the Linker might be functionally important. Indeed, the Linker is not simply a spatial connector joining the D-box and ZBR effectors: deleting 20 Linker residues impairs EMI1DLZT-mediated inhibition, which is not restored by replacement with a 20-residue glycine-rich sequence (Fig. 4c, d). As a first attempt to address whether this sequence or structure may be important, we tested two 10-residue deletions, and found only one to be severely impaired for inhibition. Triply mutating conserved Leu345, Tyr356, and Arg358 within the essential sequence to alanines, either in the context of the benign 10-residue deletion or in EMI1DLZT, is sufficient to substantially impair inhibition. Thus, specific side-chains within the Linker contribute to inhibition (Fig. 4d).","type":"Results"},{"text":"The intrinsically disordered D-box, linker and tail elements, together with a structured zinc-binding domain, bind distinct regions of APC/C(CDH1) to synergistically both block the substrate-binding site and inhibit ubiquitin-chain elongation. ","type":"Abstract"}],"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":338,"end":359,"reference_id":"23708605","reference_source":"pmid","reference_html":"Electron microscopy structure of human APC/C(CDH1)-EMI1 reveals multimodal mechanism of E3 ligase shutdown. <i> Frye JJ, Brown NG, Petzold G, Watson ER, Grace CR, Nourse A, Jarvis MA, Kriwacki RW, Peters JM, Stark H, Schulman BA. </i> Nat Struct Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01450r013","statement":[{"text":"Prompted by the structural data showing that an insertion maps to the central location between the D-box coreceptor APC10, the Arc lamp, and the Platform (Fig. 4a), we considered that the Linker might be functionally important. Indeed, the Linker is not simply a spatial connector joining the D-box and ZBR effectors: deleting 20 Linker residues impairs EMI1DLZT-mediated inhibition, which is not restored by replacement with a 20-residue glycine-rich sequence (Fig. 4c, d). As a first attempt to address whether this sequence or structure may be important, we tested two 10-residue deletions, and found only one to be severely impaired for inhibition. ","type":"Results"},{"text":"Thus, specific side-chains within the Linker contribute to inhibition (Fig. 4d).","type":"Results"},{"text":"The intrinsically disordered D-box, linker and tail elements, together with a structured zinc-binding domain, bind distinct regions of APC/C(CDH1) to synergistically both block the substrate-binding site and inhibit ubiquitin-chain elongation. ","type":"Abstract"}],"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":338,"end":359,"reference_id":"23708605","reference_source":"pmid","reference_html":"Electron microscopy structure of human APC/C(CDH1)-EMI1 reveals multimodal mechanism of E3 ligase shutdown. <i> Frye JJ, Brown NG, Petzold G, Watson ER, Grace CR, Nourse A, Jarvis MA, Kriwacki RW, Peters JM, Stark H, Schulman BA. </i> Nat Struct Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01450r014","statement":[{"text":"The linker region connects the D-box and ZBR domains of Emi1.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_Q9UKT4","date":"2018-07-18T11:38:41.000Z","acc":"Q9UKT4","name":"F-box only protein 5","length":447,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012A585","genes":[{"name":{"value":"FBXO5","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:13584","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:13584"}}]},"synonyms":[{"value":"EMI1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11988738","url":"http://www.ncbi.nlm.nih.gov/pubmed/11988738","alternativeUrl":"https://europepmc.org/abstract/MED/11988738"}}]},{"value":"FBX5","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:13584","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:13584"}}]}]}],"alphafold_very_low_content":0.47651006711409394,"disorder_content":0.8970917225950783,"disprot_consensus":{"full":[{"start":1,"end":374,"type":"D"},{"start":421,"end":447,"type":"D"}],"Structural state":[{"start":1,"end":374,"type":"D"},{"start":421,"end":447,"type":"D"}],"Molecular function":[{"start":321,"end":330,"type":"F"},{"start":338,"end":359,"type":"F"},{"start":421,"end":447,"type":"F"}],"Disorder function":[{"start":338,"end":359,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03943","name":"TAP C-terminal domain","start":569,"end":617},{"id":"PF09162","name":"Tap, RNA-binding","start":119,"end":198},{"id":"PF22602","name":"Nuclear RNA export factor, NTF2 domain","start":386,"end":537},{"id":"PF24048","name":"NXF1/2/3/5 leucine-rich repeat domain","start":217,"end":353}],"gene3D":[{"start":96,"end":201,"id":"3.30.70.330","name":"3.30.70.330"},{"start":203,"end":362,"id":"3.80.10.10","name":"Ribonuclease Inhibitor"},{"start":561,"end":619,"id":"1.10.8.10","name":"DNA helicase RuvA subunit, C-terminal domain"},{"start":370,"end":555,"id":"3.10.450.50","name":"3.10.450.50"}]},"uniref50":"UniRef50_Q9UBU9","sequence":"MADEGKSYSEHDDERVNFPQRKKKGRGPFRWKYGEGNRRSGRGGSGIRSSRLEEDDGDVAMSDAQDGPRVRYNPYTTRPNRRGDTWHDRDRIHVTVRRDRAPPERGGAGTSQDGTSKNWFKITIPYGRKYDKAWLLSMIQSKCSVPFTPIEFHYENTRAQFFVEDASTASALKAVNYKILDRENRRISIIINSSAPPHTILNELKPEQVEQLKLIMSKRYDGSQQALDLKGLRSDPDLVAQNIDVVLNRRSCMAATLRIIEENIPELLSLNLSNNRLYRLDDMSSIVQKAPNLKILNLSGNELKSERELDKIKGLKLEELWLDGNSLCDTFRDQSTYISAIRERFPKLLRLDGHELPPPIAFDVEAPTTLPPCKGSYFGTENLKSLVLHFLQQYYAIYDSGDRQGLLDAYHDGACCSLSIPFIPQNPARSSLAEYFKDSRNVKKLKDPTLRFRLLKHTRLNVVAFLNELPKTQHDVNSFVVDISAQTSTLLCFSVNGVFKEVDGKSRDSLRAFTRTFIAVPASNSGLCIVNDELFVRNASSEEIQRAFAMPAPTPSSSPVPTLSPEQQEMLQAFSTQSGMNLEWSQKCLQDNNWDYTRSAQAFTHLKAKGEIPEVAFMK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UBU9","disprot_id":"DP01451","ncbi_taxon_id":9606,"regions_counter":2,"creator":"mpajkos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":118,"region_id":"DP01451r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The structure of the mRNA export factor TAP reveals a cis arrangement of a non-canonical RNP domain and an LRR domain. <i> Liker E, Fernandez E, Izaurralde E, Conti E. </i> EMBO J, 2000","statement":[{"text":"\"The N-terminal glycine and arginine-rich portion of the molecule (residues 102–118) is disordered and may therefore be flexible in the absence of RNA.\"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":102,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1FT8"}],"reference_id":"11060011","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":117,"region_id":"DP01451r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure-function studies of nucleocytoplasmic transport of retroviral genomic RNA by mRNA export factor TAP. <i> Teplova M, Wohlbold L, Khin NW, Izaurralde E, Patel DJ. </i> Nat Struct Mol Biol, 2011","statement":[{"text":"\"Similar to previously reported structures of free TAP-NTD, N-terminal amino acids 96–117 were disordered in the crystal structure of the complex with hCTE.\"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":96,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3RW6"}],"reference_id":"21822283","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9UBU9","date":"2018-07-18T11:48:00.000Z","acc":"Q9UBU9","name":"Nuclear RNA export factor 1","length":619,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000012B9","genes":[{"name":{"value":"NXF1"},"synonyms":[{"value":"TAP"}]}],"alphafold_very_low_content":0.2035541195476575,"disorder_content":0.03715670436187399,"disprot_consensus":{"full":[{"start":96,"end":118,"type":"D"}],"Structural state":[{"start":96,"end":118,"type":"D"}]}},{"features":{"pfam":[{"id":"PF12895","name":"Anaphase-promoting complex, cyclosome, subunit 3","start":15,"end":94},{"id":"PF13424","name":"Tetratricopeptide repeat","start":447,"end":510}]},"uniref50":"UniRef50_Q13042","sequence":"MNLERLRKRVRQYLDQQQYQSALFWADKVASLSREEPQDIYWLAQCLYLTAQYHRAAHALRSRKLDKLYEACRYLAARCHYAAKEHQQALDVLDMEEPINKRLFEKYLKDESGFKDPSSDWEMSQSSIKSSICLLRGKIYDALDNRTLATYSYKEALKLDVYCFEAFDLLTSHHMLTAQEEKELLESLPLSKLCNEEQELLRFLFENKLKKYNKPSETVIPESVDGLQENLDVVVSLAERHYYNCDFKMCYKLTSVVMEKDPFHASCLPVHIGTLVELNKANELFYLSHKLVDLYPSNPVSWFAVGCYYLMVGHKNEHARRYLSKATTLEKTYGPAWIAYGHSFAVESEHDQAMAAYFTAAQLMKGCHLPMLYIGLEYGLTNNSKLAERFFSQALSIAPEDPFVMHEVGVVAFQNGEWKTAEKWFLDALEKIKAIGNEVTVDKWEPLLNNLGHVCRKLKKYAEALDYHRQALVLIPQNASTYSAIGYIHSLMGNFENAVDYFHTALGLRRDDTFSVTMLGHCIEMYIGDSEAYIGADIKDKLKCYDFDVHTMKTLKNIISPPWDFREFEVEKQTAEETGLTPLETSRKTPDSRPSLEETFEIEMNESDMMLETSMSDHST","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q13042","disprot_id":"DP01452","ncbi_taxon_id":9606,"regions_counter":6,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":126,"region_id":"DP01452r001","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The regions are specified in the Extended Data Table 2","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":96,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":123,"region_id":"DP01452r002","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The regions are specified in the Extended Data Table 2","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":96,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":620,"region_id":"DP01452r003","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The regions are specified in the Extended Data Table 2","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":528,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":126,"region_id":"DP01452r004","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Molecular mechanism of APC/C activation by mitotic phosphorylation. <i> Zhang S, Chang L, Alfieri C, Zhang Z, Yang J, Maslen S, Skehel M, Barford D. </i> Nature, 2016","statement":[{"text":"\"These sites lie within disordered regions of the APC/C (Ref. 23).\"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":94,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5G05"}],"reference_id":"27120157","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":620,"region_id":"DP01452r005","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Molecular mechanism of APC/C activation by mitotic phosphorylation. <i> Zhang S, Chang L, Alfieri C, Zhang Z, Yang J, Maslen S, Skehel M, Barford D. </i> Nature, 2016","statement":[{"text":"\"These sites lie within disordered regions of the APC/C (Ref. 23).\"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":528,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5G05"}],"reference_id":"27120157","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":620,"region_id":"DP01452r006","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The regions are specified in the Extended Data Table 2","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":534,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q13042","date":"2018-07-18T11:52:22.000Z","acc":"Q13042","name":"Cell division cycle protein 16 homolog","length":620,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000006D12D","genes":[{"name":{"value":"CDC16"},"synonyms":[{"value":"ANAPC6"}]}],"alphafold_very_low_content":0.17419354838709677,"disorder_content":0.2032258064516129,"disprot_consensus":{"full":[{"start":94,"end":126,"type":"D"},{"start":528,"end":620,"type":"D"}],"Structural state":[{"start":94,"end":126,"type":"D"},{"start":528,"end":620,"type":"D"}]}},{"features":{"pfam":[{"id":"PF10471","name":"Anaphase-promoting complex APC subunit CDC26","start":1,"end":37}]},"uniref50":"UniRef50_Q8NHZ8","sequence":"MLRRKPTRLELKLDDIEEFENIRKDLETRKKQKEDVEVVGGSDGEGAIGLSSDPKSREQMINDRIGYKPQPKPNNRSSQFGSLEF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q8NHZ8","disprot_id":"DP01453","ncbi_taxon_id":9606,"regions_counter":1,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":85,"region_id":"DP01453r001","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The region is specified in the Extended Data Table 2","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":26,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"},{"db":"PDB","id":"5A31"},{"db":"PDB","id":"5G05"},{"db":"PDB","id":"5G04"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q8NHZ8","date":"2018-07-18T12:10:53.000Z","acc":"Q8NHZ8","name":"Anaphase-promoting complex subunit CDC26","length":85,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000073C4F","genes":[{"name":{"value":"CDC26"},"synonyms":[{"value":"ANAPC12"},{"value":"C9orf17"}]}],"alphafold_very_low_content":0.17647058823529413,"disorder_content":0.7058823529411765,"disprot_consensus":{"full":[{"start":26,"end":85,"type":"D"}],"Structural state":[{"start":26,"end":85,"type":"D"}]}},{"features":{"pfam":[{"id":"PF15243","name":"Anaphase-promoting complex subunit 15","start":2,"end":92}]},"uniref50":"UniRef50_P60006","sequence":"MSTLFPSLFPRVTETLWFNLDRPCVEETELQQQEQQHQAWLQSIAEKDNNLVPIGKPASEHYDDEEEEDDEDDEDSEEDSEDDEDMQDMDEMNDYNESPDDGEVNEVDMEGNEQDQDQWMI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P60006","disprot_id":"DP01454","ncbi_taxon_id":9606,"regions_counter":1,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":121,"region_id":"DP01454r001","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The region is specified in the Extended Data Table 2","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":57,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"},{"db":"PDB","id":"5A31"},{"db":"PDB","id":"5G05"},{"db":"PDB","id":"5G04"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P60006","date":"2018-07-18T12:16:30.000Z","acc":"P60006","name":"Anaphase-promoting complex subunit 15","length":121,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000002356F","genes":[{"name":{"value":"ANAPC15"},"synonyms":[{"value":"C11orf51"}],"orfNames":[{"value":"HSPC020"}]}],"alphafold_very_low_content":0.05785123966942149,"disorder_content":0.5371900826446281,"disprot_consensus":{"full":[{"start":57,"end":121,"type":"D"}],"Structural state":[{"start":57,"end":121,"type":"D"}]}},{"features":{"pfam":[{"id":"PF17256","name":"Anaphase-promoting complex, subunit 16","start":27,"end":106}]},"uniref50":"UniRef50_Q96DE5","sequence":"MAASSSSSSAGGVSGSSVTGSGFSVSDLAPPRKALFTYPKGAGEMLEDGSERFLCESVFSYQVASTLKQVKHDQQVARMEKLAGLVEELEADEWRFKPIEQLLGFTPSSG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q96DE5","disprot_id":"DP01455","ncbi_taxon_id":9606,"regions_counter":1,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":51,"region_id":"DP01455r001","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The region is specified in the Extended Data Table 2","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":1,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"},{"db":"PDB","id":"5A31"},{"db":"PDB","id":"5G05"},{"db":"PDB","id":"5G04"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q96DE5","date":"2018-07-18T12:19:06.000Z","acc":"Q96DE5","name":"Anaphase-promoting complex subunit 16","length":110,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000002181D","genes":[{"name":{"value":"ANAPC16"},"synonyms":[{"value":"C10orf104"},{"value":"CENP-27","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"20813266","url":"http://www.ncbi.nlm.nih.gov/pubmed/20813266","alternativeUrl":"https://europepmc.org/abstract/MED/20813266"}}]}]}],"alphafold_very_low_content":0.3,"disorder_content":0.4636363636363636,"disprot_consensus":{"full":[{"start":1,"end":51,"type":"D"}],"Structural state":[{"start":1,"end":51,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":91,"end":141},{"id":"PF00642","name":"Zinc finger C-x8-C-x5-C-x3-H type (and similar)","start":14,"end":38},{"id":"PF00642","name":"Zinc finger C-x8-C-x5-C-x3-H type (and similar)","start":150,"end":174}],"gene3D":[{"start":43,"end":146,"id":"3.30.70.330","name":"3.30.70.330"}]},"uniref50":"UniRef50_Q01081","sequence":"MAEYLASIFGTEKDKVNCSFYFKIGACRHGDRCSRLHNKPTFSQTIALLNIYRNPQNSSQSADGLRCAVSDVEMQEHYDEFFEEVFTEMEEKYGEVEEMNVCDNLGDHLVGNVYVKFRREEDAEKAVIDLNNRWFNGQPIHAELSPVTDFREACCRQYEMGECTRGGFCNFMHLKPISRELRRELYGRRRKKHRSRSRSRERRSRSRDRGRGGGGGGGGGGGGRERDRRRSRDRERSGRF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q01081","disprot_id":"DP01456","ncbi_taxon_id":9606,"regions_counter":3,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":152,"region_id":"DP01456r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Induced folding of the U2AF35 RRM upon binding to U2AF65. <i> Kellenberger E, Stier G, Sattler M. </i> FEBS Lett, 2002","statement":[{"text":"The small chemical shift dispersion clearly\nindicates that the protein adopts a random coil conformation\nand is unstructured in aqueous solution.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":38,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"12297299","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":152,"term_name":"disorder to order","released":"2022_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Induced folding of the U2AF35 RRM upon binding to U2AF65. <i> Kellenberger E, Stier G, Sattler M. </i> FEBS Lett, 2002","statement":[{"text":"In the present paper, we found that the\nmonomeric free form of U2AF35 RRM is unstructured in\nsolution and that its three-dimensional structure is induced\nupon binding to its native protein partner U2AF65.","type":"Conclusion"}],"term_id":"IDPO:0000011","curator_id":"vnugnes","start":38,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12297299","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-15T20:10:32.772Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01456r002","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P26368"}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":152,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Induced folding of the U2AF35 RRM upon binding to U2AF65. <i> Kellenberger E, Stier G, Sattler M. </i> FEBS Lett, 2002","statement":[{"text":"In the present paper, we found that the\nmonomeric free form of U2AF35 RRM is unstructured in\nsolution and that its three-dimensional structure is induced\nupon binding to its native protein partner U2AF65.","type":"Conclusion"}],"term_id":"GO:0005515","curator_id":"eschad","start":38,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"12297299","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01456r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q01081","date":"2018-07-18T12:31:42.000Z","acc":"Q01081","name":"Splicing factor U2AF 35 kDa subunit","length":240,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI0000000C26","genes":[{"name":{"value":"U2AF1"},"synonyms":[{"value":"U2AF35"},{"value":"U2AFBP"}],"orfNames":[{"value":"FP793"}]}],"alphafold_very_low_content":0.2125,"disorder_content":0.4791666666666667,"disprot_consensus":{"full":[{"start":38,"end":152,"type":"T"}],"Structural state":[{"start":38,"end":152,"type":"D"}],"Structural transition":[{"start":38,"end":152,"type":"T"}],"Molecular function":[{"start":38,"end":152,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03810","name":"Importin-beta N-terminal domain","start":42,"end":108},{"id":"PF13513","name":"HEAT-like repeat","start":419,"end":473},{"id":"PF25574","name":"Importin subunit beta-1-like, TPR repeats","start":674,"end":776},{"id":"PF25780","name":"IPO5-like, TPR repeats","start":124,"end":267}],"gene3D":[{"start":9,"end":346,"id":"1.25.10.10","name":"Leucine-rich Repeat Variant"},{"start":347,"end":898,"id":"1.25.10.10","name":"Leucine-rich Repeat Variant"}]},"uniref50":"UniRef50_O14787","sequence":"MVWDRQTKMEYEWKPDEQGLQQILQLLKESQSPDTTIQRTVQQKLEQLNQYPDFNNYLIFVLTKLKSEDEPTRSLSGLILKNNVKAHFQNFPNGVTDFIKSECLNNIGDSSPLIRATVGILITTIASKGELQNWPDLLPKLCSLLDSEDYNTCEGAFGALQKICEDSAEILDSDVLDRPLNIMIPKFLQFFKHSSPKIRSHAVACVNQFIISRTQALMLHIDSFIENLFALAGDEEPEVRKNVCRALVMLLEVRMDRLLPHMHNIVEYMLQRTQDQDENVALEACEFWLTLAEQPICKDVLVRHLPKLIPVLVNGMKYSDIDIILLKGDVEEDETIPDSEQDIRPRFHRSRTVAQQHDEDGIEEEDDDDDEIDDDDTISDWNLRKCSAAALDVLANVYRDELLPHILPLLKELLFHHEWVVKESGILVLGAIAEGCMQGMIPYLPELIPHLIQCLSDKKALVRSITCWTLSRYAHWVVSQPPDTYLKPLMTELLKRILDSNKRVQEAACSAFATLEEEACTELVPYLAYILDTLVFAFSKYQHKNLLILYDAIGTLADSVGHHLNKPEYIQMLMPPLIQKWNMLKDEDKDLFPLLECLSSVATALQSGFLPYCEPVYQRCVNLVQKTLAQAMLNNAQPDQYEAPDKDFMIVALDLLSGLAEGLGGNIEQLVARSNILTLMYQCMQDKMPEVRQSSFALLGDLTKACFQHVKPCIADFMPILGTNLNPEFISVCNNATWAIGEISIQMGIEMQPYIPMVLHQLVEIINRPNTPKTLLENTAITIGRLGYVCPQEVAPMLQQFIRPWCTSLRNIRDNEEKDSAFRGICTMISVNPSGVIQDFIFFCDAVASWINPKDDLRDMFCKILHGFKNQVGDENWRRFSDQFPLPLKERLAAFYGV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q92973","disprot_id":"DP01457","ncbi_taxon_id":9606,"regions_counter":1,"creator":"mpajkos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":371,"region_id":"DP01457r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for substrate recognition and dissociation by human transportin 1. <i> Imasaki T, Shimizu T, Hashimoto H, Hidaka Y, Kose S, Imamoto N, Yamada M, Sato M. </i> Mol Cell, 2007","statement":[{"text":"In Transportin-1 the H8 loop (residue 312-374) defined as a long loop connecting H8A and H8B helices. \n\"The loops are disordered in the regions between K319 and S371 for NLS-free Trn1, and in the regions between K319 and D366 for Trn1 bound to hnRNP D NLS\"","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":319,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2Z5M"}],"reference_id":"17936704","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q92973","date":"2018-07-18T12:40:35.000Z","acc":"Q92973","name":"Transportin-1","length":898,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000000D987","genes":[{"name":{"value":"TNPO1"},"synonyms":[{"value":"KPNB2"},{"value":"MIP1"},{"value":"TRN"}]}],"alphafold_very_low_content":0.0334075723830735,"disorder_content":0.05902004454342984,"disprot_consensus":{"full":[{"start":319,"end":371,"type":"D"}],"Structural state":[{"start":319,"end":371,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":21,"end":87}],"gene3D":[{"start":15,"end":118,"id":"3.30.70.330","name":"3.30.70.330"}]},"uniref50":"UniRef50_Q9Y3B4","sequence":"MAMQAAKRANIRLPPEVNRILYIRNLPYKITAEEMYDIFGKYGPIRQIRVGNTPETRGTAYVVYEDIFDAKNACDHLSGFNVCNRYLVVLYYNANRAFQKMDTKKKEEQLKLLKEKYGINTDPPK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9Y3B4","disprot_id":"DP01458","ncbi_taxon_id":9606,"regions_counter":2,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":125,"region_id":"DP01458r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Biochemical and NMR analyses of an SF3b155-p14-U2AF-RNA interaction network involved in branch point definition during pre-mRNA splicing. <i> Spadaccini R, Reidt U, Dybkov O, Will C, Frank R, Stier G, Corsini L, Wahl MC, Lührmann R, Sattler M. </i> RNA, 2006","statement":[{"text":"The flanking N- (residues 1–\n20) and C-terminal regions (residues 100–125) are unstructured","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":100,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"16495236","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":20,"region_id":"DP01458r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Biochemical and NMR analyses of an SF3b155-p14-U2AF-RNA interaction network involved in branch point definition during pre-mRNA splicing. <i> Spadaccini R, Reidt U, Dybkov O, Will C, Frank R, Stier G, Corsini L, Wahl MC, Lührmann R, Sattler M. </i> RNA, 2006","statement":[{"text":"The flanking N- (residues 1–\n20) and C-terminal regions (residues 100–125) are unstructured.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":1,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"16495236","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9Y3B4","date":"2018-07-18T13:12:51.000Z","acc":"Q9Y3B4","name":"Splicing factor 3B subunit 6","length":125,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000000963","genes":[{"name":{"value":"SF3B6"},"synonyms":[{"value":"SAP14"},{"value":"SF3B14"},{"value":"SF3B14A"}],"orfNames":[{"value":"CGI-110"},{"value":"HSPC175"},{"value":"HT006"}]}],"alphafold_very_low_content":0.008,"disorder_content":0.368,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"D"},{"start":100,"end":125,"type":"D"}],"Structural state":[{"start":1,"end":20,"type":"D"},{"start":100,"end":125,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00091","name":"Tubulin/FtsZ family, GTPase domain","start":3,"end":211},{"id":"PF03953","name":"Tubulin C-terminal domain","start":261,"end":382}],"gene3D":[{"start":264,"end":373,"id":"3.30.1330.20","name":"Tubulin/FtsZ, C-terminal domain"},{"start":374,"end":443,"id":"1.10.287.600","name":"Helix hairpin bin"},{"start":1,"end":263,"id":"3.40.50.1440","name":"Tubulin/FtsZ, GTPase domain"}]},"uniref50":"UniRef50_Q40665","sequence":"MREIVHIQGGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLERINVYYNEATGGRYVPRAILMDLEPGTMDSVRAGPFGQLFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPDRIMETFSVVPSPKVSDTVVEPYNATLSVHQLVENADECMVIDNEALYDICFRTLKLTTPTYGDLNHLVSAAMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMIGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMCAADPRHGRYLTASALFRGRMSTKEVDEQMLNVQNKNSSYFVEWIPNNIKSSICDIPPKGLKMAVTFVGNSTAIQEMFKRVAEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEGEFEEEEGEN","taxonomy":["Eukaryota","Sar","Alveolata","Ciliophora","Intramacronucleata","Oligohymenophorea","Hymenostomatida","Tetrahymenina","Tetrahymenidae","Tetrahymena"],"uniref90":"UniRef90_P41352","disprot_id":"DP01459","ncbi_taxon_id":5911,"regions_counter":1,"creator":"mmacossay","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":443,"region_id":"DP01459r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Molecular Determinants of Tubulin's C-Terminal Tail Conformational Ensemble. <i> Wall KP, Pagratis M, Armstrong G, Balsbaugh JL, Verbeke E, Pearson CG, Hough LE. </i> ACS Chem Biol, 2016","statement":[{"text":"In this case, the peak positions were fully consistent with the supposition that the C-terminal tails are\ndisordered","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mmacossay","start":427,"term_ontology":"IDPO","curator_name":"Mauricio Macossay-Castillo","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27541566","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P41352","date":"2018-07-18T14:32:00.000Z","acc":"P41352","name":"Tubulin beta chain","length":443,"organism":"Tetrahymena thermophila","dataset":[],"UniParc":"UPI0000136A3C","genes":[{"name":{"value":"BTU1"}},{"name":{"value":"BTU2"}}],"alphafold_very_low_content":0.01805869074492099,"disorder_content":0.03837471783295711,"disprot_consensus":{"full":[{"start":427,"end":443,"type":"D"}],"Structural state":[{"start":427,"end":443,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00091","name":"Tubulin/FtsZ family, GTPase domain","start":3,"end":213},{"id":"PF03953","name":"Tubulin C-terminal domain","start":263,"end":392}],"gene3D":[{"start":1,"end":268,"id":"3.40.50.1440","name":"Tubulin/FtsZ, GTPase domain"},{"start":269,"end":383,"id":"3.30.1330.20","name":"Tubulin/FtsZ, C-terminal domain"},{"start":384,"end":449,"id":"1.10.287.600","name":"Helix hairpin bin"}]},"uniref50":"UniRef50_P04689","sequence":"MREVISIHVGQGGIQVGNACWELFCLEHGIQPDGQMPSDKTIGGGDDAFNTFFSETGAGKHVPRAVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNSVGGGTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVSTAVVEPYNSILSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTASLRFDGALNVDITEFQTNLVPYPRIHFMLSSYAPIISAEKAYHEQLSVAEITNSAFEPANMMAKCDPRHGKYMACSMMYRGDVVPKDVNASIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVMRAVCMISNSTAIAEVFSRLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGIETAEGEGEEEGY","taxonomy":["Eukaryota","Sar","Alveolata","Ciliophora","Intramacronucleata","Oligohymenophorea","Hymenostomatida","Tetrahymenina","Tetrahymenidae","Tetrahymena"],"uniref90":"UniRef90_P41351","disprot_id":"DP01460","ncbi_taxon_id":5911,"regions_counter":1,"creator":"mmacossay","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":449,"region_id":"DP01460r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Molecular Determinants of Tubulin's C-Terminal Tail Conformational Ensemble. <i> Wall KP, Pagratis M, Armstrong G, Balsbaugh JL, Verbeke E, Pearson CG, Hough LE. </i> ACS Chem Biol, 2016","statement":[{"text":"In this case, the peak positions were fully consistent with the supposition that the C-terminal tails are disordered","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mmacossay","start":431,"term_ontology":"IDPO","curator_name":"Mauricio Macossay-Castillo","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-5153-3470","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27541566","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P41351","date":"2018-07-18T14:38:07.000Z","acc":"P41351","name":"Tubulin alpha chain","length":449,"organism":"Tetrahymena thermophila","dataset":[],"UniParc":"UPI00001369B0","genes":[],"alphafold_very_low_content":0.022271714922048998,"disorder_content":0.042316258351893093,"disprot_consensus":{"full":[{"start":431,"end":449,"type":"D"}],"Structural state":[{"start":431,"end":449,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":28,"end":278},{"id":"PF11629","name":"C terminal SARAH domain of Mst1","start":437,"end":484}],"gene3D":[{"start":15,"end":101,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":102,"end":313,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"}]},"uniref50":"UniRef50_Q13188","sequence":"MEQPPAPKSKLKKLSEDSLTKQPEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVESDLQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLIEDEIATILKSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITSIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDDFTDFVKKCLVKNPEQRATATQLLQHPFIKNAKPVSILRDLITEAMEIKAKRHEEQQRELEEEEENSDEDELDSHTMVKTSVESVGTMRATSTMSEGAQTMIEHNSTMLESDLGTMVINSEDEEEEDGTMKRNATSPQVQRPSFMDYFDKQDFKNKSHENCNQNMHEPFPMSKNVFPDNWKVPQDGDFDFLKNLSLEELQMRLKALDPMMEREIEELRQRYTAKRQPILDAMDAKKRRQQNF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q13188","disprot_id":"DP01461","ncbi_taxon_id":9606,"regions_counter":7,"creator":"vsagris","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":427,"region_id":"DP01461r001","released":"2022_06","ec_id":"ECO:0006165","reference_html":"Structural basis for autoactivation of human Mst2 kinase and its regulation by RASSF5. <i> Ni L, Li S, Yu J, Min J, Brautigam CA, Tomchick DR, Pan D, Luo X. </i> Structure, 2013","statement":[{"text":"By contrast, the 1H/15N TROSY-HSQC spectrum of the Mst2 mutant with its linker between the kinase and SARAH domains deleted (Mst2ΔL) had few sharp peaks, indicating that the Mst2 linker was natively unfolded (Figure S4B).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":314,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-05-31T15:09:51.111Z","reference_source":"pmid","term_name":"disorder","reference_id":"23972470","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T13:16:21.185Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":427,"term_name":"flexible linker","released":"2022_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis for autoactivation of human Mst2 kinase and its regulation by RASSF5. <i> Ni L, Li S, Yu J, Min J, Brautigam CA, Tomchick DR, Pan D, Luo X. </i> Structure, 2013","statement":[{"text":"By contrast, the 1H/15N TROSY-HSQC spectrum of the Mst2 mutant with its linker between the kinase and SARAH domains deleted (Mst2ΔL) had few sharp peaks, indicating that the Mst2 linker was natively unfolded (Figure S4B).","type":"Results"}],"term_id":"IDPO:0000033","curator_id":"fquaglia","start":314,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23972470","version":4,"curator_orcid":"0000-0002-0341-4888","date":"2022-05-31T15:09:55.678Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01461r002","ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T13:16:31.320Z"}},{"start":365,"end":367,"reference_id":"31857374","reference_source":"pmid","reference_html":"NIMA-related kinase 9-mediated phosphorylation of the microtubule-associated LC3B protein at Thr-50 suppresses selective autophagy of p62/sequestosome 1. <i> Shrestha BK, Skytte Rasmussen M, Abudu YP, Bruun JA, Larsen KB, Alemu EA, Sjøttem E, Lamark T, Johansen T. </i> J Biol Chem, 2020","date":"2022-06-17T11:33:35.885Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","region_id":"DP01461r003","statement":[{"text":"STK3 interacts with LC3C and GABARAP via a CLIR","type":"Results"},{"text":"Figure 1. STK3 interacts with LC3C and GABARAP via a C-type atypical LIR motif. E, schematic drawing of the domain organization of STK3 with the kinase domain, the LIR motif, and the SARAH domain indicated. The extent of deletion mutants and the location of the MVI/AAA LIR mutation are shown below the domain cartoon. G, and H, GST pulldown analyses of binding of Myc-tagged STK3 WT and LIR mutant translated in vitro in the presence of [35S]methionine to GST-LC3C (G) or Myc-tagged STK3 WT translated in vitro in the presence of [35S]methionine to GST-LC3C or GST-LC3C F58A (H). The F58A mutant inhibits binding to the LDS of LC3C. I, HEK293 cells were transiently transfected with FLAG-tagged constructs of STK3 WT and LIR mutant (MVI/AAA), and whole-cell lysates were incubated with recombinant GST or GST–ATG8s family proteins. ","type":"Figure"},{"text":"However, because STK3 also bound strongly to LC3C, we searched the C-terminal part of STK3 for CLIR with the consensus ΦΦΦ, where Φ is an aliphatic amino acid. ","type":"Results"},{"text":"A candidate CLIR, “MVI” was located at positions 365–367, reminiscent of the CLIR previously described for the interaction between CALCOCO2/NDP52 and LC3C (36).","type":"Results"},{"text":"Strikingly, mutation of this CLIR motif to AAA abolished binding between STK3 and LC3C (Fig. 1G). ","type":"Results"},{"text":"Consistently, mutation of the LDS in LC3C F58A resulted in a strongly-decreased binding to STK3 (Fig. 1H).","type":"Results"},{"text":"GST-pulldown assays using extracts from HeLa cells expressing the FLAG–STK3 or the FLAG–STK3 MVI/AAA CLIR mutant verified the strong binding of FLAG–STK3 to GABARAP and LC3C, whereas the CLIR mutant FLAG–STK3 MVI/AAA did not show significant binding.","type":"Results"},{"text":"Furthermore, the GABARAP Y49A LDS mutant displayed strongly-reduced binding to FLAG–STK3 (Fig. 1I).","type":"Results"},{"text":"Taken together, the results show that the CLIR motif in STK3 mediated LDS-dependent binding to both LC3C and GABARAP.","type":"Results"},{"text":"The annotation include the non canonical CLIR motif MVI at position 365 – 367.","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:49:49.868Z"}},{"start":365,"end":367,"reference_id":"31857374","reference_source":"pmid","reference_html":"NIMA-related kinase 9-mediated phosphorylation of the microtubule-associated LC3B protein at Thr-50 suppresses selective autophagy of p62/sequestosome 1. <i> Shrestha BK, Skytte Rasmussen M, Abudu YP, Bruun JA, Larsen KB, Alemu EA, Sjøttem E, Lamark T, Johansen T. </i> J Biol Chem, 2020","date":"2022-06-17T08:22:17.277Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IEP","region_id":"DP01461r004","statement":[{"text":"STK3 interacts with LC3C and GABARAP via a CLIR","type":"Results"},{"text":"GST pulldown assays using the various deletion constructs of STK3 identified the interaction to be mediated by the fragment encompassing the C-terminal region from amino acid position 323, and not the N-terminal part (from position 1 to 357) (Fig. 1F).","type":"Results"},{"text":"GABARAP was used as an interaction partner in these LIR-mapping experiments because it bound strongly to STK3.","type":"Results"},{"text":"Figure 1. STK3 interacts with LC3C and GABARAP via a C-type atypical LIR motif. , HEK293 cells were transiently co-transfected with the indicated FLAG-tagged kinases, wildtype (WT), or kinase-dead (KD), and either GFP–LC3B or GFP-GABARAP. Cell lysates were immunoprecipitated (IP) with FLAG antibodies and analyzed by Western blotting. B, Myc-tagged STK3 kinase constructs were translated in vitro in the presence of [35S]methionine and analyzed in GST affinity isolation experiments for binding to the indicated ATG8s fused to GST. Bound proteins were detected by autoradiography and immobilized GST or GST-tagged proteins visualized by Coomassie Brilliant Blue staining. C, quantification of STK3 binding shown in B and based on three independent experiments. Values are mean ± S.E. D, Myc-tagged STK4 kinase construct was translated in vitro in the presence of [35S]methionine and analyzed in GST affinity isolation experiments for binding to the indicated ATG8s fused to GST. E, schematic drawing of the domain organization of STK3 with the kinase domain, the LIR motif, and the SARAH domain indicated. The extent of deletion mutants and the location of the MVI/AAA LIR mutation are shown below the domain cartoon. G, and H, GST pulldown analyses of binding of Myc-tagged STK3 WT and LIR mutant translated in vitro in the presence of [35S]methionine to GST-LC3C (G) or Myc-tagged STK3 WT translated in vitro in the presence of [35S]methionine to GST-LC3C or GST-LC3C F58A (H). The F58A mutant inhibits binding to the LDS of LC3C. I, HEK293 cells were transiently transfected with FLAG-tagged constructs of STK3 WT and LIR mutant (MVI/AAA), and whole-cell lysates were incubated with recombinant GST or GST–ATG8s family proteins. The bound FLAG-tagged STK3 protein was detected by Western blotting using anti-FLAG antibodies and immobilized GST or GST-tagged proteins visualized by Ponceau S staining. AR, autoradiography; CBB, Coomassie Brilliant Blue.","type":"Figure"},{"text":"However, because STK3 also bound strongly to LC3C, we searched the C-terminal part of STK3 for CLIR with the consensus ΦΦΦ, where Φ is an aliphatic amino acid. ","type":"Results"},{"text":"A candidate CLIR, “MVI” was located at positions 365–367, reminiscent of the CLIR previously described for the interaction between CALCOCO2/NDP52 and LC3C (36).","type":"Results"},{"text":"Strikingly, mutation of this CLIR motif to AAA abolished binding between STK3 and LC3C (Fig. 1G). ","type":"Results"},{"text":"Consistently, mutation of the LDS in LC3C F58A resulted in a strongly-decreased binding to STK3 (Fig. 1H).","type":"Results"},{"text":"GST-pulldown assays using extracts from HeLa cells expressing the FLAG–STK3 or the FLAG–STK3 MVI/AAA CLIR mutant verified the strong binding of FLAG–STK3 to GABARAP and LC3C, whereas the CLIR mutant FLAG–STK3 MVI/AAA did not show significant binding.","type":"Results"},{"text":"Furthermore, the GABARAP Y49A LDS mutant displayed strongly-reduced binding to FLAG–STK3 (Fig. 1I).","type":"Results"},{"text":"Taken together, the results show that the CLIR motif in STK3 mediated LDS-dependent binding to both LC3C and GABARAP.","type":"Results"},{"text":"The annotation include the non canonical CLIR motif MVI at position 365 – 367.","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:49:53.918Z"}},{"start":365,"end":367,"reference_id":"31857374","reference_source":"pmid","reference_html":"NIMA-related kinase 9-mediated phosphorylation of the microtubule-associated LC3B protein at Thr-50 suppresses selective autophagy of p62/sequestosome 1. <i> Shrestha BK, Skytte Rasmussen M, Abudu YP, Bruun JA, Larsen KB, Alemu EA, Sjøttem E, Lamark T, Johansen T. </i> J Biol Chem, 2020","date":"2022-06-17T08:39:17.510Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006076","ec_ontology":"ECO","ec_name":"protein binding evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9BXW4","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"O95166","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01461r005","statement":[{"text":"STK3 interacts with LC3C and GABARAP via a CLIR","type":"Results"},{"text":"GST pulldown assays using the various deletion constructs of STK3 identified the interaction to be mediated by the fragment encompassing the C-terminal region from amino acid position 323, and not the N-terminal part (from position 1 to 357) (Fig. 1F).","type":"Results"},{"text":"GABARAP was used as an interaction partner in these LIR-mapping experiments because it bound strongly to STK3.","type":"Results"},{"text":"Figure 1. STK3 interacts with LC3C and GABARAP via a C-type atypical LIR motif. , HEK293 cells were transiently co-transfected with the indicated FLAG-tagged kinases, wildtype (WT), or kinase-dead (KD), and either GFP–LC3B or GFP-GABARAP. Cell lysates were immunoprecipitated (IP) with FLAG antibodies and analyzed by Western blotting. B, Myc-tagged STK3 kinase constructs were translated in vitro in the presence of [35S]methionine and analyzed in GST affinity isolation experiments for binding to the indicated ATG8s fused to GST. Bound proteins were detected by autoradiography and immobilized GST or GST-tagged proteins visualized by Coomassie Brilliant Blue staining. C, quantification of STK3 binding shown in B and based on three independent experiments. Values are mean ± S.E. D, Myc-tagged STK4 kinase construct was translated in vitro in the presence of [35S]methionine and analyzed in GST affinity isolation experiments for binding to the indicated ATG8s fused to GST. E, schematic drawing of the domain organization of STK3 with the kinase domain, the LIR motif, and the SARAH domain indicated. The extent of deletion mutants and the location of the MVI/AAA LIR mutation are shown below the domain cartoon. G, and H, GST pulldown analyses of binding of Myc-tagged STK3 WT and LIR mutant translated in vitro in the presence of [35S]methionine to GST-LC3C (G) or Myc-tagged STK3 WT translated in vitro in the presence of [35S]methionine to GST-LC3C or GST-LC3C F58A (H). The F58A mutant inhibits binding to the LDS of LC3C. I, HEK293 cells were transiently transfected with FLAG-tagged constructs of STK3 WT and LIR mutant (MVI/AAA), and whole-cell lysates were incubated with recombinant GST or GST–ATG8s family proteins. The bound FLAG-tagged STK3 protein was detected by Western blotting using anti-FLAG antibodies and immobilized GST or GST-tagged proteins visualized by Ponceau S staining. AR, autoradiography; CBB, Coomassie Brilliant Blue.","type":"Figure"},{"text":"However, because STK3 also bound strongly to LC3C, we searched the C-terminal part of STK3 for CLIR with the consensus ΦΦΦ, where Φ is an aliphatic amino acid. ","type":"Results"},{"text":"A candidate CLIR, “MVI” was located at positions 365–367, reminiscent of the CLIR previously described for the interaction between CALCOCO2/NDP52 and LC3C (36).","type":"Results"},{"text":"Strikingly, mutation of this CLIR motif to AAA abolished binding between STK3 and LC3C (Fig. 1G). ","type":"Results"},{"text":"Consistently, mutation of the LDS in LC3C F58A resulted in a strongly-decreased binding to STK3 (Fig. 1H).","type":"Results"},{"text":"GST-pulldown assays using extracts from HeLa cells expressing the FLAG–STK3 or the FLAG–STK3 MVI/AAA CLIR mutant verified the strong binding of FLAG–STK3 to GABARAP and LC3C, whereas the CLIR mutant FLAG–STK3 MVI/AAA did not show significant binding.","type":"Results"},{"text":"Furthermore, the GABARAP Y49A LDS mutant displayed strongly-reduced binding to FLAG–STK3 (Fig. 1I).","type":"Results"},{"text":"Taken together, the results show that the CLIR motif in STK3 mediated LDS-dependent binding to both LC3C and GABARAP.","type":"Results"},{"text":"The annotation include the non canonical CLIR motif MVI at position 365 – 367.","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:49:55.624Z"}},{"start":365,"end":367,"reference_id":"31857374","reference_source":"pmid","reference_html":"NIMA-related kinase 9-mediated phosphorylation of the microtubule-associated LC3B protein at Thr-50 suppresses selective autophagy of p62/sequestosome 1. <i> Shrestha BK, Skytte Rasmussen M, Abudu YP, Bruun JA, Larsen KB, Alemu EA, Sjøttem E, Lamark T, Johansen T. </i> J Biol Chem, 2020","date":"2022-06-17T10:07:32.280Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9BXW4","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"O95166","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01461r006","statement":[{"text":"STK3 interacts with LC3C and GABARAP via a CLIR","type":"Results"},{"text":"Figure 1. STK3 interacts with LC3C and GABARAP via a C-type atypical LIR motif. G, and H, GST pulldown analyses of binding of Myc-tagged STK3 WT and LIR mutant translated in vitro in the presence of [35S]methionine to GST-LC3C (G) or Myc-tagged STK3 WT translated in vitro in the presence of [35S]methionine to GST-LC3C or GST-LC3C F58A (H). The F58A mutant inhibits binding to the LDS of LC3C. I, HEK293 cells were transiently transfected with FLAG-tagged constructs of STK3 WT and LIR mutant (MVI/AAA), and whole-cell lysates were incubated with recombinant GST or GST–ATG8s family proteins. ","type":"Figure"},{"text":"GST-pulldown assays using extracts from HeLa cells expressing the FLAG–STK3 or the FLAG–STK3 MVI/AAA CLIR mutant verified the strong binding of FLAG–STK3 to GABARAP and LC3C, whereas the CLIR mutant FLAG–STK3 MVI/AAA did not show significant binding.","type":"Results"},{"text":"Furthermore, the GABARAP Y49A LDS mutant displayed strongly-reduced binding to FLAG–STK3 (Fig. 1I).","type":"Results"},{"text":"The annotation include the non canonical CLIR motif MVI at position 365 – 367.","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:49:56.888Z"}},{"start":365,"end":367,"reference_id":"31857374","reference_source":"pmid","reference_html":"NIMA-related kinase 9-mediated phosphorylation of the microtubule-associated LC3B protein at Thr-50 suppresses selective autophagy of p62/sequestosome 1. <i> Shrestha BK, Skytte Rasmussen M, Abudu YP, Bruun JA, Larsen KB, Alemu EA, Sjøttem E, Lamark T, Johansen T. </i> J Biol Chem, 2020","date":"2022-06-17T10:09:09.705Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9BXW4","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"O95166","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01461r007","statement":[{"text":"TK3 interacts with LC3C and GABARAP via a CLIR","type":"Results"},{"text":"Figure 1. STK3 interacts with LC3C and GABARAP via a C-type atypical LIR motif. G, and H, GST pulldown analyses of binding of Myc-tagged STK3 WT and LIR mutant translated in vitro in the presence of [35S]methionine to GST-LC3C (G) or Myc-tagged STK3 WT translated in vitro in the presence of [35S]methionine to GST-LC3C or GST-LC3C F58A (H). The F58A mutant inhibits binding to the LDS of LC3C. I, HEK293 cells were transiently transfected with FLAG-tagged constructs of STK3 WT and LIR mutant (MVI/AAA), and whole-cell lysates were incubated with recombinant GST or GST–ATG8s family proteins. ","type":"Figure"},{"text":"GST-pulldown assays using extracts from HeLa cells expressing the FLAG–STK3 or the FLAG–STK3 MVI/AAA CLIR mutant verified the strong binding of FLAG–STK3 to GABARAP and LC3C, whereas the CLIR mutant FLAG–STK3 MVI/AAA did not show significant binding.","type":"Results"},{"text":"Furthermore, the GABARAP Y49A LDS mutant displayed strongly-reduced binding to FLAG–STK3 (Fig. 1I).","type":"Results"},{"text":"The annotation include the non canonical CLIR motif MVI at position 365 – 367.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:49:58.499Z"}}],"released":"2018_11","uniref100":"UniRef100_Q13188","date":"2018-07-18T15:17:10.000Z","acc":"Q13188","name":"Serine/threonine-protein kinase 3","length":491,"organism":"Homo sapiens","dataset":["Autophagy-related proteins"],"UniParc":"UPI00001360FE","genes":[{"name":{"value":"STK3"},"synonyms":[{"value":"KRS1"},{"value":"MST2"}]}],"alphafold_very_low_content":0.23014256619144602,"disorder_content":0.23217922606924643,"disprot_consensus":{"full":[{"start":314,"end":427,"type":"D"}],"Structural state":[{"start":314,"end":427,"type":"D"}],"Disorder function":[{"start":314,"end":427,"type":"F"}],"Biological process":[{"start":365,"end":367,"type":"F"}],"Molecular function":[{"start":365,"end":367,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05110","name":"AF-4 proto-oncoprotein N-terminal region","start":3,"end":479},{"id":"PF18875","name":"AF4 interaction motif","start":714,"end":728},{"id":"PF18876","name":"AFF4, C-terminal homology domain","start":898,"end":1161}]},"uniref50":"UniRef50_Q9UHB7","sequence":"MNREDRNVLRMKERERRNQEIQQGEDAFPPSSPLFAEPYKVTSKEDKLSSRIQSMLGNYDEMKDFIGDRSIPKLVAIPKPTVPPSADEKSNPNFFEQRHGGSHQSSKWTPVGPAPSTSQSQKRSSGLQSGHSSQRTSAGSSSGTNSSGQRHDRESYNNSGSSSRKKGQHGSEHSKSRSSSPGKPQAVSSLNSSHSRSHGNDHHSKEHQRSKSPRDPDANWDSPSRVPFSSGQHSTQSFPPSLMSKSNSMLQKPTAYVRPMDGQESMEPKLSSEHYSSQSHGNSMTELKPSSKAHLTKLKIPSQPLDASASGDVSCVDEILKEMTHSWPPPLTAIHTPCKTEPSKFPFPTKESQQSNFGTGEQKRYNPSKTSNGHQSKSMLKDDLKLSSSEDSDGEQDCDKTMPRSTPGSNSEPSHHNSEGADNSRDDSSSHSGSESSSGSDSESESSSSDSEANEPSQSASPEPEPPPTNKWQLDNWLNKVNPHKVSPASSVDSNIPSSQGYKKEGREQGTGNSYTDTSGPKETSSATPGRDSKTIQKGSESGRGRQKSPAQSDSTTQRRTVGKKQPKKAEKAAAEEPRGGLKIESETPVDLASSMPSSRHKAATKGSRKPNIKKESKSSPRPTAEKKKYKSTSKSSQKSREIIETDTSSSDSDESESLPPSSQTPKYPESNRTPVKPSSVEEEDSFFRQRMFSPMEEKELLSPLSEPDDRYPLIVKIDLNLLTRIPGKPYKETEPPKGEKKNVPEKHTREAQKQASEKVSNKGKRKHKNEDDNRASESKKPKTEDKNSAGHKPSSNRESSKQSAAKEKDLLPSPAGPVPSKDPKTEHGSRKRTISQSSSLKSSSNSNKETSGSSKNSSSTSKQKKTEGKTSSSSKEVKEKAPSSSSNCPPSAPTLDSSKPRRTKLVFDDRNYSADHYLQEAKKLKHNADALSDRFEKAVYYLDAVVSFIECGNALEKNAQESKSPFPMYSETVDLIKYTMKLKNYLAPDATAADKRLTVLCLRCESLLYLRLFKLKKENALKYSKTLTEHLKNSYNNSQAPSPGLGSKAVGMPSPVSPKLSPGNSGNYSSGASSASASGSSVTIPQKIHQMAASYVQVTSNFLYATEIWDQAEQLSKEQKEFFAELDKVMGPLIFNASIMTDLVRYTRQGLHWLRQDAKLIS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UHB7","disprot_id":"DP01463","ncbi_taxon_id":9606,"regions_counter":10,"creator":"rdavidovic","regions":[{"region_id":"DP01463r001","ec_ontology":"ECO","end":32,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":22,"version":3,"statement":[{"text":"The lack of electron density in the PDB indicates this region is disordered.","type":"Figure"}],"term_name":"disorder","reference_html":"The AFF4 scaffold binds human P-TEFb adjacent to HIV Tat. <i> Schulze-Gahmen U, Upton H, Birnberg A, Bao K, Chou S, Krogan NJ, Zhou Q, Alber T. </i> Elife, 2013","released":"2022_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"23471103","date":"2022-06-23T15:47:41.308Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4IMY"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60563 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P50750"}],"sequence_construct":"SNANREDRNVLRMKERERRNQEIQQGEDAFPPSSPLFAEPYKVTSKEDKLSSRIQSMLGNYDEMKDFIGDRSIPK","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-25T20:34:52.681Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":73,"term_name":"protein binding","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"The AFF4 scaffold binds human P-TEFb adjacent to HIV Tat. <i> Schulze-Gahmen U, Upton H, Birnberg A, Bao K, Chou S, Krogan NJ, Zhou Q, Alber T. </i> Elife, 2013","statement":[{"text":"Tandem  alanine  replacements  in  residues  3–32,  which  flank  the ordered  CycT1  contacts  in  the  crystal  structure,  showed  significant  but generally  smaller effects  on AFF4 transcriptional stimulation activity. These results implicate the P-TEFb binding site, as well as the flanking flexible sequences, in the function of the AFF4 N-terminal segment.","type":"Results"},{"text":"Residues 2–73 of AFF4, for example, are sufficient to bind P-TEFb through the CycT1 subunit, and a peptide encompassing AFF42–73 folds upon binding CycT1.","type":"Results"}],"term_id":"GO:0005515","curator_id":"vnugnes","start":2,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"23471103","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-23T17:15:07.336Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01463r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"O60563","operator":"and","partner_start":null,"partner_end":null}],"sequence_construct":"SNANREDRNVLRMKERERRNQEIQQGEDAFPPSSPLFAEPYKVTSKEDKLSSRIQSMLGNYDEMKDFIGDRSIPK","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-25T20:35:02.072Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":300,"region_id":"DP01463r003","released":"2022_06","ec_id":"ECO:0007691","reference_html":"HIV-1 Tat recruits transcription elongation factors dispersed along a flexible AFF4 scaffold. <i> Chou S, Upton H, Bao K, Schulze-Gahmen U, Samelson AJ, He N, Nowak A, Lu H, Krogan NJ, Zhou Q, Alber T. </i> Proc Natl Acad Sci U S A, 2013","statement":[{"text":"AFF41–300, AFF4300–600, and AFF4600–900 were hypersensitive to proteinase K (Fig. 2B). Limited proteolysis failed to produce large, stable fragments of these AFF4 polypeptides, suggesting intrinsic disorder over the entire sequence.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-15T20:15:39.016Z","reference_source":"pmid","term_name":"disorder","reference_id":"23251033","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-25T20:34:50.733Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":600,"region_id":"DP01463r005","released":"2022_06","ec_id":"ECO:0007691","reference_html":"HIV-1 Tat recruits transcription elongation factors dispersed along a flexible AFF4 scaffold. <i> Chou S, Upton H, Bao K, Schulze-Gahmen U, Samelson AJ, He N, Nowak A, Lu H, Krogan NJ, Zhou Q, Alber T. </i> Proc Natl Acad Sci U S A, 2013","statement":[{"text":"AFF41–300, AFF4300–600, and AFF4600–900 were hypersensitive to proteinase K (Fig. 2B). Limited proteolysis failed to produce large, stable fragments of these AFF4 polypeptides, suggesting intrinsic disorder over the entire sequence.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":300,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-15T20:15:21.704Z","reference_source":"pmid","term_name":"disorder","reference_id":"23251033","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-25T20:34:54.375Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":900,"region_id":"DP01463r007","released":"2022_06","ec_id":"ECO:0007691","reference_html":"HIV-1 Tat recruits transcription elongation factors dispersed along a flexible AFF4 scaffold. <i> Chou S, Upton H, Bao K, Schulze-Gahmen U, Samelson AJ, He N, Nowak A, Lu H, Krogan NJ, Zhou Q, Alber T. </i> Proc Natl Acad Sci U S A, 2013","statement":[{"text":"AFF41–300, AFF4300–600, and AFF4600–900 were hypersensitive to proteinase K (Fig. 2B). Limited proteolysis failed to produce large, stable fragments of these AFF4 polypeptides, suggesting intrinsic disorder over the entire sequence.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":600,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-15T20:15:12.757Z","reference_source":"pmid","term_name":"disorder","reference_id":"23251033","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-25T20:34:56.073Z"}},{"start":5,"end":23,"reference_id":"23471103","reference_source":"pmid","reference_html":"The AFF4 scaffold binds human P-TEFb adjacent to HIV Tat. <i> Schulze-Gahmen U, Upton H, Birnberg A, Bao K, Chou S, Krogan NJ, Zhou Q, Alber T. </i> Elife, 2013","date":"2022-06-23T17:16:02.334Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"4IMY"}],"region_id":"DP01463r009","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60563"}],"statement":[{"text":"Residues 2–73 of AFF4, for example, are sufficient to bind P-TEFb through the CycT1 subunit, and a peptide encompassing AFF42–73 folds upon binding CycT1. ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-25T20:34:57.603Z"}},{"start":36,"end":69,"reference_id":"23471103","reference_source":"pmid","reference_html":"The AFF4 scaffold binds human P-TEFb adjacent to HIV Tat. <i> Schulze-Gahmen U, Upton H, Birnberg A, Bao K, Chou S, Krogan NJ, Zhou Q, Alber T. </i> Elife, 2013","date":"2022-06-23T17:15:52.568Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"4IMY"}],"region_id":"DP01463r010","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60563"}],"statement":[{"text":"Residues 2–73 of AFF4, for example, are sufficient to bind P-TEFb through the CycT1 subunit, and a peptide encompassing AFF42–73 folds upon binding CycT1. ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-25T20:35:00.737Z"}}],"released":"2018_11","uniref100":"UniRef100_Q9UHB7","date":"2018-07-19T07:13:48.000Z","acc":"Q9UHB7","name":"AF4/FMR2 family member 4","length":1163,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI000006F558","genes":[{"name":{"value":"AFF4"},"synonyms":[{"value":"AF5Q31"},{"value":"MCEF"}],"orfNames":[{"value":"HSPC092"}]}],"alphafold_very_low_content":0.6870163370593293,"disorder_content":0.7738607050730868,"disprot_consensus":{"full":[{"start":1,"end":4,"type":"D"},{"start":5,"end":23,"type":"T"},{"start":24,"end":35,"type":"D"},{"start":36,"end":69,"type":"T"},{"start":70,"end":900,"type":"D"}],"Structural state":[{"start":1,"end":900,"type":"D"}],"Molecular function":[{"start":2,"end":73,"type":"F"}],"Structural transition":[{"start":5,"end":23,"type":"T"},{"start":36,"end":69,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00029","name":"Connexin","start":2,"end":254}],"gene3D":[{"start":1,"end":267,"id":"1.20.1440.80","name":"Gap junction channel protein cysteine-rich domain"}]},"uniref50":"UniRef50_P28229","sequence":"MSWSFLTRLLEEIHNHSTFVGKIWLTVLIVFRIVLTAVGGESIYYDEQSKFVCNTEQPGCENVCYDAFAPLSHVRFWVFQIILVATPSVMYLGYAIHKIAKMEHGEADKKAARSKPYAMRWKQHRALEETEEDHEEDPMMYPEMELESEKENKEQSQPKPKHDGRRRIREDGLMKIYVLQLLARTVFEVGFLIGQYFLYGFQVHPFYVCSRLPCPHKIDCFISRPTEKTIFLLIMYGVTGLCLLLNIWEMLHLGFGTIRDSLNSKRRELDDPGAYNYPFTWNTPSAPPGYNIAVKPDQIQYTELSNAKIAYKQNKANIAQEQQYGSHEEHLPADLETLQREIRMAQERLDLAIQAYHHQNNPHGPREKKAKVGSKSGSNKSSISSKSGDGKTSVWI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P28229","disprot_id":"DP01464","ncbi_taxon_id":10090,"regions_counter":5,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":332,"region_id":"DP01464r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Characterization of the connexin45 carboxyl-terminal domain structure and interactions with molecular partners. <i> Kopanic JL, Al-mugotir MH, Kieken F, Zach S, Trease AJ, Sorgen PL. </i> Biophys J, 2014","statement":[{"text":"In general, the structure of the Cx45, Cx43, and Cx40 CT domains are predominantly intrinsically disordered with varying degrees of a-helical content... The Cx45CT domain contains the largest amount of a-helical structure (19% total a-helical content), which is within one region (A333-N361).","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":265,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24853747","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":332,"region_id":"DP01464r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Characterization of the connexin45 carboxyl-terminal domain structure and interactions with molecular partners. <i> Kopanic JL, Al-mugotir MH, Kieken F, Zach S, Trease AJ, Sorgen PL. </i> Biophys J, 2014","statement":[{"text":"The data are characteristic of a protein that contains both a-helical and random coil structures... The CD data indicate that Cx45CT residues A333-N361 are predominantly a-helical.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":265,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24853747","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":332,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Characterization of the connexin45 carboxyl-terminal domain structure and interactions with molecular partners. <i> Kopanic JL, Al-mugotir MH, Kieken F, Zach S, Trease AJ, Sorgen PL. </i> Biophys J, 2014","statement":[{"text":"all of the molecular partners studied here interacted in the intrinsically disordered regions of the Cx45CT","type":"Discussion"}],"term_id":"GO:0005515","curator_id":"eschad","start":265,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"24853747","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01464r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":396,"region_id":"DP01464r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Characterization of the connexin45 carboxyl-terminal domain structure and interactions with molecular partners. <i> Kopanic JL, Al-mugotir MH, Kieken F, Zach S, Trease AJ, Sorgen PL. </i> Biophys J, 2014","statement":[{"text":"In general, the structure of the Cx45, Cx43, and Cx40 CT domains are predominantly intrinsically disordered with varying degrees of a-helical content... The Cx45CT domain contains the largest amount of a-helical structure (19% total a-helical content), which is within one region (A333-N361).","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":362,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24853747","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":396,"region_id":"DP01464r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Characterization of the connexin45 carboxyl-terminal domain structure and interactions with molecular partners. <i> Kopanic JL, Al-mugotir MH, Kieken F, Zach S, Trease AJ, Sorgen PL. </i> Biophys J, 2014","statement":[{"text":"The data are characteristic of a protein that contains both a-helical and random coil structures... The CD data indicate that Cx45CT residues A333-N361 are predominantly a-helical.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":362,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24853747","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P28229","date":"2018-07-19T09:58:55.000Z","acc":"P28229","name":"Gap junction gamma-1 protein","length":396,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000263BD","genes":[{"name":{"value":"Gjc1"},"synonyms":[{"value":"Cxn-45"},{"value":"Gja7"}]}],"alphafold_very_low_content":0.2828282828282828,"disorder_content":0.2601010101010101,"disprot_consensus":{"full":[{"start":265,"end":332,"type":"D"},{"start":362,"end":396,"type":"D"}],"Structural state":[{"start":265,"end":332,"type":"D"},{"start":362,"end":396,"type":"D"}],"Molecular function":[{"start":265,"end":332,"type":"F"}]}},{"features":{"pfam":[{"id":"PF10283","name":"PBZ domain","start":376,"end":401},{"id":"PF10283","name":"PBZ domain","start":418,"end":442},{"id":"PF17913","name":"FHA domain","start":17,"end":64}],"gene3D":[{"start":4,"end":103,"id":"2.60.200.20","name":"2.60.200.20"}]},"uniref50":"UniRef50_Q8IW19","sequence":"MSGGFELQPRDGGPRVALAPGETVIGRGPLLGITDKRVSRRHAILEVAGGQLRIKPIHTNPCFYQSSEKSQLLPLKPNLWCYLNPGDSFSLLVDKYIFRILSIPSEVEMQCTLRNSQVLDEDNILNETPKSPVINLPHETTGASQLEGSTEIAKTQMTPTNSVSFLGENRDCNKQQPILAERKRILPTWMLAEHLSDQNLSVPAISGGNVIQGSGKEEICKDKSQLNTTQQGRRQLISSGSSENTSAEQDTGEECKNTDQEESTISSKEMPQSFSAITLSNTEMNNIKTNAQRNKLPIEELGKVSKHKIATKRTPHKEDEAMSCSENCSSAQGDSLQDESQGSHSESSSNPSNPETLHAKATDSVLQGSEGNKVKRTSCMYGANCYRKNPVHFQHFSHPGDSDYGGVQIVGQDETDDRPECPYGPSCYRKNPQHKIEYRHNTLPVRNVLDEDNDNVGQPNEYDLNDSFLDDEEEDYEPTDEDSDWEPGKEDEEKEDVEELLKEAKRFMKRK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q8IW19","disprot_id":"DP01465","ncbi_taxon_id":9606,"regions_counter":5,"creator":"ldobson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":420,"region_id":"DP01465r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure and identification of ADP-ribose recognition motifs of APLF and role in the DNA damage response. <i> Li GY, McCulloch RD, Fenton AL, Cheung M, Meng L, Ikura M, Koch CA. </i> Proc Natl Acad Sci U S A, 2010","statement":[{"text":"ZF1 and ZF2 are well-struc- tured, nearly identical in their folds (rmsd 1⁄4 1.1 Å), and are con- nected via a 22-residue linker (residues 399–420), which appears to be largely flexible thus causing some degree of freedom in the domain orientation","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":399,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20439749","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":420,"term_name":"flexible linker","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structure and identification of ADP-ribose recognition motifs of APLF and role in the DNA damage response. <i> Li GY, McCulloch RD, Fenton AL, Cheung M, Meng L, Ikura M, Koch CA. </i> Proc Natl Acad Sci U S A, 2010","statement":[{"text":"Collectively, our structure and NMR data show that APLF TZF is made up with two relatively independent domains connected by a largely flexible linker due to the high degree of internal mobility of residues G406–D416.","type":"Discussion"}],"term_id":"IDPO:0000033","curator_id":"eschad","start":399,"term_ontology":"IDPO","curator_name":"Eva Schad","reference_id":"20439749","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01465r002","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":511,"region_id":"DP01465r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"DNA repair factor APLF acts as a H2A-H2B histone chaperone through binding its DNA interaction surface. <i> Corbeski I, Dolinar K, Wienk H, Boelens R, van Ingen H. </i> Nucleic Acids Res, 2018","statement":[{"text":"All backbone amide protons resonate in a narrow\nspectral region between 7.8 and 8.7 ppm, indicating\nthat APLFAD is mostly unstructured in solution.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":450,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29905837","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":511,"term_name":"protein folding chaperone","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"DNA repair factor APLF acts as a H2A-H2B histone chaperone through binding its DNA interaction surface. <i> Corbeski I, Dolinar K, Wienk H, Boelens R, van Ingen H. </i> Nucleic Acids Res, 2018","statement":[{"text":"We have performed structural investigation\non the recognition of H2A-H2B dimers and we present evidence that APLF can function as a true H2AH2B\nchaperone.","type":"Discussion"}],"term_id":"GO:0044183","curator_id":"eschad","start":450,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"29905837","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01465r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":511,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"DNA repair factor APLF acts as a H2A-H2B histone chaperone through binding its DNA interaction surface. <i> Corbeski I, Dolinar K, Wienk H, Boelens R, van Ingen H. </i> Nucleic Acids Res, 2018","statement":[{"text":"We find that APLFAD binds comparably to both (H3-\nH4)2 and H2A-H2B, implying that APLF is a generic histone\nchaperone without specificity for either type of histone\ncomplex.","type":"Discussion"}],"term_id":"GO:0005515","curator_id":"eschad","start":450,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"29905837","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01465r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q8IW19","date":"2018-07-19T11:12:36.000Z","acc":"Q8IW19","name":"Aprataxin and PNK-like factor","length":511,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000074578","genes":[{"name":{"value":"APLF","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"17353262","url":"http://www.ncbi.nlm.nih.gov/pubmed/17353262","alternativeUrl":"https://europepmc.org/abstract/MED/17353262"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:28724","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:28724"}}]},"synonyms":[{"value":"C2orf13","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:28724","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:28724"}}]},{"value":"PALF","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"17396150","url":"http://www.ncbi.nlm.nih.gov/pubmed/17396150","alternativeUrl":"https://europepmc.org/abstract/MED/17396150"}}]},{"value":"XIP1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"17507382","url":"http://www.ncbi.nlm.nih.gov/pubmed/17507382","alternativeUrl":"https://europepmc.org/abstract/MED/17507382"}}]}]}],"alphafold_very_low_content":0.49902152641878667,"disorder_content":0.1643835616438356,"disprot_consensus":{"full":[{"start":399,"end":420,"type":"D"},{"start":450,"end":511,"type":"D"}],"Structural state":[{"start":399,"end":420,"type":"D"},{"start":450,"end":511,"type":"D"}],"Disorder function":[{"start":399,"end":420,"type":"F"}],"Molecular function":[{"start":450,"end":511,"type":"F"}]}},{"acc":"A4L7I2","sequence":"MDSVYVDIDADSAFLKALQRAYPMFEVEPRQVTSNDHANARAFSHLAIKLIEQEIDPDSTILDIGSAPARRMMSDRKYHCVCPMRSAEDPERLANYARKLASAAGKVLDRNISGKIGDLQAVMAVPDTETPTFCLHTDVSCRQRADVAIYQDVYAVHAPTSLYHQAIKGVRVAYWVGFDTTPFMYNAMAGAYPSYSTNWADEQVLKAKNIGLCSTDLTEGRRGKLSIMRGKKLKPCDRVLFSVGSTLYPESRTLLKSWHLPSVFHLKGKLSFTCRCDTVVSCEGYVVKRITMSPGLYGKTTGYAVTHHADGFLMCKTTDTVDGERVSFSVCTYVPATICDQMTGILATEVTPEDAQKLLVGLNQRIVVNGRTQRNTNTMKNYLLPVVAQAFSKWAKECRKDMEDEKLLGVRERTLTCCCLWAFKKQKTHTVYKRPDTQSIQKVQAEFDSFVVPGLWSSGLSIPLRTRIKWLLRKVPKTDLIPYSGNAQEAQDAEKEAEEEREAELTHEALPPLQAAQEDVQVEIDVEQLEDRAGAGIIETPRGAIKVTAQLTDHVVGEYLVLSPQTVLRSQKLSLIHALAEQVKTCTHSGRAGRYAVEAYDGRVLVPSGYAISPEDFQSLSESATMVYNEREFVNRKLHHIAMHGPALNTDEESYELVRAERTEHEYVYDVDQRRCCKKEEAAGLVLVGDLTNPPYHEFAYEGLKIRPACPYKIAVIGVFGVPGSGKSAIIKNLVTRQDLVTSGKKENCQEISTDVMRQRGLEISARTVDSLLLNGCNRPVDVLYVDEAFACHSGTLLALIALVRPRQKVVLCGDPKQCGFFNMMQMKVNYNHNICTQVYHKSISRRCTLPVTAIVSSLHYEGKMRTTNEYNMPIVVDTTGSTKPDPGDLVLTCFRGWVKQLQIDYRGHEVMTAAASQGLTRKGVYAVRQKVNENPLYASTSEHVNVLLTRTEGKLVWKTLSGDPWIKTLQNPPKGNFKATIKEWEVEHASIMAGICSHQVTFDTFQNKANVCWAKSLVPILETAGIKLNDRQWSQIIQAFKEDKAYSPEVALNEICTRMYGVDLDSGLFSKPLVSVYYADNHWDNRPGGKMFGFNPEAASILERKYPFTKGKWNINKQICVTTRRIEDFNPTTNIIPVNRRLPHSLVAEHRPVKGERMEWLVNKINGHHVLLVSGYNLALPTKRVTWVAPLGVRGADYTYNLELGLPATLGRYDLVVINIHTPFRIHHYQQCVDHAMKLQMLGGDSLRLLKPGGSLLIRAYGYADRTSERVICVLGRKFRSSRALKPPCVTSNTEMFFLFSNFDNGRRNFTTHVMNNQLNAAFVGQATRAGCAPSYRVKRMDIAKNDEECVVNAANPRGLPGDGVCKAVYKKWPESFKNSATPVGTAKTVMCGTYPVIHAVGPNFSNYSESEGDRELAAAYREVAKEVTRLGVNSVAIPLLSTGVYSGGKDRLTQSLNHLFTAMDSTDADVVIYCRDKEWEKKISEAIQMRTQVELLDEHISIDCDVIRVHPDSSLAGRKGYSTTEGALYSYLEGTRFHQTAVDMAEIYTMWPKQTEANEQVCLYALGESIESIRQKCPVDDADASSPPKTVPCLCRYAMTPERVTRLRMNHVTNIIVCSSFPLPKYKIEGVQKVKCSKVMLFDHNVPSRVSPREYRSSQESVQEVSTTTSLTHSQFDLSADGETLPVPSDLDADAPALEPALDDGAVHTLPTIIGNLAAVSDWVMSTVPVAPPRRRRGRNLTVTCDEREGNITPMASVRFFRAELCPAVQETAETRDTAISLQAPPSTTMELSHPPISFGAPSETFPITFGDFDEGEIESLSSELLTFGDFLPGEVDDLTDSDWSTCPDTDDELXLDRAGGYIFSSDTGPGHLQQKSVRQSVLPVNTLEEVHEEKCYPPKLDELKEQLLLKKLQESASMANRSRYQSRKVENMKATIIQRLKRGCKLYLMAETPKVPTYRTIYPAPVYSPPINVRLSNPESAVAACNEFLARNYPTVSSYQITDEYDAYLDMVDGSESCLDRATFNPSKLRSYPKQHAYHAPSIRSAVPSPFQNTLQNVLAAATKRNCNVTQMRELPTLDSAVFNVECFKKFACNREYWEEFAASPIRITTENLTTYVTKLKGPKAAALFAKTHNLLPLQDVPMDRFTVDMKRDVKVTPGTKHTEERPKVQVIQAAEPLATAYLCGIHRELVRRLNAVLLPNVHTLFDMSAEDFDAIIAAHFKPGDAVLETDIASFDKSQDDSLALTALMLLEDLGVDHSLLDLIEAAFGEISSCHLPTGTRFKFGAMMKSGMFLTLFVNTLLNITIASRVLEDRLTKSACAAFIGDDNIIHGVVSDELMAARCATWMNMEVKIIDAVVSQKAPYFCGGFILHDTVTGTACRVADPLKRLFKLGKPLAAGDEQDEDRRRALADEVIRWQRTGLIDELEKAVYSRYEVQGISVAVMSMATFASSRSNFEKLRGPVITLYGGPK","creator":"mmacossay","dataset":["Viral proteins","Neglected tropical diseases proteins"],"date":"2018-07-19T14:33:39.000Z","disprot_id":"DP01466","features":{"pfam":[],"gene3D":[{"start":843,"end":982,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d90b9"},{"start":1003,"end":1140,"id":"3.90.70.110","name":"Alphavirus nsP2 protease domain","_id":"685af523b4ac24d5329d90ba"},{"start":1337,"end":1493,"id":"3.40.220.10","name":"Leucine Aminopeptidase, subunit E, domain 1","_id":"685af523b4ac24d5329d90bb"},{"start":1145,"end":1506,"id":"3.40.50.150","name":"Vaccinia Virus protein VP39","_id":"685af523b4ac24d5329d90bc"},{"start":713,"end":842,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d90bd"}]},"genes":[{"name":{"value":"CHIKVgp1","evidences":[{"source":{"id":"ABO38820.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/ABO38820.1","_id":"685af523b4ac24d5329d90f0"},"code":"ECO:0000313","_id":"685af523b4ac24d5329d90ef"}],"_id":"685af523b4ac24d5329d90f1"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d90ee"}],"length":2474,"name":"Nonstructural polyprotein","ncbi_taxon_id":37124,"organism":"Chikungunya virus","regions_counter":9,"released":"2018_11","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Alsuviricetes","Martellivirales","Togaviridae","Alphavirus"],"UniParc":"UPI0000F6DAAB","uniref100":"UniRef100_A4L7I2","uniref50":"UniRef50_P08411","uniref90":"UniRef90_Q8JUX6","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1658,"end":1856,"interaction_partner":[],"reference_html":"Multiple Host Factors Interact with the Hypervariable Domain of Chikungunya Virus nsP3 and Determine Viral Replication in Cell-Specific Mode. <i> Meshram CD, Agback P, Shiliaev N, Urakova N, Mobley JA, Agback T, Frolova EI, Frolov I. </i> J Virol, 2018","reference_id":"29899097","region_id":"DP01466r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"It exhibits a reduced chemical shift dispersion, especially in the 1H dimension between 8.5 and 7.5 ppm (Fig. 1C), which is a characteristic of the intrinsically disordered proteins (42).","_id":"685af523b4ac24d5329d90bf"},{"type":"Discussion","text":"We carried out detailed characterization of a 199-aa-long CHIKV HVD by NMR spectroscopy at atomic resolution. The results revealed the absence of stable secondary structures in this domain and clearly demonstrated that CHIKV HVD was present in solution in a disordered conformation.","_id":"685af523b4ac24d5329d90c0"},{"type":"Curator statement","text":"IDR in the publication is 100% identical to this Uniprot sequence.","_id":"685af523b4ac24d5329d90c1"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T09:01:17.430Z","_id":"685af523b4ac24d5329d90c2"},"version":3,"_id":"685af523b4ac24d5329d90be","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-09T08:28:47.645Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006030","ec_name":"co-immunoprecipitation evidence used in manual assertion","ec_ontology":"ECO","start":1658,"end":1856,"interaction_partner":[{"db":"UniProt","id":"Q96B97","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d90cb"},{"db":"UniProt","id":"Q9Y5K6","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d90cc"},{"db":"UniProt","id":"O00499","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d90cd"},{"db":"UniProt","id":"A0A182G3T6","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d90ce"}],"reference_html":"Multiple Host Factors Interact with the Hypervariable Domain of Chikungunya Virus nsP3 and Determine Viral Replication in Cell-Specific Mode. <i> Meshram CD, Agback P, Shiliaev N, Urakova N, Mobley JA, Agback T, Frolova EI, Frolov I. </i> J Virol, 2018","reference_id":"29899097","region_id":"DP01466r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":" In vertebrate cells, CHIKV HVD also coimmunoprecipitated cellular SH3-binding proteins BIN1, CD2AP, and SH3KBP1. In mosquito C7/10 cells, it interacted with A0A182G3T6, the mosquito BIN1 homolog (Fig. 6B). Interestingly, isolation of CD2AP/SH3KBP1 and BIN1 was strongly dependent on the cell type. In human Huh7 and mouse NIH 3T3 cells (35), BIN1, but not CD2AP or SH3KBP1, efficiently interacted with CHIKV HVD. However, in another human cell line, HEK 293 cells, CHIKV HVD preferentially interacted with CD2AP and SH3KBP1, but not with BIN1.","_id":"685af523b4ac24d5329d90c8"},{"type":"Discussion","text":"In the case of CHIKV, G3BP binding is particularly critical. In contrast to the results of the studies performed on SINV and SFV, deletion of even a single element of the G3BP-binding HVD repeat had a strong negative effect on CHIKV replication in both vertebrate and mosquito cells (Fig. 2) (34). Deletion of both elements, in turn, completely abrogated virus replication.","_id":"685af523b4ac24d5329d90c9"},{"type":"Curator statement","text":"IDR in the publication is 100% identical to this Uniprot sequence.","_id":"685af523b4ac24d5329d90ca"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-16T17:46:03.030Z","_id":"685af523b4ac24d5329d90cf"},"version":2,"_id":"685af523b4ac24d5329d90c7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-09T08:29:30.760Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006030","ec_name":"co-immunoprecipitation evidence used in manual assertion","ec_ontology":"ECO","start":1658,"end":1856,"interaction_partner":[{"db":"UniProt","id":"Q96B97","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d90d3"},{"db":"UniProt","id":"Q9Y5K6","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d90d4"},{"db":"UniProt","id":"O00499","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d90d5"},{"db":"UniProt","id":"A0A182G3T6","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d90d6"}],"reference_html":"Multiple Host Factors Interact with the Hypervariable Domain of Chikungunya Virus nsP3 and Determine Viral Replication in Cell-Specific Mode. <i> Meshram CD, Agback P, Shiliaev N, Urakova N, Mobley JA, Agback T, Frolova EI, Frolov I. </i> J Virol, 2018","reference_id":"29899097","region_id":"DP01466r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":" In vertebrate cells, CHIKV HVD also coimmunoprecipitated cellular SH3-binding proteins BIN1, CD2AP, and SH3KBP1. In mosquito C7/10 cells, it interacted with A0A182G3T6, the mosquito BIN1 homolog (Fig. 6B). Interestingly, isolation of CD2AP/SH3KBP1 and BIN1 was strongly dependent on the cell type. In human Huh7 and mouse NIH 3T3 cells (35), BIN1, but not CD2AP or SH3KBP1, efficiently interacted with CHIKV HVD. However, in another human cell line, HEK 293 cells, CHIKV HVD preferentially interacted with CD2AP and SH3KBP1, but not with BIN1.","_id":"685af523b4ac24d5329d90d1"},{"type":"Curator statement","text":"IDR in the publication is 100% identical to this Uniprot sequence.","_id":"685af523b4ac24d5329d90d2"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_go_domain":"F","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-16T18:01:40.662Z","_id":"685af523b4ac24d5329d90d7"},"version":2,"_id":"685af523b4ac24d5329d90d0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IEP","ec_id":"ECO:0005636","ec_name":"green fluorescent protein reporter gene assay evidence used in manual assertion","ec_ontology":"ECO","start":1658,"end":1856,"interaction_partner":[],"reference_html":"Multiple Host Factors Interact with the Hypervariable Domain of Chikungunya Virus nsP3 and Determine Viral Replication in Cell-Specific Mode. <i> Meshram CD, Agback P, Shiliaev N, Urakova N, Mobley JA, Agback T, Frolova EI, Frolov I. </i> J Virol, 2018","reference_id":"29899097","region_id":"DP01466r005","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"In the case of CHIKV, G3BP binding is particularly critical. In contrast to the results of the studies performed on SINV and SFV, deletion of even a single element of the G3BP-binding HVD repeat had a strong negative effect on CHIKV replication in both vertebrate and mosquito cells (Fig. 2) (34). Deletion of both elements, in turn, completely abrogated virus replication.","_id":"685af523b4ac24d5329d90d9"},{"type":"Results","text":"These experimental data strongly suggested that HVDs play critical roles in the adaptation of CHIKV and EILV to replication in particular cell types. Despite having very similar G3BP-binding repeating peptides, heterologous HVDs changed cell specificities of replication for both viruses. This was a strong support for the hypothesis that HVD fragments located upstream of the carboxy-terminal G3BP/Rin-binding repeat play an indispensable role in CHIKV replication.","_id":"685af523b4ac24d5329d90da"},{"type":"Curator statement","text":"IDR in the publication is 100% identical to this Uniprot sequence.","_id":"685af523b4ac24d5329d90db"}],"states_connection":[],"term_comment":"","term_def":"\"A set of processes which all viruses follow to ensure survival; includes attachment and entry of the virus particle, decoding of genome information, translation of viral mRNA by host ribosomes, genome replication, and assembly and release of viral particles containing the genome.\" [ISBN:1555811272]","term_go_domain":"P","term_id":"GO:0019058","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral life cycle","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T09:01:26.230Z","_id":"685af523b4ac24d5329d90dc"},"version":1,"_id":"685af523b4ac24d5329d90d8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IEP","ec_id":"ECO:0000279","ec_name":"qualitative western immunoblotting evidence used in manual assertion","ec_ontology":"ECO","start":1761,"end":1856,"interaction_partner":[],"reference_html":"Multiple Host Factors Interact with the Hypervariable Domain of Chikungunya Virus nsP3 and Determine Viral Replication in Cell-Specific Mode. <i> Meshram CD, Agback P, Shiliaev N, Urakova N, Mobley JA, Agback T, Frolova EI, Frolov I. </i> J Virol, 2018","reference_id":"29899097","region_id":"DP01466r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Western blot analysis with NAP1L1-specific Abs also definitively detected the latter protein in the co-IP samples generated on the cells infected with VEErep/Flag-GFP-ABCD but not with any other constructs, including VEErep/Flag-GFP-ABC and VEErep/Flag-GFP-123D (Fig. 8B). The most plausible explanation for the lack of NAP1L1 binding to CHIKV HVD deletion mutant constructs was that NAP1L1 binding requires the presence of intact aa sequences of both fragments C and D. Indeed, two isoforms of NAP1L1 were readily detectable in the samples generated from the cells infected with replicons expressing Flag-GFP-12CD and Flag-GFP-12(C3)D fusions (Fig. 8C). This was an indication that NAP1L1 interacts with HVD on the border between C and D fragments (see Fig. 11).","_id":"685af523b4ac24d5329d90de"},{"type":"Curator statement","text":"IDR in the publication is 100% identical to this Uniprot sequence.","_id":"685af523b4ac24d5329d90df"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T09:01:19.429Z","_id":"685af523b4ac24d5329d90e0"},"version":1,"_id":"685af523b4ac24d5329d90dd","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"27868","_id":"685af523b4ac24d5329d90e2"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-12-19T18:16:20.715Z","disprot_namespace":"Structural state","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1658,"end":1856,"interaction_partner":[],"reference_html":"Structural characterization and biological function of bivalent binding of CD2AP to intrinsically disordered domain of chikungunya virus nsP3 protein. <i> Agback P, Dominguez F, Pustovalova Y, Lukash T, Shiliaev N, Orekhov VY, Frolov I, Agback T, Frolova EI. </i> Virology, 2019","reference_id":"31493651","region_id":"DP01466r007","released":"2022_12","sample":[],"statement":[{"type":"Results","text":"The assignment data unambiguously proved that CHIKV HVD is disordered in solution (Supplementary Fig. 2) and allowed us to characterize in detail its interactions with the SH3-binding domains of CD2AP protein.","_id":"685af523b4ac24d5329d90e3"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d90e1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-12-19T18:23:02.599Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1758,"end":1775,"interaction_partner":[{"db":"UniProt","id":"Q9Y5K6","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d90e5"}],"reference_html":"Structural characterization and biological function of bivalent binding of CD2AP to intrinsically disordered domain of chikungunya virus nsP3 protein. <i> Agback P, Dominguez F, Pustovalova Y, Lukash T, Shiliaev N, Orekhov VY, Frolov I, Agback T, Frolova EI. </i> Virology, 2019","reference_id":"31493651","region_id":"DP01466r008","released":"2022_12","sample":[],"statement":[{"type":"Results","text":"The most significant changes in the chemical shift (2 standard deviations, 2σ) were found in three sites: aa 70–83 (Site 1), aa 101–111 (Site 2) and aa 164–172 (Site 3).","_id":"685af523b4ac24d5329d90e6"},{"type":"Results","text":"As was found for Site 1, the resonances of the residues in the docking site (aa 101–105) for SH3-A and SH3-B complexes were broadening with increasing concentration of the SH3 domains. The signals also became undetectable at saturation point (Supplementary Fig. 9). For the SH3-C complex, the corresponding 1H–15N correlation peaks moved linearly towards the chemical shifts of the bound state.","_id":"685af523b4ac24d5329d90e7"},{"type":"Results","text":"However, in the experiments with SH3-All, the Site 2-specific signals of residues 101 to 105 were already not detected at the first point of titration, at ratio 0.1:1 (Fig. 4 and Supplementary Fig. 9). This was an indication of a stronger affinity of SH3-All, compared to those of the individual domains. For aa 108R-111L, the CSP trajectories and their maximums were identical to the CSP signatures observed for binding of the SH3-A domain to CHIKV HVD (Fig. 4 and Supplementary Fig. 10).","_id":"685af523b4ac24d5329d90e8"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d90e4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-12-19T18:22:48.244Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1727,"end":1741,"interaction_partner":[{"db":"UniProt","id":"Q9Y5K6","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d90ea"}],"reference_html":"Structural characterization and biological function of bivalent binding of CD2AP to intrinsically disordered domain of chikungunya virus nsP3 protein. <i> Agback P, Dominguez F, Pustovalova Y, Lukash T, Shiliaev N, Orekhov VY, Frolov I, Agback T, Frolova EI. </i> Virology, 2019","reference_id":"31493651","region_id":"DP01466r009","released":"2022_12","sample":[],"statement":[{"type":"Results","text":"The most significant changes in the chemical shift (2 standard deviations, 2σ) were found in three sites: aa 70–83 (Site 1), aa 101–111 (Site 2) and aa 164–172 (Site 3).","_id":"685af523b4ac24d5329d90eb"},{"type":"Results","text":"As was found for Site 1, the resonances of the residues in the docking site (aa 101–105) for SH3-A and SH3-B complexes were broadening with increasing concentration of the SH3 domains. The signals also became undetectable at saturation point (Supplementary Fig. 9). For the SH3-C complex, the corresponding 1H–15N correlation peaks moved linearly towards the chemical shifts of the bound state.","_id":"685af523b4ac24d5329d90ec"},{"type":"Results","text":"However, in the experiments with SH3-All, the Site 2-specific signals of residues 101 to 105 were already not detected at the first point of titration, at ratio 0.1:1 (Fig. 4 and Supplementary Fig. 9). This was an indication of a stronger affinity of SH3-All, compared to those of the individual domains. For aa 108R-111L, the CSP trajectories and their maximums were identical to the CSP signatures observed for binding of the SH3-A domain to CHIKV HVD (Fig. 4 and Supplementary Fig. 10).","_id":"685af523b4ac24d5329d90ed"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d90e9","reference_source":"pmid"}],"__v":0,"disorder_content":0.08043654001616815,"disprot_consensus":{"full":[{"start":1658,"end":1856,"type":"D"}],"Structural state":[{"start":1658,"end":1856,"type":"D"}],"Molecular function":[{"start":1658,"end":1856,"type":"F"}],"Biological process":[{"start":1658,"end":1856,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00035","name":"Double-stranded RNA binding motif","start":1734,"end":1794},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":648,"end":765},{"id":"PF00636","name":"Ribonuclease III domain","start":1375,"end":1518},{"id":"PF00636","name":"Ribonuclease III domain","start":1594,"end":1707},{"id":"PF02170","name":"PAZ domain","start":1207,"end":1337},{"id":"PF03368","name":"Dicer dimerisation domain","start":840,"end":928},{"id":"PF04851","name":"Type III restriction enzyme, res subunit","start":250,"end":415},{"id":"PF14709","name":"double strand RNA binding domain from DEAD END PROTEIN 1","start":1832,"end":1904}],"gene3D":[{"start":1556,"end":1733,"id":"1.10.1520.10","name":"Ribonuclease III domain"},{"start":835,"end":939,"id":"3.30.160.380","name":"Dicer dimerisation domain"},{"start":457,"end":786,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":471,"end":616,"id":"1.20.1320.30","name":"1.20.1320.30"},{"start":1734,"end":1807,"id":"3.30.160.20","name":"3.30.160.20"},{"start":250,"end":456,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":1837,"end":1907,"id":"3.30.160.20","name":"3.30.160.20"},{"start":1195,"end":1324,"id":"2.170.260.10","name":"paz domain"}]},"uniref50":"UniRef50_Q9SP32","sequence":"MVMEDEPREATIKPSYWLDACEDISCDLIDDLVSEFDPSSVAVNESTDENGVINDFFGGIDHILDSIKNGGGLPNNGVSDTNSQINEVTVTPQVIAKETVKENGLQKNGGKRDEFSKEEGDKDRKRARVCSYQSERSNLSGRGHVNNSREGDRFMNRKRTRNWDEAGNNKKKRECNNYRRDGRDREVRGYWERDKVGSNELVYRSGTWEADHERDVKKVSGGNRECDVKAEENKSKPEERKEKVVEEQARRYQLDVLEQAKAKNTIAFLETGAGKTLIAILLIKSVHKDLMSQNRKMLSVFLVPKVPLVYQQAEVIRNQTCFQVGHYCGEMGQDFWDSRRWQREFESKQVLVMTAQILLNILRHSIIRMETIDLLILDECHHAVKKHPYSLVMSEFYHTTPKDKRPAIFGMTASPVNLKGVSSQVDCAIKIRNLETKLDSTVCTIKDRKELEKHVPMPSEIVVEYDKAATMWSLHETIKQMIAAVEEAAQASSRKSKWQFMGARDAGAKDELRQVYGVSERTESDGAANLIHKLRAINYTLAELGQWCAYKVGQSFLSALQSDERVNFQVDVKFQESYLSEVVSLLQCELLEGAAAEKVAAEVGKPENGNAHDEMEEGELPDDPVVSGGEHVDEVIGAAVADGKVTPKVQSLIKLLLKYQHTADFRAIVFVERVVAALVLPKVFAELPSLSFIRCASMIGHNNSQEMKSSQMQDTISKFRDGHVTLLVATSVAEEGLDIRQCNVVMRFDLAKTVLAYIQSRGRARKPGSDYILMVERGNVSHAAFLRNARNSEETLRKEAIERTDLSHLKDTSRLISIDAVPGTVYKVEATGAMVSLNSAVGLVHFYCSQLPGDRYAILRPEFSMEKHEKPGGHTEYSCRLQLPCNAPFEILEGPVCSSMRLAQQAVCLAACKKLHEMGAFTDMLLPDKGSGQDAEKADQDDEGEPVPGTARHREFYPEGVADVLKGEWVSSGKEVCESSKLFHLYMYNVRCVDFGSSKDPFLSEVSEFAILFGNELDAEVLSMSMDLYVARAMITKASLAFKGSLDITENQLSSLKKFHVRLMSIVLDVDVEPSTTPWDPAKAYLFVPVTDNTSMEPIKGINWELVEKITKTTAWDNPLQRARPDVYLGTNERTLGGDRREYGFGKLRHNIVFGQKSHPTYGIRGAVASFDVVRASGLLPVRDAFEKEVEEDLSKGKLMMADGCMVAEDLIGKIVTAAHSGKRFYVDSICYDMSAETSFPRKEGYLGPLEYNTYADYYKQKYGVDLNCKQQPLIKGRGVSYCKNLLSPRFEQSGESETVLDKTYYVFLPPELCVVHPLSGSLIRGAQRLPSIMRRVESMLLAVQLKNLISYPIPTSKILEALTAASCQETFCYERAELLGDAYLKWVVSRFLFLKYPQKHEGQLTRMRQQMVSNMVLYQFALVKGLQSYIQADRFAPSRWSAPGVPPVFDEDTKDGGSSFFDEEQKPVSEENSDVFEDGEMEDGELEGDLSSYRVLSSKTLADVVEALIGVYYVEGGKIAANHLMKWIGIHVEDDPDEVDGTLKNVNVPESVLKSIDFVGLERALKYEFKEKGLLVEAITHASRPSSGVSCYQRLEFVGDAVLDHLITRHLFFTYTSLPPGRLTDLRAAAVNNENFARVAVKHKLHLYLRHGSSALEKQIREFVKEVQTESSKPGFNSFGLGDCKAPKVLGDIVESIAGAIFLDSGKDTTAAWKVFQPLLQPMVTPETLPMHPVRELQERCQQQAEGLEYKASRSGNTATVEVFIDGVQVGVAQNPQKKMAQKLAARNALAALKEKEIAESKEKHINNGNAGEDQGENENGNKKNGHQPFTRQTLNDICLRKNWPMPSYRCVKEGGPAHAKRFTFGVRVNTSDRGWTDECIGEPMPSVKKAKDSAAVLLLELLNKTFS","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q9SP32","disprot_id":"DP01467","ncbi_taxon_id":3702,"regions_counter":28,"creator":"mlambrughi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1811,"region_id":"DP01467r001","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Induced folding in RNA recognition by Arabidopsis thaliana DCL1. <i> Suarez IP, Burdisso P, Benoit MP, Boisbouvier J, Rasia RM. </i> Nucleic Acids Res, 2015","statement":[{"text":"Quite unexpectedly, the CD spectrum of DCL1-A indicates that the polypeptide is disordered (Figure 2C) that the polypeptide is disordered","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1732,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-27T14:55:55.261Z","reference_source":"pmid","term_name":"disorder","reference_id":"26101256","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1811,"region_id":"DP01467r002","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Induced folding in RNA recognition by Arabidopsis thaliana DCL1. <i> Suarez IP, Burdisso P, Benoit MP, Boisbouvier J, Rasia RM. </i> Nucleic Acids Res, 2015","statement":[{"text":"We expressed the protein construct labeled with 15N, and we found that the 1H-15N-HMQC spectrum of DCL1-A shows a very limited dispersion, confirming that this domain does not fold by itself (Figure 2A).","type":"Results"},{"text":"Despite showing a poorly dispersed 1H-15N-HMQC spectrum DCL1-A appears to have some residual structure, since titrating the protein with Urea results in substantial chemical shift changes for most of the signals. The final state (8M Urea) shows a much better defined spectrum (Supplementary Figure S3), characteristic of fully unfolded proteins, with narrow lines due to fast conformational averaging. This suggests that the free protein is not completely unstructured.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1732,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-27T14:55:43.528Z","reference_source":"pmid","term_name":"disorder","reference_id":"26101256","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified"}],"cross_refs":[{"db":"BMRB","id":"19105"}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1811,"term_name":"DNA binding","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Induced folding in RNA recognition by Arabidopsis thaliana DCL1. <i> Suarez IP, Burdisso P, Benoit MP, Boisbouvier J, Rasia RM. </i> Nucleic Acids Res, 2015","statement":[{"text":"dsDNA binding induces minor changes in the secondary structure of DCL1-A (green vs. blue spectra), but the change in conformational sampling is negligible compared to that seen in the dsRNA complex (pink).","type":"Supplementary material"}],"term_id":"GO:0003677","curator_id":"vnugnes","start":1732,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"26101256","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-27T11:58:58.443Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01467r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":1811,"term_name":"disorder to order","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Induced folding in RNA recognition by Arabidopsis thaliana DCL1. <i> Suarez IP, Burdisso P, Benoit MP, Boisbouvier J, Rasia RM. </i> Nucleic Acids Res, 2015","statement":[{"text":" The 1H15N-TROSY spectrum of the complex displays a new set of well-dispersed signals, showing that the protein acquires a more ordered fold in the bound form  ​(Figure 4A). The new set of signals coexists with the signals corresponding to the unfolded protein, showing that the free and bound forms of the protein are in slow exchange in the NMR timescale. In order to confirm that both protein species are functional and in conformational exchange between each other we acquired ZZ exchange spectra on the sample and found the corresponding exchange crosspeaks, indicating that the folded and unfolded form are in equilibrium (Figure ​4B and Supplementary Figure S8).","type":"Results"},{"text":"These experiments indicate that DCL1-A folding is specifically induced by dsRNA.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"vnugnes","start":1732,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"26101256","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-27T14:55:27.619Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01467r005","ec_go":"EXP","disprot_namespace":"Structural transition","cross_refs":[{"db":"BMRB","id":"19104"}],"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"ENA","id":"URS0000791AEB_3702"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1811,"region_id":"DP01467r006","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Conformational sampling of the intrinsically disordered dsRBD-1 domain from Arabidopsis thaliana DCL1. <i> Suárez IP, Gauto DF, Hails G, Mascali FC, Crespo R, Zhao L, Wang J, Rasia RM. </i> Phys Chem Chem Phys, 2018","statement":[{"text":"NOESY-15N-HSQC spectra of the protein show few NOE crosspeaks, corresponding to intra and i-1 correlations, further supporting the absence of a stable structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mlambrughi","start":1732,"term_ontology":"IDPO","curator_name":"Matteo Lambrughi","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-0894-8627","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29632904","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-28T15:43:56.446Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1811,"region_id":"DP01467r007","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Conformational sampling of the intrinsically disordered dsRBD-1 domain from Arabidopsis thaliana DCL1. <i> Suárez IP, Gauto DF, Hails G, Mascali FC, Crespo R, Zhao L, Wang J, Rasia RM. </i> Phys Chem Chem Phys, 2018","statement":[{"text":"We employed SAXS data to obtain information on global shape of the ensemble. The Kratky plot shows the typical features of disordered proteins.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mlambrughi","start":1732,"term_ontology":"IDPO","curator_name":"Matteo Lambrughi","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-0894-8627","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29632904","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-28T15:44:07.684Z"}},{"start":1,"end":249,"reference_id":"34593993","reference_source":"pmid","reference_html":"Structural basis of microRNA processing by Dicer-like 1. <i> Wei X, Ke H, Wen A, Gao B, Shi J, Feng Y. </i> Nat Plants, 2021","date":"2023-11-24T15:59:21.060Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7ELE"},{"db":"PDB","id":"7ELD"},{"db":"EMDB","id":"31181"},{"db":"EMDB","id":"31182"}],"region_id":"DP01467r008","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00023119C5_3702","statements":[{"type":"Methods","text":"DCL1–pri-miRNA complex was prepared in 50 μl of reaction mixture containing 6 µM DCL1, 7.2 µM pri-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT."}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS0002311A32_3702","statements":[{"type":"Methods","text":"DCL1–pre-miRNA complex was assembled in 50 μl of reaction mixture containing 3 µM DCL1, 3.6 µM pre-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT. The reaction mixtures were incubated at 4 °C for 30 min."}]}],"statement":[{"text":"The cryo-EM structures of  Arabidopsis DCL1 in complex with pre-miRNA and pri-miRNA show this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":494,"end":525,"reference_id":"34593993","reference_source":"pmid","reference_html":"Structural basis of microRNA processing by Dicer-like 1. <i> Wei X, Ke H, Wen A, Gao B, Shi J, Feng Y. </i> Nat Plants, 2021","date":"2023-11-24T16:00:14.316Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7ELE"},{"db":"PDB","id":"7ELD"},{"db":"EMDB","id":"31181"},{"db":"EMDB","id":"31182"}],"region_id":"DP01467r009","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00023119C5_3702","statements":[{"type":"Methods","text":"DCL1–pri-miRNA complex was prepared in 50 μl of reaction mixture containing 6 µM DCL1, 7.2 µM pri-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT."}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS0002311A32_3702","statements":[{"type":"Methods","text":"DCL1–pre-miRNA complex was assembled in 50 μl of reaction mixture containing 3 µM DCL1, 3.6 µM pre-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT. The reaction mixtures were incubated at 4 °C for 30 min."}]}],"statement":[{"text":"The cryo-EM structures of  Arabidopsis DCL1 in complex with pre-miRNA and pri-miRNA show this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":595,"end":650,"reference_id":"34593993","reference_source":"pmid","reference_html":"Structural basis of microRNA processing by Dicer-like 1. <i> Wei X, Ke H, Wen A, Gao B, Shi J, Feng Y. </i> Nat Plants, 2021","date":"2023-11-24T16:00:44.523Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7ELE"},{"db":"PDB","id":"7ELD"},{"db":"EMDB","id":"31181"},{"db":"EMDB","id":"31182"}],"region_id":"DP01467r010","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00023119C5_3702","statements":[{"type":"Methods","text":"DCL1–pri-miRNA complex was prepared in 50 μl of reaction mixture containing 6 µM DCL1, 7.2 µM pri-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT."}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS0002311A32_3702","statements":[{"type":"Methods","text":"DCL1–pre-miRNA complex was assembled in 50 μl of reaction mixture containing 3 µM DCL1, 3.6 µM pre-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT. The reaction mixtures were incubated at 4 °C for 30 min."}]}],"statement":[{"text":"The cryo-EM structures of  Arabidopsis DCL1 in complex with pre-miRNA and pri-miRNA show this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":921,"end":974,"reference_id":"34593993","reference_source":"pmid","reference_html":"Structural basis of microRNA processing by Dicer-like 1. <i> Wei X, Ke H, Wen A, Gao B, Shi J, Feng Y. </i> Nat Plants, 2021","date":"2023-11-24T16:01:16.456Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7ELE"},{"db":"PDB","id":"7ELD"},{"db":"EMDB","id":"31181"},{"db":"EMDB","id":"31182"}],"region_id":"DP01467r011","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00023119C5_3702","statements":[{"type":"Methods","text":"DCL1–pri-miRNA complex was prepared in 50 μl of reaction mixture containing 6 µM DCL1, 7.2 µM pri-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT."}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS0002311A32_3702","statements":[{"type":"Methods","text":"DCL1–pre-miRNA complex was assembled in 50 μl of reaction mixture containing 3 µM DCL1, 3.6 µM pre-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT. The reaction mixtures were incubated at 4 °C for 30 min."}]}],"statement":[{"text":"Linkers between the DUF283 and the Platform (residues 921–974), between the Platform and the PAZ (residues 1,114–1,198) and between two RNase III domains (residues 1,532–1,557) are not modelled because of the high flexibility of these fragments.","type":"Results"}]},{"start":921,"end":974,"reference_id":"34593993","reference_source":"pmid","reference_html":"Structural basis of microRNA processing by Dicer-like 1. <i> Wei X, Ke H, Wen A, Gao B, Shi J, Feng Y. </i> Nat Plants, 2021","date":"2023-11-24T16:01:29.154Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7ELE"},{"db":"PDB","id":"7ELD"},{"db":"EMDB","id":"31181"},{"db":"EMDB","id":"31182"}],"region_id":"DP01467r012","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00023119C5_3702","statements":[{"type":"Methods","text":"DCL1–pri-miRNA complex was prepared in 50 μl of reaction mixture containing 6 µM DCL1, 7.2 µM pri-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT."}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS0002311A32_3702","statements":[{"type":"Methods","text":"DCL1–pre-miRNA complex was assembled in 50 μl of reaction mixture containing 3 µM DCL1, 3.6 µM pre-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT. The reaction mixtures were incubated at 4 °C for 30 min."}]}],"statement":[{"text":"Linkers between the DUF283 and the Platform (residues 921–974), between the Platform and the PAZ (residues 1,114–1,198) and between two RNase III domains (residues 1,532–1,557) are not modelled because of the high flexibility of these fragments.","type":"Results"}]},{"start":985,"end":1006,"reference_id":"34593993","reference_source":"pmid","reference_html":"Structural basis of microRNA processing by Dicer-like 1. <i> Wei X, Ke H, Wen A, Gao B, Shi J, Feng Y. </i> Nat Plants, 2021","date":"2023-11-24T16:02:18.265Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7ELE"},{"db":"PDB","id":"7ELD"},{"db":"EMDB","id":"31181"},{"db":"EMDB","id":"31182"}],"region_id":"DP01467r013","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00023119C5_3702","statements":[{"type":"Methods","text":"DCL1–pri-miRNA complex was prepared in 50 μl of reaction mixture containing 6 µM DCL1, 7.2 µM pri-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT."}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS0002311A32_3702","statements":[{"type":"Methods","text":"DCL1–pre-miRNA complex was assembled in 50 μl of reaction mixture containing 3 µM DCL1, 3.6 µM pre-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT. The reaction mixtures were incubated at 4 °C for 30 min."}]}],"statement":[{"text":"The cryo-EM structures of Arabidopsis DCL1 in complex with pre-miRNA and pri-miRNA show this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":1070,"end":1100,"reference_id":"34593993","reference_source":"pmid","reference_html":"Structural basis of microRNA processing by Dicer-like 1. <i> Wei X, Ke H, Wen A, Gao B, Shi J, Feng Y. </i> Nat Plants, 2021","date":"2023-11-24T16:07:09.337Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7ELE"},{"db":"PDB","id":"7ELD"},{"db":"EMDB","id":"31181"},{"db":"EMDB","id":"31182"}],"region_id":"DP01467r014","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00023119C5_3702","statements":[{"type":"Methods","text":"DCL1–pri-miRNA complex was prepared in 50 μl of reaction mixture containing 6 µM DCL1, 7.2 µM pri-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT."}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS0002311A32_3702","statements":[{"type":"Methods","text":"DCL1–pre-miRNA complex was assembled in 50 μl of reaction mixture containing 3 µM DCL1, 3.6 µM pre-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT. The reaction mixtures were incubated at 4 °C for 30 min."}]}],"statement":[{"text":"The cryo-EM structures of Arabidopsis DCL1 in complex with pre-miRNA and pri-miRNA show the regions 1070-1084 and 1092-1100 lack electron density. Even though the residue 1085-1091 are present in the structure, the region is too short to be considered as structured, therefore the whole region 1070-1100 is considered as disordered.","type":"Curator statement"}]},{"start":1114,"end":1198,"reference_id":"34593993","reference_source":"pmid","reference_html":"Structural basis of microRNA processing by Dicer-like 1. <i> Wei X, Ke H, Wen A, Gao B, Shi J, Feng Y. </i> Nat Plants, 2021","date":"2023-11-24T16:07:44.031Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7ELE"},{"db":"PDB","id":"7ELD"},{"db":"EMDB","id":"31181"},{"db":"EMDB","id":"31182"}],"region_id":"DP01467r015","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00023119C5_3702","statements":[{"type":"Methods","text":"DCL1–pri-miRNA complex was prepared in 50 μl of reaction mixture containing 6 µM DCL1, 7.2 µM pri-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT."}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS0002311A32_3702","statements":[{"type":"Methods","text":"DCL1–pre-miRNA complex was assembled in 50 μl of reaction mixture containing 3 µM DCL1, 3.6 µM pre-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT. The reaction mixtures were incubated at 4 °C for 30 min."}]}],"statement":[{"text":"Linkers between the DUF283 and the Platform (residues 921–974), between the Platform and the PAZ (residues 1,114–1,198) and between two RNase III domains (residues 1,532–1,557) are not modelled because of the high flexibility of these fragments.","type":"Results"}]},{"start":1114,"end":1198,"reference_id":"34593993","reference_source":"pmid","reference_html":"Structural basis of microRNA processing by Dicer-like 1. <i> Wei X, Ke H, Wen A, Gao B, Shi J, Feng Y. </i> Nat Plants, 2021","date":"2023-11-24T16:08:01.455Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7ELE"},{"db":"PDB","id":"7ELD"},{"db":"EMDB","id":"31181"},{"db":"EMDB","id":"31182"}],"region_id":"DP01467r016","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00023119C5_3702","statements":[{"type":"Methods","text":"DCL1–pri-miRNA complex was prepared in 50 μl of reaction mixture containing 6 µM DCL1, 7.2 µM pri-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT."}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS0002311A32_3702","statements":[{"type":"Methods","text":"DCL1–pre-miRNA complex was assembled in 50 μl of reaction mixture containing 3 µM DCL1, 3.6 µM pre-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT. The reaction mixtures were incubated at 4 °C for 30 min."}]}],"statement":[{"text":"Linkers between the DUF283 and the Platform (residues 921–974), between the Platform and the PAZ (residues 1,114–1,198) and between two RNase III domains (residues 1,532–1,557) are not modelled because of the high flexibility of these fragments.","type":"Results"}]},{"start":1283,"end":1299,"reference_id":"34593993","reference_source":"pmid","reference_html":"Structural basis of microRNA processing by Dicer-like 1. <i> Wei X, Ke H, Wen A, Gao B, Shi J, Feng Y. </i> Nat Plants, 2021","date":"2023-11-24T16:09:14.209Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7ELE"},{"db":"PDB","id":"7ELD"},{"db":"EMDB","id":"31181"},{"db":"EMDB","id":"31182"}],"region_id":"DP01467r017","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00023119C5_3702","statements":[{"type":"Methods","text":"DCL1–pri-miRNA complex was prepared in 50 μl of reaction mixture containing 6 µM DCL1, 7.2 µM pri-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT."}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS0002311A32_3702","statements":[{"type":"Methods","text":"DCL1–pre-miRNA complex was assembled in 50 μl of reaction mixture containing 3 µM DCL1, 3.6 µM pre-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT. The reaction mixtures were incubated at 4 °C for 30 min."}]}],"statement":[{"text":"The cryo-EM structures of Arabidopsis DCL1 in complex with pre-miRNA and pri-miRNA show this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":1431,"end":1494,"reference_id":"34593993","reference_source":"pmid","reference_html":"Structural basis of microRNA processing by Dicer-like 1. <i> Wei X, Ke H, Wen A, Gao B, Shi J, Feng Y. </i> Nat Plants, 2021","date":"2023-11-24T16:10:36.201Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7ELE"},{"db":"PDB","id":"7ELD"},{"db":"EMDB","id":"31181"},{"db":"EMDB","id":"31182"}],"region_id":"DP01467r018","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00023119C5_3702","statements":[{"type":"Methods","text":"DCL1–pri-miRNA complex was prepared in 50 μl of reaction mixture containing 6 µM DCL1, 7.2 µM pri-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT."}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS0002311A32_3702","statements":[{"type":"Methods","text":"DCL1–pre-miRNA complex was assembled in 50 μl of reaction mixture containing 3 µM DCL1, 3.6 µM pre-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT. The reaction mixtures were incubated at 4 °C for 30 min."}]}],"statement":[{"text":"The cryo-EM structures of Arabidopsis DCL1 in complex with pre-miRNA and pri-miRNA show this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":1532,"end":1557,"reference_id":"34593993","reference_source":"pmid","reference_html":"Structural basis of microRNA processing by Dicer-like 1. <i> Wei X, Ke H, Wen A, Gao B, Shi J, Feng Y. </i> Nat Plants, 2021","date":"2023-11-24T16:11:18.544Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7ELE"},{"db":"PDB","id":"7ELD"},{"db":"EMDB","id":"31181"},{"db":"EMDB","id":"31182"}],"region_id":"DP01467r019","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00023119C5_3702","statements":[{"type":"Methods","text":"DCL1–pri-miRNA complex was prepared in 50 μl of reaction mixture containing 6 µM DCL1, 7.2 µM pri-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT."}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS0002311A32_3702","statements":[{"type":"Methods","text":"DCL1–pre-miRNA complex was assembled in 50 μl of reaction mixture containing 3 µM DCL1, 3.6 µM pre-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT. The reaction mixtures were incubated at 4 °C for 30 min."}]}],"statement":[{"text":"Linkers between the DUF283 and the Platform (residues 921–974), between the Platform and the PAZ (residues 1,114–1,198) and between two RNase III domains (residues 1,532–1,557) are not modelled because of the high flexibility of these fragments.","type":"Results"}]},{"start":1532,"end":1557,"reference_id":"34593993","reference_source":"pmid","reference_html":"Structural basis of microRNA processing by Dicer-like 1. <i> Wei X, Ke H, Wen A, Gao B, Shi J, Feng Y. </i> Nat Plants, 2021","date":"2023-11-24T16:11:29.084Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7ELE"},{"db":"PDB","id":"7ELD"},{"db":"EMDB","id":"31181"},{"db":"EMDB","id":"31182"}],"region_id":"DP01467r020","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00023119C5_3702","statements":[{"type":"Methods","text":"DCL1–pri-miRNA complex was prepared in 50 μl of reaction mixture containing 6 µM DCL1, 7.2 µM pri-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT."}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS0002311A32_3702","statements":[{"type":"Methods","text":"DCL1–pre-miRNA complex was assembled in 50 μl of reaction mixture containing 3 µM DCL1, 3.6 µM pre-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT. The reaction mixtures were incubated at 4 °C for 30 min."}]}],"statement":[{"text":"Linkers between the DUF283 and the Platform (residues 921–974), between the Platform and the PAZ (residues 1,114–1,198) and between two RNase III domains (residues 1,532–1,557) are not modelled because of the high flexibility of these fragments.","type":"Results"}]},{"start":1670,"end":1688,"reference_id":"34593993","reference_source":"pmid","reference_html":"Structural basis of microRNA processing by Dicer-like 1. <i> Wei X, Ke H, Wen A, Gao B, Shi J, Feng Y. </i> Nat Plants, 2021","date":"2023-11-24T16:12:17.193Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7ELE"},{"db":"PDB","id":"7ELD"},{"db":"EMDB","id":"31181"},{"db":"EMDB","id":"31182"}],"region_id":"DP01467r021","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00023119C5_3702","statements":[{"type":"Methods","text":"DCL1–pri-miRNA complex was prepared in 50 μl of reaction mixture containing 6 µM DCL1, 7.2 µM pri-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT."}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS0002311A32_3702","statements":[{"type":"Methods","text":"DCL1–pre-miRNA complex was assembled in 50 μl of reaction mixture containing 3 µM DCL1, 3.6 µM pre-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT. The reaction mixtures were incubated at 4 °C for 30 min."}]}],"statement":[{"text":"The cryo-EM structures of Arabidopsis DCL1 in complex with pre-miRNA and pri-miRNA show this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":1795,"end":1909,"reference_id":"34593993","reference_source":"pmid","reference_html":"Structural basis of microRNA processing by Dicer-like 1. <i> Wei X, Ke H, Wen A, Gao B, Shi J, Feng Y. </i> Nat Plants, 2021","date":"2023-11-24T16:12:59.061Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7ELE"},{"db":"PDB","id":"7ELD"},{"db":"EMDB","id":"31181"},{"db":"EMDB","id":"31182"}],"region_id":"DP01467r022","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00023119C5_3702","statements":[{"type":"Methods","text":"DCL1–pri-miRNA complex was prepared in 50 μl of reaction mixture containing 6 µM DCL1, 7.2 µM pri-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT."}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS0002311A32_3702","statements":[{"type":"Methods","text":"DCL1–pre-miRNA complex was assembled in 50 μl of reaction mixture containing 3 µM DCL1, 3.6 µM pre-miRNA, 20 mM Tris-HCl, pH 7.0, 50 mM NaCl and 2 mM DTT. The reaction mixtures were incubated at 4 °C for 30 min."}]}],"statement":[{"text":"The cryo-EM structures of Arabidopsis DCL1 in complex with pre-miRNA and pri-miRNA show this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":1732,"end":1909,"reference_id":"26101256","reference_source":"pmid","reference_html":"Induced folding in RNA recognition by Arabidopsis thaliana DCL1. <i> Suarez IP, Burdisso P, Benoit MP, Boisbouvier J, Rasia RM. </i> Nucleic Acids Res, 2015","date":"2023-11-27T09:44:49.388Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003725","term_name":"double-stranded RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006277","ec_ontology":"ECO","ec_name":"fluorescence polarization evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"RNAcentral","id":"URS0000791AEB_3702","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01467r023","statement":[{"text":"The affinity of the isolated DCL1-A construct for pri-miR172a fragments is similar to the one determined previously for DCL1-B (13). DCL1-A RNA binding affinity is somewhat higher for the pri-miR172a-ls construct than for the miR172a stem loop. The secondary structure of the former is less regular than that of the latter, including one mismatch and three G•U wobble base pairs, thus suggesting that DCL1-A may have some preference for imperfect dsRNA segments. In contrast, the double domain DCL1-AB shows an affinity one order of magnitude higher for the miR172a stem-loop and threefold higher for the primiR172a-ls construct, indicating that both domains participate jointly in the recognition of the substrate.","type":"Results"}],"term_comment":"","term_def":"\"Binding to double-stranded RNA.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":1732,"end":1811,"reference_id":"26101256","reference_source":"pmid","reference_html":"Induced folding in RNA recognition by Arabidopsis thaliana DCL1. <i> Suarez IP, Burdisso P, Benoit MP, Boisbouvier J, Rasia RM. </i> Nucleic Acids Res, 2015","date":"2023-11-27T09:51:28.682Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005632","ec_ontology":"ECO","ec_name":"fluorescence anisotropy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP01467r024","statement":[{"text":"We found that both constructs do bind dsDNA, showing that DCL1-A is also peculiar in terms of nucleic acid recognition with respect to other dsRBDs. The affinity of the double domain for dsDNA is similar to that for both isolated domains, indicating that in this case the domains behave as independent binding units.","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false},{"start":1826,"end":1909,"reference_id":"26101256","reference_source":"pmid","reference_html":"Induced folding in RNA recognition by Arabidopsis thaliana DCL1. <i> Suarez IP, Burdisso P, Benoit MP, Boisbouvier J, Rasia RM. </i> Nucleic Acids Res, 2015","date":"2023-11-27T09:52:43.334Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005632","ec_ontology":"ECO","ec_name":"fluorescence anisotropy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP01467r025","statement":[{"text":"We found that both constructs do bind dsDNA, showing that DCL1-A is also peculiar in terms of nucleic acid recognition with respect to other dsRBDs. The affinity of the double domain for dsDNA is similar to that for both isolated domains, indicating that in this case the domains behave as independent binding units.","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false},{"start":1732,"end":1811,"reference_id":"26101256","reference_source":"pmid","reference_html":"Induced folding in RNA recognition by Arabidopsis thaliana DCL1. <i> Suarez IP, Burdisso P, Benoit MP, Boisbouvier J, Rasia RM. </i> Nucleic Acids Res, 2015","date":"2023-11-27T14:56:24.799Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003725","term_name":"double-stranded RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"RNAcentral","id":"URS0000791AEB_3702","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01467r026","statement":[{"text":"We first tested this by following the formation of DCL1-A:RNA complex by CD spectroscopy ​(Figure 3A) using the pri-miR172a-ls construct. The free protein shows the characteristic spectrum of unfolded polypeptides, with a negative minimum at ca. 200 nm. Addition of RNA immediately changes the spectrum in the far UV region, but due to the intense negative band of dsRNA at 210 nm it is hard to determine if the protein develops secondary structure.","type":"Results"}],"term_comment":"","term_def":"\"Binding to double-stranded RNA.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":1732,"end":1811,"reference_id":"26101256","reference_source":"pmid","reference_html":"Induced folding in RNA recognition by Arabidopsis thaliana DCL1. <i> Suarez IP, Burdisso P, Benoit MP, Boisbouvier J, Rasia RM. </i> Nucleic Acids Res, 2015","date":"2023-11-27T14:56:10.165Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01467r027","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS0000791AEB_3702"}],"statement":[{"text":"We first tested this by following the formation of DCL1-A:RNA complex by CD spectroscopy ​(Figure 3A) using the pri-miR172a-ls construct. The free protein shows the characteristic spectrum of unfolded polypeptides, with a negative minimum at ca. 200 nm. Addition of RNA immediately changes the spectrum in the far UV region, but due to the intense negative band of dsRNA at 210 nm it is hard to determine if the protein develops secondary structure.","type":"Results"},{"text":"Two of the basis spectra correspond well with the spectra of the free protein and of the free RNA, whereas the third component closely matches the spectrum of canonical dsRBDs (Supplementary Figure S6), suggesting that DCL1-A acquires the same secondary structure as other stably folded homologs.","type":"Results"},{"text":"However, the contribution of the folded protein component to the spectra can clearly be noticed at 10 equivalents added protein.","type":"Results"}]},{"start":1732,"end":1811,"reference_id":"26101256","reference_source":"pmid","reference_html":"Induced folding in RNA recognition by Arabidopsis thaliana DCL1. <i> Suarez IP, Burdisso P, Benoit MP, Boisbouvier J, Rasia RM. </i> Nucleic Acids Res, 2015","date":"2023-11-27T10:40:44.380Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","region_id":"DP01467r028","statement":[{"text":"The CD spectra of DCL1-A:DNA complexes show a slight shift in the minimum from 200 to 202 nm, and a small variation in the CD200nm/CD220nm ratio, demonstrating that binding to DNA induces a variation in the conformational sampling of the protein, but this still remains disordered (Supplementary Figure S9).","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_Q9SP32","date":"2018-07-19T14:38:02.000Z","acc":"Q9SP32","name":"Endoribonuclease Dicer homolog 1","length":1909,"organism":"Arabidopsis thaliana","dataset":["Condensates-related proteins","RNA-binding proteins"],"UniParc":"UPI00000A2EEC","genes":[{"name":{"value":"DCL1"},"synonyms":[{"value":"ASU1"},{"value":"CAF SIN1"},{"value":"SUS1"}],"orfNames":[{"value":"T25K16.4"}],"olnNames":[{"value":"At1g01040"}]}],"alphafold_very_low_content":0.26610790990047145,"disorder_content":0.43635411210057623,"disprot_consensus":{"full":[{"start":1,"end":249,"type":"D"},{"start":494,"end":525,"type":"D"},{"start":595,"end":650,"type":"D"},{"start":921,"end":974,"type":"D"},{"start":985,"end":1006,"type":"D"},{"start":1070,"end":1100,"type":"D"},{"start":1114,"end":1198,"type":"D"},{"start":1283,"end":1299,"type":"D"},{"start":1431,"end":1494,"type":"D"},{"start":1532,"end":1557,"type":"D"},{"start":1670,"end":1688,"type":"D"},{"start":1732,"end":1811,"type":"T"},{"start":1812,"end":1909,"type":"D"}],"Structural state":[{"start":1,"end":249,"type":"D"},{"start":494,"end":525,"type":"D"},{"start":595,"end":650,"type":"D"},{"start":921,"end":974,"type":"D"},{"start":985,"end":1006,"type":"D"},{"start":1070,"end":1100,"type":"D"},{"start":1114,"end":1198,"type":"D"},{"start":1283,"end":1299,"type":"D"},{"start":1431,"end":1494,"type":"D"},{"start":1532,"end":1557,"type":"D"},{"start":1670,"end":1688,"type":"D"},{"start":1732,"end":1909,"type":"D"}],"Molecular function":[{"start":1732,"end":1909,"type":"F"}],"Structural transition":[{"start":1732,"end":1811,"type":"T"}],"Disorder function":[{"start":921,"end":974,"type":"F"},{"start":1114,"end":1198,"type":"F"},{"start":1532,"end":1557,"type":"F"}]}},{"acc":"A3RMR8","sequence":"MDSVYVDIDADSAFLKALQRAYPMFEVEPRQVTSNDHANARAFSHLAIKLIEQEIDPDSTILDIGSAPARRMMSDRKYHCVCPMRSAEDPERLANYARKLASAAGKVLDRNISGKIGDLQAVMAVPDTETPTFCLHTDVSCRQRADVAIYQDVYAVHAPTSLYHQAIKGVRVAYWVGFDTTPFMYNAMAGAYPSYSTNWADEQVLKAKNIGLCSTDLTEGRRGKLSIMRGKKLKPCDRVLFSVGSTLYPESRTLLKSWHLPSVFHLKGKLSFTCRCDTVVSCEGYVVKRITMSPGLYGKTIGYAVTHHADGFLMCKTTDTVDGERVSFSVCTYVPATICDQMTGILATEVTPEDAQKLLVGLNQRIVVNGRTQRNTNTMKNYLLPVVAQAFSKWAKECRKDMEDEKLLGVRERTLTCCCLWAFKKQKTHTVYKRPDTQSIQKVQAEFDSFVVPGLWSSGLSIPLRTRIKWLLRKVPKTDLIPYSGNAQEAQDAEKEAEEEREAELTHEALPPLQAAQEDVQVEIDVEQLEDRAGAGIIETPRGAIKVTAQLTDHVVGEYLVLSPQTVLRSQKLSLIHALAEQVKTCTHSGRAGRYAVEAYDGRVLVPSGYAISPEDFQSLSESATMVYNEREFVNRKLHHIAMHGPALNTDEESYELVRAERTEHEYVYDVDQRRCCKKEEAAGLVLVGDLTNPPYHEFAYEGLKIRPACPYKIAVIGVFGVPGSGKSAIIKNLVTRQDLVTSGKKENCQEISTDVMRQRGLEISARTVDSLLLNGCNRPVDVLYVDEAFACHSGTLLALIALVRPRQKVVLCGDPKQCGFFNMMQMKVNYNHNICTQVYHKSISRRCTLPVTAIVSSLHYEGKMRTTNEYNMPIVVDTTGSTKPDPGDLVLTCFRGWVKQLQIDYRGHEVMTAAASQGLTRKGVYAVRQKVNENPLYASTSEHVNVLLTRTEGKLVWKTLSGDPWIKTLQNPPKGNFKATIKEWEVEHASIMAGICSHQVTFDTFQNKANVCWAKSLVPILETAGIKLNDRQWSQIIQAFKEDKAYSPEVALNEICTRMYGVDLDSGLFSKPLVSVYYADNHWDNRPGGKMFGFNPEAASILERKYPFTKGKWNINKQICVTTRRIEDFNPTTNIIPVNRRLPHSLVAEHRPVKGERMEWLVNKINGHHVLLVSGYNLALPTKRVTWVAPLGVRGADYTYNLELGLPATLGRYDLVVINIHTPFRIHHYQQCVDHAMKLQMLGGDSLRLLKPGGSLLIRAYGYADRTSERVICVLGRKFRSSRALKPPCVTSNTEMFFLFSNFDNGRRNFTTHVMNNQLNAAFVGQATRAGCAPSYRVKRMDIAKNDEECVVNAANPRGLPGDGVCKAVYKKWPESFKNSATPVGTAKTVMCGTYPVIHAVGPNFSNYSESEGDRELAAAYREVAKEVTRLGVNSVAIPLLSTGVYSGGKDRLTQSLNHLFTAMDSTDADVVIYCRDKEWEKKISEAIQMRTQVELLDEHISIDCDVIRVHPDSSLAGRKGYSTTEGALYSYLEGTRFHQTAVDMAEIYTMWPKQTEANEQVCLYALGESIESIRQKCPVDDADASSPPKTVPCLCRYAMTPERVTRLRMNHVTNIIVCSSFPLPKYKIEGVQKVKCSKVMLFDHNVPSRVSPREYRSSQESVQEVSTTTSLTHSQFDLSADGETLPVPSDLDADAPALEPALDDGAVHTLPTIIGNLAAVSDWVMSTVPVAPPRRRRGRNLTVTCDEREGNITPMASVRFFRAELCPAVQETAETRDTAISLQAPPSTTMELSHPPISFGAPSETFPITFGDFDEGEIESLSSELLTFGDFLPGEVDDLTDSDWSTCPDTDDELXLDRAGGYIFSSDTGPGHLQQKSVRQSVLPVNTLEEVHEEKCYPPKLDELKEQLLLKKLQESASMANRSRYQSRKVENMKATIIQRLKRGCKLYLMAETPKVPTYRTIYPAPVYSPPINVRLSNPESAVAACNEFLARNYPTVSSYQITDEYDAYLDMVDGSESCLDRATFNPSKLRSYPKQHAYHAPSIRSAVPSPFQNTLQNVLAAATKRNCNVTQMRELPTLDSAVFNVECFKKFACNREYWEEFAASPIRITTENLTTYVTKLKGPKAAALFAKTHNLLPLQDVPMDRFTVDMKRDVKVTPGTKHTEERPKVQVIQAAEPLATAYLCGIHRELVRRLNAVLLPNVHTLFDMSAEDFDAIIAAHFKPGDAVLETDIASFDKSQDDSLALTALMLLEDLGVDHSLLDLIEAAFGEISSCHLPTGTRFKFGAMMKSGMFLTLFVNTLLNITIASRVLEDRLTKSACAAFIGDDNIIHGVVSDELMAARCATWMNMEVKIIDAVVSQKAPYFCGGFILHDTVTGTACRVADPLKRLFKLGKPLAAGDEQDEDRRRALADEVIRWQRTGLIDELEKAVYSRYEVQGISVAVMSMATFASSRSNFEKLRGPVITLYGGPK","creator":"mmacossay","dataset":["Viral proteins","Neglected tropical diseases proteins"],"date":"2018-07-19T14:53:09.000Z","disprot_id":"DP01468","features":{"pfam":[],"gene3D":[{"start":1145,"end":1506,"id":"3.40.50.150","name":"Vaccinia Virus protein VP39","_id":"685af523b4ac24d5329d90f7"},{"start":1337,"end":1493,"id":"3.40.220.10","name":"Leucine Aminopeptidase, subunit E, domain 1","_id":"685af523b4ac24d5329d90f8"},{"start":843,"end":982,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d90f9"},{"start":1003,"end":1140,"id":"3.90.70.110","name":"Alphavirus nsP2 protease domain","_id":"685af523b4ac24d5329d90fa"},{"start":713,"end":842,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d90fb"}]},"genes":[{"name":{"value":"NSP","evidences":[{"source":{"id":"AYI50331.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/AYI50331.1","_id":"685af523b4ac24d5329d9121"},"code":"ECO:0000313","_id":"685af523b4ac24d5329d9120"}],"_id":"685af523b4ac24d5329d9122"},"synonyms":[],"olnNames":[],"orfNames":[{"value":"CHIKVgp1","evidences":[{"source":{"id":"ABO10016.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/ABO10016.1","_id":"685af523b4ac24d5329d9125"},"code":"ECO:0000313","_id":"685af523b4ac24d5329d9124"}],"_id":"685af523b4ac24d5329d9123"}],"_id":"685af523b4ac24d5329d911f"}],"length":2474,"name":"Nonstructural polyprotein","ncbi_taxon_id":37124,"organism":"Chikungunya virus","regions_counter":6,"released":"2018_11","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Alsuviricetes","Martellivirales","Togaviridae","Alphavirus"],"UniParc":"UPI0000F2F31B","uniref100":"UniRef100_A3RMR8","uniref50":"UniRef50_P08411","uniref90":"UniRef90_Q8JUX6","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1658,"end":1856,"interaction_partner":[],"reference_html":"Multiple Host Factors Interact with the Hypervariable Domain of Chikungunya Virus nsP3 and Determine Viral Replication in Cell-Specific Mode. <i> Meshram CD, Agback P, Shiliaev N, Urakova N, Mobley JA, Agback T, Frolova EI, Frolov I. </i> J Virol, 2018","reference_id":"29899097","region_id":"DP01468r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"It exhibits a reduced chemical shift dispersion, especially in the 1H dimension between 8.5 and 7.5 ppm (Fig. 1C), which is a characteristic of the intrinsically disordered proteins (42).","_id":"685af523b4ac24d5329d90fd"},{"type":"Discussion","text":"We carried out detailed characterization of a 199-aa-long CHIKV HVD by NMR spectroscopy at atomic resolution. The results revealed the absence of stable secondary structures in this domain and clearly demonstrated that CHIKV HVD was present in solution in a disordered conformation.","_id":"685af523b4ac24d5329d90fe"},{"type":"Curator statement","text":"IDR in the publication is 100% identical to this Uniprot sequence.","_id":"685af523b4ac24d5329d90ff"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T09:01:34.294Z","_id":"685af523b4ac24d5329d9100"},"version":3,"_id":"685af523b4ac24d5329d90fc","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IEP","ec_id":"ECO:0000279","ec_name":"qualitative western immunoblotting evidence used in manual assertion","ec_ontology":"ECO","start":1761,"end":1856,"interaction_partner":[],"reference_html":"Multiple Host Factors Interact with the Hypervariable Domain of Chikungunya Virus nsP3 and Determine Viral Replication in Cell-Specific Mode. <i> Meshram CD, Agback P, Shiliaev N, Urakova N, Mobley JA, Agback T, Frolova EI, Frolov I. </i> J Virol, 2018","reference_id":"29899097","region_id":"DP01468r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Western blot analysis with NAP1L1-specific Abs also definitively detected the latter protein in the co-IP samples generated on the cells infected with VEErep/Flag-GFP-ABCD but not with any other constructs, including VEErep/Flag-GFP-ABC and VEErep/Flag-GFP-123D (Fig. 8B). The most plausible explanation for the lack of NAP1L1 binding to CHIKV HVD deletion mutant constructs was that NAP1L1 binding requires the presence of intact aa sequences of both fragments C and D. Indeed, two isoforms of NAP1L1 were readily detectable in the samples generated from the cells infected with replicons expressing Flag-GFP-12CD and Flag-GFP-12(C3)D fusions (Fig. 8C). This was an indication that NAP1L1 interacts with HVD on the border between C and D fragments (see Fig. 11).","_id":"685af523b4ac24d5329d9106"},{"type":"Curator statement","text":"IDR in the publication is 100% identical to this Uniprot sequence.","_id":"685af523b4ac24d5329d9107"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T09:01:36.665Z","_id":"685af523b4ac24d5329d9108"},"version":1,"_id":"685af523b4ac24d5329d9105","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IEP","ec_id":"ECO:0005636","ec_name":"green fluorescent protein reporter gene assay evidence used in manual assertion","ec_ontology":"ECO","start":1658,"end":1856,"interaction_partner":[],"reference_html":"Multiple Host Factors Interact with the Hypervariable Domain of Chikungunya Virus nsP3 and Determine Viral Replication in Cell-Specific Mode. <i> Meshram CD, Agback P, Shiliaev N, Urakova N, Mobley JA, Agback T, Frolova EI, Frolov I. </i> J Virol, 2018","reference_id":"29899097","region_id":"DP01468r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"These experimental data strongly suggested that HVDs play critical roles in the adaptation of CHIKV and EILV to replication in particular cell types. Despite having very similar G3BP-binding repeating peptides, heterologous HVDs changed cell specificities of replication for both viruses. This was a strong support for the hypothesis that HVD fragments located upstream of the carboxy-terminal G3BP/Rin-binding repeat play an indispensable role in CHIKV replication.","_id":"685af523b4ac24d5329d910a"},{"type":"Discussion","text":"In the case of CHIKV, G3BP binding is particularly critical. In contrast to the results of the studies performed on SINV and SFV, deletion of even a single element of the G3BP-binding HVD repeat had a strong negative effect on CHIKV replication in both vertebrate and mosquito cells (Fig. 2) (34). Deletion of both elements, in turn, completely abrogated virus replication.","_id":"685af523b4ac24d5329d910b"},{"type":"Curator statement","text":"IDR in the publication is 100% identical to this Uniprot sequence.","_id":"685af523b4ac24d5329d910c"}],"states_connection":[],"term_comment":"","term_def":"\"A set of processes which all viruses follow to ensure survival; includes attachment and entry of the virus particle, decoding of genome information, translation of viral mRNA by host ribosomes, genome replication, and assembly and release of viral particles containing the genome.\" [ISBN:1555811272]","term_go_domain":"P","term_id":"GO:0019058","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral life cycle","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T09:01:38.926Z","_id":"685af523b4ac24d5329d910d"},"version":1,"_id":"685af523b4ac24d5329d9109","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-09T08:30:13.895Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006030","ec_name":"co-immunoprecipitation evidence used in manual assertion","ec_ontology":"ECO","start":1658,"end":1856,"interaction_partner":[{"db":"UniProt","id":"Q96B97","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9111"},{"db":"UniProt","id":"Q9Y5K6","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9112"},{"db":"UniProt","id":"O00499","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9113"},{"db":"UniProt","id":"A0A182G3T6","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9114"}],"reference_html":"Multiple Host Factors Interact with the Hypervariable Domain of Chikungunya Virus nsP3 and Determine Viral Replication in Cell-Specific Mode. <i> Meshram CD, Agback P, Shiliaev N, Urakova N, Mobley JA, Agback T, Frolova EI, Frolov I. </i> J Virol, 2018","reference_id":"29899097","region_id":"DP01468r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In vertebrate cells, CHIKV HVD also coimmunoprecipitated cellular SH3-binding proteins BIN1, CD2AP, and SH3KBP1. In mosquito C7/10 cells, it interacted with A0A182G3T6, the mosquito BIN1 homolog (Fig. 6B). Interestingly, isolation of CD2AP/SH3KBP1 and BIN1 was strongly dependent on the cell type. In human Huh7 and mouse NIH 3T3 cells (35), BIN1, but not CD2AP or SH3KBP1, efficiently interacted with CHIKV HVD. However, in another human cell line, HEK 293 cells, CHIKV HVD preferentially interacted with CD2AP and SH3KBP1, but not with BIN1.","_id":"685af523b4ac24d5329d910f"},{"type":"Curator statement","text":"IDR in the publication is 100% identical to this Uniprot sequence.","_id":"685af523b4ac24d5329d9110"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_go_domain":"F","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-16T19:06:23.827Z","_id":"685af523b4ac24d5329d9115"},"version":2,"_id":"685af523b4ac24d5329d910e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-09T08:30:55.128Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006030","ec_name":"co-immunoprecipitation evidence used in manual assertion","ec_ontology":"ECO","start":1658,"end":1856,"interaction_partner":[{"db":"UniProt","id":"Q96B97","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d911a"},{"db":"UniProt","id":"Q9Y5K6","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d911b"},{"db":"UniProt","id":"O00499","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d911c"},{"db":"UniProt","id":"A0A182G3T6","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d911d"}],"reference_html":"Multiple Host Factors Interact with the Hypervariable Domain of Chikungunya Virus nsP3 and Determine Viral Replication in Cell-Specific Mode. <i> Meshram CD, Agback P, Shiliaev N, Urakova N, Mobley JA, Agback T, Frolova EI, Frolov I. </i> J Virol, 2018","reference_id":"29899097","region_id":"DP01468r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In vertebrate cells, CHIKV HVD also coimmunoprecipitated cellular SH3-binding proteins BIN1, CD2AP, and SH3KBP1. In mosquito C7/10 cells, it interacted with A0A182G3T6, the mosquito BIN1 homolog (Fig. 6B). Interestingly, isolation of CD2AP/SH3KBP1 and BIN1 was strongly dependent on the cell type. In human Huh7 and mouse NIH 3T3 cells (35), BIN1, but not CD2AP or SH3KBP1, efficiently interacted with CHIKV HVD. However, in another human cell line, HEK 293 cells, CHIKV HVD preferentially interacted with CD2AP and SH3KBP1, but not with BIN1.","_id":"685af523b4ac24d5329d9117"},{"type":"Discussion","text":"In the case of CHIKV, G3BP binding is particularly critical. In contrast to the results of the studies performed on SINV and SFV, deletion of even a single element of the G3BP-binding HVD repeat had a strong negative effect on CHIKV replication in both vertebrate and mosquito cells (Fig. 2) (34). Deletion of both elements, in turn, completely abrogated virus replication.","_id":"685af523b4ac24d5329d9118"},{"type":"Curator statement","text":"IDR in the publication is 100% identical to this Uniprot sequence.","_id":"685af523b4ac24d5329d9119"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-16T19:06:23.771Z","_id":"685af523b4ac24d5329d911e"},"version":2,"_id":"685af523b4ac24d5329d9116","reference_source":"pmid"}],"__v":0,"disorder_content":0.08043654001616815,"disprot_consensus":{"full":[{"start":1658,"end":1856,"type":"D"}],"Structural state":[{"start":1658,"end":1856,"type":"D"}],"Molecular function":[{"start":1658,"end":1856,"type":"F"}],"Biological process":[{"start":1658,"end":1856,"type":"F"}]}},{"acc":"A4L7I4","sequence":"MDSVYVDIDADSAFLKALQRAYPMFEVEPRQVTSNDHANARAFSHLAIKLIEQEIDPDSTILDIGSAPARRMMSDRKYHCVCPMRSAEDPERLANYARKLASAAGIVLDRNISGKIGDLQAVMAVPDTETPTFCLHTDVSCRQRADVAIYQDVYAVHAPTSLYHQAIKGVRVAYWVGFDTTPFMYNAMAGAYPSYSTNWADEQVLKAKNIGLCSTDLTEGRRGKLSIMRGKKLKPCDRVLFSVGSTLYPESRTLLKSWHLPSVFHLKGKLSFTCRCDTVVSCEGYVVKRITMSPGLYGKTTGYAVTHHADGFLLCKTTDTVDGERVSFSVCTYVPATICDQMTGILATEVTPEDAQKLLVGLNQRIVVNGRTQRNTNTMKNYLLPVVAQAFSKWAKECRKDMEDEKLLGVRERTLTCCCLWAFKKQKTHTVYKRPDTQSIQKVQAEFDSFVVPGLWSSGLSIPLRTRIKWLLRKVPKTDLIPYSGNAQEAQDAEKEAEEEREAELTHEALPPLQAAQEDVQVEIDVEQLEDRAGAGIIETPRGAIKVTAQLTDHVVGEYLVLSPQTVLRSQKLSLIHALAEQVKTCTHSGRAGRYAVEAYDGRVLVPSGYAISPEDFQSLSESATMVYNEREFVNRKLHHIAMHGPALNTDEESYELVRAERTEHEYVYDVDQRRCCKKEEAAGLVLVGDLTNPPYHEFAYEGLKIRPACPYKIAVIGVFGVPGSGKSAIIKNLVTRQDLVTSGKKENCQEISTDVMRQRGLEISARTVDSLLLNGCNRPVDVLYVDEAFACHSGTLLALIALVRPRQKVVLCGDPKQCGFFNMMQMKVNYNHNICTQVYHKSISRRCTLPVTAIVSSLHYEGKMRTTNEYNMPIVVDTTGSTKPDPGDLVLTCFRGWVKQLQIDYRGHEVMTAAASQGLTRKGVYAVRQKVNENPLYASTSEHVNVLLTRTEGKLVWKTLSGDPWIKTLQNPPKGNFKATIKEWEVEHASIMAGICSHQVTFDTFQNKANVCWAKSLVPILETAGIKLNDRQWSQIIQAFKEDKAYSPEVALNEICTRMYGVDLDSGLFSKPLVSVYYADNHWDNRPGGKMFGFNPEAASILERKYPFTKGKWNINKQICVTTRRIEDFNPTTNIIPVNRRLPHSLVAEHRPVKGERMEWLVNKINGHHVLLVSGYNLALPTKRVTWVAPLGVRGADYTYNLELGLPATLGRYDLVVINIHTPFRIHHYQQCVDHAMKLQMLGGDSLRLLKPGGSLLIRAYGYADRTSERVICVLGRKFRSSRALKPPCVTSNTEMFFLFSNFDNGRRNFTTHVMNNQLNAAFVGQATRAGCAPSYRVKRMDIAKNDEECVVNAANPRGLPGDGVCKAVYKKWPESFKNSATPVGTAKTVMCGTYPVIHAVGPNFSNYSESEGDRELAAAYREVAKEVTRLGVNSVAIPLLSTGVYSGGKDRLTQSLNHLFTAMDSTDADVVIYCRDKEWEKKISEAIQMRTQVELLDEHISIDCDVIRVHPDSSLAGRKGYSTTEGALYSYLEGTRFHQTAVDMAEIYTMWPKQTEANEQVCLYALGESIESIRQKCPVDDADASSPPKTVPCLCRYAMTPERVTRLRMNHVTNIIVCSSFPLPKYKIEGVQKVKCSKVMLFDHNVPSRVSPREYRSSQESVQEVSTTTSLTHSQFDLSADGETLPVPSDLDADAPALEPALDDGAVHTLPTIIGNLAAVSDWVMSTVPVAPPRRRRGRNLTVTCDEREGNITPMASVRFFRAELCPAVQETAETRDTAISLQAPPSTTMELSHPPISFGAPSETFPITFGDFDEGEIESLSSELLTFGDFLPGEVDDLTDSDWSTCPDTDDELXLDRAGGYIFSSDTGPGHLQQKSVRQSVLPVNTLEEVHEEKCYPPKLDELKEQLLLKKLQESASMANRSRYQSRKVENMKATIIQRLKRGCKLYLMAETPKVPTYRTIYPAPVYSPPINVRLSNPESAVAACNEFLARNYPTVSSYQITDEYDAYLDMVDGSESCLDRATFNPSKLRSYPKQHAYHAPSIRSAVPSPFQNTLQNVLAAATKRNCNVTQMRELPTLDSAVFNVECFKKFACNREYWEEFAASPIRITTENLTTYVTKLKGPKAAALFAKTHNLLPLQDVPMDRFTVDMKRDVKVTPGTKHTEERPKVQVIQAAEPLATAYLCGIHRELVRRLNAVLLPNVHTLFDMSAEDFDAIIAAHFKPGDAVLETDIASFDKSQDDSLALTALMLLEDLGVDHSLLDLIEAAFGEISSCHLPTGTRFKFGAMMKSGMFLTLFVNTLLNITIASRVLEDRLTKSACAAFIGDDNIIHGVVSDELMAARCATWMNMEVKIIDAVVSQKAPYFCGGFILHDTVTGTACRVADPLKRLFKLGKPLAAGDEQDEDRRRALADEVIRWQRTGLIDELEKAVYSRYEVQGISVAVMSMATFASSRSNFEKLRGPVITLYGGPK","creator":"mmacossay","dataset":["Viral proteins","Neglected tropical diseases proteins"],"date":"2018-07-19T14:56:04.000Z","disprot_id":"DP01469","features":{"pfam":[],"gene3D":[{"start":713,"end":842,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d912b"},{"start":1003,"end":1140,"id":"3.90.70.110","name":"Alphavirus nsP2 protease domain","_id":"685af523b4ac24d5329d912c"},{"start":843,"end":982,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d912d"},{"start":1145,"end":1506,"id":"3.40.50.150","name":"Vaccinia Virus protein VP39","_id":"685af523b4ac24d5329d912e"},{"start":1337,"end":1493,"id":"3.40.220.10","name":"Leucine Aminopeptidase, subunit E, domain 1","_id":"685af523b4ac24d5329d912f"}]},"genes":[{"name":{"value":"CHIKVgp1","evidences":[{"source":{"id":"ABO38822.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/ABO38822.1","_id":"685af523b4ac24d5329d9155"},"code":"ECO:0000313","_id":"685af523b4ac24d5329d9154"}],"_id":"685af523b4ac24d5329d9156"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d9153"}],"length":2474,"name":"Nonstructural polyprotein","ncbi_taxon_id":37124,"organism":"Chikungunya virus","regions_counter":6,"released":"2018_11","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Alsuviricetes","Martellivirales","Togaviridae","Alphavirus"],"UniParc":"UPI0000F6DAAD","uniref100":"UniRef100_A4L7I4","uniref50":"UniRef50_P08411","uniref90":"UniRef90_Q8JUX6","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1658,"end":1856,"interaction_partner":[],"reference_html":"Multiple Host Factors Interact with the Hypervariable Domain of Chikungunya Virus nsP3 and Determine Viral Replication in Cell-Specific Mode. <i> Meshram CD, Agback P, Shiliaev N, Urakova N, Mobley JA, Agback T, Frolova EI, Frolov I. </i> J Virol, 2018","reference_id":"29899097","region_id":"DP01469r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"It exhibits a reduced chemical shift dispersion, especially in the 1H dimension between 8.5 and 7.5 ppm (Fig. 1C), which is a characteristic of the intrinsically disordered proteins (42).","_id":"685af523b4ac24d5329d9131"},{"type":"Discussion","text":"We carried out detailed characterization of a 199-aa-long CHIKV HVD by NMR spectroscopy at atomic resolution. The results revealed the absence of stable secondary structures in this domain and clearly demonstrated that CHIKV HVD was present in solution in a disordered conformation.","_id":"685af523b4ac24d5329d9132"},{"type":"Curator statement","text":"IDR in the publication is 100% identical to this Uniprot sequence.","_id":"685af523b4ac24d5329d9133"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T09:01:42.700Z","_id":"685af523b4ac24d5329d9134"},"version":3,"_id":"685af523b4ac24d5329d9130","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IEP","ec_id":"ECO:0000279","ec_name":"qualitative western immunoblotting evidence used in manual assertion","ec_ontology":"ECO","start":1761,"end":1856,"interaction_partner":[],"reference_html":"Multiple Host Factors Interact with the Hypervariable Domain of Chikungunya Virus nsP3 and Determine Viral Replication in Cell-Specific Mode. <i> Meshram CD, Agback P, Shiliaev N, Urakova N, Mobley JA, Agback T, Frolova EI, Frolov I. </i> J Virol, 2018","reference_id":"29899097","region_id":"DP01469r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Western blot analysis with NAP1L1-specific Abs also definitively detected the latter protein in the co-IP samples generated on the cells infected with VEErep/Flag-GFP-ABCD but not with any other constructs, including VEErep/Flag-GFP-ABC and VEErep/Flag-GFP-123D (Fig. 8B). The most plausible explanation for the lack of NAP1L1 binding to CHIKV HVD deletion mutant constructs was that NAP1L1 binding requires the presence of intact aa sequences of both fragments C and D. Indeed, two isoforms of NAP1L1 were readily detectable in the samples generated from the cells infected with replicons expressing Flag-GFP-12CD and Flag-GFP-12(C3)D fusions (Fig. 8C). This was an indication that NAP1L1 interacts with HVD on the border between C and D fragments (see Fig. 11).","_id":"685af523b4ac24d5329d913a"},{"type":"Curator statement","text":"IDR in the publication is 100% identical to this Uniprot sequence.","_id":"685af523b4ac24d5329d913b"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T09:01:45.720Z","_id":"685af523b4ac24d5329d913c"},"version":1,"_id":"685af523b4ac24d5329d9139","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-09T08:31:44.996Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006030","ec_name":"co-immunoprecipitation evidence used in manual assertion","ec_ontology":"ECO","start":1658,"end":1856,"interaction_partner":[{"db":"UniProt","id":"Q96B97","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9141"},{"db":"UniProt","id":"Q9Y5K6","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9142"},{"db":"UniProt","id":"O00499","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9143"},{"db":"UniProt","id":"A0A182G3T6","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9144"}],"reference_html":"Multiple Host Factors Interact with the Hypervariable Domain of Chikungunya Virus nsP3 and Determine Viral Replication in Cell-Specific Mode. <i> Meshram CD, Agback P, Shiliaev N, Urakova N, Mobley JA, Agback T, Frolova EI, Frolov I. </i> J Virol, 2018","reference_id":"29899097","region_id":"DP01469r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In vertebrate cells, CHIKV HVD also coimmunoprecipitated cellular SH3-binding proteins BIN1, CD2AP, and SH3KBP1. In mosquito C7/10 cells, it interacted with A0A182G3T6, the mosquito BIN1 homolog (Fig. 6B). Interestingly, isolation of CD2AP/SH3KBP1 and BIN1 was strongly dependent on the cell type. In human Huh7 and mouse NIH 3T3 cells (35), BIN1, but not CD2AP or SH3KBP1, efficiently interacted with CHIKV HVD. However, in another human cell line, HEK 293 cells, CHIKV HVD preferentially interacted with CD2AP and SH3KBP1, but not with BIN1.","_id":"685af523b4ac24d5329d913e"},{"type":"Discussion","text":"In the case of CHIKV, G3BP binding is particularly critical. In contrast to the results of the studies performed on SINV and SFV, deletion of even a single element of the G3BP-binding HVD repeat had a strong negative effect on CHIKV replication in both vertebrate and mosquito cells (Fig. 2) (34). Deletion of both elements, in turn, completely abrogated virus replication.","_id":"685af523b4ac24d5329d913f"},{"type":"Curator statement","text":"IDR in the publication is 100% identical to this Uniprot sequence.","_id":"685af523b4ac24d5329d9140"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-16T19:51:19.062Z","_id":"685af523b4ac24d5329d9145"},"version":2,"_id":"685af523b4ac24d5329d913d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-09T08:32:46.475Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006030","ec_name":"co-immunoprecipitation evidence used in manual assertion","ec_ontology":"ECO","start":1658,"end":1856,"interaction_partner":[{"db":"UniProt","id":"Q96B97","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9149"},{"db":"UniProt","id":"Q96B97","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d914a"},{"db":"UniProt","id":"O00499","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d914b"},{"db":"UniProt","id":"A0A182G3T6","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d914c"}],"reference_html":"Multiple Host Factors Interact with the Hypervariable Domain of Chikungunya Virus nsP3 and Determine Viral Replication in Cell-Specific Mode. <i> Meshram CD, Agback P, Shiliaev N, Urakova N, Mobley JA, Agback T, Frolova EI, Frolov I. </i> J Virol, 2018","reference_id":"29899097","region_id":"DP01469r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In vertebrate cells, CHIKV HVD also coimmunoprecipitated cellular SH3-binding proteins BIN1, CD2AP, and SH3KBP1. In mosquito C7/10 cells, it interacted with A0A182G3T6, the mosquito BIN1 homolog (Fig. 6B). Interestingly, isolation of CD2AP/SH3KBP1 and BIN1 was strongly dependent on the cell type. In human Huh7 and mouse NIH 3T3 cells (35), BIN1, but not CD2AP or SH3KBP1, efficiently interacted with CHIKV HVD. However, in another human cell line, HEK 293 cells, CHIKV HVD preferentially interacted with CD2AP and SH3KBP1, but not with BIN1.","_id":"685af523b4ac24d5329d9147"},{"type":"Curator statement","text":"IDR in the publication is 100% identical to this Uniprot sequence.","_id":"685af523b4ac24d5329d9148"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_go_domain":"F","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-09-16T19:51:17.922Z","_id":"685af523b4ac24d5329d914d"},"version":2,"_id":"685af523b4ac24d5329d9146","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IEP","ec_id":"ECO:0005636","ec_name":"green fluorescent protein reporter gene assay evidence used in manual assertion","ec_ontology":"ECO","start":1658,"end":1856,"interaction_partner":[],"reference_html":"Multiple Host Factors Interact with the Hypervariable Domain of Chikungunya Virus nsP3 and Determine Viral Replication in Cell-Specific Mode. <i> Meshram CD, Agback P, Shiliaev N, Urakova N, Mobley JA, Agback T, Frolova EI, Frolov I. </i> J Virol, 2018","reference_id":"29899097","region_id":"DP01469r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"These experimental data strongly suggested that HVDs play critical roles in the adaptation of CHIKV and EILV to replication in particular cell types. Despite having very similar G3BP-binding repeating peptides, heterologous HVDs changed cell specificities of replication for both viruses. This was a strong support for the hypothesis that HVD fragments located upstream of the carboxy-terminal G3BP/Rin-binding repeat play an indispensable role in CHIKV replication.","_id":"685af523b4ac24d5329d914f"},{"type":"Discussion","text":"In the case of CHIKV, G3BP binding is particularly critical. In contrast to the results of the studies performed on SINV and SFV, deletion of even a single element of the G3BP-binding HVD repeat had a strong negative effect on CHIKV replication in both vertebrate and mosquito cells (Fig. 2) (34). Deletion of both elements, in turn, completely abrogated virus replication.","_id":"685af523b4ac24d5329d9150"},{"type":"Curator statement","text":"IDR in the publication is 100% identical to this Uniprot sequence.","_id":"685af523b4ac24d5329d9151"}],"states_connection":[],"term_comment":"","term_def":"\"A set of processes which all viruses follow to ensure survival; includes attachment and entry of the virus particle, decoding of genome information, translation of viral mRNA by host ribosomes, genome replication, and assembly and release of viral particles containing the genome.\" [ISBN:1555811272]","term_go_domain":"P","term_id":"GO:0019058","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral life cycle","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T09:01:50.151Z","_id":"685af523b4ac24d5329d9152"},"version":1,"_id":"685af523b4ac24d5329d914e","reference_source":"pmid"}],"__v":0,"disorder_content":0.08043654001616815,"disprot_consensus":{"full":[{"start":1658,"end":1856,"type":"D"}],"Structural state":[{"start":1658,"end":1856,"type":"D"}],"Molecular function":[{"start":1658,"end":1856,"type":"F"}],"Biological process":[{"start":1658,"end":1856,"type":"F"}]}},{"features":{"pfam":[{"id":"PF15458","name":"Nineteen complex-related protein 2","start":77,"end":312}]},"uniref50":"UniRef50_P36118","sequence":"MAIKKRNKIRLPSGSPEEVGIDGSAHKPMQQIKPLVSNDSEDDDNDICVLQPIKFKKVPKRDITFDGEQAIKEDNSHYEDLYHSKKNTNASTRNKDDLLILNMEDLMEGNHHLLSDSSEAGSSSEGEHISSIPTRGEIAKLKAQKSLSRRKISESDVTTERDYVKLLDSEDKREIMETIRLNGGLKRNNEKEITNFSDDEMQGFQDEMLALTDNQIAIQKDSKRKIIEKAINEVPYRTNEEWETQLLSKGNINKSNEKIITPLPVLFPDDDESGNSIERINEMVSKICLQRKKVEMRLQALEKTKIDLEKSKASLINKLIGN","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P36118","disprot_id":"DP01471","ncbi_taxon_id":559292,"regions_counter":4,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":322,"region_id":"DP01471r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Intrinsically Disordered Protein Ntr2 Modulates the Spliceosomal RNA Helicase Brr2. <i> Wollenhaupt J, Henning LM, Sticht J, Becke C, Freund C, Santos KF, Wahl MC. </i> Biophys J, 2018","statement":[{"text":"Intrinsic disorder\nof full-length Ntr2 was also reflected in its 1H-15NHSQC\nNMR spectrum","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":1,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29490241","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":322,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Intrinsically Disordered Protein Ntr2 Modulates the Spliceosomal RNA Helicase Brr2. <i> Wollenhaupt J, Henning LM, Sticht J, Becke C, Freund C, Santos KF, Wahl MC. </i> Biophys J, 2018","statement":[{"text":"Together\nwith the peptide SPOT analysis, the results presented above\nshow that the N-terminal half of Ntr2 encompasses three\nBrr2-binding regions, of which the first two regions (within\nresidues 1–75) are necessary and sufficient for stable Brr2\nbinding in SEC.","type":"Results"}],"term_id":"GO:0005515","curator_id":"eschad","start":1,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"29490241","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01471r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":322,"region_id":"DP01471r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Intrinsically Disordered Protein Ntr2 Modulates the Spliceosomal RNA Helicase Brr2. <i> Wollenhaupt J, Henning LM, Sticht J, Becke C, Freund C, Santos KF, Wahl MC. </i> Biophys J, 2018","statement":[{"text":"CD spectra of\nboth Ntr2FL and the N-terminal half of the protein (residues\n1–162: Ntr21–162) at 20 \u0001 C showed a global minimum at\naround 200 nm, lacked a CD signal at 190 nm, and exhibited\na flat region in the 210–230 nm range (Fig. 1 B), which are\ntypical signatures of intrinsically disordered proteins (IDPs)","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":1,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29490241","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":322,"region_id":"DP01471r004","released":"2022_03","ec_id":"ECO:0007064","reference_html":"Intrinsically Disordered Protein Ntr2 Modulates the Spliceosomal RNA Helicase Brr2. <i> Wollenhaupt J, Henning LM, Sticht J, Becke C, Freund C, Santos KF, Wahl MC. </i> Biophys J, 2018","statement":[{"text":"The hydrodynamic\nradii of Ntr2FL, Ntr21–162, and Ntr21–75 derived from\nquasi-elastic light scattering were in excellent agreement\nwith the expected values for IDPs","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":1,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"dynamic light scattering assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29490241","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P36118","date":"2018-07-19T16:18:57.000Z","acc":"P36118","name":"Pre-mRNA-splicing factor NTR2","length":322,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000013B62A","genes":[{"name":{"value":"NTR2"},"olnNames":[{"value":"YKR022C"}]}],"alphafold_very_low_content":0.30124223602484473,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":322,"type":"D"}],"Structural state":[{"start":1,"end":322,"type":"D"}],"Molecular function":[{"start":1,"end":322,"type":"F"}]}},{"features":{"pfam":[{"id":"PF07577","name":"Domain of Unknown Function (DUF1547)","start":751,"end":810},{"id":"PF07577","name":"Domain of Unknown Function (DUF1547)","start":873,"end":930}]},"uniref50":"UniRef50_Q6GX35","sequence":"MTNSISGDQPTVTTFTSSTTSASGASGSLGASSVSTTANATVTQTANATNSAATSSIQTTGETVVNYTNSASAPTVTVSTSSSSTQATATSNKTSQAVAGKITSPDTSESSETSSTSSSDHIPSDYEPISTTENIYENIYESIDDSSTSGPENTSGGAAALNSLRGSSYSNYDDAAADYEPISTTENIYESIDDSSTSDPENTSGGAAALNSLRGSSYSNYDDAAADYEPISTTENIYENIYESIDDSSTSGPENTSGGAAALNSLRGSSYSNYDDAAADYEPISTTENIYESIDDSSTSDPENTSGGAAAALNSLRGSSYSNYDDAAADYEPISTTENIYESIDDSSTSDPENTSGGAAALNSLRGSSYSNYDDAAADYEPISTTENIYENIYESIDGSSTSDPENTSGGAAAALNSLRGSSYTTGPRNEGVFGPGPEGLPDMSLPSYDPTNKTSLLTFLSNPHVKSKMLENSGHFVFIDTDRSSFILVPNGNWDQVCSIKVQNGKTKEDLDIKDLENMCAKFCTGFNKFSGDWDSRVEPMMSAKAGVASGGNLPNTVIINNKFKTCVAYGPWNSREASSGYTPSAWRRGHQVNFGEIFEKANDFNKINWGTQAGPSSEDDGISFSNETPGAGPAAAPSPTPSSIPVINVNVNVGGTNVNIRDTNVNTTNTTPTTQSTDASTDTSDIDNINTNNQTDDINTTDKDSDGAGGVNGDISETESSSGDDSGSVSSSESDKNASVGNDGPAMKDILSAVRKHLDVVYPGDNGGSTEGPLQANQTLGDIVQDMETTGTSQETVVSPWKGSTSSTGSAGGSGSVQTLLPSPPPTPSTTTLRTGTGATTTSLMMGGPIKADIITTGGGGRIPGGGTLEKLLPRIRAHLDISFDGQGDLVSTEEPQLGSIVNKFRKETGSGGIVASVESAPGKPGSAQVLTGTGGDKGNLFQAAAAVTQALGNVAGKVNLAIQGQKLSSLVNDDGKGSVGRDLFQAATQTTQALSSLIDTVG","taxonomy":["Bacteria","Chlamydiae","Chlamydiales","Chlamydiaceae","Chlamydia/Chlamydophila group","Chlamydia"],"uniref90":"UniRef90_Q6GX35","disprot_id":"DP01472","ncbi_taxon_id":471472,"regions_counter":4,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":825,"region_id":"DP01472r001","released":"2022_12","ec_id":"ECO:0006165","reference_html":"The intrinsically disordered Tarp protein from chlamydia binds actin with a partially preformed helix. <i> Tolchard J, Walpole SJ, Miles AJ, Maytum R, Eaglen LA, Hackstadt T, Wallace BA, Blumenschein TMA. </i> Sci Rep, 2018","statement":[{"text":"The 2D [1H,15N]-HSQC spectrum\nof 15N-labelled Tarp726–825, a construct containing the G-actin binding domain (Fig. 1), shows extremely narrow\nspectral dispersion in the 1H dimension of the backbone amide chemical shifts (majority of peaks within\n~0.7 ppm). This is a typical characteristic of an intrinsically disordered protein (IDP).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":726,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-10-04T13:44:00.885Z","reference_source":"pmid","term_name":"disorder","reference_id":"29386631","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"BMRB","id":"27263"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-04T13:57:48.929Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":825,"term_name":"protein binding","released":"2022_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The intrinsically disordered Tarp protein from chlamydia binds actin with a partially preformed helix. <i> Tolchard J, Walpole SJ, Miles AJ, Maytum R, Eaglen LA, Hackstadt T, Wallace BA, Blumenschein TMA. </i> Sci Rep, 2018","statement":[{"text":"Tarp binds G-actin with high affinity and increases in helical content","type":"Results"}],"term_id":"GO:0005515","curator_id":"eschad","start":726,"term_ontology":"GO","curator_name":"Eva Schad","reference_id":"29386631","version":4,"curator_orcid":"0000-0002-3006-2910","date":"2022-10-04T15:15:06.142Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01472r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P68139","operator":null,"partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-19T16:26:16.553Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":825,"term_name":"disorder to order","released":"2022_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The intrinsically disordered Tarp protein from chlamydia binds actin with a partially preformed helix. <i> Tolchard J, Walpole SJ, Miles AJ, Maytum R, Eaglen LA, Hackstadt T, Wallace BA, Blumenschein TMA. </i> Sci Rep, 2018","statement":[{"text":"Furthermore, NMR experiments in the presence of G-actin indicate this interaction affects the proposed WH2-like α-helical region, supporting results from in silico docking calculations which suggest that, when folded, this α-helix binds within the actin hydrophobic cleft as seen for other actin-associated proteins.","type":"Abstract"}],"term_id":"IDPO:0000011","curator_id":"eschad","start":726,"term_ontology":"IDPO","curator_name":"Eva Schad","reference_id":"29386631","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-10-04T13:46:16.071Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01472r003","ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-04T13:58:02.158Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":825,"region_id":"DP01472r004","released":"2022_12","ec_id":"ECO:0006204","reference_html":"The intrinsically disordered Tarp protein from chlamydia binds actin with a partially preformed helix. <i> Tolchard J, Walpole SJ, Miles AJ, Maytum R, Eaglen LA, Hackstadt T, Wallace BA, Blumenschein TMA. </i> Sci Rep, 2018","statement":[{"text":"The SRCD spectrum of Tarp726–825 (Supplementary Fig. S4) is also consistent with a secondary structure that is primarily instrinsically disordered. Furthermore, thermal-melt SRCD studies of the construct also show behaviour typical of an IDP: the spectral changes (increase in the 224 nm shoulder and decrease in the peak around 190 nm, Supplementary Fig. S4) correspond to a decreased calculated disordered content with increasing temperature, a behaviour that directly contrasts with that seen for most fully folded (not IDP) proteins.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":726,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-10-04T13:41:20.390Z","reference_source":"pmid","term_name":"disorder","reference_id":"29386631","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-04T13:57:22.844Z"}}],"released":"2018_11","uniref100":"UniRef100_Q6GX35","date":"2018-07-19T16:51:29.000Z","acc":"Q6GX35","name":"Translocated actin-recruiting phosphoprotein","length":1005,"organism":"Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B)","dataset":["Neglected tropical diseases proteins","Bacterial virulence-related proteins"],"UniParc":"UPI00003B4AB0","genes":[{"name":{"value":"tarP"},"olnNames":[{"value":"CTL0716"}]}],"alphafold_very_low_content":0.7900497512437811,"disorder_content":0.09950248756218906,"disprot_consensus":{"full":[{"start":726,"end":825,"type":"T"}],"Structural state":[{"start":726,"end":825,"type":"D"}],"Molecular function":[{"start":726,"end":825,"type":"F"}],"Structural transition":[{"start":726,"end":825,"type":"T"}]}},{"features":{"pfam":[{"id":"PF05831","name":"GAGE protein","start":21,"end":129}]},"uniref50":"UniRef50_Q96GU1","sequence":"MQAPWAGNRGWAGTREEVRDMSEHVTRSQSSERGNDQESSQPVGPVIVQQPTEEKRQEEEPPTDNQGIAPSGEIKNEGAPAVQGTDVEAFQQELALLKIEDAPGDGPDVREGTLPTFDPTKVLEAGEGQL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q96GU1","disprot_id":"DP01473","ncbi_taxon_id":9606,"regions_counter":1,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":130,"region_id":"DP01473r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Characterization of intrinsically disordered prostate associated gene (PAGE5) at single residue resolution by NMR spectroscopy. <i> Hellman M, Tossavainen H, Rappu P, Heino J, Permi P. </i> PLoS One, 2011","statement":[{"text":"Taken together, in the present study we have shown using the experimental data at single residue resolution level that PAGE5, a member of GAGE family proteins, is an intrinsically highly disordered protein.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":20,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22073178","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q96GU1","date":"2018-07-19T19:53:19.000Z","acc":"Q96GU1","name":"P antigen family member 5","length":130,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000006D8BC","genes":[{"name":{"value":"PAGE5"},"synonyms":[{"value":"GAGEE1"}]}],"alphafold_very_low_content":0.03076923076923077,"disorder_content":0.8538461538461538,"disprot_consensus":{"full":[{"start":20,"end":130,"type":"D"}],"Structural state":[{"start":20,"end":130,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03066","name":"Nucleoplasmin/nucleophosmin domain","start":16,"end":118},{"id":"PF16276","name":"Nucleophosmin C-terminal domain","start":245,"end":293}],"gene3D":[{"start":241,"end":294,"id":"1.10.10.2100","name":"1.10.10.2100"},{"start":9,"end":124,"id":"2.60.120.340","name":"Nucleoplasmin core domain"}]},"uniref50":"UniRef50_P06748","sequence":"MEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEEEEDVKLLSISGKRSAPGGGSKVPQKKVKLAADEDDDDDDEEDDDEDDDDDDFDDEEAEEKAPVKKSIRDTPAKNAQKSNQNGKDSKPSSTPRSKGQESFKKQEKTPKTPKGPSSVEDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P06748","disprot_id":"DP01474","ncbi_taxon_id":9606,"regions_counter":23,"creator":"epapa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":259,"region_id":"DP01474r005","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Intrinsically disordered regions of nucleophosmin/B23 regulate its RNA binding activity through their inter- and intra-molecular association. <i> Hisaoka M, Nagata K, Okuwaki M. </i> Nucleic Acids Res, 2014","statement":[{"text":"His-B23.1-CR1 showed a typical random-coil pattern peaking at 195 nm (blue line), as previously reported (25).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":189,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-27T16:36:27.757Z","reference_source":"pmid","term_name":"disorder","reference_id":"24106084","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-13T17:24:20.170Z"}},{"start":120,"end":130,"reference_id":"26836305","reference_source":"pmid","reference_html":"Nucleophosmin integrates within the nucleolus via multi-modal interactions with proteins displaying R-rich linear motifs and rRNA. <i> Mitrea DM, Cika JA, Guy CS, Ban D, Banerjee PR, Stanley CB, Nourse A, Deniz AA, Kriwacki RW. </i> Elife, 2016","date":"2023-11-27T16:21:25.335Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2023_12","version":3,"region_id":"DP01474r015","statement":[{"text":"Above the phase separation threshold (>3:1 rpL5:N130), resonances for residues within the N130 core broadened beyond detection in 2D 1H-15N TROSY spectra but not those for residues within the A2 tract (Figure 4a). Chemical shift values indicated that these residues remained disordered.","type":"Results"},{"text":"Since N130 consists of a folded pentameric core and disordered N- and C-termini, proper sampling of the relaxation profiles was necessary. Therefore, experiments were recorded with different delay times for resonances from the folded core and the disordered N- and C-termini.","type":"Methods"},{"text":"Although the N- and C-termini remain disordered, the N-terminus exhibits increased rigidity as indicated by the changes in S2 values and whose relaxation behavior was best described using the globally determined τc that was fixed during the LS-MF analysis (Figure 4c,i).","type":"Methods"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-13T17:24:22.244Z"}},{"start":119,"end":243,"reference_id":"24106084","reference_source":"pmid","reference_html":"Intrinsically disordered regions of nucleophosmin/B23 regulate its RNA binding activity through their inter- and intra-molecular association. <i> Hisaoka M, Nagata K, Okuwaki M. </i> Nucleic Acids Res, 2014","date":"2023-11-30T12:04:20.433Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01474r016","statement":[{"text":"The spectrum recorded for His-B23.1 -ΔN showed negative peaks at ∼222 and 200 nm (purple line). Because negative peaks at 222 and 208 nm and that at 200 nm are indicative of α-helix and random-coil structure, respectively, we inferred that His-B23.1 -ΔN contained both α-helix and random-coil structures. Consistent with previous nuclear magnetic resonance studies (24), the spectrum of B23.1-CR1.5 (amino acids 242–294) peaked at ∼222 and 208 nm (Figure 2C, light purple line). When the sequences adjacent to CTD were elongated (His-B23.1-CR and His-B23.1 -ΔN), the peak at 208 nm shifted to ∼200 nm.","type":"Results"},{"text":"These results indicated that the central region of B23 containing acidic and basic regions was disordered in solution.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-13T17:24:24.802Z"}},{"start":120,"end":243,"reference_id":"24106084","reference_source":"pmid","reference_html":"Intrinsically disordered regions of nucleophosmin/B23 regulate its RNA binding activity through their inter- and intra-molecular association. <i> Hisaoka M, Nagata K, Okuwaki M. </i> Nucleic Acids Res, 2014","date":"2023-11-30T10:19:14.097Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019843","term_name":"rRNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","region_id":"DP01474r017","statement":[{"text":"GST-B23.1 preincubated with total RNAs was recovered in the fractions yielding 28S rRNA (Figure 3C, right panel). Consistent with this result, the fractionation pattern of 28S rRNA but not of 18S rRNA shifted slightly to the bottom (Figure 3D, top graphs), suggesting that B23.1 preferentially associated with 28S rRNA. When GST-B23.1-CR1 was preincubated with RNA, its distribution pattern shifted to high-density fractions (Figure 3C, left panel, lanes 5–10). In contrast, GST-B23.1-CR1.5 was not clearly cofractionated with rRNAs.","type":"Results"},{"text":"Consistent with this result, GST pull-down assays showed that GST-B23.1-CR1 efficiently precipitated both 18S and 28S rRNA but GST-B23.1-CR1.5 and GST did so inefficiently (data not shown). These results indicated that bIDR had potential RNA binding activity and that CTD alone could not efficiently associate with rRNAs.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a ribosomal RNA.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"RNAcentral","id":"URS00025C25E0_9606","operator":"and","partner_start":null,"partner_end":null},{"db":"RNAcentral","id":"URS00025D0EC0_9606","operator":"or","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-13T17:24:28.017Z"}},{"start":120,"end":188,"reference_id":"24106084","reference_source":"pmid","reference_html":"Intrinsically disordered regions of nucleophosmin/B23 regulate its RNA binding activity through their inter- and intra-molecular association. <i> Hisaoka M, Nagata K, Okuwaki M. </i> Nucleic Acids Res, 2014","date":"2024-05-06T17:42:04.879Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001170","ec_ontology":"ECO","ec_name":"cross-linking evidence used in manual assertion","unpublished":true,"released":"2024_06","version":1,"region_id":"DP01474r018","statement":[{"text":"His-tagged B23.1-ΔN and B23.2-ΔN were cross-linked with 0.1% glutaraldehyde and separated using SDS–PAGE, followed by CBB staining. Both His-B23.1-ΔN and His-B23.2-ΔN were found to be monomers at low protein concentrations because of the absence of the N-terminal oligomerization domain (Figure 7E, lanes 1 and 2). Bands corresponding to dimers appeared when His-B23.1-ΔN protein concentration was increased, whereas the dimer formation of His-B23.2-ΔN was inefficient (Figure 7E, lanes 5 and 6).","type":"Results"},{"text":"Therefore, we conclude that aIDR and bIDR of both B23.1-ΔN and B23.2-ΔN interact intra-molecularly, and that B23.1-ΔN also has the potential to form inter-molecular interactions (Figure 7F).","type":"Results"},{"text":"The authors refers as aIDR and bIDR to the 120-188 and 189-243 region of Nucleophosmin, respectively.","type":"Curator statement"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P06748","operator":null,"partner_start":189,"partner_end":243}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":120,"end":188,"reference_id":"24106084","reference_source":"pmid","reference_html":"Intrinsically disordered regions of nucleophosmin/B23 regulate its RNA binding activity through their inter- and intra-molecular association. <i> Hisaoka M, Nagata K, Okuwaki M. </i> Nucleic Acids Res, 2014","date":"2023-11-30T12:11:50.679Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000059","term_name":"self-inhibition","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007684","ec_ontology":"ECO","ec_name":"protein separation evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP01474r019","statement":[{"text":"The fractionation pattern of 28S and 18S rRNAs indicated that the aIDR mutants associated with both rRNAs. The fraction shifts in fractions of both rRNAs incubated with GST-B23.1-ΔA1A2 were more prominent than those of RNAs incubated with the B23.1-CR1 mutant (see Figure 3C and D), possibly due to the oligomer formation of GST-B23.1-ΔA1A2. In addition, both 28S and 18S rRNAs incubated with GST-B23.1-ΔA1A2 were recovered in higher-density fractions than those incubated with GST-B23.1-ΔA2 (Figure 5C and D).","type":"Results"},{"text":"From these results, we concluded that the RNA binding activity of bIDR is negatively regulated by aIDR and that aIDR confers RNA binding specificity on B23.1.","type":"Results"},{"text":"The authors refers as aIDR and bIDR to the 120-188 and 189-243 region of Nucleophosmin, respectively.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a domain within the same polypeptide.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Val119Asp132del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ala160Glu188del","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00025C25E0_9606"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00025D0EC0_9606"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-13T17:25:53.101Z"}},{"start":189,"end":243,"reference_id":"24106084","reference_source":"pmid","reference_html":"Intrinsically disordered regions of nucleophosmin/B23 regulate its RNA binding activity through their inter- and intra-molecular association. <i> Hisaoka M, Nagata K, Okuwaki M. </i> Nucleic Acids Res, 2014","date":"2024-05-06T17:38:53.460Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001170","ec_ontology":"ECO","ec_name":"cross-linking evidence used in manual assertion","unpublished":true,"released":"2024_06","version":1,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P06748","operator":null,"partner_start":120,"partner_end":188}],"region_id":"DP01474r020","statement":[{"text":"His-tagged B23.1-ΔN and B23.2-ΔN were cross-linked with 0.1% glutaraldehyde and separated using SDS–PAGE, followed by CBB staining. Both His-B23.1-ΔN and His-B23.2-ΔN were found to be monomers at low protein concentrations because of the absence of the N-terminal oligomerization domain (Figure 7E, lanes 1 and 2). Bands corresponding to dimers appeared when His-B23.1-ΔN protein concentration was increased, whereas the dimer formation of His-B23.2-ΔN was inefficient (Figure 7E, lanes 5 and 6).","type":"Results"},{"text":"Therefore, we conclude that aIDR and bIDR of both B23.1-ΔN and B23.2-ΔN interact intra-molecularly, and that B23.1-ΔN also has the potential to form inter-molecular interactions (Figure 7F).","type":"Results"},{"text":"The authors refers as aIDR and bIDR to the 120-188 and 189-243 region of Nucleophosmin, respectively.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":197,"end":201,"reference_id":"12058066","reference_source":"pmid","reference_html":"The RNA binding activity of a ribosome biogenesis factor, nucleophosmin/B23, is modulated by phosphorylation with a cell cycle-dependent kinase and by association with its subtype. <i> Okuwaki M, Tsujimoto M, Nagata K. </i> Mol Biol Cell, 2002","date":"2023-11-30T12:55:45.851Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001202","ec_ontology":"ECO","ec_name":"in vitro protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr199Ala","start":null,"end":null,"position":null}],"region_id":"DP01474r021","statement":[{"text":"Wild-type B23.1 and histone H1 were efficiently phosphorylated by cyclin E/cdk2 purified from NIH3T3 cells (Figure 6C, lane 2), although T199A and T4A, in which known cyclin E/cdk2-target threonine residues are substituted by alanine (Figure ​6B), were not efficiently phosphorylated (Figure 6C, lanes 3 and 4). This is consistent with the previous report that T199 in B23.1 is phosphorylated by cyclin E/cdk2 (Tokuyama et al., 2001).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-13T17:26:08.611Z"}},{"start":217,"end":221,"reference_id":"12058066","reference_source":"pmid","reference_html":"The RNA binding activity of a ribosome biogenesis factor, nucleophosmin/B23, is modulated by phosphorylation with a cell cycle-dependent kinase and by association with its subtype. <i> Okuwaki M, Tsujimoto M, Nagata K. </i> Mol Biol Cell, 2002","date":"2023-11-30T12:54:17.039Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001218","ec_ontology":"ECO","ec_name":"in vivo protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01474r022","statement":[{"text":"Migration positions of Flag-tagged T199A and T219/234/237A are also shifted from those of interphase proteins, although the band shift of these mutant proteins in mitotic extracts was less than that of the wild type.","type":"Results"},{"text":"From these in vitro and in vivo observations, it is strongly suggested that at least four threonine residues, T199, T219, T234, and T237, are the potential phosphorylation targets during mitosis possibly by cyclin B/cdc2.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr199Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr219Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr234Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr237Ala","start":null,"end":null,"position":null},{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-13T17:26:11.300Z"}},{"start":233,"end":237,"reference_id":"12058066","reference_source":"pmid","reference_html":"The RNA binding activity of a ribosome biogenesis factor, nucleophosmin/B23, is modulated by phosphorylation with a cell cycle-dependent kinase and by association with its subtype. <i> Okuwaki M, Tsujimoto M, Nagata K. </i> Mol Biol Cell, 2002","date":"2023-11-30T12:53:16.985Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001218","ec_ontology":"ECO","ec_name":"in vivo protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01474r023","statement":[{"text":"Migration positions of Flag-tagged T199A and T219/234/237A are also shifted from those of interphase proteins, although the band shift of these mutant proteins in mitotic extracts was less than that of the wild type.","type":"Results"},{"text":"From these in vitro and in vivo observations, it is strongly suggested that at least four threonine residues, T199, T219, T234, and T237, are the potential phosphorylation targets during mitosis possibly by cyclin B/cdc2.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr199Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr219Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr234Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr237Ala","start":null,"end":null,"position":null},{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-13T17:26:34.783Z"}}],"released":"2018_11","uniref100":"UniRef100_P06748","date":"2018-07-19T20:00:37.000Z","acc":"P06748","name":"Nucleophosmin","length":294,"organism":"Homo sapiens","dataset":["Condensates-related proteins","Cancer-related proteins","RNA-binding proteins"],"UniParc":"UPI00001303ED","genes":[{"name":{"value":"NPM1"},"synonyms":[{"value":"NPM"}]}],"alphafold_very_low_content":0.272108843537415,"disorder_content":0.47959183673469385,"disprot_consensus":{"full":[{"start":119,"end":259,"type":"D"}],"Structural state":[{"start":119,"end":259,"type":"D"}],"Molecular function":[{"start":120,"end":243,"type":"F"}],"Disorder function":[{"start":120,"end":188,"type":"F"},{"start":197,"end":201,"type":"F"},{"start":217,"end":221,"type":"F"},{"start":233,"end":237,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03507","name":"CagA exotoxin phosphopeptide substrate mimic region","start":940,"end":978},{"id":"PF03507","name":"CagA exotoxin phosphopeptide substrate mimic region","start":979,"end":1011},{"id":"PF18971","name":"CagA protein","start":1,"end":876}],"gene3D":[{"start":15,"end":235,"id":"1.10.357.130","name":"1.10.357.130"},{"start":646,"end":824,"id":"1.20.120.1270","name":"CagA exotoxin domain III"},{"start":987,"end":1045,"id":"1.20.120.1270","name":"CagA exotoxin domain III"}]},"uniref50":"UniRef50_P55980","sequence":"MTNETIDQTRTPDQTQSQTAFDPQQFINNLQVAFIKVDNVVASFDPDQKPIVDKNDRDNRQAFDGISQLREEYSNKAIKNPTKKNQYFSDFIDKSNDLINKDNLIDVESSTKSFQKFGDQRYQIFTSWVSHQKDPSKINTRSIRNFMENIIQPPIPDDKEKAEFLKSAKQSFAGIIIGNQIRTDQKFMGVFDESLKERQEAEKNGGPTGGDWLDIFLSFIFNKKQSSDVKEAINQEPVPHVQPDIATTTTDIQGLPPEARDLLDERGNFSKFTLGDMEMLDVEGVADIDPNYKFNQLLIHNNALSSVLMGSHNGIEPEKVSLLYAGNGGFGDKHDWNATVGYKDQQGNNVATLINVHMKNGSGLVIAGGEKGINNPSFYLYKEDQLTGSQRALSQEEIRNKVDFMEFLAQNNTKLDNLSEKEKEKFQNEIEDFQKDSKAYLDALGNDRIAFVSKKDTKHSALITEFNNGDLSYTLKDYGKKADKALDREKNVTLQGSLKHDGVMFVDYSNFKYTNASKNPNKGVGATNGVSHLEAGFNKVAVFNLPDLNNLAITSFVRRNLENKLTAKGLSLQEANKLIKDFLSSNKELAGKALNFNKAVAEAKSTGNYDEVKKAQKDLEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANSQKDEIFALINKEANRDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLGINPEWISKVENLNAALNEFKNGKNKDFSKVTQAKSDLENSVKDVIINQKVTDKVDNLNQAVSVAKAMGDFSRVEQVLADLKNFSKEQLAQQAQKNEDFNTGKNSELYQSVKNSVNKTLVGNGLSGIEATALAKNFSDIKKELNEKFKNFNNNNNGLKNSTEPIYAKVNKKKTGQVASPEEPIYTQVAKKVNAKIDRLNQIASGLGGVGQAAGFPLKRHDKVDDLSKVGLSASPEPIYATIDDLGGPFPLKRHDKVDDLSKVGRSRNQELAQKIDNLNQAVSEAKAGFFGNLEQTIDKLKDSTKKNVMNLYVESAKKVPASLSAKLDNYAINSHTRINSNIQNGAINEKATGMLTQKNPEWLKLVNDKIVAHNVGSVSLSEYDKIGFNQKNMKDYSDSFKFSTKLNNAVKDIKSGFTHFLANAFSTGYYCLARENAEHGIKNVNTKGGFQKS","taxonomy":["Bacteria","Proteobacteria","Epsilonproteobacteria","Campylobacterales","Helicobacteraceae","Helicobacter"],"uniref90":"UniRef90_P55980","disprot_id":"DP01475","ncbi_taxon_id":85962,"regions_counter":19,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1186,"region_id":"DP01475r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Tertiary structure-function analysis reveals the pathogenic signaling potentiation mechanism of Helicobacter pylori oncogenic effector CagA. <i> Hayashi T, Senda M, Morohashi H, Higashi H, Horio M, Kashiba Y, Nagase L, Sasaya D, Shimizu T, Venugopalan N, Kumeta H, Noda NN, Inagaki F, Senda T, Hatakeyama M. </i> Cell Host Microbe, 2012","statement":[{"text":"The 1 H-NMR spectrum showed weak dispersion and crowded peaks of amide proton chemical shifts around the 8-ppm region. The results of the NMR study indicated that the CagA C-terminal fragment (residues 877-1186) is virtually free from a high-order structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":877,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22817985","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1001,"region_id":"DP01475r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Conformational analysis of isolated domains of Helicobacter pylori CagA. <i> Woon AP, Tohidpour A, Alonso H, Saijo-Hamano Y, Kwok T, Roujeinikova A. </i> PLoS One, 2013","statement":[{"text":"Far-UV CD spectrum of CagA-R showed a single sharp minimum at around 203 nm and a relatively low ellipticity above 210 nm, indicative of poorly structured conformations with low content of secondary structure, a feature that is often attributed to intrinsically disordered proteins of premolten globule (PMG) type.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":893,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24223932","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1001,"region_id":"DP01475r004","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Conformational analysis of isolated domains of Helicobacter pylori CagA. <i> Woon AP, Tohidpour A, Alonso H, Saijo-Hamano Y, Kwok T, Roujeinikova A. </i> PLoS One, 2013","statement":[{"text":"CagA-R was fully degraded to small peptides within 30 min of digestion, indicating that all the potential trypsin cleavage sites are exposed and, therefore, CagA-R is either fully unfolded or intrinsically disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":893,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24223932","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1001,"region_id":"DP01475r005","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Conformational analysis of isolated domains of Helicobacter pylori CagA. <i> Woon AP, Tohidpour A, Alonso H, Saijo-Hamano Y, Kwok T, Roujeinikova A. </i> PLoS One, 2013","statement":[{"text":"Our gel filtration studies suggested that CagA-R is a PMG type intrinsically disordered protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":893,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"chromatography evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24223932","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1001,"region_id":"DP01475r006","released":"2022_03","ec_id":"ECO:0006317","reference_html":"Conformational analysis of isolated domains of Helicobacter pylori CagA. <i> Woon AP, Tohidpour A, Alonso H, Saijo-Hamano Y, Kwok T, Roujeinikova A. </i> PLoS One, 2013","statement":[{"text":"The forward and reverse melting curves for CagA-R were not sigmoidal, as for typical folded proteins, but progressive,\nindicating no obvious structural cooperativity of unfolding. The CD spectra of CagA-R prior to heating and after cooling back to 22°C were very similar, indicating that the thermal unfolding is reversible.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":893,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24223932","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":23,"region_id":"DP01475r007","start":1,"term_id":"IDPO:0000002","statement":[{"text":"The electron density map obtained from the CagA(1-876) crystal resolved the N terminus end region of CagA (residues 24-221), which corresponded to the smaller fragment of the trypsin-digested CagA N-terminal region (Figure 1A).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22817985","version":2,"reference_html":"Tertiary structure-function analysis reveals the pathogenic signaling potentiation mechanism of Helicobacter pylori oncogenic effector CagA. <i> Hayashi T, Senda M, Morohashi H, Higashi H, Horio M, Kashiba Y, Nagase L, Sasaya D, Shimizu T, Venugopalan N, Kumeta H, Noda NN, Inagaki F, Senda T, Hatakeyama M. </i> Cell Host Microbe, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4DVY"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":302,"region_id":"DP01475r008","start":222,"term_id":"IDPO:0000002","statement":[{"text":"Whereas the overall structure was defined, N-terminal CagA was characterized by the existence of short disordered stretches such as residues 222-302, 479-488, and 510-536, of which electron densities were not observed in any crystal form (Figure 4 and Table S2).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22817985","version":2,"reference_html":"Tertiary structure-function analysis reveals the pathogenic signaling potentiation mechanism of Helicobacter pylori oncogenic effector CagA. <i> Hayashi T, Senda M, Morohashi H, Higashi H, Horio M, Kashiba Y, Nagase L, Sasaya D, Shimizu T, Venugopalan N, Kumeta H, Noda NN, Inagaki F, Senda T, Hatakeyama M. </i> Cell Host Microbe, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4DVY"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":488,"region_id":"DP01475r009","start":479,"term_id":"IDPO:0000002","statement":[{"text":"Whereas the overall structure was defined, N-terminal CagA was characterized by the existence of short disordered stretches such as residues 222-302, 479-488, and 510-536, of which electron densities were not observed in any crystal form (Figure 4 and Table S2).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22817985","version":2,"reference_html":"Tertiary structure-function analysis reveals the pathogenic signaling potentiation mechanism of Helicobacter pylori oncogenic effector CagA. <i> Hayashi T, Senda M, Morohashi H, Higashi H, Horio M, Kashiba Y, Nagase L, Sasaya D, Shimizu T, Venugopalan N, Kumeta H, Noda NN, Inagaki F, Senda T, Hatakeyama M. </i> Cell Host Microbe, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4DVY"},{"db":"PDB","id":"4DVZ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":536,"region_id":"DP01475r010","start":510,"term_id":"IDPO:0000002","statement":[{"text":"Whereas the overall structure was defined, N-terminal CagA was characterized by the existence of short disordered stretches such as residues 222-302, 479-488, and 510-536, of which electron densities were not observed in any crystal form (Figure 4 and Table S2).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22817985","version":2,"reference_html":"Tertiary structure-function analysis reveals the pathogenic signaling potentiation mechanism of Helicobacter pylori oncogenic effector CagA. <i> Hayashi T, Senda M, Morohashi H, Higashi H, Horio M, Kashiba Y, Nagase L, Sasaya D, Shimizu T, Venugopalan N, Kumeta H, Noda NN, Inagaki F, Senda T, Hatakeyama M. </i> Cell Host Microbe, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4DVY"},{"db":"PDB","id":"4DVZ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":876,"region_id":"DP01475r011","start":824,"term_id":"IDPO:0000002","statement":[{"text":"On the other hand, no electron densities were observed for residues 825-876, suggesting that these residues were structurally disordered. We thus concluded that the entire CagA protein comprises a structured N-terminal region (residues 1-829) (Table S2) and an intrinsically disordered C-terminal region (830-1186).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22817985","version":2,"reference_html":"Tertiary structure-function analysis reveals the pathogenic signaling potentiation mechanism of Helicobacter pylori oncogenic effector CagA. <i> Hayashi T, Senda M, Morohashi H, Higashi H, Horio M, Kashiba Y, Nagase L, Sasaya D, Shimizu T, Venugopalan N, Kumeta H, Noda NN, Inagaki F, Senda T, Hatakeyama M. </i> Cell Host Microbe, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4DVY"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":302,"region_id":"DP01475r012","start":222,"term_id":"IDPO:0000033","statement":[{"text":"Domain I, which comprises the CagA N-terminal end, is linked to Domain II by a disordered region with about 80 amino acids.","type":"Discussion"},{"text":"Flexible linker connecting Domain I and Domain II of CagA.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22817985","version":3,"reference_html":"Tertiary structure-function analysis reveals the pathogenic signaling potentiation mechanism of Helicobacter pylori oncogenic effector CagA. <i> Hayashi T, Senda M, Morohashi H, Higashi H, Horio M, Kashiba Y, Nagase L, Sasaya D, Shimizu T, Venugopalan N, Kumeta H, Noda NN, Inagaki F, Senda T, Hatakeyama M. </i> Cell Host Microbe, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4DVY"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":536,"region_id":"DP01475r013","start":510,"term_id":"IDPO:0000033","statement":[{"text":"Interestingly, the structured N-terminal CagA still contains short disordered regions such as residues 222-302, 479-488, and 510-536. Since these disordered regions are common in all crystal forms, their presence may be a unique structural property of N-terminal CagA. Such disordered regions would not only act as flexible linkers between structured portions/domains but also serve as sites for molecular interaction, modification and so on.","type":"Discussion"},{"text":"Flexible linker connecting Domain II and Domain III of CagA.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22817985","version":3,"reference_html":"Tertiary structure-function analysis reveals the pathogenic signaling potentiation mechanism of Helicobacter pylori oncogenic effector CagA. <i> Hayashi T, Senda M, Morohashi H, Higashi H, Horio M, Kashiba Y, Nagase L, Sasaya D, Shimizu T, Venugopalan N, Kumeta H, Noda NN, Inagaki F, Senda T, Hatakeyama M. </i> Cell Host Microbe, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4DVY"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1186,"region_id":"DP01475r014","start":877,"term_id":"GO:0005515","statement":[{"text":"CagA(877-1186) produced in COS-7 cells or in E. coli was mixed with FLAG-tagged PAR1b expressed in COS-7 cells and the complex formation was determined by co-immunoprecipitation.","type":"Figure"}],"curator_id":"esalladini","released":"2022_03","ec_name":"co-immunoprecipitation evidence used in manual assertion","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"22817985","version":4,"reference_html":"Tertiary structure-function analysis reveals the pathogenic signaling potentiation mechanism of Helicobacter pylori oncogenic effector CagA. <i> Hayashi T, Senda M, Morohashi H, Higashi H, Horio M, Kashiba Y, Nagase L, Sasaya D, Shimizu T, Venugopalan N, Kumeta H, Noda NN, Inagaki F, Senda T, Hatakeyama M. </i> Cell Host Microbe, 2012","date":"2022-03-09T08:35:20.572Z","reference_source":"pmid","ec_id":"ECO:0006030","term_name":"protein binding","curator_orcid":"0000-0002-5152-5953","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"A9CP04","operator":"and","partner_start":null,"partner_end":null}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1186,"region_id":"DP01475r015","start":877,"term_id":"GO:0005515","statement":[{"text":"Using surface plasmon resonance (SPR) spectroscopy, we directly measured binding affinity of recombinant CagA to PAR1 (Figure 2A). Full-length CagA bound to PAR1b (residues 39-364) with a KD value of 3.9 ± 0.64 nM. In contrast, C-terminal CagA(877-1186) bound to PAR1b (KD = 33.0 ± 9.3 nM) with a strength that was one order of magnitude less than that of full-length CagA. Since N-terminal CagA(1-876) did not directly bind to PAR1, the result suggested the presence of a functional interplay between the N-terminal region and C-terminal region that strengthens binding of C-terminal CagA to PAR1.","type":"Figure"}],"curator_id":"esalladini","released":"2022_03","ec_name":"surface plasmon resonance evidence used in manual assertion","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"22817985","version":4,"reference_html":"Tertiary structure-function analysis reveals the pathogenic signaling potentiation mechanism of Helicobacter pylori oncogenic effector CagA. <i> Hayashi T, Senda M, Morohashi H, Higashi H, Horio M, Kashiba Y, Nagase L, Sasaya D, Shimizu T, Venugopalan N, Kumeta H, Noda NN, Inagaki F, Senda T, Hatakeyama M. </i> Cell Host Microbe, 2012","date":"2022-03-09T08:35:31.411Z","reference_source":"pmid","ec_id":"ECO:0001269","term_name":"protein binding","curator_orcid":"0000-0002-5152-5953","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"A9CP04","operator":"and","partner_start":null,"partner_end":null}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1038,"region_id":"DP01475r016","start":998,"term_id":"GO:0005515","statement":[{"text":"In addition, results of a binding-competition experiment using a series of peptides derived from C-terminal CagA and a co-immunoprecipitation experiment using internal deletion mutants of CagA(877-1186) indicated that residues 998-1038 are responsible for interaction with N-terminal CagA (Figures 2D–2F).","type":"Results"}],"curator_id":"esalladini","released":"2022_03","ec_name":"competitive binding evidence used in manual assertion","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"22817985","version":4,"reference_html":"Tertiary structure-function analysis reveals the pathogenic signaling potentiation mechanism of Helicobacter pylori oncogenic effector CagA. <i> Hayashi T, Senda M, Morohashi H, Higashi H, Horio M, Kashiba Y, Nagase L, Sasaya D, Shimizu T, Venugopalan N, Kumeta H, Noda NN, Inagaki F, Senda T, Hatakeyama M. </i> Cell Host Microbe, 2012","date":"2022-03-09T08:35:14.613Z","reference_source":"pmid","ec_id":"ECO:0006309","term_name":"protein binding","curator_orcid":"0000-0002-5152-5953","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"A9CP04","operator":"and","partner_start":null,"partner_end":null}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1038,"region_id":"DP01475r017","start":998,"term_id":"GO:0005515","statement":[{"text":"Whereas CBS contained neither an EPIYA motif nor CM sequence, a CagA mutant lacking CBS (CagAΔ998-1038) had substantially reduced SHP2-binding activity and decreased hummingbird-inducing activity in AGS cells (Figure 2H), providing additional evidence for the importance of intramolecular CagA interaction in enhancing the pathophysiological activity of C-terminal CagA.","type":"Results"},{"text":"Authors defined region 998-1038 as C-terminal binding sequence (CBS).","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"co-immunoprecipitation evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"22817985","version":3,"reference_html":"Tertiary structure-function analysis reveals the pathogenic signaling potentiation mechanism of Helicobacter pylori oncogenic effector CagA. <i> Hayashi T, Senda M, Morohashi H, Higashi H, Horio M, Kashiba Y, Nagase L, Sasaya D, Shimizu T, Venugopalan N, Kumeta H, Noda NN, Inagaki F, Senda T, Hatakeyama M. </i> Cell Host Microbe, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006030","term_name":"protein binding","curator_orcid":"0000-0002-0341-4888","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1186,"region_id":"DP01475r018","start":877,"term_id":"GO:0060090","statement":[{"text":"Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.","type":"Abstract"},{"text":"CagA(877-1186) produced in COS-7 cells or in E. coli was mixed with FLAG-tagged PAR1b expressed in COS-7 cells and the complex formation was determined by co-immunoprecipitation.","type":"Figure"},{"text":"Whereas CBS contained neither an EPIYA motif nor CM sequence, a CagA mutant lacking CBS (CagAΔ998-1038) had substantially reduced SHP2-binding activity and decreased hummingbird-inducing activity in AGS cells (Figure 2H), providing additional evidence for the importance of intramolecular CagA interaction in enhancing the pathophysiological activity of C-terminal CagA.","type":"Results"},{"text":"The C-terminal CagA(877-1186) contains the EPIYA segment and CM sequence, which respectively act as binding sites for SHP2 and PAR1 (Higashi et al., 2002b; Saadat et al., 2007). The scaffold/hub function of C-terminal CagA is responsible for the morphogenetic activity of CagA known as the hummingbird phenotype (Bagnoli et al., 2005; Higashi et al., 2005).","type":"Results"}],"curator_id":"esalladini","released":"2022_03","ec_name":"co-immunoprecipitation evidence used in manual assertion","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"22817985","version":4,"reference_html":"Tertiary structure-function analysis reveals the pathogenic signaling potentiation mechanism of Helicobacter pylori oncogenic effector CagA. <i> Hayashi T, Senda M, Morohashi H, Higashi H, Horio M, Kashiba Y, Nagase L, Sasaya D, Shimizu T, Venugopalan N, Kumeta H, Noda NN, Inagaki F, Senda T, Hatakeyama M. </i> Cell Host Microbe, 2012","date":"2022-03-09T08:35:04.949Z","reference_source":"pmid","ec_id":"ECO:0006030","term_name":"molecular adaptor activity","curator_orcid":"0000-0002-5152-5953","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"A9CP04","operator":"and","partner_start":null,"partner_end":null}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1186,"region_id":"DP01475r019","start":877,"term_id":"IDPO:0000002","statement":[{"text":"By circular dichroism (CD) spectrum analysis of E. coli-purified recombinant proteins, the N-terminal CagA(1-876) fragment gave particular CD peaks at 208 nm and 222 nm derived from α helices, and the helix content was estimated from CD spectra data to be approximately 58%, whereas the C-terminal CagA(877-1186) was virtually free of a secondary structure (Figure 6H).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22817985","version":2,"reference_html":"Tertiary structure-function analysis reveals the pathogenic signaling potentiation mechanism of Helicobacter pylori oncogenic effector CagA. <i> Hayashi T, Senda M, Morohashi H, Higashi H, Horio M, Kashiba Y, Nagase L, Sasaya D, Shimizu T, Venugopalan N, Kumeta H, Noda NN, Inagaki F, Senda T, Hatakeyama M. </i> Cell Host Microbe, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P55980","date":"2018-07-19T20:52:07.000Z","acc":"P55980","name":"Cytotoxicity-associated immunodominant antigen","length":1186,"organism":"Helicobacter pylori (strain ATCC 700392 / 26695)","dataset":[],"UniParc":"UPI0000126DD8","genes":[{"name":{"value":"cagA"},"synonyms":[{"value":"cag26"},{"value":"cai"}],"olnNames":[{"value":"HP_0547"}]}],"alphafold_very_low_content":0.34991568296795955,"disorder_content":0.42495784148397975,"disprot_consensus":{"full":[{"start":1,"end":23,"type":"D"},{"start":222,"end":302,"type":"D"},{"start":479,"end":488,"type":"D"},{"start":510,"end":536,"type":"D"},{"start":824,"end":1186,"type":"D"}],"Structural state":[{"start":1,"end":23,"type":"D"},{"start":222,"end":302,"type":"D"},{"start":479,"end":488,"type":"D"},{"start":510,"end":536,"type":"D"},{"start":824,"end":1186,"type":"D"}],"Disorder function":[{"start":222,"end":302,"type":"F"},{"start":510,"end":536,"type":"F"}],"Molecular function":[{"start":877,"end":1186,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00028","name":"Cadherin domain","start":56,"end":148},{"id":"PF00028","name":"Cadherin domain","start":163,"end":260},{"id":"PF00028","name":"Cadherin domain","start":274,"end":354},{"id":"PF01049","name":"Cadherin, Y-type LIR-motif","start":706,"end":761}],"gene3D":[{"start":676,"end":767,"id":"4.10.900.10","name":"TCF3-CBD (Catenin binding domain)"},{"start":381,"end":485,"id":"2.60.40.60","name":"Cadherins"},{"start":262,"end":379,"id":"2.60.40.60","name":"Cadherins"},{"start":41,"end":155,"id":"2.60.40.60","name":"Cadherins"},{"start":156,"end":261,"id":"2.60.40.60","name":"Cadherins"}]},"uniref50":"UniRef50_Q02413","sequence":"MDWSFFRVVAMLFIFLVVVEVNSEFRIQVRDYNTKNGTIKWHSIRRQKREWIKFAAACREGEDNSKRNPIAKIHSDCAANQQVTYRISGVGIDQPPYGIFVINQKTGEINITSIVDREVTPFFIIYCRALNSMGQDLERPLELRVRVLDINDNPPVFSMATFAGQIEENSNANTLVMILNATDADEPNNLNSKIAFKIIRQEPSDSPMFIINRNTGEIRTMNNFLDREQYGQYALAVRGSDRDGGADGMSAECECNIKILDVNDNIPYMEQSSYTIEIQENTLNSNLLEIRVIDLDEEFSANWMAVIFFISGNEGNWFEIEMNERTNVGILKVVKPLDYEAMQSLQLSIGVRNKAEFHHSIMSQYKLKASAISVTVLNVIEGPVFRPGSKTYVVTGNMGSNDKVGDFVATDLDTGRPSTTVRYVMGNNPADLLAVDSRTGKLTLKNKVTKEQYNMLGGKYQGTILSIDDNLQRTCTGTININIQSFGNDDRTNTEPNTKITTNTGRQESTSSTNYDTSTTSTDSSQVYSSEPGNGAKDLLSDNVHFGPAGIGLLIMGFLVLGLVPFLMICCDCGGAPRSAAGFEPVPECSDGAIHSWAVEGPQPEPRDITTVIPQIPPDNANIIECIDNSGVYTNEYGGREMQDLGGGERMTGFELTEGVKTSGMPEICQEYSGTLRRNSMRECREGGLNMNFMESYFCQKAYAYADEDEGRPSNDCLLIYDIEGVGSPAGSVGCCSFIGEDLDDSFLDTLGPKFKKLADISLGKESYPDLDPSWPPQSTEPVCLPQETEPVVSGHPPISPHFGTTTVISESTYPSGPGVLHPKPILDPLGYGNVTVTESYTTSDTLKPSVHVHDNRPASNVVVTERVVGPISGADLHGMLEMPDLRDGSNVIVTERVIAPSSSLPTSLTIHHPRESSNVVVTERVIQPTSGMIGSLSMHPELANAHNVIVTERVVSGAGVTGISGTTGISGGIGSSGLVGTSMGAGSGALSGAGISGGGIGLSSLGGTASIGHMRSSSDHHFNQTIGSASPSTARSRITKYSTVQYSK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q02413","disprot_id":"DP01476","ncbi_taxon_id":9606,"regions_counter":6,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1049,"region_id":"DP01476r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The desmoglein-specific cytoplasmic region is intrinsically disordered in solution and interacts with multiple desmosomal protein partners. <i> Kami K, Chidgey M, Dafforn T, Overduin M. </i> J Mol Biol, 2009","statement":[{"text":"Here, we reveal that a 276-residue DSCR construct of human desmoglein 1 is intrinsically disordered and forms an interaction hub for desmosomal proteins. In solution, it contains 6.5% helical and 10.3% beta-strand structure based on circular dichroism spectroscopy. A single monomeric state with a predominantly unfolded structure is found by size-exclusion chromatography and analytical ultracentrifugation. Thermal stability assays and nuclear magnetic resonance spectroscopy reveal a nonglobular structure under a range of solution conditions.","type":"Abstract"},{"text":"Results from nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy demonstrate that the DSCR of human Dsg1 is intrinsically disordered in solution, having little intrinsically stable structure but with inducible conformations that can be stabilized by co-solvents and micelles. Analysis of its hydrodynamic behavior demonstrates that the protein exists as a monomer and in an unfolded conformation rather than a globular form.","type":"Introduction"},{"text":"The spectrum exhibited only a single negative minimum at 198 nm, which suggests a disordered state (Fig. 5a). The estimated α-helical, β-strand, and turn content of the DSCR at 20 °C was 4.6%, 8.1%, and 7.6%, respectively, with the remaining 79.7% being assigned as disordered.","type":"Results"},{"text":"The far-UV CD spectra of the DSCR showed the typical pattern of disordered polypeptides, with little α-helical or β-strand structure.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":774,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19136012","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1049,"region_id":"DP01476r002","released":"2022_03","ec_id":"ECO:0007680","reference_html":"The desmoglein-specific cytoplasmic region is intrinsically disordered in solution and interacts with multiple desmosomal protein partners. <i> Kami K, Chidgey M, Dafforn T, Overduin M. </i> J Mol Biol, 2009","statement":[{"text":"Here, we reveal that a 276-residue DSCR construct of human desmoglein 1 is intrinsically disordered and forms an interaction hub for desmosomal proteins. In solution, it contains 6.5% helical and 10.3% beta-strand structure based on circular dichroism spectroscopy. A single monomeric state with a predominantly unfolded structure is found by size-exclusion chromatography and analytical ultracentrifugation. Thermal stability assays and nuclear magnetic resonance spectroscopy reveal a nonglobular structure under a range of solution conditions.","type":"Abstract"},{"text":"Based on its gel filtration elution profile, the Stokes radius (Rs) of DSCR was estimated to be 41.8 Å. This compares more favorably with the theoretical value of a fully unfolded protein of 28.6 kDa (47.6 Å) than that of a globular monomer (24.6 Å). Together, these results indicate that the DSCR has the dimensions of a largely unfolded monomer.","type":"Results"},{"text":"The DSCR protein eluted as a single peak by gel filtration with an apparent molecular mass of 121 kDa based on calibration against known molecular mass standards (Fig. 3a).","type":"Results"},{"text":"The hydrodynamic properties of the DSCR inferred by gel filtration and AUC show that the protein adopts an unfolded monomeric conformation.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":774,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"chromatography evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19136012","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1049,"region_id":"DP01476r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The desmoglein-specific cytoplasmic region is intrinsically disordered in solution and interacts with multiple desmosomal protein partners. <i> Kami K, Chidgey M, Dafforn T, Overduin M. </i> J Mol Biol, 2009","statement":[{"text":"Here, we reveal that a 276-residue DSCR construct of human desmoglein 1 is intrinsically disordered and forms an interaction hub for desmosomal proteins. In solution, it contains 6.5% helical and 10.3% beta-strand structure based on circular dichroism spectroscopy. A single monomeric state with a predominantly unfolded structure is found by size-exclusion chromatography and analytical ultracentrifugation. Thermal stability assays and nuclear magnetic resonance spectroscopy reveal a nonglobular structure under a range of solution conditions.","type":"Abstract"},{"text":"Results from nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy demonstrate that the DSCR of human Dsg1 is intrinsically disordered in solution, having little intrinsically stable structure but with inducible conformations that can be stabilized by co-solvents and micelles. Analysis of its hydrodynamic behavior demonstrates that the protein exists as a monomer and in an unfolded conformation rather than a globular form.","type":"Introduction"},{"text":"In contrast, the NMR signals of the DSCR were not well dispersed, with narrow, intense, and overlapped methyl proton resonances at random-coil values of 0.8 to 1.0 ppm. The backbone amide protons are almost entirely clustered between 7.9 and 8.5 ppm, with only two downfield peaks discernable at 8.70 and 9.21 ppm. The DSCR's sole Trp appeared disordered, exhibiting random-coil NɛH chemical shifts of 10.05 and 10.24 ppm, presumably due to the apparent cis–trans isomerization of its neighboring proline residues (Fig. 4). Together, this indicates a disordered region lacking in stable tertiary structure and is consistent with the largely unfolded conformation of the DSCR based on its hydrodynamic properties.","type":"Results"},{"text":"The limited dispersion of chemical shifts in the NMR spectrum confirms the absence of stable, three-dimensional structure.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":774,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19136012","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1049,"term_name":"protein binding","reference_html":"The desmoglein-specific cytoplasmic region is intrinsically disordered in solution and interacts with multiple desmosomal protein partners. <i> Kami K, Chidgey M, Dafforn T, Overduin M. </i> J Mol Biol, 2009","start":774,"region_id":"DP01476r005","term_id":"GO:0005515","version":4,"curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","statement":[{"text":"Thus, the DSCR is an intrinsically disordered functional domain with an inducible structure that, along with the membrane proximal region, forms a flexible scaffold for cytoplasmic assembly at the desmosome.","type":"Abstract"},{"text":"We conclude that the DSCR forms an intrinsically disordered state in solution with inducible structure that, together with the MPR, forms a hub for multiple protein interactions during desmosomal cell adhesion.","type":"Introduction"},{"text":"These data suggest that the entire DSCR is required for its interaction with its desmosomal protein partners and forms a single functional unit that can be regulated by caspase cleavage.","type":"Results"},{"text":"Coomassie-stained GST-fused desmosomal proteins used in pull-down assays. GST-PG, GST fused to full-length PG; GST-DP, GST fused to the plakin domain of DP (residues 10–1097); GST-PKP1, GST fused to residues 6–726 of PKP1; GST-Dsc1, GST fused to the cytoplasmic domain of Dsc1 (residues 717–894).","type":"Figure"},{"text":"Overall, the pull-down assays suggest that the entire Dsg1 cytoplasmic domain (i.e., MPR + DSCR) acts as a flexible scaffold for cytoplasmic complex assembly at the desmosome with a network of strong and weak protein–protein interactions.","type":"Results"},{"text":"The intrinsic plasticity of such intrinsically disordered regions is often used to mediate interactions with multiple biological targets. Indeed, this would appear to be the case for the DSCR as pull-down assays show that it is able to interact with multiple partners including PG, the plakin domain of DP, PKP1, and the cytoplasmic domain of Dsc1.","type":"Discussion"},{"text":"We suggest that strong interactions between some cytoplasmic desmosomal proteins (e.g., MPR and PG/PKP1) are supported by a network of weaker interactions between others (MPR and DP/Dsc1; DSCR and PG/PKP1/DP/Dsc1). This web of interactions places the desmoglein cytoplasmic domain at the heart of the desmosomal complex, thus enabling it to play important role in desmosome assembly and intercellular adhesion.","type":"Discussion"}],"curator_orcid":"0000-0002-5152-5953","date":"2022-03-09T08:36:17.393Z","reference_source":"pmid","ec_id":"ECO:0006077","reference_id":"19136012","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q02413","operator":"and","partner_start":null,"partner_end":null}]}],"released":"2018_11","uniref100":"UniRef100_Q02413","date":"2018-07-19T20:55:03.000Z","acc":"Q02413","name":"Desmoglein-1","length":1049,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000004CAAA","genes":[{"name":{"value":"DSG1"},"synonyms":[{"value":"CDHF4"}]}],"alphafold_very_low_content":0.48236415633937085,"disorder_content":0.2631077216396568,"disprot_consensus":{"full":[{"start":774,"end":1049,"type":"D"}],"Structural state":[{"start":774,"end":1049,"type":"D"}],"Molecular function":[{"start":774,"end":1049,"type":"F"}]}},{"features":{"pfam":[{"id":"PF12894","name":"Anaphase-promoting complex subunit 4 WD40 domain","start":27,"end":117},{"id":"PF12896","name":"Anaphase-promoting complex, cyclosome, subunit 4","start":233,"end":431},{"id":"PF23405","name":"APC4, WD40 domain C-terminal half","start":575,"end":745}],"gene3D":[{"start":12,"end":127,"id":"2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"}]},"uniref50":"UniRef50_Q9UJX5","sequence":"MLRFPTCFPSFRVVGEKQLPQEIIFLVWSPKRDLIALANTAGEVLLHRLASFHRVWSFPPNENTGKEVTCLAWRPDGKLLAFALADTKKIVLCDVEKPESLHSFSVEAPVSCMHWMEVTVESSVLTSFYNAEDESNLLLPKLPTLPKNYSNTSKIFSEENSDEIIKLLGDVRLNILVLGGSSGFIELYAYGMFKIARVTGIAGTCLALCLSSDLKSLSVVTEVSTNGASEVSYFQLETNLLYSFLPEVTRMARKFTHISALLQYINLSLTCMCEAWEEILMQMDSRLTKFVQEKNTTTSVQDEFMHLLLWGKASAELQTLLMNQLTVKGLKKLGQSIESSYSSIQKLVISHLQSGSESLLYHLSELKGMASWKQKYEPLGLDAAGIEEAITAVGSFILKANELLQVIDSSMKNFKAFFRWLYVAMLRMTEDHVLPELNKMTQKDITFVAEFLTEHFNEAPDLYNRKGKYFNVERVGQYLKDEDDDLVSPPNTEGNQWYDFLQNSSHLKESPLLFPYYPRKSLHFVKRRMENIIDQCLQKPADVIGKSMNQAICIPLYRDTRSEDSTRRLFKFPFLWNNKTSNLHYLLFTILEDSLYKMCILRRHTDISQSVSNGLIAIKFGSFTYATTEKVRRSIYSCLDAQFYDDETVTVVLKDTVGREGRDRLLVQLPLSLVYNSEDSAEYQFTGTYSTRLDEQCSAIPTRTMHFEKHWRLLESMKAQYVAGNGFRKVSCVLSSNLRHVRVFEMDIDDEWELDESSDEEEEASNKPVKIKEEVLSESEAENQQAGAAALAPEIVIKVEKLDPELDS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UJX5","disprot_id":"DP01478","ncbi_taxon_id":9606,"regions_counter":7,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":317,"region_id":"DP01478r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Atomic-Resolution Structures of the APC/C Subunits Apc4 and the Apc5 N-Terminal Domain. <i> Cronin NB, Yang J, Zhang Z, Kulkarni K, Chang L, Yamano H, Barford D. </i> J Mol Biol, 2015","statement":[{"text":"Table 4 of the paper","type":"Table"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":304,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5BPW"}],"reference_id":"26343760","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":444,"region_id":"DP01478r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Atomic-Resolution Structures of the APC/C Subunits Apc4 and the Apc5 N-Terminal Domain. <i> Cronin NB, Yang J, Zhang Z, Kulkarni K, Chang L, Yamano H, Barford D. </i> J Mol Biol, 2015","statement":[{"text":"Table 4 of the paper","type":"Table"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":431,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5BPW"}],"reference_id":"26343760","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":472,"region_id":"DP01478r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Atomic-Resolution Structures of the APC/C Subunits Apc4 and the Apc5 N-Terminal Domain. <i> Cronin NB, Yang J, Zhang Z, Kulkarni K, Chang L, Yamano H, Barford D. </i> J Mol Biol, 2015","statement":[{"text":"Table 4 of the paper","type":"Table"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":458,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5BPW"}],"reference_id":"26343760","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":469,"region_id":"DP01478r004","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The region is specified in the Extended Data Table 2","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":458,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"},{"db":"PDB","id":"5A31"},{"db":"PDB","id":"5G05"},{"db":"PDB","id":"5G04"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":808,"region_id":"DP01478r005","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The region is specified in the Extended Data Table 2","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":758,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"},{"db":"PDB","id":"5A31"},{"db":"PDB","id":"5G05"},{"db":"PDB","id":"5G04"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":521,"region_id":"DP01478r006","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Atomic-Resolution Structures of the APC/C Subunits Apc4 and the Apc5 N-Terminal Domain. <i> Cronin NB, Yang J, Zhang Z, Kulkarni K, Chang L, Yamano H, Barford D. </i> J Mol Biol, 2015","statement":[{"text":"Table 4 of the paper","type":"Table"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":480,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5BPW"}],"reference_id":"26343760","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":808,"region_id":"DP01478r007","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Atomic-Resolution Structures of the APC/C Subunits Apc4 and the Apc5 N-Terminal Domain. <i> Cronin NB, Yang J, Zhang Z, Kulkarni K, Chang L, Yamano H, Barford D. </i> J Mol Biol, 2015","statement":[{"text":"Authors said \".. C-terminal residues (758–808) of human Apc4 are disordered in both the crystal structure and the EM density map.\"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":758,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5BPW"}],"reference_id":"26343760","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9UJX5","date":"2018-07-20T01:48:05.000Z","acc":"Q9UJX5","name":"Anaphase-promoting complex subunit 4","length":808,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000071B77","genes":[{"name":{"value":"ANAPC4"},"synonyms":[{"value":"APC4"}]}],"alphafold_very_low_content":0.10891089108910891,"disorder_content":0.16831683168316833,"disprot_consensus":{"full":[{"start":304,"end":317,"type":"D"},{"start":431,"end":444,"type":"D"},{"start":458,"end":472,"type":"D"},{"start":480,"end":521,"type":"D"},{"start":758,"end":808,"type":"D"}],"Structural state":[{"start":304,"end":317,"type":"D"},{"start":431,"end":444,"type":"D"},{"start":458,"end":472,"type":"D"},{"start":480,"end":521,"type":"D"},{"start":758,"end":808,"type":"D"}]}},{"features":{"pfam":[{"id":"PF13181","name":"Tetratricopeptide repeat","start":340,"end":370},{"id":"PF13432","name":"Tetratricopeptide repeat","start":447,"end":508}],"gene3D":[{"start":35,"end":181,"id":"1.25.40.10","name":"Tetratricopeptide repeat domain"},{"start":473,"end":552,"id":"1.25.40.10","name":"Tetratricopeptide repeat domain"},{"start":264,"end":442,"id":"1.25.40.10","name":"Tetratricopeptide repeat domain"}]},"uniref50":"UniRef50_Q9UJX3","sequence":"MNVIDHVRDMAAAGLHSNVRLLSSLLLTMSNNNPELFSPPQKYQLLVYHADSLFHDKEYRNAVSKYTMALQQKKALSKTSKVRPSTGNSASTPQSQCLPSEIEVKYKMAECYTMLKQDKDAIAILDGIPSRQRTPKINMMLANLYKKAGQERPSVTSYKEVLRQCPLALDAILGLLSLSVKGAEVASMTMNVIQTVPNLDWLSVWIKAYAFVHTGDNSRAISTICSLEKKSLLRDNVDLLGSLADLYFRAGDNKNSVLKFEQAQMLDPYLIKGMDVYGYLLAREGRLEDVENLGCRLFNISDQHAEPWVVSGCHSFYSKRYSRALYLGAKAIQLNSNSVQALLLKGAALRNMGRVQEAIIHFREAIRLAPCRLDCYEGLIECYLASNSIREAMVMANNVYKTLGANAQTLTLLATVCLEDPVTQEKAKTLLDKALTQRPDYIKAVVKKAELLSREQKYEDGIALLRNALANQSDCVLHRILGDFLVAVNEYQEAMDQYSIALSLDPNDQKSLEGMQKMEKEESPTDATQEEDVDDMEGSGEEGDLEGSDSEAAQWADQEQWFGMQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UJX3","disprot_id":"DP01479","ncbi_taxon_id":9606,"regions_counter":4,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":97,"region_id":"DP01479r002","released":"2024_12","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The region is specified in the Extended Data Table 2","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":77,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-06-27T16:04:22.934Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":96,"region_id":"DP01479r003","released":"2024_12","ec_id":"ECO:0006220","reference_html":"Atomic-Resolution Structures of the APC/C Subunits Apc4 and the Apc5 N-Terminal Domain. <i> Cronin NB, Yang J, Zhang Z, Kulkarni K, Chang L, Yamano H, Barford D. </i> J Mol Biol, 2015","statement":[{"text":"See region in Table 4","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":77,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-06-27T16:08:24.981Z","reference_source":"pmid","term_name":"disorder","reference_id":"26343760","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":565,"region_id":"DP01479r004","released":"2024_12","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The region is specified in the Extended Data Table 2","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":507,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-06-27T16:05:25.818Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9UJX3","date":"2018-07-20T02:43:46.000Z","acc":"Q9UJX3","name":"Anaphase-promoting complex subunit 7","length":565,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000006D620","genes":[{"name":{"value":"ANAPC7","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:17380","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:17380"}}]},"synonyms":[{"value":"APC7"}]}],"alphafold_very_low_content":0.1285475792988314,"disorder_content":0.1415929203539823,"disprot_consensus":{"full":[{"start":77,"end":97,"type":"D"},{"start":507,"end":565,"type":"D"}],"Structural state":[{"start":77,"end":97,"type":"D"},{"start":507,"end":565,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01149","name":"Formamidopyrimidine-DNA glycosylase N-terminal domain","start":1,"end":123},{"id":"PF09292","name":"Endonuclease VIII-like 1, DNA bind","start":252,"end":290}],"gene3D":[{"start":1,"end":133,"id":"3.20.190.10","name":"MutM-like, N-terminal"},{"start":134,"end":282,"id":"1.10.8.50","name":"1.10.8.50"}]},"uniref50":"UniRef50_Q96FI4","sequence":"MPEGPELHLASQFVNEACRALVFGGCVEKSSVSRNPEVPFESSAYRISASARGKELRLILSPLPGAQPQQEPLALVFRFGMSGSFQLVPREELPRHAHLRFYTAPPGPRLALCFVDIRRFGRWDLGGKWQPGRGPCVLQEYQQFRENVLRNLADKAFDRPICEALLDQRFFNGIGNYLRAEILYRLKIPPFEKARSVLEALQQHRPSPELTLSQKIRTKLQNPDLLELCHSVPKEVVQLGGKGYGSESGEEDFAAFRAWLRCYGMPGMSSLQDRHGRTIWFQGDPGPLAPKGRKSRKKKSKATQLSPEDRVEDALPPSKAPSRTRRAKRDLPKRTATQRPEGTSLQQDPEAPTVPKKGRRKGRQAASGHCRPRKVKADIPSLEPEGTSAS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q96FI4","disprot_id":"DP01480","ncbi_taxon_id":9606,"regions_counter":2,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":389,"region_id":"DP01480r001","start":312,"ec_id":"ECO:0006210","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Small-angle X-ray scattering (SAXS) analysis confirms the flexibility and dynamic nature of NEIL1's CTD, a feature that may be critical to providing specificity for NEIL1's multiple, functional interactions.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23542007","version":3,"reference_html":"The disordered C-terminal domain of human DNA glycosylase NEIL1 contributes to its stability via intramolecular interactions. <i> Hegde ML, Tsutakawa SE, Hegde PM, Holthauzen LM, Li J, Oezguen N, Hilser VJ, Tainer JA, Mitra S. </i> J Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","cross_refs":[{"db":"SASBDB","id":"SASDBC7"},{"db":"SASBDB","id":"SASDBB7"},{"db":"SASBDB","id":"SASDBA7"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":389,"region_id":"DP01480r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The disordered C-terminal domain of human DNA glycosylase NEIL1 contributes to its stability via intramolecular interactions. <i> Hegde ML, Tsutakawa SE, Hegde PM, Holthauzen LM, Li J, Oezguen N, Hilser VJ, Tainer JA, Mitra S. </i> J Mol Biol, 2013","statement":[{"text":"The CD spectrum of NEIL1's C-terminal 78-residue peptide (amino acids 312–389; C78) reveals a prominently disordered structure with random-coil conformation.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":312,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23542007","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q96FI4","date":"2018-07-20T09:07:49.000Z","acc":"Q96FI4","name":"Endonuclease 8-like 1","length":390,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000006FEA1","genes":[{"name":{"value":"NEIL1"}}],"alphafold_very_low_content":0.2230769230769231,"disorder_content":0.2,"disprot_consensus":{"full":[{"start":312,"end":389,"type":"D"}],"Structural state":[{"start":312,"end":389,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03167","name":"Uracil DNA glycosylase superfamily","start":177,"end":328}],"gene3D":[{"start":130,"end":370,"id":"3.40.470.10","name":"Uracil-DNA glycosylase-like domain"}]},"uniref50":"UniRef50_Q5UPT2","sequence":"MSKKNVDPFSDSDSSSEPPSIFSSDNEENSDVDNSVIINDKNTKSDEADIKYMDEDESSDSESESESKKKSKKSKKSKKSKKSVTKKKNNLLVGNRIITEYILIDANNYHFKSWIECFPDCKVNLKLLLFRPEWFDFFKYVESKTYFPQLESKLSSYLEKRQRIVPYPELLFNTMNVLPPGKIKVVILGQDPYPGSCISGVPYAMGCSFSVPLNCPVPKSLANIYTNLIKFNHMRKAPKHGCLASWILQGTFMINSAFTTVLNESGVHARTWESFTADLIDYLTDNYDDLIFVAWGAHAHKLCQRVDPKKHYIITSSHPSPYSVSNTMTSMSYGPNPKKVTYPSFNSVDHFGKINEHLKSRNKKPIFWDL","taxonomy":["Viruses","Varidnaviria","Bamfordvirae","Nucleocytoviricota","Megaviricetes","Imitervirales","Mimiviridae","Mimivirus"],"uniref90":"UniRef90_Q5UPT2","disprot_id":"DP01481","ncbi_taxon_id":212035,"regions_counter":4,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":94,"region_id":"DP01481r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Crystal structure of mimivirus uracil-DNA glycosylase. <i> Kwon E, Pathak D, Chang HW, Kim DY. </i> PLoS One, 2017","statement":[{"text":"To evaluate the secondary structure of the invisible segment in the N-domain, we compared the CD spectra of mvUNG and mvUNG95-370. In the far-UV CD spectra, the deletion of residues 1–94 did not change the pattern and scale of the CD spectrum in the range between 210–250 nm, indicating that residues 1–94 have a random coil conformation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":1,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28763516","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-09-28T13:43:30.975Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":94,"region_id":"DP01481r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of mimivirus uracil-DNA glycosylase. <i> Kwon E, Pathak D, Chang HW, Kim DY. </i> PLoS One, 2017","statement":[{"text":"A solvent space that could accommodate residues 1–94 was insufficient in the crystal.","type":"Results"},{"text":"In contrast to the structured part of the N-domain and the motif-I, residues 1–94 in N-domain are not included in the crystal structure of mvUNG. They seem to be truncated before crystallization. Indeed, all reported crystal structures of UNG proteins display only a catalytic domain.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5X55"}],"reference_id":"28763516","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-29T13:44:14.682Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":94,"reference_id":"28763516","reference_source":"pmid","reference_html":"Crystal structure of mimivirus uracil-DNA glycosylase. <i> Kwon E, Pathak D, Chang HW, Kim DY. </i> PLoS One, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0004844","term_name":"uracil DNA N-glycosylase activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01481r003","statement":[{"text":"Activity assays and CD spectra implied that the unstructured segment (residues 1–94) in the N-domain also contributes to thermal stability and catalytic activity of mvUNG.","type":"Results"},{"text":"It seems to contribute to diverse cellular functions of UNGs. For example, the N-domain of hUNG is involved in the subcellular localization of isoforms [39] and the interaction with the DNA repair factor RPA [40, 41]. In the activity assay of the N-domain deletion mutants, mvUNG95-370 which residues 1–94 is deleted showed 55% activity, compared with full-length mvUNG (first and third bars in Fig 4b). Additional deletion of residues 95–121 reduced the activity to 15%, even though the deletion mutant contains the entire catalytic domain (first and fourth bars in Fig 4b). This result indicated that both invisible (residues 1–94) and visible (residues 95–130) segments of the N-domain are required for the intrinsic activity of mvUNG.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-29T13:20:49.031Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Catalysis of the cleavage of the N-C1' glycosidic bond between the damaged DNA base and the deoxyribose sugar, releasing a free base and leaving an apyrimidinic (AP) site. Enzymes with this activity recognize and remove uracil bases in DNA that result from the deamination of cytosine or the misincorporation of dUTP opposite an adenine.\" [GOC:elh, GOC:pr, PMID:9224623]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":94,"reference_id":"28763516","reference_source":"pmid","reference_html":"Crystal structure of mimivirus uracil-DNA glycosylase. <i> Kwon E, Pathak D, Chang HW, Kim DY. </i> PLoS One, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0004844","term_name":"uracil DNA N-glycosylase activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01481r004","statement":[{"text":"Activity assays and CD spectra implied that the unstructured segment (residues 1–94) in the N-domain also contributes to thermal stability and catalytic activity of mvUNG.","type":"Results"},{"text":"It seems to contribute to diverse cellular functions of UNGs. For example, the N-domain of hUNG is involved in the subcellular localization of isoforms [39] and the interaction with the DNA repair factor RPA [40, 41]. In the activity assay of the N-domain deletion mutants, mvUNG95-370 which residues 1–94 is deleted showed 55% activity, compared with full-length mvUNG (first and third bars in Fig 4b). Additional deletion of residues 95–121 reduced the activity to 15%, even though the deletion mutant contains the entire catalytic domain (first and fourth bars in Fig 4b). This result indicated that both invisible (residues 1–94) and visible (residues 95–130) segments of the N-domain are required for the intrinsic activity of mvUNG.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-29T13:20:47.312Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Catalysis of the cleavage of the N-C1' glycosidic bond between the damaged DNA base and the deoxyribose sugar, releasing a free base and leaving an apyrimidinic (AP) site. Enzymes with this activity recognize and remove uracil bases in DNA that result from the deamination of cytosine or the misincorporation of dUTP opposite an adenine.\" [GOC:elh, GOC:pr, PMID:9224623]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2018_11","uniref100":"UniRef100_Q5UPT2","date":"2018-07-20T09:21:13.000Z","acc":"Q5UPT2","name":"Probable uracil-DNA glycosylase","length":370,"organism":"Acanthamoeba polyphaga mimivirus","dataset":["Viral proteins"],"UniParc":"UPI00004653C6","genes":[{"name":{"value":"UNG"},"olnNames":[{"value":"MIMI_L249"}]}],"disorder_content":0.25405405405405407,"disprot_consensus":{"full":[{"start":1,"end":94,"type":"D"}],"Structural state":[{"start":1,"end":94,"type":"D"}],"Molecular function":[{"start":1,"end":94,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00293","name":"NUDIX domain","start":97,"end":211},{"id":"PF05026","name":"Dcp2, box A domain","start":11,"end":92}],"gene3D":[{"start":11,"end":94,"id":"1.10.10.1050","name":"Dcp2, box A domain"},{"start":95,"end":235,"id":"3.90.79.10","name":"Nucleoside Triphosphate Pyrophosphohydrolase"}]},"uniref50":"UniRef50_O13828","sequence":"MSFTNATFSQVLDDLSARFILNLPAEEQSSVERLCFQIEQAHWFYEDFIRAQNDQLPSLGLRVFSAKLFAHCPLLWKWSKVHEEAFDDFLRYKTRIPVRGAIMLDMSMQQCVLVKGWKASSGWGFPKGKIDKDESDVDCAIREVYEETGFDCSSRINPNEFIDMTIRGQNVRLYIIPGISLDTRFESRTRKEISKIEWHNLMDLPTFKKNKPQTMKNKFYMVIPFLAPLKKWIKKRNIANNTTKEKNISVDVDADASSQLLSLLKSSTAPSDLATPQPSTFPQPPVESHSSFDIKQKILHLLNEGNEPKSPIQLPPVSNLPLNPPIQSSNSRLSHDNNSFDPFAYLGLDPKNPSASFPRVVSQNNMLTNKPVLNNHFQQSMYSNLLKDQNSVQHLFAASDMPSPMELPSPSTVYHQVFYPPTSTSVSSYGLGKTPQPAYGSSSPYVNGHQTQQISSLPPFQSQTQFLARNSDNSGQSYNSEGDSNSKRLLSMLSQQDTTPSSSTLSKEANVQLANLFLTPNSLETKKFSDNSQGEEISDNLHGESCNNPNANSVHSAQLLQALLHPSATETKEETPKKTSDSLSLLTLLKSGLPTPANDLQNKSQNNERKASSQVKELEVKNYSKSTDLLKKTLRIPRNDEPLEAANQFDLLKVSPQQKSEVPPKRNELSQSKLKNRKKKENSETNKNHVDMSPGFVKILKRSPLADQKKEDTQESDFKGSDDHFLSYLQSVVSSNSNGLH","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"uniref90":"UniRef90_O13828","disprot_id":"DP01482","ncbi_taxon_id":284812,"regions_counter":4,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":741,"region_id":"DP01482r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The structural basis of Edc3- and Scd6-mediated activation of the Dcp1:Dcp2 mRNA decapping complex. <i> Fromm SA, Truffault V, Kamenz J, Braun JE, Hoffmann NA, Izaurralde E, Sprangers R. </i> EMBO J, 2012","statement":[{"text":"In addition, the C-terminal extension is predicted to be unstructured in isolation, which is confirmed by NMR spectra of Dcp2 residues 553–741 (Supplementary Figure S6A).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":553,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22085934","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-30T13:05:24.244Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":741,"term_name":"protein binding","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The structural basis of Edc3- and Scd6-mediated activation of the Dcp1:Dcp2 mRNA decapping complex. <i> Fromm SA, Truffault V, Kamenz J, Braun JE, Hoffmann NA, Izaurralde E, Sprangers R. </i> EMBO J, 2012","statement":[{"text":"Spectrum of Dcp2 residues 553-741 without (green, as in A) and with the Edc3 LSm domain (blue). The increase in chemical shift dispersion and the appearance of new resonances (e.g. red circle) indicates the formation of secondary structure upon the complex formation between the Dcp2 C-terminal tail and the NMR inactive Edc3 LSm domain.","type":"Supplementary material"}],"term_id":"GO:0005515","curator_id":"vnugnes","start":553,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"22085934","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-30T13:14:53.785Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01482r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"O94752","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:25:01.552Z"}},{"start":553,"end":741,"reference_id":"22085934","reference_source":"pmid","reference_html":"The structural basis of Edc3- and Scd6-mediated activation of the Dcp1:Dcp2 mRNA decapping complex. <i> Fromm SA, Truffault V, Kamenz J, Braun JE, Hoffmann NA, Izaurralde E, Sprangers R. </i> EMBO J, 2012","date":"2023-11-30T13:52:45.769Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01482r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":"O94752"}],"statement":[{"text":"Spectrum of Dcp2 residues 553-741 without (green, as in A) and with the Edc3 LSm domain (blue). The increase in chemical shift dispersion and the appearance of new resonances (e.g. red circle) indicates the formation of secondary structure upon the complex formation between the Dcp2 C-terminal tail and the NMR inactive Edc3 LSm domain.","type":"Supplementary material"},{"text":"In the reverse experiment, we probed the effect of the Edc3 LSm domain addition on the spectrum of the disordered 15N-labelled Dcp2 C-terminal residues. As expected, we clearly observed binding and resonances indicative of α-helical structure appeared (Supplementary Figure S6B). This shows that the leucine-rich motifs in the disordered Dcp2 C-terminus fold into an α-helical conformation when interacting with the Edc3 LSm domains, as we observed for the HLM-1 sequence.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:24:58.806Z"}},{"start":246,"end":266,"reference_id":"16341225","reference_source":"pmid","reference_html":"Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe. <i> She M, Decker CJ, Chen N, Tumati S, Parker R, Song H. </i> Nat Struct Mol Biol, 2006","date":"2023-11-30T13:50:16.485Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01482r004","statement":[{"text":"The crystal structure of spDcp2n was determined by SAD at a resolution of 2.5 Å. The final model contains two molecules (A and B) in the asymmetric unit. Several regions of the polypeptide chain are not visible in the electron density map and are assumed to be disordered, namely residues 79–81, 186–191, 209–214 and 246–266 for molecule A and residues 1–34, 55–57, 69–82, 116–122, 186–191, 209–214 and 244–266 for molecule B.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:24:29.083Z"}}],"released":"2018_11","uniref100":"UniRef100_O13828","date":"2018-07-20T12:21:25.000Z","acc":"O13828","name":"mRNA decapping complex subunit 2","length":741,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","dataset":["Condensates-related proteins","RNA-binding proteins"],"UniParc":"UPI000006B3D3","genes":[{"name":{"value":"dcp2"},"orfNames":[{"value":"SPAC19A8.12"}]}],"alphafold_very_low_content":0.6261808367071525,"disorder_content":0.2834008097165992,"disprot_consensus":{"full":[{"start":246,"end":266,"type":"D"},{"start":553,"end":741,"type":"T"}],"Structural state":[{"start":246,"end":266,"type":"D"},{"start":553,"end":741,"type":"D"}],"Molecular function":[{"start":553,"end":741,"type":"F"}],"Structural transition":[{"start":553,"end":741,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00757","name":"Furin-like cysteine rich region","start":190,"end":343},{"id":"PF01030","name":"Receptor L domain","start":52,"end":172},{"id":"PF01030","name":"Receptor L domain","start":366,"end":484},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":722,"end":975},{"id":"PF14843","name":"Growth factor receptor domain IV","start":511,"end":642},{"id":"PF21314","name":"Epidermal growth factor receptor transmembrane-juxtamembrane segment","start":654,"end":688}],"gene3D":[{"start":23,"end":214,"id":"3.80.20.20","name":"Receptor L-domain"},{"start":339,"end":533,"id":"3.80.20.20","name":"Receptor L-domain"},{"start":215,"end":338,"id":"2.10.220.10","name":"Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2"},{"start":646,"end":684,"id":"1.20.5.100","name":"Cytochrome c1, transmembrane anchor, C-terminal"},{"start":725,"end":799,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":801,"end":997,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"},{"start":685,"end":724,"id":"4.10.1140.10","name":"membrane-bound form of the juxtamembrane domain of the epidermal growth factor receptor like domain"},{"start":588,"end":645,"id":"2.10.220.10","name":"Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2"},{"start":534,"end":586,"id":"2.10.220.10","name":"Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2"}]},"uniref50":"UniRef50_P04626","sequence":"MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSLPDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTVPWDQLFRNPHQALLHTANRPEDECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVARCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAVVGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPEYVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLTPQGGAAPQPHPPPAFSPAFDNLYYWDQDPPERGAPPSTFKGTPTAENPEYLGLDVPV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P04626","disprot_id":"DP01484","ncbi_taxon_id":9606,"regions_counter":4,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1255,"region_id":"DP01484r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"<sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N assignments of the C-terminal intrinsically disordered cytosolic fragment of the receptor tyrosine kinase ErbB2. <i> Wang Y, Pinet L, Assrir N, Elantak L, Guerlesquin F, Badache A, Lescop E, van Heijenoort C. </i> Biomol NMR Assign, 2018","statement":[{"text":"Here we report backbone and side-chain assignment of CtErbB2, which, together with structural predictions, confirms its intrinsically disordered nature.","type":"Abstract"},{"text":"The sequence of the studied protein fragment and its 1H-15N 2D HSQC spectrum are shown in Fig. 1. The low dispersion of amide-proton chemical shifts is characteristic of a highly disordered domain, as expected from the high proline, high charged residue and low hydrophobic content of the sequence.","type":"Article"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":988,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28905237","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:25:49.246Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":988,"end":1255,"reference_id":"33741354","reference_source":"pmid","reference_html":"Structural and dynamic characterization of the C-terminal tail of ErbB2: Disordered but not random. <i> Pinet L, Wang YH, Deville C, Lescop E, Guerlesquin F, Badache A, Bontems F, Morellet N, Durand D, Assrir N, van Heijenoort C. </i> Biophys J, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01484r002","statement":[{"text":"Circular dichroism of CtErbB2 was measured at298 K and shows the characteristic signature of an IDP, with only one strong negative band at 200 nm (Fig.1B). Small angleX-ray scattering (SAXS) also supports this observation.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:25:46.493Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":988,"end":1255,"reference_id":"33741354","reference_source":"pmid","reference_html":"Structural and dynamic characterization of the C-terminal tail of ErbB2: Disordered but not random. <i> Pinet L, Wang YH, Deville C, Lescop E, Guerlesquin F, Badache A, Bontems F, Morellet N, Durand D, Assrir N, van Heijenoort C. </i> Biophys J, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01484r003","statement":[{"text":"However, ErbB2 disordered C-terminal cytoplasmic tail (CtErbB2) remains very poorly characterized in terms of structure, dynamics and detailed functional mechanism. Yet, it is where signal transduction is triggered, via phosphorylation of tyrosine residues, and carried out, via interaction with adaptor proteins. Here we report the first description of ErbB2 disordered tail at atomic resolution using NMR, complemented by SAXS.","type":"Abstract"},{"text":"The scattering curve of CtErbB2 is given in Fig.1C. The Kratky plot and the distance distribution are characteristic of a disordered protein, giving a radius of gyration of 49.2 Å from the P(r) distribution. Flory theory gives the radius of gyration Rg of a polymer with N monomers, Rg=R0Nν, where R0 and ν depend on the behavior of the polymer in solution, and especially its solvation. Its applicability to denatured or disordered proteins has already been investigated","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:25:45.919Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":988,"end":1255,"reference_id":"33741354","reference_source":"pmid","reference_html":"Structural and dynamic characterization of the C-terminal tail of ErbB2: Disordered but not random. <i> Pinet L, Wang YH, Deville C, Lescop E, Guerlesquin F, Badache A, Bontems F, Morellet N, Durand D, Assrir N, van Heijenoort C. </i> Biophys J, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01484r004","statement":[{"text":"However, ErbB2 disordered C-terminal cytoplasmic tail (CtErbB2) remains very poorly characterized in terms of structure, dynamics and detailed functional mechanism. Yet, it is where signal transduction is triggered, via phosphorylation of tyrosine residues, and carried out, via interaction with adaptor proteins. Here we report the first description of ErbB2 disordered tail at atomic resolution using NMR, complemented by SAXS.","type":"Abstract"},{"text":"At atomic resolution, the poor dispersion of CtErbB2 proton resonances in the1H-15N HSQC spectrum is typical of an intrinsically disordered protein (Fig.1D).","type":"Results"},{"text":"Moreover, backbone N-H residual dipolar couplings (RDCs) measured in stretched acrylamide gels (1DN H, Fig.2A) are negative almost all along CtErbB2 sequence,as usually observed for denatured or disordered proteins (59,60). Overall, all the data show that CtErbB2 is an intrinsically disordered region (IDR).","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-21T13:25:44.721Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P04626","date":"2018-07-20T14:36:22.000Z","acc":"P04626","name":"Receptor tyrosine-protein kinase erbB-2","length":1255,"organism":"Homo sapiens","dataset":["Autophagy-related proteins","Cancer-related proteins"],"UniParc":"UPI000003F55F","genes":[{"name":{"value":"ERBB2"},"synonyms":[{"value":"HER2"},{"value":"MLN19"},{"value":"NEU"},{"value":"NGL"}]}],"alphafold_very_low_content":0.2446215139442231,"disorder_content":0.21354581673306772,"disprot_consensus":{"full":[{"start":988,"end":1255,"type":"D"}],"Structural state":[{"start":988,"end":1255,"type":"D"}]}},{"features":{"pfam":[{"id":"PF08512","name":"Histone chaperone Rttp106-like, middle domain","start":221,"end":307},{"id":"PF18215","name":"Histone chaperone Rtt106 N-terminal domain","start":5,"end":47},{"id":"PF18469","name":"Pleckstrin homology domain","start":66,"end":203}],"gene3D":[{"start":206,"end":302,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":67,"end":205,"id":"2.30.29.120","name":"2.30.29.120"}]},"uniref50":"UniRef50_P40161","sequence":"MSKLFLDELPESLSRKIGTVVRVLPSSLEIFEELYKYALNENSNDRSGRHKKPRIDVSSDLLKTDEISETNTIFKLEGVSVLSPLRKKLDLVFYLSNVDGSPVITLLKGNDRELSIYQLNKNIKMASFLPVPEKPNLIYLFMTYTSCEDNKFSEPVVMTLNKENTLNQFKNLGLLDSNVTDFEKCVEYIRKQAILTGFKISNPFVNSTLVDTDAEKINSFHLQCHRGTKEGTLYFLPDHIIFGFKKPILLFDASDIESITYSSITRLTFNASLVTKDGEKYEFSMIDQTEYAKIDDYVKRKQMKDKSMSEELKAKSKSKGQATDGTADQPSILQEATRQMQDEKKAGVFSDDDEENDQNFEAESDLSDGSGQESSDGAEDGEEAEEDDEEDDEEEDKKGQSALNRDNSFASINGQPEQELQYKEFKEPLELEDIPIEIDNDDDEDDEDGSGVEYD","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P40161","disprot_id":"DP01485","ncbi_taxon_id":559292,"regions_counter":2,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":67,"region_id":"DP01485r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106. <i> Su D, Hu Q, Li Q, Thompson JR, Cui G, Fazly A, Davies BA, Botuyan MV, Zhang Z, Mer G. </i> Nature, 2012","statement":[{"text":"Residues 43-67 are disordered (red) and constitute the flexible linker to the tandem PH domains.","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":43,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22307274","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":67,"term_name":"flexible linker","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106. <i> Su D, Hu Q, Li Q, Thompson JR, Cui G, Fazly A, Davies BA, Botuyan MV, Zhang Z, Mer G. </i> Nature, 2012","statement":[{"text":"Residues 43-67 are disordered (red) and constitute the flexible linker to the tandem PH domains.","type":"Supplementary material"}],"term_id":"IDPO:0000033","curator_id":"eschad","start":43,"term_ontology":"IDPO","curator_name":"Eva Schad","reference_id":"22307274","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01485r002","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_P40161","date":"2018-07-20T16:42:05.000Z","acc":"P40161","name":"Histone chaperone RTT106","length":455,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000013BBBB","genes":[{"name":{"value":"RTT106","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16157874","url":"http://www.ncbi.nlm.nih.gov/pubmed/16157874","alternativeUrl":"https://europepmc.org/abstract/MED/16157874"}}]},"orfNames":[{"value":"N1346"}],"olnNames":[{"value":"YNL206C"}]}],"alphafold_very_low_content":0.2835164835164835,"disorder_content":0.054945054945054944,"disprot_consensus":{"full":[{"start":43,"end":67,"type":"D"}],"Structural state":[{"start":43,"end":67,"type":"D"}],"Disorder function":[{"start":43,"end":67,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02189","name":"Immunoreceptor tyrosine-based activation motif","start":185,"end":204},{"id":"PF13927","name":"Immunoglobulin domain","start":40,"end":108}],"gene3D":[{"start":34,"end":130,"id":"2.60.40.10","name":"Immunoglobulins"}]},"uniref50":"UniRef50_P11912","sequence":"MPGGPGVLQALPATIFLLFLLSAVYLGPGCQALWMHKVPASLMVSLGEDAHFQCPHNSSNNANVTWWRVLHGNYTWPPEFLGPGEDPNGTLIIQNVNKSHGGIYVCRVQEGNESYQQSCGTYLRVRQPPPRPFLDMGEGTKNRIITAEGIILLFCAVVPGTLLLFRKRWQNEKLGLDAGDEYEDENLYEGLNLDDCSMYEDISRGLQGTYQDVGSLNIGDVQLEKP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P11912","disprot_id":"DP01486","ncbi_taxon_id":9606,"regions_counter":1,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":226,"region_id":"DP01486r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Lipid-binding activity of intrinsically unstructured cytoplasmic domains of multichain immune recognition receptor signaling subunits. <i> Sigalov AB, Aivazian DA, Uversky VN, Stern LJ. </i> Biochemistry, 2006","statement":[{"text":"CD analysis of shows the characteristics of intrinsically unstructured proteins at both concentrations.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":166,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17176095","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P11912","date":"2018-07-20T20:33:47.000Z","acc":"P11912","name":"B-cell antigen receptor complex-associated protein alpha chain","length":226,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI000016AD0F","genes":[{"name":{"value":"CD79A"},"synonyms":[{"value":"IGA"},{"value":"MB1"}]}],"alphafold_very_low_content":0.0752212389380531,"disorder_content":0.26991150442477874,"disprot_consensus":{"full":[{"start":166,"end":226,"type":"D"}],"Structural state":[{"start":166,"end":226,"type":"D"}]}},{"features":{"pfam":[{"id":"PF07686","name":"Immunoglobulin V-set domain","start":49,"end":142}],"gene3D":[{"start":43,"end":159,"id":"2.60.40.10","name":"Immunoglobulins"}]},"uniref50":"UniRef50_P40259","sequence":"MARLALSPVPSHWMVALLLLLSAEPVPAARSEDRYRNPKGSACSRIWQSPRFIARKRGFTVKMHCYMNSASGNVSWLWKQEMDENPQQLKLEKGRMEESQNESLATLTIQGIRFEDNGIYFCQQKCNNTSEVYQGCGTELRVMGFSTLAQLKQRNTLKDGIIMIQTLLIILFIIVPIFLLLDKDDSKAGMEEDHTYEGLDIDQTATYEDIVTLRTGEVKWSVGEHPGQE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P40259","disprot_id":"DP01487","ncbi_taxon_id":9606,"regions_counter":1,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":229,"region_id":"DP01487r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Lipid-binding activity of intrinsically unstructured cytoplasmic domains of multichain immune recognition receptor signaling subunits. <i> Sigalov AB, Aivazian DA, Uversky VN, Stern LJ. </i> Biochemistry, 2006","statement":[{"text":"CD analysis of  shows the characteristics of intrinsically unstructured proteins at both concentrations.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":181,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17176095","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P40259","date":"2018-07-20T20:35:07.000Z","acc":"P40259","name":"B-cell antigen receptor complex-associated protein beta chain","length":229,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI000011C13D","genes":[{"name":{"value":"CD79B"},"synonyms":[{"value":"B29"},{"value":"IGB"}]}],"alphafold_very_low_content":0.09606986899563319,"disorder_content":0.21397379912663755,"disprot_consensus":{"full":[{"start":181,"end":229,"type":"D"}],"Structural state":[{"start":181,"end":229,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02604","name":"Antitoxin Phd_YefM, type II toxin-antitoxin system","start":1,"end":73}],"gene3D":[{"start":41,"end":83,"id":"1.10.1220.170","name":"1.10.1220.170"},{"start":1,"end":40,"id":"3.40.1620.10","name":"YefM-like domain"}]},"uniref50":"UniRef50_P69347","sequence":"MRTISYSEARQNLSATMMKAVEDHAPILITRQNGEACVLMSLEEYNSLEETAYLLRSPANARRLMDSIDSLKSGKGTEKDIIE","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P69347","disprot_id":"DP01488","dataset":["Unicellular toxins and antitoxins"],"ncbi_taxon_id":83333,"regions_counter":12,"creator":"bhajdu","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":83,"region_id":"DP01488r001","released":"2022_03","ec_id":"ECO:0007691","reference_html":"The YefM antitoxin defines a family of natively unfolded proteins: implications as a novel antibacterial target. <i> Cherny I, Gazit E. </i> J Biol Chem, 2004","statement":[{"text":"Analysis of YefM levels in E. coli, before and after repression at different intervals, reveals that the YefM antitoxin is proteolytically unstable.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":1,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T17:37:36.375Z","curator_name":"Bálint Mészáros"},"reference_id":"14672926","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":83,"region_id":"DP01488r002","released":"2022_03","ec_id":"ECO:0006228","reference_html":"The YefM antitoxin defines a family of natively unfolded proteins: implications as a novel antibacterial target. <i> Cherny I, Gazit E. </i> J Biol Chem, 2004","statement":[{"text":"FTIR spectroscopy also indicates that YefM protein is random coil-structured.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":1,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T17:34:50.636Z","curator_name":"Bálint Mészáros"},"reference_id":"14672926","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":83,"region_id":"DP01488r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The YefM antitoxin defines a family of natively unfolded proteins: implications as a novel antibacterial target. <i> Cherny I, Gazit E. </i> J Biol Chem, 2004","statement":[{"text":"The far-UV CD spectra of the purified YefM protein show a typical random coil pattern.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":1,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T17:34:55.452Z","curator_name":"Bálint Mészáros"},"reference_id":"14672926","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP01488r007","validated":{"curator_id":"bmesza","timestamp":"2020-12-10T17:38:23.468Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":23,"term_id":"GO:0005515","start":11,"version":3,"statement":[{"text":"SPR analysis was used to quantitative determine the affinity between the YoeB toxin and the YefM11–23 peptide fragment.","type":"Results"},{"text":"an equilibrium constant (KD) of 0.4 microM was determined for the YoeB-YefM11–23complex. This dissociation constant is consistent with a specific binding between the toxin and the peptide fragment.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P69348","partner_end":null}],"term_name":"protein binding","ec_name":"surface plasmon resonance evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"14672926","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001269","curator_id":"rpancsa","reference_html":"The YefM antitoxin defines a family of natively unfolded proteins: implications as a novel antibacterial target. <i> Cherny I, Gazit E. </i> J Biol Chem, 2004","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01488r008","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T10:09:25.824Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":83,"term_id":"IDPO:0000002","start":56,"version":2,"statement":[{"text":"The N-terminal segments of the two YefM monomers form a symmetrical dimer. One of the YefM C-terminal segments (H4–S4) extending from the N-terminal dimer exclusively binds the globular YoeB monomer. The other YefM C terminus is structurally disordered.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"16109374","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2A6Q"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"rpancsa","reference_html":"Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin. <i> Kamada K, Hanaoka F. </i> Mol Cell, 2005","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP01488r009","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T10:09:44.230Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":83,"term_id":"IDPO:0000011","start":1,"version":2,"statement":[{"text":"The difference in behavior indicates that the polypeptide region from the end of the H3 helix to the C terminus is a random coil in the absence of a binding target, and undergoes a disorder-to-order transition upon binding YoeB.","type":"Results"}],"term_name":"disorder to order","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"16109374","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2A6Q"}],"term_namespace":"Structural transition","ec_id":"ECO:0005670","curator_id":"rpancsa","reference_html":"Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin. <i> Kamada K, Hanaoka F. </i> Mol Cell, 2005","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP01488r010","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T10:10:00.124Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":83,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"The difference in behavior indicates that the polypeptide region from the end of the H3 helix to the C terminus is a random coil in the absence of a binding target, and undergoes a disorder-to-order transition upon binding YoeB.","type":"Results"},{"text":"One of the YefM C-terminal segments (H4–S4) extending from the N-terminal dimer exclusively binds the globular YoeB monomer.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P69348","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"16109374","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2A6Q"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"rpancsa","reference_html":"Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin. <i> Kamada K, Hanaoka F. </i> Mol Cell, 2005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01488r011","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T10:10:01.056Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":55,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"The N-terminal segments of the two YefM monomers form a symmetrical dimer.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P69346","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"16109374","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2A6Q"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"rpancsa","reference_html":"Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin. <i> Kamada K, Hanaoka F. </i> Mol Cell, 2005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01488r012","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T10:09:07.366Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":83,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"YefM  remains  soluble  through  boiling.","type":"Figure"}],"term_name":"disorder","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"14672926","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006317","curator_id":"rpancsa","reference_html":"The YefM antitoxin defines a family of natively unfolded proteins: implications as a novel antibacterial target. <i> Cherny I, Gazit E. </i> J Biol Chem, 2004","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P69347","date":"2018-07-20T20:58:58.000Z","acc":"P69346","name":"Antitoxin YefM","length":83,"organism":"Escherichia coli (strain K12)","UniParc":"UPI000013AC2A","genes":[{"name":{"value":"yefM"},"olnNames":[{"value":"b2017"},{"value":"JW5835"}]}],"alphafold_very_low_content":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":83,"type":"T"}],"Structural state":[{"start":1,"end":83,"type":"D"}],"Molecular function":[{"start":1,"end":83,"type":"F"}],"Structural transition":[{"start":1,"end":83,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":679,"end":739}],"gene3D":[{"start":620,"end":746,"id":"3.30.70.330","name":"3.30.70.330"}]},"uniref50":"UniRef50_Q9UBK2","sequence":"MAWDMCNQDSESVWSDIECAALVGEDQPLCPDLPELDLSELDVNDLDTDSFLGGLKWCSDQSEIISNQYNNEPSNIFEKIDEENEANLLAVLTETLDSLPVDEDGLPSFDALTDGDVTTDNEASPSSMPDGTPPPQEAEEPSLLKKLLLAPANTQLSYNECSGLSTQNHANHNHRIRTNPAIVKTENSWSNKAKSICQQQKPQRRPCSELLKYLTTNDDPPHTKPTENRNSSRDKCTSKKKSHTQSQSQHLQAKPTTLSLPLTPESPNDPKGSPFENKTIERTLSVELSGTAGLTPPTTPPHKANQDNPFRASPKLKSSCKTVVPPPSKKPRYSESSGTQGNNSTKKGPEQSELYAQLSKSSVLTGGHEERKTKRPSLRLFGDHDYCQSINSKTEILINISQELQDSRQLENKDVSSDWQGQICSSTDSDQCYLRETLEASKQVSPCSTRKQLQDQEIRAELNKHFGHPSQAVFDDEADKTGELRDSDFSNEQFSKLPMFINSGLAMDGLFDDSEDESDKLSYPWDGTQSYSLFNVSPSCSSFNSPCRDSVSPPKSLFSQRPQRMRSRSRSFSRHRSCSRSPYSRSRSRSPGSRSSSRSCYYYESSHYRHRTHRNSPLYVRSRSRSPYSRRPRYDSYEEYQHERLKREEYRREYEKRESERAKQRERQRQKAIEERRVIYVGKIRPDTTRTELRDRFEVFGEIEECTVNLRDDGDSYGFITYRYTCDAFAALENGYTLRRSNETDFELYFCGRKQFFKSNYADLDSNSDDFDPASTKSKYDSLDFDSLLKEAQRSLRR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UBK2","disprot_id":"DP01489","ncbi_taxon_id":9606,"regions_counter":8,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":220,"region_id":"DP01489r001","released":"2022_03","ec_id":"ECO:0006196","reference_html":"Disorder-to-order transition underlies the structural basis for the assembly of a transcriptionally active PGC-1α/ERRγ complex. <i> Devarakonda S, Gupta K, Chalmers MJ, Hunt JF, Griffin PR, Van Duyne GD, Spiegelman BM. </i> Proc Natl Acad Sci U S A, 2011","statement":[{"text":"HDX analysis of PGC1α220 revealed that most of the backbone amides were fully exchanged after 10 s incubation with deuterium, consistent with the predicted disorder.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":2,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22049338","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":220,"region_id":"DP01489r002","released":"2022_03","ec_id":"ECO:0006275","reference_html":"Disorder-to-order transition underlies the structural basis for the assembly of a transcriptionally active PGC-1α/ERRγ complex. <i> Devarakonda S, Gupta K, Chalmers MJ, Hunt JF, Griffin PR, Van Duyne GD, Spiegelman BM. </i> Proc Natl Acad Sci U S A, 2011","statement":[{"text":"SV analysis at 4 °C yields a frictional coefficient ratio (f∕f o) of 2.7 (a globular particle has an f∕f o of approximately 1.2, whereas a value greater than 1.8 indicates asymmetry in shape), indicating an extremely elongated shape.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":2,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"analytical ultracentrifugation evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22049338","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":220,"term_name":"disorder to order","released":"2022_03","ec_name":"analytical ultracentrifugation evidence used in manual assertion","reference_html":"Disorder-to-order transition underlies the structural basis for the assembly of a transcriptionally active PGC-1α/ERRγ complex. <i> Devarakonda S, Gupta K, Chalmers MJ, Hunt JF, Griffin PR, Van Duyne GD, Spiegelman BM. </i> Proc Natl Acad Sci U S A, 2011","statement":[{"text":"The reduction in f∕f 0 between PGC1α220 and the binary complex (2.0 versus 1.5) is suggestive of coactivator compaction upon complex formation.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"atantos","start":2,"term_ontology":"IDPO","curator_name":"Agnes Tantos","reference_id":"22049338","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006275","region_id":"DP01489r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":220,"region_id":"DP01489r004","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Disorder-to-order transition underlies the structural basis for the assembly of a transcriptionally active PGC-1α/ERRγ complex. <i> Devarakonda S, Gupta K, Chalmers MJ, Hunt JF, Griffin PR, Van Duyne GD, Spiegelman BM. </i> Proc Natl Acad Sci U S A, 2011","statement":[{"text":"Despite being monomeric by mass as indicated by SEC-MALS, a Stokes radius of Rs of 42.9 Å \u0002 0.46 was determined, indicative of a molten-globular, extended conformation in solution.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":2,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"chromatography evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22049338","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":220,"region_id":"DP01489r005","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Disorder-to-order transition underlies the structural basis for the assembly of a transcriptionally active PGC-1α/ERRγ complex. <i> Devarakonda S, Gupta K, Chalmers MJ, Hunt JF, Griffin PR, Van Duyne GD, Spiegelman BM. </i> Proc Natl Acad Sci U S A, 2011","statement":[{"text":"This low level of compactness is further underscored by an Rs/Rg value of approximately 1.45 for PGC1α220, similar to that expected for a random coil. The Kratky and Porod–Debye plots (22–26) for PGC1α220 are clearly indicative of a largely disordered species lacking a well-packed core.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":2,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22049338","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":220,"term_name":"protein binding","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","reference_html":"Disorder-to-order transition underlies the structural basis for the assembly of a transcriptionally active PGC-1α/ERRγ complex. <i> Devarakonda S, Gupta K, Chalmers MJ, Hunt JF, Griffin PR, Van Duyne GD, Spiegelman BM. </i> Proc Natl Acad Sci U S A, 2011","statement":[{"text":"PGC-1α and ERRγ share tissue specificity, have overlapping functions, and demonstrate a robust physical and functional interaction.","type":"Introduction"}],"term_id":"GO:0005515","curator_id":"atantos","start":2,"term_ontology":"GO","curator_name":"Agnes Tantos","reference_id":"22049338","version":3,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","region_id":"DP01489r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":220,"term_name":"disorder to order","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","reference_html":"Disorder-to-order transition underlies the structural basis for the assembly of a transcriptionally active PGC-1α/ERRγ complex. <i> Devarakonda S, Gupta K, Chalmers MJ, Hunt JF, Griffin PR, Van Duyne GD, Spiegelman BM. </i> Proc Natl Acad Sci U S A, 2011","statement":[{"text":"The Kratky and Porod–Debye plots for the complex are indicative of a well-folded globular particle. Combined, these experiments indicate that PGC1α220 undergoes\na disorder-to-order transition upon docking onto the LBD, resulting in a binary complex, which is significantly more compact and structured.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"atantos","start":2,"term_ontology":"IDPO","curator_name":"Agnes Tantos","reference_id":"22049338","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","region_id":"DP01489r007","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":220,"region_id":"DP01489r008","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Disorder-to-order transition underlies the structural basis for the assembly of a transcriptionally active PGC-1α/ERRγ complex. <i> Devarakonda S, Gupta K, Chalmers MJ, Hunt JF, Griffin PR, Van Duyne GD, Spiegelman BM. </i> Proc Natl Acad Sci U S A, 2011","statement":[{"text":"CD analysis of PGC1α220 estimated only 27% native secondary structure in the activation domain.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":2,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22049338","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9UBK2","date":"2018-07-21T18:13:05.000Z","acc":"Q9UBK2","name":"Peroxisome proliferator-activated receptor gamma coactivator 1-alpha","length":798,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000004D072","genes":[{"name":{"value":"PPARGC1A"},"synonyms":[{"value":"LEM6"},{"value":"PGC1"},{"value":"PGC1A","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16753578","url":"http://www.ncbi.nlm.nih.gov/pubmed/16753578","alternativeUrl":"https://europepmc.org/abstract/MED/16753578"}}]},{"value":"PPARGC1"}]}],"alphafold_very_low_content":0.6215538847117794,"disorder_content":0.2744360902255639,"disprot_consensus":{"full":[{"start":2,"end":220,"type":"T"}],"Structural state":[{"start":2,"end":220,"type":"D"}],"Structural transition":[{"start":2,"end":220,"type":"T"}],"Molecular function":[{"start":2,"end":220,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00008","name":"EGF-like domain","start":292,"end":318},{"id":"PF00008","name":"EGF-like domain","start":328,"end":357},{"id":"PF00008","name":"EGF-like domain","start":366,"end":398},{"id":"PF00008","name":"EGF-like domain","start":406,"end":435},{"id":"PF00008","name":"EGF-like domain","start":444,"end":474},{"id":"PF01414","name":"Delta serrate ligand","start":175,"end":220},{"id":"PF07657","name":"N terminus of Notch ligand C2-like domain","start":27,"end":173},{"id":"PF21700","name":"Delta-like/Jagged, EGF-like domain","start":260,"end":285}],"gene3D":[{"start":176,"end":221,"id":"2.10.25.140","name":"2.10.25.140"},{"start":26,"end":175,"id":"2.60.40.3510","name":"2.60.40.3510"},{"start":442,"end":480,"id":"2.10.25.10","name":"Laminin"},{"start":404,"end":441,"id":"2.10.25.10","name":"Laminin"},{"start":326,"end":362,"id":"2.10.25.10","name":"Laminin"},{"start":284,"end":324,"id":"2.10.25.10","name":"Laminin"},{"start":481,"end":521,"id":"2.10.25.10","name":"Laminin"},{"start":222,"end":283,"id":"2.10.25.10","name":"Laminin"},{"start":363,"end":403,"id":"2.10.25.10","name":"Laminin"}]},"uniref50":"UniRef50_Q9NR61","sequence":"MAAASRSASGWALLLLVALWQQRAAGSGVFQLQLQEFINERGVLASGRPCEPGCRTFFRVCLKHFQAVVSPGPCTFGTVSTPVLGTNSFAVRDDSSGGGRNPLQLPFNFTWPGTFSLIIEAWHAPGDDLRPEALPPDALISKIAIQGSLAVGQNWLLDEQTSTLTRLRYSYRVICSDNYYGDNCSRLCKKRNDHFGHYVCQPDGNLSCLPGWTGEYCQQPICLSGCHEQNGYCSKPAECLCRPGWQGRLCNECIPHNGCRHGTCSTPWQCTCDEGWGGLFCDQDLNYCTHHSPCKNGATCSNSGQRSYTCTCRPGYTGVDCELELSECDSNPCRNGGSCKDQEDGYHCLCPPGYYGLHCEHSTLSCADSPCFNGGSCRERNQGANYACECPPNFTGSNCEKKVDRCTSNPCANGGQCLNRGPSRMCRCRPGFTGTYCELHVSDCARNPCAHGGTCHDLENGLMCTCPAGFSGRRCEVRTSIDACASSPCFNRATCYTDLSTDTFVCNCPYGFVGSRCEFPVGLPPSFPWVAVSLGVGLAVLLVLLGMVAVAVRQLRLRRPDDGSREAMNNLSDFQKDNLIPAAQLKNTNQKKELEVDCGLDKSNCGKQQNHTLDYNLAPGPLGRGTMPGKFPHSDKSLGEKAPLRLHSEKPECRISAICSPRDSMYQSVCLISEERNECVIATEV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9NR61","disprot_id":"DP01490","ncbi_taxon_id":9606,"regions_counter":4,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":685,"region_id":"DP01490r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Prevalence of intrinsic disorder in the intracellular region of human single-pass type I proteins: the case of the notch ligand Delta-4. <i> De Biasio A, Guarnaccia C, Popovic M, Uversky VN, Pintar A, Pongor S. </i> J Proteome Res, 2008","statement":[{"text":"The far-UV CD spectrum of DLL4_IC in Tris buffer shows a strong minimum at 198 nm, which is typical of disordered proteins.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":553,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18435556","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":685,"region_id":"DP01490r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Prevalence of intrinsic disorder in the intracellular region of human single-pass type I proteins: the case of the notch ligand Delta-4. <i> De Biasio A, Guarnaccia C, Popovic M, Uversky VN, Pintar A, Pongor S. </i> J Proteome Res, 2008","statement":[{"text":"The lack of chemical shift dispersion in the HN region as well as in the methyl region indicates the absence of globular structure, and the presence of little, if any, secondary structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":553,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18435556","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":685,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Prevalence of intrinsic disorder in the intracellular region of human single-pass type I proteins: the case of the notch ligand Delta-4. <i> De Biasio A, Guarnaccia C, Popovic M, Uversky VN, Pintar A, Pongor S. </i> J Proteome Res, 2008","statement":[{"text":"Delta-4 was shown to interact through its evolutionarily conserved C-terminal motif (ATEV) with the PDZ domains of Dlg-1, the human homologue of Drosophila Discs Large protein.","type":"Discussion"}],"term_id":"GO:0005515","curator_id":"atantos","start":553,"term_ontology":"GO","curator_name":"Agnes Tantos","reference_id":"18435556","version":3,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01490r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":685,"region_id":"DP01490r004","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Prevalence of intrinsic disorder in the intracellular region of human single-pass type I proteins: the case of the notch ligand Delta-4. <i> De Biasio A, Guarnaccia C, Popovic M, Uversky VN, Pintar A, Pongor S. </i> J Proteome Res, 2008","statement":[{"text":"We interpret size exclusion chromatography results as indicative of the presence of a monomeric, disordered but partially compact state.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":553,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"chromatography evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18435556","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9NR61","date":"2018-07-21T18:13:47.000Z","acc":"Q9NR61","name":"Delta-like protein 4","length":685,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000047825","genes":[{"name":{"value":"DLL4"},"orfNames":[{"value":"UNQ1895/PRO4341"}]}],"alphafold_very_low_content":0.2,"disorder_content":0.19416058394160585,"disprot_consensus":{"full":[{"start":553,"end":685,"type":"D"}],"Structural state":[{"start":553,"end":685,"type":"D"}],"Molecular function":[{"start":553,"end":685,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00169","name":"PH domain","start":91,"end":179},{"id":"PF01237","name":"Oxysterol-binding protein","start":418,"end":795}],"gene3D":[{"start":87,"end":186,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":502,"end":660,"id":"2.40.160.120","name":"2.40.160.120"}]},"uniref50":"UniRef50_P22059","sequence":"MAATELRGVVGPGPAAIAALGGGGAGPPVVGGGGGRGDAGPGSGAASGTVVAAAAGGPGPGAGGVAAAGPAPAPPTGGSGGSGAGGSGSAREGWLFKWTNYIKGYQRRWFVLSNGLLSYYRSKAEMRHTCRGTINLATANITVEDSCNFIISNGGAQTYHLKASSEVERQRWVTALELAKAKAVKMLAESDESGDEESVSQTDKTELQNTLRTLSSKVEDLSTCNDLIAKHGTALQRSLSELESLKLPAESNEKIKQVNERATLFRITSNAMINACRDFLMLAQTHSKKWQKSLQYERDQRIRLEETLEQLAKQHNHLERAFRGATVLPANTPGNVGSGKDQCCSGKGDMSDEDDENEFFDAPEIITMPENLGHKRTGSNISGASSDISLDEQYKHQLEETKKEKRTRIPYKPNYSLNLWSIMKNCIGKELSKIPMPVNFNEPLSMLQRLTEDLEYHELLDRAAKCENSLEQLCYVAAFTVSSYSTTVFRTSKPFNPLLGETFELDRLEENGYRSLCEQVSHHPPAAAHHAESKNGWTLRQEIKITSKFRGKYLSIMPLGTIHCIFHATGHHYTWKKVTTTVHNIIVGKLWIDQSGEIDIVNHKTGDKCNLKFVPYSYFSRDVARKVTGEVTDPSGKVHFALLGTWDEKMECFKVQPVIGENGGDARQRGHEAEESRVMLWKRNPLPKNAENMYYFSELALTLNAWESGTAPTDSRLRPDQRLMENGRWDEANAEKQRLEEKQRLSRKKREAEAMKATEDGTPYDPYKALWFERKKDPVTKELTHIYRGEYWECKEKQDWSSCPDIF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P22059","disprot_id":"DP01491","ncbi_taxon_id":9606,"regions_counter":3,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":379,"region_id":"DP01491r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Electrostatic interaction between oxysterol-binding protein and VAMP-associated protein A revealed by NMR and mutagenesis studies. <i> Furuita K, Jee J, Fukada H, Mishima M, Kojima C. </i> J Biol Chem, 2010","statement":[{"text":"All residues of OSBPF showed negative NOE values in the unbound state, suggesting that free OSBPF is flexible. Structure analysis of free OSBPF using the TALOS program with the assigned 1HN, 15N, 13C\u0004, C\u0007, and 13C\u0001 chemical shifts also showed no ordered structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":346,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20178991","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":379,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Electrostatic interaction between oxysterol-binding protein and VAMP-associated protein A revealed by NMR and mutagenesis studies. <i> Furuita K, Jee J, Fukada H, Mishima M, Kojima C. </i> J Biol Chem, 2010","statement":[{"text":"Oxysterol-binding protein (OSBP), a cytosolic receptor of cholesterol and oxysterols, is recruited to the endoplasmic reticulum by binding to the cytoplasmic major sperm protein (MSP) domain of integral endoplasmic reticulum protein VAMP-associated protein-A (VAP-A).","type":"Abstract"}],"term_id":"GO:0005515","curator_id":"atantos","start":346,"term_ontology":"GO","curator_name":"Agnes Tantos","reference_id":"20178991","version":3,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01491r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":379,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Electrostatic interaction between oxysterol-binding protein and VAMP-associated protein A revealed by NMR and mutagenesis studies. <i> Furuita K, Jee J, Fukada H, Mishima M, Kojima C. </i> J Biol Chem, 2010","statement":[{"text":"Upon binding to VAP-AMSP, 1H,15N hetero-NOE values of the residues around the FFAT motif of OSBPF changed from negative to positive, indicating that OSBPF formed a stable structure upon binding to VAP-AMSP.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"atantos","start":346,"term_ontology":"IDPO","curator_name":"Agnes Tantos","reference_id":"20178991","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01491r003","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_P22059","date":"2018-07-21T18:14:14.000Z","acc":"P22059","name":"Oxysterol-binding protein 1","length":807,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000130EAF","genes":[{"name":{"value":"OSBP","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:8503","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8503"}}]},"synonyms":[{"value":"OSBP1"}]}],"alphafold_very_low_content":0.23543990086741015,"disorder_content":0.042131350681536554,"disprot_consensus":{"full":[{"start":346,"end":379,"type":"T"}],"Structural state":[{"start":346,"end":379,"type":"D"}],"Molecular function":[{"start":346,"end":379,"type":"F"}],"Structural transition":[{"start":346,"end":379,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00060","name":"Ligand-gated ion channel","start":556,"end":829},{"id":"PF01094","name":"Receptor family ligand binding region","start":107,"end":316},{"id":"PF10565","name":"N-methyl D-aspartate receptor 2B3 C-terminus","start":840,"end":1482},{"id":"PF10613","name":"Ligated ion channel L-glutamate- and glycine-binding site","start":455,"end":540}],"gene3D":[{"start":661,"end":769,"id":"3.40.190.10","name":"Periplasmic binding protein-like II"},{"start":770,"end":797,"id":"3.40.190.10","name":"Periplasmic binding protein-like II"},{"start":403,"end":550,"id":"3.40.190.10","name":"Periplasmic binding protein-like II"},{"start":149,"end":380,"id":"3.40.50.2300","name":"3.40.50.2300"},{"start":65,"end":360,"id":"3.40.50.2300","name":"3.40.50.2300"}]},"uniref50":"UniRef50_Q00960","sequence":"MKPSAECCSPKFWLVLAVLAVSGSKARSQKSAPSIGIAVILVGTSDEVAIKDAHEKDDFHHLSVVPRVELVAMNETDPKSIITRICDLMSDRKIQGVVLADDTDQEAIAQILDFISAQTLTPILGIHGGSSMIMADKDESSMFFQFGPSIEQQASVMLNIMEEYDWYIFSIVTTYFPGYQDFVNKIRSTIENSFVGWELEEVLLLDMSLDDGDSKIQNQLKKLQSPIILLYCTKEEATYIFEVANSVGLTGYGYTWIVPSLVAGDTDTVPSEFPTGLISVSYDEWDYGLPARVRDGIAIITTAASDMLSEHSFIPEPKSSCYNTHEKRIYQSNMLNRYLINVTFEGRNLSFSEDGYQMHPKLVIILLNKERKWERVGKWKDKSLQMKYYVWPRMCPETEEQEDDHLSIVTLEEAPFVIVESVDPLSGTCMRNTVPCQKRIISENKTDEEPGYIKKCCKGFCIDILKKISKSVKFTYDLYLVTNGKHGKKINGTWNGMIGEVVMKRAYMAVGSLTINEERSEVVDFSVPFIETGISVMVSRSNGTVSPSAFLEPFSADVWVMMFVMLLIVSAVAVFVFEYFSPVGYNRCLADGREPGGPSFTIGKAIWLLWGLVFNNSVPVQNPKGTTSKIMVSVWAFFAVIFLASYTANLAAFMIQEEYVDQVSGLSDKKFQRPNDFSPPFRFGTVPNGSTERNIRNNYAEMHAYMGKFNQRGVDDALLSLKTGKLDAFIYDAAVLNYMAGRDEGCKLVTIGSGKVFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALWLTGICHNEKNEVMSSQLDIDNMAGVFYMLGAAMALSLITFICEHLFYWQFRHCFMGVCSGKPGMVFSISRGIYSCIHGVAIEERQSVMNSPTATMNNTHSNILRLLRTAKNMANLSGVNGSPQSALDFIRRESSVYDISEHRRSFTHSDCKSYNNPPCEENLFSDYISEVERTFGNLQLKDSNVYQDHYHHHHRPHSIGSTSSIDGLYDCDNPPFTTQPRSISKKPLDIGLPSSKHSQLSDLYGKFSFKSDRYSGHDDLIRSDVSDISTHTVTYGNIEGNAAKRRKQQYKDSLKKRPASAKSRREFDEIELAYRRRPPRSPDHKRYFRDKEGLRDFYLDQFRTKENSPHWEHVDLTDIYKERSDDFKRDSVSGGGPCTNRSHLKHGTGDKHGVVGGVPAPWEKNLTNVDWEDRSGGNFCRSCPSKLHNYSSTVAGQNSGRQACIRCEACKKAGNLYDISEDNSLQELDQPAAPVAVSSNASTTKYPQSPTNSKAQKKNRNKLRRQHSYDTFVDLQKEEAALAPRSVSLKDKGRFMDGSPYAHMFEMPAGESSFANKSSVTTAGHHHNNPGSGYMLSKSLYPDRVTQNPFIPTFGDDQCLLHGSKSYFFRQPTVAGASKTRPDFRALVTNKPVVSALHGAVPGRFQKDICIGNQSNPCVPNNKNPRAFNGSSNGHVYEKLSSIESDV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q00960","disprot_id":"DP01492","ncbi_taxon_id":10090,"regions_counter":8,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1482,"region_id":"DP01492r001","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Beyond the random coil: stochastic conformational switching in intrinsically disordered proteins. <i> Choi UB, McCann JJ, Weninger KR, Bowen ME. </i> Structure, 2011","statement":[{"text":"Circular dichroism of N2B showed no signs of secondary structure (Figure 4). This is the first experimental conformation that the cytoplasmic domain is disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1259,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-30T14:01:39.680Z","reference_source":"pmid","term_name":"disorder","reference_id":"21481779","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:22:32.300Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1482,"region_id":"DP01492r003","released":"2023_12","ec_id":"ECO:0007691","reference_html":"Effect of Src kinase phosphorylation on disordered C-terminal domain of N-methyl-D-aspartic acid (NMDA) receptor subunit GluN2B protein. <i> Choi UB, Xiao S, Wollmuth LP, Bowen ME. </i> J Biol Chem, 2011","statement":[{"text":"Limited trypsin proteolysis of CTD2 with 2 μg/ml trypsin resulted in complete degradation in less than 30 min as expected for a disordered protein (Fig. 2B). High molecular weight intermediate bands are visible at early time points indicating that some cleavage sites are partially protected.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1259,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-30T14:06:30.543Z","reference_source":"pmid","term_name":"disorder","reference_id":"21712388","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:22:34.670Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1482,"region_id":"DP01492r005","released":"2022_03","ec_id":"ECO:0001183","reference_html":"Effect of Src kinase phosphorylation on disordered C-terminal domain of N-methyl-D-aspartic acid (NMDA) receptor subunit GluN2B protein. <i> Choi UB, Xiao S, Wollmuth LP, Bowen ME. </i> J Biol Chem, 2011","statement":[{"text":"Although the constructs sample different regions of CTD2, there was little dispersion in the FRET peaks suggesting a lack of local structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":1259,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21712388","ec_go":"IPI","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-30T14:05:50.606Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1482,"region_id":"DP01492r006","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Beyond the random coil: stochastic conformational switching in intrinsically disordered proteins. <i> Choi UB, McCann JJ, Weninger KR, Bowen ME. </i> Structure, 2011","statement":[{"text":"Analytical SEC of N2B gave an RH of 3.27 ± 0.021 nm for an apparent molecular weight of 70.4 ± 1.2 kDa compared with the actual molecular weight of 25.3 kDa.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":1259,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"chromatography evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21481779","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-30T14:05:03.751Z"}},{"start":1334,"end":1338,"reference_id":"21712388","reference_source":"pmid","reference_html":"Effect of Src kinase phosphorylation on disordered C-terminal domain of N-methyl-D-aspartic acid (NMDA) receptor subunit GluN2B protein. <i> Choi UB, Xiao S, Wollmuth LP, Bowen ME. </i> J Biol Chem, 2011","date":"2023-11-30T14:10:40.522Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001202","ec_ontology":"ECO","ec_name":"in vitro protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Tyr1336Thr","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Tyr1472Thr","start":null,"end":null,"position":null}],"region_id":"DP01492r007","statement":[{"text":"The shift from phosphorylation was dependent on the presence of Mg2+ as Src in the presence of ATP alone had no effect. To confirm the sites of Src phosphorylation, we mutated Tyr-1336 and Tyr-1472 to threonine (ΔY), which eliminated the mobility shift induced by Src (right lanes, Fig. 2A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:22:43.394Z"}},{"start":1470,"end":1474,"reference_id":"21712388","reference_source":"pmid","reference_html":"Effect of Src kinase phosphorylation on disordered C-terminal domain of N-methyl-D-aspartic acid (NMDA) receptor subunit GluN2B protein. <i> Choi UB, Xiao S, Wollmuth LP, Bowen ME. </i> J Biol Chem, 2011","date":"2023-11-30T14:11:14.600Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001202","ec_ontology":"ECO","ec_name":"in vitro protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Tyr1336Thr","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Tyr1472Thr","start":null,"end":null,"position":null}],"region_id":"DP01492r008","statement":[{"text":"The shift from phosphorylation was dependent on the presence of Mg2+ as Src in the presence of ATP alone had no effect. To confirm the sites of Src phosphorylation, we mutated Tyr-1336 and Tyr-1472 to threonine (ΔY), which eliminated the mobility shift induced by Src (right lanes, Fig. 2A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:22:45.893Z"}}],"released":"2018_11","uniref100":"UniRef100_Q01097","date":"2018-07-21T18:15:22.000Z","acc":"Q01097","name":"Glutamate receptor ionotropic, NMDA 2B","length":1482,"organism":"Mus musculus","dataset":["Condensates-related proteins"],"UniParc":"UPI0000028174","genes":[{"name":{"value":"Grin2b"}}],"alphafold_very_low_content":0.44129554655870445,"disorder_content":0.15114709851551958,"disprot_consensus":{"full":[{"start":1259,"end":1482,"type":"D"}],"Structural state":[{"start":1259,"end":1482,"type":"D"}],"Disorder function":[{"start":1334,"end":1338,"type":"F"},{"start":1470,"end":1474,"type":"F"}]}},{"acc":"P09429","sequence":"MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEEDEEDEEDEEEEEDEEDEDEEEDDDDE","alphafold_very_low_content":"0.22325581395348837","creator":"eficho","dataset":["NDDs-related proteins"],"date":"2018-07-23T10:39:15.000Z","disprot_id":"DP01493","features":{"pfam":[{"id":"PF00505","name":"HMG (high mobility group) box","start":95,"end":163},{"id":"PF09011","name":"HMG-box domain","start":6,"end":78}],"gene3D":[{"start":81,"end":166,"id":"1.10.30.10","name":"High mobility group box domain","_id":"685af523b4ac24d5329d9159"},{"start":1,"end":80,"id":"1.10.30.10","name":"High mobility group box domain","_id":"685af523b4ac24d5329d915a"}]},"genes":[{"name":{"value":"HMGB1","evidences":[{"source":{"id":"HGNC:4983","name":"HGNC","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4983","_id":"685af523b4ac24d5329d917e"},"code":"ECO:0000312","_id":"685af523b4ac24d5329d917d"}],"_id":"685af523b4ac24d5329d917f"},"synonyms":[{"value":"HMG1","evidences":[],"_id":"685af523b4ac24d5329d9180"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d917c"}],"length":215,"name":"High mobility group protein B1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":11,"released":"2018_11","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI000012CA20","uniref100":"UniRef100_P09429","uniref50":"UniRef50_P09429","uniref90":"UniRef90_P09429","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-05-23T17:53:16.602Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":188,"end":214,"interaction_partner":[],"reference_html":"The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes. <i> Knapp S, Müller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. </i> Biochemistry, 2004","reference_id":"15379539","region_id":"DP01493r003","released":"2023_06","sample":[],"statement":[{"type":"Results","text":"As expected, the spectra indicated that T-peptide is a random coil whereas both ABbt and HMGB1 are predominantly α-helical.","_id":"685af523b4ac24d5329d9162"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":3,"_id":"685af523b4ac24d5329d9161","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-05-23T17:54:53.019Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005647","ec_name":"isothermal titration calorimetry evidence used in manual assertion","ec_ontology":"ECO","start":188,"end":214,"interaction_partner":[{"db":"UniProt","id":"P09429","operator":null,"partner_start":1,"partner_end":89,"_id":"685af523b4ac24d5329d9166"}],"reference_html":"The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes. <i> Knapp S, Müller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. </i> Biochemistry, 2004","reference_id":"15379539","region_id":"DP01493r005","released":"2023_06","sample":[],"statement":[{"type":"Results","text":"The association constant determined by isothermal titration calorimetry (ITC) of T-peptide with box A was (1.1 ± 0.14) × 105 M-1 (KD = 9 μM) (Figure 3, trace C). The ITC tracings are typical for a weak interaction. The stoichiometry is close to 1:1. The interaction at 293 K is favorable both enthalpically (ΔHobs = −2.6 ± 0.15 kcal/mol) and entropically (TΔSobs = 4.2 kcal/mol). The negative binding enthalpy suggests the existence of favorable polar interactions.","_id":"685af523b4ac24d5329d9167"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d9165","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-05-23T17:55:03.855Z","disprot_namespace":"Disorder function","ec_id":"ECO:0005647","ec_name":"isothermal titration calorimetry evidence used in manual assertion","ec_ontology":"ECO","start":188,"end":214,"interaction_partner":[],"reference_html":"The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes. <i> Knapp S, Müller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. </i> Biochemistry, 2004","reference_id":"15379539","region_id":"DP01493r006","released":"2023_06","sample":[],"statement":[{"type":"Results","text":"The association constant determined by isothermal titration calorimetry (ITC) of T-peptide with box A was (1.1 ± 0.14) × 105 M-1 (KD = 9 μM) (Figure 3, trace C). The ITC tracings are typical for a weak interaction. The stoichiometry is close to 1:1. The interaction at 293 K is favorable both enthalpically (ΔHobs = −2.6 ± 0.15 kcal/mol) and entropically (TΔSobs = 4.2 kcal/mol). The negative binding enthalpy suggests the existence of favorable polar interactions.","_id":"685af523b4ac24d5329d9169"}],"states_connection":[],"term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","term_ontology":"IDPO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d9168","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-05-23T17:56:50.719Z","disprot_namespace":"Disorder function","ec_id":"ECO:0006275","ec_name":"analytical ultracentrifugation evidence used in manual assertion","ec_ontology":"ECO","start":188,"end":214,"interaction_partner":[],"reference_html":"The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes. <i> Knapp S, Müller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. </i> Biochemistry, 2004","reference_id":"15379539","region_id":"DP01493r007","released":"2023_06","sample":[],"statement":[{"type":"Results","text":"Sedimentation equilibrium experiments confirmed that the complex between box A and the T-peptide has a mass of16 ± 2 kDa, compatible with the formation of a strong 1:1 complex (data not shown).","_id":"685af523b4ac24d5329d916b"}],"states_connection":[],"term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","term_ontology":"IDPO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d916a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-05-23T17:57:19.275Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006275","ec_name":"analytical ultracentrifugation evidence used in manual assertion","ec_ontology":"ECO","start":188,"end":214,"interaction_partner":[{"db":"UniProt","id":"P09429","operator":null,"partner_start":1,"partner_end":89,"_id":"685af523b4ac24d5329d916d"}],"reference_html":"The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes. <i> Knapp S, Müller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. </i> Biochemistry, 2004","reference_id":"15379539","region_id":"DP01493r008","released":"2023_06","sample":[],"statement":[{"type":"Results","text":"Sedimentation equilibrium experiments confirmed that the complex between box A and the T-peptide has a mass of16 ± 2 kDa, compatible with the formation of a strong 1:1 complex (data not shown).","_id":"685af523b4ac24d5329d916e"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d916c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-05-23T20:23:10.174Z","disprot_namespace":"Structural state","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":166,"end":214,"interaction_partner":[],"reference_html":"The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes. <i> Knapp S, Müller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. </i> Biochemistry, 2004","reference_id":"15379539","region_id":"DP01493r009","released":"2023_06","sample":[],"statement":[{"type":"Results","text":"The secondary structure of the amino acids belonging to the basic region downstream of box B was assessed using Cα secondary chemical shifts and 15N NOESY-HSQC experiment. Both methods indicate that this amino acid stretch is unstructured:  ΔCα chemical shifts are negative and the NOEs typical of α-helices and β-sheets are absent (data not shown).","_id":"685af523b4ac24d5329d9170"},{"type":"Results","text":"The residues in the acidic tail have typical random coil frequencies, with sharp and intense peaks. Individual tail residues could not be assigned:  the corresponding peaks are fewer than expected because of spectral overlap and exchange with the solvent.","_id":"685af523b4ac24d5329d9171"},{"type":"Figure","text":"HMG box A comprises approximately aa 4−80 (black), HMG box B aa 90−165 (dark gray), and the acidic tail aa 185−214 (gray). The linker between box A and box B is in white, and the basic stretch between box B and the tail is in light gray.","_id":"685af523b4ac24d5329d9172"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d916f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-05-23T20:28:03.786Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":188,"end":214,"interaction_partner":[{"db":"UniProt","id":"P09429","operator":null,"partner_start":1,"partner_end":175,"_id":"685af523b4ac24d5329d9174"}],"reference_html":"The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes. <i> Knapp S, Müller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. </i> Biochemistry, 2004","reference_id":"15379539","region_id":"DP01493r010","released":"2023_06","sample":[],"statement":[{"type":"Results","text":"Chemical shift differences were small, suggesting that the conformational changes of the ABbt fragment upon binding of the T-peptide are small. This facilitated residue assignment in the complex. Most chemical shift changes were a continuous and monotonic function of the amount of added T-peptide (up to a 1:4 protein:peptide ratio), indicative of a fast-exchange regime on the NMR time scale. However, at substoichiometric ratios we observed line broadenings for the peaks corresponding to T76, I78, and I158, indicative of an intermediate exchange regime. The residues showing the largest ΔCS are T76 and I78 in box A and N92, A93, I158, and R162 in box B, as shown in the lower part of Figure 4. Several nearby residues (Y70, R72, and K81 in box A and A163, K164, and G165 in box B) are also affected to a lower extent.","_id":"685af523b4ac24d5329d9175"},{"type":"Results","text":"The interaction of the T-peptide with box A reaches saturation at a stoichiometry of 3:1 (T-peptide:box A), whereas the interaction with box B does not reach saturation up to a 5-fold excess of T-peptide (data not shown). This result is in agreement with the ITC and thermostability data indicating that the interaction of the T-peptide with box B is much weaker than with box A.","_id":"685af523b4ac24d5329d9176"},{"type":"Curator statement","text":"Box A correspond to the 4-80 region and Box B to the 90-165 region of the protein.","_id":"685af523b4ac24d5329d9177"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d9173","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-05-23T20:27:49.266Z","disprot_namespace":"Disorder function","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":188,"end":214,"interaction_partner":[],"reference_html":"The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes. <i> Knapp S, Müller S, Digilio G, Bonaldi T, Bianchi ME, Musco G. </i> Biochemistry, 2004","reference_id":"15379539","region_id":"DP01493r011","released":"2023_06","sample":[],"statement":[{"type":"Results","text":"Chemical shift differences were small, suggesting that the conformational changes of the ABbt fragment upon binding of the T-peptide are small. This facilitated residue assignment in the complex. Most chemical shift changes were a continuous and monotonic function of the amount of added T-peptide (up to a 1:4 protein:peptide ratio), indicative of a fast-exchange regime on the NMR time scale. However, at substoichiometric ratios we observed line broadenings for the peaks corresponding to T76, I78, and I158, indicative of an intermediate exchange regime. The residues showing the largest ΔCS are T76 and I78 in box A and N92, A93, I158, and R162 in box B, as shown in the lower part of Figure 4. Several nearby residues (Y70, R72, and K81 in box A and A163, K164, and G165 in box B) are also affected to a lower extent.","_id":"685af523b4ac24d5329d9179"},{"type":"Results","text":"The interaction of the T-peptide with box A reaches saturation at a stoichiometry of 3:1 (T-peptide:box A), whereas the interaction with box B does not reach saturation up to a 5-fold excess of T-peptide (data not shown). This result is in agreement with the ITC and thermostability data indicating that the interaction of the T-peptide with box B is much weaker than with box A.","_id":"685af523b4ac24d5329d917a"},{"type":"Curator statement","text":"Box A correspond to the 4-80 region and Box B to the 90-165 region of the protein.","_id":"685af523b4ac24d5329d917b"}],"states_connection":[],"term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","term_ontology":"IDPO","unpublished":true,"version":0,"_id":"685af523b4ac24d5329d9178","reference_source":"pmid"}],"__v":0,"disorder_content":0.22790697674418606,"disprot_consensus":{"full":[{"start":166,"end":214,"type":"D"}],"Structural state":[{"start":166,"end":214,"type":"D"}],"Molecular function":[{"start":188,"end":214,"type":"F"}],"Disorder function":[{"start":188,"end":214,"type":"F"}]}},{"features":{"pfam":[{"id":"PF10477","name":"Nucleocytoplasmic shuttling protein for mRNA cap-binding EIF4E","start":427,"end":944}]},"uniref50":"UniRef50_Q9VMA3","sequence":"MQMAEAEQENGAGALKIATNAGATDRPAHQQLPLPVEDQQDEVLTPAEKGKFEYPPPPPPPTPVQAPLATKATALNASQEHDDDEANSEKWEDPCAPPPPPPLPTSAFLATGLGYLKLPAFKLKDALEKAITKLEANKRTLKASPESSRSIKNKNVVALEMLPRRSNPETIGDGSMLASTSTAVMLQTKKPAVIVEMERRCKIINLLAKQNQILESISGEAIPMHGPSKHLHEDEGLTLQVLSARASTPYTQPSSMLSCTAVSCDLEHDSPRKQVASKEAVPEQQSSQVQQKRPPSTGIHKPGSLRAPKAVRPTTAPVVSSKPVKSYTRSRLMDIRNGMFNALMHRSKESFVMPRIATCDDIELEGRLRRMNIWRTSDGTRFRTRSTTANLNMNNNNNNECMPAFFKNKNKPNLISDESIIQSQPPQPQTEFQDPAIVNQRRIGSGRLNHSKWGYNDEDYHSYHNGKSQHMEEVNSKNSKNMTVLQFFDNGEISSQPQRRPNTPVMGMSINRSENDTLHSNESSEDLSRANENYVKRVMSGFLVVSKPKSRDVEDRHHRRYRNQNEEPEWFSCGPTSRLDTIELCGFDEDEEKMLKEGNKNHGLGETERETSKQKMDHKYKWTHAEPMGRSKYMPKHDTNNNHNVENMNNVMATEHQQQKEEKRPGSGRSFQFDKFNQSQQNYESSSYVNHQQPPQTQPQQMQQQSNTNTNNSKFMSFFANEGNSSSSSLNEFFKQAINQGHGNNPEQPKSLGHIGQMPSVDQLEAKWRRNSLNNVGETANKQTDNFQKLIGSLSSAKPQSQAVGYDAISNFIMQQQQYQQQQQKQHLIIQQQQQHTAFLASLQLKAILGRADTQLLLLRLTKGEISKHGLLVQLANPRLTDMDREAITAVLQFTNTQQQQQQHKQQLDMLSSTVIASQLQNLHNLAIVQQTLAARQQPQHNPQTQAPHQLSQEDLQAHANVIMRNAVMKRKIEEQTSKLINGGAKHQAQQQYLNRGQQRQARPDANSNALLHALISGGGNNHASGYPMNGQPQKHHSNLRFGDNQNFQSFESNQPHFATQYKQQYQQSQQQHPHQQPQQLNSLHQNNAGAVNSFNKAQMQAQSAISMLPNSGDEFH","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_Q9VMA3","disprot_id":"DP01494","ncbi_taxon_id":7227,"regions_counter":2,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":361,"region_id":"DP01494r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of a minimal eIF4E-Cup complex reveals a general mechanism of eIF4E regulation in translational repression. <i> Kinkelin K, Veith K, Grünwald M, Bono F. </i> RNA, 2012","statement":[{"text":"Cup interacts with eIF4E as two short a-helices connected\nby a linker that is disordered in the structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":340,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4AXG"}],"reference_id":"22832024","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":361,"term_name":"flexible linker","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of a minimal eIF4E-Cup complex reveals a general mechanism of eIF4E regulation in translational repression. <i> Kinkelin K, Veith K, Grünwald M, Bono F. </i> RNA, 2012","statement":[{"text":"Cup interacts with eIF4E as two short a-helices connected\nby a linker that is disordered in the structure.","type":"Results"}],"term_id":"IDPO:0000033","curator_id":"eschad","start":340,"term_ontology":"IDPO","curator_name":"Eva Schad","reference_id":"22832024","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01494r002","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_Q9VMA3","date":"2018-07-23T13:47:08.000Z","acc":"Q9VMA3","name":"Protein cup","length":1117,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI0000075843","genes":[{"name":{"value":"cup"},"synonyms":[{"value":"fs(2)cup"}],"orfNames":[{"value":"CG11181"}]}],"alphafold_very_low_content":0.6463742166517458,"disorder_content":0.019695613249776187,"disprot_consensus":{"full":[{"start":340,"end":361,"type":"D"}],"Structural state":[{"start":340,"end":361,"type":"D"}],"Disorder function":[{"start":340,"end":361,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00520","name":"Ion transport protein","start":227,"end":488},{"id":"PF02214","name":"BTB/POZ domain","start":99,"end":189}],"gene3D":[{"start":197,"end":378,"id":"1.20.120.350","name":"Voltage-gated potassium channels. Chain C"},{"start":96,"end":196,"id":"3.30.710.10","name":"Potassium Channel Kv1.1; Chain A"},{"start":379,"end":489,"id":"1.10.287.70","name":"1.10.287.70"}]},"uniref50":"UniRef50_P08510","sequence":"MAAVAGLYGLGEDRQHRKKQQQQQQHQKEQLEQKEEQKKIAERKLQLREQQLQRNSLDGYGSLPKLSSQDEEGGAGHGFGGGPQHFEPIPHDHDFCERVVINVSGLRFETQLRTLNQFPDTLLGDPARRLRYFDPLRNEYFFDRSRPSFDAILYYYQSGGRLRRPVNVPLDVFSEEIKFYELGDQAINKFREDEGFIKEEERPLPDNEKQRKVWLLFEYPESSQAARVVAIISVFVILLSIVIFCLETLPEFKHYKVFNTTTNGTKIEEDEVPDITDPFFLIETLCIIWFTFELTVRFLACPNKLNFCRDVMNVIDIIAIIPYFITLATVVAEEEDTLNLPKAPVSPQDKSSNQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGRTLKASMRELGLLIFFLFIGVVLFSSAVYFAEAGSENSFFKSIPDAFWWAVVTMTTVGYGDMTPVGVWGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETDQEEMQSQNFNHVTSCPYLPGTLGQHMKKSSLSESSSDMMDLDDGVESTPGLTETHPGRSAVAPFLGAQQQQQQPVASSLSMSIDKQLQHPLQQLTQTQLYQQQQQQQQQQQNGFKQQQQQTQQQLQQQQSHTINASAAAATSGSGSSGLTMRHNNALAVSIETDV","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_P08510","disprot_id":"DP01495","ncbi_taxon_id":7227,"regions_counter":6,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":655,"region_id":"DP01495r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Intrinsic disorder in the C-terminal domain of the Shaker voltage-activated K+ channel modulates its interaction with scaffold proteins. <i> Magidovich E, Orr I, Fass D, Abdu U, Yifrach O. </i> Proc Natl Acad Sci U S A, 2007","statement":[{"text":"The 1H NMR spectrum of ShB-C lacks the chemical shift dispersion typical of folded proteins. Hence, our results suggest that the C-terminal portion of the Shaker channel is an intrinsically disordered random chain.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":513,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17666528","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":655,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Intrinsic disorder in the C-terminal domain of the Shaker voltage-activated K+ channel modulates its interaction with scaffold proteins. <i> Magidovich E, Orr I, Fass D, Abdu U, Yifrach O. </i> Proc Natl Acad Sci U S A, 2007","statement":[{"text":"His6-tagged ShB-C, immobilized on Ni2\u0003 beads via its N terminus, is able to capture PSD-95 from a crude soluble protein extract of transformed Drosophila Schneider cells.","type":"Results"}],"term_id":"GO:0005515","curator_id":"atantos","start":513,"term_ontology":"GO","curator_name":"Agnes Tantos","reference_id":"17666528","version":3,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01495r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":655,"region_id":"DP01495r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Intrinsic disorder in the C-terminal domain of the Shaker voltage-activated K+ channel modulates its interaction with scaffold proteins. <i> Magidovich E, Orr I, Fass D, Abdu U, Yifrach O. </i> Proc Natl Acad Sci U S A, 2007","statement":[{"text":"The far-UV CD spectrum for ShB-C lacked the typical signatures of secondary structure. ShB-C exhibited a negative peak at 200\nnm, indicative of a strong contribution from disordered structural elements, characteristic of a protein in a random coil\nconformation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":513,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17666528","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":655,"region_id":"DP01495r004","released":"2022_03","ec_id":"ECO:0007064","reference_html":"Intrinsic disorder in the C-terminal domain of the Shaker voltage-activated K+ channel modulates its interaction with scaffold proteins. <i> Magidovich E, Orr I, Fass D, Abdu U, Yifrach O. </i> Proc Natl Acad Sci U S A, 2007","statement":[{"text":"Thus, we conclude that ShB-C behaves as a random coil with very low compactness. Dynamic light\nscattering further supports this conclusion, yielding a Stokes radius of 37.2 Å.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":513,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"dynamic light scattering assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17666528","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":655,"region_id":"DP01495r005","released":"2022_03","ec_id":"ECO:0006206","reference_html":"Intrinsic disorder in the C-terminal domain of the Shaker voltage-activated K+ channel modulates its interaction with scaffold proteins. <i> Magidovich E, Orr I, Fass D, Abdu U, Yifrach O. </i> Proc Natl Acad Sci U S A, 2007","statement":[{"text":"CD spectrum in the near-UV range (250–330 nm) was devoid of any ellipticity (not shown), indicating the absence of\noriented aromatic residues typically present in the hydrophobic cores of compact globular proteins.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":513,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"near-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17666528","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":655,"region_id":"DP01495r006","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Intrinsic disorder in the C-terminal domain of the Shaker voltage-activated K+ channel modulates its interaction with scaffold proteins. <i> Magidovich E, Orr I, Fass D, Abdu U, Yifrach O. </i> Proc Natl Acad Sci U S A, 2007","statement":[{"text":"ShB-C migrates in a size-exclusion column unusually fast for a 15.9-kDa protein. Thus, we conclude that ShB-C\nbehaves as a random coil with very low compactness.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":513,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"chromatography evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17666528","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P08510","date":"2018-07-23T13:50:55.000Z","acc":"P08510","name":"Potassium voltage-gated channel protein Shaker","length":655,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI000016BB40","genes":[{"name":{"value":"Sh"},"synonyms":[{"value":"mns"}],"orfNames":[{"value":"CG12348"}]}],"alphafold_very_low_content":0.2198473282442748,"disorder_content":0.2183206106870229,"disprot_consensus":{"full":[{"start":513,"end":655,"type":"D"}],"Structural state":[{"start":513,"end":655,"type":"D"}],"Molecular function":[{"start":513,"end":655,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00467","name":"KOW motif","start":130,"end":159},{"id":"PF02357","name":"Transcription termination factor nusG","start":7,"end":112}],"gene3D":[{"start":124,"end":181,"id":"2.30.30.30","name":"2.30.30.30"},{"start":1,"end":123,"id":"3.30.70.940","name":"NusG, N-terminal domain"}]},"uniref50":"UniRef50_Q8ZAP0","sequence":"MSEAPKKRWYVVQAFSGFEGRVATSLREHIKLHNMEDLFGEVMVPTEEVVEIRGGQRRKSERKFFPGYVLVQMVMNDASWHLVRSVPRVMGFIGGTSDRPAPISDKEVDAIMNRLQQVGDKPRPKTLFEPGEMVRVNDGPFADFNGVVEEVDYEKSRLKVSVSIFGRATPVELDFSQVEKA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0AFG1","disprot_id":"DP01496","ncbi_taxon_id":83333,"regions_counter":3,"creator":"eschad","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":131,"region_id":"DP01496r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators. <i> Mooney RA, Schweimer K, Rösch P, Gottesman M, Landick R. </i> J Mol Biol, 2009","statement":[{"text":"In PMID: 20413501 the same group states in the supplementary material based on this work: NusG-CTD (132-181; green; PDB ID: 2JVV; (16)) is connected\nwith the NTD via a flexible linker region (117-131)","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":117,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2JVV"},{"db":"PDB","id":"2K06"}],"reference_id":"19500594","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":131,"term_name":"flexible linker","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators. <i> Mooney RA, Schweimer K, Rösch P, Gottesman M, Landick R. </i> J Mol Biol, 2009","statement":[{"text":"This\nobservation suggests that (1) EcNusG consists of at\nleast two domains that are connected via a flexible\nlinker.","type":"Results"}],"term_id":"IDPO:0000033","curator_id":"eschad","start":117,"term_ontology":"IDPO","curator_name":"Eva Schad","reference_id":"19500594","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01496r002","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":65,"region_id":"DP01496r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators. <i> Mooney RA, Schweimer K, Rösch P, Gottesman M, Landick R. </i> J Mol Biol, 2009","statement":[{"text":"The sequence region P45–F65 shows\nchemical shifts typical for unstructured residues and no medium- or long-range nuclear Overhauser\nenhancement cross signals for these residues were\nobserved, suggesting that this sequence region\nforms a highly flexible loop.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"eschad","start":45,"term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2K06"}],"reference_id":"19500594","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P0AFG1","date":"2018-07-23T14:08:38.000Z","acc":"P0AFG0","name":"Transcription termination/antitermination protein NusG","length":181,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI0000061478","genes":[{"name":{"value":"nusG","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00948","url":"https://hamap.expasy.org/unirule/MF_00948"}}]},"olnNames":[{"value":"b3982"},{"value":"JW3945"}]}],"alphafold_very_low_content":0.11049723756906077,"disorder_content":0.19889502762430938,"disprot_consensus":{"full":[{"start":45,"end":65,"type":"D"},{"start":117,"end":131,"type":"D"}],"Structural state":[{"start":45,"end":65,"type":"D"},{"start":117,"end":131,"type":"D"}],"Disorder function":[{"start":117,"end":131,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00135","name":"Carboxylesterase family","start":174,"end":695}],"gene3D":[{"start":135,"end":705,"id":"3.40.50.1820","name":"alpha/beta hydrolase"}]},"uniref50":"UniRef50_Q7KT70","sequence":"MMHKLKYRDKLKWLLALLVLIGTCFIQTRGQTRDPRFYSRPGVDYHWPNPGDPDYRTYTFNDRRYGHYQPNGYGANYPGRNPPGQYPQGMPNEDRFRFDPNDPNARTQFPGVLAGWREDLQGKQRRDSLTLERDVFVTTNYGQVQGFKVYMYDNPDPKSFYRPYHSTVDRVMGECSVFLGIPYALPPTFEGRFKPPRVHRGWQLLQAVDFGPACPQPVRYTGATKGIMDMDEDCLYLNVYSPKTGAGVAQKYPVMVYIHGGEFIRGASNLFQGHILASFYDVVVVTLNYRLGALGFLSTGDENSPGNYGILDQAMALRWVYDNIEFFNGDRNSITLFGPGAGGASAGLLMVAPQTRNIVRRVIAQSGSALADWALIQDKYRAQNTSRVLGQLLGCSIESSWKLVNCLRTGRSFYELGNAEFSPQVGSFPWGPVLDHNFTLPGDDWYEGWREKDWRFLTKTPETLIRAGKFNRNIQYMTGVTTQEAAFFVAQNESLSPYYELDGRFFDQKIREHVFRYNYTLNPNGVYEAIKYMYTFWPDPNNNTIIRDQYINMLSDLYYRAPVDQMVKLMLEQKVPVYMYVLNTTVEALNLPQWRKYPHDIERYFLTGAPFMDTEFFPKKEHLQRNMWTDNDRNMSHFFMQTYTNFARYGNPTPQQVLGMHFQRAYQGEIRYLNINTTYNSSILLNYRQTECAFWTQYLPTVIGVLVPTYPPTTEYWWEPKEPLQIAFWSMSVACFFLIVLVVICCIMWRNAKRQSDRFYDEDVFINGEGLEPEQDTRGVDNAHMVTNHHALRSRDNIYEYRDSPSTKTLASKAHTDTTSLRSPSSLAMTQKSSSQASLKSGISLKETNGHLVKQSERAATPRSQQNGSIAKVASPPVEEKRLLQPLSSTPVTQLQAEPAKRVPTAASVSGSSRSTTPVPSARSTTTHTTTATLSSQPAAQPRRTHLVEGVPQTSV","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_Q7KT70","disprot_id":"DP01497","ncbi_taxon_id":7227,"regions_counter":3,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":956,"region_id":"DP01497r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The intracellular domain of the Drosophila cholinesterase-like neural adhesion protein, gliotactin, is natively unfolded. <i> Zeev-Ben-Mordehai T, Rydberg EH, Solomon A, Toker L, Auld VJ, Silman I, Botti S, Sussman JL. </i> Proteins, 2003","statement":[{"text":"In the 1D 1H-NMR spectrum of Gli-cyt in H2O, the chemical shifts are in the narrow range between 0.8 and 8.5 ppm, demonstrating that Gli-cyt exists in solution as a mixture of rapidly equilibrating extended conformers.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":750,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"14579366","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":956,"region_id":"DP01497r002","released":"2022_03","ec_id":"ECO:0007680","reference_html":"The intracellular domain of the Drosophila cholinesterase-like neural adhesion protein, gliotactin, is natively unfolded. <i> Zeev-Ben-Mordehai T, Rydberg EH, Solomon A, Toker L, Auld VJ, Silman I, Botti S, Sussman JL. </i> Proteins, 2003","statement":[{"text":"The experimentally determined RST for Gli-cyt, 33.4 Å, is significantly larger than expected for either the native orMGstates. However, it is significantly lower than\nexpected for a random coil, suggesting that it may be in a PMG state.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":750,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"chromatography evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"14579366","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":956,"region_id":"DP01497r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The intracellular domain of the Drosophila cholinesterase-like neural adhesion protein, gliotactin, is natively unfolded. <i> Zeev-Ben-Mordehai T, Rydberg EH, Solomon A, Toker L, Auld VJ, Silman I, Botti S, Sussman JL. </i> Proteins, 2003","statement":[{"text":"The far-UV CD spectrum of Gli-cyt displays a maximum negative ellipticity at \u000b200 nm and a low ellipticity at 222 nm, which are indicative of a strong contribution from disordered structural elements.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":750,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"14579366","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9NK80","date":"2018-07-23T15:28:43.000Z","acc":"Q9NK80","name":"Gliotactin","length":956,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI00000074C5","genes":[{"name":{"value":"Gli","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAC41579.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAC41579.1"}},{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0001987","url":"http://flybase.org/reports/FBgn0001987.html"}}]},"orfNames":[{"value":"CG3903","evidences":[{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0001987","url":"http://flybase.org/reports/FBgn0001987.html"}}]}]}],"alphafold_very_low_content":0.3284518828451883,"disorder_content":0.21652719665271966,"disprot_consensus":{"full":[{"start":750,"end":956,"type":"D"}],"Structural state":[{"start":750,"end":956,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00957","name":"Synaptobrevin","start":52,"end":132}],"gene3D":[{"start":20,"end":137,"id":"1.20.5.110","name":"1.20.5.110"}]},"uniref50":"UniRef50_O70480","sequence":"MPPKFKRHLNDDDVTGSVKSERRNLLEDDSDEEEDFFLRGPSGPRFGPRNDKIKHVQNQVDEVIDVMQENITKVIERGERLDELQDKSESLSDNATAFSNRSKQLRRQMWWRGCKIKAIMALAAAILLLMIIILIVVKFRT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_O70480","disprot_id":"DP01498","ncbi_taxon_id":10090,"regions_counter":3,"creator":"bmesza","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":117,"region_id":"DP01498r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies. <i> Zwilling D, Cypionka A, Pohl WH, Fasshauer D, Walla PJ, Wahl MC, Jahn R. </i> EMBO J, 2007","statement":[{"text":"SNARE motifs are unstructured in solution, but assume a helical conformation when they interact with each other. Using circular dichroism (CD, 220 nm) spectroscopy, we therefore investigated which of the possible combinations of early endosomal SNARE motifs result in increases in α‐helicity. As expected for SNARE core complexes, combination of all four SNARE motifs resulted in a major increase of α‐helical content.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":47,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"pdb","id":"2nps"}],"reference_id":"17159904","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":117,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies. <i> Zwilling D, Cypionka A, Pohl WH, Fasshauer D, Walla PJ, Wahl MC, Jahn R. </i> EMBO J, 2007","statement":[{"text":"The crystal structure of the early endosomal SNARE complex (composed of syntaxin 13, vti1a, syntaxin 6, and VAMP4) was solved and refined at a resolution of 2.7 Å. The overall structure revealed that the SNARE complex forms a four‐helix bundle with a left‐handed superhelical twist.","type":"Results"}],"term_id":"GO:0005515","curator_id":"bmesza","start":47,"term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"17159904","version":3,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","cross_refs":[{"db":"pdb","id":"2nps"}],"region_id":"DP01498r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":117,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies. <i> Zwilling D, Cypionka A, Pohl WH, Fasshauer D, Walla PJ, Wahl MC, Jahn R. </i> EMBO J, 2007","statement":[{"text":"The combination of all four SNARE motifs (syntaxin 13, vti1a, syntaxin 6, and VAMP4) resulted in a major increase of α‐helical content.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"bmesza","start":47,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"17159904","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01498r003","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_O70480","date":"2018-07-23T17:43:37.000Z","acc":"O70480","name":"Vesicle-associated membrane protein 4","length":141,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000003F2F","genes":[{"name":{"value":"Vamp4"}}],"alphafold_very_low_content":0,"disorder_content":0.5035460992907801,"disprot_consensus":{"full":[{"start":47,"end":117,"type":"T"}],"Structural state":[{"start":47,"end":117,"type":"D"}],"Molecular function":[{"start":47,"end":117,"type":"F"}],"Structural transition":[{"start":47,"end":117,"type":"T"}]}},{"features":{"pfam":[{"id":"PF05008","name":"Vesicle transport v-SNARE protein N-terminus","start":1,"end":91},{"id":"PF12352","name":"Snare region anchored in the vesicle membrane C-terminus","start":130,"end":194}],"gene3D":[{"start":1,"end":99,"id":"1.20.58.400","name":"t-snare proteins"},{"start":119,"end":199,"id":"1.20.5.110","name":"1.20.5.110"}]},"uniref50":"UniRef50_Q9JI51","sequence":"MSADFEGYEQDFAVLTAEITSKISRVPRLPPDEKKQMVANVEKQLEEARELLEQMDLEVREIPPQSRGMYSNRMRSYKQEMGKLETDFKRSRIAYSDEVRNELLGDAGNSSENQLIKLREERAHLLDNTERLERSSRRLEAGYQIAVETEQIGQEMLENLSHDRERIQRARERLRETDANLGKSSRILTGMLRRIIQNRILLVILGIIVVITILTAITFFVRGH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_Q9JI51","disprot_id":"DP01499","ncbi_taxon_id":10116,"regions_counter":3,"creator":"bmesza","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":192,"region_id":"DP01499r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies. <i> Zwilling D, Cypionka A, Pohl WH, Fasshauer D, Walla PJ, Wahl MC, Jahn R. </i> EMBO J, 2007","statement":[{"text":"SNARE motifs are unstructured in solution, but assume a helical conformation when they interact with each other. Using circular dichroism (CD, 220 nm) spectroscopy, we therefore investigated which of the possible combinations of early endosomal SNARE motifs result in increases in α‐helicity. As expected for SNARE core complexes, combination of all four SNARE motifs resulted in a major increase of α‐helical content.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":115,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"pdb","id":"2nps"}],"reference_id":"17159904","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":192,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies. <i> Zwilling D, Cypionka A, Pohl WH, Fasshauer D, Walla PJ, Wahl MC, Jahn R. </i> EMBO J, 2007","statement":[{"text":"The crystal structure of the early endosomal SNARE complex (composed of syntaxin 13, vti1a, syntaxin 6, and VAMP4) was solved and refined at a resolution of 2.7 Å. The overall structure revealed that the SNARE complex forms a four‐helix bundle with a left‐handed superhelical twist.","type":"Results"}],"term_id":"GO:0005515","curator_id":"bmesza","start":115,"term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"17159904","version":3,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","cross_refs":[{"db":"pdb","id":"2nps"}],"region_id":"DP01499r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":192,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies. <i> Zwilling D, Cypionka A, Pohl WH, Fasshauer D, Walla PJ, Wahl MC, Jahn R. </i> EMBO J, 2007","statement":[{"text":"The combination of all four SNARE motifs (syntaxin 13, vti1a, syntaxin 6, and VAMP4) resulted in a major increase of α‐helical content.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"bmesza","start":115,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"17159904","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01499r003","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_Q9JI51","date":"2018-07-23T17:53:14.000Z","acc":"Q9JI51","name":"Vesicle transport through interaction with t-SNAREs homolog 1A","length":224,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI0000138E4C","genes":[{"name":{"value":"Vti1a"},"synonyms":[{"value":"Vti1l2"}]}],"alphafold_very_low_content":0.022321428571428572,"disorder_content":0.3482142857142857,"disprot_consensus":{"full":[{"start":115,"end":192,"type":"T"}],"Structural state":[{"start":115,"end":192,"type":"D"}],"Molecular function":[{"start":115,"end":192,"type":"F"}],"Structural transition":[{"start":115,"end":192,"type":"T"}]}},{"features":{"pfam":[{"id":"PF05739","name":"SNARE domain","start":165,"end":242},{"id":"PF09177","name":"Syntaxin 6/10/61, N-terminal","start":5,"end":103}],"gene3D":[{"start":1,"end":110,"id":"1.20.58.90","name":"1.20.58.90"},{"start":170,"end":234,"id":"1.20.5.110","name":"1.20.5.110"}]},"uniref50":"UniRef50_O43752","sequence":"MSMEDPFFVVKGEVQKAVNTAQGLFQRWTELLQDPSTATREEIDWTTNELRNNLRSIEWDLEDLDETISIVEANPRKFNLDATELSIRKAFITSTRQVVRDMKDQMSTSSVQALAERKNRQALLGDSGSQNWSTGTTDKYGRLDRELQRANSHFIEEQQAQQQLIVEQQDEQLELVSGSIGVLKNMSQRIGGELEEQAVMLEDFSHELESTQSRLDNVMKKLAKVSHMTSDRRQWCAIAILFAVLLVVLILFLVL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Pongo"],"uniref90":"UniRef90_O43752","disprot_id":"DP01500","ncbi_taxon_id":9601,"regions_counter":3,"creator":"bmesza","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":232,"region_id":"DP01500r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies. <i> Zwilling D, Cypionka A, Pohl WH, Fasshauer D, Walla PJ, Wahl MC, Jahn R. </i> EMBO J, 2007","statement":[{"text":"SNARE motifs are unstructured in solution, but assume a helical conformation when they interact with each other. Using circular dichroism (CD, 220 nm) spectroscopy, we therefore investigated which of the possible combinations of early endosomal SNARE motifs result in increases in α‐helicity. As expected for SNARE core complexes, combination of all four SNARE motifs resulted in a major increase of α‐helical content.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":169,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17159904","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":232,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies. <i> Zwilling D, Cypionka A, Pohl WH, Fasshauer D, Walla PJ, Wahl MC, Jahn R. </i> EMBO J, 2007","statement":[{"text":"The crystal structure of the early endosomal SNARE complex (composed of syntaxin 13, vti1a, syntaxin 6, and VAMP4) was solved and refined at a resolution of 2.7 Å. The overall structure revealed that the SNARE complex forms a four‐helix bundle with a left‐handed superhelical twist.","type":"Results"}],"term_id":"GO:0005515","curator_id":"bmesza","start":169,"term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"17159904","version":3,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","cross_refs":[{"db":"pdb","id":"2nps"}],"region_id":"DP01500r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":232,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies. <i> Zwilling D, Cypionka A, Pohl WH, Fasshauer D, Walla PJ, Wahl MC, Jahn R. </i> EMBO J, 2007","statement":[{"text":"The combination of all four SNARE motifs (syntaxin 13, vti1a, syntaxin 6, and VAMP4) resulted in a major increase of α‐helical content.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"bmesza","start":169,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"17159904","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01500r003","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_O43752","date":"2018-07-23T17:55:43.000Z","acc":"Q5R6Q2","name":"Syntaxin-6","length":255,"organism":"Pongo abelii","dataset":[],"UniParc":"UPI00000490D6","genes":[{"name":{"value":"STX6"}}],"alphafold_very_low_content":0.050980392156862744,"disorder_content":0.25098039215686274,"disprot_consensus":{"full":[{"start":169,"end":232,"type":"T"}],"Structural state":[{"start":169,"end":232,"type":"D"}],"Molecular function":[{"start":169,"end":232,"type":"F"}],"Structural transition":[{"start":169,"end":232,"type":"T"}]}},{"features":{"pfam":[{"id":"PF05739","name":"SNARE domain","start":180,"end":257},{"id":"PF14523","name":"Syntaxin-like protein","start":25,"end":161}],"gene3D":[{"start":166,"end":273,"id":"1.20.5.110","name":"1.20.5.110"},{"start":15,"end":140,"id":"1.20.58.70","name":"1.20.58.70"}]},"uniref50":"UniRef50_G3V7P1","sequence":"MSYGPLDMYRNPGPSGPQPRDFNSIIQTCSGNIQRISQATAQIKNLMSQLGTKQDSSKLQENLQQFQHSTNQLAKETNELLKELGSLPLPLSASEQRQQKLQKERLMNDFSSALNNFQVVQRKVSEKEKESIARARAGSRLSAEDRQREEQLVSFDSHEEWNQMQSQEEEAAITEQDLELIKERETAIQQLEADILDVNQIFKDLAMMIHDQGDLIDSIEANVESSEVHVERASDQLQRAAYYQKKSRKKMCILVLVLSVIVTVLVVVIWVASK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_G3V7P1","disprot_id":"DP01501","ncbi_taxon_id":10116,"regions_counter":3,"creator":"bmesza","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":250,"region_id":"DP01501r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies. <i> Zwilling D, Cypionka A, Pohl WH, Fasshauer D, Walla PJ, Wahl MC, Jahn R. </i> EMBO J, 2007","term_id":"IDPO:0000002","curator_id":"bmesza","start":182,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"pdb","id":"2nps"}],"reference_id":"17159904","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":250,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies. <i> Zwilling D, Cypionka A, Pohl WH, Fasshauer D, Walla PJ, Wahl MC, Jahn R. </i> EMBO J, 2007","statement":[{"text":"The crystal structure of the early endosomal SNARE complex (composed of syntaxin 13, vti1a, syntaxin 6, and VAMP4) was solved and refined at a resolution of 2.7 Å. The overall structure revealed that the SNARE complex forms a four‐helix bundle with a left‐handed superhelical twist.","type":"Results"}],"term_id":"GO:0005515","curator_id":"bmesza","start":182,"term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"17159904","version":3,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","cross_refs":[{"db":"pdb","id":"2nps"}],"region_id":"DP01501r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":250,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies. <i> Zwilling D, Cypionka A, Pohl WH, Fasshauer D, Walla PJ, Wahl MC, Jahn R. </i> EMBO J, 2007","statement":[{"text":"The combination of all four SNARE motifs (syntaxin 13, vti1a, syntaxin 6, and VAMP4) resulted in a major increase of α‐helical content.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"bmesza","start":182,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"17159904","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01501r003","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_G3V7P1","date":"2018-07-23T17:58:37.000Z","acc":"G3V7P1","name":"Syntaxin-12","length":274,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI000019BD5C","genes":[{"name":{"value":"Stx12"},"synonyms":[{"value":"Stx13"}]}],"alphafold_very_low_content":0.08029197080291971,"disorder_content":0.2518248175182482,"disprot_consensus":{"full":[{"start":182,"end":250,"type":"T"}],"Structural state":[{"start":182,"end":250,"type":"D"}],"Molecular function":[{"start":182,"end":250,"type":"F"}],"Structural transition":[{"start":182,"end":250,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00957","name":"Synaptobrevin","start":28,"end":107}],"gene3D":[{"start":2,"end":111,"id":"1.20.5.110","name":"1.20.5.110"}]},"uniref50":"UniRef50_P33328","sequence":"MSSSVPYDPYVPPEESNSGANPNSQNKTAALRQEIDDTVGIMRDNINKVAERGERLTSIEDKADNLAISAQGFKRGANRVRKQMWWKDLKMRMCLFLVVIILLVVIIVPIVVHFS","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P33328","disprot_id":"DP01502","ncbi_taxon_id":559292,"regions_counter":4,"creator":"bmesza","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":91,"region_id":"DP01502r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p. <i> Nicholson KL, Munson M, Miller RB, Filip TJ, Fairman R, Hughson FM. </i> Nat Struct Biol, 1998","statement":[{"text":"Snc2p appears to be unfolded as judged by CD spectroscopy and amide proton exchange experiments, in accord with previous reports for Snc2p homologs. Therefore, the SNARE regions that form binary and ternary complexes efficiently all seem, individually, to lack significant regular secondary structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":1,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"9731774","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":91,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p. <i> Nicholson KL, Munson M, Miller RB, Filip TJ, Fairman R, Hughson FM. </i> Nat Struct Biol, 1998","statement":[{"text":"The addition of Snc2p to Sso1CT–Sec9CT binary complexes resulted in a further large increase in α-helix content, to a total value of greater than 85%. The high helix content of the ternary complex suggests strongly that Snc2p folds to adopt an α-helical structure upon binding to the binary t-SNARE complex and that one or both t-SNAREs also adopt additional helical structure.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"bmesza","start":1,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"9731774","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01502r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":91,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p. <i> Nicholson KL, Munson M, Miller RB, Filip TJ, Fairman R, Hughson FM. </i> Nat Struct Biol, 1998","statement":[{"text":"The addition of Snc2p to Sso1CT–Sec9CT binary complexes resulted in a further large increase in α-helix content, to a total value of greater than 85%. The high helix content of the ternary complex suggests strongly that Snc2p folds to adopt an α-helical structure upon binding to the binary t-SNARE complex and that one or both t-SNAREs also adopt additional helical structure.","type":"Results"}],"term_id":"GO:0005515","curator_id":"bmesza","start":1,"term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"9731774","version":3,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01502r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":91,"region_id":"DP01502r004","reference_id":"9731774","start":1,"term_id":"GO:0060090","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Binary complexes form between the target membrane SNAREs Sso1p and Sec9p; these binary complexes can subsequently bind to the vesicle SNARE Snc2p to form ternary complexes.","type":"Abstract"},{"text":"Binary and ternary SNARE complex formation induces the folding of unstructured SNARE domains.","type":"Figure"},{"text":"Ternary complexes form upon addition of the cytoplasmic domain of the post-Golgi v-SNARE Snc2p (Fig. 1c), as has been seen for the functionally redundant (and 83% identical) Snc1p.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":4,"reference_html":"Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p. <i> Nicholson KL, Munson M, Miller RB, Filip TJ, Fairman R, Hughson FM. </i> Nat Struct Biol, 1998","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"molecular adaptor activity","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P33328","date":"2018-07-23T19:00:28.000Z","acc":"P33328","name":"Synaptobrevin homolog 2","length":115,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000168E3B","genes":[{"name":{"value":"SNC2"},"olnNames":[{"value":"YOR327C"}]}],"alphafold_very_low_content":0.017391304347826087,"disorder_content":0.7913043478260869,"disprot_consensus":{"full":[{"start":1,"end":91,"type":"T"}],"Structural state":[{"start":1,"end":91,"type":"D"}],"Structural transition":[{"start":1,"end":91,"type":"T"}],"Molecular function":[{"start":1,"end":91,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00804","name":"Syntaxin","start":33,"end":177},{"id":"PF05739","name":"SNARE domain","start":192,"end":269}],"gene3D":[{"start":30,"end":225,"id":"1.20.58.70","name":"1.20.58.70"}]},"uniref50":"UniRef50_P32867","sequence":"MSYNNPYQLETPFEESYELDEGSSAIGAEGHDFVGFMNKISQINRDLDKYDHTINQVDSLHKRLLTEVNEEQASHLRHSLDNFVAQATDLQFKLKNEIKSAQRDGIHDTNKQAQAENSRQRFLKLIQDYRIVDSNYKEENKEQAKRQYMIIQPEATEDEVEAAISDVGGQQIFSQALLNANRRGEAKTALAEVQARHQELLKLEKSMAELTQLFNDMEELVIEQQENVDVIDKNVEDAQLDVEQGVGHTDKAVKSARKARKNKIRCWLIVFAIIVVVVVVVVVPAVVKTR","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P32867","disprot_id":"DP01503","ncbi_taxon_id":559292,"regions_counter":3,"creator":"bmesza","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":265,"region_id":"DP01503r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p. <i> Nicholson KL, Munson M, Miller RB, Filip TJ, Fairman R, Hughson FM. </i> Nat Struct Biol, 1998","statement":[{"text":"Unlike Sso1p and Sso2p, which display CD spectra indicative of substantial (∼70%) α-helix content, Sso1CT and Sso2CT are largely unfolded. Therefore, the SNARE regions that form binary and ternary complexes efficiently all seem, individually, to lack significant regular secondary structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":192,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"9731774","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":265,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p. <i> Nicholson KL, Munson M, Miller RB, Filip TJ, Fairman R, Hughson FM. </i> Nat Struct Biol, 1998","statement":[{"text":"A dramatic acquisition of α-helical secondary structure accompanied the combination of Sso1CT and Sec9CT, with the final α-helix content of ∼60%. [...] The observed spectrum for Sso1CT–Sec9CT differs significantly from that anticipated for a non-interacting mixture, indicating that binary complex formation is coupled to significant folding of one or both of the largely-unstructured t-SNARE domains.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"bmesza","start":192,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"9731774","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01503r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":265,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p. <i> Nicholson KL, Munson M, Miller RB, Filip TJ, Fairman R, Hughson FM. </i> Nat Struct Biol, 1998","statement":[{"text":"A dramatic acquisition of α-helical secondary structure accompanied the combination of Sso1CT and Sec9CT, with the final α-helix content of ∼60%. [...] The observed spectrum for Sso1CT–Sec9CT differs significantly from that anticipated for a non-interacting mixture, indicating that binary complex formation is coupled to significant folding of one or both of the largely-unstructured t-SNARE domains.","type":"Results"}],"term_id":"GO:0005515","curator_id":"bmesza","start":192,"term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"9731774","version":3,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","cross_refs":[{"db":"PDB","id":"3b5n"}],"region_id":"DP01503r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P32867","date":"2018-07-23T19:01:54.000Z","acc":"P32867","name":"Protein SSO1","length":290,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000135FE3","genes":[{"name":{"value":"SSO1"},"orfNames":[{"value":"P1405"}],"olnNames":[{"value":"YPL232W"}]}],"alphafold_very_low_content":0.07241379310344828,"disorder_content":0.25517241379310346,"disprot_consensus":{"full":[{"start":192,"end":265,"type":"T"}],"Structural state":[{"start":192,"end":265,"type":"D"}],"Structural transition":[{"start":192,"end":265,"type":"T"}],"Molecular function":[{"start":192,"end":265,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00804","name":"Syntaxin","start":37,"end":181},{"id":"PF05739","name":"SNARE domain","start":196,"end":273}],"gene3D":[{"start":33,"end":225,"id":"1.20.58.70","name":"1.20.58.70"}]},"uniref50":"UniRef50_P39926","sequence":"MSNANPYENNNPYAENYEMQEDLNNAPTGHSDGSDDFVAFMNKINSINANLSRYENIINQIDAQHKDLLTQVSEEQEMELRRSLDDYISQATDLQYQLKADIKDAQRDGLHDSNKQAQAENCRQKFLKLIQDYRIIDSNYKEESKEQAKRQYTIIQPEATDEEVEAAINDVNGQQIFSQALLNANRRGEAKTALAEVQARHQELLKLEKTMAELTQLFNDMEELVIEQQENVDVIDKNVEDAQQDVEQGVGHTNKAVKSARKARKNKIRCLIICFIIFAIVVVVVVVPSVVETRK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P39926","disprot_id":"DP01504","ncbi_taxon_id":559292,"regions_counter":1,"creator":"bmesza","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":269,"region_id":"DP01504r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p. <i> Nicholson KL, Munson M, Miller RB, Filip TJ, Fairman R, Hughson FM. </i> Nat Struct Biol, 1998","statement":[{"text":"Unlike Sso1p and Sso2p, which display CD spectra indicative of substantial (∼70%) α-helix content, Sso1CT and Sso2CT are largely unfolded. Therefore, the SNARE regions that form binary and ternary complexes efficiently all seem, individually, to lack significant regular secondary structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":196,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"9731774","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P39926","date":"2018-07-23T19:05:58.000Z","acc":"P39926","name":"Protein SSO2","length":295,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000148B51","genes":[{"name":{"value":"SSO2"},"orfNames":[{"value":"YM8010.13C"}],"olnNames":[{"value":"YMR183C"}]}],"alphafold_very_low_content":0.10508474576271186,"disorder_content":0.25084745762711863,"disprot_consensus":{"full":[{"start":196,"end":269,"type":"D"}],"Structural state":[{"start":196,"end":269,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00043","name":"Glutathione S-transferase, C-terminal domain","start":100,"end":192},{"id":"PF02798","name":"Glutathione S-transferase, N-terminal domain","start":6,"end":77}],"gene3D":[{"start":82,"end":190,"id":"1.20.1050.10","name":"1.20.1050.10"},{"start":5,"end":211,"id":"3.40.30.10","name":"Glutaredoxin"}]},"uniref50":"UniRef50_P08263","sequence":"MAEKPKLHYFNARGRMESTRWLLAAAGVEFEEKFIKSAEDLDKLRNDGYLMFQQVPMVEIDGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYIEGIADLGEMILLLPVCPPEEKDAKLALIKEKIKNRYFPAFEKVLKSHGQDYLVGNKLSRADIHLVELLYYVEELDSSLISSFPLLKALKTRISNLPTVKKFLQPGSPRKPPMDEKSLEEARKIFRF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P08263","disprot_id":"DP01506","ncbi_taxon_id":9606,"regions_counter":3,"creator":"bhajdu","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":222,"region_id":"DP01506r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate. <i> Cameron AD, Sinning I, L'Hermite G, Olin B, Board PG, Mannervik B, Jones TA. </i> Structure, 1995","statement":[{"text":"The model included the full dimer with the exception of the C-terminal residues beyond Met208. The C-terminal helix has been omitted from the apo-structure due to the absence of any associated electron density.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"bhajdu","start":208,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1GSD"},{"db":"PDB","id":"1GSE"},{"db":"PDB","id":"1GSF"}],"reference_id":"8591048","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":222,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate. <i> Cameron AD, Sinning I, L'Hermite G, Olin B, Board PG, Mannervik B, Jones TA. </i> Structure, 1995","statement":[{"text":"It would appear, that the presence of a hydrophobic substrate, or possibly just glutathione, stabilizes the helix. ... It seems that the environment around Phe220 (which includes Tyr9, a residue of some importance to the catalytic mechanism) is critical in determining whether the helix is ordered or not.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"bhajdu","start":208,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","reference_id":"8591048","version":2,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01506r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":222,"term_name":"molecular function regulator","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate. <i> Cameron AD, Sinning I, L'Hermite G, Olin B, Board PG, Mannervik B, Jones TA. </i> Structure, 1995","statement":[{"text":"This helix, one edge of which is made up of hydrophobic residues, forms a lid over the H-site, providing a highly hydrophobic environment for the substrate, and has been shown to be important, though not essential, in catalysis.","type":"Results"}],"term_id":"GO:0098772","curator_id":"bhajdu","start":208,"term_ontology":"GO","curator_name":"Borbála Hajdu-Soltész","reference_id":"8591048","version":3,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01506r003","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P08263","date":"2018-07-24T07:42:46.000Z","acc":"P08263","name":"Glutathione S-transferase A1","length":222,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00001119C9","genes":[{"name":{"value":"GSTA1"}}],"alphafold_very_low_content":0,"disorder_content":0.06756756756756757,"disprot_consensus":{"full":[{"start":208,"end":222,"type":"T"}],"Structural state":[{"start":208,"end":222,"type":"D"}],"Structural transition":[{"start":208,"end":222,"type":"T"}],"Molecular function":[{"start":208,"end":222,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00169","name":"PH domain","start":7,"end":116}],"gene3D":[{"start":3,"end":132,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"}]},"uniref50":"UniRef50_Q9UQC2","sequence":"MSGGGDVVCTGWLRKSPPEKKLRRYAWKKRWFILRSGRMSGDPDVLEYYKNDHSKKPLRIINLNFCEQVDAGLTFNKKELQDSFVFDIKTSERTFYLVAETEEDMNKWVQSICQICGFNQAEESTDSLRNVSSAGHGPRSSPAELSSSSQHLLRERKSSAPSHSSQPTLFTFEPPVSNHMQPTLSTSAPQEYLYLHQCISRRAENARSASFSQGTRASFLMRSDTAVQKLAQGNGHCVNGISGQVHGFYSLPKPSRHNTEFRDSTYDLPRSLASHGHTKGSLTGSETDNEDVYTFKTPSNTLCREFGDLLVDNMDVPATPLSAYQIPRTFTLDKNHNAMTVATPGDSAIAPPPRPPKPSQAETPRWGSPQQRPPISENSRSVAATIPRRNTLPAMDNSRLHRASSCETYEYPQRGGESAGRSAESMSDGVGSFLPGKMIVGRSDSTNSEDNYVPMNPGSSTLLAMERAGDNSQSVYIPMSPGAHHFDSLGYPSTTLPVHRGPSRGSEIQPPPVNRNLKPDRKAKPTPLDLRNNTVIDELPFKSPITKSWSRANHTFNSSSSQYCRPISTQSITSTDSGDSEENYVPMQNPVSASPVPSGTNSPAPKKSTGSVDYLALDFQPSSPSPHRKPSTSSVTSDEKVDYVQVDKEKTQALQNTMQEWTDVRQSSEPSKGAKL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UQC2","disprot_id":"DP01507","ncbi_taxon_id":9606,"regions_counter":2,"creator":"tszani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":524,"region_id":"DP01507r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Conformational recognition of an intrinsically disordered protein. <i> Krieger JM, Fusco G, Lewitzky M, Simister PC, Marchant J, Camilloni C, Feller SM, De Simone A. </i> Biophys J, 2014","term_id":"IDPO:0000002","curator_id":"tszani","start":504,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24739176","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":524,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Conformational recognition of an intrinsically disordered protein. <i> Krieger JM, Fusco G, Lewitzky M, Simister PC, Marchant J, Camilloni C, Feller SM, De Simone A. </i> Biophys J, 2014","term_id":"GO:0005515","curator_id":"tszani","start":504,"term_ontology":"GO","curator_name":"Tamás Szaniszló","reference_id":"24739176","version":3,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01507r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q9UQC2","date":"2018-07-24T07:52:52.000Z","acc":"Q9UQC2","name":"GRB2-associated-binding protein 2","length":676,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000073037","genes":[{"name":{"value":"GAB2"},"synonyms":[{"value":"KIAA0571"}]}],"alphafold_very_low_content":0.6479289940828402,"disorder_content":0.03106508875739645,"disprot_consensus":{"full":[{"start":504,"end":524,"type":"D"}],"Structural state":[{"start":504,"end":524,"type":"D"}],"Molecular function":[{"start":504,"end":524,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":62,"end":320},{"id":"PF00069","name":"Protein kinase domain","start":418,"end":675},{"id":"PF00433","name":"Protein kinase C terminal domain","start":345,"end":381}],"gene3D":[{"start":455,"end":675,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"},{"start":60,"end":358,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":148,"end":342,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"},{"start":420,"end":491,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"}]},"uniref50":"UniRef50_Q15418","sequence":"MPLAQLKEPWPLMELVPLDPENGQTSGEEAGLQPSKDEGVLKEISITHHVKAGSEKADPSHFELLKVLGQGSFGKVFLVRKVTRPDSGHLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFVVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALGLDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEAIDHEKKAYSFCGTVEYMAPEVVNRQGHSHSADWWSYGVLMFEMLTGSLPFQGKDRKETMTLILKAKLGMPQFLSTEAQSLLRALFKRNPANRLGSGPDGAEEIKRHVFYSTIDWNKLYRREIKPPFKPAVAQPDDTFYFDTEFTSRTPKDSPGIPPSAGAHQLFRGFSFVATGLMEDDGKPRAPQAPLHSVVQQLHGKNLVFSDGYVVKETIGVGSYSECKRCVHKATNMEYAVKVIDKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKHVYLVTELMRGGELLDKILRQKFFSEREASFVLHTIGKTVEYLHSQGVVHRDLKPSNILYVDESGNPECLRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANGPSDTPEEILTRIGSGKFTLSGGNWNTVSETAKDLVSKMLHVDPHQRLTAKQVLQHPWVTQKDKLPQSQLSHQDLQLVKGAMAATYSALNSSKPTPQLKPIESSILAQRRVRKLPSTTL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q15418","disprot_id":"DP01508","ncbi_taxon_id":9606,"regions_counter":17,"creator":"bmesza","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":735,"region_id":"DP01508r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural Basis of Ribosomal S6 Kinase 1 (RSK1) Inhibition by S100B Protein: MODULATION OF THE EXTRACELLULAR SIGNAL-REGULATED KINASE (ERK) SIGNALING CASCADE IN A CALCIUM-DEPENDENT WAY. <i> Gógl G, Alexa A, Kiss B, Katona G, Kovács M, Bodor A, Reményi A, Nyitray L. </i> J Biol Chem, 2016","statement":[{"text":"Already the narrow signal dispersion of the HSQC spectrum of the RSK1(683–735) peptide informed us about the disordered nature of this free RSK1 tail fragment.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":683,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5CSF"}],"reference_id":"26527685","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-31T08:10:01.002Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":735,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural Basis of Ribosomal S6 Kinase 1 (RSK1) Inhibition by S100B Protein: MODULATION OF THE EXTRACELLULAR SIGNAL-REGULATED KINASE (ERK) SIGNALING CASCADE IN A CALCIUM-DEPENDENT WAY. <i> Gógl G, Alexa A, Kiss B, Katona G, Kovács M, Bodor A, Reményi A, Nyitray L. </i> J Biol Chem, 2016","statement":[{"text":"Overlay of the HSQC spectra of the free and S100B complexed 15N-labeled RSK1(683–735) peptide. Addition of excess S100B resulted in changes in the spectrum. As changes were monitored from the 15N RSK1 peptide side (S100B protein was unlabeled), the consequence of complex formation would be observable as shifted and broadened peaks and also peaks broadened below the detection limit in the HSQC spectrum.","type":"Results"}],"term_id":"GO:0005515","curator_id":"bmesza","start":683,"term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"26527685","version":3,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"5CSF"}],"region_id":"DP01508r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-31T08:10:11.529Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":735,"region_id":"DP01508r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structural Basis of Ribosomal S6 Kinase 1 (RSK1) Inhibition by S100B Protein: MODULATION OF THE EXTRACELLULAR SIGNAL-REGULATED KINASE (ERK) SIGNALING CASCADE IN A CALCIUM-DEPENDENT WAY. <i> Gógl G, Alexa A, Kiss B, Katona G, Kovács M, Bodor A, Reményi A, Nyitray L. </i> J Biol Chem, 2016","statement":[{"text":"Deconvolution of the difference spectra by the program BeStSel reveals an ∼13-amino acid-long single helix in the bound state of RSK1(683–735), while the free peptide is completely disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":683,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5CSF"}],"reference_id":"26527685","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-31T08:10:03.720Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":735,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Structural Basis of Ribosomal S6 Kinase 1 (RSK1) Inhibition by S100B Protein: MODULATION OF THE EXTRACELLULAR SIGNAL-REGULATED KINASE (ERK) SIGNALING CASCADE IN A CALCIUM-DEPENDENT WAY. <i> Gógl G, Alexa A, Kiss B, Katona G, Kovács M, Bodor A, Reményi A, Nyitray L. </i> J Biol Chem, 2016","statement":[{"text":"An increase in the helical content of RSK1(683-735) upon complex formation can be observed in the CD spectra without major changes in the S100B structure itself.","type":"Results"}],"term_id":"GO:0005515","curator_id":"bmesza","start":683,"term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"26527685","version":3,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","cross_refs":[{"db":"PDB","id":"5CSF"}],"region_id":"DP01508r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-31T08:10:13.676Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":727,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Protein-peptide complex crystallization: a case study on the ERK2 mitogen-activated protein kinase. <i> Gógl G, Törő I, Reményi A. </i> Acta Crystallogr D Biol Crystallogr, 2013","statement":[{"text":"PepRSK1 contains a reverse D-­motif from a downstream MAP kinase-activated protein kinase (MAPKAP) that is a known ERK2 substrate. The bound peptides (e.g. pepRSK1) were not involved in crystal packing in the new cocrystals. For flexible linear motifs this is more favourable in order to capture them in their physiologically relevant binding geometry.","type":"Results"}],"term_id":"GO:0005515","curator_id":"bmesza","start":712,"term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"23519423","version":3,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4h3p"}],"region_id":"DP01508r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-31T08:10:17.016Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":735,"region_id":"DP01508r007","reference_id":"29083550","start":730,"term_id":"GO:0030165","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Upon complex formation with the PDZ domain, the core interaction motif (the last five residues) became invisible in the NMR spectrum as a result of signal broadening confirming their central role in complex formation (Fig. 7C,D).","type":"Introduction"}],"curator_id":"vnugnes","released":"2025_12","term_ontology":"GO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":5,"reference_html":"Dynamic control of RSK complexes by phosphoswitch-based regulation. <i> Gógl G, Biri-Kovács B, Póti ÁL, Vadászi H, Szeder B, Bodor A, Schlosser G, Ács A, Turiák L, Buday L, Alexa A, Nyitray L, Reményi A. </i> FEBS J, 2018","date":"2025-11-24T17:39:01.806Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"PDZ domain binding","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a PDZ domain of a protein, a domain found in diverse signaling proteins.\" [GOC:go_curators, Pfam:PF00595]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q96QZ7","operator":null,"partner_start":455,"partner_end":558}]},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":735,"region_id":"DP01508r008","reference_id":"29083550","start":730,"term_id":"IDPO:0000045","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"Autophosphorylation, PDZ, and MAPK binding all target the 40‐residue‐long, disordered C‐terminal tail of RSK1","type":"Introduction"},{"text":"Ras‐ERK pathway activation influences RSK‐PDZ substrate interaction and activator MAP kinase binding by using an autoregulatory phosphoswitch located in the disordered RSK C‐terminal tail","type":"Introduction"},{"text":"Changes in the 1H-15N HSQC spectra of RSK1696–735 peptides confirmed that autophosphorylation by CTKD occurred only at Ser732 (Fig. 7A).","type":"Results"}],"curator_id":"vnugnes","released":"2025_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","version":4,"reference_html":"Dynamic control of RSK complexes by phosphoswitch-based regulation. <i> Gógl G, Biri-Kovács B, Póti ÁL, Vadászi H, Szeder B, Bodor A, Schlosser G, Ács A, Turiák L, Buday L, Alexa A, Nyitray L, Reményi A. </i> FEBS J, 2018","date":"2025-11-24T17:35:47.744Z","reference_source":"pmid","ec_id":"ECO:0005642","cross_refs":[{"db":"BMRB","id":"27214"}],"term_name":"phosphorylation display site","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":735,"region_id":"DP01508r009","reference_id":"29083550","start":696,"term_id":"IDPO:0000002","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"In the 15N-HSQC spectra of [15N] NCOA3 (1018–1088), the backbone amide resonances fall between 8.0 and 8.5 p.p.m. The lack of chemical shift dispersion reflect the intrinsic mobility of this region.","type":"Curator statement"}],"curator_id":"vnugnes","released":"2025_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","version":4,"reference_html":"Dynamic control of RSK complexes by phosphoswitch-based regulation. <i> Gógl G, Biri-Kovács B, Póti ÁL, Vadászi H, Szeder B, Bodor A, Schlosser G, Ács A, Turiák L, Buday L, Alexa A, Nyitray L, Reményi A. </i> FEBS J, 2018","date":"2025-11-24T18:04:43.084Z","reference_source":"pmid","ec_id":"ECO:0005642","cross_refs":[{"db":"BMRB","id":"27213"},{"db":"BMRB","id":"27214"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":709,"end":735,"reference_id":"22683790","reference_source":"pmid","reference_html":"Structural basis for the autoinhibition of the C-terminal kinase domain of human RSK1. <i> Li D, Fu TM, Nan J, Liu C, Li LF, Su XD. </i> Acta Crystallogr D Biol Crystallogr, 2012","date":"2025-11-24T16:38:03.472Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"PDB","id":"3RNY"}],"region_id":"DP01508r010","statement":[{"text":"This region lacks electron density in the X-ray structure, indicating it is disordered.","type":"Curator statement"}]},{"start":731,"end":735,"reference_id":"22683790","reference_source":"pmid","reference_html":"Structural basis for the autoinhibition of the C-terminal kinase domain of human RSK1. <i> Li D, Fu TM, Nan J, Liu C, Li LF, Su XD. </i> Acta Crystallogr D Biol Crystallogr, 2012","date":"2025-11-24T16:44:00.188Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001202","ec_ontology":"ECO","ec_name":"in vitro protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"region_id":"DP01508r011","statement":[{"text":"Here, Ser732 was the main phosphorylated site, but we could also detect both Thr733 and Thr734 phosphorylated peptides. These latter CTT autophosphorylation sites might be mutually exclusive because no double or triple phosphorylated peptides were observed.","type":"Curator statement"}]},{"start":577,"end":588,"reference_id":"22683790","reference_source":"pmid","reference_html":"Structural basis for the autoinhibition of the C-terminal kinase domain of human RSK1. <i> Li D, Fu TM, Nan J, Liu C, Li LF, Su XD. </i> Acta Crystallogr D Biol Crystallogr, 2012","date":"2025-11-24T16:56:32.614Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"PDB","id":"3RNY"}],"region_id":"DP01508r012","statement":[{"text":"Some loop regions, including part of the ‘activation loop’, are missing in our structure owing to poor electron density (Supplementary Table S1).","type":"Results"},{"text":"Additionally to the missing regions 578-583 and 577-585 in chain A and B (respectively, shown in table S1), the deposited data in PDB shows the residues 586, 587 and 588 also lack electron coordinates, so they are  considered as part of the IDR.","type":"Curator statement"}]},{"start":729,"end":735,"reference_id":"29083550","reference_source":"pmid","reference_html":"Dynamic control of RSK complexes by phosphoswitch-based regulation. <i> Gógl G, Biri-Kovács B, Póti ÁL, Vadászi H, Szeder B, Bodor A, Schlosser G, Ács A, Turiák L, Buday L, Alexa A, Nyitray L, Reményi A. </i> FEBS J, 2018","date":"2025-11-24T17:13:21.277Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0030165","term_name":"PDZ domain binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006303","ec_ontology":"ECO","ec_name":"microscale thermophoresis evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q96QZ7","operator":null,"partner_start":455,"partner_end":558}],"region_id":"DP01508r013","statement":[{"text":"Therefore, microscale thermophoresis (MST) was used and a ~ 20 μm interaction was detected (Fig. 3B). With competitive titration experiments, we could also show that phosphorylation at the major C-terminal autophosphorylation site (Ser732) does not influence the steady-state-binding affinity of the CTT peptide (729–735) to the second PDZ domain of MAGI-1 (Fig. 3C).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a PDZ domain of a protein, a domain found in diverse signaling proteins.\" [GOC:go_curators, Pfam:PF00595]","term_is_obsolete":false,"term_not_annotate":false},{"start":730,"end":735,"reference_id":"29083550","reference_source":"pmid","reference_html":"Dynamic control of RSK complexes by phosphoswitch-based regulation. <i> Gógl G, Biri-Kovács B, Póti ÁL, Vadászi H, Szeder B, Bodor A, Schlosser G, Ács A, Turiák L, Buday L, Alexa A, Nyitray L, Reményi A. </i> FEBS J, 2018","date":"2025-11-24T17:19:36.067Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0030165","term_name":"PDZ domain binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006303","ec_ontology":"ECO","ec_name":"microscale thermophoresis evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"PDB","id":"5N7G"},{"db":"PDB","id":"5N7D"},{"db":"PDB","id":"5N7F"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q96QZ7","operator":null,"partner_start":455,"partner_end":558}],"region_id":"DP01508r014","statement":[{"text":"As expected, the bound RSK1 peptide shows a canonical class I PDZ domain-binding mode (Fig. 5A) [29].","type":"Results"},{"text":"We also solved crystal structures with phosphorylated CTT peptides (pSer732) and captured the MAGI-1–pRSK1 (CTT) complex in two slightly different crystal forms (Fig. 5B).","type":"Results"},{"text":"In summary, the CTT phosphorylation at Ser732 is compatible with PDZ binding, while phosphorylation at Thr733 would very likely disrupt RSK1–PDZ (MAGI-1) binding due to steric hindrance within the binding pocket.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a PDZ domain of a protein, a domain found in diverse signaling proteins.\" [GOC:go_curators, Pfam:PF00595]","term_is_obsolete":false,"term_not_annotate":false},{"start":725,"end":729,"reference_id":"29083550","reference_source":"pmid","reference_html":"Dynamic control of RSK complexes by phosphoswitch-based regulation. <i> Gógl G, Biri-Kovács B, Póti ÁL, Vadászi H, Szeder B, Bodor A, Schlosser G, Ács A, Turiák L, Buday L, Alexa A, Nyitray L, Reményi A. </i> FEBS J, 2018","date":"2025-11-24T17:47:37.019Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000056","term_name":"self-interaction","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":732,"end":732,"position":"Specific residue"}],"region_id":"DP01508r015","statement":[{"text":"However, the endothermic nature of binding between the PDZ domain and the longer RSK1712–735 (or RSK1696–735) peptide suggests that some degree of disordered-to-order transition occurs in the CTT upon phosphorylation. ","type":"Results"},{"text":"In contrast, comparison of the measured ΔCp values of a longer peptide (RSK712–735) to that of the shorter RSK729–735 peptide and differences in this value caused by phosphorylation (Fig. 6B, table, rows 1–3) suggest that there are intramolecular interactions in the free phosphorylated form of the longer (RSK712–735) peptide, which are absent in the shorter phosphopeptide.","type":"Results"},{"text":"Conversely, based on the discrepancy between calculated and measured ΔCp values for the longer peptide, one can estimate the hydration of the intramolecularly shielded residues, which is 60–70 cal·mol−1·K−1 suggesting that it is a small intramolecular clamp, possibly involving residues N-terminal to Lys729.","type":"Results"},{"text":"In the case of the unphosphorylated peptide, such minor peaks can be assigned to Leu730 and Ser732, which are next to cis-Pro731. In contrast, a considerably longer minor fragment (between residues 728–735) became apparent in the NMR spectrum of the phosphorylated peptide (Fig. 7F). This region showed large beta propensity based on SCS values.","type":"Results"},{"text":"Overall, this NMR data indicated significant chemical shift changes for residues of the charged motif (Arg725, Arg726, Arg728, and Lys729). Pro731 undergoes cis-trans isomerization and the chemical shift differences for Lys729 and Arg728 are more prominent in the cis-Pro peptide, suggesting the existence of a more pronounced charge clamp specifically involving these latter two residues.","type":"Results"},{"text":"Here, the phosphorylation triggers a transient local fold that can result in slowed-down conformational kinetics [43]. Similar intramolecular charge clamps have already been shown in some cases [44-46]; however, the RSK1 CTT phosphoswitch appears to be the first clear case where it acts as a modulator on the assembly of a signaling complex.","type":"Discussion"}]},{"start":725,"end":732,"reference_id":"29083550","reference_source":"pmid","reference_html":"Dynamic control of RSK complexes by phosphoswitch-based regulation. <i> Gógl G, Biri-Kovács B, Póti ÁL, Vadászi H, Szeder B, Bodor A, Schlosser G, Ács A, Turiák L, Buday L, Alexa A, Nyitray L, Reményi A. </i> FEBS J, 2018","date":"2025-11-24T17:53:43.058Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000057","term_name":"self-regulatory activity","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":732,"end":732,"position":"Specific residue"}],"region_id":"DP01508r016","statement":[{"text":"Experimental evidence for the intramolecular charge clamp in phosphorylated CTT","type":"Results"},{"text":"Interestingly, ERK2-binding affinity to the RSK1 peptide decreased five-fold (from 0.2 μm to 1 μm) when the peptide was phosphorylated at Ser732 (Fig. 3D).","type":"Results"},{"text":"This intramolecular charge clamp would prevent the formation of a presumably transient interaction between the CTT and ERK2 and will lead to weakened binding [11].","type":"Results"},{"text":"Interestingly, phosphorylation of Ser732 participates in the formation of a charged clamp, which affects ERK–RSK binding.","type":"Discussion"},{"text":"Here, the phosphorylation triggers a transient local fold that can result in slowed-down conformational kinetics [43]. Similar intramolecular charge clamps have already been shown in some cases [44-46]; however, the RSK1 CTT phosphoswitch appears to be the first clear case where it acts as a modulator on the assembly of a signaling complex.","type":"Discussion"},{"text":"The observed independent localization trends of activated ERK and activated RSK (Fig. 11D) and the charge clamp-based dissociation promoting effect of RSK1 CTT (Fig. 10F) can synergistically contribute to the periodicity and the amplitude of macroscopically observed pERK dissociation patterns.","type":"Discussion"}]},{"start":712,"end":726,"reference_id":"23519423","reference_source":"pmid","reference_html":"Protein-peptide complex crystallization: a case study on the ERK2 mitogen-activated protein kinase. <i> Gógl G, Törő I, Reményi A. </i> Acta Crystallogr D Biol Crystallogr, 2013","date":"2025-11-24T18:22:10.355Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051019","term_name":"mitogen-activated protein kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"ELM","id":"DOC_MAPK_gen_1"},{"db":"PDB","id":"4H3P"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P28482","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01508r017","statement":[{"text":"PepRSK1 contains a reverse D-­motif from a downstream MAP kinase-activated protein kinase (MAPKAP) that is a known ERK2 substrate (RSK1; Garai et al., 2012","type":"Results"}],"term_comment":"","term_def":"\"Binding to a mitogen-activated protein kinase.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_Q15418","date":"2018-07-24T08:25:25.000Z","acc":"Q15418","name":"Ribosomal protein S6 kinase alpha-1","length":735,"organism":"Homo sapiens","dataset":["Stress response proteins"],"UniParc":"UPI0000035BE4","genes":[{"name":{"value":"RPS6KA1"},"synonyms":[{"value":"MAPKAPK1A"},{"value":"RSK1"}]}],"alphafold_very_low_content":0.17006802721088435,"disorder_content":0.08843537414965986,"disprot_consensus":{"full":[{"start":577,"end":588,"type":"D"},{"start":683,"end":735,"type":"D"}],"Structural state":[{"start":577,"end":588,"type":"D"},{"start":683,"end":735,"type":"D"}],"Molecular function":[{"start":683,"end":735,"type":"F"}],"Disorder function":[{"start":725,"end":735,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03621","name":"MbtH-like protein","start":3,"end":68}],"gene3D":[{"start":1,"end":71,"id":"3.90.820.10","name":"Structural Genomics, Unknown Function 30-nov-00 1gh9 Mol_id"}]},"uniref50":"UniRef50_P9WIP5","sequence":"MSTNPFDDDNGAFFVLVNDEDQHSLWPVFADIPAGWRVVHGEASRAACLDYVEKNWTDLRPKSLRDAMVED","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"uniref90":"UniRef90_P9WIP5","disprot_id":"DP01509","ncbi_taxon_id":83332,"regions_counter":3,"creator":"bhajdu","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":71,"region_id":"DP01509r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of Rv2377c-founding member of the MbtH-like protein family. <i> Buchko GW, Kim CY, Terwilliger TC, Myler PJ. </i> Tuberculosis (Edinb), 2010","statement":[{"text":"Aside from K62, amide cross peaks are absent from W56 to D71 suggesting that the C-terminal region is unstructured in solution.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bhajdu","start":56,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2KHR"},{"db":"BMRB","id":"16253"}],"reference_id":"20434955","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-29T13:12:07.721Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":12,"region_id":"DP01509r002","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Solution structure of Rv2377c-founding member of the MbtH-like protein family. <i> Buchko GW, Kim CY, Terwilliger TC, Myler PJ. </i> Tuberculosis (Edinb), 2010","statement":[{"text":"Because both the N- and C-terminal regions are disordered, G1* - A12 and W56 - D71, respectively, most of these regions have been removed from the Figure for clarity.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-29T13:15:14.417Z","reference_source":"pmid","term_name":"disorder","reference_id":"20434955","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"GSHMSTNPFDDDNGAFFVLVNDEDQHSLWPVFADIPAGWRVVHGEASRAACLDYVEKNWTDLRPKSLRDAMVED"}],"released":"2018_11","uniref100":"UniRef100_P9WIP5","date":"2018-07-24T10:09:30.000Z","acc":"P9WIP5","name":"Protein MbtH","length":71,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","dataset":[],"UniParc":"UPI000012ED46","genes":[{"name":{"value":"mbtH"},"orfNames":[{"value":"MTCY27.03"}],"olnNames":[{"value":"Rv2377c"}]}],"alphafold_very_low_content":0.014084507042253521,"disorder_content":0.39436619718309857,"disprot_consensus":{"full":[{"start":1,"end":12,"type":"D"},{"start":56,"end":71,"type":"D"}],"Structural state":[{"start":1,"end":12,"type":"D"},{"start":56,"end":71,"type":"D"}]}},{"features":{"pfam":[{"id":"PF16777","name":"Transcriptional regulator, RHH-like, CopG","start":1,"end":73}],"gene3D":[{"start":39,"end":73,"id":"1.10.1220.10","name":"Met repressor-like"}]},"uniref50":"UniRef50_I0EUL9","sequence":"MEKTENTDETRLRGTKNKLGRKPKADANKKTRAVSLYFSDEQYQKLEKMANEEEESVGSYIKRYILKALRKIE","taxonomy":["Bacteria","Proteobacteria","Epsilonproteobacteria","Campylobacterales","Helicobacteraceae","Helicobacter"],"uniref90":"UniRef90_E8QUN1","disprot_id":"DP01510","ncbi_taxon_id":85962,"regions_counter":2,"creator":"bmesza","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":30,"region_id":"DP01510r001","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Helicobacter pylori protein HP0222 belongs to Arc/MetJ family of transcriptional regulators. <i> Popescu A, Karpay A, Israel DA, Peek RM, Krezel AM. </i> Proteins, 2005","statement":[{"text":"In gel filtration experiments, the HP0222 migrated as a molecule with a molecular mass of approximately 35 kD, and the HP0222str migrated as a 13 kDa molecule. The larger‐than‐expected apparent size of HP0222 in the above experiments was the result of the 42‐residue‐long (12 residue His‐tag and the first 30 residues of HP0222) unstructured N‐terminal sequences.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":1,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"chromatography evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"15723352","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":30,"region_id":"DP01510r002","released":"2022_03","ec_id":"ECO:0007064","reference_html":"Helicobacter pylori protein HP0222 belongs to Arc/MetJ family of transcriptional regulators. <i> Popescu A, Karpay A, Israel DA, Peek RM, Krezel AM. </i> Proteins, 2005","statement":[{"text":"Light scattering experiments on HP0222 indicated molecular size of approximately 40 kDa. The larger‐than‐expected apparent size of HP0222 in the above experiments was the result of the 42‐residue‐long (12 residue His‐tag and the first 30 residues of HP0222) unstructured N‐terminal sequences.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":1,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"dynamic light scattering assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"15723352","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_A0A238GTW9","date":"2018-07-24T11:24:59.000Z","acc":"O25010","name":"Uncharacterized protein","length":73,"organism":"Helicobacter pylori (strain ATCC 700392 / 26695)","dataset":[],"UniParc":"UPI00000C0805","genes":[{"olnNames":[{"value":"HP_0222","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAD07296.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD07296.1"}}]}]}],"alphafold_very_low_content":0.0684931506849315,"disorder_content":0.410958904109589,"disprot_consensus":{"full":[{"start":1,"end":30,"type":"D"}],"Structural state":[{"start":1,"end":30,"type":"D"}]}},{"features":{"pfam":[{"id":"PF11610","name":"Scaffold protein Ste5, Fus3-binding domain","start":276,"end":368},{"id":"PF12194","name":"Ste5, vWA domain","start":594,"end":782},{"id":"PF31261","name":"STE5, PH domain","start":375,"end":523},{"id":"PF31262","name":"Ste5, vWA N-terminal extension domain","start":542,"end":593},{"id":"PF31263","name":"Ste5, RING-type zinc finger","start":193,"end":263}],"gene3D":[{"start":591,"end":786,"id":"3.40.50.11070","name":"Protein Ste5, Fus3-binding domain"}]},"uniref50":"UniRef50_P32917","sequence":"MMETPTDNIVSPFHNFGSSTQYSGTLSRTPNQIIELEKPSTLSPLSRGKKWTEKLARFQRSSAKKKRFSPSPISSSTFSFSPKSRVTSSNSSGNEDGNLMNTPSTVSTDYLPQHPHRTSSLPRPNSNLFHASNSNLSRANEPPRAENLSDNIPPKVAPFGYPIQRTSIKKSFLNASCTLCDEPISNRRKGEKIIELACGHLSHQECLIISFGTTSKADVRALFPFCTKCKKDTNKAVQCIPENDELKDILISDFLIHKIPDSELSITPQSRFPPYSPLLPPFGLSYTPVERQTIYSQAPSLNPNLILAAPPKERNQIPQKKSNYTFLHSPLGHRRIPSGANSILADTSVALSANDSISAVSNSVRAKDDETKTTLPLLRSYFIQILLNNFQEELQDWRIDGDYGLLRLVDKLMISKDGQRYIQCWCFLFEDAFVIAEVDNDVDVLEIRLKNLEVFTPIANLRMTTLEASVLKCTLNKQHCADLSDLYIVQNINSDESTTVQKWISGILNQDFVFNEDNITSTLPILPIIKNFSKDVGNGRHETSTFLGLINPNKVVEVGNVHDNDTVIIRRGFTLNSGECSRQSTVDSIQSVLTTISSILSLKREKPDNLAIILQIDFTKLKEEDSLIVVYNSLKALTIKFARLQFCFVDRNNYVLDYGSVLHKIDSLDSISNLKSKSSSTQFSPIWLKNTLYPENIHEHLGIVAVSNSNMEAKKSILFQDYRCFTSFGRRRPNELKIKVGYLNVDYSDKIDELVEASSWTFVLETLCYSFGLSFDEHDDDDEEDNDDSTDNELDNSSGSLSDAESTTTIHIDSPFDNENATANMVNDRNLLTEGEHSNIENLETVASSVQPALIPNIRFSLHSEEEGTNENENENDMPVLLLSDMDKGIDGITRRSSFSSLIESGNNNCPLHMDYI","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P32917","disprot_id":"DP01511","ncbi_taxon_id":559292,"regions_counter":4,"creator":"bhajdu","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":238,"region_id":"DP01511r001","released":"2023_12","ec_id":"ECO:0006165","reference_html":"The RING domain of the scaffold protein Ste5 adopts a molten globular character with high thermal and chemical stability. <i> Walczak MJ, Samatanga B, van Drogen F, Peter M, Jelesarov I, Wider G. </i> Angew Chem Int Ed Engl, 2014","statement":[{"text":" First, we measured a two-dimensional (2D) 1H-15N heteronuclear correlation (HSQC) spectrum of scSte5 RH2 in the same standard conditions as in the DSC experiments above. The broad signals, indicating exchange between several conformations and the small chemical shift dispersion (Figure 2 a), are typical for a molten globule.","type":"Article"}],"term_id":"IDPO:0000003","curator_id":"vnugnes","start":149,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-29T13:34:43.073Z","reference_source":"pmid","term_name":"molten globule","reference_id":"24356903","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"GPSDNIPPKVAPFGYPIQRTSIKKSFLNASCTLCDEPISNRRKGEKIIELACGHLSHQECLIISFGTTSKADVRALFPFCTKCKKDTNKAVQ"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":238,"term_name":"molten globule to order","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The RING domain of the scaffold protein Ste5 adopts a molten globular character with high thermal and chemical stability. <i> Walczak MJ, Samatanga B, van Drogen F, Peter M, Jelesarov I, Wider G. </i> Angew Chem Int Ed Engl, 2014","statement":[{"text":"Binding was monitored by [1H,15N]-HSQC NMR spectroscopy, both with and without the addition of G protein subunits β/γ. Upon interaction with the binding partners, scSte5 RH2 underwent a dramatic conformational rearrangement (Figure S5). The resonances became more dispersed and narrower in linewidth. These changes provide evidence that, upon interaction with the Ste4/Ste18 heterodimer, the active form of scSte5 RH2 escapes the molten globule state at least partially and adopts a better-defined and less-dynamic structure.","type":"Article"}],"term_id":"IDPO:0000012","curator_id":"vnugnes","start":149,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24356903","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-29T13:39:04.882Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01511r002","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06701"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P18851"}],"sequence_construct":"GPSDNIPPKVAPFGYPIQRTSIKKSFLNASCTLCDEPISNRRKGEKIIELACGHLSHQECLIISFGTTSKADVRALFPFCTKCKKDTNKAVQ"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":238,"term_name":"protein binding","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The RING domain of the scaffold protein Ste5 adopts a molten globular character with high thermal and chemical stability. <i> Walczak MJ, Samatanga B, van Drogen F, Peter M, Jelesarov I, Wider G. </i> Angew Chem Int Ed Engl, 2014","statement":[{"text":"Binding was monitored by [1H,15N]-HSQC NMR spectroscopy, both with and without the addition of G protein subunits β/γ. Upon interaction with the binding partners, scSte5 RH2 underwent a dramatic conformational rearrangement (Figure S5). The resonances became more dispersed and narrower in linewidth. These changes provide evidence that, upon interaction with the Ste4/Ste18 heterodimer, the active form of scSte5 RH2 escapes the molten globule state at least partially and adopts a better-defined and less-dynamic structure.","type":"Article"}],"term_id":"GO:0005515","curator_id":"vnugnes","start":149,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"24356903","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-29T13:39:43.915Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01511r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P18851","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P06701","operator":"and","partner_start":null,"partner_end":null}],"sequence_construct":"GPSDNIPPKVAPFGYPIQRTSIKKSFLNASCTLCDEPISNRRKGEKIIELACGHLSHQECLIISFGTTSKADVRALFPFCTKCKKDTNKAVQ"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":238,"region_id":"DP01511r004","released":"2023_12","ec_id":"ECO:0006230","reference_html":"The RING domain of the scaffold protein Ste5 adopts a molten globular character with high thermal and chemical stability. <i> Walczak MJ, Samatanga B, van Drogen F, Peter M, Jelesarov I, Wider G. </i> Angew Chem Int Ed Engl, 2014","statement":[{"text":"Thus, the diffuse non-cooperative nature of the scSte5 RH2 melting transition indicates a heterogeneous ensemble of conformations that are characteristic for a molten globule state, which has been previously observed in other domains.","type":"Article"}],"term_id":"IDPO:0000003","curator_id":"vnugnes","start":149,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"heat capacity-based evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-29T13:34:18.959Z","reference_source":"pmid","term_name":"molten globule","reference_id":"24356903","ec_go":"IDA","disprot_namespace":"Structural state","sequence_construct":"GPSDNIPPKVAPFGYPIQRTSIKKSFLNASCTLCDEPISNRRKGEKIIELACGHLSHQECLIISFGTTSKADVRALFPFCTKCKKDTNKAVQ"}],"released":"2018_11","uniref100":"UniRef100_P32917","date":"2018-07-24T11:37:47.000Z","acc":"P32917","name":"Protein STE5","length":917,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000168E65","genes":[{"name":{"value":"STE5"},"synonyms":[{"value":"NUL3"}],"orfNames":[{"value":"YD8557.12"}],"olnNames":[{"value":"YDR103W"}]}],"alphafold_very_low_content":0.47110141766630315,"disorder_content":0.09814612868047982,"disprot_consensus":{"full":[{"start":149,"end":238,"type":"T"}],"Structural state":[{"start":149,"end":238,"type":"D"}],"Structural transition":[{"start":149,"end":238,"type":"T"}],"Molecular function":[{"start":149,"end":238,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03869","name":"Arc-like DNA binding domain","start":4,"end":53}],"gene3D":[{"start":1,"end":53,"id":"1.10.1220.10","name":"Met repressor-like"}]},"uniref50":"UniRef50_P03050","sequence":"MKGMSKMPQFNLRWPREVLDLVRKVAEENGRSVNSEIYQRVMESFKKEGRIGA","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Uroviricota","Caudoviricetes","Caudovirales","Podoviridae","Lederbergvirus"],"uniref90":"UniRef90_P03050","disprot_id":"DP01512","ncbi_taxon_id":10754,"regions_counter":4,"creator":"viglesias","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":53,"region_id":"DP01512r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"P22 Arc repressor: folding kinetics of a single-domain, dimeric protein. <i> Milla ME, Sauer RT. </i> Biochemistry, 1994","statement":[{"text":"At pH 2, 20 °C, and a protein concentration of 64 µ , Arc is unfolded by the following criteria: (i) the circular dichroism spectrum shows very little secondary structure and increased random coil content compared with native Arc (Figure 1A); (ii) the fluorescence spectrum of the single tryptophan at position 14 is red shifted and shows reduced intensity compared to native Arc (Figure IB); and (iii) the protein behaves as a monomer in sedimentation equilibrium experiments (av Mw 5560), whereas native Arc is a dimer (av Afw 12 346) (Figure 1C).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"8110744","conditions":[{"term_name":"pH","term_id":"NCIT:C45997","unit_name":"pH","unit_id":"UO:0000196","value":2,"deviation":null,"statements":[]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-12-10T15:15:49.076Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":53,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"P22 Arc repressor: folding kinetics of a single-domain, dimeric protein. <i> Milla ME, Sauer RT. </i> Biochemistry, 1994","statement":[{"text":"In the structure of the globular Arc dimer, each monomer is interwound with the other, forming a single folded domain with a conventional hydrophobic core.","type":"Results"}],"term_id":"GO:0005515","curator_id":"bmesza","start":1,"term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"8110744","version":3,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","cross_refs":[{"db":"PDB","id":"1ARQ"}],"region_id":"DP01512r002","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-12-10T15:15:43.586Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":53,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"P22 Arc repressor: folding kinetics of a single-domain, dimeric protein. <i> Milla ME, Sauer RT. </i> Biochemistry, 1994","statement":[{"text":"In the structure of the globular Arc dimer, each monomer is interwound with the other, forming a single folded domain with a conventional hydrophobic core.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"bmesza","start":1,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"8110744","version":2,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01512r003","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-12-10T15:15:44.491Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":1,"end":53,"reference_id":"8110744","reference_source":"pmid","reference_html":"P22 Arc repressor: folding kinetics of a single-domain, dimeric protein. <i> Milla ME, Sauer RT. </i> Biochemistry, 1994","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"conditions":[{"term_name":"pH","term_id":"NCIT:C45997","unit_name":"pH","unit_id":"UO:0000196","value":2,"deviation":null,"statements":[]}],"region_id":"DP01512r004","statement":[{"text":"At pH 2, 20 °C, and a protein concentration of 64 µ , Arc is unfolded by the following criteria: (i) the circular dichroism spectrum shows very little secondary structure and increased random coil content compared with native Arc (Figure 1A); (ii) the fluorescence spectrum of the single tryptophan at position 14 is red shifted and shows reduced intensity compared to native Arc (Figure IB); and (iii) the protein behaves as a monomer in sedimentation equilibrium experiments (av Mw 5560), whereas native Arc is a dimer (av Afw 12 346) (Figure 1C).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-12-10T15:15:45.602Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P03050","date":"2018-07-24T12:08:57.000Z","acc":"P03050","name":"Transcriptional repressor arc","length":53,"organism":"Salmonella phage P22","dataset":["Viral proteins"],"UniParc":"UPI0000003A79","genes":[{"name":{"value":"arc"}}],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":53,"type":"T"}],"Structural state":[{"start":1,"end":53,"type":"D"}],"Molecular function":[{"start":1,"end":53,"type":"F"}],"Structural transition":[{"start":1,"end":53,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00091","name":"Tubulin/FtsZ family, GTPase domain","start":4,"end":213},{"id":"PF03953","name":"Tubulin C-terminal domain","start":263,"end":391}],"gene3D":[{"start":382,"end":444,"id":"1.10.287.600","name":"Helix hairpin bin"},{"start":270,"end":380,"id":"3.30.1330.20","name":"Tubulin/FtsZ, C-terminal domain"},{"start":1,"end":268,"id":"3.40.50.1440","name":"Tubulin/FtsZ, GTPase domain"}]},"uniref50":"UniRef50_P53378","sequence":"MGGEIITLQAGQCGNHVGKFLWSQLAKEHAIGTDGLSQLPDSSTERDDDTKPFFRENSRNKFTPRAIMMDSEPSVIADVENTFRGFFDPRNTWVASDGASAGNSWANGYDIGTRNQDDILNKIDKEIDSTDNFEGFQLLHSVAGGTGSGLGSNLLEALCDRYPKKILTTYSVFPARSSEVVVQSYNTILALRRLIEDSDATVVFDNASLLNISGKVFRNPNIDLQHTNQLISTIISSVTNSIRFPSYMYSSMSSIYSTLIPSPELHFLSPSFTPFTSDYIHDDIAHKGHSSYDVMLDLLDPSNSLVSTAMNNPTYFNVYNTIIGNVEPRQISRAMTKLQQRIKFPSWSSSAMHVNIGRRSPYLPLQPNENEVSGMMLSNMSTVVNVFENACNTFDKVFAKGAFLNNYNVGDLFQSMQNVQDEFAESREVVQSLMEDYVAAEQDSYLDDVLVDDENMVGELEEDLDADGDHKLV","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P53378","disprot_id":"DP01513","ncbi_taxon_id":559292,"regions_counter":2,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":473,"region_id":"DP01513r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Concerted millisecond timescale dynamics in the intrinsically disordered carboxyl terminus of γ-tubulin induced by mutation of a conserved tyrosine residue. <i> Harris J, Shadrina M, Oliver C, Vogel J, Mittermaier A. </i> Protein Sci, 2018","statement":[{"text":"We performed a combination of NMR experiments and computer simulations to investigate the structural and dynamical consequences of introducing negative charge at a site in the gamma-tubulin CT(439-473)  that is phosphorylated in vivo. The results derived from the two techniques were remarkably similar. Both showed that the WT gamma-CT is largely unstructured.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":439,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"29127738","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":473,"term_name":"phosphorylation display site","start":439,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"The in vivo phosphorylation of an evolutionarily conserved Tyr (Y445) residue in the gamma-tubulin orthologue of the budding yeast was identified. Mutation of Y445 to an acidic residue alters microtubule dynamics and perturbs the function of the mitotic spindle but does not appear to alter microtubule nucleation, suggesting the S.c. gamma-CT may function in postnucleation organization and function of microtubules.","type":"Introduction"}],"curator_id":"bszabo","released":"2022_03","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"29127738","version":2,"reference_html":"Concerted millisecond timescale dynamics in the intrinsically disordered carboxyl terminus of γ-tubulin induced by mutation of a conserved tyrosine residue. <i> Harris J, Shadrina M, Oliver C, Vogel J, Mittermaier A. </i> Protein Sci, 2018","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000045","ec_id":"ECO:0006165","region_id":"DP01513r002","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_P53378","date":"2018-07-24T12:22:27.000Z","acc":"P53378","name":"Tubulin gamma chain","length":473,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000005307C","genes":[{"name":{"value":"TUB4"},"orfNames":[{"value":"L8167.21"}],"olnNames":[{"value":"YLR212C"}]}],"alphafold_very_low_content":0.07188160676532769,"disorder_content":0.07399577167019028,"disprot_consensus":{"full":[{"start":439,"end":473,"type":"D"}],"Structural state":[{"start":439,"end":473,"type":"D"}],"Disorder function":[{"start":439,"end":473,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00788","name":"Ras association (RalGDS/AF-6) domain","start":247,"end":327},{"id":"PF09235","name":"Ste50p, sterile alpha motif","start":30,"end":104}],"gene3D":[{"start":28,"end":107,"id":"1.10.150.50","name":"Transcription Factor, Ets-1"},{"start":246,"end":329,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"}]},"uniref50":"UniRef50_P25344","sequence":"MEDGKQAINEGSNDASPDLDVNGTILMNNEDFSQWSVDDVITWCISTLEVEETDPLCQRLRENDIVGDLLPELCLQDCQDLCDGDLNKAIKFKILINKMRDSKLEWKDDKTQEDMITVLKNLYTTTSAKLQEFQSQYTRLRMDVLDVMKTSSSSSPINTHGVSTTVPSSNNTIIPSSDGVSLSQTDYFDTVHNRQSPSRRESPVTVFRQPSLSHSKSLHKDSKNKVPQISTNQSHPSAVSTANTPGPSPNEALKQLRASKEDSCERILKNAMKRHNLADQDWRQYVLVICYGDQERLLELNEKPVIIFKNLKQQGLHPAIMLRRRGDFEEVAMMNGSDNVTPGGRL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P25344","disprot_id":"DP01515","ncbi_taxon_id":559292,"regions_counter":1,"creator":"bhajdu","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":249,"region_id":"DP01515r001","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Binding the atypical RA domain of Ste50p to the unfolded Opy2p cytoplasmic tail is essential for the high-osmolarity glycerol pathway. <i> Ekiel I, Sulea T, Jansen G, Kowalik M, Minailiuc O, Cheng J, Harcus D, Cygler M, Whiteway M, Wu C. </i> Mol Biol Cell, 2009","statement":[{"text":"The initial construct corresponding to the predicted Ste50p-RA domain showed a well-dispersed 1H-15N HSQC spectrum indicative of a folded protein (data not shown), with the exception of the N-terminal region that was unfolded.","type":"Results"},{"text":"To verify that the “missing strands” are not located in more distal regions of the protein, we analyzed a longer Ste50p fragment corresponding to aa187-346 was by NMR, and no additional folded elements were detected.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":187,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-29T13:53:27.734Z","reference_source":"pmid","term_name":"disorder","reference_id":"19846660","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P25344","date":"2018-07-24T15:05:02.000Z","acc":"P25344","name":"Protein STE50","length":346,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000136073","genes":[{"name":{"value":"STE50"},"orfNames":[{"value":"YCL32W"}],"olnNames":[{"value":"YCL032W"}]}],"alphafold_very_low_content":0.3786127167630058,"disorder_content":0.18208092485549132,"disprot_consensus":{"full":[{"start":187,"end":249,"type":"D"}],"Structural state":[{"start":187,"end":249,"type":"D"}]}},{"features":{"pfam":[{"id":"PF09463","name":"Opy2 protein","start":30,"end":63}]},"uniref50":"UniRef50_Q06810","sequence":"MSSSSKASASSSLSSTATSSTSATRGSDGCVVCDSTASCPVCASGEYCVMTSLTCDKCPSTYCAKQSDSQLSSLSSSSSSSSSSNSNEKTSLIVGFTVGIVGGAMLIALVALYFINKRYWKPKRQKNKALKLEEASQSYGNEEEYFDDEDDDDEDDEDDGGMRKDESHTLFNTSLVPPTLNVPGNRSSASTTRTRASNILPIAYIPGVTSGLSTDKLQSKLRSSSKRQNAAGDIRSHITLGSSILDGLDDEDDEHNQVLNKDADDNLITAIRAKPKLVQIAEEESDKEIQDLDVIEEQTEADDLSHMAKSEASHGNNDEDDDEEGSFILDLEIPESIRESTQGSRTESPFEDKFEIHDER","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q06810","disprot_id":"DP01516","ncbi_taxon_id":559292,"regions_counter":6,"creator":"bhajdu","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":333,"region_id":"DP01516r001","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Binding the atypical RA domain of Ste50p to the unfolded Opy2p cytoplasmic tail is essential for the high-osmolarity glycerol pathway. <i> Ekiel I, Sulea T, Jansen G, Kowalik M, Minailiuc O, Cheng J, Harcus D, Cygler M, Whiteway M, Wu C. </i> Mol Biol Cell, 2009","statement":[{"text":"Sequence analysis predicted that the cytoplasmic tail of Opy2p is intrinsically unstructured (Supplemental Figure S2A). This prediction was confirmed by NMR spectroscopy of a recombinant 15N-enriched fragment of Opy2p encompassing amino acid residues 194-333, which showed a 1H-15N HSQC spectrum indicative of an unstructured polypeptide (Supplemental Figure S2B).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":194,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-29T14:03:23.837Z","reference_source":"pmid","term_name":"disorder","reference_id":"19846660","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":267,"end":345,"reference_id":"19846660","reference_source":"pmid","reference_html":"Binding the atypical RA domain of Ste50p to the unfolded Opy2p cytoplasmic tail is essential for the high-osmolarity glycerol pathway. <i> Ekiel I, Sulea T, Jansen G, Kowalik M, Minailiuc O, Cheng J, Harcus D, Cygler M, Whiteway M, Wu C. </i> Mol Biol Cell, 2009","date":"2023-08-29T14:04:19.719Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01516r003","statement":[{"text":"The HSQC spectra of 15N-labeled Opy2p SID (aa 267-345) shows this region is unstructured.","type":"Curator statement"}]},{"start":325,"end":339,"reference_id":"19846660","reference_source":"pmid","reference_html":"Binding the atypical RA domain of Ste50p to the unfolded Opy2p cytoplasmic tail is essential for the high-osmolarity glycerol pathway. <i> Ekiel I, Sulea T, Jansen G, Kowalik M, Minailiuc O, Cheng J, Harcus D, Cygler M, Whiteway M, Wu C. </i> Mol Biol Cell, 2009","date":"2023-08-29T14:06:00.642Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P25344","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01516r004","statement":[{"text":"The HSQC spectra of this fragment titrated with the unlabeled Ste50p-RA domain revealed that only signals corresponding to residues 325-339 of SIDOpy2p showed significant changes in the presence of the Ste50p-RA domain (Figure 4A), suggesting that these residues contribute to the interaction. ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":325,"end":339,"reference_id":"19846660","reference_source":"pmid","reference_html":"Binding the atypical RA domain of Ste50p to the unfolded Opy2p cytoplasmic tail is essential for the high-osmolarity glycerol pathway. <i> Ekiel I, Sulea T, Jansen G, Kowalik M, Minailiuc O, Cheng J, Harcus D, Cygler M, Whiteway M, Wu C. </i> Mol Biol Cell, 2009","date":"2023-08-29T14:08:54.666Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006277","ec_ontology":"ECO","ec_name":"fluorescence polarization evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P25344","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01516r005","statement":[{"text":"To quantify the strength of this interaction, we used fluorescence polarization and isothermal titration calorimetry (ITC) measurements and determined that the affinity (apparent Kd) is in the range of 20–80 μM (Figure 4B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"The s-peptide of Opy2 was produced as GST fusion using the pGEX vector and the Gold Magic strain of E. coli."}]}]},{"start":325,"end":339,"reference_id":"19846660","reference_source":"pmid","reference_html":"Binding the atypical RA domain of Ste50p to the unfolded Opy2p cytoplasmic tail is essential for the high-osmolarity glycerol pathway. <i> Ekiel I, Sulea T, Jansen G, Kowalik M, Minailiuc O, Cheng J, Harcus D, Cygler M, Whiteway M, Wu C. </i> Mol Biol Cell, 2009","date":"2023-08-29T14:09:20.437Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"The s-peptide of Opy2 was produced as GST fusion using the pGEX vector and the Gold Magic strain of E. coli."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P25344","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01516r006","statement":[{"text":"To quantify the strength of this interaction, we used fluorescence polarization and isothermal titration calorimetry (ITC) measurements and determined that the affinity (apparent Kd) is in the range of 20–80 μM (Figure 4B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_Q06810","date":"2018-07-24T15:19:46.000Z","acc":"Q06810","name":"Protein OPY2","length":360,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000006A585","genes":[{"name":{"value":"OPY2"},"olnNames":[{"value":"YPR075C"}]}],"alphafold_very_low_content":0.25555555555555554,"disorder_content":0.4222222222222222,"disprot_consensus":{"full":[{"start":194,"end":345,"type":"D"}],"Structural state":[{"start":194,"end":345,"type":"D"}],"Molecular function":[{"start":325,"end":339,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00292","name":"'Paired box' domain","start":9,"end":133},{"id":"PF12403","name":"Paired-box protein 2 C terminal","start":339,"end":449}],"gene3D":[{"start":1,"end":77,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"start":78,"end":157,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}]},"uniref50":"UniRef50_Q06710","sequence":"MPHNSIRSGHGGLNQLGGAFVNGRPLPEVVRQRIVDLAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIRPGVIGGSKPKVATPKVVEKIGDYKRQNPTMFAWEIRDRLLAEGVCDNDTVPSVSSINRIIRTKVQQPFNLPMDSCVATKSLSPGHTLIPSSAVTPPESPQSDSLGSTYSINGLLGIAQPGSDKRKMDDSDQDSCRLSIDSQSSSSGPRKHLRTDAFSQHHLEPLECPFERQHYPEAYASPSHTKGEQGLYPLPLLNSTLDDGKATLTPSNTPLGRNLSTHQTYPVVADPHSPFAIKQETPEVSSSSSTPSSLSSSAFLDLQQVGSGVPPFNAFPHAASVYGQFTGQALLSGREMVGPTLPGYPPHIPTSGQGSYASSAIAGMVAGSEYSGNAYGHTPYSSYSEAWRFPNSSLLSSPYYYSSTSRPSAPPTTATAFDHL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q06710","disprot_id":"DP01517","ncbi_taxon_id":9606,"regions_counter":4,"creator":"bhajdu","regions":[{"region_id":"DP01517r001","ec_ontology":"ECO","end":86,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":64,"version":3,"statement":[{"text":"NOE data and chemical shift differences from random coil values (60) support the random coil nature of the linker (Figs. ​(Figs.22 and supplemental S4). Furthermore, the backbone chemical shifts of the linker are consistent with a highly flexible backbone, according to the random coil index (65) (supplemental Fig. S5).","type":"Results"}],"term_name":"disorder","reference_html":"The solution structure of DNA-free Pax-8 paired box domain accounts for redox regulation of transcriptional activity in the pax protein family. <i> Codutti L, van Ingen H, Vascotto C, Fogolari F, Corazza A, Tell G, Quadrifoglio F, Viglino P, Boelens R, Esposito G. </i> J Biol Chem, 2008","released":"2022_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18829450","date":"2022-06-23T18:09:06.521Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2K27"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-25T20:35:20.838Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":86,"term_name":"flexible linker","released":"2022_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The solution structure of DNA-free Pax-8 paired box domain accounts for redox regulation of transcriptional activity in the pax protein family. <i> Codutti L, van Ingen H, Vascotto C, Fogolari F, Corazza A, Tell G, Quadrifoglio F, Viglino P, Boelens R, Esposito G. </i> J Biol Chem, 2008","statement":[{"text":"The tertiary organization of the free Pax-8 DNA binding domain shows the characteristics of a canonical Prd domain: two HTH motifs are connected by an unstructured linker region. NOE data and chemical shift differences from random coil values (60) support the random coil nature of the linker (Figs. ​(Figs.22 and supplemental S4). Furthermore, the backbone chemical shifts of the linker are consistent with a highly flexible backbone, according to the random coil index (65) (supplemental Fig. S5).","type":"Results"}],"term_id":"IDPO:0000033","curator_id":"vnugnes","start":64,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18829450","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-23T18:09:38.105Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01517r002","ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-25T20:35:17.974Z"}},{"region_id":"DP01517r003","ec_ontology":"ECO","end":146,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":135,"version":3,"statement":[{"text":"Additionally, the random coil index indicates a random coil-like structure and high backbone flexibility for the C- and N-terminal regions flanking the two HTH domains.","type":"Results"}],"term_name":"disorder","reference_html":"The solution structure of DNA-free Pax-8 paired box domain accounts for redox regulation of transcriptional activity in the pax protein family. <i> Codutti L, van Ingen H, Vascotto C, Fogolari F, Corazza A, Tell G, Quadrifoglio F, Viglino P, Boelens R, Esposito G. </i> J Biol Chem, 2008","released":"2022_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18829450","date":"2022-06-23T18:06:14.919Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2K27"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-25T20:35:22.264Z"}},{"region_id":"DP01517r004","ec_ontology":"ECO","end":28,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":1,"version":3,"statement":[{"text":"Additionally, the random coil index indicates a random coil-like structure and high backbone flexibility for the C- and N-terminal regions flanking the two HTH domains.","type":"Results"}],"term_name":"disorder","reference_html":"The solution structure of DNA-free Pax-8 paired box domain accounts for redox regulation of transcriptional activity in the pax protein family. <i> Codutti L, van Ingen H, Vascotto C, Fogolari F, Corazza A, Tell G, Quadrifoglio F, Viglino P, Boelens R, Esposito G. </i> J Biol Chem, 2008","released":"2022_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18829450","date":"2022-06-23T18:05:22.945Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2K27"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-25T20:35:16.514Z"}}],"released":"2018_11","uniref100":"UniRef100_Q06710","date":"2018-07-24T16:16:29.000Z","acc":"Q06710","name":"Paired box protein Pax-8","length":450,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI0000131374","genes":[{"name":{"value":"PAX8"}}],"alphafold_very_low_content":0.6222222222222222,"disorder_content":0.14,"disprot_consensus":{"full":[{"start":1,"end":28,"type":"D"},{"start":64,"end":86,"type":"D"},{"start":135,"end":146,"type":"D"}],"Structural state":[{"start":1,"end":28,"type":"D"},{"start":64,"end":86,"type":"D"},{"start":135,"end":146,"type":"D"}],"Disorder function":[{"start":64,"end":86,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MEIYSPDMSEVAAERSSSPSTQLSADPSLDGLPAAEDMPEPQTEDGRTPGLVGLAVPCCACLEAERLRGCLNSEKICIVPILACLVSLCLCIAGLKWVFVDKIFEYDSPTHLDPGGLGQDPIISLDATAASAVWVSSEAYTSPVSRAQSESEVQVTVQGDKAVVSFEPSAAPTPKNRIFAFSFLPSTAPSFPSPTRNPEVRTPKSATQPQTTETNLQTAPKLSTSTSTTGTSHLVKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCPNEFTGDRCQNYVMASFYSTSTPFLSLPE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"","disprot_id":"DP01520","ncbi_taxon_id":9606,"regions_counter":5,"creator":"spdiaz","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":75,"region_id":"DP01520r001","released":"2022_03","ec_id":"ECO:0007689","reference_html":"The N-terminal cytoplasmic domain of neuregulin 1 type III is intrinsically disordered. <i> Chukhlieb M, Raasakka A, Ruskamo S, Kursula P. </i> Amino Acids, 2015","statement":[{"text":"Atypical mobility of pure NRG1-III-Nct on SDS-PAGE was observed, which is an indication of a disordered nature of the protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":1,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"25944317","version":2,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":75,"region_id":"DP01520r002","released":"2022_03","ec_id":"ECO:0006210","reference_html":"The N-terminal cytoplasmic domain of neuregulin 1 type III is intrinsically disordered. <i> Chukhlieb M, Raasakka A, Ruskamo S, Kursula P. </i> Amino Acids, 2015","statement":[{"text":"Two types of synchroton SAXS experiments were done: a highly concentrated batch of the protein was directly analysed, and the protein was also subjected to an online SAXS experiment on a SEC column. The featureless scattering curve suggests a lack of globular folded domains, which is confirmed by the Kratky plot, clearly lacking any defined maximum characteristic for a folded protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":1,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"25944317","version":2,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":75,"region_id":"DP01520r003","released":"2022_03","ec_id":"ECO:0006202","reference_html":"The N-terminal cytoplasmic domain of neuregulin 1 type III is intrinsically disordered. <i> Chukhlieb M, Raasakka A, Ruskamo S, Kursula P. </i> Amino Acids, 2015","statement":[{"text":"The folding of NRG1-III-Nct was studied by SRCD spectroscopy. In aqueous solution, the protein showed a typical spectrum for disordered proteins, with a strong negative minimum at 200 nm. This result fits well to the sequence-based predictions of disorder.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":1,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"25944317","version":2,"ec_name":"synchrotron radiation circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":75,"term_name":"nickel cation binding","start":1,"ec_name":"isothermal titration calorimetry evidence used in manual assertion","statement":[{"text":"To further investigate metal binding by NRG1-III-Nct, ITC experiments were performed. The binding assays (Fig. 4; Table 1) showed that the protein binds to Zn2+ as well as to Ni2+ with a dissociation constant Kd in the low micromolar range. No binding was observed with Mg2+ or Fe2+.","type":"Results"}],"curator_id":"vnugnes","released":"2024_12","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"25944317","version":4,"reference_html":"The N-terminal cytoplasmic domain of neuregulin 1 type III is intrinsically disordered. <i> Chukhlieb M, Raasakka A, Ruskamo S, Kursula P. </i> Amino Acids, 2015","date":"2024-10-16T15:18:45.265Z","term_id":"GO:0016151","ec_id":"ECO:0005647","region_id":"DP01520r004","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nickel (Ni) cation.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":false,"curator_orcid":"0000-0001-8399-7907","interaction_partner":[{"db":"ChEBI","id":"49786","operator":"and","partner_start":null,"partner_end":null}]},{"start":1,"end":75,"reference_id":"25944317","reference_source":"pmid","reference_html":"The N-terminal cytoplasmic domain of neuregulin 1 type III is intrinsically disordered. <i> Chukhlieb M, Raasakka A, Ruskamo S, Kursula P. </i> Amino Acids, 2015","date":"2024-10-16T15:18:54.460Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008270","term_name":"zinc ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"29105","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01520r005","statement":[{"text":"To further investigate metal binding by NRG1-III-Nct, ITC experiments were performed. The binding assays (Fig. 4; Table 1) showed that the protein binds to Zn2+ as well as to Ni2+ with a dissociation constant Kd in the low micromolar range. No binding was observed with Mg2+ or Fe2+.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a zinc ion (Zn).\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"","date":"2018-07-25T07:43:03.000Z","acc":"Q02297-10","name":"Isoform 10 of Pro-neuregulin-1, membrane-bound isoform","length":296,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000437A6","genes":[{"name":{"value":"NRG1"},"synonyms":[{"value":"GGF"},{"value":"HGL"},{"value":"HRGA"},{"value":"NDF"},{"value":"SMDF"}]}],"disorder_content":0.2533783783783784,"disprot_consensus":{"full":[{"start":1,"end":75,"type":"D"}],"Structural state":[{"start":1,"end":75,"type":"D"}],"Molecular function":[{"start":1,"end":75,"type":"F"}]}},{"features":{"gene3D":[{"start":247,"end":279,"id":"G3DSA:1.25.40.1020"}],"pfam":[{"id":"PF20491","name":"Ermin","start":1,"end":282}]},"uniref50":"UniRef50_Q5EBJ4","sequence":"MTDTPVTLSGSECNGDRPPENGQQPSSQTRKTTDADETQTYYGVEPSLQHLPAKENQEESGNSKGNVLPRGSEDEKILNENTEENLFVVHQAIQDLSLQETSAEDTVFQEGHPWKKIPLNSHNLDMSRQKERIVHQHLEQREDESAAHQATEIEWLGFQKSSQVDILHSKCDEEEEVWNEEINEEDVDECAEDEGEDEVRVIEFKRKYREGSPLKEESLAREDSPLSSPSSQPGTPDEQLVLGKKGDIARNSYSRYNTISYRKIRKGNTKQRIDEFESMMHL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_Q5RJL0","disprot_id":"DP01521","ncbi_taxon_id":10116,"regions_counter":5,"creator":"bszabo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":282,"region_id":"DP01521r001","released":"2022_03","ec_id":"ECO:0006202","reference_html":"Juxtanodin is an intrinsically disordered F-actin-binding protein. <i> Ruskamo S, Chukhlieb M, Vahokoski J, Bhargav SP, Liang F, Kursula I, Kursula P. </i> Sci Rep, 2012","statement":[{"text":"Synhrotron radiation circular dichroism (SRCD) spectra were recorded for full-length juxtanodin and truncated variants. All spectra exhibited a negative minimum close to 200 nm and a relatively low ellipticity above 210 nm, a typical observation for disordered proteins.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":1,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"23198089","version":2,"ec_name":"synchrotron radiation circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":282,"term_name":"protein binding","start":1,"ec_name":"synchrotron radiation circular dichroism evidence used in manual assertion","statement":[{"text":"Juxtanodin, also called ermin, is a 282-residue actin-binding protein, which co-localizes with filamentous actin (F-actin) and promotes the formation of cell protrusions during the differentiation of oligodendrocytes.","type":"Introduction"}],"curator_id":"bszabo","released":"2022_03","term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"23198089","version":3,"reference_html":"Juxtanodin is an intrinsically disordered F-actin-binding protein. <i> Ruskamo S, Chukhlieb M, Vahokoski J, Bhargav SP, Liang F, Kursula I, Kursula P. </i> Sci Rep, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006202","region_id":"DP01521r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":282,"region_id":"DP01521r003","released":"2022_03","ec_id":"ECO:0007689","reference_html":"Juxtanodin: an oligodendroglial protein that promotes cellular arborization and 2',3'-cyclic nucleotide-3'-phosphodiesterase trafficking. <i> Zhang B, Cao Q, Guo A, Chu H, Chan YG, Buschdorf JP, Low BC, Ling EA, Liang F. </i> Proc Natl Acad Sci U S A, 2005","statement":[{"text":"The mmunoblotting results showed a discrepancy between the calculated molecular mass (32.2 kDa) and the actual migration of JN on SDS/PAGE. Further tests attributed this atypical migration of JN largely to its residues 101-247. In vitro expression of FLAG-tagged JN, JN247, JN141, and JNc yielded products that, on Western blots, measured heavier than predicted by 30%, 41%, 16%, and 44%, respectively.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":1,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"16051705","version":2,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":282,"region_id":"DP01521r004","released":"2022_03","ec_id":"ECO:0007066","reference_html":"Juxtanodin is an intrinsically disordered F-actin-binding protein. <i> Ruskamo S, Chukhlieb M, Vahokoski J, Bhargav SP, Liang F, Kursula I, Kursula P. </i> Sci Rep, 2012","statement":[{"text":"The SLS analysis clearly illustrates that juxtanodin is monomeric in solution, with a molecular weight of 32 kDa, which is essentially identical to the expected value of 32.2 kDa for a monomer. The small elution volume indicates a large hydrodynamic radius, i.e. juxtanodin has an extended and non-globular shape.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":1,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"23198089","version":2,"ec_name":"static light scattering assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":282,"region_id":"DP01521r005","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Juxtanodin is an intrinsically disordered F-actin-binding protein. <i> Ruskamo S, Chukhlieb M, Vahokoski J, Bhargav SP, Liang F, Kursula I, Kursula P. </i> Sci Rep, 2012","statement":[{"text":"We performed SAXS experiments. The Rg values derived from the Guinier plot, the distance distribution functions and Debye functions showed highly extended particle shapes. The large maximum particle dimensions (Dmax) also support a disordered nature. The Kratky plot revealed the typical behavior of disordered proteins, with a short plateau followed by a monotonic increase, and the lack of a clear maximum.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bszabo","start":1,"term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"23198089","version":2,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q5RJL0","date":"2018-07-25T08:22:06.000Z","acc":"Q5RJL0","name":"Ermin","length":282,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI00001CF150","genes":[{"name":{"value":"Ermn"}}],"alphafold_very_low_content":0.28368794326241137,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":282,"type":"D"}],"Structural state":[{"start":1,"end":282,"type":"D"}],"Molecular function":[{"start":1,"end":282,"type":"F"}]}},{"features":{"pfam":[{"id":"PF24807","name":"CDC20/Fizzy WD40 domain","start":179,"end":470}],"gene3D":[{"start":172,"end":474,"id":"2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"}]},"uniref50":"UniRef50_Q9UM11","sequence":"MDQDYERRLLRQIVIQNENTMPRVTEMRRTLTPASSPVSSPSKHGDRFIPSRAGANWSVNFHRINENEKSPSQNRKAKDATSDNGKDGLAYSALLKNELLGAGIEKVQDPQTEDRRLQPSTPEKKGLFTYSLSTKRSSPDDGNDVSPYSLSPVSNKSQKLLRSPRKPTRKISKIPFKVLDAPELQDDFYLNLVDWSSLNVLSVGLGTCVYLWSACTSQVTRLCDLSVEGDSVTSVGWSERGNLVAVGTHKGFVQIWDAAAGKKLSMLEGHTARVGALAWNAEQLSSGSRDRMILQRDIRTPPLQSERRLQGHRQEVCGLKWSTDHQLLASGGNDNKLLVWNHSSLSPVQQYTEHLAAVKAIAWSPHQHGLLASGGGTADRCIRFWNTLTGQPLQCIDTGSQVCNLAWSKHANELVSTHGYSQNQILVWKYPSLTQVAKLTGHSYRVLYLAMSPDGEAIVTGAGDETLRFWNVFSKTRSTKVKWESVSVLNLFTRIR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UM11","disprot_id":"DP01524","ncbi_taxon_id":9606,"regions_counter":4,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":41,"region_id":"DP01524r001","released":"2023_06","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The region is specified in the Extended Data Table 2","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":1,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0003-0362-8218","date":"2023-05-17T13:30:34.110Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-17T13:31:36.008Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":87,"region_id":"DP01524r002","released":"2023_06","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The region is specified in the Extended Data Table 2","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":68,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0003-0362-8218","date":"2023-05-17T13:30:19.276Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-17T13:31:13.932Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":124,"region_id":"DP01524r003","released":"2023_06","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The region is specified in the Extended Data Table 2","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":109,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0003-0362-8218","date":"2023-05-17T13:30:10.882Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-17T13:31:03.965Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":145,"region_id":"DP01524r004","released":"2023_06","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The region is specified in the Extended Data Table 2","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":133,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0003-0362-8218","date":"2023-05-17T13:42:39.199Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-17T13:54:37.525Z"}}],"released":"2018_11","uniref100":"UniRef100_Q9UM11","date":"2018-07-25T15:18:46.000Z","acc":"Q9UM11","name":"Fizzy-related protein homolog","length":496,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI000007165B","genes":[{"name":{"value":"FZR1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:24824","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:24824"}}]},"synonyms":[{"value":"CDH1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"14701726","url":"http://www.ncbi.nlm.nih.gov/pubmed/14701726","alternativeUrl":"https://europepmc.org/abstract/MED/14701726"}}]},{"value":"FYR"},{"value":"FZR"},{"value":"KIAA1242"}]}],"alphafold_very_low_content":0.14516129032258066,"disorder_content":0.1814516129032258,"disprot_consensus":{"full":[{"start":1,"end":41,"type":"D"},{"start":68,"end":87,"type":"D"},{"start":109,"end":124,"type":"D"},{"start":133,"end":145,"type":"D"}],"Structural state":[{"start":1,"end":41,"type":"D"},{"start":68,"end":87,"type":"D"},{"start":109,"end":124,"type":"D"},{"start":133,"end":145,"type":"D"}]}},{"features":{"pfam":[{"id":"PF08672","name":"Anaphase promoting complex (APC) subunit 2","start":757,"end":817},{"id":"PF25773","name":"ANAPC2-like, TPR repeats","start":322,"end":431},{"id":"PF26557","name":"Cullin alpha+beta domain","start":595,"end":709}],"gene3D":[{"start":733,"end":822,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"start":486,"end":580,"id":"1.20.1310.10","name":"Cullin Repeats"},{"start":589,"end":729,"id":"1.10.10.2620","name":"Cullin; Chain C, Domain 2"}]},"uniref50":"UniRef50_Q9UJX6","sequence":"MAAAVVVAEGDSDSRPGQELLVAWNTVSTGLVPPAALGLVSSRTSGAVPPKEEELRAAVEVLRGHGLHSVLEEWFVEVLQNDLQANISPEFWNAISQCENSADEPQCLLLLLDAFGLLESRLDPYLRSLELLEKWTRLGLLMGTGAQGLREEVHTMLRGVLFFSTPRTFQEMIQRLYGCFLRVYMQSKRKGEGGTDPELEGELDSRYARRRYYRLLQSPLCAGCSSDKQQCWCRQALEQFHQLSQVLHRLSLLERVSAEAVTTTLHQVTRERMEDRCRGEYERSFLREFHKWIERVVGWLGKVFLQDGPARPASPEAGNTLRRWRCHVQRFFYRIYASLRIEELFSIVRDFPDSRPAIEDLKYCLERTDQRQQLLVSLKAALETRLLHPGVNTCDIITLYISAIKALRVLDPSMVILEVACEPIRRYLRTREDTVRQIVAGLTGDSDGTGDLAVELSKTDPASLETGQDSEDDSGEPEDWVPDPVDADPGKSSSKRRSSDIISLLVSIYGSKDLFINEYRSLLADRLLHQFSFSPEREIRNVELLKLRFGEAPMHFCEVMLKDMADSRRINANIREEDEKRPAEEQPPFGVYAVILSSEFWPPFKDEKLEVPEDIRAALEAYCKKYEQLKAMRTLSWKHTLGLVTMDVELADRTLSVAVTPVQAVILLYFQDQASWTLEELSKAVKMPVALLRRRMSVWLQQGVLREEPPGTFSVIEEERPQDRDNMVLIDSDDESDSGMASQADQKEEELLLFWTYIQAMLTNLESLSLDRIYNMLRMFVVTGPALAEIDLQELQGYLQKKVRDQQLVYSAGVYRLPKNCS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UJX6","disprot_id":"DP01526","ncbi_taxon_id":9606,"regions_counter":6,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":14,"region_id":"DP01526r001","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The region is specified in the Extended Data Table 2","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":1,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"},{"db":"PDB","id":"5A31"},{"db":"PDB","id":"5G04"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":52,"region_id":"DP01526r002","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The region is specified in the Extended Data Table 2","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":30,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"},{"db":"PDB","id":"5G04"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":231,"region_id":"DP01526r003","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The region is specified in the Extended Data Table 2","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":221,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"},{"db":"PDB","id":"5G04"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":475,"region_id":"DP01526r004","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The region is specified in the Extended Data Table 2","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":459,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"},{"db":"PDB","id":"5G04"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":319,"region_id":"DP01526r005","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The region is specified in the Extended Data Table 2","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":305,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"},{"db":"PDB","id":"5G04"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":822,"region_id":"DP01526r006","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Atomic structure of the APC/C and its mechanism of protein ubiquitination. <i> Chang L, Zhang Z, Yang J, McLaughlin SH, Barford D. </i> Nature, 2015","statement":[{"text":"The region is specified in the Extended Data Table 2","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":731,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4UI9"},{"db":"PDB","id":"5G05"},{"db":"PDB","id":"5G04"}],"reference_id":"26083744","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9UJX6","date":"2018-07-25T19:05:39.000Z","acc":"Q9UJX6","name":"Anaphase-promoting complex subunit 2","length":822,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000043E1B","genes":[{"name":{"value":"ANAPC2"},"synonyms":[{"value":"APC2"},{"value":"KIAA1406"}]}],"alphafold_very_low_content":0.08637469586374696,"disorder_content":0.20924574209245742,"disprot_consensus":{"full":[{"start":1,"end":14,"type":"D"},{"start":30,"end":52,"type":"D"},{"start":221,"end":231,"type":"D"},{"start":305,"end":319,"type":"D"},{"start":459,"end":475,"type":"D"},{"start":731,"end":822,"type":"D"}],"Structural state":[{"start":1,"end":14,"type":"D"},{"start":30,"end":52,"type":"D"},{"start":221,"end":231,"type":"D"},{"start":305,"end":319,"type":"D"},{"start":459,"end":475,"type":"D"},{"start":731,"end":822,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01956","name":"Integral membrane protein EMC3/TMCO1-like","start":17,"end":197}]},"uniref50":"UniRef50_Q57904","sequence":"MFGSIFDIYYKTLDAIFMPIIKVLHPALAILIIAIIVSLIINIATKLLVDQKRVAELKKEIQEFQVKFKKMSKNPEMMEKLQEEQQRIMQLNAELMKMSFRPMIYTWVPIILIFIYLRHVYGFGGVYQELNPGWNGVVVYLPIILSKILFIDFWHWLGSIFYKGGFKIVSNTALGWLGWYILCSFATSTVLRKILGIK","taxonomy":["Archaea","Euryarchaeota","Methanomada group","Methanococci","Methanococcales","Methanocaldococcaceae","Methanocaldococcus"],"uniref90":"UniRef90_Q57904","disprot_id":"DP01527","ncbi_taxon_id":243232,"regions_counter":2,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":101,"region_id":"DP01527r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"A YidC-like Protein in the Archaeal Plasma Membrane. <i> Borowska MT, Dominik PK, Anghel SA, Kossiakoff AA, Keenan RJ. </i> Structure, 2015","statement":[{"text":"in the article \"The corresponding region in Mj0480 is predicted to form a coiled coil but is disordered in the crystal\"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":46,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5C8J"}],"reference_id":"26256539","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":101,"term_name":"small molecule binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"A YidC-like Protein in the Archaeal Plasma Membrane. <i> Borowska MT, Dominik PK, Anghel SA, Kossiakoff AA, Keenan RJ. </i> Structure, 2015","statement":[{"text":"\"we propose that this region facilitates interaction with different hydrophobic substrates\"","type":"Results"}],"term_id":"GO:0036094","curator_id":"amonzon","start":46,"term_ontology":"GO","curator_name":"Alex Monzon","reference_id":"26256539","version":3,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01527r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q57904","date":"2018-07-25T19:56:15.000Z","acc":"Q57904","name":"Uncharacterized protein MJ0480","length":198,"organism":"Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)","dataset":[],"UniParc":"UPI0000139877","genes":[{"olnNames":[{"value":"MJ0480"}]}],"alphafold_very_low_content":0,"disorder_content":0.2828282828282828,"disprot_consensus":{"full":[{"start":46,"end":101,"type":"D"}],"Structural state":[{"start":46,"end":101,"type":"D"}],"Molecular function":[{"start":46,"end":101,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00102","name":"Protein-tyrosine phosphatase","start":226,"end":456},{"id":"PF09013","name":"YopH, N-terminal","start":3,"end":123}],"gene3D":[{"start":1,"end":136,"id":"3.30.1570.10","name":"Protein-tyrosine phosphatase, YopH, N-terminal domain"},{"start":187,"end":468,"id":"3.90.190.10","name":"Protein tyrosine phosphatase superfamily"}]},"uniref50":"UniRef50_P15273","sequence":"MNLSLSDLHRQVSRLVQQESGDCTGKLRGNVAANKETTFQGLTIASGARESEKVFAQTVLSHVANIVLTQEDTAKLLQSTVKHNLNNYELRSVGNGNSVLVSLRSDQMTLQDAKVLLEAALRQESGARGHVSSHSHSVLHAPGTPVREGLRSHLDPRTPPLPPRERPHTSGHHGAGEARATAPSTVSPYGPEARAELSSRLTTLRNTLAPATNDPRYLQACGGEKLNRFRDIQCCRQTAVRADLNANYIQVGNTRTIACQYPLQSQLESHFRMLAENRTPVLAVLASSSEIANQRFGMPDYFRQSGTYGSITVESKMTQQVGLGDGIMADMYTLTIREAGQKTISVPVVHVGNWPDQTAVSSEVTKALASLVDQTAETKRNMYESKGSSAVADDSKLRPVIHCRAGVGRTAQLIGAMCMNDSRNSQLSVEDMVSQMRVQRNGIMVQKDEQLDVLIKLAEGQGRPLLNS","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"],"uniref90":"UniRef90_P15273","disprot_id":"DP01528","ncbi_taxon_id":630,"regions_counter":5,"creator":"mpajkos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":50,"region_id":"DP01528r001","released":"2024_06","ec_id":"ECO:0006165","reference_html":"Structure of the type III secretion and substrate-binding domain of Yersinia YopH phosphatase. <i> Smith CL, Khandelwal P, Keliikuli K, Zuiderweg ER, Saper MA. </i> Mol Microbiol, 2001","statement":[{"text":"By examining the R2 values for individual residues (Fig. 4B), we noted that certain residues, mainly located between helices α1 and α2 (residues 19–50), showed considerably greater line broadening of their 15N resonances (up to 15 s−1 excess broadening). This indicates that these regions in the monomeric protein are undergoing conformational exchange (i.e. adopting different conformations) at the milli- to microsecond timescale.","type":"Results"},{"text":"The authors used a different strain (Yersinia pseudotuberculosis serotype I (strain IP32953)). Since the IDR is 100% identical this region is considered disordered.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":20,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-06T14:17:44.292Z","reference_source":"pmid","term_name":"disorder","reference_id":"11737640","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":21,"end":35,"reference_id":"23519663","reference_source":"pmid","reference_html":"Context-dependent protein folding of a virulence peptide in the bacterial and host environments: structure of an SycH-YopH chaperone-effector complex. <i> Vujanac M, Stebbins CE. </i> Acta Crystallogr D Biol Crystallogr, 2013","date":"2024-02-06T14:16:19.136Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01528r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q7BTX0"}],"statement":[{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"4GF3"}]}],"released":"2018_11","uniref100":"UniRef100_P15273","date":"2018-07-26T09:19:05.000Z","acc":"P15273","name":"Tyrosine-protein phosphatase YopH","length":468,"organism":"Yersinia enterocolitica","dataset":["Bacterial virulence-related proteins"],"UniParc":"UPI0000000256","genes":[{"name":{"value":"yopH"},"synonyms":[{"value":"yop51"}]}],"alphafold_very_low_content":0.1388888888888889,"disorder_content":0.06623931623931624,"disprot_consensus":{"full":[{"start":20,"end":50,"type":"D"}],"Structural state":[{"start":20,"end":50,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00397","name":"WW domain","start":127,"end":153},{"id":"PF00397","name":"WW domain","start":169,"end":194},{"id":"PF06220","name":"U1 zinc finger","start":8,"end":43}],"gene3D":[{"start":8,"end":63,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":122,"end":196,"id":"2.20.70.10","name":"2.20.70.10"}]},"uniref50":"UniRef50_O75554","sequence":"MADYWKSQPKKFCDYCKCWIADNRPSVEFHERGKNHKENVAKRISEIKQKSLDKAKEEEKASKEFAAMEAAALKAYQEDLKRLGLESEILEPSITPVTSTIPPTSTSNQQKEKKEKKKRKKDPSKGRWVEGITSEGYHYYYDLISGASQWEKPEGFQGDLKKTAVKTVWVEGLSEDGFTYYYNTETGESRWEKPDDFIPHTSDLPSSKVNENSLGTLDESKSSDSHSDSDGEQEAEEGGVSTETEKPKIKFKEKNKNSDGGSDPETQKEKSIQKQNSLGSNEEKSKTLKKSNPYGEWQEIKQEVESHEEVDLELPSTENEYVSTSEADGGGEPKVVFKEKTVTSLGVMADGVAPVFKKRRTENGKSRNLRQRGDDQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O75554","disprot_id":"DP01531","ncbi_taxon_id":9606,"regions_counter":2,"creator":"jlamb","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":376,"region_id":"DP01531r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A new role for FBP21 as regulator of Brr2 helicase activity. <i> Henning LM, Santos KF, Sticht J, Jehle S, Lee CT, Wittwer M, Urlaub H, Stelzl U, Wahl MC, Freund C. </i> Nucleic Acids Res, 2017","statement":[{"text":"The spectrum of FBP 21276–376 showed very low chemical shift dispersion, consistent with an intrinsically disordered protein region (IDPR)","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jlamb","start":276,"term_ontology":"IDPO","curator_name":"John Lamb","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0568-8281","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28838205","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":376,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"A new role for FBP21 as regulator of Brr2 helicase activity. <i> Henning LM, Santos KF, Sticht J, Jehle S, Lee CT, Wittwer M, Urlaub H, Stelzl U, Wahl MC, Freund C. </i> Nucleic Acids Res, 2017","statement":[{"text":"The spectrum of the complex suggests that the FBP21 fragment globally retains its unstructured nature when bound to Brr2C-Sec63 and does not adopt a stable fold upon complex formation.","type":"Discussion"}],"term_id":"GO:0005515","curator_id":"jlamb","start":276,"term_ontology":"GO","curator_name":"John Lamb","reference_id":"28838205","version":3,"curator_orcid":"0000-0003-0568-8281","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01531r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_O75554","date":"2018-07-26T10:41:32.000Z","acc":"O75554","name":"WW domain-binding protein 4","length":376,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000072671","genes":[{"name":{"value":"WBP4"},"synonyms":[{"value":"FBP21","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"19592703","url":"http://www.ncbi.nlm.nih.gov/pubmed/19592703","alternativeUrl":"https://europepmc.org/abstract/MED/19592703"}}]},{"value":"FNBP21"}]}],"alphafold_very_low_content":0.3484042553191489,"disorder_content":0.26861702127659576,"disprot_consensus":{"full":[{"start":276,"end":376,"type":"D"}],"Structural state":[{"start":276,"end":376,"type":"D"}],"Molecular function":[{"start":276,"end":376,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MGEAEAPSFEMTWSSTTSSGYCSQEDSDSELEQYFTARTSLARRPRRDQDEPVEWETPDLSQAEIEQKIKEYNAQINSNLFMSLNKDGSYTGFIKVQLKLVRPVSVPSSKKPPSLQDARRGPGRGTSVRRRTSFYLPKDAVKHLHVLSRTRAREVIEALLRKFLVVDDPRKFALFERAERHGQVYLRKLLDDEQPLRLRLLAGPSDKALSFVLKENDSGEVNWDAFSMPELHNFLRILQREEEEHLRQILQKYSYCRQKIQEALHACPLG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"","disprot_id":"DP01533","ncbi_taxon_id":9606,"regions_counter":5,"creator":"bhajdu","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":50,"region_id":"DP01533r001","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C. <i> Escobar-Cabrera E, Lau DK, Giovinazzi S, Ishov AM, McIntosh LP. </i> Structure, 2010","statement":[{"text":"(A) Fully annotated 15N-HSQC spectrum of unbound Rassf1C1-50, assigned by 1H13C15Ncorrelation experiments. The polypeptide chain is predominantly disordered as evidenced by limited 1HN dispersion (10 mM sodium phosphate, 0.1 mM EDTA, pH 6.5, 25 °C).","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-29T14:57:06.403Z","reference_source":"pmid","term_name":"disorder","reference_id":"21134643","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP01533r003","ec_ontology":"ECO","end":72,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":61,"version":3,"statement":[{"text":"(C) Heteronuclear 15N{1H}NOE values of 15N-Rassf1C23-38w free (gray) and bound to DAXX55-144 (black) demonstrate that residues ∼28-38 are unstructured in isolation and become ordered upon complex formation.","type":"Figure"}],"term_name":"disorder","reference_html":"Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C. <i> Escobar-Cabrera E, Lau DK, Giovinazzi S, Ishov AM, McIntosh LP. </i> Structure, 2010","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"21134643","date":"2023-08-29T14:53:00.260Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"GSQEDSDSELEQYFTARW"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":72,"term_name":"protein binding","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C. <i> Escobar-Cabrera E, Lau DK, Giovinazzi S, Ishov AM, McIntosh LP. </i> Structure, 2010","statement":[{"text":"(C) Heteronuclear 15N{1H}NOE values of 15N-Rassf1C23-38w free (gray) and bound to DAXX55-144 (black) demonstrate that residues ∼28-38 are unstructured in isolation and become ordered upon complex formation.","type":"Supplementary material"}],"term_id":"GO:0005515","curator_id":"vnugnes","start":61,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"21134643","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-29T14:59:13.492Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01533r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q9UER7","operator":"and","partner_start":null,"partner_end":null}],"sequence_construct":"GSQEDSDSELEQYFTARW"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":72,"term_name":"disorder to order","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C. <i> Escobar-Cabrera E, Lau DK, Giovinazzi S, Ishov AM, McIntosh LP. </i> Structure, 2010","statement":[{"text":"(C) Heteronuclear 15N{1H}NOE values of 15N-Rassf1C23-38w free (gray) and bound to DAXX55-144 (black) demonstrate that residues ∼28-38 are unstructured in isolation and become ordered upon complex formation.","type":"Figure"}],"term_id":"IDPO:0000011","curator_id":"vnugnes","start":61,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"21134643","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-29T14:58:29.917Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01533r005","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UER7"}],"sequence_construct":"GSQEDSDSELEQYFTARW"}],"released":"2018_11","uniref100":"","date":"2018-07-26T12:00:03.000Z","acc":"Q9NS23-4","name":"Isoform C of Ras association domain-containing protein 1","length":270,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000004EC21","genes":[{"name":{"value":"RASSF1","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAF35128.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF35128.2"}}]},"synonyms":[{"value":"RDA32","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAC16001.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAC16001.1"}}]}]}],"disorder_content":0.22962962962962963,"disprot_consensus":{"full":[{"start":1,"end":50,"type":"D"},{"start":61,"end":72,"type":"T"}],"Structural state":[{"start":1,"end":50,"type":"D"},{"start":61,"end":72,"type":"D"}],"Molecular function":[{"start":61,"end":72,"type":"F"}],"Structural transition":[{"start":61,"end":72,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00617","name":"RasGEF domain","start":783,"end":962},{"id":"PF00618","name":"RasGEF N-terminal motif","start":601,"end":717},{"id":"PF00621","name":"RhoGEF domain","start":213,"end":384},{"id":"PF22697","name":"SOS1/NGEF-like PH domain","start":443,"end":541}],"gene3D":[{"start":754,"end":957,"id":"1.10.840.10","name":"Ras guanine-nucleotide exchange factors catalytic domain"},{"start":198,"end":421,"id":"1.20.900.10","name":"Dbl homology (DH) domain"},{"start":423,"end":551,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":15,"end":169,"id":"1.10.20.10","name":"Histone, subunit A"},{"start":958,"end":1043,"id":"1.10.840.10","name":"Ras guanine-nucleotide exchange factors catalytic domain"},{"start":568,"end":753,"id":"1.20.870.10","name":"Son of sevenless (SoS) protein Chain: S domain 1"}]},"uniref50":"UniRef50_Q07889","sequence":"MQAQQLPYEFFSEENAPKWRGLLVPALKKVQGQVHPTLESNDDALQYVEELILQLLNMLCQAQPRSASDVEERVQKSFPHPIDKWAIADAQSAIEKRKRRNPLSLPVEKIHPLLKEVLGYKIDHQVSVYIVAVLEYISADILKLVGNYVRNIRHYEITKQDIKVAMCADKVLMDMFHQDVEDINILSLTDEEPSTSGEQTYYDLVKAFMAEIRQYIRELNLIIKVFREPFVSNSKLFSANDVENIFSRIVDIHELSVKLLGHIEDTVEMTDEGSPHPLVGSCFEDLAEELAFDPYESYARDILRPGFHDRFLSQLSKPGAALYLQSIGEGFKEAVQYVLPRLLLAPVYHCLHYFELLKQLEEKSEDQEDKECLKQAITALLNVQSGMEKICSKSLAKRRLSESACRFYSQQMKGKQLAIKKMNEIQKNIDGWEGKDIGQCCNEFIMEGTLTRVGAKHERHIFLFDGLMICCKSNHGQPRLPGASNAEYRLKEKFFMRKVQINDKDDTNEYKHAFEIILKDENSVIFSAKSAEEKNNWMAALISLQYRSTLERMLDVTMLQEEKEEQMRLPSADVYRFAEPDSEENIIFEENMQPKAGIPIIKAGTVIKLIERLTYHMYADPNFVRTFLTTYRSFCKPQELLSLIIERFEIPEPEPTEADRIAIENGDQPLSAELKRFRKEYIQPVQLRVLNVCRHWVEHHFYDFERDAYLLQRMEEFIGTVRGKAMKKWVESITKIIQRKKIARDNGPGHNITFQSSPPTVEWHISRPGHIETFDLLTLHPIEIARQLTLLESDLYRAVQPSELVGSVWTKEDKEINSPNLLKMIRHTTNLTLWFEKCIVETENLEERVAVVSRIIEILQVFQELNNFNGVLEVVSAMNSSPVYRLDHTFEQIPSRQKKILEEAHELSEDHYKKYLAKLRSINPPCVPFFGIYLTNILKTEEGNPEVLKRHGKELINFSKRRKVAEITGEIQQYQNQPYCLRVESDIKRFFENLNPMGNSMEKEFTDYLFNKSLEIEPRNPKPLPRFPKKYSYPLKSPGVRPSNPRPGTMRHPTPLQQEPRKISYSRIPESETESTASAPNSPRTPLTPPPASGASSTTDVCSVFDSDHSSPFHSSNDTVFIQVTLPHGPRSASVSSISLTKGTDEVPVPPPVPPRRRPESAPAESSPSKIMSKHLDSPPAIPPRQPTSKAYSPRYSISDRTSISDPPESPPLLPPREPVRTPDVFSSSPLHLQPPPLGKKSDHGNAFFPNSPSPFTPPPPQTPSPHGTRRHLPSPPLTQEVDLHSIAGPPVPPRQSTSQHIPKLPPKTYKREHTHPSMHRDGPPLLENAHSS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q07889","disprot_id":"DP01534","ncbi_taxon_id":9606,"regions_counter":6,"creator":"fkordevani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1300,"region_id":"DP01534r001","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Structural landscape of the proline-rich domain of Sos1 nucleotide exchange factor. <i> McDonald CB, Bhat V, Kurouski D, Mikles DC, Deegan BJ, Seldeen KL, Lednev IK, Farooq A. </i> Biophys Chem, 2013","statement":[{"text":"Our data show that the far-UV CD spectrum of the PR domain is characterized by a negative band centered around 208nm in the absence of denaturants (Figures 3a and 3b). This strongly suggests that the PR domain predominantly adopts a random coil-like conformation in solution though the possibility of some degree of polyproline II (PPII) helices cannot be completely ruled out.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1141,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-16T15:45:26.525Z","reference_source":"pmid","term_name":"disorder","reference_id":"23528987","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:21:45.361Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1300,"region_id":"DP01534r002","released":"2023_06","ec_id":"ECO:0007064","reference_html":"Structural landscape of the proline-rich domain of Sos1 nucleotide exchange factor. <i> McDonald CB, Bhat V, Kurouski D, Mikles DC, Deegan BJ, Seldeen KL, Lednev IK, Farooq A. </i> Biophys Chem, 2013","statement":[{"text":" Accordingly, our hydrodynamic data further substantiate the notion that the PR domain likely adopts a random coil-like conformation in solution.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1141,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"dynamic light scattering assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-16T15:44:26.424Z","reference_source":"pmid","term_name":"disorder","reference_id":"23528987","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:21:50.648Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1300,"region_id":"DP01534r003","released":"2023_06","ec_id":"ECO:0006210","reference_html":"Structural landscape of the proline-rich domain of Sos1 nucleotide exchange factor. <i> McDonald CB, Bhat V, Kurouski D, Mikles DC, Deegan BJ, Seldeen KL, Lednev IK, Farooq A. </i> Biophys Chem, 2013","statement":[{"text":"Strikingly, the Kratky plots for the PR domain at all three concentrations initially rise at low scattering angles but then plateau out at higher scattering angles. Such behavior is consistent with an extended random coil-like conformation characteristic of proteins devoid of a globular structure (59).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1141,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-16T15:44:44.517Z","reference_source":"pmid","term_name":"disorder","reference_id":"23528987","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:21:53.207Z"}},{"start":1117,"end":1319,"reference_id":"27056844","reference_source":"pmid","reference_html":"Phase separation of signaling molecules promotes T cell receptor signal transduction. <i> Su X, Ditlev JA, Hui E, Xing W, Banjade S, Okrut J, King DS, Taunton J, Rosen MK, Vale RD. </i> Science, 2016","date":"2023-05-19T15:11:51.070Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006067","ec_ontology":"ECO","ec_name":"fluorescence recovery after photobleaching evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PhaSePro","id":"Q07889"}],"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"O43561","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P62993","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01534r005","statement":[{"text":"pLAT, Grb2, and Sos1 clusters exhibited dynamic liquid-like properties.","type":"Article"},{"text":"We observed multivalent assembly and consequent phase separation of LAT and its binding partners into liquid-like, micron-sized clusters.","type":"Article"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-19T15:17:58.101Z"}},{"start":1117,"end":1319,"reference_id":"27056844","reference_source":"pmid","reference_html":"Phase separation of signaling molecules promotes T cell receptor signal transduction. <i> Su X, Ditlev JA, Hui E, Xing W, Banjade S, Okrut J, King DS, Taunton J, Rosen MK, Vale RD. </i> Science, 2016","date":"2023-05-19T15:10:17.445Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP01534r006","statement":[{"text":"Supplementary figure S1 shows this peptide migrates as higher molecular weight protein, probably due to its extended disordered nature.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:21:56.936Z"}}],"released":"2018_11","uniref100":"UniRef100_Q07889","date":"2018-07-26T12:11:56.000Z","acc":"Q07889","name":"Son of sevenless homolog 1","length":1333,"organism":"Homo sapiens","dataset":["NDDs-related proteins","Condensates-related proteins"],"UniParc":"UPI0000135CF0","genes":[{"name":{"value":"SOS1"}}],"alphafold_very_low_content":0.24081020255063765,"disorder_content":0.1522880720180045,"disprot_consensus":{"full":[{"start":1117,"end":1319,"type":"D"}],"Structural state":[{"start":1117,"end":1319,"type":"D"}],"Molecular function":[{"start":1117,"end":1319,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_A0A086QY66","sequence":"MLQMARYTANICAVSICSLVLVVALSVGILPTPDWKDRVKMGGTESGPFVLQVCASDPLLHDPKERESGSDSTRGYHGGSSSGGSSSRQGTTVRSDAGLSSQSSQSSASTSAKTSENHRQGPAFLTSVFRKGETPALDWVPYGTLEGAKWHPGQQKSKRRSSATTSRRQGASHSGNPGQLPAPRGGLQPTTTLSGTGGQPRTDSTDEGAAATSVIPNRSGYPQPVPYLIHPVGFLSGDYRSLGMLGLVPSVYTATSVQHMVGQPGTIIPLVLLPGKQEPEGLVSTGTLSDSLVYEPLGVVNLGTEMPNQGSTSQSGAVASRKRPAGGANGPDKRRRVEPAGLTESRLRPEPSLSSLTEKGSTAFSTRPPSSRSALEGLTQETVEMLLDTPSYPISSVVSSPPPARKSSTSSSQHLEARLSQSRGPPRTRPPFNPWSTKTGLLERRGVSELPPLYIPRPLASGYRNPADSRKHSTVTPQTTPPARKSSTSSSQHLEARLSQSRGPPRTRPPFNPWSTKTGLLERRGVSELPPLRIVKPPTKGN","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Conoidasida","Coccidia","Eucoccidiorida","Eimeriorina","Sarcocystidae","Toxoplasma"],"uniref90":"UniRef90_A0A086QY66","disprot_id":"DP01535","ncbi_taxon_id":432359,"regions_counter":3,"creator":"atantos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":542,"region_id":"DP01535r001","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Structural Basis for the Subversion of MAP Kinase Signaling by an Intrinsically Disordered Parasite Secreted Agonist. <i> Pellegrini E, Palencia A, Braun L, Kapp U, Bougdour A, Belrhali H, Bowler MW, Hakimi MA. </i> Structure, 2017","statement":[{"text":"SAXS was used to determine the average structure of the GRA24DN-p38a complex in solution. The radius of gyration was determined to be 4.85 nm with a Dmax of 16.96 nm and ab initio modeling showing an elongated molecule best described by a disordered protein binding two globular domains.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":337,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27889209","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":542,"term_name":"protein binding","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","reference_html":"Structural Basis for the Subversion of MAP Kinase Signaling by an Intrinsically Disordered Parasite Secreted Agonist. <i> Pellegrini E, Palencia A, Braun L, Kapp U, Bougdour A, Belrhali H, Bowler MW, Hakimi MA. </i> Structure, 2017","statement":[{"text":"One of the effector proteins secreted by T. gondii, GRA24, has been shown to interact with the MAP kinase p38a, promoting its activation and nuclear translocation.","type":"Introduction"}],"term_id":"GO:0005515","curator_id":"atantos","start":337,"term_ontology":"GO","curator_name":"Agnes Tantos","reference_id":"27889209","version":3,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","region_id":"DP01535r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":542,"region_id":"DP01535r003","released":"2022_03","ec_id":"ECO:0001591","reference_html":"Structural Basis for the Subversion of MAP Kinase Signaling by an Intrinsically Disordered Parasite Secreted Agonist. <i> Pellegrini E, Palencia A, Braun L, Kapp U, Bougdour A, Belrhali H, Bowler MW, Hakimi MA. </i> Structure, 2017","statement":[{"text":"In both AFM and EM data no secondary structure can be observed in GRA24 confirming its disordered nature.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"atantos","start":337,"term_ontology":"IDPO","curator_name":"Agnes Tantos","ec_name":"atomic force microscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1273-9841","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27889209","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_A0A125YG37","date":"2018-07-26T13:13:47.000Z","acc":"B6KJB6","name":"Putative transmembrane protein","length":542,"organism":"Toxoplasma gondii (strain ATCC 50861 / VEG)","dataset":[],"UniParc":"UPI000185E6C6","genes":[{"orfNames":[{"value":"BN1205_025320","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CEL74758.1","url":"https://www.ebi.ac.uk/ena/browser/view/CEL74758.1"}}]},{"value":"TGVEG_230180","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ESS35662.1","url":"https://www.ebi.ac.uk/ena/browser/view/ESS35662.1"}}]}]}],"alphafold_very_low_content":0.9114391143911439,"disorder_content":0.3800738007380074,"disprot_consensus":{"full":[{"start":337,"end":542,"type":"D"}],"Structural state":[{"start":337,"end":542,"type":"D"}],"Molecular function":[{"start":337,"end":542,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGIVTRRPLILQLVHVSQEDKRKTTGEENGVEAEEWGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKIFSPNVVNLTLVDLPGMTKVPVGDQPKDIELQIRELILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKKYPSLANRNGTKYLARTLNRLLMHHIRDCLPELKTRINVLAAQYQSLLNSYGEPVDDKSATLLQLITKFATEYCNTIEGTAKYIETSELCGGARICYIFHETFGRTLESVDPLGGLNTIDILTAIRNATGPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCSNYSTQELLRFPKLHDAIVEVVTCLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNNNIEEQRRNRLARELPSAVSRDKLIQDSRRETKNVASGGGGVGDGVQEPTTGNWRGMLKTSKAEELLAEEKSKPIPIMPASPQKGHAVNLLDVPVPVARKLSAREQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKALQGASQIIAEIRETHLW","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"","disprot_id":"DP01537","ncbi_taxon_id":9606,"regions_counter":8,"creator":"bhajdu","regions":[{"region_id":"DP01537r001","ec_ontology":"ECO","end":515,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":505,"version":3,"statement":[{"text":"This region lacks electron density in the PDB structure indicating it is disordered.","type":"Results"}],"term_name":"disorder","reference_html":"Structural insights into oligomerization and mitochondrial remodelling of dynamin 1-like protein. <i> Fröhlich C, Grabiger S, Schwefel D, Faelber K, Rosenbaum E, Mears J, Rocks O, Daumke O. </i> EMBO J, 2013","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"23584531","date":"2023-08-29T15:27:10.826Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4BEJ"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly401Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro402Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"We followed a similar strategy as for dynamin and MxA and introduced the GPRP401-404AAAA mutation in the corresponding loop L2S of DNM1L (from here on referred to as 4A mutation)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg403Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"We followed a similar strategy as for dynamin and MxA and introduced the GPRP401-404AAAA mutation in the corresponding loop L2S of DNM1L (from here on referred to as 4A mutation)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro404Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"We followed a similar strategy as for dynamin and MxA and introduced the GPRP401-404AAAA mutation in the corresponding loop L2S of DNM1L (from here on referred to as 4A mutation)."}]}],"sequence_construct":"GPHMGGSMEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGIVTRRPLILQLVHVSQEDKRKTTGEENGVEAEEWGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKIFSPNVVNLTLVDLPGMTKVPVGDQPKDIELQIRELILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKKYPSLANRNGTKYLARTLNRLLMHHIRDCLPELKTRINVLAAQYQSLLNSYGEPVDDKSATLLQLITKFATEYCNTIEGTAKYIETSELCGGARICYIFHETFGRTLESVDPLGGLNTIDILTAIRNATAAAAALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCSNYSTQELLRFPKLHDAIVEVVTCLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNNNIEEQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKALQGASQIIAEIRETHLW"},{"term_namespace":"Biological process","ec_ontology":"ECO","end":610,"term_name":"protein localization to mitochondrion","released":"2023_12","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","reference_html":"Structural insights into oligomerization and mitochondrial remodelling of dynamin 1-like protein. <i> Fröhlich C, Grabiger S, Schwefel D, Faelber K, Rosenbaum E, Mears J, Rocks O, Daumke O. </i> EMBO J, 2013","statement":[{"text":"When expressed in DNM1L-depleted COS-7 cells, both the 4A and ΔB mutants failed to localize to mitochondria (Figure 3D). Instead, the 4A mutant was diffusely distributed in the cytoplasm, whereas the ΔB mutant was found in large punctate structures in the cytoplasm (Figure 3D, white arrows).","type":"Results"}],"term_id":"GO:0070585","curator_id":"vnugnes","start":503,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"23584531","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-29T15:43:56.517Z","reference_source":"pmid","ec_id":"ECO:0007089","region_id":"DP01537r005","ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A process in which a protein is transported to, or maintained in, a location within the mitochondrion.\" [GOC:ecd]","disprot_namespace":"Disorder function","term_is_binding":false,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Asp503_Leu600del","start":null,"end":null,"position":null}]},{"start":74,"end":83,"reference_id":"23584531","reference_source":"pmid","reference_html":"Structural insights into oligomerization and mitochondrial remodelling of dynamin 1-like protein. <i> Fröhlich C, Grabiger S, Schwefel D, Faelber K, Rosenbaum E, Mears J, Rocks O, Daumke O. </i> EMBO J, 2013","date":"2023-08-29T15:26:13.958Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4BEJ"}],"region_id":"DP01537r007","statement":[{"text":"This region lacks electron density in the PDB structure indicating it is disordered.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly401Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"We followed a similar strategy as for dynamin and MxA and introduced the GPRP401-404AAAA mutation in the corresponding loop L2S of DNM1L (from here on referred to as 4A mutation)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro402Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"We followed a similar strategy as for dynamin and MxA and introduced the GPRP401-404AAAA mutation in the corresponding loop L2S of DNM1L (from here on referred to as 4A mutation)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg403Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"We followed a similar strategy as for dynamin and MxA and introduced the GPRP401-404AAAA mutation in the corresponding loop L2S of DNM1L (from here on referred to as 4A mutation)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro404Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"We followed a similar strategy as for dynamin and MxA and introduced the GPRP401-404AAAA mutation in the corresponding loop L2S of DNM1L (from here on referred to as 4A mutation)."}]}],"sequence_construct":"GPHMGGSMEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGIVTRRPLILQLVHVSQEDKRKTTGEENGVEAEEWGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKIFSPNVVNLTLVDLPGMTKVPVGDQPKDIELQIRELILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKKYPSLANRNGTKYLARTLNRLLMHHIRDCLPELKTRINVLAAQYQSLLNSYGEPVDDKSATLLQLITKFATEYCNTIEGTAKYIETSELCGGARICYIFHETFGRTLESVDPLGGLNTIDILTAIRNATAAAAALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCSNYSTQELLRFPKLHDAIVEVVTCLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNNNIEEQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKALQGASQIIAEIRETHLW"},{"start":503,"end":610,"reference_id":"29899447","reference_source":"pmid","reference_html":"Structural basis of mitochondrial receptor binding and constriction by DRP1. <i> Kalia R, Wang RY, Yusuf A, Thomas PV, Agard DA, Shaw JM, Frost A. </i> Nature, 2018","date":"2023-08-29T15:41:38.388Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5WP9"},{"db":"EMDB","id":"8874"}],"region_id":"DP01537r008","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q96C03"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:135440070"}],"statement":[{"text":"This region lacks electron density in the PDB structure indicating it is disordered.","type":"Results"}]}],"released":"2018_11","uniref100":"","date":"2018-07-26T13:26:19.000Z","acc":"O00429-3","name":"Isoform 2 of Dynamin-1-like protein","length":710,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00001614E2","genes":[{"name":{"value":"DNM1L"},"synonyms":[{"value":"DLP1"},{"value":"DRP1"}]}],"disorder_content":0.16619718309859155,"disprot_consensus":{"full":[{"start":74,"end":83,"type":"D"},{"start":503,"end":610,"type":"D"}],"Structural state":[{"start":74,"end":83,"type":"D"},{"start":503,"end":610,"type":"D"}],"Biological process":[{"start":503,"end":610,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":40,"end":109},{"id":"PF00076","name":"RNA recognition motif","start":128,"end":196},{"id":"PF00076","name":"RNA recognition motif","start":221,"end":289},{"id":"PF00076","name":"RNA recognition motif","start":324,"end":392},{"id":"PF00658","name":"MLLE domain","start":498,"end":563}],"gene3D":[{"start":1,"end":113,"id":"3.30.70.330","name":"3.30.70.330"},{"start":115,"end":213,"id":"3.30.70.330","name":"3.30.70.330"},{"start":320,"end":424,"id":"3.30.70.330","name":"3.30.70.330"},{"start":214,"end":319,"id":"3.30.70.330","name":"3.30.70.330"},{"start":487,"end":577,"id":"1.10.1900.10","name":"c-terminal domain of poly(a) binding protein"}]},"uniref50":"UniRef50_P04147","sequence":"MADITDKTAEQLENLNIQDDQKQAATGSESQSVENSSASLYVGDLEPSVSEAHLYDIFSPIGSVSSIRVCRDAITKTSLGYAYVNFNDHEAGRKAIEQLNYTPIKGRLCRIMWSQRDPSLRKKGSGNIFIKNLHPDIDNKALYDTFSVFGDILSSKIATDENGKSKGFGFVHFEEEGAAKEAIDALNGMLLNGQEIYVAPHLSRKERDSQLEETKAHYTNLYVKNINSETTDEQFQELFAKFGPIVSASLEKDADGKLKGFGFVNYEKHEDAVKAVEALNDSELNGEKLYVGRAQKKNERMHVLKKQYEAYRLEKMAKYQGVNLFVKNLDDSVDDEKLEEEFAPYGTITSAKVMRTENGKSKGFGFVCFSTPEEATKAITEKNQQIVAGKPLYVAIAQRKDVRRSQLAQQIQARNQMRYQQATAAAAAAAAGMPGQFMPPMFYGVMPPRGVPFNGPNPQQMNPMGGMPKNGMPPQFRNGPVYGVPPQGGFPRNANDNNQFYQQKQRQALGEQLYKKVSAKTSNEEAAGKITGMILDLPPQEVFPLLESDELFEQHYKEASAAYESFKKEQEQQTEQA","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P04147","disprot_id":"DP01538","ncbi_taxon_id":559292,"regions_counter":5,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":502,"region_id":"DP01538r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Stress-Triggered Phase Separation Is an Adaptive, Evolutionarily Tuned Response. <i> Riback JA, Katanski CD, Kear-Scott JL, Pilipenko EV, Rojek AE, Sosnick TR, Drummond DA. </i> Cell, 2017","statement":[{"text":"The CD spectrum of the unfused wild-type P domain is typical of a denatured protein (Fig. 5A), and we observe no cooperative thermal unfolding transition from 4 to 80°C.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":419,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"28283059","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-09T18:37:11.499Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":502,"region_id":"DP01538r003","released":"2022_03","ec_id":"ECO:0006317","reference_html":"Stress-Triggered Phase Separation Is an Adaptive, Evolutionarily Tuned Response. <i> Riback JA, Katanski CD, Kear-Scott JL, Pilipenko EV, Rojek AE, Sosnick TR, Drummond DA. </i> Cell, 2017","statement":[{"text":"The CD spectrum of the unfused wild-type P domain is typical of a denatured protein (Fig. 5A), and we observe no cooperative thermal unfolding transition from 4 to 80°C.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":419,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"28283059","version":3,"ec_name":"temperature-induced protein unfolding evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-09T18:37:07.757Z"}},{"start":419,"end":502,"reference_id":"28283059","reference_source":"pmid","reference_html":"Stress-Triggered Phase Separation Is an Adaptive, Evolutionarily Tuned Response. <i> Riback JA, Katanski CD, Kear-Scott JL, Pilipenko EV, Rojek AE, Sosnick TR, Drummond DA. </i> Cell, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01538r004","statement":[{"text":"Because the Pab1ΔP lacks an LCR yet retains the ability to phase-separate, we examined its assembly morphology by microscopy. Pab1ΔP assemblies largely retained the droplet-cluster morphology of full-length Pab1 quinary assemblies (Fig. 3G, H). Together, these results point to an electrostatically driven phase-separation dependent on molecular determinants in the RRM regions, which is enhanced, but not solely caused, by the P domain.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-09T19:27:38.130Z"}},{"start":1,"end":577,"reference_id":"28283059","reference_source":"pmid","reference_html":"Stress-Triggered Phase Separation Is an Adaptive, Evolutionarily Tuned Response. <i> Riback JA, Katanski CD, Kear-Scott JL, Pilipenko EV, Rojek AE, Sosnick TR, Drummond DA. </i> Cell, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0043232","term_name":"intracellular non-membrane-bounded organelle","term_namespace":"Cellular component","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01538r005","statement":[{"text":"Pab1 shows diffuse localization under favorable growth conditions (near 30°C), and localizes to stress granules—large cytosolic foci—within minutes of a shift to 46°C (Fig. 1A). At 42°C, Pab1 is not recruited to stress granules detectable by standard fluorescence microscopy (Fig. 1A, (Cherkasov et al., 2013; Wallace et al., 2015)).","type":"Results"},{"text":"After a more severe shock at 46°C, a greater proportion of Pab1 is recruited into small and large sedimentable assemblies (Fig. 1) coincident with stress-granule formation.","type":"Results"},{"text":"We found that 15μM Pab1 (physiological ~20 μM, see Methods) was soluble at 30°C, but demixed to form large particles after a 46°C, 30-minute treatment (Fig. 2A,B).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Organized structure of distinctive morphology and function, not bounded by a lipid bilayer membrane and occurring within the cell. Includes ribosomes, the cytoskeleton and chromosomes.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-09T19:27:37.783Z"}}],"released":"2018_11","uniref100":"UniRef100_P04147","date":"2018-07-26T13:31:41.000Z","acc":"P04147","name":"Polyadenylate-binding protein, cytoplasmic and nuclear","length":577,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":["Condensates-related proteins","RNA-binding proteins"],"UniParc":"UPI0000168D4D","genes":[{"name":{"value":"PAB1"},"olnNames":[{"value":"YER165W"}]}],"alphafold_very_low_content":0.17677642980935876,"disorder_content":0.14558058925476602,"disprot_consensus":{"full":[{"start":1,"end":418,"type":"F"},{"start":419,"end":502,"type":"D"},{"start":503,"end":577,"type":"F"}],"Structural state":[{"start":419,"end":502,"type":"D"}],"Molecular function":[{"start":419,"end":502,"type":"F"}],"Cellular component":[{"start":1,"end":577,"type":"F"}]}},{"features":{"pfam":[{"id":"PF11099","name":"Apoptosis regulator M11L like","start":65,"end":220}],"gene3D":[{"start":51,"end":186,"id":"G3DSA:1.10.437.40"}]},"uniref50":"UniRef50_O57173","sequence":"MLSMFMCNNIVDYVDGIVQDIEDEASNNVDHDYVYPLPENMVYRFDKSTNILDYLSTERDHVMMAVRYYMSKQRLDDLYRQLPTKTRSYIDIINIYCDKVSNDYNRDMNIMYDMASTKSFTVYDINNEVNTILMDNKGLGVRLATISFITELGRRCMNPVKTIKMFTLLSHTICDDCFVDYITDISPPDNTIPNTSTREYLKLIGITAIMFATYKTLKYMIG","taxonomy":["Viruses","Varidnaviria","Bamfordvirae","Nucleocytoviricota","Pokkesviricetes","Chitovirales","Poxviridae","Chordopoxvirinae","Orthopoxvirus","Vaccinia virus"],"uniref90":"UniRef90_O57173","disprot_id":"DP01539","ncbi_taxon_id":126794,"regions_counter":1,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":50,"region_id":"DP01539r001","reference_id":"27151220","start":1,"ec_id":"ECO:0006210","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"In the model, both F1L N termini protrude away from the Bcl-2 fold in an extended configuration spanning residues 1–50 in addition to the N-terminal hexahistidine tag (Fig. 2). The shape of both F1L N termini in the model suggests an absence of ordered secondary structure, thus rendering F1L residues 1–50 unfolded.","type":"Results"}],"curator_id":"vnugnes","released":"2022_03","term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":4,"reference_html":"The N Terminus of the Vaccinia Virus Protein F1L Is an Intrinsically Unstructured Region That Is Not Involved in Apoptosis Regulation. <i> Caria S, Marshall B, Burton RL, Campbell S, Pantaki-Eimany D, Hawkins CJ, Barry M, Kvansakul M. </i> J Biol Chem, 2016","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","cross_refs":[{"db":"SASBDB","id":"SASDBV4"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T12:02:29.499Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_O57173","date":"2018-07-26T13:51:36.000Z","acc":"O57173","name":"Protein F1","length":222,"organism":"Vaccinia virus (strain Ankara)","dataset":["Viral proteins"],"UniParc":"UPI00000F58D6","genes":[{"olnNames":[{"value":"MVA029L"},{"value":"ACAM3000_MVA_029"}]}],"disorder_content":0.22522522522522523,"disprot_consensus":{"full":[{"start":1,"end":50,"type":"D"}],"Structural state":[{"start":1,"end":50,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00620","name":"RhoGAP domain","start":414,"end":565},{"id":"PF25336","name":"C2 domain of synapse defective Rho GAP protein","start":266,"end":385}],"gene3D":[{"start":394,"end":603,"id":"1.10.555.10","name":"Rho GTPase activation protein"}]},"uniref50":"UniRef50_Q9DBZ9","sequence":"MAEPLLRKTFSRLRGREKLPRKKSEAKDRGHPAQRSEPKPPEPEPRVLEGSQAGAEVPPSPETPRSPTRGAYLQSLEPSSRRWVLGGAKPPEEISLGPRTPSSGEPAGEIWYNPIPEEDPRPPAPEPLGSQLASSEPEGPNIQGAAPTSPPTKTSRTKSPGPARRLSMKMKKLPELRRRLSLRSTRTGRDRERTAPAGSVISRYRLDSSVGTPGQASVAGGSRSPRGGYLSDGDSPERPGGPPSPTAFRPYEVGPSARTPPAALWGRLSLHLYGLGGLRPSPGATPRDLCCLLQVDGVARARTGPLRSGPDFLRLDHTFHLELEAARLLRALVLAWDPGVRRHRPCAQGTVLLPTIFRGCQAQQLAVRLEPQGFLYAKLTLSEQQEAPATAEPRVFGLPLQLLVEREQSPGQVPLIIRKCVGQIECRGLRVVGLYRLCGSAAVKKELRDAFEQDSAAVCLSEDVYPDINVITGILKDYLRELPTPLITQPLYQVVLEAMAQGHPSRASLGPEGTRGLLRCLPDVERATLTLLLDHLRLVSSFHTHNRMTPQNXAVCFGPVLLPARQTPSRPRLRSSGPGVTSAVDFKRHIEVLHYLLQSWPDTRRPSDTPDGAVAPYLRPKRQPPLHLPLAGPEVVTRPRGRGGPESPPSNRYAGDWSVCGGDLLPCGRDFLSGPDYDHVTGSDSEEDDDETGEPRGTTDFEDEFDAPFNPHLNLKDFDALILDLERELSKQINVCL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q9DBZ9","disprot_id":"DP01541","ncbi_taxon_id":10090,"regions_counter":3,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":267,"region_id":"DP01541r001","released":"2022_03","ec_id":"ECO:0006317","reference_html":"mSYD1A, a mammalian synapse-defective-1 protein, regulates synaptogenic signaling and vesicle docking. <i> Wentzel C, Sommer JE, Nair R, Stiefvater A, Sibarita JB, Scheiffele P. </i> Neuron, 2013","statement":[{"text":"The murine SYD1A N-terminal domain was resistant to thermal denaturation. Thus, mSYD1A contains an intrinsically disordered domain (IDD) at the N terminus.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":1,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"23791195","version":2,"ec_name":"temperature-induced protein unfolding evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":267,"term_name":"self-inhibition","start":1,"ec_name":"temperature-induced protein unfolding evidence used in manual assertion","statement":[{"text":"Deletion of the intrinsically disordered domain (IDD) and C2 domain resulted in a doubling of mSYD1A GAP activity. The IDD alone as well as the IDD-C2 domain supplied in cis where able to repress activity of the isolated mSYD1A GAP domain. Thus, the mSYD1A GAP activity is regulated through protein-protein interactions with the intrinsically disordered N-terminal domain.","type":"Results"}],"curator_id":"nmurvai","released":"2022_03","term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"23791195","version":3,"reference_html":"mSYD1A, a mammalian synapse-defective-1 protein, regulates synaptogenic signaling and vesicle docking. <i> Wentzel C, Sommer JE, Nair R, Stiefvater A, Sibarita JB, Scheiffele P. </i> Neuron, 2013","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000059","ec_id":"ECO:0006317","region_id":"DP01541r002","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":267,"term_name":"protein binding","start":1,"ec_name":"temperature-induced protein unfolding evidence used in manual assertion","statement":[{"text":"The N-terminal intrinsically disordered domain of mSYD1A is a critical functional module that binds at least three different ligands: the mSYD1A GAP domain, nsec1/munc18-1, and liprin-α2.","type":"Results"}],"curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"23791195","version":3,"reference_html":"mSYD1A, a mammalian synapse-defective-1 protein, regulates synaptogenic signaling and vesicle docking. <i> Wentzel C, Sommer JE, Nair R, Stiefvater A, Sibarita JB, Scheiffele P. </i> Neuron, 2013","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006317","region_id":"DP01541r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q9DBZ9","date":"2018-07-26T14:05:35.000Z","acc":"Q9DBZ9","name":"Rho GTPase-activating protein SYDE1","length":737,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000284C0","genes":[{"name":{"value":"Syde1"}}],"disorder_content":0.3622795115332429,"disprot_consensus":{"full":[{"start":1,"end":267,"type":"D"}],"Structural state":[{"start":1,"end":267,"type":"D"}],"Disorder function":[{"start":1,"end":267,"type":"F"}],"Molecular function":[{"start":1,"end":267,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00104","name":"Ligand-binding domain of nuclear hormone receptor","start":715,"end":887},{"id":"PF00105","name":"Double treble clef zinc finger, C4 type","start":566,"end":633},{"id":"PF02161","name":"Progesterone receptor","start":1,"end":564}],"gene3D":[{"start":555,"end":645,"id":"3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A"},{"start":673,"end":933,"id":"1.10.565.10","name":"Retinoid X Receptor"}]},"uniref50":"UniRef50_P06401","sequence":"MTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPFPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLDTLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQRVLSPLMSRSGCKVGDSSGTAAAHKVLPRGLSPARQLLLPASESPHWSGAPVKPSPQAAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPCASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRATPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYLRPDSEASQSPQYSFESLPQKICLICGDEASGCHYGVLTCGSCKVFFKRAMEGQHNYLCAGRNDCIVDKIRRKNCPACRLRKCCQAGMVLGGRKFKKFNKVRVVRALDAVALPQPVGVPNESQALSQRFTFSPGQDIQLIPPLINLLMSIEPDVIYAGHDNTKPDTSSSLLTSLNQLGERQLLSVVKWSKSLPGFRNLHIDDQITLIQYSWMSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKESSFYSLCLTMWQIPQEFVKLQVSQEEFLCMKVLLLLNTIPLEGLRSQTQFEEMRSSYIRELIKAIGLRQKGVVSSSQRFYQLTKLLDNLHDLVKQLHLYCLNTFIQSRALSVEFPEMMSEVIAAQLPKILAGMVKPLLFHKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P06401","disprot_id":"DP01542","ncbi_taxon_id":9606,"regions_counter":34,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":545,"region_id":"DP01542r001","released":"2023_12","ec_id":"ECO:0007691","reference_html":"Influence of domain interactions on conformational mobility of the progesterone receptor detected by hydrogen/deuterium exchange mass spectrometry. <i> Goswami D, Callaway C, Pascal BD, Kumar R, Edwards DP, Griffin PR. </i> Structure, 2014","statement":[{"text":"As shown by Coomassie stained SDS gels, the PR-NTD was highly susceptible to proteolysis resulting in nearly complete degradation with little intact NTD remaining (Fig. 6a, compare lanes 2 and 6).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24909783","version":3,"ec_name":"cleavage assay evidence used in manual assertion","date":"2023-12-05T11:22:31.438Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:14:46.643Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":566,"region_id":"DP01542r002","released":"2023_12","ec_id":"ECO:0006236","reference_html":"Influence of domain interactions on conformational mobility of the progesterone receptor detected by hydrogen/deuterium exchange mass spectrometry. <i> Goswami D, Callaway C, Pascal BD, Kumar R, Edwards DP, Griffin PR. </i> Structure, 2014","statement":[{"text":"The hinge region and N terminal domain are represented by schematics due to lack of atomic structure. Representative peptide deuterium build up curves from each domain are indicated at top.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24909783","version":3,"ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","date":"2023-12-05T11:08:37.555Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:36709","statements":[{"type":"Results","text":"We investigated the conformational flexibility of full length PR-A and PR-B bound to the hormone agonist R5020 and the results are displayed in Figure 1 (also Supplementary Fig. S2 and Supplementary Fig. S3)."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:14:52.474Z"}},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":641,"term_name":"protein binding","start":632,"ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","statement":[{"text":"However, substitution of two other residues in the CTE (R637A/K638A), which undergo chemical shift changes, abolished JDP2 binding (Fig. 4B). Truncation mutations of the CTE constructs were also examined for their effects on binding to JDP2 (Fig. 5A). JDP2 bound with equal efficiency to CTE constructs deleted from aa 650 to 648 and to 641, whereas no binding was detected with further deletion of the CTE to aa 632 (Fig. 5B). These data collectively indicate that residues in the CTE closest to the core DBD (aa 632–641) are most important for binding JDP2 and that residues in the core are dispensable.","type":"Introduction"}],"curator_id":"vnugnes","released":"2023_12","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"19553667","version":4,"reference_html":"A progesterone receptor co-activator (JDP2) mediates activity through interaction with residues in the carboxyl-terminal extension of the DNA binding domain. <i> Hill KK, Roemer SC, Jones DN, Churchill ME, Edwards DP. </i> J Biol Chem, 2009","date":"2023-12-01T15:52:20.569Z","term_id":"GO:0005515","ec_id":"ECO:0007089","region_id":"DP01542r006","ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"curator_orcid":"0000-0001-8399-7907","interaction_partner":[{"db":"UniProt","id":"Q8WYK2","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:17:36.394Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":545,"region_id":"DP01542r007","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding. <i> Kumar R, Moure CM, Khan SH, Callaway C, Grimm SL, Goswami D, Griffin PR, Edwards DP. </i> J Biol Chem, 2013","statement":[{"text":"Far UV CD spectroscopy was used to examine secondary structure of the PR NTD. The CD spectrum exhibited little or no negative ellipticity at 222 nm and has a large negative maximum below 210 nm that is typical of protein without a stable α-helix and random coil conformation (Fig. 1D).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":165,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"23995840","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-12-01T10:52:02.557Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sequence_construct":"HHHHHHMSRSGCKVGDSSGTAAAHKVLPRGLSPARQLLLPASESPHWSGAPVKPSPQAAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPCASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRATPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYL","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:15:00.821Z"}},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":545,"term_name":"disorder to order","start":165,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"An increase in negative ellipticity at 222 nm and a decrease <210 nm was observed in the presence of TMAO indicative of a gain in α-helical content and a reduction in random coil (Fig. 1D).","type":"Results"}],"curator_id":"vnugnes","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"23995840","version":3,"reference_html":"Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding. <i> Kumar R, Moure CM, Khan SH, Callaway C, Grimm SL, Goswami D, Griffin PR, Edwards DP. </i> J Biol Chem, 2013","date":"2023-12-01T10:53:32.014Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP01542r008","ec_go":"EXP","disprot_namespace":"Structural transition","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15724","entry_name":"trimethylamine N-oxide"}],"sequence_construct":"HHHHHHMSRSGCKVGDSSGTAAAHKVLPRGLSPARQLLLPASESPHWSGAPVKPSPQAAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPCASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRATPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYL","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:16:43.111Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":545,"region_id":"DP01542r010","released":"2023_12","ec_id":"ECO:0006236","reference_html":"Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding. <i> Kumar R, Moure CM, Khan SH, Callaway C, Grimm SL, Goswami D, Griffin PR, Edwards DP. </i> J Biol Chem, 2013","statement":[{"text":"The overlay shows that NTD and hinge exhibit the highest rate of hydrogen-deuterium exchange, whereas structurally stable helices in the LBD and DBD exhibit dramatically less exchange. These results demonstrate the highly dynamic unstructured properties of the NTD in the context of the intact receptor.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":165,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"23995840","version":3,"ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","date":"2023-12-01T13:15:30.466Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"curator_orcid":"0000-0001-8399-7907","sequence_construct":"HHHHHHMTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPFPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLDTLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQRVLSPLMSRSGCKVGDSSGTAAAHKVLPRGLSPARQLLLPASESPHWSGAPVKPSPQAAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPCASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRATPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYL","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:15:23.244Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":545,"region_id":"DP01542r011","released":"2023_12","ec_id":"ECO:0007691","reference_html":"Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding. <i> Kumar R, Moure CM, Khan SH, Callaway C, Grimm SL, Goswami D, Griffin PR, Edwards DP. </i> J Biol Chem, 2013","statement":[{"text":"The PR NTD was highly susceptible to proteolytic degradation resulting in nearly complete degradation with little or no intact NTD remaining (Fig. 6A, compare lane 1 with lane 3).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":165,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"23995840","version":3,"ec_name":"cleavage assay evidence used in manual assertion","date":"2023-12-01T13:35:05.296Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:15:27.315Z"}},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":428,"term_name":"disorder to order","start":350,"ec_name":"cleavage assay evidence used in manual assertion","statement":[{"text":"). When PR NTD and TBPC were mixed together, protected PR NTD fragments were detected, and the patterns were distinct with each mAb indicating that multiple sites within the NTD change their accessibility to trypsin in the presence of TBPC (Fig. 6B). Protection against partial proteolysis indicates that the NTD folds into a more compact conformation when complexed with TBPC in addition to the increased secondary structure detected by CD analysis.","type":"Results"},{"text":"CD experiments show the region that changes to a more ordered state upon TBOC binding is the 350-428.","type":"Curator statement"}],"curator_id":"vnugnes","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"23995840","version":3,"reference_html":"Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding. <i> Kumar R, Moure CM, Khan SH, Callaway C, Grimm SL, Goswami D, Griffin PR, Edwards DP. </i> J Biol Chem, 2013","date":"2023-12-01T15:38:34.909Z","term_id":"IDPO:0000011","ec_id":"ECO:0007691","region_id":"DP01542r012","ec_go":"IDA","disprot_namespace":"Structural transition","curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20226"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:16:58.530Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":535,"region_id":"DP01542r013","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Regulation of the amino-terminal transcription activation domain of progesterone receptor by a cofactor-induced protein folding mechanism. <i> Wardell SE, Kwok SC, Sherman L, Hodges RS, Edwards DP. </i> Mol Cell Biol, 2005","statement":[{"text":"The AnDBD fragment of PR absorbs with a small negative peak at 222 nm but exhibits much more absorbance below 210 nm (Fig.3A). A similar spectrum was obtained with the single-domain AN polypeptide (Fig. ​3B), indicating that both PR polypeptides contain a large amount of random coil with some underlying helical content.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":165,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16199860","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-12-01T10:00:01.308Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:15:35.259Z"}},{"start":165,"end":545,"reference_id":"23995840","reference_source":"pmid","reference_html":"Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding. <i> Kumar R, Moure CM, Khan SH, Callaway C, Grimm SL, Goswami D, Griffin PR, Edwards DP. </i> J Biol Chem, 2013","date":"2023-12-01T10:56:32.082Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"region_id":"DP01542r016","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15724","entry_name":"trimethylamine N-oxide"}],"sequence_construct":"HHHHHHMSRSGCKVGDSSGTAAAHKVLPRGLSPARQLLLPASESPHWSGAPVKPSPQAAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPCASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRATPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYL","statement":[{"text":"A more compact structure was also shown by the increased intensity of fluorescence signal and blue shift of maximal wavelength. The apparent thermodynamic parameters of TMAO-induced folding are ΔG = −3.6 ± 0.7; m = 2.2 ± 0.4 (Fig. 1B).","type":"Results"},{"text":"Both the increase in quantum yield and the blue shift in fluorescence maximum indicate the formation of a compact structure in the presence of TMAO. The conformational transition in the PR NTD occurs in a cooperative manner, as shown by monitoring the level of fluorescence at 329 nm (upon excitation at 278) and the shift in emission maximum as a function of TMAO concentration (Fig. 1C).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:17:02.003Z"}},{"start":1,"end":545,"reference_id":"23995840","reference_source":"pmid","reference_html":"Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding. <i> Kumar R, Moure CM, Khan SH, Callaway C, Grimm SL, Goswami D, Griffin PR, Edwards DP. </i> J Biol Chem, 2013","date":"2023-12-01T11:38:19.033Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"region_id":"DP01542r017","sequence_construct":"HHHHHHMTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPFPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLDTLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQRVLSPLMSRSGCKVGDSSGTAAAHKVLPRGLSPARQLLLPASESPHWSGAPVKPSPQAAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPCASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRATPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYL","statement":[{"text":"Both FE and CD analysis demonstrated that the NTD is largely unstructured under native conditions and acquires a substantial increase in α-helical content and a more compact tertiary structure in the presence of the natural osmolyte TMAO. ","type":"Results"},{"text":" Similar results were obtained with NTD of PR-B (data not shown).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:15:43.628Z"}},{"start":1,"end":545,"reference_id":"23995840","reference_source":"pmid","reference_html":"Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding. <i> Kumar R, Moure CM, Khan SH, Callaway C, Grimm SL, Goswami D, Griffin PR, Edwards DP. </i> J Biol Chem, 2013","date":"2023-12-01T11:38:29.034Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"region_id":"DP01542r018","sequence_construct":"HHHHHHMTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPFPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLDTLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQRVLSPLMSRSGCKVGDSSGTAAAHKVLPRGLSPARQLLLPASESPHWSGAPVKPSPQAAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPCASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRATPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYL","statement":[{"text":"Both FE and CD analysis demonstrated that the NTD is largely unstructured under native conditions and acquires a substantial increase in α-helical content and a more compact tertiary structure in the presence of the natural osmolyte TMAO. ","type":"Results"},{"text":" Similar results were obtained with NTD of PR-B (data not shown).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:15:56.905Z"}},{"start":165,"end":559,"reference_id":"23995840","reference_source":"pmid","reference_html":"Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding. <i> Kumar R, Moure CM, Khan SH, Callaway C, Grimm SL, Goswami D, Griffin PR, Edwards DP. </i> J Biol Chem, 2013","date":"2023-12-05T11:10:19.858Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"region_id":"DP01542r019","sequence_construct":"HHHHHHMTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPFPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLDTLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQRVLSPLMSRSGCKVGDSSGTAAAHKVLPRGLSPARQLLLPASESPHWSGAPVKPSPQAAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPCASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRATPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYL","statement":[{"text":"The overlay shows that NTD and hinge exhibit the highest rate of hydrogen-deuterium exchange, whereas structurally stable helices in the LBD and DBD exhibit dramatically less exchange. These results demonstrate the highly dynamic unstructured properties of the NTD in the context of the intact receptor.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:16:20.199Z"}},{"start":632,"end":682,"reference_id":"23995840","reference_source":"pmid","reference_html":"Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding. <i> Kumar R, Moure CM, Khan SH, Callaway C, Grimm SL, Goswami D, Griffin PR, Edwards DP. </i> J Biol Chem, 2013","date":"2023-12-05T11:28:06.676Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006196","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"region_id":"DP01542r020","sequence_construct":"HHHHHHMTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPFPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLDTLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQRVLSPLMSRSGCKVGDSSGTAAAHKVLPRGLSPARQLLLPASESPHWSGAPVKPSPQAAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPCASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRATPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYL","statement":[{"text":"The overlay shows that NTD and hinge exhibit the highest rate of hydrogen-deuterium exchange, whereas structurally stable helices in the LBD and DBD exhibit dramatically less exchange. These results demonstrate the highly dynamic unstructured properties of the NTD in the context of the intact receptor.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:16:38.117Z"}},{"start":1,"end":545,"reference_id":"23995840","reference_source":"pmid","reference_html":"Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding. <i> Kumar R, Moure CM, Khan SH, Callaway C, Grimm SL, Goswami D, Griffin PR, Edwards DP. </i> J Biol Chem, 2013","date":"2023-12-01T13:25:52.322Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P20226","operator":null,"partner_start":159,"partner_end":339}],"region_id":"DP01542r021","sequence_construct":"HHHHHHMTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPFPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLDTLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQRVLSPLMSRSGCKVGDSSGTAAAHKVLPRGLSPARQLLLPASESPHWSGAPVKPSPQAAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPCASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRATPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYL","statement":[{"text":"Full-length PR-B also bound specifically with TBPC by GST-pulldown assay with similar efficiency as the isolated PR-B NTD (Fig. 3C). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:17:39.434Z"}},{"start":165,"end":545,"reference_id":"23995840","reference_source":"pmid","reference_html":"Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding. <i> Kumar R, Moure CM, Khan SH, Callaway C, Grimm SL, Goswami D, Griffin PR, Edwards DP. </i> J Biol Chem, 2013","date":"2023-12-01T13:26:43.346Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P20226","operator":null,"partner_start":159,"partner_end":339}],"region_id":"DP01542r022","sequence_construct":"HHHHHHMTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPFPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLDTLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQRVLSPLMSRSGCKVGDSSGTAAAHKVLPRGLSPARQLLLPASESPHWSGAPVKPSPQAAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPCASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRATPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYL","statement":[{"text":"The NTD of PR-A exhibited specific binding with immobilized TBPC-GST over that of free GST, and the binding increased with varying amounts of input PR-A NTD (Fig. 3, A and B). Full-length PR-B also bound specifically with TBPC by GST-pulldown assay with similar efficiency as the isolated PR-B NTD (Fig. 3C).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:18:04.280Z"}},{"start":165,"end":545,"reference_id":"23995840","reference_source":"pmid","reference_html":"Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding. <i> Kumar R, Moure CM, Khan SH, Callaway C, Grimm SL, Goswami D, Griffin PR, Edwards DP. </i> J Biol Chem, 2013","date":"2023-12-01T13:27:44.460Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P20226","operator":null,"partner_start":159,"partner_end":339}],"region_id":"DP01542r023","sequence_construct":"HHHHHHMTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPFPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLDTLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQRVLSPLMSRSGCKVGDSSGTAAAHKVLPRGLSPARQLLLPASESPHWSGAPVKPSPQAAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPCASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRATPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYL","statement":[{"text":"The overall binding showed a moderate rate of association and a slow dissociation pattern with a calculated binding affinity (KD) of 0.17 μm (Fig. 4D). TBPC binding by SPR with isolated PR domains was only detected with NTD (Fig. 4E) but not with LBD as analyte (data not shown).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:18:10.453Z"}},{"start":350,"end":428,"reference_id":"23995840","reference_source":"pmid","reference_html":"Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding. <i> Kumar R, Moure CM, Khan SH, Callaway C, Grimm SL, Goswami D, Griffin PR, Edwards DP. </i> J Biol Chem, 2013","date":"2023-12-01T13:45:56.320Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"region_id":"DP01542r024","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20226"}],"sequence_construct":"HHHHHHMTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPFPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLDTLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQRVLSPLMSRSGCKVGDSSGTAAAHKVLPRGLSPARQLLLPASESPHWSGAPVKPSPQAAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPCASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRATPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYL","statement":[{"text":"The experimental summation of CD spectra of the protein mixtures was only different from the theoretical with the aa 350–428 fragment. No differential was detected with the other NTD fragments indicating that TBP interaction and associated structural changes require a region of the PR NTD between aa 350 and 428 (Fig. 7B).\n","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:17:22.970Z"}},{"start":350,"end":428,"reference_id":"23995840","reference_source":"pmid","reference_html":"Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding. <i> Kumar R, Moure CM, Khan SH, Callaway C, Grimm SL, Goswami D, Griffin PR, Edwards DP. </i> J Biol Chem, 2013","date":"2023-12-01T13:46:28.998Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P20226","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01542r025","sequence_construct":"HHHHHHMTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPFPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLDTLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQRVLSPLMSRSGCKVGDSSGTAAAHKVLPRGLSPARQLLLPASESPHWSGAPVKPSPQAAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPCASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRATPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYL","statement":[{"text":"The experimental summation of CD spectra of the protein mixtures was only different from the theoretical with the aa 350–428 fragment. No differential was detected with the other NTD fragments indicating that TBP interaction and associated structural changes require a region of the PR NTD between aa 350 and 428 (Fig. 7B).\n","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:18:20.989Z"}},{"start":636,"end":654,"reference_id":"23995840","reference_source":"pmid","reference_html":"Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding. <i> Kumar R, Moure CM, Khan SH, Callaway C, Grimm SL, Goswami D, Griffin PR, Edwards DP. </i> J Biol Chem, 2013","date":"2023-12-01T15:59:21.829Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":null}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P20226","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01542r026","statement":[{"text":"To further explore the role of the CTE in binding JDP2, a synthetic peptide corresponding to CTE sequence aa 636–654 (Fig. 6A) was tested for its ability to compete for JDP2 binding to PR. The CTE peptide inhibited the interaction between JDP2 bZIP and DBD-CTE650 in a GST pulldown assay, whereas a scrambled control peptide with the same amino acid composition had little effect (Fig. 6B). This result indicates that the CTE alone is sufficient for binding JDP2 and that a specific sequence is required.\n","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:18:29.757Z"}},{"start":637,"end":641,"reference_id":"20861224","reference_source":"pmid","reference_html":"The progesterone receptor hinge region regulates the kinetics of transcriptional responses through acetylation, phosphorylation, and nuclear retention. <i> Daniel AR, Gaviglio AL, Czaplicki LM, Hillard CJ, Housa D, Lange CA. </i> Mol Endocrinol, 2010","date":"2023-12-05T13:59:52.038Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000039","term_name":"acetylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys638Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To confirm that PR acetylation was indeed occurring at the putative consensus sequence (Fig. 2A) located in the hinge region (15), we created a series of mutations. Initially, we mutated the last two aa of the KXKK motif to Ala, dubbed KK6, because this uncharged residue is unable to accept acetyl group modification."},{"type":"Results","text":"This prompted us to mutate all three Lys residues in the hinge region motif to Ala (K-A) (Fig. 2A)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys640Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To confirm that PR acetylation was indeed occurring at the putative consensus sequence (Fig. 2A) located in the hinge region (15), we created a series of mutations. Initially, we mutated the last two aa of the KXKK motif to Ala, dubbed KK6, because this uncharged residue is unable to accept acetyl group modification."},{"type":"Results","text":"This prompted us to mutate all three Lys residues in the hinge region motif to Ala (K-A) (Fig. 2A)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys641Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To confirm that PR acetylation was indeed occurring at the putative consensus sequence (Fig. 2A) located in the hinge region (15), we created a series of mutations. Initially, we mutated the last two aa of the KXKK motif to Ala, dubbed KK6, because this uncharged residue is unable to accept acetyl group modification."},{"type":"Results","text":"This prompted us to mutate all three Lys residues in the hinge region motif to Ala (K-A) (Fig. 2A)."}]}],"region_id":"DP01542r027","statement":[{"text":"Again, KK6 displayed decreased levels of acetylation, suggestive that some K638 is acetylated in this mutant receptor. However, K-A PR-B, containing all three Lys to Ala mutations, appeared unmodified relative to R5020-treated wt PR-B. These data indicate that PR-B is acetylated at two or more Lys residues within the KXKK motif in the hinge region and disruption of all three Lys residues is necessary to abolish PR acetylation.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:18:42.306Z"}},{"start":188,"end":192,"reference_id":"20861224","reference_source":"pmid","reference_html":"The progesterone receptor hinge region regulates the kinetics of transcriptional responses through acetylation, phosphorylation, and nuclear retention. <i> Daniel AR, Gaviglio AL, Czaplicki LM, Hillard CJ, Housa D, Lange CA. </i> Mol Endocrinol, 2010","date":"2023-12-05T14:04:13.632Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01542r028","statement":[{"text":"We first tested K-A PR-B phosphorylation relative to wt using Western blotting and the available antibodies to CDK2 phosphorylation sites Ser190 and Ser400 and to the MAPK sites Ser294 and Ser345 (29, 31).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:18:58.864Z"}},{"start":398,"end":402,"reference_id":"20861224","reference_source":"pmid","reference_html":"The progesterone receptor hinge region regulates the kinetics of transcriptional responses through acetylation, phosphorylation, and nuclear retention. <i> Daniel AR, Gaviglio AL, Czaplicki LM, Hillard CJ, Housa D, Lange CA. </i> Mol Endocrinol, 2010","date":"2023-12-05T14:04:25.137Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01542r029","statement":[{"text":"We first tested K-A PR-B phosphorylation relative to wt using Western blotting and the available antibodies to CDK2 phosphorylation sites Ser190 and Ser400 and to the MAPK sites Ser294 and Ser345 (29, 31).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:19:18.286Z"}},{"start":292,"end":296,"reference_id":"20861224","reference_source":"pmid","reference_html":"The progesterone receptor hinge region regulates the kinetics of transcriptional responses through acetylation, phosphorylation, and nuclear retention. <i> Daniel AR, Gaviglio AL, Czaplicki LM, Hillard CJ, Housa D, Lange CA. </i> Mol Endocrinol, 2010","date":"2023-12-05T14:04:34.634Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01542r030","statement":[{"text":"We first tested K-A PR-B phosphorylation relative to wt using Western blotting and the available antibodies to CDK2 phosphorylation sites Ser190 and Ser400 and to the MAPK sites Ser294 and Ser345 (29, 31).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:19:53.032Z"}},{"start":342,"end":347,"reference_id":"20861224","reference_source":"pmid","reference_html":"The progesterone receptor hinge region regulates the kinetics of transcriptional responses through acetylation, phosphorylation, and nuclear retention. <i> Daniel AR, Gaviglio AL, Czaplicki LM, Hillard CJ, Housa D, Lange CA. </i> Mol Endocrinol, 2010","date":"2023-12-05T14:04:43.176Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01542r031","statement":[{"text":"We first tested K-A PR-B phosphorylation relative to wt using Western blotting and the available antibodies to CDK2 phosphorylation sites Ser190 and Ser400 and to the MAPK sites Ser294 and Ser345 (29, 31).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:20:14.273Z"}},{"start":637,"end":641,"reference_id":"20861224","reference_source":"pmid","reference_html":"The progesterone receptor hinge region regulates the kinetics of transcriptional responses through acetylation, phosphorylation, and nuclear retention. <i> Daniel AR, Gaviglio AL, Czaplicki LM, Hillard CJ, Housa D, Lange CA. </i> Mol Endocrinol, 2010","date":"2023-12-05T14:10:23.783Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042326","term_name":"negative regulation of phosphorylation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys338Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"This prompted us to mutate all three Lys residues in the hinge region motif to Ala (K-A) (Fig. 2A)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys400Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"This prompted us to mutate all three Lys residues in the hinge region motif to Ala (K-A) (Fig. 2A)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys401Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"This prompted us to mutate all three Lys residues in the hinge region motif to Ala (K-A) (Fig. 2A)."}]}],"ec_go":"IEP","region_id":"DP01542r032","statement":[{"text":"We first tested K-A PR-B phosphorylation relative to wt using Western blotting and the available antibodies to CDK2 phosphorylation sites Ser190 and Ser400 and to the MAPK sites Ser294 and Ser345 (29, 31).","type":"Results"},{"text":"Wt PR underwent a ligand-dependent upshift at 30 min of treatment. However, acetylation-deficient mutant PR exhibited a delay for at least 3 h of progestin exposure. Basally phosphorylated Ser190, however, is comparatively well phosphorylated between wt and K-A PR-B. Wt PR displayed heightened Ser294, Ser345, and Ser400 phosphorylation after 30 min of progestin, whereas K-A phosphorylation at these sites was not robust until at least 3 h.","type":"Results"}],"term_comment":"","term_def":"\"Any process that stops, prevents or decreases the rate of addition of phosphate groups to a molecule.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:20:00.718Z"}},{"start":637,"end":641,"reference_id":"20861224","reference_source":"pmid","reference_html":"The progesterone receptor hinge region regulates the kinetics of transcriptional responses through acetylation, phosphorylation, and nuclear retention. <i> Daniel AR, Gaviglio AL, Czaplicki LM, Hillard CJ, Housa D, Lange CA. </i> Mol Endocrinol, 2010","date":"2023-12-05T14:15:38.221Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051457","term_name":"maintenance of protein location in nucleus","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys338Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"This prompted us to mutate all three Lys residues in the hinge region motif to Ala (K-A) (Fig. 2A)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys400Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"This prompted us to mutate all three Lys residues in the hinge region motif to Ala (K-A) (Fig. 2A)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys401Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"This prompted us to mutate all three Lys residues in the hinge region motif to Ala (K-A) (Fig. 2A)."}]}],"ec_go":"IMP","region_id":"DP01542r033","statement":[{"text":"To test this possibility we transiently transfected HeLa cells with wt or K-A PR-B, serum starved, and then treated cells with R5020 (1 h) before subcellular fractionation and Western blotting (Fig. 4A). WCL were run next to cytoplasmic and nuclear fractions as controls for total PR levels among the cells. Wt PR-B was present in both the cytoplasm and the nucleus in the absence of progestin. Upon treatment, a robust band appeared in the nuclear fraction. Acetylation-deficient PR-B, however, was not detectable in the nucleus in both the absence and presence of ligand.","type":"Results"},{"text":"Taken together, these data indicate that rapid nuclear localization precedes efficient PR-B phosphorylation events; nuclear retention may facilitate persistent PR phosphorylation.","type":"Results"},{"text":"Acetylation motif mutant PR displays defective nuclear retention","type":"Results"}],"term_comment":"","term_def":"\"Any process in which a protein is maintained in the nucleus and prevented from moving elsewhere. These include sequestration within the nucleus, protein stabilization to prevent transport elsewhere and the active retrieval of proteins that escape the nucleus.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:19:57.490Z"}},{"start":637,"end":641,"reference_id":"20861224","reference_source":"pmid","reference_html":"The progesterone receptor hinge region regulates the kinetics of transcriptional responses through acetylation, phosphorylation, and nuclear retention. <i> Daniel AR, Gaviglio AL, Czaplicki LM, Hillard CJ, Housa D, Lange CA. </i> Mol Endocrinol, 2010","date":"2023-12-05T14:27:33.383Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006355","term_name":"regulation of transcription, DNA-templated","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001567","ec_ontology":"ECO","ec_name":"quantitative reverse transcription polymerase chain reaction evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys338Thr","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys400Thr","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys401Thr","start":null,"end":null,"position":null}],"ec_go":"EXP","region_id":"DP01542r034","statement":[{"text":"In response to progestin, wt PR-B robustly induced SGK expression, whereas both K-Q and K-T PR-B exhibited a weak transcriptional response to ligand. In similar experiments, TF gene regulation was assessed for wt, K-Q, and K-T PR-B at 18 h of progestin treatment. Again, regulation of TF mRNA in response to progestins was not altered by PR acetylation (data not shown). These data indicate that PR acetylation selectively inhibits hormone-dependent PR transcriptional responses on specific promoter contexts (SGK), whereas other promoters (c-myc and TF) remain insensitive to this modification (Fig. 8).","type":"Results"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.\" [GOC:go_curators, GOC:txnOH]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:36709"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:19:54.999Z"}}],"released":"2018_11","uniref100":"UniRef100_P06401","date":"2018-07-26T14:45:57.000Z","acc":"P06401","name":"Progesterone receptor","length":933,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI00001504D7","genes":[{"name":{"value":"PGR"},"synonyms":[{"value":"NR3C3"}]}],"alphafold_very_low_content":0.6312968917470525,"disorder_content":0.6613076098606645,"disprot_consensus":{"full":[{"start":1,"end":164,"type":"D"},{"start":165,"end":545,"type":"T"},{"start":546,"end":566,"type":"D"},{"start":632,"end":682,"type":"D"}],"Structural state":[{"start":1,"end":566,"type":"D"},{"start":632,"end":682,"type":"D"}],"Molecular function":[{"start":1,"end":545,"type":"F"},{"start":632,"end":654,"type":"F"}],"Structural transition":[{"start":165,"end":545,"type":"T"}],"Disorder function":[{"start":188,"end":192,"type":"F"},{"start":292,"end":296,"type":"F"},{"start":342,"end":347,"type":"F"},{"start":398,"end":402,"type":"F"},{"start":637,"end":641,"type":"F"}],"Biological process":[{"start":637,"end":641,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":126,"end":289},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":474,"end":589},{"id":"PF00636","name":"Ribonuclease III domain","start":1119,"end":1251},{"id":"PF00636","name":"Ribonuclease III domain","start":1327,"end":1436},{"id":"PF03368","name":"Dicer dimerisation domain","start":656,"end":744},{"id":"PF14709","name":"double strand RNA binding domain from DEAD END PROTEIN 1","start":1621,"end":1696}],"gene3D":[{"start":651,"end":752,"id":"3.30.160.380","name":"Dicer dimerisation domain"},{"start":1286,"end":1454,"id":"1.10.1520.10","name":"Ribonuclease III domain"},{"start":463,"end":626,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":1455,"end":1536,"id":"3.30.160.20","name":"3.30.160.20"},{"start":1627,"end":1697,"id":"3.30.160.20","name":"3.30.160.20"},{"start":123,"end":360,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":952,"end":1063,"id":"2.170.260.10","name":"paz domain"}]},"uniref50":"UniRef50_P84634","sequence":"MRDEVDLSLTIPSKLLGKRDREQKNCEEEKNKNKKAKKQQKDPILLHTSAATHKFLPPPLTMPYSEIGDDLRSLDFDHADVSSDLHLTSSSSVSSFSSSSSSLFSAAGTDDPSPKMEKDPRKIARRYQVELCKKATEENVIVYLGTGCGKTHIAVMLIYELGHLVLSPKKSVCIFLAPTVALVEQQAKVIADSVNFKVAIHCGGKRIVKSHSEWEREIAANEVLVMTPQILLHNLQHCFIKMECISLLIFDECHHAQQQSNHPYAEIMKVFYKSESLQRPRIFGMTASPVVGKGSFQSENLSKSINSLENLLNAKVYSVESNVQLDGFVSSPLVKVYYYRSALSDASQSTIRYENMLEDIKQRCLASLKLLIDTHQTQTLLSMKRLLKRSHDNLIYTLLNLGLWGAIQAAKIQLNSDHNVQDEPVGKNPKSKICDTYLSMAAEALSSGVAKDENASDLLSLAALKEPLFSRKLVQLIKILSVFRLEPHMKCIIFVNRIVTARTLSCILNNLELLRSWKSDFLVGLSSGLKSMSRRSMETILKRFQSKELNLLVATKVGEEGLDIQTCCLVIRYDLPETVTSFIQSRGRARMPQSEYAFLVDSGNEKEMDLIENFKVNEDRMNLEITYRSSEETCPRLDEELYKVHETGACISGGSSISLLYKYCSRLPHDEFFQPKPEFQFKPVDEFGGTICRITLPANAPISEIESSLLPSTEAAKKDACLKAVHELHNLGVLNDFLLPDSKDEIEDELSDDEFDFDNIKGEGCSRGDLYEMRVPVLFKQKWDPSTSCVNLHSYYIMFVPHPADRIYKKFGFFMKSPLPVEAETMDIDLHLAHQRSVSVKIFPSGVTEFDNDEIRLAELFQEIALKVLFERGELIPDFVPLELQDSSRTSKSTFYLLLPLCLHDGESVISVDWVTIRNCLSSPIFKTPSVLVEDIFPPSGSHLKLANGCWNIDDVKNSLVFTTYSKQFYFVADICHGRNGFSPVKESSTKSHVESIYKLYGVELKHPAQPLLRVKPLCHVRNLLHNRMQTNLEPQELDEYFIEIPPELSHLKIKGLSKDIGSSLSLLPSIMHRMENLLVAIELKHVLSASIPEIAEVSGHRVLEALTTEKCHERLSLERLEVLGDAFLKFAVSRHLFLHHDSLDEGELTRRRSNVVNNSNLCRLAIKKNLQVYIRDQALDPTQFFAFGHPCRVTCDEVASKEVHSLNRDLGILESNTGEIRCSKGHHWLYKKTIADVVEALVGAFLVDSGFKGAVKFLKWIGVNVDFESLQVQDACIASRRYLPLTTRNNLETLENQLDYKFLHKGLLVQAFIHPSYNRHGGGCYQRLEFLGDAVLDYLMTSYFFTVFPKLKPGQLTDLRSLSVNNEALANVAVSFSLKRFLFCESIYLHEVIEDYTNFLASSPLASGQSEGPRCPKVLGDLVESCLGALFLDCGFNLNHVWTMMLSFLDPVKNLSNLQISPIKELIELCQSYKWDREISATKKDGAFTVELKVTKNGCCLTVSATGRNKREGTKKAAQLMITNLKAHENITTSHPLEDVLKNGIRNEAKLIGYNEDPIDVVDLVGLDVENLNILETFGGNSERSSSYVIRRGLPQAPSKTEDRLPQKAIIKAGGPSSKTAKSLLHETCVANCWKPPHFECCEEEGPGHLKSFVYKVILEVEDAPNMTLECYGEARATKKGAAEHAAQAAIWCLKHSGFLC","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_P84634","disprot_id":"DP01543","ncbi_taxon_id":3702,"regions_counter":1,"creator":"jmanso","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":752,"region_id":"DP01543r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of the Arabidopsis thaliana DCL4 DUF283 domain reveals a noncanonical double-stranded RNA-binding fold for protein-protein interaction. <i> Qin H, Chen F, Huan X, Machida S, Song J, Yuan YA. </i> RNA, 2010","statement":[{"text":"Interestingly, it appears that the C-terminal ∼18 residues (residues: 735–752) are relatively unstructured and poorly defined, having distinct conformations in different structures. This observation is in good agreement with the small chemical shift deviations and lack of the interresidual NOE connectivites over the region","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jmanso","start":735,"term_ontology":"IDPO","curator_name":"Jose A Manso","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2KOU"}],"reference_id":"20106953","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P84634","date":"2018-07-26T14:49:11.000Z","acc":"P84634","name":"Dicer-like protein 4","length":1702,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI00005B2BAD","genes":[{"name":{"value":"DCL4"},"orfNames":[{"value":"F5O24.210"}],"olnNames":[{"value":"At5g20320"}]}],"alphafold_very_low_content":0.16039952996474735,"disorder_content":0.010575793184488837,"disprot_consensus":{"full":[{"start":735,"end":752,"type":"D"}],"Structural state":[{"start":735,"end":752,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00017","name":"SH2 domain","start":346,"end":429}],"gene3D":[{"start":346,"end":453,"id":"3.30.505.10","name":"SH2 domain"}]},"uniref50":"UniRef50_Q8WV28","sequence":"MDKLNKITVPASQKLRQLQKMVHDIKNNEGGIMNKIKKLKVKAPPSVPRRDYASESPADEEEQWSDDFDSDYENPDEHSDSEMYVMPAEENADDSYEPPPVEQETRPVHPALPFARGEYIDNRSSQRHSPPFSKTLPSKPSWPSEKARLTSTLPALTALQKPQVPPKPKGLLEDEADYVVPVEDNDENYIHPTESSSPPPEKAPMVNRSTKPNSSTPASPPGTASGRNSGAWETKSPPPAAPSPLPRAGKKPTTPLKTTPVASQQNASSVCEEKPIPAERHRGSSHRQEAVQSPVFPPAQKQIHQKPIPLPRFTEGGNPTVDGPLPSFSSNSTISEQEAGVLCKPWYAGACDRKSAEEALHRSNKDGSFLIRKSSGHDSKQPYTLVVFFNKRVYNIPVRFIEATKQYALGRKKNGEEYFGSVAEIIRNHQHSPLVLIDSQNNTKDSTRLKYAVKVS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q8WV28","disprot_id":"DP01544","ncbi_taxon_id":9606,"regions_counter":5,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":50,"region_id":"DP01544r001","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Macromolecular assembly of the adaptor SLP-65 at intracellular vesicles in resting B cells. <i> Engelke M, Pirkuliyeva S, Kühn J, Wong L, Boyken J, Herrmann N, Becker S, Griesinger C, Wienands J. </i> Sci Signal, 2014","statement":[{"text":"The chemical shift dispersion of the backbone amides is about 1 part per million (ppm), which is compatible with the intrinsically disordered conformation of the N terminus in aqueous solution.","type":"Figure"},{"text":"This result was further corroborated by nuclear magnetic resonance (NMR) spectroscopy, which demonstrated that the isolated SLP-65 N terminus was intrinsically disordered in solution (Fig. 1D and fig. S5) as inferred from calculations based on the chemical shifts of backbone amides, Cα and Cβ resonances (14).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":5,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"25140054","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-12-05T15:06:19.829Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","sequence_construct":"GSNKITVPASQKLRQLQKMVHDIKNNEGGIMNKIKKLKVKAPPSVPRR","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:13:14.364Z"}},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":50,"term_name":"lipid binding","start":5,"ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","statement":[{"text":"We therefore prepared small unilamellar vesicles (SUVs) composed of 75% phosphatidylcholine and 25% phosphatidylethanolamine and incubated them with recombinant wild-type SLP-65 protein or its N-terminal mutants, ΔN-SLP-65 and L18K-SLP-65.","type":"Results"},{"text":"Wild-type SLP-65 was concentrated in the SUV fractions and was almost absent in the soluble fractions. Conversely, none of the two signaling-incompetent SLP-65 mutants floated with the SUVs, but remained soluble (Fig. 1C). Hence, these data suggest that the N terminus of SLP-65 is capable of directly binding to general components of cellular membranes.","type":"Results"}],"curator_id":"vnugnes","released":"2023_12","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"25140054","version":4,"reference_html":"Macromolecular assembly of the adaptor SLP-65 at intracellular vesicles in resting B cells. <i> Engelke M, Pirkuliyeva S, Kühn J, Wong L, Boyken J, Herrmann N, Becker S, Griesinger C, Wienands J. </i> Sci Signal, 2014","date":"2023-12-05T15:11:46.049Z","term_id":"GO:0008289","ec_id":"ECO:0007089","region_id":"DP01544r002","ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"curator_orcid":"0000-0001-8399-7907","interaction_partner":[{"db":"ChEBI","id":"16038","operator":"and","partner_start":null,"partner_end":0},{"db":"ChEBI","id":"64482","operator":"or","partner_start":null,"partner_end":null}],"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Asn5Arg50del","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Constructs encoding chimeric proteins containing the OSBP1-PH domain (amino acid residues 87 to 189) and a SLP-65 variant lacking the 45 N-terminal amino acids were generated by overlap extension PCR."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:13:20.474Z"}},{"start":1,"end":330,"reference_id":"32051419","reference_source":"pmid","reference_html":"Tripartite phase separation of two signal effectors with vesicles priming B cell responsiveness. <i> Wong LE, Bhatt A, Erdmann PS, Hou Z, Maier J, Pirkuliyeva S, Engelke M, Becker S, Plitzko J, Wienands J, Griesinger C. </i> Nat Commun, 2020","date":"2023-12-05T15:18:43.348Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01544r003","statement":[{"text":"The sharp peaks observed in the 15N-HSQC (heteronuclear single quantum coherence) spectrum of SLP65 are typical for IDPs, implying fast reorientation motion of protein segments.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:13:16.400Z"}},{"start":1,"end":40,"reference_id":"32051419","reference_source":"pmid","reference_html":"Tripartite phase separation of two signal effectors with vesicles priming B cell responsiveness. <i> Wong LE, Bhatt A, Erdmann PS, Hou Z, Maier J, Pirkuliyeva S, Engelke M, Becker S, Plitzko J, Wienands J, Griesinger C. </i> Nat Commun, 2020","date":"2023-12-05T15:37:57.739Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1Lys40del","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"Authors named the construct SLP65 40–456 as SLP65ΔN."}]}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q96B97","operator":null,"partner_start":null,"partner_end":null},{"db":"ChEBI","id":"52360","operator":"and","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"74986","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01544r004","statement":[{"text":"Thus, phase separation of SLP65 and CIN85 occurs in vitro at protein concentrations found in vivo, but only in the presence of vesicles. This finding was confirmed further by the increased phase transition threshold of 10 µM for the N-terminal SLP65 deletion mutant, SLP65ΔN (Fig. 1f), which is unable to attach to vesicles13 and that does neither support granule formation nor BCR-activated Ca2+ mobilization when expressed in live B cells (see Fig. 1a and Supplementary Fig. 1). Importantly, no phase separation was observed when SLP65 was mixed with SUVs in the absence of CIN85Δ57 (Fig. 1g) demonstrating again the concerted action of all three components that is needed for droplet formation in vitro.","type":"Results"},{"text":"The vesicular attachment of SLP65 appears to provide a local seeding point that concentrates SLP65 to facilitate the recruitment of CIN85 and to initiate phase separation.","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:13:26.576Z"}},{"start":1,"end":40,"reference_id":"32051419","reference_source":"pmid","reference_html":"Tripartite phase separation of two signal effectors with vesicles priming B cell responsiveness. <i> Wong LE, Bhatt A, Erdmann PS, Hou Z, Maier J, Pirkuliyeva S, Engelke M, Becker S, Plitzko J, Wienands J, Griesinger C. </i> Nat Commun, 2020","date":"2023-12-05T15:44:25.990Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005580","ec_ontology":"ECO","ec_name":"flow cytometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1Lys40del","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"Authors named the construct SLP65 40–330 as SLP65ΔN."}]}],"ec_go":"IDA","interaction_partner":[{"db":"ChEBI","id":"52360","operator":null,"partner_start":null,"partner_end":null},{"db":"ChEBI","id":"74986","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01544r005","statement":[{"text":"Collectively, these data showed that the N-terminal lipid binding domain preferentially attaches at small vesicles with curved membranes and that this feature allows for tripartite phase separation at physiological concentrations, i.e. in vitro as well as in vivo.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:13:39.718Z"}}],"released":"2018_11","uniref100":"UniRef100_Q8WV28","date":"2018-07-26T14:57:46.000Z","acc":"Q8WV28","name":"B-cell linker protein","length":456,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI000007086E","genes":[{"name":{"value":"BLNK"},"synonyms":[{"value":"BASH"},{"value":"SLP65"}]}],"alphafold_very_low_content":0.3442982456140351,"disorder_content":0.7236842105263158,"disprot_consensus":{"full":[{"start":1,"end":330,"type":"D"}],"Structural state":[{"start":1,"end":330,"type":"D"}],"Molecular function":[{"start":1,"end":50,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00125","name":"Core histone H2A/H2B/H3/H4 domain","start":12,"end":88},{"id":"PF16211","name":"C-terminus of histone H2A","start":91,"end":124}],"gene3D":[{"start":2,"end":124,"id":"1.10.20.10","name":"Histone, subunit A"}]},"uniref50":"UniRef50_P84051","sequence":"MSGRGKGGKVKGKAKSRSNRAGLQFPVGRIHRLLRKGNYAERVGAGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLSGVTIAQGGVLPNIQAVLLPKKTEKKA","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_P84051","disprot_id":"DP01546","ncbi_taxon_id":7227,"regions_counter":8,"creator":"zskalman","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":11,"region_id":"DP01546r003","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Structure of the Drosophila nucleosome core particle highlights evolutionary constraints on the H2A-H2B histone dimer. <i> Clapier CR, Chakravarthy S, Petosa C, Fernández-Tornero C, Luger K, Müller CW. </i> Proteins, 2008","statement":[{"text":"Unstructured residues are indicated in lower case.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-29T16:04:35.222Z","reference_source":"pmid","term_name":"disorder","reference_id":"17957772","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"2PYO"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02283"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84040"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02299"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"DNA fragment derived from human α-satellite DNA with  sequence 5'-ATCAATATCCACCTGCAGATACTACCAAAAGTGTATTTGGAAACTGCTCCATCAAAAGGCATGTTCAGCTGGAATCCAGCTGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTGGTAGTATCTGCAGGTGGATATTGAT"}]}]},{"start":2,"end":25,"reference_id":"34837025","reference_source":"pmid","reference_html":"Mapping the electrostatic potential of the nucleosome acidic patch. <i> Zhang H, Eerland J, Horn V, Schellevis R, van Ingen H. </i> Sci Rep, 2021","date":"2024-11-20T08:53:13.055Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7PJ1"}],"region_id":"DP01546r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02283"}],"statement":[{"text":"Chemical shift indices obtained from the experimental Cα and Cβ chemical shifts confirm the presence of the histone fold core secondary structure elements with disordered tails for both histones, similar to the human dimer (Fig. 1a).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-03T19:21:07.752Z"}},{"start":98,"end":124,"reference_id":"34837025","reference_source":"pmid","reference_html":"Mapping the electrostatic potential of the nucleosome acidic patch. <i> Zhang H, Eerland J, Horn V, Schellevis R, van Ingen H. </i> Sci Rep, 2021","date":"2024-11-20T08:53:25.618Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7PJ1"}],"region_id":"DP01546r007","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02283"}],"statement":[{"text":"Chemical shift indices obtained from the experimental Cα and Cβ chemical shifts confirm the presence of the histone fold core secondary structure elements with disordered tails for both histones, similar to the human dimer (Fig. 1a).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-03T19:13:15.120Z"}},{"start":1,"end":11,"reference_id":"17957772","reference_source":"pmid","reference_html":"Structure of the Drosophila nucleosome core particle highlights evolutionary constraints on the H2A-H2B histone dimer. <i> Clapier CR, Chakravarthy S, Petosa C, Fernández-Tornero C, Luger K, Müller CW. </i> Proteins, 2008","date":"2025-02-03T19:22:50.556Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"2PYO"}],"region_id":"DP01546r008","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02283"}],"statement":[{"text":"Chemical shift indices obtained from the experimental Cα and Cβ chemical shifts confirm the presence of the histone fold core secondary structure elements with disordered tails for both histones, similar to the human dimer (Fig. 1a).","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_P84051","date":"2018-07-26T17:23:22.000Z","acc":"P84051","name":"Histone H2A","length":124,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI000011F9C4","genes":[{"name":{"value":"His2A"},"synonyms":[{"value":"H2a"}]},{"name":{"value":"His2A:CG31618"},"orfNames":[{"value":"CG31618"}]},{"name":{"value":"His2A:CG33808"},"orfNames":[{"value":"CG33808"}]},{"name":{"value":"His2A:CG33814"},"orfNames":[{"value":"CG33814"}]},{"name":{"value":"His2A:CG33817"},"orfNames":[{"value":"CG33817"}]},{"name":{"value":"His2A:CG33820"},"orfNames":[{"value":"CG33820"}]},{"name":{"value":"His2A:CG33823"},"orfNames":[{"value":"CG33823"}]},{"name":{"value":"His2A:CG33826"},"orfNames":[{"value":"CG33826"}]},{"name":{"value":"His2A:CG33829"},"orfNames":[{"value":"CG33829"}]},{"name":{"value":"His2A:CG33832"},"orfNames":[{"value":"CG33832"}]},{"name":{"value":"His2A:CG33835"},"orfNames":[{"value":"CG33835"}]},{"name":{"value":"His2A:CG33838"},"orfNames":[{"value":"CG33838"}]},{"name":{"value":"His2A:CG33841"},"orfNames":[{"value":"CG33841"}]},{"name":{"value":"His2A:CG33844"},"orfNames":[{"value":"CG33844"}]},{"name":{"value":"His2A:CG33847"},"orfNames":[{"value":"CG33847"}]},{"name":{"value":"His2A:CG33850"},"orfNames":[{"value":"CG33850"}]},{"name":{"value":"His2A:CG33862"},"orfNames":[{"value":"CG33862"}]},{"name":{"value":"His2A:CG33865"},"orfNames":[{"value":"CG33865"}]}],"alphafold_very_low_content":0,"disorder_content":0.41935483870967744,"disprot_consensus":{"full":[{"start":1,"end":25,"type":"D"},{"start":98,"end":124,"type":"D"}],"Structural state":[{"start":1,"end":25,"type":"D"},{"start":98,"end":124,"type":"D"}],"Disorder function":[{"start":1,"end":11,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00001","name":"7 transmembrane receptor (rhodopsin family)","start":23,"end":288}],"gene3D":[{"start":1,"end":307,"id":"1.20.1070.10","name":"Rhodopsin 7-helix transmembrane proteins"}]},"uniref50":"UniRef50_P29274","sequence":"MPIMGSSVYITVELAIAVLAILGNVLVCWAVWLNSNLQNVTNYFVVSLAAADIAVGVLAIPFAITISTGFCAACHGCLFIACFVLVLTQSSIFSLLAIAIDRYIAIRIPLRYNGLVTGTRAKGIIAICWVLSFAIGLTPMLGWNNCGQPKEGKNHSQGCGEGQVACLFEDVVPMNYMVYFNFFACVLVPLLLMLGVYLRIFLAARRQLKQMESQPLPGERARSTLQKEVHAAKSLAIIVGLFALCWLPLHIINCFTFFCPDCSHAPLWLMYLAIVLSHTNSVVNPFIYAYRIREFRQTFRKIIRSHVLRQQEPFKAAGTSARVLAAHGSDGEQVSLRLNGHPPGVWANGSAPHPERRPNGYALGLVSGGSAQESQGNTGLPDVELLSHELKGVCPEPPGLDDPLAQDGAGVS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P29274","disprot_id":"DP01547","ncbi_taxon_id":9606,"regions_counter":16,"creator":"jglavina","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":412,"region_id":"DP01547r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Human adenosine A2A receptor binds calmodulin with high affinity in a calcium-dependent manner. <i> Piirainen H, Hellman M, Tossavainen H, Permi P, Kursula P, Jaakola VP. </i> Biophys J, 2015","statement":[{"text":"The far-UV CD spectrum of A2A-ctL (residues 293-412) is typical for a protein without a globular conformation or secondary structure. It has a small negative shoulder around 222 nm, a strong negative minimum around 200 nm, and no positive signals in the far-UV range.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":293,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"25692595","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-25T10:17:30.087Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":412,"region_id":"DP01547r003","released":"2022_03","ec_id":"ECO:0001249","reference_html":"Human adenosine A2A receptor binds calmodulin with high affinity in a calcium-dependent manner. <i> Piirainen H, Hellman M, Tossavainen H, Permi P, Kursula P, Jaakola VP. </i> Biophys J, 2015","statement":[{"text":"A2A-ct has a single tryptophan residue at position 346. According to fluorescence measurements, Trp-346 is exposed to an aqueous environment.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":293,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"25692595","version":2,"ec_name":"fluorescence evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-25T10:17:41.752Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":412,"region_id":"DP01547r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Human adenosine A2A receptor binds calmodulin with high affinity in a calcium-dependent manner. <i> Piirainen H, Hellman M, Tossavainen H, Permi P, Kursula P, Jaakola VP. </i> Biophys J, 2015","statement":[{"text":"The two-dimensional 1H, 15N-HSQC spectrum of A2A-ctL shows poorly dispersed crosspeaks, with the proton chemical shifts ranging from 7.5 to 8.5 1H ppm, indicating that A2A-ct undergoes fast conformational dynamics in solution, which is typical for disordered proteins. According to chemical shifts, the A2A-ctL N-terminal transiently populates β-structures, whereas the remainder is partially α-helical.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":293,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"25692595","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-25T10:17:42.760Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":412,"region_id":"DP01547r005","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Human adenosine A2A receptor binds calmodulin with high affinity in a calcium-dependent manner. <i> Piirainen H, Hellman M, Tossavainen H, Permi P, Kursula P, Jaakola VP. </i> Biophys J, 2015","statement":[{"text":"A2A-ctL alone was highly elongated. For a fully random polymer chain, the Rg and Dmax values can be estimated from amino acid chain length; for A2A-ctL (134 residues), these values would be 3.78 nm and 10.5 nm, respectively. These results suggest A2A-ctL behaves more or less like a random chain in solution, and is even slightly more elongated than expected for a random polymer, suggesting intramolecular repulsion.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":293,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"25692595","version":2,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-25T10:17:51.492Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":412,"region_id":"DP01547r006","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Human adenosine A2A receptor binds calmodulin with high affinity in a calcium-dependent manner. <i> Piirainen H, Hellman M, Tossavainen H, Permi P, Kursula P, Jaakola VP. </i> Biophys J, 2015","statement":[{"text":"We determined Stokes radii for the peaks corresponding to A2A-ctL, CaM, and A2A-ctL-CaM samples by gel filtration, using proteins with known Stokes radii as standards. In the presence of calcium, the calculated Stokes radii for A2A-ctL, CaM, and the A2A-ctL-CaM complex were 2.74, 2.49, and 3.48 nm, respectively. The relatively high Stokes radii values were understandable because of the disordered nature of A2A-ct.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":293,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"25692595","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-25T10:17:54.463Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":293,"end":412,"reference_id":"25952762","reference_source":"pmid","reference_html":"H(N), N, C(α), C(β) and C' assignments of the intrinsically disordered C-terminus of human adenosine A2A receptor. <i> Tossavainen H, Hellman M, Piirainen H, Jaakola VP, Permi P. </i> Biomol NMR Assign, 2015","date":"2023-01-09T14:51:25.795Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2023_06","version":3,"region_id":"DP01547r007","statement":[{"text":"H(N), N, C(α), C(β) and C' assignments of the intrinsically disordered C-terminus of human adenosine A2A receptor","type":"Title"},{"text":"We have previously structurally characterized this C-terminal domain and its interaction with calmodulin. It was shown to be structurally disordered and flexible, and to bind calmodulin with high affinity in a calcium-dependent manner. Interaction with calmodulin takes place at the N-terminal end of the A2A C-terminal domain without major conformational changes in the latter. NMR was one of the biophysical methods used in the study. Here we present the H(N), N, C(α), C(β) and C' chemical shift assignments of the free form of the C-terminus residues 293-412, used in the NMR spectroscopic characterization of the domain.","type":"Abstract"},{"text":"For the assignment we employed a combination of common 3D HN-detected assignment spectra and 3D HN-detected experiments specially tailored for intrinsically disordered proteins (Mäntylahti et al. 2009; Hellman et al. 2014). Fast conformational averaging and chemical exchange and absence of structure-induced secondary chemical shifts result in a narrow HN chemical shift range as well as overlap of Cα and Cβ shifts, both commonly observed for IDPs.","type":"Article"}],"ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"BMRB","id":"25445"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-09T14:51:57.319Z"}},{"start":291,"end":311,"reference_id":"25692595","reference_source":"pmid","reference_html":"Human adenosine A2A receptor binds calmodulin with high affinity in a calcium-dependent manner. <i> Piirainen H, Hellman M, Tossavainen H, Permi P, Kursula P, Jaakola VP. </i> Biophys J, 2015","date":"2023-01-13T09:57:15.351Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005516","term_name":"calmodulin binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","released":"2023_06","version":4,"region_id":"DP01547r008","statement":[{"text":"To confirm the CaM-binding site on A2A-ctL and the importance of arginine residues for binding, we carried out binding competition experiments using a peptide corresponding to WT A2AR amino acids 291–311 and a peptide corresponding to A2AR amino acids 288–311, with six arginine to alanine mutations (Fig. 4, B and C, respectively). The WT peptide bound calmodulin as expected, because an extra protein band appeared on a native gel. This band was missing from the mutated peptide-CaM sample, demonstrating the importance of the mutated arginine residues for the interaction. When the amount of WT A2A peptide was increased from 3.7 pmol to 24.3 nmol, the peptide clearly displaced A2A-ctL from CaM. On the other hand, the mutated A2A peptide did not affect A2A-ctL-CaM binding, although some unbound CaM was present in samples containing the highest amount of the mutated peptide.","type":"Results"}],"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","disprot_namespace":"Disorder function","term_is_binding":true,"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg291Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg293Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg296Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg300Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg304Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg309Ala","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-13T13:24:15.695Z"}},{"start":293,"end":320,"reference_id":"25692595","reference_source":"pmid","reference_html":"Human adenosine A2A receptor binds calmodulin with high affinity in a calcium-dependent manner. <i> Piirainen H, Hellman M, Tossavainen H, Permi P, Kursula P, Jaakola VP. </i> Biophys J, 2015","date":"2023-01-13T09:54:22.744Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005516","term_name":"calmodulin binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","released":"2023_06","version":4,"region_id":"DP01547r009","statement":[{"text":"As previous studies have not provided information about stoichiometry and affinity of the A2AR-calmodulin interaction, we performed ITC experiments for CaM binding to A2A-ctL in the presence of calcium and EDTA (Fig. 5, A and B). The A2A-ctL-CaM interaction is a calcium-dependent exothermic binding reaction with a favorable enthalpy (−12.93 ± 0.13 kcal mol−1), but an unfavorable entropy (3.4 kcal mol−1). The dissociation constant (Kd) for the complex is 97.9 ± 9.3 nM and the stoichiometry 0.92 ± 0.04, indicating 1:1 complex formation (Table 1). In the presence of EDTA, no binding was observed. To confirm the CaM-binding site on A2A-ctL, we also titrated A2A-ctS with CaM in the presence of calcium (Fig. 5 C). In this case, much smaller exothermic peaks were observed. Consequently, the removal of amino acids 293–320 from A2A-ct clearly abolished high-affinity binding to CaM.","type":"Results"},{"text":"The C-terminal construct of the A2AR—the full-length domain (A2A-ctL) corresponds to region 293–412, while the null-binding domain (A2A-ctS) corresponds to region 321-412.","type":"Curator statement"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","disprot_namespace":"Disorder function","term_is_binding":true,"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-13T13:24:17.311Z"}},{"start":293,"end":320,"reference_id":"25692595","reference_source":"pmid","reference_html":"Human adenosine A2A receptor binds calmodulin with high affinity in a calcium-dependent manner. <i> Piirainen H, Hellman M, Tossavainen H, Permi P, Kursula P, Jaakola VP. </i> Biophys J, 2015","date":"2023-01-13T09:54:53.457Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005516","term_name":"calmodulin binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2023_06","version":4,"region_id":"DP01547r010","statement":[{"text":"Most significant chemical shift perturbations, in terms of disappearance of crosspeaks of the free A2A-ctL form upon addition of CaM, were observed in the proposed CaM binding region in the very N-terminal part of A2A-ctL (Fig. 3 B). This suggests that the CaM binding epitope of A2A-ctL comprises residues 293–321","type":"Results"},{"text":"The C-terminal construct of the A2AR—the full-length domain (A2A-ctL) corresponds to region 293–412, while the null-binding domain (A2A-ctS) corresponds to region 321-412.","type":"Curator statement"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","disprot_namespace":"Disorder function","term_is_binding":true,"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-13T13:24:19.027Z"}},{"start":293,"end":412,"reference_id":"25692595","reference_source":"pmid","reference_html":"Human adenosine A2A receptor binds calmodulin with high affinity in a calcium-dependent manner. <i> Piirainen H, Hellman M, Tossavainen H, Permi P, Kursula P, Jaakola VP. </i> Biophys J, 2015","date":"2023-01-13T09:59:34.518Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","released":"2023_06","version":6,"region_id":"DP01547r011","statement":[{"text":"Because A2A-ctL seemed to interact with negatively charged lipids, we studied the effect of CaM on the ability of A2A-ctL to bind lipid membranes. For this purpose, we immobilized a mixture of DMPC/DMPG on an L1 SPR sensor chip, and injected A2A-ctL over the lipid surface. A2A-ctL bound immediately to the lipids in a concentration-dependent manner, and no dissociation was observed (Fig. 6).","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"ChEBI","id":"45240","operator":"and","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"60723","operator":"and","partner_start":null,"partner_end":null}],"sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"60723","entry_name":"ditetradecanoyl phosphatidylglycerol"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-13T13:24:20.178Z"}},{"start":293,"end":320,"reference_id":"25692595","reference_source":"pmid","reference_html":"Human adenosine A2A receptor binds calmodulin with high affinity in a calcium-dependent manner. <i> Piirainen H, Hellman M, Tossavainen H, Permi P, Kursula P, Jaakola VP. </i> Biophys J, 2015","date":"2023-01-13T09:55:26.448Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005516","term_name":"calmodulin binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006305","ec_ontology":"ECO","ec_name":"native protein gel electrophoresis evidence used in manual assertion","released":"2023_06","version":4,"region_id":"DP01547r013","statement":[{"text":"Although A2A-ctL bound to CaM, no extra bands were detected in either of the samples containing A2A-ctS and CaM. This suggests that the CaM-binding site on A2A-ct locates between amino acids 293 and 320. This region on A2A-ct contains many positively charged arginine residues that are thought to be involved in CaM binding (19). The observed calcium dependence of the binding was surprising, because in previous studies, calcium was not thought to be involved in the interaction (42).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","disprot_namespace":"Disorder function","term_is_binding":true,"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-13T13:24:22.341Z"}},{"start":317,"end":412,"reference_id":"34269678","reference_source":"pmid","reference_html":"Homo-oligomerization of the human adenosine A<sub>2A</sub> receptor is driven by the intrinsically disordered C-terminus. <i> Nguyen KDQ, Vigers M, Sefah E, Seppälä S, Hoover JP, Schonenbach NS, Mertz B, O'Malley MA, Han S. </i> Elife, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jglavina","curator_name":"Juliana Glavina","curator_orcid":"0000-0001-6336-1290","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01547r014","statement":[{"text":"Homo-oligomerization of the human adenosine A 2A receptor is driven by the intrinsically disordered C-terminus","type":"Title"},{"text":"Herein, we focus on the human adenosine A 2A receptor (A 2A R), a model GPCR that forms oligomers both in vitro and in vivo. Combining experimental and computational approaches, we discover that the intrinsically disordered C-terminus of A 2A R drives receptor homo-oligomerization. The formation of A 2A R oligomers declines progressively with the shortening of the C-terminus. Multiple interaction types are responsible for A 2A R oligomerization, including disulfide linkages, hydrogen bonds, electrostatic interactions, and hydrophobic interactions. These interactions are enhanced by depletion interactions, giving rise to a tunable network of bonds that allow A 2A R oligomers to adopt multiple interfaces. This study uncovers the disordered C-terminus as a prominent driving factor for the oligomerization of a GPCR, offering important insight into the effect of C-terminus modification on receptor oligomerization of A 2A R and other GPCRs reconstituted in vitro for biophysical studies.","type":"Abstract"},{"text":"Using the SEC analysis described earlier (Figure 1), we evaluated the HMW oligomer and dimer levels of the A 2A R-DC variants relative to that of the A 2A R full-length-wild-type (FL-WT) control. Both the dimer and the total oligomer levels of A 2A R decreased progressively with the shortening of the C-terminus, with almost no oligomerization detected upon complete truncation of the C-terminus at site A316 (Figure 3B). This result shows that the C-terminus drives A 2A R oligomerization, with multiple potential interaction sites positioned along much of its length.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-21T07:30:58.908Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":354,"end":359,"reference_id":"34269678","reference_source":"pmid","reference_html":"Homo-oligomerization of the human adenosine A<sub>2A</sub> receptor is driven by the intrinsically disordered C-terminus. <i> Nguyen KDQ, Vigers M, Sefah E, Seppälä S, Hoover JP, Schonenbach NS, Mertz B, O'Malley MA, Han S. </i> Elife, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jglavina","curator_name":"Juliana Glavina","curator_orcid":"0000-0001-6336-1290","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01547r015","statement":[{"text":"Since segment 354–359 contains three consecutive charged residues ( 355 ERR 357 ; Figure 3A), which could be involved in electrostatic interactions, we hypothesized that this 355 ERR 357 cluster could strengthen inter-protomer A 2A R-A 2A R association. To test this hypothesis, residues 355 ERR 357 were substituted by 355 AAA 357 on A 2A R-FL-WT and A 2A R-N359DC to generate A 2A R-ERR:AAA variants (Figure 3C). We then compared the HMW oligomer and dimer levels of the resulting variants with controls (same A 2A R variants but without the ERR:AAA mutations). We found that the ERR:AAA mutations had varied effects on the dimer level: decreasing for A 2A R-FL-WT (ctrl: 0.49; ERR:AAA:0.29) but increasing for A 2A R-N359DC (ctrl: 0.33; ERR:AAA: 0.48) (Figure 3C). In contrast, the ERR:AAA mutations reduced the HMW oligomer level of both A 2A R-FL-WT (ctrl: 0.88; ERR:AAA: 0.66) and A 2A R-N359DC (ctrl: 0.68; ERR:AAA: 0.38) (Figure 3C). Consistently, the ERR:AAA mutation lowered the total oligomer level of both A 2A R-FL-WT (ctrl: 1.37; ERR:AAA: 0.94) and A 2A R-N359DC (ctrl:1.01; ERR:AAA: 0.85) (Figure 3C). These results suggest that the charged residues 355 ERR 357 participate in A 2A R oligomerization, with a greater effect in the context of a longer C-terminus and for forming higher-order oligomers. The question then arises as to what types of interactions are formed along the C-terminus that help stabilize A 2A R oligomerization.","type":"Results"},{"text":"Upon closer examination, we recognize that at the very high ionic strength of 0.95 M the increase in the dimer and total oligomer levels was robust for A 2A R-FL-WT, but less pronounced for A 2A R-FL-ERR:AAA (Figure 5). Furthermore, this high ionic strength even had an opposite effect on A 2A R-N359DC, with both its dimer and total oligomer levels abolished (Figure 5). These results indicate that the charged cluster 355 ERR 357 and the C-terminal segment after residue N359 promote the depletion interactions to drive A 2A R oligomerization. Taken together, we can conclude that A 2A R oligomerization is more robust when the C-terminus is fully present and the ionic strength higher, suggesting that depletion interactions via the C-terminus are strong driving factors of A 2A R oligomerization.","type":"Results"},{"text":"In particular, the 355 ERR 357 cluster of charged residues lies distal from the dimeric interface but still forms several salt bridges (Figure 7A, inset). This observation is supported by our experimental results showing that substituting this charged cluster with alanines reduces the total A 2A R oligomer levels (Figure 3C).","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-21T07:30:51.793Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":293,"end":412,"reference_id":"25692595","reference_source":"pmid","reference_html":"Human adenosine A2A receptor binds calmodulin with high affinity in a calcium-dependent manner. <i> Piirainen H, Hellman M, Tossavainen H, Permi P, Kursula P, Jaakola VP. </i> Biophys J, 2015","date":"2023-01-10T15:58:37.940Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005516","term_name":"calmodulin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P0DP23","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01547r016","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"Both A2A-ctL and CaM were monomeric in solution (Fig. S4), and the molecular mass calculated for their mixture indicated quantitative complex formation with 1:1 stoichiometry, which is in line with the affinity and stability of the complex described previously.","type":"Results"}],"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_P29274","date":"2018-07-26T17:57:37.000Z","acc":"P29274","name":"Adenosine receptor A2a","length":412,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI000016A417","genes":[{"name":{"value":"ADORA2A"},"synonyms":[{"value":"ADORA2"}]}],"alphafold_very_low_content":0.23300970873786409,"disorder_content":0.2912621359223301,"disprot_consensus":{"full":[{"start":291,"end":292,"type":"F"},{"start":293,"end":412,"type":"D"}],"Structural state":[{"start":293,"end":412,"type":"D"}],"Molecular function":[{"start":291,"end":412,"type":"F"}],"Disorder function":[{"start":317,"end":412,"type":"F"}]}},{"features":{"pfam":[{"id":"PF13934","name":"Nuclear pore complex assembly","start":722,"end":944},{"id":"PF16687","name":"beta-propeller of ELYS nucleoporin","start":1,"end":489}]},"uniref50":"UniRef50_Q8CJF7","sequence":"MQDLTAQVTSDLLHFPEVTIEALGEDEITLESVLRGKFAAGKNGLACLACGPQLEVVNSLTGERLSAYRFSGVNEQPPVVLAVKEFSWHKRTGLLIGLEEADGSVLCLYDLGISRVVKAVVLPGRVTAIEPIINHGGASASTQHLHPSLRWLFGVAAVVTDVGQILLIDLCLDDLSCSQNEVEASDLEVITGIPAEVPHIRERVMREGRHLCFQLVSPLGVAISTLSYINRTNQLAVGFSDGYLALWNMKSMKREYYTQLEGGRVPVHAVAFQEPENDPRNCCYLWAVQSTQDSEGDVLSLHLLQLAFGDRKCLASGQILYEGLEYCEERYTLDLAGGTFPLRGQTSNTKLLGCQSIERFPSHGDREESMREALSPDTSVSVFTWQVNIYGQGKPSVYLGLFDINRWYHAQMPDSLRSGESLHNCSYFALWSLDSVVSRTSPHHILDILVHERSLNRGVPPSYPPPEQFFNPSTFNFDATCLLDSGVIHVTCAGFQKETLTFLKKSGPTLNEVIPDSYNRCLVAGLLSPRLIDIQPSSLSQEEQLEAILSAAIQTSSLGLLTGYIRTWIIEEQPNSAANLRFVLEWTWNKVVLTKEEFDRLCVPLFDGSCRFIDPQTIQSIQQCHLLLSNLSTVLSCFAMEAQGITERGLVDLSNKHMVTQLLCQYAHMVLWFCHSGLLPEGLDDALQLSRLRYNYPVIQNYYTSRRQKSERSPRGKWNHDCLMIDGLVSQLGDEVEKLWKRDEGGTGRYPPASIHALLDIYLLDNITEASKHAITIYLLLDIMYSFPNKTDTPIESFPTAFAISWGQVKLVQGFWLLDHNDYENGLDLLFHPVTAKPASWQHSKIIEAFMSQGEHKQALRYLQTMKPTVSSSNEVILHLTVLLFNRCMVEAWNLLRQNSNRVNIEELLKHAYEVCQEMGLMEDLLKLPFTNTEQECLVKFLQSSTSVENHEFLLVHHLQRANYISALKLNQILKNNLMSDRDPRLRERSVTRNSILDQYGKILPRVQRKLAVERAKPYHLSTSSVFHEVSRPKPLSAFPKKAITGTVLTRSTFISNVLSKIGEVWASHEPRNGVSLFNSPKTEQPSPVVHSFPHPELPEAFVGTPISNTSQRISRLLDLVVHPVPQPSQCLEFIQQSPTRSPLCLLSSSLPLSSQFKRPHQNTSRPSELLLLETPLIVKKAKSLALSATSSGFAEFTPPSILRSGFRTTPLASPSLSPGRSLTPPFRVKETRISFMEEGMNTHWTDRATDDRNTKAFVSTSFHKCGLPAETEWMKTSDKNTYFPLDVPAKGPQKVVAESLATHSGRLEKLDVSKEDSTASTRSDQTSLEYHDAPSPEDLEGAVFVSPKPASSSTELTTNSTLQTERDNDKDAFKSEGAPSPVKKQIGTGDAAVEAFSELSRLDPVERAEASFAVSSVCEGETSTSNSKTSVLDGIVPIESRTSILTADHKESVANTVADVESSGSTSSKCPVTSERSLGQKLTLNLKEDEIEAHVPKENVGLPEESPRISAAPSDTHEIHLIGCENLEVQNSEEEAKNLSFDELYPLGAEKLEYNLSTIEQQFCDLPDDKDSAECDAAEVDGELFVAQSNFTLILEGEEGEAEASDSAAPNMLPKATKEKPVCHREPHNQERVTDLPSAVTADQESHKVETLPYVPEPVKVAIAENLLDVIKDTRSKEATPVAAGEAGDEDGAVIVSKAAHSSRLTNSTPKTVKEPHAETVNTSQNDDMVSSRTLTRRQHALSLNVTSEQEPSAVATPKKRTRKIKETPESSERTCSDLKVAPENQLTAQSPPAPRRGKKKDVSQGTLPSSGAVEPEPEPQGTPGRLRLRTQPPEPAAEETPSRTKVRLSSVRKGTPRRLKKSVENGQSTEILDDLKGSEAASHDGTVTELRNANLEDTQNMEYKQDEHSDQQLPLKRKRVREREVSVSSVTEEPKLDSSQLPLQTGLDVPATPRKRGRPRKVVPLEADGGTTGKEQTSPQKKDVPVVRRSTRNTPARNVSTLEKSVLVPNKEAALVVTSKRRPTKKSAEESSKDPSAAVSDLAGGAAHTESADRRDGLLAAAALTPSAQGTRTRSRRTMLLTDISEPKTEPLFPPPSVKVPKKKSKAENMEAAAQLKELVSDLSSQFVVSPPALRTRQKSISNTSKLLGELESDPKPLEIIEQKPKRSRTVKTRASRNTGKGSSWSPPPVEIKLVSPLASPVDEIKTGKPRKTAEIAGKTLGRGRKKPSSFPKQILRRKML","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q8CJF7","disprot_id":"DP01548","ncbi_taxon_id":10090,"regions_counter":1,"creator":"jlamb","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":2243,"region_id":"DP01548r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural and functional studies of the 252 kDa nucleoporin ELYS reveal distinct roles for its three tethered domains. <i> Bilokapic S, Schwartz TU. </i> Structure, 2013","statement":[{"text":"Figure 2\nIn vivo localization of metazoan ELYS domains","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jlamb","start":1018,"term_ontology":"IDPO","curator_name":"John Lamb","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0568-8281","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23499022","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q8CJF7","date":"2018-07-26T18:13:59.000Z","acc":"Q8CJF7","name":"Protein ELYS","length":2243,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000E8B59","genes":[{"name":{"value":"Ahctf1"},"synonyms":[{"value":"Elys"}]}],"alphafold_very_low_content":0.5372269282211324,"disorder_content":0.5465893892108783,"disprot_consensus":{"full":[{"start":1018,"end":2243,"type":"D"}],"Structural state":[{"start":1018,"end":2243,"type":"D"}]}},{"features":{"pfam":[{"id":"PF13934","name":"Nuclear pore complex assembly","start":722,"end":944},{"id":"PF16687","name":"beta-propeller of ELYS nucleoporin","start":1,"end":489}]},"uniref50":"UniRef50_Q8WYP5","sequence":"MRDLRAQVTSGLLPFPEVTLQALGEDEITLESVLRGKFAAGKNGLACLACGPQLEVVNSITGERLSAYRFSGVNEQPPVVLAVKEFSWQKRTGLLIGLEETEGSVLCLYDLGISKVVKAVVLPGRVTAIEPIINHGGASASTQHLHPSLRWLFGVAAVVTDVGQILLVDLCLDDLSCNQNEVEASDLEVLTGIPAEVPHIRESVMRQGRHLCFQLVSPTGTAVSTLSYISRTNQLAVGFSDGYLALWNMKSMKREYYIQLESGQVPVYAVTFQEPENDPRNCCYLWAVQSTQDSEGDVLSLHLLQLAFGNRKCLASGQILYEGLEYCEERYTLDLTGGMFPLRGQTSNTKLLGCQSIEKFRSHGDREEGVNEALSPDTSVSVFTWQVNIYGQGKPSVYLGLFDINRWYHAQMPDSLRSGEYLHNCSYFALWSLESVVSRTSPHGILDILVHERSLNRGVPPSYPPPEQFFNPSTYNFDATCLLNSGVVHLTCTGFQKETLTFLKKSGPSLNELIPDGYNRCLVAGLLSPRFVDVQPSSLSQEEQLEAILSAAIQTSSLGLLTGYIRRWITEEQPNSATNLRFVLEWTWNKVVLTKEEFDRLCVPLFDGSCHFMDPQTIQSIQQCYLLLSNLNIVLSCFASEAREITERGLIDLSNKFVVSHLICQYAQVVLWFSHSGLLPEGIDDSVQLSRLCYNYPVIQNYYTSRRQKFERLSRGKWNPDCLMIDGLVSQLGERIEKLWKRDEGGTGKYPPASLHAVLDMYLLDGVTEAAKHSITIYLLLDIMYSFPNKTDTPIESFPTVFAISWGQVKLIQGFWLIDHNDYESGLDLLFHPATAKPLSWQHSKIIQAFMSQGEHRQALRYIQTMKPTVSSGNDVILHLTVLLFNRCMVEAWNFLRQHCNRLNIEELLKHMYEVCQEMGLMEDLLKLPFTDTEQECLVKFLQSSASVQNHEFLLVHHLQRANYVPALKLNQTLKINVMNDRDPRLRERSLARNSILDQYGKILPRVHRKLAIERAKPYHLSTSSVFRLVSRPKPLSAVPKQVVTGTVLTRSVFINNVLSKIGEVWASKEPINSTTPFNSSKIEEPSPIVYSLPAPELPEAFFGTPISKASQKISRLLDLVVQPVPRPSQCSEFIQQSSMKSPLYLVSRSLPSSSQLKGSPQAISRASELHLLETPLVVKKAKSLAMSVTTSGFSEFTPQSILRSTLRSTPLASPSPSPGRSPQRLKETRISFVEEDVHPKWIPGAADDSKLEVFTTPKKCAVPVETEWLKSKDRTTSFFLNSPEKEHQEMDEGSQSLEKLDVSKGNSSVSITSDETTLEYQDAPSPEDLEETVFTASKPKSSSTALTTNVTEQTEKDGDKDVFASEVTPSDLQKQMGNLEDAETKDLLVAAEAFSELNHLSPVQGTEASLCAPSVYEGKIFTQKSKVPVLDEGLTSVETYTPAIRANDNKSMADVLGDGGNSSLTISEGPIVSERRLNQEVALNLKEDHEVEVGVLKESVDLPEEKLPISDSPPDTQEIHVIEQEKLEAQDSGEEARNLSFNELYPSGTLKLQYNFDTIDQQFCDLADNKDTAECDIAEVDGELFVAQSNFTLILEGEEGEVEPGDFASSDVLPKAANTATEEKLVCSGENDNHGQIANLPSAVTSDQKSQKVDTLPYVPEPIKVAIAENLLDVIKDTRSKEITSDTMEQSIHETIPLVSQNIMCPTKLVKSAFKTAQETSTMTMNVSQVDDVVSSKTRTRGQRIQNVNVKSAQQEASADVATPKMPGQSVRKKTRKAKEISEASENIYSDVRGLSQNQQIPQNSVTPRRGRRKKEVNQDILENTSSVEQELQITTGRESKRLKSSQLLEPAVEETTKKEVKVSSVTKRTPRRIKRSVENQESVEIINDLKVSTVTSPSRMIRKLRSTNLDASENTGNKQDDKSSDKQLRIKHVRRVRGREVSPSDVREDSNLESSQLTVQAEFDMSAIPRKRGRPRKINPSEDVGSKAVKEERSPKKKEAPSIRRRSTRNTPAKSENVDVGKPALGKSILVPNEELSMVMSSKKKLTKKTESQSQKRSLHSVSEERTDEMTHKETNEQEERLLATASFTKSSRSSRTRSSKAILLPDLSEPNNEPLFSPASEVPRKAKAKKIEVPAQLKELVSDLSSQFVISPPALRSRQKNTSNKNKLEDELKDDAQSVETLGKPKAKRIRTSKTKQASKNTEKESAWSPPPIEIRLISPLASPADGVKSKPRKTTEVTGTGLGRNRKKLSSYPKQILRRKML","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q8WYP5","disprot_id":"DP01549","ncbi_taxon_id":9606,"regions_counter":1,"creator":"jlamb","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":2266,"region_id":"DP01549r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural and functional studies of the 252 kDa nucleoporin ELYS reveal distinct roles for its three tethered domains. <i> Bilokapic S, Schwartz TU. </i> Structure, 2013","statement":[{"text":"Figure 2 In vivo localization of metazoan ELYS domains","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jlamb","start":1018,"term_ontology":"IDPO","curator_name":"John Lamb","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0568-8281","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23499022","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q8WYP5","date":"2018-07-26T18:16:36.000Z","acc":"Q8WYP5","name":"Protein ELYS","length":2266,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000006DA20","genes":[{"name":{"value":"AHCTF1"},"synonyms":[{"value":"ELYS"},{"value":"TMBS62"}],"orfNames":[{"value":"MSTP108"}]}],"alphafold_very_low_content":0.5441306266548985,"disorder_content":0.5511915269196822,"disprot_consensus":{"full":[{"start":1018,"end":2266,"type":"D"}],"Structural state":[{"start":1018,"end":2266,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":12,"end":80}],"gene3D":[{"start":1,"end":105,"id":"3.30.70.330","name":"3.30.70.330"}]},"uniref50":"UniRef50_A0A5D2WPG3","sequence":"MAESDGAEYRCFVGSLSWNTDDRGLEAAFSSFGEILDAKIINDRETGRSRGFGFVSFSNEQAMQDAIEGMNGKELDGRSIVVNEAQSRGYGGGGGGRYGGGGGGGGGRYGGGGAYGQRRDDGYGDDGYGGGRGYGGGRYGGGRGYGGRRDGGYGRGGNSDGY","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","BOP clade","Pooideae","Triticodae","Triticeae","Hordeinae","Hordeum"],"uniref90":"UniRef90_A0A287U8L9","disprot_id":"DP01550","ncbi_taxon_id":4513,"regions_counter":3,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":162,"region_id":"DP01550r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural and biochemical analysis of the Hordeum vulgare L. HvGR-RBP1 protein, a glycine-rich RNA-binding protein involved in the regulation of barley plant development and stress response. <i> Tripet BP, Mason KE, Eilers BJ, Burns J, Powell P, Fischer AM, Copié V. </i> Biochemistry, 2014","statement":[{"text":"A 2D 1H–15N HSQC spectrum recorded at a pH of 6.8 and temperature of 298 K of an 15N-labeled glycine-rich (HvGR) protein sample reveals that the glycine-rich domain of HvGR-RBP1 is unstructured in solution, displaying only broad resonances in the central “random coil” region of the spectrum.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":93,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"25495582","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":162,"term_name":"protein binding","start":93,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Spectral changes taking place upon addition of unlabeled N-HvGR-RBP1 to 15N-HvGR suggest that the two protein domains can interact in vitro in trans, although the biological significance of these interactions is unclear.","type":"Results"}],"curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"25495582","version":3,"reference_html":"Structural and biochemical analysis of the Hordeum vulgare L. HvGR-RBP1 protein, a glycine-rich RNA-binding protein involved in the regulation of barley plant development and stress response. <i> Tripet BP, Mason KE, Eilers BJ, Burns J, Powell P, Fischer AM, Copié V. </i> Biochemistry, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP01550r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":162,"term_name":"DNA binding","start":93,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Nucleic acid interaction assays indicated that the GR domain of HvGR-RBP1 can bind to single-stranded RNA (ssRNA) in the absence of the RRM domain.","type":"Results"}],"curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"25495582","version":3,"reference_html":"Structural and biochemical analysis of the Hordeum vulgare L. HvGR-RBP1 protein, a glycine-rich RNA-binding protein involved in the regulation of barley plant development and stress response. <i> Tripet BP, Mason KE, Eilers BJ, Burns J, Powell P, Fischer AM, Copié V. </i> Biochemistry, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003677","ec_id":"ECO:0006165","region_id":"DP01550r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_A0A287U8L9","date":"2018-07-26T18:41:49.000Z","acc":"J7FTI7","name":"RBP1","length":162,"organism":"Hordeum vulgare","dataset":[],"UniParc":"UPI000277AD54","genes":[{"name":{"value":"rbp1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AFP52931.1","url":"https://www.ebi.ac.uk/ena/browser/view/AFP52931.1"}}]}}],"alphafold_very_low_content":0.3888888888888889,"disorder_content":0.43209876543209874,"disprot_consensus":{"full":[{"start":93,"end":162,"type":"D"}],"Structural state":[{"start":93,"end":162,"type":"D"}],"Molecular function":[{"start":93,"end":162,"type":"F"}]}},{"features":{"pfam":[{"id":"PF15901","name":"Sortilin, neurotensin receptor 3, C-terminal","start":575,"end":740},{"id":"PF15902","name":"Sortilin, neurotensin receptor 3,","start":142,"end":572}],"gene3D":[{"start":314,"end":533,"id":"2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"},{"start":122,"end":313,"id":"2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"},{"start":667,"end":744,"id":"2.10.70.90","name":"2.10.70.90"},{"start":610,"end":666,"id":"2.10.70.80","name":"2.10.70.80"}]},"uniref50":"UniRef50_Q99523","sequence":"MERPWGAADGLSRWPHGLGLLLLLQLLPPSTLSQDRLDAPPPPAAPLPRWSGPIGVSWGLRAAAAGGAFPRGGRWRRSAPGEDEECGRVRDFVAKLANNTHQHVFDDLRGSVSLSWVGDSTGVILVLTTFHVPLVIMTFGQSKLYRSEDYGKNFKDITDLINNTFIRTEFGMAIGPENSGKVVLTAEVSGGSRGGRIFRSSDFAKNFVQTDLPFHPLTQMMYSPQNSDYLLALSTENGLWVSKNFGGKWEEIHKAVCLAKWGSDNTIFFTTYANGSCKADLGALELWRTSDLGKSFKTIGVKIYSFGLGGRFLFASVMADKDTTRRIHVSTDQGDTWSMAQLPSVGQEQFYSILAANDDMVFMHVDEPGDTGFGTIFTSDDRGIVYSKSLDRHLYTTTGGETDFTNVTSLRGVYITSVLSEDNSIQTMITFDQGGRWTHLRKPENSECDATAKNKNECSLHIHASYSISQKLNVPMAPLSEPNAVGIVIAHGSVGDAISVMVPDVYISDDGGYSWTKMLEGPHYYTILDSGGIIVAIEHSSRPINVIKFSTDEGQCWQTYTFTRDPIYFTGLASEPGARSMNISIWGFTESFLTSQWVSYTIDFKDILERNCEEKDYTIWLAHSTDPEDYEDGCILGYKEQFLRLRKSSVCQNGRDYVVTKQPSICLCSLEDFLCDFGYYRPENDSKCVEQPELKGHDLEFCLYGREEHLTTNGYRKIPGDKCQGGVNPVREVKDLKKKCTSNFLSPEKQNSKSNSVPIILAIVGLMLVTVVAGVLIVKKYVCGGRFLVHRYSVLQQHAEANGVDGVDALDTASHTNKSGYHDDSDEDLLE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q99523","disprot_id":"DP01551","ncbi_taxon_id":9606,"regions_counter":1,"creator":"jlamb","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":108,"region_id":"DP01551r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Ligands bind to Sortilin in the tunnel of a ten-bladed beta-propeller domain. <i> Quistgaard EM, Madsen P, Grøftehauge MK, Nissen P, Petersen CM, Thirup SS. </i> Nat Struct Mol Biol, 2009","statement":[{"text":"Figure 1 in original article and Supplementary material figure 4 text.","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"jlamb","start":97,"term_ontology":"IDPO","curator_name":"John Lamb","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0568-8281","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19122660","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q99523","date":"2018-07-26T18:43:01.000Z","acc":"Q99523","name":"Sortilin","length":831,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000135CE9","genes":[{"name":{"value":"SORT1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11186","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11186"}}]}}],"alphafold_very_low_content":0.16726835138387486,"disorder_content":0.01444043321299639,"disprot_consensus":{"full":[{"start":97,"end":108,"type":"D"}],"Structural state":[{"start":97,"end":108,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01023","name":"S-100/ICaBP type calcium binding domain","start":5,"end":42}],"gene3D":[{"start":1,"end":92,"id":"1.10.238.10","name":"EF-hand"}]},"uniref50":"UniRef50_P33763","sequence":"METPLEKALTTMVTTFHKYSGREGSKLTLSRKELKELIKKELCLGEMKESSIDDLMKSLDKNSDQEIDFKEYSVFLTMLCMAYNDFFLEDNK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P33763","disprot_id":"DP01552","ncbi_taxon_id":9606,"regions_counter":1,"creator":"jlamb","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":52,"region_id":"DP01552r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure and dynamics of S100A5 in the apo and Ca2+-bound states. <i> Bertini I, Das Gupta S, Hu X, Karavelas T, Luchinat C, Parigi G, Yuan J. </i> J Biol Inorg Chem, 2009","statement":[{"text":"Also see supplements. In both apo-S100A5 and Ca2-S100A5, the relaxation\nrate measurements show large mobility on a time scale\nshorter than the reorientation time (R1 increases, R2\ndecreases, the NOE decreases) in the hinge loop and for the\nlast residues at the C-terminus, thus indicating that such\nregions may be largely unstructured.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jlamb","start":38,"term_ontology":"IDPO","curator_name":"John Lamb","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0568-8281","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19536568","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P33763","date":"2018-07-26T19:11:01.000Z","acc":"P33763","name":"Protein S100-A5","length":92,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00001353F4","genes":[{"name":{"value":"S100A5"},"synonyms":[{"value":"S100D"}]}],"alphafold_very_low_content":0,"disorder_content":0.16304347826086957,"disprot_consensus":{"full":[{"start":38,"end":52,"type":"D"}],"Structural state":[{"start":38,"end":52,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":9,"end":78}],"gene3D":[{"start":2,"end":102,"id":"3.30.70.330","name":"3.30.70.330"}]},"uniref50":"UniRef50_Q03878","sequence":"MAEVEYRCFVGGLAWATTDQTLGEAFSQFGEILDSKIINDRETGRSRGFGFVTFKDEKAMRDAIEGMNGQDLDGRNITVNEAQSRGSGGGGGGGGYRGGSGGGYGGGGRREGGYGGGGGYGGGRREGGYGGGGGGGYGGGRREGGYGGGSEGNWRS","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","lamiids","Solanales","Solanaceae","Nicotianoideae","Nicotianeae","Nicotiana"],"uniref90":"UniRef90_A0A1S4A939","disprot_id":"DP01553","ncbi_taxon_id":4097,"regions_counter":2,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":156,"region_id":"DP01553r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis of nucleic acid binding by Nicotiana tabacum glycine-rich RNA-binding protein: implications for its RNA chaperone function. <i> Khan F, Daniëls MA, Folkers GE, Boelens R, Saqlan Naqvi SM, van Ingen H. </i> Nucleic Acids Res, 2014","statement":[{"text":"The significant amount of peak doubling suggests that the non-glycine residues in the GR experience different chemical environments in relatively stable different conformations of the GR. The lack of 1H chemical shift dispersion for the GR resonances indicates a lack of structure. The peak doubling, broadened GR peaks and the perturbations of RRM resonances suggest that the GR may transiently interacts with the RRM.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":86,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"24957607","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":156,"term_name":"protein binding","start":86,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Together, these observations strongly suggest that the GR of the full-length protein can associate specifically to the RRM domain in an intermolecular fashion.","type":"Results"}],"curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"24957607","version":3,"reference_html":"Structural basis of nucleic acid binding by Nicotiana tabacum glycine-rich RNA-binding protein: implications for its RNA chaperone function. <i> Khan F, Daniëls MA, Folkers GE, Boelens R, Saqlan Naqvi SM, van Ingen H. </i> Nucleic Acids Res, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP01553r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q40426","date":"2018-07-26T19:13:04.000Z","acc":"D6PZY5","name":"RNA-binding glycine-rich protein","length":156,"organism":"Nicotiana tabacum","dataset":[],"UniParc":"UPI00000A690A","genes":[{"name":{"value":"RGP-1a","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ADG03637.1","url":"https://www.ebi.ac.uk/ena/browser/view/ADG03637.1"}}]},"synonyms":[{"value":"LOC107800679","evidences":[{"code":"ECO:0000313","source":{"name":"RefSeq","id":"XP_016479391.1","url":"https://www.ncbi.nlm.nih.gov/protein/XP_016479391.1"}}]}]}],"alphafold_very_low_content":0.3974358974358974,"disorder_content":0.4551282051282051,"disprot_consensus":{"full":[{"start":86,"end":156,"type":"D"}],"Structural state":[{"start":86,"end":156,"type":"D"}],"Molecular function":[{"start":86,"end":156,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":91,"end":352},{"id":"PF00433","name":"Protein kinase C terminal domain","start":373,"end":413}],"gene3D":[{"start":91,"end":387,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":179,"end":374,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"}]},"uniref50":"UniRef50_P67999","sequence":"MRRRRRRDGFYPAPDFRDREAEDMAGVFDIDLDQPEDAGSEDELEEGGQLNESMDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPECFELLRVLGKGGYGKVFQVRKVTGANTGKIFAMKVLKKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEISMALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPFTGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFDSKFTRQTPVDSPDDSTLSESANQVFLGFTYVAPSVLESVKEKFSFEPKIRSPRRFIGSPRTPVSPVKFSPGDFWGRGASASTANPQTPVEYPMETSGIEQMDVTMSGEASAPLPIRQPNSGPYKKQAFPMISKRPEHLRMNL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P67999","disprot_id":"DP01554","ncbi_taxon_id":9606,"regions_counter":19,"creator":"zskalman","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":525,"region_id":"DP01554r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Expression, purification, and characterization of a structurally disordered and functional C-terminal autoinhibitory domain (AID) of the 70 kDa 40S ribosomal protein S6 kinase-1 (S6K1). <i> Ragan TJ, Ross DB, Keshwani MM, Harris TK. </i> Protein Expr Purif, 2008","statement":[{"text":"In the 1H-15N HSQC spectrum of uniformly 15N-labeled AID (res. 422-525) the majority of backbone amide proton resonances exhibited poor chemical shift dispersion (∼7.8-8.6 ppm), indicating substantial regions of structural disorder. In addition, the majority of resonances were either broadened or missing, indicating interconversion between multiple conformations within the “intermediate” spectroscopic timescale.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":422,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"17980619","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":525,"term_name":"self-inhibition","start":422,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"The best characterized function of the C-terminal AID is inhibition of upstream kinase-mediated HM (T412) and T-loop (T252) phosphorylation events, required for S6K1 activation. Trans-addition of purified recombinant ‘disordered’ AID does indeed effectively inhibit S6K1 phosphorylation by PDK1.","type":"Results"}],"curator_id":"nmurvai","released":"2022_03","term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"17980619","version":3,"reference_html":"Expression, purification, and characterization of a structurally disordered and functional C-terminal autoinhibitory domain (AID) of the 70 kDa 40S ribosomal protein S6 kinase-1 (S6K1). <i> Ragan TJ, Ross DB, Keshwani MM, Harris TK. </i> Protein Expr Purif, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000059","ec_id":"ECO:0006165","region_id":"DP01554r002","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":525,"term_name":"molecular recognition display site","start":422,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Multi-site Ser-Thr phosphorylation of AID (S434, S441, T444, and S447 in S6K1) destabilizes its autoinhibitory interaction with the kinase domain of S6K1.","type":"Results"}],"curator_id":"nmurvai","released":"2022_03","term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"17980619","version":2,"reference_html":"Expression, purification, and characterization of a structurally disordered and functional C-terminal autoinhibitory domain (AID) of the 70 kDa 40S ribosomal protein S6 kinase-1 (S6K1). <i> Ragan TJ, Ross DB, Keshwani MM, Harris TK. </i> Protein Expr Purif, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000037","ec_id":"ECO:0006165","region_id":"DP01554r003","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":525,"region_id":"DP01554r004","released":"2022_03","ec_id":"ECO:0007689","reference_html":"Expression, purification, and characterization of a structurally disordered and functional C-terminal autoinhibitory domain (AID) of the 70 kDa 40S ribosomal protein S6 kinase-1 (S6K1). <i> Ragan TJ, Ross DB, Keshwani MM, Harris TK. </i> Protein Expr Purif, 2008","statement":[{"text":"AID displayed anomalously slower mobility in SDS-PAGE (apparent molecular mass of 15 kDa), that is 1.25-fold higher than the molecular mass of 11,988 Da calculated from its amino acid sequence.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":422,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"17980619","version":2,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":525,"region_id":"DP01554r005","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Expression, purification, and characterization of a structurally disordered and functional C-terminal autoinhibitory domain (AID) of the 70 kDa 40S ribosomal protein S6 kinase-1 (S6K1). <i> Ragan TJ, Ross DB, Keshwani MM, Harris TK. </i> Protein Expr Purif, 2008","statement":[{"text":"AID displayed anomalously faster mobility in Superdex™ 75 size exclusion chromatography (apparent molecular mass of 15 kDa), 1.25-fold higher than the molecular mass of 11,988 Da calculated from its amino acid sequence.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":422,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"17980619","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":75,"end":84,"reference_id":"19864428","reference_source":"pmid","reference_html":"Structural basis of human p70 ribosomal S6 kinase-1 regulation by activation loop phosphorylation. <i> Sunami T, Byrne N, Diehl RE, Funabashi K, Hall DL, Ikuta M, Patel SB, Shipman JM, Smith RF, Takahashi I, Zugay-Murphy J, Iwasawa Y, Lumb KJ, Munshi SK, Sharma S. </i> J Biol Chem, 2010","date":"2025-04-02T09:18:59.426Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"3A60"},{"db":"PDB","id":"3A61"}],"region_id":"DP01554r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"44259 "}],"sequence_construct":"GSSETSVNRGPEKIRPECFELLRVLGKGGYGKVFQVRKVTGANTGKIFAMKVLKKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEISMALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPFTGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFDSKFTRQTPVDSPDDST","statement":[{"text":"Residues 75–84 at the N terminus and residues 372–399 at the C terminus are disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-04-02T18:34:42.118Z"}},{"start":130,"end":140,"reference_id":"19864428","reference_source":"pmid","reference_html":"Structural basis of human p70 ribosomal S6 kinase-1 regulation by activation loop phosphorylation. <i> Sunami T, Byrne N, Diehl RE, Funabashi K, Hall DL, Ikuta M, Patel SB, Shipman JM, Smith RF, Takahashi I, Zugay-Murphy J, Iwasawa Y, Lumb KJ, Munshi SK, Sharma S. </i> J Biol Chem, 2010","date":"2025-04-02T09:25:42.968Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"3A60"},{"db":"PDB","id":"3A61"}],"region_id":"DP01554r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"44259 "}],"sequence_construct":"GSSETSVNRGPEKIRPECFELLRVLGKGGYGKVFQVRKVTGANTGKIFAMKVLKKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEISMALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPFTGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFDSKFTRQTPVDSPDDST","statement":[{"text":"In addition, residues 130–140 of the putative helices αB and αC and residues 243–255 of the putative activation loop are also disordered (Fig. 6B).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-04-02T18:34:51.670Z"}},{"start":243,"end":254,"reference_id":"19864428","reference_source":"pmid","reference_html":"Structural basis of human p70 ribosomal S6 kinase-1 regulation by activation loop phosphorylation. <i> Sunami T, Byrne N, Diehl RE, Funabashi K, Hall DL, Ikuta M, Patel SB, Shipman JM, Smith RF, Takahashi I, Zugay-Murphy J, Iwasawa Y, Lumb KJ, Munshi SK, Sharma S. </i> J Biol Chem, 2010","date":"2025-04-02T09:25:30.484Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"3A60"},{"db":"PDB","id":"3A61"}],"region_id":"DP01554r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"44259 "}],"sequence_construct":"GSSETSVNRGPEKIRPECFELLRVLGKGGYGKVFQVRKVTGANTGKIFAMKVLKKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEISMALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPFTGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFDSKFTRQTPVDSPDDST","statement":[{"text":"In addition, residues 130–140 of the putative helices αB and αC and residues 243–255 of the putative activation loop are also disordered (Fig. 6B).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-04-02T18:34:59.836Z"}},{"start":379,"end":399,"reference_id":"19864428","reference_source":"pmid","reference_html":"Structural basis of human p70 ribosomal S6 kinase-1 regulation by activation loop phosphorylation. <i> Sunami T, Byrne N, Diehl RE, Funabashi K, Hall DL, Ikuta M, Patel SB, Shipman JM, Smith RF, Takahashi I, Zugay-Murphy J, Iwasawa Y, Lumb KJ, Munshi SK, Sharma S. </i> J Biol Chem, 2010","date":"2025-04-02T09:25:58.424Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"3A60"},{"db":"PDB","id":"3A61"}],"region_id":"DP01554r009","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"44259 "}],"sequence_construct":"GSSETSVNRGPEKIRPECFELLRVLGKGGYGKVFQVRKVTGANTGKIFAMKVLKKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEISMALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPFTGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFDSKFTRQTPVDSPDDST","statement":[{"text":"Residues 75–84 at the N terminus and residues 372–399 at the C terminus are disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-04-02T18:35:10.487Z"}},{"start":250,"end":255,"reference_id":"19864428","reference_source":"pmid","reference_html":"Structural basis of human p70 ribosomal S6 kinase-1 regulation by activation loop phosphorylation. <i> Sunami T, Byrne N, Diehl RE, Funabashi K, Hall DL, Ikuta M, Patel SB, Shipman JM, Smith RF, Takahashi I, Zugay-Murphy J, Iwasawa Y, Lumb KJ, Munshi SK, Sharma S. </i> J Biol Chem, 2010","date":"2025-04-02T09:16:48.336Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":252,"end":252,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"3A62"}],"region_id":"DP01554r016","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"27854"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"23930"}],"sequence_construct":"GSSETSVNRGPEKIRPECFELLRVLGKGGYGKVFQVRKVTGANTGKIFAMKVLKKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEISMALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPFTGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFDSKFTRQTPVDSPDDST","statement":[{"text":"At least three phosphorylation events appear necessary for activation of p70S6K1 at Thr-252, Ser-394, and Thr-412.","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-04-02T18:37:42.721Z"}},{"start":373,"end":399,"reference_id":"19864428","reference_source":"pmid","reference_html":"Structural basis of human p70 ribosomal S6 kinase-1 regulation by activation loop phosphorylation. <i> Sunami T, Byrne N, Diehl RE, Funabashi K, Hall DL, Ikuta M, Patel SB, Shipman JM, Smith RF, Takahashi I, Zugay-Murphy J, Iwasawa Y, Lumb KJ, Munshi SK, Sharma S. </i> J Biol Chem, 2010","date":"2025-06-25T06:28:13.417Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":252,"end":252,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"3A62"}],"region_id":"DP01554r017","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"44259"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"29035"}],"sequence_construct":"GSSETSVNRGPEKIRPECFELLRVLGKGGYGKVFQVRKVTGANTGKIFAMKVLKKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEISMALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPFTGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFDSKFTRQTPVDSPDDST","statement":[{"text":"Missing electron density for this region.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-30T16:12:39.731Z"}},{"start":250,"end":255,"reference_id":"19864428","reference_source":"pmid","reference_html":"Structural basis of human p70 ribosomal S6 kinase-1 regulation by activation loop phosphorylation. <i> Sunami T, Byrne N, Diehl RE, Funabashi K, Hall DL, Ikuta M, Patel SB, Shipman JM, Smith RF, Takahashi I, Zugay-Murphy J, Iwasawa Y, Lumb KJ, Munshi SK, Sharma S. </i> J Biol Chem, 2010","date":"2025-02-03T20:39:06.764Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0043549","term_name":"regulation of kinase activity","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001202","ec_ontology":"ECO","ec_name":"in vitro protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","region_id":"DP01554r018","statement":[{"text":"The dephosphorylated protein was found to be catalytically inactive. Some activity could be restored upon phosphorylation of Thr-252 with PDK1 (Fig. 3A).","type":"Results"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.\" [GOC:bf]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_P23443","date":"2018-07-26T19:56:01.000Z","acc":"P23443","name":"Ribosomal protein S6 kinase beta-1","length":525,"organism":"Homo sapiens","dataset":["Autophagy-related proteins"],"UniParc":"UPI000012DB33","genes":[{"name":{"value":"RPS6KB1"},"synonyms":[{"value":"STK14A"}]}],"alphafold_very_low_content":0.3333333333333333,"disorder_content":0.31238095238095237,"disprot_consensus":{"full":[{"start":75,"end":84,"type":"D"},{"start":130,"end":140,"type":"D"},{"start":243,"end":254,"type":"D"},{"start":255,"end":255,"type":"F"},{"start":373,"end":399,"type":"D"},{"start":422,"end":525,"type":"D"}],"Structural state":[{"start":75,"end":84,"type":"D"},{"start":130,"end":140,"type":"D"},{"start":243,"end":254,"type":"D"},{"start":373,"end":399,"type":"D"},{"start":422,"end":525,"type":"D"}],"Disorder function":[{"start":250,"end":255,"type":"F"},{"start":422,"end":525,"type":"F"}],"Biological process":[{"start":250,"end":255,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00096","name":"Zinc finger, C2H2 type","start":218,"end":240},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":246,"end":268},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":274,"end":296},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":302,"end":324},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":358,"end":380},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":387,"end":408},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":414,"end":436},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":498,"end":520},{"id":"PF01352","name":"KRAB box","start":13,"end":54},{"id":"PF13465","name":"Zinc-finger double domain","start":456,"end":481}],"gene3D":[{"start":300,"end":326,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":435,"end":463,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":464,"end":492,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":353,"end":383,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":327,"end":352,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":493,"end":522,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":386,"end":412,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":245,"end":270,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":413,"end":434,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":271,"end":299,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":216,"end":244,"id":"3.30.160.60","name":"Classic Zinc Finger"}]},"uniref50":"UniRef50_Q86Y25","sequence":"MAVDLLAARGTEPVTFRDVAVSFSQDEWLHLDPAQRTLYREVMLENYSNLASLGFQASIPPVIGKLQKGQDPCMEREAPEDTCLDFQIQSEIEASSPEQDVFIEGPSRGLLKNRSTKCAYWKISFGELVKYERLETAQEQEKKAHEPGAASPKEVTSEDGIPTDPELEKPLFMNKALVSQETDPIERVPGMYHTSEKDLPQDFDLMRNFQIYPGQKPYVCSECGKGFSQSLHLLEHKRIHTGEKPYKCSECGKSFSHRSSLLAHQRTHTGEKPYKCSECEKAFGSSSTLIKHLRVHTGEKPYRCRECGKAFSQCSTLTVHQRIHTGEKLYKCAECDKAFNCRAKLHRHQRIHTGEKPYKCAECGKGYSQFPSLAEHQRLHTGGQLCQCLQCGRTFTRVSTLIEHQRIHTGQKPYQCNECGKTFNQYSSFNEHRKIHTGEKLYTCEECGKAFGCKSNLYRHQRIHTGEKPYQCNQCGKAFSQYSFLTEHERIHTGEKLYKCMECGKAYSYRSNLCRHKKVHLKERLYKWKEYGTPFMYGSSLAPHQRCLKGEKPEDLNSSL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_Q9EPU7","disprot_id":"DP01555","ncbi_taxon_id":10116,"regions_counter":5,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":91,"region_id":"DP01555r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The structurally disordered KRAB repression domain is incorporated into a protease resistant core upon binding to KAP-1-RBCC domain. <i> Peng H, Gibson LC, Capili AD, Borden KL, Osborne MJ, Harper SL, Speicher DW, Zhao K, Marmorstein R, Rock TA, Rauscher FJ. </i> J Mol Biol, 2007","statement":[{"text":"CD spectra of AJ18–KRAB(Ab) showed that ity contains mostly random coil (56% ∼ 65%) with a small degree of helix (35% ∼ 39%) but little β sheet (0 ∼ 5%). These data suggest that the KRAB domain alone may not be highly structured.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":4,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"17512541","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":91,"region_id":"DP01555r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The structurally disordered KRAB repression domain is incorporated into a protease resistant core upon binding to KAP-1-RBCC domain. <i> Peng H, Gibson LC, Capili AD, Borden KL, Osborne MJ, Harper SL, Speicher DW, Zhao K, Marmorstein R, Rock TA, Rauscher FJ. </i> J Mol Biol, 2007","statement":[{"text":"The HSQC spectra of His-AJ18 KRAB(Ab) shows that the majority of backbone amide resonances exhibit poor dispersion, indicating substantial regions of disordered structure, consistent with CD results. NOESY of the sample exhibited minimal NOE cross-peaks providing further evidence of lack of a well defined 3D conformation. The 1D 1H spectra further confirm the lack of structure for the KRAB fragment.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":4,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"17512541","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":91,"term_name":"protein binding","start":4,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"The loss of signals is consistent with KRAB(Ab) binding to the much larger KAP-1–RBCC protein. Given that the KRAB(Ab):KAP-1–RBCC complex is 1:3 molar ratio, the complex is a 180 kDa species. Here molecular tumbling is slow therefore the NMR signals are too broad to be readily detected. Therefore, the loss of observable peaks in the complex versus in the free spectra indicates that KRAB(Ab) was binding to KAP-1–RBCC.","type":"Results"}],"curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"17512541","version":3,"reference_html":"The structurally disordered KRAB repression domain is incorporated into a protease resistant core upon binding to KAP-1-RBCC domain. <i> Peng H, Gibson LC, Capili AD, Borden KL, Osborne MJ, Harper SL, Speicher DW, Zhao K, Marmorstein R, Rock TA, Rauscher FJ. </i> J Mol Biol, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP01555r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":91,"term_name":"disorder to order","start":4,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"The results of the proteolysis of the KRAB:KAP-1 complex, suggest that KRAB is well folded upon binding KAP-1. In addition, the spectrum of KRAB in complex with KAP-1–RBCC exhibits no heterogeneity, which would be expected if some chemical exchange processes were present.","type":"Results"}],"curator_id":"nmurvai","released":"2022_03","term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"17512541","version":2,"reference_html":"The structurally disordered KRAB repression domain is incorporated into a protease resistant core upon binding to KAP-1-RBCC domain. <i> Peng H, Gibson LC, Capili AD, Borden KL, Osborne MJ, Harper SL, Speicher DW, Zhao K, Marmorstein R, Rock TA, Rauscher FJ. </i> J Mol Biol, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP01555r004","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":91,"region_id":"DP01555r005","released":"2022_03","ec_id":"ECO:0007691","reference_html":"The structurally disordered KRAB repression domain is incorporated into a protease resistant core upon binding to KAP-1-RBCC domain. <i> Peng H, Gibson LC, Capili AD, Borden KL, Osborne MJ, Harper SL, Speicher DW, Zhao K, Marmorstein R, Rock TA, Rauscher FJ. </i> J Mol Biol, 2007","statement":[{"text":"the proteolysis of the free KRAB constructs, clearly indicates that any such structure is transient as it does not lead to protection from proteases.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":4,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"17512541","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9EPU7","date":"2018-07-26T20:32:59.000Z","acc":"Q9EPU7","name":"Zinc finger protein 354C","length":560,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI00000E6828","genes":[{"name":{"value":"Znf354c"},"synonyms":[{"value":"Zfp354c"}]}],"alphafold_very_low_content":0.31607142857142856,"disorder_content":0.15714285714285714,"disprot_consensus":{"full":[{"start":4,"end":91,"type":"T"}],"Structural state":[{"start":4,"end":91,"type":"D"}],"Molecular function":[{"start":4,"end":91,"type":"F"}],"Structural transition":[{"start":4,"end":91,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00096","name":"Zinc finger, C2H2 type","start":508,"end":529},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":535,"end":557},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":563,"end":585},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":591,"end":613},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":619,"end":641},{"id":"PF01352","name":"KRAB box","start":13,"end":53},{"id":"PF01352","name":"KRAB box","start":286,"end":327},{"id":"PF02023","name":"SCAN domain","start":157,"end":245}],"gene3D":[{"start":152,"end":244,"id":"1.10.4020.10","name":"DNA breaking-rejoining enzymes"},{"start":615,"end":643,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":506,"end":534,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":535,"end":560,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":589,"end":614,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":561,"end":588,"id":"3.30.160.60","name":"Classic Zinc Finger"}]},"uniref50":"UniRef50_Q96GC6","sequence":"MASRLPTAWSCEPVTFEDVTLGFTPEEWGLLDLKQKSLYREVMLENYRNLVSVEHQLSKPDVVSQLEEAEDFWPVERGIPQDTIPEYPELQLDPKLDPLPAESPLMNIEVVEVLTLNQEVAGPRNAQIQALYAEDGSLSADAPSEQVQQQGKHPGDPEAARQRFRQFRYKDMTGPREALDQLRELCHQWLQPKARSKEQILELLVLEQFLGALPVKLRTWVESQHPENCQEVVALVEGVTWMSEEEVLPAGQPAEGTTCCLEVTAQQEEKQEDAAICPVTVLPEEPVTFQDVAVDFSREEWGLLGPTQRTEYRDVMLETFGHLVSVGWETTLENKELAPNSDIPEEEPAPSLKVQESSRDCALSSTLEDTLQGGVQEVQDTVLKQMESAQEKDLPQKKHFDNRESQANSGALDTNQVSLQKIDNPESQANSGALDTNQVLLHKIPPRKRLRKRDSQVKSMKHNSRVKIHQKSCERQKAKEGNGCRKTFSRSTKQITFIRIHKGSQVCRCSECGKIFRNPRYFSVHKKIHTGERPYVCQDCGKGFVQSSSLTQHQRVHSGERPFECQECGRTFNDRSAISQHLRTHTGAKPYKCQDCGKAFRQSSHLIRHQRTHTGERPYACNKCGKAFTQSSHLIGHQRTHNRTKRKKKQPTS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q96GC6","disprot_id":"DP01556","ncbi_taxon_id":9606,"regions_counter":4,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":77,"region_id":"DP01556r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The structurally disordered KRAB repression domain is incorporated into a protease resistant core upon binding to KAP-1-RBCC domain. <i> Peng H, Gibson LC, Capili AD, Borden KL, Osborne MJ, Harper SL, Speicher DW, Zhao K, Marmorstein R, Rock TA, Rauscher FJ. </i> J Mol Biol, 2007","statement":[{"text":"The HSQC spectra of ZNF274-KRAB(AB) shows that the majority of backbone amide resonances exhibit poor dispersion, indicating substantial regions of disordered structure. Most backbone resonances fall (> 95%) within the center of the spectrum (7.7 ppm to 8.5 ppm), some are broadened or missing indicating intermediate timescale motions. Minimal NOE cross-peaks and the 1D 1H spectra confirm the lack of structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":4,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"17512541","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":77,"term_name":"protein binding","start":4,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Transcriptional repression by the KRAB domains correlates with its binding to KAP-1 (KRAB associated protein 1), also referred to as TIF1β or KRIP-1. The KRAB domain binds directly with high affinity to the RBCC domain of KAP-1.","type":"Introduction"}],"curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"17512541","version":3,"reference_html":"The structurally disordered KRAB repression domain is incorporated into a protease resistant core upon binding to KAP-1-RBCC domain. <i> Peng H, Gibson LC, Capili AD, Borden KL, Osborne MJ, Harper SL, Speicher DW, Zhao K, Marmorstein R, Rock TA, Rauscher FJ. </i> J Mol Biol, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP01556r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":77,"region_id":"DP01556r003","released":"2022_03","ec_id":"ECO:0007691","reference_html":"The structurally disordered KRAB repression domain is incorporated into a protease resistant core upon binding to KAP-1-RBCC domain. <i> Peng H, Gibson LC, Capili AD, Borden KL, Osborne MJ, Harper SL, Speicher DW, Zhao K, Marmorstein R, Rock TA, Rauscher FJ. </i> J Mol Biol, 2007","statement":[{"text":"Consistent with these studies, the proteolysis of the free KRAB constructs, clearly indicates that any such structure is transient as it does not lead to protection from proteases.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":4,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"17512541","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":246,"region_id":"DP01556r004","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The structurally disordered KRAB repression domain is incorporated into a protease resistant core upon binding to KAP-1-RBCC domain. <i> Peng H, Gibson LC, Capili AD, Borden KL, Osborne MJ, Harper SL, Speicher DW, Zhao K, Marmorstein R, Rock TA, Rauscher FJ. </i> J Mol Biol, 2007","statement":[{"text":"CD spectra of the ZNF274–KRAB(AB)-SCAN protein construct showed that it contains mostly random coil (56% ∼ 65%) with a small degree of helix (35% ∼ 39%) but little β sheet (0 ∼ 5%). These data suggest that the KRAB domain alone may not be highly structured.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":4,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"17512541","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q96GC6","date":"2018-07-26T20:54:39.000Z","acc":"Q96GC6","name":"Neurotrophin receptor-interacting factor homolog","length":653,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000161F3D","genes":[{"name":{"value":"ZNF274"},"synonyms":[{"value":"ZKSCAN19"}],"orfNames":[{"value":"SP2114"}]}],"alphafold_very_low_content":0.4686064318529862,"disorder_content":0.3721286370597244,"disprot_consensus":{"full":[{"start":4,"end":246,"type":"D"}],"Structural state":[{"start":4,"end":246,"type":"D"}],"Molecular function":[{"start":4,"end":77,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05281","name":"Neuroendocrine protein 7B2 precursor (Secretogranin V)","start":62,"end":153}]},"uniref50":"UniRef50_P12961","sequence":"MTSRMAILSGLLFWLLLEWNPAFAYSPRTPDRVSETDIQRLLHGVMEQLGIARPRVEYPAHQAMNLVGPQSIEGGAHEGLQHLGPFGNIPNIVAELTGDNIPKDFSEDQGYPDPPNPCPLGKTADDGCLENAPDTAEFSREFQLDQHLFDPEHDYPGLGKWNKKLLYEKMKGGQRRKRRSVNPYLQGKRLDNVVAKKSVPHFSEEEKEPE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_P12961","disprot_id":"DP01557","ncbi_taxon_id":10116,"regions_counter":3,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":210,"region_id":"DP01557r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The neuroendocrine protein 7B2 is intrinsically disordered. <i> Dasgupta I, Sanglas L, Enghild JJ, Lindberg I. </i> Biochemistry, 2012","statement":[{"text":"The far-UV CD spectra of the 7B2  did not support the presence of secondary structures such as α helices or β strands. The characteristic negative peaks at 208 and 222 nm displayed by α helical proteins were not visible in 7B2 spectra. The α helical content was estimated as 29% for 27 kDa 7B2, while the β sheet content was 14%.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":25,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"22947085","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":210,"region_id":"DP01557r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The neuroendocrine protein 7B2 is intrinsically disordered. <i> Dasgupta I, Sanglas L, Enghild JJ, Lindberg I. </i> Biochemistry, 2012","statement":[{"text":"The 1H–15N HSQC spectrum displayed considerably smaller number of peaks than would be expected from a well-folded 186-residue protein. The chemical shift dispersion was extremely narrow, between 6.9 and 8.4 ppm, indicative of unfolded protein. This conclusion was strengthened by the natural abundance 13C–1H HSQC spectrum, where we observed far fewer peaks and poor chemical shift dispersion.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":25,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"22947085","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":210,"term_name":"protein binding","start":25,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"7B2 is a small secretory protein that is known to be required for the productive maturation of the subtilisin-like endoprotease prohormone convertase 2 (proPC2). The motifs and domains required for the interaction between 7B2 and proPC2 are established.","type":"Introduction"}],"curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"22947085","version":3,"reference_html":"The neuroendocrine protein 7B2 is intrinsically disordered. <i> Dasgupta I, Sanglas L, Enghild JJ, Lindberg I. </i> Biochemistry, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP01557r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P27682","date":"2018-07-26T21:40:44.000Z","acc":"P27682","name":"Neuroendocrine protein 7B2","length":210,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI0000124F9A","genes":[{"name":{"value":"Scg5"},"synonyms":[{"value":"Sgne1"}]}],"alphafold_very_low_content":0.21428571428571427,"disorder_content":0.8857142857142857,"disprot_consensus":{"full":[{"start":25,"end":210,"type":"D"}],"Structural state":[{"start":25,"end":210,"type":"D"}],"Molecular function":[{"start":25,"end":210,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05281","name":"Neuroendocrine protein 7B2 precursor (Secretogranin V)","start":39,"end":205}]},"uniref50":"UniRef50_Q9XTY3","sequence":"MIGAVSLVFFTVGVAAIYGLDLENAGDFVLPSGDFIDLISRDSENLPDLSSFGVKHISGGAGEGEQKLLEEDNFQERQEVKVDNVLPAYCEPPNPCPVGFTKEHGCLEEFENSAEFSRNYQADQHCICDQEHMFNCAEKEAQDVSESLQKILEENNMHANTIAKKFHDKRSSDEYVPRRKRSIPSSAHKVNPYLQGEPLRSMQKKNGKHSW","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"uniref90":"UniRef90_Q9XTY3","disprot_id":"DP01558","ncbi_taxon_id":6239,"regions_counter":2,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":211,"region_id":"DP01558r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The neuroendocrine protein 7B2 is intrinsically disordered. <i> Dasgupta I, Sanglas L, Enghild JJ, Lindberg I. </i> Biochemistry, 2012","statement":[{"text":"The far-UV CD spectra of the 7B2 protein samples did not support the presence of typical secondary structures elements. The characteristic negative peaks at 208 and 222 nm displayed by α helical proteins were not visible in 7B2 spectra. Estimation of secondary structure content revealed that the 27 kDa C. elegans protein contained few structural elements, only 18% α helix and 26% β sheet content.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":17,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"22947085","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":211,"term_name":"protein binding","start":17,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"Despite the low level of overall sequence conservation, the physiological functions of the C. elegans protein with regard to help the maturation of prohormone convertase 2 (proPC2) within the secretory pathway appear to be similar to those of the vertebrate proteins.","type":"Introduction"}],"curator_id":"nmurvai","released":"2022_03","term_ontology":"GO","curator_name":"Nikoletta Murvai","reference_id":"22947085","version":3,"reference_html":"The neuroendocrine protein 7B2 is intrinsically disordered. <i> Dasgupta I, Sanglas L, Enghild JJ, Lindberg I. </i> Biochemistry, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP01558r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q9XTY3","date":"2018-07-26T22:07:41.000Z","acc":"Q9XTY3","name":"Seven B Two (Mammalian 7BT prohormone convertase chaperone) homolog","length":211,"organism":"Caenorhabditis elegans","dataset":[],"UniParc":"UPI000007873E","genes":[{"name":{"value":"sbt-1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAB07408.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAB07408.1"}},{"code":"ECO:0000313","source":{"name":"WormBase","id":"T03D8.3","url":"https://www.wormbase.org/db/seq/sequence?name=T03D8.3;class=Transcript"}}]},"orfNames":[{"value":"CELE_T03D8.3","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAB07408.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAB07408.1"}}]},{"value":"T03D8.3","evidences":[{"code":"ECO:0000313","source":{"name":"WormBase","id":"T03D8.3","url":"https://www.wormbase.org/db/seq/sequence?name=T03D8.3;class=Transcript"}}]}]}],"alphafold_very_low_content":0.15165876777251186,"disorder_content":0.9241706161137441,"disprot_consensus":{"full":[{"start":17,"end":211,"type":"D"}],"Structural state":[{"start":17,"end":211,"type":"D"}],"Molecular function":[{"start":17,"end":211,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_Q04964","sequence":"MQNSQDYFYAQNRCQQQQAPSTLRTVTMAEFRRVPLPPMAEVPMLSTQNSMGSSASASASSLEMWEKDLEERLNSIDHDMNNNKFGSGELKSMFNQGKVEEMDF","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q04964","disprot_id":"DP01559","ncbi_taxon_id":559292,"regions_counter":6,"creator":"ireményi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":104,"region_id":"DP01559r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Mutational and structural analyses of the ribonucleotide reductase inhibitor Sml1 define its Rnr1 interaction domain whose inactivation allows suppression of mec1 and rad53 lethality. <i> Zhao X, Georgieva B, Chabes A, Domkin V, Ippel JH, Schleucher J, Wijmenga S, Thelander L, Rothstein R. </i> Mol Cell Biol, 2000","statement":[{"text":"Sml1 is highly flexible in solution with no defined tertiary structure. Three regions exhibited a high degree of backbone order (S2 > 0.6); residues 4 to 14, 20 to 35, and 61 to 80. Regions 4-14 and 61-80 are alpha-helical, as shown by the positive secondary Cα chemical shifts. Overall, Sml1 is best characterized as a loosely folded protein in which the two main helices are oriented in an antiparallel fashion.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":1,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"11074005","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":104,"region_id":"DP01559r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The intrinsically disordered RNR inhibitor Sml1 is a dynamic dimer. <i> Danielsson J, Liljedahl L, Bárány-Wallje E, Sønderby P, Kristensen LH, Martinez-Yamout MA, Dyson HJ, Wright PE, Poulsen FM, Mäler L, Gräslund A, Kragelund BB. </i> Biochemistry, 2008","statement":[{"text":"The small spectral width of the amide signals of Sml1 clearly indicates that the protein is mainly unfolded. Secondary chemical shifts analysis suggests the presence of two helical regions in Sml1. SSP-analysis shows that the helix propensity in region 60-80 is very high. Interestingly, the region 33-45 has β-sheet propensity. The NOE values are all above 0 and the pattern is similar as for the relaxation rates.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":1,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"19086274","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q04964","date":"2018-07-26T22:28:53.000Z","acc":"Q04964","name":"Ribonucleotide reductase inhibitor protein SML1","length":104,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000013B9AE","genes":[{"name":{"value":"SML1"},"orfNames":[{"value":"YM9958.04"}],"olnNames":[{"value":"YML058W"}]}],"alphafold_very_low_content":0.17307692307692307,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":104,"type":"D"}],"Structural state":[{"start":1,"end":104,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":117,"end":280},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":319,"end":434}],"gene3D":[{"start":303,"end":479,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":68,"end":302,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_Q9UMR2","sequence":"MATDSWALAVDEQEAAAESLSNLHLKEEKIKPDTNGAVVKTNANAEKTDEEEKEDRAAQSLLNKLIRSNLVDNTNQVEVLQRDPNSPLYSVKSFEELRLKPQLLQGVYAMGFNRPSKIQENALPLMLAEPPQNLIAQSQSGTGKTAAFVLAMLSQVEPANKYPQCLCLSPTYELALQTGKVIEQMGKFYPELKLAYAVRGNKLERGQKISEQIVIGTPGTVLDWCSKLKFIDPKKIKVFVLDEADVMIATQGHQDQSIRIQRMLPRNCQMLLFSATFEDSVWKFAQKVVPDPNVIKLKREEETLDTIKQYYVLCSSRDEKFQALCNLYGAITIAQAMIFCHTRKTASWLAAELSKEGHQVALLSGEMMVEQRAAVIERFREGKEKVLVTTNVCARGIDVEQVSVVINFDLPVDKDGNPDNETYLHRIGRTGRFGKRGLAVNMVDSKHSMNILNRIQEHFNKKIERLDTDDLDEIEKIAN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UMR2","disprot_id":"DP01560","ncbi_taxon_id":9606,"regions_counter":4,"creator":"nfoutel","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":91,"region_id":"DP01560r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The DEXD/H-box RNA helicase DDX19 is regulated by an {alpha}-helical switch. <i> Collins R, Karlberg T, Lehtiö L, Schütz P, van den Berg S, Dahlgren LG, Hammarström M, Weigelt J, Schüler H. </i> J Biol Chem, 2009","term_id":"IDPO:0000002","curator_id":"nfoutel","start":55,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"19244245","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":91,"term_name":"disorder to order","start":55,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","statement":[{"text":"The section Asp55–Ser68 of the N-terminal extension, which was partly disordered in the RNA complex, folded into an \u0001-helix that occupied the central cleft between the two lobes.","type":"Results"}],"curator_id":"nfoutel","released":"2022_03","term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"19244245","version":2,"reference_html":"The DEXD/H-box RNA helicase DDX19 is regulated by an {alpha}-helical switch. <i> Collins R, Karlberg T, Lehtiö L, Schütz P, van den Berg S, Dahlgren LG, Hammarström M, Weigelt J, Schüler H. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006220","region_id":"DP01560r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":91,"term_name":"protein binding","start":55,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","statement":[{"text":"The Asp55–Ser68 \u0001-helix makes a significant number of side chain interactions with both conserved domains.","type":"Results"}],"curator_id":"nfoutel","released":"2022_03","term_ontology":"GO","curator_name":"Nicolas Foutel","reference_id":"19244245","version":3,"reference_html":"The DEXD/H-box RNA helicase DDX19 is regulated by an {alpha}-helical switch. <i> Collins R, Karlberg T, Lehtiö L, Schütz P, van den Berg S, Dahlgren LG, Hammarström M, Weigelt J, Schüler H. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP01560r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":91,"term_name":"self-inhibition","start":55,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","statement":[{"text":"The interactions of the cleft-inserted helix with the conserved domains and with the nucleotide attest to the specificity and selectivity of the positioning of the N-terminal extension and point to a potential regulatory mechanism for the intrinsic ATPase activity of DDX19.","type":"Results"}],"curator_id":"nfoutel","released":"2022_03","term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"19244245","version":3,"reference_html":"The DEXD/H-box RNA helicase DDX19 is regulated by an {alpha}-helical switch. <i> Collins R, Karlberg T, Lehtiö L, Schütz P, van den Berg S, Dahlgren LG, Hammarström M, Weigelt J, Schüler H. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000059","ec_id":"ECO:0006220","region_id":"DP01560r004","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_Q9UMR2","date":"2018-07-27T09:40:07.000Z","acc":"Q9UMR2","name":"ATP-dependent RNA helicase DDX19B","length":479,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012907F","genes":[{"name":{"value":"DDX19B"},"synonyms":[{"value":"DBP5"},{"value":"DDX19"},{"value":"TDBP"}]}],"alphafold_very_low_content":0.10647181628392484,"disorder_content":0.07724425887265135,"disprot_consensus":{"full":[{"start":55,"end":91,"type":"T"}],"Structural state":[{"start":55,"end":91,"type":"D"}],"Structural transition":[{"start":55,"end":91,"type":"T"}],"Molecular function":[{"start":55,"end":91,"type":"F"}],"Disorder function":[{"start":55,"end":91,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00104","name":"Ligand-binding domain of nuclear hormone receptor","start":767,"end":943},{"id":"PF00105","name":"Double treble clef zinc finger, C4 type","start":602,"end":669}],"gene3D":[{"start":735,"end":984,"id":"1.10.565.10","name":"Retinoid X Receptor"},{"start":590,"end":682,"id":"3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A"}]},"uniref50":"UniRef50_P08235","sequence":"METKGYHSLPEGLDMERRWGQVSQAVERSSLGPTERTDENNYMEIVNVSCVSGAIPNNSTQGSSKEKQELLPCLQQDNNRPGILTSDIKTELESKELSATVAESMGLYMDSVRDADYSYEQQNQQGSMSPAKIYQNVEQLVKFYKGNGHRPSTLSCVNTPLRSFMSDSGSSVNGGVMRAVVKSPIMCHEKSPSVCSPLNMTSSVCSPAGINSVSSTTASFGSFPVHSPITQGTPLTCSPNVENRGSRSHSPAHASNVGSPLSSPLSSMKSSISSPPSHCSVKSPVSSPNNVTLRSSVSSPANINNSRCSVSSPSNTNNRSTLSSPAASTVGSICSPVNNAFSYTASGTSAGSSTLRDVVPSPDTQEKGAQEVPFPKTEEVESAISNGVTGQLNIVQYIKPEPDGAFSSSCLGGNSKINSDSSFSVPIKQESTKHSCSGTSFKGNPTVNPFPFMDGSYFSFMDDKDYYSLSGILGPPVPGFDGNCEGSGFPVGIKQEPDDGSYYPEASIPSSAIVGVNSGGQSFHYRIGAQGTISLSRSARDQSFQHLSSFPPVNTLVESWKSHGDLSSRRSDGYPVLEYIPENVSSSTLRSVSTGSSRPSKICLVCGDEASGCHYGVVTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRLQKCLQAGMNLGARKSKKLGKLKGIHEEQPQQQQPPPPPPPPQSPEEGTTYIAPAKEPSVNTALVPQLSTISRALTPSPVMVLENIEPEIVYAGYDSSKPDTAENLLSTLNRLAGKQMIQVVKWAKVLPGFKNLPLEDQITLIQYSWMCLSSFALSWRSYKHTNSQFLYFAPDLVFNEEKMHQSAMYELCQGMHQISLQFVRLQLTFEEYTIMKVLLLLSTIPKDGLKSQAAFEEMRTNYIKELRKMVTKCPNNSGQSWQRFYQLTKLLDSMHDLVSDLLEFCFYTFRESHALKVEFPAMLVEIISDQLPKVESGNAKPLYFHRK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P08235","disprot_id":"DP01561","ncbi_taxon_id":9606,"regions_counter":14,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":169,"region_id":"DP01561r002","released":"2023_06","ec_id":"ECO:0001249","reference_html":"Conformation of the mineralocorticoid receptor N-terminal domain: evidence for induced and stable structure. <i> Fischer K, Kelly SM, Watt K, Price NC, McEwan IJ. </i> Mol Endocrinol, 2010","statement":[{"text":"The tryptophan in MR-AF1a is essentially solvent exposed with a λmax of 351 nm, i.e. not significantly changed by urea-induced unfolding (Fig. 3A and Table 1).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"20685853","version":3,"ec_name":"fluorescence evidence used in manual assertion","date":"2023-05-05T13:50:46.824Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":169,"region_id":"DP01561r003","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Conformation of the mineralocorticoid receptor N-terminal domain: evidence for induced and stable structure. <i> Fischer K, Kelly SM, Watt K, Price NC, McEwan IJ. </i> Mol Endocrinol, 2010","statement":[{"text":"The spectrum in buffer shows a strong minimum at around 197 nm, which is indicative of nonordered structure (Fig. 4A).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"20685853","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-05-05T13:54:50.011Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":385,"region_id":"DP01561r004","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Conformation of the mineralocorticoid receptor N-terminal domain: evidence for induced and stable structure. <i> Fischer K, Kelly SM, Watt K, Price NC, McEwan IJ. </i> Mol Endocrinol, 2010","statement":[{"text":"The far-UV spectra for MR-MD showed a similar trend with a more helical conformation adopted in the presence of TFE (Fig. 4B and Table 2).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":247,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"20685853","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-05-05T13:58:14.567Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":385,"region_id":"DP01561r005","released":"2023_06","ec_id":"ECO:0007691","reference_html":"Conformation of the mineralocorticoid receptor N-terminal domain: evidence for induced and stable structure. <i> Fischer K, Kelly SM, Watt K, Price NC, McEwan IJ. </i> Mol Endocrinol, 2010","statement":[{"text":"Supplemental Fig. 1B shows that the MR-MD polypeptide is digested in a time-dependent manner, and this digestion is prevented in the presence of TMAO. This is consistent with induced folding of the MD and adoption of a more protease-resistant conformation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":247,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"20685853","version":3,"ec_name":"cleavage assay evidence used in manual assertion","date":"2023-05-05T13:54:06.364Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907"},{"start":1,"end":602,"reference_id":"20685853","reference_source":"pmid","reference_html":"Conformation of the mineralocorticoid receptor N-terminal domain: evidence for induced and stable structure. <i> Fischer K, Kelly SM, Watt K, Price NC, McEwan IJ. </i> Mol Endocrinol, 2010","date":"2023-05-05T14:06:27.758Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP01561r006","statement":[{"text":"Fluorescence and far-UV spectroscopy analysis of the full-length MR-NTD revealed some composite structural properties seen with the isolated domains, but generally, the fluorescence emission for the solvent exposed tryptophan was dominant, and the polypeptide showed a propensity to form helical secondary structure in a hydrophobic environment (Tables 1 and 2 and Supplemental Fig. 2, A and B).","type":"Results"}]},{"start":1,"end":602,"reference_id":"20685853","reference_source":"pmid","reference_html":"Conformation of the mineralocorticoid receptor N-terminal domain: evidence for induced and stable structure. <i> Fischer K, Kelly SM, Watt K, Price NC, McEwan IJ. </i> Mol Endocrinol, 2010","date":"2023-05-05T14:11:06.173Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP01561r007","statement":[{"text":"Supplemental Fig. 2, B. shows this peptide has a large negative ellipticity around 200 nm, typical of unstructured regions.","type":"Results"}]},{"start":1,"end":602,"reference_id":"20685853","reference_source":"pmid","reference_html":"Conformation of the mineralocorticoid receptor N-terminal domain: evidence for induced and stable structure. <i> Fischer K, Kelly SM, Watt K, Price NC, McEwan IJ. </i> Mol Endocrinol, 2010","date":"2023-05-05T14:18:17.606Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0017025","term_name":"TBP-class protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P20226","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01561r008","statement":[{"text":"By contrast, the TBP was found to preferentially interact with the MR-AF1b domain, and full-length NTD, in the absence of TMAO (Fig. 5B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a member of the class of TATA-binding proteins (TBP), including any of the TBP-related factors (TRFs).\" [GOC:jl, GOC:txnOH, http://www.mblab.gla.ac.uk/, PMID:16858867]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":169,"reference_id":"20685853","reference_source":"pmid","reference_html":"Conformation of the mineralocorticoid receptor N-terminal domain: evidence for induced and stable structure. <i> Fischer K, Kelly SM, Watt K, Price NC, McEwan IJ. </i> Mol Endocrinol, 2010","date":"2023-05-05T14:21:52.412Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0017025","term_name":"TBP-class protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P20226","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01561r009","statement":[{"text":"No selective interactions were indentified for the MR-AF1a domain for any of the proteins tested, although some modest binding of TBP was seen in some experiments (Fig. 5).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a member of the class of TATA-binding proteins (TBP), including any of the TBP-related factors (TRFs).\" [GOC:jl, GOC:txnOH, http://www.mblab.gla.ac.uk/, PMID:16858867]","term_is_obsolete":false,"term_not_annotate":false},{"start":450,"end":602,"reference_id":"20685853","reference_source":"pmid","reference_html":"Conformation of the mineralocorticoid receptor N-terminal domain: evidence for induced and stable structure. <i> Fischer K, Kelly SM, Watt K, Price NC, McEwan IJ. </i> Mol Endocrinol, 2010","date":"2023-05-05T14:26:02.110Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0017025","term_name":"TBP-class protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P20226","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01561r010","statement":[{"text":"By contrast, the TBP was found to preferentially interact with the MR-AF1b domain, and full-length NTD, in the absence of TMAO (Fig. 5B).","type":"Results"},{"text":"A similar analysis of the interaction of TBP with increasing amounts of GST alone or GST-MR-AF1b, but in the absence of TMAO, also resulted in saturable binding, and from the corresponding Eadie-Hofstee plot, a dissociation constant of 1.4 μm was calculated for this interaction (Fig. 7, A–C).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a member of the class of TATA-binding proteins (TBP), including any of the TBP-related factors (TRFs).\" [GOC:jl, GOC:txnOH, http://www.mblab.gla.ac.uk/, PMID:16858867]","term_is_obsolete":false,"term_not_annotate":false},{"start":247,"end":385,"reference_id":"20685853","reference_source":"pmid","reference_html":"Conformation of the mineralocorticoid receptor N-terminal domain: evidence for induced and stable structure. <i> Fischer K, Kelly SM, Watt K, Price NC, McEwan IJ. </i> Mol Endocrinol, 2010","date":"2023-05-05T14:36:22.461Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0035624","term_name":"receptor transactivation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005648","ec_ontology":"ECO","ec_name":"luciferase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IEP","region_id":"DP01561r011","statement":[{"text":"To confirm the importance of regions within the NTD for transactivation, a construct was made containing the NTD-DBD with a FLAG tag and transfected into COS-1 cells together with a luciferase reporter gene driven by two glucocorticoid response elements (GREs). ","type":"Results"},{"text":"Deletion of the MD reduced the transcriptional activity of the NTD by 35%, whereas deleting AF1a or AF1b region resulted in a loss of greater than 97% of the activity of the full NTD (Fig. 2B). Importantly, the AF1b domain alone linked to the DBD retained 26% the activity of the MR-NTD-DBD polypeptide (Fig. 1B).","type":"Results"}],"term_comment":"","term_def":"\"The process in which a receptor is activated by another receptor. Receptor transactivation can occur through different mechanisms and includes cross-talk between signaling pathways where one receptor activates a receptor for a different ligand, and also activation of subunits within a receptor oligomer.\" [GOC:al, GOC:bf, GOC:BHF, PMID:16870826, PMID:21063387]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":169,"reference_id":"20685853","reference_source":"pmid","reference_html":"Conformation of the mineralocorticoid receptor N-terminal domain: evidence for induced and stable structure. <i> Fischer K, Kelly SM, Watt K, Price NC, McEwan IJ. </i> Mol Endocrinol, 2010","date":"2023-05-05T14:37:05.732Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0035624","term_name":"receptor transactivation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005648","ec_ontology":"ECO","ec_name":"luciferase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IEP","region_id":"DP01561r012","statement":[{"text":"To confirm the importance of regions within the NTD for transactivation, a construct was made containing the NTD-DBD with a FLAG tag and transfected into COS-1 cells together with a luciferase reporter gene driven by two glucocorticoid response elements (GREs). ","type":"Results"},{"text":"Deletion of the MD reduced the transcriptional activity of the NTD by 35%, whereas deleting AF1a or AF1b region resulted in a loss of greater than 97% of the activity of the full NTD (Fig. 2B). Importantly, the AF1b domain alone linked to the DBD retained 26% the activity of the MR-NTD-DBD polypeptide (Fig. 1B).","type":"Results"}],"term_comment":"","term_def":"\"The process in which a receptor is activated by another receptor. Receptor transactivation can occur through different mechanisms and includes cross-talk between signaling pathways where one receptor activates a receptor for a different ligand, and also activation of subunits within a receptor oligomer.\" [GOC:al, GOC:bf, GOC:BHF, PMID:16870826, PMID:21063387]","term_is_obsolete":false,"term_not_annotate":false},{"start":450,"end":602,"reference_id":"20685853","reference_source":"pmid","reference_html":"Conformation of the mineralocorticoid receptor N-terminal domain: evidence for induced and stable structure. <i> Fischer K, Kelly SM, Watt K, Price NC, McEwan IJ. </i> Mol Endocrinol, 2010","date":"2023-05-05T14:37:21.741Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0035624","term_name":"receptor transactivation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005648","ec_ontology":"ECO","ec_name":"luciferase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IEP","region_id":"DP01561r013","statement":[{"text":"To confirm the importance of regions within the NTD for transactivation, a construct was made containing the NTD-DBD with a FLAG tag and transfected into COS-1 cells together with a luciferase reporter gene driven by two glucocorticoid response elements (GREs). ","type":"Results"},{"text":"Deletion of the MD reduced the transcriptional activity of the NTD by 35%, whereas deleting AF1a or AF1b region resulted in a loss of greater than 97% of the activity of the full NTD (Fig. 2B). Importantly, the AF1b domain alone linked to the DBD retained 26% the activity of the MR-NTD-DBD polypeptide (Fig. 1B).","type":"Results"}],"term_comment":"","term_def":"\"The process in which a receptor is activated by another receptor. Receptor transactivation can occur through different mechanisms and includes cross-talk between signaling pathways where one receptor activates a receptor for a different ligand, and also activation of subunits within a receptor oligomer.\" [GOC:al, GOC:bf, GOC:BHF, PMID:16870826, PMID:21063387]","term_is_obsolete":false,"term_not_annotate":false},{"start":465,"end":471,"reference_id":"20685853","reference_source":"pmid","reference_html":"Conformation of the mineralocorticoid receptor N-terminal domain: evidence for induced and stable structure. <i> Fischer K, Kelly SM, Watt K, Price NC, McEwan IJ. </i> Mol Endocrinol, 2010","date":"2023-05-05T14:40:32.811Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0035624","term_name":"receptor transactivation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ser468del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ser469del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Leu470del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP01561r014","statement":[{"text":"Mutating two serine residues and a leucine at positions 468, 469, and 470 (M5) (Fig. 8A) was predicted to disrupt local β-structure and increase α-helix. Mutating these residues or the leucine alone at 469 (M8) (Fig. 8A) impaired transactivation activity in the context of MR-NTD-DBD (Fig. 8B).","type":"Results"}],"term_comment":"","term_def":"\"The process in which a receptor is activated by another receptor. Receptor transactivation can occur through different mechanisms and includes cross-talk between signaling pathways where one receptor activates a receptor for a different ligand, and also activation of subunits within a receptor oligomer.\" [GOC:al, GOC:bf, GOC:BHF, PMID:16870826, PMID:21063387]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_P08235","date":"2018-07-27T10:56:49.000Z","acc":"P08235","name":"Mineralocorticoid receptor","length":984,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI000012EDE5","genes":[{"name":{"value":"NR3C2"},"synonyms":[{"value":"MCR"},{"value":"MLR"}]}],"alphafold_very_low_content":0.6310975609756098,"disorder_content":0.6117886178861789,"disprot_consensus":{"full":[{"start":1,"end":602,"type":"D"}],"Structural state":[{"start":1,"end":602,"type":"D"}],"Molecular function":[{"start":1,"end":602,"type":"F"}],"Biological process":[{"start":1,"end":169,"type":"F"},{"start":247,"end":385,"type":"F"},{"start":450,"end":602,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00035","name":"Double-stranded RNA binding motif","start":411,"end":464},{"id":"PF00035","name":"Double-stranded RNA binding motif","start":527,"end":588},{"id":"PF07528","name":"DZF N-terminal domain","start":11,"end":221},{"id":"PF20965","name":"DZF C-terminal domain","start":225,"end":356}],"gene3D":[{"start":348,"end":381,"id":"3.30.460.10","name":"Beta Polymerase, domain 2"},{"start":384,"end":479,"id":"3.30.160.20","name":"3.30.160.20"},{"start":520,"end":594,"id":"3.30.160.20","name":"3.30.160.20"}]},"uniref50":"UniRef50_Q12906","sequence":"MRPMRIFVNDDRHVMAKHSSVYPTQEELEAVQNMVSHTERALKAVSDWIDEQEKGNSELSEAENMDTPPDDESKEGAGEQKAEHMTRTLRGVMRVGLVAKGLLLKGDLDLELVLLCKEKPTTALLDKVADNLAIQLTTVTEDKYEILQSVDDAAIVIKNTKEPPLSLTIHLTSPVVREEMEKVLAGETLSVNDPPDVLDRQKCLAALASLRHAKWFQARANGLKSCVIVIRVLRDLCTRVPTWGPLRGWPLELLCEKSIGTANRPMGAGEALRRVLECLASGIVMPDGSGIYDPCEKEATDAIGHLDRQQREDITQSAQHALRLAAFGQLHKVLGMDPLPSKMPKKPKNENPVDYTVQIPPSTTYAITPMKRPMEEDGEEKSPSKKKKKIQKKEEKADPPQAMNALMRLNQLKPGLQYKLISQTGPVHAPIFTMSVEVDGSNFEASGPSKKTAKLHVAVKVLQDMGLPTGAEGRDSSKGEDSAEESDGKPAIVAPPPVVEAVSNPSSVFPSDATTEQGPILTKHGKNPVMELNEKRRGLKYELISETGGSHDKRFVMEVEVDGQKFQGAGSNKKVAKAYAALAALEKLFPDTPLALEANKKKRTPVPVRGGPKFAAKPHNPGFGMGGPMHNEVPPPPNIRGRGRGGNIRGRGRGRGFGGANHGGGYMNAGAGYGSYGYSSNSATAGYSQFYSNGGHSGNAGGGGSGGGGGSSSYSSYYQGDSYNSPVPPKHAGKKPLHGGQQKASYSSGYQSHQGQQQPYNQSQYSSYGTPQGKQKGYGHGQGSYSSYSNSYNSPGGGGGSDYSYDSKFNYSGSGGRSGGNSYGSSGSSSYNTGSHGGYGTGSGGSSSYQGKQGGYSSQSNYSSPGSSQSYSGPASSYQSSQGGYSRNTEHSMNYQYR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q12906-7","disprot_id":"DP01562","ncbi_taxon_id":10090,"regions_counter":3,"creator":"nfoutel","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":86,"region_id":"DP01562r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"NF45 dimerizes with NF90, Zfr and SPNR via a conserved domain that has a nucleotidyltransferase fold. <i> Wolkowicz UM, Cook AG. </i> Nucleic Acids Res, 2012","statement":[{"text":"Residues in the N- and C-termini and several loops (residues 1–5, 55–86, 341–353 and 375–380 of NF90 and 362–390 of\nNF45) could not be modeled due to poor electron density in these regions that made a clear interpretation of the map difficult.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":55,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"22833610","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":353,"region_id":"DP01562r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"NF45 dimerizes with NF90, Zfr and SPNR via a conserved domain that has a nucleotidyltransferase fold. <i> Wolkowicz UM, Cook AG. </i> Nucleic Acids Res, 2012","statement":[{"text":"Residues in the N- and C-termini and several loops (residues 1–5, 55–86, 341–353 and 375–380 of NF90 and 362–390 of\nNF45) could not be modeled due to poor electron density in these regions that made a clear interpretation of the map difficult.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":341,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"22833610","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":518,"region_id":"DP01562r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Nuclear factor 90 uses an ADAR2-like binding mode to recognize specific bases in dsRNA. <i> Jayachandran U, Grey H, Cook AG. </i> Nucleic Acids Res, 2016","statement":[{"text":"The linker region connecting the two domains (residues 468–518) is not visible, consistent with the prediction that this region is natively disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":468,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"26712564","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9Z1X4","date":"2018-07-27T11:20:35.000Z","acc":"Q9Z1X4","name":"Interleukin enhancer-binding factor 3","length":898,"organism":"Mus musculus","dataset":[],"UniParc":"UPI000002977D","genes":[{"name":{"value":"Ilf3"}}],"alphafold_very_low_content":0.44766146993318484,"disorder_content":0.10690423162583519,"disprot_consensus":{"full":[{"start":55,"end":86,"type":"D"},{"start":341,"end":353,"type":"D"},{"start":468,"end":518,"type":"D"}],"Structural state":[{"start":55,"end":86,"type":"D"},{"start":341,"end":353,"type":"D"},{"start":468,"end":518,"type":"D"}]}},{"features":{"pfam":[{"id":"PF07528","name":"DZF N-terminal domain","start":22,"end":216},{"id":"PF20965","name":"DZF C-terminal domain","start":220,"end":351}],"gene3D":[{"start":66,"end":217,"id":"3.30.460.10","name":"Beta Polymerase, domain 2"},{"start":31,"end":358,"id":"1.10.1410.40","name":"1.10.1410.40"}]},"uniref50":"UniRef50_Q12905","sequence":"MRGDRGRGRGGRFGSRGGPGGGFRPFVPHIPFDFYLCEMAFPRVKPAPDETSFSEALLKRNQDLAPNSAEQASILSLVTKINNVIDNLIVAPGTFEVQIEEVRQVGSYKKGTMTTGHNVADLVVILKILPTLEAVAALGNKVVESLRAQDPSEVLTMLTNETGFEISSSDATVKILITTVPPNLRKLDPELHLDIKVLQSALAAIRHARWFEENASQSTVKVLIRLLKDLRIRFPGFEPLTPWILDLLGHYAVMNNPTRQPLALNVAYRRCLQILAAGLFLPGSVGITDPCESGNFRVHTVMTLEQQDMVCYTAQTLVRILSHGGFRKILGQEGDASYLASEISTWDGVIVTPSEKAYEKPPEKKEGEEEEENTEEPPQGEEEESMETQE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q12905","disprot_id":"DP01563","ncbi_taxon_id":10090,"regions_counter":2,"creator":"nfoutel","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":390,"region_id":"DP01563r002","released":"2023_06","ec_id":"ECO:0006220","reference_html":"NF45 dimerizes with NF90, Zfr and SPNR via a conserved domain that has a nucleotidyltransferase fold. <i> Wolkowicz UM, Cook AG. </i> Nucleic Acids Res, 2012","statement":[{"text":"Residues in the N- and C-termini and several loops (residues 1–5, 55–86, 341–353 and 375–380 of NF90 and 362–390 of NF45) could not be modelled due to poor electron density in these regions that made a clear interpretation of the map difficult.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":362,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"22833610","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-05-16T15:40:50.924Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:9084"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:62551"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEMBL","id":"8117"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Z1X4"}],"cross_refs":[{"db":"PDB","id":"4AT7"}]}],"released":"2018_11","uniref100":"UniRef100_Q12905","date":"2018-07-27T12:02:25.000Z","acc":"Q9CXY6","name":"Interleukin enhancer-binding factor 2","length":390,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000027483","genes":[{"name":{"value":"Ilf2"},"synonyms":[{"value":"Nf45"}]}],"alphafold_very_low_content":0.11282051282051282,"disorder_content":0.07435897435897436,"disprot_consensus":{"full":[{"start":362,"end":390,"type":"D"}],"Structural state":[{"start":362,"end":390,"type":"D"}]}},{"features":{"pfam":[{"id":"PF07528","name":"DZF N-terminal domain","start":22,"end":216},{"id":"PF20965","name":"DZF C-terminal domain","start":220,"end":351}],"gene3D":[{"start":31,"end":358,"id":"1.10.1410.40","name":"1.10.1410.40"},{"start":66,"end":217,"id":"3.30.460.10","name":"Beta Polymerase, domain 2"}]},"uniref50":"UniRef50_Q12905","sequence":"MRGDRGRGRGGRFGSRGGPGGGFRPFVPHIPFDFYLCEMAFPRVKPAPDETSFSEALLKRNQDLAPNSAEQASILSLVTKINNVIDNLIVAPGTFEVQIEEVRQVGSYKKGTMTTGHNVADLVVILKILPTLEAVAALGNKVVESLRAQDPSEVLTMLTNETGFEISSSDATVKILITTVPPNLRKLDPELHLDIKVLQSALAAIRHARWFEENASQSTVKVLIRLLKDLRIRFPGFEPLTPWILDLLGHYAVMNNPTRQPLALNVAYRRCLQILAAGLFLPGSVGITDPCESGNFRVHTVMTLEQQDMVCYTAQTLVRILSHGGFRKILGQEGDASYLASEISTWDGVIVTPSEKAYEKPPEKKEGEEEEENTEEPPQGEEEESMETQE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q12905","disprot_id":"DP01564","ncbi_taxon_id":9606,"regions_counter":1,"creator":"nfoutel","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":390,"region_id":"DP01564r001","released":"2023_06","ec_id":"ECO:0006220","reference_html":"NF45 dimerizes with NF90, Zfr and SPNR via a conserved domain that has a nucleotidyltransferase fold. <i> Wolkowicz UM, Cook AG. </i> Nucleic Acids Res, 2012","statement":[{"text":"Structural studies were carried out with mouse NF90 and NF45. Mouse and human NF90 show 95% sequence identity while mouse and human NF45 are identical at the protein level.","type":"Results"},{"text":"Residues in the N- and C-termini and several loops (residues 1–5, 55–86, 341–353 and 375–380 of NF90 and 362–390 of NF45) could not be modelled due to poor electron density in these regions that made a clear interpretation of the map difficult.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":362,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"22833610","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-05-16T15:37:19.368Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"4AT7"}],"curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Z1X4"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:8117"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:62551"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:9084"}]}],"released":"2018_11","uniref100":"UniRef100_Q12905","date":"2018-07-27T12:24:48.000Z","acc":"Q12905","name":"Interleukin enhancer-binding factor 2","length":390,"organism":"Homo sapiens","dataset":["NDDs-related proteins","RNA-binding proteins"],"UniParc":"UPI00000735E4","genes":[{"name":{"value":"ILF2"},"synonyms":[{"value":"NF45"}],"orfNames":[{"value":"PRO3063"}]}],"alphafold_very_low_content":0.11282051282051282,"disorder_content":0.07435897435897436,"disprot_consensus":{"full":[{"start":362,"end":390,"type":"D"}],"Structural state":[{"start":362,"end":390,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00104","name":"Ligand-binding domain of nuclear hormone receptor","start":239,"end":441},{"id":"PF00105","name":"Double treble clef zinc finger, C4 type","start":112,"end":180}],"gene3D":[{"start":201,"end":459,"id":"1.10.565.10","name":"Retinoid X Receptor"},{"start":102,"end":193,"id":"3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A"}]},"uniref50":"UniRef50_B0X9K6","sequence":"MDPSDRGFDAALVGHMGPLSPQDMKPDLKPDISLLNGSVGPFSPGNNCGPASPGAFNQQVAAALQQQQQNVNSLNSQQSGGGGGGGGGTPTTPTNMSQQYPPNHPLSGSKHLCSICGDRASGKHYGVYSCEGCKGFFKRTVRKDLSYACREDKNCTIDKRQRNRCQYCRYQKCLACGMKREAVQEERQRSSKFSIKSEEINSTSSVRDVTIERIHEAEQLSEQKSGDNAIPYLRVGSNSMIPPEYKGAVSHLCQMVNKQIYQLIDFARRVPHFINLPRDDQVMLLRCGWNEMLIAAVAWRSMEYIETERSSDGSRITVRQPQLMCLGPNFTLHRNSAQQAGVDTLFDRILCELGIKMKRLDVTRAELGVLKAIILFNPDIRGLKCQKEIDGMREKIYACLDEHCKQQHPSEDGRFAQLLLRLPALRSISLKCLDHLNFIRLLSDKHLDSFIVEMLDMPI","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Nematocera","Culicoidea","Culicidae","Culicinae","Aedini","Aedes","Stegomyia"],"uniref90":"UniRef90_B0X9K6","disprot_id":"DP01565","ncbi_taxon_id":7159,"regions_counter":4,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":112,"region_id":"DP01565r001","released":"2022_03","ec_id":"ECO:0007689","reference_html":"Homodimerization propensity of the intrinsically disordered N-terminal domain of Ultraspiracle from Aedes aegypti. <i> Pieprzyk J, Zbela A, Jakób M, Ożyhar A, Orłowski M. </i> Biochim Biophys Acta, 2014","statement":[{"text":"Due to their unusual amino acid composition, IDPs bind less SDS molecules and move more slowly in gel than globular proteins. aaUsp-NTD (residues 1-112) exhibits such properties. The apparent molecular mass of aaUsp-NTD calculated on the basis of SDS-PAGE electrophoretical mobility was 14 kDa, whereas the theoretical molecular mass was 12.718 kDa.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":1,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"24704038","version":2,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":112,"region_id":"DP01565r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Homodimerization propensity of the intrinsically disordered N-terminal domain of Ultraspiracle from Aedes aegypti. <i> Pieprzyk J, Zbela A, Jakób M, Ożyhar A, Orłowski M. </i> Biochim Biophys Acta, 2014","statement":[{"text":"The spectrum exhibits features of spectra typical of IDPs, because it has a deep minimum at 200 nm, which is characteristic for a random coil and it has a slight negative band at 222 nm, which is typical for ordered secondary structures. CD spectra in the presence of varying concentrations of GdmCl also imply that aaUsp-NTD is a highly unfolded protein with a residual secondary structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":1,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"24704038","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":112,"region_id":"DP01565r003","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Homodimerization propensity of the intrinsically disordered N-terminal domain of Ultraspiracle from Aedes aegypti. <i> Pieprzyk J, Zbela A, Jakób M, Ożyhar A, Orłowski M. </i> Biochim Biophys Acta, 2014","statement":[{"text":"aaUsp-NTD's theoretical molecular mass is 12.718 kDa. The Ve of purified aaUsp-NTD corresponds to a pro-\ntein with an apparent molecular mass equal to 24.7 kDa and RS equal to 22.7 Å (1 Å = 0.1 nm). This indicates \nthat aaUsp-NTD may have an expanded conformation such as IDPs do.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":1,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"24704038","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":112,"region_id":"DP01565r004","released":"2022_03","ec_id":"ECO:0006275","reference_html":"Homodimerization propensity of the intrinsically disordered N-terminal domain of Ultraspiracle from Aedes aegypti. <i> Pieprzyk J, Zbela A, Jakób M, Ożyhar A, Orłowski M. </i> Biochim Biophys Acta, 2014","statement":[{"text":"Analysis of the data obtained suggests that aaUsp-NTD eluted as a monomer (eluted as a distinct, symmetric peak corresponding to a monomer and the Ve value was independent of the sample concentration). Additionally, the frictional ratio was fitted to 1.8, indicating that aaUsp-NTD is an asymmetric protein with an RS of 28.1 Å.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":1,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"24704038","version":2,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9GSG7","date":"2018-07-27T13:24:44.000Z","acc":"Q9GSG7","name":"AAEL000395-PB","length":459,"organism":"Aedes aegypti","dataset":[],"UniParc":"UPI0000077C37","genes":[],"alphafold_very_low_content":0.2549019607843137,"disorder_content":0.2440087145969499,"disprot_consensus":{"full":[{"start":1,"end":112,"type":"D"}],"Structural state":[{"start":1,"end":112,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00104","name":"Ligand-binding domain of nuclear hormone receptor","start":185,"end":388},{"id":"PF00105","name":"Double treble clef zinc finger, C4 type","start":60,"end":128}],"gene3D":[{"start":54,"end":155,"id":"3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A"},{"start":156,"end":414,"id":"1.10.565.10","name":"Retinoid X Receptor"}]},"uniref50":"UniRef50_P49700","sequence":"MMEPSRDSGLNLEGGFMSPMSPPEMKPDTAMLDGLRDDSTPPPAFKNYPPNHPLSGSKHLCSICGDRASGKHYGVYSCEGCKGFFKRTVRKDLTYACREERNCIIDKRQRNRCQYCRYQKCLACGMKREAVQEERQRGARGTEDAHPSSSVQVQELSIERLLEMESLVADPSEEFQFLRVGPDSNVPPKFRAPVSSLCQIGNKQIAALVVWARDIPHFSQLELEDQILLIKGSWNELLLFAIAWRSMEYLTEERDGVDGTGNRTTSPPQLMCLMPGMTLHRNSALQAGVGQIFDRVLSELSLKMRSLRVDQAEYVALKAIILLNPDVKGLKNRQEVEVLREKMFLCLDEYCRRSRGSEEGRFAALLLRLPALRSISLKSFEHLFFFHLVADTSIAGYIRDALRNHAPPIDTNMM","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Lepidoptera","Glossata","Ditrysia","Noctuoidea","Noctuidae","Heliothinae","Helicoverpa"],"uniref90":"UniRef90_A9UEF7","disprot_id":"DP01567","ncbi_taxon_id":29058,"regions_counter":1,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":58,"region_id":"DP01567r001","released":"2022_03","ec_id":"ECO:0006236","reference_html":"Intrinsically disordered N-terminal domain of the Helicoverpa armigera Ultraspiracle stabilizes the dimeric form via a scorpion-like structure. <i> Wycisk K, Tarczewska A, Kaus-Drobek M, Dadlez M, Hołubowicz R, Pietras Z, Dziembowski A, Taube M, Kozak M, Orłowski M, Ożyhar A. </i> J Steroid Biochem Mol Biol, 2018","statement":[{"text":"The results showed that the highest rate of exchange, approximately 80%, was observed for the peptides covering the NTD (residues 1-58), which is consistent with the results of the bioinformatic analyses, indicating that this region is disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":1,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"29944921","version":2,"ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_B9UCQ5","date":"2018-07-27T13:53:12.000Z","acc":"B9UCQ5","name":"Ultraspiracle isoform 1","length":414,"organism":"Helicoverpa armigera","dataset":[],"UniParc":"UPI00019203A9","genes":[],"alphafold_very_low_content":0.1932367149758454,"disorder_content":0.14009661835748793,"disprot_consensus":{"full":[{"start":1,"end":58,"type":"D"}],"Structural state":[{"start":1,"end":58,"type":"D"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MLTTSGQQQSKQKLSTLPSHILLQQQLAASAGPSSSVSLSPSSSAALTLHVASANGGARETTSAAAVKDKLRPTPTAIKIEPMPDVISVGTVAGGSSVATVVAPAATTTSNKPNSTAAPSTSAAAANGHLVLVPNKRPRLDVTEDWMSTPSPGSVPSSAPPLSPSPGSQNHSYNMSNGYASPMSAGSYDPYSPTGKTGRDDLSPSSSLNGYSANESCDAKKSKKGPAPRVQEELCLVCGDRASGYHYNALTCEGCKGFFRRSVTKSAVYCCKFGRACEMDMYMRRKCQECRLKKCLAVGMRPECVVPENQCAMKRREKKAQKEKDKMTTSPSSQHGGNGSLASGGGQDFVKKEILDLMTCEPPQHATIPLLPDEILAKCQARNIPSLTYNQLAVIYKLIWYQDGYEQPSEEDLRRIMSQPDENESQTDVSFRHITEITILTVQLIVEFAKGLPAFTKIPQEDQITLLKACSSEVMMLRMARRYDHSSDSIFFANNRSYTRDSYKMAGMADNIEDLLHFCRQMFSMKVDNVEYALLTAIVIFSDRPGLEKAQLVEAIQSYYIDTLRIYILNRHCGDSMSLVFYAKLLSILTELRTLGNQNAEMCFSLKLKNRKLPKFLEEIWDVHAIPPSVQSHLQITQEENERLERAERMRASVGGAITAGIDCDSASTSAAAAAAQHQPQPQPQPQPSSLTQNDSQHQTQPQLQPQLPPQLQGQLQPQLQPQLQTQLQPQIQPQPQLLPVSAPVPASVTAPGSLSAVSTSSEYMGGSAAIGPITPATTSSITAAVTASSTTSAVPMGNGVGVGVGVGGNVSMYANAQTAMALMGVALHSHQEQLIGGVAVKSEHSTTA","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"","disprot_id":"DP01569","ncbi_taxon_id":7227,"regions_counter":3,"creator":"nmurvai","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":226,"region_id":"DP01569r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The glycation-associated crosslinking of lens proteins by ascorbic acid is not mediated by oxygen free radicals. <i> Prabhakaram M, Ortwerth BJ. </i> Exp Eye Res, 1991","statement":[{"text":"EcRA-NTD spectra is reminiscent of spectra typical of proteins containing numerous disordered regions, because it displays a deep minimum around 200 nm. However, EcRA-NTD is not fully random coil-like, as it has a content of the residual secondary structure, which can be destroyed by GdmCl denaturation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":2,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"1915682","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":226,"region_id":"DP01569r002","released":"2022_03","ec_id":"ECO:0007680","reference_html":"The glycation-associated crosslinking of lens proteins by ascorbic acid is not mediated by oxygen free radicals. <i> Prabhakaram M, Ortwerth BJ. </i> Exp Eye Res, 1991","statement":[{"text":"Stokes radius determined on the basis of gel filtration was substantially bigger, 36.6 +/-1.5 A for EcRA-NTD than the theoretical Stokes radius.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":2,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"1915682","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":226,"region_id":"DP01569r003","released":"2022_03","ec_id":"ECO:0007691","reference_html":"The glycation-associated crosslinking of lens proteins by ascorbic acid is not mediated by oxygen free radicals. <i> Prabhakaram M, Ortwerth BJ. </i> Exp Eye Res, 1991","statement":[{"text":"The protein was extensively degraded, however the peptide bonds were not accessible at random. There are nineteen potential trypsin cleavage sites within the EcRA-NTD sequence, yet only nine main proteolysis products were revealed through electrophoretic gels.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nmurvai","start":2,"term_ontology":"IDPO","curator_name":"Nikoletta Murvai","reference_id":"1915682","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"","date":"2018-07-27T14:44:45.000Z","acc":"P34021-2","name":"Isoform ECR-A of Ecdysone receptor","length":849,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI0000007685","genes":[{"name":{"value":"EcR"},"synonyms":[{"value":"NR1H1"}],"orfNames":[{"value":"CG1765"}]}],"disorder_content":0.26501766784452296,"disprot_consensus":{"full":[{"start":2,"end":226,"type":"D"}],"Structural state":[{"start":2,"end":226,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00017","name":"SH2 domain","start":151,"end":233},{"id":"PF00018","name":"SH3 domain","start":90,"end":137},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":271,"end":518}],"gene3D":[{"start":139,"end":261,"id":"3.30.505.10","name":"SH2 domain"},{"start":88,"end":113,"id":"2.30.30.40","name":"SH3 Domains"},{"start":345,"end":532,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"},{"start":262,"end":344,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":114,"end":138,"id":"2.30.30.40","name":"SH3 Domains"}]},"uniref50":"UniRef50_P12931","sequence":"MGSNKSKPKDASQRRRSLEPAENVHGAGGGAFPASQTPSKPASADGHRGPSAAFAPAAAEPKLFGGFNSSDTVTSPQRAGPLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGETGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P12931","disprot_id":"DP01570","ncbi_taxon_id":9606,"regions_counter":5,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":84,"region_id":"DP01570r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural characterization of the natively unfolded N-terminal domain of human c-Src kinase: insights into the role of phosphorylation of the unique domain. <i> Pérez Y, Gairí M, Pons M, Bernadó P. </i> J Mol Biol, 2009","statement":[{"text":"The low chemical shift dispersion in the HSQC spectrum is consistent with an unfolded domain. The measured chemical shifts of HN, NH, Cα, Cβ, and C′ have been compared with random-coil values corrected for local sequence effects. The observed deviations are small, as expected for an unfolded protein. N–HN RDCs measured for USrc are predominantly negative as for unfolded proteins.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":1,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19520085","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":84,"term_name":"phosphorylation display site","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural characterization of the natively unfolded N-terminal domain of human c-Src kinase: insights into the role of phosphorylation of the unique domain. <i> Pérez Y, Gairí M, Pons M, Bernadó P. </i> J Mol Biol, 2009","statement":[{"text":"The phosphorylation of c-SRC Ser17 by PKA (cAMP-dependent protein kinase) is a well-characterized process.","type":"Introduction"}],"term_id":"IDPO:0000045","curator_id":"rpancsa","start":1,"term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"19520085","version":2,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01570r004","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_P12931","date":"2018-07-27T15:14:39.000Z","acc":"P12931","name":"Proto-oncogene tyrosine-protein kinase Src","length":536,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI0000135F28","genes":[{"name":{"value":"SRC","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11283","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11283"}}]},"synonyms":[{"value":"SRC1"}]}],"alphafold_very_low_content":0.15485074626865672,"disorder_content":0.15671641791044777,"disprot_consensus":{"full":[{"start":1,"end":84,"type":"D"}],"Structural state":[{"start":1,"end":84,"type":"D"}],"Disorder function":[{"start":1,"end":84,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00009","name":"Elongation factor Tu GTP binding domain","start":11,"end":204},{"id":"PF03143","name":"Elongation factor Tu C-terminal domain","start":301,"end":395},{"id":"PF03144","name":"Elongation factor Tu domain 2","start":228,"end":296}],"gene3D":[{"start":209,"end":337,"id":"2.40.30.10","name":"Translation factors"},{"start":341,"end":396,"id":"2.40.30.10","name":"Translation factors"},{"start":1,"end":206,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_Q88QP8","sequence":"MAKEKFDRSLPHVNVGTIGHVDHGKTTLTAALTRVCSEVFGSAIVEFDKIDSAPEEKARGITINTAHVEYNSTIRHYAHVDCPGHADYVKNMITGAAQMDGAILVCSAADGPMPQTREHILLSRQVGVPYIVVFLNKADLVDDAELLELVEMEVRDLLSTYDFPGDDTPIIIGSARMALEGKDDNEMGTTAVKKLVETLDSYIPEPVRAIDQPFLMPIEDVFSISGRGTVVTGRIERGIVRVQDPLEIVGLRDTTTTTCTGVEMFRKLLDEGRAGENCGVLLRGTKRDDVERGQVLVKPGSVKPHTKFTAEVYVLSKEEGGRHTPFFKGYRPQFYFRTTDVTGNCELPEGVEMVMPGDNIQMTVTLIKTIAMEDGLRFAIREGGRTVGAGVVAKIIE","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Pseudomonadales","Pseudomonadaceae","Pseudomonas"],"uniref90":"UniRef90_Q88QP8","disprot_id":"DP01571","ncbi_taxon_id":160488,"regions_counter":1,"creator":"nfoutel","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":62,"region_id":"DP01571r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Human oxygen sensing may have origins in prokaryotic elongation factor Tu prolyl-hydroxylation. <i> Scotti JS, Leung IK, Ge W, Bentley MA, Paps J, Kramer HB, Lee J, Aik W, Choi H, Paulsen SM, Bowman LA, Loik ND, Horita S, Ho CH, Kershaw NJ, Tang CM, Claridge TD, Preston GM, McDonough MA, Schofield CJ. </i> Proc Natl Acad Sci U S A, 2014","statement":[{"text":"The switch I loop of EF-Tuputida (residues 40–62) is disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":40,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"25197067","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q88QP8","date":"2018-07-27T15:59:34.000Z","acc":"Q88QP8","name":"Elongation factor Tu-A","length":397,"organism":"Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)","dataset":[],"UniParc":"UPI000000EB26","genes":[{"name":{"value":"tufA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00118","url":"https://hamap.expasy.org/unirule/MF_00118"}}]},"synonyms":[{"value":"tuf-1"}],"olnNames":[{"value":"PP_0440"}]}],"alphafold_very_low_content":0.0025188916876574307,"disorder_content":0.05793450881612091,"disprot_consensus":{"full":[{"start":40,"end":62,"type":"D"}],"Structural state":[{"start":40,"end":62,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00556","name":"Antenna complex alpha/beta subunit","start":14,"end":49}],"gene3D":[{"start":2,"end":49,"id":"1.20.5.250","name":"1.20.5.250"}]},"uniref50":"UniRef50_P0C0Y1","sequence":"MADKSDLGYTGLTDEQAQELHSVYMSGLWPFSAVAIVAHLAVYIWRPWF","taxonomy":["Bacteria","Proteobacteria","Alphaproteobacteria","Rhodobacterales","Rhodobacteraceae","Luteovulum"],"uniref90":"UniRef90_P0C0Y1","disprot_id":"DP01572","ncbi_taxon_id":1063,"regions_counter":1,"creator":"nfoutel","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":11,"region_id":"DP01572r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of the Rhodobacter sphaeroides light-harvesting 1 beta subunit in detergent micelles. <i> Sorgen PL, Cahill SM, Krueger-Koplin RD, Krueger-Koplin ST, Schenck CC, Girvin ME. </i> Biochemistry, 2002","statement":[{"text":"Is possible that the N-terminus (A1-L11) becomes structured in the presence of the LH1 R subunit and RC components (...). In addition, the lack of charged amino acids (L6-L11) suggests the N-terminus should be buried, and this may also occur in the presence of the LH1 R subunit and the RC.\nThe long T1 and T2 values for the N-terminus are typical of disordered polypeptides.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":1,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"11772000","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P0C0Y1","date":"2018-07-27T16:44:29.000Z","acc":"P0C0Y1","name":"Light-harvesting protein B-875 beta chain","length":49,"organism":"Rhodobacter sphaeroides","dataset":[],"UniParc":"UPI0000ED9211","genes":[{"name":{"value":"pufB"}}],"alphafold_very_low_content":0.02040816326530612,"disorder_content":0.22448979591836735,"disprot_consensus":{"full":[{"start":1,"end":11,"type":"D"}],"Structural state":[{"start":1,"end":11,"type":"D"}]}},{"features":{"pfam":[{"id":"PF07422","name":"Sexual stage antigen s48/45 domain","start":30,"end":140},{"id":"PF07422","name":"Sexual stage antigen s48/45 domain","start":176,"end":287}],"gene3D":[{"start":176,"end":311,"id":"2.60.40.2860","name":"2.60.40.2860"},{"start":99,"end":175,"id":"2.60.40.2860","name":"2.60.40.2860"},{"start":23,"end":98,"id":"2.60.40.2860","name":"2.60.40.2860"}]},"uniref50":"UniRef50_C6KSX0","sequence":"MIKLSKKYCLGISFVLYILLSVCEGHKNLTCDFNDVYKLEFHPNQQTSVTKLCNLTPNVLEKVTIKCGSDKLNYNLYPPTCFEEVYASRNMMHLKKIKEFVIGSSMFMRRSLTPNKINEVSFRIPPNMMPEKPIYCFCENKKTITINGSNGNPSSKKDIINRGIVEIIIPSLNEKVKGCDFTTSESTIFSKGYSINEISNKSSNNQQDIVCTVKAHANDLIGFKCPSNYSVEPHDCFVSAFNLSGKNENLENKLKLTNIIMDHYNNTFYSRLPSLISDNWKFFCVCSKDNEKKLVFTVEASISSSNTKLASRDNTYQDYISNSSFLTLSSYCAFITFIITSFLSFIL","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"uniref90":"UniRef90_C6KSX0","disprot_id":"DP01574","ncbi_taxon_id":36329,"regions_counter":2,"creator":"stama","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":116,"region_id":"DP01574r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural and biochemical characterization of Plasmodium falciparum 12 (Pf12) reveals a unique interdomain organization and the potential for an antiparallel arrangement with Pf41. <i> Tonkin ML, Arredondo SA, Loveless BC, Serpa JJ, Makepeace KA, Sundar N, Petrotchenko EV, Miller LH, Grigg ME, Boulanger MJ. </i> J Biol Chem, 2013","statement":[{"text":"Four regions of disorder are present in the Pf12short structure, all localized to surface loops projecting away from the core domain (dotted lines in Fig. 3A and 4A). In D1, a 33-residue region between Glu-83 and Ile-117 connecting β4 and β6 could not be modeled","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ahatos","start":84,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2YMO"}],"reference_id":"23511632","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":157,"region_id":"DP01574r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural and biochemical characterization of Plasmodium falciparum 12 (Pf12) reveals a unique interdomain organization and the potential for an antiparallel arrangement with Pf41. <i> Tonkin ML, Arredondo SA, Loveless BC, Serpa JJ, Makepeace KA, Sundar N, Petrotchenko EV, Miller LH, Grigg ME, Boulanger MJ. </i> J Biol Chem, 2013","statement":[{"text":"a 15-residue loop between Lys-142 (β7) and Asp-158 (β8) was disordered","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ahatos","start":143,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2YMO"}],"reference_id":"23511632","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_C6KSX0","date":"2018-07-29T10:37:06.000Z","acc":"C6KSX0","name":"Merozoite surface protein P12","length":347,"organism":"Plasmodium falciparum (isolate 3D7)","dataset":[],"UniParc":"UPI0000085D8E","genes":[{"name":{"value":"PF12"},"orfNames":[{"value":"PFF0615c"}]}],"alphafold_very_low_content":0.07780979827089338,"disorder_content":0.138328530259366,"disprot_consensus":{"full":[{"start":84,"end":116,"type":"D"},{"start":143,"end":157,"type":"D"}],"Structural state":[{"start":84,"end":116,"type":"D"},{"start":143,"end":157,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00178","name":"Ets-domain","start":5,"end":86}],"gene3D":[{"start":2,"end":100,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}]},"uniref50":"UniRef50_A4GTP4","sequence":"MDPSVTLWQFLLQLLREQGNGHIISWTSRDGGEFKLVDAEEVARLWGLRKNKTNMNYDKLSRALRYYYDKNIIRKVSGQKFVYKFVSYPEVAGCSTEDCPPQPEVSVTSAIAMAPATVHAGPGDTATGKPGTPKGAGMTGQGGLARSSRNEYMRSGLYSTFTIQSLQPQPQPPIPPRPASVLPNTTPAGVPAPASGSRSTSPNPLEACLEAEEAGLPLQVILTPPEAPNQKSEELSLDPSFGHPQPPEVKVEGPKEELEAARAGGFSSEAVKAEPEVSASEGLLARLPAILTENTAQVCGLSTSTTEITQPQKGRKPRDLELPLSPSLLGGQGPERTPGSGTSSGLQAPGPALTPSLLPTHTLTPVLLTPSSLPPSIHFWSTLSPIAPRSPAKLSFQFPSSGSAQVHIPSISVDGLSTPVVLSPGPQKP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_A4GTP4","disprot_id":"DP01578","ncbi_taxon_id":10090,"regions_counter":19,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":429,"region_id":"DP01578r001","released":"2024_06","ec_id":"ECO:0006165","reference_html":"Opposing effects of Elk-1 multisite phosphorylation shape its response to ERK activation. <i> Mylona A, Theillet FX, Foster C, Cheng TM, Miralles F, Bates PA, Selenko P, Treisman R. </i> Science, 2016","statement":[{"text":"Chemical shift analysis (Cα, Cβ) showed no stable secondary structure elements in unmodified or phosphorylated Elk-1 TAD (fig. S2B).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":309,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-08T15:57:35.626Z","reference_source":"pmid","term_name":"disorder","reference_id":"27738173","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"BMRB","id":"26762"}]},{"start":335,"end":339,"reference_id":"7738173","reference_source":"pmid","reference_html":"CD8 naive T cell counts decrease progressively in HIV-infected adults. <i> Roederer M, Dubs JG, Anderson MT, Raju PA, Herzenberg LA, Herzenberg LA. </i> J Clin Invest, 1995","date":"2024-02-08T16:05:40.043Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007719","ec_ontology":"ECO","ec_name":"immunodetection assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":337,"end":337,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":354,"end":354,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":364,"end":364,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":369,"end":369,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":384,"end":384,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":390,"end":390,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":418,"end":418,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":423,"end":423,"position":"Specific residue"}],"cross_refs":[{"db":"BMRB","id":"26786"}],"region_id":"DP01578r005","statement":[{"text":"To obtain atomic-resolution insights into phosphorylation of the Elk-1 TAD, we used nuclear magnetic resonance (NMR) spectroscopy (20) to monitor its modification by recombinant ERK2 in vitro (Fig. 1B; fig. S2A). Time-resolved NMR experiments revealed that each phosphorylation proceeded efficiently, but at markedly different rates. Phosphorylation of Thr369 and Ser384, which flank the central Phe–Trp (FW) motif implicated in Mediator interaction (18), occurred faster than modification of Thr364, Thr354 and Ser390, whereas residues Thr418, Ser423 and Thr337 were modified more slowly (Fig. 1C), which we confirmed by immunoblotting (Fig. 1D). ","type":"Results"}]},{"start":367,"end":371,"reference_id":"7738173","reference_source":"pmid","reference_html":"CD8 naive T cell counts decrease progressively in HIV-infected adults. <i> Roederer M, Dubs JG, Anderson MT, Raju PA, Herzenberg LA, Herzenberg LA. </i> J Clin Invest, 1995","date":"2024-02-08T16:03:43.543Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":337,"end":337,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":354,"end":354,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":364,"end":364,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":369,"end":369,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":384,"end":384,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":390,"end":390,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":418,"end":418,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":423,"end":423,"position":"Specific residue"}],"cross_refs":[{"db":"BMRB","id":"26786"}],"region_id":"DP01578r006","statement":[{"text":"To obtain atomic-resolution insights into phosphorylation of the Elk-1 TAD, we used nuclear magnetic resonance (NMR) spectroscopy (20) to monitor its modification by recombinant ERK2 in vitro (Fig. 1B; fig. S2A). Time-resolved NMR experiments revealed that each phosphorylation proceeded efficiently, but at markedly different rates. Phosphorylation of Thr369 and Ser384, which flank the central Phe–Trp (FW) motif implicated in Mediator interaction (18), occurred faster than modification of Thr364, Thr354 and Ser390, whereas residues Thr418, Ser423 and Thr337 were modified more slowly (Fig. 1C), which we confirmed by immunoblotting (Fig. 1D). ","type":"Results"}]},{"start":382,"end":386,"reference_id":"7738173","reference_source":"pmid","reference_html":"CD8 naive T cell counts decrease progressively in HIV-infected adults. <i> Roederer M, Dubs JG, Anderson MT, Raju PA, Herzenberg LA, Herzenberg LA. </i> J Clin Invest, 1995","date":"2024-02-08T16:04:04.817Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":337,"end":337,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":354,"end":354,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":364,"end":364,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":369,"end":369,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":384,"end":384,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":390,"end":390,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":418,"end":418,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":423,"end":423,"position":"Specific residue"}],"cross_refs":[{"db":"BMRB","id":"26786"}],"region_id":"DP01578r007","statement":[{"text":"To obtain atomic-resolution insights into phosphorylation of the Elk-1 TAD, we used nuclear magnetic resonance (NMR) spectroscopy (20) to monitor its modification by recombinant ERK2 in vitro (Fig. 1B; fig. S2A). Time-resolved NMR experiments revealed that each phosphorylation proceeded efficiently, but at markedly different rates. Phosphorylation of Thr369 and Ser384, which flank the central Phe–Trp (FW) motif implicated in Mediator interaction (18), occurred faster than modification of Thr364, Thr354 and Ser390, whereas residues Thr418, Ser423 and Thr337 were modified more slowly (Fig. 1C), which we confirmed by immunoblotting (Fig. 1D). ","type":"Results"}]},{"start":362,"end":366,"reference_id":"7738173","reference_source":"pmid","reference_html":"CD8 naive T cell counts decrease progressively in HIV-infected adults. <i> Roederer M, Dubs JG, Anderson MT, Raju PA, Herzenberg LA, Herzenberg LA. </i> J Clin Invest, 1995","date":"2024-02-08T16:04:19.909Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":337,"end":337,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":354,"end":354,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":364,"end":364,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":369,"end":369,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":384,"end":384,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":390,"end":390,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":418,"end":418,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":423,"end":423,"position":"Specific residue"}],"cross_refs":[{"db":"BMRB","id":"26786"}],"region_id":"DP01578r008","statement":[{"text":"To obtain atomic-resolution insights into phosphorylation of the Elk-1 TAD, we used nuclear magnetic resonance (NMR) spectroscopy (20) to monitor its modification by recombinant ERK2 in vitro (Fig. 1B; fig. S2A). Time-resolved NMR experiments revealed that each phosphorylation proceeded efficiently, but at markedly different rates. Phosphorylation of Thr369 and Ser384, which flank the central Phe–Trp (FW) motif implicated in Mediator interaction (18), occurred faster than modification of Thr364, Thr354 and Ser390, whereas residues Thr418, Ser423 and Thr337 were modified more slowly (Fig. 1C), which we confirmed by immunoblotting (Fig. 1D). ","type":"Results"}]},{"start":352,"end":357,"reference_id":"7738173","reference_source":"pmid","reference_html":"CD8 naive T cell counts decrease progressively in HIV-infected adults. <i> Roederer M, Dubs JG, Anderson MT, Raju PA, Herzenberg LA, Herzenberg LA. </i> J Clin Invest, 1995","date":"2024-02-08T16:04:29.447Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":337,"end":337,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":354,"end":354,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":364,"end":364,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":369,"end":369,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":384,"end":384,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":390,"end":390,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":418,"end":418,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":423,"end":423,"position":"Specific residue"}],"cross_refs":[{"db":"BMRB","id":"26786"}],"region_id":"DP01578r009","statement":[{"text":"To obtain atomic-resolution insights into phosphorylation of the Elk-1 TAD, we used nuclear magnetic resonance (NMR) spectroscopy (20) to monitor its modification by recombinant ERK2 in vitro (Fig. 1B; fig. S2A). Time-resolved NMR experiments revealed that each phosphorylation proceeded efficiently, but at markedly different rates. Phosphorylation of Thr369 and Ser384, which flank the central Phe–Trp (FW) motif implicated in Mediator interaction (18), occurred faster than modification of Thr364, Thr354 and Ser390, whereas residues Thr418, Ser423 and Thr337 were modified more slowly (Fig. 1C), which we confirmed by immunoblotting (Fig. 1D). ","type":"Results"}]},{"start":388,"end":392,"reference_id":"7738173","reference_source":"pmid","reference_html":"CD8 naive T cell counts decrease progressively in HIV-infected adults. <i> Roederer M, Dubs JG, Anderson MT, Raju PA, Herzenberg LA, Herzenberg LA. </i> J Clin Invest, 1995","date":"2024-02-08T16:04:41.788Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":337,"end":337,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":354,"end":354,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":364,"end":364,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":369,"end":369,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":384,"end":384,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":390,"end":390,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":418,"end":418,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":423,"end":423,"position":"Specific residue"}],"cross_refs":[{"db":"BMRB","id":"26786"}],"region_id":"DP01578r010","statement":[{"text":"To obtain atomic-resolution insights into phosphorylation of the Elk-1 TAD, we used nuclear magnetic resonance (NMR) spectroscopy (20) to monitor its modification by recombinant ERK2 in vitro (Fig. 1B; fig. S2A). Time-resolved NMR experiments revealed that each phosphorylation proceeded efficiently, but at markedly different rates. Phosphorylation of Thr369 and Ser384, which flank the central Phe–Trp (FW) motif implicated in Mediator interaction (18), occurred faster than modification of Thr364, Thr354 and Ser390, whereas residues Thr418, Ser423 and Thr337 were modified more slowly (Fig. 1C), which we confirmed by immunoblotting (Fig. 1D). ","type":"Results"}]},{"start":416,"end":420,"reference_id":"7738173","reference_source":"pmid","reference_html":"CD8 naive T cell counts decrease progressively in HIV-infected adults. <i> Roederer M, Dubs JG, Anderson MT, Raju PA, Herzenberg LA, Herzenberg LA. </i> J Clin Invest, 1995","date":"2024-02-08T16:05:12.575Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007719","ec_ontology":"ECO","ec_name":"immunodetection assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":337,"end":337,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":354,"end":354,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":364,"end":364,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":369,"end":369,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":384,"end":384,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":390,"end":390,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":418,"end":418,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":423,"end":423,"position":"Specific residue"}],"cross_refs":[{"db":"BMRB","id":"26786"}],"region_id":"DP01578r011","statement":[{"text":"To obtain atomic-resolution insights into phosphorylation of the Elk-1 TAD, we used nuclear magnetic resonance (NMR) spectroscopy (20) to monitor its modification by recombinant ERK2 in vitro (Fig. 1B; fig. S2A). Time-resolved NMR experiments revealed that each phosphorylation proceeded efficiently, but at markedly different rates. Phosphorylation of Thr369 and Ser384, which flank the central Phe–Trp (FW) motif implicated in Mediator interaction (18), occurred faster than modification of Thr364, Thr354 and Ser390, whereas residues Thr418, Ser423 and Thr337 were modified more slowly (Fig. 1C), which we confirmed by immunoblotting (Fig. 1D). ","type":"Results"}]},{"start":421,"end":425,"reference_id":"7738173","reference_source":"pmid","reference_html":"CD8 naive T cell counts decrease progressively in HIV-infected adults. <i> Roederer M, Dubs JG, Anderson MT, Raju PA, Herzenberg LA, Herzenberg LA. </i> J Clin Invest, 1995","date":"2024-02-08T16:05:22.743Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007719","ec_ontology":"ECO","ec_name":"immunodetection assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":337,"end":337,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":354,"end":354,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":364,"end":364,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":369,"end":369,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":384,"end":384,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":390,"end":390,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":418,"end":418,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":423,"end":423,"position":"Specific residue"}],"cross_refs":[{"db":"BMRB","id":"26786"}],"region_id":"DP01578r012","statement":[{"text":"To obtain atomic-resolution insights into phosphorylation of the Elk-1 TAD, we used nuclear magnetic resonance (NMR) spectroscopy (20) to monitor its modification by recombinant ERK2 in vitro (Fig. 1B; fig. S2A). Time-resolved NMR experiments revealed that each phosphorylation proceeded efficiently, but at markedly different rates. Phosphorylation of Thr369 and Ser384, which flank the central Phe–Trp (FW) motif implicated in Mediator interaction (18), occurred faster than modification of Thr364, Thr354 and Ser390, whereas residues Thr418, Ser423 and Thr337 were modified more slowly (Fig. 1C), which we confirmed by immunoblotting (Fig. 1D). ","type":"Results"}]},{"start":354,"end":390,"reference_id":"7738173","reference_source":"pmid","reference_html":"CD8 naive T cell counts decrease progressively in HIV-infected adults. <i> Roederer M, Dubs JG, Anderson MT, Raju PA, Herzenberg LA, Herzenberg LA. </i> J Clin Invest, 1995","date":"2024-02-08T16:40:07.694Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140537","term_name":"transcription regulator activator activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr369Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser384Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr354Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr364Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser390Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe379Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp380Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]}],"ec_go":"IMP","region_id":"DP01578r013","statement":[{"text":"As expected, alanine substitutions of fast and/or intermediate sites, or of the FW motif, greatly diminished or abolished the ability of Elk-1 to activate TCF-SRF target gene transcription after TPA stimulation (Fig. 3A; fig. S4D). Surprisingly, however, mutation of the slow sites substantially enhanced Elk-1-mediated activation of TCF-SRF target genes (Fig. 3A).","type":"Results"},{"text":"The reconstituted TKO MEFs exhibited enhanced proliferation rates, which correlated with the ability of each mutant to promote transcriptional activation (Fig. 3C).","type":"Results"},{"text":" Mutagenesis experiments showed that phosphorylation of fast and intermediate sites promoted Mediator interaction and transcriptional activation, whereas modification of slow sites counteracted both functions, thereby limiting Elk-1 output.","type":"Abstract"}],"term_comment":"Usage guidance: transcription regulator activators bind to a transcription regulator to allow it to reach the chromatin or to contact other transcriptional regulators. This activity does not occur at the promoter. For activities that do occur at the promoter, consider GO:0001216 ; DNA-binding transcription activator activity or GO:0003713; transcription coactivator activity; those activities respectively bind DNA themselves or positively regulate a transcription regulator when it is located at the chromatin.","term_def":"\"A molecular function regulator that increases the activity of a transcription regulator via direct binding and/or post-translational modification.\" [PMID:9597751]","term_is_obsolete":false,"term_not_annotate":false},{"start":335,"end":339,"reference_id":"7738173","reference_source":"pmid","reference_html":"CD8 naive T cell counts decrease progressively in HIV-infected adults. <i> Roederer M, Dubs JG, Anderson MT, Raju PA, Herzenberg LA, Herzenberg LA. </i> J Clin Invest, 1995","date":"2024-02-08T16:39:45.402Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140416","term_name":"transcription regulator inhibitor activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr418Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser423Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr337Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]}],"ec_go":"IMP","region_id":"DP01578r014","statement":[{"text":"As expected, alanine substitutions of fast and/or intermediate sites, or of the FW motif, greatly diminished or abolished the ability of Elk-1 to activate TCF-SRF target gene transcription after TPA stimulation (Fig. 3A; fig. S4D). Surprisingly, however, mutation of the slow sites substantially enhanced Elk-1-mediated activation of TCF-SRF target genes (Fig. 3A).","type":"Results"},{"text":"The reconstituted TKO MEFs exhibited enhanced proliferation rates, which correlated with the ability of each mutant to promote transcriptional activation (Fig. 3C).","type":"Results"}],"term_comment":"Usage guidance: transcription regulator inhibitors bind to a transcription regulator to prevent it from reaching the chromatin. This activity does not occur at the promoter. For activities that do occur at the promoter, consider GO:0001217 ; DNA-binding transcription repressor activity or GO:0003714 ; transcription corepressor activity. An example of a transcription regulator is TCF23 Q7RTU1 is an example of a protein that regulates transcription factors by heterodimerising or binding to DbTFs and prevent DNA binding and their specific genomic binding site where the dbTF would have activated or repressed transcription. Also an example is NFKBIA P25963 which has a different way of regulating transcription factor activity by sequestering the dbTF (complex) in the cytoplasm. Another example is the HSP90 and HSP23 proteins that sequester steroid receptors away from the DNA.","term_def":"\"A molecular function regulator that inhibits the activity of a transcription regulator via direct binding and/or post-translational modification.\" [PMID:10652346]","term_is_obsolete":false,"term_not_annotate":false},{"start":418,"end":423,"reference_id":"7738173","reference_source":"pmid","reference_html":"CD8 naive T cell counts decrease progressively in HIV-infected adults. <i> Roederer M, Dubs JG, Anderson MT, Raju PA, Herzenberg LA, Herzenberg LA. </i> J Clin Invest, 1995","date":"2024-02-08T16:40:30.593Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140416","term_name":"transcription regulator inhibitor activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr418Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser423Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr337Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]}],"ec_go":"IMP","region_id":"DP01578r015","statement":[{"text":"As expected, alanine substitutions of fast and/or intermediate sites, or of the FW motif, greatly diminished or abolished the ability of Elk-1 to activate TCF-SRF target gene transcription after TPA stimulation (Fig. 3A; fig. S4D). Surprisingly, however, mutation of the slow sites substantially enhanced Elk-1-mediated activation of TCF-SRF target genes (Fig. 3A).","type":"Results"},{"text":"The reconstituted TKO MEFs exhibited enhanced proliferation rates, which correlated with the ability of each mutant to promote transcriptional activation (Fig. 3C).","type":"Results"},{"text":" Mutagenesis experiments showed that phosphorylation of fast and intermediate sites promoted Mediator interaction and transcriptional activation, whereas modification of slow sites counteracted both functions, thereby limiting Elk-1 output.","type":"Abstract"}],"term_comment":"Usage guidance: transcription regulator inhibitors bind to a transcription regulator to prevent it from reaching the chromatin. This activity does not occur at the promoter. For activities that do occur at the promoter, consider GO:0001217 ; DNA-binding transcription repressor activity or GO:0003714 ; transcription corepressor activity. An example of a transcription regulator is TCF23 Q7RTU1 is an example of a protein that regulates transcription factors by heterodimerising or binding to DbTFs and prevent DNA binding and their specific genomic binding site where the dbTF would have activated or repressed transcription. Also an example is NFKBIA P25963 which has a different way of regulating transcription factor activity by sequestering the dbTF (complex) in the cytoplasm. Another example is the HSP90 and HSP23 proteins that sequester steroid receptors away from the DNA.","term_def":"\"A molecular function regulator that inhibits the activity of a transcription regulator via direct binding and/or post-translational modification.\" [PMID:10652346]","term_is_obsolete":false,"term_not_annotate":false},{"start":418,"end":423,"reference_id":"7738173","reference_source":"pmid","reference_html":"CD8 naive T cell counts decrease progressively in HIV-infected adults. <i> Roederer M, Dubs JG, Anderson MT, Raju PA, Herzenberg LA, Herzenberg LA. </i> J Clin Invest, 1995","date":"2024-02-08T16:38:04.436Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0032091","term_name":"negative regulation of protein binding","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr418Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser423Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr337Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q6PGF3","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9VSF2","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q80YQ2","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01578r016","statement":[{"text":"We prepared extracts of TKO cells expressing wildtype or mutant Elk-1 proteins and assessed Elk-1 assocation with Mediator by co-immunoprecipitation of the MED23, MED24 and MED16 subunits. Consistent with the transcription experiments, Elk-1–Mediator interaction was induced by TPA stimulation and dependent on the FW motif; it was abolished by alanine substitutions of fast and intermediate sites, and was increased in the slow-site Elk-1 mutant (Fig. 3D).","type":"Results"},{"text":" Mutagenesis experiments showed that phosphorylation of fast and intermediate sites promoted Mediator interaction and transcriptional activation, whereas modification of slow sites counteracted both functions, thereby limiting Elk-1 output.","type":"Abstract"}],"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of protein binding.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":335,"end":339,"reference_id":"7738173","reference_source":"pmid","reference_html":"CD8 naive T cell counts decrease progressively in HIV-infected adults. <i> Roederer M, Dubs JG, Anderson MT, Raju PA, Herzenberg LA, Herzenberg LA. </i> J Clin Invest, 1995","date":"2024-02-08T16:38:47.667Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0032091","term_name":"negative regulation of protein binding","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr418Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser423Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr337Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q6PGF3","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9VSF2","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q80YQ2","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01578r017","statement":[{"text":"We prepared extracts of TKO cells expressing wildtype or mutant Elk-1 proteins and assessed Elk-1 assocation with Mediator by co-immunoprecipitation of the MED23, MED24 and MED16 subunits. Consistent with the transcription experiments, Elk-1–Mediator interaction was induced by TPA stimulation and dependent on the FW motif; it was abolished by alanine substitutions of fast and intermediate sites, and was increased in the slow-site Elk-1 mutant (Fig. 3D).","type":"Results"},{"text":" Mutagenesis experiments showed that phosphorylation of fast and intermediate sites promoted Mediator interaction and transcriptional activation, whereas modification of slow sites counteracted both functions, thereby limiting Elk-1 output.","type":"Abstract"}],"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of protein binding.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":335,"end":339,"reference_id":"7738173","reference_source":"pmid","reference_html":"CD8 naive T cell counts decrease progressively in HIV-infected adults. <i> Roederer M, Dubs JG, Anderson MT, Raju PA, Herzenberg LA, Herzenberg LA. </i> J Clin Invest, 1995","date":"2024-02-08T16:42:44.111Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0032092","term_name":"positive regulation of protein binding","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr369Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser384Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr354Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr364Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser390Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe379Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp380Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Elk-1 mutants were: Elk-1F, T369A, S384A; Elk-1I, T354A, T364A, S390A; Elk-1S, T337A, T418A, S423A; Elk-1FI, T354A, T364A, T369A, S384A, S390A; Elk-1FW, F379A, W380A, Elk-1 T418A; Elk-1 S423A; Elk-1 T337A."}]}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q6PGF3","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9VSF2","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q80YQ2","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01578r018","statement":[{"text":"We prepared extracts of TKO cells expressing wildtype or mutant Elk-1 proteins and assessed Elk-1 assocation with Mediator by co-immunoprecipitation of the MED23, MED24 and MED16 subunits. Consistent with the transcription experiments, Elk-1–Mediator interaction was induced by TPA stimulation and dependent on the FW motif; it was abolished by alanine substitutions of fast and intermediate sites, and was increased in the slow-site Elk-1 mutant (Fig. 3D).","type":"Results"},{"text":" Mutagenesis experiments showed that phosphorylation of fast and intermediate sites promoted Mediator interaction and transcriptional activation, whereas modification of slow sites counteracted both functions, thereby limiting Elk-1 output.","type":"Abstract"}],"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of protein binding.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":309,"end":429,"reference_id":"7738173","reference_source":"pmid","reference_html":"CD8 naive T cell counts decrease progressively in HIV-infected adults. <i> Roederer M, Dubs JG, Anderson MT, Raju PA, Herzenberg LA, Herzenberg LA. </i> J Clin Invest, 1995","date":"2024-02-08T16:51:23.304Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0036033","term_name":"mediator complex binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":337,"end":337,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":354,"end":354,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":364,"end":364,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":369,"end":369,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":384,"end":384,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":390,"end":390,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":418,"end":418,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":423,"end":423,"position":"Specific residue"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q80YQ2","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9VSF2","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q6PGF3","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01578r019","statement":[{"text":"We obtained similar results when we used glutathione S-transferase (GST)-Elk-1 TAD proteins to recover Mediator proteins from unstimulated NIH3T3 cell extracts (Fig. 3E). In this assay, ERK2 phosphorylation time-course experiments showed that Mediator recovery by the wildtype Elk-1 TAD was most efficient prior to modifications of the slow sites (fig. S5, A and B). Taken together, these data show that according to the sites involved, ERK2 phosphorylation promotes or inhibits transcriptional activation by Elk-1, which reflects alterations in Elk-1–Mediator interactions.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a mediator complex. The mediator complex is a protein complex that interacts with the carboxy-terminal domain of the largest subunit of RNA polymerase II and plays an active role in transducing the signal from a transcription factor to the transcriptional machinery. The Saccharomyces complex contains several identifiable subcomplexes: a head domain comprising Srb2, -4, and -5, Med6, -8, and -11, and Rox3 proteins; a middle domain comprising Med1, -4, and -7, Nut1 and -2, Cse2, Rgr1, Soh1, and Srb7 proteins; a tail consisting of Gal11p, Med2p, Pgd1p, and Sin4p; and a regulatory subcomplex comprising Ssn2, -3, and -8, and Srb8 proteins. Metazoan mediator complexes have similar modular structures and include homologs of yeast Srb and Med proteins.\" [GOC:yaf, PMID:18391015]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_P41969","date":"2018-07-30T12:20:52.000Z","acc":"P41969","name":"ETS domain-containing protein Elk-1","length":429,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000027E0C","genes":[{"name":{"value":"Elk1","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:101833","url":"http://www.informatics.jax.org/marker/MGI:101833"}}]}}],"alphafold_very_low_content":0.5244755244755245,"disorder_content":0.28205128205128205,"disprot_consensus":{"full":[{"start":309,"end":429,"type":"D"}],"Structural state":[{"start":309,"end":429,"type":"D"}],"Disorder function":[{"start":335,"end":339,"type":"F"},{"start":352,"end":357,"type":"F"},{"start":362,"end":371,"type":"F"},{"start":382,"end":386,"type":"F"},{"start":388,"end":392,"type":"F"},{"start":416,"end":425,"type":"F"}],"Molecular function":[{"start":309,"end":429,"type":"F"}],"Biological process":[{"start":335,"end":339,"type":"F"},{"start":418,"end":423,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00320","name":"GATA zinc finger","start":499,"end":535}],"gene3D":[{"start":492,"end":541,"id":"3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A"}]},"uniref50":"UniRef50_P34233","sequence":"MSSLYIKTPLHALSAGPDSHANSSYYDNLLLPSFSNLSSNISRNNITTDNNINSASPRKYSFHSLNVSPILSPISLANEILGKKSNTAPASPHHMDYNPISSLTPGNSPEFNKASLSQISFTNPLNYGSGLGFSSNSQPRLPLLDRLSSVSLSKRPERPQQSLPSLRHLQLLPSPLLQENAARFPDTSKRTSNWKTDLTHWCKDTNYQDYVKIREEVAHFKPLSIPNLTNNQNNDSFNYGKELESTRSSKFHSPSKESFDRTKLIPSILEAKDQFKDLSNNAWSITPPVTPPMSPPTNRTMERTTLRGVEASFFEGKSSNNDSIFNPIISEKLVQEVKHQRQLRGNSFPMPNASHKKTNSFKALQIKKLLANRDILSNNSKSNVRKPSKNKISKQASNVFGNTARQLVMKLDNASYSSVSASSSPSPSTPTKSGKMRSRSSSPVRPKAYTPSPRSPNYHRFALDSPPQSPRRSSNSSITKKGSRRSSGSSPTRHTTRVCVSCHSSDSPCWRPSWSPRKQDQLCNSCGLRYKKTHTRCLNDLCRKIPTKGEINIMKSNGIDKEFVPERNCEIEGYRCLFCNYITETVEN","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P34233","disprot_id":"DP01579","ncbi_taxon_id":559292,"regions_counter":7,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":500,"region_id":"DP01579r001","released":"2024_06","ec_id":"ECO:0005642","reference_html":"Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and upon Multisite Phosphorylation. <i> Martin EW, Holehouse AS, Grace CR, Hughes A, Pappu RV, Mittag T. </i> J Am Chem Soc, 2016","statement":[{"text":" The HSQC spectra show poor chemical shift dispersions and sharp line widths for both sequences.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":420,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-20T17:05:43.523Z","reference_source":"pmid","term_name":"disorder","reference_id":"27807972","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"BMRB","id":"26719"}]},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":429,"term_name":"phosphorylation display site","released":"2024_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and upon Multisite Phosphorylation. <i> Martin EW, Holehouse AS, Grace CR, Hughes A, Pappu RV, Mittag T. </i> J Am Chem Soc, 2016","statement":[{"text":"The 10-fold phosphorylated version of Ash1 (referred to hereafter as pAsh1) was generated via overnight incubation of Ash1 with Cyclin A/Cdk2 (Figure S3).","type":"Results"},{"text":"Phosphorylation resulted in a downfield shift of 1H resonances and upfield shift of 15N resonances, especially for phosphorylated residues.","type":"Results"}],"term_id":"IDPO:0000045","curator_id":"vnugnes","start":424,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27807972","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-20T17:00:37.825Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01579r002","ec_go":"EXP","disprot_namespace":"Disorder function","construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":424,"end":424,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":426,"end":426,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":429,"end":429,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":442,"end":442,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":450,"end":450,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":452,"end":452,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":455,"end":455,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":465,"end":465,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":469,"end":469,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":490,"end":490,"position":"Specific residue"}],"cross_refs":[{"db":"BMRB","id":"26720"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":500,"region_id":"DP01579r003","released":"2024_06","ec_id":"ECO:0006210","reference_html":"Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and upon Multisite Phosphorylation. <i> Martin EW, Holehouse AS, Grace CR, Hughes A, Pappu RV, Mittag T. </i> J Am Chem Soc, 2016","statement":[{"text":"SAXS data for unphosphorylated Ash1420–500 (referred to hereafter as Ash1) were collected to probe the global conformational preferences of this IDR.","type":"Results"},{"text":"Experimental SAXS data indicates disordered nature of Ash1 and pAsh1","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":420,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-20T16:50:26.516Z","reference_source":"pmid","term_name":"disorder","reference_id":"27807972","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"GASASSSPSPSTPTKSGKMRSRSSSPVRPKAYTPSPRSPNYHRFALDSPPQSPRRSSNSSITKKGSRRSSGSSPTRHTTRVCV"},{"start":440,"end":445,"reference_id":"27807972","reference_source":"pmid","reference_html":"Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and upon Multisite Phosphorylation. <i> Martin EW, Holehouse AS, Grace CR, Hughes A, Pappu RV, Mittag T. </i> J Am Chem Soc, 2016","date":"2024-02-20T17:03:24.552Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":424,"end":424,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":426,"end":426,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":429,"end":429,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":442,"end":442,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":450,"end":450,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":452,"end":452,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":455,"end":455,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":465,"end":465,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":469,"end":469,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":490,"end":490,"position":"Specific residue"}],"cross_refs":[{"db":"BMRB","id":"26720"}],"region_id":"DP01579r004","statement":[{"text":"The 10-fold phosphorylated version of Ash1 (referred to hereafter as pAsh1) was generated via overnight incubation of Ash1 with Cyclin A/Cdk2 (Figure S3).","type":"Results"},{"text":"Phosphorylation resulted in a downfield shift of 1H resonances and upfield shift of 15N resonances, especially for phosphorylated residues.","type":"Results"}]},{"start":450,"end":455,"reference_id":"27807972","reference_source":"pmid","reference_html":"Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and upon Multisite Phosphorylation. <i> Martin EW, Holehouse AS, Grace CR, Hughes A, Pappu RV, Mittag T. </i> J Am Chem Soc, 2016","date":"2024-02-20T17:03:31.437Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":424,"end":424,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":426,"end":426,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":429,"end":429,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":442,"end":442,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":450,"end":450,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":452,"end":452,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":455,"end":455,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":465,"end":465,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":469,"end":469,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":490,"end":490,"position":"Specific residue"}],"cross_refs":[{"db":"BMRB","id":"26720"}],"region_id":"DP01579r005","statement":[{"text":"The 10-fold phosphorylated version of Ash1 (referred to hereafter as pAsh1) was generated via overnight incubation of Ash1 with Cyclin A/Cdk2 (Figure S3).","type":"Results"},{"text":"Phosphorylation resulted in a downfield shift of 1H resonances and upfield shift of 15N resonances, especially for phosphorylated residues.","type":"Results"}]},{"start":465,"end":469,"reference_id":"27807972","reference_source":"pmid","reference_html":"Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and upon Multisite Phosphorylation. <i> Martin EW, Holehouse AS, Grace CR, Hughes A, Pappu RV, Mittag T. </i> J Am Chem Soc, 2016","date":"2024-02-20T17:03:49.176Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":424,"end":424,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":426,"end":426,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":429,"end":429,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":442,"end":442,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":450,"end":450,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":452,"end":452,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":455,"end":455,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":465,"end":465,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":469,"end":469,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":490,"end":490,"position":"Specific residue"}],"cross_refs":[{"db":"BMRB","id":"26720"}],"region_id":"DP01579r006","statement":[{"text":"The 10-fold phosphorylated version of Ash1 (referred to hereafter as pAsh1) was generated via overnight incubation of Ash1 with Cyclin A/Cdk2 (Figure S3).","type":"Results"},{"text":"Phosphorylation resulted in a downfield shift of 1H resonances and upfield shift of 15N resonances, especially for phosphorylated residues.","type":"Results"}]},{"start":488,"end":492,"reference_id":"27807972","reference_source":"pmid","reference_html":"Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and upon Multisite Phosphorylation. <i> Martin EW, Holehouse AS, Grace CR, Hughes A, Pappu RV, Mittag T. </i> J Am Chem Soc, 2016","date":"2024-02-20T17:04:04.663Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":424,"end":424,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":426,"end":426,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":429,"end":429,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":442,"end":442,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":450,"end":450,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":452,"end":452,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":455,"end":455,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":465,"end":465,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":469,"end":469,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":490,"end":490,"position":"Specific residue"}],"cross_refs":[{"db":"BMRB","id":"26720"}],"region_id":"DP01579r007","statement":[{"text":"The 10-fold phosphorylated version of Ash1 (referred to hereafter as pAsh1) was generated via overnight incubation of Ash1 with Cyclin A/Cdk2 (Figure S3).","type":"Results"},{"text":"Phosphorylation resulted in a downfield shift of 1H resonances and upfield shift of 15N resonances, especially for phosphorylated residues.","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_P34233","date":"2018-07-30T12:53:27.000Z","acc":"P34233","name":"Transcriptional regulatory protein ASH1","length":588,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000126104","genes":[{"name":{"value":"ASH1"},"olnNames":[{"value":"YKL185W"}]}],"alphafold_very_low_content":0.30612244897959184,"disorder_content":0.1377551020408163,"disprot_consensus":{"full":[{"start":420,"end":500,"type":"D"}],"Structural state":[{"start":420,"end":500,"type":"D"}],"Disorder function":[{"start":424,"end":429,"type":"F"},{"start":440,"end":445,"type":"F"},{"start":450,"end":455,"type":"F"},{"start":465,"end":469,"type":"F"},{"start":488,"end":492,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00017","name":"SH2 domain","start":127,"end":209},{"id":"PF00018","name":"SH3 domain","start":67,"end":112},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":245,"end":493}],"gene3D":[{"start":116,"end":234,"id":"3.30.505.10","name":"SH2 domain"},{"start":235,"end":319,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":320,"end":499,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"},{"start":58,"end":115,"id":"2.30.30.40","name":"SH3 Domains"}]},"uniref50":"UniRef50_P06239","sequence":"MGCGCSSHPEDDWMENIDVCENCHYPIVPLDGKGTLLIRNGSEVRDPLVTYEGSNPPASPLQDNLVIALHSYEPSHDGDLGFEKGEQLRILEQSGEWWKAQSLTTGQEGFIPFNFVAKANSLEPEPWFFKNLSRKDAERQLLAPGNTHGSFLIRESESTAGSFSLSVRDFDQNQGEVVKHYKIRNLDNGGFYISPRITFPGLHELVRHYTNASDGLCTRLSRPCQTQKPQKPWWEDEWEVPRETLKLVERLGAGQFGEVWMGYYNGHTKVAVKSLKQGSMSPDAFLAEANLMKQLQHQRLVRLYAVVTQEPIYIITEYMENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTAREGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRMVRPDNCPEELYQLMRLCWKERPEDRPTFDYLRSVLEDFFTATEGQYQPQP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P06239","disprot_id":"DP01580","ncbi_taxon_id":9606,"regions_counter":4,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":86,"region_id":"DP01580r001","released":"2022_03","ec_id":"ECO:0006196","reference_html":"Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip. <i> Weis DD, Kjellen P, Sefton BM, Engen JR. </i> Protein Sci, 2006","statement":[{"text":"HX MS of unbound Lck SH3 shows that Lck SH3 undergoes local unfolding with a half-life of ;10 sec. This unfolding rate is in stark contrast to that observed for Hck SH3 (;17 min). Regions that undergo local unfolding are shown in red (residues 44–61) and blue (residues 16–33).","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":69,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17008721","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":86,"term_name":"order to disorder","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","reference_html":"Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip. <i> Weis DD, Kjellen P, Sefton BM, Engen JR. </i> Protein Sci, 2006","statement":[{"text":"HX MS of unbound Lck SH3 shows that Lck SH3 undergoes local unfolding with a half-life of ;10 sec. This unfolding rate is in stark contrast to that observed for Hck SH3 (;17 min). Regions that undergo local unfolding are shown in red (residues 44–61) and blue (residues 16–33).","type":"Figure"}],"term_id":"IDPO:0000014","curator_id":"ndavey","start":69,"term_ontology":"IDPO","curator_name":"Norman Davey","reference_id":"17008721","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006196","region_id":"DP01580r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":114,"region_id":"DP01580r003","released":"2022_03","ec_id":"ECO:0006196","reference_html":"Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip. <i> Weis DD, Kjellen P, Sefton BM, Engen JR. </i> Protein Sci, 2006","statement":[{"text":"HX MS of unbound Lck SH3 shows that Lck SH3 undergoes local unfolding with a half-life of ;10 sec. This unfolding rate is in stark contrast to that observed for Hck SH3 (;17 min). Regions that undergo local unfolding are shown in red (residues 44–61) and blue (residues 16–33).","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":97,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17008721","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":114,"term_name":"order to disorder","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","reference_html":"Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip. <i> Weis DD, Kjellen P, Sefton BM, Engen JR. </i> Protein Sci, 2006","statement":[{"text":"HX MS of unbound Lck SH3 shows that Lck SH3 undergoes local unfolding with a half-life of ;10 sec. This unfolding rate is in stark contrast to that observed for Hck SH3 (;17 min). Regions that undergo local unfolding are shown in red (residues 44–61) and blue (residues 16–33).","type":"Results"}],"term_id":"IDPO:0000014","curator_id":"ndavey","start":97,"term_ontology":"IDPO","curator_name":"Norman Davey","reference_id":"17008721","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006196","region_id":"DP01580r004","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_P06239","date":"2018-07-30T12:53:42.000Z","acc":"P06239","name":"Tyrosine-protein kinase Lck","length":509,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI000016AF39","genes":[{"name":{"value":"LCK"}}],"alphafold_very_low_content":0.11984282907662082,"disorder_content":0.07072691552062868,"disprot_consensus":{"full":[{"start":69,"end":86,"type":"T"},{"start":97,"end":114,"type":"T"}],"Structural state":[{"start":69,"end":86,"type":"D"},{"start":97,"end":114,"type":"D"}],"Structural transition":[{"start":69,"end":86,"type":"T"},{"start":97,"end":114,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00498","name":"FHA domain","start":68,"end":131}],"gene3D":[{"start":21,"end":140,"id":"2.60.200.20","name":"2.60.200.20"}]},"uniref50":"UniRef50_Q8NQJ3","sequence":"MSDNNGTPEPQVETTSVFRADLLKEMESSTGTAPASTGAENLPAGSALLVVKRGPNAGARFLLDQPTTTAGRHPESDIFLDDVTVSRRHAEFRINEGEFEVVDVGSLNGTYVNREPRNAQVMQTGDEIQIGKFRLVFLAGPAE","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Corynebacteriaceae","Corynebacterium"],"uniref90":"UniRef90_Q8NQJ3","disprot_id":"DP01581","ncbi_taxon_id":196627,"regions_counter":3,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":40,"region_id":"DP01581r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Dynamic and structural characterization of a bacterial FHA protein reveals a new autoinhibition mechanism. <i> Barthe P, Roumestand C, Canova MJ, Kremer L, Hurard C, Molle V, Cohen-Gonsaud M. </i> Structure, 2009","statement":[{"text":"NMR experiments revealed that the N-terminal part of the unphosphorylated OdhI protein is fully disordered (Met1-Glu40).","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":1,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2KB4"}],"reference_id":"19368890","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":40,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Dynamic and structural characterization of a bacterial FHA protein reveals a new autoinhibition mechanism. <i> Barthe P, Roumestand C, Canova MJ, Kremer L, Hurard C, Molle V, Cohen-Gonsaud M. </i> Structure, 2009","statement":[{"text":"pT15 - an important number of intense peaks centered around 8.5 ppm in the 1H dimension of the HSQC recorded on OdhI and attributed to mobile unfolded residues disappeared in the HSQC spectrum recorded on pOdhI. This suggests the structuring of a large part of the N-terminal residues upon phosphorylation. PDB:  2KB3 2KB4","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"ndavey","start":1,"term_ontology":"IDPO","curator_name":"Norman Davey","reference_id":"19368890","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01581r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":40,"term_name":"phosphorylation display site","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Dynamic and structural characterization of a bacterial FHA protein reveals a new autoinhibition mechanism. <i> Barthe P, Roumestand C, Canova MJ, Kremer L, Hurard C, Molle V, Cohen-Gonsaud M. </i> Structure, 2009","statement":[{"text":"the phosphorylation results in the folding of 26 amino acids from the N-terminal, but only seven of them, centered on pThr15, are in contact with the FHA core domain according to our NMR data.","type":"Results"}],"term_id":"IDPO:0000045","curator_id":"ndavey","start":1,"term_ontology":"IDPO","curator_name":"Norman Davey","reference_id":"19368890","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01581r003","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_Q8NQJ3","date":"2018-07-30T12:54:20.000Z","acc":"Q8NQJ3","name":"Oxoglutarate dehydrogenase inhibitor","length":143,"organism":"Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)","dataset":[],"UniParc":"UPI000003A53A","genes":[{"name":{"value":"odhI"},"olnNames":[{"value":"Cgl1441"},{"value":"cg1630"}]}],"alphafold_very_low_content":0.14685314685314685,"disorder_content":0.27972027972027974,"disprot_consensus":{"full":[{"start":1,"end":40,"type":"T"}],"Structural state":[{"start":1,"end":40,"type":"D"}],"Structural transition":[{"start":1,"end":40,"type":"T"}],"Disorder function":[{"start":1,"end":40,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00094","name":"von Willebrand factor type D domain","start":1444,"end":1614},{"id":"PF01347","name":"Vitellogenin TPR domain","start":425,"end":741},{"id":"PF09172","name":"Vitellinogen, open beta-sheet","start":775,"end":1028},{"id":"PF29934","name":"Vitellogenin N-terminal domain","start":22,"end":306}],"gene3D":[{"start":415,"end":770,"id":"1.25.10.20","name":"Vitellinogen, superhelical"},{"start":22,"end":322,"id":"2.30.230.10","name":"Lipovitellin; beta-sheet shell regions, chain A"}]},"uniref50":"UniRef50_Q868N5","sequence":"MLLLLTLLLFAGTVAADFQHNWQVGNEYTYLVRSRTLTSLGDLSDVHTGILIKALLTVQAKDSNVLAAKVWNGQYARVQQSMPDGWETEISDQMLELRDLPISGKPFQIRMKHGLIRDLIVDRDVPTWEVNILKSIVGQLQVDTQGENAVKVNSVQVPTDDEPYASFKAMEDSVGGKCEVLYDIAPLSDFVIHRSPELVPMPTLKGDGRHMEVIKIKNFDNCDQRINYHFGMTDNSRLEPGTNKNGKFFSRSSTSRIVISESLKHFTIQSSVTTSKMMVSPRLYDRQNGLVLSRMNLTLAKMEKTSKPLPMVDNPESTGNLVYIYNNPFSDVEERRVSKTAMNSNQIVSDNSLSSSEEKLKQDILNLRTDISSSSSSISSSEENDFWQPKPTLEDAPQNSLLPNFVGYKGKHIGKSGKVDVINAAKELIFQIANELEDASNIPVHATLEKFMILCNLMRTMNRKQISELESNMQISPNELKPNDKSQVIKQNTWTVFRDAITQTGTGPAFLTIKEWIERGTTKSMEAANIMSKLPKTVRTPTDSYIRSFFELLQNPKVSNEQFLNTAATLSFCEMIHNAQVNKRSIHNNYPVHTFGRLTSKHDNSLYDEYIPFLERELRKAHQEKDSPRIQTYIMALGMIGEPKILSVFEPYLEGKQQMTVFQRTLMVGSLGKLTETNPKLARSVLYKIYLNTMESHEVRCTAVFLLMKTNPPLSMLQRMAEFTKLDTNRQVNSAVKSTIQSLMKLKSPEWKDLAKKARSVNHLLTHHEYDYELSRGYIDEKILENQNIITHMILNYVGSEDSVIPRILYLTWYSSNGDIKVPSTKVLAMISSVKSFMELSLRSVKDRETIISAAEKIAEELKIVPEELVPLEGNLMINNKYALKFFPFDKHILDKLPTLISNYIEAVKEGKFMNVNMLDTYESVHSFPTETGLPFVYTFNVIKLTKTSGTVQAQINPDFAFIVNSNLRLTFSKNVQGRVGFVTPFEHRHFISGIDSNLHVYAPLKISLDVNTPKGNMQWKIWPMKGEEKSRLFHYSVVPFVSNHDILNLRPLSMEKGTRPMIPDDNTSLALPKNEGPFRLNVETAKTNEEMWELIDTEKLTDRLPYPWTMDNERYVKVDMYMNLEGEQKDPVIFSTSFDSKVMTRPDTDSENWTPKMMAVEPTDKQANSKTRRQEMMREAGRGIESAKSYVVDVRVHVPGESESETVLTLAWSESNVESKGRLLGFWRVEMPRSNADYEVCIGSQIMVSPETLLSYDEKMDQKPKMDFNVDIRYGKNCGKGERIDMNGKLRQSPRLKELVGATSIIKDCVEDMKRGNKILRTCQKAVVLSMLLDEVDISMEVPSDALIALYSQGLFSLSEIDNLDVSLDVSNPKNAGKKKIDVRAKLNEYLDKADVIVNTPIMDAHFKDVKLSDFGFSTEDILDTADEDLLINNVFYEDETSCMLDKTRAQTFDGKDYPLRLGPCWHAVMTTYPRINPDNHNEKLHIPKDKSVSVLSRENEAGQKEVKVLLGSDKIKFVPGTTSQPEVFVNGEKIVVSRNKAYQKVEENEIIFEIYKMGDRFIGLTSDKFDVSLALDGERVMLKASEDYRYSVRGLCGNFDHDSTNDFVGPKNCLFRKPEHFVASYALISNQCEGDSLNVAKSLQDHDCIRQERTQQRNVISDSESGRLDTEMSTWGYHHNVNKHCTIHRTQVKETDDKICFTMRPVVSCASGCTAVETKSKPYKFHCMEKNEAAMKLKKRIEKGANPDLSQKPVSTTEELTVPFVCKA","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Hymenoptera","Apocrita","Aculeata","Apoidea","Apidae","Apis"],"uniref90":"UniRef90_Q868N5","disprot_id":"DP01582","ncbi_taxon_id":7460,"regions_counter":7,"creator":"bjuhasz","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":392,"region_id":"DP01582r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation. <i> Havukainen H, Underhaug J, Wolschin F, Amdam G, Halskau Ø. </i> J Exp Biol, 2012","statement":[{"text":"NMR and circular dichroism (CD) evidence assign different conformational propensities to polyserine peptides from the honeybee and the jewel wasp Nasonia vitripennis; the former is extended and disordered and the latter more compact and helical.","type":"Introduction"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":358,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2LIC"}],"reference_id":"22573762","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":392,"region_id":"DP01582r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation. <i> Havukainen H, Underhaug J, Wolschin F, Amdam G, Halskau Ø. </i> J Exp Biol, 2012","statement":[{"text":"The UV spectra of the peptides show considerable differences, suggesting a random coil for AmVg(358–392).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":358,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22573762","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":385,"region_id":"DP01582r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation. <i> Havukainen H, Underhaug J, Wolschin F, Amdam G, Halskau Ø. </i> J Exp Biol, 2012","statement":[{"text":"AmVg (336–385) retains its random values and lack of NOEs indicative of any fixed structure, a result also supported by the CD spectrum","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":336,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22573762","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":385,"region_id":"DP01582r004","released":"2022_03","ec_id":"ECO:0006204","reference_html":"A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation. <i> Havukainen H, Underhaug J, Wolschin F, Amdam G, Halskau Ø. </i> J Exp Biol, 2012","statement":[{"text":"AmVg (336–385) retains its random values and lack of NOEs indicative of any fixed structure, a result also supported by the CD spectrum","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":336,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22573762","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q868N5","date":"2018-07-30T12:54:46.000Z","acc":"Q868N5","name":"Vitellogenin","length":1770,"organism":"Apis mellifera","dataset":[],"UniParc":"UPI000005D8AD","genes":[{"name":{"value":"Vg"}}],"alphafold_very_low_content":0.05084745762711865,"disorder_content":0.03220338983050847,"disprot_consensus":{"full":[{"start":336,"end":392,"type":"D"}],"Structural state":[{"start":336,"end":392,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00170","name":"bZIP transcription factor","start":67,"end":105},{"id":"PF08601","name":"Transcription factor PAP1","start":340,"end":646}],"gene3D":[{"start":565,"end":650,"id":"1.10.238.100","name":"YAP1 redox domain. Chain B"},{"start":58,"end":127,"id":"1.20.5.170","name":"1.20.5.170"}]},"uniref50":"UniRef50_P19880","sequence":"MSVSTAKRSLDVVSPGSLAEFEGSKSRHDEIENEHRRTGTRDGEDSEQPKKKGSKTSKKQDLDPETKQKRTAQNRAAQRAFRERKERKMKELEKKVQSLESIQQQNEVEATFLRDQLITLVNELKKYRPETRNDSKVLEYLARRDPNLHFSKNNVNHSNSEPIDTPNDDIQENVKQKMNFTFQYPLDNDNDNDNSKNVGKQLPSPNDPSHSAPMPINQTQKKLSDATDSSSATLDSLSNSNDVLNNTPNSSTSMDWLDNVIYTNRFVSGDDGSNSKTKNLDSNMFSNDFNFENQFDEQVSEFCSKMNQVCGTRQCPIPKKPISALDKEVFASSSILSSNSPALTNTWESHSNITDNTPANVIATDATKYENSFSGFGRLGFDMSANHYVVNDNSTGSTDSTGSTGNKNKKNNNNSDDVLPFISESPFDMNQVTNFFSPGSTGIGNNAASNTNPSLLQSSKEDIPFINANLAFPDDNSTNIQLQPFSESQSQNKFDYDMFFRDSSKEGNNLFGEFLEDDDDDKKAANMSDDESSLIKNQLINEEPELPKQYLQSVPGNESEISQKNGSSLQNADKINNGNDNDNDNDVVPSKEGSLLRCSEIWDRITTHPKYSDIDVDGLCSELMAKAKCSERGVVINAEDVQLALNKHMN","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P19880","disprot_id":"DP01584","ncbi_taxon_id":559292,"regions_counter":5,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":322,"region_id":"DP01584r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis for redox regulation of Yap1 transcription factor localization. <i> Wood MJ, Storz G, Tjandra N. </i> Nature, 2004","statement":[{"text":"Upon reduction of the disulphide bonds, Yap1 undergoes a change to an unstructured conformation","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":300,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1SSE"}],"reference_id":"15318225","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":322,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis for redox regulation of Yap1 transcription factor localization. <i> Wood MJ, Storz G, Tjandra N. </i> Nature, 2004","statement":[{"text":"The active oxidized form, a nuclear export signal (NES) in the carboxy-terminal cysteine-rich domain is masked by disulphide- bond-mediated interactions with a conserved amino-terminal a-helix. Upon reduction of the disulphide bonds, Yap1 undergoes a change to an unstructured conformation","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"ndavey","start":300,"term_ontology":"IDPO","curator_name":"Norman Davey","reference_id":"15318225","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01584r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":650,"region_id":"DP01584r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis for redox regulation of Yap1 transcription factor localization. <i> Wood MJ, Storz G, Tjandra N. </i> Nature, 2004","statement":[{"text":"Upon reduction of the disulphide bonds, Yap1 undergoes a change to an unstructured conformation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":565,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1SSE"}],"reference_id":"15318225","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":650,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis for redox regulation of Yap1 transcription factor localization. <i> Wood MJ, Storz G, Tjandra N. </i> Nature, 2004","statement":[{"text":"The active oxidized form, a nuclear export signal (NES) in the carboxy-terminal cysteine-rich domain is masked by disulphide- bond-mediated interactions with a conserved amino-terminal a-helix. Upon reduction of the disulphide bonds, Yap1 undergoes a change to an unstructured conformation.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"ndavey","start":565,"term_ontology":"IDPO","curator_name":"Norman Davey","reference_id":"15318225","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01584r004","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":650,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis for redox regulation of Yap1 transcription factor localization. <i> Wood MJ, Storz G, Tjandra N. </i> Nature, 2004","statement":[{"text":"The active oxidized form, a nuclear export signal (NES) in the carboxy-terminal cysteine-rich domain is masked by disulphide- bond-mediated interactions with a conserved amino-terminal a-helix.","type":"Results"}],"term_id":"GO:0060090","curator_id":"ndavey","start":565,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"15318225","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01584r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P19880","date":"2018-07-30T12:55:44.000Z","acc":"P19880","name":"AP-1-like transcription factor YAP1","length":650,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000168EFE","genes":[{"name":{"value":"YAP1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"2542125","url":"http://www.ncbi.nlm.nih.gov/pubmed/2542125","alternativeUrl":"https://europepmc.org/abstract/MED/2542125"}}]},"synonyms":[{"value":"PAR1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"1889413","url":"http://www.ncbi.nlm.nih.gov/pubmed/1889413","alternativeUrl":"https://europepmc.org/abstract/MED/1889413"}}]},{"value":"PDR4","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"2060792","url":"http://www.ncbi.nlm.nih.gov/pubmed/2060792","alternativeUrl":"https://europepmc.org/abstract/MED/2060792"}}]},{"value":"SNQ3","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"1878996","url":"http://www.ncbi.nlm.nih.gov/pubmed/1878996","alternativeUrl":"https://europepmc.org/abstract/MED/1878996"}}]}],"orfNames":[{"value":"YM9571.12"}],"olnNames":[{"value":"YML007W","evidences":[{"code":"ECO:0000312","source":{"name":"SGD","id":"S000004466","url":"https://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000004466"}}]}]}],"alphafold_very_low_content":0.6430769230769231,"disorder_content":0.1676923076923077,"disprot_consensus":{"full":[{"start":300,"end":322,"type":"T"},{"start":565,"end":650,"type":"T"}],"Structural state":[{"start":300,"end":322,"type":"D"},{"start":565,"end":650,"type":"D"}],"Structural transition":[{"start":300,"end":322,"type":"T"},{"start":565,"end":650,"type":"T"}],"Molecular function":[{"start":565,"end":650,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00812","name":"Ephrin","start":30,"end":164}],"gene3D":[{"start":24,"end":176,"id":"2.60.40.420","name":"Cupredoxins -  blue copper proteins"}]},"uniref50":"UniRef50_P52800","sequence":"MAVRRDSVWKYCWGVLMVLCRTAISKSIVLEPIYWNSSNSKFLPGQGLVLYPQIGDKLDIICPKVDSKTVGQYEYYKVYMVDKDQADRCTIKKENTPLLNCAKPDQDIKFTIKFQEFSPNLWGLEFQKNKDYYIISTSNGSLEGLDNQEGGVCQTRAMKILMKVGQDASSAGSTRNKDPTRRPELEAGTNGRSSTTSPFVKPNPGSSTDGNSAGHSGNNILGSEVALFAGIASGCIIFIVIIITLVVLLLKYRRRHRKHSPQHTTTLSLSTLATPKRSGNNNGSEPSDIIIPLRTADSVFCPHYEKVSGDYGHPVYIVQEMPPQSPANIYYKV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P52800","disprot_id":"DP01588","ncbi_taxon_id":9606,"regions_counter":6,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":300,"region_id":"DP01588r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure and backbone dynamics of the functional cytoplasmic subdomain of human ephrin B2, a cell-surface ligand with bidirectional signaling properties. <i> Song J, Vranken W, Xu P, Gingras R, Noyce RS, Yu Z, Shen SH, Ni F. </i> Biochemistry, 2002","statement":[{"text":"a detailed NMR study on the structural and dynamic properties of the cytoplasmic domain of human ephrin B2. Our results reveal the following: (1) the N-terminal region of the cytoplasmic domain from residues 253 to 300 lacks the ability for structure formation and is particularly prone to aggregation","type":"Introduction"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":253,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"12206665","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":333,"region_id":"DP01588r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure and backbone dynamics of the functional cytoplasmic subdomain of human ephrin B2, a cell-surface ligand with bidirectional signaling properties. <i> Song J, Vranken W, Xu P, Gingras R, Noyce RS, Yu Z, Shen SH, Ni F. </i> Biochemistry, 2002","statement":[{"text":"the C-terminal functional subdomain from residues 301 to 333 assumes two distinctive structural elements with residues 301-322 adopting a well-packed hairpin structure followed by a flexible C-terminal tail.","type":"Introduction"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":323,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"12206665","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":322,"region_id":"DP01588r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Tyrosine phosphorylation of the well packed ephrinB cytoplasmic beta-hairpin for reverse signaling. Structural consequences and binding properties. <i> Song J. </i> J Biol Chem, 2003","statement":[{"text":"the unphosphorylated 22-residue motif adopts a well formed beta-hairpin structure in isolation from the ephrinB cytoplasmic subdomain. However, this beta-hairpin is radically abolished by tyrosine phosphorylation, regardless of the relative location and number of Tyr residues.","type":"Introduction"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":301,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"12606549","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":322,"term_name":"order to disorder","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Tyrosine phosphorylation of the well packed ephrinB cytoplasmic beta-hairpin for reverse signaling. Structural consequences and binding properties. <i> Song J. </i> J Biol Chem, 2003","term_id":"IDPO:0000014","curator_id":"ndavey","start":301,"term_ontology":"IDPO","curator_name":"Norman Davey","reference_id":"12606549","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01588r004","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":322,"region_id":"DP01588r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Tyrosine phosphorylation of the well packed ephrinB cytoplasmic beta-hairpin for reverse signaling. Structural consequences and binding properties. <i> Song J. </i> J Biol Chem, 2003","statement":[{"text":"the present study reveals that, as shown by circular dichroism and NMR, the unphosphorylated 22-residue motif adopts a well formed beta-hairpin structure in isolation from the ephrinB cytoplasmic subdomain. However, this beta-hairpin is radically abolished by tyrosine phosphorylation, regardless of the relative location and number of Tyr residues.","type":"Introduction"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":301,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"12606549","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":322,"term_name":"order to disorder","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Tyrosine phosphorylation of the well packed ephrinB cytoplasmic beta-hairpin for reverse signaling. Structural consequences and binding properties. <i> Song J. </i> J Biol Chem, 2003","statement":[{"text":"However, this beta-hairpin is radically abolished by tyrosine phosphorylation, regardless of the relative location and number of Tyr residues.","type":"Introduction"}],"term_id":"IDPO:0000014","curator_id":"ndavey","start":301,"term_ontology":"IDPO","curator_name":"Norman Davey","reference_id":"12606549","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01588r006","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_P52799","date":"2018-07-30T12:56:38.000Z","acc":"P52799","name":"Ephrin-B2","length":333,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000129C9B","genes":[{"name":{"value":"EFNB2"},"synonyms":[{"value":"EPLG5"},{"value":"HTKL"},{"value":"LERK5"}]}],"alphafold_very_low_content":0.3153153153153153,"disorder_content":0.24324324324324326,"disprot_consensus":{"full":[{"start":253,"end":300,"type":"D"},{"start":301,"end":322,"type":"T"},{"start":323,"end":333,"type":"D"}],"Structural state":[{"start":253,"end":333,"type":"D"}],"Structural transition":[{"start":301,"end":322,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00498","name":"FHA domain","start":78,"end":140}],"gene3D":[{"start":24,"end":159,"id":"2.60.200.20","name":"2.60.200.20"}]},"uniref50":"UniRef50_A0QYG2","sequence":"MTDMNPDIEKDQTSDEVTVETTSVFRADFLSELDAPAQAGTESAVSGVEGLPPGSALLVVKRGPNAGSRFLLDQAITSAGRHPDSDIFLDDVTVSRRHAEFRLENNEFNVVDVGSLNGTYVNREPVDSAVLANGDEVQIGKFRLVFLTGPKQGEDDGSTGGP","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"uniref90":"UniRef90_P9WJA8","disprot_id":"DP01589","ncbi_taxon_id":83332,"regions_counter":8,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":18,"region_id":"DP01589r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"An intramolecular switch regulates phosphoindependent FHA domain interactions in Mycobacterium tuberculosis. <i> Nott TJ, Kelly G, Stach L, Li J, Westcott S, Patel D, Hunt DM, Howell S, Buxton RS, O'Hare HM, Smerdon SJ. </i> Sci Signal, 2009","statement":[{"text":"The extreme N-terminal (residues 1 to 18) and C-terminal (residues 150 to 162) regions were not defined and have been omitted for clarity.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":1,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19318624","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":33,"region_id":"DP01589r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"An intramolecular switch regulates phosphoindependent FHA domain interactions in Mycobacterium tuberculosis. <i> Nott TJ, Kelly G, Stach L, Li J, Westcott S, Patel D, Hunt DM, Howell S, Buxton RS, O'Hare HM, Smerdon SJ. </i> Sci Signal, 2009","statement":[{"text":"Rather than acting to tether a disordered N-terminal region, phosphorylation of Thr22 appears to stabilize a preexisting but low-occupancy association of residues 21 to 30 with the FHA domain. Amino acid residues 21 to 33 adopted an extended conformation that encompassed a short region with helical propensity","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":19,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19318624","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":33,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"An intramolecular switch regulates phosphoindependent FHA domain interactions in Mycobacterium tuberculosis. <i> Nott TJ, Kelly G, Stach L, Li J, Westcott S, Patel D, Hunt DM, Howell S, Buxton RS, O'Hare HM, Smerdon SJ. </i> Sci Signal, 2009","statement":[{"text":"We therefore propose that, rather than acting to tether a disordered N-terminal region, phosphorylation of Thr22 appears to sta- bilize a preexisting but low-occupancy association of residues 21 to 30 with the FHA domain.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"ndavey","start":19,"term_ontology":"IDPO","curator_name":"Norman Davey","reference_id":"19318624","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01589r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":33,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"An intramolecular switch regulates phosphoindependent FHA domain interactions in Mycobacterium tuberculosis. <i> Nott TJ, Kelly G, Stach L, Li J, Westcott S, Patel D, Hunt DM, Howell S, Buxton RS, O'Hare HM, Smerdon SJ. </i> Sci Signal, 2009","statement":[{"text":"hese data suggest a mechanism for the regulation of intermolecular interactions of Rv1827 through intramolecular binding of its N-terminal region to the FHA domain after phosphorylation at either Thr21 or Thr22 by PknG or PknB","type":"Results"}],"term_id":"GO:0005515","curator_id":"ndavey","start":19,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"19318624","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01589r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":33,"term_name":"phosphorylation display site","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"An intramolecular switch regulates phosphoindependent FHA domain interactions in Mycobacterium tuberculosis. <i> Nott TJ, Kelly G, Stach L, Li J, Westcott S, Patel D, Hunt DM, Howell S, Buxton RS, O'Hare HM, Smerdon SJ. </i> Sci Signal, 2009","statement":[{"text":"these data suggest a mechanism for the regulation of intermolecular interactions of Rv1827 through intramolecular binding of its N-terminal region to the FHA domain after phosphorylation at either Thr21 or Thr22 by PknG or PknB,","type":"Results"}],"term_id":"IDPO:0000045","curator_id":"ndavey","start":19,"term_ontology":"IDPO","curator_name":"Norman Davey","reference_id":"19318624","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01589r005","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":33,"term_name":"molecular function inhibitor activity","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"An intramolecular switch regulates phosphoindependent FHA domain interactions in Mycobacterium tuberculosis. <i> Nott TJ, Kelly G, Stach L, Li J, Westcott S, Patel D, Hunt DM, Howell S, Buxton RS, O'Hare HM, Smerdon SJ. </i> Sci Signal, 2009","statement":[{"text":"Intramolecular interactions regulate the binding of Rv1827 to target enzymes","type":"Results"}],"term_id":"GO:0140678","curator_id":"ndavey","start":19,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"19318624","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01589r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":54,"region_id":"DP01589r007","released":"2022_03","ec_id":"ECO:0006165","reference_html":"An intramolecular switch regulates phosphoindependent FHA domain interactions in Mycobacterium tuberculosis. <i> Nott TJ, Kelly G, Stach L, Li J, Westcott S, Patel D, Hunt DM, Howell S, Buxton RS, O'Hare HM, Smerdon SJ. </i> Sci Signal, 2009","statement":[{"text":"Regions of high mobility were apparent at the N- and C-termini and at the region corresponding to amino acid residues 34 to 54","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":34,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19318624","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":162,"region_id":"DP01589r008","released":"2022_03","ec_id":"ECO:0006165","reference_html":"An intramolecular switch regulates phosphoindependent FHA domain interactions in Mycobacterium tuberculosis. <i> Nott TJ, Kelly G, Stach L, Li J, Westcott S, Patel D, Hunt DM, Howell S, Buxton RS, O'Hare HM, Smerdon SJ. </i> Sci Signal, 2009","statement":[{"text":"The extreme N-terminal (residues 1 to 18) and C-terminal (residues 150 to 162) regions were not defined and have been omitted for clarity.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":150,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19318624","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P9WJA8","date":"2018-07-30T12:56:47.000Z","acc":"P9WJA9","name":"Glycogen accumulation regulator GarA","length":162,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","dataset":[],"UniParc":"UPI000013B319","genes":[{"name":{"value":"garA"},"orfNames":[{"value":"MTCY1A11.16c"}],"olnNames":[{"value":"Rv1827"}]}],"alphafold_very_low_content":0.2345679012345679,"disorder_content":0.41358024691358025,"disprot_consensus":{"full":[{"start":1,"end":18,"type":"D"},{"start":19,"end":33,"type":"T"},{"start":34,"end":54,"type":"D"},{"start":150,"end":162,"type":"D"}],"Structural state":[{"start":1,"end":54,"type":"D"},{"start":150,"end":162,"type":"D"}],"Structural transition":[{"start":19,"end":33,"type":"T"}],"Molecular function":[{"start":19,"end":33,"type":"F"}],"Disorder function":[{"start":19,"end":33,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00013","name":"KH domain","start":146,"end":209},{"id":"PF00013","name":"KH domain","start":236,"end":301},{"id":"PF00013","name":"KH domain","start":327,"end":387},{"id":"PF00013","name":"KH domain","start":427,"end":493},{"id":"PF09005","name":"Far upstream element-binding protein, C-terminal","start":611,"end":632},{"id":"PF09005","name":"Far upstream element-binding protein, C-terminal","start":670,"end":685}],"gene3D":[{"start":421,"end":503,"id":"3.30.1370.10","name":"K Homology domain, type 1"},{"start":221,"end":305,"id":"3.30.1370.10","name":"K Homology domain, type 1"},{"start":313,"end":418,"id":"3.30.1370.10","name":"K Homology domain, type 1"},{"start":130,"end":218,"id":"3.30.1370.10","name":"K Homology domain, type 1"}]},"uniref50":"UniRef50_Q92945","sequence":"MSDYSTGGPPPGPPPPAGGGGGAGGAGGGPPPGPPGAGDRGGGGPGGGGPGGGSAGGPSQPPGGGGPGIRKDAFADAVQRARQIAAKIGGDAATTVNNSTPDFGFGGQKRQLEDGDQPESKKLASQGDSISSQLGPIHPPPRTSMTEEYRVPDGMVGLIIGRGGEQINKIQQDSGCKVQISPDSGGLPERSVSLTGAPESVQKAKMMLDDIVSRGRGGPPGQFHDNANGGQNGTVQEIMIPAGKAGLVIGKGGETIKQLQERAGVKMILIQDGSQNTNVDKPLRIIGDPYKVQQACEMVMDILRERDQGGFGDRNEYGSRIGGGIDVPVPRHSVGVVIGRSGEMIKKIQNDAGVRIQFKQDDGTGPEKIAHIMGPPDRCEHAARIINDLLQSLRSGPPGPPGGPGMPPGGRGRGRGQGNWGPPGGEMTFSIPTHKCGLVIGRGGENVKAINQQTGAFVEISRQLPPNGDPNFKLFIIRGSPQQIDHAKQLIEEKIEGPLCPVGPGPGGPGPAGPMGPFNPGPFNQGPPGAPPHAGGPPPHQYPPQGWGNTYPQWQPPAPHDPSKAAAAAADPNAAWAAYYSHYYQQPPGPVPGPAPAPAAPPAQGEPPQPPPTGQSDYTKAWEEYYKKIGQQPQQPGAPPQQDYTKAWEEYYKKQAQVATGGGPGAPPGSQPDYSAAWAEYYRQQAAYYGQTPGPGGPQPPPTQQGQQQAQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q92945","disprot_id":"DP01590","ncbi_taxon_id":9606,"regions_counter":5,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":218,"region_id":"DP01590r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding. <i> Díaz-Moreno I, Hollingworth D, Frenkiel TA, Kelly G, Martin S, Howell S, García-Mayoral M, Gherzi R, Briata P, Ramos A. </i> Nat Struct Mol Biol, 2009","statement":[{"text":"igh-sensitivity SOFAST 15N-1H HMQC spectra28 were recorded on samples from the two HPLC peaks (Fig. 4a): the two spectra clearly show that the nonphosphorylated protein is folded, whereas the phosphorylated protein is essentially unfolded.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":130,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2OPU"}],"reference_id":"19198587","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":218,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding. <i> Díaz-Moreno I, Hollingworth D, Frenkiel TA, Kelly G, Martin S, Howell S, García-Mayoral M, Gherzi R, Briata P, Ramos A. </i> Nat Struct Mol Biol, 2009","statement":[{"text":"igh-sensitivity SOFAST 15N-1H HMQC spectra28 were recorded on samples from the two HPLC peaks (Fig. 4a): the two spectra clearly show that the nonphosphorylated protein is folded, whereas the phosphorylated protein is essentially unfolded.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"ndavey","start":130,"term_ontology":"IDPO","curator_name":"Norman Davey","reference_id":"19198587","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01590r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":218,"region_id":"DP01590r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding. <i> Díaz-Moreno I, Hollingworth D, Frenkiel TA, Kelly G, Martin S, Howell S, García-Mayoral M, Gherzi R, Briata P, Ramos A. </i> Nat Struct Mol Biol, 2009","statement":[{"text":"We confirmed the folding state of phospho-KH1 by recording CD spectra at different temperatures","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":130,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19198587","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":218,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding. <i> Díaz-Moreno I, Hollingworth D, Frenkiel TA, Kelly G, Martin S, Howell S, García-Mayoral M, Gherzi R, Briata P, Ramos A. </i> Nat Struct Mol Biol, 2009","statement":[{"text":"igh-sensitivity SOFAST 15N-1H HMQC spectra28 were recorded on samples from the two HPLC peaks (Fig. 4a): the two spectra clearly show that the nonphosphorylated protein is folded, whereas the phosphorylated protein is essentially unfolded.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"ndavey","start":130,"term_ontology":"IDPO","curator_name":"Norman Davey","reference_id":"19198587","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01590r004","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":218,"term_name":"protein folding chaperone","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding. <i> Díaz-Moreno I, Hollingworth D, Frenkiel TA, Kelly G, Martin S, Howell S, García-Mayoral M, Gherzi R, Briata P, Ramos A. </i> Nat Struct Mol Biol, 2009","statement":[{"text":"Our data indicate that phosphorylation of KH1 unfolds the domain and creates a site for 14-3-3ζ binding.","type":"Results"}],"term_id":"GO:0044183","curator_id":"ndavey","start":130,"term_ontology":"GO","curator_name":"Norman Davey","reference_id":"19198587","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01590r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q92945","date":"2018-07-30T12:56:54.000Z","acc":"Q92945","name":"Far upstream element-binding protein 2","length":711,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000006FE0F","genes":[{"name":{"value":"KHSRP"},"synonyms":[{"value":"FUBP2"}]}],"alphafold_very_low_content":0.44022503516174405,"disorder_content":0.12517580872011252,"disprot_consensus":{"full":[{"start":130,"end":218,"type":"T"}],"Structural state":[{"start":130,"end":218,"type":"D"}],"Structural transition":[{"start":130,"end":218,"type":"T"}],"Molecular function":[{"start":130,"end":218,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01789","name":"PsbP","start":96,"end":263}],"gene3D":[{"start":80,"end":265,"id":"3.40.1000.10","name":"Mog1/PsbP, alpha/beta/alpha sandwich"}]},"uniref50":"UniRef50_Q42029","sequence":"MASTQCFLHHHALSTPARTPLVRSIVPSLKPNQLLVCRAQKQSAPQEDNVNSVSVSRRLALTVLIGAAAVGSKVSPADAAYGEAANVFGKPKTDTDFQTYNGDGFKLQIPSKWNPNKEVEYPGQVLRFEDNFDATSNVIVAITPTDKKSITDFGSPEQFLSQVDYLLGRQAYSGKTDSEGGFESDAVAIANVLETSSAEVGGKPYYYLSVLTRTADGNEGGKHQLITATVNDGKLYICKAQAGDKRWFKGAKKFVENTATSFSLA","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","lamiids","Solanales","Solanaceae","Nicotianoideae","Nicotianeae","Nicotiana"],"uniref90":"UniRef90_P18212","disprot_id":"DP01591","ncbi_taxon_id":4097,"regions_counter":1,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":186,"region_id":"DP01591r001","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Crystal structure of the PsbP protein of photosystem II from Nicotiana tabacum. <i> Ifuku K, Nakatsu T, Kato H, Sato F. </i> EMBO Rep, 2004","statement":[{"text":"Fig 1 shows part of the final 1.6-Å-resolution 2Fo – Fc electron-density map. The electron densities of the N-terminal portion (residues 10–15) and two loop regions (residues 91–107 and 138–140) were not seen in the model because of disorder. ","type":"Results"},{"text":"Loop region 91-107 corresponds to 170-186 region in Uniprot.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":170,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-24T17:36:44.089Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1V2B"}],"reference_id":"15031714","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17925","entry_name":"alpha-D-glucose"}]}],"released":"2018_11","uniref100":"UniRef100_P18212","date":"2018-07-30T13:17:40.000Z","acc":"P18212","name":"Oxygen-evolving enhancer protein 2-2, chloroplastic","length":265,"organism":"Nicotiana tabacum","dataset":[],"UniParc":"UPI0000132736","genes":[{"name":{"value":"PSBP2"},"synonyms":[{"value":"OEE2-B"},{"value":"PSBP"}]}],"alphafold_very_low_content":0.25660377358490566,"disorder_content":0.06415094339622641,"disprot_consensus":{"full":[{"start":170,"end":186,"type":"D"}],"Structural state":[{"start":170,"end":186,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00036","name":"EF hand domain","start":129,"end":157},{"id":"PF13499","name":"EF-hand domain pair","start":206,"end":266}],"gene3D":[{"start":120,"end":190,"id":"1.10.238.10","name":"EF-hand"},{"start":192,"end":271,"id":"1.10.238.10","name":"EF-hand"}]},"uniref50":"UniRef50_Q8VHC5","sequence":"MATEHNVQLVPGSQKIPKGVVSPRSAAEGPALTRRRSKKESWHPGSQKASSGDQSSSQGSEASGSSKHPPRTKVGQEEPSSAPARPASHRHSHRHRSDPQQDAAQRTYGPLLNRMFGKDRELGPEELEELQAAFEEFDTDQDGYIGYRELGDCMRTLGYMPTEMELLEVSQHVKMRMGGFVDFEEFVELISPKLREETAHMLGVRELRIAFREFDKDRDGRITVAELRQAAPALLGEPLEGTELDEMLREMDLNGDGTIDFDEFVMMLSTG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q8VHC5","disprot_id":"DP01592","ncbi_taxon_id":10090,"regions_counter":1,"creator":"nfoutel","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":120,"region_id":"DP01592r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"¹H, ¹⁵N, and ¹³C chemical shift assignments of murine calcium-binding protein 4. <i> Park S, Li C, Ames JB. </i> Biomol NMR Assign, 2014","statement":[{"text":"The first 20 residues from the amino-terminus (residues 100–120), residues 177–178 (EF2 loop), and residues 192–195 (domain linker) all exhibited weak NMR signals with random coil chemical shifts, indicative of structural disorder in these regions.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":100,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"23925854","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q8VHC5","date":"2018-07-30T13:26:30.000Z","acc":"Q8VHC5","name":"Calcium-binding protein 4","length":271,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000022460","genes":[{"name":{"value":"Cabp4"}}],"alphafold_very_low_content":0.23616236162361623,"disorder_content":0.07749077490774908,"disprot_consensus":{"full":[{"start":100,"end":120,"type":"D"}],"Structural state":[{"start":100,"end":120,"type":"D"}]}},{"features":{"pfam":[{"id":"PF06246","name":"Isy1-like splicing family","start":1,"end":231}],"gene3D":[{"start":43,"end":98,"id":"1.10.287.660","name":"Helix hairpin bin"}]},"uniref50":"UniRef50_P21374","sequence":"MSRNVDKANSVLVRFQEQQAESAGGYKDYSRYQRPRNVSKVKSIKEANEWKRQVSKEIKQKSTRIYDPSLNEMQIAELNDELNNLFKEWKRWQWHIDHTLMEKKTKRKRLEDSHVLMNSGKLINGKRYFGRALELPEVKEWLKQSQRQNDGGSINTKCIPKDRNDFYYHGKVTAALTEFEANWTSILKAHYNVPVNEDEEEMSRQTQEIHVPTLADMEHWLVQRRKKKLMDELNL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P21374","disprot_id":"DP01593","ncbi_taxon_id":559292,"regions_counter":2,"creator":"nfoutel","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":235,"region_id":"DP01593r001","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Structure of a yeast catalytic step I spliceosome at 3.4 Å resolution. <i> Wan R, Yan C, Bai R, Huang G, Shi Y. </i> Science, 2016","statement":[{"text":"The authors could not solve the structure for this region in the Cryo-EM experiment, probably due to poor electron density  expected for a disordered region.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":97,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"27445308","version":2,"ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":235,"region_id":"DP01593r002","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Cryo-EM structure of the spliceosome immediately after branching. <i> Galej WP, Wilkinson ME, Fica SM, Oubridge C, Newman AJ, Nagai K. </i> Nature, 2016","statement":[{"text":"The authors could not solve the structure for this region in the Cryo-EM experiment, probably due to poor electron density  expected for a disordered region.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":96,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"27459055","version":2,"ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P21374","date":"2018-07-30T14:47:38.000Z","acc":"P21374","name":"Pre-mRNA-splicing factor ISY1","length":235,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000168B93","genes":[{"name":{"value":"ISY1"},"synonyms":[{"value":"NTC30"},{"value":"UTR3"}],"orfNames":[{"value":"J1657"}],"olnNames":[{"value":"YJR050W"}]}],"alphafold_very_low_content":0.00425531914893617,"disorder_content":0.5957446808510638,"disprot_consensus":{"full":[{"start":96,"end":235,"type":"D"}],"Structural state":[{"start":96,"end":235,"type":"D"}]}},{"features":{"pfam":[{"id":"PF09468","name":"Ydr279p protein family (RNase H2 complex component) wHTH domain","start":95,"end":225},{"id":"PF17745","name":"Ydr279p protein triple barrel domain","start":28,"end":92}],"gene3D":[{"start":91,"end":230,"id":"1.10.20.120","name":"1.10.20.120"},{"start":11,"end":90,"id":"2.20.25.530","name":"2.20.25.530"}]},"uniref50":"UniRef50_Q80ZV0","sequence":"MAGGRDRGDLAARQLVFLLPEHLKDASKKKKKSSLLFVKLANPHSGEGATYLIDMCLQQLFEIKVFKEKHHSWFINQSVQSGGLLHFATPMDPLFLLLHYLLKAGKEGKYQPLDQVVVDDTFPDCTLLLRFPELEKSLRHVTEEKEVNSKKYYKYSSEKTLKWLEKKVNQTVVALKANNVNVGARVQSSAYFSGGQVSRDKEEDYVRYAHGLISDYIPKELSDDLSKFLKLPEPPASLTNPPSKKLKLSDEPVEAKEDYTKFNTKDLKTGKKNSKMTAAQKALAKVDKSGMKSIDAFFGAKNKKTGKI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q80ZV0","disprot_id":"DP01594","ncbi_taxon_id":10090,"regions_counter":5,"creator":"nfoutel","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":145,"region_id":"DP01594r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The structure of the mammalian RNase H2 complex provides insight into RNA.NA hybrid processing to prevent immune dysfunction. <i> Shaban NM, Harvey S, Perrino FW, Hollis T. </i> J Biol Chem, 2010","statement":[{"text":"The authors could not solve the structure for this region in the X-ray experiment, probably due to poor electron density expected for a disordered region","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":103,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"19923215","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":122,"region_id":"DP01594r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The structure of the human RNase H2 complex defines key interaction interfaces relevant to enzyme function and human disease. <i> Reijns MA, Bubeck D, Gibson LC, Graham SC, Baillie GS, Jones EY, Jackson AP. </i> J Biol Chem, 2011","statement":[{"text":"The authors could not solve the structure for this region in the X-ray experiment, probably due to poor electron density expected for a disordered region","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":107,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"21177854","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":202,"region_id":"DP01594r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The structure of the human RNase H2 complex defines key interaction interfaces relevant to enzyme function and human disease. <i> Reijns MA, Bubeck D, Gibson LC, Graham SC, Baillie GS, Jones EY, Jackson AP. </i> J Biol Chem, 2011","statement":[{"text":"The authors could not solve the structure for this region in the X-ray experiment, probably due to poor electron density expected for a disordered region","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":182,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"21177854","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":308,"region_id":"DP01594r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The structure of the mammalian RNase H2 complex provides insight into RNA.NA hybrid processing to prevent immune dysfunction. <i> Shaban NM, Harvey S, Perrino FW, Hollis T. </i> J Biol Chem, 2010","statement":[{"text":"The authors could not solve the structure for this region in the X-ray experiment, probably due to poor electron density expected for a disordered region","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":283,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"19923215","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":266,"region_id":"DP01594r005","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The structure of the mammalian RNase H2 complex provides insight into RNA.NA hybrid processing to prevent immune dysfunction. <i> Shaban NM, Harvey S, Perrino FW, Hollis T. </i> J Biol Chem, 2010","statement":[{"text":"The authors could not solve the structure for this region in the X-ray experiment, probably due to poor electron density expected for a disordered region","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":182,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"19923215","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q80ZV0","date":"2018-07-30T15:49:30.000Z","acc":"Q80ZV0","name":"Ribonuclease H2 subunit B","length":308,"organism":"Mus musculus","dataset":[],"UniParc":"UPI000005FB58","genes":[{"name":{"value":"Rnaseh2b"},"synonyms":[{"value":"Dleu8"}]}],"alphafold_very_low_content":0.14285714285714285,"disorder_content":0.5,"disprot_consensus":{"full":[{"start":103,"end":145,"type":"D"},{"start":182,"end":266,"type":"D"},{"start":283,"end":308,"type":"D"}],"Structural state":[{"start":103,"end":145,"type":"D"},{"start":182,"end":266,"type":"D"},{"start":283,"end":308,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00046","name":"Homeodomain","start":147,"end":203}],"gene3D":[{"start":113,"end":206,"id":"1.10.10.60","name":"Homeodomain-like"}]},"uniref50":"UniRef50_P52946","sequence":"MNGEEQYYAATQLYKDPCAFQRGPAPEFSASPPACLYMGRQPPPPPPHPFPGALGALEQGSPPDISPYEVPPLADDPAVAHLHHHLPAQLALPHPPAGPFPEGAEPGVLEEPNRVQLPFPWMKSTKAHAWKGQWAGGAYAAEPEENKRTRTAYTRAQLLELEKEFLFNKYISRPRRVELAVMLNLTERHIKIWFQNRRMKWKKEEDKKRGGGTAVGGGGVAEPEQDCAVTSGEELLALPPPPPPGGAVPPAAPVAAREGRLPPGLSASPQPSSVAPRRPQEPR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P52945","disprot_id":"DP01597","ncbi_taxon_id":9606,"regions_counter":1,"creator":"tszani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":283,"region_id":"DP01597r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Generating NMR chemical shift assignments of intrinsically disordered proteins using carbon-detected NMR methods. <i> Sahu D, Bastidas M, Showalter SA. </i> Anal Biochem, 2014","term_id":"IDPO:0000002","curator_id":"tszani","start":204,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24333248","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P52945","date":"2018-07-31T09:15:37.000Z","acc":"P52945","name":"Pancreas/duodenum homeobox protein 1","length":283,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012D7D9","genes":[{"name":{"value":"PDX1"},"synonyms":[{"value":"IPF1"},{"value":"STF1"}]}],"alphafold_very_low_content":0.254416961130742,"disorder_content":0.2826855123674912,"disprot_consensus":{"full":[{"start":204,"end":283,"type":"D"}],"Structural state":[{"start":204,"end":283,"type":"D"}]}},{"features":{"pfam":[{"id":"PF05871","name":"ESCRT-II complex subunit","start":10,"end":145}],"gene3D":[{"start":1,"end":99,"id":"1.10.10.570","name":"\"Winged helix\" DNA-binding domain. Chain C. Domain 1"},{"start":100,"end":176,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}]},"uniref50":"UniRef50_Q9BRG1","sequence":"MAMSFEWPWQYRFPPFFTLQPNVDTRQKQLAAWCSLVLSFCRLHKQSSMTVMEAQESPLFNNVKLQRKLPVESIQIVLEELRKKGNLEWLDKSKSSFLIMWRRPEEWGKLIYQWVSRSGQNNSVFTLYELTNGEDTEDEEFHGLDEATLLRALQALQQEHKAEIITVSDGRGVKFF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9BRG1","disprot_id":"DP01598","ncbi_taxon_id":9606,"regions_counter":1,"creator":"nfoutel","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":145,"region_id":"DP01598r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure and function of the ESCRT-II-III interface in multivesicular body biogenesis. <i> Im YJ, Wollert T, Boura E, Hurley JH. </i> Dev Cell, 2009","term_id":"IDPO:0000002","curator_id":"nfoutel","start":133,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"19686684","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9BRG1","date":"2018-07-31T09:19:12.000Z","acc":"Q9BRG1","name":"Vacuolar protein-sorting-associated protein 25","length":176,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000728F2","genes":[{"name":{"value":"VPS25"},"synonyms":[{"value":"DERP9"},{"value":"EAP20"}]}],"alphafold_very_low_content":0.011363636363636364,"disorder_content":0.07386363636363637,"disprot_consensus":{"full":[{"start":133,"end":145,"type":"D"}],"Structural state":[{"start":133,"end":145,"type":"D"}]}},{"features":{"pfam":[{"id":"PF05871","name":"ESCRT-II complex subunit","start":7,"end":169}],"gene3D":[{"start":126,"end":202,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"start":1,"end":125,"id":"1.10.10.570","name":"\"Winged helix\" DNA-binding domain. Chain C. Domain 1"}]},"uniref50":"UniRef50_P47142","sequence":"MSALPPVYSFPPLYTRQPNSLTRRQQISTWIDIISQYCKTKKIWYMSVDGTVINDNELDSGSTDNDDSKKISKNLFNNEDIQRSVSQVFIDEIWSQMTKEGKCLPIDQSGRRSSNTTTTRYFILWKSLDSWASLILQWFEDSGKLNQVITLYELSEGDETVNWEFHRMPESLLYYCLKPLCDRNRATMLKDENDKVIAIKVV","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P47142","disprot_id":"DP01599","ncbi_taxon_id":559292,"regions_counter":3,"creator":"nfoutel","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":71,"region_id":"DP01599r001","released":"2024_06","ec_id":"ECO:0006220","reference_html":"ESCRT-II, an endosome-associated complex required for protein sorting: crystal structure and interactions with ESCRT-III and membranes. <i> Teo H, Perisic O, González B, Williams RL. </i> Dev Cell, 2004","statement":[{"text":"Following strand β1, there is a β-hairpin encompassing residues 50–74 with residues 55–71 not visible. Given that there are no unambiguous experimental sequence markers in this region (no Met and no Cys residues), there is some uncertainty of the sequence register in the 50–79 region of Vps25 WHA. The region from 55 to 74 represents an insertion in the yeast Vps25 relative to other species, so that the 50–74 β-hairpin may be unique to S. cerevisiae.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":55,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15469844","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2024-02-08T15:16:01.242Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q06696"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q12483"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":70,"region_id":"DP01599r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the ESCRT-II endosomal trafficking complex. <i> Hierro A, Sun J, Rusnak AS, Kim J, Prag G, Emr SD, Hurley JH. </i> Nature, 2004","statement":[{"text":"Vps25 is the most flexible of the three subunits. Flexible internal loops between residues 56–70, 110–115, 146–149 and 162–164, as well as the C-terminal ten residues, could not be visualized in electron density.","type":"Article"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":56,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"15329733","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-02-08T15:14:14.526Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":72,"region_id":"DP01599r003","released":"2024_06","ec_id":"ECO:0006220","reference_html":"Crystal structure of subunit VPS25 of the endosomal trafficking complex ESCRT-II. <i> Wernimont AK, Weissenhorn W. </i> BMC Struct Biol, 2004","statement":[{"text":"It lacks canonical helix 2, which instead folds into a large disordered loop followed by strands 3 and 4 that connects to helix 2 (at the corresponding position of canonical helix 3).","type":"Results"},{"text":"The final model lacks two to five flexible loops (molecule mol A, residues 56–72, 114–115, 156–157; mol B, residues 53–73, 157–158; mol C, residues 57–72, 155–158; mol D, residues 19–21, 55–73, 107–120, 156–160, 185–186).","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":56,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15579210","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2024-02-08T15:13:11.657Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"1XB4"}],"curator_orcid":"0000-0001-8399-7907"}],"released":"2018_11","uniref100":"UniRef100_P47142","date":"2018-07-31T09:36:18.000Z","acc":"P47142","name":"Vacuolar protein-sorting-associated protein 25","length":202,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000013B4D1","genes":[{"name":{"value":"VPS25"},"synonyms":[{"value":"VPT25"}],"orfNames":[{"value":"J1957"}],"olnNames":[{"value":"YJR102C"}]}],"alphafold_very_low_content":0.06930693069306931,"disorder_content":0.0891089108910891,"disprot_consensus":{"full":[{"start":55,"end":72,"type":"D"}],"Structural state":[{"start":55,"end":72,"type":"D"}]}},{"features":{"pfam":[{"id":"PF09013","name":"YopH, N-terminal","start":14,"end":111}],"gene3D":[{"start":2,"end":115,"id":"3.30.1570.10","name":"Protein-tyrosine phosphatase, YopH, N-terminal domain"}]},"uniref50":"UniRef50_Q01254","sequence":"MGSIMKINDLKSLISMQIAEFGGGEKIGRLKSTLQQVSTQAITSDERRFAYAVLEHAKNTILNRQDVAKLLPRASNFELSQGKKGEVILKGLRVEQLSLEDAKLLLDAVTRKMQKL","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"],"uniref90":"UniRef90_Q93KQ4","disprot_id":"DP01600","ncbi_taxon_id":630,"regions_counter":1,"creator":"tszani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":81,"region_id":"DP01600r001","released":"2025_06","ec_id":"ECO:0006220","reference_html":"Structure of the Yersinia pestis type III secretion chaperone SycH in complex with a stable fragment of YscM2. <i> Phan J, Tropea JE, Waugh DS. </i> Acta Crystallogr D Biol Crystallogr, 2004","term_id":"IDPO:0000002","curator_id":"tcordero","start":51,"term_ontology":"IDPO","curator_name":"Trinidad Cordero","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0003-4991-7170","date":"2025-02-03T09:43:15.465Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1TTW"}],"reference_id":"15333930","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Residues 51-81 of the YscM2(33-81) polypeptide are disordered in the crystal and only the side chains in the α-helical segment could be assigned with confidence.","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q7BTX0"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-03T12:59:49.655Z"}}],"released":"2025_06","uniref100":"UniRef100_Q93KQ4","date":"2018-07-31T09:38:29.000Z","acc":"Q93KQ4","name":"Regulatory protein YscM2","length":116,"organism":"Yersinia enterocolitica","dataset":["Bacterial virulence-related proteins"],"UniParc":"UPI00000051A1","genes":[{"name":{"value":"yscM2","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAK69250.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAK69250.1"}}]}}],"alphafold_very_low_content":0.08620689655172414,"disorder_content":0.2672413793103448,"disprot_consensus":{"full":[{"start":51,"end":81,"type":"D"}],"Structural state":[{"start":51,"end":81,"type":"D"}]}},{"features":{"pfam":[{"id":"PF11835","name":"RRM-like domain","start":178,"end":258},{"id":"PF13893","name":"RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain)","start":81,"end":144},{"id":"PF13893","name":"RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain)","start":338,"end":459},{"id":"PF22976","name":"RRM domain","start":474,"end":544}],"gene3D":[{"start":180,"end":285,"id":"3.30.70.330","name":"3.30.70.330"},{"start":41,"end":163,"id":"3.30.70.330","name":"3.30.70.330"},{"start":443,"end":531,"id":"3.30.70.330","name":"3.30.70.330"},{"start":324,"end":431,"id":"3.30.70.330","name":"3.30.70.330"}]},"uniref50":"UniRef50_P26599","sequence":"MDGIVPDIAVGTKRGSDELFSTCVTNGPFIMSSNSASAANGNDSKKFKGDSRSAGVPSRVIHIRKLPIDVTEGEVISLGLPFGKVTNLLMLKGKNQAFIEMNTEEAANTMVNYYTSVTPVLRGQPIYIQFSNHKELKTDSSPNQARAQAALQAVNSVQSGNLALAASAAAVDAGMAMAGQSPVLRIIVENLFYPVTLDVLHQIFSKFGTVLKIITFTKNNQFQALLQYADPVSAQHAKLSLDGQNIYNACCTLRIDFSKLTSLNVKYNNDKSRDYTRPDLPSGDSQPSLDQTMAAAFGAPGIISASPYAGAGFPPTFAIPQAAGLSVPNVHGALAPLAIPSAAAAAAAAGRIAIPGLAGAGNSVLLVSNLNPERVTPQSLFILFGVYGDVQRVKILFNKKENALVQMADGNQAQLAMSHLNGHKLHGKPIRITLSKHQNVQLPREGQEDQGLTKDYGNSPLHRFKKPGSKNFQNIFPPSATLHLSNIPPSVSEEDLKVLFSSNGGVVKGFKFFQKDRKMALIQMGSVEEAVQALIDLHNHDLGENHHLRVSFSKSTI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P26599","disprot_id":"DP01601","ncbi_taxon_id":9606,"regions_counter":8,"creator":"bhajdu","regions":[{"region_id":"DP01601r001","ec_ontology":"ECO","end":425,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":409,"version":3,"statement":[{"text":"This loop (residues 409–425) appears to be very mobile and is unstructured apart from a single helical turn close to the start of β5. In our construct the linker makes no observable contact with the rest of the protein; however, it is positioned above the RNA binding surface and may play a role in RNA recognition (see below).","type":"Results"}],"term_name":"disorder","reference_html":"Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM fold. <i> Conte MR, Grüne T, Ghuman J, Kelly G, Ladas A, Matthews S, Curry S. </i> EMBO J, 2000","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10856256","date":"2023-12-05T15:51:10.566Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1QM9"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"MGNSVLLVSNLNPERVTPQSLFILFGVYGDVQRVKILFNKKENALVQMADGNQAQLAMSHLNGHKLHGKPIRITLSKHQNVQLPREGQEDQGLTKDYGNSPLHRFKKPGSKNFQNIFPPSATLHLSNIPPSVSEEDLKVLFSSNGGVVKGFKFFQKDRKMALIQMGSVEEAVQALIDLHNHDLGENHHLRVSFSKSTI","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:11:11.648Z"}},{"region_id":"DP01601r003","ec_ontology":"ECO","end":454,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":431,"version":3,"statement":[{"text":"PTB-34 has a tandem domain structure in which the RRMs are tethered by a linker peptide of 25 residues in length. While the conformations of the secondary structural elements within RRMs 3 and 4 are well defined, the inter-domain linker region of PTB-34 was mostly unassigned (Conte et al., 1999).","type":"Results"}],"term_name":"disorder","reference_html":"Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM fold. <i> Conte MR, Grüne T, Ghuman J, Kelly G, Ladas A, Matthews S, Curry S. </i> EMBO J, 2000","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10856256","date":"2023-08-29T16:53:53.274Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1QM9"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"MGNSVLLVSNLNPERVTPQSLFILFGVYGDVQRVKILFNKKENALVQMADGNQAQLAMSHLNGHKLHGKPIRITLSKHQNVQLPREGQEDQGLTKDYGNSPLHRFKKPGSKNFQNIFPPSATLHLSNIPPSVSEEDLKVLFSSNGGVVKGFKFFQKDRKMALIQMGSVEEAVQALIDLHNHDLGENHHLRVSFSKSTI","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:11:13.149Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":454,"term_name":"flexible linker","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM fold. <i> Conte MR, Grüne T, Ghuman J, Kelly G, Ladas A, Matthews S, Curry S. </i> EMBO J, 2000","statement":[{"text":"In our present analysis of the NMR structure of PTB-34, the extent of flexibility of the inter-domain linker is particularly striking (Figure 3): there are no inter-domain contacts whatsoever and the two RRM domains appear to tumble independently, the long linker region making no fixed contacts with the rest of the protein, presumably due to disorder.","type":"Results"}],"term_id":"IDPO:0000033","curator_id":"vnugnes","start":431,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10856256","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-12-05T15:51:15.061Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01601r004","ec_go":"EXP","disprot_namespace":"Disorder function","cross_refs":[{"db":"PDB","id":"1QM9"}],"sequence_construct":"MGNSVLLVSNLNPERVTPQSLFILFGVYGDVQRVKILFNKKENALVQMADGNQAQLAMSHLNGHKLHGKPIRITLSKHQNVQLPREGQEDQGLTKDYGNSPLHRFKKPGSKNFQNIFPPSATLHLSNIPPSVSEEDLKVLFSSNGGVVKGFKFFQKDRKMALIQMGSVEEAVQALIDLHNHDLGENHHLRVSFSKSTI","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:11:20.827Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":184,"region_id":"DP01601r007","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Resonance assignment and topology of the 2H, 13C, 15N labelled 29 kDa N-terminal fragment of the polypyrimidine tract binding protein (PTB). <i> Simpson PJ, Davydova N, Curry S, Matthews S. </i> J Biomol NMR, 2002","statement":[{"text":"Assignments could not be made for the majority of residues within the extensive inter-domain linker sequence (residues 143–184 approximately) and also at the N- and C-termini. 15N-relaxation data confirm that these regions are highly flexible (data not shown) and are likely to be unstructured.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":143,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-29T16:28:32.885Z","reference_source":"pmid","term_name":"disorder","reference_id":"12449425","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"A 250-residue N-terminal fragment of human PTB (Gil et al., 1991), which contains the first and second RNP-CS domains (residues 51–301; designated PTB1-12) was sub-cloned by PCR into expression vector pQE9 (Qiagen) using engineered BamHI and HindIII sites which adds an N-terminal polyHistidine tag (MRGSHHHHHHGS)."}]}],"sequence_construct":"MRGSHHHHHHGSSRSSGVPSRVIHIRKLPIDVTEGEVISLGLPFGKVTNLLMLKGKNQAFIEMNTEEAANTMVNYYTSVTPVLRGQPIYIQFSNHKELKTDSSPNQARAQAALQAVNSVQSGNLALAASAAAVDAGMAMAGQSPVLRIIVENLFYPVTLDVLHQIFSKFGTVLKIITFTKNNQFQALLQYADPVSAQHAKLSLDGQNIYNACCTLRIDFSKLTSLNVKYNNDKSRDYTRPDLPSGDSQPSLDQTMAAAFGLSV","cross_refs":[{"db":"BMRB","id":"5409"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:11:17.108Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":184,"term_name":"flexible linker","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":" <i> Simpson, Peter J.; Davydova, Natalia; Curry, Stephen; Matthews, Stephen <i> Journal Of Biomolecular Nmr 2002","term_id":"IDPO:0000033","curator_id":"vnugnes","start":143,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10.1023/A:1020635912814","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-29T16:45:45.713Z","reference_source":"doi","ec_id":"ECO:0006165","region_id":"DP01601r008","ec_go":"EXP","disprot_namespace":"Disorder function","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"A 250-residue N-terminal fragment of human PTB (Gil et al., 1991), which contains the first and second RNP-CS domains (residues 51–301; designated PTB1-12) was sub-cloned by PCR into expression vector pQE9 (Qiagen) using engineered BamHI and HindIII sites which adds an N-terminal polyHistidine tag (MRGSHHHHHHGS)."}]}],"sequence_construct":"MRGSHHHHHHGSSRSSGVPSRVIHIRKLPIDVTEGEVISLGLPFGKVTNLLMLKGKNQAFIEMNTEEAANTMVNYYTSVTPVLRGQPIYIQFSNHKELKTDSSPNQARAQAALQAVNSVQSGNLALAASAAAVDAGMAMAGQSPVLRIIVENLFYPVTLDVLHQIFSKFGTVLKIITFTKNNQFQALLQYADPVSAQHAKLSLDGQNIYNACCTLRIDFSKLTSLNVKYNNDKSRDYTRP DLPSGDSQPSLDQTMAAAFGLSV","statement":[{"text":"Assignments could not be made for the majority of residues within the extensive inter-domain linker sequence (residues 143–184 approximately) and also at the N- and C-termini. 15N-relaxation data confirm that these regions are highly flexible (data not shown) and are likely to be unstructured.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T17:11:22.871Z"}}],"released":"2018_11","uniref100":"UniRef100_P26599","date":"2018-07-31T09:46:58.000Z","acc":"P26599","name":"Polypyrimidine tract-binding protein 1","length":557,"organism":"Homo sapiens","dataset":["Condensates-related proteins","RNA-binding proteins","Cancer-related proteins"],"UniParc":"UPI0000000C5E","genes":[{"name":{"value":"PTBP1"},"synonyms":[{"value":"PTB"}]}],"alphafold_very_low_content":0.2391713747645951,"disorder_content":0.1490125673249551,"disprot_consensus":{"full":[{"start":143,"end":184,"type":"D"},{"start":409,"end":425,"type":"D"},{"start":431,"end":454,"type":"D"}],"Structural state":[{"start":143,"end":184,"type":"D"},{"start":409,"end":425,"type":"D"},{"start":431,"end":454,"type":"D"}],"Disorder function":[{"start":143,"end":184,"type":"F"},{"start":431,"end":454,"type":"F"}]}},{"features":{"pfam":[{"id":"PF15009","name":"STING ligand-binding domain","start":154,"end":337},{"id":"PF23417","name":"STING transmembrane domain","start":45,"end":152}],"gene3D":[{"start":195,"end":341,"id":"3.40.50.12100","name":"Stimulator of interferon genes protein"}]},"uniref50":"UniRef50_Q86WV6","sequence":"MPHSSLHPSIPCPRGHGAQKAALVLLSACLVTLWGLGEPPEHTLRYLVLHLASLQLGLLLNGVCSLAEELRHIHSRYRGSYWRTVRACLGCPLRRGALLLLSIYFYYSLPNAVGPPFTWMLALLGLSQALNILLGLKGLAPAEISAVCEKGNFNVAHGLAWSYYIGYLRLILPELQARIRTYNQHYNNLLRGAVSQRLYILLPLDCGVPDNLSMADPNIRFLDKLPQQTGDHAGIKDRVYSNSIYELLENGQRAGTCVLEYATPLQTLFAMSQYSQAGFSREDRLEQAKLFCRTLEDILADAPESQNNCRLIAYQEPADDSSFSLSQEVLRHLRQEEKEEVTVGSLKTSAVPSTSTMSQEPELLISGMEKPLPLRTDFS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q86WV6","disprot_id":"DP01602","ncbi_taxon_id":9606,"regions_counter":8,"creator":"mpajkos","regions":[{"region_id":"DP01602r001","ec_ontology":"ECO","end":379,"ec_name":"x-ray crystallography evidence used in manual assertion","start":342,"version":3,"statement":[{"text":"pSTING adopts an extended random coil structure spanning two patches of positively charged residues and a large hydrophobic groove between them (Fig. S2 A and B).","type":"Results"}],"term_name":"disorder","reference_html":"Structural basis for concerted recruitment and activation of IRF-3 by innate immune adaptor proteins. <i> Zhao B, Shu C, Gao X, Sankaran B, Du F, Shelton CL, Herr AB, Ji JY, Li P. </i> Proc Natl Acad Sci U S A, 2016","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27302953","date":"2023-12-15T17:00:51.251Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5JEJ"}],"term_namespace":"Structural state","ec_id":"ECO:0005670","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":366,"end":366,"position":"Specific residue"},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe378Trp","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q14653"}],"sequence_construct":"STVGSLKTSAVPSTSTMSQEPELLISGMEKPLPLRTDWS"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":379,"term_name":"protein binding","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural basis for concerted recruitment and activation of IRF-3 by innate immune adaptor proteins. <i> Zhao B, Shu C, Gao X, Sankaran B, Du F, Shelton CL, Herr AB, Ji JY, Li P. </i> Proc Natl Acad Sci U S A, 2016","statement":[{"text":"The pLxIS motif interacts with IRF-3 through electrostatic interactions, hydrogen bonds, and hydrophobic interactions. A cluster of positively charged residues, Arg285, His288, His290, and Lys313, interacts with pSer366 of pSTING through electrostatic interactions (Fig. 1B and Fig. S2B). Residues pSer366, Ile365, and Leu363 form three backbone hydrogen bonds with IRF-3.","type":"Results"}],"term_id":"GO:0005515","curator_id":"vnugnes","start":359,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"27302953","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-12-15T17:05:46.219Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01602r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":366,"end":366,"position":"Specific residue"},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe378Trp","start":null,"end":null,"position":null}],"interaction_partner":[{"db":"UniProt","id":"Q14653","operator":"and","partner_start":189,"partner_end":427}],"sequence_construct":"STVGSLKTSAVPSTSTMSQEPELLISGMEKPLPLRTDWS","cross_refs":[{"db":"PDB","id":"5JEJ"}]},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":379,"term_name":"phosphorylation display site","released":"2023_12","ec_name":"mass spectrometry evidence used in manual assertion","reference_html":"Structural basis for concerted recruitment and activation of IRF-3 by innate immune adaptor proteins. <i> Zhao B, Shu C, Gao X, Sankaran B, Du F, Shelton CL, Herr AB, Ji JY, Li P. </i> Proc Natl Acad Sci U S A, 2016","statement":[{"text":"To determine how the phosphorylated STING mediates the recruitment of IRF-3, we expressed small ubiquitin-related modifier (SUMO) fusions of the human STING CTD (residues 155–379) and C-terminal tail (CTT) (residues 342–379) and phosphorylated them in vitro with TBK1.","type":"Results"},{"text":"The phosphorylation sites were identified by MS analysis of the pSTING CTT.","type":"Figure"},{"text":"Figure S1 shows the phosphorylated residues are Ser358, Ser366, Thr376 and Ser379.","type":"Curator statement"}],"term_id":"IDPO:0000045","curator_id":"vnugnes","start":358,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27302953","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-12-15T17:03:44.029Z","reference_source":"pmid","ec_id":"ECO:0001230","region_id":"DP01602r004","ec_go":"EXP","disprot_namespace":"Disorder function","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe378Trp","start":null,"end":null,"position":null}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":379,"region_id":"DP01602r005","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Structural analysis of the STING adaptor protein reveals a hydrophobic dimer interface and mode of cyclic di-GMP binding. <i> Ouyang S, Song X, Wang Y, Ru H, Shaw N, Jiang Y, Niu F, Zhu Y, Qiu W, Parvatiyar K, Li Y, Zhang R, Cheng G, Liu ZJ. </i> Immunity, 2012","statement":[{"text":"Electron density for the C-terminal end of the protein, AA344-379, positioned at the end of helix α9 was missing, suggesting that this part of the protein is flexible and probably swings around the tip of helix α9 protruding out of the concave cavity of the sheet.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":344,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-12-15T15:19:37.985Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4EF4"},{"db":"PDB","id":"4EF5"}],"reference_id":"22579474","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:135440063"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":379,"region_id":"DP01602r006","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Crystal structures of STING protein reveal basis for recognition of cyclic di-GMP. <i> Shang G, Zhu D, Li N, Zhang J, Zhu C, Lu D, Liu C, Yu Q, Zhao Y, Xu S, Gu L. </i> Nat Struct Mol Biol, 2012","statement":[{"text":"Both the final refined STINGCTD model in the apo and c-di-GMP–bound forms contains all the residues of STINGCTD except the two segments containing residues 149–150 and 344–379, which have no clear electron density and are presumed to be disordered in solution.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":344,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-12-15T15:11:40.114Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4F5W"},{"db":"PDB","id":"4F5Y"}],"reference_id":"22728660","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:135440063"}]},{"start":342,"end":379,"reference_id":"27302953","reference_source":"pmid","reference_html":"Structural basis for concerted recruitment and activation of IRF-3 by innate immune adaptor proteins. <i> Zhao B, Shu C, Gao X, Sankaran B, Du F, Shelton CL, Herr AB, Ji JY, Li P. </i> Proc Natl Acad Sci U S A, 2016","date":"2023-12-15T17:06:01.884Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":358,"end":358,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":366,"end":366,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":376,"end":376,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":379,"end":379,"position":"Specific residue"},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe378Trp","start":null,"end":null,"position":null}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q14653","operator":null,"partner_start":189,"partner_end":427}],"region_id":"DP01602r007","statement":[{"text":"Surface plasmon resonance (SPR) binding studies show that IRF-3 binds only to the pSTING CTD or CTT (Fig. S1 A and C). The affinity of the pSTING CTD for IRF-3 (Kd ∼48 μM) (Fig. S1B) is comparable to that of the pSTING CTT (Kd ∼43 μM) (Fig. S1D). These results show that STING binds to IRF-3 via its C-terminal pLxIS motif upon phosphorylation.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":358,"end":366,"reference_id":"27302953","reference_source":"pmid","reference_html":"Structural basis for concerted recruitment and activation of IRF-3 by innate immune adaptor proteins. <i> Zhao B, Shu C, Gao X, Sankaran B, Du F, Shelton CL, Herr AB, Ji JY, Li P. </i> Proc Natl Acad Sci U S A, 2016","date":"2023-12-15T17:12:55.156Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser366Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser358Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu363Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu365Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro361Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe378Trp","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q14653","operator":null,"partner_start":189,"partner_end":427}],"region_id":"DP01602r008","statement":[{"text":"To identify the phosphorylation site of STING that is essential for IRF-3 recruitment, we mutated each of the four potential phosphorylated residues (Fig. S1E) to alanine and conducted IFN-β luciferase reporter assays in HEK293T cells, which do not express STING (28). As shown in Fig. 1C, the S366A mutation abolishes IFN-β reporter activation, consistent with previous studies (23). In addition, the S358A mutation partially impairs IFN-β reporter activation (Fig. 1C). However, the T376A and S379A mutations do not affect IFN-β reporter activation (Fig. 1C).","type":"Results"},{"text":"The L363A and I365A mutations individually or in combination strongly abolish IFN-β reporter activation (Fig. 1D). In contrast, the E362A and L364A mutations have only minor effects on STING-mediated signaling (Fig. 1D). The P361A mutation upstream of the pLxIS motif also dramatically reduces IFN-β reporter activation (Fig. 1D).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_Q86WV6","date":"2018-07-31T10:40:14.000Z","acc":"Q86WV6","name":"Stimulator of interferon genes protein","length":379,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI000000DC5E","genes":[{"name":{"value":"STING1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:27962","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:27962"}}]},"synonyms":[{"value":"ERIS","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"19433799","url":"http://www.ncbi.nlm.nih.gov/pubmed/19433799","alternativeUrl":"https://europepmc.org/abstract/MED/19433799"}}]},{"value":"MITA","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"18818105","url":"http://www.ncbi.nlm.nih.gov/pubmed/18818105","alternativeUrl":"https://europepmc.org/abstract/MED/18818105"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"19285439","url":"http://www.ncbi.nlm.nih.gov/pubmed/19285439","alternativeUrl":"https://europepmc.org/abstract/MED/19285439"}}]},{"value":"STING","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"18724357","url":"http://www.ncbi.nlm.nih.gov/pubmed/18724357","alternativeUrl":"https://europepmc.org/abstract/MED/18724357"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"26669264","url":"http://www.ncbi.nlm.nih.gov/pubmed/26669264","alternativeUrl":"https://europepmc.org/abstract/MED/26669264"}}]},{"value":"TMEM173","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:27962","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:27962"}}]}]}],"alphafold_very_low_content":0.08443271767810026,"disorder_content":0.10026385224274406,"disprot_consensus":{"full":[{"start":342,"end":379,"type":"D"}],"Structural state":[{"start":342,"end":379,"type":"D"}],"Molecular function":[{"start":342,"end":379,"type":"F"}],"Disorder function":[{"start":358,"end":379,"type":"F"}]}},{"features":{"pfam":[{"id":"PF30854","name":"Par-4 C-terminal domain","start":272,"end":340},{"id":"PF30855","name":"Par-4 SAC region","start":147,"end":209}]},"uniref50":"UniRef50_Q96IZ0","sequence":"MATGGYRTSSGLGGSTTDFLEEWKAKREKMRAKQNPPGPAPPGGGSSDAAGKPPAGALGTPAAAAANELNNNLPGGAPAAPAVPGPGGVNCAVGSAMLTRAAPGPRRSEDEPPAASASAAPPPQRDEEEPDGVPEKGKSSGPSARKGKGQIEKRKLREKRRSTGVVNIPAAECLDEYEDDEAGQKERKREDAITQQNTIQNEAVNLLDPGSSYLLQEPPRTVSGRYKSTTSVSEEDVSSRYSRTDRSGFPRYNRDANVSGTLVSSSTLEKKIEDLEKEVVRERQENLRLVRLMQDKEEMIGKLKEEIDLLNRDLDDIEDENEQLKQENKTLLKVVGQLTR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q96IZ0","disprot_id":"DP01603","ncbi_taxon_id":9606,"regions_counter":5,"creator":"tszani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":77,"region_id":"DP01603r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis for Par-4 recognition by the SPRY domain- and SOCS box-containing proteins SPSB1, SPSB2, and SPSB4. <i> Filippakopoulos P, Low A, Sharpe TD, Uppenberg J, Yao S, Kuang Z, Savitsky P, Lewis RS, Nicholson SE, Norton RS, Bullock AN. </i> J Mol Biol, 2010","term_id":"IDPO:0000002","curator_id":"tszani","start":59,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20561531","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":81,"region_id":"DP01603r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for Par-4 recognition by the SPRY domain- and SOCS box-containing proteins SPSB1, SPSB2, and SPSB4. <i> Filippakopoulos P, Low A, Sharpe TD, Uppenberg J, Yao S, Kuang Z, Savitsky P, Lewis RS, Nicholson SE, Norton RS, Bullock AN. </i> J Mol Biol, 2010","term_id":"IDPO:0000002","curator_id":"tszani","start":62,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2jk9"}],"reference_id":"20561531","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":81,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural basis for Par-4 recognition by the SPRY domain- and SOCS box-containing proteins SPSB1, SPSB2, and SPSB4. <i> Filippakopoulos P, Low A, Sharpe TD, Uppenberg J, Yao S, Kuang Z, Savitsky P, Lewis RS, Nicholson SE, Norton RS, Bullock AN. </i> J Mol Biol, 2010","term_id":"GO:0005515","curator_id":"tszani","start":62,"term_ontology":"GO","curator_name":"Tamás Szaniszló","reference_id":"20561531","version":3,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2jk9"}],"region_id":"DP01603r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":77,"region_id":"DP01603r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis for Par-4 recognition by the SPRY domain- and SOCS box-containing proteins SPSB1, SPSB2, and SPSB4. <i> Filippakopoulos P, Low A, Sharpe TD, Uppenberg J, Yao S, Kuang Z, Savitsky P, Lewis RS, Nicholson SE, Norton RS, Bullock AN. </i> J Mol Biol, 2010","term_id":"IDPO:0000002","curator_id":"tszani","start":62,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20561531","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":77,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis for Par-4 recognition by the SPRY domain- and SOCS box-containing proteins SPSB1, SPSB2, and SPSB4. <i> Filippakopoulos P, Low A, Sharpe TD, Uppenberg J, Yao S, Kuang Z, Savitsky P, Lewis RS, Nicholson SE, Norton RS, Bullock AN. </i> J Mol Biol, 2010","term_id":"GO:0005515","curator_id":"tszani","start":62,"term_ontology":"GO","curator_name":"Tamás Szaniszló","reference_id":"20561531","version":3,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01603r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q96IZ0","date":"2018-07-31T10:52:36.000Z","acc":"Q96IZ0","name":"PRKC apoptosis WT1 regulator protein","length":340,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000070738","genes":[{"name":{"value":"PAWR"},"synonyms":[{"value":"PAR4"}]}],"alphafold_very_low_content":0.42058823529411765,"disorder_content":0.06764705882352941,"disprot_consensus":{"full":[{"start":59,"end":81,"type":"D"}],"Structural state":[{"start":59,"end":81,"type":"D"}],"Molecular function":[{"start":62,"end":81,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04157","name":"EAP30/Vps36 family","start":5,"end":214}],"gene3D":[{"start":87,"end":161,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"start":162,"end":233,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}]},"uniref50":"UniRef50_Q12483","sequence":"MKQFGLAAFDELKDGKYNDVNKTILEKQSVELRDQLMVFQERLVEFAKKHNSELQASPEFRSKFMHMCSSIGIDPLSLFDRDKHLFTVNDFYYEVCLKVIEICRQTKDMNGGVISFQELEKVHFRKLNVGLDDLEKSIDMLKSLECFEIFQIRGKKFLRSVPNELTSDQTKILEICSILGYSSISLLKANLGWEAVRSKSALDEMVANGLLWIDYQGGAEALYWDPSWITRQL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q12483","disprot_id":"DP01604","ncbi_taxon_id":559292,"regions_counter":3,"creator":"nfoutel","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":22,"region_id":"DP01604r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"ESCRT-II, an endosome-associated complex required for protein sorting: crystal structure and interactions with ESCRT-III and membranes. <i> Teo H, Perisic O, González B, Williams RL. </i> Dev Cell, 2004","statement":[{"text":"The N-terminal region (that encompasses residues 1 to 22 preceding the helix 1) showed to be disordered in the crystal structure.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":1,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"15469844","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":22,"term_name":"lipid binding","start":1,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","statement":[{"text":"The N-terminal region of Vps22 (...) is particularly rich in basic residues (30% inhuman Vps22) (...). Consistent with this, we observe weak but reproducible binding of the N-terminal helical domain of Vps22 (residues 1–90) to brain-derived liposomes (data not shown), suggesting that Vps22 might contribute to membrane binding of ESCRT II.","type":"Results"}],"curator_id":"nfoutel","released":"2022_03","term_ontology":"GO","curator_name":"Nicolas Foutel","reference_id":"15469844","version":3,"reference_html":"ESCRT-II, an endosome-associated complex required for protein sorting: crystal structure and interactions with ESCRT-III and membranes. <i> Teo H, Perisic O, González B, Williams RL. </i> Dev Cell, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008289","ec_id":"ECO:0006220","region_id":"DP01604r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":19,"region_id":"DP01604r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the ESCRT-II endosomal trafficking complex. <i> Hierro A, Sun J, Rusnak AS, Kim J, Prag G, Emr SD, Hurley JH. </i> Nature, 2004","statement":[{"text":"Vps22 consists of a single N-terminal coiled coil followed by two winged-helix (WH) domains (Supplementary Fig. 1a). All but the first 19 residues are ordered.","type":"Article"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":1,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"15329733","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q12483","date":"2018-07-31T11:48:09.000Z","acc":"Q12483","name":"Vacuolar-sorting protein SNF8","length":233,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI00000697FE","genes":[{"name":{"value":"SNF8"},"synonyms":[{"value":"VPS22"}],"olnNames":[{"value":"YPL002C"}]}],"alphafold_very_low_content":0.02145922746781116,"disorder_content":0.0944206008583691,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"}],"Structural state":[{"start":1,"end":22,"type":"D"}],"Molecular function":[{"start":1,"end":22,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":127,"end":197},{"id":"PF00076","name":"RNA recognition motif","start":213,"end":274}],"gene3D":[{"start":112,"end":203,"id":"3.30.70.330","name":"3.30.70.330"},{"start":204,"end":294,"id":"3.30.70.330","name":"3.30.70.330"}]},"uniref50":"UniRef50_P19339","sequence":"MYGNNNPGSNNNNGGYPPYGYNNKSSGGRGFGMSHSLPSGMSRYAFSPQDTEFSFPSSSSRRGYNDFPGCGGSGGNGGSANNLGGGNMCHLPPMASNNSLNNLCGLSLGSGGSDDLMNDPRASNTNLIVNYLPQDMTDRELYALFRAIGPINTCRIMRDYKTGYSFGYAFVDFTSEMDSQRAIKVLNGITVRNKRLKVSYARPGGESIKDTNLYVTNLPRTITDDQLDTIFGKYGSIVQKNILRDKLTGRPRGVAFVRYNKREEAQEAISALNNVIPEGGSQPLSVRLAEEHGKAKAAHFMSQMGVVPANVPPPPPQPPAHMAAAFNMMHRGRSIKSQQRFQNSHPYFDAKKFI","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_P19339","disprot_id":"DP01605","ncbi_taxon_id":7227,"regions_counter":8,"creator":"bhajdu","regions":[{"region_id":"DP01605r001","ec_ontology":"ECO","end":253,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":244,"version":3,"statement":[{"text":"The loop connecting the β2 and β3 strands of the Sxl RBD1 (β2/β3 loop) consists of ten amino acid residues (R158 to G167), and is as long as that of the Sxl RBD2 (R244 to G253), whereas the corresponding loop of the U1A RBD1 is composed of only six amino acid residues (R48 to G53).","type":"Results"}],"term_name":"disorder","reference_html":"A characteristic arrangement of aromatic amino acid residues in the solution structure of the amino-terminal RNA-binding domain of Drosophila sex-lethal. <i> Inoue M, Muto Y, Sakamoto H, Kigawa T, Takio K, Shimura Y, Yokoyama S. </i> J Mol Biol, 1997","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"9299339","date":"2023-09-25T18:21:28.799Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP01605r002","ec_ontology":"ECO","end":211,"ec_name":"x-ray crystallography evidence used in manual assertion","start":201,"version":3,"statement":[{"text":"Characteristic of a poorly ordered region, the electron density for the 10-residue interdomain linker was weak and discontinuous in maps calculated with the multiwavelength anomalous diffraction data.","type":"Results"},{"text":"From the C terminus of RRM1, the second-closest RRM2 N terminus is 28.8 Å away, a distance that two residues could not possibly bridge. Weak electron density and the high B-factors of the interdomain linker imply significant flexibility in this region.","type":"Results"}],"term_name":"disorder","reference_html":"Absence of interdomain contacts in the crystal structure of the RNA recognition motifs of Sex-lethal. <i> Crowder SM, Kanaar R, Rio DC, Alber T. </i> Proc Natl Acad Sci U S A, 1999","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10220389","date":"2023-09-25T18:30:35.774Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3SXL"}],"term_namespace":"Structural state","ec_id":"ECO:0005670","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":136,"end":136,"position":"Specific residue","statements":[{"type":"Methods","text":"Selenomethionine (SeMet) was incorporated to >98% by growth in M9 minimal medium supplemented with Leu, Ile, Val, Phe, Lys, and Thr and 75 mg⋅l−1 SeMet at mid-log phase immediately before induction with isopropyl β-d-thiogalactoside (24)."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":157,"end":157,"position":"Specific residue","statements":[{"type":"Methods","text":"Selenomethionine (SeMet) was incorporated to >98% by growth in M9 minimal medium supplemented with Leu, Ile, Val, Phe, Lys, and Thr and 75 mg⋅l−1 SeMet at mid-log phase immediately before induction with isopropyl β-d-thiogalactoside (24)."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":177,"end":177,"position":"Specific residue","statements":[{"type":"Methods","text":"Selenomethionine (SeMet) was incorporated to >98% by growth in M9 minimal medium supplemented with Leu, Ile, Val, Phe, Lys, and Thr and 75 mg⋅l−1 SeMet at mid-log phase immediately before induction with isopropyl β-d-thiogalactoside (24)."}]}],"sequence_construct":"MESDDLMNDPRASNTNLIVNYLPQDMTDRELYALFRAIGPINTCRIMRDYKTGYSFGYAFVDFTSEMDSQRAIKVLNGITVRNKRLKVSYARPGGESIKDTNLYVTNLPRTITDDQLDTIFGKYGSIVQKNILRDKLTGRPRGVAFVRYNKREEAQEAISALNNVIPEGGSQPLSVRLAEEHGK"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":211,"term_name":"flexible linker","released":"2023_12","ec_name":"x-ray crystallography evidence used in manual assertion","reference_html":"Absence of interdomain contacts in the crystal structure of the RNA recognition motifs of Sex-lethal. <i> Crowder SM, Kanaar R, Rio DC, Alber T. </i> Proc Natl Acad Sci U S A, 1999","statement":[{"text":"Characteristic of a poorly ordered region, the electron density for the 10-residue interdomain linker was weak and discontinuous in maps calculated with the multiwavelength anomalous diffraction data.","type":"Results"},{"text":" From the C terminus of RRM1, the second-closest RRM2 N terminus is 28.8 Å away, a distance that two residues could not possibly bridge. Weak electron density and the high B-factors of the interdomain linker imply significant flexibility in this region.","type":"Results"},{"text":"In summary, SXL RRM1 and RRM2 form two discreet RNA binding surfaces that are too far apart in the crystal structure to interact simultaneously with the high-affinity, r(GU8C) RNA. These results indicate that the interdomain linker acts as flexible tether, and orientation of the RRM domains is coupled to RNA binding.","type":"Results"}],"term_id":"IDPO:0000033","curator_id":"vnugnes","start":201,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10220389","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-09-25T18:35:20.446Z","reference_source":"pmid","ec_id":"ECO:0005670","region_id":"DP01605r003","ec_go":"EXP","disprot_namespace":"Disorder function","construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":136,"end":136,"position":"Specific residue","statements":[{"type":"Methods","text":"Selenomethionine (SeMet) was incorporated to >98% by growth in M9 minimal medium supplemented with Leu, Ile, Val, Phe, Lys, and Thr and 75 mg⋅l−1 SeMet at mid-log phase immediately before induction with isopropyl β-d-thiogalactoside (24)."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":157,"end":157,"position":"Specific residue","statements":[{"type":"Methods","text":"Selenomethionine (SeMet) was incorporated to >98% by growth in M9 minimal medium supplemented with Leu, Ile, Val, Phe, Lys, and Thr and 75 mg⋅l−1 SeMet at mid-log phase immediately before induction with isopropyl β-d-thiogalactoside (24)."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":177,"end":177,"position":"Specific residue","statements":[{"type":"Methods","text":"Selenomethionine (SeMet) was incorporated to >98% by growth in M9 minimal medium supplemented with Leu, Ile, Val, Phe, Lys, and Thr and 75 mg⋅l−1 SeMet at mid-log phase immediately before induction with isopropyl β-d-thiogalactoside (24)."}]}],"cross_refs":[{"db":"PDB","id":"3SXL"}],"sequence_construct":"MESDDLMNDPRASNTNLIVNYLPQDMTDRELYALFRAIGPINTCRIMRDYKTGYSFGYAFVDFTSEMDSQRAIKVLNGITVRNKRLKVSYARPGGESIKDTNLYVTNLPRTITDDQLDTIFGKYGSIVQKNILRDKLTGRPRGVAFVRYNKREEAQEAISALNNVIPEGGSQPLSVRLAEEHGK"},{"region_id":"DP01605r005","ec_ontology":"ECO","end":167,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":158,"version":3,"statement":[{"text":"(a) The 20 backbone structures of RBD1FY, which were superimposed for minimal root-mean-square deviation of the backbone atoms (N, Cα, and C′) of residues 125 to 131, 137 to 157, and 167 to 201 (stereoview).","type":"Figure"}],"term_name":"disorder","reference_html":"A characteristic arrangement of aromatic amino acid residues in the solution structure of the amino-terminal RNA-binding domain of Drosophila sex-lethal. <i> Inoue M, Muto Y, Sakamoto H, Kigawa T, Takio K, Shimura Y, Yokoyama S. </i> J Mol Biol, 1997","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"9299339","date":"2023-09-25T18:19:48.756Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2SXL"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe166Tyr","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Among these mutant proteins, RBD1FY, with a Phe→Tyr mutation at position 166, exhibited about ten-fold higher solubility as compared with that of the wild-type RBD1 (data not shown)."}]}],"sequence_construct":"ASNTNLIVNYLPQDMTDRELYALFRAIGPINTCRIMRDYKTGYSYGYAFVDFTSEMDSQRAIKVLNGITVRNKRLKVSYARPGGESIK"},{"start":158,"end":167,"reference_id":"9299339","reference_source":"pmid","reference_html":"A characteristic arrangement of aromatic amino acid residues in the solution structure of the amino-terminal RNA-binding domain of Drosophila sex-lethal. <i> Inoue M, Muto Y, Sakamoto H, Kigawa T, Takio K, Shimura Y, Yokoyama S. </i> J Mol Biol, 1997","date":"2023-09-25T18:23:39.999Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe166Tyr","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Among these mutant proteins, RBD1FY, with a Phe→Tyr mutation at position 166, exhibited about ten-fold higher solubility as compared with that of the wild-type RBD1 (data not shown). "}]}],"cross_refs":[{"db":"PDB","id":"2SXL"}],"region_id":"DP01605r006","sequence_construct":"ASNTNLIVNYLPQDMTDRELYALFRAIGPINTCRIMRDYKTGYSYGYAFVDFTSEMDSQRAIKVLNGITVRNKRLKVSYARPGGESIK","statement":[{"text":"The loop connecting the β2 and β3 strands of the Sxl RBD1 (β2/β3 loop) consists of ten amino acid residues (R158 to G167), and is as long as that of the Sxl RBD2 (R244 to G253), whereas the corresponding loop of the U1A RBD1 is composed of only six amino acid residues (R48 to G53).","type":"Results"}]},{"start":244,"end":253,"reference_id":"9299339","reference_source":"pmid","reference_html":"A characteristic arrangement of aromatic amino acid residues in the solution structure of the amino-terminal RNA-binding domain of Drosophila sex-lethal. <i> Inoue M, Muto Y, Sakamoto H, Kigawa T, Takio K, Shimura Y, Yokoyama S. </i> J Mol Biol, 1997","date":"2023-09-25T18:24:01.019Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01605r007","statement":[{"text":"The loop connecting the β2 and β3 strands of the Sxl RBD1 (β2/β3 loop) consists of ten amino acid residues (R158 to G167), and is as long as that of the Sxl RBD2 (R244 to G253), whereas the corresponding loop of the U1A RBD1 is composed of only six amino acid residues (R48 to G53).","type":"Results"}]},{"start":111,"end":123,"reference_id":"10220389","reference_source":"pmid","reference_html":"Absence of interdomain contacts in the crystal structure of the RNA recognition motifs of Sex-lethal. <i> Crowder SM, Kanaar R, Rio DC, Alber T. </i> Proc Natl Acad Sci U S A, 1999","date":"2023-09-25T18:34:10.587Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":136,"end":136,"position":"Specific residue","statements":[{"type":"Methods","text":"Selenomethionine (SeMet) was incorporated to >98% by growth in M9 minimal medium supplemented with Leu, Ile, Val, Phe, Lys, and Thr and 75 mg⋅l−1 SeMet at mid-log phase immediately before induction with isopropyl β-d-thiogalactoside (24)."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":157,"end":157,"position":"Specific residue","statements":[{"type":"Methods","text":"Selenomethionine (SeMet) was incorporated to >98% by growth in M9 minimal medium supplemented with Leu, Ile, Val, Phe, Lys, and Thr and 75 mg⋅l−1 SeMet at mid-log phase immediately before induction with isopropyl β-d-thiogalactoside (24)."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":177,"end":177,"position":"Specific residue","statements":[{"type":"Methods","text":"Selenomethionine (SeMet) was incorporated to >98% by growth in M9 minimal medium supplemented with Leu, Ile, Val, Phe, Lys, and Thr and 75 mg⋅l−1 SeMet at mid-log phase immediately before induction with isopropyl β-d-thiogalactoside (24)."}]}],"cross_refs":[{"db":"PDB","id":"3SXL"}],"region_id":"DP01605r008","sequence_construct":"MESDDLMNDPRASNTNLIVNYLPQDMTDRELYALFRAIGPINTCRIMRDYKTGYSFGYAFVDFTSEMDSQRAIKVLNGITVRNKRLKVSYARPGGESIKDTNLYVTNLPRTITDDQLDTIFGKYGSIVQKNILRDKLTGRPRGVAFVRYNKREEAQEAISALNNVIPEGGSQPLSVRLAEEHGK","statement":[{"text":"Residues left out of the model for lack of interpretable electron density include 111–123, 204–205 (interdomain linker), 276–282 (α2-β4 loop of RRM2), and 290–294 (C terminus).","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_P19339","date":"2018-07-31T12:16:23.000Z","acc":"P19339","name":"Protein sex-lethal","length":354,"organism":"Drosophila melanogaster","dataset":["RNA-binding proteins"],"UniParc":"UPI0000124D1A","genes":[{"name":{"value":"Sxl"},"synonyms":[{"value":"Sx1"}],"orfNames":[{"value":"CG43770"}]}],"alphafold_very_low_content":0.3389830508474576,"disorder_content":0.12429378531073447,"disprot_consensus":{"full":[{"start":111,"end":123,"type":"D"},{"start":158,"end":167,"type":"D"},{"start":201,"end":211,"type":"D"},{"start":244,"end":253,"type":"D"}],"Structural state":[{"start":111,"end":123,"type":"D"},{"start":158,"end":167,"type":"D"},{"start":201,"end":211,"type":"D"},{"start":244,"end":253,"type":"D"}],"Disorder function":[{"start":158,"end":167,"type":"F"},{"start":201,"end":211,"type":"F"},{"start":244,"end":253,"type":"F"}]}},{"features":{"pfam":[{"id":"PF21449","name":"RIF2, ASCE domain","start":186,"end":277},{"id":"PF21450","name":"RIF2, AAA+ lid domain","start":284,"end":368}]},"uniref50":"UniRef50_Q06208","sequence":"MEHVDSDFAPIRRSKKVVDSDKIVKAISDDLEQKNFTVLRKLNLVPIKKSVSSPKVCKPSPVKERVDHVFYQKFKSMALQELGTNYLSISYVPSLSKFLSKNLRSMKNCIVFFDKVEHIHQYAGIDRAVSETLSLVDINVVIIEMNDYLMKEGIQSSKSKECIESMGQASYSGQLDFEASEKPSNHTSDLMMMVMRKINNDESIDHIVYFKFEQLDKLSTSTIIEPSKLTEFINVLSVLEKSNNIAFKVLIYSNNVSISSLLSTSLKKKLNTKYTVFEMPILTCAQEQEYLKKMIKFTFDSGSKLLQSYNSLVTCQLNNKESNLAIFFEFLKVFPHPFTYLFNAYTEIIVQSRTFDELLDKIRNRLTIKNYPHSAYNFKKNQRLPLKLTRKVHDR","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q06208","disprot_id":"DP01606","ncbi_taxon_id":559292,"regions_counter":2,"creator":"tszani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":186,"region_id":"DP01606r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Rif1 and Rif2 shape telomere function and architecture through multivalent Rap1 interactions. <i> Shi T, Bunker RD, Mattarocci S, Ribeyre C, Faty M, Gut H, Scrima A, Rass U, Rubin SM, Shore D, Thomä NH. </i> Cell, 2013","term_id":"IDPO:0000002","curator_id":"tszani","start":152,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4bj1"}],"reference_id":"23746845","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":60,"region_id":"DP01606r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Rif1 and Rif2 shape telomere function and architecture through multivalent Rap1 interactions. <i> Shi T, Bunker RD, Mattarocci S, Ribeyre C, Faty M, Gut H, Scrima A, Rass U, Rubin SM, Shore D, Thomä NH. </i> Cell, 2013","term_id":"IDPO:0000002","curator_id":"tszani","start":49,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4bj6"}],"reference_id":"23746845","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q06208","date":"2018-07-31T12:58:22.000Z","acc":"Q06208","name":"Protein RIF2","length":395,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI00001338EF","genes":[{"name":{"value":"RIF2"},"olnNames":[{"value":"YLR453C"}]}],"alphafold_very_low_content":0.20506329113924052,"disorder_content":0.1189873417721519,"disprot_consensus":{"full":[{"start":49,"end":60,"type":"D"},{"start":152,"end":186,"type":"D"}],"Structural state":[{"start":49,"end":60,"type":"D"},{"start":152,"end":186,"type":"D"}]}},{"features":{"pfam":[{"id":"PF12231","name":"Rap1-interacting factor 1 N terminal","start":237,"end":649}]},"uniref50":"UniRef50_P29539","sequence":"MSKDFSDKKKHTIDRIDQHILRRSQHDNYSNGSSPWMKTNLPPPSPQAHMHIQSDLSPTPKRRKLASSSDCENKQFDLSAINKNLYPEDTGSRLMQSLPELSASNSDNVSPVTKSVAFSDRIESSPIYRIPGSSPKPSPSSKPGKSILRNRLPSVRTVSDLSYNKLQYTQHKLHNGNIFTSPYKETRVNPRALEYWVSGEIHGLVDNESVSEFKEIIEGGLGILRQESEDYVARRFEVYATFNNIIPILTTKNVNEVDQKFNILIVNIESIIEICIPHLQIAQDTLLSSSEKKNPFVIRLYVQIVRFFSAIMSNFKIVKWLTKRPDLVNKLKVIYRWTTGALRNENSNKIIITAQVSFLRDEKFGTFFLSNEEIKPIISTFTEIMEINSHNLIYEKLLLIRGFLSKYPKLMIETVTSWLPGEVLPRIIIGDEIYSMKILITSIVVLLELLKKCLDFVDEHERIYQCIMLSPVCETIPEKFLSKLPLNSYDSANLDKVTIGHLLTQQIKNYIVVKNDNKIAMDLWLSMTGLLYDSGKRVYDLTSESNKVWFDLNNLCFINNHPKTRLMSIKVWRIITYCICTKISQKNQEGNKSLLSLLRTPFQMTLPYVNDPSAREGIIYHLLGVVYTAFTSNKNLSTDMFELFWDHLITPIYEDYVFKYDSIHLQNVLFTVLHLLIGGKNADVALERKYKKHIHPMSVIASEGVKLKDISSLPPQIIKREYDKIMKVVFQAVEVAISNVNLAHDLILTSLKHLPEDRKDQTHLESFSSLILKVTQNNKDTPIFRDFFGAVTSSFVYTFLDLFLRKNDSSLVNFNIQISKVGISQGNMTLDLLKDVIRKARNETSEFLIIEKFLELDDKKTEVYAQNWVGSTLLPPNISFREFQSLANIVNKVPNENSIENFLDLCLKLSFPVNLFTLLHVSMWSNNNFIYFIQSYVSKNENKLNVDLITLLKTSLPGNPELFSGLLPFLRRNKFMDILEYCIHSNPNLLNSIPDLNSDLLLKLLPRSRASYFAANIKLFKCSEQLTLVRWLLKGQQLEQLNQNFSEIENVLQNASDSELEKSEIIRELLHLAMANPIEPLFSGLLNFCIKNNMADHLDEFCGNMTSEVLFKISPELLLKLLTYKEKPNGKLLAAVIEKIENGDDDYILELLEKIIIQKEIQILEKLKEPLLVFFLNPVSSNMQKHKKSTNMLRELVLLYLTKPLSRSAAKKFFSMLISILPPNPNYQTIDMVNLLIDLIKSHNRKFKDKRTYNATLKTIGKWIQESGVVHQGDSSKEIEAIPDTKSMYIPCEGSENKLSNLQRKVDSQDIQVPATQGMKEPPSSIQISSQISAKDSDSISLKNTAIMNSSQQESHANRSRSIDDETLEEVDNESIREIDQQMKSTQLDKNVANHSNICSTKSDEVDVTELHESIDTQSSEVNAYQPIEVLTSELKAVTNRSIKTNPDHNVVNSDNPLKRPSKETPTSENKRSKGHETMVDVLVSEEQAVSPSSDVICTNIKSIANEESSLALRNSIKVETNCNENSLNVTLDLDQQTITKEDGKGQVEHVQRQENQESMNKINSKSFTQDNIAQYKSVKKARPNNEGENNDYACNVEQASPVRNEVPGDGIQIPSGTILLNSSKQTEKSKVDDLRSDEDEHGTVAQEKHQVGAINSRNKNNDRMDSTPIQGTEEESREVVMTEEGINVRLEDSGTCELNKNLKGPLKGDKDANINDDFVPVEENVRDEGFLKSMEHAVSKETGLEEQPEVADISVLPEIRIPIFNSLKMQGSKSQIKEKLKKRLQRNELMPPDSPPRMTENTNINAQNGLDTVPKTIGGKEKHHEIQLGQAHTEADGEPLLGGDGNEDATSREATPSLKVHFFSKKSRRLVARLRGFTPGDLNGISVEERRNLRIELLDFMMRLEYYSNRDNDMN","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P29539","disprot_id":"DP01607","ncbi_taxon_id":559292,"regions_counter":1,"creator":"tszani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1856,"region_id":"DP01607r001","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Rif1 and Rif2 shape telomere function and architecture through multivalent Rap1 interactions. <i> Shi T, Bunker RD, Mattarocci S, Ribeyre C, Faty M, Gut H, Scrima A, Rass U, Rubin SM, Shore D, Thomä NH. </i> Cell, 2013","term_id":"IDPO:0000002","curator_id":"tszani","start":1773,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23746845","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P29539","date":"2018-07-31T13:09:44.000Z","acc":"P29539","name":"Telomere length regulator protein RIF1","length":1916,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000168DE8","genes":[{"name":{"value":"RIF1"},"orfNames":[{"value":"YBR1743"}],"olnNames":[{"value":"YBR275C"}]}],"alphafold_very_low_content":0.4102296450939457,"disorder_content":0.04384133611691023,"disprot_consensus":{"full":[{"start":1773,"end":1856,"type":"D"}],"Structural state":[{"start":1773,"end":1856,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02060","name":"Slow voltage-gated potassium channel","start":43,"end":98}]},"uniref50":"UniRef50_Q9Y6H6","sequence":"METTNGTETWYESLHAVLKALNATLHSNLLCRPGPGLGPDNQTEERRASLPGRDDNSYMYILFVMFLFAVTVGSLILGYTRSRKVDKRSDPYHVYIKNRVSMI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9Y6H6","disprot_id":"DP01608","ncbi_taxon_id":9606,"regions_counter":2,"creator":"nfoutel","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":10,"region_id":"DP01608r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis for KCNE3 modulation of potassium recycling in epithelia. <i> Kroncke BM, Van Horn WD, Smith J, Kang C, Welch RC, Song Y, Nannemann DP, Taylor KC, Sisco NJ, Sisco NJ, George AL, Meiler J, Vanoye CG, Sanders CR. </i> Sci Adv, 2016","term_id":"IDPO:0000002","curator_id":"ahatos","start":1,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27626070","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":56,"region_id":"DP01608r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis for KCNE3 modulation of potassium recycling in epithelia. <i> Kroncke BM, Van Horn WD, Smith J, Kang C, Welch RC, Song Y, Nannemann DP, Taylor KC, Sisco NJ, Sisco NJ, George AL, Meiler J, Vanoye CG, Sanders CR. </i> Sci Adv, 2016","statement":[{"text":"The KCNE3 structure is composed of an extracellular N-terminal surface-associated amphipathic helix (residues 10 to 30) connected by a flexible loop to the a-helical transmembrane domain (TMD; 57 to 82), followed by a short juxtamembrane helix (90 to 95) and a disordered C terminus (96 to 103).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":31,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"27626070","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9Y6H6","date":"2018-07-31T13:10:40.000Z","acc":"Q9Y6H6","name":"Potassium voltage-gated channel subfamily E member 3","length":103,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012F15C","genes":[{"name":{"value":"KCNE3"}}],"alphafold_very_low_content":0.10679611650485436,"disorder_content":0.34951456310679613,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"},{"start":31,"end":56,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":31,"end":56,"type":"D"}]}},{"features":{"pfam":[{"id":"PF17067","name":"Ribosomal protein S31e","start":1,"end":93}]},"uniref50":"UniRef50_P47910","sequence":"MASLLLGTPSMACHSVSFSFSHSQSVAGVSLSSPPTLSLSSSVSTSPALPLIYCGRGDRKTAKGKRFNHSFGNARPKNKNKGRGPPKAPIFPKGDPSQKED","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","Caryophyllales","Chenopodiaceae","Chenopodioideae","Anserineae","Spinacia"],"uniref90":"UniRef90_P47910","disprot_id":"DP01610","ncbi_taxon_id":3562,"regions_counter":1,"creator":"nfoutel","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":101,"region_id":"DP01610r001","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Unique localization of the plastid-specific ribosomal proteins in the chloroplast ribosome small subunit provides mechanistic insights into the chloroplastic translation. <i> Ahmed T, Shi J, Bhushan S. </i> Nucleic Acids Res, 2017","statement":[{"text":"A loop and an extended structure were assigned for the fragment encompassing residues 69 to 91, based on poor Cryo-EM electron density.  Missing electron density did not allow the authors to model the structure for residues 92 to 101. These facts suggest the region 69 to 101 is unstructured.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":69,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"28582576","version":2,"ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P47910","date":"2018-07-31T13:22:10.000Z","acc":"P47910","name":"30S ribosomal protein S31, chloroplastic","length":101,"organism":"Spinacia oleracea","dataset":[],"UniParc":"UPI0000134918","genes":[{"name":{"value":"RPS31"},"synonyms":[{"value":"PSRP4"}],"orfNames":[{"value":"SOVF_048530"}]}],"alphafold_very_low_content":0.09900990099009901,"disorder_content":0.32673267326732675,"disprot_consensus":{"full":[{"start":69,"end":101,"type":"D"}],"Structural state":[{"start":69,"end":101,"type":"D"}]}},{"features":{"pfam":[{"id":"PF04157","name":"EAP30/Vps36 family","start":323,"end":549},{"id":"PF11605","name":"Vacuolar protein sorting protein 36 Vps36","start":8,"end":95},{"id":"PF16988","name":"Vacuolar protein sorting 36 NZF-N zinc-finger domain","start":111,"end":165}],"gene3D":[{"start":491,"end":559,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"start":1,"end":124,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":406,"end":490,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"start":193,"end":289,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"}]},"uniref50":"UniRef50_Q06696","sequence":"MEYWHYVETTSSGQPLLREGEKDIFIDQSVGLYHGKSKILQRQRGRIFLTSQRIIYIDDAKPTQNSLGLELDDLAYVNYSSGFLTRSPRLILFFKDPSSKDELGKSAETASADVVSTWVCPICMVSNETQGEFTKDTLPTPICINCGVPADYELTKSSINCSNAIDPNANPQNQFGVNSENICPACTFANHPQIGNCEICGHRLPNASKVRSKLNRLNFHDSRVHIELEKNSLARNKSSHSALSSSSSTGSSTEFVQLSFRKSDGVLFSQATERALENILTEKNKHIFNQNVVSVNGVDMRKGASSHEYNNEVPFIETKLSRIGISSLEKSRENQLLNNDILFNNALTDLNKLMSLATSIERLYKNSNITMKTKTLNLQDESTVNEPKTRRPLLILDREKFLNKELFLDEIAREIYEFTLSEFKDLNSDTNYMIITLVDLYAMYNKSMRIGTGLISPMEMREACERFEHLGLNELKLVKVNKRILCVTSEKFDVVKEKLVDLIGDNPGSDLLRLTQILSSNNSKSNWTLGILMEVLQNCVDEGDLLIDKQLSGIYYYKNSYWPSHI","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q06696","disprot_id":"DP01611","ncbi_taxon_id":559292,"regions_counter":6,"creator":"nfoutel","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":395,"region_id":"DP01611r001","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Structure of the ESCRT-II endosomal trafficking complex. <i> Hierro A, Sun J, Rusnak AS, Kim J, Prag G, Emr SD, Hurley JH. </i> Nature, 2004","statement":[{"text":"The proteolytic susceptibility of the region connecting the second NZF motif at residue 203 and the start of the C-terminal domain at 396 suggests that a flexible linker connects these two domains.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":203,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"15329733","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":395,"region_id":"DP01611r002","reference_id":"15469844","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"No density is visible for residues 1–395 of Vps36","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"ESCRT-II, an endosome-associated complex required for protein sorting: crystal structure and interactions with ESCRT-III and membranes. <i> Teo H, Perisic O, González B, Williams RL. </i> Dev Cell, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1W7P"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":395,"region_id":"DP01611r003","reference_id":"15329733","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"it was determined that the crystallized complex contained a fragment of Vps36 comprising residues 396–566","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structure of the ESCRT-II endosomal trafficking complex. <i> Hierro A, Sun J, Rusnak AS, Kim J, Prag G, Emr SD, Hurley JH. </i> Nature, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1U5T"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":395,"region_id":"DP01611r004","reference_id":"15329733","start":203,"term_id":"IDPO:0000033","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The proteolytic susceptibility of the region connecting the second NZF motif at residue 203 and the start of the C-terminal domain at 396 suggests that a flexible linker connects these two domains","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cleavage assay evidence used in manual assertion","version":4,"reference_html":"Structure of the ESCRT-II endosomal trafficking complex. <i> Hierro A, Sun J, Rusnak AS, Kim J, Prag G, Emr SD, Hurley JH. </i> Nature, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","cross_refs":[{"db":"PDB","id":"1U5T"}],"term_name":"flexible linker","ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Biological process","ec_ontology":"ECO","end":205,"region_id":"DP01611r005","reference_id":"15329733","start":177,"term_id":"GO:0051179","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The N-terminal portion of Vps36 contains two copies of a NZF zinc-finger motif. The second NZF finger of Vps36 binds ubiquitin and is thought to be the main site of interaction between ESCRT-II and ubiquitinated cargo proteins","type":"Article"},{"text":"The second NZF finger, also known as Vps36-1, is also widely described in PMID:15029239 as it contains a 13TF14/Φ25 motif and binds Ub (Kd=182 μM), whereas the other NZF domain (Vps36‐2, residues 114-151) lacks this motif and does not bind Ub. Moreover, the Ub‐binding activity of the Vps36 NZF domain is required for efficient sorting of ubiquitylated substrates into the MVB.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"Structure of the ESCRT-II endosomal trafficking complex. <i> Hierro A, Sun J, Rusnak AS, Kim J, Prag G, Emr SD, Hurley JH. </i> Nature, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1U5T"}],"term_name":"localization","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":205,"region_id":"DP01611r006","reference_id":"15329733","start":177,"term_id":"GO:0005515","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The N-terminal portion of Vps36 contains two copies of a NZF zinc-finger motif. The second NZF finger of Vps36 binds ubiquitin and is thought to be the main site of interaction between ESCRT-II and ubiquitinated cargo proteins","type":"Article"},{"text":"The second NZF finger, also known as Vps36-1, is also widely described in PMID:15029239 as it contains a 13TF14/Φ25 motif and binds Ub (Kd=182 μM), whereas the other NZF domain (Vps36‐2, residues 114-151) lacks this motif and does not bind Ub. Moreover, the Ub‐binding activity of the Vps36 NZF domain is required for efficient sorting of ubiquitylated substrates into the MVB.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"Structure of the ESCRT-II endosomal trafficking complex. <i> Hierro A, Sun J, Rusnak AS, Kim J, Prag G, Emr SD, Hurley JH. </i> Nature, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1U5T"}],"term_name":"protein binding","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q06696","date":"2018-07-31T13:25:12.000Z","acc":"Q06696","name":"Vacuolar protein-sorting-associated protein 36","length":566,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000006BA9D","genes":[{"name":{"value":"VPS36"},"synonyms":[{"value":"GRD12"},{"value":"VAC3"},{"value":"VPL11"}],"olnNames":[{"value":"YLR417W"}]}],"alphafold_very_low_content":0.16431095406360424,"disorder_content":0.6978798586572438,"disprot_consensus":{"full":[{"start":1,"end":395,"type":"D"}],"Structural state":[{"start":1,"end":395,"type":"D"}],"Disorder function":[{"start":203,"end":395,"type":"F"}],"Biological process":[{"start":177,"end":205,"type":"F"}],"Molecular function":[{"start":177,"end":205,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04111","name":"Apg6 BARA domain","start":262,"end":443},{"id":"PF15285","name":"Beclin-1 BH3 domain, Bcl-2-interacting","start":103,"end":127},{"id":"PF17675","name":"Apg6 coiled-coil region","start":133,"end":259}],"gene3D":[{"start":239,"end":448,"id":"1.10.418.40","name":"Autophagy protein 6/Beclin 1"}]},"uniref50":"UniRef50_O88597","sequence":"MEGSKASSSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEEANSGEEPFIETRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEILEQMNEDDSEQLQRELKELALEEERLIQELEDVEKNRKVVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQVRYAQIQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_O88597","disprot_id":"DP01612","ncbi_taxon_id":10090,"regions_counter":1,"creator":"tszani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":150,"region_id":"DP01612r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural and biochemical bases for the inhibition of autophagy and apoptosis by viral BCL-2 of murine gamma-herpesvirus 68. <i> Ku B, Woo JS, Liang C, Lee KH, Hong HS, E X, Kim KS, Jung JU, Oh BH. </i> PLoS Pathog, 2008","term_id":"IDPO:0000002","curator_id":"tszani","start":124,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3bl2"}],"reference_id":"18248095","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_O88597","date":"2018-07-31T13:30:30.000Z","acc":"O88597","name":"Beclin-1","length":448,"organism":"Mus musculus","dataset":[],"UniParc":"UPI000052A045","genes":[{"name":{"value":"Becn1"}}],"alphafold_very_low_content":0.17633928571428573,"disorder_content":0.060267857142857144,"disprot_consensus":{"full":[{"start":124,"end":150,"type":"D"}],"Structural state":[{"start":124,"end":150,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00373","name":"FERM central domain","start":283,"end":332},{"id":"PF00373","name":"FERM central domain","start":457,"end":573},{"id":"PF18124","name":"Kindlin-2 N-terminal domain","start":13,"end":97}],"gene3D":[{"start":568,"end":662,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":373,"end":511,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":1,"end":100,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"}]},"uniref50":"UniRef50_Q96AC1","sequence":"MALDGIRMPDGCYADGTWELSVHVTDLNRDVTLRVTGEVHIGGVMLKLVEKLDVKKDWSDHALWWEKKRTWLLKTHWTLDKYGIQADAKLQFTPQHKLLRLQLPNMKYVKVKVNFSDRVFKAVSDICKTFNIRHPEELSLLKKPRDPTKKKKKKLDDQSEDEALELEGPLITPGSGSIYSSPGLYSKTMTPTYDAHDGSPLSPTSAWFGDSALSEGNPGILAVSQPITSPEILAKMFKPQALLDKAKINQGWLDSSRSLMEQDVKENEALLLRFKYYSFFDLNPKYDAIRINQLYEQAKWAILLEEIECTEEEMMMFAALQYHINKLSIMTSENHLNNSDKEVDEVDAALSDLEITLEGGKTSTILGDITSIPELADYIKVFKPKKLTLKGYKQYWCTFKDTSISCYKSKEESSGTPAHQMNLRGCEVTPDVNISGQKFNIKLLIPVAEGMNEIWLRCDNEKQYAHWMAACRLASKGKTMADSSYNLEVQNILSFLKMQHLNPDPQLIPEQITTDITPECLVSPRYLKKYKNKQITARILEAHQNVAQMSLIEAKMRFIQAWQSLPEFGITHFIARFQGGKKEELIGIAYNRLIRMDASTGDAIKTWRFSNMKQWNVNWEIKMVTVEFADEVRLSFICTEVDCKVVHEFIGGYIFLSTRAKDQNESLDEEMFYKLTSGWV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q96AC1","disprot_id":"DP01613","ncbi_taxon_id":9606,"regions_counter":8,"creator":"bhajdu","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":367,"region_id":"DP01613r001","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Molecular basis of kindlin-2 binding to integrin-linked kinase pseudokinase for regulating cell adhesion. <i> Fukuda K, Bledzka K, Yang J, Perera HD, Plow EF, Qin J. </i> J Biol Chem, 2014","statement":[{"text":"We then prepared 15N-labeled kindlin-2 residues 328–367 (termed K2F2N) (Fig. 4B). Fig. 4C shows that kindlin-2 residues 328–367 are largely unstructured but specifically bind to unlabeled ILK KLD·α-parvin CH2, with 16 kindlin-2 residues undergoing significant line-broadening and/or chemical shift perturbations including two characteristic glycine peaks.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":328,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-09-25T19:03:16.906Z","reference_source":"pmid","term_name":"disorder","reference_id":"25160619","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":357,"term_name":"protein binding","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Molecular basis of kindlin-2 binding to integrin-linked kinase pseudokinase for regulating cell adhesion. <i> Fukuda K, Bledzka K, Yang J, Perera HD, Plow EF, Qin J. </i> J Biol Chem, 2014","statement":[{"text":"We then prepared 15N-labeled kindlin-2 residues 328–367 (termed K2F2N) (Fig. 4B). Fig. 4C shows that kindlin-2 residues 328–367 are largely unstructured but specifically bind to unlabeled ILK KLD·α-parvin CH2, with 16 kindlin-2 residues undergoing significant line-broadening and/or chemical shift perturbations including two characteristic glycine peaks.","type":"Results"},{"text":"Using NMR, we further showed that 2H,15N-labeled HSQC spectrum of a double kindlin-2 F2 mutant (L353A and L357A; hereinafter referred to as LL/AA) exhibited a well dispersed spectrum that is similar to the wild type but has no chemical shift perturbation and line broadening upon addition of unlabeled ILK KLD·α-parvin CH2 (Fig. 5B). These data strongly suggest that the double amino acid substitution (LL/AA) completely abolished the kindlin-2 binding to ILK without perturbing the overall structure.","type":"Results"}],"term_id":"GO:0005515","curator_id":"vnugnes","start":350,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"25160619","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-09-25T19:08:20.283Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01613r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q13418","operator":"and","partner_start":null,"partner_end":null}]},{"region_id":"DP01613r006","ec_ontology":"ECO","end":15,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":1,"version":3,"statement":[{"text":"The structures are well converged except the N-terminal M1-D15 that appears to be highly flexible with few long range NOEs.","type":"Results"}],"term_name":"disorder","reference_html":"Membrane binding of the N-terminal ubiquitin-like domain of kindlin-2 is crucial for its regulation of integrin activation. <i> Perera HD, Ma YQ, Yang J, Hirbawi J, Plow EF, Qin J. </i> Structure, 2011","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"22078565","date":"2023-09-25T18:51:44.589Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2LGX"},{"db":"BMRB","id":"17827"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu27Val","start":null,"end":null,"position":null}],"sequence_construct":"GAMPDEFMALDGIRMPDGCYADGTWELSVHVTDVNRDVTLRVTGEVHIGGVMLKLVEKLDVKKDWSDHALWWEKKRTWLLKTHWTLDKYGIQADAKLQFTPQHKLLRLQLPN"},{"start":95,"end":105,"reference_id":"22078565","reference_source":"pmid","reference_html":"Membrane binding of the N-terminal ubiquitin-like domain of kindlin-2 is crucial for its regulation of integrin activation. <i> Perera HD, Ma YQ, Yang J, Hirbawi J, Plow EF, Qin J. </i> Structure, 2011","date":"2023-09-25T18:53:35.280Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu27Val","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"2LGX"},{"db":"BMRB","id":"17827"}],"region_id":"DP01613r007","sequence_construct":"GAMPDEFMALDGIRMPDGCYADGTWELSVHVTDVNRDVTLRVTGEVHIGGVMLKLVEKLDVKKDWSDHALWWEKKRTWLLKTHWTLDKYGIQADAKLQFTPQHKLLRLQLPN","statement":[{"text":"The structure of K2-N 1-94 was calculated according to standard protocols (95-105 were disordered and therefore excluded from the calculations). ","type":"Results"}]},{"start":350,"end":357,"reference_id":"25160619","reference_source":"pmid","reference_html":"Molecular basis of kindlin-2 binding to integrin-linked kinase pseudokinase for regulating cell adhesion. <i> Fukuda K, Bledzka K, Yang J, Perera HD, Plow EF, Qin J. </i> J Biol Chem, 2014","date":"2023-09-25T19:12:44.842Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val346Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu350Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu353Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu357Ala","start":null,"end":null,"position":null}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q13418","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01613r008","statement":[{"text":"Using GST pulldown binding experiments, we found that the four kindlin-2 F2 point mutants (V346A, L350A, L353A, or L357A) but not others abolished ILK binding (Fig. 5A).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_Q96AC1","date":"2018-07-31T14:56:50.000Z","acc":"Q96AC1","name":"Fermitin family homolog 2","length":680,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000073CC9","genes":[{"name":{"value":"FERMT2"},"synonyms":[{"value":"KIND2"},{"value":"MIG2"},{"value":"PLEKHC1"}]}],"alphafold_very_low_content":0.13088235294117648,"disorder_content":0.09705882352941177,"disprot_consensus":{"full":[{"start":1,"end":15,"type":"D"},{"start":95,"end":105,"type":"D"},{"start":328,"end":367,"type":"D"}],"Structural state":[{"start":1,"end":15,"type":"D"},{"start":95,"end":105,"type":"D"},{"start":328,"end":367,"type":"D"}],"Molecular function":[{"start":350,"end":357,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00605","name":"Interferon regulatory factor transcription factor","start":8,"end":110},{"id":"PF10401","name":"Interferon-regulatory factor 3","start":202,"end":379}],"gene3D":[{"start":187,"end":427,"id":"2.60.200.10","name":"2.60.200.10"},{"start":7,"end":113,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}]},"uniref50":"UniRef50_Q14653","sequence":"MGTPKPRILPWLVSQLDLGQLEGVAWVNKSRTRFRIPWKHGLRQDAQQEDFGIFQAWAEATGAYVPGRDKPDLPTWKRNFRSALNRKEGLRLAEDRSKDPHDPHKIYEFVNSGVGDFSQPDTSPDTNGGGSTSDTQEDILDELLGNMVLAPLPDPGPPSLAVAPEPCPQPLRSPSLDNPTPFPNLGPSENPLKRLLVPGEEWEFEVTAFYRGRQVFQQTISCPEGLRLVGSEVGDRTLPGWPVTLPDPGMSLTDRGVMSYVRHVLSCLGGGLALWRAGQWLWAQRLGHCHTYWAVSEELLPNSGHGPDGEVPKDKEGGVFDLGPFIVDLITFTEGSGRSPRYALWFCVGESWPQDQPWTKRLVMVKVVPTCLRALVEMARVGGASSLENTVDLHISNSHPLSLTSDQYKAYLQDLVEGMDFQGPGES","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q14653","disprot_id":"DP01614","ncbi_taxon_id":9606,"regions_counter":1,"creator":"mpajkos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":188,"region_id":"DP01614r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of IRF-3 reveals mechanism of autoinhibition and virus-induced phosphoactivation. <i> Qin BY, Liu C, Lam SS, Srinath H, Delston R, Correia JJ, Derynck R, Lin K. </i> Nat Struct Biol, 2003","statement":[{"text":"\"The N-terminal residues 173–188 were disordered. \"","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":173,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1QWT"}],"reference_id":"14555996","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q14653","date":"2018-07-31T15:21:04.000Z","acc":"Q14653","name":"Interferon regulatory factor 3","length":427,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012D88A","genes":[{"name":{"value":"IRF3","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9803267","url":"http://www.ncbi.nlm.nih.gov/pubmed/9803267","alternativeUrl":"https://europepmc.org/abstract/MED/9803267"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6118","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6118"}}]}}],"alphafold_very_low_content":0.17798594847775176,"disorder_content":0.03747072599531616,"disprot_consensus":{"full":[{"start":173,"end":188,"type":"D"}],"Structural state":[{"start":173,"end":188,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00518","name":"Early Protein (E6)","start":37,"end":146}],"gene3D":[{"start":6,"end":86,"id":"3.30.240.40","name":"E6 early regulatory protein"},{"start":87,"end":158,"id":"3.30.240.40","name":"E6 early regulatory protein"}]},"uniref50":"UniRef50_P03126","sequence":"MHQKRTAMFQDPQERPRKLPQLCTELQTTIHDIILECVYCKQQLLRREVYDFAFRDLCIVYRDGNPYAVCDKCLKFYSKISEYRHYCYSLYGTTLEQQYNKPLCDLLIRCINCQKPLCPEEKQRHLDKKQRFHNIRGRWTGRCMSCCRSSRTRRETQL","taxonomy":["Viruses","Monodnaviria","Shotokuvirae","Cossaviricota","Papovaviricetes","Zurhausenvirales","Papillomaviridae","Firstpapillomavirinae","Alphapapillomavirus"],"uniref90":"UniRef90_P03126","disprot_id":"DP01615","ncbi_taxon_id":333760,"regions_counter":10,"creator":"nfoutel","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":10,"region_id":"DP01615r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure analysis of the HPV16 E6 oncoprotein reveals a self-association mechanism required for E6-mediated degradation of p53. <i> Zanier K, ould M'hamed ould Sidi A, Boulade-Ladame C, Rybin V, Chappelle A, Atkinson A, Kieffer B, Travé G. </i> Structure, 2012","statement":[{"text":"The N-terminal region, corresponding to residues 1–10, adopts an extended and rather flexible structure as indicated by the low 1H-15N heteronuclear NOE values, which correlate with dynamic events in the nanosecond timescale.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"22483108","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2LJX"},{"db":"PDB","id":"2LJY"},{"db":"BMRB","id":"17967"},{"db":"BMRB","id":"17968"}],"curator_orcid":"0000-0001-8399-7907","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-20T11:15:14.897Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":158,"region_id":"DP01615r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural and functional analysis of E6 oncoprotein: insights in the molecular pathways of human papillomavirus-mediated pathogenesis. <i> Nominé Y, Masson M, Charbonnier S, Zanier K, Ristriani T, Deryckère F, Sibler AP, Desplancq D, Atkinson RA, Weiss E, Orfanoudakis G, Kieffer B, Travé G. </i> Mol Cell, 2006","statement":[{"text":"The C-terminal residues R141-L151, encompassing the PDZ binding motif (Thomas et al., 2002), adopt a random conformation.","type":"Results"},{"text":"The C-terminal 141-151 residues corresponds to the 148-158 region of the Uniprot entry, since residues are numbered as in the shorter transcript of HPV 16 E6. They use a E6 construct containing four Cys-Ser mutations, but they expect its structure to be identical to the wildtype because the mutated cysteins were not conserved in E6 alignments, the Cys/Ser change is relatively isosteric, the mutations did not prevent the domain from adopting a stable fold, all mutated positions turn out to be exposed on the surface of the calculated structure, and these mutations are also present in the full-length E6 6C/6S mutant displaying in vitro and in vivo p53 degradation properties indistinguishable from those of wild-type E6.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":148,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16507364","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2FK4"},{"db":"BMRB","id":"6707"}],"curator_orcid":"0000-0001-8399-7907","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-20T11:15:13.168Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":148,"end":158,"reference_id":"16507364","reference_source":"pmid","reference_html":"Structural and functional analysis of E6 oncoprotein: insights in the molecular pathways of human papillomavirus-mediated pathogenesis. <i> Nominé Y, Masson M, Charbonnier S, Zanier K, Ristriani T, Deryckère F, Sibler AP, Desplancq D, Atkinson RA, Weiss E, Orfanoudakis G, Kieffer B, Travé G. </i> Mol Cell, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2FK4"},{"db":"BMRB","id":"6707"}],"region_id":"DP01615r003","statement":[{"text":"The C-terminal residues R141-L151, encompassing the PDZ binding motif (Thomas et al., 2002), adopt a random conformation.","type":"Results"},{"text":" The N-terminal and C-terminal tails are highly variable in both length and sequence, but the interdomain linker has a fixed length in all HPV species and contains several highly conserved hydrophobic residues presenting the periodicity of a helix (Figure 2A).","type":"Results"},{"text":"The C-terminal 141-151 residues corresponds to the 148-158 region of the Uniprot entry, since residues are numbered as in the shorter transcript of HPV 16 E6. They use a E6 construct containing four Cys-Ser mutations, but they expect its structure to be identical to the wildtype because the mutated cysteins were not conserved in E6 alignments, the Cys/Ser change is relatively isosteric, the mutations did not prevent the domain from adopting a stable fold, all mutated positions turn out to be exposed on the surface of the calculated structure, and these mutations are also present in the full-length E6 6C/6S mutant displaying in vitro and in vivo p53 degradation properties indistinguishable from those of wild-type E6.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-20T11:15:32.809Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":148,"end":158,"reference_id":"31092861","reference_source":"pmid","reference_html":"Structural and functional characterization of the PDZ domain of the human phosphatase PTPN3 and its interaction with the human papillomavirus E6 oncoprotein. <i> Genera M, Samson D, Raynal B, Haouz A, Baron B, Simenel C, Guerois R, Wolff N, Caillet-Saguy C. </i> Sci Rep, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006232","ec_ontology":"ECO","ec_name":"differential scanning calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"P26045","partner_start":504,"partner_end":597}],"region_id":"DP01615r004","statement":[{"text":"For all the PBMs tested, an increase of 4 to 11 °C in the Tm was observed, showing that the PBM binding onto PTPN3-PDZ stabilizes the domain, whether the PBM is of cellular or viral origin.","type":"Results"},{"text":"The PBM region corresponds to the C-terminal 148-158 residues of the Human papillomavirus type 16 E6 protein. ","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-20T10:35:36.850Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":148,"end":158,"reference_id":"31092861","reference_source":"pmid","reference_html":"Structural and functional characterization of the PDZ domain of the human phosphatase PTPN3 and its interaction with the human papillomavirus E6 oncoprotein. <i> Genera M, Samson D, Raynal B, Haouz A, Baron B, Simenel C, Guerois R, Wolff N, Caillet-Saguy C. </i> Sci Rep, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"P26045","partner_start":504,"partner_end":597}],"region_id":"DP01615r005","statement":[{"text":"We obtained KD values of 29 μM, 53 μM and 37 μM for PTPN3-PDZ with HBVc PBM, HPV16E6 PBM and HPV18E6 PBM, respectively (Table 1). The KD values are all in the same tenth-of-micromolar range for the viral PBMs and are close to the one of the cellular partner p38γ. The measured affinities fall in the standard 0.1–100 μM range12 for PDZ-PBM interactions.","type":"Results"},{"text":"The PBM region corresponds to the C-terminal 148-158 residues of the Human papillomavirus type 16 E6 protein. ","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-20T10:35:31.452Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":148,"end":158,"reference_id":"31092861","reference_source":"pmid","reference_html":"Structural and functional characterization of the PDZ domain of the human phosphatase PTPN3 and its interaction with the human papillomavirus E6 oncoprotein. <i> Genera M, Samson D, Raynal B, Haouz A, Baron B, Simenel C, Guerois R, Wolff N, Caillet-Saguy C. </i> Sci Rep, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0030162","term_name":"regulation of proteolysis","term_namespace":"Biological process","term_ontology":"GO","term_xref":null,"ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"6HKS"}],"region_id":"DP01615r006","statement":[{"text":"HPV16E6 PBM binds to the PDZ domain as an anti-parallel extension of the β2-strand domain in a conventional mode.","type":"Results"},{"text":"The PBM region corresponds to the C-terminal 148-158 residues of the Human papillomavirus type 16 E6 protein. ","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-20T14:43:05.117Z"},"ec_go":"EXP","disprot_namespace":"Disorder function","term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of the hydrolysis of a peptide bond or bonds within a protein.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"term_is_binding":false},{"start":148,"end":158,"reference_id":"31092861","reference_source":"pmid","reference_html":"Structural and functional characterization of the PDZ domain of the human phosphatase PTPN3 and its interaction with the human papillomavirus E6 oncoprotein. <i> Genera M, Samson D, Raynal B, Haouz A, Baron B, Simenel C, Guerois R, Wolff N, Caillet-Saguy C. </i> Sci Rep, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"6HKS"}],"interaction_partner":[{"db":"UniProt","id":"P26045 ","partner_start":489,"partner_end":597}],"region_id":"DP01615r007","statement":[{"text":"HPV16E6 PBM binds to the PDZ domain as an anti-parallel extension of the β2-strand domain in a conventional mode.","type":"Results"},{"text":"The PBM region corresponds to the C-terminal 148-158 residues of the Human papillomavirus type 16 E6 protein. ","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-20T10:35:19.094Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":148,"end":158,"reference_id":"31092861","reference_source":"pmid","reference_html":"Structural and functional characterization of the PDZ domain of the human phosphatase PTPN3 and its interaction with the human papillomavirus E6 oncoprotein. <i> Genera M, Samson D, Raynal B, Haouz A, Baron B, Simenel C, Guerois R, Wolff N, Caillet-Saguy C. </i> Sci Rep, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0030162","term_name":"regulation of proteolysis","term_namespace":"Biological process","term_ontology":"GO","term_xref":null,"ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01615r008","statement":[{"text":"We obtained KD values of 29 μM, 53 μM and 37 μM for PTPN3-PDZ with HBVc PBM, HPV16E6 PBM and HPV18E6 PBM, respectively (Table 1). The KD values are all in the same tenth-of-micromolar range for the viral PBMs and are close to the one of the cellular partner p38γ. The measured affinities fall in the standard 0.1–100 μM range12 for PDZ-PBM interactions.","type":"Results"},{"text":"The PBM region corresponds to the C-terminal 148-158 residues of the Human papillomavirus type 16 E6 protein. ","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-20T14:43:06.565Z"},"ec_go":"EXP","disprot_namespace":"Disorder function","term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of the hydrolysis of a peptide bond or bonds within a protein.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"term_is_binding":false},{"start":148,"end":158,"reference_id":"31092861","reference_source":"pmid","reference_html":"Structural and functional characterization of the PDZ domain of the human phosphatase PTPN3 and its interaction with the human papillomavirus E6 oncoprotein. <i> Genera M, Samson D, Raynal B, Haouz A, Baron B, Simenel C, Guerois R, Wolff N, Caillet-Saguy C. </i> Sci Rep, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0030162","term_name":"regulation of proteolysis","term_namespace":"Biological process","term_ontology":"GO","term_xref":null,"ec_id":"ECO:0006232","ec_ontology":"ECO","ec_name":"differential scanning calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01615r009","statement":[{"text":"For all the PBMs tested, an increase of 4 to 11 °C in the Tm was observed, showing that the PBM binding onto PTPN3-PDZ stabilizes the domain, whether the PBM is of cellular or viral origin.","type":"Results"},{"text":"The PBM region corresponds to the C-terminal 148-158 residues of the Human papillomavirus type 16 E6 protein. ","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-21T07:37:45.768Z"},"ec_go":"IDA","disprot_namespace":"Disorder function","term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of the hydrolysis of a peptide bond or bonds within a protein.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"term_is_binding":false},{"start":1,"end":10,"reference_id":"22483108","reference_source":"pmid","reference_html":"Solution structure analysis of the HPV16 E6 oncoprotein reveals a self-association mechanism required for E6-mediated degradation of p53. <i> Zanier K, ould M'hamed ould Sidi A, Boulade-Ladame C, Rybin V, Chappelle A, Atkinson A, Kieffer B, Travé G. </i> Structure, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"BMRB","id":"17968"},{"db":"PDB","id":"2LJY"},{"db":"PDB","id":"2LJX"},{"db":"BMRB","id":"17967"}],"region_id":"DP01615r010","statement":[{"text":"The N-terminal region, corresponding to residues 1–10, adopts an extended and rather flexible structure as indicated by the low 1H-15N heteronuclear NOE values, which correlate with dynamic events in the nanosecond timescale.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-20T11:15:30.377Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_P03126","date":"2018-07-31T17:04:09.000Z","acc":"P03126","name":"Protein E6","length":158,"organism":"Human papillomavirus type 16","dataset":["Viral proteins"],"UniParc":"UPI000000138B","genes":[{"name":{"value":"E6","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04006","url":"https://hamap.expasy.org/unirule/MF_04006"}}]}}],"disorder_content":0.13291139240506328,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"},{"start":148,"end":158,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":148,"end":158,"type":"D"}],"Disorder function":[{"start":1,"end":10,"type":"F"},{"start":148,"end":158,"type":"F"}],"Molecular function":[{"start":148,"end":158,"type":"F"}],"Biological process":[{"start":148,"end":158,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02217","name":"Origin of replication binding protein","start":136,"end":229},{"id":"PF06431","name":"Polyomavirus large T antigen C-terminus","start":265,"end":681}],"gene3D":[{"start":1,"end":75,"id":"1.10.287.110","name":"DnaJ domain"},{"start":127,"end":255,"id":"3.40.1310.20","name":"3.40.1310.20"},{"start":356,"end":620,"id":"1.20.1050.70","name":"Large T antigen, SV40, domain 3"},{"start":397,"end":549,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":256,"end":355,"id":"1.10.10.510","name":"Zinc finger, large T-antigen D1 domain"}]},"uniref50":"UniRef50_P03070","sequence":"MDKVLNREESLQLMDLLGLERSAWGNIPLMRKAYLKKCKEFHPDKGGDEEKMKKMNTLYKKMEDGVKYAHQPDFGGFWDATEIPTYGTDEWEQWWNAFNEENLFCSEEMPSSDDEATADSQHSTPPKKKRKVEDPKDFPSELLSFLSHAVFSNRTLACFAIYTTKEKAALLYKKIMEKYSVTFISRHNSYNHNILFFLTPHRHRVSAINNYAQKLCTFSFLICKGVNKEYLMYSALTRDPFSVIEESLPGGLKEHDFNPEEAEETKQVSWKLVTEYAMETKCDDVLLLLGMYLEFQYSFEMCLKCIKKEQPSHYKYHEKHYANAAIFADSKNQKTICQQAVDTVLAKKRVDSLQLTREQMLTNRFNDLLDRMDIMFGSTGSADIEEWMAGVAWLHCLLPKMDSVVYDFLKCMVYNIPKKRYWLFKGPIDSGKTTLAAALLELCGGKALNVNLPLDRLNFELGVAIDQFLVVFEDVKGTGGESRDLPSGQGINNLDNLRDYLDGSVKVNLEKKHLNKRTQIFPPGIVTMNEYSVPKTLQARFVKQIDFRPKDYLKHCLERSEFLLEKRIIQSGIALLLMLIWYRPVAEFAQSIQSRIVEWKERLDKEFSLSVYQKMKFNVAMGIGVLDWLRNSDDDDEDSQENADKNEDGGEKNMEDSGHETGIDSQSQGSFQAPQSSQSVHDHNQPYHICRGFTCFKKPPTPPPEPET","taxonomy":["Viruses","Monodnaviria","Shotokuvirae","Cossaviricota","Papovaviricetes","Sepolyvirales","Polyomaviridae","Betapolyomavirus"],"uniref90":"UniRef90_P03070","disprot_id":"DP01618","ncbi_taxon_id":1891767,"regions_counter":7,"creator":"nfoutel","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":26,"region_id":"DP01618r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for the inactivation of retinoblastoma tumor suppressor by SV40 large T antigen. <i> Kim HY, Ahn BY, Cho Y. </i> EMBO J, 2001","statement":[{"text":"The N-terminal region of Tag can be divided in a  J-like domain and an extended loop (L4) containing the LxCxE sequence necessary for the interaction with the B box in Rb. PDB structure shows unstructured loops L1, L2 and L3 which are internal and allow proper folding of J-like domain. L2 contains the conserved HDB sequence that has been proved to be functionally important for interactions and chaperone-like activity","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":17,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"11226179","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":48,"region_id":"DP01618r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for the inactivation of retinoblastoma tumor suppressor by SV40 large T antigen. <i> Kim HY, Ahn BY, Cho Y. </i> EMBO J, 2001","statement":[{"text":"The N-terminal region of Tag can be divided in a  J-like domain and an extended loop (L4) containing the LxCxE sequence necessary for the interaction with the B box in Rb. PDB structure shows unstructured loops L1, L2 and L3 which are internal and allow proper folding of J-like domain. L2 contains the conserved HDB sequence that has been proved to be functionally important for interactions and chaperone-like activity","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":39,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"11226179","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":48,"term_name":"protein binding","start":39,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","statement":[{"text":"The importance of loop L2 is indicated by the strong conservation of the HPD sequence in all J domains (Tsai and Douglas, 1996). Large T antigen mutants in this region are unable to dissociate E2F from Rb and are, as a consequence, replication defective. Also, DnaJ mutants in this region have lost their chaperone function (Srinivasan et al., 1997).","type":"Results"}],"curator_id":"nfoutel","released":"2022_03","term_ontology":"GO","curator_name":"Nicolas Foutel","reference_id":"11226179","version":3,"reference_html":"Structural basis for the inactivation of retinoblastoma tumor suppressor by SV40 large T antigen. <i> Kim HY, Ahn BY, Cho Y. </i> EMBO J, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP01618r003","uniprot_changed":true,"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":87,"region_id":"DP01618r005","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for the inactivation of retinoblastoma tumor suppressor by SV40 large T antigen. <i> Kim HY, Ahn BY, Cho Y. </i> EMBO J, 2001","statement":[{"text":"The N-terminal region of Tag can be divided in a  J-like domain and an extended loop (L4) containing the LxCxE sequence necessary for the interaction with the B box in Rb. PDB structure shows unstructured loops L1, L2 and L3 which are internal and allow proper folding of J-like domain. L2 contains the conserved HDB sequence that has been proved to be functionally important for interactions and chaperone-like activity","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":68,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"11226179","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":117,"region_id":"DP01618r006","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for the inactivation of retinoblastoma tumor suppressor by SV40 large T antigen. <i> Kim HY, Ahn BY, Cho Y. </i> EMBO J, 2001","statement":[{"text":"The N-terminal region of Tag can be divided in a  J-like domain and an extended loop (L4) containing the LxCxE sequence necessary for the interaction with the B box in Rb. PDB structure shows unstructured loops L1, L2 and L3 which are internal and allow proper folding of J-like domain. L2 contains the conserved HDB sequence that has been proved to be functionally important for interactions and chaperone-like activity","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":103,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"11226179","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","uniprot_changed":true,"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":117,"term_name":"protein binding","start":103,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","statement":[{"text":"The loop containing the LxCxE motifs forms an extended conformation and binds to the shallow surface groove on the B box created by five helices, three of which are from the cyclin box (in Rb).","type":"Results"}],"curator_id":"nfoutel","released":"2022_03","term_ontology":"GO","curator_name":"Nicolas Foutel","reference_id":"11226179","version":3,"reference_html":"Structural basis for the inactivation of retinoblastoma tumor suppressor by SV40 large T antigen. <i> Kim HY, Ahn BY, Cho Y. </i> EMBO J, 2001","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP01618r007","uniprot_changed":true,"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P03070","date":"2018-07-31T17:10:12.000Z","acc":"P03070","name":"Large T antigen","length":708,"organism":"Simian virus 40","dataset":["Viral proteins"],"uniparc":"UPI00000F2C4A","genes":[],"disorder_content":0.07768361581920905,"disprot_consensus":{"full":[{"start":17,"end":26,"type":"D"},{"start":39,"end":48,"type":"D"},{"start":68,"end":87,"type":"D"},{"start":103,"end":117,"type":"D"}],"Structural state":[{"start":17,"end":26,"type":"D"},{"start":39,"end":48,"type":"D"},{"start":68,"end":87,"type":"D"},{"start":103,"end":117,"type":"D"}],"Molecular function":[{"start":39,"end":48,"type":"F"},{"start":103,"end":117,"type":"F"}]}},{"features":{"pfam":[{"id":"PF09057","name":"Second Mitochondria-derived Activator of Caspases","start":10,"end":239}],"gene3D":[{"start":56,"end":239,"id":"1.20.58.70","name":"1.20.58.70"}]},"uniref50":"UniRef50_Q9NR28","sequence":"MAALKSWLSRSVTSFFRYRQCLCVPVVANFKKRCFSELIRPWHKTVTIGFGVTLCAVPIAQKSEPHSLSSEALMRRAVSLVTDSTSTFLSQTTYALIEAITEYTKAVYTLTSLYRQYTSLLGKMNSEEEDEVWQVIIGARAEMTSKHQEYLKLETTWMTAVGLSEMAAEAAYQTGADQASITARNHIQLVKLQVEEVHQLSRKAETKLAEAQIEELRQKTQEEGEERAESEQEAYLRED","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9NR28","disprot_id":"DP01619","ncbi_taxon_id":9606,"regions_counter":5,"creator":"nfoutel","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":69,"region_id":"DP01619r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The activator of apoptosis Smac-DIABLO acts as a tetramer in solution. <i> Mastrangelo E, Vachette P, Cossu F, Malvezzi F, Bolognesi M, Milani M. </i> Biophys J, 2015","statement":[{"text":"The authors solved a structure with two molecules of Smac/DIABLO in the crystal as a dimer. In their final model, no electron density was seen for the 14 first residues in the N terminal region in Chain A and for the 12 first residues in Chain B, confirming that this protein region is highly mobile in the absence of interaction with BIR domains partners.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":56,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"25650938","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":67,"region_id":"DP01619r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The activator of apoptosis Smac-DIABLO acts as a tetramer in solution. <i> Mastrangelo E, Vachette P, Cossu F, Malvezzi F, Bolognesi M, Milani M. </i> Biophys J, 2015","statement":[{"text":"The authors solved a structure with two molecules of Smac/DIABLO in the crystal as a dimer. In their final model, no electron density was seen for the 14 first residues in the N terminal region in Chain A and for the 12 first residues in Chain B, confirming that this protein region is highly mobile in the absence of interaction with BIR domains partners.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":56,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"25650938","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":70,"region_id":"DP01619r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for recognition of H3T3ph and Smac/DIABLO N-terminal peptides by human Survivin. <i> Du J, Kelly AE, Funabiki H, Patel DJ. </i> Structure, 2012","statement":[{"text":"The authors could only trace the N-terminal segment (residues 56 to 59) of the bound peptide in the complex SmacN-Survivin in the crystal structure. Due to missing electron density the C terminal (60-70) could not be solved. The extended interaction and the missing residues suggest this region is disordered in solution in its unbound form.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":56,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"22244766","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":70,"term_name":"protein binding","start":56,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_id":"nfoutel","released":"2022_03","term_ontology":"GO","curator_name":"Nicolas Foutel","reference_id":"22244766","version":3,"reference_html":"Structural basis for recognition of H3T3ph and Smac/DIABLO N-terminal peptides by human Survivin. <i> Du J, Kelly AE, Funabiki H, Patel DJ. </i> Structure, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP01619r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":65,"region_id":"DP01619r005","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural and biochemical basis of apoptotic activation by Smac/DIABLO. <i> Chai J, Du C, Wu JW, Kyin S, Wang X, Shi Y. </i> Nature, 2000","statement":[{"text":"In the mature form of Smac (1-186), residue 1 corresponds to residue 56 of unprocessed Smac (1- 239). For this mature form, no electron density is seen corresponding to the N-terminal 10 residues suggesting this segment is disordered in solution.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":56,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"10972280","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9NR28","date":"2018-07-31T17:14:11.000Z","acc":"Q9NR28","name":"Diablo homolog, mitochondrial","length":239,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000000CBE","genes":[{"name":{"value":"DIABLO","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:21528","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:21528"}}]},"synonyms":[{"value":"SMAC","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:21528","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:21528"}}]}]}],"alphafold_very_low_content":0.11715481171548117,"disorder_content":0.06276150627615062,"disprot_consensus":{"full":[{"start":56,"end":70,"type":"D"}],"Structural state":[{"start":56,"end":70,"type":"D"}],"Molecular function":[{"start":56,"end":70,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04812","name":"Hepatocyte nuclear factor 1 (HNF-1), beta isoform C terminus","start":282,"end":540},{"id":"PF04813","name":"Hepatocyte nuclear factor 1 (HNF-1), alpha isoform C terminus","start":542,"end":630},{"id":"PF04814","name":"Hepatocyte nuclear factor 1 (HNF-1), N terminus","start":8,"end":168}],"gene3D":[{"start":193,"end":288,"id":"1.10.10.60","name":"Homeodomain-like"},{"start":84,"end":181,"id":"1.10.260.40","name":"lambda repressor-like DNA-binding domains"}]},"uniref50":"UniRef50_P20823","sequence":"MVSKLSQLQTELLAALLESGLSKEALIQALGEPGPYLLAGEGPLDKGESCGGGRGELAELPNGLGETRGSEDETDDDGEDFTPPILKELENLSPEEAAHQKAVVETLLQEDPWRVAKMVKSYLQQHNIPQREVVDTTGLNQSHLSQHLNKGTPMKTQKRAALYTWYVRKQREVAQQFTHAGQGGLIEEPTGDELPTKKGRRNRFKWGPASQQILFQAYERQKNPSKEERETLVEECNRAECIQRGVSPSQAQGLGSNLVTEVRVYNWFANRRKEEAFRHKLAMDTYSGPPPGPGPGPALPAHSSPGLPPPALSPSKVHGVRYGQPATSETAEVPSSSGGPLVTVSTPLHQVSPTGLEPSHSLLSTEAKLVSAAGGPLPPVSTLTALHSLEQTSPGLNQQPQNLIMASLPGVMTIGPGEPASLGPTFTNTGASTLVIGLASTQAQSVPVINSMGSSLTTLQPVQFSQPLHPSYQQPLMPPVQSHVTQSPFMATMAQLQSPHALYSHKPEVAQYTHTGLLPQTMLITDTTNLSALASLTPTKQVFTSDTEASSESGLHTPASQATTLHVPSQDPASIQHLQPAHRLSASPTVSSSSLVLYQSSDSSNGQSHLLPSNHSVIETFISTQMASSSQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P20823","disprot_id":"DP01620","ncbi_taxon_id":9606,"regions_counter":2,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":200,"region_id":"DP01620r001","released":"2022_06","ec_id":"ECO:0006220","reference_html":"Diabetes mutations delineate an atypical POU domain in HNF-1alpha. <i> Chi YI, Frantz JD, Oh BC, Hansen L, Dhe-Paganon S, Shoelson SE. </i> Mol Cell, 2002","statement":[{"text":"The linker between POUS and POUH domains (residues 182–200) is disordered. Nevertheless, connectivity between domains was established based on crystal packing and distance considerations (Figure 2A). The presence of neighboring molecules in the crystal lattice precludes the alternative configuration.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":181,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-24T15:09:29.779Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1IC8"}],"reference_id":"12453420","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting DNA with sequence 5'-CTTGGTTAATAATTCACCAGA."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-26T16:39:37.430Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":200,"term_name":"flexible linker","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Diabetes mutations delineate an atypical POU domain in HNF-1alpha. <i> Chi YI, Frantz JD, Oh BC, Hansen L, Dhe-Paganon S, Shoelson SE. </i> Mol Cell, 2002","term_id":"IDPO:0000033","curator_id":"vnugnes","start":181,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12453420","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-24T15:09:58.755Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01620r002","ec_go":"EXP","disprot_namespace":"Disorder function","cross_refs":[{"db":"PDB","id":"1IC8"}],"statement":[{"text":"The linker between POUS and POUH domains (residues 182–200) is disordered. Nevertheless, connectivity between domains was established based on crystal packing and distance considerations (Figure 2A). The presence of neighboring molecules in the crystal lattice precludes the alternative configuration.","type":"Results"}],"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting DNA with sequence 5'-CTTGGTTAATAATTCACCAGA."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-26T16:39:41.368Z"}}],"released":"2018_11","uniref100":"UniRef100_P20823","date":"2018-08-01T08:29:08.000Z","acc":"P20823","name":"Hepatocyte nuclear factor 1-alpha","length":631,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI000012CA94","genes":[{"name":{"value":"HNF1A"},"synonyms":[{"value":"TCF1"}]}],"alphafold_very_low_content":0.6148969889064976,"disorder_content":0.03169572107765452,"disprot_consensus":{"full":[{"start":181,"end":200,"type":"D"}],"Structural state":[{"start":181,"end":200,"type":"D"}],"Disorder function":[{"start":181,"end":200,"type":"F"}]}},{"acc":"E5LC01","sequence":"MAPPGMRLRSGRSTGAPLTRGSCRKRNRSPERCDLGNDLHLQPRRKHVADSVDGRECGPHTLPIPGSPTVFTSGLPAFVSSPTLPVAPIPSPAPATPLPPPALLSPVTTSSSPIPPSHPVSPGTTDTHSPSPALPPTQSPESSQRPPLSSPTGRPDSSTPMRPPPSQQTTPPHSPTTPPPEPPSKSSPDSLAPSTLRSLRKRRLSSPQGPSTLNPICQSPPVSPPRCDFANRSVYPPWATESPIYVGSSSDGDTPPRQPPTSPISIGSSSPSEGSWGDDTAMLVLLAEIAEEASKNEKECSENNQAGEDNGDNEISKESQVDKDDNDNKDDEEEQETDEDDEEDDEEDDEEDDEEDDEEDDEEDDEEDDEEDDEEDDEEDDEEDDEEEDEEEDEEEEEDEEDDDDEDNEDEEDDEEEDKKEDEEDGGDGNKTLSIQSSQQQQEPQQQEPQQQEPQQQEPLQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQREPQQQEPQQREPQQQEPQQREPQQREPQQREPQQREPQQREPQQREPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQEQQDEQQQQDEQQQQDEQQQQDEQQQEEQEQQEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQEQELEEVEEQEQEQEEQELEEVEEQEQEQEEQEEQELEEVEEQEEQELEEVEEQEEQELEEVEEQEQQGVEQQEQETVEEPIILHGSSSEDEMEVDYPVVSTHEQIASSPPGDNTPDDDPQPGPSREYRYVLRTSPPHRPGVRMRRVPVTHPKKPHPRYQQPPVPYRQIDDCPAKARPQHIFYRRFLGKDGRRDPKCQWKFAVIFWGNDPYGLKKLSQAFQFGGVKAGPVSCLPHLGPDQSPITYCVYVYCQNKDTSKKVQMARLAWEASHPLAGNLQSSIVKFKKPLPLTQPGENQGPGDSPQEMT","creator":"bhajdu","dataset":["Viral proteins"],"date":"2018-08-01T11:58:43.000Z","disprot_id":"DP01621","features":{"gene3D":[{"start":961,"end":1101,"id":"3.30.70.390","name":"Epstein Barr virus nuclear antigen-1, DNA-binding domain","_id":"685af523b4ac24d5329d919a"}],"pfam":[{"id":"PF21501","name":"Protein LANA1-like, DNA-binding domain","start":983,"end":1100}]},"genes":[{"name":{"value":"ORF73","evidences":[{"source":{"id":"ADQ57959.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/ADQ57959.1","_id":"685af523b4ac24d5329d91c4"},"code":"ECO:0000313","_id":"685af523b4ac24d5329d91c3"}],"_id":"685af523b4ac24d5329d91c5"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d91c2"}],"length":1117,"name":"LANA","ncbi_taxon_id":37296,"organism":"Human herpesvirus 8","regions_counter":8,"released":"2018_11","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Peploviricota","Herviviricetes","Herpesvirales","Herpesviridae","Gammaherpesvirinae","Rhadinovirus"],"UniParc":"UPI0001F25996","uniref100":"UniRef100_E5LC01","uniref50":"UniRef50_Q9QR71","uniref90":"UniRef90_Q9QR71","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"DisProt","id":"DP02334r001","_id":"685af523b4ac24d5329d919e"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1065,"end":1117,"interaction_partner":[],"reference_html":"Structural Mechanism of Transcriptional Regulator NSD3 Recognition by the ET Domain of BRD4. <i> Zhang Q, Zeng L, Shen C, Ju Y, Konuma T, Zhao C, Vakoc CR, Zhou MM. </i> Structure, 2016","reference_id":"27291650","region_id":"DP01621r001","released":"2022_03","sample":[],"sequence_construct":"DTSKKVQMARLAWEASHPLAGNLQSSIVKFKKPLPLTQPGENQGPGDSPQEMT","statement":[{"type":"Results","text":"Our observation of very narrow 1H chemical shift dispersion of merely 0.9 ppm (7.7–8.6 ppm) in the 15N-HSQC spectrum of LANA C-terminal fragment (residues 1110–1162) indicates that this region is unstructured (Figure S1A).","_id":"685af523b4ac24d5329d919c"},{"type":"Curator statement","text":"The LANA gene fragment used in this publication was derived from the Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus). IDR is 100% identical and corresponds to 1065-1117 region.","_id":"685af523b4ac24d5329d919d"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-27T08:50:49.817Z","_id":"685af523b4ac24d5329d919f"},"version":3,"_id":"685af523b4ac24d5329d919b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2ND0","_id":"685af523b4ac24d5329d91a9"},{"db":"BMRB","id":"26042","_id":"685af523b4ac24d5329d91aa"},{"db":"DisProt","id":"DP02334r004","_id":"685af523b4ac24d5329d91ab"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1086,"end":1104,"interaction_partner":[{"db":"UniProt","id":"O60885","partner_start":601,"partner_end":683,"_id":"685af523b4ac24d5329d91ac"}],"reference_html":"Structural Mechanism of Transcriptional Regulator NSD3 Recognition by the ET Domain of BRD4. <i> Zhang Q, Zeng L, Shen C, Ju Y, Konuma T, Zhao C, Vakoc CR, Zhou MM. </i> Structure, 2016","reference_id":"27291650","region_id":"DP01621r003","released":"2022_03","sample":[],"sequence_construct":"DTSKKVQMARLAWEASHPLAGNLQSSIVKFKKPLPLTQPGENQGPGDSPQEMT","statement":[{"type":"Results","text":"We thus constructed a BRD4 ET domain fused at its N-terminus to LANA comprising residues 1110–1162 via a flexible linker (GSGSGS), and determined by NMR analysis that the minimal ET binding site in LANA is confined to residues 1131–1149 (NLQSSIVKFKKPLPLTQPG) (data not shown). Notably, the 15N-HSQC spectra of the ET domain displayed nearly identical protein backbone resonance perturbation patterns induced by adding a LANA segment consisting of residues 1110–1162 or 1131–1149 (Figure S1A), or a LANA peptide of residues 1133–1144 (Figure 1B, red vs. blue signals), thereby defining the ET domain binding site in LANA to residues 1133–1144. We further determined binding affinity of the ET domain to the LANA peptide by NMR titration to be approximately Kd = 635 μM (Figure S1A).","_id":"685af523b4ac24d5329d91a7"},{"type":"Curator statement","text":"The LANA gene fragment used in this publication was derived from the Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus). IDR is 100% identical and corresponds to 1086-1104 region.","_id":"685af523b4ac24d5329d91a8"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-27T08:50:52.822Z","_id":"685af523b4ac24d5329d91ad"},"version":4,"_id":"685af523b4ac24d5329d91a6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2ND0","_id":"685af523b4ac24d5329d91b1"},{"db":"BMRB","id":"26042","_id":"685af523b4ac24d5329d91b2"},{"db":"DisProt","id":"DP02334r003","_id":"685af523b4ac24d5329d91b3"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1086,"end":1104,"interaction_partner":[],"reference_html":"Structural Mechanism of Transcriptional Regulator NSD3 Recognition by the ET Domain of BRD4. <i> Zhang Q, Zeng L, Shen C, Ju Y, Konuma T, Zhao C, Vakoc CR, Zhou MM. </i> Structure, 2016","reference_id":"27291650","region_id":"DP01621r004","released":"2022_03","sample":[],"sequence_construct":"DTSKKVQMARLAWEASHPLAGNLQSSIVKFKKPLPLTQPGENQGPGDSPQEMT","statement":[{"type":"Results","text":"We next solved the three-dimensional structure of the BRD4 ET domain bound to the LANA peptide (residues 1133–1144) using heteronuclear multidimensional NMR spectroscopy (Clore and Gronenborn, 1994) (Figure 1C and Table 1). The structure reveals that the viral peptide establishes a two-strand inter-molecular antiparallel β-sheet with the protein.","_id":"685af523b4ac24d5329d91af"},{"type":"Curator statement","text":"The LANA gene fragment used in this publication was derived from the Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus). IDR is 100% identical and corresponds to 1086-1104 region.","_id":"685af523b4ac24d5329d91b0"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-27T08:50:51.359Z","_id":"685af523b4ac24d5329d91b4"},"version":3,"_id":"685af523b4ac24d5329d91ae","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"amonzon","curator_name":"Alex Monzon","curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IC","ec_id":"ECO:0007759","ec_name":"curator inference from database used in manual assertion","ec_ontology":"ECO","start":640,"end":880,"interaction_partner":[],"reference_html":"An Entry Referenced from MobiDB","reference_id":"https://mobidb.org/E5LC01","region_id":"DP01621r005","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"This poly-E region is inferred by the curator to be disordered, based on MobiDB-Lite and according to experimental evidence demonstrating that poly-E repeats display random-coil-like conformation (PMID:16949547)","_id":"685af523b4ac24d5329d91b6"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":1,"_id":"685af523b4ac24d5329d91b5","reference_source":"mobidb"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"amonzon","curator_name":"Alex Monzon","curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IC","ec_id":"ECO:0007759","ec_name":"curator inference from database used in manual assertion","ec_ontology":"ECO","start":325,"end":423,"interaction_partner":[],"reference_html":"An Entry Referenced from MobiDB","reference_id":"https://mobidb.org/E5LC01","region_id":"DP01621r006","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"This poly-E region is inferred by the curator to be disordered, based on MobiDB-Lite and according to experimental evidence demonstrating that poly-E repeats display random-coil-like conformation (PMID:16949547)","_id":"685af523b4ac24d5329d91b8"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":1,"_id":"685af523b4ac24d5329d91b7","reference_source":"mobidb"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"amonzon","curator_name":"Alex Monzon","curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IC","ec_id":"ECO:0007759","ec_name":"curator inference from database used in manual assertion","ec_ontology":"ECO","start":586,"end":625,"interaction_partner":[],"reference_html":"An Entry Referenced from MobiDB","reference_id":"https://mobidb.org/E5LC01","region_id":"DP01621r007","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"This poly-E region is inferred by the curator to be disordered, based on MobiDB-Lite and according to experimental evidence demonstrating that poly-E repeats display random-coil-like conformation (PMID:16949547)","_id":"685af523b4ac24d5329d91ba"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":1,"_id":"685af523b4ac24d5329d91b9","reference_source":"mobidb"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2ND0","_id":"685af523b4ac24d5329d91bc"},{"db":"BMRB","id":"26042","_id":"685af523b4ac24d5329d91bd"},{"db":"DisProt","id":"DP02334r015","_id":"685af523b4ac24d5329d91be"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1086,"end":1104,"interaction_partner":[],"reference_html":"Structural Mechanism of Transcriptional Regulator NSD3 Recognition by the ET Domain of BRD4. <i> Zhang Q, Zeng L, Shen C, Ju Y, Konuma T, Zhao C, Vakoc CR, Zhou MM. </i> Structure, 2016","reference_id":"27291650","region_id":"DP01621r008","released":"2022_03","sample":[],"sequence_construct":"DTSKKVQMARLAWEASHPLAGNLQSSIVKFKKPLPLTQPGENQGPGDSPQEMT","statement":[{"type":"Results","text":"We thus constructed a BRD4 ET domain fused at its N-terminus to LANA comprising residues 1110–1162 via a flexible linker (GSGSGS), and determined by NMR analysis that the minimal ET binding site in LANA is confined to residues 1131–1149 (NLQSSIVKFKKPLPLTQPG) (data not shown). Notably, the 15N-HSQC spectra of the ET domain displayed nearly identical protein backbone resonance perturbation patterns induced by adding a LANA segment consisting of residues 1110–1162 or 1131–1149 (Figure S1A), or a LANA peptide of residues 1133–1144 (Figure 1B, red vs. blue signals), thereby defining the ET domain binding site in LANA to residues 1133–1144. We further determined binding affinity of the ET domain to the LANA peptide by NMR titration to be approximately Kd = 635 μM (Figure S1A).","_id":"685af523b4ac24d5329d91bf"},{"type":"Curator statement","text":"The LANA gene fragment used in this publication was derived from the Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus). IDR is 100% identical and corresponds to 1086-1104 region.","_id":"685af523b4ac24d5329d91c0"}],"states_connection":[],"term_comment":"","term_def":"\"A set of processes which all viruses follow to ensure survival; includes attachment and entry of the virus particle, decoding of genome information, translation of viral mRNA by host ribosomes, genome replication, and assembly and release of viral particles containing the genome.\" [ISBN:1555811272]","term_go_domain":"P","term_id":"GO:0019058","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral life cycle","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-27T08:50:54.746Z","_id":"685af523b4ac24d5329d91c1"},"version":1,"_id":"685af523b4ac24d5329d91bb","reference_source":"pmid"}],"__v":0,"disorder_content":0.38764547896150403,"disprot_consensus":{"full":[{"start":325,"end":423,"type":"D"},{"start":586,"end":625,"type":"D"},{"start":640,"end":880,"type":"D"},{"start":1065,"end":1085,"type":"D"},{"start":1086,"end":1104,"type":"T"},{"start":1105,"end":1117,"type":"D"}],"Structural state":[{"start":325,"end":423,"type":"D"},{"start":586,"end":625,"type":"D"},{"start":640,"end":880,"type":"D"},{"start":1065,"end":1117,"type":"D"}],"Molecular function":[{"start":1086,"end":1104,"type":"F"}],"Structural transition":[{"start":1086,"end":1104,"type":"T"}],"Biological process":[{"start":1086,"end":1104,"type":"F"}]}},{"features":{"pfam":[{"id":"PF08423","name":"Rad51","start":95,"end":337},{"id":"PF14520","name":"SAM-like Helix-hairpin-helix tandem","start":32,"end":79}],"gene3D":[{"start":97,"end":339,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":1,"end":85,"id":"1.10.150.20","name":"5' to 3' exonuclease, C-terminal subdomain"}]},"uniref50":"UniRef50_Q06609","sequence":"MAMQMQLEANADTSVEEESFGPQPISRLEQCGINANDVKKLEEAGFHTVEAVAYAPKKELINIKGISEAKADKILAEAAKLVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARAFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGDAKD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q06609","disprot_id":"DP01622","ncbi_taxon_id":9606,"regions_counter":8,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":15,"region_id":"DP01622r001","released":"2022_03","ec_id":"ECO:0006198","reference_html":"The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR. <i> Aihara H, Ito Y, Kurumizaka H, Yokoyama S, Shibata T. </i> J Mol Biol, 1999","statement":[{"text":"Residues 1 to 15 and 86 to 114 are disordered as judged by narrower 1H NMR linewidths compared with that of the structured region of the polypeptide, presence of strong HN-H2O crosspeaks in the 15N-separated NOESY spectrum (Marion et al., 1989), and the absence of long range nuclear Overhauser enhancement (NOE) signals.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"akajava","start":1,"term_ontology":"IDPO","curator_name":"Andrey V Kajava","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-2342-6886","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1B22"}],"reference_id":"10390347","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-24T18:16:19.446Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":114,"region_id":"DP01622r002","released":"2022_03","ec_id":"ECO:0006198","reference_html":"The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR. <i> Aihara H, Ito Y, Kurumizaka H, Yokoyama S, Shibata T. </i> J Mol Biol, 1999","statement":[{"text":"Residues 1 to 15 and 86 to 114 are disordered as judged by narrower 1H NMR linewidths compared with that of the structured region of the polypeptide, presence of strong HN-H2O crosspeaks in the 15N-separated NOESY spectrum (Marion et al., 1989), and the absence of long range nuclear Overhauser enhancement (NOE) signals.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"akajava","start":86,"term_ontology":"IDPO","curator_name":"Andrey V Kajava","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-2342-6886","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1B22"}],"reference_id":"10390347","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-24T18:16:13.815Z"}},{"start":1,"end":21,"reference_id":"27941862","reference_source":"pmid","reference_html":"Cryo-EM structures of human RAD51 recombinase filaments during catalysis of DNA-strand exchange. <i> Xu J, Zhao L, Xu Y, Zhao W, Sung P, Wang HW. </i> Nat Struct Mol Biol, 2017","date":"2022-08-24T18:13:37.274Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-9567"},{"db":"PDB","id":"5H1B"},{"db":"PDB","id":"5H1C"},{"db":"EMDB","id":"EMD-9566"}],"region_id":"DP01622r005","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting nucleic acid with sequence 5'TTTTTTTTT."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"47785","entry_name":"AMP-PNP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"}],"statement":[{"text":"The atomic models include DNA and most of the residues of RAD51 except for the N-terminal 1-21 residues and a few residues in flexible loop regions.","type":"Results"}]},{"start":273,"end":282,"reference_id":"41337480","reference_source":"pmid","reference_html":"RAD51AP1 is a versatile RAD51 modulator. <i> Kuhlen L, Argunhan B, Liang P, Zhong J, Masino L, Zhang X. </i> Proc Natl Acad Sci U S A, 2025","date":"2025-12-22T13:33:29.383Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"9QNB"}],"region_id":"DP01622r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":null}],"statement":[{"text":"Comparing the two structures, we observe the unfolding of the L2 region, losing its α-helix adjacent to the γ-phosphate as well as the β-hairpin, in the ADP bound RAD51 filament (Fig. 3F).","type":"Results"}]},{"start":273,"end":282,"reference_id":"41337480","reference_source":"pmid","reference_html":"RAD51AP1 is a versatile RAD51 modulator. <i> Kuhlen L, Argunhan B, Liang P, Zhong J, Masino L, Zhang X. </i> Proc Natl Acad Sci U S A, 2025","date":"2025-12-22T13:43:06.766Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"9QNB"},{"db":"PDB","id":"9QNC"}],"region_id":"DP01622r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15422","entry_name":null}],"statement":[{"text":"Comparing the two structures, we observe the unfolding of the L2 region, losing its α-helix adjacent to the γ-phosphate as well as the β-hairpin, in the ADP bound RAD51 filament (Fig. 3F).","type":"Results"},{"text":"Looking closer into the structural changes within RAD51, we observe that upon RAD51AP1 binding, the binding pocket, especially around Site-M, remodels to accommodate the peptide. Interestingly, we now observe density for the entire L2 region (Fig. 4F), for which the density of the tip was missing in the RAD51-ssDNA structures, suggesting L2 adopts a more rigid conformation upon RAD51AP1 binding.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","states_connection":[{"source":"DP01622r006","target":"DP01622r008"}]},{"start":273,"end":282,"reference_id":"41337480","reference_source":"pmid","reference_html":"RAD51AP1 is a versatile RAD51 modulator. <i> Kuhlen L, Argunhan B, Liang P, Zhong J, Masino L, Zhang X. </i> Proc Natl Acad Sci U S A, 2025","date":"2025-12-22T13:42:08.610Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"9QNC"}],"region_id":"DP01622r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15422","entry_name":null}],"statement":[{"text":"Looking closer into the structural changes within RAD51, we observe that upon RAD51AP1 binding, the binding pocket, especially around Site-M, remodels to accommodate the peptide. Interestingly, we now observe density for the entire L2 region (Fig. 4F), for which the density of the tip was missing in the RAD51-ssDNA structures, suggesting L2 adopts a more rigid conformation upon RAD51AP1 binding.","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_Q06609","date":"2018-08-02T13:47:35.000Z","acc":"Q06609","name":"DNA repair protein RAD51 homolog 1","length":339,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000000D8D2","genes":[{"name":{"value":"RAD51","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9817","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9817"}}]},"synonyms":[{"value":"RAD51A"},{"value":"RECA"}]}],"alphafold_very_low_content":0.05604719764011799,"disorder_content":0.17699115044247787,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"},{"start":86,"end":114,"type":"D"},{"start":273,"end":282,"type":"T"}],"Structural state":[{"start":1,"end":21,"type":"D"},{"start":86,"end":114,"type":"D"},{"start":273,"end":282,"type":"D"}],"Structural transition":[{"start":273,"end":282,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00488","name":"MutS domain V","start":979,"end":1167},{"id":"PF01624","name":"MutS domain I","start":312,"end":426},{"id":"PF05188","name":"MutS domain II","start":463,"end":593},{"id":"PF05190","name":"MutS family domain IV","start":780,"end":870},{"id":"PF05192","name":"MutS domain III","start":620,"end":779},{"id":"PF05192","name":"MutS domain III","start":871,"end":910}],"gene3D":[{"start":435,"end":617,"id":"3.30.420.110","name":"MutS, connector domain"},{"start":270,"end":432,"id":"3.40.1170.10","name":"DNA repair protein MutS, domain I"},{"start":758,"end":887,"id":"1.10.1420.10","name":"1.10.1420.10"},{"start":931,"end":1188,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":618,"end":911,"id":"1.10.1420.10","name":"1.10.1420.10"}]},"uniref50":"UniRef50_Q03834","sequence":"MAPATPKTSKTAHFENGSTSSQKKMKQSSLLSFFSKQVPSGTPSKKVQKPTPATLENTATDKITKNPQGGKTGKLFVDVDEDNDLTIAEETVSTVRSDIMHSQEPQSDTMLNSNTTEPKSTTTDEDLSSSQSRRNHKRRVNYAESDDDDSDTTFTAKRKKGKVVDSESDEDEYLPDKNDGDEDDDIADDKEDIKGELAEDSGDDDDLISLAETTSKKKFSYNTSHSSSPFTRNISRDNSKKKSRPNQAPSRSYNPSHSQPSATSKSSKFNKQNEERYQWLVDERDAQRRPKSDPEYDPRTLYIPSSAWNKFTPFEKQYWEIKSKMWDCIVFFKKGKFFELYEKDALLANALFDLKIAGGGRANMQLAGIPEMSFEYWAAQFIQMGYKVAKVDQRESMLAKEMREGSKGIVKRELQCILTSGTLTDGDMLHSDLATFCLAIREEPGNFYNETQLDSSTIVQKLNTKIFGAAFIDTATGELQMLEFEDDSECTKLDTLMSQVRPMEVVMERNNLSTLANKIVKFNSAPNAIFNEVKAGEEFYDCDKTYAEIISSEYFSTEEDWPEVLKSYYDTGKKVGFSAFGGLLYYLKWLKLDKNLISMKNIKEYDFVKSQHSMVLDGITLQNLEIFSNSFDGSDKGTLFKLFNRAITPMGKRMMKKWLMHPLLRKNDIESRLDSVDSLLQDITLREQLEITFSKLPDLERMLARIHSRTIKVKDFEKVITAFETIIELQDSLKNNDLKGDVSKYISSFPEGLVEAVKSWTNAFERQKAINENIIVPQRGFDIEFDKSMDRIQELEDELMEILMTYRKQFKCSNIQYKDSGKEIYTIEIPISATKNVPSNWVQMAANKTYKRYYSDEVRALARSMAEAKEIHKTLEEDLKNRLCQKFDAHYNTIWMPTIQAISNIDCLLAITRTSEYLGAPSCRPTIVDEVDSKTNTQLNGFLKFKSLRHPCFNLGATTAKDFIPNDIELGKEQPRLGLLTGANAAGKSTILRMACIAVIMAQMGCYVPCESAVLTPIDRIMTRLGANDNIMQGKSTFFVELAETKKILDMATNRSLLVVDELGRGGSSSDGFAIAESVLHHVATHIQSLGFFATHYGTLASSFKHHPQVRPLKMSILVDEATRNVTFLYKMLEGQSEGSFGMHVASMCGISKEIIDNAQIAADNLEHTSRLVKERDLAANNLNGEVVSVPGGLQSDFVRIAYGDGLKNTKLGSGEGVLNYDWNIKRNVLKSLFSIIDDLQS","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q03834","disprot_id":"DP01623","ncbi_taxon_id":559292,"regions_counter":2,"creator":"jmanso","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":304,"region_id":"DP01623r001","released":"2022_03","ec_id":"ECO:0006210","reference_html":"The N terminus of Saccharomyces cerevisiae Msh6 is an unstructured tether to PCNA. <i> Shell SS, Putnam CD, Kolodner RD. </i> Mol Cell, 2007","statement":[{"text":"The Msh6 NTR Is an Unstructured Peptide that Can\nInteract with PCNA Trimers at a 3:1 Ratio","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jmanso","start":1,"term_ontology":"IDPO","curator_name":"Jose A Manso","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17531814","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":304,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","reference_html":"The N terminus of Saccharomyces cerevisiae Msh6 is an unstructured tether to PCNA. <i> Shell SS, Putnam CD, Kolodner RD. </i> Mol Cell, 2007","term_id":"GO:0003676","curator_id":"jmanso","start":1,"term_ontology":"GO","curator_name":"Jose A Manso","reference_id":"17531814","version":3,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","region_id":"DP01623r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q03834","date":"2018-08-02T14:25:12.000Z","acc":"Q03834","name":"DNA mismatch repair protein MSH6","length":1242,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000053042","genes":[{"name":{"value":"MSH6"},"synonyms":[{"value":"PMS3"}],"orfNames":[{"value":"YD8557.04C"}],"olnNames":[{"value":"YDR097C"}]}],"alphafold_very_low_content":0.22544283413848631,"disorder_content":0.24476650563607086,"disprot_consensus":{"full":[{"start":1,"end":304,"type":"D"}],"Structural state":[{"start":1,"end":304,"type":"D"}],"Molecular function":[{"start":1,"end":304,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01408","name":"Oxidoreductase family, NAD-binding Rossmann fold","start":18,"end":143},{"id":"PF22685","name":"Gal80p, C-terminal domain","start":157,"end":308}]},"uniref50":"UniRef50_P04387","sequence":"MNNNKRSKLSTVPSSRPIRVGFVGLTSGKSWVAKTHFLAIQQLSSQFQIVALYNPTLKSSLQTIEQLQLKHATGFDSLESFAQYKDIDMIVVSVKVPEHYEVVKNILEHSSQNLNLRYLYVEWALAASVQQAEELYSISQQRANLQTIICLQGRKSPYIVRAKELISEGCIGDINSIEISGNGGWYGYERPMRSPEYLYDIESGVNLISNSFGHTIDVLQYITGSYFQKINAMISNNIPTQFLLDENGKRTKETISKTCPDHLLFQGILENGKVPVSCSFKGGTPVKKLTKNLVIDIHGTKGDLKIEGDAGFVEISNLVLYFYGIKNGNGSSNGTDNNGAAAIKDKEKVTKSPSPSTGTSEEEQTMEVFHLRNYNSVVGNILRIYESIADYHFLGKPESKSSRGPDDLFASTKFDKQGFRFEGFPTFKDAIILHRLIDAVFRSDKEEKTLDVSKIMI","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Kluyveromyces"],"uniref90":"UniRef90_Q06433","disprot_id":"DP01624","ncbi_taxon_id":284590,"regions_counter":2,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":361,"region_id":"DP01624r001","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Understanding a transcriptional paradigm at the molecular level. The structure of yeast Gal80p. <i> Thoden JB, Sellick CA, Reece RJ, Holden HM. </i> J Biol Chem, 2007","statement":[{"text":"Overall, the electron density for the protein was well ordered except for two short loop regions (Asp-245 to Gly-248 and Asp-309 to Ser-316 in Subunit I and Asn-247 to Arg-250 and Gly-311 to Ser-316 in Subunit II) and two larger regions that are located on the same side of the molecule (Gly-328 to Glu-362 and Leu-394 to Lys-413 in Subunit I and Gly-328 to Glu-361 and Gly-395 to Lys-413 in Subunit II).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":328,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-24T18:49:57.762Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2NVW"}],"reference_id":"17121853","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":413,"region_id":"DP01624r002","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Understanding a transcriptional paradigm at the molecular level. The structure of yeast Gal80p. <i> Thoden JB, Sellick CA, Reece RJ, Holden HM. </i> J Biol Chem, 2007","statement":[{"text":"Overall, the electron density for the protein was well ordered except for two short loop regions (Asp-245 to Gly-248 and Asp-309 to Ser-316 in Subunit I and Asn-247 to Arg-250 and Gly-311 to Ser-316 in Subunit II) and two larger regions that are located on the same side of the molecule (Gly-328 to Glu-362 and Leu-394 to Lys-413 in Subunit I and Gly-328 to Glu-361 and Gly-395 to Lys-413 in Subunit II).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":395,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-24T18:50:10.575Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2NVW"}],"reference_id":"17121853","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q06433","date":"2018-08-02T15:31:45.000Z","acc":"Q06433","name":"Galactose/lactose metabolism regulatory protein GAL80","length":457,"organism":"Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)","dataset":[],"UniParc":"UPI000012B07B","genes":[{"name":{"value":"GAL80"},"olnNames":[{"value":"KLLA0A08162g"}]}],"alphafold_very_low_content":0.09409190371991247,"disorder_content":0.11597374179431072,"disprot_consensus":{"full":[{"start":328,"end":361,"type":"D"},{"start":395,"end":413,"type":"D"}],"Structural state":[{"start":328,"end":361,"type":"D"},{"start":395,"end":413,"type":"D"}]}},{"acc":"P07567","sequence":"MGQELSQHERYVEQLKQALKTRGVKVKYADLLKFFDFVKDTCPWFPQEGTIDIKRWRRVGDCFQDYYNTFGPEKVPVTAFSYWNLIKELIDKKEVNPQVMAAVAQTEEILKSNSQTDLTKTSQNPDLDLISLDSDDEGAKSSSLQDKGLSSTKKPKRFPVLLTAQTSKDPEDPNPSEVDWDGLEDEAAKYHNPDWPPFLTRPPPYNKATPSAPTVMAVVNPKEELKEKIAQLEEQIKLEELHQALISKLQKLKTGNETVTHPDTAGGLSRTPHWPGQHIPKGKCCASREKEEQIPKDIFPVTETVDGQGQAWRHHNGFDFAVIKELKTAASQYGATAPYTLAIVESVADNWLTPTDWNTLVRAVLSGGDHLLWKSEFFENCRDTAKRNQQAGNGWDFDMLTGSGNYSSTDAQMQYDPGLFAQIQAAATKAWRKLPVKGDPGASLTGVKQGPDEPFADFVHRLITTAGRIFGSAEAGVDYVKQLAYENANPACQAAIRPYRKKTDLTGYIRLCSDIGPSYQQGLAMAAAFSGQTVKDFLNNKNKEKGGCCFKCGKKGHFAKNCHEHAHNNAEPKVPGLCPRCKRGKHWANECKSKTDNQGNPIPPHQGNGWRGQPQAPKQAYGAVSFVPANKNNPFQSLPEPPQEVQDWTSVPPPTQY","creator":"akajava","dataset":["Viral proteins"],"date":"2018-08-02T16:00:30.000Z","disprot_id":"DP01625","features":{"pfam":[{"id":"PF00607","name":"gag protein p24 N-terminal domain","start":314,"end":437},{"id":"PF02337","name":"Retroviral GAG p10 protein","start":8,"end":91},{"id":"PF14787","name":"GAG-polyprotein viral zinc-finger","start":575,"end":609},{"id":"PF19317","name":"Gag protein p24 C-terminal domain","start":443,"end":510}],"gene3D":[{"start":1,"end":100,"id":"1.10.150.490","name":"Retroviral GAG p10 protein","_id":"685af523b4ac24d5329d91c9"},{"start":300,"end":435,"id":"1.10.375.10","name":"Human Immunodeficiency Virus Type 1 Capsid Protein","_id":"685af523b4ac24d5329d91ca"},{"start":436,"end":533,"id":"1.10.1200.30","name":"1.10.1200.30","_id":"685af523b4ac24d5329d91cb"},{"start":534,"end":600,"id":"4.10.60.10","name":"Zinc finger, CCHC-type","_id":"685af523b4ac24d5329d91cc"}]},"genes":[{"name":{"value":"gag","evidences":[],"_id":"685af523b4ac24d5329d91e1"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d91e0"}],"length":657,"name":"Gag polyprotein","ncbi_taxon_id":11855,"organism":"Mason-Pfizer monkey virus","regions_counter":3,"released":"2018_11","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Betaretrovirus"],"UniParc":"UPI000010313E","uniref100":"UniRef100_P07567","uniref50":"UniRef50_P07567","uniref90":"UniRef90_P07567","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"Sequence used presents this mutation. Blast analysis shows there is no wildtype strain with this aminoacidic sequence.","_id":"685af523b4ac24d5329d91d3"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys458Ser","_id":"685af523b4ac24d5329d91d2"}],"cross_refs":[{"db":"BMRB","id":"4498","_id":"685af523b4ac24d5329d91d4"},{"db":"PDB","id":"1CL4","_id":"685af523b4ac24d5329d91d5"},{"db":"BMRB","id":"4600","_id":"685af523b4ac24d5329d91d6"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":546,"end":605,"interaction_partner":[],"reference_html":"Solution structure and backbone dynamics of Mason-Pfizer monkey virus (MPMV) nucleocapsid protein. <i> Gao Y, Kaluarachchi K, Giedroc DP. </i> Protein Sci, 1998","reference_id":"9827993","region_id":"DP01625r002","released":"2022_03","sample":[{"db":"ChEBI","deviation":null,"entry_name":"zinc(2+)","id":"29105","statements":[{"type":"Results","text":"The zinc was covalently attached to the SY atom of each of the Cys and Ne2 of each His. ","_id":"685af523b4ac24d5329d91d9"}],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d91d8"}],"sequence_construct":"GGSCFKCGKKGHFAKNCHEHAHNNAEPKVPGLCPRCKRGKHWANECKSKTDNQGNPIPPH","statement":[{"type":"Results","text":"As found in previous studies of retroviral nucleocapsid proteins studied by NMR, there was no evidence of stable, easily identifiable secondary structural regions in the molecule. Comparison of the experimentally determined Ca and Ha chemical shifts with random coil values are largely consistent with this picture, with no systematic deviation toward a-helical or /3-strand values among contiguous residues. ","_id":"685af523b4ac24d5329d91d7"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-23T10:03:03.457Z","_id":"685af523b4ac24d5329d91da"},"version":1,"_id":"685af523b4ac24d5329d91d1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1CL4","_id":"685af523b4ac24d5329d91dc"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":546,"end":605,"interaction_partner":[{"db":"ChEBI","id":"29105","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d91dd"}],"reference_html":"Solution structure and backbone dynamics of Mason-Pfizer monkey virus (MPMV) nucleocapsid protein. <i> Gao Y, Kaluarachchi K, Giedroc DP. </i> Protein Sci, 1998","reference_id":"9827993","region_id":"DP01625r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The zinc was covalently attached to the SY atom of each of the Cys and Ne2 of each His. Zn(l1)-ligand bonds were assigned distances of 2.10 8, (Zn-SY) and 2.00 A (Zn-Ne2) and a force constant of 200 kcal/(mol A2).","_id":"685af523b4ac24d5329d91de"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","term_go_domain":"F","term_id":"GO:0046872","term_is_binding":true,"term_is_obsolete":false,"term_name":"metal ion binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-23T12:00:15.934Z","_id":"685af523b4ac24d5329d91df"},"version":1,"_id":"685af523b4ac24d5329d91db","reference_source":"pmid"}],"__v":0,"disorder_content":0.091324200913242,"disprot_consensus":{"full":[{"start":546,"end":605,"type":"D"}],"Structural state":[{"start":546,"end":605,"type":"D"}],"Molecular function":[{"start":546,"end":605,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03835","name":"Rad4 transglutaminase-like domain","start":501,"end":625},{"id":"PF10403","name":"Rad4 beta-hairpin domain 1","start":632,"end":681},{"id":"PF10404","name":"Rad4 beta-hairpin domain 2","start":685,"end":744},{"id":"PF10405","name":"Rad4 beta-hairpin domain 3","start":751,"end":823}],"gene3D":[{"start":757,"end":829,"id":"3.30.70.2460","name":"Rad4, beta-hairpin domain BHD3"},{"start":189,"end":344,"id":"3.90.260.10","name":"Transglutaminase-like"},{"start":525,"end":634,"id":"3.10.620.30","name":"3.10.620.30"}]},"uniref50":"UniRef50_Q01831","sequence":"MARKRAAGGEPRGRELRSQKSKAKSKARREEEEEDAFEDEKPPKKSLLSKVSQGKRKRGCSHPGGSADGPAKKKVAKVTVKSENLKVIKDEALSDGDDLRDFPSDLKKAHHLKRGATMNEDSNEEEEESENDWEEVEELSEPVLGDVRESTAFSRSLLPVKPVEIEIETPEQAKTRERSEKIKLEFETYLRRAMKRFNKGVHEDTHKVHLLCLLANGFYRNNICSQPDLHAIGLSIIPARFTRVLPRDVDTYYLSNLVKWFIGTFTVNAELSASEQDNLQTTLERRFAIYSARDDEELVHIFLLILRALQLLTRLVLSLQPIPLKSATAKGKKPSKERLTADPGGSSETSSQVLENHTKPKTSKGTKQEETFAKGTCRPSAKGKRNKGGRKKRSKPSSSEEDEGPGDKQEKATQRRPHGRERRVASRVSYKEESGSDEAGSGSDFELSSGEASDPSDEDSEPGPPKQRKAPAPQRTKAGSKSASRTHRGSHRKDPSLPAASSSSSSSKRGKKMCSDGEKAEKRSIAGIDQWLEVFCEQEEKWVCVDCVHGVVGQPLTCYKYATKPMTYVVGIDSDGWVRDVTQRYDPVWMTVTRKCRVDAEWWAETLRPYQSPFMDREKKEDLEFQAKHMDQPLPTAIGLYKNHPLYALKRHLLKYEAIYPETAAILGYCRGEAVYSRDCVHTLHSRDTWLKKARVVRLGEVPYKMVKGFSNRARKARLAEPQLREENDLGLFGYWQTEEYQPPVAVDGKVPRNEFGNVYLFLPSMMPIGCVQLNLPNLHRVARKLDIDCVQAITGFDFHGGYSHPVTDGYIVCEEFKDVLLTAWENEQAVIERKEKEKKEKRALGNWKLLAKGLLIRERLKRRYGPKSEAAAPHTDAGGGLSSDEEEGTSSQAEAARILAASWPQNREDEEKQKLKGGPKKTKREKKAAASHLFPFEQL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q01831","disprot_id":"DP01626","ncbi_taxon_id":9606,"regions_counter":8,"creator":"bhajdu","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":940,"region_id":"DP01626r001","released":"2022_06","ec_id":"ECO:0006317","reference_html":"The carboxy-terminal domain of xeroderma pigmentosum complementation group C protein, involved in TFIIH and centrin binding, is highly disordered. <i> Miron S, Duchambon P, Blouquit Y, Durand D, Craescu CT. </i> Biochemistry, 2008","statement":[{"text":"Thermal denaturation monitored by the ellipticity at 222 nm (Figure 2B) shows that the protein loses progressively (noncooperative unfolding) its helical structure between 5 °C and 40 °C, suggesting a low degree of tertiary structural organization ( 34).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":815,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-24T16:16:16.497Z","reference_source":"pmid","term_name":"disorder","reference_id":"18177054","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-26T16:40:02.482Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":940,"region_id":"DP01626r002","released":"2022_06","ec_id":"ECO:0006210","reference_html":"The carboxy-terminal domain of xeroderma pigmentosum complementation group C protein, involved in TFIIH and centrin binding, is highly disordered. <i> Miron S, Duchambon P, Blouquit Y, Durand D, Craescu CT. </i> Biochemistry, 2008","statement":[{"text":" The Rg value is 2-fold larger than the value expected for a compact, globular protein with the same number (n) of residues which is Rg ∼ 3n1/3 = 15 Å ( 40). It can also be compared with the expected value for a completely unfolded protein. ","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":815,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-24T16:14:42.216Z","reference_source":"pmid","term_name":"disorder","reference_id":"18177054","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-26T16:40:04.235Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":940,"region_id":"DP01626r003","released":"2022_06","ec_id":"ECO:0006165","reference_html":"The carboxy-terminal domain of xeroderma pigmentosum complementation group C protein, involved in TFIIH and centrin binding, is highly disordered. <i> Miron S, Duchambon P, Blouquit Y, Durand D, Craescu CT. </i> Biochemistry, 2008","statement":[{"text":"Moreover, in the (15N)NOESY-HSQC spectrum no medium or long-range NOE cross-peaks were observed, suggesting a lack of\npersistent secondary or tertiary structure, in agreement with the SAXS results.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":815,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-24T16:15:44.189Z","reference_source":"pmid","term_name":"disorder","reference_id":"18177054","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-26T16:40:06.441Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":940,"term_name":"protein binding","released":"2022_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The carboxy-terminal domain of xeroderma pigmentosum complementation group C protein, involved in TFIIH and centrin binding, is highly disordered. <i> Miron S, Duchambon P, Blouquit Y, Durand D, Craescu CT. </i> Biochemistry, 2008","statement":[{"text":"Figure 6A shows the thermogram and the binding isotherm corresponding to the titration of HsCen2 (200 μM) into C-XPC (15 μM). Fitting the isotherm to a single-site binding model gives a stoichiometry of 1:1, a binding constant of 2.9 (1) × 108 M-1, and a reaction enthalpy ΔH = −30.2 (0.2) kcal/mol. Therefore, C-XPC binds HsCen2 with high affinity and thermodynamic parameters similar to that of the 17-mer peptide (Table 1).","type":"Results"}],"term_id":"GO:0005515","curator_id":"vnugnes","start":815,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"18177054","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-24T16:17:16.803Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01626r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P41208","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-26T16:40:46.867Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":940,"region_id":"DP01626r005","released":"2022_06","ec_id":"ECO:0006204","reference_html":"The carboxy-terminal domain of xeroderma pigmentosum complementation group C protein, involved in TFIIH and centrin binding, is highly disordered. <i> Miron S, Duchambon P, Blouquit Y, Durand D, Craescu CT. </i> Biochemistry, 2008","statement":[{"text":"A quantitative analysis of the far-UV CD spectra of C-XPC domain was made by fitting the experimental data\nto an appropriate combination of “pure” secondary structure spectra. Utilization of two different fitting procedures,\nCONTIN (32) and CDSSTR (33), gave similar values for the secondary structure content of C-XPC: 33% and 37% alpha-helix, respectively.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":815,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-24T16:15:12.859Z","reference_source":"pmid","term_name":"disorder","reference_id":"18177054","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-26T16:40:08.643Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":863,"region_id":"DP01626r006","released":"2022_06","ec_id":"ECO:0006204","reference_html":"Xeroderma pigmentosum group C protein possesses a high affinity binding site to human centrin 2 and calmodulin. <i> Popescu A, Miron S, Blouquit Y, Duchambon P, Christova P, Craescu CT. </i> J Biol Chem, 2003","statement":[{"text":"The peptide alone exhibits a CD spectrum characteristic for a highly disordered structure, as is generally the case for linear polypeptides of this size.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":847,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-24T15:48:07.806Z","reference_source":"pmid","term_name":"disorder","reference_id":"12890685","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"EEFKDVLLTAWENEQAVIERKEKEKKEKRALGNWKLLAKGLLIRERLKR","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-26T16:40:10.041Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":863,"term_name":"disorder to order","released":"2022_06","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Xeroderma pigmentosum group C protein possesses a high affinity binding site to human centrin 2 and calmodulin. <i> Popescu A, Miron S, Blouquit Y, Duchambon P, Christova P, Craescu CT. </i> J Biol Chem, 2003","statement":[{"text":"Therefore, the large variation of the negative band intensity at 222 nm, the most characteristic for the α structure, suggests that a fragment of the peptide undergoes a random coil-to-helix structural transition upon binding to the protein, bringing a significant contribution to the α-helix CD band.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"vnugnes","start":847,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12890685","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-24T15:47:54.635Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01626r007","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P41208"}],"sequence_construct":"EEFKDVLLTAWENEQAVIERKEKEKKEKRALGNWKLLAKGLLIRERLKR","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-26T16:40:37.825Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":863,"term_name":"protein binding","released":"2022_06","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Xeroderma pigmentosum group C protein possesses a high affinity binding site to human centrin 2 and calmodulin. <i> Popescu A, Miron S, Blouquit Y, Duchambon P, Christova P, Craescu CT. </i> J Biol Chem, 2003","statement":[{"text":"Adding of P1-XPC, at a 1:1 molar ratio, to SC-HsCen2/Ca2+ induces a considerable enhancement of the CD signal (by ∼50%) with a rough conservation of the relative intensities of different bands (Fig. 5A). ","type":"Results"}],"term_id":"GO:0005515","curator_id":"vnugnes","start":847,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"12890685","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-24T15:59:22.897Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01626r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"sequence_construct":"EEFKDVLLTAWENEQAVIERKEKEKKEKRALGNWKLLAKGLLIRERLKR","interaction_partner":[{"db":"UniProt","id":"P41208","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-26T16:42:34.842Z"}}],"released":"2018_11","uniref100":"UniRef100_Q01831","date":"2018-08-03T08:10:36.000Z","acc":"Q01831","name":"DNA repair protein complementing XP-C cells","length":940,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI0000043B80","genes":[{"name":{"value":"XPC"},"synonyms":[{"value":"XPCC"}]}],"alphafold_very_low_content":0.4074468085106383,"disorder_content":0.13404255319148936,"disprot_consensus":{"full":[{"start":815,"end":846,"type":"D"},{"start":847,"end":863,"type":"T"},{"start":864,"end":940,"type":"D"}],"Structural state":[{"start":815,"end":940,"type":"D"}],"Molecular function":[{"start":815,"end":940,"type":"F"}],"Structural transition":[{"start":847,"end":863,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00254","name":"FKBP-type peptidyl-prolyl cis-trans isomerase","start":165,"end":246},{"id":"PF05697","name":"Bacterial trigger factor protein (TF)","start":11,"end":152},{"id":"PF05698","name":"Bacterial trigger factor protein (TF) C-terminus","start":275,"end":439}],"gene3D":[{"start":5,"end":129,"id":"3.30.70.1050","name":"Trigger factor ribosome-binding domain"},{"start":130,"end":393,"id":"1.10.3120.10","name":"Trigger factor, C-terminal domain"},{"start":158,"end":255,"id":"3.10.50.40","name":"3.10.50.40"}]},"uniref50":"UniRef50_P47480","sequence":"MKLYKVLNSKTTDKSLCLEVEIDPNYWQATQKKLVGEMAKSIKIKGFRPGKIPPNLASQSINKAELMQKSAQNVMNSIYESVQQEEIVASNDNVIDDYPTIDFKTITEQNCVLLFYFDLIPNFQLPDYKKIKDLTPLTKLTEAEFNNEIEKLAKTKSTMVDVSDKKLANGDIAIIDFTGIVDNKKLASASAQNYELTIGSNSFIKGFETGLIAMKVNQKKTLALTFPSDYHVKELQSKPVTFEVVLKAIKKLEFTPMDETNFKSFLPEQFQSFTSLKAFKSYFHKLMENKKQETILQENNQKIRQFLLTNTKLPFLPEALIKLEANRLLKLQQSQAEQYKIPFEKLLSASNITLTELQDRNIKEAKENVTFALVMKKIADIEKIKVDNNKIKAEIENVIAVEYPFASDEMKKQLFFNMEQQKEFVESIIINRLTTTKIVSYSTH","taxonomy":["Bacteria","Tenericutes","Mollicutes","Mycoplasmataceae","Mycoplasma"],"uniref90":"UniRef90_P47480","disprot_id":"DP01627","ncbi_taxon_id":243273,"regions_counter":1,"creator":"akajava","regions":[{"region_id":"DP01627r001","ec_ontology":"ECO","end":166,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":150,"version":3,"statement":[{"text":"For the N-terminal stretch (Ser12 to Lys29), only intra-residual and sequential NOEs could be detected. This type of NOE signature is typical of unstructured polypeptide chains.","type":"Results"}],"term_name":"disorder","reference_html":"NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain of the trigger factor from Mycoplasma genitalium compared to FK506-binding protein. <i> Vogtherr M, Jacobs DM, Parac TN, Maurer M, Pahl A, Saxena K, Rüterjans H, Griesinger C, Fiebig KM. </i> J Mol Biol, 2002","released":"2022_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12054805","date":"2022-08-24T19:07:20.639Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1HXV"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"MRGSHHHHHHGSEKLAKTKSTMVDVSDKKLANGDIAIIDFTGIVDNKKLASASAQNYELTIGSNSFIKGFETGLIAMKVNQKKTLALTFPSDYHVKELQSKPVTFEVVLKAIK"}],"released":"2018_11","uniref100":"UniRef100_P47480","date":"2018-08-03T08:25:23.000Z","acc":"P47480","name":"Trigger factor","length":444,"organism":"Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195)","dataset":[],"UniParc":"UPI0000136F6E","genes":[{"name":{"value":"tig"},"olnNames":[{"value":"MG238"}]}],"alphafold_very_low_content":0,"disorder_content":0.038288288288288286,"disprot_consensus":{"full":[{"start":150,"end":166,"type":"D"}],"Structural state":[{"start":150,"end":166,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03835","name":"Rad4 transglutaminase-like domain","start":285,"end":425},{"id":"PF10403","name":"Rad4 beta-hairpin domain 1","start":432,"end":487},{"id":"PF10405","name":"Rad4 beta-hairpin domain 3","start":551,"end":624}],"gene3D":[{"start":557,"end":632,"id":"3.30.70.2460","name":"Rad4, beta-hairpin domain BHD3"},{"start":126,"end":432,"id":"3.90.260.10","name":"Transglutaminase-like"},{"start":491,"end":540,"id":"2.20.20.120","name":"Rad4, beta-hairpin domain BHD2"},{"start":433,"end":490,"id":"2.20.20.110","name":"Rad4, beta-hairpin domain BHD1"}]},"uniref50":"UniRef50_P14736","sequence":"MNEDLPKEYFELIRKALNEKEAEKAPLSRRRRVRRKNQPLPDAKKKFKTGLNELPRESVVTVNLDSSDDGVVTVPTDDSVEEIQSSEEDYDSEEFEDVTDGNEVAGVEDISVEIKPSSKRNSDARRTSRNVCSNEERKRRKYFHMLYLVCLMVHGFIRNEWINSKRLSRKLSNLVPEKVFELLHPQKDEELPLRSTRKLLDGLKKCMELWQKHWKITKKYDNVGLYMRTWKEIEMSANNKRKFKTLKRSDFLRAVSKGHGDPDISVQGFVAMLRACNVNARLIMSCQPPDFTNMKIDTSLNGNNAYKDMVKYPIFWCEVWDKFSKKWITVDPVNLKTIEQVRLHSKLAPKGVACCERNMLRYVIAYDRKYGCRDVTRRYAQWMNSKVRKRRITKDDFGEKWFRKVITALHHRKRTKIDDYEDQYFFQRDESEGIPDSVQDLKNHPYYVLEQDIKQTQIVKPGCKECGYLKVHGKVGKVLKVYAKRDIADLKSARQWYMNGRILKTGSRCKKVIKRTVGRPKGEAEEEDERLYSFEDTELYIPPLASASGEITKNTFGNIEVFAPTMIPGNCCLVENPVAIKAARFLGVEFAPAVTSFKFERGSTVKPVLSGIVVAKWLREAIETAIDGIEFIQEDDNRKEHLLGALESWNTLLLKLRIRSKLNSTYGKIAEEEPNVTKEQNIADNHDNTETFMGGGFLPGIANHEARPYSEPSEPEDSLDYVSVDKAEESATDDDVGEDYSDFMKELEMSEESD","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P14736","disprot_id":"DP01628","ncbi_taxon_id":559292,"regions_counter":2,"creator":"bhajdu","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":754,"region_id":"DP01628r001","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Recognition of DNA damage by the Rad4 nucleotide excision repair protein. <i> Min JH, Pavletich NP. </i> Nature, 2007","statement":[{"text":"Limited proteolysis of the insect-cellexpressed 754-residue Rad4 showed that the 100 N-terminal (residues 1–100) and 122 C-terminal (633–754) residues are highly susceptible to digestion, suggesting that they are unstructured or loosely folded.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"bhajdu","start":633,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17882165","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":100,"region_id":"DP01628r002","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Recognition of DNA damage by the Rad4 nucleotide excision repair protein. <i> Min JH, Pavletich NP. </i> Nature, 2007","statement":[{"text":"Limited proteolysis of the insect-cellexpressed 754-residue Rad4 showed that the 100 N-terminal (residues 1–100) and 122 C-terminal (633–754) residues are highly susceptible to digestion, suggesting that they are unstructured or loosely folded.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"bhajdu","start":1,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17882165","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P14736","date":"2018-08-03T12:15:12.000Z","acc":"P14736","name":"DNA repair protein RAD4","length":754,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000013307D","genes":[{"name":{"value":"RAD4"},"olnNames":[{"value":"YER162C"}]}],"alphafold_very_low_content":0.22679045092838196,"disorder_content":0.29442970822281167,"disprot_consensus":{"full":[{"start":1,"end":100,"type":"D"},{"start":633,"end":754,"type":"D"}],"Structural state":[{"start":1,"end":100,"type":"D"},{"start":633,"end":754,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00240","name":"Ubiquitin family","start":4,"end":75},{"id":"PF00627","name":"UBA/TS-N domain","start":148,"end":183},{"id":"PF00627","name":"UBA/TS-N domain","start":356,"end":392},{"id":"PF09280","name":"XPC-binding domain","start":264,"end":308}],"gene3D":[{"start":255,"end":309,"id":"1.10.10.540","name":"XPC-binding domain"},{"start":141,"end":188,"id":"1.10.8.10","name":"DNA helicase RuvA subunit, C-terminal domain"},{"start":1,"end":74,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"},{"start":347,"end":398,"id":"1.10.8.10","name":"DNA helicase RuvA subunit, C-terminal domain"}]},"uniref50":"UniRef50_P32628","sequence":"MVSLTFKNFKKEKVPLDLEPSNTILETKTKLAQSISCEESQIKLIYSGKVLQDSKTVSECGLKDGDQVVFMVSQKKSTKTKVTEPPIAPESATTPGRENSTEASPSTDASAAPAATAPEGSQPQEEQTATTERTESASTPGFVVGTERNETIERIMEMGYQREEVERALRAAFNNPDRAVEYLLMGIPENLRQPEPQQQTAAAAEQPSTAATTAEQPAEDDLFAQAAQGGNASSGALGTTGGATDAAQGGPPGSIGLTVEDLLSLRQVVSGNPEALAPLLENISARYPQLREHIMANPEVFVSMLLEAVGDNMQDVMEGADDMVEGEDIEVTGEAAAAGLGQGEGEGSFQVDYTPEDDQAISRLCELGFERDLVIQVYFACDKNEEAAANILFSDHAD","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P32628","disprot_id":"DP01629","ncbi_taxon_id":559292,"regions_counter":14,"creator":"bhajdu","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":147,"region_id":"DP01629r001","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Rad23 escapes degradation because it lacks a proteasome initiation region. <i> Fishbain S, Prakash S, Herrig A, Elsasser S, Matouschek A. </i> Nat Commun, 2011","statement":[{"text":"The L1, L2, and L3 regions of Rad23, consisting of amino acids 77-147, 185-265, and 311-355, respectively, were attached to the C terminus of Rad23. Rad23-L3 was degraded efficiently but Rad23-L1 and Rad23-L2 were degraded more slowly.","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"bhajdu","start":77,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21304521","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":147,"term_name":"flexible linker","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","reference_html":"Rad23 escapes degradation because it lacks a proteasome initiation region. <i> Fishbain S, Prakash S, Herrig A, Elsasser S, Matouschek A. </i> Nat Commun, 2011","statement":[{"text":"These four domains have well-defined structures but are connected by flexible linker regions ranging in length from 45 to 82 amino acids.","type":"Introduction"}],"term_id":"IDPO:0000033","curator_id":"bhajdu","start":77,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","reference_id":"21304521","version":3,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","region_id":"DP01629r002","ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":265,"region_id":"DP01629r003","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Rad23 escapes degradation because it lacks a proteasome initiation region. <i> Fishbain S, Prakash S, Herrig A, Elsasser S, Matouschek A. </i> Nat Commun, 2011","statement":[{"text":"The L1, L2, and L3 regions of Rad23, consisting of amino acids 77-147, 185-265, and 311-355, respectively, were attached to the C terminus of Rad23. Rad23-L3 was degraded efficiently but Rad23-L1 and Rad23-L2 were degraded more slowly.","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"bhajdu","start":185,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21304521","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":265,"term_name":"flexible linker","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","reference_html":"Rad23 escapes degradation because it lacks a proteasome initiation region. <i> Fishbain S, Prakash S, Herrig A, Elsasser S, Matouschek A. </i> Nat Commun, 2011","statement":[{"text":"These four domains have well-defined structures but are connected by flexible linker regions ranging in length from 45 to 82 amino acids.","type":"Introduction"}],"term_id":"IDPO:0000033","curator_id":"bhajdu","start":185,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","reference_id":"21304521","version":3,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","region_id":"DP01629r004","ec_go":"IDA","disprot_namespace":"Disorder function"},{"region_id":"DP01629r005","ec_ontology":"ECO","end":254,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":230,"version":3,"statement":[{"text":"The refined model contains residues 126–300, 304–515, 528–599 and 606–632 of Rad4, residues 255–309 and 347–395 of Rad23, and 250 water molecules.","type":"Methods"},{"text":"The final models of the ternary complexes contain residues 123–517 and 526–632 of Rad4, and 256–369 of Rad23.","type":"Methods"},{"text":"According to the PDB entries, the region 230-254 is unstructured both in the Rad4-Rad23 complex as in the ternary complex with DNA.","type":"Curator statement"}],"term_name":"disorder","reference_html":"Recognition of DNA damage by the Rad4 nucleotide excision repair protein. <i> Min JH, Pavletich NP. </i> Nature, 2007","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"17882165","date":"2023-09-26T16:27:11.819Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2QSF"},{"db":"PDB","id":"2QSG"},{"db":"PDB","id":"2QSH"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P14736"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting ssDNA with sequence 5'-TTGACTCAACATCCTTTGCTACAA"},{"type":"Article","text":"The structures of truncated Rad4–Rad23 bound to a 24 base-pair (bp) DNA duplex containing either the CPD-mismatch or the mismatch alone were determined at 3.1 Å and 2.8 Å, respectively (Supplementary Tables 1 and 2)."}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting ssDNA with sequence 5'-ATTGTAGCTTTGGATGTTGAGTCA"},{"type":"Article","text":"The structures of truncated Rad4–Rad23 bound to a 24 base-pair (bp) DNA duplex containing either the CPD-mismatch or the mismatch alone were determined at 3.1 Å and 2.8 Å, respectively (Supplementary Tables 1 and 2)."}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting ssDNA with sequence 5'-ATTGTAGCNNTGGATGTTGAGTCA"},{"type":"Article","text":"The structures of truncated Rad4–Rad23 bound to a 24 base-pair (bp) DNA duplex containing either the CPD-mismatch or the mismatch alone were determined at 3.1 Å and 2.8 Å, respectively (Supplementary Tables 1 and 2)."}]}],"sequence_construct":"GSGNASSGALGTTGGATDAAQGGPPGSIGLTVEDLLSLRQVVSGNPEALAPLLENISARYPQLREHIMANPEVFVSMLLEAVGDNMQDVMEGADDMVEGEDIEVTGEAAAAGLGQGEGEGSFQVDYTPEDDQAISRLCELGFERDLVIQVYFACDKNEEAAANILFSDHAD"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":355,"region_id":"DP01629r007","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Rad23 escapes degradation because it lacks a proteasome initiation region. <i> Fishbain S, Prakash S, Herrig A, Elsasser S, Matouschek A. </i> Nat Commun, 2011","statement":[{"text":"The L1, L2, and L3 regions of Rad23, consisting of amino acids 77-147, 185-265, and 311-355, respectively, were attached to the C terminus of Rad23. Rad23-L3 was degraded efficiently but Rad23-L1 and Rad23-L2 were degraded more slowly.","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"bhajdu","start":311,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21304521","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":355,"term_name":"flexible linker","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","reference_html":"Rad23 escapes degradation because it lacks a proteasome initiation region. <i> Fishbain S, Prakash S, Herrig A, Elsasser S, Matouschek A. </i> Nat Commun, 2011","statement":[{"text":"These four domains have well-defined structures but are connected by flexible linker regions ranging in length from 45 to 82 amino acids.","type":"Introduction"}],"term_id":"IDPO:0000033","curator_id":"bhajdu","start":311,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","reference_id":"21304521","version":3,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","region_id":"DP01629r008","ec_go":"IDA","disprot_namespace":"Disorder function"},{"region_id":"DP01629r009","ec_ontology":"ECO","end":346,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":310,"version":3,"statement":[{"text":"The refined model contains residues 126–300, 304–515, 528–599 and 606–632 of Rad4, residues 255–309 and 347–395 of Rad23, and 250 water molecules.","type":"Methods"}],"term_name":"disorder","reference_html":"Recognition of DNA damage by the Rad4 nucleotide excision repair protein. <i> Min JH, Pavletich NP. </i> Nature, 2007","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"17882165","date":"2023-09-26T15:48:24.356Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2QSF"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P14736"}],"sequence_construct":"GSGNASSGALGTTGGATDAAQGGPPGSIGLTVEDLLSLRQVVSGNPEALAPLLENISARYPQLREHIMANPEVFVSMLLEAVGDNMQDVMEGADDMVEGEDIEVTGEAAAAGLGQGEGEGSFQVDYTPEDDQAISRLCELGFERDLVIQVYFACDKNEEAAANILFSDHAD"},{"start":310,"end":398,"reference_id":"17882165","reference_source":"pmid","reference_html":"Recognition of DNA damage by the Rad4 nucleotide excision repair protein. <i> Min JH, Pavletich NP. </i> Nature, 2007","date":"2023-09-26T16:38:59.816Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2QSH"},{"db":"PDB","id":"2QSG"}],"region_id":"DP01629r011","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P14736"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting ssDNA with sequence 5'-TTGACTCAACATCCTTTGCTACAA"},{"type":"Article","text":"The structures of truncated Rad4–Rad23 bound to a 24 base-pair (bp) DNA duplex containing either the CPD-mismatch or the mismatch alone were determined at 3.1 Å and 2.8 Å, respectively (Supplementary Tables 1 and 2)."}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting ssDNA with sequence 5'-ATTGTAGCNNTGGATGTTGAGTCA"},{"type":"Article","text":"The structures of truncated Rad4–Rad23 bound to a 24 base-pair (bp) DNA duplex containing either the CPD-mismatch or the mismatch alone were determined at 3.1 Å and 2.8 Å, respectively (Supplementary Tables 1 and 2)."}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting ssDNA with sequence 5'-ATTGTAGCTTTGGATGTTGAGTCA"},{"type":"Article","text":"The structures of truncated Rad4–Rad23 bound to a 24 base-pair (bp) DNA duplex containing either the CPD-mismatch or the mismatch alone were determined at 3.1 Å and 2.8 Å, respectively (Supplementary Tables 1 and 2)."}]}],"statement":[{"text":"The final models of the ternary complexes contain residues 123–517 and 526–632 of Rad4, and 256–369 of Rad23.","type":"Methods"},{"text":"According to the PDB entries, this region is unstructured in the Rad4-Rad23-DNA complexes. In the Methods section the authors states the end of the structured region is the residue 369 but this might be a typographical error considering that in the PDB structure the structured region is 256-309.","type":"Curator statement"}],"sequence_construct":"GSGNASSGALGTTGGATDAAQGGPPGSIGLTVEDLLSLRQVVSGNPEALAPLLENISARYPQLREHIMANPEVFVSMLLEAVGDNMQDVMEGADDMVEGEDIEVTGEAAAAGLGQGEGEGSFQVDYTPEDDQAISRLCELGFERDLVIQVYFACDKNEEAAANILFSDHAD"},{"start":347,"end":395,"reference_id":"17882165","reference_source":"pmid","reference_html":"Recognition of DNA damage by the Rad4 nucleotide excision repair protein. <i> Min JH, Pavletich NP. </i> Nature, 2007","date":"2023-09-26T16:28:02.691Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2QSH"},{"db":"PDB","id":"2QSG"},{"db":"PDB","id":"2QSF"}],"region_id":"DP01629r012","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P14736"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting ssDNA with sequence 5'-TTGACTCAACATCCTTTGCTACAA"},{"type":"Article","text":"The structures of truncated Rad4–Rad23 bound to a 24 base-pair (bp) DNA duplex containing either the CPD-mismatch or the mismatch alone were determined at 3.1 Å and 2.8 Å, respectively (Supplementary Tables 1 and 2)."}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting ssDNA with sequence 5'-ATTGTAGCNNTGGATGTTGAGTCA"},{"type":"Article","text":"The structures of truncated Rad4–Rad23 bound to a 24 base-pair (bp) DNA duplex containing either the CPD-mismatch or the mismatch alone were determined at 3.1 Å and 2.8 Å, respectively (Supplementary Tables 1 and 2)."}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting ssDNA with sequence 5'-ATTGTAGCTTTGGATGTTGAGTCA"},{"type":"Article","text":"The structures of truncated Rad4–Rad23 bound to a 24 base-pair (bp) DNA duplex containing either the CPD-mismatch or the mismatch alone were determined at 3.1 Å and 2.8 Å, respectively (Supplementary Tables 1 and 2)."}]}],"statement":[{"text":"The refined model contains residues 126–300, 304–515, 528–599 and 606–632 of Rad4, residues 255–309 and 347–395 of Rad23, and 250 water molecules.","type":"Methods"},{"text":"The final models of the ternary complexes contain residues 123–517 and 526–632 of Rad4, and 256–369 of Rad23.","type":"Methods"},{"text":"In the Methods section the authors states the limit of the structured region of the Rad4-Rad23-DNA complexes as the residue 369 but this might be a typographical error considering that in the PDB the structured region is 256-309. According to the PDB entries, the region 347-395 is unstructured in the Rad4-Rad23-DNA complexes but structured in the Rad4-Rad23, when there is no DNA present. ","type":"Curator statement"},{"text":"The UBA2 domain is disordered in the DNA-bound Rad4–Rad23 crystal forms. It is conceivable that the ordered nature of UBA2 in the apoRad4–Rad23 crystals is due to the extensive crystal-packing contacts it makes. In the DNA-bound crystal forms, the area where UBA2 would be is open to a large solvent channel that would not provide any crystal packing contacts.","type":"Supplementary material"}],"states_connection":[{"source":"DP01629r013","target":"DP01629r011"}],"sequence_construct":"GSGNASSGALGTTGGATDAAQGGPPGSIGLTVEDLLSLRQVVSGNPEALAPLLENISARYPQLREHIMANPEVFVSMLLEAVGDNMQDVMEGADDMVEGEDIEVTGEAAAAGLGQGEGEGSFQVDYTPEDDQAISRLCELGFERDLVIQVYFACDKNEEAAANILFSDHAD"},{"start":347,"end":395,"reference_id":"17882165","reference_source":"pmid","reference_html":"Recognition of DNA damage by the Rad4 nucleotide excision repair protein. <i> Min JH, Pavletich NP. </i> Nature, 2007","date":"2023-09-26T16:27:52.409Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2QSF"}],"region_id":"DP01629r013","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P14736"}],"statement":[{"text":"The refined model contains residues 126–300, 304–515, 528–599 and 606–632 of Rad4, residues 255–309 and 347–395 of Rad23, and 250 water molecules.","type":"Methods"}],"sequence_construct":"GSGNASSGALGTTGGATDAAQGGPPGSIGLTVEDLLSLRQVVSGNPEALAPLLENISARYPQLREHIMANPEVFVSMLLEAVGDNMQDVMEGADDMVEGEDIEVTGEAAAAGLGQGEGEGSFQVDYTPEDDQAISRLCELGFERDLVIQVYFACDKNEEAAANILFSDHAD"},{"start":310,"end":346,"reference_id":"17882165","reference_source":"pmid","reference_html":"Recognition of DNA damage by the Rad4 nucleotide excision repair protein. <i> Min JH, Pavletich NP. </i> Nature, 2007","date":"2023-09-26T16:42:50.623Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2QSF"}],"region_id":"DP01629r014","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P14736"}],"statement":[{"text":"The refined model contains residues 126–300, 304–515, 528–599 and 606–632 of Rad4, residues 255–309 and 347–395 of Rad23, and 250 water molecules.","type":"Methods"},{"text":"The 310-346 disordered regions constitutes a linker between the R4BD (253-309) and UBA2 (347-398) domains.","type":"Curator statement"}]}],"released":"2018_11","uniref100":"UniRef100_P32628","date":"2018-08-03T12:16:48.000Z","acc":"P32628","name":"UV excision repair protein RAD23","length":398,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000053043","genes":[{"name":{"value":"RAD23"},"orfNames":[{"value":"SYGP-ORF29"}],"olnNames":[{"value":"YEL037C"}]}],"alphafold_very_low_content":0.34673366834170855,"disorder_content":0.6055276381909548,"disprot_consensus":{"full":[{"start":77,"end":147,"type":"D"},{"start":185,"end":265,"type":"D"},{"start":310,"end":346,"type":"D"},{"start":347,"end":395,"type":"T"},{"start":396,"end":398,"type":"D"}],"Structural state":[{"start":77,"end":147,"type":"D"},{"start":185,"end":265,"type":"D"},{"start":310,"end":398,"type":"D"}],"Disorder function":[{"start":77,"end":147,"type":"F"},{"start":185,"end":265,"type":"F"},{"start":310,"end":355,"type":"F"}],"Structural transition":[{"start":347,"end":395,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00752","name":"XPG N-terminal domain","start":1,"end":97},{"id":"PF00867","name":"XPG I-region","start":783,"end":864}],"gene3D":[{"start":1,"end":129,"id":"3.40.50.1010","name":"5'-nuclease"},{"start":741,"end":1016,"id":"3.40.50.1010","name":"5'-nuclease"}]},"uniref50":"UniRef50_P07276","sequence":"MGVHSFWDIAGPTARPVRLESLEDKRMAVDASIWIYQFLKAVRDQEGNAVKNSHITGFFRRICKLLYFGIRPVFVFDGGVPVLKRETIRQRKERRQGKRESAKSTARKLLALQLQNGSNDNVKNSTPSSGSSVQIFKPQDEWDLPDIPGFKYDKEDARVNSNKTFEKLMNSINGDGLEDIDLDTINPASAEFEELPKATQYLILSSLRLKSRLRMGYSKEQLETIFPNSMDFSRFQIDMVKRRNFFTQKLINTTGFQDGGASKLNEEVINRISGQKSKEYKLTKTNNGWILGLGANDGSDAQKAIVIDDKDAGALVKQLDSNAEDGDVLRWDDLEDNSLKIVRHESSNATTAPQKRSNRSEDEGCDSDECEWEEVELKPKNVKFVEDFSLKAARLPYMGQSLNNAGSKSFLDKRHDQASPSKTTPTMRISRISVEDDDEDYLKQIEEIEMMEAVQLSKMEKKPEADDKSKIAKPVTSKGTEARPPIVQYGLLGAQPDSKQPYHVTNLNSKSESVIKRTSKTVLSEFRPPSQQEDKGAILTEGEQNLNFISHKIPQFDFNNENSLLFQKNTESNVSQEATKEKSPIPEMPSWFSSTASQQLYNPYNTTNFVEDKNVRNEQESGAETTNKGSSYELLTGLNATEILERESEKESSNDENKDDDLEVLSEELFEDVPTKSQISKEAEDNDSRKVESINKEHRKPLIFDYDFSEDEEDNIVENMIKEQEEFDTFKNTTLSTSAERNVAENAFVEDELFEQQMKDKRDSDEVTMDMIKEVQELLSRFGIPYITAPMEAEAQCAELLQLNLVDGIITDDSDVFLFGGTKIYKNMFHEKNYVEFYDAESILKLLGLDRKNMIELAQLLGSDYTNGLKGMGPVSSIEVIAEFGNLKNFKDWYNNGQFDKRKQETENKFEKDLRKKLVNNEIILDDDFPSVMVYDAYMRPEVDHDTTPFVWGVPDLDMLRSFMKTQLGWPHEKSDEILIPLIRDVNKRKKKGKQKRINEFFPREYISGDKKLNTSKRISTATGKLKKRKM","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P07276","disprot_id":"DP01631","ncbi_taxon_id":559292,"regions_counter":6,"creator":"bhajdu","regions":[{"region_id":"DP01631r001","ec_ontology":"ECO","end":690,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":642,"version":3,"statement":[{"text":"Rad2642–690 exists in an extended conformation devoid of any regular secondary structural element with residues 664–678 forming the interface with Tfb1PH.","type":"Results"}],"term_name":"disorder","reference_html":"Structural and functional characterization of interactions involving the Tfb1 subunit of TFIIH and the NER factor Rad2. <i> Lafrance-Vanasse J, Arseneault G, Cappadocia L, Chen HT, Legault P, Omichinski JG. </i> Nucleic Acids Res, 2012","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"22373916","date":"2023-09-26T18:26:08.319Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2LOX"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P32776"}],"sequence_construct":"GSEILERESEKESSNDENKDDDLEVLSEELFEDVPTKSQISKEAEDNDSRKY"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":678,"term_name":"protein binding","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural and functional characterization of interactions involving the Tfb1 subunit of TFIIH and the NER factor Rad2. <i> Lafrance-Vanasse J, Arseneault G, Cappadocia L, Chen HT, Legault P, Omichinski JG. </i> Nucleic Acids Res, 2012","statement":[{"text":"Rad2642–690 exists in an extended conformation devoid of any regular secondary structural element with residues 664–678 forming the interface with Tfb1PH. This is consistent with the 1H–15N HSQC spectra of the titration of 15N-labeled Rad2642–690 with Tfb1PH as it is these residues that display significant changes in their 1H and 15N chemical shifts (Supplementary Figure S4).","type":"Results"}],"term_id":"GO:0005515","curator_id":"vnugnes","start":664,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"22373916","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-09-26T18:29:53.711Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01631r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"2LOX"}],"sequence_construct":"GSEILERESEKESSNDENKDDDLEVLSEELFEDVPTKSQISKEAEDNDSRKY","interaction_partner":[{"db":"UniProt","id":"P32776","operator":"and","partner_start":2,"partner_end":115}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":760,"region_id":"DP01631r003","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Structural and functional characterization of interactions involving the Tfb1 subunit of TFIIH and the NER factor Rad2. <i> Lafrance-Vanasse J, Arseneault G, Cappadocia L, Chen HT, Legault P, Omichinski JG. </i> Nucleic Acids Res, 2012","statement":[{"text":"NMR studies with a longer segment of the Rad2 spacer region (Rad2642–760) indicate that this segment does not contain a folded domain in the free form (Supplementary Figure S2), as observed with the free form of TFIIEαCTD.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":642,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-09-26T16:58:38.917Z","reference_source":"pmid","term_name":"disorder","reference_id":"22373916","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":642,"end":690,"reference_id":"22373916","reference_source":"pmid","reference_html":"Structural and functional characterization of interactions involving the Tfb1 subunit of TFIIH and the NER factor Rad2. <i> Lafrance-Vanasse J, Arseneault G, Cappadocia L, Chen HT, Legault P, Omichinski JG. </i> Nucleic Acids Res, 2012","date":"2023-09-26T17:03:29.386Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P32776","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01631r004","statement":[{"text":"By ITC, we determine that Rad2642–690 (Kd = 190 nM) binds with much higher affinity to Tfb1PH than Rad2692–760 (Kd = 4.6 µM).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":669,"end":673,"reference_id":"22373916","reference_source":"pmid","reference_html":"Structural and functional characterization of interactions involving the Tfb1 subunit of TFIIH and the NER factor Rad2. <i> Lafrance-Vanasse J, Arseneault G, Cappadocia L, Chen HT, Legault P, Omichinski JG. </i> Nucleic Acids Res, 2012","date":"2023-09-26T18:22:07.929Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe670Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val673Pro","start":null,"end":null,"position":null}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P32776","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01631r005","sequence_construct":"GSEILERESEKESSNDENKDDDLEVLSEELPEDPPTKSQISKEAEDNDSRKY","statement":[{"text":"The ITC studies show that neither the F670P nor V673P mutant of Rad2642–690 bind with appreciable affinity.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":642,"end":690,"reference_id":"22373916","reference_source":"pmid","reference_html":"Structural and functional characterization of interactions involving the Tfb1 subunit of TFIIH and the NER factor Rad2. <i> Lafrance-Vanasse J, Arseneault G, Cappadocia L, Chen HT, Legault P, Omichinski JG. </i> Nucleic Acids Res, 2012","date":"2023-09-26T18:55:50.507Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006309","ec_ontology":"ECO","ec_name":"competitive binding evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe670Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val673Pro","start":null,"end":null,"position":null}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P32776","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01631r006","sequence_construct":"GSEILERESEKESSNDENKDDDLEVLSEELPEDPPTKSQISKEAEDNDSRKY","statement":[{"text":"When mapped onto the structure of Tfb1PH, the residues exhibiting significant chemical shift changes are located in strands β5, β6, β7 and the helix H1 (Figure 5b) and the changes are very similar to those observed with Rad2642–690 (Figure 3a). NMR competition experiments further demonstrate that Rad2359–383 and Rad2642–690 compete for binding to Tfb1PH (Figure 5c and d).","type":"Results"},{"text":"Taken together with previous results showing that TFIIEαCTD and p53TAD2 compete for binding to Tfb1PH (19), these results demonstrate that TFIIEαCTD, p53TAD2 and Rad2642–690 all share for a common binding site on Tfb1PH.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_P07276","date":"2018-08-03T13:30:40.000Z","acc":"P07276","name":"DNA repair protein RAD2","length":1031,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000017B328","genes":[{"name":{"value":"RAD2"},"olnNames":[{"value":"YGR258C"}]}],"alphafold_very_low_content":0.38700290979631424,"disorder_content":0.11542192046556742,"disprot_consensus":{"full":[{"start":642,"end":760,"type":"D"}],"Structural state":[{"start":642,"end":760,"type":"D"}],"Molecular function":[{"start":642,"end":690,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02002","name":"TFIIE alpha subunit","start":16,"end":123},{"id":"PF08271","name":"TFIIB zinc-binding","start":127,"end":175},{"id":"PF11521","name":"C-terminal general transcription factor TFIIE alpha","start":354,"end":439}],"gene3D":[{"start":113,"end":174,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"}]},"uniref50":"UniRef50_P29083","sequence":"MADPDVLTEVPAALKRLAKYVIRGFYGIEHALALDILIRNSCVKEEDMLELLKFDRKQLRSVLNNLKGDKFIKCRMRVETAADGKTTRHNYYFINYRTLVNVVKYKLDHMRRRIETDERDSTNRASFKCPVCSSTFTDLEANQLFDPMTGTFRCTFCHTEVEEDESAMPKKDARTLLARFNEQIEPIYALLRETEDVNLAYEILEPEPTEIPALKQSKDHAATTAGAASLAGGHHREAWATKGPSYEDLYTQNVVINMDDQEDLHRASLEGKSAKERPIWLRESTVQGAYGSEDMKEGGIDMDAFQEREEGHAGPDDNEEVMRALLIHEKKTSSAMAGSVGAAAPVTAANGSDSESETSESDDDSPPRPAAVAVHKREEDEEEDDEFEEVADDPIVMVAGRPFSYSEVSQRPELVAQMTPEEKEAYIAMGQRMFEDLFE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P29083","disprot_id":"DP01633","ncbi_taxon_id":9606,"regions_counter":4,"creator":"bhajdu","regions":[{"region_id":"DP01633r001","ec_ontology":"ECO","end":393,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":378,"version":3,"statement":[{"text":"To characterize the precise interaction at the molecular level, we first solved a solution structure of the AC-D of hTFIIEα using NMR spectroscopy (Figure 1B and Table I). The protein has a globular structure with flexible and disordered tails, consisting of the 16 N-terminal residues (amino acids 378–393) and the 5 C-terminal residues (amino acids 435–439).","type":"Results"}],"term_name":"disorder","reference_html":"Structural insight into the TFIIE-TFIIH interaction: TFIIE and p53 share the binding region on TFIIH. <i> Okuda M, Tanaka A, Satoh M, Mizuta S, Takazawa M, Ohkuma Y, Nishimura Y. </i> EMBO J, 2008","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18354501","date":"2023-09-26T19:12:18.776Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2RNQ"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":393,"term_name":"disorder to order","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural insight into the TFIIE-TFIIH interaction: TFIIE and p53 share the binding region on TFIIH. <i> Okuda M, Tanaka A, Satoh M, Mizuta S, Takazawa M, Ohkuma Y, Nishimura Y. </i> EMBO J, 2008","statement":[{"text":"To characterize the precise interaction at the molecular level, we first solved a solution structure of the AC-D of hTFIIEα using NMR spectroscopy (Figure 1B and Table I). The protein has a globular structure with flexible and disordered tails, consisting of the 16 N-terminal residues (amino acids 378–393) and the 5 C-terminal residues (amino acids 435–439)","type":"Results"},{"text":"Although the N-terminal tail of hTFIIEα AC-D also becomes ordered upon binding to p62 PH-D, it forms a bent extended structure containing a S0 strand, but not α-helix.","type":"Results"},{"text":"In the free form, it is disordered (Figure 1B) but upon complex formation becomes fixed, forming a new S0 strand that extensively overlays the positively charged surface of p62 PH-D formed by K18, K19, K54, K60, K62 and K93 (Figure 3C).","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"vnugnes","start":378,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18354501","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-09-26T19:14:28.390Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01633r002","ec_go":"EXP","disprot_namespace":"Structural transition","cross_refs":[{"db":"PDB","id":"2RNQ"},{"db":"PDB","id":"2RNR"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P32780"}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":393,"term_name":"protein binding","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural insight into the TFIIE-TFIIH interaction: TFIIE and p53 share the binding region on TFIIH. <i> Okuda M, Tanaka A, Satoh M, Mizuta S, Takazawa M, Ohkuma Y, Nishimura Y. </i> EMBO J, 2008","statement":[{"text":"In hTFIIEα AC-D, the NMR signals of E386, F387, E388, E389, V390, A391 and D392 were changed significantly upon addition of p62 PH-D (Supplementary Figure 1B) and also in p62 PH-D the NMR signals of K19, Q53, K54, I55, S56, E58, K60, A61, I63, Q64, L65, Q66, T74, T75 and F77 were changed by adding hTFIIEα AC-D (Supplementary Figure 2B).","type":"Results"}],"term_id":"GO:0005515","curator_id":"vnugnes","start":378,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"18354501","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-09-26T19:16:29.546Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01633r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"2RNR"}],"interaction_partner":[{"db":"UniProt","id":"P32780","operator":"and","partner_start":19,"partner_end":77}]}],"released":"2018_11","uniref100":"UniRef100_P29083","date":"2018-08-03T13:52:15.000Z","acc":"P29083","name":"General transcription factor IIE subunit 1","length":439,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00001367F2","genes":[{"name":{"value":"GTF2E1"},"synonyms":[{"value":"TF2E1"}]}],"alphafold_very_low_content":0.26651480637813213,"disorder_content":0.03644646924829157,"disprot_consensus":{"full":[{"start":378,"end":393,"type":"T"}],"Structural state":[{"start":378,"end":393,"type":"D"}],"Structural transition":[{"start":378,"end":393,"type":"T"}],"Molecular function":[{"start":378,"end":393,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04270","name":"Streptococcal histidine triad protein","start":70,"end":89},{"id":"PF04270","name":"Streptococcal histidine triad protein","start":181,"end":231},{"id":"PF04270","name":"Streptococcal histidine triad protein","start":291,"end":335},{"id":"PF04270","name":"Streptococcal histidine triad protein","start":534,"end":585},{"id":"PF04270","name":"Streptococcal histidine triad protein","start":632,"end":653}],"gene3D":[{"start":531,"end":584,"id":"2.30.30.680","name":"2.30.30.680"},{"start":287,"end":337,"id":"2.30.30.680","name":"2.30.30.680"},{"start":178,"end":232,"id":"2.30.30.680","name":"2.30.30.680"},{"start":29,"end":166,"id":"2.30.30.680","name":"2.30.30.680"}]},"uniref50":"UniRef50_A0A4J2T148","sequence":"MKINKKYLAGSVAVLALSVCSYELGRHQAGQVKKESNRVSYIDGDQAGQKAENLTPDEVSKREGINAEQIVIKITDQGYVTSHGDHYHYYNGKVPYDAIISEELLMKDPNYQLKDSDIVNEIKGGYVIKVDGKYYVYLKDAAHADNIRTKEEIKRQKQERSHNHNSRADNAVAAARAQGRYTTDDGYIFNASDIIEDTGDAYIVPHGDHYHYIPKSDLSASELAAAQAYWNGKQGSRPSSSSSHNANPAQPRLSENHNLTVTPTYHQNQGENISSLLRELYAKPLSERHVESDGLIFDPAQITSRTANGVAVPHGDHYHFIPYSQLSPLEEKLARIIPLRYRSNHWVPDSRPEQPSPQSTPEPSPSPQPAPNPQPAPSNPIDEKLVKEAVRKVGDGYVFEENGVPRYIPAKDLSAETAAGIDSKLAKQESLSHKLGAKKTDLPSSDREFYNKAYDLLARIHQDLLDNKGRQVDFEALDNLLERLKDVSSDKVKLVDDILAFLAPIRHPERLGKPNAQITYTDDEIQVAKLAGKYTTEDGYIFDPRDITSDEGDAYVTPHMTHSHWIKKDSLSEAERAAAQAYAKEKGLTPPSTDHQDSGNTEAKGAEAIYNRVKAAKKVPLDRMPYNLQYTVEVKNGSLIIPHYDHYHNIKFEWFDEGLYEAPKGYSLEDLLATVKYYVEHPNERPHSDNGFGNASDHVQRNKNGQADTNQTEKPNEEKPQTEKPEEDKEHDEVSEPTHPESDEKENHVGLNPSADNLYKPSTDTEETEEEAEDTTDEAEIPQVEHSVINAKIAEAEALLEKVTDSSIRQNAVETLTGLKSSLLLGTKDNNTISAEVDSLLALLKESQPTPIQ","taxonomy":["Bacteria","Firmicutes","Bacilli","Lactobacillales","Streptococcaceae","Streptococcus"],"uniref90":"UniRef90_A0A2U3RZL8","disprot_id":"DP01635","ncbi_taxon_id":373153,"regions_counter":1,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":50,"region_id":"DP01635r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"New insights into histidine triad proteins: solution structure of a Streptococcus pneumoniae PhtD domain and zinc transfer to AdcAII. <i> Bersch B, Bougault C, Roux L, Favier A, Vernet T, Durmort C. </i> PLoS One, 2013","statement":[{"text":"Residues S40 to K50 do not adopt a well-defined structure within the ensemble, suggesting that this part of the protein is disordered. This was confirmed by the heteronuclear {1H}15N-heteronuclear NOE data (see below, Fig. 4C). Structural statistics are presented in Table 1.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"akajava","start":40,"term_ontology":"IDPO","curator_name":"Andrey V Kajava","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-2342-6886","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3ZFJ"}],"reference_id":"24312273","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-24T19:11:24.172Z"}}],"released":"2018_11","uniref100":"UniRef100_A0A2U3RZL8","date":"2018-08-03T14:18:51.000Z","acc":"A0A0H2ZP82","name":"Pneumococcal histidine triad protein D","length":853,"organism":"Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)","dataset":[],"UniParc":"UPI00000E3553","genes":[{"name":{"value":"phtD","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ABJ54443.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABJ54443.1"}}]},"olnNames":[{"value":"SPD_0889","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ABJ54443.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABJ54443.1"}}]}]}],"alphafold_very_low_content":0.2966002344665885,"disorder_content":0.012895662368112544,"disprot_consensus":{"full":[{"start":40,"end":50,"type":"D"}],"Structural state":[{"start":40,"end":50,"type":"D"}]}},{"features":{"pfam":[{"id":"PF13499","name":"EF-hand domain pair","start":77,"end":143}],"gene3D":[{"start":69,"end":146,"id":"1.10.238.10","name":"EF-hand"}]},"uniref50":"UniRef50_Q8NI22","sequence":"MTMRSLLRTPFLCGLLWAFCAPGARAEEPAASFSQPGSMGLDKNTVHDQEHIMEHLEGVINKPEAEMSPQELQLHYFKMHDYDGNNLLDGLELSTAITHVHKEEGSEQAPLMSEDELINIIDGVLRDDDKNNDGYIDYAEFAKSLQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q8NI22","disprot_id":"DP01637","ncbi_taxon_id":9606,"regions_counter":11,"creator":"akajava","regions":[{"region_id":"DP01637r001","ec_ontology":"ECO","end":66,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":27,"version":3,"statement":[{"text":"Resonance assignment of MCFD2 allowed localization of the disordered region to the N-terminus of the protein, approximately residues 27–66 (sequence numbered to include the signal sequence).","type":"Results"},{"text":"The N-terminus, residues 27–66, contains very few medium- or long-range restraints and a similar situation is seen for residues 102–112, a flexible loop region.","type":"Results"}],"term_name":"disorder","reference_html":"New insights into multiple coagulation factor deficiency from the solution structure of human MCFD2. <i> Guy JE, Wigren E, Svärd M, Härd T, Lindqvist Y. </i> J Mol Biol, 2008","released":"2022_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18590741","date":"2022-08-24T19:58:16.006Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2VRG"},{"db":"BMRB","id":"15789"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}]},{"start":27,"end":146,"reference_id":"18590741","reference_source":"pmid","reference_html":"New insights into multiple coagulation factor deficiency from the solution structure of human MCFD2. <i> Guy JE, Wigren E, Svärd M, Härd T, Lindqvist Y. </i> J Mol Biol, 2008","date":"2022-08-24T19:51:35.260Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP01637r002","statement":[{"text":"The NMR spectrum of MCFD2 in calcium-free phosphate buffer at pH 6.0 is characteristic of an unfolded protein, and there is no evidence of secondary structure or of a hydrophobic core.","type":"Results"}]},{"start":27,"end":146,"reference_id":"18590741","reference_source":"pmid","reference_html":"New insights into multiple coagulation factor deficiency from the solution structure of human MCFD2. <i> Guy JE, Wigren E, Svärd M, Härd T, Lindqvist Y. </i> J Mol Biol, 2008","date":"2022-08-24T19:37:43.824Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP01637r003","statement":[{"text":"Circular dichroism (CD) spectroscopy performed on MCFD2 in the presence and absence of calcium confirms the apparent calcium-dependent folding of the protein seen in the NMR spectrum. ","type":"Results"},{"text":"Authors show the protein is intrinsically unstructured in the absence of calcium by its large negative ellipticity at 200 nm and moderate ellipticity at 190 nm.","type":"Curator statement"}]},{"start":27,"end":52,"reference_id":"18590741","reference_source":"pmid","reference_html":"New insights into multiple coagulation factor deficiency from the solution structure of human MCFD2. <i> Guy JE, Wigren E, Svärd M, Härd T, Lindqvist Y. </i> J Mol Biol, 2008","date":"2022-08-24T19:47:42.204Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP01637r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"Circular dichroism (CD) spectroscopy performed on MCFD2 in the presence and absence of calcium confirms the apparent calcium-dependent folding of the protein seen in the NMR spectrum. The CD spectrum changes drastically upon addition of calcium (Fig. 3a), and the spectrum of the Ca2+-bound form reveals a dominating contribution from α-helical secondary structure with minima at 207 and 222 nm and a change of sign from negative to positive CD at 197 nm. The calcium-dependent folding is further confirmed by comparison of the CD signal measured at 222 nm as a function of calcium concentration (Fig. 3b).","type":"Results"},{"text":"The spectra of wild-type MCFD2 show higher disorder and proportionally lower helical content, when compared to the spectra of the truncated protein. The calculated difference between the two spectra yields a profile, corresponding to the signal from the first 26 residues of the N-terminus, which is characteristic of an unstructured protein.","type":"Results"}]},{"start":53,"end":146,"reference_id":"18590741","reference_source":"pmid","reference_html":"New insights into multiple coagulation factor deficiency from the solution structure of human MCFD2. <i> Guy JE, Wigren E, Svärd M, Härd T, Lindqvist Y. </i> J Mol Biol, 2008","date":"2022-08-24T19:48:28.100Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP01637r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"Circular dichroism (CD) spectroscopy performed on MCFD2 in the presence and absence of calcium confirms the apparent calcium-dependent folding of the protein seen in the NMR spectrum. The CD spectrum changes drastically upon addition of calcium (Fig. 3a), and the spectrum of the Ca2+-bound form reveals a dominating contribution from α-helical secondary structure with minima at 207 and 222 nm and a change of sign from negative to positive CD at 197 nm. The calcium-dependent folding is further confirmed by comparison of the CD signal measured at 222 nm as a function of calcium concentration (Fig. 3b).","type":"Results"},{"text":"The spectra of wild-type MCFD2 show higher disorder and proportionally lower helical content, when compared to the spectra of the truncated protein. The calculated difference between the two spectra yields a profile, corresponding to the signal from the first 26 residues of the N-terminus, which is characteristic of an unstructured protein.","type":"Results"}]},{"start":53,"end":146,"reference_id":"18590741","reference_source":"pmid","reference_html":"New insights into multiple coagulation factor deficiency from the solution structure of human MCFD2. <i> Guy JE, Wigren E, Svärd M, Härd T, Lindqvist Y. </i> J Mol Biol, 2008","date":"2022-08-24T19:49:54.948Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP01637r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"Circular dichroism (CD) spectroscopy performed on MCFD2 in the presence and absence of calcium confirms the apparent calcium-dependent folding of the protein seen in the NMR spectrum. The CD spectrum changes drastically upon addition of calcium (Fig. 3a), and the spectrum of the Ca2+-bound form reveals a dominating contribution from α-helical secondary structure with minima at 207 and 222 nm and a change of sign from negative to positive CD at 197 nm. The calcium-dependent folding is further confirmed by comparison of the CD signal measured at 222 nm as a function of calcium concentration (Fig. 3b).","type":"Results"},{"text":"The spectra of wild-type MCFD2 show higher disorder and proportionally lower helical content, when compared to the spectra of the truncated protein. The calculated difference between the two spectra yields a profile, corresponding to the signal from the first 26 residues of the N-terminus, which is characteristic of an unstructured protein.","type":"Results"}],"states_connection":[{"source":"DP01637r003","target":"DP01637r005"}]},{"start":66,"end":101,"reference_id":"18590741","reference_source":"pmid","reference_html":"New insights into multiple coagulation factor deficiency from the solution structure of human MCFD2. <i> Guy JE, Wigren E, Svärd M, Härd T, Lindqvist Y. </i> J Mol Biol, 2008","date":"2022-08-24T19:53:29.626Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"BMRB","id":"15789"},{"db":"PDB","id":"2VRG"}],"region_id":"DP01637r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"The NMR spectrum in the presence of calcium shows a marked difference, with clear indications of both secondary and tertiary structure, although some disorder evidently remains.","type":"Results"},{"text":"Resonance assignment of MCFD2 allowed localization of the disordered region to the N-terminus of the protein, approximately residues 27–66 (sequence numbered to include the signal sequence).","type":"Results"},{"text":"The N-terminus, residues 27–66, contains very few medium- or long-range restraints and a similar situation is seen for residues 102–112, a flexible loop region.","type":"Results"}]},{"start":113,"end":146,"reference_id":"18590741","reference_source":"pmid","reference_html":"New insights into multiple coagulation factor deficiency from the solution structure of human MCFD2. <i> Guy JE, Wigren E, Svärd M, Härd T, Lindqvist Y. </i> J Mol Biol, 2008","date":"2022-08-24T19:53:43.495Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"BMRB","id":"15789"},{"db":"PDB","id":"2VRG"}],"region_id":"DP01637r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"The NMR spectrum in the presence of calcium shows a marked difference, with clear indications of both secondary and tertiary structure, although some disorder evidently remains.","type":"Results"},{"text":"Resonance assignment of MCFD2 allowed localization of the disordered region to the N-terminus of the protein, approximately residues 27–66 (sequence numbered to include the signal sequence).","type":"Results"},{"text":"The N-terminus, residues 27–66, contains very few medium- or long-range restraints and a similar situation is seen for residues 102–112, a flexible loop region.","type":"Results"}]},{"start":113,"end":146,"reference_id":"18590741","reference_source":"pmid","reference_html":"New insights into multiple coagulation factor deficiency from the solution structure of human MCFD2. <i> Guy JE, Wigren E, Svärd M, Härd T, Lindqvist Y. </i> J Mol Biol, 2008","date":"2022-08-24T19:59:39.990Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"BMRB","id":"15789"},{"db":"PDB","id":"2VRG"}],"region_id":"DP01637r009","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"The NMR spectrum in the presence of calcium shows a marked difference, with clear indications of both secondary and tertiary structure, although some disorder evidently remains.","type":"Results"},{"text":"In summary, we have shown human MCFD2 to be disordered in the absence of calcium and to adopt a predominantly ordered structure on binding calcium, but with the N-terminus remaining disordered and conformational flexibility in the extended loop between the two EF-hand motifs.","type":"Results"}],"states_connection":[{"source":"DP01637r002","target":"DP01637r008"}]},{"start":66,"end":101,"reference_id":"18590741","reference_source":"pmid","reference_html":"New insights into multiple coagulation factor deficiency from the solution structure of human MCFD2. <i> Guy JE, Wigren E, Svärd M, Härd T, Lindqvist Y. </i> J Mol Biol, 2008","date":"2022-08-24T20:00:07.347Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"BMRB","id":"15789"},{"db":"PDB","id":"2VRG"}],"region_id":"DP01637r010","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"The NMR spectrum in the presence of calcium shows a marked difference, with clear indications of both secondary and tertiary structure, although some disorder evidently remains.","type":"Results"},{"text":"In summary, we have shown human MCFD2 to be disordered in the absence of calcium and to adopt a predominantly ordered structure on binding calcium, but with the N-terminus remaining disordered and conformational flexibility in the extended loop between the two EF-hand motifs.","type":"Results"}],"states_connection":[{"source":"DP01637r002","target":"DP01637r007"}]},{"start":102,"end":112,"reference_id":"18590741","reference_source":"pmid","reference_html":"New insights into multiple coagulation factor deficiency from the solution structure of human MCFD2. <i> Guy JE, Wigren E, Svärd M, Härd T, Lindqvist Y. </i> J Mol Biol, 2008","date":"2022-08-24T19:58:40.389Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"BMRB","id":"15789"},{"db":"PDB","id":"2VRG"}],"region_id":"DP01637r011","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"The N-terminus, residues 27–66, contains very few medium- or long-range restraints and a similar situation is seen for residues 102–112, a flexible loop region.","type":"Results"},{"text":"Between the two EF hands is a less well-defined and apparently flexible loop (residues 102–112) that is significantly longer than the equivalent loop in calmodulin. Assignment of the residues in this loop was extremely difficult due to the weak, broadened nature of the observed resonances, indicating conformational flexibility and exchange, as further discussed below.","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_Q8NI22","date":"2018-08-03T14:38:33.000Z","acc":"Q8NI22","name":"Multiple coagulation factor deficiency protein 2","length":146,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000005275E","genes":[{"name":{"value":"MCFD2"},"synonyms":[{"value":"SDNSF"}]}],"alphafold_very_low_content":0.1232876712328767,"disorder_content":0.821917808219178,"disprot_consensus":{"full":[{"start":27,"end":52,"type":"D"},{"start":53,"end":146,"type":"T"}],"Structural state":[{"start":27,"end":146,"type":"D"}],"Structural transition":[{"start":53,"end":146,"type":"T"}]}},{"features":{"pfam":[{"id":"PF03909","name":"BSD domain","start":176,"end":226},{"id":"PF03909","name":"BSD domain","start":244,"end":300},{"id":"PF08567","name":"TFIIH p62 subunit, N-terminal domain","start":9,"end":105}],"gene3D":[{"start":1,"end":115,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"}]},"uniref50":"UniRef50_P32776","sequence":"MSHSGAAIFEKVSGIIAINEDVSPAELTWRSTDGDKVHTVVLSTIDKLQATPASSEKMMLRLIGKVDESKKRKDNEGNEVVPKPQRHMFSFNNRTVMDNIKMTLQQIISRYKDADIYEEKRRREESAQHTETPMSSSSVTAGTPTPHLDTPQLNNGAPLINTAKLDDSLSKEKLLTNLKLQQSLLKGNKVLMKVFQETVINAGLPPSEFWSTRIPLLRAFALSTSQKVGPYNVLSTIKPVASSENKVNVNLSREKILNIFENYPIVKKAYTDNVPKNFKEPEFWARFFSSKLFRKLRGEKIMQNDRGDVIIDRYLTLDQEFDRKDDDMLLHPVKKIIDLDGNIQDDPVVRGNRPDFTMQPGVDINGNSDGTVDILKGMNRLSEKMIMALKNEYSRTNLQNKSNITNDEEDEDNDERNELKIDDLNESYKTNYAIIHLKRNAHEKTTDNDAKSSADSIKNADLKVSNQQMLQQLSLVMDNLINKLDLNQVVPNNEVSNKINKRVITAIKINAKQAKHNNVNSALGSFVDNTSQANELEVKSTLPIDLLESCRMLHTTCCEFLKHFYIHFQSGEQKQASTVKKLYNHLKDCIEKLNELFQDVLNGDGESMSNTCTAYLKPVLNSITLATHKYDEYFNEYNNNSN","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P32776","disprot_id":"DP01638","ncbi_taxon_id":559292,"regions_counter":12,"creator":"bhajdu","regions":[{"region_id":"DP01638r001","ec_ontology":"ECO","end":85,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":64,"version":3,"statement":[{"text":"Residues at the N terminus (1–4), at the C terminus (113–115), and in the flexible loop (64–85) of Tfb1PH, as well as residues at the N terminus (642–668) and at the C terminus (676–690) of Rad2 were not included in the calculation.","type":"Table"}],"term_name":"disorder","reference_html":"Structural and functional characterization of interactions involving the Tfb1 subunit of TFIIH and the NER factor Rad2. <i> Lafrance-Vanasse J, Arseneault G, Cappadocia L, Chen HT, Legault P, Omichinski JG. </i> Nucleic Acids Res, 2012","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"22373916","date":"2023-09-27T13:49:59.832Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2LOX"},{"db":"BMRB","id":"18229"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met1Pro","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P07276"}],"sequence_construct":"PSHSGAAIFEKVSGIIAINEDVSPAELTWRSTDGDKVHTVVLSTIDKLQATPASSEKMMLRLIGKVDESKKRKDNEGNEVVPKPQRHMFSFNNRTVMDNIKMTLQQIISRYKDADGNSS"},{"region_id":"DP01638r002","ec_ontology":"ECO","end":84,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":65,"version":3,"statement":[{"text":"The other difference between Tfb1 and other PH domains occurs in the loop connecting strands β6 and β7 (VL3). Tfb11-115 contains a very long (20 residues) and flexible loop that is highly basic. In fact, almost all of the amino acids in this region have 15N−1H heteronuclear NOE values in the range of 0.13−0.40 (data not shown), indicating a high degree of backbone motion on the picosecond to nanosecond time scale.","type":"Results"}],"term_name":"disorder","reference_html":"NMR structure of the amino-terminal domain from the Tfb1 subunit of TFIIH and characterization of its phosphoinositide and VP16 binding sites. <i> Di Lello P, Nguyen BD, Jones TN, Potempa K, Kobor MS, Legault P, Omichinski JG. </i> Biochemistry, 2005","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15909982","date":"2023-09-27T13:45:07.142Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1Y5O"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met1Pro","start":null,"end":null,"position":null}],"sequence_construct":"PSHSGAAIFEKVSGIIAINEDVSPAELTWRSTDGDKVHTVVLSTIDKLQATPASSEKMMLRLIGKVDESKKRKDNEGNEVVPKPQRHMFSFNNRTVMDNIKMTLQQIISRYKDAD"},{"region_id":"DP01638r003","ec_ontology":"ECO","end":84,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":66,"version":3,"statement":[{"text":"Structure of the Tfb1PH/EKLFTAD2 Complex. (A) Overlay of the 20 lowest-energy structures of the complex between Tfb1PH (blue) and EKLFTAD2 (yellow). The structures were superimposed using the backbone atoms C′, Cα, and N of residues 4–65 and 85–112 of Tfb1PH and residues 59–84 of EKLFTAD2.","type":"Figure"}],"term_name":"disorder","reference_html":"Structural and functional characterization of an atypical activation domain in erythroid Kruppel-like factor (EKLF). <i> Mas C, Lussier-Price M, Soni S, Morse T, Arseneault G, Di Lello P, Lafrance-Vanasse J, Bieker JJ, Omichinski JG. </i> Proc Natl Acad Sci U S A, 2011","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"21670263","date":"2023-09-27T13:41:34.450Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2L2I"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q13351"}]},{"region_id":"DP01638r004","ec_ontology":"ECO","end":84,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":64,"version":3,"statement":[{"text":"Residues at the N terminus (1–3), at the C terminus (113–115), and in the flexible loop (64–84) of Tfb1, as well as residues at the N terminus (45–46) and at the C terminus (57–58) of p53, were not included in the calculation.","type":"Table"}],"term_name":"disorder","reference_html":"Structure of the Tfb1/p53 complex: Insights into the interaction between the p62/Tfb1 subunit of TFIIH and the activation domain of p53. <i> Di Lello P, Jenkins LMM, Jones TN, Nguyen BD, Hara T, Yamaguchi H, Dikeakos JD, Appella E, Legault P, Omichinski JG. </i> Mol Cell, 2006","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16793543","date":"2023-09-27T13:34:58.007Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2GS0"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met1Pro","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04637"}],"sequence_construct":"PSHSGAAIFEKVSGIIAINEDVSPAELTWRSTDGDKVHTVVLSTIDKLQATPASSEKMMLRLIGKVDESKKRKDNEGNEVVPKPQRHMFSFNNRTVMDNIKMTLQQIISRYKDAD"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":84,"term_name":"flexible linker","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structure of the Tfb1/p53 complex: Insights into the interaction between the p62/Tfb1 subunit of TFIIH and the activation domain of p53. <i> Di Lello P, Jenkins LMM, Jones TN, Nguyen BD, Hara T, Yamaguchi H, Dikeakos JD, Appella E, Legault P, Omichinski JG. </i> Mol Cell, 2006","statement":[{"text":"Residues at the N terminus (1–3), at the C terminus (113–115), and in the flexible loop (64–84) of Tfb1, as well as residues at the N terminus (45–46) and at the C terminus (57–58) of p53, were not included in the calculation.","type":"Table"}],"term_id":"IDPO:0000033","curator_id":"vnugnes","start":64,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16793543","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-09-27T13:35:39.741Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01638r005","ec_go":"EXP","disprot_namespace":"Disorder function","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met1Pro","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"2GS0"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04637"}],"sequence_construct":"PSHSGAAIFEKVSGIIAINEDVSPAELTWRSTDGDKVHTVVLSTIDKLQATPASSEKMMLRLIGKVDESKKRKDNEGNEVVPKPQRHMFSFNNRTVMDNIKMTLQQIISRYKDAD"},{"start":65,"end":84,"reference_id":"15909982","reference_source":"pmid","reference_html":"NMR structure of the amino-terminal domain from the Tfb1 subunit of TFIIH and characterization of its phosphoinositide and VP16 binding sites. <i> Di Lello P, Nguyen BD, Jones TN, Potempa K, Kobor MS, Legault P, Omichinski JG. </i> Biochemistry, 2005","date":"2023-09-27T13:47:05.441Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met1Pro","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"1Y5O"}],"region_id":"DP01638r006","sequence_construct":"PSHSGAAIFEKVSGIIAINEDVSPAELTWRSTDGDKVHTVVLSTIDKLQATPASSEKMMLRLIGKVDESKKRKDNEGNEVVPKPQRHMFSFNNRTVMDNIKMTLQQIISRYKDAD","statement":[{"text":"The other difference between Tfb1 and other PH domains occurs in the loop connecting strands β6 and β7 (VL3). Tfb11-115 contains a very long (20 residues) and flexible loop that is highly basic. In fact, almost all of the amino acids in this region have 15N−1H heteronuclear NOE values in the range of 0.13−0.40 (data not shown), indicating a high degree of backbone motion on the picosecond to nanosecond time scale.","type":"Results"}]},{"start":64,"end":85,"reference_id":"22373916","reference_source":"pmid","reference_html":"Structural and functional characterization of interactions involving the Tfb1 subunit of TFIIH and the NER factor Rad2. <i> Lafrance-Vanasse J, Arseneault G, Cappadocia L, Chen HT, Legault P, Omichinski JG. </i> Nucleic Acids Res, 2012","date":"2023-09-27T13:51:25.241Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met1Pro","start":null,"end":null,"position":null}],"cross_refs":[{"db":"BMRB","id":"18229"},{"db":"PDB","id":"2LOX"}],"region_id":"DP01638r007","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P07276"}],"sequence_construct":"PSHSGAAIFEKVSGIIAINEDVSPAELTWRSTDGDKVHTVVLSTIDKLQATPASSEKMMLRLIGKVDESKKRKDNEGNEVVPKPQRHMFSFNNRTVMDNIKMTLQQIISRYKDADGNSS","statement":[{"text":"Residues at the N terminus (1–4), at the C terminus (113–115), and in the flexible loop (64–85) of Tfb1PH, as well as residues at the N terminus (642–668) and at the C terminus (676–690) of Rad2 were not included in the calculation.","type":"Table"}]},{"start":67,"end":82,"reference_id":"34133942","reference_source":"pmid","reference_html":"Structure of RNA polymerase II pre-initiation complex at 2.9 Å defines initial DNA opening. <i> Schilbach S, Aibara S, Dienemann C, Grabbe F, Cramer P. </i> Cell, 2021","date":"2023-09-27T14:55:36.764Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"12720"},{"db":"PDB","id":"7O4J"}],"region_id":"DP01638r008","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P07276"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P36145"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P36100"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P32774"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P32773"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P41896"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P41895"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P13393"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P29055"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P40422"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P38902"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P22139"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P27999"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20436"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P34087"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20435"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20434"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20433"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P16370"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08518"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04050"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q00578"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q04673"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q3E7C1"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q12004"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q03290"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06839"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q02939"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"ENA","id":"KZV11580"}],"statement":[{"text":"The consensus structure of the yeast RNA polymerase II transcription pre-initiation complex shows this region of TFB1 lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":122,"end":166,"reference_id":"34133942","reference_source":"pmid","reference_html":"Structure of RNA polymerase II pre-initiation complex at 2.9 Å defines initial DNA opening. <i> Schilbach S, Aibara S, Dienemann C, Grabbe F, Cramer P. </i> Cell, 2021","date":"2023-09-27T14:55:17.242Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"12720"},{"db":"PDB","id":"7O4J"}],"region_id":"DP01638r009","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P07276"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P36145"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P36100"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P32774"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P32773"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P41896"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P41895"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P13393"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P29055"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P40422"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P38902"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P22139"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P27999"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20436"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P34087"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20435"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20434"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20433"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P16370"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08518"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04050"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q00578"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q04673"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q3E7C1"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q12004"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q03290"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06839"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q02939"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"ENA","id":"KZV11580"}],"statement":[{"text":"The consensus structure of the yeast RNA polymerase II transcription pre-initiation complex shows this region of TFB1 lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":394,"end":412,"reference_id":"34133942","reference_source":"pmid","reference_html":"Structure of RNA polymerase II pre-initiation complex at 2.9 Å defines initial DNA opening. <i> Schilbach S, Aibara S, Dienemann C, Grabbe F, Cramer P. </i> Cell, 2021","date":"2023-09-27T14:55:05.379Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"12720"},{"db":"PDB","id":"7O4J"}],"region_id":"DP01638r010","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P07276"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P36145"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P36100"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P32774"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P32773"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P41896"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P41895"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P13393"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P29055"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P40422"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P38902"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P22139"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P27999"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20436"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P34087"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20435"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20434"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20433"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P16370"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08518"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04050"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q00578"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q04673"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q3E7C1"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q12004"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q03290"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06839"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q02939"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"ENA","id":"KZV11580"}],"statement":[{"text":"The consensus structure of the yeast RNA polymerase II transcription pre-initiation complex shows this region of TFB1 lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":447,"end":461,"reference_id":"34133942","reference_source":"pmid","reference_html":"Structure of RNA polymerase II pre-initiation complex at 2.9 Å defines initial DNA opening. <i> Schilbach S, Aibara S, Dienemann C, Grabbe F, Cramer P. </i> Cell, 2021","date":"2023-09-27T14:54:49.367Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"12720"},{"db":"PDB","id":"7O4J"}],"region_id":"DP01638r011","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P07276"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P36145"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P36100"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P32774"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P32773"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P41896"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P41895"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P13393"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P29055"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P40422"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P38902"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P22139"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P27999"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20436"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P34087"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20435"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20434"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20433"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P16370"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08518"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04050"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q00578"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q04673"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q3E7C1"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q12004"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q03290"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06839"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q02939"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"ENA","id":"KZV11580"}],"statement":[{"text":"The consensus structure of the yeast RNA polymerase II transcription pre-initiation complex shows this region of TFB1 lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":518,"end":535,"reference_id":"34133942","reference_source":"pmid","reference_html":"Structure of RNA polymerase II pre-initiation complex at 2.9 Å defines initial DNA opening. <i> Schilbach S, Aibara S, Dienemann C, Grabbe F, Cramer P. </i> Cell, 2021","date":"2023-09-27T14:54:33.808Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"12720"},{"db":"PDB","id":"7O4J"}],"region_id":"DP01638r012","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P07276"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P36145"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P36100"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P32774"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P32773"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P41896"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P41895"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P13393"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P29055"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P40422"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P38902"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P22139"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P27999"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20436"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P34087"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20435"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20434"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20433"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P16370"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08518"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04050"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q00578"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q04673"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q3E7C1"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q12004"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q03290"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06839"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q02939"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"ENA","id":"KZV11580"}],"statement":[{"text":"The consensus structure of the yeast RNA polymerase II transcription pre-initiation complex shows this region of TFB1 lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"released":"2018_11","uniref100":"UniRef100_P32776","date":"2018-08-03T14:49:04.000Z","acc":"P32776","name":"General transcription and DNA repair factor IIH subunit TFB1","length":642,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000005304B","genes":[{"name":{"value":"TFB1"},"orfNames":[{"value":"D9740.3"}],"olnNames":[{"value":"YDR311W"}]}],"alphafold_very_low_content":0.11526479750778816,"disorder_content":0.1853582554517134,"disprot_consensus":{"full":[{"start":64,"end":85,"type":"D"},{"start":122,"end":166,"type":"D"},{"start":394,"end":412,"type":"D"},{"start":447,"end":461,"type":"D"},{"start":518,"end":535,"type":"D"}],"Structural state":[{"start":64,"end":85,"type":"D"},{"start":122,"end":166,"type":"D"},{"start":394,"end":412,"type":"D"},{"start":447,"end":461,"type":"D"},{"start":518,"end":535,"type":"D"}],"Disorder function":[{"start":64,"end":85,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00560","name":"Leucine Rich Repeat","start":318,"end":333},{"id":"PF12468","name":"Type III secretion system leucine rich repeat protein","start":8,"end":63}],"gene3D":[{"start":34,"end":386,"id":"3.80.10.10","name":"Ribonuclease Inhibitor"}]},"uniref50":"UniRef50_P17778","sequence":"MFINPRNVSNTFLQEPLRHSSNLTEMPVEAENVKSKTEYYNAWSEWERNAPPGNGEQREMAVSRLRDCLDRQAHELELNNLGLSSLPELPPHLESLVASCNSLTELPELPQSLKSLLVDNNNLKALSDLPPLLEYLGVSNNQLEKLPELQNSSFLKIIDVDNNSLKKLPDLPPSLEFIAAGNNQLEELPELQNLPFLTAIYADNNSLKKLPDLPLSLESIVAGNNILEELPELQNLPFLTTIYADNNLLKTLPDLPPSLEALNVRDNYLTDLPELPQSLTFLDVSENIFSGLSELPPNLYYLNASSNEIRSLCDLPPSLEELNVSNNKLIELPALPPRLERLIASFNHLAEVPELPQNLKQLHVEYNPLREFPDIPESVEDLRMNSERVVDPYEFAHETTDKLEDDVFE","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"],"uniref90":"UniRef90_P17778","disprot_id":"DP01639","ncbi_taxon_id":632,"regions_counter":1,"creator":"mpajkos","regions":[{"region_id":"DP01639r001","ec_ontology":"ECO","end":33,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":1,"version":3,"statement":[{"text":"However, no electron density can be observed for the first 33 residues of YopM, suggesting that this part of the protein may be disordered.","type":"Results"}],"term_name":"disorder","reference_html":"Unusual molecular architecture of the Yersinia pestis cytotoxin YopM: a leucine-rich repeat protein with the shortest repeating unit. <i> Evdokimov AG, Anderson DE, Routzahn KM, Waugh DS. </i> J Mol Biol, 2001","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"11575934","date":"2024-02-06T17:41:43.186Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1G9U"},{"db":"PDB","id":"1JL5"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P17778","date":"2018-08-03T15:16:43.000Z","acc":"P17778","name":"Outer membrane protein YopM","length":409,"organism":"Yersinia pestis","dataset":[],"UniParc":"UPI000017AAAF","genes":[{"name":{"value":"yopM"},"synonyms":[{"value":"yop48"}],"olnNames":[{"value":"YPCD1.26c"},{"value":"y5054"},{"value":"y0059"},{"value":"YP_pCD60"}]}],"alphafold_very_low_content":0.1198044009779951,"disorder_content":0.08068459657701711,"disprot_consensus":{"full":[{"start":1,"end":33,"type":"D"}],"Structural state":[{"start":1,"end":33,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00096","name":"Zinc finger, C2H2 type","start":279,"end":303},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":309,"end":333},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":339,"end":361},{"id":"PF16832","name":"Erythroid krueppel-like transcription factor, transactivation 1","start":22,"end":47},{"id":"PF16833","name":"Erythroid krueppel-like transcription factor, transactivation 2","start":59,"end":85}],"gene3D":[{"start":307,"end":333,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":280,"end":306,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":334,"end":362,"id":"3.30.160.60","name":"Classic Zinc Finger"}]},"uniref50":"UniRef50_Q13351","sequence":"MATAETALPSISTLTALGPFPDTQDDFLKWWRSEEAQDMGPGPPDPTEPPLHVKSEDQPGEEEDDERGADATWDLDLLLTNFSGPEPGGAPQTCALAPSEASGAQYPPPPETLGAYAGGPGLVAGLLGSEDHSGWVRPALRARAPDAFVGPALAPAPAPEPKALALQPVYPGPGAGSSGGYFPRTGLSVPAASGAPYGLLSGYPAMYPAPQYQGHFQLFRGLQGPAPGPATSPSFLSCLGPGTVGTGLGGTAEDPGVIAETAPSKRGRRSWARKRQAAHTCAHPGCGKSYTKSSHLKAHLRTHTGEKPYACTWEGCGWRFARSDELTRHYRKHTGQRPFRCQLCPRAFSRSDHLALHMKRHL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q13351","disprot_id":"DP01640","ncbi_taxon_id":9606,"regions_counter":10,"creator":"bhajdu","regions":[{"region_id":"DP01640r001","ec_ontology":"ECO","end":90,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":51,"version":3,"statement":[{"text":"EKLFTAD2 binds Tfb1PH in an elongated conformation devoid of any regular secondary structural elements (Fig. 3 A and B).","type":"Results"}],"term_name":"disorder","reference_html":"Structural and functional characterization of an atypical activation domain in erythroid Kruppel-like factor (EKLF). <i> Mas C, Lussier-Price M, Soni S, Morse T, Arseneault G, Di Lello P, Lafrance-Vanasse J, Bieker JJ, Omichinski JG. </i> Proc Natl Acad Sci U S A, 2011","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"21670263","date":"2023-09-27T15:07:27.502Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2L2I"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P32776"}],"sequence_construct":"GSLHVKSEDQPGEEEDDERGADATWDLDLLLTNFSGPEPGGA"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":90,"term_name":"protein binding","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural and functional characterization of an atypical activation domain in erythroid Kruppel-like factor (EKLF). <i> Mas C, Lussier-Price M, Soni S, Morse T, Arseneault G, Di Lello P, Lafrance-Vanasse J, Bieker JJ, Omichinski JG. </i> Proc Natl Acad Sci U S A, 2011","term_id":"GO:0005515","curator_id":"vnugnes","start":51,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"21670263","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-09-27T15:11:41.094Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01640r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"2L2I"}],"interaction_partner":[{"db":"UniProt","id":"P32776","operator":"and","partner_start":null,"partner_end":null}],"sequence_construct":"GSLHVKSEDQPGEEEDDERGADATWDLDLLLTNFSGPEPGGA","statement":[{"text":"EKLFTAD2 binds Tfb1PH in an elongated conformation devoid of any regular secondary structural elements (Fig. 3 A and B). β-strands β5–β7 and the H1 α-helix of Tfb1PH form an extensive interface with residues between Ala69 and Thr80 of EKLFTAD2 (Fig. 3 C and D), and this is consistent with chemical shift changes of 15N-EKLFTAD2 upon addition of Tfb1PH (Fig. S2).","type":"Results"}]},{"start":1,"end":40,"reference_id":"24139988","reference_source":"pmid","reference_html":"Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF. <i> Raiola L, Lussier-Price M, Gagnon D, Lafrance-Vanasse J, Mascle X, Arseneault G, Legault P, Archambault J, Omichinski JG. </i> Structure, 2013","date":"2023-09-27T15:22:36.565Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01640r003","statement":[{"text":"Figure 1 about the 2D 1H-15N HSQC spectra of residues 1–40 of hEKLF shows a poor dispersion of amide proton chemical shifts, indicating this region is disordered. ","type":"Curator statement"}]},{"start":1,"end":90,"reference_id":"24139988","reference_source":"pmid","reference_html":"Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF. <i> Raiola L, Lussier-Price M, Gagnon D, Lafrance-Vanasse J, Mascle X, Arseneault G, Legault P, Archambault J, Omichinski JG. </i> Structure, 2013","date":"2023-09-27T15:28:41.821Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01640r004","statement":[{"text":"Figure 1 about the 2D 1H-15N HSQC spectra of residues 1-90 of hEKLF shows a poor dispersion of amide proton chemical shifts, indicating this region is disordered. ","type":"Curator statement"}]},{"start":23,"end":36,"reference_id":"24139988","reference_source":"pmid","reference_html":"Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF. <i> Raiola L, Lussier-Price M, Gagnon D, Lafrance-Vanasse J, Mascle X, Arseneault G, Legault P, Archambault J, Omichinski JG. </i> Structure, 2013","date":"2023-09-27T15:25:23.511Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0043130","term_name":"ubiquitin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2MBH"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P62987","operator":null,"partner_start":1,"partner_end":76}],"region_id":"DP01640r005","statement":[{"text":"EKLFTAD1 is disordered in the complex with the exception of a 14-residue amphipathic α helix that forms between residues Thr23 and Ala36 upon binding UBI (Figure 3B). ","type":"Results"},{"text":"With the exception of the 14-residue α helix, EKLFTAD1 is disordered and this transition of a short region from a disordered to an ordered conformation is consistent with what has been observed for several other acidic TADs upon binding to other target proteins (Di Lello et al., 2006, Ferreon et al., 2009, Langlois et al., 2008, Wojciak et al., 2009).","type":"Results"}],"term_comment":"","term_def":"\"Binding to ubiquitin, a protein that when covalently bound to other cellular proteins marks them for proteolytic degradation.\" [GOC:ecd]","term_is_obsolete":false,"term_not_annotate":false},{"start":23,"end":36,"reference_id":"24139988","reference_source":"pmid","reference_html":"Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF. <i> Raiola L, Lussier-Price M, Gagnon D, Lafrance-Vanasse J, Mascle X, Arseneault G, Legault P, Archambault J, Omichinski JG. </i> Structure, 2013","date":"2023-09-27T15:25:43.360Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2MBH"}],"region_id":"DP01640r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62987"}],"statement":[{"text":"EKLFTAD1 is disordered in the complex with the exception of a 14-residue amphipathic α helix that forms between residues Thr23 and Ala36 upon binding UBI (Figure 3B). ","type":"Results"},{"text":"With the exception of the 14-residue α helix, EKLFTAD1 is disordered and this transition of a short region from a disordered to an ordered conformation is consistent with what has been observed for several other acidic TADs upon binding to other target proteins (Di Lello et al., 2006, Ferreon et al., 2009, Langlois et al., 2008, Wojciak et al., 2009).","type":"Results"}]},{"start":23,"end":36,"reference_id":"24139988","reference_source":"pmid","reference_html":"Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF. <i> Raiola L, Lussier-Price M, Gagnon D, Lafrance-Vanasse J, Mascle X, Arseneault G, Legault P, Archambault J, Omichinski JG. </i> Structure, 2013","date":"2023-09-27T15:26:48.381Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2MBH"}],"region_id":"DP01640r007","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62987"}],"statement":[{"text":"EKLFTAD1 is disordered in the complex with the exception of a 14-residue amphipathic α helix that forms between residues Thr23 and Ala36 upon binding UBI (Figure 3B). ","type":"Results"},{"text":"With the exception of the 14-residue α helix, EKLFTAD1 is disordered and this transition of a short region from a disordered to an ordered conformation is consistent with what has been observed for several other acidic TADs upon binding to other target proteins (Di Lello et al., 2006, Ferreon et al., 2009, Langlois et al., 2008, Wojciak et al., 2009).","type":"Results"}]},{"start":27,"end":31,"reference_id":"24139988","reference_source":"pmid","reference_html":"Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF. <i> Raiola L, Lussier-Price M, Gagnon D, Lafrance-Vanasse J, Mascle X, Arseneault G, Legault P, Archambault J, Omichinski JG. </i> Structure, 2013","date":"2023-09-27T16:03:28.898Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0043130","term_name":"ubiquitin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe27Ser","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu28Ser","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp31Ser","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q13351","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01640r008","statement":[{"text":"Three EKLFTAD1 point mutants (F27S, L28S, and W31S) were generated, and the binding of the variant proteins to UBI was tested by NMR chemical shift perturbation experiments. In each experiment, unlabeled UBI was incrementally added to the 15N-labeled EKLFTAD1 variants as described in the previous section. During these three titrations, we were not able to reach saturation or determine values for the dissociation constants. Furthermore, after addition of UBI to variant (F27S, L28S, and Trp31S) EKLFTAD1 proteins, the resulting 1H-15N HSQC spectrums were very similar to that of their free form (Figure S3). These results confirm that Phe27, Leu28, and Trp31 on the hydrophobic face of the EKLFTAD1 α helix are crucial for binding to UBI.","type":"Results"}],"term_comment":"","term_def":"\"Binding to ubiquitin, a protein that when covalently bound to other cellular proteins marks them for proteolytic degradation.\" [GOC:ecd]","term_is_obsolete":false,"term_not_annotate":false},{"start":27,"end":31,"reference_id":"24139988","reference_source":"pmid","reference_html":"Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF. <i> Raiola L, Lussier-Price M, Gagnon D, Lafrance-Vanasse J, Mascle X, Arseneault G, Legault P, Archambault J, Omichinski JG. </i> Structure, 2013","date":"2023-09-27T16:09:20.290Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006511","term_name":"ubiquitin-dependent protein catabolic process","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005648","ec_ontology":"ECO","ec_name":"luciferase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe27Ser","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu28Ser","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp31Ser","start":null,"end":null,"position":null}],"ec_go":"IEP","region_id":"DP01640r009","statement":[{"text":"s expected, the RLuc/FLuc ratio of each construct was found to increase linearly as a function of the five different concentrations of EKLF expression vector tested (Figure 5A). Linear regression analysis of this data was used to calculate a slope indicative of the stability of each EKLF constructs. Under these assay conditions, the levels of the EKLF-RLuc protein were slightly more than 2-fold lower than both the ΔTAD-EKLF-RLuc and the F27S/L28S/W31S-EKLF proteins (Figure 5B). In addition, the levels of the ΔTAD-EKLF-RLuc and the F27S/L28S/W31S-EKLF proteins were very similar. These results are in agreement with earlier studies showing that the PEST1 region within the minimal TAD of EKLF plays a significant role in ubiquitin-mediated degradation of EKLF (Quadrini and Bieker, 2006) and further establishes that the UBI-interacting domain in EKLF plays an important role in regulating its steady-state levels.","type":"Results"},{"text":"The Minimal TAD of EKLF Functions as a “Degron” in Cells","type":"Figure"}],"term_comment":"","term_def":"\"The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":27,"end":31,"reference_id":"24139988","reference_source":"pmid","reference_html":"Structural characterization of a noncovalent complex between ubiquitin and the transactivation domain of the erythroid-specific factor EKLF. <i> Raiola L, Lussier-Price M, Gagnon D, Lafrance-Vanasse J, Mascle X, Arseneault G, Legault P, Archambault J, Omichinski JG. </i> Structure, 2013","date":"2023-09-27T16:09:55.630Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031648","term_name":"protein destabilization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005648","ec_ontology":"ECO","ec_name":"luciferase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe27Ser","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu28Ser","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp31Ser","start":null,"end":null,"position":null}],"ec_go":"IEP","region_id":"DP01640r010","statement":[{"text":"s expected, the RLuc/FLuc ratio of each construct was found to increase linearly as a function of the five different concentrations of EKLF expression vector tested (Figure 5A). Linear regression analysis of this data was used to calculate a slope indicative of the stability of each EKLF constructs. Under these assay conditions, the levels of the EKLF-RLuc protein were slightly more than 2-fold lower than both the ΔTAD-EKLF-RLuc and the F27S/L28S/W31S-EKLF proteins (Figure 5B). In addition, the levels of the ΔTAD-EKLF-RLuc and the F27S/L28S/W31S-EKLF proteins were very similar. These results are in agreement with earlier studies showing that the PEST1 region within the minimal TAD of EKLF plays a significant role in ubiquitin-mediated degradation of EKLF (Quadrini and Bieker, 2006) and further establishes that the UBI-interacting domain in EKLF plays an important role in regulating its steady-state levels.","type":"Results"},{"text":"The Minimal TAD of EKLF Functions as a “Degron” in Cells","type":"Figure"}],"term_comment":"","term_def":"\"Any process that decreases the stability of a protein, making it more vulnerable to degradative processes or aggregation.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_Q13351","date":"2018-08-03T15:40:05.000Z","acc":"Q13351","name":"Krueppel-like factor 1","length":362,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012DED2","genes":[{"name":{"value":"KLF1"},"synonyms":[{"value":"EKLF"}]}],"alphafold_very_low_content":0.5580110497237569,"disorder_content":0.24861878453038674,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"},{"start":23,"end":36,"type":"T"},{"start":37,"end":90,"type":"D"}],"Structural state":[{"start":1,"end":90,"type":"D"}],"Molecular function":[{"start":23,"end":36,"type":"F"},{"start":51,"end":90,"type":"F"}],"Structural transition":[{"start":23,"end":36,"type":"T"}],"Biological process":[{"start":27,"end":31,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":18,"end":85},{"id":"PF00076","name":"RNA recognition motif","start":123,"end":184}],"gene3D":[{"start":1,"end":100,"id":"3.30.70.330","name":"3.30.70.330"},{"start":120,"end":196,"id":"3.30.70.330","name":"3.30.70.330"}]},"uniref50":"UniRef50_Q07955","sequence":"MSGGGVIRGPAGNNDCRIYVGNLPPDIRTKDIEDVFYKYGAIRDIDLKNRRGGPPFAFVEFEDPRDAEDAVYGRDGYDYDGYRLRVEFPRSGRGTGRGGGGGGGGGAPRGRYGPPSRRSENRVVVSGLPPSGSWQDLKDHMREAGDVCYADVYRDGTGVVEFVRKEDMTYAVRKLDNTKFRSHEGETAYIRVKVDGPRSPSYGRSRSRSRSRSRSRSRSNSRSRSYSPRRSRGSPRYSPRHSRSRSRT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q07955","disprot_id":"DP01641","ncbi_taxon_id":9606,"regions_counter":12,"creator":"eficho","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":215,"region_id":"DP01641r001","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Structural and functional analysis of RNA and TAP binding to SF2/ASF. <i> Tintaru AM, Hautbergue GM, Hounslow AM, Hung ML, Lian LY, Craven CJ, Wilson SA. </i> EMBO Rep, 2007","statement":[{"text":"Residues from 107–120 and from 196–215 are disordered in the structure calculations, and increased mobility of this section is confirmed by 15N relaxation measurements (supplementary Fig S2 online).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":196,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-25T13:45:49.534Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2O3D"}],"reference_id":"17668007","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:45:16.992Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":120,"region_id":"DP01641r002","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Structural and functional analysis of RNA and TAP binding to SF2/ASF. <i> Tintaru AM, Hautbergue GM, Hounslow AM, Hung ML, Lian LY, Craven CJ, Wilson SA. </i> EMBO Rep, 2007","statement":[{"text":"Residues from 107–120 and from 196–215 are disordered in the structure calculations, and increased mobility of this section is confirmed by 15N relaxation measurements (supplementary Fig S2 online).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":107,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-25T13:51:54.852Z","reference_source":"pmid","term_name":"disorder","reference_id":"17668007","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"2O3D"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:45:18.941Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":248,"region_id":"DP01641r003","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Phosphorylation drives a dynamic switch in serine/arginine-rich proteins. <i> Xiang S, Gapsys V, Kim HY, Bessonov S, Hsiao HH, Möhlmann S, Klaukien V, Ficner R, Becker S, Urlaub H, Lührmann R, de Groot B, Zweckstetter M. </i> Structure, 2013","statement":[{"text":"The two-dimensional 15N-1H heteronuclear single quantum coherence (HSQC) spectrum of SRSF1(RS) had a narrow chemical shift dispersion pointing to extensive structural disorder (Figure 1B).","type":"Results"},{"text":" In addition, large NMR line-widths (Figure 1B) indicate the presence of conformational exchange occurring on the micro-to-millisecond timescale. Taken together, the NMR data demonstrate that SRSF1(RS) is disordered and highly dynamic.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":196,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-25T13:32:27.966Z","reference_source":"pmid","term_name":"disorder","reference_id":"24183573","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:45:20.144Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":248,"term_name":"disorder to order","released":"2022_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Phosphorylation drives a dynamic switch in serine/arginine-rich proteins. <i> Xiang S, Gapsys V, Kim HY, Bessonov S, Hsiao HH, Möhlmann S, Klaukien V, Ficner R, Becker S, Urlaub H, Lührmann R, de Groot B, Zweckstetter M. </i> Structure, 2013","statement":[{"text":"Phosphorylation strongly changed the 15N-1H HSQC spectrum (Figure 1B).","type":"Results"},{"text":" Taken together, NMR spectroscopy revealed that phosphorylation of the RS dipeptides in SRSF1(RS) causes a switch from a disordered conformation to a partially rigidified structure.","type":"Results"},{"text":"NMR spectroscopy demonstrated a dramatic phosphorylation-induced change in the flexibility of the RS and RS1 domains of SRSF1 (Figures 1C, 2E, and 2F).","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"vnugnes","start":196,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24183573","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-25T13:43:17.349Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01641r004","ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:45:21.932Z"}},{"start":204,"end":219,"reference_id":"24183573","reference_source":"pmid","reference_html":"Phosphorylation drives a dynamic switch in serine/arginine-rich proteins. <i> Xiang S, Gapsys V, Kim HY, Bessonov S, Hsiao HH, Möhlmann S, Klaukien V, Ficner R, Becker S, Urlaub H, Lührmann R, de Groot B, Zweckstetter M. </i> Structure, 2013","date":"2022-08-25T13:38:26.467Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP01641r007","statement":[{"text":"Sequence-specific resonance assignment unambiguously identified phosphorylated serines in the RS repeat stretches comprising residues 204–219 and 242–247.","type":"Results"},{"text":"NMR resonance assignment revealed that serines from S207–S217 were phosphorylated to 100% (Figures 2B and 2D).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:45:23.648Z"}},{"start":242,"end":247,"reference_id":"24183573","reference_source":"pmid","reference_html":"Phosphorylation drives a dynamic switch in serine/arginine-rich proteins. <i> Xiang S, Gapsys V, Kim HY, Bessonov S, Hsiao HH, Möhlmann S, Klaukien V, Ficner R, Becker S, Urlaub H, Lührmann R, de Groot B, Zweckstetter M. </i> Structure, 2013","date":"2022-08-25T13:34:51.752Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP01641r008","statement":[{"text":"Sequence-specific resonance assignment unambiguously identified phosphorylated serines in the RS repeat stretches comprising residues 204–219 and 242–247.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:45:25.624Z"}}],"released":"2018_11","uniref100":"UniRef100_Q07955","date":"2018-08-03T15:56:49.000Z","acc":"Q07955","name":"Serine/arginine-rich splicing factor 1","length":248,"organism":"Homo sapiens","dataset":["Condensates-related proteins","RNA-binding proteins"],"UniParc":"UPI00001358BB","genes":[{"name":{"value":"SRSF1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:10780","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:10780"}}]},"synonyms":[{"value":"ASF"},{"value":"SF2"},{"value":"SF2P33"},{"value":"SFRS1"}],"orfNames":[{"value":"OK/SW-cl.3"}]}],"alphafold_very_low_content":0.35080645161290325,"disorder_content":0.2701612903225806,"disprot_consensus":{"full":[{"start":107,"end":120,"type":"D"},{"start":196,"end":248,"type":"T"}],"Structural state":[{"start":107,"end":120,"type":"D"},{"start":196,"end":248,"type":"D"}],"Structural transition":[{"start":196,"end":248,"type":"T"}],"Disorder function":[{"start":204,"end":219,"type":"F"},{"start":242,"end":247,"type":"F"}]}},{"acc":"P06492","sequence":"MDLLVDELFADMNADGASPPPPRPAGGPKNTPAAPPLYATGRLSQAQLMPSPPMPVPPAALFNRLLDDLGFSAGPALCTMLDTWNEDLFSALPTNADLYRECKFLSTLPSDVVEWGDAYVPERTQIDIRAHGDVAFPTLPATRDGLGLYYEALSRFFHAELRAREESYRTVLANFCSALYRYLRASVRQLHRQAHMRGRDRDLGEMLRATIADRYYRETARLARVLFLHLYLFLTREILWAAYAEQMMRPDLFDCLCCDLESWRQLAGLFQPFMFVNGALTVRGVPIEARRLRELNHIREHLNLPLVRSAATEEPGAPLTTPPTLHGNQARASGYFMVLIRAKLDSYSSFTTSPSEAVMREHAYSRARTKNNYGSTIEGLLDLPDDDAPEEAGLAAPRLSFLPAGHTRRLSTAPPTDVSLGDELHLDGEDVAMAHADALDDFDLDMLGDGDSPGPGFTPHDSAPYGALDMADFEFEQMFTDALGIDEYGG","creator":"bhajdu","dataset":["Viral proteins"],"date":"2018-08-03T16:14:01.000Z","disprot_id":"DP01642","features":{"pfam":[{"id":"PF02232","name":"Alpha trans-inducing protein (Alpha-TIF)","start":44,"end":386},{"id":"PF12149","name":"Herpes simplex virus virion protein 16 C terminal","start":461,"end":490}],"gene3D":[{"start":47,"end":363,"id":"1.10.1290.10","name":"Alpha trans-inducing (Alpha-TIF)","_id":"685af523b4ac24d5329d91e4"}]},"genes":[{"synonyms":[],"olnNames":[],"orfNames":[{"value":"UL48","evidences":[],"_id":"685af523b4ac24d5329d9285"}],"_id":"685af523b4ac24d5329d9284"}],"length":490,"name":"Tegument protein VP16","ncbi_taxon_id":10299,"organism":"Human herpesvirus 1 (strain 17)","regions_counter":32,"released":"2018_11","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Peploviricota","Herviviricetes","Herpesvirales","Herpesviridae","Alphaherpesvirinae","Simplexvirus"],"UniParc":"UPI000012624E","uniref100":"UniRef100_P06492","uniref50":"UniRef50_P06492","uniref90":"UniRef90_P06492","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":350,"end":394,"interaction_partner":[],"reference_html":"Molecular shapes of transcription factors TFIIB and VP16 in solution: implications for recognition. <i> Grossmann JG, Sharff AJ, O'Hare P, Luisi B. </i> Biochemistry, 2001","reference_id":"11371188","region_id":"DP01642r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Interestingly, these two regions correlate well with the space most likely taken up by N-terminal residues 1−48 which were not included in the conserved VP16 core structure, and an apparent disordered segment in the crystal (residues 350−394; the boundaries correspond to the termini of the orange helix and strand, respectively).","_id":"685af523b4ac24d5329d91e6"},{"type":"Figure","text":"In the crystal structure, the peptide is disordered between the orange helix and orange strand (residues 350−394).","_id":"685af523b4ac24d5329d91e7"},{"type":"Curator statement","text":"HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d91e8"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T08:57:12.057Z","_id":"685af523b4ac24d5329d91e9"},"version":3,"_id":"685af523b4ac24d5329d91e5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":403,"end":490,"interaction_partner":[],"reference_html":"Molecular shapes of transcription factors TFIIB and VP16 in solution: implications for recognition. <i> Grossmann JG, Sharff AJ, O'Hare P, Luisi B. </i> Biochemistry, 2001","reference_id":"11371188","region_id":"DP01642r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In contrast, the area that the remaining C-terminal “domain” (residues 403−490) is anticipated to occupy (corresponding to the bottom part of the shapes in Figure 5) only shows a small spatial extension to the globular core; i.e., it would not be possible to accommodate all C-terminal residues within the envelope. It seems likely that these residues are responsible for the intensity increase (and indicative of random chainlike behavior) observed in the very low-angle scattering regime.","_id":"685af523b4ac24d5329d91eb"},{"type":"Results","text":"Thus, we conclude that the C-terminal activation domain is disordered and particularly nonglobular in its native solution state and does not contribute to the globular core but extends into the solvent.","_id":"685af523b4ac24d5329d91ec"},{"type":"Curator statement","text":"HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d91ed"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T08:57:07.259Z","_id":"685af523b4ac24d5329d91ee"},"version":3,"_id":"685af523b4ac24d5329d91ea","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":412,"end":490,"interaction_partner":[],"reference_html":"Structural studies of the acidic transactivation domain of the Vmw65 protein of herpes simplex virus using 1H NMR. <i> O'Hare P, Williams G. </i> Biochemistry, 1992","reference_id":"1314658","region_id":"DP01642r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The absence of secondary and tertiary structure in aqueous solution at 35 °C, which is implied by Figure 2, is confirmed by inspection of two-dimensional NOE (NOESY) and rotating-frame NOE (ROESY) spectra of SAD and LAD. Intraresidue and CaH,-NHm sequential NOEs are observed, characteristic of an extended polypeptide chain; however, no sequential NH-NH,+1 NOEs, which are indicative of helical\nor nonhelical turns, are observed.","_id":"685af523b4ac24d5329d91f0"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T08:57:01.584Z","_id":"685af523b4ac24d5329d91f1"},"version":3,"_id":"685af523b4ac24d5329d91ef","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"6099","_id":"685af523b4ac24d5329d91f5"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":412,"end":490,"interaction_partner":[],"reference_html":"Structural properties of the promiscuous VP16 activation domain. <i> Jonker HR, Wechselberger RW, Boelens R, Folkers GE, Kaptein R. </i> Biochemistry, 2005","reference_id":"15654739","region_id":"DP01642r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The (1H,15N)-HSQC spectrum of VP16ad shows a small dispersion of intense signals in the proton dimension (<1 ppm), indicative for a lack of secondary structure. ","_id":"685af523b4ac24d5329d91f3"},{"type":"Curator statement","text":"HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d91f4"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T08:56:59.612Z","_id":"685af523b4ac24d5329d91f6"},"version":3,"_id":"685af523b4ac24d5329d91f2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2PHG","_id":"685af523b4ac24d5329d91fc"},{"db":"PDB","id":"2PHE","_id":"685af523b4ac24d5329d91fd"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":412,"end":490,"interaction_partner":[],"reference_html":"Structural properties of the promiscuous VP16 activation domain. <i> Jonker HR, Wechselberger RW, Boelens R, Folkers GE, Kaptein R. </i> Biochemistry, 2005","reference_id":"15654739","region_id":"DP01642r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In both activation subdomains negative 1HN, 15N, and 1Hα as well as positive 13Cα and 13C‘ resonance shifts are observed, indicative for α-helix formation.","_id":"685af523b4ac24d5329d91f8"},{"type":"Results","text":"From these analysis, we can clearly observe the formation of α-helices in the 443−447 and 469−483 region (Figure 4), especially since we have to take into account that resonances have only been mapped until a 1:10 complex.","_id":"685af523b4ac24d5329d91f9"},{"type":"Results","text":"Nevertheless, the NOE patterns clearly indicate that VP16ad exhibits an α−helical propensity throughout the sequence, except for the proline-rich 453−464 region. Many NOE contacts, indicative for an α-helix, are observed for residues 429−450 and 465−488 in both subdomains.","_id":"685af523b4ac24d5329d91fa"},{"type":"Curator statement","text":"HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d91fb"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T09:07:05.092Z","_id":"685af523b4ac24d5329d91fe"},"version":3,"_id":"685af523b4ac24d5329d91f7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2PHG","_id":"685af523b4ac24d5329d9202"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":412,"end":490,"interaction_partner":[{"db":"UniProt","id":"Q00403","partner_start":112,"partner_end":316,"_id":"685af523b4ac24d5329d9203"}],"reference_html":"Structural properties of the promiscuous VP16 activation domain. <i> Jonker HR, Wechselberger RW, Boelens R, Folkers GE, Kaptein R. </i> Biochemistry, 2005","reference_id":"15654739","region_id":"DP01642r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The titration experiments show progressive changes of the amide 1H and 15N chemical shifts, indicative for fast exchange between the bound and free states on the NMR time scale.","_id":"685af523b4ac24d5329d9200"},{"type":"Curator statement","text":"HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d9201"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T09:12:36.830Z","_id":"685af523b4ac24d5329d9204"},"version":4,"_id":"685af523b4ac24d5329d91ff","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":452,"end":490,"interaction_partner":[],"reference_html":"Induced alpha helix in the VP16 activation domain upon binding to a human TAF. <i> Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL. </i> Science, 1997","reference_id":"9271577","region_id":"DP01642r007","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"The limited dispersion of the backbone 15N and1HN chemical shifts in the HSQC spectrum of15N-labeled VP16C alone (Fig.1A) and the intermediate values (∼7 Hz) of 1HN-1HCα coupling constants (11) indicated that VP16C alone has negligible secondary structure (12).","_id":"685af523b4ac24d5329d9206"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was chemically synthesized. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d9207"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T08:55:46.366Z","_id":"685af523b4ac24d5329d9208"},"version":3,"_id":"685af523b4ac24d5329d9205","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":452,"end":490,"interaction_partner":[{"db":"UniProt","id":"Q16594","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d920c"}],"reference_html":"Induced alpha helix in the VP16 activation domain upon binding to a human TAF. <i> Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL. </i> Science, 1997","reference_id":"9271577","region_id":"DP01642r008","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"Titration of15N-labeled VP16C with unlabeled TAF1–140 resulted in progressive rather than bimodal changes of the backbone 15N and 1HN chemical shifts (Fig. 1A), thus indicating that VP16C interacts weakly with TAF1–140 and hence exchanges rapidly between the free and bound states on the NMR time scale (13).","_id":"685af523b4ac24d5329d920a"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was chemically synthesized. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d920b"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T09:11:57.075Z","_id":"685af523b4ac24d5329d920d"},"version":4,"_id":"685af523b4ac24d5329d9209","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":452,"end":490,"interaction_partner":[],"reference_html":"Induced alpha helix in the VP16 activation domain upon binding to a human TAF. <i> Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL. </i> Science, 1997","reference_id":"9271577","region_id":"DP01642r009","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"Significant chemical shift changes were observed only for the β protons of Asp472, Phe479, Leu483, and Asp486 (Fig.1C). These four residues lie within and adjacent to the region of VP16C that is suggested by backbone chemical shift perturbation to undergo an induced folding transition.","_id":"685af523b4ac24d5329d920f"},{"type":"Article","text":"Titration of15N-labeled VP16C with unlabeled TAF1–140 resulted in progressive rather than bimodal changes of the backbone 15N and 1HN chemical shifts (Fig. 1A), thus indicating that VP16C interacts weakly with TAF1–140 and hence exchanges rapidly between the free and bound states on the NMR time scale (13).","_id":"685af523b4ac24d5329d9210"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was chemically synthesized. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d9211"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T08:57:57.275Z","_id":"685af523b4ac24d5329d9212"},"version":3,"_id":"685af523b4ac24d5329d920e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":452,"end":490,"interaction_partner":[],"reference_html":"Induced alpha helix in the VP16 activation domain upon binding to a human TAF. <i> Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL. </i> Science, 1997","reference_id":"9271577","region_id":"DP01642r010","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"Titration of15N-labeled VP16C with unlabeled TAF1–140 resulted in progressive rather than bimodal changes of the backbone 15N and 1HN chemical shifts (Fig. 1A), thus indicating that VP16C interacts weakly with TAF1–140 and hence exchanges rapidly between the free and bound states on the NMR time scale (13).","_id":"685af523b4ac24d5329d9214"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was chemically synthesized. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d9215"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_id":"GO:0140677","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T09:23:13.633Z","_id":"685af523b4ac24d5329d9216"},"version":4,"_id":"685af523b4ac24d5329d9213","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":456,"end":490,"interaction_partner":[],"reference_html":"NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: structural similarities between VP16 and p53. <i> Langlois C, Mas C, Di Lello P, Jenkins LM, Legault P, Omichinski JG. </i> J Am Chem Soc, 2008","reference_id":"18630911","region_id":"DP01642r011","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"NMR structural studies demonstrate that VP16C is disordered in the free state, and forms a 9-residue α-helix involving residues Asp472 to Thr480 in complex with Tfb1.","_id":"685af523b4ac24d5329d9218"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d9219"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T08:55:32.445Z","_id":"685af523b4ac24d5329d921a"},"version":3,"_id":"685af523b4ac24d5329d9217","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2K2U","_id":"685af523b4ac24d5329d9224"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":456,"end":490,"interaction_partner":[{"db":"UniProt","id":"P32776","partner_start":1,"partner_end":115,"_id":"685af523b4ac24d5329d9225"}],"reference_html":"NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: structural similarities between VP16 and p53. <i> Langlois C, Mas C, Di Lello P, Jenkins LM, Legault P, Omichinski JG. </i> J Am Chem Soc, 2008","reference_id":"18630911","region_id":"DP01642r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Addition of VP16C (VP16456−490) to 15N-labeled Tfb11−115 produced changes in 1H and 15N chemical shifts for several signals of Tfb11−115 in the 2D 1H−15N HSQC spectra (Figure 1).","_id":"685af523b4ac24d5329d9221"},{"type":"Results","text":"The structure of the Tfb11−115/VP16C complex is well defined by the NMR data (Figure 2).","_id":"685af523b4ac24d5329d9222"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d9223"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T09:08:40.567Z","_id":"685af523b4ac24d5329d9226"},"version":4,"_id":"685af523b4ac24d5329d9220","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":469,"end":485,"interaction_partner":[],"reference_html":"Induced alpha helix in the VP16 activation domain upon binding to a human TAF. <i> Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL. </i> Science, 1997","reference_id":"9271577","region_id":"DP01642r014","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"As anticipated, free VP16 469–485 exhibited very few NOEs; only sequential NOEs between CαH and NH protons [d α N(i,i+1) NOEs] were clearly observed, indicative of an extended random-coil structure (19).","_id":"685af523b4ac24d5329d9228"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was chemically synthesized. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d9229"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T08:44:00.804Z","_id":"685af523b4ac24d5329d922a"},"version":3,"_id":"685af523b4ac24d5329d9227","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":469,"end":485,"interaction_partner":[],"reference_html":"Induced alpha helix in the VP16 activation domain upon binding to a human TAF. <i> Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL. </i> Science, 1997","reference_id":"9271577","region_id":"DP01642r015","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"In contrast, VP16469–485 in the presence of 0.1 mole equivalents of TAF1–140 showed numerous NOE cross-peaks, including a substantial number arising fromdNN(i,i+1),dαN(i,i), and dαβ(i,i+3) NOEs. The overall pattern of the NOE connectivities (Fig.3B) is characteristic of that observed for α-helical secondary structure, especially in the region from Asp472 to Leu483. Thus, residues 472 to 483 of VP16C, and perhaps even residues flanking this region, adopt an α-helical structure when bound to TAF1–140(20).","_id":"685af523b4ac24d5329d922c"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was chemically synthesized. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d922d"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T08:57:51.736Z","_id":"685af523b4ac24d5329d922e"},"version":3,"_id":"685af523b4ac24d5329d922b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":469,"end":485,"interaction_partner":[{"db":"UniProt","id":"Q16594","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9233"}],"reference_html":"Induced alpha helix in the VP16 activation domain upon binding to a human TAF. <i> Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL. </i> Science, 1997","reference_id":"9271577","region_id":"DP01642r016","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"To determine the structure of VP16 469 – 485 bound to TAF1–140, we performed transferred nuclear Overhauser effect (TRNOE) experiments.","_id":"685af523b4ac24d5329d9230"},{"type":"Article","text":"Thus, residues 472 to 483 of VP16C, and perhaps even residues flanking this region, adopt an α-helical structure when bound to TAF1–140(20).","_id":"685af523b4ac24d5329d9231"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was chemically synthesized. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d9232"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T09:08:27.508Z","_id":"685af523b4ac24d5329d9234"},"version":4,"_id":"685af523b4ac24d5329d922f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":469,"end":485,"interaction_partner":[],"reference_html":"Induced alpha helix in the VP16 activation domain upon binding to a human TAF. <i> Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL. </i> Science, 1997","reference_id":"9271577","region_id":"DP01642r017","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"Thus, residues 472 to 483 of VP16C, and perhaps even residues flanking this region, adopt an α-helical structure when bound to TAF1–140(20).","_id":"685af523b4ac24d5329d9236"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was chemically synthesized. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d9237"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_id":"GO:0140677","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T09:23:12.537Z","_id":"685af523b4ac24d5329d9238"},"version":1,"_id":"685af523b4ac24d5329d9235","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":475,"end":484,"interaction_partner":[],"reference_html":"Induced alpha helix in the VP16 activation domain upon binding to a human TAF. <i> Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL. </i> Science, 1997","reference_id":"9271577","region_id":"DP01642r018","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"Sequential assignment of the HSQC cross-peaks (14) established that the backbone-perturbed residues are located within a region at the COOH-terminal end of VP16C that encompasses residues 475 to 484 (Fig. 1B).","_id":"685af523b4ac24d5329d923a"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was chemically synthesized. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d923b"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_id":"GO:0140677","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T09:23:10.241Z","_id":"685af523b4ac24d5329d923c"},"version":1,"_id":"685af523b4ac24d5329d9239","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":475,"end":484,"interaction_partner":[],"reference_html":"Induced alpha helix in the VP16 activation domain upon binding to a human TAF. <i> Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL. </i> Science, 1997","reference_id":"9271577","region_id":"DP01642r019","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"Sequential assignment of the HSQC cross-peaks (14) established that the backbone-perturbed residues are located within a region at the COOH-terminal end of VP16C that encompasses residues 475 to 484 (Fig. 1B).","_id":"685af523b4ac24d5329d923e"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was chemically synthesized. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d923f"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T08:57:43.304Z","_id":"685af523b4ac24d5329d9240"},"version":1,"_id":"685af523b4ac24d5329d923d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":475,"end":484,"interaction_partner":[{"db":"UniProt","id":"Q16594","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9242"}],"reference_html":"Induced alpha helix in the VP16 activation domain upon binding to a human TAF. <i> Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL. </i> Science, 1997","reference_id":"9271577","region_id":"DP01642r020","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"Sequential assignment of the HSQC cross-peaks (14) established that the backbone-perturbed residues are located within a region at the COOH-terminal end of VP16C that encompasses residues 475 to 484 (Fig. 1B).","_id":"685af523b4ac24d5329d9243"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was chemically synthesized. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d9244"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T09:08:14.911Z","_id":"685af523b4ac24d5329d9245"},"version":1,"_id":"685af523b4ac24d5329d9241","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005647","ec_name":"isothermal titration calorimetry evidence used in manual assertion","ec_ontology":"ECO","start":412,"end":456,"interaction_partner":[{"db":"UniProt","id":"P32776","partner_start":1,"partner_end":115,"_id":"685af523b4ac24d5329d9247"}],"reference_html":"NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: structural similarities between VP16 and p53. <i> Langlois C, Mas C, Di Lello P, Jenkins LM, Legault P, Omichinski JG. </i> J Am Chem Soc, 2008","reference_id":"18630911","region_id":"DP01642r021","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"By this method, VP16C bound to Tfb1 with an apparent Kd of 360 ± 40 nM and VP16N bound to Tfb1 with an apparent Kd of 1000 ± 100 nM (Table 1). These results suggested that both subdomains of the VP16TAD were capable of interacting with Tfb1, and the Kd obtained for the Tfb1/VP16C complex is very similar to the Kd observed between Tfb1 and the p53TAD2 (390 nM).","_id":"685af523b4ac24d5329d9248"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d9249"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T09:07:58.536Z","_id":"685af523b4ac24d5329d924a"},"version":1,"_id":"685af523b4ac24d5329d9246","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005647","ec_name":"isothermal titration calorimetry evidence used in manual assertion","ec_ontology":"ECO","start":456,"end":490,"interaction_partner":[{"db":"UniProt","id":"P32776","partner_start":1,"partner_end":115,"_id":"685af523b4ac24d5329d924c"}],"reference_html":"NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: structural similarities between VP16 and p53. <i> Langlois C, Mas C, Di Lello P, Jenkins LM, Legault P, Omichinski JG. </i> J Am Chem Soc, 2008","reference_id":"18630911","region_id":"DP01642r022","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"By this method, VP16C bound to Tfb1 with an apparent Kd of 360 ± 40 nM and VP16N bound to Tfb1 with an apparent Kd of 1000 ± 100 nM (Table 1). These results suggested that both subdomains of the VP16TAD were capable of interacting with Tfb1, and the Kd obtained for the Tfb1/VP16C complex is very similar to the Kd observed between Tfb1 and the p53TAD2 (390 nM).","_id":"685af523b4ac24d5329d924d"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d924e"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T09:07:52.722Z","_id":"685af523b4ac24d5329d924f"},"version":1,"_id":"685af523b4ac24d5329d924b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-09T08:40:43.914Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005647","ec_name":"isothermal titration calorimetry evidence used in manual assertion","ec_ontology":"ECO","start":456,"end":490,"interaction_partner":[{"db":"UniProt","id":"P32776","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9253"}],"reference_html":"NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: structural similarities between VP16 and p53. <i> Langlois C, Mas C, Di Lello P, Jenkins LM, Legault P, Omichinski JG. </i> J Am Chem Soc, 2008","reference_id":"18630911","region_id":"DP01642r023","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"By this method, VP16C bound to Tfb1 with an apparent Kd of 360 ± 40 nM and VP16N bound to Tfb1 with an apparent Kd of 1000 ± 100 nM (Table 1). These results suggested that both subdomains of the VP16TAD were capable of interacting with Tfb1, and the Kd obtained for the Tfb1/VP16C complex is very similar to the Kd observed between Tfb1 and the p53TAD2 (390 nM).","_id":"685af523b4ac24d5329d9251"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d9252"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_id":"GO:0140677","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-08-12T17:24:42.439Z","_id":"685af523b4ac24d5329d9254"},"version":2,"_id":"685af523b4ac24d5329d9250","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2K2U","_id":"685af523b4ac24d5329d9259"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":456,"end":490,"interaction_partner":[],"reference_html":"NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: structural similarities between VP16 and p53. <i> Langlois C, Mas C, Di Lello P, Jenkins LM, Legault P, Omichinski JG. </i> J Am Chem Soc, 2008","reference_id":"18630911","region_id":"DP01642r024","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Addition of VP16C (VP16456−490) to 15N-labeled Tfb11−115 produced changes in 1H and 15N chemical shifts for several signals of Tfb11−115 in the 2D 1H−15N HSQC spectra (Figure 1).","_id":"685af523b4ac24d5329d9256"},{"type":"Results","text":"The structure of the Tfb11−115/VP16C complex is well defined by the NMR data (Figure 2).","_id":"685af523b4ac24d5329d9257"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d9258"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_id":"GO:0140677","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T09:19:19.438Z","_id":"685af523b4ac24d5329d925a"},"version":1,"_id":"685af523b4ac24d5329d9255","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-09T08:40:37.754Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005647","ec_name":"isothermal titration calorimetry evidence used in manual assertion","ec_ontology":"ECO","start":412,"end":456,"interaction_partner":[{"db":"UniProt","id":"P32776","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d925e"}],"reference_html":"NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: structural similarities between VP16 and p53. <i> Langlois C, Mas C, Di Lello P, Jenkins LM, Legault P, Omichinski JG. </i> J Am Chem Soc, 2008","reference_id":"18630911","region_id":"DP01642r025","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"By this method, VP16C bound to Tfb1 with an apparent Kd of 360 ± 40 nM and VP16N bound to Tfb1 with an apparent Kd of 1000 ± 100 nM (Table 1). These results suggested that both subdomains of the VP16TAD were capable of interacting with Tfb1, and the Kd obtained for the Tfb1/VP16C complex is very similar to the Kd observed between Tfb1 and the p53TAD2 (390 nM).","_id":"685af523b4ac24d5329d925c"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d925d"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_id":"GO:0140677","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-08-12T17:25:04.583Z","_id":"685af523b4ac24d5329d925f"},"version":2,"_id":"685af523b4ac24d5329d925b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2PHE","_id":"685af523b4ac24d5329d9261"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":412,"end":490,"interaction_partner":[{"db":"UniProt","id":"P53999","partner_start":1,"partner_end":126,"_id":"685af523b4ac24d5329d9262"}],"reference_html":"Structural properties of the promiscuous VP16 activation domain. <i> Jonker HR, Wechselberger RW, Boelens R, Folkers GE, Kaptein R. </i> Biochemistry, 2005","reference_id":"15654739","region_id":"DP01642r026","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"PC4ntd specifically stimulates the VP16−PC4 interaction for most residues in the 444−448 and 474−484 regions in VP16ad as we observe 2−3-fold increased chemical shift changes in these regions for the VP16ad−PC4 versus the VP16ad−PC4ctd interaction.","_id":"685af523b4ac24d5329d9263"},{"type":"Results","text":"For the titrations of 15N-labeled VP16 with PC4 (Figures 1 and 2), we observed broadening and disappearance of peaks due to the formation of a larger complex and exchange between the PC4-bound and free VP16ad.","_id":"685af523b4ac24d5329d9264"},{"type":"Curator statement","text":"HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d9265"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T09:07:43.736Z","_id":"685af523b4ac24d5329d9266"},"version":1,"_id":"685af523b4ac24d5329d9260","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005640","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","ec_ontology":"ECO","start":412,"end":490,"interaction_partner":[{"db":"UniProt","id":"P53999","partner_start":1,"partner_end":126,"_id":"685af523b4ac24d5329d9268"}],"reference_html":"Structural properties of the promiscuous VP16 activation domain. <i> Jonker HR, Wechselberger RW, Boelens R, Folkers GE, Kaptein R. </i> Biochemistry, 2005","reference_id":"15654739","region_id":"DP01642r027","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As shown in Figure 3A, wild-type PC4 can interact with full-length VP16 (Kd = 0.7 ± 0.2 μM), and both regions are mostly indispensable for the interaction. The VP16ad/n subdomain failed to interact with PC4, while the VP16ad/c region binds at least 20 times weaker (Kd = 15 ± 6 μM).","_id":"685af523b4ac24d5329d9269"},{"type":"Curator statement","text":"HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d926a"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T09:07:36.329Z","_id":"685af523b4ac24d5329d926b"},"version":1,"_id":"685af523b4ac24d5329d9267","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005640","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","ec_ontology":"ECO","start":454,"end":490,"interaction_partner":[{"db":"UniProt","id":"P53999","partner_start":1,"partner_end":126,"_id":"685af523b4ac24d5329d926d"}],"reference_html":"Structural properties of the promiscuous VP16 activation domain. <i> Jonker HR, Wechselberger RW, Boelens R, Folkers GE, Kaptein R. </i> Biochemistry, 2005","reference_id":"15654739","region_id":"DP01642r028","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As shown in Figure 3A, wild-type PC4 can interact with full-length VP16 (Kd = 0.7 ± 0.2 μM), and both regions are mostly indispensable for the interaction. The VP16ad/n subdomain failed to interact with PC4, while the VP16ad/c region binds at least 20 times weaker (Kd = 15 ± 6 μM).","_id":"685af523b4ac24d5329d926e"},{"type":"Curator statement","text":"HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d926f"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T09:07:26.838Z","_id":"685af523b4ac24d5329d9270"},"version":1,"_id":"685af523b4ac24d5329d926c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-09T08:40:23.609Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005640","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","ec_ontology":"ECO","start":412,"end":490,"interaction_partner":[{"db":"UniProt","id":"P53999","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9274"}],"reference_html":"Structural properties of the promiscuous VP16 activation domain. <i> Jonker HR, Wechselberger RW, Boelens R, Folkers GE, Kaptein R. </i> Biochemistry, 2005","reference_id":"15654739","region_id":"DP01642r029","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As shown in Figure 3A, wild-type PC4 can interact with full-length VP16 (Kd = 0.7 ± 0.2 μM), and both regions are mostly indispensable for the interaction. The VP16ad/n subdomain failed to interact with PC4, while the VP16ad/c region binds at least 20 times weaker (Kd = 15 ± 6 μM).","_id":"685af523b4ac24d5329d9272"},{"type":"Curator statement","text":"HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d9273"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_id":"GO:0140677","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-08-12T18:21:21.309Z","_id":"685af523b4ac24d5329d9275"},"version":2,"_id":"685af523b4ac24d5329d9271","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2PHG","_id":"685af523b4ac24d5329d9277"},{"db":"PDB","id":"2PHE","_id":"685af523b4ac24d5329d9278"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":412,"end":490,"interaction_partner":[],"reference_html":"Structural properties of the promiscuous VP16 activation domain. <i> Jonker HR, Wechselberger RW, Boelens R, Folkers GE, Kaptein R. </i> Biochemistry, 2005","reference_id":"15654739","region_id":"DP01642r030","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"NMR titration experiments (Figures 1 and 2) indicate that both VP16 activation subdomains are involved in the interaction with PC4 and TFIIBc. Deletion analysis shows that the VP16ad/n region fails to interact while VP16ad/c has a reduced binding affinity (>20 times compared to the full VP16ad) for PC4 (Figure 3A), indicating that both VP16 activation subdomains are required for high-affinity cooperative binding. ","_id":"685af523b4ac24d5329d9279"},{"type":"Curator statement","text":"HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d927a"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_id":"GO:0140677","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T09:19:01.508Z","_id":"685af523b4ac24d5329d927b"},"version":1,"_id":"685af523b4ac24d5329d9276","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"16VP","_id":"685af523b4ac24d5329d927d"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":350,"end":394,"interaction_partner":[],"reference_html":"Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16. <i> Liu Y, Gong W, Huang CC, Herr W, Cheng X. </i> Genes Dev, 1999","reference_id":"10398682","region_id":"DP01642r031","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Residues 350–394 (45 residues) and 403–412 (10 residues) are missing and apparently disordered in the crystal (see Fig. ​Fig.1A,1A, bottom). The model was refined to 2.1 Å resolution with a crystallographic R factor of 0.19 and Rfree value of 0.26 (Table ​2).","_id":"685af523b4ac24d5329d927e"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-22T10:31:24.708Z","_id":"685af523b4ac24d5329d927f"},"version":1,"_id":"685af523b4ac24d5329d927c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"16VP","_id":"685af523b4ac24d5329d9281"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":403,"end":412,"interaction_partner":[],"reference_html":"Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16. <i> Liu Y, Gong W, Huang CC, Herr W, Cheng X. </i> Genes Dev, 1999","reference_id":"10398682","region_id":"DP01642r032","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Residues 350–394 (45 residues) and 403–412 (10 residues) are missing and apparently disordered in the crystal (see Fig. ​Fig.1A,1A, bottom). The model was refined to 2.1 Å resolution with a crystallographic R factor of 0.19 and Rfree value of 0.26 (Table ​2).","_id":"685af523b4ac24d5329d9282"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-22T10:31:19.762Z","_id":"685af523b4ac24d5329d9283"},"version":1,"_id":"685af523b4ac24d5329d9280","reference_source":"pmid"}],"__v":0,"disorder_content":0.2714285714285714,"disprot_consensus":{"full":[{"start":350,"end":394,"type":"D"},{"start":403,"end":411,"type":"D"},{"start":412,"end":490,"type":"T"}],"Structural state":[{"start":350,"end":394,"type":"D"},{"start":403,"end":490,"type":"D"}],"Structural transition":[{"start":412,"end":490,"type":"T"}],"Molecular function":[{"start":412,"end":490,"type":"F"}]}},{"features":{"pfam":[{"id":"PF06825","name":"Heat shock factor binding protein 1","start":10,"end":60}],"gene3D":[{"start":6,"end":53,"id":"1.20.5.430","name":"1.20.5.430"}]},"uniref50":"UniRef50_O75506","sequence":"MAETDPKTVQDLTSVVQTLLQQMQDKFQTMSDQIIGRIDDMSSRIDDLEKNIADLMTQAGVEELESENKIPATQKS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O75506","disprot_id":"DP01643","ncbi_taxon_id":9606,"regions_counter":5,"creator":"cbassot","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":10,"region_id":"DP01643r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure-function analysis of the heat shock factor-binding protein reveals a protein composed solely of a highly conserved and dynamic coiled-coil trimerization domain. <i> Tai LJ, McFall SM, Huang K, Demeler B, Fox SG, Brubaker K, Radhakrishnan I, Morimoto RI. </i> J Biol Chem, 2002","statement":[{"text":"The spectrum is contoured at a high threshold to emphasize intense correlations from flexible regions. These correlations belong to residues at the NH2 and COOH termini.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"ahatos","start":1,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"11679589","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":76,"region_id":"DP01643r002","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Structure-function analysis of the heat shock factor-binding protein reveals a protein composed solely of a highly conserved and dynamic coiled-coil trimerization domain. <i> Tai LJ, McFall SM, Huang K, Demeler B, Fox SG, Brubaker K, Radhakrishnan I, Morimoto RI. </i> J Biol Chem, 2002","statement":[{"text":"V8 proteolysis produces two fragments of 6984.8 and 7227.4 daltons, whereas trypsin digestion yields a single proteolytic product of 7682.7 daltons. These fragments mapped the proteolytic cleavage sites immediately carboxyl-terminal to residues Glu-63 and Glu-65 (in the case of V8), and Lys-69 (in the case of trypsin) in the intact protein (Fig. 2).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"cbassot","start":60,"term_ontology":"IDPO","curator_name":"Claudio Bassot","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"11679589","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":76,"term_name":"protein binding","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","reference_html":"Structure-function analysis of the heat shock factor-binding protein reveals a protein composed solely of a highly conserved and dynamic coiled-coil trimerization domain. <i> Tai LJ, McFall SM, Huang K, Demeler B, Fox SG, Brubaker K, Radhakrishnan I, Morimoto RI. </i> J Biol Chem, 2002","statement":[{"text":"Collectively, our analyses suggest three alternative structural models for HSBP1 (Fig. 1 C): 1) a single continuous helix, 2) two noninteracting helices separated by a linker region (residues 35–40), and 3) two interacting helices arranged in an anti-parallel orientation. In each of the models, the helical regions or portions thereof can engage in intermolecular interactions, giving rise to a higher order oligomer.","type":"Results"}],"term_id":"GO:0005515","curator_id":"cbassot","start":60,"term_ontology":"GO","curator_name":"Claudio Bassot","reference_id":"11679589","version":3,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","region_id":"DP01643r003","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":76,"region_id":"DP01643r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure-function analysis of the heat shock factor-binding protein reveals a protein composed solely of a highly conserved and dynamic coiled-coil trimerization domain. <i> Tai LJ, McFall SM, Huang K, Demeler B, Fox SG, Brubaker K, Radhakrishnan I, Morimoto RI. </i> J Biol Chem, 2002","statement":[{"text":"Most of the intense resonances correspond to residues at the less conserved carboxyl terminus extending approximately from Gly-60 to Ser-76. The Hα secondary chemical shifts and the pattern of1H-1H NOEs (data not shown) further indicate the absence of regular secondary structure in this region. Thus, NMR analyses and limited proteolysis both establish that the carboxyl terminus of HSBP1 is unstructured and flexible.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"cbassot","start":60,"term_ontology":"IDPO","curator_name":"Claudio Bassot","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"11679589","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":76,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structure-function analysis of the heat shock factor-binding protein reveals a protein composed solely of a highly conserved and dynamic coiled-coil trimerization domain. <i> Tai LJ, McFall SM, Huang K, Demeler B, Fox SG, Brubaker K, Radhakrishnan I, Morimoto RI. </i> J Biol Chem, 2002","statement":[{"text":"Collectively, our analyses suggest three alternative structural models for HSBP1 (Fig. 1 C): 1) a single continuous helix, 2) two noninteracting helices separated by a linker region (residues 35–40), and 3) two interacting helices arranged in an anti-parallel orientation. In each of the models, the helical regions or portions thereof can engage in intermolecular interactions, giving rise to a higher order oligomer.","type":"Results"}],"term_id":"GO:0005515","curator_id":"cbassot","start":60,"term_ontology":"GO","curator_name":"Claudio Bassot","reference_id":"11679589","version":3,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01643r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_O75506","date":"2018-08-03T18:46:26.000Z","acc":"O75506","name":"Heat shock factor-binding protein 1","length":76,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000004B12F","genes":[{"name":{"value":"HSBP1"},"synonyms":[{"value":"HSF1BP"}]}],"alphafold_very_low_content":0,"disorder_content":0.35526315789473684,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"},{"start":60,"end":76,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":60,"end":76,"type":"D"}],"Molecular function":[{"start":60,"end":76,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00167","name":"Fibroblast growth factor","start":163,"end":282}],"gene3D":[{"start":154,"end":288,"id":"2.80.10.50","name":"2.80.10.50"}]},"uniref50":"UniRef50_P09038","sequence":"MVGVGGGDVEDVTPRPGGCQISGRGARGCNGIPGAAAWEAALPRRRPRRHPSVNPRSRAAGSPRTRGRRTEERPSGSRLGDRGRGRALPGGRLGGRGRGRAPERVGGRGRGRGTAAPRAAPAARGSRPGPAGTMAAGSITTLPALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P09038","disprot_id":"DP01644","ncbi_taxon_id":9606,"regions_counter":2,"creator":"cbassot","regions":[{"start":143,"end":160,"reference_id":"1769963","reference_source":"pmid","reference_html":"Crystal structure of basic fibroblast growth factor at 1.6 A resolution. <i> Ago H, Kitagawa Y, Fujishima A, Matsuura Y, Katsube Y. </i> J Biochem, 1991","date":"2023-08-09T16:21:42.901Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1BFG"}],"region_id":"DP01644r002","statement":[{"text":"the PDB structure shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"released":"2018_11","uniref100":"UniRef100_P09038","date":"2018-08-04T13:46:34.000Z","acc":"P09038","name":"Fibroblast growth factor 2","length":288,"organism":"Homo sapiens","dataset":["Extracellular matrix proteins"],"UniParc":"UPI000159688B","genes":[{"name":{"value":"FGF2"},"synonyms":[{"value":"FGFB"}]}],"alphafold_very_low_content":0.3472222222222222,"disorder_content":0.0625,"disprot_consensus":{"full":[{"start":143,"end":160,"type":"D"}],"Structural state":[{"start":143,"end":160,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00100","name":"ZP-C domain","start":483,"end":624},{"id":"PF23344","name":"ZP-N domain","start":365,"end":460},{"id":"PF23736","name":"Zona pellucida sperm-binding protein 2, Ig-like domain","start":138,"end":259},{"id":"PF23738","name":"Zona pellucida sperm-binding protein 2, Ig-like domain","start":47,"end":118},{"id":"PF23740","name":"Zona pellucida sperm-binding protein 2, Ig-like domain","start":263,"end":355}],"gene3D":[{"start":376,"end":468,"id":"2.60.40.3210","name":"Zona pellucida, ZP-N domain"},{"start":485,"end":656,"id":"2.60.40.4100","name":"Zona pellucida, ZP-C domain"}]},"uniref50":"UniRef50_P20239","sequence":"MARWQRKASVSSPCGRSIYRFLSLLFTLVTSVNSVSLPQSENPAFPGTLICDKDEVRIEFSSRFDMEKWNPSVVDTLGSEILNCTYALDLERFVLKFPYETCTIKVVGGYQVNIRVGDTTTDVRYKDDMYHFFCPAIQAETHEISEIVVCRRDLISFSFPQLFSRLADENQNVSEMGWIVKIGNGTRAHILPLKDAIVQGFNLLIDSQKVTLHVPANATGIVHYVQESSYLYTVQLELLFSTTGQKIVFSSHAICAPDLSVACNATHMTLTIPEFPGKLESVDFGQWSIPEDQWHANGIDKEATNGLRLNFRKSLLKTKPSEKCPFYQFYLSSLKLTFYFQGNMLSTVIDPECHCESPVSIDELCAQDGFMDFEVYSHQTKPALNLDTLLVGNSSCQPIFKVQSVGLARFHIPLNGCGTRQKFEGDKVIYENEIHALWENPPSNIVFRNSEFRMTVRCYYIRDSMLLNAHVKGHPSPEAFVKPGPLVLVLQTYPDQSYQRPYRKDEYPLVRYLRQPIYMEVKVLSRNDPNIKLVLDDCWATSSEDPASAPQWQIVMDGCEYELDNYRTTFHPAGSSAAHSGHYQRFDVKTFAFVSEARGLSSLIYFHCSALICNQVSLDSPLCSVTCPASLRSKREANKEDTMTVSLPGPILLLSDVSSSKGVDPSSSEITKDIIAKDIASKTLGAVAALVGSAVILGFICYLYKKRTIRFNH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P20239","disprot_id":"DP01645","ncbi_taxon_id":10090,"regions_counter":2,"creator":"cbassot","regions":[{"start":463,"end":484,"reference_id":"26811476","reference_source":"pmid","reference_html":"A structured interdomain linker directs self-polymerization of human uromodulin. <i> Bokhove M, Nishimura K, Brunati M, Han L, de Sanctis D, Rampoldi L, Jovine L. </i> Proc Natl Acad Sci U S A, 2016","date":"2022-09-05T12:54:16.684Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP01645r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30089","entry_name":"acetate"}],"statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"released":"2018_11","uniref100":"UniRef100_P20239","date":"2018-08-04T13:46:51.000Z","acc":"P20239","name":"Zona pellucida sperm-binding protein 2","length":713,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000027D50","genes":[{"name":{"value":"Zp2"},"synonyms":[{"value":"Zp-2"},{"value":"Zpa"}]}],"alphafold_very_low_content":0.18513323983169705,"disorder_content":0.030855539971949508,"disprot_consensus":{"full":[{"start":463,"end":484,"type":"D"}],"Structural state":[{"start":463,"end":484,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00102","name":"Protein-tyrosine phosphatase","start":120,"end":347}],"gene3D":[{"start":58,"end":360,"id":"3.90.190.10","name":"Protein tyrosine phosphatase superfamily"}]},"uniref50":"UniRef50_P35236","sequence":"MVQAHGGRSRAQPLTLSLGAAMTQPPPEKTPAKKHVRLQERRGSNVALMLDVRSLGAVEPICSVNTPREVTLHFLRTAGHPLTRWALQRQPPSPKQLEEEFLKIPSNFVSPEDLDIPGHASKDRYKTILPNPQSRVCLGRAQSQEDGDYINANYIRGYDGKEKVYIATQGPMPNTVSDFWEMVWQEEVSLIVMLTQLREGKEKCVHYWPTEEETYGPFQIRIQDMKECPEYTVRQLTIQYQEERRSVKHILFSAWPDHQTPESAGPLLRLVAEVEESPETAAHPGPIVVHCSAGIGRTGCFIATRIGCQQLKARGEVDILGIVCQLRLDRGGMIQTAEQYQFLHHTLALYAGQLPEEPSP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P35236","disprot_id":"DP01646","ncbi_taxon_id":9606,"regions_counter":3,"creator":"cbassot","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":52,"region_id":"DP01646r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Docking interactions induce exposure of activation loop in the MAP kinase ERK2. <i> Zhou T, Sun L, Humphreys J, Goldsmith EJ. </i> Structure, 2006","term_id":"IDPO:0000002","curator_id":"ahatos","start":37,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2GPH"}],"reference_id":"16765894","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":52,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Docking interactions induce exposure of activation loop in the MAP kinase ERK2. <i> Zhou T, Sun L, Humphreys J, Goldsmith EJ. </i> Structure, 2006","statement":[{"text":"a 1.9 A crystallographic analysis of inactive ERK2 bound to a \"D motif\" docking peptide (pepHePTP) derived from hematopoietic tyrosine phosphatase, a negative regulator of ERK2.","type":"Abstract"}],"term_id":"GO:0005515","curator_id":"ahatos","start":37,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"16765894","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"DIBS","id":"DI1010079"}],"region_id":"DP01646r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":52,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Docking interactions induce exposure of activation loop in the MAP kinase ERK2. <i> Zhou T, Sun L, Humphreys J, Goldsmith EJ. </i> Structure, 2006","term_id":"IDPO:0000011","curator_id":"ahatos","start":37,"term_ontology":"IDPO","curator_name":"András Hatos","reference_id":"16765894","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01646r003","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_P35236","date":"2018-08-04T13:47:30.000Z","acc":"P35236","name":"Tyrosine-protein phosphatase non-receptor type 7","length":360,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000015463D","genes":[{"name":{"value":"PTPN7"}}],"alphafold_very_low_content":0.1111111111111111,"disorder_content":0.044444444444444446,"disprot_consensus":{"full":[{"start":37,"end":52,"type":"T"}],"Structural state":[{"start":37,"end":52,"type":"D"}],"Molecular function":[{"start":37,"end":52,"type":"F"}],"Structural transition":[{"start":37,"end":52,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00104","name":"Ligand-binding domain of nuclear hormone receptor","start":321,"end":486},{"id":"PF00105","name":"Double treble clef zinc finger, C4 type","start":30,"end":98}],"gene3D":[{"start":255,"end":508,"id":"1.10.565.10","name":"Retinoid X Receptor"},{"start":21,"end":134,"id":"3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A"}]},"uniref50":"UniRef50_P51449","sequence":"MDRAPQRQHRASRELLAAKKTHTSQIEVIPCKICGDKSSGIHYGVITCEGCKGFFRRSQRCNAAYSCTRQQNCPIDRTSRNRCQHCRLQKCLALGMSRDAVKFGRMSKKQRDSLHAEVQKQLQQRQQQQQEPVVKTPPAGAQGADTLTYTLGLPDGQLPLGSSPDLPEASACPPGLLKASGSGPSYSNNLAKAGLNGASCHLEYSPERGKAEGRESFYSTGSQLTPDRCGLRFEEHRHPGLGELGQGPDSYGSPSFRSTPEAPYASLTEIEHLVQSVCKSYRETCQLRLEDLLRQRSNIFSREEVTGYQRKSMWEMWERCAHHLTEAIQYVVEFAKRLSGFMELCQNDQIVLLKAGAMEVVLVRMCRAYNADNRTVFFEGKYGGMELFRALGCSELISSIFDFSHSLSALHFSEDEIALYTALVLINAHRPGLQEKRKVEQLQYNLELAFHHHLCKTHRQSILAKLPPKGKLRSLCSQHVERLQIFQHLHPIVVQAAFPPLYKELFSTETESPVGLSK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P51449","disprot_id":"DP01647","ncbi_taxon_id":9606,"regions_counter":4,"creator":"cbassot","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":518,"region_id":"DP01647r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis of digoxin that antagonizes RORgamma t receptor activity and suppresses Th17 cell differentiation and interleukin (IL)-17 production. <i> Fujita-Sato S, Ito S, Isobe T, Ohyama T, Wakabayashi K, Morishita K, Ando O, Isono F. </i> J Biol Chem, 2011","statement":[{"text":"Whereas the electron densities are excellent quality from residue 265 to residue 479 or residue 481, residues from a C-terminal part of H11 to H12 could not be modeled because no clear electron density was observed for this region.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"cbassot","start":479,"term_ontology":"IDPO","curator_name":"Claudio Bassot","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3B0W"}],"reference_id":"21733845","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":518,"term_name":"order to disorder","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural basis of digoxin that antagonizes RORgamma t receptor activity and suppresses Th17 cell differentiation and interleukin (IL)-17 production. <i> Fujita-Sato S, Ito S, Isobe T, Ohyama T, Wakabayashi K, Morishita K, Ando O, Isono F. </i> J Biol Chem, 2011","term_id":"IDPO:0000014","curator_id":"cbassot","start":479,"term_ontology":"IDPO","curator_name":"Claudio Bassot","reference_id":"21733845","version":2,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01647r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":518,"region_id":"DP01647r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Modulators of the nuclear receptor retinoic acid receptor-related orphan receptor-γ (RORγ or RORc). <i> Fauber BP, Magnuson S. </i> J Med Chem, 2014","statement":[{"text":"For the co-crystallization of inverse agonists or antagonists acting via steric clash resulting in flexible/disordered\nhelix 12, we report a method using optimal constructs which have helix 12 deleted.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"cbassot","start":500,"term_ontology":"IDPO","curator_name":"Claudio Bassot","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5NU1"}],"reference_id":"24502334","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":518,"term_name":"order to disorder","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Modulators of the nuclear receptor retinoic acid receptor-related orphan receptor-γ (RORγ or RORc). <i> Fauber BP, Magnuson S. </i> J Med Chem, 2014","term_id":"IDPO:0000014","curator_id":"cbassot","start":500,"term_ontology":"IDPO","curator_name":"Claudio Bassot","reference_id":"24502334","version":2,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01647r004","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_P51449","date":"2018-08-04T13:47:42.000Z","acc":"P51449","name":"Nuclear receptor ROR-gamma","length":518,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000013454B","genes":[{"name":{"value":"RORC"},"synonyms":[{"value":"NR1F3"},{"value":"RORG"},{"value":"RZRG"}]}],"alphafold_very_low_content":0.27606177606177607,"disorder_content":0.07722007722007722,"disprot_consensus":{"full":[{"start":479,"end":518,"type":"T"}],"Structural state":[{"start":479,"end":518,"type":"D"}],"Structural transition":[{"start":479,"end":518,"type":"T"}]}},{"features":{"pfam":[{"id":"PF03165","name":"MH1 domain","start":31,"end":131},{"id":"PF03166","name":"MH2 domain","start":231,"end":401}],"gene3D":[{"start":1,"end":144,"id":"3.90.520.10","name":"SMAD MH1 domain"},{"start":223,"end":425,"id":"2.60.200.10","name":"2.60.200.10"}]},"uniref50":"UniRef50_P84022","sequence":"MSSILPFTPPIVKRLLGWKKGEQNGQEEKWCEKAVKSLVKKLKKTGQLDELEKAITTQNVNTKCITIPRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELRAMELCEFAFNMKKDEVCVNPYHYQRVETPVLPPVLVPRHTEIPAEFPPLDDYSHSIPENTNFPAGIEPQSNIPETPPPGYLSEDGETSDHQMNHSMDAGSPNLSPNPMSPAHNNLDLQPVTYCEPAFWCSISYYELNQRVGETFHASQPSMTVDGFTDPSNSERFCLGLLSNVNRNAAVELTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSIRCSSVS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P84022","disprot_id":"DP01648","ncbi_taxon_id":9606,"regions_counter":4,"creator":"cbassot","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":10,"region_id":"DP01648r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of a Smad MH1 domain bound to DNA: insights on DNA binding in TGF-beta signaling. <i> Shi Y, Wang YF, Jayaraman L, Yang H, Massagué J, Pavletich NP. </i> Cell, 1998","statement":[{"text":"The N-terminal nine residues, which are not conserved in Smads, and the C-terminal thirteen residues, which are rich in proline, are disordered in the crystals.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ahatos","start":1,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1MHD"}],"reference_id":"9741623","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-11T15:02:38.935Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":144,"region_id":"DP01648r002","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Features of a Smad3 MH1-DNA complex. Roles of water and zinc in DNA binding. <i> Chai J, Wu JW, Yan N, Massagué J, Pavletich NP, Shi Y. </i> J Biol Chem, 2003","statement":[{"text":"The final refined model contains two molecules of Smad3 MH1 (residues 7–132 and 9–132, respectively), a 15-bp DNA duplex, 47 well ordered water molecules, and two zinc atoms. Residues at the N and C termini have no electron density in the maps, and we presume that these regions are disordered in the crystals.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":133,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-12-11T19:22:24.312Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1OZJ"}],"reference_id":"12686552","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"The 16-bp DNA (SBE) was synthesized as described previously (14)."},{"type":"Curator statement","text":"dsDNA with sequence GTATGTCTAGACTGA "}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-15T09:26:43.221Z"}}],"released":"2018_11","uniref100":"UniRef100_P84022","date":"2018-08-04T13:47:54.000Z","acc":"P84022","name":"Mothers against decapentaplegic homolog 3","length":425,"organism":"Homo sapiens","dataset":["Cancer-related proteins","Condensates-related proteins"],"UniParc":"UPI0000023A91","genes":[{"name":{"value":"SMAD3"},"synonyms":[{"value":"MADH3"}]}],"alphafold_very_low_content":0.17411764705882352,"disorder_content":0.05176470588235294,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"},{"start":133,"end":144,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":133,"end":144,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00125","name":"Core histone H2A/H2B/H3/H4 domain","start":20,"end":101}],"gene3D":[{"start":1,"end":126,"id":"1.10.20.10","name":"Histone, subunit A"}]},"uniref50":"UniRef50_P0C1H4","sequence":"MPEPAKSAPAPKKGSKKAVTKTQKKGDKKRRKSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Phasianinae","Gallus"],"uniref90":"UniRef90_P0C1H4","disprot_id":"DP01649","ncbi_taxon_id":9031,"regions_counter":1,"creator":"cbassot","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":35,"region_id":"DP01649r001","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Prognostic and pathogenetic implications of immune complexes in human cancer. <i> Salinas FA, Wee KH. </i> Adv Immun Cancer Ther, 1986","statement":[{"text":"The density is missing for residues 1-35 and fact that the histone tails are disordered is well-established (eg.Potoyan et al 2010)","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"cbassot","start":1,"term_ontology":"IDPO","curator_name":"Claudio Bassot","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2XQL"}],"reference_id":"2962476","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P0C1H4","date":"2018-08-04T13:48:31.000Z","acc":"P0C1H4","name":"Histone H2B 5","length":126,"organism":"Gallus gallus","dataset":[],"UniParc":"UPI0000171242","genes":[{"name":{"value":"H2B-V"}}],"alphafold_very_low_content":0,"disorder_content":0.2777777777777778,"disprot_consensus":{"full":[{"start":1,"end":35,"type":"D"}],"Structural state":[{"start":1,"end":35,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00542","name":"Ribosomal protein L7/L12 C-terminal domain","start":55,"end":121},{"id":"PF16320","name":"Ribosomal protein L7/L12 dimerisation domain","start":4,"end":50}],"gene3D":[{"start":51,"end":121,"id":"3.30.1390.10","name":"3.30.1390.10"},{"start":2,"end":50,"id":"1.20.5.710","name":"Single helix bin"}]},"uniref50":"UniRef50_Q8UE07","sequence":"MSITKDQIIEAVAAMSVMDVVELISAMEEKFGVSAAAAVAVAAGPVEAAEEKTEFDVILKAAGANKVAVIKAVRGATGLGLKEAKDLVESAPAALKEGVSKDDAEALKKALEEAGAEVEVK","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_Q6DAN1","disprot_id":"DP01650","ncbi_taxon_id":83333,"regions_counter":2,"creator":"cbassot","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":43,"region_id":"DP01650r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"From structure and dynamics of protein L7/L12 to molecular switching in ribosome. <i> Bocharov EV, Sobol AG, Pavlov KV, Korzhnev DM, Jaravine VA, Gudkov AT, Arseniev AS. </i> J Biol Chem, 2004","statement":[{"text":"There is an indirect evidence of the existence of transitory helical structures at least in the first part (residues 33-43) of the hinge region.","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"cbassot","start":33,"term_ontology":"IDPO","curator_name":"Claudio Bassot","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1RQU"}],"reference_id":"14960595","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":43,"term_name":"flexible linker","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"From structure and dynamics of protein L7/L12 to molecular switching in ribosome. <i> Bocharov EV, Sobol AG, Pavlov KV, Korzhnev DM, Jaravine VA, Gudkov AT, Arseniev AS. </i> J Biol Chem, 2004","term_id":"IDPO:0000033","curator_id":"cbassot","start":33,"term_ontology":"IDPO","curator_name":"Claudio Bassot","reference_id":"14960595","version":3,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01650r002","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_A7ZUK0","date":"2018-08-04T13:48:41.000Z","acc":"P0A7K2","name":"50S ribosomal protein L7/L12","length":121,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI00001341A6","genes":[{"name":{"value":"rplL","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00368","url":"https://hamap.expasy.org/unirule/MF_00368"}}]},"olnNames":[{"value":"b3986"},{"value":"JW3949"}]}],"alphafold_very_low_content":0.09917355371900827,"disorder_content":0.09090909090909091,"disprot_consensus":{"full":[{"start":33,"end":43,"type":"D"}],"Structural state":[{"start":33,"end":43,"type":"D"}],"Disorder function":[{"start":33,"end":43,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00240","name":"Ubiquitin family","start":3,"end":75},{"id":"PF00628","name":"PHD-finger","start":318,"end":363},{"id":"PF02182","name":"SAD/SRA domain","start":417,"end":585},{"id":"PF12148","name":"Tandem tudor domain within UHRF1","start":133,"end":284}],"gene3D":[{"start":671,"end":793,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":399,"end":609,"id":"2.30.280.10","name":"SRA-YDG"},{"start":210,"end":367,"id":"2.30.30.1150","name":"2.30.30.1150"},{"start":125,"end":209,"id":"2.30.30.140","name":"2.30.30.140"},{"start":1,"end":76,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"}]},"uniref50":"UniRef50_Q96T88","sequence":"MWIQVRTMDGRQTHTVDSLSRLTKVEELRRKIQELFHVEPGLQRLFYRGKQMEDGHTLFDYEVRLNDTIQLLVRQSLVLPHSTKERDSELSDTDSGCCLGQSESDKSSTHGEAAAETDSRPADEDMWDETELGLYKVNEYVDARDTNMGAWFEAQVVRVTRKAPSRDEPCSSTSRPALEEDVIYHVKYDDYPENGVVQMNSRDVRARARTIIKWQDLEVGQVVMLNYNPDNPKERGFWYDAEISRKRETRTARELYANVVLGDDSLNDCRIIFVDEVFKIERPGEGSPMVDNPMRRKSGPSCKHCKDDVNRLCRVCACHLCGGRQDPDKQLMCDECDMAFHIYCLDPPLSSVPSEDEWYCPECRNDASEVVLAGERLRESKKKAKMASATSSSQRDWGKGMACVGRTKECTIVPSNHYGPIPGIPVGTMWRFRVQVSESGVHRPHVAGIHGRSNDGAYSLVLAGGYEDDVDHGNFFTYTGSGGRDLSGNKRTAEQSCDQKLTNTNRALALNCFAPINDQEGAEAKDWRSGKPVRVVRNVKGGKNSKYAPAEGNRYDGIYKVVKYWPEKGKSGFLVWRYLLRRDDDEPGPWTKEGKDRIKKLGLTMQYPEGYLEALANREREKENSKREEEEQQEGGFASPRTGKGKWKRKSAGGGPSRAGSPRRTSKKTKVEPYSLTAQQSSLIREDKSNAKLWNEVLASLKDRPASGSPFQLFLSKVEETFQCICCQELVFRPITTVCQHNVCKDCLDRSFRAQVFSCPACRYDLGRSYAMQVNQPLQTVLNQLFPGYGNGR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q96T88","disprot_id":"DP01651","ncbi_taxon_id":9606,"regions_counter":7,"creator":"cbassot","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":181,"region_id":"DP01651r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Recognition of multivalent histone states associated with heterochromatin by UHRF1 protein. <i> Nady N, Lemak A, Walker JR, Avvakumov GV, Kareta MS, Achour M, Xue S, Duan S, Allali-Hassani A, Zuo X, Wang YX, Bronner C, Chédin F, Arrowsmith CH, Dhe-Paganon S. </i> J Biol Chem, 2011","statement":[{"text":"the lowercase sequences are flexible regions in the liganded x-ray structure","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"cbassot","start":165,"term_ontology":"IDPO","curator_name":"Claudio Bassot","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2L3R"}],"reference_id":"21489993","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":301,"region_id":"DP01651r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Recognition of modification status on a histone H3 tail by linked histone reader modules of the epigenetic regulator UHRF1. <i> Arita K, Isogai S, Oda T, Unoki M, Sugita K, Sekiyama N, Kuwata K, Hamamoto R, Tochio H, Sato M, Ariyoshi M, Shirakawa M. </i> Proc Natl Acad Sci U S A, 2012","term_id":"IDPO:0000002","curator_id":"cbassot","start":286,"term_ontology":"IDPO","curator_name":"Claudio Bassot","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2L3R"}],"reference_id":"22837395","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":301,"term_name":"phosphorylation display site","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Recognition of modification status on a histone H3 tail by linked histone reader modules of the epigenetic regulator UHRF1. <i> Arita K, Isogai S, Oda T, Unoki M, Sugita K, Sekiyama N, Kuwata K, Hamamoto R, Tochio H, Sato M, Ariyoshi M, Shirakawa M. </i> Proc Natl Acad Sci U S A, 2012","statement":[{"text":"Our data also suggest that phosphorylation of a linker residue can modulate the relative position of the reader modules, thereby altering the histone H3–binding mode.","type":"Abstract"}],"term_id":"IDPO:0000045","curator_id":"cbassot","start":286,"term_ontology":"IDPO","curator_name":"Claudio Bassot","reference_id":"22837395","version":2,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01651r003","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":501,"region_id":"DP01651r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for recognition of hemi-methylated DNA by the SRA domain of human UHRF1. <i> Avvakumov GV, Walker JR, Xue S, Li Y, Duan S, Bronner C, Arrowsmith CH, Dhe-Paganon S. </i> Nature, 2008","term_id":"IDPO:0000002","curator_id":"cbassot","start":490,"term_ontology":"IDPO","curator_name":"Claudio Bassot","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3BI7"}],"reference_id":"18772889","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":501,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural basis for recognition of hemi-methylated DNA by the SRA domain of human UHRF1. <i> Avvakumov GV, Walker JR, Xue S, Li Y, Duan S, Bronner C, Arrowsmith CH, Dhe-Paganon S. </i> Nature, 2008","statement":[{"text":"the resulting hole in the DNA is partially filled by the NKR finger","type":"Figure"}],"term_id":"GO:0003676","curator_id":"cbassot","start":490,"term_ontology":"GO","curator_name":"Claudio Bassot","reference_id":"18772889","version":3,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01651r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":678,"region_id":"DP01651r006","released":"2022_03","ec_id":"ECO:0006220","reference_html":"An Allosteric Interaction Links USP7 to Deubiquitination and Chromatin Targeting of UHRF1. <i> Zhang ZM, Rothbart SB, Allison DF, Cai Q, Harrison JS, Li L, Wang Y, Strahl BD, Wang GG, Song J. </i> Cell Rep, 2015","term_id":"IDPO:0000002","curator_id":"cbassot","start":646,"term_ontology":"IDPO","curator_name":"Claudio Bassot","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5C6D"}],"reference_id":"26299963","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":678,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"An Allosteric Interaction Links USP7 to Deubiquitination and Chromatin Targeting of UHRF1. <i> Zhang ZM, Rothbart SB, Allison DF, Cai Q, Harrison JS, Li L, Wang Y, Strahl BD, Wang GG, Song J. </i> Cell Rep, 2015","statement":[{"text":"An Allosteric Interaction Links USP7 to Deubiquitination and Chromatin Targeting of UHRF1.","type":"Title"}],"term_id":"GO:0005515","curator_id":"cbassot","start":646,"term_ontology":"GO","curator_name":"Claudio Bassot","reference_id":"26299963","version":3,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01651r007","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q96T88","date":"2018-08-04T13:48:51.000Z","acc":"Q96T88","name":"E3 ubiquitin-protein ligase UHRF1","length":793,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000006D0AD","genes":[{"name":{"value":"UHRF1"},"synonyms":[{"value":"ICBP90"},{"value":"NP95"},{"value":"RNF106"}]}],"alphafold_very_low_content":0.12610340479192939,"disorder_content":0.09836065573770492,"disprot_consensus":{"full":[{"start":165,"end":181,"type":"D"},{"start":286,"end":301,"type":"D"},{"start":490,"end":501,"type":"D"},{"start":646,"end":678,"type":"D"}],"Structural state":[{"start":165,"end":181,"type":"D"},{"start":286,"end":301,"type":"D"},{"start":490,"end":501,"type":"D"},{"start":646,"end":678,"type":"D"}],"Disorder function":[{"start":286,"end":301,"type":"F"}],"Molecular function":[{"start":490,"end":501,"type":"F"},{"start":646,"end":678,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05207","name":"CSL zinc finger","start":5,"end":59}],"gene3D":[{"start":1,"end":82,"id":"3.10.660.10","name":"DPH Zinc finger"}]},"uniref50":"UniRef50_P31386","sequence":"MSTYDEIEIEDMTFEPENQMFTYPCPCGDRFQIYLDDMFEGEKVAVCPSCSLMIDVVFDKEDLAEYYEEAGIHPPEPIAAAA","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P31386","disprot_id":"DP01653","ncbi_taxon_id":559292,"regions_counter":1,"creator":"cbassot","regions":[{"region_id":"DP01653r001","ec_ontology":"ECO","end":82,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":70,"version":3,"statement":[{"text":"Unlike the well-structured region (residues 5−70), the N- and C-terminal regions (residues 1−4 and 71−83) are disordered.","type":"Results"}],"term_name":"disorder","reference_html":"Solution structure of Kti11p from Saccharomyces cerevisiae reveals a novel zinc-binding module. <i> Sun J, Zhang J, Wu F, Xu C, Li S, Zhao W, Wu Z, Wu J, Zhou CZ, Shi Y. </i> Biochemistry, 2005","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15952786","date":"2024-02-07T15:37:17.802Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1YOP"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"27365","entry_name":"zinc ion"}]}],"released":"2018_11","uniref100":"UniRef100_P31386","date":"2018-08-04T13:49:21.000Z","acc":"Q3E840","name":"Diphthamide biosynthesis protein 3","length":82,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000015489E","genes":[{"name":{"value":"KTI11","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12940988","url":"http://www.ncbi.nlm.nih.gov/pubmed/12940988","alternativeUrl":"https://europepmc.org/abstract/MED/12940988"}},{"code":"ECO:0000312","source":{"name":"SGD","id":"S000007587","url":"https://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000007587"}}]},"synonyms":[{"value":"DPH3"}],"olnNames":[{"value":"YBL071W-A"}]}],"alphafold_very_low_content":0.024390243902439025,"disorder_content":0.15853658536585366,"disprot_consensus":{"full":[{"start":70,"end":82,"type":"D"}],"Structural state":[{"start":70,"end":82,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00573","name":"Ribosomal protein L4/L1 family","start":23,"end":262},{"id":"PF14374","name":"60S ribosomal protein L4 C-terminal domain","start":275,"end":348}],"gene3D":[{"start":2,"end":304,"id":"3.40.1370.10","name":"3.40.1370.10"}]},"uniref50":"UniRef50_P36578","sequence":"MACARPLISVYSEKGESSGKNVTLPAVFKAPIRPDIVNFVHTNLRKNNRQPYAVSELAGHQTSAESWGTGRAVARIPRVRGGGTHRSGQGAFGNMCRGGRMFAPTKTWRRWHRRVNTTQKRYAICSALAASALPALVMSKGHRIEEVPELPLVVEDKVEGYKKTKEAVLLLKKLKAWNDIKKVYASQRMRAGKGKMRNRRRIQRRGPCIIYNEDNGIIKAFRNIPGITLLNVSKLNILKLAPGGHVGRFCIWTESAFRKLDELYGTWRKAASLKSNYNLPMHKMINTDLSRILKSPEIQRALRAPRKKIHRRVLKKNPLKNLRIMLKLNPYAKTMRRNTILRQARNHKLRVDKAAAAAAALQAKSDEKAAVAGKKPVVGKKGKKAAVGVKKQKKPLVGKKAAATKKPAPEKKPAEKKPTTEEKKPAA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P36578","disprot_id":"DP01654","ncbi_taxon_id":9606,"regions_counter":4,"creator":"cbassot","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":63,"region_id":"DP01654r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure-function insights reveal the human ribosome as a cancer target for antibiotics. <i> Myasnikov AG, Kundhavai Natchiar S, Nebout M, Hazemann I, Imbert V, Khatter H, Peyron JF, Klaholz BP. </i> Nat Commun, 2016","statement":[{"text":"From PDB structure","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"cbassot","start":46,"term_ontology":"IDPO","curator_name":"Claudio Bassot","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5LKS"}],"reference_id":"27665925","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":114,"region_id":"DP01654r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure-function insights reveal the human ribosome as a cancer target for antibiotics. <i> Myasnikov AG, Kundhavai Natchiar S, Nebout M, Hazemann I, Imbert V, Khatter H, Peyron JF, Klaholz BP. </i> Nat Commun, 2016","statement":[{"text":"From PDB structure","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"cbassot","start":80,"term_ontology":"IDPO","curator_name":"Claudio Bassot","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5LKS"}],"reference_id":"27665925","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":320,"region_id":"DP01654r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure-function insights reveal the human ribosome as a cancer target for antibiotics. <i> Myasnikov AG, Kundhavai Natchiar S, Nebout M, Hazemann I, Imbert V, Khatter H, Peyron JF, Klaholz BP. </i> Nat Commun, 2016","statement":[{"text":"From PDB structure","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"cbassot","start":301,"term_ontology":"IDPO","curator_name":"Claudio Bassot","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5LKS"}],"reference_id":"27665925","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":427,"region_id":"DP01654r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure-function insights reveal the human ribosome as a cancer target for antibiotics. <i> Myasnikov AG, Kundhavai Natchiar S, Nebout M, Hazemann I, Imbert V, Khatter H, Peyron JF, Klaholz BP. </i> Nat Commun, 2016","statement":[{"text":"From PDB structure","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"cbassot","start":369,"term_ontology":"IDPO","curator_name":"Claudio Bassot","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5LKS"}],"reference_id":"27665925","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P36578","date":"2018-08-04T13:49:37.000Z","acc":"P36578","name":"60S ribosomal protein L4","length":427,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000016AFC6","genes":[{"name":{"value":"RPL4"},"synonyms":[{"value":"RPL1"}]}],"alphafold_very_low_content":0.13817330210772832,"disorder_content":0.3091334894613583,"disprot_consensus":{"full":[{"start":46,"end":63,"type":"D"},{"start":80,"end":114,"type":"D"},{"start":301,"end":320,"type":"D"},{"start":369,"end":427,"type":"D"}],"Structural state":[{"start":46,"end":63,"type":"D"},{"start":80,"end":114,"type":"D"},{"start":301,"end":320,"type":"D"},{"start":369,"end":427,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00928","name":"Adaptor complexes medium subunit family","start":266,"end":501},{"id":"PF01217","name":"Clathrin adaptor complex small chain","start":9,"end":130}],"gene3D":[{"start":273,"end":489,"id":"2.60.40.1170","name":"Mu homology domain, subdomain B"},{"start":374,"end":473,"id":"2.60.40.1170","name":"Mu homology domain, subdomain B"},{"start":3,"end":155,"id":"3.30.450.60","name":"3.30.450.60"}]},"uniref50":"UniRef50_P48444","sequence":"MVLLAAAVCTKAGKAIVSRQFVEMTRTRIEGLLAAFPKLMNTGKQHTFVETESVRYVYQPMEKLYMVLITTKNSNILEDLETLRLFSRVIPEYCRALEENEISEHCFDLIFAFDEIVALGYRENVNLAQIRTFTEMDSHEEKVFRAVRETQEREAKAEMRRKAKELQQARRDAERQGKKAPGFGGFGSSAVSGGSTAAMITETIIETDKPKVAPAPARPSGPSKALKLGAKGKEVDNFVDKLKSEGETIMSSNMGKRTSEATKVHAPPINMESVHMKIEEKITLTCGRDGGLQNMELHGMIMLRISDDKFGRIRLHVENEDKKGVQLQTHPNVDKKLFTAESLIGLKNPEKSFPVNSDVGVLKWRLQTTEESFIPLTINCWPSESGNGCDVNIEYELQEDNLELNDVVITIPLPSGVGAPVIGEIDGEYRHDSRRNTLEWCLPVIDAKNKSGSLEFSIPGQPNDFFPVQVSFISKKNYCNIQVTKVTQVDGNSPVRFSTETTFLVDKYEIL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q5XJY5","disprot_id":"DP01657","ncbi_taxon_id":10090,"regions_counter":2,"creator":"cbassot","regions":[{"region_id":"DP01657r001","ec_ontology":"ECO","end":232,"ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","start":166,"version":3,"statement":[{"text":"Each of the large adaptor subunits β- and γ-COP contains an α-solenoid ‘trunk’ domain, connected by an unstructured linker region to a small appendage domain.","type":"Introduction"},{"text":"Note, that the C-terminal domain of α-COP, ε-COP, and the δ-COP MHD, are not visualized in the leaf structure, since they compose the inter-triad linkages.","type":"Figure"}],"term_name":"disorder","reference_html":"9Å structure of the COPI coat reveals that the Arf1 GTPase occupies two contrasting molecular environments. <i> Dodonova SO, Aderhold P, Kopp J, Ganeva I, Röhling S, Hagen WJH, Sinning I, Wieland F, Briggs JAG. </i> Elife, 2017","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"28621666","date":"2024-02-07T16:09:51.942Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5NZU"},{"db":"PDB","id":"5NZR"},{"db":"PDB","id":"5NZV"},{"db":"PDB","id":"5NZT"},{"db":"PDB","id":"5NZS"},{"db":"EMDB","id":"EMD-3724"},{"db":"EMDB","id":"EMD-3723"},{"db":"EMDB","id":"EMD-3722"},{"db":"EMDB","id":"EMD-3721"},{"db":"EMDB","id":"EMD-3720"}],"term_namespace":"Structural state","ec_id":"ECO:0006224","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"IDA","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":"Q3MID3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61924"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9QZE5"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P11076"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O55029"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9JIF7"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8CIE6"}]},{"start":245,"end":261,"reference_id":"28621666","reference_source":"pmid","reference_html":"9Å structure of the COPI coat reveals that the Arf1 GTPase occupies two contrasting molecular environments. <i> Dodonova SO, Aderhold P, Kopp J, Ganeva I, Röhling S, Hagen WJH, Sinning I, Wieland F, Briggs JAG. </i> Elife, 2017","date":"2024-02-07T16:09:59.023Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"5NZU"},{"db":"PDB","id":"5NZV"},{"db":"EMDB","id":"EMD-3724"},{"db":"EMDB","id":"EMD-3723"}],"region_id":"DP01657r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61924"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9QZE5"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P11076"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":"O55029"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9JIF7"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O89079"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8CIE6"}],"statement":[{"text":"The region lack electron density in the COPI coat linkage II and IV. These structures allowed the correct visualization of the δ-COP MHD and definition of the IDR boundaries, between the c’ α-helice and the MHD.","type":"Curator statement"}]}],"released":"2018_11","uniref100":"UniRef100_Q5XJY5","date":"2018-08-04T13:50:24.000Z","acc":"Q5XJY5","name":"Coatomer subunit delta","length":511,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000443F50","genes":[{"name":{"value":"Arcn1"},"synonyms":[{"value":"Copd"}]}],"alphafold_very_low_content":0.1487279843444227,"disorder_content":0.1643835616438356,"disprot_consensus":{"full":[{"start":166,"end":232,"type":"D"},{"start":245,"end":261,"type":"D"}],"Structural state":[{"start":166,"end":232,"type":"D"},{"start":245,"end":261,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02731","name":"SKIP/SNW domain","start":183,"end":339}]},"uniref50":"UniRef50_Q09882","sequence":"MALLSEELSSILPNPDFDDEEEDYVERETSHADERQIGVKFHIPPYGQRKGWFPSSPEDFGDGGAFPEIHVAQYPLDMGRKRSAKSAGNTLALQVTSSGAVDYNAIARQGHEHGELVQASFRDLIPLRARLGVGEISLEKPSDEQKQEVANKTKLALQKILSKQIAQSQPKSAVVQQRDDPVYIRYTPSNQMGQALSKQRIIKMVTAEQDPMEPPKFRHKKVPRGPPSPPPPVLHSPPRKVSAQEQQDWQIPPSISNWKNPKGYTIPLDKRLAADGRGLNDVEINDGFAKFSEALYTVERQAREEVRYRAIMRQKMAEKEKQEKEQRLFMLAQKAREDRMGRNAASSGPSHAKPRSTSVSSEERSRSRAGSFSHHSESENEDEDSEAFRRRQELRRERRRQAEKDLRLSRMGAEKRAKLAEKDRPRDVAERVALGLSKPSMSSDTMIDSRLFNQASGLGSGFQDEDSYNVYDKPWRAAPSSTLYRPGATLSRQVDASAELERITSESRYDVLGNAHKKFKGSDEVVESRAGPVTFEKDIADPFGVDTFLNNVSSKKT","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"uniref90":"UniRef90_Q09882","disprot_id":"DP01658","ncbi_taxon_id":284812,"regions_counter":8,"creator":"cbassot","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":557,"region_id":"DP01658r003","reference_id":"26292707","start":316,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"Structure of a yeast spliceosome at 3.6-angstrom resolution. <i> Yan C, Hang J, Wan R, Huang M, Wong CC, Shi Y. </i> Science, 2015","date":"2026-01-07T15:20:20.076Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"3JB9"},{"db":"EMDB","id":"6413"}],"term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","statement":[{"text":"Prp45, a core component of NTR, has been predicted to be intrinsically disordered (59). Our structure confirms the prediction: Prp45 only contains extended secondary structural elements that span a distance of over 150 Å (Fig. 6E).","type":"Article"},{"text":"The Cryo-EM structure of the yeast spliceosome complex shows this region of the protein lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-01-07T15:20:22.866Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":99,"region_id":"DP01658r004","reference_id":"26292707","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":5,"reference_html":"Structure of a yeast spliceosome at 3.6-angstrom resolution. <i> Yan C, Hang J, Wan R, Huang M, Wong CC, Shi Y. </i> Science, 2015","date":"2026-01-07T15:20:32.501Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"3JB9"},{"db":"EMDB","id":"6413"}],"term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","statement":[{"text":"Prp45, a core component of NTR, has been predicted to be intrinsically disordered (59). Our structure confirms the prediction: Prp45 only contains extended secondary structural elements that span a distance of over 150 Å (Fig. 6E).","type":"Article"},{"text":"The Cryo-EM structure of the yeast spliceosome complex shows this region of the protein lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-01-07T15:20:34.409Z"}}],"released":"2018_11","uniref100":"UniRef100_Q09882","date":"2018-08-04T13:50:38.000Z","acc":"Q09882","name":"Pre-mRNA-processing protein 45","length":557,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","dataset":[],"UniParc":"UPI0000128739","genes":[{"name":{"value":"prp45"},"synonyms":[{"value":"cwf13"},{"value":"snw1"}],"orfNames":[{"value":"SPCC188.11"},{"value":"SPCC584.08"}]}],"alphafold_very_low_content":0.11490125673249552,"disorder_content":0.6122082585278277,"disprot_consensus":{"full":[{"start":1,"end":99,"type":"D"},{"start":316,"end":557,"type":"D"}],"Structural state":[{"start":1,"end":99,"type":"D"},{"start":316,"end":557,"type":"D"}]}},{"features":{"pfam":[{"id":"PF13499","name":"EF-hand domain pair","start":28,"end":91},{"id":"PF13499","name":"EF-hand domain pair","start":101,"end":164}],"gene3D":[{"start":89,"end":168,"id":"1.10.238.10","name":"EF-hand"},{"start":56,"end":88,"id":"1.10.238.10","name":"EF-hand"},{"start":4,"end":55,"id":"1.10.238.10","name":"EF-hand"}]},"uniref50":"UniRef50_P05434","sequence":"MSYKAKTVVSARRDQKKGRVGLTEEQKQEIREAFDLFDTDGSGTIDAKELKVAMRALGFEPKKEEIKKMISEIDKDGSGTIDFEEFLTMMTAKMGERDSREEILKAFRLFDDDNSGTITIKDLRRVAKELGENLTEEELQEMIAEADRNDDNEIDEDEFIRIMKKTSLF","taxonomy":["Eukaryota","Viridiplantae","Chlorophyta","core chlorophytes","Chlorophyceae","CS clade","Chlamydomonadales","Chlamydomonadaceae","Chlamydomonas"],"uniref90":"UniRef90_P05434","disprot_id":"DP01659","ncbi_taxon_id":3055,"regions_counter":1,"creator":"bhajdu","regions":[{"region_id":"DP01659r001","ec_ontology":"ECO","end":23,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":1,"version":3,"statement":[{"text":"Initial analysis of the NOE data indicated that the first 23 residues (Gly(2) through Gly21) of the 96-residue CRC-N construct were highly disordered.","type":"Methods"}],"term_name":"disorder","reference_html":"Structure of the N-terminal calcium sensor domain of centrin reveals the biochemical basis for domain-specific function. <i> Sheehan JH, Bunick CG, Hu H, Fagan PA, Meyn SM, Chazin WJ. </i> J Biol Chem, 2006","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16317001","date":"2023-09-27T16:39:28.373Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2AMI"},{"db":"BMRB","id":"6820"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"GSMSYKAKTVVSARRDQKKGRVGLTEEQKQEIREAFDLFDTDGSGTIDAKELKVAMRALGFEPKKEEIKKMISEIDKDGSGTIDFEEFLTMMTAKM"}],"released":"2018_11","uniref100":"UniRef100_P05434","date":"2018-08-06T07:35:19.000Z","acc":"P05434","name":"Caltractin","length":169,"organism":"Chlamydomonas reinhardtii","dataset":[],"UniParc":"UPI00001270C5","genes":[],"alphafold_very_low_content":0.11834319526627218,"disorder_content":0.13609467455621302,"disprot_consensus":{"full":[{"start":1,"end":23,"type":"D"}],"Structural state":[{"start":1,"end":23,"type":"D"}]}},{"features":{"pfam":[{"id":"PF05757","name":"Oxygen evolving enhancer protein 3","start":1,"end":232}],"gene3D":[{"start":84,"end":232,"id":"1.20.120.290","name":"Oxygen-evolving enhancer protein 3 (PsbQ), four-helix up-down bundle"}]},"uniref50":"UniRef50_P12301","sequence":"MAQAMASMAGLRGASQAVLEGSLQISGSNRLSGPTTSRVAVPKMGLNIRAQQVSAEAETSRRAMLGFVAAGLASGSFVKAVLAEARPIVVGPPPPLSGGLPGTENSDQARDGTLPYTKDRFYLQPLPPTEAAQRAKVSASEILNVKQFIDRKAWPSLQNDLRLRASYLRYDLKTVISAKPKDEKKSLQELTSKLFSSIDNLDHAAKIKSPTEAEKYYGQTVSNINEVLAKLG","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","Caryophyllales","Chenopodiaceae","Chenopodioideae","Anserineae","Spinacia"],"uniref90":"UniRef90_P12301","disprot_id":"DP01660","ncbi_taxon_id":3562,"regions_counter":3,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":116,"region_id":"DP01660r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The 1.49 A resolution crystal structure of PsbQ from photosystem II of Spinacia oleracea reveals a PPII structure in the N-terminal region. <i> Balsera M, Arellano JB, Revuelta JL, de las Rivas J, Hermoso JA. </i> J Mol Biol, 2005","statement":[{"text":"Thirdly, residues 14–33 are not visible in the electron density map, suggesting that this loop might be very flexible and presumably extended when PsbQ is free in solution","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"akajava","start":97,"term_ontology":"IDPO","curator_name":"Andrey V Kajava","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2342-6886","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1VYK"}],"reference_id":"15982665","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-25T16:00:46.301Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":119,"region_id":"DP01660r002","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Solution NMR and molecular dynamics reveal a persistent alpha helix within the dynamic region of PsbQ from photosystem II of higher plants. <i> Rathner P, Rathner A, Horničáková M, Wohlschlager C, Chandra K, Kohoutová J, Ettrich R, Wimmer R, Müller N. </i> Proteins, 2015","statement":[{"text":"The heteronuclear NOEs and relaxation rates corroborate the first 35 residues of the N‐terminal region and the residues between helix 0 and helix 1 to be highly flexible and intrinsically disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":84,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-25T14:13:50.632Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2MWQ"},{"db":"BMRB","id":"25350"}],"reference_id":"26138376","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":83,"reference_id":"27251276","reference_source":"pmid","reference_html":"Structure of spinach photosystem II-LHCII supercomplex at 3.2 Å resolution. <i> Wei X, Su X, Cao P, Liu X, Chang W, Li M, Zhang X, Liu Z. </i> Nature, 2016","date":"2022-08-25T14:18:08.062Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-6617"},{"db":"PDB","id":"3JCU"}],"region_id":"DP01660r003","statement":[{"text":"In the Cryo-EM structure of spinach PSII-LHCII supercomplex portrayed in the PDB this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"released":"2018_11","uniref100":"UniRef100_P12301","date":"2018-08-06T07:57:26.000Z","acc":"P12301","name":"Oxygen-evolving enhancer protein 3, chloroplastic","length":232,"organism":"Spinacia oleracea","dataset":[],"UniParc":"UPI000013273B","genes":[{"name":{"value":"PSBQ"}}],"alphafold_very_low_content":0.3146551724137931,"disorder_content":0.5129310344827587,"disprot_consensus":{"full":[{"start":1,"end":119,"type":"D"}],"Structural state":[{"start":1,"end":119,"type":"D"}]}},{"features":{"pfam":[{"id":"PF06393","name":"BH3 interacting domain (BID)","start":4,"end":192}],"gene3D":[{"start":1,"end":195,"id":"1.10.437.10","name":"Blc2-like"}]},"uniref50":"UniRef50_P70444","sequence":"MDSEVSNGSGLGAEHITDLLVFGFLQSSGCTRQELEVLGRELPVQAYWEADLEDELQTDGSQASRSFNQGRIEPDSESQEEIIHNIARHLAQIGDEMDHNIQPTLVRQLAAQFMNGSLSEEDKRNCLAKALDEVKTAFPRDMENDKAMLIMTMLLAKKVASHAPSLLRDVFHTTVNFINQNLFSYVRNLVRNEMD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P70444","disprot_id":"DP01661","ncbi_taxon_id":10090,"regions_counter":2,"creator":"tszani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":81,"region_id":"DP01661r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists. <i> McDonnell JM, Fushman D, Milliman CL, Korsmeyer SJ, Cowburn D. </i> Cell, 1999","term_id":"IDPO:0000002","curator_id":"tszani","start":41,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1DDB"}],"reference_id":"10089878","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":81,"term_name":"flexible linker","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists. <i> McDonnell JM, Fushman D, Milliman CL, Korsmeyer SJ, Cowburn D. </i> Cell, 1999","term_id":"IDPO:0000033","curator_id":"tszani","start":41,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","reference_id":"10089878","version":3,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01661r002","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_P70444","date":"2018-08-06T12:14:34.000Z","acc":"P70444","name":"BH3-interacting domain death agonist","length":195,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000271E5","genes":[{"name":{"value":"Bid"}}],"alphafold_very_low_content":0.21025641025641026,"disorder_content":0.21025641025641026,"disprot_consensus":{"full":[{"start":41,"end":81,"type":"D"}],"Structural state":[{"start":41,"end":81,"type":"D"}],"Disorder function":[{"start":41,"end":81,"type":"F"}]}},{"features":{"pfam":[{"id":"PF06393","name":"BH3 interacting domain (BID)","start":3,"end":192}],"gene3D":[{"start":1,"end":195,"id":"1.10.437.10","name":"Blc2-like"}]},"uniref50":"UniRef50_P55957","sequence":"MDCEVNNGSSLRDECITNLLVFGFLQSCSDNSFRRELDALGHELPVLAPQWEGYDELQTDGNRSSHSRLGRIEADSESQEDIIRNIARHLAQVGDSMDRSIPPGLVNGLALQLRNTSRSEEDRNRDLATALEQLLQAYPRDMEKEKTMLVLALLLAKKVASHTPSLLRDVFHTTVNFINQNLRTYVRSLARNGMD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P55957","disprot_id":"DP01662","ncbi_taxon_id":9606,"regions_counter":6,"creator":"tszani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":12,"region_id":"DP01662r001","released":"2022_06","ec_id":"ECO:0006165","reference_html":"Solution structure of BID, an intracellular amplifier of apoptotic signaling. <i> Chou JJ, Li H, Salvesen GS, Yuan J, Wagner G. </i> Cell, 1999","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-05-16T13:56:41.655Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2BID"}],"reference_id":"10089877","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Loops 1–12 and 43–77 are not displayed in the figure because they are completely disordered.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-01T09:11:01.339Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":77,"region_id":"DP01662r002","released":"2022_06","ec_id":"ECO:0006165","reference_html":"Solution structure of BID, an intracellular amplifier of apoptotic signaling. <i> Chou JJ, Li H, Salvesen GS, Yuan J, Wagner G. </i> Cell, 1999","term_id":"IDPO:0000002","curator_id":"fquaglia","start":43,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-05-16T13:56:54.224Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2BID"}],"reference_id":"10089877","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Loops 1–12 and 43–77 are not displayed in the figure because they are completely disordered.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-01T09:10:59.476Z"}},{"start":76,"end":106,"reference_id":"20392693","reference_source":"pmid","reference_html":"Apoptotic regulation by MCL-1 through heterodimerization. <i> Liu Q, Moldoveanu T, Sprules T, Matta-Camacho E, Mansur-Azzam N, Gehring K. </i> J Biol Chem, 2010","date":"2022-05-31T19:54:17.997Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP01662r003","sequence_construct":"GPLGSESQEDIIRNIARHLAQVGDSMDRSIPPGLV","statement":[{"text":"The signals in the free peptide spectrum (black) fall in the center of the spectrum, which is indicative of an unstructured conformation.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-01T09:06:23.776Z"}},{"start":76,"end":106,"reference_id":"20392693","reference_source":"pmid","reference_html":"Apoptotic regulation by MCL-1 through heterodimerization. <i> Liu Q, Moldoveanu T, Sprules T, Matta-Camacho E, Mansur-Azzam N, Gehring K. </i> J Biol Chem, 2010","date":"2022-05-31T19:57:18.667Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP01662r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q07820"}],"sequence_construct":"GPLGSESQEDIIRNIARHLAQVGDSMDRSIPPGLV","statement":[{"text":"When bound, most of the peaks (colored) dispersed reflecting conformational changes and folding of the peptide.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"2KBW"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-01T09:06:25.023Z"}},{"start":76,"end":106,"reference_id":"20392693","reference_source":"pmid","reference_html":"Apoptotic regulation by MCL-1 through heterodimerization. <i> Liu Q, Moldoveanu T, Sprules T, Matta-Camacho E, Mansur-Azzam N, Gehring K. </i> J Biol Chem, 2010","date":"2022-06-01T12:31:24.551Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP01662r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q07820"}],"sequence_construct":"GPLGSESQEDIIRNIARHLAQVGDSMDRSIPPGLV","statement":[{"text":"The signals in the free peptide spectrum (black) fall in the center of the spectrum, which is indicative of an unstructured conformation. When bound, most of the peaks (colored) dispersed reflecting conformational changes and folding of the peptide.","type":"Results"}],"states_connection":[{"source":"DP01662r003","target":"DP01662r004"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-01T13:41:23.907Z"}},{"start":76,"end":106,"reference_id":"20392693","reference_source":"pmid","reference_html":"Apoptotic regulation by MCL-1 through heterodimerization. <i> Liu Q, Moldoveanu T, Sprules T, Matta-Camacho E, Mansur-Azzam N, Gehring K. </i> J Biol Chem, 2010","date":"2022-05-31T20:02:42.545Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"annotation_extensions":[],"cross_refs":[{"db":"PDB","id":"2KBW"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q07820","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01662r006","sequence_construct":"GPLGSESQEDIIRNIARHLAQVGDSMDRSIPPGLV","statement":[{"text":"Chemical shift perturbations in cMCL-1 upon peptide binding were very similar (data not shown); the BID-BH3 titration spectra were selected as representative to analyze in more detail.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-01T09:06:14.458Z"}}],"released":"2018_11","uniref100":"UniRef100_P55957","date":"2018-08-06T12:21:29.000Z","acc":"P55957","name":"BH3-interacting domain death agonist","length":195,"organism":"Homo sapiens","dataset":["Autophagy-related proteins"],"UniParc":"UPI0000001637","genes":[{"name":{"value":"BID"}}],"alphafold_very_low_content":0.18461538461538463,"disorder_content":0.38974358974358975,"disprot_consensus":{"full":[{"start":1,"end":12,"type":"D"},{"start":43,"end":75,"type":"D"},{"start":76,"end":106,"type":"T"}],"Structural state":[{"start":1,"end":12,"type":"D"},{"start":43,"end":106,"type":"D"}],"Structural transition":[{"start":76,"end":106,"type":"T"}],"Molecular function":[{"start":76,"end":106,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00377","name":"Prion/Doppel alpha-helical domain","start":147,"end":270}],"gene3D":[{"start":104,"end":249,"id":"1.10.790.10","name":"Prion/Doppel protein, beta-ribbon domain"}]},"uniref50":"UniRef50_P27177","sequence":"MARLLTTCCLLALLLAACTDVALSKKGKGKPSGGGWGAGSHRQPSYPRQPGYPHNPGYPHNPGYPHNPGYPHNPGYPHNPGYPQNPGYPHNPGYPGWGQGYNPSSGGSYHNQKPWKPPKTNFKHVAGAAAAGAVVGGLGGYAMGRVMSGMNYHFDSPDEYRWWSENSARYPNRVYYRDYSSPVPQDVFVADCFNITVTEYSIGPAAKKNTSEAVAAANQTEVEMENKVVTKVIREMCVQQYREYRLASGIQLHPADTWLAVLLLLLTTLFAMH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Phasianinae","Gallus"],"uniref90":"UniRef90_P27177","disprot_id":"DP01663","ncbi_taxon_id":9031,"regions_counter":3,"creator":"bhajdu","regions":[{"region_id":"DP01663r001","ec_ontology":"ECO","end":134,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":25,"version":3,"statement":[{"text":"N-terminal to this structured domain there is a flexibly disordered tail of 110 residues for chPrP(23–225), 118 residues for tPrP(23–225), and 69 residues for mature xlPrP (Fig. 1).","type":"Results"}],"term_name":"disorder","reference_html":"Prion protein NMR structures of chickens, turtles, and frogs. <i> Calzolai L, Lysek DA, Pérez DR, Güntert P, Wüthrich K. </i> Proc Natl Acad Sci U S A, 2005","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15647366","date":"2023-09-27T17:03:16.187Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1U3M"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser156Arg","start":null,"end":null,"position":null}],"sequence_construct":"GSVVGGLGGYAMGRVMSGMNYHFDRPDEYRWWSENSARYPNRVYYRDYSSPVPQDVFVADCFNITVTEYSIGPAAKKNTSEAVAAANQTEVEMENKVVTKVIREMCVQQYREYRLAS"},{"region_id":"DP01663r002","ec_ontology":"ECO","end":217,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":200,"version":3,"statement":[{"text":"An additional “structural signature” for chPrP is provided by an insertion between the helices α2 and α3 ​(Figs.11 and ​and2), which forms a flexibly disordered loop and an N-terminal elongation of helix α3 in chPrP(121–225) (Fig. 3). This insertion is conserved in all known avian PrP sequences (4).","type":"Results"}],"term_name":"disorder","reference_html":"Prion protein NMR structures of chickens, turtles, and frogs. <i> Calzolai L, Lysek DA, Pérez DR, Güntert P, Wüthrich K. </i> Proc Natl Acad Sci U S A, 2005","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15647366","date":"2023-09-27T16:57:18.172Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1U3M"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser156Arg","start":null,"end":null,"position":null}],"sequence_construct":"GSVVGGLGGYAMGRVMSGMNYHFDRPDEYRWWSENSARYPNRVYYRDYSSPVPQDVFVADCFNITVTEYSIGPAAKKNTSEAVAAANQTEVEMENKVVTKVIREMCVQQYREYRLAS"},{"start":200,"end":217,"reference_id":"15647366","reference_source":"pmid","reference_html":"Prion protein NMR structures of chickens, turtles, and frogs. <i> Calzolai L, Lysek DA, Pérez DR, Güntert P, Wüthrich K. </i> Proc Natl Acad Sci U S A, 2005","date":"2023-09-27T17:20:52.533Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser156Arg","start":null,"end":null,"position":null}],"region_id":"DP01663r003","sequence_construct":"GSVVGGLGGYAMGRVMSGMNYHFDRPDEYRWWSENSARYPNRVYYRDYSSPVPQDVFVADCFNITVTEYSIGPAAKKNTSEAVAAANQTEVEMENKVVTKVIREMCVQQYREYRLAS","statement":[{"text":" An additional “structural signature” for chPrP is provided by an insertion between the helices α2 and α3 (Figs.11 and ​and2), which forms a flexibly disordered loop and an N-terminal elongation of helix α3 in chPrP(121–225) (Fig. 3). This insertion is conserved in all known avian PrP sequences (4).","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_P27177","date":"2018-08-06T13:08:16.000Z","acc":"P27177","name":"Major prion protein homolog","length":273,"organism":"Gallus gallus","dataset":[],"UniParc":"UPI0000171396","genes":[{"name":{"value":"PRNP"},"synonyms":[{"value":"PRN-P"}]}],"alphafold_very_low_content":0.31135531135531136,"disorder_content":0.46886446886446886,"disprot_consensus":{"full":[{"start":25,"end":134,"type":"D"},{"start":200,"end":217,"type":"D"}],"Structural state":[{"start":25,"end":134,"type":"D"},{"start":200,"end":217,"type":"D"}],"Disorder function":[{"start":200,"end":217,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00377","name":"Prion/Doppel alpha-helical domain","start":156,"end":268},{"id":"PF11587","name":"Major prion protein bPrPp - N terminal","start":1,"end":26}],"gene3D":[{"start":111,"end":248,"id":"1.10.790.10","name":"Prion/Doppel protein, beta-ribbon domain"}]},"uniref50":"UniRef50_A0A1U7S5P0","sequence":"MGRYRLTCWIVVLLVVMWSDVSFSKKGKGKGGGGGNTGSNRNPNYPSNPGYPQNPGYPRNPSYPHNPAYPPNPAYPPNPGYPHNPSYPRNPSYPQNPGYPGGGGQHYNPAGGGTNFKNQKPWKPDKPKTNMKAMAGAAAAGAVVGGLGGYALGSAMSGMRMNFDRPEERQWWNENSNRYPNQVYYKEYNDRSVPEGRFVRDCLNNTVTEYKIDPNENQNVTQVEVRVMKQVIQEMCMQQYQQYQLASGVKLLSDPSLMLIIMLVIFFVMH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Testudines","Cryptodira","Durocryptodira","Testudinoidea","Emydidae","Trachemys"],"uniref90":"UniRef90_Q9I9C0","disprot_id":"DP01664","ncbi_taxon_id":34903,"regions_counter":1,"creator":"bhajdu","regions":[{"region_id":"DP01664r001","ec_ontology":"ECO","end":142,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":25,"version":3,"statement":[{"text":"N-terminal to this structured domain there is a flexibly disordered tail of 110 residues for chPrP(23–225), 118 residues for tPrP(23–225), and 69 residues for mature xlPrP (Fig. 1).","type":"Results"}],"term_name":"disorder","reference_html":"Prion protein NMR structures of chickens, turtles, and frogs. <i> Calzolai L, Lysek DA, Pérez DR, Güntert P, Wüthrich K. </i> Proc Natl Acad Sci U S A, 2005","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15647366","date":"2023-09-27T17:24:50.235Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1U5L"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu203Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asn205Ile","start":null,"end":null,"position":null}],"sequence_construct":"GSVVGGLGGYALGSAMSGMRMNFDRPEERQWWNENSNRYPNQVYYKEYNDRSVPEGRFVRDCVNITVTEYKIDPNENQNVTQVEVRVMKQVIQEMCMQQYQQYQLASG"}],"released":"2018_11","uniref100":"UniRef100_Q9I9C0","date":"2018-08-06T13:18:55.000Z","acc":"Q9I9C0","name":"Prion protein","length":270,"organism":"Trachemys scripta","dataset":[],"UniParc":"UPI00000FD9B9","genes":[{"name":{"value":"prnp","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAB81568.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAB81568.1"}}]}}],"alphafold_very_low_content":0.34444444444444444,"disorder_content":0.43703703703703706,"disprot_consensus":{"full":[{"start":25,"end":142,"type":"D"}],"Structural state":[{"start":25,"end":142,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00377","name":"Prion/Doppel alpha-helical domain","start":81,"end":168}],"gene3D":[{"start":41,"end":171,"id":"1.10.790.10","name":"Prion/Doppel protein, beta-ribbon domain"}]},"uniref50":"UniRef50_Q6GLY6","sequence":"KKSGGGKSKTGGWNTGSNRNPNYPGGYPGNTGGSWGQQPYNPSGYNKQWKPPKSKTNMKSVAIGAAAGAIGGYMLGNAVGRMSYQFNNPMESRYYNDYYNQMPNRVYRPMYRGEEYVSEDRFVRDCYNMSVTEYIIKPAEGKNNSELNQLDTTVKSQIIREMCITEYRRGS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Amphibia","Batrachia","Anura","Pipoidea","Pipidae","Xenopodinae","Xenopus","Xenopus"],"uniref90":"UniRef90_A0A1L8H1R5","disprot_id":"DP01665","ncbi_taxon_id":8355,"regions_counter":1,"creator":"bhajdu","regions":[{"region_id":"DP01665r001","ec_ontology":"ECO","end":69,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":1,"version":3,"statement":[{"text":"N-terminal to this structured domain there is a flexibly disordered tail of 110 residues for chPrP(23–225), 118 residues for tPrP(23–225), and 69 residues for mature xlPrP (Fig. 1).","type":"Results"}],"term_name":"disorder","reference_html":"Prion protein NMR structures of chickens, turtles, and frogs. <i> Calzolai L, Lysek DA, Pérez DR, Güntert P, Wüthrich K. </i> Proc Natl Acad Sci U S A, 2005","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15647366","date":"2023-09-27T17:26:27.913Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1XU0"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"GSGYNKQWKPPKSKTNMKSVAIGAAAGAIGGYMLGNAVGRMSYQFNNPMESRYYNDYYNQMPNRVYRPMYRGEEYVSEDRFVRDCYNMSVTEYIIKPAEGKNNSELNQLDTTVKSQIIREMCITEYRRGS"}],"released":"2018_11","uniref100":"UniRef100_A0A1L8H1R5","date":"2018-08-06T13:23:17.000Z","acc":"Q5S1W7","name":"Prion protein","length":171,"organism":"Xenopus laevis","dataset":[],"UniParc":"UPI000046D34A","genes":[],"alphafold_very_low_content":0.36257309941520466,"disorder_content":0.40350877192982454,"disprot_consensus":{"full":[{"start":1,"end":69,"type":"D"}],"Structural state":[{"start":1,"end":69,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00554","name":"Rel homology DNA-binding domain","start":21,"end":186},{"id":"PF16179","name":"Rel homology dimerisation domain","start":195,"end":291}],"gene3D":[{"start":9,"end":187,"id":"2.60.40.340","name":"Rel homology domain (RHD), DNA-binding domain"},{"start":191,"end":304,"id":"2.60.40.10","name":"Immunoglobulins"}]},"uniref50":"UniRef50_Q04206-4","sequence":"MDDLFPLIFPSEPAQASGPYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGYYEADLCPDRSIHSFQNLGIQCVKKRDLEQAISQRIQTNNNPFHVPIEEQRGDYDLNAVRLCFQVTVRDPAGRPLLLTPVLSHPIFDNRAPNTAELKICRVNRNSGSCLGGDEIFLLCDKVQKEDIEVYFTGPGWEARGSFSQADVHRQVAIVFRTPPYADPSLQAPVRVSMQLRRPSDRELSEPMEFQYLPDTDDRHRIEEKRKRTYETFKSIMKKSPFNGPTEPRPPTRRIAVPTRNSTSVPKPAPQPYTFPASLSTINFDEFSPMLLPSGQISNQALALAPSSAPVLAQTMVPSSAMVPLAQPPAPAPVLTPGPPQSLSAPVPKSTQAGEGTLSEALLHLQFDADEDLGALLGNSTDPGVFTDLASVDNSEFQQLLNQGVSMSHSTAEPMLMEYPEAITRLVTGSQRPPDPAPTPLGTSGLPNGLSGDEDFSSIADMDFSALLSQISS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q04207","disprot_id":"DP01667","ncbi_taxon_id":10090,"regions_counter":2,"creator":"tszani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":490,"region_id":"DP01667r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Analysis of the RelA:CBP/p300 interaction reveals its involvement in NF-κB-driven transcription. <i> Mukherjee SP, Behar M, Birnbaum HA, Hoffmann A, Wright PE, Ghosh G. </i> PLoS Biol, 2013","term_id":"IDPO:0000002","curator_id":"tszani","start":426,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24019758","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":490,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Analysis of the RelA:CBP/p300 interaction reveals its involvement in NF-κB-driven transcription. <i> Mukherjee SP, Behar M, Birnbaum HA, Hoffmann A, Wright PE, Ghosh G. </i> PLoS Biol, 2013","term_id":"GO:0005515","curator_id":"tszani","start":426,"term_ontology":"GO","curator_name":"Tamás Szaniszló","reference_id":"24019758","version":3,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01667r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q04207","date":"2018-08-06T14:43:28.000Z","acc":"Q548Y4","name":"Nuclear transcription factor RelA","length":549,"organism":"Mus musculus","dataset":[],"UniParc":"UPI000000088B","genes":[{"name":{"value":"Rela","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF82405.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF82405.1"}},{"code":"ECO:0000313","source":{"name":"MGI","id":"MGI:103290","url":"http://www.informatics.jax.org/marker/MGI:103290"}}]}}],"alphafold_very_low_content":0.39526411657559196,"disorder_content":0.11839708561020036,"disprot_consensus":{"full":[{"start":426,"end":490,"type":"D"}],"Structural state":[{"start":426,"end":490,"type":"D"}],"Molecular function":[{"start":426,"end":490,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00458","name":"WHEP-TRS domain","start":7,"end":45},{"id":"PF03129","name":"Anticodon binding domain","start":410,"end":500},{"id":"PF13393","name":"Histidyl-tRNA synthetase","start":61,"end":389}],"gene3D":[{"start":405,"end":506,"id":"3.40.50.800","name":"Anticodon-binding domain"},{"start":1,"end":45,"id":"1.10.287.10","name":"S15/NS1, RNA-binding"},{"start":46,"end":404,"id":"3.30.930.10","name":"Bira Bifunctional Protein; Domain 2"}]},"uniref50":"UniRef50_P12081","sequence":"MAERAALEELVKLQGERVRGLKQQKASAELIEEEVAKLLKLKAQLGPDESKQKFVLKTPKGTRDYSPRQMAVREKVFDVIIRCFKRHGAEVIDTPVFELKETLMGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKLTNIKRYHIAKVYRRDNPAMTRGRYREFYQCDFDIAGNFDPMIPDAECLKIMCEILSSLQIGDFLVKVNDRRILDGMFAICGVSDSKFRTICSSVDKLDKVSWEEVKNEMVGEKGLAPEVADRIGDYVQQHGGVSLVEQLLQDPKLSQNKQALEGLGDLKLLFEYLTLFGIDDKISFDLSLARGLDYYTGVIYEAVLLQTPAQAGEEPLGVGSVAAGGRYDGLVGMFDPKGRKVPCVGLSIGVERIFSIVEQRLEALEEKIRTTETQVLVASAQKKLLEERLKLVSELWDAGIKAELLYKKNPKLLNQLQYCEEAGIPLVAIIGEQELKDGVIKLRSVTSREEVDVRREDLVEEIKRRTGQPLCIC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P12081","disprot_id":"DP01668","ncbi_taxon_id":9606,"regions_counter":2,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":355,"region_id":"DP01668r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Comparison of histidine recognition in human and trypanosomatid histidyl-tRNA synthetases. <i> Koh CY, Wetzel AB, de van der Schueren WJ, Hol WG. </i> Biochimie, 2014","statement":[{"text":"Well-defined electron density is present for most parts of the protein in all four chains of Hs-cHisRS except the N-terminal WHEP domains (52 residues). In addition, in all four chains, five residues at the C-termini, and between eight to twelve residues in two internal loops (Pro344 to Gly355; Glu401 to Glu402), are disordered. These loops are not directly involved in histidine or ATP binding.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"akajava","start":344,"term_ontology":"IDPO","curator_name":"Andrey V Kajava","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2342-6886","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4PHC"}],"reference_id":"25151410","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-25T18:53:40.721Z"}},{"start":1,"end":52,"reference_id":"25151410","reference_source":"pmid","reference_html":"Comparison of histidine recognition in human and trypanosomatid histidyl-tRNA synthetases. <i> Koh CY, Wetzel AB, de van der Schueren WJ, Hol WG. </i> Biochimie, 2014","date":"2022-08-25T18:52:49.054Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"4PHC"}],"region_id":"DP01668r002","statement":[{"text":"Well-defined electron density is present for most parts of the protein in all four chains of Hs-cHisRS except the N-terminal WHEP domains (52 residues). In addition, in all four chains, five residues at the C-termini, and between eight to twelve residues in two internal loops (Pro344 to Gly355; Glu401 to Glu402), are disordered. These loops are not directly involved in histidine or ATP binding.","type":"Methods"}]}],"released":"2018_11","uniref100":"UniRef100_P12081","date":"2018-08-06T14:59:04.000Z","acc":"P12081","name":"Histidine--tRNA ligase, cytoplasmic","length":509,"organism":"Homo sapiens","dataset":["NDDs-related proteins","RNA-binding proteins"],"UniParc":"UPI000016AAA7","genes":[{"name":{"value":"HARS1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4816","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4816"}}]},"synonyms":[{"value":"HARS"},{"value":"HRS"}]}],"alphafold_very_low_content":0.019646365422396856,"disorder_content":0.12573673870333987,"disprot_consensus":{"full":[{"start":1,"end":52,"type":"D"},{"start":344,"end":355,"type":"D"}],"Structural state":[{"start":1,"end":52,"type":"D"},{"start":344,"end":355,"type":"D"}]}},{"features":{"pfam":[{"id":"PF13499","name":"EF-hand domain pair","start":135,"end":195},{"id":"PF22592","name":"FCaBP EF-hand domain","start":37,"end":129}],"gene3D":[{"start":1,"end":218,"id":"1.10.238.10","name":"EF-hand"}]},"uniref50":"UniRef50_P17882","sequence":"MGCSASKDTTNSKDGAASKGGKDGKTTADRKVAWERIRCAIPRDKDAESKSRRIELFKQFDTNGTGKLGFREVLDGCYGILKLDEFTTHLPDIVQRAFDKAKDLGNKVKGVGEEDLVEFLEFRLMLCYIYDIFELTVMFDTMDKDGSLLLELQEFKEALPKLKEWGVDITDATTVFNEIDTNGSGVVTFDEFSCWAVTKKLQVCGDPDGEENGANEGN","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Trypanosoma"],"uniref90":"UniRef90_P17882","disprot_id":"DP01669","ncbi_taxon_id":5702,"regions_counter":2,"creator":"akajava","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":25,"region_id":"DP01669r001","start":1,"ec_id":"ECO:0006165","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The first 26 residues from the N-terminus exhibited random-coil amide chemical shifts with non-uniform intensities, indicating that the N-terminal region is indeed solvent-exposed and dynamically disordered. \n","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23011904","version":3,"reference_html":"NMR structure of the calflagin Tb24 flagellar calcium binding protein of Trypanosoma brucei. <i> Xu X, Olson CL, Engman DM, Ames JB. </i> Protein Sci, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","cross_refs":[{"db":"PDB","id":"2LVV"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-16T14:56:09.118Z"}},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":218,"region_id":"DP01669r002","start":206,"ec_id":"ECO:0006165","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"C-terminal residues (206–218) also have chemical shifts consistent with a random coil.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23011904","version":3,"reference_html":"NMR structure of the calflagin Tb24 flagellar calcium binding protein of Trypanosoma brucei. <i> Xu X, Olson CL, Engman DM, Ames JB. </i> Protein Sci, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","cross_refs":[{"db":"PDB","id":"2LVV"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-16T14:54:30.198Z"}}],"released":"2018_11","uniref100":"UniRef100_Q26680","date":"2018-08-06T15:25:36.000Z","acc":"Q26680","name":"Flagellar calcium-binding protein TB-24","length":218,"organism":"Trypanosoma brucei brucei","dataset":["Neglected tropical diseases proteins"],"UniParc":"UPI000012A590","genes":[],"alphafold_very_low_content":0.14678899082568808,"disorder_content":0.1743119266055046,"disprot_consensus":{"full":[{"start":1,"end":25,"type":"D"},{"start":206,"end":218,"type":"D"}],"Structural state":[{"start":1,"end":25,"type":"D"},{"start":206,"end":218,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01068","name":"ATP dependent DNA ligase domain","start":224,"end":399},{"id":"PF04679","name":"ATP dependent DNA ligase C terminal region","start":418,"end":515},{"id":"PF13298","name":"DNA Ligase D 3'-phosphoesterase domain","start":40,"end":145},{"id":"PF21686","name":"LigD, primase-polymerase domain","start":566,"end":819}],"gene3D":[{"start":229,"end":397,"id":"3.30.1490.70","name":"3.30.1490.70"},{"start":402,"end":523,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"},{"start":241,"end":356,"id":"3.30.470.30","name":"DNA ligase/mRNA capping enzyme"}]},"uniref50":"UniRef50_Q9I1X7","sequence":"MPSSKPLAEYARKRDFRQTPEPSGRKPRKDSTGLLRYCVQKHDASRLHYDFRLELDGTLKSWAVPKGPCLDPAVKRLAVQVEDHPLDYADFEGSIPQGHYGAGDVIVWDRGAWTPLDDPREGLEKGHLSFALDGEKLSGRWHLIRTNLRGKQSQWFLVKAKDGEARSLDRFDVLKERPDSVLSERTLLPRHGEAATPAARPARRGKSGGKTPMPEWIAPELASLVEQPPRGEWAYELKLDGYRLMSRIEDGHVRLLTRNGHDWTERLPHLEKALAGLGLQRSWLDGELVVLDEEGRPDFQALQNAFEEGRGENILYVLFDLPYHEGEDLRDVALEERRARLEALLEGRDEDPLRFSATLAEDPRDLLASACKLGLEGVIGKRLGSAYRSRRSNDWIKLKCQLRQEFVIVGYTEPKGSRRHIGALLLGLYSPDEERRLRYAGKVGSGFTAASLKKVRERLEPLAVRSSPLAKVPPARETGSVQWVRPQQLCEVSYAQMTRGGIIRQAVFHGLREDKPAREVTGERPAGPPPLRGARKASAGASRAATAGVRISHPQRLIDPSIQASKLELAEFHARYADLLLRDLRERPVSLVRGPDGIGGELFFQKHAARLKIPGIVQLDPALDPGHPPLLQIRSAEALVGAVQMGSIEFHTWNASLANLERPDRFVLDLDPDPALPWKRMLEATQLSLTLLDELGLRAFLKTSGGKGMHLLVPLERRHGWDEVKDFAQAISQHLARLMPERFSAVSGPRNRVGKIFVDYLRNSRGASTVAAYSVRAREGLPVSVPVFREELDSLQGANQWNLRSLPQRLDELAGDDPWADYAGTRQRISAAMRRQLGRG","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Pseudomonadales","Pseudomonadaceae","Pseudomonas"],"uniref90":"UniRef90_Q9I1X7","disprot_id":"DP01670","ncbi_taxon_id":208964,"regions_counter":1,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":31,"region_id":"DP01670r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure and DNA-binding properties of the phosphoesterase domain of DNA ligase D. <i> Natarajan A, Dutta K, Temel DB, Nair PA, Shuman S, Ghose R. </i> Nucleic Acids Res, 2012","statement":[{"text":"Inspection of the final NMR ensemble of 15 structures (see Table 1 for statistics) reveals a disordered N-terminus (1–31). This fact is also borne out by the extremely low 15N-{1H} NOE values (0.08 ± 0.21; see Figure 1) for this region. However, some degree of local ordering is seen encompassing residues Asp15–Thr19 (15N-{1H} NOE: 0.18 ± 0.01).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"akajava","start":1,"term_ontology":"IDPO","curator_name":"Andrey V Kajava","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-2342-6886","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2LJ6"}],"reference_id":"22084199","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-25T19:00:35.949Z"}}],"released":"2018_11","uniref100":"UniRef100_Q9I1X7","date":"2018-08-06T16:29:44.000Z","acc":"Q9I1X7","name":"Multifunctional non-homologous end joining protein LigD","length":840,"organism":"Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)","dataset":[],"UniParc":"UPI00000C55C8","genes":[{"name":{"value":"ligD"},"olnNames":[{"value":"PA2138"}]}],"alphafold_very_low_content":0.05,"disorder_content":0.036904761904761905,"disprot_consensus":{"full":[{"start":1,"end":31,"type":"D"}],"Structural state":[{"start":1,"end":31,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00498","name":"FHA domain","start":456,"end":518},{"id":"PF12401","name":"FhaA, N-terminal domain","start":9,"end":121}],"gene3D":[{"start":1,"end":132,"id":"3.30.2320.60","name":"FhaA, phosphopeptide-binding domain (DUF3662)"},{"start":431,"end":527,"id":"2.60.200.20","name":"2.60.200.20"}]},"uniref50":"UniRef50_P71590","sequence":"MGSQKRLVQRVERKLEQTVGDAFARIFGGSIVPQEVEALLRREAADGIQSLQGNRLLAPNEYIITLGVHDFEKLGADPELKSTGFARDLADYIQEQGWQTYGDVVVRFEQSSNLHTGQFRARGTVNPDVETHPPVIDCARPQSNHAFGAEPGVAPMSDNSSYRGGQGQGRPDEYYDDRYARPQEDPRGGPDPQGGSDPRGGYPPETGGYPPQPGYPRPRHPDQGDYPEQIGYPDQGGYPEQRGYPEQRGYPDQRGYQDQGRGYPDQGQGGYPPPYEQRPPVSPGPAAGYGAPGYDQGYRQSGGYGPSPGGGQPGYGGYGEYGRGPARHEEGSYVPSGPPGPPEQRPAYPDQGGYDQGYQQGATTYGRQDYGGGADYTRYTESPRVPGYAPQGGGYAEPAGRDYDYGQSGAPDYGQPAPGGYSGYGQGGYGSAGTSVTLQLDDGSGRTYQLREGSNIIGRGQDAQFRLPDTGVSRRHLEIRWDGQVALLADLNSTNGTTVNNAPVQEWQLADGDVIRLGHSEIIVRMH","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"uniref90":"UniRef90_P71590","disprot_id":"DP01671","ncbi_taxon_id":83332,"regions_counter":2,"creator":"akajava","regions":[{"region_id":"DP01671r001","ec_ontology":"ECO","end":32,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":1,"version":3,"statement":[{"text":"The N-terminal part of the protein from Met1 to Val32 is disordered and represented in gray.","type":"Figure"},{"text":"Consistent with the absence of long-range NOEs, the 32 first residues adopt a random-coil conformation, with the exception of residues Ala22 to Phe27 that form a short dynamic helix, essentially defined by TALOS restraints.","type":"Results"}],"term_name":"disorder","reference_html":"Structural insight into the Mycobacterium tuberculosis Rv0020c protein and its interaction with the PknB kinase. <i> Roumestand C, Leiba J, Galophe N, Margeat E, Padilla A, Bessin Y, Barthe P, Molle V, Cohen-Gonsaud M. </i> Structure, 2011","released":"2022_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"22000520","date":"2022-08-25T19:13:04.988Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2LC0"},{"db":"BMRB","id":"17585"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":133,"end":429,"reference_id":"22000520","reference_source":"pmid","reference_html":"Structural insight into the Mycobacterium tuberculosis Rv0020c protein and its interaction with the PknB kinase. <i> Roumestand C, Leiba J, Galophe N, Margeat E, Padilla A, Bessin Y, Barthe P, Molle V, Cohen-Gonsaud M. </i> Structure, 2011","date":"2022-08-25T19:10:32.458Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP01671r002","statement":[{"text":"The others residues, corresponding to the 133–429 PG-rich peptidic segment, gave rise to the intense cross-peaks centered at 8.5 ppm in the proton dimension of the [1H,15N] HSQC spectrum of the full-length protein, thus strongly suggesting that this segment adopts a random-coil conformation.","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_P71590","date":"2018-08-07T08:04:30.000Z","acc":"P71590","name":"FHA domain-containing protein FhaA","length":527,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","dataset":[],"UniParc":"UPI00000CA92D","genes":[{"name":{"value":"fhaA"},"synonyms":[{"value":"TB39.8"}],"olnNames":[{"value":"Rv0020c"}]}],"alphafold_very_low_content":0.5275142314990512,"disorder_content":0.6242884250474383,"disprot_consensus":{"full":[{"start":1,"end":32,"type":"D"},{"start":133,"end":429,"type":"D"}],"Structural state":[{"start":1,"end":32,"type":"D"},{"start":133,"end":429,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02037","name":"SAP domain","start":10,"end":45},{"id":"PF02891","name":"MIZ/SP-RING zinc finger","start":342,"end":390},{"id":"PF14324","name":"PINIT domain","start":146,"end":297}],"gene3D":[{"start":299,"end":427,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":1,"end":65,"id":"1.10.720.30","name":"SAP domain"},{"start":145,"end":298,"id":"2.60.120.780","name":"PINIT domain"}]},"uniref50":"UniRef50_O75928","sequence":"MADFEELRNMVSSFRVSELQVLLGFAGRNKSGRKHDLLMRALHLLKSGCSPAVQIKIRELYRRRYPRTLEGLSDLSTIKSSVFSLDGGSSPVEPDLAVAGIHSLPSTSVTPHSPSSPVGSVLLQDTKPTFEMQQPSPPIPPVHPDVQLKNLPFYDVLDVLIKPTSLVQSSIQRFQEKFFIFALTPQQVREICISRDFLPGGRRDYTVQVQLRLCLAETSCPQEDNYPNSLCIKVNGKLFPLPGYAPPPKNGIEQKRPGRPLNITSLVRLSSAVPNQISISWASEIGKNYSMSVYLVRQLTSAMLLQRLKMKGIRNPDHSRALIKEKLTADPDSEIATTSLRVSLMCPLGKMRLTIPCRAVTCTHLQCFDAALYLQMNEKKPTWICPVCDKKAAYESLILDGLFMEILNDCSDVDEIKFQEDGSWCPMRPKKEAMKVSSQPCTKIESSSVLSKPCSVTVASEASKKKVDVIDLTIESSSDEEEDPPAKRKCIFMSETQSSPTKGVLMYQPSSVRVPSVTSVDPAAIPPSLTDYSVPFHHTPISSMSSDLPGLDFLSLIPVDPQYCPPMFLDSLTSPLTASSTSVTTTSSHESSTHVSSSSSRSETGVITSSGSNIPDIISLD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O75928","disprot_id":"DP01675","ncbi_taxon_id":9606,"regions_counter":4,"creator":"aelofsson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":479,"region_id":"DP01675r002","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation. <i> Song J, Zhang Z, Hu W, Chen Y. </i> J Biol Chem, 2005","term_id":"IDPO:0000002","curator_id":"vnugnes","start":466,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-12-13T13:26:37.361Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2ASQ"}],"reference_id":"16204249","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63165"}],"sequence_construct":"KVDVIDLTIESSSDEEEDPPAKRQM","statement":[{"text":" Consistent with the previous finding (22), the SSS sequence of PIASX-P and all residues C-terminal to the SSS sequence do not show inter-residue NOEs. The resonances of these residues are very narrow and identical to those of the unbound peptide. The sharp resonances indicate that these residues are highly flexible, and their motions are not restricted by forming the peptide-SUMO complex.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-15T09:28:00.776Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":474,"term_name":"protein binding","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation. <i> Song J, Zhang Z, Hu W, Chen Y. </i> J Biol Chem, 2005","term_id":"GO:0005515","curator_id":"vnugnes","start":466,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"16204249","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-12-13T13:29:47.598Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01675r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"2ASQ"}],"interaction_partner":[{"db":"UniProt","id":"P63165","operator":"and","partner_start":null,"partner_end":null}],"statement":[{"text":"The residues from the PIASX-P peptide that contact SUMO-1 include Val-2, Asp-3, Val-4, Ile-5, Leu-7, and Thr-8. Except for residue Asp-3, all of these residues have much broader NMR resonances in the complex than in the unbound peptide, indicating that complex formation has significantly restricted their motions.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-15T09:28:02.267Z"}}],"released":"2018_11","uniref100":"UniRef100_O75928","date":"2018-08-07T11:34:48.000Z","acc":"O75928","name":"E3 SUMO-protein ligase PIAS2","length":621,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI00000747E9","genes":[{"name":{"value":"PIAS2"},"synonyms":[{"value":"PIASX"}]}],"alphafold_very_low_content":0.391304347826087,"disorder_content":0.02254428341384863,"disprot_consensus":{"full":[{"start":466,"end":479,"type":"D"}],"Structural state":[{"start":466,"end":479,"type":"D"}],"Molecular function":[{"start":466,"end":474,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00628","name":"PHD-finger","start":229,"end":273},{"id":"PF00628","name":"PHD-finger","start":276,"end":320},{"id":"PF00628","name":"PHD-finger","start":1380,"end":1427},{"id":"PF00628","name":"PHD-finger","start":1430,"end":1474},{"id":"PF00856","name":"SET domain","start":5408,"end":5513},{"id":"PF05964","name":"F/Y-rich N-terminus","start":5177,"end":5234},{"id":"PF05965","name":"F/Y rich C-terminus","start":5238,"end":5322},{"id":"PF13771","name":"PHD-like zinc-binding domain","start":139,"end":218},{"id":"PF13832","name":"PHD-zinc-finger like domain","start":5031,"end":5129}],"gene3D":[{"start":1340,"end":1427,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":5026,"end":5139,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":1428,"end":1478,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":1506,"end":1549,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":222,"end":330,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":123,"end":221,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":1991,"end":2080,"id":"1.10.30.10","name":"High mobility group box domain"},{"start":5177,"end":5315,"id":"3.30.160.360","name":"3.30.160.360"},{"start":5380,"end":5537,"id":"2.170.270.10","name":"SET domain"}]},"uniref50":"UniRef50_O14686","sequence":"MDSQKLAGEDKDSEPAADGPAASEDPSATESDLPNPHVGEVSVLSSGSPRLQETPQDCSGGPVRRCALCNCGEPSLHGQRELRRFELPFDWPRCPVVSPGGSPGPNEAVLPSEDLSQIGFPEGLTPAHLGEPGGSCWAHHWCAAWSAGVWGQEGPELCGVDKAIFSGISQRCSHCTRLGASIPCRSPGCPRLYHFPCATASGSFLSMKTLQLLCPEHSEGAAYLEEARCAVCEGPGELCDLFFCTSCGHHYHGACLDTALTARKRAGWQCPECKVCQACRKPGNDSKMLVCETCDKGYHTFCLKPPMEELPAHSWKCKACRVCRACGAGSAELNPNSEWFENYSLCHRCHKAQGGQTIRSVAEQHTPVCSRFSPPEPGDTPTDEPDALYVACQGQPKGGHVTSMQPKEPGPLQCEAKPLGKAGVQLEPQLEAPLNEEMPLLPPPEESPLSPPPEESPTSPPPEASRLSPPPEELPASPLPEALHLSRPLEESPLSPPPEESPLSPPPESSPFSPLEESPLSPPEESPPSPALETPLSPPPEASPLSPPFEESPLSPPPEELPTSPPPEASRLSPPPEESPMSPPPEESPMSPPPEASRLFPPFEESPLSPPPEESPLSPPPEASRLSPPPEDSPMSPPPEESPMSPPPEVSRLSPLPVVSRLSPPPEESPLSPPPEESPTSPPPEASRLSPPPEDSPTSPPPEDSPASPPPEDSLMSLPLEESPLLPLPEEPQLCPRSEGPHLSPRPEEPHLSPRPEEPHLSPQAEEPHLSPQPEEPCLCAVPEEPHLSPQAEGPHLSPQPEELHLSPQTEEPHLSPVPEEPCLSPQPEESHLSPQSEEPCLSPRPEESHLSPELEKPPLSPRPEKPPEEPGQCPAPEELPLFPPPGEPSLSPLLGEPALSEPGEPPLSPLPEELPLSPSGEPSLSPQLMPPDPLPPPLSPIITAAAPPALSPLGELEYPFGAKGDSDPESPLAAPILETPISPPPEANCTDPEPVPPMILPPSPGSPVGPASPILMEPLPPQCSPLLQHSLVPQNSPPSQCSPPALPLSVPSPLSPIGKVVGVSDEAELHEMETEKVSEPECPALEPSATSPLPSPMGDLSCPAPSPAPALDDFSGLGEDTAPLDGIDAPGSQPEPGQTPGSLASELKGSPVLLDPEELAPVTPMEVYPECKQTAGQGSPCEEQEEPRAPVAPTPPTLIKSDIVNEISNLSQGDASASFPGSEPLLGSPDPEGGGSLSMELGVSTDVSPARDEGSLRLCTDSLPETDDSLLCDAGTAISGGKAEGEKGRRRSSPARSRIKQGRSSSFPGRRRPRGGAHGGRGRGRARLKSTASSIETLVVADIDSSPSKEEEEEDDDTMQNTVVLFSNTDKFVLMQDMCVVCGSFGRGAEGHLLACSQCSQCYHPYCVNSKITKVMLLKGWRCVECIVCEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWCVSCMQCGAASPGFHCEWQNSYTHCGPCASLVTCPICHAPYVEEDLLIQCRHCERWMHAGCESLFTEDDVEQAADEGFDCVSCQPYVVKPVAPVAPPELVPMKVKEPEPQYFRFEGVWLTETGMALLRNLTMSPLHKRRQRRGRLGLPGEAGLEGSEPSDALGPDDKKDGDLDTDELLKGEGGVEHMECEIKLEGPVSPDVEPGKEETEESKKRKRKPYRPGIGGFMVRQRKSHTRTKKGPAAQAEVLSGDGQPDEVIPADLPAEGAVEQSLAEGDEKKKQQRRGRKKSKLEDMFPAYLQEAFFGKELLDLSRKALFAVGVGRPSFGLGTPKAKGDGGSERKELPTSQKGDDGPDIADEESRGLEGKADTPGPEDGGVKASPVPSDPEKPGTPGEGMLSSDLDRISTEELPKMESKDLQQLFKDVLGSEREQHLGCGTPGLEGSRTPLQRPFLQGGLPLGNLPSSSPMDSYPGLCQSPFLDSRERGGFFSPEPGEPDSPWTGSGGTTPSTPTTPTTEGEGDGLSYNQRSLQRWEKDEELGQLSTISPVLYANINFPNLKQDYPDWSSRCKQIMKLWRKVPAADKAPYLQKAKDNRAAHRINKVQKQAESQINKQTKVGDIARKTDRPALHLRIPPQPGALGSPPPAAAPTIFIGSPTTPAGLSTSADGFLKPPAGSVPGPDSPGELFLKLPPQVPAQVPSQDPFGLAPAYPLEPRFPTAPPTYPPYPSPTGAPAQPPMLGASSRPGAGQPGEFHTTPPGTPRHQPSTPDPFLKPRCPSLDNLAVPESPGVGGGKASEPLLSPPPFGESRKALEVKKEELGASSPSYGPPNLGFVDSPSSGTHLGGLELKTPDVFKAPLTPRASQVEPQSPGLGLRPQEPPPAQALAPSPPSHPDIFRPGSYTDPYAQPPLTPRPQPPPPESCCALPPRSLPSDPFSRVPASPQSQSSSQSPLTPRPLSAEAFCPSPVTPRFQSPDPYSRPPSRPQSRDPFAPLHKPPRPQPPEVAFKAGSLAHTSLGAGGFPAALPAGPAGELHAKVPSGQPPNFVRSPGTGAFVGTPSPMRFTFPQAVGEPSLKPPVPQPGLPPPHGINSHFGPGPTLGKPQSTNYTVATGNFHPSGSPLGPSSGSTGESYGLSPLRPPSVLPPPAPDGSLPYLSHGASQRSGITSPVEKREDPGTGMGSSLATAELPGTQDPGMSGLSQTELEKQRQRQRLRELLIRQQIQRNTLRQEKETAAAAAGAVGPPGSWGAEPSSPAFEQLSRGQTPFAGTQDKSSLVGLPPSKLSGPILGPGSFPSDDRLSRPPPPATPSSMDVNSRQLVGGSQAFYQRAPYPGSLPLQQQQQQLWQQQQATAATSMRFAMSARFPSTPGPELGRQALGSPLAGISTRLPGPGEPVPGPAGPAQFIELRHNVQKGLGPGGTPFPGQGPPQRPRFYPVSEDPHRLAPEGLRGLAVSGLPPQKPSAPPAPELNNSLHPTPHTKGPTLPTGLELVNRPPSSTELGRPNPLALEAGKLPCEDPELDDDFDAHKALEDDEELAHLGLGVDVAKGDDELGTLENLETNDPHLDDLLNGDEFDLLAYTDPELDTGDKKDIFNEHLRLVESANEKAEREALLRGVEPGPLGPEERPPPAADASEPRLASVLPEVKPKVEEGGRHPSPCQFTIATPKVEPAPAANSLGLGLKPGQSMMGSRDTRMGTGPFSSSGHTAEKASFGATGGPPAHLLTPSPLSGPGGSSLLEKFELESGALTLPGGPAASGDELDKMESSLVASELPLLIEDLLEHEKKELQKKQQLSAQLQPAQQQQQQQQQHSLLSAPGPAQAMSLPHEGSSPSLAGSQQQLSLGLAGARQPGLPQPLMPTQPPAHALQQRLAPSMAMVSNQGHMLSGQHGGQAGLVPQQSSQPVLSQKPMGTMPPSMCMKPQQLAMQQQLANSFFPDTDLDKFAAEDIIDPIAKAKMVALKGIKKVMAQGSIGVAPGMNRQQVSLLAQRLSGGPSSDLQNHVAAGSGQERSAGDPSQPRPNPPTFAQGVINEADQRQYEEWLFHTQQLLQMQLKVLEEQIGVHRKSRKALCAKQRTAKKAGREFPEADAEKLKLVTEQQSKIQKQLDQVRKQQKEHTNLMAEYRNKQQQQQQQQQQQQQQHSAVLALSPSQSPRLLTKLPGQLLPGHGLQPPQGPPGGQAGGLRLTPGGMALPGQPGGPFLNTALAQQQQQQHSGGAGSLAGPSGGFFPGNLALRSLGPDSRLLQERQLQLQQQRMQLAQKLQQQQQQQQQQQHLLGQVAIQQQQQQGPGVQTNQALGPKPQGLMPPSSHQGLLVQQLSPQPPQGPQGMLGPAQVAVLQQQHPGALGPQGPHRQVLMTQSRVLSSPQLAQQGQGLMGHRLVTAQQQQQQQQHQQQGSMAGLSHLQQSLMSHSGQPKLSAQPMGSLQQLQQQQQLQQQQQLQQQQQQQLQQQQQLQQQQLQQQQQQQQLQQQQQQQLQQQQQQLQQQQQQQQQQFQQQQQQQQMGLLNQSRTLLSPQQQQQQQVALGPGMPAKPLQHFSSPGALGPTLLLTGKEQNTVDPAVSSEATEGPSTHQGGPLAIGTTPESMATEPGEVKPSLSGDSQLLLVQPQPQPQPSSLQLQPPLRLPGQQQQQVSLLHTAGGGSHGQLGSGSSSEASSVPHLLAQPSVSLGDQPGSMTQNLLGPQQPMLERPMQNNTGPQPPKPGPVLQSGQGLPGVGIMPTVGQLRAQLQGVLAKNPQLRHLSPQQQQQLQALLMQRQLQQSQAVRQTPPYQEPGTQTSPLQGLLGCQPQLGGFPGPQTGPLQELGAGPRPQGPPRLPAPPGALSTGPVLGPVHPTPPPSSPQEPKRPSQLPSPSSQLPTEAQLPPTHPGTPKPQGPTLEPPPGRVSPAAAQLADTLFSKGLGPWDPPDNLAETQKPEQSSLVPGHLDQVNGQVVPEASQLSIKQEPREEPCALGAQSVKREANGEPIGAPGTSNHLLLAGPRSEAGHLLLQKLLRAKNVQLSTGRGSEGLRAEINGHIDSKLAGLEQKLQGTPSNKEDAAARKPLTPKPKRVQKASDRLVSSRKKLRKEDGVRASEALLKQLKQELSLLPLTEPAITANFSLFAPFGSGCPVNGQSQLRGAFGSGALPTGPDYYSQLLTKNNLSNPPTPPSSLPPTPPPSVQQKMVNGVTPSEELGEHPKDAASARDSERALRDTSEVKSLDLLAALPTPPHNQTEDVRMESDEDSDSPDSIVPASSPESILGEEAPRFPHLGSGRWEQEDRALSPVIPLIPRASIPVFPDTKPYGALGLEVPGKLPVTTWEKGKGSEVSVMLTVSAAAAKNLNGVMVAVAELLSMKIPNSYEVLFPESPARAGTEPKKGEAEGPGGKEKGLEGKSPDTGPDWLKQFDAVLPGYTLKSQLDILSLLKQESPAPEPPTQHSYTYNVSNLDVRQLSAPPPEEPSPPPSPLAPSPASPPTEPLVELPTEPLAEPPVPSPLPLASSPESARPKPRARPPEEGEDSRPPRLKKWKGVRWKRLRLLLTIQKGSGRQEDEREVAEFMEQLGTALRPDKVPRDMRRCCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGGALMNVEVALHRGLLTKCSLCQRTGATSSCNRMRCPNVYHFACAIRAKCMFFKDKTMLCPMHKIKGPCEQELSSFAVFRRVYIERDEVKQIASIIQRGERLHMFRVGGLVFHAIGQLLPHQMADFHSATALYPVGYEATRIYWSLRTNNRRCCYRCSIGENNGRPEFVIKVIEQGLEDLVFTDASPQAVWNRIIEPVAAMRKEADMLRLFPEYLKGEELFGLTVHAVLRIAESLPGVESCQNYLFRYGRHPLMELPLMINPTGCARSEPKILTHYKRPHTLNSTSMSKAYQSTFTGETNTPYSKQFVHSKSSQYRRLRTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEVANRREKIYEEQNRGIYMFRINNEHVIDATLTGGPARYINHSCAPNCVAEVVTFDKEDKIIIISSRRIPKGEELTYDYQFDFEDDQHKIPCHCGAWNCRKWMN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O14686","disprot_id":"DP01676","ncbi_taxon_id":9606,"regions_counter":3,"creator":"smribeiro","regions":[{"start":4210,"end":4280,"reference_id":"30400675","reference_source":"pmid","reference_html":"Disordered Regions of Mixed Lineage Leukemia 4 (MLL4) Protein Are Capable of RNA Binding.  <i> Szabó B, Murvai N, Abukhairan R, Schád É, Kardos J, Szeder B, Buday L, Tantos Á. </i> Int J Mol Sci, 2018","date":"2023-08-26T21:22:14.689Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01676r003","statement":[{"text":"MLL4 4210–4280 has a more pronounced disorder tendency, as demonstrated by the IUPred profile and is devoid of any predicted ANCHOR binding sites (Figure 1E). Its sequence contains a significant portion of glutamines (Figure 1D), but it does not contain Q stretches longer than 4 residues. Far-UV CD measurements confirmed the disorder predictions,","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:51:42.311Z"}}],"released":"2018_11","uniref100":"UniRef100_O14686","date":"2018-08-07T11:47:51.000Z","acc":"O14686","name":"Histone-lysine N-methyltransferase 2D","length":5537,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins","Condensates-related proteins"],"UniParc":"UPI0000EE84D6","genes":[{"name":{"value":"KMT2D"},"synonyms":[{"value":"ALR"},{"value":"MLL2"},{"value":"MLL4"}]}],"disorder_content":0.012822828246342784,"disprot_consensus":{"full":[{"start":4210,"end":4280,"type":"D"}],"Structural state":[{"start":4210,"end":4280,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03247","name":"Prothymosin/parathymosin family","start":2,"end":107}]},"uniref50":"UniRef50_P06454","sequence":"MSDAAVDTSSEITTKDLKEKKEVVEEAENGRDAPANGNAENEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAESATGKRAAEDDEDDDVDTKKQKTDEDD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P06454","disprot_id":"DP01677","ncbi_taxon_id":9606,"regions_counter":18,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":111,"region_id":"DP01677r002","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Natively unfolded human prothymosin alpha adopts partially folded collapsed conformation at acidic pH. <i> Uversky VN, Gillespie JR, Millett IS, Khodyakova AV, Vasiliev AM, Chernovskaya TV, Vasilenko RN, Kozlovskaya GD, Dolgikh DA, Fink AL, Doniach S, Abramov VM. </i> Biochemistry, 1999","statement":[{"text":"As shown in Figure 6A, the 1H NMR spectrum of prothymosin at pH 8.0 was characteristic of a highly denatured protein. The resonances were sharp (indicating a high degree of rapid local segmental motion), the amide proton resonances were weak in intensity (indicating little regular hydrogen bonding due to hydrogen exchange with bulk solvent), and the spectrum was poorly dispersed.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-09-01T18:37:37.085Z","reference_source":"pmid","term_name":"disorder","reference_id":"10555983","ec_go":"EXP","disprot_namespace":"Structural state","conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":8}]},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":111,"term_name":"disorder to order","released":"2022_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Natively unfolded human prothymosin alpha adopts partially folded collapsed conformation at acidic pH. <i> Uversky VN, Gillespie JR, Millett IS, Khodyakova AV, Vasiliev AM, Chernovskaya TV, Vasilenko RN, Kozlovskaya GD, Dolgikh DA, Fink AL, Doniach S, Abramov VM. </i> Biochemistry, 1999","statement":[{"text":"As shown in Figure 6A, the 1H NMR spectrum of prothymosin at pH 8.0 was characteristic of a highly denatured protein. The resonances were sharp (indicating a high degree of rapid local segmental motion), the amide proton resonances were weak in intensity (indicating little regular hydrogen bonding due to hydrogen exchange with bulk solvent), and the spectrum was poorly dispersed. At pH 2.4 (Figure 6B), prothymosin still gave a spectrum characteristic of a denatured protein, although significant differences were observed as compared to pH 8.5. These differences included changes in the chemical shifts of some carbon-attached protons (which, being nonexchangeable, should not be dependent on the pH of the bulk solvent) and an increase in the line widths of some aliphatic resonances. These observations strongly suggest that a structural change had occurred, with the polypeptide becoming more compact and ordered.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10555983","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-09-01T18:36:59.168Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01677r003","ec_go":"EXP","disprot_namespace":"Structural transition","conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":2.4}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":111,"region_id":"DP01677r004","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Extreme disorder in an ultrahigh-affinity protein complex. <i> Borgia A, Borgia MB, Bugge K, Kissling VM, Heidarsson PO, Fernandes CB, Sottini A, Soranno A, Buholzer KJ, Nettels D, Kragelund BB, Best RB, Schuler B. </i> Nature, 2018","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-09-01T18:55:23.211Z","reference_source":"pmid","term_name":"disorder","reference_id":"29466338","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":" 1H,15N heteronuclear single quantum coherence (HSQC) spectra of the individual proteins exhibit low dispersion of the 1H chemical shifts, as expected for IDPs14,21-23 (Fig. 1e,f).","type":"Article"}]},{"term_namespace":"Molecular function","interaction_partner":[{"db":"UniProt","id":"P07305"}],"ec_ontology":"ECO","end":111,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_source":"pmid","curator_orcid":"0000-0002-3414-4972","curator_id":"stama","released":"2022_03","term_ontology":"GO","curator_name":"Stella Tamana","reference_id":"29466338","statement":[{"text":"ProTα acts as a linker histone chaperone by interacting with H1 and increasing its mobility in the nucleus. Here we show that ProTα and H1 bind to one another with very high affinity, but that both proteins fully retain their structural disorder.","type":"Curator statement"}],"reference_html":"Extreme disorder in an ultrahigh-affinity protein complex. <i> Borgia A, Borgia MB, Bugge K, Kissling VM, Heidarsson PO, Fernandes CB, Sottini A, Soranno A, Buholzer KJ, Nettels D, Kragelund BB, Best RB, Schuler B. </i> Nature, 2018","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","version":4,"region_id":"DP01677r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-01T19:05:21.701Z"}},{"start":15,"end":110,"reference_id":"34439840","reference_source":"pmid","reference_html":"Insight into Calcium-Binding Motifs of Intrinsically Disordered Proteins. <i> Newcombe EA, Fernandes CB, Lundsgaard JE, Brakti I, Lindorff-Larsen K, Langkilde AE, Skriver K, Kragelund BB. </i> Biomolecules, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007740","ec_ontology":"ECO","ec_name":"small molecule detection assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"ChEBI","id":"3312","partner_start":null,"partner_end":null}],"region_id":"DP01677r006","statement":[{"text":"We found ProTα to interact with calcium at micromolar affinity (~70 μM; Figure 1H).","type":"Results"},{"text":"This is reflected in its affinity for calcium and a greater number of calcium binding sites, with ProTα interacting with ~10 calcium ions (Figure 1I), the same stoichiometry as was previously reported [44].","type":"Results"},{"text":"Given the high number, extensive spreading and overlapping ion binding regions in ProTα, the entire sequence could be annotated. Despite this fact, it is observable in figure 2 that the first 15 residues of the N-terminus do not follow chemical shift upon calcium binding. Therefore, they are excluded. ","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-07T13:14:35.408Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":15,"end":110,"reference_id":"34439840","reference_source":"pmid","reference_html":"Insight into Calcium-Binding Motifs of Intrinsically Disordered Proteins. <i> Newcombe EA, Fernandes CB, Lundsgaard JE, Brakti I, Lindorff-Larsen K, Langkilde AE, Skriver K, Kragelund BB. </i> Biomolecules, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"ChEBI","id":"3312","partner_start":null,"partner_end":null}],"region_id":"DP01677r007","statement":[{"text":"The NMR peaks from the highly acidic stretch overlap and addition of calcium led to large changes in chemical shifts, meaning that we could not follow all individual peaks and quantify their CSPs (regions indicated by red in Figure 1E).","type":"Results"},{"text":"Given the high number, extensive spreading and overlapping ion binding regions in ProTα, the entire sequence could be annotated. Despite this fact, it is observable in figure 2 that the first 15 residues of the N-terminus do not follow chemical shift upon calcium binding. Therefore, they are excluded. ","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-07T13:14:28.116Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":111,"reference_id":"10555983","reference_source":"pmid","reference_html":"Natively unfolded human prothymosin alpha adopts partially folded collapsed conformation at acidic pH. <i> Uversky VN, Gillespie JR, Millett IS, Khodyakova AV, Vasiliev AM, Chernovskaya TV, Vasilenko RN, Kozlovskaya GD, Dolgikh DA, Fink AL, Doniach S, Abramov VM. </i> Biochemistry, 1999","date":"2022-09-01T18:27:08.365Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP01677r008","statement":[{"text":"The inset to Figure 2 shows that at pH 7.5 ProTα is characterized by a far-UV CD spectrum, which is typical of unfolded proteins, but at pH 2.5 a considerable rearrangement of the spectrum is observed.","type":"Results"}],"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7}]},{"start":1,"end":111,"reference_id":"10555983","reference_source":"pmid","reference_html":"Natively unfolded human prothymosin alpha adopts partially folded collapsed conformation at acidic pH. <i> Uversky VN, Gillespie JR, Millett IS, Khodyakova AV, Vasiliev AM, Chernovskaya TV, Vasilenko RN, Kozlovskaya GD, Dolgikh DA, Fink AL, Doniach S, Abramov VM. </i> Biochemistry, 1999","date":"2022-09-01T18:28:01.239Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP01677r009","statement":[{"text":"The inset to Figure 2 shows that at pH 7.5 ProTα is characterized by a far-UV CD spectrum, which is typical of unfolded proteins, but at pH 2.5 a considerable rearrangement of the spectrum is observed.","type":"Results"},{"text":"Such far-UV CD spectral changes can be explained by the appearance of some α-helix in the protein at low pH ( 45, 46)","type":"Results"}],"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":2.5}]},{"start":1,"end":111,"reference_id":"10555983","reference_source":"pmid","reference_html":"Natively unfolded human prothymosin alpha adopts partially folded collapsed conformation at acidic pH. <i> Uversky VN, Gillespie JR, Millett IS, Khodyakova AV, Vasiliev AM, Chernovskaya TV, Vasilenko RN, Kozlovskaya GD, Dolgikh DA, Fink AL, Doniach S, Abramov VM. </i> Biochemistry, 1999","date":"2022-09-01T18:26:38.599Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005632","ec_ontology":"ECO","ec_name":"fluorescence anisotropy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":5}],"region_id":"DP01677r010","statement":[{"text":" The inset to Figure 3 shows that in the case of ProTα a decrease in pH leads to considerable changes in ANS fluorescence (compare curves 1 and 2), reflecting the pH-induced transformation to the partially folded compact conformation. The formation of this intermediate is reflected in the pH dependence of the ANS fluorescence intensity (see Figure 3). The pH dependence of free ANS is also presented for comparison. It follows from Figure 3 that the transition from unfolded to partially folded conformation takes place between pH 5.5 and pH 3.5","type":"Results"}]},{"start":1,"end":111,"reference_id":"10555983","reference_source":"pmid","reference_html":"Natively unfolded human prothymosin alpha adopts partially folded collapsed conformation at acidic pH. <i> Uversky VN, Gillespie JR, Millett IS, Khodyakova AV, Vasiliev AM, Chernovskaya TV, Vasilenko RN, Kozlovskaya GD, Dolgikh DA, Fink AL, Doniach S, Abramov VM. </i> Biochemistry, 1999","date":"2022-09-01T18:26:55.884Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005632","ec_ontology":"ECO","ec_name":"fluorescence anisotropy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7}],"region_id":"DP01677r011","statement":[{"text":" The inset to Figure 3 shows that in the case of ProTα a decrease in pH leads to considerable changes in ANS fluorescence (compare curves 1 and 2), reflecting the pH-induced transformation to the partially folded compact conformation. The formation of this intermediate is reflected in the pH dependence of the ANS fluorescence intensity (see Figure 3). The pH dependence of free ANS is also presented for comparison. It follows from Figure 3 that the transition from unfolded to partially folded conformation takes place between pH 5.5 and pH 3.5","type":"Results"}]},{"start":1,"end":111,"reference_id":"10555983","reference_source":"pmid","reference_html":"Natively unfolded human prothymosin alpha adopts partially folded collapsed conformation at acidic pH. <i> Uversky VN, Gillespie JR, Millett IS, Khodyakova AV, Vasiliev AM, Chernovskaya TV, Vasilenko RN, Kozlovskaya GD, Dolgikh DA, Fink AL, Doniach S, Abramov VM. </i> Biochemistry, 1999","date":"2022-09-01T18:29:53.935Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7}],"region_id":"DP01677r012","statement":[{"text":"The results of chromatographic analysis are presented in Table 2. It is evident that the hydrodynamic dimensions of ProTα at neutral pH are close to those measured in the presence of 8 M urea. The small difference between the two values is due to swelling of the unfolded polypeptide chain in a good solvent ( 20). Both values are virtually indistinguishable from RS, calculated for the completely unfolded protein with a molecular mass of 12.21 kDa.","type":"Results"}]},{"start":1,"end":111,"reference_id":"10555983","reference_source":"pmid","reference_html":"Natively unfolded human prothymosin alpha adopts partially folded collapsed conformation at acidic pH. <i> Uversky VN, Gillespie JR, Millett IS, Khodyakova AV, Vasiliev AM, Chernovskaya TV, Vasilenko RN, Kozlovskaya GD, Dolgikh DA, Fink AL, Doniach S, Abramov VM. </i> Biochemistry, 1999","date":"2022-09-01T18:30:30.516Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":2.5}],"region_id":"DP01677r013","statement":[{"text":"The results of chromatographic analysis are presented in Table 2. It is evident that the hydrodynamic dimensions of ProTα at neutral pH are close to those measured in the presence of 8 M urea. The small difference between the two values is due to swelling of the unfolded polypeptide chain in a good solvent ( 20). Both values are virtually indistinguishable from RS, calculated for the completely unfolded protein with a molecular mass of 12.21 kDa.","type":"Results"},{"text":"Table 2 shows that a decrease in pH leads to a pronounced decrease of the ProTα hydrodynamic dimension. It should be emphasized that the RS value determined for ProTα at pH 2.5 is still far from that expected for a globular protein of 12 kDa.","type":"Results"}]},{"start":1,"end":111,"reference_id":"10555983","reference_source":"pmid","reference_html":"Natively unfolded human prothymosin alpha adopts partially folded collapsed conformation at acidic pH. <i> Uversky VN, Gillespie JR, Millett IS, Khodyakova AV, Vasiliev AM, Chernovskaya TV, Vasilenko RN, Kozlovskaya GD, Dolgikh DA, Fink AL, Doniach S, Abramov VM. </i> Biochemistry, 1999","date":"2022-09-01T18:33:48.763Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":2.5}],"region_id":"DP01677r014","statement":[{"text":"The profile of the Kratky plot at neutral pH is typical for a random coil conformation, whereas at pH 2.5 considerable change in the shape of the scattering curves is detected, reflecting the presence of more ordered conformation under such conditions.","type":"Results"}]},{"start":1,"end":111,"reference_id":"10555983","reference_source":"pmid","reference_html":"Natively unfolded human prothymosin alpha adopts partially folded collapsed conformation at acidic pH. <i> Uversky VN, Gillespie JR, Millett IS, Khodyakova AV, Vasiliev AM, Chernovskaya TV, Vasilenko RN, Kozlovskaya GD, Dolgikh DA, Fink AL, Doniach S, Abramov VM. </i> Biochemistry, 1999","date":"2022-09-01T18:34:24.925Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7.5}],"region_id":"DP01677r015","statement":[{"text":"The profile of the Kratky plot at neutral pH is typical for a random coil conformation, whereas at pH 2.5 considerable change in the shape of the scattering curves is detected, reflecting the presence of more ordered conformation under such conditions.","type":"Results"}]},{"start":1,"end":111,"reference_id":"10555983","reference_source":"pmid","reference_html":"Natively unfolded human prothymosin alpha adopts partially folded collapsed conformation at acidic pH. <i> Uversky VN, Gillespie JR, Millett IS, Khodyakova AV, Vasiliev AM, Chernovskaya TV, Vasilenko RN, Kozlovskaya GD, Dolgikh DA, Fink AL, Doniach S, Abramov VM. </i> Biochemistry, 1999","date":"2022-09-01T18:50:18.890Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006313","ec_ontology":"ECO","ec_name":"urea-induced protein unfolding evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP01677r016","statement":[{"text":"Figure 7 shows that the denaturant-induced unfolding of the ProTα acid state represents a very broad transition characterized by the absence of the sigmoid shape, typical of the unfolding of native and molten globule conformations ( 50, 51).","type":"Results"}]},{"start":1,"end":111,"reference_id":"29466338","reference_source":"pmid","reference_html":"Extreme disorder in an ultrahigh-affinity protein complex. <i> Borgia A, Borgia MB, Bugge K, Kissling VM, Heidarsson PO, Fernandes CB, Sottini A, Soranno A, Buholzer KJ, Nettels D, Kragelund BB, Best RB, Schuler B. </i> Nature, 2018","date":"2022-09-01T18:55:32.255Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP01677r017","statement":[{"text":"The CD spectra of unbound ProTα and H1 reflect the low secondary structure content of the individual IDPs, except for the small helix-turn-helix domain of H113,19,20 (Fig. 1c).","type":"Article"}]},{"start":1,"end":111,"reference_id":"29466338","reference_source":"pmid","reference_html":"Extreme disorder in an ultrahigh-affinity protein complex. <i> Borgia A, Borgia MB, Bugge K, Kissling VM, Heidarsson PO, Fernandes CB, Sottini A, Soranno A, Buholzer KJ, Nettels D, Kragelund BB, Best RB, Schuler B. </i> Nature, 2018","date":"2022-09-01T19:04:09.105Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042393","term_name":"histone binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P07305","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01677r018","statement":[{"text":"The dominant contribution to the interaction with ProTα stems from the unstructured C-terminal part of H1, which alone binds with picomolar affinity. The N-terminal half and the isolated globular domain of H1 also bind ProTα, but with much lower affinity (Fig. 2b). At least four isolated globular domains can bind to ProTα at the same time, with modest chemical shift changes (Extended Data Fig. 1), suggesting the absence of a specific binding interface.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a histone, any of a group of water-soluble proteins found in association with the DNA of eukaroytic chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in nonspecific suppression of gene activity.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_P06454","date":"2018-08-07T11:56:20.000Z","acc":"P06454","name":"Prothymosin alpha","length":111,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000136F25","genes":[{"name":{"value":"PTMA"},"synonyms":[{"value":"TMSA"}]}],"alphafold_very_low_content":0.02702702702702703,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":111,"type":"T"}],"Structural state":[{"start":1,"end":111,"type":"D"}],"Structural transition":[{"start":1,"end":111,"type":"T"}],"Molecular function":[{"start":1,"end":111,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00018","name":"SH3 domain","start":984,"end":1028},{"id":"PF00435","name":"Spectrin repeat","start":53,"end":155},{"id":"PF00435","name":"Spectrin repeat","start":159,"end":261},{"id":"PF00435","name":"Spectrin repeat","start":265,"end":367},{"id":"PF00435","name":"Spectrin repeat","start":371,"end":474},{"id":"PF00435","name":"Spectrin repeat","start":477,"end":580},{"id":"PF00435","name":"Spectrin repeat","start":583,"end":685},{"id":"PF00435","name":"Spectrin repeat","start":688,"end":790},{"id":"PF00435","name":"Spectrin repeat","start":794,"end":896},{"id":"PF00435","name":"Spectrin repeat","start":900,"end":969},{"id":"PF00435","name":"Spectrin repeat","start":1086,"end":1179},{"id":"PF00435","name":"Spectrin repeat","start":1185,"end":1287},{"id":"PF00435","name":"Spectrin repeat","start":1290,"end":1392},{"id":"PF00435","name":"Spectrin repeat","start":1396,"end":1497},{"id":"PF00435","name":"Spectrin repeat","start":1501,"end":1605},{"id":"PF00435","name":"Spectrin repeat","start":1608,"end":1711},{"id":"PF00435","name":"Spectrin repeat","start":1714,"end":1817},{"id":"PF00435","name":"Spectrin repeat","start":1820,"end":1926},{"id":"PF00435","name":"Spectrin repeat","start":1929,"end":2033},{"id":"PF00435","name":"Spectrin repeat","start":2044,"end":2146},{"id":"PF00435","name":"Spectrin repeat","start":2158,"end":2258},{"id":"PF08726","name":"Ca2+ insensitive EF hand","start":2350,"end":2418}],"gene3D":[{"start":51,"end":155,"id":"1.20.58.60","name":"1.20.58.60"},{"start":582,"end":684,"id":"1.20.58.60","name":"1.20.58.60"},{"start":1277,"end":1388,"id":"1.20.58.60","name":"1.20.58.60"},{"start":2154,"end":2264,"id":"1.20.58.60","name":"1.20.58.60"},{"start":1605,"end":1713,"id":"1.20.58.60","name":"1.20.58.60"},{"start":685,"end":791,"id":"1.20.58.60","name":"1.20.58.60"},{"start":2352,"end":2419,"id":"1.10.238.10","name":"EF-hand"},{"start":2265,"end":2350,"id":"1.10.238.10","name":"EF-hand"},{"start":1391,"end":1493,"id":"1.20.58.60","name":"1.20.58.60"},{"start":19,"end":50,"id":"1.20.5.170","name":"1.20.5.170"},{"start":984,"end":1036,"id":"2.30.30.40","name":"SH3 Domains"},{"start":371,"end":473,"id":"1.20.58.60","name":"1.20.58.60"},{"start":2040,"end":2153,"id":"1.20.58.60","name":"1.20.58.60"},{"start":1715,"end":1816,"id":"1.20.58.60","name":"1.20.58.60"},{"start":1498,"end":1604,"id":"1.20.58.60","name":"1.20.58.60"},{"start":1817,"end":1920,"id":"1.20.58.60","name":"1.20.58.60"},{"start":474,"end":581,"id":"1.20.58.60","name":"1.20.58.60"}]},"uniref50":"UniRef50_P02549","sequence":"MEQFPKETVVESSGPKVLETAEEIQERRQEVLTRYQSFKERVAERGQKLEDSYHLQVFKRDADDLGKWIMEKVNILTDKSYEDPTNIQGKYQKHQSLEAEVQTKSRLMSELEKTREERFTMGHSAHEETKAHIEELRHLWDLLLELTLEKGDQLLRALKFQQYVQECADILEWIGDKEAIATSVELGEDWERTEVLHKKFEDFQVELVAKEGRVVEVNQYANECAEENHPDLPLIQSKQNEVNAAWERLRGLALQRQKALSNAANLQRFKRDVTEAIQWIKEKEPVLTSEDYGKDLVASEGLFHSHKGLERNLAVMSDKVKELCAKAEKLTLSHPSDAPQIQEMKEDLVSSWEHIRALATSRYEKLQATYWYHRFSSDFDELSGWMNEKTAAINADELPTDVAGGEVLLDRHQQHKHEIDSYDDRFQSADETGQDLVNANHEASDEVREKMEILDNNWTALLELWDERHRQYEQCLDFHLFYRDSEQVDSWMSRQEAFLENEDLGNSLGSAEALLQKHEDFEEAFTAQEEKIITVDKTATKLIGDDHYDSENIKAIRDGLLARRDALREKAATRRRLLKESLLLQKLYEDSDDLKNWINKKKKLADDEDYKDIQNLKSRVQKQQVFEKELAVNKTQLENIQKTGQEMIEGGHYASDNVTTRLSEVASLWEELLEATKQKGTQLHEANQQLQFENNAEDLQRWLEDVEWQVTSEDYGKGLAEVQNRLRKHGLLESAVAARQDQVDILTDLAAYFEEIGHPDSKDIRARQESLVCRFEALKEPLATRKKKLLDLLHLQLICRDTEDEEAWIQETEPSATSTYLGKDLIASKKLLNRHRVILENIASHEPRIQEITERGNKMVEEGHFAAEDVASRVKSLNQNMESLRARAARRQNDLEANVQFQQYLADLHEAETWIREKEPIVDNTNYGADEEAAGALLKKHEAFLLDLNSFGDSMKALRNQANACQQQQAAPVEGVAGEQRVMALYDFQARSPREVTMKKGDVLTLLSSINKDWWKVEAADHQGIVPAVYVRRLAHDEFPMLPQRRREEPGNITQRQEQIENQYRSLLDRAEERRRRLLQRYNEFLLAYEAGDMLEWIQEKKAENTGVELDDVWELQKKFDEFQKDLNTNEPRLRDINKVADDLLFEGLLTPEGAQIRQELNSRWGSLQRLADEQRQLLGSAHAVEVFHREADDTKEQIEKKCQALSAADPGSDLFSVQALQRRHEGFERDLVPLGDKVTILGETAERLSESHPDATEDLQRQKMELNEAWEDLQGRTKDRKESLNEAQKFYLFLSKARDLQNWISSIGGMVSSQELAEDLTGIEILLERHQEHRADMEAEAPTFQALEDFSAELIDSGHHASPEIEKKLQAVKLERDDLEKAWEKRKKILDQCLELQMFQGNCDQVESWMVARENSLRSDDKSSLDSLEALMKKRDDLDKAITAQEGKITDLEHFAESLIADEHYAKEEIATRLQRVLDRWKALKAQLIDERTKLGDYANLKQFYRDLEELEEWISEMLPTACDESYKDATNIQRKYLKHQTFAHEVDGRSEQVHGVINLGNSLIECSACDGNEEAMKEQLEQLKEHWDHLLERTNDKGKKLNEASRQQRFNTSIRDFEFWLSEAETLLAMKDQARDLASAGNLLKKHQLLEREMLAREDALKDLNTLAEDLLSSGTFNVDQIVKKKDNVNKRFLNVQELAAAHHEKLKEAYALFQFFQDLDDEESWIEEKLIRVSSQDYGRDLQGVQNLLKKHKRLEGELVAHEPAIQNVLDMAEKLKDKAAVGQEEIQLRLAQFVEHWEKLKELAKARGLKLEESLEYLQFMQNAEEEEAWINEKNALAVRGDCGDTLAATQSLLMKHEALENDFAVHETRVQNVCAQGEDILNKVLQEESQNKEISSKIEALNEKTPSLAKAIAAWKLQLEDDYAFQEFNWKADVVEAWIADKETSLKTNGNGADLGDFLTLLAKQDTLDASLQSFQQERLPEITDLKDKLISAQHNQSKAIEERYAALLKRWEQLLEASAVHRQKLLEKQLPLQKAEDLFVEFAHKASALNNWCEKMEENLSEPVHCVSLNEIRQLQKDHEDFLASLARAQADFKCLLELDQQIKALGVPSSPYTWLTVEVLERTWKHLSDIIEEREQELQKEEARQVKNFEMCQEFEQNASTFLQWILETRAYFLDGSLLKETGTLESQLEANKRKQKEIQAMKRQLTKIVDLGDNLEDALILDIKYSTIGLAQQWDQLYQLGLRMQHNLEQQIQAKDIKGVSEETLKEFSTIYKHFDENLTGRLTHKEFRSCLRGLNYYLPMVEEDEHEPKFEKFLDAVDPGRKGYVSLEDYTAFLIDKESENIKSSDEIENAFQALAEGKSYITKEDMKQALTPEQVSFCATHMQQYMDPRGRSHLSGYDYVGFTNSYFGN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P02549","disprot_id":"DP01700","ncbi_taxon_id":9606,"regions_counter":1,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":20,"region_id":"DP01700r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structural studies on human erythrocyte alpha-spectrin tetramerization site. <i> Park S, Caffrey MS, Johnson ME, Fung LW. </i> J Biol Chem, 2003","statement":[{"text":"We have determined the solution NMR structure of a recombinant peptide that consists of the first 156 residues of erythroid α-spectrin. The first 20 residues preceding the first helix (helix C′) are in a disordered conformation.","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"akajava","start":1,"term_ontology":"IDPO","curator_name":"Andrey V Kajava","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-2342-6886","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1OWA"}],"reference_id":"12672815","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-26T13:43:33.796Z"}}],"released":"2018_11","uniref100":"UniRef100_P02549","date":"2018-08-07T13:05:04.000Z","acc":"P02549","name":"Spectrin alpha chain, erythrocytic 1","length":2419,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000161B48","genes":[{"name":{"value":"SPTA1"},"synonyms":[{"value":"SPTA"}]}],"alphafold_very_low_content":0.033484911120297646,"disorder_content":0.00826787928896238,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"D"}],"Structural state":[{"start":1,"end":20,"type":"D"}]}},{"features":{"pfam":[{"id":"PF16000","name":"CARMIL C-terminus","start":786,"end":1079},{"id":"PF17888","name":"Carmil pleckstrin homology domain","start":26,"end":119},{"id":"PF29265","name":"CARMIL family, LRR domain","start":156,"end":666}],"gene3D":[{"start":159,"end":664,"id":"3.80.10.10","name":"Ribonuclease Inhibitor"},{"start":1,"end":114,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"}]},"uniref50":"UniRef50_Q5VZK9","sequence":"MTEESSDVPRELIESIKDVIGRKIKISVKKKVKLEVKGDKVENKVLVLTSCRAFLVTARIPTKLELTFSYLEIHGVVCSKSAQMIVETEKCSISMKMASPEDVSEVLAHIGTCLRKIFPGLSPVRIMKKVSMEPSERLASLQALWDSQTVAEQGPCGGFSQMYACVCDWLGFSYREEVQWDVDTIYLTQDTRELNLQDFSHLDHRDLIPIIAALEYNQWFTKLSSKDLKLSTDVCEQILRVVSRSNRLEELVLENAGLRTDFAQKLASALAHNPNSGLHTINLAGNPLEDRGVSSLSIQFAKLPKGLKHLNLSKTSLSPKGVNSLSQSLSANPLTASTLVHLDLSGNVLRGDDLSHMYNFLAQPNAIVHLDLSNTECSLDMVCGALLRGCLQYLAVLNLSRTVFSHRKGKEVPPSFKQFFSSSLALMHINLSGTKLSPEPLKALLLGLACNHNLKGVSLDLSNCELRSGGAQVLEGCIAEIHNITSLDISDNGLESDLSTLIVWLSKNRSIQHLALGKNFNNMKSKNLTPVLDNLVQMIQDEESPLQSLSLADSKLKTEVTIIINALGSNTSLTKVDISGNGMGDMGAKMLAKALQINTKLRTVIWDKNNITAQGFQDIAVAMEKNYTLRFMPIPMYDASQALKTNPEKTEDALQKIENYLLRNHETRKYLQEQAYRLQQGIVTSTTQQMIDRICVKVQDHLNSLRNCGGDAIQEDLKSAERLMRDAKNSKTLLPNLYHVGGASWAGASGLLSSPIQETLESMAGEVTRVVDEQLKALLESMVDAAENLCPNVMKKAHIRQDLIHASTEKISIPRTFVKNVLLEQSGIDILNKISEVKLTVASFLSDRIVDEILDALSHCHHKLADHFSRRGKTLPQQESLEIELAEEKPVKRSIITVEELTEIERLEDLDTCMMTPKSKRKSIHSRMLRPVSRAFEMEFDLDKALEEVPIHIEDPPFPSLRQEKRSSGFISELPSEEGKKLEHFTKLRPKRNKKQQPTQAAVCAANIVSQDGEQNGLMGRVDEGVDEFFTKKVTKMDSKKWSTRGSESHELNEGGDEKKKRDSRKSSGFLNLIKSRSKSERPPTILMTEEPSSPKGAVRSPPVDCPRKDTKAAEHNGNSERIEEIKTPDSFEESQGEEIGKVERSDSKSSPQAGRRYGVQVMGSGLLAEMKAKQEKRAACAQKKLGNDAVSQDSSSPALSGVERSDGGGAVPKLHPGLPENRFGLGTPEKNTKAEPKAEAGSRSRSSSSTPTSPKPLLQSPKPSLAARPVIPQKPRTASRPDDIPDSPSSPKVALLPPVLKKVPSDKERDGQSSPQPSPRTFSQEVSRRSWGQQAQEYQEQKQRSSSKDGHQGSKSNDSGEEAEKEFIFV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q5VZK9","disprot_id":"DP01701","ncbi_taxon_id":9606,"regions_counter":1,"creator":"aelofsson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1020,"region_id":"DP01701r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural characterization of a capping protein interaction motif defines a family of actin filament regulators. <i> Hernandez-Valladares M, Kim T, Kannan B, Tung A, Aguda AH, Larsson M, Cooper JA, Robinson RC. </i> Nat Struct Mol Biol, 2010","term_id":"IDPO:0000002","curator_id":"ahatos","start":1005,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3LK2"}],"reference_id":"20357771","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q5VZK9","date":"2018-08-07T13:06:30.000Z","acc":"Q5VZK9","name":"F-actin-uncapping protein LRRC16A","length":1371,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00004588AB","genes":[{"name":{"value":"CARMIL1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16054028","url":"http://www.ncbi.nlm.nih.gov/pubmed/16054028","alternativeUrl":"https://europepmc.org/abstract/MED/16054028"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:21581","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:21581"}}]},"synonyms":[{"value":"CARMIL","evidences":[{"code":"ECO:0000250","source":{"name":"UniProtKB","id":"Q95VZ3","url":"https://www.uniprot.org/uniprot/Q95VZ3"}}]},{"value":"LRRC16"},{"value":"LRRC16A"}]}],"alphafold_very_low_content":0.36980306345733044,"disorder_content":0.011670313639679067,"disprot_consensus":{"full":[{"start":1005,"end":1020,"type":"D"}],"Structural state":[{"start":1005,"end":1020,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01423","name":"LSM domain","start":9,"end":72}],"gene3D":[{"start":1,"end":84,"id":"2.30.30.100","name":"2.30.30.100"}]},"uniref50":"UniRef50_P62318","sequence":"MSIGVPIKVLHEAEGHIVTCETNTGEVYRGKLIEAEDNMNCQMSNITVTYRDGRVAQLEQVYIRGSKIRFLILPDMLKNAPMLKSMKNKNQGSGAGRGKAAILKAQVAARGRGRGMGRGNIFQKRR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P62318","disprot_id":"DP01704","ncbi_taxon_id":9606,"regions_counter":1,"creator":"jlamb","regions":[{"region_id":"DP01704r001","ec_ontology":"ECO","end":126,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":82,"version":3,"statement":[{"text":"The Sm protein D2 contains a particularly long N-terminal extension whereas B, D1 and D3 have long C-terminal extensions.","type":"Discussion"}],"term_name":"disorder","reference_html":"Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution. <i> Pomeranz Krummel DA, Oubridge C, Leung AK, Li J, Nagai K. </i> Nature, 2009","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19325628","date":"2023-08-29T20:47:24.074Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3CW1"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS000080E05C_9606"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P09234"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08621"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62308"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62304"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62306"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62316"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62314"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P14678"}]}],"released":"2018_11","uniref100":"UniRef100_P62318","date":"2018-08-07T13:15:24.000Z","acc":"P62318","name":"Small nuclear ribonucleoprotein Sm D3","length":126,"organism":"Homo sapiens","dataset":["RNA-binding proteins"],"UniParc":"UPI0000021859","genes":[{"name":{"value":"SNRPD3"}}],"alphafold_very_low_content":0.07142857142857142,"disorder_content":0.35714285714285715,"disprot_consensus":{"full":[{"start":82,"end":126,"type":"D"}],"Structural state":[{"start":82,"end":126,"type":"D"}]}},{"features":{"pfam":[{"id":"PF16274","name":"Qua1 domain","start":102,"end":153},{"id":"PF16568","name":"Tyrosine-rich domain of Sam68","start":366,"end":415},{"id":"PF22675","name":"KHDC4/BBP-like, KH-domain type I","start":166,"end":232}],"gene3D":[{"start":97,"end":284,"id":"3.30.1370.10","name":"K Homology domain, type 1"}]},"uniref50":"UniRef50_Q07666","sequence":"MQRRDDPAARMSRSSGRSGSMDPSGAHPSVRQTPSRQPPLPHRSRGGGGGSRGGARASPATQPPPLLPPSATGPDATVGGPAPTPLLPPSATASVKMEPENKYLPELMAEKDSLDPSFTHAMQLLTAEIEKIQKGDSKKDDEENYLDLFSHKNMKLKERVLIPVKQYPKFNFVGKILGPQGNTIKRLQEETGAKISVLGKGSMRDKAKEEELRKGGDPKYAHLNMDLHVFIEVFGPPCEAYALMAHAMEEVKKFLVPDMMDDICQEQFLELSYLNGVPEPSRGRGVPVRGRGAAPPPPPVPRGRGVGPPRGALVRGTPVRGAITRGATVTRGVPPPPTVRGAPAPRARTAGIQRIPLPPPPAPETYEEYGYDDTYAEQSYEGYEGYYSQSQGDSEYYDYGHGEVQDSYEAYGQDDWNGTRPSLKAPPARPVKGAYREHPYGRY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q07666","disprot_id":"DP01705","ncbi_taxon_id":9606,"regions_counter":27,"creator":"aelofsson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":156,"region_id":"DP01705r001","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Structural basis for homodimerization of the Src-associated during mitosis, 68-kDa protein (Sam68) Qua1 domain. <i> Meyer NH, Tripsianes K, Vincendeau M, Madl T, Kateb F, Brack-Werner R, Sattler M. </i> J Biol Chem, 2010","statement":[{"text":"The 20 C-terminal amino acids (residues 136–156) do not exhibit any secondary structure. 15N R1 and R2 relaxation rates as well as {1H}-15N heteronuclear NOE data show that the C terminus is highly flexible, whereas the loop connecting the two helices has a slightly increased flexibility when compared with the helical segments (Fig. 2).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":136,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2023-12-13T17:46:08.806Z","reference_source":"pmid","term_name":"disorder","reference_id":"20610388","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"BMRB","id":"16969"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-13T18:08:28.962Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":378,"region_id":"DP01705r002","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Crystal structures of the armadillo repeat domain of adenomatous polyposis coli and its complex with the tyrosine-rich domain of Sam68. <i> Morishita EC, Murayama K, Kato-Murayama M, Ishizuka-Katsura Y, Tomabechi Y, Hayashi T, Terada T, Handa N, Shirouzu M, Akiyama T, Yokoyama S. </i> Structure, 2011","statement":[{"text":"We used the 55 residue fragment Sam68-YY for crystallization, but only residues 379–389 (Sam68-2) are visible in our electron density map (Figure S1B).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":365,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-12-13T17:00:42.420Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3QHE"}],"reference_id":"22000517","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P25054"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-13T17:48:09.715Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":419,"region_id":"DP01705r003","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Crystal structures of the armadillo repeat domain of adenomatous polyposis coli and its complex with the tyrosine-rich domain of Sam68. <i> Morishita EC, Murayama K, Kato-Murayama M, Ishizuka-Katsura Y, Tomabechi Y, Hayashi T, Terada T, Handa N, Shirouzu M, Akiyama T, Yokoyama S. </i> Structure, 2011","statement":[{"text":"We used the 55 residue fragment Sam68-YY for crystallization, but only residues 379–389 (Sam68-2) are visible in our electron density map (Figure S1B).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":390,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-12-13T16:57:11.678Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3QHE"}],"reference_id":"22000517","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P25054"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-13T17:50:52.061Z"}},{"start":1,"end":96,"reference_id":"36537190","reference_source":"pmid","reference_html":"Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions. <i> Malki I, Liepina I, Kogelnik N, Watmuff H, Robinson S, Lightfoot A, Gonchar O, Bottrill A, Fry AM, Dominguez C. </i> Nucleic Acids Res, 2022","date":"2024-04-04T17:20:44.010Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"BMRB","id":"51359"}],"region_id":"DP01705r007","statement":[{"text":"The N-terminal (residues 1–96) and C-terminal (residues 267–368) regions of Sam68 were expressed in E. coli in the presence of [15N]ammonium chloride and [13C]glucose before purification. The NMR spectra show that these regions are intrinsically disordered and 72% and 65% of the non-proline residue backbone resonances for the N- and C-terminal regions, respectively, could be unambiguously assigned (Figure 1B, C).","type":"Results"}]},{"start":267,"end":368,"reference_id":"36537190","reference_source":"pmid","reference_html":"Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions. <i> Malki I, Liepina I, Kogelnik N, Watmuff H, Robinson S, Lightfoot A, Gonchar O, Bottrill A, Fry AM, Dominguez C. </i> Nucleic Acids Res, 2022","date":"2024-04-04T17:20:58.430Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"BMRB","id":"51360"}],"region_id":"DP01705r008","statement":[{"text":"The N-terminal (residues 1–96) and C-terminal (residues 267–368) regions of Sam68 were expressed in E. coli in the presence of [15N]ammonium chloride and [13C]glucose before purification. The NMR spectra show that these regions are intrinsically disordered and 72% and 65% of the non-proline residue backbone resonances for the N- and C-terminal regions, respectively, could be unambiguously assigned (Figure 1B, C).","type":"Results"}]},{"start":30,"end":35,"reference_id":"36537190","reference_source":"pmid","reference_html":"Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions. <i> Malki I, Liepina I, Kogelnik N, Watmuff H, Robinson S, Lightfoot A, Gonchar O, Bottrill A, Fry AM, Dominguez C. </i> Nucleic Acids Res, 2022","date":"2024-04-04T17:25:37.874Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001202","ec_ontology":"ECO","ec_name":"in vitro protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":33,"end":33,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":317,"end":317,"position":"Specific residue"}],"region_id":"DP01705r009","statement":[{"text":"During the experiment, the resonance peaks of T33 and T317 shifted downfield in both 1H and 15N dimensions, a typical signature of serine or threonine phosphorylation (36) (Figure 2A, B). Resonances corresponding to other threonine and serine residues were not affected by the addition of Cdk1/cyclin B, indicating that only T33 and T317 were phosphorylated by Cdk1 in vitro. Incubation of the N-terminus with Cdk1 induced CSPs of residues surrounding T33 (notably H27, S29, R31, Q32, R35 and Q36) (Figure 2C), suggesting a possible conformational change upon T33 phosphorylation.","type":"Results"}]},{"start":316,"end":320,"reference_id":"36537190","reference_source":"pmid","reference_html":"Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions. <i> Malki I, Liepina I, Kogelnik N, Watmuff H, Robinson S, Lightfoot A, Gonchar O, Bottrill A, Fry AM, Dominguez C. </i> Nucleic Acids Res, 2022","date":"2024-04-04T18:10:55.393Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001202","ec_ontology":"ECO","ec_name":"in vitro protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":33,"end":33,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":317,"end":317,"position":"Specific residue"}],"region_id":"DP01705r010","statement":[{"text":"During the experiment, the resonance peaks of T33 and T317 shifted downfield in both 1H and 15N dimensions, a typical signature of serine or threonine phosphorylation (36) (Figure 2A, B). Resonances corresponding to other threonine and serine residues were not affected by the addition of Cdk1/cyclin B, indicating that only T33 and T317 were phosphorylated by Cdk1 in vitro.","type":"Results"}]},{"start":17,"end":21,"reference_id":"36537190","reference_source":"pmid","reference_html":"Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions. <i> Malki I, Liepina I, Kogelnik N, Watmuff H, Robinson S, Lightfoot A, Gonchar O, Bottrill A, Fry AM, Dominguez C. </i> Nucleic Acids Res, 2022","date":"2024-04-04T17:32:37.515Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001218","ec_ontology":"ECO","ec_name":"in vivo protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01705r011","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"},{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0291","entry_name":"HCT116wt"}],"statement":[{"text":"In terms of serine and threonine (S/T) phosphorylation, we observed phosphorylation of either S18 or S20 (S18/S20) and of either T33 or S35 (T33/S35) in HEK293T cells; and of either S18 or S20 and of either T33 or S35 and S113 in HCT116 cells (Table 1).","type":"Results"},{"text":"S18/S20 phosphorylation was observed in all stages of the cell cycle.","type":"Results"}]},{"start":32,"end":36,"reference_id":"36537190","reference_source":"pmid","reference_html":"Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions. <i> Malki I, Liepina I, Kogelnik N, Watmuff H, Robinson S, Lightfoot A, Gonchar O, Bottrill A, Fry AM, Dominguez C. </i> Nucleic Acids Res, 2022","date":"2024-04-04T17:33:22.567Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001218","ec_ontology":"ECO","ec_name":"in vivo protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01705r012","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"},{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0291","entry_name":"HCT116wt"}],"statement":[{"text":"In terms of serine and threonine (S/T) phosphorylation, we observed phosphorylation of either S18 or S20 (S18/S20) and of either T33 or S35 (T33/S35) in HEK293T cells; and of either S18 or S20 and of either T33 or S35 and S113 in HCT116 cells (Table 1).","type":"Results"}]},{"start":56,"end":60,"reference_id":"36537190","reference_source":"pmid","reference_html":"Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions. <i> Malki I, Liepina I, Kogelnik N, Watmuff H, Robinson S, Lightfoot A, Gonchar O, Bottrill A, Fry AM, Dominguez C. </i> Nucleic Acids Res, 2022","date":"2024-04-04T17:34:45.734Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001218","ec_ontology":"ECO","ec_name":"in vivo protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01705r013","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"Additionally, S58 and S70 were phosphorylated during G1. These two specific phosphorylation events could be mediated by Erk1 as previously suggested (7). Interestingly, we identified T33 and T317 phosphorylation in mitosis.","type":"Results"}]},{"start":58,"end":72,"reference_id":"36537190","reference_source":"pmid","reference_html":"Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions. <i> Malki I, Liepina I, Kogelnik N, Watmuff H, Robinson S, Lightfoot A, Gonchar O, Bottrill A, Fry AM, Dominguez C. </i> Nucleic Acids Res, 2022","date":"2024-04-04T17:34:55.112Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001218","ec_ontology":"ECO","ec_name":"in vivo protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01705r014","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"Additionally, S58 and S70 were phosphorylated during G1. These two specific phosphorylation events could be mediated by Erk1 as previously suggested (7). Interestingly, we identified T33 and T317 phosphorylation in mitosis.","type":"Results"}]},{"start":316,"end":320,"reference_id":"36537190","reference_source":"pmid","reference_html":"Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions. <i> Malki I, Liepina I, Kogelnik N, Watmuff H, Robinson S, Lightfoot A, Gonchar O, Bottrill A, Fry AM, Dominguez C. </i> Nucleic Acids Res, 2022","date":"2024-04-04T18:11:09.603Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001218","ec_ontology":"ECO","ec_name":"in vivo protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01705r015","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"Additionally, S58 and S70 were phosphorylated during G1. These two specific phosphorylation events could be mediated by Erk1 as previously suggested (7). Interestingly, we identified T33 and T317 phosphorylation in mitosis.","type":"Results"}]},{"start":10,"end":61,"reference_id":"36537190","reference_source":"pmid","reference_html":"Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions. <i> Malki I, Liepina I, Kogelnik N, Watmuff H, Robinson S, Lightfoot A, Gonchar O, Bottrill A, Fry AM, Dominguez C. </i> Nucleic Acids Res, 2022","date":"2024-04-04T17:48:16.626Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01705r016","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting RNA with sequence CUGGGUGACACACUAGCUAUAGCAUUAAAAGACCGAGCAAGU."}]}],"statement":[{"text":"Increasing the G8.5 molar ratio with the Sam68 N- and C-termini induced chemical shift perturbations, consistent with the formation of a complex between these regions and the RNA (Figure 3B, C). These results demonstrate that the Sam68 N- and C-terminal regions can bind RNA independently of the rest of the protein. Analysis of the titration data suggests that both domains bind the G.8 RNA with dissociation constants in the low micromolar range (1–10 μM for the N-terminus and 30–70 μM for the C-terminus) (Supplementary Figure S2), very similar to the affinity of the STAR domain for the same RNA sequence (18).","type":"Results"},{"text":"Analysis of the chemical shift mapping shows that RNA binding affects most residues of the N- and C-termini, in particular residues 10–61 for the N-terminus and 281–338 for the C-terminus (Figure 3D, E).","type":"Results"},{"text":" In that case, the addition of the RNA induces only minor chemical shift perturbation, suggesting that the N- and C-terminal regions of Sam68 bind specifically to the G8.5 RNA.","type":"Results"},{"text":"G8.5 is a RNA that contains the UAAA motif and was previously identified as a high affinity Sam68 binder by SELEX.","type":"Curator statement"}],"ec_go":"EXP","term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":281,"end":338,"reference_id":"36537190","reference_source":"pmid","reference_html":"Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions. <i> Malki I, Liepina I, Kogelnik N, Watmuff H, Robinson S, Lightfoot A, Gonchar O, Bottrill A, Fry AM, Dominguez C. </i> Nucleic Acids Res, 2022","date":"2024-04-04T17:47:45.868Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","region_id":"DP01705r017","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting RNA with sequence CUGGGUGACACACUAGCUAUAGCAUUAAAAGACCGAGCAAGU."}]}],"statement":[{"text":"Increasing the G8.5 molar ratio with the Sam68 N- and C-termini induced chemical shift perturbations, consistent with the formation of a complex between these regions and the RNA (Figure 3B, C). These results demonstrate that the Sam68 N- and C-terminal regions can bind RNA independently of the rest of the protein. Analysis of the titration data suggests that both domains bind the G.8 RNA with dissociation constants in the low micromolar range (1–10 μM for the N-terminus and 30–70 μM for the C-terminus) (Supplementary Figure S2), very similar to the affinity of the STAR domain for the same RNA sequence (18).","type":"Results"},{"text":"Analysis of the chemical shift mapping shows that RNA binding affects most residues of the N- and C-termini, in particular residues 10–61 for the N-terminus and 281–338 for the C-terminus (Figure 3D, E).","type":"Results"},{"text":" In that case, the addition of the RNA induces only minor chemical shift perturbation, suggesting that the N- and C-terminal regions of Sam68 bind specifically to the G8.5 RNA.","type":"Results"},{"text":"G8.5 is a RNA that contains the UAAA motif and was previously identified as a high affinity Sam68 binder by SELEX.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":31,"end":35,"reference_id":"36537190","reference_source":"pmid","reference_html":"Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions. <i> Malki I, Liepina I, Kogelnik N, Watmuff H, Robinson S, Lightfoot A, Gonchar O, Bottrill A, Fry AM, Dominguez C. </i> Nucleic Acids Res, 2022","date":"2024-04-04T17:52:18.067Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":33,"end":33,"position":"Specific residue"}],"ec_go":"EXP","region_id":"DP01705r018","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting RNA with sequence CUGGGUGACACACUAGCUAUAGCAUUAAAAGACCGAGCAAGU."}]}],"statement":[{"text":"The phosphorylated form of the Sam68 N-terminus was still able to bind the G8.5 RNA but the intensity of the CSPs was strongly reduced compared with the non-phosphorylated regions (Figure 4C). This indicates that phosphorylation of T33 reduces but does not abolish its RNA binding ability. Analysis of the NMR titration experiment suggests that the Kd of the phosphorylated Sam68 N-terminus for the G8.5 RNA is ∼100 μM (Supplementary Figure S4), significantly higher than the Kd with the unphosphorylated form.","type":"Results"},{"text":"Together, our data demonstrate that the N- and C-terminal regions of Sam68 are capable of binding RNA and that phosphorylation of T33 and T317 by Cdk1 significantly reduces their RNA binding ability.","type":"Results"},{"text":"G8.5 is a RNA that contains the UAAA motif and was previously identified as a high affinity Sam68 binder by SELEX.","type":"Curator statement"}],"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":136,"end":140,"reference_id":"36537190","reference_source":"pmid","reference_html":"Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions. <i> Malki I, Liepina I, Kogelnik N, Watmuff H, Robinson S, Lightfoot A, Gonchar O, Bottrill A, Fry AM, Dominguez C. </i> Nucleic Acids Res, 2022","date":"2024-04-04T18:11:26.542Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":137,"end":137,"position":"Specific residue"}],"ec_go":"EXP","region_id":"DP01705r019","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting RNA with sequence CUGGGUGACACACUAGCUAUAGCAUUAAAAGACCGAGCAAGU."}]}],"statement":[{"text":"Analysis of the NMR titration experiment suggests that the Kd of the phosphorylated Sam68 N-terminus for the G8.5 RNA is ∼100 μM (Supplementary Figure S4), significantly higher than the Kd with the unphosphorylated form. For the phosphorylated C-terminus, the chemical shift changes upon RNA addition were too small (Figure 4D) to allow us to derive a meaningful estimation of the Kd, suggesting that the dissociation constant of the T317-phosphoryled C-terminus to the RNA is >100 μM.","type":"Results"},{"text":"Together, our data demonstrate that the N- and C-terminal regions of Sam68 are capable of binding RNA and that phosphorylation of T33 and T317 by Cdk1 significantly reduces their RNA binding ability.","type":"Results"},{"text":"G8.5 is a RNA that contains the UAAA motif and was previously identified as a high affinity Sam68 binder by SELEX.","type":"Curator statement"}],"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":136,"end":140,"reference_id":"36537190","reference_source":"pmid","reference_html":"Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions. <i> Malki I, Liepina I, Kogelnik N, Watmuff H, Robinson S, Lightfoot A, Gonchar O, Bottrill A, Fry AM, Dominguez C. </i> Nucleic Acids Res, 2022","date":"2024-04-04T18:22:20.048Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0032879","term_name":"regulation of localization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr33Glu","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To investigate the consequences of Sam68 T33 and T317 phosphorylation on RNA binding, we created a phospho-null (T33A/T317A) and a phospho-mimetic (T33E/T317E) GFP-tagged Sam68 mutant."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr137Glu","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To investigate the consequences of Sam68 T33 and T317 phosphorylation on RNA binding, we created a phospho-null (T33A/T317A) and a phospho-mimetic (T33E/T317E) GFP-tagged Sam68 mutant."}]},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"To investigate the consequences of Sam68 T33 and T317 phosphorylation on RNA binding, we created a phospho-null (T33A/T317A) and a phospho-mimetic (T33E/T317E) GFP-tagged Sam68 mutant."}]}],"ec_go":"IMP","region_id":"DP01705r020","statement":[{"text":"As expected, WT Sam68 is mainly diffused in the nucleus with sometimes few SNBs (76.2 ± 6.3%, pattern A), with a small proportion of cells displaying Sam68 exclusively in SNBs (9.7 ± 5.7%, pattern B) or localized in both the nucleus and the cytoplasm (9.0 ± 4.6%, pattern C) (Figure 5B). In contrast, the T33E/T317E mutant displayed significant localization differences when compared with WT Sam68, with a significant decrease in the percentage of cells displaying pattern A (60.1 ± 4.9) and a 2-fold increase in the percentage of cells displaying pattern B (23.2 ± 4.5) (Figure 5B). These changes in localization are similar to previously reported mutations in the KH RNA-binding domain of Sam68 (51).","type":"Results"},{"text":"T33 and T317 mutations alter the cellular localization of Sam68","type":"Results"},{"text":"Consider T33E/T317E is a phospho-mimetic mutant.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of any process in which a cell, a substance, or a cellular entity is transported to, or maintained in, a specific location.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0291","entry_name":"HCT116wt"}]},{"start":31,"end":35,"reference_id":"36537190","reference_source":"pmid","reference_html":"Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions. <i> Malki I, Liepina I, Kogelnik N, Watmuff H, Robinson S, Lightfoot A, Gonchar O, Bottrill A, Fry AM, Dominguez C. </i> Nucleic Acids Res, 2022","date":"2024-04-04T18:22:35.161Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0032879","term_name":"regulation of localization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr33Glu","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To investigate the consequences of Sam68 T33 and T317 phosphorylation on RNA binding, we created a phospho-null (T33A/T317A) and a phospho-mimetic (T33E/T317E) GFP-tagged Sam68 mutant."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr137Glu","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To investigate the consequences of Sam68 T33 and T317 phosphorylation on RNA binding, we created a phospho-null (T33A/T317A) and a phospho-mimetic (T33E/T317E) GFP-tagged Sam68 mutant."}]},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"To investigate the consequences of Sam68 T33 and T317 phosphorylation on RNA binding, we created a phospho-null (T33A/T317A) and a phospho-mimetic (T33E/T317E) GFP-tagged Sam68 mutant."}]}],"ec_go":"IMP","region_id":"DP01705r021","statement":[{"text":"As expected, WT Sam68 is mainly diffused in the nucleus with sometimes few SNBs (76.2 ± 6.3%, pattern A), with a small proportion of cells displaying Sam68 exclusively in SNBs (9.7 ± 5.7%, pattern B) or localized in both the nucleus and the cytoplasm (9.0 ± 4.6%, pattern C) (Figure 5B). In contrast, the T33E/T317E mutant displayed significant localization differences when compared with WT Sam68, with a significant decrease in the percentage of cells displaying pattern A (60.1 ± 4.9) and a 2-fold increase in the percentage of cells displaying pattern B (23.2 ± 4.5) (Figure 5B). These changes in localization are similar to previously reported mutations in the KH RNA-binding domain of Sam68 (51).","type":"Results"},{"text":"T33 and T317 mutations alter the cellular localization of Sam68","type":"Results"},{"text":"Consider T33E/T317E is a phospho-mimetic mutant.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of any process in which a cell, a substance, or a cellular entity is transported to, or maintained in, a specific location.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0291","entry_name":"HCT116wt"}]},{"start":31,"end":35,"reference_id":"36537190","reference_source":"pmid","reference_html":"Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions. <i> Malki I, Liepina I, Kogelnik N, Watmuff H, Robinson S, Lightfoot A, Gonchar O, Bottrill A, Fry AM, Dominguez C. </i> Nucleic Acids Res, 2022","date":"2024-04-04T18:20:13.862Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0043484","term_name":"regulation of RNA splicing","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr33Glu","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To investigate the consequences of Sam68 T33 and T317 phosphorylation on RNA binding, we created a phospho-null (T33A/T317A) and a phospho-mimetic (T33E/T317E) GFP-tagged Sam68 mutant."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr137Glu","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To investigate the consequences of Sam68 T33 and T317 phosphorylation on RNA binding, we created a phospho-null (T33A/T317A) and a phospho-mimetic (T33E/T317E) GFP-tagged Sam68 mutant."}]},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"To investigate the consequences of Sam68 T33 and T317 phosphorylation on RNA binding, we created a phospho-null (T33A/T317A) and a phospho-mimetic (T33E/T317E) GFP-tagged Sam68 mutant."}]}],"ec_go":"IMP","region_id":"DP01705r022","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0291","entry_name":"HCT116wt"}],"statement":[{"text":"As previously reported, transfection of WT Sam68 induced the inclusion of exon v5 in CD44 (Figure 6A) and increased the Bcl-xS/Bcl-xL ratio (Figure 6B). However, the T33E/T317E mutant was significantly less efficient at including CD44 exon v5 compared with the WT Sam68 (0.27 ± 0.01 for T33E/T317E compared with 0.31 ± 0.00 for WT Sam68), and both mutants were less efficient at shifting splicing towards the XS isoform [XS/(XL + XS) ratio of 0.06 ± 0.02 and 0.07 ± 0.01 for T33A/T317A and T33E/T317E compared with 0.09 ± 0.01 for WT Sam68]. Hence, phosphorylation of Sam68 T33 and T317 attenuates Sam68 regulatory activity on CD44 and Bcl-x splicing.","type":"Results"},{"text":"T33 and T317 mutants have reduced Sam68 splicing activity","type":"Results"},{"text":"Consider T33E/T317E as a phospho-mimetic mutant.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of RNA splicing, the process of removing sections of the primary RNA transcript to remove sequences not present in the mature form of the RNA and joining the remaining sections to form the mature form of the RNA.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":136,"end":140,"reference_id":"36537190","reference_source":"pmid","reference_html":"Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions. <i> Malki I, Liepina I, Kogelnik N, Watmuff H, Robinson S, Lightfoot A, Gonchar O, Bottrill A, Fry AM, Dominguez C. </i> Nucleic Acids Res, 2022","date":"2024-04-04T18:20:33.511Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0043484","term_name":"regulation of RNA splicing","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr33Glu","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To investigate the consequences of Sam68 T33 and T317 phosphorylation on RNA binding, we created a phospho-null (T33A/T317A) and a phospho-mimetic (T33E/T317E) GFP-tagged Sam68 mutant."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr137Glu","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To investigate the consequences of Sam68 T33 and T317 phosphorylation on RNA binding, we created a phospho-null (T33A/T317A) and a phospho-mimetic (T33E/T317E) GFP-tagged Sam68 mutant."}]},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"To investigate the consequences of Sam68 T33 and T317 phosphorylation on RNA binding, we created a phospho-null (T33A/T317A) and a phospho-mimetic (T33E/T317E) GFP-tagged Sam68 mutant."}]}],"ec_go":"IMP","region_id":"DP01705r023","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0291","entry_name":"HCT116wt"}],"statement":[{"text":"As previously reported, transfection of WT Sam68 induced the inclusion of exon v5 in CD44 (Figure 6A) and increased the Bcl-xS/Bcl-xL ratio (Figure 6B). However, the T33E/T317E mutant was significantly less efficient at including CD44 exon v5 compared with the WT Sam68 (0.27 ± 0.01 for T33E/T317E compared with 0.31 ± 0.00 for WT Sam68), and both mutants were less efficient at shifting splicing towards the XS isoform [XS/(XL + XS) ratio of 0.06 ± 0.02 and 0.07 ± 0.01 for T33A/T317A and T33E/T317E compared with 0.09 ± 0.01 for WT Sam68]. Hence, phosphorylation of Sam68 T33 and T317 attenuates Sam68 regulatory activity on CD44 and Bcl-x splicing.","type":"Results"},{"text":"T33 and T317 mutants have reduced Sam68 splicing activity","type":"Results"},{"text":"Consider T33E/T317E as a phospho-mimetic mutant.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of RNA splicing, the process of removing sections of the primary RNA transcript to remove sequences not present in the mature form of the RNA and joining the remaining sections to form the mature form of the RNA.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":136,"end":140,"reference_id":"36537190","reference_source":"pmid","reference_html":"Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions. <i> Malki I, Liepina I, Kogelnik N, Watmuff H, Robinson S, Lightfoot A, Gonchar O, Bottrill A, Fry AM, Dominguez C. </i> Nucleic Acids Res, 2022","date":"2024-04-04T18:29:21.155Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051726","term_name":"regulation of cell cycle","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr33Glu","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To investigate the consequences of Sam68 T33 and T317 phosphorylation on RNA binding, we created a phospho-null (T33A/T317A) and a phospho-mimetic (T33E/T317E) GFP-tagged Sam68 mutant."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr137Glu","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To investigate the consequences of Sam68 T33 and T317 phosphorylation on RNA binding, we created a phospho-null (T33A/T317A) and a phospho-mimetic (T33E/T317E) GFP-tagged Sam68 mutant."}]}],"ec_go":"IMP","region_id":"DP01705r024","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0291","entry_name":"HCT116wt"}],"statement":[{"text":"T33 and T317 mutants affect cell cycle progression, decrease apoptosis and increase proliferation","type":"Results"},{"text":"Expression of Sam68 WT significantly decreased (from 35.9 ± 3.7% to 26.0 ± 1.8%) the G2/M population and significantly increased (from 1.2 ± 0.1% to 16.2 ± 0.8%) the sub-G1 population compared with untransfected cells. In contrast, expression of Sam68 T33A/T317A and T33E/T317E mutants resulted in increased G2/M populations (30.4 ± 5.2% and 27.5 ± 1.2, respectively) compared with WT expression. Moreover, Sam68 T33E/T317E transfection resulted in a significant decrease in the sub-G1 population (14.0 ± 0.1%) and S population (15.3 ± 0.2), and an increase in the G1 population (43.2 ± 1.0%) compared with the WT.","type":"Results"},{"text":"Altogether, our data demonstrate that phosphorylation of Sam68 at T33 and T317 alters its regulatory role in cell cycle progression and apoptosis, leading to increased proliferation of HCT116 cells.","type":"Results"},{"text":"Consider T33E/T317E is a phospho-mimetic mutant.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that modulates the rate or extent of progression through the cell cycle.\" [GOC:ai, GOC:dph, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false},{"start":31,"end":35,"reference_id":"36537190","reference_source":"pmid","reference_html":"Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions. <i> Malki I, Liepina I, Kogelnik N, Watmuff H, Robinson S, Lightfoot A, Gonchar O, Bottrill A, Fry AM, Dominguez C. </i> Nucleic Acids Res, 2022","date":"2024-04-04T18:29:30.745Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051726","term_name":"regulation of cell cycle","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr33Glu","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To investigate the consequences of Sam68 T33 and T317 phosphorylation on RNA binding, we created a phospho-null (T33A/T317A) and a phospho-mimetic (T33E/T317E) GFP-tagged Sam68 mutant."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr137Glu","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To investigate the consequences of Sam68 T33 and T317 phosphorylation on RNA binding, we created a phospho-null (T33A/T317A) and a phospho-mimetic (T33E/T317E) GFP-tagged Sam68 mutant."}]}],"ec_go":"IMP","region_id":"DP01705r025","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0291","entry_name":"HCT116wt"}],"statement":[{"text":"T33 and T317 mutants affect cell cycle progression, decrease apoptosis and increase proliferation","type":"Results"},{"text":"Expression of Sam68 WT significantly decreased (from 35.9 ± 3.7% to 26.0 ± 1.8%) the G2/M population and significantly increased (from 1.2 ± 0.1% to 16.2 ± 0.8%) the sub-G1 population compared with untransfected cells. In contrast, expression of Sam68 T33A/T317A and T33E/T317E mutants resulted in increased G2/M populations (30.4 ± 5.2% and 27.5 ± 1.2, respectively) compared with WT expression. Moreover, Sam68 T33E/T317E transfection resulted in a significant decrease in the sub-G1 population (14.0 ± 0.1%) and S population (15.3 ± 0.2), and an increase in the G1 population (43.2 ± 1.0%) compared with the WT.","type":"Results"},{"text":"Altogether, our data demonstrate that phosphorylation of Sam68 at T33 and T317 alters its regulatory role in cell cycle progression and apoptosis, leading to increased proliferation of HCT116 cells.","type":"Results"},{"text":"Consider T33E/T317E is a phospho-mimetic mutant.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that modulates the rate or extent of progression through the cell cycle.\" [GOC:ai, GOC:dph, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false},{"start":31,"end":35,"reference_id":"36537190","reference_source":"pmid","reference_html":"Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions. <i> Malki I, Liepina I, Kogelnik N, Watmuff H, Robinson S, Lightfoot A, Gonchar O, Bottrill A, Fry AM, Dominguez C. </i> Nucleic Acids Res, 2022","date":"2024-04-04T18:32:40.173Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042981","term_name":"regulation of apoptotic process","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr33Glu","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To investigate the consequences of Sam68 T33 and T317 phosphorylation on RNA binding, we created a phospho-null (T33A/T317A) and a phospho-mimetic (T33E/T317E) GFP-tagged Sam68 mutant."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr137Glu","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To investigate the consequences of Sam68 T33 and T317 phosphorylation on RNA binding, we created a phospho-null (T33A/T317A) and a phospho-mimetic (T33E/T317E) GFP-tagged Sam68 mutant."}]}],"ec_go":"IMP","region_id":"DP01705r026","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0291","entry_name":"HCT116wt"}],"statement":[{"text":"T33 and T317 mutants affect cell cycle progression, decrease apoptosis and increase proliferation","type":"Results"},{"text":"Compared with untransfected cells, transfection of Sam68 WT increased the percentage of cells undergoing apoptosis as expected (from 12.1 ± 1.6% to 23.0 ± 1.7%), but this increase was significantly smaller upon transfection of the mutants (18.8 ± 1.5 and 16.6 ± 2.0 for T33AT317A and T33E/T317E, respectively) (Figure 7B).","type":"Results"},{"text":"Altogether, our data demonstrate that phosphorylation of Sam68 at T33 and T317 alters its regulatory role in cell cycle progression and apoptosis, leading to increased proliferation of HCT116 cells.","type":"Results"},{"text":"Consider T33E/T317E is a phospho-mimetic mutant.","type":"Curator statement"}],"term_comment":"This term should only be used when it is not possible to determine which phase or subtype of the apoptotic process is regulated by a gene product. Whenever detailed information is available, the more granular children terms should be used.","term_def":"\"Any process that modulates the occurrence or rate of cell death by apoptotic process.\" [GOC:jl, GOC:mtg_apoptosis]","term_is_obsolete":false,"term_not_annotate":false},{"start":136,"end":140,"reference_id":"36537190","reference_source":"pmid","reference_html":"Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions. <i> Malki I, Liepina I, Kogelnik N, Watmuff H, Robinson S, Lightfoot A, Gonchar O, Bottrill A, Fry AM, Dominguez C. </i> Nucleic Acids Res, 2022","date":"2024-04-04T18:32:50.191Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042981","term_name":"regulation of apoptotic process","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr33Glu","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To investigate the consequences of Sam68 T33 and T317 phosphorylation on RNA binding, we created a phospho-null (T33A/T317A) and a phospho-mimetic (T33E/T317E) GFP-tagged Sam68 mutant."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr137Glu","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To investigate the consequences of Sam68 T33 and T317 phosphorylation on RNA binding, we created a phospho-null (T33A/T317A) and a phospho-mimetic (T33E/T317E) GFP-tagged Sam68 mutant."}]}],"ec_go":"IMP","region_id":"DP01705r027","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0291","entry_name":"HCT116wt"}],"statement":[{"text":"T33 and T317 mutants affect cell cycle progression, decrease apoptosis and increase proliferation","type":"Results"},{"text":"Compared with untransfected cells, transfection of Sam68 WT increased the percentage of cells undergoing apoptosis as expected (from 12.1 ± 1.6% to 23.0 ± 1.7%), but this increase was significantly smaller upon transfection of the mutants (18.8 ± 1.5 and 16.6 ± 2.0 for T33AT317A and T33E/T317E, respectively) (Figure 7B).","type":"Results"},{"text":"Altogether, our data demonstrate that phosphorylation of Sam68 at T33 and T317 alters its regulatory role in cell cycle progression and apoptosis, leading to increased proliferation of HCT116 cells.","type":"Results"},{"text":"Consider T33E/T317E is a phospho-mimetic mutant.","type":"Curator statement"}],"term_comment":"This term should only be used when it is not possible to determine which phase or subtype of the apoptotic process is regulated by a gene product. Whenever detailed information is available, the more granular children terms should be used.","term_def":"\"Any process that modulates the occurrence or rate of cell death by apoptotic process.\" [GOC:jl, GOC:mtg_apoptosis]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_Q07666","date":"2018-08-07T13:23:43.000Z","acc":"Q07666","name":"KH domain-containing, RNA-binding, signal transduction-associated protein 1","length":443,"organism":"Homo sapiens","dataset":["Condensates-related proteins","RNA-binding proteins"],"UniParc":"UPI0000073DA7","genes":[{"name":{"value":"KHDRBS1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:18116","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:18116"}}]},"synonyms":[{"value":"SAM68","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"1374686","url":"http://www.ncbi.nlm.nih.gov/pubmed/1374686","alternativeUrl":"https://europepmc.org/abstract/MED/1374686"}}]}]}],"alphafold_very_low_content":0.37697516930022573,"disorder_content":0.5846501128668171,"disprot_consensus":{"full":[{"start":1,"end":96,"type":"D"},{"start":136,"end":156,"type":"D"},{"start":267,"end":378,"type":"D"},{"start":390,"end":419,"type":"D"}],"Structural state":[{"start":1,"end":96,"type":"D"},{"start":136,"end":156,"type":"D"},{"start":267,"end":378,"type":"D"},{"start":390,"end":419,"type":"D"}],"Disorder function":[{"start":17,"end":21,"type":"F"},{"start":30,"end":36,"type":"F"},{"start":56,"end":72,"type":"F"},{"start":316,"end":320,"type":"F"}],"Molecular function":[{"start":10,"end":61,"type":"F"},{"start":136,"end":140,"type":"F"},{"start":281,"end":338,"type":"F"}],"Biological process":[{"start":31,"end":35,"type":"F"},{"start":136,"end":140,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03884","name":"DNA gyrase inhibitor YacG","start":7,"end":56}],"gene3D":[{"start":1,"end":65,"id":"3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A"}]},"uniref50":"UniRef50_P44921","sequence":"MSETITVNCPTCGKTVVWGEISPFRPFCSKRCQLIDLGEWAAEEKRIPSSGDLSESDDWSEEPKQ","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_A8ALJ6","disprot_id":"DP01714","ncbi_taxon_id":83333,"regions_counter":2,"creator":"aelofsson","regions":[{"start":40,"end":65,"reference_id":"12211008","reference_source":"pmid","reference_html":"NMR structure of the Escherichia coli protein YacG: a novel sequence motif in the zinc-finger family of proteins. <i> Ramelot TA, Cort JR, Yee AA, Semesi A, Edwards AM, Arrowsmith CH, Kennedy MA. </i> Proteins, 2002","date":"2023-02-03T16:47:03.757Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP01714r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"The first 3 and last 25 residues are unstructured and shown in a random configuration.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"1LV3"}]}],"released":"2018_11","uniref100":"UniRef100_A7ZHJ2","date":"2018-08-07T13:54:06.000Z","acc":"P0A8H8","name":"DNA gyrase inhibitor YacG","length":65,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI000013A025","genes":[{"name":{"value":"yacG","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00649","url":"https://hamap.expasy.org/unirule/MF_00649"}}]},"olnNames":[{"value":"b0101"},{"value":"JW5008"}]}],"alphafold_very_low_content":0,"disorder_content":0.4,"disprot_consensus":{"full":[{"start":40,"end":65,"type":"D"}],"Structural state":[{"start":40,"end":65,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02482","name":"Sigma 54 modulation protein / S30EA ribosomal protein","start":4,"end":91}],"gene3D":[{"start":1,"end":107,"id":"3.30.160.100","name":"Ribosome hibernation promotion factor-like"}]},"uniref50":"UniRef50_P0AD51","sequence":"MTMNITSKQMEITPAIRQHVADRLAKLEKWQTHLINPHIILSKEPQGFVADATINTPNGVLVASGKHEDMYTAINELINKLERQLNKLQHKGEARRAATSVKDANFVEEVEEE","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0AD51","disprot_id":"DP01716","ncbi_taxon_id":83333,"regions_counter":2,"creator":"gerdos","regions":[{"start":91,"end":113,"reference_id":"12392550","reference_source":"pmid","reference_html":"Ribosome-associated factor Y adopts a fold resembling a double-stranded RNA binding domain scaffold. <i> Ye K, Serganov A, Hu W, Garber M, Patel DJ. </i> Eur J Biochem, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1L4S"},{"db":"BMRB","id":"5315"}],"region_id":"DP01716r002","statement":[{"text":"The 23 C-terminal residues of the protein are disordered. ","type":"Abstract"},{"text":"The protein has a βαβββα arrangement of secondary elements and a\ndisordered 23-residue C-terminal tail","type":"Introduction"},{"text":"The 23 C-terminal residues are intrinsically disordered as follows from\ntheir relaxation properties","type":"Methods"},{"text":"The 23 C-terminal residues show significantly lower H-15N heteronuclear NOE values and decreased R2, indicating that they are completely disordered in the solution.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-12T16:38:45.654Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P0AD51","date":"2018-08-07T13:57:30.000Z","acc":"P0AD49","name":"Ribosome-associated inhibitor A","length":113,"organism":"Escherichia coli (strain K12)","dataset":["RNA-binding proteins","Stress response proteins"],"UniParc":"UPI000011232B","genes":[{"name":{"value":"raiA","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11375931","url":"http://www.ncbi.nlm.nih.gov/pubmed/11375931","alternativeUrl":"https://europepmc.org/abstract/MED/11375931"}}]},"synonyms":[{"value":"yfiA","evidences":[{"code":"ECO:0000305"}]}],"olnNames":[{"value":"b2597"},{"value":"JW2578"}]}],"alphafold_very_low_content":0.05309734513274336,"disorder_content":0.20353982300884957,"disprot_consensus":{"full":[{"start":91,"end":113,"type":"D"}],"Structural state":[{"start":91,"end":113,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03987","name":"Autophagocytosis associated protein, active-site domain","start":38,"end":308}],"gene3D":[{"start":149,"end":314,"id":"3.30.1460.50","name":"3.30.1460.50"},{"start":27,"end":141,"id":"3.30.1460.50","name":"3.30.1460.50"}]},"uniref50":"UniRef50_Q9NT62","sequence":"MQNVINTVKGKALEVAEYLTPVLKESKFKETGVITPEEFVAAGDHLVHHCPTWQWATGEELKVKAYLPTGKQFLVTKNVPCYKRCKQMEYSDELEAIIEEDDGDGGWVDTYHNTGITGITEAVKEITLENKDNIRLQDCSALCEEEEDEDEGEAADMEEYEESGLLETDEATLDTRKIVEACKAKTDAGGEDAILQTRTYDLYITYDKYYQTPRLWLFGYDEQRQPLTVEHMYEDISQDHVKKTVTIENHPHLPPPPMCSVHPCRHAEVMKKIIETVAEGGGELGVHMYLLIFLKFVQAVIPTIEYDYTRHFTM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9NT62","disprot_id":"DP01720","ncbi_taxon_id":9606,"regions_counter":1,"creator":"emaiani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":158,"region_id":"DP01720r001","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Identifying intrinsically disordered protein regions likely to undergo binding-induced helical transitions. <i> Glover K, Mei Y, Sinha SC. </i> Biochim Biophys Acta, 2016","term_id":"IDPO:0000002","curator_id":"vnugnes","start":129,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-29T20:56:23.545Z","reference_source":"pmid","term_name":"disorder","reference_id":"27179590","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"ENKDNIRLQDCSALCEEEEDEDEGEAADME","statement":[{"text":"Two of the Anchor region-containing IDRs for which binding partners have not yet been identified, ATG3 residues 129-158 and ATG9A residues 810-839, also do not undergo a disorder-to-helix transition in either 25% or 40 % TFE (Figure 2). These IDRs contain two or fewer helical residues (Table 5) even in 25% and 40% TFE, which is insufficient for the formation of a single stable helical turn","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_Q9NT62","date":"2018-08-07T14:00:47.000Z","acc":"Q9NT62","name":"Ubiquitin-like-conjugating enzyme ATG3","length":314,"organism":"Homo sapiens","dataset":["Autophagy-related proteins"],"UniParc":"UPI0000073DB4","genes":[{"name":{"value":"ATG3"},"synonyms":[{"value":"APG3"},{"value":"APG3L"}]}],"alphafold_very_low_content":0.1751592356687898,"disorder_content":0.09554140127388536,"disprot_consensus":{"full":[{"start":129,"end":158,"type":"D"}],"Structural state":[{"start":129,"end":158,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00554","name":"Rel homology DNA-binding domain","start":428,"end":588},{"id":"PF16179","name":"Rel homology dimerisation domain","start":598,"end":696}],"gene3D":[{"start":414,"end":589,"id":"2.60.40.340","name":"Rel homology domain (RHD), DNA-binding domain"},{"start":590,"end":693,"id":"2.60.40.10","name":"Immunoglobulins"}]},"uniref50":"UniRef50_O95644","sequence":"MPSTSFPVPSKFPLGPAAAVFGRGETLGPAPRAGGTMKSAEEEHYGYASSNVSPALPLPTAHSTLPAPCHNLQTSTPGIIPPADHPSGYGAALDGGPAGYFLSSGHTRPDGAPALESPRIEITSCLGLYHNNNQFFHDVEVEDVLPSSKRSPSTATLSLPSLEAYRDPSCLSPASSLSSRSCNSEASSYESNYSYPYASPQTSPWQSPCVSPKTTDPEEGFPRGLGACTLLGSPRHSPSTSPRASVTEESWLGARSSRPASPCNKRKYSLNGRQPPYSPHHSPTPSPHGSPRVSVTDDSWLGNTTQYTSSAIVAAINALTTDSSLDLGDGVPVKSRKTTLEQPPSVALKVEPVGEDLGSPPPPADFAPEDYSSFQHIRKGGFCDQYLAVPQHPYQWAKPKPLSPTSYMSPTLPALDWQLPSHSGPYELRIEVQPKSHHRAHYETEGSRGAVKASAGGHPIVQLHGYLENEPLMLQLFIGTADDRLLRPHAFYQVHRITGKTVSTTSHEAILSNTKVLEIPLLPENSMRAVIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQPSGRTLSLQVASNPIECSQRSAQELPLVEKQSTDSYPVVGGKKMVLSGHNFLQDSKVIFVEKAPDGHHVWEMEAKTDRDLCKPNSLVVEIPPFRNQRITSPVHVSFYVCNGKRKRSQYQRFTYLPANVPIIKTEPTDDYEPAPTCGPVSQGLSPLPRPYYSQQLAMPPDPSSCLVAGFPPCPQRSTLMPAAPGVSPKLHDLSPAAYTKGVASPGHCHLGLPQPAGEAPAVQDVPRPVATHPGSPGQPPPALLPQQVSAPPSSSCPPGLEHSLCPSSPSPPLPPATQEPTCLQPCSPACPPATGRPQHLPSTVRRDESPTAGPRLLPEVHEDGSPNLAPIPVTVKREPEELDQLYLDDVNEIIRNDLSSTSTHS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O95644","disprot_id":"DP01724","ncbi_taxon_id":9606,"regions_counter":11,"creator":"smribeiro","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":400,"region_id":"DP01724r001","released":"2024_12","ec_id":"ECO:0006220","reference_html":"Investigating the human Calcineurin Interaction Network using the πɸLxVP SLiM. <i> Sheftic SR, Page R, Peti W. </i> Sci Rep, 2016","statement":[{"text":"The absence of electron density for NFATc1LxVP residues 391–400 suggests that these residues remain flexible upon complex formation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"smribeiro","start":391,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2024-12-02T19:53:15.506Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5SVE"}],"reference_id":"27974827","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":" DDQYLAVPQHPYQWAKPK","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q08209","statements":[{"type":"Results","text":"To determine how LxVP-containing substrates bind CN, we determined the 2.6 Å crystal structure of the CN:NFATc1LxVP complex (CNA-CNB-NFATc1LxVP; 383DDQYLAVPQHPYQWAKPK400)."},{"type":"Methods","text":"The CN:NFATc1LxVP complex (concentration: ~9 mg/ml) formed crystals in 0.1 M HEPES pH 7.0 and 15% (w/v) PEG4000 at 25 °C."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63098","statements":[{"type":"Abstract","text":"Here we describe the crystal structure of CN in complex with its substrate NFATc1 and show that the LxVP SLiM is correctly defined as πɸLxVP. "},{"type":"Results","text":"To determine how LxVP-containing substrates bind CN, we determined the 2.6 Å crystal structure of the CN:NFATc1LxVP complex (CNA-CNB-NFATc1LxVP; 383DDQYLAVPQHPYQWAKPK400) (Fig. 1B; Table S2). "}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-03T13:40:50.942Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":425,"region_id":"DP01724r002","released":"2024_12","ec_id":"ECO:0006165","reference_html":"Unusual Rel-like architecture in the DNA-binding domain of the transcription factor NFATc. <i> Wolfe SA, Zhou P, Dötsch V, Chen L, You A, Ho SN, Crabtree GR, Wagner G, Verdine GL. </i> Nature, 1997","statement":[{"text":"Residues 1-12 and 173-178 are highly disordered.","type":"Figure"},{"text":"The numbering above the sequence corresponds to that of NFATc-DBD, which corresponds to that of human NFATc (ref. 10) minus 413.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"smribeiro","start":416,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2024-11-29T18:54:34.479Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1NFA"}],"reference_id":"8990122","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"MKDWQLPSHSGPYELRIEVQPKSHHRAHYETEGSRGAVKASAGGHPIVQLHGYLENEPLMLQLFIGTADDRLLRPHAFYQVHRITGKTVSTTSHEAILSNTKVLEIPLLPENSMRAVIDCAGILKLRNSDIELRKGETDIGRKNTRVRLVFRVHVPQPSGRTLSLQVASNPIECSQRS","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-02T13:41:00.174Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":559,"region_id":"DP01724r005","released":"2024_12","ec_id":"ECO:0006165","reference_html":"Unusual Rel-like architecture in the DNA-binding domain of the transcription factor NFATc. <i> Wolfe SA, Zhou P, Dötsch V, Chen L, You A, Ho SN, Crabtree GR, Wagner G, Verdine GL. </i> Nature, 1997","statement":[{"text":"In NF-KB pSO, the 67 residues of the insert region form a compact helical bundle (Fig. 2b, red) which packs tightly against the immunoglobulin-like β-barrel2,3, whereas the much smaller insert region of NFATc-DBD (21 residues) projects out into solution and is unstructured.","type":"Article"}],"term_id":"IDPO:0000002","curator_id":"smribeiro","start":538,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2024-12-03T15:19:55.837Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1NFA"}],"reference_id":"8990122","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-04T13:02:37.560Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":398,"term_name":"protein phosphatase 2B binding","released":"2024_12","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","reference_html":"A second calcineurin binding site on the NFAT regulatory domain. <i> Park S, Uesugi M, Verdine GL. </i> Proc Natl Acad Sci U S A, 2000","statement":[{"text":"Two polypeptide sequences, CnBP-A and another located near the CO2H-terminal end of the regulatory region, CnBP-B, were found to interact strongly with Cn (refer to Fig. 2b). Further truncations indicated the minimal CnBP-A and CnBP-B to comprise residues 118–131 and 384–398, respectively (data not shown)","type":"Results"}],"term_id":"GO:0030346","curator_id":"vnugnes","start":384,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"10860980","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2024-11-27T14:39:21.360Z","reference_source":"pmid","ec_id":"ECO:0005640","region_id":"DP01724r006","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein phosphatase 2B.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"interaction_partner":[{"db":"UniProt","id":"P63098","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q08209","operator":"and","partner_start":null,"partner_end":null}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":414,"term_name":"disorder","released":"2024_12","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"A second calcineurin binding site on the NFAT regulatory domain. <i> Park S, Uesugi M, Verdine GL. </i> Proc Natl Acad Sci U S A, 2000","statement":[{"text":"The CD spectrum of unphosphorylated NFAT1–414 (Fig. 1b) closely resembles that of an unfolded protein (34) and specifically lacks the spectral features characteristic of α-helical or β-sheet secondary structure (Fig. 1b).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10860980","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2024-11-27T14:11:27.126Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01724r007","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Structural state","term_is_binding":true,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}]},{"start":1,"end":414,"reference_id":"10860980","reference_source":"pmid","reference_html":"A second calcineurin binding site on the NFAT regulatory domain. <i> Park S, Uesugi M, Verdine GL. </i> Proc Natl Acad Sci U S A, 2000","date":"2024-11-27T14:11:15.475Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"region_id":"DP01724r008","statement":[{"text":"Consistent with the notion that unphosphorylated NFAT1–414 possesses little, if any, folded structure, the protein is degraded rapidly on exposure to 500 ng/ml of trypsin or chymotrypsin, whereas the folded core domain of Cn A remained intact under these conditions (data not shown).","type":"Results"}]},{"start":118,"end":131,"reference_id":"10860980","reference_source":"pmid","reference_html":"A second calcineurin binding site on the NFAT regulatory domain. <i> Park S, Uesugi M, Verdine GL. </i> Proc Natl Acad Sci U S A, 2000","date":"2024-11-27T14:39:35.993Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0030346","term_name":"protein phosphatase 2B binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q08209","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63098","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01724r009","statement":[{"text":"Two polypeptide sequences, CnBP-A and another located near the CO2H-terminal end of the regulatory region, CnBP-B, were found to interact strongly with Cn (refer to Fig. 2b). Further truncations indicated the minimal CnBP-A and CnBP-B to comprise residues 118–131 and 384–398, respectively (data not shown).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein phosphatase 2B.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":384,"end":398,"reference_id":"10860980","reference_source":"pmid","reference_html":"A second calcineurin binding site on the NFAT regulatory domain. <i> Park S, Uesugi M, Verdine GL. </i> Proc Natl Acad Sci U S A, 2000","date":"2024-11-27T14:39:05.296Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0030346","term_name":"protein phosphatase 2B binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q08209","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63098","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01724r010","statement":[{"text":"These NMR results are consistent with those of truncation assays, indicating that the segment of CnBP-B most important for binding to Cn comprises residues 384–398.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein phosphatase 2B.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":704,"end":943,"reference_id":"29626537","reference_source":"pmid","reference_html":"Intrinsically Disordered Proteins Link Alternative Splicing and Post-translational Modifications to Complex Cell Signaling and Regulation. <i> Zhou J, Zhao S, Dunker AK. </i> J Mol Biol, 2018","date":"2024-11-27T14:27:10.512Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008035","ec_ontology":"ECO","ec_name":"author inference based on intrinsic disorder prediction used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP01724r011","statement":[{"text":"NFATs are of our particular interest because they have been confirmed by CD and NMR to contain extremely long disordered domains besides the welldefined DNA-binding domain[62]. These experimental data agree very well with the disorder prediction in Fig.6A.","type":"Results"},{"text":"PONDR FIT was used for all of the disorder predictions reported herein.","type":"Methods"},{"text":"Figure 6A shows this region is predicted as disordered. The authors prediction also matches AlphaFold prediction and therefore we consider this region as disordered.","type":"Curator statement"}]}],"released":"2018_11","uniref100":"UniRef100_O95644","date":"2018-08-07T14:03:50.000Z","acc":"O95644","name":"Nuclear factor of activated T-cells, cytoplasmic 1","length":943,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012FFB5","genes":[{"name":{"value":"NFATC1"},"synonyms":[{"value":"NFAT2"},{"value":"NFATC"}]}],"alphafold_very_low_content":0.623541887592789,"disorder_content":0.7274655355249204,"disprot_consensus":{"full":[{"start":1,"end":414,"type":"D"},{"start":416,"end":425,"type":"D"},{"start":538,"end":559,"type":"D"},{"start":704,"end":943,"type":"D"}],"Structural state":[{"start":1,"end":414,"type":"D"},{"start":416,"end":425,"type":"D"},{"start":538,"end":559,"type":"D"},{"start":704,"end":943,"type":"D"}],"Molecular function":[{"start":118,"end":131,"type":"F"},{"start":384,"end":398,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03100","name":"CcmE domain","start":35,"end":137}],"gene3D":[{"start":30,"end":143,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}]},"uniref50":"UniRef50_B2VJ02","sequence":"MNIRRKNRLWIACAVLAGLALTIGLVLYALRSNIDLFYTPGEILYGKRETQQMPEVGQRLRVGGMVMPGSVQRDPNSLKVTFTIYDAEGSVDVSYEGILPDLFREGQGVVVQGELEKGNHILAKEVLAKHDENYTPPEVEKAMEANHRRPASVYKDPAS","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_A7ZP19","disprot_id":"DP01729","ncbi_taxon_id":83333,"regions_counter":1,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":159,"region_id":"DP01729r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR structure of the heme chaperone CcmE reveals a novel functional motif. <i> Enggist E, Thöny-Meyer L, Güntert P, Pervushin K. </i> Structure, 2002","statement":[{"text":"The structurally less-well-defined C-terminal subdomain contains a single helical turn (Figure 3B) followed by an unstructured tail of 16 residues (not shown in the structure).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"akajava","start":144,"term_ontology":"IDPO","curator_name":"Andrey V Kajava","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-2342-6886","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1SR3"}],"reference_id":"12429096","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-26T13:51:39.317Z"}}],"released":"2018_11","uniref100":"UniRef100_A7ZP19","date":"2018-08-07T14:18:06.000Z","acc":"P69490","name":"Cytochrome c-type biogenesis protein CcmE","length":159,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI00001272E1","genes":[{"name":{"value":"ccmE","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01959","url":"https://hamap.expasy.org/unirule/MF_01959"}}]},"synonyms":[{"value":"yejS"}],"olnNames":[{"value":"b2197"},{"value":"JW2185"}]}],"alphafold_very_low_content":0.006289308176100629,"disorder_content":0.10062893081761007,"disprot_consensus":{"full":[{"start":144,"end":159,"type":"D"}],"Structural state":[{"start":144,"end":159,"type":"D"}]}},{"features":{"pfam":[{"id":"PF04109","name":"Autophagy protein ATG9","start":37,"end":525}]},"uniref50":"UniRef50_Q7Z3C6","sequence":"MAQFDTEYQRLEASYSDSPPGEEDLLVHVAEGSKSPWHHIENLDLFFSRVYNLHQKNGFTCMLIGEIFELMQFLFVVAFTTFLVSCVDYDILFANKMVNHSLHPTEPVKVTLPDAFLPAQVCSARIQENGSLITILVIAGVFWIHRLIKFIYNICCYWEIHSFYLHALRIPMSALPYCTWQEVQARIVQTQKEHQICIHKRELTELDIYHRILRFQNYMVALVNKSLLPLRFRLPGLGEAVFFTRGLKYNFELILFWGPGSLFLNEWSLKAEYKRGGQRLELAQRLSNRILWIGIANFLLCPLILIWQILYAFFSYAEVLKREPGALGARCWSLYGRCYLRHFNELEHELQSRLNRGYKPASKYMNCFLSPLLTLLAKNGAFFAGSILAVLIALTIYDEDVLAVEHVLTTVTLLGVTVTVCRSFIPDQHMVFCPEQLLRVILAHIHYMPDHWQGNAHRSQTRDEFAQLFQYKAVFILEELLSPIVTPLILIFCLRPRALEIIDFFRNFTVEVVGVGDTCSFAQMDVRQHGHPQWLSAGQTEASVYQQAEDGKTELSLMHFAITNPGWQPPRESTAFLGFLKEQVQRDGAAASLAQGGLLPENALFTSIQSLQSESEPLSLIANVVAGSSCRGPPLPRDLQGSRHRAEVASALRSFSPLQPGQAPTGRAHSTMTGSGVDARTASSGSSVWEGQLQSLVLSEYASTEMSLHALYMHQLHKQQAQAEPERHVWHRRESDESGESAPDEGGEGARAPQSIPRSASYPCAAPRPGAPETTALHGGFQRRYGGITDPGTVPRVPSHFSRLPLGGWAEDGQSASRHPEPVPEEGSEDELPPQVHKV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q7Z3C6","disprot_id":"DP01730","ncbi_taxon_id":9606,"regions_counter":4,"creator":"emaiani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":839,"region_id":"DP01730r001","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Identifying intrinsically disordered protein regions likely to undergo binding-induced helical transitions. <i> Glover K, Mei Y, Sinha SC. </i> Biochim Biophys Acta, 2016","term_id":"IDPO:0000002","curator_id":"fquaglia","start":810,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":4,"curator_orcid":"0000-0002-0341-4888","date":"2023-12-12T11:17:50.723Z","reference_source":"pmid","term_name":"disorder","reference_id":"27179590","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Secondary structure content estimated by analysis of CD spectra for each of the thirteen IDRs showed that none contained more than two residues in a helical conformation (Figures 1-3, Table 3-5), which is insufficient for the formation of a stable α-helix requiring a minimum of six residues. Formation of a minimal beta-structure requires six residues [38], and seven of the thirteen IDRs (Table 3-5) appear to have between six to eight residues in extended or β-conformation which may be sufficient for forming short stable β-hairpins (Table 3-5). Thus, while none of the selected IDRs had stable helical structure, several may have short β-strands.","type":"Results"}]},{"start":1,"end":35,"reference_id":"32610138","reference_source":"pmid","reference_html":"Structure of Human ATG9A, the Only Transmembrane Protein of the Core Autophagy Machinery. <i> Guardia CM, Tan XF, Lian T, Rana MS, Zhou W, Christenson ET, Lowry AJ, Faraldo-Gómez JD, Bonifacino JS, Jiang J, Banerjee A. </i> Cell Rep, 2020","date":"2022-05-13T15:32:48.255Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-21876"},{"db":"PDB","id":"6WR4"}],"region_id":"DP01730r002","statement":[{"text":"Missing residue region in the cryo-EM structure of the full-length protein.","type":"Curator statement"}]},{"start":96,"end":105,"reference_id":"32610138","reference_source":"pmid","reference_html":"Structure of Human ATG9A, the Only Transmembrane Protein of the Core Autophagy Machinery. <i> Guardia CM, Tan XF, Lian T, Rana MS, Zhou W, Christenson ET, Lowry AJ, Faraldo-Gómez JD, Bonifacino JS, Jiang J, Banerjee A. </i> Cell Rep, 2020","date":"2022-05-13T15:33:25.541Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-21876"},{"db":"PDB","id":"6WR4"}],"region_id":"DP01730r003","statement":[{"text":"Missing residue region in the cryo-EM structure of the full-length protein.","type":"Curator statement"}]},{"start":523,"end":839,"reference_id":"32610138","reference_source":"pmid","reference_html":"Structure of Human ATG9A, the Only Transmembrane Protein of the Core Autophagy Machinery. <i> Guardia CM, Tan XF, Lian T, Rana MS, Zhou W, Christenson ET, Lowry AJ, Faraldo-Gómez JD, Bonifacino JS, Jiang J, Banerjee A. </i> Cell Rep, 2020","date":"2022-05-13T15:34:46.657Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-21876"},{"db":"PDB","id":"6WR4"}],"region_id":"DP01730r004","statement":[{"text":"Missing residue region in the cryo-EM structure of the full-length protein.","type":"Curator statement"}]}],"released":"2018_11","uniref100":"UniRef100_Q7Z3C6","date":"2018-08-07T14:27:12.000Z","acc":"Q7Z3C6","name":"Autophagy-related protein 9A","length":839,"organism":"Homo sapiens","dataset":["Autophagy-related proteins"],"UniParc":"UPI00001A9D4D","genes":[{"name":{"value":"ATG9A","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"20124090","url":"http://www.ncbi.nlm.nih.gov/pubmed/20124090","alternativeUrl":"https://europepmc.org/abstract/MED/20124090"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:22408","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:22408"}}]},"synonyms":[{"value":"APG9L1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15755735","url":"http://www.ncbi.nlm.nih.gov/pubmed/15755735","alternativeUrl":"https://europepmc.org/abstract/MED/15755735"}}]}]}],"alphafold_very_low_content":0.2622169249106079,"disorder_content":0.43146603098927294,"disprot_consensus":{"full":[{"start":1,"end":35,"type":"D"},{"start":96,"end":105,"type":"D"},{"start":523,"end":839,"type":"D"}],"Structural state":[{"start":1,"end":35,"type":"D"},{"start":96,"end":105,"type":"D"},{"start":523,"end":839,"type":"D"}]}},{"features":{"pfam":[{"id":"PF10033","name":"Autophagy-related protein 13","start":15,"end":264}],"gene3D":[{"start":6,"end":268,"id":"3.30.900.10","name":"HORMA domain"}]},"uniref50":"UniRef50_Q06628","sequence":"MVAEEDIEKQVLQLIDSFFLKTTLLICSTESSRYQSSTENIFLFDDTWFEDHSELVSELPEIISKWSHYDGRKELPPLVVETYLDLRQLNSSHLVRLKDHEGHLWNVCKGTKKQEIVMERWLIELDNSSPTFKSYSEDETDVNELSKQLVLLFRYLLTLIQLLPTTELYQLLIKSYNGPQNEGSSNPITSTGPLVSIRTCVLDGSKPILSKGRIGLSKPIINTYSNALNESNLPAHLDQKKITPVWTKFGLLRVSVSYRRDWKFEINNTNDELFSARHASVSHNSQGPQNQPEQEGQSDQDIGKRQPQFQQQQQPQQQQQQQQQQQRQHQVQTQQQRQIPDRRSLSLSPCTRANSFEPQSWQKKVYPISRPVQPFKVGSIGSQSASRNPSNSSFFNQPPVHRPSMSSNYGPQMNIEGTSVGSTSKYSSSFGNIRRHSSVKTTENAEKVSKAVKSPLQPQESQEDLMDFVKLLEEKPDLTIKKTSGNNPPNINISDSLIRYQNLKPSNDLLSEDLSVSLSMDPNHTYHRGRSDSHSPLPSISPSMHYGSLNSRMSQGANASHLIARGGGNSSTSALNSRRNSLDKSSNKQGMSGLPPIFGGESTSYHHDNKIQKYNQLGVEEDDDDENDRLLNQMGNSATKFKSSISPRSIDSISSSFIKSRIPIRQPYHYSQPTTAPFQAQAKFHKPANKLIDNGNRSNSNNNNHNGNDAVGVMHNDEDDQDDDLVFFMSDMNLSKEG","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q06628","disprot_id":"DP01732","ncbi_taxon_id":559292,"regions_counter":34,"creator":"emaiani","regions":[{"region_id":"DP01732r001","ec_ontology":"ECO","end":738,"ec_name":"atomic force microscopy evidence used in manual assertion","start":269,"version":4,"statement":[{"text":"The Intrinsically Disordered Protein Atg13 Mediates Supramolecular Assembly of Autophagy Initiation Complexes","type":"Title"},{"text":"An essential autophagy factor Atg13 has a large intrinsically disordered region (IDR)","type":"Article"},{"text":"Using structural and biological techniques, we herein demonstrate that Atg13 has a large intrinsically disordered region (IDR) and interacts with two distinct Atg17 molecules using two binding regions in the IDR.","type":"Abstract"},{"text":"In the HS-AFM images of Atg13-MBP, the linkage of two globules by a string-like structure was apparent (Figure 1F and Movie S1). One of the globules was often observed to undergo transitions between ordered and disordered states within 1 s, whereas the other globule was always in an ordered state, indicating that the former is Atg13HORMA while the latter is MBP. The string-like structure is constantly disordered and highly flexible (Movie S1). This clearly demonstrates that the C-terminal region of Atg13 is actually intrinsically disordered, and thus is named IDR hereafter.","type":"Results"},{"text":"The IDR corresponds to the C-terminal region (residues 269–738).","type":"Curator statement"}],"term_name":"disorder","reference_html":"The Intrinsically Disordered Protein Atg13 Mediates Supramolecular Assembly of Autophagy Initiation Complexes. <i> Yamamoto H, Fujioka Y, Suzuki SW, Noshiro D, Suzuki H, Kondo-Kakuta C, Kimura Y, Hirano H, Ando T, Noda NN, Ohsumi Y. </i> Dev Cell, 2016","released":"2022_06","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27404361","date":"2022-05-26T09:35:08.292Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0001591","curator_id":"fquaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP01732r002","validated":{"curator_id":"fquaglia","timestamp":"2020-12-04T11:23:24.541Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":738,"term_id":"IDPO:0000002","start":268,"version":2,"statement":[{"text":"The IDR of Atg13 exhibited temporarily appearing and disappearing small globules, resulting in a double-Gaussian distribution of R_2D. Since the four small regions within the IDR are known to interact with Atg1 or Atg17, the small globules probably correspond to these regions.","type":"Results"}],"term_name":"disorder","ec_name":"atomic force microscopy evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"33230318","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0001591","curator_id":"tlazar","reference_html":"Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy. <i> Kodera N, Noshiro D, Dora SK, Mori T, Habchi J, Blocquel D, Gruet A, Dosnon M, Salladini E, Bignon C, Fujioka Y, Oda T, Noda NN, Sato M, Lotti M, Mizuguchi M, Longhi S, Ando T. </i> Nat Nanotechnol, 2021","ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP01732r003","ec_ontology":"ECO","end":436,"term_id":"GO:0005515","start":424,"version":4,"statement":[{"text":"We previously identified the first Atg17-binding region of Atg13, named Atg1317BR (residues 424–436), in which Ser428 and Ser429 are phosphorylated under nutrient-rich conditions but are dephosphorylated in response to starvation, thus enhancing the interaction with Atg17 (Fujioka et al., 2014). Immunoprecipitation analysis showed that Atg17 efficiently co-precipitated with GFP-Atg13 (Figure 1A, lanes 11 and 12), but not with GFP-Atg13 variants containing the S429D or F430A mutation in Atg1317BR (Figure 1A, lanes 13–16), confirming that Atg1317BR is crucial for the interaction with Atg17.","type":"Results"},{"text":"The IDR of Atg13 contains two distinct regions binding intermolecularly to Atg17","type":"Article"},{"text":"We also revealed that Atg13 interacts with Atg17 via a small portion (residues 424–436), called the Atg17-binding region (Atg1317BR), and found that the Atg1317BR-Atg17 interaction is also promoted by starvation-dependent dephosphorylation of Ser428 and Ser429 in Atg1317BR. ","type":"Introduction"}],"term_name":"protein binding","ec_name":"qualitative western immunoblotting evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_06","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"27404361","date":"2022-05-26T09:46:51.636Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0000279","curator_id":"fquaglia","reference_html":"The Intrinsically Disordered Protein Atg13 Mediates Supramolecular Assembly of Autophagy Initiation Complexes. <i> Yamamoto H, Fujioka Y, Suzuki SW, Noshiro D, Suzuki H, Kondo-Kakuta C, Kimura Y, Hirano H, Ando T, Noda NN, Ohsumi Y. </i> Dev Cell, 2016","ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q06410","operator":"and","partner_start":null,"partner_end":null}]},{"region_id":"DP01732r005","ec_ontology":"ECO","end":389,"term_id":"GO:0005515","start":359,"version":5,"statement":[{"text":"We next investigated the binding affinity of the Atg1317LR-Atg17 interaction by ITC. This analysis showed that a synthetic Atg1317LR peptide (residues 359–389) bound to Atg17 with a KD value of 2.0 μM (Figure 1E), indicating that although the Atg1317LR-Atg17 interaction is ∼10-fold weaker than the Atg1317BR-Atg17 interaction (Figure 1B, 220 nM), Atg1317LR can interact with Atg17 independently of Atg1317BR.","type":"Results"},{"text":"The IDR of Atg13 contains two distinct regions binding intermolecularly to Atg17","type":"Article"}],"term_name":"protein binding","ec_name":"isothermal titration calorimetry evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_06","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"27404361","date":"2022-05-26T09:49:51.109Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"fquaglia","reference_html":"The Intrinsically Disordered Protein Atg13 Mediates Supramolecular Assembly of Autophagy Initiation Complexes. <i> Yamamoto H, Fujioka Y, Suzuki SW, Noshiro D, Suzuki H, Kondo-Kakuta C, Kimura Y, Hirano H, Ando T, Noda NN, Ohsumi Y. </i> Dev Cell, 2016","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q06410","operator":"and","partner_start":null,"partner_end":null}]},{"region_id":"DP01732r011","ec_ontology":"ECO","end":389,"term_id":"GO:0070772","start":359,"version":4,"statement":[{"text":"Because Atg13 is a key factor that tethers Atg1 and Atg17 to form the Atg1 complex (Fujioka et al., 2014), we next investigated whether the Atg1317LR-Atg17 interaction is required for PAS organization. Fluorescence microscopy revealed that in cells expressing wild-type Atg13 or the S379A mutant, Atg17-GFP assembled to form the PAS upon rapamycin treatment (Figure 3D). However, in cells expressing the F375A mutant, the PAS was not observed at all (Figure 3D), and the S379D mutant was also defective in the PAS formation (Figure 3D). These observations indicate that the Atg1317LR-Atg17 interaction is required for PAS assembly.","type":"Results"},{"text":"Atg1317LR-Atg17 Interaction Is Crucial for PAS Assembly and Autophagy In Vivo","type":"Results"}],"term_name":"PAS complex","ec_name":"fluorescence microscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_06","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"27404361","date":"2022-05-26T10:07:02.744Z","reference_source":"pmid","term_namespace":"Cellular component","ec_id":"ECO:0006323","curator_id":"fquaglia","reference_html":"The Intrinsically Disordered Protein Atg13 Mediates Supramolecular Assembly of Autophagy Initiation Complexes. <i> Yamamoto H, Fujioka Y, Suzuki SW, Noshiro D, Suzuki H, Kondo-Kakuta C, Kimura Y, Hirano H, Ando T, Noda NN, Ohsumi Y. </i> Dev Cell, 2016","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A class III phosphatidylinositol 3-kinase complex that contains a phosphatidylinositol-3-phosphate 5-kinase subunit (Fab1p in yeast; PIKfyve in mammals), a kinase activator, and a phosphatase, and may also contain additional proteins; it is involved in regulating the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate. In mammals the complex is composed of PIKFYVE, FIG4 and VAC14. In yeast it is composed of Atg18p, Fig4p, Fab1p, Vac14p and Vac7p.\" [PMID:18950639, PMID:19037259, PMID:19158662]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q06410","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q12142","operator":"and","partner_start":null,"partner_end":null}]},{"region_id":"DP01732r013","ec_ontology":"ECO","end":436,"term_id":"GO:1990316","start":424,"version":4,"statement":[{"text":"We next tested the intermolecular binding model (Figure 4E, right). For this purpose, we examined whether a short fragment of Atg13 containing Atg1317LR and Atg1317BR (residues 359–459) can interlink the Atg17-Atg29-Atg31 complexes in vitro (Figure 5A). By centrifugation, the Atg17-Atg29-Atg31 complex alone was almost completely recovered in the supernatant fraction (Figure 5A, lane 1). However, on addition of the Atg13 fragment, nearly half of the Atg17-Atg29-Atg31 complex became precipitable (Figure 5A, lane 4), probably due to aggregate formation by excess interlinking among the Atg13 fragments and the Atg17-Atg29-Atg31 complexes. In contrast, the addition of an Atg13 fragment bearing a mutation in Atg1317LR (S379D) or Atg1317BR (S429D) did not result in the precipitation of the Atg17-Atg29-Atg31 complex by centrifugation (Figure 5A, lanes 6 and 8).","type":"Results"},{"text":"These results suggest that the short Atg13 fragment can link the Atg17-Atg29-Atg31 complexes with each other via Atg1317LR and Atg1317BR, irrespective of other Atg13 regions such as Atg1317BR2. These results strongly support the intermolecular binding of Atg1317LR and Atg1317BR to the Atg17-Atg29-Atg31 complexes.","type":"Results"},{"text":"We further investigated the formation of the large Atg1 complexes by analytical ultracentrifugation. By use of wild-type Atg13-MBP, we observed large assemblages with sedimentation coefficient(s) of 15–20 S (Figure 5B). By contrast, when we used the Atg1317LR and Atg1317BR mutant, the 15- to 20-S supramolecular complex was barely detectable; instead, we observed a moderately sized complex with sedimentation coefficient of ∼10 S (Figure 5B), still larger than the Atg17-Atg29-Atg31 complex alone (sedimentation coefficient of ∼5 S). These results suggest that Atg13 mediates multimeric assembly of the Atg1 complexes via Atg1317LR and Atg1317BR, leading in turn to generation of the 15- to 20-S supramolecular complexes.","type":"Results"}],"term_name":"Atg1/ULK1 kinase complex","ec_name":"analytical ultracentrifugation evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_06","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"27404361","date":"2022-05-26T10:18:36.738Z","reference_source":"pmid","term_namespace":"Cellular component","ec_id":"ECO:0006275","curator_id":"fquaglia","reference_html":"The Intrinsically Disordered Protein Atg13 Mediates Supramolecular Assembly of Autophagy Initiation Complexes. <i> Yamamoto H, Fujioka Y, Suzuki SW, Noshiro D, Suzuki H, Kondo-Kakuta C, Kimura Y, Hirano H, Ando T, Noda NN, Ohsumi Y. </i> Dev Cell, 2016","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A protein complex consisting of Atg1 (or Atg1 homologs e.g. ULK1, ULK2 in mammals) and Atg13 along with other proteins that regulate its function (e.g. Atg17 in yeast or RB1CC1(FIP200) in mammals). This complex has serine/threonine protein kinase activity and is involved in autophagosome formation.\" [GOC:bhm, GOC:DOS, GOC:rb, PMID:15743910, PMID:19211835, PMID:19258318, PMID:19597335, PMID:22885598]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01732r015","ec_ontology":"ECO","end":389,"term_id":"GO:1990316","start":359,"version":4,"statement":[{"text":"We next tested the intermolecular binding model (Figure 4E, right). For this purpose, we examined whether a short fragment of Atg13 containing Atg1317LR and Atg1317BR (residues 359–459) can interlink the Atg17-Atg29-Atg31 complexes in vitro (Figure 5A). By centrifugation, the Atg17-Atg29-Atg31 complex alone was almost completely recovered in the supernatant fraction (Figure 5A, lane 1). However, on addition of the Atg13 fragment, nearly half of the Atg17-Atg29-Atg31 complex became precipitable (Figure 5A, lane 4), probably due to aggregate formation by excess interlinking among the Atg13 fragments and the Atg17-Atg29-Atg31 complexes. In contrast, the addition of an Atg13 fragment bearing a mutation in Atg1317LR (S379D) or Atg1317BR (S429D) did not result in the precipitation of the Atg17-Atg29-Atg31 complex by centrifugation (Figure 5A, lanes 6 and 8).","type":"Results"},{"text":"These results suggest that the short Atg13 fragment can link the Atg17-Atg29-Atg31 complexes with each other via Atg1317LR and Atg1317BR, irrespective of other Atg13 regions such as Atg1317BR2. These results strongly support the intermolecular binding of Atg1317LR and Atg1317BR to the Atg17-Atg29-Atg31 complexes.","type":"Results"},{"text":"We further investigated the formation of the large Atg1 complexes by analytical ultracentrifugation. By use of wild-type Atg13-MBP, we observed large assemblages with sedimentation coefficient(s) of 15–20 S (Figure 5B). By contrast, when we used the Atg1317LR and Atg1317BR mutant, the 15- to 20-S supramolecular complex was barely detectable; instead, we observed a moderately sized complex with sedimentation coefficient of ∼10 S (Figure 5B), still larger than the Atg17-Atg29-Atg31 complex alone (sedimentation coefficient of ∼5 S). These results suggest that Atg13 mediates multimeric assembly of the Atg1 complexes via Atg1317LR and Atg1317BR, leading in turn to generation of the 15- to 20-S supramolecular complexes.","type":"Results"}],"term_name":"Atg1/ULK1 kinase complex","ec_name":"analytical ultracentrifugation evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_06","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"27404361","date":"2022-05-26T10:20:54.169Z","reference_source":"pmid","term_namespace":"Cellular component","ec_id":"ECO:0006275","curator_id":"fquaglia","reference_html":"The Intrinsically Disordered Protein Atg13 Mediates Supramolecular Assembly of Autophagy Initiation Complexes. <i> Yamamoto H, Fujioka Y, Suzuki SW, Noshiro D, Suzuki H, Kondo-Kakuta C, Kimura Y, Hirano H, Ando T, Noda NN, Ohsumi Y. </i> Dev Cell, 2016","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A protein complex consisting of Atg1 (or Atg1 homologs e.g. ULK1, ULK2 in mammals) and Atg13 along with other proteins that regulate its function (e.g. Atg17 in yeast or RB1CC1(FIP200) in mammals). This complex has serine/threonine protein kinase activity and is involved in autophagosome formation.\" [GOC:bhm, GOC:DOS, GOC:rb, PMID:15743910, PMID:19211835, PMID:19258318, PMID:19597335, PMID:22885598]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01732r017","ec_ontology":"ECO","end":436,"term_id":"GO:1990316","start":424,"version":4,"statement":[{"text":"Gel-filtration analysis showed that recombinant Atg1ΔKD-Atg13-MBP and Atg17-Atg29-Atg31 subcomplexes were distributed in fractions 15–16 and 12–14, respectively (Figures 5C and S5A). Upon mixing these two subcomplexes (10 μM each), all five components were co-distributed in large fractions (fractions 5–8) in a manner dependent on both Atg1317BR and Atg1317LR (Figure S5A). These results suggest that the five components interact with each other to form large complexes, a process in which Atg1317LR and Atg1317BR play an essential role.","type":"Results"}],"term_name":"Atg1/ULK1 kinase complex","ec_name":"chromatography evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_06","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"27404361","date":"2022-05-26T10:19:27.551Z","reference_source":"pmid","term_namespace":"Cellular component","ec_id":"ECO:0007680","curator_id":"fquaglia","reference_html":"The Intrinsically Disordered Protein Atg13 Mediates Supramolecular Assembly of Autophagy Initiation Complexes. <i> Yamamoto H, Fujioka Y, Suzuki SW, Noshiro D, Suzuki H, Kondo-Kakuta C, Kimura Y, Hirano H, Ando T, Noda NN, Ohsumi Y. </i> Dev Cell, 2016","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A protein complex consisting of Atg1 (or Atg1 homologs e.g. ULK1, ULK2 in mammals) and Atg13 along with other proteins that regulate its function (e.g. Atg17 in yeast or RB1CC1(FIP200) in mammals). This complex has serine/threonine protein kinase activity and is involved in autophagosome formation.\" [GOC:bhm, GOC:DOS, GOC:rb, PMID:15743910, PMID:19211835, PMID:19258318, PMID:19597335, PMID:22885598]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01732r019","ec_ontology":"ECO","end":389,"term_id":"GO:1990316","start":359,"version":4,"statement":[{"text":"Gel-filtration analysis showed that recombinant Atg1ΔKD-Atg13-MBP and Atg17-Atg29-Atg31 subcomplexes were distributed in fractions 15–16 and 12–14, respectively (Figures 5C and S5A). Upon mixing these two subcomplexes (10 μM each), all five components were co-distributed in large fractions (fractions 5–8) in a manner dependent on both Atg1317BR and Atg1317LR (Figure S5A). These results suggest that the five components interact with each other to form large complexes, a process in which Atg1317LR and Atg1317BR play an essential role.","type":"Results"}],"term_name":"Atg1/ULK1 kinase complex","ec_name":"chromatography evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_06","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"27404361","date":"2022-05-26T10:18:00.104Z","reference_source":"pmid","term_namespace":"Cellular component","ec_id":"ECO:0007680","curator_id":"fquaglia","reference_html":"The Intrinsically Disordered Protein Atg13 Mediates Supramolecular Assembly of Autophagy Initiation Complexes. <i> Yamamoto H, Fujioka Y, Suzuki SW, Noshiro D, Suzuki H, Kondo-Kakuta C, Kimura Y, Hirano H, Ando T, Noda NN, Ohsumi Y. </i> Dev Cell, 2016","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A protein complex consisting of Atg1 (or Atg1 homologs e.g. ULK1, ULK2 in mammals) and Atg13 along with other proteins that regulate its function (e.g. Atg17 in yeast or RB1CC1(FIP200) in mammals). This complex has serine/threonine protein kinase activity and is involved in autophagosome formation.\" [GOC:bhm, GOC:DOS, GOC:rb, PMID:15743910, PMID:19211835, PMID:19258318, PMID:19597335, PMID:22885598]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01732r021","ec_ontology":"ECO","end":436,"term_id":"GO:0010508","start":424,"version":4,"statement":[{"text":"We next studied the importance of the Atg13-mediated self-assembly of Atg1 complexes in vivo. Consistent with the in vitro biochemical analyses, fluorescence microscopy showed that PAS assembly of Atg17-GFP and Atg13-mCherry (i.e., the multimeric assembly of the Atg1 complexes in vivo) strictly required both Atg1317BR and Atg1317LR (Figure 6A): upon mutation in Atg1317BR or Atg1317LR, the PAS was barely detectable (Figure 6A), even when PAS formation was enhanced using a kinase-dead form of Atg1 (D211A) (Sekito et al., 2009).","type":"Results"},{"text":"Altogether, these data indicate that Atg13 links the Atg17-Atg29-Atg31 complexes via two distinct regions, Atg1317BR and Atg1317LR, thus leading to multimeric assembly of Atg1 complexes.","type":"Results"},{"text":"Atg13-Mediated Self-Assembly of Atg1 Complexes Is Required for Initial Events in Autophagy","type":"Results"}],"term_name":"positive regulation of autophagy","ec_name":"fluorescence microscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_06","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"27404361","date":"2022-05-25T15:21:45.679Z","reference_source":"pmid","term_namespace":"Biological process","ec_id":"ECO:0006323","curator_id":"fquaglia","reference_html":"The Intrinsically Disordered Protein Atg13 Mediates Supramolecular Assembly of Autophagy Initiation Complexes. <i> Yamamoto H, Fujioka Y, Suzuki SW, Noshiro D, Suzuki H, Kondo-Kakuta C, Kimura Y, Hirano H, Ando T, Noda NN, Ohsumi Y. </i> Dev Cell, 2016","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that activates, maintains or increases the rate of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.\" [GOC:dph, GOC:tb]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":571,"end":700,"reference_id":"31352862","reference_source":"pmid","reference_html":"The carboxy terminus of yeast Atg13 binds phospholipid membrane via motifs that overlap with the Vac8-interacting domain. <i> Gatica D, Damasio A, Pascual C, Klionsky DJ, Ragusa MJ, Popelka H. </i> Autophagy, 2020","date":"2022-05-25T13:21:52.761Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP01732r023","statement":[{"text":"Atg13[571-700] is intrinsically disordered","type":"Results"},{"text":"After screening several C-terminal constructs for expression and solubility in E. coli, we succeeded in purifying Atg13[571–700]. As expected, this region was intrinsically disordered as observed by 2D 1H-15N HSQC spectroscopy and circular dichroism (CD) (Figures S1 and S2).","type":"Results"}]},{"start":571,"end":700,"reference_id":"31352862","reference_source":"pmid","reference_html":"The carboxy terminus of yeast Atg13 binds phospholipid membrane via motifs that overlap with the Vac8-interacting domain. <i> Gatica D, Damasio A, Pascual C, Klionsky DJ, Ragusa MJ, Popelka H. </i> Autophagy, 2020","date":"2022-05-25T13:58:41.488Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001164","ec_ontology":"ECO","ec_name":"co-sedimentation assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"28874","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01732r024","statement":[{"text":"Atg13[571-700] binds negatively charged liposomes","type":"Results"},{"text":"Full-length Atg13 was shown to bind yeast polar lipids [2], suggesting that electrostatic interactions may play an important role in liposome binding by the Atg13[571–700] peptide. To test if this is the case, we performed liposome sedimentation assays in the presence of increasing concentrations of NaCl (Figure 1D,E). If electrostatic interactions are required for membrane binding, then increasing NaCl concentrations will disrupt this interaction. We found that Atg13[571–700] bound to Folch liposomes in buffer containing either 50 or 150 mM NaCl, but that binding was almost completely abolished in buffer containing 300 or 500 mM NaCl. This result suggests that Atg13 binding to liposomes is mediated primarily through electrostatic interactions. In agreement with this result, Atg13[571–700] also bound yeast polar lipids, and this binding was severely disrupted by a NaCl concentration higher than 50 mM (Figure 1 F,G).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":639,"end":643,"reference_id":"31352862","reference_source":"pmid","reference_html":"The carboxy terminus of yeast Atg13 binds phospholipid membrane via motifs that overlap with the Vac8-interacting domain. <i> Gatica D, Damasio A, Pascual C, Klionsky DJ, Ragusa MJ, Popelka H. </i> Autophagy, 2020","date":"2022-05-25T14:51:01.808Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","region_id":"DP01732r025","statement":[{"text":"To further examine the role of the 640KFK and 683KFHK motifs in liposome binding, we mutated the Atg13[571–700] sequence to F641G I645G, F641E I645E, or K683E H685E K686E. Liposome sedimentation assays were performed in 50, 150, 300 and 500 mM NaCl. All 3 mutants were significantly defective in membrane binding at a physiological concentration of 150 mM NaCl, with more than 60% reduction relative to wild type (Figure 2B). A summary of all truncation and mutagenesis data is presented in Figure S5. These data suggest that Atg13[571–700] contains 2 distinct liposome-binding motifs, 640KFK (site I) and 683KFHK (site II) (Figure 1A) and that electrostatic force is not a sole factor responsible for lipid binding of the Atg13[571–700] region. A hydrophobic insertion of aromatic residues in the motifs plays a role in binding efficiency, in agreement with data in Figure 1.","type":"Results"},{"text":"Region including the first charged motif, KFK.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"ChEBI","id":"28874","operator":"and","partner_start":null,"partner_end":null}]},{"start":682,"end":687,"reference_id":"31352862","reference_source":"pmid","reference_html":"The carboxy terminus of yeast Atg13 binds phospholipid membrane via motifs that overlap with the Vac8-interacting domain. <i> Gatica D, Damasio A, Pascual C, Klionsky DJ, Ragusa MJ, Popelka H. </i> Autophagy, 2020","date":"2022-05-25T14:50:46.383Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","interaction_partner":[{"db":"ChEBI","id":"28874","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01732r026","statement":[{"text":"To further examine the role of the 640KFK and 683KFHK motifs in liposome binding, we mutated the Atg13[571–700] sequence to F641G I645G, F641E I645E, or K683E H685E K686E. Liposome sedimentation assays were performed in 50, 150, 300 and 500 mM NaCl. All 3 mutants were significantly defective in membrane binding at a physiological concentration of 150 mM NaCl, with more than 60% reduction relative to wild type (Figure 2B). A summary of all truncation and mutagenesis data is presented in Figure S5. These data suggest that Atg13[571–700] contains 2 distinct liposome-binding motifs, 640KFK (site I) and 683KFHK (site II) (Figure 1A) and that electrostatic force is not a sole factor responsible for lipid binding of the Atg13[571–700] region. A hydrophobic insertion of aromatic residues in the motifs plays a role in binding efficiency, in agreement with data in Figure 1.","type":"Results"},{"text":"Region including the second charged motif, KFHK.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":660,"end":686,"reference_id":"31352862","reference_source":"pmid","reference_html":"The carboxy terminus of yeast Atg13 binds phospholipid membrane via motifs that overlap with the Vac8-interacting domain. <i> Gatica D, Damasio A, Pascual C, Klionsky DJ, Ragusa MJ, Popelka H. </i> Autophagy, 2020","date":"2022-05-25T14:57:19.378Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P39968","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01732r027","statement":[{"text":"To investigate whether mutations in the phospholipid-binding sites I and II of Atg13 (640KFK and 683KFHK) affect binding with Vac8, we tested the binding affinity of the Atg13 glycine and glutamate mutants with Vac8 relative to wild type. As indicated above, we also constructed a mutant with a presumably disrupted interaction between the Atg13 peptide and Vac8. The D651R Q666R P667R mutant carries cationic residues in the Vac8-binding region to repulse the peptide from the positively charged Vac8 groove. We applied isothermal calorimetry (ITC) to measure dissociation constants for Atg13[571–700] binding to recombinant purified Vac8[10–515]. The WT and all of the mutated Atg13[571–700] peptides, except for Atg13[571–700]D651,Q666,P667R, bound to Vac8 with dissociation constants from 227–736 nM (Table 1), confirming that the Atg13[571–700] region carries the Vac8-binding domain, and that the Atg13 residues required for liposome binding are not required for Vac8 binding (Figure 3A). Atg13[571–700]D651,Q666,P667R bound to Vac8 with the lowest affinity (Kd of 1885 nM; Table 1), demonstrating that the Atg13 region between the phospholipid site I and II (Figure S6A) is involved in Vac8 binding, in agreement with the crystallographic data.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":571,"end":700,"reference_id":"31352862","reference_source":"pmid","reference_html":"The carboxy terminus of yeast Atg13 binds phospholipid membrane via motifs that overlap with the Vac8-interacting domain. <i> Gatica D, Damasio A, Pascual C, Klionsky DJ, Ragusa MJ, Popelka H. </i> Autophagy, 2020","date":"2022-05-25T15:00:10.739Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","region_id":"DP01732r028","statement":[{"text":"The 2D 1 H-15 N HSQC spectra of Atg13[571-700]. The lack of dispersion in the amide region of the spectrum is indicative that this region is intrinsically disordered.","type":"Supplementary material"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":571,"end":700,"reference_id":"31352862","reference_source":"pmid","reference_html":"The carboxy terminus of yeast Atg13 binds phospholipid membrane via motifs that overlap with the Vac8-interacting domain. <i> Gatica D, Damasio A, Pascual C, Klionsky DJ, Ragusa MJ, Popelka H. </i> Autophagy, 2020","date":"2022-05-25T15:07:28.986Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0010508","term_name":"positive regulation of autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007694","ec_ontology":"ECO","ec_name":"phosphatase assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IDA","region_id":"DP01732r029","statement":[{"text":"The lipid- and Vac8-binding capability of Atg13 are required for efficient autophagy","type":"Results"},{"text":"To determine if nonselective autophagy activity is affected by a chromosomal mutation in the phospholipid- and Vac8-binding motifs of the full-length Atg13 protein, we performed the quantitative Pho8Δ60 assay, in which Pho8Δ60 is a cytosolic zymogen of the vacuolar Pho8 phosphatase that lacks the first 60 amino acids of its N terminus. Vacuolar localization and activation of this zymogen relies on nonselective autophagy [22]. Cells with wild-type (WT) Atg13 exhibited a substantial increase in Pho8Δ60 activity after 3 h of nitrogen starvation (Figure 5A). In comparison, the F641E I645E, K683E H685E K686E, and D651R Q666R P667R mutants showed an ~30% decrease in Pho8Δ60 activity; the F641G I645G mutant was even more defective, as it exhibited an ~50% decrease in autophagy activity under the same experimental conditions.","type":"Results"},{"text":"Atg13 IDR mutants reduce autophagy activity. (A) Autophagy activity was measured by the Pho8Δ60 assay in WT and atg13∆ strains, and in cells expressing the F641E I645E, F641G I645G, K683E H685E K686E, or D651R Q666R P667R mutants under nutrient-rich conditions (+N) and after 3 h of nitrogen starvation (-N 3 h).","type":"Figure"},{"text":"Autophagy was measured using the GFP-Atg8 processing assay in the same strains as in (A) under nutrient-rich conditions and after 1 or 2 h of nitrogen starvation.","type":"Figure"},{"text":"The summary diagram of the lipid- and Vac8-binding capability and autophagy activity of the Atg13 mutants (Figure 5D) shows that the Atg13 protein promotes efficient autophagy only when its interaction with both phospholipids and Vac8 is intact and thereby balanced.","type":"Results"}],"term_comment":"","term_def":"\"Any process that activates, maintains or increases the rate of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.\" [GOC:dph, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false},{"start":571,"end":700,"reference_id":"31352862","reference_source":"pmid","reference_html":"The carboxy terminus of yeast Atg13 binds phospholipid membrane via motifs that overlap with the Vac8-interacting domain. <i> Gatica D, Damasio A, Pascual C, Klionsky DJ, Ragusa MJ, Popelka H. </i> Autophagy, 2020","date":"2022-05-27T10:12:13.662Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0060341","term_name":"regulation of cellular localization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IDA","region_id":"DP01732r030","statement":[{"text":"Again, these data suggest that the Atg13-phospholipd interaction needs to be effective and in concert with the Atg13-Vac8 interaction to maintain an optimal balance in localization of Atg13 in proximity to the vacuole; too little or too much binding to either component is detrimental to autophagy (Figures 5 and 6).","type":"Results"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of a process in which a cell, a substance, or a cellular entity is transported to, or maintained in a specific location within or in the membrane of a cell.\" [GOC:dph, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false},{"start":359,"end":389,"reference_id":"27404361","reference_source":"pmid","reference_html":"The Intrinsically Disordered Protein Atg13 Mediates Supramolecular Assembly of Autophagy Initiation Complexes. <i> Yamamoto H, Fujioka Y, Suzuki SW, Noshiro D, Suzuki H, Kondo-Kakuta C, Kimura Y, Hirano H, Ando T, Noda NN, Ohsumi Y. </i> Dev Cell, 2016","date":"2022-05-26T09:57:34.497Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0010508","term_name":"positive regulation of autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","region_id":"DP01732r031","statement":[{"text":"Atg1317LR is essential for autophagy.","type":"Figure"},{"text":"The Atg1317LR-binding region of Atg17 is required for autophagy.","type":"Figure"},{"text":"We further examined several Atg17 mutants by the ALP assay and found that the I385A, P393A, and T395A mutants exhibited severe defects in autophagy (Figure 3F).","type":"Results"},{"text":"Furthermore, Atg1317LR and Atg1317BR were strictly required for autophagy as estimated by the ALP assay (Figure 4C). However, deletion of or mutations in Atg1317BR2 only slightly reduced autophagic activity even in the atg11Δ background (Figure 4C). We also found that GFP-Atg13 bearing a double mutation in Atg1317LR and Atg1317BR (F375A F430A) did not precipitate Atg17 at all (Figure 4D, lane 16), even though it still contains Atg1317BR2. It should be noted that to detect weak interactions between Atg13 and Atg17, we used a mild detergent condition (0.1% NP-40) in this experiment. These results indicate that Atg1317LR and Atg1317BR, but not Atg1317BR2, are responsible for starvation-induced autophagy.","type":"Results"},{"text":"Region corresponding to Atg1317LR peptide (residues 359–389).","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that activates, maintains or increases the rate of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.\" [GOC:dph, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false},{"start":424,"end":436,"reference_id":"27404361","reference_source":"pmid","reference_html":"The Intrinsically Disordered Protein Atg13 Mediates Supramolecular Assembly of Autophagy Initiation Complexes. <i> Yamamoto H, Fujioka Y, Suzuki SW, Noshiro D, Suzuki H, Kondo-Kakuta C, Kimura Y, Hirano H, Ando T, Noda NN, Ohsumi Y. </i> Dev Cell, 2016","date":"2022-05-26T10:01:01.871Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0010508","term_name":"positive regulation of autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","region_id":"DP01732r032","statement":[{"text":"Atg1317LR is essential for autophagy.","type":"Figure"},{"text":"The Atg1317LR-binding region of Atg17 is required for autophagy.","type":"Figure"},{"text":"We further examined several Atg17 mutants by the ALP assay and found that the I385A, P393A, and T395A mutants exhibited severe defects in autophagy (Figure 3F).","type":"Results"},{"text":"Furthermore, Atg1317LR and Atg1317BR were strictly required for autophagy as estimated by the ALP assay (Figure 4C). However, deletion of or mutations in Atg1317BR2 only slightly reduced autophagic activity even in the atg11Δ background (Figure 4C). We also found that GFP-Atg13 bearing a double mutation in Atg1317LR and Atg1317BR (F375A F430A) did not precipitate Atg17 at all (Figure 4D, lane 16), even though it still contains Atg1317BR2. It should be noted that to detect weak interactions between Atg13 and Atg17, we used a mild detergent condition (0.1% NP-40) in this experiment. These results indicate that Atg1317LR and Atg1317BR, but not Atg1317BR2, are responsible for starvation-induced autophagy.","type":"Results"},{"text":"Region corresponding to Atg1317BR peptide (residues 424-436).","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that activates, maintains or increases the rate of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.\" [GOC:dph, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false},{"start":460,"end":521,"reference_id":"24793651","reference_source":"pmid","reference_html":"Structural basis of starvation-induced assembly of the autophagy initiation complex. <i> Fujioka Y, Suzuki SW, Yamamoto H, Kondo-Kakuta C, Kimura Y, Hirano H, Akada R, Inagaki F, Ohsumi Y, Noda NN. </i> Nat Struct Mol Biol, 2014","date":"2022-06-08T13:33:34.745Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006200","ec_ontology":"ECO","ec_name":"circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP01732r033","statement":[{"text":"CD spectra showed that Atg13 (460–521) is intrinsically disordered in solution (Supplementary Fig. 1c).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-08T13:37:45.335Z"}},{"start":460,"end":521,"reference_id":"24793651","reference_source":"pmid","reference_html":"Structural basis of starvation-induced assembly of the autophagy initiation complex. <i> Fujioka Y, Suzuki SW, Yamamoto H, Kondo-Kakuta C, Kimura Y, Hirano H, Akada R, Inagaki F, Ohsumi Y, Noda NN. </i> Nat Struct Mol Biol, 2014","date":"2022-06-06T14:52:12.187Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P53104","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01732r034","statement":[{"text":"We found that 62 amino acids (residues 460–521) of Atg13 are necessary and sufficient for Atg1 binding (Supplementary Fig. 1b).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-07T09:52:28.895Z"}}],"released":"2018_11","uniref100":"UniRef100_Q06628","date":"2018-08-07T15:18:42.000Z","acc":"Q06628","name":"Autophagy-related protein 13","length":738,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":["Autophagy-related proteins","Condensates-related proteins"],"UniParc":"UPI000006B8CF","genes":[{"name":{"value":"ATG13"},"synonyms":[{"value":"APG13"}],"olnNames":[{"value":"YPR185W"}]}],"alphafold_very_low_content":0.5623306233062331,"disorder_content":0.6382113821138211,"disprot_consensus":{"full":[{"start":268,"end":738,"type":"D"}],"Structural state":[{"start":268,"end":738,"type":"D"}],"Molecular function":[{"start":359,"end":389,"type":"F"},{"start":424,"end":436,"type":"F"},{"start":460,"end":521,"type":"F"},{"start":571,"end":700,"type":"F"}],"Cellular component":[{"start":359,"end":389,"type":"F"},{"start":424,"end":436,"type":"F"}],"Biological process":[{"start":359,"end":389,"type":"F"},{"start":424,"end":436,"type":"F"},{"start":571,"end":700,"type":"F"}]}},{"features":{"pfam":[{"id":"PF12874","name":"Zinc-finger of C2H2 type","start":35,"end":58},{"id":"PF12874","name":"Zinc-finger of C2H2 type","start":96,"end":119},{"id":"PF12874","name":"Zinc-finger of C2H2 type","start":163,"end":186},{"id":"PF12874","name":"Zinc-finger of C2H2 type","start":229,"end":253},{"id":"PF12874","name":"Zinc-finger of C2H2 type","start":286,"end":310},{"id":"PF12874","name":"Zinc-finger of C2H2 type","start":343,"end":367},{"id":"PF12874","name":"Zinc-finger of C2H2 type","start":400,"end":424}],"gene3D":[{"start":73,"end":128,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":336,"end":384,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":393,"end":433,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":224,"end":269,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":16,"end":72,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":279,"end":327,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":146,"end":199,"id":"3.30.160.60","name":"Classic Zinc Finger"}]},"uniref50":"UniRef50_Q8AVN9","sequence":"MADEFGNGDALDLPVGKDAVNSLIRENSHIFSDTQCKVCSAVLISESQKLAHYQSRKHANKVRRYMAINQGEDSVPAKKFKAAPAEISDGEDRSKCCPVCNMTFSSPVVAESHYIGKTHIKNLRLREQGGVKEGMVNQAKKTRTPTVATKSDNKMDHSDRAKFCKLCHSTFNNPLMAEQHYAGKKHKKQETKTQIMTIYTSSGQTPAQAPIPLNLNSPMPGSGSAGKGFSCDKCNIVLNSIEQYQAHVSGAKHKNQLMSMTPLSEEGHQAVVAPSAIASGSAGKGFSCDTCNIVLNSIEQYQAHISGAKHKNHLKSMTPLSEEGHTAAVAPSAFASGSAGKGFSCDTCNIVLNSIEQYQAHISGAKHKNHLMSMTPLSEEGHTAAVAPSAFASGSAGKGFSCDTCNIVLNSIEQYQAHVSGAKHKNQLMSMTPSSEEGLPSAVGPSAFASPLSAGGALSSGGPSGRGFCPSGDLTPKGPSSFGSLPPLGSLLPPLYPPAHSSQPYVHDDTMSPDGYNYFNEDFE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Amphibia","Batrachia","Anura","Pipoidea","Pipidae","Xenopodinae","Xenopus","Xenopus"],"uniref90":"UniRef90_Q8AVN9","disprot_id":"DP01733","ncbi_taxon_id":8355,"regions_counter":3,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":12,"region_id":"DP01733r001","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Solution structure of the N-terminal zinc fingers of the Xenopus laevis double-stranded RNA-binding protein ZFa. <i> Möller HM, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> J Mol Biol, 2005","statement":[{"text":"The N terminus from A2 to D12 and the linker between the two zinc-binding domains, from N69 to D92, are disordered. This is demonstrated by heteronuclear 1H–15N NOE measurements (Figure 4).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-26T14:01:25.834Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1ZU1"},{"db":"BMRB","id":"6655"}],"reference_id":"16051273","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":92,"region_id":"DP01733r002","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Solution structure of the N-terminal zinc fingers of the Xenopus laevis double-stranded RNA-binding protein ZFa. <i> Möller HM, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> J Mol Biol, 2005","statement":[{"text":"The N terminus from A2 to D12 and the linker between the two zinc-binding domains, from N69 to D92, are disordered. This is demonstrated by heteronuclear 1H–15N NOE measurements (Figure 4).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":69,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-26T13:59:23.839Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1ZU1"},{"db":"BMRB","id":"6655"}],"reference_id":"16051273","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":92,"term_name":"flexible linker","released":"2022_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Solution structure of the N-terminal zinc fingers of the Xenopus laevis double-stranded RNA-binding protein ZFa. <i> Möller HM, Martinez-Yamout MA, Dyson HJ, Wright PE. </i> J Mol Biol, 2005","term_id":"IDPO:0000033","curator_id":"vnugnes","start":69,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16051273","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-26T14:00:35.233Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01733r003","ec_go":"EXP","disprot_namespace":"Disorder function","cross_refs":[{"db":"BMRB","id":"6655"},{"db":"PDB","id":"1ZU1"}],"statement":[{"text":"The N terminus from A2 to D12 and the linker between the two zinc-binding domains, from N69 to D92, are disordered. This is demonstrated by heteronuclear 1H–15N NOE measurements (Figure 4).","type":"Results"},{"text":" We have determined the solution structure of a 127 residue fragment of ZFa, which consists of two zinc finger domains connected by a linker that remains unstructured in the free protein in solution.","type":"Abstract"}]}],"released":"2018_11","uniref100":"UniRef100_Q8AVN9","date":"2018-08-07T15:29:32.000Z","acc":"Q8AVN9","name":"Zinc finger protein 346","length":524,"organism":"Xenopus laevis","dataset":[],"UniParc":"UPI00000FE4D7","genes":[{"name":{"value":"znf346","evidences":[{"code":"ECO:0000250","source":{"name":"UniProtKB","id":"Q9R0B7","url":"https://www.uniprot.org/uniprot/Q9R0B7"}}]},"synonyms":[{"value":"jaz","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAH41713.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAH41713.1"}}]}]}],"alphafold_very_low_content":0.37404580152671757,"disorder_content":0.06870229007633588,"disprot_consensus":{"full":[{"start":1,"end":12,"type":"D"},{"start":69,"end":92,"type":"D"}],"Structural state":[{"start":1,"end":12,"type":"D"},{"start":69,"end":92,"type":"D"}],"Disorder function":[{"start":69,"end":92,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03358","name":"NADPH-dependent FMN reductase","start":1,"end":141}],"gene3D":[{"start":1,"end":174,"id":"3.40.50.360","name":"3.40.50.360"}]},"uniref50":"UniRef50_P80644","sequence":"MRVITLAGSPRFPSRSSSLLEYAREKLNGLDVEVYHWNLQNFAPEDLLYARFDSPALKTFTEQLQQADGLIVATPVYKAAYSGALKTLLDLLPERALQGKVVLPLATGGTVAHLLAVDYALKPVLSALKAQEILHGVFADDSQVIDYHHRPQFTPNLQTRLDTALETFWQALHRRDVQVPDLLSLRGNAHA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P80644","disprot_id":"DP01735","ncbi_taxon_id":83333,"regions_counter":1,"creator":"lalvarez","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":191,"region_id":"DP01735r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of Escherichia coli SsuE: defining a general catalytic cycle for FMN reductases of the flavodoxin-like superfamily. <i> Driggers CM, Dayal PV, Ellis HR, Karplus PA. </i> Biochemistry, 2014","statement":[{"text":"The remaining 18 or 19 residues to the C-terminus (residue 191) had no clear electron density and were not modeled.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"lalvarez","start":173,"term_ontology":"IDPO","curator_name":"Lucía Álvarez","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-1437-5773","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4PTY"}],"reference_id":"24816272","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P80644","date":"2018-08-07T16:37:48.000Z","acc":"P80644","name":"FMN reductase (NADPH)","length":191,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI0000136050","genes":[{"name":{"value":"ssuE"},"synonyms":[{"value":"ycbP"}],"olnNames":[{"value":"b0937"},{"value":"JW0920"}]}],"alphafold_very_low_content":0.005235602094240838,"disorder_content":0.09947643979057591,"disprot_consensus":{"full":[{"start":173,"end":191,"type":"D"}],"Structural state":[{"start":173,"end":191,"type":"D"}]}},{"features":{"pfam":[{"id":"PF08080","name":"RNPHF zinc finger","start":255,"end":290},{"id":"PF28441","name":"RRM domain","start":13,"end":97},{"id":"PF28441","name":"RRM domain","start":113,"end":192},{"id":"PF28441","name":"RRM domain","start":291,"end":365}],"gene3D":[{"start":287,"end":381,"id":"3.30.70.330","name":"3.30.70.330"},{"start":1,"end":100,"id":"3.30.70.330","name":"3.30.70.330"},{"start":103,"end":195,"id":"3.30.70.330","name":"3.30.70.330"}]},"uniref50":"UniRef50_P52597","sequence":"MMLGPEGGEGFVVKLRGLPWSCSVEDVQNFLSDCTIHDGAAGVHFIYTREGRQSGEAFVELGSEDDVKMALKKDRESMGHRYIEVFKSHRTEMDWVLKHSGPNSADSANDGFVRLRGLPFGCTKEEIVQFFSGLEIVPNGITLPVDPEGKITGEAFVQFASQELAEKALGKHKERIGHRYIEVFKSSQEEVRSYSDPPLKFMSVQRPGPYDRPGTARRYIGIVKQAGLERMRPGAYSTGYGGYEEYSGLSDGYGFTTDLFGRDLSYCLSGMYDHRYGDSEFTVQSTTGHCVHMRGLPYKATENDIYNFFSPLNPVRVHIEIGPDGRVTGEADVEFATHEEAVAAMSKDRANMQHRYIELFLNSTTGASNGAYSSQVMQGMGVSAAQATYSGLESQSVSGCYGAGYSGQNSMGGYD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P52597","disprot_id":"DP01736","ncbi_taxon_id":9606,"regions_counter":3,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":10,"region_id":"DP01736r001","released":"2022_12","ec_id":"ECO:0006165","reference_html":"NMR structure of the three quasi RNA recognition motifs (qRRMs) of human hnRNP F and interaction studies with Bcl-x G-tract RNA: a novel mode of RNA recognition. <i> Dominguez C, Allain FH. </i> Nucleic Acids Res, 2006","statement":[{"text":"Except for the 10 first residues that are highly flexible [negative (1H-15N)-NOE values], the 2 qRRMs possess a rigid core [(1H-15N)-NOE values higher than 0.7]. The linker region (residues 100–110), however, shows low (1H-15N)-NOE values (between 0.19 and 0.5), which indicates that the linker between the two qRRMs is flexible and suggests that the two qRRMs tumble independently in solution.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-26T14:05:38.867Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2HGL"},{"db":"PDB","id":"2HGM"}],"reference_id":"16885237","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":100,"end":110,"reference_id":"16885237","reference_source":"pmid","reference_html":"NMR structure of the three quasi RNA recognition motifs (qRRMs) of human hnRNP F and interaction studies with Bcl-x G-tract RNA: a novel mode of RNA recognition. <i> Dominguez C, Allain FH. </i> Nucleic Acids Res, 2006","date":"2022-08-26T14:07:12.236Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"2HGL"},{"db":"PDB","id":"2HGM"}],"region_id":"DP01736r002","statement":[{"text":"Except for the 10 first residues that are highly flexible [negative (1H-15N)-NOE values], the 2 qRRMs possess a rigid core [(1H-15N)-NOE values higher than 0.7]. The linker region (residues 100–110), however, shows low (1H-15N)-NOE values (between 0.19 and 0.5), which indicates that the linker between the two qRRMs is flexible and suggests that the two qRRMs tumble independently in solution.","type":"Results"}]},{"start":100,"end":110,"reference_id":"16885237","reference_source":"pmid","reference_html":"NMR structure of the three quasi RNA recognition motifs (qRRMs) of human hnRNP F and interaction studies with Bcl-x G-tract RNA: a novel mode of RNA recognition. <i> Dominguez C, Allain FH. </i> Nucleic Acids Res, 2006","date":"2022-08-26T14:07:25.675Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"2HGL"},{"db":"PDB","id":"2HGM"}],"region_id":"DP01736r003","statement":[{"text":"Except for the 10 first residues that are highly flexible [negative (1H-15N)-NOE values], the 2 qRRMs possess a rigid core [(1H-15N)-NOE values higher than 0.7]. The linker region (residues 100–110), however, shows low (1H-15N)-NOE values (between 0.19 and 0.5), which indicates that the linker between the two qRRMs is flexible and suggests that the two qRRMs tumble independently in solution.","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_P52597","date":"2018-08-07T16:40:31.000Z","acc":"P52597","name":"Heterogeneous nuclear ribonucleoprotein F","length":415,"organism":"Homo sapiens","dataset":["NDDs-related proteins","RNA-binding proteins"],"UniParc":"UPI000017C158","genes":[{"name":{"value":"HNRNPF"},"synonyms":[{"value":"HNRPF"}]}],"alphafold_very_low_content":0.35903614457831323,"disorder_content":0.05060240963855422,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"},{"start":100,"end":110,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":100,"end":110,"type":"D"}],"Disorder function":[{"start":100,"end":110,"type":"F"}]}},{"features":{"pfam":[{"id":"PF10759","name":"Bacterial proteasome activator","start":28,"end":166}]},"uniref50":"UniRef50_Q9CD99","sequence":"MVIGLSTGSDDDDVEVIGGVDPRLIAVQENDSDESSLTDLVEQPAKVMRIGTMIKQLLEEVRAAPLDEASRNRLRDIHATSIRELEDGLAPELREELDRLTLPFNEDAVPSDAELRIAQAQLVGWLEGLFHGIQTALFAQQMAARAQLQQMRQGALPPGVGKSGQHGHGTGQYL","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"uniref90":"UniRef90_P65092","disprot_id":"DP01737","ncbi_taxon_id":83332,"regions_counter":3,"creator":"jlamb","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":35,"region_id":"DP01737r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structural Analysis of the Bacterial Proteasome Activator Bpa in Complex with the 20S Proteasome. <i> Bolten M, Delley CL, Leibundgut M, Boehringer D, Ban N, Weber-Ban E. </i> Structure, 2016","statement":[{"text":"the characteristic circular dichroism (CD) signature observed for full-length Bpa, which features two minima at 208 and 220 nm (Figure 1B). Based on our in silico analysis, we generated a truncation variant (HisBpa36–159), from which the non-homologous and likely disordered regions were excluded. The CD spectrum of this variant shows the same overall shape with a slightly stronger helical signal","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jlamb","start":1,"term_ontology":"IDPO","curator_name":"John Lamb","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0568-8281","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27839949","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":35,"region_id":"DP01737r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural analysis of the dodecameric proteasome activator PafE in Mycobacterium tuberculosis. <i> Bai L, Hu K, Wang T, Jastrab JB, Darwin KH, Li H. </i> Proc Natl Acad Sci U S A, 2016","term_id":"IDPO:0000002","curator_id":"ahatos","start":14,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5IET"}],"reference_id":"27001842","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":174,"region_id":"DP01737r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structural Analysis of the Bacterial Proteasome Activator Bpa in Complex with the 20S Proteasome. <i> Bolten M, Delley CL, Leibundgut M, Boehringer D, Ban N, Weber-Ban E. </i> Structure, 2016","statement":[{"text":"the characteristic circular dichroism (CD) signature observed for full-length Bpa, which features two minima at 208 and 220 nm (Figure 1B). Based on our in silico analysis, we generated a truncation variant (HisBpa36–159), from which the non-homologous and likely disordered regions were excluded. The CD spectrum of this variant shows the same overall shape with a slightly stronger helical signal","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ahatos","start":160,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27839949","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P65092","date":"2018-08-07T16:46:16.000Z","acc":"P9WKX3","name":"Bacterial proteasome activator","length":174,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","dataset":[],"UniParc":"UPI0000139454","genes":[{"name":{"value":"bpa","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"25469515","url":"http://www.ncbi.nlm.nih.gov/pubmed/25469515","alternativeUrl":"https://europepmc.org/abstract/MED/25469515"}}]},"orfNames":[{"value":"MTCY13D12.14"}],"olnNames":[{"value":"Rv3780"}]}],"alphafold_very_low_content":0.09195402298850575,"disorder_content":0.28735632183908044,"disprot_consensus":{"full":[{"start":1,"end":35,"type":"D"},{"start":160,"end":174,"type":"D"}],"Structural state":[{"start":1,"end":35,"type":"D"},{"start":160,"end":174,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00036","name":"EF hand domain","start":54,"end":80},{"id":"PF01023","name":"S-100/ICaBP type calcium binding domain","start":4,"end":47}],"gene3D":[{"start":1,"end":92,"id":"1.10.238.10","name":"EF-hand"}]},"uniref50":"UniRef50_P04271","sequence":"MSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDNDGDGECDFQEFMAFVAMVTTACHEFFEHE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P04271","disprot_id":"DP01738","ncbi_taxon_id":9606,"regions_counter":4,"creator":"smribeiro","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":28,"region_id":"DP01738r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Analysis of the structure of human apo-S100B at low temperature indicates a unimodal conformational distribution is adopted by calcium-free S100 proteins. <i> Malik S, Revington M, Smith SP, Shaw GS. </i> Proteins, 2008","statement":[{"text":"Thus, the poor definition of the calcium-binding loops in human apo-S100B is most consistent with flexibility of the backbone within these regions.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"smribeiro","start":18,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2PRU"}],"reference_id":"18384084","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":28,"term_name":"calcium ion binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Analysis of the structure of human apo-S100B at low temperature indicates a unimodal conformational distribution is adopted by calcium-free S100 proteins. <i> Malik S, Revington M, Smith SP, Shaw GS. </i> Proteins, 2008","statement":[{"text":"Calcium binding loop I","type":"Curator statement"}],"term_id":"GO:0005509","curator_id":"smribeiro","start":18,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"18384084","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01738r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":91,"region_id":"DP01738r003","released":"2022_03","ec_id":"ECO:0006198","reference_html":"Backbone dynamics of the calcium-signaling protein apo-S100B as determined by 15N NMR relaxation. <i> Inman KG, Baldisseri DM, Miller KE, Weber DJ. </i> Biochemistry, 2001","statement":[{"text":"In the tertiary structure of S100B, residues with exchange contributions are grouped around the mobile C-terminal loop\n(Figure 4, panel C). Exchange is detected for all HSQC correlations from the last turn of helix 4 (V80) to the\nC-terminus at E91, and no correlations are observed for residues H85, E86, and F87 due to exchange broadening. ..this region of the protein is mobile on the chemical shift time scale.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"smribeiro","start":80,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"11297409","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":91,"term_name":"protein binding","released":"2022_03","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","reference_html":"Backbone dynamics of the calcium-signaling protein apo-S100B as determined by 15N NMR relaxation. <i> Inman KG, Baldisseri DM, Miller KE, Weber DJ. </i> Biochemistry, 2001","statement":[{"text":"Main interaction site for multiple S100B protein interactors.","type":"Curator statement"}],"term_id":"GO:0005515","curator_id":"smribeiro","start":80,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"11297409","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006198","region_id":"DP01738r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P04271","date":"2018-08-07T17:37:52.000Z","acc":"P04271","name":"Protein S100-B","length":92,"organism":"Homo sapiens","dataset":["Extracellular matrix proteins"],"UniParc":"UPI00001133BD","genes":[{"name":{"value":"S100B"}}],"alphafold_very_low_content":0,"disorder_content":0.25,"disprot_consensus":{"full":[{"start":18,"end":28,"type":"D"},{"start":80,"end":91,"type":"D"}],"Structural state":[{"start":18,"end":28,"type":"D"},{"start":80,"end":91,"type":"D"}],"Molecular function":[{"start":18,"end":28,"type":"F"},{"start":80,"end":91,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05108","name":"Type VII secretion system ESX-1, transport TM domain B","start":4,"end":464}],"gene3D":[{"start":244,"end":326,"id":"2.40.50.910","name":"Type VII secretion system EccB, repeat 3 domain"},{"start":419,"end":480,"id":"2.40.50.900","name":"Type VII secretion system EccB, repeat 1 domain"},{"start":66,"end":141,"id":"2.40.50.900","name":"Type VII secretion system EccB, repeat 1 domain"}]},"uniref50":"UniRef50_A0QNJ0","sequence":"MGLRLTTKVQVSGWRFLLRRLEHAIVRRDTRMFDDPLQFYSRSIALGIVVAVLILAGAALLAYFKPQGKLGGTSLFTDRATNQLYVLLSGQLHPVYNLTSARLVLGNPANPATVKSSELSKLPMGQTVGIPGAPYATPVSAGSTSIWTLCDTVARADSTSPVVQTAVIAMPLEIDASIDPLQSHEAVLVSYQGETWIVTTKGRHAIDLTDRALTSSMGIPVTARPTPISEGMFNALPDMGPWQLPPIPAAGAPNSLGLPDDLVIGSVFQIHTDKGPQYYVVLPDGIAQVNATTAAALRATQAHGLVAPPAMVPSLVVRIAERVYPSPLPDEPLKIVSRPQDPALCWSWQRSAGDQSPQSTVLSGRHLPISPSAMNMGIKQIHGTATVYLDGGKFVALQSPDPRYTESMYYIDPQGVRYGVPNAETAKSLGLSSPQNAPWEIVRLLVDGPVLSKDAALLEHDTLPADPSPRKVPAGASGAP","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"uniref90":"UniRef90_P9WNR6","disprot_id":"DP01739","ncbi_taxon_id":83332,"regions_counter":1,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":478,"region_id":"DP01739r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Core component EccB1 of the Mycobacterium tuberculosis type VII secretion system is a periplasmic ATPase. <i> Zhang XL, Li DF, Fleming J, Wang LW, Zhou Y, Wang DC, Zhang XE, Bi LJ. </i> FASEB J, 2015","statement":[{"text":"Authors said \" Fifteen residues are missing at the C-terminal of the model due to the flexibility of the protein\nsequence making interpretation impossible\". I just annotated the region of missing electron density.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":456,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3X3N"}],"reference_id":"26396239","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P9WNR6","date":"2018-08-07T22:08:40.000Z","acc":"P9WNR7","name":"ESX-1 secretion system ATPase EccB1","length":480,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","dataset":[],"UniParc":"UPI00000D1163","genes":[{"name":{"value":"eccB1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"19876390","url":"http://www.ncbi.nlm.nih.gov/pubmed/19876390","alternativeUrl":"https://europepmc.org/abstract/MED/19876390"}}]},"olnNames":[{"value":"Rv3869"}]}],"alphafold_very_low_content":0.0020833333333333333,"disorder_content":0.04791666666666667,"disprot_consensus":{"full":[{"start":456,"end":478,"type":"D"}],"Structural state":[{"start":456,"end":478,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00462","name":"Glutaredoxin","start":4,"end":69}],"gene3D":[{"start":1,"end":85,"id":"3.40.30.10","name":"Glutaredoxin"}]},"uniref50":"UniRef50_P68688","sequence":"MQTVIFGRSGCPYCVRAKDLAEKLSNERDDFQYQYVDIRAEGITKEDLQQKAGKPVETVPQIFVDQQHIGGYTDFAAWVKENLDA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P68688","disprot_id":"DP01740","ncbi_taxon_id":83333,"regions_counter":1,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":59,"region_id":"DP01740r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins. <i> Xia TH, Bushweller JH, Sodano P, Billeter M, Björnberg O, Holmgren A, Wüthrich K. </i> Protein Sci, 1992","statement":[{"text":"Authors said about this region \"Apparent structural  disorder, indicated by a large dispersion among the 20 conformers\"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":44,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1EGO"}],"reference_id":"1304339","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P68688","date":"2018-08-07T22:22:56.000Z","acc":"P68688","name":"Glutaredoxin 1","length":85,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI00001112E0","genes":[{"name":{"value":"grxA"},"synonyms":[{"value":"grx"}],"olnNames":[{"value":"b0849"},{"value":"JW0833"}]}],"alphafold_very_low_content":0.011764705882352941,"disorder_content":0.18823529411764706,"disprot_consensus":{"full":[{"start":44,"end":59,"type":"D"}],"Structural state":[{"start":44,"end":59,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00881","name":"Nitroreductase family","start":98,"end":267}],"gene3D":[{"start":71,"end":288,"id":"3.40.109.10","name":"NADH Oxidase"}]},"uniref50":"UniRef50_Q6PHW0","sequence":"MYFLTPILVAILCILVVWIFKNADRSMEKKKGEPRTRAEARPWVDEDLKDSSDLHQAEEDADEWQESEENVEHIPFSHNHYPEKEMVKRSQEFYELLNKRRSVRFISNEQVPMEVIDNVIRTAGTAPSGAHTEPWTFVVVKDPDVKHKIRKIIEEEEEINYMKRMGHRWVTDLKKLRTNWIKEYLDTAPILILIFKQVHGFAANGKKKVHYYNEISVSIACGILLAALQNAGLVTVTTTPLNCGPRLRVLLGRPAHEKLLMLLPVGYPSKEATVPDLKRKPLDQIMVTV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q6PHW0","disprot_id":"DP01741","ncbi_taxon_id":9606,"regions_counter":5,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":70,"region_id":"DP01741r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"A switch between one- and two-electron chemistry of the human flavoprotein iodotyrosine deiodinase is controlled by substrate. <i> Hu J, Chuenchor W, Rokita SE. </i> J Biol Chem, 2015","statement":[{"text":"Missing electron density","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":32,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4TTB;PDB:4TTC"}],"reference_id":"25395621","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":178,"region_id":"DP01741r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"A switch between one- and two-electron chemistry of the human flavoprotein iodotyrosine deiodinase is controlled by substrate. <i> Hu J, Chuenchor W, Rokita SE. </i> J Biol Chem, 2015","statement":[{"text":"Authors said \"However, electron density for residues 161–178 and 199–211 was not observed in the absence of bound I-Tyr. This is presumably due to disorder and/or dynamics of these regions. \"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":161,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4TTB"}],"reference_id":"25395621","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":178,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"A switch between one- and two-electron chemistry of the human flavoprotein iodotyrosine deiodinase is controlled by substrate. <i> Hu J, Chuenchor W, Rokita SE. </i> J Biol Chem, 2015","statement":[{"text":"About these regions, the authos claimed \"However,\nthese regions were evident from a co-crystal containing I-Tyr. Under these conditions, a helix and loop surrounding the active site are stabilized. The helix in particular covers the active site and helps to sequester the I-TyrFMN complex from solvent\"","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"amonzon","start":161,"term_ontology":"IDPO","curator_name":"Alex Monzon","reference_id":"25395621","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01741r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":211,"region_id":"DP01741r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"A switch between one- and two-electron chemistry of the human flavoprotein iodotyrosine deiodinase is controlled by substrate. <i> Hu J, Chuenchor W, Rokita SE. </i> J Biol Chem, 2015","statement":[{"text":"Authors said \"However, electron density for residues 161–178 and 199–211 was not observed in the absence of bound I-Tyr. This is presumably due to disorder and/or dynamics of these regions. \"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":199,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4TTB"}],"reference_id":"25395621","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":211,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"A switch between one- and two-electron chemistry of the human flavoprotein iodotyrosine deiodinase is controlled by substrate. <i> Hu J, Chuenchor W, Rokita SE. </i> J Biol Chem, 2015","statement":[{"text":"About these regions, the authos claimed \"However,\nthese regions were evident from a co-crystal containing I-Tyr. Under these conditions, a helix and loop surrounding the active site are stabilized. The helix in particular covers the active site and helps to sequester the I-TyrFMN complex from solvent\"","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"amonzon","start":199,"term_ontology":"IDPO","curator_name":"Alex Monzon","reference_id":"25395621","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01741r005","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_Q6PHW0","date":"2018-08-07T22:41:22.000Z","acc":"Q6PHW0","name":"Iodotyrosine deiodinase 1","length":289,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00001BDB39","genes":[{"name":{"value":"IYD","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"25395621","url":"http://www.ncbi.nlm.nih.gov/pubmed/25395621","alternativeUrl":"https://europepmc.org/abstract/MED/25395621"}}]},"synonyms":[{"value":"C6orf71"},{"value":"DEHAL1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15289438","url":"http://www.ncbi.nlm.nih.gov/pubmed/15289438","alternativeUrl":"https://europepmc.org/abstract/MED/15289438"}}]}]}],"alphafold_very_low_content":0.09342560553633218,"disorder_content":0.2422145328719723,"disprot_consensus":{"full":[{"start":32,"end":70,"type":"D"},{"start":161,"end":178,"type":"T"},{"start":199,"end":211,"type":"T"}],"Structural state":[{"start":32,"end":70,"type":"D"},{"start":161,"end":178,"type":"D"},{"start":199,"end":211,"type":"D"}],"Structural transition":[{"start":161,"end":178,"type":"T"},{"start":199,"end":211,"type":"T"}]}},{"features":{"pfam":[{"id":"PF01527","name":"Transposase","start":4,"end":76}],"gene3D":[{"start":7,"end":89,"id":"1.10.10.60","name":"Homeodomain-like"}]},"uniref50":"UniRef50_Q8NM20","sequence":"MPTKTYSEEFKRDAVALYENSDGASLQQIANDLGINRVTLKNWIIKYGSNHNVQGTTPSAAVSEAEQIRQLKKENALQRARTRHPAESC","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Corynebacteriaceae","Corynebacterium"],"uniref90":"UniRef90_Q8NM20","disprot_id":"DP01742","ncbi_taxon_id":196627,"regions_counter":1,"creator":"akajava","regions":[{"region_id":"DP01742r001","ec_ontology":"ECO","end":89,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":52,"version":3,"statement":[{"text":"The intrinsically flexible nature of the C-terminal segment (52–97) was confirmed by the observation of quite intense peaks in 2D [15N,1H]-HSQC, which reflect long T2-spin relaxation times arising from large scale and rapid motional modes superimposed onto the overall rotational tumbling.\n","type":"Results"},{"text":"The residues the authors are referring to corresponds to the 52-89 region of this Uniprot.","type":"Curator statement"}],"term_name":"disorder","reference_html":"NMR structure of protein Cgl2762 from Corynebacterium glutamicum implicated in DNA transposition reveals a helix-turn-helix motif attached to a flexibly disordered leucine zipper. <i> Singarapu KK, Xiao R, Sukumaran DK, Acton T, Montelione GT, Szyperski T. </i> Proteins, 2008","released":"2022_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18175328","date":"2022-08-26T14:16:43.009Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2JN6"},{"db":"BMRB","id":"15086"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"sequence_construct":"MPTKTYSEEFKRDAVALYENSDGASLQQIANDLGINRVTLKNWIIKYGSNHNVQGTTPSAAVSEAEQIRQLKKENALQRARTRHPAESCLEHHHHHH"}],"released":"2018_11","uniref100":"UniRef100_Q8NM20","date":"2018-08-08T08:09:17.000Z","acc":"Q8NM20","name":"Uncharacterized protein","length":89,"organism":"Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)","dataset":[],"UniParc":"UPI000003AA36","genes":[{"olnNames":[{"value":"Cgl2762","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAC00156.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAC00156.1"}}]}]}],"alphafold_very_low_content":0.2696629213483146,"disorder_content":0.42696629213483145,"disprot_consensus":{"full":[{"start":52,"end":89,"type":"D"}],"Structural state":[{"start":52,"end":89,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00787","name":"PX domain","start":183,"end":296}]},"uniref50":"UniRef50_Q07528","sequence":"MSDLNDVQENAKLNSETRNTGKAEPPHGTTEYVAEAEISKNGVGSPKKSPKKGKVGKGDNNKVETELVHTALLEKDNPFMEEGPTGFTKSALLEIPGMRSHNLKNPNEDYEDDSEGLLPLNQESNAETCRTSLSGSINSMNGETSASEEPSVSNRKKSARIHILEAKRVSEGQGRAYIAYVIQFENSTVQRRYSDFESLRSILIRLFPMTLIPPIPEKQSIKNYGKSITGSSSKYLLPSEGSGSVDLSLSVIHASVNNSDEKLIRHRIRMLTEFLNKLLTNEEITKTSIITDFLDPNNHNWHEFVNSSSTFSSLPKSILQCNPLDPTNTTRIHAMLPIPGSSSQLLLNKESNDKKMDKERSKSFTNIEQDYKQYENLLDNGIYKYNRRTTKTYHDLKSDYNEIGEVFAQFAHEQAQVGELAEQLSYLSNAFSGSSISLEKLVGRLYYNINEPLNESVHMATSARELIKYRKLKYLQNEMIKKSLNSKRAQLEKLEAQNNEYKDVDKIIDNEMSKSHTINLERPNNNTGSGGKSYGGKLFNGFNKLASMVKDSVKYQETDPHTASINLKKEIEQLSESLEVTENDLEVISKVIKNDQLPKFSKEREVDLSEILKHYSRYMRNYARQNLEIWKEVKRHQDFA","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q07528","disprot_id":"DP01744","ncbi_taxon_id":559292,"regions_counter":5,"creator":"emaiani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":160,"region_id":"DP01744r001","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Structure and function of yeast Atg20, a sorting nexin that facilitates autophagy induction. <i> Popelka H, Damasio A, Hinshaw JE, Klionsky DJ, Ragusa MJ. </i> Proc Natl Acad Sci U S A, 2017","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-08-29T21:06:46.656Z","reference_source":"pmid","term_name":"disorder","reference_id":"29114050","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"CD spectra shows this region is disordered.","type":"Curator statement"}]},{"start":1,"end":160,"reference_id":"29114050","reference_source":"pmid","reference_html":"Structure and function of yeast Atg20, a sorting nexin that facilitates autophagy induction. <i> Popelka H, Damasio A, Hinshaw JE, Klionsky DJ, Ragusa MJ. </i> Proc Natl Acad Sci U S A, 2017","date":"2023-08-29T21:04:42.263Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01744r002","statement":[{"text":"The 1D 1H NMR spectra of Atg20[FR] (Fig. 2B, Right) also exhibits poor dispersion in the amide region, further confirming that the N terminus of Atg20 is disordered.","type":"Results"}]},{"start":1,"end":160,"reference_id":"29114050","reference_source":"pmid","reference_html":"Structure and function of yeast Atg20, a sorting nexin that facilitates autophagy induction. <i> Popelka H, Damasio A, Hinshaw JE, Klionsky DJ, Ragusa MJ. </i> Proc Natl Acad Sci U S A, 2017","date":"2023-08-29T21:17:58.670Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1_Arg160del","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q12527","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01744r003","statement":[{"text":"Atg20 was tagged on the N terminus with protein A (PA), and was used for affinity isolation of HA-tagged Atg11. We found that the Atg20 FR was required for efficient binding to Atg11 (Fig. 3A)","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":139,"end":145,"reference_id":"29114050","reference_source":"pmid","reference_html":"Structure and function of yeast Atg20, a sorting nexin that facilitates autophagy induction. <i> Popelka H, Damasio A, Hinshaw JE, Klionsky DJ, Ragusa MJ. </i> Proc Natl Acad Sci U S A, 2017","date":"2023-08-29T21:20:35.825Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01744r004","statement":[{"text":" Atg20 is phosphorylated on Ser139, Thr144, Ser145, Ser307, Ser342, Ser343, and Thr517, all of which are previously unreported phosphorylation sites mediated by unknown kinases. In addition to these sites, our MS analysis also detected phosphorylation on Ser45 and Ser49, which are targeted by Cdc28/Cdk1 (31), and on Ser363 and Thr365, sites recognized by casein kinase 2 (CK2) (32), in agreement with previous high-throughput studies.","type":"Results"}]},{"start":45,"end":49,"reference_id":"29114050","reference_source":"pmid","reference_html":"Structure and function of yeast Atg20, a sorting nexin that facilitates autophagy induction. <i> Popelka H, Damasio A, Hinshaw JE, Klionsky DJ, Ragusa MJ. </i> Proc Natl Acad Sci U S A, 2017","date":"2023-08-29T21:20:47.472Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01744r005","statement":[{"text":" Atg20 is phosphorylated on Ser139, Thr144, Ser145, Ser307, Ser342, Ser343, and Thr517, all of which are previously unreported phosphorylation sites mediated by unknown kinases. In addition to these sites, our MS analysis also detected phosphorylation on Ser45 and Ser49, which are targeted by Cdc28/Cdk1 (31), and on Ser363 and Thr365, sites recognized by casein kinase 2 (CK2) (32), in agreement with previous high-throughput studies.","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_Q07528","date":"2018-08-08T08:39:03.000Z","acc":"Q07528","name":"Autophagy-related protein 20","length":640,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000006BC72","genes":[{"name":{"value":"ATG20"},"synonyms":[{"value":"CVT20"},{"value":"SNX42"}],"olnNames":[{"value":"YDL113C"}]}],"alphafold_very_low_content":0.315625,"disorder_content":0.25,"disprot_consensus":{"full":[{"start":1,"end":160,"type":"D"}],"Structural state":[{"start":1,"end":160,"type":"D"}],"Molecular function":[{"start":1,"end":160,"type":"F"}],"Disorder function":[{"start":45,"end":49,"type":"F"},{"start":139,"end":145,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00992","name":"Troponin","start":15,"end":145}],"gene3D":[{"start":2,"end":161,"id":"1.20.5.350","name":"1.20.5.350"}]},"uniref50":"UniRef50_P48788","sequence":"MGDEEKRNRAITARRQHLKSVMLQIAATELEKEESRREAEKQNYLAEHCPPLHIPGSMSEVQELCKQLHAKIDAAEEEKYDMEVRVQKTSKELEDMNQKLFDLRGKFKRPPLRRVRMSADAMLKALLGSKHKVCMDLRANLKQVKKEDTEKERDLRDVGDWRKNIEEKSGMEGRKKMFESES","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P48788","disprot_id":"DP01747","ncbi_taxon_id":9606,"regions_counter":2,"creator":"lalvarez","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":182,"region_id":"DP01747r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Dynamics of the C-terminal region of TnI in the troponin complex in solution. <i> Blumenschein TM, Stone DB, Fletterick RJ, Mendelson RA, Sykes BD. </i> Biophys J, 2006","statement":[{"text":"The high intensity of the peaks corresponding to the C-terminal region of TnI, relative to the size of the troponin complex and the intensity of peaks from other regions of the protein, suggests that this is a very flexible region which moves independently from the rest of the complex.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"lalvarez","start":97,"term_ontology":"IDPO","curator_name":"Lucía Álvarez","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-1437-5773","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"16415057","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":182,"region_id":"DP01747r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Is there nascent structure in the intrinsically disordered region of troponin I? <i> Julien O, Mercier P, Allen CN, Fisette O, Ramos CH, Lagüe P, Blumenschein TM, Sykes BD. </i> Proteins, 2011","statement":[{"text":"Although the relaxation data clearly show that this region is flexible, one possibility to explain the presence of the plateau is the presence of some sort of nascent structure. A second possibility is that this profile is an intrinsic property of disordered regions in general. We found that similar results can be recognized in other IDRs attached to globular domains using 15N relaxation data.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"lalvarez","start":98,"term_ontology":"IDPO","curator_name":"Lucía Álvarez","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-1437-5773","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21322033","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P48788","date":"2018-08-08T10:16:53.000Z","acc":"P48788","name":"Troponin I, fast skeletal muscle","length":182,"organism":"Homo sapiens","dataset":["Stress response proteins"],"UniParc":"UPI00001373A8","genes":[{"name":{"value":"TNNI2"}}],"alphafold_very_low_content":0.04395604395604396,"disorder_content":0.4725274725274725,"disprot_consensus":{"full":[{"start":97,"end":182,"type":"D"}],"Structural state":[{"start":97,"end":182,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00362","name":"Integrin beta chain VWA domain","start":138,"end":382},{"id":"PF07965","name":"Integrin beta tail domain","start":639,"end":727},{"id":"PF07974","name":"EGF-like domain","start":599,"end":630},{"id":"PF08725","name":"Integrin beta cytoplasmic domain","start":752,"end":795},{"id":"PF17205","name":"Integrin plexin domain","start":25,"end":76},{"id":"PF18372","name":"Integrin beta epidermal growth factor like domain 1","start":466,"end":495},{"id":"PF23105","name":"Integrin EGF domain","start":511,"end":554}],"gene3D":[{"start":145,"end":379,"id":"3.40.50.410","name":"von Willebrand factor, type A domain"},{"start":638,"end":725,"id":"3.10.450.180","name":"3.10.450.180"},{"start":508,"end":556,"id":"2.10.25.10","name":"Laminin"},{"start":82,"end":144,"id":"2.60.40.1510","name":"ntegrin, alpha v. Chain A, domain 3"},{"start":462,"end":503,"id":"2.10.25.10","name":"Laminin"},{"start":726,"end":798,"id":"1.20.5.100","name":"Cytochrome c1, transmembrane anchor, C-terminal"},{"start":557,"end":591,"id":"2.10.25.10","name":"Laminin"},{"start":21,"end":81,"id":"3.30.1680.10","name":"ligand-binding face of the semaphorins, domain 2"},{"start":595,"end":636,"id":"2.10.25.10","name":"Laminin"}]},"uniref50":"UniRef50_P05556","sequence":"MNLQPIFWIGLISSVCCVFAQTDENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCPPDDIENPRGSKDIKKNKNVTNRSKGTAEKLKPEDITQIQPQQLVLRLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTNKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNMYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYKELKNLIPKSAVGTLSANSSNVIQLIIDAYNSLSSEVILENGKLSEGVTISYKSYCKNGVNGTGENGRKCSNISIGDEVQFEISITSNKCPKKDSDSFKIRPLGFTEEVEVILQYICECECQSEGIPESPKCHEGNGTFECGACRCNEGRVGRHCECSTDEVNSEDMDAYCRKENSSEICSNNGECVCGQCVCRKRDNTNEIYSGKFCECDNFNCDRSNGLICGGNGVCKCRVCECNPNYTGSACDCSLDTSTCEASNGQICNGRGICECGVCKCTDPKFQGQTCEMCQTCLGVCAEHKECVQCRAFNKGEKKDTCTQECSYFNITKVESRDKLPQPVQPDPVSHCKEKDVDDCWFYFTYSVNGNNEVMVHVVENPECPTGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDTGENPIYKSAVTTVVNPKYEGK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P05556","disprot_id":"DP01748","ncbi_taxon_id":9606,"regions_counter":14,"creator":"bmesza","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":798,"region_id":"DP01748r002","reference_id":"12500944","start":752,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The spectra  recorded  for  the b1wt peptide showed no distinct minima at 222 nm and a strong minimum at ~200 nm (Fig.8A ), indicating that the b1wt peptide contains little a-helix (~13% by  least-squared regression analysis).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"reference_html":"The integrin beta1 subunit cytoplasmic tail forms oligomers: a potential role in beta1 integrin clustering. <i> Laplantine E, Maurer P, Vallar L, Eble J, Paulsson M, Bruckner P, Kieffer N, Aumailley M. </i> Biol Cell, 2002","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P05556","partner_end":null}],"ec_ontology":"ECO","end":798,"region_id":"DP01748r003","reference_id":"12500944","start":752,"term_id":"GO:0005515","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The integrin b1 cytoplasmic tails self-interact in a specific and dose-dependent manner as shown  by surface plasmon resonance analysis.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"surface plasmon resonance evidence used in manual assertion","version":4,"reference_html":"The integrin beta1 subunit cytoplasmic tail forms oligomers: a potential role in beta1 integrin clustering. <i> Laplantine E, Maurer P, Vallar L, Eble J, Paulsson M, Bruckner P, Kieffer N, Aumailley M. </i> Biol Cell, 2002","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001269","term_name":"protein binding","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"O14713","partner_end":null}],"ec_ontology":"ECO","end":798,"region_id":"DP01748r004","start":784,"term_id":"GO:0005515","statement":[{"text":"We present cocrystal structures of KRIT1 with ICAP1 and ICAP1 with integrin β1 cytoplasmic tail to 2.54 and 3.0 Å resolution (the resolutions at which I/σI = 2 are 2.75 and 3.0 Å, respectively).","type":"Abstract"}],"curator_id":"bmesza","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"23317506","version":3,"reference_html":"Mechanism for KRIT1 release of ICAP1-mediated suppression of integrin activation. <i> Liu W, Draheim KM, Zhang R, Calderwood DA, Boggon TJ. </i> Mol Cell, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4DX9"}],"term_name":"protein binding","curator_orcid":"0000-0003-0919-4449","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":798,"region_id":"DP01748r005","reference_id":"23317506","start":784,"term_id":"IDPO:0000011","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"We present co-crystal structures of KRIT1 with ICAP1 and ICAP1 with integrin β1 cytoplasmic tail to 2.54 Å and 3.0 Å resolution (the resolutions at which I/σI = 2 are 2.75 Å and 3.0 Å, respectively). ","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"x-ray crystallography evidence used in manual assertion","version":3,"reference_html":"Mechanism for KRIT1 release of ICAP1-mediated suppression of integrin activation. <i> Liu W, Draheim KM, Zhang R, Calderwood DA, Boggon TJ. </i> Mol Cell, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4DX9"}],"term_name":"disorder to order","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q71LX4","partner_end":null}],"ec_ontology":"ECO","end":795,"region_id":"DP01748r006","start":752,"term_id":"GO:0005515","statement":[{"text":"Here, we report the first structure of talin bound to an authentic full-length beta integrin tail.","type":"Abstract"}],"curator_id":"bmesza","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"19798053","version":3,"reference_html":"The structure of an integrin/talin complex reveals the basis of inside-out signal transduction. <i> Anthis NJ, Wegener KL, Ye F, Kim C, Goult BT, Lowe ED, Vakonakis I, Bate N, Critchley DR, Ginsberg MH, Campbell ID. </i> EMBO J, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"3G9W"}],"term_name":"protein binding","curator_orcid":"0000-0003-0919-4449","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":796,"region_id":"DP01748r007","reference_id":"19798053","start":792,"term_id":"IDPO:0000039","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"We used high-resolution mass spectrometry to identify3600 lysine acetylation sites on 1750 proteins and quantified acetylation changes in responseto the deacetylase inhibitors suberoylanilide hydroxamic acid and MS-275.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"mass spectrometry evidence used in manual assertion","version":3,"reference_html":"The structure of an integrin/talin complex reveals the basis of inside-out signal transduction. <i> Anthis NJ, Wegener KL, Ye F, Kim C, Goult BT, Lowe ED, Vakonakis I, Bate N, Critchley DR, Ginsberg MH, Campbell ID. </i> EMBO J, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001230","term_name":"acetylation display site","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P42684","partner_end":null}],"ec_ontology":"ECO","end":798,"region_id":"DP01748r009","reference_id":"25694433","start":752,"term_id":"GO:0005515","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"We report here that the Arg kinase domain interacts directly with a lysine-rich membrane-proximal segment in the integrin β1 cytoplasmic tail, that Arg phosphorylates the membrane-proximal Tyr-783 in the β1 tail, and that the Arg Src homology domain then engages this phosphorylated region in the tail.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","version":4,"reference_html":"Direct interactions with the integrin β1 cytoplasmic tail activate the Abl2/Arg kinase. <i> Simpson MA, Bradley WD, Harburger D, Parsons M, Calderwood DA, Koleske AJ. </i> J Biol Chem, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006077","term_name":"protein binding","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":791,"region_id":"DP01748r010","reference_id":"25278023","start":786,"term_id":"IDPO:0000045","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The amounts of integrin β1 and phosphorylated Thr-788/Thr-789 β1 were detected by immunoblotting in cells with or without SDF1-α activation.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"immunodetection assay evidence used in manual assertion","version":3,"reference_html":"Specific phosphorylations transmit signals from leukocyte β2 to β1 integrins and regulate adhesion. <i> Uotila LM, Jahan F, Soto Hinojosa L, Melandri E, Grönholm M, Gahmberg CG. </i> J Biol Chem, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","term_name":"phosphorylation display site","ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":787,"region_id":"DP01748r011","reference_id":"19555977","start":783,"term_id":"IDPO:0000045","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Preventing Ser-785 or Thr 788/789 phosphorylation reduced adhesion, suggesting that phosphorylation regulates adhesiveness.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"mutant phenotype evidence used in manual assertion","version":3,"reference_html":"The effects of increased extracellular deformation, pressure, and integrin phosphorylation on fibroblast migration. <i> Flanigan TL, Craig DH, Gayer CP, Basson MD. </i> J Surg Res, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000315","term_name":"phosphorylation display site","ec_go":"IMP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":785,"region_id":"DP01748r012","reference_id":"25694433","start":781,"term_id":"IDPO:0000045","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"We report here that the Arg kinase domain interacts directly with a lysine-rich membrane-proximal segment in the integrin β1 cytoplasmic tail, that Arg phosphorylates the membrane-proximal Tyr-783 in the β1 tail, and that the Arg Src homology domain then engages this phosphorylated region in the tail.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"immunodetection assay evidence used in manual assertion","version":3,"reference_html":"Direct interactions with the integrin β1 cytoplasmic tail activate the Abl2/Arg kinase. <i> Simpson MA, Bradley WD, Harburger D, Parsons M, Calderwood DA, Koleske AJ. </i> J Biol Chem, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","term_name":"phosphorylation display site","ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":797,"region_id":"DP01748r013","reference_id":"10891511","start":793,"term_id":"IDPO:0000045","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Focal adhesion kinase (FAK) tyrosine phosphorylation and activation were severely impaired in response to beta1-dependent adhesion in GD25-beta1A(Y783/795F) cells compared to that in wild-type GD25-beta1A or mutants in which only a single tyrosine was altered (beta1A(Y783F) or beta1A(Y795F)). ","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"mutant phenotype evidence used in manual assertion","version":3,"reference_html":"The cytoplasmic tyrosines of integrin subunit beta1 are involved in focal adhesion kinase activation. <i> Wennerberg K, Armulik A, Sakai T, Karlsson M, Fässler R, Schaefer EM, Mosher DF, Johansson S. </i> Mol Cell Biol, 2000","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000315","term_name":"phosphorylation display site","ec_go":"IMP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":798,"region_id":"DP01748r014","reference_id":"12500944","start":752,"term_id":"IDPO:0000060","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The integrin b1 cytoplasmic tails self-interact in a specific and dose-dependent manner as shown by surface plasmon resonance analysis.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"surface plasmon resonance evidence used in manual assertion","version":4,"reference_html":"The integrin beta1 subunit cytoplasmic tail forms oligomers: a potential role in beta1 integrin clustering. <i> Laplantine E, Maurer P, Vallar L, Eble J, Paulsson M, Bruckner P, Kieffer N, Aumailley M. </i> Biol Cell, 2002","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001269","term_name":"self-assembly","ec_go":"IPI","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_P05556","date":"2018-08-08T11:43:34.000Z","acc":"P05556","name":"Integrin beta-1","length":798,"organism":"Homo sapiens","dataset":["Autophagy-related proteins"],"UniParc":"UPI0000034A0F","genes":[{"name":{"value":"ITGB1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6153","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6153"}}]},"synonyms":[{"value":"FNRB"},{"value":"MDF2"},{"value":"MSK12"}]}],"alphafold_very_low_content":0.03759398496240601,"disorder_content":0.05889724310776942,"disprot_consensus":{"full":[{"start":752,"end":783,"type":"D"},{"start":784,"end":798,"type":"T"}],"Structural state":[{"start":752,"end":798,"type":"D"}],"Molecular function":[{"start":752,"end":798,"type":"F"}],"Structural transition":[{"start":784,"end":798,"type":"T"}],"Disorder function":[{"start":752,"end":798,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00178","name":"Ets-domain","start":610,"end":690},{"id":"PF02198","name":"Sterile alpha motif (SAM)/Pointed domain","start":167,"end":249}],"gene3D":[{"start":594,"end":711,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"start":155,"end":252,"id":"1.10.150.50","name":"Transcription Factor, Ets-1"}]},"uniref50":"UniRef50_P51023","sequence":"MELAICKTDLSATKFMLPPALPSSAAIGSSSAVASTASHFLDKAAHELFQLNAINGHLFKSPASSHLNSVGSPSILSQLNGIGNSGNHSGQVSTMRLKKNRKVTFLSSLVESKNIFIKEEPIHGCKDLCSLSDISDHEASLEVPTALPPLTPGTNRKVNEVLKASFASWEKEVQKCNITKDPREWTEEHVIYWLNWAKNEFSLVSMNLDPFYKMKGRAMVDLGKEKFLAITPPFTGDILWEHLDILQKDCEKPNEDIVHGNSFESATTASVCGSDHQVANYPNETHANSNNSSINSRLSMDYVTSAGNSDNKNFHRATPHSHNGYNTSNTHDRINNSTPPQQQQSQQPTVNGSGSASSNNNNSMLPPAVQQSNNENNNTSSSNTNNSSNNNNNSGGSNNSNAGSNNNNNNNNNINFMAAAAIFQHHLKEEPGTQNGNIGGYGGGSNSQNDPTDLSSYGLPAHLAAYGGGSGSGPTGGRSSGGGGDESDYHSTISAQDHQSQQSSGGNGSGGASGGSTGNSNGYLDSSSEFYGSYAGRNRFHDGYPPEFTPYDAQSFQSMGPQPTAMDQWGAAHAHQHPAAYMSTLGLDKGLLGGYTTQGGVPCFTGSGPIQLWQFLLELLLDKTCQSFISWTGDGWEFKLTDPDEVARRWGIRKNKPKMNYEKLSRGLRYYYDKNIIHKTAGKRYVYRFVCDLQNLVGHTPEELVAKYDLKIEKKDVD","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_P51023","disprot_id":"DP01749","ncbi_taxon_id":7227,"regions_counter":1,"creator":"emaiani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":158,"region_id":"DP01749r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The PNT domain from Drosophila pointed-P2 contains a dynamic N-terminal helix preceded by a disordered phosphoacceptor sequence. <i> Lau DK, Okon M, McIntosh LP. </i> Protein Sci, 2012","term_id":"IDPO:0000002","curator_id":"emaiani","start":142,"term_ontology":"IDPO","curator_name":"Emiliano Maiani","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1432-5394","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22936607","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P51023","date":"2018-08-08T12:33:28.000Z","acc":"P51023","name":"ETS-like protein pointed","length":718,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI000016BD01","genes":[{"name":{"value":"pnt","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0003118","url":"http://flybase.org/reports/FBgn0003118.html"}}]},"synonyms":[{"value":"DMPOINT1A","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0003118","url":"http://flybase.org/reports/FBgn0003118.html"}}]},{"value":"ETS2","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0003118","url":"http://flybase.org/reports/FBgn0003118.html"}}]},{"value":"Ets58AB","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"2834248","url":"http://www.ncbi.nlm.nih.gov/pubmed/2834248","alternativeUrl":"https://europepmc.org/abstract/MED/2834248"}}]},{"value":"pointed","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0003118","url":"http://flybase.org/reports/FBgn0003118.html"}}]}],"orfNames":[{"value":"CG17077"}]}],"alphafold_very_low_content":0.7033426183844012,"disorder_content":0.023676880222841225,"disprot_consensus":{"full":[{"start":142,"end":158,"type":"D"}],"Structural state":[{"start":142,"end":158,"type":"D"}]}},{"features":{"pfam":[{"id":"PF12678","name":"RING-H2 zinc finger domain","start":40,"end":98}],"gene3D":[{"start":10,"end":108,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"}]},"uniref50":"UniRef50_P62877","sequence":"MAAAMDVDTPSGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P62877","disprot_id":"DP01750","ncbi_taxon_id":9606,"regions_counter":8,"creator":"emaiani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":39,"region_id":"DP01750r001","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Selective recruitment of an E2~ubiquitin complex by an E3 ubiquitin ligase. <i> Spratt DE, Wu K, Kovacev J, Pan ZQ, Shaw GS. </i> J Biol Chem, 2012","term_id":"IDPO:0000002","curator_id":"vnugnes","start":12,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":6,"curator_orcid":"0000-0001-8399-7907","date":"2023-11-30T14:29:00.138Z","reference_source":"pmid","term_name":"disorder","reference_id":"22433864","cross_refs":[{"db":"PDB","id":"2LGV"}],"statement":[{"text":"The structure also shows that residues Gly-12–Val-39 at the N terminus of sRbx112–108 are disordered, as indicated from a lack of inter-residue or long distance NOEs and near zero or negative 15N{1H} heteronuclear NOEs (supplemental Fig. 1).","type":"Results"},{"text":"Taken together, these data suggest that residues Gly-12–Val-39 at the N terminus of sRbx112–108 in the absence of a bound cullin molecule are disordered.","type":"Results"},{"text":"Four residues (W27S, V30S, L32Q, and W33S) were mutated in order to improve the solubility.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Tyr27Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"To improve the solubility of Rbx1/ROC112–108, four mutations (W27S, V30S, L32Q, and W33S) were incorporated into the N-terminal region of Rbx1/ROC1 that was predicted to have aggregation propensity by the online algorithm TANGO (20–22)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val30Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"To improve the solubility of Rbx1/ROC112–108, four mutations (W27S, V30S, L32Q, and W33S) were incorporated into the N-terminal region of Rbx1/ROC1 that was predicted to have aggregation propensity by the online algorithm TANGO (20–22)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu32Gln","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"To improve the solubility of Rbx1/ROC112–108, four mutations (W27S, V30S, L32Q, and W33S) were incorporated into the N-terminal region of Rbx1/ROC1 that was predicted to have aggregation propensity by the online algorithm TANGO (20–22)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Tyr33Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"To improve the solubility of Rbx1/ROC112–108, four mutations (W27S, V30S, L32Q, and W33S) were incorporated into the N-terminal region of Rbx1/ROC1 that was predicted to have aggregation propensity by the online algorithm TANGO (20–22)."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-15T10:14:23.772Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":39,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Selective recruitment of an E2~ubiquitin complex by an E3 ubiquitin ligase. <i> Spratt DE, Wu K, Kovacev J, Pan ZQ, Shaw GS. </i> J Biol Chem, 2012","statement":[{"text":"The structure shows that the N terminus of Rbx1/ROC1 undergoes a large structural rearrangement from a disordered conformation to a structured β-strand in the CRL complex.","type":"Results"},{"text":"Structures of Rbx1/ROC1 in complex with cullin proteins show that the N terminus of Rbx1/ROC1 forms an ordered 16-residue intermolecular β-sheet with the C-terminal domain of the cullin scaffold protein (Fig. 2C; Ref 7).","type":"Results"},{"text":"Combining these results, we suggest that the N terminus of Rbx1/ROC1 undergoes a dramatic disordered-to-ordered conformational transition that is induced by protein-protein interactions with CUL1 (Fig. 2, A and C).","type":"Results"},{"text":"Four residues (W27S, V30S, L32Q, and W33S) were mutated in order to improve the solubility.","type":"Curator statement"}],"term_id":"IDPO:0000011","curator_id":"esalladini","start":12,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"22433864","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01750r002","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-07-20T13:21:08.600Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":12,"end":39,"reference_id":"11961546","reference_source":"pmid","reference_html":"Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. <i> Zheng N, Schulman BA, Song L, Miller JJ, Jeffrey PD, Wang P, Chu C, Koepp DM, Elledge SJ, Pagano M, Conaway RC, Conaway JW, Harper JW, Pavletich NP. </i> Nature, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1LDK"},{"db":"PDB","id":"1LDJ"}],"region_id":"DP01750r005","statement":[{"text":"The 16-residue Rbx1 β strand, which contains a kink in the middle, makes β-sheet backbone hydrogen bonds with the S1, S2 and S3 strands of Cul1, and it participates in the formation of the α/β hydrophobic core. The conserved Phe 22 and Trp 27 of Rbx1 have a central role, making multiple van der Waals contacts to side chains from the WH-A, H25, S1, S2 and S3 of Cul1 (Fig. 3b). The Cul1 residues involved in these interactions are highly conserved in Cul1 orthologues and paralogues (Fig. 3b and see Supplementary Information), indicating that other combinations of cullin and Rbx family members will form a similar intermolecular β-sheet. After the Rbx1 β strand, a tryptophan-rich Rbx1 region (Trp 33–Ala 34–Trp 35) packs both with the α/β domain and the following RING domain, resulting in a continuous surface between the two.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-07-20T13:10:59.926Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":12,"end":39,"reference_id":"11961546","reference_source":"pmid","reference_html":"Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. <i> Zheng N, Schulman BA, Song L, Miller JJ, Jeffrey PD, Wang P, Chu C, Koepp DM, Elledge SJ, Pagano M, Conaway RC, Conaway JW, Harper JW, Pavletich NP. </i> Nature, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"1LDK"},{"db":"PDB","id":"1LDJ"}],"interaction_partner":[{"db":"UniProt","id":"Q13616","partner_start":null,"partner_end":null}],"region_id":"DP01750r006","statement":[{"text":"The 16-residue Rbx1 β strand, which contains a kink in the middle, makes β-sheet backbone hydrogen bonds with the S1, S2 and S3 strands of Cul1, and it participates in the formation of the α/β hydrophobic core. The conserved Phe 22 and Trp 27 of Rbx1 have a central role, making multiple van der Waals contacts to side chains from the WH-A, H25, S1, S2 and S3 of Cul1 (Fig. 3b). The Cul1 residues involved in these interactions are highly conserved in Cul1 orthologues and paralogues (Fig. 3b and see Supplementary Information), indicating that other combinations of cullin and Rbx family members will form a similar intermolecular β-sheet. After the Rbx1 β strand, a tryptophan-rich Rbx1 region (Trp 33–Ala 34–Trp 35) packs both with the α/β domain and the following RING domain, resulting in a continuous surface between the two.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-07-20T13:10:50.272Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":12,"end":39,"reference_id":"11961546","reference_source":"pmid","reference_html":"Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. <i> Zheng N, Schulman BA, Song L, Miller JJ, Jeffrey PD, Wang P, Chu C, Koepp DM, Elledge SJ, Pagano M, Conaway RC, Conaway JW, Harper JW, Pavletich NP. </i> Nature, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01750r007","statement":[{"text":"SCF complexes are the largest family of E3 ubiquitin–protein ligases and mediate the ubiquitination of diverse regulatory and signalling proteins.","type":"Abstract"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-07-20T13:10:46.090Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":18,"reference_id":"15537541","reference_source":"pmid","reference_html":"Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases. <i> Goldenberg SJ, Cascio TC, Shumway SD, Garbutt KC, Liu J, Xiong Y, Zheng N. </i> Cell, 2004","date":"2023-11-30T15:00:56.192Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1U6G"}],"region_id":"DP01750r008","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q13616 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q86VP6"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"37255","entry_name":"zinc(1+)"}],"statement":[{"text":"The PDB structure shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-15T10:14:31.217Z"}}],"released":"2018_11","uniref100":"UniRef100_P62877","date":"2018-08-08T13:14:19.000Z","acc":"P62877","name":"E3 ubiquitin-protein ligase RBX1","length":108,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI0000028E5D","genes":[{"name":{"value":"RBX1"},"synonyms":[{"value":"RNF75"},{"value":"ROC1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10230407","url":"http://www.ncbi.nlm.nih.gov/pubmed/10230407","alternativeUrl":"https://europepmc.org/abstract/MED/10230407"}}]}]}],"alphafold_very_low_content":0.08333333333333333,"disorder_content":0.3611111111111111,"disprot_consensus":{"full":[{"start":1,"end":11,"type":"D"},{"start":12,"end":39,"type":"T"}],"Structural state":[{"start":1,"end":39,"type":"D"}],"Structural transition":[{"start":12,"end":39,"type":"T"}],"Molecular function":[{"start":12,"end":39,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00400","name":"WD domain, G-beta repeat","start":230,"end":259},{"id":"PF00400","name":"WD domain, G-beta repeat","start":264,"end":309},{"id":"PF00400","name":"WD domain, G-beta repeat","start":314,"end":351},{"id":"PF00400","name":"WD domain, G-beta repeat","start":360,"end":393},{"id":"PF00400","name":"WD domain, G-beta repeat","start":397,"end":435},{"id":"PF00400","name":"WD domain, G-beta repeat","start":440,"end":477},{"id":"PF00400","name":"WD domain, G-beta repeat","start":482,"end":519},{"id":"PF08799","name":"pre-mRNA processing factor 4 (PRP4) like","start":108,"end":135}],"gene3D":[{"start":78,"end":134,"id":"1.10.720.150","name":"Pre-mRNA processing factor 4 domain"},{"start":135,"end":357,"id":"2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"},{"start":358,"end":522,"id":"2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"}]},"uniref50":"UniRef50_O43172","sequence":"MASSRASSTQATKTKAPDDLVAPVVKKPHIYYGSLEEKERERLAKGESGILGKDGLKAGIEAGNINITSGEVFEIEEHISERQAEVLAEFERRKRARQINVSTDDSEVKACLRALGEPITLFGEGPAERRERLRNILSVVGTDALKKTKKDDEKSKKSKEEYQQTWYHEGPNSLKVARLWIANYSLPRAMKRLEEARLHKEIPETTRTSQMQELHKSLRSLNNFCSQIGDDRPISYCHFSPNSKMLATACWSGLCKLWSVPDCNLLHTLRGHNTNVGAIVFHPKSTVSLDPKDVNLASCAADGSVKLWSLDSDEPVADIEGHTVRVARVMWHPSGRFLGTTCYDRSWRLWDLEAQEEILHQEGHSMGVYDIAFHQDGSLAGTGGLDAFGRVWDLRTGRCIMFLEGHLKEIYGINFSPNGYHIATGSGDNTCKVWDLRQRRCVYTIPAHQNLVTGVKFEPIHGNFLLTGAYDNTAKIWTHPGWSPLKTLAGHEGKVMGLDISSDGQLIATCSYDRTFKLWMAE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O43172","disprot_id":"DP01751","ncbi_taxon_id":9606,"regions_counter":11,"creator":"emaiani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":169,"region_id":"DP01751r001","released":"2024_06","ec_id":"ECO:0006275","reference_html":"The spliceosomal proteins PPIH and PRPF4 exhibit bi-partite binding. <i> Rajiv C, Jackson SR, Cocklin S, Eisenmesser EZ, Davis TL. </i> Biochem J, 2017","statement":[{"text":"Additionally, the large values for the frictional ratio are indicative of highly extended shape in solution, as would be expected from intrinsically disordered regions (IDRs), and this may skew the modeling of s-values, leading to larger than expected molecular mass.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"analytical ultracentrifugation evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-19T14:05:07.053Z","reference_source":"pmid","term_name":"disorder","reference_id":"28935721","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":169,"region_id":"DP01751r002","released":"2024_06","ec_id":"ECO:0006204","reference_html":"The spliceosomal proteins PPIH and PRPF4 exhibit bi-partite binding. <i> Rajiv C, Jackson SR, Cocklin S, Eisenmesser EZ, Davis TL. </i> Biochem J, 2017","term_id":"IDPO:0000003","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-19T14:03:50.902Z","reference_source":"pmid","term_name":"molten globule","reference_id":"28935721","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"PRPF41–169, PRPF4106–169, and PRPF41–98 spectra have a classically ‘irregular’ shape, as evidenced by negative ellipticity values in the far UV.","type":"Results"},{"text":"When compared with a database containing CD spectra of folded and disordered proteins, PRPF41–169 and PRPF41–98 have ellipticity values at 200 and 222 nm that place them in a region where molten globule proteins cluster (Figure 4) [29,30].","type":"Results"}]},{"start":106,"end":169,"reference_id":"28935721","reference_source":"pmid","reference_html":"The spliceosomal proteins PPIH and PRPF4 exhibit bi-partite binding. <i> Rajiv C, Jackson SR, Cocklin S, Eisenmesser EZ, Davis TL. </i> Biochem J, 2017","date":"2024-02-19T14:07:32.290Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"O43447","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01751r003","statement":[{"text":"We found that PRPF41–169 bound to PPIH with a Kd value of 0.5 µM.","type":"Results"},{"text":"We identified very tight binding between PRPF4106–169 and PPIH. The value of Kd of 0.08 µM is significantly higher affinity than that reported for the PRPF4107–136 peptide, and six times tighter than binding to PRPF41–169 (Figure 2).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":106,"end":169,"reference_id":"28935721","reference_source":"pmid","reference_html":"The spliceosomal proteins PPIH and PRPF4 exhibit bi-partite binding. <i> Rajiv C, Jackson SR, Cocklin S, Eisenmesser EZ, Davis TL. </i> Biochem J, 2017","date":"2024-02-19T14:09:37.187Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"O43447","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01751r004","statement":[{"text":"PRPF41–169 interacted with PPIH with an affinity of 0.39 ± 0.04 µM, and PRPF4106–169 with an affinity of 0.08 ± 0.01 µM (Figure 3). These values are quite similar to those obtained by ITC (Figure 2). PRPF41–98 bound to PPIH with a modest Kd value of 10.84 ± 1.37 µM (Figure 3).","type":"Results"},{"text":"SPR confirms bipartite binding between PRPF4 and PPIH","type":"Figure"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":98,"reference_id":"28935721","reference_source":"pmid","reference_html":"The spliceosomal proteins PPIH and PRPF4 exhibit bi-partite binding. <i> Rajiv C, Jackson SR, Cocklin S, Eisenmesser EZ, Davis TL. </i> Biochem J, 2017","date":"2024-02-19T14:09:25.992Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"O43447","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01751r005","statement":[{"text":"PRPF41–169 interacted with PPIH with an affinity of 0.39 ± 0.04 µM, and PRPF4106–169 with an affinity of 0.08 ± 0.01 µM (Figure 3). These values are quite similar to those obtained by ITC (Figure 2). PRPF41–98 bound to PPIH with a modest Kd value of 10.84 ± 1.37 µM (Figure 3).","type":"Results"},{"text":"SPR confirms bipartite binding between PRPF4 and PPIH","type":"Figure"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":169,"reference_id":"28935721","reference_source":"pmid","reference_html":"The spliceosomal proteins PPIH and PRPF4 exhibit bi-partite binding. <i> Rajiv C, Jackson SR, Cocklin S, Eisenmesser EZ, Davis TL. </i> Biochem J, 2017","date":"2024-02-19T14:12:16.130Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01751r006","statement":[{"text":"15N-1H HSQC spectroscopy exhibited a lack of dispersion along the proton axis, and only a limited number of peaks were visible in the spectra — hallmarks of an unfolded protein or IDR (Supplementary Figure S3).","type":"Results"}]},{"start":106,"end":169,"reference_id":"28935721","reference_source":"pmid","reference_html":"The spliceosomal proteins PPIH and PRPF4 exhibit bi-partite binding. <i> Rajiv C, Jackson SR, Cocklin S, Eisenmesser EZ, Davis TL. </i> Biochem J, 2017","date":"2024-02-19T14:18:01.938Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe122Ala","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"O43447","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01751r007","statement":[{"text":"When PRPF41–169 F122A was used as an analyte, there was more than a 10-fold reduction in binding affinity to PPIH (15.6 compared with 0.38 µM). The binding of PRPF4106–169 F122A to wild-type PPIH was also weakened, by ~7-fold (0.63 compared with 0.08 µM). These results confirm the contribution of F122 to high-affinity interaction, although it is not enough to disrupt either complex entirely (Figure 7).","type":"Results"},{"text":"These results indicate that the W133A mutation in PPIH is perturbing an interaction with the PRPF41–98 region, and F122A weakens the interaction with the PRPF4106–169 region, but total disruption of the complex is not achieved until both mutations are used.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":107,"end":137,"reference_id":"12875835","reference_source":"pmid","reference_html":"Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide. <i> Reidt U, Wahl MC, Fasshauer D, Horowitz DS, Lührmann R, Ficner R. </i> J Mol Biol, 2003","date":"2024-02-19T14:37:59.481Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01751r008","statement":[{"text":"We recorded circular dichroism (CD) spectra of the U4/U6-60K peptide (10−5 M) at 25 °C and 4 °C in physiological salt solution. Not surprisingly and in contrast to CypH, the peptide largely adopts a random coil conformation (data not shown).","type":"Results"}]},{"start":107,"end":137,"reference_id":"12875835","reference_source":"pmid","reference_html":"Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide. <i> Reidt U, Wahl MC, Fasshauer D, Horowitz DS, Lührmann R, Ficner R. </i> J Mol Biol, 2003","date":"2024-02-19T14:42:14.478Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"1MZW"}],"region_id":"DP01751r009","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O43447"}],"statement":[{"text":"The U4/U6-60K protein fragment folds into two α-helices (α1: Val107-Ala113; α2: Pro125-Ile135; numbering is according to the full-length U4/U6-60K protein) connected by an extended loop (Leu114-Gly124; Figure 1(C)).","type":"Results"},{"text":"Therefore, the entropic cost of folding upon interaction with CypH is made up by the binding energy, suggesting that the complex observed herein is strong and specific.","type":"Results"}]},{"start":107,"end":137,"reference_id":"12875835","reference_source":"pmid","reference_html":"Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide. <i> Reidt U, Wahl MC, Fasshauer D, Horowitz DS, Lührmann R, Ficner R. </i> J Mol Biol, 2003","date":"2024-02-19T14:44:52.898Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"1MZW"}],"region_id":"DP01751r010","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O43447"}],"statement":[{"text":"The U4/U6-60K protein fragment folds into two α-helices (α1: Val107-Ala113; α2: Pro125-Ile135; numbering is according to the full-length U4/U6-60K protein) connected by an extended loop (Leu114-Gly124; Figure 1(C)).","type":"Results"},{"text":"Therefore, the entropic cost of folding upon interaction with CypH is made up by the binding energy, suggesting that the complex observed herein is strong and specific.","type":"Results"}],"states_connection":[{"source":"DP01751r008","target":"DP01751r009"}]},{"start":107,"end":137,"reference_id":"12875835","reference_source":"pmid","reference_html":"Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide. <i> Reidt U, Wahl MC, Fasshauer D, Horowitz DS, Lührmann R, Ficner R. </i> J Mol Biol, 2003","date":"2024-02-19T14:44:30.874Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"1MZW"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"O43447","operator":null,"partner_start":1,"partner_end":177}],"region_id":"DP01751r011","statement":[{"text":"Binding of the U4/U6-60K peptide to a pre-shaped site on CypH","type":"Results"},{"text":"Therefore, the entropic cost of folding upon interaction with CypH is made up by the binding energy, suggesting that the complex observed herein is strong and specific.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_O43172","date":"2018-08-08T14:18:49.000Z","acc":"O43172","name":"U4/U6 small nuclear ribonucleoprotein Prp4","length":522,"organism":"Homo sapiens","dataset":["RNA-binding proteins"],"UniParc":"UPI0000169629","genes":[{"name":{"value":"PRPF4"},"synonyms":[{"value":"PRP4"}]}],"alphafold_very_low_content":0.08237547892720307,"disorder_content":0.32375478927203066,"disprot_consensus":{"full":[{"start":1,"end":106,"type":"D"},{"start":107,"end":137,"type":"T"},{"start":138,"end":169,"type":"D"}],"Structural state":[{"start":1,"end":169,"type":"D"}],"Molecular function":[{"start":1,"end":98,"type":"F"},{"start":106,"end":169,"type":"F"}],"Structural transition":[{"start":107,"end":137,"type":"T"}]}},{"features":{"pfam":[{"id":"PF02218","name":"Repeat in HS1/Cortactin","start":83,"end":117},{"id":"PF02218","name":"Repeat in HS1/Cortactin","start":120,"end":155},{"id":"PF02218","name":"Repeat in HS1/Cortactin","start":157,"end":192},{"id":"PF02218","name":"Repeat in HS1/Cortactin","start":194,"end":228},{"id":"PF02218","name":"Repeat in HS1/Cortactin","start":231,"end":266},{"id":"PF02218","name":"Repeat in HS1/Cortactin","start":268,"end":303},{"id":"PF02218","name":"Repeat in HS1/Cortactin","start":305,"end":329},{"id":"PF14604","name":"Variant SH3 domain","start":495,"end":543}],"gene3D":[{"start":475,"end":546,"id":"2.30.30.40","name":"SH3 Domains"}]},"uniref50":"UniRef50_Q60598","sequence":"MWKASAGHAVSITQDDGGADDWETDPDFVNDVSEKEQRWGAKTVQGSGHQEHINIHKLRENVFQEHQTLKEKELETGPKASHGYGGKFGVEQDRMDRSAVGHEYQSKLSKHCSQVDSVRGFGGKFGVQMDRVDQSAVGFEYQGKTEKHASQKDYSSGFGGKYGVQADRVDKSAVGFDYQGKTEKHESQKDYSKGFGGKYGIDKDKVDKSAVGFEYQGKTEKHESQKDYVKGFGGKFGVQTDRQDKCALGWDHQEKLQLHESQKDYKTGFGGKFGVQSERQDSSAVGFDYKERLAKHESQQDYAKGFGGKYGVQKDRMDKNASTFEEVVQVPSAYQKTVPIEAVTSKTSNIRANFENLAKEREQEDRRKAEAERAQRMAKERQEQEEARRKLEEQARAKKQTPPASPSPQPIEDRPPSSPIYEDAAPFKAEPSYRGSEPEPEYSIEAAGIPEAGSQQGLTYTSEPVYETTEAPGHYQAEDDTYDGYESDLGITAIALYDYQAAGDDEISFDPDDIITNIEMIDDGWWRGVCKGRYGLFPANYVELRQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q60598","disprot_id":"DP01752","ncbi_taxon_id":10090,"regions_counter":4,"creator":"emaiani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":324,"region_id":"DP01752r001","released":"2023_12","ec_id":"ECO:0006204","reference_html":"The repeat region of cortactin is intrinsically disordered in solution. <i> Li X, Tao Y, Murphy JW, Scherer AN, Lam TT, Marshall AG, Koleske AJ, Boggon TJ. </i> Sci Rep, 2017","statement":[{"text":"The repeat region of cortactin is intrinsically disordered in solution","type":"Title"},{"text":"Using circular dichroism (CD) we find that in solution the cortactin repeats resemble a coil-like intrinsically disordered protein. Small-angle X-ray scattering (SAXS) also indicates that the cortactin repeats are intrinsically unfolded, and the experimentally observed radius of gyration (R g) is coincidental to that calculated by the program Flexible-Meccano for an unfolded peptide of this length.","type":"Abstract"},{"text":"Circular dichroism suggests a coil-like intrinsically disordered structure for the cortactin repeats","type":"Results"},{"text":" In contrast, CD spectra of the cortactinCR had a minimum negative signal at 202 nm indicating the presence of mostly random coil, consistent with natively unfolded protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":83,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2023-12-05T17:39:02.941Z","reference_source":"pmid","term_name":"disorder","reference_id":"29196701","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:12:04.161Z"}},{"start":83,"end":324,"reference_id":"29196701","reference_source":"pmid","reference_html":"The repeat region of cortactin is intrinsically disordered in solution. <i> Li X, Tao Y, Murphy JW, Scherer AN, Lam TT, Marshall AG, Koleske AJ, Boggon TJ. </i> Sci Rep, 2017","date":"2023-12-05T17:40:43.457Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01752r003","statement":[{"text":"The repeat region of cortactin is intrinsically disordered in solution","type":"Title"},{"text":"Using circular dichroism (CD) we find that in solution the cortactin repeats resemble a coil-like intrinsically disordered protein. Small-angle X-ray scattering (SAXS) also indicates that the cortactin repeats are intrinsically unfolded, and the experimentally observed radius of gyration (R g) is coincidental to that calculated by the program Flexible-Meccano for an unfolded peptide of this length.","type":"Abstract"},{"text":"Small-angle X-ray scattering finds the cortactin repeats to be intrinsically disordered","type":"Results"},{"text":"We found no aggregation, and molecular weight estimation based on Porod volume corresponded well with those expected for a monomeric protein (Table 1), however Guinier approximations indicated a radius of gyration (R g) for this 324 amino acid protein of ~47.5 Å (Fig. 3B, Table 1), significantly larger than would be expected for a globular protein (~20 Å)29. Analysis of the scattering properties of cortactinCRH shows that it displays other features expected for intrinsically disordered proteins: its Kratky plot displays a monotonic increase characteristic of intrinsic disorder24 (Fig. 3C), and its Porod-Debye plot does not plateau as would be expected for a globular protein30 (Fig. 3D). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:12:05.478Z"}},{"start":83,"end":324,"reference_id":"29196701","reference_source":"pmid","reference_html":"The repeat region of cortactin is intrinsically disordered in solution. <i> Li X, Tao Y, Murphy JW, Scherer AN, Lam TT, Marshall AG, Koleske AJ, Boggon TJ. </i> Sci Rep, 2017","date":"2023-12-05T17:41:46.112Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01752r004","statement":[{"text":"The repeat region of cortactin is intrinsically disordered in solution","type":"Title"},{"text":"Using circular dichroism (CD) we find that in solution the cortactin repeats resemble a coil-like intrinsically disordered protein. Small-angle X-ray scattering (SAXS) also indicates that the cortactin repeats are intrinsically unfolded, and the experimentally observed radius of gyration (R g) is coincidental to that calculated by the program Flexible-Meccano for an unfolded peptide of this length.","type":"Abstract"},{"text":"Hydrogen-deuterium exchange mass spectrometry shows rapid exchange for most regions of the cortactin repeats","type":"Results"},{"text":"We find most regions of cortactinCR rapidly reached HDX saturation by the first time-point (Fig. 5), indicating that cortactinCR contains minimal hydrophobic core (unprotected) and is largely intrinsically disordered. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:12:06.366Z"}}],"released":"2018_11","uniref100":"UniRef100_Q60598","date":"2018-08-08T14:43:58.000Z","acc":"Q60598","name":"Src substrate cortactin","length":546,"organism":"Mus musculus","dataset":["Condensates-related proteins"],"UniParc":"UPI0000027F8C","genes":[{"name":{"value":"Cttn"},"synonyms":[{"value":"Ems1"}]}],"alphafold_very_low_content":0.21245421245421245,"disorder_content":0.4432234432234432,"disprot_consensus":{"full":[{"start":83,"end":324,"type":"D"}],"Structural state":[{"start":83,"end":324,"type":"D"}]}},{"features":{"pfam":[{"id":"PF15325","name":"Modulator of retrovirus infection","start":59,"end":157}]},"uniref50":"UniRef50_Q8BHZ5","sequence":"METLKSKTKTRVLPSWMTAPVDERKVVSVKTATRKQTAAWAQRVGAATRAPATETVYCMNEAEMVDVALGILIEGRKQEKPWEQRSLEATDKLQLSPPCSSSPGSSSEEEDSRISSLAPGLSPPRGPEASDSPCSRSPEEEKEEEDALKYVREIFFS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q8BHZ5","disprot_id":"DP01754","ncbi_taxon_id":10090,"regions_counter":13,"creator":"emaiani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":157,"region_id":"DP01754r001","released":"2024_06","ec_id":"ECO:0006236","reference_html":"MRI Is a DNA Damage Response Adaptor during Classical Non-homologous End Joining. <i> Hung PJ, Johnson B, Chen BR, Byrum AK, Bredemeyer AL, Yewdell WT, Johnson TE, Lee BJ, Deivasigamani S, Hindi I, Amatya P, Gross ML, Paull TT, Pisapia DJ, Chaudhuri J, Petrini JJH, Mosammaparast N, Amarasinghe GK, Zha S, Tyler JK, Sleckman BP. </i> Mol Cell, 2018","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-19T14:50:27.445Z","reference_source":"pmid","term_name":"disorder","reference_id":"30017584","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Many of these peptides displayed near maximal deuterium uptake at the earliest time point (10 seconds) suggesting that MRI is intrinsically disordered in solution (Fig. S7C).","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":157,"region_id":"DP01754r002","released":"2024_06","ec_id":"ECO:0006204","reference_html":"MRI Is a DNA Damage Response Adaptor during Classical Non-homologous End Joining. <i> Hung PJ, Johnson B, Chen BR, Byrum AK, Bredemeyer AL, Yewdell WT, Johnson TE, Lee BJ, Deivasigamani S, Hindi I, Amatya P, Gross ML, Paull TT, Pisapia DJ, Chaudhuri J, Petrini JJH, Mosammaparast N, Amarasinghe GK, Zha S, Tyler JK, Sleckman BP. </i> Mol Cell, 2018","statement":[{"text":"Indeed, while circular dichroism (CD) spectroscopy also demonstrates that MRI is an intrinsically disordered protein, the addition of trifluoroethanol (TFE), a helix-inducing crowding agent, resulted in CD spectra suggestive that MRI has the potential to form helical structures (Fig. S7D) (Lopes et al., 2014).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-19T14:50:43.132Z","reference_source":"pmid","term_name":"disorder","reference_id":"30017584","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":157,"reference_id":"30017584","reference_source":"pmid","reference_html":"MRI Is a DNA Damage Response Adaptor during Classical Non-homologous End Joining. <i> Hung PJ, Johnson B, Chen BR, Byrum AK, Bredemeyer AL, Yewdell WT, Johnson TE, Lee BJ, Deivasigamani S, Hindi I, Amatya P, Gross ML, Paull TT, Pisapia DJ, Chaudhuri J, Petrini JJH, Mosammaparast N, Amarasinghe GK, Zha S, Tyler JK, Sleckman BP. </i> Mol Cell, 2018","date":"2024-02-19T14:56:06.026Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051260","term_name":"protein homooligomerization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007066","ec_ontology":"ECO","ec_name":"static light scattering assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","region_id":"DP01754r003","statement":[{"text":"Finally, size-exclusion chromatography coupled with multi-angle light scattering (SEC-MALS) revealed that, in solution, MRI can exist as a monomer, dimer, or multimer (Fig. S7E).","type":"Results"}],"term_comment":"","term_def":"\"The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":157,"reference_id":"30017584","reference_source":"pmid","reference_html":"MRI Is a DNA Damage Response Adaptor during Classical Non-homologous End Joining. <i> Hung PJ, Johnson B, Chen BR, Byrum AK, Bredemeyer AL, Yewdell WT, Johnson TE, Lee BJ, Deivasigamani S, Hindi I, Amatya P, Gross ML, Paull TT, Pisapia DJ, Chaudhuri J, Petrini JJH, Mosammaparast N, Amarasinghe GK, Zha S, Tyler JK, Sleckman BP. </i> Mol Cell, 2018","date":"2024-02-19T15:21:12.773Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P97313","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q62388","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P23475","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q61216","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9R207","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P70388","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q3KNJ2","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q8K0Y7","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP01754r004","statement":[{"text":"Immunoprecipitation with the 13E10.E12.C10 anti-MRI monoclonal antibody confirmed that endogenous MRI associates with DNA-PKcs, ATM, Ku70, Mre11, Nbs1, Rad50, XLF and PAXX (Fig. 4D). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":157,"reference_id":"30017584","reference_source":"pmid","reference_html":"MRI Is a DNA Damage Response Adaptor during Classical Non-homologous End Joining. <i> Hung PJ, Johnson B, Chen BR, Byrum AK, Bredemeyer AL, Yewdell WT, Johnson TE, Lee BJ, Deivasigamani S, Hindi I, Amatya P, Gross ML, Paull TT, Pisapia DJ, Chaudhuri J, Petrini JJH, Mosammaparast N, Amarasinghe GK, Zha S, Tyler JK, Sleckman BP. </i> Mol Cell, 2018","date":"2024-02-19T15:27:47.425Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990391","term_name":"DNA repair complex","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q3KNJ2","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q8K0Y7","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P70388","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9R207","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q61216","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P23475","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q62388","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P97313","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP01754r005","statement":[{"text":"Immunoprecipitation with the 13E10.E12.C10 anti-MRI monoclonal antibody confirmed that endogenous MRI associates with DNA-PKcs, ATM, Ku70, Mre11, Nbs1, Rad50, XLF and PAXX (Fig. 4D). ","type":"Results"}],"term_comment":"","term_def":"\"A protein complex involved in DNA repair processes including direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.\" [GOC:bhm, PMID:17217467, PMID:20551348, PMID:22749910, PMID:24192350]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":17,"reference_id":"30017584","reference_source":"pmid","reference_html":"MRI Is a DNA Damage Response Adaptor during Classical Non-homologous End Joining. <i> Hung PJ, Johnson B, Chen BR, Byrum AK, Bredemeyer AL, Yewdell WT, Johnson TE, Lee BJ, Deivasigamani S, Hindi I, Amatya P, Gross ML, Paull TT, Pisapia DJ, Chaudhuri J, Petrini JJH, Mosammaparast N, Amarasinghe GK, Zha S, Tyler JK, Sleckman BP. </i> Mol Cell, 2018","date":"2024-02-19T15:40:17.993Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0520","term_name":"HA","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The murine MRI coding sequence was amplified by PCR from the cDNA clone BC000168 and ligated into a retroviral vector pOZ-FH-N downstream of a FLAG-HA tag and between a XhoI site and a NotI site."}]},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1Met17del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Mass spectrometry was used to identify proteins in WT abl pre-B cells that bind to FLAG-HA-tagged versions of full-length MRI, MRI with a deletion of the 17 N-terminal amino acids comprising the KBM (MRIΔN), and MRI with a deletion of the 15 C-terminal amino acids comprising the XLM (MRIΔC) (Fig. 4A, ​,4B4B and S7A)."}]}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P97313","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P23475","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P27641","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q3KNJ2","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q8K0Y7","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q924T3","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP01754r006","statement":[{"text":"FLAG-HA-tagged MRI, MRIΔC, MRIΔN or MRIΔNΔC were expressed in WT abl pre-B cells and immunoprecipitated with anti-HA. Members of the DNA-PK complex – Ku70, Ku80 and DNA-PKcs – as well as XLF, PAXX, and XRCC4 all interact with MRI and MRIΔC, but do not interact with MRIΔN or MRIΔNΔC, indicating that the association of these proteins with MRI depends on the N-terminal KBM (Fig. 4E).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":143,"end":157,"reference_id":"30017584","reference_source":"pmid","reference_html":"MRI Is a DNA Damage Response Adaptor during Classical Non-homologous End Joining. <i> Hung PJ, Johnson B, Chen BR, Byrum AK, Bredemeyer AL, Yewdell WT, Johnson TE, Lee BJ, Deivasigamani S, Hindi I, Amatya P, Gross ML, Paull TT, Pisapia DJ, Chaudhuri J, Petrini JJH, Mosammaparast N, Amarasinghe GK, Zha S, Tyler JK, Sleckman BP. </i> Mol Cell, 2018","date":"2024-02-19T15:44:47.948Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0520","term_name":"HA","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The murine MRI coding sequence was amplified by PCR from the cDNA clone BC000168 and ligated into a retroviral vector pOZ-FH-N downstream of a FLAG-HA tag and between a XhoI site and a NotI site."}]},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Glu143Ser157del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Mass spectrometry was used to identify proteins in WT abl pre-B cells that bind to FLAG-HA-tagged versions of full-length MRI, MRI with a deletion of the 17 N-terminal amino acids comprising the KBM (MRIΔN), and MRI with a deletion of the 15 C-terminal amino acids comprising the XLM (MRIΔC) (Fig. 4A, ​,4B4B and S7A)."}]}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q61216","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9R207","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P70388","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP01754r007","statement":[{"text":"Conversely, KAP-1, ATM, and components of the MRN complex - Mre11, Nbs1 and Rad50 - all interact with MRI and MRIΔN, but not MRIΔC or MRIΔNΔC, indicating that the binding of these proteins to MRI depends on the C-terminal XLM (Fig. 4E).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":157,"reference_id":"30017584","reference_source":"pmid","reference_html":"MRI Is a DNA Damage Response Adaptor during Classical Non-homologous End Joining. <i> Hung PJ, Johnson B, Chen BR, Byrum AK, Bredemeyer AL, Yewdell WT, Johnson TE, Lee BJ, Deivasigamani S, Hindi I, Amatya P, Gross ML, Paull TT, Pisapia DJ, Chaudhuri J, Petrini JJH, Mosammaparast N, Amarasinghe GK, Zha S, Tyler JK, Sleckman BP. </i> Mol Cell, 2018","date":"2024-02-19T15:49:34.806Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P23475","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q61216","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q62388","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P97313","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01754r008","statement":[{"text":"Third, size-exclusion chromatography revealed that, in abl pre-B cells, MRI exists in fractions that range in size from 100 kDa to over 1 MDa (Fig. 5D). The 30 kDa MRI protein was most abundant in 200 kDa fractions that contained Ku and in fractions greater than 1 MDa that contained Ku, Mre11, ATM, and DNA-PKcs (Fig. 5D). We conclude that MRI is an adaptor that forms large multimeric complexes containing DDR proteins bound at the N-terminus, C-terminus, or both.","type":"Results"}],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":157,"reference_id":"30017584","reference_source":"pmid","reference_html":"MRI Is a DNA Damage Response Adaptor during Classical Non-homologous End Joining. <i> Hung PJ, Johnson B, Chen BR, Byrum AK, Bredemeyer AL, Yewdell WT, Johnson TE, Lee BJ, Deivasigamani S, Hindi I, Amatya P, Gross ML, Paull TT, Pisapia DJ, Chaudhuri J, Petrini JJH, Mosammaparast N, Amarasinghe GK, Zha S, Tyler JK, Sleckman BP. </i> Mol Cell, 2018","date":"2024-02-19T15:55:21.166Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:2001034","term_name":"positive regulation of double-strand break repair via nonhomologous end joining","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007117","ec_ontology":"ECO","ec_name":"mutant physiological response evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IMP","region_id":"DP01754r009","statement":[{"text":"Several lines of evidence demonstrate that MRI promotes cNHEJ. MRI is required for cNHEJ-dependent repair of RAG DSBs in XLF-deficient G1-phase abl pre-B cells and for cNHEJ-mediated repair of I-PpoI DSBs in G1- and G2-phase XLF-deficient cells (Fig. 3, S4, and S5).","type":"Discussion"}],"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of double-strand break repair via nonhomologous end joining.\" [GOC:obol]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":157,"reference_id":"30017584","reference_source":"pmid","reference_html":"MRI Is a DNA Damage Response Adaptor during Classical Non-homologous End Joining. <i> Hung PJ, Johnson B, Chen BR, Byrum AK, Bredemeyer AL, Yewdell WT, Johnson TE, Lee BJ, Deivasigamani S, Hindi I, Amatya P, Gross ML, Paull TT, Pisapia DJ, Chaudhuri J, Petrini JJH, Mosammaparast N, Amarasinghe GK, Zha S, Tyler JK, Sleckman BP. </i> Mol Cell, 2018","date":"2024-02-19T16:08:15.500Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990166","term_name":"protein localization to site of double-strand break","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"MRI−/− MEFs were stably transduced with a lentiviral vector pLV (Addgene) containing a MRI-GFP fusion protein, then transiently transfected with 1.5 μg Ku80-RFP using Lipofectamine 2000 (Thermo Fisher) and imaged after 48 hours."}]}],"ec_go":"IDA","region_id":"DP01754r010","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"MRI−/− MEFs were stably transduced with a lentiviral vector pLV (Addgene) containing a MRI-GFP fusion protein, then transiently transfected with 1.5 μg Ku80-RFP using Lipofectamine 2000 (Thermo Fisher) and imaged after 48 hours."}]}],"statement":[{"text":"Robust MRI-GFP localization was also observed upon laser-induced DNA damage of serum starved G1-phase MRI−/− MEFs (Fig. S2D). We conclude that, like the core cNHEJ factor Ku, MRI localizes to DNA damage sites in MEFs, and MRI deficiency in MEFs leads to IR sensitivity, a common hallmark of cNHEJ deficiency.","type":"Results"}],"term_comment":"","term_def":"\"Any process in which a protein is transported to, or maintained at, a region of a chromosome at which a DNA double-strand break has occurred.\" [GOC:mah, PMID:23080121]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":157,"reference_id":"30017584","reference_source":"pmid","reference_html":"MRI Is a DNA Damage Response Adaptor during Classical Non-homologous End Joining. <i> Hung PJ, Johnson B, Chen BR, Byrum AK, Bredemeyer AL, Yewdell WT, Johnson TE, Lee BJ, Deivasigamani S, Hindi I, Amatya P, Gross ML, Paull TT, Pisapia DJ, Chaudhuri J, Petrini JJH, Mosammaparast N, Amarasinghe GK, Zha S, Tyler JK, Sleckman BP. </i> Mol Cell, 2018","date":"2024-02-19T16:08:43.890Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006303","term_name":"double-strand break repair via nonhomologous end joining","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"MRI−/− MEFs were stably transduced with a lentiviral vector pLV (Addgene) containing a MRI-GFP fusion protein, then transiently transfected with 1.5 μg Ku80-RFP using Lipofectamine 2000 (Thermo Fisher) and imaged after 48 hours."}]}],"ec_go":"IDA","region_id":"DP01754r011","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"MRI−/− MEFs were stably transduced with a lentiviral vector pLV (Addgene) containing a MRI-GFP fusion protein, then transiently transfected with 1.5 μg Ku80-RFP using Lipofectamine 2000 (Thermo Fisher) and imaged after 48 hours."}]}],"statement":[{"text":"Robust MRI-GFP localization was also observed upon laser-induced DNA damage of serum starved G1-phase MRI−/− MEFs (Fig. S2D). We conclude that, like the core cNHEJ factor Ku, MRI localizes to DNA damage sites in MEFs, and MRI deficiency in MEFs leads to IR sensitivity, a common hallmark of cNHEJ deficiency.","type":"Results"}],"term_comment":"","term_def":"\"The repair of a double-strand break in DNA in which the two broken ends are rejoined with little or no sequence complementarity. Information at the DNA ends may be lost due to the modification of broken DNA ends. This term covers instances of separate pathways, called classical (or canonical) and alternative nonhomologous end joining (C-NHEJ and A-NHEJ). These in turn may further branch into sub-pathways, but evidence is still unclear.\" [GOC:rph, PMID:10827453, PMID:24837021]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":157,"reference_id":"30017584","reference_source":"pmid","reference_html":"MRI Is a DNA Damage Response Adaptor during Classical Non-homologous End Joining. <i> Hung PJ, Johnson B, Chen BR, Byrum AK, Bredemeyer AL, Yewdell WT, Johnson TE, Lee BJ, Deivasigamani S, Hindi I, Amatya P, Gross ML, Paull TT, Pisapia DJ, Chaudhuri J, Petrini JJH, Mosammaparast N, Amarasinghe GK, Zha S, Tyler JK, Sleckman BP. </i> Mol Cell, 2018","date":"2024-02-19T16:10:10.974Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003684","term_name":"damaged DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"MRI−/− MEFs were stably transduced with a lentiviral vector pLV (Addgene) containing a MRI-GFP fusion protein, then transiently transfected with 1.5 μg Ku80-RFP using Lipofectamine 2000 (Thermo Fisher) and imaged after 48 hours."}]}],"ec_go":"IDA","region_id":"DP01754r012","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"MRI−/− MEFs were stably transduced with a lentiviral vector pLV (Addgene) containing a MRI-GFP fusion protein, then transiently transfected with 1.5 μg Ku80-RFP using Lipofectamine 2000 (Thermo Fisher) and imaged after 48 hours."}]}],"statement":[{"text":"MRI-GFP remained associated with DNA damage sites for at least 45 minutes (Fig. S2C).","type":"Results"},{"text":"Robust MRI-GFP localization was also observed upon laser-induced DNA damage of serum starved G1-phase MRI−/− MEFs (Fig. S2D). We conclude that, like the core cNHEJ factor Ku, MRI localizes to DNA damage sites in MEFs, and MRI deficiency in MEFs leads to IR sensitivity, a common hallmark of cNHEJ deficiency.","type":"Results"}],"term_comment":"","term_def":"\"Binding to damaged DNA.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":157,"reference_id":"30017584","reference_source":"pmid","reference_html":"MRI Is a DNA Damage Response Adaptor during Classical Non-homologous End Joining. <i> Hung PJ, Johnson B, Chen BR, Byrum AK, Bredemeyer AL, Yewdell WT, Johnson TE, Lee BJ, Deivasigamani S, Hindi I, Amatya P, Gross ML, Paull TT, Pisapia DJ, Chaudhuri J, Petrini JJH, Mosammaparast N, Amarasinghe GK, Zha S, Tyler JK, Sleckman BP. </i> Mol Cell, 2018","date":"2024-02-19T16:14:57.741Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006974","term_name":"cellular response to DNA damage stimulus","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"MRI−/− MEFs were stably transduced with a lentiviral vector pLV (Addgene) containing a MRI-GFP fusion protein, then transiently transfected with 1.5 μg Ku80-RFP using Lipofectamine 2000 (Thermo Fisher) and imaged after 48 hours."}]}],"ec_go":"IDA","region_id":"DP01754r013","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"MRI−/− MEFs were stably transduced with a lentiviral vector pLV (Addgene) containing a MRI-GFP fusion protein, then transiently transfected with 1.5 μg Ku80-RFP using Lipofectamine 2000 (Thermo Fisher) and imaged after 48 hours."}]}],"statement":[{"text":"MRI-GFP remained associated with DNA damage sites for at least 45 minutes (Fig. S2C).","type":"Results"},{"text":"Robust MRI-GFP localization was also observed upon laser-induced DNA damage of serum starved G1-phase MRI−/− MEFs (Fig. S2D). We conclude that, like the core cNHEJ factor Ku, MRI localizes to DNA damage sites in MEFs, and MRI deficiency in MEFs leads to IR sensitivity, a common hallmark of cNHEJ deficiency.","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_Q8BHZ5","date":"2018-08-08T15:12:20.000Z","acc":"Q8BHZ5","name":"Cell cycle regulator of non-homologous end joining","length":157,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000EB89D","genes":[{"name":{"value":"Cyren","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"31795137","url":"http://www.ncbi.nlm.nih.gov/pubmed/31795137","alternativeUrl":"https://europepmc.org/abstract/MED/31795137"}},{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:1925662","url":"http://www.informatics.jax.org/marker/MGI:1925662"}}]},"synonyms":[{"value":"Mri","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"30017584","url":"http://www.ncbi.nlm.nih.gov/pubmed/30017584","alternativeUrl":"https://europepmc.org/abstract/MED/30017584"}}]}]}],"alphafold_very_low_content":0.22929936305732485,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":157,"type":"D"}],"Structural state":[{"start":1,"end":157,"type":"D"}],"Biological process":[{"start":1,"end":157,"type":"F"}],"Molecular function":[{"start":1,"end":157,"type":"F"}],"Cellular component":[{"start":1,"end":157,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00096","name":"Zinc finger, C2H2 type","start":360,"end":382},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":390,"end":412},{"id":"PF13912","name":"C2H2-type zinc finger","start":483,"end":507},{"id":"PF13912","name":"C2H2-type zinc finger","start":1455,"end":1473},{"id":"PF21549","name":"PR domain zinc finger protein 2, PR domain","start":34,"end":144}],"gene3D":[{"start":358,"end":432,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":1131,"end":1218,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":2,"end":160,"id":"2.170.270.10","name":"SET domain"},{"start":480,"end":508,"id":"3.30.160.60","name":"Classic Zinc Finger"}]},"uniref50":"UniRef50_Q13029","sequence":"MNQNTTEPVAATETLAEVPEHVLRGLPEEVRLFPSAVDKTRIGVWATKPILKGKKFGPFVGDKKKRSQVKNNVYMWEVYYPNLGWMCIDATDPEKGNWLRYVNWACSGEEQNLFPLEINRAIYYKTLKPIAPGEELLVWYNGEDNPEIAAAIEEERASARSKRSSPKSRKGKKKSQENKNKGNKIQDIQLKTSEPDFTSANMRDSAEGPKEDEEKPSASALEQPATLQEVASQEVPPELATPAPAWEPQPEPDERLEAAACEVNDLGEEEEEEEEEDEEEEEDDDDDELEDEGEEEASMPNENSVKEPEIRCDEKPEDLLEEPKTTSEETLEDCSEVTPAMQIPRTKEEANGDVFETFMFPCQHCERKFTTKQGLERHMHIHISTVNHAFKCKYCGKAFGTQINRRRHERRHEAGLKRKPSQTLQPSEDLADGKASGENVASKDDSSPPSLGPDCLIMNSEKASQDTINSSVVEENGEVKELHPCKYCKKVFGTHTNMRRHQRRVHERHLIPKGVRRKGGLEEPQPPAEQAQATQNVYVPSTEPEEEGEADDVYIMDISSNISENLNYYIDGKIQTNNNTSNCDVIEMESASADLYGINCLLTPVTVEITQNIKTTQVPVTEDLPKEPLGSTNSEAKKRRTASPPALPKIKAETDSDPMVPSCSLSLPLSISTTEAVSFHKEKSVYLSSKLKQLLQTQDKLTPAGISATEIAKLGPVCVSAPASMLPVTSSRFKRRTSSPPSSPQHSPALRDFGKPSDGKAAWTDAGLTSKKSKLESHSDSPAWSLSGRDERETVSPPCFDEYKMSKEWTASSAFSSVCNQQPLDLSSGVKQKAEGTGKTPVQWESVLDLSVHKKHCSDSEGKEFKESHSVQPTCSAVKKRKPTTCMLQKVLLNEYNGIDLPVENPADGTRSPSPCKSLEAQPDPDLGPGSGFPAPTVESTPDVCPSSPALQTPSLSSGQLPPLLIPTDPSSPPPCPPVLTVATPPPPLLPTVPLPAPSSSASPHPCPSPLSNATAQSPLPILSPTVSPSPSPIPPVEPLMSAASPGPPTLSSSSSSSSSSSSFSSSSSSSSPSPPPLSAISSVVSSGDNLEASLPMISFKQEELENEGLKPREEPQSAAEQDVVVQETFNKNFVCNVCESPFLSIKDLTKHLSIHAEEWPFKCEFCVQLFKDKTDLSEHRFLLHGVGNIFVCSVCKKEFAFLCNLQQHQRDLHPDKVCTHHEFESGTLRPQNFTDPSKAHVEHMQSLPEDPLETSKEEEELNDSSEELYTTIKIMASGIKTKDPDVRLGLNQHYPSFKPPPFQYHHRNPMGIGVTATNFTTHNIPQTFTTAIRCTKCGKGVDNMPELHKHILACASASDKKRYTPKKNPVPLKQTVQPKNGVVVLDNSGKNAFRRMGQPKRLNFSVELSKMSSNKLKLNALKKKNQLVQKAILQKNKSAKQKADLKNACESSSHICPYCNREFTYIGSLNKHAAFSCPKKPLSPPKKKVSHSSKKGGHSSPASSDKNSNSNHRRRTADAEIKMQSMQTPLGKTRARSSGPTQVPLPSSSFRSKQNVKFAASVKSKKPSSSSLRNSSPIRMAKITHVEGKKPKAVAKNHSAQLSSKTSRSLHVRVQKSKAVLQSKSTLASKKRTDRFNIKSRERSGGPVTRSLQLAAAADLSENKREDGSAKQELKDFSYSLRLASRCSPPAAPYITRQYRKVKAPAAAQFQGPFFKE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q13029","disprot_id":"DP01757","ncbi_taxon_id":9606,"regions_counter":11,"creator":"lchemes","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":341,"region_id":"DP01757r001","released":"2024_12","ec_id":"ECO:0006165","reference_html":"Structural and functional characterization of the acidic region from the RIZ tumor suppressor. <i> Sun Y, Stine JM, Atwater DZ, Sharmin A, Ross JB, Briknarová K. </i> Biochemistry, 2015","statement":[{"text":"Signals in NMR spectra of AR displayed narrow line widths and limited dispersion typical of unfolded proteins (Figure 3), and the absence of residues with positive heteronuclear 1H–15N NOE indicated that AR is highly flexible (Figure 4).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":197,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"25640033","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2024-11-26T14:40:44.566Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":341,"term_name":"disorder","start":197,"ec_name":"gel-filtration evidence used in manual assertion","statement":[{"text":"AR eluted from a Superdex 75 size-exclusion column in a volume similar to that of the 60 kDa bovine albumin standard (data not shown), suggesting that it either formed oligomers or adopted an extended conformation in solution. ","type":"Results"}],"curator_id":"vnugnes","released":"2024_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"25640033","version":4,"reference_html":"Structural and functional characterization of the acidic region from the RIZ tumor suppressor. <i> Sun Y, Stine JM, Atwater DZ, Sharmin A, Ross JB, Briknarová K. </i> Biochemistry, 2015","date":"2024-11-26T14:49:03.628Z","term_id":"IDPO:0000002","ec_id":"ECO:0001184","region_id":"DP01757r002","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Structural state","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":269,"region_id":"DP01757r003","released":"2024_12","ec_id":"ECO:0005642","reference_html":"Structural and functional characterization of the acidic region from the RIZ tumor suppressor. <i> Sun Y, Stine JM, Atwater DZ, Sharmin A, Ross JB, Briknarová K. </i> Biochemistry, 2015","statement":[{"text":"The 2D 1H–15N HSQC spectra of AR-N and AR-C are shown in Figure 9. For virtually every signal in these spectra, there is a counterpart at the same position in the 1H–15N HSQC spectrum of AR (data not shown).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":197,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"25640033","version":3,"ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","date":"2024-11-26T14:41:42.432Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":267,"term_name":"protein binding","start":255,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Residues 306–322 (KEPEIRCDEKPEDLLEE) were the most affected by RbAB binding (Figure 7). This sequence contains the IRCDE motif that was proposed to mediate the interaction with Rb.21 Surprisingly, residues 255–267 (RLEAAACEVNDLG) were also affected, but the decrease in their signal intensities was delayed relative to that of residues 306–322 (Figure 7). This suggested that the pocket domain binds preferentially to residues 306–322 and that it interacts with residues 255–267 with a lower affinity.","type":"Results"}],"curator_id":"vnugnes","released":"2024_12","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"25640033","version":4,"reference_html":"Structural and functional characterization of the acidic region from the RIZ tumor suppressor. <i> Sun Y, Stine JM, Atwater DZ, Sharmin A, Ross JB, Briknarová K. </i> Biochemistry, 2015","date":"2024-11-26T14:47:01.025Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP01757r004","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P06400","operator":"and","partner_start":372,"partner_end":787}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":341,"region_id":"DP01757r005","released":"2024_12","ec_id":"ECO:0005642","reference_html":"Structural and functional characterization of the acidic region from the RIZ tumor suppressor. <i> Sun Y, Stine JM, Atwater DZ, Sharmin A, Ross JB, Briknarová K. </i> Biochemistry, 2015","statement":[{"text":"The 2D 1H–15N HSQC spectra of AR-N and AR-C are shown in Figure 9. For virtually every signal in these spectra, there is a counterpart at the same position in the 1H–15N HSQC spectrum of AR (data not shown).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":297,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"25640033","version":3,"ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","date":"2024-11-26T14:41:52.394Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":322,"term_name":"protein binding","start":306,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"vnugnes","released":"2024_12","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"25640033","version":4,"reference_html":"Structural and functional characterization of the acidic region from the RIZ tumor suppressor. <i> Sun Y, Stine JM, Atwater DZ, Sharmin A, Ross JB, Briknarová K. </i> Biochemistry, 2015","date":"2024-11-26T14:46:15.306Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP01757r006","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P06400","operator":"and","partner_start":372,"partner_end":787}],"statement":[{"text":"Residues 306–322 (KEPEIRCDEKPEDLLEE) were the most affected by RbAB binding (Figure 7). This sequence contains the IRCDE motif that was proposed to mediate the interaction with Rb.21 Surprisingly, residues 255–267 (RLEAAACEVNDLG) were also affected, but the decrease in their signal intensities was delayed relative to that of residues 306–322 (Figure 7). This suggested that the pocket domain binds preferentially to residues 306–322 and that it interacts with residues 255–267 with a lower affinity.","type":"Results"}]},{"start":297,"end":341,"reference_id":"25640033","reference_source":"pmid","reference_html":"Structural and functional characterization of the acidic region from the RIZ tumor suppressor. <i> Sun Y, Stine JM, Atwater DZ, Sharmin A, Ross JB, Briknarová K. </i> Biochemistry, 2015","date":"2024-11-25T18:03:14.756Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P06400","operator":null,"partner_start":372,"partner_end":787}],"region_id":"DP01757r007","statement":[{"text":"AR-C bound to RbAB with a Kd of 640 nM, but no interaction between AR-N and RbAB was detected (Figure 8B,C and Table 1).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":254,"end":267,"reference_id":"25640033","reference_source":"pmid","reference_html":"Structural and functional characterization of the acidic region from the RIZ tumor suppressor. <i> Sun Y, Stine JM, Atwater DZ, Sharmin A, Ross JB, Briknarová K. </i> Biochemistry, 2015","date":"2024-11-25T18:12:51.375Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005632","ec_ontology":"ECO","ec_name":"fluorescence anisotropy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Fluorescein isothiocyanate (FITC)-labeled peptides corresponding to RIZ(254–267) (ERLEAAACEVNDLG) and RIZ(309–319) (EIRCDEKPEDL), with their C-termini amidated, were obtained from Genscript at >95% purity. The fluorescein was attached to the N-termini of the peptides via a seven-atom aminohexanoyl spacer."}]},{"term_id":"MOD:00674","term_name":"amidated residue","term_namespace":"Protein modification","start":267,"end":267,"position":"Specific residue","statements":[{"type":"Methods","text":"Fluorescein isothiocyanate (FITC)-labeled peptides corresponding to RIZ(254–267) (ERLEAAACEVNDLG) and RIZ(309–319) (EIRCDEKPEDL), with their C-termini amidated, were obtained from Genscript at >95% purity. The fluorescein was attached to the N-termini of the peptides via a seven-atom aminohexanoyl spacer."}]}],"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P06400","operator":null,"partner_start":372,"partner_end":787}],"region_id":"DP01757r008","statement":[{"text":"The interaction of FITC-RIZ(254–267) with RbAB was readily observed by this method (Figure 11A), and fitting of the anisotropy data yielded a Kd of ~170 μM (Table 2).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":254,"end":267,"reference_id":"25640033","reference_source":"pmid","reference_html":"Structural and functional characterization of the acidic region from the RIZ tumor suppressor. <i> Sun Y, Stine JM, Atwater DZ, Sharmin A, Ross JB, Briknarová K. </i> Biochemistry, 2015","date":"2024-11-25T18:18:16.275Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006309","ec_ontology":"ECO","ec_name":"competitive binding evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Fluorescein isothiocyanate (FITC)-labeled peptides corresponding to RIZ(254–267) (ERLEAAACEVNDLG) and RIZ(309–319) (EIRCDEKPEDL), with their C-termini amidated, were obtained from Genscript at >95% purity. The fluorescein was attached to the N-termini of the peptides via a seven-atom aminohexanoyl spacer."}]},{"term_id":"MOD:00674","term_name":"amidated residue","term_namespace":"Protein modification","start":267,"end":267,"position":"Specific residue","statements":[{"type":"Methods","text":"Fluorescein isothiocyanate (FITC)-labeled peptides corresponding to RIZ(254–267) (ERLEAAACEVNDLG) and RIZ(309–319) (EIRCDEKPEDL), with their C-termini amidated, were obtained from Genscript at >95% purity. The fluorescein was attached to the N-termini of the peptides via a seven-atom aminohexanoyl spacer."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P06400","operator":null,"partner_start":372,"partner_end":787}],"region_id":"DP01757r009","statement":[{"text":"We also used a competitive binding assay with the FITC-RIZ(254–267) peptide (Figure 11B) and established that AR-N binds to RbAB with comparable affinity (Kd ~ 90 μM) (Table 2).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":309,"end":319,"reference_id":"25640033","reference_source":"pmid","reference_html":"Structural and functional characterization of the acidic region from the RIZ tumor suppressor. <i> Sun Y, Stine JM, Atwater DZ, Sharmin A, Ross JB, Briknarová K. </i> Biochemistry, 2015","date":"2024-11-25T18:19:40.409Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006309","ec_ontology":"ECO","ec_name":"competitive binding evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Fluorescein isothiocyanate (FITC)-labeled peptides corresponding to RIZ(254–267) (ERLEAAACEVNDLG) and RIZ(309–319) (EIRCDEKPEDL), with their C-termini amidated, were obtained from Genscript at >95% purity. The fluorescein was attached to the N-termini of the peptides via a seven-atom aminohexanoyl spacer."}]},{"term_id":"MOD:00674","term_name":"amidated residue","term_namespace":"Protein modification","start":319,"end":319,"position":"Specific residue","statements":[{"type":"Methods","text":"Fluorescein isothiocyanate (FITC)-labeled peptides corresponding to RIZ(254–267) (ERLEAAACEVNDLG) and RIZ(309–319) (EIRCDEKPEDL), with their C-termini amidated, were obtained from Genscript at >95% purity. The fluorescein was attached to the N-termini of the peptides via a seven-atom aminohexanoyl spacer."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P06400","operator":null,"partner_start":372,"partner_end":787}],"region_id":"DP01757r010","statement":[{"text":"Fluorescence anisotropy experiments with the FITC-RIZ(309–319) peptide, which contains the IRCDE motif, and competition assays with AR-C (Figure 11C,D) yielded Kd values of ~360 and ~110 nM for the interaction of RbAB with the FITC-RIZ(309–319) peptide and AR-C, respectively (Table 2).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":309,"end":319,"reference_id":"25640033","reference_source":"pmid","reference_html":"Structural and functional characterization of the acidic region from the RIZ tumor suppressor. <i> Sun Y, Stine JM, Atwater DZ, Sharmin A, Ross JB, Briknarová K. </i> Biochemistry, 2015","date":"2024-11-25T18:19:48.502Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005632","ec_ontology":"ECO","ec_name":"fluorescence anisotropy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Fluorescein isothiocyanate (FITC)-labeled peptides corresponding to RIZ(254–267) (ERLEAAACEVNDLG) and RIZ(309–319) (EIRCDEKPEDL), with their C-termini amidated, were obtained from Genscript at >95% purity. The fluorescein was attached to the N-termini of the peptides via a seven-atom aminohexanoyl spacer."}]},{"term_id":"MOD:00674","term_name":"amidated residue","term_namespace":"Protein modification","start":319,"end":319,"position":"Specific residue","statements":[{"type":"Methods","text":"Fluorescein isothiocyanate (FITC)-labeled peptides corresponding to RIZ(254–267) (ERLEAAACEVNDLG) and RIZ(309–319) (EIRCDEKPEDL), with their C-termini amidated, were obtained from Genscript at >95% purity. The fluorescein was attached to the N-termini of the peptides via a seven-atom aminohexanoyl spacer."}]}],"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P06400","operator":null,"partner_start":372,"partner_end":787}],"region_id":"DP01757r011","statement":[{"text":"Fluorescence anisotropy experiments with the FITC-RIZ(309–319) peptide, which contains the IRCDE motif, and competition assays with AR-C (Figure 11C,D) yielded Kd values of ~360 and ~110 nM for the interaction of RbAB with the FITC-RIZ(309–319) peptide and AR-C, respectively (Table 2).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_Q13029","date":"2018-08-08T15:35:48.000Z","acc":"Q13029","name":"PR domain zinc finger protein 2","length":1718,"organism":"Homo sapiens","dataset":["Cancer-related proteins","Age-related disorders proteins"],"UniParc":"UPI00001740E0","genes":[{"name":{"value":"PRDM2"},"synonyms":[{"value":"KMT8"},{"value":"RIZ"}]}],"alphafold_very_low_content":0.7339930151338766,"disorder_content":0.08440046565774156,"disprot_consensus":{"full":[{"start":197,"end":341,"type":"D"}],"Structural state":[{"start":197,"end":341,"type":"D"}],"Molecular function":[{"start":254,"end":267,"type":"F"},{"start":297,"end":341,"type":"F"}]}},{"acc":"Q0GBY3","sequence":"MSKIFVNPSAIRAGLADLEMAEETVDLINRNIEDNQAHLQGEPIEVDDLPEDMKRLHLDDEKSSNLGEMVRVGEGKYREDFQMDEGEDPNLLFQSYLDNVGVQIVRQMRSGERFLKIWSQTVEEIVSYVTVNFPNPPRRSSENKSTQTTGRELKKETTSAFSQRESQPSKARMVAQVAPGPPALEWSATNEEDDLSVEAEIAHQIAESFSKKYKFPSRSSGIFLYNFEQLKMNLDDIVKEAKNVPGVTRLAHDGSKIPLRCVLGYVALANSKKFQLLVEADKLSKIMQDDLNRYTSC","creator":"smribeiro","dataset":["Viral proteins","Neglected tropical diseases proteins"],"date":"2018-08-08T17:32:41.000Z","disprot_id":"DP01759","features":{"pfam":[{"id":"PF03012","name":"Phosphoprotein","start":1,"end":296}],"gene3D":[{"start":186,"end":297,"id":"1.20.120.820","name":"Phosphoprotein, C-terminal domain","_id":"685af523b4ac24d5329d9287"}]},"genes":[{"name":{"value":"P","evidences":[],"_id":"685af523b4ac24d5329d9295"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d9294"}],"length":297,"name":"Phosphoprotein","ncbi_taxon_id":445791,"organism":"Rabies virus (strain China/MRV)","regions_counter":4,"released":"2018_11","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Rhabdoviridae","Lyssavirus"],"UniParc":"UPI0000DE1E41","uniref100":"UniRef100_Q0GBY3","uniref50":"UniRef50_P22363","uniref90":"UniRef90_P22363","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":68,"interaction_partner":[],"reference_html":"Modular organization of rabies virus phosphoprotein. <i> Gerard FC, Ribeiro Ede A, Leyrat C, Ivanov I, Blondel D, Longhi S, Ruigrok RW, Jamin M. </i> J Mol Biol, 2009","reference_id":"19341745","region_id":"DP01759r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The far-UV CD spectrum of full-length P, PCED, PCTD, and PΔ91–131 exhibited two dichroic bands near 208 nm and 222 nm, indicating the presence of α-helical structure, while the spectrum obtained with PNTD showed one minor dichroic band near 222 nm and one below 200 nm, suggesting a low α-helical content (Fig. 6).","_id":"685af523b4ac24d5329d9289"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T12:58:51.303Z","_id":"685af523b4ac24d5329d928a"},"version":3,"_id":"685af523b4ac24d5329d9288","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":68,"interaction_partner":[],"reference_html":"Modular organization of rabies virus phosphoprotein. <i> Gerard FC, Ribeiro Ede A, Leyrat C, Ivanov I, Blondel D, Longhi S, Ruigrok RW, Jamin M. </i> J Mol Biol, 2009","reference_id":"19341745","region_id":"DP01759r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The hydrodynamic radii (Stokes' radius, RS) of full-length P, PNTD, PCED, PCTD, PΔC120, and PΔ91–131 were determined by calibrating the SEC column with standard proteins.71 On a plot of the hydrodynamic radius as a function of molecular mass (Fig. 7b), PCED and PCTD appeared as native globular proteins, PΔ91–131, PΔC120, and full-length P were intermediate between native and unfolded proteins, indicating that these proteins are non-globular, and PNTD appeared as an unfolded protein.","_id":"685af523b4ac24d5329d928f"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-13T12:58:52.335Z","_id":"685af523b4ac24d5329d9290"},"version":3,"_id":"685af523b4ac24d5329d928e","reference_source":"pmid"}],"__v":0,"disorder_content":0.22895622895622897,"disprot_consensus":{"full":[{"start":1,"end":68,"type":"D"}],"Structural state":[{"start":1,"end":68,"type":"D"}]}},{"features":{"pfam":[{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":244,"end":537},{"id":"PF08917","name":"Transforming growth factor beta receptor 2 ectodomain","start":49,"end":157}],"gene3D":[{"start":330,"end":549,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"},{"start":234,"end":329,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":38,"end":159,"id":"2.10.60.10","name":"CD59"}]},"uniref50":"UniRef50_P37173","sequence":"MGRGLLRGLWPLHIVLWTRIASTIPPHVQKSVNNDMIVTDNNGAVKFPQLCKFCDVRFSTCDNQKSCMSNCSITSICEKPQEVCVAVWRKNDENITLETVCHDPKLPYHDFILEDAASPKCIMKEKKKPGETFFMCSCSSDECNDNIIFSEEYNTSNPDLLLVIFQVTGISLLPPLGVAISVIIIFYCYRVNRQQKLSSTWETGKTRKLMEFSEHCAIILEDDRSDISSTCANNINHNTELLPIELDTLVGKGRFAEVYKAKLKQNTSEQFETVAVKIFPYEEYASWKTEKDIFSDINLKHENILQFLTAEERKTELGKQYWLITAFHAKGNLQEYLTRHVISWEDLRKLGSSLARGIAHLHSDHTPCGRPKMPIVHRDLKSSNILVKNDLTCCLCDFGLSLRLDPTLSVDDLANSGQVGTARYMAPEVLESRMNLENVESFKQTDVYSMALVLWEMTSRCNAVGEVKDYEPPFGSKVREHPCVESMKDNVLRDRGRPEIPSFWLNHQGIQMVCETLTECWDHDPEARLTAQCVAERFSELEHLDRLSGRSCSEEKIPEDGSLNTTK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P37173","disprot_id":"DP01760","ncbi_taxon_id":9606,"regions_counter":7,"creator":"smribeiro","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":48,"region_id":"DP01760r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the human TbetaR2 ectodomain--TGF-beta3 complex. <i> Hart PJ, Deep S, Taylor AB, Shu Z, Hinck CS, Hinck AP. </i> Nat Struct Biol, 2002","statement":[{"text":"Residues missing in electron density. Numbers in the manuscripts mentioning disorder in the N-terminal ligand binding domain always refer to mature protein lacking the signal peptide (residues 1-22).","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"smribeiro","start":38,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1KTZ"}],"reference_id":"11850637","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":48,"region_id":"DP01760r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure and backbone dynamics of the TGFbeta type II receptor extracellular domain. <i> Deep S, Walker KP, Shu Z, Hinck AP. </i> Biochemistry, 2003","statement":[{"text":"The N- and C-terminal segments, residues 15−25 and 127−136, respectively, exhibit no detectable long-range NOE interactions and are structurally disordered (Figure 4B).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"smribeiro","start":38,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1PLO"}],"reference_id":"12939140","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":159,"region_id":"DP01760r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure and backbone dynamics of the TGFbeta type II receptor extracellular domain. <i> Deep S, Walker KP, Shu Z, Hinck AP. </i> Biochemistry, 2003","statement":[{"text":"The N- and C-terminal segments, residues 15−25 and 127−136, respectively, exhibit no detectable long-range NOE interactions and are structurally disordered (Figure 4B).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"smribeiro","start":150,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1PLO"}],"reference_id":"12939140","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":48,"region_id":"DP01760r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Cooperative assembly of TGF-beta superfamily signaling complexes is mediated by two disparate mechanisms and distinct modes of receptor binding. <i> Groppe J, Hinck CS, Samavarchi-Tehrani P, Zubieta C, Schuermann JP, Taylor AB, Schwarz PM, Wrana JL, Hinck AP. </i> Mol Cell, 2008","statement":[{"text":"The most striking difference lies with seven residues of the flexible N-terminal extension of TβRII that become ordered in the ternary complex, providing extensive receptor-receptor contact (Figure 2A and Figure S2).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ahatos","start":38,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2PJY"}],"reference_id":"18243111","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":48,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Cooperative assembly of TGF-beta superfamily signaling complexes is mediated by two disparate mechanisms and distinct modes of receptor binding. <i> Groppe J, Hinck CS, Samavarchi-Tehrani P, Zubieta C, Schuermann JP, Taylor AB, Schwarz PM, Wrana JL, Hinck AP. </i> Mol Cell, 2008","statement":[{"text":"The bulk of receptor-receptor interaction arises from seven residues of the disordered N-terminal extension of TβRII that become ordered in the ternary complex and tether TβRI to its docking site at the composite interface.","type":"Results"}],"term_id":"GO:0005515","curator_id":"ahatos","start":38,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"18243111","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01760r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":48,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Cooperative assembly of TGF-beta superfamily signaling complexes is mediated by two disparate mechanisms and distinct modes of receptor binding. <i> Groppe J, Hinck CS, Samavarchi-Tehrani P, Zubieta C, Schuermann JP, Taylor AB, Schwarz PM, Wrana JL, Hinck AP. </i> Mol Cell, 2008","statement":[{"text":"The disordered N-terminal extension of TβRII becomes partially structured in the complex, tethering TβRI to its docking site at the composite interface.","type":"Discussion"}],"term_id":"GO:0060090","curator_id":"ahatos","start":38,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"18243111","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01760r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":48,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Cooperative assembly of TGF-beta superfamily signaling complexes is mediated by two disparate mechanisms and distinct modes of receptor binding. <i> Groppe J, Hinck CS, Samavarchi-Tehrani P, Zubieta C, Schuermann JP, Taylor AB, Schwarz PM, Wrana JL, Hinck AP. </i> Mol Cell, 2008","statement":[{"text":"The most striking difference lies with seven residues of the flexible N-terminal extension of TβRII that become ordered in the ternary complex, providing extensive receptor-receptor contact (Figure 2A and Figure S2).","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"ahatos","start":38,"term_ontology":"IDPO","curator_name":"András Hatos","reference_id":"18243111","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01760r007","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_P37173","date":"2018-08-08T22:49:32.000Z","acc":"P37173","name":"TGF-beta receptor type-2","length":567,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI0000136CD6","genes":[{"name":{"value":"TGFBR2"}}],"alphafold_very_low_content":0.1728395061728395,"disorder_content":0.037037037037037035,"disprot_consensus":{"full":[{"start":38,"end":48,"type":"T"},{"start":150,"end":159,"type":"D"}],"Structural state":[{"start":38,"end":48,"type":"D"},{"start":150,"end":159,"type":"D"}],"Molecular function":[{"start":38,"end":48,"type":"F"}],"Structural transition":[{"start":38,"end":48,"type":"T"}]}},{"features":{"pfam":[{"id":"PF05354","name":"Phage Head-Tail Attachment protein","start":8,"end":105}],"gene3D":[{"start":1,"end":117,"id":"2.40.10.180","name":"Phage tail proteins"}]},"uniref50":"UniRef50_P03714","sequence":"MADFDNLFDAAIARADETIRGYMGTSATITSGEQSGAVIRGVFDDPENISYAGQGVRVEGSSPSLFVRTDEVRQLRRGDTLTIGEENFWVDRVSPDDGGSCHLWLGRGVPPAVNRRR","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Uroviricota","Caudoviricetes","Caudovirales","Siphoviridae","Lambdavirus"],"uniref90":"UniRef90_P03714","disprot_id":"DP01762","ncbi_taxon_id":10710,"regions_counter":9,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":24,"region_id":"DP01762r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The solution structure of the bacteriophage lambda head-tail joining protein, gpFII. <i> Maxwell KL, Yee AA, Arrowsmith CH, Gold M, Davidson AR. </i> J Mol Biol, 2002","statement":[{"text":"It also displays two large unstructured regions at the N terminus (residues 1–24) and in a large loop near the middle of the protein (residues 46–62).","type":"Abstract"},{"text":"The structure of gpFII consists of a single domain, with two large disordered regions; one at the N terminus (residues 1–24), and one in the middle of the protein (residues 46–62), both of which are characterized by no medium or long range NOEs.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1K0H"}],"reference_id":"12083526","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-02T10:42:07.592Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":62,"region_id":"DP01762r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The solution structure of the bacteriophage lambda head-tail joining protein, gpFII. <i> Maxwell KL, Yee AA, Arrowsmith CH, Gold M, Davidson AR. </i> J Mol Biol, 2002","statement":[{"text":"It also displays two large unstructured regions at the N terminus (residues 1–24) and in a large loop near the middle of the protein (residues 46–62).","type":"Results"},{"text":"The structure of gpFII consists of a single domain, with two large disordered regions; one at the N terminus (residues 1–24), and one in the middle of the protein (residues 46–62), both of which are characterized by no medium or long range NOEs.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":46,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1K0H"}],"reference_id":"12083526","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-02T10:42:03.655Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":24,"reference_id":"20660769","reference_source":"pmid","reference_html":"Phages have adapted the same protein fold to fulfill multiple functions in virion assembly. <i> Cardarelli L, Pell LG, Neudecker P, Pirani N, Liu A, Baker LA, Rubinstein JL, Maxwell KL, Davidson AR. </i> Proc Natl Acad Sci U S A, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2KX4"}],"region_id":"DP01762r003","statement":[{"text":"Unstructured regions of gpFII (Fig. S2A) and gpV (3) were delineated by measuring {1H}-15N heteronuclear NOEs.","type":"Figure"},{"text":"The NMR solution structure of gpFII displays significant disorder. (A) Values of the heteronuclear {1H}15N NOE as a function of position in gpFII. Residues that fall below the red horizontal line representing a cutoff of +0.65 show increased dynamics on the fast, ns-ps time scale (1). These include residues 1–24, 46–62, and 109–117.","type":"Supplementary material"},{"text":"In this model, the large N-terminal unstructured region (residues 1–24) of gpFII protrudes from one side of the ring whereas much of the central β3–β4 unstructured region (residues 46–62) is positioned on the opposite side.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-02T10:27:51.389Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":46,"end":62,"reference_id":"20660769","reference_source":"pmid","reference_html":"Phages have adapted the same protein fold to fulfill multiple functions in virion assembly. <i> Cardarelli L, Pell LG, Neudecker P, Pirani N, Liu A, Baker LA, Rubinstein JL, Maxwell KL, Davidson AR. </i> Proc Natl Acad Sci U S A, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2KX4"}],"region_id":"DP01762r004","statement":[{"text":"Unstructured regions of gpFII (Fig. S2A) and gpV (3) were delineated by measuring {1H}-15N heteronuclear NOEs.","type":"Figure"},{"text":"The NMR solution structure of gpFII displays significant disorder. (A) Values of the heteronuclear {1H}15N NOE as a function of position in gpFII. Residues that fall below the red horizontal line representing a cutoff of +0.65 show increased dynamics on the fast, ns-ps time scale (1). These include residues 1–24, 46–62, and 109–117.","type":"Supplementary material"},{"text":"In this model, the large N-terminal unstructured region (residues 1–24) of gpFII protrudes from one side of the ring whereas much of the central β3–β4 unstructured region (residues 46–62) is positioned on the opposite side.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-02T10:27:49.959Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":53,"end":61,"reference_id":"20660769","reference_source":"pmid","reference_html":"Phages have adapted the same protein fold to fulfill multiple functions in virion assembly. <i> Cardarelli L, Pell LG, Neudecker P, Pirani N, Liu A, Baker LA, Rubinstein JL, Maxwell KL, Davidson AR. </i> Proc Natl Acad Sci U S A, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0019068","term_name":"virion assembly","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01762r005","statement":[{"text":"One of the most strongly dominant-negative mutants, Δ53–61, was titrated into a reaction containing a constant level of WT protein (Fig. S4). The inhibitory effect of this mutant was found to be strongly dose-dependent, and the curve of inhibition versus protein concentration could be fit by an exponential function assuming a simple competition between WT and mutant gpFII molecules. Fitting of these curves indicated that, if one third of the gpFII molecules incorporated into a phage were mutant, assembly would be inhibited. Further in vitro activity assays and EM experiments clearly showed that the Δ53–61 mutant inhibited phage assembly through its ability to bind heads, but not tails (SI Methods and Tables S2 and S3).","type":"Results"},{"text":"Taken together, the behavior of the gpFII mutants supports our model of the oligomeric structure of gpFII within phage particles.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-02T10:38:52.319Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A late phase of the viral life cycle during which all the components necessary for the formation of a mature virion collect at a particular site in the cell and the basic structure of the virus particle is formed.\" [ISBN:0121585336]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":53,"end":61,"reference_id":"20660769","reference_source":"pmid","reference_html":"Phages have adapted the same protein fold to fulfill multiple functions in virion assembly. <i> Cardarelli L, Pell LG, Neudecker P, Pirani N, Liu A, Baker LA, Rubinstein JL, Maxwell KL, Davidson AR. </i> Proc Natl Acad Sci U S A, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0019068","term_name":"virion assembly","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0007044","ec_ontology":"ECO","ec_name":"transmission electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01762r006","statement":[{"text":"One of the most strongly dominant-negative mutants, Δ53–61, was titrated into a reaction containing a constant level of WT protein (Fig. S4). The inhibitory effect of this mutant was found to be strongly dose-dependent, and the curve of inhibition versus protein concentration could be fit by an exponential function assuming a simple competition between WT and mutant gpFII molecules. Fitting of these curves indicated that, if one third of the gpFII molecules incorporated into a phage were mutant, assembly would be inhibited. Further in vitro activity assays and EM experiments clearly showed that the Δ53–61 mutant inhibited phage assembly through its ability to bind heads, but not tails (SI Methods and Tables S2 and S3).","type":"Results"},{"text":"Taken together, the behavior of the gpFII mutants supports our model of the oligomeric structure of gpFII within phage particles.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-02T10:38:48.960Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A late phase of the viral life cycle during which all the components necessary for the formation of a mature virion collect at a particular site in the cell and the basic structure of the virus particle is formed.\" [ISBN:0121585336]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":53,"end":61,"reference_id":"20660769","reference_source":"pmid","reference_html":"Phages have adapted the same protein fold to fulfill multiple functions in virion assembly. <i> Cardarelli L, Pell LG, Neudecker P, Pirani N, Liu A, Baker LA, Rubinstein JL, Maxwell KL, Davidson AR. </i> Proc Natl Acad Sci U S A, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0019068","term_name":"virion assembly","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0006091","ec_ontology":"ECO","ec_name":"functional complementation evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01762r007","statement":[{"text":"Fig. S3. Overlays of gpFII used to build gpFII oligomeric models. (A) Overlay of gpFII to an Hcp1 monomer. (B) Overlay of gpFII to residues 167–326 of Mu gp44. The structural overlay of gpFII and Hcp1 and gp44 is displayed in the center and the individual monomers are displayed on either side. (C ) Summary of all structural alignments discussed in this work. Initial alignments were made using DaliLite (1) or FATCAT (2) and then refined in Swiss-PDBViewer (3). 1. Holm L, Park J (2000) DaliLite workbench for protein structure comparison. Bioinformatics 16:566–567. 2. Ye Y, Godzik A (2003) Flexible structure alignment by chaining aligned fragment pairs allowing twists. Bioinformatics 19 (suppl 2):ii246–ii255. 3. Guex N, Peitsch MC (1997) SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis 18:2714–2723. Fig. S4. In vitro titration of the Δ53–61 gpFII protein. Equal volumes of purified WT and Δ53–61 gpFII protein were mixed in vitro before testing for com- plementation of an FIIam extract. WT protein was kept at a concentration of 1 μM and Δ53–61 gpFII protein concentration was varied from 0.1 to 50 μM. Even at very low ratios, e.g., 1:1, the Δ53–61 gpFII protein was able to exert a dominant negative effect on WT protein.","type":"Supplementary material"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-02T10:38:41.743Z"},"ec_go":"IGI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A late phase of the viral life cycle during which all the components necessary for the formation of a mature virion collect at a particular site in the cell and the basic structure of the virus particle is formed.\" [ISBN:0121585336]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":24,"reference_id":"20660769","reference_source":"pmid","reference_html":"Phages have adapted the same protein fold to fulfill multiple functions in virion assembly. <i> Cardarelli L, Pell LG, Neudecker P, Pirani N, Liu A, Baker LA, Rubinstein JL, Maxwell KL, Davidson AR. </i> Proc Natl Acad Sci U S A, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0019068","term_name":"virion assembly","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01762r008","statement":[{"text":"Deletions of the N-terminal unstructured region, which is predicted to lie on the top surface, caused no dominant-negative behavior. Furthermore, combining an N-terminal deletion with the Δ46–61 deletion resulted in no dominant-negative phenotype, implying that activity of the putative head-binding gpFII N terminus is required for imparting a dominant negative phenotype.","type":"Results"},{"text":"Taken together, the behavior of the gpFII mutants supports our model of the oligomeric structure of gpFII within phage particles. Mutants bearing amino acid substitutions or deletions on the putative bottom surface displayed dominant-negative phenotypes because they could still bind heads and thereby inhibit the assembly of phage even in the presence of WT gpFII. By contrast, deletion of the N-terminal region, which is expected to be involved in head-binding, caused loss of activity without a dominant-negative effect.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-02T10:38:26.145Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A late phase of the viral life cycle during which all the components necessary for the formation of a mature virion collect at a particular site in the cell and the basic structure of the virus particle is formed.\" [ISBN:0121585336]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":24,"reference_id":"20660769","reference_source":"pmid","reference_html":"Phages have adapted the same protein fold to fulfill multiple functions in virion assembly. <i> Cardarelli L, Pell LG, Neudecker P, Pirani N, Liu A, Baker LA, Rubinstein JL, Maxwell KL, Davidson AR. </i> Proc Natl Acad Sci U S A, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0019068","term_name":"virion assembly","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0007044","ec_ontology":"ECO","ec_name":"transmission electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01762r009","statement":[{"text":"Deletions of the N-terminal unstructured region, which is predicted to lie on the top surface, caused no dominant-negative behavior. Furthermore, combining an N-terminal deletion with the Δ46–61 deletion resulted in no dominant-negative phenotype, implying that activity of the putative head-binding gpFII N terminus is required for imparting a dominant negative phenotype.","type":"Results"},{"text":"Taken together, the behavior of the gpFII mutants supports our model of the oligomeric structure of gpFII within phage particles. Mutants bearing amino acid substitutions or deletions on the putative bottom surface displayed dominant-negative phenotypes because they could still bind heads and thereby inhibit the assembly of phage even in the presence of WT gpFII. By contrast, deletion of the N-terminal region, which is expected to be involved in head-binding, caused loss of activity without a dominant-negative effect.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-02T10:38:23.626Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A late phase of the viral life cycle during which all the components necessary for the formation of a mature virion collect at a particular site in the cell and the basic structure of the virus particle is formed.\" [ISBN:0121585336]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2018_11","uniref100":"UniRef100_P03714","date":"2018-08-09T08:26:02.000Z","acc":"P03714","name":"Head-tail connector protein FII","length":117,"organism":"Escherichia phage lambda","dataset":["Viral proteins"],"UniParc":"UPI0000113241","genes":[{"name":{"value":"FII"},"olnNames":[{"value":"lambdap10"}]}],"disorder_content":0.3504273504273504,"disprot_consensus":{"full":[{"start":1,"end":24,"type":"D"},{"start":46,"end":62,"type":"D"}],"Structural state":[{"start":1,"end":24,"type":"D"},{"start":46,"end":62,"type":"D"}],"Biological process":[{"start":1,"end":24,"type":"F"},{"start":53,"end":61,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00449","name":"Urease alpha-subunit, N-terminal domain","start":273,"end":392},{"id":"PF00547","name":"Urease, gamma subunit","start":1,"end":100},{"id":"PF00699","name":"Urease beta subunit","start":134,"end":230},{"id":"PF01979","name":"Amidohydrolase family","start":398,"end":724},{"id":"PF18473","name":"Urease subunit beta-alpha linker domain","start":232,"end":263}],"gene3D":[{"start":4,"end":124,"id":"3.30.280.10","name":"Urease, gamma-like subunit"},{"start":150,"end":271,"id":"2.10.150.10","name":"Urease, beta subunit"},{"start":272,"end":753,"id":"2.30.40.10","name":"Urease, subunit C, domain 1"},{"start":402,"end":821,"id":"3.20.20.140","name":"Metal-dependent hydrolases"}]},"uniref50":"UniRef50_E0ZS48","sequence":"MKLSPREVEKISLHNAGFLAQKRLARGVRLNYSESVALIASQILEHARDGEKTVAQLMSIGKHLLGRRQVLPAVPHLLNIIQVEATLPNGTKLVTVHDPIANENGDLEEALYGSFLPVPSLDKFAESKEEHKIPGEIICADGRLTLNPGRKAVFLKVVNHGDRPIQVGSHYHFIEVNPYLTFDRRKAYGMRLNIAAGDSVRFEPGDHKTVNLVSIGGNKIIRGGNAIADGPVNEANCKAAMEIVCRREFGHKEEEDASEGVTTGDPDCPFTKAIPREEYANKYGPTIGDKIRLGDTDLIAEIEKDFALYGDESVFGGGKVIRDGMGQSSGHPPAMSLDTVITSAVIIDYTGIIKADIGIKDGLIASIGKAGNPDIMNGVFPNMIIGVNTEVICGEGLIVTAGGIDCHVHYICPQSLDEAISSGITTVVGGGTGPTDGSRATTCTPAPTQMKLMLQSTDDIPLNFGFTGKGSGSHPDELHEIIKAGAMGLKLHEDWGCTPAAIDNCLAVAEQHDIQVNIHTDTVNESGFVEHTIAAFNGRTIHTYHSEGAGGGHAPDIIKVCSMKNVLPSSTNTTRPLTSNTVDEHLDMLMVCHKLNREIPEDLAFASSRVREQTIAAEDILHDIGGISIISSDAQAVGRIGEVISCTWQTADKMKAERGPLQPDGSDNDNFRIKRYIAKYTINPAIVNGISQYVGSVEVGKLADLVIWKPSFFGAKPDIVIKGGSIAWADMGDPNGSIPTPEPVLMRPMYGTLGKAGSALSIAFVSKAALDLGVKVLYGLNKRVEAVSNVRKLTKLDLKLNNSLPEITVCPETFTVTVDGQALSSEAVTTLPLSQNYFIF","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","fabids","Fabales","Fabaceae","Papilionoideae","50 kb inversion clade","NPAAA clade","indigoferoid/millettioid clade","Phaseoleae","Canavalia"],"uniref90":"UniRef90_E6Y5X0","disprot_id":"DP01763","ncbi_taxon_id":3823,"regions_counter":11,"creator":"emaiani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":321,"region_id":"DP01763r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structural analysis of the interaction between Jaburetox, an intrinsically disordered protein, and membrane models. <i> Broll V, Martinelli AHS, Lopes FC, Fruttero LL, Zambelli B, Salladini E, Dobrovolska O, Ciurli S, Carlini CR. </i> Colloids Surf B Biointerfaces, 2017","term_id":"IDPO:0000002","curator_id":"esalladini","start":232,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28892869","statement":[{"text":"Indeed, while the CD spectrum of Jbtx in the absence of SDS presented a minimum centred at ca. 200 nm, characteristic of a random coil conformation, in the presence of 3–15 mM SDS this feature shifted to ∼205–210 nm, with the insurgence of a minimum at around 207 nm, typical of the presence of α-helices and β-sheets; consistently, the ellipticity increase around 195 nm suggests the acquisition of secondary structure by Jbtx in the presence of SDS micelles.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-07-13T13:35:21.677Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP01763r002","ec_ontology":"ECO","end":321,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":232,"version":3,"statement":[{"text":"Superimposition of the NMR spectra of Jbtx in the absence and presence of bicelles revealed some changes in the chemical shift of a number of amino acids, even though the characteristic profile of an intrinsically disordered protein was maintained (Fig. 7B and D).","type":"Results"}],"term_name":"disorder","reference_html":"Structural analysis of the interaction between Jaburetox, an intrinsically disordered protein, and membrane models. <i> Broll V, Martinelli AHS, Lopes FC, Fruttero LL, Zambelli B, Salladini E, Dobrovolska O, Ciurli S, Carlini CR. </i> Colloids Surf B Biointerfaces, 2017","released":"2022_03","term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"28892869","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"esalladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-13T13:56:33.089Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":321,"term_name":"lipid binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural analysis of the interaction between Jaburetox, an intrinsically disordered protein, and membrane models. <i> Broll V, Martinelli AHS, Lopes FC, Fruttero LL, Zambelli B, Salladini E, Dobrovolska O, Ciurli S, Carlini CR. </i> Colloids Surf B Biointerfaces, 2017","term_id":"GO:0008289","curator_id":"esalladini","start":232,"term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"28892869","version":4,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01763r003","statement":[{"text":"Superimposition of the NMR spectra of Jbtx in the absence and presence of bicelles revealed some changes in the chemical shift of a number of amino acids, even though the characteristic profile of an intrinsically disordered protein was maintained (Fig. 7B and D).","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-07-13T13:35:27.278Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":232,"end":321,"reference_id":"28892869","reference_source":"pmid","reference_html":"Structural analysis of the interaction between Jaburetox, an intrinsically disordered protein, and membrane models. <i> Broll V, Martinelli AHS, Lopes FC, Fruttero LL, Zambelli B, Salladini E, Dobrovolska O, Ciurli S, Carlini CR. </i> Colloids Surf B Biointerfaces, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01763r004","statement":[{"text":"Indeed, while the CD spectrum of Jbtx in the absence of SDS presented a minimum centred at ca. 200 nm, characteristic of a random coil conformation, in the presence of 3–15 mM SDS this feature shifted to ∼205–210 nm, with the insurgence of a minimum at around 207 nm, typical of the presence of α-helices and β-sheets; consistently, the ellipticity increase around 195 nm suggests the acquisition of secondary structure by Jbtx in the presence of SDS micelles.","type":"Results"},{"text":"Compared to the CD spectrum of free Jbtx, which showed a pronounced negative peak around 200 nm typical of random coil structures, the CD spectrum of Jbtx in the presence of negatively charged bicelles shows a reduced intensity in the random coil region, indicative of an increase in the polypeptide secondary structure content (Fig. 7A).","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-07-13T13:35:24.727Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":232,"end":321,"reference_id":"28892869","reference_source":"pmid","reference_html":"Structural analysis of the interaction between Jaburetox, an intrinsically disordered protein, and membrane models. <i> Broll V, Martinelli AHS, Lopes FC, Fruttero LL, Zambelli B, Salladini E, Dobrovolska O, Ciurli S, Carlini CR. </i> Colloids Surf B Biointerfaces, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01763r005","statement":[{"text":"Indeed, while the CD spectrum of Jbtx in the absence of SDS presented a minimum centred at ca. 200 nm, characteristic of a random coil conformation, in the presence of 3–15 mM SDS this feature shifted to ∼205–210 nm, with the insurgence of a minimum at around 207 nm, typical of the presence of α-helices and β-sheets; consistently, the ellipticity increase around 195 nm suggests the acquisition of secondary structure by Jbtx in the presence of SDS micelles.","type":"Results"},{"text":"Compared to the CD spectrum of free Jbtx, which showed a pronounced negative peak around 200 nm typical of random coil structures, the CD spectrum of Jbtx in the presence of negatively charged bicelles shows a reduced intensity in the random coil region, indicative of an increase in the polypeptide secondary structure content (Fig. 7A).","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-07-13T13:35:26.457Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":232,"end":321,"reference_id":"28892869","reference_source":"pmid","reference_html":"Structural analysis of the interaction between Jaburetox, an intrinsically disordered protein, and membrane models. <i> Broll V, Martinelli AHS, Lopes FC, Fruttero LL, Zambelli B, Salladini E, Dobrovolska O, Ciurli S, Carlini CR. </i> Colloids Surf B Biointerfaces, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01763r006","statement":[{"text":"The 1H,15N-HSQC NMR spectrum of Jbtx, recorded in the absence and presence of SDS below and above its CMC (0.25 and 10–15 mM, respectively, Fig. 3C) reveals that the protein does not change its structure in the presence of SDS below its CMC, while large chemical shifts modifications are observed in solutions containing SDS above the CMC, indicative of structural conformational changes.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-07-13T13:35:23.356Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":232,"end":321,"reference_id":"25605001","reference_source":"pmid","reference_html":"Pliable natural biocide: Jaburetox is an intrinsically disordered insecticidal and fungicidal polypeptide derived from jack bean urease. <i> Lopes FC, Dobrovolska O, Real-Guerra R, Broll V, Zambelli B, Musiani F, Uversky VN, Carlini CR, Ciurli S. </i> FEBS J, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01763r007","statement":[{"text":"The SDS/PAGE profile of the final purified protein is shown in Fig. 1C. Notably, although the predicted molecular mass determined from the amino acid sequence of Jaburetox with the six-histidine extension is 11 kDa, the protein exhibited a 2 kDa shift in the SDS/PAGE and migrated as a 13 kDa polypeptide.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-07-13T13:35:19.015Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":232,"end":321,"reference_id":"25605001","reference_source":"pmid","reference_html":"Pliable natural biocide: Jaburetox is an intrinsically disordered insecticidal and fungicidal polypeptide derived from jack bean urease. <i> Lopes FC, Dobrovolska O, Real-Guerra R, Broll V, Zambelli B, Musiani F, Uversky VN, Carlini CR, Ciurli S. </i> FEBS J, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006212","ec_ontology":"ECO","ec_name":"particle scattering evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01763r008","statement":[{"text":"The hydrodynamic radius measured by QELS is 2.7 ± 0.1 nm. This value is larger than the expected value of 1.74 nm for a well-folded protein of the same molecular mass [31], and is very close to that predicted for intrinsically disordered pre-molten globular proteins (2.46 nm) or random coil proteins (2.77 nm) of the same molecular mass [31].","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-07-13T13:35:18.280Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":232,"end":321,"reference_id":"25605001","reference_source":"pmid","reference_html":"Pliable natural biocide: Jaburetox is an intrinsically disordered insecticidal and fungicidal polypeptide derived from jack bean urease. <i> Lopes FC, Dobrovolska O, Real-Guerra R, Broll V, Zambelli B, Musiani F, Uversky VN, Carlini CR, Ciurli S. </i> FEBS J, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01763r009","statement":[{"text":"The CD spectrum of the protein under native conditions (Fig. 2A) presents features typical of a random coil conformation, with a minimum centered at 200 nm.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-07-13T13:35:16.624Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":232,"end":321,"reference_id":"25605001","reference_source":"pmid","reference_html":"Pliable natural biocide: Jaburetox is an intrinsically disordered insecticidal and fungicidal polypeptide derived from jack bean urease. <i> Lopes FC, Dobrovolska O, Real-Guerra R, Broll V, Zambelli B, Musiani F, Uversky VN, Carlini CR, Ciurli S. </i> FEBS J, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"BMRB","id":"19830"},{"db":"PDB","id":"2mm8"}],"region_id":"DP01763r010","statement":[{"text":"Figure 4 shows the 1H-15N heteronuclear single quantum coherence (HSQC) spectrum of Jaburetox. The spectrum is characterized by low signal dispersion in the proton dimension, indicative of a disordered state of the protein.","type":"Results"},{"text":"The NMR-derived solution structural ensemble of Jaburetox, featuring large values of rmsd, confirms its disordered fold, as predicted by earlier [23] and the present bioinformatics studies (Fig. 3).","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-07-13T13:35:15.691Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":232,"end":321,"reference_id":"17875343","reference_source":"pmid","reference_html":"Jaburetox-2Ec: an insecticidal peptide derived from an isoform of urease from the plant Canavalia ensiformis. <i> Mulinari F, Stanisçuaski F, Bertholdo-Vargas LR, Postal M, Oliveira-Neto OB, Rigden DJ, Grossi-de-Sá MF, Carlini CR. </i> Peptides, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","released":"2022_03","version":3,"region_id":"DP01763r011","statement":[{"text":"As shown in Fig. 4, the lethal effect of Jaburetox-2Ec was time dependent, with a lag phase of 3–4 days and 100% mortality being reached after 11 days. Mortality of canatoxin-fed insects showed a slower rate with 20% insects still alive at the end of the experiments.","type":"Results"},{"text":"A lag phase of 2 days was observed before lethality of the insects and on sixth day, after ingesting a total of 47 μg jaburetox-2Ec, all larvae were dead (Fig. 5B).","type":"Results"},{"text":"In this context it is noteworthy to mention that neurotoxic symptoms (such as paralysis and uncoordinated movements of limbs and antenna) are seen in R. prolixus intoxicated by Jaburetox-2Ec.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-07-13T13:35:29.374Z"},"term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_E6Y5X0","date":"2018-08-09T08:44:40.000Z","acc":"E6Y5X0","name":"Urease","length":840,"organism":"Canavalia ensiformis","dataset":[],"UniParc":"UPI0001F342F4","genes":[],"alphafold_very_low_content":0.0011904761904761906,"disorder_content":0.10714285714285714,"disprot_consensus":{"full":[{"start":232,"end":321,"type":"T"}],"Structural state":[{"start":232,"end":321,"type":"D"}],"Molecular function":[{"start":232,"end":321,"type":"F"}],"Structural transition":[{"start":232,"end":321,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00104","name":"Ligand-binding domain of nuclear hormone receptor","start":241,"end":415},{"id":"PF00105","name":"Double treble clef zinc finger, C4 type","start":102,"end":170}],"gene3D":[{"start":97,"end":194,"id":"3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A"},{"start":207,"end":433,"id":"1.10.565.10","name":"Retinoid X Receptor"}]},"uniref50":"UniRef50_O95718","sequence":"MSSDDRHLGSSCGSFIKTEPSSPSSGIDALSHHSPSGSSDASGGFGLALGTHANGLDSPPMFAGAGLGGTPCRKSYEDCASGIMEDSAIKCEYMLNAIPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYSCPATNECEITKRRRKSCQACRFMKCLKVGMLKEGVRLDRVRGGRQKYKRRLDSESSPYLSLQISPPAKKPLTKIVSYLLVAEPDKLYAMPPPGMPEGDIKALTTLCDLADRELVVIIGWAKHIPGFSSLSLGDQMSLLQSAWMEILILGIVYRSLPYDDKLVYAEDYIMDEEHSRLAGLLELYRAILQLVRRYKKLKVEKEEFVTLKALALANSDSMYIEDLEAVQKLQDLLHEALQDYELSQRHEEPWRTGKLLLTLPLLRQTAAKAVQHFYSVKLQGKVPMHKLFLEMLEAKV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O95718","disprot_id":"DP01764","ncbi_taxon_id":9606,"regions_counter":2,"creator":"okovacs","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":194,"region_id":"DP01764r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"NMR spectroscopic studies of the DNA-binding domain of the monomer-binding nuclear orphan receptor, human estrogen related receptor-2. The carboxyl-terminal extension to the zinc-finger region is unstructured in the free form of the protein. <i> Sem DS, Casimiro DR, Kliewer SA, Provencal J, Evans RM, Wright PE. </i> J Biol Chem, 1997","statement":[{"text":"Resonances for 15 of the 20 residues C-terminal of Arg-174 could not be assigned since sequential and medium-range NOEs are either weak or absent.","type":"Results"},{"text":"Furthermore, the analysis establishes that the CTE does not adopt a regular secondary structure, but has chemical shifts characteristic of a random coil. The absence of long-range NOEs and most sequential NOEs for residues C-terminal of Arg-174 also provides strong evidence that the CTE is unstructured.","type":"Results"},{"text":"The region after helix-2 shows no sign of secondary structure and may be disordered (see below).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":169,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"9218433","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-05-16T15:25:51.402Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907"}],"released":"2018_11","uniref100":"UniRef100_O95718","date":"2018-08-09T08:45:12.000Z","acc":"O95718","name":"Steroid hormone receptor ERR2","length":433,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI000012A17F","genes":[{"name":{"value":"ESRRB","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:3473","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:3473"}}]},"synonyms":[{"value":"ERRB2"},{"value":"ESRL2"},{"value":"NR3B2"}]}],"alphafold_very_low_content":0.2748267898383372,"disorder_content":0.06004618937644342,"disprot_consensus":{"full":[{"start":169,"end":194,"type":"D"}],"Structural state":[{"start":169,"end":194,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00023","name":"Ankyrin repeat","start":163,"end":193},{"id":"PF00520","name":"Ion transport protein","start":389,"end":588},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":49,"end":145}],"gene3D":[{"start":26,"end":103,"id":"1.25.40.20","name":"Ankyrin repeat-containing domain"},{"start":104,"end":309,"id":"1.25.40.20","name":"Ankyrin repeat-containing domain"}]},"uniref50":"UniRef50_Q9H1D0","sequence":"MGGFLPKAEGPGSQLQKLLPSFLVREQDWDQHLDKLHMLQQKRILESPLLRASKENDLSVLRQLLLDCTCDVRQRGALGETALHIAALYDNLEAALVLMEAAPELVFEPTTCEAFAGQTALHIAVVNQNVNLVRALLTRRASVSARATGTAFRHSPRNLIYFGEHPLSFAACVNSEEIVRLLIEHGADIRAQDSLGNTVLHILILQPNKTFACQMYNLLLSYDGHGDHLQPLDLVPNHQGLTPFKLAGVEGNTVMFQHLMQKRRHIQWTYGPLTSILYDLTEIDSWGEELSFLELVVSSDKREARQILEQTPVKELVSFKWNKYGRPYFCILAALYLLYMICFTTCCVYRPLKFRGGNRTHSRDITILQQKLLQEAYETREDIIRLVGELVSIVGAVIILLLEIPDIFRVGASRYFGKTILGGPFHVIIITYASLVLVTMVMRLTNTNGEVVPMSFALVLGWCSVMYFTRGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAFYIIFQTEDPTSLGQFYDYPMALFTTFELFLTVIDAPANYDVDLPFMFSIVNFAFTIIATLLMLNLFIAMMGDTHWRVAQERDELWRAQVVATTVMLERKLPRCLWPRSGICGCEFGLGDRWFLRVENHNDQNPLRVLRYVEVFKNSDKEDDQEHPSEKQPSGAESGTLARASLALPTSSLSRTASQSSSHRGWEILRQNTLGHLNLGLNLSEGDGEEVYHF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9NQA5","disprot_id":"DP01765","ncbi_taxon_id":9606,"regions_counter":3,"creator":"okovacs","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":725,"region_id":"DP01765r001","released":"2022_03","ec_id":"ECO:0007689","reference_html":"Expression and purification of the C-terminal fragments of TRPV5/6 channels. <i> Kovalevskaya NV, Schilderink N, Vuister GW. </i> Protein Expr Purif, 2011","statement":[{"text":"As often observed for intrinsically unstructured proteins, all expressed fragments migrated in the SDS gel slower than expected based on amino acid sequence, including V5c20.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":587,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"21664972","version":2,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":725,"region_id":"DP01765r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Expression and purification of the C-terminal fragments of TRPV5/6 channels. <i> Kovalevskaya NV, Schilderink N, Vuister GW. </i> Protein Expr Purif, 2011","statement":[{"text":"Spectra of V5c20 (residues 587-725) with and without GB1-tag display a characteristic dip around 200 nm for proteins classified as intrinsically disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":587,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"21664972","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":725,"term_name":"protein binding","start":587,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"Several auxiliary calcium-binding proteins, such as 80K-H protein, calbindin-D28K and calmodulin, were shown to bind in vivo to the C-terminus of TRPV5 and dramatically affect calcium reabsorption in kidney.","type":"Introduction"}],"curator_id":"okovacs","released":"2022_03","term_ontology":"GO","curator_name":"Orsolya Panna Kovacs","reference_id":"21664972","version":3,"reference_html":"Expression and purification of the C-terminal fragments of TRPV5/6 channels. <i> Kovalevskaya NV, Schilderink N, Vuister GW. </i> Protein Expr Purif, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP01765r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q9NQA5","date":"2018-08-09T09:20:32.000Z","acc":"Q9NQA5","name":"Transient receptor potential cation channel subfamily V member 5","length":729,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000052B72","genes":[{"name":{"value":"TRPV5"},"synonyms":[{"value":"ECAC1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10945469","url":"http://www.ncbi.nlm.nih.gov/pubmed/10945469","alternativeUrl":"https://europepmc.org/abstract/MED/10945469"}}]}]}],"alphafold_very_low_content":0.13443072702331962,"disorder_content":0.1906721536351166,"disprot_consensus":{"full":[{"start":587,"end":725,"type":"D"}],"Structural state":[{"start":587,"end":725,"type":"D"}],"Molecular function":[{"start":587,"end":725,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00023","name":"Ankyrin repeat","start":203,"end":233},{"id":"PF00520","name":"Ion transport protein","start":394,"end":627},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":89,"end":185}],"gene3D":[{"start":144,"end":349,"id":"1.25.40.20","name":"Ankyrin repeat-containing domain"},{"start":60,"end":143,"id":"1.25.40.20","name":"Ankyrin repeat-containing domain"}]},"uniref50":"UniRef50_Q9H1D0","sequence":"MGPLQGDGGPALGGADVAPRLSPVRVWPRPQAPKEPALHPMGLSLPKEKGLILCLWSKFCRWFQRRESWAQSRDEQNLLQQKRIWESPLLLAAKDNDVQALNKLLKYEDCKVHQRGAMGETALHIAALYDNLEAAMVLMEAAPELVFEPMTSELYEGQTALHIAVVNQNMNLVRALLARRASVSARATGTAFRRSPCNLIYFGEHPLSFAACVNSEEIVRLLIEHGADIRAQDSLGNTVLHILILQPNKTFACQMYNLLLSYDRHGDHLQPLDLVPNHQGLTPFKLAGVEGNTVMFQHLMQKRKHTQWTYGPLTSTLYDLTEIDSSGDEQSLLELIITTKKREARQILDQTPVKELVSLKWKRYGRPYFCMLGAIYLLYIICFTMCCIYRPLKPRTNNRTSPRDNTLLQQKLLQEAYMTPKDDIRLVGELVTVIGAIIILLVEVPDIFRMGVTRFFGQTILGGPFHVLIITYAFMVLVTMVMRLISASGEVVPMSFALVLGWCNVMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAFYIIFQTEDPEELGHFYDYPMALFSTFELFLTIIDGPANYNVDLPFMYSITYAAFAIIATLLMLNLLIAMMGDTHWRVAHERDELWRAQIVATTVMLERKLPRCLWPRSGICGREYGLGDRWFLRVEDRQDLNRQRIQRYAQAFHTRGSEDLDKDSVEKLELGCPFSPHLSLPMPSVSRSTSRSSANWERLRQGTLRRDLRGIINRGLEDGESWEYQI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9H1D0","disprot_id":"DP01767","ncbi_taxon_id":9606,"regions_counter":3,"creator":"okovacs","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":725,"region_id":"DP01767r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Expression and purification of the C-terminal fragments of TRPV5/6 channels. <i> Kovalevskaya NV, Schilderink N, Vuister GW. </i> Protein Expr Purif, 2011","statement":[{"text":"The remainder of the peaks belongs to TRPV6 and the linker region (thrombin cleavage site LVPRGS). Lower intensity or absence of the peaks may be indicative of flexibility of the protein. Dispersion of the chemical shifts is quite low as most of the peaks are located in the region of the spectrum characteristic for random coil and alpha-helical proteins (1H chemical shift 7.6–8.2).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":655,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"21664972","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":725,"term_name":"protein binding","start":655,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Upon addition of calmodulin to V6c7 at 1:1 molar ratio the followings changes were observed: approximately 20 new peaks appeared in the spectrum, several peaks became more intense and spectral dispersion generally increased.","type":"Results"}],"curator_id":"okovacs","released":"2022_03","term_ontology":"GO","curator_name":"Orsolya Panna Kovacs","reference_id":"21664972","version":3,"reference_html":"Expression and purification of the C-terminal fragments of TRPV5/6 channels. <i> Kovalevskaya NV, Schilderink N, Vuister GW. </i> Protein Expr Purif, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP01767r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":725,"region_id":"DP01767r003","released":"2022_03","ec_id":"ECO:0007689","reference_html":"Expression and purification of the C-terminal fragments of TRPV5/6 channels. <i> Kovalevskaya NV, Schilderink N, Vuister GW. </i> Protein Expr Purif, 2011","statement":[{"text":"As often observed for intrinsically unstructured proteins, all expressed fragments migrated in the SDS gel slower than expected based on amino acid sequence, including V6c7 (residues 655-725).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":655,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"21664972","version":2,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9H1D0","date":"2018-08-09T09:30:03.000Z","acc":"Q9H1D0","name":"Transient receptor potential cation channel subfamily V member 6","length":765,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000052C020","genes":[{"name":{"value":"TRPV6"},"synonyms":[{"value":"ECAC2"}]}],"alphafold_very_low_content":0.1568627450980392,"disorder_content":0.09281045751633987,"disprot_consensus":{"full":[{"start":655,"end":725,"type":"D"}],"Structural state":[{"start":655,"end":725,"type":"D"}],"Molecular function":[{"start":655,"end":725,"type":"F"}]}},{"features":{"pfam":[{"id":"PF13676","name":"TIR domain","start":88,"end":206}],"gene3D":[{"start":76,"end":221,"id":"3.40.50.10140","name":"Toll/interleukin-1 receptor homology (TIR) domain"}]},"uniref50":"UniRef50_P58753","sequence":"MASSTSLPAPGSRPKKPLGKMADWFRQTLLKKPKKRPNSPESTSSDASQPTSQDSPLPPSLSSVTSPSLPPTHASDSGSSRWSKDYDVCVCHSEEDLVAAQDLVSYLEGSTASLRCFLQLRDATPGGAIVSELCQALSSSHCRVLLITPGFLQDPWCKYQMLQALTEAPGAEGCTIPLLSGLSRAAYPPELRFMYYVDGRGPDGGFRQVKEAVMRYLQTLS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P58753","disprot_id":"DP01768","ncbi_taxon_id":9606,"regions_counter":3,"creator":"emaiani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":35,"region_id":"DP01768r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Membrane targeting of TIRAP is negatively regulated by phosphorylation in its phosphoinositide-binding motif. <i> Zhao X, Xiong W, Xiao S, Tang TX, Ellena JF, Armstrong GS, Finkielstein CV, Capelluto DG. </i> Sci Rep, 2017","statement":[{"text":"TIRAP PBM transitions from a disordered to a helical conformation in the presence of either zwitterionic micelles or monodispersed PIs.","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"emaiani","start":15,"term_ontology":"IDPO","curator_name":"Emiliano Maiani","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1432-5394","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28225045","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":35,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Membrane targeting of TIRAP is negatively regulated by phosphorylation in its phosphoinositide-binding motif. <i> Zhao X, Xiong W, Xiao S, Tang TX, Ellena JF, Armstrong GS, Finkielstein CV, Capelluto DG. </i> Sci Rep, 2017","term_id":"IDPO:0000011","curator_id":"emaiani","start":15,"term_ontology":"IDPO","curator_name":"Emiliano Maiani","reference_id":"28225045","version":2,"curator_orcid":"0000-0003-1432-5394","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01768r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":35,"region_id":"DP01768r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Membrane targeting of TIRAP is negatively regulated by phosphorylation in its phosphoinositide-binding motif. <i> Zhao X, Xiong W, Xiao S, Tang TX, Ellena JF, Armstrong GS, Finkielstein CV, Capelluto DG. </i> Sci Rep, 2017","term_id":"IDPO:0000002","curator_id":"emaiani","start":15,"term_ontology":"IDPO","curator_name":"Emiliano Maiani","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1432-5394","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28225045","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P58753","date":"2018-08-09T09:38:12.000Z","acc":"P58753","name":"Toll/interleukin-1 receptor domain-containing adapter protein","length":221,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000136FBA","genes":[{"name":{"value":"TIRAP"},"synonyms":[{"value":"MAL"}]}],"alphafold_very_low_content":0.3031674208144796,"disorder_content":0.09502262443438914,"disprot_consensus":{"full":[{"start":15,"end":35,"type":"T"}],"Structural state":[{"start":15,"end":35,"type":"D"}],"Structural transition":[{"start":15,"end":35,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00083","name":"Sugar (and other) transporter","start":217,"end":615}],"gene3D":[{"start":76,"end":506,"id":"1.20.1250.20","name":"MFS general substrate transporter like domains"}]},"uniref50":"UniRef50_Q8WUG5","sequence":"MAPRVATGTPEPNGGGGGKIDNTVEITPTSNGQVGTLGDAVPTEQLQGEREREREGEGDAGGDGLGSSLSLAVPPGPLSFEALLAQVGALGGGQQLQLGLCCLPVLFVALGMASDPIFTLAPPLHCHYGAFPPNASGWEQPPNASGVSVASAALAASAASRVATSTDPSCSGFAPPDFNHCLKDWDYNGLPVLTTNAIGQWDLVCDLGWQVILEQILFILGFASGYLFLGYPADRFGRRGIVLLTLGLVGPCGVGGAAAGSSTGVMALRFLLGFLLAGVDLGVYLMRLELCDPTQRLRVALAGELVGVGGHFLFLGLALVSKDWRFLQRMITAPCILFLFYGWPGLFLESARWLIVKRQIEEAQSVLRILAERNRPHGQMLGEEAQEALQDLENTCPLPATSSFSFASLLNYRNIWKNLLILGFTNFIAHAIRHCYQPVGGGGSPSDFYLCSLLASGTAALACVFLGVTVDRFGRRGILLLSMTLTGIASLVLLGLWDCEHPIFPTVWAQQGNPNRDLNEAAITTFSVLGLFSSQAAAILSTLLAAEVIPTTVRGRGLGLIMALGALGGLSGPAQRLHMGHGAFLQHVVLAACALLCILSIMLLPETKRKLLPEVLRDGELCRRPSLLRQPPPTRCDHVPLLATPNPAL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q8WUG5","disprot_id":"DP01769","ncbi_taxon_id":9606,"regions_counter":4,"creator":"okovacs","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":216,"region_id":"DP01769r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Biochemical and Structural Characterization of the Interaction between the Siderocalin NGAL/LCN2 (Neutrophil Gelatinase-associated Lipocalin/Lipocalin 2) and the N-terminal Domain of Its Endocytic Receptor SLC22A17. <i> Cabedo Martinez AI, Weinhäupl K, Lee WK, Wolff NA, Storch B, Żerko S, Konrat R, Koźmiński W, Breuker K, Thévenod F, Coudevylle N. </i> J Biol Chem, 2016","statement":[{"text":"The 1H,15N HSQC spectrum of hLCN2-R-NTD exhibits the distinctive narrow 1HN dispersion of IDPs. Surprisingly, the spectrum also exhibits unusually broad resonances for an IDP, which would indicate that hLCN2-R-NTD, although devoid of any stable secondary or tertiary structures, experiences significant conformational exchange on the micro-to-millisecond timescale.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":112,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"26635366","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":216,"term_name":"protein binding","start":112,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"When performing a 1H,15N HSQC-based titration of 15N-labeled hLCN2-R-NTD with unlabeled NGAL many resonances disappear upon the addition of unlabeled NGAL whereas only very limited chemical shift changes can be observed. This type of signal decrease is often observed in complexes involving one or more disordered partners, hampering the direct characterization of the bound state.","type":"Results"}],"curator_id":"okovacs","released":"2022_03","term_ontology":"GO","curator_name":"Orsolya Panna Kovacs","reference_id":"26635366","version":3,"reference_html":"Biochemical and Structural Characterization of the Interaction between the Siderocalin NGAL/LCN2 (Neutrophil Gelatinase-associated Lipocalin/Lipocalin 2) and the N-terminal Domain of Its Endocytic Receptor SLC22A17. <i> Cabedo Martinez AI, Weinhäupl K, Lee WK, Wolff NA, Storch B, Żerko S, Konrat R, Koźmiński W, Breuker K, Thévenod F, Coudevylle N. </i> J Biol Chem, 2016","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP01769r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":216,"region_id":"DP01769r003","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Biochemical and Structural Characterization of the Interaction between the Siderocalin NGAL/LCN2 (Neutrophil Gelatinase-associated Lipocalin/Lipocalin 2) and the N-terminal Domain of Its Endocytic Receptor SLC22A17. <i> Cabedo Martinez AI, Weinhäupl K, Lee WK, Wolff NA, Storch B, Żerko S, Konrat R, Koźmiński W, Breuker K, Thévenod F, Coudevylle N. </i> J Biol Chem, 2016","statement":[{"text":"After refolding, the protein is pure, soluble, and appears on the size exclusion chromatography profile to have an hydrodynamic radius consistent with a monomeric intrinsically disordered protein (IDP) of this molecular weight.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":112,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"26635366","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":216,"term_name":"protein binding","start":112,"ec_name":"chromatography evidence used in manual assertion","statement":[{"text":"To determine whether hLCN2-R-NTD can interact with NGAL, we first used ITC. hLCN2-R-NTD binds to NGAL with an affinity (KD) of 10 μm and a stoichiometry of 1 to 1. Noteworthy, after being loaded with ferric-enterobactin, NGAL is no longer able to interact with hLCN2-R-NTD, suggesting that enterobactin and hLCN2-R-NTD bind to the same site on NGAL.","type":"Results"}],"curator_id":"okovacs","released":"2022_03","term_ontology":"GO","curator_name":"Orsolya Panna Kovacs","reference_id":"26635366","version":3,"reference_html":"Biochemical and Structural Characterization of the Interaction between the Siderocalin NGAL/LCN2 (Neutrophil Gelatinase-associated Lipocalin/Lipocalin 2) and the N-terminal Domain of Its Endocytic Receptor SLC22A17. <i> Cabedo Martinez AI, Weinhäupl K, Lee WK, Wolff NA, Storch B, Żerko S, Konrat R, Koźmiński W, Breuker K, Thévenod F, Coudevylle N. </i> J Biol Chem, 2016","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0007680","region_id":"DP01769r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q8WUG5","date":"2018-08-09T09:50:17.000Z","acc":"Q8WUG5","name":"Solute carrier family 22 member 17","length":649,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000126A49","genes":[{"name":{"value":"SLC22A17"},"synonyms":[{"value":"BOCT"},{"value":"BOIT"}]}],"alphafold_very_low_content":0.17100371747211895,"disorder_content":0.1617873651771957,"disprot_consensus":{"full":[{"start":112,"end":216,"type":"D"}],"Structural state":[{"start":112,"end":216,"type":"D"}],"Molecular function":[{"start":112,"end":216,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03020","name":"LEM domain","start":3,"end":47}],"gene3D":[{"start":2,"end":54,"id":"1.10.720.40","name":"1.10.720.40"}]},"uniref50":"UniRef50_P50402","sequence":"MDNYADLSDTELTTLLRRYNIPHGPVVGSTRRLYEKKIFEYETQRRRLSPPSSSAASSYSFSDLNSTRGDADMYDLPKKEDALLYQSKGYNDDYYEESYFTTRTYGEPESAGPSRAVRQSVTSFPDADAFHHQVHDDDLLSSSEEECKDRERPMYGRDSAYQSITHYRPVSASRSSLDLSYYPTSSSTSFMSSSSSSSSWLTRRAIRPENRAPGAGLGQDRQVPLWGQLLLFLVFVIVLFFIYHFMQAEEGNPF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P50402","disprot_id":"DP01770","ncbi_taxon_id":9606,"regions_counter":4,"creator":"emaiani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":187,"region_id":"DP01770r001","released":"2024_06","ec_id":"ECO:0006165","reference_html":"Muscular Dystrophy Mutations Impair the Nuclear Envelope Emerin Self-assembly Properties. <i> Herrada I, Samson C, Velours C, Renault L, Östlund C, Chervy P, Puchkov D, Worman HJ, Buendia B, Zinn-Justin S. </i> ACS Chem Biol, 2015","term_id":"IDPO:0000002","curator_id":"vnugnes","start":46,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-19T16:34:53.922Z","reference_source":"pmid","term_name":"disorder","reference_id":"26415001","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Analysis of the NMR 1H–15N HSQC spectrum of refolded EmN showed that this emerin fragment is only partially structured. Indeed, about 50 HSQC signals show a nonrandom coil 1H chemical shift and/or correspond to positive 1H → 15N NOE values (Figure 1D). Most of these signals can be assigned to the emerin LEM domain based on previous 1H chemical shift assignments (BMRB entry 5074). The remaining HSQC signals have a 1H chemical shift comprised between 7.8 and 8.4 ppm (Figure 1D).","type":"Results"},{"text":"The authors refers as LEM domain to the 1-45 region.","type":"Curator statement"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":170,"region_id":"DP01770r002","released":"2024_06","ec_id":"ECO:0006165","reference_html":"1H, 13C and 15N backbone resonance assignment of the intrinsically disordered region of the nuclear envelope protein emerin. <i> Samson C, Herrada I, Celli F, Theillet FX, Zinn-Justin S. </i> Biomol NMR Assign, 2016","term_id":"IDPO:0000002","curator_id":"vnugnes","start":67,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-19T16:28:30.289Z","reference_source":"pmid","term_name":"disorder","reference_id":"26725056","statement":[{"text":"Here we report 1H, 15N, 13CO, 13Cα and 13Cβ NMR chemical shift assignments of the emerin fragment from residue 67 to residue 170, which is sufficient for nuclear localization and involved in lamin A binding. Chemical shift analysis confirms that this fragment is intrinsically disordered in 0 and 8 M urea.","type":"Abstract"},{"text":"The limited chemical shift dispersion of the 1H–15N HSQC signals, particularly in the 1H dimension (between 7.6 and 8.7 ppm), indicates that the emerin fragment is not folded in the NMR experimental conditions (20 mM phosphate, 30 mM NaCl, pH 6.5).","type":"Article"}],"ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"BMRB","id":"26654"}]},{"start":95,"end":99,"reference_id":"26415001","reference_source":"pmid","reference_html":"Muscular Dystrophy Mutations Impair the Nuclear Envelope Emerin Self-assembly Properties. <i> Herrada I, Samson C, Velours C, Renault L, Östlund C, Chervy P, Puchkov D, Worman HJ, Buendia B, Zinn-Justin S. </i> ACS Chem Biol, 2015","date":"2024-02-19T16:46:55.464Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001237","ec_ontology":"ECO","ec_name":"natural variation mutant evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Tyr95Tyr99del","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Mutations encoding emerin variants S54F, Q133H, Δ95–99, P183H, and P183T were inserted in the EmN cDNA using a standard QuikChange Site-Directed Mutagenesis kit (Stratagene)."}]}],"ec_go":"EXP","region_id":"DP01770r003","statement":[{"text":"EmN Variants del95–99 and Q133H Occurring in EDMD Are Impaired in Their Capacity to Self-assemble","type":"Results"},{"text":"Observation by negative staining EM of the different variants after incubation at a concentration higher than 300 µM and a temperature of 65 °C for 1 h confirmed that, if del95–99 was unable to form filaments under these conditions (data not shown), Q133H and P183T self-assembled into filaments (Figure 6). Filaments obtained from variant P183T were indistinguishable from wild-type filaments, whereas filaments formed by Q133H at a similar time point were systematically shorter and less regular.","type":"Results"},{"text":"Altogether, these experiments suggest that P183H has the strongest capacity to self-assemble or aggregate, whereas Q133H and then del95–99 have the lowest capacities to form filament-like structures.","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false},{"start":131,"end":135,"reference_id":"26415001","reference_source":"pmid","reference_html":"Muscular Dystrophy Mutations Impair the Nuclear Envelope Emerin Self-assembly Properties. <i> Herrada I, Samson C, Velours C, Renault L, Östlund C, Chervy P, Puchkov D, Worman HJ, Buendia B, Zinn-Justin S. </i> ACS Chem Biol, 2015","date":"2024-02-19T16:47:31.067Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001237","ec_ontology":"ECO","ec_name":"natural variation mutant evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gln133His","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Mutations encoding emerin variants S54F, Q133H, Δ95–99, P183H, and P183T were inserted in the EmN cDNA using a standard QuikChange Site-Directed Mutagenesis kit (Stratagene)."}]}],"ec_go":"EXP","region_id":"DP01770r004","statement":[{"text":"EmN Variants del95–99 and Q133H Occurring in EDMD Are Impaired in Their Capacity to Self-assemble","type":"Results"},{"text":"Observation by negative staining EM of the different variants after incubation at a concentration higher than 300 µM and a temperature of 65 °C for 1 h confirmed that, if del95–99 was unable to form filaments under these conditions (data not shown), Q133H and P183T self-assembled into filaments (Figure 6). Filaments obtained from variant P183T were indistinguishable from wild-type filaments, whereas filaments formed by Q133H at a similar time point were systematically shorter and less regular.","type":"Results"},{"text":"Altogether, these experiments suggest that P183H has the strongest capacity to self-assemble or aggregate, whereas Q133H and then del95–99 have the lowest capacities to form filament-like structures.","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_P50402","date":"2018-08-09T09:52:01.000Z","acc":"P50402","name":"Emerin","length":254,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000129EA0","genes":[{"name":{"value":"EMD"},"synonyms":[{"value":"EDMD"},{"value":"STA"}]}],"alphafold_very_low_content":0.4763779527559055,"disorder_content":0.5590551181102362,"disprot_consensus":{"full":[{"start":46,"end":187,"type":"D"}],"Structural state":[{"start":46,"end":187,"type":"D"}],"Biological process":[{"start":95,"end":99,"type":"F"},{"start":131,"end":135,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00531","name":"Death domain","start":118,"end":188},{"id":"PF00619","name":"Caspase recruitment domain","start":7,"end":82}],"gene3D":[{"start":98,"end":199,"id":"1.10.533.10","name":"Death Domain, Fas"},{"start":1,"end":97,"id":"1.10.533.10","name":"Death Domain, Fas"}]},"uniref50":"UniRef50_P78560","sequence":"MEARDKQVLRSLRLELGAEVLVEGLVLQYLYQEGILTENHIQEINAQTTGLRKTMLLLDILPSRGPKAFDTFLDSLQEFPWVREKLKKAREEAMTDLPAGDRLTGIPSHILNSSPSDRQINQLAQRLGPEWEPMVLSLGLSQTDIYRCKANHPHNVQSQVVEAFIRWRQRFGKQATFQSLHNGLRAVEVDPSLLLHMLE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P78560","disprot_id":"DP01771","ncbi_taxon_id":9606,"regions_counter":1,"creator":"bhajdu","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":136,"region_id":"DP01771r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment. <i> Chou JJ, Matsuo H, Duan H, Wagner G. </i> Cell, 1998","statement":[{"text":" The terminal residues 1–3 and 95–136 could not be assigned at all, as they appear unstructured and their amide protons exchange rapidly with the solvent.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":95,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-15T17:11:47.676Z","reference_source":"pmid","term_name":"disorder","reference_id":"9695946","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P78560","date":"2018-08-09T09:59:12.000Z","acc":"P78560","name":"Death domain-containing protein CRADD","length":199,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI00001283AA","genes":[{"name":{"value":"CRADD"},"synonyms":[{"value":"RAIDD"}]}],"alphafold_very_low_content":0.04020100502512563,"disorder_content":0.21105527638190955,"disprot_consensus":{"full":[{"start":95,"end":136,"type":"D"}],"Structural state":[{"start":95,"end":136,"type":"D"}]}},{"features":{"pfam":[{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":127,"end":384},{"id":"PF09027","name":"GTPase binding","start":450,"end":513},{"id":"PF11555","name":"EGFR receptor inhibitor Mig-6","start":775,"end":837},{"id":"PF14604","name":"Variant SH3 domain","start":395,"end":444},{"id":"PF22931","name":"SAM domain-like","start":10,"end":65}],"gene3D":[{"start":450,"end":489,"id":"4.10.680.10","name":"Cdc42-like binding domain"},{"start":114,"end":207,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":963,"end":994,"id":"1.10.8.10","name":"DNA helicase RuvA subunit, C-terminal domain"},{"start":208,"end":449,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"}]},"uniref50":"UniRef50_Q07912","sequence":"MQPEEGTGWLLELLSEVQLQQYFLRLRDDLNVTRLSHFEYVKNEDLEKIGMGRPGQRRLWEAVKRRKALCKRKSWMSKVFSGKRLEAEFPPHHSQSTFRKTSPAPGGPAGEGPLQSLTCLIGEKDLRLLEKLGDGSFGVVRRGEWDAPSGKTVSVAVKCLKPDVLSQPEAMDDFIREVNAMHSLDHRNLIRLYGVVLTPPMKMVTELAPLGSLLDRLRKHQGHFLLGTLSRYAVQVAEGMGYLESKRFIHRDLAARNLLLATRDLVKIGDFGLMRALPQNDDHYVMQEHRKVPFAWCAPESLKTRTFSHASDTWMFGVTLWEMFTYGQEPWIGLNGSQILHKIDKEGERLPRPEDCPQDIYNVMVQCWAHKPEDRPTFVALRDFLLEAQPTDMRALQDFEEPDKLHIQMNDVITVIEGRAENYWWRGQNTRTLCVGPFPRNVVTSVAGLSAQDISQPLQNSFIHTGHGDSDPRHCWGFPDRIDELYLGNPMDPPDLLSVELSTSRPPQHLGGVKKPTYDPVSEDQDPLSSDFKRLGLRKPGLPRGLWLAKPSARVPGTKASRGSGAEVTLIDFGEEPVVPALRPCAPSLAQLAMDACSLLDETPPQSPTRALPRPLHPTPVVDWDARPLPPPPAYDDVAQDEDDFEICSINSTLVGAGVPAGPSQGQTNYAFVPEQARPPPPLEDNLFLPPQGGGKPPSSAQTAEIFQALQQECMRQLQAPAGSPAPSPSPGGDDKPQVPPRVPIPPRPTRPHVQLSPAPPGEEETSQWPGPASPPRVPPREPLSPQGSRTPSPLVPPGSSPLPPRLSSSPGKTMPTTQSFASDPKYATPQVIQAPGPRAGPCILPIVRDGKKVSSTHYYLLPERPSYLERYQRFLREAQSPEEPTPLPVPLLLPPPSTPAPAAPTATVRPMPQAALDPKANFSTNNSNPGARPPPPRATARLPQRGCPGDGPEAGRPADKIQMAMVHGVTTEECQAALQCHGWSVQRAAQYLKVEQLFGLGLRPRGECHKVLEMFDWNLEQAGCHLLGSWGPAHHKR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q07912","disprot_id":"DP01772","ncbi_taxon_id":9606,"regions_counter":1,"creator":"emaiani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":489,"region_id":"DP01772r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of Cdc42 bound to the GTPase binding domain of PAK. <i> Morreale A, Venkatesan M, Mott HR, Owen D, Nietlispach D, Lowe PN, Laue ED. </i> Nat Struct Biol, 2000","term_id":"IDPO:0000002","curator_id":"emaiani","start":448,"term_ontology":"IDPO","curator_name":"Emiliano Maiani","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1432-5394","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"10802735","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q07912","date":"2018-08-09T10:07:18.000Z","acc":"Q07912","name":"Activated CDC42 kinase 1","length":1038,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000017A3C1","genes":[{"name":{"value":"TNK2"},"synonyms":[{"value":"ACK1"}]}],"alphafold_very_low_content":0.46917148362235067,"disorder_content":0.04046242774566474,"disprot_consensus":{"full":[{"start":448,"end":489,"type":"D"}],"Structural state":[{"start":448,"end":489,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00653","name":"Inhibitor of Apoptosis domain","start":29,"end":93},{"id":"PF00653","name":"Inhibitor of Apoptosis domain","start":166,"end":230},{"id":"PF00653","name":"Inhibitor of Apoptosis domain","start":268,"end":330},{"id":"PF13920","name":"Zinc finger, C3HC4 type (RING finger)","start":446,"end":489},{"id":"PF21290","name":"BIRC2/3-like, UBA domain","start":371,"end":418}],"gene3D":[{"start":425,"end":497,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":22,"end":99,"id":"1.10.1170.10","name":"Inhibitor Of Apoptosis Protein (2mihbC-IAP-1); Chain A"},{"start":121,"end":240,"id":"1.10.1170.10","name":"Inhibitor Of Apoptosis Protein (2mihbC-IAP-1); Chain A"},{"start":367,"end":420,"id":"1.10.8.10","name":"DNA helicase RuvA subunit, C-terminal domain"},{"start":245,"end":354,"id":"1.10.1170.10","name":"Inhibitor Of Apoptosis Protein (2mihbC-IAP-1); Chain A"}]},"uniref50":"UniRef50_P98170","sequence":"MTFNSFEGSKTCVPADINKEEEFVEEFNRLKTFANFPSGSPVSASTLARAGFLYTGEGDTVRCFSCHAAVDRWQYGDSAVGRHRKVSPNCRFINGFYLENSATQSTNSGIQNGQYKVENYLGSRDHFALDRPSETHADYLLRTGQVVDISDTIYPRNPAMYSEEARLKSFQNWPDYAHLTPRELASAGLYYTGIGDQVQCFCCGGKLKNWEPCDRAWSEHRRHFPNCFFVLGRNLNIRSESDAVSSDRNFPNSTNLPRNPSMADYEARIFTFGTWIYSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKPSEDPWEQHAKWYPGCKYLLEQKGQEYINNIHLTHSLEECLVRTTEKTPSLTRRIDDTIFQNPMVQEAIRMGFSFKDIKKIMEEKIQISGSNYKSLEVLVADLVNAQKDSMQDESSQTSLQKEISTEEQLRRLQEEKLCKICMDRNIAIVFVPCGHLVTCKQCAEAVDKCPMCYTVITFKQKIFMS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P98170","disprot_id":"DP01773","ncbi_taxon_id":9606,"regions_counter":2,"creator":"bhajdu","regions":[{"region_id":"DP01773r001","ec_ontology":"ECO","end":254,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":241,"version":3,"statement":[{"text":"The N terminus (residues 241–254) and C terminus (residues 345–356) corresponding to the amino acids outside of the Bir3 domain are disordered.","type":"Results"}],"term_name":"disorder","reference_html":"NMR structure and mutagenesis of the third Bir domain of the inhibitor of apoptosis protein XIAP. <i> Sun C, Cai M, Meadows RP, Xu N, Gunasekera AH, Herrmann J, Wu JC, Fesik SW. </i> J Biol Chem, 2000","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10934209","date":"2023-09-27T17:30:59.353Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1F9X"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"GSHMSDAVSSDRNFPNSTNLPRNPSMADYEARIFTFGTWIYSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKPSEDPWEQHAKWYPGCKYLLEQKGQEYINNIHLTHSLEECLVRTT"},{"region_id":"DP01773r002","ec_ontology":"ECO","end":356,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":345,"version":3,"statement":[{"text":"The N terminus (residues 241–254) and C terminus (residues 345–356) corresponding to the amino acids outside of the Bir3 domain are disordered.","type":"Results"}],"term_name":"disorder","reference_html":"NMR structure and mutagenesis of the third Bir domain of the inhibitor of apoptosis protein XIAP. <i> Sun C, Cai M, Meadows RP, Xu N, Gunasekera AH, Herrmann J, Wu JC, Fesik SW. </i> J Biol Chem, 2000","released":"2023_12","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10934209","date":"2023-09-27T17:31:07.527Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1F9X"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"GSHMSDAVSSDRNFPNSTNLPRNPSMADYEARIFTFGTWIYSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKPSEDPWEQHAKWYPGCKYLLEQKGQEYINNIHLTHSLEECLVRTT"}],"released":"2018_11","uniref100":"UniRef100_P98170","date":"2018-08-09T10:10:29.000Z","acc":"P98170","name":"E3 ubiquitin-protein ligase XIAP","length":497,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000004A35A","genes":[{"name":{"value":"XIAP"},"synonyms":[{"value":"API3"},{"value":"BIRC4"},{"value":"IAP3"}]}],"alphafold_very_low_content":0.21327967806841047,"disorder_content":0.052313883299798795,"disprot_consensus":{"full":[{"start":241,"end":254,"type":"D"},{"start":345,"end":356,"type":"D"}],"Structural state":[{"start":241,"end":254,"type":"D"},{"start":345,"end":356,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00017","name":"SH2 domain","start":382,"end":436},{"id":"PF07525","name":"SOCS box","start":480,"end":515},{"id":"PF12610","name":"Suppressor of cytokine signalling","start":147,"end":195}],"gene3D":[{"start":362,"end":532,"id":"3.30.505.10","name":"SH2 domain"}]},"uniref50":"UniRef50_O54928","sequence":"MDKVGKMWNNLKYRCQNLFSHEGGSRNENVEMNPNRCPSVKEKSISLGEAAPQQESSPLRENVALQLGLSPSKTFSRRNQNCAAEIPQVVEISIEKDSDSGATPGTRLARRDSYSRHAPWGGKKKHSCSTKTQSSLDTEKKFGRTRSGLQRRERRYGVSSMQDMDSVSSRAVGSRSLRQRLQDTVGLCFPMRTYSKQSKPLFSNKRKIHLSELMLEKCPFPAGSDLAQKWHLIKQHTAPVSPHSTFFDTFDPSLVSTEDEEDRLRERRRLSIEEGVDPPPNAQIHTFEATAQVNPLYKLGPKLAPGMTEISGDGSAIPQTNCDSEEDSTTLCLQSRRQKQRQVSGDSHAHVSRQGAWKVHTQIDYIHCLVPDLLQITGNPCYWGVMDRYEAEALLEGKPEGTFLLRDSAQEDYLFSVSFRRYNRSLHARIEQWNHNFSFDAHDPCVFHSSTVTGLLEHYKDPSSCMFFEPLLTISLNRTFPFSLQYICRAVICRCTTYDGIDGLPLPSMLQDFLKEYHYKQKVRVRWLEREPVKAK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_O54928","disprot_id":"DP01774","ncbi_taxon_id":10090,"regions_counter":3,"creator":"okovacs","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":244,"region_id":"DP01774r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure and Functional Characterization of the Conserved JAK Interaction Region in the Intrinsically Disordered N-Terminus of SOCS5. <i> Chandrashekaran IR, Mohanty B, Linossi EM, Dagley LF, Leung EW, Murphy JM, Babon JJ, Nicholson SE, Norton RS. </i> Biochemistry, 2015","statement":[{"text":"The 1H-15N HSQC spectrum of mSOCS5 175-244 is characteristic of a largely disordered protein, with the amide proton shifts confined to 6.9–8.9 ppm. While IDPs usually have uniformly sharp resonances, these spectra displayed a diversity of peak intensities and peak shapes, indicating conformational heterogeneity. Residues Asp225–Ile233 are helical, while the N-terminal region shows random coil Cα chemical shifts.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":175,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"26173083","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":244,"term_name":"protein binding","start":175,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"The conserved N-terminal region in SOCS5 (SOCS5175-244) facilitates a direct interaction with the kinase domain of JAK and has therefore been designated the JAK interaction region (JIR).The KD for the interaction of SOCS5 JIR with the kinase domain of JAK1 was found to be 0.5 μM.","type":"Introduction"}],"curator_id":"okovacs","released":"2022_03","term_ontology":"GO","curator_name":"Orsolya Panna Kovacs","reference_id":"26173083","version":3,"reference_html":"Structure and Functional Characterization of the Conserved JAK Interaction Region in the Intrinsically Disordered N-Terminus of SOCS5. <i> Chandrashekaran IR, Mohanty B, Linossi EM, Dagley LF, Leung EW, Murphy JM, Babon JJ, Nicholson SE, Norton RS. </i> Biochemistry, 2015","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP01774r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":244,"term_name":"phosphorylation display site","start":175,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Using mass spectrometry, we identified Ser211 within the JAK interaction region (JIR) of SOCS5, as a candidate phosphorylation site. A high confidence peptide corresponding to phosphorylated Ser211 was identified with a MaxQuant score of 143.25.","type":"Results"}],"curator_id":"okovacs","released":"2022_03","term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"26173083","version":2,"reference_html":"Structure and Functional Characterization of the Conserved JAK Interaction Region in the Intrinsically Disordered N-Terminus of SOCS5. <i> Chandrashekaran IR, Mohanty B, Linossi EM, Dagley LF, Leung EW, Murphy JM, Babon JJ, Nicholson SE, Norton RS. </i> Biochemistry, 2015","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000045","ec_id":"ECO:0006165","region_id":"DP01774r003","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_O54928","date":"2018-08-09T10:17:30.000Z","acc":"O54928","name":"Suppressor of cytokine signaling 5","length":536,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000028347","genes":[{"name":{"value":"Socs5"},"synonyms":[{"value":"Cish5"}]}],"alphafold_very_low_content":0.47947761194029853,"disorder_content":0.13059701492537312,"disprot_consensus":{"full":[{"start":175,"end":244,"type":"D"}],"Structural state":[{"start":175,"end":244,"type":"D"}],"Molecular function":[{"start":175,"end":244,"type":"F"}],"Disorder function":[{"start":175,"end":244,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03828","name":"Cid1 family poly A polymerase","start":371,"end":431},{"id":"PF22600","name":"Poly(A) RNA polymerase, mitochondrial-like, central palm domain","start":181,"end":311}],"gene3D":[{"start":163,"end":456,"id":"1.10.1410.10","name":"1.10.1410.10"},{"start":194,"end":303,"id":"3.30.460.10","name":"Beta Polymerase, domain 2"}]},"uniref50":"UniRef50_P53632","sequence":"MGAKSVTASSSKKIKNRHNGKVKKSKKIKKVRKPQKSISLNDENEVEILPSRNEQETNKLPKDHVTADGILVLEHKSDDDEGFDVYDGHFDNPTDIPSTTEESKTPSLAVHGDEKDLANNDDFISLSASSEDEQAEQEEEREKQELEIKKEKQKEILNTDYPWILNHDHSKQKEISDWLTFEIKDFVAYISPSREEIEIRNQTISTIREAVKQLWPDADLHVFGSYSTDLYLPGSDIDCVVTSELGGKESRNNLYSLASHLKKKNLATEVEVVAKARVPIIKFVEPHSGIHIDVSFERTNGIEAAKLIREWLDDTPGLRELVLIVKQFLHARRLNNVHTGGLGGFSIICLVFSFLHMHPRIITNEIDPKDNLGVLLIEFFELYGKNFGYDDVALGSSDGYPVYFPKSTWSAIQPIKNPFSLAIQDPGDESNNISRGSFNIRDIKKAFAGAFDLLTNRCFELHSATFKDRLGKSILGNVIKYRGKARDFKDERGLVLNKAIIENENYHKKRSRIIHDEDFAEDTVTSTATATTTDDDYEITNPPAKKAKIEEKPESEPAKRNSGETYITVSSEDDDEDGYNPYTL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P53632","disprot_id":"DP01775","ncbi_taxon_id":559292,"regions_counter":6,"creator":"smribeiro","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":160,"region_id":"DP01775r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The molecular architecture of the TRAMP complex reveals the organization and interplay of its two catalytic activities. <i> Falk S, Weir JR, Hentschel J, Reichelt P, Bonneau F, Conti E. </i> Mol Cell, 2014","statement":[{"text":"Missing electron density","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"smribeiro","start":128,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4U4C"}],"reference_id":"25175027","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":160,"region_id":"DP01775r002","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Structure and function of the polymerase core of TRAMP, a RNA surveillance complex. <i> Hamill S, Wolin SL, Reinisch KM. </i> Proc Natl Acad Sci U S A, 2010","statement":[{"text":"Due to significant sample degradation during purification (Fig. S1), we were not able to isolate a complex consisting of full-length forms of Trf4p and Air2p. We therefore worked with Trf4p/Air2p subcomplexes, where the proteolytically sensitive N and C termini of both proteins were removed.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"smribeiro","start":1,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20696927","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Biological process","ec_ontology":"ECO","end":160,"term_name":"localization","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","reference_html":"Structure and function of the polymerase core of TRAMP, a RNA surveillance complex. <i> Hamill S, Wolin SL, Reinisch KM. </i> Proc Natl Acad Sci U S A, 2010","statement":[{"text":"Colocalization by tethering for increasing the local effective concentrations of Trf4 and Air2, promoting   synergistic binding to Mtr4 (ref. PubMedID: 25175027).","type":"Curator statement"}],"term_id":"GO:0051179","curator_id":"smribeiro","start":1,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"20696927","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","region_id":"DP01775r003","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":160,"term_name":"protein binding","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","reference_html":"Structure and function of the polymerase core of TRAMP, a RNA surveillance complex. <i> Hamill S, Wolin SL, Reinisch KM. </i> Proc Natl Acad Sci U S A, 2010","statement":[{"text":"Residues 121–127 interact with Mtr4 DExH-helicase core (ref. PubMed ID: 25175027)","type":"Curator statement"}],"term_id":"GO:0005515","curator_id":"smribeiro","start":1,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"20696927","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","cross_refs":[{"db":"imex ","id":" IM-15808-1"}],"region_id":"DP01775r004","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":584,"region_id":"DP01775r005","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Structure and function of the polymerase core of TRAMP, a RNA surveillance complex. <i> Hamill S, Wolin SL, Reinisch KM. </i> Proc Natl Acad Sci U S A, 2010","statement":[{"text":"Due to significant sample degradation during purification (Fig. S1), we were not able to isolate a complex consisting of full-length forms of Trf4p and Air2p. We therefore worked with Trf4p/Air2p subcomplexes, where the proteolytically sensitive N and C termini of both proteins were removed.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"smribeiro","start":482,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20696927","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":584,"term_name":"protein binding","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","reference_html":"Structure and function of the polymerase core of TRAMP, a RNA surveillance complex. <i> Hamill S, Wolin SL, Reinisch KM. </i> Proc Natl Acad Sci U S A, 2010","statement":[{"text":"Residues 573-584 bind to NDR1 (ref. PubMedID: 25066235).","type":"Curator statement"}],"term_id":"GO:0005515","curator_id":"smribeiro","start":482,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"20696927","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","cross_refs":[{"db":"imex ","id":" IM-26196-1"}],"region_id":"DP01775r006","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P53632","date":"2018-08-09T10:19:12.000Z","acc":"P53632","name":"Poly(A) RNA polymerase protein 2","length":584,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000005309C","genes":[{"name":{"value":"PAP2"},"synonyms":[{"value":"TRF4"}],"orfNames":[{"value":"HRC584"},{"value":"O0716"}],"olnNames":[{"value":"YOL115W"}]}],"alphafold_very_low_content":0.3236301369863014,"disorder_content":0.4503424657534247,"disprot_consensus":{"full":[{"start":1,"end":160,"type":"D"},{"start":482,"end":584,"type":"D"}],"Structural state":[{"start":1,"end":160,"type":"D"},{"start":482,"end":584,"type":"D"}],"Biological process":[{"start":1,"end":160,"type":"F"}],"Molecular function":[{"start":1,"end":160,"type":"F"},{"start":482,"end":584,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05627","name":"Cleavage site for pathogenic type III effector avirulence factor Avr","start":3,"end":31},{"id":"PF05627","name":"Cleavage site for pathogenic type III effector avirulence factor Avr","start":145,"end":176}]},"uniref50":"UniRef50_Q8GYN5","sequence":"MARSNVPKFGNWEAEENVPYTAYFDKARKTRAPGSKIMNPNDPEYNSDSQSQAPPHPPSSRTKPEQVDTVRRSREHMRSREESELKQFGDAGGSSNEAANKRQGRASQNNSYDNKSPLHKNSYDGTGKSRPKPTNLRADESPEKVTVVPKFGDWDENNPSSADGYTHIFNKVREERSSGANVSGSSRTPTHQSSRNPNNTSSCCCFGFGGK","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q8GYN5","disprot_id":"DP01776","ncbi_taxon_id":3702,"regions_counter":3,"creator":"okovacs","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":211,"region_id":"DP01776r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Phosphorylation of the Plant Immune Regulator RPM1-INTERACTING PROTEIN4 Enhances Plant Plasma Membrane H⁺-ATPase Activity and Inhibits Flagellin-Triggered Immune Responses in Arabidopsis. <i> Lee D, Bourdais G, Yu G, Robatzek S, Coaker G. </i> Plant Cell, 2015","statement":[{"text":"Consistent with the in silico prediction, full-length RIN4 circular dichroism spectra displayed a characteristic shape, including low ellipticity at 190 nm and strong negative ellipticity at 200 nm, consistent with an intrinsically disordered protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":1,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"26198070","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":211,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"RIN4 is a key accessory protein that associates with the plasma membrane localized NLRs, RPM1, and RPS2. The Arabidopsis protein RIN4 is targeted by multiple bacterial effectors, including HopF2, AvrPto, AvrRpt2, AvrB, and AvrRpm1.","type":"Introduction"}],"curator_id":"okovacs","released":"2022_03","term_ontology":"GO","curator_name":"Orsolya Panna Kovacs","reference_id":"26198070","version":3,"reference_html":"Phosphorylation of the Plant Immune Regulator RPM1-INTERACTING PROTEIN4 Enhances Plant Plasma Membrane H⁺-ATPase Activity and Inhibits Flagellin-Triggered Immune Responses in Arabidopsis. <i> Lee D, Bourdais G, Yu G, Robatzek S, Coaker G. </i> Plant Cell, 2015","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP01776r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":211,"term_name":"phosphorylation display site","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"RPM1-INDUCED PROTEIN KINASE (RIPK), a receptor-like cytoplasmic kinase, phosphorylates RIN4 at three residues: Thr-21, Ser-160, and Thr-166.","type":"Introduction"}],"curator_id":"okovacs","released":"2022_03","term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"26198070","version":2,"reference_html":"Phosphorylation of the Plant Immune Regulator RPM1-INTERACTING PROTEIN4 Enhances Plant Plasma Membrane H⁺-ATPase Activity and Inhibits Flagellin-Triggered Immune Responses in Arabidopsis. <i> Lee D, Bourdais G, Yu G, Robatzek S, Coaker G. </i> Plant Cell, 2015","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000045","ec_id":"ECO:0006204","region_id":"DP01776r003","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_Q8GYN5","date":"2018-08-09T10:47:59.000Z","acc":"Q8GYN5","name":"RPM1-interacting protein 4","length":211,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI00000ADDA8","genes":[{"name":{"value":"RIN4"},"orfNames":[{"value":"MJL12_1"}],"olnNames":[{"value":"At3g25070"}]}],"alphafold_very_low_content":0.3412322274881517,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":211,"type":"D"}],"Structural state":[{"start":1,"end":211,"type":"D"}],"Molecular function":[{"start":1,"end":211,"type":"F"}],"Disorder function":[{"start":1,"end":211,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_A1DWS9","sequence":"MEVKVTLIVAIVAALAISAHAQRDFNERRGKENDTERGQGGFGGRPGGMQMGGRRQDGGPMGEMRFDGPESGAPQMDGRRQNGGPMGGRRFDGPVFGGSRPDGAGGRPFFGQGGRRGDGEEETDAAQQIGDGLGGRGQFDGPGRRHHGRKPFGDRPFGRRNHTEGHQGHNETGDHPHDGHGRGHHGHRQGPPQDRPEEQPFGQRNESSDEDGRPHPRHHGRHHQHHHRNHTEGHQGHNETGDHPHRHHNKTGDGDQDRPMFEMRPFRFNPFGRKPFGDRPFGRRNGTEEGSARRDGQRRPYGNRGRWGENESEEEEHPTTESVTTSSPP","taxonomy":["Eukaryota","Metazoa","Echinodermata","Eleutherozoa","Echinozoa","Echinoidea","Euechinoidea","Echinacea","Camarodonta","Echinidea","Strongylocentrotidae","Strongylocentrotus"],"uniref90":"UniRef90_Q3LS93","disprot_id":"DP01777","ncbi_taxon_id":7668,"regions_counter":2,"creator":"okovacs","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":329,"region_id":"DP01777r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The Recombinant Sea Urchin Immune Effector Protein, rSpTransformer-E1, Binds to Phosphatidic Acid and Deforms Membranes. <i> Lun CM, Samuel RL, Gillmor SD, Boyd A, Smith LC. </i> Front Immunol, 2017","statement":[{"text":"In the absence of lipids, rSpTrf-E1 remained intrinsically disordered (~2% α helical) in agreement with a disordered structure in the absence of binding targets.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":22,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"28553283","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":329,"term_name":"lipid binding","start":22,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"we investigated possible interactions of rSpTrf-E1 and the recombinant fragments with phospholipids and identified specific binding to phosphatidic acid (PA) by the full-length protein and the rGly-rich and rHis-rich fragments. In addition, the rHis-rich fragment also binds to phosphatidyl inositol 4 phosphate [PtnIns(4)P], although with lower affinity.","type":"Results"}],"curator_id":"okovacs","released":"2022_03","term_ontology":"GO","curator_name":"Orsolya Panna Kovacs","reference_id":"28553283","version":3,"reference_html":"The Recombinant Sea Urchin Immune Effector Protein, rSpTransformer-E1, Binds to Phosphatidic Acid and Deforms Membranes. <i> Lun CM, Samuel RL, Gillmor SD, Boyd A, Smith LC. </i> Front Immunol, 2017","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008289","ec_id":"ECO:0006204","region_id":"DP01777r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q3LS93","date":"2018-08-09T11:12:03.000Z","acc":"Q3LS93","name":"Uncharacterized protein","length":329,"organism":"Strongylocentrotus purpuratus","dataset":[],"UniParc":"UPI00005B70E0","genes":[],"alphafold_very_low_content":0.8419452887537994,"disorder_content":0.9361702127659575,"disprot_consensus":{"full":[{"start":22,"end":329,"type":"D"}],"Structural state":[{"start":22,"end":329,"type":"D"}],"Molecular function":[{"start":22,"end":329,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00046","name":"Homeodomain","start":201,"end":257},{"id":"PF10525","name":"Engrailed homeobox C-terminal signature domain","start":258,"end":287}],"gene3D":[{"start":169,"end":261,"id":"1.10.10.60","name":"Homeodomain-like"}]},"uniref50":"UniRef50_Q05917","sequence":"MEEGGRSPREEAAEPQESGGDAEPGGGRRALLLPPGDPPHPHPHPHRITNFFIDNILRPEFGRRKEAGGTAGEPRRPGAESRRSPAAAAPAPGAPVPGGGGGGGGGSPGRGEGGPAALALHGAAKKGGDPAALEAALKARGLSGAELSVSSDSDSSQAGSNAGNQPMLWPAWVYCTRYSDRPSSGPRSRKPKKKNPNKEDKRPRTAFTAEQLQRLKAEFQTNRYLTEQRRQSLAQELGLNESQIKIWFQNKRAKIKKATGSKNSLAVHLMAQGLYNHSTTAKDGKSDSE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Phasianinae","Gallus"],"uniref90":"UniRef90_Q05917","disprot_id":"DP01779","ncbi_taxon_id":9031,"regions_counter":5,"creator":"okovacs","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":199,"region_id":"DP01779r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"1H, 13C and 15N resonance assignment of a 114-residue fragment of Engrailed 2 homeoprotein, a partially disordered protein. <i> Augustyniak R, Balayssac S, Ferrage F, Bodenhausen G, Lequin O. </i> Biomol NMR Assign, 2011","statement":[{"text":"The NH resona1H, 13C and 15N resonance assignment of a 114-residue fragment of Engrailed 2 homeoprotein, a partially disordered proteinnces corresponding to homeodomain residues are well dispersed, while those belonging to the N-terminal extension are all in a narrow range between 7.6 and 8.6 ppm, which indicates intrinsic disorder in regions outside the homeodomain.","type":"Title"},{"text":"The weak dispersion in the proton dimension of the (1)H-(15)N HSQC spectrum indicates the presence of disordered regions that do not belong to the homeodomain. This work is a first step toward the NMR investigation of the structure and dynamics of Engrailed 2 protein that contains a well-structured globular domain and partially disordered regions.","type":"Abstract"},{"text":"The NH resonances corresponding to homeodomain residues are well dispersed, while those belonging to the N-terminal extension are all in a narrow range between 7.6 and 8.6 ppm (see Fig. 1) which indicates intrinsic disorder in regions outside the homeodomain.","type":"Article"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":146,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21516336","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":146,"end":199,"reference_id":"12642491","reference_source":"pmid","reference_html":"Joint regulation of the MAP1B promoter by HNF3beta/Foxa2 and Engrailed is the result of a highly conserved mechanism for direct interaction of homeoproteins and Fox transcription factors. <i> Foucher I, Montesinos ML, Volovitch M, Prochiantz A, Trembleau A. </i> Development, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006077","ec_ontology":"ECO","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P32182","partner_start":null,"partner_end":null}],"region_id":"DP01779r004","statement":[{"text":"This led us to investigate if Engrailed and Foxa2 interact directly. Direct interaction was confirmed by pull-down experiments, and the regions participating in this interaction were identified. In Foxa2 the interacting domain is the Forkhead box DNA-binding domain. In Engrailed, two independent interacting domains exist: the homeodomain and a region that includes the Pbx-binding domain.","type":"Abstract"},{"text":"As illustrated in Fig. 6B (left panel), fragment 146-199 (containing the Pbx-interacting domain) and the homeodomain bind Foxa2. The 146-199 domain was further sub-divided into fragments 146-167 and 168-199 (the latter containing only the EH2-EH3 Pbx-interacting domain). Fig.6B (right panel) shows that these two sub-fragments still retain Foxa2, although less efficiently than the entire sequence. It can thus be concluded that the homeodomain and a domain N-terminal to the homeodomain, including the Pbx-interacting domain, bind Foxa2","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":146,"end":199,"reference_id":"12642491","reference_source":"pmid","reference_html":"Joint regulation of the MAP1B promoter by HNF3beta/Foxa2 and Engrailed is the result of a highly conserved mechanism for direct interaction of homeoproteins and Fox transcription factors. <i> Foucher I, Montesinos ML, Volovitch M, Prochiantz A, Trembleau A. </i> Development, 2003","date":"2022-03-08T15:07:00.055Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005648","ec_ontology":"ECO","ec_name":"luciferase reporter gene assay evidence used in manual assertion","released":"2022_03","version":4,"region_id":"DP01779r005","statement":[{"text":"Foxa2 physiologically interacts with Engrailed in regulating the MAP1B promoter ex vivo","type":"Results"},{"text":"At a higher dose (5 μg of plasmid), Foxa2 activates the MAP1B promoter and this activation is partially antagonized by the co-expression of low levels of Engrailed (2μg of plasmid) which have no significant effect per se (Fig.3C). Taken together these results suggest that Foxa2 and Engrailed physically interact and/or compete for overlapping DNA target sequences.","type":"Results"}],"ec_go":"IEP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q05917","date":"2018-08-09T12:05:04.000Z","acc":"Q05917","name":"Homeobox protein engrailed-2","length":289,"organism":"Gallus gallus","dataset":[],"UniParc":"UPI000240B465","genes":[{"name":{"value":"EN2"},"synonyms":[{"value":"EN-2"}]}],"alphafold_very_low_content":0.3391003460207612,"disorder_content":0.18685121107266436,"disprot_consensus":{"full":[{"start":146,"end":199,"type":"D"}],"Structural state":[{"start":146,"end":199,"type":"D"}],"Molecular function":[{"start":146,"end":199,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00527","name":"E7 protein, Early protein","start":5,"end":102}],"gene3D":[{"start":51,"end":106,"id":"G3DSA:3.30.160.730"}]},"uniref50":"UniRef50_P06788","sequence":"MHGPRETLQEIVLHLEPQNELDPVDLLCYEQLSESEEENDEADGVSHAQLPARRAEPQRHKILCVCCKCDGRIELTVESSAEDLRTLQQLFLSTLSFVCPWCATNQ","taxonomy":["Viruses","Monodnaviria","Shotokuvirae","Cossaviricota","Papovaviricetes","Zurhausenvirales","Papillomaviridae","Firstpapillomavirinae","Alphapapillomavirus"],"uniref90":"UniRef90_P21736","disprot_id":"DP01780","ncbi_taxon_id":10593,"regions_counter":1,"creator":"lchemes","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":54,"region_id":"DP01780r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of the partially folded high-risk human papilloma virus 45 oncoprotein E7. <i> Ohlenschläger O, Seiboth T, Zengerling H, Briese L, Marchanka A, Ramachandran R, Baum M, Korbas M, Meyer-Klaucke W, Dürst M, Görlach M. </i> Oncogene, 2006","statement":[{"text":"In contrast, the 1H–15N HSQC spectrum of the full-length E7 of HPV45 contained additional signals only in a very narrow chemical shift range, whereas the signals arising from the C-terminus remained virtually unaffected (Figure 2a). Such a spectral ‘fingerprint’ indicates an unstructured and flexible N-terminus (a.a. 1–54) and, importantly so, that the C-terminus of E7 folds autonomously into a well-structured domain","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16636661","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-27T07:20:07.569Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P21736","date":"2018-08-09T12:14:30.000Z","acc":"P21736","name":"Protein E7","length":106,"organism":"Human papillomavirus type 45","dataset":["Viral proteins"],"UniParc":"UPI0000170F8D","genes":[{"name":{"value":"E7","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04004","url":"https://hamap.expasy.org/unirule/MF_04004"}}]}}],"disorder_content":0.5094339622641509,"disprot_consensus":{"full":[{"start":1,"end":54,"type":"D"}],"Structural state":[{"start":1,"end":54,"type":"D"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MSYSVTLTGPGPWGFRLQGGKDFNMPLTISRITPGSKAAQSQLSQGDLVVAIDGVNTDTMTHLEAQNKIKSASYNLSLTLQKSKRPIPISTTAPPVQTPLPVIPHQKVVVNSPANADYQERFNPSALKDSALSTHKPIEVKGLGGKATIIHAQYNTPISMYSQDAIMDAIAGQAQAQGSDFSGSLPIKDLAVDSASPVYQAVIKSQNKPEDEADEWARRSSNLQSRSFRILAQMTGTEFMQDPDEEALRRSRERFETERNSPRFAKLRNWHHGLSAQILNVKS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"","disprot_id":"DP01781","ncbi_taxon_id":9606,"regions_counter":3,"creator":"okovacs","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":283,"region_id":"DP01781r001","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Expression and Purification of ZASP Subdomains and Clinically Important Isoforms: High-Affinity Binding to G-Actin. <i> Watts NR, Zhuang X, Kaufman JD, Palmer IW, Dearborn AD, Coscia S, Blech-Hermoni Y, Alfano C, Pastore A, Mankodi A, Wingfield PT. </i> Biochemistry, 2017","statement":[{"text":"After trypsin digestion, analysis of the main digestion product by mass spectrometry indicated a main product with mass of 26 648 Da corresponding to residues 1−228. Minor processing was observed at residues 217, 218, and 224, indicating a hot spot region consistent with high arginine content. The processed C-terminal sequence includes exon 9 (residues 252−282).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":229,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"28349680","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":283,"region_id":"DP01781r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Expression and Purification of ZASP Subdomains and Clinically Important Isoforms: High-Affinity Binding to G-Actin. <i> Watts NR, Zhuang X, Kaufman JD, Palmer IW, Dearborn AD, Coscia S, Blech-Hermoni Y, Alfano C, Pastore A, Mankodi A, Wingfield PT. </i> Biochemistry, 2017","statement":[{"text":"The HSQC spectrum of ZASP-S is indicative of a largely unstructured species with well-folded regions, as shown by the low dispersion of resonances in the center of the spectrum together with the highly dispersed peaks surrounding them. Comparison of the spectrum with that of the isolated PDZ domain shows that the dispersed peaks mostly belong to the PDZ domain (residues 1-84).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":85,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"28349680","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":283,"term_name":"protein binding","start":85,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Addition of ZASP-S to skeletal muscle G-actin resulted in the formation of F-actin (filaments). The PDZ domain was not required for array formation as ABRΔ10, both WT and mutant, formed similar arrays when mixed with F-actin.","type":"Discussion"}],"curator_id":"okovacs","released":"2022_03","term_ontology":"GO","curator_name":"Orsolya Panna Kovacs","reference_id":"28349680","version":3,"reference_html":"Expression and Purification of ZASP Subdomains and Clinically Important Isoforms: High-Affinity Binding to G-Actin. <i> Watts NR, Zhuang X, Kaufman JD, Palmer IW, Dearborn AD, Coscia S, Blech-Hermoni Y, Alfano C, Pastore A, Mankodi A, Wingfield PT. </i> Biochemistry, 2017","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP01781r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"","date":"2018-08-09T12:37:16.000Z","acc":"O75112-6","name":"Isoform 6 of LIM domain-binding protein 3","length":283,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000004FDF8","genes":[{"name":{"value":"LDB3","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:15710","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:15710"}}]},"synonyms":[{"value":"KIAA0613","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"BAA31588.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAA31588.1"}}]},{"value":"ZASP","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"CAB46728.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAB46728.1"}}]}]}],"disorder_content":0.7031802120141343,"disprot_consensus":{"full":[{"start":85,"end":283,"type":"D"}],"Structural state":[{"start":85,"end":283,"type":"D"}],"Molecular function":[{"start":85,"end":283,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00412","name":"LIM domain","start":294,"end":344},{"id":"PF00595","name":"PDZ domain","start":8,"end":80},{"id":"PF15936","name":"Domain of unknown function (DUF4749)","start":184,"end":267}],"gene3D":[{"start":1,"end":98,"id":"2.30.42.10","name":"2.30.42.10"},{"start":289,"end":350,"id":"2.10.110.10","name":"Cysteine Rich Protein"}]},"uniref50":"UniRef50_Q53GG5","sequence":"MPQTVILPGPAPWGFRLSGGIDFNQPLVITRITPGSKAAAANLCPGDVILAIDGFGTESMTHADAQDRIKAAAHQLCLKIDRGETHLWSPQVSEDGKAHPFKINLESEPQDGNYFEHKHNIRPKPFVIPGRSSGCSTPSGIDCGSGRSTPSSVSTVSTICPGDLKVAAKLAPNIPLEMELPGVKIVHAQFNTPMQLYSDDNIMETLQGQVSTALGETPLMSEPTASVPPESDVYRMLHDNRNEPTQPRQSGSFRVLQGMVDDGSDDRPAGTRSVRAPVTKVHGGSGGAQRMPLCDKCGSGIVGAVVKARDKYRHPECFVCADCNLNLKQKGYFFIEGELYCETHARARTKPPEGYDTVTLYPKA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q53GG5","disprot_id":"DP01782","ncbi_taxon_id":9606,"regions_counter":5,"creator":"okovacs","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":273,"region_id":"DP01782r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Characterization of the interaction between Actinin-Associated LIM Protein (ALP) and the rod domain of alpha-actinin. <i> Klaavuniemi T, Alho N, Hotulainen P, Kelloniemi A, Havukainen H, Permi P, Mattila S, Ylänne J. </i> BMC Cell Biol, 2009","statement":[{"text":"The CD spectrum suggested that ALP107-273 is mostly unfolded. No features characteristic of either α-helical or β-sheet structures were seen.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":107,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"19327143","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":273,"region_id":"DP01782r002","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Characterization of the interaction between Actinin-Associated LIM Protein (ALP) and the rod domain of alpha-actinin. <i> Klaavuniemi T, Alho N, Hotulainen P, Kelloniemi A, Havukainen H, Permi P, Mattila S, Ylänne J. </i> BMC Cell Biol, 2009","statement":[{"text":"Size exclusion chromatography showed that ALP107-273 eluted faster than expected based on its calculated monomer molecular weight (18 265 Da).","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":107,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"19327143","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":273,"region_id":"DP01782r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Characterization of the interaction between Actinin-Associated LIM Protein (ALP) and the rod domain of alpha-actinin. <i> Klaavuniemi T, Alho N, Hotulainen P, Kelloniemi A, Havukainen H, Permi P, Mattila S, Ylänne J. </i> BMC Cell Biol, 2009","statement":[{"text":"The 15N-HSQC spectrum measured in normal buffer conditions from uniformly 15N-labeled ALP107-273 was in line with the CD measurements as it showed the collapsed spectrum characteristic of an unfolded protein. When the 13C chemical shift values were compared to those of the random coil conformation, no clear indications of either α helix or β sheet secondary structures were observed.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":107,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"19327143","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":273,"term_name":"disorder to order","start":107,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"The NMR titration studies suggested that structure of ALP107-273 was partially stabilized by the interaction with the α-actinin rod region.","type":"Results"}],"curator_id":"okovacs","released":"2022_03","term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"19327143","version":2,"reference_html":"Characterization of the interaction between Actinin-Associated LIM Protein (ALP) and the rod domain of alpha-actinin. <i> Klaavuniemi T, Alho N, Hotulainen P, Kelloniemi A, Havukainen H, Permi P, Mattila S, Ylänne J. </i> BMC Cell Biol, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP01782r004","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":273,"term_name":"protein binding","start":107,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"To test whether ALP107-273 was functional, we measured the interaction of the purified protein fragment with α-actinin by surface plasmon resonance (SPR). A clear interaction was observed in both experimental setups and the apparent dissociation equilibrium constants (Kd) were in the low micromolar range.","type":"Results"}],"curator_id":"okovacs","released":"2022_03","term_ontology":"GO","curator_name":"Orsolya Panna Kovacs","reference_id":"19327143","version":3,"reference_html":"Characterization of the interaction between Actinin-Associated LIM Protein (ALP) and the rod domain of alpha-actinin. <i> Klaavuniemi T, Alho N, Hotulainen P, Kelloniemi A, Havukainen H, Permi P, Mattila S, Ylänne J. </i> BMC Cell Biol, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP01782r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q53GG5","date":"2018-08-09T13:05:07.000Z","acc":"Q53GG5","name":"PDZ and LIM domain protein 3","length":364,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000013DDB6","genes":[{"name":{"value":"PDLIM3"},"synonyms":[{"value":"ALP"}]}],"alphafold_very_low_content":0.23626373626373626,"disorder_content":0.45879120879120877,"disprot_consensus":{"full":[{"start":107,"end":273,"type":"T"}],"Structural state":[{"start":107,"end":273,"type":"D"}],"Structural transition":[{"start":107,"end":273,"type":"T"}],"Molecular function":[{"start":107,"end":273,"type":"F"}]}},{"features":{"pfam":[],"gene3D":[{"start":9,"end":210,"id":"3.30.450.40","name":"3.30.450.40"},{"start":212,"end":408,"id":"3.30.450.40","name":"3.30.450.40"},{"start":430,"end":588,"id":"3.30.450.40","name":"3.30.450.40"},{"start":668,"end":822,"id":"3.30.565.10","name":"Histidine kinase-like ATPase, C-terminal domain"},{"start":589,"end":667,"id":"1.10.287.130","name":"1.10.287.130"}]},"uniref50":"UniRef50_Q2JIZ5","sequence":"MDTETWAAAARPSRDALINRITHQIRQSLELDQILRATVEEVRAFLGTDRVKVYRFDPEGHGTVVAEARGGERLPSLLGLTFPAGDIPEEARRLFRLAQVRVIVDVEAQSRSISQPESWGLSARVPLGEPLQRPVDPCHVHYLKSMGVASSLVVPLMHHQELWGLLVSHHAEPRPYSQEELQVVQLLADQVSIAIAQAELLEQARQKAQQERLINQIAALVYSPLHPETTLTTVLEQLAAGLQGIGARLRIHFMGADTLCCHGVQPPASYDTWLQEQLGRAGGAGGWVKMWSLSHLEKWPELQEQMKQTPIRGLLVAQLAWNDQPVGWLSVFRGAVYQETHWAGYRWFTQGDPRQELPLISFAAWRELKIDEPKAWSAAEQELMSRVGVHLALSITQNQLYRQLQTLNARLEQEVQERTAALQRSLAMDALLQRVTDQVRSSLEEAQILRAVVQELALGLPIQGCDLCLYDWASGQATVRYEYTSALPPAGGITLTLADYPDLYRHLQGGQAVQFCHLPGQGWIPRREGLTLLVCPLRDDQGVLGDLWLAKPAAKCFDELEVQVVQQVADHCAIAIRQARLYQASVQQIGELERLNRLKDDFLSTVSHELRTPITNMRMAIQLLKTARAPQKREQYLKILEQECEREAELVNDLLDLQRLEQGSKTLHLEEVPLATWLPSVLEPFLQRAQVNQQRLQWQIAPNVGKVLTDQGGLERVVQELVNNACKYTPPGCSIWVTAQRPGPQQVEIRVINEGVEISPAEQERIFEKFYRIPSGDPWKRGGTGLGLALVKQWMQRLGGSVSVESSQGKTCFTLVLPQGSLPVQTSPLAHNCA","taxonomy":["Bacteria","Cyanobacteria","Synechococcales","Synechococcaceae","Synechococcus","unclassified Synechococcus"],"uniref90":"UniRef90_Q2JIZ5","disprot_id":"DP01783","ncbi_taxon_id":321332,"regions_counter":1,"creator":"akajava","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":30,"region_id":"DP01783r001","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Solution structure of a cyanobacterial phytochrome GAF domain in the red-light-absorbing ground state. <i> Cornilescu G, Ulijasz AT, Cornilescu CC, Markley JL, Vierstra RD. </i> J Mol Biol, 2008","statement":[{"text":"The final NMR model (Protein Data Bank (PDB) code 2K2N) is absent the C-terminal 6His tag and the first 30 amino acids, which include the RIT consensus motif present in many members of the PAS-less Cph subfamily.12 Both regions are highly dynamic and largely unstructured, which broadened out most of their NMR signals.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-26T14:21:06.571Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2K2N"},{"db":"PDB","id":"2LB9"},{"db":"BMRB","id":"15717"}],"reference_id":"18762196","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"48863","entry_name":"phycocyanobilin"}]}],"released":"2018_11","uniref100":"UniRef100_Q2JIZ5","date":"2018-08-09T13:22:52.000Z","acc":"Q2JIZ5","name":"Sensor histidine kinase","length":834,"organism":"Synechococcus sp. (strain JA-2-3B'a(2-13))","dataset":[],"UniParc":"UPI000069529D","genes":[{"olnNames":[{"value":"CYB_2465","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ABD03399.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABD03399.1"}}]}]}],"alphafold_very_low_content":0.050359712230215826,"disorder_content":0.03597122302158273,"disprot_consensus":{"full":[{"start":1,"end":30,"type":"D"}],"Structural state":[{"start":1,"end":30,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00169","name":"PH domain","start":371,"end":455},{"id":"PF00373","name":"FERM central domain","start":263,"end":370},{"id":"PF00373","name":"FERM central domain","start":456,"end":557},{"id":"PF18124","name":"Kindlin-2 N-terminal domain","start":11,"end":98}],"gene3D":[{"start":350,"end":486,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":553,"end":647,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":1,"end":101,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"}]},"uniref50":"UniRef50_Q86UX7","sequence":"MAGMKTASGDYIDSSWELRVFVGEEDPEAESVTLRVTGESHIGGVLLKIVEQINRKQDWSDHAIWWEQKRQWLLQTHWTLDKYGILADARLFFGPQHRPVILRLPNRRALRLRASFSQPLFQAVAAICRLLSIRHPEELSLLRAPEKKEKKKKEKEPEEELYDLSKVVLAGGVAPALFRGMPAHFSDSAQTEACYHMLSRPQPPPDPLLLQRLPRPSSLSDKTQLHSRWLDSSRCLMQQGIKAGDALWLRFKYYSFFDLDPKTDPVRLTQLYEQARWDLLLEEIDCTEEEMMVFAALQYHINKLSQSGEVGEPAGTDPGLDDLDVALSNLEVKLEGSAPTDVLDSLTTIPELKDHLRIFRIPRRPRKLTLKGYRQHWVVFKETTLSYYKSQDEAPGDPIQQLNLKGCEVVPDVNVSGQKFCIKLLVPSPEGMSEIYLRCQDEQQYARWMAGCRLASKGRTMADSSYTSEVQAILAFLSLQRTGSGGPGNHPHGPDASAEGLNPYGLVAPRFQRKFKAKQLTPRILEAHQNVAQLSLAEAQLRFIQAWQSLPDFGISYVMVRFKGSRKDEILGIANNRLIRIDLAVGDVVKTWRFSNMRQWNVNWDIRQVAIEFDEHINVAFSCVSASCRIVHEYIGGYIFLSTRERARGEELDEDLFLQLTGGHEAF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q86UX7","disprot_id":"DP01784","ncbi_taxon_id":9606,"regions_counter":3,"creator":"okovacs","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":224,"region_id":"DP01784r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR Characterization and Membrane Interactions of the Loop Region of Kindlin-3 F1 Subdomain. <i> Chua GL, Tan SM, Bhattacharjya S. </i> PLoS One, 2016","statement":[{"text":"The 15N-1H HSQC spectrum of the 83-residue loop region of kindlin-3 showed limited chemical shift dispersion, ~ 0.8 ppm, of the amide proton resonances, whereas 15N chemical shifts of the amino acids were better dispersed. These spectral features are typically observed for natively unfolded proteins and denatured proteins. The NOE pattern also suggests an absence of stably folded conformations.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":142,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"27101375","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":224,"term_name":"lipid binding","start":142,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"NMR 15N-1H HSQC titration experiments were performed to demonstrate residue specific interactions of F1 loop region with liposomes containing zwitterionic lipid POPC, negatively charged lipids POPS or POPG. Membrane specific association of kindlin-3 by its large loop region is a key requirement for the activation of integrins.","type":"Introduction"}],"curator_id":"okovacs","released":"2022_03","term_ontology":"GO","curator_name":"Orsolya Panna Kovacs","reference_id":"27101375","version":3,"reference_html":"NMR Characterization and Membrane Interactions of the Loop Region of Kindlin-3 F1 Subdomain. <i> Chua GL, Tan SM, Bhattacharjya S. </i> PLoS One, 2016","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008289","ec_id":"ECO:0006165","region_id":"DP01784r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":224,"region_id":"DP01784r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"NMR Characterization and Membrane Interactions of the Loop Region of Kindlin-3 F1 Subdomain. <i> Chua GL, Tan SM, Bhattacharjya S. </i> PLoS One, 2016","statement":[{"text":"UV CD spectra (240–190 nm) of the kindlin-3 loop in detergent free solutions and in solutions containing 50 mM detergents showed a relatively intense band at 208 nm and a less pronounced band around 222–225 nm.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":142,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"27101375","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q86UX7","date":"2018-08-09T13:29:29.000Z","acc":"Q86UX7","name":"Fermitin family homolog 3","length":667,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000019270B","genes":[{"name":{"value":"FERMT3"},"synonyms":[{"value":"KIND3"},{"value":"MIG2B"},{"value":"URP2"}]}],"alphafold_very_low_content":0.0944527736131934,"disorder_content":0.12443778110944528,"disprot_consensus":{"full":[{"start":142,"end":224,"type":"D"}],"Structural state":[{"start":142,"end":224,"type":"D"}],"Molecular function":[{"start":142,"end":224,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_A0A454B9Z9","sequence":"MVNINTSHMQSLSQLTSHLATQNQADDKEIRAHNGKDIFVKEGAPKNKSVSARISHQNKAKDIVVNLLTKQGIPKDVAKQMLQNVLNGENKLTLGNLKNLERLSSGPSSHWPAAQTDTSSSKTSKASSSVALINEHKDNLQKLGDFACTDLNTFGQKGSQFYETKGAPRLKALYANQARIAQDQRATMSASAVQAAAQRGNAPQLSTLQNIAKYVQNAKAGCCTTFAFAAAAEMIQGMSGTPENQPKVEVVAFKKGHSGTHLYVLVGRQEGSDIKDPSTWNKDVKIVDPWAASAFGATMFGDAQRPPVSNMFPPTEVIFDSHKLG","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Vibrionales","Vibrionaceae","Vibrio"],"uniref90":"UniRef90_A0A0D1EYU5","disprot_id":"DP01785","ncbi_taxon_id":223926,"regions_counter":3,"creator":"okovacs","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":125,"region_id":"DP01785r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Effectors of animal and plant pathogens use a common domain to bind host phosphoinositides. <i> Salomon D, Guo Y, Kinch LN, Grishin NV, Gardner KH, Orth K. </i> Nat Commun, 2013","statement":[{"text":"Alone, the spectrum of His-Gβ1-VopR (residues 1–125) chiefly contained peaks that could be attributed to the N-terminal Gβ1 domain; most of the remaining peaks originating from VopR 1–125 had heterogenous line widths and poor 1H chemical shift dispersion, consistent with unfolding.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":1,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"24346350","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":125,"term_name":"lipid binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"These results indicated that the BPDVopR is unstructured in solution without a phosphoinositide ligand, but that specific binding of PIP2 induces its folding. Further analysis using circular dichroism (CD) spectroscopy revealed a PIP2-dependent increase in secondary structure within His-Gβ1-VopR1–125, corroborating these findings.","type":"Results"}],"curator_id":"okovacs","released":"2022_03","term_ontology":"GO","curator_name":"Orsolya Panna Kovacs","reference_id":"24346350","version":3,"reference_html":"Effectors of animal and plant pathogens use a common domain to bind host phosphoinositides. <i> Salomon D, Guo Y, Kinch LN, Grishin NV, Gardner KH, Orth K. </i> Nat Commun, 2013","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008289","ec_id":"ECO:0006165","region_id":"DP01785r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":125,"term_name":"disorder to order","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"These results indicated that the BPDVopR is unstructured in solution without a phosphoinositide ligand, but that specific binding of PIP2 induces its folding. Further analysis using circular dichroism (CD) spectroscopy revealed a PIP2-dependent increase in secondary structure within His-Gβ1-VopR1–125, corroborating these findings.","type":"Results"}],"curator_id":"okovacs","released":"2022_03","term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"24346350","version":2,"reference_html":"Effectors of animal and plant pathogens use a common domain to bind host phosphoinositides. <i> Salomon D, Guo Y, Kinch LN, Grishin NV, Gardner KH, Orth K. </i> Nat Commun, 2013","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP01785r003","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_A0A0L8DKU1","date":"2018-08-09T14:37:35.000Z","acc":"Q87P35","name":"Uncharacterized protein","length":325,"organism":"Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)","dataset":[],"UniParc":"UPI0000009E22","genes":[{"olnNames":[{"value":"VP1683","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAC59946.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAC59946.1"}}]}]}],"alphafold_very_low_content":0.05846153846153846,"disorder_content":0.38461538461538464,"disprot_consensus":{"full":[{"start":1,"end":125,"type":"T"}],"Structural state":[{"start":1,"end":125,"type":"D"}],"Molecular function":[{"start":1,"end":125,"type":"F"}],"Structural transition":[{"start":1,"end":125,"type":"T"}]}},{"features":{"pfam":[{"id":"PF02496","name":"ABA/WDS induced protein","start":55,"end":132}]},"uniref50":"UniRef50_D2JX50","sequence":"MAEEKHHHHLFHHHKEEKPAEEVIYSETAYSGGGDYASGYTETVVAESASDEYEKYKKEEKHHKHKEHLGEMGAVAAGAFALYEKHEAKKDPDHAHKHKIEEEIAAAVAVGSGGYAFHEHHEKKDAKKEAEEASGKKHHHHLF","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Zingiberales","Musaceae","Musa"],"uniref90":"UniRef90_D2JX50","disprot_id":"DP01786","ncbi_taxon_id":485264,"regions_counter":6,"creator":"okovacs","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":143,"region_id":"DP01786r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"MpAsr encodes an intrinsically unstructured protein and enhances osmotic tolerance in transgenic Arabidopsis. <i> Dai JR, Liu B, Feng DR, Liu HY, He YM, Qi KB, Wang HB, Wang JF. </i> Plant Cell Rep, 2011","statement":[{"text":"The secondary structure of MpASR was revealed by CD spectroscopy. The far-UV CD spectrum of recombinant MpASR has a maximum negative ellipticity at 200.8 nm and low ellipticity around 215–229 nm , which indicates a disordered protein structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":1,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"21327389","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":143,"region_id":"DP01786r002","released":"2022_03","ec_id":"ECO:0007689","reference_html":"MpAsr encodes an intrinsically unstructured protein and enhances osmotic tolerance in transgenic Arabidopsis. <i> Dai JR, Liu B, Feng DR, Liu HY, He YM, Qi KB, Wang HB, Wang JF. </i> Plant Cell Rep, 2011","statement":[{"text":"By SDS–PAGE analysis, MpASR showed a characteristic low mobility. The predicted molecular mass of MpASR is 16.2 kDa, but it ran at 22 kDa. This high apparent molecular mass is caused by a highly hydrophilic property which is often characteristic of IDPs.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":1,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"21327389","version":2,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":143,"region_id":"DP01786r003","released":"2022_03","ec_id":"ECO:0006317","reference_html":"MpAsr encodes an intrinsically unstructured protein and enhances osmotic tolerance in transgenic Arabidopsis. <i> Dai JR, Liu B, Feng DR, Liu HY, He YM, Qi KB, Wang HB, Wang JF. </i> Plant Cell Rep, 2011","statement":[{"text":"MpASR proteins were heat stable, suggesting that compared with globular proteins such as BSA, MpASR is not likely to collapse and aggregate during high temperature treatment or boiling.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":1,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"21327389","version":2,"ec_name":"temperature-induced protein unfolding evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":143,"region_id":"DP01786r004","released":"2022_03","ec_id":"ECO:0007691","reference_html":"MpAsr encodes an intrinsically unstructured protein and enhances osmotic tolerance in transgenic Arabidopsis. <i> Dai JR, Liu B, Feng DR, Liu HY, He YM, Qi KB, Wang HB, Wang JF. </i> Plant Cell Rep, 2011","statement":[{"text":"Incubation of recombinant MpASR with 200 ng trypsin for 1 h resulted in a large amount of low molecular weight proteolytic products.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":1,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"21327389","version":2,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":143,"term_name":"disorder to order","start":1,"ec_name":"cleavage assay evidence used in manual assertion","statement":[{"text":"In the presence of Zn2+, MpASR was less susceptible to proteolysis in a zinc concentration-dependent manner.","type":"Results"}],"curator_id":"okovacs","released":"2022_03","term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"21327389","version":2,"reference_html":"MpAsr encodes an intrinsically unstructured protein and enhances osmotic tolerance in transgenic Arabidopsis. <i> Dai JR, Liu B, Feng DR, Liu HY, He YM, Qi KB, Wang HB, Wang JF. </i> Plant Cell Rep, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0007691","region_id":"DP01786r005","ec_go":"IDA","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":143,"term_name":"zinc ion binding","start":1,"ec_name":"cleavage assay evidence used in manual assertion","statement":[{"text":"Desiccation and zinc binding can induce structure and homodimerization in ASR1 protein. ASR1 protein also possess zinc-dependent DNA-binding activity. In the presence of Zn2+, MpASR was less susceptible to proteolysis in a zinc concentration-dependent manner.","type":"Results"}],"curator_id":"okovacs","released":"2022_03","term_ontology":"GO","curator_name":"Orsolya Panna Kovacs","reference_id":"21327389","version":3,"reference_html":"MpAsr encodes an intrinsically unstructured protein and enhances osmotic tolerance in transgenic Arabidopsis. <i> Dai JR, Liu B, Feng DR, Liu HY, He YM, Qi KB, Wang HB, Wang JF. </i> Plant Cell Rep, 2011","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008270","ec_id":"ECO:0007691","region_id":"DP01786r006","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_D2JX50","date":"2018-08-09T14:55:51.000Z","acc":"D2JX42","name":"Abscisic stress ripening","length":143,"organism":"Musa AAB Group","dataset":[],"UniParc":"UPI0001BEF216","genes":[{"name":{"value":"ASR1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ACZ60126.1","url":"https://www.ebi.ac.uk/ena/browser/view/ACZ60126.1"}}]}}],"alphafold_very_low_content":0.46853146853146854,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":143,"type":"T"}],"Structural state":[{"start":1,"end":143,"type":"D"}],"Structural transition":[{"start":1,"end":143,"type":"T"}],"Molecular function":[{"start":1,"end":143,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02496","name":"ABA/WDS induced protein","start":51,"end":127}]},"uniref50":"UniRef50_D2JX50","sequence":"MAEEKHHHHLFHHKKEGEDFQPAADGGADVYGYSTETVVTGTGNEGEYERITKEEKHHKHKEHLGEMGAVAAGAFALYEKHEAKKDPEHAHKHKIEEELAAAAAVGAGGFVFHEHHEKKQDHKEAKEASGEKKHHLFG","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","BOP clade","Pooideae","Triticodae","Triticeae","Hordeinae","Hordeum"],"uniref90":"UniRef90_A0A3B6HYQ0","disprot_id":"DP01787","ncbi_taxon_id":4513,"regions_counter":18,"creator":"okovacs","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":138,"region_id":"DP01787r001","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","statement":[{"text":"By comparing the experimentally determined Stokes radius (RS obs) of HvASR1 and TtASR1 with the Stokes radii expected for various conformational states (native, molten globule, pre-molten globule, and denaturant-unfolded), the two proteins were found to have an RS higher than the value expected for a monomeric, natively folded form (~20 Å) (Table 2).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"29138428","version":3,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:29:16.312Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":138,"region_id":"DP01787r002","released":"2022_03","ec_id":"ECO:0006317","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","statement":[{"text":"As shown in Supplementary Fig. S4, the experimentally observed profiles for HvASR1 and TtASR1 are consistent with lack of a stable 3D structure, as judged from their rather high basal fluorescence at 20 °C and from the flatness of their profile.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"29138428","version":3,"ec_name":"temperature-induced protein unfolding evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:29:18.076Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":138,"region_id":"DP01787r003","released":"2022_03","ec_id":"ECO:0007689","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","statement":[{"text":"Both HvASR1 and TtASR1 exhibit an abnormally slow migration in SDS-PAGE, with an apparent molecular mass (MM) comprised between 20 and 25 kDa (expected MM ~16 kDa) (Fig. 2).","type":"Results"},{"text":"The aberrant electrophoretic migration of HvASR1 and TtASR1 proteins constitutes the first experimental hint of their disordered nature.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"29138428","version":3,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:29:19.801Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":138,"region_id":"DP01787r004","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","statement":[{"text":"The experimental Rg values are therefore in very good agreement with the expected Rg values using parameters inferred from IDPs, while they are three times smaller that those expected for fully unfolded forms.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"29138428","version":3,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:29:21.197Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":138,"region_id":"DP01787r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","statement":[{"text":"Under native conditions and neutral pH, both proteins present spectra typical of proteins lacking any stable organized secondary structure, as judged from their large negative ellipticity at 200 nm, low amplitude in the 210–230 nm region, and low ellipticity at 190 nm (Fig. 5A). Spectral deconvolution revealed a high content (>60%) of unordered structure in both ASR1 proteins (see insets in Fig. 5A).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"29138428","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:29:22.954Z"}},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":138,"term_name":"zinc ion binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"We then recorded the far-UV CD spectra in the presence of zinc (Fig. 10). The addition of 2.5 mM ZnSO4 does not trigger a gain in α-helical structure, but rather, leads to a decrease in the amplitude of the negative peak at 200 nm, consistent with a decrease in disorder content.","type":"Results"},{"text":"By combining 10% TFE and 2 mM ZnSO4, a much more pronounced gain of structure is observed (Fig. 10), resulting in an increase in α-helical content, as judged from the appearance of the characteristic double minima at 208 and 222 nm (Fig. 10).","type":"Results"}],"curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"29138428","version":4,"reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008270","ec_id":"ECO:0006204","region_id":"DP01787r006","curator_orcid":"0000-0002-5152-5953","interaction_partner":[{"db":"ChEBI","id":"35176","partner_start":null,"partner_end":null}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:29:31.794Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":138,"region_id":"DP01787r007","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","statement":[{"text":"In the absence of TFE, the two proteins are readily degraded after an incubation as short as one hour, and entirely digested after 6 hours (Fig. 8), a behavior that is consistent with an overall high solvent accessibility and disordered nature.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"29138428","version":3,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:29:24.370Z"}},{"start":1,"end":138,"reference_id":"29138428","reference_source":"pmid","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006206","ec_ontology":"ECO","ec_name":"near-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01787r008","statement":[{"text":"Near-UV CD studies further support this conclusion (Supplementary Text 5). For both proteins, the addition of 2 mM ZnSO4 results in a spectral modification, consistent with the gain of some tertiary structure (Fig. 5D).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:29:27.139Z"}},{"start":1,"end":138,"reference_id":"29138428","reference_source":"pmid","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0008270","term_name":"zinc ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006206","ec_ontology":"ECO","ec_name":"near-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01787r009","statement":[{"text":"Near-UV CD studies further support this conclusion (Supplementary Text 5). For both proteins, the addition of 2 mM ZnSO4 results in a spectral modification, consistent with the gain of some tertiary structure (Fig. 5D).","type":"Results"}],"interaction_partner":[{"db":"ChEBI","id":"35176","partner_start":null,"partner_end":null}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:29:32.848Z"}},{"start":1,"end":138,"reference_id":"29138428","reference_source":"pmid","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-12-06T10:29:10.050Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140486","term_name":"zinc ion sequestering activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006206","ec_ontology":"ECO","ec_name":"near-UV circular dichroism evidence used in manual assertion","released":"2022_12","version":4,"region_id":"DP01787r010","statement":[{"text":"Near-UV CD studies further support this conclusion (Supplementary Text 5). For both proteins, the addition of 2 mM ZnSO4 results in a spectral modification, consistent with the gain of some tertiary structure (Fig. 5D).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a zinc ion to prevent it from interacting with sensitive components of a biological system.\" [PMID:12050156]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-06T12:48:21.839Z"}},{"start":1,"end":138,"reference_id":"29138428","reference_source":"pmid","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-12-06T10:29:00.046Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140486","term_name":"zinc ion sequestering activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_12","version":4,"region_id":"DP01787r011","statement":[{"text":"We then recorded the far-UV CD spectra in the presence of zinc (Fig. 10). The addition of 2.5 mM ZnSO4 does not trigger a gain in α-helical structure, but rather, leads to a decrease in the amplitude of the negative peak at 200 nm, consistent with a decrease in disorder content.","type":"Results"},{"text":"By combining 10% TFE and 2 mM ZnSO4, a much more pronounced gain of structure is observed (Fig. 10), resulting in an increase in α-helical content, as judged from the appearance of the characteristic double minima at 208 and 222 nm (Fig. 10).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a zinc ion to prevent it from interacting with sensitive components of a biological system.\" [PMID:12050156]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-06T12:48:22.321Z"}},{"start":1,"end":138,"reference_id":"29138428","reference_source":"pmid","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01787r012","statement":[{"text":"Both proteins reached their maximum exchange after 10 sec of labeling, indicating that HvASR1 and TtASR1 are predominantly unfolded in their native state.","type":"Results"},{"text":"Both ASR1 proteins are intrinsically disordered in their native state.","type":"Figure"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:29:25.751Z"}},{"start":1,"end":138,"reference_id":"29138428","reference_source":"pmid","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-12-06T10:28:46.523Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140486","term_name":"zinc ion sequestering activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","released":"2022_12","version":4,"region_id":"DP01787r013","statement":[{"text":"The addition of 2 mM ZnSO4 induced a weak dynamic HDX-MS behavior, indicative of structure formation, throughout the entire polypeptide chain of both proteins (Panels C, Fig. 11). Notably, the addition of both 10% TFE and 2 mM ZnSO4 in a combined fashion resulted in an more pronounced change in magnitude of HDX dynamics (Panels D, Fig. 11).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a zinc ion to prevent it from interacting with sensitive components of a biological system.\" [PMID:12050156]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-06T12:48:23.396Z"}},{"start":1,"end":138,"reference_id":"29138428","reference_source":"pmid","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01787r014","statement":[{"text":"The addition of 2 mM ZnSO4 induced a weak dynamic HDX-MS behavior, indicative of structure formation, throughout the entire polypeptide chain of both proteins (Panels C, Fig. 11). Notably, the addition of both 10% TFE and 2 mM ZnSO4 in a combined fashion resulted in an more pronounced change in magnitude of HDX dynamics (Panels D, Fig. 11).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:29:28.831Z"}},{"start":1,"end":138,"reference_id":"29138428","reference_source":"pmid","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0008270","term_name":"zinc ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"ChEBI","id":"35176","partner_start":null,"partner_end":null}],"region_id":"DP01787r015","statement":[{"text":"The addition of 2 mM ZnSO4 induced a weak dynamic HDX-MS behavior, indicative of structure formation, throughout the entire polypeptide chain of both proteins (Panels C, Fig. 11). Notably, the addition of both 10% TFE and 2 mM ZnSO4 in a combined fashion resulted in an more pronounced change in magnitude of HDX dynamics (Panels D, Fig. 11).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:29:35.751Z"}},{"start":1,"end":138,"reference_id":"29138428","reference_source":"pmid","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01787r016","statement":[{"text":"We first recorded the fluorescence emission spectra of the proteins either in the presence or absence of increasing zinc concentrations (Fig. 9). As expected for Tyr-containing proteins, both ASR1 proteins exhibit a maximum close to 303 nm. Interestingly, the intensity of the emission peak is gradually quenched with increasing zinc concentration, reflecting a decrease in the solvent exposure of Tyr residues. This behavior is indicative of a zinc-induced gain of tertiary structure.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural transition","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:29:30.233Z"}},{"start":1,"end":138,"reference_id":"29138428","reference_source":"pmid","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0008270","term_name":"zinc ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"ChEBI","id":"35176","partner_start":null,"partner_end":null}],"region_id":"DP01787r017","statement":[{"text":"We first recorded the fluorescence emission spectra of the proteins either in the presence or absence of increasing zinc concentrations (Fig. 9). As expected for Tyr-containing proteins, both ASR1 proteins exhibit a maximum close to 303 nm. Interestingly, the intensity of the emission peak is gradually quenched with increasing zinc concentration, reflecting a decrease in the solvent exposure of Tyr residues. This behavior is indicative of a zinc-induced gain of tertiary structure.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:29:37.376Z"}},{"start":1,"end":138,"reference_id":"29138428","reference_source":"pmid","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-12-06T10:28:33.480Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140486","term_name":"zinc ion sequestering activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","released":"2022_12","version":4,"region_id":"DP01787r018","statement":[{"text":"We first recorded the fluorescence emission spectra of the proteins either in the presence or absence of increasing zinc concentrations (Fig. 9). As expected for Tyr-containing proteins, both ASR1 proteins exhibit a maximum close to 303 nm. Interestingly, the intensity of the emission peak is gradually quenched with increasing zinc concentration, reflecting a decrease in the solvent exposure of Tyr residues. This behavior is indicative of a zinc-induced gain of tertiary structure.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a zinc ion to prevent it from interacting with sensitive components of a biological system.\" [PMID:12050156]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-06T12:48:25.971Z"}}],"released":"2018_11","uniref100":"UniRef100_A0A1Z3GD05","date":"2018-08-09T15:12:41.000Z","acc":"A0A1Z3GD05","name":"Abcissic acid stress ripening","length":138,"organism":"Hordeum vulgare","dataset":[],"UniParc":"UPI000B601618","genes":[{"name":{"value":"ASR1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ASC55655.1","url":"https://www.ebi.ac.uk/ena/browser/view/ASC55655.1"}}]}}],"alphafold_very_low_content":0.6376811594202898,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":138,"type":"T"}],"Structural state":[{"start":1,"end":138,"type":"D"}],"Molecular function":[{"start":1,"end":138,"type":"F"}],"Structural transition":[{"start":1,"end":138,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00250","name":"Forkhead domain","start":103,"end":184},{"id":"PF16676","name":"Transactivation domain of FOXO protein family","start":463,"end":503}],"gene3D":[{"start":92,"end":190,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}]},"uniref50":"UniRef50_P98177","sequence":"MDPGNENSATEAAAIIDLDPDFEPQSRPRSCTWPLPRPEIANQPSEPPEVEPDLGEKVHTEGRSEPILLPSRLPEPAGGPQPGILGAVTGPRKGGSRRNAWGNQSYAELISQAIESAPEKRLTLAQIYEWMVRTVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIKVHNEATGKSSWWMLNPEGGKSGKAPRRRAASMDSSSKLLRGRSKAPKKKPSVLPAPPEGATPTSPVGHFAKWSGSPCSRNREEADMWTTFRPRSSSNASSVSTRLSPLRPESEVLAEEIPASVSSYAGGVPPTLNEGLELLDGLNLTSSHSLLSRSGLSGFSLQHPGVTGPLHTYSSSLFSPAEGPLSAGEGCFSSSQALEALLTSDTPPPPADVLMTQVDPILSQAPTLLLLGGLPSSSKLATGVGLCPKPLEAPGPSSLVPTLSMIAPPPVMASAPIPKALGTPVLTPPTEAASQDRMPQDLDLDMYMENLECDMDNIISDLMDEGEGLDFNFEPDP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P98177","disprot_id":"DP01788","ncbi_taxon_id":9606,"regions_counter":13,"creator":"xcastro","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":91,"region_id":"DP01788r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of the DNA binding domain of the human forkhead transcription factor AFX (FOXO4). <i> Weigelt J, Climent I, Dahlman-Wright K, Wikström M. </i> Biochemistry, 2001","statement":[{"text":"The residues outside the structured DNA binding domain (residues 100−180) all showed random coil chemical shifts and very narrow resonance lines resulting in severe resonance overlap in some spectral regions. Nevertheless, complete backbone resonance assignments were obtained for nearly all residues, and side chain resonance assignments were more than 96% complete for residues 95−181.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"smribeiro","start":82,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1E17"}],"reference_id":"11352721","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":91,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Solution structure of the DNA binding domain of the human forkhead transcription factor AFX (FOXO4). <i> Weigelt J, Climent I, Dahlman-Wright K, Wikström M. </i> Biochemistry, 2001","statement":[{"text":"Non-specific contacts involving this segment are important for DNA binding affinity of FOXO4 (ref.  PubMed ID: 17244620).","type":"Curator statement"}],"term_id":"GO:0003676","curator_id":"smribeiro","start":82,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"11352721","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01788r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":96,"region_id":"DP01788r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the human FOXO4-DBD-DNA complex at 1.9 Å resolution reveals new details of FOXO binding to the DNA. <i> Boura E, Rezabkova L, Brynda J, Obsilova V, Obsil T. </i> Acta Crystallogr D Biol Crystallogr, 2010","statement":[{"text":"Missing electron density.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"smribeiro","start":86,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3L2C"}],"reference_id":"21123876","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":204,"region_id":"DP01788r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of the DNA binding domain of the human forkhead transcription factor AFX (FOXO4). <i> Weigelt J, Climent I, Dahlman-Wright K, Wikström M. </i> Biochemistry, 2001","statement":[{"text":"The residues outside the structured DNA binding domain (residues 100−180) all showed random coil chemical shifts and very narrow resonance lines resulting in severe resonance overlap in some spectral regions. Nevertheless, complete backbone resonance assignments were obtained for nearly all residues, and side chain resonance assignments were more than 96% complete for residues 95−181.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"smribeiro","start":182,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1E17"}],"reference_id":"11352721","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":204,"term_name":"phosphorylation display site","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Solution structure of the DNA binding domain of the human forkhead transcription factor AFX (FOXO4). <i> Weigelt J, Climent I, Dahlman-Wright K, Wikström M. </i> Biochemistry, 2001","statement":[{"text":"The PKB phosphorylation/14-3-3 protein-binding motif is RRAAS (residues 189-193, ref. PubMedID:    17244620).","type":"Curator statement"}],"term_id":"IDPO:0000045","curator_id":"smribeiro","start":182,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"11352721","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01788r005","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":204,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Solution structure of the DNA binding domain of the human forkhead transcription factor AFX (FOXO4). <i> Weigelt J, Climent I, Dahlman-Wright K, Wikström M. </i> Biochemistry, 2001","statement":[{"text":"Non-specific contacts involving this segment are important for DNA binding affinity and specificity of FOXO4 (refs. PubMed ID:  24121535 and PubMed ID: 17244620).","type":"Curator statement"}],"term_id":"GO:0003676","curator_id":"smribeiro","start":182,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"11352721","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01788r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P98177","date":"2018-08-09T15:20:31.000Z","acc":"P98177","name":"Forkhead box protein O4","length":505,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI000016A0B6","genes":[{"name":{"value":"FOXO4"},"synonyms":[{"value":"AFX"},{"value":"AFX1"},{"value":"MLLT7"}]}],"alphafold_very_low_content":0.5782178217821782,"disorder_content":0.07524752475247524,"disprot_consensus":{"full":[{"start":82,"end":96,"type":"D"},{"start":182,"end":204,"type":"D"}],"Structural state":[{"start":82,"end":96,"type":"D"},{"start":182,"end":204,"type":"D"}],"Molecular function":[{"start":82,"end":91,"type":"F"},{"start":182,"end":204,"type":"F"}],"Disorder function":[{"start":182,"end":204,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02496","name":"ABA/WDS induced protein","start":49,"end":125}]},"uniref50":"UniRef50_D2JX50","sequence":"MAEEKHHHLFHHKEGEDFQPAADGGVDTYGYSTETVVTATGNDGEYERITKEEKHHKHKEHLGEMGAAAAGAFALYEKHEAKKDPEHAHKHKIEEEVAAAAAVGAGGFVFHEHHEKKQDHKEAKEASGEKKHHLFG","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","BOP clade","Pooideae","Triticodae","Triticeae","Triticinae","Triticum"],"uniref90":"UniRef90_A0A3B6HYQ0","disprot_id":"DP01789","ncbi_taxon_id":4567,"regions_counter":18,"creator":"okovacs","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":136,"region_id":"DP01789r001","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","statement":[{"text":"By comparing the experimentally determined Stokes radius (RS obs) of HvASR1 and TtASR1 with the Stokes radii expected for various conformational states (native, molten globule, pre-molten globule, and denaturant-unfolded), the two proteins were found to have an RS higher than the value expected for a monomeric, natively folded form (~20 Å) (Table 2).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"29138428","version":3,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:31:56.331Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":136,"region_id":"DP01789r002","released":"2022_03","ec_id":"ECO:0006317","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","statement":[{"text":"As shown in Supplementary Fig. S4, the experimentally observed profiles for HvASR1 and TtASR1 are consistent with lack of a stable 3D structure, as judged from their rather high basal fluorescence at 20 °C and from the flatness of their profile.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"29138428","version":3,"ec_name":"temperature-induced protein unfolding evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:31:57.526Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":136,"region_id":"DP01789r003","released":"2022_03","ec_id":"ECO:0007689","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","statement":[{"text":"Both HvASR1 and TtASR1 exhibit an abnormally slow migration in SDS-PAGE, with an apparent molecular mass (MM) comprised between 20 and 25 kDa (expected MM ~16 kDa) (Fig. 2).","type":"Results"},{"text":"The aberrant electrophoretic migration of HvASR1 and TtASR1 proteins constitutes the first experimental hint of their disordered nature.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"29138428","version":3,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:31:59.039Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":136,"region_id":"DP01789r004","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","statement":[{"text":"The experimental Rg values are therefore in very good agreement with the expected Rg values using parameters inferred from IDPs, while they are three times smaller that those expected for fully unfolded forms.","type":"Results"},{"text":"The Rg value obtained for the ASR1 proteins (~35 Å) is 2.25 times higher than that expected for globular, fully unfolded proteins and IDPs of the same size (~15.5 Å) (see Eq. 10 in Methods)45","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"29138428","version":3,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:32:00.891Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":136,"region_id":"DP01789r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","statement":[{"text":"Under native conditions and neutral pH, both proteins present spectra typical of proteins lacking any stable organized secondary structure, as judged from their large negative ellipticity at 200 nm, low amplitude in the 210–230 nm region, and low ellipticity at 190 nm (Fig. 5A). Spectral deconvolution revealed a high content (>60%) of unordered structure in both ASR1 proteins (see insets in Fig. 5A).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"29138428","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:32:05.100Z"}},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":136,"term_name":"zinc ion binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"We then recorded the far-UV CD spectra in the presence of zinc (Fig. 10). The addition of 2.5 mM ZnSO4 does not trigger a gain in α-helical structure, but rather, leads to a decrease in the amplitude of the negative peak at 200 nm, consistent with a decrease in disorder content. By combining 10% TFE and 2 mM ZnSO4, a much more pronounced gain of structure is observed (Fig. 10), resulting in an increase in α-helical content, as judged from the appearance of the characteristic double minima at 208 and 222 nm (Fig. 10). While the addition of Zn2+ and 10% TFE does not promote an additional gain in α-helicity in HvASR1 (Fig. 10A), the reverse is observed for TtASR1, where the effects appear cumulative (Fig. 10B).","type":"Results"}],"curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"29138428","version":4,"reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008270","ec_id":"ECO:0006204","region_id":"DP01789r006","curator_orcid":"0000-0002-5152-5953","interaction_partner":[{"db":"ChEBI","id":"35176","partner_start":null,"partner_end":null}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:32:12.104Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":136,"region_id":"DP01789r007","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","statement":[{"text":"In the absence of TFE, the two proteins are readily degraded after an incubation as short as one hour, and entirely digested after 6 hours (Fig. 8), a behavior that is consistent with an overall high solvent accessibility and disordered nature.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":1,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"29138428","version":3,"ec_name":"cleavage assay evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-5152-5953","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:32:06.043Z"}},{"start":1,"end":136,"reference_id":"29138428","reference_source":"pmid","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01789r008","statement":[{"text":"We first recorded the fluorescence emission spectra of the proteins either in the presence or absence of increasing zinc concentrations (Fig. 9). As expected for Tyr-containing proteins, both ASR1 proteins exhibit a maximum close to 303 nm. Interestingly, the intensity of the emission peak is gradually quenched with increasing zinc concentration, reflecting a decrease in the solvent exposure of Tyr residues. This behavior is indicative of a zinc-induced gain of tertiary structure.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural transition","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:32:09.187Z"}},{"start":1,"end":136,"reference_id":"29138428","reference_source":"pmid","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0008270","term_name":"zinc ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"ChEBI","id":"35176","partner_start":null,"partner_end":null}],"region_id":"DP01789r009","statement":[{"text":"We first recorded the fluorescence emission spectra of the proteins either in the presence or absence of increasing zinc concentrations (Fig. 9). As expected for Tyr-containing proteins, both ASR1 proteins exhibit a maximum close to 303 nm. Interestingly, the intensity of the emission peak is gradually quenched with increasing zinc concentration, reflecting a decrease in the solvent exposure of Tyr residues. This behavior is indicative of a zinc-induced gain of tertiary structure.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:32:13.457Z"}},{"start":1,"end":136,"reference_id":"29138428","reference_source":"pmid","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-12-06T10:30:54.574Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140486","term_name":"zinc ion sequestering activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","released":"2022_12","version":4,"region_id":"DP01789r010","statement":[{"text":"We first recorded the fluorescence emission spectra of the proteins either in the presence or absence of increasing zinc concentrations (Fig. 9). As expected for Tyr-containing proteins, both ASR1 proteins exhibit a maximum close to 303 nm. Interestingly, the intensity of the emission peak is gradually quenched with increasing zinc concentration, reflecting a decrease in the solvent exposure of Tyr residues. This behavior is indicative of a zinc-induced gain of tertiary structure.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a zinc ion to prevent it from interacting with sensitive components of a biological system.\" [PMID:12050156]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-06T12:48:42.675Z"}},{"start":1,"end":136,"reference_id":"29138428","reference_source":"pmid","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-12-06T10:31:06.876Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140486","term_name":"zinc ion sequestering activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006206","ec_ontology":"ECO","ec_name":"near-UV circular dichroism evidence used in manual assertion","released":"2022_12","version":4,"region_id":"DP01789r011","statement":[{"text":"Near-UV CD studies further support this conclusion (Supplementary Text 5). For both proteins, the addition of 2 mM ZnSO4 results in a spectral modification, consistent with the gain of some tertiary structure (Fig. 5D). In particular, a peak between 275 and 282 nm, which corresponds to Tyr residues60, becomes discernible, reflecting a conformational change in the environment of Tyr residues (Fig. 5D).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a zinc ion to prevent it from interacting with sensitive components of a biological system.\" [PMID:12050156]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-06T12:48:44.035Z"}},{"start":1,"end":136,"reference_id":"29138428","reference_source":"pmid","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006206","ec_ontology":"ECO","ec_name":"near-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01789r012","statement":[{"text":"Near-UV CD studies further support this conclusion (Supplementary Text 5). For both proteins, the addition of 2 mM ZnSO4 results in a spectral modification, consistent with the gain of some tertiary structure (Fig. 5D). In particular, a peak between 275 and 282 nm, which corresponds to Tyr residues60, becomes discernible, reflecting a conformational change in the environment of Tyr residues (Fig. 5D).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-06T12:50:31.789Z"}},{"start":1,"end":136,"reference_id":"29138428","reference_source":"pmid","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0008270","term_name":"zinc ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006206","ec_ontology":"ECO","ec_name":"near-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01789r013","statement":[{"text":"Near-UV CD studies further support this conclusion (Supplementary Text 5). For both proteins, the addition of 2 mM ZnSO4 results in a spectral modification, consistent with the gain of some tertiary structure (Fig. 5D). In particular, a peak between 275 and 282 nm, which corresponds to Tyr residues60, becomes discernible, reflecting a conformational change in the environment of Tyr residues (Fig. 5D).","type":"Results"}],"interaction_partner":[{"db":"ChEBI","id":"35176","partner_start":null,"partner_end":null}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:32:15.632Z"}},{"start":1,"end":136,"reference_id":"29138428","reference_source":"pmid","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-12-06T10:31:17.397Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140486","term_name":"zinc ion sequestering activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_12","version":4,"region_id":"DP01789r014","statement":[{"text":"We then recorded the far-UV CD spectra in the presence of zinc (Fig. 10). The addition of 2.5 mM ZnSO4 does not trigger a gain in α-helical structure, but rather, leads to a decrease in the amplitude of the negative peak at 200 nm, consistent with a decrease in disorder content. By combining 10% TFE and 2 mM ZnSO4, a much more pronounced gain of structure is observed (Fig. 10), resulting in an increase in α-helical content, as judged from the appearance of the characteristic double minima at 208 and 222 nm (Fig. 10). While the addition of Zn2+ and 10% TFE does not promote an additional gain in α-helicity in HvASR1 (Fig. 10A), the reverse is observed for TtASR1, where the effects appear cumulative (Fig. 10B).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a zinc ion to prevent it from interacting with sensitive components of a biological system.\" [PMID:12050156]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-06T12:48:47.887Z"}},{"start":1,"end":136,"reference_id":"29138428","reference_source":"pmid","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01789r015","statement":[{"text":"Both proteins reached their maximum exchange after 10 sec of labeling, indicating that HvASR1 and TtASR1 are predominantly unfolded in their native state.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:32:07.500Z"}},{"start":1,"end":136,"reference_id":"29138428","reference_source":"pmid","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-12-06T10:31:27.880Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140486","term_name":"zinc ion sequestering activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","released":"2022_12","version":4,"region_id":"DP01789r016","statement":[{"text":"The addition of 2 mM ZnSO4 induced a weak dynamic HDX-MS behavior, indicative of structure formation, throughout the entire polypeptide chain of both proteins (Panels C, Fig. 11). Notably, the addition of both 10% TFE and 2 mM ZnSO4 in a combined fashion resulted in an more pronounced change in magnitude of HDX dynamics (Panels D, Fig. 11).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a zinc ion to prevent it from interacting with sensitive components of a biological system.\" [PMID:12050156]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-06T12:48:49.053Z"}},{"start":1,"end":136,"reference_id":"29138428","reference_source":"pmid","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01789r017","statement":[{"text":"The addition of 2 mM ZnSO4 induced a weak dynamic HDX-MS behavior, indicative of structure formation, throughout the entire polypeptide chain of both proteins (Panels C, Fig. 11). Notably, the addition of both 10% TFE and 2 mM ZnSO4 in a combined fashion resulted in an more pronounced change in magnitude of HDX dynamics (Panels D, Fig. 11).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:32:10.682Z"}},{"start":1,"end":136,"reference_id":"29138428","reference_source":"pmid","reference_html":"Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins. <i> Hamdi K, Salladini E, O'Brien DP, Brier S, Chenal A, Yacoubi I, Longhi S. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0008270","term_name":"zinc ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"ChEBI","id":"35176","partner_start":null,"partner_end":null}],"region_id":"DP01789r018","statement":[{"text":"The addition of 2 mM ZnSO4 induced a weak dynamic HDX-MS behavior, indicative of structure formation, throughout the entire polypeptide chain of both proteins (Panels C, Fig. 11). Notably, the addition of both 10% TFE and 2 mM ZnSO4 in a combined fashion resulted in an more pronounced change in magnitude of HDX dynamics (Panels D, Fig. 11).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-06T10:32:17.003Z"}}],"released":"2018_11","uniref100":"UniRef100_A0A1Z3GD08","date":"2018-08-09T15:37:09.000Z","acc":"A0A1Z3GD08","name":"Abcissic acid stress ripening","length":136,"organism":"Triticum turgidum subsp. durum","dataset":[],"UniParc":"UPI000B617730","genes":[{"name":{"value":"ASR1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ASC55654.1","url":"https://www.ebi.ac.uk/ena/browser/view/ASC55654.1"}}]}}],"alphafold_very_low_content":0.5882352941176471,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":136,"type":"T"}],"Structural state":[{"start":1,"end":136,"type":"D"}],"Molecular function":[{"start":1,"end":136,"type":"F"}],"Structural transition":[{"start":1,"end":136,"type":"T"}]}},{"features":{"pfam":[{"id":"PF01390","name":"SEA domain","start":1043,"end":1123}],"gene3D":[{"start":1032,"end":1097,"id":"3.30.70.960","name":"SEA domain"}]},"uniref50":"UniRef50_P15941","sequence":"MTPGTQSPFFLLLLLTVLTVVTGSGHASSTPGGEKETSATQRSSVPSSTEKNAVSMTSSVLSSHSPGSGSSTTQGQDVTLAPATEPASGSAATWGQDVTSVPVTRPALGSTTPPAHDVTSAPDNKPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDNRPALGSTAPPVHNVTSASGSASGSASTLVHNGTSARATTTPASKSTPFSIPSHHSDTPTTLASHSTKTDASSTHHSSVPPLTSSNHSTSPQLSTGVSFFFLSFHISNLQFNSSLEDPSTDYYQELQRDISEMFLQIYKQGGFLGLSNIKFRPGSVVVQLTLAFREGTINVHDVETQFNQYKTEAASRYNLTISDVSVSDVPFPFSAQSGAGVPGWGIALLVLVCVLVALAIVYLIALAVCQCRRKNYGQLDIFPARDTYHPMSEYPTYHTHGRYVPPSSTDRSPYEKVSAGNGGSSLSYTNPAVAATSANL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P15941","disprot_id":"DP01790","ncbi_taxon_id":9606,"regions_counter":4,"creator":"emaiani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1198,"region_id":"DP01790r002","start":1184,"term_id":"IDPO:0000002","statement":[{"text":"In addition, NMR analysis of MUC1-CD confirmed the absence of a detectable secondary structure (Fig 1B–1D), as shown by the presence of the peaks between 7.5 and 8.5 ppm, consistent with MUC1-CD being an unstructured protein.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26267657","version":2,"reference_html":"Characterization of the MUC1-C Cytoplasmic Domain as a Cancer Target. <i> Raina D, Agarwal P, Lee J, Bharti A, McKnight CJ, Sharma P, Kharbanda S, Kufe D. </i> PLoS One, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-09T15:48:55.996Z"}},{"term_namespace":"Biological process","ec_ontology":"ECO","end":1187,"region_id":"DP01790r003","start":1183,"term_id":"GO:0051179","statement":[{"text":"The double mutant chimera AQA+Y20N had reduced endocytosis and recycling rates and accumulated in EGFP-Rab11-positive endosomes, indicating that palmitoylation is the dominant feature modulating MUC1 recycling from endosomes back to the plasma membrane.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"immunodetection assay evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"26267657","version":3,"reference_html":"Characterization of the MUC1-C Cytoplasmic Domain as a Cancer Target. <i> Raina D, Agarwal P, Lee J, Bharti A, McKnight CJ, Sharma P, Kharbanda S, Kufe D. </i> PLoS One, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","term_name":"localization","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-09T15:48:41.110Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":1187,"region_id":"DP01790r004","start":1183,"term_id":"IDPO:0000044","statement":[{"text":"Palmitoylation of transmembrane proteins can affect their membrane trafficking, and the MUC1 sequence CQC3RRK at the boundary of the transmembrane and cytoplasmic domains mimics reported site(s) of S-palmitoylation.","type":"Abstract"},{"text":"Palmitoylation of transmembrane proteins can affect their membrane trafficking, and the MUC1 sequence CQC3RRK at the boundary of the transmembrane and cytoplasmic domains mimics reported site(s) of S-palmitoylation.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"immunodetection assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16507569","version":2,"reference_html":"Recycling of MUC1 is dependent on its palmitoylation. <i> Kinlough CL, McMahan RJ, Poland PA, Bruns JB, Harkleroad KL, Stremple RJ, Kashlan OB, Weixel KM, Weisz OA, Hughey RP. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","term_name":"palmitoylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-09T15:48:40.542Z"}}],"released":"2018_11","uniref100":"UniRef100_P15941","date":"2018-08-09T15:56:26.000Z","acc":"P15941","name":"Mucin-1","length":1255,"organism":"Homo sapiens","dataset":["Cancer-related proteins","Extracellular matrix proteins"],"UniParc":"UPI000059C524","genes":[{"name":{"value":"MUC1"},"synonyms":[{"value":"PUM"}]}],"alphafold_very_low_content":0.7123505976095618,"disorder_content":0.01195219123505976,"disprot_consensus":{"full":[{"start":1183,"end":1183,"type":"F"},{"start":1184,"end":1198,"type":"D"}],"Structural state":[{"start":1184,"end":1198,"type":"D"}],"Biological process":[{"start":1183,"end":1187,"type":"F"}],"Disorder function":[{"start":1183,"end":1187,"type":"F"}]}},{"features":{"pfam":[{"id":"PF09816","name":"RNA polymerase II transcription elongation factor","start":9,"end":107}]},"uniref50":"UniRef50_A0ZWU1","sequence":"MNSLQKGSYKVIPGSSFSKNSNGLLSIKYNFIPESVDPSRRGVLEKAQEAYRLRLPSTFDDDRPHIFEGSCQRARNVDCVLIFNAKTKTFTLEHIDEIARLNALRNPKVSKTVPSNAITQSDNSQISESKSTSQSAVTTNSTRRKEKELEASKDGKIKPSSSNTRYPAISSKGPITTDTNDEPDMEVMELDDFAKELELGFDQEFNSIDDPSTVSQTASKPISLRGLSSQERDYASSAQAEGISSASEDED","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"uniref90":"UniRef90_A0ZWU1","disprot_id":"DP01791","ncbi_taxon_id":284812,"regions_counter":2,"creator":"emaiani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":251,"region_id":"DP01791r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structure function characterization of the ELL Associated Factor (EAF) from Schizosaccharomyces pombe. <i> Dabas P, Sweta K, Ekka M, Sharma N. </i> Gene, 2018","term_id":"IDPO:0000002","curator_id":"emaiani","start":158,"term_ontology":"IDPO","curator_name":"Emiliano Maiani","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1432-5394","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29032152","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":251,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Structure function characterization of the ELL Associated Factor (EAF) from Schizosaccharomyces pombe. <i> Dabas P, Sweta K, Ekka M, Sharma N. </i> Gene, 2018","statement":[{"text":"Addition of increasing concentration of TFE showed progressive folding and increase in regularity by stimulating formation of α-helical secondary structure. Disordered region in SpEAF(158–251aa) decreased from 99% in absence of TFE to 31% in presence of 0.5% TFE","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"emaiani","start":158,"term_ontology":"IDPO","curator_name":"Emiliano Maiani","reference_id":"29032152","version":2,"curator_orcid":"0000-0003-1432-5394","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01791r002","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_A0ZWU1","date":"2018-08-09T16:09:03.000Z","acc":"A0ZWU1","name":"Ell1-associated factor 1","length":251,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","dataset":[],"UniParc":"UPI0000EA261C","genes":[{"name":{"value":"eaf1"},"orfNames":[{"value":"SPCC1223.10c"}]}],"alphafold_very_low_content":0.00796812749003984,"disorder_content":0.3745019920318725,"disprot_consensus":{"full":[{"start":158,"end":251,"type":"T"}],"Structural state":[{"start":158,"end":251,"type":"D"}],"Structural transition":[{"start":158,"end":251,"type":"T"}]}},{"features":{"pfam":[{"id":"PF15826","name":"Bcl-2-binding component 3, p53 upregulated modulator of apoptosis","start":2,"end":193}]},"uniref50":"UniRef50_Q9BXH1","sequence":"MARARQEGSSPEPVEGLARDSPRPFPLGRLMPSAVSCSLCEPGLPAAPAAPALLPAAYLCAPTAPPAVTAALGGPRWPGGHRSRPRGPRPDGPQPSLSPAQQHLESPVPSAPEALAGGPTQAAPGVRVEEEEWAREIGAQLRRMADDLNAQYERRRQEEQHRHRPSPWRVMYNLFMGLLPLPRDPGAPEMEPN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q9BXH1","disprot_id":"DP01794","ncbi_taxon_id":10090,"regions_counter":5,"creator":"smribeiro","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":161,"region_id":"DP01794r001","released":"2022_03","ec_id":"ECO:0001249","reference_html":"Folding and binding of an intrinsically disordered protein: fast, but not 'diffusion-limited'. <i> Rogers JM, Steward A, Clarke J. </i> J Am Chem Soc, 2013","statement":[{"text":"Fluorescence spectra of Mcl-1 and PUMA peptide show Mcl-1 is folded,\nPUMA is unfolded and binding occurs.","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"smribeiro","start":128,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"fluorescence evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23301700","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":161,"region_id":"DP01794r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Folding and binding of an intrinsically disordered protein: fast, but not 'diffusion-limited'. <i> Rogers JM, Steward A, Clarke J. </i> J Am Chem Soc, 2013","statement":[{"text":"From the CD spectrum, it can be calculated that the PUMA peptide has ∼20% residual helicity in the unbound state (in 50 mM PO4, pH 7.0, 25 °C),24 consistent with the high predicted helicity of the BH3 region in the context of the full-length PUMA protein (Figure ​(Figure1B).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"smribeiro","start":128,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23301700","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":161,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Folding and binding of an intrinsically disordered protein: fast, but not 'diffusion-limited'. <i> Rogers JM, Steward A, Clarke J. </i> J Am Chem Soc, 2013","term_id":"IDPO:0000011","curator_id":"smribeiro","start":128,"term_ontology":"IDPO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"23301700","version":2,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01794r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":161,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Folding and binding of an intrinsically disordered protein: fast, but not 'diffusion-limited'. <i> Rogers JM, Steward A, Clarke J. </i> J Am Chem Soc, 2013","statement":[{"text":"Interaction with Induced myeloid leukemia cell differentiation protein Mcl-1 homolog.","type":"Curator statement"}],"term_id":"GO:0005515","curator_id":"smribeiro","start":128,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"23301700","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01794r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":161,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Folding and binding of an intrinsically disordered protein: fast, but not 'diffusion-limited'. <i> Rogers JM, Steward A, Clarke J. </i> J Am Chem Soc, 2013","statement":[{"text":"Interaction with Induced myeloid leukemia cell differentiation protein Mcl-1 homolog.","type":"Curator statement"}],"term_id":"GO:0005515","curator_id":"smribeiro","start":128,"term_ontology":"GO","curator_name":"Sandra Macedo-Ribeiro","reference_id":"23301700","version":3,"curator_orcid":"0000-0002-7698-1170","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01794r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q99ML1","date":"2018-08-09T20:58:36.000Z","acc":"Q99ML1","name":"Bcl-2-binding component 3","length":193,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000020C0E","genes":[{"name":{"value":"Bbc3"},"synonyms":[{"value":"Puma"}]}],"alphafold_very_low_content":0.36787564766839376,"disorder_content":0.17616580310880828,"disprot_consensus":{"full":[{"start":128,"end":161,"type":"T"}],"Structural state":[{"start":128,"end":161,"type":"D"}],"Structural transition":[{"start":128,"end":161,"type":"T"}],"Molecular function":[{"start":128,"end":161,"type":"F"}]}},{"features":{"pfam":[{"id":"PF15384","name":"PAXX, PAralog of XRCC4 and XLF, also called C9orf142","start":8,"end":204}]},"uniref50":"UniRef50_Q9BUH6","sequence":"MDPLSPPLCTLPPGPEPPRFVCYCEGEESGEGDRGGFNLYVTDAAELWSTCFTPDSLAALKARFGLSAAEDITPRFRAACEQQAVALTLQEDRASLTLSGGPSALAFDLSKVPGPEAAPRLRALTLGLAKRVWSLERRLAAAEETAVSPRKSPRPAGPQLFLPDPDPQRGGPGPGVRRRCPGESLINPGFKSKKPAGGVDFDET","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9BUH6","disprot_id":"DP01795","ncbi_taxon_id":9606,"regions_counter":3,"creator":"npalopoli","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":204,"region_id":"DP01795r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"DNA repair. PAXX, a paralog of XRCC4 and XLF, interacts with Ku to promote DNA double-strand break repair. <i> Ochi T, Blackford AN, Coates J, Jhujh S, Mehmood S, Tamura N, Travers J, Wu Q, Draviam VM, Robinson CV, Blundell TL, Jackson SP. </i> Science, 2015","statement":[{"text":"Due to their being disordered, PAXX residues after 145 were not observed in the crystal structures.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"npalopoli","start":143,"term_ontology":"IDPO","curator_name":"Nicolás Palopoli","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7925-6436","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3WTF"}],"reference_id":"25574025","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":204,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"DNA repair. PAXX, a paralog of XRCC4 and XLF, interacts with Ku to promote DNA double-strand break repair. <i> Ochi T, Blackford AN, Coates J, Jhujh S, Mehmood S, Tamura N, Travers J, Wu Q, Draviam VM, Robinson CV, Blundell TL, Jackson SP. </i> Science, 2015","statement":[{"text":"Homodimer. Direct interaction with the DNA-bound XRCC5/Ku80 and XRCC6/Ku70 heterodimer as part of the non-homologous end joining (NHEJ) complex for DNA repair. Mass-spectrometry, western-blotting, mutation analysis, inhibition assays and surface plasmon resonance confirmed interaction between PAXX residues 177-204 and Ku complex.","type":"Curator statement"}],"term_id":"GO:0005515","curator_id":"npalopoli","start":143,"term_ontology":"GO","curator_name":"Nicolás Palopoli","reference_id":"25574025","version":3,"curator_orcid":"0000-0001-7925-6436","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"IntAct","id":"ebi:EBI-16137950"},{"db":" imex","id":"IM-24329-5"},{"db":" dip","id":"DIP-198956E"}],"region_id":"DP01795r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q9BUH6","date":"2018-08-10T03:56:01.000Z","acc":"Q9BUH6","name":"Protein PAXX","length":204,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00001BD908","genes":[{"name":{"value":"PAXX","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"25574025","url":"http://www.ncbi.nlm.nih.gov/pubmed/25574025","alternativeUrl":"https://europepmc.org/abstract/MED/25574025"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:27849","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:27849"}}]},"synonyms":[{"value":"C9orf142","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:27849","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:27849"}}]},{"value":"XLS","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"25941166","url":"http://www.ncbi.nlm.nih.gov/pubmed/25941166","alternativeUrl":"https://europepmc.org/abstract/MED/25941166"}}]}]}],"alphafold_very_low_content":0.0784313725490196,"disorder_content":0.30392156862745096,"disprot_consensus":{"full":[{"start":143,"end":204,"type":"D"}],"Structural state":[{"start":143,"end":204,"type":"D"}],"Molecular function":[{"start":143,"end":204,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":221,"end":486},{"id":"PF00498","name":"FHA domain","start":113,"end":191}],"gene3D":[{"start":304,"end":510,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"},{"start":211,"end":303,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":92,"end":210,"id":"2.60.200.20","name":"2.60.200.20"}]},"uniref50":"UniRef50_O96017","sequence":"MSRESDVEAQQSHGSSACSQPHGSVTQSQGSSSQSQGISSSSTSTMPNSSQSSHSSSGTLSSLETVSTQELYSIPEDQEPEDQEPEEPTPAPWARLWALQDGFANLECVNDNYWFGRDKSCEYCFDEPLLKRTDKYRTYSKKHFRIFREVGPKNSYIAYIEDHSGNGTFVNTELVGKGKRRPLNNNSEIALSLSRNKVFVFFDLTVDDQSVYPKALRDEYIMSKTLGSGACGEVKLAFERKTCKKVAIKIISKRKFAIGSAREADPALNVETEIEILKKLNHPCIIKIKNFFDAEDYYIVLELMEGGELFDKVVGNKRLKEATCKLYFYQMLLAVQYLHENGIIHRDLKPENVLLSSQEEDCLIKITDFGHSKILGETSLMRTLCGTPTYLAPEVLVSVGTAGYNRAVDCWSLGVILFICLSGYPPFSEHRTQVSLKDQITSGKYNFIPEVWAEVSEKALDLVKKLLVVDPKARFTTEEALRHPWLQDEDMKRKFQDLLSEENESTALPQVLAQPSTSRKRPREGEAEGAETTKRPAVCAAVL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O96017","disprot_id":"DP01797","ncbi_taxon_id":9606,"regions_counter":18,"creator":"bhajdu","regions":[{"region_id":"DP01797r001","ec_ontology":"ECO","end":90,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":64,"version":3,"statement":[{"text":"These maps were readily interpretable, allowing a model consisting of residues 91–207, together with 8 residues of the phosphopeptide, to be built using “O” (Jones et al. 1991).","type":"Methods"}],"term_name":"disorder","reference_html":"Structural and functional versatility of the FHA domain in DNA-damage signaling by the tumor suppressor kinase Chk2. <i> Li J, Williams BL, Haire LF, Goldberg M, Wilker E, Durocher D, Yaffe MB, Jackson SP, Smerdon SJ. </i> Mol Cell, 2002","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12049740","date":"2024-02-06T13:40:04.991Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1GXC"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"For crystallization, the phosphopeptide RHFDpTYLIRR was mixed with the Chk2 FHA fragment in a 1.5:1 stoichiometric excess and concentrated to ∼0.2 mM in a buffer containing 20 mM Tris-HCl (pH 8.0)."}]}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":70,"region_id":"DP01797r003","released":"2024_06","ec_id":"ECO:0007691","reference_html":"Structure and activation mechanism of the CHK2 DNA damage checkpoint kinase. <i> Cai Z, Chehab NH, Pavletich NP. </i> Mol Cell, 2009","statement":[{"text":"Limited proteolysis of full-length CHK2K249R indicated that the ∼70 N-terminal residues containing the SCD and the ∼30 C-terminal residues are highly susceptible to digestion, suggesting that they are unstructured or loosely folded (data not shown).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-05T17:15:30.991Z","reference_source":"pmid","term_name":"disorder","reference_id":"19782031","ec_go":"IDA","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys249Arg","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Thus, in order to investigate the mechanism of dimerization and to avoid heterogeneous phosphorylation, we used a CHK2 mutant harboring the K249R mutation (CHK2K249R) in the kinase active site."}]}]},{"region_id":"DP01797r006","ec_ontology":"ECO","end":91,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":70,"version":3,"statement":[{"text":"The P1 form contains four dimers in the asymmetric unit. The refined model of four dimers encompasses residues 92–501 of each CHK2, with residues 228–232, 254–267, 383–387, and 398–401 disordered.","type":"Methods"}],"term_name":"disorder","reference_html":"Structure and activation mechanism of the CHK2 DNA damage checkpoint kinase. <i> Cai Z, Chehab NH, Pavletich NP. </i> Mol Cell, 2009","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19782031","date":"2024-02-05T17:57:29.745Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3I6W"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys249Arg","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Thus, in order to investigate the mechanism of dimerization and to avoid heterogeneous phosphorylation, we used a CHK2 mutant harboring the K249R mutation (CHK2K249R) in the kinase active site."}]}],"sequence_construct":"ELYSIPEDQEPEDQEPEEPTPAPWARLWALQDGFANLECVNDNYWFGRDKSCEYCFDEPLLKRTDKYRTYSKKHFRIFREVGPKNSYIAYIEDHSGNGTFVNTELVGKGKRRPLNNNSEIALSLSRNKVFVFFDLTVDDQSVYPKALRDEYIMSKTLGSGACGEVKLAFERKTCKKVAIRIISKRKFAIGSAREADPALNVETEIEILKKLNHPCIIKIKNFFDAEDYYIVLELMEGGELFDKVVGNKRLKEATCKLYFYQMLLAVQYLHENGIIHRDLKPENVLLSSQEEDCLIKITDFGHSKILGETSLMRTLCGTPTYLAPEVLVSVGTAGYNRAVDCWSLGVILFICLSGYPPFSEHRTQVSLKDQITSGKYNFIPEVWAEVSEKALDLVKKLLVVDPKARFTTEEALRHPWLQDEDMKRKFQDLLSEENESTALPQVL"},{"region_id":"DP01797r007","ec_ontology":"ECO","end":267,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":254,"version":3,"statement":[{"text":"The P1 form contains four dimers in the asymmetric unit. The refined model of four dimers encompasses residues 92–501 of each CHK2, with residues 228–232, 254–267, 383–387, and 398–401 disordered.","type":"Methods"}],"term_name":"disorder","reference_html":"Structure and activation mechanism of the CHK2 DNA damage checkpoint kinase. <i> Cai Z, Chehab NH, Pavletich NP. </i> Mol Cell, 2009","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19782031","date":"2024-02-05T17:28:54.663Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3I6W"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys249Arg","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Thus, in order to investigate the mechanism of dimerization and to avoid heterogeneous phosphorylation, we used a CHK2 mutant harboring the K249R mutation (CHK2K249R) in the kinase active site."}]}],"sequence_construct":"ELYSIPEDQEPEDQEPEEPTPAPWARLWALQDGFANLECVNDNYWFGRDKSCEYCFDEPLLKRTDKYRTYSKKHFRIFREVGPKNSYIAYIEDHSGNGTFVNTELVGKGKRRPLNNNSEIALSLSRNKVFVFFDLTVDDQSVYPKALRDEYIMSKTLGSGACGEVKLAFERKTCKKVAIRIISKRKFAIGSAREADPALNVETEIEILKKLNHPCIIKIKNFFDAEDYYIVLELMEGGELFDKVVGNKRLKEATCKLYFYQMLLAVQYLHENGIIHRDLKPENVLLSSQEEDCLIKITDFGHSKILGETSLMRTLCGTPTYLAPEVLVSVGTAGYNRAVDCWSLGVILFICLSGYPPFSEHRTQVSLKDQITSGKYNFIPEVWAEVSEKALDLVKKLLVVDPKARFTTEEALRHPWLQDEDMKRKFQDLLSEENESTALPQVL"},{"region_id":"DP01797r011","ec_ontology":"ECO","end":387,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":377,"version":3,"statement":[{"text":"The P212121 crystals contain one dimer in the asymmetric unit. In the refined model, both protomers encompass residues 89–501, with residues 260–267 (αB-αC loop), 377–387 (C-terminal portion of activation loop), and 398–401 (αEF-αF loop) disordered.","type":"Methods"}],"term_name":"disorder","reference_html":"Structure and activation mechanism of the CHK2 DNA damage checkpoint kinase. <i> Cai Z, Chehab NH, Pavletich NP. </i> Mol Cell, 2009","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19782031","date":"2024-02-05T17:40:22.379Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3I6U"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys249Arg","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Thus, in order to investigate the mechanism of dimerization and to avoid heterogeneous phosphorylation, we used a CHK2 mutant harboring the K249R mutation (CHK2K249R) in the kinase active site."}]}],"sequence_construct":"EPEEPTPAPWARLWALQDGFANLECVNDNYWFGRDKSCEYCFDEPLLKRTDKYRTYSKKHFRIFREVGPKNSYIAYIEDHSGNGTFVNTELVGKGKRRPLNNNSEIALSLSRNKVFVFFDLTVDDQSVYPKALRDEYIMSKTLGSGACGEVKLAFERKTCKKVAIRIISKRKFAIGSAREADPALNVETEIEILKKLNHPCIIKIKNFFDAEDYYIVLELMEGGELFDKVVGNKRLKEATCKLYFYQMLLAVQYLHENGIIHRDLKPENVLLSSQEEDCLIKITDFGHSKILGETSLMRTLCGTPTYLAPEVLVSVGTAGYNRAVDCWSLGVILFICLSGYPPFSEHRTQVSLKDQITSGKYNFIPEVWAEVSEKALDLVKKLLVVDPKARFTTEEALRHPWLQDEDMKRKFQDLLSEE"},{"region_id":"DP01797r014","ec_ontology":"ECO","end":268,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":255,"version":3,"statement":[{"text":"Clear interpretable electron density is seen for residues 210–504 of the molecule, except for the loop comprised of residues 255–268 (connecting strand β3 to helix αC), which appears to be poorly ordered in these crystals. Similarly, at the C-terminus residues 505–531 have no discernable electron density and are also considered to be disordered.","type":"Results"}],"term_name":"disorder","reference_html":"Trans-activation of the DNA-damage signalling protein kinase Chk2 by T-loop exchange. <i> Oliver AW, Paul A, Boxall KJ, Barrie SE, Aherne GW, Garrett MD, Mittnacht S, Pearl LH. </i> EMBO J, 2006","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16794575","date":"2024-02-05T18:07:37.698Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2CN5"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17632","entry_name":"nitrate"}],"sequence_construct":"GPLGSHMSVYPKALRDEYIMSKTLGSGACGEVKLAFERKTCKKVAIKIISKRKFAIGSAREADPALNVETEIEILKKLNHPCIIKIKNFFDAEDYYIVLELMEGGELFDKVVGNKRLKEATCKLYFYQMLLAVQYLHENGIIHRDLKPENVLLSSQEEDCLIKITDFGHSKILGETSLMRTLCGTPTYLAPEVLVSVGTAGYNRAVDCWSLGVILFICLSGYPPFSEHRTQVSLKDQITSGKYNFIPEVWAEVSEKALDLVKKLLVVDPKARFTTEEALRHPWLQDEDMKRKFQDLLSEENESTALPQVLAQPSTSRKRPREGEAEGAE"},{"region_id":"DP01797r015","ec_ontology":"ECO","end":531,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":505,"version":3,"statement":[{"text":"Clear interpretable electron density is seen for residues 210–504 of the molecule, except for the loop comprised of residues 255–268 (connecting strand β3 to helix αC), which appears to be poorly ordered in these crystals. Similarly, at the C-terminus residues 505–531 have no discernable electron density and are also considered to be disordered.","type":"Results"}],"term_name":"disorder","reference_html":"Trans-activation of the DNA-damage signalling protein kinase Chk2 by T-loop exchange. <i> Oliver AW, Paul A, Boxall KJ, Barrie SE, Aherne GW, Garrett MD, Mittnacht S, Pearl LH. </i> EMBO J, 2006","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16794575","date":"2024-02-05T18:06:38.539Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2CN5"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17632","entry_name":"nitrate"}],"sequence_construct":"GPLGSHMSVYPKALRDEYIMSKTLGSGACGEVKLAFERKTCKKVAIKIISKRKFAIGSAREADPALNVETEIEILKKLNHPCIIKIKNFFDAEDYYIVLELMEGGELFDKVVGNKRLKEATCKLYFYQMLLAVQYLHENGIIHRDLKPENVLLSSQEEDCLIKITDFGHSKILGETSLMRTLCGTPTYLAPEVLVSVGTAGYNRAVDCWSLGVILFICLSGYPPFSEHRTQVSLKDQITSGKYNFIPEVWAEVSEKALDLVKKLLVVDPKARFTTEEALRHPWLQDEDMKRKFQDLLSEENESTALPQVLAQPSTSRKRPREGEAEGAE"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":543,"region_id":"DP01797r016","released":"2024_06","ec_id":"ECO:0007691","reference_html":"Structure and activation mechanism of the CHK2 DNA damage checkpoint kinase. <i> Cai Z, Chehab NH, Pavletich NP. </i> Mol Cell, 2009","statement":[{"text":"Limited proteolysis of full-length CHK2K249R indicated that the ∼70 N-terminal residues containing the SCD and the ∼30 C-terminal residues are highly susceptible to digestion, suggesting that they are unstructured or loosely folded (data not shown).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":513,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-05T17:05:11.184Z","reference_source":"pmid","term_name":"disorder","reference_id":"19782031","ec_go":"IDA","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys249Arg","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Thus, in order to investigate the mechanism of dimerization and to avoid heterogeneous phosphorylation, we used a CHK2 mutant harboring the K249R mutation (CHK2K249R) in the kinase active site."}]}]},{"start":66,"end":70,"reference_id":"16794575","reference_source":"pmid","reference_html":"Trans-activation of the DNA-damage signalling protein kinase Chk2 by T-loop exchange. <i> Oliver AW, Paul A, Boxall KJ, Barrie SE, Aherne GW, Garrett MD, Mittnacht S, Pearl LH. </i> EMBO J, 2006","date":"2024-02-05T18:15:39.441Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007719","ec_ontology":"ECO","ec_name":"immunodetection assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01797r017","statement":[{"text":"The baculovirus expressed protein, which contains high-levels of pThr68 (as measured by phospho-specific antibody) and is therefore likely to be substantially phosphorylated on T-loop residues Thr383 and Thr387, was found to be very significantly (100-fold compared to GST-CHK2-KD, 400-fold to CHK2-KD) more active than either of the kinase domain constructs over the course of the assay period (Figure 5G).","type":"Results"}]},{"start":1,"end":63,"reference_id":"12049740","reference_source":"pmid","reference_html":"Structural and functional versatility of the FHA domain in DNA-damage signaling by the tumor suppressor kinase Chk2. <i> Li J, Williams BL, Haire LF, Goldberg M, Wilker E, Durocher D, Yaffe MB, Jackson SP, Smerdon SJ. </i> Mol Cell, 2002","date":"2024-02-06T13:38:11.002Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01797r018","statement":[{"text":"An N-terminal fragment of human Chk2 (residues 1–225) was expressed in E. coli BL21(DE3) cells as a GST-fusion protein, purified by glutathione-affinity chromatography, and released by digestion with viral protease 3C (Pharmacia-LKB). Limited proteolysis with chymotrypsin and endoproteinase Glu-C (Promega) was performed essentially as described previously (Durocher et al. 2000). N- and C- terminal limits were determined by Edman sequencing and electrospray mass spectrometry, and the minimal chymotryptic FHA fragment (residues 64–219) was purified by anion exchange and gel filtration chromatography prior to further use in binding and crystallization experiments.","type":"Methods"}]}],"released":"2018_11","uniref100":"UniRef100_O96017","date":"2018-08-10T07:04:03.000Z","acc":"O96017","name":"Serine/threonine-protein kinase Chk2","length":543,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI00000316FF","genes":[{"name":{"value":"CHEK2"},"synonyms":[{"value":"CDS1"},{"value":"CHK2"},{"value":"RAD53"}]}],"alphafold_very_low_content":0.23204419889502761,"disorder_content":0.287292817679558,"disprot_consensus":{"full":[{"start":1,"end":91,"type":"D"},{"start":254,"end":268,"type":"D"},{"start":377,"end":387,"type":"D"},{"start":505,"end":543,"type":"D"}],"Structural state":[{"start":1,"end":91,"type":"D"},{"start":254,"end":268,"type":"D"},{"start":377,"end":387,"type":"D"},{"start":505,"end":543,"type":"D"}],"Disorder function":[{"start":66,"end":70,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00641","name":"Zn-finger in Ran binding protein and others","start":657,"end":686},{"id":"PF00641","name":"Zn-finger in Ran binding protein and others","start":723,"end":751},{"id":"PF00641","name":"Zn-finger in Ran binding protein and others","start":794,"end":822},{"id":"PF00641","name":"Zn-finger in Ran binding protein and others","start":851,"end":880},{"id":"PF08604","name":"Nucleoporin Nup153-like","start":113,"end":621},{"id":"PF10599","name":"Retro-transposon transporting motif","start":1386,"end":1475}],"gene3D":[{"start":697,"end":751,"id":"4.10.1060.10","name":"Zinc finger, RanBP2-type"},{"start":823,"end":880,"id":"4.10.1060.10","name":"Zinc finger, RanBP2-type"},{"start":766,"end":822,"id":"4.10.1060.10","name":"Zinc finger, RanBP2-type"},{"start":637,"end":686,"id":"4.10.1060.10","name":"Zinc finger, RanBP2-type"}]},"uniref50":"UniRef50_P49790","sequence":"MASGAGGVGGGGGGKIRTRRCHQGPIKPYQQGRQQHQGILSRVTESVKNIVPGWLQRYFNKNEDVCSCSTDTSEVPRWPENKEDHLVYADEESSNITDGRITPEPAVSNTEEPSTTSTASNYPDVLTRPSLHRSHLNFSMLESPALHCQPSTSSAFPIGSSGFSLVKEIKDSTSQHDDDNISTTSGFSSRASDKDITVSKNTSLPPLWSPEAERSHSLSQHTATSSKKPAFNLSAFGTLSPSLGNSSILKTSQLGDSPFYPGKTTYGGAAAAVRQSKLRNTPYQAPVRRQMKAKQLSAQSYGVTSSTARRILQSLEKMSSPLADAKRIPSIVSSPLNSPLDRSGIDITDFQAKREKVDSQYPPVQRLMTPKPVSIATNRSVYFKPSLTPSGEFRKTNQRIDNKCSTGYEKNMTPGQNREQRESGFSYPNFSLPAANGLSSGVGGGGGKMRRERTRFVASKPLEEEEMEVPVLPKISLPITSSSLPTFNFSSPEITTSSPSPINSSQALTNKVQMTSPSSTGSPMFKFSSPIVKSTEANVLPPSSIGFTFSVPVAKTAELSGSSSTLEPIISSSAHHVTTVNSTNCKKTPPEDCEGPFRPAEILKEGSVLDILKSPGFASPKIDSVAAQPTATSPVVYTRPAISSFSSSGIGFGESLKAGSSWQCDTCLLQNKVTDNKCIACQAAKLSPRDTAKQTGIETPNKSGKTTLSASGTGFGDKFKPVIGTWDCDTCLVQNKPEAIKCVACETPKPGTCVKRALTLTVVSESAETMTASSSSCTVTTGTLGFGDKFKRPIGSWECSVCCVSNNAEDNKCVSCMSEKPGSSVPASSSSTVPVSLPSGGSLGLEKFKKPEGSWDCELCLVQNKADSTKCLACESAKPGTKSGFKGFDTSSSSSNSAASSSFKFGVSSSSSGPSQTLTSTGNFKFGDQGGFKIGVSSDSGSINPMSEGFKFSKPIGDFKFGVSSESKPEEVKKDSKNDNFKFGLSSGLSNPVSLTPFQFGVSNLGQEEKKEELPKSSSAGFSFGTGVINSTPAPANTIVTSENKSSFNLGTIETKSASVAPFTCKTSEAKKEEMPATKGGFSFGNVEPASLPSASVFVLGRTEEKQQEPVTSTSLVFGKKADNEEPKCQPVFSFGNSEQTKDENSSKSTFSFSMTKPSEKESEQPAKATFAFGAQTSTTADQGAAKPVFSFLNNSSSSSSTPATSAGGGIFGSSTSSSNPPVATFVFGQSSNPVSSSAFGNTAESSTSQSLLFSQDSKLATTSSTGTAVTPFVFGPGASSNNTTTSGFGFGATTTSSSAGSSFVFGTGPSAPSASPAFGANQTPTFGQSQGASQPNPPGFGSISSSTALFPTGSQPAPPTFGTVSSSSQPPVFGQQPSQSAFGSGTTPNSSSAFQFGSSTTNFNFTNNSPSGVFTFGANSSTPAASAQPSGSGGFPFNQSPAAFTVGSNGKNVFSSSGTSFSGRKIKTAVRRRK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P49790","disprot_id":"DP01799","ncbi_taxon_id":9606,"regions_counter":8,"creator":"emaiani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1390,"region_id":"DP01799r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Plasticity of an ultrafast interaction between nucleoporins and nuclear transport receptors. <i> Milles S, Mercadante D, Aramburu IV, Jensen MR, Banterle N, Koehler C, Tyagi S, Clarke J, Shammas SL, Blackledge M, Gräter F, Lemke EA. </i> Cell, 2015","statement":[{"text":"The amino acid specific backbone dihedral angle distributions determined from the ensemble selections (Figure S1) show that negligible secondary structure is present.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"emaiani","start":1313,"term_ontology":"IDPO","curator_name":"Emiliano Maiani","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1432-5394","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"26456112","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-11T19:50:29.995Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1390,"term_name":"protein binding","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Plasticity of an ultrafast interaction between nucleoporins and nuclear transport receptors. <i> Milles S, Mercadante D, Aramburu IV, Jensen MR, Banterle N, Koehler C, Tyagi S, Clarke J, Shammas SL, Blackledge M, Gräter F, Lemke EA. </i> Cell, 2015","term_id":"GO:0005515","curator_id":"vnugnes","start":1313,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"26456112","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-12-11T19:58:23.704Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01799r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q14974","operator":null,"partner_start":null,"partner_end":null}],"statement":[{"text":"To characterize the effects of Importinβ binding on Nup153FGPxFG at atomic resolution, we titrated Importinβ into a solution of 15N labeled Nup153FGPxFG and measured 1H-15N HSQC spectra at different molar ratios. Peak intensities, as well as 1HN and 15N chemical shifts of Nup153FGPxFG, were analyzed for each titration step (Figures 3 and ​S4).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-15T10:12:12.997Z"}},{"start":1313,"end":1390,"reference_id":"26456112","reference_source":"pmid","reference_html":"Plasticity of an ultrafast interaction between nucleoporins and nuclear transport receptors. <i> Milles S, Mercadante D, Aramburu IV, Jensen MR, Banterle N, Koehler C, Tyagi S, Clarke J, Shammas SL, Blackledge M, Gräter F, Lemke EA. </i> Cell, 2015","date":"2023-12-11T19:58:32.500Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q14974","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01799r003","statement":[{"text":"We added unlabeled Importinβ to the FRET labeled Nup153FGPxFG and followed the smFRET response. While the diffusion of Nup153FGPxFG in the absence and presence of Importinβ confirmed the binding of Importinβ under single molecule conditions (Figures 2 and ​andS2),S2), we detected neither substantial changes in EFRET nor in the width of the histograms indicating absence of significant changes in the distance distribution (Figure S2 shows an all F to all A negative control).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-15T10:12:14.946Z"}},{"start":875,"end":1475,"reference_id":"21961597","reference_source":"pmid","reference_html":"Single molecule study of the intrinsically disordered FG-repeat nucleoporin 153. <i> Milles S, Lemke EA. </i> Biophys J, 2011","date":"2023-12-12T16:12:37.959Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01799r004","statement":[{"text":"As shown in Fig. 3 a, our measured distances are much shorter than expected for an IDP behaving like a relaxed coil (42,50). In fact, the distances are reminiscent of molten-globule or collapsed-coil behavior (23,42,51), showing that the protein stretches are compact in their native state.","type":"Results"},{"text":"Despite the different characteristics of the N-terminal stretch, a similar phenotypic property (RE) of both the N-terminal and the C-terminal stretches was observed.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser883Cys","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser990Cys","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser1042Cys","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser1354Cys","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser1391Cys","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser935Phe","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"For the other labeling site, we genetically encoded the unnatural amino-acid AcF, which serves as a unique linker to attach an Alexa 488 (D) hydroxylamine dye."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser938Phe","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"For the other labeling site, we genetically encoded the unnatural amino-acid AcF, which serves as a unique linker to attach an Alexa 488 (D) hydroxylamine dye."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser1042Phe","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser1094Phe","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"For the other labeling site, we genetically encoded the unnatural amino-acid AcF, which serves as a unique linker to attach an Alexa 488 (D) hydroxylamine dye."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala1312Phe","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"For the other labeling site, we genetically encoded the unnatural amino-acid AcF, which serves as a unique linker to attach an Alexa 488 (D) hydroxylamine dye."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala1349Phe","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"For the other labeling site, we genetically encoded the unnatural amino-acid AcF, which serves as a unique linker to attach an Alexa 488 (D) hydroxylamine dye."}]},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"Specific residue","statements":[{"type":"Results","text":"In this technology, one artificially mutated cysteine serves as a unique handle to install Alexa 594 (A) selectively via maleimide chemistry. For the other labeling site, we genetically encoded the unnatural amino-acid AcF, which serves as a unique linker to attach an Alexa 488 (D) hydroxylamine dye."}]},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"Specific residue","statements":[{"type":"Results","text":"In this technology, one artificially mutated cysteine serves as a unique handle to install Alexa 594 (A) selectively via maleimide chemistry. For the other labeling site, we genetically encoded the unnatural amino-acid AcF, which serves as a unique linker to attach an Alexa 488 (D) hydroxylamine dye."}]},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":1349,"end":null,"position":"Specific residue","statements":[{"type":"Results","text":"In this technology, one artificially mutated cysteine serves as a unique handle to install Alexa 594 (A) selectively via maleimide chemistry. For the other labeling site, we genetically encoded the unnatural amino-acid AcF, which serves as a unique linker to attach an Alexa 488 (D) hydroxylamine dye."}]},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":1312,"end":1312,"position":"Specific residue","statements":[{"type":"Results","text":"In this technology, one artificially mutated cysteine serves as a unique handle to install Alexa 594 (A) selectively via maleimide chemistry. For the other labeling site, we genetically encoded the unnatural amino-acid AcF, which serves as a unique linker to attach an Alexa 488 (D) hydroxylamine dye."}]},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":1094,"end":1094,"position":"Specific residue","statements":[{"type":"Results","text":"In this technology, one artificially mutated cysteine serves as a unique handle to install Alexa 594 (A) selectively via maleimide chemistry. For the other labeling site, we genetically encoded the unnatural amino-acid AcF, which serves as a unique linker to attach an Alexa 488 (D) hydroxylamine dye."}]},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":1042,"end":1042,"position":"Specific residue","statements":[{"type":"Results","text":"In this technology, one artificially mutated cysteine serves as a unique handle to install Alexa 594 (A) selectively via maleimide chemistry. For the other labeling site, we genetically encoded the unnatural amino-acid AcF, which serves as a unique linker to attach an Alexa 488 (D) hydroxylamine dye."}]},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":938,"end":938,"position":"Specific residue","statements":[{"type":"Results","text":"In this technology, one artificially mutated cysteine serves as a unique handle to install Alexa 594 (A) selectively via maleimide chemistry. For the other labeling site, we genetically encoded the unnatural amino-acid AcF, which serves as a unique linker to attach an Alexa 488 (D) hydroxylamine dye."}]},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":935,"end":935,"position":"Specific residue","statements":[{"type":"Results","text":"In this technology, one artificially mutated cysteine serves as a unique handle to install Alexa 594 (A) selectively via maleimide chemistry. For the other labeling site, we genetically encoded the unnatural amino-acid AcF, which serves as a unique linker to attach an Alexa 488 (D) hydroxylamine dye."}]},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":1391,"end":1391,"position":"Specific residue","statements":[{"type":"Results","text":"In this technology, one artificially mutated cysteine serves as a unique handle to install Alexa 594 (A) selectively via maleimide chemistry. For the other labeling site, we genetically encoded the unnatural amino-acid AcF, which serves as a unique linker to attach an Alexa 488 (D) hydroxylamine dye."}]},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":1354,"end":1354,"position":"Specific residue","statements":[{"type":"Results","text":"In this technology, one artificially mutated cysteine serves as a unique handle to install Alexa 594 (A) selectively via maleimide chemistry. For the other labeling site, we genetically encoded the unnatural amino-acid AcF, which serves as a unique linker to attach an Alexa 488 (D) hydroxylamine dye."}]},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":990,"end":990,"position":"Specific residue","statements":[{"type":"Results","text":"In this technology, one artificially mutated cysteine serves as a unique handle to install Alexa 594 (A) selectively via maleimide chemistry. For the other labeling site, we genetically encoded the unnatural amino-acid AcF, which serves as a unique linker to attach an Alexa 488 (D) hydroxylamine dye."}]},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":883,"end":883,"position":"Specific residue","statements":[{"type":"Results","text":"In this technology, one artificially mutated cysteine serves as a unique handle to install Alexa 594 (A) selectively via maleimide chemistry. For the other labeling site, we genetically encoded the unnatural amino-acid AcF, which serves as a unique linker to attach an Alexa 488 (D) hydroxylamine dye."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-15T10:11:55.822Z"}},{"start":875,"end":1475,"reference_id":"21961597","reference_source":"pmid","reference_html":"Single molecule study of the intrinsically disordered FG-repeat nucleoporin 153. <i> Milles S, Lemke EA. </i> Biophys J, 2011","date":"2023-12-12T16:21:06.062Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP01799r005","statement":[{"text":"As shown in Fig. 4 a, Nup153FG indeed formed a hydrogel.","type":"Results"},{"text":"A gel was mounted on a microscope and in Fig. 4 b, we show the results of a dual color fluorescence experiment. The large transport receptor Importin β (97 kDa) added to the surrounding buffer could easily enter the gel. The smaller dextran (70 kDa) added simultaneously did not considerably penetrate the gel. These findings demonstrate that highly concentrated human Nup153FG can also form a functional hydrogel in vitro.","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-15T10:12:16.760Z"}},{"start":875,"end":1475,"reference_id":"23238392","reference_source":"pmid","reference_html":"Facilitated aggregation of FG nucleoporins under molecular crowding conditions. <i> Milles S, Huy Bui K, Koehler C, Eltsov M, Beck M, Lemke EA. </i> EMBO Rep, 2013","date":"2023-12-13T18:43:52.821Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006333","ec_ontology":"ECO","ec_name":"thioflavin T based fluorescence spectroscopy evidence","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01799r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:16953"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5951"}],"statement":[{"text":"The ThT assay reported dramatically fastened amyloid formation kinetics of hNup153FG in buffer containing serine. Increasing serine concentrations even led to instantaneous aggregation of the protein (Fig 1A).","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-15T10:12:18.172Z"}},{"start":875,"end":1475,"reference_id":"23238392","reference_source":"pmid","reference_html":"Facilitated aggregation of FG nucleoporins under molecular crowding conditions. <i> Milles S, Huy Bui K, Koehler C, Eltsov M, Beck M, Lemke EA. </i> EMBO Rep, 2013","date":"2023-12-13T18:56:54.966Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","region_id":"DP01799r007","statement":[{"text":"This aggregation occurred even at the single-molecule level (pM protein concentrations, see Fig 1F; supplementary Fig S2 online) and is thus extremely high under molecular crowding conditions. As enhanced aggregation also occurred in the presence of other cosolutes such as lysine, trimethylaminoxid and the large molecule polyethylene glycol 20,000, we conclude that the aggregation accelerating effect is not owing to a specific chemical functionality but rather a general phenomenon, like space restriction or sequestering of water.","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"P49790","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-15T10:12:20.313Z"}},{"start":875,"end":1475,"reference_id":"23238392","reference_source":"pmid","reference_html":"Facilitated aggregation of FG nucleoporins under molecular crowding conditions. <i> Milles S, Huy Bui K, Koehler C, Eltsov M, Beck M, Lemke EA. </i> EMBO Rep, 2013","date":"2023-12-13T18:54:05.683Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP01799r008","statement":[{"text":"Figure 3 and supplementary Movie S1 online show that hNup153FG hydrogels are formed from interlaced fibres that build up a meshwork giving rise to the supramolecular architecture of a hydrogel (see supplementary Fig S3 online; supplementary Movie S2 online for yNup49FG).","type":"Results"},{"text":"To exclude artifacts that might arise from sample preparation, we confirmed these results using alternative preparation and imaging methods, namely scanning electron microscopy of heavy metal-shaded samples (Fig 3; supplementary Fig S3 online), as well as transmission electron microscopy of frozen-hydrated cryosections (supplementary Fig S5 online). We consistently observed fibrous networks within the hydrogels.","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-15T10:12:23.136Z"}}],"released":"2018_11","uniref100":"UniRef100_P49790","date":"2018-08-10T08:33:18.000Z","acc":"P49790","name":"Nuclear pore complex protein Nup153","length":1475,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI000012FC15","genes":[{"name":{"value":"NUP153"}}],"alphafold_very_low_content":0.8467796610169491,"disorder_content":0.4074576271186441,"disprot_consensus":{"full":[{"start":875,"end":1475,"type":"D"}],"Structural state":[{"start":875,"end":1475,"type":"D"}],"Molecular function":[{"start":875,"end":1475,"type":"F"}],"Biological process":[{"start":875,"end":1475,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_P15502-5","sequence":"MRSLTAAARRPEVLLLLLCILQPSQPGGVPGAVPGGVPGGVFFPGAGLGGLGVGGLGPGVKPAKPGVGGLVGPGLGAEGSALPGAFPGGFFGAGGGAAGAAAAYKAAAKAGAAGLGVGGIGGVGGLGVSTGAVVPQLGAGVGAGVKPGKVPGVGLPGVYPGGVLPGAGARFPGIGVLPGVPTGAGVKPKAQVGAGAFAGIPGVGPFGGQQPGLPLGYPIKAPKLPAGYGLPYKTGKLPYGFGPGGVAGSAGKAGYPTGTGVGPQAAAAAAKAAAKLGAGGAGVLPGVGVGGPGIPGAPGAIPGIGGIAGVGAPDAAAAAAAAAKAAKFGAAGGLPGVGVPGVGVPGVGVPGVGVPGVGVPGVGVPGVGVPGVGVPGVGVPGVGVPGVGVPGALSPAATAKAAAKAAKFGARGAVGIGGIPTFGLGPGGFPGIGDAAAAPAAAAAKAAKIGAGGVGALGGVVPGAPGAIPGLPGVGGVPGVGIPAAAAAKAAAKAAQFGLGPGVGVAPGVGVVPGVGVVPGVGVAPGIGLGPGGVIGAGVPAAAKSAAKAAAKAQFRAAAGLPAGVPGLGVGAGVPGLGVGAGVPGLGVGAGVPGPGAVPGTLAAAKAAKFGPGGVGALGGVGDLGGAGIPGGVAGVVPAAAAAAKAAAKAAQFGLGGVGGLGVGGLGAVPGAVGLGGVSPAAAAKAAKFGAAGLGGVLGAGQPFPIGGGAGGLGVGGKPPKPFGGALGALGFPGGACLGKSCGRKRK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P04985","disprot_id":"DP01801","ncbi_taxon_id":9913,"regions_counter":1,"creator":"emaiani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":747,"region_id":"DP01801r001","released":"2024_06","ec_id":"ECO:0006165","reference_html":"Quantitative observation of backbone disorder in native elastin. <i> Pometun MS, Chekmenev EY, Wittebort RJ. </i> J Biol Chem, 2004","statement":[{"text":"The primary focus of these experiments was to determine the degree of spatial averaging in hydrated elastin, and all results indicate that functional elastin is highly disordered.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-19T16:54:29.213Z","reference_source":"pmid","term_name":"disorder","reference_id":"14625282","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P04985","date":"2018-08-10T09:07:24.000Z","acc":"P04985","name":"Elastin","length":747,"organism":"Bos taurus","dataset":[],"UniParc":"UPI0000129E6C","genes":[{"name":{"value":"ELN"}}],"alphafold_very_low_content":0.9732262382864793,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":747,"type":"D"}],"Structural state":[{"start":1,"end":747,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02229","name":"Transcriptional Coactivator p15 (PC4)","start":64,"end":115}],"gene3D":[{"start":62,"end":127,"id":"2.30.31.10","name":"Transcriptional Coactivator Pc4; Chain A"}]},"uniref50":"UniRef50_P53999","sequence":"MPKSKELVSSSSSGSDSDSEVDKKLKRKKQVAPEKPVKKQKTGETSRALSSSKQSSSSRDDNMFQIGKMRYVSVRDFKGKVLIDIREYWMDPEGEMKPGRKGISLNPEQWSQLKEQISDIDDAVRKL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P53999","disprot_id":"DP01804","ncbi_taxon_id":9606,"regions_counter":4,"creator":"emaiani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":60,"region_id":"DP01804r001","released":"2022_06","ec_id":"ECO:0006165","reference_html":"The intrinsically unstructured domain of PC4 modulates the activity of the structured core through inter- and intramolecular interactions. <i> Jonker HR, Wechselberger RW, Boelens R, Kaptein R, Folkers GE. </i> Biochemistry, 2006","statement":[{"text":"However, the moderate NOE signal intensities, in combination with the chemical-shift data, indicate that these regions are predominantly unstructured in nature, which suggests either a pliable structure or exchange between the random-coil and more ordered structures. Also upon interaction with VP16ad, we did not observe significant changes in NOE contacts for PC4ntd, which suggest that PC4ntd is highly flexible and mostly unstructured both in the free form and in the complex with the activator.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-22T13:36:49.133Z","reference_source":"pmid","term_name":"disorder","reference_id":"16605275","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":60,"reference_id":"16605275","reference_source":"pmid","reference_html":"The intrinsically unstructured domain of PC4 modulates the activity of the structured core through inter- and intramolecular interactions. <i> Jonker HR, Wechselberger RW, Boelens R, Kaptein R, Folkers GE. </i> Biochemistry, 2006","date":"2022-06-22T13:05:14.766Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051101","term_name":"regulation of DNA binding","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","region_id":"DP01804r002","statement":[{"text":"Remarkably, the presence of PC4ntd can either be stimulatory (VP16 interaction), neutral (dsDNA), or inhibitory (ssDNA) on the PC4ctd functions. The apparent Kd values at room temperature for the interaction with PC4 and PC4ctd, respectively, are 391 ± 80 and 991 ± 195 nM for VP16ad, 55 ± 33 and 41 ± 21 nM for dsDNA, and 25 ± 4 nM and 0.98 ± 0.23 nM for ssDNA.","type":"Results"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of DNA binding. DNA binding is any process in which a gene product interacts selectively with DNA (deoxyribonucleic acid).\" [GOC:ai, GOC:dph, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":60,"reference_id":"16605275","reference_source":"pmid","reference_html":"The intrinsically unstructured domain of PC4 modulates the activity of the structured core through inter- and intramolecular interactions. <i> Jonker HR, Wechselberger RW, Boelens R, Kaptein R, Folkers GE. </i> Biochemistry, 2006","date":"2023-02-16T19:27:52.162Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"ec_go":"IPI","region_id":"DP01804r003","statement":[{"text":"Remarkably, the presence of PC4ntd can either be stimulatory (VP16 interaction), neutral (dsDNA), or inhibitory (ssDNA) on the PC4ctd functions. The apparent Kd values at room temperature for the interaction with PC4 and PC4ctd, respectively, are 391 ± 80 and 991 ± 195 nM for VP16ad, 55 ± 33 and 41 ± 21 nM for dsDNA, and 25 ± 4 nM and 0.98 ± 0.23 nM for ssDNA.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-22T13:06:26.319Z"}},{"start":1,"end":60,"reference_id":"16605275","reference_source":"pmid","reference_html":"The intrinsically unstructured domain of PC4 modulates the activity of the structured core through inter- and intramolecular interactions. <i> Jonker HR, Wechselberger RW, Boelens R, Kaptein R, Folkers GE. </i> Biochemistry, 2006","date":"2024-11-19T17:30:46.787Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000057","term_name":"self-regulatory activity","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001254","ec_ontology":"ECO","ec_name":"radioisotope assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":1,"ec_go":"IDA","region_id":"DP01804r004","statement":[{"text":"The modulatory role for PC4ntd, as observed for the other interactions, is underscored by the small increase in unwinding activity upon the mutation of the lysine residues within the amino-terminal domain and reflects the higher unwinding activity of PC4ctd in comparison with full-length PC4.","type":"Results"}],"term_comment":"","term_def":"\"Any process that stops, prevents or reduces the frequency, rate or extent of DNA duplex unwinding.\" [GO_REF:0000058, GOC:TermGenie, PMID:26503245]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_P53999","date":"2018-08-10T09:49:59.000Z","acc":"P53999","name":"Activated RNA polymerase II transcriptional coactivator p15","length":127,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000044938","genes":[{"name":{"value":"SUB1"},"synonyms":[{"value":"PC4"},{"value":"RPO2TC1"}]}],"alphafold_very_low_content":0.14960629921259844,"disorder_content":0.47244094488188976,"disprot_consensus":{"full":[{"start":1,"end":60,"type":"D"}],"Structural state":[{"start":1,"end":60,"type":"D"}],"Biological process":[{"start":1,"end":60,"type":"F"}],"Molecular function":[{"start":1,"end":60,"type":"F"}],"Disorder function":[{"start":1,"end":60,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04614","name":"Pex19 protein family","start":76,"end":299}],"gene3D":[{"start":158,"end":283,"id":"1.20.120.900","name":"Pex19, mPTS binding domain"}]},"uniref50":"UniRef50_P40855","sequence":"MAAAEEGCSVGAEADRELEELLESALDDFDKAKPSPAPPSTTTAPDASGPQKRSPGDTAKDALFASQEKFFQELFDSELASQATAEFEKAMKELAEEEPHLVEQFQKLSEAAGRVGSDMTSQQEFTSCLKETLSGLAKNATDLQNSSMSEEELTKAMEGLGMDEGDGEGNILPIMQSIMQNLLSKDVLYPSLKEITEKYPEWLQSHRESLPPEQFEKYQEQHSVMCKICEQFEAETPTDSETTQKARFEMVLDLMQQLQDLGHPPKELAGEMPPGLNFDLDALNLSGPPGASGEQCLIM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P40855","disprot_id":"DP01805","ncbi_taxon_id":9606,"regions_counter":6,"creator":"tszani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":165,"region_id":"DP01805r001","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Domain architecture and activity of human Pex19p, a chaperone-like protein for intracellular trafficking of peroxisomal membrane proteins. <i> Shibata H, Kashiwayama Y, Imanaka T, Kato H. </i> J Biol Chem, 2004","statement":[{"text":"We carried out limited proteolysis experiments with trypsin and V8 protease. Facts suggest that the C-terminal half of Pex19p is a relatively stable domain. On the other hand, the N-terminal half of Pex19p was susceptible to proteolytic degradation, which suggests that it has a flexible conformation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bhajdu","start":1,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"15252024","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":165,"term_name":"protein binding","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","reference_html":"Domain architecture and activity of human Pex19p, a chaperone-like protein for intracellular trafficking of peroxisomal membrane proteins. <i> Shibata H, Kashiwayama Y, Imanaka T, Kato H. </i> J Biol Chem, 2004","statement":[{"text":"We performed cell-free translation assays for each half as well as the full-length protein. Pex19p(N-half) bound to Pex3p-(34–373). Binding of Pex19p to PMP22, PMP70, and Pex16p requires more than the C-terminal half-sized domain of Pex19p.","type":"Results"}],"term_id":"GO:0005515","curator_id":"bhajdu","start":1,"term_ontology":"GO","curator_name":"Borbála Hajdu-Soltész","reference_id":"15252024","version":3,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","region_id":"DP01805r002","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":165,"region_id":"DP01805r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Domain architecture and activity of human Pex19p, a chaperone-like protein for intracellular trafficking of peroxisomal membrane proteins. <i> Shibata H, Kashiwayama Y, Imanaka T, Kato H. </i> J Biol Chem, 2004","statement":[{"text":"His10-Pex19p(N-half) displayed little secondary structure; its α-helix content was estimated as 6%. The additive spectrum of His10-Pex19p(N-half) plus Pex19p(C-half) almost coincided with that of the full-length His10-Pex19p. Therefore, we conclude that both halves of Pex19p maintain their respective three-dimensional structures as in the corresponding regions of the full-length His10-Pex19p.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bhajdu","start":1,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"15252024","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":165,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Domain architecture and activity of human Pex19p, a chaperone-like protein for intracellular trafficking of peroxisomal membrane proteins. <i> Shibata H, Kashiwayama Y, Imanaka T, Kato H. </i> J Biol Chem, 2004","statement":[{"text":"We performed cell-free translation assays for each half as well as the full-length protein. Pex19p(N-half) bound to Pex3p-(34–373). Binding of Pex19p to PMP22, PMP70, and Pex16p requires more than the C-terminal half-sized domain of Pex19p.","type":"Results"}],"term_id":"GO:0005515","curator_id":"bhajdu","start":1,"term_ontology":"GO","curator_name":"Borbála Hajdu-Soltész","reference_id":"15252024","version":3,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01805r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":182,"region_id":"DP01805r005","released":"2022_03","ec_id":"ECO:0006196","reference_html":"Association between the intrinsically disordered protein PEX19 and PEX3. <i> Hattula K, Hirschberg D, Kalkkinen N, Butcher SJ, Ora A. </i> PLoS One, 2014","statement":[{"text":"All PEX19 peptides from the N-terminal region A4 - L182, as well as the C-terminal end F278 - L297 were already fully deuterated after 30 seconds incubation in D2O (Figure 3A and Figure S1) indicating that these areas, consisting of two thirds of the protein, are highly solvent exposed and structurally disordered","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"tszani","start":4,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"25062251","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":297,"region_id":"DP01805r006","released":"2022_03","ec_id":"ECO:0006196","reference_html":"Association between the intrinsically disordered protein PEX19 and PEX3. <i> Hattula K, Hirschberg D, Kalkkinen N, Butcher SJ, Ora A. </i> PLoS One, 2014","statement":[{"text":"All PEX19 peptides from the N-terminal region A4 - L182, as well as the C-terminal end F278 - L297 were already fully deuterated after 30 seconds incubation in D2O (Figure 3A and Figure S1) indicating that these areas, consisting of two thirds of the protein, are highly solvent exposed and structurally disordered","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"tszani","start":278,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"25062251","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P40855","date":"2018-08-10T10:10:42.000Z","acc":"P40855","name":"Peroxisomal biogenesis factor 19","length":299,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000132BAD","genes":[{"name":{"value":"PEX19","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9713","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9713"}}]},"synonyms":[{"value":"HK33"},{"value":"PXF"}],"orfNames":[{"value":"OK/SW-cl.22"}]}],"alphafold_very_low_content":0.1939799331103679,"disorder_content":0.6755852842809364,"disprot_consensus":{"full":[{"start":1,"end":182,"type":"D"},{"start":278,"end":297,"type":"D"}],"Structural state":[{"start":1,"end":182,"type":"D"},{"start":278,"end":297,"type":"D"}],"Molecular function":[{"start":1,"end":165,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00695","name":"Major surface antigen from hepadnavirus","start":46,"end":445}]},"uniref50":"UniRef50_P03138","sequence":"MQLIITSKLGIIYILCGRLAFYIREKLHAVPHFVGHHILGNKSYSMGGWSSKPRQGMGTNLSVPNPLGFFPDHQLDPAFGANSNNPDWDFNPNKDHWPEAKQVGAGAFGPGFTPPHGGLLGWSPQAQGTLTTVPAAPPPASTNRQSGRQPTPISPPLRDSHPQAMQWNSTTFHQALLDPRVRGLYFPAGGSSSGTVNPVPTTASPISSIFSRTGDPAPNMESTTSGFLGPLLVLQAGFFLLTRILTIPQSLDSWLTSLNFLGGTPKCPGQNSQSPTSNHSPTSCPPTCPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYKGMLPVCPLLPGTSTTSTGPCKTCTIPAQNTSMFPSCCCTKPSDGNCTCIPIPSSWAFARFLWEWASVRFSWLSLLVPFVQWSAGLSPTVWLSVIWTMWYWGPSLYNILSPFLPLLPILCCLWAYI","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Blubervirales","Hepadnaviridae","Orthohepadnavirus"],"uniref90":"UniRef90_Q76R62","disprot_id":"DP01806","ncbi_taxon_id":10407,"regions_counter":7,"creator":"gbalatti","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":108,"region_id":"DP01806r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The hepatitis B virus preS1 domain hijacks host trafficking proteins by motif mimicry. <i> Jürgens MC, Vörös J, Rautureau GJ, Shepherd DA, Pye VE, Muldoon J, Johnson CM, Ashcroft AE, Freund SM, Ferguson N. </i> Nat Chem Biol, 2013","statement":[{"text":"The 13Cα chemical-shift index (Supplementary Fig. 2b), an indicator of secondary structure27, confirmed that preS1 had only short segments of partially populated α-helical or extended structure. Thus, the 108-residue preS1 domain is an IDP","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"emaiani","start":1,"term_ontology":"IDPO","curator_name":"Emiliano Maiani","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1432-5394","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23851574","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-12T11:44:23.300Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":108,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The hepatitis B virus preS1 domain hijacks host trafficking proteins by motif mimicry. <i> Jürgens MC, Vörös J, Rautureau GJ, Shepherd DA, Pye VE, Muldoon J, Johnson CM, Ashcroft AE, Freund SM, Ferguson N. </i> Nat Chem Biol, 2013","term_id":"GO:0005515","curator_id":"gbalatti","start":1,"term_ontology":"GO","curator_name":"Galo Balatti","reference_id":"23851574","version":4,"curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01806r002","interaction_partner":[{"db":"UniProt","id":"O75843","partner_start":665,"partner_end":785}],"statement":[{"text":"We report here atomic-resolution descriptions of the binding thermodynamics and structural biology of the interaction between preS1 and the EAR domain of g2-adaptin. NMR, protein engineering, X-ray crystallography and MS showed that preS1 contains multiple g2-EAR–binding motifs that mimic the membrane-trafficking motifs (and binding modes) of host proteins.","type":"Abstract"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-29T11:43:19.395Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":108,"region_id":"DP01806r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Purification and structural analysis of the hepatitis B virus preS1 expressed from Escherichia coli. <i> Maeng CY, Oh MS, Park IH, Hong HJ. </i> Biochem Biophys Res Commun, 2001","statement":[{"text":"The CD analysis showed that the purified preS1, which was largely unstructured in aqueous solution, acquired a significant (16%) alpha-helical structure when analyzed in 50% trifluoroethanol or 20 mM SDS. The results suggest that the preS1 assumes a mainly unstructured conformation and may form induced secondary structures upon binding to target proteins or under hydrophobic environment.","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"emaiani","start":1,"term_ontology":"IDPO","curator_name":"Emiliano Maiani","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1432-5394","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"11401532","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-12T11:44:09.688Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":108,"region_id":"DP01806r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Pre-structured motifs in the natively unstructured preS1 surface antigen of hepatitis B virus. <i> Chi SW, Kim DH, Lee SH, Chang I, Han KH. </i> Protein Sci, 2007","statement":[{"text":"The spectrum shows narrow chemical-shift dispersion in both dimensions, indicating that it is largely unstructured with no tertiary structure under a nondenaturing experimental condition.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"emaiani","start":1,"term_ontology":"IDPO","curator_name":"Emiliano Maiani","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1432-5394","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17766372","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-12T11:43:45.789Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":66,"end":92,"reference_id":"1732412","reference_source":"pmid","reference_html":"Search for hepatitis B virus cell receptors reveals binding sites for interleukin 6 on the virus envelope protein. <i> Neurath AR, Strick N, Sproul P. </i> J Exp Med, 1992","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0007695","ec_ontology":"ECO","ec_name":"cell-based assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"P05231","partner_start":null,"partner_end":null}],"region_id":"DP01806r005","statement":[{"text":"IL-6 and Not IL-6R Carries the Binding Site for the preS(21-47)\nSegment of the HBV env Protein.","type":"Results"},{"text":"This search revealed that interleukin 6 contains recognition sites for the preS(21-47) sequence and mediates HBV-cell interactions. Thus, HBV belongs to a group of viruses utilizing cytokines or cytokine receptors for replication and interference with the host immune system.","type":"Abstract"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-07T11:00:57.343Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":72,"end":90,"reference_id":"17766372","reference_source":"pmid","reference_html":"Pre-structured motifs in the natively unstructured preS1 surface antigen of hepatitis B virus. <i> Chi SW, Kim DH, Lee SH, Chang I, Han KH. </i> Protein Sci, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01806r007","statement":[{"text":"The most prominent pre-structured region encompasses\nresidues 27–45 and contains two helical turn motifs\n(black bars in Fig. 6) composed of residues Pro 32 –Ala 36\nand Pro 41 –Phe 45 , both of which are located within the\nputative HBD (residues 21–47) proposed by other techniques.","type":"Discussion"},{"text":"Location of pre-structured regions (this work) and previously suggested functional domains in preS1. Pre-structured regions\nare shown above the amino acid sequence of preS1 N-terminal 60 residues and are indicated by black, gray, or hatched bars. The most\nprominently pre-structured region is formed by residues 27–45.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-07T11:00:55.308Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_Q67953","date":"2018-08-10T11:03:15.000Z","acc":"Q67953","name":"Large envelope protein","length":445,"organism":"Hepatitis B virus","dataset":["Viral proteins"],"UniParc":"UPI00000F18F0","genes":[{"name":{"value":"S","evidences":[{"code":"ECO:0000256","source":{"name":"HAMAP-Rule","id":"MF_04075","url":"https://hamap.expasy.org/unirule/MF_04075"}}]}}],"disorder_content":0.24269662921348314,"disprot_consensus":{"full":[{"start":1,"end":71,"type":"D"},{"start":72,"end":90,"type":"T"},{"start":91,"end":108,"type":"D"}],"Structural state":[{"start":1,"end":108,"type":"D"}],"Molecular function":[{"start":1,"end":108,"type":"F"}],"Structural transition":[{"start":72,"end":90,"type":"T"}]}},{"features":{"pfam":[{"id":"PF04042","name":"DNA polymerase alpha/epsilon subunit B","start":196,"end":411},{"id":"PF18018","name":"DNA polymerase delta subunit OB-fold domain","start":49,"end":176}],"gene3D":[{"start":52,"end":453,"id":"3.60.21.50","name":"3.60.21.50"},{"start":55,"end":194,"id":"2.40.50.430","name":"2.40.50.430"}]},"uniref50":"UniRef50_P49005","sequence":"MFSEQAAQRAHTLLSPPSANNATFARVPVATYTNSSQPFRLGERSFSRQYAHIYATRLIQMRPFLENRAQQHWGSGVGVKKLCELQPEEKCCVVGTLFKAMPLQPSILREVSEEHNLLPQPPRSKYIHPDDELVLEDELQRIKLKGTIDVSKLVTGTVLAVFGSVRDDGKFLVEDYCFADLAPQKPAPPLDTDRFVLLVSGLGLGGGGGESLLGTQLLVDVVTGQLGDEGEQCSAAHVSRVILAGNLLSHSTQSRDSINKAKYLTKKTQAASVEAVKMLDEILLQLSASVPVDVMPGEFDPTNYTLPQQPLHPCMFPLATAYSTLQLVTNPYQATIDGVRFLGTSGQNVSDIFRYSSMEDHLEILEWTLRVRHISPTAPDTLGCYPFYKTDPFIFPECPHVYFCGNTPSFGSKIIRGPEDQTVLLVTVPDFSATQTACLVNLRSLACQPISFSGFGAEDDDLGGLGLGP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P49005","disprot_id":"DP01807","ncbi_taxon_id":9606,"regions_counter":2,"creator":"mpajkos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":53,"region_id":"DP01807r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"X-ray structure of the complex of regulatory subunits of human DNA polymerase delta. <i> Baranovskiy AG, Babayeva ND, Liston VG, Rogozin IB, Koonin EV, Pavlov YI, Vassylyev DG, Tahirov TH. </i> Cell Cycle, 2008","statement":[{"text":"The crystal structure of POLD2 (p50) and N-terminal domain of POLD3 (p66N) has been solved.\n\"The density was not observed for the total of 56 residues, including p50 amino acid residues 42–53, 102–122, 251–253, 382–387 and 466–469.\"\n\"each molecule contained all amino acid residues of p66N and p50, except disordered regions in four loops and the C-terminal tail of p50.\"","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":42,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3E0J"}],"reference_id":"18818516","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":122,"region_id":"DP01807r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"X-ray structure of the complex of regulatory subunits of human DNA polymerase delta. <i> Baranovskiy AG, Babayeva ND, Liston VG, Rogozin IB, Koonin EV, Pavlov YI, Vassylyev DG, Tahirov TH. </i> Cell Cycle, 2008","statement":[{"text":"The crystal structure of POLD2 (p50) and N-terminal domain of POLD3 (p66N) has been solved.\n\"The density was not observed for the total of 56 residues, including p50 amino acid residues 42–53, 102–122, 251–253, 382–387 and 466–469.\"\n\"each molecule contained all amino acid residues of p66N and p50, except disordered regions in four loops and the C-terminal tail of p50.\"","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":102,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3E0J"}],"reference_id":"18818516","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P49005","date":"2018-08-10T11:36:22.000Z","acc":"P49005","name":"DNA polymerase delta subunit 2","length":469,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000004D0E7","genes":[{"name":{"value":"POLD2"}}],"alphafold_very_low_content":0.03411513859275053,"disorder_content":0.07036247334754797,"disprot_consensus":{"full":[{"start":42,"end":53,"type":"D"},{"start":102,"end":122,"type":"D"}],"Structural state":[{"start":42,"end":53,"type":"D"},{"start":102,"end":122,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00865","name":"Osteopontin","start":36,"end":231}]},"uniref50":"UniRef50_P23498","sequence":"MKLTLLCLCFISITAAWPVSKSKQHAISASSEEKYDPRSHHTHRYHQDHVDSQSQEHLQQTQNDLASLQQTHYSSEENADVPEQPDFPDVPSKSQETVDDDDDDDNDSNDTDESDEVFTDFPTEAPVAPFNRGDNAGRGDSVAYGFRAKAHVVKASKIRKAARKLIEDDATTEDGDSQPAGLWWPKESREQNSRELPQHQSVENDSRPKFDSREVDGGDSKASAGVDSRESQGSVPAVDASNQTLESAEDAEDRHSIENNEVTR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Perdicinae","Coturnix"],"uniref90":"UniRef90_P23498","disprot_id":"DP01808","ncbi_taxon_id":93934,"regions_counter":4,"creator":"emaiani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":120,"region_id":"DP01808r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Compensatory adaptations of structural dynamics in an intrinsically disordered protein complex. <i> Kurzbach D, Schwarz TC, Platzer G, Höfler S, Hinderberger D, Konrat R. </i> Angew Chem Int Ed Engl, 2014","statement":[{"text":"the region encompassing residues 90–120 exhibitsincreased backbone flexibility as evidenced by both decreasedR2values and more negative heteronuclear NOEs.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"emaiani","start":90,"term_ontology":"IDPO","curator_name":"Emiliano Maiani","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1432-5394","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24604825","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":120,"term_name":"order to disorder","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Compensatory adaptations of structural dynamics in an intrinsically disordered protein complex. <i> Kurzbach D, Schwarz TC, Platzer G, Höfler S, Hinderberger D, Konrat R. </i> Angew Chem Int Ed Engl, 2014","statement":[{"text":"Concluding, the PRE (paramagnetic relaxation enhancement) data indicate that the central segment (residues 90–150) of OPN expands upon heparin binding, comparable to an “unfolding-upon-binding”event.","type":"Results"}],"term_id":"IDPO:0000014","curator_id":"emaiani","start":90,"term_ontology":"IDPO","curator_name":"Emiliano Maiani","reference_id":"24604825","version":2,"curator_orcid":"0000-0003-1432-5394","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01808r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":120,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Compensatory adaptations of structural dynamics in an intrinsically disordered protein complex. <i> Kurzbach D, Schwarz TC, Platzer G, Höfler S, Hinderberger D, Konrat R. </i> Angew Chem Int Ed Engl, 2014","term_id":"GO:0005515","curator_id":"emaiani","start":90,"term_ontology":"GO","curator_name":"Emiliano Maiani","reference_id":"24604825","version":3,"curator_orcid":"0000-0003-1432-5394","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01808r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":264,"reference_id":"38547550","reference_source":"pmid","reference_html":"A set of cross-correlated relaxation experiments to probe the correlation time of two different and complementary spin pairs. <i> Ceccolini I, Kauffmann C, Holzinger J, Konrat R, Zawadzka-Kazimierczuk A. </i> J Magn Reson, 2024","date":"2024-11-01T16:07:37.909Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0379","term_name":"13C label","term_namespace":"Labels and dyes","start":null,"end":null,"position":null},{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":null}],"region_id":"DP01808r004","statement":[{"text":"In contrast to the uniformity observed in ubiquitin, qOPN rates present a distinctive profile. This is particularly noticeable in the transverse rates (Fig. 6A), where three regions encompassing residues 120–132, 140–175 and 176–190 are less flexible (higher rates) [82], [88].","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_Q9I832","date":"2018-08-10T11:52:44.000Z","acc":"Q9I832","name":"Osteopontin","length":264,"organism":"Coturnix japonica","dataset":[],"UniParc":"UPI00000FD971","genes":[{"name":{"value":"OPN","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF63330.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF63330.1"}}]}}],"alphafold_very_low_content":0.4734848484848485,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":89,"type":"D"},{"start":90,"end":120,"type":"T"},{"start":121,"end":264,"type":"D"}],"Structural state":[{"start":1,"end":264,"type":"D"}],"Structural transition":[{"start":90,"end":120,"type":"T"}],"Molecular function":[{"start":90,"end":120,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00856","name":"SET domain","start":623,"end":726},{"id":"PF11616","name":"WD repeat binding protein EZH2","start":39,"end":68},{"id":"PF18118","name":"Polycomb repressive complex 2 tri-helical domain","start":158,"end":249},{"id":"PF18264","name":"CXC domain","start":559,"end":590},{"id":"PF21358","name":"Ezh2, MCSS domain","start":257,"end":309}],"gene3D":[{"start":371,"end":475,"id":"1.20.58.1880","name":"1.20.58.1880"},{"start":520,"end":729,"id":"2.170.270.10","name":"SET domain"}]},"uniref50":"UniRef50_Q15910","sequence":"MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEWKQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPAPAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q15910","disprot_id":"DP01817","ncbi_taxon_id":9606,"regions_counter":17,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":421,"region_id":"DP01817r001","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Structural basis of oncogenic histone H3K27M inhibition of human polycomb repressive complex 2. <i> Justin N, Zhang Y, Tarricone C, Martin SR, Chen S, Underwood E, De Marco V, Haire LF, Walker PA, Reinberg D, Wilson JR, Gamblin SJ. </i> Nat Commun, 2016","statement":[{"text":"Recombinant PRC2 was much less prone to aggregation when EZH2 was expressed in two parts (EZH2N 1–385 and EZH2C 421–746), removing the linker between the end of MCSS and the beginning of SANT2, thus 28 residues are missing from the middle lobe as indicated in Fig. 1d.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":346,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-16T15:02:51.754Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5HYN"}],"reference_id":"27121947","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92833"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P68431"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15022"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75530"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":514,"region_id":"DP01817r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis of oncogenic histone H3K27M inhibition of human polycomb repressive complex 2. <i> Justin N, Zhang Y, Tarricone C, Martin SR, Chen S, Underwood E, De Marco V, Haire LF, Walker PA, Reinberg D, Wilson JR, Gamblin SJ. </i> Nat Commun, 2016","statement":[{"text":"This region are missing in two different x-ray experiments","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"amonzon","start":480,"term_ontology":"IDPO","curator_name":"Alex Monzon","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5HYN"}],"reference_id":"27121947","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-16T15:05:07.093Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":746,"region_id":"DP01817r005","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Structure of the catalytic domain of EZH2 reveals conformational plasticity in cofactor and substrate binding sites and explains oncogenic mutations. <i> Wu H, Zeng H, Dong A, Li F, He H, Senisterra G, Seitova A, Duan S, Brown PJ, Vedadi M, Arrowsmith CH, Schapira M. </i> PLoS One, 2013","statement":[{"text":"However, the 17 C-terminal residues including most of the post-SET domain were not observed.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":730,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-16T15:10:08.014Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4MI0"}],"reference_id":"24367611","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":210,"region_id":"DP01817r006","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Structural basis of oncogenic histone H3K27M inhibition of human polycomb repressive complex 2. <i> Justin N, Zhang Y, Tarricone C, Martin SR, Chen S, Underwood E, De Marco V, Haire LF, Walker PA, Reinberg D, Wilson JR, Gamblin SJ. </i> Nat Commun, 2016","statement":[{"text":"This region lacks electron density in the PDB structure of the Human Polycomb Repressive Complex 2 (PRC2) with oncogenic histone H3K27M peptide, indicating it is disordered.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":183,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-16T15:05:48.620Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5HYN"}],"reference_id":"27121947","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75530"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15022"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P68431"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92833"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":746,"region_id":"DP01817r007","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Structural context of disease-associated mutations and putative mechanism of autoinhibition revealed by X-ray crystallographic analysis of the EZH2-SET domain. <i> Antonysamy S, Condon B, Druzina Z, Bonanno JB, Gheyi T, Zhang F, MacEwan I, Zhang A, Ashok S, Rodgers L, Russell M, Gately Luz J. </i> PLoS One, 2013","statement":[{"text":"The final model consisted of one EZH2-SET domain (chain A) containing a total of 209 residues, 6 zinc atoms, 159 water molecules, and 1 sulfate ion. 96.6% of residues are in the most favored region of the Ramachandran plot, and 100% are in the allowed region. The C-terminal residues 737-751 are disordered. Due to lack of representative electron density, internal residues 598-603 and the side chain atoms of residues Q559, D597, V604, K616, D625, K661, D664, K665, and M667 were omitted.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":732,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-16T15:12:36.922Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4MI5"}],"reference_id":"24367637","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":746,"region_id":"DP01817r008","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Structural basis of oncogenic histone H3K27M inhibition of human polycomb repressive complex 2. <i> Justin N, Zhang Y, Tarricone C, Martin SR, Chen S, Underwood E, De Marco V, Haire LF, Walker PA, Reinberg D, Wilson JR, Gamblin SJ. </i> Nat Commun, 2016","statement":[{"text":"In the isolated structure, residues 727–729 partially fold into the substrate-binding channel and thereafter the chain is disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":733,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-16T14:55:08.540Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5HYN"}],"reference_id":"27121947","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92833"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P68431"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15022 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75530"}]},{"start":386,"end":420,"reference_id":"27121947","reference_source":"pmid","reference_html":"Structural basis of oncogenic histone H3K27M inhibition of human polycomb repressive complex 2. <i> Justin N, Zhang Y, Tarricone C, Martin SR, Chen S, Underwood E, De Marco V, Haire LF, Walker PA, Reinberg D, Wilson JR, Gamblin SJ. </i> Nat Commun, 2016","date":"2023-11-28T13:50:18.772Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"5HYN"}],"region_id":"DP01817r009","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92833"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P68431"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15022"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75530"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"}],"statement":[{"text":"Recombinant PRC2 was much less prone to aggregation when EZH2 was expressed in two parts (EZH2N 1–385 and EZH2C 421–746), removing the linker between the end of MCSS and the beginning of SANT2, thus 28 residues are missing from the middle lobe as indicated in Fig. 1d.","type":"Methods"}]},{"start":1,"end":10,"reference_id":"27121947","reference_source":"pmid","reference_html":"Structural basis of oncogenic histone H3K27M inhibition of human polycomb repressive complex 2. <i> Justin N, Zhang Y, Tarricone C, Martin SR, Chen S, Underwood E, De Marco V, Haire LF, Walker PA, Reinberg D, Wilson JR, Gamblin SJ. </i> Nat Commun, 2016","date":"2023-11-28T13:49:02.523Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"5HYN"}],"region_id":"DP01817r010","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92833"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P68431"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15022"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75530"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"}],"statement":[{"text":"This region lacks electron density in the PDB structure of the Human Polycomb Repressive Complex 2 (PRC2) with oncogenic histone H3K27M peptide, indicating it is disordered.","type":"Curator statement"}]},{"start":480,"end":514,"reference_id":"33479123","reference_source":"pmid","reference_html":"JARID2 and AEBP2 regulate PRC2 in the presence of H2AK119ub1 and other histone modifications.  <i> Kasinath V, Beck C, Sauer P, Poepsel S, Kosmatka J, Faini M, Toso D, Aebersold R, Nogales E. </i> Science, 2021","date":"2024-03-25T17:31:47.176Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00429","term_name":"dimethylated residue","term_namespace":"Protein modification","start":509,"end":509,"position":"Specific residue","statements":[{"type":"Results","text":"The region includes lysines K509\nand K510 within the IQLKK motif of EZH2,\nwhich had been predicted to be disordered\nand had been shown to be modified during\nPRC2 automethylation (25, 26). Mass spectrometry\nanalysis of our PRC2-AJ1-450 sample\nconfirms the presence of dimethylation of\nboth K509 and K510."}]},{"term_id":"MOD:00429","term_name":"dimethylated residue","term_namespace":"Protein modification","start":510,"end":510,"position":"Specific residue","statements":[{"type":"Results","text":"The region includes lysines K509\nand K510 within the IQLKK motif of EZH2,\nwhich had been predicted to be disordered\nand had been shown to be modified during\nPRC2 automethylation (25, 26). Mass spectrometry\nanalysis of our PRC2-AJ1-450 sample\nconfirms the presence of dimethylation of\nboth K509 and K510."}]}],"cross_refs":[{"db":"EMDB","id":"EMD-21707"},{"db":"PDB","id":"6WKR"}],"region_id":"DP01817r011","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0CG48"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15022"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75530"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09028"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92833"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6ZN18"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84233"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62799"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06897"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02281"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16680","entry_name":"S-adenosyl-L-homocysteine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"sequence_construct":"MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEWKQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPAPAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP","statement":[{"text":"When bound to substrate nucleosome, the amino-acids-497-to-511 segment in EZH2 forms an alpha helix that is sandwiched between the nucleosomal DNA, the EZH2 (SET) domain, and the H3 tail, which we therefore call the EZH2 bridge helix (Fig. 2A). Its tripartite interaction results in the stabilization of this EZH2 region that has otherwise been unstructured or highly flexible in previous structural studies of PRC2 lacking nucleosome substrate (22, 27, 28).","type":"Article"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-25T18:22:58.100Z"}},{"start":487,"end":513,"reference_id":"33479123","reference_source":"pmid","reference_html":"JARID2 and AEBP2 regulate PRC2 in the presence of H2AK119ub1 and other histone modifications.  <i> Kasinath V, Beck C, Sauer P, Poepsel S, Kosmatka J, Faini M, Toso D, Aebersold R, Nogales E. </i> Science, 2021","date":"2024-03-25T15:39:10.195Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"GO:0031491","term_name":"nucleosome binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00429","term_name":"dimethylated residue","term_namespace":"Protein modification","start":509,"end":509,"position":"Specific residue","statements":[{"type":"Article","text":"The region includes lysines K509\nand K510 within the IQLKK motif of EZH2,\nwhich had been predicted to be disordered\nand had been shown to be modified during\nPRC2 automethylation (25, 26). Mass spectrometry\nanalysis of our PRC2-AJ1-450 sample\nconfirms the presence of dimethylation of\nboth K509 and K510."}]},{"term_id":"MOD:00429","term_name":"dimethylated residue","term_namespace":"Protein modification","start":510,"end":510,"position":"Specific residue","statements":[{"type":"Article","text":"The region includes lysines K509\nand K510 within the IQLKK motif of EZH2,\nwhich had been predicted to be disordered\nand had been shown to be modified during\nPRC2 automethylation (25, 26). Mass spectrometry\nanalysis of our PRC2-AJ1-450 sample\nconfirms the presence of dimethylation of\nboth K509 and K510."}]}],"cross_refs":[{"db":"EMDB","id":"EMD-21707"},{"db":"PDB","id":"6WKR"}],"ec_go":"IDA","region_id":"DP01817r012","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0CG48"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15022"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75530"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09028"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92833"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6ZN18"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84233"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62799"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06897"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02281"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16680","entry_name":"S-adenosyl-L-homocysteine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"sequence_construct":"MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEWKQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPAPAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP","statement":[{"text":"In the present structure, we have identified and modeled a region of EZH2 rich in lysines and arginines (amino acids 487 to 513) that interacts extensively with the nucleosomal DNA.","type":"Article"}],"term_comment":"","term_def":"\"Binding to a nucleosome, a complex comprised of DNA wound around a multisubunit core and associated proteins, which forms the primary packing unit of DNA into higher order structures.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-25T16:13:07.955Z"}},{"start":507,"end":511,"reference_id":"33479123","reference_source":"pmid","reference_html":"JARID2 and AEBP2 regulate PRC2 in the presence of H2AK119ub1 and other histone modifications. <i> Kasinath V, Beck C, Sauer P, Poepsel S, Kosmatka J, Faini M, Toso D, Aebersold R, Nogales E. </i> Science, 2021","date":"2024-03-25T15:38:20.404Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000042","term_name":"methylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001582","ec_ontology":"ECO","ec_name":"liquid chromatography coupled with tandem mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-21707"},{"db":"PDB","id":"6WKR"}],"region_id":"DP01817r013","statement":[{"text":"The region includes lysines K509 and K510 within the IQLKK motif of EZH2, which had been predicted to be disordered and had been shown to be modified during PRC2 automethylation (25, 26). Mass spectrometry analysis of our PRC2-AJ1–450 sample confirms the presence of dimethylation of both K509 and K510.","type":"Article"}],"construct_alterations":[{"term_id":"MOD:00429","term_name":"dimethylated residue","term_namespace":"Protein modification","start":509,"end":509,"position":"Specific residue","statements":[{"type":"Article","text":"The region includes lysines K509 and K510 within the IQLKK motif of EZH2, which had been predicted to be disordered and had been shown to be modified during PRC2 automethylation (25, 26). Mass spectrometry analysis of our PRC2-AJ1-450 sample confirms the presence of dimethylation of both K509 and K510."}]},{"term_id":"MOD:00429","term_name":"dimethylated residue","term_namespace":"Protein modification","start":510,"end":510,"position":"Specific residue","statements":[{"type":"Article","text":"The region includes lysines K509 and K510 within the IQLKK motif of EZH2, which had been predicted to be disordered and had been shown to be modified during PRC2 automethylation (25, 26). Mass spectrometry analysis of our PRC2-AJ1-450 sample confirms the presence of dimethylation of both K509 and K510."}]}],"sequence_construct":"MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEWKQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPAPAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-25T16:13:34.254Z"}},{"start":497,"end":513,"reference_id":"33479123","reference_source":"pmid","reference_html":"JARID2 and AEBP2 regulate PRC2 in the presence of H2AK119ub1 and other histone modifications. <i> Kasinath V, Beck C, Sauer P, Poepsel S, Kosmatka J, Faini M, Toso D, Aebersold R, Nogales E. </i> Science, 2021","date":"2024-03-27T10:30:07.076Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"GO:0042393","term_name":"histone binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00429","term_name":"dimethylated residue","term_namespace":"Protein modification","start":509,"end":509,"position":"Specific residue"},{"term_id":"MOD:00429","term_name":"dimethylated residue","term_namespace":"Protein modification","start":510,"end":510,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"6WKR"},{"db":"EMDB","id":"EMD-21707"}],"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P84233","operator":null,"partner_start":22,"partner_end":41}],"region_id":"DP01817r015","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0CG48"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15022"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75530"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09028"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92833"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6ZN18"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84233"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62799"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06897"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02281"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16680","entry_name":"S-adenosyl-L-homocysteine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"}],"sequence_construct":"MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEWKQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPAPAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP","statement":[{"text":"Fig. 2 Interaction of EZH2 with the histone H3 tail and nucleosomal DNA.\n(A) (Top) Cartoon representation of the newly defined EZH2 bridge helix (amino acids 497 to 513) that interacts with nucleosomal DNA and the H3 tail. (Left) Cryo-EM structure of the PRC2-AEBP2-JARID2 complex bound to an H2AK119ub1-containing nucleosome. The zoom out shows the bridge helix, with residues interacting with the EZH2 (SET) domain, nucleosomal DNA, and the histone tail depicted in stick representation. (Right) Helix wheel diagram for the bridge helix that shows the distribution of positively charged residues on the nucleosomal DNA interacting face (cyan), positive and hydrophobic residues on the EZH2 (SET) interacting face (blue), and the residues interacting with the backbone of the H3 tail (pink). aa, amino acids.","type":"Figure"},{"text":"(B) (Left) Density map of the histone H3 tail (amino acids 21 to 40) (contour level:0.024) with the corresponding atomic model.","type":"Figure"}],"term_comment":"","term_def":"\"Binding to a histone, any of a group of water-soluble proteins found in association with the DNA of eukaroytic chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in nonspecific suppression of gene activity.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-03T16:30:40.828Z"}},{"start":340,"end":435,"reference_id":"35682829","reference_source":"pmid","reference_html":"The Disordered EZH2 Loop: Atomic Level Characterization by <sup>1</sup>H<sup>N</sup>- and <sup>1</sup>H<sup>α</sup>-Detected NMR Approaches, Interaction with the Long Noncoding HOTAIR RNA. <i> Szabó CL, Szabó B, Sebák F, Bermel W, Tantos A, Bodor A. </i> Int J Mol Sci, 2022","date":"2024-04-05T08:03:08.478Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"BMRB","id":"51420"}],"region_id":"DP01817r016","sequence_construct":"MDAERIKTPPKRPGGRRRGRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGALEHHHHHH","statement":[{"text":"As\na result of the successful resonance assignment, the obtained chemical shift values indicate the\nhighly disordered nature of the EZH2 loop, with some nascent helical tendency in the Ser407–Ser412\nregion.","type":"Abstract"},{"text":"The signal dispersion of both 1HN and 1Hα dimensions is only ca. 1 ppm (Figure 2a,b), indicating a similar chemical environment for each residue (Figure 2b). This is already indicative of a protein without any defined structure.","type":"Results"},{"text":"Results show that the two predictors give a similar picture (Figure 3 and Figure S3a,b), with SCS values close to 0.0, and no expanded constant sign tendencies are observed. The only exception is the Ser407–Ser412 segment with a helical tendency, although, even in this case, SCS values are below 0.6 ppm. This suggests a highly disordered random coil nature with a short nascent helical motif at Ser407–Ser412.","type":"Results"},{"text":"Analysis of the determined chemical shifts experimentally proved the highly disordered\nbehavior of the EZH2 loop. An α-helical tendency is observed in the Ser408–Ser412\nregion, and the high disorder is maintained over a large temperature range. This lack of\ntransient structural elements is relatively uncommon even amongst IDPs. EZH2 maintains\nits highly disordered state even when bound to RNA, and the nascent helical region does\nnot play any role in the interaction.","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-06T15:09:26.769Z"}},{"start":367,"end":375,"reference_id":"35682829","reference_source":"pmid","reference_html":"The Disordered EZH2 Loop: Atomic Level Characterization by <sup>1</sup>H<sup>N</sup>- and <sup>1</sup>H<sup>α</sup>-Detected NMR Approaches, Interaction with the Long Noncoding HOTAIR RNA. <i> Szabó CL, Szabó B, Sebák F, Bermel W, Tantos A, Bodor A. </i> Int J Mol Sci, 2022","date":"2024-04-05T08:20:58.551Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"ec_go":"EXP","interaction_partner":[{"db":"Ensembl","id":"ENSG00000228630","operator":null,"partner_start":1,"partner_end":140}],"region_id":"DP01817r017","sequence_construct":"MDAERIKTPPKRPGGRRRGRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGALEHHHHHH","statement":[{"text":"The interaction and determination of the binding sites on the EZH2 loop was monitored by chemical shift mapping in the absence and presence of Mg2+. In both cases, the same result is obtained: the addition of RNA causes significant chemical shift perturbations in the Thr367–Ser375 region (Figure 5).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-06T15:09:53.365Z"}}],"released":"2018_11","uniref100":"UniRef100_Q15910","date":"2018-08-10T13:08:19.000Z","acc":"Q15910","name":"Histone-lysine N-methyltransferase EZH2","length":746,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins","RNA-binding proteins"],"UniParc":"UPI000016B348","genes":[{"name":{"value":"EZH2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:3527","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:3527"}}]},"synonyms":[{"value":"KMT6"}]}],"alphafold_very_low_content":0.2131367292225201,"disorder_content":0.24932975871313673,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"},{"start":183,"end":210,"type":"D"},{"start":340,"end":435,"type":"D"},{"start":480,"end":514,"type":"T"},{"start":730,"end":746,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":183,"end":210,"type":"D"},{"start":340,"end":435,"type":"D"},{"start":480,"end":514,"type":"D"},{"start":730,"end":746,"type":"D"}],"Disorder function":[{"start":386,"end":420,"type":"F"},{"start":507,"end":511,"type":"F"}],"Structural transition":[{"start":480,"end":514,"type":"T"}],"Molecular function":[{"start":367,"end":375,"type":"F"},{"start":487,"end":513,"type":"F"}]}},{"features":{"pfam":[{"id":"PF09770","name":"Topoisomerase II-associated protein PAT1","start":3,"end":55},{"id":"PF09770","name":"Topoisomerase II-associated protein PAT1","start":257,"end":742}]},"uniref50":"UniRef50_P25644","sequence":"MSFFGLENSGNARDGPLDFEESYKGYGEHELEENDYLNDETFGDNVQVGTDFDFGNPHSSGSSGNAIGGNGVGATARSYVAATAEGISGPRTDGTAAAGPLDLKPMESLWSTAPPPAMAPSPQSTMAPAPAPQQMAPLQPILSMQDLERQQRQMQQQFMNFHAMGHPQGLPQGPPQQQFPMQPASGQPGPSQFAPPPPPPGVNVNMNQMPMGPVQVPVQASPSPIGMSNTPSPGPVVGATKMPLQSGRRSKRDLSPEEQRRLQIRHAKVEKILKYSGLMTPRDKDFITRYQLSQIVTEDPYNEDFYFQVYKIIQRGGITSESNKGLIARAYLEHSGHRLGGRYKRTDIALQRMQSQVEKAVTVAKERPSKLKDQQAAAGNSSQDNKQANTVLGKISSTLNSKNPRRQLQIPRQQPSDPDALKDVTDSLTNVDLASSGSSSTGSSAAAVASKQRRRSSYAFNNGNGATNLNKSGGKKFILELIETVYEEILDLEANLRNGQQTDSTAMWEALHIDDSSYDVNPFISMLSFDKGIKIMPRIFNFLDKQQKLKILQKIFNELSHLQIIILSSYKTTPKPTLTQLKKVDLFQMIILKIIVSFLSNNSNFIEIMGLLLQLIRNNNVSFLTTSKIGLNLITILISRAALIKQDSSRSNILSSPEISTWNEIYDKLFTSLESKIQLIFPPREYNDHIMRLQNDKFMDEAYIWQFLASLALSGKLNHQRIIIDEVRDEIFATINEAETLQKKEKELSVLPQRSQELDTELKSIIYNKEKLYQDLNLFLNVMGLVYRDGEISELK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P25644","disprot_id":"DP01825","ncbi_taxon_id":559292,"regions_counter":3,"creator":"amonzon","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":469,"region_id":"DP01825r001","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Lsm2 and Lsm3 bridge the interaction of the Lsm1-7 complex with Pat1 for decapping activation. <i> Wu D, Muhlrad D, Bowler MW, Jiang S, Liu Z, Parker R, Song H. </i> Cell Res, 2014","statement":[{"text":" Some residues are not visible in the electron density map and assumed to be disordered. These include residues 81-89 in chains A and B, residues 49-55 and 94-95 in chain C, residues 50-58 and 94-95 in chain D, residues 48-59 and 81-89 in chain E, residues 53-56 and 80-89 in chain F, residues 49-55 and 94-95 in chain G, residues 422-469, 751-757 and 795-796 in chains H, I and J, respectively, and residue 794 in chain I.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":422,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-12-12T18:15:00.768Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4N0A"}],"reference_id":"24247251","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P38203"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P57743"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-15T09:34:32.339Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":24,"region_id":"DP01825r002","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Structural analysis of the yeast Dhh1-Pat1 complex reveals how Dhh1 engages Pat1, Edc3 and RNA in mutually exclusive interactions. <i> Sharif H, Ozgur S, Sharma K, Basquin C, Urlaub H, Conti E. </i> Nucleic Acids Res, 2013","statement":[{"text":"No ordered electron density was present for residues 5–24 and 55–79 of Pat1, consistent with the results from the binding assays (Figure 1B, D and Supplementary Figure S1).","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":5,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-12-12T18:10:31.810Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4BRW"}],"reference_id":"23851565","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P39517"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:62551"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5288834"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-15T09:37:06.336Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":79,"region_id":"DP01825r003","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Structural analysis of the yeast Dhh1-Pat1 complex reveals how Dhh1 engages Pat1, Edc3 and RNA in mutually exclusive interactions. <i> Sharif H, Ozgur S, Sharma K, Basquin C, Urlaub H, Conti E. </i> Nucleic Acids Res, 2013","statement":[{"text":"No ordered electron density was present for residues 5–24 and 55–79 of Pat1, consistent with the results from the binding assays (Figure 1B, D and Supplementary Figure S1).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":55,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-12-12T18:09:19.379Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4BRW"}],"reference_id":"23851565","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P39517 "},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:62551"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5288834"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-15T09:37:13.027Z"}}],"released":"2018_11","uniref100":"UniRef100_P25644","date":"2018-08-10T14:38:14.000Z","acc":"P25644","name":"DNA topoisomerase 2-associated protein PAT1","length":796,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":["Condensates-related proteins","RNA-binding proteins"],"UniParc":"UPI00000530D6","genes":[{"name":{"value":"PAT1"},"synonyms":[{"value":"MRT1"}],"orfNames":[{"value":"YCR77C"}],"olnNames":[{"value":"YCR077C"}]}],"alphafold_very_low_content":0.3806532663316583,"disorder_content":0.11683417085427136,"disprot_consensus":{"full":[{"start":5,"end":24,"type":"D"},{"start":55,"end":79,"type":"D"},{"start":422,"end":469,"type":"D"}],"Structural state":[{"start":5,"end":24,"type":"D"},{"start":55,"end":79,"type":"D"},{"start":422,"end":469,"type":"D"}]}},{"features":{"pfam":[{"id":"PF10731","name":"Thrombin inhibitor from mosquito","start":1,"end":65}]},"uniref50":"UniRef50_O97416","sequence":"MASKLFVLAFLCLALVVVVQSAPQYARGDVPTYDEEDFDEESLKPHSSSSSDDGEEEFDPSLLEEHADAPTARDPGRNPEFLRNSNTDEQASAPAASSSESDE","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Nematocera","Culicoidea","Culicidae","Anophelinae","Anopheles"],"uniref90":"UniRef90_O97416","disprot_id":"DP01832","ncbi_taxon_id":7165,"regions_counter":7,"creator":"ppere","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":103,"region_id":"DP01832r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Functional analyses yield detailed insight into the mechanism of thrombin inhibition by the antihemostatic salivary protein cE5 from <i>Anopheles gambiae</i>. <i> Pirone L, Ripoll-Rozada J, Leone M, Ronca R, Lombardo F, Fiorentino G, Andersen JF, Pereira PJB, Arcà B, Pedone E. </i> J Biol Chem, 2017","statement":[{"text":"cE5 displayed a typical circular dichroism (CD) spectrum of an unstructured protein, with a minimum at 202 nm (Fig. 2)","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":22,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28592490","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":103,"region_id":"DP01832r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Functional analyses yield detailed insight into the mechanism of thrombin inhibition by the antihemostatic salivary protein cE5 from <i>Anopheles gambiae</i>. <i> Pirone L, Ripoll-Rozada J, Leone M, Ronca R, Lombardo F, Fiorentino G, Andersen JF, Pereira PJB, Arcà B, Pedone E. </i> J Biol Chem, 2017","statement":[{"text":"The 1H,15N HSQC spectrum of 15N- labeled cE5 showed a limited chemical shift range (Fig. 3A), indicative of an unfolded molecule having few secondary structure elements, consistent with the random-coil state suggested by CD data.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":22,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28592490","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":103,"region_id":"DP01832r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Functional analyses yield detailed insight into the mechanism of thrombin inhibition by the antihemostatic salivary protein cE5 from <i>Anopheles gambiae</i>. <i> Pirone L, Ripoll-Rozada J, Leone M, Ronca R, Lombardo F, Fiorentino G, Andersen JF, Pereira PJB, Arcà B, Pedone E. </i> J Biol Chem, 2017","statement":[{"text":"No significant density was present for the N-terminal tetrapeptide cE5(Asp-31) to cE5(Glu-34) or for the C-terminal 21 amino acids (cE5(Ser-64) to cE5(Glu-82) of the P5 fragment...","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":85,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5NHU"}],"reference_id":"28592490","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":84,"region_id":"DP01832r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Functional analyses yield detailed insight into the mechanism of thrombin inhibition by the antihemostatic salivary protein cE5 from <i>Anopheles gambiae</i>. <i> Pirone L, Ripoll-Rozada J, Leone M, Ronca R, Lombardo F, Fiorentino G, Andersen JF, Pereira PJB, Arcà B, Pedone E. </i> J Biol Chem, 2017","statement":[{"text":"...complex A comprising thrombin residues T(Ser-1E) to T(Arg-15) and T(Ile-16) to T(Gly-246) and inhibitor residues cE5(Glu-35) to cE5(Asn-63)...","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":56,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5NHU"}],"reference_id":"28592490","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":84,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Functional analyses yield detailed insight into the mechanism of thrombin inhibition by the antihemostatic salivary protein cE5 from <i>Anopheles gambiae</i>. <i> Pirone L, Ripoll-Rozada J, Leone M, Ronca R, Lombardo F, Fiorentino G, Andersen JF, Pereira PJB, Arcà B, Pedone E. </i> J Biol Chem, 2017","statement":[{"text":"In agreement with the results of CD (Fig. 2) and NMR measurements (Fig. 3), the inhibitor adopts a mostly extended conformation, running in a reverse orientation to substrates on the surface of thrombin and interacting with both the exosite I and the active-site region of the proteinase (Fig. 7, A, C, and D).","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"ppereira","start":56,"term_ontology":"IDPO","curator_name":"Pedro Pereira","reference_id":"28592490","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01832r005","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":84,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Functional analyses yield detailed insight into the mechanism of thrombin inhibition by the antihemostatic salivary protein cE5 from <i>Anopheles gambiae</i>. <i> Pirone L, Ripoll-Rozada J, Leone M, Ronca R, Lombardo F, Fiorentino G, Andersen JF, Pereira PJB, Arcà B, Pedone E. </i> J Biol Chem, 2017","statement":[{"text":"...the cE5 fragment spanning residues cE5(Glu-35) to cE5(Asp-47) blocks the exosite I of the proteinase (Figs. 4 and 7C).","type":"Results"}],"term_id":"GO:0005515","curator_id":"ppereira","start":56,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"28592490","version":3,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01832r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":84,"term_name":"molecular function inhibitor activity","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Functional analyses yield detailed insight into the mechanism of thrombin inhibition by the antihemostatic salivary protein cE5 from <i>Anopheles gambiae</i>. <i> Pirone L, Ripoll-Rozada J, Leone M, Ronca R, Lombardo F, Fiorentino G, Andersen JF, Pereira PJB, Arcà B, Pedone E. </i> J Biol Chem, 2017","statement":[{"text":"Overall, the cE5 central region represented by the P2 peptide appeared as the main responsible for both thrombin binding and inhibition.","type":"Discussion"}],"term_id":"GO:0140678","curator_id":"ppereira","start":56,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"28592490","version":3,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01832r007","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_A0A182HV03","date":"2018-08-12T14:51:28.000Z","acc":"Q7Q3R9","name":"AGAP008004-PA","length":103,"organism":"Anopheles gambiae","dataset":[],"UniParc":"UPI0000243F5F","genes":[{"name":{"value":"1277947","evidences":[{"code":"ECO:0000313","source":{"name":"EnsemblMetazoa","id":"AGAP008004-PA","url":"http://www.ensemblgenomes.org/id/AGAP008004-PA"}}]},"orfNames":[{"value":"AgaP_AGAP008004","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EAA12433.3","url":"https://www.ebi.ac.uk/ena/browser/view/EAA12433.3"}}]}]}],"alphafold_very_low_content":0.10679611650485436,"disorder_content":0.7961165048543689,"disprot_consensus":{"full":[{"start":22,"end":55,"type":"D"},{"start":56,"end":84,"type":"T"},{"start":85,"end":103,"type":"D"}],"Structural state":[{"start":22,"end":103,"type":"D"}],"Structural transition":[{"start":56,"end":84,"type":"T"}],"Molecular function":[{"start":56,"end":84,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_P85800","sequence":"SDQGDVAEPKMHKTAPPFDFEAIPEEYLDDES","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Chelicerata","Arachnida","Acari","Parasitiformes","Ixodida","Ixodoidea","Ixodidae","Amblyomminae","Amblyomma"],"uniref90":"UniRef90_P85800","disprot_id":"DP01833","ncbi_taxon_id":34610,"regions_counter":10,"creator":"ppere","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":32,"region_id":"DP01833r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Variegin, a novel fast and tight binding thrombin inhibitor from the tropical bont tick. <i> Koh CY, Kazimirova M, Trimnell A, Takac P, Labuda M, Nuttall PA, Kini RM. </i> J Biol Chem, 2007","statement":[{"text":"CD spectra of s-variegin, EP25, and AP18 are all similar to that of n-variegin, typical of random-coil proteins (supplemental Fig. S2).","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":1,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17684009","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":32,"region_id":"DP01833r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Variegin, a novel fast and tight binding thrombin inhibitor from the tropical bont tick. <i> Koh CY, Kazimirova M, Trimnell A, Takac P, Labuda M, Nuttall PA, Kini RM. </i> J Biol Chem, 2007","statement":[{"text":"CD spectra of s-variegin, EP25, and AP18 are all similar to that of n-variegin, typical of random-coil proteins (supplemental Fig. S2).","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":8,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17684009","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":32,"region_id":"DP01833r003","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Noncompetitive inhibitor of thrombin. <i> Koh CY, Kazimirova M, Nuttall PA, Kini RM. </i> Chembiochem, 2009","statement":[{"text":"To investigate how the cleavage affects the activity, MH22, s- variegin, and hirulog-1 were preincubated with thrombin for different lengths of time before determination of their residual thrombin inhibitory activities (Table 1 and Figure 2A).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":11,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19644995","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":32,"term_name":"protein binding","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","reference_html":"Noncompetitive inhibitor of thrombin. <i> Koh CY, Kazimirova M, Nuttall PA, Kini RM. </i> Chembiochem, 2009","term_id":"GO:0005515","curator_id":"ppereira","start":11,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"19644995","version":3,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","region_id":"DP01833r004","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":32,"term_name":"molecular function inhibitor activity","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","reference_html":"Noncompetitive inhibitor of thrombin. <i> Koh CY, Kazimirova M, Nuttall PA, Kini RM. </i> Chembiochem, 2009","term_id":"GO:0140678","curator_id":"ppereira","start":11,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"19644995","version":3,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","region_id":"DP01833r005","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":32,"region_id":"DP01833r006","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Variegin, a novel fast and tight binding thrombin inhibitor from the tropical bont tick. <i> Koh CY, Kazimirova M, Trimnell A, Takac P, Labuda M, Nuttall PA, Kini RM. </i> J Biol Chem, 2007","statement":[{"text":"CD spectra of s-variegin, EP25, and AP18 are all similar to that of n-variegin, typical of random-coil proteins (supplemental Fig. S2).","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":15,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17684009","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":28,"region_id":"DP01833r007","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of thrombin in complex with S-variegin: insights of a novel mechanism of inhibition and design of tunable thrombin inhibitors. <i> Koh CY, Kumar S, Kazimirova M, Nuttall PA, Radhakrishnan UP, Kim S, Jagadeeswaran P, Imamura T, Mizuguchi J, Iwanaga S, Swaminathan K, Kini RM. </i> PLoS One, 2011","statement":[{"text":"Only 17 out of the 32 residues (VHis12 to VLeu28) of s-variegin have well-defined density (Figure 1C).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":12,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3B23"}],"reference_id":"22053189","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":28,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of thrombin in complex with S-variegin: insights of a novel mechanism of inhibition and design of tunable thrombin inhibitors. <i> Koh CY, Kumar S, Kazimirova M, Nuttall PA, Radhakrishnan UP, Kim S, Jagadeeswaran P, Imamura T, Mizuguchi J, Iwanaga S, Swaminathan K, Kini RM. </i> PLoS One, 2011","statement":[{"text":"In contrast, the C-terminal fragment MH22 V(11MHKTAPPFDFEAIPEEYLDDES32) remains bound to thrombin after cleavage.","type":"Results"}],"term_id":"GO:0005515","curator_id":"ppereira","start":12,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"22053189","version":3,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01833r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":28,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of thrombin in complex with S-variegin: insights of a novel mechanism of inhibition and design of tunable thrombin inhibitors. <i> Koh CY, Kumar S, Kazimirova M, Nuttall PA, Radhakrishnan UP, Kim S, Jagadeeswaran P, Imamura T, Mizuguchi J, Iwanaga S, Swaminathan K, Kini RM. </i> PLoS One, 2011","statement":[{"text":"Only 17 out of the 32 residues (VHis12 to VLeu28) of s-variegin have well-defined density (Figure 1C).","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"ppereira","start":12,"term_ontology":"IDPO","curator_name":"Pedro Pereira","reference_id":"22053189","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01833r009","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":28,"term_name":"molecular function inhibitor activity","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of thrombin in complex with S-variegin: insights of a novel mechanism of inhibition and design of tunable thrombin inhibitors. <i> Koh CY, Kumar S, Kazimirova M, Nuttall PA, Radhakrishnan UP, Kim S, Jagadeeswaran P, Imamura T, Mizuguchi J, Iwanaga S, Swaminathan K, Kini RM. </i> PLoS One, 2011","statement":[{"text":"s-Variegin fits firmly into the canyon-like cleft extending from the thrombin active site to exosite-I.","type":"Results"}],"term_id":"GO:0140678","curator_id":"ppereira","start":12,"term_ontology":"GO","curator_name":"Pedro Pereira","reference_id":"22053189","version":3,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01833r010","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P85800","date":"2018-08-12T23:12:07.000Z","acc":"P85800","name":"Variegin","length":32,"organism":"Amblyomma variegatum","dataset":[],"UniParc":"UPI00003E75D4","genes":[],"alphafold_very_low_content":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":11,"type":"D"},{"start":12,"end":28,"type":"T"},{"start":29,"end":32,"type":"D"}],"Structural state":[{"start":1,"end":32,"type":"D"}],"Molecular function":[{"start":11,"end":32,"type":"F"}],"Structural transition":[{"start":12,"end":28,"type":"T"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_Q6F3E8","sequence":"MLKNIVLLLAAGLSGPAVLAKPKWSPLFEEATNALEARSGGHQTAVPKVSKQGLGGDFEEIPSDEIIKRALEDRSGGHQTAVPKISKQGLGGDFEEIPSDEIIERALEARSDGHQTAVPKMSKQGLGGDIEEIPSDEIIERALEARSGGHQTAVPKMSKQGLGGDSEEIPSNEIIERALEARSGGHETAVPKMSKQGLGGDFEEIPSDEIIERALQARG","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Chelicerata","Arachnida","Acari","Parasitiformes","Ixodida","Ixodoidea","Ixodidae","Amblyomminae","Amblyomma"],"uniref90":"UniRef90_Q6F3E8","disprot_id":"DP01834","ncbi_taxon_id":34610,"regions_counter":4,"creator":"ppere","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":156,"region_id":"DP01834r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Avathrin: a novel thrombin inhibitor derived from a multicopy precursor in the salivary glands of the ixodid tick, <i>Amblyomma variegatum</i>. <i> Iyer JK, Koh CY, Kazimirova M, Roller L, Jobichen C, Swaminathan K, Mizuguchi J, Iwanaga S, Nuttall PA, Chan MY, Kini RM. </i> FASEB J, 2017","term_id":"IDPO:0000002","curator_id":"ahatos","start":147,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5GIM"}],"reference_id":"28363953","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":156,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Avathrin: a novel thrombin inhibitor derived from a multicopy precursor in the salivary glands of the ixodid tick, <i>Amblyomma variegatum</i>. <i> Iyer JK, Koh CY, Kazimirova M, Roller L, Jobichen C, Swaminathan K, Mizuguchi J, Iwanaga S, Nuttall PA, Chan MY, Kini RM. </i> FASEB J, 2017","statement":[{"text":"Thus, we built 2 segments of the peptide, representing the active site binding region N terminus to the scissile bond A(5QTAVPK10) and exosite-I binding region A(19DFEEIPSDEI28) (Fig. 5A, B).","type":"Results"}],"term_id":"GO:0005515","curator_id":"ahatos","start":147,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"28363953","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01834r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":156,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Avathrin: a novel thrombin inhibitor derived from a multicopy precursor in the salivary glands of the ixodid tick, <i>Amblyomma variegatum</i>. <i> Iyer JK, Koh CY, Kazimirova M, Roller L, Jobichen C, Swaminathan K, Mizuguchi J, Iwanaga S, Nuttall PA, Chan MY, Kini RM. </i> FASEB J, 2017","term_id":"IDPO:0000011","curator_id":"ahatos","start":147,"term_ontology":"IDPO","curator_name":"András Hatos","reference_id":"28363953","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01834r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":156,"term_name":"molecular function inhibitor activity","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Avathrin: a novel thrombin inhibitor derived from a multicopy precursor in the salivary glands of the ixodid tick, <i>Amblyomma variegatum</i>. <i> Iyer JK, Koh CY, Kazimirova M, Roller L, Jobichen C, Swaminathan K, Mizuguchi J, Iwanaga S, Nuttall PA, Chan MY, Kini RM. </i> FASEB J, 2017","term_id":"GO:0140678","curator_id":"ahatos","start":147,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"28363953","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01834r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q6F3E8","date":"2018-08-12T23:54:52.000Z","acc":"Q6F3E8","name":"Uncharacterized protein avahiru","length":219,"organism":"Amblyomma variegatum","dataset":[],"UniParc":"UPI00003CEC6F","genes":[{"name":{"value":"avahiru","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAD29729.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAD29729.1"}}]}}],"alphafold_very_low_content":0.7625570776255708,"disorder_content":0.045662100456621,"disprot_consensus":{"full":[{"start":147,"end":156,"type":"T"}],"Structural state":[{"start":147,"end":156,"type":"D"}],"Molecular function":[{"start":147,"end":156,"type":"F"}],"Structural transition":[{"start":147,"end":156,"type":"T"}]}},{"features":{"pfam":[{"id":"PF05254","name":"Uncharacterised protein family (UPF0203)","start":2,"end":58}]},"uniref50":"UniRef50_O43715","sequence":"MNSVGEACTDMKREYDQCFNRWFAEKFLKGDSSGDPCTDLFKRYQQCVQKAIKEKEIPIEGLEFMGHGKEKPENSS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O43715","disprot_id":"DP01835","ncbi_taxon_id":9606,"regions_counter":1,"creator":"jlecle","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":76,"region_id":"DP01835r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural insight into the TRIAP1/PRELI-like domain family of mitochondrial phospholipid transfer complexes. <i> Miliara X, Garnett JA, Tatsuta T, Abid Ali F, Baldie H, Pérez-Dorado I, Simpson P, Yague E, Langer T, Matthews S. </i> EMBO Rep, 2015","statement":[{"text":"These were assigned to the C-terminus, and their elevated transverse 15N relaxation times, as evidenced by narrow line widths, indicate that the C-terminal region (after K53) is highly disordered and dynamic on a pico- to nanosecond timescale.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jlecle","start":54,"term_ontology":"IDPO","curator_name":"Jeremy Y Leclercq","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-0372-3277","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4XZS"}],"reference_id":"26071602","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_O43715","date":"2018-08-13T09:54:54.000Z","acc":"O43715","name":"TP53-regulated inhibitor of apoptosis 1","length":76,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000124E0B","genes":[{"name":{"value":"TRIAP1"},"synonyms":[{"value":"15E1.1"}],"orfNames":[{"value":"HSPC132"}]}],"alphafold_very_low_content":0.06578947368421052,"disorder_content":0.3026315789473684,"disprot_consensus":{"full":[{"start":54,"end":76,"type":"D"}],"Structural state":[{"start":54,"end":76,"type":"D"}]}},{"features":{"pfam":[{"id":"PF10480","name":"Beta-1 integrin binding protein","start":1,"end":200}],"gene3D":[{"start":47,"end":200,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"}]},"uniref50":"UniRef50_O14713","sequence":"MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNNNSDTCAEFRIKYVGAIEKLKLSEGKGLEGPLDLINYIDVAQQDGKLPFVPPEEEFIMGVSKYGIKVSTSDQYDVLHRHALYLIIRMVCYDDGLGAGKSLLALKTTDASNEEYSLWVYQCNSLEQAQAICKVLSTAFDSVLTSEKP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O14713","disprot_id":"DP01836","ncbi_taxon_id":9606,"regions_counter":2,"creator":"mpajkos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":59,"region_id":"DP01836r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Mechanism for KRIT1 release of ICAP1-mediated suppression of integrin activation. <i> Liu W, Draheim KM, Zhang R, Calderwood DA, Boggon TJ. </i> Mol Cell, 2013","statement":[{"text":"\"In the KRIT1-ICAP1 co-crystal structure the ICAP1 construct spans residues 49 to 200 but the first residue visible in all copies of the asymmetric unit is C60-ICAP and the final well-ordered residue is Ser193-ICAP. \"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":49,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4DX8"}],"reference_id":"23317506","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":59,"region_id":"DP01836r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Cocrystal structure of the ICAP1 PTB domain in complex with a KRIT1 peptide. <i> Liu W, Boggon TJ. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2013","statement":[{"text":"The crystal structure of  ICAP1(residues 49–200)–KRIT1(residues 170–198) has been solved. The first residue visible in the structure is C60.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":49,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4JIF"}],"reference_id":"23695561","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_O14713","date":"2018-08-13T10:46:07.000Z","acc":"O14713","name":"Integrin beta-1-binding protein 1","length":200,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012DA43","genes":[{"name":{"value":"ITGB1BP1"},"synonyms":[{"value":"ICAP1"}]}],"alphafold_very_low_content":0.16,"disorder_content":0.055,"disprot_consensus":{"full":[{"start":49,"end":59,"type":"D"}],"Structural state":[{"start":49,"end":59,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01274","name":"Malate synthase, TIM barrel domain","start":335,"end":579},{"id":"PF20656","name":"Malate synthase, N-terminal domain","start":16,"end":77},{"id":"PF20658","name":"Malate synthase G, alpha-beta insertion domain","start":158,"end":233},{"id":"PF20659","name":"Malate synthase, C-terminal","start":591,"end":695}],"gene3D":[{"start":135,"end":262,"id":"2.170.170.11","name":"Malate synthase G - maily-beta sub-domain"},{"start":588,"end":723,"id":"1.20.1220.12","name":"Malate synthase, domain III"},{"start":12,"end":582,"id":"3.20.20.360","name":"Malate synthase, domain 3"}]},"uniref50":"UniRef50_P37330","sequence":"MSQTITQSRLRIDANFKRFVDEEVLPGTGLDAAAFWRNFDEIVHDLAPENRQLLAERDRIQAALDEWHRSNPGPVKDKAAYKSFLRELGYLVPQPERVTVETTGIDSEITSQAGPQLVVPAMNARYALNAANARWGSLYDALYGSDIIPQEGAMVSGYDPQRGEQVIAWVRRFLDESLPLENGSYQDVVAFKVVDKQLRIQLKNGKETTLRTPAQFVGYRGDAAAPTCILLKNNGLHIELQIDANGRIGKDDPAHINDVIVEAAISTILDCEDSVAAVDAEDKILLYRNLLGLMQGTLQEKMEKNGRQIVRKLNDDRHYTAADGSEISLHGRSLLFIRNVGHLMTIPVIWDSEGNEIPEGILDGVMTGAIALYDLKVQKNSRTGSVYIVKPKMHGPQEVAFANKLFTRIETMLGMAPNTLKMGIMDEERRTSLNLRSCIAQARNRVAFINTGFLDRTGDEMHSVMEAGPMLRKNQMKSTPWIKAYERNNVLSGLFCGLRGKAQIGKGMWAMPDLMADMYSQKGDQLRAGANTAWVPSPTAATLHALHYHQTNVQSVQANIAQTEFNAEFEPLLDDLLTIPVAENANWSAQEIQQELDNNVQGILGYVVRWVEQGIGCSKVPDIHNVALMEDRATLRISSQHIANWLRHGILTKEQVQASLENMAKVVDQQNAGDPAYRPMAGNFANSCAFKAASDLIFLGVKQPNGYTEPLLHAWRLREKESH","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P37330","disprot_id":"DP01837","ncbi_taxon_id":83333,"regions_counter":1,"creator":"lalvarez","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":310,"region_id":"DP01837r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of Escherichia coli malate synthase G complexed with magnesium and glyoxylate at 2.0 A resolution: mechanistic implications. <i> Howard BR, Endrizzi JA, Remington SJ. </i> Biochemistry, 2000","statement":[{"text":"This includes residues 3-722 with the exception of a surface loop from 300 to 310 for which the electron density is weak and essentially uninterpretable","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"lalvarez","start":300,"term_ontology":"IDPO","curator_name":"Lucía Álvarez","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-1437-5773","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1D8C"}],"reference_id":"10715138","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P37330","date":"2018-08-13T10:48:19.000Z","acc":"P37330","name":"Malate synthase G","length":723,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI000012EBE6","genes":[{"name":{"value":"glcB","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00641","url":"https://hamap.expasy.org/unirule/MF_00641"}}]},"synonyms":[{"value":"glc"}],"olnNames":[{"value":"b2976"},{"value":"JW2943"}]}],"alphafold_very_low_content":0,"disorder_content":0.015214384508990318,"disprot_consensus":{"full":[{"start":300,"end":310,"type":"D"}],"Structural state":[{"start":300,"end":310,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00159","name":"Pancreatic hormone peptide","start":2,"end":36}]},"uniref50":"UniRef50_P68004","sequence":"YPAKPEAPGEDASPEELSRYYASLRHYLNLVTRQRY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Suina","Suidae","Sus"],"uniref90":"UniRef90_P68004","disprot_id":"DP01838","ncbi_taxon_id":9823,"regions_counter":1,"creator":"lalvarez","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":13,"region_id":"DP01838r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural similarities of micelle-bound peptide YY (PYY) and neuropeptide Y (NPY) are related to their affinity profiles at the Y receptors. <i> Lerch M, Mayrhofer M, Zerbe O. </i> J Mol Biol, 2004","statement":[{"text":"\"The N terminus is unstructured. \"\n\"Two features are immediately obvious from the data: first, signal attenuations are very small for the N-terminal, unstructured segment. \"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"lalvarez","start":1,"term_ontology":"IDPO","curator_name":"Lucía Álvarez","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-1437-5773","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1RU5"}],"reference_id":"15178255","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P68004","date":"2018-08-13T11:14:54.000Z","acc":"P68005","name":"Peptide YY","length":36,"organism":"Sus scrofa","dataset":[],"UniParc":"UPI00000351BA","genes":[{"name":{"value":"PYY"}}],"alphafold_very_low_content":0,"disorder_content":0.3611111111111111,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"D"}],"Structural state":[{"start":1,"end":13,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00400","name":"WD domain, G-beta repeat","start":101,"end":137},{"id":"PF00400","name":"WD domain, G-beta repeat","start":247,"end":286},{"id":"PF07304","name":"Steroid receptor RNA activator (SRA1)","start":1138,"end":1266},{"id":"PF11549","name":"Protein transport protein SEC31","start":902,"end":945},{"id":"PF12931","name":"Sec16 Sec23-binding domain","start":514,"end":679}],"gene3D":[{"start":1,"end":331,"id":"2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"},{"start":508,"end":746,"id":"1.25.40.980","name":"1.25.40.980"},{"start":1168,"end":1272,"id":"1.20.940.10","name":"Functional domain of the splicing factor Prp18"},{"start":369,"end":413,"id":"2.20.25.400","name":"2.20.25.400"}]},"uniref50":"UniRef50_P38968","sequence":"MVKLAEFSRTATFAWSHDKIPLLVSGTVSGTVDANFSTDSSLELWSLLAADSEKPIASLQVDSKFNDLDWSHNNKIIAGALDNGSLELYSTNEANNAINSMARFSNHSSSVKTVKFNAKQDNVLASGGNNGEIFIWDMNKCTESPSNYTPLTPGQSMSSVDEVISLAWNQSLAHVFASAGSSNFASIWDLKAKKEVIHLSYTSPNSGIKQQLSVVEWHPKNSTRVATATGSDNDPSILIWDLRNANTPLQTLNQGHQKGILSLDWCHQDEHLLLSSGRDNTVLLWNPESAEQLSQFPARGNWCFKTKFAPEAPDLFACASFDNKIEVQTLQNLTNTLDEQETETKQQESETDFWNNVSREESKEKPTVFHLQAPTWYGEPSPAAHWAFGGKLVQITPDGKGVSITNPKISGLESNTTLSEALKTKDFKPLINQRLVKVIDDVNEEDWNLLEKLSMDGTEEFLKEALAFDNDESDAQDDANNEKEDDGEEFFQQIETNFQPEGDFSLSGNIEQTISKNLVSGNIKSAVKNSLENDLLMEAMVIALDSNNERLKESVKNAYFAKYGSKSSLSRILYSISKREVDDLVENLDVSQWKFISKAIQNLYPNDIAQRNEMLIKLGDRLKENGHRQDSLTLYLAAGSLDKVASIWLSEFPDLEDKLKKDNKTIYEAHSECLTEFIERFTVFSNFINGSSTINNEQLIAKFLEFINLTTSTGNFELATEFLNSLPSDNEEVKTEKARVLIASGKSLPAQNPATATTSKAKYTNAKTNKNVPVLPTPGMPSTTSIPSMQAPFYGMTPGASANALPPKPYVPATTTSAPVHTEGKYAPPSQPSMASPFVNKTNSSTRLNSFAPPPNPYATATVPATNVSTTSIPQNTFAPIQPGMPIMGDYNAQSSSIPSQPPINAVSGQTPHLNRKANDGWNDLPLKVKEKPSRAKAVSVAPPNILSTPTPLNGIPANAASTMPPPPLSRAPSSVSMVSPPPLHKNSRVPSLVATSESPRASISNPYAPPQSSQQFPIGTISTANQTSNTAQVASSNPYAPPPQQRVATPLSGGVPPAPLPKASNPYAPTATTQPNGSSYPPTGPYTNNHTMTSPPPVFNKPPTGPPPISMKKRSNKLASIEQNPSQGATYPPTLSSSASPLQPSQPPTLASQVNTSAENVSHEIPADQQPIVDFLKEELARVTPLTPKEYSKQLKDCDKRLKILFYHLEKQDLLTQPTIDCLHDLVALMKEKKYKEAMVIHANIATNHAQEGGNWLTGVKRLIGIAEATLN","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P38968","disprot_id":"DP01840","ncbi_taxon_id":559292,"regions_counter":1,"creator":"lalvarez","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1100,"region_id":"DP01840r001","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Structure and organization of coat proteins in the COPII cage. <i> Fath S, Mancias JD, Bi X, Goldberg J. </i> Cell, 2007","statement":[{"text":"The low sequence complexity of the prolinerich segment and its sensitivity to proteolysis suggest that this region is largely unstructured and forms a flexible linker to the terminal a-solenoid and that the 55K region projects in toward the membrane to engage Sec23/24 (via a portion of the proline-rich segment)","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"lalvarez","start":770,"term_ontology":"IDPO","curator_name":"Lucía Álvarez","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-1437-5773","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4BZJ"}],"reference_id":"17604721","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P38968","date":"2018-08-13T11:40:09.000Z","acc":"P38968","name":"Protein transport protein SEC31","length":1273,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI00001689F0","genes":[{"name":{"value":"SEC31"},"synonyms":[{"value":"WEB1"}],"orfNames":[{"value":"D1229"}],"olnNames":[{"value":"YDL195W"}]}],"alphafold_very_low_content":0.3401413982717989,"disorder_content":0.26001571091908876,"disprot_consensus":{"full":[{"start":770,"end":1100,"type":"D"}],"Structural state":[{"start":770,"end":1100,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00357","name":"Integrin alpha cytoplasmic region","start":1020,"end":1033},{"id":"PF01839","name":"FG-GAP repeat","start":320,"end":362},{"id":"PF01839","name":"FG-GAP repeat","start":387,"end":423},{"id":"PF08441","name":"Integrin alpha Ig-like domain 1","start":481,"end":631},{"id":"PF20805","name":"Integrin alpha Ig-like domain 2","start":633,"end":773},{"id":"PF20806","name":"Integrin alpha Ig-like domain 3","start":779,"end":987}],"gene3D":[{"start":32,"end":485,"id":"2.130.10.130","name":"Integrin alpha, N-terminal"},{"start":990,"end":1039,"id":"1.20.5.930","name":"Bicelle-embedded integrin alpha(iib) transmembrane segment"},{"start":486,"end":636,"id":"2.60.40.1460","name":"Integrin domains. Chain A, domain 2"},{"start":637,"end":776,"id":"2.60.40.1510","name":"ntegrin, alpha v. Chain A, domain 3"}]},"uniref50":"UniRef50_P08514","sequence":"MARALCPLQALWLLEWVLLLLGPCAAPPAWALNLDPVQLTFYAGPNGSQFGFSLDFHKDSHGRVAIVVGAPRTLGPSQEETGGVFLCPWRAEGGQCPSLLFDLRDETRNVGSQTLQTFKARQGLGASVVSWSDVIVACAPWQHWNVLEKTEEAEKTPVGSCFLAQPESGRRAEYSPCRGNTLSRIYVENDFSWDKRYCEAGFSSVVTQAGELVLGAPGGYYFLGLLAQAPVADIFSSYRPGILLWHVSSQSLSFDSSNPEYFDGYWGYSVAVGEFDGDLNTTEYVVGAPTWSWTLGAVEILDSYYQRLHRLRGEQMASYFGHSVAVTDVNGDGRHDLLVGAPLYMESRADRKLAEVGRVYLFLQPRGPHALGAPSLLLTGTQLYGRFGSAIAPLGDLDRDGYNDIAVAAPYGGPSGRGQVLVFLGQSEGLRSRPSQVLDSPFPTGSAFGFSLRGAVDIDDNGYPDLIVGAYGANQVAVYRAQPVVKASVQLLVQDSLNPAVKSCVLPQTKTPVSCFNIQMCVGATGHNIPQKLSLNAELQLDRQKPRQGRRVLLLGSQQAGTTLNLDLGGKHSPICHTTMAFLRDEADFRDKLSPIVLSLNVSLPPTEAGMAPAVVLHGDTHVQEQTRIVLDCGEDDVCVPQLQLTASVTGSPLLVGADNVLELQMDAANEGEGAYEAELAVHLPQGAHYMRALSNVEGFERLICNQKKENETRVVLCELGNPMKKNAQIGIAMLVSVGNLEEAGESVSFQLQIRSKNSQNPNSKIVLLDVPVRAEAQVELRGNSFPASLVVAAEEGEREQNSLDSWGPKVEHTYELHNNGPGTVNGLHLSIHLPGQSQPSDLLYILDIQPQGGLQCFPQPPVNPLKVDWGLPIPSPSPIHPAHHKRDRRQIFLPEPEQPSRLQDPVLVSCDSAPCTVVQCDLQEMARGQRAMVTVLAFLWLPSLYQRPLDQFVLQSHAWFNVSSLPYAVPPLSLPRGEAQVWTQLLRALEERAIPIWWVLVGVLGGLLLLTILVLAMWKVGFFKRNRPPLEEDDEEGE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P08514","disprot_id":"DP01841","ncbi_taxon_id":9606,"regions_counter":3,"creator":"tszani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1039,"region_id":"DP01841r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR analysis of structure and dynamics of the cytosolic tails of integrin alpha IIb beta 3 in aqueous solution. <i> Ulmer TS, Yaspan B, Ginsberg MH, Campbell ID. </i> Biochemistry, 2001","term_id":"IDPO:0000002","curator_id":"tszani","start":989,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"11412103","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1039,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"NMR analysis of structure and dynamics of the cytosolic tails of integrin alpha IIb beta 3 in aqueous solution. <i> Ulmer TS, Yaspan B, Ginsberg MH, Campbell ID. </i> Biochemistry, 2001","term_id":"GO:0060090","curator_id":"tszani","start":989,"term_ontology":"GO","curator_name":"Tamás Szaniszló","reference_id":"11412103","version":3,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01841r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1008,"region_id":"DP01841r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of an integrin alphaIIb beta3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activation. <i> Yang J, Ma YQ, Page RC, Misra S, Plow EF, Qin J. </i> Proc Natl Acad Sci U S A, 2009","statement":[{"text":"The C terminus of αIIb (R997-E1008) is rich in acidic residues and largely unstructured, as was observed previously","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"tszani","start":997,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19805198","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P08514","date":"2018-08-13T12:36:07.000Z","acc":"P08514","name":"Integrin alpha-IIb","length":1039,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000153B72","genes":[{"name":{"value":"ITGA2B"},"synonyms":[{"value":"GP2B"},{"value":"ITGAB"}]}],"alphafold_very_low_content":0.07699711260827719,"disorder_content":0.04908565928777671,"disprot_consensus":{"full":[{"start":989,"end":1039,"type":"D"}],"Structural state":[{"start":989,"end":1039,"type":"D"}],"Molecular function":[{"start":989,"end":1039,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00362","name":"Integrin beta chain VWA domain","start":134,"end":381},{"id":"PF07965","name":"Integrin beta tail domain","start":632,"end":717},{"id":"PF07974","name":"EGF-like domain","start":593,"end":624},{"id":"PF08725","name":"Integrin beta cytoplasmic domain","start":742,"end":785},{"id":"PF17205","name":"Integrin plexin domain","start":29,"end":75},{"id":"PF18372","name":"Integrin beta epidermal growth factor like domain 1","start":463,"end":492},{"id":"PF23105","name":"Integrin EGF domain","start":507,"end":548}],"gene3D":[{"start":133,"end":381,"id":"3.40.50.410","name":"von Willebrand factor, type A domain"},{"start":631,"end":714,"id":"3.10.450.180","name":"3.10.450.180"},{"start":501,"end":548,"id":"2.10.25.10","name":"Laminin"},{"start":27,"end":83,"id":"3.30.1680.10","name":"ligand-binding face of the semaphorins, domain 2"},{"start":549,"end":588,"id":"2.10.25.10","name":"Laminin"},{"start":715,"end":788,"id":"1.20.5.100","name":"Cytochrome c1, transmembrane anchor, C-terminal"},{"start":105,"end":491,"id":"2.60.40.1510","name":"ntegrin, alpha v. Chain A, domain 3"},{"start":589,"end":630,"id":"2.10.25.10","name":"Laminin"}]},"uniref50":"UniRef50_P05106","sequence":"MRARPRPRPLWATVLALGALAGVGVGGPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDLKENLLKDNCAPESIEFPVSEARVLEDRPLSDKGSGDSSQVTQVSPQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDLSYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKPVSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRNDASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQNYSELIPGTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVRDLPEELSLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIEAKVRGCPQEKEKSFTIKPVGFKDSLIVQVTFDCDCACQAQAEPNSHRCNNGNGTFECGVCRCGPGWLGSQCECSEEDYRPSQQDECSPREGQPVCSQRGECLCGQCVCHSSDFGKITGKYCECDDFSCVRYKGEMCSGHGQCSCGDCLCDSDWTGYYCNCTTRTDTCMSSNGLLCSGRGKCECGSCVCIQPGSYGDTCEKCPTCPDACTFKKECVECKKFDRGALHDENTCNRYCRDEIESVKELKDTGKDAVNCTYKNEDDCVVRFQYYEDSSGKSILYVVEEPECPKGPDILVVLLSVMGAILLIGLAALLIWKLLITIHDRKEFAKFEEERARAKWDTANNPLYKEATSTFTNITYRGT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P05106","disprot_id":"DP01842","ncbi_taxon_id":9606,"regions_counter":11,"creator":"vsagris","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":788,"region_id":"DP01842r001","released":"2022_06","ec_id":"ECO:0006165","reference_html":"NMR analysis of structure and dynamics of the cytosolic tails of integrin alpha IIb beta 3 in aqueous solution. <i> Ulmer TS, Yaspan B, Ginsberg MH, Campbell ID. </i> Biochemistry, 2001","statement":[{"text":"In aqueous solution, the αIIb and β3 tails are largely unstructured, although part of the β3 tail has a propensity to form a helix (residues Arg724−Ala735) and part (the NPLY motif) has a tendency to form a β-turn.\n\"In aqueous solution, the alphaIIb and beta3 tails are largely unstructured.\"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":741,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-06-21T15:04:22.669Z","reference_source":"pmid","term_name":"disorder","reference_id":"11412103","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T13:13:11.082Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":788,"region_id":"DP01842r003","reference_id":"12230976","start":763,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"However, its C-terminal A737–T762 is disordered, consistent with the secondary structure analysis.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"reference_html":"A structural mechanism of integrin alpha(IIb)beta(3) \"inside-out\" activation as regulated by its cytoplasmic face. <i> Vinogradova O, Velyvis A, Velyviene A, Hu B, Haas T, Plow E, Qin J. </i> Cell, 2002","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T12:51:22.783Z"}},{"region_id":"DP01842r004","ec_ontology":"ECO","end":775,"term_id":"GO:0005515","start":765,"version":4,"statement":[{"text":"Here we report the crystal structure of the principal integrin binding and activating fragment of talin, alone and in complex with fragments of the beta 3 integrin tail.","type":"Abstract"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P54939","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"12535520","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1MK7"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"fquaglia","reference_html":"Structural determinants of integrin recognition by talin. <i> García-Alvarez B, de Pereda JM, Calderwood DA, Ulmer TS, Critchley D, Campbell ID, Ginsberg MH, Liddington RC. </i> Mol Cell, 2003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T13:12:50.853Z"}},{"region_id":"DP01842r005","ec_ontology":"ECO","end":788,"term_id":"GO:0005515","start":762,"version":5,"statement":[{"text":"Here we present the detailed structural analysis of Shc phosphotyrosine-binding (PTB) domain in complex with the bi-phosphorylated β(3)integrin cytoplasmic tail (CT).","type":"Abstract"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P29353","partner_end":null}],"term_name":"protein binding","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_06","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"20739287","date":"2022-06-28T13:12:07.509Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2L1C"}],"term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"fquaglia","reference_html":"Integrin {beta}3 phosphorylation dictates its complex with the Shc phosphotyrosine-binding (PTB) domain. <i> Deshmukh L, Gorbatyuk V, Vinogradova O. </i> J Biol Chem, 2010","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":773,"end":773,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":785,"end":785,"position":"Specific residue"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T13:13:40.978Z"}},{"region_id":"DP01842r006","ec_ontology":"ECO","end":788,"term_id":"GO:0005515","start":742,"version":5,"statement":[{"text":"Here, we report the structure of the cytoplasmic domain of human integrin αIIbβ3 bound to its inhibitor, the immunoglobin repeat 21 of filamin A (FLNa-Ig21).","type":"Abstract"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P21333","partner_end":null}],"term_name":"protein binding","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_06","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"25849143","date":"2022-06-28T13:10:55.479Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2MTP"}],"term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"fquaglia","reference_html":"Structural mechanism of integrin inactivation by filamin. <i> Liu J, Das M, Yang J, Ithychanda SS, Yakubenko VP, Plow EF, Qin J. </i> Nat Struct Mol Biol, 2015","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08514"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T13:13:40.409Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":787,"region_id":"DP01842r007","reference_id":"8631894","start":783,"term_id":"IDPO:0000045","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In this paper we demonstrate that the beta 3 subunit of alpha IIb beta 3 was phosphorylated on tyrosine residues in response to thrombin-induced platelet aggregation.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"immunodetection assay evidence used in manual assertion","version":3,"reference_html":"Outside-in integrin signal transduction. Alpha IIb beta 3-(GP IIb IIIa) tyrosine phosphorylation induced by platelet aggregation. <i> Law DA, Nannizzi-Alaimo L, Phillips DR. </i> J Biol Chem, 1996","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","term_name":"phosphorylation display site","ec_go":"IDA","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T13:02:36.160Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":781,"region_id":"DP01842r008","reference_id":"10896934","start":777,"term_id":"IDPO:0000045","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"However, the presence of phosphate on this threonine inhibited the binding of Shc to tyrosyl-phosphorylated β3 peptide.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_06","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"immunodetection assay evidence used in manual assertion","version":4,"reference_html":"Threonine phosphorylation of the beta 3 integrin cytoplasmic tail, at a site recognized by PDK1 and Akt/PKB in vitro, regulates Shc binding. <i> Kirk RI, Sanderson MR, Lerea KM. </i> J Biol Chem, 2000","date":"2022-06-28T13:10:24.840Z","reference_source":"pmid","ec_id":"ECO:0007719","term_name":"phosphorylation display site","ec_go":"IDA","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T13:13:29.402Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":775,"region_id":"DP01842r009","reference_id":"19141530","start":771,"term_id":"IDPO:0000045","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Interestingly, alpha(nu)beta(3) was also found to directly interact with RPTPbeta/zeta, and PTN-induced Y773 phosphorylation of beta(3) integrin was dependent on both RPTPbeta/zeta and the downstream c-src kinase activation.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_06","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"immunodetection assay evidence used in manual assertion","version":4,"reference_html":"Integrin alpha(v)beta(3) is a pleiotrophin receptor required for pleiotrophin-induced endothelial cell migration through receptor protein tyrosine phosphatase beta/zeta. <i> Mikelis C, Sfaelou E, Koutsioumpa M, Kieffer N, Papadimitriou E. </i> FASEB J, 2009","date":"2022-06-28T13:09:59.244Z","reference_source":"pmid","ec_id":"ECO:0007719","term_name":"phosphorylation display site","ec_go":"IDA","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T13:13:26.932Z"}},{"start":780,"end":783,"reference_id":"33436498","reference_source":"pmid","reference_html":"Cytoplasmic short linear motifs in ACE2 and integrin β3 link SARS-CoV-2 host cell receptors to mediators of endocytosis and autophagy.  <i> Kliche J, Kuss H, Ali M, Ivarsson Y. </i> Sci Signal, 2021","date":"2022-06-21T19:21:14.163Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006277","ec_ontology":"ECO","ec_name":"fluorescence polarization evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":779,"end":779,"position":"Specific residue","statements":[{"type":"Results","text":"Concomitant phosphorylation of Thr779 and Tyr785 (double phosphorylated integrin β3 peptide) promoted ATG8 domain binding and increased the binding affinity of MAP1LC3C even further (KI = 8 μM), indicating a synergistic effect of the two phosphosites (Fig. 5)."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":785,"end":785,"position":"Specific residue","statements":[{"type":"Results","text":"Concomitant phosphorylation of Thr779 and Tyr785 (double phosphorylated integrin β3 peptide) promoted ATG8 domain binding and increased the binding affinity of MAP1LC3C even further (KI = 8 μM), indicating a synergistic effect of the two phosphosites (Fig. 5)."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"O95166","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P60520","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9H492","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9GZQ8","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9BXW4","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01842r010","statement":[{"text":"Furthermore, we validated that an LC3-interacting region (LIR) in integrin β3 bound to the ATG8 domains of the autophagy receptors MAP1LC3 and GABARAP in a manner enhanced by LIR-adjacent phosphorylation.","type":"Abstract"},{"text":"The integrin β3 tail contains a phospho-regulated LIR motif","type":"Results"},{"text":"Table 3 Affinities of ATG8 domains for the integrin β3 peptide.\nKI values for ATG8 domains calculated from displacement experiments using unphosphorylated integrin β3 peptide and phosphorylated peptides (pThr777, pSer778, pThr779, pTyr785, or pThr779 pTyr785). Indicated error is the error of the mean (SEM); n = 3 replicates. N.B., no or low affinity (KI > 100 μM); N.M., not measured.","type":"Table"},{"text":"Table 4 Constructs used for expression of protein domains.\nProtein domains and the encoding plasmids. Species is human unless otherwise stated.","type":"Table"},{"text":"The functional LIR motif FTNI in positions 780-783 is inside the disordered fragment region in positions 741-788.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:26:23.723Z"}},{"start":780,"end":783,"reference_id":"33436498","reference_source":"pmid","reference_html":"Cytoplasmic short linear motifs in ACE2 and integrin β3 link SARS-CoV-2 host cell receptors to mediators of endocytosis and autophagy.  <i> Kliche J, Kuss H, Ali M, Ivarsson Y. </i> Sci Signal, 2021","date":"2022-06-21T19:23:48.640Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006277","ec_ontology":"ECO","ec_name":"fluorescence polarization evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":779,"end":779,"position":"Specific residue","statements":[{"type":"Results","text":"Concomitant phosphorylation of Thr779 and Tyr785 (double phosphorylated integrin β3 peptide) promoted ATG8 domain binding and increased the binding affinity of MAP1LC3C even further (KI = 8 μM), indicating a synergistic effect of the two phosphosites (Fig. 5)."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":785,"end":785,"position":"Specific residue","statements":[{"type":"Results","text":"Concomitant phosphorylation of Thr779 and Tyr785 (double phosphorylated integrin β3 peptide) promoted ATG8 domain binding and increased the binding affinity of MAP1LC3C even further (KI = 8 μM), indicating a synergistic effect of the two phosphosites (Fig. 5)."}]}],"ec_go":"IPI","region_id":"DP01842r011","statement":[{"text":"Furthermore, we validated that an LC3-interacting region (LIR) in integrin β3 bound to the ATG8 domains of the autophagy receptors MAP1LC3 and GABARAP in a manner enhanced by LIR-adjacent phosphorylation.","type":"Abstract"},{"text":"The integrin β3 tail contains a phospho-regulated LIR motif","type":"Results"},{"text":"Table 3 Affinities of ATG8 domains for the integrin β3 peptide.\nKI values for ATG8 domains calculated from displacement experiments using unphosphorylated integrin β3 peptide and phosphorylated peptides (pThr777, pSer778, pThr779, pTyr785, or pThr779 pTyr785). Indicated error is the error of the mean (SEM); n = 3 replicates. N.B., no or low affinity (KI > 100 μM); N.M., not measured.","type":"Table"},{"text":"Table 4 Constructs used for expression of protein domains.\nProtein domains and the encoding plasmids. Species is human unless otherwise stated.","type":"Table"},{"text":"The functional LIR motif FTNI in positions 780-783 is inside the disordered fragment region in positions 741-788.","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-22T10:26:21.134Z"}}],"released":"2018_11","uniref100":"UniRef100_P05106","date":"2018-08-13T14:03:26.000Z","acc":"P05106","name":"Integrin beta-3","length":788,"organism":"Homo sapiens","dataset":["Autophagy-related proteins","NDDs-related proteins"],"UniParc":"UPI0000048135","genes":[{"name":{"value":"ITGB3","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6156","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6156"}}]},"synonyms":[{"value":"GP3A"}]}],"alphafold_very_low_content":0.03680203045685279,"disorder_content":0.06091370558375635,"disprot_consensus":{"full":[{"start":741,"end":788,"type":"D"}],"Structural state":[{"start":741,"end":788,"type":"D"}],"Molecular function":[{"start":742,"end":788,"type":"F"}],"Disorder function":[{"start":771,"end":775,"type":"F"},{"start":777,"end":781,"type":"F"},{"start":783,"end":787,"type":"F"}],"Biological process":[{"start":780,"end":783,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00469","name":"Negative factor, (F-Protein) or Nef","start":2,"end":205}],"gene3D":[{"start":2,"end":57,"id":"4.10.890.10","name":"HIV 1 nef anchor domain"},{"start":58,"end":206,"id":"3.30.62.10","name":"Nef Regulatory Factor"}]},"uniref50":"UniRef50_P03406","sequence":"MGGKWSKSSVIGWPAVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAANNAACAWLEAQEEEKVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGIRYPLTFGWCYKLVPVEPDKVEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"uniref90":"UniRef90_P03404","disprot_id":"DP01843","ncbi_taxon_id":11678,"regions_counter":1,"creator":"jbergier","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":25,"region_id":"DP01843r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of a polypeptide from the N terminus of the HIV protein Nef. <i> Barnham KJ, Monks SA, Hinds MG, Azad AA, Norton RS. </i> Biochemistry, 1997","statement":[{"text":"In dilute aqueous solution, the N terminus is unstructured, but in nonpolar, membrane-like environments, this helical structure is quite stable.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"lalvarez","start":1,"term_ontology":"IDPO","curator_name":"Lucía Álvarez","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-1437-5773","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"9166767","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-06T14:18:30.043Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P03404","date":"2018-08-13T16:18:29.000Z","acc":"P03404","name":"Protein Nef","length":206,"organism":"Human immunodeficiency virus type 1 group M subtype B (isolate BH10)","dataset":["Viral proteins"],"UniParc":"UPI000012FEFB","genes":[{"name":{"value":"nef","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04078","url":"https://hamap.expasy.org/unirule/MF_04078"}}]}}],"disorder_content":0.12135922330097088,"disprot_consensus":{"full":[{"start":1,"end":25,"type":"D"}],"Structural state":[{"start":1,"end":25,"type":"D"}]}},{"features":{"pfam":[{"id":"PF10373","name":"Est1 DNA/RNA binding domain","start":171,"end":430},{"id":"PF10374","name":"Telomerase activating protein Est1","start":55,"end":168}]},"uniref50":"UniRef50_Q92540","sequence":"MSLQSAQYLRQAEVLKADMTDSKLGPAEVWTSRQALQDLYQKMLVTDLEYALDKKVEQDLWNHAFKNQITTLQGQAKNRANPNRSEVQANLSLFLEAASGFYTQLLQELCTVFNVDLPCRVKSSQLGIISNKQTHTSAIVKPQSSSCSYICQHCLVHLGDIARYRNQTSQAESYYRHAAQLVPSNGQPYNQLAILASSKGDHLTTIFYYCRSIAVKFPFPAASTNLQKALSKALESRDEVKTKWGVSDFIKAFIKFHGHVYLSKSLEKLSPLREKLEEQFKRLLFQKAFNSQQLVHVTVINLFQLHHLRDFSNETEQHTYSQDEQLCWTQLLALFMSFLGILCKCPLQNESQEESYNAYPLPAVKVSMDWLRLRPRVFQEAVVDERQYIWPWLISLLNSFHPHEEDLSSISATPLPEEFELQGFLALRPSFRNLDFSKGHQGITGDKEGQQRRIRQQRLISIGKWIADNQPRLIQCENEVGKLLFITEIPELILEDPSEAKENLILQETSVIESLAADGSPGLKSVLSTSRNLSNNCDTGEKPVVTFKENIKTREVNRDQGRSFPPKEVRRDYSKGITVTKNDGKKDNNKRKTETKKCTLEKLQETGKQNVAVQVKSQTELRKTPVSEARKTPVTQTPTQASNSQFIPIHHPGAFPPLPSRPGFPPPTYVIPPPVAFSMGSGYTFPAGVSVPGTFLQPTAHSPAGNQVQAGKQSHIPYSQQRPSGPGPMNQGPQQSQPPSQQPLTSLPAQPTAQSTSQLQVQALTQQQQSPTKAVPALGKSPPHHSGFQQYQQADASKQLWNPPQVQGPLGKIMPVKQPYYLQTQDPIKLFEPSLQPPVMQQQPLEKKMKPFPMEPYNHNPSEVKVPEFYWDSSYSMADNRSVMAQQANIDRRGKRSPGVFRPEQDPVPRMPFEKSLLEKPSELMSHSSSFLSLTGFSLNQERYPNNSMFNEVYGKNLTSSSKAELSPSMAPQETSLYSLFEGTPWSPSLPASSDHSTPASQSPHSSNPSSLPSSPPTHNHNSVPFSNFGPIGTPDNRDRRTADRWKTDKPAMGGFGIDYLSATSSSESSWHQASTPSGTWTGHGPSMEDSSAVLMESLKSIWSSSMMHPGPSALEQLLMQQKQKQQRGQGTMNPPH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q92540","disprot_id":"DP01844","ncbi_taxon_id":9606,"regions_counter":1,"creator":"lalvarez","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":143,"region_id":"DP01844r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"SMG7 is a 14-3-3-like adaptor in the nonsense-mediated mRNA decay pathway. <i> Fukuhara N, Ebert J, Unterholzner L, Lindner D, Izaurralde E, Conti E. </i> Mol Cell, 2005","statement":[{"text":"\"a long, disordered loop between residues 111 to 143","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"lalvarez","start":111,"term_ontology":"IDPO","curator_name":"Lucía Álvarez","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-1437-5773","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1YA0"}],"reference_id":"15721257","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q92540","date":"2018-08-13T16:32:53.000Z","acc":"Q92540","name":"Protein SMG7","length":1137,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000139502","genes":[{"name":{"value":"SMG7","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:16792","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:16792"}}]},"synonyms":[{"value":"C1orf16","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:16792","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:16792"}}]},{"value":"EST1C","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:16792","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:16792"}}]},{"value":"KIAA0250","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:16792","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:16792"}}]}]}],"alphafold_very_low_content":0.5576077396657871,"disorder_content":0.029023746701846966,"disprot_consensus":{"full":[{"start":111,"end":143,"type":"D"}],"Structural state":[{"start":111,"end":143,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00254","name":"FKBP-type peptidyl-prolyl cis-trans isomerase","start":44,"end":135},{"id":"PF00254","name":"FKBP-type peptidyl-prolyl cis-trans isomerase","start":160,"end":248},{"id":"PF00515","name":"Tetratricopeptide repeat","start":319,"end":348},{"id":"PF13181","name":"Tetratricopeptide repeat","start":354,"end":384}],"gene3D":[{"start":260,"end":425,"id":"1.25.40.10","name":"Tetratricopeptide repeat domain"},{"start":141,"end":253,"id":"3.10.50.40","name":"3.10.50.40"},{"start":14,"end":140,"id":"3.10.50.40","name":"3.10.50.40"}]},"uniref50":"UniRef50_Q13451","sequence":"MTTDEGAKNNEESPTATVAEQGEDITSKKDRGVLKIVKRVGNGEETPMIGDKVYVHYKGKLSNGKKFDSSHDRNEPFVFSLGKGQVIKAWDIGVATMKKGEICHLLCKPEYAYGSAGSLPKIPSNATLFFEIELLDFKGEDLFEDGGIIRRTKRKGEGYSNPNEGATVEIHLEGRCGGRMFDCRDVAFTVGEGEDHDIPIGIDKALEKMQREEQCILYLGPRYGFGEAGKPKFGIEPNAELIYEVTLKSFEKAKESWEMDTKEKLEQAAIVKEKGTVYFKGGKYMQAVIQYGKIVSWLEMEYGLSEKESKASESFLLAAFLNLAMCYLKLREYTKAVECCDKALGLDSANEKGLYRRGEAQLLMNEFESAKGDFEKVLEVNPQNKAARLQISMCQKKAKEHNERDRRIYANMFKKFAEQDAKEEANKAMGKKTSEGVTNEKGTDSQAMEEEKPEGHV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q13451","disprot_id":"DP01845","ncbi_taxon_id":9606,"regions_counter":1,"creator":"lalvarez","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":12,"region_id":"DP01845r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90. <i> Bracher A, Kozany C, Thost AK, Hausch F. </i> Acta Crystallogr D Biol Crystallogr, 2011","statement":[{"text":"The residues 1–12 upstream of helix 1 were disordered in the structures of FKBP51(1–140), consistent with the poor sequence conservation in this segment.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"lalvarez","start":1,"term_ontology":"IDPO","curator_name":"Lucía Álvarez","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-1437-5773","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3O5E"}],"reference_id":"21636895","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q13451","date":"2018-08-13T16:43:57.000Z","acc":"Q13451","name":"Peptidyl-prolyl cis-trans isomerase FKBP5","length":457,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000016A29C","genes":[{"name":{"value":"FKBP5"},"synonyms":[{"value":"AIG6"},{"value":"FKBP51","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"28147277","url":"http://www.ncbi.nlm.nih.gov/pubmed/28147277","alternativeUrl":"https://europepmc.org/abstract/MED/28147277"}}]}]}],"alphafold_very_low_content":0.05908096280087528,"disorder_content":0.0262582056892779,"disprot_consensus":{"full":[{"start":1,"end":12,"type":"D"}],"Structural state":[{"start":1,"end":12,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00362","name":"Integrin beta chain VWA domain","start":122,"end":367},{"id":"PF07965","name":"Integrin beta tail domain","start":621,"end":699},{"id":"PF08725","name":"Integrin beta cytoplasmic domain","start":724,"end":766},{"id":"PF17205","name":"Integrin plexin domain","start":24,"end":73},{"id":"PF23105","name":"Integrin EGF domain","start":492,"end":535}],"gene3D":[{"start":724,"end":768,"id":"1.20.5.630","name":"Integrin beta subunit, cytoplasmic domain"},{"start":124,"end":366,"id":"3.40.50.410","name":"von Willebrand factor, type A domain"},{"start":443,"end":473,"id":"2.10.25.10","name":"Laminin"},{"start":487,"end":540,"id":"2.10.25.10","name":"Laminin"},{"start":580,"end":636,"id":"2.10.25.10","name":"Laminin"},{"start":541,"end":577,"id":"2.10.25.10","name":"Laminin"},{"start":23,"end":81,"id":"3.30.1680.10","name":"ligand-binding face of the semaphorins, domain 2"},{"start":637,"end":705,"id":"3.10.450.180","name":"3.10.450.180"}]},"uniref50":"UniRef50_P05107","sequence":"MLGLRPPLLALVGLLSLGCVLSQECTKFKVSSCRECIESGPGCTWCQKLNFTGPGDPDSIRCDTRPQLLMRGCAADDIMDPTSLAETQEDHNGGQKQLSPQKVTLYLRPGQAAAFNVTFRRAKGYPIDLYYLMDLSYSMLDDLRNVKKLGGDLLRALNEITESGRIGFGSFVDKTVLPFVNTHPDKLRNPCPNKEKECQPPFAFRHVLKLTNNSNQFQTEVGKQLISGNLDAPEGGLDAMMQVAACPEEIGWRNVTRLLVFATDDGFHFAGDGKLGAILTPNDGRCHLEDNLYKRSNEFDYPSVGQLAHKLAENNIQPIFAVTSRMVKTYEKLTEIIPKSAVGELSEDSSNVVHLIKNAYNKLSSRVFLDHNALPDTLKVTYDSFCSNGVTHRNQPRGDCDGVQINVPITFQVKVTATECIQEQSFVIRALGFTDIVTVQVLPQCECRCRDQSRDRSLCHGKGFLECGICRCDTGYIGKNCECQTQGRSSQELEGSCRKDNNSIICSGLGDCVCGQCLCHTSDVPGKLIYGQYCECDTINCERYNGQVCGGPGRGLCFCGKCRCHPGFEGSACQCERTTEGCLNPRRVECSGRGRCRCNVCECHSGYQLPLCQECPGCPSPCGKYISCAECLKFEKGPFGKNCSAACPGLQLSNNPVKGRTCKERDSEGCWVAYTLEQQDGMDRYLIYVDESRECVAGPNIAAIVGGTVAGIVLIGILLLVIWKALIHLSDLREYRRFEKEKLKSQWNNDNPLFKSATTTVMNPKFAES","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P05107","disprot_id":"DP01848","ncbi_taxon_id":9606,"regions_counter":6,"creator":"bmesza","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":769,"region_id":"DP01848r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Beta2 integrin phosphorylation on Thr758 acts as a molecular switch to regulate 14-3-3 and filamin binding. <i> Takala H, Nurminen E, Nurmi SM, Aatonen M, Strandin T, Takatalo M, Kiema T, Gahmberg CG, Ylänne J, Fagerholm SC. </i> Blood, 2008","statement":[{"text":"Both of them are extended, but the peptide does not form a β-strand in the 14-3-3 complex as seen in the filamin complex. This indicates that the integrin cytoplasmic tail can adopt different conformations depending of its binding partner. In the crystal structures, we see only those parts of the cytoplasmic tail peptides that are in direct contacts, whereas the other regions apparently are disordered.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"tszani","start":735,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2jf1"}],"reference_id":"18550856","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":769,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Beta2 integrin phosphorylation on Thr758 acts as a molecular switch to regulate 14-3-3 and filamin binding. <i> Takala H, Nurminen E, Nurmi SM, Aatonen M, Strandin T, Takatalo M, Kiema T, Gahmberg CG, Ylänne J, Fagerholm SC. </i> Blood, 2008","term_id":"GO:0005515","curator_id":"tszani","start":735,"term_ontology":"GO","curator_name":"Tamás Szaniszló","reference_id":"18550856","version":3,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01848r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":769,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Beta2 integrin phosphorylation on Thr758 acts as a molecular switch to regulate 14-3-3 and filamin binding. <i> Takala H, Nurminen E, Nurmi SM, Aatonen M, Strandin T, Takatalo M, Kiema T, Gahmberg CG, Ylänne J, Fagerholm SC. </i> Blood, 2008","statement":[{"text":"The β2 peptide bound to IgFLNa21 in a very similar way as the β7 peptide,3 forming a hydrogen-bonded β-strand next to the strand C of IgFLNa21 and interacting hydrophobically with the side chains of strand D (Figure 3C,D)","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"tszani","start":735,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","reference_id":"18550856","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01848r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":769,"region_id":"DP01848r005","reference_id":"18550856","start":735,"term_id":"GO:0098772","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Our results suggest that the phosphorylation of beta2 integrins on Thr758 acts as a molecular switch to inhibit filamin binding and allow 14-3-3 protein binding to the integrin cytoplasmic domain, thereby modulating T-cell adhesion.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"x-ray crystallography evidence used in manual assertion","version":4,"reference_html":"Beta2 integrin phosphorylation on Thr758 acts as a molecular switch to regulate 14-3-3 and filamin binding. <i> Takala H, Nurminen E, Nurmi SM, Aatonen M, Strandin T, Takatalo M, Kiema T, Gahmberg CG, Ylänne J, Fagerholm SC. </i> Blood, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","term_name":"molecular function regulator","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":760,"region_id":"DP01848r006","reference_id":"18550856","start":756,"term_id":"IDPO:0000045","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Our results suggest that the phosphorylation of beta2 integrins on Thr758 acts as a molecular switch to inhibit filamin binding and allow 14-3-3 protein binding to the integrin cytoplasmic domain, thereby modulating T-cell adhesion.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"qualitative western immunoblotting evidence used in manual assertion","version":3,"reference_html":"Beta2 integrin phosphorylation on Thr758 acts as a molecular switch to regulate 14-3-3 and filamin binding. <i> Takala H, Nurminen E, Nurmi SM, Aatonen M, Strandin T, Takatalo M, Kiema T, Gahmberg CG, Ylänne J, Fagerholm SC. </i> Blood, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000279","term_name":"phosphorylation display site","ec_go":"IEP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_P05107","date":"2018-08-14T08:45:19.000Z","acc":"P05107","name":"Integrin beta-2","length":769,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000016A19B","genes":[{"name":{"value":"ITGB2"},"synonyms":[{"value":"CD18"},{"value":"MFI7"}]}],"alphafold_very_low_content":0.03901170351105332,"disorder_content":0.045513654096228866,"disprot_consensus":{"full":[{"start":735,"end":769,"type":"T"}],"Structural state":[{"start":735,"end":769,"type":"D"}],"Molecular function":[{"start":735,"end":769,"type":"F"}],"Structural transition":[{"start":735,"end":769,"type":"T"}],"Disorder function":[{"start":756,"end":760,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00240","name":"Ubiquitin family","start":3,"end":72},{"id":"PF17976","name":"RING/Ubox like zinc-binding domain","start":145,"end":217},{"id":"PF17978","name":"RING/Ubox like zinc-binding domain","start":228,"end":318},{"id":"PF22605","name":"IBR domain","start":411,"end":459}],"gene3D":[{"start":397,"end":464,"id":"1.20.120.1750","name":"1.20.120.1750"},{"start":321,"end":396,"id":"2.20.25.20","name":"2.20.25.20"},{"start":1,"end":76,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"}]},"uniref50":"UniRef50_O60260","sequence":"MIVFVRFNSSHGFPVEVDSDTSIFQLKEVVAKRQGVPADQLRVIFAGKELRNDWTVQNCDLDQQSIVHIVQRPWRKGQEMNATGGDDPRNAAGGCEREPQSLTRVDLSSSVLPGDSVGLAVILHTDSRKDSPPAGSPAGRSIYNSFYVYCKGPCQRVQPGKLRVQCSTCRQATLTLTQGPSCWDDVLIPNRMSGECQSPHCPGTSAEFFFKCGAHPTSDKETSVALHLIATNSRNITCITCTDVRSPVLVFQCNSRHVICLDCFHLYCVTRLNDRQFVHDPQLGYSLPCVAGCPNSLIKELHHFRILGEEQYNRYQQYGAEECVLQMGGVLCPRPGCGAGLLPEPDQRKVTCEGGNGLGCGFAFCRECKEAYHEGECSAVFEASGTTTQAYRVDERAAEQARWEAASKETIKKTTKPCPRCHVPVEKNGGCMHMKCPQPQCRLEWCWNCGCEWNRVCMGDHWFDV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O60260","disprot_id":"DP01849","ncbi_taxon_id":9606,"regions_counter":6,"creator":"mpajkos","regions":[{"region_id":"DP01849r003","validated":{"curator_id":"fquaglia","timestamp":"2020-11-25T16:19:40.834Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":391,"term_id":"IDPO:0000002","start":378,"version":2,"statement":[{"text":"The IBR-R2 linker region (which we refer to as the tether: residues 378–414) is 37 residues long. Most of the beginning of the tether (14 residues) is disordered, while the latter part runs across the surface of R1","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-5791-9825","released":"2022_03","term_ontology":"IDPO","curator_name":"Mátyás Pajkos","reference_id":"23770887","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4I1H"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"mpajkos","reference_html":"Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases. <i> Riley BE, Lougheed JC, Callaway K, Velasquez M, Brecht E, Nguyen L, Shaler T, Walker D, Yang Y, Regnstrom K, Diep L, Zhang Z, Chiou S, Bova M, Artis DR, Yao N, Baker J, Yednock T, Johnston JA. </i> Nat Commun, 2013","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP01849r004","validated":{"curator_id":"fquaglia","timestamp":"2020-11-25T16:19:44.367Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":391,"term_id":"IDPO:0000033","start":378,"version":3,"statement":[{"text":"The IBR-R2 linker region (which we refer to as the tether: residues 378–414) is 37 residues long. Most of the beginning of the tether (14 residues) is disordered, while the latter part runs across the surface of R1","type":"Results"}],"term_name":"flexible linker","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0001-5791-9825","released":"2022_03","term_ontology":"IDPO","curator_name":"Mátyás Pajkos","reference_id":"23770887","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4I1H"}],"term_namespace":"Disorder function","ec_id":"ECO:0005670","curator_id":"mpajkos","reference_html":"Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases. <i> Riley BE, Lougheed JC, Callaway K, Velasquez M, Brecht E, Nguyen L, Shaler T, Walker D, Yang Y, Regnstrom K, Diep L, Zhang Z, Chiou S, Bova M, Artis DR, Yao N, Baker J, Yednock T, Johnston JA. </i> Nat Commun, 2013","ec_go":"EXP","disprot_namespace":"Disorder function"},{"region_id":"DP01849r005","validated":{"curator_id":"fquaglia","timestamp":"2020-11-25T16:19:41.816Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":99,"term_id":"IDPO:0000002","start":73,"version":2,"statement":[{"text":"Residues before the ACT element (amino acids 73–99) and after the ACT element (amino acids 109–142) are disordered in our structure.","type":"Article"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-5791-9825","released":"2022_03","term_ontology":"IDPO","curator_name":"Mátyás Pajkos","reference_id":"29995846","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6GLC"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"mpajkos","reference_html":"Mechanism of parkin activation by PINK1. <i> Gladkova C, Maslen SL, Skehel JM, Komander D. </i> Nature, 2018","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP01849r006","validated":{"curator_id":"fquaglia","timestamp":"2020-11-25T16:19:43.302Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":142,"term_id":"IDPO:0000002","start":109,"version":2,"statement":[{"text":"Residues before the ACT element (amino acids 73–99) and after the ACT element (amino acids 109–142) are disordered in our structure.","type":"Article"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-5791-9825","released":"2022_03","term_ontology":"IDPO","curator_name":"Mátyás Pajkos","reference_id":"29995846","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6GLC"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"mpajkos","reference_html":"Mechanism of parkin activation by PINK1. <i> Gladkova C, Maslen SL, Skehel JM, Komander D. </i> Nature, 2018","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_O60260","date":"2018-08-14T10:00:15.000Z","acc":"O60260","name":"E3 ubiquitin-protein ligase parkin","length":465,"organism":"Homo sapiens","dataset":["Autophagy-related proteins","NDDs-related proteins","Age-related disorders proteins"],"UniParc":"UPI0000052360","genes":[{"name":{"value":"PRKN","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:8607","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8607"}}]},"synonyms":[{"value":"PARK2"}]}],"alphafold_very_low_content":0.15698924731182795,"disorder_content":0.16129032258064516,"disprot_consensus":{"full":[{"start":73,"end":99,"type":"D"},{"start":109,"end":142,"type":"D"},{"start":378,"end":391,"type":"D"}],"Structural state":[{"start":73,"end":99,"type":"D"},{"start":109,"end":142,"type":"D"},{"start":378,"end":391,"type":"D"}],"Disorder function":[{"start":378,"end":391,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00240","name":"Ubiquitin family","start":3,"end":73},{"id":"PF17976","name":"RING/Ubox like zinc-binding domain","start":145,"end":217},{"id":"PF17978","name":"RING/Ubox like zinc-binding domain","start":228,"end":318},{"id":"PF22605","name":"IBR domain","start":411,"end":459}],"gene3D":[{"start":330,"end":384,"id":"2.20.25.20","name":"2.20.25.20"},{"start":390,"end":464,"id":"1.20.120.1750","name":"1.20.120.1750"},{"start":1,"end":76,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"}]},"uniref50":"UniRef50_O60260","sequence":"MIVFVRFNSSYGFPVEVDSDTSIFQLKEVVAKRQGVPADQLRVIFAGKELQNHLTVQNCDLEQQSIVHIVQRPQRKSHETNASGGDKPQSTPEGSIWEPRSLTRVDLSSHILPADSVGLAVILDTDSKSDSEAARGPEAKPTYHSFFVYCKGPCHKVQPGKLRVQCGTCRQATLTLAQGPSCWDDVLIPNRMSGECQSPDCPGTRAEFFFKCGAHPTSDKDTSVALNLITNNSRSIPCIACTDVRNPVLVFQCNHRHVICLDCFHLYCVTRLNDRQFVHDAQLGYSLPCVAGCPNSLIKELHHFRILGEEQYNRYQQYGAEECVLQMGGVLCPRPGCGAGLLPEQGQKKVTCEGGNGLGCGFVFCRDCKEAYHEGECDSMFEASGATSQAYRVDQRAAEQARWEEASKETIKKTTKPCPRCNVPIEKNGGCMHMKCPQPQCKLEWCWNCGCEWNRACMGDHWFDV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_Q9JK66","disprot_id":"DP01850","ncbi_taxon_id":10116,"regions_counter":3,"creator":"lalvarez","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":392,"region_id":"DP01850r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of parkin reveals mechanisms for ubiquitin ligase activation. <i> Trempe JF, Sauvé V, Grenier K, Seirafi M, Tang MY, Ménade M, Al-Abdul-Wahid S, Krett J, Wong K, Kozlov G, Nagar B, Fon EA, Gehring K. </i> Science, 2013","statement":[{"text":"The repressing REP is surrounded by unstructured regions","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"lalvarez","start":378,"term_ontology":"IDPO","curator_name":"Lucía Álvarez","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-1437-5773","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4K7D"}],"reference_id":"23661642","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":141,"region_id":"DP01850r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of parkin reveals mechanisms for ubiquitin ligase activation. <i> Trempe JF, Sauvé V, Grenier K, Seirafi M, Tang MY, Ménade M, Al-Abdul-Wahid S, Krett J, Wong K, Kozlov G, Nagar B, Fon EA, Gehring K. </i> Science, 2013","statement":[{"text":"The long linker following the Ubl is not visible in the crystal structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"lalvarez","start":76,"term_ontology":"IDPO","curator_name":"Lucía Álvarez","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-1437-5773","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"undefined","id":"undefined"}],"reference_id":"23661642","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":392,"region_id":"DP01850r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"A Ubl/ubiquitin switch in the activation of Parkin. <i> Sauvé V, Lilov A, Seirafi M, Vranas M, Rasool S, Kozlov G, Sprules T, Wang J, Trempe JF, Gehring K. </i> EMBO J, 2015","statement":[{"text":"In the new structure, residues 382–391 preceding the REP are again disordered","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"lalvarez","start":378,"term_ontology":"IDPO","curator_name":"Lucía Álvarez","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-1437-5773","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4ZYN"}],"reference_id":"26254305","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9JK66","date":"2018-08-14T10:14:37.000Z","acc":"Q9JK66","name":"E3 ubiquitin-protein ligase parkin","length":465,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI00000E700E","genes":[{"name":{"value":"Prkn","evidences":[{"code":"ECO:0000250","source":{"name":"UniProtKB","id":"O60260","url":"https://www.uniprot.org/uniprot/O60260"}}]},"synonyms":[{"value":"Park2","evidences":[{"code":"ECO:0000312","source":{"name":"RGD","id":"61797","url":"https://rgd.mcw.edu/tools/genes/genes_view.cgi?id=61797"}}]}]}],"alphafold_very_low_content":0.16129032258064516,"disorder_content":0.17419354838709677,"disprot_consensus":{"full":[{"start":76,"end":141,"type":"D"},{"start":378,"end":392,"type":"D"}],"Structural state":[{"start":76,"end":141,"type":"D"},{"start":378,"end":392,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00017","name":"SH2 domain","start":550,"end":639},{"id":"PF00017","name":"SH2 domain","start":668,"end":741},{"id":"PF00018","name":"SH3 domain","start":797,"end":843},{"id":"PF00168","name":"C2 domain","start":1090,"end":1186},{"id":"PF00169","name":"PH domain","start":57,"end":140},{"id":"PF00387","name":"Phosphatidylinositol-specific phospholipase C, Y domain","start":953,"end":1067},{"id":"PF00388","name":"Phosphatidylinositol-specific phospholipase C, X domain","start":322,"end":465},{"id":"PF23329","name":"PLCG EF-hand motif 1","start":147,"end":220},{"id":"PF23583","name":"PLCG EF-hand motif 2","start":243,"end":313}],"gene3D":[{"start":662,"end":766,"id":"3.30.505.10","name":"SH2 domain"},{"start":903,"end":1079,"id":"3.20.20.190","name":"Phosphatidylinositol (PI) phosphodiesterase"},{"start":318,"end":496,"id":"3.20.20.190","name":"Phosphatidylinositol (PI) phosphodiesterase"},{"start":528,"end":661,"id":"3.30.505.10","name":"SH2 domain"},{"start":1081,"end":1247,"id":"2.60.40.150","name":"C2 domain"},{"start":23,"end":145,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":146,"end":306,"id":"1.10.238.10","name":"EF-hand"},{"start":788,"end":853,"id":"2.30.30.40","name":"SH3 Domains"}]},"uniref50":"UniRef50_P19174","sequence":"MAGVGTPCANGCGPSAPSEAEVLHLCRSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQITWSRGADKIEGSIDIREIKEIRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTLSLQATSEDEVNMWIKGLTWLMEDTLQAATPLQIERWLRKQFYSVDRNREDRISAKDLKNMLSQVNYRVPNMRFLRERLTDFEQRSGDITYGQFAQLYRSLMYSAQKTMDLPFLETNTLRTGERPELCQVSLSEFQQFLLEYQGELWAVDRLQVQEFMLSFLRDPLREIEEPYFFLDELVTFLFSKENSVWNSQLDAVCPETMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDGPDGMPVIYHGHTLTTKIKFSDVLHTIKEHAFVASEYPVILSIEDHCSIAQQRNMAQHFRKVLGDTLLTKPVDIAADGLPSPNQLKRKILIKHKKLAEGSAYEEVPTSVMYSENDISNSIKNGILYLEDPVNHEWYPHYFVLTSSKIYYSEETSSDQGNEDEEEPKEASGSTELHSSEKWFHGKLGAGRDGRHIAERLLTEYCIETGAPDGSFLVRESETFVGDYTLSFWRNGKVQHCRIHSRQDAGTPKFFLTDNLVFDSLYDLITHYQQVPLRCNEFEMRLSEPVPQTNAHESKEWYHASLTRAQAEHMLMRVPRDGAFLVRKRNEPNSYAISFRAEGKIKHCRVQQEGQTVMLGNSEFDSLVDLISYYEKHPLYRKMKLRYPINEEALEKIGTAEPDYGALYEGRNPGFYVEANPMPTFKCAVKALFDYKAQREDELTFTKSAIIQNVEKQDGGWWRGDYGGKKQLWFPSNYVEEMINPAILEPEREHLDENSPLGDLLRGVLDVPACQIAIRPEGKNNRLFVFSISMPSVAQWSLDVAADSQEELQDWVKKIREVAQTADARLTEGKMMERRKKIALELSELVVYCRPVPFDEEKIGTERACYRDMSSFPETKAEKYVNKAKGKKFLQYNRLQLSRIYPKGQRLDSSNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFMAGGHCGYVLQPSTMRDEAFDPFDKSSLRGLEPCVICIEVLGARHLPKNGRGIVCPFVEIEVAGAEYDSTKQKTEFVVDNGLNPVWPAKPFHFQISNPEFAFLRFVVYEEDMFSDQNFLAQATFPVKGLKTGYRAVPLKNNYSEDLELASLLIKIDIFPAKENGDLSPFSGTSLRERASDASSQLFHVRAREGSFEARYQQPFEDFRISQEHLADHFDSRERRAPRRTRVNGDNRL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_P10686","disprot_id":"DP01851","ncbi_taxon_id":10116,"regions_counter":2,"creator":"tszani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":779,"region_id":"DP01851r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes. <i> Hajicek N, Charpentier TH, Rush JR, Harden TK, Sondek J. </i> Biochemistry, 2013","statement":[{"text":"Although the phosphopeptide consists of 18 residues, only the C-terminal eight have clear electron density in the structure and bury ~430 Å2 of solvent-accessible surface of the cSH2 domain upon complex formation. The remainder of the peptide is presumably disordered and not required for complex formation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"tszani","start":770,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4k45"}],"reference_id":"23777354","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":779,"term_name":"self-inhibition","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes. <i> Hajicek N, Charpentier TH, Rush JR, Harden TK, Sondek J. </i> Biochemistry, 2013","term_id":"IDPO:0000059","curator_id":"tszani","start":770,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","reference_id":"23777354","version":3,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01851r002","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_P10686","date":"2018-08-14T10:14:43.000Z","acc":"P10686","name":"1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1","length":1290,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI0000131AA6","genes":[{"name":{"value":"Plcg1","evidences":[{"code":"ECO:0000312","source":{"name":"RGD","id":"3347","url":"https://rgd.mcw.edu/tools/genes/genes_view.cgi?id=3347"}}]}}],"alphafold_very_low_content":0.1186046511627907,"disorder_content":0.007751937984496124,"disprot_consensus":{"full":[{"start":770,"end":779,"type":"D"}],"Structural state":[{"start":770,"end":779,"type":"D"}],"Disorder function":[{"start":770,"end":779,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01024","name":"Colicin pore forming domain","start":392,"end":585},{"id":"PF22348","name":"Colicin-A N-terminal domain","start":57,"end":102}],"gene3D":[{"start":388,"end":592,"id":"1.10.490.30","name":"Colicin"},{"start":51,"end":112,"id":"2.30.30.970","name":"2.30.30.970"}]},"uniref50":"UniRef50_P04480","sequence":"MPGFNYGGKGDGTGWSSERGSGPEPGGGSHGNSGGHDRGDSSNVGNESVTVMKPGDSYNTPWGKVIINAAGQPTMNGTVMTADNSSMVPYGRGFTRVLNSLVNNPVSPAGQNGGKSPVQTAVENYLMVQSGNLPPGYWLSNGKVMTEVREERTSGGGGKNGNERTWTVKVPREVPQLTASYNEGMRIRQEAADRARAEANARALAEEEARAIASGKSKAEFDAGKRVEAAQAAINTAQLNVNNLSGAVSAANQVITQKQAEMTPLKNELAAANQRVQETLKFINDPIRSRIHFNMRSGLIRAQHNVDTKQNEINAAVANRDALNSQLSQANNILQNARNEKSAADAALSAATAQRLQAEAALRAAAEAAEKARQRQAEEAERQRQAMEVAEKAKDERELLEKTSELIAGMGDKIGEHLGDKYKAIAKDIADNIKNFQGKTIRSFDDAMASLNKITANPAMKINKADRDALVNAWKHVDAQDMANKLGNLSKAFKVADVVMKVEKVREKSIEGYETGNWGPLMLEVESWVLSGIASSVALGIFSATLGAYALSLGVPAIAVGIAGILLAAVVGALIDDKFADALNNEIIRPAH","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Citrobacter","Citrobacter freundii complex"],"uniref90":"UniRef90_P04480","disprot_id":"DP01852","dataset":["Unicellular toxins and antitoxins"],"ncbi_taxon_id":546,"regions_counter":11,"creator":"tszani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":172,"region_id":"DP01852r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Macromolecular import into Escherichia coli: the TolA C-terminal domain changes conformation when interacting with the colicin A toxin. <i> Deprez C, Blanchard L, Guerlesquin F, Gavioli M, Simorre JP, Lazdunski C, Marion D, Lloubès R. </i> Biochemistry, 2002","statement":[{"text":"In agreement with what was previously observed with the N-terminal domain of colicin N (42), the far-UV circular dichroism (CD) spectrum of ATh shows no significant amount of ordered secondary structure (Figure 4) and was similar to that of AT1","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"tszani","start":1,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T09:48:16.678Z","curator_name":"Federica Quaglia"},"reference_id":"11851406","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP01852r002","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T09:51:58.909Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":107,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":21,"version":2,"statement":[{"text":"Even though 107 amino acids of the translocation domain of ColA were included in the crystallization, only residues 9–20 could be resolved in the electron density maps (Fig. 3A). No additional peaks of density were observed at any stage of the model building and refinement, therefore the remaining residues of the TA1–107 polypeptide are assumed to be disordered in the solvent channels within the crystal lattice.","type":"Results"}],"term_name":"disorder","reference_html":"The crystal structure of the TolB box of colicin A in complex with TolB reveals important differences in the recruitment of the common TolB translocation portal used by group A colicins. <i> Zhang Y, Li C, Vankemmelbeke MN, Bardelang P, Paoli M, Penfold CN, James R. </i> Mol Microbiol, 2010","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamás Szaniszló","reference_id":"19627502","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3iax"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"tszani","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":172,"region_id":"DP01852r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Macromolecular import into Escherichia coli: the TolA C-terminal domain changes conformation when interacting with the colicin A toxin. <i> Deprez C, Blanchard L, Guerlesquin F, Gavioli M, Simorre JP, Lazdunski C, Marion D, Lloubès R. </i> Biochemistry, 2002","statement":[{"text":"The HSQC spectra of 15N-labeled ATh result in a significant amount of poorly dispersed signals superimposing in the middle of the spectra (Figure 5), confirming this lack of structure, which is in agreement with the CD data.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"tszani","start":1,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T09:48:19.135Z","curator_name":"Federica Quaglia"},"reference_id":"11851406","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP01852r004","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T10:45:31.976Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":172,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":1,"version":4,"statement":[{"text":"The  HSQC  spectrum  of 15N-labeled  TolAIII3  is significantly altered after addition of unlabeled ATh.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P19934","partner_end":null}],"term_name":"protein binding","reference_html":"Macromolecular import into Escherichia coli: the TolA C-terminal domain changes conformation when interacting with the colicin A toxin. <i> Deprez C, Blanchard L, Guerlesquin F, Gavioli M, Simorre JP, Lazdunski C, Marion D, Lloubès R. </i> Biochemistry, 2002","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"11851406","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"rpancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":172,"term_name":"molecular adaptor activity","reference_html":"Macromolecular import into Escherichia coli: the TolA C-terminal domain changes conformation when interacting with the colicin A toxin. <i> Deprez C, Blanchard L, Guerlesquin F, Gavioli M, Simorre JP, Lazdunski C, Marion D, Lloubès R. </i> Biochemistry, 2002","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":4,"term_id":"GO:0060090","curator_id":"rpancsa","start":1,"term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"11851406","statement":[{"text":"Here  we  show  that  in  vitro  the  translocation  domain  of colicin  A  has  a  strongly  perturbing  effect  on  the  tertiary structure of TolAIII, and thus presumably also on the whole Tol-Pal system within the periplasm of E. coli.","type":"Discussion"}],"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T10:21:49.129Z","curator_name":"Federica Quaglia"},"released":"2022_03","region_id":"DP01852r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01852r006","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T10:45:33.739Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":172,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"Purified TolAIII2 and TolAIII3 were analyzed by a Western blot and dot blot, which were incubated with 200 nM ATh followed by immunodetection with 1C11 monoclonal antibody (mAb) directed against the colicin domain. Under these conditions, the ATh protein was found to recognize TolAIII2 and TolAIII3.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P19934","partner_end":null}],"term_name":"protein binding","ec_name":"immunodetection assay evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"11851406","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0007719","curator_id":"rpancsa","reference_html":"Macromolecular import into Escherichia coli: the TolA C-terminal domain changes conformation when interacting with the colicin A toxin. <i> Deprez C, Blanchard L, Guerlesquin F, Gavioli M, Simorre JP, Lazdunski C, Marion D, Lloubès R. </i> Biochemistry, 2002","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01852r007","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T10:45:36.313Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":172,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"Immunoprecipitation experiments using mAb 1C11, which recognizes an epitope located within the N-terminal sequenceof ATh, were also checked with ATh and TolAIII derivative mixtures.  Coomassie  blue-stained  SDS-PAGE  analyses indicated that TolAIII2 and TolAIII3 co-immunoprecipitate with ATh","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P19934","partner_end":null}],"term_name":"protein binding","ec_name":"co-immunoprecipitation evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"11851406","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006030","curator_id":"rpancsa","reference_html":"Macromolecular import into Escherichia coli: the TolA C-terminal domain changes conformation when interacting with the colicin A toxin. <i> Deprez C, Blanchard L, Guerlesquin F, Gavioli M, Simorre JP, Lazdunski C, Marion D, Lloubès R. </i> Biochemistry, 2002","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01852r008","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T10:45:39.047Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":172,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"SDS-PAGE shift experiments(30) were performed with the purified ATh and TolAIII3. A TolAIII3-ATh protein complex could be clearly detected having a relative electrophoretic mobility corresponding to a heterodimer, while this complex slightly dissociated into monomeric forms upon migration (Figure 6).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P19934","partner_end":null}],"term_name":"protein binding","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"11851406","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0007689","curator_id":"rpancsa","reference_html":"Macromolecular import into Escherichia coli: the TolA C-terminal domain changes conformation when interacting with the colicin A toxin. <i> Deprez C, Blanchard L, Guerlesquin F, Gavioli M, Simorre JP, Lazdunski C, Marion D, Lloubès R. </i> Biochemistry, 2002","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01852r009","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T10:45:45.059Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":172,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"Gel  filtration  experiments  using  ATh,  TolAIII3,  and TolAIII3 with ATh, loaded at the same concentration and in the same buffer used for NMR interaction analyses, further indicated the formation of a heterodimer.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P19934","partner_end":null}],"term_name":"protein binding","ec_name":"chromatography evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"11851406","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0007680","curator_id":"rpancsa","reference_html":"Macromolecular import into Escherichia coli: the TolA C-terminal domain changes conformation when interacting with the colicin A toxin. <i> Deprez C, Blanchard L, Guerlesquin F, Gavioli M, Simorre JP, Lazdunski C, Marion D, Lloubès R. </i> Biochemistry, 2002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01852r010","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T10:19:52.074Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":20,"term_id":"GO:0005515","start":9,"version":3,"statement":[{"text":"Structure of the TA1–107–TolB complex at 2.6 Å resolution showing the colicin binding site of the β-propeller domain.","type":"Figure"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P0A855","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"19627502","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3IAX"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"rpancsa","reference_html":"The crystal structure of the TolB box of colicin A in complex with TolB reveals important differences in the recruitment of the common TolB translocation portal used by group A colicins. <i> Zhang Y, Li C, Vankemmelbeke MN, Bardelang P, Paoli M, Penfold CN, James R. </i> Mol Microbiol, 2010","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP01852r011","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T10:46:07.668Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":172,"term_id":"GO:0051179","start":1,"version":3,"statement":[{"text":"Prior to their action, the import of colicins is mediated by their binding to specific receptors of the outer membrane, and their translocation through the cell envelope which requires either the Tol-Pal system (group A colicins) or the TonB system(group B colicins) (15). The three-dimensional structure of several of these toxins shows a similar type of organization(16-19). It comprises three distinct domains:  the N-terminal domain   involved   in   the   translocation   across   the   outer membrane, the central domain or receptor binding domain,and  the  C-terminal  domain  that  is  responsible  for  lethal activity. Membrane fractionation shows that the Tol proteins form a complex with imported colicin A (20) and that, during pore formation, colicin A retains interactions with its receptor and the Tol machinery (21).","type":"Introduction"}],"term_name":"localization","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"11851406","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Biological process","ec_id":"ECO:0006218","curator_id":"rpancsa","reference_html":"Macromolecular import into Escherichia coli: the TolA C-terminal domain changes conformation when interacting with the colicin A toxin. <i> Deprez C, Blanchard L, Guerlesquin F, Gavioli M, Simorre JP, Lazdunski C, Marion D, Lloubès R. </i> Biochemistry, 2002","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2018_11","uniref100":"UniRef100_P04480","date":"2018-08-14T11:41:41.000Z","acc":"P04480","name":"Colicin-A","length":592,"organism":"Citrobacter freundii","UniParc":"UPI0000127499","genes":[{"name":{"value":"caa"}}],"alphafold_very_low_content":0.11486486486486487,"disorder_content":0.2905405405405405,"disprot_consensus":{"full":[{"start":1,"end":172,"type":"D"}],"Structural state":[{"start":1,"end":172,"type":"D"}],"Molecular function":[{"start":1,"end":172,"type":"F"}],"Biological process":[{"start":1,"end":172,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00257","name":"Dehydrin","start":29,"end":130}]},"uniref50":"UniRef50_Q3ZNL4","sequence":"MAYQQDPCANPTRQTGKTGGQTDQYGNPVHQTEALGAYGAGTGTGMHGGEHQQQPHQQPGVLHRSGSSSSEDDGQGGRRKKGMKEKIKERIPGMGRKDEQKQTSATSTPGQGQQQKGMMEKIKEKLPGAH","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","Vitales","Vitaceae","Viteae","Vitis"],"uniref90":"UniRef90_Q3ZNL4","disprot_id":"DP01854","ncbi_taxon_id":96939,"regions_counter":4,"creator":"grivas","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":93,"region_id":"DP01854r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Cryoprotective mechanism of a small intrinsically disordered dehydrin protein. <i> Hughes S, Graether SP. </i> Protein Sci, 2011","statement":[{"text":"As an IDP, all of K2 is flexible but the K-segments show a weak tendency for forming an a- helix, whereas the Φ-segment has no clear secondary structure preference and is even more flexible than the K-regions","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"achasapi","start":83,"term_ontology":"IDPO","curator_name":"Anastasia Chasapi","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1986-5007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21031484","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":113,"region_id":"DP01854r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Cryoprotective mechanism of a small intrinsically disordered dehydrin protein. <i> Hughes S, Graether SP. </i> Protein Sci, 2011","statement":[{"text":"As an IDP, all of K2 is flexible but the K-segments show a weak tendency for forming an a- helix, whereas the Φ-segment has no clear secondary structure preference and is even more flexible than the K-regions","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"achasapi","start":93,"term_ontology":"IDPO","curator_name":"Anastasia Chasapi","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1986-5007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21031484","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":130,"region_id":"DP01854r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Cryoprotective mechanism of a small intrinsically disordered dehydrin protein. <i> Hughes S, Graether SP. </i> Protein Sci, 2011","statement":[{"text":"As an IDP, all of K2 is flexible but the K-segments show a weak tendency for forming an a- helix, whereas the Φ-segment has no clear secondary structure preference and is even more flexible than the K-regions","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"achasapi","start":114,"term_ontology":"IDPO","curator_name":"Anastasia Chasapi","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1986-5007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21031484","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":130,"region_id":"DP01854r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Cryoprotective mechanism of a small intrinsically disordered dehydrin protein. <i> Hughes S, Graether SP. </i> Protein Sci, 2011","statement":[{"text":"As an IDP, all of K2 is flexible but the K-segments show a weak tendency for forming an a- helix, whereas the Φ-segment has no clear secondary structure preference and is even more flexible than the K-regions","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"achasapi","start":83,"term_ontology":"IDPO","curator_name":"Anastasia Chasapi","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1986-5007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21031484","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9M605","date":"2018-08-14T14:00:09.000Z","acc":"Q9M605","name":"Dehydrin 1","length":130,"organism":"Vitis riparia","dataset":[],"UniParc":"UPI00000A9854","genes":[{"name":{"value":"Dhn","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF37268.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF37268.1"}}]},"synonyms":[{"value":"DHN1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AFG16902.1","url":"https://www.ebi.ac.uk/ena/browser/view/AFG16902.1"}}]}]}],"alphafold_very_low_content":0.33076923076923076,"disorder_content":0.36923076923076925,"disprot_consensus":{"full":[{"start":83,"end":130,"type":"D"}],"Structural state":[{"start":83,"end":130,"type":"D"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MEDLDQSPLVSSSDSPPRPQPAFKYQFVREPEDEEEEEEEEEEDEDEDLEELEVLERKPAAGLSAAPVPTAPAAGAPLMDFGNDFVPPAPRGPLPAAPPVAPERQPSWDPSPVSSTVPAPSPLSAAAVSPSKLPEDDEPPARPPPPPPASVSPQAEPVWTPPAPAPAAPPSTPAAPKRRGSSGSVDETLFALPAASEPVIRSSAENMDLKEQPGNTISAGQEDFPSVLLETAASLPSLSPLSAASFKEHEYLGNLSTVLPTEGTLQENVSEASKEVSEKAKTLLIDRDLTEFSELEYSEMGSSFSVSPKAESAVIVANPREEIIVKNKDEEEKLVSNNILHNQQELPTALTKLVKEDEVVSSEKAKDSFNEKRVAVEAPMREEYADFKPFERVWEVKDSKEDSDMLAAGGKIESNLESKVDKKCFADSLEQTNHEKDSESSNDDTSFPSTPEGIKDRSGAYITCAPFNPAATESIATNIFPLLGDPTSENKTDEKKIEEKKAQIVTEKNTSTKTSNPFLVAAQDSETDYVTTDNLTKVTEEVVANMPEGLTPDLVQEACESELNEVTGTKIAYETKMDLVQTSEVMQESLYPAAQLCPSFEESEATPSPVLPDIVMEAPLNSAVPSAGASVIQPSSSPLEASSVNYESIKHEPENPPPYEEAMSVSLKKVSGIKEEIKEPENINAALQETEAPYISIACDLIKETKLSAEPAPDFSDYSEMAKVEQPVPDHSELVEDSSPDSEPVDLFSDDSIPDVPQKQDETVMLVKESLTETSFESMIEYENKEKLSALPPEGGKPYLESFKLSLDNTKDTLLPDEVSTLSKKEKIPLQMEELSTAVYSNDDLFISKEAQIRETETFSDSSPIEIIDEFPTLISSKTDSFSKLAREYTDLEVSHKSEIANAPDGAGSLPCTELPHDLSLKNIQPKVEEKISFSDDFSKNGSATSKVLLLPPDVSALATQAEIESIVKPKVLVKEAEKKLPSDTEKEDRSPSAIFSAELSKTSVVDLLYWRDIKKTGVVFGASLFLLLSLTVFSIVSVTAYIALALLSVTISFRIYKGVIQAIQKSDEGHPFRAYLESEVAISEELVQKYSNSALGHVNCTIKELRRLFLVDDLVDSLKFAVLMWVFTYVGALFNGLTLLILALISLFSVPVIYERHQAQIDHYLGLANKNVKDAMAKIQAKIPGLKRKAE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"","disprot_id":"DP01855","ncbi_taxon_id":9606,"regions_counter":46,"creator":"bhajdu","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":748,"region_id":"DP01855r006","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structural characterization of the human Nogo-A functional domains. Solution structure of Nogo-40, a Nogo-66 receptor antagonist enhancing injured spinal cord regeneration. <i> Li M, Shi J, Wei Z, Teng FY, Tang BL, Song J. </i> Eur J Biochem, 2004","statement":[{"text":"The structural properties of Nogo‐A(567–748) were first investigated by CD spectroscopy. As shown in Fig. 3A, the CD spectrum of Nogo‐A(567–748) in aqueous buffer had a maximal negative peak at ≈202 nm and had no significant positive signal at 198 nm, indicating that the polypeptide was not fully structured [[23]]. However, the existence of the maximal negative signal at around 202 nm, rather than 198 nm, together with the negative shoulder signal at ≈225 nm, indicated that the polypeptide was also not assuming a ‘random coil’ structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":567,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"15317586","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:00.925Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1187,"region_id":"DP01855r009","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","statement":[{"text":"Similarly, Nogo-33 identical for all three Nogo proteinswas predicated [Fig. 2(a)] and subsequently experimentally shown to be highly disordered as judged from its far-UV CD [Fig. 4(a)] and narrowly-dispersed HSQC spectrum (only 0.5 ppm over 1H and 19 ppm over 15N dimensions) [Fig. 4(b)].","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":1155,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17397058","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:02.347Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1094,"region_id":"DP01855r010","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural characterization of the human Nogo-A functional domains. Solution structure of Nogo-40, a Nogo-66 receptor antagonist enhancing injured spinal cord regeneration. <i> Li M, Shi J, Wei Z, Teng FY, Tang BL, Song J. </i> Eur J Biochem, 2004","statement":[{"text":"NMR spectroscopy was further utilized to explore the structural properties of Nogo‐40. The very narrow resonance dispersion of amide protons (≈0.7p.p.m) and the lack of side‐chain packing with aromatic ring protons in aqueous buffer (Fig. 5C) demonstrate that Nogo‐40 in aqueous buffer had no stable structure, which is consistent with the CD results above. ","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":1055,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"15317586","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:03.809Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1187,"region_id":"DP01855r011","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","statement":[{"text":"Similarly, Nogo-33 identical for all three Nogo proteinswas predicated [Fig. 2(a)] and subsequently experimentally shown to be highly disordered as judged from its far-UV CD [Fig. 4(a)] and narrowly-dispersed HSQC spectrum (only 0.5 ppm over 1H and 19 ppm over 15N dimensions) [Fig. 4(b)].","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bmesza","start":1155,"term_ontology":"IDPO","curator_name":"Bálint Mészáros","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0919-4449","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17397058","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:05.157Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":31,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r012","statement":[{"text":"Unfortunately we found that the first 31 residues were amenable to cellular proteolysis which made it very difficult to obtain the entire Nogo-B (1–200). This observation suggests that Nogo-B is highly disordered because disordered proteins have been extensively found to be very sensitive to proteolytic digestion.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:06.481Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":1,"end":200,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r013","statement":[{"text":"As seen in Fig. 3(a), Nogo-B (1–200) and Nogo-B (32–200) owned very similar far-UV CD spectra with a negative signal at198 nm and without any positive signal at190 nm. This observation clearly indicated that both Nogo-B (1–200) and Nogo-B (32–200) were lacking predominant secondary structures in solution","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:08.288Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":32,"end":200,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006206","ec_ontology":"ECO","ec_name":"near-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r014","statement":[{"text":"We then recorded the near-UV CD spectra of Nogo-B (32–200) in the absence and presence of 8M denaturant urea [Fig. 3(b)]. The high similarity between two near-UV spectra suggested that the N-terminus of Nogo-B had no tight tertiary packing even under the native condition.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:09.016Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":200,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r015","statement":[{"text":"Completely consistent with CD results, 1H15N NMR HSQC spectra of both Nogo-B (1–200) and Nogo-B (32–200) were very similar, with very narrow spectral dispersions over both dimensions (1 ppm over 1H and 20ppm over 15N dimensions) [Fig. 3(c)]. Moreover, no significant change in the spectral dispersion and peak numberswere observed for 1H15N NMR HSQC spectra of Nogo-B(32–200) in the absence and in presence of 8Murea [Fig.3(d)]. These results provided the strongest evidence that both Nogo-B (1–200) and Nogo-B (32–200) were highly disordered with no tight tertiary packing.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:10.288Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":32,"end":200,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006196","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r016","statement":[{"text":"Hydrogen exchange experiment offers a very sensitiveprobe to detect tertiary packing property. When the 15N-labeled Nogo-B (32–200) was lyophilized and redissolved in 100% D2O, all HSQC peaks disappeared withinthe experimental dead time (spectrum not shown). This result again indicated that Nogo-B (32–200) was highly flexible in solution and all of its amide protons were openly accessible to the bulk solvent.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:11.755Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":200,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r017","statement":[{"text":"Consequently, we dissected Nogo-A (201–1016) into two sets of overlapped fragments,with each set having four 200 residue fragments as the size of autonomous protein folding domains usually ranges from120 to 200 residues. The two sets of dissected Nogo-A fragments P1-P8 were successfully expressed and purified by HPLC. Very interestingly, the apparent molecular weights of all eight fragments as estimated from SDS-PAGE were 1.5 times larger than those calculated from their sequences. Moreover, the same phenomenon was observed for Nogo-B (1–200) and Nogo-B (32–200). This observation could serve as evidence that these Nogo fragments are intrinsically unstructured because previously this abnormal behavior on SDS-PAGE was proposed as anindicator of intrinsically unstructured proteins.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:12.822Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":210,"end":408,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r018","statement":[{"text":"Consequently, we dissected Nogo-A (201–1016) into two sets of overlapped fragments,with each set having four 200 residue fragments as the size of autonomous protein folding domains usually ranges from120 to 200 residues. The two sets of dissected Nogo-A fragments P1-P8 were successfully expressed and purified by HPLC. Very interestingly, the apparent molecular weights of all eight fragments as estimated from SDS-PAGE were 1.5 times larger than those calculated from their sequences. Moreover, the same phenomenon was observed for Nogo-B (1–200) and Nogo-B (32–200). This observation could serve as evidence that these Nogo fragments are intrinsically unstructured because previously this abnormal behavior on SDS-PAGE was proposed as anindicator of intrinsically unstructured proteins.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:14.222Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":409,"end":616,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r019","statement":[{"text":"Consequently, we dissected Nogo-A (201–1016) into two sets of overlapped fragments,with each set having four 200 residue fragments as the size of autonomous protein folding domains usually ranges from120 to 200 residues. The two sets of dissected Nogo-A fragments P1-P8 were successfully expressed and purified by HPLC. Very interestingly, the apparent molecular weights of all eight fragments as estimated from SDS-PAGE were 1.5 times larger than those calculated from their sequences. Moreover, the same phenomenon was observed for Nogo-B (1–200) and Nogo-B (32–200). This observation could serve as evidence that these Nogo fragments are intrinsically unstructured because previously this abnormal behavior on SDS-PAGE was proposed as anindicator of intrinsically unstructured proteins.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:16.211Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":617,"end":824,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r020","statement":[{"text":"Consequently, we dissected Nogo-A (201–1016) into two sets of overlapped fragments,with each set having four 200 residue fragments as the size of autonomous protein folding domains usually ranges from120 to 200 residues. The two sets of dissected Nogo-A fragments P1-P8 were successfully expressed and purified by HPLC. Very interestingly, the apparent molecular weights of all eight fragments as estimated from SDS-PAGE were 1.5 times larger than those calculated from their sequences. Moreover, the same phenomenon was observed for Nogo-B (1–200) and Nogo-B (32–200). This observation could serve as evidence that these Nogo fragments are intrinsically unstructured because previously this abnormal behavior on SDS-PAGE was proposed as anindicator of intrinsically unstructured proteins.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:17.001Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":825,"end":1016,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r021","statement":[{"text":"Consequently, we dissected Nogo-A (201–1016) into two sets of overlapped fragments,with each set having four 200 residue fragments as the size of autonomous protein folding domains usually ranges from120 to 200 residues. The two sets of dissected Nogo-A fragments P1-P8 were successfully expressed and purified by HPLC. Very interestingly, the apparent molecular weights of all eight fragments as estimated from SDS-PAGE were 1.5 times larger than those calculated from their sequences. Moreover, the same phenomenon was observed for Nogo-B (1–200) and Nogo-B (32–200). This observation could serve as evidence that these Nogo fragments are intrinsically unstructured because previously this abnormal behavior on SDS-PAGE was proposed as anindicator of intrinsically unstructured proteins.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:18.455Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":210,"end":358,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r022","statement":[{"text":"Consequently, we dissected Nogo-A (201–1016) into two sets of overlapped fragments,with each set having four 200 residue fragments as the size of autonomous protein folding domains usually ranges from120 to 200 residues. The two sets of dissected Nogo-A fragments P1-P8 were successfully expressed and purified by HPLC. Very interestingly, the apparent molecular weights of all eight fragments as estimated from SDS-PAGE were 1.5 times larger than those calculated from their sequences. Moreover, the same phenomenon was observed for Nogo-B (1–200) and Nogo-B (32–200). This observation could serve as evidence that these Nogo fragments are intrinsically unstructured because previously this abnormal behavior on SDS-PAGE was proposed as anindicator of intrinsically unstructured proteins.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:19.670Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":359,"end":566,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r023","statement":[{"text":"Consequently, we dissected Nogo-A (201–1016) into two sets of overlapped fragments,with each set having four 200 residue fragments as the size of autonomous protein folding domains usually ranges from120 to 200 residues. The two sets of dissected Nogo-A fragments P1-P8 were successfully expressed and purified by HPLC. Very interestingly, the apparent molecular weights of all eight fragments as estimated from SDS-PAGE were 1.5 times larger than those calculated from their sequences. Moreover, the same phenomenon was observed for Nogo-B (1–200) and Nogo-B (32–200). This observation could serve as evidence that these Nogo fragments are intrinsically unstructured because previously this abnormal behavior on SDS-PAGE was proposed as anindicator of intrinsically unstructured proteins.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:20.371Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":567,"end":774,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r024","statement":[{"text":"Consequently, we dissected Nogo-A (201–1016) into two sets of overlapped fragments,with each set having four 200 residue fragments as the size of autonomous protein folding domains usually ranges from120 to 200 residues. The two sets of dissected Nogo-A fragments P1-P8 were successfully expressed and purified by HPLC. Very interestingly, the apparent molecular weights of all eight fragments as estimated from SDS-PAGE were 1.5 times larger than those calculated from their sequences. Moreover, the same phenomenon was observed for Nogo-B (1–200) and Nogo-B (32–200). This observation could serve as evidence that these Nogo fragments are intrinsically unstructured because previously this abnormal behavior on SDS-PAGE was proposed as anindicator of intrinsically unstructured proteins.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:21.939Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":775,"end":1016,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r025","statement":[{"text":"Consequently, we dissected Nogo-A (201–1016) into two sets of overlapped fragments,with each set having four 200 residue fragments as the size of autonomous protein folding domains usually ranges from120 to 200 residues. The two sets of dissected Nogo-A fragments P1-P8 were successfully expressed and purified by HPLC. Very interestingly, the apparent molecular weights of all eight fragments as estimated from SDS-PAGE were 1.5 times larger than those calculated from their sequences. Moreover, the same phenomenon was observed for Nogo-B (1–200) and Nogo-B (32–200). This observation could serve as evidence that these Nogo fragments are intrinsically unstructured because previously this abnormal behavior on SDS-PAGE was proposed as anindicator of intrinsically unstructured proteins.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:23.392Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":210,"end":408,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r026","statement":[{"text":"Figure 5 shows the far-UV CD and HSQC spectra of the first set of four fragments P1-P4 spanning over the Nogo-A residues 201–1016. Similar to those observed for Nogo-B, all four fragments had far-UV CD spectra typical of disordered proteins and their HSQC spectra showed sharp resonance peaks distributed within very narrow spectral dispersions. Therefore the results indicated that this set of fragments owned no populated secondary structures and tight tertiary packing. Moreover, the second group of the fragments P5-P8 dissected in a very different way also gave rise to far-UV CD and HSQC spectra characteristic of disordered proteins (Fig. 6), again indicating that the second group of fragments were also largely disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:24.194Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":409,"end":616,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r027","statement":[{"text":"Figure 5 shows the far-UV CD and HSQC spectra of the first set of four fragments P1-P4 spanning over the Nogo-A residues 201–1016. Similar to those observed for Nogo-B, all four fragments had far-UV CD spectra typical of disordered proteins and their HSQC spectra showed sharp resonance peaks distributed within very narrow spectral dispersions. Therefore the results indicated that this set of fragments owned no populated secondary structures and tight tertiary packing. Moreover, the second group of the fragments P5-P8 dissected in a very different way also gave rise to far-UV CD and HSQC spectra characteristic of disordered proteins (Fig. 6), again indicating that the second group of fragments were also largely disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:25.577Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":617,"end":824,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r028","statement":[{"text":"Figure 5 shows the far-UV CD and HSQC spectra of the first set of four fragments P1-P4 spanning over the Nogo-A residues 201–1016. Similar to those observed for Nogo-B, all four fragments had far-UV CD spectra typical of disordered proteins and their HSQC spectra showed sharp resonance peaks distributed within very narrow spectral dispersions. Therefore the results indicated that this set of fragments owned no populated secondary structures and tight tertiary packing. Moreover, the second group of the fragments P5-P8 dissected in a very different way also gave rise to far-UV CD and HSQC spectra characteristic of disordered proteins (Fig. 6), again indicating that the second group of fragments were also largely disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:26.356Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":825,"end":1016,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r029","statement":[{"text":"Figure 5 shows the far-UV CD and HSQC spectra of the first set of four fragments P1-P4 spanning over the Nogo-A residues 201–1016. Similar to those observed for Nogo-B, all four fragments had far-UV CD spectra typical of disordered proteins and their HSQC spectra showed sharp resonance peaks distributed within very narrow spectral dispersions. Therefore the results indicated that this set of fragments owned no populated secondary structures and tight tertiary packing. Moreover, the second group of the fragments P5-P8 dissected in a very different way also gave rise to far-UV CD and HSQC spectra characteristic of disordered proteins (Fig. 6), again indicating that the second group of fragments were also largely disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:27.824Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":210,"end":358,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r030","statement":[{"text":"Figure 5 shows the far-UV CD and HSQC spectra of the first set of four fragments P1-P4 spanning over the Nogo-A residues 201–1016. Similar to those observed for Nogo-B, all four fragments had far-UV CD spectra typical of disordered proteins and their HSQC spectra showed sharp resonance peaks distributed within very narrow spectral dispersions. Therefore the results indicated that this set of fragments owned no populated secondary structures and tight tertiary packing. Moreover, the second group of the fragments P5-P8 dissected in a very different way also gave rise to far-UV CD and HSQC spectra characteristic of disordered proteins (Fig. 6), again indicating that the second group of fragments were also largely disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:29.208Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":359,"end":566,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r031","statement":[{"text":"Figure 5 shows the far-UV CD and HSQC spectra of the first set of four fragments P1-P4 spanning over the Nogo-A residues 201–1016. Similar to those observed for Nogo-B, all four fragments had far-UV CD spectra typical of disordered proteins and their HSQC spectra showed sharp resonance peaks distributed within very narrow spectral dispersions. Therefore the results indicated that this set of fragments owned no populated secondary structures and tight tertiary packing. Moreover, the second group of the fragments P5-P8 dissected in a very different way also gave rise to far-UV CD and HSQC spectra characteristic of disordered proteins (Fig. 6), again indicating that the second group of fragments were also largely disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:30.372Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":567,"end":774,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r032","statement":[{"text":"Figure 5 shows the far-UV CD and HSQC spectra of the first set of four fragments P1-P4 spanning over the Nogo-A residues 201–1016. Similar to those observed for Nogo-B, all four fragments had far-UV CD spectra typical of disordered proteins and their HSQC spectra showed sharp resonance peaks distributed within very narrow spectral dispersions. Therefore the results indicated that this set of fragments owned no populated secondary structures and tight tertiary packing. Moreover, the second group of the fragments P5-P8 dissected in a very different way also gave rise to far-UV CD and HSQC spectra characteristic of disordered proteins (Fig. 6), again indicating that the second group of fragments were also largely disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:31.658Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":775,"end":1016,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r033","statement":[{"text":"Figure 5 shows the far-UV CD and HSQC spectra of the first set of four fragments P1-P4 spanning over the Nogo-A residues 201–1016. Similar to those observed for Nogo-B, all four fragments had far-UV CD spectra typical of disordered proteins and their HSQC spectra showed sharp resonance peaks distributed within very narrow spectral dispersions. Therefore the results indicated that this set of fragments owned no populated secondary structures and tight tertiary packing. Moreover, the second group of the fragments P5-P8 dissected in a very different way also gave rise to far-UV CD and HSQC spectra characteristic of disordered proteins (Fig. 6), again indicating that the second group of fragments were also largely disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:33.851Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":210,"end":408,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r034","statement":[{"text":"Figure 5 shows the far-UV CD and HSQC spectra of the first set of four fragments P1-P4 spanning over the Nogo-A residues 201–1016. Similar to those observed for Nogo-B, all four fragments had far-UV CD spectra typical of disordered proteins and their HSQC spectra showed sharp resonance peaks distributed within very narrow spectral dispersions. Therefore the results indicated that this set of fragments owned no populated secondary structures and tight tertiary packing. Moreover, the second group of the fragments P5-P8 dissected in a very different way also gave rise to far-UV CD and HSQC spectra characteristic of disordered proteins (Fig. 6), again indicating that the second group of fragments were also largely disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:34.919Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":409,"end":616,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r035","statement":[{"text":"Figure 5 shows the far-UV CD and HSQC spectra of the first set of four fragments P1-P4 spanning over the Nogo-A residues 201–1016. Similar to those observed for Nogo-B, all four fragments had far-UV CD spectra typical of disordered proteins and their HSQC spectra showed sharp resonance peaks distributed within very narrow spectral dispersions. Therefore the results indicated that this set of fragments owned no populated secondary structures and tight tertiary packing. Moreover, the second group of the fragments P5-P8 dissected in a very different way also gave rise to far-UV CD and HSQC spectra characteristic of disordered proteins (Fig. 6), again indicating that the second group of fragments were also largely disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:37.324Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":617,"end":824,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r036","statement":[{"text":"Figure 5 shows the far-UV CD and HSQC spectra of the first set of four fragments P1-P4 spanning over the Nogo-A residues 201–1016. Similar to those observed for Nogo-B, all four fragments had far-UV CD spectra typical of disordered proteins and their HSQC spectra showed sharp resonance peaks distributed within very narrow spectral dispersions. Therefore the results indicated that this set of fragments owned no populated secondary structures and tight tertiary packing. Moreover, the second group of the fragments P5-P8 dissected in a very different way also gave rise to far-UV CD and HSQC spectra characteristic of disordered proteins (Fig. 6), again indicating that the second group of fragments were also largely disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:38.722Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":825,"end":1016,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r037","statement":[{"text":"Figure 5 shows the far-UV CD and HSQC spectra of the first set of four fragments P1-P4 spanning over the Nogo-A residues 201–1016. Similar to those observed for Nogo-B, all four fragments had far-UV CD spectra typical of disordered proteins and their HSQC spectra showed sharp resonance peaks distributed within very narrow spectral dispersions. Therefore the results indicated that this set of fragments owned no populated secondary structures and tight tertiary packing. Moreover, the second group of the fragments P5-P8 dissected in a very different way also gave rise to far-UV CD and HSQC spectra characteristic of disordered proteins (Fig. 6), again indicating that the second group of fragments were also largely disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:39.417Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":210,"end":358,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r038","statement":[{"text":"Figure 5 shows the far-UV CD and HSQC spectra of the first set of four fragments P1-P4 spanning over the Nogo-A residues 201–1016. Similar to those observed for Nogo-B, all four fragments had far-UV CD spectra typical of disordered proteins and their HSQC spectra showed sharp resonance peaks distributed within very narrow spectral dispersions. Therefore the results indicated that this set of fragments owned no populated secondary structures and tight tertiary packing. Moreover, the second group of the fragments P5-P8 dissected in a very different way also gave rise to far-UV CD and HSQC spectra characteristic of disordered proteins (Fig. 6), again indicating that the second group of fragments were also largely disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:41.172Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":359,"end":566,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r039","statement":[{"text":"Figure 5 shows the far-UV CD and HSQC spectra of the first set of four fragments P1-P4 spanning over the Nogo-A residues 201–1016. Similar to those observed for Nogo-B, all four fragments had far-UV CD spectra typical of disordered proteins and their HSQC spectra showed sharp resonance peaks distributed within very narrow spectral dispersions. Therefore the results indicated that this set of fragments owned no populated secondary structures and tight tertiary packing. Moreover, the second group of the fragments P5-P8 dissected in a very different way also gave rise to far-UV CD and HSQC spectra characteristic of disordered proteins (Fig. 6), again indicating that the second group of fragments were also largely disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:42.106Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":567,"end":774,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r040","statement":[{"text":"Figure 5 shows the far-UV CD and HSQC spectra of the first set of four fragments P1-P4 spanning over the Nogo-A residues 201–1016. Similar to those observed for Nogo-B, all four fragments had far-UV CD spectra typical of disordered proteins and their HSQC spectra showed sharp resonance peaks distributed within very narrow spectral dispersions. Therefore the results indicated that this set of fragments owned no populated secondary structures and tight tertiary packing. Moreover, the second group of the fragments P5-P8 dissected in a very different way also gave rise to far-UV CD and HSQC spectra characteristic of disordered proteins (Fig. 6), again indicating that the second group of fragments were also largely disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:43.372Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":775,"end":1016,"reference_id":"17397058","reference_source":"pmid","reference_html":"The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. <i> Li M, Song J. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r041","statement":[{"text":"Figure 5 shows the far-UV CD and HSQC spectra of the first set of four fragments P1-P4 spanning over the Nogo-A residues 201–1016. Similar to those observed for Nogo-B, all four fragments had far-UV CD spectra typical of disordered proteins and their HSQC spectra showed sharp resonance peaks distributed within very narrow spectral dispersions. Therefore the results indicated that this set of fragments owned no populated secondary structures and tight tertiary packing. Moreover, the second group of the fragments P5-P8 dissected in a very different way also gave rise to far-UV CD and HSQC spectra characteristic of disordered proteins (Fig. 6), again indicating that the second group of fragments were also largely disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:44.409Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":567,"end":748,"reference_id":"15317586","reference_source":"pmid","reference_html":"Structural characterization of the human Nogo-A functional domains. Solution structure of Nogo-40, a Nogo-66 receptor antagonist enhancing injured spinal cord regeneration. <i> Li M, Shi J, Wei Z, Teng FY, Tang BL, Song J. </i> Eur J Biochem, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r042","statement":[{"text":"To explore whether Nogo‐A(567–748) had any specific interaction with metal ions, we utilized CD measurements to monitor conformational changes induced by the addition of metal ions, including Ca2+, Mg2+, Cu2+, Ni2+ and Zn2+. Only Zn2+ was able to induce a significant conformational change in the polypeptide. As shown in Fig. 3A, the CD spectrum of Nogo‐A(567–748) with dual negative signals at ≈206 and 221nm in the presence of 4mm Zn2+ resembles that for a typical helical protein. The results indicate that Zn2+ could specifically induce, to a significant degree, the polypeptide to assume a helical conformation.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":567,"end":748,"reference_id":"15317586","reference_source":"pmid","reference_html":"Structural characterization of the human Nogo-A functional domains. Solution structure of Nogo-40, a Nogo-66 receptor antagonist enhancing injured spinal cord regeneration. <i> Li M, Shi J, Wei Z, Teng FY, Tang BL, Song J. </i> Eur J Biochem, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01855r043","statement":[{"text":"To explore whether Nogo‐A(567–748) had any specific interaction with metal ions, we utilized CD measurements to monitor conformational changes induced by the addition of metal ions, including Ca2+, Mg2+, Cu2+, Ni2+ and Zn2+. Only Zn2+ was able to induce a significant conformational change in the polypeptide. As shown in Fig. 3A, the CD spectrum of Nogo‐A(567–748) with dual negative signals at ≈206 and 221nm in the presence of 4mm Zn2+ resembles that for a typical helical protein. The results indicate that Zn2+ could specifically induce, to a significant degree, the polypeptide to assume a helical conformation.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":567,"end":748,"reference_id":"15317586","reference_source":"pmid","reference_html":"Structural characterization of the human Nogo-A functional domains. Solution structure of Nogo-40, a Nogo-66 receptor antagonist enhancing injured spinal cord regeneration. <i> Li M, Shi J, Wei Z, Teng FY, Tang BL, Song J. </i> Eur J Biochem, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01855r044","statement":[{"text":"Interestingly, upon addition of 4mm Zn2+, no new HSQC peaks appeared but the intensities of the existing peaks became stronger (spectrum not shown). This observation suggests that although the introduction of Zn2+ was able to significantly enhance the helical structure of Nogo‐A(567–748) as detected by CD, it was not sufficient to make the tertiary packing as tight as those found in a well‐structured protein. ","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":567,"end":748,"reference_id":"15317586","reference_source":"pmid","reference_html":"Structural characterization of the human Nogo-A functional domains. Solution structure of Nogo-40, a Nogo-66 receptor antagonist enhancing injured spinal cord regeneration. <i> Li M, Shi J, Wei Z, Teng FY, Tang BL, Song J. </i> Eur J Biochem, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r045","statement":[{"text":"As shown in Fig. 3B, the poor chemical dispersions of the spectrum at both 1H and 15N dimensions indicated that Nogo‐A(567–748) did not have a tight side‐chain packing. In particular, the number of observed NMR cross peaks was only about 35, much less than expected for a 182 residue protein, thus indicating that slow conformational exchanges existed over most regions of the protein. Usually, slow conformational exchange would result in significant line‐broadening for HSQC peaks and make these peaks undetectable. The manifested HSQC peaks in Fig. 3B most likely resulted from the unstructured and flexible regions of the Nogo‐A(567–748), while the peaks for the regions undergoing slow conformational changes were undetectable. The results above indicated that Nogo‐A(567–748) was partially structured, probably with some properties characteristic of molten globule states [[24-27]].","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:49.322Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1055,"end":1094,"reference_id":"15317586","reference_source":"pmid","reference_html":"Structural characterization of the human Nogo-A functional domains. Solution structure of Nogo-40, a Nogo-66 receptor antagonist enhancing injured spinal cord regeneration. <i> Li M, Shi J, Wei Z, Teng FY, Tang BL, Song J. </i> Eur J Biochem, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"bmesza","curator_name":"Bálint Mészáros","curator_orcid":"0000-0003-0919-4449","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01855r046","statement":[{"text":"The CD spectrum of Nogo‐40 in the aqueous buffer has a negative peak at ≈198nm, indicating that Nogo‐40 had no stable conformation in aqueous buffer [[23]]. Interestingly, with the introduction of methanol, the CD spectra of Nogo‐40 undergo dramatic changes. The CD spectra of Nogo‐40 in the presence of methanol at a concentration of 74% or above show one positive peak at ≈198nm and two negative peaks at ≈208 and 222nm, respectively. This observation clearly indicates that Nogo‐40 adopts a well‐formed helical conformation in the presence of 74% or higher percentages of methanol. Similarly, as shown in Fig. 5B, TFE is also able to stabilize the helical conformation of Nogo‐40. It appears that 50% TFE is sufficient to stabilize a full helical conformation for the peptide.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T11:09:52.637Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"","date":"2018-08-14T14:11:15.000Z","acc":"Q9NQC3-1","name":"Isoform A of Reticulon-4","length":1192,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000000D81D","genes":[{"name":{"value":"RTN4","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:14085","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:14085"}}]},"synonyms":[{"value":"KIAA0886"},{"value":"NOGO","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12488097","url":"http://www.ncbi.nlm.nih.gov/pubmed/12488097","alternativeUrl":"https://europepmc.org/abstract/MED/12488097"}}]}],"orfNames":[{"value":"My043"},{"value":"SP1507"}]}],"disorder_content":0.9060402684563759,"disprot_consensus":{"full":[{"start":1,"end":200,"type":"D"},{"start":210,"end":566,"type":"D"},{"start":567,"end":748,"type":"T"},{"start":749,"end":1016,"type":"D"},{"start":1055,"end":1094,"type":"D"},{"start":1155,"end":1187,"type":"D"}],"Structural state":[{"start":1,"end":200,"type":"D"},{"start":210,"end":1016,"type":"D"},{"start":1055,"end":1094,"type":"D"},{"start":1155,"end":1187,"type":"D"}],"Structural transition":[{"start":567,"end":748,"type":"T"}],"Molecular function":[{"start":567,"end":748,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":12,"end":82},{"id":"PF00076","name":"RNA recognition motif","start":210,"end":272}],"gene3D":[{"start":195,"end":282,"id":"3.30.70.330","name":"3.30.70.330"},{"start":3,"end":107,"id":"3.30.70.330","name":"3.30.70.330"}]},"uniref50":"UniRef50_P09012","sequence":"MAVPETRPNHTIYINNLNEKIKKDELKKSLYAIFSQFGQILDILVSRSLKMRGQAFVIFKEVSSATNALRSMQGFPFYDKPMRIQYAKTDSDIIAKMKGTFVERDRKREKRKPKSQETPATKKAVQGGGATPVVGAVQGPVPGMPPMTQAPRIMHHMPGQPPYMPPPGMIPPPGLAPGQIPPGAMPPQQLMPGQMPPAQPLSENPPNHILFLTNLPEETNELMLSMLFNQFPGFKEVRLVPGRHDIAFVEFDNEVQAGAARDALQGFKITQNNAMKISFAKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P09012","disprot_id":"DP01857","ncbi_taxon_id":9606,"regions_counter":6,"creator":"sventura","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":117,"region_id":"DP01857r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of the N-terminal RNP domain of U1A protein: the role of C-terminal residues in structure stability and RNA binding. <i> Avis JM, Allain FH, Howe PW, Varani G, Nagai K, Neuhaus D. </i> J Mol Biol, 1996","statement":[{"text":"The backbone resonances for residues Val102 to Glu117 have very narrow linewidths, suggesting considerable flexibility in this C-terminal region and facilitating assignment through strong dαN connectivities, characteristic of\nan extended conformation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"sventura","start":102,"term_ontology":"IDPO","curator_name":"Salvador Ventura","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1fht"}],"reference_id":"8609632","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":117,"term_name":"DNA binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Solution structure of the N-terminal RNP domain of U1A protein: the role of C-terminal residues in structure stability and RNA binding. <i> Avis JM, Allain FH, Howe PW, Varani G, Nagai K, Neuhaus D. </i> J Mol Biol, 1996","statement":[{"text":"This region was not included in the isolated crystal structure of the U1-A N-terminal RRM-SL2 complex (Oubridge et al, 1994) and was disordered in the absence of RNA in an NMR-structure of a U1-A fragment spanning residues 1–117 (Avis et al, 1996), demonstrating that its fold is induced on RNA binding.","type":"Results"}],"term_id":"GO:0003677","curator_id":"sventura","start":102,"term_ontology":"GO","curator_name":"Salvador Ventura","reference_id":"8609632","version":3,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PMID","id":"21113136"}],"region_id":"DP01857r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":207,"region_id":"DP01857r003","reference_id":"21113136","start":115,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"a second RRM at the C terminus of the U1-A protein (residues 208–282), which is connected to the N-terminal RRM by a flexible linker (residues 115–207)","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Functional organization of the Sm core in the crystal structure of human U1 snRNP. <i> Weber G, Trowitzsch S, Kastner B, Lührmann R, Wahl MC. </i> EMBO J, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3PGW"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":207,"region_id":"DP01857r004","reference_id":"21113136","start":115,"term_id":"IDPO:0000033","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"a second RRM at the C terminus of the U1-A protein (residues 208–282), which is connected to the N-terminal RRM by a flexible linker (residues 115–207)","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"Functional organization of the Sm core in the crystal structure of human U1 snRNP. <i> Weber G, Trowitzsch S, Kastner B, Lührmann R, Wahl MC. </i> EMBO J, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3PGW"}],"term_name":"flexible linker","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":117,"region_id":"DP01857r005","reference_id":"8609632","start":99,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The   N terminus  (residues  2  to  7)  and  the  C  terminus (residues 99 to 117) are poorly ordered and show no long-range  NOE  connectivity  to  the  rest  of  the protein","type":"Results"},{"text":"The backbone resonances for  residues  Val102  to  Glu117  have  very  narrow line widths,   suggesting   considerable   flexibility   in this  C-terminal  region","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"reference_html":"Solution structure of the N-terminal RNP domain of U1A protein: the role of C-terminal residues in structure stability and RNA binding. <i> Avis JM, Allain FH, Howe PW, Varani G, Nagai K, Neuhaus D. </i> J Mol Biol, 1996","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"1FHT"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P09012","date":"2018-08-14T14:33:13.000Z","acc":"P09012","name":"U1 small nuclear ribonucleoprotein A","length":282,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000002C8F2","genes":[{"name":{"value":"SNRPA"}}],"alphafold_very_low_content":0.06028368794326241,"disorder_content":0.38652482269503546,"disprot_consensus":{"full":[{"start":99,"end":207,"type":"D"}],"Structural state":[{"start":99,"end":207,"type":"D"}],"Molecular function":[{"start":102,"end":117,"type":"F"}],"Disorder function":[{"start":115,"end":207,"type":"F"}]}},{"features":{"pfam":[{"id":"PF27970","name":"LEA protein 1/2/D7/Stress-induced protein KIN2","start":103,"end":141}]},"uniref50":"UniRef50_Q96270","sequence":"MASHQEQSYKAGETRGKAQEKTGEAMGTMGDKTQAAKDKTQETAQSAQQKAHETAQSAKDKTSQAAQTTQERAQESKDKTGSYMSETGEAIKNKAHDAAEYTKETAEAGKEKTSGILGQTGEQVKQMAMGATDAVKHTLGLRTDEGNKEHVSSAPSTTTTTTTRETQRK","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q96270","disprot_id":"DP01858","ncbi_taxon_id":3702,"regions_counter":9,"creator":"grivas","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":169,"region_id":"DP01858r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structural transitions in the intrinsically disordered plant dehydration stress protein LEA7 upon drying are modulated by the presence of membranes. <i> Popova AV, Hundertmark M, Seckler R, Hincha DK. </i> Biochim Biophys Acta, 2011","statement":[{"text":"The CD spectrum of the hydrated protein indicated a low content of stable secondary structures, with a well defined minimal ellipticity around 200 nm","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"achasapi","start":1,"term_ontology":"IDPO","curator_name":"Anastasia Chasapi","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1986-5007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21443857","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:52:06.047Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":169,"region_id":"DP01858r002","released":"2022_03","ec_id":"ECO:0006228","reference_html":"Structural transitions in the intrinsically disordered plant dehydration stress protein LEA7 upon drying are modulated by the presence of membranes. <i> Popova AV, Hundertmark M, Seckler R, Hincha DK. </i> Biochim Biophys Acta, 2011","statement":[{"text":"The minimum at 1642 cm− 1 indicating unstructured elements in the protein is the most prominent. This is in good agreement with the CD spectra, which also indicate that the unstructured components of LEA7 dominate in its hydrated state.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"achasapi","start":1,"term_ontology":"IDPO","curator_name":"Anastasia Chasapi","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1986-5007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21443857","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:52:06.869Z"}},{"start":1,"end":169,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins.  <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2023-08-27T19:50:54.602Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01858r003","statement":[{"text":"We therefore monitored secondary structure of the six LEA_4 proteins in response to decreasing relative humidity (RH) using the Amide I band of Fourier-transform infrared (FTIR) spectra (Figure 6). This absorbance band mainly results from the C=O stretching vibration and is directly related to the protein backbone conformation. A maximum at 1650–1640 cm-1 indicated that all proteins were mainly disordered at 100% RH, which is in line with the CD data.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:52:08.145Z"}},{"start":1,"end":169,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins.  <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2023-08-27T19:51:13.629Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01858r004","statement":[{"text":"Simultaneous static and dynamic light scattering (SLS/DLS) measurements were conducted to determine the apparent average single particle mass (Mapp) and the apparent average hydrodynamic radius (RS) of the proteins in solution as a function of concentration (Figure S4, [30]). Absolute molecular mass and RS were obtained by extrapolation of apparent molecular mass and RS to infinite dilution. All investigated LEA proteins are essentially monomeric under fully hydrated conditions. Compared to globular proteins, RS of all investigated LEA proteins was rather large, indicating their expanded, non-compact nature.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:52:09.291Z"}},{"start":1,"end":169,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among <i>Arabidopsis thaliana</i> LEA_4 Proteins. <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2024-08-28T11:40:02.844Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP01858r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":"ethylene glycol"}],"statement":[{"text":"Figure S5 shows FTIR spectra of the six LEA_4 proteins in EG concentrations ranging from 0 to 12 osM. Similar to decreasing RH, increasing osmolarity induces coil-helix transitions, indicated by a shift of the Amide I maxima to higher wavenumbers.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:08:33.094Z"}},{"start":1,"end":169,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among <i>Arabidopsis thaliana</i> LEA_4 Proteins. <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2024-08-28T11:40:35.753Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP01858r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":"ethylene glycol"}],"statement":[{"text":"All proteins showed typical random coil spectra in dilute solution. With increasing concentrations of each of the co-solvents, the changes in the spectral shape report on the formation of ordered secondary structure.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:08:32.055Z"}},{"start":1,"end":169,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among <i>Arabidopsis thaliana</i> LEA_4 Proteins. <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2024-09-17T09:14:51.742Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0009409","term_name":"response to cold","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IDA","region_id":"DP01858r009","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"39073","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}],"entry_name":"6-carboxyfluorescein"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"170453367","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"10724471","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"56842030","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"45109789","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]}],"statement":[{"text":"Therefore, we analyzed the stability of liposomes modeling the lipid composition of inner chloroplast membranes (ICMM) after a freeze/thaw cycle and a dehydration/rehydration cycle in the ethylene glycolpresence of all six LEA_4 proteins at different LEA protein: lipid mass ratios (Figure 13).","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cold stimulus, a temperature stimulus below the optimal temperature for that organism.\" [GOC:lr]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_Q96270","date":"2018-08-14T15:06:41.000Z","acc":"Q96270","name":"Late embryogenesis abundant protein 7","length":169,"organism":"Arabidopsis thaliana","dataset":["Stress response proteins"],"UniParc":"UPI00000AD08E","genes":[{"name":{"value":"LEA7","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"18318901","url":"http://www.ncbi.nlm.nih.gov/pubmed/18318901","alternativeUrl":"https://europepmc.org/abstract/MED/18318901"}}]},"orfNames":[{"value":"F6D8.9","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAD55596.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD55596.1"}}]}],"olnNames":[{"value":"At1g52690","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT1G52690","url":""}}]}]}],"alphafold_very_low_content":0.2603550295857988,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":169,"type":"T"}],"Structural state":[{"start":1,"end":169,"type":"D"}],"Structural transition":[{"start":1,"end":169,"type":"T"}],"Biological process":[{"start":1,"end":169,"type":"F"}]}},{"features":{"pfam":[{"id":"PF28479","name":"Uncharacterized protein At4g13230","start":257,"end":311}]},"uniref50":"UniRef50_G7ISC0","sequence":"MAAMFTTRNAIFRFSKSFPNVPSLSLPKPSRVFVASASHQSDWRNAADGKRNSSMDWAYNSTSKARQDADEIADRERKTLNGDVDSEDVKQYVRDAKERTKEAANRAAENADSAGVKSRDYAYDAKEKTKDAANRAAENVESAGEKAKDYAYDAKERTKDAANRAAENAESVGEKARDYAYDAKERTKEAAQNAGETAKDYAYGAKERTKEAAESAGGTARDYAYDATDKTKEAVGTVADKTKEGAKKTAEMTKEGAEKTAETTGEVAGAATEALKSAGEMAKRTAQGAWETAKDATQKIKETVVGKDDDDNDRGGGVGAVVDEYDVELKRKGYGESKGYDMSKGYGENKGYDQNRGY","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","fabids","Fabales","Fabaceae","Papilionoideae","50 kb inversion clade","NPAAA clade","Hologalegina","IRL clade","Fabeae","Pisum"],"uniref90":"UniRef90_Q5NJL5","disprot_id":"DP01859","ncbi_taxon_id":3888,"regions_counter":2,"creator":"achasapi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":358,"region_id":"DP01859r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"A mitochondrial late embryogenesis abundant protein stabilizes model membranes in the dry state. <i> Tolleter D, Hincha DK, Macherel D. </i> Biochim Biophys Acta, 2010","statement":[{"text":"The CD spectrum of the protein in aqueous solution appeared typical of a random coil structure, with a 195-nm minimum of ellipticity. LEAM is thus a monomer that is natively unfolded in solution","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"achasapi","start":1,"term_ontology":"IDPO","curator_name":"Anastasia Chasapi","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1986-5007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20637181","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":358,"region_id":"DP01859r002","released":"2022_03","ec_id":"ECO:0006228","reference_html":"A mitochondrial late embryogenesis abundant protein stabilizes model membranes in the dry state. <i> Tolleter D, Hincha DK, Macherel D. </i> Biochim Biophys Acta, 2010","statement":[{"text":"In solution, the LEAM spectra revealed a maximum at 1649 cm−1, with a main peak at 1647.5 cm−1 surrounded by two other peaks at 1663 and 1630 cm−1. These values were assigned to random coil structures according to published data and in light of the CD observations","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"achasapi","start":1,"term_ontology":"IDPO","curator_name":"Anastasia Chasapi","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1986-5007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20637181","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q5NJL5","date":"2018-08-14T15:32:49.000Z","acc":"Q5NJL5","name":"Late embryogenesis abundant protein","length":358,"organism":"Pisum sativum","dataset":[],"UniParc":"UPI000049C14D","genes":[{"name":{"value":"lea","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAF32327.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAF32327.1"}}]}}],"alphafold_very_low_content":1,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":358,"type":"D"}],"Structural state":[{"start":1,"end":358,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00477","name":"Small hydrophilic plant seed protein","start":2,"end":64}]},"uniref50":"UniRef50_Q02973","sequence":"MASQQEKKELDARARQGETVVPGGTGGKSLEAQQHLAEGRSKGGQTRKEQLGGEGYHEMGRKGGLSNNDMSGGERAEQEGIDIDESKFRTKK","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","campanulids","Apiales","Apiaceae","Apioideae","Scandiceae","Daucinae","Daucus","Daucus sect. Daucus"],"uniref90":"UniRef90_P17639","disprot_id":"DP01860","ncbi_taxon_id":4039,"regions_counter":1,"creator":"achasapi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":92,"region_id":"DP01860r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The Embryo-Specific Emb-1 Protein Of Daucus Carota Is Flexible And Unstructured In Solution <i> Eom, Juwhan; Baker, Wayne R.; Kintanar, Agustin; Wurtele, Eve Syrkin <i> Plant Science 1996","statement":[{"text":"The embryo-specific EMB-1 protein of Daucus carota is flexible and unstructured in solution","type":"Title"},{"text":"The NMR results reveal poor chemical shift dispersion, rapid chemical exchange of the amide backbone protons, unexpectedly narrow linewidths and the general absence of nuclear Overhauser effects. Together, these results indicate the EMB-1 protein has no defined secondary or tertiary structure in solution and the polypeptide backbone of the EMB-1 protein is flexible on a sub-nanosecond time scale.","type":"Abstract"},{"text":"In the spectrum of EMB-1 (Fig. 4a), the alpha proton resonances, aromatic proton resonances of the tyr and phe residues, and the methyl proton resonances of the val, leu and ile residues are found at chemical shift positions characteristic of a random coil structure (i.e., about 7 ppm, 4 ppm, and 1 - 1.5 ppm, respectively) [16] and exhibit low chemical shift dispersion. These data indicate the absence of secondary or environmental-dependent chemical shifts and hence the absence of ordered structure of EMB-1 in aqueous solution. ","type":"Results"},{"text":"In EMB-1, amide proton exchange is rapid, indicating the absence of a stably-folded structure (Fig. 4a).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"doi","term_name":"disorder","reference_id":"10.1016/0168-9452(96)04332-4","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-14T12:07:45.933Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P17639","date":"2018-08-14T15:35:11.000Z","acc":"P17639","name":"Protein EMB-1","length":92,"organism":"Daucus carota","dataset":[],"UniParc":"UPI0000129E8D","genes":[{"name":{"value":"EMB-1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"2339072","url":"http://www.ncbi.nlm.nih.gov/pubmed/2339072","alternativeUrl":"https://europepmc.org/abstract/MED/2339072"}}]},"synonyms":[{"value":"CAISE4","evidences":[{"code":"ECO:0000303","source":{"name":"Citation","id":"Ref.3","url":"https://www.uniprot.org/uniprot/null#ref3"}}]},{"value":"EMB1","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"BAD86647.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAD86647.1"}}]}]}],"alphafold_very_low_content":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":92,"type":"D"}],"Structural state":[{"start":1,"end":92,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00031","name":"Cystatin domain","start":24,"end":114},{"id":"PF00031","name":"Cystatin domain","start":144,"end":236},{"id":"PF00031","name":"Cystatin domain","start":266,"end":360}],"gene3D":[{"start":150,"end":250,"id":"3.10.450.10","name":"3.10.450.10"},{"start":32,"end":129,"id":"3.10.450.10","name":"3.10.450.10"},{"start":267,"end":373,"id":"3.10.450.10","name":"3.10.450.10"}]},"uniref50":"UniRef50_P01042","sequence":"MKLITILFLCSRLLLSLTQESQSEEIDCNDKDLFKAVDAALKKYNSQNQSNNQFVLYRITEATKTVGSDTFYSFKYEIKEGDCPVQSGKTWQDCEYKDAAKAATGECTATVGKRSSTKFSVATQTCQITPAEGPVVTAQYDCLGCVHPISTQSPDLEPILRHGIQYFNNNTQHSSLFMLNEVKRAQRQVVAGLNFRITYSIVQTNCSKENFLFLTPDCKSLWNGDTGECTDNAYIDIQLRIASFSQNCDIYPGKDFVQPPTKICVGCPRDIPTNSPELEETLTHTITKLNAENNATFYFKIDNVKKARVQVVAGKKYFIDFVARETTCSKESNEELTESCETKKLGQSLDCNAEVYVVPWEKKIYPTVNCQPLGMISLMKRPPGFSPFRSSRIGEIKEETTVSPPHTSMAPAQDEERDSGKEQGHTRRHDWGHEKQRKHNLGHGHKHERDQGHGHQRGHGLGHGHEQQHGLGHGHKFKLDDDLEHQGGHVLDHGHKHKHGHGHGKHKNKGKKNGKHNGWKTEHLASSSEDSTTPSAQTQEKTEGPTPIPSLAKPGVTVTFSDFQDSDLIATMMPPISPAPIQSDDDWIPDIQIDPNGLSFNPISDFPDTTSPKCPGRPWKSVSEINPTTQMKESYYFDLTDGLS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P01042","disprot_id":"DP01861","ncbi_taxon_id":9606,"regions_counter":3,"creator":"achasapi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":531,"region_id":"DP01861r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The high-molecular-weight kininogen domain 5 is an intrinsically unstructured protein and its interaction with ferritin is metal mediated. <i> Huhn AJ, Parsonage D, Horita DA, Torti FM, Torti SV, Hollis T. </i> Protein Sci, 2014","statement":[{"text":"What was observed were CD spectra consistent with a random coil structure and minimal α-helix or β sheet, which is demonstrated by the lack of negative peaks at 222 nm for α-helices and 215 nm for β-sheets","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":438,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24810540","validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-05-26T16:23:22.119Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":531,"region_id":"DP01861r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The high-molecular-weight kininogen domain 5 is an intrinsically unstructured protein and its interaction with ferritin is metal mediated. <i> Huhn AJ, Parsonage D, Horita DA, Torti FM, Torti SV, Hollis T. </i> Protein Sci, 2014","statement":[{"text":"The results suggest that under all measured conditions, HK5 has little secondary structure (Fig. 2), as exhibited by the lack of distinct peaks and the small 1H and 15N chemical shift ranges. Titration of Zn2+, Co2+, or Fe2+ up to 400 μM, did not induce any additional secondary structure. Taken together, these data suggest HK5 is likely an intrinsically unstructured protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rpancsa","start":438,"term_ontology":"IDPO","curator_name":"Rita Pancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0849-9312","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24810540","validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-05-26T16:34:00.168Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":438,"end":531,"reference_id":"24810540","reference_source":"pmid","reference_html":"The high-molecular-weight kininogen domain 5 is an intrinsically unstructured protein and its interaction with ferritin is metal mediated. <i> Huhn AJ, Parsonage D, Horita DA, Torti FM, Torti SV, Hollis T. </i> Protein Sci, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000269","ec_ontology":"ECO","ec_name":"experimental evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01861r003","statement":[{"text":"Here we demonstrate that HK5 is an intrinsically unstructured protein (IUP) and binds to ferritin in a metal-mediated interaction that occurs on the surface of ferritin and works independently of oxidized iron in its ferrihydrite core.","type":"Discussion"},{"text":"To test whether HK5 had a preference for interacting with one of the subunits in vitro, binding affinity for HK5 and ferritin H or ferritin L were measured individually. In the absence of metal ions, HK5 has similar binding affinities to ferritin L and ferritin H, with Kd values of 247 µM and 129 µM, respectively.","type":"Results"}],"interaction_partner":[{"db":"UniProt","id":"P02794","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P02792","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-05-26T16:45:47.146Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P01042","date":"2018-08-14T19:04:52.000Z","acc":"P01042","name":"Kininogen-1","length":644,"organism":"Homo sapiens","dataset":["Extracellular matrix proteins"],"UniParc":"UPI000013D5AC","genes":[{"name":{"value":"KNG1"},"synonyms":[{"value":"BDK"},{"value":"KNG"}]}],"alphafold_very_low_content":0.40683229813664595,"disorder_content":0.14596273291925466,"disprot_consensus":{"full":[{"start":438,"end":531,"type":"D"}],"Structural state":[{"start":438,"end":531,"type":"D"}],"Molecular function":[{"start":438,"end":531,"type":"F"}]}},{"features":{"pfam":[{"id":"PF08920","name":"Splicing factor 3B subunit 1","start":329,"end":451},{"id":"PF22646","name":"PPP2R1A-like HEAT repeat","start":1086,"end":1158}],"gene3D":[{"start":794,"end":1198,"id":"1.25.10.10","name":"Leucine-rich Repeat Variant"},{"start":477,"end":793,"id":"1.25.10.10","name":"Leucine-rich Repeat Variant"}]},"uniref50":"UniRef50_O75533","sequence":"MAKIAKTHEDIEAQIREIQGKKAALDEAQGVGLDSTGYYDQEIYGGSDSRFAGYVTSIAATELEDDDDDYSSSTSLLGQKKPGYHAPVALLNDIPQSTEQYDPFAEHRPPKIADREDEYKKHRRTMIISPERLDPFADGGKTPDPKMNARTYMDVMREQHLTKEEREIRQQLAEKAKAGELKVVNGAAASQPPSKRKRRWDQTADQTPGATPKKLSSWDQAETPGHTPSLRWDETPGRAKGSETPGATPGSKIWDPTPSHTPAGAATPGRGDTPGHATPGHGGATSSARKNRWDETPKTERDTPGHGSGWAETPRTDRGGDSIGETPTPGASKRKSRWDETPASQMGGSTPVLTPGKTPIGTPAMNMATPTPGHIMSMTPEQLQAWRWEREIDERNRPLSDEELDAMFPEGYKVLPPPAGYVPIRTPARKLTATPTPLGGMTGFHMQTEDRTMKSVNDQPSGNLPFLKPDDIQYFDKLLVDVDESTLSPEEQKERKIMKLLLKIKNGTPPMRKAALRQITDKAREFGAGPLFNQILPLLMSPTLEDQERHLLVKVIDRILYKLDDLVRPYVHKILVVIEPLLIDEDYYARVEGREIISNLAKAAGLATMISTMRPDIDNMDEYVRNTTARAFAVVASALGIPSLLPFLKAVCKSKKSWQARHTGIKIVQQIAILMGCAILPHLRSLVEIIEHGLVDEQQKVRTISALAIAALAEAATPYGIESFDSVLKPLWKGIRQHRGKGLAAFLKAIGYLIPLMDAEYANYYTREVMLILIREFQSPDEEMKKIVLKVVKQCCGTDGVEANYIKTEILPPFFKHFWQHRMALDRRNYRQLVDTTVELANKVGAAEIISRIVDDLKDEAEQYRKMVMETIEKIMGNLGAADIDHKLEEQLIDGILYAFQEQTTEDSVMLNGFGTVVNALGKRVKPYLPQICGTVLWRLNNKSAKVRQQAADLISRTAVVMKTCQEEKLMGHLGVVLYEYLGEEYPEVLGSILGALKAIVNVIGMHKMTPPIKDLLPRLTPILKNRHEKVQENCIDLVGRIADRGAEYVSAREWMRICFELLELLKAHKKAIRRATVNTFGYIAKAIGPHDVLATLLNNLKVQERQNRVCTTVAIAIVAETCSPFTVLPALMNEYRVPELNVQNGVLKSLSFLFEYIGEMGKDYIYAVTPLLEDALMDRDLVHRQTASAVVQHMSLGVYGFGCEDSLNHLLNYVWPNVFETSPHVIQAVMGALEGLRVAIGPCRMLQYCLQGLFHPARKVRDVYWKIYNSIYIGSQDALIAHYPRIYNDDKNTYIRYELDYIL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O75533","disprot_id":"DP01863","ncbi_taxon_id":9606,"regions_counter":8,"creator":"sgovind","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":462,"region_id":"DP01863r001","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Molecular Architecture of SF3b and Structural Consequences of Its Cancer-Related Mutations. <i> Cretu C, Schmitzová J, Ponce-Salvatierra A, Dybkov O, De Laurentiis EI, Sharma K, Will CL, Urlaub H, Lührmann R, Pena V. </i> Mol Cell, 2016","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-31T13:12:37.879Z","reference_source":"pmid","term_name":"disorder","reference_id":"27720643","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"5IFE"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15393 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q7RTV0"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9BWJ5 "},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:813"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"}],"statement":[{"text":"On the basis of bioinformatics predictions and limited proteolysis, we removed intrinsically disordered regions from SF3b (Figure S1A, available online). The resulting SF3b core complex formed crystals and enabled de novo structure determination by combining single isomorphous replacement with anomalous scattering (SIRAS) and molecular replacement-single-wavelength anomalous dispersion (MR-SAD) (Figures S1B–S1E).","type":"Results"},{"text":" One molecule is present in the asymmetric unit and comprises SF3b155 residues 463–1,304 (the HEAT domain), SF3b130 residues 1–1,217, SF3b14b residues 7–95, and SF3b10 residues 15–80 (Figures 1C–1F).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-15T10:13:38.612Z"}},{"start":190,"end":344,"reference_id":"16376933","reference_source":"pmid","reference_html":"Multiple U2AF65 binding sites within SF3b155: thermodynamic and spectroscopic characterization of protein-protein interactions among pre-mRNA splicing factors. <i> Thickman KR, Swenson MC, Kabogo JM, Gryczynski Z, Kielkopf CL. </i> J Mol Biol, 2006","date":"2023-05-31T12:49:29.443Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP01863r007","statement":[{"text":"Circular dichroism (CD) was used to investigate the secondary structural organization of the SF3b155r domain (Figure 4(b)). The pronounced negative band just below 200 nm of the SF3b155r CD spectrum is characteristic of a protein that is in a largely unstructured conformation33.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-15T10:13:40.686Z"}},{"start":190,"end":344,"reference_id":"16376933","reference_source":"pmid","reference_html":"Multiple U2AF65 binding sites within SF3b155: thermodynamic and spectroscopic characterization of protein-protein interactions among pre-mRNA splicing factors. <i> Thickman KR, Swenson MC, Kabogo JM, Gryczynski Z, Kielkopf CL. </i> J Mol Biol, 2006","date":"2023-05-31T13:00:13.899Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990935","term_name":"splicing factor binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P26368","operator":null,"partner_start":375,"partner_end":475}],"region_id":"DP01863r008","statement":[{"text":"Assuming identical and independent (non-cooperative) binding sites, the best fit of the wild-type SF3b155r binding isotherm was obtained with a stoichiometry of three binding sites for U2AF65 within SF3b155r (Figure 5(a)). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein involved in the process of removing sections of the primary RNA transcript to form the mature form of the RNA.\" [PMID:11118435]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-15T10:13:42.804Z"}}],"released":"2018_11","uniref100":"UniRef100_O75533","date":"2018-08-15T07:19:43.000Z","acc":"O75533","name":"Splicing factor 3B subunit 1","length":1304,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins","Condensates-related proteins","RNA-binding proteins"],"UniParc":"UPI000013546D","genes":[{"name":{"value":"SF3B1"},"synonyms":[{"value":"SAP155"}]}],"alphafold_very_low_content":0.24386503067484663,"disorder_content":0.35429447852760737,"disprot_consensus":{"full":[{"start":1,"end":462,"type":"D"}],"Structural state":[{"start":1,"end":462,"type":"D"}],"Molecular function":[{"start":190,"end":344,"type":"F"}]}},{"features":{"pfam":[{"id":"PF09607","name":"Brinker DNA-binding domain","start":43,"end":100}],"gene3D":[{"start":43,"end":101,"id":"1.10.10.60","name":"Homeodomain-like"}]},"uniref50":"UniRef50_Q9XTN4","sequence":"MDSSSEQLNGSGALNFKRPKDSSENATNSHTNNGNSSGSPKMGSRRIFTPHFKLQVLESYRNDNDCKGNQRATARKYNIHRRQIQKWLQCESNLRSSVANNQQQQQQQQQQQQQQQQQQQLLPQQSVSPTPAVKVFHQLSHPLVHQLHHHHAAAVGHHHHHAAHHHAAHHHHAAAAAAAAAAAAAAAAAHHHAAHHLLAANGMVPHPLAAHPHLHVPVAMHPQMQHQKEQQQQQQQLQQEQQQQDQQQSQQETPATIATNGSNQGSSNVLSAAKIAAVVAAAMATSNGNPTPTATIPASSSSSSNTLPSSNNSSCHNSSSSSNSCNSNQVPIQVPILSGSPGSTSSASHIPHVPFAYHHNLHGYLENRLEAVATPAPMDLSLGSSARRQMQLHEKDPSGVDLTFRKRKVITSPMQPDKISKLEEVIKKEPETETENEDVEVDVETEQPEEHKLPSKQVKLFKPYLLDDDEEQDHHHHHHHHRQEDLDEGAAEEEQDDEEESRYADDDEVDSKEAADKKQRRLKKKPSAINEQREPIIWSNHPYPGGCVSPGSSITSSFQCPTSMQQQQTFPVAGGSPNQQFQDNCSSSKATTPLSPFSAPALSPTGFCCPKGSPVSGYESSSSTYSDSGSNYSLNLQLHAVYNDNLMYMQQQQQQQQQQHHLQHQQHLQRWLDQESLATARTSSVNRPLILVADTAPTNLTLVA","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_Q9XTN4","disprot_id":"DP01864","ncbi_taxon_id":7227,"regions_counter":7,"creator":"bhajdu","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":101,"region_id":"DP01864r001","released":"2024_06","ec_id":"ECO:0006165","reference_html":"DNA recognition by the brinker repressor--an extreme case of coupling between binding and folding. <i> Cordier F, Hartmann B, Rogowski M, Affolter M, Grzesiek S. </i> J Mol Biol, 2006","statement":[{"text":"The finding that the N-terminal half of BrkNter remains unfolded upon DNA binding prompted us to design a smaller construct, BrkDBD (residues G43 to N101), restricted to the DNA-binding domain proper. Again, in the absence of DNA, BrkDBD is unfolded at 25 °C as judged from the weak spectral dispersion (see Figure 7(a), red resonances) and low {1H}-15N NOEs (not shown). ","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":43,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-06T15:01:56.322Z","reference_source":"pmid","term_name":"disorder","reference_id":"16876822","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"BMRB","id":"7134"}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":95,"term_name":"nucleic acid binding","released":"2024_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"DNA recognition by the brinker repressor--an extreme case of coupling between binding and folding. <i> Cordier F, Hartmann B, Rogowski M, Affolter M, Grzesiek S. </i> J Mol Biol, 2006","statement":[{"text":"Thus, DNA binding induces partial folding of BrkNter. During the sequential assignment process by standard triple-resonance NMR techniques, it became clear that the folded amino acid residues belong to the C-terminal part of BrkNter (residues R46 to R95), which therefore constitutes the proper DNA-binding domain.","type":"Results"},{"text":"Spectra of BrkDBD in complex with the respective double-stranded 12-mer DNA, omb12T5, no longer showed this heterogeneity and had nearly identical chemical shifts to the BrkDBD–omb12 complex (data not shown).","type":"Results"},{"text":"The binding was confirmed to both Double-stranded DNA omb12 (5′d-TGAGGCGCCAAC) and omb12t5 (5′d-TGAGGCGTCAAC).","type":"Curator statement"}],"term_id":"GO:0003676","curator_id":"vnugnes","start":46,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"16876822","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-06T15:09:05.549Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01864r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"BMRB","id":"7097"},{"db":"PDB","id":"2GLO"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":101,"region_id":"DP01864r004","released":"2024_06","ec_id":"ECO:0005642","reference_html":"DNA recognition by the brinker repressor--an extreme case of coupling between binding and folding. <i> Cordier F, Hartmann B, Rogowski M, Affolter M, Grzesiek S. </i> J Mol Biol, 2006","statement":[{"text":"The 1H-15N-heteronuclear single quantum coherence (HSQC) spectrum of BrkNter in the absence of DNA (Figure 2(a)) at 25 °C reveals very limited dispersion, with chemical shifts for many of the 1H/15N resonances around 8 ppm/120 ppm. This indicates that the respective amino acid residues are in random coil conformation and therefore that apo-BrkNter is not folded at 25 °C.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-06T14:37:19.983Z","reference_source":"pmid","term_name":"disorder","reference_id":"16876822","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":101,"term_name":"disorder to order","released":"2024_06","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","reference_html":"DNA recognition by the brinker repressor--an extreme case of coupling between binding and folding. <i> Cordier F, Hartmann B, Rogowski M, Affolter M, Grzesiek S. </i> J Mol Biol, 2006","statement":[{"text":"In contrast, addition of an equimolar amount of omb12 DNA (which corresponds in sequence to an in vivo binding site of Brk6) induces a drastic change in the 1H-15N-HSQC spectrum (Figure 2(b), blue resonances): approximately half of the resonances shift strongly to widely dispersed spectral positions, indicative of a folded structure.","type":"Results"},{"text":"Assignment was completed only for residues K41 to N101, since the N-terminal part (before R46) remained unfolded and highly flexible, as indicated by unchanged random coil chemical shifts, strong overlap, and {1H}-15N NOE values below 0.3 (Figure 2(d), blue circles).","type":"Results"},{"text":"Spectra of BrkDBD in complex with the respective double-stranded 12-mer DNA, omb12T5, no longer showed this heterogeneity and had nearly identical chemical shifts to the BrkDBD–omb12 complex (data not shown).","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"vnugnes","start":46,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16876822","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-06T15:08:32.732Z","reference_source":"pmid","ec_id":"ECO:0005642","region_id":"DP01864r005","ec_go":"EXP","disprot_namespace":"Structural transition","cross_refs":[{"db":"BMRB","id":"7097"},{"db":"PDB","id":"2GLO"}],"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting Double-stranded DNA omb12 (5′d-TGAGGCGCCAAC) or omb12t5 (5′d-TGAGGCGTCAAC)."}]}]},{"start":43,"end":101,"reference_id":"16876822","reference_source":"pmid","reference_html":"DNA recognition by the brinker repressor--an extreme case of coupling between binding and folding. <i> Cordier F, Hartmann B, Rogowski M, Affolter M, Grzesiek S. </i> J Mol Biol, 2006","date":"2024-02-06T15:20:09.753Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","region_id":"DP01864r007","statement":[{"text":"Gel mobility assays indicated that the affinities for all three complexes BrkNter–omb12, BrkDBD–omb12 and BrkDBD–omb12T5 are very similar (data not shown). Therefore, the smallest and most homogeneous complex, BrkDBD–omb12T5, appeared best suited for NMR analysis, and the subsequent structure determination was carried out on this complex.","type":"Results"},{"text":"The binding was confirmed to both Double-stranded DNA omb12 (5′d-TGAGGCGCCAAC) and omb12t5 (5′d-TGAGGCGTCAAC).","type":"Curator statement"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"NCBIgene","id":"CP121947","operator":"and","partner_start":460452,"partner_end":460463}]}],"released":"2018_11","uniref100":"UniRef100_Q9XTN4","date":"2018-08-15T07:29:25.000Z","acc":"Q9XTN4","name":"Brinker","length":704,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI000007D0BC","genes":[{"name":{"value":"brk","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF46251.3","url":"https://www.ebi.ac.uk/ena/browser/view/AAF46251.3"}},{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0024250","url":"http://flybase.org/reports/FBgn0024250.html"}}]},"synonyms":[{"value":"brinker","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAD22080.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD22080.1"}}]},{"value":"BRK","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF46251.3","url":"https://www.ebi.ac.uk/ena/browser/view/AAF46251.3"}}]},{"value":"Brk","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF46251.3","url":"https://www.ebi.ac.uk/ena/browser/view/AAF46251.3"}}]},{"value":"brk-RA","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ACK77656.1","url":"https://www.ebi.ac.uk/ena/browser/view/ACK77656.1"}}]},{"value":"Dm brk","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF46251.3","url":"https://www.ebi.ac.uk/ena/browser/view/AAF46251.3"}}]},{"value":"Dmel\\CG9653","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF46251.3","url":"https://www.ebi.ac.uk/ena/browser/view/AAF46251.3"}}]},{"value":"ssg-1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF46251.3","url":"https://www.ebi.ac.uk/ena/browser/view/AAF46251.3"}}]}],"orfNames":[{"value":"CG9653","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF46251.3","url":"https://www.ebi.ac.uk/ena/browser/view/AAF46251.3"}},{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0024250","url":"http://flybase.org/reports/FBgn0024250.html"}}]},{"value":"Dmel_CG9653","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF46251.3","url":"https://www.ebi.ac.uk/ena/browser/view/AAF46251.3"}}]}]}],"alphafold_very_low_content":0.4588068181818182,"disorder_content":0.1434659090909091,"disprot_consensus":{"full":[{"start":1,"end":45,"type":"D"},{"start":46,"end":101,"type":"T"}],"Structural state":[{"start":1,"end":101,"type":"D"}],"Molecular function":[{"start":43,"end":101,"type":"F"}],"Structural transition":[{"start":46,"end":101,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":152,"end":299},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":469,"end":548},{"id":"PF08148","name":"DSHCT (NUC185) domain","start":899,"end":1067},{"id":"PF13234","name":"Mtr4-like, beta-barrel domain","start":666,"end":872},{"id":"PF21408","name":"Exosome RNA helicase MTR4-like, stalk","start":602,"end":665}],"gene3D":[{"start":675,"end":804,"id":"2.40.30.300","name":"2.40.30.300"},{"start":117,"end":322,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":323,"end":580,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":609,"end":872,"id":"1.20.1500.20","name":"1.20.1500.20"},{"start":587,"end":1064,"id":"1.10.3380.30","name":"1.10.3380.30"}]},"uniref50":"UniRef50_P47047","sequence":"MDSTDLFDVFEETPVELPTDSNGEKNADTNVGDTPDHTQDKKHGLEEEKEEHEENNSENKKIKSNKSKTEDKNKKVVVPVLADSFEQEASREVDASKGLTNSETLQVEQDGKVRLSHQVRHQVALPPNYDYTPIAEHKRVNEARTYPFTLDPFQDTAISCIDRGESVLVSAHTSAGKTVVAEYAIAQSLKNKQRVIYTSPIKALSNQKYRELLAEFGDVGLMTGDITINPDAGCLVMTTEILRSMLYRGSEVMREVAWVIFDEVHYMRDKERGVVWEETIILLPDKVRYVFLSATIPNAMEFAEWICKIHSQPCHIVYTNFRPTPLQHYLFPAHGDGIYLVVDEKSTFREENFQKAMASISNQIGDDPNSTDSRGKKGQTYKGGSAKGDAKGDIYKIVKMIWKKKYNPVIVFSFSKRDCEELALKMSKLDFNSDDEKEALTKIFNNAIALLPETDRELPQIKHILPLLRRGIGIHHSGLLPILKEVIEILFQEGFLKVLFATETFSIGLNMPAKTVVFTSVRKWDGQQFRWVSGGEYIQMSGRAGRRGLDDRGIVIMMIDEKMEPQVAKGMVKGQADRLDSAFHLGYNMILNLMRVEGISPEFMLEHSFFQFQNVISVPVMEKKLAELKKDFDGIEVEDEENVKEYHEIEQAIKGYREDVRQVVTHPANALSFLQPGRLVEISVNGKDNYGWGAVVDFAKRINKRNPSAVYTDHESYIVNVVVNTMYIDSPVNLLKPFNPTLPEGIRPAEEGEKSICAVIPITLDSIKSIGNLRLYMPKDIRASGQKETVGKSLREVNRRFPDGIPVLDPVKNMKIEDEDFLKLMKKIDVLNTKLSSNPLTNSMRLEELYGKYSRKHDLHEDMKQLKRKISESQAVIQLDDLRRRKRVLRRLGFCTPNDIIELKGRVACEISSGDELLLTELIFNGNFNELKPEQAAALLSCFAFQERCKEAPRLKPELAEPLKAMREIAAKIAKIMKDSKIEVVEKDYVESFRHELMEVVYEWCRGATFTQICKMTDVYEGSLIRMFKRLEELVKELVDVANTIGNSSLKEKMEAVLKLIHRDIVSAGSLYL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P47047","disprot_id":"DP01867","ncbi_taxon_id":559292,"regions_counter":17,"creator":"bhajdu","regions":[{"region_id":"DP01867r001","ec_ontology":"ECO","end":85,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":1,"version":3,"statement":[{"text":"Gaps in the current model include 85 residues of the native sequence at the N‐terminus and 11 loops of varying length throughout the rest of the sequence (Figure 1).","type":"Results"}],"term_name":"disorder","reference_html":"The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing. <i> Jackson RN, Klauer AA, Hintze BJ, Robinson H, van Hoof A, Johnson SJ. </i> EMBO J, 2010","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"20512111","date":"2024-02-06T17:28:09.250Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":389,"region_id":"DP01867r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing. <i> Jackson RN, Klauer AA, Hintze BJ, Robinson H, van Hoof A, Johnson SJ. </i> EMBO J, 2010","statement":[{"text":"Several large loops, which are disordered in the current structure, potentially interact with the incoming RNA. These loops include: a 15-residue loop (699–713) in the fist, a 29-residue region (361–389) in domain 2, and an 18-residue loop (943–961) in domain 4.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bhajdu","start":361,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3L9O"}],"reference_id":"20512111","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-02-06T17:26:35.031Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":713,"region_id":"DP01867r006","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing. <i> Jackson RN, Klauer AA, Hintze BJ, Robinson H, van Hoof A, Johnson SJ. </i> EMBO J, 2010","statement":[{"text":"Several large loops, which are disordered in the current structure, potentially interact with the incoming RNA. These loops include: a 15-residue loop (699–713) in the fist, a 29-residue region (361–389) in domain 2, and an 18-residue loop (943–961) in domain 4.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bhajdu","start":699,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3L9O"}],"reference_id":"20512111","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-02-06T17:26:09.263Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":961,"region_id":"DP01867r008","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing. <i> Jackson RN, Klauer AA, Hintze BJ, Robinson H, van Hoof A, Johnson SJ. </i> EMBO J, 2010","statement":[{"text":"Several large loops, which are disordered in the current structure, potentially interact with the incoming RNA. These loops include: a 15-residue loop (699–713) in the fist, a 29-residue region (361–389) in domain 2, and an 18-residue loop (943–961) in domain 4.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"bhajdu","start":943,"term_ontology":"IDPO","curator_name":"Borbála Hajdu-Soltész","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7451-5240","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3L9O"}],"reference_id":"20512111","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-02-06T17:26:04.808Z"}},{"region_id":"DP01867r010","ec_ontology":"ECO","end":78,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":1,"version":3,"statement":[{"text":"A dashed line in the secondary structure plot indicates regions\nthat are not observed in the electron density.","type":"Supplementary material"}],"term_name":"disorder","reference_html":"The Mtr4 ratchet helix and arch domain both function to promote RNA unwinding. <i> Taylor LL, Jackson RN, Rexhepaj M, King AK, Lott LK, van Hoof A, Johnson SJ. </i> Nucleic Acids Res, 2014","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"25414331","date":"2024-02-06T16:05:19.127Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4QU4"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18367","entry_name":"phosphate(3-)"}]},{"region_id":"DP01867r011","ec_ontology":"ECO","end":391,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":363,"version":3,"statement":[{"text":"The crystal asymmetric unit contains two independent molecules. Molecule A includes most of the Mtr4 polypeptide chain, with the exception of residues 363–391. Molecule B has well-defined electron density for the DExH core, which is essentially identical to that of molecule A.","type":"Results"}],"term_name":"disorder","reference_html":"Structural analysis reveals the characteristic features of Mtr4, a DExH helicase involved in nuclear RNA processing and surveillance. <i> Weir JR, Bonneau F, Hentschel J, Conti E. </i> Proc Natl Acad Sci U S A, 2010","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"20566885","date":"2024-02-06T16:44:33.487Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2XGJ"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"173115","entry_name":"poly(RNA)-3'-adenine ribonucleotide polyanion"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"}]},{"region_id":"DP01867r012","ec_ontology":"ECO","end":958,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":943,"version":3,"statement":[{"text":"A dashed line in the secondary structure plot indicates regions\nthat are not observed in the electron density.","type":"Supplementary material"}],"term_name":"disorder","reference_html":"The Mtr4 ratchet helix and arch domain both function to promote RNA unwinding. <i> Taylor LL, Jackson RN, Rexhepaj M, King AK, Lott LK, van Hoof A, Johnson SJ. </i> Nucleic Acids Res, 2014","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"25414331","date":"2024-02-06T16:02:45.233Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4QU4"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"CAS Registry Number","id":"18367"}]},{"region_id":"DP01867r013","ec_ontology":"ECO","end":389,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":361,"version":3,"statement":[{"text":"A dashed line in the secondary structure plot indicates regions\nthat are not observed in the electron density.","type":"Supplementary material"}],"term_name":"disorder","reference_html":"The Mtr4 ratchet helix and arch domain both function to promote RNA unwinding. <i> Taylor LL, Jackson RN, Rexhepaj M, King AK, Lott LK, van Hoof A, Johnson SJ. </i> Nucleic Acids Res, 2014","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"25414331","date":"2024-02-06T16:02:13.963Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4QU4"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18367","entry_name":"phosphate(3-)"}]},{"start":4,"end":17,"reference_id":"25319414","reference_source":"pmid","reference_html":"The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase. <i> Schuch B, Feigenbutz M, Makino DL, Falk S, Basquin C, Mitchell P, Conti E. </i> EMBO J, 2014","date":"2023-08-14T16:17:06.009Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4WFD"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P38801","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q12149","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01867r014","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:168049"}],"statement":[{"text":"Mtr4N binds as a short α-helix (residues 6–11), with extended segments at both ends. Apolar residues of Mtr4 (Leu6, Phe7, Val9, Phe10, Val 15 and Leu17) contact hydrophobic residues of Rrp6 (Leu10, Ile14 and Val17) and Rrp47 (Tyr10, Tyr55, Phe62, Leu77, Leu80 and Met87) ​(Fig5B).","type":"Results"},{"text":"The region that contacts the protein complex formed by UniProt Q12149 and P38801 is larger that just the Helix region, as shown by the gain of electron density in the PDB structure, and so the binding region corresponds to the 4-17 residues.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":20,"reference_id":"25319414","reference_source":"pmid","reference_html":"The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase. <i> Schuch B, Feigenbutz M, Makino DL, Falk S, Basquin C, Mitchell P, Conti E. </i> EMBO J, 2014","date":"2023-08-14T17:27:05.580Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P38801","operator":null,"partner_start":1,"partner_end":133},{"db":"UniProt","id":"Q12149","operator":"and","partner_start":1,"partner_end":111}],"region_id":"DP01867r015","statement":[{"text":"Rrp6N and Rrp47ΔC co-eluted with the N-terminal region of Mtr4 (Mtr480) (Fig1F, lane and peak 1), while no interaction was detected with the helicase domain (Mtr4Δ80) ​(Fig1E, peaks and lanes 4 and 5). In isolation, neither Rrp6N nor Rrp47ΔC interacted with Mtr4 (Fig1G, peaks and lanes 1, 2 and 3, 4, respectively), suggesting that both proteins are required for binding.","type":"Results"},{"text":"Rrp6N–Rrp47ΔC indeed formed a ternary complex with an Mtr41-20 peptide (Mtr4N) (Supplementary Fig S1B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":6,"end":11,"reference_id":"25319414","reference_source":"pmid","reference_html":"The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase. <i> Schuch B, Feigenbutz M, Makino DL, Falk S, Basquin C, Mitchell P, Conti E. </i> EMBO J, 2014","date":"2023-08-14T17:26:54.475Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"The construct encoding mtr4-gfp was cloned in yeast by homologous recombination, using HindIII linearized pAv675 (after deletion of the HindIII polylinker site) and a PCR amplicon encompassing the mtr4-gfp::HIS3 allele."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe7Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe10Ala","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q12149","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01867r016","statement":[{"text":"Immobilized zz-Rrp6 protein retained the wild-type Mtr4-gfp protein, whereas binding of the mtr4-gfpF7A,F10A mutant was only slightly above background levels (Fig​(Fig8B,8B, right panel). These data support the conclusion that the structurally defined Rrp6N–Rrp47N–Mtr4N complex forms the principal interaction between Rrp6 and Mtr4 in yeast.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":80,"reference_id":"20566885","reference_source":"pmid","reference_html":"Structural analysis reveals the characteristic features of Mtr4, a DExH helicase involved in nuclear RNA processing and surveillance. <i> Weir JR, Bonneau F, Hentschel J, Conti E. </i> Proc Natl Acad Sci U S A, 2010","date":"2024-02-06T16:31:22.658Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01867r017","statement":[{"text":"We identified by limited proteolysis the stable and conserved RNA-binding region of Saccharomyces cerevisiae Mtr4 encompassing residues 81–1073 (Mtr4-Δ80) (Figs. S1 and S2).","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_P47047","date":"2018-08-15T08:39:30.000Z","acc":"P47047","name":"ATP-dependent RNA helicase DOB1","length":1073,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000052EB1","genes":[{"name":{"value":"MTR4"},"synonyms":[{"value":"DOB1"}],"orfNames":[{"value":"J1158"}],"olnNames":[{"value":"YJL050W"}]}],"alphafold_very_low_content":0.10344827586206896,"disorder_content":0.13979496738117428,"disprot_consensus":{"full":[{"start":1,"end":85,"type":"D"},{"start":361,"end":391,"type":"D"},{"start":699,"end":713,"type":"D"},{"start":943,"end":961,"type":"D"}],"Structural state":[{"start":1,"end":85,"type":"D"},{"start":361,"end":391,"type":"D"},{"start":699,"end":713,"type":"D"},{"start":943,"end":961,"type":"D"}],"Molecular function":[{"start":1,"end":20,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00634","name":"BRCA2 repeat","start":1005,"end":1033},{"id":"PF00634","name":"BRCA2 repeat","start":1216,"end":1243},{"id":"PF00634","name":"BRCA2 repeat","start":1424,"end":1452},{"id":"PF00634","name":"BRCA2 repeat","start":1522,"end":1548},{"id":"PF00634","name":"BRCA2 repeat","start":1667,"end":1695},{"id":"PF00634","name":"BRCA2 repeat","start":1975,"end":2002},{"id":"PF00634","name":"BRCA2 repeat","start":2055,"end":2082},{"id":"PF09103","name":"BRCA2, oligonucleotide/oligosaccharide-binding, domain 1","start":2670,"end":2795},{"id":"PF09104","name":"BRCA2, oligonucleotide/oligosaccharide-binding, domain 3","start":3052,"end":3185},{"id":"PF09121","name":"Tower","start":2831,"end":2872},{"id":"PF09169","name":"BRCA2, helical","start":2482,"end":2667},{"id":"PF21318","name":"BRCA2, OB2","start":2969,"end":3035},{"id":"PF22687","name":"BRCA2 TR2 domain","start":3260,"end":3334}],"gene3D":[{"start":2800,"end":3043,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"},{"start":2669,"end":2799,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"},{"start":3052,"end":3197,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}]},"uniref50":"UniRef50_P51587","sequence":"MPIGSKERPTFFEIFKTRCNKADLGPISLNWFEELSSEAPPYNSEPAEESEHKNNNYEPNLFKTPQRKPSYNQLASTPIIFKEQGLTLPLYQSPVKELDKFKLDLGRNVPNSRHKSLRTVKTKMDQADDVSCPLLNSCLSESPVVLQCTHVTPQRDKSVVCGSLFHTPKFVKGRQTPKHISESLGAEVDPDMSWSSSLATPPTLSSTVLIVRNEEASETVFPHDTTANVKSYFSNHDESLKKNDRFIASVTDSENTNQREAASHGFGKTSGNSFKVNSCKDHIGKSMPNVLEDEVYETVVDTSEEDSFSLCFSKCRTKNLQKVRTSKTRKKIFHEANADECEKSKNQVKEKYSFVSEVEPNDTDPLDSNVANQKPFESGSDKISKEVVPSLACEWSQLTLSGLNGAQMEKIPLLHISSCDQNISEKDLLDTENKRKKDFLTSENSLPRISSLPKSEKPLNEETVVNKRDEEQHLESHTDCILAVKQAISGTSPVASSFQGIKKSIFRIRESPKETFNASFSGHMTDPNFKKETEASESGLEIHTVCSQKEDSLCPNLIDNGSWPATTTQNSVALKNAGLISTLKKKTNKFIYAIHDETSYKGKKIPKDQKSELINCSAQFEANAFEAPLTFANADSGLLHSSVKRSCSQNDSEEPTLSLTSSFGTILRKCSRNETCSNNTVISQDLDYKEAKCNKEKLQLFITPEADSLSCLQEGQCENDPKSKKVSDIKEEVLAAACHPVQHSKVEYSDTDFQSQKSLLYDHENASTLILTPTSKDVLSNLVMISRGKESYKMSDKLKGNNYESDVELTKNIPMEKNQDVCALNENYKNVELLPPEKYMRVASPSRKVQFNQNTNLRVIQKNQEETTSISKITVNPDSEELFSDNENNFVFQVANERNNLALGNTKELHETDLTCVNEPIFKNSTMVLYGDTGDKQATQVSIKKDLVYVLAEENKNSVKQHIKMTLGQDLKSDISLNIDKIPEKNNDYMNKWAGLLGPISNHSFGGSFRTASNKEIKLSEHNIKKSKMFFKDIEEQYPTSLACVEIVNTLALDNQKKLSKPQSINTVSAHLQSSVVVSDCKNSHITPQMLFSKQDFNSNHNLTPSQKAEITELSTILEESGSQFEFTQFRKPSYILQKSTFEVPENQMTILKTTSEECRDADLHVIMNAPSIGQVDSSKQFEGTVEIKRKFAGLLKNDCNKSASGYLTDENEVGFRGFYSAHGTKLNVSTEALQKAVKLFSDIENISEETSAEVHPISLSSSKCHDSVVSMFKIENHNDKTVSEKNNKCQLILQNNIEMTTGTFVEEITENYKRNTENEDNKYTAASRNSHNLEFDGSDSSKNDTVCIHKDETDLLFTDQHNICLKLSGQFMKEGNTQIKEDLSDLTFLEVAKAQEACHGNTSNKEQLTATKTEQNIKDFETSDTFFQTASGKNISVAKESFNKIVNFFDQKPEELHNFSLNSELHSDIRKNKMDILSYEETDIVKHKILKESVPVGTGNQLVTFQGQPERDEKIKEPTLLGFHTASGKKVKIAKESLDKVKNLFDEKEQGTSEITSFSHQWAKTLKYREACKDLELACETIEITAAPKCKEMQNSLNNDKNLVSIETVVPPKLLSDNLCRQTENLKTSKSIFLKVKVHENVEKETAKSPATCYTNQSPYSVIENSALAFYTSCSRKTSVSQTSLLEAKKWLREGIFDGQPERINTADYVGNYLYENNSNSTIAENDKNHLSEKQDTYLSNSSMSNSYSYHSDEVYNDSGYLSKNKLDSGIEPVLKNVEDQKNTSFSKVISNVKDANAYPQTVNEDICVEELVTSSSPCKNKNAAIKLSISNSNNFEVGPPAFRIASGKIVCVSHETIKKVKDIFTDSFSKVIKENNENKSKICQTKIMAGCYEALDDSEDILHNSLDNDECSTHSHKVFADIQSEEILQHNQNMSGLEKVSKISPCDVSLETSDICKCSIGKLHKSVSSANTCGIFSTASGKSVQVSDASLQNARQVFSEIEDSTKQVFSKVLFKSNEHSDQLTREENTAIRTPEHLISQKGFSYNVVNSSAFSGFSTASGKQVSILESSLHKVKGVLEEFDLIRTEHSLHYSPTSRQNVSKILPRVDKRNPEHCVNSEMEKTCSKEFKLSNNLNVEGGSSENNHSIKVSPYLSQFQQDKQQLVLGTKVSLVENIHVLGKEQASPKNVKMEIGKTETFSDVPVKTNIEVCSTYSKDSENYFETEAVEIAKAFMEDDELTDSKLPSHATHSLFTCPENEEMVLSNSRIGKRRGEPLILVGEPSIKRNLLNEFDRIIENQEKSLKASKSTPDGTIKDRRLFMHHVSLEPITCVPFRTTKERQEIQNPNFTAPGQEFLSKSHLYEHLTLEKSSSNLAVSGHPFYQVSATRNEKMRHLITTGRPTKVFVPPFKTKSHFHRVEQCVRNINLEENRQKQNIDGHGSDDSKNKINDNEIHQFNKNNSNQAVAVTFTKCEEEPLDLITSLQNARDIQDMRIKKKQRQRVFPQPGSLYLAKTSTLPRISLKAAVGGQVPSACSHKQLYTYGVSKHCIKINSKNAESFQFHTEDYFGKESLWTGKGIQLADGGWLIPSNDGKAGKEEFYRALCDTPGVDPKLISRIWVYNHYRWIIWKLAAMECAFPKEFANRCLSPERVLLQLKYRYDTEIDRSRRSAIKKIMERDDTAAKTLVLCVSDIISLSANISETSSNKTSSADTQKVAIIELTDGWYAVKAQLDPPLLAVLKNGRLTVGQKIILHGAELVGSPDACTPLEAPESLMLKISANSTRPARWYTKLGFFPDPRPFPLPLSSLFSDGGNVGCVDVIIQRAYPIQWMEKTSSGLYIFRNEREEEKEAAKYVEAQQKRLEALFTKIQEEFEEHEENTTKPYLPSRALTRQQVRALQDGAELYEAVKNAADPAYLEGYFSEEQLRALNNHRQMLNDKKQAQIQLEIRKAMESAEQKEQGLSRDVTTVWKLRIVSYSKKEKDSVILSIWRPSSDLYSLLTEGKRYRIYHLATSKSKSKSERANIQLAATKKTQYQQLPVSDEILFQIYQPREPLHFSKFLDPDFQPSCSEVDLIGFVVSVVKKTGLAPFVYLSDECYNLLAIKFWIDLNEDIIKPHMLIAASNLQWRPESKSGLLTLFAGDFSVFSASPKEGHFQETFNKMKNTVENIDILCNEAENKLMHILHANDPKWSTPTKDCTSGPYTAQIIPGTGNKLLMSSPNCEIYYQSPLSLCMAKRKSVSTPVSAQMTSKSCKGEKEIDDQKNCKKRRALDFLSRLPLPPPVSPICTFVSPAAQKAFQPPRSCGTKYETPIKKKELNSPQMTPFKKFNEISLLESNSIADEELALINTQALLSGSTGEKQFISVSESTRTAPTSSEDYLRLKRRCTTSLIKEQESSQASTEECEKNKQDTITTKKYI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P51587","disprot_id":"DP01869","ncbi_taxon_id":9606,"regions_counter":4,"creator":"nfarahi","regions":[{"start":48,"end":284,"reference_id":"31900740","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N backbone resonance assignment of the human BRCA2 N-terminal region. <i> Julien M, Miron S, Carreira A, Theillet FX, Zinn-Justin S. </i> Biomol NMR Assign, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"BMRB","id":"50077"},{"db":"BMRB","id":"50078"},{"db":"BMRB","id":"50079"}],"region_id":"DP01869r004","statement":[{"text":"Analysis of these chemical shifts confirmed that BRCA2 48–284 shows no stable fold: it is intrinsically disordered, with only short, transient α-helices.","type":"Abstract"},{"text":"The narrow range of backbone amide 1H chemical shifts (between 7.5 and 8.5 ppm) for all BRCA2 fragments reveals their disordered behavior.","type":"Article"},{"text":"The secondary structure analysis, based on 13Cα and 13Cβ chemical shifts and the neighbor corrected structural propensity method (Tamiola et al. 2010; Tamiola and Mulder 2012), confirms the absence of a stable fold for BRCA2 53–131, BRCA2 48–218(C4A) and BRCA2 190–284.","type":"Article"},{"text":"We concluded that the fragment of BRCA2 from amino acid 48 to amino acid 284 is disordered and that its shorter segments BRCA2 53–131, BRCA2 48–218(C4A) and BRCA2 190–284 have the same structural properties when isolated or within BRCA2 48–284(C4A).","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-09T11:45:15.080Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P51587","date":"2018-08-15T09:06:33.000Z","acc":"P51587","name":"Breast cancer type 2 susceptibility protein","length":3418,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI00001D9A9C","genes":[{"name":{"value":"BRCA2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:1101","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:1101"}}]},"synonyms":[{"value":"FACD"},{"value":"FANCD1"}]}],"disorder_content":0.06933879461673494,"disprot_consensus":{"full":[{"start":48,"end":284,"type":"D"}],"Structural state":[{"start":48,"end":284,"type":"D"}]}},{"features":{"pfam":[{"id":"PF15511","name":"Centromere kinetochore component CENP-T histone fold","start":44,"end":96}],"gene3D":[{"start":2,"end":103,"id":"1.10.20.10","name":"Histone, subunit A"}]},"uniref50":"UniRef50_P84040","sequence":"MTGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_P84040","disprot_id":"DP01870","ncbi_taxon_id":7227,"regions_counter":5,"creator":"zskalman","regions":[{"start":1,"end":26,"reference_id":"32134144","reference_source":"pmid","reference_html":"Structural basis for centromere maintenance by Drosophila CENP-A chaperone CAL1. <i> Medina-Pritchard B, Lazou V, Zou J, Byron O, Abad MA, Rappsilber J, Heun P, Jeyaprakash AA. </i> EMBO J, 2020","date":"2024-11-20T08:41:40.770Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"6XWS"},{"db":"PDB","id":"6XWT"}],"region_id":"DP01870r003","statement":[{"text":"Missing electron density for the region.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9V6Q2"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":" Q9VEN2"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-03T19:52:16.756Z"}},{"start":2,"end":15,"reference_id":"17957772","reference_source":"pmid","reference_html":"Structure of the Drosophila nucleosome core particle highlights evolutionary constraints on the H2A-H2B histone dimer. <i> Clapier CR, Chakravarthy S, Petosa C, Fernández-Tornero C, Luger K, Müller CW. </i> Proteins, 2008","date":"2025-02-03T19:46:40.406Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"2PYO"}],"region_id":"DP01870r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02283"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84051"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02299"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"DNA fragment derived from human α-satellite DNA with sequence 5'-ATCAATATCCACCTGCAGATACTACCAAAAGTGTATTTGGAAACTGCTCCATCAAAAGGCATGTTCAGCTGGAATCCAGCTGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTGGTAGTATCTGCAGGTGGATATTGAT"}]}],"statement":[{"text":"Unstructured residues are indicated in lower case.","type":"Figure"}]},{"start":2,"end":15,"reference_id":"17957772","reference_source":"pmid","reference_html":"Structure of the Drosophila nucleosome core particle highlights evolutionary constraints on the H2A-H2B histone dimer. <i> Clapier CR, Chakravarthy S, Petosa C, Fernández-Tornero C, Luger K, Müller CW. </i> Proteins, 2008","date":"2025-02-03T19:46:51.260Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"2PYO"}],"region_id":"DP01870r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02283"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84051"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02299"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"DNA fragment derived from human α-satellite DNA with sequence 5'-ATCAATATCCACCTGCAGATACTACCAAAAGTGTATTTGGAAACTGCTCCATCAAAAGGCATGTTCAGCTGGAATCCAGCTGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTGGTAGTATCTGCAGGTGGATATTGAT"}]}],"statement":[{"text":"Unstructured residues are indicated in lower case.","type":"Figure"}]}],"released":"2018_11","uniref100":"UniRef100_P84040","date":"2018-08-15T09:26:25.000Z","acc":"P84040","name":"Histone H4","length":103,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI000011F964","genes":[{"name":{"value":"His4"},"synonyms":[{"value":"H4"}]},{"name":{"value":"His4r"},"synonyms":[{"value":"H4r"}],"orfNames":[{"value":"CG3379"}]},{"name":{"value":"His4:CG31611"},"orfNames":[{"value":"CG31611"}]},{"name":{"value":"His4:CG33869"},"orfNames":[{"value":"CG33869"}]},{"name":{"value":"His4:CG33871"},"orfNames":[{"value":"CG33871"}]},{"name":{"value":"His4:CG33873"},"orfNames":[{"value":"CG33873"}]},{"name":{"value":"His4:CG33875"},"orfNames":[{"value":"CG33875"}]},{"name":{"value":"His4:CG33877"},"orfNames":[{"value":"CG33877"}]},{"name":{"value":"His4:CG33879"},"orfNames":[{"value":"CG33879"}]},{"name":{"value":"His4:CG33881"},"orfNames":[{"value":"CG33881"}]},{"name":{"value":"His4:CG33883"},"orfNames":[{"value":"CG33883"}]},{"name":{"value":"His4:CG33885"},"orfNames":[{"value":"CG33885"}]},{"name":{"value":"His4:CG33887"},"orfNames":[{"value":"CG33887"}]},{"name":{"value":"His4:CG33889"},"orfNames":[{"value":"CG33889"}]},{"name":{"value":"His4:CG33891"},"orfNames":[{"value":"CG33891"}]},{"name":{"value":"His4:CG33893"},"orfNames":[{"value":"CG33893"}]},{"name":{"value":"His4:CG33895"},"orfNames":[{"value":"CG33895"}]},{"name":{"value":"His4:CG33897"},"orfNames":[{"value":"CG33897"}]},{"name":{"value":"His4:CG33899"},"orfNames":[{"value":"CG33899"}]},{"name":{"value":"His4:CG33901"},"orfNames":[{"value":"CG33901"}]},{"name":{"value":"His4:CG33903"},"orfNames":[{"value":"CG33903"}]},{"name":{"value":"His4:CG33905"},"orfNames":[{"value":"CG33905"}]},{"name":{"value":"His4:CG33907"},"orfNames":[{"value":"CG33907"}]},{"name":{"value":"His4:CG33909"},"orfNames":[{"value":"CG33909"}]}],"alphafold_very_low_content":0,"disorder_content":0.2524271844660194,"disprot_consensus":{"full":[{"start":1,"end":26,"type":"D"}],"Structural state":[{"start":1,"end":26,"type":"D"}],"Disorder function":[{"start":2,"end":15,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00992","name":"Troponin","start":15,"end":145}],"gene3D":[{"start":1,"end":161,"id":"1.20.5.350","name":"1.20.5.350"}]},"uniref50":"UniRef50_P48788","sequence":"MSDEEKKRRAATARRQHLKSAMLQLAVTEIEKEAAAKEVEKQNYLAEHCPPLSLPGSMQELQELCKKLHAKIDSVDEERYDTEVKLQKTNKELEDLSQKLFDLRGKFKRPPLRRVRMSADAMLRALLGSKHKVNMDLRANLKQVKKEDTEKEKDLRDVGDWRKNIEEKSGMEGRKKMFEAGES","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Phasianinae","Gallus"],"uniref90":"UniRef90_P68246","disprot_id":"DP01871","ncbi_taxon_id":9031,"regions_counter":2,"creator":"mpajkos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":181,"region_id":"DP01871r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Is there nascent structure in the intrinsically disordered region of troponin I? <i> Julien O, Mercier P, Allen CN, Fisette O, Ramos CH, Lagüe P, Blumenschein TM, Sykes BD. </i> Proteins, 2011","statement":[{"text":"They have constructed a skeletal TnC-TnI chimera to study the structure and dynamics of the regulatory region of troponin, combining the skeletal N-terminal domain of TnC (sNTnC) and the C-terminal region of TnI (sTnI) in a single polypeptidic chain (chicken fast skeletal was used).\n\"These values are typical for a globular domain for sTnC and a disordered region for the C-terminal region of sTnI.\"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":137,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21322033","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP01871r002","ec_ontology":"ECO","end":183,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":145,"version":3,"statement":[{"text":"There was no visible electron density for the 39 C-terminal amino acid residues (144–182) of TnI or the C-terminal residues of TnT2 (249–262).","type":"Methods"}],"term_name":"disorder","reference_html":"Ca(2+)-regulated structural changes in troponin. <i> Vinogradova MV, Stone DB, Malanina GG, Karatzaferi C, Cooke R, Mendelson RA, Fletterick RJ. </i> Proc Natl Acad Sci U S A, 2005","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15784741","date":"2024-02-06T17:49:43.428Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1YTZ"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P12620"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02588"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:14123494"}]}],"released":"2018_11","uniref100":"UniRef100_P68246","date":"2018-08-15T09:32:44.000Z","acc":"P68246","name":"Troponin I, fast skeletal muscle","length":183,"organism":"Gallus gallus","dataset":[],"UniParc":"UPI00001711E5","genes":[{"name":{"value":"TNNI2"}}],"alphafold_very_low_content":0.07650273224043716,"disorder_content":0.2568306010928962,"disprot_consensus":{"full":[{"start":137,"end":183,"type":"D"}],"Structural state":[{"start":137,"end":183,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01398","name":"JAB1/Mov34/MPN/PAD-1 ubiquitin protease","start":253,"end":361},{"id":"PF08969","name":"USP8 dimerisation domain","start":13,"end":116}],"gene3D":[{"start":246,"end":424,"id":"3.40.140.10","name":"Cytidine Deaminase, domain 2"}]},"uniref50":"UniRef50_O95630","sequence":"MSDHGDVSLPPEDRVRALSQLGSAVEVNEDIPPRRYFRSGVEIIRMASIYSEEGNIEHAFILYNKYITLFIEKLPKHRDYKSAVIPEKKDTVKKLKEIAFPKAEELKAELLKRYTKEYTEYNEEKKKEAEELARNMAIQQELEKEKQRVAQQKQQQLEQEQFHAFEEMIRNQELEKERLKIVQEFGKVDPGLGGPLVPDLEKPSLDVFPTLTVSSIQPSDCHTTVRPAKPPVVDRSLKPGALSNSESIPTIDGLRHVVVPGRLCPQFLQLASANTARGVETCGILCGKLMRNEFTITHVLIPKQSAGSDYCNTENEEELFLIQDQQGLITLGWIHTHPTQTAFLSSVDLHTHCSYQMMLPESVAIVCSPKFQETGFFKLTDHGLEEISSCRQKGFHPHSKDPPLFCSCSHVTVVDRAVTITDLR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O95630","disprot_id":"DP01872","ncbi_taxon_id":9606,"regions_counter":3,"creator":"bhajdu","regions":[{"region_id":"DP01872r001","ec_ontology":"ECO","end":241,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":228,"version":3,"statement":[{"text":"Only i,i + 1 sequential intra-NOEs could be detected from NOESY experiments, which support the previous prediction and reflect the fact that AMSH-P2 is unstructured in the free state.","type":"Results"},{"text":"As in the free state, it is important to mention that we only detected i,i + 1 sequential NOEs, supporting the fact that AMSH-P2 is also unstructured when bound to SH3.","type":"Results"}],"term_name":"disorder","reference_html":"NMR Reveals the Interplay among the AMSH SH3 Binding Motif, STAM2, and Lys63-Linked Diubiquitin. <i> Hologne M, Cantrelle FX, Riviere G, Guillière F, Trivelli X, Walker O. </i> J Mol Biol, 2016","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27725184","date":"2023-05-15T16:51:22.603Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5IXF"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75886"}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":241,"term_name":"protein binding","released":"2023_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"NMR Reveals the Interplay among the AMSH SH3 Binding Motif, STAM2, and Lys63-Linked Diubiquitin. <i> Hologne M, Cantrelle FX, Riviere G, Guillière F, Trivelli X, Walker O. </i> J Mol Biol, 2016","statement":[{"text":"As in the free state, it is important to mention that we only detected i,i + 1 sequential NOEs, supporting the fact that AMSH-P2 is also unstructured when bound to SH3.","type":"Results"}],"term_id":"GO:0005515","curator_id":"vnugnes","start":228,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"27725184","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-15T16:52:16.856Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01872r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"5IXF"}],"interaction_partner":[{"db":"UniProt","id":"O75886","operator":"and","partner_start":null,"partner_end":null}]},{"start":219,"end":245,"reference_id":"21888914","reference_source":"pmid","reference_html":"Structural and thermodynamic comparison of the catalytic domain of AMSH and AMSH-LP: nearly identical fold but different stability. <i> Davies CW, Paul LN, Kim MI, Das C. </i> J Mol Biol, 2011","date":"2023-05-15T16:59:12.932Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu280Ala","start":null,"end":null,"position":null}],"region_id":"DP01872r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"}],"statement":[{"text":" The N-terminal SH3-binding peptide segment was not visualized in the structure perhaps because of disorder in the crystal, suggesting that this peptide segment is flexible and is easily accessible for binding to the SH3 domain of STAM.","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_O95630","date":"2018-08-15T10:00:12.000Z","acc":"O95630","name":"STAM-binding protein","length":424,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI0000038DA0","genes":[{"name":{"value":"STAMBP"},"synonyms":[{"value":"AMSH","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10383417","url":"http://www.ncbi.nlm.nih.gov/pubmed/10383417","alternativeUrl":"https://europepmc.org/abstract/MED/10383417"}}]}]}],"alphafold_very_low_content":0.11320754716981132,"disorder_content":0.06367924528301887,"disprot_consensus":{"full":[{"start":219,"end":245,"type":"D"}],"Structural state":[{"start":219,"end":245,"type":"D"}],"Molecular function":[{"start":228,"end":241,"type":"F"}]}},{"features":{"pfam":[{"id":"PF27818","name":"Proheparin-binding EGF-like growth factor C-terminal domain","start":152,"end":196}],"gene3D":[{"start":97,"end":145,"id":"2.10.25.10","name":"Laminin"}]},"uniref50":"UniRef50_Q99075","sequence":"MKLLPSVVLKLFLAAVLSALVTGESLERLRRGLAAGTSNPDPPTVSTDQLLPLGGGRDRKVRDLQEADLDLLRVTLSSKPQALATPNKEEHGKRKKKGKGLGKKRDPCLRKYKDFCIHGECKYVKELRAPSCICHPGYHGERCHGLSLPVENRLYTYDHTTILAVVAVVLSSVCLLVIVGLLMFRYHRRGGYDVENEEKVKLGMTNSH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q99075","disprot_id":"DP01873","ncbi_taxon_id":9606,"regions_counter":1,"creator":"sgovind","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":106,"region_id":"DP01873r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the complex of diphtheria toxin with an extracellular fragment of its receptor. <i> Louie GV, Yang W, Bowman ME, Choe S. </i> Mol Cell, 1997","statement":[{"text":"Residues of the heparin-binding module of HBEGF (residues 73–106). These are not visible in electron-density maps and are presumably disordered.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"sgovind","start":73,"term_ontology":"IDPO","curator_name":"Sudha Govindarajan","reference_id":"9659904","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1XDT"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q99075","date":"2018-08-15T10:01:44.000Z","acc":"Q99075","name":"Proheparin-binding EGF-like growth factor","length":208,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000035E3F","genes":[{"name":{"value":"HBEGF"},"synonyms":[{"value":"DTR"},{"value":"DTS"},{"value":"HEGFL"}]}],"alphafold_very_low_content":0.2644230769230769,"disorder_content":0.16346153846153846,"disprot_consensus":{"full":[{"start":73,"end":106,"type":"D"}],"Structural state":[{"start":73,"end":106,"type":"D"}]}},{"features":{"pfam":[{"id":"PF11538","name":"Snurportin1","start":25,"end":64},{"id":"PF21974","name":"Snurportin1, m3G cap-binding domain","start":101,"end":279}],"gene3D":[{"start":3,"end":312,"id":"3.30.470.30","name":"DNA ligase/mRNA capping enzyme"}]},"uniref50":"UniRef50_O95149","sequence":"MEELSQALASSFSVSQDLNSTAAPHPRLSQYKSKYSSLEQSERRRRLLELQKSKRLDYVNHARRLAEDDWTGMESEEENKKDDEEMDIDTVKKLPKHYANQLMLSEWLIDVPSDLGQEWIVVVCPVGKRALIVASRGSTSAYTKSGYCVNRFSSLLPGGNRRNSTAKDYTILDCIYNEVNQTYYVLDVMCWRGHPFYDCQTDFRFYWMHSKLPEEEGLGEKTKLNPFKFVGLKNFPCTPESLCDVLSMDFPFEVDGLLFYHKQTHYSPGSTPLVGWLRPYMVSDVLGVAVPAGPLTTKPDYAGHQLQQIMEHKKSQKEGMKEKLTHKASENGHYELEHLSTPKLKGSSHSPDHPGCLMEN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O95149","disprot_id":"DP01874","ncbi_taxon_id":9606,"regions_counter":2,"creator":"lalvarez","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":348,"region_id":"DP01874r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the nuclear export receptor CRM1 in complex with Snurportin1 and RanGTP. <i> Monecke T, Güttler T, Neumann P, Dickmanns A, Görlich D, Ficner R. </i> Science, 2009","statement":[{"text":"In the final model of SPN1, residues 31-33, 72-91, 162-165 and 288-348 of one complex in the asymmetric unit, and residues 30-32, 74-92, 162-165 and 291-348 of the other one were not defined in the electron density map and thus they were not built.","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"lalvarez","start":288,"term_ontology":"IDPO","curator_name":"Lucía Álvarez","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-1437-5773","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3GJX"}],"reference_id":"19389996","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":91,"region_id":"DP01874r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the nuclear export receptor CRM1 in complex with Snurportin1 and RanGTP. <i> Monecke T, Güttler T, Neumann P, Dickmanns A, Görlich D, Ficner R. </i> Science, 2009","statement":[{"text":"In the final model of SPN1, residues 31-33, 72-91, 162-165 and 288-348 of one complex in the asymmetric unit, and residues 30-32, 74-92, 162-165 and 291-348 of the other one were not defined in the electron density map and thus they were not built.","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"lalvarez","start":72,"term_ontology":"IDPO","curator_name":"Lucía Álvarez","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-1437-5773","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3GJX"}],"reference_id":"19389996","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_O95149","date":"2018-08-15T10:01:56.000Z","acc":"O95149","name":"Snurportin-1","length":360,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000031A89","genes":[{"name":{"value":"SNUPN"},"synonyms":[{"value":"RNUT1"},{"value":"SPN1"}]}],"alphafold_very_low_content":0.13055555555555556,"disorder_content":0.225,"disprot_consensus":{"full":[{"start":72,"end":91,"type":"D"},{"start":288,"end":348,"type":"D"}],"Structural state":[{"start":72,"end":91,"type":"D"},{"start":288,"end":348,"type":"D"}]}},{"features":{"pfam":[{"id":"PF09528","name":"Ehrlichia tandem repeat (Ehrlichia_rpt)","start":56,"end":91},{"id":"PF09528","name":"Ehrlichia tandem repeat (Ehrlichia_rpt)","start":136,"end":171},{"id":"PF09528","name":"Ehrlichia tandem repeat (Ehrlichia_rpt)","start":216,"end":251},{"id":"PF09528","name":"Ehrlichia tandem repeat (Ehrlichia_rpt)","start":296,"end":331},{"id":"PF09528","name":"Ehrlichia tandem repeat (Ehrlichia_rpt)","start":376,"end":414}]},"uniref50":"UniRef50_Q2GI62","sequence":"MDIDNSNISTADIRSNTDGLIDIIMRILGFGNKNIVQPQDLGSEIYQQEQEDDTVSQPSLEPFVAESEVSKVEQEKTNPEVLIKDLQDVASHESGVSDQPAQVVTERENEIESHQGETEKESGITESHQKEDEIVSQSSSEPFVAESEVSKVEQEETNPEVLIKDLQDVASHESGVSDQPAQVVTERESEIESHQGETEKESGITESHQKEDEIVSQPSSEPFVAESEVSKVEQEETNPEVLIKDLQDVASHESGVSDQPAQVVTERESEIESHQGETEKESGITESHQKEDEIVSQPSSEPFVAESEVSKVEQEETNPEVLIKDLQDVASHESGVSDQPAQVVTERESEIESHQGETEKESGITESHQKEDEIVSQPSSEPFVAESEVSKVEQEKTNPEILVEDLPLGQVIPVVVEKDEMFAPSFNPIVIKEEDKVCETCEQEFEIVKDSQTVKGSEDIISPIECLESMDSIVSTIFESGMLCPMSKPGQYVCGYEMYMYGFQDVKDLLGGLLSNVPVCCNVSLYFMEHNYFTNHENINHNVVNDIV","taxonomy":["Bacteria","Proteobacteria","Alphaproteobacteria","Rickettsiales","Anaplasmataceae","Ehrlichia"],"uniref90":"UniRef90_Q2GI62","disprot_id":"DP01875","ncbi_taxon_id":205920,"regions_counter":4,"creator":"okovacs","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":221,"region_id":"DP01875r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Ehrlichia chaffeensis TRP120 nucleomodulin binds DNA with disordered tandem repeat domain. <i> Klema VJ, Sepuru KM, Füllbrunn N, Farris TR, Dunphy PS, McBride JW, Rajarathnam K, Choi KH. </i> PLoS One, 2018","statement":[{"text":"We first collected 1H-15N NMR HSQC spectra of TRP120-1TR as a function of pH (5.5, 6.0, 6.5 and 7.0), and observed that the protein is essentially unstructured in solution at all pHs tested. The NMR spectrum shows around 80 (of the 102 residues) resonances between 6.7 and 8.6 ppm. Most of the chemical shifts correspond to that of a random and thus NMR data are consistent with a natively unfolded protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":142,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"29641592","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":221,"term_name":"nucleic acid binding","start":142,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"The pH of ehrlichial morulae where TRP120 is expressed is slightly acidic. Addition of DNA to TRP120-1TR at pH 5.5 resulted in several new peaks with significant differences in chemical shifts, suggesting an increase in β-strand content. Peaks corresponding to several side chain NH2 of Asn/Gln residues were resolved in the DNA-bound spectrum, indicating that they become structured upon DNA binding.","type":"Results"}],"curator_id":"okovacs","released":"2022_03","term_ontology":"GO","curator_name":"Orsolya Panna Kovacs","reference_id":"29641592","version":3,"reference_html":"Ehrlichia chaffeensis TRP120 nucleomodulin binds DNA with disordered tandem repeat domain. <i> Klema VJ, Sepuru KM, Füllbrunn N, Farris TR, Dunphy PS, McBride JW, Rajarathnam K, Choi KH. </i> PLoS One, 2018","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006165","region_id":"DP01875r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":221,"region_id":"DP01875r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Ehrlichia chaffeensis TRP120 nucleomodulin binds DNA with disordered tandem repeat domain. <i> Klema VJ, Sepuru KM, Füllbrunn N, Farris TR, Dunphy PS, McBride JW, Rajarathnam K, Choi KH. </i> PLoS One, 2018","statement":[{"text":"The far-UV CD spectra of TRP120-1TR at pH 7.0 showed a profile with a minimum centered at 200 nm, indicating that TRP120 TR units are mostly intrinsically disordered. A shallow negative feature centered at 220 nm suggests a small percentage of β-turn/β-sheet secondary structure. CD spectra of TRP120-2TR measured as a function of pH (7.0, 6.0 and 4.5) showed similar profiles.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":142,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"29641592","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":221,"region_id":"DP01875r004","released":"2022_03","ec_id":"ECO:0007689","reference_html":"Ehrlichia chaffeensis TRP120 nucleomodulin binds DNA with disordered tandem repeat domain. <i> Klema VJ, Sepuru KM, Füllbrunn N, Farris TR, Dunphy PS, McBride JW, Rajarathnam K, Choi KH. </i> PLoS One, 2018","statement":[{"text":"Although the predicted molecular weight of TRP120-1TR based on the primary sequences is 11.5 kDa, the construct migrates with apparent molecular weight of ~19 kDa. The analytical ultracentrifugation clearly shows that both TRP120-1TR and -2TR proteins are monomers with expected molecular weights. Thus, aberrant migration of the TRP120 TR unit on SDS-PAGE is intrinsic to the nature of the domain.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":142,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"29641592","version":2,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q2GI62","date":"2018-08-15T10:10:51.000Z","acc":"Q2GI62","name":"120 kDa immunodominant surface protein","length":548,"organism":"Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas)","dataset":[],"UniParc":"UPI00006A825D","genes":[{"olnNames":[{"value":"ECH_0039","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ABD44969.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABD44969.1"}}]}]}],"alphafold_very_low_content":1,"disorder_content":0.145985401459854,"disprot_consensus":{"full":[{"start":142,"end":221,"type":"D"}],"Structural state":[{"start":142,"end":221,"type":"D"}],"Molecular function":[{"start":142,"end":221,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02178","name":"AT hook motif","start":26,"end":36},{"id":"PF02178","name":"AT hook motif","start":46,"end":58},{"id":"PF02178","name":"AT hook motif","start":74,"end":85}]},"uniref50":"UniRef50_P52926","sequence":"MSARGEGAGQPSTSAQGQPAAPAPQKRGRGRPRKQQQEPTGEPSPKRPRGRPKGSKNKSPSKAAQKKAEATGEKRPRGRPRKWPQQVVQKKPAQEETEETSSQESAEED","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P52926","disprot_id":"DP01876","ncbi_taxon_id":9606,"regions_counter":4,"creator":"okovacs","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":109,"region_id":"DP01876r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Nanoscale Assembly of High-Mobility Group AT-Hook 2 Protein with DNA Replication Fork. <i> Krahn N, Meier M, To V, Booy EP, McEleney K, O'Neil JD, McKenna SA, Patel TR, Stetefeld J. </i> Biophys J, 2017","statement":[{"text":"Far-UV CD spectropolarimetry of HMGA2 produced a spectrum with a minimum at 199 nm followed by a flat line from 210 to 250 nm. This spectrum appeared identical to that of a disordered protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":1,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"29262356","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-04-07T08:27:15.206Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":109,"region_id":"DP01876r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Nanoscale Assembly of High-Mobility Group AT-Hook 2 Protein with DNA Replication Fork. <i> Krahn N, Meier M, To V, Booy EP, McEleney K, O'Neil JD, McKenna SA, Patel TR, Stetefeld J. </i> Biophys J, 2017","statement":[{"text":"The HSQC spectrum of HMGA2 displayed a very narrow chemical shift range in the proton dimension that is highly characteristic of a disordered protein. In particular, the 1H resonances fall between 7.9 and 8.6 ppm.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":1,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"29262356","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-04-07T08:27:16.158Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":109,"term_name":"nucleic acid binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Upon interaction with a replication fork (RF), HMGA2 forms an equimolar complex by binding in a side-by-side orientation. It is necessary for HMGA2 to be in a disordered state such that it has the flexibility to stabilize a stalled RF by binding to the necessary AT-rich sites.","type":"Introduction"}],"curator_id":"okovacs","released":"2022_03","term_ontology":"GO","curator_name":"Orsolya Panna Kovacs","reference_id":"29262356","version":3,"reference_html":"Nanoscale Assembly of High-Mobility Group AT-Hook 2 Protein with DNA Replication Fork. <i> Krahn N, Meier M, To V, Booy EP, McEleney K, O'Neil JD, McKenna SA, Patel TR, Stetefeld J. </i> Biophys J, 2017","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006165","region_id":"DP01876r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":109,"region_id":"DP01876r004","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Nanoscale Assembly of High-Mobility Group AT-Hook 2 Protein with DNA Replication Fork. <i> Krahn N, Meier M, To V, Booy EP, McEleney K, O'Neil JD, McKenna SA, Patel TR, Stetefeld J. </i> Biophys J, 2017","statement":[{"text":"In general, the Kratky analysis of SAXS data for proteins provided qualitative information on the overall shape of the biomolecule of interest. The ascending linear curve (coral) observed for HMGA2 in the Porod-Debye Plateau region was indicative of a disordered protein, which agrees with results from the CD and NMR analyses.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":1,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"29262356","version":2,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-04-07T08:27:17.916Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P52926","date":"2018-08-15T10:34:32.000Z","acc":"P52926","name":"High mobility group protein HMGI-C","length":109,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI0000000CE6","genes":[{"name":{"value":"HMGA2"},"synonyms":[{"value":"HMGIC"}]}],"alphafold_very_low_content":0.13761467889908258,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":109,"type":"D"}],"Structural state":[{"start":1,"end":109,"type":"D"}],"Molecular function":[{"start":1,"end":109,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02732","name":"ERCC4 domain","start":270,"end":439},{"id":"PF21292","name":"EME1/MUS81, C-terminal","start":481,"end":554}],"gene3D":[{"start":467,"end":570,"id":"1.10.150.670","name":"Crossover junction endonuclease EME1, DNA-binding domain"},{"start":380,"end":447,"id":"3.40.50.11760","name":"ERCC4, Mus81-Eme1 complex, nuclease domain, subdomain 2"},{"start":309,"end":378,"id":"3.40.50.11760","name":"ERCC4, Mus81-Eme1 complex, nuclease domain, subdomain 2"},{"start":247,"end":308,"id":"3.40.1620.30","name":"ERCC4, Mus81-Eme1 complex, nuclease domain, subdomain 1"}]},"uniref50":"UniRef50_Q96AY2","sequence":"MALKKSSPSLDSGDSDSEELPTFAFLKKEPSSTKRRQPEREEKIVVVDISDCEASCPPAPELFSPPVPEIAETVTQTQPVRLLSSESEDEEEFIPLAQRLTCKFLTHKQLSPEDSSSPVKSVLDHQNNEGASCDWKKPFPKIPEVPLHDTPERSAADNKDLILDPCCQLPAYLSTCPGQSSSLAVTKTNSDILPPQKKTKPSQKVQGRGSHGCRQQRQARQKESTLRRQERKNAALVTRMKAQRPEECLKHIIVVLDPVLLQMEGGGQLLGALQTMECRCVIEAQAVPCSVTWRRRAGPSEDREDWVEEPTVLVLLRAEAFVSMIDNGKQGSLDSTMKGKETLQGFVTDITAKTAGKALSLVIVDQEKCFSAQNPPRRGKQGANKQTKKQQQRQPEASIGSMVSRVDAEEALVDLQLHTEAQAQIVQSWKELADFTCAFTKAVAEAPFKKLRDETTFSFCLESDWAGGVKVDLAGRGLALVWRRQIQQLNRVSLEMASAVVNAYPSPQLLVQAYQQCFSDKERQNLLADIQVRRGEGVTSTSRRIGPELSRRIYLQMTTLQPHLSLDSAD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q96AY2","disprot_id":"DP01877","ncbi_taxon_id":9606,"regions_counter":6,"creator":"lalvarez","regions":[{"term_namespace":"Structural transition","ec_ontology":"ECO","end":455,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structures of the structure-selective nuclease Mus81-Eme1 bound to flap DNA substrates. <i> Gwon GH, Jo A, Baek K, Jin KS, Fu Y, Lee JB, Kim Y, Cho Y. </i> EMBO J, 2014","statement":[{"text":"The disordered loop (residues 445–455) becomes ordered and extends the five-turn helix (a7) to a continuous and kinked (at Pro447) eight-turn helix (Fig 2A–D).","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"lalvarez","start":445,"term_ontology":"IDPO","curator_name":"Lucía Álvarez","reference_id":"24733841","version":2,"curator_orcid":"0000-0002-1437-5773","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01877r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":402,"region_id":"DP01877r003","reference_id":"18413719","start":369,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The limited proteolytic digestion analysis suggested that residues between 368 and 403 in hEme1 are connected by a highly flexible linker, which we presumed to be a loop region","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cleavage assay evidence used in manual assertion","version":3,"reference_html":"Crystal structure of the Mus81-Eme1 complex. <i> Chang JH, Kim JJ, Choi JM, Lee JH, Cho Y. </i> Genes Dev, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","cross_refs":[{"db":"PDB","id":"2ZIW"},{"db":"PDB","id":"2ZIV"},{"db":"PDB","id":"2ZIU"},{"db":"PDB","id":"2ZIX"}],"term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":402,"region_id":"DP01877r004","reference_id":"18413719","start":369,"term_id":"GO:0003677","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The limited proteolytic digestion analysis suggested that residues between 368 and 403 in hEme1 are connected by a highly flexible linker, which we presumed to be a loop region","type":"Results"},{"text":"Cleavage of the 36R linker of hEme1 into two parts also significantly decreased the nuclease activity and the DNA-binding affinity of the hMUS81ΔN complex. Reducing the size of this cleaved linker of hEme1 by 10 or 26 residues abrogated the DNA-binding and nuclease activities of hMUS81ΔN on 3′ flap and nHJ substrates, demonstrating the importance of this 36R linker in DNA binding and cleavage.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"Crystal structure of the Mus81-Eme1 complex. <i> Chang JH, Kim JJ, Choi JM, Lee JH, Cho Y. </i> Genes Dev, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2ZIW"},{"db":"PDB","id":"2ZIV"},{"db":"PDB","id":"2ZIU"},{"db":"PDB","id":"2ZIX"}],"term_name":"DNA binding","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":402,"region_id":"DP01877r005","reference_id":"18413719","start":369,"term_id":"IDPO:0000033","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The limited proteolytic digestion analysis suggested that residues between 368 and 403 in hEme1 are connected by a highly flexible linker, which we presumed to be a loop region","type":"Results"},{"text":"Cleavage of the 36R linker of hEme1 into two parts also significantly decreased the nuclease activity and the DNA-binding affinity of the hMUS81ΔN complex. Reducing the size of this cleaved linker of hEme1 by 10 or 26 residues abrogated the DNA-binding and nuclease activities of hMUS81ΔN on 3′ flap and nHJ substrates, demonstrating the importance of this 36R linker in DNA binding and cleavage.","type":"Results"},{"text":"Taken together, we propose that the primary role of the 36R linker is to recognize the duplex portion of a substrate DNA and to stabilize the interaction between the MUS81ΔN complex and the substrate DNA, which appears to be required for efficient cleavage.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"Crystal structure of the Mus81-Eme1 complex. <i> Chang JH, Kim JJ, Choi JM, Lee JH, Cho Y. </i> Genes Dev, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2ZIW"},{"db":"PDB","id":"2ZIV"},{"db":"PDB","id":"2ZIU"},{"db":"PDB","id":"2ZIX"}],"term_name":"flexible linker","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":402,"region_id":"DP01877r006","reference_id":"18413719","start":369,"term_id":"GO:0098772","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The limited proteolytic digestion analysis suggested that residues between 368 and 403 in hEme1 are connected by a highly flexible linker, which we presumed to be a loop region","type":"Results"},{"text":"Cleavage of the 36R linker of hEme1 into two parts also significantly decreased the nuclease activity and the DNA-binding affinity of the hMUS81ΔN complex. Reducing the size of this cleaved linker of hEme1 by 10 or 26 residues abrogated the DNA-binding and nuclease activities of hMUS81ΔN on 3′ flap and nHJ substrates, demonstrating the importance of this 36R linker in DNA binding and cleavage.","type":"Results"},{"text":"Taken together, we propose that the primary role of the 36R linker is to recognize the duplex portion of a substrate DNA and to stabilize the interaction between the MUS81ΔN complex and the substrate DNA, which appears to be required for efficient cleavage.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"Crystal structure of the Mus81-Eme1 complex. <i> Chang JH, Kim JJ, Choi JM, Lee JH, Cho Y. </i> Genes Dev, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2ZIW"},{"db":"PDB","id":"2ZIV"},{"db":"PDB","id":"2ZIU"},{"db":"PDB","id":"2ZIX"}],"term_name":"molecular function regulator","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q96AY2","date":"2018-08-15T10:39:31.000Z","acc":"Q96AY2","name":"Crossover junction endonuclease EME1","length":570,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000735E6","genes":[{"name":{"value":"EME1"},"synonyms":[{"value":"MMS4"}]}],"alphafold_very_low_content":0.4017543859649123,"disorder_content":0.05964912280701754,"disprot_consensus":{"full":[{"start":369,"end":402,"type":"D"},{"start":445,"end":455,"type":"T"}],"Structural state":[{"start":369,"end":402,"type":"D"}],"Structural transition":[{"start":445,"end":455,"type":"T"}],"Molecular function":[{"start":369,"end":402,"type":"F"}],"Disorder function":[{"start":369,"end":402,"type":"F"}]}},{"features":{"pfam":[{"id":"PF10373","name":"Est1 DNA/RNA binding domain","start":197,"end":396},{"id":"PF10374","name":"Telomerase activating protein Est1","start":77,"end":188},{"id":"PF13638","name":"PIN domain","start":857,"end":939}],"gene3D":[{"start":853,"end":1016,"id":"3.40.50.1010","name":"5'-nuclease"}]},"uniref50":"UniRef50_Q9UPR3","sequence":"MSQGPPTGESSEPEAKVLHTKRLYRAVVEAVHRLDLILCNKTAYQEVFKPENISLRNKLRELCVKLMFLHPVDYGRKAEELLWRKVYYEVIQLIKTNKKHIHSRSTLECAYRTHLVAGIGFYQHLLLYIQSHYQLELQCCIDWTHVTDPLIGCKKPVSASGKEMDWAQMACHRCLVYLGDLSRYQNELAGVDTELLAERFYYQALSVAPQIGMPFNQLGTLAGSKYYNVEAMYCYLRCIQSEVSFEGAYGNLKRLYDKAAKMYHQLKKCETRKLSPGKKRCKDIKRLLVNFMYLQSLLQPKSSSVDSELTSLCQSVLEDFNLCLFYLPSSPNLSLASEDEEEYESGYAFLPDLLIFQMVIICLMCVHSLERAGSKQYSAAIAFTLALFSHLVNHVNIRLQAELEEGENPVPAFQSDGTDEPESKEPVEKEEEPDPEPPPVTPQVGEGRKSRKFSRLSCLRRRRHPPKVGDDSDLSEGFESDSSHDSARASEGSDSGSDKSLEGGGTAFDAETDSEMNSQESRSDLEDMEEEEGTRSPTLEPPRGRSEAPDSLNGPLGPSEASIASNLQAMSTQMFQTKRCFRLAPTFSNLLLQPTTNPHTSASHRPCVNGDVDKPSEPASEEGSESEGSESSGRSCRNERSIQEKLQVLMAEGLLPAVKVFLDWLRTNPDLIIVCAQSSQSLWNRLSVLLNLLPAAGELQESGLALCPEVQDLLEGCELPDLPSSLLLPEDMALRNLPPLRAAHRRFNFDTDRPLLSTLEESVVRICCIRSFGHFIARLQGSILQFNPEVGIFVSIAQSEQESLLQQAQAQFRMAQEEARRNRLMRDMAQLRLQLEVSQLEGSLQQPKAQSAMSPYLVPDTQALCHHLPVIRQLATSGRFIVIIPRTVIDGLDLLKKEHPGARDGIRYLEAEFKKGNRYIRCQKEVGKSFERHKLKRQDADAWTLYKILDSCKQLTLAQGAGEEDPSGMVTIITGLPLDNPSVLSGPMQAALQAAAHASVDIKNVLDFYKQWKEIG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UPR3","disprot_id":"DP01878","ncbi_taxon_id":9606,"regions_counter":1,"creator":"lalvarez","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":946,"region_id":"DP01878r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structures of the PIN domains of SMG6 and SMG5 reveal a nuclease within the mRNA surveillance complex. <i> Glavan F, Behm-Ansmant I, Izaurralde E, Conti E. </i> EMBO J, 2006","statement":[{"text":"The relatively high Rfree is likely due to the significant proportion of poorly disordered residues","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"lalvarez","start":924,"term_ontology":"IDPO","curator_name":"Lucía Álvarez","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-1437-5773","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2HWY"}],"reference_id":"17053788","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9UPR3","date":"2018-08-15T11:02:24.000Z","acc":"Q9UPR3","name":"Protein SMG5","length":1016,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000052A51B","genes":[{"name":{"value":"SMG5","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:24644","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:24644"}}]},"synonyms":[{"value":"EST1B","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:24644","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:24644"}}]},{"value":"KIAA1089","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:24644","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:24644"}}]}]}],"alphafold_very_low_content":0.24606299212598426,"disorder_content":0.022637795275590553,"disprot_consensus":{"full":[{"start":924,"end":946,"type":"D"}],"Structural state":[{"start":924,"end":946,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00638","name":"RanBP1 domain","start":350,"end":463},{"id":"PF08911","name":"NUP50 (Nucleoporin 50 kDa)","start":2,"end":64}],"gene3D":[{"start":278,"end":463,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"}]},"uniref50":"UniRef50_Q9JIH2","sequence":"MAKRVAEKELTDRNWDEEDEVEEMGTFSVASEEVMKNRAVKKAKRRNVGFESDSGGAFKGFKGLVVPSGGGGFSGFGGSGGKPLEGLTNGNSTDNATPFSNVKTAAEPKAAFGSFAVNGPTTLVDKKISSPKCNNSNQPPSSGPASSTACPGNAYHKQLAGLNCSVRDWIVKHVNTNPLCDLTPIFKDYERYLATIEKQLENGGGSSSESQTDRATAGMEPPSLFGSTKLQQESPFSFHGNKAEDTSEKVEFTAEKKSDAAQGATSASFSFGKKIESSALGSLSSGSLTGFSFSAGSSSLFGKDAAQSKAASSLFSAKASESPAGGGSSECRDGEEEENDEPPKVVVTEVKEEDAFYSKKCKLFYKKDNEFKEKGVGTLHLKPTATQKTQLLVRADTNLGNILLNVLIAPNMPCTRTGKNNVLIVCVPNPPLDEKQPTLPATMLIRVKTSEDADELHKILLEKKDA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q9JIH2","disprot_id":"DP01879","ncbi_taxon_id":10090,"regions_counter":1,"creator":"sgovind","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":109,"region_id":"DP01879r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Nup50/Npap60 function in nuclear protein import complex disassembly and importin recycling. <i> Matsuura Y, Stewart M. </i> EMBO J, 2005","statement":[{"text":"Residues 47–109 of Nup50 were not visible and were probably disordered in the crystal, possibly because this region of Nup50 is rich in glycine.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"sgovind","start":47,"term_ontology":"IDPO","curator_name":"Sudha Govindarajan","reference_id":"16222336","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2C1M"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9JIH2","date":"2018-08-15T11:11:03.000Z","acc":"Q9JIH2","name":"Nuclear pore complex protein Nup50","length":466,"organism":"Mus musculus","dataset":[],"UniParc":"UPI000002852B","genes":[{"name":{"value":"Nup50"},"synonyms":[{"value":"Npap60"}]}],"alphafold_very_low_content":0.4742489270386266,"disorder_content":0.1351931330472103,"disprot_consensus":{"full":[{"start":47,"end":109,"type":"D"}],"Structural state":[{"start":47,"end":109,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00989","name":"PAS fold","start":119,"end":175},{"id":"PF07469","name":"Nuclear receptor coactivator, DUF1518","start":1281,"end":1338},{"id":"PF08815","name":"Nuclear receptor coactivator","start":1071,"end":1117},{"id":"PF08832","name":"Steroid receptor coactivator","start":636,"end":709},{"id":"PF14598","name":"PAS domain","start":268,"end":378},{"id":"PF16279","name":"Domain of unknown function (DUF4927)","start":731,"end":816},{"id":"PF16665","name":"Unstructured region on nuclear receptor coactivator protein","start":463,"end":586},{"id":"PF23172","name":"Nuclear receptor coactivators bHLH domain","start":1,"end":80}],"gene3D":[{"start":34,"end":123,"id":"4.10.280.10","name":"Helix-loop-helix DNA-binding domain"},{"start":263,"end":376,"id":"3.30.450.20","name":"PAS domain"},{"start":124,"end":257,"id":"3.30.450.20","name":"PAS domain"}]},"uniref50":"UniRef50_Q9WUI9","sequence":"MSGMGENTSDPSRAETRKRKECPDQLGPSPKRNTEKRNREQENKYIEELAELIFANFNDIDNFNFKPDKCAILKETVKQIRQIKEQEKAAAANIDEVQKSDVSSTGQGVIDKDALGPMMLEALDGFFFVVNLEGNVVFVSENVTQYLRYNQEELMNKSVYSILHVGDHTEFVKNLLPKSIVNGGSWSGEPPRRNSHTFNCRMLVKPLPDSEEEGHDNQEAHQKYETMQCFAVSQPKSIKEEGEDLQSCLICVARRVPMKERPVLPSSESFTTRQDLQGKITSLDTSTMRAAMKPGWEDLVRRCIQKFHAQHEGESVSYAKRHHHEVLRQGLAFSQIYRFSLSDGTLVAAQTKSKLIRSQTTNEPQLVISLHMLHREQNVCVMNPDLTGQTMGKPLNPISSNSPAHQALCSGNPGQDMTLSSNINFPINGPKEQMGMPMGRFGGSGGMNHVSGMQATTPQGSNYALKMNSPSQSSPGMNPGQPTSMLSPRHRMSPGVAGSPRIPPSQFSPAGSLHSPVGVCSSTGNSHSYTNSSLNALQALSEGHGVSLGSSLASPDLKMGNLQNSPVNMNPPPLSKMGSLDSKDCFGLYGEPSEGTTGQAESSCHPGEQKETNDPNLPPAVSSERADGQSRLHDSKGQTKLLQLLTTKSDQMEPSPLASSLSDTNKDSTGSLPGSGSTHGTSLKEKHKILHRLLQDSSSPVDLAKLTAEATGKDLSQESSSTAPGSEVTIKQEPVSPKKKENALLRYLLDKDDTKDIGLPEITPKLERLDSKTDPASNTKLIAMKTEKEEMSFEPGDQPGSELDNLEEILDDLQNSQLPQLFPDTRPGAPAGSVDKQAIINDLMQLTAENSPVTPVGAQKTALRISQSTFNNPRPGQLGRLLPNQNLPLDITLQSPTGAGPFPPIRNSSPYSVIPQPGMMGNQGMIGNQGNLGNSSTGMIGNSASRPTMPSGEWAPQSSAVRVTCAATTSAMNRPVQGGMIRNPAASIPMRPSSQPGQRQTLQSQVMNIGPSELEMNMGGPQYSQQQAPPNQTAPWPESILPIDQASFASQNRQPFGSSPDDLLCPHPAAESPSDEGALLDQLYLALRNFDGLEEIDRALGIPELVSQSQAVDPEQFSSQDSNIMLEQKAPVFPQQYASQAQMAQGSYSPMQDPNFHTMGQRPSYATLRMQPRPGLRPTGLVQNQPNQLRLQLQHRLQAQQNRQPLMNQISNVSNVNLTLRPGVPTQAPINAQMLAQRQREILNQHLRQRQMHQQQQVQQRTLMMRGQGLNMTPSMVAPSGMPATMSNPRIPQANAQQFPFPPNYGISQQPDPGFTGATTPQSPLMSPRMAHTQSPMMQQSQANPAYQAPSDINGWAQGNMGGNSMFSQQSPPHFGQQANTSMYSNNMNINVSMATNTGGMSSMNQMTGQISMTSVTSVPTSGLSSMGPEQVNDPALRGGNLFPNQLPGMDMIKQEGDTTRKYC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q15596","disprot_id":"DP01880","ncbi_taxon_id":9606,"regions_counter":2,"creator":"okovacs","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":829,"region_id":"DP01880r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Synergistic Regulation of Coregulator/Nuclear Receptor Interaction by Ligand and DNA. <i> de Vera IMS, Zheng J, Novick S, Shang J, Hughes TS, Brust R, Munoz-Tello P, Gardner WJ, Marciano DP, Kong X, Griffin PR, Kojetin DJ. </i> Structure, 2017","statement":[{"text":"2D [1 H,15N]-HSQC NMR analysis of SRC-2 RID (res. 624-829), which contains three LXXLL motifs revealed very poor spectral dispersion and missing peaks which often make the analysis of disordered proteins such as SRC-2 RID problematic. Using 2D and 3D 13C-detected NMR methods, we obtained backbone chemical shift assignments for 213 of the 235 residues (91%) of tagged SRC-2 RID.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"okovacs","start":624,"term_ontology":"IDPO","curator_name":"Orsolya Panna Kovacs","reference_id":"28890360","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":829,"term_name":"protein binding","start":624,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Addition of PPARg-RXRa LBD heterodimer resulted in significant peak line broadening and disappearance of NMR peaks for residues within, flanking, and linking all three LXXLL motifs in SRC-2 RID. This indicates that all three LXXLL motifs are likely in direct contact with PPARg-RXRa.","type":"Results"}],"curator_id":"okovacs","released":"2022_03","term_ontology":"GO","curator_name":"Orsolya Panna Kovacs","reference_id":"28890360","version":3,"reference_html":"Synergistic Regulation of Coregulator/Nuclear Receptor Interaction by Ligand and DNA. <i> de Vera IMS, Zheng J, Novick S, Shang J, Hughes TS, Brust R, Munoz-Tello P, Gardner WJ, Marciano DP, Kong X, Griffin PR, Kojetin DJ. </i> Structure, 2017","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP01880r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q15596","date":"2018-08-15T11:24:19.000Z","acc":"Q15596","name":"Nuclear receptor coactivator 2","length":1464,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI0000527E90","genes":[{"name":{"value":"NCOA2"},"synonyms":[{"value":"BHLHE75"},{"value":"SRC2"},{"value":"TIF2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8670870","url":"http://www.ncbi.nlm.nih.gov/pubmed/8670870","alternativeUrl":"https://europepmc.org/abstract/MED/8670870"}}]}]}],"alphafold_very_low_content":0.7165300546448088,"disorder_content":0.1407103825136612,"disprot_consensus":{"full":[{"start":624,"end":829,"type":"D"}],"Structural state":[{"start":624,"end":829,"type":"D"}],"Molecular function":[{"start":624,"end":829,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05016","name":"ParE toxin of type II toxin-antitoxin system, parDE","start":6,"end":83}],"gene3D":[{"start":1,"end":95,"id":"3.30.2310.20","name":"RelE-like"}]},"uniref50":"UniRef50_P0C077","sequence":"MAYFLDFDERALKEWRKLGSTVREQLKKKLVEVLESPRIEANKLRGMPDCYKIKLRSSGYRLVYQVIDEKVVVFVISVGKRERSEVYSEAVKRIL","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0C077","disprot_id":"DP01881","dataset":["Unicellular toxins and antitoxins","RNA-binding proteins","Stress response proteins"],"ncbi_taxon_id":83333,"regions_counter":3,"creator":"sgovind","regions":[{"region_id":"DP01881r001","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:46:21.175Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":95,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":85,"version":3,"statement":[{"text":"Here, we present the crystal structure of the intact Escherichia coli RelB2E2 complex at 2.8 Å resolution, comprising both the RelB-inhibited RelE and the RelB dimerization domain that binds DNA.  The results thus provide a firm basis for understanding the model of conditional cooperativity at the molecular level.","type":"Abstract"},{"text":"The structure covers most of RelE (residues 2–80 of 95) and one molecule of RelB (residues 2–79 of 79), whereas the other two RelB molecules lack either the C terminus (residues 2–69) or N terminus (residues 33–79) due to poor electron density (Figure 1A). The flexible, C-terminal helix of RelE (helix α3, residues 85–95) is disordered in all molecules in this crystal form","type":"Results"}],"term_name":"disorder","reference_html":"The crystal structure of the intact E. coli RelBE toxin-antitoxin complex provides the structural basis for conditional cooperativity. <i> Bøggild A, Sofos N, Andersen KR, Feddersen A, Easter AD, Passmore LA, Brodersen DE. </i> Structure, 2012","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"22981948","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4FXE"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lchemes","curator_orcid":"0000-0003-0192-9906","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP01881r002","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:46:22.593Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":95,"term_id":"IDPO:0000011","start":81,"version":2,"statement":[{"text":"In the free RelE(R81A/R83A) structure, helix alpha4 at the C terminus adopts a closed conformation contacting with the beta-sheet core and adjacent loops. In the RelE(R81A/R83A)-RelB(C) complex, helix alpha3(*) of RelB(C) displaces alpha4 of RelE(R81A/R83A) from the binding site on the beta-sheet core. This helix replacement results in neutralization of a conserved positively charged cluster of RelE by acidic residues from alpha3(*) of RelB. The released helix alpha4 becomes unfolded, adopting an open conformation with increased mobility\n\nOur structures indicate that RelB counteracts the toxic activity of RelE by displacing alpha4 helix from the catalytically competent position found in the free RelE structure.\n","type":"Abstract"},{"text":"On the other hand, the chemical shift index analysis of RelER81A/R83A revealed an unfolding of a C-terminal helix (α4) coupled with RelBC binding (supplemental Fig. S3, C and D)\nthe C-terminal tail (Ala81-Leu95) in cyan [...] Comparison of RelBC-bound RelER81A/R83A to the unbound structure reveals a pronounced conformational change of α4 and adjacent loops (loop α3-β2 and β4-α4). The α4 swings out from the surface of the central β-sheet as it is displaced by the amphipathic helix α3* from RelBC in the complex (Figs. (Figs.33 and and4).4). The large chemical shift perturbation in the C-terminal tail region of RelER81A/R83A by RelBC is because of a conformational change rather than direct interaction (Fig. 2, A and C, and supplemental Fig. S4, A and B). The released α4 becomes unfolded, as evidenced by the chemical shift index analysis results (supplemental Fig. S3, C and D).[...] Upon binding of RelBC, RelER81A/R83A displays large changes in both the hetNOE and R2 values, especially around the C-terminal helix α4 region. A dramatic reduction in hetNOE and R2 values within the α4 region is observed, indicating an increase in the mobility of this region (supplemental Fig. S5, B and D).\n","type":"Results"}],"term_name":"disorder to order","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"19297318","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2KC9"}],"term_namespace":"Structural transition","ec_id":"ECO:0006165","curator_id":"lchemes","reference_html":"Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module involves a helix displacement near an mRNA interferase active site. <i> Li GY, Zhang Y, Inouye M, Ikura M. </i> J Biol Chem, 2009","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP01881r003","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:46:23.539Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":95,"term_id":"GO:0097351","start":81,"version":3,"statement":[{"text":"In the free RelE(R81A/R83A) structure, helix alpha4 at the C terminus adopts a closed conformation contacting with the beta-sheet core and adjacent loops. In the RelE(R81A/R83A)-RelB(C) complex, helix alpha3(*) of RelB(C) displaces alpha4 of RelE(R81A/R83A) from the binding site on the beta-sheet core. This helix replacement results in neutralization of a conserved positively charged cluster of RelE by acidic residues from alpha3(*) of RelB. The released helix alpha4 becomes unfolded, adopting an open conformation with increased mobility\n\nOur structures indicate that RelB counteracts the toxic activity of RelE by displacing alpha4 helix from the catalytically competent position found in the free RelE structure.\n","type":"Abstract"},{"text":"\nThe perturbation of the proper arrangement of critical residues at an active site seems to be a common theme for the inactivation mechanism of RelE/ParE superfamily TA systems.  Our structural studies provide evidence that RelB antitoxin directly inhibits RelE toxin through binding to the active site, although the formation of a RelE2-RelB2 complex mediated through the N-terminal dimerization domain of RelB (16) may also spatially block RelE from entering the ribosomal A-site where the RNA cleavage takes place","type":"Discussion"}],"term_name":"toxin sequestering activity","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"19297318","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2KC9"},{"db":"PDB","id":"2KC8"}],"term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"lchemes","reference_html":"Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module involves a helix displacement near an mRNA interferase active site. <i> Li GY, Zhang Y, Inouye M, Ikura M. </i> J Biol Chem, 2009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a toxic protein, disabling its function. There may be more than one antitoxin to a toxic protein. Instances of this activity are known only in prokaryotes, where the toxic protein may be a ribonuclease, a DNA gyrase, or other.\" [GOC:rs, PMID:19143615, PMID:19325885, PMID:21819231, PMID:22545240, PMID:24806488, Wikipedia:Toxin-antitoxin_system#Type_II]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P0C077","date":"2018-08-15T11:29:23.000Z","acc":"P0C077","name":"mRNA interferase toxin RelE","length":95,"organism":"Escherichia coli (strain K12)","UniParc":"UPI0000133667","genes":[{"name":{"value":"relE"},"olnNames":[{"value":"b1563"},{"value":"JW1555"}]}],"alphafold_very_low_content":0,"disorder_content":0.11578947368421053,"disprot_consensus":{"full":[{"start":81,"end":95,"type":"T"}],"Structural state":[{"start":85,"end":95,"type":"D"}],"Structural transition":[{"start":81,"end":95,"type":"T"}],"Molecular function":[{"start":81,"end":95,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05355","name":"Apolipoprotein C-II","start":24,"end":100}],"gene3D":[{"start":23,"end":101,"id":"1.10.1440.10","name":"Apolipoprotein C-II"}]},"uniref50":"UniRef50_P02655","sequence":"MGTRLLPALFLVLLVLGFEVQGTQQPQQDEMPSPTFLTQVKESLSSYWESAKTAAQNLYEKTYLPAVDEKLRDLYSKSTAAMSTYTGIFTDQVLSVLKGEE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P02655","disprot_id":"DP01883","ncbi_taxon_id":9606,"regions_counter":2,"creator":"sgovind","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":65,"region_id":"DP01883r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The structure and interactions of human apolipoprotein C-II in dodecyl phosphocholine. <i> MacRaild CA, Howlett GJ, Gooley PR. </i> Biochemistry, 2004","statement":[{"text":"The central region, comprising residues 40−65, is substantially disordered despite having a significant role in the activation of LpL.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"sgovind","start":40,"term_ontology":"IDPO","curator_name":"Sudha Govindarajan","reference_id":"15209504","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1SOH"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":65,"term_name":"molecular function activator activity","start":40,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"The central region, comprising residues 40−65, is substantially disordered despite having a significant role in the activation of LpL","type":"Results"}],"curator_id":"sgovind","released":"2022_03","term_ontology":"GO","curator_name":"Sudha Govindarajan","reference_id":"15209504","version":3,"reference_html":"The structure and interactions of human apolipoprotein C-II in dodecyl phosphocholine. <i> MacRaild CA, Howlett GJ, Gooley PR. </i> Biochemistry, 2004","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0140677","ec_id":"ECO:0006165","region_id":"DP01883r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P02655","date":"2018-08-15T12:24:34.000Z","acc":"P02655","name":"Apolipoprotein C-II","length":101,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000125C21","genes":[{"name":{"value":"APOC2"},"synonyms":[{"value":"APC2"}]}],"alphafold_very_low_content":0.10891089108910891,"disorder_content":0.25742574257425743,"disprot_consensus":{"full":[{"start":40,"end":65,"type":"D"}],"Structural state":[{"start":40,"end":65,"type":"D"}],"Molecular function":[{"start":40,"end":65,"type":"F"}]}},{"features":{"pfam":[{"id":"PF12937","name":"F-box-like","start":60,"end":104}],"gene3D":[{"start":57,"end":148,"id":"1.20.1280.50","name":"1.20.1280.50"},{"start":177,"end":381,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_Q9UKT5","sequence":"MAGSEPRSGTNSPPPPFSDWGRLEAAILSGWKTFWQSVSKERVARTTSREEVDEAASTLTRLPIDVQLYILSFLSPHDLCQLGSTNHYWNETVRDPILWRYFLLRDLPSWSSVDWKSLPDLEILKKPISEVTDGAFFDYMAVYRMCCPYTRRASKSSRPMYGAVTSFLHSLIIQNEPRFAMFGPGLEELNTSLVLSLMSSEELCPTAGLPQRQIDGIGSGVNFQLNNQHKFNILILYSTTRKERDRAREEHTSAVNKMFSRHNEGDDQQGSRYSVIPQIQKVCEVVDGFIYVANAEAHKRHEWQDEFSHIMAMTDPAFGSSGRPLLVLSCISQGDVKRMPCFYLAHELHLNLLNHPWLVQDTEAETLTGFLNGIEWILEEVESKRAR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9UKT5","disprot_id":"DP01884","ncbi_taxon_id":9606,"regions_counter":1,"creator":"lalvarez","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":271,"region_id":"DP01884r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis of dimerization-dependent ubiquitination by the SCF(Fbx4) ubiquitin ligase. <i> Li Y, Hao B. </i> J Biol Chem, 2010","statement":[{"text":"In the refined model, residues 161–163 of Skp1 and residues 132–135, 242–271, and 384–387 of Fbx4core were not visible in the electron density maps and are likely to be disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ahatos","start":242,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3L2O"}],"reference_id":"20181953","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9UKT5","date":"2018-08-15T13:17:13.000Z","acc":"Q9UKT5","name":"F-box only protein 4","length":387,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012A584","genes":[{"name":{"value":"FBXO4"},"synonyms":[{"value":"FBX4"}]}],"alphafold_very_low_content":0.11627906976744186,"disorder_content":0.07751937984496124,"disprot_consensus":{"full":[{"start":242,"end":271,"type":"D"}],"Structural state":[{"start":242,"end":271,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00014","name":"Kunitz/Bovine pancreatic trypsin inhibitor domain","start":290,"end":341},{"id":"PF02177","name":"Amyloid A4 N-terminal heparin-binding","start":31,"end":131},{"id":"PF03494","name":"Beta-amyloid peptide (beta-APP)","start":679,"end":713},{"id":"PF10515","name":"Beta-amyloid precursor protein C-terminus","start":716,"end":766},{"id":"PF12924","name":"Copper-binding of amyloid precursor, CuBD","start":132,"end":188},{"id":"PF12925","name":"E2 domain of amyloid precursor protein","start":367,"end":548}],"gene3D":[{"start":17,"end":123,"id":"3.90.570.10","name":"Amyloidogenic glycoprotein, heparin-binding domain"},{"start":672,"end":711,"id":"4.10.230.10","name":"Amyloidogenic glycoprotein, amyloid-beta peptide"},{"start":131,"end":189,"id":"3.30.1490.140","name":"Amyloidogenic glycoprotein, copper-binding domain"},{"start":363,"end":580,"id":"1.20.120.770","name":"Amyloid precursor protein, E2 domain"},{"start":278,"end":354,"id":"4.10.410.10","name":"Pancreatic trypsin inhibitor Kunitz domain"},{"start":742,"end":770,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"}]},"uniref50":"UniRef50_P05067","sequence":"MLPSLALLLLAAWTVRALEVPTDGNAGLLAEPQIAMFCGKLNMHMNVQNGKWESDPSGTKTCIGTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHTHIVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDSIDSADAEEDDSDVWWGGADTDYADGGEDKVVEVAEEEEVADVEEEEAEDDEDVEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSVSSQSLLKTTSEPLPQDPVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPHHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHPFGVDSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFGHDSGFEVRHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_P05067","disprot_id":"DP01887","ncbi_taxon_id":10116,"regions_counter":2,"creator":"nfoutel","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":687,"region_id":"DP01887r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"NMR solution structure of rat aβ(1-16): toward understanding the mechanism of rats' resistance to Alzheimer's disease. <i> Istrate AN, Tsvetkov PO, Mantsyzov AB, Kulikova AA, Kozin SA, Makarov AA, Polshakov VI. </i> Biophys J, 2012","statement":[{"text":"After performing NMR experiments, the authors found nor the free nor the bound to Zn(+2) A-b peptides (1-16) (from the Amyloid beta-A4 region 672 to 687) have a regular structure but a serie of bend, coil and turn regions without regular secondary structure. In addition, they described a relatively fast (in NMR timescale) exchange between several conformational states, typical from an unstructured peptides/proteins.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":672,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"22225807","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":687,"term_name":"zinc ion binding","start":672,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"The NMR spectra of free rat Ab(1–16) contain sharp signals typical of small monomeric peptides, but they become broader upon addition of Zn(2+). The observed changes in the spectra indicate the formation of a complex of rat Ab(1–16) with Zn(2+) ions.","type":"Results"}],"curator_id":"nfoutel","released":"2022_03","term_ontology":"GO","curator_name":"Nicolas Foutel","reference_id":"22225807","version":3,"reference_html":"NMR solution structure of rat aβ(1-16): toward understanding the mechanism of rats' resistance to Alzheimer's disease. <i> Istrate AN, Tsvetkov PO, Mantsyzov AB, Kulikova AA, Kozin SA, Makarov AA, Polshakov VI. </i> Biophys J, 2012","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008270","ec_id":"ECO:0006165","region_id":"DP01887r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P08592","date":"2018-08-15T13:51:10.000Z","acc":"P08592","name":"Amyloid-beta A4 protein","length":770,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI000002A2FB","genes":[{"name":{"value":"App","evidences":[{"code":"ECO:0000312","source":{"name":"RGD","id":"2139","url":"https://rgd.mcw.edu/tools/genes/genes_view.cgi?id=2139"}}]},"synonyms":[{"value":"A4","evidences":[{"code":"ECO:0000250","source":{"name":"UniProtKB","id":"P05067","url":"https://www.uniprot.org/uniprot/P05067"}}]},{"value":"AD1","evidences":[{"code":"ECO:0000250","source":{"name":"UniProtKB","id":"P05067","url":"https://www.uniprot.org/uniprot/P05067"}}]}]}],"alphafold_very_low_content":0.35974025974025975,"disorder_content":0.02077922077922078,"disprot_consensus":{"full":[{"start":672,"end":687,"type":"D"}],"Structural state":[{"start":672,"end":687,"type":"D"}],"Molecular function":[{"start":672,"end":687,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00498","name":"FHA domain","start":126,"end":188}],"gene3D":[{"start":47,"end":204,"id":"2.60.200.20","name":"2.60.200.20"}]},"uniref50":"UniRef50_Q07930","sequence":"MFHRRKRPYNTRNYGHDDKKFKSQYIDIMPDFSPSGLLELESNNKEGIALKHVEPQDAISPDNYMDMLGLEARDRTMYELVIYRKNDKDKGPWKRYDLNGRSCYLVGRELGHSLDTDLDDRTEIVVADIGIPEETSSKQHCVIQFRNVRGILKCYVMDLDSSNGTCLNNVVIPGARYIELRSGDVLTLSEFEEDNDYELIFMNV","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q07930","disprot_id":"DP01890","ncbi_taxon_id":559292,"regions_counter":5,"creator":"nfoutel","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":51,"region_id":"DP01890r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the Pml1p subunit of the yeast precursor mRNA retention and splicing complex. <i> Trowitzsch S, Weber G, Lührmann R, Wahl MC. </i> J Mol Biol, 2009","statement":[{"text":"Apart from a long, flexible loop (residues 112–121), amino acids 52–204 could be modeled unequivocally\ninto the electron density map of full-length Pml1p. The remaining N-terminal part (residues1–51) could not be traced (...). This finding confirmed the results of our biochemical analyses, suggesting that the first 51 residues of Pml1p are unstructured in the isolated protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":1,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"19010333","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":121,"region_id":"DP01890r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the Pml1p subunit of the yeast precursor mRNA retention and splicing complex. <i> Trowitzsch S, Weber G, Lührmann R, Wahl MC. </i> J Mol Biol, 2009","statement":[{"text":"Apart from a long, flexible loop (residues 112–121), amino acids 52–204 could be modeled unequivocally\ninto the electron density map of full-length Pml1p. The remaining N-terminal part (residues1–51) could not be traced (...). This finding confirmed the results of our biochemical analyses, suggesting that the first 51 residues of Pml1p are unstructured in the isolated protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":112,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"19010333","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":42,"region_id":"DP01890r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. <i> Wysoczański P, Schneider C, Xiang S, Munari F, Trowitzsch S, Wahl MC, Lührmann R, Becker S, Zweckstetter M. </i> Nat Struct Mol Biol, 2014","statement":[{"text":"NMR secondary chemical shifts for the free Pml1p (22-42)  clearly evidenced a disordered structure -no secondary structure tendency-.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":22,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"25218446","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":42,"term_name":"protein binding","start":22,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"nfoutel","released":"2022_03","term_ontology":"GO","curator_name":"Nicolas Foutel","reference_id":"25218446","version":3,"reference_html":"Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex. <i> Wysoczański P, Schneider C, Xiang S, Munari F, Trowitzsch S, Wahl MC, Lührmann R, Becker S, Zweckstetter M. </i> Nat Struct Mol Biol, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP01890r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":61,"region_id":"DP01890r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"An unusual RNA recognition motif acts as a scaffold for multiple proteins in the pre-mRNA retention and splicing complex. <i> Trowitzsch S, Weber G, Lührmann R, Wahl MC. </i> J Biol Chem, 2008","statement":[{"text":"Equilibrium CD spectra of Pml1p-(1– 61) were consistent with a random coil structure in this part of the protein (Fig. 3B). Thus, an intrinsically unstructured portion at the N terminus of Pml1p (residues 1– 61) is sufficient for interaction with Snu17p, reminiscent of the situation in Bud13p.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"nfoutel","start":1,"term_ontology":"IDPO","curator_name":"Nicolas Foutel","reference_id":"18809678","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q07930","date":"2018-08-15T13:53:04.000Z","acc":"Q07930","name":"Pre-mRNA leakage protein 1","length":204,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000013B7A1","genes":[{"name":{"value":"PML1"},"orfNames":[{"value":"L1591"}],"olnNames":[{"value":"YLR016C"}]}],"alphafold_very_low_content":0.049019607843137254,"disorder_content":0.3480392156862745,"disprot_consensus":{"full":[{"start":1,"end":61,"type":"D"},{"start":112,"end":121,"type":"D"}],"Structural state":[{"start":1,"end":61,"type":"D"},{"start":112,"end":121,"type":"D"}],"Molecular function":[{"start":22,"end":42,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00397","name":"WW domain","start":137,"end":162},{"id":"PF00397","name":"WW domain","start":434,"end":460},{"id":"PF01846","name":"FF domain","start":662,"end":709},{"id":"PF01846","name":"FF domain","start":727,"end":776},{"id":"PF01846","name":"FF domain","start":794,"end":843},{"id":"PF01846","name":"FF domain","start":898,"end":949},{"id":"PF01846","name":"FF domain","start":956,"end":1007},{"id":"PF01846","name":"FF domain","start":1015,"end":1071},{"id":"PF23517","name":"TCERG1 WW domain","start":521,"end":574}],"gene3D":[{"start":723,"end":780,"id":"1.10.10.440","name":"FF domain"},{"start":654,"end":722,"id":"1.10.10.440","name":"FF domain"},{"start":958,"end":1014,"id":"1.10.10.440","name":"FF domain"},{"start":1015,"end":1081,"id":"1.10.10.440","name":"FF domain"},{"start":781,"end":858,"id":"1.10.10.440","name":"FF domain"},{"start":881,"end":957,"id":"1.10.10.440","name":"FF domain"},{"start":133,"end":165,"id":"2.20.70.10","name":"2.20.70.10"},{"start":513,"end":583,"id":"2.20.70.10","name":"2.20.70.10"},{"start":419,"end":484,"id":"2.20.70.10","name":"2.20.70.10"}]},"uniref50":"UniRef50_O14776","sequence":"MAERGGDGGESERFNPGELRMAQQQALRFRGPAPPPNAVMRGPPPLMRPPPPFGMMRGPPPPPRPPFGRPPFDPNMPPMPPPGGIPPPMGPPHLQRPPFMPPPMSSMPPPPGMMFPPGMPPVTAPGTPALPPTEEIWVENKTPDGKVYYYNARTRESAWTKPDGVKVIQQSELTPMLAAQAQVQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQVQAQVQAQVQAQAVGASTPTTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPTATPVQTVPQPHPQTLPPAVPHSVPQPTTAIPAFPPVMVPPFRVPLPGMPIPLPGVAMMQIVSCPYVKTVATTKTGVLPGMAPPIVPMIHPQVAIAASPATLAGATAVSEWTEYKTADGKTYYYNNRTLESTWEKPQELKEKEKLEEKIKEPIKEPSEEPLPMETEEEDPKEEPIKEIKEEPKEEEMTEEEKAAQKAKPVATAPIPGTPWCVVWTGDERVFFYNPTTRLSMWDRPDDLIGRADVDKIIQEPPHKKGMEELKKLRHPTPTMLSIQKWQFSMSAIKEEQELMEEINEDEPVKAKKRKRDDNKDIDSEKEAAMEAEIKAARERAIVPLEARMKQFKDMLLERGVSAFSTWEKELHKIVFDPRYLLLNPKERKQVFDQYVKTRAEEERREKKNKIMQAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAARKKEKEDSKTRGEKIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEKIAKNLDSEKEKELERQARIEASLREREREVQKARSEQTKEIDREREQHKREEAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWESGSLLEREEKEKLFNEHIEALTKKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCIKFSSSDRKKQREFEEYIRDKYITAKADFRTLLKETKFITYRSKKLIQESDQHLKDVEKILQNDKRYLVLDCVPEERRKLIVAYVDDLDRRGPPPPPTASEPTRRSTK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O14776","disprot_id":"DP01893","ncbi_taxon_id":9606,"regions_counter":3,"creator":"cbassot","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":108,"region_id":"DP01893r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"From crystal packing to molecular recognition: prediction and discovery of a binding site on the surface of polo-like kinase 1. <i> Śledź P, Stubbs CJ, Lang S, Yang YQ, McKenzie GJ, Venkitaraman AR, Hyvönen M, Abell C. </i> Angew Chem Int Ed Engl, 2011","term_id":"IDPO:0000002","curator_id":"ahatos","start":98,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3Q1I"}],"reference_id":"21472932","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":108,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"From crystal packing to molecular recognition: prediction and discovery of a binding site on the surface of polo-like kinase 1. <i> Śledź P, Stubbs CJ, Lang S, Yang YQ, McKenzie GJ, Venkitaraman AR, Hyvönen M, Abell C. </i> Angew Chem Int Ed Engl, 2011","term_id":"GO:0005515","curator_id":"ahatos","start":98,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"21472932","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01893r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":108,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"From crystal packing to molecular recognition: prediction and discovery of a binding site on the surface of polo-like kinase 1. <i> Śledź P, Stubbs CJ, Lang S, Yang YQ, McKenzie GJ, Venkitaraman AR, Hyvönen M, Abell C. </i> Angew Chem Int Ed Engl, 2011","term_id":"IDPO:0000011","curator_id":"ahatos","start":98,"term_ontology":"IDPO","curator_name":"András Hatos","reference_id":"21472932","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01893r003","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_O14776","date":"2018-08-15T14:06:07.000Z","acc":"O14776","name":"Transcription elongation regulator 1","length":1098,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000072769","genes":[{"name":{"value":"TCERG1"},"synonyms":[{"value":"CA150"},{"value":"TAF2S"}]}],"alphafold_very_low_content":0.33788706739526414,"disorder_content":0.010018214936247723,"disprot_consensus":{"full":[{"start":98,"end":108,"type":"T"}],"Structural state":[{"start":98,"end":108,"type":"D"}],"Molecular function":[{"start":98,"end":108,"type":"F"}],"Structural transition":[{"start":98,"end":108,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00439","name":"Bromodomain","start":70,"end":151},{"id":"PF00439","name":"Bromodomain","start":357,"end":444},{"id":"PF17035","name":"Bromodomain extra-terminal - transcription regulation","start":609,"end":672},{"id":"PF17105","name":"C-terminal domain of bromodomain protein 4","start":1319,"end":1362}],"gene3D":[{"start":345,"end":463,"id":"1.20.920.10","name":"Bromodomain-like"},{"start":602,"end":682,"id":"1.20.1270.220","name":"1.20.1270.220"},{"start":34,"end":181,"id":"1.20.920.10","name":"Bromodomain-like"}]},"uniref50":"UniRef50_O60885","sequence":"MSAESGPGTRLRNLPVMGDGLETSQMSTTQAQAQPQPANAASTNPPPPETSNPNKPKRQTNQLQYLLRVVLKTLWKHQFAWPFQQPVDAVKLNLPDYYKIIKTPMDMGTIKKRLENNYYWNAQECIQDFNTMFTNCYIYNKPGDDIVLMAEALEKLFLQKINELPTEETEIMIVQAKGRGRGRKETGTAKPGVSTVPNTTQASTPPQTQTPQPNPPPVQATPHPFPAVTPDLIVQTPVMTVVPPQPLQTPPPVPPQPQPPPAPAPQPVQSHPPIIAATPQPVKTKKGVKRKADTTTPTTIDPIHEPPSLPPEPKTTKLGQRRESSRPVKPPKKDVPDSQQHPAPEKSSKVSEQLKCCSGILKEMFAKKHAAYAWPFYKPVDVEALGLHDYCDIIKHPMDMSTIKSKLEAREYRDAQEFGADVRLMFSNCYKYNPPDHEVVAMARKLQDVFEMRFAKMPDEPEEPVVAVSSPAVPPPTKVVAPPSSSDSSSDSSSDSDSSTDDSEEERAQRLAELQEQLKAVHEQLAALSQPQQNKPKKKEKDKKEKKKEKHKRKEEVEENKKSKAKEPPPKKTKKNNSSNSNVSKKEPAPMKSKPPPTYESEEEDKCKPMSYEEKRQLSLDINKLPGEKLGRVVHIIQSREPSLKNSNPDEIEIDFETLKPSTLRELERYVTSCLRKKRKPQAEKVDVIAGSSKMKGFSSSESESSSESSSSDSEDSETEMAPKSKKKGHPGREQKKHHHHHHQQMQQAPAPVPQQPPPPPQQPPPPPPPQQQQQPPPPPPPPSMPQQAAPAMKSSPPPFIATQVPVLEPQLPGSVFDPIGHFTQPILHLPQPELPPHLPQPPEHSTPPHLNQHAVVSPPALHNALPQQPSRPSNRAAALPPKPARPPAVSPALTQTPLLPQPPMAQPPQVLLEDEEPPAPPLTSMQMQLYLQQLQKVQPPTPLLPSVKVQSQPPPPLPPPPHPSVQQQLQQQPPPPPPPQPQPPPQQQHQPPPRPVHLQPMQFSTHIQQPPPPQGQQPPHPPPGQQPPPPQPAKPQQVIQHHHSPRHHKSDPYSTGHLREAPSPLMIHSPQMSQFQSLTHQSPPQQNVQPKKQELRAASVVQPQPLVVVKEEKIHSPIIRSEPFSPSLRPEPPKHPESIKAPVHLPQRPEMKPVDVGRPVIRPPEQNAPPPGAPDKDKQKQEPKTPVAPKKDLKIKNMGSWASLVQKHPTTPSSTAKSSSDSFEQFRRAAREKEEREKALKAQAEHAEKEKERLRQERMRSREDEDALEQARRAHEEARRRQEQQQQQRQEQQQQQQQQAAAVAAAATPQAQSSQPQSMLDQQRELARKREQERRRREAMAATIDMNFQSDLLSIFEENLF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O60885","disprot_id":"DP01898","ncbi_taxon_id":9606,"regions_counter":3,"creator":"cbassot","regions":[{"start":333,"end":349,"reference_id":"22464331","reference_source":"pmid","reference_html":"Histone recognition and large-scale structural analysis of the human bromodomain family. <i> Filippakopoulos P, Picaud S, Mangos M, Keates T, Lambert JP, Barsyte-Lovejoy D, Felletar I, Volkmer R, Müller S, Pawson T, Gingras AC, Arrowsmith CH, Knapp S. </i> Cell, 2012","date":"2022-10-11T12:26:42.117Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"2OUO"}],"region_id":"DP01898r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":"ethylene glycol"}],"statement":[{"text":"The amminoacid residues, 333-349, are missing in the crystallized structure, as is known from the PDB.\n\n","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-26T12:56:25.007Z"}}],"released":"2018_11","uniref100":"UniRef100_O60885","date":"2018-08-15T14:32:26.000Z","acc":"O60885","name":"Bromodomain-containing protein 4","length":1362,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins","Condensates-related proteins"],"UniParc":"UPI0000160C9C","genes":[{"name":{"value":"BRD4"},"synonyms":[{"value":"HUNK1"}]}],"alphafold_very_low_content":0.617474302496329,"disorder_content":0.012481644640234948,"disprot_consensus":{"full":[{"start":333,"end":349,"type":"D"}],"Structural state":[{"start":333,"end":349,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00605","name":"Interferon regulatory factor transcription factor","start":16,"end":121},{"id":"PF10401","name":"Interferon-regulatory factor 3","start":248,"end":431}],"gene3D":[{"start":10,"end":122,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"start":232,"end":433,"id":"2.60.200.10","name":"2.60.200.10"}]},"uniref50":"UniRef50_Q13568","sequence":"MNQSIPVAPTPPRRVRLKPWLVAQVNSCQYPGLQWVNGEKKLFCIPWRHATRHGPSQDGDNTIFKAWAKETGKYTEGVDEADPAKWKANLRCALNKSRDFRLIYDGPRDMPPQPYKIYEVCSNGPAPTDSQPPEDYSFGAGEEEEEEEELQRMLPSLSLTEDVKWPPTLQPPTLRPPTLQPPTLQPPVVLGPPAPDPSPLAPPPGNPAGFRELLSEVLEPGPLPASLPPAGEQLLPDLLISPHMLPLTDLEIKFQYRGRPPRALTISNPHGCRLFYSQLEATQEQVELFGPISLEQVRFPSPEDIPSDKQRFYTNQLLDVLDRGLILQLQGQDLYAIRLCQCKVFWSGPCASAHDSCPNPIQREVKTKLFSLEHFLNELILFQKGQTNTPPPFEIFFCFGEEWPDRKPREKKLITVQVVPVAARLLLEMFSGELSWSADSIRLQISNPDLKDRMVEQFKELHHIWQSQQRLQPVAQAPPGAGLGVGQGPWPMHPAGMQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q13568","disprot_id":"DP01907","ncbi_taxon_id":9606,"regions_counter":1,"creator":"lalvarez","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":467,"region_id":"DP01907r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Insights into interferon regulatory factor activation from the crystal structure of dimeric IRF5. <i> Chen W, Lam SS, Srinath H, Jiang Z, Correia JJ, Schiffer CA, Fitzgerald KA, Lin K, Royer WE. </i> Nat Struct Mol Biol, 2008","statement":[{"text":"Residues 458–467 were not visible in the electron density maps and are not included in the refined model","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"lalvarez","start":458,"term_ontology":"IDPO","curator_name":"Lucía Álvarez","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-1437-5773","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3DSH"}],"reference_id":"18836453","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q13568","date":"2018-08-15T15:02:38.000Z","acc":"Q13568","name":"Interferon regulatory factor 5","length":498,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000167B29","genes":[{"name":{"value":"IRF5","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11303025","url":"http://www.ncbi.nlm.nih.gov/pubmed/11303025","alternativeUrl":"https://europepmc.org/abstract/MED/11303025"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6120","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6120"}}]}}],"alphafold_very_low_content":0.30522088353413657,"disorder_content":0.020080321285140562,"disprot_consensus":{"full":[{"start":458,"end":467,"type":"D"}],"Structural state":[{"start":458,"end":467,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00104","name":"Ligand-binding domain of nuclear hormone receptor","start":298,"end":469},{"id":"PF00105","name":"Double treble clef zinc finger, C4 type","start":136,"end":202}],"gene3D":[{"start":255,"end":486,"id":"1.10.565.10","name":"Retinoid X Receptor"},{"start":130,"end":210,"id":"3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A"}]},"uniref50":"UniRef50_Q96RI1","sequence":"MVMQFQGLENPIQISPHCSCTPSGFFMEMMSMKPAKGVLTEQVAGPLGQNLEVEPYSQYSNVQFPQVQPQISSSSYYSNLGFYPQQPEEWYSPGIYELRRMPAETLYQGETEVAEMPVTKKPRMGASAGRIKGDELCVVCGDRASGYHYNALTCEGCKGFFRRSITKNAVYKCKNGGNCVMDMYMRRKCQECRLRKCKEMGMLAECMYTGLLTEIQCKSKRLRKNVKQHADQTVNEDSEGRDLRQVTSTTKSCREKTELTPDQQTLLHFIMDSYNKQRMPQEITNKILKEEFSAEENFLILTEMATNHVQVLVEFTKKLPGFQTLDHEDQIALLKGSAVEAMFLRSAEIFNKKLPSGHSDLLEERIRNSGISDEYITPMFSFYKSIGELKMTQEEYALLTAIVILSPDRQYIKDREAVEKLQEPLLDVLQKLCKIHQPENPQHFACLLGRLTELRTFNHHHAEMLMSWRVNDHKFTPLLCEIWDVQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q96RI1","disprot_id":"DP01914","ncbi_taxon_id":9606,"regions_counter":1,"creator":"lalvarez","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":290,"region_id":"DP01914r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"A chemical, genetic, and structural analysis of the nuclear bile acid receptor FXR. <i> Downes M, Verdecia MA, Roecker AJ, Hughes R, Hogenesch JB, Kast-Woelbern HR, Bowman ME, Ferrer JL, Anisfeld AM, Edwards PA, Rosenfeld JM, Alvarez JG, Noel JP, Nicolaou KC, Evans RM. </i> Mol Cell, 2003","statement":[{"text":"the 15 residue insertion region between helices 1 and 3 is completely disordered in the FXR crystal structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"lalvarez","start":275,"term_ontology":"IDPO","curator_name":"Lucía Álvarez","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-1437-5773","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1OSH"}],"reference_id":"12718892","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q96RI1","date":"2018-08-15T15:39:21.000Z","acc":"Q96RI1","name":"Bile acid receptor","length":486,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000006E701","genes":[{"name":{"value":"NR1H4"},"synonyms":[{"value":"BAR"},{"value":"FXR"},{"value":"HRR1"},{"value":"RIP14"}]}],"alphafold_very_low_content":0.33539094650205764,"disorder_content":0.03292181069958848,"disprot_consensus":{"full":[{"start":275,"end":290,"type":"D"}],"Structural state":[{"start":275,"end":290,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01458","name":"SUF system FeS cluster assembly, SufBD core domain","start":225,"end":466},{"id":"PF19295","name":"SufBD protein N-terminal region","start":156,"end":217}]},"uniref50":"UniRef50_P77522","sequence":"MSRNTEATDDVKTWTGGPLNYKEGFFTQLATDELAKGINEEVVRAISAKRNEPEWMLEFRLNAYRAWLEMEEPHWLKAHYDKLNYQDYSYYSAPSCGNCDDTCASEPGAVQQTGANAFLSKEVEAAFEQLGVPVREGKEVAVDAIFDSVSVATTYREKLAEQGIIFCSFGEAIHDHPELVRKYLGTVVPGNDNFFAALNAAVASDGTFIYVPKGVRCPMELSTYFRINAEKTGQFERTILVADEDSYVSYIEGCSAPVRDSYQLHAAVVEVIIHKNAEVKYSTVQNWFPGDNNTGGILNFVTKRALCEGENSKMSWTQSETGSAITWKYPSCILRGDNSIGEFYSVALTSGHQQADTGTKMIHIGKNTKSTIISKGISAGHSQNSYRGLVKIMPTATNARNFTQCDSMLIGANCGAHTFPYVECRNNSAQLEHEATTSRIGEDQLFYCLQRGISEEDAISMIVNGFCKDVFSELPLEFAVEAQKLLAISLEHSVG","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P77522","disprot_id":"DP01920","ncbi_taxon_id":83333,"regions_counter":2,"creator":"jlecle","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":156,"region_id":"DP01920r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Functional Dynamics Revealed by the Structure of the SufBCD Complex, a Novel ATP-binding Cassette (ABC) Protein That Serves as a Scaffold for Iron-Sulfur Cluster Biogenesis. <i> Hirabayashi K, Yuda E, Tanaka N, Katayama S, Iwasaki K, Matsumoto T, Kurisu G, Outten FW, Fukuyama K, Takahashi Y, Wada K. </i> J Biol Chem, 2015","term_id":"IDPO:0000002","curator_id":"jlecle","start":80,"term_ontology":"IDPO","curator_name":"Jeremy Y Leclercq","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0372-3277","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5AWF"}],"reference_id":"26472926","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":33,"region_id":"DP01920r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Functional Dynamics Revealed by the Structure of the SufBCD Complex, a Novel ATP-binding Cassette (ABC) Protein That Serves as a Scaffold for Iron-Sulfur Cluster Biogenesis. <i> Hirabayashi K, Yuda E, Tanaka N, Katayama S, Iwasaki K, Matsumoto T, Kurisu G, Outten FW, Fukuyama K, Takahashi Y, Wada K. </i> J Biol Chem, 2015","term_id":"IDPO:0000002","curator_id":"jlecle","start":1,"term_ontology":"IDPO","curator_name":"Jeremy Y Leclercq","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0372-3277","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5AWF"}],"reference_id":"26472926","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P77522","date":"2018-08-16T09:40:22.000Z","acc":"P77522","name":"FeS cluster assembly protein SufB","length":495,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI00001680C6","genes":[{"name":{"value":"sufB"},"synonyms":[{"value":"ynhE"}],"olnNames":[{"value":"b1683"},{"value":"JW5273"}]}],"alphafold_very_low_content":0.07676767676767676,"disorder_content":0.2222222222222222,"disprot_consensus":{"full":[{"start":1,"end":33,"type":"D"},{"start":80,"end":156,"type":"D"}],"Structural state":[{"start":1,"end":33,"type":"D"},{"start":80,"end":156,"type":"D"}]}},{"acc":"Q92900","sequence":"MSVEAYGPSSQTLTFLDTEEAELLGADTQGSEFEFTDFTLPSQTQTPPGGPGGPGGGGAGGPGGAGAGAAAGQLDAQVGPEGILQNGAVDDSVAKTSQLLAELNFEEDEEDTYYTKDLPIHACSYCGIHDPACVVYCNTSKKWFCNGRGNTSGSHIVNHLVRAKCKEVTLHKDGPLGETVLECYNCGCRNVFLLGFIPAKADSVVVLLCRQPCASQSSLKDINWDSSQWQPLIQDRCFLSWLVKIPSEQEQLRARQITAQQINKLEELWKENPSATLEDLEKPGVDEEPQHVLLRYEDAYQYQNIFGPLVKLEADYDKKLKESQTQDNITVRWDLGLNKKRIAYFTLPKTDSGNEDLVIIWLRDMRLMQGDEICLRYKGDLAPLWKGIGHVIKVPDNYGDEIAIELRSSVGAPVEVTHNFQVDFVWKSTSFDRMQSALKTFAVDETSVSGYIYHKLLGHEVEDVIIKCQLPKRFTAQGLPDLNHSQVYAVKTVLQRPLSLIQGPPGTGKTVTSATIVYHLARQGNGPVLVCAPSNIAVDQLTEKIHQTGLKVVRLCAKSREAIDSPVSFLALHNQIRNMDSMPELQKLQQLKDETGELSSADEKRYRALKRTAERELLMNADVICCTCVGAGDPRLAKMQFRSILIDESTQATEPECMVPVVLGAKQLILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVVLGIRPIRLQVQYRMHPALSAFPSNIFYEGSLQNGVTAADRVKKGFDFQWPQPDKPMFFYVTQGQEEIASSGTSYLNRTEAANVEKITTKLLKAGAKPDQIGIITPYEGQRSYLVQYMQFSGSLHTKLYQEVEIASVDAFQGREKDFIILSCVRANEHQGIGFLNDPRRLNVALTRARYGVIIVGNPKALSKQPLWNHLLNYYKEQKVLVEGPLNNLRESLMQFSKPRKLVNTINPGARFMTTAMYDAREAIIPGSVYDRSSQGRPSSMYFQTHDQIGMISAGPSHVAAMNIPIPFNLVMPPMPPPGYFGQANGPAAGRGTPKGKTGRGGRQKNRFGLPGPSQTNLPNSQASQDVASQPFSQGALTQGYISMSQPSQMSQPGLSQPELSQDSYLGDEFKSQIDVALSQDSTYQGERAYQHGGVTGLSQY","alphafold_very_low_content":"0.29317980513728964","creator":"vacs","dataset":[],"date":"2018-08-16T10:41:45.000Z","disprot_id":"DP01921","features":{"pfam":[{"id":"PF04851","name":"Type III restriction enzyme, res subunit","start":482,"end":551},{"id":"PF09416","name":"RNA helicase (UPF2 interacting domain)","start":121,"end":272},{"id":"PF13086","name":"AAA domain","start":585,"end":682},{"id":"PF13087","name":"AAA domain","start":691,"end":887},{"id":"PF18141","name":"RNA helicase UPF1, 1B domain","start":324,"end":425}],"gene3D":[{"start":714,"end":925,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d929b"},{"start":324,"end":425,"id":"2.40.30.230","name":"2.40.30.230","_id":"685af523b4ac24d5329d929c"}]},"genes":[{"name":{"value":"UPF1","evidences":[{"source":{"id":"HGNC:9962","name":"HGNC","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9962","_id":"685af523b4ac24d5329d92bf"},"code":"ECO:0000312","_id":"685af523b4ac24d5329d92be"}],"_id":"685af523b4ac24d5329d92c0"},"synonyms":[{"value":"KIAA0221","evidences":[],"_id":"685af523b4ac24d5329d92c1"},{"value":"RENT1","evidences":[{"source":{"id":"HGNC:9962","name":"HGNC","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9962","_id":"685af523b4ac24d5329d92c4"},"code":"ECO:0000312","_id":"685af523b4ac24d5329d92c3"}],"_id":"685af523b4ac24d5329d92c2"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d92bd"}],"length":1129,"name":"Regulator of nonsense transcripts 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":7,"released":"2018_11","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI000014CCB5","uniref100":"UniRef100_Q92900","uniref50":"UniRef50_Q92900","uniref90":"UniRef90_Q92900","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6EJ5","_id":"685af523b4ac24d5329d92a6"}],"curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":348,"end":359,"interaction_partner":[],"reference_html":"A conserved structural element in the RNA helicase UPF1 regulates its catalytic activity in an isoform-specific manner. <i> Gowravaram M, Bonneau F, Kanaan J, Maciej VD, Fiorini F, Raj S, Croquette V, Le Hir H, Chakrabarti S. </i> Nucleic Acids Res, 2018","reference_id":"29378013","region_id":"DP01921r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"First, the regulatory loop of UPF12ΔCH is well ordered and folded into a 310 helix, whereas that of UPF11ΔCH is partially disordered and in an extended conformation.","_id":"685af523b4ac24d5329d92a7"},{"type":"Results","text":"Therefore, the extended loop of UPF11 points away from the helicase core and is oriented toward the solvent (Figure 4B, inset). Our structural observations suggest that the longer regulatory loop of UPF11 has a higher intrinsic flexibility than that of the regulatory loop of UPF12.","_id":"685af523b4ac24d5329d92a8"},{"type":"Figure","text":"The shorter regulatory loop of UPF12ΔCH (in blue) is well ordered and folded into a 310 helix which is positioned toward the helicase core while the partially disordered longer loop of UPF11ΔCH (in cyan) is highly flexible and oriented toward the solvent.","_id":"685af523b4ac24d5329d92a9"},{"type":"Curator statement","text":"Residues 348-359 are not visible in the electron density map.","_id":"685af523b4ac24d5329d92aa"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":2,"_id":"685af523b4ac24d5329d92a5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007694","ec_name":"phosphatase assay evidence used in manual assertion","ec_ontology":"ECO","start":348,"end":359,"interaction_partner":[],"reference_html":"A conserved structural element in the RNA helicase UPF1 regulates its catalytic activity in an isoform-specific manner. <i> Gowravaram M, Bonneau F, Kanaan J, Maciej VD, Fiorini F, Raj S, Croquette V, Le Hir H, Chakrabarti S. </i> Nucleic Acids Res, 2018","reference_id":"29378013","region_id":"DP01921r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"We compared the ATPase activities of UPF11 and UPF12 and found that a longer regulatory loop did not inhibit the catalytic activity of the helicase (Figure 1C, compare purple and yellow traces). In fact, UPF11 showed a marginally higher ATPase activity than UPF12.","_id":"685af523b4ac24d5329d92ac"},{"type":"Results","text":"Contrary to our expectations of stronger inhibition of catalytic activity by the long regulatory loop, we find that activated UPF11 shows significantly higher ATPase activity than activated UPF12 (Figure 2C, compare first two columns in the middle and right stacks). Furthermore, the ATPase activity of UPF11ΔCH is identical to that of the UPF1ΔCHΔloop mutant (Figure 2C, compare second and third column in the right stack), indicating that deletion or elongation of the regulatory loop mediates similar effects on the activity of UPF1.","_id":"685af523b4ac24d5329d92ad"},{"type":"Curator statement","text":"Residues 348-359 are not visible in the electron density map and therefore this region is disordered within the regulatory loop (PDB: 6EJ5).","_id":"685af523b4ac24d5329d92ae"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","term_id":"GO:0098772","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function regulator","term_namespace":"Molecular function","term_not_annotate":true,"term_ontology":"GO","version":3,"_id":"685af523b4ac24d5329d92ab","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0000269","ec_name":"experimental evidence used in manual assertion","ec_ontology":"ECO","start":348,"end":359,"interaction_partner":[],"reference_html":"A conserved structural element in the RNA helicase UPF1 regulates its catalytic activity in an isoform-specific manner. <i> Gowravaram M, Bonneau F, Kanaan J, Maciej VD, Fiorini F, Raj S, Croquette V, Le Hir H, Chakrabarti S. </i> Nucleic Acids Res, 2018","reference_id":"29378013","region_id":"DP01921r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"We sought to determine whether presence of a longer regulatory loop in UPF1 would also mediate a similar effect on its RNA-binding affinity. To address this, we performed fluorescence anisotropy assays with UPF11ΔCH and UPF12ΔCH using a fluorescein-labeled 26-mer RNA, in the presence and absence of ATP. As previously reported, UPF12ΔCH shows a significant (18-fold) reduction in RNA-binding affinity in the presence of ATP while UPF11ΔCH shows only a modest 5-fold decrease (Figure 2D, compare cyan and green traces) (21,22). A similar trend was observed when comparing constructs encompassing the CH domain; UPF12 shows a 16-fold reduction in RNA-binding affinity in the presence of ATP in comparison to the 5-fold decrease exhibited by UPF11 (Figure 2D, compare purple and yellow traces). However, perturbing the length of the regulatory loop did not affect the length of RNA bound by UPF1 in the presence or absence of nucleotides, as observed in RNase protection assays (Supplementary Figure S2D and data not shown). Our results suggest that deletion or elongation of the regulatory loop modulates the RNA-binding affinity as well as the catalytic activity of UPF1 in a similar manner.","_id":"685af523b4ac24d5329d92b0"},{"type":"Curator statement","text":"Residues 348-359 are not visible in the electron density map and therefore this region is disordered within the regulatory loop (PDB: 6EJ5).","_id":"685af523b4ac24d5329d92b1"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","term_id":"GO:0098772","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function regulator","term_namespace":"Molecular function","term_not_annotate":true,"term_ontology":"GO","version":3,"_id":"685af523b4ac24d5329d92af","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6EJ5","_id":"685af523b4ac24d5329d92b3"}],"curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":348,"end":359,"interaction_partner":[],"reference_html":"A conserved structural element in the RNA helicase UPF1 regulates its catalytic activity in an isoform-specific manner. <i> Gowravaram M, Bonneau F, Kanaan J, Maciej VD, Fiorini F, Raj S, Croquette V, Le Hir H, Chakrabarti S. </i> Nucleic Acids Res, 2018","reference_id":"29378013","region_id":"DP01921r006","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"To determine the mechanistic basis of this differential catalytic activity, we have determined the X-ray crystal structure of the helicase core of UPF11 in its apo-state. Our results point toward a novel mechanism of regulation of RNA helicases, wherein alternative splicing leads to subtle structural rearrangements within the protein that are critical to modulate enzyme movements and catalytic activity.","_id":"685af523b4ac24d5329d92b4"},{"type":"Figure","text":"The short regulatory loop of UPF12 is more rigid and occupies part of the RNA binding surface in the apo- and AMPPNP-bound states of UPF1. Therefore, it poses as a barrier to translocation of UPF1 upon ATP hydrolysis and has to be displaced from the RNA-binding pocket in each cycle (top panel). In contrast, the longer regulatory loop of UPF11 is flexible and does not effectively block RNA binding in the presence of ATP or impede translocation (bottom panel). As a consequence, this loop does not have to be removed from the RNA-binding surface each time to allow ATP-dependent translocation of UPF1, resulting in a more active helicase.","_id":"685af523b4ac24d5329d92b5"},{"type":"Supplementary material","text":"The regulatory loop of UPF11ΔCH approaches the RNA binding surface but does not significantly occlude it or clash with the RNA (inset), in comparison to the regulatory loop of UPF12ΔCH (Figure S1B).","_id":"685af523b4ac24d5329d92b6"},{"type":"Curator statement","text":"Residues 348-359 are not visible in the electron density map.","_id":"685af523b4ac24d5329d92b7"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","term_id":"GO:0098772","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function regulator","term_namespace":"Molecular function","term_not_annotate":true,"term_ontology":"GO","version":3,"_id":"685af523b4ac24d5329d92b2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-08T15:06:31.884Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007159","ec_name":"ATP bioluminescence assay evidence used in manual assertion","ec_ontology":"ECO","start":348,"end":359,"interaction_partner":[],"reference_html":"A conserved structural element in the RNA helicase UPF1 regulates its catalytic activity in an isoform-specific manner. <i> Gowravaram M, Bonneau F, Kanaan J, Maciej VD, Fiorini F, Raj S, Croquette V, Le Hir H, Chakrabarti S. </i> Nucleic Acids Res, 2018","reference_id":"29378013","region_id":"DP01921r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"To assess whether the elongation of the regulatory loop has an impact on the properties of single molecules of UPF1, we compared the unwinding and translocation activities of UPF11ΔCH and UPF12ΔCH onto a long DNA hairpin.","_id":"685af523b4ac24d5329d92b9"},{"type":"Results","text":"However, UPF11ΔCH was two times faster than UPF12ΔCH with a weighted average rate of 2.4 bp/s during unwinding (1.0 bp/s for UPF12CH), and 4.6 bp/s during rezipping (2.4 bp/s for UPF12CH) (Figure 3 and Supplementary Figure S3). This result correlates perfectly with the higher ATP consumption rate of UPF11ΔCH compared to UPF12ΔCH (Figure 2C and Supplementary Figure S2C). Therefore, the recording of numerous and independent translocation events of single molecules of UPF1 revealed that its two natural isoforms possess different translocation speeds.","_id":"685af523b4ac24d5329d92ba"},{"type":"Figure","text":"UPF11ΔCH unwinds nucleic acid with a higher translocation speed than UPF12ΔCH.","_id":"685af523b4ac24d5329d92bb"},{"type":"Curator statement","text":"Residues 348-359 are not visible in the electron density map and therefore this region is disordered within the regulatory loop (PDB: 6EJ5).","_id":"685af523b4ac24d5329d92bc"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","term_id":"GO:0098772","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function regulator","term_namespace":"Molecular function","term_not_annotate":true,"term_ontology":"GO","version":4,"_id":"685af523b4ac24d5329d92b8","reference_source":"pmid"}],"__v":0,"disorder_content":0.010628875110717449,"disprot_consensus":{"full":[{"start":348,"end":359,"type":"D"}],"Structural state":[{"start":348,"end":359,"type":"D"}],"Molecular function":[{"start":348,"end":359,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00319","name":"SRF-type transcription factor (DNA-binding and dimerisation domain)","start":10,"end":57},{"id":"PF12347","name":"Holliday junction regulator protein family C-terminal repeat","start":95,"end":153}],"gene3D":[{"start":13,"end":94,"id":"3.40.1810.10","name":"Transcription factor, MADS-box"}]},"uniref50":"UniRef50_Q02078","sequence":"MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVEALNKKEHRGCDSPDPDTSYVLTPHTEEKYKKINEEFDNMMRNHKIAPGLPPQNFSMSVTVPVTSPNALSYTNPGSSLVSPSLAASSTLTDSSMLSPPQTTLHRNVSPGAPQRPPSTGNAGGMLSTTDLTVPNGAGSSPVGNGFVNSRASPNLIGATGANSLGKVMPTKSPPPPGGGNLGMNSRKPDLRVVIPPSSKGMMPPLSEEEELELNTQRISSSQATQPLATPVVSVTTPSLPPQGLVYSAMPTAYNTDYSLTSADLSALQGFNSPGMLSLGQVSAWQQHHLGQAALSSLVAGGQLSQGSNLSINTNQNISIKSEPISPPRDRMTPSGFQQQQQQQQQQQPPPPPQPQPQPPQPQPRQEMGRSPVDSLSSSSSSYDGSDREDPRGDFHSPIVLGRPPNTEDRESPSVKRMRMDAWVT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q02078","disprot_id":"DP01925","ncbi_taxon_id":9606,"regions_counter":1,"creator":"mpajkos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":86,"region_id":"DP01925r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of the MEF2A-DNA complex: structural basis for the modulation of DNA bending and specificity by MADS-box transcription factors. <i> Huang K, Louis JM, Donaldson L, Lim FL, Sharrocks AD, Clore GM. </i> EMBO J, 2000","statement":[{"text":"Note that the protein sequence starts at Gly1, and the N-terminal methionine is completely excised.\n\"Residues 74–85 of the protein are disordered in solution.\"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":75,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"10835359","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q02078","date":"2018-08-16T13:09:24.000Z","acc":"Q02078","name":"Myocyte-specific enhancer factor 2A","length":507,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012EEB3","genes":[{"name":{"value":"MEF2A"},"synonyms":[{"value":"MEF2"}]}],"alphafold_very_low_content":0.6765285996055227,"disorder_content":0.023668639053254437,"disprot_consensus":{"full":[{"start":75,"end":86,"type":"D"}],"Structural state":[{"start":75,"end":86,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00152","name":"tRNA synthetases class II (D, K and N)","start":150,"end":318},{"id":"PF00152","name":"tRNA synthetases class II (D, K and N)","start":354,"end":559},{"id":"PF01336","name":"OB-fold nucleic acid binding domain","start":54,"end":127},{"id":"PF01588","name":"Putative tRNA binding domain","start":615,"end":709}],"gene3D":[{"start":1,"end":145,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"},{"start":608,"end":768,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}]},"uniref50":"UniRef50_A0A5K1VR98","sequence":"MSKQLFLNRCKDVEEYQKAGHNPWPHKFNVSITVPEFIAKYSGLEKSQVSDDIVSVAGRVLSKRSSSSALMFIDLHDSQTKLQIMLNKSAYENKEDFVSLTKMIYRGDICGFTGHPTRTKTGELSLIPISGMILSPCLHMLPSMHYGLGDQETRFRKRYLDLIVNPESVKNFVLRTKVVKAVRKYLDDKGFLEVETPILNTIPGGATARPFITHHNQLDIQMYMRIAPELYLKELVVGGINRVYEIGRLFRNEGIDQTHNPEFTTCEFYMAYADYNDIMKMTEELLGNMVKDITGGSTKLEIKDRLMDINNEEDIKMLEKFFKEPIPRPFNSAECSKVIEKHCTELNYYYDGNNEKAMKKLFADFVTEKKMVLDFTAPFKRISYVHALEEKFGEKIPRPLDGPEALTFLKKQAIRFNAICAEPQTTARVMDKLFGDLIEVDLVQPTFVCDQPQLMSPLAKYHRSEPELTERFELFILKREIANAYTELNNPIVQRSNFEQQAKDKAAGDDEAQLVDEVFLDAIEHAFPPTGGWGLGIDRLAMLLADVDNIKEVILFPTMRPEDELEKKAREAKEDAMVAQELAATEEKGGKKVVKPKANKQQPVKEVLDGFQLEIRVGKIVEAGPHPNSEHLLALKVDVGEEKPRSVVAGLAEHYKPEELLNQKATFVCNLKPSKLRGVASEAMILAATSLDGTKVKFCHPSADAAIGAQVIPKEGKVTISAKKISIDVVGKMNLALKGGLVRTNDVPLIVKDTELTVTVDEVVDGTVR","taxonomy":["Eukaryota","Amoebozoa","Evosea","Archamoebae","Mastigamoebida","Entamoebidae","Entamoeba"],"uniref90":"UniRef90_A0A5K1VR98","disprot_id":"DP01926","ncbi_taxon_id":5759,"regions_counter":1,"creator":"jlecle","regions":[{"region_id":"DP01926r001","ec_ontology":"ECO","end":769,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":583,"version":3,"statement":[{"text":"In all structures, residues 304–368 between strands β13 and β14, residues 507–513 between helices α15 and α16, and residues after position 583 are disordered.","type":"Article"}],"term_name":"disorder","reference_html":"Crystal structures of Entamoeba histolytica lysyl-tRNA synthetase reveal conformational changes upon lysine binding and a specific helix bundle domain. <i> Bonnefond L, Castro de Moura M, Ribas de Pouplana L, Nureki O. </i> FEBS Lett, 2014","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"25448989","date":"2024-02-07T16:33:01.900Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4UP7"},{"db":"PDB","id":"4UP8"},{"db":"PDB","id":"4UPA"},{"db":"PDB","id":"4UP9"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu582Lys","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val764Ile","start":null,"end":null,"position":null},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:33113"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5957"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:445205"}],"sequence_construct":"MHHHHHHMLSKQLFLNRCKDVEEYQKAGHNPWPHKFNVSITVPEFIAKYSGLEKSQVSDDIVSVAGRVLSKRSSSSALMFIDLHDSQTKLQIMLNKSAYENKEDFVSLTKMIYRGDICGFTGHPTRTKTGELSLIPISGMILSPCLHMLPSMHYGLGDQETRFRKRYLDLIVNPESVKNFVLRTKVVKAVRKYLDDKGFLEVETPILNTIPGGATARPFITHHNQLDIQMYMRIAPELYLKELVVGGINRVYEIGRLFRNEGIDQTHNPEFTTCEFYMAYADYNDIMKMTEELLGNMVKDITGGSTKLEIKDRLMDINNEEDIKMLEKFFKEPIPRPFNSAECSKVIEKHCTELNYYYDGNNEKAMKKLFADFVTEKKMVLDFTAPFKRISYVHALEEKFGEKIPRPLDGPEALTFLKKQAIRFNAICAEPQTTARVMDKLFGDLIEVDLVQPTFVCDQPQLMSPLAKYHRSEPELTERFELFILKREIANAYTELNNPIVQRSNFEQQAKDKAAGDDEAQLVDEVFLDAIEHAFPPTGGWGLGIDRLAMLLADVDNIKEVILFPTMRPEDELEKKAREAKEDAMVAQEKAATEEKGGKKVVKPKANKQQPVKEVLDGFQLEIRVGKIVEAGPHPNSEHLLALKVDVGEEKPRSVVAGLAEHYKPEELLNQKATFVCNLKPSKLRGVASEAMILAATSLDGTKVKFCHPSADAAIGAQVIPKEGKVTISAKKISIDVVGKMNLALKGGLVRTNDVPLIVKDTELTVTVDEVIDGTVR"}],"released":"2018_11","uniref100":"UniRef100_A0A5K1VR98","date":"2018-08-16T13:13:10.000Z","acc":"C4M7X2","name":"Lysine--tRNA ligase","length":769,"organism":"Entamoeba histolytica","dataset":[],"UniParc":"UPI000172F769","genes":[{"orfNames":[{"value":"EHI_047810","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EAL45214.2","url":"https://www.ebi.ac.uk/ena/browser/view/EAL45214.2"}}]}]}],"alphafold_very_low_content":0.031209362808842653,"disorder_content":0.24317295188556567,"disprot_consensus":{"full":[{"start":583,"end":769,"type":"D"}],"Structural state":[{"start":583,"end":769,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02703","name":"Early E1A protein","start":1,"end":163}]},"uniref50":"UniRef50_P03255","sequence":"MRHIICHGGVITEEMAASLLDQLIEEVLADNLPPPSHFEPPTLHELYDLDVTAPEDPNEEAVSQIFPDSVMLAVQEGIDLLTFPPAPGSPEPPHLSRQPEQPEQRALGPVSMPNLVPEVIDLTCHEAGFPPSDDEDEEGEEFVLDYVEHPGHGCRSCHYHRRNTGDPDIMCSLCYMRTCGMFVYSPVSEPEPEPEPEPEPARPTRRPKLVPAILRRPTSPVSRECNSSTDSCDSGPSNTPPEIHPVVPLCPIKPVAVRVGGRRQAVECIEDLLNESGQPLDLSCKRPRP","taxonomy":["Viruses","Varidnaviria","Bamfordvirae","Preplasmiviricota","Tectiliviricetes","Rowavirales","Adenoviridae","Mastadenovirus"],"uniref90":"UniRef90_P03255","disprot_id":"DP01928","ncbi_taxon_id":10515,"regions_counter":6,"creator":"jbergier","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":137,"region_id":"DP01928r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural and Dynamic Characterization of the Molecular Hub Early Region 1A (E1A) from Human Adenovirus. <i> Hošek T, Calçada EO, Nogueira MO, Salvi M, Pagani TD, Felli IC, Pierattelli R. </i> Chemistry, 2016","statement":[{"text":"The 2D 1H–15N correlation NMR experiments acquired on E1A289 and E1A243 (Figure 2 A,B) confirm that both isoforms of E1A are highly disordered and flexible, as inferred from the small chemical shift dispersion of the NMR signals.[27] (Figure 2)","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"lchemes","start":1,"term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"27490777","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0003-0192-9906","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-13T11:02:51.781Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":289,"region_id":"DP01928r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural and Dynamic Characterization of the Molecular Hub Early Region 1A (E1A) from Human Adenovirus. <i> Hošek T, Calçada EO, Nogueira MO, Salvi M, Pagani TD, Felli IC, Pierattelli R. </i> Chemistry, 2016","statement":[{"text":"The 2D 1H–15N correlation NMR experiments acquired on E1A289 and E1A243 (Figure 2 A,B) confirm that both isoforms of E1A are highly disordered and flexible, as inferred from the small chemical shift dispersion of the NMR signals.[27] (figure 2)","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"lchemes","start":191,"term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"27490777","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0003-0192-9906","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-13T11:02:46.809Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":289,"reference_id":"27490777","reference_source":"pmid","reference_html":"Structural and Dynamic Characterization of the Molecular Hub Early Region 1A (E1A) from Human Adenovirus. <i> Hošek T, Calçada EO, Nogueira MO, Salvi M, Pagani TD, Felli IC, Pierattelli R. </i> Chemistry, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01928r003","statement":[{"text":"The 2D 1H–15N correlation NMR experiments acquired on E1A289 and E1A243 (Figure 2 A,B) confirm that both isoforms of E1A are highly disordered and flexible, as inferred from the small chemical shift dispersion of the NMR signals.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-13T11:02:45.481Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":154,"end":174,"reference_id":"27490777","reference_source":"pmid","reference_html":"Structural and Dynamic Characterization of the Molecular Hub Early Region 1A (E1A) from Human Adenovirus. <i> Hošek T, Calçada EO, Nogueira MO, Salvi M, Pagani TD, Felli IC, Pierattelli R. </i> Chemistry, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"ChEBI","id":"29105","partner_start":null,"partner_end":null}],"region_id":"DP01928r004","statement":[{"text":"The five cysteine residues were assigned and the chemical shifts values for the Cα and Cβ of Cys 154, 157, 171, and 174 are consistent with their involvement in ZnII-binding.","type":"Results"},{"text":"On the other hand, the results on the E1ACR3 clearly indicate the presence of a minimal fold composed by just two helices of less than 10 amino acids embedded in a relatively flexible polypeptide. The binding of ZnII restricts the conformational space for the two helices, which should face each other to properly locate the ligand cysteines.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-13T11:03:34.052Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":153,"end":180,"reference_id":"27490777","reference_source":"pmid","reference_html":"Structural and Dynamic Characterization of the Molecular Hub Early Region 1A (E1A) from Human Adenovirus. <i> Hošek T, Calçada EO, Nogueira MO, Salvi M, Pagani TD, Felli IC, Pierattelli R. </i> Chemistry, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP01928r005","statement":[{"text":"A similar analysis was accomplished for E1ACR3. The SSP plot derived for the amino acids of this construct indicates the presence of two α-helices beginning with the CXXC motifs and including residues 153–165 and 170–180 (Figure 3).","type":"Results"},{"text":"On the other hand, the results on the E1ACR3 clearly indicate the presence of a minimal fold composed by just two helices of less than 10 amino acids embedded in a relatively flexible polypeptide. The binding of ZnII restricts the conformational space for the two helices, which should face each other to properly locate the ligand cysteines.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-13T12:22:25.389Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_P03254","date":"2018-08-16T16:43:45.000Z","acc":"P03254","name":"Early E1A protein","length":289,"organism":"Human adenovirus C serotype 2","dataset":["Viral proteins"],"UniParc":"UPI0000129A7D","genes":[],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":152,"type":"D"},{"start":153,"end":180,"type":"T"},{"start":181,"end":289,"type":"D"}],"Structural state":[{"start":1,"end":289,"type":"D"}],"Molecular function":[{"start":154,"end":174,"type":"F"}],"Structural transition":[{"start":153,"end":180,"type":"T"}]}},{"acc":"P17763","sequence":"MNNQRKKTGRPSFNMLKRARNRVSTVSQLAKRFSKGLLSGQGPMKLVMAFIAFLRFLAIPPTAGILARWGSFKKNGAIKVLRGFKKEISNMLNIMNRRKRSVTMLLMLLPTALAFHLTTRGGEPHMIVSKQERGKSLLFKTSAGVNMCTLIAMDLGELCEDTMTYKCPRITETEPDDVDCWCNATETWVTYGTCSQTGEHRRDKRSVALAPHVGLGLETRTETWMSSEGAWKQIQKVETWALRHPGFTVIALFLAHAIGTSITQKGIIFILLMLVTPSMAMRCVGIGNRDFVEGLSGATWVDVVLEHGSCVTTMAKDKPTLDIELLKTEVTNPAVLRKLCIEAKISNTTTDSRCPTQGEATLVEEQDTNFVCRRTFVDRGWGNGCGLFGKGSLITCAKFKCVTKLEGKIVQYENLKYSVIVTVHTGDQHQVGNETTEHGTTATITPQAPTSEIQLTDYGALTLDCSPRTGLDFNEMVLLTMEKKSWLVHKQWFLDLPLPWTSGASTSQETWNRQDLLVTFKTAHAKKQEVVVLGSQEGAMHTALTGATEIQTSGTTTIFAGHLKCRLKMDKLTLKGMSYVMCTGSFKLEKEVAETQHGTVLVQVKYEGTDAPCKIPFSSQDEKGVTQNGRLITANPIVTDKEKPVNIEAEPPFGESYIVVGAGEKALKLSWFKKGSSIGKMFEATARGARRMAILGDTAWDFGSIGGVFTSVGKLIHQIFGTAYGVLFSGVSWTMKIGIGILLTWLGLNSRSTSLSMTCIAVGMVTLYLGVMVQADSGCVINWKGRELKCGSGIFVTNEVHTWTEQYKFQADSPKRLSAAIGKAWEEGVCGIRSATRLENIMWKQISNELNHILLENDMKFTVVVGDVSGILAQGKKMIRPQPMEHKYSWKSWGKAKIIGADVQNTTFIIDGPNTPECPDNQRAWNIWEVEDYGFGIFTTNIWLKLRDSYTQVCDHRLMSAAIKDSKAVHADMGYWIESEKNETWKLARASFIEVKTCIWPKSHTLWSNGVLESEMIIPKIYGGPISQHNYRPGYFTQTAGPWHLGKLELDFDLCEGTTVVVDEHCGNRGPSLRTTTVTGKTIHEWCCRSCTLPPLRFKGEDGCWYGMEIRPVKEKEENLVKSMVSAGSGEVDSFSLGLLCISIMIEEVMRSRWSRKMLMTGTLAVFLLLTMGQLTWNDLIRLCIMVGANASDKMGMGTTYLALMATFRMRPMFAVGLLFRRLTSREVLLLTVGLSLVASVELPNSLEELGDGLAMGIMMLKLLTDFQSHQLWATLLSLTFVKTTFSLHYAWKTMAMILSIVSLFPLCLSTTSQKTTWLPVLLGSLGCKPLTMFLITENKIWGRKSWPLNEGIMAVGIVSILLSSLLKNDVPLAGPLIAGGMLIACYVISGSSADLSLEKAAEVSWEEEAEHSGASHNILVEVQDDGTMKIKDEERDDTLTILLKATLLAISGVYPMSIPATLFVWYFWQKKKQRSGVLWDTPSPPEVERAVLDDGIYRILQRGLLGRSQVGVGVFQEGVFHTMWHVTRGAVLMYQGKRLEPSWASVKKDLISYGGGWRFQGSWNAGEEVQVIAVEPGKNPKNVQTAPGTFKTPEGEVGAIALDFKPGTSGSPIVNREGKIVGLYGNGVVTTSGTYVSAIAQAKASQEGPLPEIEDEVFRKRNLTIMDLHPGSGKTRRYLPAIVREAIRRNVRTLVLAPTRVVASEMAEALKGMPIRYQTTAVKSEHTGKEIVDLMCHATFTMRLLSPVRVPNYNMIIMDEAHFTDPASIAARGYISTRVGMGEAAAIFMTATPPGSVEAFPQSNAVIQDEERDIPERSWNSGYDWITDFPGKTVWFVPSIKSGNDIANCLRKNGKRVVQLSRKTFDTEYQKTKNNDWDYVVTTDISEMGANFRADRVIDPRRCLKPVILKDGPERVILAGPMPVTVASAAQRRGRIGRNQNKEGDQYIYMGQPLNNDEDHAHWTEAKMLLDNINTPEGIIPALFEPEREKSAAIDGEYRLRGEARKTFVELMRRGDLPVWLSYKVASEGFQYSDRRWCFDGERNNQVLEENMDVEIWTKEGERKKLRPRWLDARTYSDPLALREFKEFAAGRRSVSGDLILEIGKLPQHLTQRAQNALDNLVMLHNSEQGGKAYRHAMEELPDTIETLMLLALIAVLTGGVTLFFLSGRGLGKTSIGLLCVIASSALLWMASVEPHWIAASIILEFFLMVLLIPEPDRQRTPQDNQLAYVVIGLLFMILTAAANEMGLLETTKKDLGIGHAAAENHHHAAMLDVDLHPASAWTLYAVATTIITPMMRHTIENTTANISLTAIANQAAILMGLDKGWPISKMDIGVPLLALGCYSQVNPLTLTAAVFMLVAHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGIVAIDLDPVVYDAKFEKQLGQIMLLILCTSQILLMRTTWALCESITLATGPLTTLWEGSPGKFWNTTIAVSMANIFRGSYLAGAGLAFSLMKSLGGGRRGTGAQGETLGEKWKRQLNQLSKSEFNTYKRSGIIEVDRSEAKEGLKRGEPTKHAVSRGTAKLRWFVERNLVKPEGKVIDLGCGRGGWSYYCAGLKKVTEVKGYTKGGPGHEEPIPMATYGWNLVKLYSGKDVFFTPPEKCDTLLCDIGESSPNPTIEEGRTLRVLKMVEPWLRGNQFCIKILNPYMPSVVETLEQMQRKHGGMLVRNPLSRNSTHEMYWVSCGTGNIVSAVNMTSRMLLNRFTMAHRKPTYERDVDLGAGTRHVAVEPEVANLDIIGQRIENIKNGHKSTWHYDEDNPYKTWAYHGSYEVKPSGSASSMVNGVVRLLTKPWDVIPMVTQIAMTDTTPFGQQRVFKEKVDTRTPKAKRGTAQIMEVTARWLWGFLSRNKKPRICTREEFTRKVRSNAAIGAVFVDENQWNSAKEAVEDERFWDLVHRERELHKQGKCATCVYNMMGKREKKLGEFGKAKGSRAIWYMWLGARFLEFEALGFMNEDHWFSRENSLSGVEGEGLHKLGYILRDISKIPGGNMYADDTAGWDTRITEDDLQNEAKITDIMEPEHALLATSIFKLTYQNKVVRVQRPAKNGTVMDVISRRDQRGSGQVGTYGLNTFTNMEAQLIRQMESEGIFSPSELETPNLAERVLDWLKKHGTERLKRMAISGDDCVVKPIDDRFATALTALNDMGKVRKDIPQWEPSKGWNDWQQVPFCSHHFHQLIMKDGREIVVPCRNQDELVGRARVSQGAGWSLRETACLGKSYAQMWQLMYFHRRDLRLAANAICSAVPVDWVPTSRTTWSIHAHHQWMTTEDMLSVWNRVWIEENPWMEDKTHVSSWEDVPYLGKREDRWCGSLIGLTARATWATNIQVAINQVRRLIGNENYLDFMTSMKRFKNESDPEGALW","creator":"lchemes","dataset":["Viral proteins","Neglected tropical diseases proteins","RNA-binding proteins"],"date":"2018-08-16T17:05:52.000Z","disprot_id":"DP01929","features":{"pfam":[{"id":"PF00869","name":"Flavivirus glycoprotein, central and dimerisation domains","start":282,"end":576},{"id":"PF00948","name":"Flavivirus non-structural Protein NS1","start":777,"end":1130},{"id":"PF00949","name":"Peptidase S7, Flavivirus NS3 serine protease","start":1493,"end":1642},{"id":"PF00972","name":"Flavivirus RNA-directed RNA polymerase, fingers and palm domains","start":2743,"end":3192},{"id":"PF01002","name":"Flavivirus non-structural protein NS2B","start":1349,"end":1475},{"id":"PF01003","name":"Flavivirus capsid protein C","start":6,"end":112},{"id":"PF01004","name":"Flavivirus envelope glycoprotein M","start":207,"end":280},{"id":"PF01005","name":"Flavivirus non-structural protein NS2A","start":1138,"end":1312},{"id":"PF01349","name":"Flavivirus non-structural protein NS4B","start":2245,"end":2486},{"id":"PF01350","name":"Flavivirus non-structural protein NS4A","start":2099,"end":2239},{"id":"PF01570","name":"Flavivirus polyprotein propeptide","start":120,"end":204},{"id":"PF01728","name":"FtsJ-like methyltransferase","start":2548,"end":2714},{"id":"PF02832","name":"Flavivirus glycoprotein, immunoglobulin-like domain","start":578,"end":673},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1659,"end":1806},{"id":"PF20483","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","start":3196,"end":3359},{"id":"PF20907","name":"Flavivirus NS3 helicase, C-terminal helical domain","start":1950,"end":2092},{"id":"PF21659","name":"Flavivirus envelope glycoprotein E, stem/anchor domain","start":676,"end":770}],"gene3D":[{"start":206,"end":280,"id":"1.10.8.970","name":"Flavivirus envelope glycoprotein M-like","_id":"685af523b4ac24d5329d92d3"},{"start":115,"end":195,"id":"2.60.260.50","name":"Flavivirus polyprotein propeptide domain","_id":"685af523b4ac24d5329d92d4"},{"start":283,"end":573,"id":"2.60.98.10","name":"Tick-borne Encephalitis virus Glycoprotein, domain 1","_id":"685af523b4ac24d5329d92d5"},{"start":332,"end":554,"id":"3.30.67.10","name":"Viral Envelope Glycoprotein, domain 2","_id":"685af523b4ac24d5329d92d6"},{"start":21,"end":100,"id":"1.10.10.930","name":"1.10.10.930","_id":"685af523b4ac24d5329d92d7"},{"start":574,"end":677,"id":"2.60.40.350","name":"2.60.40.350","_id":"685af523b4ac24d5329d92d8"},{"start":678,"end":775,"id":"1.20.1280.260","name":"1.20.1280.260","_id":"685af523b4ac24d5329d92d9"},{"start":342,"end":535,"id":"3.30.387.10","name":"Viral Envelope Glycoprotein, domain 3","_id":"685af523b4ac24d5329d92da"},{"start":2494,"end":2761,"id":"3.40.50.150","name":"Vaccinia Virus protein VP39","_id":"685af523b4ac24d5329d92db"},{"start":1659,"end":1991,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d92dc"},{"start":2833,"end":2874,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d92dd"},{"start":2762,"end":2826,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d92de"},{"start":1496,"end":1564,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d92df"},{"start":3022,"end":3088,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d92e0"},{"start":1389,"end":1454,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d92e1"},{"start":1798,"end":1957,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d92e2"},{"start":2886,"end":2981,"id":"1.10.260.90","name":"1.10.260.90","_id":"685af523b4ac24d5329d92e3"},{"start":1469,"end":1642,"id":"2.40.10.10","name":"Trypsin-like serine proteases","_id":"685af523b4ac24d5329d92e4"}]},"genes":[],"length":3392,"name":"Genome polyprotein","ncbi_taxon_id":11059,"organism":"Dengue virus type 1 (strain Nauru/West Pac/1974)","regions_counter":2,"released":"2018_11","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Flavivirus"],"UniParc":"UPI0000131DF1","uniref100":"UniRef100_P17763","uniref50":"UniRef50_P17763","uniref90":"UniRef90_P17763","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3L6P","_id":"685af523b4ac24d5329d92ea"},{"db":"PDB","id":"3LKW","_id":"685af523b4ac24d5329d92eb"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1649,"end":1661,"interaction_partner":[],"reference_html":"Serotype-specific structural differences in the protease-cofactor complexes of the dengue virus family. <i> Chandramouli S, Joseph JS, Daudenarde S, Gatchalian J, Cornillez-Ty C, Kuhn P. </i> J Virol, 2010","reference_id":"20042502","region_id":"DP01929r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"While residues C terminal to Glu173 are disordered in the DEN1proΔ11-20 structure, they are visible and stabilized through crystal contacts in the S135A structure.","_id":"685af523b4ac24d5329d92ec"},{"type":"Curator statement","text":"The PDB 3L6P shows the structure without the mutation S135A (S1610A in the Uniprot) and has the C-terminal disordered. ","_id":"685af523b4ac24d5329d92ed"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T09:15:46.318Z","_id":"685af523b4ac24d5329d92ee"},"version":1,"_id":"685af523b4ac24d5329d92e9","reference_source":"pmid"}],"__v":0,"disorder_content":0.0038325471698113208,"disprot_consensus":{"full":[{"start":1649,"end":1661,"type":"D"}],"Structural state":[{"start":1649,"end":1661,"type":"D"}]}},{"acc":"P29990","sequence":"MNDQRKKAKNTPFNMLKRERNRVSTVQQLTKRFSLGMLQGRGPLKLYMALVAFLRFLTIPPTAGILKRWGTIKKSKAINVLRGFRKEIGRMLNILNRRRRSAGMIIMLIPTVMAFHLTTRNGEPHMIVSRQEKGKSLLFKTEDGVNMCTLMAMDLGELCEDTITYKCPLLRQNEPEDIDCWCNSTSTWVTYGTCTTMGEHRRQKRSVALVPHVGMGLETRTETWMSSEGAWKHVQRIETWILRHPGFTMMAAILAYTIGTTHFQRALIFILLTAVTPSMTMRCIGMSNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPTLDFELIKTEAKQPATLRKYCIEAKLTNTTTESRCPTQGEPSLNEEQDKRFVCKHSMVDRGWGNGCGLFGKGGIVTCAMFRCKKNMEGKVVQPENLEYTIVITPHSGEEHAVGNDTGKHGKEIKITPQSSTTEAELTGYGTVTMECSPRTGLDFNEMVLLQMENKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFTGHLKCRLRMDKLQLKGMSYSMCTGKFKVVKEIAETQHGTIVIRVQYEGDGSPCKIPFEIMDLEKRHVLGRLITVNPIVTEKDSPVNIEAEPPFGDSYIIIGVEPGQLKLNWFKKGSSIGQMFETTMRGAKRMAILGDTAWDFGSLGGVFTSIGKALHQVFGAIYGAAFSGVSWTMKILIGVIITWIGMNSRSTSLSVTLVLVGIVTLYLGVMVQADSGCVVSWKNKELKCGSGIFITDNVHTWTEQYKFQPESPSKLASAIQKAHEEGICGIRSVTRLENLMWKQITPELNHILSENEVKLTIMTGDIKGIMQAGKRSLRPQPTELKYSWKTWGKAKMLSTESHNQTFLIDGPETAECPNTNRAWNSLEVEDYGFGVFTTNIWLKLKEKQDVFCDSKLMSAAIKDNRAVHADMGYWIESALNDTWKIEKASFIEVKNCHWPKSHTLWSNGVLESEMIIPKNLAGPVSQHNYRPGYHTQITGPWHLGKLEMDFDFCDGTTVVVTEDCGNRGPSLRTTTASGKLITEWCCRSCTLPPLRYRGEDGCWYGMEIRPLKEKEENLVNSLVTAGHGQVDNFSLGVLGMALFLEEMLRTRVGTKHAILLVAVSFVTLIIGNMSFRDLGRVMVMVGATMTDDIGMGVTYLALLAAFKVRPTFAAGLLLRKLTSKALMMTTIGIVLSSQSTTPETILELTDALALGMMVLKMVRNMEKYQLAVTIMAILCVPNAVILQNAWKVSCTILAVVSVSPLFLTSSQQKTDWIPLALTIKGLNPTAIFLTTLSRTSKKRSWPLNEAIMAVGMVSILASSLLKNDIPMTGPLVAGGPLTVCYVLTGRSADLELERAADVKWEDQAEISGSSPILSITISEDGSMSIKNEEEEQTLTILIRTGLLVISGLFPVSIPITAAAWYLWEVKKQRAGVLWDVPSPPPMGKAELEDGAYRIKQKGILGYSQIGAGVYKEGTFHTMWHVTRGAVLMHKGKRIEPSWADVKKDLISYGGGWKLEGEWKEGEEVQVLALEPGKNPRAVQTKPGLFKTNAGTIGAVSLDFSPGTSGSPIIDKKGKVVGLYGNGVVTRSGAYVSAIAQTEKSIEDNPEIEDDIFRKRRLTIMDLHPGAGKTKRYLPAIVREAIKRGLRTLILAPTRVVAAEMEEALRGLPIRYQTPAIRAEHTGREIVDLMCHATFTMRLLSPVRVPNYNLIIMDEAHFTDPASIAARGYISTRVEMGEAAGIFMTATPPGSRDPFPQSNAPIIDEEREIPERSWNSGHEWVTDFKGKTVWFVPSIKAGNDIAACLSKNGKKVIQLSRKTFDSEYAKTRTNDWDFVVTTDISEMGANFKAERVIDPRRCMKPVILTDGEERVILAGPMPVTHSSAAQRRGRIGRNPKNENDQYIYMGEPLENDEDCAHWKEAKMLLDNINTPEGIIPSMFEPEREKVDAIDGEYRLRGEARTTFVDLMRRGDLPVWLAYRVAAEGINYADRRWCFDGVKNNQILEENVEVEIWTKEGERKKLKPRWLDARIYSDPLALKEFKEFAAGRKSLTLNLITEMGRLPTFMTQKARDALDNLAVLHTAEAGGRAYNHALSELPETLETLLLLTLLATVTGGILLFLMSGRGIGKMTLGMCCIITASILLWYAQIQPHWIAASIILEFFLIVLLIPEPEKQRTPQDNQLTYVVIAILTVVAATMANEMGFLEKTKKDLGLGSIATQQPESNILDIDLRPASAWTLYAVATTFVTPMLRHSIENSSVNVSLTAIANQATVLMGLGKGWPLSKMDIGVPLLAIGCYSQVNPTTLTAALFLLVAHYAIIGPALQAKASREAQKRAAAGIMKNPTVDGITVIDLDPIPYDPKFEKQLGQVMLLVLCVTQVLMMRTTWALCEVLTLATGPISTLWEGNPGRFWNTTIAVSMANIFRGSYLAGAGLLFSIMKNTTNARRGTGNIGETLGEKWKSRLNALGKSEFQIYKKSGIQEVDRTLAKEGIKRGETDHHAVSRGSAKLRWFVERNMVTPEGKVVDLGCGRGGWSYYCGGLKNVREVKGLTKGGPGHEEPIPMSTYGWNLVRLQSGVDVFFIPPEKCDTLLCDIGESSPNPTVEAGRTLRVLNLVENWLNNNTQFCIKVLNPYMPSVIEKMEALQRKYGGALVRNPLSRNSTHEMYWVSNASGNIVSSVNMISRMLINRFTMRYKKATYEPDVDLGSGTRNIGIESEIPNLDIIGKRIEKIKQEHETSWHYDQDHPYKTWAYHGSYETKQTGSASSMVNGVFRLLTKPWDVVPMVTQMAMTDTTPFGQQRVFKEKVDTRTQEPKEGTKKLMKITAEWLWKELGKKKTPRMCTREEFTRKVRSNAALGAIFTDENKWKSAREAVEDSRFWELVDKERNLHLEGKCETCVYNIMGKREKKLGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWFSRENSLSGVEGEGLHKLGYILRDVSKKEGGAMYADDTAGWDTRITLEDLKNEAMVTNHMEGEHKKLAEAIFKLTYQNKVVRVQRPTPRGTVMDIISRRDQRGSGQVGTYGLNTFTNMEAQLIRQMEGEGVFKSIQHLTITEEIAVQNWLARVGRERLSRMAISGDDCVVKPLDDRLPSALTALNDTGKIRKDIQQWEPSRGWNDWTQVPFCSHHFHELIMKDGRVLVVPCRNQDELIGRARISQGAGWSLRETACLGKSYDQMWSLMYFHRRDLRLAANAICSAVPSHWVPTSRTTWSIHAKHEWMTTEDMLTVWNRVWIQENPWMEDKTPVESWEEIPYLGKREDQWCGSLIGLTSRATWAKNIQAAINQVRSLIGNEEYTDYMPSMKRFRREEEEAGVLW","creator":"lchemes","dataset":["Viral proteins","Neglected tropical diseases proteins","RNA-binding proteins"],"date":"2018-08-16T17:06:09.000Z","disprot_id":"DP01930","features":{"pfam":[{"id":"PF00869","name":"Flavivirus glycoprotein, central and dimerisation domains","start":282,"end":576},{"id":"PF00948","name":"Flavivirus non-structural Protein NS1","start":777,"end":1129},{"id":"PF00949","name":"Peptidase S7, Flavivirus NS3 serine protease","start":1492,"end":1643},{"id":"PF00972","name":"Flavivirus RNA-directed RNA polymerase, fingers and palm domains","start":2742,"end":3191},{"id":"PF01002","name":"Flavivirus non-structural protein NS2B","start":1349,"end":1475},{"id":"PF01003","name":"Flavivirus capsid protein C","start":5,"end":113},{"id":"PF01004","name":"Flavivirus envelope glycoprotein M","start":207,"end":279},{"id":"PF01005","name":"Flavivirus non-structural protein NS2A","start":1138,"end":1313},{"id":"PF01349","name":"Flavivirus non-structural protein NS4B","start":2244,"end":2484},{"id":"PF01350","name":"Flavivirus non-structural protein NS4A","start":2099,"end":2240},{"id":"PF01570","name":"Flavivirus polyprotein propeptide","start":120,"end":204},{"id":"PF01728","name":"FtsJ-like methyltransferase","start":2546,"end":2713},{"id":"PF02832","name":"Flavivirus glycoprotein, immunoglobulin-like domain","start":578,"end":673},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1658,"end":1805},{"id":"PF20483","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","start":3196,"end":3358},{"id":"PF20907","name":"Flavivirus NS3 helicase, C-terminal helical domain","start":1949,"end":2091},{"id":"PF21659","name":"Flavivirus envelope glycoprotein E, stem/anchor domain","start":676,"end":770}],"gene3D":[{"start":342,"end":535,"id":"3.30.387.10","name":"Viral Envelope Glycoprotein, domain 3","_id":"685af523b4ac24d5329d92fd"},{"start":21,"end":100,"id":"1.10.10.930","name":"1.10.10.930","_id":"685af523b4ac24d5329d92fe"},{"start":332,"end":554,"id":"3.30.67.10","name":"Viral Envelope Glycoprotein, domain 2","_id":"685af523b4ac24d5329d92ff"},{"start":283,"end":571,"id":"2.60.98.10","name":"Tick-borne Encephalitis virus Glycoprotein, domain 1","_id":"685af523b4ac24d5329d9300"},{"start":679,"end":775,"id":"1.20.1280.260","name":"1.20.1280.260","_id":"685af523b4ac24d5329d9301"},{"start":115,"end":195,"id":"2.60.260.50","name":"Flavivirus polyprotein propeptide domain","_id":"685af523b4ac24d5329d9302"},{"start":572,"end":678,"id":"2.60.40.350","name":"2.60.40.350","_id":"685af523b4ac24d5329d9303"},{"start":206,"end":280,"id":"1.10.8.970","name":"Flavivirus envelope glycoprotein M-like","_id":"685af523b4ac24d5329d9304"},{"start":1496,"end":1564,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d9305"},{"start":1389,"end":1452,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d9306"},{"start":1658,"end":1991,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d9307"},{"start":2885,"end":2980,"id":"1.10.260.90","name":"1.10.260.90","_id":"685af523b4ac24d5329d9308"},{"start":2492,"end":2760,"id":"3.40.50.150","name":"Vaccinia Virus protein VP39","_id":"685af523b4ac24d5329d9309"},{"start":1797,"end":1956,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d930a"},{"start":3019,"end":3087,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d930b"},{"start":1469,"end":1642,"id":"2.40.10.10","name":"Trypsin-like serine proteases","_id":"685af523b4ac24d5329d930c"},{"start":2761,"end":2823,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d930d"},{"start":2831,"end":2872,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d930e"}]},"genes":[],"length":3391,"name":"Genome polyprotein","ncbi_taxon_id":31634,"organism":"Dengue virus type 2 (strain Thailand/16681/1984)","regions_counter":2,"released":"2018_11","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Flavivirus"],"UniParc":"UPI0000131DF5","uniref100":"UniRef100_P29990","uniref50":"UniRef50_P17763","uniref90":"UniRef90_P29990","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"4O6B","_id":"685af523b4ac24d5329d9314"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":883,"end":903,"interaction_partner":[],"reference_html":"Flavivirus NS1 structures reveal surfaces for associations with membranes and the immune system. <i> Akey DL, Brown WC, Dutta S, Konwerski J, Jose J, Jurkiw TJ, DelProposto J, Ogata CM, Skiniotis G, Kuhn RJ, Smith JL. </i> Science, 2014","reference_id":"24505133","region_id":"DP01930r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The second domain (amino acids 30-180) of each monomer protrudes from the central β-domain like a wing (Fig. 1A, yellow). Each “wing” domain contains two glycosylation sites (Asn130, Asn175), an internal disulfide (Cys55-Cys143), and two discreet subdomains. An α/β subdomain (amino acids 38 – 151) comprises a four-stranded β-sheet, two α-helices and a disordered distal tip (amino acids 108 – 128; Fig. 1A, dotted line).","_id":"685af523b4ac24d5329d9315"},{"type":"Curator statement","text":"Region 108-128 of NS1 protein corresponds to the region 884-904 of the polyprotein of Dengue virus type 2 (strain Thailand/16681/1984).","_id":"685af523b4ac24d5329d9316"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-26T07:22:19.234Z","_id":"685af523b4ac24d5329d9317"},"version":1,"_id":"685af523b4ac24d5329d9313","reference_source":"pmid"}],"__v":0,"disorder_content":0.006192863462105573,"disprot_consensus":{"full":[{"start":883,"end":903,"type":"D"}],"Structural state":[{"start":883,"end":903,"type":"D"}]}},{"acc":"Q2YHF0","sequence":"MNQRKKVARPPFNMLKRERNRVSTPQGLVKRFSTGLFSGKGPLRMVLAFITFLRVLSIPPTAGILKRWGQLKKNKAIKILTGFRKEIGRMLNILNGRKRSTITLLCLIPTVMAFHLSTRDGEPLMIVAKHERGRPLLFKTTEGINKCTLIAMDLGEMCEDTVTYKCPLLVNTEPEDIDCWCNLTSAWVMYGTCTQSGERRREKRSVALTPHSGMGLETRAETWMSSEGAWKHAQRVESWILRNPGFALLAGFMAYMIGQTGIQRTVFFILMMLVAPSYGMRCVGVGNRDFVEGVSGGAWVDLVLEHGGCVTTMAQGKPTLDFELIKTTAKEVALLRTYCIEASISNITTATRCPTQGEPYLKEEQDQQYICRRDMVDRGWGNGCGLFGKGGVVTCAKFSCSGKITGNLVQIENLEYTVVVTVHNGDTHAVGNDTSNHGVTATITPRSPSVEVKLPDYGELTLDCEPRSGIDFNEMILMKMKTKTWLVHKQWFLDLPLPWTAGADTLEVHWNHKERMVTFKVPHAKRQDVTVLGSQEGAMHSALAGATEVDSGDGNHMFAGHLKCKVRMEKLRIKGMSYTMCSGKFSIDKEMAETQHGTTVVKVKYEGTGAPCKVPIEIRDVNKEKVVGRIISSTPFAENTNSVTNIELEPPFGDSYIVIGVGDSALTLHWFRKGSSIGKMFESTYRGAKRMAILGETAWDFGSVGGLLTSLGKAVHQVFGSVYTTMFGGVSWMVRILIGLLVLWIGTNSRNTSMAMSCIAVGGITLFLGFTVHADMGCAVSWSGKELKCGSGIFVIDNVHTWTEQYKFQPESPARLASAILNAHKDGVCGIRSTTRLENVMWKQITNELNYVLWEGGHDLTVVAGDVKGVLSKGKRALAPPVNDLKYSWKTWGKAKIFTPETRNSTFLVDGPDTSECPNERRAWNFLEVEDYGFGMFTTNIWMKFREGSSEVCDHRLMSAAIKDQKAVHADMGYWIESSKNQTWQIEKASLIEVKTCLWPKTHTLWSNGVLESQMLIPKAYAGPISQHNYRQGYATQTVGPWHLGKLEIDFGECPGTTVTIQEDCDHRGPSLRTTTASGKLVTQWCCRSCTMPPLRFLGEDGCWYGMEIRPLNEKEENMVKSQVSAGQGTSETFSMGLLCLTLFVEECLRRRVTRKHMILVVVTTLCAIILGGLTWMDLLRALIMLGDTMSGRMGGQIHLAIMAVFKMSPGYVLGIFLRKLTSRETALMVIGMAMTTVLSIPHDLMEFIDGISLGLILLKMVTHFDNTQVGTLALSLTFIKSTMPLVMAWRTIMAVLFVVTLIPLCRTSCLQKQSHWVEITALILGAQALPVYLMTLMKGASKRSWPLNEGIMAVGLVSLLGSALLKNDVPLAGPMVAGGLLLAAYVMSGSSADLSLEKAANVQWDEMADITGSSPIIEVKQDEDGSFSIRDVEETNMITLLVKLALITVSGLYPLAIPVTMTLWYMWQVKTQRSGALWDVPSPAAAQKATLTEGVYRIMQRGLFGKTQVGVGIHMEGVFHTMWHVTRGSVICHESGRLEPSWADVRNDMISYGGGWRLGDKWDKEEDVQVLAIEPGKNPKHVQTKPGLFKTLTGEIGAVTLDFKPGTSGSPIINRKGKVIGLYGNGVVTKSGDYVSAITQAERIGEPDYEVDEDIFRKKRLTIMDLHPGAGKTKRILPSIVREALKRRLRTLILAPTRVVAAEMEEALRGLPIRYQTPAVKSEHTGREIVDLMCHATFTTRLLSSTRVPNYNLIVMDEAHFTDPSSVAARGYISTRVEMGEAAAIFMTATPPGTTDPFPQSNSPIEDIEREIPERSWNTGFDWITDYQGKTVWFVPSIKAGNDIANCLRKSGKKVIQLSRKTFDTEYPKTKLTDWDFVVTTDISEMGANFRAGRVIDPRRCLKPVILTDGPERVILAGPIPVTPASAAQRRGRIGRNPAQEDDQYVFSGDPLRNDEDHAHWTEAKMLLDNIYTPEGIIPTLFGPEREKTQAIDGEFRLRGEQRKTFVELMRRGDLPVWLSYKVASAGISYKDREWCFTGERNNQILEENMEVEIWTREGEKKKLRPKWLDARVYADPMALKDFKEFASGRKSITLDILTEIASLPTYLSSRAKLALDNIVMLHTTERGGKAYQHALNELPESLETLMLVALLGAMTAGIFLFFMQGKGIGKLSMGLIAIAVASGLLWVAEIQPQWIAASIILEFFLMVLLVPEPEKQRTPQDNQLIYVILTILTIIALVAANEMGLIEKTKTDFGFYQAKTETTILDVDLRPASAWTLYAVATTILTPMLRHTIENTSANLSLAAIANQAAVLMGLGKGWPLHRMDLGVPLLAMGCYSQVNPTTLTASLVMLLVHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGITVIDLEPISYDPKFEKQLGQVMLLVLCAGQLLLMRTTWAFCEVLTLATGPILTLWEGNPGRFWNTTIAVSTANIFRGSYLAGAGLAFSLIKNAQTPRRGTGTTGETLGEKWKRQLNSLDRKEFEEYKRSGILEVDRTEAKSALKDGSKIKYAVSRGTSKIRWIVERGMVKPKGKVVDLGCGRGGWSYYMATLKNVTEVKGYTKGGPGHEEPIPMATYGWNLVKLHSGVDVFYKPTEQVDTLLCDIGESSSNPTIEEGRTLRVLKMVEPWLSSKPEFCIKVLNPYMPTVIEELEKLQRKHGGSLVRCPLSRNSTHEMYWVSGVSGNIVSSVNTTSKMLLNRFTTRHRKPTYEKDADLGAGTRSVSTETEKPDMTIIGRRLQRLQEEHKETWHYDHENPYRTWAYHGSYEAPSTGSASSMVNGVVKLLTKPWDVVPMVTQLAMTDTTPFGQQRVFKEKVDTRTPQPKPGTRVVMTTTANWLWALLGRKKNPRLCTREEFISKVRSNAAIGAVFQEEQGWTSASEAVNDSRFWELVDKERALHQEGKCESCVYNMMGKREKKLGEFGRAKGSRAIWYMWLGARFLEFEALGFLNEDHWFGRENSWSGVEGEGLHRLGYILEDIDKKDGDLIYADDTAGWDTRITEDDLLNEELITEQMAPHHKILAKAIFKLTYQNKVVKVLRPTPKGAVMDIISRKDQRGSGQVGTYGLNTFTNMEVQLIRQMEAEGVITRDDMHNPKGLKERVEKWLKECGVDRLKRMAISGDDCVVKPLDERFSTSLLFLNDMGKVRKDIPQWEPSKGWKNWQEVPFCSHHFHKIFMKDGRSLVVPCRNQDELIGRARISQGAGWSLRETACLGKAYAQMWSLMYFHRRDLRLASMAICSAVPTEWFPTSRTTWSIHAHHQWMTTEDMLKVWNRVWIEDNPNMIDKTPVHSWEDIPYLGKREDLWCGSLIGLSSRATWAKNIQTAITQVRNLIGKEEYVDYMPVMKRYSAHFESEGVL","creator":"lchemes","dataset":["Viral proteins","Neglected tropical diseases proteins","RNA-binding proteins"],"date":"2018-08-16T17:06:25.000Z","disprot_id":"DP01931","features":{"pfam":[{"id":"PF00869","name":"Flavivirus glycoprotein, central and dimerisation domains","start":281,"end":575},{"id":"PF00948","name":"Flavivirus non-structural Protein NS1","start":777,"end":1128},{"id":"PF00949","name":"Peptidase S7, Flavivirus NS3 serine protease","start":1492,"end":1641},{"id":"PF00972","name":"Flavivirus RNA-directed RNA polymerase, fingers and palm domains","start":2738,"end":3188},{"id":"PF01002","name":"Flavivirus non-structural protein NS2B","start":1348,"end":1474},{"id":"PF01003","name":"Flavivirus capsid protein C","start":5,"end":112},{"id":"PF01004","name":"Flavivirus envelope glycoprotein M","start":206,"end":278},{"id":"PF01005","name":"Flavivirus non-structural protein NS2A","start":1137,"end":1308},{"id":"PF01349","name":"Flavivirus non-structural protein NS4B","start":2243,"end":2480},{"id":"PF01350","name":"Flavivirus non-structural protein NS4A","start":2097,"end":2238},{"id":"PF01570","name":"Flavivirus polyprotein propeptide","start":119,"end":203},{"id":"PF01728","name":"FtsJ-like methyltransferase","start":2542,"end":2709},{"id":"PF02832","name":"Flavivirus glycoprotein, immunoglobulin-like domain","start":577,"end":672},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1657,"end":1804},{"id":"PF20483","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","start":3192,"end":3355},{"id":"PF20907","name":"Flavivirus NS3 helicase, C-terminal helical domain","start":1950,"end":2090},{"id":"PF21659","name":"Flavivirus envelope glycoprotein E, stem/anchor domain","start":675,"end":769}],"gene3D":[{"start":678,"end":774,"id":"1.20.1280.260","name":"1.20.1280.260","_id":"685af523b4ac24d5329d9326"},{"start":20,"end":99,"id":"1.10.10.930","name":"1.10.10.930","_id":"685af523b4ac24d5329d9327"},{"start":331,"end":553,"id":"3.30.67.10","name":"Viral Envelope Glycoprotein, domain 2","_id":"685af523b4ac24d5329d9328"},{"start":574,"end":677,"id":"2.60.40.350","name":"2.60.40.350","_id":"685af523b4ac24d5329d9329"},{"start":114,"end":194,"id":"2.60.260.50","name":"Flavivirus polyprotein propeptide domain","_id":"685af523b4ac24d5329d932a"},{"start":282,"end":572,"id":"2.60.98.10","name":"Tick-borne Encephalitis virus Glycoprotein, domain 1","_id":"685af523b4ac24d5329d932b"},{"start":205,"end":279,"id":"1.10.8.970","name":"Flavivirus envelope glycoprotein M-like","_id":"685af523b4ac24d5329d932c"},{"start":341,"end":534,"id":"3.30.387.10","name":"Viral Envelope Glycoprotein, domain 3","_id":"685af523b4ac24d5329d932d"},{"start":2828,"end":2866,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d932e"},{"start":2881,"end":2976,"id":"1.10.260.90","name":"1.10.260.90","_id":"685af523b4ac24d5329d932f"},{"start":1468,"end":1641,"id":"2.40.10.10","name":"Trypsin-like serine proteases","_id":"685af523b4ac24d5329d9330"},{"start":1388,"end":1446,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d9331"},{"start":3018,"end":3083,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d9332"},{"start":1495,"end":1563,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d9333"},{"start":2488,"end":2757,"id":"3.40.50.150","name":"Vaccinia Virus protein VP39","_id":"685af523b4ac24d5329d9334"},{"start":2758,"end":2821,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d9335"},{"start":1657,"end":1990,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d9336"},{"start":1796,"end":1955,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d9337"}]},"genes":[],"length":3387,"name":"Genome polyprotein","ncbi_taxon_id":408688,"organism":"Dengue virus type 4 (strain Thailand/0348/1991)","regions_counter":4,"released":"2018_11","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Flavivirus"],"UniParc":"UPI00005ED855","uniref100":"UniRef100_Q2YHF0","uniref50":"UniRef50_P17763","uniref90":"UniRef90_P09866","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"statements":[{"type":"Introduction","text":"To investigate the functional significance of the interdomain flexibility conferred by the linker region (residues 169ERIGEPDYEVD179) in terms of enzymatic activity and virus replication, a Gly residue before Pro174 (underlined) was introduced or the Pro residue was replaced with Gly in DENV4 NS2B18NS3.","_id":"685af523b4ac24d5329d9342"},{"type":"Curator statement","text":"There is also another construct with an instertion of a Gly before Pro174 ","_id":"685af523b4ac24d5329d9343"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro174Gly","_id":"685af523b4ac24d5329d9341"}],"cross_refs":[{"db":"PDB","id":"2WZQ","_id":"685af523b4ac24d5329d933f"},{"db":"PDB","id":"2WHX","_id":"685af523b4ac24d5329d9340"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1644,"end":1654,"interaction_partner":[],"reference_html":"Flexibility between the protease and helicase domains of the dengue virus NS3 protein conferred by the linker region and its functional implications. <i> Luo D, Wei N, Doan DN, Paradkar PN, Chong Y, Davidson AD, Kotaka M, Lescar J, Vasudevan SG. </i> J Biol Chem, 2010","reference_id":"20375022","region_id":"DP01931r002","released":"2022_03","sample":[],"sequence_construct":"ERIGEPDYEVD","statement":[{"type":"Discussion","text":"A flexible linker region is identified which joins the NS3 protease and helicase domains allowing alternative conformations. The flexibility in this region is important for protease and helicase activity: \"Our results indicate that the linker region has evolved to an optimum length to confer flexibility to the NS3 protein that is required both for polyprotein processing and RNA replication.","_id":"685af523b4ac24d5329d933d"},{"type":"Results","text":"Thus, in both crystal forms, the protease domain appears significantly more mobile, which is consistent with proteolysis data showing that the protease domain is more labile. In the second conformation, only a few interactions are observed between the linker and either of the two domains: Glu169, Gly172, and Glu173 from the linker interact with Lys88 and Tyr83 from the protease and Arg202 and Ala197 from the P-loop (Fig. 2A). However, as a caveat, the electron density map for the linker region is less well defined for side chains of residues 169–176 (Fig. 2A). The overall B factor for the linker is 73.2 Å2, a value significantly higher than the average value for the other domains of NS3. This suggests some intrinsic degree of freedom conferred to the protein by the linker in solution.","_id":"685af523b4ac24d5329d933e"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-27T10:29:47.411Z","_id":"685af523b4ac24d5329d9344"},"version":3,"_id":"685af523b4ac24d5329d933c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"statements":[{"type":"Introduction","text":"To investigate the functional significance of the interdomain flexibility conferred by the linker region (residues 169ERIGEPDYEVD179) in terms of enzymatic activity and virus replication, a Gly residue before Pro174 (underlined) was introduced or the Pro residue was replaced with Gly in DENV4 NS2B18NS3.","_id":"685af523b4ac24d5329d9348"}],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro174Gly","_id":"685af523b4ac24d5329d9347"}],"cross_refs":[{"db":"PDB","id":"2WHX","_id":"685af523b4ac24d5329d9349"},{"db":"PDB","id":"2WZQ","_id":"685af523b4ac24d5329d934a"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1644,"end":1654,"interaction_partner":[],"reference_html":"Flexibility between the protease and helicase domains of the dengue virus NS3 protein conferred by the linker region and its functional implications. <i> Luo D, Wei N, Doan DN, Paradkar PN, Chong Y, Davidson AD, Kotaka M, Lescar J, Vasudevan SG. </i> J Biol Chem, 2010","reference_id":"20375022","region_id":"DP01931r003","released":"2022_03","sample":[],"sequence_construct":"ERIGEPDYEVD","statement":[{"type":"Results","text":"The two domains of NS3 are linked by a polypeptide segment spanning residues 169–179. This interdomain (“linker”) acid-rich segment displays some sequence variation, yet its overall length appears to be restricted to 11 or 12 amino acids across flaviviruses. In both conformation I and II, the linker region was partially disordered with only clear electron density for the backbone (Fig. 2) (10).","_id":"685af523b4ac24d5329d9346"}],"states_connection":[],"term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-27T10:29:48.122Z","_id":"685af523b4ac24d5329d934b"},"version":4,"_id":"685af523b4ac24d5329d9345","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2WHX","_id":"685af523b4ac24d5329d934d"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1475,"end":1494,"interaction_partner":[],"reference_html":"Flexibility between the protease and helicase domains of the dengue virus NS3 protein conferred by the linker region and its functional implications. <i> Luo D, Wei N, Doan DN, Paradkar PN, Chong Y, Davidson AD, Kotaka M, Lescar J, Vasudevan SG. </i> J Biol Chem, 2010","reference_id":"20375022","region_id":"DP01931r004","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The PDB shows a disordered region that corresponds to the N-terminal region of the NS3 protein.","_id":"685af523b4ac24d5329d934e"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-27T10:29:45.862Z","_id":"685af523b4ac24d5329d934f"},"version":1,"_id":"685af523b4ac24d5329d934c","reference_source":"pmid"}],"__v":0,"disorder_content":0.009152642456451136,"disprot_consensus":{"full":[{"start":1475,"end":1494,"type":"D"},{"start":1644,"end":1654,"type":"D"}],"Structural state":[{"start":1475,"end":1494,"type":"D"},{"start":1644,"end":1654,"type":"D"}],"Disorder function":[{"start":1644,"end":1654,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00331","name":"Glycosyl hydrolase family 10","start":45,"end":352},{"id":"PF00553","name":"Cellulose binding domain","start":382,"end":481}],"gene3D":[{"start":376,"end":484,"id":"2.60.40.290","name":"2.60.40.290"},{"start":42,"end":356,"id":"3.20.20.80","name":"Glycosidases"}]},"uniref50":"UniRef50_P07986","sequence":"MPRTTPAPGHPARGARTALRTTRRRAATLVVGATVVLPAQAATTLKEAADGAGRDFGFALDPNRLSEAQYKAIADSEFNLVVAENAMKWDATEPSQNSFSFGAGDRVASYAADTGKELYGHTLVWHSQLPDWAKNLNGSAFESAMVNHVTKVADHFEGKVASWDVVNEAFADGDGPPQDSAFQQKLGNGYIETAFRAARAADPTAKLCINDYNVEGINAKSNSLYDLVKDFKARGVPLDCVGFQSHLIVGQVPGDFRQNLQRFADLGVDVRITELDIRMRTPSDATKLATQAADYKKVVQACMQVTRCQGVTVWGITDKYSWVPDVFPGEGAALVWDASYAKKPAYAAVMEAFGASPTPTPTTPTPTPTTPTPTPTSGPAGCQVLWGVNQWNTGFTANVTVKNTSSAPVDGWTLTFSFPSGQQVTQAWSSTVTQSGSAVTVRNAPWNGSIPAGGTAQFGFNGSHTGTNAAPTAFSLNGTPCTVG","taxonomy":["Bacteria","Actinobacteria","Micrococcales","Cellulomonadaceae","Cellulomonas"],"uniref90":"UniRef90_P07986","disprot_id":"DP01933","ncbi_taxon_id":1708,"regions_counter":2,"creator":"thorvath","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":376,"region_id":"DP01933r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Direct demonstration of the flexibility of the glycosylated proline-threonine linker in the Cellulomonas fimi Xylanase Cex through NMR spectroscopic analysis. <i> Poon DK, Withers SG, McIntosh LP. </i> J Biol Chem, 2007","statement":[{"text":"Nevertheless, it is readily apparent that all of the linker threonines have poorly dispersed amide 1HN chemical shifts within the range expected for a random coil polypeptide","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"thorvath","start":357,"term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"17121820","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":376,"term_name":"flexible linker","start":357,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Cex Is Composed of Independent Catalytic and Cellulosebinding Domains Tethered by a Flexible PT Linker","type":"Discussion"}],"curator_id":"thorvath","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"17121820","version":3,"reference_html":"Direct demonstration of the flexibility of the glycosylated proline-threonine linker in the Cellulomonas fimi Xylanase Cex through NMR spectroscopic analysis. <i> Poon DK, Withers SG, McIntosh LP. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006165","region_id":"DP01933r002","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_P07986","date":"2018-08-16T19:42:08.000Z","acc":"P07986","name":"Exoglucanase/xylanase","length":484,"organism":"Cellulomonas fimi","dataset":[],"UniParc":"UPI000012BE19","genes":[{"name":{"value":"cex"},"synonyms":[{"value":"xynB"}]}],"alphafold_very_low_content":0.07024793388429752,"disorder_content":0.04132231404958678,"disprot_consensus":{"full":[{"start":357,"end":376,"type":"D"}],"Structural state":[{"start":357,"end":376,"type":"D"}],"Disorder function":[{"start":357,"end":376,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00553","name":"Cellulose binding domain","start":265,"end":353},{"id":"PF03067","name":"Lytic polysaccharide mono-oxygenase, cellulose-degrading","start":35,"end":225}],"gene3D":[{"start":260,"end":362,"id":"2.60.40.290","name":"2.60.40.290"},{"start":35,"end":230,"id":"2.70.50.50","name":"chitin-binding protein cbp21"}]},"uniref50":"UniRef50_D2BFT3","sequence":"MVRRTRLLTLAAVLATLLGSLGVTLLLGQGRAEAHGVAMMPGSRTYLCQLDAKTGTGALDPTNPACQAALDQSGATALYNWFAVLDSNAGGRGAGYVPDGTLCSAGDRSPYDFSAYNAARSDWPRTHLTSGATIPVEYSNWAAHPGDFRVYLTKPGWSPTSELGWDDLELIQTVTNPPQQGSPGTDGGHYYWDLALPSGRSGDALIFMQWVRSDSQENFFSCSDVVFDGGNGEVTGIRGSGSTPDPDPTPTPTDPTTPPTHTGSCMAVYSVENSWSGGFQGSVEVMNHGTEPLNGWAVQWQPGGGTTLGGVWNGSLTSGSDGTVTVRNVDHNRVVPPDGSVTFGFTATSTGNDFPVDSIGCVAP","taxonomy":["Bacteria","Actinobacteria","Streptomycetales","Streptomycetaceae","Streptomyces","Streptomyces albidoflavus group"],"uniref90":"UniRef90_A0A1R1WUJ3","disprot_id":"DP01934","ncbi_taxon_id":100226,"regions_counter":2,"creator":"thorvath","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":264,"region_id":"DP01934r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The carbohydrate-binding module and linker of a modular lytic polysaccharide monooxygenase promote localized cellulose oxidation. <i> Courtade G, Forsberg Z, Heggset EB, Eijsink VGH, Aachmann FL. </i> J Biol Chem, 2018","statement":[{"text":"The result was an ensemble showing large  conformational variation as a result of the low structural restriction in the linker region","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"thorvath","start":235,"term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"29967065","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":264,"term_name":"flexible linker","start":235,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"The  linker  in ScLPMO10C serves  as  a flexible spacer, maintaining a distance between the carbohydrate-binding and catalytic domains, while simultaneously  enabling  these domains to  move independently of each other","type":"Discussion"}],"curator_id":"thorvath","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"29967065","version":3,"reference_html":"The carbohydrate-binding module and linker of a modular lytic polysaccharide monooxygenase promote localized cellulose oxidation. <i> Courtade G, Forsberg Z, Heggset EB, Eijsink VGH, Aachmann FL. </i> J Biol Chem, 2018","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006165","region_id":"DP01934r002","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_A0A7K2U9D5","date":"2018-08-16T20:50:23.000Z","acc":"Q9RJY2","name":"Putative secreted cellulose binding protein","length":364,"organism":"Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)","dataset":[],"UniParc":"UPI00000DB615","genes":[{"olnNames":[{"value":"SCO1188","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAB61600.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAB61600.1"}}]}]}],"alphafold_very_low_content":0.14560439560439561,"disorder_content":0.08241758241758242,"disprot_consensus":{"full":[{"start":235,"end":264,"type":"D"}],"Structural state":[{"start":235,"end":264,"type":"D"}],"Disorder function":[{"start":235,"end":264,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01246","name":"Ribosomal protein L24e","start":1,"end":66}],"gene3D":[{"start":1,"end":68,"id":"2.30.170.20","name":"Ribosomal protein L24e"},{"start":69,"end":98,"id":"3.30.160.440","name":"3.30.160.440"}]},"uniref50":"UniRef50_P83731","sequence":"MKVELCSFSGYKIYPGHGRRYARTDGKVFQFLNAKCESAFLSKRNPRQINWTVLYRRKHKKGQSEEIQKKRTRRAVKFQRAITGASLADIMAKRNQKPEVRKAQREQAIRAAKEAKKAKQASKKTAMAAAKAPTKAAPKQKIVKPVKVSAPRVGGKR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P83731","disprot_id":"DP01935","ncbi_taxon_id":9606,"regions_counter":2,"creator":"npalopoli","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":157,"region_id":"DP01935r001","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Visualization of chemical modifications in the human 80S ribosome structure. <i> Natchiar SK, Myasnikov AG, Kratzat H, Hazemann I, Klaholz BP. </i> Nature, 2017","term_id":"IDPO:0000002","curator_id":"npalopoli","start":125,"term_ontology":"IDPO","curator_name":"Nicolás Palopoli","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7925-6436","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"6EK0"}],"reference_id":"29143818","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":157,"region_id":"DP01935r002","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Structural snapshots of actively translating human ribosomes. <i> Behrmann E, Loerke J, Budkevich TV, Yamamoto K, Schmidt A, Penczek PA, Vos MR, Bürger J, Mielke T, Scheerer P, Spahn CM. </i> Cell, 2015","statement":[{"text":"Chain: AW; Unified name: eL24; Human name: L24; Template: 3U5E chain W; Swiss-Prot: P83731; Seq. length: 157; Residues modelled: 2-122","type":"Supplementary material"}],"term_id":"IDPO:0000002","curator_id":"npalopoli","start":123,"term_ontology":"IDPO","curator_name":"Nicolás Palopoli","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7925-6436","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5AJ0"}],"reference_id":"25957688","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P83731","date":"2018-08-16T21:59:26.000Z","acc":"P83731","name":"60S ribosomal protein L24","length":157,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000001688","genes":[{"name":{"value":"RPL24"}}],"alphafold_very_low_content":0.07006369426751592,"disorder_content":0.2229299363057325,"disprot_consensus":{"full":[{"start":123,"end":157,"type":"D"}],"Structural state":[{"start":123,"end":157,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00916","name":"Sulfate permease family","start":81,"end":475},{"id":"PF01740","name":"STAS domain","start":528,"end":708}]},"uniref50":"UniRef50_Q9EPH0","sequence":"MDHAEENEIPAETQKYLVERPIFSHPVLQERLHVKDKVTDSIGDKLKQAFTCTPKKVRNIIYMFLPITKWLPAYKFKEYVLGDLVSGISTGVLQLPQGLAFAMLAAVPPVFGLYSSFYPVIMYCFFGTSRHISIGPFAVISLMIGGVAVRLVPDDIVIPGGVNATNGTEARDALRVKVAMSVTLLSGIIQFCLGVCRFGFVAIYLTEPLVRGFTTAAAVHVFTSMLKYLFGVKTKRYSGIFSVVYSTVAVLQNVKNLNVCSLGVGLMVFGLLLGGKEFNERFKEKLPAPIPLEFFAVVMGTGISAGFNLHESYSVDVVGTLPLGLLPPANPDTSLFHLVYVDAIAIAIVGFSVTISMAKTLANKHGYQVDGNQELIALGICNSIGSLFQTFSISCSLSRSLVQEGTGGKTQLAGCLASLMILLVILATGFLFESLPQAVLSAIVIVNLKGMFMQFSDLPFFWRTSKIELTIWLTTFVSSLFLGLDYGLITAVIIALLTVIYRTQSPSYTVLGQLPDTDVYIDIDAYEEVKEIPGIKIFQINAPIYYANSDLYSSALKRKTGVNPAIIMGARRKAMRKYAKEVGNANIANATVVKVDAEVDGENATKPEEEDDEVKFPPIVIKTTFPEELQRFLPQGENIHTVILDFTQVNFMDSVGVKTLAGIVKEYGDVGIYVYLAGCSAQVVNDLTSNRFFENPALKELLFHSIHDAVLGSQVREAMAEQETTVLPPQEDMEPNATPTTPEA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_Q9EPH0","disprot_id":"DP01937","ncbi_taxon_id":10116,"regions_counter":1,"creator":"cbassot","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":636,"region_id":"DP01937r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structure of the cytosolic portion of the motor protein prestin and functional role of the STAS domain in SLC26/SulP anion transporters. <i> Pasqualetto E, Aiello R, Gesiot L, Bonetto G, Bellanda M, Battistutta R. </i> J Mol Biol, 2010","statement":[{"text":"Prestin STAS constructs without the variable loop, which is predicted to be mostly disordered, showed a better behavior in solution, with circular dichroism (CD)","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"cbassot","start":564,"term_ontology":"IDPO","curator_name":"Claudio Bassot","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3LLO"}],"reference_id":"20471983","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9EPH0","date":"2018-08-17T08:52:41.000Z","acc":"Q9EPH0","name":"Prestin","length":744,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI0000132197","genes":[{"name":{"value":"Slc26a5"},"synonyms":[{"value":"Pres"}]}],"alphafold_very_low_content":0.08064516129032258,"disorder_content":0.09811827956989247,"disprot_consensus":{"full":[{"start":564,"end":636,"type":"D"}],"Structural state":[{"start":564,"end":636,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00012","name":"Hsp70 protein","start":30,"end":635}],"gene3D":[{"start":406,"end":532,"id":"2.60.34.10","name":"Substrate Binding Domain Of DNAk; Chain A, domain 1"},{"start":533,"end":637,"id":"1.20.1270.10","name":"1.20.1270.10"},{"start":30,"end":402,"id":"3.30.420.40","name":"3.30.420.40"},{"start":254,"end":337,"id":"3.90.640.10","name":"Actin; Chain A, domain 4"},{"start":210,"end":388,"id":"3.30.420.40","name":"3.30.420.40"}]},"uniref50":"UniRef50_P11021","sequence":"MKLSLVAAMLLLLSAARAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGEEDTAEKDEL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P11021","disprot_id":"DP01938","ncbi_taxon_id":9606,"regions_counter":3,"creator":"cbassot","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":24,"region_id":"DP01938r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Conformation transitions of the polypeptide-binding pocket support an active substrate release from Hsp70s. <i> Yang J, Zong Y, Su J, Li H, Zhu H, Columbus L, Zhou L, Liu Q. </i> Nat Commun, 2017","statement":[{"text":"Schematic of human BiP domain structure. The positions for key elements are indicated. The first 24 residues (signal sequence) and the last 20 residues (largely disordered) are not colored","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"cbassot","start":1,"term_ontology":"IDPO","curator_name":"Claudio Bassot","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"6ASY"}],"reference_id":"29084938","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:44:16.151Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":654,"region_id":"DP01938r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Conformation transitions of the polypeptide-binding pocket support an active substrate release from Hsp70s. <i> Yang J, Zong Y, Su J, Li H, Zhu H, Columbus L, Zhou L, Liu Q. </i> Nat Commun, 2017","statement":[{"text":"Schematic of human BiP domain structure. The positions for key elements are indicated. The first 24 residues (signal sequence) and the last 20 residues (largely disordered) are not colored","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"cbassot","start":634,"term_ontology":"IDPO","curator_name":"Claudio Bassot","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7161-9028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"6ASY"}],"reference_id":"29084938","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:44:15.429Z"}}],"released":"2018_11","uniref100":"UniRef100_P11021","date":"2018-08-17T10:03:31.000Z","acc":"P11021","name":"Endoplasmic reticulum chaperone BiP","length":654,"organism":"Homo sapiens","dataset":["Autophagy-related proteins","Condensates-related proteins"],"UniParc":"UPI000016A9EF","genes":[{"name":{"value":"HSPA5","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:5238","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:5238"}}]},"synonyms":[{"value":"GRP78","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"2840249","url":"http://www.ncbi.nlm.nih.gov/pubmed/2840249","alternativeUrl":"https://europepmc.org/abstract/MED/2840249"}}]}]}],"alphafold_very_low_content":0.04434250764525994,"disorder_content":0.06880733944954129,"disprot_consensus":{"full":[{"start":1,"end":24,"type":"D"},{"start":634,"end":654,"type":"D"}],"Structural state":[{"start":1,"end":24,"type":"D"},{"start":634,"end":654,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":16,"end":172},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":344,"end":461},{"id":"PF02732","name":"ERCC4 domain","start":599,"end":718},{"id":"PF12826","name":"Helix-hairpin-helix motif","start":751,"end":797},{"id":"PF21210","name":"Putative ATP-dependent RNA helicase, helical bundle","start":215,"end":337}],"gene3D":[{"start":592,"end":733,"id":"3.40.50.10130","name":"3.40.50.10130"},{"start":734,"end":803,"id":"1.10.150.20","name":"5' to 3' exonuclease, C-terminal subdomain"},{"start":213,"end":339,"id":"1.20.1320.20","name":"hef helicase domain"},{"start":210,"end":479,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":3,"end":200,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_Q8TZH8","sequence":"MQYLRRDLIEPRVYQEVIYARCKEANCLVVLPTGLGKTLIAMLIADYRLSKYGGKVLMLAPTKPLAVQHAESFKKLFNIPPEKINVLTGELSPKQRAEVWKNSVVITATPQTVENDILTGRISLEDVVLLVFDEAHRAVGNYSYVFIAKEYLKTAKHPLVLGLTASPGSDEEKIREIVRNLGIERIEIRTESSPDVKPYVQKIAFEWVKVDLPGIYKEVRSILREMLKESLKPLAQFKLVSTYSPDISKKEVLQAGSKINQEVARGNYELGRLRMHQAKAVKLLHALELLETQGLTALRAYLKKLKEDKRTKSSKELMEDPRMRKVIYLLVQAKESGLDHPKMEKLKELVKEQLGKKPSSKIIVFTNYRDTGKKIVEELRSMGITAERFIGQASRKDDRGMSQREQKEVLDRFSRGEFNVLVATSVGEEGLDVPEVDLVVFYEPVPSAIRSIQRRGRTGRHRPGRVVILMAKGTRDEAYYWASRRKEKGMFDAIKKIARELEKLQRARIKAQGEEGKIHAGVEKSKGSVDVSKGKIAPLDAFLKPKKVENTEIRESKAVGKAAPQASEEKSAEKPKETTEELPIKPIFVRKPKGIVVYVDSRELRSGVPKHLRELGAEVEVRTLDVADYVVSEEVGIERKSANDFIQSIIDGRLFDQVERLKRAYEKPVIIIEGELYGIRNVHPNAIRGAIAAVTLDWGVPILFSSGPEETAQFIYLMAKREQEERKKEVRLRSEKKALTLAERQRLIVEGLPNVSATLAKRLLKHFGNVERVFTATEEELKEVEGIGPKKAREIRRVITGTLR","taxonomy":["Archaea","Euryarchaeota","Thermococci","Thermococcales","Thermococcaceae","Thermococcus"],"uniref90":"UniRef90_Q5JJ98","disprot_id":"DP01939","ncbi_taxon_id":69014,"regions_counter":13,"creator":"eficho","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":588,"region_id":"DP01939r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Multiple interactions of the intrinsically disordered region between the helicase and nuclease domains of the archaeal Hef protein. <i> Ishino S, Yamagami T, Kitamura M, Kodera N, Mori T, Sugiyama S, Ando T, Goda N, Tenno T, Hiroaki H, Ishino Y. </i> J Biol Chem, 2014","statement":[{"text":"We analyzed the interdomain region of Thermococcus kodakarensis Hef and demonstrated its disordered structure by CD, NMR, and high speed atomic force microscopy (AFM).","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"couzo","start":493,"term_ontology":"IDPO","curator_name":"Christos Ouzounis","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-0086-8657","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24947516","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":588,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Multiple interactions of the intrinsically disordered region between the helicase and nuclease domains of the archaeal Hef protein. <i> Ishino S, Yamagami T, Kitamura M, Kodera N, Mori T, Sugiyama S, Ando T, Goda N, Tenno T, Hiroaki H, Ishino Y. </i> J Biol Chem, 2014","statement":[{"text":"two-hybrid screen","type":"Table"}],"term_id":"GO:0005515","curator_id":"couzo","start":493,"term_ontology":"GO","curator_name":"Christos Ouzounis","reference_id":"24947516","version":3,"curator_orcid":"0000-0002-0086-8657","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"uniprot","id":"Q5JFJ4"}],"region_id":"DP01939r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":588,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Multiple interactions of the intrinsically disordered region between the helicase and nuclease domains of the archaeal Hef protein. <i> Ishino S, Yamagami T, Kitamura M, Kodera N, Mori T, Sugiyama S, Ando T, Goda N, Tenno T, Hiroaki H, Ishino Y. </i> J Biol Chem, 2014","statement":[{"text":"two-hybrid screen","type":"Table"}],"term_id":"GO:0005515","curator_id":"couzo","start":493,"term_ontology":"GO","curator_name":"Christos Ouzounis","reference_id":"24947516","version":3,"curator_orcid":"0000-0002-0086-8657","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"uniprot","id":"Q5JCW9"}],"region_id":"DP01939r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":588,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Multiple interactions of the intrinsically disordered region between the helicase and nuclease domains of the archaeal Hef protein. <i> Ishino S, Yamagami T, Kitamura M, Kodera N, Mori T, Sugiyama S, Ando T, Goda N, Tenno T, Hiroaki H, Ishino Y. </i> J Biol Chem, 2014","statement":[{"text":"two-hybrid screen","type":"Table"}],"term_id":"GO:0005515","curator_id":"couzo","start":493,"term_ontology":"GO","curator_name":"Christos Ouzounis","reference_id":"24947516","version":3,"curator_orcid":"0000-0002-0086-8657","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"uniprot","id":"Q5JG97"}],"region_id":"DP01939r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":588,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Multiple interactions of the intrinsically disordered region between the helicase and nuclease domains of the archaeal Hef protein. <i> Ishino S, Yamagami T, Kitamura M, Kodera N, Mori T, Sugiyama S, Ando T, Goda N, Tenno T, Hiroaki H, Ishino Y. </i> J Biol Chem, 2014","statement":[{"text":"two-hybrid screen","type":"Table"}],"term_id":"GO:0005515","curator_id":"couzo","start":493,"term_ontology":"GO","curator_name":"Christos Ouzounis","reference_id":"24947516","version":3,"curator_orcid":"0000-0002-0086-8657","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"uniprot","id":"Q5JF12"}],"region_id":"DP01939r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":588,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Multiple interactions of the intrinsically disordered region between the helicase and nuclease domains of the archaeal Hef protein. <i> Ishino S, Yamagami T, Kitamura M, Kodera N, Mori T, Sugiyama S, Ando T, Goda N, Tenno T, Hiroaki H, Ishino Y. </i> J Biol Chem, 2014","statement":[{"text":"two-hybrid screen","type":"Table"}],"term_id":"GO:0005515","curator_id":"couzo","start":493,"term_ontology":"GO","curator_name":"Christos Ouzounis","reference_id":"24947516","version":3,"curator_orcid":"0000-0002-0086-8657","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"uniprot","id":"Q5JJ48"}],"region_id":"DP01939r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":588,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Multiple interactions of the intrinsically disordered region between the helicase and nuclease domains of the archaeal Hef protein. <i> Ishino S, Yamagami T, Kitamura M, Kodera N, Mori T, Sugiyama S, Ando T, Goda N, Tenno T, Hiroaki H, Ishino Y. </i> J Biol Chem, 2014","statement":[{"text":"two-hybrid screen","type":"Table"}],"term_id":"GO:0005515","curator_id":"couzo","start":493,"term_ontology":"GO","curator_name":"Christos Ouzounis","reference_id":"24947516","version":3,"curator_orcid":"0000-0002-0086-8657","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"uniprot","id":"Q5JII4"}],"region_id":"DP01939r007","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":588,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Multiple interactions of the intrinsically disordered region between the helicase and nuclease domains of the archaeal Hef protein. <i> Ishino S, Yamagami T, Kitamura M, Kodera N, Mori T, Sugiyama S, Ando T, Goda N, Tenno T, Hiroaki H, Ishino Y. </i> J Biol Chem, 2014","statement":[{"text":"two-hybrid screen","type":"Table"}],"term_id":"GO:0005515","curator_id":"couzo","start":493,"term_ontology":"GO","curator_name":"Christos Ouzounis","reference_id":"24947516","version":3,"curator_orcid":"0000-0002-0086-8657","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"uniprot","id":"Q5JDD8"}],"region_id":"DP01939r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":588,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Multiple interactions of the intrinsically disordered region between the helicase and nuclease domains of the archaeal Hef protein. <i> Ishino S, Yamagami T, Kitamura M, Kodera N, Mori T, Sugiyama S, Ando T, Goda N, Tenno T, Hiroaki H, Ishino Y. </i> J Biol Chem, 2014","statement":[{"text":"two-hybrid screen","type":"Table"}],"term_id":"GO:0005515","curator_id":"couzo","start":493,"term_ontology":"GO","curator_name":"Christos Ouzounis","reference_id":"24947516","version":3,"curator_orcid":"0000-0002-0086-8657","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"uniprot","id":"Q52500"}],"region_id":"DP01939r009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":493,"end":593,"reference_id":"39719827","reference_source":"pmid","reference_html":"Revealing an origin of temperature-dependent structural change in intrinsically disordered proteins. <i> Inoue R, Oda T, Nakagawa H, Tominaga T, Ikegami T, Konuma T, Iwase H, Kawakita Y, Sato M, Sugiyama M. </i> Biophys J, 2025","date":"2025-04-22T11:14:13.241Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006301","ec_ontology":"ECO","ec_name":"protein thermal shift assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP01939r010","statement":[{"text":"Although the detailed temperature dependence of Rg was unclear only from the SANS results owing to large error bars, at least a tendency for a reduction in Rg was observed with increasing temperature (Figs. S2 and S3). In the case of unfolding of\nFGPs by an increment of temperature, the collapse of secondary structures such as the a helix and b sheet occurs, leading to an increment of Rg with increasing temperature (27). This process is normally irreversible in FGPs, whereas heat-induced structural changes are reversible in IDPs (3).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-02T14:26:41.404Z"}},{"start":493,"end":593,"reference_id":"39719827","reference_source":"pmid","reference_html":"Revealing an origin of temperature-dependent structural change in intrinsically disordered proteins. <i> Inoue R, Oda T, Nakagawa H, Tominaga T, Ikegami T, Konuma T, Iwase H, Kawakita Y, Sato M, Sugiyama M. </i> Biophys J, 2025","date":"2025-02-27T08:14:17.044Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006200","ec_ontology":"ECO","ec_name":"circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":"increased","value":313}],"region_id":"DP01939r011","statement":[{"text":"As shown in Fig. 2 a, only a broad band at 222 nm was observed in the\nCD spectra. Therefore, we focused on the temperature dependence of ellipticity at 222 nm (q222nm). The variation of the q222nm value against temperature was almost flat up to 313 K, whereas a reduction of the q222nm value was\nobserved in the temperature range above 313 K. (Fig. 2 b). The transition temperature (Ttra), which ranged from 313 to 323 K, was observed in the SAXS and CD measurements. Structural changes in other IDPs have been observed in similar temperature ranges (2).","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":10,"db":"ChEBI","id":"46756 ","statements":[{"type":"Methods","text":"A solution of 40 μM Hef-IDR in a buffer solution comprising 10 mM HEPES (pH 7.5), 100 mM NaCl, and 0.1 mM EDTA was analyzed. "}],"entry_name":"HEPES"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":100,"db":"ChEBI","id":"26710","statements":[{"type":"Methods","text":"A solution of 40 μM Hef-IDR in a buffer solution comprising 10 mM HEPES (pH 7.5), 100 mM NaCl, and 0.1 mM EDTA was analyzed. "}],"entry_name":"sodium chloride"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":0.1,"db":"ChEBI","id":"4735","statements":[{"type":"Methods","text":"A solution of 40 μM Hef-IDR in a buffer solution comprising 10 mM HEPES (pH 7.5), 100 mM NaCl, and 0.1 mM EDTA was analyzed. "}],"entry_name":"ethylenediaminetetraacetic acid"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-19T16:26:34.784Z"}},{"start":493,"end":593,"reference_id":"39719827","reference_source":"pmid","reference_html":"Revealing an origin of temperature-dependent structural change in intrinsically disordered proteins. <i> Inoue R, Oda T, Nakagawa H, Tominaga T, Ikegami T, Konuma T, Iwase H, Kawakita Y, Sato M, Sugiyama M. </i> Biophys J, 2025","date":"2025-02-26T11:42:11.029Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP01939r012","statement":[{"text":"Although the 13C chemical shifts have been corrected by the sodium trimethylsilylpropanesulfonate (DSS) peak, the chemical shifts of both 13C0 and 13Ca shifted upfield with increasing temperature. It was reported that these chemical shifts in IDPs exhibited temperature dependency (31,32); hence, we focused on the largest differences in the 13Ca and 13C0 chemical shifts between 298 and 349 K. Fig. 3, c and d, shows a histogram of the difference in the 13Ca chemical shifts between 298 and 349 K (D13Ca 349–298K) and the 13C0 chemical shifts between 298 and 349 K (D13C0 349–298K), respectively.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-19T16:35:45.224Z"}},{"start":493,"end":593,"reference_id":"39719827","reference_source":"pmid","reference_html":"Revealing an origin of temperature-dependent structural change in intrinsically disordered proteins. <i> Inoue R, Oda T, Nakagawa H, Tominaga T, Ikegami T, Konuma T, Iwase H, Kawakita Y, Sato M, Sugiyama M. </i> Biophys J, 2025","date":"2025-02-27T08:11:07.778Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006214","ec_ontology":"ECO","ec_name":"small-angle neutron scattering evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":null,"value":298,"statements":[{"type":"Methods","text":"The resolution function was determined from vanadium measurements at 298 K, and the energy resolution (δE) was calculated to be 12 μeV, covering the timescale from 5 to 200 ps. "}]}],"region_id":"DP01939r013","statement":[{"text":"As the scattering cross section of a hydrogen (H) atom is significantly larger than those of other constituent atoms in Hef-IDR, the observed QENS profile is mainly dominated by incoherent dynamic scattering laws. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-19T16:35:50.087Z"}}],"released":"2018_11","uniref100":"UniRef100_Q5JJ98","date":"2018-08-17T10:10:53.000Z","acc":"Q5JJ98","name":"Helicase-associated endonuclease for fork-structured DNA","length":804,"organism":"Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)","dataset":[],"UniParc":"UPI00004A3432","genes":[{"olnNames":[{"value":"TK1021","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAD85210.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAD85210.1"}}]}]}],"alphafold_very_low_content":0.11318407960199005,"disorder_content":0.1256218905472637,"disprot_consensus":{"full":[{"start":493,"end":593,"type":"D"}],"Structural state":[{"start":493,"end":593,"type":"D"}],"Molecular function":[{"start":493,"end":588,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00350","name":"Dynamin family","start":61,"end":221},{"id":"PF12763","name":"EH domain","start":448,"end":537},{"id":"PF16880","name":"N-terminal EH-domain containing protein","start":25,"end":56},{"id":"PF18150","name":"Domain of unknown function (DUF5600)","start":288,"end":394}],"gene3D":[{"start":436,"end":539,"id":"1.10.238.10","name":"EF-hand"},{"start":61,"end":285,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":24,"end":386,"id":"1.10.268.20","name":"1.10.268.20"}]},"uniref50":"UniRef50_Q8BH64","sequence":"MFSWLKKGGARGQRPEAIRTVTSSLKELYRTKLLPLEEHYRFGSFHSPALEDADFDGKPMVLVAGQYSTGKTSFIQYLLEQEVPGSRVGPEPTTDCFVAVMHGETEGTVPGNALVVDPEKPFRKLNPFGNTFLNRFMCAQLPNQVLESISIIDTPGILSGAKQRVSRGYDFPAVLRWFAERVDLIILLFDAHKLEISDEFSEAIGALRGHEDKIRVVLNKADMVETQQLMRVYGALMWALGKVVGTPEVLRVYIGSFWSQPLLVPDNRRLFELEEQDLFRDIQGLPRHAALRKLNDLVKRARLVRVHAYIISYLKKEMPTVFGKENKKKQLILKLPVIFAKIQLEHHISPGDFPDCQKMQELLMAHDFTKFHSLKPKLLEALDDMLAQDIAKLMPLLRQEELESVEAGVQGGAFEGTRMGPFVERGPDEAIEDGEEGSEDDAEWVVTKDKSKYDEIFYNLAPADGKLSGSKAKTWMVGTKLPNSVLGRIWKLSDVDRDGMLDDEEFALASHLIEAKLEGHGLPTNLPRRLVPPSKRRQKGSAE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q8BH64","disprot_id":"DP01940","ncbi_taxon_id":10090,"regions_counter":3,"creator":"achasapi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":18,"region_id":"DP01940r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Architectural and mechanistic insights into an EHD  ATPase involved in membrane remodelling. <i> Daumke O, Lundmark R, Vallis Y, Martens S, Butler PJ, McMahon HT. </i> Nature, 2007","statement":[{"text":"The helical domain is composed of helix a1 and a2 from the N-terminal region (residues 18–55, which follow disordered residues 1–18)","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"achasapi","start":1,"term_ontology":"IDPO","curator_name":"Anastasia Chasapi","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-1986-5007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2QPT"}],"reference_id":"17914359","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":130,"region_id":"DP01940r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Architectural and mechanistic insights into an EHD  ATPase involved in membrane remodelling. <i> Daumke O, Lundmark R, Vallis Y, Martens S, Butler PJ, McMahon HT. </i> Nature, 2007","statement":[{"text":"Residues 110–130, which are distal to switch I, are disordered and contain predicted EH-domain binding motifs, KPFxxxNPF","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"achasapi","start":110,"term_ontology":"IDPO","curator_name":"Anastasia Chasapi","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-1986-5007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2QPT"}],"reference_id":"17914359","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":130,"region_id":"DP01940r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Studies on operations of recurrent gastric cancer cases. <i> Iwasa H, Imamura K, Ishii T, Sekizuka H. </i> Bull Tokyo Med Dent Univ, 1972","statement":[{"text":"Superposition showing the KPFxxxNPF loop from EHD2 Q410A (blue, pdb 2QPT) and EHD2 L5M Q410A (lightblue)","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"achasapi","start":110,"term_ontology":"IDPO","curator_name":"Anastasia Chasapi","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-1986-5007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4CID"}],"reference_id":"4508342","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q8BH64","date":"2018-08-17T12:35:46.000Z","acc":"Q8BH64","name":"EH domain-containing protein 2","length":543,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000EB96C","genes":[{"name":{"value":"Ehd2","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:2154274","url":"http://www.informatics.jax.org/marker/MGI:2154274"}}]}}],"alphafold_very_low_content":0.06813996316758748,"disorder_content":0.0718232044198895,"disprot_consensus":{"full":[{"start":1,"end":18,"type":"D"},{"start":110,"end":130,"type":"D"}],"Structural state":[{"start":1,"end":18,"type":"D"},{"start":110,"end":130,"type":"D"}]}},{"features":{"pfam":[{"id":"PF06733","name":"DEAD_2","start":88,"end":189},{"id":"PF13307","name":"Helicase C-terminal domain","start":389,"end":540}],"gene3D":[{"start":5,"end":339,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":193,"end":300,"id":"1.10.275.30","name":"1.10.275.30"},{"start":355,"end":551,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_Q4JC68","sequence":"MLKLRDWQEKLKDKVIEGLRNNFLVALNAPTGSGKTLFSLLVSLEVKPKVLFVVRTHNEFYPIYRDLTKIREKRNITFSFLVGKPSSCLYAEKGAESEDIPCKYCELKGSIVEVKTDDSPLSLVKKLKKDGLQDKFCPYYSLLNSLYKADVIALTYPYFFIDRYREFIDIDLREYMIVIDEAHNLDKVNELEERSLSEITIQMAIKQSKSEESRRILSKLLNQLREVVLPDEKYIKVENVPKLSKEELEILADDYEDIRKDSLKQGKVNKIHIGSILRFFSLLSIGSFIPFSYSKRLVIKNPEISYYLNLLNDNELSIILMSGTLPPREYMEKVWGIKRNMLYLDVEREIQKRVSGSYECYIGVDVTSKYDMRSDNMWKRYADYLLKIYFQAKANVLVVFPSYEIMDRVMSRISLPKYVESEDSSVEDLYSAISANNKVLIGSVGKGKLAEGIELRNNDRSLISDVVIVGIPYPPPDDYLKILAQRVSLKMNRENEEFLFKIPALVTIKQAIGRAIRDVNDKCNVWLLDKRFESLYWKKNLKCLNANKMKL","taxonomy":["Archaea","Crenarchaeota","Thermoprotei","Sulfolobales","Sulfolobaceae","Sulfolobus"],"uniref90":"UniRef90_Q4JC68","disprot_id":"DP01941","ncbi_taxon_id":330779,"regions_counter":3,"creator":"jmanso","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":143,"region_id":"DP01941r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations. <i> Fan L, Fuss JO, Cheng QJ, Arvai AS, Hammel M, Roberts VA, Cooper PK, Tainer JA. </i> Cell, 2008","statement":[{"text":"Disordered regions (1-9, 72-76, 89-96, 98-144) show the 4Fe-4S cluster acts in ordering the 4FeS domain, the Arch interface, and parts of HD1.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jmanso","start":99,"term_ontology":"IDPO","curator_name":"Jose A Manso","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3CRW"}],"reference_id":"18510924","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":143,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations. <i> Fan L, Fuss JO, Cheng QJ, Arvai AS, Hammel M, Roberts VA, Cooper PK, Tainer JA. </i> Cell, 2008","term_id":"IDPO:0000011","curator_id":"jmanso","start":99,"term_ontology":"IDPO","curator_name":"Jose A Manso","reference_id":"18510924","version":2,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01941r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":143,"term_name":"metal ion binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations. <i> Fan L, Fuss JO, Cheng QJ, Arvai AS, Hammel M, Roberts VA, Cooper PK, Tainer JA. </i> Cell, 2008","term_id":"GO:0046872","curator_id":"jmanso","start":99,"term_ontology":"GO","curator_name":"Jose A Manso","reference_id":"18510924","version":3,"curator_orcid":"0000-0002-2565-6239","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01941r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q4JC68","date":"2018-08-17T13:20:19.000Z","acc":"Q4JC68","name":"ATP-dependent DNA helicase Saci_0192","length":551,"organism":"Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)","dataset":[],"UniParc":"UPI000055219D","genes":[{"olnNames":[{"value":"Saci_0192"}]}],"alphafold_very_low_content":0,"disorder_content":0.08166969147005444,"disprot_consensus":{"full":[{"start":99,"end":143,"type":"T"}],"Structural state":[{"start":99,"end":143,"type":"D"}],"Structural transition":[{"start":99,"end":143,"type":"T"}],"Molecular function":[{"start":99,"end":143,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00010","name":"Helix-loop-helix DNA-binding domain","start":121,"end":171}],"gene3D":[{"start":121,"end":176,"id":"4.10.280.10","name":"Helix-loop-helix DNA-binding domain"}]},"uniref50":"UniRef50_Q02067","sequence":"MESSAKMESGGAGQQPQPQPQQPFLPPAACFFATAAAAAAAAAAAAAQSAQQQQQQQQQQQQAPQLRPAADGQPSGGGHKSAPKQVKRQRSSSPELMRCKRRLNFSGFGYSLPQQQPAAVARRNERERNRVKLVNLGFATLREHVPNGAANKKMSKVETLRSAVEYIRALQQLLDEHDAVSAAFQAGVLSPTISPNYSNDLNSMAGSPVSSYSSDEGSYDPLSPEEQELLDFTNWF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P50553","disprot_id":"DP01942","ncbi_taxon_id":9606,"regions_counter":3,"creator":"thorvath","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":236,"region_id":"DP01942r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Fragment-Based NMR Study of the Conformational Dynamics in the bHLH Transcription Factor Ascl1. <i> Baronti L, Hošek T, Gil-Caballero S, Raveh-Amit H, Calçada EO, Ayala I, Dinnyés A, Felli IC, Pierattelli R, Brutscher B. </i> Biophys J, 2017","statement":[{"text":"Ascl1 forms an extended polypeptide chain lacking persistent tertiary interactions, similar to a string of several loosely coupled peptide segments with a high propensity to adopt α-helical conformation","type":"Conclusion"}],"term_id":"IDPO:0000002","curator_id":"thorvath","start":1,"term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"28402879","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":236,"term_name":"nucleic acid binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"a central bHLH domain (residues 122–179) that is responsible for homo- and heterodimerization of the protein, as well as for DNA binding through interaction of positively charged residues (basic region) with the negatively charged DNA backbone","type":"Introduction"}],"curator_id":"thorvath","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Horvath","reference_id":"28402879","version":3,"reference_html":"Fragment-Based NMR Study of the Conformational Dynamics in the bHLH Transcription Factor Ascl1. <i> Baronti L, Hošek T, Gil-Caballero S, Raveh-Amit H, Calçada EO, Ayala I, Dinnyés A, Felli IC, Pierattelli R, Brutscher B. </i> Biophys J, 2017","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0003676","ec_id":"ECO:0006165","region_id":"DP01942r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":236,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Phosphorylation through proline-directed kinases of these serine residues contributes to the regulation of Ascl1 activity","type":"Introduction"}],"curator_id":"thorvath","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Horvath","reference_id":"28402879","version":3,"reference_html":"Fragment-Based NMR Study of the Conformational Dynamics in the bHLH Transcription Factor Ascl1. <i> Baronti L, Hošek T, Gil-Caballero S, Raveh-Amit H, Calçada EO, Ayala I, Dinnyés A, Felli IC, Pierattelli R, Brutscher B. </i> Biophys J, 2017","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP01942r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P50553","date":"2018-08-17T13:50:19.000Z","acc":"P50553","name":"Achaete-scute homolog 1","length":236,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000047566","genes":[{"name":{"value":"ASCL1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:738","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:738"}}]},"synonyms":[{"value":"ASH1"},{"value":"BHLHA46","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:738","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:738"}}]},{"value":"HASH1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8390674","url":"http://www.ncbi.nlm.nih.gov/pubmed/8390674","alternativeUrl":"https://europepmc.org/abstract/MED/8390674"}}]}]}],"alphafold_very_low_content":0.13135593220338984,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":236,"type":"D"}],"Structural state":[{"start":1,"end":236,"type":"D"}],"Molecular function":[{"start":1,"end":236,"type":"F"}]}},{"features":{"pfam":[{"id":"PF15925","name":"SOSS complex subunit C","start":18,"end":101}]},"uniref50":"UniRef50_Q9NRY2","sequence":"MAANSSGQGFQNKNRVAILAELDKEKRKLLMQNQSSTNHPGASIALSRPSLNKDFRDHAEQQHIAAQQKAALQHAHAHSSGYFITQDSAFGNLILPVLPRLDPE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9NRY2","disprot_id":"DP01943","ncbi_taxon_id":9606,"regions_counter":1,"creator":"jlecle","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":62,"region_id":"DP01943r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis of SOSS1 complex assembly and recognition of ssDNA. <i> Ren W, Chen H, Sun Q, Tang X, Lim SC, Huang J, Song H. </i> Cell Rep, 2014","statement":[{"text":"Several regions of the polypeptide chains are disordered, namely, residues 1–32 and 499–500 in SOSSAN, residues 1–4, 11–18, 28–37, 71–81, 87–90, and 110–211 in SOSSB1, and residues 1–62 and 102–104 in SOSSC.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jlecle","start":1,"term_ontology":"IDPO","curator_name":"Jeremy Y Leclercq","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0372-3277","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4OWT"}],"reference_id":"24630995","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9NRY2","date":"2018-08-17T15:25:47.000Z","acc":"Q9NRY2","name":"SOSS complex subunit C","length":104,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000006FF52","genes":[{"name":{"value":"INIP"},"synonyms":[{"value":"C9orf80"},{"value":"SSBIP1"}],"orfNames":[{"value":"HSPC043"},{"value":"HSPC291"}]}],"alphafold_very_low_content":0.18269230769230768,"disorder_content":0.5961538461538461,"disprot_consensus":{"full":[{"start":1,"end":62,"type":"D"}],"Structural state":[{"start":1,"end":62,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00027","name":"Cyclic nucleotide-binding domain","start":172,"end":256},{"id":"PF00027","name":"Cyclic nucleotide-binding domain","start":293,"end":383},{"id":"PF02197","name":"Regulatory subunit of type II PKA R-subunit","start":8,"end":44}],"gene3D":[{"start":112,"end":255,"id":"2.60.120.10","name":"Jelly Rolls"},{"start":256,"end":407,"id":"2.60.120.10","name":"Jelly Rolls"},{"start":1,"end":43,"id":"1.20.890.10","name":"cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain"}]},"uniref50":"UniRef50_P31323","sequence":"MSIEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQENERKGAARFGHEGRTWGDAGAAAGGGIPSKGVNFAEEPMRSDSENGEEEEAAEAGAFNAPVINRFTRRASVCAEAYNPDEEEDDAESRIIHPKTDDQRNRLQEACKDILLFKNLDPEQMSQVLDAMFEKLVKEGEHVIDQGDDGDNFYVIDRGTFDIYVKCDGVGRCVGNYDNRGSFGELALMYNTPRAATITATSPGALWGLDRVTFRRIIVKNNAKKRKMYESFIESLPFLKSLEVSERLKVVDVIGTKVYNDGEQIIAQGDLADSFFIVESGEVKITMKRKGKSEVEENGAVEIARCFRGQYFGELALVTNKPRAASAHAIGTVKCLAMDVQAFERLLGPCMEIMKRNIATYEEQLVALFGTNMDIVEPTA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P31323","disprot_id":"DP01944","ncbi_taxon_id":10090,"regions_counter":2,"creator":"jlecle","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":103,"region_id":"DP01944r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure and allostery of the PKA RIIβ tetrameric holoenzyme. <i> Zhang P, Smith-Nguyen EV, Keshwani MM, Deal MS, Kornev AP, Taylor SS. </i> Science, 2012","statement":[{"text":"Although residues 1 to 103, 122 to 129, and 394 to 416 of RIIβ and residues 1 to 13 of C are missing in the electron density, we validated by using gel electrophoresis that the full-length RIIβ2:C2 complex is in the protein crystal. The absence of density for the N-terminal D/D domain and the following linker is likely related to the flexible nature of this region.","type":"Article"}],"term_id":"IDPO:0000002","curator_id":"jlecle","start":1,"term_ontology":"IDPO","curator_name":"Jeremy Y Leclercq","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0372-3277","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3TNP"}],"reference_id":"22323819","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":416,"region_id":"DP01944r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure and allostery of the PKA RIIβ tetrameric holoenzyme. <i> Zhang P, Smith-Nguyen EV, Keshwani MM, Deal MS, Kornev AP, Taylor SS. </i> Science, 2012","statement":[{"text":"Although residues 1 to 103, 122 to 129, and 394 to 416 of RIIβ and residues 1 to 13 of C are missing in the electron density, we validated by using gel electrophoresis that the full-length RIIβ2:C2 complex is in the protein crystal. The absence of density for the N-terminal D/D domain and the following linker is likely related to the flexible nature of this region.","type":"Article"}],"term_id":"IDPO:0000002","curator_id":"jlecle","start":394,"term_ontology":"IDPO","curator_name":"Jeremy Y Leclercq","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0372-3277","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3TNP"}],"reference_id":"22323819","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P31324","date":"2018-08-17T15:53:26.000Z","acc":"P31324","name":"cAMP-dependent protein kinase type II-beta regulatory subunit","length":416,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000EAD64","genes":[{"name":{"value":"Prkar2b"}}],"alphafold_very_low_content":0.13942307692307693,"disorder_content":0.30288461538461536,"disprot_consensus":{"full":[{"start":1,"end":103,"type":"D"},{"start":394,"end":416,"type":"D"}],"Structural state":[{"start":1,"end":103,"type":"D"},{"start":394,"end":416,"type":"D"}]}},{"features":{"pfam":[{"id":"PF27970","name":"LEA protein 1/2/D7/Stress-induced protein KIN2","start":95,"end":159}]},"uniref50":"UniRef50_A0A0C4FST8","sequence":"MASHGQSYRAGEATGRAEEKADQMMGKTRGATEAMKNKAQQAKDKTMETAQAAKEKTSEKAYEAKDKTSNMAQSAKGQAQQSKDQTGSFASDKAQAAKDKAYQAAQATKEKASDMTEYAKETAEAGKEKTGGILQRTGEQVKSMAQGAADAVKNTFGMGEPEEDDPIKTTRP","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","Caryophyllales","Amaranthaceae","Amaranthus"],"uniref90":"UniRef90_A0A2K8FR49","disprot_id":"DP01945","ncbi_taxon_id":117272,"regions_counter":2,"creator":"achasapi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":172,"region_id":"DP01945r001","released":"2022_03","ec_id":"ECO:0006198","reference_html":"Insights on Structure and Function of a Late Embryogenesis Abundant Protein from <i>Amaranthus cruentus</i>: An Intrinsically Disordered Protein Involved in Protection against Desiccation, Oxidant Conditions, and Osmotic Stress. <i> Saucedo AL, Hernández-Domínguez EE, de Luna-Valdez LA, Guevara-García AA, Escobedo-Moratilla A, Bojorquéz-Velázquez E, Del Río-Portilla F, Fernández-Velasco DA, Barba de la Rosa AP. </i> Front Plant Sci, 2017","statement":[{"text":"Narrow signal distribution in amide region, between 6.5 and 8.5 ppm, strongly suggest the lack of a well-defined tridimentional structure distintive of intrinsically disordered proteins.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"achasapi","start":1,"term_ontology":"IDPO","curator_name":"Anastasia Chasapi","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1986-5007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28439280","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":172,"region_id":"DP01945r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Insights on Structure and Function of a Late Embryogenesis Abundant Protein from <i>Amaranthus cruentus</i>: An Intrinsically Disordered Protein Involved in Protection against Desiccation, Oxidant Conditions, and Osmotic Stress. <i> Saucedo AL, Hernández-Domínguez EE, de Luna-Valdez LA, Guevara-García AA, Escobedo-Moratilla A, Bojorquéz-Velázquez E, Del Río-Portilla F, Fernández-Velasco DA, Barba de la Rosa AP. </i> Front Plant Sci, 2017","statement":[{"text":"The lack of a temperature-induced transition strongly suggests that if secondary structure segments are formed, those segments are fluctuating and do not participate in the compact core structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"achasapi","start":1,"term_ontology":"IDPO","curator_name":"Anastasia Chasapi","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1986-5007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28439280","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_A0A2K8FR49","date":"2018-08-17T16:28:20.000Z","acc":"A0A2K8FR49","name":"LEA","length":172,"organism":"Amaranthus cruentus","dataset":[],"UniParc":"UPI000CE5EEF2","genes":[],"alphafold_very_low_content":0.20348837209302326,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":172,"type":"D"}],"Structural state":[{"start":1,"end":172,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00005","name":"ABC transporter","start":335,"end":482},{"id":"PF00498","name":"FHA domain","start":29,"end":92},{"id":"PF00498","name":"FHA domain","start":230,"end":293},{"id":"PF01061","name":"ABC-2 type transporter","start":596,"end":810}],"gene3D":[{"start":2,"end":98,"id":"2.60.200.20","name":"2.60.200.20"},{"start":214,"end":309,"id":"2.60.200.20","name":"2.60.200.20"},{"start":310,"end":554,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_O65934","sequence":"MPMSQPAAPPVLTVRYEGSERTFAAGHDVVVGRDLRADVRVAHPLISRAHLLLRFDQGRWVAIDNGSLNGLYLNNRRVPVVDIYDAQRVHIGNPDGPALDFEVGRHRGSAGRPPQTTSIRLPNLSAGAWPTDGPPQTGTLGSGQLQQLPPATTRIPAAPPSGPQPRYPTGGQQLWPPSGPQRAPQIYRPPTAAPPPAGARGGTEAGNLATSMMKILRPGRLTGELPPGAVRIGRANDNDIVIPEVLASRHHATLVPTPGGTEIRDNRSINGTFVNGARVDAALLHDGDVVTIGNIDLVFADGTLARREENLLETRVGGLDVRGVTWTIDGDKTLLDGISLTARPGMLTAVIGPSGAGKSTLARLVAGYTHPTDGTVTFEGHNVHAEYASLRSRIGMVPQDDVVHGQLTVKHALMYAAELRLPPDTTKDDRTQVVARVLEELEMSKHIDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDRQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLLAPGGKTAFCGPPTQIGPVMGTTNWADIFSTVADDPDAAKARYLARTGPTPPPPPVEQPAELGDPAHTSLFRQFSTIARRQLRLIVSDRGYFVFLALLPFIMGALSMSVPGDVGFGFPNPMGDAPNEPGQILVLLNVGAVFMGTALTIRDLIGERAIFRREQAVGLSTTAYLIAKVCVYTVLAVVQSAIVTVIVLVGKGGPTQGAVALSKPDLELFVDVAVTCVASAMLGLALSAIAKSNEQIMPLLVVAVMSQLVFSGGMIPVTGRVPLDQMSWVTPARWGFAASAATVDLIKLVPGPLTPKDSHWHHTASAWWFDMAMLVALSVIYVGFVRWKIRLKAC","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"uniref90":"UniRef90_O65934","disprot_id":"DP01947","ncbi_taxon_id":83332,"regions_counter":5,"creator":"thorvath","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":230,"region_id":"DP01947r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Biophysical Characterization of the Tandem FHA Domain Regulatory Module from the Mycobacterium tuberculosis ABC Transporter Rv1747. <i> Heinkel F, Shen L, Richard-Greenblatt M, Okon M, Bui JM, Gee CL, Gay LM, Alber T, Av-Gay Y, Gsponer J, McIntosh LP. </i> Structure, 2018","statement":[{"text":"In addition to lacking any predominant secondary structure, the linker residues exhibited MICS-calculated random coil index squared order parameters (RCI-S2) indicative of conformational disorder","type":"Introduction"}],"term_id":"IDPO:0000002","curator_id":"thorvath","start":104,"term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"29861345","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:05:14.728Z"}},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":230,"term_name":"protein binding","start":104,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"FHA-1 and FHA-2 Bind the Phosphorylated Linker to Form Inter- and Intramolecular Complexes","type":"Results"},{"text":"FHA-2 Exhibits Larger NMR Spectral Perturbations than FHA-1 upon Phosphopeptide Binding\n","type":"Results"},{"text":"The NMR-monitored titration experiments also provide insights into the mechanism of phosphopeptide binding. When mapped onto the structures of FHA-1 and FHA-2, residues showing pronounced amide chemical shift perturbations upon addition of either the pT152 or pT210 peptides cluster near the canonical FHA domain binding interface (Figures 4B–4D). However, a visual comparison of the 15 N-HSQC titration spectra presented in Figures 4A, S4, and S5 shows clear differences in the effects of the peptides on the two FHA domains. In the case of FHA-1, only a relatively small number of amides had perturbed NMR signals and, of those, most exhibited progressive chemical shift changes upon titration with either phosphopeptide","type":"Results"},{"text":"Overall, our NMR titrations reveal that pT152 and pT210 phosphopeptide binding leads to significantly more amides showing larger chemical shift perturbations and exchange broadening in FHA-2 compared with FHA-1. ","type":"Results"},{"text":"FHA-1 and FHA-2 Bind the Phosphorylated Linker to Form Inter- and Intramolecular Complexes","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"29861345","version":4,"reference_html":"Biophysical Characterization of the Tandem FHA Domain Regulatory Module from the Mycobacterium tuberculosis ABC Transporter Rv1747. <i> Heinkel F, Shen L, Richard-Greenblatt M, Okon M, Bui JM, Gee CL, Gay LM, Alber T, Av-Gay Y, Gsponer J, McIntosh LP. </i> Structure, 2018","date":"2023-12-05T17:19:21.142Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP01947r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":152,"end":152,"position":"Specific residue","statements":[{"type":"Abstract","text":"Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting Forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr)."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":210,"end":210,"position":"Specific residue","statements":[{"type":"Abstract","text":"Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting Forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr)."}]}],"curator_orcid":"0000-0002-0341-4888","interaction_partner":[{"db":"UniProt","id":"O65934","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:13:57.927Z"}},{"start":104,"end":230,"reference_id":"29861345","reference_source":"pmid","reference_html":"Biophysical Characterization of the Tandem FHA Domain Regulatory Module from the Mycobacterium tuberculosis ABC Transporter Rv1747. <i> Heinkel F, Shen L, Richard-Greenblatt M, Okon M, Bui JM, Gee CL, Gay LM, Alber T, Av-Gay Y, Gsponer J, McIntosh LP. </i> Structure, 2018","date":"2023-12-05T17:13:22.915Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":152,"end":152,"position":"Specific residue","statements":[{"type":"Abstract","text":"Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting Forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr)."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":210,"end":210,"position":"Specific residue"}],"region_id":"DP01947r003","statement":[{"text":"Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting Forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr).","type":"Abstract"},{"text":"Rv1747 Regulatory Module Is Composed of Independent FHA-1 and FHA-2 Domains Joined by a Disordered Linker","type":"Results"},{"text":"Collectively, these data demonstrate that the Rv1747 regulatory module has a beads-on-a-string organization with two structurally independent FHA domains joined by an ID linker.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:13:59.814Z"}},{"start":150,"end":154,"reference_id":"29861345","reference_source":"pmid","reference_html":"Biophysical Characterization of the Tandem FHA Domain Regulatory Module from the Mycobacterium tuberculosis ABC Transporter Rv1747. <i> Heinkel F, Shen L, Richard-Greenblatt M, Okon M, Bui JM, Gee CL, Gay LM, Alber T, Av-Gay Y, Gsponer J, McIntosh LP. </i> Structure, 2018","date":"2023-12-05T17:25:58.200Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01947r004","statement":[{"text":"NMR spectral perturbations resulting from the single-site phosphorylation of the T152A and T210A variants provided evi- dence for differential interactions of the two FHA domains and the two linker phospho-acceptors (Figures S10B and S10C). In the case of the Rv17471-213 constructs, phosphorylation at pT152 yielded only small chemical shift changes of diagnostic amides relative to the unmodified protein, whereas phosphorylation at pT210 caused changes resembling those resulting from double phosphorylation of the wild-type protein.","type":"Results"},{"text":"Phosphorylation site corresponding to T152.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:14:02.728Z"}},{"start":208,"end":212,"reference_id":"29861345","reference_source":"pmid","reference_html":"Biophysical Characterization of the Tandem FHA Domain Regulatory Module from the Mycobacterium tuberculosis ABC Transporter Rv1747. <i> Heinkel F, Shen L, Richard-Greenblatt M, Okon M, Bui JM, Gee CL, Gay LM, Alber T, Av-Gay Y, Gsponer J, McIntosh LP. </i> Structure, 2018","date":"2023-12-05T17:26:23.261Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP01947r005","statement":[{"text":"NMR spectral perturbations resulting from the single-site phosphorylation of the T152A and T210A variants provided evi- dence for differential interactions of the two FHA domains and the two linker phospho-acceptors (Figures S10B and S10C). In the case of the Rv17471-213 constructs, phosphorylation at pT152 yielded only small chemical shift changes of diagnostic amides relative to the unmodified protein, whereas phosphorylation at pT210 caused changes resembling those resulting from double phosphorylation of the wild-type protein.","type":"Results"},{"text":"Phosphorylation site corresponding to T210.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:14:00.945Z"}}],"released":"2018_11","uniref100":"UniRef100_O65934","date":"2018-08-17T18:08:06.000Z","acc":"O65934","name":"ABC transporter ATP-binding/permease protein Rv1747","length":865,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","dataset":["Condensates-related proteins"],"UniParc":"UPI00000D4FE6","genes":[{"olnNames":[{"value":"Rv1747"}]}],"alphafold_very_low_content":0.15953757225433526,"disorder_content":0.14682080924855492,"disprot_consensus":{"full":[{"start":104,"end":230,"type":"D"}],"Structural state":[{"start":104,"end":230,"type":"D"}],"Molecular function":[{"start":104,"end":230,"type":"F"}],"Disorder function":[{"start":104,"end":230,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03846","name":"Cell division inhibitor SulA","start":55,"end":153}],"gene3D":[{"start":43,"end":161,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_Q9HZJ8","sequence":"MQTSHSLPSAQLPLFQEAFWASNGAPLLDDVIDSPSSASIEEPAAFSELSLSGLPGHCLTLLAPILRELSEEQDARWLTLIAPPASLTHEWLRRAGLNRERILLLQAKDNAAALALSCEALRLGRSHTVVSWLEPLSRAARKQLSRAAQLGQAQSLNIRLG","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Pseudomonadales","Pseudomonadaceae","Pseudomonas"],"uniref90":"UniRef90_Q9HZJ8","disprot_id":"DP01948","ncbi_taxon_id":208964,"regions_counter":1,"creator":"achasapi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":42,"region_id":"DP01948r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the SOS cell division inhibitor SulA and in complex with FtsZ. <i> Cordell SC, Robinson EJ, Lowe J. </i> Proc Natl Acad Sci U S A, 2003","statement":[{"text":"The N-terminal residues of SulA (1–42), which were not ordered in the previous structure, are not ordered in the complex structure either.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"achasapi","start":1,"term_ontology":"IDPO","curator_name":"Anastasia Chasapi","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-1986-5007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1OFT"}],"reference_id":"12808143","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9HZJ8","date":"2018-08-18T12:00:41.000Z","acc":"Q9HZJ8","name":"Cell division inhibitor SulA","length":161,"organism":"Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)","dataset":[],"UniParc":"UPI00000C58C4","genes":[{"name":{"value":"sulA"},"olnNames":[{"value":"PA3008"}]}],"alphafold_very_low_content":0.14906832298136646,"disorder_content":0.2608695652173913,"disprot_consensus":{"full":[{"start":1,"end":42,"type":"D"}],"Structural state":[{"start":1,"end":42,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00307","name":"Calponin homology (CH) domain","start":44,"end":149},{"id":"PF00307","name":"Calponin homology (CH) domain","start":167,"end":266},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":279,"end":371},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":379,"end":471},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":478,"end":567},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":577,"end":659},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":670,"end":760},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":767,"end":862},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":871,"end":961},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":969,"end":1057},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":1065,"end":1151},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":1158,"end":1245},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":1253,"end":1346},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":1353,"end":1439},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":1446,"end":1536},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":1544,"end":1633},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":1640,"end":1737},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":1802,"end":1856},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":1866,"end":1949},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":1962,"end":2035},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":2045,"end":2130},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":2174,"end":2227},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":2237,"end":2322},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":2330,"end":2417},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":2427,"end":2513},{"id":"PF00630","name":"Filamin/ABP280 repeat","start":2554,"end":2643}],"gene3D":[{"start":2230,"end":2337,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1788,"end":1863,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1351,"end":1444,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":275,"end":374,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1254,"end":1350,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1159,"end":1251,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":478,"end":575,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":26,"end":153,"id":"1.10.418.10","name":"Calponin-like domain"},{"start":2044,"end":2146,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1864,"end":1964,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1969,"end":2043,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":2338,"end":2425,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":375,"end":477,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1638,"end":1757,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":766,"end":868,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":869,"end":968,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":2171,"end":2229,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":2426,"end":2522,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":667,"end":765,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":969,"end":1063,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":154,"end":269,"id":"1.10.418.10","name":"Calponin-like domain"},{"start":2551,"end":2647,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1445,"end":1541,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1064,"end":1158,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":576,"end":666,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":1542,"end":1637,"id":"2.60.40.10","name":"Immunoglobulins"}]},"uniref50":"UniRef50_P21333","sequence":"MSSSHSRAGQSAAGAAPGGGVDTRDAEMPATEKDLAEDAPWKKIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENVSVALEFLDRESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWDEEEDEEAKKQTPKQRLLGWIQNKLPQLPITNFSRDWQSGRALGALVDSCAPGLCPDWDSWDASKPVTNAREAMQQADDWLGIPQVITPEEIVDPNVDEHSVMTYLSQFPKAKLKPGAPLRPKLNPKKARAYGPGIEPTGNMVKKRAEFTVETRSAGQGEVLVYVEDPAGHQEEAKVTANNDKNRTFSVWYVPEVTGTHKVTVLFAGQHIAKSPFEVYVDKSQGDASKVTAQGPGLEPSGNIANKTTYFEIFTAGAGTGEVEVVIQDPMGQKGTVEPQLEARGDSTYRCSYQPTMEGVHTVHVTFAGVPIPRSPYTVTVGQACNPSACRAVGRGLQPKGVRVKETADFKVYTKGAGSGELKVTVKGPKGEERVKQKDLGDGVYGFEYYPMVPGTYIVTITWGGQNIGRSPFEVKVGTECGNQKVRAWGPGLEGGVVGKSADFVVEAIGDDVGTLGFSVEGPSQAKIECDDKGDGSCDVRYWPQEAGEYAVHVLCNSEDIRLSPFMADIRDAPQDFHPDRVKARGPGLEKTGVAVNKPAEFTVDAKHGGKAPLRVQVQDNEGCPVEALVKDNGNGTYSCSYVPRKPVKHTAMVSWGGVSIPNSPFRVNVGAGSHPNKVKVYGPGVAKTGLKAHEPTYFTVDCAEAGQGDVSIGIKCAPGVVGPAEADIDFDIIRNDNDTFTVKYTPRGAGSYTIMVLFADQATPTSPIRVKVEPSHDASKVKAEGPGLSRTGVELGKPTHFTVNAKAAGKGKLDVQFSGLTKGDAVRDVDIIDHHDNTYTVKYTPVQQGPVGVNVTYGGDPIPKSPFSVAVSPSLDLSKIKVSGLGEKVDVGKDQEFTVKSKGAGGQGKVASKIVGPSGAAVPCKVEPGLGADNSVVRFLPREEGPYEVEVTYDGVPVPGSPFPLEAVAPTKPSKVKAFGPGLQGGSAGSPARFTIDTKGAGTGGLGLTVEGPCEAQLECLDNGDGTCSVSYVPTEPGDYNINILFADTHIPGSPFKAHVVPCFDASKVKCSGPGLERATAGEVGQFQVDCSSAGSAELTIEICSEAGLPAEVYIQDHGDGTHTITYIPLCPGAYTVTIKYGGQPVPNFPSKLQVEPAVDTSGVQCYGPGIEGQGVFREATTEFSVDARALTQTGGPHVKARVANPSGNLTETYVQDRGDGMYKVEYTPYEEGLHSVDVTYDGSPVPSSPFQVPVTEGCDPSRVRVHGPGIQSGTTNKPNKFTVETRGAGTGGLGLAVEGPSEAKMSCMDNKDGSCSVEYIPYEAGTYSLNVTYGGHQVPGSPFKVPVHDVTDASKVKCSGPGLSPGMVRANLPQSFQVDTSKAGVAPLQVKVQGPKGLVEPVDVVDNADGTQTVNYVPSREGPYSISVLYGDEEVPRSPFKVKVLPTHDASKVKASGPGLNTTGVPASLPVEFTIDAKDAGEGLLAVQITDPEGKPKKTHIQDNHDGTYTVAYVPDVTGRYTILIKYGGDEIPFSPYRVRAVPTGDASKCTVTVSIGGHGLGAGIGPTIQIGEETVITVDTKAAGKGKVTCTVCTPDGSEVDVDVVENEDGTFDIFYTAPQPGKYVICVRFGGEHVPNSPFQVTALAGDQPSVQPPLRSQQLAPQYTYAQGGQQTWAPERPLVGVNGLDVTSLRPFDLVIPFTIKKGEITGEVRMPSGKVAQPTITDNKDGTVTVRYAPSEAGLHEMDIRYDNMHIPGSPLQFYVDYVNCGHVTAYGPGLTHGVVNKPATFTVNTKDAGEGGLSLAIEGPSKAEISCTDNQDGTCSVSYLPVLPGDYSILVKYNEQHVPGSPFTARVTGDDSMRMSHLKVGSAADIPINISETDLSLLTATVVPPSGREEPCLLKRLRNGHVGISFVPKETGEHLVHVKKNGQHVASSPIPVVISQSEIGDASRVRVSGQGLHEGHTFEPAEFIIDTRDAGYGGLSLSIEGPSKVDINTEDLEDGTCRVTYCPTEPGNYIINIKFADQHVPGSPFSVKVTGEGRVKESITRRRRAPSVANVGSHCDLSLKIPEISIQDMTAQVTSPSGKTHEAEIVEGENHTYCIRFVPAEMGTHTVSVKYKGQHVPGSPFQFTVGPLGEGGAHKVRAGGPGLERAEAGVPAEFSIWTREAGAGGLAIAVEGPSKAEISFEDRKDGSCGVAYVVQEPGDYEVSVKFNEEHIPDSPFVVPVASPSGDARRLTVSSLQESGLKVNQPASFAVSLNGAKGAIDAKVHSPSGALEECYVTEIDQDKYAVRFIPRENGVYLIDVKFNGTHIPGSPFKIRVGEPGHGGDPGLVSAYGAGLEGGVTGNPAEFVVNTSNAGAGALSVTIDGPSKVKMDCQECPEGYRVTYTPMAPGSYLISIKYGGPYHIGGSPFKAKVTGPRLVSNHSLHETSSVFVDSLTKATCAPQHGAPGPGPADASKVVAKGLGLSKAYVGQKSSFTVDCSKAGNNMLLVGVHGPRTPCEEILVKHVGSRLYSVSYLLKDKGEYTLVVKWGDEHIPGSPYRVVVP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P21333","disprot_id":"DP01950","ncbi_taxon_id":9606,"regions_counter":1,"creator":"rdavidovic","regions":[{"region_id":"DP01950r001","ec_ontology":"ECO","end":36,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":1,"version":3,"statement":[{"text":"The N-terminal extension of 36 residues (chain A) and 38 (chain\nB) are not observed and are assumed to be disordered.","type":"Results"}],"term_name":"disorder","reference_html":"Skeletal dysplasias due to filamin A mutations result from a gain-of-function mechanism distinct from allelic neurological disorders. <i> Clark AR, Sawyer GM, Robertson SP, Sutherland-Smith AJ. </i> Hum Mol Genet, 2009","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19773341","date":"2023-05-15T16:37:23.947Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3HOP"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1061"}]}],"released":"2018_11","uniref100":"UniRef100_P21333","date":"2018-08-18T21:56:22.000Z","acc":"P21333","name":"Filamin-A","length":2647,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI000012AA0C","genes":[{"name":{"value":"FLNA"},"synonyms":[{"value":"FLN"},{"value":"FLN1"}]}],"alphafold_very_low_content":0.055156781261805815,"disorder_content":0.01360030222893842,"disprot_consensus":{"full":[{"start":1,"end":36,"type":"D"}],"Structural state":[{"start":1,"end":36,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00191","name":"Annexin","start":47,"end":111},{"id":"PF00191","name":"Annexin","start":118,"end":183},{"id":"PF00191","name":"Annexin","start":202,"end":267},{"id":"PF00191","name":"Annexin","start":277,"end":342}],"gene3D":[{"start":274,"end":346,"id":"1.10.220.10","name":"Annexin"},{"start":41,"end":113,"id":"1.10.220.10","name":"Annexin"},{"start":114,"end":190,"id":"1.10.220.10","name":"Annexin"},{"start":191,"end":273,"id":"1.10.220.10","name":"Annexin"}]},"uniref50":"UniRef50_P04083","sequence":"MAMVSEFLKQAWFIENEEQEYVQTVKSSKGGPGSAVSPYPTFNPSSDVAALHKAIMVKGVDEATIIDILTKRNNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLALLKTPAQFDADELRAAMKGLGTDEDTLIEILASRTNKEIRDINRVYREELKRDLAKDITSDTSGDFRNALLSLAKGDRSEDFGVNEDLADSDARALYEAGERRKGTDVNVFNTILTTRSYPQLRRVFQKYTKYSKHDMNKVLDLELKGDIEKCLTAIVKCATSKPAFFAEKLHQAMKGVGTRHKALIRIMVSRSEIDMNDIKAFYQKMYGISLCQAILDETKGDYEKILVALCGGN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P04083","disprot_id":"DP01951","ncbi_taxon_id":9606,"regions_counter":20,"creator":"ppere","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":185,"region_id":"DP01951r006","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Folding properties of an annexin I domain: a 1H-15N NMR and CD study. <i> Cordier-Ochsenbein F, Guerois R, Baleux F, Huynh-Dinh T, Chaffotte A, Neumann JM, Sanson A. </i> Biochemistry, 1996","statement":[{"text":"Deconvolution of the far-UV CD spectrum of the isolated domain in aqueous solution, using the Yang reference, gave a secondary structure content of, at most, 25% alpha-helix, 75% coil, and no beta-structure. This helix content is quite far from the native content.","type":"Results"},{"text":"This fragment was studied by circular dichroism and by NMR. Both techniques clearly showed that the domain was poorly folded in pure aqueous solution although the residual helix structure is far from negligible.","type":"Introduction"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":116,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"8756690","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:39:01.523Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":185,"region_id":"DP01951r007","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Folding properties of an annexin I domain: a 1H-15N NMR and CD study. <i> Cordier-Ochsenbein F, Guerois R, Baleux F, Huynh-Dinh T, Chaffotte A, Neumann JM, Sanson A. </i> Biochemistry, 1996","statement":[{"text":"A first set of NMR experiments was performed on the domain solubilized in pure aqueous solution, in which the very weak spectral dispersion of the amide proton resonances (1.1 ppm) showed that the peptide is poorly folded.","type":"Results"},{"text":"This fragment was studied by circular dichroism and by NMR. Both techniques clearly showed that the domain was poorly folded in pure aqueous solution although the residual helix structure is far from negligible.","type":"Introduction"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":116,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"8756690","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:39:02.687Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":2,"end":12,"reference_id":"10673436","reference_source":"pmid","reference_html":"Structural basis of the Ca(2+)-dependent association between S100C (S100A11) and its target, the N-terminal part of annexin I. <i> Réty S, Osterloh D, Arié JP, Tabaries S, Seeman J, Russo-Marie F, Gerke V, Lewit-Bentley A. </i> Structure, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1QLS"}],"region_id":"DP01951r009","statement":[{"text":"The annexin I N-terminal peptide is clearly visible in the complex, despite its high temperature factor.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:39:06.871Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":2,"end":12,"reference_id":"10673436","reference_source":"pmid","reference_html":"Structural basis of the Ca(2+)-dependent association between S100C (S100A11) and its target, the N-terminal part of annexin I. <i> Réty S, Osterloh D, Arié JP, Tabaries S, Seeman J, Russo-Marie F, Gerke V, Lewit-Bentley A. </i> Structure, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1QLS"}],"region_id":"DP01951r010","statement":[{"text":"The annexin I N-terminal peptide is clearly visible in the complex, despite its high temperature factor.","type":"Results"},{"text":"The peptide forms an amphiphilic α helix, as predicted [20].","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:39:22.416Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":2,"end":12,"reference_id":"10673436","reference_source":"pmid","reference_html":"Structural basis of the Ca(2+)-dependent association between S100C (S100A11) and its target, the N-terminal part of annexin I. <i> Réty S, Osterloh D, Arié JP, Tabaries S, Seeman J, Russo-Marie F, Gerke V, Lewit-Bentley A. </i> Structure, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"1QLS"}],"interaction_partner":[{"db":"UniProt","id":"P31950","partner_start":null,"partner_end":null}],"region_id":"DP01951r011","statement":[{"text":"The annexin I N-terminal peptide is clearly visible in the complex, despite its high temperature factor (Figure 2). Although the stoichiometry is one peptide bound to one S100C monomer, the binding zone on S100C is formed by regions of both molecules of the dimer: the C-terminal helix and the L2 linker region of one molecule and the N-terminal helix of the other molecule.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:39:30.241Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":116,"end":185,"reference_id":"8756690","reference_source":"pmid","reference_html":"Folding properties of an annexin I domain: a 1H-15N NMR and CD study. <i> Cordier-Ochsenbein F, Guerois R, Baleux F, Huynh-Dinh T, Chaffotte A, Neumann JM, Sanson A. </i> Biochemistry, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01951r012","statement":[{"text":"Nevertheless, the 15N chemical shift variations, Δδ15N, are good indicators of the course of the structural change, within the different segments of the domain, associated with DPC titration.","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:39:30.995Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":116,"end":185,"reference_id":"8756690","reference_source":"pmid","reference_html":"Folding properties of an annexin I domain: a 1H-15N NMR and CD study. <i> Cordier-Ochsenbein F, Guerois R, Baleux F, Huynh-Dinh T, Chaffotte A, Neumann JM, Sanson A. </i> Biochemistry, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01951r013","statement":[{"text":"As expected, addition of micelles led to a considerable increase in the helix content (Figure 10).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:39:25.061Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":116,"end":185,"reference_id":"8756690","reference_source":"pmid","reference_html":"Folding properties of an annexin I domain: a 1H-15N NMR and CD study. <i> Cordier-Ochsenbein F, Guerois R, Baleux F, Huynh-Dinh T, Chaffotte A, Neumann JM, Sanson A. </i> Biochemistry, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01951r014","statement":[{"text":"Nevertheless, the 15N chemical shift variations, Δδ15N, are good indicators of the course of the structural change, within the different segments of the domain, associated with DPC titration.","type":"Discussion"},{"text":"At high DPC concentration (150 mM), the NH spectral range was considerably larger than that observed in pure aqueous solution (1.7 ppm against 1.1 ppm for the pure aqueous solution).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:39:26.362Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":2,"end":26,"reference_id":"11078886","reference_source":"pmid","reference_html":"Solution structure and membrane-binding property of the N-terminal tail domain of human annexin I. <i> Yoon MK, Park SH, Won HS, Na DS, Lee BJ. </i> FEBS Lett, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01951r015","statement":[{"text":"In aqueous buffer, the CD spectrum of AnxIN26 showed a strong negative band at 200 nm and a broad band around 222 nm, indicating a predominantly random-coil conformation with a slight helical propensity [33,34].","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:39:17.725Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":2,"end":26,"reference_id":"11078886","reference_source":"pmid","reference_html":"Solution structure and membrane-binding property of the N-terminal tail domain of human annexin I. <i> Yoon MK, Park SH, Won HS, Na DS, Lee BJ. </i> FEBS Lett, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01951r016","statement":[{"text":"The CD spectrum of AnxIN26 in 10 mM SDS, which is above the critical micellar concentration of SDS [38], also showed a typical α-helix pattern.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:39:27.878Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":2,"end":26,"reference_id":"11078886","reference_source":"pmid","reference_html":"Solution structure and membrane-binding property of the N-terminal tail domain of human annexin I. <i> Yoon MK, Park SH, Won HS, Na DS, Lee BJ. </i> FEBS Lett, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","released":"2022_03","version":3,"region_id":"DP01951r017","statement":[{"text":"The CD spectrum of AnxIN26 in 10 mM SDS, which is above the critical micellar concentration of SDS [38], also showed a typical α-helix pattern.","type":"Results"},{"text":"Thus, it can be suggested that the conformational transition of AnxIN26, from random-coil in aqueous buffer to α-helix in membrane-mimetic environments, reflects its binding to the membrane.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:39:33.107Z"},"term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":4,"end":19,"reference_id":"11078886","reference_source":"pmid","reference_html":"Solution structure and membrane-binding property of the N-terminal tail domain of human annexin I. <i> Yoon MK, Park SH, Won HS, Na DS, Lee BJ. </i> FEBS Lett, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP01951r018","statement":[{"text":"As shown in Fig. 2, the presence of a typical α-helix from V4 to Q19 is supported, both in TFE/water and in SDS micelles, by the frequent observations of dNN(i,i+1), dNN(i,i+2), dαL(i,i+3), dαN(i,i+3) and dαN(i,i+4) NOE connectivities, and slowly exchanging amide protons.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:39:28.523Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":2,"end":26,"reference_id":"11078886","reference_source":"pmid","reference_html":"Solution structure and membrane-binding property of the N-terminal tail domain of human annexin I. <i> Yoon MK, Park SH, Won HS, Na DS, Lee BJ. </i> FEBS Lett, 2000","date":"2022-12-06T11:16:39.872Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_12","version":4,"region_id":"DP01951r019","statement":[{"text":"The C-terminal region of the AnxIN26 helix contains frequent glutamate residues (-E15-NE-E-Q-E20-; Fig. 4A). Thus, we suggest that Ca2-ions bind to the negatively charged glutamate-rich region of AnxIN26 and function as salt-bridges between the peptide and SDS micelle molecules. The calcium-bridge in this region seems to stabilize the helical conformation of AnxIN26 as a membrane-bound form, resulting in the intensification of CD signals as shown in Fig. 5.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a calcium ion (Ca2+).\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-20T17:39:48.985Z"}},{"start":116,"end":185,"reference_id":"8756690","reference_source":"pmid","reference_html":"Folding properties of an annexin I domain: a 1H-15N NMR and CD study. <i> Cordier-Ochsenbein F, Guerois R, Baleux F, Huynh-Dinh T, Chaffotte A, Neumann JM, Sanson A. </i> Biochemistry, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP01951r020","statement":[{"text":"Calcium ions participate in the functional binding of annexin to membranes.","type":"Introduction"},{"text":"Nevertheless, the 15N chemical shift variations, Δδ15N, are good indicators of the course of the structural change, within the different segments of the domain, associated with DPC titration.","type":"Results"},{"text":"At high DPC concentration (150 mM), the NH spectral range was considerably larger than that observed in pure aqueous solution (1.7 ppm against 1.1 ppm for the pure aqueous solution).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:39:35.829Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2018_11","uniref100":"UniRef100_P04083","date":"2018-08-18T22:54:15.000Z","acc":"P04083","name":"Annexin A1","length":346,"organism":"Homo sapiens","dataset":["Extracellular matrix proteins","NDDs-related proteins"],"UniParc":"UPI0000125B6F","genes":[{"name":{"value":"ANXA1"},"synonyms":[{"value":"ANX1"},{"value":"LPC1"}]}],"alphafold_very_low_content":0,"disorder_content":0.2745664739884393,"disprot_consensus":{"full":[{"start":2,"end":26,"type":"T"},{"start":116,"end":185,"type":"T"}],"Structural state":[{"start":2,"end":26,"type":"D"},{"start":116,"end":185,"type":"D"}],"Structural transition":[{"start":2,"end":26,"type":"T"},{"start":116,"end":185,"type":"T"}],"Molecular function":[{"start":2,"end":26,"type":"F"},{"start":116,"end":185,"type":"F"}],"Biological process":[{"start":116,"end":185,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":20,"end":276}],"gene3D":[{"start":1,"end":97,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":98,"end":315,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"}]},"uniref50":"UniRef50_Q14012","sequence":"MPGAVEGPRWKQAEDIRDIYDFRDVLGTGAFSEVILAEDKRTQKLVAIKCIAKKALEGKEGSMENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSGGELFDRIVEKGFYTERDASRLIFQVLDAVKYLHDLGIVHRDLKPENLLYYSLDEDSKIMISDFGLSKMEDPGSVLSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSPYWDDISDSAKDFIRHLMEKDPEKRFTCEQALQHPWIAGDTALDKNIHQSVSEQIKKNFAKSKWKQAFNATAVVRHMRKLQLGTSQEGQGQTASHGELLTPTAGGPAAGCCCRDCCVEPGSELPPAPPPSSRAMD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_Q63450","disprot_id":"DP01958","ncbi_taxon_id":10116,"regions_counter":3,"creator":"ppere","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":11,"region_id":"DP01958r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for the autoinhibition of calcium/calmodulin-dependent protein kinase I. <i> Goldberg J, Nairn AC, Kuriyan J. </i> Cell, 1996","statement":[{"text":"11 residues at the N-terminus and 4 at the C-terminus that are also disordered","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ahatos","start":1,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1A06"}],"reference_id":"8601311","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":63,"region_id":"DP01958r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for the autoinhibition of calcium/calmodulin-dependent protein kinase I. <i> Goldberg J, Nairn AC, Kuriyan J. </i> Cell, 1996","statement":[{"text":"There are two regions of high conformational disorder within the catalytic core of CaMKI, with no observable electron density for the corresponding residues. The loop between β8 and αEF in the C-terminal domain...","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":54,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1A06"}],"reference_id":"8601311","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":181,"region_id":"DP01958r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for the autoinhibition of calcium/calmodulin-dependent protein kinase I. <i> Goldberg J, Nairn AC, Kuriyan J. </i> Cell, 1996","statement":[{"text":"The disorder of another loop, between β3 and αC in the ATP-binding domain, may also be coupled to the activation state of the enzyme...","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":164,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1A06"}],"reference_id":"8601311","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q63450","date":"2018-08-18T23:00:55.000Z","acc":"Q63450","name":"Calcium/calmodulin-dependent protein kinase type 1","length":374,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI0000170ADA","genes":[{"name":{"value":"Camk1"}}],"alphafold_very_low_content":0.20320855614973263,"disorder_content":0.10427807486631016,"disprot_consensus":{"full":[{"start":1,"end":11,"type":"D"},{"start":54,"end":63,"type":"D"},{"start":164,"end":181,"type":"D"}],"Structural state":[{"start":1,"end":11,"type":"D"},{"start":54,"end":63,"type":"D"},{"start":164,"end":181,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00573","name":"Ribosomal protein L4/L1 family","start":18,"end":223}],"gene3D":[{"start":1,"end":234,"id":"3.40.1370.10","name":"3.40.1370.10"}]},"uniref50":"UniRef50_P38516","sequence":"MAQVDLLNVKGEKVGTLEISDFVFNIDPNYDVMWRYVDMQLSNRRAGTASTKTRGEVSGGGRKPWPQKHTGRARHGSIRSPIWRHGGVVHGPKPRDWSKKLNKKMKKLALRSALSVKYRENKLLVLDDLKLERPKTKSLKEILQNLQLSDKKTLIVLPWKEEGYMNVKLSGRNLPDVKVIIADNPNNSKNGEKAVRIDGLNVFDMLKYDYLVLTRDMVSKIEEVLGNEAGKALTA","taxonomy":["Bacteria","Thermotogae","Thermotogales","Thermotogaceae","Thermotoga"],"uniref90":"UniRef90_P38516","disprot_id":"DP01961","ncbi_taxon_id":243274,"regions_counter":2,"creator":"npalopoli","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":95,"region_id":"DP01961r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of ribosomal protein L4 shows RNA-binding sites for ribosome incorporation and feedback control of the S10 operon. <i> Worbs M, Huber R, Wahl MC. </i> EMBO J, 2000","statement":[{"text":"Crystals of TmaL4 contain full-length protein, as seen from SDS-PAGE analysis of dissolved experiments ... A void seen in the crystal packing could accomodate the unobserved part of the molecule in a folded conformation. All these observations suggest that a large portion of TmaL4 is internally disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"npalopoli","start":43,"term_ontology":"IDPO","curator_name":"Nicolás Palopoli","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7925-6436","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1DMG"}],"reference_id":"10698923","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":95,"term_name":"DNA binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of ribosomal protein L4 shows RNA-binding sites for ribosome incorporation and feedback control of the S10 operon. <i> Worbs M, Huber R, Wahl MC. </i> EMBO J, 2000","statement":[{"text":"The putative RNA interaction surface can be subdivided into two spatially separated regions. The first is made up mainly of the N-terminal part of helix alpha3. It is preceded by the 55 residue disordered loop, which is the most conserved portion in prokaryotic L4 proteins and displays many basic residues. The loop may therefore be the central element of this RNA-binding patch.","type":"Results"}],"term_id":"GO:0003677","curator_id":"npalopoli","start":43,"term_ontology":"GO","curator_name":"Nicolás Palopoli","reference_id":"10698923","version":3,"curator_orcid":"0000-0001-7925-6436","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01961r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P38516","date":"2018-08-18T23:21:14.000Z","acc":"P38516","name":"50S ribosomal protein L4","length":235,"organism":"Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)","dataset":[],"UniParc":"UPI0000170499","genes":[{"name":{"value":"rplD"},"olnNames":[{"value":"TM_1499"}]}],"alphafold_very_low_content":0.029787234042553193,"disorder_content":0.225531914893617,"disprot_consensus":{"full":[{"start":43,"end":95,"type":"D"}],"Structural state":[{"start":43,"end":95,"type":"D"}],"Molecular function":[{"start":43,"end":95,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00191","name":"Annexin","start":47,"end":111},{"id":"PF00191","name":"Annexin","start":118,"end":183},{"id":"PF00191","name":"Annexin","start":202,"end":265},{"id":"PF00191","name":"Annexin","start":277,"end":342}],"gene3D":[{"start":114,"end":190,"id":"1.10.220.10","name":"Annexin"},{"start":274,"end":346,"id":"1.10.220.10","name":"Annexin"},{"start":41,"end":113,"id":"1.10.220.10","name":"Annexin"},{"start":191,"end":273,"id":"1.10.220.10","name":"Annexin"}]},"uniref50":"UniRef50_P46193","sequence":"MAMVSEFLKQAWFIDNEEQEYIKTVKGSKGGPGSAVSPYPTFNPSSDVEASHKAITVKGVDEATIIEIHTKRTNAQRQQIKAAYLQEKGKPLDEALKKALTGHLEEVALALLKTPAQFDADELRAAMKGLGTDEDTLNEILASRTNREIREINRVYKEELKRDLAKDITSDTSGDYQKALLSLAKGDRSEDLAINDDLADTDARALYEAGERRKGTDLNVFITILTTRSYLHLRRVFQKYSKYSKHDMNKVLDLELKGDIENCLTVVVKCATSKPMFFAEKLHQAMKGNGTRHKTLIRIMVSRSEIDMNDIKACYQKLYGISLCQAILDETKGDYEKILVALCGGD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Suina","Suidae","Sus"],"uniref90":"UniRef90_P46193","disprot_id":"DP01963","ncbi_taxon_id":9823,"regions_counter":3,"creator":"ppere","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":40,"region_id":"DP01963r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"A calcium-driven conformational switch of the N-terminal and core domains of annexin A1. <i> Rosengarth A, Luecke H. </i> J Mol Biol, 2003","statement":[{"text":"Although we observe the large conformational change in the core domain that was anticipated upon calcium binding, we were not be able to model residues 1–40 in the full-length annexin A1 structure. The mass spectrum shows without a doubt that the crystals do contain the full-length protein, however the N-terminal domain is disordered in the X-ray structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":1,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1MCX"}],"reference_id":"12595246","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":41,"region_id":"DP01963r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"X-ray structure of full-length annexin 1 and implications for membrane aggregation. <i> Rosengarth A, Gerke V, Luecke H. </i> J Mol Biol, 2001","statement":[{"text":"The N-terminal domain of annexin 1 contains 41 residues.","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":1,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1HM6"}],"reference_id":"11178908","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":41,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"X-ray structure of full-length annexin 1 and implications for membrane aggregation. <i> Rosengarth A, Gerke V, Luecke H. </i> J Mol Biol, 2001","statement":[{"text":"Annexin 1 is active in membrane aggregation and its refined 1.8 Å structure shows an alpha-helical N-terminal domain connected to the core domain by a flexible linker.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"ppereira","start":1,"term_ontology":"IDPO","curator_name":"Pedro Pereira","reference_id":"11178908","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01963r003","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_P19619","date":"2018-08-19T02:35:29.000Z","acc":"P19619","name":"Annexin A1","length":346,"organism":"Sus scrofa","dataset":[],"UniParc":"UPI000016C687","genes":[{"name":{"value":"ANXA1"},"synonyms":[{"value":"ANX1"}]}],"alphafold_very_low_content":0,"disorder_content":0.11849710982658959,"disprot_consensus":{"full":[{"start":1,"end":41,"type":"T"}],"Structural state":[{"start":1,"end":41,"type":"D"}],"Structural transition":[{"start":1,"end":41,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00009","name":"Elongation factor Tu GTP binding domain","start":10,"end":201},{"id":"PF03143","name":"Elongation factor Tu C-terminal domain","start":298,"end":392},{"id":"PF03144","name":"Elongation factor Tu domain 2","start":225,"end":294}],"gene3D":[{"start":206,"end":334,"id":"2.40.30.10","name":"Translation factors"},{"start":338,"end":393,"id":"2.40.30.10","name":"Translation factors"},{"start":1,"end":203,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_P14647","sequence":"MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVGAGVVAKVLS","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P14647","disprot_id":"DP01965","ncbi_taxon_id":83333,"regions_counter":5,"creator":"npalopoli","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":63,"region_id":"DP01965r001","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Structure of the E. coli ribosome-EF-Tu complex at <3 Å resolution by Cs-corrected cryo-EM. <i> Fischer N, Neumann P, Konevega AL, Bock LV, Ficner R, Rodnina MV, Stark H. </i> Nature, 2015","term_id":"IDPO:0000002","curator_id":"npalopoli","start":42,"term_ontology":"IDPO","curator_name":"Nicolás Palopoli","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7925-6436","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5AFI"}],"reference_id":"25707802","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":63,"region_id":"DP01965r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the Qbeta replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins. <i> Kidmose RT, Vasiliev NN, Chetverin AB, Andersen GR, Knudsen CR. </i> Proc Natl Acad Sci U S A, 2010","statement":[{"text":"X-ray diffraction data extending to a maximum resolution of 2.5 Å were collected and the structure of the Qβ core replicase was determined by molecular replacement ... disordered are the ... EF-Tu residues 1–8 and 42–63","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"npalopoli","start":43,"term_ontology":"IDPO","curator_name":"Nicolás Palopoli","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7925-6436","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3MMP"}],"reference_id":"20534494","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":63,"region_id":"DP01965r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for RNA-genome recognition during bacteriophage Qβ replication. <i> Gytz H, Mohr D, Seweryn P, Yoshimura Y, Kutlubaeva Z, Dolman F, Chelchessa B, Chetverin AB, Mulder FA, Brodersen DE, Knudsen CR. </i> Nucleic Acids Res, 2015","statement":[{"text":"The structure is complete except for residues constituting ... the switch I region 42–63 of EF-Tu","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"npalopoli","start":43,"term_ontology":"IDPO","curator_name":"Nicolás Palopoli","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7925-6436","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4R71"}],"reference_id":"26578560","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":64,"region_id":"DP01965r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution. <i> Kawashima T, Berthet-Colominas C, Wulff M, Cusack S, Leberman R. </i> Nature, 1996","statement":[{"text":"In EF-Tu, we have not modelled residues 42-63, including the effector loop (some scattered densities are visible)","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"npalopoli","start":44,"term_ontology":"IDPO","curator_name":"Nicolás Palopoli","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-7925-6436","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1EFU"}],"reference_id":"8596629","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P14647","date":"2018-08-19T06:50:04.000Z","acc":"P0CE48","name":"Elongation factor Tu 2","length":394,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI0000110FB2","genes":[{"name":{"value":"tufB","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00118","url":"https://hamap.expasy.org/unirule/MF_00118"}}]},"olnNames":[{"value":"b3980"},{"value":"JW3943"}]}],"alphafold_very_low_content":0.0025380710659898475,"disorder_content":0.0583756345177665,"disprot_consensus":{"full":[{"start":42,"end":64,"type":"D"}],"Structural state":[{"start":42,"end":64,"type":"D"}]}},{"features":{"pfam":[{"id":"PF07654","name":"Immunoglobulin C1-set domain","start":14,"end":94}],"gene3D":[{"start":4,"end":127,"id":"2.60.40.10","name":"Immunoglobulins"}]},"uniref50":"UniRef50_P03986","sequence":"DKQLDADVSPKPTIFLPSIAETKLQKAGTYLCLLEKFFPDVIKIHWQEKKSNTILGSQEGNTMKTNDTYMKFSWLTVPEKSLDKEHRCIVRHENNKNGVDQEIIFPPIKTDVITMDPKDNCSKDANDTLLLQLTNTSAYYMYLLLLLKSVVYFAIITCCLLRRTAFCCNGEKS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P0CF51","disprot_id":"DP01967","ncbi_taxon_id":9606,"regions_counter":4,"creator":"ppere","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":112,"region_id":"DP01967r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"CD1d-lipid antigen recognition by the γδ TCR. <i> Uldrich AP, Le Nours J, Pellicci DG, Gherardin NA, McPherson KG, Lim RT, Patel O, Beddoe T, Gras S, Rossjohn J, Godfrey DI. </i> Nat Immunol, 2013","statement":[{"text":"...the mobile CDR3γ loop in the unligated state became ordered upon CD1d–α-GalCer engagement.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ahatos","start":102,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4LHU"}],"reference_id":"24076636","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":112,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"CD1d-lipid antigen recognition by the γδ TCR. <i> Uldrich AP, Le Nours J, Pellicci DG, Gherardin NA, McPherson KG, Lim RT, Patel O, Beddoe T, Gras S, Rossjohn J, Godfrey DI. </i> Nat Immunol, 2013","statement":[{"text":"...the mobile CDR3γ loop in the unligated state became ordered upon CD1d–α-GalCer engagement.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"ahatos","start":102,"term_ontology":"IDPO","curator_name":"András Hatos","reference_id":"24076636","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01967r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":112,"term_name":"small molecule binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"CD1d-lipid antigen recognition by the γδ TCR. <i> Uldrich AP, Le Nours J, Pellicci DG, Gherardin NA, McPherson KG, Lim RT, Patel O, Beddoe T, Gras S, Rossjohn J, Godfrey DI. </i> Nat Immunol, 2013","statement":[{"text":"Within the 9C2 γδ TCR ternary complex, Arg103γ and Tyr111γ contacted directly the galactose moiety...","type":"Results"}],"term_id":"GO:0036094","curator_id":"ahatos","start":102,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"24076636","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01967r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":112,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"CD1d-lipid antigen recognition by the γδ TCR. <i> Uldrich AP, Le Nours J, Pellicci DG, Gherardin NA, McPherson KG, Lim RT, Patel O, Beddoe T, Gras S, Rossjohn J, Godfrey DI. </i> Nat Immunol, 2013","statement":[{"text":"Tyr111γ and the main chain of the CDR3γ loop also formed van der Waals contacts with Trp153, a CD1d residue...","type":"Results"}],"term_id":"GO:0005515","curator_id":"ahatos","start":102,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"24076636","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01967r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P0CF51","date":"2018-08-19T19:09:48.000Z","acc":"P0CF51","name":"T cell receptor gamma constant 1","length":173,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000176EF9","genes":[{"name":{"value":"TRGC1","evidences":[{"code":"ECO:0000303","source":{"name":"Citation","id":"Ref.3","url":"https://www.uniprot.org/uniprot/null#ref3"}}]},"synonyms":[{"value":"TCRGC1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:12275","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:12275"}}]}]}],"alphafold_very_low_content":0.05202312138728324,"disorder_content":0.06358381502890173,"disprot_consensus":{"full":[{"start":102,"end":112,"type":"T"}],"Structural state":[{"start":102,"end":112,"type":"D"}],"Structural transition":[{"start":102,"end":112,"type":"T"}],"Molecular function":[{"start":102,"end":112,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00313","name":"'Cold-shock' DNA-binding domain","start":90,"end":149}],"gene3D":[{"start":89,"end":150,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}]},"uniref50":"UniRef50_A0A2H1EAH9","sequence":"MAKSQQTFSKSEKEKKRLKKRQDKQKKMDARKADRDEHGPSGIQFAYVDHNGNLTDTPPDPELKVEYELEDIQISVSKKEDLPEEDPVRKGKVSFFDSSKGFGFIIDMENNEKYFTHVSGLIDDIVENDKVSFELERGMRGMNAVKVTKI","taxonomy":["Bacteria","Bacteroidetes","Flavobacteriia","Flavobacteriales","Flavobacteriaceae","Polaribacter"],"uniref90":"UniRef90_A0A1B8U5A6","disprot_id":"DP01968","ncbi_taxon_id":313594,"regions_counter":1,"creator":"ppere","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":86,"region_id":"DP01968r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"An intrinsically disordered domain in Polaribacter irgensii KOPRI 22228 CspB confers extraordinary freeze-tolerance. <i> Jung YH, Uh JH, Lee K, Im H. </i> Biochem Biophys Res Commun, 2018","statement":[{"text":"The far-UV CD spectra of CspBNPi show a minimum close to 200 nm and weak ellipticity around 222 nm (Fig. 3B), which are also typical of a random coil conformation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":1,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29330047","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_A4C1A5","date":"2018-08-20T03:09:29.000Z","acc":"A4C1A5","name":"Cold shock protein, putative DNA-binding protein","length":150,"organism":"Polaribacter irgensii 23-P","dataset":[],"UniParc":"UPI00006B6EDA","genes":[{"orfNames":[{"value":"PI23P_11262","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EAR11908.1","url":"https://www.ebi.ac.uk/ena/browser/view/EAR11908.1"}}]}]}],"alphafold_very_low_content":0,"disorder_content":0.5733333333333334,"disprot_consensus":{"full":[{"start":1,"end":86,"type":"D"}],"Structural state":[{"start":1,"end":86,"type":"D"}]}},{"features":{"pfam":[{"id":"PF07376","name":"Prosystemin","start":1,"end":200}]},"uniref50":"UniRef50_P27058","sequence":"MGTPSYDIKNKGDDMQEEPKVKLHHEKGGDEKEKIIEKETPSQDINNKDTISSYVLRDDTQEIPKMEHEEGGYVKEKIVEKETISQYIIKIEGDDDAQEKLKVEYEEEEYEKEKIVEKETPSQDINNKGDDAQEKPKVEHEEGDDKETPSQDIIKMEGEGALEITKVVCEKIIVREDLAVQSKPPSKRDPPKMQTDNNKL","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","lamiids","Solanales","Solanaceae","Solanoideae","Solaneae","Solanum","Solanum subgen. Lycopersicon"],"uniref90":"UniRef90_P27058","disprot_id":"DP01969","ncbi_taxon_id":4081,"regions_counter":7,"creator":"ppere","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":200,"region_id":"DP01969r001","released":"2022_03","ec_id":"ECO:0007064","reference_html":"Prosystemin, a prohormone that modulates plant defense barriers, is an intrinsically disordered protein. <i> Buonanno M, Coppola M, Di Lelio I, Molisso D, Leone M, Pennacchio F, Langella E, Rao R, Monti SM. </i> Protein Sci, 2018","statement":[{"text":"By means of light scattering studies, the hydrodynamic properties of Prosys were elucidated, showing that, in solution, the prohormone occurs as a monomeric protein, with a molecular mass of 23.7 ± 0.1 kDa [Fig. 1(C)], and an apparent hydrodynamic radius of 5.61 ± 0.01 nm of the monodisperse peak, which is indicative of a protein with low compactness.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":1,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"dynamic light scattering assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29168260","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":200,"region_id":"DP01969r002","released":"2022_03","ec_id":"ECO:0007689","reference_html":"Prosystemin, a prohormone that modulates plant defense barriers, is an intrinsically disordered protein. <i> Buonanno M, Coppola M, Di Lelio I, Molisso D, Leone M, Pennacchio F, Langella E, Rao R, Monti SM. </i> Protein Sci, 2018","statement":[{"text":"As assessed by SDS-PAGE, Prosys showed an aberrant migration with an apparent molecular mass of 40 kDa, exceeding the expected molecular mass of 26 kDa (inclusive of the His-tag)...","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":1,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29168260","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":200,"region_id":"DP01969r003","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Prosystemin, a prohormone that modulates plant defense barriers, is an intrinsically disordered protein. <i> Buonanno M, Coppola M, Di Lelio I, Molisso D, Leone M, Pennacchio F, Langella E, Rao R, Monti SM. </i> Protein Sci, 2018","statement":[{"text":"Elution from the SEC column occurred as a sharp peak with an apparent molecular mass (MM app) of about 71 kDa [Fig. 1(B)], as estimated by the calibration curve [inset Fig. 1(B)]. This value was well above the expected value (MM theo) and was not compatible with a monomeric globular structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":1,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"chromatography evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29168260","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":200,"region_id":"DP01969r004","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Prosystemin, a prohormone that modulates plant defense barriers, is an intrinsically disordered protein. <i> Buonanno M, Coppola M, Di Lelio I, Molisso D, Leone M, Pennacchio F, Langella E, Rao R, Monti SM. </i> Protein Sci, 2018","statement":[{"text":"Prosys, incubated with different E:S ratio and at different time intervals, was readily digested already after 1 h of incubation (Fig. S1).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":1,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29168260","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":200,"region_id":"DP01969r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Prosystemin, a prohormone that modulates plant defense barriers, is an intrinsically disordered protein. <i> Buonanno M, Coppola M, Di Lelio I, Molisso D, Leone M, Pennacchio F, Langella E, Rao R, Monti SM. </i> Protein Sci, 2018","statement":[{"text":"Prosys spectrum at neutral pH showed low ellipticity at 190 nm and a large negative ellipticity at 198 nm, typically observed for proteins in a largely disordered conformation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":1,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29168260","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":200,"region_id":"DP01969r006","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Prosystemin, a prohormone that modulates plant defense barriers, is an intrinsically disordered protein. <i> Buonanno M, Coppola M, Di Lelio I, Molisso D, Leone M, Pennacchio F, Langella E, Rao R, Monti SM. </i> Protein Sci, 2018","statement":[{"text":"The 1D [1H] NMR spectrum together with the 2D [1H,1H] TOCSY and 2D [1H,1H] NOESY experiments of Prosys presented the canonical features of the unstructured proteins, being dominated by a poor spectral dispersion, typical of IDPs.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":1,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29168260","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":178,"reference_id":"35053122","reference_source":"pmid","reference_html":"Tomato Prosystemin Is Much More than a Simple Systemin Precursor. <i> Molisso D, Coppola M, Buonanno M, Di Lelio I, Monti SM, Melchiorre C, Amoresano A, Corrado G, Delano-Frier JP, Becchimanzi A, Pennacchio F, Rao R. </i> Biology (Basel), 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP01969r007","statement":[{"text":"Indeed, CD spectra revealed a disorder content (Figure 2), a reversible temperature-induced behavior, and a capability to increase secondary structure content in the presence of TFE co-solvent (Figure S4a,b).","type":"Results"},{"text":"ProSys(1-178) recombinant protein is intrinsically disordered. The Far-UV CD spectrum was recorded from 260 to 190 nm at 20 °C in 10 mM phosphate buffer pH 7.4 at a protein concentration of 6.8 µM.","type":"Figure"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P27058","date":"2018-08-20T03:37:22.000Z","acc":"P27058","name":"Systemin","length":200,"organism":"Solanum lycopersicum","dataset":[],"UniParc":"UPI0000136673","genes":[],"alphafold_very_low_content":0.845,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":200,"type":"D"}],"Structural state":[{"start":1,"end":200,"type":"D"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_M1GUG5","sequence":"TSANSRTHGATSTSTHGATSTAKPAASTPPKAAATSTIKPTVTTPKAAATSTTEPTVTTKPSPAKPAASNTAKPAASTPKKPHDER","taxonomy":["Eukaryota","Metazoa","Spiralia","Lophotrochozoa","Platyhelminthes","Trematoda","Digenea","Strigeidida","Schistosomatoidea","Schistosomatidae","Schistosoma"],"uniref90":"UniRef90_M1GUG5","disprot_id":"DP01970","ncbi_taxon_id":6183,"regions_counter":11,"creator":"jssuarez","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":86,"region_id":"DP01970r001","released":"2022_03","ec_id":"ECO:0006202","reference_html":"Folding factors and partners for the intrinsically disordered protein micro-exon gene 14 (MEG-14). <i> Lopes JL, Orcia D, Araujo AP, DeMarco R, Wallace BA. </i> Biophys J, 2013","statement":[{"text":"The SRCD measurements confirm experimentally that MEG-14 should be classified as an IDP.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":1,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"synchrotron radiation circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23746524","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-16T15:44:42.800Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":86,"region_id":"DP01970r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins. <i> Kumagai PS, DeMarco R, Lopes JLS. </i> Eur Biophys J, 2017","statement":[{"text":"For the protein MEG-14, as a result of its quite flexible and almost fully disordered state (Lopes et al. 2013), no spectral bands were observed at ~225-nm region (lacking any ordered content), but a negative peak of ~198 nm with similar shape was observed (Suppl. Figure 2a).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":1,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28258312","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-16T15:42:33.798Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":86,"region_id":"DP01970r003","released":"2022_12","ec_id":"ECO:0007689","reference_html":"Folding factors and partners for the intrinsically disordered protein micro-exon gene 14 (MEG-14). <i> Lopes JL, Orcia D, Araujo AP, DeMarco R, Wallace BA. </i> Biophys J, 2013","statement":[{"text":"The molecular mass of the recombinant MEG-14 was determined to be 10,613 ± 7 Da by MS (...) whereas SDS-PAGE analyses gave an apparent molecular mass of 13.7 kDa (Fig. 1 b). As observed for other IDPs (34, 35), the discrepancies between the sequence and hydrodynamic methods are a consequence of the extended (not globular) conformation of MEG-14 in solution and its high content of hydrophilic amino acids, which reduce its mobility on polyacrylamide gels because it binds less SDS.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":1,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0969-5438","date":"2022-09-20T14:23:06.133Z","reference_source":"pmid","term_name":"disorder","reference_id":"23746524","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-22T20:37:20.671Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":86,"region_id":"DP01970r004","released":"2022_12","ec_id":"ECO:0006202","reference_html":"Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins. <i> Kumagai PS, DeMarco R, Lopes JLS. </i> Eur Biophys J, 2017","statement":[{"text":"Moreover, a small band at ~184 nm could be observed in the SRCD spectra of IDPs, appearing as a shoulder for STI and a small positive peak for MEG-14 (Suppl. Figure 2c). This spectral band can also be attributed to the unordered content of the protein (Wallace and Janes 2009; Lopes et al. 2013).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":1,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"synchrotron radiation circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0969-5438","date":"2022-09-20T14:20:57.669Z","reference_source":"pmid","term_name":"disorder","reference_id":"28258312","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-22T20:37:19.630Z"}},{"start":1,"end":86,"reference_id":"27639541","reference_source":"pmid","reference_html":"Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response. <i> Orcia D, Zeraik AE, Lopes JLS, Macedo JNA, Santos CRD, Oliveira KC, Anderson L, Wallace BA, Verjovski-Almeida S, Araujo APU, DeMarco R. </i> Biochim Biophys Acta Gen Subj, 2017","date":"2022-10-25T09:27:35.089Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP01970r005","statement":[{"text":"The SRCD spectrum of sMEG-14 in aqueous solution is typical of a disordered protein with high flexibility, aspreviously described","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-19T18:05:55.035Z"}},{"start":1,"end":86,"reference_id":"27639541","reference_source":"pmid","reference_html":"Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response. <i> Orcia D, Zeraik AE, Lopes JLS, Macedo JNA, Santos CRD, Oliveira KC, Anderson L, Wallace BA, Verjovski-Almeida S, Araujo APU, DeMarco R. </i> Biochim Biophys Acta Gen Subj, 2017","date":"2022-10-25T09:35:46.898Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005805","ec_ontology":"ECO","ec_name":"yeast 2-hybrid evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P06702","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q6P1N0","operator":"or","partner_start":637,"partner_end":771}],"region_id":"DP01970r006","statement":[{"text":"To that end, a yeast two hybrid screening was performed using as bait the soluble portion of MEG-14\nisoform 1 (previously defined in [6]) and human leukocyte cDNA library as prey.d","type":"Results"},{"text":"Using these criteria, only two clones remained as positives, one containing a\ncDNA encoding S100A9 and another encoding the C2 Freud-1 domain from the\nCC2D1A protein.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-19T18:05:51.388Z"}},{"start":1,"end":86,"reference_id":"27639541","reference_source":"pmid","reference_html":"Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response. <i> Orcia D, Zeraik AE, Lopes JLS, Macedo JNA, Santos CRD, Oliveira KC, Anderson L, Wallace BA, Verjovski-Almeida S, Araujo APU, DeMarco R. </i> Biochim Biophys Acta Gen Subj, 2017","date":"2022-10-25T09:38:36.636Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P06702","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01970r007","statement":[{"text":"It was only possible to recover sMEG-14 in the fraction bound to the resin, after the washing steps, when this protein was incubated with S100A9-GST immobilized in a glutathionesepharose resin in the presence of calcium.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-19T18:05:09.258Z"}},{"start":1,"end":86,"reference_id":"27639541","reference_source":"pmid","reference_html":"Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response. <i> Orcia D, Zeraik AE, Lopes JLS, Macedo JNA, Santos CRD, Oliveira KC, Anderson L, Wallace BA, Verjovski-Almeida S, Araujo APU, DeMarco R. </i> Biochim Biophys Acta Gen Subj, 2017","date":"2022-10-25T09:40:55.559Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P06702","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01970r008","statement":[{"text":"Figure 3A shows a sensorgram indicating that both proteins interact immediately after S100A9 solution is applied onto the sensor chip surface in which sMEG-14 was covalently immobilized and that the intensity of the signal obtained is dependent on the concentration of S100A9 in the solution.","type":"Results"},{"text":"Experimental binding curves were fit in a plain 1:1 Langmuir binding model\nand the dissociation constant (Kd) calculated under this model for the MEG-14/S100A9 complex was 1.89 µM.","type":"Results"},{"text":"The interaction of sMEG14 with the heterodimer\nS100A9/S100A8 was also investigated by SPR, and although it was possible to observe interaction (Figure 3B), the affinity (Kd = 44.1 µM) has shown to be much lower than the observed for S100A9 alone.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-19T18:04:20.595Z"}},{"start":1,"end":86,"reference_id":"27639541","reference_source":"pmid","reference_html":"Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response. <i> Orcia D, Zeraik AE, Lopes JLS, Macedo JNA, Santos CRD, Oliveira KC, Anderson L, Wallace BA, Verjovski-Almeida S, Araujo APU, DeMarco R. </i> Biochim Biophys Acta Gen Subj, 2017","date":"2022-10-25T09:41:31.855Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006303","ec_ontology":"ECO","ec_name":"microscale thermophoresis evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P06702","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01970r009","statement":[{"text":"A profile suggestive of interaction between sMEG-14 and S100A9 was also obtained by performing an experiment of microscale thermophoresis (Supplementary Figure 3)","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-19T18:03:00.021Z"}},{"start":1,"end":86,"reference_id":"27639541","reference_source":"pmid","reference_html":"Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response. <i> Orcia D, Zeraik AE, Lopes JLS, Macedo JNA, Santos CRD, Oliveira KC, Anderson L, Wallace BA, Verjovski-Almeida S, Araujo APU, DeMarco R. </i> Biochim Biophys Acta Gen Subj, 2017","date":"2022-10-25T09:50:52.226Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P06702","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP01970r010","statement":[{"text":"Comparison of the spectrum produced by the sum of these two spectra with the spectra obtained experimentally for an equimolar mixture of these two proteins shows there is a significant red shift and increase in the peak magnitude at 184 nm. Changes of this type at this wavelength are primarily associated with a decrease in disordered content. In addition, a small increase of the peak at 222 nm was detected, thus suggesting a concomitant increase in alpha-helix content (Table 1). These results clearly show that the proteins physically interact to form a complex, and upon formation of the complex, they undergo a conformational change consistent with ordering of the MEG-14 partner.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-19T18:02:22.272Z"}},{"start":1,"end":86,"reference_id":"27639541","reference_source":"pmid","reference_html":"Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response. <i> Orcia D, Zeraik AE, Lopes JLS, Macedo JNA, Santos CRD, Oliveira KC, Anderson L, Wallace BA, Verjovski-Almeida S, Araujo APU, DeMarco R. </i> Biochim Biophys Acta Gen Subj, 2017","date":"2022-10-25T09:51:33.346Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP01970r011","statement":[{"text":"Comparison of the spectrum produced by the sum of these two spectra with the spectra obtained experimentally for an equimolar mixture of these two proteins shows there is a significant red shift and increase in the peak magnitude at 184 nm. Changes of this type at this wavelength are primarily associated with a decrease in disordered content. In addition, a small increase of the peak at 222 nm was detected, thus suggesting a concomitant increase in alpha-helix content (Table 1). These results clearly show that the proteins physically interact to form a complex, and upon formation of the complex, they undergo a conformational change consistent with ordering of the MEG-14 partner.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-19T18:01:32.587Z"}}],"released":"2018_11","uniref100":"UniRef100_M1GUG5","date":"2018-08-20T04:03:54.000Z","acc":"M1GUG5","name":"MEG-14","length":86,"organism":"Schistosoma mansoni","dataset":["Neglected tropical diseases proteins"],"UniParc":"UPI0002B29380","genes":[],"alphafold_very_low_content":0.10465116279069768,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":86,"type":"T"}],"Structural state":[{"start":1,"end":86,"type":"D"}],"Molecular function":[{"start":1,"end":86,"type":"F"}],"Structural transition":[{"start":1,"end":86,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00197","name":"Trypsin and protease inhibitor","start":3,"end":175}],"gene3D":[{"start":1,"end":177,"id":"2.80.10.50","name":"2.80.10.50"}]},"uniref50":"UniRef50_P01070","sequence":"DFVLDNEGNPLSNGGTYYILSDITAFGGIRAAPTGNERCPLTVVQSRNELDKGIGTIISSPFRIRFIAEGNPLRLKFDSFAVIMLCVGIPTEWSVVEDLPEGPAVKIGENKDAVDGWFRIERVSDDEFNNYKLVFCTQQAEDDKCGDIGISIDHDDGTRRLVVSKNKPLVVQFQKVDKESL","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","fabids","Fabales","Fabaceae","Papilionoideae","50 kb inversion clade","NPAAA clade","indigoferoid/millettioid clade","Phaseoleae","Glycine","Glycine subgen. Soja"],"uniref90":"UniRef90_P01070","disprot_id":"DP01971","ncbi_taxon_id":3847,"regions_counter":2,"creator":"ppere","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":181,"region_id":"DP01971r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins. <i> Kumagai PS, DeMarco R, Lopes JLS. </i> Eur Biophys J, 2017","statement":[{"text":"STI presents a CD spectrum of a protein lacking any content in helix, but presenting contributions of β-strands together with a high amount of disordered elements, known as βII class proteins...","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":1,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28258312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":181,"region_id":"DP01971r002","released":"2022_03","ec_id":"ECO:0006202","reference_html":"Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins. <i> Kumagai PS, DeMarco R, Lopes JLS. </i> Eur Biophys J, 2017","statement":[{"text":"Moreover, a small band at ~184 nm could be observed in the SRCD spectra of IDPs, appearing as a shoulder for STI and a small positive peak for MEG-14 (Suppl. Figure 2c). This spectral band can also be attributed to the unordered content of the protein...","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ppereira","start":1,"term_ontology":"IDPO","curator_name":"Pedro Pereira","ec_name":"synchrotron radiation circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0969-5438","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28258312","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P01071","date":"2018-08-20T04:06:50.000Z","acc":"P01071","name":"Trypsin inhibitor B","length":181,"organism":"Glycine max","dataset":[],"UniParc":"UPI000012DA67","genes":[],"alphafold_very_low_content":0.011049723756906077,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":181,"type":"D"}],"Structural state":[{"start":1,"end":181,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00838","name":"Translationally controlled tumour protein","start":1,"end":168}],"gene3D":[{"start":1,"end":172,"id":"2.170.150.10","name":"Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A"}]},"uniref50":"UniRef50_P13693","sequence":"MIIYRDLISHDEMFSDIYKIREIADGLCLEVEGKMVSRTEGNIDDSLIGGNASAEGPEGEGTESTVITGVDIVMNHHLQETSFTKEAYKKYIKDYMKSIKGKLEEQRPERVKPFMTGAAEQIKHILANFKNYQFFIGENMNPDGMVALLDYREDGVTPYMIFFKDGLEMEKC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P13693","disprot_id":"DP01972","ncbi_taxon_id":9606,"regions_counter":5,"creator":"mlambrughi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":68,"region_id":"DP01972r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Conformational Ensemble and Biological Role of the TCTP Intrinsically Disordered Region: Influence of Calcium and Phosphorylation. <i> Malard F, Assrir N, Alami M, Messaoudi S, Lescop E, Ha-Duong T. </i> J Mol Biol, 2018","statement":[{"text":"In this work, we combined NMR experiments and MD simulations to characterize the conformational ensemble of the TCTP intrinsically disordered loop, in the presence or not of calcium ions and with or without the phosphorylation of Ser46 and Ser64","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"mlambrughi","start":37,"term_ontology":"IDPO","curator_name":"Matteo Lambrughi","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-0894-8627","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29719201","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":68,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Conformational Ensemble and Biological Role of the TCTP Intrinsically Disordered Region: Influence of Calcium and Phosphorylation. <i> Malard F, Assrir N, Alami M, Messaoudi S, Lescop E, Ha-Duong T. </i> J Mol Biol, 2018","statement":[{"text":"we propose that the TCTP intrinsically disordered region could play an important role in participating to the interactions with other proteins and non-peptidic ligands, in remodeling the core domain surface, and modulating its accessibility to its partners in response to a variety of cellular conditions, in particularly the presence of calcium ions, or to chemical modifications, such as phosphorylations.","type":"Results"}],"term_id":"GO:0005515","curator_id":"mlambrughi","start":37,"term_ontology":"GO","curator_name":"Matteo Lambrughi","reference_id":"29719201","version":3,"curator_orcid":"0000-0002-0894-8627","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01972r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":68,"region_id":"DP01972r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure and mapping of a very weak calcium-binding site of human translationally controlled tumor protein by NMR. <i> Feng Y, Liu D, Yao H, Yao H, Wang J. </i> Arch Biochem Biophys, 2007","statement":[{"text":"in the loop of residues T39-V66 have 1H–15N NOE values <0.5 with an average value of −0.11 ± 0.49. This clearly indicates that hTCTP has a rather rigid well-folded core and a very flexible loop Lβ5β6, and the rigid to flexible transitions occur in the β-sheet C between these two structural regions. The analysis of R1 and R2 values also indicates the same conclusion.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mlambrughi","start":37,"term_ontology":"IDPO","curator_name":"Matteo Lambrughi","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-0894-8627","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17897616","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":61,"region_id":"DP01972r004","reference_id":"29216544","start":42,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Residues 1–41 and 62–180, and 1–40 and 64–180 were modeled for chains A and B of the hHRF-1 structure, respectively, and as in the mHRF structure, a substantial portion of the mobile loop region was disordered.","type":"Results"},{"text":"Residues 1–41 and 63–178, and 1–37 and 50–177 were modeled for chains A and B of the hHRF-2 structure, respectively.","type":"Results"},{"text":"Two structures of hHRF are described in the publication, hHRF-1 (PDB:5o9l) and hHRF-2 (PDB:5o9m), the latter revealing a disulphide-linked dimer","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Crystal structures of murine and human Histamine-Releasing Factor (HRF/TCTP) and a model for HRF dimerisation in mast cell activation. <i> Doré KA, Kashiwakura JI, McDonnell JM, Gould HJ, Kawakami T, Sutton BJ, Davies AM. </i> Mol Immunol, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5O9L"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":61,"region_id":"DP01972r005","reference_id":"29216544","start":42,"term_id":"GO:0098772","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"HRF crystal and solution structures have provided little insight into either the formation of disulphide-linked HRF dimers or the ability of HRF to activate mast cells.","type":"Abstract"},{"text":"The current model for the activity of HRF in mast cell activation involves cross-linking of FcεRI-bound IgE by dimeric HRF, mediated by interactions between HRF and the Fab regions of IgE","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"Crystal structures of murine and human Histamine-Releasing Factor (HRF/TCTP) and a model for HRF dimerisation in mast cell activation. <i> Doré KA, Kashiwakura JI, McDonnell JM, Gould HJ, Kawakami T, Sutton BJ, Davies AM. </i> Mol Immunol, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5O9L"}],"term_name":"molecular function regulator","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P13693","date":"2018-08-20T07:22:09.000Z","acc":"P13693","name":"Translationally-controlled tumor protein","length":172,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000000FED","genes":[{"name":{"value":"TPT1"}}],"alphafold_very_low_content":0.05232558139534884,"disorder_content":0.18604651162790697,"disprot_consensus":{"full":[{"start":37,"end":68,"type":"D"}],"Structural state":[{"start":37,"end":68,"type":"D"}],"Molecular function":[{"start":37,"end":68,"type":"F"}]}},{"features":{"pfam":[],"gene3D":[{"start":19,"end":215,"id":"1.10.490.10","name":"Globins"}]},"uniref50":"UniRef50_Q09514","sequence":"MGATLCAPKKKKTQVGASWVGNESENPFDLALNKKDRTLLRETWQRLDDPKDIVGLIFLDIVNDIEPDLKKVFGVDRAPRAAMLKMPKFGGHILRFYEFMEQLTSMLGTSENLTGAWQLVRKTGRSHVRQGFLEQNQNQMEKNYFEIVINVFIERLIPFLTGEQELPSSEGKENKKVRFAQNYTTSQITDVWKKFLNTVISQMTDSFELERAKQKSAQTTKALAPHQHIEISERKKKRVAEKQSEIENTAVSNEPKAQEQMFEDPF","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"uniref90":"UniRef90_Q09514","disprot_id":"DP01973","ncbi_taxon_id":6239,"regions_counter":3,"creator":"jlecle","regions":[{"region_id":"DP01973r001","ec_ontology":"ECO","end":18,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":1,"version":3,"statement":[{"text":"No electron density was detected for residues 1–18, 167–181 and 216–266.","type":"Methods"}],"term_name":"disorder","reference_html":"A redox signalling globin is essential for reproduction in Caenorhabditis elegans. <i> De Henau S, Tilleman L, Vangheel M, Luyckx E, Trashin S, Pauwels M, Germani F, Vlaeminck C, Vanfleteren JR, Bert W, Pesce A, Nardini M, Bolognesi M, De Wael K, Moens L, Dewilde S, Braeckman BP. </i> Nat Commun, 2015","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"26621324","date":"2024-02-07T16:48:18.280Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4BJA"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys6Ser","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30089","entry_name":"acetate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:4971"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":181,"region_id":"DP01973r002","released":"2024_06","ec_id":"ECO:0006220","reference_html":"A redox signalling globin is essential for reproduction in Caenorhabditis elegans. <i> De Henau S, Tilleman L, Vangheel M, Luyckx E, Trashin S, Pauwels M, Germani F, Vlaeminck C, Vanfleteren JR, Bert W, Pesce A, Nardini M, Bolognesi M, De Wael K, Moens L, Dewilde S, Braeckman BP. </i> Nat Commun, 2015","statement":[{"text":"No electron density was detected for residues 1–18, 167–181 and 216–266.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":167,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-07T16:49:05.581Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4BJA"}],"reference_id":"26621324","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys6Ser","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30089","entry_name":"acetate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:4971"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":266,"region_id":"DP01973r003","released":"2024_06","ec_id":"ECO:0006220","reference_html":"A redox signalling globin is essential for reproduction in Caenorhabditis elegans. <i> De Henau S, Tilleman L, Vangheel M, Luyckx E, Trashin S, Pauwels M, Germani F, Vlaeminck C, Vanfleteren JR, Bert W, Pesce A, Nardini M, Bolognesi M, De Wael K, Moens L, Dewilde S, Braeckman BP. </i> Nat Commun, 2015","statement":[{"text":"No electron density was detected for residues 1–18, 167–181 and 216–266.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":216,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-07T16:56:05.228Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4BJA"}],"reference_id":"26621324","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys6Ser","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30089","entry_name":"acetate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:4971"}]}],"released":"2018_11","uniref100":"UniRef100_Q09514","date":"2018-08-20T08:55:50.000Z","acc":"Q09514","name":"GLoBin related","length":266,"organism":"Caenorhabditis elegans","dataset":[],"UniParc":"UPI0000076BDD","genes":[{"name":{"value":"glb-12","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAA86764.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA86764.1"}},{"code":"ECO:0000313","source":{"name":"WormBase","id":"C52A11.2","url":"https://www.wormbase.org/db/seq/sequence?name=C52A11.2;class=Transcript"}}]},"orfNames":[{"value":"C52A11.2","evidences":[{"code":"ECO:0000313","source":{"name":"WormBase","id":"C52A11.2","url":"https://www.wormbase.org/db/seq/sequence?name=C52A11.2;class=Transcript"}}]},{"value":"CELE_C52A11.2","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAA86764.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA86764.1"}}]}]}],"alphafold_very_low_content":0.14285714285714285,"disorder_content":0.3157894736842105,"disprot_consensus":{"full":[{"start":1,"end":18,"type":"D"},{"start":167,"end":181,"type":"D"},{"start":216,"end":266,"type":"D"}],"Structural state":[{"start":1,"end":18,"type":"D"},{"start":167,"end":181,"type":"D"},{"start":216,"end":266,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00752","name":"XPG N-terminal domain","start":1,"end":107},{"id":"PF00867","name":"XPG I-region","start":149,"end":233}],"gene3D":[{"start":2,"end":357,"id":"3.40.50.1010","name":"5'-nuclease"}]},"uniref50":"UniRef50_P39748","sequence":"MGIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQFLIAVRQGGDVLQNEEGETTSHLMGMFYRTIRMMENGIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAEQEVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEASCAALVKAGKVYAAATEDMDCLTFGSPVLMRHLTASEAKKLPIQEFHLSRILQELGLNQEQFVDLCILLGSDYCESIRGIGPKRAVDLIQKHKSIEEIVRRLDPNKYPVPENWLHKEAHQLFLEPEVLDPESVELKWSEPNEEELIKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPKGSTKKKAKTGAAGKFKRGK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P39748","disprot_id":"DP01974","ncbi_taxon_id":9606,"regions_counter":3,"creator":"mlambrughi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":61,"region_id":"DP01974r001","released":"2024_06","ec_id":"ECO:0006165","reference_html":"Regional conformational flexibility couples substrate specificity and scissile phosphate diester selectivity in human flap endonuclease 1. <i> Bennet IA, Finger LD, Baxter NJ, Ambrose B, Hounslow AM, Thompson MJ, Exell JC, Shahari NNBM, Craggs TD, Waltho JP, Grasby JA. </i> Nucleic Acids Res, 2018","statement":[{"text":"Regions that showed particularly low R2/R1 ratios and low hNOE values were the α2–α3 loop, the arch region and the non-native C-terminal residues. These regions were associated with higher than average B-factors or lacked observable electron density in crystal structures (Figure ​(Figure1D1D–F and Supplementary Figure S2) (11,22).","type":"Results"},{"text":"The lowest S2 values (<0.5) were generally observed in the C-terminal tail, arch and α2–α3 loop residues, thereby indicating that these residues were extremely flexible in solution.","type":"Results"},{"text":"The observable regions of the arch, α2–α3 loop and C-terminal residues showed only small differences (≤1) (Figure ​(Figure4A4A and B), suggesting that these residues were disordered in the free protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":45,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-20T13:38:00.491Z","reference_source":"pmid","term_name":"disorder","reference_id":"29718417","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"BMRB","id":"27160"}],"sequence_construct":"GIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQFLIAVRQGGDVLQNEEGETTSHLMGMFYRTIRMMENGIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAEQEVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEASCAALVKAGKVYAAATEDMDCLTFGSPVLMRHLTASEAKKLPIQEFHLSRILQELGLNQEQFVDLCILLGSDYCESIRGIGPKRAVDLIQKHKSIEEIVRRLDPNKYPVPENWLHKEAHQLFLEPEVLDPESVELKWSEPNEEELIKFMCGEKQFSEERIRSGVKRLSKSRQGSTLEVLFQ"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":130,"region_id":"DP01974r002","released":"2024_06","ec_id":"ECO:0006165","reference_html":"Regional conformational flexibility couples substrate specificity and scissile phosphate diester selectivity in human flap endonuclease 1. <i> Bennet IA, Finger LD, Baxter NJ, Ambrose B, Hounslow AM, Thompson MJ, Exell JC, Shahari NNBM, Craggs TD, Waltho JP, Grasby JA. </i> Nucleic Acids Res, 2018","statement":[{"text":"Regions that showed particularly low R2/R1 ratios and low hNOE values were the α2–α3 loop, the arch region and the non-native C-terminal residues. These regions were associated with higher than average B-factors or lacked observable electron density in crystal structures (Figure ​(Figure1D1D–F and Supplementary Figure S2) (11,22).","type":"Results"},{"text":"The lowest S2 values (<0.5) were generally observed in the C-terminal tail, arch and α2–α3 loop residues, thereby indicating that these residues were extremely flexible in solution.","type":"Results"},{"text":"The observable regions of the arch, α2–α3 loop and C-terminal residues showed only small differences (≤1) (Figure ​(Figure4A4A and B), suggesting that these residues were disordered in the free protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":90,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-20T13:37:26.127Z","reference_source":"pmid","term_name":"disorder","reference_id":"29718417","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"BMRB","id":"27160"}],"sequence_construct":"GIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQFLIAVRQGGDVLQNEEGETTSHLMGMFYRTIRMMENGIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAEQEVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEASCAALVKAGKVYAAATEDMDCLTFGSPVLMRHLTASEAKKLPIQEFHLSRILQELGLNQEQFVDLCILLGSDYCESIRGIGPKRAVDLIQKHKSIEEIVRRLDPNKYPVPENWLHKEAHQLFLEPEVLDPESVELKWSEPNEEELIKFMCGEKQFSEERIRSGVKRLSKSRQGSTLEVLFQ"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":342,"region_id":"DP01974r003","released":"2024_06","ec_id":"ECO:0006165","reference_html":"Regional conformational flexibility couples substrate specificity and scissile phosphate diester selectivity in human flap endonuclease 1. <i> Bennet IA, Finger LD, Baxter NJ, Ambrose B, Hounslow AM, Thompson MJ, Exell JC, Shahari NNBM, Craggs TD, Waltho JP, Grasby JA. </i> Nucleic Acids Res, 2018","statement":[{"text":"Regions that showed particularly low R2/R1 ratios and low hNOE values were the α2–α3 loop, the arch region and the non-native C-terminal residues. These regions were associated with higher than average B-factors or lacked observable electron density in crystal structures (Figure ​(Figure1D1D–F and Supplementary Figure S2) (11,22).","type":"Results"},{"text":"The lowest S2 values (<0.5) were generally observed in the C-terminal tail, arch and α2–α3 loop residues, thereby indicating that these residues were extremely flexible in solution.","type":"Results"},{"text":"The observable regions of the arch, α2–α3 loop and C-terminal residues showed only small differences (≤1) (Figure ​(Figure4A4A and B), suggesting that these residues were disordered in the free protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":330,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-20T13:35:55.255Z","reference_source":"pmid","term_name":"disorder","reference_id":"29718417","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"BMRB","id":"27160"}],"sequence_construct":"GIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQFLIAVRQGGDVLQNEEGETTSHLMGMFYRTIRMMENGIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAEQEVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEASCAALVKAGKVYAAATEDMDCLTFGSPVLMRHLTASEAKKLPIQEFHLSRILQELGLNQEQFVDLCILLGSDYCESIRGIGPKRAVDLIQKHKSIEEIVRRLDPNKYPVPENWLHKEAHQLFLEPEVLDPESVELKWSEPNEEELIKFMCGEKQFSEERIRSGVKRLSKSRQGSTLEVLFQ"}],"released":"2018_11","uniref100":"UniRef100_P39748","date":"2018-08-20T09:02:47.000Z","acc":"P39748","name":"Flap endonuclease 1","length":380,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI0000050E0F","genes":[{"name":{"value":"FEN1","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03140","url":"https://hamap.expasy.org/unirule/MF_03140"}}]},"synonyms":[{"value":"RAD2"}]}],"alphafold_very_low_content":0.0868421052631579,"disorder_content":0.1868421052631579,"disprot_consensus":{"full":[{"start":45,"end":61,"type":"D"},{"start":90,"end":130,"type":"D"},{"start":330,"end":342,"type":"D"}],"Structural state":[{"start":45,"end":61,"type":"D"},{"start":90,"end":130,"type":"D"},{"start":330,"end":342,"type":"D"}]}},{"features":{"pfam":[{"id":"PF04146","name":"YT521-B-like domain","start":350,"end":476}],"gene3D":[{"start":316,"end":488,"id":"3.10.590.10","name":"ph1033 like domains"}]},"uniref50":"UniRef50_O74958","sequence":"MSNTNFSTSRSSKSIPELPNLEALRSLWPPPSLNESGDTRSVWTTHTGEPVASSVLSTSGSNNFSSPLKRPAPESHDAPIGRRLMVDDPRLIKHGKYDFSRHCTDYGHSYEWPYFRSLRRESMLYHTSGSYPESQPPYSSYSTDAPHYYHAGSESSAYYDSRSRLHGIQPPPKRRTLSPPPRRLADPVVVGSSRYVEEEVYRRPPYTLASEVPSSASAYQAGYSSYPVRSSPQLSHEDTRHGIASSGSTRYPFVPANTRASHSPSLLEPYAHSLPSSVAPVGAYPEKSSYLLSNSSNDSASRKEKPKARASTPPPLNFSRASEHRNEKGERISMINPRVVLDENGISHRSRYFIMLCDNETAIAHAKKTSIWAVKKDSSKRISDAYKKASVYFIFVAQQTYNALGYAQVVSDLNSTELPFWSDSSHAGGVRIKWIKTCNLFSAEISEIVSHMDHGSEARDGMEMMYDEGSRLCTLINYAIMKRIGRDR","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"uniref90":"UniRef90_O74958","disprot_id":"DP01975","ncbi_taxon_id":284812,"regions_counter":5,"creator":"mlambrughi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":327,"region_id":"DP01975r001","released":"2024_06","ec_id":"ECO:0006165","reference_html":"A low-complexity region in the YTH domain protein Mmi1 enhances RNA binding. <i> Stowell JAW, Wagstaff JL, Hill CH, Yu M, McLaughlin SH, Freund SMV, Passmore LA. </i> J Biol Chem, 2018","statement":[{"text":"Taken together, this indicates a highly dynamic domain with a rigid core consisting of the β-sheet and more flexible regions where only broad or no signals were observed. In total, only ∼60% of residues were assignable. This included only 14 confirmed residues in the low-complexity region, suggesting that the remainder of the signals from this region are missing due to line broadening; there were ∼50 fewer cross-peaks than expected, even in the BEST-TROSY experiment with nondeuterated protein.","type":"Results"},{"text":"This N-terminal, low-complexity region does not adopt any formal secondary structure but forms a stably-folded platform encompassing the N-clamp and extending across the YTH domain to contact the C-terminal helix (Fig. 8A).","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":282,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-20T14:47:28.981Z","reference_source":"pmid","term_name":"disorder","reference_id":"29695507","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"BMRB","id":"27398"}]},{"start":282,"end":327,"reference_id":"29695507","reference_source":"pmid","reference_html":"A low-complexity region in the YTH domain protein Mmi1 enhances RNA binding. <i> Stowell JAW, Wagstaff JL, Hill CH, Yu M, McLaughlin SH, Freund SMV, Passmore LA. </i> J Biol Chem, 2018","date":"2024-02-20T14:41:29.936Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003730","term_name":"mRNA 3'-UTR binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","region_id":"DP01975r003","statement":[{"text":"In contrast, the USR–YTH construct had a binding affinity of 6.1 ± 0.7 nm, ∼25-fold stronger than YTH (Fig. 1D). A similar trend was observed at lower salt (Table 1). Therefore, the USR stabilizes the interaction between the YTH domain and RNA.","type":"Results"},{"text":"The experiment confirmed the bising to an RNA substrate composed of a DSR sequence from the rec8 3′-UTR. DSR stands for determinants of selective removal.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a 3' untranslated region of an mRNA molecule.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"RNAcentral","id":"URS0000D56C42_4896","operator":"and","partner_start":null,"partner_end":null}]},{"start":282,"end":327,"reference_id":"29695507","reference_source":"pmid","reference_html":"A low-complexity region in the YTH domain protein Mmi1 enhances RNA binding. <i> Stowell JAW, Wagstaff JL, Hill CH, Yu M, McLaughlin SH, Freund SMV, Passmore LA. </i> J Biol Chem, 2018","date":"2024-02-20T14:53:04.954Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01975r004","statement":[{"text":"Finally, CD spectra recorded for all the constructs showed a similar line shape, although the magnitude of the signal at ∼225 nm increases as more of the low-complexity region is included (Fig. S1B). This can be characteristic of proteins with a molten-globule conformation (29).","type":"Discussion"}]},{"start":282,"end":327,"reference_id":"29695507","reference_source":"pmid","reference_html":"A low-complexity region in the YTH domain protein Mmi1 enhances RNA binding. <i> Stowell JAW, Wagstaff JL, Hill CH, Yu M, McLaughlin SH, Freund SMV, Passmore LA. </i> J Biol Chem, 2018","date":"2024-02-20T15:17:02.489Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"BMRB","id":"27399"},{"db":"BMRB","id":"27398"}],"region_id":"DP01975r005","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS0000D56C42_4896"}],"statement":[{"text":"Surprisingly, 31 additional amide peaks of the low-complexity region could be assigned in the presence of RNA (Fig. 5B, yellow lines). Some of these correspond to residues not observed in the crystal structure. Thus, in the presence of RNA, it is likely that the conformation of the USR and N-clamp become even more constrained, reducing the line broadening in NMR spectra and thereby leading to the appearance of additional protein amide peaks.","type":"Results"},{"text":"On RNA binding, these regions become more ordered and contact or reinforce contacts with RNA.","type":"Figure"}]}],"released":"2018_11","uniref100":"UniRef100_O74958","date":"2018-08-20T09:03:02.000Z","acc":"O74958","name":"YTH domain-containing protein mmi1","length":488,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","dataset":["RNA-binding proteins"],"UniParc":"UPI000006A028","genes":[{"name":{"value":"mmi1"},"orfNames":[{"value":"SPCC736.12c"}]}],"alphafold_very_low_content":0.4057377049180328,"disorder_content":0.0942622950819672,"disprot_consensus":{"full":[{"start":282,"end":327,"type":"T"}],"Structural state":[{"start":282,"end":327,"type":"D"}],"Molecular function":[{"start":282,"end":327,"type":"F"}],"Structural transition":[{"start":282,"end":327,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00291","name":"Pyridoxal-phosphate dependent enzyme","start":81,"end":376},{"id":"PF00571","name":"CBS domain","start":420,"end":468}],"gene3D":[{"start":84,"end":384,"id":"3.40.50.1100","name":"3.40.50.1100"},{"start":398,"end":551,"id":"3.10.580.10","name":"CBS-domain"},{"start":116,"end":229,"id":"3.40.50.1100","name":"3.40.50.1100"}]},"uniref50":"UniRef50_P35520","sequence":"MPSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKEPLWIRPDAPSRCTWQLGRPASESPHHHTAPAKSPKILPDILKKIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQIQYHSTGKSSQRQMVFGVVTAIDLLNFVAAQERDQK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P35520","disprot_id":"DP01976","ncbi_taxon_id":9606,"regions_counter":3,"creator":"mlambrughi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":40,"region_id":"DP01976r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Heme interaction of the intrinsically disordered N-terminal peptide segment of human cystathionine-β-synthase. <i> Kumar A, Wißbrock A, Goradia N, Bellstedt P, Ramachandran R, Imhof D, Ohlenschläger O. </i> Sci Rep, 2018","statement":[{"text":"The calculation of the chemical shift index based on the obtained resonance assignment indicates an intrinsically disordered peptide which is supported by the prediction of the web server (IUPRED53) using the primary sequence as sole input.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-06-19T12:21:46.273Z","reference_source":"pmid","term_name":"disorder","reference_id":"29410458","ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"ENLYFQGVDMPSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKE","cross_refs":[{"db":"BMRB","id":"27351"}],"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"It was cloned in pET28a vector with GB1 domain attached to N-terminal of CBS(1–40) with flexible linker (TEV protease site - ENLYFQG) to avoid proteolytic cleavage of CBS(1–40) and additionally increasing the yield with stability."}]}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":40,"term_name":"heme binding","released":"2023_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Heme interaction of the intrinsically disordered N-terminal peptide segment of human cystathionine-β-synthase. <i> Kumar A, Wißbrock A, Goradia N, Bellstedt P, Ramachandran R, Imhof D, Ohlenschläger O. </i> Sci Rep, 2018","statement":[{"text":"Here we report the NMR resonance assignment and heme interaction studies for the N-terminal peptide stretch of CBS. We present NMR-spectral evidence that residues 1–40 constitute an intrinsically disordered region in CBS and interact with heme via a cysteine-proline based motif.","type":"Abstract"},{"text":"Viewed in totality, the results reported here suggest that the wild-type N-terminal CBS peptide upon heme binding undergoes a conformational change to a hexacoordinated complex with cysteine-15 and histidine-22 as ligands that is sparsely populated and is in exchange with a highly populated free peptide.","type":"Results"},{"text":"We also observed that the single mutation C15S (Fig. 5c) essentially leads to no effect on the relative intensities of the cross peaks in the HSQC spectra upon heme addition. This indicates that mutation of this residue leads to no heme binding and is consistent with the UV/Vis data of this mutant which shows no sharp Soret peak (Supplementary Figure S5) either at ~420 nm (hexacoordination) or at ~370 nm (pentacoordination).","type":"Results"}],"term_id":"GO:0020037","curator_id":"vnugnes","start":1,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"29410458","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-06-19T12:21:22.607Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01976r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"It was cloned in pET28a vector with GB1 domain attached to N-terminal of CBS(1–40) with flexible linker (TEV protease site - ENLYFQG) to avoid proteolytic cleavage of CBS(1–40) and additionally increasing the yield with stability."}]}],"sequence_construct":"ENLYFQGVDMPSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKE"},{"start":1,"end":40,"reference_id":"29410458","reference_source":"pmid","reference_html":"Heme interaction of the intrinsically disordered N-terminal peptide segment of human cystathionine-β-synthase. <i> Kumar A, Wißbrock A, Goradia N, Bellstedt P, Ramachandran R, Imhof D, Ohlenschläger O. </i> Sci Rep, 2018","date":"2023-06-19T12:11:42.869Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0020037","term_name":"heme binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001258","ec_ontology":"ECO","ec_name":"spectrophotometry evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"EXP","region_id":"DP01976r003","statement":[{"text":"Thus, this bathochromic effect is characteristic of heme binding and suggests formation of a hexacoordinated state which in CBS involves residues cysteine-15 and histidine-22. The KD value was determined to be 2.18 ± 0.64 μM. According to the best fit possible GB1CBS(1–40) binds to heme with a 1:1 stoichiometry (Fig. 2b).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"The N-terminal CBS peptide (GB1CBS(1–40)), consisting of the residues 1–40 of CBS (MPSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKE), was expressed as fusion to the B1 domain of streptococcal protein G (GB1)45."}]}],"sequence_construct":"MPSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKE"}],"released":"2018_11","uniref100":"UniRef100_P35520","date":"2018-08-20T09:04:49.000Z","acc":"P35520","name":"Cystathionine beta-synthase","length":551,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI00001271F2","genes":[{"name":{"value":"CBS"}}],"alphafold_very_low_content":0.06352087114337568,"disorder_content":0.07259528130671507,"disprot_consensus":{"full":[{"start":1,"end":40,"type":"D"}],"Structural state":[{"start":1,"end":40,"type":"D"}],"Molecular function":[{"start":1,"end":40,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00493","name":"MCM P-loop domain","start":461,"end":683},{"id":"PF12619","name":"Mini-chromosome maintenance protein 2","start":62,"end":181},{"id":"PF14551","name":"MCM N-terminal domain","start":197,"end":286},{"id":"PF17207","name":"MCM OB domain","start":294,"end":420},{"id":"PF17855","name":"MCM AAA-lid domain","start":718,"end":802},{"id":"PF23669","name":"DNA replication licensing factor MCM2-like, winged-helix domain","start":826,"end":900}],"gene3D":[{"start":297,"end":444,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"},{"start":192,"end":290,"id":"3.30.1640.10","name":"mini-chromosome maintenance (MCM) complex, chain A, domain 1"},{"start":321,"end":371,"id":"2.20.28.10","name":"2.20.28.10"},{"start":457,"end":807,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_P49736","sequence":"MAESSESFTMASSPAQRRRGNDPLTSSPGRSSRRTDALTSSPGRDLPPFEDESEGLLGTEGPLEEEEDGEELIGDGMERDYRAIPELDAYEAEGLALDDEDVEELTASQREAAERAMRQRDREAGRGLGRMRRGLLYDSDEEDEERPARKRRQVERATEDGEEDEEMIESIENLEDLKGHSVREWVSMAGPRLEIHHRFKNFLRTHVDSHGHNVFKERISDMCKENRESLVVNYEDLAAREHVLAYFLPEAPAELLQIFDEAALEVVLAMYPKYDRITNHIHVRISHLPLVEELRSLRQLHLNQLIRTSGVVTSCTGVLPQLSMVKYNCNKCNFVLGPFCQSQNQEVKPGSCPECQSAGPFEVNMEETIYQNYQRIRIQESPGKVAAGRLPRSKDAILLADLVDSCKPGDEIELTGIYHNNYDGSLNTANGFPVFATVILANHVAKKDNKVAVGELTDEDVKMITSLSKDQQIGEKIFASIAPSIYGHEDIKRGLALALFGGEPKNPGGKHKVRGDINVLLCGDPGTAKSQFLKYIEKVSSRAIFTTGQGASAVGLTAYVQRHPVSREWTLEAGALVLADRGVCLIDEFDKMNDQDRTSIHEAMEQQSISISKAGIVTSLQARCTVIAAANPIGGRYDPSLTFSENVDLTEPIISRFDILCVVRDTVDPVQDEMLARFVVGSHVRHHPSNKEEEGLANGSAAEPAMPNTYGVEPLPQEVLKKYIIYAKERVHPKLNQMDQDKVAKMYSDLRKESMATGSIPITVRHIESMIRMAEAHARIHLRDYVIEDDVNMAIRVMLESFIDTQKFSVMRSMRKTFARYLSFRRDNNELLLFILKQLVAEQVTYQRNRFGAQQDTIEVPEKDLVDKARQINIHNLSAFYDSELFRMNKFSHDLKRKMILQQF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P49736","disprot_id":"DP01977","ncbi_taxon_id":9606,"regions_counter":9,"creator":"rdavidovic","regions":[{"region_id":"DP01977r001","ec_ontology":"ECO","end":160,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","start":1,"version":3,"statement":[{"text":"We purified a uniformly 15N labeled sample of human MCM2 (1–160) as a recombinant protein in E. coli and analyzed its structure by standard heteronuclear NMR techniques. Spectral dispersion of NH resonances demonstrates that this fragment is mainly disordered in solution (Supplementary Figure S2 in black).","type":"Results"}],"term_name":"disorder","reference_html":"Structural insight into how the human helicase subunit MCM2 may act as a histone chaperone together with ASF1 at the replication fork. <i> Richet N, Liu D, Legrand P, Velours C, Corpet A, Gaubert A, Bakail M, Moal-Raisin G, Guerois R, Compper C, Besle A, Guichard B, Almouzni G, Ochsenbein F. </i> Nucleic Acids Res, 2015","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"25618846","date":"2024-02-20T19:25:47.905Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified"}]},{"start":69,"end":138,"reference_id":"25618846","reference_source":"pmid","reference_html":"Structural insight into how the human helicase subunit MCM2 may act as a histone chaperone together with ASF1 at the replication fork. <i> Richet N, Liu D, Legrand P, Velours C, Corpet A, Gaubert A, Bakail M, Moal-Raisin G, Guerois R, Compper C, Besle A, Guichard B, Almouzni G, Ochsenbein F. </i> Nucleic Acids Res, 2015","date":"2024-02-20T19:23:45.158Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042393","term_name":"histone binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified"},{"term_id":"MI:0379","term_name":"13C label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P02299","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P84040","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01977r003","statement":[{"text":"Upon addition of full-length recombinant H3-H4 histones, two subsets of resonances from residues 71–96 and 104–133 vanish and delineate two segments of MCM2 in contact with histones (Figure ​(Figure1C),1C), one of them including the residual helix (107–122) identified above.","type":"Results"},{"text":"The histone binding region could thus be further restricted to the (69–138) segment.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a histone, any of a group of water-soluble proteins found in association with the DNA of eukaroytic chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in nonspecific suppression of gene activity.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":69,"end":138,"reference_id":"25618846","reference_source":"pmid","reference_html":"Structural insight into how the human helicase subunit MCM2 may act as a histone chaperone together with ASF1 at the replication fork. <i> Richet N, Liu D, Legrand P, Velours C, Corpet A, Gaubert A, Bakail M, Moal-Raisin G, Guerois R, Compper C, Besle A, Guichard B, Almouzni G, Ochsenbein F. </i> Nucleic Acids Res, 2015","date":"2024-02-20T19:24:39.010Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042393","term_name":"histone binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P02299","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P84040","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01977r004","statement":[{"text":"Affinities of MCM2 (1–160) and MCM2 (69–138) for histones were measured using ITC with dissociation constants of 0.19 ± 0.02 μM (Supplementary Figure S4A, Supplementary Table S1) and 0.24 ± 0.1 μM (Supplementary Figure S4B, Supplementary Table S1), respectively, confirming that the shorter region recapitulates all interactions made by the MCM2 N-terminal region with histones.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a histone, any of a group of water-soluble proteins found in association with the DNA of eukaroytic chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in nonspecific suppression of gene activity.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":69,"end":121,"reference_id":"25618846","reference_source":"pmid","reference_html":"Structural insight into how the human helicase subunit MCM2 may act as a histone chaperone together with ASF1 at the replication fork. <i> Richet N, Liu D, Legrand P, Velours C, Corpet A, Gaubert A, Bakail M, Moal-Raisin G, Guerois R, Compper C, Besle A, Guichard B, Almouzni G, Ochsenbein F. </i> Nucleic Acids Res, 2015","date":"2024-02-20T19:29:21.508Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042393","term_name":"histone binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"4UUZ"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P02299","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P84040","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP01977r005","statement":[{"text":"The MCM2 fragment (69–121) wraps around the H3-H4 dimer complex and follows the position of DNA in the nucleosome so that it clearly competes with the binding of DNA.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a histone, any of a group of water-soluble proteins found in association with the DNA of eukaroytic chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in nonspecific suppression of gene activity.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":69,"end":106,"reference_id":"25618846","reference_source":"pmid","reference_html":"Structural insight into how the human helicase subunit MCM2 may act as a histone chaperone together with ASF1 at the replication fork. <i> Richet N, Liu D, Legrand P, Velours C, Corpet A, Gaubert A, Bakail M, Moal-Raisin G, Guerois R, Compper C, Besle A, Guichard B, Almouzni G, Ochsenbein F. </i> Nucleic Acids Res, 2015","date":"2024-02-20T19:30:58.953Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"4UUZ"}],"region_id":"DP01977r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84040"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02299"}],"statement":[{"text":"The MCM2 fragment (69–121) wraps around the H3-H4 dimer complex and follows the position of DNA in the nucleosome so that it clearly competes with the binding of DNA. MCM2 residues G69-L97 and V102-R120 have extensive contacts with both histones H3 and H4 and adopt mainly an extended conformation interrupted by two helical segments: one helical turn involving residues M79-Y81 and a well-defined helix from residues A107 to R118.","type":"Results"}]},{"start":119,"end":138,"reference_id":"25618846","reference_source":"pmid","reference_html":"Structural insight into how the human helicase subunit MCM2 may act as a histone chaperone together with ASF1 at the replication fork. <i> Richet N, Liu D, Legrand P, Velours C, Corpet A, Gaubert A, Bakail M, Moal-Raisin G, Guerois R, Compper C, Besle A, Guichard B, Almouzni G, Ochsenbein F. </i> Nucleic Acids Res, 2015","date":"2024-02-20T19:31:20.098Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"4UUZ"}],"region_id":"DP01977r007","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84040"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02299"}],"statement":[{"text":"The MCM2 fragment (69–121) wraps around the H3-H4 dimer complex and follows the position of DNA in the nucleosome so that it clearly competes with the binding of DNA. MCM2 residues G69-L97 and V102-R120 have extensive contacts with both histones H3 and H4 and adopt mainly an extended conformation interrupted by two helical segments: one helical turn involving residues M79-Y81 and a well-defined helix from residues A107 to R118.","type":"Results"}]},{"start":107,"end":118,"reference_id":"25618846","reference_source":"pmid","reference_html":"Structural insight into how the human helicase subunit MCM2 may act as a histone chaperone together with ASF1 at the replication fork. <i> Richet N, Liu D, Legrand P, Velours C, Corpet A, Gaubert A, Bakail M, Moal-Raisin G, Guerois R, Compper C, Besle A, Guichard B, Almouzni G, Ochsenbein F. </i> Nucleic Acids Res, 2015","date":"2024-02-20T19:32:35.605Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"4UUZ"}],"region_id":"DP01977r008","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84040"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02299"}],"statement":[{"text":"The MCM2 fragment (69–121) wraps around the H3-H4 dimer complex and follows the position of DNA in the nucleosome so that it clearly competes with the binding of DNA. MCM2 residues G69-L97 and V102-R120 have extensive contacts with both histones H3 and H4 and adopt mainly an extended conformation interrupted by two helical segments: one helical turn involving residues M79-Y81 and a well-defined helix from residues A107 to R118.","type":"Results"}]},{"start":107,"end":118,"reference_id":"25618846","reference_source":"pmid","reference_html":"Structural insight into how the human helicase subunit MCM2 may act as a histone chaperone together with ASF1 at the replication fork. <i> Richet N, Liu D, Legrand P, Velours C, Corpet A, Gaubert A, Bakail M, Moal-Raisin G, Guerois R, Compper C, Besle A, Guichard B, Almouzni G, Ochsenbein F. </i> Nucleic Acids Res, 2015","date":"2024-02-20T19:33:44.466Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"4UUZ"}],"region_id":"DP01977r009","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84040"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02299"}],"statement":[{"text":"The MCM2 fragment (69–121) wraps around the H3-H4 dimer complex and follows the position of DNA in the nucleosome so that it clearly competes with the binding of DNA. MCM2 residues G69-L97 and V102-R120 have extensive contacts with both histones H3 and H4 and adopt mainly an extended conformation interrupted by two helical segments: one helical turn involving residues M79-Y81 and a well-defined helix from residues A107 to R118.","type":"Results"}],"states_connection":[{"source":"DP01977r001","target":"DP01977r008"}]}],"released":"2018_11","uniref100":"UniRef100_P49736","date":"2018-08-20T10:43:55.000Z","acc":"P49736","name":"DNA replication licensing factor MCM2","length":904,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000016AABB","genes":[{"name":{"value":"MCM2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6944","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6944"}}]},"synonyms":[{"value":"BM28"},{"value":"CCNL1"},{"value":"CDCL1"},{"value":"KIAA0030"}]}],"alphafold_very_low_content":0.13827433628318583,"disorder_content":0.17699115044247787,"disprot_consensus":{"full":[{"start":1,"end":106,"type":"D"},{"start":107,"end":118,"type":"T"},{"start":119,"end":160,"type":"D"}],"Structural state":[{"start":1,"end":160,"type":"D"}],"Molecular function":[{"start":69,"end":138,"type":"F"}],"Structural transition":[{"start":107,"end":118,"type":"T"}]}},{"features":{"pfam":[{"id":"PF04037","name":"Domain of unknown function (DUF382)","start":143,"end":275},{"id":"PF04046","name":"PSP","start":290,"end":335}]},"uniref50":"UniRef50_Q02554","sequence":"MARTKSRKRSGNNQNKNASVVNNKAEIAAMIDARRLEQKKKGGVTNSKGKTNKVVDAKLEKEFKDVLQRFQVQENDTPKEITKDEKNNHVVIVEKNPVMNRKHTAEDELEDTPSDGIEEHLSARKRRKTEKPSLSQLKSQVPYPQIIEWYDCDARYPGLLASIKCTKNVIPVPSHWQSKKEYLSGRSLLGKRPFELPDIIKKTNIEQMRSTLPQSGLDGQDEKSLKEASRARVQPKMGALDLDYKKLHDVFFKIGANWKPDHLLCFGDVYYENRNLFEETNWKRMVDHKRPGRISQELRAIMNLPEGQLPPWCMKMKDIGLPTGYPDLKIAGLNWDITNLKGDVYGKIIPNHHSRSKKQGRNYFGALISFETPEFENSKEDTQANAENGRQDDKIDDEVEHKLDHFQEDISEVTSAEEKLERNEEESEKQLYTVLK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q02554","disprot_id":"DP01978","ncbi_taxon_id":559292,"regions_counter":1,"creator":"viglesias","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":368,"region_id":"DP01978r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of U2 snRNP SF3b components: Hsh49p in complex with Cus1p-binding domain. <i> van Roon AM, Oubridge C, Obayashi E, Sposito B, Newman AJ, Séraphin B, Nagai K. </i> RNA, 2017","statement":[{"text":"Crystals contained Cus1(290–368)p but residues 351–368 were disordered.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"viglesias","start":351,"term_ontology":"IDPO","curator_name":"Valentín Iglesias","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6133-0869","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"28348170","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q02554","date":"2018-08-20T10:45:23.000Z","acc":"Q02554","name":"Cold sensitive U2 snRNA suppressor 1","length":436,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000053202","genes":[{"name":{"value":"CUS1"},"orfNames":[{"value":"YM9408.02C"}],"olnNames":[{"value":"YMR240C"}]}],"alphafold_very_low_content":0.2981651376146789,"disorder_content":0.04128440366972477,"disprot_consensus":{"full":[{"start":351,"end":368,"type":"D"}],"Structural state":[{"start":351,"end":368,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03810","name":"Importin-beta N-terminal domain","start":26,"end":90},{"id":"PF25574","name":"Importin subunit beta-1-like, TPR repeats","start":397,"end":535},{"id":"PF25780","name":"IPO5-like, TPR repeats","start":97,"end":230}],"gene3D":[{"start":1,"end":1100,"id":"1.25.10.10","name":"Leucine-rich Repeat Variant"}]},"uniref50":"UniRef50_P40069","sequence":"MDQQFVAQLEQALGAIVQPTGSLKDATKTLQSQFYTQSAALPALIHILQNSSNDGIKQLAGVEARKQVSKHWGSLDAATQTSVKQSLLNSAFNEGKDAVRHANARVIASIGSEELDEKKWPELIPNLLQAACDSNPKIRETAIFIILSLLESFNANLALHIDDFLNLFAQTINDSASLETRSLSAQALSYVSSLIEEEGEINPQYAAKFASLIPSVVQVLDATIREGDTTNTKLIFNCLNDFLLLDSQLTGNTIADLVKLALQIAVNSDVDEDIRVFAVQFVTSALVYRKSKINQAKLGPEITLAALKVASEEIDVEDELTNEDEAGENEENTPALTALRLISNASGELSPSQVGVPIIEHLPTMLSSSNPFERRSILLAISVLVTGSPDYTLSQFDKIIPATVTGLKDSEAVVQLAALKCIVQLSTNLQDEVARYHEQYLPLVIDIIDSAKHVVIYKYATLALDGLLEFIAHNDIIKYLDPLMNKLFQMLETQQSPKLRAAIVSAIGSCAFAAGSGFVPYFKTSVQYLQQFIQNVSQIEGLSEDDIELKALTFENISTMGRAVKSAAFAEYAEPLVNAAYEAIKTDSARLRESGYAFIANMAKVYGKDFAPFLQTIIPEIFKTLEQEEYQFNFDGDEDFLEGIEDLDEEELQSKFTVNTGIAYEKEVAAAALSELAIASKEHFLEYVEPSLKVLAEQVNESYGLKETALHSMWAIVKAVLLTANLKEGEYPKGVPSGSYVDASALAVIQTVREVSLNNVIEEVETSMVISVFQDLSEMLRLFGPIIIMDNGDSTHLDQLCREALSVLKGEHACQTIHFEEDVPEDEDLDASETEATLLDVALDIYVALSTNLVGGFAQVFTTAKPVILQLCQSKSKNKRSFAVGALSEIALGMRDENPFIQELLEALIISLTNDKSLEVRCNASYGVGLLIEYSSFDVSAIYSPVLKSLYEILSVADEKNLATEDDEATKEIVDRTFSNVCGCVARMILKHQNLVPLEHTIPALLSHLPFNTAFEEYDPIFKLFLKLFQEQNSTIINEAPKVIAIFATVFEKESERIELETNSTLGREENLEKRKQFQSEEIKQQVIELLKHLNQQFNGAVAQNPVLAQVIA","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Kluyveromyces"],"uniref90":"UniRef90_W0TIN4","disprot_id":"DP01979","ncbi_taxon_id":284590,"regions_counter":3,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":39,"region_id":"DP01979r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure-based nuclear import mechanism of histones H3 and H4 mediated by Kap123. <i> An S, Yoon J, Kim H, Song JJ, Cho US. </i> Elife, 2017","statement":[{"text":"The first HEAT repeat (residues 1–39), an intra-\nloop of repeat 8 (residues 325–329), repeat 15 (residues 631–656) and repeat 18 (residues 818–828)\nare disordered in the final structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":1,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5VCH"}],"reference_id":"29035199","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":656,"region_id":"DP01979r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure-based nuclear import mechanism of histones H3 and H4 mediated by Kap123. <i> An S, Yoon J, Kim H, Song JJ, Cho US. </i> Elife, 2017","statement":[{"text":"The first HEAT repeat (residues 1–39), an intra-\nloop of repeat 8 (residues 325–329), repeat 15 (residues 631–656) and repeat 18 (residues 818–828)\nare disordered in the final structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":631,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5VCH"}],"reference_id":"29035199","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":828,"region_id":"DP01979r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure-based nuclear import mechanism of histones H3 and H4 mediated by Kap123. <i> An S, Yoon J, Kim H, Song JJ, Cho US. </i> Elife, 2017","statement":[{"text":"The first HEAT repeat (residues 1–39), an intra-\nloop of repeat 8 (residues 325–329), repeat 15 (residues 631–656) and repeat 18 (residues 818–828)\nare disordered in the final structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":818,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5VCH"}],"reference_id":"29035199","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q6CMF0","date":"2018-08-20T11:06:33.000Z","acc":"Q6CMF0","name":"KLLA0E20769p","length":1113,"organism":"Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)","dataset":[],"UniParc":"UPI00003BB1B0","genes":[{"orfNames":[{"value":"KLLA0_E20769g","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAG99976.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAG99976.1"}}]}]}],"alphafold_very_low_content":0.015274034141958671,"disorder_content":0.06828391734052111,"disprot_consensus":{"full":[{"start":1,"end":39,"type":"D"},{"start":631,"end":656,"type":"D"},{"start":818,"end":828,"type":"D"}],"Structural state":[{"start":1,"end":39,"type":"D"},{"start":631,"end":656,"type":"D"},{"start":818,"end":828,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00781","name":"Diacylglycerol kinase catalytic domain","start":8,"end":129},{"id":"PF19279","name":"YegS C-terminal NAD kinase beta sandwich-like domain","start":150,"end":288}],"gene3D":[{"start":25,"end":287,"id":"3.40.50.10330","name":"Probable inorganic polyphosphate/atp-NAD kinase; domain 1"},{"start":126,"end":284,"id":"2.60.200.40","name":"2.60.200.40"}]},"uniref50":"UniRef50_P76407","sequence":"MAEFPASLLILNGKSTDNLPLREAIMLLREEGMTIHVRVTWEKGDAARYVEEARKFGVATVIAGGGDGTINEVSTALIQCEGDDIPALGILPLGTANDFATSVGIPEALDKALKLAIAGDAIAIDMAQVNKQTCFINMATGGFGTRITTETPEKLKAALGSVSYIIHGLMRMDTLQPDRCEIRGENFHWQGDALVIGIGNGRQAGGGQQLCPNALINDGLLQLRIFTGDEILPALVSTLKSDEDNPNIIEGASSWFDIQAPHDITFNLDGEPLSGQNFHIEILPAALRCRLPPDCPLLR","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P76407","disprot_id":"DP01981","ncbi_taxon_id":83333,"regions_counter":1,"creator":"viglesias","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":158,"region_id":"DP01981r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of YegS, a homologue to the mammalian diacylglycerol kinases, reveals a novel regulatory metal binding site. <i> Bakali HM, Herman MD, Johnson KA, Kelly AA, Wieslander A, Hallberg BM, Nordlund P. </i> J Biol Chem, 2007","statement":[{"text":"The disordered region 147–158...","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"viglesias","start":147,"term_ontology":"IDPO","curator_name":"Valentín Iglesias","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6133-0869","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2BON"}],"reference_id":"17351295","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P76407","date":"2018-08-20T13:36:52.000Z","acc":"P76407","name":"Lipid kinase YegS","length":299,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI000013AC3C","genes":[{"name":{"value":"yegS"},"olnNames":[{"value":"b2086"},{"value":"JW2070"}]}],"alphafold_very_low_content":0.043478260869565216,"disorder_content":0.04013377926421405,"disprot_consensus":{"full":[{"start":147,"end":158,"type":"D"}],"Structural state":[{"start":147,"end":158,"type":"D"}]}},{"features":{"pfam":[{"id":"PF25890","name":"Osteocalcin, C-terminal domain","start":14,"end":47}]},"uniref50":"UniRef50_Q8HYY9","sequence":"YLDHGLGAPAPYPDPLEPRREVCELNPDCDELADHIGFQEAYRRFYGIA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Suina","Suidae","Sus"],"uniref90":"UniRef90_Q8HYY9","disprot_id":"DP01982","ncbi_taxon_id":9823,"regions_counter":1,"creator":"jlecle","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":12,"region_id":"DP01982r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Bone recognition mechanism of porcine osteocalcin from crystal structure. <i> Hoang QQ, Sicheri F, Howard AJ, Yang DS. </i> Nature, 2003","statement":[{"text":"The N-terminal 12 residues are disordered and so excluded from the final model.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"jlecle","start":1,"term_ontology":"IDPO","curator_name":"Jeremy Y Leclercq","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0372-3277","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1Q8H"}],"reference_id":"14586470","validated":{"curator_name":"Rita Pancsa","curator_id":"rpancsa","timestamp":"2021-06-18T20:28:11.112Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q8HYY9","date":"2018-08-20T14:16:55.000Z","acc":"Q8HYY9","name":"Osteocalcin","length":49,"organism":"Sus scrofa","dataset":["Extracellular matrix proteins"],"UniParc":"UPI000053E862","genes":[{"name":{"value":"BGLAP"}}],"alphafold_very_low_content":0.14285714285714285,"disorder_content":0.24489795918367346,"disprot_consensus":{"full":[{"start":1,"end":12,"type":"D"}],"Structural state":[{"start":1,"end":12,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03287","name":"Poxvirus C7/F8A protein","start":4,"end":150}]},"uniref50":"UniRef50_Q9Q907","sequence":"MEEGIVHKLDVFLIDENVSIKHVNLFDGDSYGCNIHLKTATCKYITFILVLEPDWENIVEAKPIHMRLNGKKIRVPLVAKTHTSLIYKVVIYVEEDALARFYSDVERSYTDVYPTFLVNTDTRRYYILDSGRTYTYIDPFISDGDKRRWLTREIEEAYDASTEEEEEDDTEEDMDTVHLYCLEEEDEEKIADTGNDNQKDAED","taxonomy":["Viruses","Varidnaviria","Bamfordvirae","Nucleocytoviricota","Pokkesviricetes","Chitovirales","Poxviridae","Chordopoxvirinae","Leporipoxvirus"],"uniref90":"UniRef90_Q9Q8N4","disprot_id":"DP01983","ncbi_taxon_id":31530,"regions_counter":1,"creator":"jlecle","regions":[{"region_id":"DP01983r001","ec_ontology":"ECO","end":203,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":151,"version":3,"statement":[{"text":"The structure lacks the 53 C-terminal residues, presumably because these residues were disordered in the crystal packing or degraded during the extended crystallization period.","type":"Methods"}],"term_name":"disorder","reference_html":"Structural basis for antagonizing a host restriction factor by C7 family of poxvirus host-range proteins. <i> Meng X, Krumm B, Li Y, Deng J, Xiang Y. </i> Proc Natl Acad Sci U S A, 2015","released":"2022_03","term_ontology":"IDPO","curator_name":"Julian Bergier","reference_id":"26578811","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5CZ3"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"jbergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-01T11:15:28.643Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9Q8N4","date":"2018-08-20T15:12:37.000Z","acc":"Q9Q8N4","name":"Probable host range protein 2-3","length":203,"organism":"Myxoma virus (strain Lausanne)","dataset":["Viral proteins"],"UniParc":"UPI0000138783","genes":[{"olnNames":[{"value":"m064R"}]}],"disorder_content":0.26108374384236455,"disprot_consensus":{"full":[{"start":151,"end":203,"type":"D"}],"Structural state":[{"start":151,"end":203,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00740","name":"Parvovirus coat protein VP1/VP2","start":207,"end":704},{"id":"PF08398","name":"Phospholipase A2-like domain","start":43,"end":122}],"gene3D":[{"start":214,"end":733,"id":"2.170.30.10","name":"Parvovirus coat protein VP1/VP2"}]},"uniref50":"UniRef50_P03135","sequence":"MAADGYLPDWLEDNLSEGIREWWDLKPGAPKPKANQQKQDDGRGLVLPGYKYLGPFNGLDKGEPVNAADAAALEHDKAYDQQLKAGDNPYLRYNHADAEFQERLQEDTSFGGNLGRAVFQAKKRVLEPLGLVEEGAKTAPGKKRPLESPQEPDSSSGIGKKGKQPAKKRLNFEEDTGAGDGPPEGSDTSAMSSDIEMRAAPGGNAVDAGQGSDGVGNASGDWHCDSTWSEGKVTTTSTRTWVLPTYNNHLYLRLGTTSNSNTYNGFSTPWGYFDFNRFHCHFSPRDWQRLINNNWGLRPKAMRVKIFNIQVKEVTTSNGETTVANNLTSTVQIFADSSYELPYVMDAGQEGSLPPFPNDVFMVPQYGYCGIVTGENQNQTDRNAFYCLEYFPSQMLRTGNNFEMAYNFEKVPFHSMYAHSQSLDRLMNPLLDQYLWHLQSTTSGETLNQGNAATTFGKIRSGDFAFYRKNWLPGPCVKQQRFSKTASQNYKIPASGGNALLKYDTHYTLNNRWSNIAPGPPMATAGPSDGDFSNAQLIFPGPSVTGNTTTSANNLLFTSEEEIAATNPRDTDMFGQIADNNQNATTAPITGNVTAMGVLPGMVWQNRDIYYQGPIWAKIPHADGHFHPSPLIGGFGLKHPPPQIFIKNTPVPANPATTFTAARVDSFITQYSTGQVAVQIEWEIEKERSKRWNPEVQFTSNYGNQSSMLWAPDTTGKYTEPRVIGSRYLTNHL","taxonomy":["Viruses","Monodnaviria","Shotokuvirae","Cossaviricota","Quintoviricetes","Piccovirales","Parvoviridae","Parvovirinae","Dependoparvovirus","unclassified Dependoparvovirus"],"uniref90":"UniRef90_Q808X9","disprot_id":"DP01984","ncbi_taxon_id":272636,"regions_counter":1,"creator":"jlecle","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":213,"region_id":"DP01984r001","start":1,"ec_id":"ECO:0006220","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Amino acid residues 1 to 213, which includes the first eleven residues of VP3, were not ordered in the density maps. The lack of ordering of the N-terminus region of VP1–VP3 is consistent with all known parvovirus structures determined to date, except for B19 in which the entire VP2 was observed in a structure determined by cryo-electron microscopy.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24704217","version":3,"reference_html":"The structure of AAVrh32.33, a novel gene delivery vector. <i> Mikals K, Nam HJ, Van Vliet K, Vandenberghe LH, Mays LE, McKenna R, Wilson JM, Agbandje-McKenna M. </i> J Struct Biol, 2014","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","cross_refs":[{"db":"PDB","id":"4IOV"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-02T09:11:51.174Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_B4Y891","date":"2018-08-20T15:53:36.000Z","acc":"B4Y891","name":"Capsid protein VP1","length":733,"organism":"Adeno-associated virus","dataset":["Viral proteins"],"UniParc":"UPI0000F0833F","genes":[],"disorder_content":0.29058663028649384,"disprot_consensus":{"full":[{"start":1,"end":213,"type":"D"}],"Structural state":[{"start":1,"end":213,"type":"D"}]}},{"features":{"pfam":[{"id":"PF08123","name":"Histone methylation protein DOT1","start":115,"end":317}],"gene3D":[{"start":4,"end":124,"id":"1.10.260.60","name":"1.10.260.60"},{"start":125,"end":344,"id":"3.40.50.150","name":"Vaccinia Virus protein VP39"}]},"uniref50":"UniRef50_Q8TEK3","sequence":"MGEKLELRLKSPVGAEPAVYPWPLPVYDKHHDAAHEIIETIRWVCEEIPDLKLAMENYVLIDYDTKSFESMQRLCDKYNRAIDSIHQLWKGTTQPMKLNTRPSTGLLRHILQQVYNHSVTDPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTDDDLFVDLGSGVGQVVLQVAAATNCKHHYGVEKADIPAKYAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERIANTSVIFVNNFAFGPEVDHQLKERFANMKEGGRIVSSKPFAPLNFRINSRNLSDIGTIMRVVELSPLKGSVSWTGKPVSYYLHTIDRTILENYFSSLKNPKLREEQEAARRRQQRESKSNAATPTKGPEGKVAGPADAPMDSGAEEEKAGAATVKKPSPSKARKKKLNKKGRKMAGRKRGRPKKMNTANPERKPKKNQTALDALHAQTVSQTAASSPQDAYRSPHSPFYQLPPSVQRHSPNPLLVAPTPPALQKLLESFKIQYLQFLAYTKTPQYKASLQELLGQEKEKNAQLLGAAQQLLSHCQAQKEEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEQDNRALRGQSLQLLKARCEELQLDWATLSLEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQRQQELLQLKSCVPPDDALSLHLRGKGALGRELEPDASRLHLELDCTKFSLPHLSSMSPELSMNGQAAGYELCGVLSRPSSKQNTPQYLASPLDQEVVPCTPSHVGRPRLEKLSGLAAPDYTRLSPAKIVLRRHLSQDHTVPGRPAASELHSRAEHTKENGLPYQSPSVPGSMKLSPQDPRPLSPGALQLAGEKSSEKGLRERAYGSSGELITSLPISIPLSTVQPNKLPVSIPLASVVLPSRAERARSTPSPVLQPRDPSSTLEKQIGANAHGAGSRSLALAPAGFSYAGSVAISGALAGSPASLTPGAEPATLDESSSSGSLFATVGSRSSTPQHPLLLAQPRNSLPASPAHQLSSSPRLGGAAQGPLPEASKGDLPSDSGFSDPESEAKRRIVFTITTGAGSAKQSPSSKHSPLTASARGDCVPSHGQDSRRRGRRKRASAGTPSLSAGVSPKRRALPSVAGLFTQPSGSPLNLNSMVSNINQPLEITAISSPETSLKSSPVPYQDHDQPPVLKKERPLSQTNGAHYSPLTSDEEPGSEDEPSSARIERKIATISLESKSPPKTLENGGGLAGRKPAPAGEPVNSSKWKSTFSPISDIGLAKSADSPLQASSALSQNSLFTFRPALEEPSADAKLAAHPRKGFPGSLSGADGLSPGTNPANGCTFGGGLAADLSLHSFSDGASLPHKGPEAAGLSSPLSFPSQRGKEGSDANPFLSKRQLDGLAGLKGEGSRGKEAGEGGLPLCGPTDKTPLLSGKAAKARDREVDLKNGHNLFISAAAVPPGSLLSGPGLAPAASSAGGAASSAQTHRSFLGPFPPGPQFALGPMSLQANLGSVAGSSVLQSLFSSVPAAAGLVHVSSAATRLTNSHAMGSFSGVAGGTVGGN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q8TEK3","disprot_id":"DP01985","ncbi_taxon_id":9606,"regions_counter":2,"creator":"viglesias","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":416,"region_id":"DP01985r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase. <i> Min J, Feng Q, Li Z, Zhang Y, Xu RM. </i> Cell, 2003","statement":[{"text":"Amino acids C-terminal to αK (aa 333–416) are disordered in the structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"viglesias","start":333,"term_ontology":"IDPO","curator_name":"Valentín Iglesias","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6133-0869","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1NW3"}],"reference_id":"12628190","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":416,"term_name":"nucleic acid binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase. <i> Min J, Feng Q, Li Z, Zhang Y, Xu RM. </i> Cell, 2003","statement":[{"text":"Our modeling of hDOT1L-nucleosome interaction suggests that the C-terminal region is near DNA, which led us to hypothesize that the disordered C-terminal positively charged region might be involved in substrate binding by interacting with the negatively charged nucleosomal DNA.","type":"Results"}],"term_id":"GO:0003676","curator_id":"viglesias","start":333,"term_ontology":"GO","curator_name":"Valentín Iglesias","reference_id":"12628190","version":3,"curator_orcid":"0000-0002-6133-0869","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01985r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q8TEK3","date":"2018-08-20T17:04:29.000Z","acc":"Q8TEK3","name":"Histone-lysine N-methyltransferase, H3 lysine-79 specific","length":1537,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000169CA3","genes":[{"name":{"value":"DOT1L","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:24948","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:24948"}}]},"synonyms":[{"value":"KIAA1814"},{"value":"KMT4"}]}],"alphafold_very_low_content":0.6473649967469096,"disorder_content":0.05465191932335719,"disprot_consensus":{"full":[{"start":333,"end":416,"type":"D"}],"Structural state":[{"start":333,"end":416,"type":"D"}],"Molecular function":[{"start":333,"end":416,"type":"F"}]}},{"features":{"pfam":[{"id":"PF15247","name":"Histone RNA hairpin-binding protein RNA-binding domain","start":130,"end":199}],"gene3D":[{"start":127,"end":199,"id":"1.10.8.1120","name":"Histone RNA hairpin-binding protein RNA-binding domain"}]},"uniref50":"UniRef50_Q14493","sequence":"MACRPRSPPRHQSRCDGDASPPSPARWSLGRKRRADGRRWRPEDAEEAEHRGAERRPESFTTPEGPKPRSRCSDWASAVEEDEMRTRVNKEMARYKRKLLINDFGRERKSSSGSSDSKESMSTVPADFETDESVLMRRQKQINYGKNTIAYDRYIKEVPRHLRQPGIHPKTPNKFKKYSRRSWDQQIKLWKVALHFWDPPAEEGCDLQEIHPVDLESAESSSEPQTSSQDDFDVYSGTPTKVRHMDSQVEDEFDLEACLTEPLRDFSAMS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q14493","disprot_id":"DP01987","ncbi_taxon_id":9606,"regions_counter":1,"creator":"achasapi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":224,"region_id":"DP01987r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Molecular mechanisms for the regulation of histone mRNA stem-loop-binding protein by phosphorylation. <i> Zhang J, Tan D, DeRose EF, Perera L, Dominski Z, Marzluff WF, Tong L, Hall TM. </i> Proc Natl Acad Sci U S A, 2014","term_id":"IDPO:0000002","curator_id":"ahatos","start":200,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4QOZ"}],"reference_id":"25002523","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q14493","date":"2018-08-21T08:02:16.000Z","acc":"Q14493","name":"Histone RNA hairpin-binding protein","length":270,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000135A0D","genes":[{"name":{"value":"SLBP"},"synonyms":[{"value":"HBP"}]}],"alphafold_very_low_content":0.17777777777777778,"disorder_content":0.09259259259259259,"disprot_consensus":{"full":[{"start":200,"end":224,"type":"D"}],"Structural state":[{"start":200,"end":224,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01064","name":"Activin types I and II receptor domain","start":58,"end":135},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":234,"end":520},{"id":"PF08515","name":"Transforming growth factor beta type I GS-motif","start":205,"end":232}],"gene3D":[{"start":196,"end":313,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":57,"end":152,"id":"2.10.60.10","name":"CD59"},{"start":314,"end":532,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"}]},"uniref50":"UniRef50_P36894","sequence":"MPQLYIYIRLLGAYLFIISRVQGQNLDSMLHGTGMKSDSDQKKSENGVTLAPEDTLPFLKCYCSGHCPDDAINNTCITNGHCFAIIEEDDQGETTLASGCMKYEGSDFQCKDSPKAQLRRTIECCRTNLCNQYLQPTLPPVVIGPFFDGSIRWLVLLISMAVCIIAMIIFSSCFCYKHYCKSISSRRRYNRDLEQDEAFIPVGESLKDLIDQSQSSGSGSGLPLLVQRTIAKQIQMVRQVGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDFLKCATLDTRALLKLAYSAACGLCHLHTEIYGTQGKPAIAHRDLKSKNILIKKNGSCCIADLGLAVKFNSDTNEVDVPLNTRVGTKRYMAPEVLDESLNKNHFQPYIMADIYSFGLIIWEMARRCITGGIVEEYQLPYYNMVPSDPSYEDMREVVCVKRLRPIVSNRWNSDECLRAVLKLMSECWAHNPASRLTALRIKKTLAKMVESQDVKI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P36894","disprot_id":"DP01990","ncbi_taxon_id":9606,"regions_counter":4,"creator":"viglesias","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":120,"region_id":"DP01990r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The solution structure of BMPR-IA reveals a local disorder-to-order transition upon BMP-2 binding. <i> Klages J, Kotzsch A, Coles M, Sebald W, Nickel J, Müller T, Kessler H. </i> Biochemistry, 2008","statement":[{"text":"In addition, the \u00014\u00015\nloop is highly disordered (Figure 2), showing large structural\nvariations with distances between corresponding CR positions\nof up to 10 Å (Phe85)","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ahatos","start":104,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2K3G"}],"reference_id":"18937504","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":120,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The solution structure of BMPR-IA reveals a local disorder-to-order transition upon BMP-2 binding. <i> Klages J, Kotzsch A, Coles M, Sebald W, Nickel J, Müller T, Kessler H. </i> Biochemistry, 2008","statement":[{"text":"type I\nreceptor BMPR-IA, a significant part of the binding interface\nwith BMP-2 is disordered prior to ligand binding and thus\nrequires a disorder-to-order transition","type":"Discussion"}],"term_id":"IDPO:0000011","curator_id":"ahatos","start":104,"term_ontology":"IDPO","curator_name":"András Hatos","reference_id":"18937504","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01990r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":120,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"The solution structure of BMPR-IA reveals a local disorder-to-order transition upon BMP-2 binding. <i> Klages J, Kotzsch A, Coles M, Sebald W, Nickel J, Müller T, Kessler H. </i> Biochemistry, 2008","statement":[{"text":"The significance of the\nrearrangement of the \u00014\u00015 loop is illustrated by the shifts of Phe85\nand Gln86 of BMPR-IA into binding-competent positions. Gln86\nrepresents the main binding determinant in the BMP-2-BMPRIA\ninteraction, demonstrating that a stable complex can be formed\nonly if the \u00014\u00015 loop adopts a helical structure.","type":"Figure"}],"term_id":"GO:0005515","curator_id":"ahatos","start":104,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"18937504","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP01990r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P36894","date":"2018-08-21T13:30:18.000Z","acc":"P36894","name":"Bone morphogenetic protein receptor type-1A","length":532,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI000006EB08","genes":[{"name":{"value":"BMPR1A"},"synonyms":[{"value":"ACVRLK3"},{"value":"ALK3"}]}],"alphafold_very_low_content":0.09210526315789473,"disorder_content":0.03195488721804511,"disprot_consensus":{"full":[{"start":104,"end":120,"type":"T"}],"Structural state":[{"start":104,"end":120,"type":"D"}],"Structural transition":[{"start":104,"end":120,"type":"T"}],"Molecular function":[{"start":104,"end":120,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01417","name":"ENTH domain","start":17,"end":140}],"gene3D":[{"start":1,"end":144,"id":"1.25.40.90","name":"1.25.40.90"}]},"uniref50":"UniRef50_O88339","sequence":"MSTSSLRRQMKNIVHNYSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREERAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDVQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADVFTTPAPPQASDPWGGPASVPTAVPVAAAASDPWGGPAVPPAADPWGGAAPTPASGDPWRPAAPTGPSVDPWGGTPAPAAGEGPTPDPWGSSDGGAPVSGPPSSDPWAPAPAFSDPWGGSPAKPSSNGTAVGGFDTEPDEFSDFDRLRTALPTSGSSTGELELLAGEVPARSPGAFDMSGVGGSLAESVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGSKASNPFLPSGAPPTGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_O88339","disprot_id":"DP01993","ncbi_taxon_id":10090,"regions_counter":4,"creator":"viglesias","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":407,"region_id":"DP01993r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Accessory protein recruitment motifs in clathrin-mediated endocytosis. <i> Brett TJ, Traub LM, Fremont DH. </i> Structure, 2002","statement":[{"text":"Circular dichroism (CD) spectra of the epsin DPW region show little absorption above 210 nm and a large minimum at 200 nm, indicating little secondary structure in solution","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"viglesias","start":229,"term_ontology":"IDPO","curator_name":"Valentín Iglesias","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-6133-0869","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"12057195","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":407,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Accessory protein recruitment motifs in clathrin-mediated endocytosis. <i> Brett TJ, Traub LM, Fremont DH. </i> Structure, 2002","statement":[{"text":"Solution studies of the 17.7 kDa epsin DPW region (aa 229–407) indicate that the repeated binding motifs are highly accessible for interaction with the α-ear.","type":"Results"}],"term_id":"GO:0005515","curator_id":"viglesias","start":229,"term_ontology":"GO","curator_name":"Valentín Iglesias","reference_id":"12057195","version":3,"curator_orcid":"0000-0002-6133-0869","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01993r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":407,"region_id":"DP01993r003","released":"2022_03","ec_id":"ECO:0007064","reference_html":"Accessory protein recruitment motifs in clathrin-mediated endocytosis. <i> Brett TJ, Traub LM, Fremont DH. </i> Structure, 2002","statement":[{"text":"Dynamic light scattering of the DPW region corroborates that this region is predominantly disordered in solution.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"viglesias","start":229,"term_ontology":"IDPO","curator_name":"Valentín Iglesias","ec_name":"dynamic light scattering assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-6133-0869","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"12057195","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":407,"term_name":"protein binding","released":"2022_03","ec_name":"dynamic light scattering assay evidence used in manual assertion","reference_html":"Accessory protein recruitment motifs in clathrin-mediated endocytosis. <i> Brett TJ, Traub LM, Fremont DH. </i> Structure, 2002","statement":[{"text":"Solution studies of the 17.7 kDa epsin DPW region (aa 229–407) indicate that the repeated binding motifs are highly accessible for interaction with the α-ear.","type":"Results"}],"term_id":"GO:0005515","curator_id":"viglesias","start":229,"term_ontology":"GO","curator_name":"Valentín Iglesias","reference_id":"12057195","version":3,"curator_orcid":"0000-0002-6133-0869","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007064","region_id":"DP01993r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q80VP1","date":"2018-08-21T14:27:53.000Z","acc":"Q80VP1","name":"Epsin-1","length":575,"organism":"Mus musculus","dataset":[],"UniParc":"UPI000034E529","genes":[{"name":{"value":"Epn1"}}],"alphafold_very_low_content":0.3634782608695652,"disorder_content":0.31130434782608696,"disprot_consensus":{"full":[{"start":229,"end":407,"type":"D"}],"Structural state":[{"start":229,"end":407,"type":"D"}],"Molecular function":[{"start":229,"end":407,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00748","name":"Calpain inhibitor","start":131,"end":251},{"id":"PF00748","name":"Calpain inhibitor","start":269,"end":391},{"id":"PF00748","name":"Calpain inhibitor","start":406,"end":501},{"id":"PF00748","name":"Calpain inhibitor","start":516,"end":638}]},"uniref50":"UniRef50_P27321","sequence":"MSRPGPKPAASSRPRRGAAASHTQEHVNEKNIGSSSKPAEKKGSDEVTASSAATGTSPRMSTTGAKAVKIESEKSQSSEPPVIHEKKPKGKPKEGSEPQTLPKHASDTGSKHAHKEKALSRSNEQIVSEKSSESKTKFQDAPSADGESVAGGVTVATASDKVVVKKKEKKSLTPTLPMESTLNKLSDKSGVNAALDDLIDTLGECEDTNKDDPPYTGPVVLDPMDSTYLEALGIKEGTIPPEYRKLLEKNEAITGPLPDSPKPMGIDHAIDALSSDFTCSSPTGKQTEKEKSTGESSKAQSAGVTRSAVPPQEKKRKVEEEVMNDQALQALSDSLGTRQPDPQSHLRQAKQVKEAKAKEERQEKCGEDEDTVPAEYRLKPAKDKDGKPLLPEPEETSKCLSESELIGELSADFVQPTYQEKPSMPAAKIKKGVVPDDAVETLARSLGTRKEDPEDEKSLVDKVKEKAKEEDHEKLGEKEETIPPDYRLEIVKDKDGKPLLPKEAEEQLPPLSDDFLLDALSQDFSSPANILSLGFEDAKLSAAVSETVSQVPAPSNHTAAPPPGTERRDKELDDALDELSDSLGQRQPDPDENKPLDDKVKEKIKAEHSEKLGERDDTIPPEYRHLLDNDGKDKPEKPLTKNTEKLGQDQDPIDALSEDLDSCPPTTETSQNTTKEKGKKTSSSKASKNEEKTKDSSKKTEEVPKPKVDEDAT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_P27321","disprot_id":"DP01994","ncbi_taxon_id":10116,"regions_counter":6,"creator":"viglesias","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":652,"region_id":"DP01994r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Calcium-bound structure of calpain and its mechanism of inhibition by calpastatin. <i> Hanna RA, Campbell RL, Davies PL. </i> Nature, 2008","statement":[{"text":"Gaps in the electron density of CAST4 are indicated by missing residues between D589 and K594, and between N629 and P652.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"viglesias","start":629,"term_ontology":"IDPO","curator_name":"Valentín Iglesias","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6133-0869","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3bow"}],"reference_id":"19020623","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-21T16:58:18.018Z"}},{"start":187,"end":285,"reference_id":"19020622","reference_source":"pmid","reference_html":"Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains. <i> Moldoveanu T, Gehring K, Green DR. </i> Nature, 2008","date":"2024-03-21T16:47:43.732Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP01994r003","statement":[{"text":"Intrinsic disorder in the free state enables calpastatin to structurally adapt upon binding to the substrate binding cleft of calpain, distantly resembling the inhibitory conformation of the broad-specificity, structured protease inhibitors, the cystatins15 (Suppl. Fig. 4).","type":"Results"},{"text":"Numbering in the publication correspond to this boundaries of the Uniprot sequence.","type":"Curator statement"}]},{"start":194,"end":205,"reference_id":"19020622","reference_source":"pmid","reference_html":"Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains. <i> Moldoveanu T, Gehring K, Green DR. </i> Nature, 2008","date":"2024-03-21T16:53:38.688Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"3DF0"}],"region_id":"DP01994r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q07009"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q64537"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"The divergent intervening sequences connecting regions A, B and C are devoid of electron density (red dots in Fig. 1a). NMR analysis of the complex between 15N-labeled calpastatin and unlabeled calpain (Fig. 1c, Suppl. Fig. 1a) corroborated the disorder in the calpastatin intervening sequences (orange in Fig. 1d), which were detectable and could be partially assigned. Conversely, calpastatin regions A, B and C bind calpain, become ordered and tumble slowly in solution as part of the 111 kDa complex, and were undetectable by NMR.","type":"Results"}]},{"start":219,"end":251,"reference_id":"19020622","reference_source":"pmid","reference_html":"Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains. <i> Moldoveanu T, Gehring K, Green DR. </i> Nature, 2008","date":"2024-03-21T16:53:28.698Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"3DF0"}],"region_id":"DP01994r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q07009"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q64537"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"The divergent intervening sequences connecting regions A, B and C are devoid of electron density (red dots in Fig. 1a). NMR analysis of the complex between 15N-labeled calpastatin and unlabeled calpain (Fig. 1c, Suppl. Fig. 1a) corroborated the disorder in the calpastatin intervening sequences (orange in Fig. 1d), which were detectable and could be partially assigned. Conversely, calpastatin regions A, B and C bind calpain, become ordered and tumble slowly in solution as part of the 111 kDa complex, and were undetectable by NMR.","type":"Results"}]},{"start":268,"end":278,"reference_id":"19020622","reference_source":"pmid","reference_html":"Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains. <i> Moldoveanu T, Gehring K, Green DR. </i> Nature, 2008","date":"2024-03-21T16:53:19.222Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"3DF0"}],"region_id":"DP01994r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q07009"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q64537"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"The divergent intervening sequences connecting regions A, B and C are devoid of electron density (red dots in Fig. 1a). NMR analysis of the complex between 15N-labeled calpastatin and unlabeled calpain (Fig. 1c, Suppl. Fig. 1a) corroborated the disorder in the calpastatin intervening sequences (orange in Fig. 1d), which were detectable and could be partially assigned. Conversely, calpastatin regions A, B and C bind calpain, become ordered and tumble slowly in solution as part of the 111 kDa complex, and were undetectable by NMR.","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_P27321","date":"2018-08-21T17:32:42.000Z","acc":"P27321","name":"Calpastatin","length":713,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI0000170C12","genes":[{"name":{"value":"Cast"}}],"alphafold_very_low_content":0.43338008415147267,"disorder_content":0.17251051893408134,"disprot_consensus":{"full":[{"start":187,"end":193,"type":"D"},{"start":194,"end":205,"type":"T"},{"start":206,"end":218,"type":"D"},{"start":219,"end":251,"type":"T"},{"start":252,"end":267,"type":"D"},{"start":268,"end":278,"type":"T"},{"start":279,"end":285,"type":"D"},{"start":629,"end":652,"type":"D"}],"Structural state":[{"start":187,"end":285,"type":"D"},{"start":629,"end":652,"type":"D"}],"Structural transition":[{"start":194,"end":205,"type":"T"},{"start":219,"end":251,"type":"T"},{"start":268,"end":278,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00648","name":"Calpain family cysteine protease","start":46,"end":342},{"id":"PF01067","name":"Calpain large subunit, domain III","start":362,"end":502},{"id":"PF13833","name":"EF-hand domain pair","start":545,"end":603}],"gene3D":[{"start":530,"end":700,"id":"1.10.238.10","name":"EF-hand"},{"start":210,"end":352,"id":"3.90.70.10","name":"Cysteine proteinases"},{"start":355,"end":513,"id":"2.60.120.380","name":"2.60.120.380"}]},"uniref50":"UniRef50_Q07009","sequence":"MAGIAMKLAKDREAAEGLGSHERAIKYLNQDYETLRNECLEAGALFQDPSFPALPSSLGFKELGPYSSKTRGIEWKRPTEICADPQFIIGGATRTDICQGALGDCWLLAAIASLTLNEEILARVVPLDQSFQENYAGIFHFQFWQYGEWVEVVVDDRLPTKDGELLFVHSAEGSEFWSALLEKAYAKINGCYEALSGGATTEGFEDFTGGIAEWYELRKPPPNLFKIIQKALEKGSLLGCSIDITSAADSEAVTYQKLVKGHAYSVTGAEEVESSGSLQKLIRIRNPWGQVEWTGKWNDNCPSWNTVDPEVRANLTERQEDGEFWMSFSDFLRHYSRLEICNLTPDTLTCDSYKKWKLTKMDGNWRRGSTAGGCRNYPNTFWMNPQYLIKLEEEDEDDEDGERGCTFLVGLIQKHRRRQRKMGEDMHTIGFGIYEVPEELTGQTNIHLSKNFFLTTRARERSDTFINLREVLNRFKLPPGEYVLVPSTFEPHKNGDFCIRVFSEKKADYQTVDDEIEANIEEIEANEEDIGDGFRRLFAQLAGEDAEISAFELQTILRRVLAKREDIKSDGFSIETCKIMVDMLDEDGSGKLGLKEFYILWTKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKLPCQLHQVIVARFADDELIIDFDNFVRCLVRLEILFKIFKQLDPENTGTIQLDLISWLSFSVL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_Q07009","disprot_id":"DP01996","ncbi_taxon_id":10116,"regions_counter":5,"creator":"viglesias","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":260,"region_id":"DP01996r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation. <i> Hosfield CM, Elce JS, Davies PL, Jia Z. </i> EMBO J, 1999","statement":[{"text":"The final model (refined against data collected previously at the Cornell High Energy Synchrotron Source on P1 native crystal form) is well defined with the exception of the following disordered regions that were omitted: 245-260, 273-278, 292-321, 437-459 and 565-566 (indicated by dotted lines in Figure 1B).","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"viglesias","start":245,"term_ontology":"IDPO","curator_name":"Valentín Iglesias","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6133-0869","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1df0"}],"reference_id":"10601010","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":321,"region_id":"DP01996r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation. <i> Hosfield CM, Elce JS, Davies PL, Jia Z. </i> EMBO J, 1999","statement":[{"text":"The final model (refined against data collected previously at the Cornell High Energy Synchrotron Source on P1 native crystal form) is well defined with the exception of the following disordered regions that were omitted: 245-260, 273-278, 292-321, 437-459 and 565-566 (indicated by dotted lines in Figure 1B).","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"viglesias","start":292,"term_ontology":"IDPO","curator_name":"Valentín Iglesias","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6133-0869","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1df0"}],"reference_id":"10601010","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":459,"region_id":"DP01996r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation. <i> Hosfield CM, Elce JS, Davies PL, Jia Z. </i> EMBO J, 1999","statement":[{"text":"The final model (refined against data collected previously at the Cornell High Energy Synchrotron Source on P1 native crystal form) is well defined with the exception of the following disordered regions that were omitted: 245-260, 273-278, 292-321, 437-459 and 565-566 (indicated by dotted lines in Figure 1B).","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"viglesias","start":437,"term_ontology":"IDPO","curator_name":"Valentín Iglesias","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6133-0869","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1df0"}],"reference_id":"10601010","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":536,"region_id":"DP01996r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of a micro-like calpain reveals a partially activated conformation with low Ca2+ requirement. <i> Pal GP, De Veyra T, Elce JS, Jia Z. </i> Structure, 2003","statement":[{"text":"In domain IV, there are several disordered regions including residues 541-549 and residues 588-593 corresponding to EF hands 1 and 2, as well as the linker between domains III and IV, residues 527-536.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"viglesias","start":527,"term_ontology":"IDPO","curator_name":"Valentín Iglesias","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6133-0869","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1qxp"}],"reference_id":"14656436","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":536,"term_name":"flexible linker","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of a micro-like calpain reveals a partially activated conformation with low Ca2+ requirement. <i> Pal GP, De Veyra T, Elce JS, Jia Z. </i> Structure, 2003","statement":[{"text":"In domain IV, there are several disordered regions including residues 541-549 and residues 588-593 corresponding to EF hands 1 and 2, as well as the linker between domains III and IV, residues 527-536.","type":"Results"}],"term_id":"IDPO:0000033","curator_id":"viglesias","start":527,"term_ontology":"IDPO","curator_name":"Valentín Iglesias","reference_id":"14656436","version":3,"curator_orcid":"0000-0002-6133-0869","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP01996r005","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_Q07009","date":"2018-08-21T18:11:40.000Z","acc":"Q07009","name":"Calpain-2 catalytic subunit","length":700,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI0000039F0F","genes":[{"name":{"value":"Capn2"}}],"alphafold_very_low_content":0.005714285714285714,"disorder_content":0.11285714285714285,"disprot_consensus":{"full":[{"start":245,"end":260,"type":"D"},{"start":292,"end":321,"type":"D"},{"start":437,"end":459,"type":"D"},{"start":527,"end":536,"type":"D"}],"Structural state":[{"start":245,"end":260,"type":"D"},{"start":292,"end":321,"type":"D"},{"start":437,"end":459,"type":"D"},{"start":527,"end":536,"type":"D"}],"Disorder function":[{"start":527,"end":536,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02037","name":"SAP domain","start":385,"end":418},{"id":"PF02755","name":"RPEL repeat","start":17,"end":38},{"id":"PF02755","name":"RPEL repeat","start":61,"end":83},{"id":"PF02755","name":"RPEL repeat","start":105,"end":125}],"gene3D":[{"start":366,"end":434,"id":"1.10.720.30","name":"SAP domain"}]},"uniref50":"UniRef50_Q8K4J6","sequence":"MTLLEPEMLMMAVQSVLQLKLQQRRTREELVSQGIMPPLKSPAAFHEQRRSLERARTEDYLKRKIRSRPERAELVRMHILEETSAEPSLQAKQLKLKRARLADDLNEKIAQRPGPMELVEKNILPVESSLKEAIIVGQVNYPKVADSSSFDEDSSDALSPEQPASHESQGSVPSPLESRVSDPLPSATSISPTQVLSQLPMAPDPGETLFLAEQPPLPPAPLLPPSLANGSIVPTAKPAPTLIKQSQPKSASEKSQRSKKAKELKPKVKKLKYHQYIPPDQKQDKGAPAMDSSYAKILQQQQLFLQLQILNQQQQQQQQQHYNYQAILPAPPKPSAETPGSSAPTPSRSLSTSSSPSSGTPGPSGLARQSSTALAAKPGALPANLDDMKVAELKQELKLRSLPVSGTKTELIERLRAYQDQVSPAPGAPKAPATTSVLSKAGEVVVAFPAALLSTGSALVTAGLAPAEMVVATVTSNGMVKFGSTGSTPPVSPTPSERSLLSTGDENSTPGDAFGEMVTSPLTQLTLQASPLQIVKEEGARAASCCLSPGARAELEGLDKDQMLQEKDKQIEELTRMLQQKQQLVELLRLQLEQQKRAQQPAPASSPVKRESGFSSCQLSCQPQGSAHAFGSGLVVPTTNHGDTQAPAPESPPVVVKQEAGPPEPDLAPSSQLLLGSQGTSFLKRVSPPTLVTDSTGTHLILTVTNKSADGPGLPAGSPQQPLSQPGSPAPGPPAQMDLEHPPQPPFATPTSLLKKEPPGYEETVTQQPKQQENGSSSQHMDDLFDILIQSGEISADFKEPPSLPGKEKSPPAAAAYGPPLTPQPSPLSELPQAAPPPGSPTLPGRLEDFLESSTGLPLLTSGHEGPEPLSLIDDLHSQMLSSSAILDHPPSPMDTSELHFAPEPSSGMGLDLAVGHLDSMDWLELSSGGPVLSLAPLSTAAPSLFSMDFLDGHDLQLHWDSCL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q8K4J6","disprot_id":"DP01999","ncbi_taxon_id":10090,"regions_counter":12,"creator":"tszani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":98,"region_id":"DP01999r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL. <i> Mouilleron S, Guettler S, Langer CA, Treisman R, McDonald NQ. </i> EMBO J, 2008","statement":[{"text":"circular dichroism (CD) experiments revealed that each RPEL peptide is largely unstructured in solution (α-helical content of 5.2, 4 and 4.3%, respectively) (Supplementary Figure S1), indicating that the observed RPEL peptide secondary structure is induced on binding actin.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"tszani","start":67,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19008859","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":98,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL. <i> Mouilleron S, Guettler S, Langer CA, Treisman R, McDonald NQ. </i> EMBO J, 2008","term_id":"GO:0060090","curator_id":"tszani","start":67,"term_ontology":"GO","curator_name":"Tamás Szaniszló","reference_id":"19008859","version":3,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01999r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":98,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL. <i> Mouilleron S, Guettler S, Langer CA, Treisman R, McDonald NQ. </i> EMBO J, 2008","statement":[{"text":"G-actin binds individual RPEL peptides from the MAL N-terminal regulatory domain","type":"Discussion"}],"term_id":"GO:0005515","curator_id":"tszani","start":67,"term_ontology":"GO","curator_name":"Tamás Szaniszló","reference_id":"19008859","version":3,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01999r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":98,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL. <i> Mouilleron S, Guettler S, Langer CA, Treisman R, McDonald NQ. </i> EMBO J, 2008","statement":[{"text":"circular dichroism (CD) experiments revealed that each RPEL peptide is largely unstructured in solution (α-helical content of 5.2, 4 and 4.3%, respectively) (Supplementary Figure S1), indicating that the observed RPEL peptide secondary structure is induced on binding actin.\nG-actin binds individual RPEL peptides from the MAL N-terminal regulatory domain and the structural fold adopted by an RPEL motif","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"tszani","start":67,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","reference_id":"19008859","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01999r004","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":142,"region_id":"DP01999r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL. <i> Mouilleron S, Guettler S, Langer CA, Treisman R, McDonald NQ. </i> EMBO J, 2008","statement":[{"text":"circular dichroism (CD) experiments revealed that each RPEL peptide is largely unstructured in solution (α-helical content of 5.2, 4 and 4.3%, respectively) (Supplementary Figure S1), indicating that the observed RPEL peptide secondary structure is induced on binding actin.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"tszani","start":111,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19008859","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":142,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL. <i> Mouilleron S, Guettler S, Langer CA, Treisman R, McDonald NQ. </i> EMBO J, 2008","term_id":"GO:0060090","curator_id":"tszani","start":111,"term_ontology":"GO","curator_name":"Tamás Szaniszló","reference_id":"19008859","version":3,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01999r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":142,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL. <i> Mouilleron S, Guettler S, Langer CA, Treisman R, McDonald NQ. </i> EMBO J, 2008","statement":[{"text":"G-actin binds individual RPEL peptides from the MAL N-terminal regulatory domain","type":"Discussion"}],"term_id":"GO:0005515","curator_id":"tszani","start":111,"term_ontology":"GO","curator_name":"Tamás Szaniszló","reference_id":"19008859","version":3,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01999r007","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":142,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL. <i> Mouilleron S, Guettler S, Langer CA, Treisman R, McDonald NQ. </i> EMBO J, 2008","statement":[{"text":"circular dichroism (CD) experiments revealed that each RPEL peptide is largely unstructured in solution (α-helical content of 5.2, 4 and 4.3%, respectively) (Supplementary Figure S1), indicating that the observed RPEL peptide secondary structure is induced on binding actin.\nG-actin binds individual RPEL peptides from the MAL N-terminal regulatory domain and the structural fold adopted by an RPEL motif","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"tszani","start":111,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","reference_id":"19008859","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01999r008","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":186,"region_id":"DP01999r009","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL. <i> Mouilleron S, Guettler S, Langer CA, Treisman R, McDonald NQ. </i> EMBO J, 2008","statement":[{"text":"circular dichroism (CD) experiments revealed that each RPEL peptide is largely unstructured in solution (α-helical content of 5.2, 4 and 4.3%, respectively) (Supplementary Figure S1), indicating that the observed RPEL peptide secondary structure is induced on binding actin.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"tszani","start":155,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19008859","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":186,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL. <i> Mouilleron S, Guettler S, Langer CA, Treisman R, McDonald NQ. </i> EMBO J, 2008","statement":[{"text":"G-actin binds individual RPEL peptides from the MAL N-terminal regulatory domain","type":"Discussion"}],"term_id":"GO:0005515","curator_id":"tszani","start":155,"term_ontology":"GO","curator_name":"Tamás Szaniszló","reference_id":"19008859","version":3,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01999r010","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":186,"term_name":"disorder to order","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL. <i> Mouilleron S, Guettler S, Langer CA, Treisman R, McDonald NQ. </i> EMBO J, 2008","statement":[{"text":"circular dichroism (CD) experiments revealed that each RPEL peptide is largely unstructured in solution (α-helical content of 5.2, 4 and 4.3%, respectively) (Supplementary Figure S1), indicating that the observed RPEL peptide secondary structure is induced on binding actin.\nG-actin binds individual RPEL peptides from the MAL N-terminal regulatory domain and the structural fold adopted by an RPEL motif","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"tszani","start":155,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","reference_id":"19008859","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01999r011","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":186,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL. <i> Mouilleron S, Guettler S, Langer CA, Treisman R, McDonald NQ. </i> EMBO J, 2008","term_id":"GO:0060090","curator_id":"tszani","start":155,"term_ontology":"GO","curator_name":"Tamás Szaniszló","reference_id":"19008859","version":3,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP01999r012","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q8K4J6","date":"2018-08-22T08:29:33.000Z","acc":"Q8K4J6","name":"Myocardin-related transcription factor A","length":964,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000028C89","genes":[{"name":{"value":"Mrtfa"},"synonyms":[{"value":"Bsac","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12019265","url":"http://www.ncbi.nlm.nih.gov/pubmed/12019265","alternativeUrl":"https://europepmc.org/abstract/MED/12019265"}}]},{"value":"Mal","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12732141","url":"http://www.ncbi.nlm.nih.gov/pubmed/12732141","alternativeUrl":"https://europepmc.org/abstract/MED/12732141"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"19008859","url":"http://www.ncbi.nlm.nih.gov/pubmed/19008859","alternativeUrl":"https://europepmc.org/abstract/MED/19008859"}}]},{"value":"Mkl1","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:2384495","url":"http://www.informatics.jax.org/marker/MGI:2384495"}}]}]}],"alphafold_very_low_content":0.6213692946058091,"disorder_content":0.0995850622406639,"disprot_consensus":{"full":[{"start":67,"end":98,"type":"T"},{"start":111,"end":142,"type":"T"},{"start":155,"end":186,"type":"T"}],"Structural state":[{"start":67,"end":98,"type":"D"},{"start":111,"end":142,"type":"D"},{"start":155,"end":186,"type":"D"}],"Molecular function":[{"start":67,"end":98,"type":"F"},{"start":111,"end":142,"type":"F"},{"start":155,"end":186,"type":"F"}],"Structural transition":[{"start":67,"end":98,"type":"T"},{"start":111,"end":142,"type":"T"},{"start":155,"end":186,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00595","name":"PDZ domain","start":156,"end":230},{"id":"PF09007","name":"EBP50, C-terminal","start":235,"end":358},{"id":"PF17820","name":"PDZ domain","start":39,"end":91}],"gene3D":[{"start":149,"end":236,"id":"2.30.42.10","name":"2.30.42.10"},{"start":7,"end":120,"id":"2.30.42.10","name":"2.30.42.10"}]},"uniref50":"UniRef50_O14745","sequence":"MSADAAAGAPLPRLCCLEKGPNGYGFHLHGEKGKLGQYIRLVEPGSPAEKAGLLAGDRLVEVNGENVEKETHQQVVSRIRAALNAVRLLVVDPETDEQLQKLGVQVREELLRAQEAPGQAEPPAAAEVQGAGNENEPREADKSHPEQRELRPRLCTMKKGPSGYGFNLHSDKSKPGQFIRSVDPDSPAEASGLRAQDRIVEVNGVCMEGKQHGDVVSAIRAGGDETKLLVVDRETDEFFKKCRVIPSQEHLNGPLPVPFTNGEIQKENSREALAEAALESPRPALVRSASSDTSEELNSQDSPPKQDSTAPSSTSSSDPILDFNISLAMAKERAHQKRSSKRAPQMDWSKKNELFSNL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O14745","disprot_id":"DP02000","ncbi_taxon_id":9606,"regions_counter":9,"creator":"ameszaros","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":358,"region_id":"DP02000r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"A conformational switch in the scaffolding protein NHERF1 controls autoinhibition and complex formation. <i> Bhattacharya S, Dai Z, Li J, Baxter S, Callaway DJE, Cowburn D, Bu Z. </i> J Biol Chem, 2010","statement":[{"text":"This disordered state is supported by CD results of the isolated domains, which show that the PDZ2 domains are structured, but the CT domain is largely disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ameszaros","start":242,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"20042604","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":358,"term_name":"protein binding","start":242,"ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_id":"ameszaros","released":"2022_03","term_ontology":"GO","curator_name":"Attila Meszaros","reference_id":"20042604","version":3,"reference_html":"A conformational switch in the scaffolding protein NHERF1 controls autoinhibition and complex formation. <i> Bhattacharya S, Dai Z, Li J, Baxter S, Callaway DJE, Cowburn D, Bu Z. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP02000r002","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":358,"region_id":"DP02000r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Autoinhibitory interactions between the PDZ2 and C-terminal domains in the scaffolding protein NHERF1. <i> Cheng H, Li J, Fazlieva R, Dai Z, Bu Z, Roder H. </i> Structure, 2009","statement":[{"text":"The far-ultraviolet irradiation circular dichroism (CD) spectrum\nof the isolated CT (Figure 3B) exhibits a strong negative band at 205 nm and a weak shoulder near 220 nm, consistent with a largely disordered conformation with little regular secondary structure","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ameszaros","start":242,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"19446522","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":358,"term_name":"disorder to order","start":242,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"The spectra of  PDZ2-CT construct (residues 150–358) show a pronounced negative band at 222 nm indicative of helical conformation","type":"Results"}],"curator_id":"ameszaros","released":"2022_03","term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"19446522","version":2,"reference_html":"Autoinhibitory interactions between the PDZ2 and C-terminal domains in the scaffolding protein NHERF1. <i> Cheng H, Li J, Fazlieva R, Dai Z, Bu Z, Roder H. </i> Structure, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006204","region_id":"DP02000r004","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":358,"region_id":"DP02000r005","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Autoinhibitory interactions between the PDZ2 and C-terminal domains in the scaffolding protein NHERF1. <i> Cheng H, Li J, Fazlieva R, Dai Z, Bu Z, Roder H. </i> Structure, 2009","statement":[{"text":"The remaining unassigned peaks due to the C-terminal segment form a dense cluster in the center of the HSQC spectrum characteristic of a disordered conformation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ameszaros","start":242,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"19446522","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2JXO"}],"term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","reference_source":"pmid","ec_ontology":"ECO","end":358,"term_name":"disorder to order","start":242,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"The NMR results indicate that the last 11 residues at the C terminus of NHERF1 participate in binding and adopt an a-helical conformation when bound to PDZ2.","type":"Results"}],"curator_id":"ameszaros","released":"2022_03","term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"19446522","version":2,"reference_html":"Autoinhibitory interactions between the PDZ2 and C-terminal domains in the scaffolding protein NHERF1. <i> Cheng H, Li J, Fazlieva R, Dai Z, Bu Z, Roder H. </i> Structure, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000011","ec_id":"ECO:0006165","region_id":"DP02000r006","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":358,"term_name":"protein binding","start":242,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"the noncovalent complex between the isolated PDZ2 and CT domains serves as a reliable model for understanding the intramolecular interaction between PDZ2 and the C-terminal domain of NHERF1","type":"Results"}],"curator_id":"ameszaros","released":"2022_03","term_ontology":"GO","curator_name":"Attila Meszaros","reference_id":"19446522","version":3,"reference_html":"Autoinhibitory interactions between the PDZ2 and C-terminal domains in the scaffolding protein NHERF1. <i> Cheng H, Li J, Fazlieva R, Dai Z, Bu Z, Roder H. </i> Structure, 2009","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP02000r007","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":358,"region_id":"DP02000r008","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A conformational switch in the scaffolding protein NHERF1 controls autoinhibition and complex formation. <i> Bhattacharya S, Dai Z, Li J, Baxter S, Callaway DJE, Cowburn D, Bu Z. </i> J Biol Chem, 2010","statement":[{"text":"The 1H-15 N HSQC spectrum of PDZ2CT (amino acid residues 150–358) is characteristic of a heterogeneous conformation of a structured PDZ domain, coexisting with a largely disordered C-terminal region that typically yields a high density of sharp peaks between 8 and 8.5 ppm in the proton dimension.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ameszaros","start":242,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"20042604","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2KRG"}],"term_name":"disorder","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":358,"term_name":"protein binding","start":242,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"ameszaros","released":"2022_03","term_ontology":"GO","curator_name":"Attila Meszaros","reference_id":"20042604","version":3,"reference_html":"A conformational switch in the scaffolding protein NHERF1 controls autoinhibition and complex formation. <i> Bhattacharya S, Dai Z, Li J, Baxter S, Callaway DJE, Cowburn D, Bu Z. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP02000r009","curator_orcid":"0000-0002-4578-4879","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_O14745","date":"2018-08-22T10:29:29.000Z","acc":"O14745","name":"Na(+)/H(+) exchange regulatory cofactor NHE-RF1","length":358,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00005296EC","genes":[{"name":{"value":"SLC9A3R1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11075","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11075"}}]},"synonyms":[{"value":"NHERF"},{"value":"NHERF1"}]}],"alphafold_very_low_content":0.1452513966480447,"disorder_content":0.3268156424581006,"disprot_consensus":{"full":[{"start":242,"end":358,"type":"T"}],"Structural state":[{"start":242,"end":358,"type":"D"}],"Molecular function":[{"start":242,"end":358,"type":"F"}],"Structural transition":[{"start":242,"end":358,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00578","name":"AhpC/TSA family","start":85,"end":216},{"id":"PF10417","name":"C-terminal domain of 1-Cys peroxiredoxin","start":237,"end":264}],"gene3D":[{"start":78,"end":274,"id":"3.40.30.10","name":"Glutaredoxin"}]},"uniref50":"UniRef50_O08807","sequence":"MEARSKLLDGTTASRRWTRKLVLLLPPLLLFLLRTESLQGLESDERFRTRENECHFYAGGQVYPGEASRVSVADHSLHLSKAKISKPAPYWEGTAVINGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRIEEFKSINTEVVACSVDSQFTHLAWINTPRRQGGLGPIRIPLLSDLNHQISKDYGVYLEDSGHTLRGLFIIDDKGVLRQITLNDLPVGRSVDETLRLVQAFQYTDKHGEVCPAGWKPGSETIIPDPAGKLKYFDKLN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_O08807","disprot_id":"DP02001","ncbi_taxon_id":10090,"regions_counter":6,"creator":"mpajkos","regions":[{"region_id":"DP02001r001","ec_ontology":"ECO","end":274,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":256,"version":3,"statement":[{"text":"We modeled amino acid residues 79–241 and 247–255, but not those of the C-terminal segments, due to the lack of electron density (supplementary Fig. S5D, left).","type":"Results"}],"term_name":"disorder","reference_html":"Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding. <i> Sato Y, Kojima R, Okumura M, Hagiwara M, Masui S, Maegawa K, Saiki M, Horibe T, Suzuki M, Inaba K. </i> Sci Rep, 2013","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"23949117","date":"2024-02-06T18:03:17.758Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3VWU"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":263,"region_id":"DP02001r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding. <i> Sato Y, Kojima R, Okumura M, Hagiwara M, Masui S, Maegawa K, Saiki M, Horibe T, Suzuki M, Inaba K. </i> Sci Rep, 2013","statement":[{"text":"They determined the crystal structure of P5 in complex with the Prdx4 C-terminal peptide (residues 244-263 from Mus musculus Prdx4). \n\"peptide electron density was visible only for the region from Glu246 to Gly251, and, thus, we found it bound a hydrophobic groove of P5\"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ahatos","start":244,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3W8J"}],"reference_id":"23949117","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":263,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding. <i> Sato Y, Kojima R, Okumura M, Hagiwara M, Masui S, Maegawa K, Saiki M, Horibe T, Suzuki M, Inaba K. </i> Sci Rep, 2013","statement":[{"text":"\"Here, we established the structural basis of the interaction between Prx4 and PDIs by showing that a locally unstructured C-terminal segment of oxidized Prx4 binds to the peptide-binding groove of Trx\"","type":"Discussion"}],"term_id":"GO:0005515","curator_id":"ahatos","start":244,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"23949117","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02001r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":263,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding. <i> Sato Y, Kojima R, Okumura M, Hagiwara M, Masui S, Maegawa K, Saiki M, Horibe T, Suzuki M, Inaba K. </i> Sci Rep, 2013","term_id":"IDPO:0000011","curator_id":"ahatos","start":244,"term_ontology":"IDPO","curator_name":"András Hatos","reference_id":"23949117","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02001r004","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":263,"region_id":"DP02001r005","reference_id":"23949117","start":252,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"They determined the crystal structure of P5 in complex with the Prdx4 C-terminal peptide (residues 244-263 from Mus musculus Prdx4). \"peptide electron density was visible only for the region from Glu246 to Gly251, and, thus, we found it bound a hydrophobic groove of P5","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding. <i> Sato Y, Kojima R, Okumura M, Hagiwara M, Masui S, Maegawa K, Saiki M, Horibe T, Suzuki M, Inaba K. </i> Sci Rep, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3W8J"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02001r006","ec_ontology":"ECO","end":251,"term_id":"GO:0005515","start":246,"version":4,"statement":[{"text":"They determined the crystal structure of P5 in complex with the Prdx4 C-terminal peptide (residues 244-263 from Mus musculus Prdx4). \"peptide electron density was visible only for the region from Glu246 to Gly251, and, thus, we found it bound a hydrophobic groove of P5","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q15084-4","partner_end":null}],"term_name":"protein binding","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"23949117","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3W8J"}],"term_namespace":"Molecular function","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding. <i> Sato Y, Kojima R, Okumura M, Hagiwara M, Masui S, Maegawa K, Saiki M, Horibe T, Suzuki M, Inaba K. </i> Sci Rep, 2013","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_O08807","date":"2018-08-22T12:17:04.000Z","acc":"O08807","name":"Peroxiredoxin-4","length":274,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000001845","genes":[{"name":{"value":"Prdx4"}}],"alphafold_very_low_content":0.20802919708029197,"disorder_content":0.11313868613138686,"disprot_consensus":{"full":[{"start":244,"end":263,"type":"T"},{"start":264,"end":274,"type":"D"}],"Structural state":[{"start":244,"end":274,"type":"D"}],"Molecular function":[{"start":244,"end":263,"type":"F"}],"Structural transition":[{"start":244,"end":263,"type":"T"}]}},{"features":{"pfam":[{"id":"PF03372","name":"Endonuclease/Exonuclease/phosphatase family","start":133,"end":437}],"gene3D":[{"start":90,"end":447,"id":"3.60.10.10","name":"Endonuclease/exonuclease/phosphatase"}]},"uniref50":"UniRef50_O15922","sequence":"MASKRCRQCSGDSASSSTSSLSPSELPPSKKAAGGQRVTAEVEVAPITTDATSATVTAAGGAKKKATTGSPARRTSSAAKITNGDAGELIRTAEALAALNAKKSEKEIWSDVVPFVRRTTDSDFDPSRMYKFITWNVAGLRGLLKKNASALRAFMEAEKPDVLCLQETKLNVDEADANATLGVVDGYSFVDHPCAFKRGYSGTRTYMKNSTTVKGLHARCTRGFALPSEPQADAAAGSRVLVEGAGDEEGRVLTTFLSPDPDSASSSSRIALVNTYVANSGMGLTRLPYRVQSFDPSMREYLHRLDTWATENAAVPSAAAMGSGSSPHGFIWAGDLNVAERDYDRYYAGTFKSMQECSGFAPEERMSFRETMQRTNSVDIFRQLYPQAGPVYSFWSQRINGRPRNLGWRLDYFVVSSRLASYVVDCFPMPTVMGSDHCPFQMWMRHP","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"uniref90":"UniRef90_O15922","disprot_id":"DP02002","ncbi_taxon_id":5664,"regions_counter":3,"creator":"jlecle","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":89,"region_id":"DP02002r001","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Crystal structure and DNA repair activities of the AP endonuclease from Leishmania major. <i> Vidal AE, Harkiolaki M, Gallego C, Castillo-Acosta VM, Ruiz-Pérez LM, Wilson K, González-Pacanowska D. </i> J Mol Biol, 2007","statement":[{"text":"There is no density for 89 residues at the N terminus, which were either not present or not ordered in those crystals.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-09-16T15:32:03.624Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2J63"}],"reference_id":"17870086","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:13:59.940Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":240,"region_id":"DP02002r002","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Crystal structure and DNA repair activities of the AP endonuclease from Leishmania major. <i> Vidal AE, Harkiolaki M, Gallego C, Castillo-Acosta VM, Ruiz-Pérez LM, Wilson K, González-Pacanowska D. </i> J Mol Biol, 2007","term_id":"IDPO:0000002","curator_id":"vnugnes","start":230,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-09-16T15:33:00.893Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2J63"}],"reference_id":"17870086","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Three additional disordered loops lie on the outer surface of the protein away from the active site.","type":"Methods"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:14:01.096Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":324,"region_id":"DP02002r003","released":"2022_12","ec_id":"ECO:0006220","reference_html":"Crystal structure and DNA repair activities of the AP endonuclease from Leishmania major. <i> Vidal AE, Harkiolaki M, Gallego C, Castillo-Acosta VM, Ruiz-Pérez LM, Wilson K, González-Pacanowska D. </i> J Mol Biol, 2007","term_id":"IDPO:0000002","curator_id":"vnugnes","start":315,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-09-16T15:33:38.977Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2J63"}],"reference_id":"17870086","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Three additional disordered loops lie on the outer surface of the protein away from the active site.","type":"Methods"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:14:03.589Z"}}],"released":"2018_11","uniref100":"UniRef100_O15922","date":"2018-08-22T12:59:30.000Z","acc":"O15922","name":"DNA-(apurinic or apyrimidinic site) lyase","length":447,"organism":"Leishmania major","dataset":["Neglected tropical diseases proteins"],"UniParc":"UPI0000076A4D","genes":[{"name":{"value":"LmAP","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAD11457.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD11457.1"}}]},"orfNames":[{"value":"LMJF_16_0680","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAJ03609.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAJ03609.1"}}]}]}],"alphafold_very_low_content":0.2214765100671141,"disorder_content":0.24608501118568232,"disprot_consensus":{"full":[{"start":1,"end":89,"type":"D"},{"start":230,"end":240,"type":"D"},{"start":315,"end":324,"type":"D"}],"Structural state":[{"start":1,"end":89,"type":"D"},{"start":230,"end":240,"type":"D"},{"start":315,"end":324,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00170","name":"bZIP transcription factor","start":267,"end":322},{"id":"PF02173","name":"pKID domain","start":99,"end":139}],"gene3D":[{"start":285,"end":339,"id":"1.20.5.170","name":"1.20.5.170"}]},"uniref50":"UniRef50_P16220","sequence":"MTMESGAENQQSGDAAVTEAENQQMTVQAQPQIATLAQVSMPAAHATSSAPTVTLVQLPNGQTVQVHGVIQAAQPSVIQSPQVQTVQISTIAESEDSQESVDSVTDSQKRREILSRRPSYRKILNDLSSDAPGVPRIEEEKSEEETSAPAITTVTVPTPIYQTSSGQYIAITQGGAIQLANNGTDGVQGLQTLTMTNAAATQPGTTILQYAQTTDGQQILVPSNQVVVQAASGDVQTYQIRTAPTSTIAPGVVMASSPALPTQPAEEAARKREVRLMKNREAARECRRKKKEYVKCLENRVAVLENQNKTLIEELKALKDLYCHKSD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P16220","disprot_id":"DP02003","ncbi_taxon_id":9606,"regions_counter":2,"creator":"randerson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":160,"region_id":"DP02003r001","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Transcriptional activator-coactivator recognition: nascent folding of a kinase-inducible transactivation domain predicts its structure on coactivator binding. <i> Hua QX, Jia WH, Bullock BP, Habener JF, Weiss MA. </i> Biochemistry, 1998","statement":[{"text":"Biochemical studies of intact CREB have demontrated that the pKID domain is unusually susceptible to proteolysis  [PMID:1671708] and hence likely to be unstructured. Biophysical characterization of the isolated pKID domain (residues 101 - 160 of human CREB, 60 residues) was limited in the original study of a pKID-CBP complex by the phosphopeptide’s sparing solubility in the absence of guanidine hydrochloride.","type":"Introduction"}],"term_id":"IDPO:0000002","curator_id":"lpaladin","start":101,"term_ontology":"IDPO","curator_name":"Lisanna Paladin","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0011-9397","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"9558319","uniprot_changed":true,"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":160,"term_name":"disorder to order","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","reference_html":"Transcriptional activator-coactivator recognition: nascent folding of a kinase-inducible transactivation domain predicts its structure on coactivator binding. <i> Hua QX, Jia WH, Bullock BP, Habener JF, Weiss MA. </i> Biochemistry, 1998","statement":[{"text":"The three-dimensional structure of a CREB pKID-CBP regulatory complex has recently been described [PMID:9413984] and provides a model of a coil to helix transition on assembly of a transcriptional activator-coactivator complex.","type":"Introduction"}],"term_id":"IDPO:0000011","curator_id":"lpaladin","start":101,"term_ontology":"IDPO","curator_name":"Lisanna Paladin","reference_id":"9558319","version":2,"curator_orcid":"0000-0003-0011-9397","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","region_id":"DP02003r002","uniprot_changed":true,"ec_go":"IDA","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_P16220","date":"2018-08-22T13:25:11.000Z","acc":"P16220","name":"Cyclic AMP-responsive element-binding protein 1","length":327,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"uniparc":"UPI000002A717","genes":[{"name":{"value":"CREB1"}}],"alphafold_very_low_content":0.46788990825688076,"disorder_content":0.1834862385321101,"disprot_consensus":{"full":[{"start":101,"end":160,"type":"T"}],"Structural state":[{"start":101,"end":160,"type":"D"}],"Structural transition":[{"start":101,"end":160,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00439","name":"Bromodomain","start":1104,"end":1178},{"id":"PF00569","name":"Zinc finger, ZZ type","start":1702,"end":1742},{"id":"PF02135","name":"TAZ zinc finger","start":354,"end":430},{"id":"PF02135","name":"TAZ zinc finger","start":1772,"end":1843},{"id":"PF02172","name":"KIX domain","start":588,"end":667},{"id":"PF06001","name":"CREB-binding protein/p300, atypical RING domain","start":1192,"end":1231},{"id":"PF09030","name":"Creb binding","start":2014,"end":2113},{"id":"PF23570","name":"Histone acetyltransferase p300-like, PHD domain","start":1276,"end":1314},{"id":"PF29847","name":"Histone acetyltransferase domain KAT3","start":1342,"end":1649}],"gene3D":[{"start":1761,"end":1872,"id":"1.20.1020.10","name":"TAZ domain"},{"start":1273,"end":1318,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":1050,"end":1197,"id":"1.20.920.10","name":"Bromodomain-like"},{"start":2058,"end":2116,"id":"1.10.1630.10","name":"Nuclear receptor coactivator, CREB-bp-like, interlocking domain"},{"start":1206,"end":1272,"id":"2.10.110.40","name":"2.10.110.40"},{"start":341,"end":440,"id":"1.20.1020.10","name":"TAZ domain"},{"start":1699,"end":1751,"id":"3.30.60.90","name":"3.30.60.90"},{"start":587,"end":673,"id":"1.10.246.20","name":"Coactivator CBP, KIX domain"}]},"uniref50":"UniRef50_Q92793","sequence":"MAENLLDGPPNPKRAKLSSPGFSANDSTDFGSLFDLENDLPDELIPNGGELGLLNSGNLVPDAASKHKQLSELLRGGSGSSINPGIGNVSASSPVQQGLGGQAQGQPNSANMASLSAMGKSPLSQGDSSAPSLPKQAASTSGPTPAASQALNPQAQKQVGLATSSPATSQTGPGICMNANFNQTHPGLLNSNSGHSLINQASQGQAQVMNGSLGAAGRGRGAGMPYPTPAMQGASSSVLAETLTQVSPQMTGHAGLNTAQAGGMAKMGITGNTSPFGQPFSQAGGQPMGATGVNPQLASKQSMVNSLPTFPTDIKNTSVTNVPNMSQMQTSVGIVPTQAIATGPTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRACSLPHCRTMKNVLNHMTHCQAGKACQVAHCASSRQIISHWKNCTRHDCPVCLPLKNASDKRNQQTILGSPASGIQNTIGSVGTGQQNATSLSNPNPIDPSSMQRAYAALGLPYMNQPQTQLQPQVPGQQPAQPQTHQQMRTLNPLGNNPMNIPAGGITTDQQPPNLISESALPTSLGATNPLMNDGSNSGNIGTLSTIPTAAPPSSTGVRKGWHEHVTQDLRSHLVHKLVQAIFPTPDPAALKDRRMENLVAYAKKVEGDMYESANSRDEYYHLLAEKIYKIQKELEEKRRSRLHKQGILGNQPALPAPGAQPPVIPQAQPVRPPNGPLSLPVNRMQVSQGMNSFNPMSLGNVQLPQAPMGPRAASPMNHSVQMNSMGSVPGMAISPSRMPQPPNMMGAHTNNMMAQAPAQSQFLPQNQFPSSSGAMSVGMGQPPAQTGVSQGQVPGAALPNPLNMLGPQASQLPCPPVTQSPLHPTPPPASTAAGMPSLQHTTPPGMTPPQPAAPTQPSTPVSSSGQTPTPTPGSVPSATQTQSTPTVQAAAQAQVTPQPQTPVQPPSVATPQSSQQQPTPVHAQPPGTPLSQAAASIDNRVPTPSSVASAETNSQQPGPDVPVLEMKTETQAEDTEPDPGESKGEPRSEMMEEDLQGASQVKEETDIAEQKSEPMEVDEKKPEVKVEVKEEEESSSNGTASQSTSPSQPRKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQSLGYCCGRKYEFSPQTLCCYGKQLCTIPRDAAYYSYQNRYHFCEKCFTEIQGENVTLGDDPSQPQTTISKDQFEKKKNDTLDPEPFVDCKECGRKMHQICVLHYDIIWPSGFVCDNCLKKTGRPRKENKFSAKRLQTTRLGNHLEDRVNKFLRRQNHPEAGEVFVRVVASSDKTVEVKPGMKSRFVDSGEMSESFPYRTKALFAFEEIDGVDVCFFGMHVQEYGSDCPPPNTRRVYISYLDSIHFFRPRCLRTAVYHEILIGYLEYVKKLGYVTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAFAERIIHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKKEESTAASETTEGSQGDSKNAKKKNNKKTNKNKSSISRANKKKPSMPNVSNDLSQKLYATMEKHKEVFFVIHLHAGPVINTLPPIVDPDPLLSCDLMDGRDAFLTLARDKHWEFSSLRRSKWSTLCMLVELHTQGQDRFVYTCNECKHHVETRWHCTVCEDYDLCINCYNTKSHAHKMVKWGLGLDDEGSSQGEPQSKSPQESRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPVCKQLIALCCYHAKHCQENKCPVPFCLNIKHKLRQQQIQHRLQQAQLMRRRMATMNTRNVPQQSLPSPTSAPPGTPTQQPSTPQTPQPPAQPQPSPVSMSPAGFPSVARTQPPTTVSTGKPTSQVPAPPPPAQPPPAAVEAARQIEREAQQQQHLYRVNINNSMPPGRTGMGTPGSQMAPVSLNVPRPNQVSGPVMPSMPPGQWQQAPLPQQQPMPGLPRPVISMQAQAAVAGPRMPSVQPPRSISPSALQDLLRTLKSPSSPQQQQQVLNILKSNPQLMAAFIKQRTAKYVANQPGMQPQPGLQSQPGMQPQPGMHQQPSLQNLNAMQAGVPRPGVPPQQQAMGGLNPQGQALNIMNPGHNPNMASMNPQYREMLRRQLLQQQQQQQQQQQQQQQQQQGSAGMAGGMAGHGQFQQPQGPGGYPPAMQQQQRMQQHLPLQGSSMGQMAAQMGQLGQMGQPGLGADSTPNIQQALQQRILQQQQMKQQIGSPGQPNPMSPQQHMLSGQPQASHLPGQQIATSLSNQVRSPAPVQSPRPQSQPPHSSPSPRIQPQPSPHHVSPQTGSPHPGLAVTMASSIDQGHLGNPEQSAMLPQLNTPSRSALSSELSLVGDTTGDTLEKFVEGL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q92793","disprot_id":"DP02004","ncbi_taxon_id":9606,"regions_counter":12,"creator":"ralderson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1080,"region_id":"DP02004r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP. <i> Contreras-Martos S, Piai A, Kosol S, Varadi M, Bekesi A, Lebrun P, Volkov AN, Gevaert K, Pierattelli R, Felli IC, Tompa P. </i> Sci Rep, 2017","statement":[{"text":"In far-ultraviolet (UV) circular dichroism, ID3 has a strong negative peak around 200 nm, typical of random coil proteins, with a slight tendency to local secondary structure formation","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"thorvath","start":674,"term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"28680062","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T21:14:28.878Z"}},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":1050,"term_name":"protein binding","start":999,"ec_name":"site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion","statement":[{"text":"The PREs observed with the three ZFP106-f constructs confirmed the interaction and highlighted two significantly affected ID3 regions, one in the N-terminal region (NTR, 674–780) and the other in the C-terminal region (CTR, 999–1050) (Fig. 6b).","type":"Results"},{"text":"Further corroboration came with additional control experiments, in which the paramagnetic label free in solution (upon reduction of the disulfide bond between ZFP106-M2-cys and the label) also gave rise to same type of nonspecific signal in NTR of ID3, whereas it did not affect the signal at the CTR, confirming that the observed effects at the CTR of ID3 are due to the specific interaction of the two proteins (Supplementary Fig. S7d).","type":"Results"}],"curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"28680062","version":4,"reference_html":"Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP. <i> Contreras-Martos S, Piai A, Kosol S, Varadi M, Bekesi A, Lebrun P, Volkov AN, Gevaert K, Pierattelli R, Felli IC, Tompa P. </i> Sci Rep, 2017","date":"2023-05-04T21:33:11.912Z","term_id":"GO:0005515","ec_id":"ECO:0006289","region_id":"DP02004r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"curator_orcid":"0000-0001-8399-7907","interaction_partner":[{"db":"UniProt","id":"Q9H2Y7","operator":"and","partner_start":1265,"partner_end":1521}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:42:49.542Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":2057,"region_id":"DP02004r003","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Just a Flexible Linker? The Structural and Dynamic Properties of CBP-ID4 Revealed by NMR Spectroscopy. <i> Piai A, Calçada EO, Tarenzi T, Grande AD, Varadi M, Tompa P, Felli IC, Pierattelli R. </i> Biophys J, 2016","statement":[{"text":"The 1H-15N correlation spectrum exhibits all of the peculiar NMR features of an IDP, namely, a reduced chemical-shift dispersion that is particularly pronounced in the 1H dimension, and a high degree of signal crowding.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1852,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"26789760","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-05-04T21:37:46.062Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:42:43.398Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1080,"region_id":"DP02004r004","released":"2023_06","ec_id":"ECO:0007689","reference_html":"Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP. <i> Contreras-Martos S, Piai A, Kosol S, Varadi M, Bekesi A, Lebrun P, Volkov AN, Gevaert K, Pierattelli R, Felli IC, Tompa P. </i> Sci Rep, 2017","statement":[{"text":"Both in SDS-PAGE and size-exclusion chromatography (SEC), the apparent molecular weight (Mw) of ID3 is about 70 kDa, two times its actual Mw, which is often the first indication of structural disorder16. ","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":674,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"28680062","version":3,"ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","date":"2023-05-04T20:59:58.543Z","reference_source":"pmid","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:42:44.945Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1080,"region_id":"DP02004r005","released":"2022_03","ec_id":"ECO:0007680","reference_html":"Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP. <i> Contreras-Martos S, Piai A, Kosol S, Varadi M, Bekesi A, Lebrun P, Volkov AN, Gevaert K, Pierattelli R, Felli IC, Tompa P. </i> Sci Rep, 2017","statement":[{"text":"Both in SDS-PAGE and size-exclusion chromatography (SEC), the apparent molecular weight (Mw) of ID3 is about 70 kDa, two times its actual Mw, which is often the first indication of structural disorder","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"thorvath","start":674,"term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"28680062","version":2,"ec_name":"chromatography evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T21:02:49.333Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1080,"region_id":"DP02004r006","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP. <i> Contreras-Martos S, Piai A, Kosol S, Varadi M, Bekesi A, Lebrun P, Volkov AN, Gevaert K, Pierattelli R, Felli IC, Tompa P. </i> Sci Rep, 2017","statement":[{"text":"SAXS, circular dichroism and NMR spectroscopy showed for ID3 a random coil state. By integrating 1H-detected and 13C-detected high-resolution multi-dimensional NMR experiments18, 20–22 we assigned about 95% of backbone chemical shifts, providing atomic resolution information on its structural and dynamic features.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":674,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"28680062","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-05-04T21:13:16.025Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:42:47.820Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1080,"region_id":"DP02004r007","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP. <i> Contreras-Martos S, Piai A, Kosol S, Varadi M, Bekesi A, Lebrun P, Volkov AN, Gevaert K, Pierattelli R, Felli IC, Tompa P. </i> Sci Rep, 2017","statement":[{"text":"SAXS measurements [following removal of potential aggregates by high-pressure liquid chromatography (HPLC)] yielded an average radius of gyration (Rg) of 80 Å of the different conformers in solution (Fig. 1c and e), corresponding to a disordered state.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"thorvath","start":674,"term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"28680062","version":2,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T20:57:42.826Z"}},{"start":674,"end":1080,"reference_id":"28680062","reference_source":"pmid","reference_html":"Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP. <i> Contreras-Martos S, Piai A, Kosol S, Varadi M, Bekesi A, Lebrun P, Volkov AN, Gevaert K, Pierattelli R, Felli IC, Tompa P. </i> Sci Rep, 2017","date":"2023-05-04T21:27:29.937Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP02004r008","statement":[{"text":"In far-ultraviolet (UV) circular dichroism, ID3 has a strong negative peak around 200 nm, typical of random coil proteins, with a slight tendency to local secondary structure formation16 (Supplementary Fig. S1b)","type":"Results"},{"text":"The intrinsically disordered region 3 (ID3, aa674–1080) is located between the KIX domain and bromodomain of CBP.","type":"Results"},{"text":"Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP.","type":"Title"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:42:51.434Z"}},{"start":674,"end":1080,"reference_id":"28680062","reference_source":"pmid","reference_html":"Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP. <i> Contreras-Martos S, Piai A, Kosol S, Varadi M, Bekesi A, Lebrun P, Volkov AN, Gevaert K, Pierattelli R, Felli IC, Tompa P. </i> Sci Rep, 2017","date":"2023-05-05T12:52:32.989Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006309","ec_ontology":"ECO","ec_name":"competitive binding evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP02004r009","statement":[{"text":"The free ID3 was found to compete with the ID3 of full-length CBP for binding the substrate, ZFP106-f, causing a significant concentration-dependent decrease in the acetylation of ZFP106-f (Fig. 4a).","type":"Results"},{"text":"Overall, these results show that ID3 specifically binds to ZFP106-f via defined sequence features.","type":"Results"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9H2Y7","operator":null,"partner_start":1256,"partner_end":1521}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:42:53.813Z"}},{"start":674,"end":1080,"reference_id":"28680062","reference_source":"pmid","reference_html":"Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP. <i> Contreras-Martos S, Piai A, Kosol S, Varadi M, Bekesi A, Lebrun P, Volkov AN, Gevaert K, Pierattelli R, Felli IC, Tompa P. </i> Sci Rep, 2017","date":"2023-05-05T12:53:02.132Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP02004r010","statement":[{"text":"We observed on SDS-PAGE the formation of high-Mw complexes in which the presence (and thus interaction) of both protein partners was proven by two consecutive Western blots (with a membrane stripping step in between) with anti-His and anti-GST antibody to visualize high-Mw overlapping bands (box).","type":"Results"}],"ec_go":"IEP","interaction_partner":[{"db":"UniProt","id":"Q9H2Y7","operator":null,"partner_start":1256,"partner_end":1521}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:42:55.104Z"}},{"start":1852,"end":2057,"reference_id":"28680062","reference_source":"pmid","reference_html":"Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP. <i> Contreras-Martos S, Piai A, Kosol S, Varadi M, Bekesi A, Lebrun P, Volkov AN, Gevaert K, Pierattelli R, Felli IC, Tompa P. </i> Sci Rep, 2017","date":"2023-05-04T21:52:57.878Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP02004r011","statement":[{"text":"The 1H-15N correlation spectrum exhibits all of the peculiar NMR features of an IDP, namely, a reduced chemical-shift dispersion that is particularly pronounced in the 1H dimension, and a high degree of signal crowding.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:42:57.057Z"}}],"released":"2018_11","uniref100":"UniRef100_Q92793","date":"2018-08-22T14:40:42.000Z","acc":"Q92793","name":"CREB-binding protein","length":2442,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins","Condensates-related proteins"],"UniParc":"UPI000003B44A","genes":[{"name":{"value":"CREBBP"},"synonyms":[{"value":"CBP"}]}],"alphafold_very_low_content":0.6081081081081081,"disorder_content":0.251023751023751,"disprot_consensus":{"full":[{"start":674,"end":1080,"type":"D"},{"start":1852,"end":2057,"type":"D"}],"Structural state":[{"start":674,"end":1080,"type":"D"},{"start":1852,"end":2057,"type":"D"}],"Molecular function":[{"start":674,"end":1080,"type":"F"}],"Disorder function":[{"start":674,"end":1080,"type":"F"},{"start":1852,"end":2057,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_P47710","sequence":"MRLLILTCLVAVALARPKLPLRYPERLQNPSESSEPIPLESREEYMNGMNRQRNILREKQTDEIKDTRNESTQNCVVAEPEKMESSISSSSEEMSLSKCAEQFCRLNEYNQLQLQAAHAQEQIRRMNENSHVQVPFQQLNQLAAYPYAVWYYPQIMQYVPFPPFSDISNPTAHENYEKNNVMLQW","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P47710","disprot_id":"DP02005","ncbi_taxon_id":9606,"regions_counter":1,"creator":"lpaladin","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":185,"region_id":"DP02005r001","released":"2022_03","ec_id":"ECO:0007691","reference_html":"ADP-ribosylation factor 6 acts as an allosteric activator for the folded but not disordered cholera toxin A1 polypeptide. <i> Banerjee T, Taylor M, Jobling MG, Burress H, Yang Z, Serrano A, Holmes RK, Tatulian SA, Teter K. </i> Mol Microbiol, 2014","statement":[{"text":"Lipid raft LUVs did not prevent the degradation of α-casein, a protein with an open conformation that is susceptible to proteolysisat all temperatures.","type":"Article"}],"term_id":"IDPO:0000002","curator_id":"lpaladin","start":1,"term_ontology":"IDPO","curator_name":"Lisanna Paladin","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-0011-9397","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"25257027","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P47710","date":"2018-08-22T14:49:02.000Z","acc":"P47710","name":"Alpha-S1-casein","length":185,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000126FCB","genes":[{"name":{"value":"CSN1S1"},"synonyms":[{"value":"CASA"},{"value":"CSN1"}]}],"alphafold_very_low_content":0.33513513513513515,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":185,"type":"D"}],"Structural state":[{"start":1,"end":185,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00265","name":"Thymidine kinase","start":19,"end":189}],"gene3D":[{"start":18,"end":149,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":150,"end":194,"id":"3.30.60.20","name":"3.30.60.20"}]},"uniref50":"UniRef50_P04183","sequence":"MSCINLPTVLPGSPSKTRGQIQVILGPMFSGKSTELMRRVRRFQIAQYKCLVIKYAKDTRYSSSFCTHDRNTMEALPACLLRDVAQEALGVAVIGIDEGQFFPDIVEFCEAMANAGKTVIVAALDGTFQRKPFGAILNLVPLAESVVKLTAVCMECFREAAYTKRLGTEKEVEVIGGADKYHSVCRLCYFKKASGQPAGPDNKENCPVPGKPGEAVAARKLFAPQQILQCSPAN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P04183","disprot_id":"DP02006","ncbi_taxon_id":9606,"regions_counter":3,"creator":"jlecle","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":73,"region_id":"DP02006r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Comparative active-site mutation study of human and Caenorhabditis elegans thymidine kinase 1. <i> Skovgaard T, Uhlin U, Munch-Petersen B. </i> FEBS J, 2012","statement":[{"text":"Owing to flexible parts, none of the subunits display electron density before amino acid 18 and after amino acid 192. Density is also absent for the loop between amino acids 64 and 73.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jlecle","start":64,"term_ontology":"IDPO","curator_name":"Jeremy Y Leclercq","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0372-3277","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2WVJ"}],"reference_id":"22385435","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":17,"region_id":"DP02006r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Comparative active-site mutation study of human and Caenorhabditis elegans thymidine kinase 1. <i> Skovgaard T, Uhlin U, Munch-Petersen B. </i> FEBS J, 2012","statement":[{"text":"Owing to flexible parts, none of the subunits display electron density before amino acid 18 and after amino acid 192. Density is also absent for the loop between amino acids 64 and 73.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jlecle","start":1,"term_ontology":"IDPO","curator_name":"Jeremy Y Leclercq","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0372-3277","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2WVJ"}],"reference_id":"22385435","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":234,"region_id":"DP02006r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Comparative active-site mutation study of human and Caenorhabditis elegans thymidine kinase 1. <i> Skovgaard T, Uhlin U, Munch-Petersen B. </i> FEBS J, 2012","statement":[{"text":"Owing to flexible parts, none of the subunits display electron density before amino acid 18 and after amino acid 192. Density is also absent for the loop between amino acids 64 and 73.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jlecle","start":193,"term_ontology":"IDPO","curator_name":"Jeremy Y Leclercq","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0372-3277","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2WVJ"}],"reference_id":"22385435","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P04183","date":"2018-08-22T15:06:06.000Z","acc":"P04183","name":"Thymidine kinase, cytosolic","length":234,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000161B4B","genes":[{"name":{"value":"TK1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11830","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11830"}}]}}],"alphafold_very_low_content":0.18803418803418803,"disorder_content":0.2948717948717949,"disprot_consensus":{"full":[{"start":1,"end":17,"type":"D"},{"start":64,"end":73,"type":"D"},{"start":193,"end":234,"type":"D"}],"Structural state":[{"start":1,"end":17,"type":"D"},{"start":64,"end":73,"type":"D"},{"start":193,"end":234,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00400","name":"WD domain, G-beta repeat","start":1525,"end":1557},{"id":"PF00400","name":"WD domain, G-beta repeat","start":1562,"end":1602},{"id":"PF00400","name":"WD domain, G-beta repeat","start":1647,"end":1684},{"id":"PF00400","name":"WD domain, G-beta repeat","start":1692,"end":1723},{"id":"PF00400","name":"WD domain, G-beta repeat","start":1730,"end":1765}],"gene3D":[{"start":1617,"end":1804,"id":"2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"},{"start":1455,"end":1616,"id":"2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"},{"start":1805,"end":1877,"id":"3.30.160.60","name":"Classic Zinc Finger"}]},"uniref50":"UniRef50_O88466","sequence":"MPVGRIECPSSPSFPRDISHECRVCGVTEVGLSAYAKHISGQLHKDNVDAQEREDDGKGEEEEEDYFDKELIQLIKQRKEQSRQDEPSNSNQEINSDDRRPQWRREDRIPYQDRESYSQPAWHHRGPPQRDWKWEKDGFNNTRKNSFPHSLRNGGGPRGRSGWHKGVAGGSSTWFHNHSNSGGGWLSNSGAVDWNHNGTGRNSSWLSEGTGGFSSWHMNNSNGNWKSSVRSTNNWNYSGPGDKFQPGRNRNSNCQMEDMTMLWNKKSNKSNKYSHDRYNWQRQENDKLGTVATYRGPSEGFTSDKFPSEGLLDFNFEQLESQTTKQADTATSKVSGKNGSAAREKPRRWTPYPSQKTLDLQSGLKDITGNKSEMIEKPLFDFSLITTGIQEPQTDETRNSPTQKTQKEIHTGSLNHKASSDSAASFEVVRQCPTAEKPEQEHTPNKMPSLKSPLLPCPATKSLSQKQDPKNISKNTKTNFFSPGEHSNPSNKPTVEDNHGPYISKLRSSCPHVLKGNKSTFGSQKQSGDNLNDTLRKAKEVLQCHESLQNPLLSTSKSTRNYAKASRNVEESEKGSLKIEFQVHALEDESDGETSDTEKHGTKIGTLGSATTELLSGSTRTADEKEEDDRILKTSRELSTSPCNPIVRQKESELQMTSAASPHPGLLLDLKTSLEDAQVDDSIKSHVSYETEGFESASLDAELQKSDISQPSGPLLPELSKLGFPASLQRDLTRHISLKSKTGVHLPEPNLNSARRIRNISGHRKSETEKESGLKPTLRQILNASRRNVNWEQVIQQVTKKKQELGKGLPRFGIEMVPLVQNEQEALDLDGEPDLSSLEGFQWEGVSISSSPGLARKRSLSESSVIMDRAPSVYSFFSEEGTGKENEPQQMVSPSNSLRAGQSQKATMHLKQEVTPRAASLRTGERAENVATQRRHSAQLSSDHIIPLMHLAKDLNSQERSIPPSENQNSQESNGEGNCLSSSASSALAISSLADAATDSSCTSGAEQNDGQSIRKKRRATGDGSSPELPSLERKNKRRKIKGKKERSQVDQLLNISLREEELSKSLQCMDNNLLQARAALQTAYVEVQRLLMLKQQITMEMSALRTHRIQILQGLQETYEPSEHPDQVPCSLTRERRNSRSQTSIDAALLPTPFFPLFLEPPSSHVSPSPTGASLQITTSPTFQTHGSVPAPDSSVQIKQEPMSPEQDENVNAVPPSSACNVSKELLEANREISDSCPVYPVITARLSLPESTESFHEPSQELKFSVEQRNTRNRENSPSSQSAGLSSINKEGEEPTKGNSGSEACTSSFLRLSFASETPLEKEPHSPADQPEQQAESTLTSAETRGSKKKKKLRKKKSLRAAHVPENSDTEQDVLTVKPVRKVKAGKLIKGGKVTTSTWEDSRTGREQESVRDEPDSDSSLEVLEIPNPQLEVVAIDSSESGEEKPDSPSKKDIWNSTEQNPLETSRSGCDEVSSTSEIGTRYKDGIPVSVAETQTVISSIKGSKNSSEISSEPGDDDEPTEGSFEGHQAAVNAIQIFGNLLYTCSADKTVRVYNLVSRKCIGVFEGHTSKVNCLLVTQTSGKNAALYTGSSDHTIRCYNVKSRECVEQLQLEDRVLCLHSRWRILYAGLANGTVVTFNIKNNKRLEIFECHGPRAVSCLATAQEGARKLLVVGSYDCTISVRDARNGLLLRTLEGHSKTILCMKVVNDLVFSGSSDQSVHAHNIHTGELVRIYKGHNHAVTVVNILGKVMVTACLDKFVRVYELQSHDRLQVYGGHKDMIMCMTIHKSMIYTGCYDGSIQAVRLNLMQNYRCWWHGCSLIFGVVDHLKQHLLTDHTNPNFQTLKCRWKNCDAFFTARKGSKQDAAGHIERHAEDDSKIDS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9H2Y7","disprot_id":"DP02007","ncbi_taxon_id":9606,"regions_counter":4,"creator":"thorvath","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1521,"region_id":"DP02007r001","released":"2023_06","ec_id":"ECO:0006204","reference_html":"Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP. <i> Contreras-Martos S, Piai A, Kosol S, Varadi M, Bekesi A, Lebrun P, Volkov AN, Gevaert K, Pierattelli R, Felli IC, Tompa P. </i> Sci Rep, 2017","statement":[{"text":"In silico analysis and circular dichroism experiments (Fig. 5) showed that ZFP106-f is also largely disordered, which suggests a rather transient binding between the two IDRs that can occur either via a mutual (synergistic) folding39 or a “fuzzy” interaction31, in which both IDRs remain largely disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1265,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"28680062","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2023-05-04T21:22:53.510Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":1521,"term_name":"protein binding","start":1265,"ec_name":"qualitative western immunoblotting evidence used in manual assertion","statement":[{"text":"We observed on SDS-PAGE the formation of high-Mw complexes in which the presence (and thus interaction) of both protein partners was proven by two consecutive Western blots (with a membrane stripping step in between) with anti-His and anti-GST antibody to visualize high-Mw overlapping bands (box).","type":"Results"}],"curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"28680062","version":4,"reference_html":"Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP. <i> Contreras-Martos S, Piai A, Kosol S, Varadi M, Bekesi A, Lebrun P, Volkov AN, Gevaert K, Pierattelli R, Felli IC, Tompa P. </i> Sci Rep, 2017","date":"2023-05-04T21:26:00.885Z","term_id":"GO:0005515","ec_id":"ECO:0000279","region_id":"DP02007r002","ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"curator_orcid":"0000-0001-8399-7907","interaction_partner":[{"db":"UniProt","id":"Q92793","operator":"and","partner_start":674,"partner_end":1080}]},{"start":1256,"end":1521,"reference_id":"28680062","reference_source":"pmid","reference_html":"Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP. <i> Contreras-Martos S, Piai A, Kosol S, Varadi M, Bekesi A, Lebrun P, Volkov AN, Gevaert K, Pierattelli R, Felli IC, Tompa P. </i> Sci Rep, 2017","date":"2023-05-05T12:55:32.902Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006309","ec_ontology":"ECO","ec_name":"competitive binding evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q92793","operator":null,"partner_start":674,"partner_end":1080}],"region_id":"DP02007r003","statement":[{"text":"The free ID3 was found to compete with the ID3 of full-length CBP for binding the substrate, ZFP106-f, causing a significant concentration-dependent decrease in the acetylation of ZFP106-f (Fig. 4a).","type":"Results"},{"text":"Overall, these results show that ID3 specifically binds to ZFP106-f via defined sequence features.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1300,"end":1400,"reference_id":"28680062","reference_source":"pmid","reference_html":"Linking functions: an additional role for an intrinsically disordered linker domain in the transcriptional coactivator CBP. <i> Contreras-Martos S, Piai A, Kosol S, Varadi M, Bekesi A, Lebrun P, Volkov AN, Gevaert K, Pierattelli R, Felli IC, Tompa P. </i> Sci Rep, 2017","date":"2023-05-05T12:58:31.433Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006289","ec_ontology":"ECO","ec_name":"site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"EXP","region_id":"DP02007r004","statement":[{"text":"Moreover, the interacting region(s) of ZFP106-f can be delineated from the different effects the presence of the three ZFP106-f constructs has on ID3 signal intensities in the 2D 1H-15N NMR spectra (Fig. 6b). A strong signal decrease was observed with the ZFP106-f-M2, and much weaker effect with ZFP106-f-M1. The paramagnetic tag sites M1 and M2 are in relative close proximity to each other (Fig. 6a). In contrast, ZFP106-f-M3 caused no change in signal intensity in the CTR of ID3, suggesting an interaction site between residues 1300–1400 of ZFP106 (Fig. 6).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_Q9H2Y7","date":"2018-08-22T15:24:23.000Z","acc":"Q9H2Y7","name":"Zinc finger protein 106","length":1883,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000006D6CC","genes":[{"name":{"value":"ZNF106"},"synonyms":[{"value":"SH3BP3"},{"value":"ZFP106"},{"value":"ZNF474"}]}],"alphafold_very_low_content":0.724907063197026,"disorder_content":0.13648433351035583,"disprot_consensus":{"full":[{"start":1256,"end":1264,"type":"F"},{"start":1265,"end":1521,"type":"D"}],"Structural state":[{"start":1265,"end":1521,"type":"D"}],"Molecular function":[{"start":1256,"end":1521,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03062","name":"MBOAT, membrane-bound O-acyltransferase family","start":255,"end":487}]},"uniref50":"UniRef50_A0A161IUT7","sequence":"MEILDSGGVTMPTENGGADLDTLRHRKPRSDSSNGLLPDSVTVSDADVRDRVDSAVEDTQGKANLAGENEIRESGGEAGGNVDVRYTYRPSVPAHRRVRESPLSSDAIFKQSHAGLFNLCVVVLVAVNSRLIIENLMKYGWLIRTDFWFSSTSLRDWPLFMCCLSLSIFPLAAFTVEKLVLQKCISEPVVIILHIIITMTEVLYPVYVTLRCDSAFLSGVTLMLLTCIVWLKLVSYAHTNYDIRTLANSSDKANPEVSYYVSLKSLAYFMLAPTLCYQPSYPRSPCIRKGWVARQFAKLIIFTGFMGFIIEQYINPIVRNSKHPLKGDLLYGVERVLKLSVPNLYVWLCMFYCFFHLWLNILAELLCFGDREFYKDWWNAKSVGDYWRMWNMPVHKWMVRHVYFPCLRRNIPKVPAIILAFLVSAVFHELCIAVPCRLFKLWAFLGIMFQVPLVFITNYLQERFGSMVGNMIFWFTFCIFGQPMCVLLYYHDLMNRKGKMS","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Brassiceae","Brassica"],"uniref90":"UniRef90_A0A078J7P3","disprot_id":"DP02008","ncbi_taxon_id":3708,"regions_counter":9,"creator":"nfarahi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":80,"region_id":"DP02008r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Diacylglycerol Acyltransferase 1 Is Regulated by Its N-Terminal Domain in Response to Allosteric Effectors. <i> Caldo KMP, Acedo JZ, Panigrahi R, Vederas JC, Weselake RJ, Lemieux MJ. </i> Plant Physiol, 2017","statement":[{"text":"Figure 4. CD spectra of BnaDGAT11-80 and BnaDGAT181-113. Residues 1 to 80 are highly disordered","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"nfarahi","start":1,"term_ontology":"IDPO","curator_name":"Nazanin Farahi","reference_id":"28827454","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0002-6834-8578","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:11:14.552Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":80,"term_name":"protein binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"The highly disordered region of BnaDGAT1, residues 1 to 80, was found to facilitate dimerization, as evident from cross-linking studies (Fig. 7).","type":"Discussion"}],"curator_id":"nfarahi","released":"2022_03","term_ontology":"GO","curator_name":"Nazanin Farahi","reference_id":"28827454","version":4,"reference_html":"Diacylglycerol Acyltransferase 1 Is Regulated by Its N-Terminal Domain in Response to Allosteric Effectors. <i> Caldo KMP, Acedo JZ, Panigrahi R, Vederas JC, Weselake RJ, Lemieux MJ. </i> Plant Physiol, 2017","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006204","region_id":"DP02008r002","curator_orcid":"0000-0002-6834-8578","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:11:10.727Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":80,"reference_id":"30420764","reference_source":"pmid","reference_html":"Intrinsic disorder in the regulatory N-terminal domain of diacylglycerol acyltransferase 1 from Brassica napus. <i> Panigrahi R, Matsui T, Song AH, Caldo KMP, Young HS, Weselake RJ, Lemieux MJ. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP02008r003","statement":[{"text":"The mobility of these recombinant proteins on SDS-PAGE was atypical as they migrated slower than expected, based on their expected molecular masses (16 kDa and 9 kDa, respectively) (Fig. 2 inset). This lower mobility, specifically observed with the recombinant N-terminal domains of BnaDGAT11-80, is often observed in IDPs (eg. Juxtanodin) and attributed to the lack of hydrophobic amino acid residues and anomalous interaction with SDS.","type":"Results"},{"text":"Disorder is also claimed for the longer segment 1-113, but in the previous paper they have shown that the segment 81-113 is folded.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:11:15.525Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":1,"end":80,"reference_id":"30420764","reference_source":"pmid","reference_html":"Intrinsic disorder in the regulatory N-terminal domain of diacylglycerol acyltransferase 1 from Brassica napus. <i> Panigrahi R, Matsui T, Song AH, Caldo KMP, Young HS, Weselake RJ, Lemieux MJ. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP02008r004","statement":[{"text":"Additionally, these purified constructs were susceptible to proteolysis despite the addition of protease inhibitors.","type":"Results"},{"text":"Disorder is also claimed for the longer segment 1-113, but in the previous paper they have shown that the segment 81-113 is folded.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:11:19.093Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":1,"end":80,"reference_id":"30420764","reference_source":"pmid","reference_html":"Intrinsic disorder in the regulatory N-terminal domain of diacylglycerol acyltransferase 1 from Brassica napus. <i> Panigrahi R, Matsui T, Song AH, Caldo KMP, Young HS, Weselake RJ, Lemieux MJ. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP02008r005","statement":[{"text":"These studies confirmed the molecular masses 13.9 kDa (BnaDGAT11-113) and 8.6 kDa (BnaDGAT11-80). The apparent molecular mass calculated from SEC-MALLS were lower than that calculated using SEC standards demonstrating the nonglobular and monomeric nature of the purified constructs.","type":"Results"},{"text":"Disorder is also claimed for the longer segment 1-113, but in the previous paper they have shown that the segment 81-113 is folded.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:11:20.054Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":80,"reference_id":"30420764","reference_source":"pmid","reference_html":"Intrinsic disorder in the regulatory N-terminal domain of diacylglycerol acyltransferase 1 from Brassica napus. <i> Panigrahi R, Matsui T, Song AH, Caldo KMP, Young HS, Weselake RJ, Lemieux MJ. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP02008r006","statement":[{"text":"In the absence of ligand, both proteins exhibited a negative minimum close to 200 nm, a typical observation for disordered proteins37 (Fig. 4A,B).","type":"Results"},{"text":"Disorder is also claimed for the longer segment 1-113, but in the previous paper they have shown that the segment 81-113 is folded.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:11:21.357Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":113,"reference_id":"30420764","reference_source":"pmid","reference_html":"Intrinsic disorder in the regulatory N-terminal domain of diacylglycerol acyltransferase 1 from Brassica napus. <i> Panigrahi R, Matsui T, Song AH, Caldo KMP, Young HS, Weselake RJ, Lemieux MJ. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP02008r007","statement":[{"text":"The scattering profiles, for the various forms of BnaDGAT11-113, exhibited a typical profile of IDRs (Fig. 5A).","type":"Results"},{"text":"Here, with the low-resolution techniques disorder is claimed for the longer segment 1-113, but in the previous paper they have shown that the segment 81-113 is folded.","type":"Curator statement"},{"text":"The Kratky plots do not have maxima, but instead have a short plateau followed by a monotonic increase at higher value of [q]. This indicates the presence of a highly extended particle for BnaDGAT11-113, thus confirming the intrinsically disordered nature of the N-terminal region of BnaDGAT11-113 (Fig. 5B).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:11:23.436Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":80,"reference_id":"30420764","reference_source":"pmid","reference_html":"Intrinsic disorder in the regulatory N-terminal domain of diacylglycerol acyltransferase 1 from Brassica napus. <i> Panigrahi R, Matsui T, Song AH, Caldo KMP, Young HS, Weselake RJ, Lemieux MJ. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0036094","term_name":"small molecule binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP02008r008","statement":[{"text":"ITC was performed to investigate the interaction thermodynamics of BnaDGAT1 N-terminal domain with acyl-CoA and CoA. Four independent systems were analyzed: BnaDGAT11-113 or BnaDGAT11-80 in combination with oleoyl-CoA or CoA.","type":"Results"},{"text":"Interestingly, BnaDGAT11-80 also interacted with both ligands but with lower affinity (Kd of 117 μM for oleoyl-CoA and Kd of 178 μM for CoA) (Fig. 3C, D).","type":"Results"}],"interaction_partner":[{"db":"ChEBI","id":"15346","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"15534","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:11:11.484Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":80,"reference_id":"30420764","reference_source":"pmid","reference_html":"Intrinsic disorder in the regulatory N-terminal domain of diacylglycerol acyltransferase 1 from Brassica napus. <i> Panigrahi R, Matsui T, Song AH, Caldo KMP, Young HS, Weselake RJ, Lemieux MJ. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0036094","term_name":"small molecule binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP02008r009","statement":[{"text":"Contrary to the above, BnaDGAT11-80 showed a decreased helicity upon ligand binding, along with a decrease in random coil nature as demonstrated by the decrease in negative ellipticity at ~200 nm (Fig. 4B). Overall, these observations suggest that there is some gain in helical structure for the entire segment (1-113) and reduction in the random coil nature of the shorter segment upon ligand binding.","type":"Results"}],"interaction_partner":[{"db":"ChEBI","id":"15534","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"15346","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:11:13.536Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q9M4V2","date":"2018-08-22T15:25:59.000Z","acc":"Q9M4V2","name":"O-acyltransferase","length":501,"organism":"Brassica napus","dataset":[],"UniParc":"UPI00000A0807","genes":[{"name":{"value":"DGAT1.a","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AFM31259.1","url":"https://www.ebi.ac.uk/ena/browser/view/AFM31259.1"}}]},"synonyms":[{"value":"DGAT1-4","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AIA67022.1","url":"https://www.ebi.ac.uk/ena/browser/view/AIA67022.1"}}]}]}],"alphafold_very_low_content":0.19560878243512975,"disorder_content":0.22554890219560877,"disprot_consensus":{"full":[{"start":1,"end":113,"type":"D"}],"Structural state":[{"start":1,"end":113,"type":"D"}],"Molecular function":[{"start":1,"end":80,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04935","name":"Surfeit locus protein 6","start":141,"end":340}]},"uniref50":"UniRef50_P70279","sequence":"MASLLAKDAYLQSLAKKICSHSAPEQQARTRAGKTQGSETAGPPKKKRKKTQKKFRKREEKAAEHKAKSLGEKSPAASGARRPEAAKEEAAWASSSAGNPADGLATEPESVFALDVLRQRLHEKIQEARGQGSAKELSPAALEKRRRRKQERDRKKRKRKELRAKEKARKAEEATEAQEVVEATPEGACTEPREPPGLIFNKVEVSEDEPASKAQRRKEKRQRVKGNLTPLTGRNYRQLLERLQARQSRLDELRGQDEGKAQELEAKMKWTNLLYKAEGVKIRDDERLLQEALKRKEKRRAQRQRRWEKRTAGVVEKMQQRQDRRRQNLRRKKAARAERRLLRARKKGRILPQDLERAGLV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O75683","disprot_id":"DP02009","ncbi_taxon_id":9606,"regions_counter":3,"creator":"thorvath","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":182,"region_id":"DP02009r001","released":"2023_12","ec_id":"ECO:0006165","reference_html":"Direct detection of carbon and nitrogen nuclei for high-resolution analysis of intrinsically disordered proteins using NMR spectroscopy. <i> Gibbs EB, Kriwacki RW. </i> Methods, 2018","statement":[{"text":"Here, we compared spectral resolution and sensitivity for 2D 1H-15N and 13C-15N correlation spectra recorded through direct detection of each of the two correlated nuclei for two protein regions that are entirely disordered (Hdm2-ABD and Surf6-N) and 2D 1H-15N correlation spectra for a ~73 kDa folded, pentameric protein with two short IDRs (N130).","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"29341926","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-12-12T18:39:56.582Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0001-8399-7907"},{"start":1,"end":195,"reference_id":"37410842","reference_source":"pmid","reference_html":"Principles of human pre-60<i>S</i> biogenesis. <i> Vanden Broeck A, Klinge S. </i> Science, 2023","date":"2023-12-12T18:55:16.978Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"8FKQ"},{"db":"PDB","id":"8FKP"},{"db":"PDB","id":"8FKR"},{"db":"PDB","id":"8FKS"},{"db":"EMDB","id":"29252"},{"db":"EMDB","id":"29253"},{"db":"EMDB","id":"29254"},{"db":"EMDB","id":"29255"}],"region_id":"DP02009r002","statement":[{"text":"The Cryo-EM structures of human pre-60S particles as they matured in the nucleolus and nucleus show this region of the Surfeit locus protein 6 lacks electron density, indicating it is disordered. ","type":"Curator statement"}]},{"start":1,"end":182,"reference_id":"30498217","reference_source":"pmid","reference_html":"Compositional adaptability in NPM1-SURF6 scaffolding networks enabled by dynamic switching of phase separation mechanisms. <i> Ferrolino MC, Mitrea DM, Michael JR, Kriwacki RW. </i> Nat Commun, 2018","date":"2023-12-12T19:10:25.430Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P06748","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02009r003","statement":[{"text":"To these pre-equilibrated homotypic NPM1 droplets, which incorporated client S6N, we added an extra 3.5 mole equivalents of S6N and monitored their composition using time-lapse imaging. Upon addition of this extra amount, S6N was slowly incorporated within the scaffold, as demonstrated by an increase in the S6N-A647:NPM1-A488 fluorescence intensity ratio over time (Fig. 5c, d). Furthermore, S6N competed for pre-existing NPM1-NPM1 interactions, resulting in a decrease in NPM1-Alexa Fluor 488 intensity within droplets (Fig. 5d). This S6N-dependent, partial expulsion of NPM1 from the NPM1-S6N droplets concomitantly triggered formation of de novo, heterotypic droplets with S6N molecules in the light phase (Supplementary Fig. 12).","type":"Results"},{"text":"Together, the results of these scaffold rearrangement experiments suggest that the homotypic (NPM1-NPM1) and heterotypic (NPM1-S6N) scaffolds form miscible, co-existing liquid phases that dynamically interconvert in response to changes in the protein composition of the surrounding milieu.","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_O75683","date":"2018-08-22T15:27:38.000Z","acc":"O75683","name":"Surfeit locus protein 6","length":361,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI000016A3B3","genes":[{"name":{"value":"SURF6"},"synonyms":[{"value":"SURF-6"}]}],"alphafold_very_low_content":0.23545706371191136,"disorder_content":0.5401662049861495,"disprot_consensus":{"full":[{"start":1,"end":195,"type":"D"}],"Structural state":[{"start":1,"end":195,"type":"D"}],"Molecular function":[{"start":1,"end":182,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00048","name":"Small cytokines (intecrine/chemokine), interleukin-8 like","start":28,"end":86}],"gene3D":[{"start":39,"end":95,"id":"2.40.50.40","name":"2.40.50.40"}]},"uniref50":"UniRef50_Q9NRJ3","sequence":"MQQRGLAIVALAVCAALHASEAILPIASSCCTEVSHHISRRLLERVNMCRIQRADGDCDLAAVILHVKRRRICVSPHNHTVKQWMKVQAAKKNGKGNVCHRKKHHGKRNSNRAHQGKHETYGHKTPY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9NRJ3","disprot_id":"DP02010","ncbi_taxon_id":9606,"regions_counter":4,"creator":"thorvath","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":10,"region_id":"DP02010r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The Solution Structure of CCL28 Reveals Structural Lability that Does Not Constrain Antifungal Activity. <i> Thomas MA, He J, Peterson FC, Huppler AR, Volkman BF. </i> J Mol Biol, 2018","statement":[{"text":"The tertiary fold of chemokines is largely stabilized by two characteristic disulfide bonds which link the flexible N-terminus to the chemokine core.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"thorvath","start":1,"term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"29913161","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":108,"region_id":"DP02010r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The Solution Structure of CCL28 Reveals Structural Lability that Does Not Constrain Antifungal Activity. <i> Thomas MA, He J, Peterson FC, Huppler AR, Volkman BF. </i> J Mol Biol, 2018","statement":[{"text":"We propose that the pH-dependent structural lability of CCL28 is important for its role as both a chemoattractant and antimicrobial agent","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"thorvath","start":1,"term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"29913161","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":127,"region_id":"DP02010r004","reference_id":"29913161","start":99,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In addition to having a third, non-canonical disulfide bond, CCL28 has an extended C-terminal domain of 28 residues which follows the most C-terminal cysteine residue (cysteine 80). Our structural and functional analyses revealed that the extended C-terminal domain of CCL28 is unstructured and dynamic","type":"Discussion"},{"text":"The last cysteine in the sequence is Cys99, referred to as \"cysteine 80\" in the paper since the authors cloned the human CCL28 gene lacking its signal peptide (19 amino acids)\"","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"reference_html":"The Solution Structure of CCL28 Reveals Structural Lability that Does Not Constrain Antifungal Activity. <i> Thomas MA, He J, Peterson FC, Huppler AR, Volkman BF. </i> J Mol Biol, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"6CWS"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9NRJ3","date":"2018-08-22T15:29:10.000Z","acc":"Q9NRJ3","name":"C-C motif chemokine 28","length":127,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00001362E3","genes":[{"name":{"value":"CCL28"},"synonyms":[{"value":"SCYA28"}]}],"alphafold_very_low_content":0.1732283464566929,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":127,"type":"D"}],"Structural state":[{"start":1,"end":127,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00849","name":"RNA pseudouridylate synthase","start":69,"end":195},{"id":"PF01479","name":"S4 domain","start":7,"end":52}],"gene3D":[{"start":134,"end":207,"id":"3.30.70.1560","name":"Alpha-L RNA-binding motif"},{"start":1,"end":62,"id":"3.10.290.10","name":"RNA-binding S4 domain"},{"start":70,"end":229,"id":"3.30.70.580","name":"Pseudouridine synthase I, catalytic domain, N-terminal subdomain"}]},"uniref50":"UniRef50_P32684","sequence":"MLPDSSVRLNKYISESGICSRREADRYIEQGNVFLNGKRATIGDQVKPGDVVKVNGQLIEPREAEDLVLIALNKPVGIVSTTEDGERDNIVDFVNHSKRVFPIGRLDKDSQGLIFLTNHGDLVNKILRAGNDHEKEYLVTVDKPITEEFIRGMSAGVPILGTVTKKCKVKKEAPFVFRITLVQGLNRQIRRMCEHFGYEVKKLERTRIMNVSLSGIPLGEWRDLTDDELIDLFKLIENSSSEVKPKAKAKPKTAGIKRPVVKMEKTAEKGGRPASNGKRFTSPGRKKKGR","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P32684","disprot_id":"DP02011","ncbi_taxon_id":83333,"regions_counter":1,"creator":"jlecle","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":290,"region_id":"DP02011r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of an RluF-RNA complex: a base-pair rearrangement is the key to selectivity of RluF for U2604 of the ribosome. <i> Alian A, DeGiovanni A, Griner SL, Finer-Moore JS, Stroud RM. </i> J Mol Biol, 2009","statement":[{"text":"Only residues corresponding to the N-terminal and central domains are visible in our RluF–RNA electron density maps. The C-terminal domain, shown by limited proteolysis to comprise residues Thr253–Arg290, is disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jlecle","start":253,"term_ontology":"IDPO","curator_name":"Jeremy Y Leclercq","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0372-3277","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3DH3"}],"reference_id":"19298824","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P32684","date":"2018-08-22T16:05:51.000Z","acc":"P32684","name":"Dual-specificity RNA pseudouridine synthase RluF","length":290,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI000013B51F","genes":[{"name":{"value":"rluF"},"synonyms":[{"value":"yjbC"}],"olnNames":[{"value":"b4022"},{"value":"JW3982"}]}],"alphafold_very_low_content":0.13793103448275862,"disorder_content":0.1310344827586207,"disprot_consensus":{"full":[{"start":253,"end":290,"type":"D"}],"Structural state":[{"start":253,"end":290,"type":"D"}]}},{"features":{"pfam":[{"id":"PF07201","name":"HrpJ-like domain","start":60,"end":228},{"id":"PF22342","name":"T3SS, Low calcium response E, third helical domain","start":279,"end":377}]},"uniref50":"UniRef50_Q9Z8L4","sequence":"MAASGGTGGLGGTQGVNLAAVEAAAAKADAAEVVASQEGSEMNMIQQSQDLTNPAAATRTKKKEEKFQTLESRKKGEAGKAEKKSESTEEKPDTDLADKYASGNSEISGQELRGLRDAIGDDASPEDILALVQEKIKDPALQSTALDYLVQTTPPSQGKLKEALIQARNTHTEQFGRTAIGAKNILFASQEYADQLNVSPSGLRSLYLEVTGDTHTCDQLLSMLQDRYTYQDMAIVSSFLMKGMATELKRQGPYVPSAQLQVLMTETRNLQAVLTSYDYFESRVPILLDSLKAEGIQTPSDLNFVKVAESYHKIINDKFPTASKVEREVRNLIGDDVDSVTGVLNLFFSALRQTSSRLFSSADKRQQLGAMIANALDAVNINNEDYPKASDFPKPYPWS","taxonomy":["Bacteria","Chlamydiae","Chlamydiales","Chlamydiaceae","Chlamydia/Chlamydophila group","Chlamydia"],"uniref90":"UniRef90_Q9Z8L4","disprot_id":"DP02012","ncbi_taxon_id":83558,"regions_counter":2,"creator":"jlecle","regions":[{"region_id":"DP02012r001","ec_ontology":"ECO","end":95,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":1,"version":3,"statement":[{"text":"The N-terminal region, corresponding to the first ∼95 residues in FL_pCopN, and the last ∼15 C-terminal residues were disordered both in FL_pCopN and in D29.","type":"Results"}],"term_name":"disorder","reference_html":"Biochemical and structural insights into microtubule perturbation by CopN from Chlamydia pneumoniae. <i> Nawrotek A, Guimarães BG, Velours C, Subtil A, Knossow M, Gigant B. </i> J Biol Chem, 2014","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"25056950","date":"2024-02-07T17:35:50.749Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4P40"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MOD:00599","term_name":"monomethylated residue","term_namespace":"Protein modification","start":313,"end":313,"position":"Specific residue"},{"term_id":"MOD:00429","term_name":"dimethylated residue","term_namespace":"Protein modification","start":242,"end":242,"position":"Specific residue"},{"term_id":"MOD:00783","term_name":"dimethylated L-arginine","term_namespace":"Protein modification","start":249,"end":249,"position":"Specific residue"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17170","entry_name":"dimethylamine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"42485","entry_name":"formyl group"}]},{"region_id":"DP02012r002","ec_ontology":"ECO","end":399,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":384,"version":3,"statement":[{"text":"The N-terminal region, corresponding to the first ∼95 residues in FL_pCopN, and the last ∼15 C-terminal residues were disordered both in FL_pCopN and in D29.","type":"Results"}],"term_name":"disorder","reference_html":"Biochemical and structural insights into microtubule perturbation by CopN from Chlamydia pneumoniae. <i> Nawrotek A, Guimarães BG, Velours C, Subtil A, Knossow M, Gigant B. </i> J Biol Chem, 2014","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"25056950","date":"2024-02-07T17:35:42.959Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4P40"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MOD:00599","term_name":"monomethylated residue","term_namespace":"Protein modification","start":313,"end":313,"position":"Specific residue"},{"term_id":"MOD:00429","term_name":"dimethylated residue","term_namespace":"Protein modification","start":242,"end":242,"position":"Specific residue"},{"term_id":"MOD:00429","term_name":"dimethylated residue","term_namespace":"Protein modification","start":249,"end":249,"position":"Specific residue"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17170","entry_name":"dimethylamine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"42485","entry_name":"formyl group"}]}],"released":"2018_11","uniref100":"UniRef100_Q9Z8L4","date":"2018-08-22T16:33:35.000Z","acc":"Q9Z8L4","name":"Low calcium response E","length":399,"organism":"Chlamydia pneumoniae","dataset":[],"UniParc":"UPI0000047085","genes":[{"name":{"value":"lcrE","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAA88665.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAA88665.1"}}]},"orfNames":[{"value":"BN1224_CV15_B_02610","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CRI37938.1","url":"https://www.ebi.ac.uk/ena/browser/view/CRI37938.1"}}]},{"value":"BN1224_DC9_BL_00250","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CRI42437.1","url":"https://www.ebi.ac.uk/ena/browser/view/CRI42437.1"}}]},{"value":"BN1224_GiD_A_03370","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CRI41336.1","url":"https://www.ebi.ac.uk/ena/browser/view/CRI41336.1"}}]},{"value":"BN1224_H12_DC_00070","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CRI43559.1","url":"https://www.ebi.ac.uk/ena/browser/view/CRI43559.1"}}]},{"value":"BN1224_MUL2216_E_00610","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CRI45800.1","url":"https://www.ebi.ac.uk/ena/browser/view/CRI45800.1"}}]},{"value":"BN1224_Panola_E_01460","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CRI46929.1","url":"https://www.ebi.ac.uk/ena/browser/view/CRI46929.1"}}]},{"value":"BN1224_PB1_B_03230","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CRI50354.1","url":"https://www.ebi.ac.uk/ena/browser/view/CRI50354.1"}}]},{"value":"BN1224_U1271_C_01640","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CRI49224.1","url":"https://www.ebi.ac.uk/ena/browser/view/CRI49224.1"}}]},{"value":"BN1224_UZG1_A_03360","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CRI51481.1","url":"https://www.ebi.ac.uk/ena/browser/view/CRI51481.1"}}]},{"value":"BN1224_Wien2_E_01090","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CRI52665.1","url":"https://www.ebi.ac.uk/ena/browser/view/CRI52665.1"}}]},{"value":"BN1224_YK41_BG_00220","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CRI72973.1","url":"https://www.ebi.ac.uk/ena/browser/view/CRI72973.1"}}]},{"value":"CWL029c_C_01640","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CRI40204.1","url":"https://www.ebi.ac.uk/ena/browser/view/CRI40204.1"}}]}],"olnNames":[{"value":"CP_0433","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF38275.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF38275.1"}}]},{"value":"CPn_0324","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAD18473.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD18473.1"}}]}]}],"alphafold_very_low_content":0.09022556390977443,"disorder_content":0.2781954887218045,"disprot_consensus":{"full":[{"start":1,"end":95,"type":"D"},{"start":384,"end":399,"type":"D"}],"Structural state":[{"start":1,"end":95,"type":"D"},{"start":384,"end":399,"type":"D"}]}},{"features":{"pfam":[{"id":"PF13499","name":"EF-hand domain pair","start":12,"end":73},{"id":"PF13499","name":"EF-hand domain pair","start":83,"end":147}],"gene3D":[{"start":1,"end":50,"id":"1.10.238.10","name":"EF-hand"},{"start":112,"end":147,"id":"1.10.238.10","name":"EF-hand"},{"start":51,"end":111,"id":"1.10.238.10","name":"EF-hand"}]},"uniref50":"UniRef50_P0DP23","sequence":"MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P0DP23","disprot_id":"DP02013","ncbi_taxon_id":9606,"regions_counter":4,"creator":"tlazar","regions":[{"start":76,"end":85,"reference_id":"34480001","reference_source":"pmid","reference_html":"Calmodulin extracts the Ras family protein RalA from lipid bilayers by engagement with two membrane-targeting motifs.  <i> Chamberlain SG, Gohlke A, Shafiq A, Squires IJ, Owen D, Mott HR. </i> Proc Natl Acad Sci U S A, 2021","date":"2022-08-08T13:11:57.296Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"BMRB","id":"34608"},{"db":"PDB","id":"7NQC"}],"region_id":"DP02013r002","statement":[{"text":"Upon interaction with the RalA-HVR, the central helix of CaM undergoes extensive unfolding between residues Lys75 and Glu84. Melting of this helix to this extent, although uncommon in CaM structures, is consistent with previous observations that helical content decreases upon complex formation with the RalA HVR (23). This unfolded linker, coupled with the partial disorder of the HVR, results in the lack of fixed orientation of the N-lobe with respect to the C-lobe (Fig. 3A). There is a notable absence of interlobe NOEs, and residues of the central linker show only short-range, mostly intraresidue NOEs, which are not indicative of secondary structure.","type":"Results"}]},{"start":76,"end":85,"reference_id":"34480001","reference_source":"pmid","reference_html":"Calmodulin extracts the Ras family protein RalA from lipid bilayers by engagement with two membrane-targeting motifs.  <i> Chamberlain SG, Gohlke A, Shafiq A, Squires IJ, Owen D, Mott HR. </i> Proc Natl Acad Sci U S A, 2021","date":"2022-08-08T13:12:22.669Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"BMRB","id":"34608"},{"db":"PDB","id":"7NQC"}],"region_id":"DP02013r003","statement":[{"text":"Upon interaction with the RalA-HVR, the central helix of CaM undergoes extensive unfolding between residues Lys75 and Glu84. Melting of this helix to this extent, although uncommon in CaM structures, is consistent with previous observations that helical content decreases upon complex formation with the RalA HVR (23). This unfolded linker, coupled with the partial disorder of the HVR, results in the lack of fixed orientation of the N-lobe with respect to the C-lobe (Fig. 3A). There is a notable absence of interlobe NOEs, and residues of the central linker show only short-range, mostly intraresidue NOEs, which are not indicative of secondary structure.","type":"Results"}]},{"start":76,"end":85,"reference_id":"34480001","reference_source":"pmid","reference_html":"Calmodulin extracts the Ras family protein RalA from lipid bilayers by engagement with two membrane-targeting motifs.  <i> Chamberlain SG, Gohlke A, Shafiq A, Squires IJ, Owen D, Mott HR. </i> Proc Natl Acad Sci U S A, 2021","date":"2022-08-08T13:13:02.464Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"BMRB","id":"34608"},{"db":"PDB","id":"7NQC"}],"region_id":"DP02013r004","statement":[{"text":"Upon interaction with the RalA-HVR, the central helix of CaM undergoes extensive unfolding between residues Lys75 and Glu84. Melting of this helix to this extent, although uncommon in CaM structures, is consistent with previous observations that helical content decreases upon complex formation with the RalA HVR (23). This unfolded linker, coupled with the partial disorder of the HVR, results in the lack of fixed orientation of the N-lobe with respect to the C-lobe (Fig. 3A). There is a notable absence of interlobe NOEs, and residues of the central linker show only short-range, mostly intraresidue NOEs, which are not indicative of secondary structure.","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_P0DP23","date":"2018-08-22T19:00:36.000Z","acc":"P0DP23","name":"Calmodulin-1","length":149,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000000C1","genes":[{"name":{"value":"CALM1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"7925473","url":"http://www.ncbi.nlm.nih.gov/pubmed/7925473","alternativeUrl":"https://europepmc.org/abstract/MED/7925473"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:1442","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:1442"}}]},"synonyms":[{"value":"CALM"},{"value":"CAM"},{"value":"CAM1"}]}],"alphafold_very_low_content":0.020134228187919462,"disorder_content":0.06711409395973154,"disprot_consensus":{"full":[{"start":76,"end":85,"type":"T"}],"Structural state":[{"start":76,"end":85,"type":"D"}],"Structural transition":[{"start":76,"end":85,"type":"T"}],"Disorder function":[{"start":76,"end":85,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":74,"end":143},{"id":"PF00076","name":"RNA recognition motif","start":206,"end":274},{"id":"PF00076","name":"RNA recognition motif","start":655,"end":722},{"id":"PF11532","name":"HnRNP M nuclear localisation signal","start":41,"end":70}],"gene3D":[{"start":204,"end":279,"id":"3.30.70.330","name":"3.30.70.330"},{"start":651,"end":730,"id":"3.30.70.330","name":"3.30.70.330"},{"start":12,"end":158,"id":"3.30.70.330","name":"3.30.70.330"}]},"uniref50":"UniRef50_P52272","sequence":"MAAGVEAAAEVAATEIKMEEESGAPGVPSGNGAPGPKGEGERPAQNEKRKEKNIKRGGNRFEPYANPTKRYRAFITNIPFDVKWQSLKDLVKEKVGEVTYVELLMDAEGKSRGCAVVEFKMEESMKKAAEVLNKHSLSGRPLKVKEDPDGEHARRAMQKVMATTGGMGMGPGGPGMITIPPSILNNPNIPNEIIHALQAGRLGSTVFVANLDYKVGWKKLKEVFSMAGVVVRADILEDKDGKSRGIGTVTFEQSIEAVQAISMFNGQLLFDRPMHVKMDERALPKGDFFPPERPQQLPHGLGGIGMGLGPGGQPIDANHLNKGIGMGNIGPAGMGMEGIGFGINKMGGMEGPFGGGMENMGRFGSGMNMGRINEILSNALKRGEIIAKQGGGGGGGSVPGIERMGPGIDRLGGAGMERMGAGLGHGMDRVGSEIERMGLVMDRMGSVERMGSGIERMGPLGLDHMASSIERMGQTMERIGSGVERMGAGMGFGLERMAAPIDRVGQTIERMGSGVERMGPAIERMGLSMERMVPAGMGAGLERMGPVMDRMATGLERMGANNLERMGLERMGANSLERMGLERMGANSLERMGPAMGPALGAGIERMGLAMGGGGGASFDRAIEMERGNFGGSFAGSFGGAGGHAPGVARKACQIFVRNLPFDFTWKMLKDKFNECGHVLYADIKMENGKSKGCGVVKFESPEVAERACRMMNGMKLSGREIDVRIDRNA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P52272","disprot_id":"DP02015","ncbi_taxon_id":9606,"regions_counter":3,"creator":"msalva","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":70,"region_id":"DP02015r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure-based design of a pathway-specific nuclear import inhibitor. <i> Cansizoglu AE, Lee BJ, Zhang ZC, Fontoura BM, Chook YM. </i> Nat Struct Mol Biol, 2007","term_id":"IDPO:0000002","curator_id":"ahatos","start":41,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2OT8"}],"reference_id":"17435768","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":70,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure-based design of a pathway-specific nuclear import inhibitor. <i> Cansizoglu AE, Lee BJ, Zhang ZC, Fontoura BM, Chook YM. </i> Nat Struct Mol Biol, 2007","term_id":"IDPO:0000011","curator_id":"ahatos","start":41,"term_ontology":"IDPO","curator_name":"András Hatos","reference_id":"17435768","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02015r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":70,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure-based design of a pathway-specific nuclear import inhibitor. <i> Cansizoglu AE, Lee BJ, Zhang ZC, Fontoura BM, Chook YM. </i> Nat Struct Mol Biol, 2007","statement":[{"text":"both bPY-NLSs and hPY-NLSs bind Kapβ2 in an extended conformation, with structural conservation at the arginine and proline-tyrosine residues of their C-terminal R/K/Hx2–5PY motifs and at their N-terminal basic or hydrophobic motifs.","type":"Article"}],"term_id":"GO:0005515","curator_id":"ahatos","start":41,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"17435768","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2OT8"}],"region_id":"DP02015r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P52272","date":"2018-08-23T08:24:41.000Z","acc":"P52272","name":"Heterogeneous nuclear ribonucleoprotein M","length":730,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00004650C3","genes":[{"name":{"value":"HNRNPM"},"synonyms":[{"value":"HNRPM"},{"value":"NAGR1"}]}],"alphafold_very_low_content":0.584931506849315,"disorder_content":0.0410958904109589,"disprot_consensus":{"full":[{"start":41,"end":70,"type":"T"}],"Structural state":[{"start":41,"end":70,"type":"D"}],"Structural transition":[{"start":41,"end":70,"type":"T"}],"Molecular function":[{"start":41,"end":70,"type":"F"}]}},{"features":{"pfam":[],"gene3D":[{"start":1,"end":99,"id":"1.10.287.850","name":"HP0062-like domain"}]},"uniref50":"UniRef50_I6X486","sequence":"MSFVITNPEALTVAATEVRRIRDRAIQSDAQVAPMTTAVRPPAADLVSEKAATFLVEYARKYRQTIAAAAVVLEEFAHALTTGADKYATAEADNIKTFS","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"uniref90":"UniRef90_I6X486","disprot_id":"DP02017","ncbi_taxon_id":652616,"regions_counter":1,"creator":"msalva","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":99,"region_id":"DP02017r001","released":"2024_06","ec_id":"ECO:0006220","reference_html":"Structure of a PE-PPE-EspG complex from Mycobacterium tuberculosis reveals molecular specificity of ESX protein secretion. <i> Ekiert DC, Cox JS. </i> Proc Natl Acad Sci U S A, 2014","statement":[{"text":"This region lacks electron density, indicating it is disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":90,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"25275011","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2024-02-08T14:49:38.457Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4W4K"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A0H3LBN6"}]}],"released":"2018_11","uniref100":"UniRef100_I6X486","date":"2018-08-23T08:27:32.000Z","acc":"A0A0H3LBR3","name":"PE family protein","length":99,"organism":"Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman)","dataset":[],"UniParc":"UPI00000D6009","genes":[{"name":{"value":"PE25","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAL66464.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAL66464.1"}}]},"olnNames":[{"value":"ERDMAN_2675","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAL66464.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAL66464.1"}}]}]}],"alphafold_very_low_content":0.010101010101010102,"disorder_content":0.10101010101010101,"disprot_consensus":{"full":[{"start":90,"end":99,"type":"D"}],"Structural state":[{"start":90,"end":99,"type":"D"}]}},{"features":{"pfam":[],"gene3D":[{"start":395,"end":571,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"start":1,"end":109,"id":"1.10.533.10","name":"Death Domain, Fas"},{"start":110,"end":312,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":313,"end":392,"id":"1.10.8.490","name":"Ced-4 linker helical domain-like"}]},"uniref50":"UniRef50_P30429","sequence":"MLCEIECRALSTAHTRLIHDFEPRDALTYLEGKNIFTEDHSELISKMSTRLERIANFLRIYRRQASELGPLIDFFNYNNQSHLADFLEDYIDFAINEPDLLRPVVIAPQFSRQMLDRKLLLGNVPKQMTCYIREYHVDRVIKKLDEMCDLDSFFLFLHGRAGSGKSVIASQALSKSDQLIGINYDSIVWLKDSGTAPKSTFDLFTDILLMLARVVSDTDDSHSITDFINRVLSRSEDDLLNFPSVEHVTSVVLKRMICNALIDRPNTLFVFDDVVQEETIRWAQELRLRCLVTTRDVEISNAASQTCEFIEVTSLEIDECYDFLEAYGMPMPVGEKEEDVLNKTIELSSGNPATLMMFFKSCEPKTFEKMAQLNNKLESRGLVGVECITPYSYKSLAMALQRCVEVLSDEDRSALAFAVVMPPGVDIPVKLWSCVIPVDICSNEEEQLDDEVADRLKRLSKRGALLSGKRMPVLTFKIDHIIHMFLKHVVDAQTIANGISILEQRLLEIGNNNVSVPERHIPSHFQKFRRSSASEMYPKTTEETVIRPEDFPKFMQLHQKFYDSLKNFACC","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"uniref90":"UniRef90_P30429","disprot_id":"DP02025","ncbi_taxon_id":6239,"regions_counter":3,"creator":"spenadias","regions":[{"start":1,"end":108,"reference_id":"16208361","reference_source":"pmid","reference_html":"Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans. <i> Yan N, Chai J, Lee ES, Gu L, Liu Q, He J, Wu JW, Kokel D, Li H, Hao Q, Xue D, Shi Y. </i> Nature, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2A5Y"}],"region_id":"DP02025r003","statement":[{"text":"CED-4b exhibits a similar structure, except that its CARD domain is flexible and disordered in the crystals.","type":"Article"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-05-31T16:15:10.576Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P30429","date":"2018-08-23T08:30:02.000Z","acc":"P30429-1","name":"Cell death protein 4","length":571,"organism":"Caenorhabditis elegans","dataset":[],"UniParc":"UPI00001274C8","genes":[{"name":{"value":"ced-4"},"orfNames":[{"value":"C35D10.9"}]}],"alphafold_very_low_content":0.06830122591943957,"disorder_content":0.18914185639229422,"disprot_consensus":{"full":[{"start":1,"end":108,"type":"D"}],"Structural state":[{"start":1,"end":108,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00149","name":"Calcineurin-like phosphoesterase","start":202,"end":462},{"id":"PF19272","name":"Acid sphingomyelin phosphodiesterase C-terminal region","start":492,"end":600}],"gene3D":[{"start":378,"end":474,"id":"3.60.21.10","name":"3.60.21.10"}]},"uniref50":"UniRef50_P17405","sequence":"MPRYGASLRQSCPRSGREQGQDGTAGAPGLLWMGLVLALALALALALALSDSRVLWAPAEAHPLSPQGHPARLHRIVPRLRDVFGWGNLTCPICKGLFTAINLGLKKEPNVARVGSVAIKLCNLLKIAPPAVCQSIVHLFEDDMVEVWRRSVLSPSEACGLLLGSTCGHWDIFSSWNISLPTVPKPPPKPPSPPAPGAPVSRILFLTDLHWDHDYLEGTDPDCADPLCCRRGSGLPPASRPGAGYWGEYSKCDLPLRTLESLLSGLGPAGPFDMVYWTGDIPAHDVWHQTRQDQLRALTTVTALVRKFLGPVPVYPAVGNHESTPVNSFPPPFIEGNHSSRWLYEAMAKAWEPWLPAEALRTLRIGGFYALSPYPGLRLISLNMNFCSRENFWLLINSTDPAGQLQWLVGELQAAEDRGDKVHIIGHIPPGHCLKSWSWNYYRIVARYENTLAAQFFGHTHVDEFEVFYDEETLSRPLAVAFLAPSATTYIGLNPGYRVYQIDGNYSGSSHVVLDHETYILNLTQANIPGAIPHWQLLYRARETYGLPNTLPTAWHNLVYRMRGDMQLFQTFWFLYHKGHPPSEPCGTPCRLATLCAQLSARADSPALCRHLMPDGSLPEAQSLWPRPLFC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P17405","disprot_id":"DP02027","ncbi_taxon_id":9606,"regions_counter":9,"creator":"msalva","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":85,"region_id":"DP02027r006","start":49,"term_id":"IDPO:0000002","statement":[{"text":"Residues that are not visible in the structure are grey","type":"Figure"}],"curator_id":"ahatos","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"András Hatos","reference_id":"27725636","version":2,"reference_html":"Human acid sphingomyelinase structures provide insight to molecular basis of Niemann-Pick disease. <i> Zhou YF, Metcalf MC, Garman SC, Edmunds T, Qiu H, Wei RR. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5I81"}],"term_name":"disorder","curator_orcid":"0000-0001-9224-9820","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-31T13:31:44.519Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":631,"region_id":"DP02027r009","start":614,"term_id":"IDPO:0000002","curator_id":"vnugnes","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27725636","version":3,"reference_html":"Human acid sphingomyelinase structures provide insight to molecular basis of Niemann-Pick disease. <i> Zhou YF, Metcalf MC, Garman SC, Edmunds T, Qiu H, Wei RR. </i> Nat Commun, 2016","date":"2023-05-31T13:36:57.912Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5I81"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"}],"statement":[{"text":"The same residue range is visible in the olipudase alfa structure, suggesting ASM N and C termini are inherently disordered and flexible. The structure includes an N-terminal saposin domain (residues 84–167), a proline-rich linker (168–195), a catalytic metallophosphatase domain (196–538), and a helical C-terminal domain (539–611) (Fig. 1).","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_P17405","date":"2018-08-23T08:33:50.000Z","acc":"P17405","name":"Sphingomyelin phosphodiesterase","length":631,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI0000146EEE","genes":[{"name":{"value":"SMPD1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11120","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11120"}}]},"synonyms":[{"value":"ASM","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"25339683","url":"http://www.ncbi.nlm.nih.gov/pubmed/25339683","alternativeUrl":"https://europepmc.org/abstract/MED/25339683"}}]}]}],"alphafold_very_low_content":0.12836767036450078,"disorder_content":0.08716323296354993,"disprot_consensus":{"full":[{"start":49,"end":85,"type":"D"},{"start":614,"end":631,"type":"D"}],"Structural state":[{"start":49,"end":85,"type":"D"},{"start":614,"end":631,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00171","name":"Aldehyde dehydrogenase family","start":659,"end":1103},{"id":"PF01619","name":"Proline dehydrogenase","start":268,"end":569},{"id":"PF14850","name":"DNA-binding domain of Proline dehydrogenase","start":148,"end":259},{"id":"PF18327","name":"Proline utilization A proline dehydrogenase N-terminal domain","start":89,"end":136},{"id":"PF21775","name":"PutA, RHH domain","start":11,"end":43}],"gene3D":[{"start":87,"end":138,"id":"1.20.5.550","name":"Single Helix bin"},{"start":885,"end":1082,"id":"3.40.309.10","name":"Aldehyde Dehydrogenase; Chain A, domain 2"},{"start":655,"end":1112,"id":"3.40.605.10","name":"Aldehyde Dehydrogenase; Chain A, domain 1"},{"start":11,"end":52,"id":"1.10.1220.10","name":"Met repressor-like"},{"start":220,"end":610,"id":"3.20.20.220","name":"3.20.20.220"}]},"uniref50":"UniRef50_P09546","sequence":"MGTTTMGVKLDDATRERIKSAATRIDRTPHWLIKQAIFSYLEQLENSDTLPELPALLSGAANESDEAPTPAEEPHQPFLDFAEQILPQSVSRAAITAAYRRPETEAVSMLLEQARLPQPVAEQAHKLAYQLADKLRNQKNASGRAGMVQGLLQEFSLSSQEGVALMCLAEALLRIPDKATRDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGKLVSTHNEASLSRSLNRIIGKSGEPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEEKGFRYSYDMLGEAALTAADAQAYMVSYQQAIHAIGKASNGRGIYEGPGISIKLSALHPRYSRAQYDRVMEELYPRLKSLTLLARQYDIGINIDAEESDRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCPLVIDYLIDLATRSRRRLMIRLVKGAYWDSEIKRAQMDGLEGYPVYTRKVYTDVSYLACAKKLLAVPNLIYPQFATHNAHTLAAIYQLAGQNYYPGQYEFQCLHGMGEPLYEQVTGKVADGKLNRPCRIYAPVGTHETLLAYLVRRLLENGANTSFVNRIADTSLPLDELVADPVTAVEKLAQQEGQTGLPHPKIPLPRDLYGHGRDNSAGLDLANEHRLASLSSALLNSALQKWQALPMLEQPVAAGEMSPVINPAEPKDIVGYVREATPREVEQALESAVNNAPIWFATPPAERAAILHRAAVLMESQMQQLIGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRDDFANETHRPLGPVVCISPWNFPLAIFTGQIAAALAAGNSVLAKPAEQTPLIAAQGIAILLEAGVPPGVVQLLPGRGETVGAQLTGDDRVRGVMFTGSTEVATLLQRNIASRLDAQGRPIPLIAETGGMNAMIVDSSALTEQVVVDVLASAFDSAGQRCSALRVLCLQDEIADHTLKMLRGAMAECRMGNPGRLTTDIGPVIDSEAKANIERHIQTMRSKGRPVFQAVRENSEDAREWQSGTFVAPTLIELDDFAELQKEVFGPVLHVVRYNRNQLPELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTGPKAGGPLYLYRLLANRPESALAVTLARQDAKYPVDAQLKAALTQPLNALREWAANRPELQALCTQYGELAQAGTQRLLPGPTGERNTWTLLPRERVLCIADDEQDALTQLAAVLAVGSQVLWPDDALHRQLVKALPSAVSERIQLAKAENITAQPFDAVIFHGDSDQLRALCEAVAARDGTIVSVQGFARGESNILLERLYIERSLSVNTAAAGGNASLMTIG","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P09546","disprot_id":"DP02030","ncbi_taxon_id":83333,"regions_counter":2,"creator":"msalva","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":669,"region_id":"DP02030r001","released":"2024_06","ec_id":"ECO:0006220","reference_html":"Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors. <i> Zhang M, White TA, Schuermann JP, Baban BA, Becker DF, Tanner JJ. </i> Biochemistry, 2004","statement":[{"text":"Although residues 611–669 were not observed in any of the structures, the protein had not been degraded by proteolysis. Mass spectroscopy of a PutA86-669 crystal returned an unambiguous result of 66.8 kDa. Thus, residues 611–669 appear to be disordered in the PutA86-669 structures.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":611,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15449943","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2024-02-08T14:56:38.896Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1TIW"},{"db":"PDB","id":"1TJ2"},{"db":"PDB","id":"1TJ0"},{"db":"PDB","id":"1TJ1"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:175"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:107689"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:86079"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:643975"}]},{"start":185,"end":243,"reference_id":"15449943","reference_source":"pmid","reference_html":"Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors. <i> Zhang M, White TA, Schuermann JP, Baban BA, Becker DF, Tanner JJ. </i> Biochemistry, 2004","date":"2024-02-08T14:59:55.300Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02030r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:643975"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:175"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:107689"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:86079"}],"statement":[{"text":"The electron density was quite strong and unambiguous for residues 88–144, 162–184, and 244–610 in all four of the PutA86-669 structures.","type":"Methods"},{"text":" In full-length PutA, residues 188–241 are probably stabilized by interactions with a domain not present in the PutA86-669 construct, and, in the absence of these contacts, residues 188–241 are not properly folded.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"1TJ0"},{"db":"PDB","id":"1TJ2"},{"db":"PDB","id":"1TIW"},{"db":"PDB","id":"1TJ1"}]}],"released":"2018_11","uniref100":"UniRef100_P09546","date":"2018-08-23T08:34:37.000Z","acc":"P09546","name":"Bifunctional protein PutA","length":1320,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI000016EC4A","genes":[{"name":{"value":"putA"},"synonyms":[{"value":"poaA"}],"olnNames":[{"value":"b1014"},{"value":"JW0999"}]}],"alphafold_very_low_content":0.051515151515151514,"disorder_content":0.0893939393939394,"disprot_consensus":{"full":[{"start":185,"end":243,"type":"D"},{"start":611,"end":669,"type":"D"}],"Structural state":[{"start":185,"end":243,"type":"D"},{"start":611,"end":669,"type":"D"}]}},{"features":{"pfam":[{"id":"PF12550","name":"Transcriptional activator of glycolytic enzymes","start":843,"end":922},{"id":"PF16787","name":"Centromere DNA-binding protein complex CBF3 subunit, domain 2","start":185,"end":496},{"id":"PF21400","name":"Ndc10 N-terminal domain","start":28,"end":158}],"gene3D":[{"start":182,"end":537,"id":"1.10.443.20","name":"Centromere DNA-binding protein complex CBF3 subunit, domain 2"},{"start":44,"end":168,"id":"1.10.150.130","name":"1.10.150.130"}]},"uniref50":"UniRef50_P32504","sequence":"MRSSILFLLKLMKIMDVQQQQEAMSSEDRFQELVDSLKPRTAHQYKTYYTKYIQWCQLNQIIPTPEDNSVNSVPYKDLPISAELIHWFLLDTLITDDKPGEKREETEDLDEEEENSFKIATLKKIIGSLNFLSKLCKVHENPNANIDTKYLESVTKLHTHWIDSQKAITTNETNNTNTQVLCPPLLKVSLNLWNPETNHLSEKFFKTCSEKLRFLVDFQLRSYLNLSFEERSKIRFGSLKLGKRDRDAIIYHKVTHSAEKKDTPGHHQLLALLPQDCPFICPQTTLAAYLYLRFYGIPSVSKGDGFPNLNADENGSLLQDIPILRGKSLTTYPREETFSNYYTTVFRYCHLPYKRREYFNKCNLVYPTWDEDTFRTFFNEENHGNWLEQPEAFAFPDKIPFDFKKIMNFKSPYTSYSTNAKKDPFPPPKDLLVQIFPEIDEYKRHDYEGLSQNSRDFLDLMEVLRERFLSNLPWIYKFFPNHDIFQDPIFGNSDFQSYFNDKTIHSKGSPILSFDILPGFNKIYKNKTNFYSLLIERPSQLTFASSHNPDTHPTQKQESEGPLQMSQLDTTQLNELLKQQSFEYVQFQTLSNFQILLSVFNKIFEKLEMKKSSRGYILHQLNLFKITLDERIKKSKIDDADKFIRDNQPIKKEENIVNEDGPNTSRRTKRPKQIRLLSIADSSDESSTEDSNVFKKDGESIEDGAYGENEDENDSEMQEQLKSMINELINSKISTFLRDQMDQFELKINALLDKILEEKVTRIIEQKLGSHTGKFSTLKRPQLYMTEEHNVGFDMEVPKKLRTSGKYAETVKDNDDHQAMSTTASPSPEQDQEAKSYTDEQEFMLDKSIDSIEGIILEWFTPNAKYANQCVHSMNKSGNKSWRANCEALYKERKSIVEFYIYLVNHESLDRYKAVDICEKLRDQNEGSFSRLAKFLRKWRHDHQNSFDGLLVYLSN","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P32504","disprot_id":"DP02033","ncbi_taxon_id":559292,"regions_counter":8,"creator":"jlecle","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":43,"region_id":"DP02033r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of yeast kinetochore Ndc10 DNA-binding domain reveals unexpected evolutionary relationship to tyrosine recombinases. <i> Perriches T, Singleton MR. </i> J Biol Chem, 2012","statement":[{"text":"No clear electron density was seen for residues 1–43 or 538–551, and loops between residues 65–72, 97–108, 168–182, 257–264, and 414–423 were also disordered and not included in the final model.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jlecle","start":1,"term_ontology":"IDPO","curator_name":"Jeremy Y Leclercq","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0372-3277","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4ACO"}],"reference_id":"22215672","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":108,"region_id":"DP02033r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of yeast kinetochore Ndc10 DNA-binding domain reveals unexpected evolutionary relationship to tyrosine recombinases. <i> Perriches T, Singleton MR. </i> J Biol Chem, 2012","statement":[{"text":"No clear electron density was seen for residues 1–43 or 538–551, and loops between residues 65–72, 97–108, 168–182, 257–264, and 414–423 were also disordered and not included in the final model.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jlecle","start":97,"term_ontology":"IDPO","curator_name":"Jeremy Y Leclercq","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0372-3277","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4ACO"}],"reference_id":"22215672","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":182,"region_id":"DP02033r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of yeast kinetochore Ndc10 DNA-binding domain reveals unexpected evolutionary relationship to tyrosine recombinases. <i> Perriches T, Singleton MR. </i> J Biol Chem, 2012","statement":[{"text":"No clear electron density was seen for residues 1–43 or 538–551, and loops between residues 65–72, 97–108, 168–182, 257–264, and 414–423 were also disordered and not included in the final model.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jlecle","start":168,"term_ontology":"IDPO","curator_name":"Jeremy Y Leclercq","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0372-3277","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4ACO"}],"reference_id":"22215672","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":423,"region_id":"DP02033r004","reference_id":"22215672","start":414,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"No clear electron density was seen for residues 1–43 or 538–551, and loops between residues 65–72, 97–108, 168–182, 257–264, and 414–423 were also disordered and not included in the final model.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structure of yeast kinetochore Ndc10 DNA-binding domain reveals unexpected evolutionary relationship to tyrosine recombinases. <i> Perriches T, Singleton MR. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4ACO"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":551,"region_id":"DP02033r005","reference_id":"22215672","start":538,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"No clear electron density was seen for residues 1–43 or 538–551, and loops between residues 65–72, 97–108, 168–182, 257–264, and 414–423 were also disordered and not included in the final model.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structure of yeast kinetochore Ndc10 DNA-binding domain reveals unexpected evolutionary relationship to tyrosine recombinases. <i> Perriches T, Singleton MR. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4ACO"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":956,"region_id":"DP02033r006","reference_id":"22215672","start":538,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Residues 538-956 are unobserved in the crystal structure of yeast Ndc10.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structure of yeast kinetochore Ndc10 DNA-binding domain reveals unexpected evolutionary relationship to tyrosine recombinases. <i> Perriches T, Singleton MR. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4ACO"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":956,"region_id":"DP02033r007","reference_id":"22215672","start":552,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"During purifications of the full-length protein, we identified a 64.6-kDa proteolytically derived fragment of Ndc10, which was determined to contain residues 1–551 of the N-terminal.","type":"Results"},{"text":"Residues 538-956 are unobserved in the crystal structure of yeast Ndc10.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cleavage assay evidence used in manual assertion","version":3,"reference_html":"Structure of yeast kinetochore Ndc10 DNA-binding domain reveals unexpected evolutionary relationship to tyrosine recombinases. <i> Perriches T, Singleton MR. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","cross_refs":[{"db":"PDB","id":"4ACO"}],"term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":956,"region_id":"DP02033r008","reference_id":"22215672","start":1,"term_id":"GO:0003677","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Both the full-length protein and this fragment were found to be competent for DNA binding against a random (non-centromeric) DNA sequence (Fig. 1b).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"gel electrophoresis evidence used in manual assertion","version":4,"reference_html":"Structure of yeast kinetochore Ndc10 DNA-binding domain reveals unexpected evolutionary relationship to tyrosine recombinases. <i> Perriches T, Singleton MR. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007688","cross_refs":[{"db":"PDB","id":"4ACO"}],"term_name":"DNA binding","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P32504","date":"2018-08-23T13:55:33.000Z","acc":"P32504","name":"Centromere DNA-binding protein complex CBF3 subunit A","length":956,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000127151","genes":[{"name":{"value":"CBF2"},"synonyms":[{"value":"CBF3A"},{"value":"CEP2"},{"value":"CTF14"},{"value":"NDC10"}],"olnNames":[{"value":"YGR140W"}]}],"alphafold_very_low_content":0.22071129707112971,"disorder_content":0.5219665271966527,"disprot_consensus":{"full":[{"start":1,"end":43,"type":"D"},{"start":44,"end":96,"type":"F"},{"start":97,"end":108,"type":"D"},{"start":109,"end":167,"type":"F"},{"start":168,"end":182,"type":"D"},{"start":183,"end":413,"type":"F"},{"start":414,"end":423,"type":"D"},{"start":424,"end":537,"type":"F"},{"start":538,"end":956,"type":"D"}],"Structural state":[{"start":1,"end":43,"type":"D"},{"start":97,"end":108,"type":"D"},{"start":168,"end":182,"type":"D"},{"start":414,"end":423,"type":"D"},{"start":538,"end":956,"type":"D"}],"Molecular function":[{"start":1,"end":956,"type":"F"}]}},{"features":{"pfam":[{"id":"PF15511","name":"Centromere kinetochore component CENP-T histone fold","start":44,"end":96}],"gene3D":[{"start":2,"end":103,"id":"1.10.20.10","name":"Histone, subunit A"}]},"uniref50":"UniRef50_P62805","sequence":"MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P62805","disprot_id":"DP02034","ncbi_taxon_id":9606,"regions_counter":1,"creator":"thorvath","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":25,"region_id":"DP02034r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Structure and Dynamics in the Nucleosome Revealed by Solid-State NMR. <i> Shi X, Prasanna C, Nagashima T, Yamazaki T, Pervushin K, Nordenskiöld L. </i> Angew Chem Int Ed Engl, 2018","statement":[{"text":"The tail region of hH4 (S1–D24) is not observable in all dipolar‐based experiments due to significant scaling down of the relevant dipolar couplings caused by high flexibility.","type":"Introduction"},{"text":"However, the N-terminal tail in the array retains structural flexibility as the cross-peaks corresponding to the residues 1–25 are absent in the cross-polarization-based spectra.","type":"Article"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"29905032","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2023-05-08T21:02:10.504Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"BMRB","id":"27457"}],"curator_orcid":"0000-0001-8399-7907"}],"released":"2018_11","uniref100":"UniRef100_P62805","date":"2018-08-23T14:51:11.000Z","acc":"P62805","name":"Histone H4","length":103,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI0000027039","genes":[{"name":{"value":"H4C1"},"synonyms":[{"value":"H4/A"},{"value":"H4FA"},{"value":"HIST1H4A"}]},{"name":{"value":"H4C2"},"synonyms":[{"value":"H4/I"},{"value":"H4FI"},{"value":"HIST1H4B"}]},{"name":{"value":"H4C3"},"synonyms":[{"value":"H4/G"},{"value":"H4FG"},{"value":"HIST1H4C"}]},{"name":{"value":"H4C4"},"synonyms":[{"value":"H4/B"},{"value":"H4FB"},{"value":"HIST1H4D"}]},{"name":{"value":"H4C5"},"synonyms":[{"value":"H4/J"},{"value":"H4FJ"},{"value":"HIST1H4E"}]},{"name":{"value":"H4C6"},"synonyms":[{"value":"H4/C"},{"value":"H4FC"},{"value":"HIST1H4F"}]},{"name":{"value":"H4C8"},"synonyms":[{"value":"H4/H"},{"value":"H4FH"},{"value":"HIST1H4H"}]},{"name":{"value":"H4C9"},"synonyms":[{"value":"H4/M"},{"value":"H4FM"},{"value":"HIST1H4I"}]},{"name":{"value":"H4C11"},"synonyms":[{"value":"H4/E"},{"value":"H4FE"},{"value":"HIST1H4J"}]},{"name":{"value":"H4C12"},"synonyms":[{"value":"H4/D"},{"value":"H4FD"},{"value":"HIST1H4K"}]},{"name":{"value":"H4C13"},"synonyms":[{"value":"H4/K"},{"value":"H4FK"},{"value":"HIST1H4L"}]},{"name":{"value":"H4C14"},"synonyms":[{"value":"H4/N"},{"value":"H4F2"},{"value":"H4FN"},{"value":"HIST2H4"},{"value":"HIST2H4A"}]},{"name":{"value":"H4C15"},"synonyms":[{"value":"H4/O"},{"value":"H4FO"},{"value":"HIST2H4B"}]},{"name":{"value":"H4-16"},"synonyms":[{"value":"HIST4H4"}]}],"alphafold_very_low_content":0.009708737864077669,"disorder_content":0.24271844660194175,"disprot_consensus":{"full":[{"start":1,"end":25,"type":"D"}],"Structural state":[{"start":1,"end":25,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00579","name":"tRNA synthetases class I (W and Y)","start":30,"end":324},{"id":"PF22421","name":"Tyrosine--tRNA ligase SYY-like C-terminal domain","start":335,"end":417}],"gene3D":[{"start":3,"end":223,"id":"3.40.50.620","name":"HUPs"},{"start":327,"end":420,"id":"3.10.290.10","name":"RNA-binding S4 domain"},{"start":224,"end":326,"id":"1.10.240.10","name":"Tyrosyl-Transfer RNA Synthetase"}]},"uniref50":"UniRef50_P0DM33","sequence":"MTNVLIEDLKWRGLIYQQTDEQGIEDLLNKEQVTLYCGADPTADSLHIGHLLPFLTLRRFQEHGHRPIVLIGGGTGMIGDPSGKSEERVLQTEEQVDKNIEGISKQMHNIFEFGTDHGAVLVNNRDWLGQISLISFLRDYGKHVGVNYMLGKDSIQSRLEHGISYTEFTYTILQAIDFGHLNRELNCKIQVGGSDQWGNITSGIELMRRMYGQTDAYGLTIPLVTKSDGKKFGKSESGAVWLDAEKTSPYEFYQFWINQSDEDVIKFLKYFTFLGKEEIDRLEQSKNEAPHLREAQKTLAEEVTKFIHGEDALNDAIRISQALFSGDLKSLSAKELKDGFKDVPQVTLSNDTTNIVEVLIETGISPSKRQAREDVNNGAIYINGERQQDVNYALAPEDKIDGEFTIIRRGKKKYFMVNYQ","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Staphylococcaceae","Staphylococcus"],"uniref90":"UniRef90_Q5HF45","disprot_id":"DP02035","ncbi_taxon_id":426430,"regions_counter":1,"creator":"jlecle","regions":[{"region_id":"DP02035r001","ec_ontology":"ECO","end":420,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":323,"version":3,"statement":[{"text":"The N-terminal α/β domain (0–220) and the α-helical domain (248–323) are connected via a linker peptide (221–247),while the C-terminal domain (324–421) is disordered in the crystal (Fig. 2B).","type":"Results"}],"term_name":"disorder","reference_html":"Crystal structure of Staphylococcus aureus tyrosyl-tRNA synthetase in complex with a class of potent and specific inhibitors. <i> Qiu X, Janson CA, Smith WW, Green SM, McDevitt P, Johanson K, Carter P, Hibbs M, Lewis C, Chalker A, Fosberry A, Lalonde J, Berge J, Brown P, Houge-Frydrych CS, Jarvest RL. </i> Protein Sci, 2001","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"11567092","date":"2024-02-07T17:43:06.945Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1JII"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:446497"}]}],"released":"2018_11","uniref100":"UniRef100_A7X3G2","date":"2018-08-23T15:16:27.000Z","acc":"A6QHR2","name":"Tyrosine--tRNA ligase","length":420,"organism":"Staphylococcus aureus (strain Newman)","dataset":["RNA-binding proteins"],"UniParc":"UPI000002E8ED","genes":[{"name":{"value":"tyrS","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_02006","url":"https://hamap.expasy.org/unirule/MF_02006"}}]},"olnNames":[{"value":"NWMN_1622"}]}],"alphafold_very_low_content":0,"disorder_content":0.23333333333333334,"disprot_consensus":{"full":[{"start":323,"end":420,"type":"D"}],"Structural state":[{"start":323,"end":420,"type":"D"}]}},{"acc":"Q98325","sequence":"MSDSKEVPSLPFLRHLLEELDSHEDSLLLFLCHDAAPGCTTVTQALCSLSQQRKLTLAALVEMLYVLQRMDLLKSRFGLSKEGAEQLLGTSFLTRYRKLMVCVGEELDSSELRALRLFACNLNPSLSTALSESSRFVELVLALENVGLVSPSSVSVLADMLRTLRRLDLCQQLVEYEQQEQARYRYCYAASPSLPVRTLRRGHGASEHEQLCMPVQESSDSPELLRTPVQESSSDSPEQTT","creator":"jlecle","dataset":["Viral proteins"],"date":"2018-08-23T16:05:51.000Z","disprot_id":"DP02042","features":{"pfam":[{"id":"PF01335","name":"Death effector domain","start":96,"end":179}],"gene3D":[{"start":1,"end":90,"id":"1.10.533.10","name":"Death Domain, Fas","_id":"685af523b4ac24d5329d9351"},{"start":91,"end":193,"id":"1.10.533.10","name":"Death Domain, Fas","_id":"685af523b4ac24d5329d9352"}]},"genes":[{"synonyms":[],"olnNames":[{"value":"MC159L","evidences":[],"_id":"685af523b4ac24d5329d9387"}],"orfNames":[{"value":"H-H2.2","evidences":[],"_id":"685af523b4ac24d5329d9386"}],"_id":"685af523b4ac24d5329d9385"}],"length":241,"name":"Viral CASP8 and FADD-like apoptosis regulator","ncbi_taxon_id":10280,"organism":"Molluscum contagiosum virus subtype 1","regions_counter":12,"released":"2018_11","taxonomy":["Viruses","Varidnaviria","Bamfordvirae","Nucleocytoviricota","Pokkesviricetes","Chitovirales","Poxviridae","Chordopoxvirinae","Molluscipoxvirus"],"UniParc":"UPI000003046F","uniref100":"UniRef100_Q98325","uniref50":"UniRef50_Q98325","uniref90":"UniRef90_Q98325","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2BBZ","_id":"685af523b4ac24d5329d9358"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":192,"end":241,"interaction_partner":[],"reference_html":"Crystal structure of MC159 reveals molecular mechanism of DISC assembly and FLIP inhibition. <i> Yang JK, Wang L, Zheng L, Wan F, Ahmed M, Lenardo MJ, Wu H. </i> Mol Cell, 2005","reference_id":"16364918","region_id":"DP02042r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The structure of full-length MC159 was first solved at 3.8Å resolution by single-wavelength anomalous diffraction and fourfold non-crystallographic symmetry averaging (Figure 2A). It revealed that more than fifty residues at the C-terminal tail of MC159 were disordered in the crystal.","_id":"685af523b4ac24d5329d9359"},{"type":"Methods","text":"The structure revealed that a large segment of the C-terminal tail (residues 188–241) is disordered in the crystal. This C-terminal tail is not important for the function of MC159 (Garvey et al., 2002a).","_id":"685af523b4ac24d5329d935a"},{"type":"Curator statement","text":"The missing electron density region starts at residue Pro192.","_id":"685af523b4ac24d5329d935b"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T14:10:38.992Z","_id":"685af523b4ac24d5329d935c"},"version":1,"_id":"685af523b4ac24d5329d9357","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006030","ec_name":"co-immunoprecipitation evidence used in manual assertion","ec_ontology":"ECO","start":214,"end":218,"interaction_partner":[{"db":"UniProt","id":"Q13114","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d935e"}],"reference_html":"The TRAF3-binding site of human molluscipox virus FLIP molecule MC159 is critical for its capacity to inhibit Fas-induced apoptosis. <i> Thurau M, Everett H, Tapernoux M, Tschopp J, Thome M. </i> Cell Death Differ, 2006","reference_id":"16410799","region_id":"DP02042r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"To address the relevance of the TRAF consensus-binding motif for the observed interactions, we generated MC159 expression constructs that were either doubly mutated in the first two identical TRAF-binding motifs (MC159 DM) or C-terminally deleted to remove all three potential binding sites (MC159 Δ) (Figure 2a). Co-immunoprecipitation experiments using these MC159 FLIP mutants revealed that the first two TRAF-binding motifs were specifically required for TRAF3 binding, while binding of TRAF1 and TRAF2 did not appear to be affected by the mutation or deletion of these TRAF-binding sites under conditions of overexpression (Figure 2c).","_id":"685af523b4ac24d5329d935f"},{"type":"Curator statement","text":"Region corresponding to the first PVQES TRAF-binding motif.","_id":"685af523b4ac24d5329d9360"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T14:10:42.441Z","_id":"685af523b4ac24d5329d9361"},"version":1,"_id":"685af523b4ac24d5329d935d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006030","ec_name":"co-immunoprecipitation evidence used in manual assertion","ec_ontology":"ECO","start":228,"end":232,"interaction_partner":[{"db":"UniProt","id":"Q13114","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9363"}],"reference_html":"The TRAF3-binding site of human molluscipox virus FLIP molecule MC159 is critical for its capacity to inhibit Fas-induced apoptosis. <i> Thurau M, Everett H, Tapernoux M, Tschopp J, Thome M. </i> Cell Death Differ, 2006","reference_id":"16410799","region_id":"DP02042r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"To address the relevance of the TRAF consensus-binding motif for the observed interactions, we generated MC159 expression constructs that were either doubly mutated in the first two identical TRAF-binding motifs (MC159 DM) or C-terminally deleted to remove all three potential binding sites (MC159 Δ) (Figure 2a). Co-immunoprecipitation experiments using these MC159 FLIP mutants revealed that the first two TRAF-binding motifs were specifically required for TRAF3 binding, while binding of TRAF1 and TRAF2 did not appear to be affected by the mutation or deletion of these TRAF-binding sites under conditions of overexpression (Figure 2c).","_id":"685af523b4ac24d5329d9364"},{"type":"Curator statement","text":"Region corresponding to the second PVQES TRAF-binding motif.","_id":"685af523b4ac24d5329d9365"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T14:10:41.324Z","_id":"685af523b4ac24d5329d9366"},"version":1,"_id":"685af523b4ac24d5329d9362","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IMP","ec_id":"ECO:0001175","ec_name":"deletion mutation phenotypic evidence used in manual assertion","ec_ontology":"ECO","start":211,"end":241,"interaction_partner":[{"db":"UniProt","id":"Q13114","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9372"}],"reference_html":"The TRAF3-binding site of human molluscipox virus FLIP molecule MC159 is critical for its capacity to inhibit Fas-induced apoptosis. <i> Thurau M, Everett H, Tapernoux M, Tschopp J, Thome M. </i> Cell Death Differ, 2006","reference_id":"16410799","region_id":"DP02042r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The double mutant (DM) and the C-terminally deleted form of MC159 FLIP (Δ) failed to bind to TRAF3, as was previously observed under conditions of overexpression in 293T cells (Figure 2c). TRAF2 still bound to both mutants, although at reduced levels, possibly because TRAF3 contributed to optimal recruitment and/or stabilization of endogenous TRAF2 in the complex.","_id":"685af523b4ac24d5329d9373"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T14:10:40.243Z","_id":"685af523b4ac24d5329d9374"},"version":1,"_id":"685af523b4ac24d5329d9371","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0005580","ec_name":"flow cytometry evidence used in manual assertion","ec_ontology":"ECO","start":228,"end":232,"interaction_partner":[],"reference_html":"The TRAF3-binding site of human molluscipox virus FLIP molecule MC159 is critical for its capacity to inhibit Fas-induced apoptosis. <i> Thurau M, Everett H, Tapernoux M, Tschopp J, Thome M. </i> Cell Death Differ, 2006","reference_id":"16410799","region_id":"DP02042r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The percentage of cells that had internalized the receptor correlated well with the percentage of annexin V-positive, apoptotic cells in the same experiments, suggesting that the TRAF3-binding-dependent capacity of MC159 FLIP to inhibit receptor internalization accounted for its antiapoptotic effect (Figure 5c). Together, these data suggest that the intact TRAF3-binding site of MC159 FLIP is required to fully prevent ligand-induced Fas internalization and apoptosis.","_id":"685af523b4ac24d5329d9380"}],"states_connection":[],"term_comment":"","term_def":"\"Any process that stops, prevents or reduces the frequency, rate or extent of apoptotic signaling pathway.\" [GOC:mtg_apoptosis]","term_id":"GO:2001234","term_is_binding":false,"term_is_obsolete":false,"term_name":"negative regulation of apoptotic signaling pathway","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T14:10:44.815Z","_id":"685af523b4ac24d5329d9381"},"version":1,"_id":"685af523b4ac24d5329d937f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0005580","ec_name":"flow cytometry evidence used in manual assertion","ec_ontology":"ECO","start":214,"end":218,"interaction_partner":[],"reference_html":"The TRAF3-binding site of human molluscipox virus FLIP molecule MC159 is critical for its capacity to inhibit Fas-induced apoptosis. <i> Thurau M, Everett H, Tapernoux M, Tschopp J, Thome M. </i> Cell Death Differ, 2006","reference_id":"16410799","region_id":"DP02042r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The percentage of cells that had internalized the receptor correlated well with the percentage of annexin V-positive, apoptotic cells in the same experiments, suggesting that the TRAF3-binding-dependent capacity of MC159 FLIP to inhibit receptor internalization accounted for its antiapoptotic effect (Figure 5c). Together, these data suggest that the intact TRAF3-binding site of MC159 FLIP is required to fully prevent ligand-induced Fas internalization and apoptosis.","_id":"685af523b4ac24d5329d9383"}],"states_connection":[],"term_comment":"","term_def":"\"Any process that stops, prevents or reduces the frequency, rate or extent of apoptotic signaling pathway.\" [GOC:mtg_apoptosis]","term_id":"GO:2001234","term_is_binding":false,"term_is_obsolete":false,"term_name":"negative regulation of apoptotic signaling pathway","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-27T14:10:43.709Z","_id":"685af523b4ac24d5329d9384"},"version":1,"_id":"685af523b4ac24d5329d9382","reference_source":"pmid"}],"__v":0,"disorder_content":0.2074688796680498,"disprot_consensus":{"full":[{"start":192,"end":241,"type":"D"}],"Structural state":[{"start":192,"end":241,"type":"D"}],"Molecular function":[{"start":211,"end":241,"type":"F"}],"Biological process":[{"start":214,"end":218,"type":"F"},{"start":228,"end":232,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00009","name":"Elongation factor Tu GTP binding domain","start":176,"end":397},{"id":"PF08938","name":"HBS1 N-terminus","start":13,"end":81},{"id":"PF22594","name":"GTP-eEF1A C-terminal domain-like","start":497,"end":589}],"gene3D":[{"start":240,"end":396,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":397,"end":490,"id":"2.40.30.10","name":"Translation factors"},{"start":491,"end":592,"id":"2.40.30.10","name":"Translation factors"}]},"uniref50":"UniRef50_O74774","sequence":"MSRHRDVKNLDLDDYELDEEPGEEELTEEQEEEFRSAVATVRETLLGVPISEKEIADTVWYYYFDVEKSVNYLLQKASSKAGAKEKQNTDSQKEKKQNKSKEALADAKDPLDESSNGIKNLSLNKNDEPAFQTNGEVKMKNSSESDNQPEKKKIKKQNPTDLVSVPEIFEQSNPKPVVHLVVTGHVDSGKSTMLGRIMFELGEINSRSMQKLHNEAANSGKGSFSYAWLLDTTEEERARGVTMDVASTTFESDKKIYEIGDAPGHRDFISGMIAGASSADFAVLVVDSSQNNFERGFLENGQTREHAYLLRALGISEIVVSVNKLDLMSWSEDRFQEIKNIVSDFLIKMVGFKTSNVHFVPISAISGTNLIQKDSSDLYKWYKGPTLLSALDQLVPPEKPYRKPLRLSIDDVYRSPRSVTVTGRVEAGNVQVNQVLYDVSSQEDAYVKNVIRNSDPSSTWAVAGDTVTLQLADIEVNQLRPGDILSNYENPVRRVRSFVAEIQTFDIHGPILSGSTLVLHLGRTVTSVSLKIVTVNNKRSRHIASRKRALVRISFLDGLFPLCLAEECPALGRFILRRSGDTVAAGIVKELC","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"uniref90":"UniRef90_O74774","disprot_id":"DP02049","ncbi_taxon_id":284812,"regions_counter":2,"creator":"jlecle","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":155,"region_id":"DP02049r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the Dom34-Hbs1 complex and implications for no-go decay. <i> Chen L, Muhlrad D, Hauryliuk V, Cheng Z, Lim MK, Shyp V, Parker R, Song H. </i> Nat Struct Mol Biol, 2010","statement":[{"text":"three regions (residues 1–155, 204–259 and 274–282) in Hbs1 are not visible in the electron density map and are assumed to be disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jlecle","start":1,"term_ontology":"IDPO","curator_name":"Jeremy Y Leclercq","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0372-3277","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3MCA"}],"reference_id":"20890290","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":259,"region_id":"DP02049r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of the Dom34-Hbs1 complex and implications for no-go decay. <i> Chen L, Muhlrad D, Hauryliuk V, Cheng Z, Lim MK, Shyp V, Parker R, Song H. </i> Nat Struct Mol Biol, 2010","statement":[{"text":"three regions (residues 1–155, 204–259 and 274–282) in Hbs1 are not visible in the electron density map and are assumed to be disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jlecle","start":204,"term_ontology":"IDPO","curator_name":"Jeremy Y Leclercq","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0372-3277","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3MCA"}],"reference_id":"20890290","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_O74774","date":"2018-08-23T16:33:10.000Z","acc":"O74774","name":"Elongation factor 1 alpha-like protein","length":592,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","dataset":[],"UniParc":"UPI000006C873","genes":[{"name":{"value":"hbs1","evidences":[{"code":"ECO:0000250","source":{"name":"UniProtKB","id":"P32769","url":"https://www.uniprot.org/uniprot/P32769"}}]},"orfNames":[{"value":"SPBC25B2.01"},{"value":"SPBC2G5.08"}]}],"alphafold_very_low_content":0.15878378378378377,"disorder_content":0.3564189189189189,"disprot_consensus":{"full":[{"start":1,"end":155,"type":"D"},{"start":204,"end":259,"type":"D"}],"Structural state":[{"start":1,"end":155,"type":"D"},{"start":204,"end":259,"type":"D"}]}},{"features":{"pfam":[{"id":"PF04189","name":"Gcd10p family","start":6,"end":329}]},"uniref50":"UniRef50_P41814","sequence":"MNALTTIDFNQHVIVRLPSKNYKIVELKPNTSVSLGKFGAFEVNDIIGYPFGLTFEIYYDGEEVSSDENRDSKPKNKIPIGKVRLLSQEIKDVNNDKDDGQSEPPLSIKEKSVSLELSSIDSSATNQNLVNMGSKAQELTVEEIEKMKQESLSSKEIIDKIIKSHKSFHNKTVYSQEKYVNRKKQKFAKYFTVEYLSSSNLLQFLIDKGDIQRVLDMSQESMGMLLNLANIQSEGNYLCMDETGGLLVYFLLERMFGGDNESKSKGKVIVIHENEHANLDLLKFANYSEKFIKEHVHTISLLDFFEPPTLQEIQSRFTPLPKEEARALKGGKKNSYYRKLRWYNTQWQILELTGEFLYDGLVMATTLHLPTLVPKLAEKIHGSRPIVCYGQFKETLLELAHTLYSDLRFLAPSILETRCRPYQSIRGKLHPLMTMKGGGGYLMWCHRVIPAPEPVSENATAADSSEKLAEHGAKKQKI","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P41814","disprot_id":"DP02050","ncbi_taxon_id":559292,"regions_counter":3,"creator":"jlecle","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":78,"region_id":"DP02050r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the two-subunit tRNA m(1)A58 methyltransferase TRM6-TRM61 from Saccharomyces cerevisiae. <i> Wang M, Zhu Y, Wang C, Fan X, Jiang X, Ebrahimi M, Qiao Z, Niu L, Teng M, Li X. </i> Sci Rep, 2016","statement":[{"text":"TRM6 contains 478 amino acid residues, comprising an N-terminal β-barrel domain (residues 1–196) and a C-terminal Rossmann fold domain (residues 197–451). Due to the flexibility, residues 61–78, residues 88–188, residues 322–325 and residues 453–478 are not observed.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jlecle","start":61,"term_ontology":"IDPO","curator_name":"Jeremy Y Leclercq","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0372-3277","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5EQJ"}],"reference_id":"27582183","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":188,"region_id":"DP02050r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the two-subunit tRNA m(1)A58 methyltransferase TRM6-TRM61 from Saccharomyces cerevisiae. <i> Wang M, Zhu Y, Wang C, Fan X, Jiang X, Ebrahimi M, Qiao Z, Niu L, Teng M, Li X. </i> Sci Rep, 2016","statement":[{"text":"TRM6 contains 478 amino acid residues, comprising an N-terminal β-barrel domain (residues 1–196) and a C-terminal Rossmann fold domain (residues 197–451). Due to the flexibility, residues 61–78, residues 88–188, residues 322–325 and residues 453–478 are not observed.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jlecle","start":88,"term_ontology":"IDPO","curator_name":"Jeremy Y Leclercq","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0372-3277","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5EQJ"}],"reference_id":"27582183","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":478,"region_id":"DP02050r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the two-subunit tRNA m(1)A58 methyltransferase TRM6-TRM61 from Saccharomyces cerevisiae. <i> Wang M, Zhu Y, Wang C, Fan X, Jiang X, Ebrahimi M, Qiao Z, Niu L, Teng M, Li X. </i> Sci Rep, 2016","statement":[{"text":"TRM6 contains 478 amino acid residues, comprising an N-terminal β-barrel domain (residues 1–196) and a C-terminal Rossmann fold domain (residues 197–451). Due to the flexibility, residues 61–78, residues 88–188, residues 322–325 and residues 453–478 are not observed.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jlecle","start":453,"term_ontology":"IDPO","curator_name":"Jeremy Y Leclercq","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0372-3277","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5EQJ"}],"reference_id":"27582183","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P41814","date":"2018-08-23T16:47:16.000Z","acc":"P41814","name":"tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6","length":478,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000012D323","genes":[{"name":{"value":"GCD10"},"synonyms":[{"value":"TIF33"},{"value":"TRM6"}],"orfNames":[{"value":"N2422"}],"olnNames":[{"value":"YNL062C"}]}],"alphafold_very_low_content":0.1087866108786611,"disorder_content":0.303347280334728,"disprot_consensus":{"full":[{"start":61,"end":78,"type":"D"},{"start":88,"end":188,"type":"D"},{"start":453,"end":478,"type":"D"}],"Structural state":[{"start":61,"end":78,"type":"D"},{"start":88,"end":188,"type":"D"},{"start":453,"end":478,"type":"D"}]}},{"acc":"P14335","sequence":"MSKKPGGPGKSRAVNMLKRGMPRVLSLTGLKRAMLSLIDGRGPTRFVLALLAFFRFTAIAPTRAVLDRWRSVNKQTAMKHLLSFKKELGTLTSAINRRSSKQKKRGGKTGIAFMIGLIAGVGAVTLSNFQGKVMMTVNATDVTDIITIPPAAGKNLCIVRAMDVGHMCDDTITYECPVLSAGNDPEDIDCWCTKLAVYVRYGRCTKTRHSRRSRRSLTVQTHGESTLSNKKGAWMDSTKATRYLVKTESWILRNPGYALVAAVIGWMLGSNTMQRVVFAVLLLLVAPAYSFNCLGMSNRDFLEGVSGATWVDLVLEGDSCVTIMSKDKPTIDVKMMNMEAANLAEVRSYCYLATVSELSTKAACPTMGEAHNDKRADPSFVCKQGVVDRGWGNGCGLFGKGSIDTCAKFACSTKATGRTILKENIKYEVAIFVHGPTTVESHGNYFTQTGAAQAGRFSITPAAPSYTLKLGEYGEVTVDCEPRSGIDTSAYYVMTVGTKTFLVHREWFMDLNLPWSSAESNVWRNRETLMEFEEPHATKQSVIALGSQEGALHQALAGAIPVEFSSNTVKLTSGHLKCRVKMEKLQLKGTTYGVCSKAFRFLGTPADTGHGTVVLELQYTGTDGPCKIPISSVASLNDLTPVGRLVTVNPFVSVSTANAKVLIELEPPFGDSYIVVGRGEQQINHHWHKSGSSIGKAFTATLKGAQRLAALGDTAWDFGSVGGVFTSVGKAVHQVFGGAFRSLFGGMSWITQGLLGALLLWMGINARDRSIALTFLAVGGVLLFLSVNVHADTGCAIDISRQELRCGSGVFIHNDVEAWIDRYKYYPETPQGLAKIIQKAHKEGVCGLRSVSRLEHQMWEAVKDELNTLLKENGVDLSIVVEKQEGMYKSAPRRLTATTEKLEIGWKAWGKSILFAPELANNTFVIDGPETKECPTQNRAWNNLEVEDFGFGLTSTRMFLRVRESNTTECDSKIIGTAVKNNLAIHSDLSYWIESRFNDTWKLERAVLGEVKSCTWPETHTLWGDGVLESDLIIPITLAGPRSNHNRRPGYKTQSQGPWDEGRVEIDFDYCPGTTVTLSESCGHRGPATRTTTESGKLITDWCCRSCTLPPLRYQTDNGCWYGMEIRPQRHDEKTLVQSQVNAYNADMIDPFQLGLLVVFLATQEVLRKRWTAKISMPAILIALLVLVFGGITYTDVLRYVILVGAAFAESNSGGDVVHLALMATFKIQPVFMVASFLKARWTNQENILLMLAAAFFQMAYYDARQILLWEMPDVLNSLAVAWMILRAITFTTTSNVVVPLLALLTPGLRCLNLDVYRILLLMVGIGSLIREKRSAAAKKKGASLLCLALASTGFFNPMILAAGLVACDPNRKRGWPATEVMTAVGLMFAIVGGLAELDIDSMAIPMTIAGLMFAAFVISGKSTDMWIERTADISWEGDAEITGSSERVDVRLDDDGNFQLMNDPGAPWKIWMLRMACLAISAYTPWAILPSVVGFWITLQYTKRGGVLWDTPSPKEYKRGDTTTGVYRIMTRGLLGSYQAGAGVMVEGVFHTLWHTTKGAALMSGEGRLDPYWGSVKEDRLCYGGPWKLQHKWNGQDEVQMIVVEPGKNVKNVQTKPGVFKTPEGEIGAVTLDFPTGTSGSPIVDKNGDVIGLYGNGVIMPNGSYISAIVQGERMDEPVPAGFEPEMLRKKQITVLDLHPGAGKTRRILPQIIKEAINRRLRTAVLAPTRVVAAEMAEALRGLPIRYQTSAVAREHNGNEIVDVMCHATLTHRLMSPHRVPNYNLFVMDEAHFTDPASIAARGYISTRVELGEAAAIFMTATPPGTSDPFPESNAPISDLQTEIPDRAWNSGYEWITEYIGKTVWFVPSVKMGNEIALCLQRAGKKVIQLNRKSYETEYPKCKNDDWDFVVTTDISEMGANFKASRVIDSRKSVKPTIITEGEGRVILGEPSAVTAASAAQRRGRTGRNPSQAGDEYCYGGHTNEDDSNCAHWTEARIMLDNINMPNGLIAQFYQPEREKVYTMDGEYRLRGEERKNFLELLRTADLPVWLAYKVAAAGVSYHDRRWCFDGPRTNTILEDNNEVEVITKLGERKILRPRWIDARVYSDHQALKSFKDFASGKRSQIGFIEVLGKMPEHFMGKTWEALDTMYVVATAEKGGRAHRMALEELPDALQTIALIALLSVMTMGVFFLLMQRKGIGKIGLGGVVLGAATFFCWMAEVPGTKIAGMLLLSLLLMIVLIPEPEKQRSQTDNQLAVFLICVLTLVGAVAANEMGWLDKTKSDISGLFGQRIETKENFSIGEFLLDLRPATAWSLYAVTTAVLTPLLKHLITSDYITTSLTSINVQASALFTLARGFPFVDVGVSALLLAAGCWGQVTLTVTVTSATLLFCHYAYMVPGWQAEAMRSAQRRTAAGIMKNAVVDGIVATDVPELERTTPIMQKKVGQVMLILVSLAALVVNPSVKTVREAGILITAAAVTLWENGASSVWNATTAIGLCHIMRGGWLSCLSITWTLVKNMEKPGLKRGGAKGRTLGEVWKERLNQMTKEEFIRYRKEAITEVDRSAAKHARKERNITGGHPVSRGTAKLRWLVERRFLEPVGKVIDLGCGRGGWCYYMATQKRVQEVRGYTKGGPGHEEPQLVQSYGWNIVTMKSGVDVFYRPSECCDTLLCDIGESSSSAEVEEHRTLRVLEMVEDWLHRGPKEFCVKVLCPYMPKVIEKMELLQRRYGGGLVRNPLSRNSTHEMYWVSRASGNVVHSVNMTSQVLLGRMEKKTWKGPQYEEDVNLGSGTRAVGKPLLNSDTSKIKNRIERLRREYSSTWHHDENHPYRTWNYHGSYEVKPTGSASSLVNGVVRLLSKPWDTITNVTTMAMTDTTPFGQQRVFKEKVDTKAPEPPEGVKYVLNETTNWLWAFLAREKRPRMCSREEFIRKVNSNAALGAMFEEQNQWRSAREAVEDPKFWEMVDEEREAHLRGECHTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARFLEFEALGFLNEDHWLGRKNSGGGVEGLGLQKLGYILREVGTRPGGRIYADDTAGWDTRITRADLENEAKVLELLDGEHRRLARAIIELTYRHKVVKVMRPAADGRTVMDVISREDQRGSGQVVTYALNTFTNLAVQLVRMMEGEGVIGPDDVEKLTKGKGPKVRTWLSENGEERLSRMAVSGDDCVVKPLDDRFATSLHFLNAMSKVRKDIQEWKPSTGWYDWQQVPFCSNHFTELIMKDGRTLVTPCRGQDELVGRARISPGAGWNVRDTACLAKSYAQMWLLLYFHRRDLRLMANAICSAVPVNWVPTGRTTWSIHAGGEWMTTEDMLEVWNRVWIEENEWMEDKTPVEKWSDVPYSGKREDIWCGSLIGTRARATWAENIQVAINQVRSIIGDEKYVDYMSSLKRYEDTTLVEDTVL","creator":"lchemes","dataset":["Viral proteins","Neglected tropical diseases proteins","RNA-binding proteins"],"date":"2018-08-23T16:56:21.000Z","disprot_id":"DP02051","features":{"pfam":[{"id":"PF00869","name":"Flavivirus glycoprotein, central and dimerisation domains","start":293,"end":589},{"id":"PF00948","name":"Flavivirus non-structural Protein NS1","start":794,"end":1143},{"id":"PF00949","name":"Peptidase S7, Flavivirus NS3 serine protease","start":1523,"end":1672},{"id":"PF00972","name":"Flavivirus RNA-directed RNA polymerase, fingers and palm domains","start":2781,"end":3233},{"id":"PF01002","name":"Flavivirus non-structural protein NS2B","start":1380,"end":1499},{"id":"PF01003","name":"Flavivirus capsid protein C","start":6,"end":122},{"id":"PF01004","name":"Flavivirus envelope glycoprotein M","start":218,"end":290},{"id":"PF01005","name":"Flavivirus non-structural protein NS2A","start":1155,"end":1308},{"id":"PF01349","name":"Flavivirus non-structural protein NS4B","start":2274,"end":2519},{"id":"PF01350","name":"Flavivirus non-structural protein NS4A","start":2130,"end":2271},{"id":"PF01570","name":"Flavivirus polyprotein propeptide","start":133,"end":214},{"id":"PF01728","name":"FtsJ-like methyltransferase","start":2583,"end":2752},{"id":"PF02832","name":"Flavivirus glycoprotein, immunoglobulin-like domain","start":592,"end":689},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1690,"end":1836},{"id":"PF20483","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","start":3237,"end":3400},{"id":"PF20907","name":"Flavivirus NS3 helicase, C-terminal helical domain","start":1980,"end":2122},{"id":"PF21659","name":"Flavivirus envelope glycoprotein E, stem/anchor domain","start":692,"end":786}],"gene3D":[{"start":216,"end":290,"id":"1.10.8.970","name":"Flavivirus envelope glycoprotein M-like","_id":"685af523b4ac24d5329d9396"},{"start":588,"end":696,"id":"2.60.40.350","name":"2.60.40.350","_id":"685af523b4ac24d5329d9397"},{"start":23,"end":98,"id":"1.10.10.930","name":"1.10.10.930","_id":"685af523b4ac24d5329d9398"},{"start":291,"end":587,"id":"2.60.98.10","name":"Tick-borne Encephalitis virus Glycoprotein, domain 1","_id":"685af523b4ac24d5329d9399"},{"start":124,"end":205,"id":"2.60.260.50","name":"Flavivirus polyprotein propeptide domain","_id":"685af523b4ac24d5329d939a"},{"start":697,"end":791,"id":"1.20.1280.260","name":"1.20.1280.260","_id":"685af523b4ac24d5329d939b"},{"start":2859,"end":2907,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d939c"},{"start":1517,"end":1591,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d939d"},{"start":1828,"end":1987,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d939e"},{"start":1516,"end":1674,"id":"2.40.10.10","name":"Trypsin-like serine proteases","_id":"685af523b4ac24d5329d939f"},{"start":2924,"end":3019,"id":"1.10.260.90","name":"1.10.260.90","_id":"685af523b4ac24d5329d93a0"},{"start":1419,"end":1468,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d93a1"},{"start":3061,"end":3127,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d93a2"},{"start":1689,"end":2022,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d93a3"},{"start":2801,"end":2856,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d93a4"},{"start":2528,"end":2800,"id":"3.40.50.150","name":"Vaccinia Virus protein VP39","_id":"685af523b4ac24d5329d93a5"}]},"genes":[],"length":3433,"name":"Genome polyprotein","ncbi_taxon_id":11078,"organism":"Kunjin virus (strain MRM61C)","regions_counter":3,"released":"2018_11","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Flavivirus"],"UniParc":"UPI0000131E43","uniref100":"UniRef100_P14335","uniref50":"UniRef50_P06935","uniref90":"UniRef90_P06935","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":22,"interaction_partner":[],"reference_html":"West Nile virus core protein; tetramer structure and ribbon formation. <i> Dokland T, Walsh M, Mackenzie JM, Khromykh AA, Ee KH, Wang S. </i> Structure, 2004","reference_id":"15242592","region_id":"DP02051r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Crystals of the full-length C protein were unstable and disordered and did not diffract X-rays to high resolution. Assuming that the crystal disorder was caused by flexible regions in the protein, we treated the full-length protein with trypsin, resulting in a stable fragment starting at Val23 and ending at Arg98 (Figure 1).","_id":"685af523b4ac24d5329d93ab"},{"type":"Results","text":" The N-terminal region corresponds to the disordered region (residues 1–22) that was cleaved off by the trypsin treatment, and the C-terminal region corresponds to helix α4, which forms an 11 Å wide tunnel in the tetramer (Figure 3B).","_id":"685af523b4ac24d5329d93ac"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-11T09:18:28.423Z","_id":"685af523b4ac24d5329d93ad"},"version":1,"_id":"685af523b4ac24d5329d93aa","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":22,"interaction_partner":[],"reference_html":"West Nile virus core protein; tetramer structure and ribbon formation. <i> Dokland T, Walsh M, Mackenzie JM, Khromykh AA, Ee KH, Wang S. </i> Structure, 2004","reference_id":"15242592","region_id":"DP02051r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Crystals of the full-length C protein were unstable and disordered and did not diffract X-rays to high resolution. Assuming that the crystal disorder was caused by flexible regions in the protein, we treated the full-length protein with trypsin, resulting in a stable fragment starting at Val23 and ending at Arg98 (Figure 1).","_id":"685af523b4ac24d5329d93af"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-11T12:50:35.665Z","_id":"685af523b4ac24d5329d93b0"},"version":1,"_id":"685af523b4ac24d5329d93ae","reference_source":"pmid"}],"__v":0,"disorder_content":0.006408389163996504,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"}],"Structural state":[{"start":1,"end":22,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01472","name":"PUA domain","start":267,"end":340},{"id":"PF01509","name":"TruB family pseudouridylate synthase (N terminal domain)","start":80,"end":196},{"id":"PF08068","name":"DKCLD (NUC011) domain","start":19,"end":76},{"id":"PF16198","name":"tRNA pseudouridylate synthase B C-terminal domain","start":197,"end":263}],"gene3D":[{"start":52,"end":258,"id":"3.30.2350.10","name":"Pseudouridine synthase"}]},"uniref50":"UniRef50_P33322","sequence":"MSKEDFVIKPEAAGASTDTSEWPLLLKNFDKLLVRSGHYTPIPAGSSPLKRDLKSYISSGVINLDKPSNPSSHEVVAWIKRILRCEKTGHSGTLDPKVTGCLIVCIDRATRLVKSQQGAGKEYVCIVRLHDALKDEKDLGRSLENLTGALFQRPPLISAVKRQLRVRTIYESNLIEFDNKRNLGVFWASCEAGTYMRTLCVHLGMLLGVGGHMQELRRVRSGALSENDNMVTLHDVMDAQWVYDNTRDESYLRSIIQPLETLLVGYKRIVVKDSAVNAVCYGAKLMIPGLLRYEEGIELYDEIVLITTKGEAIAVAIAQMSTVDLASCDHGVVASVKRCIMERDLYPRRWGLGPVAQKKKQMKADGKLDKYGRVNENTPEQWKKEYVPLDNAEQSTSSSQETKETEEEPKKAKEDSLIKEVETEKEEVKEDDSKKEKKEKKDKKEKKEKKEKKDKKEKKEKKEKKRKSEDGDSEEKKSKKSKK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P33322","disprot_id":"DP02055","ncbi_taxon_id":559292,"regions_counter":1,"creator":"msalva","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":394,"region_id":"DP02055r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Reconstitution and structural analysis of the yeast box H/ACA RNA-guided pseudouridine synthase. <i> Li S, Duan J, Li D, Yang B, Dong M, Ye K. </i> Genes Dev, 2011","statement":[{"text":"The Cbf5 CTE was not observed in crystal, likely due to protein degradation and intrinsic disorder","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ahatos","start":351,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3U28"}],"reference_id":"22085967","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P33322","date":"2018-08-24T07:07:35.000Z","acc":"P33322","name":"H/ACA ribonucleoprotein complex subunit CBF5","length":483,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000052ECF","genes":[{"name":{"value":"CBF5"},"orfNames":[{"value":"L9470.11"}],"olnNames":[{"value":"YLR175W"}]}],"alphafold_very_low_content":0.14492753623188406,"disorder_content":0.09109730848861283,"disprot_consensus":{"full":[{"start":351,"end":394,"type":"D"}],"Structural state":[{"start":351,"end":394,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00010","name":"Helix-loop-helix DNA-binding domain","start":113,"end":164}],"gene3D":[{"start":112,"end":169,"id":"4.10.280.10","name":"Helix-loop-helix DNA-binding domain"}]},"uniref50":"UniRef50_P70447","sequence":"MFVKSETLELKEEEEVLMLLGSASPASATLTPMSSSADEEEDEELRRPGSARGQRGAEAEQGVQGSPASGAGGCRPGRLLGLMHECKRRPSRSRAVSRGAKTAETVQRIKKTRRLKANNRERNRMHNLNAALDALREVLPTFPEDAKLTKIETLRFAHNYIWALTETLRLADHCAGAGGLQGALFTEAVLLSPGAALGASGDSPSPPSSWSCTNSPASSSNSTSPYSCTLSPASPGSDVDYWQPPPPEKHRYAPHLPLARDCI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P70447","disprot_id":"DP02061","ncbi_taxon_id":10090,"regions_counter":2,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":75,"region_id":"DP02061r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Phosphorylation in intrinsically disordered regions regulates the activity of Neurogenin2. <i> McDowell GS, Hindley CJ, Lippens G, Landrieu I, Philpott A. </i> BMC Biochem, 2014","statement":[{"text":"Assignment of the backbone atom resonances of mNgn2 was performed based on 3D experiments on the 15N, 13C doubly-labelled protein (Additional file 4: Table S1, Additional file 5: 3D NMR dataset). This assignment does not cover the full-length protein: the detected domains correspond to residues 1 to 31 and 49 to 75, containing two SP sites and one TP site.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":49,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"25374254","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":31,"region_id":"DP02061r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Phosphorylation in intrinsically disordered regions regulates the activity of Neurogenin2. <i> McDowell GS, Hindley CJ, Lippens G, Landrieu I, Philpott A. </i> BMC Biochem, 2014","statement":[{"text":"Assignment of the backbone atom resonances of mNgn2 was performed based on 3D experiments on the 15N, 13C doubly-labelled protein (Additional file 4: Table S1, Additional file 5: 3D NMR dataset). This assignment does not cover the full-length protein: the detected domains correspond to residues 1 to 31 and 49 to 75, containing two SP sites and one TP site.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":1,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"25374254","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P70447","date":"2018-08-24T08:58:52.000Z","acc":"P70447","name":"Neurogenin-2","length":263,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000271EA","genes":[{"name":{"value":"Neurog2"},"synonyms":[{"value":"Ath4a"},{"value":"Atoh4"},{"value":"Ngn2"}]}],"alphafold_very_low_content":0.3688212927756654,"disorder_content":0.22053231939163498,"disprot_consensus":{"full":[{"start":1,"end":31,"type":"D"},{"start":49,"end":75,"type":"D"}],"Structural state":[{"start":1,"end":31,"type":"D"},{"start":49,"end":75,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01423","name":"LSM domain","start":15,"end":90}],"gene3D":[{"start":1,"end":93,"id":"2.30.30.100","name":"2.30.30.100"}]},"uniref50":"UniRef50_Q9Y7M4","sequence":"MESAQAVAEPLDLVRLSLDEIVYVKLRGDRELNGRLHAYDEHLNMVLGDAEEIVTIFDDEETDKDKALKTIRKHYEMLFVRGDSVILIAPPRN","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"uniref90":"UniRef90_Q9Y7M4","disprot_id":"DP02065","ncbi_taxon_id":284812,"regions_counter":1,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":69,"region_id":"DP02065r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structures of Lsm3, Lsm4 and Lsm5/6/7 from Schizosaccharomyces pombe. <i> Wu D, Jiang S, Bowler MW, Song H. </i> PLoS One, 2012","statement":[{"text":"The structure of SpLsm3 was solved by single-wavelength anomalous dispersion (SAD) phasing method using a SeMet-substituted crystal. The final model has been refined to an R factor of 24.3% and Rfree of 27.7% with good stereochemical geometry. Residues 1–8 in the N-terminal and residues 56–69 in the loop region are disordered in the electron density map.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":56,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4EMG"}],"reference_id":"22615807","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9Y7M4","date":"2018-08-24T09:29:47.000Z","acc":"Q9Y7M4","name":"Probable U6 snRNA-associated Sm-like protein LSm3","length":93,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","dataset":[],"UniParc":"UPI000012E964","genes":[{"name":{"value":"lsm3"},"orfNames":[{"value":"SPBC9B6.05c"}]}],"alphafold_very_low_content":0.010752688172043012,"disorder_content":0.15053763440860216,"disprot_consensus":{"full":[{"start":56,"end":69,"type":"D"}],"Structural state":[{"start":56,"end":69,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03760","name":"Late embryogenesis abundant (LEA) group 1","start":1,"end":78}]},"uniref50":"UniRef50_Q9FG31","sequence":"MQSMKETASNIAASAKSGMDKTKATLEEKAEKMKTRDPVQKQMATQVKEDKINQAEMQKRETRQHNAAMKEAAGAGTGLGLGTATHSTTGQVGHGTGTHQMSALPGHGTGQLTDRVVEGTAVTDPIGRNTGTGRTTAHNTHVGGGGATGYGTGGGYTG","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q9FG31","disprot_id":"DP02066","ncbi_taxon_id":3702,"regions_counter":15,"creator":"mlambrughi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":158,"region_id":"DP02066r001","released":"2024_06","ec_id":"ECO:0006204","reference_html":"Metal-binding polymorphism in late embryogenesis abundant protein AtLEA4-5, an intrinsically disordered protein. <i> French-Pacheco L, Cuevas-Velazquez CL, Rivillas-Acevedo L, Covarrubias AA, Amero C. </i> PeerJ, 2018","statement":[{"text":"AtLEA4-5 was predicted to be disordered based on previous amino acid sequence analysis, while CD spectra showed a typical spectrum for a disorder protein, as indicated by the presence of minimum at ∼200 nm (Fig. S1), in agreement with previous reports (Cuevas-Velazquez et al., 2016).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-01T16:30:51.968Z","reference_source":"pmid","term_name":"disorder","reference_id":"29892507","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":158,"term_name":"copper ion binding","released":"2024_06","ec_name":"circular dichroism evidence used in manual assertion","reference_html":"Metal-binding polymorphism in late embryogenesis abundant protein AtLEA4-5, an intrinsically disordered protein. <i> French-Pacheco L, Cuevas-Velazquez CL, Rivillas-Acevedo L, Covarrubias AA, Amero C. </i> PeerJ, 2018","statement":[{"text":"These results indicate that AtLEA4-5 coordinates Cu(II) through at least one nitrogen of a histidine imidazole and backbone deprotonated amides.","type":"Results"}],"term_id":"GO:0005507","curator_id":"vnugnes","start":1,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"29892507","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-01T16:42:30.671Z","reference_source":"pmid","ec_id":"ECO:0006200","region_id":"DP02066r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a copper (Cu) ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"ChEBI","id":"29036","operator":null,"partner_start":null,"partner_end":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"23414","entry_name":"copper(II) sulfate"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":158,"region_id":"DP02066r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The Unstructured N-terminal Region of Arabidopsis Group 4 Late Embryogenesis Abundant (LEA) Proteins Is Required for Folding and for Chaperone-like Activity under Water Deficit. <i> Cuevas-Velazquez CL, Saab-Rincón G, Reyes JL, Covarrubias AA. </i> J Biol Chem, 2016","statement":[{"text":"To determine the secondary structure of AtLEA4-2 and AtLEA4-5 in solution, the purified proteins were analyzed by far UV CD. The results obtained corroborated that both proteins are mostly disordered in solution over a wide range of temperatures (Fig. 2, A and B) and pH (data not shown), with the characteristic negative band for random coil structures around 198 nm.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mlambrughi","start":1,"term_ontology":"IDPO","curator_name":"Matteo Lambrughi","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-0894-8627","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27006402","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-02-01T16:31:25.505Z"}},{"start":1,"end":158,"reference_id":"29892507","reference_source":"pmid","reference_html":"Metal-binding polymorphism in late embryogenesis abundant protein AtLEA4-5, an intrinsically disordered protein. <i> French-Pacheco L, Cuevas-Velazquez CL, Rivillas-Acevedo L, Covarrubias AA, Amero C. </i> PeerJ, 2018","date":"2024-02-01T16:34:58.258Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008270","term_name":"zinc ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006082","ec_ontology":"ECO","ec_name":"affinity chromatography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"29105","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02066r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"35176","entry_name":"zinc sulfate"}],"statement":[{"text":"For Zn(II), Cu(II), and Ni(II) columns, the protein was eluted only when EDTA was added, showing that the protein is able to bind these metal ions (Fig. S2).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a zinc ion (Zn).\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":158,"reference_id":"29892507","reference_source":"pmid","reference_html":"Metal-binding polymorphism in late embryogenesis abundant protein AtLEA4-5, an intrinsically disordered protein. <i> French-Pacheco L, Cuevas-Velazquez CL, Rivillas-Acevedo L, Covarrubias AA, Amero C. </i> PeerJ, 2018","date":"2024-02-01T16:35:52.252Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0016151","term_name":"nickel cation binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006082","ec_ontology":"ECO","ec_name":"affinity chromatography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"49786","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02066r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"53001","entry_name":"nickel sulfate"}],"statement":[{"text":"For Zn(II), Cu(II), and Ni(II) columns, the protein was eluted only when EDTA was added, showing that the protein is able to bind these metal ions (Fig. S2).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a nickel (Ni) cation.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":158,"reference_id":"29892507","reference_source":"pmid","reference_html":"Metal-binding polymorphism in late embryogenesis abundant protein AtLEA4-5, an intrinsically disordered protein. <i> French-Pacheco L, Cuevas-Velazquez CL, Rivillas-Acevedo L, Covarrubias AA, Amero C. </i> PeerJ, 2018","date":"2024-02-01T16:36:41.219Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005507","term_name":"copper ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006082","ec_ontology":"ECO","ec_name":"affinity chromatography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"29036","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02066r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"23414","entry_name":"copper(II) sulfate"}],"statement":[{"text":"For Zn(II), Cu(II), and Ni(II) columns, the protein was eluted only when EDTA was added, showing that the protein is able to bind these metal ions (Fig. S2).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a copper (Cu) ion.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":158,"reference_id":"29892507","reference_source":"pmid","reference_html":"Metal-binding polymorphism in late embryogenesis abundant protein AtLEA4-5, an intrinsically disordered protein. <i> French-Pacheco L, Cuevas-Velazquez CL, Rivillas-Acevedo L, Covarrubias AA, Amero C. </i> PeerJ, 2018","date":"2024-02-01T16:44:23.854Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005507","term_name":"copper ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006289","ec_ontology":"ECO","ec_name":"site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"29036","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02066r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"23414","entry_name":"copper(II) sulfate"}],"statement":[{"text":"We estimated the binding parameters by plotting average EPR signals changes as function of Cu(II) concentrations. The data was fitted with to a hyperbolic equation and provided an apparent metal binding dissociation constant in the micromolar range (∼300 μM) (Fig. S4).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a copper (Cu) ion.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":158,"reference_id":"29892507","reference_source":"pmid","reference_html":"Metal-binding polymorphism in late embryogenesis abundant protein AtLEA4-5, an intrinsically disordered protein. <i> French-Pacheco L, Cuevas-Velazquez CL, Rivillas-Acevedo L, Covarrubias AA, Amero C. </i> PeerJ, 2018","date":"2024-02-01T16:54:03.593Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051260","term_name":"protein homooligomerization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","region_id":"DP02066r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"23414","entry_name":"copper(II) sulfate"}],"statement":[{"text":"From this we could conclude that under these conditions AtLEA4-5 consist of different states, that include monomer, probably tetramers, and higher order oligomers.","type":"Results"},{"text":"DLS measurements of AtLEA4-5 in the presence of different Cu(II) concentration yielded a decrease in the translational diffusion coefficient consistent with a size increase due to oligomerization induced by metal binding (Fig. 5). ","type":"Results"}],"term_comment":"","term_def":"\"The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":158,"reference_id":"29892507","reference_source":"pmid","reference_html":"Metal-binding polymorphism in late embryogenesis abundant protein AtLEA4-5, an intrinsically disordered protein. <i> French-Pacheco L, Cuevas-Velazquez CL, Rivillas-Acevedo L, Covarrubias AA, Amero C. </i> PeerJ, 2018","date":"2024-02-01T16:55:05.521Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005507","term_name":"copper ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"29036","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02066r009","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"23414","entry_name":"copper(II) sulfate"}],"statement":[{"text":"As shown in Fig. 6, the addition of Ni(II) produced a simple exothermic thermogram, which was best fitted to a single binding site model with a 1:1 stoichiometry; whereas the addition of Cu(II) and Zn(II) exhibited a complex behavior involving both exothermic and endothermic processes.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a copper (Cu) ion.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":158,"reference_id":"29892507","reference_source":"pmid","reference_html":"Metal-binding polymorphism in late embryogenesis abundant protein AtLEA4-5, an intrinsically disordered protein. <i> French-Pacheco L, Cuevas-Velazquez CL, Rivillas-Acevedo L, Covarrubias AA, Amero C. </i> PeerJ, 2018","date":"2024-02-01T16:55:35.595Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008270","term_name":"zinc ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"29105","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02066r010","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"35176","entry_name":"zinc sulfate"}],"statement":[{"text":"As shown in Fig. 6, the addition of Ni(II) produced a simple exothermic thermogram, which was best fitted to a single binding site model with a 1:1 stoichiometry; whereas the addition of Cu(II) and Zn(II) exhibited a complex behavior involving both exothermic and endothermic processes.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a zinc ion (Zn).\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":158,"reference_id":"29892507","reference_source":"pmid","reference_html":"Metal-binding polymorphism in late embryogenesis abundant protein AtLEA4-5, an intrinsically disordered protein. <i> French-Pacheco L, Cuevas-Velazquez CL, Rivillas-Acevedo L, Covarrubias AA, Amero C. </i> PeerJ, 2018","date":"2024-02-01T16:56:12.466Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0016151","term_name":"nickel cation binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"49786","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02066r011","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"53001","entry_name":"nickel sulfate"}],"statement":[{"text":"As shown in Fig. 6, the addition of Ni(II) produced a simple exothermic thermogram, which was best fitted to a single binding site model with a 1:1 stoichiometry; whereas the addition of Cu(II) and Zn(II) exhibited a complex behavior involving both exothermic and endothermic processes.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a nickel (Ni) cation.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":77,"reference_id":"27006402","reference_source":"pmid","reference_html":"The Unstructured N-terminal Region of Arabidopsis Group 4 Late Embryogenesis Abundant (LEA) Proteins Is Required for Folding and for Chaperone-like Activity under Water Deficit. <i> Cuevas-Velazquez CL, Saab-Rincón G, Reyes JL, Covarrubias AA. </i> J Biol Chem, 2016","date":"2025-11-25T16:06:01.121Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"region_id":"DP02066r012","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":null}],"statement":[{"text":"Together, these data indicate that AtLEA4-2 and AtLEA4-5 can acquire secondary structure under low water availability or macromolecular crowding in vitro, possibly reflecting what occurs in plant cells under water deficit.","type":"Results"},{"text":"Likewise, treatments with glycerol and PEG led to the same behavior in this protein (Fig. 4, C and D), reaching up to 55 and 42% α-helix at the highest glycerol and PEG concentrations, respectively (Table 2).","type":"Results"},{"text":"This finding was further supported by the results obtained from the addition of glycerol or PEG to AtLEA4-578–158 solutions, which showed no effect on its structure (Fig. 4, G and H), given that the negative band at [θ]222 did not show any change and that only a slight increase in the [θ]198 signal was detected.","type":"Results"},{"text":"Together, these data demonstrate that the AtLEA4-5 N-terminal region (AtLEA4-51–77) is necessary and sufficient to drive α-helix conformations in this protein under low water availability or macromolecular crowding conditions.","type":"Results"}]},{"start":1,"end":77,"reference_id":"27006402","reference_source":"pmid","reference_html":"The Unstructured N-terminal Region of Arabidopsis Group 4 Late Embryogenesis Abundant (LEA) Proteins Is Required for Folding and for Chaperone-like Activity under Water Deficit. <i> Cuevas-Velazquez CL, Saab-Rincón G, Reyes JL, Covarrubias AA. </i> J Biol Chem, 2016","date":"2025-11-25T16:24:38.989Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0050821","term_name":"protein stabilization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"IDA","region_id":"DP02066r013","statement":[{"text":" For this purpose, LDH in the presence or absence of AtLEA4-5, AtLEA4-2, AtLEA4-51–77, or AtLEA4-578–158 was subjected to in vitro freeze-thaw cycles and partial dehydration treatments.","type":"Results"},{"text":"Interestingly, a comparable protection was produced by AtLEA4-51–77, contrasting with the negligible protective levels showed by the AtLEA4-5 C-terminal region (AtLEA4-578–158), whose values were rather close to those shown by lysozyme, an unrelated globular protein (Fig. 5, A and B).","type":"Results"},{"text":"Because the hydrophilicity index and length are similar between the N-terminal and C-terminal regions, these data are consistent with the hypothesis that the protective activity of these proteins is rather dependent on the conserved motifs present in the N-terminal region and/or on its ability to fold into α-helical conformations.","type":"Results"}],"term_comment":"","term_def":"\"Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":77,"reference_id":"27006402","reference_source":"pmid","reference_html":"The Unstructured N-terminal Region of Arabidopsis Group 4 Late Embryogenesis Abundant (LEA) Proteins Is Required for Folding and for Chaperone-like Activity under Water Deficit. <i> Cuevas-Velazquez CL, Saab-Rincón G, Reyes JL, Covarrubias AA. </i> J Biol Chem, 2016","date":"2025-11-25T16:24:47.500Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0009631","term_name":"cold acclimation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"IDA","region_id":"DP02066r014","statement":[{"text":" For this purpose, LDH in the presence or absence of AtLEA4-5, AtLEA4-2, AtLEA4-51–77, or AtLEA4-578–158 was subjected to in vitro freeze-thaw cycles and partial dehydration treatments.","type":"Results"},{"text":"Interestingly, a comparable protection was produced by AtLEA4-51–77, contrasting with the negligible protective levels showed by the AtLEA4-5 C-terminal region (AtLEA4-578–158), whose values were rather close to those shown by lysozyme, an unrelated globular protein (Fig. 5, A and B).","type":"Results"},{"text":"Because the hydrophilicity index and length are similar between the N-terminal and C-terminal regions, these data are consistent with the hypothesis that the protective activity of these proteins is rather dependent on the conserved motifs present in the N-terminal region and/or on its ability to fold into α-helical conformations.","type":"Results"}],"term_comment":"","term_def":"\"Any process that increases freezing tolerance of an organism in response to low, nonfreezing temperatures.\" [GOC:syr]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":77,"reference_id":"27006402","reference_source":"pmid","reference_html":"The Unstructured N-terminal Region of Arabidopsis Group 4 Late Embryogenesis Abundant (LEA) Proteins Is Required for Folding and for Chaperone-like Activity under Water Deficit. <i> Cuevas-Velazquez CL, Saab-Rincón G, Reyes JL, Covarrubias AA. </i> J Biol Chem, 2016","date":"2025-11-25T16:26:29.650Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0009269","term_name":"response to desiccation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"ec_go":"IDA","region_id":"DP02066r015","statement":[{"text":"AtLEA4-2, the smallest protein of this group, mostly consisting of the N-terminal region (Fig. 1A), showed a similar protective effect on LDH activity as AtLEA4-5 after partial dehydration (Fig. 5A).","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a desiccation stimulus, extreme dryness resulting from the prolonged deprivation of water.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_Q9FG31","date":"2018-08-24T09:36:38.000Z","acc":"Q9FG31","name":"Late embryogenesis abundant protein 46","length":158,"organism":"Arabidopsis thaliana","dataset":["Stress response proteins"],"UniParc":"UPI000009D416","genes":[{"name":{"value":"LEA46","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"18318901","url":"http://www.ncbi.nlm.nih.gov/pubmed/18318901","alternativeUrl":"https://europepmc.org/abstract/MED/18318901"}}]},"synonyms":[{"value":"LEA4-5","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"20668063","url":"http://www.ncbi.nlm.nih.gov/pubmed/20668063","alternativeUrl":"https://europepmc.org/abstract/MED/20668063"}}]}],"orfNames":[{"value":"MPH15.12","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"BAB09810.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAB09810.1"}}]}],"olnNames":[{"value":"At5g06760","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT5G06760","url":""}}]}]}],"alphafold_very_low_content":0.4620253164556962,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":77,"type":"T"},{"start":78,"end":158,"type":"D"}],"Structural state":[{"start":1,"end":158,"type":"D"}],"Molecular function":[{"start":1,"end":158,"type":"F"}],"Biological process":[{"start":1,"end":158,"type":"F"}],"Structural transition":[{"start":1,"end":77,"type":"T"}]}},{"features":{"pfam":[{"id":"PF01423","name":"LSM domain","start":27,"end":98}],"gene3D":[{"start":4,"end":107,"id":"2.30.30.100","name":"2.30.30.100"}]},"uniref50":"UniRef50_O74499","sequence":"MSSLQKRPGPGNSSQPTERPRKESILDLSRYQDQRIQATFTGGRQITGILKGFDQLMNLVLDDVEEQLRNPEDGKLTGAIRKLGLVVVRGTTLVLIAPMDGSEEIPNPFVQAE","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"uniref90":"UniRef90_O74499","disprot_id":"DP02067","ncbi_taxon_id":284812,"regions_counter":2,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":31,"region_id":"DP02067r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structures of Lsm3, Lsm4 and Lsm5/6/7 from Schizosaccharomyces pombe. <i> Wu D, Jiang S, Bowler MW, Song H. </i> PLoS One, 2012","statement":[{"text":"Several regions are disordered, namely residues 1–5 and 78–80 in Sp-Lsm5, residues 74–75 in SpLsm6, and residues 1–31, 69–77 and 101–113 in SpLsm7.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":1,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4EMK"}],"reference_id":"22615807","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":113,"region_id":"DP02067r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structures of Lsm3, Lsm4 and Lsm5/6/7 from Schizosaccharomyces pombe. <i> Wu D, Jiang S, Bowler MW, Song H. </i> PLoS One, 2012","statement":[{"text":"Several regions are disordered, namely residues 1–5 and 78–80 in Sp-Lsm5, residues 74–75 in SpLsm6, and residues 1–31, 69–77 and 101–113 in SpLsm7.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":101,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4EMK"}],"reference_id":"22615807","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_O74499","date":"2018-08-24T09:36:41.000Z","acc":"O74499","name":"U6 snRNA-associated Sm-like protein LSm7","length":113,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","dataset":[],"UniParc":"UPI000006BE7F","genes":[{"name":{"value":"lsm7"},"orfNames":[{"value":"SPCC285.12"}]}],"alphafold_very_low_content":0,"disorder_content":0.3893805309734513,"disprot_consensus":{"full":[{"start":1,"end":31,"type":"D"},{"start":101,"end":113,"type":"D"}],"Structural state":[{"start":1,"end":31,"type":"D"},{"start":101,"end":113,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01423","name":"LSM domain","start":6,"end":70}],"gene3D":[{"start":1,"end":83,"id":"2.30.30.100","name":"2.30.30.100"}]},"uniref50":"UniRef50_O14352","sequence":"MLPLTLLNATQGRPILVELKNGETFNGHLENCDNYMNLTLREVIRTMPDGDKFFRLPECYIRGNNIKYLRIQDEVLSQVAKQQAQQRENRGSRFRGRGQRGRGNYGHTAPNRRGRGRGGHM","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"uniref90":"UniRef90_O14352","disprot_id":"DP02068","ncbi_taxon_id":284812,"regions_counter":2,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":11,"region_id":"DP02068r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structures of Lsm3, Lsm4 and Lsm5/6/7 from Schizosaccharomyces pombe. <i> Wu D, Jiang S, Bowler MW, Song H. </i> PLoS One, 2012","statement":[{"text":"The structure of SpLsm4N was also determined by the SAD method using the data obtained from a SeMet derivative crystal. The structure has been refined at a resolution of 2.2 Å to an R factor of 23.7% and Rfree of 25.2% with good geometry. The final model covers residues 12–71 of every molecule in the AU. Residues 1–11 and 72–91 are not visible in the electron density map and assumed to be disordered","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":1,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4EMH"}],"reference_id":"22615807","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":91,"region_id":"DP02068r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structures of Lsm3, Lsm4 and Lsm5/6/7 from Schizosaccharomyces pombe. <i> Wu D, Jiang S, Bowler MW, Song H. </i> PLoS One, 2012","statement":[{"text":"The structure of SpLsm4N was also determined by the SAD method using the data obtained from a SeMet derivative crystal. The structure has been refined at a resolution of 2.2 Å to an R factor of 23.7% and Rfree of 25.2% with good geometry. The final model covers residues 12–71 of every molecule in the AU. Residues 1–11 and 72–91 are not visible in the electron density map and assumed to be disordered","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":72,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4EMH"}],"reference_id":"22615807","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_O14352","date":"2018-08-24T10:34:22.000Z","acc":"O14352","name":"Probable U6 snRNA-associated Sm-like protein LSm4","length":121,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","dataset":[],"UniParc":"UPI000012E967","genes":[{"name":{"value":"lsm4"},"orfNames":[{"value":"SPBC30D10.06"}]}],"alphafold_very_low_content":0.15702479338842976,"disorder_content":0.256198347107438,"disprot_consensus":{"full":[{"start":1,"end":11,"type":"D"},{"start":72,"end":91,"type":"D"}],"Structural state":[{"start":1,"end":11,"type":"D"},{"start":72,"end":91,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":63,"end":225},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":264,"end":372}],"gene3D":[{"start":21,"end":242,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":243,"end":411,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_P38919","sequence":"MATTATMATSGSARKRLLKEEDMTKVEFETSEEVDVTPTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILAPTRELAVQIQKGLLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEMPMNVADLI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P38919","disprot_id":"DP02069","ncbi_taxon_id":9606,"regions_counter":5,"creator":"mpajkos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":21,"region_id":"DP02069r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Insights into the recruitment of the NMD machinery from the crystal structure of a core EJC-UPF3b complex. <i> Buchwald G, Ebert J, Basquin C, Sauliere J, Jayachandran U, Bono F, Le Hir H, Conti E. </i> Proc Natl Acad Sci U S A, 2010","statement":[{"text":"The human EJC core complex was reconstituted combining full-length MAGO bound to the RRM domain of Y14, full-length eIF4AIII bound to the SELOR domain of BTZ,  a U15 RNA, AMPPNP, and magnesium ions. In the final model  eIF4AIII residues 22–411 was observed, other portions of the protein are not present in the structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":1,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2XB2"}],"reference_id":"20479275","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-02-15T13:51:20.613Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":20,"region_id":"DP02069r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA. <i> Bono F, Ebert J, Lorentzen E, Conti E. </i> Cell, 2006","statement":[{"text":"\"The final model includes six bases of polyU RNA, AMPPNP, essentially all of Mago-Y14 (Mago residues 4–146 and Y14 residues 66-154), most of eIF4AIII (except for the 20 N-terminal residues that are disordered)\"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":1,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2J0S"}],"reference_id":"16923391","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-02-15T13:53:15.393Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":21,"reference_id":"28502770","reference_source":"pmid","reference_html":"An Atomic Structure of the Human Spliceosome. <i> Zhang X, Yan C, Hang J, Finci LI, Lei J, Shi Y. </i> Cell, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5XJC"}],"region_id":"DP02069r003","statement":[{"text":"The N-terminal region of eIF4AIII is disordered, as referenced in Table S2 and confirmed upon visual inspection of the structure.","type":"Curator statement"}],"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":1,"end":20,"reference_id":"24218557","reference_source":"pmid","reference_html":"Crystal structure of the human eIF4AIII-CWC22 complex shows how a DEAD-box protein is inhibited by a MIF4G domain. <i> Buchwald G, Schüssler S, Basquin C, Le Hir H, Conti E. </i> Proc Natl Acad Sci U S A, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4C9B"}],"region_id":"DP02069r004","statement":[{"text":"No ordered electron density was present for the N-terminal region of eIF4AIII (residues 1–20) and for the N-terminal residues and a disordered loop of CWC22 (residues 116–122 and 142–148).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P38919","date":"2018-08-24T11:48:33.000Z","acc":"P38919","name":"Eukaryotic initiation factor 4A-III","length":411,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI000014F40B","genes":[{"name":{"value":"EIF4A3"},"synonyms":[{"value":"DDX48"},{"value":"KIAA0111"}]}],"alphafold_very_low_content":0.04866180048661801,"disorder_content":0.051094890510948905,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"}],"Structural state":[{"start":1,"end":21,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00729","name":"Viral coat protein (S domain)","start":52,"end":245},{"id":"PF08462","name":"Carmovirus coat protein","start":250,"end":348}],"gene3D":[{"start":76,"end":244,"id":"2.60.120.20","name":"2.60.120.20"},{"start":246,"end":348,"id":"2.60.40.1780","name":"Carmovirus coat protein"}]},"uniref50":"UniRef50_P04383","sequence":"MENKGEKIAMNPTVQTLAQKGDKLAVKLVTRGWASLSTNQKRRAEMLAGYTPAILAFTPRRPRMTNPPPRTSRNSPGQAGKSMTMSKTELLSTVKGTTGVIPSFEDWVVSPRNVAVFPQLSLLATNFNKYRITALTVKYSPACSFETNGRVALGFNDDASDTPPTTKVGFYDLGKHVETAAQTAKDLVIPVDGKTRFIRDSASDDAKLVDFGRIVLSTYGFDKADTVVGELFIQYTIVLSDPTKTAKISQASNDKVSDGPTYVVPSVNGNELQLRVVAAGKWCIIVRGTVEGGFTKPTLIGPGISGDVDYESARPIAVCELVTQMEGQILKITKTSAEQPLQWVVYRM","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Tolucaviricetes","Tolivirales","Tombusviridae","Procedovirinae","Alphacarmovirus"],"uniref90":"UniRef90_P04383","disprot_id":"DP02071","ncbi_taxon_id":11986,"regions_counter":1,"creator":"ameszaros","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":81,"region_id":"DP02071r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The atomic structure of Carnation Mottle Virus capsid protein. <i> Morgunova EYu, Dauter Z, Fry E, Stuart DI, Stel'mashchuk VYa, Mikhailov AM, Wilson KS, Vainshtein BK. </i> FEBS Lett, 1994","statement":[{"text":"The  electron  density  maps  did  not  show  any  ordered  density  for  the  N-terminal  arm  of  any  of  three protein  subunits.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ameszaros","start":1,"term_ontology":"IDPO","curator_name":"Attila Meszaros","reference_id":"8307192","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1OPO"}],"term_name":"disorder","curator_orcid":"0000-0002-4578-4879","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-09-28T14:29:16.743Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P04383","date":"2018-08-24T12:32:06.000Z","acc":"P04383","name":"Capsid protein","length":348,"organism":"Carnation mottle virus","dataset":["Viral proteins","RNA-binding proteins"],"UniParc":"UPI0000127D2E","genes":[{"orfNames":[{"value":"ORF4"}]}],"disorder_content":0.23275862068965517,"disprot_consensus":{"full":[{"start":1,"end":81,"type":"D"}],"Structural state":[{"start":1,"end":81,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00004","name":"ATPase family associated with various cellular activities (AAA)","start":530,"end":672},{"id":"PF01426","name":"BAH domain","start":45,"end":168},{"id":"PF09079","name":"CDC6, C terminal winged helix domain","start":766,"end":857},{"id":"PF17872","name":"AAA lid domain","start":698,"end":734}],"gene3D":[{"start":486,"end":677,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":8,"end":171,"id":"2.30.30.490","name":"2.30.30.490"}]},"uniref50":"UniRef50_Q13415","sequence":"MAHYPTRLKTRKTYSWVGRPLLDRKLHYQTYREMCVKTEGCSTEIHIQIGQFVLIEGDDDENPYVAKLLELFEDDSDPPPKKRARVQWFVRFCEVPACKRHLLGRKPGAQEIFWYDYPACDSNINAETIIGLVRVIPLAPKDVVPTNLKNEKTLFVKLSWNEKKFRPLSSELFAELNKPQESAAKCQKPVRAKSKSAESPSWTPAEHVAKRIESRHSASKSRQTPTHPLTPRARKRLELGNLGNPQMSQQTSCASLDSPGRIKRKVAFSEITSPSKRSQPDKLQTLSPALKAPEKTRETGLSYTEDDKKASPEHRIILRTRIAASKTIDIREERTLTPISGGQRSSVVPSVILKPENIKKRDAKEAKAQNEATSTPHRIRRKSSVLTMNRIRQQLRFLGNSKSDQEEKEILPAAEISDSSSDEEEASTPPLPRRAPRTVSRNLRSSLKSSLHTLTKVPKKSLKPRTPRCAAPQIRSRSLAAQEPASVLEEARLRLHVSAVPESLPCREQEFQDIYNFVESKLLDHTGGCMYISGVPGTGKTATVHEVIRCLQQAAQANDVPPFQYIEVNGMKLTEPHQVYVQILQKLTGQKATANHAAELLAKQFCTRGSPQETTVLLVDELDLLWTHKQDIMYNLFDWPTHKEARLVVLAIANTMDLPERIMMNRVSSRLGLTRMCFQPYTYSQLQQILRSRLKHLKAFEDDAIQLVARKVAALSGDARRCLDICRRATEICEFSQQKPDSPGLVTIAHSMEAVDEMFSSSYITAIKNSSVLEQSFLRAILAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSHLGSCRLLLVEPSRNDLLLRVRLNVSQDDVLYALKDE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q13415","disprot_id":"DP02072","ncbi_taxon_id":9606,"regions_counter":6,"creator":"ireményi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":673,"region_id":"DP02072r001","released":"2023_06","ec_id":"ECO:0006224","reference_html":"Structure of the active form of human origin recognition complex and its ATPase motor module. <i> Tocilj A, On KF, Yuan Z, Sun J, Elkayam E, Li H, Stillman B, Joshua-Tor L. </i> Elife, 2017","statement":[{"text":"The helix of ORC1 that includes residues 661–674 is disordered in our structure, but by homology to ORC4, they would contain the R-finger as R666 and the tether as R670 in the proper position.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":662,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"28112645","version":3,"ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","date":"2023-05-08T20:56:34.791Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5UJ7"},{"db":"PDB","id":"5UJM"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5957"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:813"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T12:01:09.946Z"}},{"start":471,"end":489,"reference_id":"28112645","reference_source":"pmid","reference_html":"Structure of the active form of human origin recognition complex and its ATPase motor module.  <i> Tocilj A, On KF, Yuan Z, Sun J, Elkayam E, Li H, Stillman B, Joshua-Tor L. </i> Elife, 2017","date":"2023-05-08T20:56:58.091Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5UJM"},{"db":"PDB","id":"5UJ7"}],"region_id":"DP02072r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:813"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5957"}],"statement":[{"text":"The PDB structures show this region lacks electron density, indicating it is disordered. ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T12:01:11.804Z"}}],"released":"2018_11","uniref100":"UniRef100_Q13415","date":"2018-08-24T12:44:35.000Z","acc":"Q13415","name":"Origin recognition complex subunit 1","length":861,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI0000130E56","genes":[{"name":{"value":"ORC1"},"synonyms":[{"value":"ORC1L"},{"value":"PARC1"}]}],"alphafold_very_low_content":0.3333333333333333,"disorder_content":0.036004645760743324,"disprot_consensus":{"full":[{"start":471,"end":489,"type":"D"},{"start":662,"end":673,"type":"D"}],"Structural state":[{"start":471,"end":489,"type":"D"},{"start":662,"end":673,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02840","name":"Prp18 domain","start":132,"end":244}],"gene3D":[{"start":79,"end":251,"id":"1.20.940.10","name":"Functional domain of the splicing factor Prp18"}]},"uniref50":"UniRef50_P33411","sequence":"MDLDLASILKGEISKKKKELANSKGVQPPCTEKFQPHESANIDETPRQVEQESTDEENLSDNQSDDIRTTISKLENRPERIQEAIAQDKTISVIIDPSQIGSTEGKPLLSMKCNLYIHEILSRWKASLEAYHPELFLDTKKALFPLLLQLRRNQLAPDLLISLATVLYHLQQPKEINLAVQSYMKLSIGNVAWPIGVTSVGIHARSAHSKIQGGRNAANIMIDERTRLWITSIKRLITFEEWYTSNHDSLA","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P33411","disprot_id":"DP02073","ncbi_taxon_id":559292,"regions_counter":1,"creator":"jlecle","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":217,"region_id":"DP02073r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of the functional domain of the splicing factor Prp18. <i> Jiang J, Horowitz DS, Xu RM. </i> Proc Natl Acad Sci U S A, 2000","statement":[{"text":"The main chain electron density is continuous except for a 20-aa segment (Thr-198–Ala-217), which was disordered in both of the molecules in the asymmetric unit and could not be modeled reliably. \nPart of loop-5, residues 198–217, is disordered and appears to be entirely exposed to the solvent.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jlecle","start":198,"term_ontology":"IDPO","curator_name":"Jeremy Y Leclercq","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0372-3277","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1DVK"}],"reference_id":"10737784","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P33411","date":"2018-08-24T12:52:20.000Z","acc":"P33411","name":"Pre-mRNA-splicing factor 18","length":251,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000053214","genes":[{"name":{"value":"PRP18"},"olnNames":[{"value":"YGR006W"}]}],"alphafold_very_low_content":0.199203187250996,"disorder_content":0.0796812749003984,"disprot_consensus":{"full":[{"start":198,"end":217,"type":"D"}],"Structural state":[{"start":198,"end":217,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01186","name":"Lysyl oxidase","start":213,"end":412}]},"uniref50":"UniRef50_P28300","sequence":"MRFAWTVLLLGPLQLCALVHCAPPAAGQQQPPREPPAAPGAWRQQIQWENNGQVFSLLSLGSQYQPQRRRDPGAAVPGAANASAQQPRTPILLIRDNRTAAARTRTAGSSGVTAGRPRPTARHWFQAGYSTSRAREAGASRAENQTAPGEVPALSNLRPPSRVDGMVGDDPYNPYKYSDDNPYYNYYDTYERPRPGGRYRPGYGTGYFQYGLPDLVADPYYIQASTYVQKMSMYNLRCAAEENCLASTAYRADVRDYDHRVLLRFPQRVKNQGTSDFLPSRPRYSWEWHSCHQHYHSMDEFSHYDLLDANTQRRVAEGHKASFCLEDTSCDYGYHRRFACTAHTQGLSPGCYDTYGADIDCQWIDITDVKPGNYILKVSVNPSYLVPESDYTNNVVRCDIRYTGHHAYASGCTISPY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P28300","disprot_id":"DP02075","ncbi_taxon_id":9606,"regions_counter":8,"creator":"mlambrughi","regions":[{"start":22,"end":168,"reference_id":"30082873","reference_source":"pmid","reference_html":"Insights into the structure and dynamics of lysyl oxidase propeptide, a flexible protein with numerous partners. <i> Vallet SD, Miele AE, Uciechowska-Kaczmarzyk U, Liwo A, Duclos B, Samsonov SA, Ricard-Blum S. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP02075r003","statement":[{"text":"Circular dichroism spectra of LOX-PP showed a single minimum near 200 nm, which is characteristic of an intrinsically disordered protein (IDP) (Fig. 2a). ","type":"Results"},{"text":"The presence of intrinsic disorder has been confirmed experimentally by CD and SAXS experiments. However, LOX-PP is partially structured as shown by deconvolution of CD spectra, which demonstrated the presence of a low amount of α-helix and β-strands.","type":"Discussion"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-18T13:29:15.480Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":22,"end":168,"reference_id":"30082873","reference_source":"pmid","reference_html":"Insights into the structure and dynamics of lysyl oxidase propeptide, a flexible protein with numerous partners. <i> Vallet SD, Miele AE, Uciechowska-Kaczmarzyk U, Liwo A, Duclos B, Samsonov SA, Ricard-Blum S. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP02075r004","statement":[{"text":"The experimental Rg/Rh ratio (1.2) was higher than 0.7, which indicates that LOX-PP behaves as a non-globular protein, and is likely to be extended, which is consistent with the presence of intrinsic disorder in LOX-PP. Furthermore, the Kratky plot was indicative of a non-globular natively unfolded molecule (Fig. 4c), and the normalized Kratky plot confirmed that LOX-PP is indeed flexible (Fig. 4d).","type":"Results"},{"text":"The presence of intrinsic disorder has been confirmed experimentally by CD and SAXS experiments. However, LOX-PP is partially structured as shown by deconvolution of CD spectra, which demonstrated the presence of a low amount of α-helix and β-strands.","type":"Discussion"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-18T13:30:22.389Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":22,"end":168,"reference_id":"30082873","reference_source":"pmid","reference_html":"Insights into the structure and dynamics of lysyl oxidase propeptide, a flexible protein with numerous partners. <i> Vallet SD, Miele AE, Uciechowska-Kaczmarzyk U, Liwo A, Duclos B, Samsonov SA, Ricard-Blum S. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"Q9H6X2-2","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P02452","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P12109","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q07507","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P01133","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P13605","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P02751","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q14766","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9Y4K0","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P08253","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P00747","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P15502","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P21980","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P08123","partner_start":null,"partner_end":null}],"region_id":"DP02075r005","statement":[{"text":"Potential partners of LOX-PP were screened by Surface Plasmon Resonance imaging (SPRi), SPR, and Bio-Layer Interferometry (BLI) (Supplementary Tables 6 and 7). We have identified 17 new partners of LOX-PP including four GAGs (chondroitin sulfate, dermatan sulfate, heparan sulfate, hyaluronan), collagen I, cross-linking and proteolytic enzymes (lysyl oxidase-like 2, transglutaminase-2, and MMP-2), one proteoglycan (fibromodulin), one matricryptin (anastellin), and the ectodomain of one membrane protein (Tumor Endothelial Marker-8 also known as anthrax receptor-137).","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-21T12:32:43.496Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":22,"end":168,"reference_id":"30082873","reference_source":"pmid","reference_html":"Insights into the structure and dynamics of lysyl oxidase propeptide, a flexible protein with numerous partners. <i> Vallet SD, Miele AE, Uciechowska-Kaczmarzyk U, Liwo A, Duclos B, Samsonov SA, Ricard-Blum S. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0036094","term_name":"small molecule binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"ChEBI","id":"37397","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"18376","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"28304","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"16336","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"28815","partner_start":null,"partner_end":null}],"region_id":"DP02075r006","statement":[{"text":"Potential partners of LOX-PP were screened by Surface Plasmon Resonance imaging (SPRi), SPR, and Bio-Layer Interferometry (BLI) (Supplementary Tables 6 and 7). We have identified 17 new partners of LOX-PP including four GAGs (chondroitin sulfate, dermatan sulfate, heparan sulfate, hyaluronan), collagen I, cross-linking and proteolytic enzymes (lysyl oxidase-like 2, transglutaminase-2, and MMP-2), one proteoglycan (fibromodulin), one matricryptin (anastellin), and the ectodomain of one membrane protein (Tumor Endothelial Marker-8 also known as anthrax receptor-137).","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-21T12:30:39.165Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":22,"end":168,"reference_id":"30082873","reference_source":"pmid","reference_html":"Insights into the structure and dynamics of lysyl oxidase propeptide, a flexible protein with numerous partners. <i> Vallet SD, Miele AE, Uciechowska-Kaczmarzyk U, Liwo A, Duclos B, Samsonov SA, Ricard-Blum S. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005645","ec_ontology":"ECO","ec_name":"interferometric reflectance imaging sensor evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P02751","partner_start":null,"partner_end":null}],"region_id":"DP02075r007","statement":[{"text":"Moreover, LOX-PP bound with very high affinity to tropoelastin and to plasminogen, and with high affinity to anastellin, a fragment of fibronectin (Table 3, Supplementary Fig. 8b).","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-21T12:32:40.804Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":22,"end":168,"reference_id":"30082873","reference_source":"pmid","reference_html":"Insights into the structure and dynamics of lysyl oxidase propeptide, a flexible protein with numerous partners. <i> Vallet SD, Miele AE, Uciechowska-Kaczmarzyk U, Liwo A, Duclos B, Samsonov SA, Ricard-Blum S. </i> Sci Rep, 2018","date":"2022-03-08T15:05:58.982Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","released":"2022_03","version":4,"region_id":"DP02075r008","statement":[{"text":" LOX-PP likely participates in collagen fibrillogenesis in association with fibromodulin, in fibronectin supramolecular assembly and in elastic fiber formation. Several LOX-PP partners such as fibrillar collagen I45, elastin10, fibronectin23, dermatopontin46,47, and fibromodulin48 bind to mature LOX, suggesting that both mature LOX and the propeptide are involved in ECM assembly and organization.","type":"Discussion"},{"text":"This suggests new roles for the propeptide in ECM assembly and cross-linking, cell-matrix adhesion, and in the regulation of EGF signaling pathways.","type":"Abstract"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"ChEBI","id":"37397","operator":"and","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"18376","operator":"or","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"28304","operator":"or","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"16336","operator":"or","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"28815","operator":"or","partner_start":null,"partner_end":null}]}],"released":"2018_11","uniref100":"UniRef100_P28300","date":"2018-08-24T12:58:56.000Z","acc":"P28300","name":"Protein-lysine 6-oxidase","length":417,"organism":"Homo sapiens","dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000033A7F","genes":[{"name":{"value":"LOX"}}],"alphafold_very_low_content":0.3501199040767386,"disorder_content":0.35251798561151076,"disprot_consensus":{"full":[{"start":22,"end":168,"type":"D"}],"Structural state":[{"start":22,"end":168,"type":"D"}],"Molecular function":[{"start":22,"end":168,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00027","name":"Cyclic nucleotide-binding domain","start":44,"end":121},{"id":"PF13545","name":"Crp-like helix-turn-helix domain","start":159,"end":229}],"gene3D":[{"start":38,"end":155,"id":"2.60.120.10","name":"Jelly Rolls"},{"start":156,"end":232,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}]},"uniref50":"UniRef50_Q89RK6","sequence":"MLTQTLKTQVINTQIGGKIAPPHQVSDQFGAITGHVGLVATEFSYRKDEEIYGEDEPAEYVYQVVTGAVRSYKLLSDGRRQIGAFHLPGDVFGLESGPSHRLAAEAIIDTSVRLVKRSSLEKAAGIDVQVARKLWAMTAGELRHAEDHMLLLGRKTAMERVATFLLEMDRRLAVAGMMALPMCRRDIGDYLGLTLETVSRALSQLHTQGILGFSGARQIVLRNRQRLHNLDA","taxonomy":["Bacteria","Proteobacteria","Alphaproteobacteria","Rhizobiales","Bradyrhizobiaceae","Bradyrhizobium"],"uniref90":"UniRef90_Q89RK6","disprot_id":"DP02076","ncbi_taxon_id":375,"regions_counter":1,"creator":"jlecle","regions":[{"region_id":"DP02076r001","ec_ontology":"ECO","end":37,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":1,"version":3,"statement":[{"text":"Due to the lack of electron density at the N terminus, the first 37 amino acids of FixK2(C183S)-His6 could not be modeled.","type":"Figure"}],"term_name":"disorder","reference_html":"The structure of Bradyrhizobium japonicum transcription factor FixK2 unveils sites of DNA binding and oxidation. <i> Bonnet M, Kurz M, Mesa S, Briand C, Hennecke H, Grütter MG. </i> J Biol Chem, 2013","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"23546876","date":"2024-02-07T17:50:38.783Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4I2O"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"ENA","id":"L07487.1","statements":[{"type":"Methods","text":"Unlabeled native and SeMet-labeled FixK2(C183S)-His6 were crystallized in the presence of 30-mer double-stranded target DNA from the FixK2-binding site of the fixN promoter (CCACCTATCTTGATTTCAATCAATTCCCCG, with the two binding half-sites underlined)."}]}]}],"released":"2018_11","uniref100":"UniRef100_Q89RK6","date":"2018-08-24T13:48:24.000Z","acc":"O69245","name":"FixK2 protein","length":232,"organism":"Bradyrhizobium japonicum","dataset":[],"UniParc":"UPI00000BC8E2","genes":[{"name":{"value":"fixK2","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAA06287.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA06287.1"}}]}}],"alphafold_very_low_content":0.10775862068965517,"disorder_content":0.15948275862068967,"disprot_consensus":{"full":[{"start":1,"end":37,"type":"D"}],"Structural state":[{"start":1,"end":37,"type":"D"}]}},{"features":{"pfam":[{"id":"PF07813","name":"LTXXQ motif family protein","start":47,"end":141}],"gene3D":[{"start":37,"end":147,"id":"1.20.120.1490","name":"1.20.120.1490"}]},"uniref50":"UniRef50_P77754","sequence":"MRKLTALFVASTLALGAANLAHAADTTTAAPADAKPMMHHKGKFGPHQDMMFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIITSDTFDKVKAEAQIAKMEEQRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLTERPAAKGKMPATAE","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P77754","disprot_id":"DP02077","ncbi_taxon_id":469008,"regions_counter":2,"creator":"jlecle","regions":[{"region_id":"DP02077r001","ec_ontology":"ECO","end":161,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":144,"version":3,"statement":[{"text":"Residues that were not observed in the electron density map due to disorder include N-terminal residues 24–52 and C-terminal residues 144–161 ​[Fig. 3(C)].","type":"Results"}],"term_name":"disorder","reference_html":"The crystal structure Escherichia coli Spy. <i> Kwon E, Kim DY, Gross CA, Gross JD, Kim KK. </i> Protein Sci, 2010","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"20799348","date":"2024-02-07T17:54:10.447Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3OEO"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"48775","entry_name":"cadmium(2+)"}]},{"start":24,"end":52,"reference_id":"20799348","reference_source":"pmid","reference_html":"The crystal structure Escherichia coli Spy. <i> Kwon E, Kim DY, Gross CA, Gross JD, Kim KK. </i> Protein Sci, 2010","date":"2024-02-07T17:54:57.569Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"3OEO"}],"region_id":"DP02077r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"48775","entry_name":"cadmium(2+)"}],"statement":[{"text":"Residues that were not observed in the electron density map due to disorder include N-terminal residues 24–52 and C-terminal residues 144–161 ​[Fig. 3(C)].","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_C6ECL5","date":"2018-08-24T14:36:14.000Z","acc":"C6ECL5","name":"Periplasmic chaperone Spy","length":161,"organism":"Escherichia coli (strain B / BL21-DE3)","dataset":["Stress response proteins"],"UniParc":"UPI0000673DFB","genes":[{"name":{"value":"spy"},"olnNames":[{"value":"ECBD_1902"}]}],"alphafold_very_low_content":0.18012422360248448,"disorder_content":0.2919254658385093,"disprot_consensus":{"full":[{"start":24,"end":52,"type":"D"},{"start":144,"end":161,"type":"D"}],"Structural state":[{"start":24,"end":52,"type":"D"},{"start":144,"end":161,"type":"D"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFGGDRGAPKRGSGKDSHHPARTAHYGSLPQKSHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQRPGFGYGGRASDYKSAHKGFKGVDAQGTLSKIFKLGGRDSRSGSPMARR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"","disprot_id":"DP02078","ncbi_taxon_id":9606,"regions_counter":13,"creator":"thorvath","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":171,"region_id":"DP02078r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Backbone dynamics of the 18.5 kDa isoform of myelin basic protein reveals transient alpha-helices and a calmodulin-binding site. <i> Libich DS, Harauz G. </i> Biophys J, 2008","statement":[{"text":"In aqueous solution, the classic 18.5 kDa isoform of MBP is primarily disordered, but has transient α-helices that are stabilized by membrane-mimetic conditions","type":"Conclusion"}],"term_id":"IDPO:0000002","curator_id":"thorvath","start":1,"term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"18326633","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":171,"term_name":"protein binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":", although the amphipathic α-helix represents the well-studied, canonical CaM-target, it has become recognized that CaM-binding sites and modes of interaction are quite diverse","type":"Results"}],"curator_id":"thorvath","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Horvath","reference_id":"18326633","version":3,"reference_html":"Backbone dynamics of the 18.5 kDa isoform of myelin basic protein reveals transient alpha-helices and a calmodulin-binding site. <i> Libich DS, Harauz G. </i> Biophys J, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP02078r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":171,"term_name":"lipid binding","start":1,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"These conditions were chosen to mimic the membrane environment of the myelin sheath, while keeping the system experimentally tractable to solution NMR methodology (7). We argue that 30% TFE stabilizes transient α-helices within the protein (83–85) on the basis of multiple, complementary studies on the immunodominant epitope of MBP","type":"Results"}],"curator_id":"thorvath","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Horvath","reference_id":"18326633","version":3,"reference_html":"Backbone dynamics of the 18.5 kDa isoform of myelin basic protein reveals transient alpha-helices and a calmodulin-binding site. <i> Libich DS, Harauz G. </i> Biophys J, 2008","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0008289","ec_id":"ECO:0006165","region_id":"DP02078r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":171,"reference_id":"7500383","reference_source":"pmid","reference_html":"Three isoforms of human myelin basic protein: purification and structure. <i> Deibler GE, Burlin TV, Stone AL. </i> J Neurosci Res, 1995","date":"2023-02-15T16:44:29.164Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP02078r004","statement":[{"text":"An activity check of the thrombin showed that HMBP-I, the nonphosphorylated 18.5 kDa protein, was completely digested by 2 hr (data not shown; described for bovine MBP-1 by Deibler et al., 1990).","type":"Results"}]},{"start":82,"end":99,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T14:09:40.901Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP02078r005","statement":[{"text":"The CSI analyses of our assignments, shown in Fig. 3, indicate a noticeable tendency of a central 10-residue segment of the polypeptide to adopt a helical conformation from residues 5′ to 14′, for samples in TFE-d2 (Fig. 3B) and in DPC-d38 (Fig. 3C), but not in KCl (Fig. 3A).","type":"Results"}],"cross_refs":[{"db":"BMRB","id":"6857"}]},{"start":86,"end":96,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T14:09:20.528Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP02078r006","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:162343649"}],"statement":[{"text":"The CSI analyses of our assignments, shown in Fig. 3, indicate a noticeable tendency of a central 10-residue segment of the polypeptide to adopt a helical conformation from residues 5′ to 14′, for samples in TFE-d2 (Fig. 3B) and in DPC-d38 (Fig. 3C), but not in KCl (Fig. 3A).","type":"Results"}],"states_connection":[{"source":"DP02078r005","target":"DP02078r007"}],"cross_refs":[{"db":"BMRB","id":"6857"}]},{"start":86,"end":96,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T14:09:14.048Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP02078r007","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:162343649"}],"statement":[{"text":"The CSI analyses of our assignments, shown in Fig. 3, indicate a noticeable tendency of a central 10-residue segment of the polypeptide to adopt a helical conformation from residues 5′ to 14′, for samples in TFE-d2 (Fig. 3B) and in DPC-d38 (Fig. 3C), but not in KCl (Fig. 3A).","type":"Results"}],"cross_refs":[{"db":"BMRB","id":"6857"}]},{"start":82,"end":99,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T14:14:22.554Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP02078r008","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:162343649"}],"statement":[{"text":"In aqueous solution (pure water, and 100 mm KCl, pH 6.5), the spectra indicated that the polypeptide had little or no regular secondary structure. In organic and membrane-mimetic conditions (30% TFE and 20 mm DPC, respectively), the spectra clearly indicated an α-helical conformation.","type":"Results"}]},{"start":82,"end":99,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T14:15:40.364Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP02078r009","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:162343649"}],"statement":[{"text":"In aqueous solution (pure water, and 100 mm KCl, pH 6.5), the spectra indicated that the polypeptide had little or no regular secondary structure. In organic and membrane-mimetic conditions (30% TFE and 20 mm DPC, respectively), the spectra clearly indicated an α-helical conformation.","type":"Results"}],"states_connection":[{"source":"DP02078r010","target":"DP02078r008"}]},{"start":82,"end":99,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T14:14:36.944Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP02078r010","statement":[{"text":"In aqueous solution (pure water, and 100 mm KCl, pH 6.5), the spectra indicated that the polypeptide had little or no regular secondary structure. In organic and membrane-mimetic conditions (30% TFE and 20 mm DPC, respectively), the spectra clearly indicated an α-helical conformation.","type":"Results"}]},{"start":86,"end":96,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T14:27:40.128Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006287","ec_ontology":"ECO","ec_name":"electron paramagnetic resonance evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"78018","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02078r011","statement":[{"text":"These results demonstrate that the polypeptide α helix forms distinct hydrophobic and electrostatic contacts with the DPC micelles, and are in agreement with the SDSL/EPR mapping and positioning of the α-helical model of this epitope of MBP on the surface of a lipid bilayer [6,7].","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":82,"end":99,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T14:30:25.597Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"78018","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02078r012","statement":[{"text":"In aqueous solution (pure water, and 100 mm KCl, pH 6.5), the spectra indicated that the polypeptide had little or no regular secondary structure. In organic and membrane-mimetic conditions (30% TFE and 20 mm DPC, respectively), the spectra clearly indicated an α-helical conformation.","type":"Results"},{"text":"Here, we focused on a conserved segment of MBP which is known to be a-helical when bound to a membrane, is a potential calmodulin-binding site, and also a primary immunodominant epitope in multiple sclerosis.","type":"Discussion"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":86,"end":96,"reference_id":"16420483","reference_source":"pmid","reference_html":"Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. <i> Farès C, Libich DS, Harauz G. </i> FEBS J, 2006","date":"2025-03-21T14:31:55.069Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"78018","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02078r013","statement":[{"text":"The CSI analyses of our assignments, shown in Fig. 3, indicate a noticeable tendency of a central 10-residue segment of the polypeptide to adopt a helical conformation from residues 5′ to 14′, for samples in TFE-d2 (Fig. 3B) and in DPC-d38 (Fig. 3C), but not in KCl (Fig. 3A).","type":"Results"},{"text":"Here, we focused on a conserved segment of MBP which is known to be a-helical when bound to a membrane, is a potential calmodulin-binding site, and also a primary immunodominant epitope in multiple sclerosis.","type":"Discussion"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"","date":"2018-08-24T14:51:19.000Z","acc":"P02686-5","name":"Isoform 5 of Myelin basic protein","length":171,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000002ADA6","genes":[{"name":{"value":"MBP"}}],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":81,"type":"D"},{"start":82,"end":99,"type":"T"},{"start":100,"end":171,"type":"D"}],"Structural state":[{"start":1,"end":171,"type":"D"}],"Molecular function":[{"start":1,"end":171,"type":"F"}],"Structural transition":[{"start":82,"end":99,"type":"T"}]}},{"features":{"pfam":[{"id":"PF15630","name":"CENP-S protein","start":14,"end":89}],"gene3D":[{"start":1,"end":106,"id":"1.10.20.10","name":"Histone, subunit A"}]},"uniref50":"UniRef50_E1BSW7","sequence":"MEAAGGEQRELLIQRLRAAVHYTTGCLCQDVAEDKGVLFSKQTVAAISEITFRQCENFARDLEMFARHAKRSTITSEDVKLLARRSNSLLKYITQKSDELASSNMEQKEKKKKKSSAAKGRKTEENETPVTESEDSNMA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Phasianinae","Gallus"],"uniref90":"UniRef90_E1BSW7","disprot_id":"DP02079","ncbi_taxon_id":9031,"regions_counter":1,"creator":"msalva","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":139,"region_id":"DP02079r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"CENP-T-W-S-X forms a unique centromeric chromatin structure with a histone-like fold. <i> Nishino T, Takeuchi K, Gascoigne KE, Suzuki A, Hori T, Oyama T, Morikawa K, Cheeseman IM, Fukagawa T. </i> Cell, 2012","statement":[{"text":". Boxes (a1 - a4), solid lines, and dashed\nlines indicate a helices, random coil regions, and disordered residues, respectively","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"msalva","start":107,"term_ontology":"IDPO","curator_name":"Marco Salvatore","reference_id":"22304917","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-5775-0417","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_E1BSW7","date":"2018-08-24T15:08:20.000Z","acc":"E1BSW7","name":"Centromere protein S","length":139,"organism":"Gallus gallus","dataset":[],"UniParc":"UPI0002032E94","genes":[{"name":{"value":"CENPS"},"synonyms":[{"value":"APITD1"}]}],"alphafold_very_low_content":0.050359712230215826,"disorder_content":0.23741007194244604,"disprot_consensus":{"full":[{"start":107,"end":139,"type":"D"}],"Structural state":[{"start":107,"end":139,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01298","name":"C-lobe and N-lobe beta barrels of Tf-binding protein B","start":315,"end":424}],"gene3D":[{"start":307,"end":427,"id":"2.40.160.90","name":"2.40.160.90"}]},"uniref50":"UniRef50_Q9JPH1","sequence":"MFERSVIAMACIFALSACGGGGGGSPDVKSADTLSKPAAPVVAEKETEVKEDAPQAGSQGQGAPSTQGSQDMAAVSAENTGNGGAATTDKPKNEDEGPQNDMLQNSAESANQTGNNQPADSSDSAPASNPAPANGGSNFGRVDLANGVLIDGPSQNITLTHCKGDSCNGDNLLDEEAPSKSEFENLNESERIEKYKKDGKSDKFTNLVATAVQANGTNKYVIIYKDKSASSSFARFRRSARSRRSLPAEMPLIPVNQADTLIVDGEAVSLTGHSGNIFAPEGNYRYLTYGAEKLPGGSYALRVQGEPAKGEMLAGTAVYNGEVLHFHTENGRPYPTRGRFAAKVDFGSKSVDGIIDSGDDLHMGTQKFKAAIDGNGFKGTWTENGGGDVSGRFYGPAGEEVAGKYSYRPTDAEKGGFGVFAGKKEQD","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"uniref90":"UniRef90_A0A425B1Z7","disprot_id":"DP02086","ncbi_taxon_id":487,"regions_counter":2,"creator":"msalva","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":274,"region_id":"DP02086r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structures of NHBA elucidate a broadly conserved epitope identified by a vaccine induced antibody. <i> Maritan M, Veggi D, Cozzi R, Dello Iacono L, Bartolini E, Lo Surdo P, Maruggi G, Spraggon G, Bottomley MJ, Malito E. </i> PLoS One, 2018","statement":[{"text":"The crystal structure of NHBA133-427 was solved by molecular replacement (MR) at 1.8 Å resolution (Table 1), revealing a β-hairpin and a β-barrel encompassing residues 275–427","type":"Results"},{"text":" In agreement with the fact that the N-terminal region of NHBA is predicted to lack secondary structures, and is thus annotated as an intrinsically disordered protein (IDP), we were unable to solve the structures of this region.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":133,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"6CUJ"}],"reference_id":"30133484","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:27:14.136Z"}},{"start":245,"end":275,"reference_id":"21965688","reference_source":"pmid","reference_html":"Structure of the C-terminal domain of Neisseria heparin binding antigen (NHBA), one of the main antigens of a novel vaccine against Neisseria meningitidis. <i> Esposito V, Musi V, de Chiara C, Veggi D, Serruto D, Scarselli M, Kelly G, Pizza M, Pastore A. </i> J Biol Chem, 2011","date":"2022-02-14T15:38:23.797Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":0,"cross_refs":[{"db":"PDB","id":"2LFU"}],"region_id":"DP02086r002","statement":[{"text":"The protein is connected to the membrane by a flexible linker, which leaves it mostly solvent exposed (10, 11).","type":"Introduction"},{"text":"We show that although the N terminus of NHBA is annotated as an intrinsically unfolded region by the most common prediction methods, the C terminus has all the features of an independently folded globular domain.","type":"Introduction"},{"text":"However, we realized very early on that the number of resonances present in the 15N-HSQC spectrum, which represents the protein fingerprint, contained at least 10–20% resonances more than expected, suggesting the presence in solution of different forms. Particularly diagnostic was, for instance, the resonance that resulted that corresponds to residue 287 (12.1 and 128.5 ppm), which was clearly doubled.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:27:18.799Z"}}],"released":"2018_11","uniref100":"UniRef100_Q9JPP1","date":"2018-08-24T15:42:10.000Z","acc":"Q9JPP1","name":"Gna2132","length":427,"organism":"Neisseria meningitidis","dataset":["Bacterial virulence-related proteins"],"UniParc":"UPI00000B35F0","genes":[{"name":{"value":"gna2132","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF42596.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF42596.1"}}]},"synonyms":[{"value":"nhba","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AFF59579.1","url":"https://www.ebi.ac.uk/ena/browser/view/AFF59579.1"}}]}]}],"alphafold_very_low_content":0.48711943793911006,"disorder_content":0.33489461358313816,"disprot_consensus":{"full":[{"start":133,"end":275,"type":"D"}],"Structural state":[{"start":133,"end":275,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00179","name":"Ubiquitin-conjugating enzyme","start":15,"end":154}],"gene3D":[{"start":5,"end":184,"id":"3.10.110.10","name":"Ubiquitin Conjugating Enzyme"}]},"uniref50":"UniRef50_P49427","sequence":"MARPLVPSSQKALLLELKGLQEEPVEGFRVTLVDEGDLYNWEVAIFGPPNTYYEGGYFKARLKFPIDYPYSPPAFRFLTKMWHPNIYETGDVCISILHPPVDDPQSGELPSERWNPTQNVRTILLSVISLLNEPNTFSPANVDASVMYRKWKESKGKDREYTDIIRKQVLGTKVDAERDGVKVPTTLAEYCVKTKAPAPDEGSDLFYDDYYEDGEVEEEADSCFGDDEDDSGTEES","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P49427","disprot_id":"DP02094","ncbi_taxon_id":9606,"regions_counter":4,"creator":"epapa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":236,"region_id":"DP02094r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Association of the disordered C-terminus of CDC34 with a catalytically bound ubiquitin. <i> Spratt DE, Shaw GS. </i> J Mol Biol, 2011","statement":[{"text":"The  (HSQC) spectrum of CDC34C (Fig. 1a) shows a collapsed amide peak profile in the 1 H dimension, denoting that the protein assumes a disordered conformation with little regular secondary structure.\nWe also confirmed the disordered state of CDC34C using the chemical shift index for Cα , Cβ, CO, and Hα resonances.\nTo further support the disordered state for the C-terminus of CDC34, we utilized  (NOE) experiments.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"epapa","start":183,"term_ontology":"IDPO","curator_name":"Elena Papaleo","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21296085","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":236,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Association of the disordered C-terminus of CDC34 with a catalytically bound ubiquitin. <i> Spratt DE, Shaw GS. </i> J Mol Biol, 2011","term_id":"GO:0005515","curator_id":"epapa","start":183,"term_ontology":"GO","curator_name":"Elena Papaleo","reference_id":"21296085","version":3,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP02094r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":115,"region_id":"DP02094r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Association of the disordered C-terminus of CDC34 with a catalytically bound ubiquitin. <i> Spratt DE, Shaw GS. </i> J Mol Biol, 2011","statement":[{"text":"Reduced 15N{1 H} NOEs were observed for residues\nV101–N115 corresponding to the acidic loop in\nCDC34. Several of these residues are not visible in\nthe crystal structure of CDC34.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"epapa","start":101,"term_ontology":"IDPO","curator_name":"Elena Papaleo","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21296085","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":115,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Association of the disordered C-terminus of CDC34 with a catalytically bound ubiquitin. <i> Spratt DE, Shaw GS. </i> J Mol Biol, 2011","term_id":"GO:0005515","curator_id":"epapa","start":101,"term_ontology":"GO","curator_name":"Elena Papaleo","reference_id":"21296085","version":3,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP02094r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P49427","date":"2018-08-24T20:53:16.000Z","acc":"P49427","name":"Ubiquitin-conjugating enzyme E2 R1","length":236,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000048D5E","genes":[{"name":{"value":"CDC34"},"synonyms":[{"value":"UBCH3"},{"value":"UBE2R1"}]}],"alphafold_very_low_content":0.13559322033898305,"disorder_content":0.2923728813559322,"disprot_consensus":{"full":[{"start":101,"end":115,"type":"D"},{"start":183,"end":236,"type":"D"}],"Structural state":[{"start":101,"end":115,"type":"D"},{"start":183,"end":236,"type":"D"}],"Molecular function":[{"start":101,"end":115,"type":"F"},{"start":183,"end":236,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00096","name":"Zinc finger, C2H2 type","start":357,"end":378},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":384,"end":406},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":412,"end":434},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":440,"end":462},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":541,"end":563},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":569,"end":591},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":597,"end":619},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":625,"end":647},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":653,"end":675},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":681,"end":703},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":709,"end":731},{"id":"PF02023","name":"SCAN domain","start":40,"end":127}],"gene3D":[{"start":36,"end":128,"id":"1.10.4020.10","name":"DNA breaking-rejoining enzymes"},{"start":620,"end":648,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":677,"end":701,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":436,"end":463,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":702,"end":734,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":566,"end":593,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":538,"end":565,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":649,"end":676,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":594,"end":619,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":409,"end":435,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":484,"end":509,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":357,"end":382,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":383,"end":408,"id":"3.30.160.60","name":"Classic Zinc Finger"},{"start":510,"end":537,"id":"3.30.160.60","name":"Classic Zinc Finger"}]},"uniref50":"UniRef50_P28698","sequence":"MRPAVLGSPDRAPPEDEGPVMVKLEDSEEEGEAALWDPGPEAARLRFRCFRYEEATGPQEALAQLRELCRQWLRPEVRSKEQMLELLVLEQFLGALPPEIQARVQGQRPGSPEEAAALVDGLRREPGGPRRWVTVQVQGQEVLSEKMEPSSFQPLPETEPPTPEPGPKTPPRTMQESPLGLQVKEESEVTEDSDFLESGPLAATQESVPTLLPEEAQRCGTVLDQIFPHSKTGPEGPSWREHPRALWHEEAGGIFSPGFALQLGSISAGPGSVSPHLHVPWDLGMAGLSGQIQSPSREGGFAHALLLPSDLRSEQDPTDEDPCRGVGPALITTRWRSPRGRSRGRPSTGGGVVRGGRCDVCGKVFSQRSNLLRHQKIHTGERPFVCSECGRSFSRSSHLLRHQLTHTEERPFVCGDCGQGFVRSARLEEHRRVHTGEQPFRCAECGQSFRQRSNLLQHQRIHGDPPGPGAKPPAPPGAPEPPGPFPCSECRESFARRAVLLEHQAVHTGDKSFGCVECGERFGRRSVLLQHRRVHSGERPFACAECGQSFRQRSNLTQHRRIHTGERPFACAECGKAFRQRPTLTQHLRVHTGEKPFACPECGQRFSQRLKLTRHQRTHTGEKPYHCGECGLGFTQVSRLTEHQRIHTGERPFACPECGQSFRQHANLTQHRRIHTGERPYACPECGKAFRQRPTLTQHLRTHRREKPFACQDCGRRFHQSTKLIQHQRVHSAE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P28698","disprot_id":"DP02096","ncbi_taxon_id":9606,"regions_counter":1,"creator":"epapa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":13,"region_id":"DP02096r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of the SCAN domain from the tumor suppressor protein MZF1. <i> Peterson FC, Hayes PL, Waltner JK, Heisner AK, Jensen DR, Sander TL, Volkman BF. </i> J Mol Biol, 2006","statement":[{"text":"MZF1 includes a novel N-terminal region that is 13 residues in length and shares no homology to any established protein interaction modules\nFurther inspection of the MZF1(1-128) spectrum identified ∼30 additional sharp\nresonances clustered around the random coil chemical shift value of ∼8.2 ppm. The presence of these resonances only in the longer construct suggests that the novel N-terminal region is unstructured","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"epapa","start":1,"term_ontology":"IDPO","curator_name":"Elena Papaleo","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"16950398","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P28698","date":"2018-08-24T21:24:44.000Z","acc":"P28698","name":"Myeloid zinc finger 1","length":734,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000161B62","genes":[{"name":{"value":"MZF1"},"synonyms":[{"value":"MZF"},{"value":"ZNF42"},{"value":"ZSCAN6"}]}],"alphafold_very_low_content":0.36648501362397823,"disorder_content":0.017711171662125342,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"D"}],"Structural state":[{"start":1,"end":13,"type":"D"}]}},{"features":{"pfam":[{"id":"PF05693","name":"Glycogen synthase","start":12,"end":683}],"gene3D":[{"start":10,"end":615,"id":"3.40.50.2000","name":"Glycogen Phosphorylase B;"},{"start":272,"end":600,"id":"3.40.50.2000","name":"Glycogen Phosphorylase B;"}]},"uniref50":"UniRef50_P27472","sequence":"MSRDLQNHLLFETATEVANRVGGIYSVLKSKAPITVAQYKDHYHLIGPLNKATYQNEVDILDWKKPEAFSDEMRPVQHALQTMESRGVHFVYGRWLIEGAPKVILFDLDSVRGYSNEWKGDLWSLVGIPSPENDFETNDAILLGYTVAWFLGEVAHLDSQHAIVAHFHEWLAGVALPLCRKRRIDVVTIFTTHATLLGRYLCASGSFDFYNCLESVDVDHEAGRFGIYHRYCIERAAAHSADVFTTVSQITAFEAEHLLKRKPDGILPNGLNVIKFQAFHEFQNLHALKKEKINDFVRGHFHGCFDFDLDNTLYFFIAGRYEYKNKGADMFIEALARLNYRLKVSGSKKTVVAFIVMPAKNNSFTVEALKGQAEVRALENTVHEVTTSIGKRIFDHAIRYPHNGLTTELPTDLGELLKSSDKVMLKRRILALRRPEGQLPPIVTHNMVDDANDLILNKIRQVQLFNSPSDRVKMIFHPEFLNANNPILGLDYDEFVRGCHLGVFPSYYEPWGYTPAECTVMGVPSITTNVSGFGAYMEDLIETNQAKDYGIYIVDRRFKAPDESVEQLVDYMEEFVKKTRRQRINQRNRTERLSDLLDWKRMGLEYVKARQLALRRGYPDQFRELVGEELNDSNMDALAGGKKLKVARPLSVPGSPRDLRSNSTVYMTPGDLGTLQEVNNADDYFSLGVNPAADDDDDGPYADDS","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P27472","disprot_id":"DP02097","ncbi_taxon_id":559292,"regions_counter":9,"creator":"npalopoli","regions":[{"region_id":"DP02097r001","ec_ontology":"ECO","end":705,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":640,"version":3,"statement":[{"text":"As previously described, residues C-terminal from position 639 are disordered and were not included in the models.","type":"Results"}],"term_name":"disorder","reference_html":"Structural basis for 2'-phosphate incorporation into glycogen by glycogen synthase. <i> Chikwana VM, Khanna M, Baskaran S, Tagliabracci VS, Contreras CJ, DePaoli-Roach A, Roach PJ, Hurley TD. </i> Proc Natl Acad Sci U S A, 2013","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24324135","date":"2024-02-22T14:03:29.094Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4KQ2"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala535Ser","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg589Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg592Ala","start":null,"end":null,"position":null},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17659","entry_name":"UDP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"37136","entry_name":"barium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46807","entry_name":"diethylene glycol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17665","entry_name":"alpha-D-glucose 6-phosphate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:191723"}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSMSRDLQNHLLFETATEVANRVGGIYSVLKSKAPITVAQYKDHYHLIGPLNKATYQNEVDILDWKKPEAFSDEMRPVQHALQTMESRGVHFVYGRWLIEGAPKVILFDLDSVRGYSNEWKGDLWSLVGIPSPENDFETNDAILLGYTVAWFLGEVAHLDSQHAIVAHFHEWLAGVALPLCRKRRIDVVTIFTTHATLLGRYLCASGSFDFYNCLESVDVDHEAGRFGIYHRYCIERAAAHSADVFTTVSQITAFEAEHLLKRKPDGILPNGLNVIKFQAFHEFQNLHALKKEKINDFVRGHFHGCFDFDLDNTLYFFIAGRYEYKNKGADMFIEALARLNYRLKVSGSKKTVVAFIVMPAKNNSFTVEALKGQAEVRALENTVHEVTTSIGKRIFDHAIRYPHNGLTTELPTDLGELLKSSDKVMLKRRILALRRPEGQLPPIVTHNMVDDANDLILNKIRQVQLFNSPSDRVKMIFHPEFLNANNPILGLDYDEFVRGCHLGVFPSYYEPWGYTPAECTVMGVPSITTNVSGFGSYMEDLIETNQAKDYGIYIVDRRFKAPDESVEQLVDYMEEFVKKTRRQRINQRNATEALSDLLDWKRMGLEYVKARQLALRRGYPDQFRELVGEELNDSNMDALAGGKKLKVARPLSVPGSPRDLRSNSTVYMTPGDLGTLQEVNNADDYFSLGVNPAADDDDDGPYADDS"},{"region_id":"DP02097r002","ec_ontology":"ECO","end":705,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":640,"version":3,"statement":[{"text":"The structure exhibited defined electron density for residues 2–277; 283–401and 415–639 in one monomer of the dimer and for residues 2–277; 283–401 and 415–626 in the other monomer. Both the monomers lacked interpretable electron density for the C-terminal 60–70 residues.","type":"Results"},{"text":"The X-ray structure of the mutated inhibited state structure of yGsy2p, shows the disordered region boundaries are 640-705.","type":"Curator statement"}],"term_name":"disorder","reference_html":"Redox Switch for the Inhibited State of Yeast Glycogen Synthase Mimics Regulation by Phosphorylation. <i> Mahalingan KK, Baskaran S, DePaoli-Roach AA, Roach PJ, Hurley TD. </i> Biochemistry, 2017","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27935293","date":"2024-02-22T13:56:37.905Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5SUL"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg589Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Overall structure of yeast Gsy2-R589A/R592A"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg592Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Overall structure of yeast Gsy2-R589A/R592A"}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46470","entry_name":"uridine 5'-monophosphate residue"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17659","entry_name":"UDP"}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSHMSRDLQNHLLFETATEVANRVGGIYSVLKSKAPITVAQYKDHYHLIGPLNKATYQNEVDILDWKKPEAFSDEMRPVQHALQTMESRGVHFVYGRWLIEGAPKVILFDLDSVRGYSNEWKGDLWSLVGIPSPENDFETNDAILLGYTVAWFLGEVAHLDSQHAIVAHFHEWLAGVALPLCRKRRIDVVTIFTTHATLLGRYLCASGSFDFYNCLESVDVDHEAGRFGIYHRYCIERAAAHSADVFTTVSQITAFEAEHLLKRKPDGILPNGLNVIKFQAFHEFQNLHALKKEKINDFVRGHFHGCFDFDLDNTLYFFIAGRYEYKNKGADMFIEALARLNYRLKVSGSKKTVVAFIVMPAKNNSFTVEALKGQAEVRALENTVHEVTTSIGKRIFDHAIRYPHNGLTTELPTDLGELLKSSDKVMLKRRILALRRPEGQLPPIVTHNMVDDANDLILNKIRQVQLFNSPSDRVKMIFHPEFLNANNPILGLDYDEFVRGCHLGVFPSYYEPWGYTPAECTVMGVPSITTNVSGFGSYMEDLIETNQAKDYGIYIVDRRFKAPDESVEQLVDYMEEFVKKTRRQRINQRNATEALSDLLDWKRMGLEYVKARQLALRRGYPDQFRELVGEELNDSNMDALAGGKKLKVARPLSVPGSPRDLRSNSTVYMTPGDLGTLQEVNNADDYFSLGVNPAADDDDDGPYADDS"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":705,"region_id":"DP02097r006","released":"2024_06","ec_id":"ECO:0006220","reference_html":"Structural basis for glucose-6-phosphate activation of glycogen synthase. <i> Baskaran S, Roach PJ, DePaoli-Roach AA, Hurley TD. </i> Proc Natl Acad Sci U S A, 2010","statement":[{"text":"In all cases, the subunits lack interpretable electron density C-terminal to residue 646, and both activity states of yeast glycogen synthase are tetramers (Fig. 1).","type":"Results"},{"text":"The X-ray structure of the basal state of Gsy2p, shows the disordered region boundaries are 640-705.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":640,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-21T13:20:00.865Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3NCH"}],"reference_id":"20876143","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg580Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Crystals of the R580/581/583A3 Gsy2p were grown by hanging drop vapor diffusion after combining 2 μL of protein at 3 mg/mL with 2 μL of reservoir solution containing 100 mM Tris-HCl, pH 8.0-8.5, 200 mM Li2SO4 and 18–22% PEG 3400 and were cryoprotected through slow introduction of a cryogenic solution containing 20% glycerol in the mother liquor."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg581Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Crystals of the R580/581/583A3 Gsy2p were grown by hanging drop vapor diffusion after combining 2 μL of protein at 3 mg/mL with 2 μL of reservoir solution containing 100 mM Tris-HCl, pH 8.0-8.5, 200 mM Li2SO4 and 18–22% PEG 3400 and were cryoprotected through slow introduction of a cryogenic solution containing 20% glycerol in the mother liquor."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg583Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Crystals of the R580/581/583A3 Gsy2p were grown by hanging drop vapor diffusion after combining 2 μL of protein at 3 mg/mL with 2 μL of reservoir solution containing 100 mM Tris-HCl, pH 8.0-8.5, 200 mM Li2SO4 and 18–22% PEG 3400 and were cryoprotected through slow introduction of a cryogenic solution containing 20% glycerol in the mother liquor."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala535Ser","start":null,"end":null,"position":null},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"His-tagged Gsy2 proteins were expressed in E.coli BL21(DE3) cells and purified by a two step procedure that included affinity chromatography on Ni2+-nitrilotriacetic acid-agarose (9) and ion exchange purification on Q-sepharose."}]}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSHMSRDLQNHLLFETATEVANRVGGIYSVLKSKAPITVAQYKDHYHLIGPLNKATYQNEVDILDWKKPEAFSDEMRPVQHALQTMESRGVHFVYGRWLIEGAPKVILFDLDSVRGYSNEWKGDLWSLVGIPSPENDFETNDAILLGYTVAWFLGEVAHLDSQHAIVAHFHEWLAGVALPLCRKRRIDVVTIFTTHATLLGRYLCASGSFDFYNCLESVDVDHEAGRFGIYHRYCIERAAAHSADVFTTVSQITAFEAEHLLKRKPDGILPNGLNVIKFQAFHEFQNLHALKKEKINDFVRGHFHGCFDFDLDNTLYFFIAGRYEYKNKGADMFIEALARLNYRLKVSGSKKTVVAFIVMPAKNNSFTVEALKGQAEVRALENTVHEVTTSIGKRIFDHAIRYPHNGLTTELPTDLGELLKSSDKVMLKRRILALRRPEGQLPPIVTHNMVDDANDLILNKIRQVQLFNSPSDRVKMIFHPEFLNANNPILGLDYDEFVRGCHLGVFPSYYEPWGYTPAECTVMGVPSITTNVSGFGSYMEDLIETNQAKDYGIYIVDRRFKAPDESVEQLVDYMEEFVKKTAAQAINQRNRTERLSDLLDWKRMGLEYVKARQLALRRGYPDQFRELVGEELNDSNMDALAGGKKLKVARPLSVPGSPRDLRSNSTVYMTPGDLGTLQEVNNADDYFSLGVNPAADDDDDGPYADDS"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":413,"region_id":"DP02097r007","released":"2024_06","ec_id":"ECO:0006220","reference_html":"Structural basis for glucose-6-phosphate activation of glycogen synthase. <i> Baskaran S, Roach PJ, DePaoli-Roach AA, Hurley TD. </i> Proc Natl Acad Sci U S A, 2010","statement":[{"text":"A 12-residue loop between these two helices (residues 401–412) is disordered in the basal state but becomes ordered as the interface changes in response to glucose-6-phosphate binding.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":402,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-21T13:24:55.088Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3NCH"}],"reference_id":"20876143","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg580Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Crystals of the R580/581/583A3 Gsy2p were grown by hanging drop vapor diffusion after combining 2 μL of protein at 3 mg/mL with 2 μL of reservoir solution containing 100 mM Tris-HCl, pH 8.0-8.5, 200 mM Li2SO4 and 18–22% PEG 3400 and were cryoprotected through slow introduction of a cryogenic solution containing 20% glycerol in the mother liquor."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg581Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Crystals of the R580/581/583A3 Gsy2p were grown by hanging drop vapor diffusion after combining 2 μL of protein at 3 mg/mL with 2 μL of reservoir solution containing 100 mM Tris-HCl, pH 8.0-8.5, 200 mM Li2SO4 and 18–22% PEG 3400 and were cryoprotected through slow introduction of a cryogenic solution containing 20% glycerol in the mother liquor."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg583Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Crystals of the R580/581/583A3 Gsy2p were grown by hanging drop vapor diffusion after combining 2 μL of protein at 3 mg/mL with 2 μL of reservoir solution containing 100 mM Tris-HCl, pH 8.0-8.5, 200 mM Li2SO4 and 18–22% PEG 3400 and were cryoprotected through slow introduction of a cryogenic solution containing 20% glycerol in the mother liquor."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala535Ser","start":null,"end":null,"position":null},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"is-tagged Gsy2 proteins were expressed in E.coli BL21(DE3) cells and purified by a two step procedure that included affinity chromatography on Ni2+-nitrilotriacetic acid-agarose (9) and ion exchange purification on Q-sepharose."}]}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSHMSRDLQNHLLFETATEVANRVGGIYSVLKSKAPITVAQYKDHYHLIGPLNKATYQNEVDILDWKKPEAFSDEMRPVQHALQTMESRGVHFVYGRWLIEGAPKVILFDLDSVRGYSNEWKGDLWSLVGIPSPENDFETNDAILLGYTVAWFLGEVAHLDSQHAIVAHFHEWLAGVALPLCRKRRIDVVTIFTTHATLLGRYLCASGSFDFYNCLESVDVDHEAGRFGIYHRYCIERAAAHSADVFTTVSQITAFEAEHLLKRKPDGILPNGLNVIKFQAFHEFQNLHALKKEKINDFVRGHFHGCFDFDLDNTLYFFIAGRYEYKNKGADMFIEALARLNYRLKVSGSKKTVVAFIVMPAKNNSFTVEALKGQAEVRALENTVHEVTTSIGKRIFDHAIRYPHNGLTTELPTDLGELLKSSDKVMLKRRILALRRPEGQLPPIVTHNMVDDANDLILNKIRQVQLFNSPSDRVKMIFHPEFLNANNPILGLDYDEFVRGCHLGVFPSYYEPWGYTPAECTVMGVPSITTNVSGFGSYMEDLIETNQAKDYGIYIVDRRFKAPDESVEQLVDYMEEFVKKTAAQAINQRNRTERLSDLLDWKRMGLEYVKARQLALRRGYPDQFRELVGEELNDSNMDALAGGKKLKVARPLSVPGSPRDLRSNSTVYMTPGDLGTLQEVNNADDYFSLGVNPAADDDDDGPYADDS"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":413,"term_name":"disorder to order","released":"2024_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural basis for glucose-6-phosphate activation of glycogen synthase. <i> Baskaran S, Roach PJ, DePaoli-Roach AA, Hurley TD. </i> Proc Natl Acad Sci U S A, 2010","statement":[{"text":"A 12-residue loop between these two helices (residues 401–412) is disordered in the basal state but becomes ordered as the interface changes in response to glucose-6-phosphate binding.","type":"Results"},{"text":"As might be expected for an allosteric ligand that induces such large conformational changes, the interactions between the enzyme and glucose-6-phosphate are extensive and involve residues from more than one subunit.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"vnugnes","start":402,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"20876143","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-21T15:22:40.600Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02097r008","ec_go":"EXP","disprot_namespace":"Structural transition","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg580Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Crystals of the R580/581/583A3 Gsy2p were grown by hanging drop vapor diffusion after combining 2 μL of protein at 3 mg/mL with 2 μL of reservoir solution containing 100 mM Tris-HCl, pH 8.0-8.5, 200 mM Li2SO4 and 18–22% PEG 3400 and were cryoprotected through slow introduction of a cryogenic solution containing 20% glycerol in the mother liquor."},{"type":"Curator statement","text":"This mutation is present in the protein basal state structure, PDB: 3NCH."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg581Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Crystals of the R580/581/583A3 Gsy2p were grown by hanging drop vapor diffusion after combining 2 μL of protein at 3 mg/mL with 2 μL of reservoir solution containing 100 mM Tris-HCl, pH 8.0-8.5, 200 mM Li2SO4 and 18–22% PEG 3400 and were cryoprotected through slow introduction of a cryogenic solution containing 20% glycerol in the mother liquor."},{"type":"Curator statement","text":"This mutation is present in the protein basal state structure, PDB: 3NCH."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg583Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Crystals of the R580/581/583A3 Gsy2p were grown by hanging drop vapor diffusion after combining 2 μL of protein at 3 mg/mL with 2 μL of reservoir solution containing 100 mM Tris-HCl, pH 8.0-8.5, 200 mM Li2SO4 and 18–22% PEG 3400 and were cryoprotected through slow introduction of a cryogenic solution containing 20% glycerol in the mother liquor."},{"type":"Curator statement","text":"This mutation is present in the protein basal state structure, PDB: 3NCH."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala535Ser","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"This mutation is present in both proteins structures."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"His-tagged Gsy2 proteins were expressed in E.coli BL21(DE3) cells and purified by a two step procedure that included affinity chromatography on Ni2+-nitrilotriacetic acid-agarose (9) and ion exchange purification on Q-sepharose."},{"type":"Curator statement","text":"This mutation is present in both proteins structures."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":null,"start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg592Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"In contrast, the R589A/R592A double mutant, whose glucose-6-phosphate activated structure is reported here, exhibited a specific activity and activity ratio similar to the phosphorylated enzymes and could be completely activated by the presence of glucose-6-phosphate (Table 2)."},{"type":"Curator statement","text":"This mutation is present in the glucose-6-phosphate activated state protein structure, PDB: 3NB0."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg589Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"In contrast, the R589A/R592A double mutant, whose glucose-6-phosphate activated structure is reported here, exhibited a specific activity and activity ratio similar to the phosphorylated enzymes and could be completely activated by the presence of glucose-6-phosphate (Table 2)."},{"type":"Curator statement","text":"This mutation is present in the glucose-6-phosphate activated state protein structure, PDB: 3NB0."}]}],"cross_refs":[{"db":"PDB","id":"3NCH"},{"db":"PDB","id":"3NB0"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","statements":[{"type":"Curator statement","text":"This molecule is present in the protein basal state structure, PDB: 3NCH."}],"entry_name":"sulfate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46807","statements":[{"type":"Curator statement","text":"This molecule is present in the glucose-6-phosphate activated state protein structure, PDB: 3NB0."}],"entry_name":"diethylene glycol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17665","statements":[{"type":"Curator statement","text":"This molecule is present in the glucose-6-phosphate activated state protein structure, PDB: 3NB0."}],"entry_name":"alpha-D-glucose 6-phosphate"}]},{"start":648,"end":705,"reference_id":"20876143","reference_source":"pmid","reference_html":"Structural basis for glucose-6-phosphate activation of glycogen synthase. <i> Baskaran S, Roach PJ, DePaoli-Roach AA, Hurley TD. </i> Proc Natl Acad Sci U S A, 2010","date":"2024-02-21T13:19:04.046Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg592Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"In contrast, the R589A/R592A double mutant, whose glucose-6-phosphate activated structure is reported here, exhibited a specific activity and activity ratio similar to the phosphorylated enzymes and could be completely activated by the presence of glucose-6-phosphate (Table 2)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg589Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"In contrast, the R589A/R592A double mutant, whose glucose-6-phosphate activated structure is reported here, exhibited a specific activity and activity ratio similar to the phosphorylated enzymes and could be completely activated by the presence of glucose-6-phosphate (Table 2)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala535Ser","start":null,"end":null,"position":null},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"His-tagged Gsy2 proteins were expressed in E.coli BL21(DE3) cells and purified by a two step procedure that included affinity chromatography on Ni2+-nitrilotriacetic acid-agarose (9) and ion exchange purification on Q-sepharose."}]}],"cross_refs":[{"db":"PDB","id":"3NB0"}],"region_id":"DP02097r009","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46807","entry_name":"diethylene glycol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17665","entry_name":"alpha-D-glucose 6-phosphate"}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSHMSRDLQNHLLFETATEVANRVGGIYSVLKSKAPITVAQYKDHYHLIGPLNKATYQNEVDILDWKKPEAFSDEMRPVQHALQTMESRGVHFVYGRWLIEGAPKVILFDLDSVRGYSNEWKGDLWSLVGIPSPENDFETNDAILLGYTVAWFLGEVAHLDSQHAIVAHFHEWLAGVALPLCRKRRIDVVTIFTTHATLLGRYLCASGSFDFYNCLESVDVDHEAGRFGIYHRYCIERAAAHSADVFTTVSQITAFEAEHLLKRKPDGILPNGLNVIKFQAFHEFQNLHALKKEKINDFVRGHFHGCFDFDLDNTLYFFIAGRYEYKNKGADMFIEALARLNYRLKVSGSKKTVVAFIVMPAKNNSFTVEALKGQAEVRALENTVHEVTTSIGKRIFDHAIRYPHNGLTTELPTDLGELLKSSDKVMLKRRILALRRPEGQLPPIVTHNMVDDANDLILNKIRQVQLFNSPSDRVKMIFHPEFLNANNPILGLDYDEFVRGCHLGVFPSYYEPWGYTPAECTVMGVPSITTNVSGFGSYMEDLIETNQAKDYGIYIVDRRFKAPDESVEQLVDYMEEFVKKTRRQRINQRNATEALSDLLDWKRMGLEYVKARQLALRRGYPDQFRELVGEELNDSNMDALAGGKKLKVARPLSVPGSPRDLRSNSTVYMTPGDLGTLQEVNNADDYFSLGVNPAADDDDDGPYADDS","statement":[{"text":"In all cases, the subunits lack interpretable electron density C-terminal to residue 646, and both activity states of yeast glycogen synthase are tetramers (Fig. 1).","type":"Results"},{"text":"The X-ray structure of the glucose-6-phosphate activated state of Gsy2p, shows the disordered region boundaries are 648-705","type":"Curator statement"}]}],"released":"2018_11","uniref100":"UniRef100_P27472","date":"2018-08-24T21:31:57.000Z","acc":"P27472","name":"Glycogen [starch] synthase isoform 2","length":705,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI00001683A4","genes":[{"name":{"value":"GSY2"},"orfNames":[{"value":"L8479.8"}],"olnNames":[{"value":"YLR258W"}]}],"alphafold_very_low_content":0.08085106382978724,"disorder_content":0.11063829787234042,"disprot_consensus":{"full":[{"start":402,"end":413,"type":"T"},{"start":640,"end":705,"type":"D"}],"Structural state":[{"start":402,"end":413,"type":"D"},{"start":640,"end":705,"type":"D"}],"Structural transition":[{"start":402,"end":413,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00179","name":"Ubiquitin-conjugating enzyme","start":8,"end":158}],"gene3D":[{"start":2,"end":165,"id":"3.10.110.10","name":"Ubiquitin Conjugating Enzyme"}]},"uniref50":"UniRef50_P60604","sequence":"MAGTALKRLMAEYKQLTLNPPEGIVAGPMNEENFFEWEALIMGPEDTCFEFGVFPAILSFPLDYPLSPPKMRFTCEMFHPNIYPDGRVCISILHAPGDDPMGYESSAERWSPVQSVEKILLSVVSMLAEPNDESGANVDASKMWRDDREQFYKIAKQIVQKSLGL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P60604","disprot_id":"DP02100","ncbi_taxon_id":9606,"regions_counter":1,"creator":"epapa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":109,"region_id":"DP02100r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure and dynamics of human ubiquitin conjugating enzyme Ube2g2. <i> Ju T, Bocik W, Majumdar A, Tolman JR. </i> Proteins, 2010","statement":[{"text":"the 13-residue insertion (residues 95–107) and the loop spanning residues 130–135. These loops are in fact very poorly defined in the NMR structural ensemble, with an average backbone RMSD (from the closest to mean NMR model) of 1.8 A˚ for residues 96–109 and 1.07 A˚ for residues 130–135. The poor definition\nof the insert loop and the 130s loop  clearly arises from the near absence of long range NOE.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"epapa","start":95,"term_ontology":"IDPO","curator_name":"Elena Papaleo","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2KLY"}],"reference_id":"20014027","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P60604","date":"2018-08-24T21:48:00.000Z","acc":"P60604","name":"Ubiquitin-conjugating enzyme E2 G2","length":165,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000027925","genes":[{"name":{"value":"UBE2G2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:12483","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:12483"}}]},"synonyms":[{"value":"UBC7","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"23223569","url":"http://www.ncbi.nlm.nih.gov/pubmed/23223569","alternativeUrl":"https://europepmc.org/abstract/MED/23223569"}}]}]}],"alphafold_very_low_content":0,"disorder_content":0.09090909090909091,"disprot_consensus":{"full":[{"start":95,"end":109,"type":"D"}],"Structural state":[{"start":95,"end":109,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02482","name":"Sigma 54 modulation protein / S30EA ribosomal protein","start":5,"end":99},{"id":"PF16321","name":"Sigma 54 modulation/S30EA ribosomal protein C terminus","start":130,"end":184}],"gene3D":[{"start":142,"end":187,"id":"3.30.505.50","name":"Sigma 54 modulation/S30EA ribosomal protein, C-terminal domain"},{"start":3,"end":104,"id":"3.30.160.100","name":"Ribosome hibernation promotion factor-like"}]},"uniref50":"UniRef50_P47908","sequence":"MKLLIQGNNITVTEAIHDYVEEKVERAVKHFQNLTTKVDVHLSVARNARITNKHKAEVTVYANGTVIRAQEGSENLYASIDLVADKIARQLRKYKERIQDKQHGNVKTSEIVEDKPVEENLIGDRAPELPSEVLRMKYFAMPPMAIEDALEQLQLVDHDFYMFRNKDTDEINVIYIRNHGGYGVIQPHQAS","taxonomy":["Bacteria","Cyanobacteria","Synechococcales","Merismopediaceae","Synechocystis","unclassified Synechocystis"],"uniref90":"UniRef90_P74518","disprot_id":"DP02105","ncbi_taxon_id":1111708,"regions_counter":7,"creator":"eficho","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":191,"region_id":"DP02105r001","released":"2024_06","ec_id":"ECO:0007013","reference_html":"The Cyanobacterial Ribosomal-Associated Protein LrtA from <i>Synechocystis</i> sp. PCC 6803 Is an Oligomeric Protein in Solution with Chameleonic Sequence Properties. <i> Contreras LM, Sevilla P, Cámara-Artigas A, Hernández-Cifre JG, Rizzuti B, Florencio FJ, Muro-Pastor MI, García de la Torre J, Neira JL. </i> Int J Mol Sci, 2018","statement":[{"text":"Our modelling and molecular dynamics (MD) simulations indicate that the protein adopted the same fold observed in other members of the HPF family (β-α-β-β-β-α) at its N-terminal region (residues 1–100), whereas the C terminus (residues 100–197) appeared disordered and collapsed, supporting the overall percentage of overall secondary structure obtained by CD deconvolution.","type":"Abstract"},{"text":"The first-half of LrtA sequence (residues 1–100) more distinctly belonged to the region occupied by ordered polypeptides. In contrast, the second-half (residues 100–191) fell in the region of the diagram that is populated by IDPs, although also accessible to some well-folded proteins.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":100,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"combinatorial experimental and author inference evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-20T16:45:53.654Z","reference_source":"pmid","term_name":"disorder","reference_id":"29937518","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":102,"end":191,"reference_id":"30563168","reference_source":"pmid","reference_html":"The C Terminus of the Ribosomal-Associated Protein LrtA Is an Intrinsically Disordered Oligomer. <i> Neira JL, Giudici AM, Hornos F, Arbe A, Rizzuti B. </i> Int J Mol Sci, 2018","date":"2025-04-22T13:55:17.258Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006196","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The final construct contained an N-terminal His-tag to allow for purification (MGSSHHHHHHSSGPQQGLR), and had the overall sequence: MGSSHHHHHHSSGPQQGLRQHGNVKTSEIVEDKPVEENLIGDRA\nPELPSEVLRMKYFAMPPMAIEDALEQLQLVDHDFYMFRNKDTDEINVIYIRNHGGYGVIQPHQAS."}]}],"region_id":"DP02105r002","statement":[{"text":"The NMR spectrum showed significant broadening in all the signals. On the basis of the results of the other techniques (see below in this section, and later in Section 2.2), this could be due to the presence of conformational exchange (equilibria) among protein species with different self-associated order. However, given the mobility of the protein (see MD simulations results, below in this section), we cannot exclude that the broadening observed could be due to conformational exchange in a single protein species. Therefore, we can conclude from the NMR spectrum that C-LrtA was disordered.","type":"Results"},{"text":"The intrinsically disordered nature of C-LrtA was suggested by several pieces of evidence: (i) the lack of dispersion in NMR spectra (Figure 1); (ii) the shape (Figure 2A) and the deconvolution of far-UV CD spectrum; (iii) the absence of all-or-none co-operative transitions in the thermal and chemical denaturations (Figure 2B,C); and (iv) a model of the structure without the His-tag obtained with MD simulation (Figure 3).","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-05-14T15:50:11.521Z"}},{"start":102,"end":191,"reference_id":"30563168","reference_source":"pmid","reference_html":"The C Terminus of the Ribosomal-Associated Protein LrtA Is an Intrinsically Disordered Oligomer. <i> Neira JL, Giudici AM, Hornos F, Arbe A, Rizzuti B. </i> Int J Mol Sci, 2018","date":"2025-04-22T13:57:26.804Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The final construct contained an N-terminal His-tag to allow for purification (MGSSHHHHHHSSGPQQGLR), and had the overall sequence: MGSSHHHHHHSSGPQQGLRQHGNVKTSEIVEDKPVEENLIGDRA\nPELPSEVLRMKYFAMPPMAIEDALEQLQLVDHDFYMFRNKDTDEINVIYIRNHGGYGVIQPHQAS."}]}],"region_id":"DP02105r003","statement":[{"text":"The intrinsically disordered nature of C-LrtA was suggested by several pieces of evidence: (i) the lack of dispersion in NMR spectra (Figure 1); (ii) the shape (Figure 2A) and the deconvolution of far-UV CD spectrum; (iii) the absence of all-or-none co-operative transitions in the thermal and chemical denaturations (Figure 2B,C); and (iv) a model of the structure without the His-tag obtained with MD simulation (Figure 3).","type":"Results"},{"text":"Therefore, we can conclude from the far-UV CD data that C-LrtA was disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-05-14T15:50:07.929Z"}},{"start":102,"end":191,"reference_id":"30563168","reference_source":"pmid","reference_html":"The C Terminus of the Ribosomal-Associated Protein LrtA Is an Intrinsically Disordered Oligomer. <i> Neira JL, Giudici AM, Hornos F, Arbe A, Rizzuti B. </i> Int J Mol Sci, 2018","date":"2025-06-08T19:58:44.941Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The final construct contained an N-terminal His-tag to allow for purification (MGSSHHHHHHSSGPQQGLR), and had the overall sequence: MGSSHHHHHHSSGPQQGLRQHGNVKTSEIVEDKPVEENLIGDRA\nPELPSEVLRMKYFAMPPMAIEDALEQLQLVDHDFYMFRNKDTDEINVIYIRNHGGYGVIQPHQAS."}]}],"region_id":"DP02105r004","statement":[{"text":"Fluorescence spectra of C-LrtA showed a maximum at 307 nm, corresponding to its 4 tyrosine residues [20,21]. We carried out GdmCl denaturations by following the <λ> (at two different C-LrtA concentrations) after excitation at 280 nm. At both protein concentrations, we observed a linear decrease in the <λ> as the concentration of chemical denaturant was increased (Figure 2B, right axis, red circles). We could not fit these data to the linear extrapolation model, as fitting led to thermodynamic parameters (m- or [GdmCl]1/2-values) with non-physical meaning (i.e., either negative values or values higher than the protein concentration explored). A similar linear tendency was observed in thermal denaturations (Figure 2C, right axis, red circles). Therefore, we can conclude from the fluorescence data that C-LrtA was disordered.","type":"Results"},{"text":"The intrinsically disordered nature of C-LrtA was suggested by several pieces of evidence: (i) the lack of dispersion in NMR spectra (Figure 1); (ii) the shape (Figure 2A) and the deconvolution of far-UV CD spectrum; (iii) the absence of all-or-none co-operative transitions in the thermal and chemical denaturations (Figure 2B,C); and (iv) a model of the structure without the His-tag obtained with MD simulation (Figure 3).","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T21:53:45.427Z"}},{"start":102,"end":191,"reference_id":"30563168","reference_source":"pmid","reference_html":"The C Terminus of the Ribosomal-Associated Protein LrtA Is an Intrinsically Disordered Oligomer. <i> Neira JL, Giudici AM, Hornos F, Arbe A, Rizzuti B. </i> Int J Mol Sci, 2018","date":"2025-04-22T14:06:21.860Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006301","ec_ontology":"ECO","ec_name":"protein thermal shift assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The final construct contained an N-terminal His-tag to allow for purification (MGSSHHHHHHSSGPQQGLR), and had the overall sequence: MGSSHHHHHHSSGPQQGLRQHGNVKTSEIVEDKPVEENLIGDRA\nPELPSEVLRMKYFAMPPMAIEDALEQLQLVDHDFYMFRNKDTDEINVIYIRNHGGYGVIQPHQAS."}]}],"region_id":"DP02105r005","statement":[{"text":"The intrinsically disordered nature of C-LrtA was suggested by several pieces of evidence: (i) the lack of dispersion in NMR spectra (Figure 1); (ii) the shape (Figure 2A) and the deconvolution of far-UV CD spectrum; (iii) the absence of all-or-none co-operative transitions in the thermal and chemical denaturations (Figure 2B,C); and (iv) a model of the structure without the His-tag obtained with MD simulation (Figure 3).","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-05-14T15:50:06.332Z"}},{"start":102,"end":191,"reference_id":"30563168","reference_source":"pmid","reference_html":"The C Terminus of the Ribosomal-Associated Protein LrtA Is an Intrinsically Disordered Oligomer. <i> Neira JL, Giudici AM, Hornos F, Arbe A, Rizzuti B. </i> Int J Mol Sci, 2018","date":"2025-04-22T14:09:45.252Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The final construct contained an N-terminal His-tag to allow for purification (MGSSHHHHHHSSGPQQGLR), and had the overall sequence: MGSSHHHHHHSSGPQQGLRQHGNVKTSEIVEDKPVEENLIGDRA\nPELPSEVLRMKYFAMPPMAIEDALEQLQLVDHDFYMFRNKDTDEINVIYIRNHGGYGVIQPHQAS."}]}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P74518","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02105r006","statement":[{"text":"The experiments with C-LrtA indicate a Rg ≈ 26 Å with a υ ≈ 0.33, close to a compact species value, but with a value of Rg larger than that of a well-folded protein (Section 4, Figure 4C), which is within the range observed for unfolded polypeptide chains [27]. We obtained a good agreement with the expected Guinier regime at low Q values, indicating that, although the protein was self-associated, the size of the C-LrtA species was relatively small.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-05-14T15:49:59.803Z"}},{"start":102,"end":191,"reference_id":"30563168","reference_source":"pmid","reference_html":"The C Terminus of the Ribosomal-Associated Protein LrtA Is an Intrinsically Disordered Oligomer. <i> Neira JL, Giudici AM, Hornos F, Arbe A, Rizzuti B. </i> Int J Mol Sci, 2018","date":"2025-04-22T14:10:21.851Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The final construct contained an N-terminal His-tag to allow for purification (MGSSHHHHHHSSGPQQGLR), and had the overall sequence: MGSSHHHHHHSSGPQQGLRQHGNVKTSEIVEDKPVEENLIGDRA\nPELPSEVLRMKYFAMPPMAIEDALEQLQLVDHDFYMFRNKDTDEINVIYIRNHGGYGVIQPHQAS."}]}],"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P74518","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02105r007","statement":[{"text":"The protein species in the fastest migrating band corresponded to an apparent molecular weight of 33 kDa (close to the molecular weight of a dimer, and similar to that observed at the most diluted protein concentration in the SEC experiments). On the other hand, the other band corresponded to an apparent molecular weight of 66 kDa, denoting a pentamer. Our results also suggest that increasing the amount of SDS (well-below the concentration used in denaturing SDS-PAGE gels: 33 mM [28]) had significant effects on the population of self-associated C-LrtA species: the larger the proportion of SDS, the higher the amount of self-associated species detected (the critic micellar concentration of SDS is 1.33 mM).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-05-14T15:50:14.399Z"}}],"released":"2018_11","uniref100":"UniRef100_P74518","date":"2018-08-24T22:06:54.000Z","acc":"P74518","name":"Ribosome hibernation promotion factor","length":191,"organism":"Synechocystis sp. (strain PCC 6803 / Kazusa)","dataset":[],"UniParc":"UPI000012E94A","genes":[{"name":{"value":"hpf","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00839","url":"https://hamap.expasy.org/unirule/MF_00839"}}]},"synonyms":[{"value":"lrtA"}],"olnNames":[{"value":"sll0947"}]}],"alphafold_very_low_content":0.1099476439790576,"disorder_content":0.4816753926701571,"disprot_consensus":{"full":[{"start":100,"end":191,"type":"D"}],"Structural state":[{"start":100,"end":191,"type":"D"}],"Molecular function":[{"start":102,"end":191,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00009","name":"Elongation factor Tu GTP binding domain","start":140,"end":328},{"id":"PF00679","name":"Elongation factor G C-terminus","start":840,"end":928},{"id":"PF03144","name":"Elongation factor Tu domain 2","start":504,"end":579},{"id":"PF03764","name":"Elongation factor G, domain IV","start":720,"end":837},{"id":"PF16004","name":"116 kDa U5 small nuclear ribonucleoprotein component N-terminus","start":4,"end":122}],"gene3D":[{"start":683,"end":960,"id":"3.30.230.10","name":"3.30.230.10"},{"start":678,"end":957,"id":"3.30.70.240","name":"3.30.70.240"},{"start":332,"end":436,"id":"3.90.1430.10","name":"Yeast translation eEF2 (G' domain)"},{"start":599,"end":674,"id":"3.30.70.870","name":"Elongation Factor G (Translational Gtpase), domain 3"},{"start":174,"end":581,"id":"2.40.30.10","name":"Translation factors"},{"start":138,"end":452,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_O94316","sequence":"MMEEDLYDEFGNYIGPENEEDEEELFPQAPSPTIAQVPSFEEVIPDEELEDVERAEEMALSHLEPQNAVVLHEDKQYYPSAEEVYGSNVDIMVQEQDTQPLSQPIIEPIRHKRIAIETTNVPDTVYKKEFLFGLLTGTDDVRSFIVAGHLHHGKSALLDLLVYYTHPDTKPPKRRSLRYTDTHYLERERVMSIKSTPLTLAVSDMKGKTFAFQCIDTPGHVDFVDEVAAPMAISDGVVLVVDVIEGVMINTTRIIKHAILHDMPIVLVLNKVDRLILELRLPPNDAYHKLRHVIDEVNDNICQISKDLKYRVSPELGNVCFASCDLGYCFTLSSFAKLYIDRHGGIDVDLFSKRLWGDIYFDSKTRKFAKQSLDGSGVRSFVHFILEPLYKLHTLTISDEAEKLKKHLSSFQIYLKPKDYLLDPKPLLQLICASFFGFPVGFVNAVTRHIPSPRENAARKASQSYIGPINSSIGKAILEMSREESAPLVMHVTKLYNTVDANNFYAFARVYSGQVKKGQKVKVLGENYSLEDEEDMVVAHIAEICVPCARYRLHVDGAVAGMLVLLGGVDNSISKTATIVSDNLKDDPYIFRPIAHMSESVFKVAVEPHNPSELPKLLDGLRKTNKSYPLSITKVEESGEHTIFGTGEMYMDCLLYDLRTLYSEIEIRVSDPVARFCETAVDTSSIKCFSDTPNKKNRITMVVEPLEKGISNDIENGKVNINWPQKRISEFFQKNYDWDLLASRSIWAFGPDDRGTNILRDDTLSTDVDKNVLNSVKEYIKQGFQWGTREGPLCDETIRNVNFRLMDVVLAPEQIYRGGGQIIPTARRVCYSSFLTASPRLMEPVYMVEVHAPADSLPIIYDLLTRRRGHVLQDIPRPGSPLYLVRALIPVIDSCGFETDLRVHTQGQAMCQMVFDHWQVVPGDPLDKSIKPKPLEPARGSDLARDFLIKTRRRKGLVEDVSTTRYFDQEMIDSLKEAGVVLSL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"uniref90":"UniRef90_O94316","disprot_id":"DP02109","ncbi_taxon_id":284812,"regions_counter":1,"creator":"epapa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":60,"region_id":"DP02109r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural and functional characterization of the N terminus of Schizosaccharomyces pombe Cwf10. <i> Livesay SB, Collier SE, Bitton DA, Bähler J, Ohi MD. </i> Eukaryot Cell, 2013","statement":[{"text":"Thus, the NMR analysis confirms  both the computational and CD analyses that the Cwf10 NTE contains regions of disorder, most likely in the first 60 amino acids (Fig. 6A).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"epapa","start":1,"term_ontology":"IDPO","curator_name":"Elena Papaleo","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24014766","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_O94316","date":"2018-08-24T22:33:22.000Z","acc":"O94316","name":"Pre-mRNA-splicing factor cwf10","length":984,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","dataset":[],"UniParc":"UPI000228F3E9","genes":[{"name":{"value":"cwf10"},"synonyms":[{"value":"snu114"},{"value":"spef2"}],"orfNames":[{"value":"SPBC215.12"}]}],"alphafold_very_low_content":0.049796747967479675,"disorder_content":0.06097560975609756,"disprot_consensus":{"full":[{"start":1,"end":60,"type":"D"}],"Structural state":[{"start":1,"end":60,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01467","name":"Cytidylyltransferase-like","start":80,"end":208}],"gene3D":[{"start":40,"end":267,"id":"3.40.50.620","name":"HUPs"}]},"uniref50":"UniRef50_P19836","sequence":"MDAQSSAKVNSRKRRKEVPGPNGATEEDGIPSKVQRCAVGLRQPAPFSDEIEVDFSKPYVRVTMEEACRGTPCERPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLAEHRIDFVAHDDIPYSSAGSDDVYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKKYHLQERVDKVKKKVKDVEEKSKEFVQKVEEKSIDLIQKWEEKSREFIGSFLEMFGPEGALKHMLKEGKGRMLQAISPKQSPSSSPTHERSPSPSFRWPFSGKTSPSSSPASLSRCKAVTCDISEDEED","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_P19836","disprot_id":"DP02118","ncbi_taxon_id":10116,"regions_counter":25,"creator":"npalopoli","regions":[{"region_id":"DP02118r001","ec_ontology":"ECO","end":39,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":1,"version":3,"statement":[{"text":"The refined structure at 2.2 Å resolution shows electron density for 353 residues of the possible 472 residues comprising the homodimer, with two bound CDP-choline molecules and 249 solvent molecules (Fig. 3A). Electron density is lacking for the N and C termini of both chains. Chain A accounts for residues 40–215 and chain B for residues 40–216. The crystal packing contacts allow sufficient space between adjacent stacked dimers to accommodate both N- and C-terminal regions as a disordered array.","type":"Results"}],"term_name":"disorder","reference_html":"Crystal structure of a mammalian CTP: phosphocholine cytidylyltransferase catalytic domain reveals novel active site residues within a highly conserved nucleotidyltransferase fold. <i> Lee J, Johnson J, Ding Z, Paetzel M, Cornell RB. </i> J Biol Chem, 2009","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19783652","date":"2024-02-27T15:15:43.227Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3HL4"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":"glycerol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16436","entry_name":"CDP-choline"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30751","entry_name":"formic acid"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":15,"region_id":"DP02118r002","released":"2024_06","ec_id":"ECO:0007691","reference_html":"Interdomain and membrane interactions of CTP:phosphocholine cytidylyltransferase revealed via limited proteolysis and mass spectrometry. <i> Bogan MJ, Agnes GR, Pio F, Cornell RB. </i> J Biol Chem, 2005","statement":[{"text":"Arg-C generated immediate cleavage at Arg12 and Arg14 in both CCTsol and CCTmem, showing for the first time that the N-terminal 15 residues of CCT are not a part of a compact fold (Fig. 8).","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-27T15:56:31.358Z","reference_source":"pmid","term_name":"disorder","reference_id":"15713672","ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP02118r004","ec_ontology":"ECO","end":236,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":217,"version":3,"statement":[{"text":"The refined structure at 2.2 Å resolution shows electron density for 353 residues of the possible 472 residues comprising the homodimer, with two bound CDP-choline molecules and 249 solvent molecules (Fig. 3A). Electron density is lacking for the N and C termini of both chains. Chain A accounts for residues 40–215 and chain B for residues 40–216. The crystal packing contacts allow sufficient space between adjacent stacked dimers to accommodate both N- and C-terminal regions as a disordered array.","type":"Results"}],"term_name":"disorder","reference_html":"Crystal structure of a mammalian CTP: phosphocholine cytidylyltransferase catalytic domain reveals novel active site residues within a highly conserved nucleotidyltransferase fold. <i> Lee J, Johnson J, Ding Z, Paetzel M, Cornell RB. </i> J Biol Chem, 2009","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19783652","date":"2024-02-27T15:16:37.478Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3HL4"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":"glycerol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16436","entry_name":"CDP-choline"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30751","entry_name":"formic acid"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":293,"region_id":"DP02118r006","released":"2024_06","ec_id":"ECO:0006204","reference_html":"Lipid-induced conformational switch in the membrane binding domain of CTP:phosphocholine cytidylyltransferase: a circular dichroism study. <i> Taneva S, Johnson JE, Cornell RB. </i> Biochemistry, 2003","statement":[{"text":"The CD spectra of domain M peptide in buffer or in the presence of OG were typical for predominantly random coil conformation as seen by the single negative maximum at 200 nm (Figure 6).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":237,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-26T15:29:46.947Z","reference_source":"pmid","term_name":"disorder","reference_id":"14529288","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","start":237,"end":237,"position":"Specific residue","statements":[{"type":"Methods","text":"A 57-mer peptide corresponding to residues 237−293 of rat liver CCTα was synthesized on an ABI model 431A peptide synthesizer using Fmoc chemistry by Dr. Krystyna Piotrowska at the University of British Columbia Peptide Service Laboratory (Vancouver, BC). The peptide was acetylated at the N-terminus and aminated at the C-terminus to eliminate the influence of the charged terminal groups."}]},{"term_id":"MOD:00674","term_name":"amidated residue","term_namespace":"Protein modification","start":293,"end":293,"position":"Specific residue","statements":[{"type":"Methods","text":"A 57-mer peptide corresponding to residues 237−293 of rat liver CCTα was synthesized on an ABI model 431A peptide synthesizer using Fmoc chemistry by Dr. Krystyna Piotrowska at the University of British Columbia Peptide Service Laboratory (Vancouver, BC). The peptide was acetylated at the N-terminus and aminated at the C-terminus to eliminate the influence of the charged terminal groups."}]}]},{"region_id":"DP02118r007","ec_ontology":"ECO","end":312,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":294,"version":3,"statement":[{"text":"Each AI helix interacts with both αE helices, and together they form an antiparallel four-helix bundle near the opening of the active site. The two AI segments have very similar conformations with a bend at Lys281. AI-2 is unraveled between residues Gln276 and Trp278. Each AI helix ends in a sharp turn at 294GP (the AI-turn), which interacts with loop L2 at the mouth of the active site (discussed below).","type":"Results"},{"text":"The initial solution for the CCT-312 diffraction set was obtained using CCT-236 structure (Protein Data Bank code 3HL4) as a search model. Subsequent to the solution of the 3-Å CCT-312(Δ32) structure (Protein Data Bank code 4MVC), it was used as the search model for the 8-Å data set for CCT-312, which afforded a better fit to the experimental density.","type":"Figure"}],"term_name":"disorder","reference_html":"Structural basis for autoinhibition of CTP:phosphocholine cytidylyltransferase (CCT), the regulatory enzyme in phosphatidylcholine synthesis, by its membrane-binding amphipathic helix. <i> Lee J, Taneva SG, Holland BW, Tieleman DP, Cornell RB. </i> J Biol Chem, 2014","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24275660","date":"2024-02-27T15:11:47.314Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4MVD"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16436","entry_name":"CDP-choline"}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSHMDAQSSAKVNSRKRRKEVPGPNGATEEDGIPSKVQRCAVGLRQPAPFSDEIEVDFSKPYVRVTMEEACRGTPCERPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLAEHRIDFVAHDDIPYSSAGSDDVYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKKYHLQERVDKVKKKVKDVEEKSKEFVQKVEEKSIDLIQKWEEKSREFIGSFLEMFGPEGALKHMLKEGKGRMLQ"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":367,"region_id":"DP02118r008","released":"2024_06","ec_id":"ECO:0007691","reference_html":"Identification of the membrane-binding domain of rat liver CTP:phosphocholine cytidylyltransferase using chymotrypsin proteolysis. <i> Craig L, Johnson JE, Cornell RB. </i> J Biol Chem, 1994","statement":[{"text":"Thus chymotrypsin digestion proceeds from the more accessible C terminus, which was predicted to be loosely folded. The 42-kDa band is not quantitatively converted into the lower molecular mass fragments. This is likely because progressive removal of the C terminus results in increased protease sensitivity of the N-terminal domain. The molecular mass determinations for each fragment are considered accurate to within 1 kDa. Given this error factor there are actually three possible cleavage sites for the 35-kDa fragment: Leu-299, Leu-303, and Leu-311.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":311,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-26T15:35:23.245Z","reference_source":"pmid","term_name":"disorder","reference_id":"8106370","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":367,"term_name":"phosphorylation display site","released":"2024_06","ec_name":"radioisotope quantification assay evidence used in manual assertion","reference_html":"Functions of the C-terminal domain of CTP: phosphocholine cytidylyltransferase. Effects of C-terminal deletions on enzyme activity, intracellular localization and phosphorylation potential. <i> Cornell RB, Kalmar GB, Kay RJ, Johnson MA, Sanghera JS, Pelech SL. </i> Biochem J, 1995","statement":[{"text":"CT was the major phosphoprotein visible in the COS cell extracts (Figure 3). The amount of 32P associated with the CT band decreased with progressive deletion of the C-terminus (Figure 3). The radioactivity associated with each CT band was examined using four separate gels from two independent labelling experiments. Substitution of Ser-362 with alanine resulted in a 21 + 60'/ reduction in label; deletion of the\nC-terminal 18 or 31 amino acids yielded a 26 + 14 % or 41 + 6%h reduction in 32P label respectively, and deletion of the C-terminal 55 amino acids eliminated all 32p label. This result suggests that the C-terminal 55 amino acids constitute the sole phosphorylation domain in CT and that there are multiple sites of phosphorylation.","type":"Results"}],"term_id":"IDPO:0000045","curator_id":"vnugnes","start":313,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"7654214","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-26T16:23:09.244Z","reference_source":"pmid","ec_id":"ECO:0007846","region_id":"DP02118r011","ec_go":"IDA","disprot_namespace":"Disorder function"},{"start":237,"end":293,"reference_id":"14529288","reference_source":"pmid","reference_html":"Lipid-induced conformational switch in the membrane binding domain of CTP:phosphocholine cytidylyltransferase: a circular dichroism study. <i> Taneva S, Johnson JE, Cornell RB. </i> Biochemistry, 2003","date":"2024-02-27T16:22:06.385Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02118r014","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"60479","entry_name":"lysophosphatidylcholine"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17517","entry_name":"phosphatidylglycerol"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"61995","entry_name":"lecithin"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16196","entry_name":"oleic acid"}],"statement":[{"text":"The CD spectra of domain M peptide in buffer or in the presence of OG were typical for predominantly random coil conformation as seen by the single negative maximum at 200 nm (Figure 6). However, in the presence of LPC/PG micelles, or vesicles of PC/OA or PG, the CD spectra were characteristic of α-helices (strong positive band at ∼195 nm; strong minima at ∼208 and ∼222 nm).","type":"Results"}]},{"start":237,"end":293,"reference_id":"14529288","reference_source":"pmid","reference_html":"Lipid-induced conformational switch in the membrane binding domain of CTP:phosphocholine cytidylyltransferase: a circular dichroism study. <i> Taneva S, Johnson JE, Cornell RB. </i> Biochemistry, 2003","date":"2024-02-27T16:18:05.873Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02118r015","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"60479","entry_name":"lysophosphatidylcholine"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17517","entry_name":"phosphatidylglycerol"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"61995 ","entry_name":"lecithin"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16196","entry_name":"oleic acid"}],"statement":[{"text":"The CD spectra of domain M peptide in buffer or in the presence of OG were typical for predominantly random coil conformation as seen by the single negative maximum at 200 nm (Figure 6). However, in the presence of LPC/PG micelles, or vesicles of PC/OA or PG, the CD spectra were characteristic of α-helices (strong positive band at ∼195 nm; strong minima at ∼208 and ∼222 nm).","type":"Results"},{"text":"The three activating lipid systems increased the α-helix content to a similar level of about 80% at the expense of β-strand, turn, and unordered, and nearly eliminated the β character from the spectra.","type":"Results"}],"states_connection":[{"source":"DP02118r006","target":"DP02118r014"}]},{"start":238,"end":299,"reference_id":"7654214","reference_source":"pmid","reference_html":"Functions of the C-terminal domain of CTP: phosphocholine cytidylyltransferase. Effects of C-terminal deletions on enzyme activity, intracellular localization and phosphorylation potential. <i> Cornell RB, Kalmar GB, Kay RJ, Johnson MA, Sanghera JS, Pelech SL. </i> Biochem J, 1995","date":"2024-02-27T16:20:29.078Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0004105","term_name":"choline-phosphate cytidylyltransferase activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IMP","region_id":"DP02118r016","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"61995","entry_name":"lecithin"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16196","entry_name":"oleic acid"}],"statement":[{"text":"The activities of the C-terminal mutants are shown in Table 1. Neither substitution of Ser-362 with alanine nor deletion of the final 18, 31 or 55 residues had an effect on the activity of CT in the presence or absence of activating vesicles (PC: oleic acid, 1: 1) using a standard assay [45]. These mutants all contain the complete amphipathic helix domain of CT (see Figure 1) and were stimulated 3-4-fold by anionic lipid vesicles (Table 1). On the other hand, the mutant missing the last 140 amino acids, including the amphipathic helix and eight residues of the conserved domain, had less than 10 % of the catalytic activity of the wild type in the presence of PC-oleic acid vesicles. T","type":"Results"},{"text":"Domain M, but not domain P, is required for enzyme activity, lipid responsiveness and lntracellular localization\n","type":"Discussion"}],"term_comment":"","term_def":"\"Catalysis of the reaction: CTP + choline phosphate = diphosphate + CDP-choline.\" [EC:2.7.7.15]","term_is_obsolete":false,"term_not_annotate":false},{"start":238,"end":299,"reference_id":"7654214","reference_source":"pmid","reference_html":"Functions of the C-terminal domain of CTP: phosphocholine cytidylyltransferase. Effects of C-terminal deletions on enzyme activity, intracellular localization and phosphorylation potential. <i> Cornell RB, Kalmar GB, Kay RJ, Johnson MA, Sanghera JS, Pelech SL. </i> Biochem J, 1995","date":"2024-02-26T16:18:08.163Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IMP","region_id":"DP02118r017","statement":[{"text":"The subcellular distribution of the A228 mutant was altered. Whereas the other mutants were distributed, according to activity measurements, in approximately the same manner as the wildtype CT (63 + 3 %, cytosol; 15 + 3 %, microsomes; 22 + 7 %, low speed pellet), less than 3 % of the A228 mutant activity was in the microsomal fraction. This result was confirmed when we used digitonin permeabilization to assess the intracellular distribution. In cells transfected with wild-type CT or any of the mutants other than A228, 60-70 % of the CT activity was found in the cell lysate (soluble or cytosolic fraction). On the other hand 86 % of the A228 activity was associated with the lysate (Table 1).\n","type":"Results"},{"text":"Domain M, but not domain P, is required for enzyme activity, lipid responsiveness and lntracellular localization\n","type":"Discussion"}],"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","term_is_obsolete":false,"term_not_annotate":false},{"start":271,"end":293,"reference_id":"24275660","reference_source":"pmid","reference_html":"Structural basis for autoinhibition of CTP:phosphocholine cytidylyltransferase (CCT), the regulatory enzyme in phosphatidylcholine synthesis, by its membrane-binding amphipathic helix. <i> Lee J, Taneva SG, Holland BW, Tieleman DP, Cornell RB. </i> J Biol Chem, 2014","date":"2024-02-27T16:19:28.521Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P19836","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02118r018","statement":[{"text":"Upon loss of the segment between residues 312 and 271, kcat values for the CCT soluble form transitioned from silenced (0.5 s−1) to the partially active rate (∼ 3 s−1) characteristic of CCT-236 (Fig. 1B). The construct ending at residue 271 showed a higher kcat than did CCT-255 or CCT-236, perhaps reflecting different consequences of specific truncation sites on protein dynamics. Loss of the AI segment was linked to a transition in the CTP Km from ∼9 to ∼5.5 mm (Fig. 1C). Thus, the presence of the AI segment suppresses kcat/Km by about 10-fold. However, the kinetic parameters of the full-length soluble enzyme were achieved only when the segment between residues 293 and 312 was intact. These results strengthen previous results implicating a key silencing role for the AI motif (16) but suggest additional participation of the flanking segment between residues 293 and 312.","type":"Results"}],"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17517","statements":[{"type":"Methods","text":"All CCT variants were analyzed using a standard assay (23, 25) in which substrate concentrations are optimal for WT CCT (16) in the absence or presence of egg PC/egg PG (1:1) sonicated vesicles (26)."}],"entry_name":"phosphatidylglycerol"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"61995","statements":[{"type":"Methods","text":"All CCT variants were analyzed using a standard assay (23, 25) in which substrate concentrations are optimal for WT CCT (16) in the absence or presence of egg PC/egg PG (1:1) sonicated vesicles (26)."}],"entry_name":"lecithin"}]},{"start":275,"end":295,"reference_id":"24275660","reference_source":"pmid","reference_html":"Structural basis for autoinhibition of CTP:phosphocholine cytidylyltransferase (CCT), the regulatory enzyme in phosphatidylcholine synthesis, by its membrane-binding amphipathic helix. <i> Lee J, Taneva SG, Holland BW, Tieleman DP, Cornell RB. </i> J Biol Chem, 2014","date":"2024-05-06T17:37:37.643Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Lys238Glu269del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"CCT-312(Δ32) missing 32 residues (residues 238–269) from both the non-conserved and polybasic sections of domain M readily crystallized in the presence of CDP-choline."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"cross_refs":[{"db":"PDB","id":"4MVC"}],"ec_go":"EXP","region_id":"DP02118r019","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16436","entry_name":null}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSHMDAQSSAKVNSRKRRKEVPGPNGATEEDGIPSKVQRCAVGLRQPAPFSDEIEVDFSKPYVRVTMEEACRGTPCERPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLAEHRIDFVAHDDIPYSSAGSDDVYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKSIDLIQKWEEKSREFIGSFLEMFGPEGALKHMLKEGKGRMLQ","statement":[{"text":"A CCT-312(Δ32) crystal generated a 3-Å resolution diffraction data set that was solved by molecular replacement using CCT-236 (Protein Data Bank code 3HL4) (see Table 1). The asymmetric unit was a dimer. The resolved portion of this dimer encompasses the catalytic domains and the AI segments of domain M (Fig. 3A).","type":"Results"},{"text":"Each AI helix interacts with both αE helices, and together they form an antiparallel four-helix bundle near the opening of the active site.","type":"Results"},{"text":"The AI positioning in the CCT-312(Δ32) structure is not an artifact of the large domain M deletion. A very similar AI-αE-L2 interaction is found in CCT-312 with no deletion.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a domain within the same polypeptide.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":312,"end":367,"reference_id":"15713672","reference_source":"pmid","reference_html":"Interdomain and membrane interactions of CTP:phosphocholine cytidylyltransferase revealed via limited proteolysis and mass spectrometry. <i> Bogan MJ, Agnes GR, Pio F, Cornell RB. </i> J Biol Chem, 2005","date":"2024-02-27T15:39:57.927Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007730","ec_ontology":"ECO","ec_name":"cleavage arrested development evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02118r020","statement":[{"text":"The PBAMs reveal that domain P in both CCT forms was highly accessible to both chymotrypsin and Arg-C.","type":"Results"}]},{"start":312,"end":367,"reference_id":"15713672","reference_source":"pmid","reference_html":"Interdomain and membrane interactions of CTP:phosphocholine cytidylyltransferase revealed via limited proteolysis and mass spectrometry. <i> Bogan MJ, Agnes GR, Pio F, Cornell RB. </i> J Biol Chem, 2005","date":"2024-02-27T15:42:37.849Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005527","ec_ontology":"ECO","ec_name":"matrix-assisted laser desorption/ionization time-of-flight mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02118r021","statement":[{"text":"For the peptide spanning the entire domain P, Gln312-Asp367, the masses matched for four, five, six, and seven phosphates. Our analysis did not enable identification of each phosphorylated site; however, the results (Table II) indicate a phosphorylation pattern that is very similar to that obtained by MacDonald and Kent (12). The phosphorylated serines are spread over the entire 50-residue domain.","type":"Results"}]},{"start":36,"end":69,"reference_id":"15713672","reference_source":"pmid","reference_html":"Interdomain and membrane interactions of CTP:phosphocholine cytidylyltransferase revealed via limited proteolysis and mass spectrometry. <i> Bogan MJ, Agnes GR, Pio F, Cornell RB. </i> J Biol Chem, 2005","date":"2024-02-27T16:22:28.427Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02118r022","sample":[{"term_id":"IDPO:00489","term_name":"interacting membrane","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17517","statements":[{"type":"Methods","text":"To prepare CCTmem, sonicated egg phosphatidylglycerol (PG) vesicles were prepared (18) and mixed at ≥100-fold molar excess over CCT 5 min prior to the initiation of proteolysis reactions."}],"entry_name":"phosphatidylglycerol"}],"statement":[{"text":"The low mass peptide data contributing to the PBAMs shown in Fig. 6 revealed enhanced accessibility of amino acids 41 and 59 in domain N of CCTmem and CCT236 (region II).","type":"Results"},{"text":"Two other important differences between CCTsol and CCTmem, evidenced from chymotrypsin digestion, were also revealed by Arg-C digestion: (i) Sites within domain N at Arg36, Arg42, Arg61, and Arg69 were cleaved to generate a variety of peptides in CCTmem, whereas none of these sites were cleaved in CCTsol for at least 10 min of digestion (Fig. 6C and Supplementary Fig. 1C). Thus the limited digestion pattern generated by two different proteases indicate that membrane binding increases the accessibility of the C-terminal side of domain N (Fig. 6, region II).","type":"Results"},{"text":"Because membrane binding exposes a region of domain N, but not domain C, we hypothesize that in the soluble form domain M of CCT interacts with the region of domain N that becomes exposed upon membrane binding of domain M.","type":"Discussion"}]},{"start":36,"end":69,"reference_id":"15713672","reference_source":"pmid","reference_html":"Interdomain and membrane interactions of CTP:phosphocholine cytidylyltransferase revealed via limited proteolysis and mass spectrometry. <i> Bogan MJ, Agnes GR, Pio F, Cornell RB. </i> J Biol Chem, 2005","date":"2024-02-27T16:21:09.265Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02118r023","sample":[{"term_id":"IDPO:00489","term_name":"interacting membrane","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17517","statements":[{"type":"Methods","text":"To prepare CCTmem, sonicated egg phosphatidylglycerol (PG) vesicles were prepared (18) and mixed at ≥100-fold molar excess over CCT 5 min prior to the initiation of proteolysis reactions."}],"entry_name":"phosphatidylglycerol"}],"statement":[{"text":"The low mass peptide data contributing to the PBAMs shown in Fig. 6 revealed enhanced accessibility of amino acids 41 and 59 in domain N of CCTmem and CCT236 (region II).","type":"Results"},{"text":"Two other important differences between CCTsol and CCTmem, evidenced from chymotrypsin digestion, were also revealed by Arg-C digestion: (i) Sites within domain N at Arg36, Arg42, Arg61, and Arg69 were cleaved to generate a variety of peptides in CCTmem, whereas none of these sites were cleaved in CCTsol for at least 10 min of digestion (Fig. 6C and Supplementary Fig. 1C). Thus the limited digestion pattern generated by two different proteases indicate that membrane binding increases the accessibility of the C-terminal side of domain N (Fig. 6, region II).","type":"Results"},{"text":"Because membrane binding exposes a region of domain N, but not domain C, we hypothesize that in the soluble form domain M of CCT interacts with the region of domain N that becomes exposed upon membrane binding of domain M.","type":"Discussion"}],"states_connection":[{"source":"DP02118r024","target":"DP02118r022"}]},{"start":36,"end":69,"reference_id":"15713672","reference_source":"pmid","reference_html":"Interdomain and membrane interactions of CTP:phosphocholine cytidylyltransferase revealed via limited proteolysis and mass spectrometry. <i> Bogan MJ, Agnes GR, Pio F, Cornell RB. </i> J Biol Chem, 2005","date":"2024-02-27T15:54:37.906Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02118r024","statement":[{"text":"Two other important differences between CCTsol and CCTmem, evidenced from chymotrypsin digestion, were also revealed by Arg-C digestion: (i) Sites within domain N at Arg36, Arg42, Arg61, and Arg69 were cleaved to generate a variety of peptides in CCTmem, whereas none of these sites were cleaved in CCTsol for at least 10 min of digestion (Fig. 6C and Supplementary Fig. 1C). Thus the limited digestion pattern generated by two different proteases indicate that membrane binding increases the accessibility of the C-terminal side of domain N (Fig. 6, region II).","type":"Results"}]},{"start":237,"end":293,"reference_id":"14529288","reference_source":"pmid","reference_html":"Lipid-induced conformational switch in the membrane binding domain of CTP:phosphocholine cytidylyltransferase: a circular dichroism study. <i> Taneva S, Johnson JE, Cornell RB. </i> Biochemistry, 2003","date":"2024-02-27T16:16:42.004Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"60479","operator":null,"partner_start":null,"partner_end":null},{"db":"ChEBI","id":"17517","operator":"or","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"61995","operator":"or","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"16196","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP02118r025","statement":[{"text":"The CD spectra of domain M peptide in buffer or in the presence of OG were typical for predominantly random coil conformation as seen by the single negative maximum at 200 nm (Figure 6). However, in the presence of LPC/PG micelles, or vesicles of PC/OA or PG, the CD spectra were characteristic of α-helices (strong positive band at ∼195 nm; strong minima at ∼208 and ∼222 nm).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_P19836","date":"2018-08-25T23:41:52.000Z","acc":"P19836","name":"Choline-phosphate cytidylyltransferase A","length":367,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI000012864C","genes":[{"name":{"value":"Pcyt1a"},"synonyms":[{"value":"Ctpct"},{"value":"Pcyt1"}]}],"alphafold_very_low_content":0.25885558583106266,"disorder_content":0.5994550408719346,"disprot_consensus":{"full":[{"start":1,"end":35,"type":"D"},{"start":36,"end":69,"type":"T"},{"start":217,"end":236,"type":"D"},{"start":237,"end":293,"type":"T"},{"start":294,"end":367,"type":"D"}],"Structural state":[{"start":1,"end":69,"type":"D"},{"start":217,"end":367,"type":"D"}],"Disorder function":[{"start":275,"end":295,"type":"F"},{"start":312,"end":367,"type":"F"}],"Structural transition":[{"start":36,"end":69,"type":"T"},{"start":237,"end":293,"type":"T"}],"Molecular function":[{"start":237,"end":299,"type":"F"}],"Biological process":[{"start":238,"end":299,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00373","name":"FERM central domain","start":136,"end":248},{"id":"PF03623","name":"Focal adhesion targeting region","start":913,"end":1050},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":422,"end":676},{"id":"PF18038","name":"FERM N-terminal domain","start":35,"end":130},{"id":"PF21477","name":"FAK1/PYK2, FERM domain C-lobe","start":260,"end":357}],"gene3D":[{"start":128,"end":252,"id":"1.20.80.10","name":"1.20.80.10"},{"start":253,"end":394,"id":"2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":502,"end":686,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"},{"start":947,"end":1053,"id":"1.20.120.330","name":"Nucleotidyltransferases  domain 2"},{"start":411,"end":501,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":31,"end":127,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"},{"start":909,"end":946,"id":"1.20.5.540","name":"Single helix bin"}]},"uniref50":"UniRef50_Q05397","sequence":"MAAAYLDPNLNHTPSSSAKTHLGTGMERSPGAMERVLKVFHYFENSSEPTTWASIIRHGDATDVRGIIQKIVDCHKVKNVACYGLRLSHLQSEEVHWLHLDMGVSNVREKFELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKNDYMLEIADQVDQEIALKLGCLEIRRSYGEMRGNALEKKSNYEVLEKDVGLRRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGANPTHLADFNQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGATQSFIIRPQKEGERALPSIPKLANNEKQGVRSHTVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPAMAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKFSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSATDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKLQQEERMRMESRRQVTVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQPNHYQVSGYSGSHGIPAMAGSIYPGQASLLDQTDSWNHRPQEVSAWQPNMEDSGTLDVRGMGQVLPTHLMEERLIRQQQEMEEDQRWLEKEERFLVMKPDVRLSRGSIEREDGGLQGPAGNQHIYQPVGKPDHAAPPKKPPRPGAPHLGSLASLNSPVDSYNEGVKIKPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDESLPVLPASTHREIEMAQKLLNSDLAELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMISQSRPH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Phasianinae","Gallus"],"uniref90":"UniRef90_Q00944","disprot_id":"DP02120","ncbi_taxon_id":9031,"regions_counter":4,"creator":"epapa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":393,"region_id":"DP02120r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for the autoinhibition of focal adhesion kinase. <i> Lietha D, Cai X, Ceccarelli DF, Li Y, Schaller MD, Eck MJ. </i> Cell, 2007","statement":[{"text":"The amino-terminal portion of the linker—including the Src SH3 docking site—is disordered in the present structure (residues 363–393)","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"epapa","start":363,"term_ontology":"IDPO","curator_name":"Elena Papaleo","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2J0K"}],"reference_id":"17574028","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":393,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural basis for the autoinhibition of focal adhesion kinase. <i> Lietha D, Cai X, Ceccarelli DF, Li Y, Schaller MD, Eck MJ. </i> Cell, 2007","term_id":"GO:0005515","curator_id":"epapa","start":363,"term_ontology":"GO","curator_name":"Elena Papaleo","reference_id":"17574028","version":3,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02120r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":584,"region_id":"DP02120r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for the autoinhibition of focal adhesion kinase. <i> Lietha D, Cai X, Ceccarelli DF, Li Y, Schaller MD, Eck MJ. </i> Cell, 2007","statement":[{"text":"The kinase activation loop adopts an inactive conformation in which it extends toward the FERM domain (near Ser46 in the F1 lobe) and is then unstructured between residues Asp573 and Leu584.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"epapa","start":573,"term_ontology":"IDPO","curator_name":"Elena Papaleo","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2J0K"}],"reference_id":"17574028","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":584,"term_name":"molecular function activator activity","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural basis for the autoinhibition of focal adhesion kinase. <i> Lietha D, Cai X, Ceccarelli DF, Li Y, Schaller MD, Eck MJ. </i> Cell, 2007","term_id":"GO:0140677","curator_id":"epapa","start":573,"term_ontology":"GO","curator_name":"Elena Papaleo","reference_id":"17574028","version":3,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02120r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q00944","date":"2018-08-26T12:22:22.000Z","acc":"Q00944","name":"Focal adhesion kinase 1","length":1053,"organism":"Gallus gallus","dataset":[],"UniParc":"UPI000012A4FA","genes":[{"name":{"value":"PTK2"},"synonyms":[{"value":"FAK"},{"value":"FAK1"}]}],"alphafold_very_low_content":0.2573599240265907,"disorder_content":0.04083570750237417,"disprot_consensus":{"full":[{"start":363,"end":393,"type":"D"},{"start":573,"end":584,"type":"D"}],"Structural state":[{"start":363,"end":393,"type":"D"},{"start":573,"end":584,"type":"D"}],"Molecular function":[{"start":363,"end":393,"type":"F"},{"start":573,"end":584,"type":"F"}]}},{"features":{"pfam":[{"id":"PF13634","name":"Nucleoporin FG repeat region","start":64,"end":141},{"id":"PF13634","name":"Nucleoporin FG repeat region","start":181,"end":246}]},"uniref50":"UniRef50_Q02199","sequence":"MFGLNKASSTPAGGLFGQASGASTGNANTGFSFGGTQTGQNTGPSTGGLFGAKPAGSTGGLGASFGQQQQQSQTNAFGGSATTGGGLFGNKPNNTANTGGGLFGANSNSNSGSLFGSNNAQTSRGLFGNNNTNNINNSSSGMNNASAGLFGSKPAGGTSLFGNTSTSSAPAQNQGMFGAKPAGTSLFGNNAGNTTTGGGLFGSKPTGATSLFGSSNNNNNNNNSNNIMSASGGLFGNQQQQLQQQPQMQCALQNLSQLPITPMTRISELPPQIRQEIEQLDQYIQKQVQISHHLKADTIDHDELIDSIPRDVAYLLKSESATSQYLKQDLKKISSFKSLIDEDLLDTQTFSVLLQQLLTPGSKISSNDLDKFFQKKIHLYEKKLEDYCRILSDIETAVNGIDTDLFGAPNNPNSTAITADLGSSEAENLLQLKTGLAAIVSTVIEEFTLFMDIAERIAVLHQKTKTLASLSI","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q02199","disprot_id":"DP02122","ncbi_taxon_id":559292,"regions_counter":7,"creator":"lchemes","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":154,"region_id":"DP02122r001","reference_id":"28716919","start":121,"ec_id":"ECO:0001183","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"This fragment is demonstrated to be intrinsically disordered by smFRET as well as by SAXS measurements","type":"Curator statement"}],"curator_id":"fquaglia","released":"2023_12","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","version":4,"reference_html":"Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. <i> Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA. </i> Proc Natl Acad Sci U S A, 2017","date":"2023-12-14T12:15:57.932Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"IPI","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T14:30:37.203Z"}},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":154,"region_id":"DP02122r002","reference_id":"28716919","start":121,"ec_id":"ECO:0006210","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"This fragment is demonstrated to be intrinsically disordered by smFRET as well as by SAXS measurements","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":3,"reference_html":"Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. <i> Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA. </i> Proc Natl Acad Sci U S A, 2017","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","cross_refs":[{"db":"SASBDB","id":"SASDEH2"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-13T18:13:37.567Z"}},{"start":1,"end":269,"reference_id":"37738963","reference_source":"pmid","reference_html":"Implications of a multiscale structure of the yeast nuclear pore complex. <i> Akey CW, Echeverria I, Ouch C, Nudelman I, Shi Y, Wang J, Chait BT, Sali A, Fernandez-Martinez J, Rout MP. </i> Mol Cell, 2023","date":"2023-12-13T18:24:46.577Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"8TJ5"}],"region_id":"DP02122r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P48837"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P14907"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P40064"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P38181"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P47054"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q03790"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P52593"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P34077"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q05166"}],"statement":[{"text":"The Cryo-EM structure of the Inner spoke ring of the yeast NPC shows this region of the NUP49 protein lacks electron density, indicating it is disordered. ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-14T12:16:11.695Z"}},{"start":408,"end":428,"reference_id":"37738963","reference_source":"pmid","reference_html":"Implications of a multiscale structure of the yeast nuclear pore complex. <i> Akey CW, Echeverria I, Ouch C, Nudelman I, Shi Y, Wang J, Chait BT, Sali A, Fernandez-Martinez J, Rout MP. </i> Mol Cell, 2023","date":"2023-12-13T18:24:59.580Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"8TJ5"}],"region_id":"DP02122r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P48837"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P14907"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P40064"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P38181"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P47054"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q03790"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P52593"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P34077"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q05166"}],"statement":[{"text":"The Cryo-EM structure of the Inner spoke ring of the yeast NPC shows this region of the NUP49 protein lacks electron density, indicating it is disordered. ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-14T12:16:16.487Z"}},{"start":1,"end":260,"reference_id":"23238392","reference_source":"pmid","reference_html":"Facilitated aggregation of FG nucleoporins under molecular crowding conditions. <i> Milles S, Huy Bui K, Koehler C, Eltsov M, Beck M, Lemke EA. </i> EMBO Rep, 2013","date":"2025-09-23T19:13:04.462Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006333","ec_ontology":"ECO","ec_name":"thioflavin T based fluorescence spectroscopy evidence","unpublished":true,"released":"2025_12","version":1,"region_id":"DP02122r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:16953"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5951"}],"statement":[{"text":"The ThT assay reported dramatically fastened amyloid formation kinetics of hNup153FG in buffer containing serine. Increasing serine concentrations even led to instantaneous aggregation of the protein (Fig 1A).","type":"Results"},{"text":"A similar phenomenon was observed for yNup49FG (supplementary Fig S1 online), indicating that also crowding-induced aggregation might be a common property of FG Nups and conserved across species.","type":"Results"},{"text":"Amyloid formation proceeded readily at 28°C under agitation.","type":"Supplementary material"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":260,"reference_id":"23238392","reference_source":"pmid","reference_html":"Facilitated aggregation of FG nucleoporins under molecular crowding conditions. <i> Milles S, Huy Bui K, Koehler C, Eltsov M, Beck M, Lemke EA. </i> EMBO Rep, 2013","date":"2025-09-23T19:12:46.456Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2025_12","version":1,"ec_go":"IPI","region_id":"DP02122r006","statement":[{"text":"This aggregation occurred even at the single-molecule level (pM protein concentrations, see Fig 1F; supplementary Fig S2 online) and is thus extremely high under molecular crowding conditions. As enhanced aggregation also occurred in the presence of other cosolutes such as lysine, trimethylaminoxid and the large molecule polyethylene glycol 20,000, we conclude that the aggregation accelerating effect is not owing to a specific chemical functionality but rather a general phenomenon, like space restriction or sequestering of water.","type":"Results"},{"text":"A similar phenomenon was observed for yNup49FG (supplementary Fig S1 online), indicating that also crowding-induced aggregation might be a common property of FG Nups and conserved across species.","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":260,"reference_id":"23238392","reference_source":"pmid","reference_html":"Facilitated aggregation of FG nucleoporins under molecular crowding conditions. <i> Milles S, Huy Bui K, Koehler C, Eltsov M, Beck M, Lemke EA. </i> EMBO Rep, 2013","date":"2023-12-13T18:54:50.451Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP02122r007","statement":[{"text":"Figure 3 and supplementary Movie S1 online show that hNup153FG hydrogels are formed from interlaced fibres that build up a meshwork giving rise to the supramolecular architecture of a hydrogel (see supplementary Fig S3 online; supplementary Movie S2 online for yNup49FG).","type":"Results"},{"text":"To exclude artifacts that might arise from sample preparation, we confirmed these results using alternative preparation and imaging methods, namely scanning electron microscopy of heavy metal-shaded samples (Fig 3; supplementary Fig S3 online), as well as transmission electron microscopy of frozen-hydrated cryosections (supplementary Fig S5 online). We consistently observed fibrous networks within the hydrogels.","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-14T12:16:45.544Z"}}],"released":"2018_11","uniref100":"UniRef100_Q02199","date":"2018-08-27T11:12:32.000Z","acc":"Q02199","name":"Nucleoporin NUP49/NSP49","length":472,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":["Condensates-related proteins"],"UniParc":"UPI000013071E","genes":[{"name":{"value":"NUP49"},"synonyms":[{"value":"NSP49"}],"orfNames":[{"value":"G1648"}],"olnNames":[{"value":"YGL172W"}]}],"alphafold_very_low_content":0.559322033898305,"disorder_content":0.614406779661017,"disprot_consensus":{"full":[{"start":1,"end":269,"type":"D"},{"start":408,"end":428,"type":"D"}],"Structural state":[{"start":1,"end":269,"type":"D"},{"start":408,"end":428,"type":"D"}],"Molecular function":[{"start":1,"end":260,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04096","name":"Nup98-96 autopeptidase S59","start":739,"end":885},{"id":"PF12110","name":"Nuclear protein 96","start":1332,"end":1623},{"id":"PF21240","name":"Nup98, Gle2-binding sequence","start":170,"end":208}],"gene3D":[{"start":733,"end":887,"id":"3.30.1610.10","name":"Peptidase S59, nucleoporin"},{"start":1315,"end":1407,"id":"1.25.40.690","name":"1.25.40.690"},{"start":158,"end":213,"id":"1.10.10.2360","name":"1.10.10.2360"}]},"uniref50":"UniRef50_P52948","sequence":"MFNKSFGTPFGGGTGGFGTTSTFGQNTGFGTTSGGAFGTSAFGSSNNTGGLFGNSQTKPGGLFGTSSFSQPATSTSTGFGFGTSTGTANTLFGTASTGTSLFSSQNNAFAQNKPTGFGNFGTSTSSGGLFGTTNTTSNPFGSTSGSLFGPSSFTAAPTGTTIKFNPPTGTDTMVKAGVSTNISTKHQCITAMKEYESKSLEELRLEDYQANRKGPQNQVGAGTTTGLFGSSPATSSATGLFSSSTTNSGFAYGQNKTAFGTSTTGFGTNPGGLFGQQNQQTTSLFSKPFGQATTTQNTGFSFGNTSTIGQPSTNTMGLFGVTQASQPGGLFGTATNTSTGTAFGTGTGLFGQTNTGFGAVGSTLFGNNKLTTFGSSTTSAPSFGTTSGGLFGNKPTLTLGTNTNTSNFGFGTNTSGNSIFGSKPAPGTLGTGLGAGFGTALGAGQASLFGNNQPKIGGPLGTGAFGAPGFNTTTATLGFGAPQAPVALTDPNASAAQQAVLQQHINSLTYSPFGDSPLFRNPMSDPKKKEERLKPTNPAAQKALTTPTHYKLTPRPATRVRPKALQTTGTAKSHLFDGLDDDEPSLANGAFMPKKSIKKLVLKNLNNSNLFSPVNRDSENLASPSEYPENGERFSFLSKPVDENHQQDGDEDSLVSHFYTNPIAKPIPQTPESAGNKHSNSNSVDDTIVALNMRAALRNGLEGSSEETSFHDESLQDDREEIENNSYHMHPAGIILTKVGYYTIPSMDDLAKITNEKGECIVSDFTIGRKGYGSIYFEGDVNLTNLNLDDIVHIRRKEVVVYLDDNQKPPVGEGLNRKAEVTLDGVWPTDKTSRCLIKSPDRLADINYEGRLEAVSRKQGAQFKEYRPETGSWVFKVSHFSKYGLQDSDEEEEEHPSKTSTKKLKTAPLPPASQTTPLQMALNGKPAPPPQSQSPEVEQLGRVVELDSDMVDITQEPVLDTMLEESMPEDQEPVSASTHIASSLGINPHVLQIMKASLLTDEEDVDMALDQRFSRLPSKADTSQEICSPRLPISASHSSKTRSLVGGLLQSKFTSGAFLSPSVSVQECRTPRAASLMNIPSTSSWSVPPPLTSVFTMPSPAPEVPLKTVGTRRQLGLVPREKSVTYGKGKLLMDMALFMGRSFRVGWGPNWTLANSGEQLNGSHELENHQIADSMEFGFLPNPVAVKPLTESPFKVHLEKLSLRQRKPDEDMKLYQTPLELKLKHSTVHVDELCPLIVPNLGVAVIHDYADWVKEASGDLPEAQIVKHWSLTWTLCEALWGHLKELDSQLNEPREYIQILERRRAFSRWLSCTATPQIEEEVSLTQKNSPVEAVFSYLTGKRISEACSLAQQSGDHRLALLLSQFVGSQSVRELLTMQLVDWHQLQADSFIQDERLRIFALLAGKPVWQLSEKKQINVCSQLDWKRSLAIHLWYLLPPTASISRALSMYEEAFQNTSDSDRYACSPLPSYLEGSGCVIAEEQNSQTPLRDVCFHLLKLYSDRHYDLNQLLEPRSITADPLDYRLSWHLWEVLRALNYTHLSAQCEGVLQASYAGQLESEGLWEWAIFVLLHIDNSGIREKAVRELLTRHCQLLETPESWAKETFLTQKLRVPAKWIHEAKAVRAHMESDKHLEALCLFKAEHWNRCHKLIIRHLASDAIINENYDYLKGFLEDLAPPERSSLIQDWETSGLVYLDYIRVIEMLRHIQQVDCSGNDLEQLHIKVTSLCSRIEQIQCYSAKDRLAQSDMAKRVANLLRVVLSLHHPPDRTSDSTPDPQRVPLRLLAPHIGRLPMPEDYAMDELRSLTQSYLRELAVGSL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P52948","disprot_id":"DP02123","ncbi_taxon_id":9606,"regions_counter":8,"creator":"lchemes","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":150,"region_id":"DP02123r001","reference_id":"28716919","start":2,"ec_id":"ECO:0006210","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Region is shown to be intrinsically disordered by smFRET and SAXS measurements","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":3,"reference_html":"Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. <i> Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA. </i> Proc Natl Acad Sci U S A, 2017","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","cross_refs":[{"db":"SASBDB","id":"SASDEB3"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-13T19:04:19.343Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":150,"region_id":"DP02123r002","released":"2022_03","ec_id":"ECO:0001183","reference_html":"Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. <i> Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA. </i> Proc Natl Acad Sci U S A, 2017","statement":[{"text":"Region is shown to be intrinsically disordered by smFRET and SAXS measurements","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"lchemes","start":2,"term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"28716919","version":2,"ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"IPI","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-13T19:04:19.828Z"}},{"start":1,"end":730,"reference_id":"35679397","reference_source":"pmid","reference_html":"AI-based structure prediction empowers integrative structural analysis of human nuclear pores. <i> Mosalaganti S, Obarska-Kosinska A, Siggel M, Taniguchi R, Turoňová B, Zimmerli CE, Buczak K, Schmidt FH, Margiotta E, Mackmull MT, Hagen WJH, Hummer G, Kosinski J, Beck M. </i> Science, 2022","date":"2023-12-13T19:12:39.619Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7R5J"},{"db":"PDB","id":"7R5K"},{"db":"EMDB","id":"14322"},{"db":"EMDB","id":"14321"}],"region_id":"DP02123r003","statement":[{"text":"The electron microscopy structures of the Human nuclear pore complex (both dilated and constricted), shows this region from the NUP98 protein lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-14T15:10:09.669Z"}},{"start":881,"end":1111,"reference_id":"35679397","reference_source":"pmid","reference_html":"AI-based structure prediction empowers integrative structural analysis of human nuclear pores. <i> Mosalaganti S, Obarska-Kosinska A, Siggel M, Taniguchi R, Turoňová B, Zimmerli CE, Buczak K, Schmidt FH, Margiotta E, Mackmull MT, Hagen WJH, Hummer G, Kosinski J, Beck M. </i> Science, 2022","date":"2023-12-13T19:13:06.589Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7R5J"},{"db":"PDB","id":"7R5K"},{"db":"EMDB","id":"14322"},{"db":"EMDB","id":"14321"}],"region_id":"DP02123r004","statement":[{"text":"The electron microscopy structures of the Human nuclear pore complex (both dilated and constricted), shows this region from the NUP98 protein lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-14T15:10:11.254Z"}},{"start":1161,"end":1193,"reference_id":"35679397","reference_source":"pmid","reference_html":"AI-based structure prediction empowers integrative structural analysis of human nuclear pores. <i> Mosalaganti S, Obarska-Kosinska A, Siggel M, Taniguchi R, Turoňová B, Zimmerli CE, Buczak K, Schmidt FH, Margiotta E, Mackmull MT, Hagen WJH, Hummer G, Kosinski J, Beck M. </i> Science, 2022","date":"2023-12-13T19:13:16.677Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7R5J"},{"db":"PDB","id":"7R5K"},{"db":"EMDB","id":"14322"},{"db":"EMDB","id":"14321"}],"region_id":"DP02123r005","statement":[{"text":"The electron microscopy structures of the Human nuclear pore complex (both dilated and constricted), shows this region from the NUP98 protein lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-14T15:10:13.273Z"}},{"start":1,"end":499,"reference_id":"25562883","reference_source":"pmid","reference_html":"Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity.  <i> Schmidt HB, Görlich D. </i> Elife, 2015","date":"2023-12-13T19:26:51.743Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02123r006","statement":[{"text":"We next extended our analysis of spontaneous FG phase formation to the entire set of Nup98 FG domains. We observed that all of them showed the same readiness to phase-separate and form FG particles as the ScNup100 FG domain (Figures 6 and 7).","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"ec_go":"IDA","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-14T15:10:15.250Z"}},{"start":1,"end":499,"reference_id":"25562883","reference_source":"pmid","reference_html":"Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity.  <i> Schmidt HB, Görlich D. </i> Elife, 2015","date":"2023-12-13T19:26:58.822Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006333","ec_ontology":"ECO","ec_name":"thioflavin T based fluorescence spectroscopy evidence","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02123r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:16953"}],"statement":[{"text":"Particles were formed at 5 µM (HsNup98, TtMacNup98, TbNup158) or 10 µM FG domain concentration (all other FG domains). The suspensions were afterwards supplemented with 3 µM MBP-mCherry and 1 µM ThioflavinT, a diagnostic dye for the presence of amyloid-like cross-β-structures.","type":"Figure"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-14T15:10:17.062Z"}},{"start":1,"end":499,"reference_id":"25562883","reference_source":"pmid","reference_html":"Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity.  <i> Schmidt HB, Görlich D. </i> Elife, 2015","date":"2023-12-13T19:30:56.020Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006077","ec_ontology":"ECO","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q14974","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02123r008","statement":[{"text":"As a first step, we constructed bacterial expression vectors, and recombinantly expressed, purified, and immobilized all ten Nup98 domains. We observed that all of them bound human Importin β specifically and to a similar extend (Figure 5B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-14T15:10:18.683Z"}}],"released":"2018_11","uniref100":"UniRef100_P52948","date":"2018-08-27T11:24:32.000Z","acc":"P52948","name":"Nuclear pore complex protein Nup98-Nup96","length":1817,"organism":"Homo sapiens","dataset":["Cancer-related proteins","Condensates-related proteins"],"UniParc":"UPI00001BBB12","genes":[{"name":{"value":"NUP98","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:8068","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8068"}}]},"synonyms":[{"value":"ADAR2"}]}],"alphafold_very_low_content":0.519537699504678,"disorder_content":0.5470555861309851,"disprot_consensus":{"full":[{"start":1,"end":730,"type":"D"},{"start":881,"end":1111,"type":"D"},{"start":1161,"end":1193,"type":"D"}],"Structural state":[{"start":1,"end":730,"type":"D"},{"start":881,"end":1111,"type":"D"},{"start":1161,"end":1193,"type":"D"}],"Molecular function":[{"start":1,"end":499,"type":"F"}],"Biological process":[{"start":1,"end":499,"type":"F"}]}},{"features":{"pfam":[{"id":"PF09402","name":"Man1-Src1p-C-terminal domain","start":329,"end":661},{"id":"PF12949","name":"HeH/LEM domain","start":8,"end":42}]},"uniref50":"UniRef50_Q03281","sequence":"MDHRNLDPKTLKVSQLRRVLVENDVAFPANARKPVLVKLFEEKVRQRLQSSPEASKVRTSIQKVVKSGAKNADRKKTLKSKKLESSSSESKTVKDENVETNKRKREQISTDNEAKMQIQEEKSPKKKRKKRSSKANKPPESPPQSKSDGKATSADLTSELETVEELHKKDSSDDKPRVKELPKPELPNLKVSNEFLAQLNKELASAATENYDHSIKSTDLSSIRIETEEPVGPSTGAETRNESEVMENINLEVQPEVKEAKEELTKISETFDNQDEEDTSRLSSKKNIRSPKGRTRHFIANKTKRGIDIMKPFIAHLFIWLWNGAIFLSIICPILFGLWYREQRIQVGYCGHEKPLKSLAISAFPQTERVDSVLQAYRPNCLECPEHGICSSFMNVECEPGYEPKSSILETYGIIPFPKYCAKDESKEKEVDELVWKVNEYLKKKNAQHECGEGENLFESGETETKLYDIFSHSRPSWESQREFNDHWKNVLEILKKKDDIIWLPLDFETNGKREKSKSNNTNYIYRSTSKKWVTLQCHLEGDIQEYITKYGGSLFITLGVLFLIKKIQSTLDNYVQGEQIIEKLVKEAIDKLKDVKKNKGEEPFLTTVQLRATLLSDIPNIKEQNNLWAQTKEKIMKEQSENIELYLLEENGEIMTCWEWKE","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q03281","disprot_id":"DP02124","ncbi_taxon_id":559292,"regions_counter":2,"creator":"lchemes","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":140,"region_id":"DP02124r001","released":"2022_03","ec_id":"ECO:0001183","reference_html":"Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. <i> Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA. </i> Proc Natl Acad Sci U S A, 2017","statement":[{"text":"The region was demonstrated to be intrinsically disordered by smFRET as well as SAXS measurements","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"lchemes","start":99,"term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"28716919","version":2,"ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"IPI","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":140,"region_id":"DP02124r002","reference_id":"28716919","start":99,"ec_id":"ECO:0006210","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The region was demonstrated to be intrinsically disordered by smFRET as well as SAXS measurements","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":3,"reference_html":"Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. <i> Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA. </i> Proc Natl Acad Sci U S A, 2017","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","cross_refs":[{"db":"SASBDB","id":"SASDEM2"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q03281","date":"2018-08-27T11:25:06.000Z","acc":"Q03281","name":"Inner nuclear membrane protein HEH2","length":663,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000013A86E","genes":[{"name":{"value":"HEH2"},"orfNames":[{"value":"D8035.2"}],"olnNames":[{"value":"YDR458C"}]}],"alphafold_very_low_content":0.3740573152337858,"disorder_content":0.06334841628959276,"disprot_consensus":{"full":[{"start":99,"end":140,"type":"D"}],"Structural state":[{"start":99,"end":140,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00581","name":"Rhodanese-like domain","start":323,"end":419},{"id":"PF06617","name":"M-phase inducer phosphatase","start":200,"end":247}],"gene3D":[{"start":280,"end":462,"id":"3.40.250.10","name":"Rhodanese-like domain"}]},"uniref50":"UniRef50_P30307","sequence":"MSTELFSSTREEGSSGSGPSFRSNQRKMLNLLLERDTSFTVCPDVPRTPVGKFLGDSANLSILSGGTPKRCLDLSNLSSGEITATQLTTSADLDETGHLDSSGLQEVHLAGMNHDQHLMKCSPAQLLCSTPNGLDRGHRKRDAMCSSSANKENDNGNLVDSEMKYLGSPITTVPKLDKNPNLGEDQAEEISDELMEFSLKDQEAKVSRSGLYRSPSMPENLNRPRLKQVEKFKDNTIPDKVKKKYFSGQGKLRKGLCLKKTVSLCDITITQMLEEDSNQGHLIGDFSKVCALPTVSGKHQDLKYVNPETVAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEELFNFFLKKPIVPLDTQKRIIIVFHCEFSSERGPRMCRCLREEDRSLNQYPALYYPELYILKGGYRDFFPEYMELCEPQSYCPMHHQDHKTELLRCRSQSKVQEGERQLREQIALLVKDMSP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P30307","disprot_id":"DP02126","ncbi_taxon_id":9606,"regions_counter":3,"creator":"couzo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":225,"region_id":"DP02126r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The Molecular Tweezer CLR01 Stabilizes a Disordered Protein-Protein Interface. <i> Bier D, Mittal S, Bravo-Rodriguez K, Sowislok A, Guillory X, Briels J, Heid C, Bartel M, Wettig B, Brunsveld L, Sanchez-Garcia E, Schrader T, Ottmann C. </i> J Am Chem Soc, 2017","statement":[{"text":"Protein crystallography, biophysical affinity determination and biomolecular simulations unanimously deliver a remarkable finding: a supramolecular \"Janus\" ligand can bind simultaneously to a flexible peptidic PPI recognition motif and to a well-structured adapter protein.","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"couzo","start":208,"term_ontology":"IDPO","curator_name":"Christos Ouzounis","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0086-8657","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5M37"}],"reference_id":"29039919","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":225,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"The Molecular Tweezer CLR01 Stabilizes a Disordered Protein-Protein Interface. <i> Bier D, Mittal S, Bravo-Rodriguez K, Sowislok A, Guillory X, Briels J, Heid C, Bartel M, Wettig B, Brunsveld L, Sanchez-Garcia E, Schrader T, Ottmann C. </i> J Am Chem Soc, 2017","statement":[{"text":"Upon binding to the rigid 14-3-3 protein, the recognition motifs undergo a disorder-to-order transition which might impose a specific functional fold of the IDP.","type":"Introduction"}],"term_id":"IDPO:0000011","curator_id":"couzo","start":208,"term_ontology":"IDPO","curator_name":"Christos Ouzounis","reference_id":"29039919","version":2,"curator_orcid":"0000-0002-0086-8657","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02126r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":225,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"The Molecular Tweezer CLR01 Stabilizes a Disordered Protein-Protein Interface. <i> Bier D, Mittal S, Bravo-Rodriguez K, Sowislok A, Guillory X, Briels J, Heid C, Bartel M, Wettig B, Brunsveld L, Sanchez-Garcia E, Schrader T, Ottmann C. </i> J Am Chem Soc, 2017","statement":[{"text":"The crystal structure of the ternary complex between 14-3-3ζ, the Cdc25CpS216 peptide and CLR01 revealed that the molecular tweezer is bound to R208 of the Cdc25C peptide (R208Cdc25C).","type":"Introduction"}],"term_id":"GO:0005515","curator_id":"couzo","start":208,"term_ontology":"GO","curator_name":"Christos Ouzounis","reference_id":"29039919","version":3,"curator_orcid":"0000-0002-0086-8657","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"uniprot","id":"P31946"}],"region_id":"DP02126r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P30307","date":"2018-08-27T15:35:31.000Z","acc":"P30307","name":"M-phase inducer phosphatase 3","length":473,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000003753D","genes":[{"name":{"value":"CDC25C"}}],"alphafold_very_low_content":0.5221987315010571,"disorder_content":0.03805496828752643,"disprot_consensus":{"full":[{"start":208,"end":225,"type":"T"}],"Structural state":[{"start":208,"end":225,"type":"D"}],"Structural transition":[{"start":208,"end":225,"type":"T"}],"Molecular function":[{"start":208,"end":225,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00006","name":"ATP synthase alpha/beta family, nucleotide-binding domain","start":160,"end":363},{"id":"PF07497","name":"Rho termination factor, RNA-binding domain","start":52,"end":125},{"id":"PF07498","name":"Rho termination factor, N-terminal domain","start":5,"end":47}],"gene3D":[{"start":130,"end":417,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":1,"end":47,"id":"1.10.720.10","name":"1.10.720.10"},{"start":48,"end":117,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}]},"uniref50":"UniRef50_Q89A22","sequence":"MNLTELKNTPVSELITLGENMGLENLARMRKQDIIFAILKQHAKSGEDIFGDGVLEILQDGFGFLRSADSSYLAGPDDIYVSPSQIRRFNLRTGDTISGKIRPPKEGERYFALLKVNEVNFDKPENARNKILFENLTPLHANSRLRMERGNGSTEDLTARVLDLASPIGRGQRGLIVAPPKAGKTMLLQNIAQSIAYNHPDCVLMVLLIDERPEEVTEMQRLVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVIILLDSITRLARAYNTVVPASGKVLTGGVDANALHRPKRFFGAARNVEEGGSLTIIATALIDTGSKMDEVIYEEFKGTGNMELHLSRKIAEKRVFPAIDYNRSGTRKEELLTTQEELQKMWILRKIIHPMGEIDAMEFLINKLAMTKTNDDFFEMMKRS","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0AG32","disprot_id":"DP02127","ncbi_taxon_id":83333,"regions_counter":3,"creator":"csanchezrocha","regions":[{"start":1,"end":30,"reference_id":"17081977","reference_source":"pmid","reference_html":"Structural insights into RNA-dependent ring closure and ATPase activation by the Rho termination factor. <i> Skordalakes E, Berger JM. </i> Cell, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2HT1"}],"region_id":"DP02127r002","statement":[{"text":"Electron density was evident for residues 31–354 of both Rho protomers and for three RNA segments. The final model has been refined to 3.5 A ̊ resolution and shows good stereochemistry.","type":"Results"},{"text":"This movement is concomitant with a loss of interpretable electron density for the first 30 amino acids at the extreme N terminus, a highly variable and typically Arg/Gly-rich region of Rho orthologs.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-15T15:54:53.650Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":355,"end":411,"reference_id":"17081977","reference_source":"pmid","reference_html":"Structural insights into RNA-dependent ring closure and ATPase activation by the Rho termination factor. <i> Skordalakes E, Berger JM. </i> Cell, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2HT1"}],"region_id":"DP02127r003","statement":[{"text":"Electron density was evident for residues 31–354 of both Rho protomers and for three RNA segments. The final model has been refined to 3.5 A ̊ resolution and shows good stereochemistry.","type":"Results"},{"text":"This movement is concomitant with a loss of interpretable electron density for the first 30 amino acids at the extreme N terminus, a highly variable and typically Arg/Gly-rich region of Rho orthologs. Another difference is that the last 65 amino acids of the C-terminal domain are disordered and have been displaced in part by residues from the connector loop that links the N- and C-terminal domains.","type":"Results"},{"text":"Since Phe355 lies within the C-terminal region of Rho that is disordered in this crystal form, and since Rho411 retains length-dependent RNA-stimulated ATPase activity.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-15T15:54:52.455Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P0AG32","date":"2018-08-27T15:50:59.000Z","acc":"P0AG30","name":"Transcription termination factor Rho","length":419,"organism":"Escherichia coli (strain K12)","dataset":["RNA-binding proteins"],"UniParc":"UPI000013389B","genes":[{"name":{"value":"rho"},"synonyms":[{"value":"nitA"},{"value":"psuA"},{"value":"rnsC"},{"value":"sbaA"},{"value":"tsu"}],"olnNames":[{"value":"b3783"},{"value":"JW3756"}]}],"alphafold_very_low_content":0,"disorder_content":0.20763723150357996,"disprot_consensus":{"full":[{"start":1,"end":30,"type":"D"},{"start":355,"end":411,"type":"D"}],"Structural state":[{"start":1,"end":30,"type":"D"},{"start":355,"end":411,"type":"D"}]}},{"acc":"P06437","sequence":"MHQGAPSWGRRWFVVWALLGLTLGVLVASAAPTSPGTPGVAAATQAANGGPATPAPPPLGAAPTGDPKPKKNKKPKNPTPPRPAGDNATVAAGHATLREHLRDIKAENTDANFYVCPPPTGATVVQFEQPRRCPTRPEGQNYTEGIAVVFKENIAPYKFKATMYYKDVTVSQVWFGHRYSQFMGIFEDRAPVPFEEVIDKINAKGVCRSTAKYVRNNLETTAFHRDDHETDMELKPANAATRTSRGWHTTDLKYNPSRVEAFHRYGTTVNCIVEEVDARSVYPYDEFVLATGDFVYMSPFYGYREGSHTEHTTYAADRFKQVDGFYARDLTTKARATAPTTRNLLTTPKFTVAWDWVPKRPSVCTMTKWQEVDEMLRSEYGGSFRFSSDAISTTFTTNLTEYPLSRVDLGDCIGKDARDAMDRIFARRYNATHIKVGQPQYYQANGGFLIAYQPLLSNTLAELYVREHLREQSRKPPNPTPPPPGASANASVERIKTTSSIEFARLQFTYNHIQRHVNDMLGRVAIAWCELQNHELTLWNEARKLNPNAIASVTVGRRVSARMLGDVMAVSTCVPVAADNVIVQNSMRISSRPGACYSRPLVSFRYEDQGPLVEGQLGENNELRLTRDAIEPCTVGHRRYFTFGGGYVYFEEYAYSHQLSRADITTVSTFIDLNITMLEDHEFVPLEVYTRHEIKDSGLLDYTEVQRRNQLHDLRFADIDTVIHADANAAMFAGLGAFFEGMGDLGRAVGKVVMGIVGGVVSAVSGVSSFMSNPFGALAVGLLVLAGLAAAFFAFRYVMRLQSNPMKALYPLTTKELKNPTNPDASGEGEEGGDFDEAKLAEAREMIRYMALVSAMERTEHKAKKKGTSALLSAKVTDMVMRKRRNTNYTQVPNKDGDADEDDL","creator":"viglesias","dataset":["Viral proteins"],"date":"2018-08-27T16:31:29.000Z","disprot_id":"DP02128","features":{"pfam":[{"id":"PF00606","name":"Herpesvirus Glycoprotein B ectodomain","start":500,"end":721},{"id":"PF17416","name":"Herpesvirus Glycoprotein B","start":153,"end":364},{"id":"PF17417","name":"Herpesvirus Glycoprotein B PH-like domain","start":366,"end":463}],"gene3D":[{"start":350,"end":497,"id":"2.30.29.100","name":"2.30.29.100","_id":"685af523b4ac24d5329d93b4"},{"start":564,"end":665,"id":"3.30.1450.20","name":"3.30.1450.20","_id":"685af523b4ac24d5329d93b5"}]},"genes":[{"name":{"value":"gB","evidences":[{"source":{"id":"MF_04032","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04032","_id":"685af523b4ac24d5329d93cc"},"code":"ECO:0000255","_id":"685af523b4ac24d5329d93cb"}],"_id":"685af523b4ac24d5329d93cd"},"synonyms":[],"olnNames":[],"orfNames":[{"value":"UL27","evidences":[],"_id":"685af523b4ac24d5329d93ce"}],"_id":"685af523b4ac24d5329d93ca"}],"length":904,"name":"Envelope glycoprotein B","ncbi_taxon_id":10306,"organism":"Human herpesvirus 1 (strain KOS)","regions_counter":5,"released":"2018_11","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Peploviricota","Herviviricetes","Herpesvirales","Herpesviridae","Alphaherpesvirinae","Simplexvirus"],"UniParc":"UPI0000147055","uniref100":"UniRef100_P06437","uniref50":"UniRef50_P06437","uniref90":"UniRef90_P06437","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":31,"end":102,"interaction_partner":[],"reference_html":"Crystal structure of glycoprotein B from herpes simplex virus 1. <i> Heldwein EE, Lou H, Bender FC, Cohen GH, Eisenberg RJ, Harrison SC. </i> Science, 2006","reference_id":"16840698","region_id":"DP02128r004","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"Trypsin cleavage before crystallization separates residues Ala31 to Arg102, which are poorly conserved and relatively unstructured, from the rest of the molecule, probably because this segment, which contains a heparan sulfate interaction site (23), is not firmly anchored.","_id":"685af523b4ac24d5329d93c4"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-02T11:00:01.684Z","_id":"685af523b4ac24d5329d93c5"},"version":1,"_id":"685af523b4ac24d5329d93c3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2GUM","_id":"685af523b4ac24d5329d93c7"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":462,"end":490,"interaction_partner":[],"reference_html":"Crystal structure of glycoprotein B from herpes simplex virus 1. <i> Heldwein EE, Lou H, Bender FC, Cohen GH, Eisenberg RJ, Harrison SC. </i> Science, 2006","reference_id":"16840698","region_id":"DP02128r005","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"Trypsin cleavage before crystallization separates residues Ala31 to Arg102, which are poorly conserved and relatively unstructured, from the rest of the molecule, probably because this segment, which contains a heparan sulfate interaction site (23), is not firmly anchored.","_id":"685af523b4ac24d5329d93c8"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-02T11:00:00.253Z","_id":"685af523b4ac24d5329d93c9"},"version":1,"_id":"685af523b4ac24d5329d93c6","reference_source":"pmid"}],"__v":0,"disorder_content":0.11172566371681415,"disprot_consensus":{"full":[{"start":31,"end":102,"type":"D"},{"start":462,"end":490,"type":"D"}],"Structural state":[{"start":31,"end":102,"type":"D"},{"start":462,"end":490,"type":"D"}]}},{"features":{"pfam":[{"id":"PF13519","name":"von Willebrand factor type A domain","start":6,"end":115}],"gene3D":[{"start":3,"end":184,"id":"3.40.50.410","name":"von Willebrand factor, type A domain"}]},"uniref50":"UniRef50_O94444","sequence":"MVLEATMILIDNSEWMINGDYIPTRFEAQKDTVHMIFNQKINDNPENMCGLMTIGDNSPQVLSTLTRDYGKFLSAMHDLPVRGNAKFGDGIQIAQLALKHRENKIQRQRIVAFVGSPIVEDEKNLIRLAKRMKKNNVAIDIIHIGELQNESALQHFIDAANSSDSCHLVSIPPSPQLLSDLVNQSPIGQGVVASQNQFEYGVDPNLDVELALALELSMAEERARQEVAAQKSSEETEDKKMQE","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"uniref90":"UniRef90_O94444","disprot_id":"DP02129","ncbi_taxon_id":284812,"regions_counter":2,"creator":"mlambrughi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":243,"region_id":"DP02129r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of Rpn10 and its interactions with polyubiquitin chains and the proteasome subunit Rpn12. <i> Riedinger C, Boehringer J, Trempe JF, Lowe ED, Brown NR, Gehring K, Noble ME, Gordon C, Endicott JA. </i> J Biol Chem, 2010","statement":[{"text":"Taken together, the crystallographic and NMR data suggest a structure for Rpn10 in which a compact VWA fold (residues 1–191) is connected via a long (approximately 16 amino acids), flexible linker to an extended α-helix that in solution does not interact with the VWA domain (Fig. 4C).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mlambrughi","start":229,"term_ontology":"IDPO","curator_name":"Matteo Lambrughi","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-0894-8627","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20739285","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":209,"region_id":"DP02129r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of Rpn10 and its interactions with polyubiquitin chains and the proteasome subunit Rpn12. <i> Riedinger C, Boehringer J, Trempe JF, Lowe ED, Brown NR, Gehring K, Noble ME, Gordon C, Endicott JA. </i> J Biol Chem, 2010","statement":[{"text":"Taken together, the crystallographic and NMR data suggest a structure for Rpn10 in which a compact VWA fold (residues 1–191) is connected via a long (approximately 16 amino acids), flexible linker to an extended α-helix that in solution does not interact with the VWA domain (Fig. 4C).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mlambrughi","start":192,"term_ontology":"IDPO","curator_name":"Matteo Lambrughi","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-0894-8627","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20739285","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_O94444","date":"2018-08-27T16:37:53.000Z","acc":"O94444","name":"26S proteasome regulatory subunit rpn10","length":243,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","dataset":[],"UniParc":"UPI000013464F","genes":[{"name":{"value":"rpn10"},"synonyms":[{"value":"pus1"}],"orfNames":[{"value":"SPAC637.10c"}]}],"alphafold_very_low_content":0.04938271604938271,"disorder_content":0.13580246913580246,"disprot_consensus":{"full":[{"start":192,"end":209,"type":"D"},{"start":229,"end":243,"type":"D"}],"Structural state":[{"start":192,"end":209,"type":"D"},{"start":229,"end":243,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00147","name":"Fibrinogen beta and gamma chains, C-terminal globular domain","start":630,"end":862},{"id":"PF08702","name":"Fibrinogen alpha/beta chain family","start":49,"end":189},{"id":"PF12160","name":"Fibrinogen alpha C domain","start":445,"end":509}],"gene3D":[{"start":46,"end":235,"id":"1.20.5.50","name":"1.20.5.50"}]},"uniref50":"UniRef50_P02671","sequence":"MFSMRIVCLVLSVVGTAWTADSGEGDFLAEGGGVRGPRVVERHQSACKDSDWPFCSDEDWNYKCPSGCRMKGLIDEVNQDFTNRINKLKNSLFEYQKNNKDSHSLTTNIMEILRGDFSSANNRDNTYNRVSEDLRSRIEVLKRKVIEKVQHIQLLQKNVRAQLVDMKRLEVDIDIKIRSCRGSCSRALAREVDLKDYEDQQKQLEQVIAKDLLPSRDRQHLPLIKMKPVPDLVPGNFKSQLQKVPPEWKALTDMPQMRMELERPGGNEITRGGSTSYGTGSETESPRNPSSAGSWNSGSSGPGSTGNRNPGSSGTGGTATWKPGSSGPGSTGSWNSGSSGTGSTGNQNPGSPRPGSTGTWNPGSSERGSAGHWTSESSVSGSTGQWHSESGSFRPDSPGSGNARPNNPDWGTFEEVSGNVSPGTRREYHTEKLVTSKGDKELRTGKEKVTSGSTTTTRRSCSKTVTKTVIGPDGHKEVTKEVVTSEDGSDCPEAMDLGTLSGIGTLDGFRHRHPDEAAFFDTASTGKTFPGFFSPMLGEFVSETESRGSESGIFTNTKESSSHHPGIAEFPSRGKSSSYSKQFTSSTSYNRGDSTFESKSYKMADEAGSEADHEGTHSTKRGHAKSRPVRDCDDVLQTHPSGTQSGIFNIKLPGSSKIFSVYCDQETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDEGEGEFWLGNDYLHLLTQRGSVLRVELEDWAGNEAYAEYHFRVGSEAEGYALQVSSYEGTAGDALIEGSVEEGAEYTSHNNMQFSTFDRDADQWEENCAEVYGGGWWYNNCQAANLNGIYYPGGSYDPRNNSPYEIENGVVWVSFRGADYSLRAVRMKIRPLVTQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P02671","disprot_id":"DP02130","ncbi_taxon_id":9606,"regions_counter":3,"creator":"viglesias","regions":[{"start":232,"end":581,"reference_id":"19296670","reference_source":"pmid","reference_html":"Crystal structure of human fibrinogen. <i> Kollman JM, Pandi L, Sawaya MR, Riley M, Doolittle RF. </i> Biochemistry, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3GHG"}],"region_id":"DP02130r003","statement":[{"text":"In human fibrinogen α chains, there are ten 13-residue repeats that are absent in chicken fibrinogen. The repeat region and the αC domain are mostly disordered and cannot be discerned in electron density maps.","type":"Figure"},{"text":"The flexibly attached and mobile αC domains, which cannot be identified in electron density maps, are only ∼30% identical in the two species.","type":"Article"},{"text":"As was the case for native chicken fibrinogen, no resolvable electron density could be associated with αC domains.","type":"Abstract"},{"text":"There was no discernible electron density corresponding to the αC domains.","type":"Article"},{"text":"Beyond that, the lack of electron density for regions corresponding to the αC domains, often termed “free swimming appendages”, is further testimony to the mobile nature of these entities (46), elegant NMR studies showing some core structure notwithstanding (47, 48).","type":"Discussion"},{"text":"As such, it is not surprising that in this study no density was found that could be assigned to αC domains with any certainty.","type":"Discussion"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-14T07:53:16.609Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P02671","date":"2018-08-27T17:24:49.000Z","acc":"P02671","name":"Fibrinogen alpha chain","length":866,"organism":"Homo sapiens","dataset":["Extracellular matrix proteins","NDDs-related proteins"],"UniParc":"UPI000012A75A","genes":[{"name":{"value":"FGA"}}],"alphafold_very_low_content":0.4387990762124711,"disorder_content":0.40415704387990764,"disprot_consensus":{"full":[{"start":232,"end":581,"type":"D"}],"Structural state":[{"start":232,"end":581,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00172","name":"Fungal Zn(2)-Cys(6) binuclear cluster domain","start":9,"end":47},{"id":"PF03902","name":"Gal4-like dimerisation domain","start":50,"end":93},{"id":"PF04082","name":"Fungal specific transcription factor domain","start":244,"end":446}],"gene3D":[{"start":1,"end":40,"id":"4.10.240.10","name":"Zn(2)-C6 fungal-type DNA-binding domain"},{"start":50,"end":106,"id":"1.20.5.170","name":"1.20.5.170"}]},"uniref50":"UniRef50_P04386","sequence":"MKLLSSIEQACDICRLKKLKCSKEKPKCAKCLKNNWECRYSPKTKRSPLTRAHLTEVESRLERLEQLFLLIFPREDLDMILKMDSLQDIKALLTGLFVQDNVNKDAVTDRLASVETDMPLTLRQHRISATSSSEESSNKGQRQLTVSIDSAAHHDNSTIPLDFMPRDALHGFDWSEEDDMSDGLPFLKTDPNNNGFFGDGSLLCILRSIGFKPENYTNSNVNRLPTMITDRYTLASRSTTSRLLQSYLNNFHPYCPIVHSPTLMMLYNNQIEIASKDQWQILFNCILAIGAWCIEGESTDIDVFYYQNAKSHLTSKVFESGSIILVTALHLLSRYTQWRQKTNTSYNFHSFSIRMAISLGLNRDLPSSFSDSSILEQRRRIWWSVYSWEIQLSLLYGRSIQLSQNTISFPSSVDDVQRTTTGPTIYHGIIETARLLQVFTKIYELDKTVTAEKSPICAKKCLMICNEIEEVSRQAPKFLQMDISTTALTNLLKEHPWLSFTRFELKWKQLSLIIYVLRDFFTNFTQKKSQLEQDQNDHQSYEVKRCSIMLSDAAQRTVMSVSSYMDNHNVTPYFAWNCSYYLFNAVLVPIKTLLSNSKSNAENNETAQLLQQINTVLMLLKKLATFKIQTCEKYIQVLEEVCAPFLLSQCAIPLPHISYNNSNGSAIKNIVGSATIAQYPTLPEENVNNISVKYVSPGSVGPSPVPLKSGASFSDLVKLLSNRPPSRNSPVTIPRSTPSHRSVTPFLGQQQQLQSLVPLTPSALFGGANFNQSGNIADSSLSFTFTNSSNGPNLITTQTNSQALSQPIASSNVHDNFMNNEITASKIDDGNNSKPLSPGWTDQTAYNAFGITTGMFNTTTMDDVYNYLFDDEDTPPNPKKE","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P04386","disprot_id":"DP02132","ncbi_taxon_id":559292,"regions_counter":1,"creator":"thorvath","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":144,"region_id":"DP02132r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The acidic activation domains of the GCN4 and GAL4 proteins are not alpha helical but form beta sheets. <i> Van Hoy M, Leuther KK, Kodadek T, Johnston SA. </i> Cell, 1993","statement":[{"text":"The CD spectrum of the GCN4 fragment in buffered aqueous solution (pH 7.0) consists of a single negative absorption at 197nm, characteristic of a conformationally mobile species","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"thorvath","start":107,"term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"8440022","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P04386","date":"2018-08-27T17:45:48.000Z","acc":"P04386","name":"Regulatory protein GAL4","length":881,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000000980","genes":[{"name":{"value":"GAL4"},"olnNames":[{"value":"YPL248C"}]}],"alphafold_very_low_content":0.3598183881952327,"disorder_content":0.043132803632236094,"disprot_consensus":{"full":[{"start":107,"end":144,"type":"D"}],"Structural state":[{"start":107,"end":144,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01807","name":"CHC2 zinc finger","start":6,"end":101},{"id":"PF08275","name":"DNA primase catalytic core, N-terminal domain","start":126,"end":251},{"id":"PF08278","name":"DNA primase DnaG DnaB-binding","start":451,"end":574},{"id":"PF10410","name":"DnaB-helicase binding domain of primase","start":369,"end":424},{"id":"PF13155","name":"Toprim-like","start":263,"end":349}],"gene3D":[{"start":115,"end":240,"id":"3.90.980.10","name":"DNA primase, catalytic core, N-terminal domain"},{"start":1,"end":100,"id":"3.90.580.10","name":"Zinc finger, CHC2-type domain"},{"start":434,"end":581,"id":"1.10.860.10","name":"DNAb Helicase; Chain A"},{"start":368,"end":426,"id":"1.20.50.20","name":"DnaG, RNA polymerase domain, helical bundle"},{"start":241,"end":367,"id":"3.40.1360.10","name":"3.40.1360.10"}]},"uniref50":"UniRef50_P07362","sequence":"MAGRIPRVFINDLLARTDIVDLIDARVKLKKQGKNFHACCPFHNEKTPSFTVNGEKQFYHCFGCGAHGNAIDFLMNYDKLEFVETVEELAAMHNLEVPFEAGSGPSQIERHQRQTLYQLMDGLNTFYQQSLQQPVATSARQYLEKRGLSHEVIARFAIGFAPPGWDNVLKRFGGNPENRQSLIDAGMLVTNDQGRSYDRFRERVMFPIRDKRGRVIGFGGRVLGNDTPKYLNSPETDIFHKGRQLYGLYEAQQDNAEPNRLLVVEGYMDVVALAQYGINYAVASLGTSTTADHIQLLFRATNNVICCYDGDRAGRDAAWRALETALPYMTDGRQLRFMFLPDGEDPDTLVRKEGKEAFEARMEQAMPLSAFLFNSLMPQVDLSTPDGRARLSTLALPLISQVPGETLRIYLRQELGNKLGILDDSQLERLMPKAAESGVSRPVPQLKRTTMRILIGLLVQNPELATLVPPLENLDENKLPGLGLFRELVNTCLSQPGLTTGQLLEHYRGTNNAATLEKLSMWDDIADKNIAEQTFTDSLNHMFDSLLELRQEELIARERTHGLSNEERLELWTLNQELAKK","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0ABS6","disprot_id":"DP02134","ncbi_taxon_id":83333,"regions_counter":1,"creator":"viglesias","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":12,"region_id":"DP02134r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Monomeric solution structure of the helicase-binding domain of Escherichia coli DnaG primase. <i> Su XC, Schaeffer PM, Loscha KV, Gan PH, Dixon NE, Otting G. </i> FEBS J, 2006","statement":[{"text":"Increased R1 and decreased R2 relaxation rates indicated increased mobility and structural disorder for about 12 and three residues at the N-terminus and C-terminus of the construct, respectively.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"viglesias","start":1,"term_ontology":"IDPO","curator_name":"Valentín Iglesias","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-6133-0869","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2haj"}],"reference_id":"17010164","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P0ABS6","date":"2018-08-27T17:47:58.000Z","acc":"P0ABS5","name":"DNA primase","length":581,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI00001321D4","genes":[{"name":{"value":"dnaG","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00974","url":"https://hamap.expasy.org/unirule/MF_00974"}}]},"synonyms":[{"value":"dnaP"},{"value":"parB"}],"olnNames":[{"value":"b3066"},{"value":"JW3038"}]}],"alphafold_very_low_content":0.025817555938037865,"disorder_content":0.020654044750430294,"disprot_consensus":{"full":[{"start":1,"end":12,"type":"D"}],"Structural state":[{"start":1,"end":12,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00436","name":"Single-strand binding protein family","start":6,"end":112}],"gene3D":[{"start":2,"end":146,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}]},"uniref50":"UniRef50_P0AGE2","sequence":"MASRGVNKVILVGNLGQDPEVRYMPNGGAVANITLATSESWRDKATGEMKEQTEWHRVVLFGKLAEVASEYLRKGSQVYIEGQLRTRKWTDQSGQDRYTTEVVVNVGGTMQMLGGRQGGGAPAGGNIGGGQPQGGWGQPQQPQGGNQFSGGAQSRPQQSAPAAPSNEPPMDFDDDIPF","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0AGE2","disprot_id":"DP02137","ncbi_taxon_id":83333,"regions_counter":1,"creator":"thorvath","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":178,"region_id":"DP02137r001","released":"2023_12","ec_id":"ECO:0006220","reference_html":"The C-terminal domain of full-length E. coli SSB is disordered even when bound to DNA. <i> Savvides SN, Raghunathan S, Fütterer K, Kozlov AG, Lohman TM, Waksman G. </i> Protein Sci, 2004","statement":[{"text":"The C-terminal domain of full-length E. coli SSB is disordered even when bound to DNA","type":"Title"},{"text":"The crystal structure of full-length homotetrameric single-stranded DNA (ssDNA)-binding protein from Escherichia coli (SSB) has been determined to 3.3 Å resolution and reveals that the entire C-terminal domain is disordered even in the presence of ssDNA.","type":"Abstract"},{"text":"Although the effective resolution of our analysis is a limiting 3.3 Å, the sharp contrast in electron density quality between the disordered C-terminal domain and the well-ordered core domain strongly suggests that our interpretation is qualitatively correct. Furthermore, the low-resolution diffraction of SSB-dC(pC)34 crystals is consistent with the observed molecular disorder and with the consensus that macromolecules with high degrees of flexibility and/or lack of regular structure either fail to crystallize or yield weakly diffracting crystals.","type":"Results"},{"text":"The core domain of SSB could be readily modeled in the experimental electron density maps up to residue 112 in each molecule, whereas the electron density of the anticipated C-terminal domain was undecipherable suggesting extreme disorder.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":114,"term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15169953","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-12-14T12:17:55.582Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0002-0341-4888","cross_refs":[{"db":"PDB","id":"1SRU"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T14:31:45.149Z"}}],"released":"2018_11","uniref100":"UniRef100_P0AGE2","date":"2018-08-27T17:51:31.000Z","acc":"P0AGE0","name":"Single-stranded DNA-binding protein","length":178,"organism":"Escherichia coli (strain K12)","dataset":["Condensates-related proteins"],"UniParc":"UPI0000135FA7","genes":[{"name":{"value":"ssb"},"synonyms":[{"value":"exrB"},{"value":"lexC"}],"olnNames":[{"value":"b4059"},{"value":"JW4020"}]}],"alphafold_very_low_content":0.10674157303370786,"disorder_content":0.3651685393258427,"disprot_consensus":{"full":[{"start":114,"end":178,"type":"D"}],"Structural state":[{"start":114,"end":178,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00505","name":"HMG (high mobility group) box","start":95,"end":163},{"id":"PF09011","name":"HMG-box domain","start":6,"end":78}],"gene3D":[{"start":81,"end":166,"id":"1.10.30.10","name":"High mobility group box domain"},{"start":1,"end":80,"id":"1.10.30.10","name":"High mobility group box domain"}]},"uniref50":"UniRef50_P63158","sequence":"MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEDDEEDEEDEEEEEEEEDEDEEEDDDDE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_P63158","disprot_id":"DP02138","ncbi_taxon_id":10116,"regions_counter":14,"creator":"eficho","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":99,"region_id":"DP02138r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Tail-mediated collapse of HMGB1 is dynamic and occurs via differential binding of the acidic tail to the A and B domains. <i> Stott K, Watson M, Howe FS, Grossmann JG, Thomas JO. </i> J Mol Biol, 2010","term_id":"IDPO:0000002","curator_id":"ahatos","start":73,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20691192","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":99,"term_name":"flexible linker","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Tail-mediated collapse of HMGB1 is dynamic and occurs via differential binding of the acidic tail to the A and B domains. <i> Stott K, Watson M, Howe FS, Grossmann JG, Thomas JO. </i> J Mol Biol, 2010","term_id":"IDPO:0000033","curator_id":"ahatos","start":73,"term_ontology":"IDPO","curator_name":"András Hatos","reference_id":"20691192","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP02138r002","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":184,"region_id":"DP02138r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Tail-mediated collapse of HMGB1 is dynamic and occurs via differential binding of the acidic tail to the A and B domains. <i> Stott K, Watson M, Howe FS, Grossmann JG, Thomas JO. </i> J Mol Biol, 2010","term_id":"IDPO:0000002","curator_id":"thorvath","start":165,"term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"20691192","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":184,"term_name":"flexible linker","start":165,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"thorvath","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"20691192","version":3,"reference_html":"Tail-mediated collapse of HMGB1 is dynamic and occurs via differential binding of the acidic tail to the A and B domains. <i> Stott K, Watson M, Howe FS, Grossmann JG, Thomas JO. </i> J Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006165","region_id":"DP02138r004","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":184,"region_id":"DP02138r005","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Tail-mediated collapse of HMGB1 is dynamic and occurs via differential binding of the acidic tail to the A and B domains. <i> Stott K, Watson M, Howe FS, Grossmann JG, Thomas JO. </i> J Mol Biol, 2010","term_id":"IDPO:0000002","curator_id":"thorvath","start":165,"term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"20691192","version":2,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","reference_source":"pmid","ec_ontology":"ECO","end":184,"term_name":"flexible linker","start":165,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","curator_id":"thorvath","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"20691192","version":3,"reference_html":"Tail-mediated collapse of HMGB1 is dynamic and occurs via differential binding of the acidic tail to the A and B domains. <i> Stott K, Watson M, Howe FS, Grossmann JG, Thomas JO. </i> J Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000033","ec_id":"ECO:0006210","region_id":"DP02138r006","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":214,"region_id":"DP02138r007","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Tail-mediated collapse of HMGB1 is dynamic and occurs via differential binding of the acidic tail to the A and B domains. <i> Stott K, Watson M, Howe FS, Grossmann JG, Thomas JO. </i> J Mol Biol, 2010","term_id":"IDPO:0000002","curator_id":"thorvath","start":184,"term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"20691192","version":2,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":214,"term_name":"protein binding","start":184,"ec_name":"small-angle X-ray scattering evidence used in manual assertion","curator_id":"thorvath","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Horvath","reference_id":"20691192","version":3,"reference_html":"Tail-mediated collapse of HMGB1 is dynamic and occurs via differential binding of the acidic tail to the A and B domains. <i> Stott K, Watson M, Howe FS, Grossmann JG, Thomas JO. </i> J Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006210","region_id":"DP02138r008","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":214,"region_id":"DP02138r009","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Tail-mediated collapse of HMGB1 is dynamic and occurs via differential binding of the acidic tail to the A and B domains. <i> Stott K, Watson M, Howe FS, Grossmann JG, Thomas JO. </i> J Mol Biol, 2010","term_id":"IDPO:0000002","curator_id":"thorvath","start":184,"term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"20691192","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":214,"term_name":"protein binding","start":184,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_id":"thorvath","released":"2022_03","term_ontology":"GO","curator_name":"Tamas Horvath","reference_id":"20691192","version":3,"reference_html":"Tail-mediated collapse of HMGB1 is dynamic and occurs via differential binding of the acidic tail to the A and B domains. <i> Stott K, Watson M, Howe FS, Grossmann JG, Thomas JO. </i> J Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006165","region_id":"DP02138r010","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":185,"end":214,"reference_id":"38331917","reference_source":"pmid","reference_html":"The acidic intrinsically disordered region of the inflammatory mediator HMGB1 mediates fuzzy interactions with CXCL12. <i> Mantonico MV, De Leo F, Quilici G, Colley LS, De Marchis F, Crippa M, Mezzapelle R, Schulte T, Zucchelli C, Pastorello C, Carmeno C, Caprioglio F, Ricagno S, Giachin G, Ghitti M, Bianchi ME, Musco G. </i> Nat Commun, 2024","date":"2024-05-09T20:35:45.224Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02138r011","statement":[{"text":"The dynamic nature of the acidic IDR interaction with CXCL12 was further confirmed by NMR titrations of recombinant 15N acidic IDR (Acpeprec) with unlabelled CXCL12. As is typical for fuzzy interactions involving IDRs or intrinsically disordered proteins (IDPs) the 1H-15N HSQC spectrum of 15N Ac-peprec, in both the absence and presence of equimolar CXCL12, displayed reduced peak dispersion and high signal overlap, with minimal chemical shift perturbations (Fig. 4a).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:53:34.268Z"}},{"start":185,"end":214,"reference_id":"38331917","reference_source":"pmid","reference_html":"The acidic intrinsically disordered region of the inflammatory mediator HMGB1 mediates fuzzy interactions with CXCL12. <i> Mantonico MV, De Leo F, Quilici G, Colley LS, De Marchis F, Crippa M, Mezzapelle R, Schulte T, Zucchelli C, Pastorello C, Carmeno C, Caprioglio F, Ricagno S, Giachin G, Ghitti M, Bianchi ME, Musco G. </i> Nat Commun, 2024","date":"2024-05-09T20:46:05.190Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02138r012","statement":[{"text":"We therefore focused our SAXS analysis on the sample comprising two CXCL12\nequivalents. We observed an overall increase of the derived parameters with respect to free frHMGB1, compatible with complex formation (Rg of 2.93 nm and Dmax of 10.5 nm) and a mass estimation corresponding to frHMGB1•CXCL12 heterocomplex (Supplementary Fig. 8a). The normalized Kratky plot and the P(r) plot confirmed the dynamic and flexible nature of the complex, containing both folded domains and unstructured segments (Fig. 7b, Supplementary Fig. 8b).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:53:30.505Z"}},{"start":185,"end":214,"reference_id":"38331917","reference_source":"pmid","reference_html":"The acidic intrinsically disordered region of the inflammatory mediator HMGB1 mediates fuzzy interactions with CXCL12. <i> Mantonico MV, De Leo F, Quilici G, Colley LS, De Marchis F, Crippa M, Mezzapelle R, Schulte T, Zucchelli C, Pastorello C, Carmeno C, Caprioglio F, Ricagno S, Giachin G, Ghitti M, Bianchi ME, Musco G. </i> Nat Commun, 2024","date":"2024-05-09T20:48:32.526Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0046982","term_name":"protein heterodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P48061","operator":null,"partner_start":23,"partner_end":89}],"region_id":"DP02138r013","statement":[{"text":"We therefore focused our SAXS analysis on the sample comprising two CXCL12\nequivalents. We observed an overall increase of the derived parameters with respect to free frHMGB1, compatible with complex formation (Rg of 2.93 nm and Dmax of 10.5 nm) and a mass estimation corresponding to frHMGB1•CXCL12 heterocomplex (Supplementary Fig. 8a). The normalized Kratky plot and the P(r) plot confirmed the dynamic and flexible nature of the complex, containing both folded domains and unstructured segments (Fig. 7b, Supplementary Fig. 8b).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a nonidentical protein to form a heterodimer.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:53:47.651Z"}},{"start":185,"end":214,"reference_id":"38331917","reference_source":"pmid","reference_html":"The acidic intrinsically disordered region of the inflammatory mediator HMGB1 mediates fuzzy interactions with CXCL12. <i> Mantonico MV, De Leo F, Quilici G, Colley LS, De Marchis F, Crippa M, Mezzapelle R, Schulte T, Zucchelli C, Pastorello C, Carmeno C, Caprioglio F, Ricagno S, Giachin G, Ghitti M, Bianchi ME, Musco G. </i> Nat Commun, 2024","date":"2024-05-09T20:52:47.185Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0046982","term_name":"protein heterodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P48061","operator":null,"partner_start":23,"partner_end":89}],"region_id":"DP02138r014","statement":[{"text":"Taken together, comparison of 15N CXCL12 NMR titrations with frHMGB1 fragments revealed that the acidic IDR of HMGB1 is directly involved in frHMGB1•CXCL12 heterocomplex formation and that the CXCL12 dimerization surface works as hub for multivalent interactions with both the acidic IDR and the HMG tandem domain.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a nonidentical protein to form a heterodimer.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:53:45.920Z"}}],"released":"2018_11","uniref100":"UniRef100_P63158","date":"2018-08-27T17:52:30.000Z","acc":"P63159","name":"High mobility group protein B1","length":215,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI00000008A6","genes":[{"name":{"value":"Hmgb1"},"synonyms":[{"value":"Hmg-1"},{"value":"Hmg1"}]}],"alphafold_very_low_content":0.21395348837209302,"disorder_content":0.3581395348837209,"disprot_consensus":{"full":[{"start":73,"end":99,"type":"D"},{"start":165,"end":214,"type":"D"}],"Structural state":[{"start":73,"end":99,"type":"D"},{"start":165,"end":214,"type":"D"}],"Disorder function":[{"start":73,"end":99,"type":"F"},{"start":165,"end":184,"type":"F"}],"Molecular function":[{"start":184,"end":214,"type":"F"}]}},{"features":{"pfam":[{"id":"PF13329","name":"Autophagy-related protein 2","start":13,"end":240},{"id":"PF13329","name":"Autophagy-related protein 2","start":1110,"end":1436},{"id":"PF13329","name":"Autophagy-related protein 2","start":1475,"end":1932}]},"uniref50":"UniRef50_Q2TAZ0","sequence":"MSRWLWPWSNCVKERVCRYLLHHYLGHFFQEHLSLDQLSLDLYKGSVALRDIHLEIWSVNEVLESMESPLELVEGFVGSIEVAVPWAALLTDHCTVRVSGLQLTLQPRRGPAPGAADSQSWASCMTTSLQLAQECLRDGLPEPSEPPQPLEGLEMFAQTIETVLRRIKVTFLDTVVRVEHSPGDGERGVAVEVRVQRLEYCDEAVRDPSQAPPVDVHQPPAFLHKLLQLAGVRLHYEELPAQEEPPEPPLQIGSCSGYMELMVKLKQNEAFPGPKLEVAGQLGSLHLLLTPRQLQQLQELLSAVSLTDHEGLADKLNKSRPLGAEDLWLIEQDLNQQLQAGAVAEPLSPDPLTNPLLNLDNTDLFFSMAGLTSSVASALSELSLSDVDLASSVRSDMASRRLSAQAHPAGKMAPNPLLDTMRPDSLLKMTLGGVTLTLLQTSAPSSGPPDLATHFFTEFDATKDGPFGSRDFHHLRPRFQRACPCSHVRLTGTAVQLSWELRTGSRGRRTTSMEVHFGQLEVLECLWPRGTSEPEYTEILTFPGTLGSQASARPCAHLRHTQILRRVPKSRPRRSVACHCHSELALDLANFQADVELGALDRLAALLRLATVPAEPPAGLLTEPLPAMEQQTVFRLSAPRATLRLRFPIADLRPEPDPWAGQAVRAEQLRLELSEPQFRSELSSGPGPPVPTHLELTCSDLHGIYEDGGKPPVPCLRVSKALDPKSTGRKYFLPQVVVTVNPQSSSTQWEVAPEKGEELELSVESPCELREPEPSPFSSKRTMYETEEMVIPGDPEEMRTFQSRTLALSRCSLEVILPSVHIFLPSKEVYESIYNRINNDLLMWEPADLLPTPDPAAQPSGFPGPSGFWHDSFKMCKSAFKLANCFDLTPDSDSDDEDAHFFSVGASGGPQAAAPEAPSLHLQSTFSTLVTVLKGRITALCETKDEGGKRLEAVHGELVLDMEHGTLFSVSQYCGQPGLGYFCLEAEKATLYHRAAVDDYPLPSHLDLPSFAPPAQLAPTIYPSEEGVTERGASGRKGQGRGPHMLSTAVRIHLDPHKNVKEFLVTLRLHKATLRHYMALPEQSWHSQLLEFLDVLDDPVLGYLPPTVITILHTHLFSCSVDYRPLYLPVRVLITAETFTLSSNIIMDTSTFLLRFILDDSALYLSDKCEVETLDLRRDYVCVLDVDLLELVIKTWKGSTEGKLSQPLFELRCSNNVVHVHSCADSCALLVNLLQYVMSTGDLHPPPRPPSPTEIAGQKLSESPASLPSCPPVETALINQRDLADALLDTERSLRELAQPSGGHLPQASPISVYLFPGERSGAPPPSPPVGGPAGSLGSCSEEKEDEREEEGDGDTLDSDEFCILDAPGLGIPPRDGEPVVTQLHPGPIVVRDGYFSRPIGSTDLLRAPAHFPVPSTRVVLREVSLVWHLYGGRDFGPHPGHRARTGLSGPRSSPSRCSGPNRPQNSWRTQGGSGRQHHVLMEIQLSKVSFQHEVYPAEPATGPAAPSQELEERPLSRQVFIVQELEVRDRLASSQINKFLYLHTSERMPRRAHSNMLTIKALHVAPTTNLGGPECCLRVSLMPLRLNVDQDALFFLKDFFTSLVAGINPVVPGETSAEARPETRAQPSSPLEGQAEGVETTGSQEAPGGGHSPSPPDQQPIYFREFRFTSEVPIWLDYHGKHVTMDQVGTFAGLLIGLAQLNCSELKLKRLCCRHGLLGVDKVLGYALNEWLQDIRKNQLPGLLGGVGPMHSVVQLFQGFRDLLWLPIEQYRKDGRLMRGLQRGAASFGSSTASAALELSNRLVQAIQATAETVYDILSPAAPVSRSLQDKRSARRLRRGQQPADLREGVAKAYDTVREGILDTAQTICDVASRGHEQKGLTGAVGGVIRQLPPTVVKPLILATEATSSLLGGMRNQIVPDAHKDHALKWRSDSAQD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q2TAZ0","disprot_id":"DP02142","ncbi_taxon_id":9606,"regions_counter":26,"creator":"baykac","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1273,"region_id":"DP02142r001","released":"2024_12","ec_id":"ECO:0006204","reference_html":"Identifying intrinsically disordered protein regions likely to undergo binding-induced helical transitions. <i> Glover K, Mei Y, Sinha SC. </i> Biochim Biophys Acta, 2016","term_id":"IDPO:0000002","curator_id":"vnugnes","start":1244,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-09-06T15:44:52.462Z","reference_source":"pmid","term_name":"disorder","reference_id":"27179590","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Secondary structure content estimated by analysis of CD spectra for each of the thirteen IDRs showed that none contained more than two residues in a helical conformation (Figures 1-​-3,3, Table 3-​-5),5), which is insufficient for the formation of a stable α-helix requiring a minimum of six residues.","type":"Results"},{"text":"However, the marginal secondary structure content suggests that all the peptides tested are IDRs.","type":"Results"}]},{"start":1,"end":172,"reference_id":"39174844","reference_source":"pmid","reference_html":"Structural basis for lipid transfer by the ATG2A-ATG9A complex. <i> Wang Y, Dahmane S, Ti R, Mai X, Zhu L, Carlson LA, Stjepanovic G. </i> Nat Struct Mol Biol, 2024","date":"2024-09-06T13:47:25.471Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8KBY"}],"region_id":"DP02142r002","statement":[{"text":"Most of the main chain in ATG2A could be traced except for two long loop regions (residues 304–424 and 1237–1416) that were not visible in the map (Fig. 1a). The N-terminal domain responsible for lipid extraction and ATG_C were also too flexible to directly model.","type":"Results"}]},{"start":304,"end":424,"reference_id":"39174844","reference_source":"pmid","reference_html":"Structural basis for lipid transfer by the ATG2A-ATG9A complex. <i> Wang Y, Dahmane S, Ti R, Mai X, Zhu L, Carlson LA, Stjepanovic G. </i> Nat Struct Mol Biol, 2024","date":"2024-09-06T13:48:49.213Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8KBY"}],"region_id":"DP02142r003","statement":[{"text":"Most of the main chain in ATG2A could be traced except for two long loop regions (residues 304–424 and 1237–1416) that were not visible in the map (Fig. 1a). The N-terminal domain responsible for lipid extraction and ATG_C were also too flexible to directly model.","type":"Results"}]},{"start":1237,"end":1416,"reference_id":"39174844","reference_source":"pmid","reference_html":"Structural basis for lipid transfer by the ATG2A-ATG9A complex. <i> Wang Y, Dahmane S, Ti R, Mai X, Zhu L, Carlson LA, Stjepanovic G. </i> Nat Struct Mol Biol, 2024","date":"2024-09-06T13:49:41.962Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8KBY"}],"region_id":"DP02142r004","statement":[{"text":"Most of the main chain in ATG2A could be traced except for two long loop regions (residues 304–424 and 1237–1416) that were not visible in the map (Fig. 1a). The N-terminal domain responsible for lipid extraction and ATG_C were also too flexible to directly model.","type":"Results"}]},{"start":1736,"end":1938,"reference_id":"39174844","reference_source":"pmid","reference_html":"Structural basis for lipid transfer by the ATG2A-ATG9A complex. <i> Wang Y, Dahmane S, Ti R, Mai X, Zhu L, Carlson LA, Stjepanovic G. </i> Nat Struct Mol Biol, 2024","date":"2024-09-06T13:50:02.480Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8KBY"}],"region_id":"DP02142r005","statement":[{"text":"Most of the main chain in ATG2A could be traced except for two long loop regions (residues 304–424 and 1237–1416) that were not visible in the map (Fig. 1a). The N-terminal domain responsible for lipid extraction and ATG_C were also too flexible to directly model.","type":"Results"}]},{"start":204,"end":220,"reference_id":"39174844","reference_source":"pmid","reference_html":"Structural basis for lipid transfer by the ATG2A-ATG9A complex. <i> Wang Y, Dahmane S, Ti R, Mai X, Zhu L, Carlson LA, Stjepanovic G. </i> Nat Struct Mol Biol, 2024","date":"2024-09-06T13:51:14.611Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8KBY"},{"db":"EMDB","id":"37087"}],"region_id":"DP02142r006","statement":[{"text":"Most of the main chain in ATG2A could be traced except for two long loop regions (residues 304–424 and 1237–1416) that were not visible in the map (Fig. 1a). The N-terminal domain responsible for lipid extraction and ATG_C were also too flexible to directly model.","type":"Results"},{"text":"The Cryo-EM structure deposited in PDB shows this region lacks electron density, indicating it is also disordered. ","type":"Curator statement"}]},{"start":464,"end":483,"reference_id":"39174844","reference_source":"pmid","reference_html":"Structural basis for lipid transfer by the ATG2A-ATG9A complex. <i> Wang Y, Dahmane S, Ti R, Mai X, Zhu L, Carlson LA, Stjepanovic G. </i> Nat Struct Mol Biol, 2024","date":"2024-09-06T13:51:36.147Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8KBY"},{"db":"EMDB","id":"37087"}],"region_id":"DP02142r007","statement":[{"text":"Most of the main chain in ATG2A could be traced except for two long loop regions (residues 304–424 and 1237–1416) that were not visible in the map (Fig. 1a). The N-terminal domain responsible for lipid extraction and ATG_C were also too flexible to directly model.","type":"Results"},{"text":"The Cryo-EM structure deposited in PDB shows this region lacks electron density, indicating it is also disordered. ","type":"Curator statement"}]},{"start":617,"end":628,"reference_id":"39174844","reference_source":"pmid","reference_html":"Structural basis for lipid transfer by the ATG2A-ATG9A complex. <i> Wang Y, Dahmane S, Ti R, Mai X, Zhu L, Carlson LA, Stjepanovic G. </i> Nat Struct Mol Biol, 2024","date":"2024-09-06T13:51:53.751Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8KBY"},{"db":"EMDB","id":"37087"}],"region_id":"DP02142r008","statement":[{"text":"Most of the main chain in ATG2A could be traced except for two long loop regions (residues 304–424 and 1237–1416) that were not visible in the map (Fig. 1a). The N-terminal domain responsible for lipid extraction and ATG_C were also too flexible to directly model.","type":"Results"},{"text":"The Cryo-EM structure deposited in PDB shows this region lacks electron density, indicating it is also disordered. ","type":"Curator statement"}]},{"start":747,"end":793,"reference_id":"39174844","reference_source":"pmid","reference_html":"Structural basis for lipid transfer by the ATG2A-ATG9A complex. <i> Wang Y, Dahmane S, Ti R, Mai X, Zhu L, Carlson LA, Stjepanovic G. </i> Nat Struct Mol Biol, 2024","date":"2024-09-06T13:52:06.715Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8KBY"},{"db":"EMDB","id":"37087"}],"region_id":"DP02142r009","statement":[{"text":"Most of the main chain in ATG2A could be traced except for two long loop regions (residues 304–424 and 1237–1416) that were not visible in the map (Fig. 1a). The N-terminal domain responsible for lipid extraction and ATG_C were also too flexible to directly model.","type":"Results"},{"text":"The Cryo-EM structure deposited in PDB shows this region lacks electron density, indicating it is also disordered. ","type":"Curator statement"}]},{"start":850,"end":923,"reference_id":"39174844","reference_source":"pmid","reference_html":"Structural basis for lipid transfer by the ATG2A-ATG9A complex. <i> Wang Y, Dahmane S, Ti R, Mai X, Zhu L, Carlson LA, Stjepanovic G. </i> Nat Struct Mol Biol, 2024","date":"2024-09-06T13:52:17.608Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8KBY"},{"db":"EMDB","id":"37087"}],"region_id":"DP02142r010","statement":[{"text":"Most of the main chain in ATG2A could be traced except for two long loop regions (residues 304–424 and 1237–1416) that were not visible in the map (Fig. 1a). The N-terminal domain responsible for lipid extraction and ATG_C were also too flexible to directly model.","type":"Results"},{"text":"The Cryo-EM structure deposited in PDB shows this region lacks electron density, indicating it is also disordered. ","type":"Curator statement"}]},{"start":940,"end":957,"reference_id":"39174844","reference_source":"pmid","reference_html":"Structural basis for lipid transfer by the ATG2A-ATG9A complex. <i> Wang Y, Dahmane S, Ti R, Mai X, Zhu L, Carlson LA, Stjepanovic G. </i> Nat Struct Mol Biol, 2024","date":"2024-09-06T13:52:36.847Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8KBY"},{"db":"EMDB","id":"37087"}],"region_id":"DP02142r011","statement":[{"text":"Most of the main chain in ATG2A could be traced except for two long loop regions (residues 304–424 and 1237–1416) that were not visible in the map (Fig. 1a). The N-terminal domain responsible for lipid extraction and ATG_C were also too flexible to directly model.","type":"Results"},{"text":"The Cryo-EM structure deposited in PDB shows this region lacks electron density, indicating it is also disordered. ","type":"Curator statement"}]},{"start":996,"end":1015,"reference_id":"39174844","reference_source":"pmid","reference_html":"Structural basis for lipid transfer by the ATG2A-ATG9A complex. <i> Wang Y, Dahmane S, Ti R, Mai X, Zhu L, Carlson LA, Stjepanovic G. </i> Nat Struct Mol Biol, 2024","date":"2024-09-06T13:53:11.692Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8KBY"},{"db":"EMDB","id":"37087"}],"region_id":"DP02142r012","statement":[{"text":"Most of the main chain in ATG2A could be traced except for two long loop regions (residues 304–424 and 1237–1416) that were not visible in the map (Fig. 1a). The N-terminal domain responsible for lipid extraction and ATG_C were also too flexible to directly model.","type":"Results"},{"text":"The Cryo-EM structure deposited in PDB shows this region lacks electron density, indicating it is also disordered. ","type":"Curator statement"}]},{"start":1025,"end":1041,"reference_id":"39174844","reference_source":"pmid","reference_html":"Structural basis for lipid transfer by the ATG2A-ATG9A complex. <i> Wang Y, Dahmane S, Ti R, Mai X, Zhu L, Carlson LA, Stjepanovic G. </i> Nat Struct Mol Biol, 2024","date":"2024-09-06T13:53:22.083Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8KBY"},{"db":"EMDB","id":"37087"}],"region_id":"DP02142r013","statement":[{"text":"Most of the main chain in ATG2A could be traced except for two long loop regions (residues 304–424 and 1237–1416) that were not visible in the map (Fig. 1a). The N-terminal domain responsible for lipid extraction and ATG_C were also too flexible to directly model.","type":"Results"},{"text":"The Cryo-EM structure deposited in PDB shows this region lacks electron density, indicating it is also disordered. ","type":"Curator statement"}]},{"start":441,"end":450,"reference_id":"39174844","reference_source":"pmid","reference_html":"Structural basis for lipid transfer by the ATG2A-ATG9A complex. <i> Wang Y, Dahmane S, Ti R, Mai X, Zhu L, Carlson LA, Stjepanovic G. </i> Nat Struct Mol Biol, 2024","date":"2024-09-06T13:53:42.819Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8KBY"},{"db":"EMDB","id":"37087"}],"region_id":"DP02142r014","statement":[{"text":"Most of the main chain in ATG2A could be traced except for two long loop regions (residues 304–424 and 1237–1416) that were not visible in the map (Fig. 1a). The N-terminal domain responsible for lipid extraction and ATG_C were also too flexible to directly model.","type":"Results"},{"text":"The Cryo-EM structure deposited in PDB shows this region lacks electron density, indicating it is also disordered. ","type":"Curator statement"}]},{"start":1430,"end":1478,"reference_id":"39174844","reference_source":"pmid","reference_html":"Structural basis for lipid transfer by the ATG2A-ATG9A complex. <i> Wang Y, Dahmane S, Ti R, Mai X, Zhu L, Carlson LA, Stjepanovic G. </i> Nat Struct Mol Biol, 2024","date":"2024-09-06T13:54:16.766Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8KBY"},{"db":"EMDB","id":"37087"}],"region_id":"DP02142r015","statement":[{"text":"Most of the main chain in ATG2A could be traced except for two long loop regions (residues 304–424 and 1237–1416) that were not visible in the map (Fig. 1a). The N-terminal domain responsible for lipid extraction and ATG_C were also too flexible to directly model.","type":"Results"},{"text":"The Cryo-EM structure deposited in PDB shows this region lacks electron density, indicating it is also disordered. ","type":"Curator statement"}]},{"start":1497,"end":1513,"reference_id":"39174844","reference_source":"pmid","reference_html":"Structural basis for lipid transfer by the ATG2A-ATG9A complex. <i> Wang Y, Dahmane S, Ti R, Mai X, Zhu L, Carlson LA, Stjepanovic G. </i> Nat Struct Mol Biol, 2024","date":"2024-09-06T13:54:36.124Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8KBY"},{"db":"EMDB","id":"37087"}],"region_id":"DP02142r016","statement":[{"text":"Most of the main chain in ATG2A could be traced except for two long loop regions (residues 304–424 and 1237–1416) that were not visible in the map (Fig. 1a). The N-terminal domain responsible for lipid extraction and ATG_C were also too flexible to directly model.","type":"Results"},{"text":"The Cryo-EM structure deposited in PDB shows this region lacks electron density, indicating it is also disordered. ","type":"Curator statement"}]},{"start":1543,"end":1554,"reference_id":"39174844","reference_source":"pmid","reference_html":"Structural basis for lipid transfer by the ATG2A-ATG9A complex. <i> Wang Y, Dahmane S, Ti R, Mai X, Zhu L, Carlson LA, Stjepanovic G. </i> Nat Struct Mol Biol, 2024","date":"2024-09-06T13:55:02.213Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8KBY"},{"db":"EMDB","id":"37087"}],"region_id":"DP02142r017","statement":[{"text":"Most of the main chain in ATG2A could be traced except for two long loop regions (residues 304–424 and 1237–1416) that were not visible in the map (Fig. 1a). The N-terminal domain responsible for lipid extraction and ATG_C were also too flexible to directly model.","type":"Results"},{"text":"The Cryo-EM structure deposited in PDB shows this region lacks electron density, indicating it is also disordered. ","type":"Curator statement"}]},{"start":1566,"end":1575,"reference_id":"39174844","reference_source":"pmid","reference_html":"Structural basis for lipid transfer by the ATG2A-ATG9A complex. <i> Wang Y, Dahmane S, Ti R, Mai X, Zhu L, Carlson LA, Stjepanovic G. </i> Nat Struct Mol Biol, 2024","date":"2024-09-06T13:55:24.495Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8KBY"},{"db":"EMDB","id":"37087"}],"region_id":"DP02142r018","statement":[{"text":"Most of the main chain in ATG2A could be traced except for two long loop regions (residues 304–424 and 1237–1416) that were not visible in the map (Fig. 1a). The N-terminal domain responsible for lipid extraction and ATG_C were also too flexible to directly model.","type":"Results"},{"text":"The Cryo-EM structure deposited in PDB shows this region lacks electron density, indicating it is also disordered. ","type":"Curator statement"}]},{"start":1615,"end":1664,"reference_id":"39174844","reference_source":"pmid","reference_html":"Structural basis for lipid transfer by the ATG2A-ATG9A complex. <i> Wang Y, Dahmane S, Ti R, Mai X, Zhu L, Carlson LA, Stjepanovic G. </i> Nat Struct Mol Biol, 2024","date":"2024-09-06T13:55:36.415Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8KBY"},{"db":"EMDB","id":"37087"}],"region_id":"DP02142r019","statement":[{"text":"Most of the main chain in ATG2A could be traced except for two long loop regions (residues 304–424 and 1237–1416) that were not visible in the map (Fig. 1a). The N-terminal domain responsible for lipid extraction and ATG_C were also too flexible to directly model.","type":"Results"},{"text":"The Cryo-EM structure deposited in PDB shows this region lacks electron density, indicating it is also disordered. ","type":"Curator statement"}]},{"start":1679,"end":1690,"reference_id":"39174844","reference_source":"pmid","reference_html":"Structural basis for lipid transfer by the ATG2A-ATG9A complex. <i> Wang Y, Dahmane S, Ti R, Mai X, Zhu L, Carlson LA, Stjepanovic G. </i> Nat Struct Mol Biol, 2024","date":"2024-09-06T13:55:46.050Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8KBY"},{"db":"EMDB","id":"37087"}],"region_id":"DP02142r020","statement":[{"text":"Most of the main chain in ATG2A could be traced except for two long loop regions (residues 304–424 and 1237–1416) that were not visible in the map (Fig. 1a). The N-terminal domain responsible for lipid extraction and ATG_C were also too flexible to directly model.","type":"Results"},{"text":"The Cryo-EM structure deposited in PDB shows this region lacks electron density, indicating it is also disordered. ","type":"Curator statement"}]},{"start":12,"end":16,"reference_id":"39174844","reference_source":"pmid","reference_html":"Structural basis for lipid transfer by the ATG2A-ATG9A complex. <i> Wang Y, Dahmane S, Ti R, Mai X, Zhu L, Carlson LA, Stjepanovic G. </i> Nat Struct Mol Biol, 2024","date":"2024-09-06T15:27:14.445Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0120013","term_name":"lipid transfer activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys13Asp","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To verify these findings, we designed three mutants, K13D, R15D and Y200E;K255E, and examined their lipid transfer activities in vitro (Supplementary Fig. 5a)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg15Asp","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To verify these findings, we designed three mutants, K13D, R15D and Y200E;K255E, and examined their lipid transfer activities in vitro (Supplementary Fig. 5a)."}]}],"cross_refs":[{"db":"PDB","id":"8KBY"},{"db":"EMDB","id":"37087"}],"ec_go":"IMP","region_id":"DP02142r021","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"10350317","statements":[{"type":"Results","text":"The highly curved small unilamellar vesicles (SUVs) met the curvature requirement for phospholipid transfer by ATG2A and were used as the lipid donor and acceptor. The SUVs were composed of 75% DOPC, 15% 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE), 8% nitrobenzoxadiazole (NBD)–PE and 2% rhodamine–PE for the donor and 75% DOPC and 25% DOPE for the acceptor."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"9546757","statements":[{"type":"Results","text":"The highly curved small unilamellar vesicles (SUVs) met the curvature requirement for phospholipid transfer by ATG2A and were used as the lipid donor and acceptor. The SUVs were composed of 75% DOPC, 15% 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE), 8% nitrobenzoxadiazole (NBD)–PE and 2% rhodamine–PE for the donor and 75% DOPC and 25% DOPE for the acceptor.N-(7-nitrobenz-2-oxa-1,3-diazol-4-il)-1,2-dihexadecanoil-sn-glicero-3-fosfoetanolamina, sal de trietilamonio"}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"21284689","statements":[{"type":"Results","text":"The highly curved small unilamellar vesicles (SUVs) met the curvature requirement for phospholipid transfer by ATG2A and were used as the lipid donor and acceptor. The SUVs were composed of 75% DOPC, 15% 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE), 8% nitrobenzoxadiazole (NBD)–PE and 2% rhodamine–PE for the donor and 75% DOPC and 25% DOPE for the acceptor."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"6694","statements":[{"type":"Results","text":"The highly curved small unilamellar vesicles (SUVs) met the curvature requirement for phospholipid transfer by ATG2A and were used as the lipid donor and acceptor. The SUVs were composed of 75% DOPC, 15% 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE), 8% nitrobenzoxadiazole (NBD)–PE and 2% rhodamine–PE for the donor and 75% DOPC and 25% DOPE for the acceptor."}]}],"statement":[{"text":"The transfer of NBD–PE and/or rhodamine–PE to acceptor liposomes, as well as the transfer of nonfluorescent lipids to donor liposomes, would result in FRET pair dilution and an increase in NBD fluorescence (Fig. 3f). The wild-type ATG2A can transfer lipids between donor and acceptor liposomes, resulting in increased NBD fluorescence. All three mutants showed substantially reduced activity relative to the wild-type protein, which confirms the simulation predictions (Fig. 3g).","type":"Results"}],"term_comment":"","term_def":"\"Removes a lipid from a membrane or a monolayer lipid particle, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to an acceptor membrane or lipid particle. This results in intermembrane transfer of lipids.\" [GOC:krc, PMID:20823909, PMID:24220498, PMID:25797198]","term_is_obsolete":false,"term_not_annotate":false},{"start":1374,"end":1404,"reference_id":"32483132","reference_source":"pmid","reference_html":"Multi-site-mediated entwining of the linear WIR-motif around WIPI β-propellers for autophagy. <i> Ren J, Liang R, Wang W, Zhang D, Yu L, Feng W. </i> Nat Commun, 2020","date":"2024-09-19T09:52:30.153Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q5MNZ6","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02142r022","statement":[{"text":"Based on the primary sequence analysis of ATG2, we removed the N-terminal 15 residues from this region and used the two fragments of ATG2A (the long fragment (1358–1404) and short fragment (1374–1404), referred to as ATG2Along and ATG2Ashort, respectively) tagged with GB1 for the isothermal titration calorimetry (ITC) assay (Supplementary Fig. 1a, b). As the control, GB1 alone did not bind to WIPI3, but both ATG2Along and ATG2Ashort bound to WIPI3 with a similar affinity (with the Kd of 8.6 ± 0.1 μM and 8.7 ± 0.1 μM, respectively) (Supplementary Fig. 1c), indicating that the N-terminal 15 residues of ATG2Along is not involved in the binding to WIPI3. Thus, ATG2Ashort could be the minimum WIPI-interacting region in ATG2A for binding to WIPI3 and was referred to as the WIR-peptide.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1378,"end":1399,"reference_id":"32483132","reference_source":"pmid","reference_html":"Multi-site-mediated entwining of the linear WIR-motif around WIPI β-propellers for autophagy. <i> Ren J, Liang R, Wang W, Zhang D, Yu L, Feng W. </i> Nat Commun, 2020","date":"2024-09-19T10:44:03.163Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Results","text":"We then adopted the fusion strategy by which the WIR-peptide is fused to either the N-terminus or C-terminus of WIPI3-Δloop to stabilize the complex or facilitate crystallization. After extensive trials, the crystals of WIPI3-Δloop with N-terminal fusion of the WIR-peptide were obtained for structural determination (Fig. 1a)."}]}],"cross_refs":[{"db":"PDB","id":"6KLR"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q5MNZ6","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02142r023","sequence_construct":"GPGSPRDGEPVVTQLHPGPIVVRDGYFSRPIGSTDGSPHGNGLLYAGFNQDHGCFACGMENGFRVYNTDPLKEKEKQEFLEGGVGHVEMLFRCNYLALVGGGKKKVMIWDDLKKKTVIEIEFSTEVKAVKLRRDRIVVVLDSMIKVFTFTHNPHQLHVFETCYNPKGLCVLCPNSNNSLLAFPGTHTGHVQLVDLASTEKPPVDIPAHEGVLSCIALNLQGTRIATASEKGTLIRIFDTSSGHLIQELRRGSQAANIYCINFNQDASLICVSSDHGTVHIFAAEDPKSKWSFSKFQVPSGSPCICAFGTEPNAVIAICADGSYYKFLFNPKGECIRDVYAQFLEMTDDKL","statement":[{"text":"The complex structure was determined by the molecular replacement method and refined to 2.2 Å (Supplementary Table 1). The WIR-peptide of ATG2A was resolved (from 1378 to 1399) based on its electron density map (Fig. 1a–c). Consistent with the stoichiometry of 1:1 in the ITC assay, a single WIR-peptide binds to WIPI3-Δloop (Fig. 1b and Supplementary Fig. 1d).","type":"Results"},{"text":"From overall structure, the WIR-peptide spans across blades 1–3 and binds to multiple inter-blade sites embedded in the β-propeller (Fig. 1d, e).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1374,"end":1404,"reference_id":"32483132","reference_source":"pmid","reference_html":"Multi-site-mediated entwining of the linear WIR-motif around WIPI β-propellers for autophagy. <i> Ren J, Liang R, Wang W, Zhang D, Yu L, Feng W. </i> Nat Commun, 2020","date":"2024-09-19T10:27:29.558Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val1381Gln","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile1389Gln","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val1391Gln","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Tyr1395Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe1396Ala","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q5MNZ6","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02142r024","statement":[{"text":"We made point mutations in each part of the WIR-peptide (V1381Q, I1389Q, V1391Q, Y1395A, and F1396A) to evaluate the essential roles of these residues for binding to WIPI3. As expected, all the mutations severely impaired the binding to WIPI3-Δloop (Fig. 3e and Supplementary Fig. 6). Consistent with mutational studies of WIPI3 (Fig. 3a), mutations in the middle segment and C-terminal tail of the WIR-peptide have more impact on the binding (Fig. 3e), supporting the primary roles of M-site and C-site and the auxiliary function of N-site.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1381,"end":1396,"reference_id":"32483132","reference_source":"pmid","reference_html":"Multi-site-mediated entwining of the linear WIR-motif around WIPI β-propellers for autophagy. <i> Ren J, Liang R, Wang W, Zhang D, Yu L, Feng W. </i> Nat Commun, 2020","date":"2024-09-19T10:48:38.083Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val1381Gln","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile1389Gln","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val1391Gln","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Tyr1395Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe1396Ala","start":null,"end":null,"position":null},{"term_id":"MI:0988","term_name":"STREP","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"GFP-tagged WIPI4 and Tandem-Strep-Flag (TSF)-tagged ATG2A (wild-type or mutants) plasmids were co-transfected into HEK293T cells (ATCC, CRL-3216) using Lipofectamine 3000 transfection reagent (Thermo Fisher Scientific)."}]}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q9Y484","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02142r025","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","statements":[{"type":"Methods","text":"GFP-tagged WIPI4 and Tandem-Strep-Flag (TSF)-tagged ATG2A (wild-type or mutants) plasmids were co-transfected into HEK293T cells (ATCC, CRL-3216) using Lipofectamine 3000 transfection reagent (Thermo Fisher Scientific)."}],"entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"As expected, mutations in each part of the WIR-motif in ATG2A (V1381Q, T1382Q, I1389Q, Y1395A, and F1396A) decreased the binding to WIPI4 (Fig. 3f), supporting that the WIR-motif is essential for ATG2A to interact with WIPI4.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1381,"end":1396,"reference_id":"32483132","reference_source":"pmid","reference_html":"Multi-site-mediated entwining of the linear WIR-motif around WIPI β-propellers for autophagy. <i> Ren J, Liang R, Wang W, Zhang D, Yu L, Feng W. </i> Nat Commun, 2020","date":"2024-09-19T10:54:55.571Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0010508","term_name":"positive regulation of autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val1381Gln","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile1389Gln","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val1391Gln","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Tyr1395Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe1396Ala","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP02142r026","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_3758","statements":[{"type":"Results","text":"To evaluate the essential role of the WIR-motif in ATG2A for its cellular functions, we further used the normal rat kidney epithelial (NRK) cells with depletions of both ATG2A and ATG2B and stable expression of GFP-tagged LC3 and also checked the autophagic flux with the presence of bafilomycin A1 (an inhibitor of autophagosome–lysosome fusion)."}],"entry_name":"Normal Rat Kidney"}],"statement":[{"text":"In contrast, transfection of all the WIR-motif mutants (V1381Q, T1382Q, I1389Q, Y1395A, and F1396A) could not rescue the depletion defect (Fig. 4a, b). Although the cellular level of LC3-positive structures was also increased after adding bafilomycin A1, the increments of LC3-positive clusters (with transfection of the ATG2A mutants) were significantly lower than that upon transfection of wild-type ATG2A (Supplementary Fig. 8). Thus, the conserved WIR-motif in ATG2A mediates the binding to WIPI4 and is essential for the ATG2A-mediated autophagic process.","type":"Results"},{"text":"Moreover, the formation of the ATG2A/WIPI4 complex was proposed to be important for the expansion and maturation of autophagosome and depletions of ATG2 proteins in mammalian cells led to the accumulation of immature phagophores21,28.","type":"Results"}],"term_comment":"","term_def":"\"Any process that activates, maintains or increases the rate of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.\" [GOC:dph, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_Q2TAZ0","date":"2018-08-27T21:49:25.000Z","acc":"Q2TAZ0","name":"Autophagy-related protein 2 homolog A","length":1938,"organism":"Homo sapiens","dataset":["Autophagy-related proteins"],"UniParc":"UPI00006633BF","genes":[{"name":{"value":"ATG2A","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"21887408","url":"http://www.ncbi.nlm.nih.gov/pubmed/21887408","alternativeUrl":"https://europepmc.org/abstract/MED/21887408"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:29028","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:29028"}}]},"synonyms":[{"value":"KIAA0404","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9455477","url":"http://www.ncbi.nlm.nih.gov/pubmed/9455477","alternativeUrl":"https://europepmc.org/abstract/MED/9455477"}}]}]}],"alphafold_very_low_content":0.2585139318885449,"disorder_content":0.5474716202270382,"disprot_consensus":{"full":[{"start":1,"end":172,"type":"D"},{"start":204,"end":220,"type":"D"},{"start":304,"end":424,"type":"D"},{"start":441,"end":450,"type":"D"},{"start":464,"end":483,"type":"D"},{"start":617,"end":628,"type":"D"},{"start":747,"end":793,"type":"D"},{"start":850,"end":923,"type":"D"},{"start":940,"end":957,"type":"D"},{"start":996,"end":1015,"type":"D"},{"start":1025,"end":1041,"type":"D"},{"start":1237,"end":1416,"type":"D"},{"start":1430,"end":1478,"type":"D"},{"start":1497,"end":1513,"type":"D"},{"start":1543,"end":1554,"type":"D"},{"start":1566,"end":1575,"type":"D"},{"start":1615,"end":1664,"type":"D"},{"start":1679,"end":1690,"type":"D"},{"start":1736,"end":1938,"type":"D"}],"Structural state":[{"start":1,"end":172,"type":"D"},{"start":204,"end":220,"type":"D"},{"start":304,"end":424,"type":"D"},{"start":441,"end":450,"type":"D"},{"start":464,"end":483,"type":"D"},{"start":617,"end":628,"type":"D"},{"start":747,"end":793,"type":"D"},{"start":850,"end":923,"type":"D"},{"start":940,"end":957,"type":"D"},{"start":996,"end":1015,"type":"D"},{"start":1025,"end":1041,"type":"D"},{"start":1237,"end":1416,"type":"D"},{"start":1430,"end":1478,"type":"D"},{"start":1497,"end":1513,"type":"D"},{"start":1543,"end":1554,"type":"D"},{"start":1566,"end":1575,"type":"D"},{"start":1615,"end":1664,"type":"D"},{"start":1679,"end":1690,"type":"D"},{"start":1736,"end":1938,"type":"D"}],"Molecular function":[{"start":12,"end":16,"type":"F"},{"start":1374,"end":1404,"type":"F"}],"Biological process":[{"start":1381,"end":1396,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00453","name":"Ribosomal protein L20","start":4,"end":106}],"gene3D":[{"start":54,"end":118,"id":"1.10.1900.20","name":"Ribosomal protein L20"}]},"uniref50":"UniRef50_P46246","sequence":"MRVKGPSSRRKKKKILKLAKGYRGQRSRSYRRAKEAVMRALYYQYRDRKLRKREFRRLWIARINAAVRAYGLNYSTFINGLKKAGIELDRKILADMAVRDPQAFEQVVNKVKEALQVQ","taxonomy":["Bacteria","Aquificae","Aquificales","Aquificaceae","Aquifex"],"uniref90":"UniRef90_O67086","disprot_id":"DP02143","ncbi_taxon_id":224324,"regions_counter":5,"creator":"couzo","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":118,"region_id":"DP02143r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Coexistence of two protein folding states in the crystal structure of ribosomal protein L20. <i> Timsit Y, Allemand F, Chiaruttini C, Springer M. </i> EMBO Rep, 2006","statement":[{"text":"Figure 4B:  Partially unfolded C terminus of form 2. Arg 90 and Lys 91 form salt bridges with Glu 87 and Asp 95, respectively.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"couzo","start":90,"term_ontology":"IDPO","curator_name":"Christos Ouzounis","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0086-8657","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2GHJ"}],"reference_id":"16977336","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":118,"term_name":"order to disorder","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Coexistence of two protein folding states in the crystal structure of ribosomal protein L20. <i> Timsit Y, Allemand F, Chiaruttini C, Springer M. </i> EMBO Rep, 2006","term_id":"IDPO:0000014","curator_id":"couzo","start":90,"term_ontology":"IDPO","curator_name":"Christos Ouzounis","reference_id":"16977336","version":2,"curator_orcid":"0000-0002-0086-8657","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02143r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":59,"region_id":"DP02143r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Coexistence of two protein folding states in the crystal structure of ribosomal protein L20. <i> Timsit Y, Allemand F, Chiaruttini C, Springer M. </i> EMBO Rep, 2006","statement":[{"text":"L20 shows a highly charged α-helical amino-terminal extension (aa 1–59) that contains clusters of conserved basic residues involved in RNA contacts in the ribosome.","type":"Introduction"}],"term_id":"IDPO:0000002","curator_id":"couzo","start":1,"term_ontology":"IDPO","curator_name":"Christos Ouzounis","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0086-8657","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2GHJ"}],"reference_id":"16977336","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":59,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Coexistence of two protein folding states in the crystal structure of ribosomal protein L20. <i> Timsit Y, Allemand F, Chiaruttini C, Springer M. </i> EMBO Rep, 2006","statement":[{"text":"Indeed, nuclear magnetic resonance studies have indicated that L20 extension is fully unstructured in the absence of its RNA target (Raibaud et al, 2002).","type":"Introduction"}],"term_id":"IDPO:0000011","curator_id":"couzo","start":1,"term_ontology":"IDPO","curator_name":"Christos Ouzounis","reference_id":"16977336","version":2,"curator_orcid":"0000-0002-0086-8657","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02143r004","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":59,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Coexistence of two protein folding states in the crystal structure of ribosomal protein L20. <i> Timsit Y, Allemand F, Chiaruttini C, Springer M. </i> EMBO Rep, 2006","term_id":"IDPO:0000011","curator_id":"couzo","start":1,"term_ontology":"IDPO","curator_name":"Christos Ouzounis","reference_id":"16977336","version":2,"curator_orcid":"0000-0002-0086-8657","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02143r005","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_O67086","date":"2018-08-27T21:49:46.000Z","acc":"O67086","name":"50S ribosomal protein L20","length":118,"organism":"Aquifex aeolicus (strain VF5)","dataset":[],"UniParc":"UPI00000564B9","genes":[{"name":{"value":"rplT"},"olnNames":[{"value":"aq_952"}]}],"alphafold_very_low_content":0.00847457627118644,"disorder_content":0.7457627118644068,"disprot_consensus":{"full":[{"start":1,"end":59,"type":"T"},{"start":90,"end":118,"type":"T"}],"Structural state":[{"start":1,"end":59,"type":"D"},{"start":90,"end":118,"type":"D"}],"Structural transition":[{"start":1,"end":59,"type":"T"},{"start":90,"end":118,"type":"T"}]}},{"features":{"pfam":[{"id":"PF13513","name":"HEAT-like repeat","start":381,"end":435},{"id":"PF13513","name":"HEAT-like repeat","start":466,"end":519},{"id":"PF18808","name":"Importin repeat","start":274,"end":365},{"id":"PF18816","name":"Importin repeat","start":1001,"end":1053},{"id":"PF18829","name":"Importin repeat 6","start":767,"end":868},{"id":"PF25780","name":"IPO5-like, TPR repeats","start":116,"end":267}]},"uniref50":"UniRef50_P32337","sequence":"MSALPEEVNRTLLQIVQAFASPDNQIRSVAEKALSEEWITENNIEYLLTFLAEQAAFSQDTTVAALSAVLFRKLALKAPPSSKLMIMSKNITHIRKEVLAQIRSSLLKGFLSERADSIRHKLSDAIAECVQDDLPAWPELLQALIESLKSGNPNFRESSFRILTTVPYLITAVDINSILPIFQSGFTDASDNVKIAAVTAFVGYFKQLPKSEWSKLGILLPSLLNSLPRFLDDGKDDALASVFESLIELVELAPKLFKDMFDQIIQFTDMVIKNKDLEPPARTTALELLTVFSENAPQMCKSNQNYGQTLVMVTLIMMTEVSIDDDDAAEWIESDDTDDEEEVTYDHARQALDRVALKLGGEYLAAPLFQYLQQMITSTEWRERFAAMMALSSAAEGCADVLIGEIPKILDMVIPLINDPHPRVQYGCCNVLGQISTDFSPFIQRTAHDRILPALISKLTSECTSRVQTHAAAALVNFSEFASKDILEPYLDSLLTNLLVLLQSNKLYVQEQALTTIAFIAEAAKNKFIKYYDTLMPLLLNVLKVNNKDNSVLKGKCMECATLIGFAVGKEKFHEHSQELISILVALQNSDIDEDDALRSYLEQSWSRICRILGDDFVPLLPIVIPPLLITAKATQDVGLIEEEEAANFQQYPDWDVVQVQGKHIAIHTSVLDDKVSAMELLQSYATLLRGQFAVYVKEVMEEIALPSLDFYLHDGVRAAGATLIPILLSCLLAATGTQNEELVLLWHKASSKLIGGLMSEPMPEITQVYHNSLVNGIKVMGDNCLSEDQLAAFTKGVSANLTDTYERMQDRHGDGDEYNENIDEEEDFTDEDLLDEINKSIAAVLKTTNGHYLKNLENIWPMINTFLLDNEPILVIFALVVIGDLIQYGGEQTASMKNAFIPKVTECLISPDARIRQAASYIIGVCAQYAPSTYADVCIPTLDTLVQIVDFPGSKLEENRSSTENASAAIAKILYAYNSNIPNVDTYTANWFKTLPTITDKEAASFNYQFLSQLIENNSPIVCAQSNISAVVDSVIQALNERSLTEREGQTVISSVKKLLGFLPSSDAMAIFNRYPADIMEKVHKWFA","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P32337","disprot_id":"DP02144","ncbi_taxon_id":559292,"regions_counter":2,"creator":"viglesias","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":90,"region_id":"DP02144r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for cell-cycle-dependent nuclear import mediated by the karyopherin Kap121p. <i> Kobayashi J, Matsuura Y. </i> J Mol Biol, 2013","statement":[{"text":"The residues 80–90 of Kap121p correspond to a loop connecting HEATs 2 and 3, which has no electron density in Kap121p–RanGTP complex. Truncation of this loop was vital to obtain crystals of Kap121p–cargo complexes, Kap121p–Nup53p complex, and unliganded Kap121p.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"viglesias","start":80,"term_ontology":"IDPO","curator_name":"Valentín Iglesias","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6133-0869","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3w3y"}],"reference_id":"23541588","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":90,"term_name":"flexible linker","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural basis for cell-cycle-dependent nuclear import mediated by the karyopherin Kap121p. <i> Kobayashi J, Matsuura Y. </i> J Mol Biol, 2013","statement":[{"text":"The residues 80–90 of Kap121p correspond to a loop connecting HEATs 2 and 3","type":"Methods"}],"term_id":"IDPO:0000033","curator_id":"viglesias","start":80,"term_ontology":"IDPO","curator_name":"Valentín Iglesias","reference_id":"23541588","version":3,"curator_orcid":"0000-0002-6133-0869","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02144r002","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_P32337","date":"2018-08-27T21:50:15.000Z","acc":"P32337","name":"Importin subunit beta-3","length":1089,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000016898A","genes":[{"name":{"value":"PSE1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"1522152","url":"http://www.ncbi.nlm.nih.gov/pubmed/1522152","alternativeUrl":"https://europepmc.org/abstract/MED/1522152"}}]},"synonyms":[{"value":"KAP121","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9182759","url":"http://www.ncbi.nlm.nih.gov/pubmed/9182759","alternativeUrl":"https://europepmc.org/abstract/MED/9182759"}}]}],"orfNames":[{"value":"YM9952.10C"}],"olnNames":[{"value":"YMR308C","evidences":[{"code":"ECO:0000312","source":{"name":"SGD","id":"S000004925","url":"https://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000004925"}}]}]}],"alphafold_very_low_content":0.005509641873278237,"disorder_content":0.010101010101010102,"disprot_consensus":{"full":[{"start":80,"end":90,"type":"D"}],"Structural state":[{"start":80,"end":90,"type":"D"}],"Disorder function":[{"start":80,"end":90,"type":"F"}]}},{"features":{"pfam":[{"id":"PF11894","name":"Nuclear pore complex scaffold, nucleoporins 186/192/205","start":3,"end":1677}]},"uniref50":"UniRef50_P47054","sequence":"MKWSAIPFQTLYRSIESGEFDFDLFKEVLPDLQNLNLNTDKLKNNASRSQLEKGEIELSDGSTFKVNQEFIFEAISLSDELNLDEIVACELILSGDTTANNGKVQYFLRRQYILQIVSFIVNCFHEDTELYQELIKNGALVSNILSAFKFIHTQLSEIKQQINKAQILENYNALFQQNIKFRRDFLLREYDILSQILYGLVDKGAIMKNKDFILSLLHHVSELDSNDFFIIYYTPAFFHLFASLRVLPDADVKLLHSQFMKDLKDDSIYTKPVKVALIFIFFAYFIGWCKEDPKRRADTMDFKTDVDEPMTSAVELGAIEQILIFAADTSIVEQDKSMELFYDIRSLLERHIPRLIPKQLLDDEKIFSQTTNSTYNPASATDNMSGRGLWNPSYPGMMSTTGTARLNSMPNNVNEYSYTTIVLSDQTQEFFLSSFDDVLQTIITDCAFLLTKIKDAEEDSLLSGEDLTLDDISLKADLERFFLSIYFFYASRPEYSCTFWSDKESNAYGFIEWCSRCNDNLMRSCFYLMVSSLSFGPENALNVYHYFGENSSISWKNIAQCLSDYTKKISNFNSSLHKRQQFSESTHNDIDSTAVALEEGLNEEAVIFLSSLLTLVGSVTYQVDEDVKSSLSKVFSDVLFEFTKINTPLVGAAFKVISNLVPKLESSRTKFWSFLDSLIFKDSSLNYSSESYRNAFTNVLTKYSDVLGFLQLFHNLISIHSRENNSEYMVFGKLAFPTRLGQGYRKVGIWPYFDYIFNDILAHVDQIVDIRNKRAVQLPILKIIYTGLCSFDYSVILNSIPAAANLDALVDCENFFNYVQECPAIPIFNYIFTEKIYKSIFNVVDVGVDQLSIELEGGKNQAELLQLAVKIINKVLDYQETYVEELFPIVKKHGKTDYFLPKNYSLHGLRSFYDAIFFNIPLVAHLGLYVGVDDQILATNSLRILAKLSERSNGSVASLSKRNKLLTIFDSVDESARIKDAFITQLESSITDAGVLALKLELLDFLTSNLSNYSRTMTISHLLLGFQVSNVISLGPNLATFISSGTSLLDSLISVLEASLNSITKDNIDYAPMRLATAALEIILKLCRNPLTSGLLYSYLIKENFFERIMILDPQVTRFTTWNGSPFDNSTEEKCKNFIESESVGAFLSFLAYRNYWTQYLGLFIHKISFSGTKSEVLTYVNYLISNTMYSVRLFSFLDPLNYGNICEPKETLSIFTNVPLNLEQVTLNKYCSGNIYDFHKMENLMRLIKRVRAESLHSNSFSLTVSKEQFLKDADVECIKAKSHFTNIISRNKALELNLSVLHSWVQLVQIIVTDGKLEPSTRSNFILEVFGTIIPKISDYIEFNITFSEELVSLAVFLFDIYNRDRKLITDKGTVDGRLYQLFKTCIQGINSPLSSVALRSDFYILANHYLSRVLSDQVGSEKVLQDLRLGSKKLVEIIWNDVVYGEGTSRVTGILLLDSLIQLANRSKENFILDSLMKTTRLLLIIRSLKNTDALLNSTTEHINIDDLLYELTAFKATVFFLIRVAETRGGASALIENNLFRIIAELSFLKVDPDLGLDLMFDEVYVQNSKFLKVNVTLDNPLLVDKDANGVSLFELIVPIFQLISAVLVSMGSSNKAVVQTVKGLLNTYKRLVIGIFKRDLLREKEDKKNSSDPNNQSLNEMVKLIVMLCTLTGYQNND","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P47054","disprot_id":"DP02145","ncbi_taxon_id":559292,"regions_counter":3,"creator":"viglesias","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":424,"region_id":"DP02145r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure, dynamics, evolution, and function of a major scaffold component in the nuclear pore complex. <i> Sampathkumar P, Kim SJ, Upla P, Rice WJ, Phillips J, Timney BL, Pieper U, Bonanno JB, Fernandez-Martinez J, Hakhverdyan Z, Ketaren NE, Matsui T, Weiss TM, Stokes DL, Sauder JM, Burley SK, Sali A, Rout MP, Almo SC. </i> Structure, 2013","statement":[{"text":"The D2 domain contains two long loops: (L1) a long, ~100 amino acid (residues 328–424) loop that seems to adopt a mostly random coil conformation, within which residues 363–416 could not be modeled in the electron density maps and (L2) an ~30 amino acid loop (residues 575–601) that could not be modeled in the electron density maps","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"viglesias","start":328,"term_ontology":"IDPO","curator_name":"Valentín Iglesias","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6133-0869","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4ifq"}],"reference_id":"23499021","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":601,"region_id":"DP02145r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure, dynamics, evolution, and function of a major scaffold component in the nuclear pore complex. <i> Sampathkumar P, Kim SJ, Upla P, Rice WJ, Phillips J, Timney BL, Pieper U, Bonanno JB, Fernandez-Martinez J, Hakhverdyan Z, Ketaren NE, Matsui T, Weiss TM, Stokes DL, Sauder JM, Burley SK, Sali A, Rout MP, Almo SC. </i> Structure, 2013","statement":[{"text":"The D2 domain contains two long loops: (L1) a long, ~100 amino acid (residues 328–424) loop that seems to adopt a mostly random coil conformation, within which residues 363–416 could not be modeled in the electron density maps and (L2) an ~30 amino acid loop (residues 575–601) that could not be modeled in the electron density maps","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"viglesias","start":576,"term_ontology":"IDPO","curator_name":"Valentín Iglesias","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6133-0869","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4ifq"}],"reference_id":"23499021","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":813,"region_id":"DP02145r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure, dynamics, evolution, and function of a major scaffold component in the nuclear pore complex. <i> Sampathkumar P, Kim SJ, Upla P, Rice WJ, Phillips J, Timney BL, Pieper U, Bonanno JB, Fernandez-Martinez J, Hakhverdyan Z, Ketaren NE, Matsui T, Weiss TM, Stokes DL, Sauder JM, Burley SK, Sali A, Rout MP, Almo SC. </i> Structure, 2013","statement":[{"text":"The D3 domain of ScNup192(2–960) has a globular shape composed of 15 helices (from α35 to α49) and includes two disordered loop regions (residues 799–813 between α41 and α42 [L3], and residues 850–856 between α44 and α45 [L4]).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"viglesias","start":799,"term_ontology":"IDPO","curator_name":"Valentín Iglesias","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6133-0869","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4ifq"}],"reference_id":"23499021","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P47054","date":"2018-08-27T22:00:09.000Z","acc":"P47054","name":"Nucleoporin NUP192","length":1683,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000013B540","genes":[{"name":{"value":"NUP192"},"orfNames":[{"value":"J1216"}],"olnNames":[{"value":"YJL039C"}]}],"alphafold_very_low_content":0.050505050505050504,"disorder_content":0.08199643493761141,"disprot_consensus":{"full":[{"start":328,"end":424,"type":"D"},{"start":576,"end":601,"type":"D"},{"start":799,"end":813,"type":"D"}],"Structural state":[{"start":328,"end":424,"type":"D"},{"start":576,"end":601,"type":"D"},{"start":799,"end":813,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00400","name":"WD domain, G-beta repeat","start":315,"end":349},{"id":"PF00400","name":"WD domain, G-beta repeat","start":358,"end":393},{"id":"PF00400","name":"WD domain, G-beta repeat","start":400,"end":436},{"id":"PF00400","name":"WD domain, G-beta repeat","start":538,"end":562},{"id":"PF00400","name":"WD domain, G-beta repeat","start":574,"end":604},{"id":"PF08614","name":"Autophagy protein 16 (ATG16)","start":16,"end":206}],"gene3D":[{"start":535,"end":606,"id":"2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"},{"start":460,"end":534,"id":"2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"}]},"uniref50":"UniRef50_Q676U5","sequence":"MSSGLRAADFPRWKRHISEQLRRRDRLQRQAFEEIILQYNKLLEKSDLHSVLAQKLQAEKHDVPNRHEISPGHDGTWNDNQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATKRLSQPAGGLLDSITNIFGRRSVSSFPVPQDNVDTHPGSGKEVRVPATALCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVFGEKCEFKGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTVFAGSSCNDIVCTEQCVMSGHFDKKIRFWDIRSESIVREMELLGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPGFKCGSDWTRVVFSPDGSYVAAGSAEGSLYIWSVLTGKVEKVLSKQHSSSINAVAWSPSGSHVVSVDKGCKAVLWAQY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q676U5","disprot_id":"DP02148","ncbi_taxon_id":9606,"regions_counter":6,"creator":"ldobson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":84,"region_id":"DP02148r001","released":"2022_06","ec_id":"ECO:0006204","reference_html":"Identifying intrinsically disordered protein regions likely to undergo binding-induced helical transitions. <i> Glover K, Mei Y, Sinha SC. </i> Biochim Biophys Acta, 2016","term_id":"IDPO:0000002","curator_id":"esalladini","start":59,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-05-31T12:10:06.944Z","reference_source":"pmid","term_name":"disorder","reference_id":"27179590","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"All the selected IDRs lack α-helical structure in solution","type":"Results"},{"text":"However, the marginal secondary structure content suggests that all the peptides tested are IDRs.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-05-31T15:08:02.505Z"}},{"start":12,"end":31,"reference_id":"31145591","reference_source":"pmid","reference_html":"Design, Synthesis, Antibacterial Potential, and Structural Characterization of N-Acylated Derivatives of the Human Autophagy 16 Polypeptide. <i> Varnava KG, Mohid SA, Calligari P, Stella L, Reynison J, Bhunia A, Sarojini V. </i> Bioconjug Chem, 2019","date":"2024-05-07T14:19:19.427Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"5ZYX"}],"region_id":"DP02148r004","statement":[{"text":"The marked chemical shift deviation of CαH resonances of\nK30 from the random coil values also supports a folded\nconformation of peptide K30 in D8PG micelles.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:11846228"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-24T14:47:15.028Z"}}],"released":"2018_11","uniref100":"UniRef100_Q676U5","date":"2018-08-28T08:11:26.000Z","acc":"Q676U5","name":"Autophagy-related protein 16-1","length":607,"organism":"Homo sapiens","dataset":["Autophagy-related proteins"],"UniParc":"UPI0000427052","genes":[{"name":{"value":"ATG16L1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"17200669","url":"http://www.ncbi.nlm.nih.gov/pubmed/17200669","alternativeUrl":"https://europepmc.org/abstract/MED/17200669"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:21498","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:21498"}}]},"synonyms":[{"value":"APG16L","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15620219","url":"http://www.ncbi.nlm.nih.gov/pubmed/15620219","alternativeUrl":"https://europepmc.org/abstract/MED/15620219"}}]}],"orfNames":[{"value":"UNQ9393/PRO34307","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12975309","url":"http://www.ncbi.nlm.nih.gov/pubmed/12975309","alternativeUrl":"https://europepmc.org/abstract/MED/12975309"}}]}]}],"alphafold_very_low_content":0.15485996705107083,"disorder_content":0.0757825370675453,"disprot_consensus":{"full":[{"start":12,"end":31,"type":"S"},{"start":59,"end":84,"type":"D"}],"Structural state":[{"start":12,"end":31,"type":"S"},{"start":59,"end":84,"type":"D"}]}},{"features":{"pfam":[{"id":"PF30113","name":"Cell death protein Grim","start":82,"end":106}]},"uniref50":"UniRef50_Q24570","sequence":"MAIAYFIPDQAQLLARSYQQNGQQTAASPRTTATAAAPSQQQQQSQQQQQQQRHHHQQQRPQFRANISVPLGSQQGSMTMSEFGCWDLLAQIFCYALRIYSYSSSQRQPTVIQISFEISSGGQNNDEDDVTDATSKEN","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_Q24570","disprot_id":"DP02149","ncbi_taxon_id":7227,"regions_counter":1,"creator":"baykac","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":15,"region_id":"DP02149r001","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Identifying intrinsically disordered protein regions likely to undergo binding-induced helical transitions. <i> Glover K, Mei Y, Sinha SC. </i> Biochim Biophys Acta, 2016","term_id":"IDPO:0000002","curator_id":"fquaglia","start":1,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2023-12-12T10:36:34.440Z","reference_source":"pmid","term_name":"disorder","reference_id":"27179590","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Secondary structure content estimated by analysis of CD spectra for each of the thirteen IDRs showed that none contained more than two residues in a helical conformation (Figures 1-3, Table 3-5), which is insufficient for the formation of a stable α-helix requiring a minimum of six residues. Formation of a minimal beta-structure requires six residues [38], and seven of the thirteen IDRs (Table 3-5) appear to have between six to eight residues in extended or β-conformation which may be sufficient for forming short stable β-hairpins (Table 3-5). Thus, while none of the selected IDRs had stable helical structure, several may have short β-strands.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-01-12T14:30:19.624Z"}}],"released":"2018_11","uniref100":"UniRef100_Q24570","date":"2018-08-28T08:16:47.000Z","acc":"Q24570","name":"Cell death protein Grim","length":138,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI000014ADF9","genes":[{"name":{"value":"grim"},"orfNames":[{"value":"CG4345"}]}],"alphafold_very_low_content":0.34782608695652173,"disorder_content":0.10869565217391304,"disprot_consensus":{"full":[{"start":1,"end":15,"type":"D"}],"Structural state":[{"start":1,"end":15,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00595","name":"PDZ domain","start":290,"end":367}],"gene3D":[{"start":284,"end":370,"id":"2.30.42.10","name":"2.30.42.10"}]},"uniref50":"UniRef50_Q9HD26","sequence":"MSAGGPCPAAAGGGPGGASCSVGAPGGVSMFRWLEVLEKEFDKAFVDVDLLLGEIDPDQADITYEGRQKMTSLSSCFAQLCHKAQSVSQINHKLEAQLVDLKSELTETQAEKVVLEKEVHDQLLQLHSIQLQLHAKTGQSADSGTIKAKLSGPSVEELERELEANKKEKMKEAQLEAEVKLLRKENEALRRHIAVLQAEVYGARLAAKYLDKELAGRVQQIQLLGRDMKGPAHDKLWNQLEAEIHLHRHKTVIRACRGRNDLKRPMQAPPGHDQDSLKKSQGVGPIRKVLLLKEDHEGLGISITGGKEHGVPILISEIHPGQPADRCGGLHVGDAILAVNGVNLRDTKHKEAVTILSQQRGEIEFEVVYVAPEVDSDDENVEYEDESGHRYRLYLDELEGGGNPGASCKDTSGEIKVLQGFNKKAVTDTHENGDLGTASETPLDDGASKLDDLHTLYHKKSY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9HD26","disprot_id":"DP02150","ncbi_taxon_id":9606,"regions_counter":2,"creator":"baykac","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":277,"region_id":"DP02150r001","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Identifying intrinsically disordered protein regions likely to undergo binding-induced helical transitions. <i> Glover K, Mei Y, Sinha SC. </i> Biochim Biophys Acta, 2016","term_id":"IDPO:0000002","curator_id":"fquaglia","start":248,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2023-12-12T10:39:42.045Z","reference_source":"pmid","term_name":"disorder","reference_id":"27179590","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Secondary structure content estimated by analysis of CD spectra for each of the thirteen IDRs showed that none contained more than two residues in a helical conformation (Figures 1-3, Table 3-5), which is insufficient for the formation of a stable α-helix requiring a minimum of six residues. Formation of a minimal beta-structure requires six residues [38], and seven of the thirteen IDRs (Table 3-5) appear to have between six to eight residues in extended or β-conformation which may be sufficient for forming short stable β-hairpins (Table 3-5). Thus, while none of the selected IDRs had stable helical structure, several may have short β-strands.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":279,"region_id":"DP02150r002","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Identifying intrinsically disordered protein regions likely to undergo binding-induced helical transitions. <i> Glover K, Mei Y, Sinha SC. </i> Biochim Biophys Acta, 2016","term_id":"IDPO:0000002","curator_id":"fquaglia","start":255,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2023-12-12T10:40:05.815Z","reference_source":"pmid","term_name":"disorder","reference_id":"27179590","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Secondary structure content estimated by analysis of CD spectra for each of the thirteen IDRs showed that none contained more than two residues in a helical conformation (Figures 1-3, Table 3-5), which is insufficient for the formation of a stable α-helix requiring a minimum of six residues. Formation of a minimal beta-structure requires six residues [38], and seven of the thirteen IDRs (Table 3-5) appear to have between six to eight residues in extended or β-conformation which may be sufficient for forming short stable β-hairpins (Table 3-5). Thus, while none of the selected IDRs had stable helical structure, several may have short β-strands.","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_Q9HD26","date":"2018-08-28T08:19:24.000Z","acc":"Q9HD26","name":"Golgi-associated PDZ and coiled-coil motif-containing protein","length":462,"organism":"Homo sapiens","dataset":["Autophagy-related proteins","Cancer-related proteins"],"UniParc":"UPI0000070C27","genes":[{"name":{"value":"GOPC","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:17643","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:17643"}}]},"synonyms":[{"value":"CAL","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"14570915","url":"http://www.ncbi.nlm.nih.gov/pubmed/14570915","alternativeUrl":"https://europepmc.org/abstract/MED/14570915"}}]},{"value":"FIG"}]}],"alphafold_very_low_content":0.23593073593073594,"disorder_content":0.06926406926406926,"disprot_consensus":{"full":[{"start":248,"end":279,"type":"D"}],"Structural state":[{"start":248,"end":279,"type":"D"}]}},{"features":{"pfam":[{"id":"PF10744","name":"Mediator of RNA polymerase II transcription subunit 1","start":60,"end":426}]},"uniref50":"UniRef50_Q15648","sequence":"MKAQGETEDSERLSKMSSLLERLHAKFNQNRPWSETIKLVRQVMEKRVVMSSGGHQHLVSCLETLQKALKVTSLPAMTDRLESIARQNGLGSHLSASGTECYITSDMFYVEVQLDPAGQLCDVKVAHHGENPVSCPELVQQLREKNFEEFSKHLKGLVNLYNLPGDNKLKTKMYLALQSLEQDLSKMAIMYWKATNAAPLDKILHGSVGYLTPRSGGHLMNMKYYASPSDLLDDKTASPIILHEKNVPRSLGMNASVTIEGTSAMYKLPIAPLIMGSHPADNKWTPSFSAVTSANSVDLPACFFLKFPQPIPVSKAFVQKLQNCTGIPLFETPPTYLPLYELITQFELSKDPDPLPLNHNMRFYAALPGQQHCYFLNKDAPLPDGQSLQGTLVSKITFQHPGRVPLILNMIRHQVAYNTLIGSCVKRTILKEDSPGLLQFEVCPLSESRFSVSFQHPVNDSLVCVVMDVQDSTHVSCKLYKGLSDALICTDDFIAKVVQRCMSIPVTMRAIRRKAETIQADTPALSLIAETVEDMVKKNLPPASSPGYGMTTGNNPMSGTTTPTNTFPGGPITTLFNMSMSIKDRHESVGHGEDFSKVSQNPILTSLLQITGNGGSTIGSSPTPPHHTPPPVSSMAGNTKNHPMLMNLLKDNPAQDFSTLYGSSPLERQNSSSGSPRMEMCSGSNKAKKKKSSRVPPDKPKHQTEDDFQRELFSMDVDSQNPMFDVSMTADALDTPHITPAPSQCSTPPATYPQPVSHPQPSIQRMVRLSSSDSIGPDVTDILSDIAEEASKLPSTSDDCPPIGTPVRDSSSSGHSQSALFDSDVFQTNNNENPYTDPADLIADAAGSPNSDSPTNHFFPDGVDFNPDLLNSQSQSGFGEEYFDESSQSGDNDDFKGFASQALNTLGMPMLGGDNGEPKFKGSSQADTVDFSIISVAGKALGAADLMEHHSGSQSPLLTTGELGKEKTQKRVKEGNGTGASSGSGPGSDSKPGKRSRTPSNDGKSKDKPPKRKKADTEGKSPSHSSSNRPFTPPTSTGGSKSPGSSGRSQTPPGVATPPIPKITIQIPKGTVMVGKPSSHSQYTSSGSVSSSGSKSHHSHSSSSSSLASASTSGKVKSSKSEGSSSSKLSGSMYASQGSSGSSQSKNSSQTGGKPGSSPITKHGLSSGSSSTKMKPQGKPSSLMNPSISKPNISPSHSRPPGGSDKLASPMKPVPGTPPSSKAKSPISSGSSGSHVSGTSSSSGMKSSSGSASSGSVSQKTPPASNSCTPSSSSFSSSGSSMSSSQNQHGSSKGKSPSRNKKPSLTAVIDKLKHGVVTSGPGGEDPIDSQMGASTNSSNHPMSSKHNTSGGEFQSKREKSDKDKSKVSASGGSVDSSKKTSESKNVGSTGVAKIIISKHDGGSPSIKAKVTLQKPGESGGDGLRPQIASSKNYGSPLISGSTPKHERGSPSHSKSPAYTPQNVDSESESGSSIAERSYQNSPSSEDGIRPLPEYSTEKHKKHKKEKKKVRDKDRDKKKSHSMKPENWSKSPISSDPTASVTNNPILSADRPSRLSPDFMIGEEDDDLMDVALIGN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q15648","disprot_id":"DP02151","ncbi_taxon_id":10090,"regions_counter":2,"creator":"baykac","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":654,"region_id":"DP02151r001","released":"2023_12","ec_id":"ECO:0006204","reference_html":"Identifying intrinsically disordered protein regions likely to undergo binding-induced helical transitions. <i> Glover K, Mei Y, Sinha SC. </i> Biochim Biophys Acta, 2016","term_id":"IDPO:0000002","curator_id":"fquaglia","start":637,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2023-12-12T10:36:24.603Z","reference_source":"pmid","term_name":"disorder","reference_id":"27179590","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Secondary structure content estimated by analysis of CD spectra for each of the thirteen IDRs showed that none contained more than two residues in a helical conformation (Figures 1-3, Table 3-5), which is insufficient for the formation of a stable α-helix requiring a minimum of six residues. Formation of a minimal beta-structure requires six residues [38], and seven of the thirteen IDRs (Table 3-5) appear to have between six to eight residues in extended or β-conformation which may be sufficient for forming short stable β-hairpins (Table 3-5). Thus, while none of the selected IDRs had stable helical structure, several may have short β-strands.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:17:44.445Z"}}],"released":"2018_11","uniref100":"UniRef100_Q925J9","date":"2018-08-28T08:22:13.000Z","acc":"Q925J9","name":"Mediator of RNA polymerase II transcription subunit 1","length":1575,"organism":"Mus musculus","dataset":["Condensates-related proteins"],"UniParc":"UPI00001E653A","genes":[{"name":{"value":"Med1"},"synonyms":[{"value":"Crsp210"},{"value":"Drip205"},{"value":"Pbp"},{"value":"Pparbp"},{"value":"Trap220"},{"value":"Trip2"}]}],"alphafold_very_low_content":0.6526984126984127,"disorder_content":0.011428571428571429,"disprot_consensus":{"full":[{"start":637,"end":654,"type":"D"}],"Structural state":[{"start":637,"end":654,"type":"D"}]}},{"features":{"pfam":[{"id":"PF04096","name":"Nup98-96 autopeptidase S59","start":460,"end":610},{"id":"PF12110","name":"Nuclear protein 96","start":898,"end":1150},{"id":"PF13634","name":"Nucleoporin FG repeat region","start":71,"end":157}],"gene3D":[{"start":459,"end":610,"id":"3.30.1610.10","name":"Peptidase S59, nucleoporin"},{"start":736,"end":784,"id":"2.20.25.480","name":"2.20.25.480"},{"start":881,"end":972,"id":"1.25.40.690","name":"1.25.40.690"}]},"uniref50":"UniRef50_P49687","sequence":"MFNKSVNSGFTFGNQNTSTPTSTPAQPSSSLQFPQKSTGLFGNVNVNANTSTPSPSGGLFNANSNANSISQQPANNSLFGNKPAQPSGGLFGATNNTTSKSAGSLFGNNNATANSTGSTGLFSGSNNIASSTQNGGLFGNSNNNNITSTTQNGGLFGKPTTTPAGAGGLFGNSSSTNSTTGLFGSNNTQSSTGIFGQKPGASTTGGLFGNNGASFPRSGETTGTMSTNPYGINISNVPMAVADMPRSITSSLSDVNGKSDAEPKPIENRRTYSFSSSVSGNAPLPLASQSSLVSRLSTRLKATQKSTSPNEIFSPSYSKPWLNGAGSAPLVDDFFSSKMTSLAPNENSIFPQNGFNFLSSQRADLTELRKLKIDSNRSAAKKLKLLSGTPAITKKHMQDEQDSSENEPIANADSVTNIDRKENRDNNLDNTYLNGKEQSNNLNKQDGENTLQHEKSSSFGYWCSPSPEQLERLSLKQLAAVSNFVIGRRGYGCITFQHDVDLTAFTKSFREELFGKIVIFRSSKTVEVYPDEATKPMIGHGLNVPAIITLENVYPVDKKTKKPMKDTTKFAEFQVFDRKLRSMREMNYISYNPFGGTWTFKVNHFSIWGLVNEEDAEIDEDDLSKQEDGGEQPLRKVRTLAQSKPSDKEVILKTDGTFGTLSGKDDSIVEEKAYEPDLSDADFEGIEASPKLDVSKDWVEQLILAGSSLRSVFATSKEFDGPCQNEIDLLFSECNDEIDNAKLIMKERRFTASYTFAKFSTGSMLLTKDIVGKSGVSIKRLPTELQRKFLFDDVYLDKEIEKVTIEARKSNPYPQISESSLLFKDALDYMEKTSSDYNLWKLSSILFDPVSYPYKTDNDQVKMALLKKERHCRLTSWIVSQIGPEIEEKIRNSSNEIEQIFLYLLLNDVVRASKLAIESKNGHLSVLISYLGSNDPRIRDLAELQLQKWSTGGCSIDKNISKIYKLLSGSPFEGLFSLKELESEFSWLCLLNLTLCYGQIDEYSLESLVQSHLDKFSLPYDDPIGVIFQLYAANENTEKLYKEVRQRTNALDVQFCWYLIQTLRFNGTRVFSKETSDEATFAFAAQLEFAQLHGHSLFVSCFLNDDKAAEDTIKRLVMREITLLRASTNDHILNRLKIPSQLIFNAQALKDRYEGNYLSEVQNLLLGSSYDLAEMAIVTSLGPRLLLSNNPVQNNELKTLREILNEFPDSERDKWSVSINVFEVYLKLVLDNVETQETIDSLISGMKIFYDQYKHCREVAACCNVMSQEIVSKILEKNNPSIGDSKAKLLELPLGQPEKAYLRGEFAQDLMKCTYKI","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P49687","disprot_id":"DP02155","ncbi_taxon_id":559292,"regions_counter":3,"creator":"sventura","regions":[{"start":606,"end":734,"reference_id":"34982960","reference_source":"pmid","reference_html":"Comprehensive structure and functional adaptations of the yeast nuclear pore complex. <i> Akey CW, Singh D, Ouch C, Echeverria I, Nudelman I, Varberg JM, Yu Z, Fang F, Shi Y, Wang J, Salzberg D, Song K, Xu C, Gumbart JC, Suslov S, Unruh J, Jaspersen SL, Chait BT, Sali A, Fernandez-Martinez J, Ludtke SJ, Villa E, Rout MP. </i> Cell, 2022","date":"2023-12-15T14:42:15.013Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7N9F"}],"region_id":"DP02155r003","statement":[{"text":"The Cryo-EM Structure of the in situ yeast NPC shows this region of the NUP145 protein is disordered. \n","type":"Curator statement"}]}],"released":"2018_11","uniref100":"UniRef100_P49687","date":"2018-08-28T10:53:16.000Z","acc":"P49687","name":"Nucleoporin NUP145","length":1317,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":["Condensates-related proteins","RNA-binding proteins"],"UniParc":"UPI0000052F85","genes":[{"name":{"value":"NUP145"},"synonyms":[{"value":"RAT10"}],"olnNames":[{"value":"YGL092W"}]}],"alphafold_very_low_content":0.3895216400911162,"disorder_content":0.0979498861047836,"disprot_consensus":{"full":[{"start":606,"end":734,"type":"D"}],"Structural state":[{"start":606,"end":734,"type":"D"}]}},{"features":{"pfam":[{"id":"PF07575","name":"Nup85 Nucleoporin","start":89,"end":697}],"gene3D":[{"start":38,"end":94,"id":"2.20.25.500","name":"2.20.25.500"}]},"uniref50":"UniRef50_P46673","sequence":"MTIDDSNRLLMDVDQFDFLDDGTAQLSNNKTDEEEQLYKRDPVSGAILVPMTVNDQPIEKNGDKMPLKFKLGPLSYQNMAFITAKDKYKLYPVRIPRLDTSKEFSAYVSGLFEIYRDLGDDRVFNVPTIGVVNSNFAKEHNATVNLAMEAILNELEVFIGRVKDQDGRVNRFYELEESLTVLNCLRTMYFILDGQDVEENRSEFIESLLNWINRSDGEPDEEYIEQVFSVKDSTAGKKVFETQYFWKLLNQLVLRGLLSQAIGCIERSDLLPYLSDTCAVSFDAVSDSIELLKQYPKDSSSTFREWKNLVLKLSQAFGSSATDISGELRDYIEDFLLVIGGNQRKILQYSRTWYESFCGFLLYYIPSLELSAEYLQMSLEANVVDITNDWEQPCVDIISGKIHSILPVMESLDSCTAAFTAMICEAKGLIENIFEGEKNSDDYSNEDNEMLEDLFSYRNGMASYMLNSFAFELCSLGDKELWPVAIGLIALSATGTRSAKKMVIAELLPHYPFVTNDDIEWMLSICVEWRLPEIAKEIYTTLGNQMLSAHNIIESIANFSRAGKYELVKSYSWLLFEASCMEGQKLDDPVLNAIVSKNSPAEDDVIIPQDILDCVVTNSMRQTLAPYAVLSQFYELRDREDWGQALRLLLLLIEFPYLPKHYLVLLVAKFLYPIFLLDDKKLMDEDSVATVIEVIETKWDDADEKSSNLYETIIEADKSLPSSMATLLKNLRKKLNFKLCQAFM","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P46673","disprot_id":"DP02156","ncbi_taxon_id":559292,"regions_counter":3,"creator":"sventura","regions":[{"start":1,"end":46,"reference_id":"33268786","reference_source":"pmid","reference_html":"A nanobody suite for yeast scaffold nucleoporins provides details of the nuclear pore complex structure. <i> Nordeen SA, Andersen KR, Knockenhauer KE, Ingram JR, Ploegh HL, Schwartz TU. </i> Nat Commun, 2020","date":"2024-02-22T14:24:25.044Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"6X08"}],"region_id":"DP02156r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P53011"}],"statement":[{"text":"The cryo-EM structure of the Nup85-Seh1 from S. cerevisiae bound by nanobodies shows this region lacks electron density, indicating it is disordered. The nanobodies are single-domain (VHH) antibody fragments derived from camelid heavy-chain only antibodies.","type":"Curator statement"}]},{"start":432,"end":450,"reference_id":"33268786","reference_source":"pmid","reference_html":"A nanobody suite for yeast scaffold nucleoporins provides details of the nuclear pore complex structure. <i> Nordeen SA, Andersen KR, Knockenhauer KE, Ingram JR, Ploegh HL, Schwartz TU. </i> Nat Commun, 2020","date":"2024-02-22T14:24:45.765Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"6X08"}],"region_id":"DP02156r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P53011"}],"statement":[{"text":"The cryo-EM structure of the Nup85-Seh1 from S. cerevisiae bound by nanobodies shows this region lacks electron density, indicating it is disordered. The nanobodies are single-domain (VHH) antibody fragments derived from camelid heavy-chain only antibodies.","type":"Curator statement"}]}],"released":"2018_11","uniref100":"UniRef100_P46673","date":"2018-08-28T11:09:54.000Z","acc":"P46673","name":"Nucleoporin NUP85","length":744,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000052F87","genes":[{"name":{"value":"NUP85"},"synonyms":[{"value":"RAT9"}],"orfNames":[{"value":"J1624"}],"olnNames":[{"value":"YJR042W"}]}],"alphafold_very_low_content":0.0739247311827957,"disorder_content":0.08736559139784947,"disprot_consensus":{"full":[{"start":1,"end":46,"type":"D"},{"start":432,"end":450,"type":"D"}],"Structural state":[{"start":1,"end":46,"type":"D"},{"start":432,"end":450,"type":"D"}]}},{"features":{"pfam":[{"id":"PF11715","name":"Nucleoporin Nup120/160, beta-propeller domain","start":87,"end":386},{"id":"PF22114","name":"Nucleoporin NUP120, helical domain","start":510,"end":692},{"id":"PF23300","name":"Nucleoporin Nup120, HEAT repeats","start":726,"end":902}]},"uniref50":"UniRef50_P35729","sequence":"MACLSRIDANLLQYYEKPEPNNTVDLYVSNNSNNNGLKEGDKSISTPVPQPYGSEYSNCLLLSNSEYICYHFSSRSTLLTFYPLSDAYHGKTINIHLPNASMNQRYTLTIQEVEQQLLVNVILKDGSFLTLQLPLSFLFSSANTLNGEWFHLQNPYDFTVRVPHFLFYVSPQFSVVFLEDGGLLGLKKVDGVHYEPLLFNDNSYLKSLTRFFSRSSKSDYDSVISCKLFHERYLIVLTQNCHLKIWDLTSFTLIQDYDMVSQSDSDPSHFRKVEAVGEYLSLYNNTLVTLLPLENGLFQMGTLLVDSSGILTYTFQNNIPTNLSASAIWSIVDLVLTRPLELNVEASYLNLIVLWKSGTASKLQILNVNDESFKNYEWIESVNKSLVDLQSEHDLDIVTKTGDVERGFCNLKSRYGTQIFERAQQILSENKIIMAHNEDEEYLANLETILRDVKTAFNEASSITLYGDEIILVNCFQPYNHSLYKLNTTVENWFYNMHSETDGSELFKYLRTLNGFASTLSNDVLRSISKKFLDIITGELPDSMTTVEKFTDIFKNCLENQFEITNLKILFDELNSFDIPVVLNDLINNQMKPGIFWKKDFISAIKFDGFTSIISLESLHQLLSIHYRITLQVLLTFVLFDLDTEIFGQHISTLLDLHYKQFLLLNLYRQDKCLLAEVLLKDSSEFSFGVKFFNYGQLIAYIDSLNSNVYNASITENSFFMTFFRSYIIENTSHKNIRFFLENVECPFYLRHNEVQEFMFAMTLFSCGNFDQSYEIFQLHDYPEAINDKLPTFLEDLKSENYHGDSIWKDLLCTFTVPYRHSAFYYQLSLLFDRNNSQEFALKCISKSAEYSLKEIQIEELQDFKEKQHIHYLNLLIHFRMFEEVLDVLRLGHECLSDTVRTNFLQLLLQEDIYSRDFFSTLLRLCNAHSDNGELYLRTVDIKIVDSILSQNLRSGDWECFKKLYCFRMLNKSERAAAEVLYQYILMQADLDVIRKRKCYLMVINVLSSFDSAYDQWILNGSKVVTLTDLRDELRGL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P35729","disprot_id":"DP02157","ncbi_taxon_id":559292,"regions_counter":1,"creator":"sventura","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":52,"region_id":"DP02157r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural and functional analysis of Nup120 suggests ring formation of the Nup84 complex. <i> Seo HS, Ma Y, Debler EW, Wacker D, Kutik S, Blobel G, Hoelz A. </i> Proc Natl Acad Sci U S A, 2009","statement":[{"text":"Because the major part of the surface-exposed 1E1A and 5CD loops (residues 30–52 and 306–310) are invisible in the electron density, presumably due to disorder, these 2 regions were omitted from the final model.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"sventura","start":30,"term_ontology":"IDPO","curator_name":"Salvador Ventura","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3h7n"}],"reference_id":"19706512","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P35729","date":"2018-08-28T11:20:14.000Z","acc":"P35729","name":"Nucleoporin NUP120","length":1037,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000052F84","genes":[{"name":{"value":"NUP120"},"synonyms":[{"value":"RAT2"}],"orfNames":[{"value":"YKL313"},{"value":"YKL314"}],"olnNames":[{"value":"YKL057C"}]}],"alphafold_very_low_content":0.03182256509161042,"disorder_content":0.022179363548698167,"disprot_consensus":{"full":[{"start":30,"end":52,"type":"D"}],"Structural state":[{"start":30,"end":52,"type":"D"}]}},{"features":{"pfam":[{"id":"PF08801","name":"Nup133 N terminal like","start":63,"end":475}],"gene3D":[{"start":552,"end":1102,"id":"1.25.40.700","name":"1.25.40.700"}]},"uniref50":"UniRef50_P36161","sequence":"MSEKKVHLRLRKELSVPIAVVENESLAQLSYEEESQASLMDISMEQQQLRLHSHFDNSKVFTENNRYIVKTLQTDYSSGFSNDDELNGYIDMQIGYGLVNDHKKVYIWNIHSTQKDTPYITVPFRSDDNDEIAVAPRCILTFPATMDESPLALNPNDQDETGGLIIIKGSKAIYYEDINSINNLNFKLSEKFSHELELPINSSGGEKCDLMLNCEPAGIVLSTNMGRIFFITIRNSMGKPQLKLGKLLNKPFKLGIWSKIFNTNSSVVSLRNGPILGKGTRLVYITTNKGIFQTWQLSATNSHPTKLIDVNIYEAILESLQDLYPFAHGTLKIWDSHPLQDESSQLFLSSIYDSSCNETYYILSTIIFDSSSNSFTIFSTYRLNTFMESITDTKFKPKIFIPQMENANDTNEVTSILVMFPNAVVITQVNSKLDSSYSMRRKWEDIVSLRNDIDIIGSGYDSKSLYVLTKQMGVLQFFVKENEETNSKPEVGFVKSHVDQAVYFSKINANPIDFNLPPEISLDQESIEHDLKLTSEEIFHSNGKYIPPMLNTLGQHLSVRKEFFQNFLTFVAKNFNYKISPELKLDLIEKFEILNCCIKFNSIIRQSDVLNDIWEKTLSNYNLTQNEHLTTKTVVINSPDVFPVIFKQFLNHVVFVLFPSQNQNFKLNVTNLINLCFYDGILEEGEKTIRYELLELDPMEVDTSKLPWFINFDYLNCINQCFFDFTFACEEEGSLDSYKEGLLKIVKILYYQFNQFKIWINTQPVKSVNANDNFININNLYDDNHLDWNHVLCKVNLKEQCIQIAEFYKDLSGLVQTLQTLDQNDSTTVSLYETFFNEFPKEFSFTLFEYLIKHKKLNDLIFRFPQQHDVLIQFFQESAPKYGHVAWIQQILDGSYADAMNTLKNITVDDSKKGESLSECELHLNVAKLSSLLVEKDNLDINTLRKIQYNLDTIDAEKNISNKLKKGEVQICKRFKNGSIREVFNILVEELKSTTVVNLSDLVELYSMLDDEESLFIPLRLLSVDGNLLNFEVKKFLNALVWRRIVLLNASNEGDKLLQHIVKRVFDEELPKNNDFPLPSVDLLCDKSLLTPEYISETYGRFPIDQNAIREEIYEEISQVETLNSDNSLEIKLHSTIGSVAKEKNYTINYETNTVEY","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P36161","disprot_id":"DP02158","ncbi_taxon_id":559292,"regions_counter":2,"creator":"sventura","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":55,"region_id":"DP02158r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structural and functional analysis of Nup120 suggests ring formation of the Nup84 complex. <i> Seo HS, Ma Y, Debler EW, Wacker D, Kutik S, Blobel G, Hoelz A. </i> Proc Natl Acad Sci U S A, 2009","statement":[{"text":"Secondary structure predictions and limited proteolysis experiments suggest that the ≈55 N-terminal residues also are unstructured in the yeast Nup133 NTD. We refer to this 55-residue fragment (residues 1–55) as the N-terminal extension (NTE). Using circular dichroism spectroscopy, we confirmed a random coil conformation of the Nup133 NTE.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"sventura","start":1,"term_ontology":"IDPO","curator_name":"Salvador Ventura","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19706512","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":55,"term_name":"protein binding","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Structural and functional analysis of Nup120 suggests ring formation of the Nup84 complex. <i> Seo HS, Ma Y, Debler EW, Wacker D, Kutik S, Blobel G, Hoelz A. </i> Proc Natl Acad Sci U S A, 2009","statement":[{"text":"\"Further analysis revealed that an N-terminal Nup133 fragment containing only residues 1–15 was sufficient for complex formation with Nup120.\"","type":"Results"}],"term_id":"GO:0005515","curator_id":"sventura","start":1,"term_ontology":"GO","curator_name":"Salvador Ventura","reference_id":"19706512","version":3,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","cross_refs":[{"db":"PMID","id":"19706512"}],"region_id":"DP02158r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P36161","date":"2018-08-28T11:28:50.000Z","acc":"P36161","name":"Nucleoporin NUP133","length":1157,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000012FC14","genes":[{"name":{"value":"NUP133"},"synonyms":[{"value":"RAT3"}],"orfNames":[{"value":"YKR402"}],"olnNames":[{"value":"YKR082W"}]}],"alphafold_very_low_content":0.07087294727744166,"disorder_content":0.04753673292999136,"disprot_consensus":{"full":[{"start":1,"end":55,"type":"D"}],"Structural state":[{"start":1,"end":55,"type":"D"}],"Molecular function":[{"start":1,"end":55,"type":"F"}]}},{"features":{"pfam":[{"id":"PF09346","name":"SMI1 / KNR4 family (SUKH-1)","start":115,"end":286}]},"uniref50":"UniRef50_P32566","sequence":"MDLFKRKVKEWVYSLSTDDHYAEYNPDETPTFNMGKRLNSNNGQVNPSQMHLNSVDEEMSMGFQNGVPSNEDINIDEFTSTESNDGVSETLLAWRHIDFWTSEHNPDLNATLSDPCTQNDITHAEEDLEVSFPNPVKASFKIHDGQEDLESMTGTSGLFYGFQLMTLDQVVAMTQAWRNVAKNLNKRSQQGLSHVTSTGSSSSMERLNGNKFKLPNIPDQKSIPPNAVQPVYAHPAWIPLITDNAGNHIGVDLAPGPNGKYAQIITFGRDFDTKFVIAENWGEFLLSFANDLEAGNWYLVDDNDDYFSGDGELVFRDKKSNGPIQDYFEVLKRRTWIKYQENLRSQQQKSQPDTSLQEQKYVPASQKKVAAEQPSTLNAESIKGEDSGSADVQSVQDHESVKIVKTEPSEAETTTVNTESLGQAEHEIKADNVDIKQESERKEDEKQPKVEEKEHVENEHVTESAKKDDDVNKQTEEMNKKEENEIRSDDAKVEEAREEFENIAL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P32566","disprot_id":"DP02159","ncbi_taxon_id":559292,"regions_counter":1,"creator":"baykac","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":505,"region_id":"DP02159r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structure-function analysis of Knr4/Smi1, a newly member of intrinsically disordered proteins family, indispensable in the absence of a functional PKC1-SLT2 pathway in Saccharomyces cerevisiae. <i> Durand F, Dagkessamanskaia A, Martin-Yken H, Graille M, Van Tilbeurgh H, Uversky VN, François JM. </i> Yeast, 2008","term_id":"IDPO:0000002","curator_id":"baykac","start":340,"term_ontology":"IDPO","curator_name":"Burcu Aykac-Fas","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-3842-731X","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18668512","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P32566","date":"2018-08-28T11:33:29.000Z","acc":"P32566","name":"Cell wall assembly regulator SMI1","length":505,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000135AAD","genes":[{"name":{"value":"SMI1"},"synonyms":[{"value":"KNR4"},{"value":"KTR4"}],"orfNames":[{"value":"G8553"}],"olnNames":[{"value":"YGR229C"}]}],"alphafold_very_low_content":0.3702970297029703,"disorder_content":0.3287128712871287,"disprot_consensus":{"full":[{"start":340,"end":505,"type":"D"}],"Structural state":[{"start":340,"end":505,"type":"D"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MESKEPQLKGIVTRLFSQQGYFLQMHPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKASLYVAMNGEGYLYSSDVFTPECKFKESVFENYYVIYSSTLYRQQESGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPKPIEVCMYREPSLHEIGEKQGRSRKSSGTPTMNGGKVVNQDST","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"","disprot_id":"DP02160","ncbi_taxon_id":9606,"regions_counter":2,"creator":"rdavidovic","regions":[{"start":148,"end":181,"reference_id":"25232683","reference_source":"pmid","reference_html":"Structural analyses of Ca²⁺/CaM interaction with NaV channel C-termini reveal mechanisms of calcium-dependent regulation. <i> Wang C, Chung BC, Yan H, Wang HG, Lee SY, Pitt GS. </i> Nat Commun, 2014","date":"2022-10-26T14:20:52.915Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"4JQ0"}],"region_id":"DP02160r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0DP23"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":" Q14524"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"The PDB evidence shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T14:21:31.139Z"}}],"released":"2018_11","uniref100":"","date":"2018-08-28T11:51:43.000Z","acc":"P61328-2","name":"Isoform 2 of Fibroblast growth factor 12","length":181,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000E8058","genes":[{"name":{"value":"FGF12"},"synonyms":[{"value":"FGF12B"},{"value":"FHF1"}]}],"disorder_content":0.1878453038674033,"disprot_consensus":{"full":[{"start":148,"end":181,"type":"D"}],"Structural state":[{"start":148,"end":181,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00305","name":"Lipoxygenase","start":210,"end":643},{"id":"PF01477","name":"PLAT/LH2 domain","start":4,"end":102}],"gene3D":[{"start":2,"end":111,"id":"2.60.60.20","name":"PLAT/LH2 domain"},{"start":329,"end":661,"id":"1.20.245.10","name":"Lipoxygenase-1; Domain 5"},{"start":112,"end":248,"id":"1.20.245.10","name":"Lipoxygenase-1; Domain 5"}]},"uniref50":"UniRef50_P16050","sequence":"MGLYRIRVSTGASLYAGSNNQVQLWLVGQHGEAALGKRLWPARGKETELKVEVPEYLGPLLFVKLRKRHLLKDDAWFCNWISVQGPGAGDEVRFPCYRWVEGNGVLSLPEGTGRTVGEDPQGLFQKHREEELEERRKLYRWGNWKDGLILNMAGAKLYDLPVDERFLEDKRVDFEVSLAKGLADLAIKDSLNVLTCWKDLDDFNRIFWCGQSKLAERVRDSWKEDALFGYQFLNGANPVVLRRSAHLPARLVFPPGMEELQAQLEKELEGGTLFEADFSLLDGIKANVILCSQQHLAAPLVMLKLQPDGKLLPMVIQLQLPRTGSPPPPLFLPTDPPMAWLLAKCWVRSSDFQLHELQSHLLRGHLMAEVIVVATMRCLPSIHPIFKLIIPHLRYTLEINVRARTGLVSDMGIFDQIMSTGGGGHVQLLKQAGAFLTYSSFCPPDDLADRGLLGVKSSFYAQDALRLWEIIYRYVEGIVSLHYKTDVAVKDDPELQTWCREITEIGLQGAQDRGFPVSLQARDQVCHFVTMCIFTCTGQHASVHLGQLDWYSWVPNAPCTMRLPPPTTKDATLETVMATLPNFHQASLQMSITWQLGRRQPVMVAVGQHEEEYFSGPEPKAVLKKFREELAALDKEIEIRNAKLDMPYEYLRPSVVENSVAI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P16050","disprot_id":"DP02162","ncbi_taxon_id":9606,"regions_counter":1,"creator":"epapa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":162,"region_id":"DP02162r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Insights into the structure and dynamics of lysyl oxidase propeptide, a flexible protein with numerous partners. <i> Vallet SD, Miele AE, Uciechowska-Kaczmarzyk U, Liwo A, Duclos B, Samsonov SA, Ricard-Blum S. </i> Sci Rep, 2018","statement":[{"text":"Circular dichroism spectra of\nLOX-PP showed a single minimum near 200 nm, which is characteristic of an intrinsically disordered protein\n(IDP) (Fig. 2a). Te content in secondary structure of LOX-PP was calculated by deconvoluting the spectra with\nCONTIN-LL. Te content in α-helix and β-sheet was found to be 3.4% and 20.4% respectively, whereas the turn\ncontent was 11.8%, and the disorder 64.5%.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"epapa","start":22,"term_ontology":"IDPO","curator_name":"Elena Papaleo","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"30082873","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P16050","date":"2018-08-28T12:13:41.000Z","acc":"P16050","name":"Arachidonate 15-lipoxygenase","length":662,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000013E118","genes":[{"name":{"value":"ALOX15","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:433","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:433"}}]},"synonyms":[{"value":"LOG15"}]}],"alphafold_very_low_content":0,"disorder_content":0.21299093655589124,"disprot_consensus":{"full":[{"start":22,"end":162,"type":"D"}],"Structural state":[{"start":22,"end":162,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00014","name":"Kunitz/Bovine pancreatic trypsin inhibitor domain","start":2876,"end":2929},{"id":"PF00041","name":"Fibronectin type III domain","start":233,"end":316},{"id":"PF00041","name":"Fibronectin type III domain","start":332,"end":405},{"id":"PF00041","name":"Fibronectin type III domain","start":427,"end":487},{"id":"PF00041","name":"Fibronectin type III domain","start":509,"end":582},{"id":"PF00041","name":"Fibronectin type III domain","start":602,"end":675},{"id":"PF00041","name":"Fibronectin type III domain","start":688,"end":767},{"id":"PF00041","name":"Fibronectin type III domain","start":872,"end":948},{"id":"PF00041","name":"Fibronectin type III domain","start":958,"end":1042},{"id":"PF00092","name":"von Willebrand factor type A domain","start":38,"end":206},{"id":"PF00092","name":"von Willebrand factor type A domain","start":1054,"end":1224},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":1252,"end":1309},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":1489,"end":1547},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":1651,"end":1706},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":1718,"end":1774},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":2034,"end":2092},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":2101,"end":2157},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":2257,"end":2316},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":2324,"end":2372},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":2374,"end":2429},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":2466,"end":2522},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":2527,"end":2581},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":2583,"end":2632},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":2634,"end":2677},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":2722,"end":2782}],"gene3D":[{"start":776,"end":867,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":229,"end":330,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":868,"end":956,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":419,"end":502,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":686,"end":775,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":2868,"end":2937,"id":"4.10.410.10","name":"Pancreatic trypsin inhibitor Kunitz domain"},{"start":331,"end":418,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":599,"end":685,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":957,"end":1048,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":503,"end":598,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":36,"end":223,"id":"3.40.50.410","name":"von Willebrand factor, type A domain"},{"start":1051,"end":1244,"id":"3.40.50.410","name":"von Willebrand factor, type A domain"},{"start":2754,"end":2800,"id":"1.20.5.320","name":"6-Phosphogluconate Dehydrogenase, domain 3"}]},"uniref50":"UniRef50_Q02388","sequence":"MTLRLLVAALCAGILAEAPRVRAQHRERVTCTRLYAADIVFLLDGSSSIGRSNFREVRSFLEGLVLPFSGAASAQGVRFATVQYSDDPRTEFGLDALGSGGDVIRAIRELSYKGGNTRTGAAILHVADHVFLPQLARPGVPKVCILITDGKSQDLVDTAAQRLKGQGVKLFAVGIKNADPEELKRVASQPTSDFFFFVNDFSILRTLLPLVSRRVCTTAGGVPVTRPPDDSTSAPRDLVLSEPSSQSLRVQWTAASGPVTGYKVQYTPLTGLGQPLPSERQEVNVPAGETSVRLRGLRPLTEYQVTVIALYANSIGEAVSGTARTTALEGPELTIQNTTAHSLLVAWRSVPGATGYRVTWRVLSGGPTQQQELGPGQGSVLLRDLEPGTDYEVTVSTLFGRSVGPATSLMARTDASVEQTLRPVILGPTSILLSWNLVPEARGYRLEWRRETGLEPPQKVVLPSDVTRYQLDGLQPGTEYRLTLYTLLEGHEVATPATVVPTGPELPVSPVTDLQATELPGQRVRVSWSPVPGATQYRIIVRSTQGVERTLVLPGSQTAFDLDDVQAGLSYTVRVSARVGPREGSASVLTVRREPETPLAVPGLRVVVSDATRVRVAWGPVPGASGFRISWSTGSGPESSQTLPPDSTATDITGLQPGTTYQVAVSVLRGREEGPAAVIVARTDPLGPVRTVHVTQASSSSVTITWTRVPGATGYRVSWHSAHGPEKSQLVSGEATVAELDGLEPDTEYTVHVRAHVAGVDGPPASVVVRTAPEPVGRVSRLQILNASSDVLRITWVGVTGATAYRLAWGRSEGGPMRHQILPGNTDSAEIRGLEGGVSYSVRVTALVGDREGTPVSIVVTTPPEAPPALGTLHVVQRGEHSLRLRWEPVPRAQGFLLHWQPEGGQEQSRVLGPELSSYHLDGLEPATQYRVRLSVLGPAGEGPSAEVTARTESPRVPSIELRVVDTSIDSVTLAWTPVSRASSYILSWRPLRGPGQEVPGSPQTLPGISSSQRVTGLEPGVSYIFSLTPVLDGVRGPEASVTQTPVCPRGLADVVFLPHATQDNAHRAEATRRVLERLVLALGPLGPQAVQVGLLSYSHRPSPLFPLNGSHDLGIILQRIRDMPYMDPSGNNLGTAVVTAHRYMLAPDAPGRRQHVPGVMVLLVDEPLRGDIFSPIREAQASGLNVVMLGMAGADPEQLRRLAPGMDSVQTFFAVDDGPSLDQAVSGLATALCQASFTTQPRPEPCPVYCPKGQKGEPGEMGLRGQVGPPGDPGLPGRTGAPGPQGPPGSATAKGERGFPGADGRPGSPGRAGNPGTPGAPGLKGSPGLPGPRGDPGERGPRGPKGEPGAPGQVIGGEGPGLPGRKGDPGPSGPPGPRGPLGDPGPRGPPGLPGTAMKGDKGDRGERGPPGPGEGGIAPGEPGLPGLPGSPGPQGPVGPPGKKGEKGDSEDGAPGLPGQPGSPGEQGPRGPPGAIGPKGDRGFPGPLGEAGEKGERGPPGPAGSRGLPGVAGRPGAKGPEGPPGPTGRQGEKGEPGRPGDPAVVGPAVAGPKGEKGDVGPAGPRGATGVQGERGPPGLVLPGDPGPKGDPGDRGPIGLTGRAGPPGDSGPPGEKGDPGRPGPPGPVGPRGRDGEVGEKGDEGPPGDPGLPGKAGERGLRGAPGVRGPVGEKGDQGDPGEDGRNGSPGSSGPKGDRGEPGPPGPPGRLVDTGPGAREKGEPGDRGQEGPRGPKGDPGLPGAPGERGIEGFRGPPGPQGDPGVRGPAGEKGDRGPPGLDGRSGLDGKPGAAGPSGPNGAAGKAGDPGRDGLPGLRGEQGLPGPSGPPGLPGKPGEDGKPGLNGKNGEPGDPGEDGRKGEKGDSGASGREGRDGPKGERGAPGILGPQGPPGLPGPVGPPGQGFPGVPGGTGPKGDRGETGSKGEQGLPGERGLRGEPGSVPNVDRLLETAGIKASALREIVETWDESSGSFLPVPERRRGPKGDSGEQGPPGKEGPIGFPGERGLKGDRGDPGPQGPPGLALGERGPPGPSGLAGEPGKPGIPGLPGRAGGVGEAGRPGERGERGEKGERGEQGRDGPPGLPGTPGPPGPPGPKVSVDEPGPGLSGEQGPPGLKGAKGEPGSNGDQGPKGDRGVPGIKGDRGEPGPRGQDGNPGLPGERGMAGPEGKPGLQGPRGPPGPVGGHGDPGPPGAPGLAGPAGPQGPSGLKGEPGETGPPGRGLTGPTGAVGLPGPPGPSGLVGPQGSPGLPGQVGETGKPGAPGRDGASGKDGDRGSPGVPGSPGLPGPVGPKGEPGPTGAPGQAVVGLPGAKGEKGAPGGLAGDLVGEPGAKGDRGLPGPRGEKGEAGRAGEPGDPGEDGQKGAPGPKGFKGDPGVGVPGSPGPPGPPGVKGDLGLPGLPGAPGVVGFPGQTGPRGEMGQPGPSGERGLAGPPGREGIPGPLGPPGPPGSVGPPGASGLKGDKGDPGVGLPGPRGERGEPGIRGEDGRPGQEGPRGLTGPPGSRGERGEKGDVGSAGLKGDKGDSAVILGPPGPRGAKGDMGERGPRGLDGDKGPRGDNGDPGDKGSKGEPGDKGSAGLPGLRGLLGPQGQPGAAGIPGDPGSPGKDGVPGIRGEKGDVGFMGPRGLKGERGVKGACGLDGEKGDKGEAGPPGRPGLAGHKGEMGEPGVPGQSGAPGKEGLIGPKGDRGFDGQPGPKGDQGEKGERGTPGIGGFPGPSGNDGSAGPPGPPGSVGPRGPEGLQGQKGERGPPGERVVGAPGVPGAPGERGEQGRPGPAGPRGEKGEAALTEDDIRGFVRQEMSQHCACQGQFIASGSRPLPSYAADTAGSQLHAVPVLRVSHAEEEERVPPEDDEYSEYSEYSVEEYQDPEAPWDSDDPCSLPLDEGSCTAYTLRWYHRAVTGSTEACHPFVYGGCGGNANRFGTREACERRCPPRVVQSQGTGTAQD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q02388","disprot_id":"DP02163","ncbi_taxon_id":9606,"regions_counter":2,"creator":"baykac","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1978,"region_id":"DP02163r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The hinge region of type VII collagen is intrinsically disordered. <i> Richer BC, Seeger K. </i> Matrix Biol, 2014","term_id":"IDPO:0000002","curator_id":"lchemes","start":1940,"term_ontology":"IDPO","curator_name":"Lucia Chemes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0003-0192-9906","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24810542","statement":[{"text":"To gain insight into the potential function of the hinge region we investigated a heterologous expressed peptide by CD and NMR spectroscopy. CD spectroscopy implies that the hinge region is intrinsically disordered. Resonance assignment was performed and allowed secondary structure analysis based on the chemical shift values. Seven amino acids in the N-terminal moiety show residual α-helical conformation.","type":"Abstract"},{"text":"The CD spectrum (Fig. 3 a) of the hinge peptide shows a negative minimum at 200 nm and a negative shoulder at about 220 nm at 5 °C that are characteristic for intrinsically disordered proteins (Kjaergaard et al., 2010).","type":"Results"},{"text":"(b) Monitoring the CD signal at 200 nm indicates that alterations in the CD spectrum are not due to unfolding. Temperature dependency of the CD signal at 220 nm is provided in the supplemental information (supplemental Fig. A1).","type":"Figure"},{"text":"It was speculated that the hinge region might represent the trimerization domain of Col7 due to the presence of heptad repeats characteristic for coiled coil structures (McAlinden et al., 2003). However, CD spectroscopy clearly demonstrates that the hinge region does not adopt a coiled coil structure under the employed experimental conditions. Moreover, the CD-spectrum of the hinge region is typical for an intrinsically disordered protein. The negative shoulder at 220 nm can be interpreted as residual α-helical structure. This is in line with data obtained by NMR spectroscopy: (I) there is no signal dispersion observed in an 1H,15N-HSQC spectrum indicating the absence of secondary structure and (II) secondary structure prediction based on chemical shifts identified only seven amino acids (R24, L25, E27, T28, K32, A33, and S34) with dihedral angles corresponding to an α-helical conformation. The presence of residual secondary structure is commonly observed in disordered proteins (Dunker et al., 2002, Tompa, 2002).","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-04T08:12:38.978Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1940,"end":1978,"reference_id":"24810542","reference_source":"pmid","reference_html":"The hinge region of type VII collagen is intrinsically disordered. <i> Richer BC, Seeger K. </i> Matrix Biol, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP02163r002","statement":[{"text":"To gain insight into the potential function of the hinge region we investigated a heterologous expressed peptide by CD and NMR spectroscopy. CD spectroscopy implies that the hinge region is intrinsically disordered. Resonance assignment was performed and allowed secondary structure analysis based on the chemical shift values. Seven amino acids in the N-terminal moiety show residual α-helical conformation.","type":"Abstract"},{"text":"In the 1H,15N-HSQC of the hinge peptide the signals corresponding to the peptide backbone amide protons are not dispersed (Fig. 4). This lack of dispersion is characteristic for unfolded proteins. Resonance assignment of the backbone chemical shifts is nearly complete enabling determination of the secondary structure (Fig. 5 b)","type":"Results"},{"text":"For a patch of about 10 amino acids in the N-terminal moiety of the hinge peptide, the chemical shifts indicate an α-helical conformation for several amino acids. All other residues of the hinge peptide do not adopt neither α-helix nor β-strand conformation","type":"Results"},{"text":"Moreover, the CD-spectrum of the hinge region is typical for an intrinsically disordered protein. The negative shoulder at 220 nm can be interpreted as residual α-helical structure. This is in line with data obtained by NMR spectroscopy: (I) there is no signal dispersion observed in an 1H,15N-HSQC spectrum indicating the absence of secondary structure and (II) secondary structure prediction based on chemical shifts identified only seven amino acids (R24, L25, E27, T28, K32, A33, and S34) with dihedral angles corresponding to an α-helical conformation. The presence of residual secondary structure is commonly observed in disordered proteins (Dunker et al., 2002, Tompa, 2002).","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-04T08:12:36.597Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q02388","date":"2018-08-28T12:16:59.000Z","acc":"Q02388","name":"Collagen alpha-1(VII) chain","length":2944,"organism":"Homo sapiens","dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000126D20","genes":[{"name":{"value":"COL7A1"}}],"disorder_content":0.013247282608695652,"disprot_consensus":{"full":[{"start":1940,"end":1978,"type":"D"}],"Structural state":[{"start":1940,"end":1978,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03177","name":"Non-repetitive/WGA-negative nucleoporin C-terminal","start":739,"end":1062}],"gene3D":[{"start":65,"end":477,"id":"2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"},{"start":513,"end":1156,"id":"1.25.40.700","name":"1.25.40.700"}]},"uniref50":"UniRef50_Q8WUM0","sequence":"MFPAAPSPRTPGTGSRRGPLAGLGPGSTPRTASRKGLPLGSAVSSPVLFSPVGRRSSLSSRGTPTRMFPHHSITESVNYDVKTFGSSLPVKVMEALTLAEVDDQLTINIDEGGWACLVCKEKLIIWKIALSPITKLSVCKELQLPPSDFHWSADLVALSYSSPSGEAHSTQAVAVMVATREGSIRYWPSLAGEDTYTEAFVDSGGDKTYSFLTAVQGGSFILSSSGSQLIRLIPESSGKIHQHILPQGQGMLSGIGRKVSSLFGILSPSSDLTLSSVLWDRERSSFYSLTSSNISKWELDDSSEKHAYSWDINRALKENITDAIWGSESNYEAIKEGVNIRYLDLKQNCDGLVILAAAWHSADNPCLIYYSLITIEDNGCQMSDAVTVEVTQYNPPFQSEDLILCQLTVPNFSNQTAYLYNESAVYVCSTGTGKFSLPQEKIVFNAQGDSVLGAGACGGVPIIFSRNSGLVSITSRENVSILAEDLEGSLASSVAGPNSESMIFETTTKNETIAQEDKIKLLKAAFLQYCRKDLGHAQMVVDELFSSHSDLDSDSELDRAVTQISVDLMDDYPASDPRWAESVPEEAPGFSNTSLIILHQLEDKMKAHSFLMDFIHQVGLFGRLGSFPVRGTPMATRLLLCEHAEKLSAAIVLKNHHSRLSDLVNTAILIALNKREYEIPSNLTPADVFFREVSQVDTICECLLEHEEQVLRDAPMDSIEWAEVVINVNNILKDMLQAASHYRQNRNSLYRREESLEKEPEYVPWTATSGPGGIRTVIIRQHEIVLKVAYPQADSNLRNIVTEQLVALIDCFLDGYVSQLKSVDKSSNRERYDNLEMEYLQKRSDLLSPLLSLGQYLWAASLAEKYCDFDILVQMCEQTDNQSRLQRYMTQFADQNFSDFLFRWYLEKGKRGKLLSQPISQHGQLANFLQAHEHLSWLHEINSQELEKAHATLLGLANMETRYFAKKKTLLGLSKLAALASDFSEDMLQEKIEEMAEQERFLLHQETLPEQLLAEKQLNLSAMPVLTAPQLIGLYICEENRRANEYDFKKALDLLEYIDEEEDININDLKLEILCKALQRDNWSSSDGKDDPIEVSKDSIFVKILQKLLKDGIQLSEYLPEVKDLLQADQLGSLKSNPYFEFVLKANYEYYVQGQI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q8WUM0","disprot_id":"DP02164","ncbi_taxon_id":9606,"regions_counter":4,"creator":"sventura","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":269,"region_id":"DP02164r001","released":"2023_06","ec_id":"ECO:0006220","reference_html":"Structural and functional analysis of Nup133 domains reveals modular building blocks of the nuclear pore complex. <i> Berke IC, Boehmer T, Blobel G, Schwartz TU. </i> J Cell Biol, 2004","statement":[{"text":"A disordered 20-residue insertion is present in the DA loop connecting blades 3 and 4 (DA34).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":252,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-08T20:23:35.846Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1XKS"}],"reference_id":"15557116","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:43:22.254Z"}},{"start":478,"end":514,"reference_id":"15557116","reference_source":"pmid","reference_html":"Structural and functional analysis of Nup133 domains reveals modular building blocks of the nuclear pore complex. <i> Berke IC, Boehmer T, Blobel G, Schwartz TU. </i> J Cell Biol, 2004","date":"2023-05-08T20:29:48.204Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1XKS"}],"region_id":"DP02164r002","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered. ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:43:24.291Z"}},{"start":1,"end":70,"reference_id":"35679397","reference_source":"pmid","reference_html":"AI-based structure prediction empowers integrative structural analysis of human nuclear pores. <i> Mosalaganti S, Obarska-Kosinska A, Siggel M, Taniguchi R, Turoňová B, Zimmerli CE, Buczak K, Schmidt FH, Margiotta E, Mackmull MT, Hagen WJH, Hummer G, Kosinski J, Beck M. </i> Science, 2022","date":"2023-05-08T20:37:18.265Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7R5J"},{"db":"PDB","id":"7R5K"},{"db":"EMDB","id":"EMD-14321"},{"db":"EMDB","id":"EMD-14322"}],"region_id":"DP02164r003","statement":[{"text":"The electron microscopy structures of the Human nuclear pore complex (both dilated and constricted), shows this region from the NUP133 protein lacks electron density, indicating it is disordered. ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:43:27.648Z"}},{"start":1,"end":70,"reference_id":"35679397","reference_source":"pmid","reference_html":"AI-based structure prediction empowers integrative structural analysis of human nuclear pores. <i> Mosalaganti S, Obarska-Kosinska A, Siggel M, Taniguchi R, Turoňová B, Zimmerli CE, Buczak K, Schmidt FH, Margiotta E, Mackmull MT, Hagen WJH, Hummer G, Kosinski J, Beck M. </i> Science, 2022","date":"2023-12-11T14:15:08.429Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7R5K"},{"db":"PDB","id":"7R5J"},{"db":"EMDB","id":"14322"},{"db":"EMDB","id":"14321"}],"region_id":"DP02164r004","statement":[{"text":"The electron microscopy structures of the Human nuclear pore complex (both dilated and constricted), shows this region from the NUP133 protein lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-11T14:32:35.037Z"}}],"released":"2018_11","uniref100":"UniRef100_Q8WUM0","date":"2018-08-28T12:22:40.000Z","acc":"Q8WUM0","name":"Nuclear pore complex protein Nup133","length":1156,"organism":"Homo sapiens","dataset":["NDDs-related proteins","Condensates-related proteins"],"UniParc":"UPI0000073C12","genes":[{"name":{"value":"NUP133"}}],"alphafold_very_low_content":0.12024221453287197,"disorder_content":0.10813148788927336,"disprot_consensus":{"full":[{"start":1,"end":70,"type":"D"},{"start":252,"end":269,"type":"D"},{"start":478,"end":514,"type":"D"}],"Structural state":[{"start":1,"end":70,"type":"D"},{"start":252,"end":269,"type":"D"},{"start":478,"end":514,"type":"D"}],"Disorder function":[{"start":1,"end":70,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05450","name":"Nicastrin large lobe","start":232,"end":440},{"id":"PF18266","name":"Nicastrin small lobe","start":41,"end":197}],"gene3D":[{"start":183,"end":472,"id":"3.40.630.10","name":"Zn peptidases"}]},"uniref50":"UniRef50_Q54JT7","sequence":"MRFKNVLVLLLLLVFSVINSEPSAPATISDNIYTTLYSSYPCTKIMTSDGQFGCSSKHGGNSGILYLIDDDESYNNYFSYSQQKDIIVVLDTNYFNSTSVLNLHNKSKIEGIIVLTDTKKTYPYSPDSRYPNKIYGLYPNSNLEWNPNADGFTYFSFPFPIFAIDNQTSVAIRNVSKHNRDGQYPAWGAELDSFMQGAINSETCLRRGFCEPVGGQSIWSSFSSKIDKEKEIILVMLPFDTTAFFRDLSIGADQSSFATVTLLSVIKSLAAVDRSSWNKEVVFAFWNAERWGYVGSEYFINDLLNFQCKTYNSDKSKCIDPPRADLAFQTQINFTKISTIIELNQIGRAQLDKNLGKYSLYLHTAGTKTSSVTDILDQVASSYENSTITFKPTTQTELPPSSSMSFLKKTNKIPVVVITDHDYKYSNPYYGYEQDDNENVLGSTLNDIVYILSTFIDRIAGGNNNITIDKNFINILYPCFTSSITCFNILMKTYPLNEVPNFYSSVFGTSLTTTLSPYETKLIHRLLYSITQYNSTLTNCTSDNDCPSSLCYSGQCVSSNTHLHNALSLGFDFDTSKNVWKIVNSSYPIFTESNWDYTALKVFKIGNSTTEIWFLVSGLIELLVSIGLILYVKKFLSNRYKLL","taxonomy":["Eukaryota","Amoebozoa","Evosea","Eumycetozoa","Dictyostelia","Dictyosteliales","Dictyosteliaceae","Dictyostelium"],"uniref90":"UniRef90_F0ZBA6","disprot_id":"DP02165","ncbi_taxon_id":5786,"regions_counter":1,"creator":"rdavidovic","regions":[{"region_id":"DP02165r001","ec_ontology":"ECO","end":32,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":19,"version":3,"statement":[{"text":"The ECD of D. purpureum nicastrin (DpNCT; residues 19–611) yielded well-diffracting crystals in the space group P41212 (Table S1). The structure was determined by a combination of molecular replacement and bromide-based single-wavelength anomalous dispersion (SAD). The atomic model was refined to 1.95-Å resolution (Fig. 1A, Fig. S1, and Table S1). Residues 33–605 were assigned in the structure; 20 residues at the N and C termini are disordered in the crystals.","type":"Results"}],"term_name":"disorder","reference_html":"Crystal structure of the γ-secretase component nicastrin. <i> Xie T, Yan C, Zhou R, Zhao Y, Sun L, Yang G, Lu P, Ma D, Shi Y. </i> Proc Natl Acad Sci U S A, 2014","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"25197054","date":"2024-02-20T19:56:06.855Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4R12"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"506227","entry_name":"N-acetyl-D-glucosamine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}]}],"released":"2018_11","uniref100":"UniRef100_F0ZBA6","date":"2018-08-28T12:28:04.000Z","acc":"F0ZBA6","name":"Ncstrn_small domain-containing protein","length":643,"organism":"Dictyostelium purpureum","dataset":[],"UniParc":"UPI0002055B48","genes":[{"name":{"value":"ncstn","evidences":[{"code":"ECO:0000250","source":{"name":"UniProtKB","id":"Q54JT7","url":"https://www.uniprot.org/uniprot/Q54JT7"}}]},"orfNames":[{"value":"DICPUDRAFT_96800","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"EGC38810.1","url":"https://www.ebi.ac.uk/ena/browser/view/EGC38810.1"}}]}]}],"alphafold_very_low_content":0.006220839813374806,"disorder_content":0.02177293934681182,"disprot_consensus":{"full":[{"start":19,"end":32,"type":"D"}],"Structural state":[{"start":19,"end":32,"type":"D"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MVRRFLVTLRIRRACGPPRVRVFVVHIPRLTGEWAAPGAPAAVALVLMLLRSQRLGQQPLPRRPGHDDGQRPSGGAAAAPRRGAQLRRPRHSHPTRARRCPGGLPGHAGGAAPGRGAAGRARCLGPSARGPG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"","disprot_id":"DP02167","ncbi_taxon_id":9606,"regions_counter":16,"creator":"epapa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":132,"region_id":"DP02167r001","released":"2022_12","ec_id":"ECO:0006204","reference_html":"Identification of a novel nucleophosmin-interaction motif in the tumor suppressor p14arf. <i> Luchinat E, Chiarella S, Franceschini M, Di Matteo A, Brunori M, Banci L, Federici L. </i> FEBS J, 2018","statement":[{"text":"Figure 1C,D show the CD spectrum of p14arf and its thermal denaturation, respectively. The shape of the spectrum is that typical of unstructured proteins, and the thermal denaturation profile suggests the absence of cooperative transitions from folded to unfolded species.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-07-26T18:42:49.484Z","reference_source":"pmid","term_name":"disorder","reference_id":"29283500","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:21:52.763Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":132,"region_id":"DP02167r003","released":"2022_12","ec_id":"ECO:0006165","reference_html":"Identification of a novel nucleophosmin-interaction motif in the tumor suppressor p14arf. <i> Luchinat E, Chiarella S, Franceschini M, Di Matteo A, Brunori M, Banci L, Federici L. </i> FEBS J, 2018","statement":[{"text":"The longitudinal (R1), and transverse (R2) 15N-amide relaxation rates (Fig. 2B), the 15N-nuclear overhauser effect (NOE; Fig. 2C) and the neighbor-corrected secondary structure propensity values calculated from the backbone chemical shifts (Fig. 2D) all indicate that the C-terminal fragment 57–132 of p14arf is intrinsically unstructured and does not have any secondary structure propensity in solution.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":57,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-07-26T18:35:10.913Z","reference_source":"pmid","term_name":"disorder","reference_id":"29283500","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:21:55.435Z"}},{"start":1,"end":14,"reference_id":"12630860","reference_source":"pmid","reference_html":"Peptides derived from two dynamically disordered proteins self-assemble into amyloid-like fibrils. <i> Bothner B, Aubin Y, Kriwacki RW. </i> J Am Chem Soc, 2003","date":"2022-07-26T18:16:33.551Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP02167r004","statement":[{"text":"Circular dichroism (CD) spectropolarimetry shows that isolated peptides comprised of the A1 and H1 motifs (p14Arf 1−14 and Hdm2 240−254, respectively) are highly disordered in solution (Figure 1A and B, red and violet traces, respectively).","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:21:56.879Z"}},{"start":1,"end":14,"reference_id":"12630860","reference_source":"pmid","reference_html":"Peptides derived from two dynamically disordered proteins self-assemble into amyloid-like fibrils. <i> Bothner B, Aubin Y, Kriwacki RW. </i> J Am Chem Soc, 2003","date":"2022-07-26T18:19:55.772Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q00987","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02167r005","statement":[{"text":"However, when combined, the components of the binary mixture self-assemble, forming β-strand-containing supramolecular structures of low solubility (Figure 1A and B, other traces). The appearance of a minimum in the CD spectra of the assemblies at 216 nm and the increase in ellipticity at 193 nm are consistent with the formation of β-strand-containing structures. ","type":"Article"},{"text":"When either peptide was titrated into a solution of the other, both NMR and CD spectra revealed that binding was saturable.","type":"Article"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:22:00.729Z"}},{"start":1,"end":14,"reference_id":"12630860","reference_source":"pmid","reference_html":"Peptides derived from two dynamically disordered proteins self-assemble into amyloid-like fibrils. <i> Bothner B, Aubin Y, Kriwacki RW. </i> J Am Chem Soc, 2003","date":"2022-07-26T18:21:40.051Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP02167r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q00987"}],"statement":[{"text":"However, when combined, the components of the binary mixture self-assemble, forming β-strand-containing supramolecular structures of low solubility (Figure 1A and B, other traces). The appearance of a minimum in the CD spectra of the assemblies at 216 nm and the increase in ellipticity at 193 nm are consistent with the formation of β-strand-containing structures. ","type":"Article"},{"text":"Maximal β-strand character was observed when the molar ratio of A1:H1 was 1:1 (Figure 1A and B, green trace versus others). ","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:21:58.392Z"}},{"start":1,"end":14,"reference_id":"12630860","reference_source":"pmid","reference_html":"Peptides derived from two dynamically disordered proteins self-assemble into amyloid-like fibrils. <i> Bothner B, Aubin Y, Kriwacki RW. </i> J Am Chem Soc, 2003","date":"2022-07-26T18:22:39.725Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q00987","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02167r007","statement":[{"text":"The solution of binary assemblies is characterized by visible turbidity and the disappearance of 1H NMR resonances that, before mixing, were observed for the monodisperse, free peptides (data not shown). When either peptide was titrated into a solution of the other, both NMR and CD spectra revealed that binding was saturable. ","type":"Article"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:22:03.917Z"}},{"start":1,"end":14,"reference_id":"12630860","reference_source":"pmid","reference_html":"Peptides derived from two dynamically disordered proteins self-assemble into amyloid-like fibrils. <i> Bothner B, Aubin Y, Kriwacki RW. </i> J Am Chem Soc, 2003","date":"2022-07-26T18:27:58.676Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","region_id":"DP02167r008","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q00987"}],"statement":[{"text":"Figure 3A shows that A1/H1 co-assemblies are networks of short, thin fibrils that are 10−20 nm long and less than 5 nm wide. These structures are morphologically similar to amyloid protofibrils derived from the β-amyloid peptide,24 insulin,23 lysozyme, 25 and an SH3 domain.","type":"Article"},{"text":"To test their stability and potential for further self-assembly, A1/H1 protofibrils were heated. The structure of A1/H1 co-assemblies became more organized after treatment (Figure 3B), appearing as distinct fibrils that were hundreds of nanometers in length. The long fibrils appeared to be bundled together into parallel, flat ribbons comprised of 3−6 individual fibrils.","type":"Article"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:22:05.404Z"}},{"start":84,"end":103,"reference_id":"29283500","reference_source":"pmid","reference_html":"Identification of a novel nucleophosmin-interaction motif in the tumor suppressor p14arf. <i> Luchinat E, Chiarella S, Franceschini M, Di Matteo A, Brunori M, Banci L, Federici L. </i> FEBS J, 2018","date":"2022-07-26T18:49:57.447Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P06748","operator":null,"partner_start":16,"partner_end":123}],"region_id":"DP02167r009","statement":[{"text":"A broad peak is observed in the chromatogram of a 1 : 2 mixture of NPM1-Nter:p14arf-NoLS, at a smaller elution volume than free pentameric NPM1-Nter. This peak has a calculated MW of 200–500 kDa, consistent with the formation of large aggregates, while the MW calculated on the peak of pentameric NPM1-Nter increases from 72 kDa to 95 kDa, suggesting that a complex could be formed between a NPM1 pentamer and several p14arf-NoLS peptides.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:22:06.911Z"}},{"start":84,"end":103,"reference_id":"29283500","reference_source":"pmid","reference_html":"Identification of a novel nucleophosmin-interaction motif in the tumor suppressor p14arf. <i> Luchinat E, Chiarella S, Franceschini M, Di Matteo A, Brunori M, Banci L, Federici L. </i> FEBS J, 2018","date":"2022-07-26T18:51:08.079Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P06748","operator":null,"partner_start":16,"partner_end":123}],"region_id":"DP02167r010","statement":[{"text":"Under these conditions, small chemical shift variations were observed, together with an increase in line-width, indicative of an exchange between the free protein and the aggregated, high molecular weight complex, which could be mapped to the NPM1-Nter structure (Fig. 8B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:22:09.470Z"}},{"start":1,"end":22,"reference_id":"10801444","reference_source":"pmid","reference_html":"Contribution of two independent MDM2-binding domains in p14(ARF) to p53 stabilization. <i> Lohrum MA, Ashcroft M, Kubbutat MH, Vousden KH. </i> Curr Biol, 2000","date":"2022-07-26T19:36:23.638Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0097371","term_name":"MDM2/MDM4 family protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005644","ec_ontology":"ECO","ec_name":"immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q00987","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02167r011","statement":[{"text":"Analysis of smaller p14ARF peptides showed that residues 1–22 retained the ability to bind MDM2, whereas Tx–ARF23–44 and Tx–ARF56–64 showed no evidence of binding (Figure 1b, left).","type":"Results"},{"text":"MDM2 is an E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a member of the MDM2/MDM4 protein family, comprising negative regulators of p53.\" [InterPro:IPR016495]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:22:10.897Z"}},{"start":1,"end":22,"reference_id":"10801444","reference_source":"pmid","reference_html":"Contribution of two independent MDM2-binding domains in p14(ARF) to p53 stabilization. <i> Lohrum MA, Ashcroft M, Kubbutat MH, Vousden KH. </i> Curr Biol, 2000","date":"2022-07-26T19:20:20.817Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1902570","term_name":"protein localization to nucleolus","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005804","ec_ontology":"ECO","ec_name":"immunofluorescence evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q00987","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02167r012","statement":[{"text":"Analysis of proteins containing amino-terminal p14ARF peptides showed that each protein that contained the first 22 amino acids localized to the nucleolus (Figure 2e–h,k,l). In contrast, constructs expressing p14ARF peptides that failed to interact with MDM2 (Tx–ARF35–64, Tx–ARF23–44 and Tx–ARF56–64) also failed to localize to the nucleolus (Figure 2i,j,m–p).","type":"Results"},{"text":"Expression of each of the amino-terminal Tx–ARF proteins that retained the ability to bind MDM2 and localize to the nucleolus also resulted in relocalization of MDM2 to the nucleolus (Figure 3e–h,k,l). MDM2 expressed with non-binding thioredoxin-p14ARF proteins (Tx–ARF35–64, Tx–ARF23–44 and Tx–ARF56–64) remained in the nucleoplasm, with evidence of nucleolar exclusion (Figure 3i,j,m–p).","type":"Results"}],"term_comment":"","term_def":"\"A process in which a protein is transported to, or maintained in, a location within a nucleolus.\" [GOC:TermGenie, PMID:22809626]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:22:12.431Z"}},{"start":1,"end":34,"reference_id":"10801444","reference_source":"pmid","reference_html":"Contribution of two independent MDM2-binding domains in p14(ARF) to p53 stabilization. <i> Lohrum MA, Ashcroft M, Kubbutat MH, Vousden KH. </i> Curr Biol, 2000","date":"2022-07-26T19:36:06.275Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1904666","term_name":"regulation of ubiquitin protein ligase activity","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005644","ec_ontology":"ECO","ec_name":"immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q00987","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02167r013","statement":[{"text":"MDM2-mediated degradation of p53 was efficiently inhibited by coexpression of full-length p14ARF (Figure 4a). Analysis of smaller regions of p14ARF showed that each amino-terminal p14ARF peptide that retained the ability to bind and relocalize MDM2 to the nucleolus inhibited the degradation of p53 (Figure 4a), although the smallest peptide (1–22) was reproducibly slightly less efficient than the full-length protein. In contrast, proteins containing p14ARF peptides that failed to bind MDM2 (Tx–ARF35–64 and Tx–ARF56–64) did not prevent MDM2-mediated degradation of p53 (Figure 4a). ","type":"Results"},{"text":"MDM2 is an E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome. ","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of ubiquitin protein ligase activity.\" [GO_REF:0000059, GOC:dph, GOC:TermGenie, GOC:vw, PMID:10921876, PMID:26216882]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:22:14.226Z"}},{"start":85,"end":101,"reference_id":"10360174","reference_source":"pmid","reference_html":"Mutations in human ARF exon 2 disrupt its nucleolar localization and impair its ability to block nuclear export of MDM2 and p53. <i> Zhang Y, Xiong Y. </i> Mol Cell, 1999","date":"2022-07-26T19:49:24.271Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0034504","term_name":"protein localization to nucleus","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007106","ec_ontology":"ECO","ec_name":"green fluorescent protein fusion protein localization evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","region_id":"DP02167r014","statement":[{"text":"These experiments identified a sequence—between residues 83 and 101 within exon 2 of ARF—necessary for localizing ARF to the nucleolus.","type":"Results"},{"text":"The ARF85–101-GFP fusion protein exhibited significant accumulation both in the nucleoplasm and nucleolus (Figure 1Db and 1Dd), demonstrating that residues 85 through 101 are also sufficient for localizing a heterologous protein to the nucleus and nucleolus.","type":"Results"}],"term_comment":"","term_def":"\"A process in which a protein transports or maintains the localization of another protein to the nucleus.\" [GOC:ecd]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:22:16.156Z"}},{"start":1,"end":132,"reference_id":"10360174","reference_source":"pmid","reference_html":"Mutations in human ARF exon 2 disrupt its nucleolar localization and impair its ability to block nuclear export of MDM2 and p53. <i> Zhang Y, Xiong Y. </i> Mol Cell, 1999","date":"2022-07-27T13:36:21.020Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031647","term_name":"regulation of protein stability","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006170","ec_ontology":"ECO","ec_name":"quantitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IEP","region_id":"DP02167r015","statement":[{"text":"The p53 protein level was increased about 150% when cotransfected with an ARF-expressing plasmid (lane 2). However, when cotransfected with equal amounts of plasmid DNA expressing the exon 1β–encoded ARF N-terminal domain (lane 3) or tumor-associated ARFR98L (lane 4) and ARFR98Q (lane 5) mutant proteins, the level of p53, albeit still higher than that accumulated in the absence of ARF, is reproducibly half that seen with wild-type ARF cotransfection.","type":"Results"},{"text":"These results indicate that the ARF N-terminal domain is capable of inhibiting MDM2-mediated p53 degradation when overexpressed, but deletion or tumor-derived mutations in the exon 2 domain reduce ARF’s ability to stabilize p53. Hence, the full activity of ARF in stabilizing p53 requires both the N- and C-terminal domains.","type":"Results"},{"text":"Mutations in Exon 2 Reduce ARF’s Ability to Stabilize p53","type":"Results"}],"term_comment":"","term_def":"\"Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.\" [GOC:dph, GOC:mah, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:22:17.737Z"}},{"start":1,"end":132,"reference_id":"10360174","reference_source":"pmid","reference_html":"Mutations in human ARF exon 2 disrupt its nucleolar localization and impair its ability to block nuclear export of MDM2 and p53. <i> Zhang Y, Xiong Y. </i> Mol Cell, 1999","date":"2022-07-27T14:38:08.529Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0030575","term_name":"nuclear body organization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005804","ec_ontology":"ECO","ec_name":"immunofluorescence evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","region_id":"DP02167r016","statement":[{"text":"ARF Colocalizes with MDM2 in the Nucleoplasm to Form Nuclear Bodies","type":"Results"},{"text":"The MDM2 and ARF nuclear bodies display identical punctate patterns, suggesting MDM2 and ARF colocalized in the nuclear bodies, which were not seen in control virus–infected cells (Figure 3C) or in ARF-negative (uninfected) cells in the same viewing field of Ad-E2F1-infected populations. ","type":"Results"},{"text":"p53 was also relocalized, from an even distribution in the nucleoplasm to colocalization with MDM2 and ARF in the nuclear bodies (Figure 3C, α-p53 staining).","type":"Results"},{"text":"RF-MDM2-p53 nuclear bodies were also observed in cells triply transfected with plasmid DNAs expressing each of the three proteins (Figure 4B, column 1).","type":"Results"},{"text":"Thus, both the MDM2-binding activity, encoded by the exon 1β, and the nucleolus-localizing activity residing in the exon 2 domain are important for ARF, p53, and MDM2 to form nuclear bodies.","type":"Results"}],"term_comment":"","term_def":"\"A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of any of the extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins.\" [GOC:dph, GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-28T13:22:19.529Z"}}],"released":"2018_11","uniref100":"","date":"2018-08-28T12:49:25.000Z","acc":"Q8N726-1","name":"Isoform tumor suppressor ARF of Tumor suppressor ARF","length":132,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI000006E6F2","genes":[{"name":{"value":"CDKN2A","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAM77919.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAM77919.1"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:1787","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:1787"}}]},"synonyms":[{"value":"CDKN2","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAC60649.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAC60649.1"}}]},{"value":"MLM"}]}],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":14,"type":"T"},{"start":15,"end":132,"type":"D"}],"Structural state":[{"start":1,"end":132,"type":"D"}],"Molecular function":[{"start":1,"end":22,"type":"F"},{"start":84,"end":103,"type":"F"}],"Structural transition":[{"start":1,"end":14,"type":"T"}],"Biological process":[{"start":1,"end":132,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00005","name":"ABC transporter","start":376,"end":526},{"id":"PF00664","name":"ABC transporter transmembrane region","start":30,"end":307}],"gene3D":[{"start":2,"end":340,"id":"1.20.1560.10","name":"ABC transporter type 1, transmembrane domain"},{"start":349,"end":600,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_F2NQU3","sequence":"MTEDTYSKAFDRALFARILRYVWPYRLQVVLALLFLLVVTLAAAATPLFFKWAIDLALVPTEPRPLAERFHLLLWISLGFLAVRAVHFAATYGETYLIQWVGQRVLFDLRSDLFAKLMRLHPGFYDRNPVGRLMTRVTSDVDAINQFITGGLVGVIADLFTLVGLLGFMLFLSPKLTLVVLLVAPVLLAVTTWVRLGMRSAYREMRLRLARVNAALQENLSGVETIQLFVKEREREEKFDRLNRDLFRAWVEIIRWFALFFPVVGFLGDFAVASLVYYGGGEVVRGAVSLGLLVAFVDYTRQLFQPLQDLSDKFNLFQGAMASAERIFGVLDTEEELKDPEDPTPIRGFRGEVEFRDVWLAYTPKGVEPTEKDWVLKGVSFRVRPGEKVALVGATGAGKTSVVSLIARFYDPQRGCVFLDGVDVRRYRQEELRRHVGIVLQEPFLFSGTVLDNLRLFDPSVPPERVEEVARFLGAHEFILRLPKGYQTVLGERGAGLSTGEKQLLALVRALLASPDILLILDEATASVDSETEKRLQEALYKAMEGRTSLIIAHRLSTIRHVDRILVFRKGRLVEEGSHEELLAKGGYYAALYRLQFQEA","taxonomy":["Bacteria","Deinococcus-Thermus","Deinococci","Thermales","Thermaceae","Thermus"],"uniref90":"UniRef90_F6DI55","disprot_id":"DP02168","ncbi_taxon_id":262724,"regions_counter":1,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":319,"region_id":"DP02168r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure and mechanistic basis of a functional homolog of the antigen transporter TAP. <i> Nöll A, Thomas C, Herbring V, Zollmann T, Barth K, Mehdipour AR, Tomasiak TM, Brüchert S, Joseph B, Abele R, Oliéric V, Wang M, Diederichs K, Hummer G, Stroud RM, Pos KM, Tampé R. </i> Proc Natl Acad Sci U S A, 2017","statement":[{"text":"The region with the highest mobility in TmrAB is indeed located in TM6 of TmrA right above the elbow helix and spans roughly 16 aa (residues 304–319). The weak electron density in this region, which includes a proline and glycine, reflects its high mobility.","type":"Discussion"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":304,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5MKK"}],"reference_id":"28069938","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q72J05","date":"2018-08-28T12:56:21.000Z","acc":"Q72J05","name":"Multidrug resistance ABC transporter ATP-binding and permease protein","length":600,"organism":"Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)","dataset":[],"UniParc":"UPI00003523F3","genes":[{"olnNames":[{"value":"TT_C0976","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAS81318.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAS81318.1"}}]}]}],"alphafold_very_low_content":0.018333333333333333,"disorder_content":0.02666666666666667,"disprot_consensus":{"full":[{"start":304,"end":319,"type":"D"}],"Structural state":[{"start":304,"end":319,"type":"D"}]}},{"features":{"pfam":[{"id":"PF01497","name":"Periplasmic binding protein","start":26,"end":217}],"gene3D":[{"start":21,"end":140,"id":"3.40.50.1980","name":"Nitrogenase molybdenum iron protein domain"},{"start":141,"end":266,"id":"3.40.50.1980","name":"Nitrogenase molybdenum iron protein domain"}]},"uniref50":"UniRef50_P37028","sequence":"MAKSLFRALVALSFLAPLWLNAAPRVITLSPANTELAFAAGITPVGVSSYSDYPPQAQKIEQVSTWQGMNLERIVALKPDLVIAWRGGNAERQVDQLASLGIKVMWVDATSIEQIANALRQLAPWSPQPDKAEQAAQSLLDQYAQLKAQYADKPKKRVFLQFGINPPFTSGKESIQNQVLEVCGGENIFKDSRVPWPQVSREQVLARSPQAIVITGGPDQIPKIKQYWGEQLKIPVIPLTSDWFERASPRIILAAQQLCNALSQVD","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P37028","disprot_id":"DP02169","ncbi_taxon_id":83333,"regions_counter":1,"creator":"sventura","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":232,"region_id":"DP02169r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Conformational Change of a Tryptophan Residue in BtuF Facilitates Binding and Transport of Cobinamide by the Vitamin B12 Transporter BtuCD-F. <i> Mireku SA, Ruetz M, Zhou T, Korkhov VM, Kräutler B, Locher KP. </i> Sci Rep, 2017","statement":[{"text":"The disordered amino acid residue stretch (217 to 232) is indicated with a dashed black line.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"sventura","start":217,"term_ontology":"IDPO","curator_name":"Salvador Ventura","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5m29"}],"reference_id":"28128319","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P37028","date":"2018-08-28T12:59:38.000Z","acc":"P37028","name":"Vitamin B12-binding protein","length":266,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI0000126B26","genes":[{"name":{"value":"btuF"},"synonyms":[{"value":"yadT"}],"olnNames":[{"value":"b0158"},{"value":"JW0154"}]}],"alphafold_very_low_content":0,"disorder_content":0.06015037593984962,"disprot_consensus":{"full":[{"start":217,"end":232,"type":"D"}],"Structural state":[{"start":217,"end":232,"type":"D"}]}},{"features":{"pfam":[{"id":"PF09405","name":"CASC3/Barentsz eIF4AIII binding","start":144,"end":248}]},"uniref50":"UniRef50_O15234","sequence":"MADRRRQRASQDTEDEESGASGSDSGGSPLRGGGSCSGSAGGGGSGSLPSQRGGRTGALHLRRVESGGAKSAEESECESEDGIEGDAVLSDYESAEDSEGEEGEYSEEENSKVELKSEANDAVNSSTKEEKGEEKPDTKSTVTGERQSGDGQESTEPVENKVGKKGPKHLDDDEDRKNPAYIPRKGLFFEHDLRGQTQEEEVRPKGRQRKLWKDEGRWEHDKFREDEQAPKSRQELIALYGYDIRSAHNPDDIKPRRIRKPRYGSPPQRDPNWNGERLNKSHRHQGLGGTLPPRTFINRNAAGTGRMSAPRNYSRSGGFKEGRAGFRPVEAGGQHGGRSGETVKHEISYRSRRLEQTSVRDPSPEADAPVLGSPEKEEAASEPPAAAPDAAPPPPDRPIEKKSYSRARRTRTKVGDAVKLAEEVPPPPEGLIPAPPVPETTPTPPTKTGTWEAPVDSSTSGLEQDVAQLNIAEQNWSPGQPSFLQPRELRGMPNHIHMGAGPPPQFNRMEEMGVQGGRAKRYSSQRQRPVPEPPAPPVHISIMEGHYYDPLQFQGPIYTHGDSPAPLPPQGMLVQPGMNLPHPGLHPHQTPAPLPNPGLYPPPVSMSPGQPPPQQLLAPTYFSAPGVMNFGNPSYPYAPGALPPPPPPHLYPNTQAPSQVYGGVTYYNPAQQQVQPKPSPPRRTPQPVTIKPPPPEVVSRGSS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O15234","disprot_id":"DP02170","ncbi_taxon_id":9606,"regions_counter":17,"creator":"vacs","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":215,"region_id":"DP02170r001","released":"2025_12","ec_id":"ECO:0006220","reference_html":"Insights into the recruitment of the NMD machinery from the crystal structure of a core EJC-UPF3b complex. <i> Buchwald G, Ebert J, Basquin C, Sauliere J, Jayachandran U, Bono F, Le Hir H, Conti E. </i> Proc Natl Acad Sci U S A, 2010","statement":[{"text":"The refined model consists of MAGO residues 4–146, Y14 residues 66–154, eIF4AIII residues 22–411, two segments of BTZ comprising residues 169–194 and 216–248, and the C-terminal region of UPF3b encompassing residues 418–432 (Fig. 1). Other portions of the proteins are not present in the structure, and are either poorly ordered or were separated upon proteolysis.","type":"Results"},{"text":"After a disordered linker of about 20 residues, BTZ extends onto the first RecA-like domain.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":195,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2025-11-21T18:48:46.704Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2XB2"}],"reference_id":"20479275","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y5S9 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61326"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P38919"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9BZI7"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":213,"region_id":"DP02170r002","released":"2025_12","ec_id":"ECO:0006220","reference_html":"The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA. <i> Bono F, Ebert J, Lorentzen E, Conti E. </i> Cell, 2006","statement":[{"text":"The dotted line in red shows the approximate path of a portion of Btz not present in the electron density (residues 198–213; Figure 1).","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":198,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2025-11-21T18:57:52.871Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2J0S"},{"db":"PDB","id":"2J0Q"}],"reference_id":"16923391","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61326 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y5S9"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P38919"}]},{"start":137,"end":168,"reference_id":"20479275","reference_source":"pmid","reference_html":"Insights into the recruitment of the NMD machinery from the crystal structure of a core EJC-UPF3b complex. <i> Buchwald G, Ebert J, Basquin C, Sauliere J, Jayachandran U, Bono F, Le Hir H, Conti E. </i> Proc Natl Acad Sci U S A, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2XB2"}],"region_id":"DP02170r003","statement":[{"text":"The refined model consists of MAGO residues 4–146, Y14 residues 66–154, eIF4AIII residues 22–411, two segments of BTZ comprising residues 169–194 and 216–248, and the C-terminal region of UPF3b encompassing residues 418–432 (Fig. 1). Other portions of the proteins are not present in the structure, and are either poorly ordered or were separated upon proteolysis.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-11-21T18:52:13.856Z"}},{"start":249,"end":286,"reference_id":"20479275","reference_source":"pmid","reference_html":"Insights into the recruitment of the NMD machinery from the crystal structure of a core EJC-UPF3b complex. <i> Buchwald G, Ebert J, Basquin C, Sauliere J, Jayachandran U, Bono F, Le Hir H, Conti E. </i> Proc Natl Acad Sci U S A, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2XB2"}],"region_id":"DP02170r004","statement":[{"text":"The refined model consists of MAGO residues 4–146, Y14 residues 66–154, eIF4AIII residues 22–411, two segments of BTZ comprising residues 169–194 and 216–248, and the C-terminal region of UPF3b encompassing residues 418–432 (Fig. 1). Other portions of the proteins are not present in the structure, and are either poorly ordered or were separated upon proteolysis.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-11-21T18:52:36.327Z"}},{"start":195,"end":215,"reference_id":"20479275","reference_source":"pmid","reference_html":"Insights into the recruitment of the NMD machinery from the crystal structure of a core EJC-UPF3b complex. <i> Buchwald G, Ebert J, Basquin C, Sauliere J, Jayachandran U, Bono F, Le Hir H, Conti E. </i> Proc Natl Acad Sci U S A, 2010","date":"2025-11-21T18:50:55.737Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"PDB","id":"2XB2"}],"region_id":"DP02170r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61326"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9BZI7"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P38919"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y5S9"}],"statement":[{"text":"The refined model consists of MAGO residues 4–146, Y14 residues 66–154, eIF4AIII residues 22–411, two segments of BTZ comprising residues 169–194 and 216–248, and the C-terminal region of UPF3b encompassing residues 418–432 (Fig. 1). Other portions of the proteins are not present in the structure, and are either poorly ordered or were separated upon proteolysis.","type":"Results"},{"text":"After a disordered linker of about 20 residues, BTZ extends onto the first RecA-like domain.","type":"Results"}]},{"start":1,"end":169,"reference_id":"28502770","reference_source":"pmid","reference_html":"An Atomic Structure of the Human Spliceosome. <i> Zhang X, Yan C, Hang J, Finci LI, Lei J, Shi Y. </i> Cell, 2017","date":"2025-11-24T14:43:16.596Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008037","ec_ontology":"ECO","ec_name":"curator inference based on intrinsic disorder prediction used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"PDB","id":"5XJC"}],"region_id":"DP02170r006","statement":[{"text":"Cryo-EM structure of the human spliceosome just prior to exon ligation show this region of the MLN51protein lacks electron density. In combination with prediction data from MobiDB and AlphaFold, is posible to infer this region is likely disordered.","type":"Article"}]},{"start":195,"end":703,"reference_id":"28502770","reference_source":"pmid","reference_html":"An Atomic Structure of the Human Spliceosome. <i> Zhang X, Yan C, Hang J, Finci LI, Lei J, Shi Y. </i> Cell, 2017","date":"2025-11-24T14:43:08.336Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008037","ec_ontology":"ECO","ec_name":"curator inference based on intrinsic disorder prediction used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"PDB","id":"5XJC"}],"region_id":"DP02170r007","statement":[{"text":"Cryo-EM structure of the human spliceosome just prior to exon ligation show this region of the MLN51protein lacks electron density. In combination with prediction data from MobiDB and AlphaFold, is posible to infer this region is likely disordered.","type":"Article"}]},{"start":216,"end":246,"reference_id":"16931718","reference_source":"pmid","reference_html":"Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA. <i> Andersen CB, Ballut L, Johansen JS, Chamieh H, Nielsen KH, Oliveira CL, Pedersen JS, Séraphin B, Le Hir H, Andersen GR. </i> Science, 2006","date":"2025-11-24T14:19:24.241Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0017151","term_name":"DEAD/H-box RNA helicase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"PDB","id":"2HYI"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P38919","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02170r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"8758","entry_name":null},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61326"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y5S9"}],"statement":[{"text":"Residues 216 to 246 contact patches C, D, and E in eIF4AIII domain 1 (Fig. 1C and fig. S2), explaining why the mutation of MLN51 Tyr240 and Gly241 disrupts formation of the EJC core (3). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a DEAD/H-box RNA helicase.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":216,"end":246,"reference_id":"16931718","reference_source":"pmid","reference_html":"Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA. <i> Andersen CB, Ballut L, Johansen JS, Chamieh H, Nielsen KH, Oliveira CL, Pedersen JS, Séraphin B, Le Hir H, Andersen GR. </i> Science, 2006","date":"2025-11-24T14:52:52.055Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000019","term_name":"disorder to pre-molten globule","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"region_id":"DP02170r009","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61326"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P38919"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y5S9"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"8758","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"6102784"}],"statement":[{"text":"For the MLN51 fragment expressed for this study (residues 137 to 283), only residues 170 to 194 and 216 to 246 could be traced, and the fragment only contains limited secondary structure (Fig. 1A). Residues 216 to 246 contact patches C, D, and E in eIF4AIII domain 1 (Fig. 1C and fig. S2), explaining why the mutation of MLN51 Tyr240 and Gly241 disrupts formation of the EJC core (3). Residues 170 to 194 are located at the 5′ end of the bound RNA and contact eIF4AIII domain 2 (Fig. 1C).","type":"Article"},{"text":"The flexible non-conserved linker (10) between the two ordered MLN51 fragments allows the protein to remain associated with rather different conformations of eIF4AIII.","type":"Article"}],"cross_refs":[{"db":"PDB","id":"2HYI"}]},{"start":216,"end":246,"reference_id":"16931718","reference_source":"pmid","reference_html":"Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA. <i> Andersen CB, Ballut L, Johansen JS, Chamieh H, Nielsen KH, Oliveira CL, Pedersen JS, Séraphin B, Le Hir H, Andersen GR. </i> Science, 2006","date":"2025-11-24T14:51:00.169Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"PDB","id":"2HYI"}],"region_id":"DP02170r010","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61326"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P38919"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y5S9"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"8758","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"6102784"}],"statement":[{"text":"For the MLN51 fragment expressed for this study (residues 137 to 283), only residues 170 to 194 and 216 to 246 could be traced, and the fragment only contains limited secondary structure (Fig. 1A). Residues 216 to 246 contact patches C, D, and E in eIF4AIII domain 1 (Fig. 1C and fig. S2), explaining why the mutation of MLN51 Tyr240 and Gly241 disrupts formation of the EJC core (3). Residues 170 to 194 are located at the 5′ end of the bound RNA and contact eIF4AIII domain 2 (Fig. 1C).","type":"Article"},{"text":"The flexible non-conserved linker (10) between the two ordered MLN51 fragments allows the protein to remain associated with rather different conformations of eIF4AIII.","type":"Article"}]},{"start":170,"end":194,"reference_id":"16931718","reference_source":"pmid","reference_html":"Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA. <i> Andersen CB, Ballut L, Johansen JS, Chamieh H, Nielsen KH, Oliveira CL, Pedersen JS, Séraphin B, Le Hir H, Andersen GR. </i> Science, 2006","date":"2025-11-24T14:54:38.863Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"PDB","id":"2HYI"}],"region_id":"DP02170r011","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61326"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P38919"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y5S9"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"8758","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"6102784"}],"statement":[{"text":"For the MLN51 fragment expressed for this study (residues 137 to 283), only residues 170 to 194 and 216 to 246 could be traced, and the fragment only contains limited secondary structure (Fig. 1A).","type":"Article"},{"text":"Residues 170 to 194 are located at the 5′ end of the bound RNA and contact eIF4AIII domain 2 (Fig. 1C).","type":"Article"}]},{"start":216,"end":246,"reference_id":"16931718","reference_source":"pmid","reference_html":"Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA. <i> Andersen CB, Ballut L, Johansen JS, Chamieh H, Nielsen KH, Oliveira CL, Pedersen JS, Séraphin B, Le Hir H, Andersen GR. </i> Science, 2006","date":"2025-11-24T14:52:11.221Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"PDB","id":"2HYI"}],"region_id":"DP02170r012","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61326"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P38919"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y5S9"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"8758","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"6102784"}],"statement":[{"text":"or the MLN51 fragment expressed for this study (residues 137 to 283), only residues 170 to 194 and 216 to 246 could be traced, and the fragment only contains limited secondary structure (Fig. 1A). Residues 216 to 246 contact patches C, D, and E in eIF4AIII domain 1 (Fig. 1C and fig. S2), explaining why the mutation of MLN51 Tyr240 and Gly241 disrupts formation of the EJC core (3).","type":"Article"}]},{"start":1,"end":703,"reference_id":"16931718","reference_source":"pmid","reference_html":"Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA. <i> Andersen CB, Ballut L, Johansen JS, Chamieh H, Nielsen KH, Oliveira CL, Pedersen JS, Séraphin B, Le Hir H, Andersen GR. </i> Science, 2006","date":"2025-11-24T14:51:29.408Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0035145","term_name":"exon-exon junction complex","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"PDB","id":"2HYI"}],"ec_go":"EXP","region_id":"DP02170r013","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":"P38919"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":"P61326"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":"Q9Y5S9"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"8758","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"6102784"}],"statement":[{"text":"Here, we present the crystal structure of a tetrameric exon junction core complex containing the DEAD-box adenosine triphosphatase (ATPase) eukaryotic initiation factor 4AIII (eIF4AIII) bound to an ATP analog, MAGOH, Y14, a fragment of MLN51, and a polyuracil mRNA mimic.","type":"Abstract"},{"text":"To shed light on both the EJC core architecture and the molecular mechanism of DEAD-box proteins, we determined the crystal structure of a minimal reconstituted EJC core assembled on a poly(U) oligonucleotide mimicking the mRNA at 2.3 Å resolution (8) (table S1).","type":"Article"}],"term_comment":"","term_def":"\"A multi-subunit complex deposited by the spliceosome upstream of messenger RNA exon-exon junctions. The exon-exon junction complex provides a binding platform for factors involved in mRNA export and nonsense-mediated mRNA decay.\" [PMID:11532962, PMID:11743026]","term_is_obsolete":false,"term_not_annotate":false},{"start":137,"end":283,"reference_id":"16170325","reference_source":"pmid","reference_html":"The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity. <i> Ballut L, Marchadier B, Baguet A, Tomasetto C, Séraphin B, Le Hir H. </i> Nat Struct Mol Biol, 2005","date":"2025-11-24T15:09:28.101Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"construct_alterations":[{"term_id":"MI:0677","term_name":"tandem tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":" MAGOH-Y14ΔN, MLN51-S and full-length eIF4AIII were fused to a C-terminal His6 tag and in some cases to an N-terminal tandem affinity purification (TAP) tag."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P38919 ","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9Y5S9","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP02170r014","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"The 46-mer and 33-mer ssRNAs corresponded, respectively, to 5′-GGGAGGAGCTCTTCGAGCTTGCTCATGGTGGTGGATTGTAATTGTA-3′ and 5′-GGAGC(UC)14-3′."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"6102784"}],"statement":[{"text":"MLN51-S corresponds to a short region of MLN51 (residues 137–283 of a total of 703 residues). We tested whether a similar complex can be assembled with the N-terminal half (TAP-MLN51-Nt, 1–351), the C-terminal half (TAP-MLN51-Ct, 352–703) or the full-length MLN51 protein (TAP-MLN51-FL, 1–703). We separately mixed TAP-MLN51-S, TAP-MLN51-Nt, TAP-MLN51-Ct and TAP-MLN51-FL with eIF4AIII and MAGOH-Y14ΔN in the presence of AMP-PNP and ssRNA as in our previous assays. TAP-MLN51-S, TAP-MLN51-Nt and TAP-MLN51-FL, which contain the SELOR domain, coprecipitated eIF4AIII and MAGOH-Y14ΔN with the same efficiency.","type":"Results"},{"text":"When TAP-MLN51-S was used as bait, neither eIF4AIII nor MAGOH-Y14ΔN were coprecipitated, indicating that MLN51-S does not stably interact with eIF4AIII or MAGOH-Y14ΔN individually (Fig. 1a, lanes 2 and 6). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":137,"end":283,"reference_id":"16170325","reference_source":"pmid","reference_html":"The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity. <i> Ballut L, Marchadier B, Baguet A, Tomasetto C, Séraphin B, Le Hir H. </i> Nat Struct Mol Biol, 2005","date":"2025-11-24T15:20:05.594Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003727","term_name":"single-stranded RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001170","ec_ontology":"ECO","ec_name":"cross-linking evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"construct_alterations":[{"term_id":"MI:0677","term_name":"tandem tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":" MAGOH-Y14ΔN, MLN51-S and full-length eIF4AIII were fused to a C-terminal His6 tag and in some cases to an N-terminal tandem affinity purification (TAP) tag."}]}],"ec_go":"IPI","region_id":"DP02170r015","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"The 46-mer and 33-mer ssRNAs corresponded, respectively, to 5′-GGGAGGAGCTCTTCGAGCTTGCTCATGGTGGTGGATTGTAATTGTA-3′ and 5′-GGAGC(UC)14-3′."}]}],"statement":[{"text":"eIF4AIII and MLN51-S crosslinked to the RNA only in the presence of AMP-PNP, and no cross-linking was detected when the same mixture was not UV irradiated (Fig. 5, lanes 4–6). Thus, RNA cross-linking depends on complex assembly. This was confirmed by analyzing TAP-eIF4AIII and TAP-MLN51-S, as corresponding cross-links were shifted in the presence of the tag (Fig. 5, lanes 7–12). Therefore, both eIF4AIII and MLN51-S directly bind ssRNA in the complex.","type":"Results"}],"term_comment":"","term_def":"\"Binding to single-stranded RNA.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":137,"end":283,"reference_id":"16170325","reference_source":"pmid","reference_html":"The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity. <i> Ballut L, Marchadier B, Baguet A, Tomasetto C, Séraphin B, Le Hir H. </i> Nat Struct Mol Biol, 2005","date":"2025-11-24T15:27:06.739Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1902280","term_name":"regulation of RNA helicase activity","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"construct_alterations":[{"term_id":"MI:0677","term_name":"tandem tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":" MAGOH-Y14ΔN, MLN51-S and full-length eIF4AIII were fused to a C-terminal His6 tag and in some cases to an N-terminal tandem affinity purification (TAP) tag."}]}],"ec_go":"IDA","region_id":"DP02170r016","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"The 46-mer and 33-mer ssRNAs corresponded, respectively, to 5′-GGGAGGAGCTCTTCGAGCTTGCTCATGGTGGTGGATTGTAATTGTA-3′ and 5′-GGAGC(UC)14-3′."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P38919"}],"statement":[{"text":"We measured eIF4AIII ATPase activity with or without its binding partners. TAP-tagged proteins purified successively on nickel and calmodulin affinity columns were used for this assay to reduce background NTPase activity originating from contaminating E. coli NTPases31. As expected, TAP-eIF4AIII had weak ATPase activity (Fig. 7b, top). Addition of an equimolar amount of TAP-MLN51-S increased this activity three-fold, correlating with the ability of MLN51-S to enhance binding of eIF4AIII to RNA.","type":"Results"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of ATP-dependent RNA helicase activity.\" [GOC:rb, GOC:TermGenie, PMID:23721653]","term_is_obsolete":false,"term_not_annotate":false},{"start":137,"end":283,"reference_id":"16170325","reference_source":"pmid","reference_html":"The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity. <i> Ballut L, Marchadier B, Baguet A, Tomasetto C, Séraphin B, Le Hir H. </i> Nat Struct Mol Biol, 2005","date":"2025-11-24T15:35:28.221Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005654","term_name":"nucleoplasm","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":". To test this, plasmids encoding WT or mutant MLN51-S fused to an N-terminal EYFP peptide were transiently transfected into HeLa cells."}]}],"ec_go":"IDA","region_id":"DP02170r017","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"statement":[{"text":"Confocal microscopic analysis indicated that MLN51-S WT was mainly restricted to the speckles' periphery (stained with antibodies raised against the splicing factor 9G8 in Fig. 8a–d).","type":"Results"}],"term_comment":"","term_def":"\"That part of the nuclear content other than the chromosomes or the nucleolus.\" [GOC:ma, ISBN:0124325653]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_O15234","date":"2018-08-28T13:03:25.000Z","acc":"O15234","name":"Protein CASC3","length":703,"organism":"Homo sapiens","dataset":["Stress response proteins"],"UniParc":"UPI000014C6E6","genes":[{"name":{"value":"CASC3"},"synonyms":[{"value":"MLN51","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12080473","url":"http://www.ncbi.nlm.nih.gov/pubmed/12080473","alternativeUrl":"https://europepmc.org/abstract/MED/12080473"}}]}]}],"alphafold_very_low_content":0.534850640113798,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":215,"type":"D"},{"start":216,"end":246,"type":"T"},{"start":247,"end":703,"type":"D"}],"Structural state":[{"start":1,"end":703,"type":"D"}],"Disorder function":[{"start":195,"end":246,"type":"F"}],"Molecular function":[{"start":137,"end":283,"type":"F"}],"Structural transition":[{"start":216,"end":246,"type":"T"}],"Cellular component":[{"start":1,"end":703,"type":"F"}],"Biological process":[{"start":137,"end":283,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":105,"end":174},{"id":"PF12220","name":"U1 small nuclear ribonucleoprotein of 70kDa MW N terminal","start":3,"end":94}],"gene3D":[{"start":90,"end":215,"id":"3.30.70.330","name":"3.30.70.330"}]},"uniref50":"UniRef50_P08621","sequence":"MTQFLPPNLLALFAPRDPIPYLPPLEKLPHEKHHNQPYCGIAPYIREFEDPRDAPPPTRAETREERMERKRREKIERRQQEVETELKMWDPHNDPNAQGDAFKTLFVARVNYDTTESKLRREFEVYGPIKRIHMVYSKRSGKPRGYAFIEYEHERDMHSAYKHADGKKIDGRRVLVDVERGRTVKGWRPRRLGGGLGGTRRGGADVNIRHSGRDDTSRYDERPGPSPLPHRDRDRDRERERRERSRERDKERERRRSRSRDRRRRSRSRDKEERRRSRERSKDKDRDRKRRSSRSRERARRERERKEELRGGGGDMAEPSEAGDAPPDDGPPGELGPDGPDGPEEKGRDRDRERRRSHRSERERRRDRDRDRDRDREHKRGERGSERGRDEARGGGGGQDNGLEGLGNDSRDMYMESEGGDGYLAPENGYLMEAAPE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P08621","disprot_id":"DP02171","ncbi_taxon_id":9606,"regions_counter":15,"creator":"eficho","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":33,"region_id":"DP02171r002","reference_id":"21113136","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The present model of the chymotrypsin-trimmed U1 snRNP (hereafter referred to as U1 snRNP) includes residues 1–164 of native U1 snRNA, a region covering the RRM and an N-terminal extension of the U1-70K protein (residues 34–183 out of 437 amino acids total), the N-terminal RRM of the U1-A protein (residues 1–114 out of 282 amino acids total) and the Sm folds with varying terminal appendices of all seven Sm proteins but lacks U1-C (see also Supplementary Figure S3 and Supplementary Table SI for protein residues included in the model).","type":"Results"},{"text":"In our structure, the electron density for the U1-70K N-terminal extension fades out beyond the centre of the Sm ring, indicating that the very N terminus of U1-70K is degraded or disordered.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Functional organization of the Sm core in the crystal structure of human U1 snRNP. <i> Weber G, Trowitzsch S, Kastner B, Lührmann R, Wahl MC. </i> EMBO J, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3PGW"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":33,"region_id":"DP02171r003","reference_id":"21113136","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The present model of the chymotrypsin-trimmed U1 snRNP (hereafter referred to as U1 snRNP) includes residues 1–164 of native U1 snRNA, a region covering the RRM and an N-terminal extension of the U1-70K protein (residues 34–183 out of 437 amino acids total), the N-terminal RRM of the U1-A protein (residues 1–114 out of 282 amino acids total) and the Sm folds with varying terminal appendices of all seven Sm proteins but lacks U1-C (see also Supplementary Figure S3 and Supplementary Table SI for protein residues included in the model).","type":"Results"},{"text":"In our structure, the electron density for the U1-70K N-terminal extension fades out beyond the centre of the Sm ring, indicating that the very N terminus of U1-70K is degraded or disordered.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cleavage assay evidence used in manual assertion","version":3,"reference_html":"Functional organization of the Sm core in the crystal structure of human U1 snRNP. <i> Weber G, Trowitzsch S, Kastner B, Lührmann R, Wahl MC. </i> EMBO J, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":437,"region_id":"DP02171r004","reference_id":"21113136","start":184,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The present model of the chymotrypsin-trimmed U1 snRNP (hereafter referred to as U1 snRNP) includes residues 1–164 of native U1 snRNA, a region covering the RRM and an N-terminal extension of the U1-70K protein (residues 34–183 out of 437 amino acids total), the N-terminal RRM of the U1-A protein (residues 1–114 out of 282 amino acids total) and the Sm folds with varying terminal appendices of all seven Sm proteins but lacks U1-C (see also Supplementary Figure S3 and Supplementary Table SI for protein residues included in the model).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cleavage assay evidence used in manual assertion","version":3,"reference_html":"Functional organization of the Sm core in the crystal structure of human U1 snRNP. <i> Weber G, Trowitzsch S, Kastner B, Lührmann R, Wahl MC. </i> EMBO J, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":437,"region_id":"DP02171r005","reference_id":"21113136","start":184,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The present model of the chymotrypsin-trimmed U1 snRNP (hereafter referred to as U1 snRNP) includes residues 1–164 of native U1 snRNA, a region covering the RRM and an N-terminal extension of the U1-70K protein (residues 34–183 out of 437 amino acids total), the N-terminal RRM of the U1-A protein (residues 1–114 out of 282 amino acids total) and the Sm folds with varying terminal appendices of all seven Sm proteins but lacks U1-C (see also Supplementary Figure S3 and Supplementary Table SI for protein residues included in the model).","type":"Results"},{"text":"Analysis of washed crystals revealed that a C-terminal RS-like region of U1-70K, a C-terminal RNA recognition motif (RRM) of U1-A, the U1-C protein as well as a C-terminal RG-repeat/Pro-rich region of Sm protein B were removed during the crystallization, while the RNA remained intact (Supplementary Figure S1).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Functional organization of the Sm core in the crystal structure of human U1 snRNP. <i> Weber G, Trowitzsch S, Kastner B, Lührmann R, Wahl MC. </i> EMBO J, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3PGW"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02171r006","ec_ontology":"ECO","end":437,"term_id":"GO:0005515","start":184,"version":4,"statement":[{"text":"The present model of the chymotrypsin-trimmed U1 snRNP (hereafter referred to as U1 snRNP) includes residues 1–164 of native U1 snRNA, a region covering the RRM and an N-terminal extension of the U1-70K protein (residues 34–183 out of 437 amino acids total), the N-terminal RRM of the U1-A protein (residues 1–114 out of 282 amino acids total) and the Sm folds with varying terminal appendices of all seven Sm proteins but lacks U1-C (see also Supplementary Figure S3 and Supplementary Table SI for protein residues included in the model).","type":"Results"},{"text":"Analysis of washed crystals revealed that a C-terminal RS-like region of U1-70K, a C-terminal RNA recognition motif (RRM) of U1-A, the U1-C protein as well as a C-terminal RG-repeat/Pro-rich region of Sm protein B were removed during the crystallization, while the RNA remained intact (Supplementary Figure S1).","type":"Results"},{"text":"For example, the alternative splicing factor ASF/SF2 binds to the RS-like domain of U1-70K (Xiao and Manley, 1997).","type":"Discussion"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q07955","partner_end":null}],"term_name":"protein binding","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"21113136","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3PGW"}],"term_namespace":"Molecular function","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Functional organization of the Sm core in the crystal structure of human U1 snRNP. <i> Weber G, Trowitzsch S, Kastner B, Lührmann R, Wahl MC. </i> EMBO J, 2010","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":277,"end":281,"reference_id":"39023093","reference_source":"pmid","reference_html":"The U1-70K and SRSF1 interaction is modulated by phosphorylation during the early stages of spliceosome assembly. <i> Paul T, Zhang P, Zhang Z, Fargason T, De Silva NIU, Powell E, Ekpenyong E, Jamal S, Yu Y, Prevelige P, Lu R, Zhang J. </i> Protein Sci, 2024","date":"2025-03-20T14:09:39.245Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP02171r007","statement":[{"text":"We found that BAD1 was phosphorylated by SRPK1 in vitro, and the binding affinity of phosphorylated BAD1 to SRSF1, with a K d of 700nM, was 60‐fold weaker than that of the nonphosphorylated protein. Using mass spectrometry, we found that SRPK1 adds 8 to 9 phosphate groups on BAD1, and further identified the phosphorylation sites (Figure 4e). We identified seven unambiguous phosphorylation sites (Figure 4e). Two of three serine residues in the RSSRS motif (residues 291–295) were phosphorylated.","type":"Results"},{"text":"Figure 4 shows the phosphorylated serine residues are at position 245, 257, 259, 266, 268, 277, 281, and the serine residues in the RSSRS motif at 292, 293 and 295.","type":"Curator statement"}]},{"start":265,"end":269,"reference_id":"39023093","reference_source":"pmid","reference_html":"The U1-70K and SRSF1 interaction is modulated by phosphorylation during the early stages of spliceosome assembly. <i> Paul T, Zhang P, Zhang Z, Fargason T, De Silva NIU, Powell E, Ekpenyong E, Jamal S, Yu Y, Prevelige P, Lu R, Zhang J. </i> Protein Sci, 2024","date":"2025-03-20T14:09:46.049Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP02171r008","statement":[{"text":"We found that BAD1 was phosphorylated by SRPK1 in vitro, and the binding affinity of phosphorylated BAD1 to SRSF1, with a K d of 700nM, was 60‐fold weaker than that of the nonphosphorylated protein. Using mass spectrometry, we found that SRPK1 adds 8 to 9 phosphate groups on BAD1, and further identified the phosphorylation sites (Figure 4e). We identified seven unambiguous phosphorylation sites (Figure 4e). Two of three serine residues in the RSSRS motif (residues 291–295) were phosphorylated.","type":"Results"},{"text":"Figure 4 shows the phosphorylated serine residues are at position 245, 257, 259, 266, 268, 277, 281, and the serine residues in the RSSRS motif at 292, 293 and 295.","type":"Curator statement"}]},{"start":255,"end":259,"reference_id":"39023093","reference_source":"pmid","reference_html":"The U1-70K and SRSF1 interaction is modulated by phosphorylation during the early stages of spliceosome assembly. <i> Paul T, Zhang P, Zhang Z, Fargason T, De Silva NIU, Powell E, Ekpenyong E, Jamal S, Yu Y, Prevelige P, Lu R, Zhang J. </i> Protein Sci, 2024","date":"2025-03-20T14:09:54.249Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP02171r009","statement":[{"text":"We found that BAD1 was phosphorylated by SRPK1 in vitro, and the binding affinity of phosphorylated BAD1 to SRSF1, with a K d of 700nM, was 60‐fold weaker than that of the nonphosphorylated protein. Using mass spectrometry, we found that SRPK1 adds 8 to 9 phosphate groups on BAD1, and further identified the phosphorylation sites (Figure 4e). We identified seven unambiguous phosphorylation sites (Figure 4e). Two of three serine residues in the RSSRS motif (residues 291–295) were phosphorylated.","type":"Results"},{"text":"Figure 4 shows the phosphorylated serine residues are at position 245, 257, 259, 266, 268, 277, 281, and the serine residues in the RSSRS motif at 292, 293 and 295.","type":"Curator statement"}]},{"start":243,"end":247,"reference_id":"39023093","reference_source":"pmid","reference_html":"The U1-70K and SRSF1 interaction is modulated by phosphorylation during the early stages of spliceosome assembly. <i> Paul T, Zhang P, Zhang Z, Fargason T, De Silva NIU, Powell E, Ekpenyong E, Jamal S, Yu Y, Prevelige P, Lu R, Zhang J. </i> Protein Sci, 2024","date":"2025-03-20T14:10:04.618Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP02171r010","statement":[{"text":"We found that BAD1 was phosphorylated by SRPK1 in vitro, and the binding affinity of phosphorylated BAD1 to SRSF1, with a K d of 700nM, was 60‐fold weaker than that of the nonphosphorylated protein. Using mass spectrometry, we found that SRPK1 adds 8 to 9 phosphate groups on BAD1, and further identified the phosphorylation sites (Figure 4e). We identified seven unambiguous phosphorylation sites (Figure 4e). Two of three serine residues in the RSSRS motif (residues 291–295) were phosphorylated.","type":"Results"},{"text":"Figure 4 shows the phosphorylated serine residues are at position 245, 257, 259, 266, 268, 277, 281, and the serine residues in the RSSRS motif at 292, 293 and 295.","type":"Curator statement"}]},{"start":291,"end":295,"reference_id":"39023093","reference_source":"pmid","reference_html":"The U1-70K and SRSF1 interaction is modulated by phosphorylation during the early stages of spliceosome assembly. <i> Paul T, Zhang P, Zhang Z, Fargason T, De Silva NIU, Powell E, Ekpenyong E, Jamal S, Yu Y, Prevelige P, Lu R, Zhang J. </i> Protein Sci, 2024","date":"2025-03-20T14:10:12.629Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP02171r011","statement":[{"text":"We found that BAD1 was phosphorylated by SRPK1 in vitro, and the binding affinity of phosphorylated BAD1 to SRSF1, with a K d of 700nM, was 60‐fold weaker than that of the nonphosphorylated protein. Using mass spectrometry, we found that SRPK1 adds 8 to 9 phosphate groups on BAD1, and further identified the phosphorylation sites (Figure 4e). We identified seven unambiguous phosphorylation sites (Figure 4e). Two of three serine residues in the RSSRS motif (residues 291–295) were phosphorylated.","type":"Results"},{"text":"Figure 4 shows the phosphorylated serine residues are at position 245, 257, 259, 266, 268, 277, 281, and the serine residues in the RSSRS motif at 292, 293 and 295.","type":"Curator statement"}]},{"start":230,"end":306,"reference_id":"39023093","reference_source":"pmid","reference_html":"The U1-70K and SRSF1 interaction is modulated by phosphorylation during the early stages of spliceosome assembly. <i> Paul T, Zhang P, Zhang Z, Fargason T, De Silva NIU, Powell E, Ekpenyong E, Jamal S, Yu Y, Prevelige P, Lu R, Zhang J. </i> Protein Sci, 2024","date":"2025-06-17T09:59:59.561Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006277","ec_ontology":"ECO","ec_name":"fluorescence polarization evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q07955","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02171r013","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":200,"db":"ChEBI","id":"157844","entry_name":"Glu-Arg"}],"statement":[{"text":"In addition, BAD1 alone interacts with SRSF1 with a binding affinity comparable with full‐length U1‐70K, whereas BAD2 or RRM alone cannot.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-17T16:00:36.262Z"}},{"start":230,"end":306,"reference_id":"39023093","reference_source":"pmid","reference_html":"The U1-70K and SRSF1 interaction is modulated by phosphorylation during the early stages of spliceosome assembly. <i> Paul T, Zhang P, Zhang Z, Fargason T, De Silva NIU, Powell E, Ekpenyong E, Jamal S, Yu Y, Prevelige P, Lu R, Zhang J. </i> Protein Sci, 2024","date":"2025-06-08T20:04:29.150Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q07955","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02171r014","statement":[{"text":"To confirm our FP results and to eliminate possible interference of Arg/Glu in protein interaction, we further performed pull‐down assays in a buffer that has no Arg/Glu using purified His‐SUMO‐tagged U1‐70K constructs and phosphorylated SRSF1 obtained from E. coli (Figure 2). Our pull‐down assays confirmed the interaction between U1‐70K and SRSF1 (Figure 2), in consistent with FP assays shown in Figure 1. ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.His229_Lys306del","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T21:53:04.289Z"}},{"start":230,"end":306,"reference_id":"39023093","reference_source":"pmid","reference_html":"The U1-70K and SRSF1 interaction is modulated by phosphorylation during the early stages of spliceosome assembly. <i> Paul T, Zhang P, Zhang Z, Fargason T, De Silva NIU, Powell E, Ekpenyong E, Jamal S, Yu Y, Prevelige P, Lu R, Zhang J. </i> Protein Sci, 2024","date":"2025-06-16T22:06:12.932Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP02171r015","statement":[{"text":"Our circular dichroism (CD) spectra show that BAD1 contains both α‐helical structure and random coil, and hyper phosphorylated RS (pi‐RS) is mainly disordered (Figure 5a, dotted lines).","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_P08621","date":"2018-08-28T13:26:17.000Z","acc":"P08621","name":"U1 small nuclear ribonucleoprotein 70 kDa","length":437,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI0000163B53","genes":[{"name":{"value":"SNRNP70"},"synonyms":[{"value":"RNPU1Z"},{"value":"RPU1"},{"value":"SNRP70"},{"value":"U1AP1"}]}],"alphafold_very_low_content":0.2608695652173913,"disorder_content":0.6567505720823799,"disprot_consensus":{"full":[{"start":1,"end":33,"type":"D"},{"start":184,"end":437,"type":"D"}],"Structural state":[{"start":1,"end":33,"type":"D"},{"start":184,"end":437,"type":"D"}],"Molecular function":[{"start":184,"end":437,"type":"F"}],"Disorder function":[{"start":243,"end":247,"type":"F"},{"start":255,"end":259,"type":"F"},{"start":265,"end":269,"type":"F"},{"start":277,"end":281,"type":"F"},{"start":291,"end":295,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00085","name":"Thioredoxin","start":33,"end":137},{"id":"PF13848","name":"Thioredoxin-like domain","start":167,"end":350}],"gene3D":[{"start":244,"end":406,"id":"3.40.30.10","name":"Glutaredoxin"},{"start":143,"end":243,"id":"3.40.30.10","name":"Glutaredoxin"},{"start":25,"end":142,"id":"3.40.30.10","name":"Glutaredoxin"}]},"uniref50":"UniRef50_Q9BS26","sequence":"MHPAVFLSLPDLRCSLLLLVTWVFTPVTTEITSLDTENIDEILNNADVALVNFYADWCRFSQMLHPIFEEASDVIKEEFPNENQVVFARVDCDQHSDIAQRYRISKYPTLKLFRNGMMMKREYRGQRSVKALADYIRQQKSDPIQEIRDLAEITTLDRSKRNIIGYFEQKDSDNYRVFERVANILHDDCAFLSAFGDVSKPERYSGDNIIYKPPGHSAPDMVYLGAMTNFDVTYNWIQDKCVPLVREITFENGEELTEEGLPFLILFHMKEDTESLEIFQNEVARQLISEKGTINFLHADCDKFRHPLLHIQKTPADCPVIAIDSFRHMYVFGDFKDVLIPGKLKQFVFDLHSGKLHREFHHGPDPTDTAPGEQAQDVASSPPESSFQKLAPSEYRYTLLRDRDEL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9BS26","disprot_id":"DP02173","ncbi_taxon_id":9606,"regions_counter":5,"creator":"sventura","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":379,"region_id":"DP02173r001","released":"2025_12","ec_id":"ECO:0006220","reference_html":"Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy-terminal tail. <i> Wang L, Wang L, Vavassori S, Li S, Ke H, Anelli T, Degano M, Ronzoni R, Sitia R, Sun F, Wang CC. </i> EMBO Rep, 2008","statement":[{"text":"The C-tail (residues 326–377) is flexible and mainly composed of random coils in addition to one short strand β16 (residues 369–370), which is antiparallel to β3 in domain a, and two short 310 helices: η4 (residues 326–328) and η5 (residues 358–360) filling the cavity lined by helices α7 and α9 in domain b′ (Fig 1A).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":361,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2025-11-19T19:26:08.737Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2R2J"}],"reference_id":"18552768","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":63,"end":63,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":117,"end":117,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":118,"end":118,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":119,"end":119,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":221,"end":221,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":227,"end":227,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":269,"end":269,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":329,"end":329,"position":"Specific residue"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":406,"region_id":"DP02173r002","released":"2025_12","ec_id":"ECO:0006220","reference_html":"Crystal Structure of the ERp44-Peroxiredoxin 4 Complex Reveals the Molecular Mechanisms of Thiol-Mediated Protein Retention. <i> Yang K, Li DF, Wang X, Liang J, Sitia R, Wang CC, Wang X. </i> Structure, 2016","statement":[{"text":"Moreover, the flexible C-tail (residues 351–372) becomes disordered with its electron density untraceable. The movements of the C-tail and the b′ domain disrupt the interactions among domains a, b′ and the C-tail, favoring an open conformation, thus making the inner space of ERp44 more accessible to Prx4.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":361,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2025-11-19T19:00:08.262Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5HQP"}],"reference_id":"27642162","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q13162"}]},{"start":380,"end":401,"reference_id":"27642162","reference_source":"pmid","reference_html":"Crystal Structure of the ERp44-Peroxiredoxin 4 Complex Reveals the Molecular Mechanisms of Thiol-Mediated Protein Retention. <i> Yang K, Li DF, Wang X, Liang J, Sitia R, Wang CC, Wang X. </i> Structure, 2016","date":"2025-11-19T19:16:51.856Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0007013","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"PDB","id":"5HQP"}],"region_id":"DP02173r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q13162"}],"statement":[{"text":"The intact ERp44 molecule (chain C, Figure 3) in the complex was taken for further structural comparison with free ERp44 (Figure 4), which clearly shows that the C-tail and even domain b′ in free ERp44 block the access of Prx4 by steric hindrance. When bound to Prx4, the three thioredoxin domains remain in the typical clover-like structure but with domain b′ rotated ∼40° anticlockwise relative to domain b. Moreover, the flexible C-tail (residues 351–372) becomes disordered with its electron density untraceable. The movements of the C-tail and the b′ domain disrupt the interactions among domains a, b′ and the C-tail, favoring an open conformation, thus making the inner space of ERp44 more accessible to Prx4.","type":"Results"},{"text":" In the complex, the b′ domain in chain C rotates ∼40° and the visible part of the C-tail (residues 351–372) in free ERp44 colored in green becomes untraceable.","type":"Figure"}]},{"start":380,"end":401,"reference_id":"27642162","reference_source":"pmid","reference_html":"Crystal Structure of the ERp44-Peroxiredoxin 4 Complex Reveals the Molecular Mechanisms of Thiol-Mediated Protein Retention. <i> Yang K, Li DF, Wang X, Liang J, Sitia R, Wang CC, Wang X. </i> Structure, 2016","date":"2025-11-19T19:22:04.160Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000057","term_name":"self-regulatory activity","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007013","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"PDB","id":"5HQP"}],"region_id":"DP02173r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q13162"}],"statement":[{"text":"The intact ERp44 molecule (chain C, Figure 3) in the complex was taken for further structural comparison with free ERp44 (Figure 4), which clearly shows that the C-tail and even domain b′ in free ERp44 block the access of Prx4 by steric hindrance. When bound to Prx4, the three thioredoxin domains remain in the typical clover-like structure but with domain b′ rotated ∼40° anticlockwise relative to domain b. Moreover, the flexible C-tail (residues 351–372) becomes disordered with its electron density untraceable. The movements of the C-tail and the b′ domain disrupt the interactions among domains a, b′ and the C-tail, favoring an open conformation, thus making the inner space of ERp44 more accessible to Prx4.","type":"Results"},{"text":"The first structure we solved portrayed ERp44 in its inactive state and revealed that C-tail movements regulate substrate binding and release (Wang et al., 2008). ","type":"Discussion"}]}],"released":"2018_11","uniref100":"UniRef100_Q9BS26","date":"2018-08-28T13:48:17.000Z","acc":"Q9BS26","name":"Endoplasmic reticulum resident protein 44","length":406,"organism":"Homo sapiens","dataset":["Stress response proteins"],"UniParc":"UPI0000072130","genes":[{"name":{"value":"ERP44"},"synonyms":[{"value":"KIAA0573"},{"value":"TXNDC4"}],"orfNames":[{"value":"UNQ532/PRO1075"}]}],"alphafold_very_low_content":0.059113300492610835,"disorder_content":0.11330049261083744,"disprot_consensus":{"full":[{"start":361,"end":379,"type":"D"},{"start":380,"end":401,"type":"T"},{"start":402,"end":406,"type":"D"}],"Structural state":[{"start":361,"end":406,"type":"D"}],"Structural transition":[{"start":380,"end":401,"type":"T"}],"Disorder function":[{"start":380,"end":401,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01022","name":"Bacterial regulatory protein, arsR family","start":31,"end":75}],"gene3D":[{"start":14,"end":108,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}]},"uniref50":"UniRef50_P52695","sequence":"MPYLKGAPMNLQEMEKNSAKAVVLLKAMANERRLQILCMLLDNELSVGELSSRLELSQSALSQHLAWLRRDGLVNTRKEAQTVFYTLSSTEVKAMIELLHRLYCQANQ","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Vibrionales","Vibrionaceae","Vibrio"],"uniref90":"UniRef90_P52695","disprot_id":"DP02188","ncbi_taxon_id":243277,"regions_counter":2,"creator":"thorvath","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":10,"region_id":"DP02188r001","released":"2025_06","ec_id":"ECO:0006220","reference_html":"Crystal structure of HlyU, the hemolysin gene transcription activator, from Vibrio cholerae N16961 and functional implications. <i> Mukherjee D, Datta AB, Chakrabarti P. </i> Biochim Biophys Acta, 2014","statement":[{"text":"Three residues could not be located at the C-terminal end and varying regions (10–13 residues) are found to be disordered at the N-termini of different subunits indicating the flexibility of these ends.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"tcordero","start":1,"term_ontology":"IDPO","curator_name":"Trinidad Cordero","reference_id":"25450504","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2025-02-05T08:13:24.341Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4OOI"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","curator_orcid":"0000-0003-4991-7170","conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":20,"statements":[{"type":"Methods","text":"Suitable crystals (crystal I) were obtained by hanging-drop, vapor-diffusion method at 20 °C, in about 7–10 days using 0.05 M potassium phosphate monobasic and 20% w/v PEG 8000 as precipitant. "}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-05T13:18:48.127Z"}},{"start":1,"end":10,"reference_id":"25450504","reference_source":"pmid","reference_html":"Crystal structure of HlyU, the hemolysin gene transcription activator, from Vibrio cholerae N16961 and functional implications. <i> Mukherjee D, Datta AB, Chakrabarti P. </i> Biochim Biophys Acta, 2014","date":"2025-01-31T17:30:39.328Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"4OOI"}],"region_id":"DP02188r002","statement":[{"text":"While only 4 residues are missing in the α1 helix in HlyU_Vv, the N-terminus of HlyU_Vc appears to be more flexible (10–13 residues could not be traced).","type":"Results"}]}],"released":"2025_06","uniref100":"UniRef100_P52695","date":"2018-08-28T13:53:19.000Z","acc":"P52695","name":"Transcriptional activator HlyU","length":108,"organism":"Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)","dataset":["Bacterial virulence-related proteins"],"UniParc":"UPI000012C966","genes":[{"name":{"value":"hlyU"},"olnNames":[{"value":"VC_0678"}]}],"alphafold_very_low_content":0.037037037037037035,"disorder_content":0.09259259259259259,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"}],"Disorder function":[{"start":1,"end":10,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00179","name":"Ubiquitin-conjugating enzyme","start":51,"end":187}],"gene3D":[{"start":21,"end":193,"id":"3.10.110.10","name":"Ubiquitin Conjugating Enzyme"}]},"uniref50":"UniRef50_P51965","sequence":"MSDDDSRASTSSSSSSSSNQQTEKETNTPKKKESKVSMSKNSKLLSTSAKRIQKELADITLDPPPNCSAGPKGDNIYEWRSTILGPPGSVYEGGVFFLDITFTPEYPFKPPKVTFRTRIYHCNINSQGVICLDILKDNWSPALTISKVLLSICSLLTDCNPADPLVGSIATQYMTNRAEHDRMARQWTKRYAT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P51965","disprot_id":"DP02191","ncbi_taxon_id":9606,"regions_counter":3,"creator":"epapa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":40,"region_id":"DP02191r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The N-terminal extension of UBE2E ubiquitin-conjugating enzymes limits chain assembly. <i> Schumacher FR, Wilson G, Day CL. </i> J Mol Biol, 2013","statement":[{"text":"In the\ncrystal structure of UBE2E1, most of the N-terminal\nresidues are missing, suggesting that they were\nflexible (Fig. 2a) and analysis of the sequence using\nIUPred indicates that they have features expected\nfor disordered regions.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"epapa","start":1,"term_ontology":"IDPO","curator_name":"Elena Papaleo","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23871895","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":40,"region_id":"DP02191r002","released":"2022_03","ec_id":"ECO:0007691","reference_html":"The N-terminal extension of UBE2E ubiquitin-conjugating enzymes limits chain assembly. <i> Schumacher FR, Wilson G, Day CL. </i> J Mol Biol, 2013","statement":[{"text":"In support of this, the N-terminal residues of UBE2E1 were sensitive to proteolytic cleavage.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"epapa","start":1,"term_ontology":"IDPO","curator_name":"Elena Papaleo","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23871895","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":40,"region_id":"DP02191r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"The N-terminal extension of UBE2E ubiquitin-conjugating enzymes limits chain assembly. <i> Schumacher FR, Wilson G, Day CL. </i> J Mol Biol, 2013","statement":[{"text":"and circular dichroism (CD) spectroscopy (Fig. 2e)\nshowed that the mean residue ellipticity for E2E1full\nis decreased relative to E2E1core. Notably, the mean\nresidue ellipticity at 208 and 222 nM is reduced by\n~ 20% in the E2E1full spectra, consistent with the\nabsence of regions of α-helical and β-sheet structure\nin the 40 N-terminal residues.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"epapa","start":1,"term_ontology":"IDPO","curator_name":"Elena Papaleo","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23871895","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P51965","date":"2018-08-28T14:15:54.000Z","acc":"P51965","name":"Ubiquitin-conjugating enzyme E2 E1","length":193,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000137964","genes":[{"name":{"value":"UBE2E1"},"synonyms":[{"value":"UBCH6"}]}],"alphafold_very_low_content":0.11917098445595854,"disorder_content":0.20725388601036268,"disprot_consensus":{"full":[{"start":1,"end":40,"type":"D"}],"Structural state":[{"start":1,"end":40,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":204,"end":391},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":427,"end":536}],"gene3D":[{"start":405,"end":580,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":167,"end":404,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_O00571","sequence":"MSHVAVENALGLDQQFAGLDLNSSDNQSGGSTASKGRYIPPHLRNREATKGFYDKDSSGWSSSKDKDAYSSFGSRSDSRGKSSFFSDRGSGSRGRFDDRGRSDYDGIGSRGDRSGFGKFERGGNSRWCDKSDEDDWSKPLPPSERLEQELFSGGNTGINFEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGEALRAMKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEESDKRSFLLDLLNATGKDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLLVEAKQEVPSWLENMAYEHHYKGSSRGRSKSSRFSGGFGARDYRQSSGASSSSFSSSRASSSRSGGGGHGSSRGFGGGGYGGFYNSDGYGGNYNSQGVDWWGN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O00571","disprot_id":"DP02192","ncbi_taxon_id":9606,"regions_counter":1,"creator":"sventura","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":167,"region_id":"DP02192r001","released":"2022_06","ec_id":"ECO:0006204","reference_html":"Structural basis for targeting of human RNA helicase DDX3 by poxvirus protein K7. <i> Oda S, Schröder M, Khan AR. </i> Structure, 2009","statement":[{"text":"The N-terminal region of DDX3 (1–167) was presumed to be unstructured, and a circular dichroism (CD) analysis supports this prediction.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-27T20:37:40.339Z","reference_source":"pmid","term_name":"disorder","reference_id":"19913487","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:59:17.188Z"}}],"released":"2018_11","uniref100":"UniRef100_O00571","date":"2018-08-28T14:17:57.000Z","acc":"O00571","name":"ATP-dependent RNA helicase DDX3X","length":662,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins","Condensates-related proteins"],"UniParc":"UPI000013CB6D","genes":[{"name":{"value":"DDX3X"},"synonyms":[{"value":"DBX","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15294876","url":"http://www.ncbi.nlm.nih.gov/pubmed/15294876","alternativeUrl":"https://europepmc.org/abstract/MED/15294876"}}]},{"value":"DDX3"}]}],"alphafold_very_low_content":0.29607250755287007,"disorder_content":0.25226586102719034,"disprot_consensus":{"full":[{"start":1,"end":167,"type":"D"}],"Structural state":[{"start":1,"end":167,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00179","name":"Ubiquitin-conjugating enzyme","start":6,"end":143},{"id":"PF09288","name":"Fungal ubiquitin-associated domain","start":161,"end":215}],"gene3D":[{"start":2,"end":150,"id":"3.10.110.10","name":"Ubiquitin Conjugating Enzyme"},{"start":159,"end":215,"id":"1.10.8.10","name":"DNA helicase RuvA subunit, C-terminal domain"}]},"uniref50":"UniRef50_P21734","sequence":"MSRAKRIMKEIQAVKDDPAAHITLEFVSESDIHHLKGTFLGPPGTPYEGGKFVVDIEVPMEYPFKPPKMQFDTKVYHPNISSVTGAICLDILKNAWSPVITLKSALISLQALLQSPEPNDPQDAEVAQHYLRDRESFNKTAALWTRLYASETSNGQKGNVEESDLYGIDHDLIDEFESQGFEKDKIVEVLRRLGVKSLDPNDNNTANRIIEELLK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P21734","disprot_id":"DP02193","ncbi_taxon_id":559292,"regions_counter":2,"creator":"epapa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":172,"region_id":"DP02193r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of the flexible class II ubiquitin-conjugating enzyme Ubc1 provides insights for polyubiquitin chain assembly. <i> Merkley N, Shaw GS. </i> J Biol Chem, 2004","statement":[{"text":"The\nthree-dimensional structure of Ubc1 was determined by NMR\nspectroscopy using standard triple resonance and 15N-edited, 13C-edited, and methyl-specific NOE experiments. A family of\n21 structures was chosen (Fig. 1) based on their low energy and\nthe absence of distance violations (Table I). The structure of\nUbc1 contains two individually well defined domains tethered\nby a 22-residue linker.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"epapa","start":150,"term_ontology":"IDPO","curator_name":"Elena Papaleo","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-7376-5894","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"15328341","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-11-19T18:52:04.912Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":172,"term_name":"flexible linker","released":"2025_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Solution structure of the flexible class II ubiquitin-conjugating enzyme Ubc1 provides insights for polyubiquitin chain assembly. <i> Merkley N, Shaw GS. </i> J Biol Chem, 2004","term_id":"IDPO:0000033","curator_id":"vnugnes","start":150,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15328341","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2025-11-19T18:51:59.785Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP02193r002","ec_go":"EXP","disprot_namespace":"Disorder function","cross_refs":[{"db":"BMRB","id":"6202"},{"db":"PDB","id":"1TTE"}],"statement":[{"text":"The three-dimensional structure of Ubc1 was determined by NMR spectroscopy using standard triple resonance and 15N-edited, 13C-edited, and methyl-specific NOE experiments. A family of 21 structures was chosen (Fig. 1) based on their low energy and the absence of distance violations (Table I). The structure of Ubc1 contains two individually well defined domains tethered by a 22-residue linker.","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_P21734","date":"2018-08-28T14:22:49.000Z","acc":"P21734","name":"Ubiquitin-conjugating enzyme E2 1","length":215,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":["Stress response proteins"],"UniParc":"UPI0000137952","genes":[{"name":{"value":"UBC1"},"orfNames":[{"value":"YD9395.10"}],"olnNames":[{"value":"YDR177W"}]}],"alphafold_very_low_content":0.037209302325581395,"disorder_content":0.10697674418604651,"disprot_consensus":{"full":[{"start":150,"end":172,"type":"D"}],"Structural state":[{"start":150,"end":172,"type":"D"}],"Disorder function":[{"start":150,"end":172,"type":"F"}]}},{"features":{"pfam":[{"id":"PF06227","name":"Poxvirus Bcl-2-like proteins","start":12,"end":137}],"gene3D":[{"start":1,"end":149,"id":"1.10.437.20","name":"dsDNA poxvirus"}]},"uniref50":"UniRef50_Q76ZX2","sequence":"MATKLDYEDAVFYFVDDDKICSRDSIIDLIDEYITWRNHVIVFNKDITSCGRLYKELMKFDDVAIRYYGIDKINEIVEAMSEGDHYINFTKVHDQESLFATIGICAKITEHWGYKKISESRFQSLGNITDLMTDDNINILILFLEKKLN","taxonomy":["Viruses","Varidnaviria","Bamfordvirae","Nucleocytoviricota","Pokkesviricetes","Chitovirales","Poxviridae","Chordopoxvirinae","Orthopoxvirus","Vaccinia virus"],"uniref90":"UniRef90_Q76ZX2","disprot_id":"DP02194","ncbi_taxon_id":10254,"regions_counter":4,"creator":"sventura","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":94,"region_id":"DP02194r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Poxvirus K7 protein adopts a Bcl-2 fold: biochemical mapping of its interactions with human DEAD box RNA helicase DDX3. <i> Kalverda AP, Thompson GS, Vogel A, Schröder M, Bowie AG, Khan AR, Homans SW. </i> J Mol Biol, 2009","statement":[{"text":"The disordered regions correspond to residues 83–94 and 116–128 (α5–α6 loop).","type":"Figure"},{"text":"Elevated R1 rates and lower 15N{1H} NOE values measured in the loop 83–94 show that nanosecond time scale internal motions are also present, suggesting that K7 has substantial flexibility in this region relative to other viral and cellular Bcl-2 proteins.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":83,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2K36"},{"db":"BMRB","id":"15740"}],"reference_id":"18845156","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-20T08:08:12.592Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":128,"region_id":"DP02194r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Poxvirus K7 protein adopts a Bcl-2 fold: biochemical mapping of its interactions with human DEAD box RNA helicase DDX3. <i> Kalverda AP, Thompson GS, Vogel A, Schröder M, Bowie AG, Khan AR, Homans SW. </i> J Mol Biol, 2009","statement":[{"text":"The disordered regions correspond to residues 83–94 and 116–128 (α5–α6 loop).","type":"Figure"},{"text":"Cross peaks in the 1H–15N heteronuclear single quantum coherence (HSQC) for one of the regions in the protein (residues 116–128, α5–α6 loop) were relatively weak. In this region, peaks for residues F122, Q123, S124, L125 and I128 were missing from the spectra and could not be assigned, suggesting conformational exchange.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":116,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2K36"},{"db":"BMRB","id":"15740"}],"reference_id":"18845156","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-20T08:08:14.680Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":127,"region_id":"DP02194r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis for targeting of human RNA helicase DDX3 by poxvirus protein K7. <i> Oda S, Schröder M, Khan AR. </i> Structure, 2009","statement":[{"text":"The NMR structure of K7 revealed considerable flexibility in the region 118–127, which is an α helix (α6) in all other known viral and cellular Bcl-2 proteins.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"sventura","start":118,"term_ontology":"IDPO","curator_name":"Salvador Ventura","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-9652-6351","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"19913487","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-20T08:08:15.952Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":118,"end":127,"reference_id":"19913487","reference_source":"pmid","reference_html":"Structural basis for targeting of human RNA helicase DDX3 by poxvirus protein K7. <i> Oda S, Schröder M, Khan AR. </i> Structure, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3JRV"}],"region_id":"DP02194r004","statement":[{"text":"The hydrophobic binding pocket in K7 is bordered by the N terminus (Tyr7), α1, and the region 118–127, which is predominantly nonhelical but is labeled “α6” to remain consistent with the canonical Bcl-2 fold. Despite lacking secondary structure, the backbone in this segment is well ordered in electron density maps.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-20T08:08:11.121Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_Q76ZX2","date":"2018-08-28T14:27:00.000Z","acc":"P68466","name":"Protein K7","length":149,"organism":"Vaccinia virus (strain Western Reserve)","dataset":["Viral proteins"],"UniParc":"UPI0000000007","genes":[{"orfNames":[{"value":"K7R"}],"olnNames":[{"value":"VACWR039"}]}],"disorder_content":0.16778523489932887,"disprot_consensus":{"full":[{"start":83,"end":94,"type":"D"},{"start":116,"end":117,"type":"D"},{"start":118,"end":127,"type":"T"},{"start":128,"end":128,"type":"D"}],"Structural state":[{"start":83,"end":94,"type":"D"},{"start":116,"end":128,"type":"D"}],"Structural transition":[{"start":118,"end":127,"type":"T"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_P53136","sequence":"MRLLVSCVDSGSIKEVLCNIGTDTSVQSALQPFHVAPHLAEGLKAYVDRMWVISEDEAILARNSGVVELVKISKHLKENEALQVDPKGESKNEKSLSDDLPKFDISEFEITSSVSDLFDDAKLESLSSKSVKRTKLVDGFVTLCPIKKDSSNNTFVAATKSGLLHIIKKGEDKKLIKLASLGLKAPVEFLQLYDLEDTDTDKYIFAYGGEENLIKLVEIDSSFQSLKQIWEAKNVKNDRLDMRVPVWPMALRFLEPSPGKTEKGKLNYQFAAITRWSHLTKYSTQHGRKPFAQIDLLPNREPLSQMEVFDAKGENVVSSLGNFQSETFNELNVITTDYKKNVFKFDGNGRMLGKVGRDDITGSSTYIHVHDGKYLLQGGLDRYVRIFDIKTNKMLVKVYVGSRINFIVMLDDVEIEMPLSPSAKAAKGKQKRKVTELEEDADELWNKLEGKVAASKASKKSKI","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P53136","disprot_id":"DP02195","ncbi_taxon_id":559292,"regions_counter":1,"creator":"mlambrughi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":463,"region_id":"DP02195r001","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae. <i> Lo YH, Pillon MC, Stanley RE. </i> J Vis Exp, 2018","statement":[{"text":"Nsa1 is suitable for a hybrid structural approach because it contains a well-structured WD40 domain followed by a functional, but flexible Cterminus\nwhich is not amenable to X-ray crystallography methods. Following is a protocol for the cloning, expression, and purification of S.\ncerevisiae Nsa1 for hybrid structural determination by X-ray crystallography and SAXS.","type":"Introduction"}],"term_id":"IDPO:0000002","curator_id":"mlambrughi","start":434,"term_ontology":"IDPO","curator_name":"Matteo Lambrughi","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-0894-8627","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29364241","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P53136","date":"2018-08-28T14:35:13.000Z","acc":"P53136","name":"Ribosome biogenesis protein NSA1","length":463,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000053232","genes":[{"name":{"value":"NSA1"},"orfNames":[{"value":"G2990"}],"olnNames":[{"value":"YGL111W"}]}],"alphafold_very_low_content":0.047516198704103674,"disorder_content":0.06479481641468683,"disprot_consensus":{"full":[{"start":434,"end":463,"type":"D"}],"Structural state":[{"start":434,"end":463,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00436","name":"Single-strand binding protein family","start":2,"end":103}],"gene3D":[{"start":1,"end":109,"id":"2.40.50.140","name":"Nucleic acid-binding proteins"}]},"uniref50":"UniRef50_P37455","sequence":"MLNRVVLVGRLTKDPELRYTPNGAAVATFTLAVNRTFTNQSGEREADFINCVTWRRQAENVANFLKKGSLAGVDGRLQTRNYENQQGQRVFVTEVQAESVQFLEPKNGGGSGSGGYNEGNSGGGQYFGGGQNDNPFGGNQNNQRRNQGNSFNDDPFANDGKPIDISDDDLPF","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Bacillus"],"uniref90":"UniRef90_P37455","disprot_id":"DP02196","ncbi_taxon_id":224308,"regions_counter":2,"creator":"mlambrughi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":171,"region_id":"DP02196r001","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Defining the Intrinsically Disordered C-Terminal Domain of SSB Reveals DNA-Mediated Compaction. <i> Green M, Hatter L, Brookes E, Soultanas P, Scott DJ. </i> J Mol Biol, 2016","statement":[{"text":"Since removal of the CTD moved the peak, this confirms that it is exclusively the CTDs (residues 107–171) that\ncontribute to this flexibility in solution. This result is in line with previous observations that the SSB CTD\nhas flexible properties","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mlambrughi","start":107,"term_ontology":"IDPO","curator_name":"Matteo Lambrughi","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-0894-8627","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"26707201","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":171,"region_id":"DP02196r002","released":"2022_03","ec_id":"ECO:0006214","reference_html":"Defining the Intrinsically Disordered C-Terminal Domain of SSB Reveals DNA-Mediated Compaction. <i> Green M, Hatter L, Brookes E, Soultanas P, Scott DJ. </i> J Mol Biol, 2016","statement":[{"text":"Since removal of the CTD moved the peak, this confirms that it is exclusively the CTDs (residues 107–171) that\ncontribute to this flexibility in solution. This result is in line with previous observations that the SSB CTD\nhas flexible properties","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mlambrughi","start":107,"term_ontology":"IDPO","curator_name":"Matteo Lambrughi","ec_name":"small-angle neutron scattering evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-0894-8627","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"26707201","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P37455","date":"2018-08-28T14:58:57.000Z","acc":"P37455","name":"Single-stranded DNA-binding protein A","length":172,"organism":"Bacillus subtilis (strain 168)","dataset":[],"UniParc":"UPI0000043503","genes":[{"name":{"value":"ssbA"},"olnNames":[{"value":"BSU40900"}]}],"alphafold_very_low_content":0.22093023255813954,"disorder_content":0.37790697674418605,"disprot_consensus":{"full":[{"start":107,"end":171,"type":"D"}],"Structural state":[{"start":107,"end":171,"type":"D"}]}},{"features":{"pfam":[{"id":"PF06835","name":"Lipopolysaccharide-assembly, LptC-related","start":9,"end":183}],"gene3D":[{"start":59,"end":191,"id":"2.60.450.10","name":"Lipopolysaccharide (LPS) transport protein A like domain"}]},"uniref50":"UniRef50_P0ADW1","sequence":"MSKARRWVIIVLSLAVLVMIGINMAEKDDTAQVVVNNNDPTYKSEHTDTLVYNPEGALSYRLIAQHVEYYSDQAVSWFTQPVLTTFDKDKIPTWSVKADKAKLTNDRMLYLYGHVEVNALVPDSQLRRITTDNAQINLVTQDVTSEDLVTLYGTTFNSSGLKMRGNLRSKNAELIEKVRTSYEIQNKQTQP","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P0ADW1","disprot_id":"DP02197","ncbi_taxon_id":83333,"regions_counter":1,"creator":"mlambrughi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":58,"region_id":"DP02197r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure and functional analysis of LptC, a conserved membrane protein involved in the lipopolysaccharide export pathway in Escherichia coli. <i> Tran AX, Dong C, Whitfield C. </i> J Biol Chem, 2010","statement":[{"text":"Residues 59–184 were observed in the electron density map, but two regions (residues 24–58 and 185–191) were disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mlambrughi","start":24,"term_ontology":"IDPO","curator_name":"Matteo Lambrughi","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-0894-8627","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20720015","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P0ADW1","date":"2018-08-28T15:16:45.000Z","acc":"P0ADV9","name":"Lipopolysaccharide export system protein LptC","length":191,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI000013BFB4","genes":[{"name":{"value":"lptC","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01915","url":"https://hamap.expasy.org/unirule/MF_01915"}}]},"synonyms":[{"value":"yrbK"}],"olnNames":[{"value":"b3199"},{"value":"JW3166"}]}],"alphafold_very_low_content":0,"disorder_content":0.18324607329842932,"disprot_consensus":{"full":[{"start":24,"end":58,"type":"D"}],"Structural state":[{"start":24,"end":58,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00091","name":"Tubulin/FtsZ family, GTPase domain","start":13,"end":172},{"id":"PF12327","name":"FtsZ family, C-terminal domain","start":221,"end":315}],"gene3D":[{"start":9,"end":316,"id":"3.40.50.1440","name":"Tubulin/FtsZ, GTPase domain"}]},"uniref50":"UniRef50_Q9ALA4","sequence":"MFEPMELTNDAVIKVIGVGGGGGNAVEHMVRERIEGVEFFAVNTDAQALRKTAVGQTIQIGSGITKGLGAGANPEVGRNAADEDRDALRAALEGADMVFIAAGMGGGTGTGAAPVVAEVAKDLGILTVAVVTKPFNFEGKKRMAFAEQGITELSKHVDSLITIPNDKLLKVLGRGISLLDAFGAANDVLKGAVQGIAELITRPGLMNVDFADVRTVMSEMGYAMMGSGVASGEDRAEEAAEMAISSPLLEDIDLSGARGVLVNITAGFDLRLDEFETVGNTIRAFASDNATVVIGTSLDPDMNDELRVTVVATGIGMDKRPEITLVTNKQVQQPVMDRYQQHGMAPLTQEQKPVAKVVNDNAPQTAKEPDYLDIPAFLRKQAD","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_Q9ALA4","disprot_id":"DP02201","ncbi_taxon_id":83333,"regions_counter":2,"creator":"mlambrughi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":383,"region_id":"DP02201r001","released":"2022_06","ec_id":"ECO:0006204","reference_html":"The C-terminal linker of Escherichia coli FtsZ functions as an intrinsically disordered peptide. <i> Gardner KA, Moore DA, Erickson HP. </i> Mol Microbiol, 2013","statement":[{"text":"The CD spectra of both Ct tails are similar to each other and to those of other intrinsically disordered peptides","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mlambrughi","start":317,"term_ontology":"IDPO","curator_name":"Matteo Lambrughi","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0894-8627","date":"2022-05-03T08:30:10.999Z","reference_source":"pmid","term_name":"disorder","reference_id":"23714328","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-05-03T08:31:55.958Z"}},{"start":317,"end":383,"reference_id":"35481648","reference_source":"pmid","reference_html":"An enhancer sequence in the intrinsically disordered region of FtsZ promotes polymer-guided substrate processing by ClpXP protease. <i> Viola MG, Perdikari TM, Trebino CE, Rahmani N, Mathews KL, Pena CM, Chua XY, Xuan B, LaBreck CJ, Fawzi NL, Camberg JL. </i> Protein Sci, 2022","date":"2022-05-03T09:25:19.805Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP02201r002","statement":[{"text":"NMR of the monomeric FtsZ C-terminus demonstrates that it is intrinsically disordered","type":"Results"},{"text":"Here, we used solution NMR spectroscopy to elucidate the secondary structure of the monomeric FtsZ CTR. The two-dimensional 1H-15N (heteronuclear single-quantum coherence—HSQC) NMR correlation spectra of FtsZ CTR exhibits narrow chemical shift dispersion, typical of a disordered protein, suggesting a lack of structural order consistent with sequence-based predictions (Figure 1a). Furthermore, we assigned the 13Cα and 13Cβ chemical shifts for FtsZ CTR and computed the secondary chemical shifts (ΔδCα–ΔδCβ), obtained by measuring the difference in the observed 13Cα and 13Cβ chemical shifts and those predicted for a completely disordered structure. These secondary chemical shifts are mostly near zero for all residues, consistent with intrinsic disorder.","type":"Results"},{"text":"Taken together, our data suggest that FtsZ CTR is monomeric and remains mostly intrinsically disordered, although we observe two consecutive residues with strong signatures of partial α-helical conformations and prediction of a short, partially helical motif, amino acids 375 through 379, near the multiprotein interaction site that overlaps the C-terminal ClpX recognition site (amino acids 375–383).","type":"Results"},{"text":"1H-15N HSQC spectrum of FtsZ CTR is consistent with intrinsic disorder.","type":"Figure"},{"text":"Secondary structure populations derived from the observed chemical shifts using the δ2D algorithm confirms the dominance of random coil (i.e., disordered) conformations","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:22:36.074Z"}}],"released":"2018_11","uniref100":"UniRef100_P0A9A8","date":"2018-08-28T16:56:18.000Z","acc":"P0A9A6","name":"Cell division protein FtsZ","length":383,"organism":"Escherichia coli (strain K12)","dataset":["Condensates-related proteins"],"UniParc":"UPI0000047C69","genes":[{"name":{"value":"ftsZ","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00909","url":"https://hamap.expasy.org/unirule/MF_00909"}}]},"synonyms":[{"value":"sfiB"},{"value":"sulB"}],"olnNames":[{"value":"b0095"},{"value":"JW0093"}]}],"alphafold_very_low_content":0.15926892950391644,"disorder_content":0.17493472584856398,"disprot_consensus":{"full":[{"start":317,"end":383,"type":"D"}],"Structural state":[{"start":317,"end":383,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00091","name":"Tubulin/FtsZ family, GTPase domain","start":13,"end":174},{"id":"PF12327","name":"FtsZ family, C-terminal domain","start":222,"end":315}],"gene3D":[{"start":8,"end":220,"id":"3.40.50.1440","name":"Tubulin/FtsZ, GTPase domain"},{"start":221,"end":330,"id":"3.30.1330.20","name":"Tubulin/FtsZ, C-terminal domain"}]},"uniref50":"UniRef50_P17865","sequence":"MLEFETNIDGLASIKVIGVGGGGNNAVNRMIENEVQGVEYIAVNTDAQALNLSKAEVKMQIGAKLTRGLGAGANPEVGKKAAEESKEQIEEALKGADMVFVTAGMGGGTGTGAAPVIAQIAKDLGALTVGVVTRPFTFEGRKRQLQAAGGISAMKEAVDTLIVIPNDRILEIVDKNTPMLEAFREADNVLRQGVQGISDLIATPGLINLDFADVKTIMSNKGSALMGIGIATGENRAAEAAKKAISSPLLEAAIDGAQGVLMNITGGTNLSLYEVQEAADIVASASDQDVNMIFGSVINENLKDEIVVTVIATGFIEQEKDVTKPQRPSLNQSIKTHNQSVPKREPKREEPQQQNTVSRHTSQPADDTLDIPTFLRNRNKRG","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Bacillus"],"uniref90":"UniRef90_P17865","disprot_id":"DP02202","ncbi_taxon_id":224308,"regions_counter":5,"creator":"jssuarez","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":382,"region_id":"DP02202r001","released":"2024_06","ec_id":"ECO:0006204","reference_html":"The C-terminal linker of Escherichia coli FtsZ functions as an intrinsically disordered peptide. <i> Gardner KA, Moore DA, Erickson HP. </i> Mol Microbiol, 2013","statement":[{"text":"The CD spectra of both Ct tails are similar to each other and to those of other intrinsically disordered peptides, such as the adducin tail (Hughes & Bennett, 1995), prothymosin alpha (Gast et al., 1995), and p21 (Kriwacki et al., 1996), suggesting the lack of any prominent secondary structure (Fig. 6a).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":317,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-03-18T15:30:04.274Z","reference_source":"pmid","term_name":"disorder","reference_id":"23714328","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":315,"end":382,"reference_id":"36215496","reference_source":"pmid","reference_html":"Connecting sequence features within the disordered C-terminal linker of <i>Bacillus subtilis</i> FtsZ to functions and bacterial cell division. <i> Shinn MK, Cohan MC, Bullock JL, Ruff KM, Levin PA, Pappu RV. </i> Proc Natl Acad Sci U S A, 2022","date":"2022-10-14T07:36:54.338Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP02202r002","statement":[{"text":"Consistent with the predictions from simulations, ultraviolet circular dichroism (UV-CD) measurements for the isolated CTT peptide indicate that it is conformationally heterogeneous","type":"Results"}]},{"start":315,"end":382,"reference_id":"36215496","reference_source":"pmid","reference_html":"Connecting sequence features within the disordered C-terminal linker of <i>Bacillus subtilis</i> FtsZ to functions and bacterial cell division. <i> Shinn MK, Cohan MC, Bullock JL, Ruff KM, Levin PA, Pappu RV. </i> Proc Natl Acad Sci U S A, 2022","date":"2022-10-14T07:39:07.402Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP02202r003","statement":[{"text":"The spectrum of full-length FtsZ closely resembles that of the ΔCTT construct with a mixture of structures. The sum of the spectra for the core domain and the CTT does not reproduce the spectrum of a full-length protein. This suggests that the CTT likely undergoes conformational changes when it is tethered to the core domain by forming intermodule interactions with the core.","type":"Results"}]},{"start":377,"end":382,"reference_id":"22298780","reference_source":"pmid","reference_html":"Extreme C terminus of bacterial cytoskeletal protein FtsZ plays fundamental role in assembly independent of modulatory proteins. <i> Buske PJ, Levin PA. </i> J Biol Chem, 2012","date":"2022-10-14T08:02:11.174Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP02202r004","statement":[{"text":"Swapping the 6-residue CTV from B. subtilis FtsZ with the 4-residue CTV from Escherichia coli FtsZ completely abolished lateral interactions between chimeric B. subtilis FtsZ polymers.","type":"Abstract"},{"text":"EM images of Bs FtsZ ΔC17 assembled in the presence of GTP indicate that it is almost exclusively in single-stranded protofilaments.","type":"Results"},{"text":"Under standard polymerization conditions, Bs FtsZ CTVE was able to form single-stranded polymers; however, no FtsZ filament bundles were observed (Fig. 3A). ","type":"Results"},{"text":"Data from Ec FtsZ CTVB indicates that the CTV from B. subtilis is sufficient to promote lateral interactions between single-stranded FtsZ polymers.","type":"Results"},{"text":"Our data suggest that CTV charge is the primary determinant of Bs FtsZ lateral interaction potential.","type":"Results"}]},{"start":377,"end":382,"reference_id":"22298780","reference_source":"pmid","reference_html":"Extreme C terminus of bacterial cytoskeletal protein FtsZ plays fundamental role in assembly independent of modulatory proteins. <i> Buske PJ, Levin PA. </i> J Biol Chem, 2012","date":"2022-10-14T08:05:04.486Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0051301","term_name":"cell division","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","region_id":"DP02202r005","statement":[{"text":"Analysis of Bs ftsZ CTVE mutants suggests that the lateral interactions we observed in vitro are critical for FtsZ ring integrity in vivo and support a role for the CTV in stabilizing FtsZ polymers within the cytokinetic ring. Although B. subtilis cells expressing Bs ftsZ CTVE grew normally and exhibited exclusively medial FtsZ rings (Fig. 5A), they were on average ∼85% longer than congenic wild-type cells (Fig. 5D). ∼31% (90 of 290) of Bs ftsZ CTVE mutants were filamentous (>5 cell lengths), suggesting that cells expressing the chimera failed to divide at a relatively high frequency.","type":"Results"},{"text":"Comparisons of cell length (L) with the number of FtsZ rings (R) indicated that the L/R ratio of the Bs ftsZ CTVE mutants was nearly 75% greater than wild-type cells.","type":"Results"}],"term_comment":"Note that this term differs from 'cytokinesis ; GO:0000910' in that cytokinesis does not include nuclear division.","term_def":"\"The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.\" [GOC:di, GOC:go_curators, GOC:pr]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_P17865","date":"2018-08-28T17:12:19.000Z","acc":"P17865","name":"Cell division protein FtsZ","length":382,"organism":"Bacillus subtilis (strain 168)","dataset":[],"UniParc":"UPI000016E7E9","genes":[{"name":{"value":"ftsZ","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00909","url":"https://hamap.expasy.org/unirule/MF_00909"}}]},"olnNames":[{"value":"BSU15290"}]}],"alphafold_very_low_content":0.14921465968586387,"disorder_content":0.17801047120418848,"disprot_consensus":{"full":[{"start":315,"end":382,"type":"T"}],"Structural state":[{"start":315,"end":382,"type":"D"}],"Structural transition":[{"start":315,"end":382,"type":"T"}],"Disorder function":[{"start":377,"end":382,"type":"F"}],"Biological process":[{"start":377,"end":382,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00869","name":"Flavivirus glycoprotein, central and dimerisation domains","start":293,"end":589},{"id":"PF00948","name":"Flavivirus non-structural Protein NS1","start":794,"end":1143},{"id":"PF00949","name":"Peptidase S7, Flavivirus NS3 serine protease","start":1523,"end":1672},{"id":"PF00972","name":"Flavivirus RNA-directed RNA polymerase, fingers and palm domains","start":2781,"end":3233},{"id":"PF01002","name":"Flavivirus non-structural protein NS2B","start":1380,"end":1499},{"id":"PF01003","name":"Flavivirus capsid protein C","start":6,"end":123},{"id":"PF01004","name":"Flavivirus envelope glycoprotein M","start":218,"end":290},{"id":"PF01005","name":"Flavivirus non-structural protein NS2A","start":1155,"end":1308},{"id":"PF01349","name":"Flavivirus non-structural protein NS4B","start":2274,"end":2519},{"id":"PF01350","name":"Flavivirus non-structural protein NS4A","start":2129,"end":2271},{"id":"PF01570","name":"Flavivirus polyprotein propeptide","start":133,"end":214},{"id":"PF01728","name":"FtsJ-like methyltransferase","start":2583,"end":2752},{"id":"PF02832","name":"Flavivirus glycoprotein, immunoglobulin-like domain","start":592,"end":689},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1690,"end":1836},{"id":"PF20483","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","start":3237,"end":3400},{"id":"PF20907","name":"Flavivirus NS3 helicase, C-terminal helical domain","start":1980,"end":2122},{"id":"PF21659","name":"Flavivirus envelope glycoprotein E, stem/anchor domain","start":692,"end":786}],"gene3D":[{"start":588,"end":696,"id":"2.60.40.350","name":"2.60.40.350"},{"start":124,"end":205,"id":"2.60.260.50","name":"Flavivirus polyprotein propeptide domain"},{"start":291,"end":587,"id":"2.60.98.10","name":"Tick-borne Encephalitis virus Glycoprotein, domain 1"},{"start":697,"end":791,"id":"1.20.1280.260","name":"1.20.1280.260"},{"start":23,"end":98,"id":"1.10.10.930","name":"1.10.10.930"},{"start":216,"end":290,"id":"1.10.8.970","name":"Flavivirus envelope glycoprotein M-like"},{"start":1516,"end":1674,"id":"2.40.10.10","name":"Trypsin-like serine proteases"},{"start":1419,"end":1468,"id":"2.40.10.120","name":"2.40.10.120"},{"start":3060,"end":3127,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain"},{"start":2924,"end":3019,"id":"1.10.260.90","name":"1.10.260.90"},{"start":2528,"end":2800,"id":"3.40.50.150","name":"Vaccinia Virus protein VP39"},{"start":2801,"end":2856,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain"},{"start":1689,"end":2022,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":1828,"end":1987,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":1517,"end":1591,"id":"2.40.10.120","name":"2.40.10.120"},{"start":2859,"end":2907,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain"}]},"uniref50":"UniRef50_P06935","sequence":"MSKKPGGPGKSRAVNMLKRGMPRVLSLIGLKRAMLSLIDGKGPIRFVLALLAFFRFTAIAPTRAVLDRWRGVNKQTAMKHLLSFKKELGTLTSAINRRSSKQKKRGGKTGIAVMIGLIASVGAVTLSNFQGKVMMTVNATDVTDVITIPTAAGKNLCIVRAMDVGYMCDDTITYECPVLSAGNDPEDIDCWCTKSAVYVRYGRCTKTRHSRRSRRSLTVQTHGESTLANKKGAWMDSTKATRYLVKTESWILRNPGYALVAAVIGWMLGSNTMQRVVFVVLLLLVAPAYSFNCLGMSNRDFLEGVSGATWVDLVLEGDSCVTIMSKDKPTIDVKMMNMEAANLAEVRSYCYLATVSDLSTKAACPTMGEAHNDKRADPAFVCRQGVVDRGWGNGCGLFGKGSIDTCAKFACSTKAIGRTILKENIKYEVAIFVHGPTTVESHGNYSTQVGATQAGRFSITPAAPSYTLKLGEYGEVTVDCEPRSGIDTNAYYVMTVGTKTFLVHREWFMDLNLPWSSAGSTVWRNRETLMEFEEPHATKQSVIALGSQEGALHQALAGAIPVEFSSNTVKLTSGHLKCRVKMEKLQLKGTTYGVCSKAFKFLGTPADTGHGTVVLELQYTGTDGPCKVPISSVASLNDLTPVGRLVTVNPFVSVATANAKVLIELEPPFGDSYIVVGRGEQQINHHWHKSGSSIGKAFTTTLKGAQRLAALGDTAWDFGSVGGVFTSVGKAVHQVFGGAFRSLFGGMSWITQGLLGALLLWMGINARDRSIALTFLAVGGVLLFLSVNVHADTGCAIDISRQELRCGSGVFIHNDVEAWMDRYKYYPETPQGLAKIIQKAHKEGVCGLRSVSRLEHQMWEAVKDELNTLLKENGVDLSVVVEKQEGMYKSAPKRLTATTEKLEIGWKAWGKSILFAPELANNTFVVDGPETKECPTQNRAWNSLEVEDFGFGLTSTRMFLKVRESNTTECDSKIIGTAVKNNLAIHSDLSYWIESRLNDTWKLERAVLGEVKSCTWPETHTLWGDGILESDLIIPVTLAGPRSNHNRRPGYKTQNQGPWDEGRVEIDFDYCPGTTVTLSESCGHRGPATRTTTESGKLITDWCCRSCTLPPLRYQTDSGCWYGMEIRPQRHDEKTLVQSQVNAYNADMIDPFQLGLLVVFLATQEVLRKRWTAKISMPAILIALLVLVFGGITYTDVLRYVILVGAAFAESNSGGDVVHLALMATFKIQPVFMVASFLKARWTNQENILLMLAAVFFQMAYHDARQILLWEIPDVLNSLAVAWMILRAITFTTTSNVVVPLLALLTPGLRCLNLDVYRILLLMVGIGSLIREKRSAAAKKKGASLLCLALASTGLFNPMILAAGLIACDPNRKRGWPATEVMTAVGLMFAIVGGLAELDIDSMAIPMTIAGLMFAAFVISGKSTDMWIERTADISWESDAEITGSSERVDVRLDDDGNFQLMNDPGAPWKIWMLRMVCLAISAYTPWAILPSVVGFWITLQYTKRGGVLWDTPSPKEYKKGDTTTGVYRIMTRGLLGSYQAGAGVMVEGVFHTLWHTTKGAALMSGEGRLDPYWGSVKEDRLCYGGPWKLQHKWNGQDEVQMIVVEPGKNVKNVQTKPGVFKTPEGEIGAVTLDFPTGTSGSPIVDKNGDVIGLYGNGVIMPNGSYISAIVQGERMDEPIPAGFEPEMLRKKQITVLDLHPGAGKTRRILPQIIKEAINRRLRTAVLAPTRVVAAEMAEALRGLPIRYQTSAVPREHNGNEIVDVMCHATLTHRLMSPHRVPNYNLFVMDEAHFTDPASIAARGYISTKVELGEAAAIFMTATPPGTSDPFPESNSPISDLQTEIPDRAWNSGYEWITEYTGKTVWFVPSVKMGNEIALCLQRAGKKVVQLNRKSYETEYPKCKNDDWDFVITTDISEMGANFKASRVIDSRKSVKPTIITEGEGRVILGEPSAVTAASAAQRRGRIGRNPSQVGDEYCYGGHTNEDDSNFAHWTEARIMLDNINMPNGLIAQFYQPEREKVYTMDGEYRLRGEERKNFLELLRTADLPVWLAYKVAAAGVSYHDRRWCFDGPRTNTILEDNNEVEVITKLGERKILRPRWIDARVYSDHQALKAFKDFASGKRSQIGLIEVLGKMPEHFMGKTWEALDTMYVVATAEKGGRAHRMALEELPDALQTIALIALLSVMTMGVFFLLMQRKGIGKIGLGGAVLGVATFFCWMAEVPGTKIAGMLLLSLLLMIVLIPEPEKQRSQTDNQLAVFLICVMTLVSAVAANEMGWLDKTKSDISSLFGQRIEVKENFSMGEFLLDLRPATAWSLYAVTTAVLTPLLKHLITSDYINTSLTSINVQASALFTLARGFPFVDVGVSALLLAAGCWGQVTLTVTVTAATLLFCHYAYMVPGWQAEAMRSAQRRTAAGIMKNAVVDGIVATDVPELERTTPIMQKKVGQIMLILVSLAAVVVNPSVKTVREAGILITAAAVTLWENGASSVWNATTAIGLCHIMRGGWLSCLSITWTLIKNMEKPGLKRGGAKGRTLGEVWKERLNQMTKEEFTRYRKEAIIEVDRSAAKHARKEGNVTGGHPVSRGTAKLRWLVERRFLEPVGKVIDLGCGRGGWCYYMATQKRVQEVRGYTKGGPGHEEPQLVQSYGWNIVTMKSGVDVFYRPSECCDTLLCDIGESSSSAEVEEHRTIRVLEMVEDWLHRGPREFCVKVLCPYMPKVIEKMELLQRRYGGGLVRNPLSRNSTHEMYWVSRASGNVVHSVNMTSQVLLGRMEKRTWKGPQYEEDVNLGSGTRAVGKPLLNSDTSKIKNRIERLRREYSSTWHHDENHPYRTWNYHGSYDVKPTGSASSLVNGVVRLLSKPWDTITNVTTMAMTDTTPFGQQRVFKEKVDTKAPEPPEGVKYVLNETTNWLWAFLAREKRPRMCSREEFIRKVNSNAALGAMFEEQNQWRSAREAVEDPKFWEMVDEEREAHLRGECHTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARFLEFEALGFLNEDHWLGRKNSGGGVEGLGLQKLGYILREVGTRPGGKIYADDTAGWDTRITRADLENEAKVLELLDGEHRRLARAIIELTYRHKVVKVMRPAADGRTVMDVISREDQRGSGQVVTYALNTFTNLAVQLVRMMEGEGVIGPDDVEKLTKGKGPKVRTWLFENGEERLSRMAVSGDDCVVKPLDDRFATSLHFLNAMSKVRKDIQEWKPSTGWYDWQQVPFCSNHFTELIMKDGRTLVVPCRGQDELVGRARISPGAGWNVRDTACLAKSYAQMWLLLYFHRRDLRLMANAICSAVPVNWVPTGRTTWSIHAGGEWMTTEDMLEVWNRVWIEENEWMEDKTPVEKWSDVPYSGKREDIWCGSLIGTRARATWAENIQVAINQVRAIIGDEKYVDYMSSLKRYEDTTLVEDTVL","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Flavivirus"],"uniref90":"UniRef90_P06935","disprot_id":"DP02203","ncbi_taxon_id":1968826,"regions_counter":1,"creator":"lchemes","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":919,"region_id":"DP02203r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Flavivirus NS1 structures reveal surfaces for associations with membranes and the immune system. <i> Akey DL, Brown WC, Dutta S, Konwerski J, Jose J, Jurkiw TJ, DelProposto J, Ogata CM, Skiniotis G, Kuhn RJ, Smith JL. </i> Science, 2014","statement":[{"text":"Flexible region in the West Nile Virus NS1 protein, corresponds to a disordered loop which is also disordered in the DENV2 NS1 protein. Corresponds to an antigenic region containing a conserved hydrophobic WKxW motif","type":"Curator statement"},{"text":"Each “wing” domain contains two glycosylation sites (Asn130, Asn175), an internal disulfide (Cys55-Cys143), and two discreet subdomains. An α/β subdomain (amino acids 38 – 151) comprises a four-stranded β-sheet, two α-helices and a disordered distal tip (amino acids 108 – 128; Fig. 1A, dotted line).","type":"Article"},{"text":"A 20-residue disordered region is indicated with dotted lines.","type":"Figure"},{"text":"Ns1 disordered distal tip (amino acids 108 – 128) corresponds to 899-919 region of the West Nile virus (strain NY-99) polyprotein.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":899,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24505133","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","cross_refs":[{"db":"PDB","id":"4O6C"},{"db":"PDB","id":"4O6D"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-11T12:50:29.794Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9Q6P4","date":"2018-08-28T23:20:45.000Z","acc":"Q9Q6P4","name":"Genome polyprotein","length":3433,"organism":"West Nile virus (strain NY-99)","dataset":["Viral proteins","Neglected tropical diseases proteins","RNA-binding proteins"],"UniParc":"UPI000052ABFC","genes":[{"name":{"value":"GP1","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"ANW69091.1","url":"https://www.ebi.ac.uk/ena/browser/view/ANW69091.1"}}]},"orfNames":[{"value":"MZ11_60484gpGP1","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"ANW69091.1","url":"https://www.ebi.ac.uk/ena/browser/view/ANW69091.1"}}]},{"value":"MZ11_60553gpGP1","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"ANW69112.1","url":"https://www.ebi.ac.uk/ena/browser/view/ANW69112.1"}}]}]}],"disorder_content":0.006117098747451209,"disprot_consensus":{"full":[{"start":899,"end":919,"type":"D"}],"Structural state":[{"start":899,"end":919,"type":"D"}]}},{"acc":"Q5UB51","sequence":"MNNQRKKTGKPSINMLKRVRNRVSTGSQLAKRFSRGLLNGQGPMKLVMAFIAFLRFLAIPPTAGVLARWGTFKKSGAIKVLKGFKKEISNMLSIINKRKKTSLCLMMILPATLAFHLTSRDGEPRMIVGKNERGKSLLFKTASGINMCTLIAMDLGEMCDDTVTYKCPLIAEVEPEDIDCWCNLTSTWVTYGTCNQAGEHRRDKRSVALAPHVGMGLDTRTQTWMSAEGAWRQVEKVETWALRHPGFTILALFLAHYIGTSLTQKVVIFILLMLVTPSMTMRCVGVGNRDFVEGLSGATWVDVVLEHGGCVTTMAKNKPTLDIELQKTEATQLATLRKLCIEGKITNITTDSRCPTQGEAILPEEQDQNYVCKHTYVDRGWGNGCGLFGKGSLVTCAKFQCLEPIEGKVVQHENLKYTVIITVHTGDQHQVGNDTQGVTVEITPQASTVEAILPEYGTLGLECSPRTGLDFNEMILLTMKNKAWMVHRQWFFDLPLPWTSGATTEAPTWNRKELLVTFKNAHAKKQEVVVLGSQEGAMHTALTGATEIQNSGGTSIFAGHLKCRLKMDKLELKGMSYAMCLNTFVLKKEVSETQHGTILIKVEYKGEDAPCKIPFSTEDGQGKAHNGRLITANPVVTKKEEPVNIEAEPPFGESNIVIGIGDKALKINWYKKGSSIGKMFEATARGARRMAILGDTAWDFGSVGGVLNSLGKMVHQIFGSAYTALFSGVSWIMKIGIGVLLTWIGLNSKNTSMSFSCIAIGIITLYLGAVVQADMGCVINWKGKELKCGSGIFVTNEVHTWTEQYKFQADSPKRLATAIAGAWENGVCGIRSTTRMENLLWKQIANELNYILWENNIKLTVVVGDIIGVLEQGKRTLTPQPMELKYSWKTWGKAKIVTAETQNSSFIIDGPNTPECPSASRAWNVWEVEDYGFGVFTTNIWLKLREVYTQSCDHRLMSAAIKDERAVHADMGYWIESQKNGSWKLEKASFIEVKTCTWPKSHTLWSNGVLESDMIIPKSLAGPISQHNHRPGYHTQTAGPWHLGKLELDFNYCEGTTVVITENCGTRGPSLRATTVSGKLIHEWCCRSCTLPPLRYMGEDGCWYGMEIRPVNEKEENMVKSLVSAGSGKVDNFTMGVLCLAILFEEVMRGKFGKKHMIAGVLFTFVLLLSGQITWRDMAHTLIMIGSNASDRMGMGVTCLALIATFKIQPFLALGFFLRKLTSRENLLLGVGLAMATTLQLPEDIEQMANGIALGLMTLKLITQFETYQLWTALVSLTCSNTIFTLTVAWRTATLILAGVSLLPVCQSSSMRKTDWLPMTVAAMGVPPLPLFIFSLKDALKRRSWPLNEGVMAVGLVSILASSLLRNDVPMAGPLVAGGLLIACYVITGTSADLTVEKAADVTWEEEAEQTGVSHNLMITVDDDGTMRIKDDETENILTVLLKTALLIVSGIFPYSIPATLLVWHTWQKQTQRSGVLWDVPSPPETQKAELEEGVYRIKQQGIFGKTQVGVGVQKEGVFHTMWHVTRGAVLTHNGKRLEPNWASVKKDLISYGGGWRLSAQWQKGEEVQVIAVEPGKNPKNFQTMPGIFQTTTGEIGAIALDFKPGTSGSPIINREGKVVGLYGNGVVTKNGGYVSGIAQTNAEPDGPTPELEEEMFKKRNLTIMDLHPGSGKTRKYLPAIVREAIKRRLRTLILAPTRVVAAEMEEALKGLPIRYQTTATKSEHTGREIVDLMCHATFTMRLLSPVRVPNYNLIIMDEAHFTDPASIAARGYISTRVGMGEAAAIFMTATPPGTAEAFPQSNAPIQDEERDIPERSWNSGNEWITDFVGKTVWFVPSIKAGNDIANCLRKNGKKVIQLSRKTFDTEYQKTKLNDWDFVVTTDISEMGANFKADRVIDPRRCLKPVILTDGPERVILAGPMPVTAASAAQRRGRVGRNPQKENDQYIFTGQPLNNDEDHAHWTEAKMLLDNINTPEGIIPALFEPEREKSAAIDGEYRLKGESRKTFVELMRRGDLPVWLAHKVASEGIKYTDRKWCFDGERNNQILEENMDVEIWTKEGERKKLRPRWLDARTYSDPLALKEFKDFAAGRKSIALDLVTEIGRVPSHLAHRTRNALDNLVMLHTSEHGGRAYRHAVEELPETMETLLLLGLMILLTGGAMLFLISGKGIGKTSIGLICVIASSGMLWMADVPLQWIASAIVLEFFMMVLLIPEPEKQRTPQDNQLAYVVIGILTLAAIVAANEMGLLETTKRNLGMSKEPGVVSPTSYLDVDLHPASAWTLYAVATTVITPMLRHTIENSTANVSLAAIANQAVVLMGLDKGWPISKMDLGVPLLALGCYSQVNPLTLTAAVLLLVTHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGIMTIDLDPVIYDSKFEKQLGQVMLLVLCAVQLLLMKTSWALCEVLTLATGPITTLWEGSPGKFWNTTIAVSMANIFRGSYLAGAGLAFSIMKSVGTGKRGTGSQGETLGEKWKKKLNQLSRKEFDLYKKSGITEVDRTEAKEGLKRGEITHHAVSRGSAKLQWFVERNMVIPEGRVIDLGCGRGGWSYYCAGLKKVTEVRGYTKGGPGHEEPVPMSTYGWNIVKLMSGKDVFYLPPEKCDTLLCDIGESSPSPTVEESRTIRVLKMVEPWLKNNQFCIKVLNPYMPTVIEHLERLQRKHGGMLVRNPLSRNSTHEMYWISNGTGNIVSSVNMVSRLLLNRFTMTHRRPTIEKDVDLGAGTRHVNAEPETPNMDVIGERIKRIKEEHSSTWHYDDENPYKTWAYHGSYEVKATGSASSMINGVVKLLTKPWDVVPMVTQMAMTDTTPFGQQRVFKEKVDTRTPRPMPGTRKVMEITAEWLWRTLGRNKRPRLCTREEFTKKVRTNAAMGAVFTEENQWDSARAAVEDEEFWKLVDRERELHKLGKCGSCVYNMMGKREKKLGEFGKAKGSRAIWYMWLGARYLEFEALGFLNEDHWFSRENSYSGVEGEGLHKLGYILRDISKIPGGAMYADDTAGWDTRITEDDLHNEEKITQQMDPEHRQLANAIFKLTYQNKVVKVQRPTPKGTVMDIISRKDQRGSGQVGTYGLNTFTNMEAQLVRQMEGEGVLSKADLENPHPLEKKITQWLETKGVERLKRMAISGDDCVVKPIDDRFANALLALNDMGKVRKDIPQWQPSKGWHDWQQVPFCSHHFHELIMKDGRKLVVPCRPQDELIGRARISQGAGWSLKETACLGKAYAQMWSLMYFHRRDLRLASNAICSAVPVHWVPTSRTTWSIHAHHQWMTTEDMLTVWNRVWIEDNPWMEDKTPVTTWEDVPYLGKREDQWCGSLIGLTSRATWAQNILIAIQQVRSLIGDEEFLDYMPSMKRFRKEEESEGAIW","creator":"lchemes","dataset":["Viral proteins","Neglected tropical diseases proteins","RNA-binding proteins"],"date":"2018-08-28T23:44:19.000Z","disprot_id":"DP02204","features":{"pfam":[{"id":"PF00869","name":"Flavivirus glycoprotein, central and dimerisation domains","start":282,"end":574},{"id":"PF00948","name":"Flavivirus non-structural Protein NS1","start":776,"end":1128},{"id":"PF00949","name":"Peptidase S7, Flavivirus NS3 serine protease","start":1490,"end":1641},{"id":"PF00972","name":"Flavivirus RNA-directed RNA polymerase, fingers and palm domains","start":2740,"end":3190},{"id":"PF01002","name":"Flavivirus non-structural protein NS2B","start":1347,"end":1473},{"id":"PF01003","name":"Flavivirus capsid protein C","start":6,"end":110},{"id":"PF01004","name":"Flavivirus envelope glycoprotein M","start":207,"end":279},{"id":"PF01005","name":"Flavivirus non-structural protein NS2A","start":1136,"end":1309},{"id":"PF01349","name":"Flavivirus non-structural protein NS4B","start":2243,"end":2483},{"id":"PF01350","name":"Flavivirus non-structural protein NS4A","start":2097,"end":2238},{"id":"PF01570","name":"Flavivirus polyprotein propeptide","start":120,"end":204},{"id":"PF01728","name":"FtsJ-like methyltransferase","start":2545,"end":2712},{"id":"PF02832","name":"Flavivirus glycoprotein, immunoglobulin-like domain","start":576,"end":671},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1658,"end":1804},{"id":"PF20483","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","start":3194,"end":3354},{"id":"PF20907","name":"Flavivirus NS3 helicase, C-terminal helical domain","start":1950,"end":2090},{"id":"PF21659","name":"Flavivirus envelope glycoprotein E, stem/anchor domain","start":674,"end":768}],"gene3D":[{"start":115,"end":195,"id":"2.60.260.50","name":"Flavivirus polyprotein propeptide domain","_id":"685af523b4ac24d5329d93dd"},{"start":282,"end":572,"id":"2.60.98.10","name":"Tick-borne Encephalitis virus Glycoprotein, domain 1","_id":"685af523b4ac24d5329d93de"},{"start":677,"end":773,"id":"1.20.1280.260","name":"1.20.1280.260","_id":"685af523b4ac24d5329d93df"},{"start":573,"end":676,"id":"2.60.40.350","name":"2.60.40.350","_id":"685af523b4ac24d5329d93e0"},{"start":206,"end":280,"id":"1.10.8.970","name":"Flavivirus envelope glycoprotein M-like","_id":"685af523b4ac24d5329d93e1"},{"start":21,"end":100,"id":"1.10.10.930","name":"1.10.10.930","_id":"685af523b4ac24d5329d93e2"},{"start":344,"end":532,"id":"3.30.387.10","name":"Viral Envelope Glycoprotein, domain 3","_id":"685af523b4ac24d5329d93e3"},{"start":332,"end":547,"id":"3.30.67.10","name":"Viral Envelope Glycoprotein, domain 2","_id":"685af523b4ac24d5329d93e4"},{"start":2759,"end":2824,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d93e5"},{"start":1657,"end":1989,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d93e6"},{"start":2491,"end":2758,"id":"3.40.50.150","name":"Vaccinia Virus protein VP39","_id":"685af523b4ac24d5329d93e7"},{"start":2883,"end":2978,"id":"1.10.260.90","name":"1.10.260.90","_id":"685af523b4ac24d5329d93e8"},{"start":1387,"end":1451,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d93e9"},{"start":1796,"end":1955,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d93ea"},{"start":2829,"end":2869,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d93eb"},{"start":3018,"end":3085,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d93ec"},{"start":1494,"end":1562,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d93ed"},{"start":1467,"end":1640,"id":"2.40.10.10","name":"Trypsin-like serine proteases","_id":"685af523b4ac24d5329d93ee"}]},"genes":[],"length":3390,"name":"Genome polyprotein","ncbi_taxon_id":408693,"organism":"Dengue virus type 3 (strain Singapore/8120/1995)","regions_counter":4,"released":"2018_11","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Flavivirus"],"UniParc":"UPI0000452530","uniref100":"UniRef100_Q5UB51","uniref50":"UniRef50_P17763","uniref90":"UniRef90_Q6YMS4","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3U1J","_id":"685af523b4ac24d5329d93f1"}],"curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1413,"end":1438,"interaction_partner":[],"reference_html":"Ligand-bound structures of the dengue virus protease reveal the active conformation. <i> Noble CG, Seh CC, Chao AT, Shi PY. </i> J Virol, 2012","reference_id":"22031935","region_id":"DP02204r001","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The region corresponds to a flexible and disordered region of the NS2B protein, which is an NS3 protease cofactor. This region can be crystallized in different conformations, or be missing from the electron densities","_id":"685af523b4ac24d5329d93f0"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-26T13:36:41.647Z","_id":"685af523b4ac24d5329d93f2"},"version":2,"_id":"685af523b4ac24d5329d93ef","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3U1J","_id":"685af523b4ac24d5329d93f9"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1413,"end":1419,"interaction_partner":[{"db":"UniProt","id":"Q5UB51","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d93fa"}],"reference_html":"Ligand-bound structures of the dengue virus protease reveal the active conformation. <i> Noble CG, Seh CC, Chao AT, Shi PY. </i> J Virol, 2012","reference_id":"22031935","region_id":"DP02204r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Residues 50 to 61 of NS2B form a tight complex with NS3, and it has been proposed that W61 is the last residue that is tightly bound to NS3, after which the rest of the residues (residues 62 to 88) are flexible and able to adopt multiple conformations (1). However, the structures of both DENV-1 protease and DENV-3 protease-aprotinin show that more residues (beyond W61) from NS2B are interacting with NS3 (up to T68 and E66 of NS2B, respectively). These results suggest that the conformational change to the closed form is a dynamic and iterative process.","_id":"685af523b4ac24d5329d93fb"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-26T13:36:39.579Z","_id":"685af523b4ac24d5329d93fc"},"version":1,"_id":"685af523b4ac24d5329d93f8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3U1J","_id":"685af523b4ac24d5329d93fe"},{"db":"PDB","id":"3U1I","_id":"685af523b4ac24d5329d93ff"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1645,"end":1655,"interaction_partner":[],"reference_html":"Ligand-bound structures of the dengue virus protease reveal the active conformation. <i> Noble CG, Seh CC, Chao AT, Shi PY. </i> J Virol, 2012","reference_id":"22031935","region_id":"DP02204r004","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The PDB shows the disorder region from 1645-1655 (NS3).","_id":"685af523b4ac24d5329d9400"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-26T13:36:46.448Z","_id":"685af523b4ac24d5329d9401"},"version":1,"_id":"685af523b4ac24d5329d93fd","reference_source":"pmid"}],"__v":0,"disorder_content":0.010914454277286136,"disprot_consensus":{"full":[{"start":1413,"end":1438,"type":"D"},{"start":1645,"end":1655,"type":"D"}],"Structural state":[{"start":1413,"end":1438,"type":"D"},{"start":1645,"end":1655,"type":"D"}],"Molecular function":[{"start":1413,"end":1419,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02496","name":"ABA/WDS induced protein","start":150,"end":227}]},"uniref50":"UniRef50_Q2TUW1","sequence":"MAEEKHHKHRLFHHHKDEDNKPVETDTGYDNTSYSKPSDDYDSGFNKPSYESSGGGYEGGYNKTSYSSDEPASGGGYEGGYKKTGYSGGIDETSGGYGAGGGGYSDVTDGGYGKPSGGYGAAGGGGVYPDTTTDGGYSKTSGGGYDDEVDYKKEEKHHKHLEHLGELGAASAAAYALHEKHKAEKDPEHAHRHKIEEEVAAAAAVGSGGFAFHEHHEKKEAKEQDEEAHGKKHHHLFG","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","fabids","Fabales","Fabaceae","Papilionoideae","50 kb inversion clade","NPAAA clade","indigoferoid/millettioid clade","Phaseoleae","Glycine","Glycine subgen. Soja"],"uniref90":"UniRef90_Q2TUW1","disprot_id":"DP02205","ncbi_taxon_id":3847,"regions_counter":12,"creator":"lchemes","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":238,"region_id":"DP02205r001","released":"2024_06","ec_id":"ECO:0006204","reference_html":"Effects of Fe3+ and Zn2+ on the structural and thermodynamic properties of a soybean ASR protein. <i> Li RH, Liu GB, Wang H, Zheng YZ. </i> Biosci Biotechnol Biochem, 2013","statement":[{"text":"The protein was disordered in aqueous solution, as indicated by a single minimum at about 198 nm in the CD spectra.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"23470734","version":3,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2024-02-01T15:20:56.255Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":238,"term_name":"zinc ion binding","start":1,"ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"In contrast, the CD signal decayed sharply when various concentrations of Zn2þ (4–40 mM) were added (Fig. 3B), indicating that the structures of GmASR changed in the presence of Zn2þ.","type":"Abstract"}],"curator_id":"vnugnes","released":"2024_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"23470734","version":4,"reference_html":"Effects of Fe3+ and Zn2+ on the structural and thermodynamic properties of a soybean ASR protein. <i> Li RH, Liu GB, Wang H, Zheng YZ. </i> Biosci Biotechnol Biochem, 2013","date":"2024-02-01T15:39:30.947Z","term_id":"GO:0008270","ec_id":"ECO:0006204","region_id":"DP02205r002","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a zinc ion (Zn).\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"ChEBI","id":"29105","operator":null,"partner_start":null,"partner_end":null}]},{"start":1,"end":238,"reference_id":"23470734","reference_source":"pmid","reference_html":"Effects of Fe3+ and Zn2+ on the structural and thermodynamic properties of a soybean ASR protein. <i> Li RH, Liu GB, Wang H, Zheng YZ. </i> Biosci Biotechnol Biochem, 2013","date":"2024-02-01T15:17:23.765Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0016151","term_name":"nickel cation binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006082","ec_ontology":"ECO","ec_name":"affinity chromatography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"49786","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02205r003","statement":[{"text":"Since the GmASR protein itself bound to the Ni beads in the purification column, there was no need to add His tags, usually a necessary step in this method.","type":"Results"},{"text":"However, it did remain in the columns immobilizing Fe3þ, Ni2þ, Cu2þ, and Zn2þ ions. The proteins retained in these columns were eluted by EDTA, indicating that GmASR was retained in the columns due to binding to Fe3þ, Ni2þ, Cu2þ, and Zn2þ (Fig. 1B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a nickel (Ni) cation.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":238,"reference_id":"23470734","reference_source":"pmid","reference_html":"Effects of Fe3+ and Zn2+ on the structural and thermodynamic properties of a soybean ASR protein. <i> Li RH, Liu GB, Wang H, Zheng YZ. </i> Biosci Biotechnol Biochem, 2013","date":"2024-02-01T15:15:30.606Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005506","term_name":"iron ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006082","ec_ontology":"ECO","ec_name":"affinity chromatography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"29034","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02205r004","statement":[{"text":"However, it did remain in the columns immobilizing Fe3þ, Ni2þ, Cu2þ,\nand Zn2þ ions. The proteins retained in these columns were eluted by EDTA, indicating that GmASR was retained in the columns due to binding to Fe3þ, Ni2þ, Cu2þ, and Zn2þ (Fig. 1B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an iron (Fe) ion.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":238,"reference_id":"23470734","reference_source":"pmid","reference_html":"Effects of Fe3+ and Zn2+ on the structural and thermodynamic properties of a soybean ASR protein. <i> Li RH, Liu GB, Wang H, Zheng YZ. </i> Biosci Biotechnol Biochem, 2013","date":"2024-02-01T15:16:11.849Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005507","term_name":"copper ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006082","ec_ontology":"ECO","ec_name":"affinity chromatography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"29036","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02205r005","statement":[{"text":"However, it did remain in the columns immobilizing Fe3þ, Ni2þ, Cu2þ,\nand Zn2þ ions. The proteins retained in these columns were eluted by EDTA, indicating that GmASR was retained in the columns due to binding to Fe3þ, Ni2þ, Cu2þ, and Zn2þ (Fig. 1B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a copper (Cu) ion.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":238,"reference_id":"23470734","reference_source":"pmid","reference_html":"Effects of Fe3+ and Zn2+ on the structural and thermodynamic properties of a soybean ASR protein. <i> Li RH, Liu GB, Wang H, Zheng YZ. </i> Biosci Biotechnol Biochem, 2013","date":"2024-02-01T15:16:40.145Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008270","term_name":"zinc ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006082","ec_ontology":"ECO","ec_name":"affinity chromatography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"29105","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02205r006","statement":[{"text":"However, it did remain in the columns immobilizing Fe3þ, Ni2þ, Cu2þ,\nand Zn2þ ions. The proteins retained in these columns were eluted by EDTA, indicating that GmASR was retained in the columns due to binding to Fe3þ, Ni2þ, Cu2þ, and Zn2þ (Fig. 1B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a zinc ion (Zn).\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":238,"reference_id":"23470734","reference_source":"pmid","reference_html":"Effects of Fe3+ and Zn2+ on the structural and thermodynamic properties of a soybean ASR protein. <i> Li RH, Liu GB, Wang H, Zheng YZ. </i> Biosci Biotechnol Biochem, 2013","date":"2024-02-01T15:18:21.015Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008270","term_name":"zinc ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006329","ec_ontology":"ECO","ec_name":"static fluorescence quenching evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"29105","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02205r007","statement":[{"text":"The results showed that the addition of Fe3þ or Zn2þ quenched the fluorescence of the GmASR protein markedly (Fig. 1C and D), providing further evidence that the protein does indeed bind directly to Fe3þ and Zn2þ ions.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a zinc ion (Zn).\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":238,"reference_id":"23470734","reference_source":"pmid","reference_html":"Effects of Fe3+ and Zn2+ on the structural and thermodynamic properties of a soybean ASR protein. <i> Li RH, Liu GB, Wang H, Zheng YZ. </i> Biosci Biotechnol Biochem, 2013","date":"2024-02-01T15:18:39.468Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005506","term_name":"iron ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006329","ec_ontology":"ECO","ec_name":"static fluorescence quenching evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"29034","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02205r008","statement":[{"text":"The results showed that the addition of Fe3þ or Zn2þ quenched the fluorescence of the GmASR protein markedly (Fig. 1C and D), providing further evidence that the protein does indeed bind directly to Fe3þ and Zn2þ ions.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an iron (Fe) ion.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":238,"reference_id":"23470734","reference_source":"pmid","reference_html":"Effects of Fe3+ and Zn2+ on the structural and thermodynamic properties of a soybean ASR protein. <i> Li RH, Liu GB, Wang H, Zheng YZ. </i> Biosci Biotechnol Biochem, 2013","date":"2024-02-01T15:20:03.756Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005506","term_name":"iron ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"29034","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02205r009","statement":[{"text":"The calorimetric data for Fe3þ titration into a GmASR solution were fitted to a sequential three-site binding model, while the corresponding data for Zn2þ titration were fitted to a sequential two-site binding\nmodel (Fig. 2, Table 1).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an iron (Fe) ion.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":238,"reference_id":"23470734","reference_source":"pmid","reference_html":"Effects of Fe3+ and Zn2+ on the structural and thermodynamic properties of a soybean ASR protein. <i> Li RH, Liu GB, Wang H, Zheng YZ. </i> Biosci Biotechnol Biochem, 2013","date":"2024-02-01T15:20:22.564Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008270","term_name":"zinc ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"29105","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02205r010","statement":[{"text":"The calorimetric data for Fe3þ titration into a GmASR solution were fitted to a sequential three-site binding model, while the corresponding data for Zn2þ titration were fitted to a sequential two-site binding\nmodel (Fig. 2, Table 1).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a zinc ion (Zn).\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":238,"reference_id":"23470734","reference_source":"pmid","reference_html":"Effects of Fe3+ and Zn2+ on the structural and thermodynamic properties of a soybean ASR protein. <i> Li RH, Liu GB, Wang H, Zheng YZ. </i> Biosci Biotechnol Biochem, 2013","date":"2024-02-01T16:00:41.372Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140315","term_name":"iron ion sequestering activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"29034","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02205r011","statement":[{"text":"Hydroxyl radicals in particular are highly reactive, and can be generated by the Fe-promoted Fenton reaction.13,18,21) To determine whether the GmASR protein can inhibit hydroxyl radical\ngeneration, the effect of GmASR on hydroxyl radicals generated by Fe3þ was analyzed by measuring the degree of deoxyribose degradation.","type":"Results"},{"text":"The results showed that GmASR protein caused concentration-dependent inhibition of deoxyribose degradation under conditions consistent with a site-specific mechanism (Fig. 4A and B), but no\nevidence was found of non-site-specific scavenging by GmASR of hydroxyl radicals (data not shown).","type":"Results"},{"text":"These results indicate that the GmASR protein blocks the generation of hydroxyl radicals by chelating Fe3þ ions (the site-specific mechanism) rather than by directly scavenging generated hydroxyl radicals (the non-sitespecific mechanism).","type":"Results"}],"term_comment":"","term_def":"\"The selective interaction of a protein with an iron ion to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:27780864]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":238,"reference_id":"23470734","reference_source":"pmid","reference_html":"Effects of Fe3+ and Zn2+ on the structural and thermodynamic properties of a soybean ASR protein. <i> Li RH, Liu GB, Wang H, Zheng YZ. </i> Biosci Biotechnol Biochem, 2013","date":"2024-02-01T16:00:50.827Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0016209","term_name":"antioxidant activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001258","ec_ontology":"ECO","ec_name":"spectrophotometry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","region_id":"DP02205r012","statement":[{"text":"The anti-oxidative activity of the GmASR protein was found to be much higher than that of BSA, a standard protective agent against the hydroxyl radical (Fig. 4B). These results indicate that GmASR protein can reduce the levels of hydroxyl radical generated by the Fe3þ/H2O2 system via a site-specific mechanism, thereby inhibiting deoxyribose degradation as a consequence of its Fe3þ binding capability.","type":"Results"},{"text":"A common index of DNA damage is the conversion of the supercoiled form (SC) of plasmid DNA to the open circular (OC) and the linear form (LC).17) The inhibitory effect of the GmASR protein against oxidative DNA damage was investigated by a DNA cleavage assay using pET15b plasmid DNA. As Fig. 4C shows, in the absence of the protein, most of the supercoiled DNA was cut by the hydroxyl radicals generated by the\nFenton reaction (Fig. 4C, lanes 2–3). The GmASR protein protected DNA from oxidative damage in the absence of EDTA.","type":"Results"},{"text":"These results indicate that the GmASR protein blocks the generation of hydroxyl radicals by chelating Fe3þ ions (the site-specific mechanism) rather than by directly scavenging generated hydroxyl radicals (the non-sitespecific mechanism).","type":"Results"}],"term_comment":"","term_def":"\"Inhibition of the reactions brought about by dioxygen (O2) or peroxides. Usually the antioxidant is effective because it can itself be more easily oxidized than the substance protected. The term is often applied to components that can trap free radicals, thereby breaking the chain reaction that normally leads to extensive biological damage.\" [ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_Q2TUW1","date":"2018-08-29T09:00:18.000Z","acc":"Q2TUW1","name":"Abscisic stress ripening-like protein","length":238,"organism":"Glycine max","dataset":[],"UniParc":"UPI0000679744","genes":[{"name":{"value":"732594","evidences":[{"code":"ECO:0000313","source":{"name":"EnsemblPlants","id":"KRG91659","url":"http://www.ensemblgenomes.org/id/KRG91659"}}]},"orfNames":[{"value":"GLYMA_20G167500","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"KRG91659.1","url":"https://www.ebi.ac.uk/ena/browser/view/KRG91659.1"}}]}]}],"alphafold_very_low_content":0.5462184873949579,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":238,"type":"D"}],"Structural state":[{"start":1,"end":238,"type":"D"}],"Molecular function":[{"start":1,"end":238,"type":"F"}]}},{"features":{"pfam":[{"id":"PF30867","name":"Histatin-1-like","start":20,"end":51}]},"uniref50":"UniRef50_P15516","sequence":"MKFFVFALILALMLSMTGADSHAKRHHGYKRKFHEKHHSHRGYRSNYLYDN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P15516","disprot_id":"DP02206","ncbi_taxon_id":9606,"regions_counter":5,"creator":"mlambrughi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":51,"region_id":"DP02206r001","released":"2024_06","ec_id":"ECO:0006165","reference_html":"NMR studies of the antimicrobial salivary peptides histatin 3 and histatin 5 in aqueous and nonaqueous solutions. <i> Brewer D, Hunter H, Lajoie G. </i> Biochem Cell Biol, 1998","statement":[{"text":"However, H3 remains essentially unordered as suggested by the lack of longer range nuclear Overhauser effects (NOEs) in the NOESY spectrum.","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":20,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-20T15:57:34.048Z","reference_source":"pmid","term_name":"disorder","reference_id":"9923693","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":43,"region_id":"DP02206r002","released":"2024_06","ec_id":"ECO:0006165","reference_html":"Structure of human salivary histatin 5 in aqueous and nonaqueous solutions. <i> Raj PA, Marcus E, Sukumaran DK. </i> Biopolymers, 1998","statement":[{"text":"Col- lectively, the nmr data provide evidence that histatin 5 molecules are unstructured in aqueous solution.","type":"Results"},{"text":"Histatin 5 is a truncated form of Histatin 3.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":20,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-20T16:13:53.226Z","reference_source":"pmid","term_name":"disorder","reference_id":"9433185","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":43,"region_id":"DP02206r003","released":"2024_06","ec_id":"ECO:0006210","reference_html":"Coarse-grained modeling of the intrinsically disordered protein Histatin 5 in solution: Monte Carlo simulations in combination with SAXS. <i> Cragnell C, Durand D, Cabane B, Skepö M. </i> Proteins, 2016","statement":[{"text":"The plot enhances the large q region and reveals the flexibility/rigidity of the peptide. His5 shows a characteristic representation, typical for an IDP, indicated by the lack of a clear maximum in the curve. ","type":"Results"},{"text":"Histatin 5 is a truncated form of Histatin 3.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":20,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-20T16:21:14.095Z","reference_source":"pmid","term_name":"disorder","reference_id":"26914439","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":51,"region_id":"DP02206r004","released":"2024_06","ec_id":"ECO:0006204","reference_html":"NMR studies of the antimicrobial salivary peptides histatin 3 and histatin 5 in aqueous and nonaqueous solutions. <i> Brewer D, Hunter H, Lajoie G. </i> Biochem Cell Biol, 1998","statement":[{"text":"CD analysis of H3 indicated that H3 also has no well-defined secondary structure\nin aqueous solution at pH 7.4.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":20,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-20T15:56:25.889Z","reference_source":"pmid","term_name":"disorder","reference_id":"9923693","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":20,"end":43,"reference_id":"9433185","reference_source":"pmid","reference_html":"Structure of human salivary histatin 5 in aqueous and nonaqueous solutions. <i> Raj PA, Marcus E, Sukumaran DK. </i> Biopolymers, 1998","date":"2024-02-20T16:19:14.135Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02206r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"193041","entry_name":"dimethyl sulfoxide-d6"}],"statement":[{"text":"However, histatin 5 prefers largelya-helical confor- mation  in  polar  aprotic  ( CD3)2SO  solution  that mimics the membrane environment.","type":"Results"},{"text":"Histatin 5 is a truncated form of Histatin 3.","type":"Curator statement"}]}],"released":"2018_11","uniref100":"UniRef100_P15516","date":"2018-08-29T09:08:34.000Z","acc":"P15516","name":"Histatin-3","length":51,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000143497","genes":[{"name":{"value":"HTN3"},"synonyms":[{"value":"HIS2"}]}],"alphafold_very_low_content":0.0196078431372549,"disorder_content":0.6274509803921569,"disprot_consensus":{"full":[{"start":20,"end":43,"type":"T"},{"start":44,"end":51,"type":"D"}],"Structural state":[{"start":20,"end":51,"type":"D"}],"Structural transition":[{"start":20,"end":43,"type":"T"}]}},{"features":{"pfam":[{"id":"PF03875","name":"Statherin","start":20,"end":60}]},"uniref50":"UniRef50_P02808","sequence":"MKFLVFAFILALMVSMIGADSSEEKFLRRIGRFGYGYGPYQPVPEQPLYPQPYQPQYQQYTF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P02808","disprot_id":"DP02207","ncbi_taxon_id":9606,"regions_counter":1,"creator":"mlambrughi","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":62,"region_id":"DP02207r001","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Utilizing Coarse-Grained Modeling and Monte Carlo Simulations to Evaluate the Conformational Ensemble of Intrinsically Disordered Proteins and Regions. <i> Cragnell C, Rieloff E, Skepö M. </i> J Mol Biol, 2018","statement":[{"text":"Fig. 6a shows the dimensionless Kratky plot, and as clearly visible, the profiles from the experiment and the simulation agree very well and display a random coil behavior, that is, a linear rise to a plateau at higher scattering angles.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mlambrughi","start":20,"term_ontology":"IDPO","curator_name":"Matteo Lambrughi","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-0894-8627","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29573987","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P02808","date":"2018-08-29T09:49:00.000Z","acc":"P02808","name":"Statherin","length":62,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00001744FC","genes":[{"name":{"value":"STATH"}}],"alphafold_very_low_content":0.08064516129032258,"disorder_content":0.6935483870967742,"disprot_consensus":{"full":[{"start":20,"end":62,"type":"D"}],"Structural state":[{"start":20,"end":62,"type":"D"}]}},{"features":{"pfam":[{"id":"PF05363","name":"Herpesvirus US12 family","start":1,"end":82}]},"uniref50":"UniRef50_P03170","sequence":"MSWALEMADTFLDNMRVGPRTYADVRDEINKRGREDREAARTAVHDPERPLLRSPGLLPEIAPNASLGVVHRRTGGTVTDSPRNPVTR","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Peploviricota","Herviviricetes","Herpesvirales","Herpesviridae","Alphaherpesvirinae","Simplexvirus"],"uniref90":"UniRef90_P03170","disprot_id":"DP02208","ncbi_taxon_id":10298,"regions_counter":1,"creator":"ldobson","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":88,"region_id":"DP02208r001","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Structure of the transporter associated with antigen processing trapped by herpes simplex virus. <i> Oldham ML, Grigorieff N, Chen J. </i> Elife, 2016","statement":[{"text":"The N-terminal 55 residues of ICP47 form a helical hairpin structure, which inserts into the opening between the two TM bundles. No density was observed for either the C-terminal 33 residues of ICP47 or the two TMD0s, indicating these regions are flexible in this conformation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":56,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5U1D"}],"reference_id":"27935481","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-12T11:02:52.214Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_A0A140GKJ0","date":"2018-08-29T11:49:37.000Z","acc":"A0A140GKJ0","name":"TAP transporter inhibitor ICP47","length":88,"organism":"Human herpesvirus 1","dataset":["Viral proteins"],"UniParc":"UPI00078DA18E","genes":[{"name":{"value":"US12","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AMN09839.1","url":"https://www.ebi.ac.uk/ena/browser/view/AMN09839.1"}}]}}],"disorder_content":0.375,"disprot_consensus":{"full":[{"start":56,"end":88,"type":"D"}],"Structural state":[{"start":56,"end":88,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00847","name":"AP2 domain","start":78,"end":127}],"gene3D":[{"start":78,"end":137,"id":"3.30.730.10","name":"AP2/ERF domain"}]},"uniref50":"UniRef50_O82132","sequence":"MAVYDQSGDRNRTQIDTSRKRKSRSRGDGTTVAERLKRWKEYNETVEEVSTKKRKVPAKGSKKGCMKGKGGPENSRCSFRGVRQRIWGKWVAEIREPNRGSRLWLGTFPTAQEAASAYDEAAKAMYGPLARLNFPRSDASEVTSTSSQSEVCTVETPGCVHVKTEDPDCESKPFSGGVEPMYCLENGAEEMKRGVKADKHWLSEFEHNYWSDILKEKEKQKEQGIVETCQQQQQDSLSVADYGWPNDVDQSHLDSSDMFDVDELLRDLNGDDVFAGLNQDRYPGNSVANGSYRPESQQSGFDPLQSLNYGIPPFQLEGKDGNGFFDDLSYLDLEN","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_O82132","disprot_id":"DP02209","ncbi_taxon_id":3702,"regions_counter":20,"creator":"grivas","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":272,"region_id":"DP02209r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1. <i> O'Shea C, Staby L, Bendsen SK, Tidemand FG, Redsted A, Willemoës M, Kragelund BB, Skriver K. </i> J Biol Chem, 2017","statement":[{"text":"The 1H,15N HSQC spectrum of free DREB2A(255–272) showed limited dispersion in the proton dimension, indicating a lack of structure (Fig. 7A, black spectrum) (35). Consistent with this and with its far-UV CD spectrum (Fig. 6A), most residues have near-random coil secondary Cα chemical shifts (ΔδCα ≈0, Fig. 7D, top figure)","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jssuarez","start":255,"term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-9045-7765","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27881680","validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-13T15:45:01.905Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":272,"region_id":"DP02209r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1. <i> O'Shea C, Staby L, Bendsen SK, Tidemand FG, Redsted A, Willemoës M, Kragelund BB, Skriver K. </i> J Biol Chem, 2017","statement":[{"text":"Experimental analysis for secondary structure content by far-UV CD indicated low α-helical contents of 12, 18, 10, and 13% in the ANAC013(254–274), DREB2A(255–272), COL10(175–208), and bZIP23(15–36) peptides, respectively","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jssuarez","start":255,"term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-9045-7765","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"27881680","validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-13T15:45:26.790Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02209r003","validated":{"curator_id":"bmesza","timestamp":"2020-12-17T11:57:07.065Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":335,"term_id":"IDPO:0000002","start":168,"version":2,"statement":[{"text":"Using Far-UV CD, we found that the spectrum of the Dreb2a168–335 domain indicated a lack of secondary structure for this domain in solution. The negative maximum ∼200 nm implies an unstructured random coil conformation (Figure 1D).","type":"Results"}],"term_name":"disorder","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"22447446","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006204","curator_id":"jssuarez","reference_html":"Interactions between DNA, transcriptional regulator Dreb2a and the Med25 mediator subunit from Arabidopsis thaliana involve conformational changes. <i> Blomberg J, Aguilar X, Brännström K, Rautio L, Olofsson A, Wittung-Stafshede P, Björklund S. </i> Nucleic Acids Res, 2012","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02209r004","validated":{"curator_id":"bmesza","timestamp":"2020-12-17T12:03:24.510Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":335,"term_id":"GO:0005515","start":168,"version":3,"statement":[{"text":"We found that only the extended C-terminal domain, Dreb2a 168–335 which includes both the BD and the AD, interacted with Med25 551–680 with significant affinity. ","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q7XYY2","partner_end":null}],"term_name":"protein binding","ec_name":"surface plasmon resonance evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"GO","curator_name":"Jaime Santos Suárez","reference_id":"22447446","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001269","curator_id":"jssuarez","reference_html":"Interactions between DNA, transcriptional regulator Dreb2a and the Med25 mediator subunit from Arabidopsis thaliana involve conformational changes. <i> Blomberg J, Aguilar X, Brännström K, Rautio L, Olofsson A, Wittung-Stafshede P, Björklund S. </i> Nucleic Acids Res, 2012","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":255,"end":272,"reference_id":"27881680","reference_source":"pmid","reference_html":"Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1. <i> O'Shea C, Staby L, Bendsen SK, Tidemand FG, Redsted A, Willemoës M, Kragelund BB, Skriver K. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"Q8RY59","partner_start":null,"partner_end":null}],"region_id":"DP02209r006","statement":[{"text":"The spectrum of RCD1-RST(499–572) in complex with DREB2A(255–272) showed an absolute minimum shifted toward a higher wavelength compared with the theoretical spectrum. Moreover, the overall α-helical content in the complex was calculated to 39% compared with 31% in the theoretical complex. This indicated induction of structure upon complex formation (Fig. 6B).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-11-25T20:06:58.228Z"}},{"start":255,"end":272,"reference_id":"27881680","reference_source":"pmid","reference_html":"Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1. <i> O'Shea C, Staby L, Bendsen SK, Tidemand FG, Redsted A, Willemoës M, Kragelund BB, Skriver K. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP02209r007","statement":[{"text":"The spectrum of RCD1-RST(499–572) in complex with DREB2A(255–272) showed an absolute minimum shifted toward a higher wavelength compared with the theoretical spectrum. Moreover, the overall α-helical content in the complex was calculated to 39% compared with 31% in the theoretical complex. This indicated induction of structure upon complex formation (Fig. 6B).","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-13T15:50:18.517Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":255,"end":272,"reference_id":"27881680","reference_source":"pmid","reference_html":"Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1. <i> O'Shea C, Staby L, Bendsen SK, Tidemand FG, Redsted A, Willemoës M, Kragelund BB, Skriver K. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP02209r008","statement":[{"text":"The 1H,15N HSQC was dramatically changed upon addition of RCD1-RST(499–572) with a substantial increase in the 1H resonance dispersion (Fig. 7A, red spectrum). Furthermore, the Cα resonances for residues Val-261–Asp-267 experienced a significant downfield shift (ΔδCα >0), thus confirming the formation of an almost fully formed helical structure in this region (Fig. 7D, bottom figure) (34). Notably, the HSQC as well as the different triple resonance spectra lacked peaks for Phe-259 and Asp-260. This is consistent with the abolished binding of the F259A mutant (Fig. 2D; Table 3) and suggests that these residues are involved in the interaction.","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-13T15:50:03.381Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":255,"end":272,"reference_id":"27881680","reference_source":"pmid","reference_html":"Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1. <i> O'Shea C, Staby L, Bendsen SK, Tidemand FG, Redsted A, Willemoës M, Kragelund BB, Skriver K. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP02209r009","statement":[{"text":"The 1H,15N HSQC was dramatically changed upon addition of RCD1-RST(499–572) with a substantial increase in the 1H resonance dispersion (Fig. 7A, red spectrum). Furthermore, the Cα resonances for residues Val-261–Asp-267 experienced a significant downfield shift (ΔδCα >0), thus confirming the formation of an almost fully formed helical structure in this region (Fig. 7D, bottom figure) (34). Notably, the HSQC as well as the different triple resonance spectra lacked peaks for Phe-259 and Asp-260. This is consistent with the abolished binding of the F259A mutant (Fig. 2D; Table 3) and suggests that these residues are involved in the interaction.","type":"Results"}],"interaction_partner":[{"db":"UniProt","id":"Q8RY59","partner_start":null,"partner_end":null}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-11-26T13:13:49.790Z"}},{"start":255,"end":272,"reference_id":"27881680","reference_source":"pmid","reference_html":"Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1. <i> O'Shea C, Staby L, Bendsen SK, Tidemand FG, Redsted A, Willemoës M, Kragelund BB, Skriver K. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"Q8RY59","partner_start":null,"partner_end":null}],"region_id":"DP02209r010","statement":[{"text":"The affinity of the interaction between RCD1-RST(499–572) and a short peptide of DREB2A, DREB2A(255–272), containing a predicted α-helix, was significantly lower, corresponding to a Kd of 117 nm, but with a large enthalpic contribution to binding of −51 kJ/mol (Fig. 2C).","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-13T15:51:40.702Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":259,"end":270,"reference_id":"29657132","reference_source":"pmid","reference_html":"Structure of Radical-Induced Cell Death1 Hub Domain Reveals a Common αα-Scaffold for Disorder in Transcriptional Networks. <i> Bugge K, Staby L, Kemplen KR, O'Shea C, Bendsen SK, Jensen MK, Olsen JG, Skriver K, Kragelund BB. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"BMRB","id":"34152"},{"db":"PDB","id":"5OAP"}],"region_id":"DP02209r011","statement":[{"text":"When bound to RCD1-RST, DREB2A255-272 formed an a helix from V261-G270, with D260 forming an N-cap supported by the interaction between the residues in the N0-(F259) and N4-(L264) positions of the hydrophobic staple motif (Munoz et al., 1995) (Figure 2F).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-15T13:27:07.103Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":259,"end":270,"reference_id":"29657132","reference_source":"pmid","reference_html":"Structure of Radical-Induced Cell Death1 Hub Domain Reveals a Common αα-Scaffold for Disorder in Transcriptional Networks. <i> Bugge K, Staby L, Kemplen KR, O'Shea C, Bendsen SK, Jensen MK, Olsen JG, Skriver K, Kragelund BB. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"BMRB","id":"34152"},{"db":"PDB","id":"5OAP"}],"interaction_partner":[{"db":"UniProt","id":"Q8RY59","partner_start":null,"partner_end":null}],"region_id":"DP02209r012","statement":[{"text":"The structure of bound DREB2A255-272 was solved using NMR data acquired with only DREB2A isotope labeled.","type":"Results"},{"text":"When bound to RCD1-RST, DREB2A255-272 formed an a helix from V261-G270, with D260 forming an N-cap supported by the interaction between the residues in the N0-(F259) and N4-(L264) positions of the hydrophobic staple motif (Munoz et al., 1995) (Figure 2F).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-15T13:27:13.065Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":234,"end":276,"reference_id":"34473923","reference_source":"pmid","reference_html":"Quantification of Conformational Entropy Unravels Effect of Disordered Flanking Region in Coupled Folding and Binding. <i> Theisen FF, Staby L, Tidemand FG, O'Shea C, Prestel A, Willemoës M, Kragelund BB, Skriver K. </i> J Am Chem Soc, 2021","date":"2026-06-25T15:57:19.872Z","curator_id":"grivas","curator_name":"Gabriel Alejandro Rivas","curator_orcid":"0000-0001-9987-3159","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP02209r013","statement":[{"text":"(A) Unbound DREB2A234–276 conformational ensemble.","type":"Figure"},{"text":"In the 1H-15N-HSQC spectra in BMRB, shows the backbone amide resonances fall between 8.5 and 7.8 p.p.m. The lack of chemical shift dispersion reflect the intrinsic mobility of this region.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sequence_construct":"GQDSLSVADYGWPNDVDQSHLDSSDMEDVDELLRDLNGDDVFAG","cross_refs":[{"db":"BMRB","id":"51055"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-25T15:57:28.412Z"}},{"start":257,"end":270,"reference_id":"34473923","reference_source":"pmid","reference_html":"Quantification of Conformational Entropy Unravels Effect of Disordered Flanking Region in Coupled Folding and Binding. <i> Theisen FF, Staby L, Tidemand FG, O'Shea C, Prestel A, Willemoës M, Kragelund BB, Skriver K. </i> J Am Chem Soc, 2021","date":"2026-06-25T15:59:46.479Z","curator_id":"grivas","curator_name":"Gabriel Alejandro Rivas","curator_orcid":"0000-0001-9987-3159","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"BMRB","id":"51056"}],"region_id":"DP02209r015","sequence_construct":"GQDSLSVADYGWPNDVDQSHLDSSDMEDVDELLRDLNGDDVFAG","statement":[{"text":"Analysis of chemical shifts of the bound state of DREB2A using the motif identification from chemical shifts (MICS) server (42) returned a high probability that residue D260 functions as an Ncap of the V261–G270 α-helix (Figure S6F).","type":"Results"},{"text":"DREB2A backbone CSPs upon binding were dominated by residues D257−G270, which are the residues that are buried in the binding groove of RCD1-RST","type":"Results"},{"text":"In addition, secondary chemical shifts of residues D257–D260 indicated formation of previously unidentified, highly populated extended structure in the complex.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8RY59","statements":[{"type":"Results","text":"DREB2A backbone CSPs upon binding were dominated by residues D257-G270, which are the residues that are buried in the binding groove of RCD1-RST."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-25T16:00:25.923Z"}},{"start":257,"end":270,"reference_id":"34473923","reference_source":"pmid","reference_html":"Quantification of Conformational Entropy Unravels Effect of Disordered Flanking Region in Coupled Folding and Binding. <i> Theisen FF, Staby L, Tidemand FG, O'Shea C, Prestel A, Willemoës M, Kragelund BB, Skriver K. </i> J Am Chem Soc, 2021","date":"2026-06-25T16:00:19.277Z","curator_id":"grivas","curator_name":"Gabriel Alejandro Rivas","curator_orcid":"0000-0001-9987-3159","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"region_id":"DP02209r016","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8RY59","statements":[{"type":"Results","text":"DREB2A backbone CSPs upon binding were dominated by residues D257-G270, which are the residues that are buried in the binding groove of RCD1-RST."}]}],"sequence_construct":"GQDSLSVADYGWPNDVDQSHLDSSDMEDVDELLRDLNGDDVFAG","statement":[{"text":"DREB2A backbone CSPs upon binding (Figure5A and B) were dominated by residues D257–G270, which are the residues that are buried in the binding groove of RCD1-RST.","type":"Results"},{"text":"In addition, secondary chemical shifts of residues D257–D260 indicated formation of previously unidentified, highly populated extended structure in the complex.","type":"Results"},{"text":"Analysis of chemical shifts of the bound state of DREB2A using the motif identification from chemical shifts (MICS) server (42) returned a high probability that residue D260 functions as an Ncap of the V261–G270 α-helix (Figure S6F).","type":"Results"}],"states_connection":[{"source":"DP02209r013","target":"DP02209r015"}],"cross_refs":[{"db":"BMRB","id":"51056"},{"db":"BMRB","id":"51055"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-25T16:00:22.191Z"}},{"start":243,"end":272,"reference_id":"34473923","reference_source":"pmid","reference_html":"Quantification of Conformational Entropy Unravels Effect of Disordered Flanking Region in Coupled Folding and Binding. <i> Theisen FF, Staby L, Tidemand FG, O'Shea C, Prestel A, Willemoës M, Kragelund BB, Skriver K. </i> J Am Chem Soc, 2021","date":"2026-06-25T15:30:48.677Z","curator_id":"grivas","curator_name":"Gabriel Alejandro Rivas","curator_orcid":"0000-0001-9987-3159","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q8RY59","operator":null,"partner_start":499,"partner_end":572}],"region_id":"DP02209r017","statement":[{"text":"This suggested that the G243-D272 region represents the full RCD1-binding region.","type":"Results"},{"text":"This further supported the entire 243–272 region of DREB2A being involved in RCD1 binding.","type":"Results"},{"text":"Examining the affinities, only the N-terminal extension from the SLiM affected the affinity significantly, with DREB2A243–272 and DREB2A234–287 displaying the strongest binding, both in the low nM regime.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sequence_construct":"GGWPNDVDQSHLDSSDMEDVDELLRDLNGDD","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-25T15:31:11.057Z"}},{"start":257,"end":270,"reference_id":"27881680","reference_source":"pmid","reference_html":"Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1. <i> O'Shea C, Staby L, Bendsen SK, Tidemand FG, Redsted A, Willemoës M, Kragelund BB, Skriver K. </i> J Biol Chem, 2017","date":"2026-06-25T15:48:53.049Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0001221","term_name":"transcription coregulator binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"BMRB","id":"51056"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q8RY59","operator":null,"partner_start":499,"partner_end":572}],"region_id":"DP02209r020","statement":[{"text":"DREB2A backbone CSPs upon binding (Figure5A and B) were dominated by residues D257–G270, which are the residues that are buried in the binding groove of RCD1-RST.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a transcription coregulator, a protein involved in regulation of transcription via protein-protein interactions with transcription factors and other transcription regulatory proteins. Cofactors do not bind DNA directly, but rather mediate protein-protein interactions between regulatory transcription factors and the basal transcription machinery.\" [GOC:krc]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_O82132","date":"2018-08-29T12:01:17.000Z","acc":"O82132","name":"Dehydration-responsive element-binding protein 2A","length":335,"organism":"Arabidopsis thaliana","dataset":["Stress response proteins"],"UniParc":"UPI00000A36B6","genes":[{"name":{"value":"DREB2A","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10809011","url":"http://www.ncbi.nlm.nih.gov/pubmed/10809011","alternativeUrl":"https://europepmc.org/abstract/MED/10809011"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"9707537","url":"http://www.ncbi.nlm.nih.gov/pubmed/9707537","alternativeUrl":"https://europepmc.org/abstract/MED/9707537"}}]},"synonyms":[{"value":"ERF045","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16407444","url":"http://www.ncbi.nlm.nih.gov/pubmed/16407444","alternativeUrl":"https://europepmc.org/abstract/MED/16407444"}}]}],"orfNames":[{"value":"K18I23.22","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"BAB09984.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAB09984.1"}}]}],"olnNames":[{"value":"At5g05410","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT5G05410","url":""}}]}]}],"alphafold_very_low_content":0.208955223880597,"disorder_content":0.5014925373134328,"disprot_consensus":{"full":[{"start":168,"end":254,"type":"D"},{"start":255,"end":272,"type":"T"},{"start":273,"end":335,"type":"D"}],"Structural state":[{"start":168,"end":335,"type":"D"}],"Molecular function":[{"start":168,"end":335,"type":"F"}],"Structural transition":[{"start":255,"end":272,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00005","name":"ABC transporter","start":486,"end":635},{"id":"PF00664","name":"ABC transporter transmembrane region","start":153,"end":416}],"gene3D":[{"start":135,"end":458,"id":"1.20.1560.10","name":"ABC transporter type 1, transmembrane domain"},{"start":459,"end":685,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_Q03519","sequence":"MRLPDLRPWTSLLLVDAALLWLLQGPLGTLLPQGLPGLWLEGTLRLGGLWGLLKLRGLLGFVGTLLLPLCLATPLTVSLRALVAGASRAPPARVASAPWSWLLVGYGAAGLSWSLWAVLSPPGAQEKEQDQVNNKVLMWRLLKLSRPDLPLLVAAFFFLVLAVLGETLIPHYSGRVIDILGGDFDPHAFASAIFFMCLFSFGSSLSAGCRGGCFTYTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLVRRVLHLGVQMLMLSCGLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKVFSYMDRQPNLPSPGTLAPTTLQGVVKFQDVSFAYPNRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQCEQALQDWNSRGDRTVLVIAHRLQTVQRAHQILVLQEGKLQKLAQL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q03519","disprot_id":"DP02210","ncbi_taxon_id":9606,"regions_counter":1,"creator":"rdavidovic","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":129,"region_id":"DP02210r001","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Structure of the transporter associated with antigen processing trapped by herpes simplex virus. <i> Oldham ML, Grigorieff N, Chen J. </i> Elife, 2016","statement":[{"text":"No density was observed for either the C-terminal 33 residues of ICP47 or the two TMD0s, indicating these regions are flexible in this conformation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":1,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5U1D"}],"reference_id":"27935481","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q03519","date":"2018-08-29T12:02:45.000Z","acc":"Q03519","name":"Antigen peptide transporter 2","length":686,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000011D578","genes":[{"name":{"value":"TAP2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10605026","url":"http://www.ncbi.nlm.nih.gov/pubmed/10605026","alternativeUrl":"https://europepmc.org/abstract/MED/10605026"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:44","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:44"}}]},"synonyms":[{"value":"ABCB3"},{"value":"PSF2"},{"value":"RING11"},{"value":"Y1"}]}],"alphafold_very_low_content":0.029154518950437316,"disorder_content":0.1880466472303207,"disprot_consensus":{"full":[{"start":1,"end":129,"type":"D"}],"Structural state":[{"start":1,"end":129,"type":"D"}]}},{"acc":"P05769","sequence":"MSKKPGGPGKPRVVNMLKRGIPRVFPLVGVKRVVMNLLDGRGPIRFVLALLAFFRFTALAPTKALMRRWKSVNKTTAMKHLTSFKKELGTLIDVVNKRGKKQKKRGGSETSVLMLIFMLIGFAAALKLSTFQGKIMMTVNATDIADVIAIPTPKGPNQCWIRAIDIGFMCDDTITYECPKLESGNDPEDIDCWCDKQAVYVNYGRCTRARHSKRSRRSITVQTHGESTLVNKKDAWLDSTKATRYLTKTENWIIRNPGYALVAVVLGWMLGSNTGQKVIFTVLLLLVAPAYSFNCLGMSSRDFIEGASGATWVDLVLEGDSCITIMAADKPTLDIRMMNIEATNLALVRNYCYAATVSDVSTVSNCPTTGESHNTKRADHNYLCKRGVTDRGWGNGCGLFGKGSIDTCAKFTCSNSAAGRLILPEDIKYEVGVFVHGSTDSTSHGNYSTQIGANQAVRFTISPNAPAITAKMGDYGEVTVECEPRSGLNTEAYYVMTIGTKHFLVHREWFNDLLLPWTSPASTEWRNREILVEFEEPHATKQSVVALGSQEGALHQALAGAIPVEFSSSTLKLTSGHLKCRVKMEKLKLKGTTYGMCTEKFTFSKNPADTGHGTVVLELQYTGSDGPCKIPISSVASLNDMTPVGRMVTANPYVASSTANAKVLVEIEPPFGDSYIVVGRGDKQINHHWHKEGSSIGKAFSTTLKGAQRLAALGDTAWDFGSVGGVFNSIGKAVHQVFGGAFRTLFGGMSWISPGLLGALLLWMGVNARDKSIALAFLATGGVLLFLATNVHADTGCAIDITRRELKCGSGIFIHNDVEAWIDRYKYLPETPKQLAKVVENAHKSGICGIRSVNRFEHQMWESVRDELNALLKENAIDLSVVVEKQKGMYRAAPNRLRLTVEELDIGWKAWGKSLLFAAELANSTFVVDGPETAECPNSKRAWNSFEIEDFGFGITSTRGWLKLREENTSECDSTIIGTAVKGNHAVHSDLSYWIESGLNGTWKLERAIFGEVKSCTWPETHTLWGDAVEETELIIPVTLAGPRSKHNRREGYKVQVQGPWDEEDIKLDFDYCPGTTVTVSEHCGKRGPSVRTTTDSGKLVTDWCCRSCTLPPLRFTTASGCWYGMEIRPMKHDESTLVKSRVQAFNGDMIDPFQLGLLVMFLATQEVLRKRWTARLTLPAAVGALLVLLLGGITYTDLVRYLILVGSAFAESNNGGDVIHLALIAVFKVQPAFLVASLTRSRWTNQENLVLVLGAAFFQMAASDLELTIPGLLNSAATAWMVLRAMAFPSTSAIAMPMLAMLAPGMRMLHLDTYRIVLLLIGICSLLNERRRSVEKKKGAVLIGLALTSTGYFSPTIMAAGLMICNPNKKRGWPATEVLTAVGLMFAIVGGLAELDIDSMSVPFTIAGLMLVSYVISGKATDMWLERAADVSWEAGAAITGTSERLDVQLDDDGDFHLLNDPGVPWKIWVLRMTCLSVAAITPRAILPSAFGYWLTLKYTKRGGVFWDTPSPKVYPKGDTTPGVYRIMARGILGRYQAGVGVMHEGVFHTLWHTTRGAAIMSGEGRLTPYWGNVKEDRVTYGGPWKLDQKWNGVDDVQMIVVEPGKPAINVQTKPGIFKTAHGEIGAVSLDYPIGTSGSPIVNSNGEIIGLYGNGVILGNGAYVSAIVQGERVEEPVPEAYNPEMLKKRQLTVLDLHPGAGKTRRILPQIIKDAIQKRLRTAVLAPTRVVAAEMAEALRGLPVRYLTPAVQREHSGNEIVDVMCHATLTHRLMSPLRVPNYNLFVMDEAHFTDPASIAARGYIATRVEAGEAAAIFMTATPPGTSDPFPDTNSPVHDVSSEIPDRAWSSGFEWITDYAGKTVWFVASVKMSNEIAQCLQRAGKRVIQLNRKSYDTEYPKCKNGDWDFVITTDISEMGANFGASRVIDCRKSVKPTILDEGEGRVILSVPSAITSASAAQRRGRVGRNPSQIGDEYHYGGGTSEDDTMLAHWTEAKILLDNIHLPNGLVAQLYGPERDKTYTMDGEYRLRGEERKTFLELIKTADLPVWLAYKVASNGIQYNDRKWCFDGPRSNIILEDNNEVEIITRIGERKVLKPRWLDARVYSDHQSLKWFKDFAAGKRSAIGFFEVLGRMPEHFAGKTREALDTMYLVATSEKGGKAHRMALEELPDALETITLIAALGVMTAGFFLLMMQRKGIGKLGLGALVLVVATFFLWMSDVSGTKIAGVLLLALLMMVVLIPEPEKQRSQTDNQLAVFLICVLLVVGLVAANEYGMLERTKTDIRNLFGKSLIEENEVHIPPFDFFTLDLKPATAWALYGGSTVVLTPLIKHLVTSQYVTTSLASINAQAGSLFTLPKGIPFTDFDLSVALVFLGCWGQVTLTTLIMATILVTLHYGYLLPGWQAEALRAAQKRTAAGIMKNAVVDGIVATDVPELERTTPQMQKRLGQILLVLASVAAVCVNPRITTIREAGILCTAAALTLWDNNASAAWNSTTATGLCHVMRGSWIAGASIAWTLIKNAEKPAFKRGRAGGRTLGEQWKEKLNAMGKEEFFSYRKEAILEVDRTEARRARREGNKVGGHPVSRGTAKLRWLVERRFVQPIGKVVDLGCGRGGWSYYAATMKNVQEVRGYTKGGPGHEEPMLMQSYGWNIVTMKSGVDVFYKPSEISDTLLCDIGESSPSAEIEEQRTLRILEMVSDWLSRGPKEFCIKILCPYMPKVIEKLESLQRRFGGGLVRVPLSRNSNHEMYWVSGASGNIVHAVNMTSQVLIGRMDKKIWKGPKYEEDVNLGSGTRAVGKGVQHTDYKRIKSRIEKLKEEYAATWHTDDNHPYRTWTYHGSYEVKPSGSASTLVNGVVRLLSKPWDAITGVTTMAMTDTTPFGQQRVFKEKVDTKAPEPPQGVKTVMDETTNWLWAYLARNKKARLCTREEFVKKVNSHAALGAMFEEQNQWKNAREAVEDPKFWEMVDEERECHLRGECRTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARFLEFEALGFLNEDHWMSRENSGGGVEGAGIQKLGYILRDVAQKPGGKIYADDTAGWDTRITQADLENEAKVLELMEGEQRTLARAIIELTYRHKVVKVMRPAAGGKTVMDVISREDQRGSGQVVTYALNTFTNIAVQLVRLMEAEAVIGPDDIESIERKKKFAVRTWLFENAEERVQRMAVSGDDCVVKPLDDRFSTALHFLNAMSKVRKDIQEWKPSQGWYDWQQVPFCSNHFQEVIMKDGRTLVVPCRGQDELIGRARISPGSGWNVRDTACLAKAYAQMWLVLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLSVWNRVWILENEWMEDKTTVSDWTEVPYVGKREDIWCGSLIGTRTRATWAENIYAAINQVRSVIGKEKYVDYVQSLRRYEETHVSEDRVL","creator":"lchemes","dataset":["Viral proteins","RNA-binding proteins"],"date":"2018-08-29T12:40:55.000Z","disprot_id":"DP02212","features":{"pfam":[{"id":"PF00869","name":"Flavivirus glycoprotein, central and dimerisation domains","start":295,"end":591},{"id":"PF00948","name":"Flavivirus non-structural Protein NS1","start":796,"end":1145},{"id":"PF00949","name":"Peptidase S7, Flavivirus NS3 serine protease","start":1521,"end":1670},{"id":"PF00972","name":"Flavivirus RNA-directed RNA polymerase, fingers and palm domains","start":2782,"end":3234},{"id":"PF01002","name":"Flavivirus non-structural protein NS2B","start":1378,"end":1502},{"id":"PF01003","name":"Flavivirus capsid protein C","start":7,"end":119},{"id":"PF01004","name":"Flavivirus envelope glycoprotein M","start":219,"end":292},{"id":"PF01005","name":"Flavivirus non-structural protein NS2A","start":1157,"end":1262},{"id":"PF01349","name":"Flavivirus non-structural protein NS4B","start":2272,"end":2520},{"id":"PF01350","name":"Flavivirus non-structural protein NS4A","start":2130,"end":2267},{"id":"PF01570","name":"Flavivirus polyprotein propeptide","start":135,"end":216},{"id":"PF01728","name":"FtsJ-like methyltransferase","start":2584,"end":2752},{"id":"PF02832","name":"Flavivirus glycoprotein, immunoglobulin-like domain","start":594,"end":691},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1688,"end":1833},{"id":"PF20483","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","start":3238,"end":3400},{"id":"PF20907","name":"Flavivirus NS3 helicase, C-terminal helical domain","start":1978,"end":2120},{"id":"PF21659","name":"Flavivirus envelope glycoprotein E, stem/anchor domain","start":694,"end":788}],"gene3D":[{"start":126,"end":207,"id":"2.60.260.50","name":"Flavivirus polyprotein propeptide domain","_id":"685af523b4ac24d5329d9410"},{"start":23,"end":98,"id":"1.10.10.930","name":"1.10.10.930","_id":"685af523b4ac24d5329d9411"},{"start":293,"end":587,"id":"2.60.98.10","name":"Tick-borne Encephalitis virus Glycoprotein, domain 1","_id":"685af523b4ac24d5329d9412"},{"start":218,"end":292,"id":"1.10.8.970","name":"Flavivirus envelope glycoprotein M-like","_id":"685af523b4ac24d5329d9413"},{"start":695,"end":793,"id":"1.20.1280.260","name":"1.20.1280.260","_id":"685af523b4ac24d5329d9414"},{"start":588,"end":694,"id":"2.60.40.350","name":"2.60.40.350","_id":"685af523b4ac24d5329d9415"},{"start":1687,"end":2020,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d9416"},{"start":3061,"end":3128,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d9417"},{"start":1590,"end":1672,"id":"2.40.10.10","name":"Trypsin-like serine proteases","_id":"685af523b4ac24d5329d9418"},{"start":2925,"end":3020,"id":"1.10.260.90","name":"1.10.260.90","_id":"685af523b4ac24d5329d9419"},{"start":2803,"end":2870,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d941a"},{"start":1417,"end":1465,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d941b"},{"start":1826,"end":1985,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases","_id":"685af523b4ac24d5329d941c"},{"start":2529,"end":2802,"id":"3.40.50.150","name":"Vaccinia Virus protein VP39","_id":"685af523b4ac24d5329d941d"},{"start":1516,"end":1589,"id":"2.40.10.120","name":"2.40.10.120","_id":"685af523b4ac24d5329d941e"},{"start":2871,"end":2909,"id":"3.30.70.2840","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","_id":"685af523b4ac24d5329d941f"}]},"genes":[],"length":3434,"name":"Genome polyprotein","ncbi_taxon_id":301478,"organism":"Murray valley encephalitis virus (strain MVE-1-51)","regions_counter":4,"released":"2018_11","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Flavivirus","Murray Valley encephalitis virus"],"UniParc":"UPI0000131E50","uniref100":"UniRef100_P05769","uniref50":"UniRef50_P17763","uniref90":"UniRef90_P05769","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2WV9","_id":"685af523b4ac24d5329d9422"}],"curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1442,"end":1465,"interaction_partner":[],"reference_html":"Crystal structure of a novel conformational state of the flavivirus NS3 protein: implications for polyprotein processing and viral replication. <i> Assenberg R, Mastrangelo E, Walter TS, Verma A, Milani M, Owens RJ, Stuart DI, Grimes JM, Mancini EJ. </i> J Virol, 2009","reference_id":"19793813","region_id":"DP02212r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As observed for the DENV NS2B-NS3pro structure, in the absence of a substrate, the MVEV NS2B region beyond residue 69 is disordered. Upon the addition of a substrate, the C-terminal part of NS2B undergoes a dramatic conformational change, wrapping around the C-terminal barrel and forming a stabilizing β hairpin that inserts into the active site (2, 19, 47).","_id":"685af523b4ac24d5329d9421"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-04T08:22:40.736Z","_id":"685af523b4ac24d5329d9423"},"version":2,"_id":"685af523b4ac24d5329d9420","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2WV9","_id":"685af523b4ac24d5329d9428"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1504,"end":1520,"interaction_partner":[],"reference_html":"Crystal structure of a novel conformational state of the flavivirus NS3 protein: implications for polyprotein processing and viral replication. <i> Assenberg R, Mastrangelo E, Walter TS, Verma A, Milani M, Owens RJ, Stuart DI, Grimes JM, Mancini EJ. </i> J Virol, 2009","reference_id":"19793813","region_id":"DP02212r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Regarding electron density, a total number of 580 out of 618 residues of full-length NS3 are well defined, together with 21 residues out of 45 of NS2B45. The 9 residues of the nonapeptide linker, 24 residues at the C terminus of the NS2B cofactor, 18 residues at the N terminus of the protease domain, and 7 residues in the linker region between protease and helicase are missing from the refined model.","_id":"685af523b4ac24d5329d9429"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-04T08:22:39.661Z","_id":"685af523b4ac24d5329d942a"},"version":1,"_id":"685af523b4ac24d5329d9427","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2WV9","_id":"685af523b4ac24d5329d942c"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":2085,"end":2095,"interaction_partner":[],"reference_html":"Crystal structure of a novel conformational state of the flavivirus NS3 protein: implications for polyprotein processing and viral replication. <i> Assenberg R, Mastrangelo E, Walter TS, Verma A, Milani M, Owens RJ, Stuart DI, Grimes JM, Mancini EJ. </i> J Virol, 2009","reference_id":"19793813","region_id":"DP02212r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The PDB shows disorder in the NS3 region 2085-2095 .","_id":"685af523b4ac24d5329d942d"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-04T08:12:16.837Z","_id":"685af523b4ac24d5329d942e"},"version":1,"_id":"685af523b4ac24d5329d942b","reference_source":"pmid"}],"__v":0,"disorder_content":0.015142690739662202,"disprot_consensus":{"full":[{"start":1442,"end":1465,"type":"D"},{"start":1504,"end":1520,"type":"D"},{"start":2085,"end":2095,"type":"D"}],"Structural state":[{"start":1442,"end":1465,"type":"D"},{"start":1504,"end":1520,"type":"D"},{"start":2085,"end":2095,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00245","name":"Alkaline phosphatase","start":22,"end":500}],"gene3D":[{"start":458,"end":521,"id":"3.40.720.10","name":"Alkaline Phosphatase, subunit A"},{"start":384,"end":441,"id":"1.10.1200.140","name":"Alkaline phosphatase, crown domain"},{"start":20,"end":373,"id":"3.40.720.10","name":"Alkaline Phosphatase, subunit A"}]},"uniref50":"UniRef50_A0A1E3WM23","sequence":"MKPIVTAVVTSTLSFNVLSAEIKNVILMIGDGMGPQQVGLLETYANQAPNSIYKGNKTAIYQLAQEGVIGSSLTHPEDAIVVDSACSATMLATGIYSSSEVIGIDSQGNHVETVLEKAKKAGKATGLVSDTRLTHATPASFAAHQPHRSLENQIASDMLATGADVMLSGGLRHWIPKSTNDKGETYKQLEKLTQGDVYLKSKRKDDRNLLTEAEKDGYQLAFNRNMLDDAKGDKLLGLFAYSGMDDGIAYSNKKKSGERTQPSLKEMTQKALNILSKDEDGFFLMVEGGQIDWAGHSNDAGTMLHELLKFDEAIQTVYEWAKDREDTIVIVTADHETGSFGFSYSSNDLPKPQKRSGEAFADRDYAPNFNFGAFDILDGLYNQKQSYYGMISEFQKLDKSLQTPEKLAEIVNKNSEFPITAEQAKNVLASKPNPYRLAQHKYLSAEEVPAINDFDAFFPYNDRGNLLAREQATGQNIVWGTGTHTHTPVNVFAWGPAEKILPVSKIMHHSELGEYIKQQVN","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Vibrionales","Vibrionaceae","Vibrio"],"uniref90":"UniRef90_A0A2G4B473","disprot_id":"DP02215","ncbi_taxon_id":169049,"regions_counter":2,"creator":"baykac","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":427,"region_id":"DP02215r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The 1.4 A crystal structure of the large and cold-active Vibrio sp. alkaline phosphatase. <i> Helland R, Larsen RL, Asgeirsson B. </i> Biochim Biophys Acta, 2009","term_id":"IDPO:0000002","curator_id":"baykac","start":414,"term_ontology":"IDPO","curator_name":"Burcu Aykac-Fas","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-3842-731X","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3E2D"}],"reference_id":"18977465","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":444,"region_id":"DP02215r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The 1.4 A crystal structure of the large and cold-active Vibrio sp. alkaline phosphatase. <i> Helland R, Larsen RL, Asgeirsson B. </i> Biochim Biophys Acta, 2009","term_id":"IDPO:0000002","curator_id":"baykac","start":431,"term_ontology":"IDPO","curator_name":"Burcu Aykac-Fas","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-3842-731X","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3E2D"}],"reference_id":"18977465","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q93P54","date":"2018-08-29T13:33:17.000Z","acc":"Q93P54","name":"Alkaline phosphatase","length":521,"organism":"Vibrio sp. G15-21","dataset":[],"UniParc":"UPI00000AFD99","genes":[],"alphafold_very_low_content":0.03262955854126679,"disorder_content":0.053742802303262956,"disprot_consensus":{"full":[{"start":414,"end":427,"type":"D"},{"start":431,"end":444,"type":"D"}],"Structural state":[{"start":414,"end":427,"type":"D"},{"start":431,"end":444,"type":"D"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_O62011","sequence":"MSESDDDYPELDISDQYIDPLGIVVGPPPASYTETDREETPMQNRTEDDTNSYGNSSGEHDYDSYLDSGDDDFDVDAYYANDNMDEPPPETIPDNLIQNVIGRNDNADYDFSDASNPEIMKLFLSSSLLSNPLKFRSGYSSDELDDCLKSCMGYSLQVTAVLLLPPEIISQLPNDSKTEHAHALVRGGWLQSKEGAFFPVISDSERETVVSLMNGSEEQHKRQERKKKEADTFESEEKEIRTLLTFNMIAELLMAVRNEYSIRSVKYQILSTAYTNMVTGAAHANIFRKYKDILQLDPEKLWNNDWFKEYTNRGTLKKFLTTARFSEIVVSQANGKTVELYFRADDEGNRPVVLFTDEHIADVRNKWKTGNQRNQNYGSQGNYRAGGQRSDDRRGPQQRRNVIVPDPNYQPSTFAGGISNNADDDGSLQPTTSSHFNRNTDRSTSRPPRAPTSPVNRVMETDPLMGQGTSSGAPQRSAIPNPFGGAPALSRSTITNGNRGPSYGDRGERVQDVGDTTSDSEITSEGSYSDEDPEQKEIKRQRRKDKLKKKQERELRSREKHTKSKQQPPSKIETRFNTYKKKSESSATDTSNTPPVDTVNVALPTPVVESSSTTAAPSIPVSTRPEVVVPPENPAPLREVGNFYSKSNHDEDRRNVQLPFTPADTHKPIKVAPKEPVRNPLLKERPSANGFINRRLPSHPAPPPVNQSQPANQPMQTAVYQNSHPGAPYIPQQPTYQPQLPVQQPQPHQYAPQPIHHQQPIHQPMHGQQYPPVNQQQPIYQQPAPQYPPYNSIQNNPQHGPSPFNYSQVPQPAYNHVGQQPSHMSNQPHINQNGYQNSYNPNQGPTSSDPNYGCNPQFNHYGSRSVYHEDHSSQRRRSPDQFPPNPPEYDPHGNFKLADYERDRMTVGYSQNPHQFDHHGSHMPHQSQPQGYDNFNGNSAPYFNKNGGQSNHQPEAQRSFSVLSSNRQPSNRELIFQDGIEKELRDIILRYRSMNLTVLTVQELRTEVSRRPAIPRYIDIVQYIRDSSSVAIVERGDIEPYVVLKDDIRN","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"uniref90":"UniRef90_O62011","disprot_id":"DP02216","ncbi_taxon_id":6239,"regions_counter":11,"creator":"baykac","regions":[{"start":1,"end":100,"reference_id":"30036386","reference_source":"pmid","reference_html":"Distinct regions of the intrinsically disordered protein MUT-16 mediate assembly of a small RNA amplification complex and promote phase separation of Mutator foci. <i> Uebel CJ, Uebel CJ, Anderson DC, Mandarino LM, Manage KI, Aynaszyan S, Phillips CM. </i> PLoS Genet, 2018","date":"2024-03-20T16:36:20.901Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02216r003","statement":[{"text":"MUT-16 has a short IDR near the N-terminus (first ~100 amino acids) and a much longer IDR comprising approximately 60% of the protein (Fig 1A). In total, more than 70% of the protein is predicted to be unstructured.","type":"Results"},{"text":"We also observed that the MUT-16 protein is highly prone to degradation during the immunoprecipitation procedure. While full-length MUT-16 could be observed in most lanes, we also could detect multiple degradation products, with a prominent product of ~70kD in most lanes (S5 Fig). We did not observe substantial degradation with other proteins we worked with and suspect the highly disordered nature of MUT-16 may leave it more exposed to proteases during the immunoprecipitation procedure.","type":"Results"},{"text":"This region is ~70% disordered, but contains the structured L region that is also key to the formation of Mutator foci.","type":"Results"},{"text":"The IUPred analysis in combination to the high degree of degradation highlight the flexibility and high solvent exposure of the protein. The curator resorted to the deletion experiments and to MobiDB for further structural information to determine the IDRs boundaries.","type":"Curator statement"}]},{"start":366,"end":946,"reference_id":"30036386","reference_source":"pmid","reference_html":"Distinct regions of the intrinsically disordered protein MUT-16 mediate assembly of a small RNA amplification complex and promote phase separation of Mutator foci. <i> Uebel CJ, Uebel CJ, Anderson DC, Mandarino LM, Manage KI, Aynaszyan S, Phillips CM. </i> PLoS Genet, 2018","date":"2024-03-20T16:37:38.582Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02216r004","statement":[{"text":"MUT-16 has a short IDR near the N-terminus (first ~100 amino acids) and a much longer IDR comprising approximately 60% of the protein (Fig 1A). In total, more than 70% of the protein is predicted to be unstructured.","type":"Results"},{"text":"We also observed that the MUT-16 protein is highly prone to degradation during the immunoprecipitation procedure. While full-length MUT-16 could be observed in most lanes, we also could detect multiple degradation products, with a prominent product of ~70kD in most lanes (S5 Fig). We did not observe substantial degradation with other proteins we worked with and suspect the highly disordered nature of MUT-16 may leave it more exposed to proteases during the immunoprecipitation procedure.","type":"Results"},{"text":"This region is ~70% disordered, but contains the structured L region that is also key to the formation of Mutator foci.","type":"Results"},{"text":"The IUPred analysis in combination to the high degree of degradation highlight the flexibility and high solvent exposure of the protein. The curator resorted to the deletion experiments and to MobiDB for further structural information to determine the IDRs boundaries. The authors refer to L region to the 947-1033 residues.","type":"Curator statement"}]},{"start":773,"end":884,"reference_id":"30036386","reference_source":"pmid","reference_html":"Distinct regions of the intrinsically disordered protein MUT-16 mediate assembly of a small RNA amplification complex and promote phase separation of Mutator foci. <i> Uebel CJ, Uebel CJ, Anderson DC, Mandarino LM, Manage KI, Aynaszyan S, Phillips CM. </i> PLoS Genet, 2018","date":"2024-03-20T17:42:40.253Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140694","term_name":"non-membrane-bounded organelle assembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Val773Pro884del","start":null,"end":null,"position":null},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"},{"term_id":"MI:0520","term_name":"HA","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"ec_go":"IMP","region_id":"DP02216r005","statement":[{"text":"In contrast, ΔJ, ΔK, and ΔL displayed severely disrupted foci, though the overall expression of cytoplasmic MUT-16 was not reduced (Fig 3A and 3D).","type":"Results"},{"text":"Together, these data indicate that C-terminal region of MUT-16 (J, K, and L) contains a region essential for foci formation.","type":"Results"},{"text":"Mutator focus is a type of punctate focus. Mutator foci are required for RNA interference (RNAi). Additionally, the authors refer to J as the 773-884 region, and K as the 885-945 region.","type":"Curator statement"},{"text":"This finding suggests that isolated stretches of disordered amino acids are not sufficient to mediate phase separation, but require the neighboring protein environment to promote Mutator foci formation.","type":"Discussion"}],"term_comment":"","term_def":"\"The aggregation, arrangement and bonding together of a set of components to form a non-membrane-bounded organelle.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false},{"start":885,"end":945,"reference_id":"30036386","reference_source":"pmid","reference_html":"Distinct regions of the intrinsically disordered protein MUT-16 mediate assembly of a small RNA amplification complex and promote phase separation of Mutator foci. <i> Uebel CJ, Uebel CJ, Anderson DC, Mandarino LM, Manage KI, Aynaszyan S, Phillips CM. </i> PLoS Genet, 2018","date":"2024-03-20T17:42:30.317Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140694","term_name":"non-membrane-bounded organelle assembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Asn885Asn945del","start":null,"end":null,"position":null},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"},{"term_id":"MI:0520","term_name":"HA","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"ec_go":"IMP","region_id":"DP02216r006","statement":[{"text":"In contrast, ΔJ, ΔK, and ΔL displayed severely disrupted foci, though the overall expression of cytoplasmic MUT-16 was not reduced (Fig 3A and 3D).","type":"Results"},{"text":"Together, these data indicate that C-terminal region of MUT-16 (J, K, and L) contains a region essential for foci formation.","type":"Results"},{"text":"Mutator focus is a type of punctate focus. Mutator foci are required for RNA interference (RNAi). Additionally, the authors refer to J as the 773-884 region, and K as the 885-945 region.","type":"Curator statement"},{"text":"This finding suggests that isolated stretches of disordered amino acids are not sufficient to mediate phase separation, but require the neighboring protein environment to promote Mutator foci formation.","type":"Discussion"}],"term_comment":"","term_def":"\"The aggregation, arrangement and bonding together of a set of components to form a non-membrane-bounded organelle.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false},{"start":484,"end":569,"reference_id":"30036386","reference_source":"pmid","reference_html":"Distinct regions of the intrinsically disordered protein MUT-16 mediate assembly of a small RNA amplification complex and promote phase separation of Mutator foci. <i> Uebel CJ, Uebel CJ, Anderson DC, Mandarino LM, Manage KI, Aynaszyan S, Phillips CM. </i> PLoS Genet, 2018","date":"2024-03-20T17:22:36.077Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0016441","term_name":"posttranscriptional gene silencing","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gly484Pro569del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP02216r007","statement":[{"text":"Surprisingly, our RNAi assays revealed that only mut-16 deletions ΔC, ΔF, ΔH-I, and ΔL have a significant impact on somatic RNAi (Fig 2A and 2B). The remaining deletions had only mild or no RNAi defect. In contrast, all deletions in mut-16 had defects in germline RNAi, though deletions in ΔA and ΔG had more modest effects (Fig 2C). These data reveal that the majority of the MUT-16 protein is necessary for robust germline RNAi. In contrast, some regions of MUT-16 are dispensable for the response to at least some somatic RNAi clones, suggesting that the soma may be more resilient to mild perturbations in MUT-16.","type":"Results"},{"text":"The authors refer to F as the 484-569 region, and H-I as the 632-772 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"The inactivation of gene expression by a posttranscriptional mechanism.\" [GOC:mah, PMID:15020054]","term_is_obsolete":false,"term_not_annotate":false},{"start":632,"end":772,"reference_id":"30036386","reference_source":"pmid","reference_html":"Distinct regions of the intrinsically disordered protein MUT-16 mediate assembly of a small RNA amplification complex and promote phase separation of Mutator foci. <i> Uebel CJ, Uebel CJ, Anderson DC, Mandarino LM, Manage KI, Aynaszyan S, Phillips CM. </i> PLoS Genet, 2018","date":"2024-03-20T17:21:57.509Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0016441","term_name":"posttranscriptional gene silencing","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Glu632Pro772del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP02216r008","statement":[{"text":"Surprisingly, our RNAi assays revealed that only mut-16 deletions ΔC, ΔF, ΔH-I, and ΔL have a significant impact on somatic RNAi (Fig 2A and 2B). The remaining deletions had only mild or no RNAi defect. In contrast, all deletions in mut-16 had defects in germline RNAi, though deletions in ΔA and ΔG had more modest effects (Fig 2C). These data reveal that the majority of the MUT-16 protein is necessary for robust germline RNAi. In contrast, some regions of MUT-16 are dispensable for the response to at least some somatic RNAi clones, suggesting that the soma may be more resilient to mild perturbations in MUT-16.","type":"Results"},{"text":"The authors refer to F as the 484-569 region, and H-I as the 632-772 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"The inactivation of gene expression by a posttranscriptional mechanism.\" [GOC:mah, PMID:15020054]","term_is_obsolete":false,"term_not_annotate":false},{"start":484,"end":772,"reference_id":"30036386","reference_source":"pmid","reference_html":"Distinct regions of the intrinsically disordered protein MUT-16 mediate assembly of a small RNA amplification complex and promote phase separation of Mutator foci. <i> Uebel CJ, Uebel CJ, Anderson DC, Mandarino LM, Manage KI, Aynaszyan S, Phillips CM. </i> PLoS Genet, 2018","date":"2024-03-20T17:37:14.415Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0070063","term_name":"RNA polymerase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gly484Pro569del","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"G5ECM1","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02216r009","statement":[{"text":"Only the ΔF mutant completely disrupted the interaction between MUT-16 and RRF-1, though the amount of RRF-1 immunoprecipitated by the ΔB, ΔC, and ΔG mutants was modestly reduced relative to full-length MUT-16 (Fig 4F). ","type":"Results"},{"text":"In particular, region F recruits the RdRP protein RRF-1 and the H-I region recruits the exonuclease MUT-7 through its interaction with RDE-2. ","type":"Discussion"},{"text":"The authors refer to F as the 484-569 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to an RNA polymerase molecule or complex.\" [GOC:BHF, GOC:mah, GOC:txnOH]","term_is_obsolete":false,"term_not_annotate":false},{"start":484,"end":772,"reference_id":"30036386","reference_source":"pmid","reference_html":"Distinct regions of the intrinsically disordered protein MUT-16 mediate assembly of a small RNA amplification complex and promote phase separation of Mutator foci. <i> Uebel CJ, Uebel CJ, Anderson DC, Mandarino LM, Manage KI, Aynaszyan S, Phillips CM. </i> PLoS Genet, 2018","date":"2024-03-20T17:40:13.576Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Glu632Pro772del","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P90897","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02216r010","statement":[{"text":"In contrast, RDE-2 fails to localize to Mutator foci in the ΔH-I deletion, and RRF-1 is at least partially disrupted in ΔB, ΔC, ΔF, and ΔG mutants (Fig 4A and S4 Fig). ","type":"Results"},{"text":"In particular, region F recruits the RdRP protein RRF-1 and the H-I region recruits the exonuclease MUT-7 through its interaction with RDE-2. ","type":"Discussion"},{"text":"The authors refer to H-I as the 632-772 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":773,"end":945,"reference_id":"30036386","reference_source":"pmid","reference_html":"Distinct regions of the intrinsically disordered protein MUT-16 mediate assembly of a small RNA amplification complex and promote phase separation of Mutator foci. <i> Uebel CJ, Uebel CJ, Anderson DC, Mandarino LM, Manage KI, Aynaszyan S, Phillips CM. </i> PLoS Genet, 2018","date":"2024-03-20T17:48:59.386Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990633","term_name":"mutator focus","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gly386Asn945del","start":null,"end":null,"position":null},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"},{"term_id":"MI:0520","term_name":"HA","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"ec_go":"IMP","region_id":"DP02216r011","statement":[{"text":"Surprisingly, ΔE-I, which removes 387 amino acids (~37% of the protein) and encompasses a substantial portion of the IDR, does not affect MUT-16 localization, indicating that a large portion of the IDR is dispensable for foci formation. In contrast, ΔE-K does disrupt MUT-16 localization, which is not unexpected given that it includes J and K regions, which individually disrupted foci formation.","type":"Results"},{"text":"The authors describe how the deletion of the J-K region (773-945) leads to the mis-localization of the protein outside the Mutator focus.","type":"Curator statement"}],"term_comment":"","term_def":"\"A type of punctate focus localized to the perinuclear region of germline cytoplasm in C. elegans. Mutator foci are required for RNA interference (RNAi) and serve as sites of small inhibitory RNA (siRNA) amplification. As such, proteins that localize to mutator foci include RNA-directed RNA polymerases (RdRPs) and beta-nucleotidyltransferases. Mutator foci are distinct from, but adjacent to or partially overlap, P granules.\" [GOC:kmv, PMID:22713602, PMID:25635455]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_Q9U3S5","date":"2018-08-29T13:55:20.000Z","acc":"Q9U3S5","name":"MUTator","length":1050,"organism":"Caenorhabditis elegans","dataset":["Condensates-related proteins"],"UniParc":"UPI0000DD084F","genes":[{"name":{"value":"mut-16","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAB54187.3","url":"https://www.ebi.ac.uk/ena/browser/view/CAB54187.3"}},{"code":"ECO:0000313","source":{"name":"WormBase","id":"B0379.3b","url":"https://www.wormbase.org/db/seq/sequence?name=B0379.3b;class=Transcript"}}]},"orfNames":[{"value":"B0379.3","evidences":[{"code":"ECO:0000313","source":{"name":"WormBase","id":"B0379.3b","url":"https://www.wormbase.org/db/seq/sequence?name=B0379.3b;class=Transcript"}}]},{"value":"CELE_B0379.3","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAB54187.3","url":"https://www.ebi.ac.uk/ena/browser/view/CAB54187.3"}}]}]}],"alphafold_very_low_content":0.6752380952380952,"disorder_content":0.6485714285714286,"disprot_consensus":{"full":[{"start":1,"end":100,"type":"D"},{"start":366,"end":946,"type":"D"}],"Structural state":[{"start":1,"end":100,"type":"D"},{"start":366,"end":946,"type":"D"}],"Biological process":[{"start":484,"end":569,"type":"F"},{"start":632,"end":945,"type":"F"}],"Molecular function":[{"start":484,"end":772,"type":"F"}],"Cellular component":[{"start":773,"end":945,"type":"F"}]}},{"features":{"pfam":[{"id":"PF08226","name":"Domain of unknown function (DUF1720)","start":165,"end":243},{"id":"PF08226","name":"Domain of unknown function (DUF1720)","start":389,"end":453},{"id":"PF08226","name":"Domain of unknown function (DUF1720)","start":468,"end":525},{"id":"PF12763","name":"EH domain","start":267,"end":350},{"id":"PF12763","name":"EH domain","start":597,"end":689}],"gene3D":[{"start":257,"end":359,"id":"1.10.238.10","name":"EF-hand"},{"start":574,"end":687,"id":"1.10.238.10","name":"EF-hand"}]},"uniref50":"UniRef50_P32521","sequence":"MYNPYQQQGMGYQQQQQQQQQQPNGFYPQQQQGQSSNQPQGQPQPQQQMAFNQPQATGIGGMPQSFGNSFSSMPQQPQTGYNNNGNNGSVYGNGNFGQQPQQQQQQAKPQHTGYVPNSSMPMMNTTGTMPPPNPAQQPQLQSIQPQGTGYYQAANTANVHSVQPLQSQGTGYYVSTPNLISSNQTQQPLQAQGTGYYQSQPQQVPPPQQAQSLQPLKPQQTGFYLQPQNQAPLEPLKPTATGFVNSFANNGLNNDIKIPAIRLSFITAQDQAKFETLFRSIVTNGSNTVSGANCRKILMRSGLPPSQLARIWTLCDTSKAGELLFPEFALAMHLINDVLQGDTIPYELDSKTKNEVSSFIDAINLSIANQDSSANDAPKTPFDEFITAGVQNLQPQPTGYMPQTSFGIPLQSQITGGGVASALNPQSTGFMAPTTFNMSMNTGTPGLNPQITGGAPASMQPNITGNALQPQTTGMMPQTTGMMPQTTGMMPQTSFGVNLGPQLTGGALQSQYTGGYGSVMPQQSGPASMPNLSFNQQGLQSQLTGLQPQPTGFLPPSNFSATMPLTAQKTGFGNNEIYTKSNFNNNLIDNSSQDKISTEEKSLFYKIFETFDTQNKGLLDSPTAVEIFRKSGLNRADLEQIWNLCDINNTGQLNKQEFALGMHLVYGKLNGKPIPNVLPSSLIPSSTKLLDNLKNQLKTEPTTTKEKPSFGKIDALSYKNNDDDVLPNYRNRRKVYSAKNEEQSSFSSPSAKSVNHSSSTLQTDDISVDKTVEKKTAKPKYAGFSREINLKNIASLENEIKNISNPENCYDSSIPSDLTSRFDAIIAKLPNLFNEISTIDNEITNAKIQLYRKKNPSSIIGSGPNGEITENDRKKAKSRALLRARMSALTGKSTESEDSLSMEDEQQSAEIKRIQQENGKNQEIIKDIRSSISDISASLKSTMTGSNMISNQEFERWEFGIGLEDGVREFLDDLKSNSNKSVTESSPFVPSSTPTPVDDRSSSPSYSQFKTAEERAAYLKEQAKKRMKEKLAKFDKNRRNVTQSSRSISSENSREQPQQIAGSSNLVEPRATPFQEEKYVEVAQPTQPVQSTQPVQPTQPVQPTQPVQPTQPVQPTQPVQPTQPVQNVYNAKQESDDEDEDDEEKRLQEELKRLKLKKKADKEKRLAALRKQIEDAQNESDEEETNGKDNFGGHVNVPQAAPVAPSAAFSQNSTNAPRSVHAAVTPAAGKNSTGLPSTTMGHNPYFKDASASSTSTFDARAAEMQRRIQRGLDEDEDDGWSDEDESNNRVAVDNKVEEAKIGHPDHARAPPVTAAPLPSVTPVPPAVPVPQANTSNEKSSPIPIAPIPPSVTQEPPVPLAPPLPAVDGFQEPPIPSAPAIATAVQKSGSSTPALAGGVLPPPPPLPTQQASTSEPIIAHVDNYNGAEKGTGAYGSDSDDDVLSIPESVGTDEEEEGAQPVSTAGIPSIPPAGIPPPPPLP","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P32521","disprot_id":"DP02220","ncbi_taxon_id":559292,"regions_counter":2,"creator":"baykac","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1480,"region_id":"DP02220r001","released":"2022_03","ec_id":"ECO:0007689","reference_html":"Pan1 is an intrinsically disordered protein with homotypic interactions. <i> Pierce BD, Toptygin D, Wendland B. </i> Proteins, 2013","statement":[{"text":"In general, disordered regions do not pellet after heating while structured regions tend to unfold upon boiling and\naggregate upon cooling, causing them to be found in the pellet after centrifugation. ... In contrast, the C-terminal fragment (His6-Pan1 1191–1480) did not pellet after boiling, consistent with the unstructured prediction from the PONDR analysis.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"baykac","start":1191,"term_ontology":"IDPO","curator_name":"Burcu Aykac-Fas","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-3842-731X","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23801378","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1480,"region_id":"DP02220r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Pan1 is an intrinsically disordered protein with homotypic interactions. <i> Pierce BD, Toptygin D, Wendland B. </i> Proteins, 2013","statement":[{"text":"The Pan1 N-terminal fragment (amino acids 230–700) exhibited the typical CD spectrum for a-helices, with peaks at 222 and 208 nm, while the CD spectrum of the C-terminus (amino acids 1191–1480) indicated that this region is mostly random coil.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"baykac","start":1191,"term_ontology":"IDPO","curator_name":"Burcu Aykac-Fas","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-3842-731X","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"23801378","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P32521","date":"2018-08-29T16:20:12.000Z","acc":"P32521","name":"Actin cytoskeleton-regulatory complex protein PAN1","length":1480,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000168D51","genes":[{"name":{"value":"PAN1"},"synonyms":[{"value":"DIM2"},{"value":"MDP3"},{"value":"MIP3"}],"orfNames":[{"value":"YIB6C"}],"olnNames":[{"value":"YIR006C"}]}],"alphafold_very_low_content":0.6452702702702703,"disorder_content":0.19594594594594594,"disprot_consensus":{"full":[{"start":1191,"end":1480,"type":"D"}],"Structural state":[{"start":1191,"end":1480,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00628","name":"PHD-finger","start":296,"end":340},{"id":"PF00628","name":"PHD-finger","start":1164,"end":1215},{"id":"PF01388","name":"ARID/BRIGHT DNA binding domain","start":88,"end":170},{"id":"PF02373","name":"JmjC domain, hydroxylase","start":470,"end":586},{"id":"PF02375","name":"jmjN domain","start":20,"end":53},{"id":"PF02928","name":"C5HC2 zinc finger","start":676,"end":728},{"id":"PF08429","name":"PLU-1-like protein","start":741,"end":1072},{"id":"PF21323","name":"Lysine-specific demethylase 5, C-terminal helical domain","start":590,"end":644}],"gene3D":[{"start":1607,"end":1666,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":1157,"end":1219,"id":"3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":86,"end":183,"id":"1.10.150.60","name":"ARID DNA-binding domain"},{"start":324,"end":609,"id":"2.60.120.650","name":"Cupin"},{"start":19,"end":85,"id":"2.60.120.650","name":"Cupin"}]},"uniref50":"UniRef50_P29375","sequence":"MAGVGPGGYAAEFVPPPECPVFEPSWEEFTDPLSFIGRIRPLAEKTGICKIRPPKDWQPPFACEVKSFRFTPRVQRLNELEAMTRVRLDFLDQLAKFWELQGSTLKIPVVERKILDLYALSKIVASKGGFEMVTKEKKWSKVGSRLGYLPGKGTGSLLKSHYERILYPYELFQSGVSLMGVQMPNLDLKEKVEPEVLSTDTQTSPEPGTRMNILPKRTRRVKTQSESGDVSRNTELKKLQIFGAGPKVVGLAMGTKDKEDEVTRRRKVTNRSDAFNMQMRQRKGTLSVNFVDLYVCMFCGRGNNEDKLLLCDGCDDSYHTFCLIPPLPDVPKGDWRCPKCVAEECSKPREAFGFEQAVREYTLQSFGEMADNFKSDYFNMPVHMVPTELVEKEFWRLVSSIEEDVIVEYGADISSKDFGSGFPVKDGRRKILPEEEEYALSGWNLNNMPVLEQSVLAHINVDISGMKVPWLYVGMCFSSFCWHIEDHWSYSINYLHWGEPKTWYGVPSHAAEQLEEVMRELAPELFESQPDLLHQLVTIMNPNVLMEHGVPVYRTNQCAGEFVVTFPRAYHSGFNQGYNFAEAVNFCTADWLPIGRQCVNHYRRLRRHCVFSHEELIFKMAADPECLDVGLAAMVCKELTLMTEEETRLRESVVQMGVLMSEEEVFELVPDDERQCSACRTTCFLSALTCSCNPERLVCLYHPTDLCPCPMQKKCLRYRYPLEDLPSLLYGVKVRAQSYDTWVSRVTEALSANFNHKKDLIELRVMLEDAEDRKYPENDLFRKLRDAVKEAETCASVAQLLLSKKQKHRQSPDSGRTRTKLTVEELKAFVQQLFSLPCVISQARQVKNLLDDVEEFHERAQEAMMDETPDSSKLQMLIDMGSSLYVELPELPRLKQELQQARWLDEVRLTLSDPQQVTLDVMKKLIDSGVGLAPHHAVEKAMAELQELLTVSERWEEKAKVCLQARPRHSVASLESIVNEAKNIPAFLPNVLSLKEALQKAREWTAKVEAIQSGSNYAYLEQLESLSAKGRPIPVRLEALPQVESQVAAARAWRERTGRTFLKKNSSHTLLQVLSPRTDIGVYGSGKNRRKKVKELIEKEKEKDLDLEPLSDLEEGLEETRDTAMVVAVFKEREQKEIEAMHSLRAANLAKMTMVDRIEEVKFCICRKTASGFMLQCELCKDWFHNSCVPLPKSSSQKKGSSWQAKEVKFLCPLCMRSRRPRLETILSLLVSLQKLPVRLPEGEALQCLTERAMSWQDRARQALATDELSSALAKLSVLSQRMVEQAAREKTEKIISAELQKAAANPDLQGHLPSFQQSAFNRVVSSVSSSPRQTMDYDDEETDSDEDIRETYGYDMKDTASVKSSSSLEPNLFCDEEIPIKSEEVVTHMWTAPSFCAEHAYSSASKSCSQGSSTPRKQPRKSPLVPRSLEPPVLELSPGAKAQLEELMMVGDLLEVSLDETQHIWRILQATHPPSEDRFLHIMEDDSMEEKPLKVKGKDSSEKKRKRKLEKVEQLFGEGKQKSKELKKMDKPRKKKLKLGADKSKELNKLAKKLAKEEERKKKKEKAAAAKVELVKESTEKKREKKVLDIPSKYDWSGAEESDDENAVCAAQNCQRPCKDKVDWVQCDGGCDEWFHQVCVGVSPEMAENEDYICINCAKKQGPVSPGPAPPPSFIMSYKLPMEDLKETS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P29375","disprot_id":"DP02224","ncbi_taxon_id":9606,"regions_counter":2,"creator":"lchemes","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":360,"region_id":"DP02224r001","released":"2023_06","ec_id":"ECO:0006220","reference_html":"An inhibitor of KDM5 demethylases reduces survival of drug-tolerant cancer cells. <i> Vinogradova M, Gehling VS, Gustafson A, Arora S, Tindell CA, Wilson C, Williamson KE, Guler GD, Gangurde P, Manieri W, Busby J, Flynn EM, Lan F, Kim HJ, Odate S, Cochran AG, Liu Y, Wongchenko M, Yang Y, Cheung TK, Maile TM, Lau T, Costa M, Hegde GV, Jackson E, Pitti R, Arnott D, Bailey C, Bellon S, Cummings RT, Albrecht BK, Harmange JC, Kiefer JR, Trojer P, Classon M. </i> Nat Chem Biol, 2016","statement":[{"text":"The final model contained amino acids 12–183 and 361–785, with remaining amino acid residues disordered. Relatively strong but discontinuous difference electron density for a short stretch of amino acids (approximately ten residues) beyond residue 183 exists but was not sufficient to convincingly set the registration of the chain.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":184,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27214401","version":3,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2023-05-31T15:32:12.888Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5CEH"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:935"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:78426698"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":360,"region_id":"DP02224r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Design and evaluation of 1,7-naphthyridones as novel KDM5 inhibitors. <i> Labadie SS, Dragovich PS, Cummings RT, Deshmukh G, Gustafson A, Han N, Harmange JC, Kiefer JR, Li Y, Liang J, Liederer BM, Liu Y, Manieri W, Mao W, Murray L, Ortwine DF, Trojer P, VanderPorten E, Vinogradova M, Wen L. </i> Bioorg Med Chem Lett, 2016","statement":[{"text":"This region also corresponds to the KDM5A PHD1 domain, which is disordered in this structure too as in 5CEH","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"lchemes","start":184,"term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"27499454","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5K4L"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T20:40:53.023Z"}}],"released":"2018_11","uniref100":"UniRef100_P29375","date":"2018-08-30T09:20:39.000Z","acc":"P29375","name":"Lysine-specific demethylase 5A","length":1690,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI00001740DF","genes":[{"name":{"value":"KDM5A","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9886","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9886"}}]},"synonyms":[{"value":"JARID1A"},{"value":"RBBP2"},{"value":"RBP2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"18270511","url":"http://www.ncbi.nlm.nih.gov/pubmed/18270511","alternativeUrl":"https://europepmc.org/abstract/MED/18270511"}}]}]}],"alphafold_very_low_content":0.25502958579881657,"disorder_content":0.10473372781065089,"disprot_consensus":{"full":[{"start":184,"end":360,"type":"D"}],"Structural state":[{"start":184,"end":360,"type":"D"}]}},{"features":{"pfam":[{"id":"PF02365","name":"No apical meristem (NAM) protein","start":21,"end":146}],"gene3D":[{"start":29,"end":175,"id":"3.30.310.150","name":"NAC domain"}]},"uniref50":"UniRef50_Q9SQQ6","sequence":"MVEEGGVVVNQGGDQEVVDLPPGFRFHPTDEEIITHYLKEKVFNIRFTAAAIGQADLNKNEPWDLPKIAKMGEKEFYFFCQRDRKYPTGMRTNRATVSGYWKATGKDKEIFRGKGCLVGMKKTLVFYTGRAPKGEKTNWVMHEYRLDGKYSYHNLPKTARDEWVVCRVFHKNAPSTTITTTKQLSRIDSLDNIDHLLDFSSLPPLIDPGFLGQPGPSFSGARQQHDLKPVLHHPTTAPVDNTYLPTQALNFPYHSVHNSGSDFGYGAGSGNNNKGMIKLEHSLVSVSQETGLSSDVNTTATPEISSYPMMMNPAMMDGSKSACDGLDDLIFWEDLYTS","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q9SQQ6","disprot_id":"DP02225","ncbi_taxon_id":3702,"regions_counter":20,"creator":"grivas","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":338,"region_id":"DP02225r001","released":"2024_06","ec_id":"ECO:0006204","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","statement":[{"text":"Although the spectra of the six recombinant proteins showed different characteristics, they all had a minimum around 200 nm and only slightly negative ellipticities at 222 nm (Figure 4a). Both the [θ]222 and [θ]200 values suggested that histidine–NTL8 (156–335), ANAC013 (161–498), NAP (162–268) and ANAC019 (163–317) are similar, populating pre-molten globule like ensembles, whereas the values for histidine–SOG1 (210–449) and ANAC046 (172–338) suggest more random coil-like ensembles.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":172,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-22T16:25:52.975Z","reference_source":"pmid","term_name":"disorder","reference_id":"25348421","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":319,"end":338,"reference_id":"27881680","reference_source":"pmid","reference_html":"Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1. <i> O'Shea C, Staby L, Bendsen SK, Tidemand FG, Redsted A, Willemoës M, Kragelund BB, Skriver K. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP02225r003","statement":[{"text":"Similar to DREB2A(255–272), free ANAC013(254–274) and ANAC046(319–338) had poorly dispersed HSQC spectra (Fig. 7, B and C, black spectra), and ΔδCα values close to zero (Fig. 7, E and F, top figures) again confirming a lack of preformed structure.","type":"Results"},{"text":"In support of this, no indications of transiently formed structure were apparent from the secondary Cα chemical shifts (Fig. 7F, top figure) or AGADIR predictions (Fig. 5A) for ANAC046. ","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-13T16:00:43.277Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":319,"end":338,"reference_id":"27881680","reference_source":"pmid","reference_html":"Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1. <i> O'Shea C, Staby L, Bendsen SK, Tidemand FG, Redsted A, Willemoës M, Kragelund BB, Skriver K. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"Q8RY59","partner_start":null,"partner_end":null}],"region_id":"DP02225r004","statement":[{"text":"Comparison of the HSQC spectra of free and bound ANAC013(254–274) and ANAC046(319–338) confirmed their interaction with RCD1-RST(499–572) (Fig. 7, B and C), but in contrast to those of DREB2A(255–272), the dispersion in the proton dimension appeared immediately unaffected. ","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-13T16:01:30.282Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":319,"end":338,"reference_id":"27881680","reference_source":"pmid","reference_html":"Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1. <i> O'Shea C, Staby L, Bendsen SK, Tidemand FG, Redsted A, Willemoës M, Kragelund BB, Skriver K. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"Q8RY59","partner_start":null,"partner_end":null}],"region_id":"DP02225r006","statement":[{"text":"The ANAC046(319–338)·RCD1-RST(499–572) complex had an overall α-helical content of 38%, compared with 34% in the theoretical complex. However, in this case a shift toward a lower wavelength in the complex was observed (Fig. 6D). Together, the results suggested that complex formation involving ANAC046(319–338) and ANAC013(254–274) resulted in structure induction, although to a lower degree than that of the DREB2A(255–272)·RCD1-RST(499–572) complex.","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-13T16:01:34.857Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":315,"end":338,"reference_id":"34439840","reference_source":"pmid","reference_html":"Insight into Calcium-Binding Motifs of Intrinsically Disordered Proteins. <i> Newcombe EA, Fernandes CB, Lundsgaard JE, Brakti I, Lindorff-Larsen K, Langkilde AE, Skriver K, Kragelund BB. </i> Biomolecules, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP02225r007","statement":[{"text":"Here, based on the CSPs, we observed binding in the region of M315 to S338, indicating a localized C-terminal interaction occurring at the same binding site at which ANAC046 interacts with radical induced cell death1 (RCD1) [43].","type":"Results"}],"interaction_partner":[{"db":"ChEBI","id":"3312","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-07T13:15:10.025Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":315,"end":338,"reference_id":"34439840","reference_source":"pmid","reference_html":"Insight into Calcium-Binding Motifs of Intrinsically Disordered Proteins. <i> Newcombe EA, Fernandes CB, Lundsgaard JE, Brakti I, Lindorff-Larsen K, Langkilde AE, Skriver K, Kragelund BB. </i> Biomolecules, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jpujols","curator_name":"Jordi Pujols Pujol","curator_orcid":"0000-0001-9424-5866","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007740","ec_ontology":"ECO","ec_name":"small molecule detection assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"ChEBI","id":"3312","partner_start":null,"partner_end":null}],"region_id":"DP02225r008","statement":[{"text":"Here, based on the CSPs, we observed binding in the region of M315 to S338, indicating a localized C-terminal interaction occurring at the same binding site at which ANAC046 interacts with radical induced cell death1 (RCD1) [43].","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-07T13:15:03.702Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":172,"end":338,"reference_id":"34439840","reference_source":"pmid","reference_html":"Insight into Calcium-Binding Motifs of Intrinsically Disordered Proteins. <i> Newcombe EA, Fernandes CB, Lundsgaard JE, Brakti I, Lindorff-Larsen K, Langkilde AE, Skriver K, Kragelund BB. </i> Biomolecules, 2021","date":"2024-02-22T15:39:14.721Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"BMRB","id":"51033"}],"region_id":"DP02225r010","statement":[{"text":"ANAC046172-338 narrow secondary chemical shifts dispersion (confined in the region 8.0 to 8.5 ppm) shown in the Supplementary figures and the BMRB file, indicates this region is disordered.","type":"Curator statement"}]},{"start":172,"end":338,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2024-02-22T15:51:59.083Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02225r011","statement":[{"text":"Although the relative migration pattern of the recombinant proteins by SDS/PAGE was in accordance with their relative molecular mass values [NAP (162–268): 15.0 kDa; ANAC019 (163–317): 17.2 kDa; ANAC046 (172–338): 18.2 kDa; histidine–NTL8 (156–335): 20.3 kDa; histidine–SOG (210–449): 29.0 kDa; ANAC013 (161–498): 37.5 kDa], they displayed slow migration during SDS/PAGE compared with standard globular proteins, which is in accordance with their ID nature and previous analysis of two NAC TRDs [39].","type":"Results"}]},{"start":172,"end":338,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2024-02-22T16:17:36.275Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02225r012","statement":[{"text":"This aspect was analysed by size-exclusion chromatography for the four untagged NAC TRDs. The hydrodynamic radii (Stokes radii) of ANAC046 (172–338), NAP (162–268) and ANAC019 (163–317) corresponded to pre-molten globule states, whereasANAC013 (161–498) had a more compact structure consistent with its disorder profile (Figures 1d and 3).","type":"Results"}]},{"start":315,"end":338,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2024-02-22T16:49:33.038Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140537","term_name":"transcription regulator activator activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006295","ec_ontology":"ECO","ec_name":"beta galactosidase functional complementation evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0693","term_name":"Gal4 DNA-binding domain tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"region_id":"DP02225r013","statement":[{"text":"After demonstrating the ability of full-length ANAC046 and its TRD to activate transcription, analysis of C-terminally truncated versions of these suggested the importance of the MoRF region for the activity (Figure 7c). This was supported by the ability of ANAC046 (315–338) to activate transcription.","type":"Results"}],"ec_go":"IPI","term_comment":"Usage guidance: transcription regulator activators bind to a transcription regulator to allow it to reach the chromatin or to contact other transcriptional regulators. This activity does not occur at the promoter. For activities that do occur at the promoter, consider GO:0001216 ; DNA-binding transcription activator activity or GO:0003713; transcription coactivator activity; those activities respectively bind DNA themselves or positively regulate a transcription regulator when it is located at the chromatin.","term_def":"\"A molecular function regulator that increases the activity of a transcription regulator via direct binding and/or post-translational modification.\" [PMID:9597751]","term_is_obsolete":false,"term_not_annotate":false},{"start":315,"end":338,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2024-02-22T17:08:12.780Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005805","ec_ontology":"ECO","ec_name":"yeast 2-hybrid evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0693","term_name":"Gal4 DNA-binding domain tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Figure","text":"Fusions of GAL4 DBD and the RST domain of RCD1 (residues 498–573; DBD–RST) and of GAL4 AD and the NAP fragment shown were expressed in yeast and screened for interactions through the ability to activate the reporter genes HIS3 and ADE2."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q8RY59","operator":null,"partner_start":487,"partner_end":589}],"region_id":"DP02225r014","statement":[{"text":"As expected, the RST domain of RCD1 interacted with both full-length ANAC013 and ANAC046 and their TRDs (Figures 7b and 7c), whereas no interaction was detected with NAP (Figure 7a) [27].","type":"Results"},{"text":"C-terminal truncations were also analysed for their ability to interact with DBD–RCD1 (498-573). This suggested that residues 205–299 of ANAC013 and that the very C-terminal MoRF region of ANAC046 were responsible for the interactions (Figures 7b–7c).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":172,"end":338,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2024-02-22T17:11:49.846Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q8RY59","operator":null,"partner_start":487,"partner_end":589}],"region_id":"DP02225r015","statement":[{"text":"A slight change of the absolute minimum towards a lower wavelength for the complex compared with the theoretical complex, obtained by adding the individualANAC046 (172–338) and histidine–RCD1–RST (487–589) spectra, suggested that complex formation does not involve folding, but is suggestive of unfolding.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":328,"end":338,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2024-02-22T17:15:40.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q8RY59","operator":null,"partner_start":499,"partner_end":572}],"region_id":"DP02225r016","statement":[{"text":"The affinities of the ANAC013 TRD, ANAC013 (161–498) and the ANAC046 TRD, ANAC046 (172–338), for the RST domain, RCD1–RST (499–572), was approximately the same with Kd values of 537 nM and 609 nM respectively (Figures 8a and 8b; Table 1).","type":"Results"},{"text":"Binding to the synthetic peptidesANAC046 (319–338) andANAC046 (328–338)was also analysed. Both span the MoRF region (Figure 5).","type":"Results"},{"text":"Binding of these peptides to RCD1–RST (499–572) showed approximately the same Kd as was obtained for binding of ANAC046 (172–338) to RST.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_Q9SQQ6","date":"2018-08-30T09:21:09.000Z","acc":"Q9SQQ6","name":"NAC domain-containing protein 46","length":338,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI000005EC7B","genes":[{"name":{"value":"NAC046","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AEE74032.1","url":"https://www.ebi.ac.uk/ena/browser/view/AEE74032.1"}}]},"orfNames":[{"value":"T11I18.17","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAF05864.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF05864.1"}}]}],"olnNames":[{"value":"At3g04060","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT3G04060","url":""}}]}]}],"alphafold_very_low_content":0.4437869822485207,"disorder_content":0.4940828402366864,"disprot_consensus":{"full":[{"start":172,"end":338,"type":"D"}],"Structural state":[{"start":172,"end":338,"type":"D"}],"Molecular function":[{"start":172,"end":338,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00134","name":"Cyclin, N-terminal domain","start":27,"end":152},{"id":"PF02984","name":"Cyclin, C-terminal domain","start":155,"end":274}],"gene3D":[{"start":41,"end":153,"id":"1.10.472.10","name":"Cyclin-like"},{"start":26,"end":254,"id":"1.10.472.10","name":"Cyclin-like"}]},"uniref50":"UniRef50_P24385","sequence":"MEHQLLCCEVETIRRAYPDANLLNDRVLRAMLKAEETCAPSVSYFKCVQKEVLPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLAAMTPHDFIEHFLSKMPEAEENKQIIRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAVQGLNLRSPNNFLSYYRLTRFLSRVIKCDPDCLRACQEQIEALLESSLRQAQQNMDPKAAEEEEEEEEEVDLACTPTDVRDVDI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P24385","disprot_id":"DP02226","ncbi_taxon_id":9606,"regions_counter":4,"creator":"lchemes","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":24,"region_id":"DP02226r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of human CDK4 in complex with a D-type cyclin. <i> Day PJ, Cleasby A, Tickle IJ, O'Reilly M, Coyle JE, Holding FP, McMenamin RL, Yon J, Chopra R, Lengauer C, Jhoti H. </i> Proc Natl Acad Sci U S A, 2009","statement":[{"text":"Cyclin D1 is known to contain 2 Rb binding sites (17) comprised of an N-terminal LxCxE consensus motif and a peptide recruitment site. The cyclin D1 structure exhibits N-terminal disorder, so the LxCxE motif cannot be visualized.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"lchemes","start":1,"term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"19237565","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2W96"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T14:37:03.651Z"}},{"start":256,"end":295,"reference_id":"38191593","reference_source":"pmid","reference_html":"A cyclin D1 intrinsically disordered domain accesses modified histone motifs to govern gene transcription. <i> Jiao X, Di Sante G, Casimiro MC, Tantos A, Ashton AW, Li Z, Quach Y, Bhargava D, Di Rocco A, Pupo C, Crosariol M, Lazar T, Tompa P, Wang C, Yu Z, Zhang Z, Aldaaysi K, Vadlamudi R, Mann M, Skordalakes E, Kossenkov A, Du Y, Pestell RG. </i> Oncogenesis, 2024","date":"2024-01-12T10:45:47.804Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006216","ec_ontology":"ECO","ec_name":"author inference used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02226r004","statement":[{"text":"The predictors agree that most of the cyclin D1 sequence encodes for a structured protein (aa1-aa255, corresponding to a carboxyl-terminal and an amino-terminal domain), whereas the carboxyl-terminal 40 residues (aa256-aa295) have a strong tendency to be intrinsically disordered. Considering the training sets of the predictors relying on examples of IDPs/IDRs, we can be sure that this region does not fluctuate around an equilibrium conformation (that is, it is not “flexible”). Rather it is disordered and can assume a broad ensemble of conformations most appropriate for potentially adapting to diverse binding partners. This is particularly true for the E-rich region. The last carboxyl-terminal 15 residues appear as a down-peak on the disordered pattern (Fig. 4A) with alternating acidic and aliphatic residues, and its behavior of predicted disorder and local hydrophobicity is characteristic of IDP binding motifs. In agreement, this region gives a very strong signal by the ANCHOR predictor (Fig. 4A) developed to recognize specific protein recognition sites embedded in IDPs/IDRs [48].","type":"Results"},{"text":"Disorder tendency and disordered binding site prediction. PRDos (blue), IUPred long (maroon), PONDR (orange) predictions show that the carboxy-terminal 40 residues (aa 256 - aa295) have a strong tendency to be intrinsically disordered, whereas ANCHOR (black) suggests that last 15 amino acids contain a protein-protein interaction site.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T13:57:00.064Z"}}],"released":"2018_11","uniref100":"UniRef100_P24385","date":"2018-08-30T09:41:45.000Z","acc":"P24385","name":"G1/S-specific cyclin-D1","length":295,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI0000001285","genes":[{"name":{"value":"CCND1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8204893","url":"http://www.ncbi.nlm.nih.gov/pubmed/8204893","alternativeUrl":"https://europepmc.org/abstract/MED/8204893"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:1582","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:1582"}}]},"synonyms":[{"value":"BCL1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"1826542","url":"http://www.ncbi.nlm.nih.gov/pubmed/1826542","alternativeUrl":"https://europepmc.org/abstract/MED/1826542"}}]},{"value":"PRAD1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"1826542","url":"http://www.ncbi.nlm.nih.gov/pubmed/1826542","alternativeUrl":"https://europepmc.org/abstract/MED/1826542"}}]}]}],"alphafold_very_low_content":0.04067796610169491,"disorder_content":0.21694915254237288,"disprot_consensus":{"full":[{"start":1,"end":24,"type":"D"},{"start":256,"end":295,"type":"D"}],"Structural state":[{"start":1,"end":24,"type":"D"},{"start":256,"end":295,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":120,"end":160},{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":163,"end":201},{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":205,"end":244},{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":248,"end":286},{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":289,"end":327},{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":330,"end":370},{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":372,"end":411},{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":418,"end":456},{"id":"PF01749","name":"Importin beta binding domain","start":17,"end":108},{"id":"PF16186","name":"Atypical Arm repeat","start":471,"end":523}],"gene3D":[{"start":87,"end":509,"id":"1.25.10.10","name":"Leucine-rich Repeat Variant"},{"start":16,"end":58,"id":"1.20.5.690","name":"Importin-alpha, importin-beta-binding domain"}]},"uniref50":"UniRef50_Q02821","sequence":"MDNGTDSSTSKFVPEYRRTNFKNKGRFSADELRRRRDTQQVELRKAKRDEALAKRRNFIPPTDGADSDEEDESSVSADQQFYSQLQQELPQMTQQLNSDDMQEQLSATVKFRQILSREHRPPIDVVIQAGVVPRLVEFMRENQPEMLQLEAAWALTNIASGTSAQTKVVVDADAVPLFIQLLYTGSVEVKEQAIWALGNVAGDSTDYRDYVLQCNAMEPILGLFNSNKPSLIRTATWTLSNLCRGKKPQPDWSVVSQALPTLAKLIYSMDTETLVDACWAISYLSDGPQEAIQAVIDVRIPKRLVELLSHESTLVQTPALRAVGNIVTGNDLQTQVVINAGVLPALRLLLSSPKENIKKEACWTISNITAGNTEQIQAVIDANLIPPLVKLLEVAEYKTKKEACWAISNASSGGLQRPDIIRYLVSQGCIKPLCDLLEIADNRIIEVTLDALENILKMGEADKEARGLNINENADFIEKAGGMEKIFNCQQNENDKIYEKAYKIIETYFGEEEDAVDETMAPQNAGNTFGFGSNVNQQFNFN","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q02821","disprot_id":"DP02227","ncbi_taxon_id":559292,"regions_counter":1,"creator":"mpajkos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":530,"region_id":"DP02227r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha. <i> Conti E, Uy M, Leighton L, Blobel G, Kuriyan J. </i> Cell, 1998","statement":[{"text":"Crystal diffracting was obtained with a shorter fragment, comprising residues 88-530.\n\"The refined model comprises residues 89–509 of karyopherin α, 140 water molecules, and a cobalt ion, while the 20 carboxy-terminal residues are disordered and not modeled.\"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":510,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"9695948","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q02821","date":"2018-08-30T10:06:52.000Z","acc":"Q02821","name":"Importin subunit alpha","length":542,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000003311C","genes":[{"name":{"value":"SRP1"},"synonyms":[{"value":"KAP60"}],"orfNames":[{"value":"N1606"}],"olnNames":[{"value":"YNL189W"}]}],"alphafold_very_low_content":0.12177121771217712,"disorder_content":0.03874538745387454,"disprot_consensus":{"full":[{"start":510,"end":530,"type":"D"}],"Structural state":[{"start":510,"end":530,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00250","name":"Forkhead domain","start":72,"end":157}],"gene3D":[{"start":71,"end":171,"id":"1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}]},"uniref50":"UniRef50_Q61850","sequence":"MQARYSVSDPNALGVVPYLSEQNYYRAAGSYGGMASPMGVYSGHPEQYSAGMGRSYAPYHHHQPAAPKDLVKPPYSYIALITMAIQNAPEKKITLNGIYQFIMDRFPFYRENKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKDVSKEKEERAHLKEPPPAASKGAPATPHLADAPKEAEKKVVIKSEAASPALPVITKVETLSPESALQGSPRSAASTPAGSPDGSLPEHHAAAPNGLPGFSVENIMTLRTSPPGGELSPGAGRAGLVVPPLALPYAAAPPAAYGQPCAQGLEAGAAGGYQCSMRAMSLYTGAERPAHMCVPPALDEALSDHPSGPTSPLSALNLAAGQEGALAATGHHHQHHGHHHPQAPPPPPAPQPQPTPQPGAAAAQAASWYLNHSGDLNHLPGHTFAAQQQTFPNVREMFNSHRLGIENSTLGESQVSGNASCQLPYRSTPPLYRHAAPYSYDCTKY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q99958","disprot_id":"DP02231","ncbi_taxon_id":9606,"regions_counter":1,"creator":"mpajkos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":144,"region_id":"DP02231r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure and dynamics of the DNA-binding domain of the adipocyte-transcription factor FREAC-11. <i> van Dongen MJ, Cederberg A, Carlsson P, Enerbäck S, Wikström M. </i> J Mol Biol, 2000","statement":[{"text":"\"the region running from residue 66 to 76 are significantly less ordered.\"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":134,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1D5V"}],"reference_id":"10669593","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q99958","date":"2018-08-30T11:49:03.000Z","acc":"Q99958","name":"Forkhead box protein C2","length":501,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012ADC6","genes":[{"name":{"value":"FOXC2"},"synonyms":[{"value":"FKHL14"},{"value":"MFH1"}]}],"alphafold_very_low_content":0.5588822355289421,"disorder_content":0.021956087824351298,"disprot_consensus":{"full":[{"start":134,"end":144,"type":"D"}],"Structural state":[{"start":134,"end":144,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00850","name":"Histone deacetylase domain","start":28,"end":318}],"gene3D":[{"start":1,"end":376,"id":"3.40.800.20","name":"Histone deacetylase domain"}]},"uniref50":"UniRef50_Q13547","sequence":"MAQTQGTRRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEDDPDKRISICSSDKRIACEEEFSDSEEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q13547","disprot_id":"DP02233","ncbi_taxon_id":9606,"regions_counter":2,"creator":"lchemes","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":482,"region_id":"DP02233r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Class I HDACs share a common mechanism of regulation by inositol phosphates. <i> Millard CJ, Watson PJ, Celardo I, Gordiyenko Y, Cowley SM, Robinson CV, Fairall L, Schwabe JW. </i> Mol Cell, 2013","statement":[{"text":"HDAC is crystallised in complex with the MTA1 protein, and the C-terminal region of HDAC remains disordered in the complex.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"lchemes","start":377,"term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"23791785","version":2,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4BKX"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","reference_source":"pmid","ec_ontology":"ECO","end":482,"term_name":"protein binding","start":377,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","statement":[{"text":"This region contains an IxCxE motif (414-420) that binds to the Retinoblastoma tumor suppressor (pRb)","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"23791785","version":3,"reference_html":"Class I HDACs share a common mechanism of regulation by inositol phosphates. <i> Millard CJ, Watson PJ, Celardo I, Gordiyenko Y, Cowley SM, Robinson CV, Fairall L, Schwabe JW. </i> Mol Cell, 2013","date":"2022-02-14T09:00:00.000Z","term_id":"GO:0005515","ec_id":"ECO:0006220","region_id":"DP02233r002","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q13547","date":"2018-08-30T12:18:51.000Z","acc":"Q13547","name":"Histone deacetylase 1","length":482,"organism":"Homo sapiens","dataset":["Autophagy-related proteins"],"UniParc":"UPI0000035528","genes":[{"name":{"value":"HDAC1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10846170","url":"http://www.ncbi.nlm.nih.gov/pubmed/10846170","alternativeUrl":"https://europepmc.org/abstract/MED/10846170"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4852","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4852"}}]},"synonyms":[{"value":"RPD3L1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8602529","url":"http://www.ncbi.nlm.nih.gov/pubmed/8602529","alternativeUrl":"https://europepmc.org/abstract/MED/8602529"}}]}]}],"alphafold_very_low_content":0.12448132780082988,"disorder_content":0.21991701244813278,"disprot_consensus":{"full":[{"start":377,"end":482,"type":"D"}],"Structural state":[{"start":377,"end":482,"type":"D"}],"Molecular function":[{"start":377,"end":482,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00019","name":"Transforming growth factor beta like domain","start":321,"end":425},{"id":"PF00688","name":"TGF-beta propeptide","start":55,"end":293}],"gene3D":[{"start":311,"end":426,"id":"2.10.90.10","name":"Cystine-knot cytokines"},{"start":45,"end":305,"id":"2.60.120.970","name":"2.60.120.970"}]},"uniref50":"UniRef50_P08476","sequence":"MPLLWLRGFLLASCWIIVRSSPTPGSEGHSAAPDCPSCALAALPKDVPNSQPEMVEAVKKHILNMLHLKKRPDVTQPVPKAALLNAIRKLHVGKVGENGYVEIEDDIGRRAEMNELMEQTSEIITFAESGTARKTLHFEISKEGSDLSVVERAEVWLFLKVPKANRTRTKVTIRLFQQQKHPQGSLDTGEEAEEVGLKGERSELLLSEKVVDARKSTWHVFPVSSSIQRLLDQGKSSLDVRIACEQCQESGASLVLLGKKKKKEEEGEGKKKGGGEGGAGADEEKEQSHRPFLMLQARQSEDHPHRRRRRGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P08476","disprot_id":"DP02234","ncbi_taxon_id":9606,"regions_counter":1,"creator":"tszani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":386,"region_id":"DP02234r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structures of an ActRIIB:activin A complex reveal a novel binding mode for TGF-beta ligand:receptor interactions. <i> Thompson TB, Woodruff TK, Jardetzky TS. </i> EMBO J, 2003","statement":[{"text":"For activin A, residues 49–76 that form the canonical TGF-β ‘wrist’ region are disordered in both crystal forms, similar to the TGF-β3:TβRII complex.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"tszani","start":359,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"pdb","id":"1nyu"}],"reference_id":"12660162","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P08476","date":"2018-08-30T12:20:32.000Z","acc":"P08476","name":"Inhibin beta A chain","length":426,"organism":"Homo sapiens","dataset":["Extracellular matrix proteins"],"UniParc":"UPI00000474C9","genes":[{"name":{"value":"INHBA"}}],"alphafold_very_low_content":0.19953051643192488,"disorder_content":0.06572769953051644,"disprot_consensus":{"full":[{"start":359,"end":386,"type":"D"}],"Structural state":[{"start":359,"end":386,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00047","name":"Immunoglobulin domain","start":220,"end":302},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":590,"end":922}],"gene3D":[{"start":1,"end":116,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":309,"end":411,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":208,"end":308,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":412,"end":518,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":117,"end":207,"id":"2.60.40.10","name":"Immunoglobulins"},{"start":740,"end":935,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"},{"start":542,"end":672,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"}]},"uniref50":"UniRef50_P10721","sequence":"MRGARGAWDFLCVLLLLLRVQTGSSQPSVSPGEPSPPSIHPGKSDLIVRVGDEIRLLCTDPGFVKWTFEILDETNENKQNEWITEKAEATNTGKYTCTNKHGLSNSIYVFVRDPAKLFLVDRSLYGKEDNDTLVRCPLTDPEVTNYSLKGCQGKPLPKDLRFIPDPKAGIMIKSVKRAYHRLCLHCSVDQEGKSVLSEKFILKVRPAFKAVPVVSVSKASYLLREGEEFTVTCTIKDVSSSVYSTWKRENSQTKLQEKYNSWHHGDFNYERQATLTISSARVNDSGVFMCYANNTFGSANVTTTLEVVDKGFINIFPMINTTVFVNDGENVDLIVEYEAFPKPEHQQWIYMNRTFTDKWEDYPKSENESNIRYVSELHLTRLKGTEGGTYTFLVSNSDVNAAIAFNVYVNTKPEILTYDRLVNGMLQCVAAGFPEPTIDWYFCPGTEQRCSASVLPVDVQTLNSSGPPFGKLVVQSSIDSSAFKHNGTVECKAYNDVGKTSAYFNFAFKGNNKEQIHPHTLFTPLLIGFVIVAGMMCIIVMILTYKYLQKPMYEVQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRNRLSFGKTLGAGAFGKVVEATAYGLIKSDAAMTVAVKMLKPSAHLTEREALMSELKVLSYLGNHMNIVNLLGACTIGGPTLVITEYCCYGDLLNFLRRKRDSFICSKQEDHAEAALYKNLLHSKESSCSDSTNEYMDMKPGVSYVVPTKADKRRSVRIGSYIERDVTPAIMEDDELALDLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIKNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGIFLWELFSLGSSPYPGMPVDSKFYKMIKEGFRMLSPEHAPAEMYDIMKTCWDADPLKRPTFKQIVQLIEKQISESTNHIYSNLANCSPNRQKPVVDHSVRINSVGSTASSSQPLLVHDDV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P10721","disprot_id":"DP02247","ncbi_taxon_id":9606,"regions_counter":1,"creator":"mpajkos","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":565,"region_id":"DP02247r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of a c-kit product complex reveals the basis for kinase transactivation. <i> Mol CD, Lim KB, Sridhar V, Zou H, Chien EY, Sang BC, Nowakowski J, Kassel DB, Cronin CN, McRee DE. </i> J Biol Chem, 2003","statement":[{"text":"The structure of activated c-Kit kinase was determined (residues 544–935). This structure contains two c-Kit enzyme molecules in the asymmetric unit and clear electron density was observed for residues 566–935.\n\"The amino-terminal ∼20 amino acid residues of both enzymes are disordered\"","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"mpajkos","start":544,"term_ontology":"IDPO","curator_name":"Mátyás Pajkos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-5791-9825","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1PKG"}],"reference_id":"12824176","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P10721","date":"2018-08-30T14:56:41.000Z","acc":"P10721","name":"Mast/stem cell growth factor receptor Kit","length":976,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI000003F17D","genes":[{"name":{"value":"KIT"},"synonyms":[{"value":"SCFR"}]}],"alphafold_very_low_content":0.15778688524590165,"disorder_content":0.022540983606557378,"disprot_consensus":{"full":[{"start":544,"end":565,"type":"D"}],"Structural state":[{"start":544,"end":565,"type":"D"}]}},{"features":{"pfam":[{"id":"PF15862","name":"Coilin N-terminus","start":6,"end":196},{"id":"PF23086","name":"Coilin, C-terminal Tudor domain","start":407,"end":509}]},"uniref50":"UniRef50_Q8RWK8","sequence":"MEEEKVRVRLVFEDRRILSKYQKKQGLTRSWVVLNRKCHRTISEFSDHIFHTFSLCEACPHGLSLSMEGFVLPPFESSCVLKDKDIVCVKKKKESLLEIVGEDSDENVYNAIEVEERPQIRPGEMLLANEEFQKETGGYESESEEDELEEEAEEFVPEKKASKKRKTSSKNQSTKRKKCKLDTTEESPDERENTAVVSNVVKKKKKKKSLDVQSANNDEQNNDSTKPMTKSKRSSQQEESKEHNDLCQLSAETKKTPSRSARRKKAKRQWLREKTKLEKEELLQTQLVVAPSQKPVITIDHQATKEKHCETLENQQAEEVSDGFGDEVVPVEVRPGHIRFKPLAGTDEASLDSEPLVENVLWNGNMTKKKGQKWGTEKSGFSKRYAQDFNEDATTQPAEAETLANCPIDYEQLVAYTGSVKKGDVIAYRLIELTSSWTPEVSSFRVGKISYYDPDSKMVTLMPVQEFPIEKKTEEDDDFCMQPDTSLYKEDGSLEIEFSALLDVRSVKTSSSDSAEVAKSALPEPDQSAKKPKLSANKELQTPAKENGEVSPWEELSEALSAKKAALSQANNGWNKKGSSSGGSWSYKALRGSAMGPVMNYLRSQKEI","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q8RWK8","disprot_id":"DP02248","ncbi_taxon_id":3702,"regions_counter":8,"creator":"vpromp","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":350,"region_id":"DP02248r001","released":"2024_06","ec_id":"ECO:0006204","reference_html":"Plant coilin: structural characteristics and RNA-binding properties. <i> Makarov V, Rakitina D, Protopopova A, Yaminsky I, Arutiunian A, Love AJ, Taliansky M, Kalinina N. </i> PLoS One, 2013","statement":[{"text":"The IDD spectrum is quite different: the single negative maximum at 200 nm indicates that this domain contains long completely unfolded regions, and moreover, the overall low signal intensity suggests that β-strands are present in insignificant amounts judging from the form of the curve [32], [33].","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":117,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-23T16:19:44.439Z","reference_source":"pmid","term_name":"disorder","reference_id":"23320094","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The resulting proteins contained a 6×histidine sequence on the N-terminus."}]}]},{"start":117,"end":350,"reference_id":"23320094","reference_source":"pmid","reference_html":"Plant coilin: structural characteristics and RNA-binding properties. <i> Makarov V, Rakitina D, Protopopova A, Yaminsky I, Arutiunian A, Love AJ, Taliansky M, Kalinina N. </i> PLoS One, 2013","date":"2024-02-23T16:23:55.665Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The resulting proteins contained a 6×histidine sequence on the N-terminus."}]}],"region_id":"DP02248r003","statement":[{"text":"The spectrum of tryptophan fluorescence of the wt coilin has a peak at 347 nm, indicating both the hydrophilic environment of the tryptophan side chains and the poor formation of a globular hydrophobic core in the protein molecule. The central and C-terminal domains of coilin have fluorescence maxima at 350 nm for IDD and 354 nm for CTD, which indicates an even greater level of hydrophilicity in the local tryptophan environment.","type":"Results"}]},{"start":212,"end":350,"reference_id":"23320094","reference_source":"pmid","reference_html":"Plant coilin: structural characteristics and RNA-binding properties. <i> Makarov V, Rakitina D, Protopopova A, Yaminsky I, Arutiunian A, Love AJ, Taliansky M, Kalinina N. </i> PLoS One, 2013","date":"2024-02-23T16:41:36.544Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0030620","term_name":"U2 snRNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The resulting proteins contained a 6×histidine sequence on the N-terminus."}]}],"ec_go":"IPI","interaction_partner":[{"db":"RNAcentral","id":"URS0000444588_3702","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02248r004","statement":[{"text":"In this report we have tested the ability of coilin to directly interact with two snRNAs - U2 snRNA and U1 snRNA and a non-specific artificial RNA (160 nt).","type":"Results"},{"text":"In contrast, the IDD complexes with RNA enter into the agarose gel. In this case no free RNA remains in the gel at the protein:RNA molar ratio 2[ratio]1. Further addition of the protein gradually increases retardation of the complex. The apparent Kd (0.04 µM) is lower than that of the wt protein (Figure 3A). These results suggest that coilin has at least two RNA-binding sites.","type":"Results"},{"text":"The distal part of IDD (IDD-212-350) provides RNA binding similar to that of the intact IDD with a Kd of 0.06 uM (Figure 3A, ​,4C). Interestingly, the C-terminus of IDD (IDD-282-350) shows no ability to bind RNA (Figure 3A, ​,4C). Consequently the NLS2 plays a main role as an RNA-binding cluster.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a U2 small nuclear RNA (U2 snRNA).\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":212,"end":350,"reference_id":"23320094","reference_source":"pmid","reference_html":"Plant coilin: structural characteristics and RNA-binding properties. <i> Makarov V, Rakitina D, Protopopova A, Yaminsky I, Arutiunian A, Love AJ, Taliansky M, Kalinina N. </i> PLoS One, 2013","date":"2024-02-23T16:41:24.248Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0030619","term_name":"U1 snRNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The resulting proteins contained a 6×histidine sequence on the N-terminus."}]}],"ec_go":"IPI","interaction_partner":[{"db":"RNAcentral","id":"URS000037A8FF_3702","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02248r005","statement":[{"text":"In this report we have tested the ability of coilin to directly interact with two snRNAs - U2 snRNA and U1 snRNA and a non-specific artificial RNA (160 nt).","type":"Results"},{"text":"In contrast, the IDD complexes with RNA enter into the agarose gel. In this case no free RNA remains in the gel at the protein:RNA molar ratio 2[ratio]1. Further addition of the protein gradually increases retardation of the complex. The apparent Kd (0.04 µM) is lower than that of the wt protein (Figure 3A). These results suggest that coilin has at least two RNA-binding sites.","type":"Results"},{"text":"The distal part of IDD (IDD-212-350) provides RNA binding similar to that of the intact IDD with a Kd of 0.06 uM (Figure 3A, ​,4C). Interestingly, the C-terminus of IDD (IDD-282-350) shows no ability to bind RNA (Figure 3A, ​,4C). Consequently the NLS2 plays a main role as an RNA-binding cluster.","type":"Results"}],"term_comment":"Note that this term may be useful for annotating other small nuclear RNAs (snRNAs).","term_def":"\"Binding to a U1 small nuclear RNA (U1 snRNA).\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":212,"end":350,"reference_id":"23320094","reference_source":"pmid","reference_html":"Plant coilin: structural characteristics and RNA-binding properties. <i> Makarov V, Rakitina D, Protopopova A, Yaminsky I, Arutiunian A, Love AJ, Taliansky M, Kalinina N. </i> PLoS One, 2013","date":"2024-02-23T16:41:06.171Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The resulting proteins contained a 6×histidine sequence on the N-terminus."}]}],"ec_go":"IPI","region_id":"DP02248r006","statement":[{"text":"In this report we have tested the ability of coilin to directly interact with two snRNAs - U2 snRNA and U1 snRNA and a non-specific artificial RNA (160 nt).","type":"Results"},{"text":"In contrast, the IDD complexes with RNA enter into the agarose gel. In this case no free RNA remains in the gel at the protein:RNA molar ratio 2[ratio]1. Further addition of the protein gradually increases retardation of the complex. The apparent Kd (0.04 µM) is lower than that of the wt protein (Figure 3A). These results suggest that coilin has at least two RNA-binding sites.","type":"Results"},{"text":"The distal part of IDD (IDD-212-350) provides RNA binding similar to that of the intact IDD with a Kd of 0.06 uM (Figure 3A, ​,4C). Interestingly, the C-terminus of IDD (IDD-282-350) shows no ability to bind RNA (Figure 3A, ​,4C). Consequently the NLS2 plays a main role as an RNA-binding cluster.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":350,"end":409,"reference_id":"23320094","reference_source":"pmid","reference_html":"Plant coilin: structural characteristics and RNA-binding properties. <i> Makarov V, Rakitina D, Protopopova A, Yaminsky I, Arutiunian A, Love AJ, Taliansky M, Kalinina N. </i> PLoS One, 2013","date":"2024-02-23T17:00:52.892Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006216","ec_ontology":"ECO","ec_name":"author inference used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02248r007","statement":[{"text":"Using bioinformatic predictions of coilin structure, we suggest that Atcoilin contains two structural domains in the N-terminal part including an ordered domain on the N terminus (NOD) and a central internal disordered domain (IDD) and at least one domain in the C-terminal part (C-terminal domain, CTD) with a presumable Tudor-like structure abutting an intrinsically disordered C-terminus (Figure 1A).","type":"Results"},{"text":"The shift of a negative peak from 208 nm (which is characteristic for α-proteins) to 200 nm demonstrates that alongside the ordered secondary structure elements, the C-terminal domain also contains substantial unfolded regions, which likely correspond to the big loops between elements of the Tudor-like domain and also the long unfolded C-terminus.","type":"Results"},{"text":"All these residues are localized in unfolded regions of the CTD: one is within a loop between the Tudor fold β-sheets, two are more upstream, and the remainder is in the disordered extreme C-terminus.","type":"Results"},{"text":"The biophysical analysis assessed by circular dichroism and tryptophan fluorescence supports this region is disordered. Their combination with the the bioinformatic studies allows the authors to state that the CTD (350-608) contains a high degree of disorder interrupted by Tudor-like structured region (410-510).","type":"Curator statement"}]},{"start":511,"end":608,"reference_id":"23320094","reference_source":"pmid","reference_html":"Plant coilin: structural characteristics and RNA-binding properties. <i> Makarov V, Rakitina D, Protopopova A, Yaminsky I, Arutiunian A, Love AJ, Taliansky M, Kalinina N. </i> PLoS One, 2013","date":"2024-02-23T17:01:01.517Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006216","ec_ontology":"ECO","ec_name":"author inference used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02248r008","statement":[{"text":"Using bioinformatic predictions of coilin structure, we suggest that Atcoilin contains two structural domains in the N-terminal part including an ordered domain on the N terminus (NOD) and a central internal disordered domain (IDD) and at least one domain in the C-terminal part (C-terminal domain, CTD) with a presumable Tudor-like structure abutting an intrinsically disordered C-terminus (Figure 1A).","type":"Results"},{"text":"The shift of a negative peak from 208 nm (which is characteristic for α-proteins) to 200 nm demonstrates that alongside the ordered secondary structure elements, the C-terminal domain also contains substantial unfolded regions, which likely correspond to the big loops between elements of the Tudor-like domain and also the long unfolded C-terminus.","type":"Results"},{"text":"All these residues are localized in unfolded regions of the CTD: one is within a loop between the Tudor fold β-sheets, two are more upstream, and the remainder is in the disordered extreme C-terminus.","type":"Results"},{"text":"The biophysical analysis assessed by circular dichroism and tryptophan fluorescence supports this region is disordered. Their combination with the the bioinformatic studies allows the authors to state that the CTD (350-608) contains a high degree of disorder interrupted by Tudor-like structured region (410-510).","type":"Curator statement"}]}],"released":"2018_11","uniref100":"UniRef100_Q8RWK8","date":"2018-08-30T15:48:55.000Z","acc":"Q8RWK8","name":"Coilin","length":608,"organism":"Arabidopsis thaliana","dataset":["RNA-binding proteins"],"UniParc":"UPI00000A3D81","genes":[{"name":{"value":"COIL","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16624863","url":"http://www.ncbi.nlm.nih.gov/pubmed/16624863","alternativeUrl":"https://europepmc.org/abstract/MED/16624863"}}]},"orfNames":[{"value":"F3F19.5","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAD31056.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD31056.1"}}]}],"olnNames":[{"value":"At1g13030","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT1G13030","url":""}}]}]}],"alphafold_very_low_content":0.5,"disorder_content":0.6430921052631579,"disprot_consensus":{"full":[{"start":117,"end":409,"type":"D"},{"start":511,"end":608,"type":"D"}],"Structural state":[{"start":117,"end":409,"type":"D"},{"start":511,"end":608,"type":"D"}],"Molecular function":[{"start":212,"end":350,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00899","name":"ThiF family","start":309,"end":562},{"id":"PF16420","name":"Ubiquitin-like modifier-activating enzyme ATG7 N-terminus","start":8,"end":291}],"gene3D":[{"start":11,"end":263,"id":"3.40.140.100","name":"Ubiquitin-like modifier-activating enzyme ATG7 C-terminal domain"},{"start":13,"end":288,"id":"3.40.140.70","name":"Ubiquitin-like modifier-activating enzyme ATG7 N-terminal domain"},{"start":292,"end":630,"id":"3.40.50.720","name":"NAD(P)-binding Rossmann-like Domain"}]},"uniref50":"UniRef50_P38862","sequence":"MSSERVLSYAPAFKSFLDTSFFQELSRLKLDVLKLDSTCQPLTVNLDLHNIPKSADQVPLFLTNRSFEKHNNKRTNEVPLQGSIFNFNVLDEFKNLDKQLFLHQRALECWEDGIKDINKCVSFVIISFADLKKYRFYYWLGVPCFQRPSSTVLHVRPEPSLKGLFSKCQKWFDVNYSKWVCILDADDEIVNYDKCIIRKTKVLAIRDTSTMENVPSALTKNFLSVLQYDVPDLIDFKLLIIRQNEGSFALNATFASIDPQSSSSNPDMKVSGWERNVQGKLAPRVVDLSSLLDPLKIADQSVDLNLKLMKWRILPDLNLDIIKNTKVLLLGAGTLGCYVSRALIAWGVRKITFVDNGTVSYSNPVRQALYNFEDCGKPKAELAAASLKRIFPLMDATGVKLSIPMIGHKLVNEEAQHKDFDRLRALIKEHDIIFLLVDSRESRWLPSLLSNIENKTVINAALGFDSYLVMRHGNRDEQSSKQLGCYFCHDVVAPTDSLTDRTLDQMCTVTRPGVAMMASSLAVELMTSLLQTKYSGSETTVLGDIPHQIRGFLHNFSILKLETPAYEHCPACSPKVIEAFTDLGWEFVKKALEHPLYLEEISGLSVIKQEVERLGNDVFEWEDDESDEIA","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P38862","disprot_id":"DP02249","ncbi_taxon_id":559292,"regions_counter":2,"creator":"tszani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":630,"region_id":"DP02249r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis of Atg8 activation by a homodimeric E1, Atg7. <i> Noda NN, Satoo K, Fujioka Y, Kumeta H, Ogura K, Nakatogawa H, Ohsumi Y, Inagaki F. </i> Mol Cell, 2011","statement":[{"text":"Truncation and mutagenesis analyses clearly showed that the binding affinity of Atg7 for Atg8 is predominantly provided by the C-terminal tail of ECTD, especially by residues 618–630, which were observed in our NMR structure but disordered in the crystal structure.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"tszani","start":618,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22055191","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":630,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis of Atg8 activation by a homodimeric E1, Atg7. <i> Noda NN, Satoo K, Fujioka Y, Kumeta H, Ogura K, Nakatogawa H, Ohsumi Y, Inagaki F. </i> Mol Cell, 2011","statement":[{"text":"Truncation and mutagenesis analyses clearly showed that the binding affinity of Atg7 for Atg8 is predominantly provided by the C-terminal tail of ECTD, especially by residues 618–630, which were observed in our NMR structure but disordered in the crystal structure.","type":"Discussion"}],"term_id":"GO:0005515","curator_id":"tszani","start":618,"term_ontology":"GO","curator_name":"Tamás Szaniszló","reference_id":"22055191","version":3,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP02249r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P38862","date":"2018-08-30T15:52:08.000Z","acc":"P38862","name":"Ubiquitin-like modifier-activating enzyme ATG7","length":630,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":["Autophagy-related proteins"],"UniParc":"UPI0000125C64","genes":[{"name":{"value":"ATG7"},"synonyms":[{"value":"APG7"},{"value":"CVT2"}],"olnNames":[{"value":"YHR171W"}]}],"alphafold_very_low_content":0.015873015873015872,"disorder_content":0.020634920634920634,"disprot_consensus":{"full":[{"start":618,"end":630,"type":"D"}],"Structural state":[{"start":618,"end":630,"type":"D"}],"Molecular function":[{"start":618,"end":630,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00091","name":"Tubulin/FtsZ family, GTPase domain","start":3,"end":213},{"id":"PF03953","name":"Tubulin C-terminal domain","start":263,"end":392}],"gene3D":[{"start":269,"end":383,"id":"3.30.1330.20","name":"Tubulin/FtsZ, C-terminal domain"},{"start":1,"end":268,"id":"3.40.50.1440","name":"Tubulin/FtsZ, GTPase domain"},{"start":384,"end":450,"id":"1.10.287.600","name":"Helix hairpin bin"}]},"uniref50":"UniRef50_P68363","sequence":"MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P68363","disprot_id":"DP02251","ncbi_taxon_id":9606,"regions_counter":2,"creator":"tszani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":447,"region_id":"DP02251r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis for tubulin recognition by cytoplasmic linker protein 170 and its autoinhibition. <i> Mishima M, Maesaki R, Kasa M, Watanabe T, Fukata M, Kaibuchi K, Hakoshima T. </i> Proc Natl Acad Sci U S A, 2007","statement":[{"text":"The rms deviations of backbone and all heavy atoms over residues 212–281 of the CAP-Gly-2 domain and residues 448–451 of the peptide are 0.13 and 0.51 Å, respectively. The rest of the peptide residues are disordered even in complex with the CAP-Gly-2 domain.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"tszani","start":416,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"pdb","id":"2e4h"}],"reference_id":"17563362","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":447,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis for tubulin recognition by cytoplasmic linker protein 170 and its autoinhibition. <i> Mishima M, Maesaki R, Kasa M, Watanabe T, Fukata M, Kaibuchi K, Hakoshima T. </i> Proc Natl Acad Sci U S A, 2007","term_id":"GO:0005515","curator_id":"tszani","start":416,"term_ontology":"GO","curator_name":"Tamás Szaniszló","reference_id":"17563362","version":3,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP02251r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_P68363","date":"2018-08-30T16:10:12.000Z","acc":"P68363","name":"Tubulin alpha-1B chain","length":451,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000015EA","genes":[{"name":{"value":"TUBA1B"}}],"alphafold_very_low_content":0.031042128603104215,"disorder_content":0.07095343680709534,"disprot_consensus":{"full":[{"start":416,"end":447,"type":"D"}],"Structural state":[{"start":416,"end":447,"type":"D"}],"Molecular function":[{"start":416,"end":447,"type":"F"}]}},{"features":{"pfam":[{"id":"PF03853","name":"YjeF-related protein N-terminus","start":303,"end":465},{"id":"PF09532","name":"FDF domain","start":199,"end":300},{"id":"PF12701","name":"Scd6-like Sm domain","start":4,"end":66},{"id":"PF16598","name":"Linker region of enhancer of mRNA-decapping protein 3","start":103,"end":194}],"gene3D":[{"start":250,"end":508,"id":"3.40.50.10260","name":"YjeF N-terminal domain"},{"start":1,"end":82,"id":"2.30.30.100","name":"2.30.30.100"}]},"uniref50":"UniRef50_Q96F86","sequence":"MATDWLGSIVSINCGDSLGVYQGRVSAVDQVSQTISLTRPFHNGVKCLVPEVTFRAGDITELKILEIPGPGDNQHFGDLHQTELGPSGAGCQVGINQNGTGKFVKKPASSSSAPQNIPKRTDVKSQDVAVSPQQQQCSKSYVDRHMESLSQSKSFRRRHNSWSSSSRHPNQATPKKSGLKNGQMKNKDDECFGDDIEEIPDTDFDFEGNLALFDKAAVFEEIDTYERRSGTRSRGIPNERPTRYRHDENILESEPIVYRRIIVPHNVSKEFCTDSGLVVPSISYELHKKLLSVAEKHGLTLERRLEMTGVCASQMALTLLGGPNRLNPKNVHQRPTVALLCGPHVKGAQGISCGRHLANHDVQVILFLPNFVKMLESITNELSLFSKTQGQQVSSLKDLPTSPVDLVINCLDCPENVFLRDQPWYKAAVAWANQNRAPVLSIDPPVHEVEQGIDAKWSLALGLPLPLGEHAGRIYLCDIGIPQQVFQEVGINYHSPFGCKFVIPLHSA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q96F86","disprot_id":"DP02253","ncbi_taxon_id":9606,"regions_counter":4,"creator":"vpromp","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":258,"region_id":"DP02253r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of human Edc3 and its functional implications. <i> Ling SH, Decker CJ, Walsh MA, She M, Parker R, Song H. </i> Mol Cell Biol, 2008","statement":[{"text":"The N-terminal region encompassing the FDF motif (amino acids 203 to 258) is disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vpromp","start":203,"term_ontology":"IDPO","curator_name":"Vasilis J Promponas","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-3352-4831","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3D3J"}],"reference_id":"18678652","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":258,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Crystal structure of human Edc3 and its functional implications. <i> Ling SH, Decker CJ, Walsh MA, She M, Parker R, Song H. </i> Mol Cell Biol, 2008","term_id":"GO:0005515","curator_id":"vpromp","start":203,"term_ontology":"GO","curator_name":"Vasilis J Promponas","reference_id":"18678652","version":3,"curator_orcid":"0000-0003-3352-4831","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02253r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":258,"region_id":"DP02253r003","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural basis for the mutually exclusive anchoring of P body components EDC3 and Tral to the DEAD box protein DDX6/Me31B. <i> Tritschler F, Braun JE, Eulalio A, Truffault V, Izaurralde E, Weichenrieder O. </i> Mol Cell, 2009","term_id":"IDPO:0000002","curator_id":"vpromp","start":203,"term_ontology":"IDPO","curator_name":"Vasilis J Promponas","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-3352-4831","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2WAX"},{"db":"PDB","id":"2WAY"}],"reference_id":"19285948","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":258,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural basis for the mutually exclusive anchoring of P body components EDC3 and Tral to the DEAD box protein DDX6/Me31B. <i> Tritschler F, Braun JE, Eulalio A, Truffault V, Izaurralde E, Weichenrieder O. </i> Mol Cell, 2009","statement":[{"text":"Co-crystalisation with the human DDX6 C-terminal domain.","type":"Curator statement"}],"term_id":"GO:0005515","curator_id":"vpromp","start":203,"term_ontology":"GO","curator_name":"Vasilis J Promponas","reference_id":"19285948","version":3,"curator_orcid":"0000-0003-3352-4831","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"imex","id":"IM-23318-24635"}],"region_id":"DP02253r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q96F86","date":"2018-08-30T16:20:20.000Z","acc":"Q96F86","name":"Enhancer of mRNA-decapping protein 3","length":508,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000007309A","genes":[{"name":{"value":"EDC3"},"synonyms":[{"value":"LSM16"},{"value":"YJDC"},{"value":"YJEFN2"}],"orfNames":[{"value":"PP844"}]}],"alphafold_very_low_content":0.23228346456692914,"disorder_content":0.11023622047244094,"disprot_consensus":{"full":[{"start":203,"end":258,"type":"D"}],"Structural state":[{"start":203,"end":258,"type":"D"}],"Molecular function":[{"start":203,"end":258,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00018","name":"SH3 domain","start":162,"end":207},{"id":"PF00018","name":"SH3 domain","start":232,"end":277},{"id":"PF00787","name":"PX domain","start":31,"end":120},{"id":"PF08944","name":"NADPH oxidase subunit p47Phox, C terminal domain","start":358,"end":390},{"id":"PF16621","name":"Neutrophil cytosol factor 1, PBR/AIR","start":292,"end":339}],"gene3D":[{"start":1,"end":141,"id":"3.30.1520.10","name":"Phox-like domain"},{"start":148,"end":200,"id":"2.30.30.40","name":"SH3 Domains"},{"start":215,"end":282,"id":"2.30.30.40","name":"SH3 Domains"}]},"uniref50":"UniRef50_P14598","sequence":"MGDTFIRHIALLGFEKRFVPSQHYVYMFLVKWQDLSEKVVYRRFTEIYEFHKTLKEMFPIEAGAINPENRIIPHLPAPKWFDGQRAAENRQGTLTEYCSTLMSLPTKISRCPHLLDFFKVRPDDLKLPTDNQTKKPETYLMPKDGKSTATDITGPIILQTYRAIANYEKTSGSEMALSTGDVVEVVEKSESGWWFCQMKAKRGWIPASFLEPLDSPDETEDPEPNYAGEPYVAIKAYTAVEGDEVSLLEGEAVEVIHKLLDGWWVIRKDDVTGYFPSMYLQKSGQDVSQAQRQIKRGAPPRRSSIRNAHSIHQRSRKRLSQDAYRRNSVRFLQQRRRQARPGPQSPGSPLEEERQTQRSKPQPAVPPRPSADLILNRCSESTKRKLASAV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P14598","disprot_id":"DP02254","ncbi_taxon_id":9606,"regions_counter":13,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":228,"region_id":"DP02254r002","released":"2024_06","ec_id":"ECO:0006220","reference_html":"Molecular basis of phosphorylation-induced activation of the NADPH oxidase. <i> Groemping Y, Lapouge K, Smerdon SJ, Rittinger K. </i> Cell, 2003","statement":[{"text":"The SH3A-SH3B linker is disordered in one of the molecules in the asymmetric unit.","type":"Methods"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":213,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2024-02-29T06:53:57.601Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1NG2"}],"reference_id":"12732142","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T14:38:16.131Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":228,"region_id":"DP02254r003","released":"2024_06","ec_id":"ECO:0006165","reference_html":"NMR solution structure of the tandem Src homology 3 domains of p47phox complexed with a p22phox-derived proline-rich peptide. <i> Ogura K, Nobuhisa I, Yuzawa S, Takeya R, Torikai S, Saikawa K, Sumimoto H, Inagaki F. </i> J Biol Chem, 2006","statement":[{"text":"However, the linker region (residues 213-228) had different NOE intensities in the free and complex forms. In the free state, the linker region showed negative NOE intensities (Fig. 3a), indicating that this region is highly flexible.","type":"Results"},{"text":"Whereas both SH3 domains form well defined structural cores, the linker region is moderately disordered due to a lack of long-range NOEs, consistent with the smaller hetNOE intensities (Fig. 3b).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"fquaglia","start":213,"term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-0341-4888","date":"2024-02-29T06:51:55.022Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1WLP"}],"reference_id":"16326715","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T14:38:17.369Z"}},{"start":296,"end":330,"reference_id":"12732142","reference_source":"pmid","reference_html":"Molecular basis of phosphorylation-induced activation of the NADPH oxidase. <i> Groemping Y, Lapouge K, Smerdon SJ, Rittinger K. </i> Cell, 2003","date":"2024-02-23T11:29:58.318Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02254r004","statement":[{"text":"Circular dichroism studies show that peptide1 exists as a random coil in solution and does not have the same degree of helical structure as present in the auto-inhibited complex (data not shown).","type":"Results"},{"text":"The authors have previously specified that peptide 1 corresponds to residues 296-330.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T06:45:03.646Z"}},{"start":296,"end":330,"reference_id":"12732142","reference_source":"pmid","reference_html":"Molecular basis of phosphorylation-induced activation of the NADPH oxidase. <i> Groemping Y, Lapouge K, Smerdon SJ, Rittinger K. </i> Cell, 2003","date":"2024-02-23T11:31:57.395Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"1NG2"}],"region_id":"DP02254r005","statement":[{"text":"Circular dichroism studies show that peptide1 exists as a random coil in solution and does not have the same degree of helical structure as present in the auto-inhibited complex (data not shown). This suggests that the low affinity of this interaction is a consequence of formation of secondary structure for which an energetic penalty has to be paid. This interpretation is supported by our ITC studies that show that this interaction is entropically unfavored and entirely driven by the enthalpic contribution.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T06:45:08.317Z"}},{"start":296,"end":330,"reference_id":"12732142","reference_source":"pmid","reference_html":"Molecular basis of phosphorylation-induced activation of the NADPH oxidase. <i> Groemping Y, Lapouge K, Smerdon SJ, Rittinger K. </i> Cell, 2003","date":"2024-02-23T11:32:21.606Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"1NG2"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P14598","operator":null,"partner_start":156,"partner_end":285}],"region_id":"DP02254r006","statement":[{"text":"The structure reveals an unexpected mode of target recognition by SH3 domains in which the conserved ligand binding surfaces of both SH3 domains are juxtaposed so as to create a single binding groove that is occupied by the N-terminal portion of the polybasic region (Figures 2A and 2B).","type":"Results"},{"text":"After exiting the conserved, tandem SH3 domain binding groove the remainder of the polybasic region changes its direction to run along SH3A and make extensive contacts with this domain and the N-terminal portion of the SH3A-SH3B linker. This is followed by another turn that allows residues 310–330 to run across both SH3 domains, approximately parallel to the SH3A-SH3B linker.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T06:45:23.446Z"}},{"start":296,"end":330,"reference_id":"12732142","reference_source":"pmid","reference_html":"Molecular basis of phosphorylation-induced activation of the NADPH oxidase. <i> Groemping Y, Lapouge K, Smerdon SJ, Rittinger K. </i> Cell, 2003","date":"2024-02-23T11:28:22.693Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P14598","operator":null,"partner_start":156,"partner_end":285}],"region_id":"DP02254r007","statement":[{"text":"We measured the binding affinity of the tandem SH3 domains, as well as the individual SH3 domains to a 35-mer peptide comprising residues 296–330 of the polybasic region (peptide1) by isothermal titration calorimetry (ITC). Binding of this peptide to either of the isolated SH3 domains (termed SH3A and SH3B) was undetectable under the experimental conditions, while the tandem SH3 domains bound with a Kd of 1.5 μM and a 1:1 stoichiometry (Figure 1B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T06:45:25.387Z"}},{"start":296,"end":304,"reference_id":"12732142","reference_source":"pmid","reference_html":"Molecular basis of phosphorylation-induced activation of the NADPH oxidase. <i> Groemping Y, Lapouge K, Smerdon SJ, Rittinger K. </i> Cell, 2003","date":"2024-02-23T11:28:36.661Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P14598","operator":null,"partner_start":156,"partner_end":285}],"region_id":"DP02254r008","statement":[{"text":"The additional interactions between the tandem SH3 domains and the C-terminal portion of the polybasic region, outside of the conserved binding groove, are crucial for the auto-inhibited conformation as evidenced by the low affinity of 29 μM of a peptide comprising residues 296–304 (peptide 2) for the tandem SH3 domains (Figure 1B).","type":"Results"},{"text":"The authors refer back to Figure 1B which shows ITC data with measured affinities.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T06:45:27.660Z"}},{"start":343,"end":390,"reference_id":"30630949","reference_source":"pmid","reference_html":"Quantitative live-cell imaging and 3D modeling reveal critical functional features in the cytosolic complex of phagocyte NADPH oxidase. <i> Ziegler CS, Bouchab L, Tramier M, Durand D, Fieschi F, Dupré-Crochet S, Mérola F, Nüße O, Erard M. </i> J Biol Chem, 2019","date":"2024-02-23T13:29:32.213Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02254r009","statement":[{"text":"This model of truncated p47phox was then used as starting point for the fit of the experimental SAXS pattern of the full-length p47phox protein (Fig. 6B and Table S4), resulting in a set of full-length models carrying a mainly unstructured C-terminal part.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T06:45:05.942Z"}},{"start":343,"end":390,"reference_id":"30630949","reference_source":"pmid","reference_html":"Quantitative live-cell imaging and 3D modeling reveal critical functional features in the cytosolic complex of phagocyte NADPH oxidase. <i> Ziegler CS, Bouchab L, Tramier M, Durand D, Fieschi F, Dupré-Crochet S, Mérola F, Nüße O, Erard M. </i> J Biol Chem, 2019","date":"2024-02-23T13:46:32.076Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P19878","operator":null,"partner_start":1,"partner_end":526},{"db":"UniProt","id":"Q15080","operator":"and","partner_start":1,"partner_end":339}],"region_id":"DP02254r010","statement":[{"text":"The co-expression of p47phoxΔCter-CFP with p67phox-YFP gives clearly different FLIM images as compared with p47phox-CFP, with well-separated average lifetime distributions (Fig. 4, A and B), and measured Eapp values in the range of the first negative control (Fig. 4C and Fig. S3A). The observation of a plateau value for Eapp, well above the values of the controls, provides strong evidence for a specific interaction (17). The absence of significant FRET in the case of p47phoxΔCter shows in addition that the PRR domain of p47phox is required for this interaction in live cells.","type":"Results"},{"text":"We co-expressed p40phox and p47phox or its truncated version p47phoxΔCter with NC or CC labeling (Fig. 4, E and H). We found specific FRET in both cases with equivalent Eapp, which indicates that the FP tags at both termini of p40phox have a similar average geometry relative to the C terminus of p47phox. When p47phoxΔCter was used instead of full-length p47phox, no significant FRET was observed (Fig. 4E and Fig. S3C). This confirms the requirement of the PRR domain of p47phox for the interaction with p40phox in live cells.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T06:45:29.205Z"}},{"start":343,"end":390,"reference_id":"30630949","reference_source":"pmid","reference_html":"Quantitative live-cell imaging and 3D modeling reveal critical functional features in the cytosolic complex of phagocyte NADPH oxidase. <i> Ziegler CS, Bouchab L, Tramier M, Durand D, Fieschi F, Dupré-Crochet S, Mérola F, Nüße O, Erard M. </i> J Biol Chem, 2019","date":"2024-02-23T13:42:00.149Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006335","ec_ontology":"ECO","ec_name":"fluorescence correlation spectroscopy evidence","unpublished":true,"released":"2024_06","version":0,"interaction_partner":[{"db":"UniProt","id":"P19878","operator":null,"partner_start":1,"partner_end":526}],"region_id":"DP02254r011","statement":[{"text":"To evaluate independently the occurrence of an interaction between p47phox and p67phox tagged at their N termini, we used FCCS. In this technique, the fluctuations of the fluorescence intensities of FP-tagged p47phox and p67phox diffusing in and out a confocal volume in the cytosol of COS7 cells are analyzed by auto- and cross-correlation functions (see “Experimental procedures”). A cross-correlation function with a non-null amplitude was observed for p47phox and p67phox tagged either at their CC and NN termini (Fig. 5A), showing in both cases a co-diffusion of the fluorophores indicative of complex formation.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T06:45:31.149Z"}},{"start":213,"end":228,"reference_id":"16326715","reference_source":"pmid","reference_html":"NMR solution structure of the tandem Src homology 3 domains of p47phox complexed with a p22phox-derived proline-rich peptide. <i> Ogura K, Nobuhisa I, Yuzawa S, Takeya R, Torikai S, Saikawa K, Sumimoto H, Inagaki F. </i> J Biol Chem, 2006","date":"2024-02-29T06:51:31.285Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"1WLP"}],"region_id":"DP02254r012","statement":[{"text":"However, the linker region (residues 213-228) had different NOE intensities in the free and complex forms. In the free state, the linker region showed negative NOE intensities (Fig. 3a), indicating that this region is highly flexible.","type":"Results"},{"text":"Whereas both SH3 domains form well defined structural cores, the linker region is moderately disordered due to a lack of long-range NOEs, consistent with the smaller hetNOE intensities (Fig. 3b). forms.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T14:38:12.128Z"}},{"start":343,"end":390,"reference_id":"30630949","reference_source":"pmid","reference_html":"Quantitative live-cell imaging and 3D modeling reveal critical functional features in the cytosolic complex of phagocyte NADPH oxidase. <i> Ziegler CS, Bouchab L, Tramier M, Durand D, Fieschi F, Dupré-Crochet S, Mérola F, Nüße O, Erard M. </i> J Biol Chem, 2019","date":"2025-04-25T22:05:24.385Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP02254r013","statement":[{"text":"This model of truncated p47phox was then used as starting point for the fit of the experimental SAXS pattern of the full-length p47phox protein (Fig. 6B and Table S4), resulting in a set of full-length models carrying a mainly unstructured C-terminal part.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T22:27:07.562Z"}}],"released":"2018_11","uniref100":"UniRef100_P14598","date":"2018-08-30T16:23:29.000Z","acc":"P14598","name":"Neutrophil cytosol factor 1","length":390,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000059C546","genes":[{"name":{"value":"NCF1"},"synonyms":[{"value":"NOXO2"},{"value":"SH3PXD1A"}]}],"alphafold_very_low_content":0.08205128205128205,"disorder_content":0.25384615384615383,"disprot_consensus":{"full":[{"start":213,"end":228,"type":"D"},{"start":296,"end":330,"type":"T"},{"start":343,"end":390,"type":"D"}],"Structural state":[{"start":213,"end":228,"type":"D"},{"start":296,"end":330,"type":"D"},{"start":343,"end":390,"type":"D"}],"Structural transition":[{"start":296,"end":330,"type":"T"}],"Molecular function":[{"start":296,"end":330,"type":"F"},{"start":343,"end":390,"type":"F"}],"Disorder function":[{"start":213,"end":228,"type":"F"},{"start":343,"end":390,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00518","name":"Early Protein (E6)","start":30,"end":139}],"gene3D":[{"start":80,"end":151,"id":"3.30.240.40","name":"E6 early regulatory protein"},{"start":1,"end":79,"id":"3.30.240.40","name":"E6 early regulatory protein"}]},"uniref50":"UniRef50_P06427","sequence":"MFEDKRERPRTLHELCEALNVSMHNIQVVCVYCKKELCRADVYNVAFTEIKIVYRDNNPYAVCKQCLLFYSKIREYRRYSRSVYGTTLEAITKKSLYDLSIRCHRCQRPLGPEEKQKLVDEKKRFHEIAGRWTGQCANCWQRTRQRNETQV","taxonomy":["Viruses","Monodnaviria","Shotokuvirae","Cossaviricota","Papovaviricetes","Zurhausenvirales","Papillomaviridae","Firstpapillomavirinae","Alphapapillomavirus"],"uniref90":"UniRef90_P26554","disprot_id":"DP02256","ncbi_taxon_id":10595,"regions_counter":6,"creator":"sventura","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":151,"region_id":"DP02256r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural insights into a wildtype domain of the oncoprotein E6 and its interaction with a PDZ domain. <i> Mischo A, Ohlenschläger O, Hortschansky P, Ramachandran R, Görlach M. </i> PLoS One, 2013","statement":[{"text":"The calculated structural ensemble (Figure 3a) exhibits a backbone r.m.s.d. of 0.62 Å for the structured 51Z2 region (residues 80 to 140 of the full length E6) while the backbone r.m.s.d. drops to 2.37 Å when including the less ordered E6 C-terminus (residues 141–151, numbering according to full-length sequence). This C-terminus gave rise to only few NOEs consistent with a less ordered organization.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":141,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"BMRB","id":"18967"},{"db":"PDB","id":"2M3L"}],"reference_id":"23638119","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-28T07:06:23.755Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":151,"term_name":"disorder to order","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural insights into a wildtype domain of the oncoprotein E6 and its interaction with a PDZ domain. <i> Mischo A, Ohlenschläger O, Hortschansky P, Ramachandran R, Görlach M. </i> PLoS One, 2013","statement":[{"text":"An interaction is observed, as several chemical shifts of amide groups arising from the C-terminus of 51Z2 were perturbed in presence of hDlgPDZ2 (Figure 4a). Surprisingly, the perturbation affected the C-terminal nine E6 residues (143 to 151), more than anticipated from either the canonical PDZ-BM or from the already published hDlgPDZ2-E6 peptide complex structures [52], [53]. Importantly, no further E6 resonances experienced chemical shift perturbation, clearly indicating that the interaction with the hDlgPDZ2 is confined to the disordered C-terminal region harboring the PDZ-BM of HPV51 E6.","type":"Results"},{"text":"The malleability of E6 is reminiscent of intrinsically disordered proteins that undergo a disorder-to-order transition upon productive complex formation with specific ligands [67].","type":"Discussion"}],"term_id":"IDPO:0000011","curator_id":"vnugnes","start":141,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"23638119","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP02256r002","cross_refs":[{"db":"PDB","id":"2M3M"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-28T07:06:29.383Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":141,"end":151,"reference_id":"23638119","reference_source":"pmid","reference_html":"Structural insights into a wildtype domain of the oncoprotein E6 and its interaction with a PDZ domain. <i> Mischo A, Ohlenschläger O, Hortschansky P, Ramachandran R, Görlach M. </i> PLoS One, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2M3M"}],"interaction_partner":[{"db":"UniProt","id":"Q12959","partner_start":318,"partner_end":406}],"region_id":"DP02256r003","statement":[{"text":"An interaction is observed, as several chemical shifts of amide groups arising from the C-terminus of 51Z2 were perturbed in presence of hDlgPDZ2 (Figure 4a). Surprisingly, the perturbation affected the C-terminal nine E6 residues (143 to 151), more than anticipated from either the canonical PDZ-BM or from the already published hDlgPDZ2-E6 peptide complex structures [52], [53]. Importantly, no further E6 resonances experienced chemical shift perturbation, clearly indicating that the interaction with the hDlgPDZ2 is confined to the disordered C-terminal region harboring the PDZ-BM of HPV51 E6.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-28T07:07:13.620Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":141,"end":151,"reference_id":"23638119","reference_source":"pmid","reference_html":"Structural insights into a wildtype domain of the oncoprotein E6 and its interaction with a PDZ domain. <i> Mischo A, Ohlenschläger O, Hortschansky P, Ramachandran R, Görlach M. </i> PLoS One, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"Q12959","partner_start":318,"partner_end":406}],"region_id":"DP02256r004","statement":[{"text":"The SPR data indicate a contribution to binding of the additional residues as the E6CT11 binds with higher affinity to hDlgPDZ2 than the E6CT6 (Kd 9.6 µM versus 28.3 µM, respectively; Figure 5).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-28T07:07:12.546Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":141,"end":151,"reference_id":"23638119","reference_source":"pmid","reference_html":"Structural insights into a wildtype domain of the oncoprotein E6 and its interaction with a PDZ domain. <i> Mischo A, Ohlenschläger O, Hortschansky P, Ramachandran R, Görlach M. </i> PLoS One, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0030162","term_name":"regulation of proteolysis","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2M3M"}],"region_id":"DP02256r005","statement":[{"text":"An interaction is observed, as several chemical shifts of amide groups arising from the C-terminus of 51Z2 were perturbed in presence of hDlgPDZ2 (Figure 4a). Surprisingly, the perturbation affected the C-terminal nine E6 residues (143 to 151), more than anticipated from either the canonical PDZ-BM or from the already published hDlgPDZ2-E6 peptide complex structures [52], [53]. Importantly, no further E6 resonances experienced chemical shift perturbation, clearly indicating that the interaction with the hDlgPDZ2 is confined to the disordered C-terminal region harboring the PDZ-BM of HPV51 E6.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-28T07:07:19.863Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of the hydrolysis of a peptide bond or bonds within a protein.\" [GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2018_11","uniref100":"UniRef100_P26554","date":"2018-08-30T16:52:45.000Z","acc":"P26554","name":"Protein E6","length":151,"organism":"Human papillomavirus type 51","dataset":["Viral proteins"],"UniParc":"UPI00001383DC","genes":[{"name":{"value":"E6","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04006","url":"https://hamap.expasy.org/unirule/MF_04006"}}]}}],"disorder_content":0.0728476821192053,"disprot_consensus":{"full":[{"start":141,"end":151,"type":"T"}],"Structural state":[{"start":141,"end":151,"type":"D"}],"Structural transition":[{"start":141,"end":151,"type":"T"}],"Molecular function":[{"start":141,"end":151,"type":"F"}],"Biological process":[{"start":141,"end":151,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01641","name":"SelR domain","start":12,"end":105}],"gene3D":[{"start":8,"end":112,"id":"2.170.150.20","name":"Peptide methionine sulfoxide reductase."}]},"uniref50":"UniRef50_Q9JLC3","sequence":"MSFCSFFGGEVFQNHFEPGVYVCAKCSYELFSSHSKYAHSSPWPAFTETIHPDSVTKCPEKNRPEALKVSCGKCGNGLGHEFLNDGPKRGQSRFUIFSSSLKFVPKGKEAAASQGH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q9JLC3","disprot_id":"DP02258","ncbi_taxon_id":10090,"regions_counter":3,"creator":"npalopoli","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":18,"region_id":"DP02258r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Insights into function, catalytic mechanism, and fold evolution of selenoprotein methionine sulfoxide reductase B1 through structural analysis. <i> Aachmann FL, Sal LS, Kim HY, Marino SM, Gladyshev VN, Dikiy A. </i> J Biol Chem, 2010","statement":[{"text":"Both N-terminal (amino acids 1–18) and C-terminal (amino acids 105–116) regions are flexible ... This observation is consistent with the 15N-{H} NOE and 15N backbone relaxation data.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"npalopoli","start":1,"term_ontology":"IDPO","curator_name":"Nicolás Palopoli","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7925-6436","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2KV1"}],"reference_id":"20605785","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":44,"region_id":"DP02258r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Insights into function, catalytic mechanism, and fold evolution of selenoprotein methionine sulfoxide reductase B1 through structural analysis. <i> Aachmann FL, Sal LS, Kim HY, Marino SM, Gladyshev VN, Dikiy A. </i> J Biol Chem, 2010","statement":[{"text":"A more disordered region, consisting of 13 residues (amino acids 31–44) between beta2- and beta3-strands, connects front side and back side beta-sheets of the protein.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"npalopoli","start":31,"term_ontology":"IDPO","curator_name":"Nicolás Palopoli","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7925-6436","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2KV1"}],"reference_id":"20605785","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":116,"region_id":"DP02258r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Insights into function, catalytic mechanism, and fold evolution of selenoprotein methionine sulfoxide reductase B1 through structural analysis. <i> Aachmann FL, Sal LS, Kim HY, Marino SM, Gladyshev VN, Dikiy A. </i> J Biol Chem, 2010","statement":[{"text":"Both N-terminal (amino acids 1–18) and C-terminal (amino acids 105–116) regions are flexible ... This observation is consistent with the 15N-{H} NOE and 15N backbone relaxation data.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"npalopoli","start":105,"term_ontology":"IDPO","curator_name":"Nicolás Palopoli","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-7925-6436","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2KV1"}],"reference_id":"20605785","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9JLC3","date":"2018-08-30T22:30:50.000Z","acc":"Q9JLC3","name":"Methionine-R-sulfoxide reductase B1","length":116,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000161D0C","genes":[{"name":{"value":"Msrb1"},"synonyms":[{"value":"Sepr"},{"value":"Sepx1"}]}],"disorder_content":0.3793103448275862,"disprot_consensus":{"full":[{"start":1,"end":18,"type":"D"},{"start":31,"end":44,"type":"D"},{"start":105,"end":116,"type":"D"}],"Structural state":[{"start":1,"end":18,"type":"D"},{"start":31,"end":44,"type":"D"},{"start":105,"end":116,"type":"D"}]}},{"features":{"pfam":[{"id":"PF15511","name":"Centromere kinetochore component CENP-T histone fold","start":36,"end":96}],"gene3D":[{"start":2,"end":103,"id":"1.10.20.10","name":"Histone, subunit A"}]},"uniref50":"UniRef50_P02309","sequence":"MSGRGKGGKGLGKGGAKRHRKILRDNIQGITKPAIRRLARRGGVKRISGLIYEEVRAVLKSFLESVIRDSVTYTEHAKRKTVTSLDVVYALKRQGRTLYGFGG","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P02309","disprot_id":"DP02260","ncbi_taxon_id":559292,"regions_counter":6,"creator":"jpujols","regions":[{"start":1,"end":18,"reference_id":"11566884","reference_source":"pmid","reference_html":"Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions. <i> White CL, Suto RK, Luger K. </i> EMBO J, 2001","date":"2026-05-07T17:12:12.220Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"1ID3"}],"region_id":"DP02260r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04911"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02294"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61830"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"The histone proteins were refolded to a histone octamer, and reconstituted into nucleosome core particles using a 146 bp palindromic DNA fragment derived from human α-satellite regions (Luger et al., 1997a)."},{"type":"Curator statement","text":"DNA with sequence: 5'-\nATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGGAAACTGCTCCATCAAAAGGCATGTTCAGCGGAATTCCGCTGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTGGTAGAATCTGCAGGTGGATATTGAT"}]}],"statement":[{"text":"cAtomic model: 757 amino acids (H2A, 15–124; H2A′, 12–119; H2B, 30–122; H2B′, 29–124; H3, 38–134; H3′, 38–134; H4, 24–102; H4′, 18–102), 60 water molecules and 17 manganese ions (a total of 12 129 atoms). The remainder of the histone tails was too disordered to be included in the final model.","type":"Figure"},{"text":"However, the histone tails quickly become disordered as they extend past the DNA superhelix.","type":"Results"},{"text":"We show for the first time that the H4 N-terminal tail can assume completely different conformations depending upon the structural context. We have evidence that this holds true for all histone tails (unpublished data). This structural heterogeneity might allow the histone tails to interact with a variety of different protein factors and to perform a large number of different functions (Hansen et al., 1998).","type":"Discussion"}]},{"start":1,"end":18,"reference_id":"11566884","reference_source":"pmid","reference_html":"Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions. <i> White CL, Suto RK, Luger K. </i> EMBO J, 2001","date":"2026-05-07T17:12:23.572Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"1ID3"}],"region_id":"DP02260r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04911"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02294"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61830"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"The histone proteins were refolded to a histone octamer, and reconstituted into nucleosome core particles using a 146 bp palindromic DNA fragment derived from human α-satellite regions (Luger et al., 1997a)."},{"type":"Curator statement","text":"DNA with sequence: 5'-\nATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGGAAACTGCTCCATCAAAAGGCATGTTCAGCGGAATTCCGCTGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTGGTAGAATCTGCAGGTGGATATTGAT"}]}],"statement":[{"text":"cAtomic model: 757 amino acids (H2A, 15–124; H2A′, 12–119; H2B, 30–122; H2B′, 29–124; H3, 38–134; H3′, 38–134; H4, 24–102; H4′, 18–102), 60 water molecules and 17 manganese ions (a total of 12 129 atoms). The remainder of the histone tails was too disordered to be included in the final model.","type":"Figure"},{"text":"However, the histone tails quickly become disordered as they extend past the DNA superhelix.","type":"Results"},{"text":"We show for the first time that the H4 N-terminal tail can assume completely different conformations depending upon the structural context. We have evidence that this holds true for all histone tails (unpublished data). This structural heterogeneity might allow the histone tails to interact with a variety of different protein factors and to perform a large number of different functions (Hansen et al., 1998).","type":"Discussion"}]}],"released":"2018_11","uniref100":"UniRef100_P02309","date":"2018-08-31T01:56:44.000Z","acc":"P02309","name":"Histone H4","length":103,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000111D40","genes":[{"name":{"value":"HHF1"},"orfNames":[{"value":"YBR0122"}],"olnNames":[{"value":"YBR009C"}]},{"name":{"value":"HHF2"},"orfNames":[{"value":"N2752"}],"olnNames":[{"value":"YNL030W"}]}],"alphafold_very_low_content":0.009708737864077669,"disorder_content":0.17475728155339806,"disprot_consensus":{"full":[{"start":1,"end":18,"type":"D"}],"Structural state":[{"start":1,"end":18,"type":"D"}],"Disorder function":[{"start":1,"end":18,"type":"F"}]}},{"acc":"P13848","sequence":"MPLKPEEHEDILNKLLDPELAQSERTEALQQLRVNYGSFVSEYNDLTKSHEKLAAEKDDLIVSNSKLFRQIGLTDKQEEDHKKADISETITIEDLEAK","creator":"jpujols","dataset":["Viral proteins"],"date":"2018-08-31T03:33:08.000Z","disprot_id":"DP02261","features":{"pfam":[{"id":"PF11418","name":"Phi29 scaffolding protein","start":2,"end":98}],"gene3D":[{"start":2,"end":78,"id":"1.20.5.400","name":"1.20.5.400","_id":"685af523b4ac24d5329d9430"}]},"genes":[{"name":{"value":"7","evidences":[],"_id":"685af523b4ac24d5329d944f"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d944e"}],"length":98,"name":"Capsid assembly scaffolding protein","ncbi_taxon_id":10756,"organism":"Bacillus phage phi29","regions_counter":7,"released":"2018_11","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Uroviricota","Caudoviricetes","Caudovirales","Podoviridae","Picovirinae","Salasvirus"],"UniParc":"UPI000013861E","uniref100":"UniRef100_P13848","uniref50":"UniRef50_P13848","uniref90":"UniRef90_P13848","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1NO4","_id":"685af523b4ac24d5329d943e"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":79,"end":98,"interaction_partner":[],"reference_html":"Bacteriophage phi29 scaffolding protein gp7 before and after prohead assembly. <i> Morais MC, Kanamaru S, Badasso MO, Koti JS, Owen BA, McMurray CT, Anderson DL, Rossmann MG. </i> Nat Struct Biol, 2003","reference_id":"12778115","region_id":"DP02261r005","released":"2022_03","sample":[],"sequence_construct":"PLKPEEHEDILNKLLDPELAQSERTEALQQLRVNYGSFVSEYNDLTKSHEKLAAEKDDLIVSNSKLFRQIGLTEKQEEDHKKADISETITIEDLEAK","statement":[{"type":"Results","text":"The terminal 15 residues are disordered","_id":"685af523b4ac24d5329d943f"},{"type":"Curator statement","text":"The authors refers to the 80-98 region of this Uniprot, which has an extra methionine as a first residue, unlike the peptide they assessed.","_id":"685af523b4ac24d5329d9440"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-06T08:36:44.877Z","_id":"685af523b4ac24d5329d9441"},"version":1,"_id":"685af523b4ac24d5329d943d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":80,"end":98,"interaction_partner":[],"reference_html":"Molecular dissection of ø29 scaffolding protein function in an in vitro assembly system. <i> Fu CY, Morais MC, Battisti AJ, Rossmann MG, Prevelige PE. </i> J Mol Biol, 2007","reference_id":"17198713","region_id":"DP02261r006","released":"2022_03","sample":[{"db":"UniProt","deviation":null,"id":"P13849","statements":[{"type":"Methods","text":"360 μl of 10.2% PEG-3350 in 100 mM Tris, pH 8, 10 mM MgCl2 was added to the cuvette and allowed to temperature equilibrate to 13°C. 45 ul of scaffolding protein and 120 ul of capsid protein were mixed subsequently to give a final buffer composition of 7%PEG-3350, 100 mM Tris, pH 8, 10 mM MgCl2 and 38 mM NaCl. The assembly kinetics was monitored by recording the turbidity at 340 nm at 40 second intervals for 2 hours using the Beckman DU640 spectrometer.","_id":"685af523b4ac24d5329d9446"}],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d9445"}],"statement":[{"type":"Results","text":"In the first of these mutants the disordered C-terminal, residues 79-97 were deleted (Δ79-97 mutant), and in the second mutant residues 62-97, which comprises the last three helical turns of helix 3, were deleted. Both C-terminal deletions abolished the assembly activity (Fig 6).","_id":"685af523b4ac24d5329d9443"},{"type":"Curator statement","text":"The authors refers to the 80-98 region of this Uniprot, which has an extra methionine as a first residue, unlike the peptide they assessed.","_id":"685af523b4ac24d5329d9444"}],"states_connection":[],"term_comment":"","term_def":"\"A late phase of the viral life cycle during which all the components necessary for the formation of a mature virion collect at a particular site in the cell and the basic structure of the virus particle is formed.\" [ISBN:0121585336]","term_go_domain":"P","term_id":"GO:0019068","term_is_binding":false,"term_is_obsolete":false,"term_name":"virion assembly","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-06T08:37:04.196Z","_id":"685af523b4ac24d5329d9447"},"version":1,"_id":"685af523b4ac24d5329d9442","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1NOH","_id":"685af523b4ac24d5329d9449"},{"db":"PDB","id":"1NO4","_id":"685af523b4ac24d5329d944a"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":79,"end":98,"interaction_partner":[],"reference_html":"Bacteriophage phi29 scaffolding protein gp7 before and after prohead assembly. <i> Morais MC, Kanamaru S, Badasso MO, Koti JS, Owen BA, McMurray CT, Anderson DL, Rossmann MG. </i> Nat Struct Biol, 2003","reference_id":"12778115","region_id":"DP02261r007","released":"2022_03","sample":[],"sequence_construct":"PLKPEEHEDILNKLLDPELAQSERTEALQQLRVNYGSFVSEYNDLTKSHEKLAAEKDDLIVSNSKLFRQIGLTEKQEEDHKKADISETITIEDLEAK","statement":[{"type":"Results","text":"The terminal 15 residues are disordered.","_id":"685af523b4ac24d5329d944b"},{"type":"Curator statement","text":"The PDBs show the protein lacks electron density starting from the residue 79 when assessed by X-ray.","_id":"685af523b4ac24d5329d944c"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-06T08:36:27.837Z","_id":"685af523b4ac24d5329d944d"},"version":1,"_id":"685af523b4ac24d5329d9448","reference_source":"pmid"}],"__v":0,"disorder_content":0.20408163265306123,"disprot_consensus":{"full":[{"start":79,"end":98,"type":"D"}],"Structural state":[{"start":79,"end":98,"type":"D"}],"Disorder function":[{"start":79,"end":98,"type":"F"}],"Biological process":[{"start":80,"end":98,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00017","name":"SH2 domain","start":538,"end":616},{"id":"PF01017","name":"STAT transcription factor, coiled-coil domain","start":182,"end":242},{"id":"PF02864","name":"STAT protein, DNA binding domain","start":277,"end":413},{"id":"PF02865","name":"STAT protein, protein interaction domain","start":2,"end":113},{"id":"PF14596","name":"STAT6 C-terminal","start":655,"end":847},{"id":"PF21354","name":"Signal transducer and activator of transcription, linker domain","start":436,"end":518}],"gene3D":[{"start":542,"end":649,"id":"3.30.505.10","name":"SH2 domain"},{"start":1,"end":112,"id":"1.10.532.10","name":"STAT transcription factor, N-terminal domain"},{"start":274,"end":415,"id":"2.60.40.630","name":"STAT transcription factor, DNA-binding domain"},{"start":416,"end":536,"id":"1.10.238.10","name":"EF-hand"},{"start":113,"end":273,"id":"1.20.1050.20","name":"STAT transcription factor, all-alpha domain"}]},"uniref50":"UniRef50_P42226","sequence":"MSLWGLVSKMPPEKVQRLYVDFPQHLRHLLGDWLESQPWEFLVGSDAFCCNLASALLSDTVQHLQASVGEQGEGSTILQHISTLESIYQRDPLKLVATFRQILQGEKKAVMEQFRHLPMPFHWKQEELKFKTGLRRLQHRVGEIHLLREALQKGAEAGQVSLHSLIETPANGTGPSEALAMLLQETTGELEAAKALVLKRIQIWKRQQQLAGNGAPFEESLAPLQERCESLVDIYSQLQQEVGAAGGELEPKTRASLTGRLDEVLRTLVTSCFLVEKQPPQVLKTQTKFQAGVRFLLGLRFLGAPAKPPLVRADMVTEKQARELSVPQGPGAGAESTGEIINNTVPLENSIPGNCCSALFKNLLLKKIKRCERKGTESVTEEKCAVLFSASFTLGPGKLPIQLQALSLPLVVIVHGNQDNNAKATILWDNAFSEMDRVPFVVAERVPWEKMCETLNLKFMAEVGTNRGLLPEHFLFLAQKIFNDNSLSMEAFQHRSVSWSQFNKEILLGRGFTFWQWFDGVLDLTKRCLRSYWSDRLIIGFISKQYVTSLLLNEPDGTFLLRFSDSEIGGITIAHVIRGQDGSPQIENIQPFSAKDLSIRSLGDRIRDLAQLKNLYPKKPKDEAFRSHYKPEQMGKDGRGYVPATIKMTVERDQPLPTPELQMPTMVPSYDLGMAPDSSMSMQLGPDMVPQVYPPHSHSIPPYQGLSPEESVNVLSAFQEPHLQMPPSLGQMSLPFDQPHPQGLLPCQPQEHAVSSPDPLLCSDVTMVEDSCLSQPVTAFPQGTWIGEDIFPPLLPPTEQDLTKLLLEGQGESGGGSLGAQPLLQPSHYGQSGISMSHMDLRANPSW","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P42226","disprot_id":"DP02262","ncbi_taxon_id":9606,"regions_counter":10,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":814,"region_id":"DP02262r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Insight into the molecular recognition mechanism of the coactivator NCoA1 by STAT6. <i> Russo L, Giller K, Pfitzner E, Griesinger C, Becker S. </i> Sci Rep, 2017","statement":[{"text":"The 1H,15N-HSQC spectrum of 15N-13C-labeled STAT6783–814 (SI Fig. 1) shows narrow dispersion of signals in both proton and nitrogen dimensions indicating that the peptide adopts an unstructured conformation in absence of the binding partner.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"esalladini","start":783,"term_ontology":"IDPO","curator_name":"Edoardo Salladini","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29203888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T20:26:33.044Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":814,"term_name":"protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Insight into the molecular recognition mechanism of the coactivator NCoA1 by STAT6. <i> Russo L, Giller K, Pfitzner E, Griesinger C, Becker S. </i> Sci Rep, 2017","statement":[{"text":"Altogether, the NMR structure indicates that the coactivator recognition mechanism by STAT6 occurs by the formation of a complex in which two folded regions are connected by a linker that adopts an extended conformation","type":"Discussion"},{"text":"The NMR structure of the NCoA1257–385/STAT6783–814 complex (PDB ID: 5NWM), is of high quality (Table SI 4).","type":"Results"}],"term_id":"GO:0005515","curator_id":"esalladini","start":783,"term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"29203888","version":4,"curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP02262r002","cross_refs":[{"db":"PDB","id":"5NWM"}],"interaction_partner":[{"db":"UniProt","id":"Q15788","partner_start":null,"partner_end":null}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T20:25:48.932Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":799,"region_id":"DP02262r004","released":"2022_06","ec_id":"ECO:0006165","reference_html":"Insight into the molecular recognition mechanism of the coactivator NCoA1 by STAT6. <i> Russo L, Giller K, Pfitzner E, Griesinger C, Becker S. </i> Sci Rep, 2017","statement":[{"text":"the NMR structure indicates that the coactivator recognition mechanism by STAT6 occurs by the formation of a complex in which two folded regions are connected by a linker that adopts an extended conformation.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":790,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-06-16T17:52:59.525Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5NWM"}],"reference_id":"29203888","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15788","statements":[{"type":"Results","text":"The NMR structure of the NCoA1257–385/STAT6783–814 complex (PDB ID: 5NWM), is of high quality (Table SI 4)."}]}]},{"start":783,"end":793,"reference_id":"29203888","reference_source":"pmid","reference_html":"Insight into the molecular recognition mechanism of the coactivator NCoA1 by STAT6. <i> Russo L, Giller K, Pfitzner E, Griesinger C, Becker S. </i> Sci Rep, 2017","date":"2022-06-16T17:51:27.531Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_06","version":3,"cross_refs":[{"db":"PDB","id":"5NWX"}],"region_id":"DP02262r006","statement":[{"text":"In this crystal structure the residues located in the N-terminal part (Gly783 - Pro793) are not ordered indicating that this region is too dynamic to be resolved in the crystal (SI Fig. 3).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P70365","statements":[{"type":"Results","text":"In order to understand the increase of affinity of the STAT6783–814 peptide compared to the STAT6794–814 peptide in complex with NCoA1 by a factor of 10 we first solved the crystal structure of the NCoA-1 PAS-B domain in complex with the STAT6783–814 peptide (PDB ID: 5NWX) (SI Tables 2 and 3)."}]}]},{"start":786,"end":808,"reference_id":"29203888","reference_source":"pmid","reference_html":"Insight into the molecular recognition mechanism of the coactivator NCoA1 by STAT6. <i> Russo L, Giller K, Pfitzner E, Griesinger C, Becker S. </i> Sci Rep, 2017","date":"2022-06-16T17:54:37.686Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_06","version":3,"cross_refs":[{"db":"PDB","id":"5NWM"}],"region_id":"DP02262r007","statement":[{"text":"A subset of STAT6783–814 backbone amide resonances becomes well dispersed in the presence of the binding partner (Fig. 3A). These changes are indicative of a well-structured region within the bound STAT6783–814 peptide.","type":"Results"},{"text":"Regarding the STAT6783–814 peptide in the bound form, the analysis from chemical shifts, 3JHNHα couplings and the relative weight of interresidual NOEs (Fig. 2C) suggests that the STAT6783–814 peptide presents a flexible N-terminal tail, followed by an α-helix in the region Ile786-Ile790 whose population increases from around 10% in the free form to close to 100% upon binding to NcoA1 PAS-B (Fig. 2C) (SI Fig. 9). Then a short extended linker follows and finally the second α-helix (Glu799-Glu808) (Fig. 2A,B) whose population increases from 30% to close to 100%.","type":"Discussion"},{"text":"Given that existing prestructured motifs are enhanced in the bound form, the data suggest that the recognition of the coactivator by STAT6 occurs by a conformational selection25 mechanism regarding the secondary structure.","type":"Discussion"}],"ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15788"}]},{"start":786,"end":790,"reference_id":"29203888","reference_source":"pmid","reference_html":"Insight into the molecular recognition mechanism of the coactivator NCoA1 by STAT6. <i> Russo L, Giller K, Pfitzner E, Griesinger C, Becker S. </i> Sci Rep, 2017","date":"2022-06-16T18:01:33.291Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0001223","term_name":"transcription coactivator binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_06","version":4,"cross_refs":[{"db":"PDB","id":"5NWM"}],"region_id":"DP02262r008","statement":[{"text":"Regarding the STAT6783–814 peptide in the bound form, the analysis from chemical shifts, 3JHNHα couplings and the relative weight of interresidual NOEs (Fig. 2C) suggests that the STAT6783–814 peptide presents a flexible N-terminal tail, followed by an α-helix in the region Ile786-Ile790 whose population increases from around 10% in the free form to close to 100% upon binding to NcoA1 PAS-B (Fig. 2C) (SI Fig. 9). Then a short extended linker follows and finally the second α-helix (Glu799-Glu808) (Fig. 2A,B) whose population increases from 30% to close to 100%.","type":"Discussion"},{"text":"Given that existing prestructured motifs are enhanced in the bound form, the data suggest that the recognition of the coactivator by STAT6 occurs by a conformational selection25 mechanism regarding the secondary structure.","type":"Discussion"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a transcription coactivator, a protein involved in positive regulation of transcription via protein-protein interactions with transcription factors and other proteins that positively regulate transcription. Transcription coactivators do not bind DNA directly, but rather mediate protein-protein interactions between activating transcription factors and the basal transcription machinery.\" [GOC:krc]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q15788","operator":null,"partner_start":257,"partner_end":385}]},{"start":799,"end":808,"reference_id":"29203888","reference_source":"pmid","reference_html":"Insight into the molecular recognition mechanism of the coactivator NCoA1 by STAT6. <i> Russo L, Giller K, Pfitzner E, Griesinger C, Becker S. </i> Sci Rep, 2017","date":"2022-06-16T18:01:48.092Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0001223","term_name":"transcription coactivator binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_06","version":4,"cross_refs":[{"db":"PDB","id":"5NWM"}],"region_id":"DP02262r009","statement":[{"text":"Regarding the STAT6783–814 peptide in the bound form, the analysis from chemical shifts, 3JHNHα couplings and the relative weight of interresidual NOEs (Fig. 2C) suggests that the STAT6783–814 peptide presents a flexible N-terminal tail, followed by an α-helix in the region Ile786-Ile790 whose population increases from around 10% in the free form to close to 100% upon binding to NcoA1 PAS-B (Fig. 2C) (SI Fig. 9). Then a short extended linker follows and finally the second α-helix (Glu799-Glu808) (Fig. 2A,B) whose population increases from 30% to close to 100%.","type":"Discussion"},{"text":"Given that existing prestructured motifs are enhanced in the bound form, the data suggest that the recognition of the coactivator by STAT6 occurs by a conformational selection25 mechanism regarding the secondary structure.","type":"Discussion"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a transcription coactivator, a protein involved in positive regulation of transcription via protein-protein interactions with transcription factors and other proteins that positively regulate transcription. Transcription coactivators do not bind DNA directly, but rather mediate protein-protein interactions between activating transcription factors and the basal transcription machinery.\" [GOC:krc]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q15788","operator":null,"partner_start":257,"partner_end":385}]},{"start":791,"end":798,"reference_id":"29203888","reference_source":"pmid","reference_html":"Insight into the molecular recognition mechanism of the coactivator NCoA1 by STAT6. <i> Russo L, Giller K, Pfitzner E, Griesinger C, Becker S. </i> Sci Rep, 2017","date":"2022-06-16T17:55:01.174Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_06","version":4,"cross_refs":[{"db":"PDB","id":"5NWM"}],"region_id":"DP02262r010","statement":[{"text":"Regarding the STAT6783–814 peptide in the bound form, the analysis from chemical shifts, 3JHNHα couplings and the relative weight of interresidual NOEs (Fig. 2C) suggests that the STAT6783–814 peptide presents a flexible N-terminal tail, followed by an α-helix in the region Ile786-Ile790 whose population increases from around 10% in the free form to close to 100% upon binding to NcoA1 PAS-B (Fig. 2C) (SI Fig. 9). Then a short extended linker follows and finally the second α-helix (Glu799-Glu808) (Fig. 2A,B) whose population increases from 30% to close to 100%.","type":"Discussion"},{"text":"Given that existing prestructured motifs are enhanced in the bound form, the data suggest that the recognition of the coactivator by STAT6 occurs by a conformational selection25 mechanism regarding the secondary structure.","type":"Discussion"}],"ec_go":"EXP","disprot_namespace":"Disorder function","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15788"}]}],"released":"2018_11","uniref100":"UniRef100_P42226","date":"2018-08-31T04:19:02.000Z","acc":"P42226","name":"Signal transducer and activator of transcription 6","length":847,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI00000473FE","genes":[{"name":{"value":"STAT6"}}],"alphafold_very_low_content":0.24321133412042503,"disorder_content":0.03778040141676505,"disprot_consensus":{"full":[{"start":783,"end":785,"type":"D"},{"start":786,"end":808,"type":"T"},{"start":809,"end":814,"type":"D"}],"Structural state":[{"start":783,"end":814,"type":"D"}],"Molecular function":[{"start":783,"end":814,"type":"F"}],"Structural transition":[{"start":786,"end":808,"type":"T"}],"Disorder function":[{"start":791,"end":798,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00339","name":"Arrestin (or S-antigen), N-terminal domain","start":20,"end":174},{"id":"PF02752","name":"Arrestin (or S-antigen), C-terminal domain","start":195,"end":348}],"gene3D":[{"start":181,"end":397,"id":"2.60.40.640","name":"2.60.40.640"},{"start":1,"end":177,"id":"2.60.40.840","name":"2.60.40.840"}]},"uniref50":"UniRef50_P49407-2","sequence":"MGEKPGTRVFKKSSPNCKLTVYLGKRDFVDHLDKVDPVDGVVLVDPDYLKDRKVFVTLTCAFRYGREDLDVLGLSFRKDLFIANYQAFPPTPNPPRPPTRLQERLLRKLGQHAHPFFFTIPQNLPCSVTLQPGPEDTGKACGVDFEIRAFCAKSLEEKSHKRNSVRLVIRKVQFAPEKPGPQPSAETTRHFLMSDRSLHLEASLDKELYYHGEPLNVNVHVTNNSTKTVKKIKVSVRQYADICLFSTAQYKCPVAQVEQDDQVSPSSTFCKVYTITPLLSNNREKRGLALDGKLKHEDTNLASSTIVKEGANKEVLGILVSYRVKVKLVVSRGGDVSVELPFVLMHPKPHDHIALPRPQSAATHPPTLLPSAVPETDAPVDTNLIEFETNYATDDDIVFEDFARLRLKGLKDEDYDDQFC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_P32120","disprot_id":"DP02263","ncbi_taxon_id":9913,"regions_counter":8,"creator":"npalopoli","regions":[{"start":352,"end":390,"reference_id":"38175886","reference_source":"pmid","reference_html":"Molecular insights into atypical modes of β-arrestin interaction with seven transmembrane receptors. <i> Maharana J, Sano FK, Sarma P, Yadav MK, Duan L, Stepniewski TM, Chaturvedi M, Ranjan A, Singh V, Saha S, Mahajan G, Chami M, Shihoya W, Selent J, Chung KY, Banerjee R, Nureki O, Shukla AK. </i> Science, 2024","date":"2024-02-27T17:32:19.671Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys17Gly","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys60Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu69Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys126Ser","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys141Leu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys151Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys243Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys252Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys270Ser","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu278Phe","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser280Ala","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"8J8V"},{"db":"EMDB","id":"36081"}],"region_id":"DP02263r006","sample":[{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ABCD","id":"ABCD_AH039"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O00590"}],"statement":[{"text":"The cryo-EM structure of beta-arrestin2 in complex with D6Rpp shows this region lacks electron density, indicating it is disordered. ","type":"Curator statement"}]},{"start":409,"end":420,"reference_id":"38175886","reference_source":"pmid","reference_html":"Molecular insights into atypical modes of β-arrestin interaction with seven transmembrane receptors. <i> Maharana J, Sano FK, Sarma P, Yadav MK, Duan L, Stepniewski TM, Chaturvedi M, Ranjan A, Singh V, Saha S, Mahajan G, Chami M, Shihoya W, Selent J, Chung KY, Banerjee R, Nureki O, Shukla AK. </i> Science, 2024","date":"2024-02-27T17:32:07.353Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys17Gly","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys60Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu69Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys126Ser","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys141Leu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys151Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys243Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys252Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys270Ser","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu278Phe","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser280Ala","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"8J8V"},{"db":"EMDB","id":"36081"}],"region_id":"DP02263r007","sample":[{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ABCD","id":"ABCD_AH039"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O00590"}],"statement":[{"text":"The cryo-EM structure of beta-arrestin2 in complex with D6Rpp shows this region lacks electron density, indicating it is disordered. ","type":"Curator statement"}]},{"start":351,"end":420,"reference_id":"38175886","reference_source":"pmid","reference_html":"Molecular insights into atypical modes of β-arrestin interaction with seven transmembrane receptors. <i> Maharana J, Sano FK, Sarma P, Yadav MK, Duan L, Stepniewski TM, Chaturvedi M, Ranjan A, Singh V, Saha S, Mahajan G, Chami M, Shihoya W, Selent J, Chung KY, Banerjee R, Nureki O, Shukla AK. </i> Science, 2024","date":"2024-02-27T17:33:08.057Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys17Gly","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys60Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu69Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys126Ser","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys141Leu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys151Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys243Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys252Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys270Ser","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu278Phe","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser280Ala","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"8J8R"},{"db":"EMDB","id":"36078"}],"region_id":"DP02263r008","sample":[{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ABCD","id":"ABCD_AH039"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08172"}],"statement":[{"text":"The cryo-EM structure of beta-arrestin2 in complex with M2Rpp shows this region lacks electron density, indicating it is disordered. ","type":"Curator statement"}]}],"released":"2018_11","uniref100":"UniRef100_P32120","date":"2018-08-31T05:29:03.000Z","acc":"P32120","name":"Beta-arrestin-2","length":420,"organism":"Bos taurus","dataset":[],"UniParc":"UPI000012607B","genes":[{"name":{"value":"ARRB2"}}],"alphafold_very_low_content":0.13333333333333333,"disorder_content":0.16666666666666666,"disprot_consensus":{"full":[{"start":351,"end":420,"type":"D"}],"Structural state":[{"start":351,"end":420,"type":"D"}]}},{"features":{"pfam":[{"id":"PF11976","name":"Ubiquitin-2 like Rad60 SUMO-like","start":24,"end":91}],"gene3D":[{"start":13,"end":98,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"}]},"uniref50":"UniRef50_Q12306","sequence":"MSDSEVNQEAKPEVKPEVKPETHINLKVSDGSSEIFFKIKKTTPLRRLMEAFAKRQGKEMDSLRFLYDGIRIQADQTPEDLDMEDNDIIEAHREQIGGATY","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q12306","disprot_id":"DP02264","ncbi_taxon_id":559292,"regions_counter":1,"creator":"tszani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":23,"region_id":"DP02264r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of a yeast ubiquitin-like protein Smt3: the role of structurally less defined sequences in protein-protein recognitions. <i> Sheng W, Liao X. </i> Protein Sci, 2002","statement":[{"text":"Similar to Sumo-1, the data indicated that the first 23 residues at the N-terminus were disordered.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"tszani","start":1,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"pdb","id":"1l2n"}],"reference_id":"12021447","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q12306","date":"2018-08-31T09:39:10.000Z","acc":"Q12306","name":"Ubiquitin-like protein SMT3","length":101,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI00001122F6","genes":[{"name":{"value":"SMT3"},"orfNames":[{"value":"D9719.15"}],"olnNames":[{"value":"YDR510W"}]}],"alphafold_very_low_content":0.16831683168316833,"disorder_content":0.22772277227722773,"disprot_consensus":{"full":[{"start":1,"end":23,"type":"D"}],"Structural state":[{"start":1,"end":23,"type":"D"}]}},{"features":{"pfam":[{"id":"PF15040","name":"Humanin family","start":1,"end":23}]},"uniref50":"UniRef50_Q8IVG9","sequence":"MAPRGFSCLLLLTSEIDLPVKRRA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q8IVG9","disprot_id":"DP02267","ncbi_taxon_id":9606,"regions_counter":2,"creator":"vpromp","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":24,"region_id":"DP02267r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure of humanin, a peptide against Alzheimer's disease-related neurotoxicity. <i> Benaki D, Zikos C, Evangelou A, Livaniou E, Vlassi M, Mikros E, Pelecanou M. </i> Biochem Biophys Res Commun, 2005","statement":[{"text":"Unstructured in aqueous solution but adopts a helical conformation at the presence of 30% TFE. NMR data are only available for the structure in 30% TFE solution (PDB:1Y32).","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"vpromp","start":1,"term_ontology":"IDPO","curator_name":"Vasilis J Promponas","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-3352-4831","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"15721287","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":24,"region_id":"DP02267r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Solution structure of humanin, a peptide against Alzheimer's disease-related neurotoxicity. <i> Benaki D, Zikos C, Evangelou A, Livaniou E, Vlassi M, Mikros E, Pelecanou M. </i> Biochem Biophys Res Commun, 2005","statement":[{"text":"In the absence of TFE, the CD spectrum shows strong negative dichroism below 200 nm, indicative of a small degree of ordering in the peptide. On addition of TFE, changes diagnostic of conformational equilibrium between unordered structures and helical conformations of humanin in solution take place in the CD spectra.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vpromp","start":1,"term_ontology":"IDPO","curator_name":"Vasilis J Promponas","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-3352-4831","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"15721287","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q8IVG9","date":"2018-08-31T10:48:06.000Z","acc":"Q8IVG9","name":"Humanin","length":24,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000074630","genes":[{"name":{"value":"MT-RNR2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:7471","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:7471"}}]},"synonyms":[{"value":"HN","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11371646","url":"http://www.ncbi.nlm.nih.gov/pubmed/11371646","alternativeUrl":"https://europepmc.org/abstract/MED/11371646"}}]}]}],"alphafold_very_low_content":0.041666666666666664,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":24,"type":"D"}],"Structural state":[{"start":1,"end":24,"type":"D"}]}},{"features":{"pfam":[{"id":"PF11577","name":"NF-kappa-B essential modulator NEMO","start":44,"end":111},{"id":"PF16516","name":"Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator","start":257,"end":344},{"id":"PF18414","name":"C2H2 type zinc-finger","start":393,"end":418}],"gene3D":[{"start":196,"end":253,"id":"1.20.5.390","name":"L1 transposable element, trimerization domain"},{"start":257,"end":346,"id":"1.20.5.990","name":"Nemo cc2-lz domain - 1d5 darpin complex"},{"start":43,"end":111,"id":"1.20.5.390","name":"L1 transposable element, trimerization domain"}]},"uniref50":"UniRef50_Q9Y6K9","sequence":"MNRHLWKSQLCEMVQPSGGPAADQDVLGEESPLGKPAMLHLPSEQGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIKSSVVGSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDMRKRHVEVSQAPLPPAPAYLSSPLALPSQRRSPPEEPPDFCCPKCQYQAPDMDTLQIHVMECIE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9Y6K9","disprot_id":"DP02269","ncbi_taxon_id":9606,"regions_counter":4,"creator":"rdavidovic","regions":[{"region_id":"DP02269r001","ec_ontology":"ECO","end":272,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":252,"version":3,"statement":[{"text":"The secondary structure of IKKγ is shown above the residues, where dark blue arrows indicate α helices and dashed dark blue lines indicate disordered regions","type":"Figure"}],"term_name":"disorder","reference_html":"Crystal structure of a vFlip-IKKgamma complex: insights into viral activation of the IKK signalosome. <i> Bagnéris C, Ageichik AV, Cronin N, Wallace B, Collins M, Boshoff C, Waksman G, Barrett T. </i> Mol Cell, 2008","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18538660","date":"2023-05-08T20:10:39.719Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3CL3"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q76RF1"}]},{"region_id":"DP02269r002","ec_ontology":"ECO","end":192,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":150,"version":3,"statement":[{"text":"The secondary structure of IKKγ is shown above the residues, where dark blue arrows indicate α helices and dashed dark blue lines indicate disordered regions.","type":"Figure"}],"term_name":"disorder","reference_html":"Crystal structure of a vFlip-IKKgamma complex: insights into viral activation of the IKK signalosome. <i> Bagnéris C, Ageichik AV, Cronin N, Wallace B, Collins M, Boshoff C, Waksman G, Barrett T. </i> Mol Cell, 2008","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"18538660","date":"2023-05-08T20:10:11.683Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3CL3"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q76RF1"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":43,"region_id":"DP02269r004","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. <i> Rushe M, Silvian L, Bixler S, Chen LL, Cheung A, Bowes S, Cuervo H, Berkowitz S, Zheng T, Guckian K, Pellegrini M, Lugovskoy A. </i> Structure, 2008","statement":[{"text":"Proteins starting at residue 1 produced NMR spectra with ∼40 very intense crosspeaks with poor dispersion (data not shown), whereas proteins starting at residue 44 did not display this characteristic. This finding was attributed to a disordered N terminus of ∼40 residues; therefore, residue 44 was selected as the N-terminal start site for crystallization constructs.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"rdavidovic","start":1,"term_ontology":"IDPO","curator_name":"Radoslav Davidović","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"18462684","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T20:02:23.206Z"}}],"released":"2018_11","uniref100":"UniRef100_Q9Y6K9","date":"2018-08-31T10:57:42.000Z","acc":"Q9Y6K9","name":"NF-kappa-B essential modulator","length":419,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI00001697C4","genes":[{"name":{"value":"IKBKG","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:5961","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:5961"}}]},"synonyms":[{"value":"FIP3"},{"value":"NEMO"}]}],"alphafold_very_low_content":0.18854415274463007,"disorder_content":0.2553699284009546,"disprot_consensus":{"full":[{"start":1,"end":43,"type":"D"},{"start":150,"end":192,"type":"D"},{"start":252,"end":272,"type":"D"}],"Structural state":[{"start":1,"end":43,"type":"D"},{"start":150,"end":192,"type":"D"},{"start":252,"end":272,"type":"D"}]}},{"features":{"pfam":[{"id":"PF05036","name":"SPOR domain","start":246,"end":313}],"gene3D":[{"start":239,"end":319,"id":"3.30.70.1070","name":"Sporulation related repeat"}]},"uniref50":"UniRef50_P29131","sequence":"MAQRDYVRRSQPAPSRRKKSTSRKKQRNLPAVSPAMVAIAAAVLVTFIGGLYFITHHKKEESETLQSQKVTGNGLPPKPEERWRYIKELESRQPGVRAPTEPSAGGEVKTPEQLTPEQRQLLEQMQADMRQQPTQLVEVPWNEQTPEQRQQTLQRQRQAQQLAEQQRLAQQSRTTEQSWQQQTRTSQAAPVQAQPRQSKPASSQQPYQDLLQTPAHTTAQSKPQQAAPVARAADAPKPTAEKKDERRWMVQCGSFRGAEQAETVRAQLAFEGFDSKITTNNGWNRVVIGPVKGKENADSTLNRLKMAGHTNCIRLAAGG","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref90":"UniRef90_P29131","disprot_id":"DP02271","ncbi_taxon_id":83333,"regions_counter":3,"creator":"vpromp","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":79,"region_id":"DP02271r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure and domain architecture of the divisome protein FtsN. <i> Yang JC, Van Den Ent F, Neuhaus D, Brevier J, Löwe J. </i> Mol Microbiol, 2004","statement":[{"text":"Full domain structure depicted in Figure 6.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"vpromp","start":68,"term_ontology":"IDPO","curator_name":"Vasilis J Promponas","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-3352-4831","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"BMRB","id":"5984"},{"db":"PDB","id":"1UTA"}],"reference_id":"15101973","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":215,"region_id":"DP02271r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure and domain architecture of the divisome protein FtsN. <i> Yang JC, Van Den Ent F, Neuhaus D, Brevier J, Löwe J. </i> Mol Microbiol, 2004","statement":[{"text":"Full domain structure depicted in Figure 6.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"vpromp","start":124,"term_ontology":"IDPO","curator_name":"Vasilis J Promponas","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-3352-4831","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"BMRB","id":"5984"},{"db":"PDB","id":"1UTA"}],"reference_id":"15101973","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":116,"region_id":"DP02271r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution structure and domain architecture of the divisome protein FtsN. <i> Yang JC, Van Den Ent F, Neuhaus D, Brevier J, Löwe J. </i> Mol Microbiol, 2004","statement":[{"text":"Full domain structure depicted in Figure 6.","type":"Figure"}],"term_id":"IDPO:0000002","curator_id":"vpromp","start":94,"term_ontology":"IDPO","curator_name":"Vasilis J Promponas","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-3352-4831","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"BMRB","id":"5984"},{"db":"PDB","id":"1UTA"}],"reference_id":"15101973","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P29131","date":"2018-08-31T11:24:08.000Z","acc":"P29131","name":"Cell division protein FtsN","length":319,"organism":"Escherichia coli (strain K12)","dataset":[],"UniParc":"UPI000016F1E0","genes":[{"name":{"value":"ftsN","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_02039","url":"https://hamap.expasy.org/unirule/MF_02039"}}]},"synonyms":[{"value":"msgA"}],"olnNames":[{"value":"b3933"},{"value":"JW3904"}]}],"alphafold_very_low_content":0.2664576802507837,"disorder_content":0.3981191222570533,"disprot_consensus":{"full":[{"start":68,"end":79,"type":"D"},{"start":94,"end":116,"type":"D"},{"start":124,"end":215,"type":"D"}],"Structural state":[{"start":68,"end":79,"type":"D"},{"start":94,"end":116,"type":"D"},{"start":124,"end":215,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00018","name":"SH3 domain","start":544,"end":596},{"id":"PF03114","name":"BAR domain","start":14,"end":230}],"gene3D":[{"start":19,"end":243,"id":"1.20.1270.60","name":"Arfaptin homology (AH) domain/BAR domain"},{"start":529,"end":602,"id":"2.30.30.40","name":"SH3 Domains"}]},"uniref50":"UniRef50_Q7KLE5","sequence":"MTENKGIMLAKSVQKHAGRAKEKILQNLGKVDRTADEIFDDHLNNFNRQQASANRLQKEFNNYIRCVRAAQAASKTLMDSVCEIYEPQWSGYDALQAQTGASESLWADFAHKLGDQVLIPLNTYTGQFPEMKKKVEKRNRKLIDYDGQRHSFQNLQANANKRKDDVKLTKGREQLEEARRTYEILNTELHDELPALYDSRILFLVTNLQTLFATEQVFHNETAKIYSELEAIVDKLATESQRGSNTLRKQTSNPIKTSSPVQSPVNKLNNANINSNYQNQITTNGGSSLANSPTSTSSSLQEPRFDSVSSTPEPRPESPAAALVSATPSSPVENGVTTKSLERPELSGLNASAKATTTTQTSPTEDKAVVSEAVKPSETEGAAVAASVTPAPPATPAQINGNNNEPSIVKEGGKQPKELPSTTSNAEAAAEAAANNGNSIEEHKQKKLGNDTTVTATETVTVTQHSVTSTDTDNIVTISDTNTDTDTKTSTGTSQKGRPVPVVNRHSVNNLNKNPFEDDDERIYEVPADANTADLPPGVLYRVKATYGYAKEDVDELSFEIGDLIRVIEYDDPEDQEEGWLMGQKEGTNEKGLFPANFTRPI","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_Q7KLE5","disprot_id":"DP02272","ncbi_taxon_id":7227,"regions_counter":8,"creator":"baykac","regions":[{"start":1,"end":26,"reference_id":"14645856","reference_source":"pmid","reference_html":"BAR domains as sensors of membrane curvature: the amphiphysin BAR structure. <i> Peter BJ, Kent HM, Mills IG, Vallis Y, Butler PJ, Evans PR, McMahon HT. </i> Science, 2004","date":"2024-03-20T14:19:22.035Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue","statements":[{"type":"Supplementary material","text":"Drosophila amphiphysin (residues 1-245) was expressed as an NH2-terminal GST fusion\nprotein in minimal medium supplemented with selenomethionine."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":8,"end":8,"position":"Specific residue","statements":[{"type":"Supplementary material","text":"Drosophila amphiphysin (residues 1-245) was expressed as an NH2-terminal GST fusion\nprotein in minimal medium supplemented with selenomethionine."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":78,"end":78,"position":"Specific residue","statements":[{"type":"Supplementary material","text":"Drosophila amphiphysin (residues 1-245) was expressed as an NH2-terminal GST fusion\nprotein in minimal medium supplemented with selenomethionine."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":131,"end":131,"position":"Specific residue","statements":[{"type":"Supplementary material","text":"Drosophila amphiphysin (residues 1-245) was expressed as an NH2-terminal GST fusion\nprotein in minimal medium supplemented with selenomethionine."}]},{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Supplementary material","text":"Drosophila amphiphysin (residues 1-245) was expressed as an NH2-terminal GST fusion\nprotein in minimal medium supplemented with selenomethionine."}]}],"cross_refs":[{"db":"PDB","id":"1URU"}],"region_id":"DP02272r003","statement":[{"text":"The N-terminus is disordered before residue 26, and the C-terminus is disordered beyond residue 242.","type":"Article"}]},{"start":1,"end":26,"reference_id":"14645856","reference_source":"pmid","reference_html":"BAR domains as sensors of membrane curvature: the amphiphysin BAR structure. <i> Peter BJ, Kent HM, Mills IG, Vallis Y, Butler PJ, Evans PR, McMahon HT. </i> Science, 2004","date":"2024-03-20T14:22:58.333Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02272r004","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Supplementary material","text":"Top, Circular dichroism (CD) spectra of\nthe N-BAR (residues 1-244) or BAR (residues 27-244) domain of Drosophila amphiphysin taken in the presence or absence\nof brain lipid liposomes."}]}],"statement":[{"text":"On lipid binding, the helical content of the N-BAR domain of amphiphysin increased, as shown by circular dichroism spectroscopy (fig. S2B), which suggested that the N-terminus folded into an extra helix. This increase in helical content is not seen when residues 1 to 26 are deleted.","type":"Article"}]},{"start":158,"end":170,"reference_id":"14645856","reference_source":"pmid","reference_html":"BAR domains as sensors of membrane curvature: the amphiphysin BAR structure. <i> Peter BJ, Kent HM, Mills IG, Vallis Y, Butler PJ, Evans PR, McMahon HT. </i> Science, 2004","date":"2024-03-20T14:28:49.032Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":8,"end":8,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":78,"end":78,"position":"Specific residue","statements":[{"type":"Supplementary material","text":"Drosophila amphiphysin (residues 1-245) was expressed as an NH2-terminal GST fusion\nprotein in minimal medium supplemented with selenomethionine."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":131,"end":131,"position":"Specific residue","statements":[{"type":"Supplementary material","text":"Drosophila amphiphysin (residues 1-245) was expressed as an NH2-terminal GST fusion\nprotein in minimal medium supplemented with selenomethionine."}]},{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Supplementary material","text":"Drosophila amphiphysin (residues 1-245) was expressed as an NH2-terminal GST fusion\nprotein in minimal medium supplemented with selenomethionine."}]}],"cross_refs":[{"db":"PDB","id":"1URU"}],"region_id":"DP02272r005","statement":[{"text":"The positively charged loop between helices 2 and 3 found at the extreme ends of the dimer is flexible and poorly ordered (residues 158 to 165 in dAmph) and is the location of a splice variant in mammalian amphiphysin2 (residues 173 to 205 in Fig. 1E).","type":"Article"},{"text":"The deposited data shows the flexible region spans from 158 to the 170 residue.","type":"Curator statement"}]},{"start":158,"end":170,"reference_id":"14645856","reference_source":"pmid","reference_html":"BAR domains as sensors of membrane curvature: the amphiphysin BAR structure. <i> Peter BJ, Kent HM, Mills IG, Vallis Y, Butler PJ, Evans PR, McMahon HT. </i> Science, 2004","date":"2024-03-20T14:29:20.224Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":8,"end":8,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":78,"end":78,"position":"Specific residue","statements":[{"type":"Supplementary material","text":"Drosophila amphiphysin (residues 1-245) was expressed as an NH2-terminal GST fusion\nprotein in minimal medium supplemented with selenomethionine."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":131,"end":131,"position":"Specific residue","statements":[{"type":"Supplementary material","text":"Drosophila amphiphysin (residues 1-245) was expressed as an NH2-terminal GST fusion\nprotein in minimal medium supplemented with selenomethionine."}]},{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Supplementary material","text":"Drosophila amphiphysin (residues 1-245) was expressed as an NH2-terminal GST fusion\nprotein in minimal medium supplemented with selenomethionine."}]}],"cross_refs":[{"db":"PDB","id":"1URU"}],"region_id":"DP02272r006","statement":[{"text":"The positively charged loop between helices 2 and 3 found at the extreme ends of the dimer is flexible and poorly ordered (residues 158 to 165 in dAmph) and is the location of a splice variant in mammalian amphiphysin2 (residues 173 to 205 in Fig. 1E).","type":"Article"},{"text":"The deposited data shows the flexible loop spans from 158 to the 170 residue.","type":"Curator statement"}]},{"start":160,"end":164,"reference_id":"14645856","reference_source":"pmid","reference_html":"BAR domains as sensors of membrane curvature: the amphiphysin BAR structure. <i> Peter BJ, Kent HM, Mills IG, Vallis Y, Butler PJ, Evans PR, McMahon HT. </i> Science, 2004","date":"2024-03-20T14:37:11.668Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0060988","term_name":"lipid tube assembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys161Glu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys163Glu","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP02272r007","statement":[{"text":"To test if this tubulating ability is due to the Drosophila amphiphysin BAR domain, we mutated pairs of basic residues to glutamates, Lys161 + Lys163 on the disordered loop between helices 2 and 3 (mut1) and Lys137 + Arg140 on the concave face (mut2). Neither of these mutations interfered with the structure, and both double-mutants reduced the binding to liposomes; the quadruple-mutant (mut3) was more effective (Fig. 2A). These mutants also effectively inhibited the tubulation of liposomes as assessed by electron microscopy (Fig. 2B). At higher concentrations, the double-mutants showed some tubulation, whereas the quadruple-mutant did not. ","type":"Article"}],"term_comment":"","term_def":"\"The aggregation, arrangement and bonding together of a set of macromolecules to form a macromolecular complex that contains a tube of lipid surrounded by a protein coat involved in membrane shaping of vesicle membranes as they fuse or undergo fission.\" [GOC:ascb_2009, GOC:dph, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":26,"reference_id":"14645856","reference_source":"pmid","reference_html":"BAR domains as sensors of membrane curvature: the amphiphysin BAR structure. <i> Peter BJ, Kent HM, Mills IG, Vallis Y, Butler PJ, Evans PR, McMahon HT. </i> Science, 2004","date":"2024-03-20T14:47:06.480Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1Gln26del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP02272r008","statement":[{"text":"Deletion of residues 1 to 26 of Drosophila amphiphysin or residues 1 to 27 in mammalian amphiphysin1, or mutation of Phe9 to glutamate, reduced liposome binding as expected (16), but these proteins still tubulated at high concentrations (Fig. 2, B and E).","type":"Article"},{"text":"Lipid binding was assessed by electron microscopy and sedimentation assay with total bovine brain lipids.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_Q7KLE5","date":"2018-08-31T11:26:46.000Z","acc":"Q7KLE5","name":"Amphiphysin","length":602,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI0000079688","genes":[{"name":{"value":"Amph","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF58486.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF58486.1"}},{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0027356","url":"http://flybase.org/reports/FBgn0027356.html"}}]},"synonyms":[{"value":"Amp","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF58486.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF58486.1"}}]},{"value":"amph","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF58486.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF58486.1"}}]},{"value":"DAMP","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF58486.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF58486.1"}}]},{"value":"Damp","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF58486.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF58486.1"}}]},{"value":"dAmp","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF58486.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF58486.1"}}]},{"value":"dAmph","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF58486.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF58486.1"}}]},{"value":"damph","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF58486.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF58486.1"}}]},{"value":"Dmel\\CG8604","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF58486.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF58486.1"}}]}],"orfNames":[{"value":"CG8604","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF58486.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF58486.1"}},{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0027356","url":"http://flybase.org/reports/FBgn0027356.html"}}]},{"value":"Dmel_CG8604","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF58486.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF58486.1"}}]}]}],"alphafold_very_low_content":0.4568106312292359,"disorder_content":0.06478405315614617,"disprot_consensus":{"full":[{"start":1,"end":26,"type":"T"},{"start":158,"end":170,"type":"D"}],"Structural state":[{"start":1,"end":26,"type":"D"},{"start":158,"end":170,"type":"D"}],"Structural transition":[{"start":1,"end":26,"type":"T"}],"Disorder function":[{"start":158,"end":170,"type":"F"}],"Biological process":[{"start":160,"end":164,"type":"F"}],"Molecular function":[{"start":1,"end":26,"type":"F"}]}},{"features":{"pfam":[{"id":"PF01398","name":"JAB1/Mov34/MPN/PAD-1 ubiquitin protease","start":52,"end":163},{"id":"PF18323","name":"Cop9 signalosome subunit 5 C-terminal domain","start":251,"end":329}],"gene3D":[{"start":1,"end":257,"id":"3.40.140.10","name":"Cytidine Deaminase, domain 2"}]},"uniref50":"UniRef50_Q92905","sequence":"MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMSQVIKDKLFNQINIS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q92905","disprot_id":"DP02290","ncbi_taxon_id":9606,"regions_counter":2,"creator":"npalopoli","regions":[{"region_id":"DP02290r001","ec_ontology":"ECO","end":218,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":198,"version":3,"statement":[{"text":"It is noteworthy that the lack of electron density for the CSN5 portion consisting of residues 197–219 [corresponding to Ins-2 in the structure of associated molecule with the SH3 domain of STAM (signal transducing adapter molecule) deubiquitinase (AMSH-LP) (20)] prevented accurate modeling and analysis of this segment.","type":"Results"},{"text":"Correct positioning of the K63-Ub2 isopeptide bond in the long recognition groove of AMSH-LP is ensured by interactions between AMSH-LP [in particular, the Ins-1 region, the Ins-2 loop (disordered in CSN5), and the segment between these two insertions) and the proximal and distal ubiquitins (SI Appendix, Fig. S2)].","type":"Discussion"}],"term_name":"disorder","reference_html":"Insights into the regulation of the human COP9 signalosome catalytic subunit, CSN5/Jab1. <i> Echalier A, Pan Y, Birol M, Tavernier N, Pintard L, Hoh F, Ebel C, Galophe N, Claret FX, Dumas C. </i> Proc Natl Acad Sci U S A, 2013","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"23288897","date":"2024-02-29T15:52:00.718Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4F7O"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":8,"end":8,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":19,"end":19,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":65,"end":65,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":67,"end":67,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":78,"end":78,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":81,"end":81,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":90,"end":90,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":93,"end":93,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":117,"end":117,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":156,"end":156,"position":"Specific residue"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":295,"region_id":"DP02290r002","released":"2024_06","ec_id":"ECO:0006220","reference_html":"Crystal structure of the human COP9 signalosome. <i> Lingaraju GM, Bunker RD, Cavadini S, Hess D, Hassiepen U, Renatus M, Fischer ES, Thomä NH. </i> Nature, 2014","term_id":"IDPO:0000002","curator_id":"vnugnes","start":284,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-29T15:46:15.241Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4D10"},{"db":"PDB","id":"4D18"}],"reference_id":"25043011","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q99627"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBW8"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q7L5N1"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9BT78 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UNS2"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61201"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q13098"}],"statement":[{"text":"Disordered residues are represented by dashed lines.","type":"Figure"}]}],"released":"2018_11","uniref100":"UniRef100_Q92905","date":"2018-08-31T12:46:02.000Z","acc":"Q92905","name":"COP9 signalosome complex subunit 5","length":334,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000073D74","genes":[{"name":{"value":"COPS5"},"synonyms":[{"value":"CSN5"},{"value":"JAB1"}]}],"alphafold_very_low_content":0.03592814371257485,"disorder_content":0.09880239520958084,"disprot_consensus":{"full":[{"start":198,"end":218,"type":"D"},{"start":284,"end":295,"type":"D"}],"Structural state":[{"start":198,"end":218,"type":"D"},{"start":284,"end":295,"type":"D"}]}},{"acc":"P04486","sequence":"MDLLVDELFADMDADGASPPPPRPAGGPKNTPAAPPLYATGRLSQAQLMPSPPMPVPPAALFNRLLDDLGFSAGPALCTMLDTWNEDLFSALPTNADLYRECKFLSTLPSDVVEWGDAYVPERAQIDIRAHGDVAFPTLPATRDGLGLYYEALSRFFHAELRAREESYRTVLANFCSALYRYLRASVRQLHRQAHMRGRDRDLGEMLRATIADRYYRETARLARVLFLHLYLFLTREILWAAYAEQMMRPDLFDCLCCDLESWRQLAGLFQPFMFVNGALTVRGVPIEARRLRELNHIREHLNLPLVRSAATEEPGAPLTTPPTLHGNQARASGYFMVLIRAKLDSYSSFTTSPSEAVMREHAYSRARTKNNYGSTIEGLLDLPDDDAPEEAGLAAPRLSFLPAGHTRRLSTAPPTDVSLGDELHLDGEDVAMAHADALDDFDLDMLGDGDSPGPGFTPHDSAPYGALDMADFEFEQMFTDALGIDEYGG","creator":"tszani","dataset":["Viral proteins"],"date":"2018-08-31T12:55:02.000Z","disprot_id":"DP02291","features":{"pfam":[{"id":"PF02232","name":"Alpha trans-inducing protein (Alpha-TIF)","start":44,"end":386},{"id":"PF12149","name":"Herpes simplex virus virion protein 16 C terminal","start":461,"end":490}],"gene3D":[{"start":47,"end":363,"id":"1.10.1290.10","name":"Alpha trans-inducing (Alpha-TIF)","_id":"685af523b4ac24d5329d9452"}]},"genes":[{"synonyms":[],"olnNames":[],"orfNames":[{"value":"UL48","evidences":[],"_id":"685af523b4ac24d5329d94d1"}],"_id":"685af523b4ac24d5329d94d0"}],"length":490,"name":"Tegument protein VP16","ncbi_taxon_id":10304,"organism":"Human herpesvirus 1 (strain F)","regions_counter":25,"released":"2018_11","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Peploviricota","Herviviricetes","Herpesvirales","Herpesviridae","Alphaherpesvirinae","Simplexvirus"],"UniParc":"UPI000012624F","uniref100":"UniRef100_P04486","uniref50":"UniRef50_P06492","uniref90":"UniRef90_P06492","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"6099","_id":"685af523b4ac24d5329d9457"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":412,"end":490,"interaction_partner":[],"reference_html":"Structural properties of the promiscuous VP16 activation domain. <i> Jonker HR, Wechselberger RW, Boelens R, Folkers GE, Kaptein R. </i> Biochemistry, 2005","reference_id":"15654739","region_id":"DP02291r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"VP16 was shown before to be unstructured in solution (16, 32, 33). We confirm this notion by the absence of NOE contacts that are indicative for secondary structure elements.","_id":"685af523b4ac24d5329d9454"},{"type":"Results","text":"The (1H,15N)-HSQC spectrum of VP16ad shows a small dispersion of intense signals in the proton dimension (<1 ppm), indicative for a lack of secondary structure.","_id":"685af523b4ac24d5329d9455"},{"type":"Curator statement","text":"HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d9456"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:02:51.417Z","_id":"685af523b4ac24d5329d9458"},"version":3,"_id":"685af523b4ac24d5329d9453","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":456,"end":490,"interaction_partner":[],"reference_html":"NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: structural similarities between VP16 and p53. <i> Langlois C, Mas C, Di Lello P, Jenkins LM, Legault P, Omichinski JG. </i> J Am Chem Soc, 2008","reference_id":"18630911","region_id":"DP02291r002","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"NMR structural studies demonstrate that VP16C is disordered in the free state, and forms a 9-residue α-helix involving residues Asp472 to Thr480 in complex with Tfb1.","_id":"685af523b4ac24d5329d945a"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d945b"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T08:51:55.815Z","_id":"685af523b4ac24d5329d945c"},"version":3,"_id":"685af523b4ac24d5329d9459","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":456,"end":490,"interaction_partner":[],"reference_html":"NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: structural similarities between VP16 and p53. <i> Langlois C, Mas C, Di Lello P, Jenkins LM, Legault P, Omichinski JG. </i> J Am Chem Soc, 2008","reference_id":"18630911","region_id":"DP02291r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Addition of VP16C (VP16456−490) to 15N-labeled Tfb11−115 produced changes in 1H and 15N chemical shifts for several signals of Tfb11−115 in the 2D 1H−15N HSQC spectra (Figure 1).","_id":"685af523b4ac24d5329d945e"},{"type":"Results","text":"The structure of the Tfb11−115/VP16C complex is well defined by the NMR data (Figure 2).","_id":"685af523b4ac24d5329d945f"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d9460"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:05:16.724Z","_id":"685af523b4ac24d5329d9461"},"version":4,"_id":"685af523b4ac24d5329d945d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2K2U","_id":"685af523b4ac24d5329d946d"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":456,"end":490,"interaction_partner":[{"db":"UniProt","id":"P32776","partner_start":1,"partner_end":115,"_id":"685af523b4ac24d5329d946e"}],"reference_html":"NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: structural similarities between VP16 and p53. <i> Langlois C, Mas C, Di Lello P, Jenkins LM, Legault P, Omichinski JG. </i> J Am Chem Soc, 2008","reference_id":"18630911","region_id":"DP02291r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The binding interface of the Tfb1/VP16C complex comprises strands β5, β6 and β7 and the loop connecting β5 and β6 of Tfb1 and the 9-residue α-helix of VP16C (Asp472−Thr480).","_id":"685af523b4ac24d5329d9469"},{"type":"Results","text":"Addition of VP16C (VP16456−490) to 15N-labeled Tfb11−115 produced changes in 1H and 15N chemical shifts for several signals of Tfb11−115 in the 2D 1H−15N HSQC spectra (Figure 1).","_id":"685af523b4ac24d5329d946a"},{"type":"Results","text":"The structure of the Tfb11−115/VP16C complex is well defined by the NMR data (Figure 2).","_id":"685af523b4ac24d5329d946b"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d946c"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:05:33.670Z","_id":"685af523b4ac24d5329d946f"},"version":4,"_id":"685af523b4ac24d5329d9468","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005647","ec_name":"isothermal titration calorimetry evidence used in manual assertion","ec_ontology":"ECO","start":412,"end":456,"interaction_partner":[{"db":"UniProt","id":"P32776 ","partner_start":1,"partner_end":115,"_id":"685af523b4ac24d5329d9471"}],"reference_html":"NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: structural similarities between VP16 and p53. <i> Langlois C, Mas C, Di Lello P, Jenkins LM, Legault P, Omichinski JG. </i> J Am Chem Soc, 2008","reference_id":"18630911","region_id":"DP02291r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"By this method, VP16C bound to Tfb1 with an apparent Kd of 360 ± 40 nM and VP16N bound to Tfb1 with an apparent Kd of 1000 ± 100 nM (Table 1). These results suggested that both subdomains of the VP16TAD were capable of interacting with Tfb1, and the Kd obtained for the Tfb1/VP16C complex is very similar to the Kd observed between Tfb1 and the p53TAD2 (390 nM).","_id":"685af523b4ac24d5329d9472"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d9473"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:05:35.883Z","_id":"685af523b4ac24d5329d9474"},"version":1,"_id":"685af523b4ac24d5329d9470","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005647","ec_name":"isothermal titration calorimetry evidence used in manual assertion","ec_ontology":"ECO","start":456,"end":490,"interaction_partner":[{"db":"UniProt","id":"P32776 ","partner_start":1,"partner_end":115,"_id":"685af523b4ac24d5329d9476"}],"reference_html":"NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: structural similarities between VP16 and p53. <i> Langlois C, Mas C, Di Lello P, Jenkins LM, Legault P, Omichinski JG. </i> J Am Chem Soc, 2008","reference_id":"18630911","region_id":"DP02291r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"By this method, VP16C bound to Tfb1 with an apparent Kd of 360 ± 40 nM and VP16N bound to Tfb1 with an apparent Kd of 1000 ± 100 nM (Table 1). These results suggested that both subdomains of the VP16TAD were capable of interacting with Tfb1, and the Kd obtained for the Tfb1/VP16C complex is very similar to the Kd observed between Tfb1 and the p53TAD2 (390 nM).","_id":"685af523b4ac24d5329d9477"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d9478"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:05:37.224Z","_id":"685af523b4ac24d5329d9479"},"version":1,"_id":"685af523b4ac24d5329d9475","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-08T15:01:52.661Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005647","ec_name":"isothermal titration calorimetry evidence used in manual assertion","ec_ontology":"ECO","start":456,"end":490,"interaction_partner":[{"db":"UniProt","id":"P32776","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d947d"}],"reference_html":"NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: structural similarities between VP16 and p53. <i> Langlois C, Mas C, Di Lello P, Jenkins LM, Legault P, Omichinski JG. </i> J Am Chem Soc, 2008","reference_id":"18630911","region_id":"DP02291r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"By this method, VP16C bound to Tfb1 with an apparent Kd of 360 ± 40 nM and VP16N bound to Tfb1 with an apparent Kd of 1000 ± 100 nM (Table 1). These results suggested that both subdomains of the VP16TAD were capable of interacting with Tfb1, and the Kd obtained for the Tfb1/VP16C complex is very similar to the Kd observed between Tfb1 and the p53TAD2 (390 nM).","_id":"685af523b4ac24d5329d947b"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d947c"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_id":"GO:0140677","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-08-26T17:25:43.684Z","_id":"685af523b4ac24d5329d947e"},"version":2,"_id":"685af523b4ac24d5329d947a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-08T15:01:43.172Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005647","ec_name":"isothermal titration calorimetry evidence used in manual assertion","ec_ontology":"ECO","start":412,"end":490,"interaction_partner":[{"db":"UniProt","id":"P32776","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9482"}],"reference_html":"NMR structure of the complex between the Tfb1 subunit of TFIIH and the activation domain of VP16: structural similarities between VP16 and p53. <i> Langlois C, Mas C, Di Lello P, Jenkins LM, Legault P, Omichinski JG. </i> J Am Chem Soc, 2008","reference_id":"18630911","region_id":"DP02291r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"By this method, VP16C bound to Tfb1 with an apparent Kd of 360 ± 40 nM and VP16N bound to Tfb1 with an apparent Kd of 1000 ± 100 nM (Table 1). These results suggested that both subdomains of the VP16TAD were capable of interacting with Tfb1, and the Kd obtained for the Tfb1/VP16C complex is very similar to the Kd observed between Tfb1 and the p53TAD2 (390 nM).","_id":"685af523b4ac24d5329d9480"},{"type":"Curator statement","text":"The VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d9481"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_id":"GO:0140677","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-08-26T18:02:12.375Z","_id":"685af523b4ac24d5329d9483"},"version":2,"_id":"685af523b4ac24d5329d947f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"DisProt","id":"DP01642r005","_id":"685af523b4ac24d5329d9485"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"IC","ec_id":"ECO:0000305","ec_name":"curator inference used in manual assertion","ec_ontology":"ECO","start":412,"end":490,"interaction_partner":[],"reference_html":"Structural properties of the promiscuous VP16 activation domain. <i> Jonker HR, Wechselberger RW, Boelens R, Folkers GE, Kaptein R. </i> Biochemistry, 2005","reference_id":"15654739","region_id":"DP02291r010","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"IDR is 100% identical to the Human herpesvirus 1 (strain 17), UniProtKB:P06492.\nThe VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d9486"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:03:38.812Z","_id":"685af523b4ac24d5329d9487"},"version":1,"_id":"685af523b4ac24d5329d9484","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"DisProt","id":"DP01642r028","_id":"685af523b4ac24d5329d9489"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IC","ec_id":"ECO:0000305","ec_name":"curator inference used in manual assertion","ec_ontology":"ECO","start":454,"end":490,"interaction_partner":[{"db":"UniProt","id":"P53999","partner_start":1,"partner_end":126,"_id":"685af523b4ac24d5329d948a"}],"reference_html":"Structural properties of the promiscuous VP16 activation domain. <i> Jonker HR, Wechselberger RW, Boelens R, Folkers GE, Kaptein R. </i> Biochemistry, 2005","reference_id":"15654739","region_id":"DP02291r011","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"IDR is 100% identical to the Human herpesvirus 1 (strain 17), UniProtKB:P06492.\nThe VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d948b"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:05:38.792Z","_id":"685af523b4ac24d5329d948c"},"version":1,"_id":"685af523b4ac24d5329d9488","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"DisProt","id":"DP01642r027","_id":"685af523b4ac24d5329d948e"},{"db":"DisProt","id":"DP01642r026","_id":"685af523b4ac24d5329d948f"},{"db":"DisProt","id":"DP01642r006","_id":"685af523b4ac24d5329d9490"},{"db":"PDB","id":"2PHE","_id":"685af523b4ac24d5329d9491"},{"db":"PDB","id":"2PHG","_id":"685af523b4ac24d5329d9492"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IC","ec_id":"ECO:0000305","ec_name":"curator inference used in manual assertion","ec_ontology":"ECO","start":412,"end":490,"interaction_partner":[{"db":"UniProt","id":"P53999","partner_start":1,"partner_end":126,"_id":"685af523b4ac24d5329d9493"},{"db":"UniProt","id":"Q00403","partner_start":112,"partner_end":316,"_id":"685af523b4ac24d5329d9494"}],"reference_html":"Structural properties of the promiscuous VP16 activation domain. <i> Jonker HR, Wechselberger RW, Boelens R, Folkers GE, Kaptein R. </i> Biochemistry, 2005","reference_id":"15654739","region_id":"DP02291r012","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"IDR is 100% identical to the Human herpesvirus 1 (strain 17), UniProtKB:P06492.\nThe VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d9495"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:04:25.045Z","_id":"685af523b4ac24d5329d9496"},"version":1,"_id":"685af523b4ac24d5329d948d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"DisProt","id":"DP01642r030","_id":"685af523b4ac24d5329d9498"},{"db":"DisProt","id":"DP01642r029","_id":"685af523b4ac24d5329d9499"},{"db":"PDB","id":"PDB:2PHE","_id":"685af523b4ac24d5329d949a"},{"db":"PDB","id":"PDB:2PHG","_id":"685af523b4ac24d5329d949b"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IC","ec_id":"ECO:0000305","ec_name":"curator inference used in manual assertion","ec_ontology":"ECO","start":412,"end":490,"interaction_partner":[],"reference_html":"Structural properties of the promiscuous VP16 activation domain. <i> Jonker HR, Wechselberger RW, Boelens R, Folkers GE, Kaptein R. </i> Biochemistry, 2005","reference_id":"15654739","region_id":"DP02291r013","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"IDR is 100% identical to the Human herpesvirus 1 (strain 17), UniProtKB:P06492.\nThe VP16 gene fragment used in this publication was derived from the Human herpesvirus 1 KOS strain. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d949c"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_id":"GO:0140677","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:05:27.244Z","_id":"685af523b4ac24d5329d949d"},"version":1,"_id":"685af523b4ac24d5329d9497","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"DisProt","id":"DP01642r014","_id":"685af523b4ac24d5329d949f"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IC","ec_id":"ECO:0000305","ec_name":"curator inference used in manual assertion","ec_ontology":"ECO","start":469,"end":485,"interaction_partner":[],"reference_html":"Induced alpha helix in the VP16 activation domain upon binding to a human TAF. <i> Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL. </i> Science, 1997","reference_id":"9271577","region_id":"DP02291r014","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"IDR is 100% identical to the Human herpesvirus 1 (strain 17), UniProtKB:P06492. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d94a0"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:01:45.041Z","_id":"685af523b4ac24d5329d94a1"},"version":1,"_id":"685af523b4ac24d5329d949e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"DisProt","id":"DP01642r007","_id":"685af523b4ac24d5329d94a3"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IC","ec_id":"ECO:0000305","ec_name":"curator inference used in manual assertion","ec_ontology":"ECO","start":452,"end":490,"interaction_partner":[],"reference_html":"Induced alpha helix in the VP16 activation domain upon binding to a human TAF. <i> Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL. </i> Science, 1997","reference_id":"9271577","region_id":"DP02291r015","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"IDR is 100% identical to the Human herpesvirus 1 (strain 17), UniProtKB:P06492. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d94a4"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:01:42.147Z","_id":"685af523b4ac24d5329d94a5"},"version":1,"_id":"685af523b4ac24d5329d94a2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"DisProt","id":"DP01642r019","_id":"685af523b4ac24d5329d94a7"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"IC","ec_id":"ECO:0000305","ec_name":"curator inference used in manual assertion","ec_ontology":"ECO","start":475,"end":484,"interaction_partner":[],"reference_html":"Induced alpha helix in the VP16 activation domain upon binding to a human TAF. <i> Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL. </i> Science, 1997","reference_id":"9271577","region_id":"DP02291r016","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"IDR is 100% identical to the Human herpesvirus 1 (strain 17), UniProtKB:P06492. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d94a8"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:03:35.379Z","_id":"685af523b4ac24d5329d94a9"},"version":1,"_id":"685af523b4ac24d5329d94a6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"DisProt","id":"DP01642r015","_id":"685af523b4ac24d5329d94ab"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"IC","ec_id":"ECO:0000305","ec_name":"curator inference used in manual assertion","ec_ontology":"ECO","start":469,"end":485,"interaction_partner":[],"reference_html":"Induced alpha helix in the VP16 activation domain upon binding to a human TAF. <i> Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL. </i> Science, 1997","reference_id":"9271577","region_id":"DP02291r017","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"IDR is 100% identical to the Human herpesvirus 1 (strain 17), UniProtKB:P06492. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d94ac"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:03:30.152Z","_id":"685af523b4ac24d5329d94ad"},"version":1,"_id":"685af523b4ac24d5329d94aa","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"DisProt","id":"DP01642r009","_id":"685af523b4ac24d5329d94af"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"IC","ec_id":"ECO:0000305","ec_name":"curator inference used in manual assertion","ec_ontology":"ECO","start":452,"end":490,"interaction_partner":[],"reference_html":"Induced alpha helix in the VP16 activation domain upon binding to a human TAF. <i> Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL. </i> Science, 1997","reference_id":"9271577","region_id":"DP02291r018","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"IDR is 100% identical to the Human herpesvirus 1 (strain 17), UniProtKB:P06492. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d94b0"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:03:10.137Z","_id":"685af523b4ac24d5329d94b1"},"version":1,"_id":"685af523b4ac24d5329d94ae","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"DisProt","id":"DP01642r016","_id":"685af523b4ac24d5329d94b3"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IC","ec_id":"ECO:0000305","ec_name":"curator inference used in manual assertion","ec_ontology":"ECO","start":469,"end":485,"interaction_partner":[{"db":"UniProt","id":"Q16594","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d94b4"}],"reference_html":"Induced alpha helix in the VP16 activation domain upon binding to a human TAF. <i> Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL. </i> Science, 1997","reference_id":"9271577","region_id":"DP02291r019","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"IDR is 100% identical to the Human herpesvirus 1 (strain 17), UniProtKB:P06492. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d94b5"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:04:19.370Z","_id":"685af523b4ac24d5329d94b6"},"version":1,"_id":"685af523b4ac24d5329d94b2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"DisProt","id":"DP01642r016","_id":"685af523b4ac24d5329d94b8"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IC","ec_id":"ECO:0000305","ec_name":"curator inference used in manual assertion","ec_ontology":"ECO","start":452,"end":490,"interaction_partner":[{"db":"UniProt","id":"Q16594","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d94b9"}],"reference_html":"Induced alpha helix in the VP16 activation domain upon binding to a human TAF. <i> Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL. </i> Science, 1997","reference_id":"9271577","region_id":"DP02291r020","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"IDR is 100% identical to the Human herpesvirus 1 (strain 17), UniProtKB:P06492. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d94ba"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:04:09.084Z","_id":"685af523b4ac24d5329d94bb"},"version":1,"_id":"685af523b4ac24d5329d94b7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"DisProt","id":"DP01642r018","_id":"685af523b4ac24d5329d94bd"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IC","ec_id":"ECO:0000305","ec_name":"curator inference used in manual assertion","ec_ontology":"ECO","start":475,"end":484,"interaction_partner":[],"reference_html":"Induced alpha helix in the VP16 activation domain upon binding to a human TAF. <i> Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL. </i> Science, 1997","reference_id":"9271577","region_id":"DP02291r021","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"IDR is 100% identical to the Human herpesvirus 1 (strain 17), UniProtKB:P06492. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d94be"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_id":"GO:0140677","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:05:29.667Z","_id":"685af523b4ac24d5329d94bf"},"version":1,"_id":"685af523b4ac24d5329d94bc","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"DisProt","id":"DP01642r017","_id":"685af523b4ac24d5329d94c1"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IC","ec_id":"ECO:0000305","ec_name":"curator inference used in manual assertion","ec_ontology":"ECO","start":469,"end":485,"interaction_partner":[],"reference_html":"Induced alpha helix in the VP16 activation domain upon binding to a human TAF. <i> Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL. </i> Science, 1997","reference_id":"9271577","region_id":"DP02291r022","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"IDR is 100% identical to the Human herpesvirus 1 (strain 17), UniProtKB:P06492. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d94c2"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_id":"GO:0140677","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:05:30.986Z","_id":"685af523b4ac24d5329d94c3"},"version":1,"_id":"685af523b4ac24d5329d94c0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"DisProt","id":"DP01642r010","_id":"685af523b4ac24d5329d94c5"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IC","ec_id":"ECO:0000305","ec_name":"curator inference used in manual assertion","ec_ontology":"ECO","start":452,"end":490,"interaction_partner":[],"reference_html":"Induced alpha helix in the VP16 activation domain upon binding to a human TAF. <i> Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL. </i> Science, 1997","reference_id":"9271577","region_id":"DP02291r023","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"IDR is 100% identical to the Human herpesvirus 1 (strain 17), UniProtKB:P06492. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d94c6"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_id":"GO:0140677","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function activator activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:05:32.141Z","_id":"685af523b4ac24d5329d94c7"},"version":1,"_id":"685af523b4ac24d5329d94c4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"DisProt","id":"DP01642r001","_id":"685af523b4ac24d5329d94c9"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IC","ec_id":"ECO:0000305","ec_name":"curator inference used in manual assertion","ec_ontology":"ECO","start":350,"end":394,"interaction_partner":[],"reference_html":"Molecular shapes of transcription factors TFIIB and VP16 in solution: implications for recognition. <i> Grossmann JG, Sharff AJ, O'Hare P, Luisi B. </i> Biochemistry, 2001","reference_id":"11371188","region_id":"DP02291r024","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"IDR is 100% identical to the Human herpesvirus 1 (strain 17), UniProtKB:P06492. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d94ca"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-18T08:01:38.537Z","_id":"685af523b4ac24d5329d94cb"},"version":1,"_id":"685af523b4ac24d5329d94c8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"DisProt","id":"DP01642r002","_id":"685af523b4ac24d5329d94cd"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IC","ec_id":"ECO:0000305","ec_name":"curator inference used in manual assertion","ec_ontology":"ECO","start":403,"end":490,"interaction_partner":[],"reference_html":"Molecular shapes of transcription factors TFIIB and VP16 in solution: implications for recognition. <i> Grossmann JG, Sharff AJ, O'Hare P, Luisi B. </i> Biochemistry, 2001","reference_id":"11371188","region_id":"DP02291r025","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"IDR is 100% identical to the Human herpesvirus 1 (strain 17), UniProtKB:P06492. HSV-1 VP16 amino acid sequences of the KOS and F strains are identical for all 490 residues and differ from strain 17 by only two amino acid substitutions (Asp-Asn at position 13 and Ala-Thr at position 124).","_id":"685af523b4ac24d5329d94ce"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-19T08:20:41.811Z","_id":"685af523b4ac24d5329d94cf"},"version":1,"_id":"685af523b4ac24d5329d94cc","reference_source":"pmid"}],"__v":0,"disorder_content":0.2714285714285714,"disprot_consensus":{"full":[{"start":350,"end":394,"type":"D"},{"start":403,"end":411,"type":"D"},{"start":412,"end":490,"type":"T"}],"Structural state":[{"start":350,"end":394,"type":"D"},{"start":403,"end":490,"type":"D"}],"Molecular function":[{"start":412,"end":490,"type":"F"}],"Structural transition":[{"start":412,"end":490,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00168","name":"C2 domain","start":21,"end":119},{"id":"PF00397","name":"WW domain","start":195,"end":224},{"id":"PF00397","name":"WW domain","start":387,"end":416},{"id":"PF00397","name":"WW domain","start":499,"end":528},{"id":"PF00397","name":"WW domain","start":550,"end":579},{"id":"PF00632","name":"HECT-domain (ubiquitin-transferase)","start":670,"end":972}],"gene3D":[{"start":15,"end":188,"id":"2.60.40.150","name":"C2 domain"},{"start":856,"end":975,"id":"3.30.2410.10","name":"Hect, E3 ligase catalytic domain"},{"start":549,"end":851,"id":"3.90.1750.10","name":"Hect, E3 ligase catalytic domains"},{"start":189,"end":234,"id":"2.20.70.10","name":"2.20.70.10"},{"start":351,"end":426,"id":"2.20.70.10","name":"2.20.70.10"},{"start":743,"end":819,"id":"3.30.2160.10","name":"Hect, E3 ligase catalytic domain"},{"start":499,"end":534,"id":"2.20.70.10","name":"2.20.70.10"}]},"uniref50":"UniRef50_Q96PU5","sequence":"MATGLGEPVYGLSEDEGESRILRVKVVSGIDLAKKDIFGASDPYVKLSLYVADENRELALVQTKTIKKTLNPKWNEEFYFRVNPSNHRLLFEVFDENRLTRDDFLGQVDVPLSHLPTEDPTMERPYTFKDFLLRPRSHKSRVKGFLRLKMAYMPKNGGQDEENSDQRDDMEHGWEVVDSNDSASQHQEELPPPPLPPGWEEKVDNLGRTYYVNHNNRTTQWHRPSLMDVSSESDNNIRQINQEAAHRRFRSRRHISEDLEPEPSEGGDVPEPWETISEEVNIAGDSLGLALPPPPASPGSRTSPQELSEELSRRLQITPDSNGEQFSSLIQREPSSRLRSCSVTDAVAEQGHLPPPSAPAGRARSSTVTGGEEPTPSVAYVHTTPGLPSGWEERKDAKGRTYYVNHNNRTTTWTRPIMQLAEDGASGSATNSNNHLIEPQIRRPRSLSSPTVTLSAPLEGAKDSPVRRAVKDTLSNPQSPQPSPYNSPKPQHKVTQSFLPPGWEMRIAPNGRPFFIDHNTKTTTWEDPRLKFPVHMRSKTSLNPNDLGPLPPGWEERIHLDGRTFYIDHNSKITQWEDPRLQNPAITGPAVPYSREFKQKYDYFRKKLKKPADIPNRFEMKLHRNNIFEESYRRIMSVKRPDVLKARLWIEFESEKGLDYGGVAREWFFLLSKEMFNPYYGLFEYSATDNYTLQINPNSGLCNEDHLSYFTFIGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPTELDLMFCIDEENFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSNGPQLFTIEQWGSPEKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGFEGVD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q96PU5","disprot_id":"DP02292","ncbi_taxon_id":9606,"regions_counter":2,"creator":"tszani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":480,"region_id":"DP02292r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"A Smad action turnover switch operated by WW domain readers of a phosphoserine code. <i> Aragón E, Goerner N, Zaromytidou AI, Xi Q, Escobedo A, Massagué J, Macias MJ. </i> Genes Dev, 2011","statement":[{"text":"The α and β 13C chemical shifts analysis revealed that the segment connecting the WW2–WW3 pair (residues 400–480) lacks elements of a secondary structure in both the free and bound conformations, and is unaffected by binding of the Smad3 peptide.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"tszani","start":400,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21685363","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T19:58:42.678Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":480,"term_name":"flexible linker","released":"2023_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"A Smad action turnover switch operated by WW domain readers of a phosphoserine code. <i> Aragón E, Goerner N, Zaromytidou AI, Xi Q, Escobedo A, Massagué J, Macias MJ. </i> Genes Dev, 2011","statement":[{"text":"The 80-amino-acid region connecting the WW2 and WW3 domains (dotted line) does not adopt a defined secondary or tertiary structure, as indicated by near-random 13C chemical shifts.","type":"Results"}],"term_id":"IDPO:0000033","curator_id":"vnugnes","start":400,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"21685363","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2023-05-08T19:58:40.133Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP02292r002","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_Q96PU5","date":"2018-08-31T15:05:34.000Z","acc":"Q96PU5","name":"E3 ubiquitin-protein ligase NEDD4-like","length":975,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI0000072494","genes":[{"name":{"value":"NEDD4L","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11840194","url":"http://www.ncbi.nlm.nih.gov/pubmed/11840194","alternativeUrl":"https://europepmc.org/abstract/MED/11840194"}}]},"synonyms":[{"value":"KIAA0439","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11244092","url":"http://www.ncbi.nlm.nih.gov/pubmed/11244092","alternativeUrl":"https://europepmc.org/abstract/MED/11244092"}}]},{"value":"NEDL3"}]}],"alphafold_very_low_content":0.29435897435897435,"disorder_content":0.08307692307692308,"disprot_consensus":{"full":[{"start":400,"end":480,"type":"D"}],"Structural state":[{"start":400,"end":480,"type":"D"}],"Disorder function":[{"start":400,"end":480,"type":"F"}]}},{"features":{"pfam":[{"id":"PF11976","name":"Ubiquitin-2 like Rad60 SUMO-like","start":22,"end":91}],"gene3D":[{"start":1,"end":97,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"}]},"uniref50":"UniRef50_P63165","sequence":"MSDQEAKPSTEDLGDKKEGEYIKLKVIGQDSSEIHFKVKMTTHLKKLKESYCQRQGVPMNSLRFLFEGQRIADNHTPKELGMEEEDVIEVYQEQTGGHSTV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P63165","disprot_id":"DP02294","ncbi_taxon_id":9606,"regions_counter":3,"creator":"tszani","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":18,"region_id":"DP02294r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of thymine DNA glycosylase conjugated to SUMO-1. <i> Baba D, Maita N, Jee JG, Uchimura Y, Saitoh H, Sugasawa K, Hanaoka F, Tochio H, Hiroaki H, Shirakawa M. </i> Nature, 2005","statement":[{"text":"The 18 N-terminal amino acids for which electron densities are not observed in the SUMO-1–TDG crystal have been shown to be flexible in unconjugated SUMO-1 in solution","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"tszani","start":1,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"pdb","id":"1wyw"}],"reference_id":"15959518","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":18,"region_id":"DP02294r002","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structure determination of the small ubiquitin-related modifier SUMO-1. <i> Bayer P, Arndt A, Metzger S, Mahajan R, Melchior F, Jaenicke R, Becker J. </i> J Mol Biol, 1998","statement":[{"text":"SUMO-1 contains an N-terminal extension, which forms a flexible appendix that protrudes from the core protein\n...However, only 34 NOEs could be used to characterize the flexible termini (Gly2 to Glu18 and Gln94 to Val101),","type":"Introduction"}],"term_id":"IDPO:0000002","curator_id":"tszani","start":2,"term_ontology":"IDPO","curator_name":"Tamás Szaniszló","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3130-9284","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"pdb","id":"1a5r"}],"reference_id":"9654451","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":18,"reference_id":"20164921","reference_source":"pmid","reference_html":"Active site remodelling accompanies thioester bond formation in the SUMO E1. <i> Olsen SK, Capili AD, Lu X, Tan DS, Lima CD. </i> Nature, 2010","date":"2023-11-24T12:39:00.323Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"3KYC"}],"region_id":"DP02294r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBE0"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UBT2"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:44620962","statements":[{"type":"Curator statement","text":"Interacting with the complex is a non-hydrolyzable mimic of the acyl-adenylate intermediate (AMSN) was made by linking a cysteylglycylglycyl tripeptide to 5′-(sulfamoylaminodeoxy)adenosine (CGG-AMSN)12"}]}],"statement":[{"text":"The final model contained SUMO1(19–97)-AMSN, SAE1 amino acids (aa) 9–180 and 205–345, and UBA2 aa 5–217, 235–291, 305–548 and 608–640. As full-length proteins were used in crystallization, residues not observed in electron density were presumed disordered.","type":"Methods"}]}],"released":"2018_11","uniref100":"UniRef100_P63165","date":"2018-08-31T15:34:58.000Z","acc":"P63165","name":"Small ubiquitin-related modifier 1","length":101,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000001227","genes":[{"name":{"value":"SUMO1"},"synonyms":[{"value":"SMT3C"},{"value":"SMT3H3"},{"value":"UBL1"}],"orfNames":[{"value":"OK/SW-cl.43"}]}],"alphafold_very_low_content":0.1782178217821782,"disorder_content":0.1782178217821782,"disprot_consensus":{"full":[{"start":1,"end":18,"type":"D"}],"Structural state":[{"start":1,"end":18,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00176","name":"SNF2-related domain","start":699,"end":998},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":1250,"end":1359},{"id":"PF07529","name":"HSA domain","start":349,"end":411}],"gene3D":[{"start":664,"end":958,"id":"3.40.50.10810","name":"Tandem AAA-ATPase domain"},{"start":1208,"end":1492,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_Q05471","sequence":"MTTSRKSHAKDKKAGGEQDLADLKFRYDLLTNELFHLREFVSLVDYDPTHFNDSESFQKFLRETHLSLEERGEKFTDDVAKKGTNGDLTRRRRNLRTSTVVSSETTNEKKGDIELKLESIAPLVRNKCEELKYKLSDHSNRKSIVPQKRPIQHLKKREAAKSLKFKSERKENPLPLHEHIAEERYDHIAKVEEPSEAFTIKCPSDDSSFENTSEHYSDNFYFTTSSEEEDIKKKRGRKKKKPRIKLVVHPPKQTITNPLHVVKPGYESLHEYIASFKSLEDDLTLEEYNKYIDEQRRLLSRLKKGIENGALKYDKETDSLQPITSKEIKTIITYKPDPISYFYKQQDLQIHTDHLINQGIHMSKLFRSSTKARIARAKKVSQMIEQHFKHVAGAEERKAKEEERHKKSLARFAVQAVKKRWNMAEKAYRILRKDEEEQLKRIEGKQHLSKMLEKSTQLLEAQLNQVNDDGRSSTPSSDSNDVLSESDDDMDDELSTSSDEDEEVDADVGLENSPASTEATPTDESLNLIQLKEKYGHFNGSSTVYDSRNKDEKFPTLDKHESSSSESSVMTGEESSIYSSSENESQNENDRESDDKTPSVGLSALFGKGEESDGDLDLDDSEDFTVNSSSVEGEELEKDQVDNSAATFERAGDFVHTQNENRDDIKDVEEDAETKVQEEQLSVVDVPVPSLLRGNLRTYQKQGLNWLASLYNNHTNGILADEMGLGKTIQTISLLAYLACEKENWGPHLIVVPTSVLLNWEMEFKRFAPGFKVLTYYGSPQQRKEKRKGWNKPDAFHVCIVSYQLVVQDQHSFKRKRWQYMVLDEAHNIKNFRSTRWQALLNFNTQRRLLLTGTPLQNNLAELWSLLYFLMPQTVIDGKKVSGFADLDAFQQWFGRPVDKIIETGQNFGQDKETKKTVAKLHQVLRPYLLRRLKADVEKQMPAKYEHIVYCKLSKRQRFLYDDFMSRAQTKATLASGNFMSIVNCLMQLRKVCNHPNLFEVRPILTSFVLEHCVASDYKDVERTLLKLFKKNNQVNRVDLDFLNLVFTLNDKDLTSYHAEEISKLTCVKNFVEEVNKLRETNKQLQEEFGEASFLNFQDANQYFKYSNKQKLEGTVDMLNFLKMVNKLRCDRRPIFGKNLIDLLTKDRRVKYDKSSIIDNELIKPLQTRVLDNRKIIDTFAVLTPSAVSLDMRKLALGLNDDSSVGENTRLKVMQNCFEVSNPLHQLQTKLTIAFPDKSLLQYDCGKLQKLAILLQQLKDNGHRALIFTQMTKVLDVLEQFLNYHGYLYMRLDGATKIEDRQILTERFNTDSRITVFILSSRSGGLGINLTGADTVIFYDSDWNPAMDKQCQDRCHRIGQTRDVHIYRFVSEHTIESNILKKANQKRQLDNVVIQEGDFTTDYFSKLSVRDLLGSELPENASGGDKPLIADADVAAKDPRQLERLLAQAEDEDDVKAANLAMREVEIDNDDFDESTEKKAANEEEENHAELDEYEGTAHVDEYMIRFIANGYYY","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q05471","disprot_id":"DP02295","ncbi_taxon_id":559292,"regions_counter":5,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":614,"region_id":"DP02295r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The catalytic subunit of the SWR1 remodeler is a histone chaperone for the H2A.Z-H2B dimer. <i> Hong J, Feng H, Wang F, Ranjan A, Chen J, Jiang J, Ghirlando R, Xiao TS, Wu C, Bai Y. </i> Mol Cell, 2014","term_id":"IDPO:0000002","curator_id":"ahatos","start":605,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4M6B"}],"reference_id":"24507717","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":627,"region_id":"DP02295r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The catalytic subunit of the SWR1 remodeler is a histone chaperone for the H2A.Z-H2B dimer. <i> Hong J, Feng H, Wang F, Ranjan A, Chen J, Jiang J, Ghirlando R, Xiao TS, Wu C, Bai Y. </i> Mol Cell, 2014","term_id":"IDPO:0000002","curator_id":"ahatos","start":599,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4M6B"}],"reference_id":"24507717","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":627,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"The catalytic subunit of the SWR1 remodeler is a histone chaperone for the H2A.Z-H2B dimer. <i> Hong J, Feng H, Wang F, Ranjan A, Chen J, Jiang J, Ghirlando R, Xiao TS, Wu C, Bai Y. </i> Mol Cell, 2014","term_id":"IDPO:0000011","curator_id":"ahatos","start":599,"term_ontology":"IDPO","curator_name":"András Hatos","reference_id":"24507717","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02295r003","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":627,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"The catalytic subunit of the SWR1 remodeler is a histone chaperone for the H2A.Z-H2B dimer. <i> Hong J, Feng H, Wang F, Ranjan A, Chen J, Jiang J, Ghirlando R, Xiao TS, Wu C, Bai Y. </i> Mol Cell, 2014","statement":[{"text":"We observed that the Swr1 subunit uses the intrinsically disordered Swr1-Z domain to specifically recognize H2A.Z-H2B through interac- tions between the LxxLF motif of the Swr1-Z domain and the hydrophobic residues in the aC helix of H2A.Z. Mutation of\nthe hydrophobic residues in the LxxLF motif or deletion of the Swr1-Z domain leads to slow-cell-growth phenotype in the presence of caffeine.","type":"Discussion"}],"term_id":"GO:0060090","curator_id":"ahatos","start":599,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"24507717","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02295r004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":627,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"The catalytic subunit of the SWR1 remodeler is a histone chaperone for the H2A.Z-H2B dimer. <i> Hong J, Feng H, Wang F, Ranjan A, Chen J, Jiang J, Ghirlando R, Xiao TS, Wu C, Bai Y. </i> Mol Cell, 2014","term_id":"GO:0005515","curator_id":"ahatos","start":599,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"24507717","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4M6B"}],"region_id":"DP02295r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q05471","date":"2018-08-31T16:59:25.000Z","acc":"Q05471","name":"Helicase SWR1","length":1514,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000013A81C","genes":[{"name":{"value":"SWR1"},"orfNames":[{"value":"D9651.6"}],"olnNames":[{"value":"YDR334W"}]}],"alphafold_very_low_content":0.3368560105680317,"disorder_content":0.01915455746367239,"disprot_consensus":{"full":[{"start":599,"end":627,"type":"T"}],"Structural state":[{"start":599,"end":627,"type":"D"}],"Structural transition":[{"start":599,"end":627,"type":"T"}],"Molecular function":[{"start":599,"end":627,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00612","name":"IQ calmodulin-binding motif","start":28,"end":47}],"gene3D":[{"start":22,"end":50,"id":"1.20.5.190","name":"1.20.5.190"}]},"uniref50":"UniRef50_P60761","sequence":"MDCCTESACSKPDDDILDIPLDDPGANAAAAKIQASFRGHMARKKIKSGECGRKGPGPGGPGGAGGARGGAGGGPSGD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P60761","disprot_id":"DP02296","ncbi_taxon_id":10090,"regions_counter":8,"creator":"stama","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":47,"region_id":"DP02296r001","released":"2022_03","ec_id":"ECO:0006232","reference_html":"Structural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with Calmodulin. <i> Kumar V, Chichili VP, Zhong L, Tang X, Velazquez-Campoy A, Sheu FS, Seetharaman J, Gerges NZ, Sivaraman J. </i> Sci Rep, 2013","statement":[{"text":"Here, we report the structure of IQ peptides (24aa) of Nm/Ng complexed with CaM and their functional studies with full-length proteins. Nm/Ng and their respective IQ peptides are intrinsically unstructured; however, upon binding with CaM, IQ motifs adopt a helical conformation. Ser41 (Ser36) of Nm (Ng) is located in a negatively charged pocket in the apo CaM and, when phosphorylated, it will repel Nm/Ng from CaM.","type":"Abstract"}],"term_id":"IDPO:0000002","curator_id":"stama","start":26,"term_ontology":"IDPO","curator_name":"Stella Tamana","ec_name":"differential scanning calorimetry evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4E50"}],"reference_id":"23462742","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":47,"term_name":"disorder to molten globule","released":"2022_03","ec_name":"differential scanning calorimetry evidence used in manual assertion","reference_html":"Structural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with Calmodulin. <i> Kumar V, Chichili VP, Zhong L, Tang X, Velazquez-Campoy A, Sheu FS, Seetharaman J, Gerges NZ, Sivaraman J. </i> Sci Rep, 2013","term_id":"IDPO:0000018","curator_id":"stama","start":26,"term_ontology":"IDPO","curator_name":"Stella Tamana","reference_id":"23462742","version":2,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006232","region_id":"DP02296r002","ec_go":"IDA","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":47,"region_id":"DP02296r003","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with Calmodulin. <i> Kumar V, Chichili VP, Zhong L, Tang X, Velazquez-Campoy A, Sheu FS, Seetharaman J, Gerges NZ, Sivaraman J. </i> Sci Rep, 2013","term_id":"IDPO:0000002","curator_id":"stama","start":26,"term_ontology":"IDPO","curator_name":"Stella Tamana","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4E50"}],"reference_id":"23462742","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":47,"term_name":"disorder to molten globule","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with Calmodulin. <i> Kumar V, Chichili VP, Zhong L, Tang X, Velazquez-Campoy A, Sheu FS, Seetharaman J, Gerges NZ, Sivaraman J. </i> Sci Rep, 2013","term_id":"IDPO:0000018","curator_id":"stama","start":26,"term_ontology":"IDPO","curator_name":"Stella Tamana","reference_id":"23462742","version":2,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP02296r004","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":62,"region_id":"DP02296r005","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Structural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with Calmodulin. <i> Kumar V, Chichili VP, Zhong L, Tang X, Velazquez-Campoy A, Sheu FS, Seetharaman J, Gerges NZ, Sivaraman J. </i> Sci Rep, 2013","term_id":"IDPO:0000002","curator_id":"stama","start":51,"term_ontology":"IDPO","curator_name":"Stella Tamana","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4E50"}],"reference_id":"23462742","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":62,"term_name":"disorder to pre-molten globule","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","reference_html":"Structural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with Calmodulin. <i> Kumar V, Chichili VP, Zhong L, Tang X, Velazquez-Campoy A, Sheu FS, Seetharaman J, Gerges NZ, Sivaraman J. </i> Sci Rep, 2013","term_id":"IDPO:0000019","curator_id":"stama","start":51,"term_ontology":"IDPO","curator_name":"Stella Tamana","reference_id":"23462742","version":2,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP02296r006","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":62,"region_id":"DP02296r007","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with Calmodulin. <i> Kumar V, Chichili VP, Zhong L, Tang X, Velazquez-Campoy A, Sheu FS, Seetharaman J, Gerges NZ, Sivaraman J. </i> Sci Rep, 2013","term_id":"IDPO:0000002","curator_id":"stama","start":51,"term_ontology":"IDPO","curator_name":"Stella Tamana","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4E50"}],"reference_id":"23462742","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":62,"term_name":"disorder to molten globule","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with Calmodulin. <i> Kumar V, Chichili VP, Zhong L, Tang X, Velazquez-Campoy A, Sheu FS, Seetharaman J, Gerges NZ, Sivaraman J. </i> Sci Rep, 2013","term_id":"IDPO:0000018","curator_id":"stama","start":51,"term_ontology":"IDPO","curator_name":"Stella Tamana","reference_id":"23462742","version":2,"curator_orcid":"0000-0002-3414-4972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP02296r008","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_P60761","date":"2018-08-31T17:12:04.000Z","acc":"P60761","name":"Neurogranin","length":78,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000000923","genes":[{"name":{"value":"Nrgn"}}],"alphafold_very_low_content":0.2948717948717949,"disorder_content":0.4358974358974359,"disprot_consensus":{"full":[{"start":26,"end":47,"type":"T"},{"start":51,"end":62,"type":"T"}],"Structural state":[{"start":26,"end":47,"type":"D"},{"start":51,"end":62,"type":"D"}],"Structural transition":[{"start":26,"end":47,"type":"T"},{"start":51,"end":62,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00985","name":"Merozoite Surface Antigen 2 (MSA-2) family","start":102,"end":272}]},"uniref50":"UniRef50_P50498","sequence":"MKVIKTLSIINFFIFVTFNIKNESKYSNTFINNAYNMSIRRSMAESKPSTGAGGSAGGSAGGSAGGSAGGSAGGSAGSGDGNGADAEGSSSTPATTTTTKTTTTTTTTNDAEASTSTSSENPNHKNAETNPKGKGEVQEPNQANKETQNNSNVQQDSQTKSNVPPTQDADTKSPTAQPEQAENSAPTAEQTESPELQSAPENKGTGQHGHMHGSRNNHPQNTSDSQKECTDGNKENCGAATSLLNNSSNIASINKFVVLISATLVLSFAIFI","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"uniref90":"UniRef90_P50498","disprot_id":"DP02299","ncbi_taxon_id":36329,"regions_counter":4,"creator":"thorvath","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":272,"region_id":"DP02299r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Solution conformation, backbone dynamics and lipid interactions of the intrinsically unstructured malaria surface protein MSP2. <i> Zhang X, Perugini MA, Yao S, Adda CG, Murphy VJ, Low A, Anders RF, Norton RS. </i> J Mol Biol, 2008","statement":[{"text":"The spectra for 3D7-6H under all conditions examined are remarkably similar, showing a single minimum at approximately 198 nm, indicative of a largely unstructured protein","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"thorvath","start":1,"term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"18440022","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":272,"region_id":"DP02299r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Solution conformation, backbone dynamics and lipid interactions of the intrinsically unstructured malaria surface protein MSP2. <i> Zhang X, Perugini MA, Yao S, Adda CG, Murphy VJ, Low A, Anders RF, Norton RS. </i> J Mol Biol, 2008","statement":[{"text":"One-dimensional 1H NMR spectra of MSP2 under both physiological and acidic conditions show typical characteristics of an unstructured protein,","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"thorvath","start":1,"term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"18440022","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":270,"region_id":"DP02299r003","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Plasmodium falciparum merozoite surface protein 2 is unstructured and forms amyloid-like fibrils. <i> Adda CG, Murphy VJ, Sunde M, Waddington LJ, Schloegel J, Talbo GH, Vingas K, Kienzle V, Masciantonio R, Howlett GJ, Hodder AN, Foley M, Anders RF. </i> Mol Biochem Parasitol, 2009","statement":[{"text":"The CD spectra of both monomeric and polymeric 3D7 MSP2 are dominated by an ellipticity minimum at ~210 nm, indicating a high content of random coil","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"thorvath","start":1,"term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"19450733","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":272,"region_id":"DP02299r004","released":"2022_03","ec_id":"ECO:0006275","reference_html":"Solution conformation, backbone dynamics and lipid interactions of the intrinsically unstructured malaria surface protein MSP2. <i> Zhang X, Perugini MA, Yao S, Adda CG, Murphy VJ, Low A, Anders RF, Norton RS. </i> J Mol Biol, 2008","statement":[{"text":"Furthermore, the axial ratio (a/b) of 17.2, calculated from the sedimentation coefficient and monomeric molecular mass assuming a prolate ellipsoidal shape (Table 1), indicates that the 3D7-6H monomer is significantly elongated in solution","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"thorvath","start":1,"term_ontology":"IDPO","curator_name":"Tamas Horvath","reference_id":"18440022","version":2,"ec_name":"analytical ultracentrifugation evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P50498","date":"2018-08-31T17:29:02.000Z","acc":"P50498","name":"Merozoite surface antigen 2","length":272,"organism":"Plasmodium falciparum (isolate 3D7)","dataset":[],"UniParc":"UPI000002C0CC","genes":[{"name":{"value":"MSA2"},"orfNames":[{"value":"PFB0300c"}]}],"alphafold_very_low_content":0.7463235294117647,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":272,"type":"D"}],"Structural state":[{"start":1,"end":272,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00125","name":"Core histone H2A/H2B/H3/H4 domain","start":10,"end":93},{"id":"PF16211","name":"C-terminus of histone H2A","start":95,"end":127}],"gene3D":[{"start":4,"end":128,"id":"1.10.20.10","name":"Histone, subunit A"}]},"uniref50":"UniRef50_Q71UI9","sequence":"MAGGKAGKDSGKAKAKAVSRSQRAGLQFPVGRIHRHLKTRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q71UI9","disprot_id":"DP02301","ncbi_taxon_id":9606,"regions_counter":3,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":48,"region_id":"DP02301r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structural polymorphism in the L1 loop regions of human H2A.Z.1 and H2A.Z.2. <i> Horikoshi N, Sato K, Shimada K, Arimura Y, Osakabe A, Tachiwana H, Hayashi-Takanaka Y, Iwasaki W, Kagawa W, Harata M, Kimura H, Kurumizaka H. </i> Acta Crystallogr D Biol Crystallogr, 2013","statement":[{"text":"The H2A.Z.1 and H2A.Z.2 L1 loop regions are flexible.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jpujols","start":39,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3WAA"}],"reference_id":"24311584","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":48,"term_name":"molecular adaptor activity","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural polymorphism in the L1 loop regions of human H2A.Z.1 and H2A.Z.2. <i> Horikoshi N, Sato K, Shimada K, Arimura Y, Osakabe A, Tachiwana H, Hayashi-Takanaka Y, Iwasaki W, Kagawa W, Harata M, Kimura H, Kurumizaka H. </i> Acta Crystallogr D Biol Crystallogr, 2013","statement":[{"text":"Region 39-39 of H2A.V correlates with the canonical loop 1 of the H2A and H2B protein family.\n([Pubmed ID: 23002134]: Furthermore, contacts between the H2A L1 loops of the two H2A–H2B dimers stabilize their association within the nucleosome)","type":"Curator statement"}],"term_id":"GO:0060090","curator_id":"jpujols","start":39,"term_ontology":"GO","curator_name":"Jordi Pujols Pujol","reference_id":"24311584","version":3,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02301r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":48,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structural polymorphism in the L1 loop regions of human H2A.Z.1 and H2A.Z.2. <i> Horikoshi N, Sato K, Shimada K, Arimura Y, Osakabe A, Tachiwana H, Hayashi-Takanaka Y, Iwasaki W, Kagawa W, Harata M, Kimura H, Kurumizaka H. </i> Acta Crystallogr D Biol Crystallogr, 2013","statement":[{"text":"Region 39-39 of H2A.V correlates with the canonical loop 1 of the H2A and H2B protein family.\n([Pubmed ID: 23002134]: Furthermore, contacts between the H2A L1 loops of the two H2A–H2B dimers stabilize their association within the nucleosome)","type":"Curator statement"}],"term_id":"GO:0005515","curator_id":"jpujols","start":39,"term_ontology":"GO","curator_name":"Jordi Pujols Pujol","reference_id":"24311584","version":3,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02301r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q71UI9","date":"2018-08-31T17:40:20.000Z","acc":"Q71UI9","name":"Histone H2A.V","length":128,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000001D4","genes":[{"name":{"value":"H2AZ2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:20664","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:20664"}}]},"synonyms":[{"value":"H2AFV","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:20664","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:20664"}}]},{"value":"H2AV"}]}],"alphafold_very_low_content":0.0703125,"disorder_content":0.078125,"disprot_consensus":{"full":[{"start":39,"end":48,"type":"D"}],"Structural state":[{"start":39,"end":48,"type":"D"}],"Molecular function":[{"start":39,"end":48,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00240","name":"Ubiquitin family","start":3,"end":73}],"gene3D":[{"start":1,"end":77,"id":"3.10.20.90","name":"Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1"}]},"uniref50":"UniRef50_Q15843","sequence":"MLIKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQQRLIYSGKQMNDEKTAADYKILGGSVLHLVLALRGGGGLRQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q15843","disprot_id":"DP02302","ncbi_taxon_id":9606,"regions_counter":3,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":81,"region_id":"DP02302r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"The structure of the APPBP1-UBA3-NEDD8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an E1. <i> Walden H, Podgorski MS, Huang DT, Miller DW, Howard RJ, Minor DL, Holton JM, Schulman BA. </i> Mol Cell, 2003","statement":[{"text":"The most striking difference between free (Whitby et al., 1998) and complexed NEDD8 is the C-terminal tail (Figure 5B), which rotates 30  about Leu69 to form the complex. Complex formation induces order in the C-terminal 3 residues, which are disordered in free NEDD8. The C-terminal tail adopts an extended strand-like conformation as it docks into the nucleotide binding pocket in UBA3.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ahatos","start":69,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1R4M"}],"reference_id":"14690597","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":81,"term_name":"disorder to order","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"The structure of the APPBP1-UBA3-NEDD8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an E1. <i> Walden H, Podgorski MS, Huang DT, Miller DW, Howard RJ, Minor DL, Holton JM, Schulman BA. </i> Mol Cell, 2003","statement":[{"text":"The C-terminal tail adopts an extended strand-like conformation as it docks into the nucleotide binding pocket in UBA3.","type":"Results"}],"term_id":"IDPO:0000011","curator_id":"ahatos","start":69,"term_ontology":"IDPO","curator_name":"András Hatos","reference_id":"14690597","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02302r002","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":81,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"The structure of the APPBP1-UBA3-NEDD8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an E1. <i> Walden H, Podgorski MS, Huang DT, Miller DW, Howard RJ, Minor DL, Holton JM, Schulman BA. </i> Mol Cell, 2003","statement":[{"text":"The C-terminal tail adopts an extended strand-like conformation as it docks into the nucleotide binding pocket in UBA3.","type":"Results"}],"term_id":"GO:0005515","curator_id":"ahatos","start":69,"term_ontology":"GO","curator_name":"András Hatos","reference_id":"14690597","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02302r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q15843","date":"2018-08-31T18:32:18.000Z","acc":"Q15843","name":"NEDD8","length":81,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000009A5","genes":[{"name":{"value":"NEDD8","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9694792","url":"http://www.ncbi.nlm.nih.gov/pubmed/9694792","alternativeUrl":"https://europepmc.org/abstract/MED/9694792"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:7732","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:7732"}}]}}],"alphafold_very_low_content":0.07407407407407407,"disorder_content":0.16049382716049382,"disprot_consensus":{"full":[{"start":69,"end":81,"type":"T"}],"Structural state":[{"start":69,"end":81,"type":"D"}],"Structural transition":[{"start":69,"end":81,"type":"T"}],"Molecular function":[{"start":69,"end":81,"type":"F"}]}},{"features":{"pfam":[{"id":"PF10291","name":"Muniscin C-terminal mu homology domain","start":543,"end":808},{"id":"PF22699","name":"GEM-interacting protein-like, FCH domain","start":16,"end":262}],"gene3D":[{"start":2,"end":274,"id":"1.20.1270.60","name":"Arfaptin homology (AH) domain/BAR domain"}]},"uniref50":"UniRef50_Q3UQN2","sequence":"MVMAYFVENFWGEKNSGFDVLYHNMKHGQISTKELADFVRERATIEEAYSRSMTKLAKSASNYSQLGTFAPVWDVFKTSTEKLANCHLDLVRKLQELIKEVQKYGEEQVKSHKKTKEEVAGTLEAVQTIQSITQALQKSKENYNAKCVEQERLKKEGATQREIEKAAVKSKKATDTYKLYVEKYALAKADFEQKMTETAQKFQDIEETHLIHIKEIIGSLSNAIKEIHLQIGQVHEEFINNMANTTVESLIQKFAESKGTGKERPGLIEFEECDTASAVEGIKPRKRKTFALPGIIKKEKDAESVECPDADSLNIPDVDEEGYSIKPETNQNDTKENHFYSSSDSDSEDEEPKKYRIEIKPMHPNNSHHTMASLDELKVSIGNITLSPAISRHSPVQMNRNLSNEELTKSKPSAPPNEKGTSDLLAWDPLFGPSLDSSSSSSLTSSSSARPTTPLSVGTIVPPPRPASRPKLTSGKLSGINEIPRPFSPPVTSNTSPPPAAPLARAESSSSISSSASLSAANTPTVGVSRGPSPVSLGNQDTLPVAVALTESVNAYFKGADPTKCIVKITGDMTMSFPSGIIKVFTSNPTPAVLCFRVKNISRLEQILPNAQLVFSDPSQCDSNTKDFWMNMQAVTVYLKKLSEQNPAASYYNVDVLKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMVAPSVLSNIQVVVPVDGGVTNMQSLPPAIWNAEQMKAFWKLSSISEKSENGGSGSLRAKFDLSEGPSKPTTLAVQFLSEGSTLSGVDFELVGTGYRLSLIKKRFATGRYLADC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q3UQN2","disprot_id":"DP02303","ncbi_taxon_id":9606,"regions_counter":1,"creator":"baykac","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":274,"region_id":"DP02303r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature. <i> Henne WM, Kent HM, Ford MG, Hegde BG, Daumke O, Butler PJ, Mittal R, Langen R, Evans PR, McMahon HT. </i> Structure, 2007","term_id":"IDPO:0000002","curator_id":"baykac","start":259,"term_ontology":"IDPO","curator_name":"Burcu Aykac-Fas","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-3842-731X","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"2V0O"}],"reference_id":"17540576","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q0JRZ9","date":"2018-08-31T18:40:14.000Z","acc":"Q0JRZ9","name":"F-BAR domain only protein 2","length":810,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000019971A","genes":[{"name":{"value":"FCHO2"}}],"alphafold_very_low_content":0.29506172839506173,"disorder_content":0.019753086419753086,"disprot_consensus":{"full":[{"start":259,"end":274,"type":"D"}],"Structural state":[{"start":259,"end":274,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00787","name":"PX domain","start":306,"end":380},{"id":"PF10456","name":"WASP-binding domain of Sorting nexin protein","start":386,"end":541},{"id":"PF14604","name":"Variant SH3 domain","start":7,"end":57}],"gene3D":[{"start":256,"end":391,"id":"3.30.1520.10","name":"Phox-like domain"},{"start":434,"end":545,"id":"1.20.1270.60","name":"Arfaptin homology (AH) domain/BAR domain"},{"start":1,"end":66,"id":"2.30.30.40","name":"SH3 Domains"}]},"uniref50":"UniRef50_Q96RF0","sequence":"MALRARALYDFRSENPGEISLREHEVLSLCSEQDIEGWLEGVNSRGDRGLFPASYVQVIRAPEPGPAGDGGPGAPARYANVPPGGFEPLPVAPPASFKPPPDAFQALLQPQQAPPPSTFQPPGAGFPYGGGALQPSPQQLYGGYQASQGSDDDWDDEWDDSSTVADEPGALGSGAYPDLDGSSSAGVGAAGRYRLSTRSDLSLGSRGGSVPPQHHPSGPKSSATVSRNLNRFSTFVKSGGEAFVLGEASGFVKDGDKLCVVLGPYGPEWQENPYPFQCTIDDPTKQTKFKGMKSYISYKLVPTHTQVPVHRRYKHFDWLYARLAEKFPVISVPHLPEKQATGRFEEDFISKRRKGLIWWMNHMASHPVLAQCDVFQHFLTCPSSTDEKAWKQGKRKAEKDEMVGANFFLTLSTPPAAALDLQEVESKIDGFKCFTKKMDDSALQLNHTANEFARKQVTGFKKEYQKVGQSFRGLSQAFELDQQAFSVGLNQAIAFTGDAYDAIGELFAEQPRQDLDPVMDLLALYQGHLANFPDIIHVQKGKAWPLEQVIWSVLCRLKGATLTAVPLWVSESYSTGEEASRDVDAWVFSLECKLDCSTGSFLLEYLALGNEYSFSKVQRVPLMTVLSF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q96RF0","disprot_id":"DP02309","ncbi_taxon_id":9606,"regions_counter":9,"creator":"vsagris","regions":[{"start":154,"end":158,"reference_id":"23878278","reference_source":"pmid","reference_html":"Membrane remodeling by the PX-BAR protein SNX18 promotes autophagosome formation. <i> Knævelsrud H, Søreng K, Raiborg C, Håberg K, Rasmuson F, Brech A, Liestøl K, Rusten TE, Stenmark H, Neufeld TP, Carlsson SR, Simonsen A. </i> J Cell Biol, 2013","date":"2022-06-17T09:33:05.716Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001245","ec_ontology":"ECO","ec_name":"peptide array evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","region_id":"DP02309r003","statement":[{"text":"The SNX18 WDDEW motif found to interact with LC3/GABARAP is a noncanonical motif because of the presence of the W and several acidic residues, and the lack of the hydrophobic residue in the L position.","type":"Discussion"},{"text":"Interestingly, this motif is also required for the SNX18 interaction with AP-1, an adaptor protein implicated in autophagosome biogenesis from the trans-Golgi network (Guo et al., 2012).","type":"Discussion"},{"text":"The interaction site was mapped to the SNX18 SH3-LC region (Fig. 7 A) and the exact sequence was determined by a peptide array covering the entire SNX18 SH3-LC sequence, where GST-GABARAP bound to all peptides containing 154-WDDEW-158 (Fig. 7 B), the same motif previously found to mediate binding of SNX18 to AP-1 (Håberg et al., 2008).","type":"Results"},{"text":"In summary, SNX18 interacts with Atg8 proteins through a WDDEW sequence in its SH3-LC region, and this interaction is required for localization of GFP-LC3 to SNX18-induced tubules and for GFP-LC3 spot formation.","type":"Results"},{"text":"The annotation includes the noncanonical motif WDDEW at position 154-158.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"Q9GZQ8","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"O95166","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q05140","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q10567","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:54:16.878Z"}},{"start":154,"end":158,"reference_id":"23878278","reference_source":"pmid","reference_html":"Membrane remodeling by the PX-BAR protein SNX18 promotes autophagosome formation. <i> Knævelsrud H, Søreng K, Raiborg C, Håberg K, Rasmuson F, Brech A, Liestøl K, Rusten TE, Stenmark H, Neufeld TP, Carlsson SR, Simonsen A. </i> J Cell Biol, 2013","date":"2022-06-17T09:36:44.453Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","region_id":"DP02309r004","statement":[{"text":"The SNX18 WDDEW motif found to interact with LC3/GABARAP is a noncanonical motif because of the presence of the W and several acidic residues, and the lack of the hydrophobic residue in the L position.","type":"Discussion"},{"text":"Interestingly, this motif is also required for the SNX18 interaction with AP-1, an adaptor protein implicated in autophagosome biogenesis from the trans-Golgi network (Guo et al., 2012).","type":"Discussion"},{"text":"Mutation of one or both of the tryptophan residues (W154S and/or W158S) abolished the interaction with LC3/GABARAP (Fig. 7, C and D).","type":"Results"},{"text":"Furthermore, although tubules were still formed in cells expressing the myc-SNX18 W154S/W158S mutant, these were negative for GFP-LC3 (Fig. 7 E), and the number of GFP-LC3 spots was also significantly reduced compared with SNX18 WT (Fig. 7 F).","type":"Results"},{"text":"In summary, SNX18 interacts with Atg8 proteins through a WDDEW sequence in its SH3-LC region, and this interaction is required for localization of GFP-LC3 to SNX18-induced tubules and for GFP-LC3 spot formation.","type":"Results"},{"text":"Figure 7. A WDDEW sequence in the SNX18 LC region mediates the interaction with LC3/GABARAP. The annotation includes the noncanonical motif WDDEW at position 154-158. (C) Peptides with the sequence YGGYQASQGSDDDWDDEWDDSSTVADEPGAL (SNX18 WT) or with the first (SNX18 W154S), the second (SNX18 W158S), or both (SNX18 W154S/W158S) W mutated to S were spotted on membranes that were incubated with GST, GST-LC3B, or GST-GABARAP. Binding was analyzed as in B. (D) GFP-SNX18 WT and the indicated mutants were in vitro translated and incubated with GST-LC3B or -GABARAP, and their binding was analyzed as in A. (E) HeLa GFP-LC3 cells were transfected with myc-SNX18 W154S/W158S mutant, starved for 2 h, immunostained against myc, and analyzed by confocal imaging. Bar, 10 µm.","type":"Figure"},{"text":"The annotation includes the noncanonical motif WDDEW at position 154-158.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"Q9GZQ8","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"O95166","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q05140","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q10567","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:54:31.128Z"}},{"start":154,"end":158,"reference_id":"23878278","reference_source":"pmid","reference_html":"Membrane remodeling by the PX-BAR protein SNX18 promotes autophagosome formation. <i> Knævelsrud H, Søreng K, Raiborg C, Håberg K, Rasmuson F, Brech A, Liestøl K, Rusten TE, Stenmark H, Neufeld TP, Carlsson SR, Simonsen A. </i> J Cell Biol, 2013","date":"2022-06-17T09:38:26.459Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001245","ec_ontology":"ECO","ec_name":"peptide array evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","region_id":"DP02309r005","statement":[{"text":"The SNX18 WDDEW motif found to interact with LC3/GABARAP is a noncanonical motif because of the presence of the W and several acidic residues, and the lack of the hydrophobic residue in the L position. \n\n","type":"Discussion"},{"text":"Interestingly, this motif is also required for the SNX18 interaction with AP-1, an adaptor protein implicated in autophagosome biogenesis from the trans-Golgi network (Guo et al., 2012).","type":"Discussion"},{"text":"The interaction site was mapped to the SNX18 SH3-LC region (Fig. 7 A) and the exact sequence was determined by a peptide array covering the entire SNX18 SH3-LC sequence, where GST-GABARAP bound to all peptides containing 154-WDDEW-158 (Fig. 7 B), the same motif previously found to mediate binding of SNX18 to AP-1 (Håberg et al., 2008).","type":"Results"},{"text":" In summary, SNX18 interacts with Atg8 proteins through a WDDEW sequence in its SH3-LC region, and this interaction is required for localization of GFP-LC3 to SNX18-induced tubules and for GFP-LC3 spot formation.","type":"Results"},{"text":"The annotation includes the noncanonical motif WDDEW at position 154-158.","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"Q9GZQ8","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"O95166","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q05140","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q10567","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:54:32.393Z"}},{"start":154,"end":158,"reference_id":"23878278","reference_source":"pmid","reference_html":"Membrane remodeling by the PX-BAR protein SNX18 promotes autophagosome formation. <i> Knævelsrud H, Søreng K, Raiborg C, Håberg K, Rasmuson F, Brech A, Liestøl K, Rusten TE, Stenmark H, Neufeld TP, Carlsson SR, Simonsen A. </i> J Cell Biol, 2013","date":"2022-06-17T07:42:14.821Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","region_id":"DP02309r006","statement":[{"text":"The SNX18 WDDEW motif found to interact with LC3/GABARAP is a noncanonical motif because of the presence of the W and several acidic residues, and the lack of the hydrophobic residue in the L position. ","type":"Discussion"},{"text":"Interestingly, this motif is also required for the SNX18 interaction with AP-1, an adaptor protein implicated in autophagosome biogenesis from the trans-Golgi network (Guo et al., 2012).","type":"Discussion"},{"text":"Mutation of one or both of the tryptophan residues (W154S and/or W158S) abolished the interaction with LC3/GABARAP (Fig. 7, C and D).","type":"Results"},{"text":"Furthermore, although tubules were still formed in cells expressing the myc-SNX18 W154S/W158S mutant, these were negative for GFP-LC3 (Fig. 7 E), and the number of GFP-LC3 spots was also significantly reduced compared with SNX18 WT (Fig. 7 F).","type":"Results"},{"text":" In summary, SNX18 interacts with Atg8 proteins through a WDDEW sequence in its SH3-LC region, and this interaction is required for localization of GFP-LC3 to SNX18-induced tubules and for GFP-LC3 spot formation.","type":"Results"},{"text":"Figure 7. A WDDEW sequence in the SNX18 LC region mediates the interaction with LC3/GABARAP. The annotation includes the noncanonical motif WDDEW at position 154-158. (C) Peptides with the sequence YGGYQASQGSDDDWDDEWDDSSTVADEPGAL (SNX18 WT) or with the first (SNX18 W154S), the second (SNX18 W158S), or both (SNX18 W154S/W158S) W mutated to S were spotted on membranes that were incubated with GST, GST-LC3B, or GST-GABARAP. Binding was analyzed as in B. (D) GFP-SNX18 WT and the indicated mutants were in vitro translated and incubated with GST-LC3B or -GABARAP, and their binding was analyzed as in A. (E) HeLa GFP-LC3 cells were transfected with myc-SNX18 W154S/W158S mutant, starved for 2 h, immunostained against myc, and analyzed by confocal imaging. Bar, 10 µm.","type":"Figure"},{"text":"The annotation includes the noncanonical motif WDDEW at position 154-158.","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:54:35.536Z"}},{"start":154,"end":158,"reference_id":"23878278","reference_source":"pmid","reference_html":"Membrane remodeling by the PX-BAR protein SNX18 promotes autophagosome formation. <i> Knævelsrud H, Søreng K, Raiborg C, Håberg K, Rasmuson F, Brech A, Liestøl K, Rusten TE, Stenmark H, Neufeld TP, Carlsson SR, Simonsen A. </i> J Cell Biol, 2013","date":"2022-06-17T09:37:13.700Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"Q9GZQ8","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"O95166","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q05140","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q10567","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP02309r007","statement":[{"text":"Figure 7. A WDDEW sequence in the SNX18 LC region mediates the interaction with LC3/GABARAP. (A) GFP-p62 or -SNX18 full-length, SH3-LC, or PX-BAR regions were in vitro translated and incubated with GST-LC3B or -GABARAP. The resulting pulldowns were separated by SDS-PAGE. Bound proteins were detected by autoradiography and GST proteins by Coomassie blue staining.","type":"Figure"},{"text":"The annotation includes the noncanonical motif WDDEW at position 154-158.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:54:36.753Z"}},{"start":154,"end":158,"reference_id":"23878278","reference_source":"pmid","reference_html":"Membrane remodeling by the PX-BAR protein SNX18 promotes autophagosome formation. <i> Knævelsrud H, Søreng K, Raiborg C, Håberg K, Rasmuson F, Brech A, Liestøl K, Rusten TE, Stenmark H, Neufeld TP, Carlsson SR, Simonsen A. </i> J Cell Biol, 2013","date":"2022-06-17T09:37:53.957Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IEP","interaction_partner":[{"db":"UniProt","id":"Q9GZQ8","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"O95166","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q05140","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q10567","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP02309r008","statement":[{"text":"Figure 7. A WDDEW sequence in the SNX18 LC region mediates the interaction with LC3/GABARAP. (B) 18-mer peptides covering the entire sequence of the SNX18 SH3-LC region were spotted on a membrane that was incubated with GST or GST-GABARAP, which were detected by immunoblotting against GST. The peptide sequences that specifically bound GST-GABARAP are shown with the common WDDEW motif in bold.","type":"Figure"},{"text":"The annotation includes the noncanonical motif WDDEW at position 154-158.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:54:38.451Z"}},{"start":59,"end":224,"reference_id":"29437695","reference_source":"pmid","reference_html":"SNX18 regulates ATG9A trafficking from recycling endosomes by recruiting Dynamin-2. <i> Søreng K, Munson MJ, Lamb CA, Bjørndal GT, Pankiv S, Carlsson SR, Tooze SA, Simonsen A. </i> EMBO Rep, 2018","date":"2024-03-19T16:52:01.142Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02309r009","statement":[{"text":"The domain structure of SNX18 consists of an N‐terminal SH3 domain followed by an unstructured LC region and a C‐terminal PX‐BAR domain responsible for membrane binding and tubulation.","type":"Figure"}]}],"released":"2018_11","uniref100":"UniRef100_Q96RF0","date":"2018-08-31T20:07:08.000Z","acc":"Q96RF0","name":"Sorting nexin-18","length":628,"organism":"Homo sapiens","dataset":["Autophagy-related proteins"],"UniParc":"UPI0000135B4F","genes":[{"name":{"value":"SNX18","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"18411244","url":"http://www.ncbi.nlm.nih.gov/pubmed/18411244","alternativeUrl":"https://europepmc.org/abstract/MED/18411244"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:19245","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:19245"}}]},"synonyms":[{"value":"SH3PXD3B"}]}],"alphafold_very_low_content":0.4028662420382166,"disorder_content":0.2643312101910828,"disprot_consensus":{"full":[{"start":59,"end":224,"type":"D"}],"Structural state":[{"start":59,"end":224,"type":"D"}],"Molecular function":[{"start":154,"end":158,"type":"F"}],"Biological process":[{"start":154,"end":158,"type":"F"}]}},{"acc":"Q7DD77","sequence":"MKHYALLISFLALSACSQGSEDLNEWMAQTRREAKAEIIPFQAPTLPVAPVYSPPQLTGPNAFDFRRMETDKKGENAPDTKRIKETLEKFSLENMRYVGILKSGQKVSGFIEAEGYVYTVGVGNYLGQNYGRIESITDDSIVLNELIEDSTGNWVSRKAELLLNSSDKNTEQAAAPAAEQN","alphafold_very_low_content":"0.016574585635359115","creator":"thorvath","dataset":[],"date":"2018-08-31T20:33:12.000Z","disprot_id":"DP02311","features":{"pfam":[{"id":"PF04351","name":"Pilus assembly protein, PilP","start":22,"end":163}],"gene3D":[{"start":85,"end":164,"id":"2.30.30.830","name":"2.30.30.830","_id":"685af523b4ac24d5329d94d3"}]},"genes":[{"name":{"value":"pilP","evidences":[{"source":{"id":"AAF42147.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/AAF42147.1","_id":"685af523b4ac24d5329d94e4"},"code":"ECO:0000313","_id":"685af523b4ac24d5329d94e3"}],"_id":"685af523b4ac24d5329d94e5"},"synonyms":[],"olnNames":[{"value":"NMB1811","evidences":[{"source":{"id":"AAF42147.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/AAF42147.1","_id":"685af523b4ac24d5329d94e8"},"code":"ECO:0000313","_id":"685af523b4ac24d5329d94e7"}],"_id":"685af523b4ac24d5329d94e6"}],"orfNames":[],"_id":"685af523b4ac24d5329d94e2"}],"length":181,"name":"PilP protein","ncbi_taxon_id":122586,"organism":"Neisseria meningitidis serogroup B (strain MC58)","regions_counter":4,"released":"2018_11","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"UniParc":"UPI00000C4E86","uniref100":"UniRef100_A0A0E1I940","uniref50":"UniRef50_E4ZF16","uniref90":"UniRef90_A0A7U8ZGF4","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2IVW","_id":"685af523b4ac24d5329d94d5"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":69,"end":84,"interaction_partner":[],"reference_html":"The solution structure of a domain from the Neisseria meningitidis lipoprotein PilP reveals a new beta-sandwich fold. <i> Golovanov AP, Balasingham S, Tzitzilonis C, Goult BT, Lian LY, Homberset H, Tønjum T, Derrick JP. </i> J Mol Biol, 2006","reference_id":"17007878","region_id":"DP02311r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Whereas MxiM requires the presence of a detergent ligand to form a folded structure, PilP has a folded domain, which requires no ligand for formation, but has significant portions of the structure in an unfolded state, particularly within the N terminus.","_id":"685af523b4ac24d5329d94d6"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-10-13T20:28:54.496Z","_id":"685af523b4ac24d5329d94d7"},"version":3,"_id":"685af523b4ac24d5329d94d4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":20,"end":69,"interaction_partner":[],"reference_html":"The solution structure of a domain from the Neisseria meningitidis lipoprotein PilP reveals a new beta-sandwich fold. <i> Golovanov AP, Balasingham S, Tzitzilonis C, Goult BT, Lian LY, Homberset H, Tønjum T, Derrick JP. </i> J Mol Biol, 2006","reference_id":"17007878","region_id":"DP02311r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Limited digestion with chymotrypsin was found to yield a stable fragment; peptide sequencing was used to identify the N terminus, which starts from Glu69, and mass spectrometry demonstrated that the C terminus of the protein was not cleaved (data not shown).","_id":"685af523b4ac24d5329d94d9"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-10-13T20:28:55.638Z","_id":"685af523b4ac24d5329d94da"},"version":3,"_id":"685af523b4ac24d5329d94d8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2IVW","_id":"685af523b4ac24d5329d94dc"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":164,"end":181,"interaction_partner":[],"reference_html":"The solution structure of a domain from the Neisseria meningitidis lipoprotein PilP reveals a new beta-sandwich fold. <i> Golovanov AP, Balasingham S, Tzitzilonis C, Goult BT, Lian LY, Homberset H, Tønjum T, Derrick JP. </i> J Mol Biol, 2006","reference_id":"17007878","region_id":"DP02311r003","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The C-terminus is unstructured even if it was not mentioned in the text.","_id":"685af523b4ac24d5329d94dd"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-10-13T20:28:57.311Z","_id":"685af523b4ac24d5329d94de"},"version":3,"_id":"685af523b4ac24d5329d94db","reference_source":"pmid"}],"__v":0,"disorder_content":0.4585635359116022,"disprot_consensus":{"full":[{"start":20,"end":84,"type":"D"},{"start":164,"end":181,"type":"D"}],"Structural state":[{"start":20,"end":84,"type":"D"},{"start":164,"end":181,"type":"D"}]}},{"features":{"pfam":[{"id":"PF10185","name":"Chaperone for wingless signalling and trafficking of LDL receptor","start":31,"end":178}],"gene3D":[{"start":32,"end":74,"id":"3.30.70.260","name":"3.30.70.260"},{"start":77,"end":173,"id":"3.30.70.260","name":"3.30.70.260"}]},"uniref50":"UniRef50_Q8T9B6","sequence":"MQTRLVLLLLALTPLVLAKKFKEEEKPAWAKKDIRDYSEADLERLLDQWEEDEEPLEDDELPEHLRPQPKLDLSNLDSKSPEDLLKVSKKGRTLMTFVSVTGNPTREESDTITKLWQTSLWNNHIQAERYMVDDNRAIFLFKDGTQAWDAKDFLIEQERCKGVTIENKEYPGVNAKKDEL","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_Q8T9B6","disprot_id":"DP02312","ncbi_taxon_id":7227,"regions_counter":2,"creator":"vpromp","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":91,"region_id":"DP02312r001","released":"2024_06","ec_id":"ECO:0007691","reference_html":"Structural characterization of the Boca/Mesd maturation factors for LDL-receptor-type β propeller domains. <i> Collins MN, Hendrickson WA. </i> Structure, 2011","statement":[{"text":"We used limited proteolysis to map the domain structure of the mature proteins from three family members: Mus musculus (mm) Mesd; Drosophila melanogaster (dm) Boca; and Caenorhabditis elegans (ce) BMY-1. Each of these proteins reveals a similar proteolytic profile (Figure S1). The variable sequences from the N- and C-termini of the mature protein are removed at low protease concentrations. At higher protease concentrations, the rapid removal of an additional ~50 residues from the N-terminus generates a ~10 kDa protease-resistant fragment.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":19,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-26T14:04:50.952Z","reference_source":"pmid","term_name":"disorder","reference_id":"21397184","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":91,"region_id":"DP02312r002","released":"2024_06","ec_id":"ECO:0006165","reference_html":"Structural characterization of the Boca/Mesd maturation factors for LDL-receptor-type β propeller domains. <i> Collins MN, Hendrickson WA. </i> Structure, 2011","statement":[{"text":"Nearly all the dispersed peaks within the CC spectra overlap with those of the SD spectra, implying that SD includes all of the well structured regions of the CC. The extra ~50 residues in the N-terminal region of dmBocaCC have resonance frequencies corresponding to those of an unstructured peptide, typified by limited dispersion centered at 1H resonance frequencies of ~8.2 ppm.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":31,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-26T14:07:12.170Z","reference_source":"pmid","term_name":"disorder","reference_id":"21397184","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q8T9B6","date":"2018-08-31T20:33:24.000Z","acc":"Q8T9B6","name":"LDLR chaperone boca","length":180,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI000005E9F2","genes":[{"name":{"value":"boca"},"orfNames":[{"value":"CG30498"}]}],"alphafold_very_low_content":0.03333333333333333,"disorder_content":0.40555555555555556,"disprot_consensus":{"full":[{"start":19,"end":91,"type":"D"}],"Structural state":[{"start":19,"end":91,"type":"D"}]}},{"features":{"pfam":[{"id":"PF10185","name":"Chaperone for wingless signalling and trafficking of LDL receptor","start":24,"end":178}],"gene3D":[{"start":81,"end":174,"id":"3.30.70.260","name":"3.30.70.260"}]},"uniref50":"UniRef50_Q8IG33","sequence":"MKWRTVFIFLLAAHIGLANVKQKKKDLSSYTDAELEKLYEEWEENDEDELEEDEKPEHKRKPPQLDLESMKAKAKDPEDLLMMSKKGQTLMLFVGVVDPSQPDRSDIRPFTEKWTQIWQSQLYNNHVDLQVFVIDDNRAIFMFKNGEQAFEAKKFLLKQEFVSEVTIEGQSFDGPAKKFKTGKKEL","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"uniref90":"UniRef90_Q8IG33","disprot_id":"DP02313","ncbi_taxon_id":6239,"regions_counter":1,"creator":"vpromp","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":88,"region_id":"DP02313r001","released":"2024_06","ec_id":"ECO:0007691","reference_html":"Structural characterization of the Boca/Mesd maturation factors for LDL-receptor-type β propeller domains. <i> Collins MN, Hendrickson WA. </i> Structure, 2011","statement":[{"text":"We used limited proteolysis to map the domain structure of the mature proteins from three family members: Mus musculus (mm) Mesd; Drosophila melanogaster (dm) Boca; and Caenorhabditis elegans (ce) BMY-1. Each of these proteins reveals a similar proteolytic profile (Figure S1). The variable sequences from the N- and C-termini of the mature protein are removed at low protease concentrations. At higher protease concentrations, the rapid removal of an additional ~50 residues from the N-terminus generates a ~10 kDa protease-resistant fragment.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":18,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-26T14:05:15.823Z","reference_source":"pmid","term_name":"disorder","reference_id":"21397184","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q8IG33","date":"2018-08-31T20:41:48.000Z","acc":"Q8IG33","name":"Boca/MESD chaperone for YWTD beta-propeller-EGF","length":186,"organism":"Caenorhabditis elegans","dataset":[],"UniParc":"UPI00000851E4","genes":[{"name":{"value":"bmy-1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CCD68769.1","url":"https://www.ebi.ac.uk/ena/browser/view/CCD68769.1"}},{"code":"ECO:0000313","source":{"name":"WormBase","id":"F09E5.17","url":"https://www.wormbase.org/db/seq/sequence?name=F09E5.17;class=Transcript"}}]},"orfNames":[{"value":"CELE_F09E5.17","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CCD68769.1","url":"https://www.ebi.ac.uk/ena/browser/view/CCD68769.1"}}]},{"value":"F09E5.17","evidences":[{"code":"ECO:0000313","source":{"name":"WormBase","id":"F09E5.17","url":"https://www.wormbase.org/db/seq/sequence?name=F09E5.17;class=Transcript"}}]}]}],"alphafold_very_low_content":0.03225806451612903,"disorder_content":0.3817204301075269,"disprot_consensus":{"full":[{"start":18,"end":88,"type":"D"}],"Structural state":[{"start":18,"end":88,"type":"D"}]}},{"features":{"pfam":[{"id":"PF10185","name":"Chaperone for wingless signalling and trafficking of LDL receptor","start":43,"end":194}],"gene3D":[{"start":44,"end":73,"id":"3.30.70.260","name":"3.30.70.260"},{"start":88,"end":184,"id":"3.30.70.260","name":"3.30.70.260"}]},"uniref50":"UniRef50_Q9ERE7","sequence":"MAASRWLRAVLLFLCASDLLLLPPPNAYAADTPGEATPPPRKKKDIRDYNDADMARLLEQWEKDDDIEEGDLPEHKRPSAPIDFSKLDPGKPESILKMTKKGKTLMMFVTVSGNPTEKETEEITSLWQGSLFNANYDVQRFIVGSDRAIFMLRDGSYAWEIKDFLVSQDRCAEVTLEGQMYPGKGGGSKEKNKTKPEKAKKKEGDPKPRASKEDNRAGSRREDL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q9ERE7","disprot_id":"DP02314","ncbi_taxon_id":10090,"regions_counter":2,"creator":"vpromp","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":102,"region_id":"DP02314r001","released":"2024_06","ec_id":"ECO:0007691","reference_html":"Structural characterization of the Boca/Mesd maturation factors for LDL-receptor-type β propeller domains. <i> Collins MN, Hendrickson WA. </i> Structure, 2011","statement":[{"text":"We used limited proteolysis to map the domain structure of the mature proteins from three family members: Mus musculus (mm) Mesd; Drosophila melanogaster (dm) Boca; and Caenorhabditis elegans (ce) BMY-1. Each of these proteins reveals a similar proteolytic profile (Figure S1). The variable sequences from the N- and C-termini of the mature protein are removed at low protease concentrations. At higher protease concentrations, the rapid removal of an additional ~50 residues from the N-terminus generates a ~10 kDa protease-resistant fragment.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":30,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cleavage assay evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-02-26T14:05:24.539Z","reference_source":"pmid","term_name":"disorder","reference_id":"21397184","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":92,"region_id":"DP02314r002","released":"2022_03","ec_id":"ECO:0007691","reference_html":"Requirement for natively unstructured regions of mesoderm development candidate 2 in promoting low-density lipoprotein receptor-related protein 6 maturation. <i> Koduri V, Blacklow SC. </i> Biochemistry, 2007","statement":[{"text":"The majority of potential trypsin and V8 protease cleavage sites are highly protected within a core region spanning residues 64-150, indicating that this part of the protein represents a core, folded domain.\n\nNote: residue numbers correspond to the mature form of the protein and have been amended in this entry.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vpromp","start":29,"term_ontology":"IDPO","curator_name":"Vasilis J Promponas","ec_name":"cleavage assay evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-3352-4831","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"17488095","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q9ERE7","date":"2018-08-31T20:46:59.000Z","acc":"Q9ERE7","name":"LRP chaperone MESD","length":224,"organism":"Mus musculus","dataset":[],"UniParc":"UPI000000410C","genes":[{"name":{"value":"Mesd","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:1891421","url":"http://www.informatics.jax.org/marker/MGI:1891421"}}]},"synonyms":[{"value":"Mesdc2"}]}],"alphafold_very_low_content":0.23214285714285715,"disorder_content":0.33035714285714285,"disprot_consensus":{"full":[{"start":29,"end":102,"type":"D"}],"Structural state":[{"start":29,"end":102,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03999","name":"Microtubule associated protein (MAP65/ASE1 family)","start":16,"end":476}],"gene3D":[{"start":338,"end":466,"id":"1.20.58.1520","name":"1.20.58.1520"}]},"uniref50":"UniRef50_O43663","sequence":"MRRSEVLAEESIVCLQKALNHLREIWELIGIPEDQRLQRTEVVKKHIKELLDMMIAEEESLKERLIKSISVCQKELNTLCSELHVEPFQEEGETTILQLEKDLRTQVELMRKQKKERKQELKLLQEQDQELCEILCMPHYDIDSASVPSLEELNQFRQHVTTLRETKASRREEFVSIKRQIILCMEALDHTPDTSFERDVVCEDEDAFCLSLENIATLQKLLRQLEMQKSQNEAVCEGLRTQIRELWDRLQIPEEEREAVATIMSGSKAKVRKALQLEVDRLEELKMQNMKKVIEAIRVELVQYWDQCFYSQEQRQAFAPFCAEDYTESLLQLHDAEIVRLKNYYEVHKELFEGVQKWEETWRLFLEFERKASDPNRFTNRGGNLLKEEKQRAKLQKMLPKLEEELKARIELWEQEHSKAFMVNGQKFMEYVAEQWEMHRLEKERAKQERQLKNKKQTETEMLYGSAPRTPSKRRGLAPNTPGKARKLNTTTMSNATANSSIRPIFGGTVYHSPVSRLPPSGSKPVAASTCSGKKTPRTGRHGANKENLELNGSILSGGYPGSAPLQRNFSINSVASTYSEFAKDPSLSDSSTVGLQRELSKASKSDATSGILNSTNIQS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O43663","disprot_id":"DP02316","ncbi_taxon_id":9606,"regions_counter":3,"creator":"vpromp","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":620,"region_id":"DP02316r001","released":"2023_12","ec_id":"ECO:0006220","reference_html":"Insights into antiparallel microtubule crosslinking by PRC1, a conserved nonmotor microtubule binding protein. <i> Subramanian R, Wilson-Kubalek EM, Arthur CP, Bick MJ, Campbell EA, Darst SA, Milligan RA, Kapoor TM. </i> Cell, 2010","term_id":"IDPO:0000002","curator_id":"vpromp","start":467,"term_ontology":"IDPO","curator_name":"Vasilis J Promponas","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0003-3352-4831","date":"2023-12-13T13:30:58.851Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"3NRY"}],"reference_id":"20691902","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"As we do not observe any additional density past the C terminus of the spectrin domain that is close to the microtubule lattice, we favor the possibility that the Lys/Arg-rich domain is disordered even when PRC1 is bound to a microtubule.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-13T14:45:53.117Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":620,"term_name":"protein binding","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Insights into antiparallel microtubule crosslinking by PRC1, a conserved nonmotor microtubule binding protein. <i> Subramanian R, Wilson-Kubalek EM, Arthur CP, Bick MJ, Campbell EA, Darst SA, Milligan RA, Kapoor TM. </i> Cell, 2010","statement":[{"text":"We were unable to detect microtubule associations of single molecules of GFP-PRC1-NS at the concentrations needed to resolve single molecules using TIRF microscopy (<10 nM; data not shown), suggesting that residues in the C terminus domain contribute to microtubule binding","type":"Results"}],"term_id":"GO:0005515","curator_id":"vpromp","start":467,"term_ontology":"GO","curator_name":"Vasilis J Promponas","reference_id":"20691902","version":4,"curator_orcid":"0000-0003-3352-4831","date":"2023-12-13T14:18:33.222Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02316r002","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"3NRX"},{"db":"PDB","id":"3NRY"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-13T14:45:57.205Z"}},{"region_id":"DP02316r003","ec_ontology":"ECO","end":486,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":451,"version":3,"statement":[{"text":"The main chain atoms of most of the N-terminal 486 residues in PRC1-NSΔC could be assigned, except the C-terminal 36 residues that were disordered in the crystal and not included in the final model.","type":"Results"}],"term_name":"disorder","reference_html":"Marking and measuring single microtubules by PRC1 and kinesin-4. <i> Subramanian R, Ti SC, Tan L, Darst SA, Kapoor TM. </i> Cell, 2013","released":"2023_12","term_ontology":"IDPO","curator_name":"Vasilis J Promponas","reference_id":"23870126","date":"2023-12-13T13:33:31.716Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4L3I"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vpromp","curator_orcid":"0000-0003-3352-4831","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-13T14:45:54.305Z"}}],"released":"2018_11","uniref100":"UniRef100_O43663","date":"2018-08-31T23:03:05.000Z","acc":"O43663","name":"Protein regulator of cytokinesis 1","length":620,"organism":"Homo sapiens","dataset":["Cancer-related proteins","Condensates-related proteins"],"UniParc":"UPI00001A5ED8","genes":[{"name":{"value":"PRC1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9341","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9341"}}]}}],"alphafold_very_low_content":0.22903225806451613,"disorder_content":0.27419354838709675,"disprot_consensus":{"full":[{"start":451,"end":620,"type":"D"}],"Structural state":[{"start":451,"end":620,"type":"D"}],"Molecular function":[{"start":467,"end":620,"type":"F"}]}},{"features":{"pfam":[{"id":"PF11558","name":"Het-s 218-289","start":218,"end":282},{"id":"PF14479","name":"Prion-inhibition and propagation","start":6,"end":199}],"gene3D":[{"start":2,"end":221,"id":"1.20.120.1020","name":"Prion-inhibition and propagation, HeLo domain"}]},"uniref50":"UniRef50_Q03689","sequence":"MSEPFGIVAGALNVAGLFNNCVDCFEYVQLGRPFGRDYERCQLRLDIAKARLSRWGEAVKINDDPRFHSDAPTDKSVQLAKSIVEEILLLFESAQKTSKRYELVADQQDLVVFEDKDMKPIGRALHRRLNDLVSRRQKQTSLAKKTAWALYDGKSLEKIVDQVARFVDELEKAFPIEAVCHKLAEIEIEEVEDEASLTILKDAAGGIDAAMSDAAAQKIDAIVGRNSAKDIRTEERARVQLGNVVTAAALHGGIRISDQTTNSVETVVGKGESRVLIGNEYGGKGFWDN","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Sordariomycetidae","Sordariales","Chaetomiaceae","Podospora"],"uniref90":"UniRef90_Q03689","disprot_id":"DP02317","ncbi_taxon_id":5145,"regions_counter":1,"creator":"vpromp","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":289,"region_id":"DP02317r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"The mechanism of prion inhibition by HET-S. <i> Greenwald J, Buhtz C, Ritter C, Kwiatkowski W, Choe S, Maddelein ML, Ness F, Cescau S, Soragni A, Leitz D, Saupe SJ, Riek R. </i> Mol Cell, 2010","statement":[{"text":"[..] the per-residue chemical shift deviation of HET-S shows that it is composed of an N-terminal mostly helical structured domain comprising at least residues 13–222 followed by an unstructured and flexible C-terminal tail.\nNote: Evidence also found in Supplementary Figures S2b and S3.\n\nNote: In constructs roughly corresponding to this region (e.g. PDB:2RNM; Pubmed: 18339938) it forms a left-handed beta solenoid.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vpromp","start":228,"term_ontology":"IDPO","curator_name":"Vasilis J Promponas","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-3352-4831","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"20620958","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q03689","date":"2018-09-01T00:24:39.000Z","acc":"Q03689","name":"Heterokaryon incompatibility protein s","length":289,"organism":"Podospora anserina","dataset":[],"UniParc":"UPI0000168953","genes":[{"name":{"value":"het-s"},"synonyms":[{"value":"small s"}]}],"alphafold_very_low_content":0.01384083044982699,"disorder_content":0.21453287197231835,"disprot_consensus":{"full":[{"start":228,"end":289,"type":"D"}],"Structural state":[{"start":228,"end":289,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00200","name":"Disintegrin","start":466,"end":545},{"id":"PF13574","name":"Metallo-peptidase family M12B Reprolysin-like","start":243,"end":445},{"id":"PF21299","name":"ADAM10, cysteine-rich domain","start":591,"end":646}],"gene3D":[{"start":216,"end":455,"id":"3.40.390.10","name":"Collagenase (Catalytic Domain)"},{"start":456,"end":547,"id":"4.10.70.10","name":"Disintegrin domain"}]},"uniref50":"UniRef50_O14672","sequence":"MVLLRVLILLLSWAAGMGGQYGNPLNKYIRHYEGLSYNVDSLHQKHQRAKRAVSHEDQFLRLDFHAHGRHFNLRMKRDTSLFSDEFKVETSNKVLDYDTSHIYTGHIYGEEGSFSHGSVIDGRFEGFIQTRGGTFYVEPAERYIKDRTLPFHSVIYHEDDINYPHKYGPQGGCADHSVFERMRKYQMTGVEEVTQIPQEEHAANGPELLRKKRTTSAEKNTCQLYIQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTDFSGIRNISFMVKRIRINTTADEKDPTNPFRFPNIGVEKFLELNSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPSGSSGGICEKSKLYSDGKKKSLNTGIITVQNYGSHVPPKVSHITFAHEVGHNFGSPHDSGTECTPGESKNLGQKENGNYIMYARATSGDKLNNNKFSLCSIRNISQVLEKKRNNCFVESGQPICGNGMVEQGEECDCGYSDQCKDECCFDANQPEGRKCKLKPGKQCSPSQGPCCTAQCAFKSKSEKCRDDSDCAREGICNGFTALCPASDPKPNFTDCNRHTQVCINGQCAGSICEKYGLEECTCASSDGKDDKELCHVCCMKKMDPSTCASTGSVQWSRHFSGRTITLQPGSPCNDFRGYCDVFMRCRLVDADGPLARLKKAIFSPELYENIAEWIVAHWWAVLLMGIALIMLMAGFIKICSVHTPSSNPKLPPPKPLPGTLKRRRPPQPIQQPQRQRPRESYQMGHMRR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O14672","disprot_id":"DP02318","ncbi_taxon_id":9606,"regions_counter":7,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":748,"region_id":"DP02318r001","released":"2024_06","ec_id":"ECO:0006204","reference_html":"Membrane-enabled dimerization of the intrinsically disordered cytoplasmic domain of ADAM10. <i> Deng W, Cho S, Su PC, Berger BW, Li R. </i> Proc Natl Acad Sci U S A, 2014","statement":[{"text":"Consistent with the assessment by SPINE-D, recombinant cytoplasmic domain of human ADAM10 (A10Cp-6H, containing residues Lys697–Arg748 and a C-terminal hexahistidine tag) in the dodecylphosphocholine (DPC) micellar solution (10 mM DPC, 20 mM Tris·HCl, 100 mM NaCl, and 1 mM DTT, pH 8.0) contained little stable secondary structure as indicated by its circular dichroism (CD) spectrum (Fig. 2A and Fig. S1).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":697,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-01-30T14:59:38.155Z","reference_source":"pmid","term_name":"disorder","reference_id":"25349418","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"78018","entry_name":"dodecylphosphocholine"}],"sequence_construct":"GSGGGKICSVHTPSSNPKLPPPKPLPGTLKRRRPPQPIQQPPRQRPRESYQMGHMRRHHHHHH"},{"start":697,"end":748,"reference_id":"25349418","reference_source":"pmid","reference_html":"Membrane-enabled dimerization of the intrinsically disordered cytoplasmic domain of ADAM10. <i> Deng W, Cho S, Su PC, Berger BW, Li R. </i> Proc Natl Acad Sci U S A, 2014","date":"2024-01-30T15:01:31.788Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"region_id":"DP02318r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"78018","entry_name":"dodecylphosphocholine"}],"sequence_construct":"GSGGGLYENIAEWIVAHWWAVLLMGIALIMLMAGFIKICSVHTPSSNPKLPPPKPLPGTLKRRRPPQPIQ QPPRQRPRESYQMGHMRRHHHHHH","statement":[{"text":"However, recombinant transmembrane-cytoplasmic domains of human ADAM10 (A10TmCp-6H, containing residues Leu666–Arg748 and a C-terminal hexahistidine tag) reconstituted in the same DPC micelles contained significant amount of α-helical structure (Fig. 2A and Fig. S1). Deconvolution of its CD spectrum (α helix: 87%, β strand: 1%, coil: 12%) suggested that most residues in A10TmCp-6H adopt the α-helical conformation (19). Because the transmembrane domain constitutes only 30% of the residues in A10TmCp-6H, significant amount of helical structure should be present in the cytoplasmic domain.","type":"Results"}]},{"start":697,"end":748,"reference_id":"25349418","reference_source":"pmid","reference_html":"Membrane-enabled dimerization of the intrinsically disordered cytoplasmic domain of ADAM10. <i> Deng W, Cho S, Su PC, Berger BW, Li R. </i> Proc Natl Acad Sci U S A, 2014","date":"2024-01-30T15:04:20.627Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"region_id":"DP02318r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"78018","entry_name":"dodecylphosphocholine"}],"sequence_construct":"GSGGGLYENIAEWIVAHWWAVLLMGIALIMLMAGFIKICSVHTPSSNPKLPPPKPLPGTLKRRRPPQPIQ QPPRQRPRESYQMGHMRRHHHHHH","statement":[{"text":"Consistent with the assessment by SPINE-D, recombinant cytoplasmic domain of human ADAM10 (A10Cp-6H, containing residues Lys697–Arg748 and a C-terminal hexahistidine tag) in the dodecylphosphocholine (DPC) micellar solution (10 mM DPC, 20 mM Tris·HCl, 100 mM NaCl, and 1 mM DTT, pH 8.0) contained little stable secondary structure as indicated by its circular dichroism (CD) spectrum (Fig. 2A and Fig. S1).","type":"Results"},{"text":"However, recombinant transmembrane-cytoplasmic domains of human ADAM10 (A10TmCp-6H, containing residues Leu666–Arg748 and a C-terminal hexahistidine tag) reconstituted in the same DPC micelles contained significant amount of α-helical structure (Fig. 2A and Fig. S1). Deconvolution of its CD spectrum (α helix: 87%, β strand: 1%, coil: 12%) suggested that most residues in A10TmCp-6H adopt the α-helical conformation (19). Because the transmembrane domain constitutes only 30% of the residues in A10TmCp-6H, significant amount of helical structure should be present in the cytoplasmic domain.","type":"Results"},{"text":"In other words, the cytoplasmic domain of ADAM10 is intrinsically disordered, but in the presence of its neighboring transmembrane domain, it takes on an ordered conformation.","type":"Results"}],"states_connection":[{"source":"DP02318r001","target":"DP02318r004"}]},{"start":697,"end":748,"reference_id":"25349418","reference_source":"pmid","reference_html":"Membrane-enabled dimerization of the intrinsically disordered cytoplasmic domain of ADAM10. <i> Deng W, Cho S, Su PC, Berger BW, Li R. </i> Proc Natl Acad Sci U S A, 2014","date":"2024-01-30T15:09:37.957Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"O14672","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02318r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"78018","entry_name":"dodecylphosphocholine"}],"sequence_construct":"GSGGGLYENIAEWIVAHWWAVLLMGIALIMLMAGFIKICSVHTPSSNPKLPPPKPLPGTLKRRRPPQPIQ QPPRQRPRESYQMGHMRRHHHHHH","statement":[{"text":"These results indicate that A10TmCp-6H, but not A10Cp-6H, forms homo-oligomers in DPC micelles. It is noteworthy that the protein/detergent molar ratio in this experiment was 1/50,000 (200 nM protein/10 mM DPC). It is much lower than 1/200–1/1,000, a range typically used in the studies of homo-association of transmembrane helical peptides (23–26), suggesting that homo-association of A10TmCp-6H is not mediated by its transmembrane domain.","type":"Results"},{"text":"Overall, these results indicate that the dimerization of A10TmCp is mediated by its cytoplasmic domain.","type":"Results"},{"text":"What is unique and intriguing about our finding is that dimerization of the cytoplasmic domain of ADAM10 requires attachment to a transmembrane domain, yet the attached transmembrane domain does not directly mediate dimerization.","type":"Discussion"}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":697,"end":748,"reference_id":"25349418","reference_source":"pmid","reference_html":"Membrane-enabled dimerization of the intrinsically disordered cytoplasmic domain of ADAM10. <i> Deng W, Cho S, Su PC, Berger BW, Li R. </i> Proc Natl Acad Sci U S A, 2014","date":"2024-01-30T15:28:11.646Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005636","ec_ontology":"ECO","ec_name":"green fluorescent protein reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":" The MBP-TmCp-AraC constructs containing the ADAM10 transmembrane domain (a10Tm), the ADAM10 transmembrane and cytoplasmic domains (a10TmCp), the l-selectin transmembrane and cytoplasmic domains (lselTmCp), and a chimeric l-selectin transmembrane and ADAM10 cytoplasmic domains (lselTm-a10Cp) were transformed into the AraC-deficient E. coli strain SB1676 (Fig. 5A)."}]},{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Results","text":" The MBP-TmCp-AraC constructs containing the ADAM10 transmembrane domain (a10Tm), the ADAM10 transmembrane and cytoplasmic domains (a10TmCp), the l-selectin transmembrane and cytoplasmic domains (lselTmCp), and a chimeric l-selectin transmembrane and ADAM10 cytoplasmic domains (lselTm-a10Cp) were transformed into the AraC-deficient E. coli strain SB1676 (Fig. 5A)."}]}],"ec_go":"IEP","interaction_partner":[{"db":"UniProt","id":"O14672","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02318r007","statement":[{"text":"Comparison of the GFP fluorescence intensities indicated that, although MBP-a10Tm-AraC exhibited little dimerization in the membrane, MBP-a10TmCp-AraC dimerized as strongly as the positive control (Fig. 5C and Fig. S7).","type":"Results"},{"text":"Consistent with recent reports that the transmembrane and cytoplasmic domains of l-selectin or full-length l-selectin are monomeric in membrane conditions (30, 31), expression of MBP-lselTmCp-AraC induced little GFP fluorescence in the AraTM assay (Fig. 5C). In comparison, expression of MBP-lselTm-a10Cp-AraC produced as strong a GFP fluorescence as the positive control or MBP-A10TmCp-AraC. These results indicate that the cytoplasmic domain of ADAM10, when placed next to an unrelated transmembrane domain, can mediate strong dimerization of the host protein.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2018_11","uniref100":"UniRef100_O14672","date":"2018-09-01T00:25:57.000Z","acc":"O14672","name":"Disintegrin and metalloproteinase domain-containing protein 10","length":748,"organism":"Homo sapiens","dataset":["Extracellular matrix proteins"],"UniParc":"UPI00001254C8","genes":[{"name":{"value":"ADAM10"},"synonyms":[{"value":"KUZ"},{"value":"MADM"}]}],"alphafold_very_low_content":0.09893048128342247,"disorder_content":0.06951871657754011,"disprot_consensus":{"full":[{"start":697,"end":748,"type":"T"}],"Structural state":[{"start":697,"end":748,"type":"D"}],"Structural transition":[{"start":697,"end":748,"type":"T"}],"Molecular function":[{"start":697,"end":748,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_P0C8E0","sequence":"GEDEYAEGIREYQLIHGKI","taxonomy":["Eukaryota","Metazoa","Spiralia","Lophotrochozoa","Mollusca","Gastropoda","Caenogastropoda","Neogastropoda","Conoidea","Conidae","Conus","Phasmoconus"],"uniref90":"UniRef90_P0C8E0","disprot_id":"DP02320","dataset":[],"ncbi_taxon_id":505247,"regions_counter":1,"creator":"vpromp","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":19,"region_id":"DP02320r001","start":1,"ec_id":"ECO:0006204","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Conantokins-Pr1 and -Pr2 adopt alpha-helical conformations in the presence of divalent cations (Mg2+ and Ca2+) but are generally unstructured in the absence of divalent cations.","type":"Abstract"},{"text":"Because con-Pr1, -Pr2, and -Pr3 all shared common characteristics of conantokins, we hypothesized that they would be structurally related to con-G, which adopts an α-helical conformation in solution in the presence of divalent cations. However, it is nearly structureless in the absence of divalent cations (22). To estimate the α-helical content of the C. parius conantokins, circular dichroism spectroscopy was employed. The α-helical content of con-Pr1 and -Pr2 was estimated to be much greater in the presence of Mg2+ or Ca2+ than in the absence of divalent cations, like con-G (Fig. 3).","type":"Results"},{"text":"con-Pr1 is unstructured in the absence of divalent cations, i.e. Mg2+ and Ca2+.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17962189","version":3,"reference_html":"Novel conantokins from Conus parius venom are specific antagonists of N-methyl-D-aspartate receptors. <i> Teichert RW, Jimenez EC, Twede V, Watkins M, Hollmann M, Bulaj G, Olivera BM. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P0C8E0","date":"2018-09-01T01:05:40.000Z","acc":"P0C8E0","name":"Conantokin-Pr1","length":19,"organism":"Conus parius","UniParc":"UPI00017B8D56","genes":[],"alphafold_very_low_content":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":19,"type":"D"}],"Structural state":[{"start":1,"end":19,"type":"D"}]}},{"features":{"pfam":[]},"uniref50":"UniRef50_P0C8E1","sequence":"DEPEYAEAIREYQLKYGKI","taxonomy":["Eukaryota","Metazoa","Spiralia","Lophotrochozoa","Mollusca","Gastropoda","Caenogastropoda","Neogastropoda","Conoidea","Conidae","Conus","Phasmoconus"],"uniref90":"UniRef90_P0C8E1","disprot_id":"DP02321","dataset":[],"ncbi_taxon_id":505247,"regions_counter":1,"creator":"vpromp","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":19,"region_id":"DP02321r001","start":1,"ec_id":"ECO:0006204","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Conantokins-Pr1 and -Pr2 adopt alpha-helical conformations in the presence of divalent cations (Mg2+ and Ca2+) but are generally unstructured in the absence of divalent cations.","type":"Abstract"},{"text":"Because con-Pr1, -Pr2, and -Pr3 all shared common characteristics of conantokins, we hypothesized that they would be structurally related to con-G, which adopts an α-helical conformation in solution in the presence of divalent cations. However, it is nearly structureless in the absence of divalent cations (22). To estimate the α-helical content of the C. parius conantokins, circular dichroism spectroscopy was employed. The α-helical content of con-Pr1 and -Pr2 was estimated to be much greater in the presence of Mg2+ or Ca2+ than in the absence of divalent cations, like con-G (Fig. 3).","type":"Results"},{"text":"con-Pr2 is unstructured in the absence of divalent cations, i.e. Mg2+ and Ca2+.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17962189","version":3,"reference_html":"Novel conantokins from Conus parius venom are specific antagonists of N-methyl-D-aspartate receptors. <i> Teichert RW, Jimenez EC, Twede V, Watkins M, Hollmann M, Bulaj G, Olivera BM. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P0C8E1","date":"2018-09-01T01:13:52.000Z","acc":"P0C8E1","name":"Conantokin-Pr2","length":19,"organism":"Conus parius","UniParc":"UPI00017B8D57","genes":[],"alphafold_very_low_content":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":19,"type":"D"}],"Structural state":[{"start":1,"end":19,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03136","name":"Pup-ligase protein","start":3,"end":456}]},"uniref50":"UniRef50_A0LU48","sequence":"MHRVMGIETEYGISVPHQPNANAMAASSQVVNAYAPIGAPAQRQARWDFEEENPLRDARGFEVAREAADPSQLTDEDLGLANVILTNGARLYVDHAHPEYSTPEVTNPRDAVLWDKAGERIMAEAARRAADLPMGWTIQLYKNNTDNKGASYGCHENYLMNRSTPFADIVRHLIPFFVTRQVFCGAGRVGIGADGRGEGFQLSQRADFFEVEVGLETTLKRPIINTRDEPHADPEKYRRLHVIIGDANMSEIATYLKLGTTALVLAMIEDGFLSQDFSVESPVGALRAVSHDPTLRYQLRLHDGRRLTAVQLQMEYLEQARKYVEDRFGTDVDDMTRDVLDRWETTLVRLADDPMQLSRDLDWVAKLSILEGYRQRENLPWSAHKLQLVDLQYHDVRPDRGLYNRLVARGRMNLLVDEAAVRTAMHEPPNDTRAYFRGRCLAKFGAEIAAASWDSVIFDLPGRDSLQRVPTLEPLRGTRAHVGDLLDRCRSATELVAALTGGR","taxonomy":["Bacteria","Actinobacteria","Acidothermales","Acidothermaceae","Acidothermus"],"uniref90":"UniRef90_A0LU48","disprot_id":"DP02322","ncbi_taxon_id":351607,"regions_counter":1,"creator":"vpromp","regions":[{"region_id":"DP02322r001","ec_ontology":"ECO","end":80,"ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","start":36,"version":3,"statement":[{"text":"The final electron density map showed continuous density except for a disordered region between residues 36 to 80.","type":"Results"},{"text":"Although it is disordered in our structure, this region could become more ordered in the presence of substrates or could play a role in the interaction with other potential binding partners.","type":"Discussion"}],"term_name":"disorder","reference_html":"Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification pathway. <i> Özcelik D, Barandun J, Schmitz N, Sutter M, Guth E, Damberger FF, Allain FH, Ban N, Weber-Ban E. </i> Nat Commun, 2012","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"22910360","date":"2024-02-26T14:25:06.502Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4B0R"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_A0LU48","date":"2018-09-01T01:46:18.000Z","acc":"A0LU48","name":"Depupylase","length":503,"organism":"Acidothermus cellulolyticus (strain ATCC 43068 / 11B)","dataset":[],"UniParc":"UPI00006BF0FF","genes":[{"name":{"value":"dop"},"olnNames":[{"value":"Acel_1186"}]}],"alphafold_very_low_content":0.009940357852882704,"disorder_content":0.08946322067594434,"disprot_consensus":{"full":[{"start":36,"end":80,"type":"D"}],"Structural state":[{"start":36,"end":80,"type":"D"}]}},{"features":{"pfam":[{"id":"PF03799","name":"Cell division protein FtsQ/DivIB, C-terminal","start":122,"end":235},{"id":"PF08478","name":"POTRA domain, FtsQ-type","start":52,"end":117}],"gene3D":[{"start":51,"end":116,"id":"3.10.20.310","name":"membrane protein fhac"},{"start":117,"end":233,"id":"3.40.50.10960","name":"3.40.50.10960"}]},"uniref50":"UniRef50_Q5L0X5","sequence":"MEKGKVVVLEDRVPKLKERRRQKANRRLIAYLSFFFLFILCVLYFQSPLGAVGHVEVSGNRHLTAERIISLSGITKRTSFWKVNEQNVEKKLTRHPEIKEATVEKQLPNTIAIHVREWRRIAYVYDRQTFFPLLENGRLLKQEGTKTAPSDAPVLVGWKDGDAIAEMTGQLAELPAAVLGAMSEIHYKPTREYEDRVIVYMNDGYEVSATIRQFADKLSHYPAIAAALDRNVKGVIHLEVGSYFVPYSPPKKEDGDETTSP","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Geobacillus","Geobacillus thermoleovorans group"],"uniref90":"UniRef90_Q5L0X5","disprot_id":"DP02323","ncbi_taxon_id":235909,"regions_counter":2,"creator":"vpromp","regions":[{"start":231,"end":261,"reference_id":"16618922","reference_source":"pmid","reference_html":"Domain architecture and structure of the bacterial cell division protein DivIB. <i> Robson SA, King GF. </i> Proc Natl Acad Sci U S A, 2006","date":"2024-02-26T14:32:08.567Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02323r002","statement":[{"text":"Fig. 2B shows the fragments obtained when Gste-ecDivIB was proteolyzed with trypsin for 3 h by using a DivIB:protease ratio of 100:1 at ambient temperature (fragment 1, Fig. 2B Left) or by using a DivIB:protease ratio of 200:1 at 37°C (fragment 2, Fig. 2B Right). Five cycles of N-terminal sequencing indicated that fragment 1 had an intact N terminus (i.e., G47SPLG), whereas the N terminus of fragment 2 (E117WRRI) corresponded to a trypsin cleavage after Arg-116 (Fig. 2C). Mass spectrometry indicated that the C terminus of both fragments was Arg-230.","type":"Results"}]}],"released":"2018_11","uniref100":"UniRef100_Q5L0X5","date":"2018-09-01T03:00:05.000Z","acc":"Q5L0X5","name":"Cell division protein DivIB","length":261,"organism":"Geobacillus kaustophilus (strain HTA426)","dataset":[],"UniParc":"UPI0000496D3B","genes":[{"name":{"value":"divIB","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00912","url":"https://hamap.expasy.org/unirule/MF_00912"}}]},"olnNames":[{"value":"GK1120"}]}],"alphafold_very_low_content":0.0421455938697318,"disorder_content":0.11877394636015326,"disprot_consensus":{"full":[{"start":231,"end":261,"type":"D"}],"Structural state":[{"start":231,"end":261,"type":"D"}]}},{"features":{"pfam":[{"id":"PF11778","name":"Septation initiation","start":444,"end":575}],"gene3D":[{"start":383,"end":581,"id":"1.20.5.400","name":"1.20.5.400"}]},"uniref50":"UniRef50_P53865","sequence":"MTDFDLMNFPFHERLDSPVSENGEIKDGEPIPQNWLNENHVGKSILPLFVNPEDVINCNFSNARDSYEENKSPSMDQMNYARNTSYQESPGLQERPKNEKDKSPIGTDVHKKDVPNFIHSTPRENSSKHFTRANEQASAQPTDEHTSPDISIEDCNGAKIFLQNSLSKEDFRMLENVILGYQKKVIELGRDNLRQEERANSLQKELEAATKSNDKTLDNKKKIEEQTVLIENLTKDLSLNKEMLEKANDTIQTKHTALLSLTDSLRKAELFEIPIGILFFDLYDSEENSSKLDHILQEKYPNIKGFLCASQQEELSRISQRFKNAKAEAEDLRNELENKKIEIQTMREKNNTLIGTNKTLSKQNKILCDKFDKLTIDEKEILKGCNEEIKIKLERLNERLGSWEKSKEKYETSLKDKEKMLADAEKKTNTLSKELDNLRSRFGNLEGNTSERITIKNILQSRPDISAEECNFLMVEQIDSANLTTLQNTVKEIVLAVGIPYPKLRRKIPLLAIKLKYENIMLSNFAQRLHRQVYSQEMNLKKFTDQAYYDFMSTRRMDSIDHHLERCLDHLYDHILEKMVK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P53865","disprot_id":"DP02324","ncbi_taxon_id":559292,"regions_counter":2,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":581,"region_id":"DP02324r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure-function analysis of the C-terminal domain of CNM67, a core component of the Saccharomyces cerevisiae spindle pole body. <i> Klenchin VA, Frye JJ, Jones MH, Winey M, Rayment I. </i> J Biol Chem, 2011","statement":[{"text":"the electron density for the C-terminal residues of Cnm67 (residues His-574—Lys-581) is largely missing. Lys-581 is the C-terminal residue in Cnm67. [Note: they are afterwards demonstrated as disordered residues]","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ahatos","start":572,"term_ontology":"IDPO","curator_name":"András Hatos","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"21454609","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":581,"term_name":"flexible C-terminal tail","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure-function analysis of the C-terminal domain of CNM67, a core component of the Saccharomyces cerevisiae spindle pole body. <i> Klenchin VA, Frye JJ, Jones MH, Winey M, Rayment I. </i> J Biol Chem, 2011","statement":[{"text":"Collectively, the experimental evidence suggests that without its hydrophobic terminus, the seemingly very tight Cnm67 globular dimer (with >4000 Å2 buried!) unfolds and aggregates. The likeliest explanation for this is that the C-terminal residues function as a cover or clamp for a large hydrophobic patch that is evident at the tip of the globular domain adjacent to the dimer interface (Fig. 7A).","type":"Results"}],"term_id":"IDPO:0000031","curator_id":"ahatos","start":572,"term_ontology":"IDPO","curator_name":"András Hatos","reference_id":"21454609","version":3,"curator_orcid":"0000-0001-9224-9820","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02324r002","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_P53865","date":"2018-09-01T12:24:14.000Z","acc":"P53865","name":"Chaotic nuclear migration protein 67","length":581,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000013BBCA","genes":[{"name":{"value":"CNM67"},"orfNames":[{"value":"N1264"}],"olnNames":[{"value":"YNL225C"}]}],"alphafold_very_low_content":0.26506024096385544,"disorder_content":0.01721170395869191,"disprot_consensus":{"full":[{"start":572,"end":581,"type":"D"}],"Structural state":[{"start":572,"end":581,"type":"D"}],"Disorder function":[{"start":572,"end":581,"type":"F"}]}},{"features":{"pfam":[{"id":"PF05254","name":"Uncharacterised protein family (UPF0203)","start":7,"end":75}]},"uniref50":"UniRef50_Q05776","sequence":"MGNIMSASFAPECTDLKTKYDSCFNEWYSEKFLKGKSVENECSKQWYAYTTCVNAALVKQGIKPALDEAREEAPFENGGKLKEVDK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q05776","disprot_id":"DP02325","ncbi_taxon_id":559292,"regions_counter":1,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":81,"region_id":"DP02325r001","released":"2022_03","ec_id":"ECO:0006198","reference_html":"Structural and mechanistic insights into phospholipid transfer by Ups1-Mdm35 in mitochondria. <i> Watanabe Y, Tamura Y, Kawano S, Endo T. </i> Nat Commun, 2015","statement":[{"text":"Residues 67–81 did not exhibit defined electron density, suggesting that the C-terminal segment is disordered in solution.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jpujols","start":67,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4YTV"}],"reference_id":"26235513","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_Q05776","date":"2018-09-01T15:17:41.000Z","acc":"O60200","name":"Mitochondrial distribution and morphology protein 35","length":86,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000013B6D1","genes":[{"name":{"value":"MDM35"},"olnNames":[{"value":"YKL053C-A"}]}],"alphafold_very_low_content":0.023255813953488372,"disorder_content":0.1744186046511628,"disprot_consensus":{"full":[{"start":67,"end":81,"type":"D"}],"Structural state":[{"start":67,"end":81,"type":"D"}]}},{"features":{"pfam":[{"id":"PF04707","name":"PRELI-like family","start":17,"end":169}]},"uniref50":"UniRef50_Q05776","sequence":"MVLLHKSTHIFPTDFASVSRAFFNRYPNPYSPHVLSIDTISRNVDQEGNLRTTRLLKKSGKLPTWVKPFLRGITETWIIEVSVVNPANSTMKTYTRNLDHTGIMKVEEYTTYQFDSATSSTIADSRVKFSSGFNMGIKSKVEDWSRTKFDENVKKSRMGMAFVIQKLEEARNPQF","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_Q05776","disprot_id":"DP02326","ncbi_taxon_id":559292,"regions_counter":3,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":71,"region_id":"DP02326r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural and mechanistic insights into phospholipid transfer by Ups1-Mdm35 in mitochondria. <i> Watanabe Y, Tamura Y, Kawano S, Endo T. </i> Nat Commun, 2015","statement":[{"text":"The crystallographic B-factors of loop Ω1 are high as compared with those for the other regions, suggesting its flexible nature (Fig. 3d). As having been speculated for other START domains with such a flexible Ω loop, the loop Ω1 of Ups1 may function as a lid that regulates lipid binding to the pocket (see below).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jpujols","start":62,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"4YTW"}],"reference_id":"26235513","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":71,"term_name":"molecular function regulator","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural and mechanistic insights into phospholipid transfer by Ups1-Mdm35 in mitochondria. <i> Watanabe Y, Tamura Y, Kawano S, Endo T. </i> Nat Commun, 2015","statement":[{"text":"The crystallographic B-factors of loop Ω1 are high as compared with those for the other regions, suggesting its flexible nature (Fig. 3d). As having been speculated for other START domains with such a flexible Ω loop, the loop Ω1 of Ups1 may function as a lid that regulates lipid binding to the pocket (see below).","type":"Results"}],"term_id":"GO:0098772","curator_id":"jpujols","start":62,"term_ontology":"GO","curator_name":"Jordi Pujols Pujol","reference_id":"26235513","version":3,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP02326r002","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":71,"term_name":"lipid binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural and mechanistic insights into phospholipid transfer by Ups1-Mdm35 in mitochondria. <i> Watanabe Y, Tamura Y, Kawano S, Endo T. </i> Nat Commun, 2015","statement":[{"text":"Deletion of the Ω1 loop (ΔLid) also completely impaired the PA transfer activity of Ups1–Mdm35. These results indicate that conserved basic residues at the bottom and near the entrance of the pocket and the Ω1 lid play essential roles in the PA transfer activity of Ups1–Mdm35.","type":"Results"}],"term_id":"GO:0008289","curator_id":"jpujols","start":62,"term_ontology":"GO","curator_name":"Jordi Pujols Pujol","reference_id":"26235513","version":3,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP02326r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2018_11","uniref100":"UniRef100_Q05776","date":"2018-09-01T15:24:30.000Z","acc":"Q05776","name":"Protein UPS1, mitochondrial","length":175,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000006984C","genes":[{"name":{"value":"UPS1"},"olnNames":[{"value":"YLR193C"}]}],"alphafold_very_low_content":0,"disorder_content":0.05714285714285714,"disprot_consensus":{"full":[{"start":62,"end":71,"type":"D"}],"Structural state":[{"start":62,"end":71,"type":"D"}],"Molecular function":[{"start":62,"end":71,"type":"F"}]}},{"features":{"pfam":[{"id":"PF02121","name":"Phosphatidylinositol transfer protein","start":3,"end":251}],"gene3D":[{"start":2,"end":270,"id":"3.30.530.20","name":"3.30.530.20"}]},"uniref50":"UniRef50_Q00169","sequence":"MVLLKEYRVILPVSVDEYQVGQLYSVAEASKNETGGGEGVEVLVNEPYEKDGEKGQYTHKIYHLQSKVPTFVRMLAPEGALNIHEKAWNAYPYCRTVITNEYMKEDFLIKIETWHKPDLGTQENVHKLEPEAWKHVEAVYIDIADRSQVLSKDYKAEEDPAKFKSIKTGRGPLGPNWKQELVNQKDCPYMCAYKLVTVKFKWWGLQNKVENFIHKQERRLFTNFHRQLFCWLDKWVDLTMDDIRRMEEETKRQLDEMRQKDPVKGMTADD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q00169","disprot_id":"DP02327","ncbi_taxon_id":9606,"regions_counter":9,"creator":"jpujols","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":12,"region_id":"DP02327r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of a multifunctional protein. Mammalian phosphatidylinositol transfer protein complexed with phosphatidylcholine. <i> Yoder MD, Thomas LM, Tremblay JM, Oliver RL, Yarbrough LR, Helmkamp GM. </i> J Biol Chem, 2001","statement":[{"text":"Electron density for the first 12 or 13 residues was not observed in all cases, because of disorder.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jpujols","start":1,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"11104777","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":190,"region_id":"DP02327r002","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of a multifunctional protein. Mammalian phosphatidylinositol transfer protein complexed with phosphatidylcholine. <i> Yoder MD, Thomas LM, Tremblay JM, Oliver RL, Yarbrough LR, Helmkamp GM. </i> J Biol Chem, 2001","statement":[{"text":"Consistent with their proposed functions, both the regulatory loop and the C-terminal region were predicted to exhibit significant polypeptide backbone flexibility, a structural feature corroborated by specific B factors from the x-ray data.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jpujols","start":119,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"11104777","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":190,"term_name":"molecular recognition display site","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of a multifunctional protein. Mammalian phosphatidylinositol transfer protein complexed with phosphatidylcholine. <i> Yoder MD, Thomas LM, Tremblay JM, Oliver RL, Yarbrough LR, Helmkamp GM. </i> J Biol Chem, 2001","statement":[{"text":"Examination of the PITP structure reveals that the intervening residues 119–190 form an extensive loop region between strands 7 and 8. Postulating that this loop is likely required for the association of PITP with a wide variety of lipid- and protein-modifying enzymes, we refer to this region as the regulatory loop.","type":"Results"}],"term_id":"IDPO:0000037","curator_id":"jpujols","start":119,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","reference_id":"11104777","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02327r003","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":190,"region_id":"DP02327r004","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure-function analysis of human [corrected] phosphatidylinositol transfer protein alpha bound to phosphatidylinositol. <i> Tilley SJ, Skippen A, Murray-Rust J, Swigart PM, Stewart A, Morgan CP, Cockcroft S, McDonald NQ. </i> Structure, 2004","statement":[{"text":"two distinct forms of PITP\u0001 exist: (1) a “closed” loaded PITP\u0001. form in which the PC lipid is buried within the structure and (2) an “open” lipid-free form in which the phosphoIntroduction lipid-binding cavity is opened up and the lipid-exchange loop is swung away from the body of the structure. [The mostly disordered loop acts as a lid]","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jpujols","start":119,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1uw5"}],"reference_id":"14962392","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":190,"term_name":"protein binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure-function analysis of human [corrected] phosphatidylinositol transfer protein alpha bound to phosphatidylinositol. <i> Tilley SJ, Skippen A, Murray-Rust J, Swigart PM, Stewart A, Morgan CP, Cockcroft S, McDonald NQ. </i> Structure, 2004","term_id":"GO:0005515","curator_id":"jpujols","start":119,"term_ontology":"GO","curator_name":"Jordi Pujols Pujol","reference_id":"14962392","version":3,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02327r005","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":190,"term_name":"lipid binding","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure-function analysis of human [corrected] phosphatidylinositol transfer protein alpha bound to phosphatidylinositol. <i> Tilley SJ, Skippen A, Murray-Rust J, Swigart PM, Stewart A, Morgan CP, Cockcroft S, McDonald NQ. </i> Structure, 2004","term_id":"GO:0008289","curator_id":"jpujols","start":119,"term_ontology":"GO","curator_name":"Jordi Pujols Pujol","reference_id":"14962392","version":3,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02327r006","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":190,"term_name":"molecular function regulator","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure-function analysis of human [corrected] phosphatidylinositol transfer protein alpha bound to phosphatidylinositol. <i> Tilley SJ, Skippen A, Murray-Rust J, Swigart PM, Stewart A, Morgan CP, Cockcroft S, McDonald NQ. </i> Structure, 2004","term_id":"GO:0098772","curator_id":"jpujols","start":119,"term_ontology":"GO","curator_name":"Jordi Pujols Pujol","reference_id":"14962392","version":3,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02327r007","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":270,"region_id":"DP02327r008","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Structure of a multifunctional protein. Mammalian phosphatidylinositol transfer protein complexed with phosphatidylcholine. <i> Yoder MD, Thomas LM, Tremblay JM, Oliver RL, Yarbrough LR, Helmkamp GM. </i> J Biol Chem, 2001","statement":[{"text":"Consistent with their proposed functions, both the regulatory loop and the C-terminal region were predicted to exhibit significant polypeptide backbone flexibility, a structural feature corroborated by specific B factors from the x-ray data. The relative instability of portions of this helix is supported by the high B-factors calculated for residues 243–250","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"jpujols","start":233,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"11104777","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":270,"term_name":"order to pre-molten globule","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Structure of a multifunctional protein. Mammalian phosphatidylinositol transfer protein complexed with phosphatidylcholine. <i> Yoder MD, Thomas LM, Tremblay JM, Oliver RL, Yarbrough LR, Helmkamp GM. </i> J Biol Chem, 2001","statement":[{"text":"It seems that the interaction with lipid vesicles induce a conformational change of the C-terminus domain (helix), which adopts flexible conformation (not described, maybe a partial unfolding). This conformation allows the cleavage by trypsin in arg 253 and 259. This process is needed to extract the lipid from the vesicle.","type":"Curator statement"}],"term_id":"IDPO:0000016","curator_id":"jpujols","start":233,"term_ontology":"IDPO","curator_name":"Jordi Pujols Pujol","reference_id":"11104777","version":2,"curator_orcid":"0000-0001-9424-5866","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","region_id":"DP02327r009","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2018_11","uniref100":"UniRef100_Q00169","date":"2018-09-01T15:49:03.000Z","acc":"Q00169","name":"Phosphatidylinositol transfer protein alpha isoform","length":270,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000000DAD0","genes":[{"name":{"value":"PITPNA"},"synonyms":[{"value":"PITPN"}]}],"alphafold_very_low_content":0,"disorder_content":0.45185185185185184,"disprot_consensus":{"full":[{"start":1,"end":12,"type":"D"},{"start":119,"end":190,"type":"D"},{"start":233,"end":270,"type":"T"}],"Structural state":[{"start":1,"end":12,"type":"D"},{"start":119,"end":190,"type":"D"},{"start":233,"end":270,"type":"D"}],"Disorder function":[{"start":119,"end":190,"type":"F"}],"Molecular function":[{"start":119,"end":190,"type":"F"}],"Structural transition":[{"start":233,"end":270,"type":"T"}]}},{"features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":64,"end":359}],"gene3D":[{"start":57,"end":398,"id":"3.30.200.20","name":"Phosphorylase Kinase; domain 1"},{"start":151,"end":372,"id":"1.10.510.10","name":"Transferase(Phosphotransferase) domain 1"}]},"uniref50":"UniRef50_P53779","sequence":"MSLHFLYYCSEPTLDVKIAFCQGFDKQVDVSYIAKHYNMSKSKVDNQFYSVEVGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQPTVRNYVENRPKYAGLTFPKLFPDSLFPADSEHNKLKASQARDLLSKMLVIDPAKRISVDDALQHPYINVWYDPAEVEAPPPQIYDKQLDEREHTIEEWKELIYKEVMNSEEKTKNGVVKGQPSPSGAAVNSSESLPPSSSVNDISSMSTDQTLASDTDSSLEASAGPLGCCR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P53779","disprot_id":"DP02328","ncbi_taxon_id":9606,"regions_counter":1,"creator":"baykac","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":231,"region_id":"DP02328r001","released":"2022_03","ec_id":"ECO:0006220","reference_html":"Crystal structure of JNK3: a kinase implicated in neuronal apoptosis. <i> Xie X, Gu Y, Fox T, Coll JT, Fleming MA, Markland W, Caron PR, Wilson KP, Su MS. </i> Structure, 1998","term_id":"IDPO:0000002","curator_id":"baykac","start":206,"term_ontology":"IDPO","curator_name":"Burcu Aykac-Fas","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0003-3842-731X","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","cross_refs":[{"db":"PDB","id":"1JNK"}],"reference_id":"9739089","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_P53779","date":"2018-09-03T08:12:46.000Z","acc":"P53779","name":"Mitogen-activated protein kinase 10","length":464,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000002AE11","genes":[{"name":{"value":"MAPK10"},"synonyms":[{"value":"JNK3"},{"value":"JNK3A"},{"value":"PRKM10"},{"value":"SAPK1B"}]}],"alphafold_very_low_content":0.2349137931034483,"disorder_content":0.05603448275862069,"disprot_consensus":{"full":[{"start":206,"end":231,"type":"D"}],"Structural state":[{"start":206,"end":231,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00094","name":"von Willebrand factor type D domain","start":1446,"end":1614},{"id":"PF01347","name":"Vitellogenin TPR domain","start":427,"end":744},{"id":"PF09172","name":"Vitellinogen, open beta-sheet","start":776,"end":1027},{"id":"PF29934","name":"Vitellogenin N-terminal domain","start":22,"end":305}],"gene3D":[{"start":22,"end":322,"id":"2.30.230.10","name":"Lipovitellin; beta-sheet shell regions, chain A"},{"start":417,"end":772,"id":"1.25.10.20","name":"Vitellinogen, superhelical"}]},"uniref50":"UniRef50_A0A6P3DVD4","sequence":"MWLPLTVLLLAGIVSADYDHGWHVNNEYIYLVRSRTLVNLNELSDQHTGILMKALLTIQVKDPQMLTAKVSQSQYARILKSLPEGWDAEISDQMLELRDMPLSGKPFNIKLKHGVIRDIIVDRTIPTWEVNILKSIVSQLQVDSLGENAIRTSEMQIPTDEHPYGMFRAMEDSVGGKCEVLYDITPLPEQNVYVQPELVPVPDLKREGQYIDIRKSKNFNKCDQRMNYQFGITGNKYWEAGSNKNGKFFSQSAMSRIIISGTLKSYTIQSAVTTNIMYISPRFYDHEHGMVTSRMNLTLAAVKKITNPLPKPNSPESTGNLVYIYSNPYSDMEERRVGKVVEDSDNMMLSDSISSISSSEEATKGQNYRSLSSDSSSSSSFSNSEEDHYWQPKPTMEDAPQNPLSSIYIGYMGKYIGKSNEVDVVEKSKELISQIANEMEDPNDVYENHILEKYTVLCNLLRTMNKEQMLQVDKHVRLSPHELKSMDKTQVLKQNAWTVLKSAVAQAGTGPAFLVIKNWIEMKEVDSKRGADLLAKLPKTARAPTAEYIMEFFKLATGETVKNDLALNSSAIIAFSELVYNAQVSRKGLHNHYPVHTYGRLTPKHNKAVTEYYIPYLETELKKAVESGQSTVIQTYIMALGNIGHPKILPVLEPYLEGKVRMTVFQRTLMVSTLAKLAENFPKLARSILYKIYLNTMEEHQVRCTAVFILMQTDPPLTMLQRMAEFTKIDKNKYVNSAVKSTLESLANLKDAEYQTLAKKARVAKNLLSPSDYSYHYSRGYITESIMDEGNIISHMMLKYIGSDDSLIPNAIYYAVFSTYGDFKLPPFEVVTMVSSIRSILELNTSPEEKERIKLAAEKIAEQLNIISDEFIPLEGNIMWNGKYGARFLPFDQSCLSLLRELLLMYLKGESEGKLINRLGSYDITYGFPTETGLPFVYNFELPMLLKITGAMNNEAKNLKTIKMKTDFRILYAMKIQGRMSFVTPFEHQEYIAGVDVDFNLHLPMKLTLDIDLPKQSFEIKIWPLKGEDKAQLLHYSVVPYVANHNILSLRPLLTEKTAQMIIPDDIYLDTISDSDLLKVVLETDKSYDYKNWLDLDIDDLFNVVIAPWSSDNDNYRKVDVFLNLKREQVAPFVLKMSYDFMEMAPTAEDAKLWTPKATAMEPSDKHPDSEVRRKQWMDEAAKGVKSAKSQVIDIRLEVPVTSEETIMNVITVATSNSEIEKKGRTLVYWNFETLFEVCAASQTKVTPDNTVFYEEVAQLKPKVEFNADFRIGKVCSTGEQLNINSVATQSKELRERIKNSSLIKTCEKQMQQGNKILRACQNAAAISMILDQITISVDFQSQHFINFITKALNVMMNIDYLNEIAYIHTELSDLKVAGKRKIDIVANLTNDFESADVLISTPNMNIYANDIDLSALEISAEDVLMAADEDMDIQNLLYNEDEPACILDKTRAQTFDSKEYPLRLGKCWHVVVTTYPRVNPNNPNEKMRMHKFDSVSILTRDMENGQREMKVLLGDKELKFVPTSSQPKIFVNEQLIKVTKDMSWQEKMDDEVLYEIFQINDHSVGLVSDEYELNLVYDGKRIMMKAGDKFRKAIRGLCGNYDGKLINDFMAPEKCVFRKPEQFIASYALTKEECESEFFENSKLLMDQDCVYEEKNHLSNVISDKESGRRDIEESNWGYHKQTKSKQCTIMKAHMKEIEHMICFTIRQVPSCAPGCWATEMKPKDYQYHCMKRNAASLALKARIEKGAKPDLSQKSVTLTEPINVPLACKA","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Hymenoptera","Apocrita","Aculeata","Apoidea","Apidae","Bombus","Bombus"],"uniref90":"UniRef90_A0A6P3TLJ9","disprot_id":"DP02330","ncbi_taxon_id":130704,"regions_counter":1,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":395,"region_id":"DP02330r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation. <i> Havukainen H, Underhaug J, Wolschin F, Amdam G, Halskau Ø. </i> J Exp Biol, 2012","statement":[{"text":"The polyserine region in Bombus ignitus and Pimpla nipponica vitellogenin is a random coil.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":361,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22573762","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_C4PB33","date":"2018-09-05T15:57:56.000Z","acc":"C4PB33","name":"Vitellogenin","length":1772,"organism":"Bombus ignitus","dataset":[],"UniParc":"UPI0001A45FCF","genes":[],"disorder_content":0.019751693002257337,"disprot_consensus":{"full":[{"start":361,"end":395,"type":"D"}],"Structural state":[{"start":361,"end":395,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00094","name":"von Willebrand factor type D domain","start":1474,"end":1637},{"id":"PF01347","name":"Vitellogenin TPR domain","start":430,"end":746},{"id":"PF09172","name":"Vitellinogen, open beta-sheet","start":779,"end":1043},{"id":"PF29934","name":"Vitellogenin N-terminal domain","start":22,"end":304}],"gene3D":[{"start":418,"end":775,"id":"1.25.10.20","name":"Vitellinogen, superhelical"},{"start":22,"end":323,"id":"2.30.230.10","name":"Lipovitellin; beta-sheet shell regions, chain A"}]},"uniref50":"UniRef50_O17428","sequence":"MWCPLFLVLLAGAATAEHLQAWKTDTEYQYAVRGRTLSALHDVADQYSGIIMRALLTIQPKSDGTLEAKVTKARYAQIHTKLPGGWNSEIPDHKLEMKQFPMSEKVFEIKMKHGVVRDLIVDKDVPTWEVNVLKSIVSQLQVDTQGENLMASKYNQEPEDEGVTAMFKTMEDTVGGRCEVLYDINPLPEFVLQKRPELVPMPDIRGDGEIIDIVKTKNYSNCEQRSGYHFGIPGTNKWEPSSGASGNFLSRSSVSRVIVTGNLKSFTIQSSVSTNKVILSPNFHENRKGMVSSRVNVTLVKIGAPSTGDWSTPANPESTGNLVYNYNNPFAGVGEDRRASRPQDNRNSEEKVRSLYNLYRRNRINDNDDDSSASDSSKSAKSLESNEEQLYWQPKPTLNEAPAMAMLPFFIGNHGKSIHKTDEIEPITMAKTLASQIGSDFQDPNSITDEQTLEKFTLLVRIIRTMSTQQIAEAERDLYQSNNEIDPHDESQSVRRGTWAAFRDAVAQAGTAPALVTITLWIKQKKIRGVEAASVVGVLAKTARTPTREYIDVFFELATMPETIHEPFLNTTALFTFSELVRYSQMDNPSSHTRYPVHTFGRFSDKINPEVFRMYVPYLAEKLKTSIEKNENAKAHTYIVSLGNIAHPKILAVFEPYLEGKMPASTFQRLLMVISLNKLATLKPKLARGVFYRIYKNTGEAHQLRCAAVTALMSTNPPASMLQRMAEFTNEDHSKHVNAAVKSAIESASELETPQWQELAENARNAKPLLNKESYGFEYSKLYLTDFIEREMNVAYQAQASFISSDDSYVPEALFVKARAIFGGFTFPRTSAGAMVSSAKDLLSAFEDAFKGEKTSHKHSHVEFSPENVAKLLKIKSEPNEDVEGAFMLQSAYNNKFMSLDKNTLKNLPELSSKALKALKDGHHFNTARIESYEMTMSFPMESGFPFVYTMKVPSMLKLAGSVKGDSNEDSLDGHVHLRAVYSVQFQSKLGFVTPFEHQHYMAGINKNYQAYVPLRVNVNYEDSDKRVTLKIQPIEQNEKFKLWHHSVVPFTSRHDILKMSPVLKDKETQKIITEEVSKNEYNFGSDKHGVKFTVLAEADNDNSPLNFEDAKWERNPLTQLFHLFVEQPVYHKVDIFMQPSKSSEQSIILSTAFETLQDDTTKYDEDRSKHIKAEAPKVENKKLNDPQRRRKLLKEAAKGIAAADAFAVDIGLEYPGQAPVQAFATLAFASSEVDEKSRGLVYWRLTDAGNDFEFESCTSLEARSPRTSDFGKDMLDQPEFRSRKFDIDLRYGQTCEKGYKVEIQGSQEQTEKYRDTIKRLPTAIECIRAAKKGMKSLPACHDVSVKMTMLDKTRITIKYDKDSREMYQLFDDYLDSMSDADDDLKSSKKRLNAVKDDDKAYDDTVKIAVDLSPNDNNGRFSYESDFVKLEARDVPINGIGPLVNVHPDLETAERLDMDMSDEPVRQRICVLDSHSATTFDESTYPINLGKCWHVVMTTFPKTNKNSGSAEPIDEDMALSILVRDAGDKKKDIKVTLGDKELQFSHADSKNKVTLDGKKVDLSEKRSYRHKNGKDIDFEVLQRPDGTLGLVSSKYDIDAWYDGQRVQIKASGKYRSDIRGLCGNFDGEPDNDFTSPKDCVLLKPEEFAASYALTTKDCHGSALEHARKASQAVCSQKSPRPGNVVSDRDAGRKYSENSNWGYHSRQNSDDEQGKNDSSDHKRCNTLRTKVIEEEDQICFSLRPLPTCAEGCTANRTKPKVMPMHCMPKNIAAERMADRIKQGANPDFSQKSYTKKNGFDIPVGCHAA","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Hymenoptera","Apocrita","Parasitoida","Ichneumonoidea","Ichneumonidae","Pimplinae","Pimplini","Pimpla"],"uniref90":"UniRef90_O17428","disprot_id":"DP02331","ncbi_taxon_id":67752,"regions_counter":1,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":397,"region_id":"DP02331r001","released":"2022_03","ec_id":"ECO:0006204","reference_html":"A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation. <i> Havukainen H, Underhaug J, Wolschin F, Amdam G, Halskau Ø. </i> J Exp Biol, 2012","statement":[{"text":"The polyserine region in Bombus ignitus and Pimpla nipponica vitellogenin is a random coil.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":356,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"far-UV circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"22573762","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2018_11","uniref100":"UniRef100_O17428","date":"2018-09-05T15:58:53.000Z","acc":"O17428","name":"Vitellogenin","length":1807,"organism":"Pimpla nipponica","dataset":[],"UniParc":"UPI000008083D","genes":[{"name":{"value":"Vg","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAC32024.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAC32024.1"}}]}}],"disorder_content":0.02324294410625346,"disprot_consensus":{"full":[{"start":356,"end":397,"type":"D"}],"Structural state":[{"start":356,"end":397,"type":"D"}]}},{"features":{"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":415,"end":615},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":651,"end":759},{"id":"PF25430","name":"DDX23-like domain","start":272,"end":356}],"gene3D":[{"start":632,"end":820,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"},{"start":352,"end":631,"id":"3.40.50.300","name":"P-loop containing nucleotide triphosphate hydrolases"}]},"uniref50":"UniRef50_Q9BUQ8","sequence":"MAGELADKKDRDASPSKEERKRSRTPDRERDRDRDRKSSPSKDRKRHRSRDRRRGGSRSRSRSRSKSAERERRHKERERDKERDRNKKDRDRDKDGHRRDKDRKRSSLSPGRGKDFKSRKDRDSKKDEEDEHGDKKPKAQPLSLEELLAKKKAEEEAEAKPKFLSKAEREAEALKRRQQEVEERQRMLEEERKKRKQFQDLGRKMLEDPQERERRERRERMERETNGNEDEEGRQKIREEKDKSKELHAIKERYLGGIKKRRRTRHLNDRKFVFEWDASEDTSIDYNPLYKERHQVQLLGRGFIAGIDLKQQKREQSRFYGDLMEKRRTLEEKEQEEARLRKLRKKEAKQRWDDRHWSQKKLDEMTDRDWRIFREDYSITTKGGKIPNPIRSWKDSSLPPHILEVIDKCGYKEPTPIQRQAIPIGLQNRDIIGVAETGSGKTAAFLIPLLVWITTLPKIDRIEESDQGPYAIILAPTRELAQQIEEETIKFGKPLGIRTVAVIGGISREDQGFRLRMGCEIVIATPGRLIDVLENRYLVLSRCTYVVLDEADRMIDMGFEPDVQKILEHMPVSNQKPDTDEAEDPEKMLANFESGKHKYRQTVMFTATMPPAVERLARSYLRRPAVVYIGSAGKPHERVEQKVFLMSESEKRKKLLAILEQGFDPPIIIFVNQKKGCDVLAKSLEKMGYNACTLHGGKGQEQREFALSNLKAGAKDILVATDVAGRGIDIQDVSMVVNYDMAKNIEDYIHRIGRTGRAGKSGVAITFLTKEDSAVFYELKQAILESPVSSCPPELANHPDAQHKPGTILTKKRREETIFA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9BUQ8","disprot_id":"DP02332","ncbi_taxon_id":9606,"regions_counter":12,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":257,"region_id":"DP02332r001","released":"2023_06","ec_id":"ECO:0006165","reference_html":"Phosphorylation drives a dynamic switch in serine/arginine-rich proteins. <i> Xiang S, Gapsys V, Kim HY, Bessonov S, Hsiao HH, Möhlmann S, Klaukien V, Ficner R, Becker S, Urlaub H, Lührmann R, de Groot B, Zweckstetter M. </i> Structure, 2013","statement":[{"text":"A) Domain organization of hPrp28. The 100 kDa hPrp28 contains three domains: disordered domain (residues 1–257, green), DEAD box domain (residues 410–642, orange), and HELICc domain (residues 678–759, red). Residues 1–138 comprise the RS domain of hPrp28.","type":"Figure"},{"text":"Although full-length hPrp28 has an additional 563 residues, the number of NMR signals in a 15N-1H HSQC spectrum was only slightly increased when compared to hPrp(1–257) (Figure 9A). Thus, the globular parts of hPrp28(1–820) tumble to slowly to be detected by solution-state NMR. Nevertheless, the close match of peak positions for the two proteins demonstrates that conformations of the isolated RS domain are retained in the intact protein.","type":"Results"},{"text":"The poor dispersion in 1H-NMR spectra, with signals clustered around the 8.0-8.5 ppm region, shows this region is disordered.","type":"Curator statement"}],"term_id":"IDPO:0000002","curator_id":"maspromonte","start":1,"term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":4,"curator_orcid":"0000-0002-4937-6952","date":"2023-06-21T13:15:22.588Z","reference_source":"pmid","term_name":"disorder","reference_id":"24183573","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T14:51:10.533Z"}},{"start":1,"end":138,"reference_id":"24183573","reference_source":"pmid","reference_html":"Phosphorylation drives a dynamic switch in serine/arginine-rich proteins. <i> Xiang S, Gapsys V, Kim HY, Bessonov S, Hsiao HH, Möhlmann S, Klaukien V, Ficner R, Becker S, Urlaub H, Lührmann R, de Groot B, Zweckstetter M. </i> Structure, 2013","date":"2023-06-21T18:33:43.265Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP02332r003","statement":[{"text":"(B) Mass spectrometric (MS) determination of phosphorylation sites within the\nN-terminal RS domain of hPrp28 in native U5 snRNP (square) and functional\nspliceosomal B complex (circle).","type":"Figure"},{"text":"Here, we analyzed the phosphorylation sites of hPrp28 in U5 snRNPs and assembled B complexes by mass spectrometry. The analysis identified serine residues at positions 14, 23, 38, 39, 41, 65, 67, 106, 107, 109, as well as T25, to be phosphorylated in both complexes (Figure 8B; Table S3). Phosphorylation at S16\nand S63 was found only in U5 snRNP.","type":"Results"},{"text":"Table S3, related to Figure 8 | Phosphorylation sites (marked in red) in the RS domain of hPrP28 as identified by mass spectrometry in native U5 snRNP and spliceosomal B complex.","type":"Supplementary material"}],"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":14,"end":14,"position":"Specific residue","statements":[{"type":"Supplementary material","text":"Table S3, related to Figure 8 | Phosphorylation sites (marked in red) in the RS domain of hPrP28 as identified by mass spectrometry in native U5 snRNP and spliceosomal B complex."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":16,"end":16,"position":"Specific residue","statements":[{"type":"Supplementary material","text":"Table S3, related to Figure 8 | Phosphorylation sites (marked in red) in the RS domain of hPrP28 as identified by mass spectrometry in native U5 snRNP and spliceosomal B complex."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":23,"end":23,"position":"Specific residue","statements":[{"type":"Supplementary material","text":"Table S3, related to Figure 8 | Phosphorylation sites (marked in red) in the RS domain of hPrP28 as identified by mass spectrometry in native U5 snRNP and spliceosomal B complex."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":25,"end":25,"position":"Specific residue","statements":[{"type":"Supplementary material","text":"Table S3, related to Figure 8 | Phosphorylation sites (marked in red) in the RS domain of hPrP28 as identified by mass spectrometry in native U5 snRNP and spliceosomal B complex."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":38,"end":38,"position":"Specific residue","statements":[{"type":"Supplementary material","text":"Table S3, related to Figure 8 | Phosphorylation sites (marked in red) in the RS domain of hPrP28 as identified by mass spectrometry in native U5 snRNP and spliceosomal B complex."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":39,"end":39,"position":"Specific residue","statements":[{"type":"Supplementary material","text":"Table S3, related to Figure 8 | Phosphorylation sites (marked in red) in the RS domain of hPrP28 as identified by mass spectrometry in native U5 snRNP and spliceosomal B complex."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":41,"end":41,"position":"Specific residue","statements":[{"type":"Supplementary material","text":"Table S3, related to Figure 8 | Phosphorylation sites (marked in red) in the RS domain of hPrP28 as identified by mass spectrometry in native U5 snRNP and spliceosomal B complex."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":65,"end":65,"position":"Specific residue","statements":[{"type":"Supplementary material","text":"Table S3, related to Figure 8 | Phosphorylation sites (marked in red) in the RS domain of hPrP28 as identified by mass spectrometry in native U5 snRNP and spliceosomal B complex."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":67,"end":67,"position":"Specific residue","statements":[{"type":"Supplementary material","text":"Table S3, related to Figure 8 | Phosphorylation sites (marked in red) in the RS domain of hPrP28 as identified by mass spectrometry in native U5 snRNP and spliceosomal B complex."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":63,"end":63,"position":"Specific residue","statements":[{"type":"Supplementary material","text":"Table S3, related to Figure 8 | Phosphorylation sites (marked in red) in the RS domain of hPrP28 as identified by mass spectrometry in native U5 snRNP and spliceosomal B complex."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":106,"end":106,"position":"Specific residue","statements":[{"type":"Supplementary material","text":"Table S3, related to Figure 8 | Phosphorylation sites (marked in red) in the RS domain of hPrP28 as identified by mass spectrometry in native U5 snRNP and spliceosomal B complex."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":107,"end":107,"position":"Specific residue","statements":[{"type":"Supplementary material","text":"Table S3, related to Figure 8 | Phosphorylation sites (marked in red) in the RS domain of hPrP28 as identified by mass spectrometry in native U5 snRNP and spliceosomal B complex."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":109,"end":109,"position":"Specific residue","statements":[{"type":"Supplementary material","text":"Table S3, related to Figure 8 | Phosphorylation sites (marked in red) in the RS domain of hPrP28 as identified by mass spectrometry in native U5 snRNP and spliceosomal B complex."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-22T14:01:25.149Z"}},{"start":807,"end":820,"reference_id":"24914973","reference_source":"pmid","reference_html":"Structural and functional analysis of the human spliceosomal DEAD-box helicase Prp28. <i> Möhlmann S, Mathew R, Neumann P, Schmitt A, Lührmann R, Ficner R. </i> Acta Crystallogr D Biol Crystallogr, 2014","date":"2023-06-21T15:05:55.554Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":1,"cross_refs":[{"db":"PDB","id":"4NHO"}],"region_id":"DP02332r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"191088","entry_name":"Cyclohexylaminopropanesulfonic acid"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16793","entry_name":"mercury(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":"glycerol"}],"statement":[{"text":"The final hPrp28ΔN model consists of residues 352–806, five sulfate\nions, two glycerol molecules, 3-cyclohexyl-1-propylsulfonic acid, one disordered Hg atom and 220 solvent molecules. Missing residues, namely the N-terminal residues 338–351, loops 695–702 and 724–727 and the C-terminal residues 807–820, resulted from non-interpretable electron density and are most likely to be disordered.","type":"Results"},{"text":"Two loop regions (residues 695–702 and 724–727) as well as the N-terminal residues 338–351 and the C-terminal residues 807–820 are not defined in the electron-density map and are most likely to be disordered.","type":"Results"}],"construct_alterations":[{"term_id":"MOD:00677","term_name":"hydroxylated residue","term_namespace":"Protein modification","start":519,"end":519,"position":"Specific residue"},{"term_id":"MOD:00677","term_name":"hydroxylated residue","term_namespace":"Protein modification","start":791,"end":791,"position":"Specific residue"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T15:27:05.653Z"}},{"start":791,"end":820,"reference_id":"30315277","reference_source":"pmid","reference_html":"Structures of the human pre-catalytic spliceosome and its precursor spliceosome. <i> Zhan X, Yan C, Zhang X, Lei J, Shi Y. </i> Cell Res, 2018","date":"2023-06-21T12:52:20.377Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP02332r007","statement":[{"text":"The Electron Microscopy structure of the Precusor of Human Pre-catalytic Spliceosome (pre-B complex), shows this region of the Probable ATP-dependent RNA helicase DDX23 (alternative name Prp28) lacks electron density, indicating it is disordered.","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"6AH0"},{"db":"EMDB","id":"EMD-9621"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17401","entry_name":"myo-inositol hexakisphosphate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15996","entry_name":"GTP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T14:42:59.771Z"}},{"start":1,"end":157,"reference_id":"30975767","reference_source":"pmid","reference_html":"Mechanism of 5' splice site transfer for human spliceosome activation. <i> Charenton C, Wilkinson ME, Nagai K. </i> Science, 2019","date":"2023-06-21T15:45:23.829Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":1,"cross_refs":[{"db":"PDB","id":"6QX9"},{"db":"PDB","id":"6QW6"},{"db":"EMDB","id":"EMD-4665"},{"db":"EMDB","id":"EMD-4658"}],"region_id":"DP02332r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17401","entry_name":"myo-inositol hexakisphosphate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15996","entry_name":"GTP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"The Electron Microscopy structure of the human U5.U4/U6 tri-snRNP and human fully-assembled precatalytic spliceosome (pre-B complex), shows this region of the Probable ATP-dependent RNA helicase DDX23 (alternative name Prp28) lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-22T13:17:32.221Z"}},{"start":204,"end":240,"reference_id":"30975767","reference_source":"pmid","reference_html":"Mechanism of 5' splice site transfer for human spliceosome activation. <i> Charenton C, Wilkinson ME, Nagai K. </i> Science, 2019","date":"2023-06-21T12:48:38.366Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6QX9"},{"db":"PDB","id":"6QW6"},{"db":"EMDB","id":"EMD-4665"},{"db":"EMDB","id":"EMD-4658"}],"region_id":"DP02332r009","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17401","entry_name":"myo-inositol hexakisphosphate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15996","entry_name":"GTP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"The Electron Microscopy structure of the human U5.U4/U6 tri-snRNP and human fully-assembled precatalytic spliceosome (pre-B complex), shows this region of the Probable ATP-dependent RNA helicase DDX23 (alternative name Prp28) lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-22T13:17:30.565Z"}},{"start":338,"end":351,"reference_id":"24914973","reference_source":"pmid","reference_html":"Structural and functional analysis of the human spliceosomal DEAD-box helicase Prp28. <i> Möhlmann S, Mathew R, Neumann P, Schmitt A, Lührmann R, Ficner R. </i> Acta Crystallogr D Biol Crystallogr, 2014","date":"2023-06-21T15:07:05.322Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4NHO"}],"region_id":"DP02332r010","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"191088","entry_name":"Cyclohexylaminopropanesulfonic acid"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16793","entry_name":"mercury(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":"glycerol"}],"statement":[{"text":"The final hPrp28ΔN model consists of residues 352–806, five sulfate ions, two glycerol molecules, 3-cyclohexyl-1-propylsulfonic acid, one disordered Hg atom and 220 solvent molecules. Missing residues, namely the N-terminal residues 338–351, loops 695–702 and 724–727 and the C-terminal residues 807–820, resulted from non-interpretable electron density and are most likely to be disordered.","type":"Results"},{"text":"Two loop regions (residues 695–702 and 724–727) as well as the N-terminal residues 338–351 and the C-terminal residues 807–820 are not defined in the electron-density map and are most likely to be disordered.","type":"Results"}],"construct_alterations":[{"term_id":"MOD:00677","term_name":"hydroxylated residue","term_namespace":"Protein modification","start":519,"end":519,"position":"Specific residue"},{"term_id":"MOD:00677","term_name":"hydroxylated residue","term_namespace":"Protein modification","start":791,"end":791,"position":"Specific residue"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T15:27:01.130Z"}},{"start":204,"end":219,"reference_id":"24183573","reference_source":"pmid","reference_html":"Phosphorylation drives a dynamic switch in serine/arginine-rich proteins. <i> Xiang S, Gapsys V, Kim HY, Bessonov S, Hsiao HH, Möhlmann S, Klaukien V, Ficner R, Becker S, Urlaub H, Lührmann R, de Groot B, Zweckstetter M. </i> Structure, 2013","date":"2023-06-21T18:24:00.179Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP02332r011","statement":[{"text":"The assignment was only possible by using five- and six-dimensional NMR spectra. Sequence-specific resonance assignment unambiguously identified\nphosphorylated serines in the RS repeat stretches comprising residues 204–219 and 242–247.","type":"Results"},{"text":"Sequence-specific resonance assignment of hPrp28 (1–138) phosphorylated by SRPK1 revealed 13 phosphorylation sites including 12 serines and one threonine (Figure 9A). The in vitro phosphorylation pattern is largely consistent with that in\nnative U5 snRNPs and spliceosomal B complexes (Figure 9B).","type":"Results"},{"text":"(B) Mass spectrometric (MS) determination of phosphorylation sites within the\nN-terminal RS domain of hPrp28 in native U5 snRNP (square) and functional\nspliceosomal B complex (circle). Phosphorylation sites determined by NMR\nafter in vitro phosphorylation with SRPK1 are in red letters.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-22T14:02:59.875Z"}},{"start":242,"end":247,"reference_id":"24183573","reference_source":"pmid","reference_html":"Phosphorylation drives a dynamic switch in serine/arginine-rich proteins. <i> Xiang S, Gapsys V, Kim HY, Bessonov S, Hsiao HH, Möhlmann S, Klaukien V, Ficner R, Becker S, Urlaub H, Lührmann R, de Groot B, Zweckstetter M. </i> Structure, 2013","date":"2023-06-21T18:26:02.271Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP02332r012","statement":[{"text":"The assignment was only possible by using five- and six-dimensional NMR spectra. Sequence-specific resonance assignment unambiguously identified phosphorylated serines in the RS repeat stretches comprising residues 204–219 and 242–247.","type":"Results"},{"text":"Sequence-specific resonance assignment of hPrp28 (1–138) phosphorylated by SRPK1 revealed 13 phosphorylation sites including 12 serines and one threonine (Figure 9A). The in vitro phosphorylation pattern is largely consistent with that in native U5 snRNPs and spliceosomal B complexes (Figure 9B).","type":"Results"},{"text":"(B) Mass spectrometric (MS) determination of phosphorylation sites within the N-terminal RS domain of hPrp28 in native U5 snRNP (square) and functional spliceosomal B complex (circle). Phosphorylation sites determined by NMR after in vitro phosphorylation with SRPK1 are in red letters.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-22T14:03:00.776Z"}}],"released":"2018_11","uniref100":"UniRef100_Q9BUQ8","date":"2018-09-05T16:29:16.000Z","acc":"Q9BUQ8","name":"Probable ATP-dependent RNA helicase DDX23","length":820,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI000006EFFB","genes":[{"name":{"value":"DDX23","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:17347","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:17347"}}]}}],"alphafold_very_low_content":0.18048780487804877,"disorder_content":0.3670731707317073,"disprot_consensus":{"full":[{"start":1,"end":257,"type":"D"},{"start":338,"end":351,"type":"D"},{"start":791,"end":820,"type":"D"}],"Structural state":[{"start":1,"end":257,"type":"D"},{"start":338,"end":351,"type":"D"},{"start":791,"end":820,"type":"D"}],"Disorder function":[{"start":1,"end":138,"type":"F"},{"start":204,"end":219,"type":"F"},{"start":242,"end":247,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00027","name":"Cyclic nucleotide-binding domain","start":158,"end":243},{"id":"PF00027","name":"Cyclic nucleotide-binding domain","start":280,"end":371},{"id":"PF02197","name":"Regulatory subunit of type II PKA R-subunit","start":9,"end":45}],"gene3D":[{"start":259,"end":389,"id":"2.60.120.10","name":"Jelly Rolls"},{"start":106,"end":258,"id":"2.60.120.10","name":"Jelly Rolls"},{"start":1,"end":45,"id":"1.20.890.10","name":"cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain"}]},"uniref50":"UniRef50_P13861","sequence":"MSHIQIPPGLTELLQGYTVEVLRQQPPDLVEFAVEYFTRLREARAPASVLPAATPRQSLGHPPPEPGPDRVADAKGDSESEEDEDLEVPVPSRFNRRVSVCAETYNPDEEEEDTDPRVIHPKTDEQRCRLQEACKDILLFKNLDQEQLSQVLDAMFERIVKADEHVIDQGDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNRGSFGELALMYNTPRAATIVATSEGSLWGLDRVTFRRIIVKNNAKKRKMFESFIESVPLLKSLEVSERMKIVDVIGEKIYKDGERIITQGEKADSFYIIESGEVSILIRSRTKSNKDGGNQEVEIARCHKGQYFGELALVTNKPRAASAYAVGDVKCLVMDVQAFERLLGPCMDIMKRNISHYEEQLVKMFGSSVDLGNLGQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P13861","disprot_id":"DP02333","ncbi_taxon_id":9606,"regions_counter":2,"creator":"ndavey","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":90,"region_id":"DP02333r001","released":"2022_03","ec_id":"ECO:0006224","reference_html":"Intrinsic disorder within an AKAP-protein kinase A complex guides local substrate phosphorylation. <i> Smith FD, Reichow SL, Esseltine JL, Shi D, Langeberg LK, Scott JD, Gonen T. </i> Elife, 2013","statement":[{"text":"Electron microscopy and three-dimensional reconstructions of type-II PKA-AKAP18γ complexes reveal hetero-pentameric assemblies that adopt a range of flexible tripartite configurations. Intrinsically disordered regions within each PKA regulatory subunit impart the molecular plasticity that affords an ∼16 nanometer radius of motion to the associated catalytic subunits.","type":"Introduction"}],"term_id":"IDPO:0000002","curator_id":"ndavey","start":44,"term_ontology":"IDPO","curator_name":"Norman Davey","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":2,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24192038","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":90,"term_name":"flexible linker","released":"2022_03","ec_name":"cryogenic electron microscopy evidence used in manual assertion","reference_html":"Intrinsic disorder within an AKAP-protein kinase A complex guides local substrate phosphorylation. <i> Smith FD, Reichow SL, Esseltine JL, Shi D, Langeberg LK, Scott JD, Gonen T. </i> Elife, 2013","statement":[{"text":"conformational plasticity observed in these analyses is facilitated by this intrinsically disordered region between residues 44 and 90 of RIIα, a linker that connects the AKAP docking site to the cAMP-responsive transduction domains. This notion is substantiated by a primary sequence analysis of RIIα orthologs, showing that the linker regions are of similar length but exhibit low amino acid identity","type":"Results"}],"term_id":"IDPO:0000033","curator_id":"ndavey","start":44,"term_ontology":"IDPO","curator_name":"Norman Davey","reference_id":"24192038","version":3,"curator_orcid":"0000-0001-6988-4850","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","region_id":"DP02333r002","ec_go":"IDA","disprot_namespace":"Disorder function"}],"released":"2018_11","uniref100":"UniRef100_P13861","date":"2018-09-05T16:43:27.000Z","acc":"P13861","name":"cAMP-dependent protein kinase type II-alpha regulatory subunit","length":404,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012DC0D","genes":[{"name":{"value":"PRKAR2A"},"synonyms":[{"value":"PKR2"},{"value":"PRKAR2"}]}],"alphafold_very_low_content":0.15594059405940594,"disorder_content":0.11633663366336634,"disprot_consensus":{"full":[{"start":44,"end":90,"type":"D"}],"Structural state":[{"start":44,"end":90,"type":"D"}],"Disorder function":[{"start":44,"end":90,"type":"F"}]}},{"acc":"Q98148","sequence":"MAPPGMRLRSGRSTGAPLTRGSCRKRNRSPERCDLGDDLHLQPRRKHVADSIDGRECGPHTLPIPGSPTVFTSGLPAFVSSPTLPVAPIPSPAPATPLPPPALLPPVTTSSSPIPPSHPVSPGTTDTHSPSPALPPTQSPESSQRPPLSSPTGRPDSSTPMRPPPSQQTTPPHSPTTPPPEPPSKSSPDSLAPSTLRSLRKRRLSSPQGPSTLNPICQSPPVSPPRCDFANRSVYPPWATESPIYVGSSSDGDTPPRQPPTSPISIGSSSPSEGSWGDDTAMLVLLAEIAEEASKNEKECSENNQAGEDNGDNEISKESQVDKDDNDNKDDEEEQETDEEDEEDDEEDDEEDDEEDDEEDDEEDDEEDDEEDDEEDDEEDDEEDDEEEDEEEDEEEDEEEEDEEDDDDEDNEDEEDDEEEDKKEDEEDGGDGNKTLSIQSSQQQQEPQQQEPQQQEPQQQEPLQEPQQQEPQQQEPQQQEPLQEPQQQEPQQQEPLQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQREPQQREPQQREPQQREPQQREPQQREPQQREPQQREPQQREPQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQEQQDEQEQQDEQEQQDEQQQDEQQQQDEQQQQDEQQQQDEQQQQDEQQQQDEQEQQEEQEQQEEQEQELEEQEQELEDQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEVEEQEQEVEEQEQEQEEQELEEVEEQEQEQEEQEEQELEEVEEQEEQELEEVEEQEEQELEEVEEQEQQELEEVEEQEQQGVEQQEQETVEEPIILHGSSSEDEMEVDYPVVSTHEQIASSPPGDNTPDDDPQPGPSREYRYVLRTSPPHRPGVRMRRVPVTHPKKPHPRYQQPPVPYRQIDDCPAKARPQHIFYRRFLGKDGRRDPKCQWKFAVIFWGNDPYGLKKLSQAFQFGGVKAGPVSCLPHPGPDQSPITYCVYVYCQNKDTSKKVQMARLAWEASHPLAGNLQSSIVKFKKPLPLTQPGENQGPGDSPQEMT","creator":"bmesza","dataset":["Viral proteins"],"date":"2018-09-08T15:40:08.000Z","disprot_id":"DP02334","features":{"gene3D":[{"start":1006,"end":1146,"id":"3.30.70.390","name":"Epstein Barr virus nuclear antigen-1, DNA-binding domain","_id":"685af523b4ac24d5329d94e9"}],"pfam":[{"id":"PF21501","name":"Protein LANA1-like, DNA-binding domain","start":1028,"end":1145}]},"genes":[],"length":1162,"name":"Kaposi's sarcoma-associated herpes-like virus ORF73 homolog","ncbi_taxon_id":37296,"organism":"Human herpesvirus 8","regions_counter":15,"released":"2018_11","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Peploviricota","Herviviricetes","Herpesvirales","Herpesviridae","Gammaherpesvirinae","Rhadinovirus"],"UniParc":"UPI0000039921","uniref100":"UniRef100_Q98148","uniref50":"UniRef50_Q9QR71","uniref90":"UniRef90_Q9QR71","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1110,"end":1162,"interaction_partner":[],"reference_html":"Structural Mechanism of Transcriptional Regulator NSD3 Recognition by the ET Domain of BRD4. <i> Zhang Q, Zeng L, Shen C, Ju Y, Konuma T, Zhao C, Vakoc CR, Zhou MM. </i> Structure, 2016","reference_id":"27291650","region_id":"DP02334r001","released":"2022_03","sample":[],"sequence_construct":"DTSKKVQMARLAWEASHPLAGNLQSSIVKFKKPLPLTQPGENQGPGDSPQEMT","statement":[{"type":"Results","text":"Our observation of very narrow 1H chemical shift dispersion of merely 0.9 ppm (7.7–8.6 ppm) in the 15N-HSQC spectrum of LANA C-terminal fragment (residues 1110–1162) indicates that this region is unstructured (Figure S1A).","_id":"685af523b4ac24d5329d94eb"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-26T13:04:33.550Z","_id":"685af523b4ac24d5329d94ec"},"version":3,"_id":"685af523b4ac24d5329d94ea","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2ND0","_id":"685af523b4ac24d5329d94f1"},{"db":"BMRB","id":"26042","_id":"685af523b4ac24d5329d94f2"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1133,"end":1144,"interaction_partner":[],"reference_html":"Structural Mechanism of Transcriptional Regulator NSD3 Recognition by the ET Domain of BRD4. <i> Zhang Q, Zeng L, Shen C, Ju Y, Konuma T, Zhao C, Vakoc CR, Zhou MM. </i> Structure, 2016","reference_id":"27291650","region_id":"DP02334r003","released":"2022_03","sample":[],"sequence_construct":"DTSKKVQMARLAWEASHPLAGNLQSSIVKFKKPLPLTQPGENQGPGDSPQEMT","statement":[{"type":"Results","text":"The structure reveals that the viral peptide establishes a two-strand inter-molecular antiparallel β-sheet with the protein.","_id":"685af523b4ac24d5329d94f0"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-27T08:50:02.230Z","_id":"685af523b4ac24d5329d94f3"},"version":3,"_id":"685af523b4ac24d5329d94ef","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"26042","_id":"685af523b4ac24d5329d94f6"},{"db":"PDB","id":"2ND0","_id":"685af523b4ac24d5329d94f7"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1133,"end":1144,"interaction_partner":[{"db":"UniProt","id":"O60885","partner_start":601,"partner_end":683,"_id":"685af523b4ac24d5329d94f8"}],"reference_html":"Structural Mechanism of Transcriptional Regulator NSD3 Recognition by the ET Domain of BRD4. <i> Zhang Q, Zeng L, Shen C, Ju Y, Konuma T, Zhao C, Vakoc CR, Zhou MM. </i> Structure, 2016","reference_id":"27291650","region_id":"DP02334r004","released":"2022_03","sample":[],"sequence_construct":"DTSKKVQMARLAWEASHPLAGNLQSSIVKFKKPLPLTQPGENQGPGDSPQEMT","statement":[{"type":"Results","text":"We thus constructed a BRD4 ET domain fused at its N-terminus to LANA comprising residues 1110–1162 via a flexible linker (GSGSGS), and determined by NMR analysis that the minimal ET binding site in LANA is confined to residues 1131–1149 (NLQSSIVKFKKPLPLTQPG) (data not shown). Notably, the 15N-HSQC spectra of the ET domain displayed nearly identical protein backbone resonance perturbation patterns induced by adding a LANA segment consisting of residues 1110–1162 or 1131–1149 (Figure S1A), or a LANA peptide of residues 1133–1144 (Figure 1B, red vs. blue signals), thereby defining the ET domain binding site in LANA to residues 1133–1144. We further determined binding affinity of the ET domain to the LANA peptide by NMR titration to be approximately Kd = 635 μM (Figure S1A).","_id":"685af523b4ac24d5329d94f5"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-27T08:50:04.822Z","_id":"685af523b4ac24d5329d94f9"},"version":4,"_id":"685af523b4ac24d5329d94f4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"amonzon","curator_name":"Alex Monzon","curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IC","ec_id":"ECO:0007759","ec_name":"curator inference from database used in manual assertion","ec_ontology":"ECO","start":745,"end":925,"interaction_partner":[],"reference_html":"An Entry Referenced from MobiDB","reference_id":"https://mobidb.org/Q98148","region_id":"DP02334r005","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"This poly-E region is inferred by the curator to be disordered, based on MobiDB-Lite and according to experimental evidence demonstrating that poly-E repeats display random-coil-like conformation (PMID:16949547)","_id":"685af523b4ac24d5329d94fb"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":1,"_id":"685af523b4ac24d5329d94fa","reference_source":"mobidb"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"amonzon","curator_name":"Alex Monzon","curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IC","ec_id":"ECO:0007759","ec_name":"curator inference from database used in manual assertion","ec_ontology":"ECO","start":620,"end":723,"interaction_partner":[],"reference_html":"An Entry Referenced from MobiDB","reference_id":"https://mobidb.org/Q98148","region_id":"DP02334r006","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"This poly-E region is inferred by the curator to be disordered, based on MobiDB-Lite and according to experimental evidence demonstrating that poly-E repeats display random-coil-like conformation (PMID:16949547)","_id":"685af523b4ac24d5329d94fd"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":1,"_id":"685af523b4ac24d5329d94fc","reference_source":"mobidb"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"amonzon","curator_name":"Alex Monzon","curator_orcid":"0000-0003-0362-8218","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IC","ec_id":"ECO:0007759","ec_name":"curator inference from database used in manual assertion","ec_ontology":"ECO","start":325,"end":426,"interaction_partner":[],"reference_html":"An Entry Referenced from MobiDB","reference_id":"https://mobidb.org/Q98148","region_id":"DP02334r007","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"This poly-E region is inferred by the curator to be disordered, based on MobiDB-Lite and according to experimental evidence demonstrating that poly-E repeats display random-coil-like conformation (PMID:16949547)","_id":"685af523b4ac24d5329d94ff"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"version":1,"_id":"685af523b4ac24d5329d94fe","reference_source":"mobidb"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2ND0","_id":"685af523b4ac24d5329d951f"},{"db":"BMRB","id":"26042","_id":"685af523b4ac24d5329d9520"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1133,"end":1144,"interaction_partner":[],"reference_html":"Structural Mechanism of Transcriptional Regulator NSD3 Recognition by the ET Domain of BRD4. <i> Zhang Q, Zeng L, Shen C, Ju Y, Konuma T, Zhao C, Vakoc CR, Zhou MM. </i> Structure, 2016","reference_id":"27291650","region_id":"DP02334r015","released":"2022_03","sample":[],"sequence_construct":"DTSKKVQMARLAWEASHPLAGNLQSSIVKFKKPLPLTQPGENQGPGDSPQEMT","statement":[{"type":"Results","text":"We thus constructed a BRD4 ET domain fused at its N-terminus to LANA comprising residues 1110–1162 via a flexible linker (GSGSGS), and determined by NMR analysis that the minimal ET binding site in LANA is confined to residues 1131–1149 (NLQSSIVKFKKPLPLTQPG) (data not shown). Notably, the 15N-HSQC spectra of the ET domain displayed nearly identical protein backbone resonance perturbation patterns induced by adding a LANA segment consisting of residues 1110–1162 or 1131–1149 (Figure S1A), or a LANA peptide of residues 1133–1144 (Figure 1B, red vs. blue signals), thereby defining the ET domain binding site in LANA to residues 1133–1144. We further determined binding affinity of the ET domain to the LANA peptide by NMR titration to be approximately Kd = 635 μM (Figure S1A).","_id":"685af523b4ac24d5329d9521"}],"states_connection":[],"term_comment":"","term_def":"\"A set of processes which all viruses follow to ensure survival; includes attachment and entry of the virus particle, decoding of genome information, translation of viral mRNA by host ribosomes, genome replication, and assembly and release of viral particles containing the genome.\" [ISBN:1555811272]","term_go_domain":"P","term_id":"GO:0019058","term_is_binding":false,"term_is_obsolete":false,"term_name":"viral life cycle","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-27T08:50:05.948Z","_id":"685af523b4ac24d5329d9522"},"version":1,"_id":"685af523b4ac24d5329d951e","reference_source":"pmid"}],"__v":0,"disorder_content":0.37865748709122204,"disprot_consensus":{"full":[{"start":325,"end":426,"type":"D"},{"start":620,"end":723,"type":"D"},{"start":745,"end":925,"type":"D"},{"start":1110,"end":1132,"type":"D"},{"start":1133,"end":1144,"type":"T"},{"start":1145,"end":1162,"type":"D"}],"Structural state":[{"start":325,"end":426,"type":"D"},{"start":620,"end":723,"type":"D"},{"start":745,"end":925,"type":"D"},{"start":1110,"end":1162,"type":"D"}],"Structural transition":[{"start":1133,"end":1144,"type":"T"}],"Molecular function":[{"start":1133,"end":1144,"type":"F"}],"Biological process":[{"start":1133,"end":1144,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00626","name":"Gelsolin repeat","start":1445,"end":1497},{"id":"PF02209","name":"Villin headpiece domain","start":2159,"end":2194}],"gene3D":[{"start":1980,"end":2104,"id":"3.40.20.10","name":"Severin"},{"start":1726,"end":1864,"id":"3.40.20.10","name":"Severin"},{"start":2128,"end":2194,"id":"1.10.950.10","name":"Villin headpiece domain"},{"start":1411,"end":1528,"id":"3.40.20.10","name":"Severin"},{"start":1865,"end":1967,"id":"3.40.20.10","name":"Severin"},{"start":1554,"end":1664,"id":"3.40.20.10","name":"Severin"}]},"uniref50":"UniRef50_O95425-3","creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref90":"UniRef90_O46385","disprot_id":"DP02337","ncbi_taxon_id":9913,"regions_counter":5,"sequence":"MKRKERIARRLEGIETDTQPILLQSCTGLVTHRLLEEDTPRYMRATDPASPHIGRSNEEEETSDSSLEKQTRSKQCTETSGIHADSPYSSGIMDTQSLESKAERIARYKAERRRQLAEKYGLTLDPEADSETPSRYSRSRKDPEAAEKRGVRSERSAESSRDAGSSYSRTELSGLRTCVAESKDYGLHRSDGVSDTEVLLNAENQRRGQEPSATGLARDLPLAGEVSSSFSFSGRDSALGEVPRSPKAVHSLPSPSPGQPASPSHSTSDLPLPAEARASIGKPKHEWFLQKDSEGDTPSLINWPSRVKVREKLVREESARSSPELTSESLTQRRHQTAPGHYLAFQSENSAFDRVSGKVASSARQPIRGYVQPAEPVHTITLVTSDTPESISEGSWVGPAPQTVTKPPPSKVLEGERRDTPVLHICESKAEDVLFSDALEKTRKTLAVLEDRGSGRSQEAPSGTEDLSQPAVGIVTAEPQKESESLAHPPMAQQQPTERMGRSEMVMYVQSEAVSQGHRKEVPTRKHRVLTRSLSDYTGPPQLQALKAKAPAPKRDAESQTSKAELELGLLDTKVSVAQLRNAFLESARASRKPELHSRVEGSSEGPGVERERGSRKPRRYFSPGENRKTSERFRTQPITSAERKESDRSTSNSEMPAAEDEEKVDERARLSVAAKRLLFREMEKSFDEKSVPKRRSRNAAVEQRLRRLQDRSHTQPVTTEEVVIAAEPTPASCSVATHPVMTRHPSPTVAKSPVQPARTLQASAHQKALARDQTNESKDSAEQGEPDSSTLSLAEKLALFNKLSQPVSKAISTRNRLDMRQRRMNARYQTQPVTLGEVEQVQSGKLMAFSPTINTSVSTVASTVPPMYAGNLRTKPLPDDSFGATEQKFASSLENSDSPVRSILKSQGWQPSVEGAGSKAMLREFEETERKGGLTGGDGGVTKYGSFEEAELSYPVLSRVREGDNHKEAIYALPRKGSLELAHPPIAQLGDDLKEFSTPKSTMQASPDWKERQLFEEKVDLENVTKRKFSLKAAEFGEPTSEQTGAAAGKPAAPTATPVSWKPQDPSEQPQEKRYQSPCAMFAAGEIKAPAVEGSLDSPSKTMSIKERLALLKKSGEEDWRNRLNRKQEYGKASITSSLHIQETEQSLKKKRVTESRESQMTIEERKHLITVREDAWKTRGKGAANDSTQFTVAGRMVKRGLASPTAITPVASPVSSKARGTTPVSRPLEDIEARPDMQLESDLKLDRLETFLRRLNNKVGGMQETVLTVTGKSVKEVMKPDDDETFAKFYRSVDSSLPRSPVELDEDFDVIFDPYAPRLTSSVAEHKRAVRPKRRVQASKNPLKMLAAREDLLQEYTEQRLNVAFVESKRMKVEKLSANSSFSEVTLAGLASKENFSNVSLRSVNLTEQNSNNSAVPYKKLMLLQVKGRRHVQTRLVEPRAPSLNSGDCFLLLSPHHCFLWVGEFANVIEKAKASELASLIQTKRELGCRATYIQTVEEGINTHTHAAKDFWKLLGGQASYQSAGDPKEDELYETAIIETNCIYRLMDDKLVPDDDYWGKIPKCSLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGTFDYENCDINPLDPGECNPLIPRKGQGRPDWAIFGRLTEHNETILFKEKFLDWTELKRPNEKNASELAQHKDDARAEVKPYDVTRMVPVPQTTAGTVLDGVNVGRGYGLVEGDDRRQFEIASISVDVWHILEFDYSRLPKQSIGQFHEGDAYVVKWKFIVSTAVGSRQKGEHSVRVAGKEKCVYFFWQGRQSTVSEKGTSALMTVELDEERGAQVQVLQGKEPPCFLQCFQGGMVVHSGRREEEEENTQSEWRLYCVRGEVPVEGNLLEVACHCSSLRSRTSMVVLNVHKALIYLWHGCKAQAHTKEVGRTAANKIKDQCPLEAGLHSSSKVTIHECDEGSEPLGFWDALGRRDRKAYDCMLQDPGNFNFTPRLFILSSSSGDFSATEFMYPARDPSVVNSMPFLQEDLYSAPQPALFLVDNHHEVYLWQGWWPIENKITGSARIRWASDRKSAMETVLQYCRGKNLKKPPPKSYLIHAGLEPLTFTNMFPSWEHREDIAEITEMDTEVSNQITLVEDVLAKLCKTIYPLADLLARPLPEGVDPLKLEIYLTDEDFEFALDMTRDEYNALPAWKQVNLKKAKGLF","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":342,"term_name":"disorder","reference_html":"An N-terminal, 830 residues intrinsically disordered region of the cytoskeleton-regulatory protein supervillin contains Myosin II- and F-actin-binding sites. <i> Fedechkin SO, Brockerman J, Luna EJ, Lobanov MY, Galzitskaya OV, Smirnov SL. </i> J Biomol Struct Dyn, 2013","start":1,"region_id":"DP02337r002","term_id":"IDPO:0000002","version":2,"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"An N-terminal, 830-residue Intrinsically Disordered Region of the Cytoskeleton-regulatory Protein Supervillin Contains Myosin II- and F-actin- Binding Sites","type":"Title"},{"text":"Here, we utilize Circular Dichroism (CD) and bioinformatics sequence analysis to demonstrate that the N-terminal part of supervillin forms an extended intrinsically disordered region (IDR). Our combined data indicate that the N-terminus of human and bovine supervillin sequences (positions 1–830) represents an intrinsically disordered region, which is the largest IDR known to date in the villin/gelsolin family. Moreover, this result suggests a potentially novel mechanism of regulation of myosin II and F-actin via the intrinsically disordered N-terminal region of hub protein supervillin.","type":"Abstract"},{"text":"Major cytoskeletal interactors, including filamentous actin and myosin II, bind within the unique supervillin amino terminus, amino acids 1-830.","type":"Abstract"},{"text":"Here, we present CD spectra and bioinformatics analyses to show that this region of supervillin is predominately disordered in the unbound state.","type":"Introduction"},{"text":"Furthermore, the incidence of charged side chains within residues 1–830 is also somewhat higher in the N-terminus of supervillin than in its C-terminus or in villin and gelsolin. These hydrophobicity-charge features of the supervillin N-terminus are typical for intrinsically disordered proteins (IDP), which lack the capacity to fold in an aqueous solvent","type":"Results"},{"text":"This N-terminal disordered region of bovine supervillin interacts with at least 17 proteins.","type":"Discussion"},{"text":"Based on the disordered nature of the N-terminus, we can propose certain features of the mechanisms of binding of F-actin and myosin II by supervillin. Its sequence M binds the S2 fragment of nonmuscle and smooth muscle myosin II, whereas fragments A1, A2 and A3 bind F-actin","type":"Discussion"},{"text":"Our CD data indicate that the first 342 residues of supervillin form an intrinsically disordered region. The complementary bioinformatics analysis suggests that the entire N-terminus of supervillin likely represents a large IDR.","type":"Conclusion"}],"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","reference_id":"23075227","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":174,"term_name":"protein binding","reference_html":"F-actin and myosin II binding domains in supervillin. <i> Chen Y, Takizawa N, Crowley JL, Oh SW, Gatto CL, Kambara T, Sato O, Li XD, Ikebe M, Luna EJ. </i> J Biol Chem, 2003","start":11,"region_id":"DP02337r003","term_id":"GO:0005515","version":4,"curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","ec_name":"yeast 2-hybrid evidence used in manual assertion","statement":[{"text":"Minimal sequences required for the binding to myosin II are supervillin amino acids 11-174 and sequences within myosin subdomain S2.","type":"Discussion"}],"curator_orcid":"0000-0002-5152-5953","date":"2022-03-09T10:46:07.000Z","reference_source":"pmid","ec_id":"ECO:0005805","reference_id":"12917436","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P07313","operator":"and","partner_start":null,"partner_end":null}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":174,"term_name":"protein binding","reference_html":"F-actin and myosin II binding domains in supervillin. <i> Chen Y, Takizawa N, Crowley JL, Oh SW, Gatto CL, Kambara T, Sato O, Li XD, Ikebe M, Luna EJ. </i> J Biol Chem, 2003","start":11,"region_id":"DP02337r004","term_id":"GO:0005515","version":4,"curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","ec_name":"co-sedimentation assay evidence used in manual assertion","statement":[{"text":"Supervillin sequences capable of binding to actin filaments include a site near the C terminus of SV-(171-342), the N terminus of SV-(343-571), and the C terminus of SV-(570-830) (Fig. 2C).","type":"Discussion"},{"text":"Similar amounts of co-sedimentation with F-actin were observed for SV-(343-571) as for SV-(171-342) and SV-(570-830) (Fig. 2A), each of which contains a single C-terminal actin-binding site (Fig. 2C).","type":"Discussion"},{"text":"F-actin binds independently and directly to three regions of supervillin (SV-(171-342), SV-(343-571), and SV570-830)).","type":"Figure"}],"curator_orcid":"0000-0002-5152-5953","date":"2022-03-09T10:43:38.792Z","reference_source":"pmid","ec_id":"ECO:0001164","reference_id":"12917436","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P68135","operator":"and","partner_start":null,"partner_end":null}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":342,"term_name":"molecular adaptor activity","reference_html":"F-actin and myosin II binding domains in supervillin. <i> Chen Y, Takizawa N, Crowley JL, Oh SW, Gatto CL, Kambara T, Sato O, Li XD, Ikebe M, Luna EJ. </i> J Biol Chem, 2003","start":1,"region_id":"DP02337r005","term_id":"GO:0060090","version":3,"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"fluorescence microscopy evidence used in manual assertion","statement":[{"text":"Overexpression of supervillin amino acids 1-174 in COS7 cells disrupted the localization of myosin IIB without obviously affecting actin filaments. Taken together, these results suggest that supervillin may mediate actin and myosin II filament organization at cholesterol-rich membrane domains.","type":"Abstract"},{"text":"Minimal sequences required for the binding to myosin II are supervillin amino acids 11-174 and sequences within myosin subdomain S2.","type":"Discussion"},{"text":"F-actin binds independently and directly to three regions of supervillin (SV-(171-342), SV-(343-571), and SV570-830)).","type":"Figure"},{"text":"Supervillin sequences capable of binding to actin filaments include a site near the C terminus of SV-(171-342), the N terminus of SV-(343-571), and the C terminus of SV-(570-830) (Fig. 2C).","type":"Discussion"},{"text":"Similar amounts of co-sedimentation with F-actin were observed for SV-(343-571) as for SV-(171-342) and SV-(570-830) (Fig. 2A), each of which contains a single C-terminal actin-binding site (Fig. 2C).","type":"Discussion"}],"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006323","reference_id":"12917436","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2019_09","uniref100":"UniRef100_O46385","date":"2019-09-05T08:14:43.114Z","acc":"O46385","name":"Supervillin","length":2194,"organism":"Bos taurus","dataset":[],"UniParc":"UPI0001A61553","genes":[{"name":{"value":"SVIL","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9382871","url":"http://www.ncbi.nlm.nih.gov/pubmed/9382871","alternativeUrl":"https://europepmc.org/abstract/MED/9382871"}}]}}],"alphafold_very_low_content":0.5706472196900638,"disorder_content":0.15587967183226983,"disprot_consensus":{"full":[{"start":1,"end":342,"type":"D"}],"Structural state":[{"start":1,"end":342,"type":"D"}],"Molecular function":[{"start":1,"end":342,"type":"F"}]}},{"features":{"pfam":[{"id":"PF00984","name":"UDP-glucose/GDP-mannose dehydrogenase family, central domain","start":214,"end":308},{"id":"PF03720","name":"UDP-glucose/GDP-mannose dehydrogenase family, UDP binding domain","start":332,"end":446},{"id":"PF03721","name":"UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain","start":5,"end":202}],"gene3D":[{"start":1,"end":212,"id":"3.40.50.720","name":"NAD(P)-binding Rossmann-like Domain"},{"start":245,"end":474,"id":"3.40.50.720","name":"NAD(P)-binding Rossmann-like Domain"},{"start":213,"end":244,"id":"1.20.5.100","name":"Cytochrome c1, transmembrane anchor, C-terminal"}]},"uniref50":"UniRef50_O60701","creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O60701","disprot_id":"DP02338","ncbi_taxon_id":9606,"regions_counter":3,"sequence":"MFEIKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIKEADLVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKPNLNLQVLSNPEFLAEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYEHWVPREKILTTNTWSSELSKLAANAFLAQRISSINSISALCEATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIIDSLFNTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPGVSEDDQVSRLVTISKDPYEACDGAHAVVICTEWDMFKELDYERIHKKMLKPAFIFDGRRVLDGLHNELQTIGFQIETIGKKVSSKRIPYAPSGEIPKFSLQDPPNKKPKV","regions":[{"term_namespace":"Disorder function","ec_ontology":"ECO","end":494,"region_id":"DP02338r002","reference_id":"30420606","start":465,"term_id":"IDPO:0000031","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Here we show that the entropic force produced by an ID carboxy-terminus (ID-tail) shifts the conformational ensemble of human UDP-α-D-glucose-6-dehydrogenase (hUGDH) toward a substate with a high affinity for an allosteric inhibitor.","type":"Abstract"},{"text":"The function of the ID-tail does not depend on its sequence or chemical composition. Instead, the affinity enhancement can be accurately predicted based on the length of the ID segment and is consistent with the entropic force generated by an unstructured peptide attached to the protein surface","type":"Abstract"},{"text":"Our data show that the unfolded state of the ID-tail rectifies the dynamics and structure of hUGDH to favor inhibitor binding","type":"Abstract"},{"text":"For example, the 30-residue disordered C-terminus of hUGDH (residues 465–494) is often removed with no apparent impact on kinetic parameters19. Here, we show that this C-terminal segment (called the ‘ID-tail’) plays a novel role in the allosteric mechanism of hUGDH. hUGDH catalyzes the NAD+-dependent oxidation of UDP-α-D-glucose (UDP-Glc) to UDP-α-D-glucuronic acid19 and is regulated by the allosteric feedback inhibitor UDP-α-D-Xylose (UDP-Xyl)","type":"Article"},{"text":"We used the allostery quenching A136M substitution to see if the ID-tail functions independently of the allosteric switch; this substitution has been shown to lock the allosteric switch and the hexamer in the low UDP-Xyl affinity, E state22. Inhibition studies show no significant difference in UDP-Xyl affinity between hUGDHFL-A136M and hUGDHΔID-A136M, which suggests that the ID-tail requires a functional allosteric switch and the EΩ state to enhance the affinity for UDP-Xyl","type":"Article"},{"text":"the ID-tail functions as a length-dependent (l) entropic rectifier that biases (k) the distribution toward the high affinity substate","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"The entropic force generated by intrinsically disordered segments tunes protein function. <i> Keul ND, Oruganty K, Schaper Bergman ET, Beattie NR, McDonald WE, Kadirvelraj R, Gross ML, Phillips RS, Harvey SC, Wood ZA. </i> Nature, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5VR8"}],"term_name":"flexible C-terminal tail","ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T09:28:43.067Z"}},{"start":465,"end":494,"reference_id":"30420606","reference_source":"pmid","reference_html":"The entropic force generated by intrinsically disordered segments tunes protein function. <i> Keul ND, Oruganty K, Schaper Bergman ET, Beattie NR, McDonald WE, Kadirvelraj R, Gross ML, Phillips RS, Harvey SC, Wood ZA. </i> Nature, 2018","date":"2023-05-31T16:00:03.536Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5VR8"}],"region_id":"DP02338r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:9235"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022"}],"statement":[{"text":"For example, the 30-residue disordered C-terminus of hUGDH (residues 465–494) is often removed with no apparent impact on kinetic parameters19.","type":"Article"},{"text":"The PDB structure shows this region lacks electron density indicating it is disordered. ","type":"Curator statement"}]}],"released":"2019_09","uniref100":"UniRef100_O60701","date":"2019-09-05T15:36:17.486Z","acc":"O60701","name":"UDP-glucose 6-dehydrogenase","length":494,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI0000001075","genes":[{"name":{"value":"UGDH"}}],"alphafold_very_low_content":0.03643724696356275,"disorder_content":0.06072874493927125,"disprot_consensus":{"full":[{"start":465,"end":494,"type":"D"}],"Structural state":[{"start":465,"end":494,"type":"D"}],"Disorder function":[{"start":465,"end":494,"type":"F"}]}},{"features":{"pfam":[{"id":"PF04012","name":"PspA/IM30 family","start":2,"end":214}]},"uniref50":"UniRef50_O80796","creator":"ahatos","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_O80796","disprot_id":"DP02341","ncbi_taxon_id":3702,"regions_counter":3,"sequence":"MNLFERFSRVVKSYANALISSFEDPEKILEQTVIEMNSDLTKMRQATAQVLASQKQLQNKYKAAQQSSDDWYKRAQLALAKGDEDLAREALKRRKSFADNATALKTQLDQQKGVVDNLVSNTRLLESKIQEAKAKKDTLLARARTAKTATKVQEMIGTVNTSGALSAFEKMEEKVMAMESEADALTQIGTDELEGKFQMLETSSVDDDLADLKKELSGSSKKGELPPGRSTVAASTRYPFKDSEIENELNELRRKANDF","regions":[{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":259,"region_id":"DP02341r001","start":221,"ec_id":"ECO:0006204","statement":[{"text":"To ascertain whether Vc represents an IDR or not, circular dichroism (CD) spectra of a synthetic peptide precisely corresponding to Vc (38 amino acids) were examined. A large negative peak at approximately 202 nm is characteristic to the coil conformation that dominates in disordered proteins. The minimum spectrum of Vc at around 200 nm typically showed the property of IDR.","type":"Results"}],"curator_id":"bszabo","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"27208228","version":2,"reference_html":"VIPP1 Has a Disordered C-Terminal Tail Necessary for Protecting Photosynthetic Membranes against Stress. <i> Zhang L, Kondo H, Kamikubo H, Kataoka M, Sakamoto W. </i> Plant Physiol, 2016","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","reference_source":"pmid","ec_ontology":"ECO","end":259,"region_id":"DP02341r002","start":221,"ec_id":"ECO:0006317","statement":[{"text":"The ellipticity at 202 nm was monitored upon increasing the temperature, and was found to increase gradually. However, the lack of an obvious thermal transition indicated that Vc does not take a prominent secondary structure. In addition, the slight CD spectral change was reversible.","type":"Results"}],"curator_id":"bszabo","released":"2022_03","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Beata Szabo","reference_id":"27208228","version":2,"reference_html":"VIPP1 Has a Disordered C-Terminal Tail Necessary for Protecting Photosynthetic Membranes against Stress. <i> Zhang L, Kondo H, Kamikubo H, Kataoka M, Sakamoto W. </i> Plant Physiol, 2016","date":"2022-02-14T09:00:00.000Z","term_id":"IDPO:0000002","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":259,"term_name":"protein folding chaperone","released":"2022_03","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","statement":[{"text":"Vc (VIPP1 C-terminal tail) acts in promoting flexible mobility against stress by preventing self-association of FVPs; and the elevated expression of VIPP1 improves the tolerance of chloroplasts against heat shock. Dynamic movement of VIPP1 upon stress is a prerequisite for such tolerance,","type":"Discussion"}],"term_id":"GO:0044183","curator_id":"bszabo","start":221,"term_ontology":"GO","curator_name":"Beata Szabo","reference_id":"27208228","version":3,"reference_html":"VIPP1 Has a Disordered C-Terminal Tail Necessary for Protecting Photosynthetic Membranes against Stress. <i> Zhang L, Kondo H, Kamikubo H, Kataoka M, Sakamoto W. </i> Plant Physiol, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006317","region_id":"DP02341r003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2019_09","uniref100":"UniRef100_O80796","date":"2019-09-09T16:26:28.510Z","acc":"A0A178W0D3","name":"Plastid transcriptionally active 4","length":259,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI0007E24479","genes":[{"name":{"value":"PTAC4","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ANM60036.1","url":"https://www.ebi.ac.uk/ena/browser/view/ANM60036.1"}}]},"synonyms":[{"value":"VIPP1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ANM60036.1","url":"https://www.ebi.ac.uk/ena/browser/view/ANM60036.1"}}]}],"orfNames":[{"value":"T8F5.2","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ANM60036.1","url":"https://www.ebi.ac.uk/ena/browser/view/ANM60036.1"}}]},{"value":"T8F5_2","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ANM60036.1","url":"https://www.ebi.ac.uk/ena/browser/view/ANM60036.1"}}]}],"olnNames":[{"value":"At1g65260","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ANM60036.1","url":"https://www.ebi.ac.uk/ena/browser/view/ANM60036.1"}}]}]}],"alphafold_very_low_content":0.2277992277992278,"disorder_content":0.15057915057915058,"disprot_consensus":{"full":[{"start":221,"end":259,"type":"D"}],"Structural state":[{"start":221,"end":259,"type":"D"}],"Molecular function":[{"start":221,"end":259,"type":"F"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF00612","name":"IQ calmodulin-binding motif","start":32,"end":52},{"id":"PF06614","name":"Neuromodulin","start":68,"end":227},{"id":"PF10580","name":"Gap junction protein N-terminal region","start":2,"end":31}]},"uniref50":"UniRef50_P07936","sequence":"MLCCMRRTKQVEKNDEDQKIEQDGVKPEDKAHKAATKIQASFRGHITRKKLKGEKKGDAPAAEAEAKEKDDAPVADGVEKKEGDGSATTDAAPATSPKAEEPSKAGDAPSEEKKGEGDAAPSEEKAGSAETESAAKATTDNSPSSKAEDGPAKEEPKQADVPAAVTDAAATTPAAEDAATKAAQPPTETAESSQAEEEKDAVDEAKPKESARQDEGKEDPEADQEHA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P07936","disprot_id":"DP02342","ncbi_taxon_id":10090,"regions_counter":13,"creator":"fquaglia","regions":[{"region_id":"DP02342r003","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T15:49:32.551Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":227,"term_id":"IDPO:0000004","start":1,"version":3,"statement":[{"text":"CD spectra of Nm and Ng showed an intense minimum at 201 and 204 nm respectively, indicating the presence of disordered regions in these proteins. The CD analysis further supports that Nm and Ng both have residual secondary structural elements (mainly α-helix) and suggests that these two proteins exist in a premolten globular conformational state of protein quartet model under physiological conditions (Supplementary Figure 2A).","type":"Results"}],"term_name":"pre-molten globule","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2023_12","term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"23462742","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006204","curator_id":"bmesza","reference_html":"Structural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with Calmodulin. <i> Kumar V, Chichili VP, Zhong L, Tang X, Velazquez-Campoy A, Sheu FS, Seetharaman J, Gerges NZ, Sivaraman J. </i> Sci Rep, 2013","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02342r006","unpublished":true,"validated":{"curator_id":"bmesza","timestamp":"2020-11-26T15:43:23.626Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":57,"term_id":"GO:0051179","start":34,"version":3,"statement":[{"text":"One proposed biochemical function of Nm and Ng is to target CaM at the membrane in the vicinity of ‘CaM-activated enzymes’ under low Ca2+ conditions at the pre- and post-synaptic terminals, respectively1,22,24. Therefore, Nm and Ng might serve as a Ca2+-regulated modulators of CaM activity in neurons.","type":"Discussion"}],"term_name":"localization","ec_name":"isothermal titration calorimetry evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2023_12","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"23462742","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Biological process","ec_id":"ECO:0005647","curator_id":"fquaglia","reference_html":"Structural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with Calmodulin. <i> Kumar V, Chichili VP, Zhong L, Tang X, Velazquez-Campoy A, Sheu FS, Seetharaman J, Gerges NZ, Sivaraman J. </i> Sci Rep, 2013","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"region_id":"DP02342r007","unpublished":true,"validated":{"curator_id":"bmesza","timestamp":"2020-11-26T15:43:34.306Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":57,"term_id":"GO:0098772","start":34,"version":3,"statement":[{"text":"One proposed biochemical function of Nm and Ng is to target CaM at the membrane in the vicinity of ‘CaM-activated enzymes’ under low Ca2+ conditions at the pre- and post-synaptic terminals, respectively1,22,24. Therefore, Nm and Ng might serve as a Ca2+-regulated modulators of CaM activity in neurons.","type":"Discussion"}],"term_name":"molecular function regulator","ec_name":"isothermal titration calorimetry evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2023_12","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"23462742","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"fquaglia","reference_html":"Structural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with Calmodulin. <i> Kumar V, Chichili VP, Zhong L, Tang X, Velazquez-Campoy A, Sheu FS, Seetharaman J, Gerges NZ, Sivaraman J. </i> Sci Rep, 2013","ec_go":"IPI","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":227,"region_id":"DP02342r009","start":1,"term_id":"IDPO:0000004","unpublished":true,"statement":[{"text":"The NMR spectra of full-length Nm and Ng were very similar to those previously observed for other unstructured proteins (Supplementary Figures 2B and 2C). The resonance of both protein's methyl group protons (at 0.9 and 0.95 ppm) and amide groups (around 8.4 ppm), along with very limited spectral dispersion of these signals, indicated the lack of a stable tertiary structure in both Nm and Ng","type":"Results"},{"text":"Nm and Ng have a low percentage of order-promoting amino acids and high percentage of disorder-promoting amino acids (Supplementary table 1). The acidic pI and low hydrophobicity of these two proteins indicates that they are unfolded (See supplementary text). Besides, gel filtration chromatography and Dynamic Light Scattering experiments show the higher hydrodynamic radii and molecular weight for both Nm and Ng (See supplementary text). Thus, the biophysical studies on Nm and Ng support the classification of these proteins as intrinsically unstructured, lacking a compact globular fold, and having very little secondary structure27,28,29.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23462742","version":2,"reference_html":"Structural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with Calmodulin. <i> Kumar V, Chichili VP, Zhong L, Tang X, Velazquez-Campoy A, Sheu FS, Seetharaman J, Gerges NZ, Sivaraman J. </i> Sci Rep, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","validated":{"curator_id":"bmesza","timestamp":"2020-11-26T15:32:01.604Z","curator_name":"Bálint Mészáros"},"term_name":"pre-molten globule","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02342r010","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T15:49:41.948Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":57,"term_id":"GO:0005515","start":34,"version":4,"statement":[{"text":"ITC experiments revealed that the full-length Nm and Ng bind to apo CaM (in the absence of Ca2+) with a higher affinity than that to Ca2+/CaM. These observations are consistent with the previous fluorescence experiments1 (Table 1). Further, the ITC results show that NmIQ and NgIQ peptides have a similar affinity toward apo CaM as their full-length counterparts; thus, the IQ peptides almost mimic their full-length proteins. Nm and Ng interacted with CaM mainly through their IQ motifs with a stoichiometric ratio of 1[ratio]1.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P0DP26","partner_end":null}],"term_name":"protein binding","ec_name":"isothermal titration calorimetry evidence used in manual assertion","reference_html":"Structural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with Calmodulin. <i> Kumar V, Chichili VP, Zhong L, Tang X, Velazquez-Campoy A, Sheu FS, Seetharaman J, Gerges NZ, Sivaraman J. </i> Sci Rep, 2013","released":"2023_12","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"23462742","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"bmesza","curator_orcid":"0000-0003-0919-4449","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02342r011","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T15:49:45.487Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":57,"term_id":"GO:0005515","start":34,"version":4,"statement":[{"text":"Here, we report the structure of IQ peptides (24aa) of Nm/Ng complexed with CaM and their functional studies with full-length proteins. Nm/Ng and their respective IQ peptides are intrinsically unstructured; however, upon binding with CaM, IQ motifs adopt a helical conformation.","type":"Abstract"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P0DP26","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","reference_html":"Structural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with Calmodulin. <i> Kumar V, Chichili VP, Zhong L, Tang X, Velazquez-Campoy A, Sheu FS, Seetharaman J, Gerges NZ, Sivaraman J. </i> Sci Rep, 2013","released":"2023_12","term_ontology":"GO","curator_name":"Bálint Mészáros","reference_id":"23462742","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"bmesza","curator_orcid":"0000-0003-0919-4449","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02342r013","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T15:49:37.095Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":57,"term_id":"IDPO:0000013","start":34,"version":2,"statement":[{"text":"In summary, this is the first report of the crystal structure of the intrinsically unstructured, neuron-specific substrate proteins, Nm/Ng, as IQ peptides in complex with CaM. The unstructured IQ peptides (24 aa) interact with the C-lobe of CaM and gain an α-helical conformation","type":"Discussion"},{"text":"Nm/Ng and their respective IQ peptides are intrinsically unstructured; however, upon binding with CaM, IQ motifs adopt a helical conformation. Ser41 (Ser36) of Nm (Ng) is located in a negatively charged pocket in the apo CaM and, when phosphorylated, it will repel Nm/Ng from CaM","type":"Abstract"}],"term_name":"pre-molten globule to order","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2023_12","term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"23462742","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4E53"}],"term_namespace":"Structural transition","ec_id":"ECO:0005670","curator_id":"bmesza","reference_html":"Structural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with Calmodulin. <i> Kumar V, Chichili VP, Zhong L, Tang X, Velazquez-Campoy A, Sheu FS, Seetharaman J, Gerges NZ, Sivaraman J. </i> Sci Rep, 2013","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2023_12","uniref100":"UniRef100_P06837","date":"2019-11-11T11:20:25.539Z","acc":"P06837","name":"Neuromodulin","length":227,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000011D6","genes":[{"name":{"value":"Gap43"},"synonyms":[{"value":"Basp2"}]}],"alphafold_very_low_content":0.4185022026431718,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":33,"type":"D"},{"start":34,"end":57,"type":"T"},{"start":58,"end":227,"type":"D"}],"Structural state":[{"start":1,"end":227,"type":"D"}],"Biological process":[{"start":34,"end":57,"type":"F"}],"Molecular function":[{"start":34,"end":57,"type":"F"}],"Structural transition":[{"start":34,"end":57,"type":"T"}]}},{"features":{"gene3D":[{"start":233,"end":318,"id":"G3DSA:3.30.70.330","name":"G3DSA:3.30.70.330"}],"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":236,"end":313}]},"uniref50":"UniRef50_Q92804","sequence":"MSDSGSYGQSGGEQQSYSTYGNPGSQGYGQASQSYSGYGQTTDSSYGQNYSGYSSYGQSQSGYSQSYGGYENQKQSSYSQQPYNNQGQQQNMESSGSQGGRAPSYDQPDYGQQDSYDQQSGYDQHQGSYDEQSNYDQQHDSYSQNQQSYHSQRENYSHHTQDDRRDVSRYGEDNRGYGGSQGGGRGRGGYDKDGRGPMTGSSGGDRGGFKNFGGHRDYGPRTDADSESDNSDNNTIFVQGLGEGVSTDQVGEFFKQIGIIKTNKKTGKPMINLYTDKDTGKPKGEATVSFDDPPSAKAAIDWFDGKEFHGNIIKVSFATRRPEFMRGGGSGGGRRGRGGYRGRGGFQGRGGDPKSGDWVCPNPSCGNMNFARRNSCNQCNEPRPEDSRPSGGDFRGRGYGGERGYRGRGGRGGDRGGYGGDRSGGGYGGDRSSGGGYSGDRSGGGYGGDRSGGGYGGDRGGGYGGDRGGGYGGDRGGGYGGDRGGYGGDRGGGYGGDRGGYGGDRGGYGGDRGGYGGDRGGYGGDRSRGGYGGDRGGGSGYGGDRSGGYGGDRSGGGYGGDRGGGYGGDRGGYGGKMGGRNDYRNDQRNRPY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q92804","disprot_id":"DP02345","ncbi_taxon_id":9606,"regions_counter":5,"creator":"elamberti","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":354,"region_id":"DP02345r001","start":323,"term_id":"IDPO:0000002","statement":[{"text":"Architecturally, TAF15 is composed of an intrinsically unstructured N-terminal QGSY rich activation domain which is retained in the oncogenic fusions and possesses trans-activating properties, followed by a central and the C-terminal region comprising the RNA recognition motif (RRM) and a (Cys)4 RanBP2 type Zinc finger (ZnF) with interspersed unstructured elements rich in arginine and glycine, known as RGG motifs. The RRM exhibits highest degree of sequence conservation among the members of the FET family.","type":"Article"},{"text":"15N-{1H} Het-NOE values, corresponding to an average of ~0.75 in the RRM and ZnF domains, and ~0.38 in the RGG linker, indicated the presence of highly dynamic linker between the structured RRM and the RanBP2 type ZnF domain in the multi-domain protein","type":"Results"},{"text":"Moreover, random coil index analysis (RCI) of the backbone32 revealed the absence of any secondary structural elements between E323-K354, which constitute the RGG motif.","type":"Results"},{"text":"conclusively establish the predominant role played by RRM in mediating RNA binding and negate any significant contributions toward RNA recognition by the RGG motifs and the RanBP2 type zinc finger","type":"Results"},{"text":"Very few residues in the RGG motif (E323-R326 and G342), and the RanBP2 type zinc finger domain (S355, F370-R372) exhibited CSPs above the averaged CSP + 1σ (Fig. 2C). The CSPs in E323-R326 region can be explained from its existence as an extension of the C-terminal region of the RRM, which may provide additional contributions in stabilizing the complex. Despite these additional contributions, N- or C-terminal extensions in an RRM have been rarely shown to provide specificity in recognition","type":"Results"}],"curator_id":"fquaglia","released":"2022_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26612539","version":3,"reference_html":"Structural delineation of stem-loop RNA binding by human TAF15 protein. <i> Kashyap M, Ganguly AK, Bhavesh NS. </i> Sci Rep, 2015","date":"2022-06-28T07:55:30.897Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T12:14:44.332Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":354,"region_id":"DP02345r002","start":323,"term_id":"IDPO:0000033","statement":[{"text":"Architecturally, TAF15 is composed of an intrinsically unstructured N-terminal QGSY rich activation domain which is retained in the oncogenic fusions and possesses trans-activating properties, followed by a central and the C-terminal region comprising the RNA recognition motif (RRM) and a (Cys)4 RanBP2 type Zinc finger (ZnF) with interspersed unstructured elements rich in arginine and glycine, known as RGG motifs. The RRM exhibits highest degree of sequence conservation among the members of the FET family.","type":"Article"},{"text":"15N-{1H} Het-NOE values, corresponding to an average of ~0.75 in the RRM and ZnF domains, and ~0.38 in the RGG linker, indicated the presence of highly dynamic linker between the structured RRM and the RanBP2 type ZnF domain in the multi-domain protein","type":"Results"},{"text":"Moreover, random coil index analysis (RCI) of the backbone32 revealed the absence of any secondary structural elements between E323-K354, which constitute the RGG motif.","type":"Results"},{"text":"conclusively establish the predominant role played by RRM in mediating RNA binding and negate any significant contributions toward RNA recognition by the RGG motifs and the RanBP2 type zinc finger","type":"Results"},{"text":"Very few residues in the RGG motif (E323-R326 and G342), and the RanBP2 type zinc finger domain (S355, F370-R372) exhibited CSPs above the averaged CSP + 1σ (Fig. 2C). The CSPs in E323-R326 region can be explained from its existence as an extension of the C-terminal region of the RRM, which may provide additional contributions in stabilizing the complex. Despite these additional contributions, N- or C-terminal extensions in an RRM have been rarely shown to provide specificity in recognition","type":"Results"}],"curator_id":"fquaglia","released":"2022_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26612539","version":4,"reference_html":"Structural delineation of stem-loop RNA binding by human TAF15 protein. <i> Kashyap M, Ganguly AK, Bhavesh NS. </i> Sci Rep, 2015","date":"2022-06-28T07:55:36.855Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T12:14:45.819Z"}}],"released":"2020_12","uniref100":"UniRef100_Q92804","date":"2019-11-11T17:02:43.154Z","acc":"Q92804","name":"TATA-binding protein-associated factor 2N","length":592,"organism":"Homo sapiens","dataset":["Cancer-related proteins","Condensates-related proteins","RNA-binding proteins"],"UniParc":"UPI000013317D","genes":[{"name":{"value":"TAF15"},"synonyms":[{"value":"RBP56"},{"value":"TAF2N"}]}],"alphafold_very_low_content":0.7567567567567568,"disorder_content":0.05405405405405406,"disprot_consensus":{"full":[{"start":323,"end":354,"type":"D"}],"Structural state":[{"start":323,"end":354,"type":"D"}],"Disorder function":[{"start":323,"end":354,"type":"F"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF15320","name":"mRNA cap methylation, RNMT-activating mini protein","start":10,"end":87}]},"uniref50":"UniRef50_Q9BTL3","sequence":"MTDTAEAVPKFEEMFASRFTENDKEYQEYLKRPPESPPIVEEWNSRAGGNQRNRGNRLQDNRQFRGRDNRWGWPSDNRSNQWHGRSWGNNYPQHRQEPYYPQQYGHYGYNQRPPYGYY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9BTL3","disprot_id":"DP02346","ncbi_taxon_id":9606,"regions_counter":5,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":45,"region_id":"DP02346r001","start":2,"term_id":"IDPO:0000002","statement":[{"text":"The HSQC of the unbound RAM shows that the majority of backbone amide peaks lie within a narrow range of chemical shifts in the proton dimension (7.9-8.5 PPM). There are 3–5 peaks at lower 1H chemical shifts which may indicate some small region(s) of ordered structure. However, the signals broadened significantly in presence of RNMT, showing a wider range of chemical shifts. These data indicate that RAM 2–45 is likely to be flexible in solution, but stabilised by binding to RNMT.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27422871","version":2,"reference_html":"Molecular basis of RNA guanine-7 methyltransferase (RNMT) activation by RAM. <i> Varshney D, Petit AP, Bueren-Calabuig JA, Jansen C, Fletcher DA, Peggie M, Weidlich S, Scullion P, Pisliakov AV, Cowling VH. </i> Nucleic Acids Res, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":45,"region_id":"DP02346r002","start":2,"term_id":"IDPO:0000011","statement":[{"text":"The HSQC of the unbound RAM shows that the majority of backbone amide peaks lie within a narrow range of chemical shifts in the proton dimension (7.9-8.5 PPM). There are 3–5 peaks at lower 1H chemical shifts which may indicate some small region(s) of ordered structure. However, the signals broadened significantly in presence of RNMT, showing a wider range of chemical shifts. These data indicate that RAM 2–45 is likely to be flexible in solution, but stabilised by binding to RNMT.","type":"Results"},{"text":"RNMT - RAM interaction does not alter the RNMT core structure but stabilises RAM.","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27422871","version":2,"reference_html":"Molecular basis of RNA guanine-7 methyltransferase (RNMT) activation by RAM. <i> Varshney D, Petit AP, Bueren-Calabuig JA, Jansen C, Fletcher DA, Peggie M, Weidlich S, Scullion P, Pisliakov AV, Cowling VH. </i> Nucleic Acids Res, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"5E8J"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP02346r003","ec_ontology":"ECO","end":45,"term_id":"GO:0005515","start":2,"version":3,"statement":[{"text":"RAM 2–45 is likely to be flexible in solution, but stabilised by binding to RNMT.","type":"Results"},{"text":"RNMT - RAM interaction does not alter the RNMT core structure but stabilises RAM.","type":"Figure"},{"text":"RAM binds to the RNMT surface distal to the active site, resulting in stabilisation of a series of RNMT structures including a lobe which co-evolved with RAM in vertebrates.","type":"Introduction"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"O43148","partner_end":null}],"term_name":"protein binding","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"27422871","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5E8J"}],"term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"fquaglia","reference_html":"Molecular basis of RNA guanine-7 methyltransferase (RNMT) activation by RAM. <i> Varshney D, Petit AP, Bueren-Calabuig JA, Jansen C, Fletcher DA, Peggie M, Weidlich S, Scullion P, Pisliakov AV, Cowling VH. </i> Nucleic Acids Res, 2016","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":45,"region_id":"DP02346r004","start":2,"term_id":"GO:0140677","statement":[{"text":"RAM binds to the RNMT surface distal to the active site, resulting in stabilisation of a series of RNMT structures including a lobe which co-evolved with RAM in vertebrates.","type":"Introduction"},{"text":"RNMT also has an activating subunit, RAM (RNMT-activating miniprotein)","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"27422871","version":3,"reference_html":"Molecular basis of RNA guanine-7 methyltransferase (RNMT) activation by RAM. <i> Varshney D, Petit AP, Bueren-Calabuig JA, Jansen C, Fletcher DA, Peggie M, Weidlich S, Scullion P, Pisliakov AV, Cowling VH. </i> Nucleic Acids Res, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"5E8J"}],"term_name":"molecular function activator activity","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","uniref100":"UniRef100_Q9BTL3","date":"2019-11-12T14:41:04.160Z","acc":"Q9BTL3","name":"RNA guanine-N7 methyltransferase activating subunit","length":118,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000467E0","genes":[{"name":{"value":"RAMAC","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:31022","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:31022"}}]},"synonyms":[{"value":"C15orf18"},{"value":"FAM103A1"},{"value":"RAMMET"}]}],"alphafold_very_low_content":0.4491525423728814,"disorder_content":0.3728813559322034,"disprot_consensus":{"full":[{"start":2,"end":45,"type":"T"}],"Structural state":[{"start":2,"end":45,"type":"D"}],"Structural transition":[{"start":2,"end":45,"type":"T"}],"Molecular function":[{"start":2,"end":45,"type":"F"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF06047","name":"NF-kappa-B-activating protein C-terminal domain","start":308,"end":405},{"id":"PF15692","name":"NF-kappa-B-activating protein","start":121,"end":207}]},"uniref50":"UniRef50_Q8N5F7","sequence":"MAPVSGSRSPDREASGSGGRRRSSSKSPKPSKSARSPRGRRSRSHSCSRSGDRNGLTHQLGGLSQGSRNQSYRSRSRSRSRERPSAPRGIPFASASSSVYYGSYSRPYGSDKPWPSLLDKEREESLRQKRLSERERIGELGAPEVWGLSPKNPEPDSDEHTPVEDEEPKKSTTSASTSEEEKKKKSSRSKERSKKRRKKKSSKRKHKKYSEDSDSDSDSETDSSDEDNKRRAKKAKKKEKKKKHRSKKYKKKRSKKSRKESSDSSSKESQEEFLENPWKDRTKAEEPSDLIGPEAPKTLTSQDDKPLNYGHALLPGEGAAMAEYVKAGKRIPRRGEIGLTSEEIASFECSGYVMSGSRHRRMEAVRLRKENQIYSADEKRALASFNQEERRKRENKILASFREMVYRKTKGKDDK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q8N5F7","disprot_id":"DP02348","ncbi_taxon_id":9606,"regions_counter":11,"creator":"fquaglia","regions":[{"start":1,"end":328,"reference_id":"36867703","reference_source":"pmid","reference_html":"Regulation of 3' splice site selection after step 1 of splicing by spliceosomal C* proteins. <i> Dybkov O, Preußner M, El Ayoubi L, Feng VY, Harnisch C, Merz K, Leupold P, Yudichev P, Agafonov DE, Will CL, Girard C, Dienemann C, Urlaub H, Kastner B, Heyd F, Lührmann R. </i> Sci Adv, 2023","date":"2024-03-21T17:32:31.985Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"8C6J"},{"db":"EMDB","id":"16452"}],"region_id":"DP02348r007","statement":[{"text":"Tha Cryo-EM structure of the Human spliceosomal PM5 C* complex, shows this region is disordered.","type":"Curator statement"}]},{"start":1,"end":328,"reference_id":"30705154","reference_source":"pmid","reference_html":"A human postcatalytic spliceosome structure reveals essential roles of metazoan factors for exon ligation. <i> Fica SM, Oubridge C, Wilkinson ME, Newman AJ, Nagai K. </i> Science, 2019","date":"2024-03-21T17:34:08.614Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02348r008","statement":[{"text":"NKAP is a 415 residue protein implicated in T-cell development; it consists of highly charged repetitive sequences like Ser-Arg and poly-Lys and is expected to be intrinsically disordered through almost its entire length. However, residues 329-358 form a short helix that bridges the N- and C-terminal fragments of Slu7 bound to Prp8 and stabilizes the P complex.","type":"Results"},{"text":"The PDB structure is about the Human post-catalytic P complex spliceosome not of this protein in solution. ","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"6QDV"},{"db":"EMDB","id":"4525"}]},{"start":359,"end":415,"reference_id":"30705154","reference_source":"pmid","reference_html":"A human postcatalytic spliceosome structure reveals essential roles of metazoan factors for exon ligation. <i> Fica SM, Oubridge C, Wilkinson ME, Newman AJ, Nagai K. </i> Science, 2019","date":"2024-03-21T17:32:57.116Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"6QDV"},{"db":"EMDB","id":"4525"}],"region_id":"DP02348r009","statement":[{"text":"NKAP is a 415 residue protein implicated in T-cell development; it consists of highly charged repetitive sequences like Ser-Arg and poly-Lys and is expected to be intrinsically disordered through almost its entire length. However, residues 329-358 form a short helix that bridges the N- and C-terminal fragments of Slu7 bound to Prp8 and stabilizes the P complex.","type":"Results"},{"text":"The PDB structure is about the Human post-catalytic P complex spliceosome not of this protein in solution.","type":"Curator statement"}]},{"start":1,"end":328,"reference_id":"35705093","reference_source":"pmid","reference_html":"Mechanism of exon ligation by human spliceosome. <i> Zhan X, Lu Y, Zhang X, Yan C, Shi Y. </i> Mol Cell, 2022","date":"2024-03-21T17:31:50.220Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"EMDB","id":"32321"},{"db":"PDB","id":"7W5B"}],"region_id":"DP02348r010","statement":[{"text":"Table S2 shows the region 329-358 is the only one with electron density capable of being modeled. Indicating the rest of the protein is disordered in the cryo-EM structure of human C* complex.","type":"Curator statement"}]},{"start":359,"end":415,"reference_id":"35705093","reference_source":"pmid","reference_html":"Mechanism of exon ligation by human spliceosome. <i> Zhan X, Lu Y, Zhang X, Yan C, Shi Y. </i> Mol Cell, 2022","date":"2024-03-21T17:31:57.738Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"EMDB","id":"32321"},{"db":"PDB","id":"7W5B"}],"region_id":"DP02348r011","statement":[{"text":"Table S2 shows the region 329-358 is the only one with electron density capable of being modeled. Indicating the rest of the protein is disordered in the cryo-EM structure of human C* complex.","type":"Curator statement"}]}],"released":"2023_06","uniref100":"UniRef100_Q8N5F7","date":"2019-11-13T09:55:32.480Z","acc":"Q8N5F7","name":"NF-kappa-B-activating protein","length":415,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI000004A07B","genes":[{"name":{"value":"NKAP"}}],"alphafold_very_low_content":0.4072289156626506,"disorder_content":0.927710843373494,"disprot_consensus":{"full":[{"start":1,"end":328,"type":"D"},{"start":359,"end":415,"type":"D"}],"Structural state":[{"start":1,"end":328,"type":"D"},{"start":359,"end":415,"type":"D"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF05110","name":"AF-4 proto-oncoprotein N-terminal region","start":8,"end":520},{"id":"PF18875","name":"AF4 interaction motif","start":761,"end":775},{"id":"PF18876","name":"AFF4, C-terminal homology domain","start":949,"end":1209}]},"uniref50":"UniRef50_P51825","sequence":"MAAQSSLYNDDRNLLRIREKERRNQEAHQEKEAFPEKIPLFGEPYKTAKGDELSSRIQNMLGNYEEVKEFLSTKSHTHRLDASENRLGKPKYPLIPDKGSSIPSSSFHTSVHHQSIHTPASGPLSVGNISHNPKMAQPRTEPMPSLHAKSCGPPDSQHLTQDRLGQEGFGSSHHKKGDRRADGDHCASVTDSAPERELSPLISLPSPVPPLSPIHSNQQTLPRTQGSSKVHGSSNNSKGYCPAKSPKDLAVKVHDKETPQDSLVAPAQPPSQTFPPPSLPSKSVAMQQKPTAYVRPMDGQDQAPSESPELKPLPEDYRQQTFEKTDLKVPAKAKLTKLKMPSQSVEQTYSNEVHCVEEILKEMTHSWPPPLTAIHTPSTAEPSKFPFPTKDSQHVSSVTQNQKQYDTSSKTHSNSQQGTSSMLEDDLQLSDSEDSDSEQTPEKPPSSSAPPSAPQSLPEPVASAHSSSAESESTSDSDSSSDSESESSSSDSEENEPLETPAPEPEPPTTNKWQLDNWLTKVSQPAAPPEGPRSTEPPRRHPESKGSSDSATSQEHSESKDPPPKSSSKAPRAPPEAPHPGKRSCQKSPAQQEPPQRQTVGTKQPKKPVKASARAGSRTSLQGEREPGLLPYGSRDQTSKDKPKVKTKGRPRAAASNEPKPAVPPSSEKKKHKSSLPAPSKALSGPEPAKDNVEDRTPEHFALVPLTESQGPPHSGSGSRTSGCRQAVVVQEDSRKDRLPLPLRDTKLLSPLRDTPPPQSLMVKITLDLLSRIPQPPGKGSRQRKAEDKQPPAGKKHSSEKRSSDSSSKLAKKRKGEAERDCDNKKIRLEKEIKSQSSSSSSSHKESSKTKPSRPSSQSSKKEMLPPPPVSSSSQKPAKPALKRSRREADTCGQDPPKSASSTKSNHKDSSIPKQRRVEGKGSRSSSEHKGSSGDTANPFPVPSLPNGNSKPGKPQVKFDKQQADLHMREAKKMKQKAELMTDRVGKAFKYLEAVLSFIECGIATESESQSSKSAYSVYSETVDLIKFIMSLKSFSDATAPTQEKIFAVLCMRCQSILNMAMFRCKKDIAIKYSRTLNKHFESSSKVAQAPSPCIASTGTPSPLSPMPSPASSVGSQSSAGSVGSSGVAATISTPVTIQNMTSSYVTITSHVLTAFDLWEQAEALTRKNKEFFARLSTNVCTLALNSSLVDLVHYTRQGFQQLQELTKTP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P51825","disprot_id":"DP02349","ncbi_taxon_id":9606,"regions_counter":2,"creator":"fquaglia","regions":[{"region_id":"DP02349r002","unpublished":true,"ec_ontology":"ECO","end":760,"term_id":"IDPO:0000002","start":738,"version":2,"statement":[{"text":"1H-15N heteronuclear NOE experiments show that AF4 residues 761-775 are ordered in the complex whereas the remainder is flexible","type":"Results"},{"text":"The AF4-AF9 fusion included an N-terminal 6-his tag and TEV protease site, with the coding sequence for AF4 residues 738-779 directly fused to AF9 residues 490-568 in pET 32a","type":"Methods"}],"term_name":"disorder","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_06","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23260655","date":"2022-06-28T07:54:59.598Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2LM0"}],"term_namespace":"Structural state","ec_id":"ECO:0006204","curator_id":"fquaglia","reference_html":"Leukemia fusion target AF9 is an intrinsically disordered transcriptional regulator that recruits multiple partners via coupled folding and binding. <i> Leach BI, Kuntimaddi A, Schmidt CR, Cierpicki T, Johnson SA, Bushweller JH. </i> Structure, 2013","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T12:17:03.165Z"}}],"released":"2022_06","uniref100":"UniRef100_P51825","date":"2019-11-13T15:16:15.476Z","acc":"P51825","name":"AF4/FMR2 family member 1","length":1210,"organism":"Homo sapiens","dataset":["Cancer-related proteins"],"UniParc":"UPI0000125658","genes":[{"name":{"value":"AFF1"},"synonyms":[{"value":"AF4"},{"value":"FEL"},{"value":"MLLT2"},{"value":"PBM1"}]}],"alphafold_very_low_content":0.6834710743801653,"disorder_content":0.019008264462809916,"disprot_consensus":{"full":[{"start":738,"end":760,"type":"D"}],"Structural state":[{"start":738,"end":760,"type":"D"}]}},{"features":{"gene3D":[{"start":381,"end":543,"id":"G3DSA:2.60.34.10","name":"Substrate Binding Domain Of DNAk; Chain A, domain 1"},{"start":510,"end":619,"id":"G3DSA:1.20.1270.10","name":"G3DSA:1.20.1270.10"}],"pfam":[{"id":"PF00012","name":"Hsp70 protein","start":6,"end":611}]},"uniref50":"UniRef50_P0DMV8","sequence":"MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P0DMV8","disprot_id":"DP02353","ncbi_taxon_id":9606,"regions_counter":1,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":306,"region_id":"DP02353r001","start":229,"term_id":"IDPO:0000002","statement":[{"text":"Here, we describe a new crystal form of the human Hsp70 ATPase domain. The refined structure of this new crystal form is compared with that previously reported (Sriram et al., 1997) and provides evidence for the flexibility of the IIB subdomain of the structure, which corresponds to residues 229-306 (Flaherty et al., 1990)","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10216320","version":2,"reference_html":"Structure of a new crystal form of human Hsp70 ATPase domain. <i> Osipiuk J, Walsh MA, Freeman BC, Morimoto RI, Joachimiak A. </i> Acta Crystallogr D Biol Crystallogr, 1999","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","uniref100":"UniRef100_P0DMV8","date":"2019-11-13T16:52:59.413Z","acc":"P0DMV9","name":"Heat shock 70 kDa protein 1B","length":641,"organism":"Homo sapiens","dataset":["Stress response proteins"],"UniParc":"UPI0000000C40","genes":[{"name":{"value":"HSPA1B","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:5233","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:5233"}}]},"synonyms":[{"value":"HSP72","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"24318877","url":"http://www.ncbi.nlm.nih.gov/pubmed/24318877","alternativeUrl":"https://europepmc.org/abstract/MED/24318877"}}]}]}],"alphafold_very_low_content":0.0499219968798752,"disorder_content":0.12168486739469579,"disprot_consensus":{"full":[{"start":229,"end":306,"type":"D"}],"Structural state":[{"start":229,"end":306,"type":"D"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF04935","name":"Surfeit locus protein 6","start":199,"end":400},{"id":"PF15459","name":"60S ribosome biogenesis protein Rrp14","start":8,"end":58}]},"uniref50":"UniRef50_P36080","sequence":"MSNSLEERLRANSSAFDGLLALIPAKYYYDEKSQEQWKAKKKTKEQSKNDKLKKLDPEQRDDETSSTLEVMKKKEKDAKPVVLPGEKFKHMKMQKQKEATSKVEGDSDLNVEVNDPMIIAPDEDEEEEEDIKVIFDDEGNEIPLESKKDTTEPDRSVEKKSITEEEKLQRKKNLEALRSKLQAKISDMKSKRKAPGSREAILAQRKRKEELKKRKRLESEQEQDQDEIASDSDMEDIDSDLENNSKKRFKKGKKDSEINADGVMFQNIIFDDGARATSDLQRLRKAGRTKGPAKNDVKSHLKLLEAKKNKMEAKDELEQIKQKEKEKWQKAMLQAEGIKIRDDEKLLRKAIKRKEAQKRKSAIEWSERKRVVEDTISERQKRREENLRIRKDNKGKKRNKQEKMKRKYVGSAVPKKRAGFEGRLKTGKKKGGPK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P36080","disprot_id":"DP02355","ncbi_taxon_id":559292,"regions_counter":4,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":295,"region_id":"DP02355r001","start":1,"term_id":"IDPO:0000002","curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29512650","version":2,"reference_html":"Modular assembly of the nucleolar pre-60S ribosomal subunit. <i> Sanghai ZA, Miller L, Molloy KR, Barandun J, Hunziker M, Chaker-Margot M, Wang J, Chait BT, Klinge S. </i> Nature, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6C0F"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":434,"region_id":"DP02355r002","start":394,"term_id":"IDPO:0000002","curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29512650","version":2,"reference_html":"Modular assembly of the nucleolar pre-60S ribosomal subunit. <i> Sanghai ZA, Miller L, Molloy KR, Barandun J, Hunziker M, Chaker-Margot M, Wang J, Chait BT, Klinge S. </i> Nature, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6C0F"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2021_06","uniref100":"UniRef100_P36080","date":"2019-11-14T15:27:56.095Z","acc":"P36080","name":"Ribosomal RNA-processing protein 14","length":434,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000013B6FF","genes":[{"name":{"value":"RRP14"},"olnNames":[{"value":"YKL082C"}]}],"alphafold_very_low_content":0.16820276497695852,"disorder_content":0.7741935483870968,"disprot_consensus":{"full":[{"start":1,"end":295,"type":"D"},{"start":394,"end":434,"type":"D"}],"Structural state":[{"start":1,"end":295,"type":"D"},{"start":394,"end":434,"type":"D"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF04889","name":"Cwf15/Cwc15 cell cycle control protein","start":1,"end":264}]},"uniref50":"UniRef50_P78794","sequence":"MTTAHRPQFDPARGHSEMAPTRITSSRALPAHLKLKYRQESQGTEEEVRKQDLREALLRAEAAHFATQEHGASSEEVSQNSKLIEGFTSPSTDDKPNNDVEVDYQELLRQTLEADEDASDSDDSVDSSNKNSEVSIKRRKTESNSQESVDSSNSESSDEESDSEDETQQLLRELENIKQERKREQMLQEEKNRALEQEKREREIAFGNELLNKASSGSFQVKRRWDEDVVFRNTHKGVDDTPRPGFVNDMLRSEFHKKFLARFVD","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"uniref90":"UniRef90_P78794","disprot_id":"DP02356","ncbi_taxon_id":284812,"regions_counter":2,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":23,"region_id":"DP02356r001","start":1,"term_id":"IDPO:0000002","curator_id":"vnugnes","released":"2026_06","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"26292707","version":3,"reference_html":"Structure of a yeast spliceosome at 3.6-angstrom resolution. <i> Yan C, Hang J, Wan R, Huang M, Wong CC, Shi Y. </i> Science, 2015","date":"2026-01-07T14:13:04.310Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"3JB9"},{"db":"EMDB","id":"6413"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","disprot_namespace":"Structural state","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","statement":[{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":222,"region_id":"DP02356r002","start":71,"term_id":"IDPO:0000002","curator_id":"vnugnes","released":"2026_06","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"26292707","version":3,"reference_html":"Structure of a yeast spliceosome at 3.6-angstrom resolution. <i> Yan C, Hang J, Wan R, Huang M, Wong CC, Shi Y. </i> Science, 2015","date":"2026-01-07T14:12:45.882Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"3JB9"},{"db":"EMDB","id":"6413"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","disprot_namespace":"Structural state","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","statement":[{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"released":"2021_06","uniref100":"UniRef100_P78794","date":"2019-11-14T16:58:41.199Z","acc":"P78794","name":"Pre-mRNA-splicing factor cwf15","length":265,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","dataset":[],"UniParc":"UPI00001690EC","genes":[{"name":{"value":"cwf15"},"orfNames":[{"value":"SPBC337.06c"}]}],"alphafold_very_low_content":0.23773584905660378,"disorder_content":0.660377358490566,"disprot_consensus":{"full":[{"start":1,"end":23,"type":"D"},{"start":71,"end":222,"type":"D"}],"Structural state":[{"start":1,"end":23,"type":"D"},{"start":71,"end":222,"type":"D"}]}},{"features":{"gene3D":[{"start":1209,"end":1327,"id":"G3DSA:1.20.58.1750","name":"G3DSA:1.20.58.1750"},{"start":1785,"end":1945,"id":"G3DSA:3.30.420.230","name":"G3DSA:3.30.420.230"},{"start":1946,"end":2044,"id":"G3DSA:1.20.80.40","name":"G3DSA:1.20.80.40"}],"pfam":[{"id":"PF01398","name":"JAB1/Mov34/MPN/PAD-1 ubiquitin protease","start":2128,"end":2229},{"id":"PF08082","name":"PRO8NT (NUC069), PrP8 N-terminal domain","start":79,"end":229},{"id":"PF08083","name":"PROCN (NUC071) domain","start":419,"end":824},{"id":"PF08084","name":"PROCT (NUC072) domain","start":2239,"end":2360},{"id":"PF10596","name":"U6-snRNA interacting domain of PrP8","start":1466,"end":1624},{"id":"PF10597","name":"U5-snRNA binding site 2 of PrP8","start":1261,"end":1396},{"id":"PF10598","name":"RNA recognition motif of the spliceosomal PrP8","start":1009,"end":1099},{"id":"PF12134","name":"PRP8 domain IV core","start":1784,"end":2012}]},"uniref50":"UniRef50_O14187","sequence":"MASLPPGNPPPPPPPPGFEPPSQPPPPPPPGYVKKRKNKTPAQSGNLEKQLNERARKWRASQKSKFGVKRKQGYVQTEKADLPPEHLRKIMKDRGDMSSRKFRADKRSYLGALKYLPHAVLKLLENMPMPWEEYREVKVLYHVTGAITFVNESPRVIEPHFIAQWGTMWMMMRREKRDRKNFKRLRFPPFDDEEPPFSIDQLLDLEPLEAIRMDLDEEDDAPVMDWFYENKALEDTPHVNGPTYRRWKLNLPQMANLHRLGYQLLSDLRDDNYFYLFNDNSFFTAKALNVAIPGGPKFEPLYKDEAPEMEDWNEFNDIYKLIIRHPIKTEYRIAFPYLYNSRARSVALSEYHQPSNVFVPPEDPDLPAFFWDPIINPITSRQLTLHELDTSPEDSAIEEDPNFEIPFDPFFHSEDIEFEHTASALILLWAPHPFNKRSGATKRAQDVPLIKHWYLEHCPPNQPVKVRVSYQKLLKSHVMNKLHMAHPKSHTNRSLLRQLKNTKFFQSTSIDWVEAGLQVCRQGYNMLQLLIHRKGLTYLHLDYNCNLKPTKTLTTKERKKSRFGNAFHLMREILRLTKLIVDSHVQYRLGNIDAYQLADGLHYIFNHVGQLTGMYRYKYRLMRQIRACKDFKHLIYYRFNTGPVGKGPGCGFWAPSWRVWLFFLRGIVPLLERWLGNLLARQFEGRHSTGVAKQITKQRVDSHQDLELRAAVMNDILDMIPEGIRQGKSKTILQHLSEAWRCWKANIPWKVPGLPAPIENMILRYVKSKADWWTSVAHFNRERIRRGATVDKTVAKKNLGRLTRLWLKAEQERQHNYLKDGPYVTADEAVAIYTTFVHWLESRRFQPIPFPPLSYKHDTKLLVLALERLKEAYSVKGRLNQSQREELALVEQAYDNPHEMLSQIKRRLLTMRTFKEVGIEFMDMYSHLIPVYSVDPMEKICDAYLDQYLWFEADRRHLFPSWVKPSDSEPPPLLVYKWCQGINNLTDVWETSNGECNVLMETRLSKVFEKVDLTLLNRLMSLLMDTNLASYASAKNNVVLSYKDMSHTNSYGLVRGLQFSSFIWQFYGLVLDLLILGLQRATEIAGPADAPNDFLHFKDQATETSHPIRLYTRYIDKVYIMFRFTDEESRDLIQRFLNENPDPTNSNVVNYSKGKKNCWPRDARMRLMKHDVNLGRAVFWEIRNRLPRSLTTLEWEDTFPSVYSKDNPNLLFSMTGFEVRILPKIRQNEEFSLKDGVWNLTDNRTKQRTAQAFIRVTEDGINQFGNRIRQILMSSGSTTFTKIANKWNTALIALMTYYREAAISTPELLDLLVKCESKIQTRVKISLNSKMPSRFPPAVFYSPKELGGLGMLSMGHVLIPQSDLRWSKQTDTGITHFRSGMTTNGEHLIPNLYRYIQPWESEFIDSQRVWAEYAMKRQEALQQNRRLTLEDLEDSWDRGIPRINTLFQKDRHTLAYDKGWRVRTEFKQYQLLKNNPFWWTSQRHDGKLWQLNNYRVDVIQALGGVEGILEHTMFKATGFPSWEGLFWEKASGFEESMKFKKLTNAQRSGLNQIPNRRFTLWWSPTINRANVYVGFQVQLDLTGIMMHGKIPTLKISLIQIFRSHLWQKIHESVVWDLCQVLDQELESLQIETVQKETIHPRKSYKMNSSCADILLLAAYKWNVSRPSLLNDNRDVLDNTTTNKYWIDVQLRFGDYDSHDIERYTRAKFLDYSTDAQSMYPSPTGVLIGIDLCYNMHSAYGNWIPGMKPLIQQSMNKIMKANPALYVLRERIRKGLQLYASEPQEQYLSSSNYAELFSNQIQLFVDDTNVYRVTIHKTFEGNLTTKPINGAIFIFNPRTGQLFLKVIHTSVWAGQKRLGQLAKWKTAEEVAALIRSLPVEEQPRQIIVTRKGMLDPLEVHLLDFPNITIKGSELQLPFQAIIKLDKINDLILRATEPQMVLFNLYDDWLQSVSSYTAFSRLILILRALNVNTEKTKLILRPDKSIITKENHVWPNLDDQQWLDVEPKLRDLILADYAKKNNINVASLTNSEVRDIILGMTITAPSLQRQQIAEIEKQGRENAQVTAVTTKTTNVHGDEMVVTTTSAYENEKFSSKTEWRNRAISSISLPLRTKNIYVNSDNISETFPYTYILPQNLLRKFVTISDLRTQVAGYMYGKSPSDNPQIKEIRCIALVPQLGSIRNVQLPSKLPHDLQPSILEDLEPLGWIHTQSSELPYLSSVDVTTHAKILSSHPEWDTKAVTLTVSYIPGSISLAAYTVSKEGIEWGSKNMDINSDEAIGYEPSMAEKCQLLLSDRIQGFFLVPEEGVWNYNFNGASFSPKMTYSLKLDVPLPFFALEHRPTHVISYTELETNDRLEEDMPDAFA","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"uniref90":"UniRef90_O14187","disprot_id":"DP02357","ncbi_taxon_id":284812,"regions_counter":5,"creator":"fquaglia","regions":[{"region_id":"DP02357r001","ec_ontology":"ECO","end":46,"term_id":"IDPO:0000002","start":1,"version":4,"statement":[{"text":"Except for the N-terminal 46 amino acids and the C-terminal Jab1/MPN domain, most of the Spp42 sequences have a well-defined EM density (fig. S10, A to H, and fig. S11A).","type":"Abstract"}],"term_name":"disorder","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26292707","date":"2026-01-07T14:13:34.399Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3JB9"},{"db":"EMDB","id":"6413"}],"term_namespace":"Structural state","ec_id":"ECO:0006224","curator_id":"fquaglia","reference_html":"Structure of a yeast spliceosome at 3.6-angstrom resolution. <i> Yan C, Hang J, Wan R, Huang M, Wong CC, Shi Y. </i> Science, 2015","ec_go":"IDA","disprot_namespace":"Structural state","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-01-07T14:13:36.624Z"}},{"region_id":"DP02357r002","ec_ontology":"ECO","end":2363,"term_id":"IDPO:0000002","start":2044,"version":5,"statement":[{"text":"Except for the N-terminal 46 amino acids and the C-terminal Jab1/MPN domain, most of the Spp42 sequences have a well-defined EM density (fig. S10, A to H, and fig. S11A).","type":"Abstract"},{"text":"The Jab1/MPN domain (residues 2044 to 2363) is disordered","type":"Figure"},{"text":"The Jab1/MPN domain, responsible for binding the ATPase/helicase Brr2 (17, 18), is flexible and disordered in our structure.","type":"Article"}],"term_name":"disorder","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26292707","date":"2026-01-07T14:13:49.783Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3JB9"},{"db":"EMDB","id":"6413"}],"term_namespace":"Structural state","ec_id":"ECO:0006224","curator_id":"fquaglia","reference_html":"Structure of a yeast spliceosome at 3.6-angstrom resolution. <i> Yan C, Hang J, Wan R, Huang M, Wong CC, Shi Y. </i> Science, 2015","ec_go":"IDA","disprot_namespace":"Structural state","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-01-07T14:13:51.850Z"}}],"released":"2020_12","uniref100":"UniRef100_O14187","date":"2019-11-15T11:21:40.948Z","acc":"O14187","name":"Pre-mRNA-splicing factor spp42","length":2363,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","dataset":[],"UniParc":"UPI000006A413","genes":[{"name":{"value":"spp42"},"synonyms":[{"value":"cwf6"}],"orfNames":[{"value":"SPAC4F8.12c"}]}],"alphafold_very_low_content":0.04274227676682184,"disorder_content":0.15488785442234448,"disprot_consensus":{"full":[{"start":1,"end":46,"type":"D"},{"start":2044,"end":2363,"type":"D"}],"Structural state":[{"start":1,"end":46,"type":"D"},{"start":2044,"end":2363,"type":"D"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF01480","name":"PWI domain","start":46,"end":115}]},"uniref50":"UniRef50_Q8IYB3","sequence":"MDAGFFRGTSAEQDNRFSNKQKKLLKQLKFAECLEKKVDMSKVNLEVIKPWITKRVTEILGFEDDVVIEFIFNQLEVKNPDSKMMQINLTGFLNGKNAREFMGELWPLLLSAQENIAGIPSAFLELKKEEIKQRQIEQEKLASMKKQDEDKDKRDKEEKESSREKRERSRSPRRRKSRSPSPRRRSSPVRRERKRSHSRSPRHRTKSRSPSPAPEKKEKTPELPEPSVKVKEPSVQEATSTSDILKVPKPEPIPEPKEPSPEKNSKKEKEKEKTRPRSRSRSKSRSRTRSRSPSHTRPRRRHRSRSRSYSPRRRPSPRRRPSPRRRTPPRRMPPPPRHRRSRSPVRRRRRSSASLSGSSSSSSSSRSRSPPKKPPKRTSSPPRKTRRLSPSASPPRRRHRPSPPATPPPKTRHSPTPQQSNRTRKSRVSVSPGRTSGKVTKHKGTEKRESPSPAPKPRKVELSESEEDKGGKMAAADSVQQRRQYRRQNQQSSSDSGSSSSSEDERPKRSHVKNGEVGRRRRHSPSRSASPSPRKRQKETSPRGRRRRSPSPPPTRRRRSPSPAPPPRRRRTPTPPPRRRTPSPPPRRRSPSPRRYSPPIQRRYSPSPPPKRRTASPPPPPKRRASPSPPPKRRVSHSPPPKQRSSPVTKRRSPSLSSKHRKGSSPSRSTREARSPQPNKRHSPSPRPRAPQTSSSPPPVRRGASSSPQRRQSPSPSTRPIRRVSRTPEPKKIKKAASPSPQSVRRVSSSRSVSGSPEPAAKKPPAPPSPVQSQSPSTNWSPAVPVKKAKSPTPSPSPPRNSDQEGGGKKKKKKKDKKHKKDKKHKKHKKHKKEKAVAAAAAAAVTPAAIAAATTTLAQEEPVAAPEPKKETESEAEDNLDDLEKHLREKALRSMRKAQVSPQS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q8IYB3","disprot_id":"DP02359","ncbi_taxon_id":9606,"regions_counter":6,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":31,"region_id":"DP02359r001","start":1,"term_id":"IDPO:0000002","curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29361316","version":2,"reference_html":"Structure and Conformational Dynamics of the Human Spliceosomal Bact Complex. <i> Haselbach D, Komarov I, Agafonov DE, Hartmuth K, Graf B, Dybkov O, Urlaub H, Kastner B, Lührmann R, Stark H. </i> Cell, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6FF4"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":904,"region_id":"DP02359r002","start":127,"term_id":"IDPO:0000002","curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29361316","version":2,"reference_html":"Structure and Conformational Dynamics of the Human Spliceosomal Bact Complex. <i> Haselbach D, Komarov I, Agafonov DE, Hartmuth K, Graf B, Dybkov O, Urlaub H, Kastner B, Lührmann R, Stark H. </i> Cell, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6FF4"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Biological process","ec_ontology":"ECO","end":350,"region_id":"DP02359r004","start":300,"term_id":"GO:0051179","statement":[{"text":"Dissecting the N-terminal domain further showed that SRm160300–350 was sufficient to target EGFP to the paraspeckle region adjacent to speckled domains","type":"Figure"},{"text":"Amino acids 300–350 targeted SRm160 to sites on the nuclear matrix and peripheral to speckled domains. EGFP-SRm160300–350 was transiently expressed in HeLa cells. EGFP-SRm160300–350 (A) in fixed cells was concentrated in and around speckled domains (overlay, C) as visualized by the B1C8 antibody for SRm160 (B) but was also visible in nucleoli. (D) EGFP-SRm300300–350 remained bound after the removal of soluble proteins and chromatin in a nuclear matrix preparation.","type":"Figure"},{"text":"amino acids 300–350, although necessary for targeting the SRm160 N terminus to speckled domains, were inefficient in anchoring the EGFP fusion protein to speckled domains.","type":"Results"},{"text":"Using a series of FLAG- and enhanced GFP-conjugated deletion mutants we found two contiguous sequences that independently target SRm160 to nuclear matrix sites at splicing speckled domains: amino acids 300–350 and 351–688. Constructs containing amino acids 300–350 were also targeted to sites peripheral to speckled domains where most mRNA originate subsequent to splicing. Sequences from the N-terminal domain localized proteins to the nuclear lamina near sites where mRNA leaves the nucleus.","type":"Abstract"},{"text":"In this study we identified domains of SRm160 important for spatial targeting within the nucleus and for binding to the nuclear matrix.","type":"Abstract"},{"text":"The spatial targeting and nuclear matrix binding domains of SRm160.","type":"Title"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"immunodetection assay evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"12624182","version":3,"reference_html":"The spatial targeting and nuclear matrix binding domains of SRm160. <i> Wagner S, Chiosea S, Nickerson JA. </i> Proc Natl Acad Sci U S A, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","term_name":"localization","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"term_namespace":"Biological process","ec_ontology":"ECO","end":688,"region_id":"DP02359r005","start":351,"term_id":"GO:0051179","statement":[{"text":"We have identified the sequences within the splicing coactivator SRm160 that target it to the splicing factor-rich, speckled domains of the nucleus. These consist of two contiguous sequence domains of SRm160: amino acids 300–350 and 351–688. Both sequences are characterized by an unusual high content of arginine, proline, and serine: 88% for SRm160300–350 and 64% for SRm160351–688.","type":"Discussion"},{"text":"Using a series of FLAG- and enhanced GFP-conjugated deletion mutants we found two contiguous sequences that independently target SRm160 to nuclear matrix sites at splicing speckled domains: amino acids 300–350 and 351–688. ","type":"Abstract"},{"text":"In this study we identified domains of SRm160 important for spatial targeting within the nucleus and for binding to the nuclear matrix.","type":"Abstract"},{"text":"The spatial targeting and nuclear matrix binding domains of SRm160.","type":"Title"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"immunodetection assay evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"12624182","version":3,"reference_html":"The spatial targeting and nuclear matrix binding domains of SRm160. <i> Wagner S, Chiosea S, Nickerson JA. </i> Proc Natl Acad Sci U S A, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","term_name":"localization","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":151,"end":377,"reference_id":"39558160","reference_source":"pmid","reference_html":"Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation. <i> Niedner-Boblenz A, Monecke T, Hennig J, Klostermann M, Hofweber M, Davydova E, Gerber AP, Anosova I, Mayer W, Müller M, Heym RG, Janowski R, Paillart JC, Dormann D, Zarnack K, Sattler M, Niessing D. </i> Nucleic Acids Res, 2024","date":"2025-06-23T16:32:03.799Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000244","ec_ontology":"ECO","ec_name":"combinatorial evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"interaction_partner":[{"db":"ChEBI","id":"33697","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02359r006","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Total HeLa cell RNA"}]}],"statement":[{"text":"To test whether this SRRM1 fragment undergoes RNA-dependent phase separation, we performed titration experiments with total HeLa cell RNA followed by microscopic analyses. At protein/RNA ratios of 0.25 and 0.5, formation of condensates was observed at protein concentrations of 2.5–30 μM SRRM1 (Figure ​7A and B). Also, in the inverse experiment, a titration of increasing amounts of RNA at a given SRRM1 concentration of 10 μM resulted in robust condensate formation (Figure  7C). These findings were cross-validated in centrifugation sedimentation experiments (Figure ​7D). In none of the experiments, condensate formation or sedimentation was observed in the absence of RNA, demonstrating that SRRM1 is capable of RNA-dependent phase separation as observed for Loc1p.\n","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2021_06","uniref100":"UniRef100_Q8IYB3","date":"2019-11-21T16:04:26.592Z","acc":"Q8IYB3","name":"Serine/arginine repetitive matrix protein 1","length":904,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000074292","genes":[{"name":{"value":"SRRM1"},"synonyms":[{"value":"SRM160"}]}],"alphafold_very_low_content":0.672566371681416,"disorder_content":0.8949115044247787,"disprot_consensus":{"full":[{"start":1,"end":31,"type":"D"},{"start":127,"end":904,"type":"D"}],"Structural state":[{"start":1,"end":31,"type":"D"},{"start":127,"end":904,"type":"D"}],"Biological process":[{"start":300,"end":688,"type":"F"}],"Molecular function":[{"start":151,"end":377,"type":"F"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF05835","name":"Synaphin protein","start":1,"end":132}]},"uniref50":"UniRef50_O14810","sequence":"MEFVMKQALGGATKDMGKMLGGDEEKDPDAAKKEEERQEALRQAEEERKAKYAKMEAEREAVRQGIRDKYGIKKKEEREAEAQAAMEANSEGSLTRPKKAIPPGCGDEVEEEDESILDTVIKYLPGPLQDMLKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O14810","disprot_id":"DP02360","ncbi_taxon_id":9606,"regions_counter":1,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":83,"region_id":"DP02360r001","start":74,"term_id":"IDPO:0000002","statement":[{"text":"We next co-crystallized SNAREΔ60 with a CPX fragment (scCPX) consisting of its central and accessory helices (residues 26–83) and containing three “superclamp” mutations (D27L, E34F, R37A) that increase its clamping efficiency both in vitro19 and in vivo38. The structure was determined at 3.5 Å resolution using the truncated SNARE complex as a search model in the molecular replacement method (Table 1), and CPX was modeled into difference electron density. The final model includes residues 190–250 of syntaxin1, 10–74 and 141–203 of SNAP25, 29–60 of VAMP2, and 26–73 of CPX","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21785414","version":2,"reference_html":"Complexin cross-links prefusion SNAREs into a zigzag array. <i> Kümmel D, Krishnakumar SS, Radoff DT, Li F, Giraudo CG, Pincet F, Rothman JE, Reinisch KM. </i> Nat Struct Mol Biol, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3RL0"},{"db":"PDB","id":"3RK3"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T09:29:43.300Z"}}],"released":"2020_12","uniref100":"UniRef100_O14810","date":"2019-11-21T16:26:12.711Z","acc":"O14810","name":"Complexin-1","length":134,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI0000127BB3","genes":[{"name":{"value":"CPLX1"}}],"alphafold_very_low_content":0.04477611940298507,"disorder_content":0.07462686567164178,"disprot_consensus":{"full":[{"start":74,"end":83,"type":"D"}],"Structural state":[{"start":74,"end":83,"type":"D"}]}},{"features":{"gene3D":[{"start":350,"end":457,"id":"G3DSA:1.20.58.120","name":"BAG domain"}],"pfam":[{"id":"PF02179","name":"BAG domain","start":385,"end":455}]},"uniref50":"UniRef50_O95429","sequence":"MSALRRSGYGPSDGPSYGRYYGPGGGDVPVHPPPPLYPLRPEPPQPPISWRVRGGGPAETTWLGEGGGGDGYYPSGGAWPEPGRAGGSHQEQPPYPSYNSNYWNSTARSRAPYPSTYPVRPELQGQSLNSYTNGAYGPTYPPGPGANTASYSGAYYAPGYTQTSYSTEVPSTYRSSGNSPTPVSRWIYPQQDCQTEAPPLRGQVPGYPPSQNPGMTLPHYPYGDGNRSVPQSGPTVRPQEDAWASPGAYGMGGRYPWPSSAPSAPPGNLYMTESTSPWPSSGSPQSPPSPPVQQPKDSSYPYSQSDQSMNRHNFPCSVHQYESSGTVNNDDSDLLDSQVQYSAEPQLYGNATSDHPNNQDQSSSLPEECVPSDESTPPSIKKIIHVLEKVQYLEQEVEEFVGKKTDKAYWLLEEMLTKELLELDSVETGGQDSVRQARKEAVCKIQAILEKLEKKGL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_O95429","disprot_id":"DP02361","ncbi_taxon_id":9606,"regions_counter":1,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":376,"region_id":"DP02361r001","start":357,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Chemical shift distribution and local flexibility of the construct. The upper panel shows the chemical shift distribution for Cα and Cβ as determined by Eq. 1. Positive values are indicators for α‐helical secondary structure. The lower panel shows the ratio of T 1/T 2 15N relaxation times as a measure for local flexibility. Lower values indicate higher flexibility.","type":"Figure"},{"text":"The green box shows the N‐terminal unstructured region present in our construct","type":"Figure"},{"text":"The N‐terminus G353–T376 of our construct is unstructured as indicated by the lower T 1/T 2 ratios measured from the relaxation rates (Fig. 2). Furthermore, these residues do not show any long‐range NOEs. This demonstrates that the N‐terminus of our construct does not belong to the BAG domain of SODD and its presence does not induce a shift of helix 1 to a position suggested by the original sequence alignment.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14759524","version":2,"reference_html":"The solution structure of the SODD BAG domain reveals additional electrostatic interactions in the HSP70 complexes of SODD subfamily BAG domains. <i> Brockmann C, Leitner D, Labudde D, Diehl A, Sievert V, Büssow K, Kühne R, Oschkinat H. </i> FEBS Lett, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"1M7K"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-12T13:50:28.761Z"}}],"released":"2023_12","uniref100":"UniRef100_O95429","date":"2019-11-21T16:55:59.041Z","acc":"O95429","name":"BAG family molecular chaperone regulator 4","length":457,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000126769","genes":[{"name":{"value":"BAG4"},"synonyms":[{"value":"SODD"}]}],"alphafold_very_low_content":0.6083150984682714,"disorder_content":0.0437636761487965,"disprot_consensus":{"full":[{"start":357,"end":376,"type":"D"}],"Structural state":[{"start":357,"end":376,"type":"D"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MADLANEEKPAIAPPVFVFQKDKGQKRSAGGSSPEGGEDSDREDGNYCPPVKRERTSSLTQFPPSQSEERSSGFRLKPPTLIHGQAPSAGLPSQKPKEQQRSVLRPAVLQAPQPKALSQTVPSSGTNGVSLPADCTGAVPAASPDTAAWRSPSEAADEVCALEEKEPQKNESSNASEEEACEKKDPATQQAFVFGQNLRDRVKLINESVDEADMENAGHPSADTPTATNYFLQYISSSLENSTNSADASSNKFVFGQNMSERVLSPPKLNEVSSDANRENAAAESGSESSSQEATPEKESLAESAAAYTKATARKCLLEKVEVITGEEAESNVLQMQCKLFVFDKTSQSWVERGRGLLRLNDMASTDDGTLQSRLVMRTQGSLRLILNTKLWAQMQIDKASEKSIRITAMDTEDQGVKVFLISASSKDTGQLYAALHHRILALRSRVEQEQEAKMPAPEPGAAPSNEEDDSDDDDVLAPSGATAAGAGDEGDGQTTGST","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"","disprot_id":"DP02364","ncbi_taxon_id":9606,"regions_counter":2,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":45,"region_id":"DP02364r001","start":31,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"N-terminally GST-tagged RanBP3 NLS (human, isoform 3, also known as RanBP3-b, residues 31–60; UniProt code, Q9H6Z4)","type":"Methods"},{"text":"Residues 46–59 of RanBP3 bound to the major NLS-binding site in an extended conformation were identified unambiguously in the electron density map (Fig. 1A). The other residues of RanBP3 did not have defined electron density, indicating that these residues were disordered in the crystal.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28760339","version":2,"reference_html":"Crystal structure of importin-α3 bound to the nuclear localization signal of Ran-binding protein 3. <i> Koyama M, Matsuura Y. </i> Biochem Biophys Res Commun, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5XZX"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2023_12","uniref100":"","date":"2019-11-22T10:15:21.086Z","acc":"Q9H6Z4-3","name":"Isoform 3 of Ran-binding protein 3","length":499,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00002031A7","genes":[{"name":{"value":"RANBP3"}}],"disorder_content":0.03006012024048096,"disprot_consensus":{"full":[{"start":31,"end":45,"type":"D"}],"Structural state":[{"start":31,"end":45,"type":"D"}]}},{"features":{"gene3D":[{"start":1119,"end":1225,"id":"G3DSA:2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"}],"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":76,"end":338},{"id":"PF08912","name":"Rho Binding","start":948,"end":1014},{"id":"PF25346","name":"MRCK kinase PH domain","start":1121,"end":1202}]},"uniref50":"UniRef50_Q13464","sequence":"MSTGDSFETRFEKMDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNFLSRYKDTINKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFPDDNDISKEAKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDLEEDKGEEETFPIPKAFVGNQLPFVGFTYYSNRRYLSSANPNDNRTSSNADKSLQESLQKTIYKLEEQLHNEMQLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLESTVSQIEKEKMLLQHRINEYQRKAEQENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKLSQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQLESLNRELQERNRILENSKSQTDKDYYQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLNHSEKEKNNLEIDLNYKLKSLQQRLEQEVNEHKVTKARLTDKHQSIEEAKSVAMCEMEKKLKEEREAREKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKERMEDEVKNLTLQLEQESNKRLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMRELQDQLEAEQYFSTLYKTQVKELKEEIEEKNRENLKKIQELQNEKETLATQLDLAETKAESEQLARGLLEEQYFELTQESKKAASRNRQEITDKDHTVSRLEEANSMLTKDIEILRRENEELTEKMKKAEEEYKLEKEEEISNLKAAFEKNINTERTLKTQAVNKLAEIMNRKDFKIDRKKANTQDLRKKEKENRKLQLELNQEREKFNQMVVKHQKELNDMQAQLVEECAHRNELQMQLASKESDIEQLRAKLLDLSDSTSVASFPSADETDGNLPESRIEGWLSVPNRGNIKRYGWKKQYVVVSSKKILFYNDEQDKEQSNPSMVLDIDKLFHVRPVTQGDVYRAETEEIPKIFQILYANEGECRKDVEMEPVQQAEKTNFQNHKGHEFIPTLYHFPANCDACAKPLWHVFKPPPALECRRCHVKCHRDHLDKKEDLICPCKVSYDVTSARDMLLLACSQDEQKKWVTHLVKKIPKNPPSGFVRASPRTLSTRSTANQSFRKVVKNTSGKTS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q13464","disprot_id":"DP02365","ncbi_taxon_id":9606,"regions_counter":3,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":913,"region_id":"DP02365r001","start":895,"term_id":"IDPO:0000002","statement":[{"text":"However, unlike our previous structure of the Rock SBD, residues 895–913 were disordered","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27758857","version":2,"reference_html":"Structure of the Shroom-Rho Kinase Complex Reveals a Binding Interface with Monomeric Shroom That Regulates Cell Morphology and Stimulates Kinase Activity. <i> Zalewski JK, Mo JH, Heber S, Heroux A, Gardner RG, Hildebrand JD, VanDemark AP. </i> J Biol Chem, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5F5P"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","uniref100":"UniRef100_Q13464","date":"2019-11-22T14:56:21.953Z","acc":"Q13464","name":"Rho-associated protein kinase 1","length":1354,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000006F0A4","genes":[{"name":{"value":"ROCK1"}}],"alphafold_very_low_content":0.08567208271787297,"disorder_content":0.014032496307237814,"disprot_consensus":{"full":[{"start":895,"end":913,"type":"D"}],"Structural state":[{"start":895,"end":913,"type":"D"}]}},{"features":{"gene3D":[{"start":299,"end":486,"id":"G3DSA:3.80.10.10","name":"Ribonuclease Inhibitor"}],"pfam":[{"id":"PF02205","name":"WH2 motif","start":572,"end":597},{"id":"PF03250","name":"Tropomodulin","start":13,"end":85},{"id":"PF27087","name":"TMOD/LMOD Leucine-rich domain","start":319,"end":472}]},"uniref50":"UniRef50_P29536","sequence":"MSRVAKYRRQVSEDPDIDSLLETLSPEEMEELEKELDVVDPDGSVPVGLRQRNQTEKQSTGVYNREAMLNFCEKETKKLMQREMSMDESKQVETKTDAKNGEERGRDASKKALGPRRDSDLGKEPKRGGLKKSFSRDRDEAGGKSGEKPKEEKIIRGIDKGRVRAAVDKKEAGKDGRGEERAVATKKEEEKKGSDRNTGLSRDKDKKREEMKEVAKKEDDEKVKGERRNTDTRKEGEKMKRAGGNTDMKKEDEKVKRGTGNTDTKKDDEKVKKNEPLHEKEAKDDSKTKTPEKQTPSGPTKPSEGPAKVEEEAAPSIFDEPLERVKNNDPEMTEVNVNNSDCITNEILVRFTEALEFNTVVKLFALANTRADDHVAFAIAIMLKANKTITSLNLDSNHITGKGILAIFRALLQNNTLTELRFHNQRHICGGKTEMEIAKLLKENTTLLKLGYHFELAGPRMTVTNLLSRNMDKQRQKRLQEQRQAQEAKGEKKDLLEVPKAGAVAKGSPKPSPQPSPKPSPKNSPKKGGAPAAPPPPPPPLAPPLIMENLKNSLSPATQRKMGDKVLPAQEKNSRDQLLAAIRSSNLKQLKKVEVPKLLQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P29536","disprot_id":"DP02368","ncbi_taxon_id":9606,"regions_counter":1,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":313,"region_id":"DP02368r001","start":299,"term_id":"IDPO:0000002","statement":[{"text":"The structure of Lmod1ABS2, the strongest nucleator among the naturally occurring ABS2s analysed here , was determined at 1.54 Å resolution , and shows residues Ala-314 to Gln-486","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26370058","version":2,"reference_html":"How Leiomodin and Tropomodulin use a common fold for different actin assembly functions. <i> Boczkowska M, Rebowski G, Kremneva E, Lappalainen P, Dominguez R. </i> Nat Commun, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4Z79"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","uniref100":"UniRef100_P29536","date":"2019-11-26T15:07:25.992Z","acc":"P29536","name":"Leiomodin-1","length":600,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012E775","genes":[{"name":{"value":"LMOD1"}}],"alphafold_very_low_content":0.43,"disorder_content":0.025,"disprot_consensus":{"full":[{"start":299,"end":313,"type":"D"}],"Structural state":[{"start":299,"end":313,"type":"D"}]}},{"features":{"gene3D":[{"start":614,"end":744,"id":"G3DSA:2.60.120.40","name":"G3DSA:2.60.120.40"}],"pfam":[{"id":"PF00386","name":"C1q domain","start":617,"end":741},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":159,"end":207},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":469,"end":527}]},"uniref50":"UniRef50_P27658","sequence":"MAVPPRPLQLLGILFIISLNSVRLIQAGAYYGIKPLPPQIPPQIPPQIPQYQPLGQQVPHMPLGKDGLSMGKEMPHMQYGKEYPHLPQYMKEIPPVPRMGKEVVPKKGKGEVPLASLRGEQGPRGEPGPRGPPGPPGLPGHGMPGIKGKPGPQGYPGIGKPGMPGMPGKPGAMGMPGAKGEIGPKGEIGPMGIPGPQGPPGPHGLPGIGKPGGPGLPGQPGAKGERGPKGPPGPPGLQGPKGEKGFGMPGLPGLKGPPGMHGPPGPVGLPGVGKPGVTGFPGPQGPLGKPGPPGEPGPQGLIGVPGVQGPPGMPGVGKPGQDGIPGQPGFPGGKGEQGLPGLPGPPGLPGVGKPGFPGPKGDRGIGGVPGVLGPRGEKGPIGAPGMGGPPGEPGLPGIPGPMGPPGAIGFPGPKGEGGVVGPQGPPGPKGEPGLQGFPGKPGFLGEVGPPGMRGLPGPIGPKGEGGHKGLPGLPGVPGLLGPKGEPGIPGDQGLQGPPGIPGIVGPSGPIGPPGIPGPKGEPGLPGPPGFPGVGKPGVAGLHGPPGKPGALGPQGQPGLPGPPGPPGPPGPPAVMPTPSPQGEYLPDMGLGIDGVKPPHAYAGKKGKHGGPAYEMPAFTAELTVPFPPVGAPVKFDKLLYNGRQNYNPQTGIFTCEVPGVYYFAYHVHCKGGNVWVALFKNNEPMMYTYDEYKKGFLDQASGSAVLLLRPGDQVFLQMPSEQAAGLYAGQYVHSSFSGYLLYPM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P27658","disprot_id":"DP02369","ncbi_taxon_id":10090,"regions_counter":1,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":612,"region_id":"DP02369r001","start":570,"term_id":"IDPO:0000002","statement":[{"text":"Residues 613–743 of each crystallographically independent chain have clear and continuous density, whereas the N-terminal 42 residues and the His6 tag are invisible and presumed disordered.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12782141","version":2,"reference_html":"Crystal structure of the collagen alpha1(VIII) NC1 trimer. <i> Kvansakul M, Bogin O, Hohenester E, Yayon A. </i> Matrix Biol, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1O91"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","uniref100":"UniRef100_Q00780","date":"2019-11-26T15:24:09.528Z","acc":"Q00780","name":"Collagen alpha-1(VIII) chain","length":744,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000161D30","genes":[{"name":{"value":"Col8a1"}}],"alphafold_very_low_content":0.40053763440860213,"disorder_content":0.05779569892473118,"disprot_consensus":{"full":[{"start":570,"end":612,"type":"D"}],"Structural state":[{"start":570,"end":612,"type":"D"}]}},{"features":{"gene3D":[{"start":91,"end":191,"id":"G3DSA:3.30.70.330","name":"G3DSA:3.30.70.330"}],"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":107,"end":175},{"id":"PF13865","name":"C-terminal duplication domain of Friend of PRMT1","start":198,"end":251}]},"uniref50":"UniRef50_O08583","sequence":"MADKMDMSLDDIIKLNRSQRGGRGGGRGRGRAGSQGGRGGAVQAAARVNRGGGPMRNRPAIARGAAGGGRNRPAPYSRPKQLPDKWQHDLFDSGFGGGAGVETGGKLLVSNLDFGVSDADIQELFAEFGTLKKAAVHYDRSGRSLGTADVHFERKADALKAMKQYNGVPLDGRPMNIQLVTSQIDTQRRPAQSINRGGMTRNRGSGGFGGGGTRRGTRGGSRGRGRGTGRNSKQQLSAEELDAQLDAYNARMDTS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_O08583","disprot_id":"DP02371","ncbi_taxon_id":10090,"regions_counter":6,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":104,"region_id":"DP02371r001","start":77,"term_id":"IDPO:0000002","statement":[{"text":"The N-terminal tail consisting of residues Ser77 to Gly104 is highly disordered, as deduced from the secondary chemical shifts, the lack of medium-range and long-range NOEs and the {1H}-15N heteronuclear NOEs","type":"Results"},{"text":"It should also be noted that the N-terminal region of ALY77−182 which corresponds to residues 77−104 is flexible and without regular structure. This N-terminal “tail” contains several aliphatic and aromatic side chains that could also modulate interactions.","type":"Results"},{"text":"Although chemical shift dispersion of the majority of the backbone HN protons is good, overlap was observed for many of the loop regions as well as the N-terminal flexible region.","type":"Results"},{"text":"1H-15N-correlated NMR spectrum of ALY77−182 exhibits signals characteristic of a folded protein plus sharp overlapped resonances indicative of flexible regions","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12809490","version":2,"reference_html":"Structure of the nuclear factor ALY: insights into post-transcriptional regulatory and mRNA nuclear export processes. <i> Pérez-Alvarado GC, Martínez-Yamout M, Allen MM, Grosschedl R, Dyson HJ, Wright PE. </i> Biochemistry, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"1NO8"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":95,"region_id":"DP02371r002","start":84,"term_id":"IDPO:0000011","statement":[{"text":"Nevertheless, residues Asp84 to Phe95 exhibit some restriction of motion, as indicated by {1H}-15N heteronuclear NOEs in the range of 0.1−0.2.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12809490","version":2,"reference_html":"Structure of the nuclear factor ALY: insights into post-transcriptional regulatory and mRNA nuclear export processes. <i> Pérez-Alvarado GC, Martínez-Yamout M, Allen MM, Grosschedl R, Dyson HJ, Wright PE. </i> Biochemistry, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"1NO8"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":182,"region_id":"DP02371r004","start":77,"term_id":"GO:0140691","statement":[{"text":"ALY itself exhibits RNA binding activity and may act as an RNA chaperone by modulating the formation of RNA−protein and RNA−RNA complexes","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"12809490","version":3,"reference_html":"Structure of the nuclear factor ALY: insights into post-transcriptional regulatory and mRNA nuclear export processes. <i> Pérez-Alvarado GC, Martínez-Yamout M, Allen MM, Grosschedl R, Dyson HJ, Wright PE. </i> Biochemistry, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"1NO8"}],"term_name":"RNA folding chaperone","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA or an RNA-containing complex to assist the folding process.\" [PMID:31165735]","disprot_namespace":"Disorder function","term_is_binding":false},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":182,"region_id":"DP02371r006","start":77,"term_id":"GO:0060090","statement":[{"text":"ALY itself exhibits RNA binding activity and may act as an RNA chaperone by modulating the formation of RNA−protein and RNA−RNA complexes","type":"Article"},{"text":"Recently, it was reported that ALY is a component of the general mRNA export machinery","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"12809490","version":3,"reference_html":"Structure of the nuclear factor ALY: insights into post-transcriptional regulatory and mRNA nuclear export processes. <i> Pérez-Alvarado GC, Martínez-Yamout M, Allen MM, Grosschedl R, Dyson HJ, Wright PE. </i> Biochemistry, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"1NO8"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","uniref100":"UniRef100_O08583","date":"2019-11-26T17:16:12.318Z","acc":"O08583","name":"THO complex subunit 4","length":255,"organism":"Mus musculus","dataset":[],"UniParc":"UPI000002795D","genes":[{"name":{"value":"Alyref"},"synonyms":[{"value":"Aly"},{"value":"Ref1"},{"value":"Refbp1"},{"value":"THOC4"}]}],"alphafold_very_low_content":0.4,"disorder_content":0.10980392156862745,"disprot_consensus":{"full":[{"start":77,"end":83,"type":"D"},{"start":84,"end":95,"type":"T"},{"start":96,"end":104,"type":"D"},{"start":105,"end":182,"type":"F"}],"Structural state":[{"start":77,"end":104,"type":"D"}],"Structural transition":[{"start":84,"end":95,"type":"T"}],"Molecular function":[{"start":77,"end":182,"type":"F"}]}},{"features":{"gene3D":[{"start":1,"end":92,"id":"G3DSA:3.30.2310.20","name":"RelE-like"}],"pfam":[{"id":"PF05015","name":"RelE-like toxin of type II toxin-antitoxin system HigB","start":12,"end":92}]},"uniref50":"UniRef50_A0A158IQJ0","sequence":"MIRSFSCADTEALFTTGKTRRGSDIKSVAERKLAMLDAATELRDLRSPPGNRLESLSGNRADQHSIRVNDQWRLCFTWTEHGPVNVEIVDYH","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Pseudomonadales","Pseudomonadaceae","Pseudomonas"],"uniref90":"UniRef90_A0A445ZT61","disprot_id":"DP02372","dataset":["Unicellular toxins and antitoxins"],"ncbi_taxon_id":160488,"regions_counter":6,"creator":"rpancsa","regions":[{"region_id":"DP02372r001","validated":{"curator_id":"bmesza","timestamp":"2020-12-12T21:25:06.945Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":22,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"In GraT, on the other hand, the first 22 N-terminal residues together with the 6-His tag are located in an interstitial space and could not be traced due to lack of electron density.","type":"Results"},{"text":"The N-terminus of GraT is intrinsically disordered","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30814507","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6F8S"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"rpancsa","reference_html":"A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT. <i> Talavera A, Tamman H, Ainelo A, Konijnenberg A, Hadži S, Sobott F, Garcia-Pino A, Hõrak R, Loris R. </i> Nat Commun, 2019","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02372r002","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T10:47:34.484Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":22,"term_id":"GO:0140677","start":1,"version":3,"statement":[{"text":"GraT induction results in a distinct cleavage pattern on lpp mRNA, which is not detected in non-induced samples (Fig. 6, source data are provided as a Source Data file). Most of the observed cut sites are located between the 2nd and 3rd nucleotides of codons with adenine in the 2nd position. The only exception is the 10th cleavage (Fig. 6), which is found between two codons but still following an A nucleotide. Strong codon dependence suggests that, like other HigB family toxins, GraT acts as a ribosome-dependent mRNase. Given that induction of Δ22GraT did not result in mRNA cleavage (Fig. 6), the N-terminal disordered region is necessary for GraT mRNAse activity.","type":"Results"}],"term_name":"molecular function activator activity","ec_name":"mutant phenotype evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30814507","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0000315","curator_id":"rpancsa","reference_html":"A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT. <i> Talavera A, Tamman H, Ainelo A, Konijnenberg A, Hadži S, Sobott F, Garcia-Pino A, Hõrak R, Loris R. </i> Nat Commun, 2019","ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02372r004","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T10:48:18.521Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":22,"term_id":"IDPO:0000030","start":1,"version":3,"statement":[{"text":"On the other hand, this disordered stretch is more likely to work as an entropic barrier that sterically impedes the formation of the GraT2A2-DNA complex.","type":"Discussion"}],"term_name":"entropic chain","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","reference_html":"A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT. <i> Talavera A, Tamman H, Ainelo A, Konijnenberg A, Hadži S, Sobott F, Garcia-Pino A, Hõrak R, Loris R. </i> Nat Commun, 2019","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30814507","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6F8S"}],"term_namespace":"Disorder function","ec_id":"ECO:0006218","curator_id":"fquaglia","curator_orcid":"0000-0002-0341-4888","disprot_namespace":"Disorder function"},{"region_id":"DP02372r005","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T10:47:54.612Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":22,"term_id":"IDPO:0000030","start":1,"version":3,"statement":[{"text":"EMSAs using different (GraT2A2 or Δ22GraT2A2):operator molar ratios further confirm that in contrast to the wild-type GraT2A2, the Δ22GraT2A2 complex readily binds the graTA operator (Fig. 7c, d). These experiments suggest that the intrinsically disordered N-terminus of GraT is directly responsible for impairment of operator binding, likely via steric hindrance.","type":"Results"}],"term_name":"entropic chain","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30814507","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Disorder function","ec_id":"ECO:0001807","curator_id":"rpancsa","reference_html":"A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT. <i> Talavera A, Tamman H, Ainelo A, Konijnenberg A, Hadži S, Sobott F, Garcia-Pino A, Hõrak R, Loris R. </i> Nat Commun, 2019","ec_go":"IPI","disprot_namespace":"Disorder function"},{"region_id":"DP02372r006","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T10:48:08.390Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":22,"term_id":"IDPO:0000030","start":1,"version":3,"statement":[{"text":"β-Galactosidase measurements show that while GraA alone represses the graTA promoter activity, the expression of the GraTA complex leads to full derepression of the promoter (Fig. 8a, source data are provided as a Source Data file). Expression of the Δ22GraTA with N-terminally truncated GraT again represses the promoter (Fig. 8a), which is in good accordance with strong binding of Δ22GraT2A2 to the operator (Fig. 7).","type":"Results"}],"term_name":"entropic chain","ec_name":"beta galactosidase functional complementation evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30814507","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Disorder function","ec_id":"ECO:0006295","curator_id":"rpancsa","reference_html":"A dual role in regulation and toxicity for the disordered N-terminus of the toxin GraT. <i> Talavera A, Tamman H, Ainelo A, Konijnenberg A, Hadži S, Sobott F, Garcia-Pino A, Hõrak R, Loris R. </i> Nat Commun, 2019","ec_go":"IPI","disprot_namespace":"Disorder function"}],"released":"2020_12","uniref100":"UniRef100_A0A2V4FDM0","date":"2019-11-27T08:03:50.768Z","acc":"Q88MI5","name":"Putative Killer protein","length":92,"organism":"Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)","UniParc":"UPI000000EF89","genes":[{"olnNames":[{"value":"PP_1586","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAN67207.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAN67207.1"}}]}]}],"alphafold_very_low_content":0,"disorder_content":0.2391304347826087,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"}],"Structural state":[{"start":1,"end":22,"type":"D"}],"Molecular function":[{"start":1,"end":22,"type":"F"}],"Disorder function":[{"start":1,"end":22,"type":"F"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF05350","name":"Glycogen synthase kinase-3 binding","start":1,"end":239}]},"uniref50":"UniRef50_Q92837","sequence":"MPCRREEEEEAGEEAEGEEEEEDSFLLLQQSVALGSSGEVDRLVAQIGETLQLDAAQHSPASPCGPPGAPLRAPGPLAAAVPADKARSPAVPLLLPPALAETVGPAPPGVLRCALGDRGRVRGRAAPYCVAELATGPSALSPLPPQADLDGPPGAGKQGIPQPLSGPCRRGWLRGAAASRRLQQRRGSQPETRTGDDDPHRLLQQLVLSGNLIKEAVRRLHSRRLQLRAKLPQRPLLGPLSAPVHEPPSPRSPRAACSDPGASGRAQLRTGDGVLVPGS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q92837","disprot_id":"DP02373","ncbi_taxon_id":9606,"regions_counter":3,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":198,"region_id":"DP02373r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"missing residues in the PDB","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29057057","version":2,"reference_html":"From PIM1 to PI3Kδ via GSK3β: Target Hopping through the Kinome. <i> Henley ZA, Bax BD, Inglesby LM, Champigny A, Gaines S, Faulder P, Le J, Thomas DA, Washio Y, Baldwin IR. </i> ACS Med Chem Lett, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5OY4"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":279,"region_id":"DP02373r002","start":224,"term_id":"IDPO:0000002","statement":[{"text":"missing residues in the PDB","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29057057","version":2,"reference_html":"From PIM1 to PI3Kδ via GSK3β: Target Hopping through the Kinome. <i> Henley ZA, Bax BD, Inglesby LM, Champigny A, Gaines S, Faulder P, Le J, Thomas DA, Washio Y, Baldwin IR. </i> ACS Med Chem Lett, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5OY4"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":226,"region_id":"DP02373r003","start":188,"term_id":"GO:0140678","statement":[{"text":"we demonstrate that FRATtide (a peptide corresponding to residues 188–226 of FRAT1) binds to GSK3 and prevents GSK3 from interacting with Axin.","type":"Abstract"},{"text":"Demonstrated also in PMID:19802005, a short peptide (FRATtide) comprising amino-acids 188–226 from human FRAT1 is sufficient to inhibit GSK3","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"10481074","version":3,"reference_html":"A GSK3-binding peptide from FRAT1 selectively inhibits the GSK3-catalysed phosphorylation of axin and beta-catenin. <i> Thomas GM, Frame S, Goedert M, Nathke I, Polakis P, Cohen P. </i> FEBS Lett, 1999","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007689","term_name":"molecular function inhibitor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","uniref100":"UniRef100_Q92837","date":"2019-11-27T14:51:08.260Z","acc":"Q92837","name":"Proto-oncogene FRAT1","length":279,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000527ED8","genes":[{"name":{"value":"FRAT1"}}],"alphafold_very_low_content":0.36917562724014336,"disorder_content":0.910394265232975,"disprot_consensus":{"full":[{"start":1,"end":198,"type":"D"},{"start":199,"end":223,"type":"F"},{"start":224,"end":279,"type":"D"}],"Structural state":[{"start":1,"end":198,"type":"D"},{"start":224,"end":279,"type":"D"}],"Molecular function":[{"start":188,"end":226,"type":"F"}]}},{"features":{"gene3D":[{"start":513,"end":607,"id":"G3DSA:3.30.70.330","name":"G3DSA:3.30.70.330"},{"start":513,"end":607,"id":"G3DSA:3.30.70.330","name":"G3DSA:3.30.70.330"},{"start":513,"end":607,"id":"G3DSA:3.30.70.330","name":"G3DSA:3.30.70.330"},{"start":513,"end":607,"id":"G3DSA:3.30.70.330","name":"G3DSA:3.30.70.330"},{"start":3495,"end":3664,"id":"G3DSA:2.40.290.10","name":"G3DSA:2.40.290.10"}],"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":8,"end":69},{"id":"PF00076","name":"RNA recognition motif","start":339,"end":406},{"id":"PF00076","name":"RNA recognition motif","start":440,"end":507},{"id":"PF00076","name":"RNA recognition motif","start":520,"end":583},{"id":"PF07744","name":"SPOC domain","start":3501,"end":3662},{"id":"PF20808","name":"Msx2-interacting protein, RAM7 domain","start":2645,"end":2754},{"id":"PF20809","name":"Msx2-interacting protein, MID domain","start":2059,"end":2389},{"id":"PF20810","name":"Msx2-interacting protein, nuclear receptor-interacting domain","start":2401,"end":2639}]},"uniref50":"UniRef50_Q96T58","sequence":"MVRETRHLWVGNLPENVREEKIIEHFKRYGRVESVKILPKRGSEGGVAAFVDFVDIKSAQKAHNSVNKMGDRDLRTDYNEPGTIPSAARGLDDTVSIASRSREVSGFRGGGGGPAYGPPPSLHAREGRYERRLDGASDNRERAYEHSAYGHHERGTGGFDRTRHYDQDYYRDPRERTLQHGLYYASRSRSPNRFDAHDPRYEPRAREQFTLPSVVHRDIYRDDITREVRGRRPERNYQHSRSRSPHSSQSRNQSPQRLASQASRPTRSPSGSGSRSRSSSSDSISSSSSTSSDSSDSSSSSSDDSPARSVQSAAVPAPTSQLLSSLEKDEPRKSFGIKVQNLPVRSTDTSLKDGLFHEFKKFGKVTSVQIHGTSEERYGLVFFRQQEDQEKALTASKGKLFFGMQIEVTAWIGPETESENEFRPLDERIDEFHPKATRTLFIGNLEKTTTYHDLRNIFQRFGEIVDIDIKKVNGVPQYAFLQYCDIASVCKAIKKMDGEYLGNNRLKLGFGKSMPTNCVWLDGLSSNVSDQYLTRHFCRYGPVVKVVFDRLKGMALVLYNEIEYAQAAVKETKGRKIGGNKIKVDFANRESQLAFYHCMEKSGQDIRDFYEMLAERREERRASYDYNQDRTYYESVRTPGTYPEDSRRDYPARGREFYSEWETYQGDYYESRYYDDPREYRDYRNDPYEQDIREYSYRQRERERERERFESDRDRDHERRPIERSQSPVHLRRPQSPGASPSQAERLPSDSERRLYSRSSDRSGSCSSLSPPRYEKLDKSRLERYTKNEKTDKERTFDPERVERERRLIRKEKVEKDKTDKQKRKGKVHSPSSQSSETDQENEREQSPEKPRSCNKLSREKADKEGIAKNRLELMPCVVLTRVKEKEGKVIDHTPVEKLKAKLDNDTVKSSALDQKLQVSQTEPAKSDLSKLESVRMKVPKEKGLSSHVEVVEKEGRLKARKHLKPEQPADGVSAVDLEKLEARKRRFADSNLKAEKQKPEVKKSSPEMEDARVLSKKQPDVSSREVILLREGEAERKPVRKEILKRESKKIKLDRLNTVASPKDCQELASISVGSGSRPSSDLQARLGELAGESVENQEVQSKKPIPSKPQLKQLQVLDDQGPEREDVRKNYCSLRDETPERKSGQEKSHSVNTEEKIGIDIDHTQSYRKQMEQSRRKQQMEMEIAKSEKFGSPKKDVDEYERRSLVHEVGKPPQDVTDDSPPSKKKRMDHVDFDICTKRERNYRSSRQISEDSERTGGSPSVRHGSFHEDEDPIGSPRLLSVKGSPKVDEKVLPYSNITVREESLKFNPYDSSRREQMADMAKIKLSVLNSEDELNRWDSQMKQDAGRFDVSFPNSIIKRDSLRKRSVRDLEPGEVPSDSDEDGEHKSHSPRASALYESSRLSFLLRDREDKLRERDERLSSSLERNKFYSFALDKTITPDTKALLERAKSLSSSREENWSFLDWDSRFANFRNNKDKEKVDSAPRPIPSWYMKKKKIRTDSEGKMDDKKEDHKEEEQERQELFASRFLHSSIFEQDSKRLQHLERKEEDSDFISGRIYGKQTSEGANSTTDSIQEPVVLFHSRFMELTRMQQKEKEKDQKPKEVEKQEDTENHPKTPESAPENKDSELKTPPSVGPPSVTVVTLESAPSALEKTTGDKTVEAPLVTEEKTVEPATVSEEAKPASEPAPAPVEQLEQVDLPPGADPDKEAAMMPAGVEEGSSGDQPPYLDAKPPTPGASFSQAESNVDPEPDSTQPLSKPAQKSEEANEPKAEKPDATADAEPDANQKAEAAPESQPPASEDLEVDPPVAAKDKKPNKSKRSKTPVQAAAVSIVEKPVTRKSERIDREKLKRSNSPRGEAQKLLELKMEAEKITRTASKNSAADLEHPEPSLPLSRTRRRNVRSVYATMGDHENRSPVKEPVEQPRVTRKRLERELQEAAAVPTTPRRGRPPKTRRRADEEEENEAKEPAETLKPPEGWRSPRSQKTAAGGGPQGKKGKNEPKVDATRPEATTEVGPQIGVKESSMEPKAAEEEAGSEQKRDRKDAGTDKNPPETAPVEVVEKKPAPEKNSKSKRGRSRNSRLAVDKSASLKNVDAAVSPRGAAAQAGERESGVVAVSPEKSESPQKEDGLSSQLKSDPVDPDKEPEKEDVSASGPSPEATQLAKQMELEQAVEHIAKLAEASASAAYKADAPEGLAPEDRDKPAHQASETELAAAIGSIINDISGEPENFPAPPPYPGESQTDLQPPAGAQALQPSEEGMETDEAVSGILETEAATESSRPPVNAPDPSAGPTDTKEARGNSSETSHSVPEAKGSKEVEVTLVRKDKGRQKTTRSRRKRNTNKKVVAPVESHVPESNQAQGESPAANEGTTVQHPEAPQEEKQSEKPHSTPPQSCTSDLSKIPSTENSSQEISVEERTPTKASVPPDLPPPPQPAPVDEEPQARFRVHSIIESDPVTPPSDPSIPIPTLPSVTAAKLSPPVASGGIPHQSPPTKVTEWITRQEEPRAQSTPSPALPPDTKASDVDTSSSTLRKILMDPKYVSATSVTSTSVTTAIAEPVSAAPCLHEAPPPPVDSKKPLEEKTAPPVTNNSEIQASEVLVAADKEKVAPVIAPKITSVISRMPVSIDLENSQKITLAKPAPQTLTGLVSALTGLVNVSLVPVNALKGPVKGSVTTLKSLVSTPAGPVNVLKGPVNVLTGPVNVLTTPVNATVGTVNAAPGTVNAAASAVNATASAVTVTAGAVTAASGGVTATTGTVTMAGAVIAPSTKCKQRASANENSRFHPGSMPVIDDRPADAGSGAGLRVNTSEGVVLLSYSGQKTEGPQRISAKISQIPPASAMDIEFQQSVSKSQVKPDSVTASQPPSKGPQAPAGYANVATHSTLVLTAQTYNASPVISSVKADRPSLEKPEPIHLSVSTPVTQGGTVKVLTQGINTPPVLVHNQLVLTPSIVTTNKKLADPVTLKIETKVLQPANLGSTLTPHHPPALPSKLPTEVNHVPSGPSIPADRTVSHLAAAKLDAHSPRPSGPGPSSFPRASHPSSTASTALSTNATVMLAAGIPVPQFISSIHPEQSVIMPPHSITQTVSLSHLSQGEVRMNTPTLPSITYSIRPEALHSPRAPLQPQQIEVRAPQRASTPQPAPAGVPALASQHPPEEEVHYHLPVARATAPVQSEVLVMQSEYRLHPYTVPRDVRIMVHPHVTAVSEQPRAADGVVKVPPASKAPQQPGKEAAKTPDAKAAPTPTPAPVPVPVPLPAPAPAPHGEARILTVTPSNQLQGLPLTPPVVVTHGVQIVHSSGELFQEYRYGDIRTYHPPAQLTHTQFPAASSVGLPSRTKTAAQGPPPEGEPLQPPQPVQSTQPAQPAPPCPPSQLGQPGQPPSSKMPQVSQEAKGTQTGVEQPRLPAGPANRPPEPHTQVQRAQAETGPTSFPSPVSVSMKPDLPVSLPTQTAPKQPLFVPTTSGPSTPPGLVLPHTEFQPAPKQDSSPHLTSQRPVDMVQLLKKYPIVWQGLLALKNDTAAVQLHFVSGNNVLAHRSLPLSEGGPPLRIAQRMRLEATQLEGVARRMTVETDYCLLLALPCGRDQEDVVSQTESLKAAFITYLQAKQAAGIINVPNPGSNQPAYVLQIFPPCEFSESHLSRLAPDLLASISNISPHLMIVIASV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q96T58","disprot_id":"DP02375","ncbi_taxon_id":9606,"regions_counter":1,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":3494,"region_id":"DP02375r001","start":3470,"term_id":"IDPO:0000002","statement":[{"text":"No electron density was observed for the 25 N-terminal residues (amino acids 3470-3494) and three residues (amino acids 3542-3544) in a loop region. SDS-PAGE analysis of dissolved crystals showed that the crystals contain the full-length fragment, suggesting that these regions are disordered (data not shown).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12897056","version":2,"reference_html":"A conserved structural motif reveals the essential transcriptional repression function of Spen proteins and their role in developmental signaling. <i> Ariyoshi M, Schwabe JW. </i> Genes Dev, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1OW1"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T19:37:14.577Z"}}],"released":"2020_12","uniref100":"UniRef100_Q96T58","date":"2019-11-27T16:05:24.273Z","acc":"Q96T58","name":"Msx2-interacting protein","length":3664,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins","RNA-binding proteins"],"UniParc":"UPI000006FF0C","genes":[{"name":{"value":"SPEN"},"synonyms":[{"value":"KIAA0929"},{"value":"MINT"},{"value":"SHARP"}]}],"disorder_content":0.006823144104803494,"disprot_consensus":{"full":[{"start":3470,"end":3494,"type":"D"}],"Structural state":[{"start":3470,"end":3494,"type":"D"}]}},{"features":{"gene3D":[{"start":1662,"end":1730,"id":"G3DSA:1.10.150.50","name":"Transcription Factor, Ets-1"},{"start":559,"end":669,"id":"G3DSA:2.30.42.10","name":"G3DSA:2.30.42.10"},{"start":104,"end":363,"id":"G3DSA:1.25.40.20","name":"Ankyrin repeat-containing domain"}],"pfam":[{"id":"PF00536","name":"SAM domain (Sterile alpha motif)","start":1666,"end":1727},{"id":"PF07653","name":"Variant SH3 domain","start":475,"end":527},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":123,"end":213},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":254,"end":336},{"id":"PF17820","name":"PDZ domain","start":610,"end":658}]},"uniref50":"UniRef50_Q4ACU6","sequence":"MDGPGASAVVVRVGIPDLQQTKCLRLDPTAPVWAAKQRVLCALNHSLQDALNYGLFQPPSRGRAGKFLDEERLLQDYPPNLDTPLPYLEFRYKRRVYAQNLIDDKQFAKLHTKANLKKFMDYVQLHSTDKVARLLDKGLDPNFHDPDSGECPLSLAAQLDNATDLLKVLRNGGAHLDFRTRDGLTAVHCATRQRNAGALTTLLDLGASPDYKDSRGLTPLYHSALGGGDALCCELLLHDHAQLGTTDENGWQEIHQACRFGHVQHLEHLLFYGANMGAQNASGNTALHICALYNQESCARVLLFRGANKDVRNYNSQTAFQVAIIAGNFELAEVIKTHKDSDVVPFRETPSYAKRRRLAGPSGLASPRPLQRSASDINLKGDQPAASPGPTLRSLPHQLLLQRLQEEKDRDRDGELENDISGPSAGRGGHNKISPSGPGGSGPAPGPGPASPAPPAPPPRGPKRKLYSAVPGRKFIAVKAHSPQGEGEIPLHRGEAVKVLSIGEGGFWEGTVKGRTGWFPADCVEEVQMRQYDTRHETREDRTKRLFRHYTVGSYDSLTSHSDYVIDDKVAILQKRDHEGFGFVLRGAKAETPIEEFTPTPAFPALQYLESVDVEGVAWRAGLRTGDFLIEVNGVNVVKVGHKQVVGLIRQGGNRLVMKVVSVTRKPEEDGARRRAPPPPKRAPSTTLTLRSKSMTAELEELASIRRRKGEKLDEILAVAAEPTLRPDIADADSRAATVKQRPTSRRITPAEISSLFERQGLPGPEKLPGSLRKGIPRTKSVGEDEKLASLLEGRFPRSTSMQDTVREGRGIPPPPQTAPPPPPAPYYFDSGPPPTFSPPPPPGRAYDTVRSSFKPGLEARLGAGAAGLYDPSTPLGPLPYPERQKRARSMIILQDSAPEVGDVPRPAPAATPPERPKRRPRPSGPDSPYANLGAFSASLFAPSKPQRRKSPLVKQLQVEDAQERAALAVGSPGPVGGSFAREPSPTHRGPRPGSLDYSSGEGLGLTFGGPSPGPVKERRLEERRRSTVFLSVGAIEGSPPSADLPSLQPSRSIDERLLGTGATTGRDLLLPSPVSALKPLVGGPSLGPSGSTFIHPLTGKPLDPSSPLALALAARERALASQTPSRSPTPVHSPDADRPGPLFVDVQTRDSERGPLASPAFSPRSPAWIPVPARREAEKPPREERKSPEDKKSMILSVLDTSLQRPAGLIVVHATSNGQEPSRLGAEEERPGTPELAPAPMQAAAVAEPMPSPRAQPPGSIPADPGPGQGSSEEEPELVFAVNLPPAQLSSSDEETREELARIGLVPPPEEFANGILLTTPPPGPGPLPTTVPSPASGKPSSELPPAPESAADSGVEEADTRSSSDPHLETTSTISTVSSMSTLSSESGELTDTHTSFADGHTFLLEKPPVPPKPKLKSPLGKGPVTFRDPLLKQSSDSELMAQQHHAASTGLASAAGPARPRYLFQRRSKLWGDPVESRGLPGPEDDKPTVISELSSRLQQLNKDTRSLGEEPVGGLGSLLDPAKKSPIAAARLFSSLGELSTISAQRSPGGPGGGASYSVRPSGRYPVARRAPSPVKPASLERVEGLGAGVGGAGRPFGLTPPTILKSSSLSIPHEPKEVRFVVRSVSARSRSPSPSPLPSPSPGSGPSAGPRRPFQQKPLQLWSKFDVGDWLESIHLGEHRDRFEDHEIEGAHLPALTKEDFVELGVTRVGHRMNIERALRQLDGS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q4ACU6","disprot_id":"DP02376","ncbi_taxon_id":10090,"regions_counter":5,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":600,"region_id":"DP02376r001","start":588,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Superposition of the eight molecules per asymmetric unit of Shank3 PDZ showed that they diverge structurally mainly in the more or less defined loop (disordered loop region between residues 588‐600 for all molecules) connecting strands βB and βC as well as in the location of their N‐ and C‐termini","type":"Results"},{"text":"The dashed line indicates a disordered loop (residues 588–600)","type":"Figure"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21626699","version":2,"reference_html":"Discovery, structure-activity relationship studies, and crystal structure of nonpeptide inhibitors bound to the Shank3 PDZ domain. <i> Saupe J, Roske Y, Schillinger C, Kamdem N, Radetzki S, Diehl A, Oschkinat H, Krause G, Heinemann U, Rademann J. </i> ChemMedChem, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3O5N"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-02T15:42:27.362Z"}},{"start":377,"end":532,"reference_id":"33235361","reference_source":"pmid","reference_html":"CaMKIIα-driven, phosphatase-checked postsynaptic plasticity via phase separation. <i> Cai Q, Zeng M, Wu X, Wu H, Zhan Y, Tian R, Zhang M. </i> Cell Res, 2021","date":"2022-11-09T19:31:26.466Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP02376r002","statement":[{"text":"This version of Shank3 contains known target binding domains/motifs and lacks most of the unstructured regions (Supplementary information, Fig. S3a, referred to as Shank3 from here on) as well as the previously identified active CaMKIIα binding site in the middle of the protein.","type":"Results"},{"text":"This contrasts with a recent finding that an unstructured fragment of Shank3 in the middle of the protein (aa 931–1014) binds to T286-autophosphorylated CaMKII.","type":"Results"},{"text":"The simplified version of Shank3 was generated by using an overlap PCR method to fuse multiple fragments, including residues 1–376 (NTD-ANK), 533–665 (N-PDZ), 1294–1323 (HBS), 1400–1426 (CBS) and 1654–1730 (SAM) with three point mutations (L231R, F304Y and M1718A) to improve solubility and homogeneity of the recombinant protein.","type":"Methods"},{"text":"The authors consider the regions 377-532, 666-1295, 1324-1399 and 1427-1653 as unstructured. ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:58:28.924Z"}},{"start":666,"end":1293,"reference_id":"33235361","reference_source":"pmid","reference_html":"CaMKIIα-driven, phosphatase-checked postsynaptic plasticity via phase separation. <i> Cai Q, Zeng M, Wu X, Wu H, Zhan Y, Tian R, Zhang M. </i> Cell Res, 2021","date":"2022-11-09T19:32:09.093Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP02376r003","statement":[{"text":"This version of Shank3 contains known target binding domains/motifs and lacks most of the unstructured regions (Supplementary information, Fig. S3a, referred to as Shank3 from here on) as well as the previously identified active CaMKIIα binding site in the middle of the protein.","type":"Results"},{"text":"This contrasts with a recent finding that an unstructured fragment of Shank3 in the middle of the protein (aa 931–1014) binds to T286-autophosphorylated CaMKII.","type":"Results"},{"text":"The simplified version of Shank3 was generated by using an overlap PCR method to fuse multiple fragments, including residues 1–376 (NTD-ANK), 533–665 (N-PDZ), 1294–1323 (HBS), 1400–1426 (CBS) and 1654–1730 (SAM) with three point mutations (L231R, F304Y and M1718A) to improve solubility and homogeneity of the recombinant protein.","type":"Methods"},{"text":"The authors consider the regions 377-532, 666-1293, 1324-1399 and 1427-1653 as unstructured. ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:58:33.881Z"}},{"start":1324,"end":1399,"reference_id":"33235361","reference_source":"pmid","reference_html":"CaMKIIα-driven, phosphatase-checked postsynaptic plasticity via phase separation. <i> Cai Q, Zeng M, Wu X, Wu H, Zhan Y, Tian R, Zhang M. </i> Cell Res, 2021","date":"2022-11-09T19:32:26.943Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP02376r004","statement":[{"text":"This version of Shank3 contains known target binding domains/motifs and lacks most of the unstructured regions (Supplementary information, Fig. S3a, referred to as Shank3 from here on) as well as the previously identified active CaMKIIα binding site in the middle of the protein.","type":"Results"},{"text":"This contrasts with a recent finding that an unstructured fragment of Shank3 in the middle of the protein (aa 931–1014) binds to T286-autophosphorylated CaMKII.","type":"Results"},{"text":"The simplified version of Shank3 was generated by using an overlap PCR method to fuse multiple fragments, including residues 1–376 (NTD-ANK), 533–665 (N-PDZ), 1294–1323 (HBS), 1400–1426 (CBS) and 1654–1730 (SAM) with three point mutations (L231R, F304Y and M1718A) to improve solubility and homogeneity of the recombinant protein.","type":"Methods"},{"text":"The authors consider the regions 377-532, 666-1293, 1324-1399 and 1427-1653 as unstructured. ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:58:35.177Z"}},{"start":1427,"end":1653,"reference_id":"33235361","reference_source":"pmid","reference_html":"CaMKIIα-driven, phosphatase-checked postsynaptic plasticity via phase separation. <i> Cai Q, Zeng M, Wu X, Wu H, Zhan Y, Tian R, Zhang M. </i> Cell Res, 2021","date":"2022-11-09T19:32:44.061Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP02376r005","statement":[{"text":"This version of Shank3 contains known target binding domains/motifs and lacks most of the unstructured regions (Supplementary information, Fig. S3a, referred to as Shank3 from here on) as well as the previously identified active CaMKIIα binding site in the middle of the protein.","type":"Results"},{"text":"This contrasts with a recent finding that an unstructured fragment of Shank3 in the middle of the protein (aa 931–1014) binds to T286-autophosphorylated CaMKII.","type":"Results"},{"text":"The simplified version of Shank3 was generated by using an overlap PCR method to fuse multiple fragments, including residues 1–376 (NTD-ANK), 533–665 (N-PDZ), 1294–1323 (HBS), 1400–1426 (CBS) and 1654–1730 (SAM) with three point mutations (L231R, F304Y and M1718A) to improve solubility and homogeneity of the recombinant protein.","type":"Methods"},{"text":"The authors consider the regions 377-532, 666-1293, 1324-1399 and 1427-1653 as unstructured. ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:58:57.929Z"}}],"released":"2023_06","uniref100":"UniRef100_Q4ACU6","date":"2019-11-27T16:14:39.228Z","acc":"Q4ACU6","name":"SH3 and multiple ankyrin repeat domains protein 3","length":1730,"organism":"Mus musculus","dataset":["NDDs-related proteins","Condensates-related proteins"],"UniParc":"UPI0001529A70","genes":[{"name":{"value":"Shank3"},"synonyms":[{"value":"Kiaa1650"},{"value":"Prosap2"}]}],"alphafold_very_low_content":0.6277456647398844,"disorder_content":0.6358381502890174,"disprot_consensus":{"full":[{"start":377,"end":532,"type":"D"},{"start":588,"end":600,"type":"D"},{"start":666,"end":1293,"type":"D"},{"start":1324,"end":1399,"type":"D"},{"start":1427,"end":1653,"type":"D"}],"Structural state":[{"start":377,"end":532,"type":"D"},{"start":588,"end":600,"type":"D"},{"start":666,"end":1293,"type":"D"},{"start":1324,"end":1399,"type":"D"},{"start":1427,"end":1653,"type":"D"}]}},{"features":{"gene3D":[],"pfam":[]},"uniref50":"UniRef50_Q9GRZ3","sequence":"MRSTTFDKNSGAPEEPRRPRGPRTPDGEPTEANERPCSSSSSLSNDSFVPAPQGPQNGHTSSSHDNDYSEYRPRRGPKTPPLPPPDEPVKQQQQQQPIVAPYSYYPTYGSSTGYPYPYPTMMMPQQGIPGPSQHPATPSYYIQHPPPPSMSNGAPYYPHMNPSPYYQPRPNYVTQPPAPIIPPPQPPVMTASAAAAAYRDRLPPPPPKPPMPDLRTKEPIGIRSWNGSGIPPPPILPPVACLSSTMSPGMLRSPVPRERFNSVESNGSFSLHPPPPVPPPAKKPLNMDVRELLNGAHQTTVESVKKDPPAPQPRPRPIPVPPTTSYNSSFCGLLPPPPVPPDLRASAASAAASPPMVQDASFSSVLTPKTKAPEKIPSPPATVTSSTDSLEHMQRKRKKQQETEEQEKAAKKAKRHQEERERQKIEAEKRKKAILEEAAKVTRPPAEKKPPVVVEETIRAVPFVFKQEMPLPFVLAAAAAAAKEPETRPEPRPEPKQNGYHVKQAEPLQAEPPQNGYRLAAAQALQHEPRQASEPLQNVQPEPSKQASELVQNGYAAPQEPRRATPPPEPLRNELPKHSDLLNVSKPSEPAEPPKPSDAPREPEVAAAEAVIPEPSPAVSVEEPPRREERAASMAGIPPPPPTSSRHSPVPRREDRAEFMARSTPPAPGKDRKSLGGRMAMWRNKKNKTASMVGPPEPKELPAVVEVEAIVEPVVEDQPEPVVSEELKPTEPEPVEPEPMEVEPVVAKEVVEEVVEEVVETQEPWVPLSECSRSSSLELLAELPPPPRASEPPPPPPPPVATAPVPASMEEDEIIDIETIDEITSTSTKKPEKVEKIKKAPVVTKAALKMVGRPKKTPGRRRKKDRGASPSPSPSPPPPPETTLTPIVLPRKKQRIEKKKLTPPPPQQAPVTSHTPPPVEQLMSRKKQIMMEHSSLDHIQFKLIEIELAAKRRKAEAAAKAAAAVEQKDEKAEEVENRETPPGPSTSMRSSSLHTPNTSEEDEVIFVEPSTLEKPERRNGTTEERVMTADQRAMFDAKIEEARRSRMSTRDCSVVSTLGPVKSKASQRLHDIIEGKEELEDSMDDPTNNNGTLAGILYPMRSERAESVSSNHRSEGAGGSMSLKHHLARKNELKEEANVARRSEILKAVVKRQREIGVPTTLMSKSAIELVEEDEKERKNHKNNKTLSHPDYVRSKNEAEKAEFHGKGGTMRITNRNLKMLTRQFDLPKMSSRFRKFVRIRRHPNGMATIISCDYNQIKQHLGPNEMKHFERQFVRLGFAENNGVPLFAIGVMENAAEALHDQFEWLAKNSPNTQVKVGSLTNKQFIETMPMKKYYESAMETLDMGTFRFGPLMSLSMVGTKNEEAGGNFKEMLDALNAAPFLGPIMPWGDFSEVQGIKEDTSDDGPIFWVRPGEQMVPTDGKNRSTEPRHPLATRGNDRRETAFNDRTNAHADQVRESTEDDPTTTTTTTTTTSSSSSSSKSKKSAKSDPTFVKSTAAVGVLQGIRNPDANDDDEYYEDERKAVKEVIVFDAHDLHKVAHHLAMDLYEPPVSQCHRWVDDAILNTMRREGIRYAKLELHENDMYFLPRNVIHQFRTVSACSSVAWHVRLRHYYDVDQPASLSDPQFECDSDYSDDGDFDD","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"uniref90":"UniRef90_Q9GRZ3","disprot_id":"DP02377","ncbi_taxon_id":6239,"regions_counter":2,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1441,"region_id":"DP02377r001","start":1420,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Dashed lines represent regions of DPY−21 that are disordered and not built in the DPY−211210–1617 structure","type":"Figure"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28867287","version":2,"reference_html":"Dynamic Control of X Chromosome Conformation and Repression by a Histone H4K20 Demethylase. <i> Brejc K, Bian Q, Uzawa S, Wheeler BS, Anderson EC, King DS, Kranzusch PJ, Preston CG, Meyer BJ. </i> Cell, 2017","date":"2022-09-14T08:57:52.787Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5UQD"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30915","entry_name":"2-oxoglutaric acid"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"44836","entry_name":"2-(2-methoxyethoxy)ethanol"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29033","entry_name":"iron(2+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-14T14:00:35.154Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1494,"region_id":"DP02377r002","start":1458,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Dashed lines represent regions of DPY−21 that are disordered and not built in the DPY−211210–1617 structure","type":"Figure"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28867287","version":2,"reference_html":"Dynamic Control of X Chromosome Conformation and Repression by a Histone H4K20 Demethylase. <i> Brejc K, Bian Q, Uzawa S, Wheeler BS, Anderson EC, King DS, Kranzusch PJ, Preston CG, Meyer BJ. </i> Cell, 2017","date":"2022-09-14T08:58:22.411Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5UQD"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30915","entry_name":"2-oxoglutaric acid"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"44836","entry_name":"2-(2-methoxyethoxy)ethanol"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29033","entry_name":"iron(2+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-14T14:00:31.900Z"}}],"released":"2023_12","uniref100":"UniRef100_Q9GRZ3","date":"2019-11-27T16:43:03.204Z","acc":"Q9GRZ3","name":"Lysine-specific demethylase 9","length":1641,"organism":"Caenorhabditis elegans","dataset":[],"UniParc":"UPI00000612E3","genes":[{"name":{"value":"dpy-21","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"Y59A8B.1a","url":"https://www.wormbase.org/db/seq/sequence?name=Y59A8B.1a;class=Transcript"}}]},"orfNames":[{"value":"Y59A8B.1","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"Y59A8B.1a","url":"https://www.wormbase.org/db/seq/sequence?name=Y59A8B.1a;class=Transcript"}}]}]}],"alphafold_very_low_content":0.6447288238878732,"disorder_content":0.03595368677635588,"disprot_consensus":{"full":[{"start":1420,"end":1441,"type":"D"},{"start":1458,"end":1494,"type":"D"}],"Structural state":[{"start":1420,"end":1441,"type":"D"},{"start":1458,"end":1494,"type":"D"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF11498","name":"Transcriptional activator LAG-3","start":23,"end":490}]},"uniref50":"UniRef50_Q09260","sequence":"MDDLSEFFVIEEMFISEPSVAGMKPSTSKTTHSPPPEEPTAPFVNDNLPNPEDEPTIGDLNAFHSGEELHRQRSELARANYEKARPEMIANQRAVTAHLFNRYTEDEERKRVEQQKNKEAMNASTSAPTSSRNGGQSVENRKRRNDVVVAPPTSEEEWKRAQQQHWMGQQQPQMQFQMQQQYHSQQQQYIMMQQQHHHMTGMQQIHHQMPSTSSADSIRSVPTPASSMHQPSPAEMRNGCGMSRNATMDMTCSPMSGGQPIVDENNLAVPEGEWFDKLALAVAEQYNVDTILGPDTYDTFLAELDFSSSESPTKQSPMEMNGDRMPSTAPPPAQNPQHIAQLQQQQNKMRLMQQQQQEMQRIEQQRRQQIMQQQQQQQQQEHQRQQMLLQQQQQQQQMQQHHQMNGGGQFATQAHQQAAYMQQMQRMEQIRHQQQQAQQHQQAQQQHQQQAQHHQMGYGIPNGYPQQMHMHPPAYGAHHMPQPTAFANIN","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"uniref90":"UniRef90_Q09260","disprot_id":"DP02378","ncbi_taxon_id":6239,"regions_counter":1,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":132,"region_id":"DP02378r001","start":115,"term_id":"IDPO:0000002","statement":[{"text":"N-terminal domain of Sel-8 (Mastermind), residues 49–132, were cloned into pGEX-6P-1","type":"Methods"},{"text":"The final refined model consists of CSL residues 195–267, 278–311, 319–372, 380–433, and 440–663, NotchIC residues 933–952 and 1021–1297, Mastermind residues 52–114","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16530045","version":2,"reference_html":"Crystal structure of the CSL-Notch-Mastermind ternary complex bound to DNA. <i> Wilson JJ, Kovall RA. </i> Cell, 2006","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2FO1"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","uniref100":"UniRef100_Q09260","date":"2019-11-27T16:54:26.655Z","acc":"Q09260","name":"Protein lag-3","length":490,"organism":"Caenorhabditis elegans","dataset":[],"UniParc":"UPI000002AD0D","genes":[{"name":{"value":"sel-8"},"synonyms":[{"value":"lag-3"}],"orfNames":[{"value":"C32A3.1"}]}],"alphafold_very_low_content":0.45102040816326533,"disorder_content":0.036734693877551024,"disprot_consensus":{"full":[{"start":115,"end":132,"type":"D"}],"Structural state":[{"start":115,"end":132,"type":"D"}]}},{"features":{"gene3D":[{"start":149,"end":287,"id":"G3DSA:2.40.330.10","name":"DNA-binding pseudobarrel domain"}],"pfam":[{"id":"PF02362","name":"B3 DNA binding domain","start":159,"end":260},{"id":"PF06507","name":"Auxin response factor ancillary domain","start":308,"end":390}]},"uniref50":"UniRef50_O23661","sequence":"MGGLIDLNVMETEEDETQTQTPSSASGSVSPTSSSSASVSVVSSNSAGGGVCLELWHACAGPLISLPKRGSLVLYFPQGHLEQAPDFSAAIYGLPPHVFCRILDVKLHAETTTDEVYAQVSLLPESEDIERKVREGIIDVDGGEEDYEVLKRSNTPHMFCKTLTASDTSTHGGFSVPRRAAEDCFPPLDYSQPRPSQELLARDLHGLEWRFRHIYRGQPRRHLLTTGWSAFVNKKKLVSGDAVLFLRGDDGKLRLGVRRASQIEGTAALSAQYNQNMNHNNFSEVAHAISTHSVFSISYNPKASWSNFIIPAPKFLKVVDYPFCIGMRFKARVESEDASERRSPGIISGISDLDPIRWPGSKWRCLLVRWDDIVANGHQQRVSPWEIEPSGSISNSGSFVTTGPKRSRIGFSSGKPDIPVSEGIRATDFEESLRFQRVLQGQEIFPGFINTCSDGGAGARRGRFKGTEFGDSYGFHKVLQGQETVPAYSITDHRQQHGLSQRNIWCGPFQNFSTRILPPSVSSSPSSVLLTNSNSPNGRLEDHHGGSGRCRLFGFPLTDETTAVASATAVPCVEGNSMKGASAVQSNHHHSQGRDIYAMRDMLLDIAL","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_O23661","disprot_id":"DP02380","ncbi_taxon_id":3702,"regions_counter":4,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":594,"region_id":"DP02380r001","start":388,"term_id":"IDPO:0000002","statement":[{"text":"CD analysis of the ETT_388-594 construct showing characteristic spectrum of an unstructured protein","type":"Figure"},{"text":"Circular dichroism and thermal stability analyses confirmed the bioinformatic predictions of near-complete disorder of the ES domain","type":"Discussion"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30202032","version":2,"reference_html":"Auxin sensing is a property of an unstructured domain in the Auxin Response Factor ETTIN of Arabidopsis thaliana. <i> Simonini S, Mas PJ, Mas CMVS, Østergaard L, Hart DJ. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006200","validated":{"curator_id":"fquaglia","timestamp":"2020-12-01T16:40:16.116Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02380r002","ec_ontology":"ECO","end":594,"term_id":"GO:0140677","start":388,"version":4,"statement":[{"text":"Analyses by Y2H revealed the ETT_388-594 construct retained full responsiveness to increases in auxin concentration (Fig. 4A; ETT-BD and ES-BD and ETT-388-594-BD rows) confirming it to be a stable and purifiable form of the ETT auxin-responsive domain capable of binding the Arabidopsis INDEHISCENT (IND) transcription factor used as the bait in the assay.","type":"Results"}],"term_name":"molecular function activator activity","ec_name":"yeast 2-hybrid evidence used in manual assertion","curator_orcid":"0000-0002-5152-5953","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"30202032","date":"2022-03-08T14:59:48.826Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005805","curator_id":"esalladini","reference_html":"Auxin sensing is a property of an unstructured domain in the Auxin Response Factor ETTIN of Arabidopsis thaliana. <i> Simonini S, Mas PJ, Mas CMVS, Østergaard L, Hart DJ. </i> Sci Rep, 2018","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"O81313","operator":"and","partner_start":null,"partner_end":null}]},{"region_id":"DP02380r003","ec_ontology":"ECO","end":594,"term_id":"GO:0036094","start":388,"version":4,"statement":[{"text":"Analyses by Y2H revealed the ETT_388-594 construct retained full responsiveness to increases in auxin concentration (Fig. 4A; ETT-BD and ES-BD and ETT-388-594-BD rows) confirming it to be a stable and purifiable form of the ETT auxin-responsive domain capable of binding the Arabidopsis INDEHISCENT (IND) transcription factor used as the bait in the assay.","type":"Results"},{"text":"To probe the auxin sensing ability of the ES domain, random mutations were introduced into the ES domain sequence by error prone mutagenesis. A pool of ES mutants was cloned and tested in Y2H assay in the presence of IAA to isolate viable clones exhibiting IAA insensitivity. Tree ES domain variants were isolated (Fig.  4A, clones ES_EP1-3 BD) harbouring amino acid substitutions at the beginning (Fig.  4A, I393T, I424T, F445I) and the end (Fig.  4A, T562A, Y597H, D601G) of the ES domain. Mutations were also identified in proximity to the Motif 1B (Fig.  4A, Q436L) and in the Ser patch (Fig.  4A, S520T) which impair the auxin sensing property of the ETT-IND dimer. In parallel to the error-prone approach, we also introduced manually point mutations into the Ser patch by site-specific mutagenesis (S523T, S S524T, S526T and S527T; Fig.  4a). Interestingly, these specific mutations within the Ser patch strongly inhibited auxin perception.","type":"Results"}],"term_name":"small molecule binding","ec_name":"mutant phenotype evidence used in manual assertion","curator_orcid":"0000-0002-5152-5953","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"30202032","date":"2022-03-08T14:59:42.466Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0000315","curator_id":"esalladini","reference_html":"Auxin sensing is a property of an unstructured domain in the Auxin Response Factor ETTIN of Arabidopsis thaliana. <i> Simonini S, Mas PJ, Mas CMVS, Østergaard L, Hart DJ. </i> Sci Rep, 2018","ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02380r004","ec_ontology":"ECO","end":594,"term_id":"GO:0005515","start":388,"version":4,"statement":[{"text":"Analyses by Y2H revealed the ETT_388-594 construct retained full responsiveness to increases in auxin concentration (Fig. 4A; ETT-BD and ES-BD and ETT-388-594-BD rows) confirming it to be a stable and purifiable form of the ETT auxin-responsive domain capable of binding the Arabidopsis INDEHISCENT (IND) transcription factor used as the bait in the assay.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"O81313","partner_end":null}],"term_name":"protein binding","ec_name":"yeast 2-hybrid evidence used in manual assertion","reference_html":"Auxin sensing is a property of an unstructured domain in the Auxin Response Factor ETTIN of Arabidopsis thaliana. <i> Simonini S, Mas PJ, Mas CMVS, Østergaard L, Hart DJ. </i> Sci Rep, 2018","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"30202032","date":"2022-03-08T14:59:31.003Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005805","curator_id":"esalladini","curator_orcid":"0000-0002-5152-5953","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","uniref100":"UniRef100_O23661","date":"2019-11-28T07:58:17.985Z","acc":"O23661","name":"Auxin response factor 3","length":608,"organism":"Arabidopsis thaliana","dataset":[],"UniParc":"UPI00000AADC5","genes":[{"name":{"value":"ARF3"},"synonyms":[{"value":"ETT"}],"orfNames":[{"value":"T1B8.30"}],"olnNames":[{"value":"At2g33860"}]}],"alphafold_very_low_content":0.45723684210526316,"disorder_content":0.3404605263157895,"disprot_consensus":{"full":[{"start":388,"end":594,"type":"D"}],"Structural state":[{"start":388,"end":594,"type":"D"}],"Molecular function":[{"start":388,"end":594,"type":"F"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MSLSFCGNNISSYNINDGVLQNSCFVDALNLVPHVFLLFITFPILFIGWGSQSSKVQIHHNTWLHFPGHNLRWILTFALLFVHVCEIAEGIVSDSRRESRHLHLFMPAVMGFVATTTSIVYYHNIETSNFPKLLLALFLYWVMAFITKTIKLVKYCQSGLDISNLRFCITGMMVILNGLLMAVEINVIRVRRYVFFMNPQKVKPPEDLQDLGVRFLQPFVNLLSKATYWWMNTLIISAHKKPIDLKAIGKLPIAMRAVTNYVCLKDAYEEQKKKVADHPNRTPSIWLAMYRAFGRPILLSSTFRYLADLLGFAGPLCISGIVQRVNETQNGTNNTTGISETLSSKEFLENAYVLAVLLFLALILQRTFLQASYYVTIETGINLRGALLAMIYNKILRLSTSNLSMGEMTLGQINNLVAIETNQLMWFLFLCPNLWAMPVQIIMGVILLYNLLGSSALVGAAVIVLLAPIQYFIATKLAEAQKSTLDYSTERLKKTNEILKGIKLLKLYAWEHIFCKSVEETRMKELSSLKTFALYTSLSIFMNAAIPIAAVLATFVTHAYASGNNLKPAEAFASLSLFHILVTPLFLLSTVVRFAVKAIISVQKLNEFLLSDEIGDDSWRTGESSLPFESCKKHTGVQPKTINRKQPGRYHLDSYEQSTRRLRPAETEDIAIKVTNGYFSWGSGLATLSNIDIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNVNESEPSFEATRSRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLTHADWIIAMKDGSVLREGTLKDIQTKDVELYEHWKTLMNRQDQELEKDMEADQTTLERKTLRRAMYSREAKAQMEDEDEEEEEEEDEDDNMSTVMRLRTKMPWKTCWRYLTSGGFFLLILMIFSKLLKHSVIVAIDYWLATWTSEYSINNTGKADQTYYVAGFSILCGAGIFLCLVTSLTVEWMGLTAAKNLHHNLLNKIILGPIRFFDTTPLGLILNRFSADTNIIDQHIPPTLESLTRSTLLCLSAIGMISYATPVFLVALLPLGVAFYFIQKYFRVASKDLQELDDSTQLPLLCHFSETAEGLTTIRAFRHETRFKQRMLELTDTNNIAYLFLSAANRWLEVRTDYLGACIVLTASIASISGSSNSGLVGLGLLYALTITNYLNWVVRNLADLEVQMGAVKKVNSFLTMESENYEGTMDPSQVPEHWPQEGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILTADLVIVMKRGNILEYDTPESLLAQENGVFASFVRADM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"","disprot_id":"DP02381","ncbi_taxon_id":9606,"regions_counter":6,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":669,"region_id":"DP02381r001","start":618,"term_id":"IDPO:0000002","statement":[{"text":"Two-dimensional 15N-HSQC spectra of the non-phosphorylated and phosphorylated L1\nlinker have limited dispersion in the 1H dimension, with almost all backbone amide 1H\nresonances having chemical shifts of 7.9 to 8.6 ppm, and sharp resonances (Figure 1).\nResonances for L1 linker residues in spectra of L1-NBD1 also display limited dispersion and sharp line shapes (42). The limited dispersion of resonances in the 1H dimension is a\ncharacteristic feature in the NMR spectra of disordered proteins and IDRs, in which each amide 1H nucleus experiences on average the same chemical environment.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30273482","version":2,"reference_html":"Phosphorylation Alters the Residual Structure and Interactions of the Regulatory L1 Linker Connecting NBD1 to the Membrane-Bound Domain in SUR2B. <i> Sooklal CR, López-Alonso JP, Papp N, Kanelis V. </i> Biochemistry, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T11:44:28.738Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":669,"region_id":"DP02381r002","start":618,"term_id":"IDPO:0000002","statement":[{"text":"Additionally, the L1 linker elutes from a size exclusion column at the volume expected for elution of globular proteins of ~14 kDa, rather than proteins of ~6 kDa that are the size of the L1 linker (Supplementary Figure 4). The earlier elution of the L1 linker is also consistent with its disordered nature and larger hydrodynamic radii of the ensemble of the L1 linker conformers compared to globular proteins of the same molecular weight","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"chromatography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30273482","version":2,"reference_html":"Phosphorylation Alters the Residual Structure and Interactions of the Regulatory L1 Linker Connecting NBD1 to the Membrane-Bound Domain in SUR2B. <i> Sooklal CR, López-Alonso JP, Papp N, Kanelis V. </i> Biochemistry, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T11:44:27.976Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":669,"region_id":"DP02381r003","start":618,"term_id":"IDPO:0000002","statement":[{"text":"The CD spectra of the non-phosphorylated and phosphorylated L1 linker are typical of\nwhat is observed for primarily disordered proteins","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30273482","version":2,"reference_html":"Phosphorylation Alters the Residual Structure and Interactions of the Regulatory L1 Linker Connecting NBD1 to the Membrane-Bound Domain in SUR2B. <i> Sooklal CR, López-Alonso JP, Papp N, Kanelis V. </i> Biochemistry, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006200","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T11:44:32.490Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":669,"region_id":"DP02381r004","start":618,"term_id":"IDPO:0000045","statement":[{"text":"Phosphorylation of the L1 linker, by protein kinase A, disrupts its interactions with\nNBD1, which increases the MgATP affinity of NBD1 and KATP channel gating. ","type":"Abstract"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30273482","version":2,"reference_html":"Phosphorylation Alters the Residual Structure and Interactions of the Regulatory L1 Linker Connecting NBD1 to the Membrane-Bound Domain in SUR2B. <i> Sooklal CR, López-Alonso JP, Papp N, Kanelis V. </i> Biochemistry, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"phosphorylation display site","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":669,"region_id":"DP02381r005","start":618,"term_id":"GO:0098772","statement":[{"text":"Phosphorylation of the L1 linker, by protein kinase A, disrupts its interactions with\nNBD1, which increases the MgATP affinity of NBD1 and KATP channel gating. ","type":"Abstract"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30273482","version":3,"reference_html":"Phosphorylation Alters the Residual Structure and Interactions of the Regulatory L1 Linker Connecting NBD1 to the Membrane-Bound Domain in SUR2B. <i> Sooklal CR, López-Alonso JP, Papp N, Kanelis V. </i> Biochemistry, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"molecular function regulator","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":669,"region_id":"DP02381r006","start":618,"term_id":"GO:0005515","statement":[{"text":"Phosphorylation of the L1 linker, by protein kinase A, disrupts its interactions with the\nNBD1 domain, which increases the MgATP affinity of NBD1 and KATP channel gating. ","type":"Abstract"},{"text":"Spectroscopic and biochemical studies indicate that the L1 linker possesses residual secondary and compact structure that is disrupted with phosphorylation, which leads to differential interactions of the nonphosphorylated and phosphorylated L1 linker with NBD1.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30273482","version":3,"reference_html":"Phosphorylation Alters the Residual Structure and Interactions of the Regulatory L1 Linker Connecting NBD1 to the Membrane-Bound Domain in SUR2B. <i> Sooklal CR, López-Alonso JP, Papp N, Kanelis V. </i> Biochemistry, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"protein binding","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","uniref100":"","date":"2019-11-28T09:28:19.688Z","acc":"O60706-2","name":"Isoform SUR2B of ATP-binding cassette sub-family C member 9","length":1549,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000013D13F","genes":[{"name":{"value":"ABCC9"},"synonyms":[{"value":"SUR2"}]}],"disorder_content":0.03357004519044545,"disprot_consensus":{"full":[{"start":618,"end":669,"type":"D"}],"Structural state":[{"start":618,"end":669,"type":"D"}],"Disorder function":[{"start":618,"end":669,"type":"F"}],"Molecular function":[{"start":618,"end":669,"type":"F"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF00152","name":"tRNA synthetases class II (D, K and N)","start":222,"end":573},{"id":"PF01336","name":"OB-fold nucleic acid binding domain","start":127,"end":206}]},"uniref50":"UniRef50_Q15046","sequence":"MAAVQAAEVKVDGSEPKLSKNELKRRLKAEKKVAEKEAKQKELSEKQLSQATAAATNHTTDNGVGPEEESVDPNQYYKIRSQAIHQLKVNGEDPYPHKFHVDISLTDFIQKYSHLQPGDHLTDITLKVAGRIHAKRASGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFIHINNKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYHPDGPEGQAYDVDFTPPFRRINMVEELEKALGMKLPETNLFETEETRKILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKEGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFPAMKPEDKKENVATTDTLESTTVGTSV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q15046","disprot_id":"DP02382","ncbi_taxon_id":9606,"regions_counter":6,"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":70,"region_id":"DP02382r002","start":1,"term_id":"IDPO:0000002","statement":[{"text":"Interestingly, the apparent molecular weight (MW) of hRID in the gel was two-fold higher than the calculated MW (8.3 kDa). This phenomenon might result from the intrinsic disorder of the hRID structure","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30282926","version":2,"reference_html":"Nucleic Acid-Dependent Structural Transition of the Intrinsically Disordered N-Terminal Appended Domain of Human Lysyl-tRNA Synthetase. <i> Kwon SB, Yu JE, Park C, Lee J, Seong BL. </i> Int J Mol Sci, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007689","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T17:40:12.702Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":70,"region_id":"DP02382r003","start":1,"term_id":"IDPO:0000011","statement":[{"text":"Upon polyP addition, the circular dichroism (CD) score at 225 nm was decreased, and the CD score at 190 nm was increased, indicating that helical content increased.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30282926","version":2,"reference_html":"Nucleic Acid-Dependent Structural Transition of the Intrinsically Disordered N-Terminal Appended Domain of Human Lysyl-tRNA Synthetase. <i> Kwon SB, Yu JE, Park C, Lee J, Seong BL. </i> Int J Mol Sci, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006200","term_name":"disorder to order","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T17:44:38.074Z"}}],"released":"2021_06","uniref100":"UniRef100_Q15046","date":"2019-11-28T10:51:27.407Z","acc":"Q15046","name":"Lysine--tRNA ligase","length":597,"organism":"Homo sapiens","dataset":["NDDs-related proteins","RNA-binding proteins"],"UniParc":"UPI000016AE21","genes":[{"name":{"value":"KARS1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6215","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6215"}}]},"synonyms":[{"value":"KARS"},{"value":"KIAA0070"}]}],"alphafold_very_low_content":0.08207705192629816,"disorder_content":0.11725293132328309,"disprot_consensus":{"full":[{"start":1,"end":70,"type":"T"}],"Structural state":[{"start":1,"end":70,"type":"D"}],"Structural transition":[{"start":1,"end":70,"type":"T"}]}},{"features":{"gene3D":[{"start":135,"end":281,"id":"G3DSA:3.30.505.10","name":"SH2 domain"}],"pfam":[{"id":"PF00017","name":"SH2 domain","start":144,"end":226},{"id":"PF00018","name":"SH3 domain","start":84,"end":130},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":262,"end":511}]},"uniref50":"UniRef50_P08631","sequence":"MGGRSSCEDPGCPRDEERAPRMGCMKSKFLQVGGNTFSKTETSASPHCPVYVPDPTSTIKPGPNSHNSNTPGIREAGSEDIIVVALYDYEAIHHEDLSFQKGDQMVVLEESGEWWKARSLATRKEGYIPSNYVARVDSLETEEWFFKGISRKDAERQLLAPGNMLGSFMIRDSETTKGSYSLSVRDYDPRQGDTVKHYKIRTLDNGGFYISPRSTFSTLQELVDHYKKGNDGLCQKLSVPCMSSKPQKPWEKDAWEIPRESLKLEKKLGAGQFGEVWMATYNKHTKVAVKTMKPGSMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEPIYIITEFMAKGSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPENCPEELYNIMMRCWKNRPEERPTFEYIQSVLDDFYTATESQYQQQP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P08631","disprot_id":"DP02383","ncbi_taxon_id":9606,"regions_counter":6,"creator":"rpancsa","regions":[{"region_id":"DP02383r001","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T11:45:10.343Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":79,"term_id":"IDPO:0000002","start":2,"version":2,"statement":[{"text":"The anticipated intrinsic disorder of these constructs (Amata et al. 2014) was evident in the low chemical shift dispersion in the 1H dimension (Fig.  1)","type":"Results"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30284668","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"27554"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"rpancsa","reference_html":"<sup>1</sup>H, <sup>15</sup>N, and <sup>13</sup>C resonance assignments of the intrinsically disordered SH4 and Unique domains of Hck. <i> Pond MP, Blachowicz L, Roux B. </i> Biomol NMR Assign, 2019","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Biological process","ec_ontology":"ECO","end":79,"region_id":"DP02383r002","start":2,"term_id":"GO:0051179","statement":[{"text":"the intrinsically disordered nature of the SH4 and Unique domains has resulted in a lack of information for this important region of the protein that is responsible for membrane association","type":"Abstract"},{"text":"These enzymes are often found anchored to the intracellular side of the membrane via lipidation of the SH4 domain and are integral components of signaling cascades localized at the cell surface.","type":"Abstract"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30284668","version":3,"reference_html":"<sup>1</sup>H, <sup>15</sup>N, and <sup>13</sup>C resonance assignments of the intrinsically disordered SH4 and Unique domains of Hck. <i> Pond MP, Blachowicz L, Roux B. </i> Biomol NMR Assign, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"localization","curator_orcid":"0000-0003-0849-9312","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":6,"region_id":"DP02383r003","start":2,"term_id":"IDPO:0000043","statement":[{"text":"Both isoforms may be myristoylated at the N-terminus but p59Hck can also be palmitoylated on Cys3. The variable acylation is thought to be a major determinant in localizations within the cell: p59Hck is mainly associated with the plasma membrane and p61Hck with lysosomal membranes.","type":"Introduction"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30284668","version":2,"reference_html":"<sup>1</sup>H, <sup>15</sup>N, and <sup>13</sup>C resonance assignments of the intrinsically disordered SH4 and Unique domains of Hck. <i> Pond MP, Blachowicz L, Roux B. </i> Biomol NMR Assign, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"myristoylation display site","curator_orcid":"0000-0003-0849-9312","disprot_namespace":"Disorder function"},{"term_namespace":"Biological process","ec_ontology":"ECO","end":21,"region_id":"DP02383r004","start":2,"term_id":"GO:0051179","statement":[{"text":"The two dominant isoforms of human Hck are referred to as p59Hck and p61Hck. The longer p61 isoform contains an additional 21 residues at the N-terminal end (MGGRSSCEDPGCPRDEERAPR), and is derived from an alternate start codon of the same mRNA. Both isoforms may be myristoylated at the N-terminus but p59Hck can also be palmitoylated on Cys3. The variable acylation is thought to be a major determinant in localizations within the cell: p59Hck is mainly associated with the plasma membrane and p61Hck with lysosomal membranes.","type":"Introduction"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30284668","version":3,"reference_html":"<sup>1</sup>H, <sup>15</sup>N, and <sup>13</sup>C resonance assignments of the intrinsically disordered SH4 and Unique domains of Hck. <i> Pond MP, Blachowicz L, Roux B. </i> Biomol NMR Assign, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"localization","curator_orcid":"0000-0003-0849-9312","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"term_namespace":"Biological process","ec_ontology":"ECO","end":79,"region_id":"DP02383r005","start":2,"term_id":"GO:0051179","statement":[{"text":"As in our previous work [39], we study an unmyristoylated construct of the Hck SH4-U domains containing residues 2–79, hereafter referred to as SH 4   UHck− (previously referred to as p61HckSH 4   U−). Experimental characterization of the average spatial distribution of SH 4   UHck− at the membrane surface is carried out using nuclear magnetic resonance (NMR) and neutron reflectometry (NR) experiments. Restrained-ensemble molecular dynamics (re-MD) simulations are then utilized to generate statistical models of membrane-bound Hck. The results confirm an interaction between the SH4 domain and acidic lipids, and yield an atomically detailed model of membrane bound SH 4   UHck−.","type":"Introduction"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31877324","version":3,"reference_html":"Membrane Anchoring of Hck Kinase via the Intrinsically Disordered SH4-U and Length Scale Associated with Subcellular Localization. <i> Pond MP, Eells R, Treece BW, Heinrich F, Lösche M, Roux B. </i> J Mol Biol, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"localization","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":79,"region_id":"DP02383r006","start":2,"term_id":"GO:0008289","statement":[{"text":"As in our previous work [39], we study an unmyristoylated construct of the Hck SH4-U domains containing residues 2–79, hereafter referred to as SH 4   UHck− (previously referred to as p61HckSH 4   U−). Experimental characterization of the average spatial distribution of SH 4   UHck− at the membrane surface is carried out using nuclear magnetic resonance (NMR) and neutron reflectometry (NR) experiments. Restrained-ensemble molecular dynamics (re-MD) simulations are then utilized to generate statistical models of membrane-bound Hck. The results confirm an interaction between the SH4 domain and acidic lipids, and yield an atomically detailed model of membrane bound SH 4   UHck−.","type":"Introduction"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31877324","version":3,"reference_html":"Membrane Anchoring of Hck Kinase via the Intrinsically Disordered SH4-U and Length Scale Associated with Subcellular Localization. <i> Pond MP, Eells R, Treece BW, Heinrich F, Lösche M, Roux B. </i> J Mol Biol, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"lipid binding","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","uniref100":"UniRef100_P08631","date":"2019-11-28T11:41:21.870Z","acc":"P08631","name":"Tyrosine-protein kinase HCK","length":526,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000053F913","genes":[{"name":{"value":"HCK"}}],"alphafold_very_low_content":0.1596958174904943,"disorder_content":0.1482889733840304,"disprot_consensus":{"full":[{"start":2,"end":79,"type":"D"}],"Structural state":[{"start":2,"end":79,"type":"D"}],"Biological process":[{"start":2,"end":79,"type":"F"}],"Disorder function":[{"start":2,"end":6,"type":"F"}],"Molecular function":[{"start":2,"end":79,"type":"F"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF09282","name":"Mago binding","start":11,"end":35}]},"uniref50":"UniRef50_P82804","sequence":"MSTYLQSSEGKFIPATKRPDGTWRKARRVKDGYVPQEEVPLYESKGKQFVAQRQAGVPPGMCPLLAAESKKEREKQERTRAKKQEKESGRQPKAPAPGVLVMPPSTCPPPKVSQQQQQQQQQPSGSRDINSISKTLEDTLKLDAAQEVVDPAKQLKKLRKKIREIEQIESRIQAGEQKKLDKDQLDKVKKKSEILRQIKDLESTPRS","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_P82804","disprot_id":"DP02384","ncbi_taxon_id":7227,"regions_counter":4,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":58,"region_id":"DP02384r001","start":33,"term_id":"IDPO:0000002","statement":[{"text":"Although the crystallized construct contains 25 additional C-terminal residues, these are disordered in the structure and do not contribute to Mago–Y14 binding","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14968132","version":2,"reference_html":"Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex. <i> Bono F, Ebert J, Unterholzner L, Güttler T, Izaurralde E, Conti E. </i> EMBO Rep, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1RK8"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","uniref100":"UniRef100_P82804","date":"2019-11-29T09:27:17.655Z","acc":"P82804","name":"Partner of Y14 and mago","length":207,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI0000124769","genes":[{"name":{"value":"Pym","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0034918","url":"http://flybase.org/reports/FBgn0034918.html"}}]},"synonyms":[{"value":"wibg","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0034918","url":"http://flybase.org/reports/FBgn0034918.html"}}]}],"orfNames":[{"value":"CG30176","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0034918","url":"http://flybase.org/reports/FBgn0034918.html"}}]}]}],"alphafold_very_low_content":0.08695652173913043,"disorder_content":0.12560386473429952,"disprot_consensus":{"full":[{"start":33,"end":58,"type":"D"}],"Structural state":[{"start":33,"end":58,"type":"D"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF00018","name":"SH3 domain","start":457,"end":501},{"id":"PF07815","name":"Abl-interactor HHR","start":93,"end":164},{"id":"PF27594","name":"Abl interactor protein","start":4,"end":79}]},"uniref50":"UniRef50_Q9NYB9","sequence":"MAELQMLLEEEIPGGRRALFDSYTNLERVADYCENNYIQSADKQRALEETKAYTTQSLASVAYLINTLANNVLQMLDIQASQLRRMESSINHISQTVDIHKEKVARREIGILTTNKNTSRTHKIIAPANLERPVRYIRKPIDYTILDDIGHGVKWLLRFKVSTQNMKMGGLPRTTPPTQKPPSPPMSGKGTLGRHSPYRTLEPVRPPVVPNDYVPSPTRNMAPSQQSPVRTASVNQRNRTYSSSGSSGGSHPSSRSSSRENSGSGSVGVPIAVPTPSPPSVFPAPAGSAGTPPLPATSASAPAPLVPATVPSSTAPNAAAGGAPNLADGFTSPTPPVVSSTPPTGHPVQFYSMNRPASRHTPPTIGGSLPYRRPPSITSQTSLQNQMNGGPFYSQNPVSDTPPPPPPVEEPVFDESPPPPPPPEDYEEEEAAVVEYSDPYAEEDPPWAPRSYLEKVVAIYDYTKDKEDELSFQEGAIIYVIKKNDDGWYEGVMNGVTGLFPGNYVESIMHYSE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9NYB9","disprot_id":"DP02386","ncbi_taxon_id":9606,"regions_counter":1,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":513,"region_id":"DP02386r001","reference_id":"24439376","start":156,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"We next sought to determine where and how the WIRS motif binds to the WRC. For this, we determined the 2.43-Å crystal structure of a complex cocrystallized from a variant of the WIRS-containing peptide (WGAERSM∗STFGKEKA, M∗ for selenomethionine, Figure 1B) and a minimal inhibited WRC, which lacks the C terminus of Abi and the proline-rich region of WAVE, miniWRC (Figure 2 and Table S1) (Chen et al., 2010).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"The WAVE regulatory complex links diverse receptors to the actin cytoskeleton. <i> Chen B, Brinkmann K, Chen Z, Pak CW, Liao Y, Shi S, Henry L, Grishin NV, Bogdan S, Rosen MK. </i> Cell, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4N78"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","uniref100":"UniRef100_Q9NYB9","date":"2019-11-29T10:00:53.364Z","acc":"Q9NYB9","name":"Abl interactor 2","length":513,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000071313","genes":[{"name":{"value":"ABI2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"28397838","url":"http://www.ncbi.nlm.nih.gov/pubmed/28397838","alternativeUrl":"https://europepmc.org/abstract/MED/28397838"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:24011","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:24011"}}]},"synonyms":[{"value":"ARGBPIA"}]}],"alphafold_very_low_content":0.4678362573099415,"disorder_content":0.6978557504873294,"disprot_consensus":{"full":[{"start":156,"end":513,"type":"D"}],"Structural state":[{"start":156,"end":513,"type":"D"}]}},{"features":{"gene3D":[{"start":1,"end":117,"id":"G3DSA:2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":372,"end":413,"id":"G3DSA:1.20.5.1160","name":"Vasodilator-stimulated phosphoprotein"}],"pfam":[{"id":"PF00568","name":"WH1 domain","start":4,"end":105},{"id":"PF08776","name":"VASP tetramerisation domain","start":376,"end":409}]},"uniref50":"UniRef50_Q9UI08","sequence":"MSEQSICQARASVMVYDDTSKKWVPIKPGQQGFSRINIYHNTASSTFRVVGVKLQDQQVVINYSIVKGLKYNQATPTFHQWRDARQVYGLNFASKEEATTFSNAMLFALNIMNSQEGGPSTQRQVQNGPSPEEMDIQRRQVMEQQHRQESLERRISATGPILPPGHPSSAASTTLSCSGPPPPPPPPVPPPPTGSTPPPPPPLPAGGAQGTNHDESSASGLAAALAGAKLRRVQRPEDASGGSSPSGTSKSDANRASSGGGGGGLMEEMNKLLAKRRKAASQTDKPADRKEDESQTEDPSTSPSPGTRATSQPPNSSEAGRKPWERSNSVEKPVSSLLSRTPSVAKSPEAKSPLQSQPHSRVKPAGSVNDVGLDALDLDRMKQEILEEVVRELHKVKEEIIDAIRQELSGISTT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P70429","disprot_id":"DP02387","ncbi_taxon_id":10090,"regions_counter":1,"creator":"fquaglia","regions":[{"region_id":"DP02387r001","ec_ontology":"ECO","end":130,"term_id":"IDPO:0000002","start":114,"version":2,"statement":[{"text":"The lack of density corresponding to the N- and C-terminal residues of the peptides is consistent with deletion studies showing no significant effect on binding unless residues within the FPPPP core are deleted","type":"Article"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10404224","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1QC6"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function. <i> Fedorov AA, Fedorov E, Gertler F, Almo SC. </i> Nat Struct Biol, 1999","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","uniref100":"UniRef100_P70429","date":"2019-11-29T10:16:28.950Z","acc":"P70429","name":"Ena/VASP-like protein","length":414,"organism":"Mus musculus","dataset":[],"UniParc":"UPI00000278C1","genes":[{"name":{"value":"Evl"}}],"alphafold_very_low_content":0.3671497584541063,"disorder_content":0.04106280193236715,"disprot_consensus":{"full":[{"start":114,"end":130,"type":"D"}],"Structural state":[{"start":114,"end":130,"type":"D"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":77,"end":327}]},"uniref50":"UniRef50_Q96GD4","sequence":"MAQKENSYPWPYGRQTAPSGLSTLPQRVLRKEPVTPSALVLMSRSNVQPTAAPGQKVMENSSGTPDILTRHFTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERLPLAQVSAHPWVRANSRRVLPPSALQSVA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q96GD4","disprot_id":"DP02389","ncbi_taxon_id":9606,"regions_counter":6,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":236,"region_id":"DP02389r001","start":221,"term_id":"IDPO:0000002","statement":[{"text":"In the Aurora B:INCENP complex, the activation segment is disordered after the DFG motif, including the phosphorylation site Thr232. The C-terminal part of the activation segment is dislodged from the lower lobe and interacts with a deep groove generated by the displaced activation segment in the interacting protomer. Overall, there is a buried surface area of interaction of 3460 Å2, and the segment is anchored mainly by aromatic and hydrophobic interactions of Y239, L237, Pro242, and I245","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22920039","version":2,"reference_html":"Crystal structure of human aurora B in complex with INCENP and VX-680. <i> Elkins JM, Santaguida S, Musacchio A, Knapp S. </i> J Med Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4AF3"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":234,"region_id":"DP02389r002","start":230,"term_id":"IDPO:0000045","statement":[{"text":"In the Aurora B:INCENP complex, the activation segment is disordered after the DFG motif, including the phosphorylation site Thr232. ","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22920039","version":2,"reference_html":"Crystal structure of human aurora B in complex with INCENP and VX-680. <i> Elkins JM, Santaguida S, Musacchio A, Knapp S. </i> J Med Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4AF3"}],"term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":234,"region_id":"DP02389r003","start":230,"term_id":"IDPO:0000045","statement":[{"text":"We report here evidence that human Aurora-B is phosphorylated at Thr-232 through interaction with the INCENP in vivo. This phosphorylation of Thr-232 occurs by means of an autophosphorylation mechanism and is essential for the Aurora-B kinase activity. ","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"spectrometry evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14722118","version":2,"reference_html":"Autophosphorylation of a newly identified site of Aurora-B is indispensable for cytokinesis. <i> Yasui Y, Urano T, Kawajiri A, Nagata K, Tatsuka M, Saya H, Furukawa K, Takahashi T, Izawa I, Inagaki M. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007731","term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"region_id":"DP02389r004","ec_ontology":"ECO","end":236,"term_id":"GO:0005515","start":221,"version":3,"statement":[{"text":"In the Aurora B:INCENP complex, the activation segment is disordered after the DFG motif, including the phosphorylation site Thr232. The C-terminal part of the activation segment is dislodged from the lower lobe and interacts with a deep groove generated by the displaced activation segment in the interacting protomer. Overall, there is a buried surface area of interaction of 3460 Å2, and the segment is anchored mainly by aromatic and hydrophobic interactions of Y239, L237, Pro242, and I245","type":"Results"},{"text":"we determined the structure of human Aurora B kinase domain, in complex with the C-terminal IN-box section of human INCENP (residues 835–903)","type":"Introduction"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9NQS7","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"22920039","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4AF3"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"fquaglia","reference_html":"Crystal structure of human aurora B in complex with INCENP and VX-680. <i> Elkins JM, Santaguida S, Musacchio A, Knapp S. </i> J Med Chem, 2012","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":236,"region_id":"DP02389r006","start":221,"term_id":"GO:0098772","statement":[{"text":"We report here evidence that human Aurora-B is phosphorylated at Thr-232 through interaction with the INCENP in vivo. This phosphorylation of Thr-232 occurs by means of an autophosphorylation mechanism and is essential for the Aurora-B kinase activity.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"14722118","version":3,"reference_html":"Autophosphorylation of a newly identified site of Aurora-B is indispensable for cytokinesis. <i> Yasui Y, Urano T, Kawajiri A, Nagata K, Tatsuka M, Saya H, Furukawa K, Takahashi T, Izawa I, Inagaki M. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","term_name":"molecular function regulator","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","uniref100":"UniRef100_Q96GD4","date":"2019-12-02T10:08:00.167Z","acc":"Q96GD4","name":"Aurora kinase B","length":344,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000136107","genes":[{"name":{"value":"AURKB"},"synonyms":[{"value":"AIK2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9858806","url":"http://www.ncbi.nlm.nih.gov/pubmed/9858806","alternativeUrl":"https://europepmc.org/abstract/MED/9858806"}}]},{"value":"AIM1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9809983","url":"http://www.ncbi.nlm.nih.gov/pubmed/9809983","alternativeUrl":"https://europepmc.org/abstract/MED/9809983"}}]},{"value":"AIRK2"},{"value":"ARK2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9514916","url":"http://www.ncbi.nlm.nih.gov/pubmed/9514916","alternativeUrl":"https://europepmc.org/abstract/MED/9514916"}}]},{"value":"STK1"},{"value":"STK12","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9858806","url":"http://www.ncbi.nlm.nih.gov/pubmed/9858806","alternativeUrl":"https://europepmc.org/abstract/MED/9858806"}}]},{"value":"STK5"}]}],"alphafold_very_low_content":0.21511627906976744,"disorder_content":0.046511627906976744,"disprot_consensus":{"full":[{"start":221,"end":236,"type":"D"}],"Structural state":[{"start":221,"end":236,"type":"D"}],"Disorder function":[{"start":230,"end":234,"type":"F"}],"Molecular function":[{"start":221,"end":236,"type":"F"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF03941","name":"Inner centromere protein, ARK binding region","start":825,"end":881},{"id":"PF12178","name":"Chromosome passenger complex (CPC) protein INCENP N terminal","start":6,"end":41}]},"uniref50":"UniRef50_Q9NQS7","sequence":"MGTTAPGPIHLLELCDQKLMEFLCNMDNKDLVWLEEIQEEAERMFTREFSKEPELMPKTPSQKNRRKKRRISYVQDENRDPIRRRLSRRKSRSSQLSSRRLRSKDSVEKLATVVGENGSVLRRVTRAAAAAAAATMALAAPSSPTPESPTMLTKKPEDNHTQCQLVPVVEIGISERQNAEQHVTQLMSTEPLPRTLSPTPASATAPTSQGIPTSDEESTPKKSKARILESITVSSLMATPQDPKGQGVGTGRSASKLRIAQVSPGPRDSPAFPDSPWRERVLAPILPDNFSTPTGSRTDSQSVRHSPIAPSSPSPQVLAQKYSLVAKQESVVRRASRRLAKKTAEEPAASGRIICHSYLERLLNVEVPQKVGSEQKEPPEEAEPVAAAEPEVPENNGNNSWPHNDTEIANSTPNPKPAASSPETPSAGQQEAKTDQADGPREPPQSARRKRSYKQAVSELDEEQHLEDEELQPPRSKTPSSPCPASKVVRPLRTFLHTVQRNQMLMTPTSAPRSVMKSFIKRNTPLRMDPKCSFVEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQERLRKAAEAKRLAEQREQERREQERREQERREQERREQERREQERQLAEQERRREQERLQAERELQEREKALRLQKEQLQRELEEKKKKEEQQRLAERQLQEEQEKKAKEAAGASKALNVTVDVQSPACTSYQMTPQGHRAPPKINPDNYGMDLNSDDSTDDEAHPRKPIPTWARGTPLSQAIIHQYYHPPNLLELFGTILPLDLEDIFKKSKPRYHKRTSSAVWNSPPLQGARVPSSLAYSLKKH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9NQS7","disprot_id":"DP02390","ncbi_taxon_id":9606,"regions_counter":4,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":903,"region_id":"DP02390r001","start":883,"term_id":"IDPO:0000002","statement":[{"text":"Therefore, a bacterial expression construct for the C-terminal part of human INCENP was prepared, spanning residues 835–903, which is the Aurora-binding region.","type":"Results"},{"text":"To provide a model for structure-based design and to gain insight into the molecular mechanism of human Aurora B activation, we determined the structure of human Aurora B kinase domain, in complex with the C-terminal IN-box section of human INCENP (residues 835–903) and the type II inhibitor 1 (Figure ​(Figure11).","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22920039","version":2,"reference_html":"Crystal structure of human aurora B in complex with INCENP and VX-680. <i> Elkins JM, Santaguida S, Musacchio A, Knapp S. </i> J Med Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4AF3"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-22T19:35:44.011Z"}},{"region_id":"DP02390r002","ec_ontology":"ECO","end":903,"term_id":"GO:0005515","start":853,"version":3,"statement":[{"text":"Therefore, a bacterial expression construct for the C-terminal part of human INCENP was prepared, spanning residues 835–903, which is the Aurora-binding region.","type":"Results"},{"text":"To provide a model for structure-based design and to gain insight into the molecular mechanism of human Aurora B activation, we determined the structure of human Aurora B kinase domain, in complex with the C-terminal IN-box section of human INCENP (residues 835–903) and the type II inhibitor 1 (Figure ​(Figure11).","type":"Introduction"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q96GD4","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"22920039","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4AF3"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"fquaglia","reference_html":"Crystal structure of human aurora B in complex with INCENP and VX-680. <i> Elkins JM, Santaguida S, Musacchio A, Knapp S. </i> J Med Chem, 2012","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-22T19:35:46.924Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":896,"region_id":"DP02390r003","start":892,"term_id":"IDPO:0000045","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"We next evaluated whether or not the TSS motif (T893, S894, S895) within the IN box domain of INCENP is involved in Aurora-C activation","type":"Results"},{"text":"In vitro kinase assays on pulled down protein complexes from Sf-9 cells co-infected with WT or 3A mutant of INCENP together with the Aurora-B and -C kinases also confirmed the role of the TSS motif phosphorylation of INCENP in the activation of the two kinases","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"mass spectrometry evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27332895","version":2,"reference_html":"Aurora-C Interactions with Survivin and INCENP Reveal Shared and Distinct Features Compared with Aurora-B Chromosome Passenger Protein Complex. <i> Sasai K, Katayama H, Hawke DH, Sen S. </i> PLoS One, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001230","term_name":"phosphorylation display site","ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-22T19:35:39.902Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":903,"region_id":"DP02390r004","start":883,"term_id":"GO:0140677","statement":[{"text":"We next evaluated whether or not the TSS motif (T893, S894, S895) within the IN box domain of INCENP is involved in Aurora-C activation","type":"Results"},{"text":"In vitro kinase assays on pulled down protein complexes from Sf-9 cells co-infected with WT or 3A mutant of INCENP together with the Aurora-B and -C kinases also confirmed the role of the TSS motif phosphorylation of INCENP in the activation of the two kinases","type":"Introduction"}],"curator_id":"esalladini","released":"2022_03","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"27332895","version":4,"reference_html":"Aurora-C Interactions with Survivin and INCENP Reveal Shared and Distinct Features Compared with Aurora-B Chromosome Passenger Protein Complex. <i> Sasai K, Katayama H, Hawke DH, Sen S. </i> PLoS One, 2016","date":"2022-03-08T14:56:54.816Z","reference_source":"pmid","ec_id":"ECO:0006077","term_name":"molecular function activator activity","curator_orcid":"0000-0002-5152-5953","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q96GD4","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-22T19:35:45.341Z"}}],"released":"2020_12","uniref100":"UniRef100_Q9NQS7","date":"2019-12-02T10:37:43.374Z","acc":"Q9NQS7","name":"Inner centromere protein","length":918,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI000006D10F","genes":[{"name":{"value":"INCENP"}}],"alphafold_very_low_content":0.4662309368191721,"disorder_content":0.02287581699346405,"disprot_consensus":{"full":[{"start":853,"end":882,"type":"F"},{"start":883,"end":903,"type":"D"}],"Structural state":[{"start":883,"end":903,"type":"D"}],"Molecular function":[{"start":853,"end":903,"type":"F"}],"Disorder function":[{"start":892,"end":896,"type":"F"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF04959","name":"Arsenite-resistance protein 2","start":436,"end":631},{"id":"PF12066","name":"SERRATE/Ars2, N-terminal domain","start":199,"end":280}]},"uniref50":"UniRef50_Q9ZVD0","sequence":"MADVNLPPSDSVDNRLPEKSTSSSPPPPPPSSSLPQQEQEQDQQQLPLRRERDSRERRDERDIERPPPNRRERDRSPLPPPRRDYKRRPSLSPPPPYRDRRHSPPQRRSPPQKRYRRDDNGYDGRRGSPRGGYGPPDRRFGYDHGGGYDREMGGRPGYGDERPHGRFMGRYQDWEGGRGGYGDASNSGNPQRDGLMSYKQFIQELEDDILPSEAERRYQEYKSEYITTQKRAFFNTHKEEDWLKNKYHPTNLLSVIERRNDLAQKVAKDFLLDLQSGTLDLGPAVTALNKSGRTSEPNSEDEAAGVGKRKRHGMGGAKENELLSAAPKAPSFTSDPKRILTDVEQTQALVRKLDSEKKIEENVLQGSETEKSGREKLHSGSTGPVVIIRGLTSVKGLEGVELLDTLVTYLWRVHGLDYYGKVETNEAKGLRHVRAEGKVSDAKGDENESKFDSHWQERLKGQDPLEVMAAKEKIDAAATEALDPHVRKIRDEKYGWKYGCGAKGCTKLFHAAEFVYKHLKLKHTELVTELTTKVREELYFQNYMNDPNAPGGQPATQQSGPRDRPIRRKPSMENRLRDDRGGRRERDGRANGNDRNDRSEDQQRGDNDGGNPGEVGYDAFGGQGGVHVPPFLSDINPPPMLMPVPGAGPLGPFVPAPPEVAMQMFRDPSGPNPPFEGSGRGGPAPFLLSPAFRQDPRRLRSYQDLDAPEEEVTVIDYRSL","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref90":"UniRef90_Q9ZVD0","disprot_id":"DP02392","ncbi_taxon_id":3702,"regions_counter":6,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":324,"region_id":"DP02392r001","start":290,"term_id":"IDPO:0000002","statement":[{"text":"The presence of three disordered loops (residues 290–324, 366–380 and 435–444) in Middle domain implicates its role in protein–protein interaction with SE partners and/or substrates.","type":"Results"},{"text":"SE might possess structural features to sort out the substrates among RNAs rich in variety of size and structures, and to allocate binding partners to form either splicing or dicing complexes","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21685453","version":2,"reference_html":"Molecular insights into miRNA processing by Arabidopsis thaliana SERRATE. <i> Machida S, Chen HY, Adam Yuan Y. </i> Nucleic Acids Res, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3AX1"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:26:38.457Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":444,"region_id":"DP02392r005","start":435,"term_id":"IDPO:0000002","statement":[{"text":"The presence of three disordered loops (residues 290–324, 366–380 and 435–444) in Middle domain implicates its role in protein–protein interaction with SE partners and/or substrates.","type":"Results"},{"text":"SE might possess structural features to sort out the substrates among RNAs rich in variety of size and structures, and to allocate binding partners to form either splicing or dicing complexes","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21685453","version":2,"reference_html":"Molecular insights into miRNA processing by Arabidopsis thaliana SERRATE. <i> Machida S, Chen HY, Adam Yuan Y. </i> Nucleic Acids Res, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3AX1"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:26:38.710Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":380,"region_id":"DP02392r006","start":366,"term_id":"IDPO:0000002","statement":[{"text":"The presence of three disordered loops (residues 290–324, 366–380 and 435–444) in Middle domain implicates its role in protein–protein interaction with SE partners and/or substrates.","type":"Results"},{"text":"SE might possess structural features to sort out the substrates among RNAs rich in variety of size and structures, and to allocate binding partners to form either splicing or dicing complexes","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21685453","version":2,"reference_html":"Molecular insights into miRNA processing by Arabidopsis thaliana SERRATE. <i> Machida S, Chen HY, Adam Yuan Y. </i> Nucleic Acids Res, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3AX1"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T20:26:49.064Z"}}],"released":"2021_06","uniref100":"UniRef100_Q9ZVD0","date":"2019-12-02T11:41:01.347Z","acc":"Q9ZVD0","name":"Serrate RNA effector molecule","length":720,"organism":"Arabidopsis thaliana","dataset":["Condensates-related proteins","RNA-binding proteins"],"UniParc":"UPI00000AC10E","genes":[{"name":{"value":"SE"},"orfNames":[{"value":"T20P8.15"}],"olnNames":[{"value":"At2g27100"}]}],"alphafold_very_low_content":0.4597222222222222,"disorder_content":0.08333333333333333,"disprot_consensus":{"full":[{"start":290,"end":324,"type":"D"},{"start":366,"end":380,"type":"D"},{"start":435,"end":444,"type":"D"}],"Structural state":[{"start":290,"end":324,"type":"D"},{"start":366,"end":380,"type":"D"},{"start":435,"end":444,"type":"D"}]}},{"features":{"gene3D":[{"start":109,"end":188,"id":"G3DSA:3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"}],"pfam":[{"id":"PF00856","name":"SET domain","start":343,"end":445},{"id":"PF20826","name":"PhD finger domain","start":117,"end":164}]},"uniref50":"UniRef50_Q8IZD2","sequence":"MSIVIPLGVDTAETSYLEMAAGSEPESVEASPVVVEKSNSYPHQLYTSSSHHSHSYIGLPYADHNYGARPPPTPPASPPPSVLISKNEVGIFTTPNFDETSSATTISTSEDGSYGTDVTRCICGFTHDDGYMICCDKCSVWQHIDCMGIDRQHIPDTYLCERCQPRNLDKERAVLLQRRKRENMSDGDTSATESGDEVPVELYTAFQHTPTSITLTASRVSKVNDKRRKKSGEKEQHISKCKKAFREGSRKSSRVKGSAPEIDPSSDGSNFGWETKIKAWMDRYEEANNNQYSEGVQREAQRIALRLGNGNDKKEMNKSDLNTNNLLFKPPVESHIQKNKKILKSAKDLPPDALIIEYRGKFMLREQFEANGYFFKRPYPFVLFYSKFHGLEMCVDARTFGNEARFIRRSCTPNAEVRHEIQDGTIHLYIYSIHSIPKGTEITIAFDFDYGNCKYKVDCACLKENPECPVLKRSSESMENINSGYETRRKKGKKDKDISKEKDTQNQNITLDCEGTTNKMKSPETKQRKLSPLRLSVSNNQEPDFIDDIEEKTPISNEVEMESEEQIAERKRKMTREERKMEAILQAFARLEKREKRREQALERISTAKTEVKTECKDTQIVSDAEVIQEQAKEENASKPTPAKVNRTKQRKSFSRSRTHIGQQRRRHRTVSMCSDIQPSSPDIEVTSQQNDIENTVLTIEPETETALAEIITETEVPALNKCPTKYPKTKKHLVNEWLSEKNEKTGKPSDGLSERPLRITTDPEVLATQLNSLPGLTYSPHVYSTPKHYIRFTSPFLSEKRRRKEPTENISGSCKKRWLKQALEEENSAILHRFNSPCQERSRSPAVNGENKSPLLLNDSCSLPDLTTPLKKRRFYQLLDSVYSETSTPTPSPYATPTHTDITPMDPSFATPPRIKSDDETCRNGYKPIYSPVTPVTPGTPGNTMHFENISSPESSPEIKRRTYSQEGYDRSSTMLTLGPFRNSNLTELGLQEIKTIGYTSPRSRTEVNRQCPGEKEPVSDLQLGLDAVEPTALHKTLETPAHDRAEPNSQLDSTHSGRGTMYSSWVKSPDRTGVNFSVNSNLRDLTPSHQLEVGGGFRISESKCLMQDDTRGMFMETTVFCTSEDGLVSGFGRTVNDNLIDGNCTPQNPPQKKKVSLLEYRKRQREARKSGSKTENFPLISVSPHASGSLSNNGDGCASSNDNGEQVDHTASLPLPTPATVYNATSEETSNNCPVKDATASEKNEPEVQWTASTSVEQVRERSYQRALLLSDHRKDKDSGGESPCVSCSPSHVQSSPSSHSNHIPQLQAKGPVPSFSELMEDPDPENPEPTTTNECPSPDTSQNTCKSPPKMSKPGSPGSVIPAQAHGKIFTKPDPQWDSTVSASEAENGVHLKTELQQKQLSNNNQALSKNHPPQTHVRNSSEQLSQKLPSVPTKLHCPPSPHLENPPKSSTPHTPVQHGYLSPKPPSQQLGSPYRPHHSQSPQVGTPQREPQRNFYPAAQNLPANTQQATSGTLFTQTPSGQSSATYSQFNQQSLNSTAPPPPPPPPPSSSYYQNQQPSANFQNYNQLKGSLSQQTVFTSGPNQALPGTTSQQTVPGHHVTPGHFLPSQNPTIHHQTAAAVVPPPPPPPPAPGPHLVQQPNSHQQHSVAHVVGPVHAVTPGSHIHSQTAGHHLPPPPPPPGPAPHHHPPPHPSTGLQGLQAQHQHVVNSAPPPPPPPPPSSVLASGHHTTSAQALHHPPHQGPPLFPSSAHPTVPPYPSQATHHTTLGPGPQHQPSGTGPHCPLPVTGPHLQPQGPNSIPTPTASGFCPHPGSVALPHGVQGPQQASPVPGQIPIHRAQVPPTFQNNYHGSGWH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q8IZD2","disprot_id":"DP02393","ncbi_taxon_id":9606,"regions_counter":2,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":339,"region_id":"DP02393r001","start":323,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Molecule B had well defined electron density for SET core, however residues 327 to 339 at the N-terminus and 449 to the end at the C-terminus were disordered and could not be modeled from X-ray data.","type":"Results"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27812132","version":2,"reference_html":"The Human Mixed Lineage Leukemia 5 (MLL5), a Sequentially and Structurally Divergent SET Domain-Containing Protein with No Intrinsic Catalytic Activity. <i> Mas-Y-Mas S, Barbon M, Teyssier C, Déméné H, Carvalho JE, Bird LE, Lebedev A, Fattori J, Schubert M, Dumas C, Bourguet W, le Maire A. </i> PLoS One, 2016","date":"2022-08-04T08:31:08.706Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5HT6"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-04T14:53:37.076Z"}}],"released":"2023_06","uniref100":"UniRef100_Q8IZD2","date":"2019-12-02T13:46:57.968Z","acc":"Q8IZD2","name":"Inactive histone-lysine N-methyltransferase 2E","length":1858,"organism":"Homo sapiens","dataset":["NDDs-related proteins"],"UniParc":"UPI0000074133","genes":[{"name":{"value":"KMT2E"},"synonyms":[{"value":"MLL5"}]}],"alphafold_very_low_content":0.8035522066738429,"disorder_content":0.00914962325080732,"disprot_consensus":{"full":[{"start":323,"end":339,"type":"D"}],"Structural state":[{"start":323,"end":339,"type":"D"}]}},{"features":{"gene3D":[{"start":437,"end":530,"id":"G3DSA:2.60.120.10","name":"Jelly Rolls"}],"pfam":[{"id":"PF11699","name":"Mif2/CENP-C like","start":439,"end":526},{"id":"PF15624","name":"Kinetochore CENP-C fungal homologue, Mif2, N-terminal","start":3,"end":48}]},"uniref50":"UniRef50_P35201","sequence":"MDYMKLGLKSRKTGIDVKQDIPKDEYSMENIDDFFKDDETSLISMRRKSRRKSSLFLPSTLNGDTKNVLPPFLQSYKSQDDEVVQSPSGKGDGSRRSSLLSHQSNFLSPANDFEPIEEEPEQEENDIRGNDFATPITQKLSKPTYKRKYSTRYSLDTSESPSVRLTPDRITNKNVYSDVPDLVADEDDDDRVNTSLNTSDNALLEDELEDDGFIPESEEDGDYIESDSSLDSGSDSASDSDGDNTYQEVEEEAEVNTNDNEDDYIRRQASDVVRTDSIIDRNGLRKSTRVKVAPLQYWRNEKIVYKRKSNKPVLDIDKIVTYDESEDEEEILAAQRRKKQKKKPTPTRPYNYVPTGRPRGRPKKDPNAKENLIPEDPNEDIIERIESGGIENGEWLKHGILEANVKISDTKEETKDEIIAFAPNLSQTEQVKDTKDENFALEIMFDKHKEYFASGILKLPAISGQKKLSNSFRTYITFHVIQGIVEVTVCKNKFLSVKGSTFQIPAFNEYAIANRGNDEAKMFFVQVTVSEDANDDNDKELDSTFDTFG","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P35201","disprot_id":"DP02395","ncbi_taxon_id":559292,"regions_counter":2,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":436,"region_id":"DP02395r001","start":365,"term_id":"IDPO:0000002","statement":[{"text":"The final model included density for residues 437–530 (Figure 3), but residues 365–436 were not visible, implying that they were disordered","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18701705","version":2,"reference_html":"Structural and functional dissection of Mif2p, a conserved DNA-binding kinetochore protein. <i> Cohen RL, Espelin CW, De Wulf P, Sorger PK, Harrison SC, Simons KT. </i> Mol Biol Cell, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2VPV"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Biological process","ec_ontology":"ECO","end":438,"region_id":"DP02395r002","start":331,"term_id":"GO:0051179","statement":[{"text":"The final model included density for residues 437–530 (Figure 3), but residues 365–436 were not visible, implying that they were disordered","type":"Results"},{"text":"Two of the five regions of Mif2p were found to be essential for function: those between residues 267 and 347, a segment that contains the CENP-C signature box (green; Figure 1), and those between 331 and 438. These regions contain the likely nuclear localization sequence (QRRKKQKK; Nair and Rost, 2005 blue right-pointing triangle), but we did not explicitly test whether the sequence is essential for correct localization.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18701705","version":3,"reference_html":"Structural and functional dissection of Mif2p, a conserved DNA-binding kinetochore protein. <i> Cohen RL, Espelin CW, De Wulf P, Sorger PK, Harrison SC, Simons KT. </i> Mol Biol Cell, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2VPV"}],"term_name":"localization","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2021_06","uniref100":"UniRef100_P35201","date":"2019-12-02T14:15:08.408Z","acc":"P35201","name":"Inner kinetochore subunit MIF2","length":549,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI000012F0EC","genes":[{"name":{"value":"MIF2"},"olnNames":[{"value":"YKL089W"}]}],"alphafold_very_low_content":0.366120218579235,"disorder_content":0.13114754098360656,"disprot_consensus":{"full":[{"start":331,"end":364,"type":"F"},{"start":365,"end":436,"type":"D"},{"start":437,"end":438,"type":"F"}],"Structural state":[{"start":365,"end":436,"type":"D"}],"Biological process":[{"start":331,"end":438,"type":"F"}]}},{"features":{"gene3D":[{"start":87,"end":469,"id":"G3DSA:3.50.50.60","name":"FAD/NAD(P)-binding domain"},{"start":389,"end":628,"id":"G3DSA:1.10.418.10","name":"Calponin-like domain"}],"pfam":[{"id":"PF00307","name":"Calponin homology (CH) domain","start":522,"end":624},{"id":"PF00412","name":"LIM domain","start":764,"end":819},{"id":"PF01494","name":"FAD binding domain","start":87,"end":123},{"id":"PF12130","name":"Bivalent Mical/EHBP Rab binding domain","start":1854,"end":1988},{"id":"PF25413","name":"Mical, Rossman domain","start":241,"end":370}]},"uniref50":"UniRef50_Q7RTP6","sequence":"MEERKHETMNPAHVLFDRFVQATTCKGTLKAFQELCDHLELKPKDYRSFYHKLKSKLNYWKAKALWAKLDKRGSHKDYKKGKACTNTKCLIIGAGPCGLRTAIDLSLLGAKVVVIEKRDAFSRNNVLHLWPFTIHDLRGLGAKKFYGKFCAGAIDHISIRQLQLILLKVALILGIEIHVNVEFQGLIQPPEDQENERIGWRALVHPKTHPVSEYEFEVIIGGDGRRNTLEGFRRKEFRGKLAIAITANFINRNTTAEAKVEEISGVAFIFNQKFFQELREATGIDLENIVYYKDDTHYFVMTAKKQSLLDKGVILHDYADTELLLSRENVDQEALLSYAREAADFSTQQQLPSLDFAINHYGQPDVAMFDFTCMYASENAALVREQNGHQLLVALVGDSLLEPFWPMGTGIARGFLAAMDSAWMVRSWSLGTSPLEVLAERESIYRLLPQTTPENVSKNFSQYSIDPVTRYPNINVNFLRPSQVRHLYDTGETKDIHLEMESLVNSRTTPKLTRNESVARSSKLLGWCQRQTDGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQNVEKNNQLAFDIAEKELGISPIMTGKEMASVGEPDKLSMVMYLTQFYEMFKDSLPSSDTLDLNAEEKAVLIASTRSPISFLSKLGQTISRKRSPKDKKEKDLDGAGKRRKTSQSEEEEAPRGHRGERPTLVSTLTDRRMDVAVGNQNKVKYMATQLLAKFEENAPAQSIGIRRQGSMKKEFPQNLGGSDTCYFCQKRVYVMERLSAEGKFFHRSCFKCEYCATTLRLSAYAYDIEDGKFYCKPHYCYRLSGYAQRKRPAVAPLSGKEAKGPLQDGATTDANGRANAVASSTERTPGSGVNGLEEPSIAKRLRGTPERIELENYRLSLRQAEALQEVPEETQAEHNLSSVLDTGAEEDVASSSSESEMEEEGEEEEEEPRLPPSDLGGVPWKEAVRIHALLKGKSEEELEASKSFGPGNEEEEEEEEEYEEEEEEDYDEEEEESSEAGNQRLQQVMHAADPLEIQADVHWTHIREREEEERMAPASESSASGAPLDENDLEEDVDSEPAEIEGEAAEDGDPGDTGAELDDDQHWSDSPSDADRELRLPCPAEGEAELELRVSEDEEKLPASPKHQERGPSQATSPIRSPQESALLFIPVHSPSTEGPQLPPVPAATQEKSPEERLFPEPLLPKEKPKADAPSDLKAVHSPIRSQPVTLPEARTPVSPGSPQPQPPVAASTPPPSPLPICSQPQPSTEATVPSPTQSPIRFQPAPAKTSTPLAPLPVQSQSDTKDRLGSPLAVDEALRRSDLVEEFWMKSAEIRRSLGLTPVDRSKGPEPSFPTPAFRPVSLKSYSVEKSPQDEGLHLLKPLSIPKRLGLPKPEGEPLSLPTPRSPSDRELRSAQEERRELSSSSGLGLHGSSSNMKTLGSQSFNTSDSAMLTPPSSPPPPPPPGEEPATLRRKLREAEPNASVVPPPLPATWMRPPREPAQPPREEVRKSFVESVEEIPFADDVEDTYDDKTEDSSLQEKFFTPPSCWPRPEKPRHPPLAKENGRLPALEGTLQPQKRGLPLVSAEAKELAEERMRAREKSVKSQALRDAMARQLSRMQQMELASGAPRPRKASSAPSQGKERRPDSPTRPTLRGSEEPTLKHEATSEEVLSPPSDSGGPDGSFTSSEGSSGKSKKRSSLFSPRRNKKEKKSKGEGRPPEKPSSNLLEEAAAKPKSLWKSVFSGYKKDKKKKADDKSCPSTPSSGATVDSGKHRVLPVVRAELQLRRQLSFSEDSDLSSDDVLEKSSQKSRREPRTYTEEELNAKLTRRVQKAARRQAKQEELKRLHRAQIIQRQLQQVEERQRRLEERGVAVEKALRGEAGMGKKDDPKLMQEWFKLVQEKNAMVRYESELMIFARELELEDRQSRLQQELRERMAVEDHLKTEEELSEEKQILNEMLEVVEQRDSLVALLEEQRLREREEDKDLEAAMLSKGFSLNWS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q7RTP6","disprot_id":"DP02396","ncbi_taxon_id":9606,"regions_counter":4,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1990,"region_id":"DP02396r001","start":1881,"term_id":"IDPO:0000002","statement":[{"text":"missing residues in the PDB","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27552051","version":2,"reference_html":"bMERB domains are bivalent Rab8 family effectors evolved by gene duplication. <i> Rai A, Oprisko A, Campos J, Fu Y, Friese T, Itzen A, Goody RS, Gazdag EM, Müller MP. </i> Elife, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5SZG"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q02241","partner_end":null}],"ec_ontology":"ECO","end":1918,"region_id":"DP02396r002","start":1735,"term_id":"GO:0005515","statement":[{"text":"The minimum region of MICAL3 required for the binding of MKLP1 corresponds to the deletion mutant MICAL3-CC4 (Fig. 2A, 2B) that spans amino acids 1735-1918","type":"Curator statement"},{"text":"Taken together, our results show that MKLP1 and MICAL3 primarily interact through the unstructured polypeptide region in MKLP1 and the C-terminal coiled-coil domain of MICAL3, with additional contacts provided by the second coiled-coil domain of MICAL3 and the coiled-coil domain of MKLP1","type":"Results"},{"text":"MICAL3 Interacts with MKLP1","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"spectrometry evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"27528609","version":3,"reference_html":"MICAL3 Flavoprotein Monooxygenase Forms a Complex with Centralspindlin and Regulates Cytokinesis. <i> Liu Q, Liu F, Yu KL, Tas R, Grigoriev I, Remmelzwaal S, Serra-Marques A, Kapitein LC, Heck AJ, Akhmanova A. </i> J Biol Chem, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007731","term_name":"protein binding","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Biological process","ec_ontology":"ECO","end":1918,"region_id":"DP02396r003","start":1735,"term_id":"GO:0051179","statement":[{"text":"The minimum region of MICAL3 required for the binding of MKLP1 corresponds to the deletion mutant MICAL3-CC4 (Fig. 2A, 2B) that spans amino acids 1735-1918","type":"Curator statement"},{"text":"Taken together, our results show that MKLP1 and MICAL3 primarily interact through the unstructured polypeptide region in MKLP1 and the C-terminal coiled-coil domain of MICAL3, with additional contacts provided by the second coiled-coil domain of MICAL3 and the coiled-coil domain of MKLP1","type":"Results"},{"text":"MICAL3 Interacts with MKLP1","type":"Results"},{"text":"We showed that MKLP1 recruits MICAL3 to the central spindle, whereas MICAL3 participates in targeting to the midbody its binding partners ELKS and Rab8A, and the loss of both ELKS and Rab8A also caused cytokinesis defects.","type":"Introduction"},{"text":"We conclude that MICAL3 can form a triple complex with MKLP1 and ELKS and through the interaction with the former, target the latter to the midbody.","type":"Results"},{"text":"In a mechanism independent of its enzymatic activity, MICAL3 targets the adaptor protein ELKS and Rab8A-positive vesicles to the midbody, and the depletion of ELKS and Rab8A also leads to cytokinesis defects.","type":"Abstract"},{"text":"We propose that MICAL3 acts as a midbody-associated scaffold for vesicle targeting, which promotes maturation of the intercellular bridge and abscission.","type":"Abstract"},{"text":"MICAL3 is required for ELKS localization to the midbody.","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"spectrometry evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"27528609","version":3,"reference_html":"MICAL3 Flavoprotein Monooxygenase Forms a Complex with Centralspindlin and Regulates Cytokinesis. <i> Liu Q, Liu F, Yu KL, Tas R, Grigoriev I, Remmelzwaal S, Serra-Marques A, Kapitein LC, Heck AJ, Akhmanova A. </i> J Biol Chem, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007731","term_name":"localization","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1918,"region_id":"DP02396r004","start":1735,"term_id":"GO:0060090","statement":[{"text":"We conclude that MICAL3 can form a triple complex with MKLP1 and ELKS and through the interaction with the former, target the latter to the midbody","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"spectrometry evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"27528609","version":3,"reference_html":"MICAL3 Flavoprotein Monooxygenase Forms a Complex with Centralspindlin and Regulates Cytokinesis. <i> Liu Q, Liu F, Yu KL, Tas R, Grigoriev I, Remmelzwaal S, Serra-Marques A, Kapitein LC, Heck AJ, Akhmanova A. </i> J Biol Chem, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007731","term_name":"molecular adaptor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","uniref100":"UniRef100_Q7RTP6","date":"2019-12-02T14:42:37.551Z","acc":"Q7RTP6","name":"[F-actin]-monooxygenase MICAL3","length":2002,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0001823FDE","genes":[{"name":{"value":"MICAL3"},"synonyms":[{"value":"KIAA0819"},{"value":"KIAA1364"}]}],"alphafold_very_low_content":0.5399600399600399,"disorder_content":0.054945054945054944,"disprot_consensus":{"full":[{"start":1735,"end":1880,"type":"F"},{"start":1881,"end":1990,"type":"D"}],"Structural state":[{"start":1881,"end":1990,"type":"D"}],"Molecular function":[{"start":1735,"end":1918,"type":"F"}],"Biological process":[{"start":1735,"end":1918,"type":"F"}]}},{"features":{"gene3D":[{"start":18,"end":100,"id":"G3DSA:3.40.1810.10","name":"Transcription factor, MADS-box"}],"pfam":[{"id":"PF00319","name":"SRF-type transcription factor (DNA-binding and dimerisation domain)","start":25,"end":72}]},"uniref50":"UniRef50_P11746","sequence":"MSDIEEGTPTNNGQQKERRKIEIKFIENKTRRHVTFSKRKHGIMKKAFELSVLTGTQVLLLVVSETGLVYTFSTPKFEPIVTQQEGRNLIQACLNAPDDEEEDEEEDGDDDDDDDDDGNDMQRQQPQQQQPQQQQQVLNAHANSLGHLNQDQVPAGALKQEVKSQLLGGANPNQNSMIQQQQHHTQNSQPQQQQQQQPQQQMSQQQMSQHPRPQQGIPHPQQSQPQQQQQQQQQLQQQQQQQQQQPLTGIHQPHQQAFANAASPYLNAEQNAAYQQYFQEPQQGQY","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref90":"UniRef90_P11746","disprot_id":"DP02397","ncbi_taxon_id":559292,"regions_counter":4,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":17,"region_id":"DP02397r001","start":2,"term_id":"IDPO:0000002","statement":[{"text":"No interpretable electron density for MCM1 cis residues 2–14 and trans residues 2–17 was observed, and we presume that these residues are disordered in the crystal. These N-terminal residues are not necessary for cell-type-specific transcription or viability, but appear to be involved in a phosphorylation-dependent manner in the yeast cell's response to stress, for example high salt concentrations","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9490409","version":2,"reference_html":"Crystal structure of the yeast MATalpha2/MCM1/DNA ternary complex. <i> Tan S, Richmond TJ. </i> Nature, 1998","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1MNM"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":17,"region_id":"DP02397r002","start":2,"term_id":"IDPO:0000045","statement":[{"text":"No interpretable electron density for MCM1 cis residues 2–14 and trans residues 2–17 was observed, and we presume that these residues are disordered in the crystal. These N-terminal residues are not necessary for cell-type-specific transcription or viability, but appear to be involved in a phosphorylation-dependent manner in the yeast cell's response to stress, for example high salt concentrations","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9490409","version":2,"reference_html":"Crystal structure of the yeast MATalpha2/MCM1/DNA ternary complex. <i> Tan S, Richmond TJ. </i> Nature, 1998","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1MNM"}],"term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":17,"region_id":"DP02397r003","start":2,"term_id":"GO:0140313","statement":[{"text":"No interpretable electron density for MCM1 cis residues 2–14 and trans residues 2–17 was observed, and we presume that these residues are disordered in the crystal. These N-terminal residues are not necessary for cell-type-specific transcription or viability, but appear to be involved in a phosphorylation-dependent manner in the yeast cell's response to stress, for example high salt concentrations","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"9490409","version":3,"reference_html":"Crystal structure of the yeast MATalpha2/MCM1/DNA ternary complex. <i> Tan S, Richmond TJ. </i> Nature, 1998","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1MNM"}],"term_name":"molecular sequestering activity","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":17,"region_id":"DP02397r004","start":2,"term_id":"IDPO:0000045","statement":[{"text":"two major phosphorylation sites lie in the N-terminal 17 amino acids","type":"Abstract"},{"text":"both S2 and T8 are phosphorylation sites","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9001236","version":2,"reference_html":"Multiple phosphorylated forms of the Saccharomyces cerevisiae Mcm1 protein include an isoform induced in response to high salt concentrations. <i> Kuo MH, Nadeau ET, Grayhack EJ. </i> Mol Cell Biol, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","uniref100":"UniRef100_P11746","date":"2019-12-02T15:12:08.161Z","acc":"P11746","name":"Pheromone receptor transcription factor","length":286,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","dataset":[],"UniParc":"UPI0000168C1C","genes":[{"name":{"value":"MCM1"},"synonyms":[{"value":"FUN80"}],"orfNames":[{"value":"YM9532.08"}],"olnNames":[{"value":"YMR043W"}]}],"alphafold_very_low_content":0.4230769230769231,"disorder_content":0.055944055944055944,"disprot_consensus":{"full":[{"start":2,"end":17,"type":"D"}],"Structural state":[{"start":2,"end":17,"type":"D"}],"Disorder function":[{"start":2,"end":17,"type":"F"}],"Molecular function":[{"start":2,"end":17,"type":"F"}]}},{"features":{"gene3D":[{"start":1442,"end":1592,"id":"G3DSA:1.25.40.180","name":"G3DSA:1.25.40.180"},{"start":1442,"end":1592,"id":"G3DSA:1.25.40.180","name":"G3DSA:1.25.40.180"},{"start":1442,"end":1592,"id":"G3DSA:1.25.40.180","name":"G3DSA:1.25.40.180"}],"pfam":[{"id":"PF02020","name":"eIF4-gamma/eIF5/eIF2-epsilon","start":1521,"end":1598},{"id":"PF02847","name":"MA3 domain","start":1242,"end":1353},{"id":"PF02854","name":"MIF4G domain","start":762,"end":987}]},"uniref50":"UniRef50_Q04637","sequence":"MNKAPQSTGPPPAPSPGLPQPAFPPGQTAPVVFSTPQATQMNTPSQPRQHFYPSRAQPPSSAASRVQSAAPARPGPAAHVYPAGSQVMMIPSQISYPASQGAYYIPGQGRSTYVVPTQQYPVQPGAPGFYPGASPTEFGTYAGAYYPAQGVQQFPTGVAPTPVLMNQPPQIAPKRERKTIRIRDPNQGGKDITEEIMSGARTASTPTPPQTGGGLEPQANGETPQVAVIVRPDDRSQGAIIADRPGLPGPEHSPSESQPSSPSPTPSPSPVLEPGSEPNLAVLSIPGDTMTTIQMSVEESTPISRETGEPYRLSPEPTPLAEPILEVEVTLSKPVPESEFSSSPLQAPTPLASHTVEIHEPNGMVPSEDLEPEVESSPELAPPPACPSESPVPIAPTAQPEELLNGAPSPPAVDLSPVSEPEEQAKEVTASMAPPTIPSATPATAPSATSPAQEEEMEEEEEEEEGEAGEAGEAESEKGGEELLPPESTPIPANLSQNLEAAAATQVAVSVPKRRRKIKELNKKEAVGDLLDAFKEANPAVPEVENQPPAGSNPGPESEGSGVPPRPEEADETWDSKEDKIHNAENIQPGEQKYEYKSDQWKPLNLEEKKRYDREFLLGFQFIFASMQKPEGLPHISDVVLDKANKTPLRPLDPTRLQGINCGPDFTPSFANLGRTTLSTRGPPRGGPGGELPRGPAGLGPRRSQQGPRKEPRKIIATVLMTEDIKLNKAEKAWKPSSKRTAADKDRGEEDADGSKTQDLFRRVRSILNKLTPQMFQQLMKQVTQLAIDTEERLKGVIDLIFEKAISEPNFSVAYANMCRCLMALKVPTTEKPTVTVNFRKLLLNRCQKEFEKDKDDDEVFEKKQKEMDEAATAEERGRLKEELEEARDIARRRSLGNIKFIGELFKLKMLTEAIMHDCVVKLLKNHDEESLECLCRLLTTIGKDLDFEKAKPRMDQYFNQMEKIIKEKKTSSRIRFMLQDVLDLRGSNWVPRRGDQGPKTIDQIHKEAEMEEHREHIKVQQLMAKGSDKRRGGPPGPPISRGLPLVDDGGWNTVPISKGSRPIDTSRLTKITKPGSIDSNNQLFAPGGRLSWGKGSSGGSGAKPSDAASEAARPATSTLNRFSALQQAVPTESTDNRRVVQRSSLSRERGEKAGDRGDRLERSERGGDRGDRLDRARTPATKRSFSKEVEERSRERPSQPEGLRKAASLTEDRDRGRDAVKREAALPPVSPLKAALSEEELEKKSKAIIEEYLHLNDMKEAVQCVQELASPSLLFIFVRHGVESTLERSAIAREHMGQLLHQLLCAGHLSTAQYYQGLYEILELAEDMEIDIPHVWLYLAELVTPILQEGGVPMGELFREITKPLRPLGKAASLLLEILGLLCKSMGPKKVGTLWREAGLSWKEFLPEGQDIGAFVAEQKVEYTLGEESEAPGQRALPSEELNRQLEKLLKEGSSNQRVFDWIEANLSEQQIVSNTLVRALMTAVCYSAIIFETPLRVDVAVLKARAKLLQKYLCDEQKELQALYALQALVVTLEQPPNLLRMFFDALYDEDVVKEDAFYSWESSKDPAEQQGKGVALKSVTAFFKWLREAEEESDHN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q04637","disprot_id":"DP02398","ncbi_taxon_id":9606,"regions_counter":16,"creator":"vacs","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":606,"region_id":"DP02398r001","start":592,"term_id":"IDPO:0000002","statement":[{"text":"In the Hs complex, the equivalent N-terminal eIF4G residues (Q592–L606) were not visible in the electron density map, suggesting either high flexibility or susceptibility to proteolytic degradation during crystallization.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27773676","version":2,"reference_html":"The Structures of eIF4E-eIF4G Complexes Reveal an Extended Interface to Regulate Translation Initiation. <i> Grüner S, Peter D, Weber R, Wohlbold L, Chung MY, Weichenrieder O, Valkov E, Igreja C, Izaurralde E. </i> Mol Cell, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5T46"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-30T15:30:13.356Z"}},{"start":161,"end":216,"reference_id":"23041282","reference_source":"pmid","reference_html":"Interdomain allostery promotes assembly of the poly(A) mRNA complex with PABP and eIF4G. <i> Safaee N, Kozlov G, Noronha AM, Xie J, Wilds CJ, Gehring K. </i> Mol Cell, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP02398r003","statement":[{"text":"The 1H,15N HSQC spectrum of 15N-Nt4G displays poorly dispersed signals, particularly in the 1H dimension, which suggests that the eIF4G fragment is not structured in solution (Figure 2D).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-27T07:34:50.228Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":178,"end":202,"reference_id":"23041282","reference_source":"pmid","reference_html":"Interdomain allostery promotes assembly of the poly(A) mRNA complex with PABP and eIF4G. <i> Safaee N, Kozlov G, Noronha AM, Xie J, Wilds CJ, Gehring K. </i> Mol Cell, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP02398r004","statement":[{"text":"Upon addition of RRM2, the Nt4G signals became widely dispersed, indicating that the polypeptide folds upon binding to RRM2 (Figure 2E). Backbone assignments of 13C,15N-labeled Nt4G alone and in complex with RRM2 showed that eIF4G residues from Lys178 to Thr202 were affected by RRM2 binding (Figure 2F). No chemical shift changes were observed for the N- and C-terminal residues, suggesting that they do not participate in binding RRM1-2. The large magnitude of the changes (up to 1.56 ppm) reflects the dramatic change from a flexible polypeptide to a rigid, structured conformation in the complex (Figures 2D–2F).","type":"Results"}],"cross_refs":[{"db":"PDB","id":"4F02"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-27T07:35:13.696Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":178,"end":203,"reference_id":"23041282","reference_source":"pmid","reference_html":"Interdomain allostery promotes assembly of the poly(A) mRNA complex with PABP and eIF4G. <i> Safaee N, Kozlov G, Noronha AM, Xie J, Wilds CJ, Gehring K. </i> Mol Cell, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP02398r005","statement":[{"text":"In contrast, NMR titrations of 15N-RRM2 (PABP residues 86–192) with the eIF4G fragment led to specific chemical shift changes of the 1H,15N HSQC signals.","type":"Results"},{"text":"Backbone assignments of 13C,15N-labeled Nt4G alone and in complex with RRM2 showed that eIF4G residues from Lys178 to Thr202 were affected by RRM2 binding (Figure 2F). ","type":"Results"},{"text":"The spectra identify residues 178–203 as the region of eIF4G that binds RRM2.","type":"Figure"}],"interaction_partner":[{"db":"UniProt","id":"P11940","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-27T07:35:51.349Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":179,"end":198,"reference_id":"23041282","reference_source":"pmid","reference_html":"Interdomain allostery promotes assembly of the poly(A) mRNA complex with PABP and eIF4G. <i> Safaee N, Kozlov G, Noronha AM, Xie J, Wilds CJ, Gehring K. </i> Mol Cell, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"4F02"}],"region_id":"DP02398r006","statement":[{"text":"In both structures, we observed electron density for PABP residues 10–183, nine adenosine nucleotides, and residues 179-198 of eIF4G. The eIF4G peptide adopts a secondary structure of two short b strands and one a helix bound to PABP RRM2 (Figure 3A).","type":"Results"}],"interaction_partner":[{"db":"UniProt","id":"P11940","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-27T07:35:34.333Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":161,"end":216,"reference_id":"23041282","reference_source":"pmid","reference_html":"Interdomain allostery promotes assembly of the poly(A) mRNA complex with PABP and eIF4G. <i> Safaee N, Kozlov G, Noronha AM, Xie J, Wilds CJ, Gehring K. </i> Mol Cell, 2012","date":"2023-11-30T15:28:33.854Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1905537","term_name":"positive regulation of eukaryotic translation initiation factor 4F complex assembly","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","released":"2023_12","version":5,"region_id":"DP02398r007","statement":[{"text":"In the presence of Nt4G, the RRM1-2·poly(A) interaction was enhanced, and a supershifted ternary complex was observed. The enhancement of RNA binding was also observed with RRM1-2-3-4 binding to 32P-labeled poly(A)25. Quantification of the amount of poly(A) bound to RRM1-2-3-4 shows that the presence of Nt4G increases the affinity of the RRMs for poly(A) by at least 10-fold (Figure 4B).","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of eukaryotic translation initiation factor 4F complex assembly.\" [GO_REF:0000058, GOC:bc, GOC:PARL, GOC:TermGenie, PMID:18426977]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P11940","operator":null,"partner_start":null,"partner_end":null},{"db":"ChEBI","id":"8756","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:57:42.966Z"}},{"start":179,"end":198,"reference_id":"23041282","reference_source":"pmid","reference_html":"Interdomain allostery promotes assembly of the poly(A) mRNA complex with PABP and eIF4G. <i> Safaee N, Kozlov G, Noronha AM, Xie J, Wilds CJ, Gehring K. </i> Mol Cell, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4F02"}],"region_id":"DP02398r008","statement":[{"text":"In both structures, we observed electron density for PABP residues 10–183, nine adenosine nucleotides, and residues 179-198 of eIF4G. The eIF4G peptide adopts a secondary structure of two short b strands and one a helix bound to PABP RRM2 (Figure 3A).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-27T07:35:05.282Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":161,"end":216,"reference_id":"23041282","reference_source":"pmid","reference_html":"Interdomain allostery promotes assembly of the poly(A) mRNA complex with PABP and eIF4G. <i> Safaee N, Kozlov G, Noronha AM, Xie J, Wilds CJ, Gehring K. </i> Mol Cell, 2012","date":"2023-11-30T15:27:16.494Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1905537","term_name":"positive regulation of eukaryotic translation initiation factor 4F complex assembly","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","released":"2023_12","version":5,"region_id":"DP02398r009","statement":[{"text":"To quantify the cooperativity, we measured the binding affinities using ITC. In agreement with the gel shift studies, we found that poly(A)11 binds to the RRM1-2·Nt4G complex with 10-fold better affinity than to RRM1-2, 62 nM and 0.6 μM, respectively (Figure 4C).","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of eukaryotic translation initiation factor 4F complex assembly.\" [GO_REF:0000058, GOC:bc, GOC:PARL, GOC:TermGenie, PMID:18426977]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P11940","operator":null,"partner_start":null,"partner_end":null},{"db":"ChEBI","id":"8756","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:57:45.093Z"}},{"start":161,"end":216,"reference_id":"23041282","reference_source":"pmid","reference_html":"Interdomain allostery promotes assembly of the poly(A) mRNA complex with PABP and eIF4G. <i> Safaee N, Kozlov G, Noronha AM, Xie J, Wilds CJ, Gehring K. </i> Mol Cell, 2012","date":"2022-03-08T14:54:55.884Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","released":"2022_03","version":4,"interaction_partner":[{"db":"UniProt","id":"P11940","partner_start":null,"partner_end":null}],"region_id":"DP02398r010","statement":[{"text":"To quantify the cooperativity, we used ITC to measure the affinities of eIF4G for RRM2, RRM1-2, and RRM2-3. Comparison of the affinities of RRM1-2 and RRM2 showed that RRM1 decreased the affinity in the absence of poly(A) RNA. Under identical conditions, PABP RRM2 bound Nt4G with 3-fold better affinity than RRM1-2, Kd of 5 μM and 19 μM, respectively (Figure 5C).","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-30T15:29:17.591Z"}},{"start":161,"end":216,"reference_id":"23041282","reference_source":"pmid","reference_html":"Interdomain allostery promotes assembly of the poly(A) mRNA complex with PABP and eIF4G. <i> Safaee N, Kozlov G, Noronha AM, Xie J, Wilds CJ, Gehring K. </i> Mol Cell, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P11940","partner_start":null,"partner_end":null}],"region_id":"DP02398r011","statement":[{"text":"We carried out coimmunoprecipitation (coIP) assays on HeLa cell extracts to test the role of RNA on the PABP·eIF4G interaction in cells (Figure 6). Endogenous eIF4G could be immunoprecipitated with an anti-PABP antibody (Figure 6B).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-27T07:35:20.996Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1427,"end":1436,"reference_id":"16698552","reference_source":"pmid","reference_html":"Two structurally atypical HEAT domains in the C-terminal portion of human eIF4G support binding to eIF4A and Mnk1. <i> Bellsolell L, Cho-Park PF, Poulin F, Sonenberg N, Burley SK. </i> Structure, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"1UG3"}],"region_id":"DP02398r012","statement":[{"text":"The C-terminal region of human eIF4GI consists of two a-helical domains, 4G/C1 and 4G/C2, joined by a 13 residue linker (Figures 1B and 2).","type":"Results"},{"text":"The linker connecting domains 4G/C1 and 4G/C2 is both highly polar and apparently flexible (10/13 residues were not visible in our electron density maps).","type":"Results"},{"text":"Ten residues in the interdomain linker of 4G/C (left) were not observed in the electron density maps and are shown as a polyalanine trace (violet).","type":"Figure"},{"text":"At the final stages of refinement, NCS operators were re-evaluated, and restrained NCS refinement yielded a final model (residues\n1234–1566, excluding 1428–1437 from the interdomain linker, rmsd = 0.2 A˚ for 323 a-carbon pairs) with an R factor of 24.4% and an R free of 29.2% (Table 1).","type":"Methods"},{"text":"The authors used isoform 8 (DP03499) in their experiments, which is 1 residue longer than isoform A. Thus, region 1428-1437 corresponds to region 1427-1436 of the canonical UniProt sequence. The sequence of the disordered region is identical in both isoforms.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-27T08:31:32.748Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1427,"end":1436,"reference_id":"16698552","reference_source":"pmid","reference_html":"Two structurally atypical HEAT domains in the C-terminal portion of human eIF4G support binding to eIF4A and Mnk1. <i> Bellsolell L, Cho-Park PF, Poulin F, Sonenberg N, Burley SK. </i> Structure, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"1UG3"}],"region_id":"DP02398r013","statement":[{"text":"The C-terminal region of human eIF4GI consists of two a-helical domains, 4G/C1 and 4G/C2, joined by a 13 residue linker (Figures 1B and 2).","type":"Results"},{"text":"The linker connecting domains 4G/C1 and 4G/C2 is both highly polar and apparently flexible (10/13 residues were not visible in our electron density maps).","type":"Results"},{"text":"Ten residues in the interdomain linker of 4G/C (left) were not observed in the electron density maps and are shown as a polyalanine trace (violet).","type":"Figure"},{"text":"At the final stages of refinement, NCS operators were re-evaluated, and restrained NCS refinement yielded a final model (residues\n1234–1566, excluding 1428–1437 from the interdomain linker, rmsd = 0.2 A˚ for 323 a-carbon pairs) with an R factor of 24.4% and an R free of 29.2% (Table 1).","type":"Methods"},{"text":"The authors used isoform 8 (DP03499) in their experiments, which is 1 residue longer than isoform A. Thus, region 1428-1437 corresponds to region 1427-1436 of the canonical UniProt sequence. The sequence of the disordered region is identical in both isoforms.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-27T08:31:40.589Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":1079,"end":1233,"reference_id":"16698552","reference_source":"pmid","reference_html":"Two structurally atypical HEAT domains in the C-terminal portion of human eIF4G support binding to eIF4A and Mnk1. <i> Bellsolell L, Cho-Park PF, Poulin F, Sonenberg N, Burley SK. </i> Structure, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP02398r014","statement":[{"text":"Sequence comparisons (Figure 1A), secondary structure predictions (data not shown), and limited proteolysis combined with mass spectrometry (data not shown) permitted identification of a protease-resistant C-terminal portion of human eIF4GI that supports binding to eIF4A and Mnk1 (data not shown). Further truncation (eIF4GI[1235–1572]) yielded a two-domain protein that gives high-quality crystals with two protomers per asymmetric unit (Experimental Procedures).","type":"Results"},{"text":"Limited proteolysis of the C-terminal region of human eIF4GI (residues 1080–1600) with a panel of specific endoproteases yielded a resistant core of approximately 40 kDa, as judged by gel electrophoresis (data not shown). Matrix-assisted laser desorption ionization mass spectrometry and N-terminal sequencing of proteolytic fragments mapped a large number of proteolytic cleavage sites to residues 1080–1234.","type":"Methods"},{"text":"The authors used isoform 8 (DP03499) in their experiments, which is 1 residue longer than isoform A. Thus, region 1080-1234 corresponds to region 1079-1233 of the canonical UniProt sequence. The sequence of the disordered region is identical in both isoforms.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-27T07:29:15.479Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":290,"end":754,"reference_id":"32883864","reference_source":"pmid","reference_html":"Structure of a human 48<i>S</i> translational initiation complex. <i> Brito Querido J, Sokabe M, Kraatz S, Gordiyenko Y, Skehel JM, Fraser CS, Ramakrishnan V. </i> Science, 2020","date":"2023-11-30T15:38:28.149Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6ZMW"}],"region_id":"DP02398r015","statement":[{"text":" It is likely that other domains of eIF4G, not visible in this work because of possible flexibility, could also make interactions with nearby subunits such as the eIF3d-NTT and eIF3e, which has been previously suggested by biochemical cross-linking (4).","type":"Article"},{"text":"The Cryo-EM structure of the 48S translational initiation complex shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":992,"end":1599,"reference_id":"32883864","reference_source":"pmid","reference_html":"Structure of a human 48<i>S</i> translational initiation complex. <i> Brito Querido J, Sokabe M, Kraatz S, Gordiyenko Y, Skehel JM, Fraser CS, Ramakrishnan V. </i> Science, 2020","date":"2023-11-30T15:38:40.993Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6ZMW"}],"region_id":"DP02398r016","statement":[{"text":" It is likely that other domains of eIF4G, not visible in this work because of possible flexibility, could also make interactions with nearby subunits such as the eIF3d-NTT and eIF3e, which has been previously suggested by biochemical cross-linking (4).","type":"Article"},{"text":"The Cryo-EM structure of the 48S translational initiation complex shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:57:37.610Z"}}],"released":"2020_12","uniref100":"UniRef100_Q04637","date":"2019-12-02T16:09:11.768Z","acc":"Q04637","name":"Eukaryotic translation initiation factor 4 gamma 1","length":1599,"organism":"Homo sapiens","dataset":["Autophagy-related proteins","Condensates-related proteins","RNA-binding proteins"],"UniParc":"UPI0000161B6A","genes":[{"name":{"value":"EIF4G1"},"synonyms":[{"value":"EIF4F"},{"value":"EIF4G"},{"value":"EIF4GI"}]}],"alphafold_very_low_content":0.5522201375859912,"disorder_content":0.706066291432145,"disprot_consensus":{"full":[{"start":161,"end":177,"type":"D"},{"start":178,"end":202,"type":"T"},{"start":203,"end":216,"type":"D"},{"start":290,"end":754,"type":"D"},{"start":992,"end":1599,"type":"D"}],"Structural state":[{"start":161,"end":216,"type":"D"},{"start":290,"end":754,"type":"D"},{"start":992,"end":1599,"type":"D"}],"Structural transition":[{"start":178,"end":202,"type":"T"}],"Molecular function":[{"start":161,"end":216,"type":"F"}],"Biological process":[{"start":161,"end":216,"type":"F"}],"Disorder function":[{"start":1427,"end":1436,"type":"F"}]}},{"features":{"gene3D":[{"start":6,"end":217,"id":"G3DSA:3.30.760.10","name":"RNA Cap, Translation Initiation Factor Eif4e"}],"pfam":[{"id":"PF01652","name":"Eukaryotic initiation factor 4E","start":38,"end":212}]},"uniref50":"UniRef50_P06730","sequence":"MATVEPETTPTPNPPTTEEEKTESNQEVANPEHYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMPGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRSDLDRFWLETLLCLIGESFDDYSDDVCGAVVNVRAKGDKIAIWTTECENREAVTHIGRVYKERLGLPPKIVIGYQSHADTATKSGSTTKNRFVV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P06730","disprot_id":"DP02399","ncbi_taxon_id":9606,"regions_counter":4,"creator":"vacs","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":29,"region_id":"DP02399r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"The N-terminal Regions of Hs and Dm eIF4E Are Not Required for Binding to eIF4G","type":"Results"},{"text":"Although full-length eIF4E was used in the human complex, the first 29 residues (M1–A29) are not visible in the electron density map","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27773676","version":2,"reference_html":"The Structures of eIF4E-eIF4G Complexes Reveal an Extended Interface to Regulate Translation Initiation. <i> Grüner S, Peter D, Weber R, Wohlbold L, Chung MY, Weichenrieder O, Valkov E, Igreja C, Izaurralde E. </i> Mol Cell, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5T46"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-21T14:26:26.136Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":2,"end":35,"reference_id":"17036047","reference_source":"pmid","reference_html":"Cap-free structure of eIF4E suggests a basis for conformational regulation by its ligands. <i> Volpon L, Osborne MJ, Topisirovic I, Siddiqui N, Borden KL. </i> EMBO J, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2GPQ"}],"region_id":"DP02399r003","statement":[{"text":"In this NMR ensemble of the apo-eIF4E, the loops S1–S2, H2–S3, H4–S5 and S7–S8 are less defined while the first 35 residues at the N-terminus are completely disordered.","type":"Results"},{"text":"The authors mention in the Results and discussion section that the N-terminal methionine is removed from the protein: As can be seen in Figure 2A, the molecular mass of eIF4E is 24964.373.2 Da slightly less than the predicted mass 25097.2 Da. This mass difference (132.9 Da) corresponds to the loss of methionine (131.2 Da) at the N-terminus, which is a common event (Huang et al, 1987). The absence of Met1 in the NMR data corroborates this hypothesis.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-21T14:23:58.902Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":26,"reference_id":"11879179","reference_source":"pmid","reference_html":"Crystal structures of 7-methylguanosine 5'-triphosphate (m(7)GTP)- and P(1)-7-methylguanosine-P(3)-adenosine-5',5'-triphosphate (m(7)GpppA)-bound human full-length eukaryotic initiation factor 4E: biological importance of the C-terminal flexible region. <i> Tomoo K, Shen X, Okabe K, Nozoe Y, Fukuhara S, Morino S, Ishida T, Taniguchi T, Hasegawa H, Terashima A, Sasaki M, Katsuya Y, Kitamura K, Miyoshi H, Ishikawa M, Miura K. </i> Biochem J, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"1IPB"},{"db":"PDB","id":"1IPC"}],"region_id":"DP02399r004","statement":[{"text":"The present results provide the structural basis for the biological function of both N- and C-terminal mobile regions of eIF4E in translation initiation, especially the regulatory function through the switch-on/off of eIF4E-binding protein–eIF4E phosphorylation.","type":"Abstract"},{"text":"However, the structures of the N- and C-terminal regions are still unclear, because of the high flexibility of these regions in eIF4E.","type":"Introduction"},{"text":"As is shown in Figure 1, we could determine the structure from Glu27 (in both complexes of human full-length eIF4E; it was impossible to determine the structure from the N-terminus to Gln26 because of the high flexibility.","type":"Results"},{"text":"In contrast with large flexibility at both N- and C-terminal regions, the core regions consisting of eight-stranded anti-parallel b-sheets and three long a-helices are very similar to each other.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-21T14:20:26.538Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","uniref100":"UniRef100_P06730","date":"2019-12-02T16:17:08.948Z","acc":"P06730","name":"Eukaryotic translation initiation factor 4E","length":217,"organism":"Homo sapiens","dataset":["NDDs-related proteins","RNA-binding proteins"],"UniParc":"UPI00001782D7","genes":[{"name":{"value":"EIF4E","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:3287","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:3287"}}]},"synonyms":[{"value":"EIF4EL1"},{"value":"EIF4F"}]}],"alphafold_very_low_content":0.03686635944700461,"disorder_content":0.16129032258064516,"disprot_consensus":{"full":[{"start":1,"end":35,"type":"D"}],"Structural state":[{"start":1,"end":35,"type":"D"}]}},{"features":{"gene3D":[{"start":49,"end":259,"id":"G3DSA:3.30.760.10","name":"RNA Cap, Translation Initiation Factor Eif4e"}],"pfam":[{"id":"PF01652","name":"Eukaryotic initiation factor 4E","start":82,"end":251}]},"uniref50":"UniRef50_P48598","sequence":"MQSDFHRMKNFANPKSMFKTSAPSTEQGRPEPPTSAAAPAEAKDVKPKEDPQETGEPAGNTATTTAPAGDDAVRTEHLYKHPLMNVWTLWYLENDRSKSWEDMQNEITSFDTVEDFWSLYNHIKPPSEIKLGSDYSLFKKNIRPMWEDAANKQGGRWVITLNKSSKTDLDNLWLDVLLCLIGEAFDHSDQICGAVINIRGKSNKISIWTADGNNEEAALEIGHKLRDALRLGRNNSLQYQLHKDTMVKQGSNVKSIYTL","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_P48598","disprot_id":"DP02400","ncbi_taxon_id":7227,"regions_counter":2,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":68,"region_id":"DP02400r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"N-terminal unstructured regions of metazoan eIF4Es","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27773676","version":2,"reference_html":"The Structures of eIF4E-eIF4G Complexes Reveal an Extended Interface to Regulate Translation Initiation. <i> Grüner S, Peter D, Weber R, Wohlbold L, Chung MY, Weichenrieder O, Valkov E, Igreja C, Izaurralde E. </i> Mol Cell, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5T48"},{"db":"PDB","id":"5T47"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","uniref100":"UniRef100_P48598","date":"2019-12-02T16:26:17.064Z","acc":"P48598","name":"Eukaryotic translation initiation factor 4E1","length":259,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI0000124818","genes":[{"name":{"value":"eIF4E1","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0015218","url":"http://flybase.org/reports/FBgn0015218.html"}}]},"synonyms":[{"value":"eIF-4E","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"7742371","url":"http://www.ncbi.nlm.nih.gov/pubmed/7742371","alternativeUrl":"https://europepmc.org/abstract/MED/7742371"}}]},{"value":"Eif4e","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"14691132","url":"http://www.ncbi.nlm.nih.gov/pubmed/14691132","alternativeUrl":"https://europepmc.org/abstract/MED/14691132"}}]}],"orfNames":[{"value":"CG4035","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0015218","url":"http://flybase.org/reports/FBgn0015218.html"}}]}]}],"alphafold_very_low_content":0.23938223938223938,"disorder_content":0.2625482625482625,"disprot_consensus":{"full":[{"start":1,"end":68,"type":"D"}],"Structural state":[{"start":1,"end":68,"type":"D"}]}},{"features":{"gene3D":[{"start":1515,"end":1662,"id":"G3DSA:1.25.40.180","name":"G3DSA:1.25.40.180"},{"start":1515,"end":1662,"id":"G3DSA:1.25.40.180","name":"G3DSA:1.25.40.180"},{"start":1515,"end":1662,"id":"G3DSA:1.25.40.180","name":"G3DSA:1.25.40.180"}],"pfam":[{"id":"PF02020","name":"eIF4-gamma/eIF5/eIF2-epsilon","start":1593,"end":1664},{"id":"PF02847","name":"MA3 domain","start":1310,"end":1424},{"id":"PF02854","name":"MIF4G domain","start":751,"end":999},{"id":"PF21140","name":"Translation initiation factor eIF4G-like, eIF4E-binding domain","start":601,"end":656}]},"uniref50":"UniRef50_O61380","sequence":"MQQAIPTLPTQSDIDKAMQPHSAQNMYVSTGNNNSGNTRSNPQSGGIFRGPPSTPNAPRGASGGATRHVHVQPMYSQPLHQNMVLQQYTQYNPRQQTFPASHLQYAPAPMPYYQYQYVPTLQQQPPHTRSAVTVNTNVNVGNNLQPVQSGPNGPLPVPGASSSQIQLLTSTVQPGASTVMGVGGPGSTMGQVGVPPMVGVGVMTTSVQPQPVQVQPASRRRHQHRLQIIDPTTKKNILDDFDKTKSNTDNEFSDQVTSTNTPATVLSEGPIRIPQQESVGLNNLTSTSSQGSESRTNAPYIPIETTPISRTDVGPTPIVSAMTDAPSVEILPTPQRGRSKKIPIVSPKNVSESIVAPITDETDDAGSTPISRATEESMPPNQTHPNLLISDSSKHKQAVSNSEISKDAPTGLKEMHVAELESSVASENHPAGILDVNVNKSSQSLDFSADPEIDSIGAISPTSPNAVSPILHEVLDNTELSKKLENSTTERFKDSQSVEKPTHQELSLRNATDETEISAMALQDVNSLDNNQIEKTYPSKPKLNVDVSEDISSRESAIKSTSTKNTGVDVGLQSDSKPETTLNDKQDSTDLKVKVSAKISSIINYNEGQWSPNNPSGKKQYDREQLLQLREVKASRIQPEVKNVSILPQPNLMPSFIRNNNNNKRVQSMVGIIGNRSNESAGNYIGKQMSMSGVQSGGGRSSMKGMIHVNLSLNQDVKLSENENAWRPRVLNKSDGDSDAKSALEKDELVRRVRGILNKLTPERFDTLVEEIIKLKIDTPDKVDEVIVLVFEKAIDEPNFSVSYARLCQRLAAEVKVIDERMESETKSNSAHFRNALLDKTEQEFTQNVSQSTAKEKKLQPIVDKIKKCTDANEKAELEAFLEEEERKIRRRSGGTVRFIGELFKISMLTGKIIYSCIDTLLNPHSEDMLECLCKLLTTVGAKFEKTPVNSKDPSRCYSLEKSITRMQAIASKTDKDGARVSSRVRFMLQDVIDLRKNKWQTSRNEAPKTMGQIEKEAKNEQLSAQYFGTLSSTTPGGSQGGSGKRDDRGNSRYGESRSSSAYGGSHSQRGDNGNLRHQQQNNVGGNVSGGAGHSNGNNDENTWHVQTSKGSRSLAVDSNKLEGLSKLSDQNLETKKMGGLTQFIWISSDTTRLSSAPTPTPSNPFAVLSSLIDKNSNERDRDRSGPRNKGSYNKGSMERDRYDRGMHSRTGSSQGSRENSSSRGGQQGRTLLSSSVQKSTSHSKYTQQAPPTRHTVKAQSSVGSSNVNTGPLYRGSEQQTSATFSQTTRSVAPVAVFIEASETDLKLIKSVVSEIVDLSAASKEVTPGAVSCIKRVPEKLRCSFIYYILTDYLHLANVGKQYRRYLSIAVSQLIQQNYISADHLRLAYNEFTVYANDLIVDIPELWLYILQFAGPLIVKKILTISDLWNNNLKENSPSNVAKKFLKTYLIYCTQEVGPNFARNMWIKFNLKWSDFMPESEVADFIKFNRLEYVENESKSPVIDHRETPEKHVKNVIDHIEHLLKEGTTADCIIDYSNGNIMVVDKLFIRGLTETLSNFSIHYKDNSYKLESETFQKFCIPVLQRYIDSNEDHQLECLYTLQLLVHGLEHPRGLLSELIGELYDAFVIQKESLCKWRDSKDQSAGKGVAVKSLNPFFNSLLNDDAN","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref90":"UniRef90_O61380","disprot_id":"DP02401","ncbi_taxon_id":7227,"regions_counter":7,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":660,"region_id":"DP02401r003","start":633,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"the N-terminal region establishes a stabilizing network of intramolecular hydrogen bonds (Figure 3H) and likely undergoes a disorder-to-order transition when binding to eIF4E.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27773676","version":2,"reference_html":"The Structures of eIF4E-eIF4G Complexes Reveal an Extended Interface to Regulate Translation Initiation. <i> Grüner S, Peter D, Weber R, Wohlbold L, Chung MY, Weichenrieder O, Valkov E, Igreja C, Izaurralde E. </i> Mol Cell, 2016","date":"2022-08-05T14:13:33.521Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5T48"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-08T17:23:59.936Z"}},{"start":578,"end":601,"reference_id":"25702871","reference_source":"pmid","reference_html":"Molecular architecture of 4E-BP translational inhibitors bound to eIF4E. <i> Peter D, Igreja C, Weber R, Wohlbold L, Weiler C, Ebertsch L, Weichenrieder O, Izaurralde E. </i> Mol Cell, 2015","date":"2023-11-24T12:40:25.620Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4UEC"}],"region_id":"DP02401r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"48598"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEMBL","id":"1234306"}],"statement":[{"text":"In the eIF4G-eIF4E complex, only the canonical motif and additional short N- and C-terminal extensions were observed (Figures 1H and S2B–S2F). The auxiliary VKNVSI was not visible in our structure, suggesting that it may form transient interactions or may be susceptible to proteolysis.","type":"Results"}]},{"start":638,"end":650,"reference_id":"25702871","reference_source":"pmid","reference_html":"Molecular architecture of 4E-BP translational inhibitors bound to eIF4E. <i> Peter D, Igreja C, Weber R, Wohlbold L, Weiler C, Ebertsch L, Weichenrieder O, Izaurralde E. </i> Mol Cell, 2015","date":"2023-11-24T12:40:34.694Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4UEC"}],"region_id":"DP02401r007","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"48598"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEMBL","id":"1234306"}],"statement":[{"text":"In the eIF4G-eIF4E complex, only the canonical motif and additional short N- and C-terminal extensions were observed (Figures 1H and S2B–S2F). The auxiliary VKNVSI was not visible in our structure, suggesting that it may form transient interactions or may be susceptible to proteolysis.","type":"Results"}]}],"released":"2023_12","uniref100":"UniRef100_O61380","date":"2019-12-02T16:36:35.072Z","acc":"O61380","name":"Eukaryotic translation initiation factor 4G1, isoform A","length":1666,"organism":"Drosophila melanogaster","dataset":[],"UniParc":"UPI00000077A8","genes":[{"name":{"value":"eIF4G1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF59403.3","url":"https://www.ebi.ac.uk/ena/browser/view/AAF59403.3"}},{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0023213","url":"http://flybase.org/reports/FBgn0023213.html"}}]},"synonyms":[{"value":"deIF4G","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF59403.3","url":"https://www.ebi.ac.uk/ena/browser/view/AAF59403.3"}}]},{"value":"Dmel\\CG10811","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF59403.3","url":"https://www.ebi.ac.uk/ena/browser/view/AAF59403.3"}}]},{"value":"eIF-4G","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF59403.3","url":"https://www.ebi.ac.uk/ena/browser/view/AAF59403.3"}},{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0023213","url":"http://flybase.org/reports/FBgn0023213.html"}}]},{"value":"EIF4G","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF59403.3","url":"https://www.ebi.ac.uk/ena/browser/view/AAF59403.3"}}]},{"value":"Eif4G","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF59403.3","url":"https://www.ebi.ac.uk/ena/browser/view/AAF59403.3"}}]},{"value":"eIF4G","evidences":[{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0023213","url":"http://flybase.org/reports/FBgn0023213.html"}}]},{"value":"eIF4g","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF59403.3","url":"https://www.ebi.ac.uk/ena/browser/view/AAF59403.3"}}]},{"value":"eIF4G-RA","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ACK77586.1","url":"https://www.ebi.ac.uk/ena/browser/view/ACK77586.1"}}]},{"value":"p200","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF59403.3","url":"https://www.ebi.ac.uk/ena/browser/view/AAF59403.3"}}]}],"orfNames":[{"value":"CG10811","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF59403.3","url":"https://www.ebi.ac.uk/ena/browser/view/AAF59403.3"}},{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0023213","url":"http://flybase.org/reports/FBgn0023213.html"}}]},{"value":"Dmel_CG10811","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF59403.3","url":"https://www.ebi.ac.uk/ena/browser/view/AAF59403.3"}}]}]}],"disorder_content":0.031212484993997598,"disprot_consensus":{"full":[{"start":578,"end":601,"type":"D"},{"start":633,"end":660,"type":"D"}],"Structural state":[{"start":578,"end":601,"type":"D"},{"start":633,"end":660,"type":"D"}]}},{"features":{"gene3D":[{"start":8,"end":136,"id":"G3DSA:1.25.40.90","name":"G3DSA:1.25.40.90"}],"pfam":[{"id":"PF01417","name":"ENTH domain","start":24,"end":131},{"id":"PF25827","name":"Tepsin VHS/ENTH-like domain","start":244,"end":348}]},"uniref50":"UniRef50_Q96N21","sequence":"MAAAPPLRDRLSFLHRLPILLKGTSDDDVPCPGYLFEEIAKISHESPGSSQCLLEYLLSRLHSSSGHGKLKVLKILLYLCSHGSSFFLLILKRNSAFIQEAAAFAGPPDPLHGNSLYQKVRAAAQDLGSTLFSDTVLPLAPSQPLGTPPATGMGSQARPHSTLQGFGYSKEHGRTAVRHQPGQAGGGWDELDSGPSSQNSSQNSDLSRVSDSGSHSGSDSHSGASREPGDLAERVEVVALSDCQQELSLVRTVTRGPRAFLSREEAQHFIKACGLLNCEAVLQLLTCHLRGTSECTQLRALCAIASLGSSDLLPQEHILLRTRPWLQELSMGSPGPVTNKATKILRHFEASCGQLSPARGTSAEPGPTAALPGPSDLLTDAVPLPGSQVFLQPLSSTPVSSRSPAPSSGMPSSPVPTPPPDASPIPAPGDPSEAEARLAESRRWRPERIPGGTDSPKRGPSSCAWSRDSLFAGMELVACPRLVGAGAAAGESCPDAPRAPQTSSQRTAAKEPPGSEPSAFAFLNA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q96N21","disprot_id":"DP02404","ncbi_taxon_id":9606,"regions_counter":1,"creator":"fquaglia","regions":[{"region_id":"DP02404r001","ec_ontology":"ECO","end":153,"term_id":"IDPO:0000002","start":136,"version":2,"statement":[{"text":"Together these data suggest that additional amino acids beyond residue 136 in the longer construct are disordered and the tepsin ENTH domain is indeed smaller than other published ENTH structures by two α-helices.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28691777","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5WF9"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structure and evolution of ENTH and VHS/ENTH-like domains in tepsin. <i> Archuleta TL, Frazier MN, Monken AE, Kendall AK, Harp J, McCoy AJ, Creanza N, Jackson LP. </i> Traffic, 2017","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","uniref100":"UniRef100_Q96N21","date":"2019-12-02T17:15:00.157Z","acc":"Q96N21","name":"AP-4 complex accessory subunit Tepsin","length":525,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000071221","genes":[{"name":{"value":"TEPSIN","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"22472443","url":"http://www.ncbi.nlm.nih.gov/pubmed/22472443","alternativeUrl":"https://europepmc.org/abstract/MED/22472443"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:26458","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:26458"}}]},"synonyms":[{"value":"C17orf56","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:26458","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:26458"}}]},{"value":"ENTHD2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:26458","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:26458"}}]}]}],"alphafold_very_low_content":0.4361904761904762,"disorder_content":0.03428571428571429,"disprot_consensus":{"full":[{"start":136,"end":153,"type":"D"}],"Structural state":[{"start":136,"end":153,"type":"D"}]}},{"features":{"gene3D":[{"start":1,"end":113,"id":"G3DSA:3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"}],"pfam":[{"id":"PF14447","name":"Prokaryotic RING finger family 4","start":16,"end":64}]},"uniref50":"UniRef50_Q8IYW5","sequence":"MALPKDAIPSLSECQCGICMEILVEPVTLPCNHTLCKPCFQSTVEKASLCCPFCRRRVSSWTRYHTRRNSLVNVELWTIIQKHYPRECKLRASGQESEEVADDYQPVRLLSKPGELRREYEEEISKVAAERRASEEEENKASEEYIQRLLAEEEEEEKRQAEKRRRAMEEQLKSDEELARKLSIDINNFCEGSISASPLNSRKSDPVTPKSEKKSKNKQRNTGDIQKYLTPKSQFGSASHSEAVQEVRKDSVSKDIDSSDRKSPTGQDTEIEDMPTLSPQISLGVGEQGADSSIESPMPWLCACGAEWYHEGNVKTRPSNHGKELCVLSHERPKTRVPYSKETAVMPCGRTESGCAPTSGVTQTNGNNTGETENEESCLLISKEISKRKNQESSFEAVKDPCFSAKRRKVSPESSPDQEETEINFTQKLIDLEHLLFERHKQEEQDRLLALQLQKEVDKEQMVPNRQKGSPDEYHLRATSSPPDKVLNGQRKNPKDGNFKRQTHTKHPTPERGSRDKNRQVSLKMQLKQSVNRRKMPNSTRDHCKVSKSAHSLQPSISQKSVFQMFQRCTK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q8IYW5","disprot_id":"DP02405","ncbi_taxon_id":9606,"regions_counter":1,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":111,"region_id":"DP02405r001","start":94,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The overall structure of RNF168N-111 contains ordered residues from L3 to S93. The residues from G94 to S111 could not be observed in the electron density map, indicating high flexibility of this region","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23255131","version":2,"reference_html":"Structural basis for role of ring finger protein RNF168 RING domain. <i> Zhang X, Chen J, Wu M, Wu H, Arokiaraj AW, Wang C, Zhang W, Tao Y, Huen MS, Zang J. </i> Cell Cycle, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4GB0"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-19T13:52:35.886Z"}}],"released":"2023_12","uniref100":"UniRef100_Q8IYW5","date":"2019-12-03T10:44:05.710Z","acc":"Q8IYW5","name":"E3 ubiquitin-protein ligase RNF168","length":571,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00000741D1","genes":[{"name":{"value":"RNF168","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03066","url":"https://hamap.expasy.org/unirule/MF_03066"}}]}}],"alphafold_very_low_content":0.5236427320490368,"disorder_content":0.03152364273204904,"disprot_consensus":{"full":[{"start":94,"end":111,"type":"D"}],"Structural state":[{"start":94,"end":111,"type":"D"}]}},{"features":{"pfam":[]},"uniref50":"","sequence":"MPGMMEKGPELLGKNRSANGSAKSPAGGGGSGASSTNGGLHYSEPESGCSSDDEHDVGMRVGAEYQARIPEFDPGATKYTDKDNGGMLVWSPYHSIPDAKLDEYIAIAKEKHGYNVEQALGMLFWHKHNIEKSLADLPNFTPFPDEWTVEDKVLFEQAFSFHGKSFHRIQQMLPDKTIASLVKYYYSWKKTRSRTSLMDRQARKLANRHNQGDSDDDVEETHPMDGNDSDYDPKKEAKKEGNTEQPVQTSKIGLGRREYQSLQHRHHSQRSKCRPPKGMYLTQEDVVAVSCSPNAANTILRQLDMELISLKRQVQNAKQVNSALKQKMEGGIEEFKPPESNQKINARWTTEEQLLAVQGVRKYGKDFQAIADVIGNKTVGQVKNFFVNYRRRFNLEEVLQEWEAEQGTQASNGDASTLGEETKSASNVPSGKSTDEEEEAQTPQAPRTLGPSPPAPSSTPTPTAPIATLNQPPPLLRPTLPAAPALHRQPPPLQQQARFIQPRPTLNQPPPPLIRPANSMPPRLNPRPVLSTVGGQQPPSLIGIQTDSQSSLH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"","disprot_id":"DP02408","ncbi_taxon_id":9606,"regions_counter":2,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":272,"region_id":"DP02408r001","reference_id":"24820421","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The final model consists of residues 171 to 836 of LSD1/KDM1A, a FAD molecule, and residues 273 to 405 of CoREST3","type":"Table"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Differential properties of transcriptional complexes formed by the CoREST family. <i> Barrios ÁP, Gómez AV, Sáez JE, Ciossani G, Toffolo E, Battaglioli E, Mattevi A, Andrés ME. </i> Mol Cell Biol, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4CZZ"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":553,"region_id":"DP02408r002","reference_id":"24820421","start":406,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The final model consists of residues 171 to 836 of LSD1/KDM1A, a FAD molecule, and residues 273 to 405 of CoREST3","type":"Table"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Differential properties of transcriptional complexes formed by the CoREST family. <i> Barrios ÁP, Gómez AV, Sáez JE, Ciossani G, Toffolo E, Battaglioli E, Mattevi A, Andrés ME. </i> Mol Cell Biol, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4CZZ"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","uniref100":"","date":"2019-12-03T11:29:29.206Z","acc":"Q9P2K3-3","name":"Isoform 3 of REST corepressor 3","length":553,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI00005AE45B","genes":[{"name":{"value":"RCOR3"},"synonyms":[{"value":"KIAA1343"}]}],"disorder_content":0.759493670886076,"disprot_consensus":{"full":[{"start":1,"end":272,"type":"D"},{"start":406,"end":553,"type":"D"}],"Structural state":[{"start":1,"end":272,"type":"D"},{"start":406,"end":553,"type":"D"}]}},{"features":{"gene3D":[{"start":1,"end":164,"id":"G3DSA:3.80.10.10","name":"Ribonuclease Inhibitor"}],"pfam":[{"id":"PF14580","name":"Leucine-rich repeat","start":33,"end":146}]},"uniref50":"UniRef50_Q9BTT0","sequence":"MEMKKKINLELRNRSPEEVTELVLDNCLCVNGEIEGLNDTFKELEFLSMANVELSSLARLPSLNKLRKLELSDNIISGGLEVLAEKCPNLTYLNLSGNKIKDLSTVEALQNLKNLKSLDLFNCEITNLEDYRESIFELLQQITYLDGFDQEDNEAPDSEEEDDEDGDEDDEEEEENEAGPPEGYEEEEEEEEEEDEDEDEDEDEAGSELGEGEEEVGLSYLMKEEIQDEEDDDDYVEEGEEEEEEEEGGLRGEKRKRDAEDDGEEEDD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9BTT0","disprot_id":"DP02409","ncbi_taxon_id":9606,"regions_counter":4,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":213,"region_id":"DP02409r001","start":186,"term_id":"IDPO:0000002","statement":[{"text":"Anp32e residues 186-213 and 225-232 were not observable in the structure because of lack of electron density","type":"Results"},{"text":"We determined the crystal structure of the Anp32e chaperone domain (186-232) in complex with the H2A.Z-H2B dimer. In this structure, the region containing Anp32e residues 214-224, which is absent in other Anp32 family proteins, specifically interacts with the extended H2A.Z αC helix, which exhibits an unexpected conformational change.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24613878","version":2,"reference_html":"Anp32e, a higher eukaryotic histone chaperone directs preferential recognition for H2A.Z. <i> Mao Z, Pan L, Wang W, Sun J, Shan S, Dong Q, Liang X, Dai L, Ding X, Chen S, Zhang Z, Zhu B, Zhou Z. </i> Cell Res, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4NFT"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":224,"region_id":"DP02409r002","start":214,"term_id":"IDPO:0000011","statement":[{"text":"We determined the crystal structure of the Anp32e chaperone domain (186-232) in complex with the H2A.Z-H2B dimer. In this structure, the region containing Anp32e residues 214-224, which is absent in other Anp32 family proteins, specifically interacts with the extended H2A.Z αC helix, which exhibits an unexpected conformational change.","type":"Abstract"},{"text":"The overall structure of the Anp32e186-232-lnkH2B-H2A.Z complex. The sequence of the observable part of Anp32e in the structure is 214EEVGLSYLMKE224","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24613878","version":2,"reference_html":"Anp32e, a higher eukaryotic histone chaperone directs preferential recognition for H2A.Z. <i> Mao Z, Pan L, Wang W, Sun J, Shan S, Dong Q, Liang X, Dai L, Ding X, Chen S, Zhang Z, Zhu B, Zhou Z. </i> Cell Res, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4NFT"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP02409r003","ec_ontology":"ECO","end":224,"term_id":"GO:0005515","start":214,"version":3,"statement":[{"text":"We determined the crystal structure of the Anp32e chaperone domain (186-232) in complex with the H2A.Z-H2B dimer. In this structure, the region containing Anp32e residues 214-224, which is absent in other Anp32 family proteins, specifically interacts with the extended H2A.Z αC helix, which exhibits an unexpected conformational change.","type":"Abstract"},{"text":"The overall structure of the Anp32e186-232-lnkH2B-H2A.Z complex. The sequence of the observable part of Anp32e in the structure is 214EEVGLSYLMKE224","type":"Figure"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P0C0S5","partner_end":null},{"partner_start":null,"db":"UniProt","id":"Q16778","partner_end":null}],"term_name":"protein binding","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"24613878","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4NFT"}],"term_namespace":"Molecular function","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Anp32e, a higher eukaryotic histone chaperone directs preferential recognition for H2A.Z. <i> Mao Z, Pan L, Wang W, Sun J, Shan S, Dong Q, Liang X, Dai L, Ding X, Chen S, Zhang Z, Zhu B, Zhou Z. </i> Cell Res, 2014","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":232,"region_id":"DP02409r004","start":186,"term_id":"GO:0044183","statement":[{"text":"We determined the crystal structure of the Anp32e chaperone domain (186-232) in complex with the H2A.Z-H2B dimer. ","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"24613878","version":3,"reference_html":"Anp32e, a higher eukaryotic histone chaperone directs preferential recognition for H2A.Z. <i> Mao Z, Pan L, Wang W, Sun J, Shan S, Dong Q, Liang X, Dai L, Ding X, Chen S, Zhang Z, Zhu B, Zhou Z. </i> Cell Res, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4NFT"}],"term_name":"protein folding chaperone","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","uniref100":"UniRef100_Q9BTT0","date":"2019-12-03T13:52:41.009Z","acc":"Q9BTT0","name":"Acidic leucine-rich nuclear phosphoprotein 32 family member E","length":268,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0000071679","genes":[{"name":{"value":"ANP32E"}}],"alphafold_very_low_content":0.11194029850746269,"disorder_content":0.1044776119402985,"disprot_consensus":{"full":[{"start":186,"end":213,"type":"D"},{"start":214,"end":224,"type":"T"},{"start":225,"end":232,"type":"F"}],"Structural state":[{"start":186,"end":213,"type":"D"}],"Structural transition":[{"start":214,"end":224,"type":"T"}],"Molecular function":[{"start":186,"end":232,"type":"F"}]}},{"features":{"gene3D":[{"start":249,"end":319,"id":"G3DSA:1.10.260.40","name":"lambda repressor-like DNA-binding domains"}],"pfam":[{"id":"PF00046","name":"Homeodomain","start":338,"end":394},{"id":"PF00157","name":"Pou domain - N-terminal to homeobox domain","start":250,"end":319}]},"uniref50":"UniRef50_P20267","sequence":"MATTAQYLPRGPGGGAGGTGPLMHPDAAAAAAAAAERLHAGAAYREVQKLMHHEWLGAGAGHPVGLAHPQWLPTGGGGGGDWAGGPHLEHGKAGGGGTGRADDGGGGGGFHARLVHQGAAHAGAAWAQGGTAHHLGPAMSPSPGAGGGHQPQPLGLYAQAAYPGGGGGGLAGMLAAGGGGAGPGLHHALHEDGHEAQLEPSPPPHLGAHGHAHGHAHAGGLHAAAAHLHPGAGGGGSSVGEHSDEDAPSSDDLEQFAKQFKQRRIKLGFTQADVGLALGTLYGNVFSQTTICRFEALQLSFKNMCKLKPLLNKWLEETDSSSGSPTNLDKIAAQGRKRKKRTSIEVGVKGALESHFLKCPKPSAHEITGLADSLQLEKEVVRVWFCNRRQKEKRMTPAAGAGHPPMDDVYAPGELGPGGGSASPPSAPPPPPPAALHHHHHHTLPGSVQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_P20267","disprot_id":"DP02410","ncbi_taxon_id":10090,"regions_counter":2,"creator":"fquaglia","regions":[{"region_id":"DP02410r001","validated":{"curator_id":"bmesza","timestamp":"2020-11-27T14:56:07.781Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":342,"term_id":"IDPO:0000033","start":319,"version":3,"statement":[{"text":"The final model comprises POU specific (POUS) and POU homeodomain (POUHD) but the connecting linker was structurally disordered and could thus not be built.","type":"Results"}],"term_name":"flexible linker","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21117060","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2XSD"}],"term_namespace":"Disorder function","ec_id":"ECO:0006165","curator_id":"fquaglia","reference_html":"Crystal structure of the dimeric Oct6 (POU3f1) POU domain bound to palindromic MORE DNA. <i> Jauch R, Choo SH, Ng CK, Kolatkar PR. </i> Proteins, 2011","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"region_id":"DP02410r002","validated":{"curator_id":"bmesza","timestamp":"2020-11-27T14:56:06.187Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":342,"term_id":"IDPO:0000002","start":319,"version":2,"statement":[{"text":"The final model comprises POU specific (POUS) and POU homeodomain (POUHD) but the connecting linker was structurally disordered and could thus not be built.","type":"Results"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21117060","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2XSD"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"fquaglia","reference_html":"Crystal structure of the dimeric Oct6 (POU3f1) POU domain bound to palindromic MORE DNA. <i> Jauch R, Choo SH, Ng CK, Kolatkar PR. </i> Proteins, 2011","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","uniref100":"UniRef100_P21952","date":"2019-12-03T14:18:13.467Z","acc":"P21952","name":"POU domain, class 3, transcription factor 1","length":449,"organism":"Mus musculus","dataset":[],"UniParc":"UPI000002961F","genes":[{"name":{"value":"Pou3f1"},"synonyms":[{"value":"Oct6"},{"value":"Otf-6"},{"value":"Otf6"},{"value":"Scip"}]}],"alphafold_very_low_content":0.512249443207127,"disorder_content":0.053452115812917596,"disprot_consensus":{"full":[{"start":319,"end":342,"type":"D"}],"Structural state":[{"start":319,"end":342,"type":"D"}],"Disorder function":[{"start":319,"end":342,"type":"F"}]}},{"features":{"gene3D":[{"start":219,"end":321,"id":"G3DSA:1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}],"pfam":[{"id":"PF00250","name":"Forkhead domain","start":235,"end":315}]},"uniref50":"UniRef50_Q08050","sequence":"MKTSPRRPLILKRRRLPLPVQNAPSETSEEEPKRSPAQQESNQAEASKEVAESNSCKFPAGIKIINHPTMPNTQVVAIPNNANIHSIITALTAKGKESGSSGPNKFILISCGGAPTQPPGLRPQTQTSYDAKRTEVTLETLGPKPAARDVNLPRPPGALCEQKRETCADGEAAGCTINNSLSNIQWLRKMSSDGLGSRSIKQEMEEKENCHLEQRQVKVEEPSRPSASWQNSVSERPPYSYMAMIQFAINSTERKRMTLKDIYTWIEDHFPYFKHIAKPGWKNSIRHNLSLHDMFVRETSANGKVSFWTIHPSANRYLTLDQVFKPLDPGSPQLPEHLESQQKRPNPELRRNMTIKTELPLGARRKMKPLLPRVSSYLVPIQFPVNQSLVLQPSVKVPLPLAASLMSSELARHSKRVRIAPKVLLAEEGIAPLSSAGPGKEEKLLFGEGFSPLLPVQTIKEEEIQPGEEMPHLARPIKVESPPLEEWPSPAPSFKEESSHSWEDSSQSPTPRPKKSYSGLRSPTRCVSEMLVIQHRERRERSRSRRKQHLLPPCVDEPELLFSEGPSTSRWAAELPFPADSSDPASQLSYSQEVGGPFKTPIKETLPISSTPSKSVLPRTPESWRLTPPAKVGGLDFSPVQTSQGASDPLPDPLGLMDLSTTPLQSAPPLESPQRLLSSEPLDLISVPFGNSSPSDIDVPKPGSPEPQVSGLAANRSLTEGLVLDTMNDSLSKILLDISFPGLDEDPLGPDNINWSQFIPELQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q08050","disprot_id":"DP02411","ncbi_taxon_id":9606,"regions_counter":9,"creator":"smribeiro","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":231,"region_id":"DP02411r001","start":222,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Neither molecule displays electron density for the first 10 N-terminal residues or the 25–30 C-terminal ones, indicating a degree of disorder in these regions.","type":"Results"},{"text":"Our model consists of: the entire double-stranded DNA molecule; 2 magnesium ions; 163 water molecules; FoxM1 residues 232–321 in the A molecule and residues 235–327 in the B molecule","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20360045","version":2,"reference_html":"Structure of the FoxM1 DNA-recognition domain bound to a promoter sequence. <i> Littler DR, Alvarez-Fernández M, Stein A, Hibbert RG, Heidebrecht T, Aloy P, Medema RH, Perrakis A. </i> Nucleic Acids Res, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3G73"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T07:43:30.575Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":360,"region_id":"DP02411r002","start":327,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Neither molecule displays electron density for the first 10 N-terminal residues or the 25–30 C-terminal ones, indicating a degree of disorder in these regions.","type":"Results"},{"text":"Our model consists of: the entire double-stranded DNA molecule; 2 magnesium ions; 163 water molecules; FoxM1 residues 232–321 in the A molecule and residues 235–327 in the B molecule","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20360045","version":2,"reference_html":"Structure of the FoxM1 DNA-recognition domain bound to a promoter sequence. <i> Littler DR, Alvarez-Fernández M, Stein A, Hibbert RG, Heidebrecht T, Aloy P, Medema RH, Perrakis A. </i> Nucleic Acids Res, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3G73"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T07:43:29.608Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":114,"reference_id":"31134895","reference_source":"pmid","reference_html":"An order-to-disorder structural switch activates the FoxM1 transcription factor. <i> Marceau AH, Brison CM, Nerli S, Arsenault HE, McShan AC, Chen E, Lee HW, Benanti JA, Sgourakis NG, Rubin SM. </i> Elife, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP02411r005","statement":[{"text":"To probe the structures of the NRD and TAD once they are dissociated, we acquired circular dichroism (CD) spectra on isolated human NRD (residues 1–114) and TAD (694-748) domains and compared them to the human homolog of the NRD-TAD fusion construct used for NMR (1-117/694-748; Δ25–50) (Figure 5A and Figure 5—figure supplement 1A). We used the minimal NRD construct for CD analysis, because NMR data suggest the region between 115–203 is disordered (Figure 5—figure supplement 2).","type":"Results"},{"text":"WT NRD alone is already considerably disordered","type":"Results"},{"text":"We observe that while both the FoxM1 NRD and TAD are primarily intrinsically disordered domains, they associate and adopt a structured conformation.","type":"Abstract"},{"text":"In contrast, the TAD and NRD spectra indicate relatively greater disorder, although they do reflect some secondary structure content. ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T06:57:23.838Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":694,"end":748,"reference_id":"31134895","reference_source":"pmid","reference_html":"An order-to-disorder structural switch activates the FoxM1 transcription factor. <i> Marceau AH, Brison CM, Nerli S, Arsenault HE, McShan AC, Chen E, Lee HW, Benanti JA, Sgourakis NG, Rubin SM. </i> Elife, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP02411r006","statement":[{"text":"To probe the structures of the NRD and TAD once they are dissociated, we acquired circular dichroism (CD) spectra on isolated human NRD (residues 1–114) and TAD (694-748) domains and compared them to the human homolog of the NRD-TAD fusion construct used for NMR (1-117/694-748; Δ25–50) (Figure 5A and Figure 5—figure supplement 1A).","type":"Results"},{"text":"In contrast, the TAD and NRD spectra indicate relatively greater disorder, although they do reflect some secondary structure content. ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T06:57:21.988Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":694,"end":748,"reference_id":"31134895","reference_source":"pmid","reference_html":"An order-to-disorder structural switch activates the FoxM1 transcription factor. <i> Marceau AH, Brison CM, Nerli S, Arsenault HE, McShan AC, Chen E, Lee HW, Benanti JA, Sgourakis NG, Rubin SM. </i> Elife, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP02411r007","statement":[{"text":"We tested three common TAD interaction domains in CBP and found that purified TAZ2 and KIX domains bind the FoxM1 TAD, while TAZ1 does not ","type":"Results"},{"text":"Using sequence conservation we designed a minimal NRD (1-114) and minimal TAD (696-748) and found that they associate with comparable affinity (Kd = 3 ± 2 µM). ","type":"Results"}],"interaction_partner":[{"db":"UniProt","id":"Q09472","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T09:59:40.872Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":114,"reference_id":"31134895","reference_source":"pmid","reference_html":"An order-to-disorder structural switch activates the FoxM1 transcription factor. <i> Marceau AH, Brison CM, Nerli S, Arsenault HE, McShan AC, Chen E, Lee HW, Benanti JA, Sgourakis NG, Rubin SM. </i> Elife, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP02411r008","statement":[{"text":"Both the NRD and fusion elute in earlier fractions than expected based on their molecular weights, suggesting larger hydrodynamic radii than the standard globular proteins due to structural disorder. ","type":"Supplementary material"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T09:58:36.043Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":114,"reference_id":"31134895","reference_source":"pmid","reference_html":"An order-to-disorder structural switch activates the FoxM1 transcription factor. <i> Marceau AH, Brison CM, Nerli S, Arsenault HE, McShan AC, Chen E, Lee HW, Benanti JA, Sgourakis NG, Rubin SM. </i> Elife, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP02411r009","statement":[{"text":" Using sequence conservation we designed a minimal NRD (1-114) and minimal TAD (696-748) and found that they associate with comparable affinity (Kd = 3 ± 2 µM). ","type":"Results"}],"interaction_partner":[{"db":"UniProt","id":"Q08050","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T09:59:33.871Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2023_12","uniref100":"UniRef100_Q08050","date":"2019-12-03T14:37:04.644Z","acc":"Q08050","name":"Forkhead box protein M1","length":763,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI000016AD75","genes":[{"name":{"value":"FOXM1"},"synonyms":[{"value":"FKHL16"},{"value":"HFH11"},{"value":"MPP2"},{"value":"WIN"}]}],"alphafold_very_low_content":0.6972477064220184,"disorder_content":0.27916120576671033,"disprot_consensus":{"full":[{"start":1,"end":114,"type":"D"},{"start":222,"end":231,"type":"D"},{"start":327,"end":360,"type":"D"},{"start":694,"end":748,"type":"D"}],"Structural state":[{"start":1,"end":114,"type":"D"},{"start":222,"end":231,"type":"D"},{"start":327,"end":360,"type":"D"},{"start":694,"end":748,"type":"D"}],"Molecular function":[{"start":1,"end":114,"type":"F"},{"start":694,"end":748,"type":"F"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF07412","name":"Geminin","start":1,"end":180}]},"uniref50":"UniRef50_O75496","sequence":"MNLSMKQKQEGAQENVKNSPVPRRTLKMIQPSADGSLVGRENELPKGLFKRKLWDDQLASQTSSCGPEANENKDVGDLTQEAFDLISKENPSSQYWKEVAEQRRKALYEALKENEKLHKEIEQKDSEIARLRKENKDLAEVAEHVQYMAEVIERLSNEPLDNFESPDSQEFDSEEEAVEYSELEDSGAGTCAEETVSSSTDARPCT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_O88513","disprot_id":"DP02412","ncbi_taxon_id":10090,"regions_counter":5,"creator":"fquaglia","regions":[{"region_id":"DP02412r001","ec_ontology":"ECO","end":89,"term_id":"IDPO:0000002","start":79,"version":2,"statement":[{"text":"The N-terminal ten residues are structured in the tGeminin monomer that binds to tCdt1 but are disordered in the other tGeminin monomer, indicating that this region might undergo induced folding after binding to tCdt1","type":"Figure"},{"text":"Here we describe the crystal structure of the mouse geminin–Cdt1 complex using tGeminin (residues 79–157, truncated geminin) and tCdt1 (residues 172–368, truncated Cdt1). The amino-terminal region of a coiled-coil dimer of tGeminin interacts with both N-terminal and carboxy-terminal parts of tCdt1","type":"Abstract"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15286659","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2ZXX"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structural basis for inhibition of the replication licensing factor Cdt1 by geminin. <i> Lee C, Hong B, Choi JM, Kim Y, Watanabe S, Ishimi Y, Enomoto T, Tada S, Kim Y, Cho Y. </i> Nature, 2004","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02412r002","ec_ontology":"ECO","end":89,"term_id":"IDPO:0000011","start":79,"version":2,"statement":[{"text":"The N-terminal ten residues are structured in the tGeminin monomer that binds to tCdt1 but are disordered in the other tGeminin monomer, indicating that this region might undergo induced folding after binding to tCdt1","type":"Figure"},{"text":"Here we describe the crystal structure of the mouse geminin–Cdt1 complex using tGeminin (residues 79–157, truncated geminin) and tCdt1 (residues 172–368, truncated Cdt1). The amino-terminal region of a coiled-coil dimer of tGeminin interacts with both N-terminal and carboxy-terminal parts of tCdt1","type":"Abstract"}],"term_name":"disorder to order","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15286659","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2ZXX"}],"term_namespace":"Structural transition","ec_id":"ECO:0005670","curator_id":"fquaglia","reference_html":"Structural basis for inhibition of the replication licensing factor Cdt1 by geminin. <i> Lee C, Hong B, Choi JM, Kim Y, Watanabe S, Ishimi Y, Enomoto T, Tada S, Kim Y, Cho Y. </i> Nature, 2004","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP02412r003","ec_ontology":"ECO","end":89,"term_id":"GO:0005515","start":79,"version":3,"statement":[{"text":"The N-terminal ten residues are structured in the tGeminin monomer that binds to tCdt1 but are disordered in the other tGeminin monomer, indicating that this region might undergo induced folding after binding to tCdt1","type":"Figure"},{"text":"Here we describe the crystal structure of the mouse geminin–Cdt1 complex using tGeminin (residues 79–157, truncated geminin) and tCdt1 (residues 172–368, truncated Cdt1). The amino-terminal region of a coiled-coil dimer of tGeminin interacts with both N-terminal and carboxy-terminal parts of tCdt1","type":"Abstract"},{"text":"The crystal structure, in conjunction with our biochemical data, indicates that the N-terminal region of tGeminin might be required to anchor tCdt1","type":"Abstract"},{"text":"In the second part of the tGeminin–tCdt1 interface, a surface groove on Cdt1 formed by helix H6 and loop L2 of tCdt1 binds the ten residues in the N-terminal loop of tGemimin monomer (Fig. 2b).","type":"Article"},{"text":"The ten residues immediately N-terminal to the coiled-coil domain form a loop and a short helix. These residues and the N-terminal part of the coiled coil of tGeminin bind to tCdt1.","type":"Article"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q8R4E9","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","reference_html":"Structural basis for inhibition of the replication licensing factor Cdt1 by geminin. <i> Lee C, Hong B, Choi JM, Kim Y, Watanabe S, Ishimi Y, Enomoto T, Tada S, Kim Y, Cho Y. </i> Nature, 2004","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15286659","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2ZXX"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"fquaglia","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02412r005","ec_ontology":"ECO","end":89,"term_id":"GO:0005515","start":79,"version":3,"statement":[{"text":"Structural basis for inhibition of the replication licensing factor Cdt1 by geminin\" Article \"The deletion of these ten residues decreased tGeminin's binding affinity to tCdt1 about 15-fold (Supplementary Table 2).","type":"Title"},{"text":"Dissociation constants of Cdt1 to geminin - determined by ITC (Supplementary Table 2) - correspond to 4.4 ± 2.2 nM in the case of tGeminin (geminin79-157) and to 56.2 ± 10.1 nM in the case of geminin89-157 where the first ten residues are deleted, thus indicating a decrease in the binding affinity.","type":"Curator statement"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q8R4E9","partner_end":null}],"term_name":"protein binding","ec_name":"isothermal titration calorimetry evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15286659","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"fquaglia","reference_html":"Structural basis for inhibition of the replication licensing factor Cdt1 by geminin. <i> Lee C, Hong B, Choi JM, Kim Y, Watanabe S, Ishimi Y, Enomoto T, Tada S, Kim Y, Cho Y. </i> Nature, 2004","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_12","uniref100":"UniRef100_O88513","date":"2019-12-03T15:01:07.832Z","acc":"O88513","name":"Geminin","length":206,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000020FC1","genes":[{"name":{"value":"Gmnn"}}],"alphafold_very_low_content":0.23300970873786409,"disorder_content":0.05339805825242718,"disprot_consensus":{"full":[{"start":79,"end":89,"type":"T"}],"Structural state":[{"start":79,"end":89,"type":"D"}],"Structural transition":[{"start":79,"end":89,"type":"T"}],"Molecular function":[{"start":79,"end":89,"type":"F"}]}},{"features":{"gene3D":[{"start":378,"end":464,"id":"G3DSA:4.10.280.10","name":"Helix-loop-helix DNA-binding domain"}],"pfam":[{"id":"PF00010","name":"Helix-loop-helix DNA-binding domain","start":382,"end":434},{"id":"PF01056","name":"Myc amino-terminal region","start":9,"end":372}]},"uniref50":"UniRef50_P04198","sequence":"MPSCSTSTMPGMICKNPDLEFDSLQPCFYPDEDDFYFGGPDSTPPGEDIWKKFELLPTPPLSPSRGFAEHSSEPPSWVTEMLLENELWGSPAEEDAFGLGGLGGLTPNPVILQDCMWSGFSAREKLERAVSEKLQHGRGPPTAGSTAQSPGAGAASPAGRGHGGAAGAGRAGAALPAELAHPAAECVDPAVVFPFPVNKREPAPVPAAPASAPAAGPAVASGAGIAAPAGAPGVAPPRPGGRQTSGGDHKALSTSGEDTLSDSDDEDDEEEDEEEEIDVVTVEKRRSSSNTKAVTTFTITVRPKNAALGPGRAQSSELILKRCLPIHQQHNYAAPSPYVESEDAPPQKKIKSEASPRPLKSVIPPKAKSLSPRNSDSEDSERRRNHNILERQRRNDLRSSFLTLRDHVPELVKNEKAAKVVILKKATEYVHSLQAEEHQLLLEKEKLQARQQQLLKKIEHARTC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P04198","disprot_id":"DP02413","ncbi_taxon_id":9606,"regions_counter":2,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":60,"region_id":"DP02413r001","start":28,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Residues 28–60 of N-Myc are not observed in the structure, whereas residues 61–89 are associated with the cleft between the N- and C-lobes of the Aurora-A kinase domain formed by the αB/αC helices, the activation loop, and the αG helix","type":"Results"},{"text":"The section of the AIR that was not resolved in the crystal structure, residues 28–60 of N-Myc, includes the MB0 and MBI regions and is conserved in c-Myc","type":"Results"},{"text":"residues 28–89 of N-Myc as the minimal Aurora-A–interaction region (AIR), which spans MB0 through MBI but does not include MBII or beyond","type":"Results"},{"text":"Other conserved sequence motifs called “Myc boxes” (MB0–IV) serve as docking sites for protein–protein interactions. The Myc transactivation domain (TAD) spans the N-terminal conserved motifs MB0, MBI, and MBII","type":"Article"}],"curator_id":"vnugnes","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"27837025","version":3,"reference_html":"Structural basis of N-Myc binding by Aurora-A and its destabilization by kinase inhibitors. <i> Richards MW, Burgess SG, Poon E, Carstensen A, Eilers M, Chesler L, Bayliss R. </i> Proc Natl Acad Sci U S A, 2016","date":"2022-06-15T20:48:12.650Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5G1X"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O14965"}]}],"released":"2022_06","uniref100":"UniRef100_P04198","date":"2019-12-03T16:48:39.750Z","acc":"P04198","name":"N-myc proto-oncogene protein","length":464,"organism":"Homo sapiens","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI00001732CE","genes":[{"name":{"value":"MYCN"},"synonyms":[{"value":"BHLHE37"},{"value":"NMYC"}]}],"alphafold_very_low_content":0.3922413793103448,"disorder_content":0.07112068965517242,"disprot_consensus":{"full":[{"start":28,"end":60,"type":"D"}],"Structural state":[{"start":28,"end":60,"type":"D"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF00046","name":"Homeodomain","start":207,"end":260}]},"uniref50":"UniRef50_P14653","sequence":"MDYNRMNSFLEYPLCNRGPSAYSAHSAPTSFPPSSAQAVDSYASEGRYGGGLSSPAFQQNSGYPAQQPPSTLGVPFPSSAPSGYAPAACSPSYGPSQYYPLGQSEGDGGYFHPSSYGAQLGGLSDGYGAGGAGPGPYPPQHPPYGNEQTASFAPAYADLLSEDKETPCPSEPNTPTARTFDWMKVKRNPPKTAKVSEPGLGSPSGLRTNFTTRQLTELEKEFHFNKYLSRARRVEIAATLELNETQVKIWFQNRRMKQKKREREEGRVPPAPPGCPKEAAGDASDQSTCTSPEASPSSVTS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P14653","disprot_id":"DP02414","ncbi_taxon_id":9606,"regions_counter":2,"creator":"fquaglia","regions":[{"region_id":"DP02414r001","ec_ontology":"ECO","end":206,"term_id":"IDPO:0000002","start":187,"version":2,"statement":[{"text":"The hexapeptide is joined to the HoxB1 homeodomain by a flexible linker, of which 20 amino acids (residues −17 to +3) are disordered in the ternary complex structure.","type":"Results"},{"text":"20 disordered residues in the HoxB1 linker","type":"Figure"},{"text":"This hexapeptide, whose consensus sequence is hydrophobic-Y/F -P-W-M-K/R, is joined to the N-terminal arm of the homeodomain by a linker that varies in length and sequence among different Hox proteins and between different species.","type":"Introduction"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10052460","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1B72"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structure of a HoxB1-Pbx1 heterodimer bound to DNA: role of the hexapeptide and a fourth homeodomain helix in complex formation. <i> Piper DE, Batchelor AH, Chang CP, Cleary ML, Wolberger C. </i> Cell, 1999","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02414r002","ec_ontology":"ECO","end":206,"term_id":"IDPO:0000033","start":187,"version":3,"statement":[{"text":"The hexapeptide is joined to the HoxB1 homeodomain by a flexible linker, of which 20 amino acids (residues −17 to +3) are disordered in the ternary complex structure.","type":"Results"},{"text":"20 disordered residues in the HoxB1 linker","type":"Figure"},{"text":"This hexapeptide, whose consensus sequence is hydrophobic-Y/F -P-W-M-K/R, is joined to the N-terminal arm of the homeodomain by a linker that varies in length and sequence among different Hox proteins and between different species.","type":"Introduction"}],"term_name":"flexible linker","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10052460","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1B72"}],"term_namespace":"Disorder function","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structure of a HoxB1-Pbx1 heterodimer bound to DNA: role of the hexapeptide and a fourth homeodomain helix in complex formation. <i> Piper DE, Batchelor AH, Chang CP, Cleary ML, Wolberger C. </i> Cell, 1999","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2020_12","uniref100":"UniRef100_P14653","date":"2019-12-04T10:02:53.466Z","acc":"P14653","name":"Homeobox protein Hox-B1","length":301,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000012CF4A","genes":[{"name":{"value":"HOXB1"},"synonyms":[{"value":"HOX2I"}]}],"alphafold_very_low_content":0.36212624584717606,"disorder_content":0.0664451827242525,"disprot_consensus":{"full":[{"start":187,"end":206,"type":"D"}],"Structural state":[{"start":187,"end":206,"type":"D"}],"Disorder function":[{"start":187,"end":206,"type":"F"}]}},{"features":{"gene3D":[{"start":58,"end":268,"id":"G3DSA:1.25.40.210","name":"Telomere repeat-binding factor, dimerisation domain"}],"pfam":[{"id":"PF00249","name":"Myb-like DNA-binding domain","start":380,"end":427},{"id":"PF08558","name":"Telomere repeat binding factor (TRF)","start":77,"end":269}]},"uniref50":"UniRef50_P54274","sequence":"MAEDVSSAAPSPRGCADGRDADPTEEQMAETERNDEEQFECQELLECQVQVGAPEEEEEEEEDAGLVAEAEAVAAGWMLDFLCLSLCRAFRDGRSEDFRRTRNSAEAIIHGLSSLTACQLRTIYICQFLTRIAAGKTLDAQFENDERITPLESALMIWGSIEKEHDKLHEEIQNLIKIQAIAVCMENGNFKEAEEVFERIFGDPNSHMPFKSKLLMIISQKDTFHSFFQHFSYNHMMEKIKSYVNYVLSEKSSTFLMKAAAKVVESKRTRTITSQDKPSGNDVEMETEANLDTRKSVSDKQSAVTESSEGTVSLLRSHKNLFLSKLQHGTQQQDLNKKERRVGTPQSTKKKKESRRATESRIPVSKSQPVTPEKHRARKRQAWLWEEDKNLRSGVRKYGEGNWSKILLHYKFNNRTSVMLKDRWRTMKKLKLISSDSED","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P54274","disprot_id":"DP02415","ncbi_taxon_id":9606,"regions_counter":6,"creator":"fquaglia","regions":[{"start":1,"end":10,"reference_id":"27050267","reference_source":"pmid","reference_html":"Crystal structure of a tankyrase 1-telomere repeat factor 1 complex. <i> Li B, Qiao R, Wang Z, Zhou W, Li X, Xu W, Rao Z. </i> Acta Crystallogr F Struct Biol Commun, 2016","date":"2023-12-13T20:23:08.449Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5HKP"}],"region_id":"DP02415r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6PFX9"}],"statement":[{"text":"Although the hTRF1(1–55) fragment was used in our crystallization and the fragment remained intact in our crystallographic lattice (Supplementary Fig. S1), only hTRF1 residues 11–22 were clearly visible in the electron-density map.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-14T15:10:59.288Z"}},{"start":23,"end":55,"reference_id":"27050267","reference_source":"pmid","reference_html":"Crystal structure of a tankyrase 1-telomere repeat factor 1 complex. <i> Li B, Qiao R, Wang Z, Zhou W, Li X, Xu W, Rao Z. </i> Acta Crystallogr F Struct Biol Commun, 2016","date":"2023-12-13T20:23:14.558Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5HKP"}],"region_id":"DP02415r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6PFX9"}],"statement":[{"text":"Although the hTRF1(1–55) fragment was used in our crystallization and the fragment remained intact in our crystallographic lattice (Supplementary Fig. S1), only hTRF1 residues 11–22 were clearly visible in the electron-density map.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-14T15:11:03.149Z"}}],"released":"2021_06","uniref100":"UniRef100_P54274","date":"2019-12-04T11:11:38.930Z","acc":"P54274","name":"Telomeric repeat-binding factor 1","length":439,"organism":"Homo sapiens","dataset":["Condensates-related proteins"],"UniParc":"UPI0000001C9C","genes":[{"name":{"value":"TERF1"},"synonyms":[{"value":"PIN2"},{"value":"TRBF1"},{"value":"TRF"},{"value":"TRF1"}]}],"alphafold_very_low_content":0.32574031890660593,"disorder_content":0.0979498861047836,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"},{"start":23,"end":55,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":23,"end":55,"type":"D"}]}},{"features":{"gene3D":[{"start":31,"end":129,"id":"G3DSA:2.10.90.10","name":"Cystine-knot cytokines"}],"pfam":[{"id":"PF00341","name":"PDGF/VEGF domain","start":47,"end":124}]},"uniref50":"UniRef50_P49765","sequence":"MSPLLRRLLLAALLQLAPAQAPVSQPDAPGHQRKVVSWIDVYTRATCQPREVVVPLTVELMGTVAKQLVPSCVTVQRCGGCCPDDGLECVPTGQHQVRMQILMIRYPSSQLGEMSLEEHSQCECRPKKKDSAVKPDRAATPHHRPQPRSVPGWDSAPGAPSPADITHPTPAPGPSAHAAPSTTSALTPGPAAAAADAAASSVAKGGA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P49765","disprot_id":"DP02417","ncbi_taxon_id":9606,"regions_counter":4,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":46,"region_id":"DP02417r001","start":37,"term_id":"IDPO:0000002","statement":[{"text":"ne of the major conformational changes in VEGF-B10–108 structure is observed in the loop comprising residues 37–46 of VEGF-B10–108","type":"Discussion"},{"text":"The Cα atoms of Leu39, Met40, and Gly41 are displaced by 5.7 Å, 5.2 Å, and 5.8 Å, respectively. This loop is involved in crystal packing with the constant domain of the Fab molecule. Extensive symmetry-related interactions have stabilised the loop, which was disordered in the native structure of VEGF-B10–108","type":"Discussion"},{"text":"Despite preservation of the overall structure in the complex, conformational differences in three loop regions 37–46, 61–67, and 84–89 of the VEGF-B10–108 dimer were observed.","type":"Results"},{"text":"Here, we present the structural features of the ‘highly ordered’ interaction of the Fab fragment of this antibody (Fab-2H10) with VEGF-B.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18930733","version":2,"reference_html":"Crystal structure of vascular endothelial growth factor-B in complex with a neutralising antibody Fab fragment. <i> Leonard P, Scotney PD, Jabeen T, Iyer S, Fabri LJ, Nash AD, Acharya KR. </i> J Mol Biol, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2VWE"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":46,"region_id":"DP02417r002","start":37,"term_id":"IDPO:0000011","statement":[{"text":"ne of the major conformational changes in VEGF-B10–108 structure is observed in the loop comprising residues 37–46 of VEGF-B10–108","type":"Discussion"},{"text":"The Cα atoms of Leu39, Met40, and Gly41 are displaced by 5.7 Å, 5.2 Å, and 5.8 Å, respectively. This loop is involved in crystal packing with the constant domain of the Fab molecule. Extensive symmetry-related interactions have stabilised the loop, which was disordered in the native structure of VEGF-B10–108","type":"Discussion"},{"text":"Despite preservation of the overall structure in the complex, conformational differences in three loop regions 37–46, 61–67, and 84–89 of the VEGF-B10–108 dimer were observed.","type":"Results"},{"text":"Here, we present the structural features of the ‘highly ordered’ interaction of the Fab fragment of this antibody (Fab-2H10) with VEGF-B.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18930733","version":2,"reference_html":"Crystal structure of vascular endothelial growth factor-B in complex with a neutralising antibody Fab fragment. <i> Leonard P, Scotney PD, Jabeen T, Iyer S, Fabri LJ, Nash AD, Acharya KR. </i> J Mol Biol, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"2VWE"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP02417r003","ec_ontology":"ECO","end":46,"term_id":"GO:0005515","start":37,"version":3,"statement":[{"text":"One of the major conformational changes in VEGF-B10–108 structure is observed in the loop comprising residues 37–46 of VEGF-B10–108","type":"Discussion"},{"text":"The Cα atoms of Leu39, Met40, and Gly41 are displaced by 5.7 Å, 5.2 Å, and 5.8 Å, respectively. This loop is involved in crystal packing with the constant domain of the Fab molecule. Extensive symmetry-related interactions have stabilised the loop, which was disordered in the native structure of VEGF-B10–108","type":"Discussion"},{"text":"Despite preservation of the overall structure in the complex, conformational differences in three loop regions 37–46, 61–67, and 84–89 of the VEGF-B10–108 dimer were observed.","type":"Results"},{"text":"Here, we present the structural features of the ‘highly ordered’ interaction of the Fab fragment of this antibody (Fab-2H10) with VEGF-B.","type":"Abstract"}],"interaction_partner":[{"partner_start":null,"db":"ABCD","id":"ABCD_AG653","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18930733","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2VWE"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"fquaglia","reference_html":"Crystal structure of vascular endothelial growth factor-B in complex with a neutralising antibody Fab fragment. <i> Leonard P, Scotney PD, Jabeen T, Iyer S, Fabri LJ, Nash AD, Acharya KR. </i> J Mol Biol, 2008","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":188,"region_id":"DP02417r004","start":130,"term_id":"IDPO:0000002","statement":[{"text":"The electron density for the first N-terminal residue and the last C-terminal residue could not be observed for both monomers of VEGF-B10–108. Both chains consist of residues 11–107.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18930733","version":2,"reference_html":"Crystal structure of vascular endothelial growth factor-B in complex with a neutralising antibody Fab fragment. <i> Leonard P, Scotney PD, Jabeen T, Iyer S, Fabri LJ, Nash AD, Acharya KR. </i> J Mol Biol, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2VWE"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","uniref100":"UniRef100_P49765","date":"2019-12-04T13:48:07.740Z","acc":"P49765","name":"Vascular endothelial growth factor B","length":207,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000002B6B4","genes":[{"name":{"value":"VEGFB"},"synonyms":[{"value":"VRF"}]}],"alphafold_very_low_content":0.14009661835748793,"disorder_content":0.3333333333333333,"disprot_consensus":{"full":[{"start":37,"end":46,"type":"T"},{"start":130,"end":188,"type":"D"}],"Structural state":[{"start":37,"end":46,"type":"D"},{"start":130,"end":188,"type":"D"}],"Structural transition":[{"start":37,"end":46,"type":"T"}],"Molecular function":[{"start":37,"end":46,"type":"F"}]}},{"features":{"gene3D":[{"start":159,"end":267,"id":"G3DSA:2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":159,"end":267,"id":"G3DSA:2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"}],"pfam":[{"id":"PF00169","name":"PH domain","start":21,"end":112},{"id":"PF02174","name":"PTB domain (IRS-1 type)","start":167,"end":260}]},"uniref50":"UniRef50_P35568","sequence":"MASPPESDGFSDVRKVGYLRKPKSMHKRFFVLRAASEAGGPARLEYYENEKKWRHKSSAPKRSIPLESCFNINKRADSKNKHLVALYTRDEHFAIAADSEAEQDSWYQALLQLHNRAKGHHDGAAALGAGGGGGSCSGSSGLGEAGEDLSYGDVPPGPAFKEVWQVILKPKGLGQTKNLIGIYRLCLTSKTISFVKLNSEAAAVVLQLMNIRRCGHSENFFFIEVGRSAVTGPGEFWMQVDDSVVAQNMHETILEAMRAMSDEFRPRSKSQSSSNCSNPISVPLRRHHLNNPPPSQVGLTRRSRTESITATSPASMVGGKPGSFRVRASSDGEGTMSRPASVDGSPVSPSTNRTHAHRHRGSARLHPPLNHSRSIPMPASRCSPSATSPVSLSSSSTSGHGSTSDCLFPRRSSASVSGSPSDGGFISSDEYGSSPCDFRSSFRSVTPDSLGHTPPARGEEELSNYICMGGKGPSTLTAPNGHYILSRGGNGHRCTPGTGLGTSPALAGDEAASAADLDNRFRKRTHSAGTSPTITHQKTPSQSSVASIEEYTEMMPAYPPGGGSGGRLPGHRHSAFVPTRSYPEEGLEMHPLERRGGHHRPDSSTLHTDDGYMPMSPGVAPVPSGRKGSGDYMPMSPKSVSAPQQIINPIRRHPQRVDPNGYMMMSPSGGCSPDIGGGPSSSSSSSNAVPSGTSYGKLWTNGVGGHHSHVLPHPKPPVESSGGKLLPCTGDYMNMSPVGDSNTSSPSDCYYGPEDPQHKPVLSYYSLPRSFKHTQRPGEPEEGARHQHLRLSTSSGRLLYAATADDSSSSTSSDSLGGGYCGARLEPSLPHPHHQVLQPHLPRKVDTAAQTNSRLARPTRLSLGDPKASTLPRAREQQQQQQPLLHPPEPKSPGEYVNIEFGSDQSGYLSGPVAFHSSPSVRCPSQLQPAPREEETGTEEYMKMDLGPGRRAAWQESTGVEMGRLGPAPPGAASICRPTRAVPSSRGDYMTMQMSCPRQSYVDTSPAAPVSYADMRTGIAAEEVSLPRATMAAASSSSAASASPTGPQGAAELAAHSSLLGGPQGPGGMSAFTRVNLSPNRNQSAKVIRADPQGCRRRHSSETFSSTPSATRVGNTVPFGAGAAVGGGGGSSSSSEDVKRHSSASFENVWLRPGELGGAPKEPAKLCGAAGGLENGLNYIDLDLVKDFKQCPQECTPEPQPPPPPPPHQPLGSGESSSTRRSSEDLSAYASISFQKQPEDRQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P35568","disprot_id":"DP02418","ncbi_taxon_id":9606,"regions_counter":2,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":159,"region_id":"DP02418r001","start":117,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Residues 117–159 corresponding to the interdomain linker are disordered","type":"Methods"},{"text":"No electron density is observed for the interdomain linker region (residues 117–159). Considering the linker composition, this is not surprising; 26 (60%) of the 43 residues are glycine, alanine, and serine. Unlike the PH and PTB domains, whose sequences are well conserved, interdomain linkers of the four IRS proteins vary greatly in length, from 28 to 51 residues, and composition, suggesting that this region of each IRS protein serves similarly as a flexible tether between PH and PTB domains.","type":"Results"},{"text":"Because the linker is disordered, it is not possible to unequivocally establish covalent connections between domains","type":"Results"},{"text":"The final model includes all residues of the PH (12–116) and PTB (160–264) domains and 90 solvent molecules. Residues 117–159 corresponding to the interdomain linker are disordered.","type":"Methods"},{"text":"The nonconserved 46-residue linker between the domains is disordered","type":"Abstract"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10411883","version":2,"reference_html":"Crystal structure of the pleckstrin homology-phosphotyrosine binding (PH-PTB) targeting region of insulin receptor substrate 1. <i> Dhe-Paganon S, Ottinger EA, Nolte RT, Eck MJ, Shoelson SE. </i> Proc Natl Acad Sci U S A, 1999","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1QQG"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":159,"region_id":"DP02418r002","start":117,"term_id":"IDPO:0000033","unpublished":true,"statement":[{"text":"Residues 117–159 corresponding to the interdomain linker are disordered","type":"Methods"},{"text":"No electron density is observed for the interdomain linker region (residues 117–159). Considering the linker composition, this is not surprising; 26 (60%) of the 43 residues are glycine, alanine, and serine. Unlike the PH and PTB domains, whose sequences are well conserved, interdomain linkers of the four IRS proteins vary greatly in length, from 28 to 51 residues, and composition, suggesting that this region of each IRS protein serves similarly as a flexible tether between PH and PTB domains.","type":"Results"},{"text":"Because the linker is disordered, it is not possible to unequivocally establish covalent connections between domains","type":"Results"},{"text":"The final model includes all residues of the PH (12–116) and PTB (160–264) domains and 90 solvent molecules. Residues 117–159 corresponding to the interdomain linker are disordered.","type":"Methods"},{"text":"The nonconserved 46-residue linker between the domains is disordered","type":"Abstract"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10411883","version":3,"reference_html":"Crystal structure of the pleckstrin homology-phosphotyrosine binding (PH-PTB) targeting region of insulin receptor substrate 1. <i> Dhe-Paganon S, Ottinger EA, Nolte RT, Eck MJ, Shoelson SE. </i> Proc Natl Acad Sci U S A, 1999","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1QQG"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2023_12","uniref100":"UniRef100_P35568","date":"2019-12-04T14:50:04.407Z","acc":"P35568","name":"Insulin receptor substrate 1","length":1242,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000003BB52","genes":[{"name":{"value":"IRS1"}}],"alphafold_very_low_content":0.7818035426731079,"disorder_content":0.03462157809983897,"disprot_consensus":{"full":[{"start":117,"end":159,"type":"D"}],"Structural state":[{"start":117,"end":159,"type":"D"}],"Disorder function":[{"start":117,"end":159,"type":"F"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF05301","name":"GNAT acetyltransferase, Mec-17","start":3,"end":196}]},"uniref50":"UniRef50_Q5SQI0","sequence":"MEFPFDVDALFPERITVLDQHLRPPARRPGTTTPARVDLQQQIMTIIDELGKASAKAQNLSAPITSASRMQSNRHVVYILKDSSARPAGKGAIIGFIKVGYKKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQYMLQKERVEPHQLAIDRPSQKLLKFLNKHYNLETTVPQVNNFVIFEGFFAHQHRPPAPSLRATRHSRAAAVDPTPAAPARKLPPKRAEGDIKPYSSSDREFLKVAVEPPWPLNRAPRRATPPAHPPPRSSSLGNSPERGPLRPFVPEQELLRSLRLCPPHPTARLLLAADPGGSPAQRRRTRGTPPGLVAQSCCYSRHGGVNSSSPNTGNQDSKQGEQETKNRSASEEQALSQDGSGEKPMHTAPPQAPAPPAQSWTVGGDILNARFIRNLQERRSTRPW","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q5SQI0","disprot_id":"DP02419","ncbi_taxon_id":9606,"regions_counter":3,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":36,"region_id":"DP02419r001","start":26,"term_id":"IDPO:0000002","statement":[{"text":"The refined αTAT1/AcCoA structure reveals continuous electron density from amino acid 3 to 195, except for two short unresolved loops (residues 26–36 and 84–91)","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23071314","version":2,"reference_html":"Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylation. <i> Friedmann DR, Aguilar A, Fan J, Nachury MV, Marmorstein R. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4GS4"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":236,"region_id":"DP02419r002","start":196,"term_id":"IDPO:0000002","statement":[{"text":"The refined αTAT1/AcCoA structure reveals continuous electron density from amino acid 3 to 195, except for two short unresolved loops (residues 26–36 and 84–91)","type":"Results"},{"text":"An expression construct encoding residues 2–236 of human αTAT1 was shown to retain almost 100% of microtubule acetyltransferase activity relative to the full-length protein, and secondary structure prediction algorithms suggested that the C terminus of the protein, residues ∼230–333, were disordered","type":"Results"},{"text":"Although the expression construct used for crystallization contained ∼40 residues C-terminal to the last resolved residue, and confirmed by mass spectrometry to be present in the crystals, this portion of the protein was not observed in the electron density map","type":"Results"},{"text":"Based on this result, we conclude that residues 196–236 are disordered in the crystals.","type":"Results"},{"text":"We found it interesting that residues 196–236 of αTAT1 were disordered in the crystal structure because K233 was reported to be acetylated, suggesting that K233 acetylation does not play a regulatory role for catalysis","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23071314","version":2,"reference_html":"Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylation. <i> Friedmann DR, Aguilar A, Fan J, Nachury MV, Marmorstein R. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4GS4"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":235,"region_id":"DP02419r003","start":231,"term_id":"IDPO:0000039","statement":[{"text":"An expression construct encoding residues 2–236 of human αTAT1 was shown to retain almost 100% of microtubule acetyltransferase activity relative to the full-length protein, and secondary structure prediction algorithms suggested that the C terminus of the protein, residues ∼230–333, were disordered","type":"Results"},{"text":"We found it interesting that residues 196–236 of αTAT1 were disordered in the crystal structure because K233 was reported to be acetylated, suggesting that K233 acetylation does not play a regulatory role for catalysis, similar to autoacetylation sites in the Rtt109 and MYST histone acetyltransferases (HATs) that are highly ordered in the corresponding crystal structures (15, 21).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"enzymatic activity assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23071314","version":2,"reference_html":"Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylation. <i> Friedmann DR, Aguilar A, Fan J, Nachury MV, Marmorstein R. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005801","cross_refs":[{"db":"PDB","id":"4GS4"}],"term_name":"acetylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Disorder function"}],"released":"2021_06","uniref100":"UniRef100_Q5SQI0","date":"2019-12-04T15:45:11.063Z","acc":"Q5SQI0","name":"Alpha-tubulin N-acetyltransferase 1","length":421,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000014137B","genes":[{"name":{"value":"ATAT1","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03130","url":"https://hamap.expasy.org/unirule/MF_03130"}}]},"synonyms":[{"value":"C6orf134"},{"value":"MEC17","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03130","url":"https://hamap.expasy.org/unirule/MF_03130"}}]}],"orfNames":[{"value":"Nbla00487"}]}],"alphafold_very_low_content":0.3586698337292161,"disorder_content":0.12351543942992874,"disprot_consensus":{"full":[{"start":26,"end":36,"type":"D"},{"start":196,"end":236,"type":"D"}],"Structural state":[{"start":26,"end":36,"type":"D"},{"start":196,"end":236,"type":"D"}],"Disorder function":[{"start":231,"end":235,"type":"F"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":1087,"end":1154}]},"uniref50":"UniRef50_D3ZMK9","sequence":"MHQTLCLNPESLKMSACSDFVEHIWKPGSCKNCFCLRSDHQLVAGPPQPRAGSLPPPPRLPPRPENCRLEDEGVNSSPYSKPTIAVKPTMMSSEASDVWTEANLSAEVSQVIWRRAPGKLPLPKQEDAPVVYLGSFRGVQKPAGPSTSPDGNSRCPPAYTMVGLHNLEPRGERNIAFHPVSFPEEKAVHKEKPSFPYQDRPSTQESFRQKLAAFAGTTSGCHQGPGPLRESLPSEDDSDQRCSPSGDSEGGEYCSILDCCPGSPVAKAASQTAGSRGRHGGRDCSPTCWEQGKCSGPAEQEKRGPSFPKECCSQGPTAHPSCLGPKKLSLTSEAAISSDGLSCGSGSGSGSGASSPFVPHLESDYCSLMKEPAPEKQQDPGCPGVTPSRCLGLTGEPQPPAHPREATQPEPIYAESTKRKKAAPVPSKSQAKIEHAAAAQGQGQVCTGNAWAQKAASGWGRDSPDPTPQVSATITVMAAHPEEDHRTIYLSSPDSAVGVQWPRGPVSQNSEVGEEETSAGQGLSSRESHAHSASESKPKERPAIPPKLSKSSPVGSPVSPSAGGPPVSPLADLSDGSSGGSSIGPQPPSQGPADPAPSCRTNGVAISDPSRCPQPAASSASEQRRPRFQAGTWSRQCRIEEEEEVEQELLSHSWGRETKNGPTDHSNSTTWHRLHPTDGSSGQNSKVGTGMSKSASFAFEFPKDRSGIETFSPPPPPPKSRHLLKMNKSSSDLEKVSQGSAESLSPSFRGVHVSFTTGSTDSLASDSRTCSDGGPSSELAHSPTNSGKKLFAPVPFPSGSTEDVSPSGPQQPPPLPQKKIVSRAASSPDGFFWTQGSPKPGTASPKLNLSHSETNVHDESHFSYSLSPGNRHHPVFSSSDPLEKAFKGSGHWLPAAGLAGNRGGCGSPGLQCKGAPSASSSQLSVSSQASTGSTQLQLHGLLSNISSKEGTYAKLGGLYTQSLARLVAKCEDLFMGGQKKELHFNENNWSLFKLTCNKPCCDSGDAIYYCATCSEDPGSTYAVKICKAPEPKTVSYCSPSVPVHFNIQQDCGHFVASVPSSMLSSPDAPKDPVPALPTHPPAQEQDCVVVITREVPHQTASDFVRDSAASHQAEPEAYERRVCFLLLQLCNGLEHLKEHGIIHRDLCLENLLLVHCTLQAGPGPAPAPAPAPAPAAAAPPCSSAAPPAGGTLSPAAGPASPEGPREKQLPRLIISNFLKAKQKPGGTPNLQQKKSQARLAPEIVSASQYRKFDEFQTGILIYELLHQPNPFEVRAQLRERDYRQEDLPPLPALSLYSPGLQQLAHLLLEADPIKRIRIGEAKRVLQCLLWGPRRELVQQPGTSEEALCGTLHNWIDMKRALMMMKFAEKAVDRRRGVELEDWLCCQYLASAEPGALLQSLKLLQLL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q86YV5","disprot_id":"DP02420","ncbi_taxon_id":9606,"regions_counter":5,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":943,"region_id":"DP02420r001","start":932,"term_id":"IDPO:0000002","statement":[{"text":"The majority of the residues were visible in the structure with the exception of residues present in surface exposed loops: 932–943, 977–983, 1030–1039, 1065–1081, 1159–1207, 1218–1238 and 1336–1345.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29079850","version":2,"reference_html":"Structure of SgK223 pseudokinase reveals novel mechanisms of homotypic and heterotypic association. <i> Patel O, Griffin MDW, Panjikar S, Dai W, Ma X, Chan H, Zheng C, Kropp A, Murphy JM, Daly RJ, Lucet IS. </i> Nat Commun, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5VE6"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1039,"region_id":"DP02420r002","start":1030,"term_id":"IDPO:0000002","statement":[{"text":"The majority of the residues were visible in the structure with the exception of residues present in surface exposed loops: 932–943, 977–983, 1030–1039, 1065–1081, 1159–1207, 1218–1238 and 1336–1345.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29079850","version":2,"reference_html":"Structure of SgK223 pseudokinase reveals novel mechanisms of homotypic and heterotypic association. <i> Patel O, Griffin MDW, Panjikar S, Dai W, Ma X, Chan H, Zheng C, Kropp A, Murphy JM, Daly RJ, Lucet IS. </i> Nat Commun, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5VE6"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1081,"region_id":"DP02420r003","start":1065,"term_id":"IDPO:0000002","statement":[{"text":"The majority of the residues were visible in the structure with the exception of residues present in surface exposed loops: 932–943, 977–983, 1030–1039, 1065–1081, 1159–1207, 1218–1238 and 1336–1345.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29079850","version":2,"reference_html":"Structure of SgK223 pseudokinase reveals novel mechanisms of homotypic and heterotypic association. <i> Patel O, Griffin MDW, Panjikar S, Dai W, Ma X, Chan H, Zheng C, Kropp A, Murphy JM, Daly RJ, Lucet IS. </i> Nat Commun, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5VE6"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1238,"region_id":"DP02420r004","start":1218,"term_id":"IDPO:0000002","statement":[{"text":"The majority of the residues were visible in the structure with the exception of residues present in surface exposed loops: 932–943, 977–983, 1030–1039, 1065–1081, 1159–1207, 1218–1238 and 1336–1345.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29079850","version":2,"reference_html":"Structure of SgK223 pseudokinase reveals novel mechanisms of homotypic and heterotypic association. <i> Patel O, Griffin MDW, Panjikar S, Dai W, Ma X, Chan H, Zheng C, Kropp A, Murphy JM, Daly RJ, Lucet IS. </i> Nat Commun, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5VE6"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1345,"region_id":"DP02420r005","start":1336,"term_id":"IDPO:0000002","statement":[{"text":"The majority of the residues were visible in the structure with the exception of residues present in surface exposed loops: 932–943, 977–983, 1030–1039, 1065–1081, 1159–1207, 1218–1238 and 1336–1345.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29079850","version":2,"reference_html":"Structure of SgK223 pseudokinase reveals novel mechanisms of homotypic and heterotypic association. <i> Patel O, Griffin MDW, Panjikar S, Dai W, Ma X, Chan H, Zheng C, Kropp A, Murphy JM, Daly RJ, Lucet IS. </i> Nat Commun, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5VE6"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","uniref100":"UniRef100_Q86YV5","date":"2019-12-04T16:12:29.334Z","acc":"Q86YV5","name":"Inactive tyrosine-protein kinase PRAG1","length":1406,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI0003EAF98F","genes":[{"name":{"value":"PRAG1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:25438","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:25438"}}]},"synonyms":[{"value":"SGK223"}]}],"alphafold_very_low_content":0.6941678520625889,"disorder_content":0.049786628733997154,"disprot_consensus":{"full":[{"start":932,"end":943,"type":"D"},{"start":1030,"end":1039,"type":"D"},{"start":1065,"end":1081,"type":"D"},{"start":1218,"end":1238,"type":"D"},{"start":1336,"end":1345,"type":"D"}],"Structural state":[{"start":932,"end":943,"type":"D"},{"start":1030,"end":1039,"type":"D"},{"start":1065,"end":1081,"type":"D"},{"start":1218,"end":1238,"type":"D"},{"start":1336,"end":1345,"type":"D"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF21487","name":"Tas3, C-terminal helical domains","start":494,"end":542},{"id":"PF22378","name":"Tas3-like, N-terminal domain","start":10,"end":81}]},"uniref50":"UniRef50_O94687","sequence":"MEKGIKKYLPSLPFLACISDFPENHGTSRRSATVSLERVHELFTEHWLSNLKNRREKRQELAEEAVYCRSEMLSQRKLLAAVDFPQQLKNSPAKAKATHTSSGVTKEVRASKKYTSSNVEFPLVTDGKEKPVKSKQLRKNSVTEFEKPIETKKSKHRKSRNKFLDKSSGSMEIESWDNSTSDSIIESSSRLHESISLRENDIRSSDSKSVGWDDNSTGFRESSKSLDHTDTSMFMELDSNSDPQFRPKYQAKSSWFAPDDPEASWGNLDDGWGETNGSWSSTDDTKHYKNEWAESINLDNFNRPSQQEDYDKPKNTQVSRSSNHHRRYDSYHPDSRSDSYRSKREHYDNRDTGPRSKHLEKSSYVYNQNFEDRTHLSDHGAHFHLGNANDFNMQGSSRKRKASDRQRESRENELPTKKLNASDSHNPLASLTTDKNDLYINWLKSLSFFQTNSSCAEALVKVIPHYHNKLIDFSQVLQLVFSASEKFPIQENQPLPEQLMFLSNLEKQTPFAKAVGSSIYKLVTGKNLSLDFASQILKEASILEHKNEK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"uniref90":"UniRef90_O94687","disprot_id":"DP02421","ncbi_taxon_id":284812,"regions_counter":2,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":436,"region_id":"DP02421r001","start":426,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Secondary structure alignment of the TAM-containing Te1 construct (426−545) used for the crystallographic study. Dotted line denotes the unmodeled parts of Te1 in the solved crystal structure due to their high flexibility.","type":"Figure"},{"text":"In the solved structures from both crystal forms, approximately eight to ten residues from the N terminus and one residue from the C terminus were not modeled due to high flexibility and lack of sufficient density.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19394293","version":2,"reference_html":"An alpha motif at Tas3 C terminus mediates RITS cis spreading and promotes heterochromatic gene silencing. <i> Li H, Motamedi MR, Yip CK, Wang Z, Walz T, Patel DJ, Moazed D. </i> Mol Cell, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3D1B"},{"db":"PDB","id":"3D1D"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-09T18:07:55.957Z"}},{"start":117,"end":452,"reference_id":"28608349","reference_source":"pmid","reference_html":"Identification and Evolutionary Characterization of ARGONAUTE-Binding Platforms. <i> Trujillo JT, Mosher RA. </i> Methods Mol Biol, 2017","date":"2022-11-09T18:19:03.796Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006216","ec_ontology":"ECO","ec_name":"author inference used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02421r002","statement":[{"text":"Although ARGONAUTE-interacting proteins might possess well-conserved and highly structured domains, such as the polymerase domains in NRPE1, AGO-binding platforms generally have poor sequence conservation between species and are intrinsically disordered [2, 6, 9,10,11,12].","type":"Introduction"},{"text":"The repetitive sequence units tend to contain at least one AGO hook and are enriched in disorder-promoting amino acids that contribute to the intrinsic disorder of the region [12].","type":"Introduction"},{"text":"The argonaute hook domain comprises the 117-452 protein region according to Pfam (PF10427).","type":"Curator statement"}]}],"released":"2023_12","uniref100":"UniRef100_O94687","date":"2019-12-04T16:29:33.096Z","acc":"O94687","name":"RNA-induced transcriptional silencing complex protein tas3","length":549,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","dataset":[],"UniParc":"UPI000006B698","genes":[{"name":{"value":"tas3"},"orfNames":[{"value":"SPBC83.03c"}]}],"alphafold_very_low_content":0.6429872495446266,"disorder_content":0.6120218579234973,"disprot_consensus":{"full":[{"start":117,"end":452,"type":"D"}],"Structural state":[{"start":117,"end":452,"type":"D"}]}},{"features":{"gene3D":[{"start":1,"end":210,"id":"G3DSA:2.30.42.10","name":"G3DSA:2.30.42.10"}],"pfam":[{"id":"PF04495","name":"GRASP55/65 PDZ-like domain","start":68,"end":203}]},"uniref50":"UniRef50_Q9BQQ3","sequence":"MGLGASSEQPAGGEGFHLHGVQENSPAQQAGLEPYFDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVFNMKTMRVREVEVVPSNMWGGQGLLGASVRFCSFRRASEHVWHVLDVEPSSPAALAGLRPYTDYIVGSDQILQESEDFFTLIESHEGKPLKLMVYNSESDSCREVTVTPNAAWGGEGSLGCGIGYGYLHRIPTQPSSQYKKPPSASSPGTPAKTPQPNAFPLGAPPPWPIPQDSSGPELGSRQSDYMEALPQVPGGFMEEQLPGPGSPGHGTADYGGCLHSMEIPLQPPPPVQRVMDPGFLDVSGMSLLDSNNTSVCPSLSSSSLLTPTAVSALGPEDIGSSSSSHERGGEATWSGSEFEISFPDSPGSQAQVDHLPRLTLPDGLTSAASPEEGLSAELLEAQTEEPAHTASLDCMAQTEGPAGQVQAAPDPEPGLCEGPW","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_O35254","disprot_id":"DP02422","ncbi_taxon_id":10116,"regions_counter":1,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":11,"region_id":"DP02422r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"Crystals of GRASP65 were obtained ~1 month after the crystallization setup. A 2.2-Å dataset was collected, and the structure was determined by molecular replacement (Table 1), but only residues 12–210 were visible in the electron density.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23940043","version":2,"reference_html":"Structural insight into Golgi membrane stacking by GRASP65 and GRASP55 proteins. <i> Feng Y, Yu W, Li X, Lin S, Zhou Y, Hu J, Liu X. </i> J Biol Chem, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4KFV"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","uniref100":"UniRef100_O35254","date":"2019-12-04T16:51:23.294Z","acc":"O35254","name":"Golgi reassembly-stacking protein 1","length":451,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI00000E6C57","genes":[{"name":{"value":"Gorasp1"},"synonyms":[{"value":"Grasp65","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9346242","url":"http://www.ncbi.nlm.nih.gov/pubmed/9346242","alternativeUrl":"https://europepmc.org/abstract/MED/9346242"}}]}]}],"alphafold_very_low_content":0.5210643015521065,"disorder_content":0.024390243902439025,"disprot_consensus":{"full":[{"start":1,"end":11,"type":"D"}],"Structural state":[{"start":1,"end":11,"type":"D"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":34,"end":284},{"id":"PF21115","name":"BRSK1/2 UBA domain","start":316,"end":358},{"id":"PF21122","name":"BRSK1/2 KA1 domain","start":597,"end":715}]},"uniref50":"UniRef50_Q5RJI5","sequence":"MSSGSKEGGGGSPAYHLPHPHPHPPQHAQYVGPYRLEKTLGKGQTGLVKLGVHCITGQKVAVKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIVSALDFCHSYSICHRDLKPENLLLDEKNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIKGEKYDGRRADMWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVEPEKRLSLEQIQKHPWYLGGKHEPDPCLEPAPGRRVAMRSLPSNGELDPDVLESMASLGCFRDRERLHRELRSEEENQEKMIYYLLLDRKERYPSCEDQDLPPRNDVDPPRKRVDSPMLSRHGKRRPERKSMEVLSITDAGSGGSPVPTRRALEMAQHSQRSRSVSGASTGLSSSPLSSPRSPVFSFSPEPGAGDEARGGGSPTSKTQTLPSRGPRGGGAGEQPPPPSARSTPLPGPPGSPRSSGGTPLHSPLHTPRASPTGTPGTTPPPSPGGGVGGAAWRSRLNSIRNSFLGSPRFHRRKMQVPTAEEMSSLTPESSPELAKRSWFGNFISLDKEEQIFLVLKDKPLSSIKADIVHAFLSIPSLSHSVLSQTSFRAEYKASGGPSVFQKPVRFQVDISSSEGPEPSPRRDGSSGGGIYSVTFTLISGPSRRFKRVVETIQAQLLSTHDQPSVQALADEKNGAQTRPAGTPPRSLQPPPGRSDPDLSSSPRRGPPKDKKLLATNGTPLP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q5RJI5","disprot_id":"DP02423","ncbi_taxon_id":10090,"regions_counter":3,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":603,"region_id":"DP02423r001","start":592,"term_id":"IDPO:0000002","statement":[{"text":"the isolated AIS sequence is highly flexible and solvent-accessible","type":"Abstract"},{"text":"Here, we report the crystal structure of the mouse SAD-B C-terminal fragment including the AIS and the kinase-associated domain 1 (KA1) at 2.8 Å resolution. The KA1 domain is structurally conserved, while the isolated AIS sequence is highly flexible and solvent-accessible. Our biochemical studies indicated that the SAD-B AIS exerts the same autoinhibitory role as that in SAD-A. We believe that the flexible isolated AIS sequence is readily available for interaction with KD-UBA and thus inhibits SAD-B activity.","type":"Abstract"},{"text":"the free AIS sequence in SAD-B is highly flexible, accessible to the KD-UBA interaction.","type":"Article"},{"text":"our results revealed the flexible shift of AIS between the free state and the inhibitory state, implicating its regulatory role for controlling the kinase activity.","type":"Article"},{"text":"the AIS sequence is largely flexible in isolated the AIS-KA1 fragment and readily available to interact with the KD-UBA domain, thereby inhibiting the SAD activity.","type":"Results"},{"text":"The structural analyses indicated that the isolated AIS sequence is largely flexible and solvent accessible, and that AIS in the AIS-KA1 fragment is readily available for binding to the KD-UBA junction and inhibiting the SAD activity.","type":"Results"},{"text":"Taken together, the AIS sequence of SAD-B is flexible in the isolated state and characterized by the autoinhibitory role.","type":"Results"},{"text":"Our recent study of mouse SAD-A identified a unique autoinhibitory sequence (AIS), which binds at the junction of the kinase domain (KD) and the ubiquitin-associated (UBA) domain and exerts autoregulation in cooperation with UBA.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27251228","version":2,"reference_html":"Structure and inhibition analysis of the mouse SAD-B C-terminal fragment. <i> Ma H, Wu JX, Wang J, Wang ZX, Wu JW. </i> Biosci Biotechnol Biochem, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5IRI"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":603,"region_id":"DP02423r002","start":592,"term_id":"IDPO:0000059","statement":[{"text":"the isolated AIS sequence is highly flexible and solvent-accessible","type":"Abstract"},{"text":"Here, we report the crystal structure of the mouse SAD-B C-terminal fragment including the AIS and the kinase-associated domain 1 (KA1) at 2.8 Å resolution. The KA1 domain is structurally conserved, while the isolated AIS sequence is highly flexible and solvent-accessible. Our biochemical studies indicated that the SAD-B AIS exerts the same autoinhibitory role as that in SAD-A. We believe that the flexible isolated AIS sequence is readily available for interaction with KD-UBA and thus inhibits SAD-B activity.","type":"Abstract"},{"text":"the free AIS sequence in SAD-B is highly flexible, accessible to the KD-UBA interaction.","type":"Article"},{"text":"our results revealed the flexible shift of AIS between the free state and the inhibitory state, implicating its regulatory role for controlling the kinase activity.","type":"Article"},{"text":"the AIS sequence is largely flexible in isolated the AIS-KA1 fragment and readily available to interact with the KD-UBA domain, thereby inhibiting the SAD activity.","type":"Results"},{"text":"The structural analyses indicated that the isolated AIS sequence is largely flexible and solvent accessible, and that AIS in the AIS-KA1 fragment is readily available for binding to the KD-UBA junction and inhibiting the SAD activity.","type":"Results"},{"text":"Taken together, the AIS sequence of SAD-B is flexible in the isolated state and characterized by the autoinhibitory role.","type":"Results"},{"text":"Our recent study of mouse SAD-A identified a unique autoinhibitory sequence (AIS), which binds at the junction of the kinase domain (KD) and the ubiquitin-associated (UBA) domain and exerts autoregulation in cooperation with UBA.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27251228","version":3,"reference_html":"Structure and inhibition analysis of the mouse SAD-B C-terminal fragment. <i> Ma H, Wu JX, Wang J, Wang ZX, Wu JW. </i> Biosci Biotechnol Biochem, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5IRI"}],"term_name":"self-inhibition","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":603,"region_id":"DP02423r003","start":592,"term_id":"GO:0140678","statement":[{"text":"Here, we report the crystal structure of the mouse SAD-B C-terminal fragment including the AIS and the kinase-associated domain 1 (KA1) at 2.8 Å resolution. The KA1 domain is structurally conserved, while the isolated AIS sequence is highly flexible and solvent-accessible. Our biochemical studies indicated that the SAD-B AIS exerts the same autoinhibitory role as that in SAD-A. We believe that the flexible isolated AIS sequence is readily available for interaction with KD-UBA and thus inhibits SAD-B activity.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"27251228","version":3,"reference_html":"Structure and inhibition analysis of the mouse SAD-B C-terminal fragment. <i> Ma H, Wu JX, Wang J, Wang ZX, Wu JW. </i> Biosci Biotechnol Biochem, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5IRI"}],"term_name":"molecular function inhibitor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","uniref100":"UniRef100_Q5RJI5","date":"2019-12-04T17:13:30.929Z","acc":"Q5RJI5","name":"Serine/threonine-protein kinase BRSK1","length":778,"organism":"Mus musculus","dataset":[],"UniParc":"UPI0000470E43","genes":[{"name":{"value":"Brsk1"},"synonyms":[{"value":"Gm1100"},{"value":"Sadb"}]}],"alphafold_very_low_content":0.41773778920308485,"disorder_content":0.015424164524421594,"disprot_consensus":{"full":[{"start":592,"end":603,"type":"D"}],"Structural state":[{"start":592,"end":603,"type":"D"}],"Disorder function":[{"start":592,"end":603,"type":"F"}],"Molecular function":[{"start":592,"end":603,"type":"F"}]}},{"features":{"gene3D":[{"start":819,"end":917,"id":"G3DSA:2.30.42.10","name":"G3DSA:2.30.42.10"},{"start":819,"end":917,"id":"G3DSA:2.30.42.10","name":"G3DSA:2.30.42.10"},{"start":819,"end":917,"id":"G3DSA:2.30.42.10","name":"G3DSA:2.30.42.10"}],"pfam":[{"id":"PF00595","name":"PDZ domain","start":143,"end":216},{"id":"PF00595","name":"PDZ domain","start":288,"end":357},{"id":"PF00595","name":"PDZ domain","start":831,"end":898}]},"uniref50":"UniRef50_Q80VW5","sequence":"MNAQLDGLSVSSSSTGSLGSAAAAAGGGGGAGLRLLSANVRQLHQALTALLSEPEREQFTHCLNAYHARRNVFDLVRTLRVLLDSPVKRRLLPMLRLVIPRSDQLLFDQYTAEGLYLPATTPYRQPAWAAPDGAGPGEVRLVSLRRAKAHEGLGFSIRGGSEHGVGIYVSLVEPGSLAEKEGLRVGDQILRVNDKSLARVTHAEAVKALKGSKKLVLSVYSAGRIPGGYVTNHIYTWVDPQGRSTSPPSSLPQPHGSTLRQREDDRRSTLHLLQSGDEKKVNLVLGDGRSLGLTIRGGAEYGLGIYITGVDPGSEAESSGLKVGDQILEVNGRSFLNILHDEAVKLLKSSRHLILTVKDVGRLPHARTTVDQTKWIASSRIGESVANSAGFPGDHTEEGTSKPGFYKGPAGSQVTLSSLGNQTRALLDDQARHLLTEQERATMMYYLAQYRGGTISVEAMVMALFELLNTHAKFSLLSEVRSIISPQDLDRFDHLVLRREIESMKARQPPGPGVGDTYSMVSYSDTGSSTGSHGTSTTVSSARERLLWLIDLMENTLDLEGTGETTQGSTNALPDVSVDDVKSPSEDLPGIKPPPPPPPLAQGHDRLLGQPRKPGREDPAPLSSAAHSGIVFSAPRNRSPPPGTAPTPGPSSAQDSPSSPIYASISHANPSSRKPLDTHLALVNQHPIGPFPRVQSPPHLKSPPAETPGAGACLPPPSPSEHPDAVGANQHFVLVEVHRPDSEPDVNEVRALPQTRTASTLSQLSDSGQTLSEDSGVDAGETEASTSGRGRQTASAKNKNGKEQPRTERTAEGANKPPGLLEPTSTLVRVRKSAATLGIAIEGGANTRQPLPRIVTIQRGGSAHNCGQLKVGHVILEVNGQTLRGKEHKEAARIIAEAFKTKERDYIDFLVTEFNVML","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref90":"UniRef90_Q80VW5","disprot_id":"DP02426","ncbi_taxon_id":10090,"regions_counter":1,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":430,"region_id":"DP02426r001","start":420,"term_id":"IDPO:0000002","statement":[{"text":"However, the first 12 N‐terminal residues are not visible in the electron density of the dimer, indicating increased disorder or conformational heterogeneity of helix α1 compared to the five‐helix structure.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30053338","version":2,"reference_html":"Structural plasticity of the HHD2 domain of whirlin. <i> Delhommel F, Cordier F, Saul F, Chataigner L, Haouz A, Wolff N. </i> FEBS J, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6FDE"},{"db":"PDB","id":"6FDD"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","uniref100":"UniRef100_Q80VW5","date":"2019-12-05T11:24:58.266Z","acc":"Q80VW5","name":"Whirlin","length":918,"organism":"Mus musculus","dataset":[],"UniParc":"UPI000024E051","genes":[{"name":{"value":"Whrn","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:2682003","url":"http://www.informatics.jax.org/marker/MGI:2682003"}}]},"synonyms":[{"value":"Dfnb31"},{"value":"Kiaa1526"}]}],"alphafold_very_low_content":0.48257080610021785,"disorder_content":0.011982570806100218,"disprot_consensus":{"full":[{"start":420,"end":430,"type":"D"}],"Structural state":[{"start":420,"end":430,"type":"D"}]}},{"features":{"gene3D":[{"start":643,"end":707,"id":"G3DSA:3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"}],"pfam":[{"id":"PF12618","name":"PHD finger protein 20, AT-hook","start":176,"end":280},{"id":"PF18115","name":"DNA repair protein Crb2 Tudor domain","start":90,"end":136},{"id":"PF20826","name":"PhD finger domain","start":645,"end":699}]},"uniref50":"UniRef50_Q9BVI0","sequence":"MTKHPPNRRGISFEVGAQLEARDRLKNWYPAHIEDIDYEEGKVLIHFKRWNHRYDEWFCWDSPYLRPLEKIQLRKEGLHEEDGSSEFQINEQVLACWSDCRFYPAKVTAVNKDGTYTVKFYDGVVQTVKHIHVKAFSKDQNIVGNARPKETDHKSLSSSPDKREKFKEQRKATVNVKKDKEDKPLKTEKRPKQPDKEGKLICSEKGKVSEKSLPKNEKEDKENISENDREYSGDAQVDKKPENDIVKSPQENLREPKRKRGRPPSIAPTAVDSNSQTLQPITLELRRRKISKGCEVPLKRPRLDKNSSQEKSKNYSENTDKDLSRRRSSRLSTNGTHEILDPDLVVSDLVDTDPLQDTLSSTKESEEGQLKSALEAGQVSSALTCHSFGDGSGAAGLELNCPSMGENTMKTEPTSPLVELQEISTVEVTNTFKKTDDFGSSNAPAVDLDHKFRCKVVDCLKFFRKAKLLHYHMKYFHGMEKSLEPEESPGKRHVQTRGPSASDKPSQETLTRKRVSASSPTTKDKEKNKEKKFKEFVRVKPKKKKKKKKKTKPECPCSEEISDTSQEPSPPKAFAVTRCGSSHKPGVHMSPQLHGPESGHHKGKVKALEEDNLSESSSESFLWSDDEYGQDVDVTTNPDEELDGDDRYDFEVVRCICEVQEENDFMIQCEECQCWQHGVCMGLLEENVPEKYTCYVCQDPPGQRPGFKYWYDKEWLSRGHMHGLAFLEENYSHQNAKKIVATHQLLGDVQRVIEVLHGLQLKMSILQSREHPDLPLWCQPWKQHSGEGRSHFRNIPVTDTRSKEEAPSYRTLNGAVEKPRPLALPLPRSVEESYITSEHCYQKPRAYYPAVEQKLVVETRGSALDDAVNPLHENGDDSLSPRLGWPLDQDRSKGDSDPKPGSPKVKEYVSKKALPEEAPARKLLDRGGEGLLSSQHQWQFNLLTHVESLQDEVTHRMDSIEKELDVLESWLDYTGELEPPEPLARLPQLKHCIKQLLMDLGKVQQIALCCST","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q9BVI0","disprot_id":"DP02427","ncbi_taxon_id":9606,"regions_counter":1,"creator":"fquaglia","regions":[{"region_id":"DP02427r001","ec_ontology":"ECO","end":85,"term_id":"IDPO:0000002","start":70,"version":2,"statement":[{"text":"Strong electron density was apparent for residues 4–69. Terminal residues were disordered and without supporting electron density.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22449972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3QII"},{"db":"PDB","id":"3Q1J"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Crystal structures of the Tudor domains of human PHF20 reveal novel structural variations on the Royal Family of proteins. <i> Adams-Cioaba MA, Li Z, Tempel W, Guo Y, Bian C, Li Y, Lam R, Min J. </i> FEBS Lett, 2012","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","uniref100":"UniRef100_Q9BVI0","date":"2019-12-05T14:24:36.802Z","acc":"Q9BVI0","name":"PHD finger protein 20","length":1012,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000006E61B","genes":[{"name":{"value":"PHF20"},"synonyms":[{"value":"C20orf104"},{"value":"GLEA2"},{"value":"HCA58"},{"value":"NZF"},{"value":"TZP"}]}],"alphafold_very_low_content":0.6294466403162056,"disorder_content":0.015810276679841896,"disprot_consensus":{"full":[{"start":70,"end":85,"type":"D"}],"Structural state":[{"start":70,"end":85,"type":"D"}]}},{"features":{"gene3D":[{"start":121,"end":220,"id":"G3DSA:2.10.90.10","name":"Cystine-knot cytokines"}],"pfam":[{"id":"PF00019","name":"Transforming growth factor beta like domain","start":123,"end":218}]},"uniref50":"UniRef50_Q5T4W7","sequence":"MELGLGGLSTLSHCPWPRQQPALWPTLAALALLSSVAEASLGSAPRSPAPREGPPPVLASPAGHLPGGRTARWCSGRARRPPPQPSRPAPPPPAPPSALPRGGRAARAGGPGSRARAAGARGCRLRSQLVPVRALGLGHRSDELVRFRFCSGSCRRARSPHDLSLASLLGAGALRPPPGSRPVSQPCCRPTRYEAVSFMDVNSTWRTVDRLSATACGCLG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_Q5T4W7","disprot_id":"DP02428","ncbi_taxon_id":9606,"regions_counter":1,"creator":"fquaglia","regions":[{"region_id":"DP02428r001","ec_ontology":"ECO","end":120,"term_id":"IDPO:0000002","start":108,"version":2,"statement":[{"text":"The amino-terminal 12 residues are disordered in each monomer; both monomers start at residue 13","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16734417","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2ASK"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Artemin crystal structure reveals insights into heparan sulfate binding. <i> Silvian L, Jin P, Carmillo P, Boriack-Sjodin PA, Pelletier C, Rushe M, Gong B, Sah D, Pepinsky B, Rossomando A. </i> Biochemistry, 2006","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","uniref100":"UniRef100_Q5T4W7","date":"2019-12-05T14:35:51.240Z","acc":"Q5T4W7","name":"Artemin","length":220,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000013C9E4","genes":[{"name":{"value":"ARTN"},"synonyms":[{"value":"EVN"}]}],"alphafold_very_low_content":0.1318181818181818,"disorder_content":0.05909090909090909,"disprot_consensus":{"full":[{"start":108,"end":120,"type":"D"}],"Structural state":[{"start":108,"end":120,"type":"D"}]}},{"features":{"gene3D":[],"pfam":[{"id":"PF00071","name":"Ras family","start":117,"end":279}]},"uniref50":"UniRef50_Q9WTY2","sequence":"MHTDLDTDMDADTETVALCSSSSRQASPSGTPTPEADTTLLKQKPEKLLAELDRGGPPPAPGVPRRRGSMPVPYKHQLRRAQAVDELDWPPQASSSGSSDSLGSGEAALAQKDGVFKVMLLGESGVGKSTLAGTFGGLQGDNAHEMENSEDTYERRIMVDKEEVTLIVYDIWEQGDAGGWLQDHCLQTGDAFLIVFSVTDRRSFSKVPETLLRLRAGRPHHDLPVILVGNKSDLARSREVSLEEGRHLAGTLSCKHIETSAALHHNTRELFEGAVRQIRLRRGRGHAGGQRPEPSSPDGPAPPTRRESLTKKAKRFLANLVPRNAKFFKQRSRSCHDLSVL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref90":"UniRef90_Q9WTY2","disprot_id":"DP02429","ncbi_taxon_id":10116,"regions_counter":2,"creator":"fquaglia","regions":[{"region_id":"DP02429r001","ec_ontology":"ECO","end":150,"term_id":"IDPO:0000002","start":137,"version":2,"statement":[{"text":"The absence of electron density suggests that switches I and II are disordered.","type":"Results"},{"text":"Overall, our structure reveals that switch I and switch II of Rem2 are flexible regions in the GDP-bound form and in the absence of the N- and C-terminal extensions.","type":"Results"},{"text":"Our analysis supports the idea that the crystal-packing environment stabilizes or imposes a conformation on the switch regions and that the switch regions are disordered in the absence of contact.","type":"Results"},{"text":"Differences in the crystal-packing environment revealed that the switch I and switch II regions are flexible and not ordered as previously reported","type":"Abstract"},{"text":"No defined electron density was observed in the switch I and II regions, i.e. residues 137–150 and 171–182 of molecule A, and residues 138–149 and 171–182 of molecule B.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22684057","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4AII"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structure of the GDP-bound G domain of the RGK protein Rem2. <i> Reymond P, Coquard A, Chenon M, Zeghouf M, El Marjou A, Thompson A, Ménétrey J. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02429r002","ec_ontology":"ECO","end":182,"term_id":"IDPO:0000002","start":171,"version":2,"statement":[{"text":"The absence of electron density suggests that switches I and II are disordered.","type":"Results"},{"text":"Overall, our structure reveals that switch I and switch II of Rem2 are flexible regions in the GDP-bound form and in the absence of the N- and C-terminal extensions.","type":"Results"},{"text":"Our analysis supports the idea that the crystal-packing environment stabilizes or imposes a conformation on the switch regions and that the switch regions are disordered in the absence of contact.","type":"Results"},{"text":"Differences in the crystal-packing environment revealed that the switch I and switch II regions are flexible and not ordered as previously reported","type":"Abstract"},{"text":"No defined electron density was observed in the switch I and II regions, i.e. residues 137–150 and 171–182 of molecule A, and residues 138–149 and 171–182 of molecule B.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22684057","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4AII"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structure of the GDP-bound G domain of the RGK protein Rem2. <i> Reymond P, Coquard A, Chenon M, Zeghouf M, El Marjou A, Thompson A, Ménétrey J. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","uniref100":"UniRef100_Q9WTY2","date":"2019-12-05T16:15:24.133Z","acc":"Q9WTY2","name":"GTP-binding protein REM 2","length":341,"organism":"Rattus norvegicus","dataset":[],"UniParc":"UPI00000E7B02","genes":[{"name":{"value":"Rem2"}}],"alphafold_very_low_content":0.2991202346041056,"disorder_content":0.07624633431085044,"disprot_consensus":{"full":[{"start":137,"end":150,"type":"D"},{"start":171,"end":182,"type":"D"}],"Structural state":[{"start":137,"end":150,"type":"D"},{"start":171,"end":182,"type":"D"}]}},{"features":{"gene3D":[{"start":182,"end":282,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"}],"pfam":[{"id":"PF28825","name":"CD19 transmembrane domain","start":280,"end":315}]},"uniref50":"UniRef50_P15391","sequence":"MPPPRLLFFLLFLTPMEVRPEEPLVVKVEEGDNAVLQCLKGTSDGPTQQLTWSRESPLKPFLKLSLGLPGLGIHMRPLAIWLFIFNVSQQMGGFYLCQPGPPSEKAWQPGWTVNVEGSGELFRWNVSDLGGLGCGLKNRSSEGPSSPSGKLMSPKLYVWAKDRPEIWEGEPPCLPPRDSLNQSLSQDLTMAPGSTLWLSCGVPPDSVSRGPLSWTHVHPKGPKSLLSLELKDDRPARDMWVMETGLLLPRATAQDAGKYYCHRGNLTMSFHLEITARPVLWHWLLRTGGWKVSAVTLAYLIFCLCSLVGILHLQRALVLRRKRKRMTDPTRRFFKVTPPPGSGPQNQYGNVLSLPTPTSGLGRAQRWAAGLGGTAPSYGNPSSDVQADGALGSRSPPGVGPEEEEGEGYEEPDSEEDSEFYENDSNLGQDQLSQDGSGYENPEDEPLGPEDEDSFSNAESYENEDEELTQPVARTMDFLSPHGSAWDPSREATSLGSQSYEDMRGILYAAPQLRSIRGQPGPNHEEDADSYENMDNPDGPDPAWGGGGRMGTWSTR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref90":"UniRef90_P15391","disprot_id":"DP02431","ncbi_taxon_id":9606,"regions_counter":2,"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":152,"region_id":"DP02431r001","start":138,"term_id":"IDPO:0000002","statement":[{"text":"Residues 118–185 form a three‐stranded β‐sheet of mixed topology (strands I, J, K) and two presumably unstructured partially disordered loops.","type":"Results"},{"text":"Residues 138–152 and 177–183 are not defined in the electron density and were not included in the model.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29490423","version":2,"reference_html":"Crystal structure of B-cell co-receptor CD19 in complex with antibody B43 reveals an unexpected fold. <i> Teplyakov A, Obmolova G, Luo J, Gilliland GL. </i> Proteins, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6AL5"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","uniref100":"UniRef100_P15391","date":"2019-12-06T09:36:06.634Z","acc":"P15391","name":"B-lymphocyte antigen CD19","length":556,"organism":"Homo sapiens","dataset":[],"UniParc":"UPI000016A560","genes":[{"name":{"value":"CD19"}}],"alphafold_very_low_content":0.44244604316546765,"disorder_content":0.02697841726618705,"disprot_consensus":{"full":[{"start":138,"end":152,"type":"D"}],"Structural state":[{"start":138,"end":152,"type":"D"}]}},{"acc":"Q96RS0","name":"Trimethylguanosine synthase","sequence":"MCCEKWSRVAEMFLFIEEREDCKILCLCSRAFVEDRKLYNLGLKGYYIRDSGNNSGDQATEEEEGGYSCGTAESHDSKGIGLDESELDSEAELMRSMGLPLQFGRITAHKDFEVSMNTRNKVKIKKKKHQKKYLDEIVQESWRKEYEEDDILASDDPSSIEQYENTRTYELQSKKDTETENPPVENTLSPKLEITEKWEKYWNEYGGGLLWQSWQEKHPGQALSSEPWNFPDTKEEWEQHYSQLYWYYLEQFQYWEAQGWTFDASQSCDTDTYTSKTEADDKNDEKCMKVDLVSFPSSPIMVDNDSSGTSDKDHSEILDGISNIKLNSEEVTQSQLDSCTSHDGHQQLSEVSSKRECPASGQSEPRNGGTNEESNSSGNTNTDPPAEDSQKSSGANTSKDRPHASGTDGDESEEDPPEHKPSKLKRSHELDIDENPASDFDDSGSLLGFKYGSGQKYGGIPNFSHRQVRYLEKNVKLKSKYLDMRRQIKMKNKHIFFTKESEKPFFKKSKILSKVEKFLTWVNKPMDEEASQESSSHDNVHDASTSSDSEEQDMSVKKGDDLLETNNPEPEKCQSVSSAGELETENYERDSLLATVPDEQDCVTQEVPDSRQAETEAEVKKKKNKKKNKKVNGLPPEIAAVPELAKYWAQRYRLFSRFDDGIKLDREGWFSVTPEKIAEHIAGRVSQSFKCDVVVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLASFLKADVVFLSPPWGGPDYATAETFDIRTMMSPDGFEIFRLSKKITNNIVYFLPRNADIDQVASLAGPGGQVEIEQNFLNNKLKTITAYFGDLIRRPASET","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":633,"region_id":"DP02445r001","start":618,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Residues 634–844 of monomer 1 are well defined in the electron density map, whereas for monomers 2 and 3 only the residues 637–847 and 641–847 could be placed.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19386620","version":2,"reference_html":"Structural basis for m7G-cap hypermethylation of small nuclear, small nucleolar and telomerase RNA by the dimethyltransferase TGS1. <i> Monecke T, Dickmanns A, Ficner R. </i> Nucleic Acids Res, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3GDH"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-22T13:59:55.518Z"}}],"released":"2023_12","length":853,"ncbi_taxon_id":9606,"date":"2019-12-06T13:01:23.831Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF09445","name":"RNA cap guanine-N2 methyltransferase","start":692,"end":844}]},"disprot_id":"DP02445","regions_counter":1,"dataset":["RNA-binding proteins"],"UniParc":"UPI000006DC33","uniref100":"UniRef100_Q96RS0","uniref90":"UniRef90_Q96RS0","uniref50":"UniRef50_Q96RS0","genes":[{"name":{"value":"TGS1"},"synonyms":[{"value":"HCA137"},{"value":"NCOA6IP"},{"value":"PIMT"}]}],"alphafold_very_low_content":0.4771395076201641,"disorder_content":0.01875732708089097,"disprot_consensus":{"full":[{"start":618,"end":633,"type":"D"}],"Structural state":[{"start":618,"end":633,"type":"D"}]}},{"acc":"Q8IU57","name":"Interferon lambda receptor 1","sequence":"MAGPERWGPLLLCLLQAAPGRPRLAPPQNVTLLSQNFSVYLTWLPGLGNPQDVTYFVAYQSSPTRRRWREVEECAGTKELLCSMMCLKKQDLYNKFKGRVRTVSPSSKSPWVESEYLDYLFEVEPAPPVLVLTQTEEILSANATYQLPPCMPPLDLKYEVAFWKEGAGNKTLFPVTPHGQPVQITLQPAASEHHCLSARTIYTFSVPKYSKFSKPTCFLLEVPEANWAFLVLPSLLILLLVIAAGGVIWKTLMGNPWFQRAKMPRALDFSGHTHPVATFQPSRPESVNDLFLCPQKELTRGVRPTPRVRAPATQQTRWKKDLAEDEEEEDEEDTEDGVSFQPYIEPPSFLGQEHQAPGHSEAGGVDSGRPRAPLVPSEGSSAWDSSDRSWASTVDSSWDRAGSSGYLAEKGPGQGPGGDGHQESLPPPEFSKDSGFLEELPEDNLSSWATWGTLPPEPNLVPGGPPVSLQTLTFCWESSPEEEEEARESEIEDSDAGSWGAESTQRTEDRGRTLGHYMAR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":299,"region_id":"DP02446r001","start":270,"term_id":"IDPO:0000002","statement":[{"text":"Beyond Ser270, the electron density for IFNLR1 is poor, suggesting disorder of the peptide backbone likely due to a lack of contacts with JAK1. In addition, we were unable to model the IFNLR1 box2 motif due to significant structural disorder in the JAK1 SH2 domain.","type":"Results"},{"text":"IFNLR1 box2 containing peptide (residues 270–299) showed no detectable binding to JAK1","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27133025","version":2,"reference_html":"The Structural Basis for Class II Cytokine Receptor Recognition by JAK1. <i> Ferrao R, Wallweber HJ, Ho H, Tam C, Franke Y, Quinn J, Lupardus PJ. </i> Structure, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5IXD"},{"db":"PDB","id":"5IXI"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":520,"ncbi_taxon_id":9606,"date":"2019-12-06T13:56:20.291Z","organism":"Homo sapiens","features":{"gene3D":[{"start":125,"end":223,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":125,"end":223,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"}],"pfam":[{"id":"PF01108","name":"Tissue factor","start":10,"end":111}]},"disprot_id":"DP02446","regions_counter":1,"dataset":[],"UniParc":"UPI000004D3FC","uniref100":"UniRef100_Q8IU57","uniref90":"UniRef90_Q8IU57","uniref50":"UniRef50_Q8IU57","genes":[{"name":{"value":"IFNLR1"},"synonyms":[{"value":"IL28RA"},{"value":"LICR2"}]}],"alphafold_very_low_content":0.4653846153846154,"disorder_content":0.057692307692307696,"disprot_consensus":{"full":[{"start":270,"end":299,"type":"D"}],"Structural state":[{"start":270,"end":299,"type":"D"}]}},{"acc":"Q03707","name":"Inner nuclear membrane protein SRC1","sequence":"MNSDLEYLEDGFDPNSMKVATLRRILVENNVDFPSNARKNALVGLFDEKVKPQIPQLRKMYLNVRPSDEGIVKMDRPSSSPSIASPRRSRRARREKSASPMAKQFKKNRILDDVSNDDDDDDDDDDDNDKKDDPLIVPSGTDTDEVDDEEDDVITSSSNKSDTNDFQQNSDTRKKRKDPDSDDWSESNSKENKIDNKHLNLLSSDSEIEQDYQKAKKRKTSDLNQEHGNGSAILGKLSVKTPIKNTNRKPVSMDNFNDSLTSSGTENDPFVPNIRHNPKELGTANGTGHSTPLSKLKVSASFADKLPQKEVPSTILVPEVEQQEPSQSERTPSLFSSEGSGSESEAPLLPEITTPGPHQPMGNTSNNVVEMIDTDSSNLVSDEDEVLVPTRIETPQLPTEKDVEKCEARVQELQEEVNEQLEHENGSEFDVKQGSGKVGNRHKFKRALKFLSKSLLALFLFCIFIVIPLLFGLWYREQRLLIGYCGHEVPSHRVSGNSFEFIQKLDNLLQDYRPKCIPCPPNGICYPYLKLKCKPDYKLAPSRLDFLEIIPAQGKCVKDDKKQQLVSEVVEKSLEFLRAKNAQISCGDGKDDIESGMTEDALYQIFNEARAPWIRDDEFEDLWIQVIKDLTEEPEILWRQLSPTDNNIGGNSNNIIKTNDVPRQKRHLPEKFISKTRNFRSTSKKYIGMKCRFEREIYQTYKKFQRPIWLMFLLIVISKVIEIKLKNYYRKKARIEELVTQTMEKLKFQKIKSMSDPKENAYLSIVQLRDIFLSDIVDLKYKNQLWSEVVKYLEHNNSNIKSNLTEIRGEIMKCWEWIGPMELNEPKDSAENKI","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":221,"region_id":"DP02448r001","start":196,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The crystal structure of ΔIBB-Kap60 crystallized in complex with a 50-mer spanning Heh1 resides 171-221 has density only for the first half of the Heh1 construct (residues 173-195), while no discernable electron density was observed for residues 196-221.","type":"Results"},{"text":"it was shown that a region between residues 173-220, encoding several basic patches similar to a cNLS, and a ~200 residues unfolded linker were required and sufficient for nuclear import","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26051712","version":2,"reference_html":"Distinctive Properties of the Nuclear Localization Signals of Inner Nuclear Membrane Proteins Heh1 and Heh2. <i> Lokareddy RK, Hapsari RA, van Rheenen M, Pumroy RA, Bhardwaj A, Steen A, Veenhoff LM, Cingolani G. </i> Structure, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4XZR"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":222,"end":454,"reference_id":"23357007","reference_source":"pmid","reference_html":"Quantitative analysis of membrane protein transport across the nuclear pore complex. <i> Meinema AC, Poolman B, Veenhoff LM. </i> Traffic, 2013","date":"2022-11-10T18:45:20.474Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02448r005","statement":[{"text":"Sufficient for efficient import to the INM are the high-affinity NLS of Heh2 (h2NLS) or Heh1 and a long intrinsically disordered linker (L) between the NLS and the transmembrane domain. The disordered linker needs to be longer than 120 residues but no specific amino acid sequence is required.","type":"Article"}]},{"start":222,"end":454,"reference_id":"26051712","reference_source":"pmid","reference_html":"Distinctive Properties of the Nuclear Localization Signals of Inner Nuclear Membrane Proteins Heh1 and Heh2. <i> Lokareddy RK, Hapsari RA, van Rheenen M, Pumroy RA, Bhardwaj A, Steen A, Veenhoff LM, Cingolani G. </i> Structure, 2015","date":"2022-11-10T18:45:05.768Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02448r006","statement":[{"text":"More recently, it was found (Meinema et al., 2011) that the NLS together with an intrinsically disordered (ID) linker ∼180–230 amino acids long in the extra-luminal surface of Heh1 and Heh2 is essential and sufficient for INM targeting.","type":"Abstract"},{"text":"The exact boundaries of the Heh1 NLS were unknown before this study, although it was shown that a region between residues 173 and 220, encoding several basic patches similar to a cNLS, and a ∼200-residue unfolded linker were required and sufficient for nuclear import (Meinema et al., 2011). ","type":"Results"},{"text":"Considering that a NLS domain was describe for the region 171–220 and the transmembrane region starts at the 455 residue, the authors are referring to the 221-454 region as the flexible linker region.","type":"Curator statement"}]},{"start":222,"end":454,"reference_id":"26051712","reference_source":"pmid","reference_html":"Distinctive Properties of the Nuclear Localization Signals of Inner Nuclear Membrane Proteins Heh1 and Heh2. <i> Lokareddy RK, Hapsari RA, van Rheenen M, Pumroy RA, Bhardwaj A, Steen A, Veenhoff LM, Cingolani G. </i> Structure, 2015","date":"2022-11-10T18:45:48.917Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02448r007","statement":[{"text":"More recently, it was found (Meinema et al., 2011) that the NLS together with an intrinsically disordered (ID) linker ∼180–230 amino acids long in the extra-luminal surface of Heh1 and Heh2 is essential and sufficient for INM targeting.","type":"Abstract"},{"text":"The exact boundaries of the Heh1 NLS were unknown before this study, although it was shown that a region between residues 173 and 220, encoding several basic patches similar to a cNLS, and a ∼200-residue unfolded linker were required and sufficient for nuclear import (Meinema et al., 2011). ","type":"Results"},{"text":"Considering that a NLS domain was describe for the region 171–220 and the transmembrane region starts at the 455 residue, the authors are referring to the 221-454 region as the flexible linker region.","type":"Curator statement"}]}],"released":"2023_12","length":834,"ncbi_taxon_id":559292,"date":"2019-12-09T09:15:19.962Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","features":{"gene3D":[{"start":721,"end":817,"id":"G3DSA:1.10.10.1180","name":"G3DSA:1.10.10.1180"}],"pfam":[{"id":"PF09402","name":"Man1-Src1p-C-terminal domain","start":463,"end":820},{"id":"PF12949","name":"HeH/LEM domain","start":14,"end":48}]},"disprot_id":"DP02448","regions_counter":7,"dataset":[],"UniParc":"UPI0000168A8A","uniref100":"UniRef100_Q03707","uniref90":"UniRef90_Q03707","uniref50":"UniRef50_Q03707","genes":[{"name":{"value":"SRC1"},"synonyms":[{"value":"HEH1"}],"orfNames":[{"value":"YML033W"}],"olnNames":[{"value":"YML034W"}]}],"alphafold_very_low_content":0.43285371702637887,"disorder_content":0.3105515587529976,"disprot_consensus":{"full":[{"start":196,"end":454,"type":"D"}],"Structural state":[{"start":196,"end":454,"type":"D"}],"Disorder function":[{"start":222,"end":454,"type":"F"}]}},{"acc":"Q15583","name":"Homeobox protein TGIF1","sequence":"MVLAQSRVSAGVGSPHCSGSGGGGSDSFPWPASHPGNPQCSFSTAFLASPRLSRGTLAYLPPAPWSSLATPSALLGSSCAPPPPPARCPQPRALSPELGTKAGPRRPHRWELPRSPSQGAQGPAPRRRLLETMKGIVAASGSETEDEDSMDIPLDLSSSAGSGKRRRRGNLPKESVQILRDWLYEHRYNAYPSEQEKALLSQQTHLSTLQVCNWFINARRRLLPDMLRKDGKDPNQFTISRRGAKISETSSVESVMGIKNFMPALEETPFHSCTAGPNPTLGRPLSPKPSSPGSVLARPSVICHTTVTALKDVPFSLCQSVGVGQNTDIQQIAAKNFTDTSLMYPEDTCKSGPSTNTQSGLFNTPPPTPPDLNQDFSGFQLLVDVALKRAAEMELQAKLTA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":167,"region_id":"DP02449r001","start":150,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Residues 168–234 (chain A), 164–229 (chain B), and the 16mer dsDNA are well-defined in the electron density map","type":"Results"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30060237","version":2,"reference_html":"TGIF1 homeodomain interacts with Smad MH1 domain and represses TGF-β signaling. <i> Guca E, Suñol D, Ruiz L, Konkol A, Cordero J, Torner C, Aragon E, Martin-Malpartida P, Riera A, Macias MJ. </i> Nucleic Acids Res, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6FQP"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-26T13:16:40.388Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":248,"region_id":"DP02449r002","start":235,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Residues 168–234 (chain A), 164–229 (chain B), and the 16mer dsDNA are well-defined in the electron density map","type":"Results"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30060237","version":2,"reference_html":"TGIF1 homeodomain interacts with Smad MH1 domain and represses TGF-β signaling. <i> Guca E, Suñol D, Ruiz L, Konkol A, Cordero J, Torner C, Aragon E, Martin-Malpartida P, Riera A, Macias MJ. </i> Nucleic Acids Res, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6FQP"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-26T13:16:40.159Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":347,"region_id":"DP02449r003","start":256,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The TGIF1 C-term domain is intrinsically disordered in solution","type":"Results"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30060237","version":2,"reference_html":"TGIF1 homeodomain interacts with Smad MH1 domain and represses TGF-β signaling. <i> Guca E, Suñol D, Ruiz L, Konkol A, Cordero J, Torner C, Aragon E, Martin-Malpartida P, Riera A, Macias MJ. </i> Nucleic Acids Res, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"BMRB","id":"27461"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-26T13:12:38.845Z"}},{"region_id":"DP02449r005","unpublished":true,"ec_ontology":"ECO","end":347,"term_id":"GO:0005515","start":256,"version":3,"statement":[{"text":"The TGIF1 C-term domain is intrinsically disordered in solution","type":"Results"},{"text":"We found weak-medium interactions between the phosphorylated TGIF1 C-term and Smad2 linker-MH2 construct","type":"Discussion"},{"text":"We have shown how two distinct regions of TGIF1, namely the HD and the C-term domain, interact with the MH1 and MH2 domains of Smad proteins respectively.","type":"Discussion"},{"text":"We propose that the binding of the TGIF1 C-term to the Smad2-MH2 domain brings both the HD and MH1 domain into close proximity.","type":"Abstract"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q15796","partner_end":null}],"term_name":"protein binding","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2023_06","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"30060237","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"27461"}],"term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"fquaglia","reference_html":"TGIF1 homeodomain interacts with Smad MH1 domain and represses TGF-β signaling. <i> Guca E, Suñol D, Ruiz L, Konkol A, Cordero J, Torner C, Aragon E, Martin-Malpartida P, Riera A, Macias MJ. </i> Nucleic Acids Res, 2018","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":288,"region_id":"DP02449r007","start":284,"term_id":"IDPO:0000045","unpublished":true,"statement":[{"text":"The TGIF1 C-term domain is intrinsically disordered in solution","type":"Results"},{"text":"The C-term domain of TGIF1 holds the Smad-binding domain, which includes several phosphorylatable residues. Three of these residues, Ser286, 291 and 294, are phosphorylated in vivo, although the specific roles of these phosphorylations are not fully understood.","type":"Results"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30060237","version":2,"reference_html":"TGIF1 homeodomain interacts with Smad MH1 domain and represses TGF-β signaling. <i> Guca E, Suñol D, Ruiz L, Konkol A, Cordero J, Torner C, Aragon E, Martin-Malpartida P, Riera A, Macias MJ. </i> Nucleic Acids Res, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"BMRB","id":"27461"}],"term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":293,"region_id":"DP02449r008","start":289,"term_id":"IDPO:0000045","unpublished":true,"statement":[{"text":"The TGIF1 C-term domain is intrinsically disordered in solution\" Results \"The C-term domain of TGIF1 holds the Smad-binding domain, which includes several phosphorylatable residues. Three of these residues, Ser286, 291 and 294, are phosphorylated in vivo, although the specific roles of these phosphorylations are not fully understood.","type":"Results"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30060237","version":2,"reference_html":"TGIF1 homeodomain interacts with Smad MH1 domain and represses TGF-β signaling. <i> Guca E, Suñol D, Ruiz L, Konkol A, Cordero J, Torner C, Aragon E, Martin-Malpartida P, Riera A, Macias MJ. </i> Nucleic Acids Res, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":296,"region_id":"DP02449r009","start":292,"term_id":"IDPO:0000045","unpublished":true,"statement":[{"text":"The TGIF1 C-term domain is intrinsically disordered in solution\" Results \"The C-term domain of TGIF1 holds the Smad-binding domain, which includes several phosphorylatable residues. Three of these residues, Ser286, 291 and 294, are phosphorylated in vivo, although the specific roles of these phosphorylations are not fully understood.","type":"Results"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30060237","version":2,"reference_html":"TGIF1 homeodomain interacts with Smad MH1 domain and represses TGF-β signaling. <i> Guca E, Suñol D, Ruiz L, Konkol A, Cordero J, Torner C, Aragon E, Martin-Malpartida P, Riera A, Macias MJ. </i> Nucleic Acids Res, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2023_06","length":401,"ncbi_taxon_id":9606,"date":"2019-12-09T11:18:41.798Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF05920","name":"Homeobox KN domain","start":182,"end":221}]},"disprot_id":"DP02449","regions_counter":9,"dataset":["NDDs-related proteins"],"UniParc":"UPI0000140386","uniref100":"UniRef100_Q15583","uniref90":"UniRef90_Q15583","uniref50":"UniRef50_Q15583","genes":[{"name":{"value":"TGIF1"},"synonyms":[{"value":"TGIF"}]}],"alphafold_very_low_content":0.5261845386533666,"disorder_content":0.3092269326683292,"disprot_consensus":{"full":[{"start":150,"end":167,"type":"D"},{"start":235,"end":248,"type":"D"},{"start":256,"end":347,"type":"D"}],"Structural state":[{"start":150,"end":167,"type":"D"},{"start":235,"end":248,"type":"D"},{"start":256,"end":347,"type":"D"}],"Molecular function":[{"start":256,"end":347,"type":"F"}],"Disorder function":[{"start":284,"end":296,"type":"F"}]}},{"acc":"P46938","name":"Transcriptional coactivator YAP1","sequence":"MEPAQQPPPQPAPQGPAPPSVSPAGTPAAPPAPPAGHQVVHVRGDSETDLEALFNAVMNPKTANVPQTVPMRLRKLPDSFFKPPEPKSHSRQASTDAGTAGALTPQHVRAHSSPASLQLGAVSPGTLTASGVVSGPAAAPAAQHLRQSSFEIPDDVPLPAGWEMAKTSSGQRYFLNHNDQTTTWQDPRKAMLSQLNVPAPASPAVPQTLMNSASGPLPDGWEQAMTQDGEVYYINHKNKTTSWLDPRLDPRFAMNQRITQSAPVKQPPPLAPQSPQGGVLGGGSSNQQQQIQLQQLQMEKERLRLKQQELFRQAIRNINPSTANAPKCQELALRSQLPTLEQDGGTPNAVSSPGMSQELRTMTTNSSDPFLNSGTYHSRDESTDSGLSMSSYSIPRTPDDFLNSVDEMDTGDTISQSTLPSQQSRFPDYLEALPGTNVDLGTLEGDAMNIEGEELMPSLQEALSSEILDVESVLAATKLDKESFLTWL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":64,"region_id":"DP02451r001","start":35,"term_id":"IDPO:0000002","statement":[{"text":"Several regions of the polypeptide chains are not visible in the electron density map and are assumed to be disordered;\nresidue chain B: 35–46 and 87–92; chain D: 35–47 and 83–92; chain F: 35–47 and 84–92; and chain H: 35–64 and 84–92.","type":"Methods"},{"text":"annotated positions are referred to chain H","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20123908","version":2,"reference_html":"Structural basis of YAP recognition by TEAD4 in the hippo pathway. <i> Chen L, Chan SW, Zhang X, Walsh M, Lim CJ, Hong W, Song H. </i> Genes Dev, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3JUA"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":488,"ncbi_taxon_id":10090,"date":"2019-12-09T12:51:12.922Z","organism":"Mus musculus","features":{"gene3D":[],"pfam":[{"id":"PF00397","name":"WW domain","start":158,"end":187},{"id":"PF00397","name":"WW domain","start":217,"end":246},{"id":"PF15238","name":"Omega loop, TEAD interacting region 3","start":69,"end":84}]},"disprot_id":"DP02451","regions_counter":1,"dataset":[],"UniParc":"UPI00000E5DEC","uniref100":"UniRef100_P46938","uniref90":"UniRef90_P46938","uniref50":"UniRef50_P46937-6","genes":[{"name":{"value":"Yap1"},"synonyms":[{"value":"Yap"},{"value":"Yap65"}]}],"alphafold_very_low_content":0.48565573770491804,"disorder_content":0.06147540983606557,"disprot_consensus":{"full":[{"start":35,"end":64,"type":"D"}],"Structural state":[{"start":35,"end":64,"type":"D"}]}},{"acc":"Q8TEA8","name":"D-aminoacyl-tRNA deacylase 1","sequence":"MKAVVQRVTRASVTVGGEQISAIGRGICVLLGISLEDTQKELEHMVRKILNLRVFEDESGKHWSKSVMDKQYEILCVSQFTLQCVLKGNKPDFHLAMPTEQAEGFYNSFLEQLRKTYRPELIKDGKFGAYMQVHIQNDGPVTIELESPAPGTATSDPKQLSKLEKQQQRKEKTRAKGPSESSKERNTPRKEDRSASSGAEGDVSSEREP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":209,"region_id":"DP02452r001","start":152,"term_id":"IDPO:0000002","statement":[{"text":"The C-terminal portion of DUE-B (amino acids 152–209) is not visible in the crystal structure and is predicted to be dynamically disordered","type":"Results"},{"text":"We further demonstrate that the C-terminal portion of the enzyme is disordered and not essential for dimerization. However, this region is essential for DNA binding in vitro and becomes ordered in the presence of DNA. ","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17264083","version":2,"reference_html":"Structure and function of the c-myc DNA-unwinding element-binding protein DUE-B. <i> Kemp M, Bae B, Yu JP, Ghosh M, Leffak M, Nair SK. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2OKV"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":209,"region_id":"DP02452r002","start":152,"term_id":"GO:0003677","statement":[{"text":"The C-terminal portion of DUE-B (amino acids 152–209) is not visible in the crystal structure and is predicted to be dynamically disordered","type":"Results"},{"text":"We further demonstrate that the C-terminal portion of the enzyme is disordered and not essential for dimerization. However, this region is essential for DNA binding in vitro and becomes ordered in the presence of DNA. ","type":"Abstract"},{"text":"The C-terminal residues that are involved in mediating interactions with target DNA are largely disordered in the crystal","type":"Article"},{"text":"the C terminus is necessary for binding of purified DUE-B to DNA.","type":"Results"},{"text":"Disordered regions of DNA-binding proteins often become ordered upon DNA binding","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"17264083","version":3,"reference_html":"Structure and function of the c-myc DNA-unwinding element-binding protein DUE-B. <i> Kemp M, Bae B, Yu JP, Ghosh M, Leffak M, Nair SK. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"2OKV"}],"term_name":"DNA binding","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":209,"region_id":"DP02452r003","start":152,"term_id":"IDPO:0000011","statement":[{"text":"The C-terminal portion of DUE-B (amino acids 152–209) is not visible in the crystal structure and is predicted to be dynamically disordered","type":"Results"},{"text":"We further demonstrate that the C-terminal portion of the enzyme is disordered and not essential for dimerization. However, this region is essential for DNA binding in vitro and becomes ordered in the presence of DNA. ","type":"Abstract"},{"text":"The C-terminal residues that are involved in mediating interactions with target DNA are largely disordered in the crystal","type":"Article"},{"text":"the C terminus is necessary for binding of purified DUE-B to DNA.","type":"Results"},{"text":"Disordered regions of DNA-binding proteins often become ordered upon DNA binding","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17264083","version":2,"reference_html":"Structure and function of the c-myc DNA-unwinding element-binding protein DUE-B. <i> Kemp M, Bae B, Yu JP, Ghosh M, Leffak M, Nair SK. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"2OKV"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2021_06","length":209,"ncbi_taxon_id":9606,"date":"2019-12-09T13:24:03.429Z","organism":"Homo sapiens","features":{"gene3D":[{"start":1,"end":149,"id":"G3DSA:3.50.80.10","name":"G3DSA:3.50.80.10"}],"pfam":[{"id":"PF02580","name":"D-Tyr-tRNA(Tyr) deacylase","start":4,"end":146}]},"disprot_id":"DP02452","regions_counter":4,"dataset":[],"UniParc":"UPI0000072859","uniref100":"UniRef100_Q8TEA8","uniref90":"UniRef90_Q8TEA8","uniref50":"UniRef50_Q8TEA8","genes":[{"name":{"value":"DTD1"},"synonyms":[{"value":"C20orf88"},{"value":"DUEB"},{"value":"HARS2"}]}],"alphafold_very_low_content":0.10526315789473684,"disorder_content":0.27751196172248804,"disprot_consensus":{"full":[{"start":152,"end":209,"type":"T"}],"Structural state":[{"start":152,"end":209,"type":"D"}],"Molecular function":[{"start":152,"end":209,"type":"F"}],"Structural transition":[{"start":152,"end":209,"type":"T"}]}},{"acc":"Q9UKX7","name":"Nuclear pore complex protein Nup50","sequence":"MAKRNAEKELTDRNWDQEDEAEEVGTFSMASEEVLKNRAIKKAKRRNVGFESDTGGAFKGFKGLVVPSGGGRFSGFGSGAGGKPLEGLSNGNNITSAPPFASAKAAADPKVAFGSLAANGPTTLVDKVSNPKTNGDSQQPSSSGLASSKACVGNAYHKQLAALNCSVRDWIVKHVNTNPLCDLTPIFKDYEKYLANIEQQHGNSGRNSESESNKVAAETQSPSLFGSTKLQQESTFLFHGNKTEDTPDKKMEVASEKKTDPSSLGATSASFNFGKKVDSSVLGSLSSVPLTGFSFSPGNSSLFGKDTTQSKPVSSPFPTKPLEGQAEGDSGECKGGDEEENDEPPKVVVTEVKEEDAFYSKKCKLFYKKDNEFKEKGIGTLHLKPTANQKTQLLVRADTNLGNILLNVLIPPNMPCTRTGKNNVLIVCVPNPPIDEKNATMPVTMLIRVKTSEDADELHKILLEKKDA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"region_id":"DP02455r001","ec_ontology":"ECO","end":109,"term_id":"IDPO:0000002","start":48,"version":2,"statement":[{"text":"Finally, residues 48–109 were not visible in the crystal structure, although they were present in the crystal. This region contains 15 glycines and is likely highly flexible.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22130666","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3TJ3"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Nucleoporin Nup50 stabilizes closed conformation of armadillo repeat 10 in importin α5. <i> Pumroy RA, Nardozzi JD, Hart DJ, Root MJ, Cingolani G. </i> J Biol Chem, 2012","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":468,"ncbi_taxon_id":9606,"date":"2019-12-09T14:13:37.246Z","organism":"Homo sapiens","features":{"gene3D":[{"start":348,"end":468,"id":"G3DSA:2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"}],"pfam":[{"id":"PF00638","name":"RanBP1 domain","start":352,"end":465},{"id":"PF08911","name":"NUP50 (Nucleoporin 50 kDa)","start":2,"end":64}]},"disprot_id":"DP02455","regions_counter":2,"dataset":[],"UniParc":"UPI00001698D2","uniref100":"UniRef100_Q9UKX7","uniref90":"UniRef90_Q9UKX7","uniref50":"UniRef50_Q9UKX7","genes":[{"name":{"value":"NUP50"},"synonyms":[{"value":"NPAP60L"}],"orfNames":[{"value":"PRO1146"}]}],"alphafold_very_low_content":0.4337606837606838,"disorder_content":0.13247863247863248,"disprot_consensus":{"full":[{"start":48,"end":109,"type":"D"}],"Structural state":[{"start":48,"end":109,"type":"D"}]}},{"acc":"O35625","name":"Axin-1","sequence":"MNVQEQGFPLDLGASFTEDAPRPPVPGEEGELVSTDSRPVNHSFCSGKGTSIKSETSTATPRRSDLDLGYEPEGSASPTPPYLRWAESLHSLLDDQDGISLFRTFLKQEGCADLLDFWFACSGFRKLEPCDSNEEKRLKLARAIYRKYILDSNGIVSRQTKPATKSFIKDCVMKQQIDPAMFDQAQTEIQSTMEENTYPSFLKSDIYLEYTRTGSESPKVCSDQSSGSGTGKGMSGYLPTLNEDEEWKCDQDADEDDGRDPLPPSRLTQKLLLETAAPRAPSSRRYNEGRELRYGSWREPVNPYYVNSGYALAPATSANDSEQQSLSSDADTLSLTDSSVDGIPPYRIRKQHRREMQESIQVNGRVPLPHIPRTYRMPKEIRVEPQKFAEELIHRLEAVQRTREAEEKLEERLKRVRMEEEGEDGEMPSGPMASHKLPSVPAWHHFPPRYVDMGCSGLRDAHEENPESILDEHVQRVMRTPGCQSPGPGHRSPDSGHVAKTAVLGGTASGHGKHVPKLGLKLDTAGLHHHRHVHHHVHHNSARPKEQMEAEVARRVQSSFSWGPETHGHAKPRSYSENAGTTLSAGDLAFGGKTSAPSKRNTKKAESGKNANAEVPSTTEDAEKNQKIMQWIIEGEKEISRHRKAGHGSSGLRKQQAHESSRPLSIERPGAVHPWVSAQLRNSVQPSHLFIQDPTMPPNPAPNPLTQLEEARRRLEEEEKRANKLPSKQRYVQAVMQRGRTCVRPACAPVLSVVPAVSDLELSETETKSQRKAGGGSAPPCDSIVVAYYFCGEPIPYRTLVRGRAVTLGQFKELLTKKGSYRYYFKKVSDEFDCGVVFEEVREDEAVLPVFEEKIIGKVEKVD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"region_id":"DP02456r001","ec_ontology":"ECO","end":17,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"Electron densities of two Axin1 segments, Axin1(18-30) and Axin1(60-79), can be clearly visualized on the two ARC2 surfaces in the swapped TNKS dimers (Fig. S4). While the remaining parts of Axin1 cannot be seen in the electron density maps, these two Axin1 segments are likely from the same Axin1(1-80) molecule, since SEC results indicate that Axin1(1-80) stabilizes TNKS(308-655) dimerization in solution (Fig. S3), most likely by interacting with both copies of the swapped dimer. In addition, the distance between Axin1 G30 and A60 Cα atoms in our structure is 49.4 Å, which can be covered by the 29 missing residues in between","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22307604","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3UTM"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Crystal structure of a Tankyrase-Axin complex and its implications for Axin turnover and Tankyrase substrate recruitment. <i> Morrone S, Cheng Z, Moon RT, Cong F, Xu W. </i> Proc Natl Acad Sci U S A, 2012","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02456r002","ec_ontology":"ECO","end":59,"term_id":"IDPO:0000002","start":31,"version":2,"statement":[{"text":"Electron densities of two Axin1 segments, Axin1(18-30) and Axin1(60-79), can be clearly visualized on the two ARC2 surfaces in the swapped TNKS dimers (Fig. S4). While the remaining parts of Axin1 cannot be seen in the electron density maps, these two Axin1 segments are likely from the same Axin1(1-80) molecule, since SEC results indicate that Axin1(1-80) stabilizes TNKS(308-655) dimerization in solution (Fig. S3), most likely by interacting with both copies of the swapped dimer. In addition, the distance between Axin1 G30 and A60 Cα atoms in our structure is 49.4 Å, which can be covered by the 29 missing residues in between","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22307604","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3UTM"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Crystal structure of a Tankyrase-Axin complex and its implications for Axin turnover and Tankyrase substrate recruitment. <i> Morrone S, Cheng Z, Moon RT, Cong F, Xu W. </i> Proc Natl Acad Sci U S A, 2012","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02456r003","ec_ontology":"ECO","end":30,"term_id":"GO:0005515","start":19,"version":3,"statement":[{"text":"Electron densities of two Axin1 segments, Axin1(18-30) and Axin1(60-79), can be clearly visualized on the two ARC2 surfaces in the swapped TNKS dimers (Fig. S4). While the remaining parts of Axin1 cannot be seen in the electron density maps, these two Axin1 segments are likely from the same Axin1(1-80) molecule, since SEC results indicate that Axin1(1-80) stabilizes TNKS(308-655) dimerization in solution (Fig. S3), most likely by interacting with both copies of the swapped dimer. In addition, the distance between Axin1 G30 and A60 Cα atoms in our structure is 49.4 Å, which can be covered by the 29 missing residues in between","type":"Results"},{"text":"The N-terminal domain of mouse Axin1, which contains residues 1-80, was shown to be responsible for TNKS binding, whereas residues 19-30, which is fully conserved in all Axin1 analogues, is necessary for this interaction","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q6PFX9","partner_end":null}],"term_name":"protein binding","ec_name":"isothermal titration calorimetry evidence used in manual assertion","reference_html":"Crystal structure of a Tankyrase-Axin complex and its implications for Axin turnover and Tankyrase substrate recruitment. <i> Morrone S, Cheng Z, Moon RT, Cong F, Xu W. </i> Proc Natl Acad Sci U S A, 2012","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"22307604","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3UTM"}],"term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"fquaglia","curator_orcid":"0000-0002-0341-4888","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_12","length":863,"ncbi_taxon_id":10090,"date":"2019-12-09T15:40:02.276Z","organism":"Mus musculus","features":{"gene3D":[{"start":193,"end":212,"id":"G3DSA:1.10.196.10","name":"G3DSA:1.10.196.10"},{"start":193,"end":212,"id":"G3DSA:1.10.196.10","name":"G3DSA:1.10.196.10"},{"start":780,"end":863,"id":"G3DSA:3.10.20.380","name":"G3DSA:3.10.20.380"}],"pfam":[{"id":"PF00615","name":"Regulator of G protein signaling domain","start":88,"end":210},{"id":"PF00778","name":"DIX domain","start":784,"end":859},{"id":"PF08833","name":"Axin beta-catenin binding motif","start":464,"end":495},{"id":"PF16646","name":"Axin-1 tankyrase binding domain","start":9,"end":82}]},"disprot_id":"DP02456","regions_counter":5,"dataset":[],"UniParc":"UPI0000151A74","uniref100":"UniRef100_O35625","uniref90":"UniRef90_O35625","uniref50":"UniRef50_O35625","genes":[{"name":{"value":"Axin1"},"synonyms":[{"value":"Axin"},{"value":"Fu"}]}],"alphafold_very_low_content":0.5028968713789108,"disorder_content":0.05330243337195829,"disprot_consensus":{"full":[{"start":1,"end":17,"type":"D"},{"start":19,"end":30,"type":"F"},{"start":31,"end":59,"type":"D"}],"Structural state":[{"start":1,"end":17,"type":"D"},{"start":31,"end":59,"type":"D"}],"Molecular function":[{"start":19,"end":30,"type":"F"}]}},{"acc":"O95400","name":"CD2 antigen cytoplasmic tail-binding protein 2","sequence":"MPKRKVTFQGVGDEEDEDEIIVPKKKLVDPVAGSGGPGSRFKGKHSLDSDEEEDDDDGGSSKYDILASEDVEGQEAATLPSEGGVRITPFNLQEEMEEGHFDADGNYFLNRDAQIRDSWLDNIDWVKIRERPPGQRQASDSEEEDSLGQTSMSAQALLEGLLELLLPRETVAGALRRLGARGGGKGRKGPGQPSSPQRLDRLSGLADQMVARGNLGVYQETRERLAMRLKGLGCQTLGPHNPTPPPSLDMFAEELAEEELETPTPTQRGEAESRGDGLVDVMWEYKWENTGDAELYGPFTSAQMQTWVSEGYFPDGVYCRKLDPPGGQFYNSKRIDFDLYT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":280,"region_id":"DP02457r001","start":256,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The structures of the U5-15K and GYF-domain are well defined in the electron density map except for some flexible regions in the C and/or N termini. The refined model of the U5-15K present in the complex consists of amino acid residues 3–137. The structure of the GYF-domain of U5-52K (residues 256–341) lacks the N-terminal 24 residues due to conformational flexibility.","type":"Article"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17467737","version":2,"reference_html":"Structural basis for the bifunctionality of the U5 snRNP 52K protein (CD2BP2). <i> Nielsen TK, Liu S, Lührmann R, Ficner R. </i> J Mol Biol, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1SYX"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2023_12","length":341,"ncbi_taxon_id":9606,"date":"2019-12-09T16:40:38.550Z","organism":"Homo sapiens","features":{"gene3D":[{"start":278,"end":341,"id":"G3DSA:3.30.1490.40","name":"G3DSA:3.30.1490.40"}],"pfam":[{"id":"PF02213","name":"GYF domain","start":283,"end":331}]},"disprot_id":"DP02457","regions_counter":1,"dataset":[],"UniParc":"UPI000006D625","uniref100":"UniRef100_O95400","uniref90":"UniRef90_O95400","uniref50":"UniRef50_O95400","genes":[{"name":{"value":"CD2BP2"},"synonyms":[{"value":"KIAA1178"}]}],"alphafold_very_low_content":0.2316715542521994,"disorder_content":0.07331378299120235,"disprot_consensus":{"full":[{"start":256,"end":280,"type":"D"}],"Structural state":[{"start":256,"end":280,"type":"D"}]}},{"acc":"P17181","name":"Interferon alpha/beta receptor 1","sequence":"MMVVLLGATTLVLVAVAPWVLSAAAGGKNLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQNITSTKCNFSSLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHISPGTKDSVMWALDGLSFTYSLVIWKNSSGVEERIENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQNQNYVLKWDYTYANMTFQVQWLHAFLKRNPGNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSEEIKFDTEIQAFLLPPVFNIRSLSDSFHIYIGAPKQSGNTPVIQDYPLIYEIIFWENTSNAERKIIEKKTDVTVPNLKPLTVYCVKARAHTMDEKLNKSSVFSDAVCEKTKPGNTSKIWLIVGICIALFALPFVIYAAKVFLRCINYVFFPSLKPSSSIDEYFSEQPLKNLLLSTSEEQIEKCFIIENISTIATVEETNQTDEDHKKYSSQTSQDSGNYSNEDESESKTSEELQQDFV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":58,"region_id":"DP02458r001","start":49,"term_id":"IDPO:0000002","statement":[{"text":"missing residues in the PDB","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21854986","version":2,"reference_html":"Structural linkage between ligand discrimination and receptor activation by type I interferons. <i> Thomas C, Moraga I, Levin D, Krutzik PO, Podoplelova Y, Trejo A, Lee C, Yarden G, Vleck SE, Glenn JS, Nolan GP, Piehler J, Schreiber G, Garcia KC. </i> Cell, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3SE4"},{"db":"PDB","id":"3S98"},{"db":"PDB","id":"3SE3"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":436,"region_id":"DP02458r002","start":330,"term_id":"IDPO:0000002","statement":[{"text":"The SD4 of IFNAR1 has been shown to be unnecessary for IFN binding (Lamken et al., 2005) and, consistent with electron-microscopic studies (Li et al., 2008), it was not visible in the electron density maps.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21854986","version":2,"reference_html":"Structural linkage between ligand discrimination and receptor activation by type I interferons. <i> Thomas C, Moraga I, Levin D, Krutzik PO, Podoplelova Y, Trejo A, Lee C, Yarden G, Vleck SE, Glenn JS, Nolan GP, Piehler J, Schreiber G, Garcia KC. </i> Cell, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3SE4"},{"db":"PDB","id":"3S98"},{"db":"PDB","id":"3SE3"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":557,"ncbi_taxon_id":9606,"date":"2019-12-10T10:44:04.872Z","organism":"Homo sapiens","features":{"gene3D":[{"start":333,"end":436,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":333,"end":436,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":333,"end":436,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":333,"end":436,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"}],"pfam":[{"id":"PF01108","name":"Tissue factor","start":12,"end":113},{"id":"PF09294","name":"Interferon-alpha/beta receptor, fibronectin type III","start":127,"end":224},{"id":"PF09294","name":"Interferon-alpha/beta receptor, fibronectin type III","start":332,"end":430}]},"disprot_id":"DP02458","regions_counter":2,"dataset":[],"UniParc":"UPI000002D51B","uniref100":"UniRef100_P17181","uniref90":"UniRef90_P17181","uniref50":"UniRef50_P17181","genes":[{"name":{"value":"IFNAR1"},"synonyms":[{"value":"IFNAR"}]}],"alphafold_very_low_content":0.20646319569120286,"disorder_content":0.21005385996409337,"disprot_consensus":{"full":[{"start":49,"end":58,"type":"D"},{"start":330,"end":436,"type":"D"}],"Structural state":[{"start":49,"end":58,"type":"D"},{"start":330,"end":436,"type":"D"}]}},{"acc":"Q23985","name":"Protein deltex","sequence":"MASSAGSAASGSVVPGGGGSAASSCATMALSTAGSGGPPVNHAHAVCVWEFESRGKWLPYSPAVSQHLERAHAKKLTRVMLSDADPSLEQYYVNVRTMTQESEAETAGSGLLTIGVRRMFYAPSSPAGKGTKWEWSGGSADSNNDWRPYNMHVQCIIEDAWARGEQTLDLCNTHIGLPYTINFCNLTQLRQPSGPMRSIRRTQQAPYPLVKLTPQQANQLKSNSASVSSQYNTLPKLGDTKSLHRVPMTRQQHPLPTSHQVQQQQHQHQHQQQQQQQHHHQHQQQQHQQQQQHQMQHHQIHHQTAPRKPPKKHSEISTTNLRQILNNLNIFSSSTKHQSNMSTAASASSSSSSASLHHANHLSHAHFSHAKNMLTASMNSHHSRCSEGSLQSQRSSRMGSHRSRSRTRTSDTDTNSVKSHRRRPSVDTVSTYLSHESKESLRSRNFAISVNDLLDCSLGSDEVFVPSLPPSSLGERAPVPPPLPLHPRQQQQQQQQQQQLQMQQQQQAQQQQQQSIAGSIVGVDPASDMISRFVKVVEPPLWPNAQPCPMCMEELVHSAQNPAISLSRCQHLMHLQCLNGMIIAQQNEMNKNLFIECPVCGIVYGEKVGNQPIGSMSWSIISKNLPGHEGQNTIQIVYDIASGLQTEEHPHPGRAFFAVGFPRICYLPDCPLGRKVLRFLKIAFDRRLLFSIGRSVTTGREDVVIWNSVDHKTQFNMFPDPTYLQRTMQQLVHLGVTD","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"creator":"fquaglia","regions":[{"region_id":"DP02460r001","ec_ontology":"ECO","end":43,"term_id":"IDPO:0000002","start":26,"version":2,"statement":[{"text":"Outside of the two WWE modules and the 12 C-terminal residues described above, electron density corresponding to the fairly long N- and C-terminal flanking sequences (17 and 60 residues, respectively; see the dashed regions in Figure 1B) is not interpretable, indicating that these two regions are disordered. This apparent disorder suggests that these terminal sequences might not be necessary for the structural integrity of the tandem WWE domain, despite moderate sequence conservation among Deltex orthologs","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16271883","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2A90"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structure and Notch receptor binding of the tandem WWE domain of Deltex. <i> Zweifel ME, Leahy DJ, Barrick D. </i> Structure, 2005","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02460r002","ec_ontology":"ECO","end":261,"term_id":"IDPO:0000002","start":212,"version":2,"statement":[{"text":"Outside of the two WWE modules and the 12 C-terminal residues described above, electron density corresponding to the fairly long N- and C-terminal flanking sequences (17 and 60 residues, respectively; see the dashed regions in Figure 1B) is not interpretable, indicating that these two regions are disordered. This apparent disorder suggests that these terminal sequences might not be necessary for the structural integrity of the tandem WWE domain, despite moderate sequence conservation among Deltex orthologs","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16271883","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2A90"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structure and Notch receptor binding of the tandem WWE domain of Deltex. <i> Zweifel ME, Leahy DJ, Barrick D. </i> Structure, 2005","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":738,"ncbi_taxon_id":7227,"date":"2019-12-10T11:19:38.212Z","organism":"Drosophila melanogaster","features":{"gene3D":[{"start":525,"end":604,"id":"G3DSA:3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":44,"end":210,"id":"G3DSA:3.30.720.50","name":"G3DSA:3.30.720.50"},{"start":607,"end":737,"id":"G3DSA:3.30.390.130","name":"G3DSA:3.30.390.130"}],"pfam":[{"id":"PF02825","name":"WWE domain","start":48,"end":104},{"id":"PF02825","name":"WWE domain","start":132,"end":201},{"id":"PF18102","name":"Deltex C-terminal domain","start":609,"end":736}]},"disprot_id":"DP02460","regions_counter":2,"dataset":[],"UniParc":"UPI000007A4B8","uniref100":"UniRef100_Q23985","uniref90":"UniRef90_Q23985","uniref50":"UniRef50_Q23985","genes":[{"name":{"value":"dx"},"orfNames":[{"value":"CG3929"}]}],"alphafold_very_low_content":0.3875338753387534,"disorder_content":0.0921409214092141,"disprot_consensus":{"full":[{"start":26,"end":43,"type":"D"},{"start":212,"end":261,"type":"D"}],"Structural state":[{"start":26,"end":43,"type":"D"},{"start":212,"end":261,"type":"D"}]}},{"acc":"P17105","name":"Inositol-trisphosphate 3-kinase A","sequence":"MTLPGHPTGMARPRGAGPCSPGLERAPRRSVGELRLLFEARCAAVAAAAAAGEPRARGAKRRGGQVPNGLPRAAPAPVIPQLTVTSEEDVAPASPGPPDREGNWLPAAGSHLQQPRRLSTSSLSSTGSSSLLEDSEDDLLSDSESRSRGNVQLETSEDVGQKSHWQKIRTMVNLPVMSPFKKRYSWVQLAGHTGSFKAAGTSGLILKRSSEPEHYCLVRLMADVLRGCVPAFHGVVERDGESYLQLQDLLDGFDGPCVLDCKMGVRTYLEEELTKARERPKLRKDMYKKMLAVDPEAPTEEEHAQRAVTKPRYMQWREGISSSTTLGFRIEGIKKADGSCSTDFKTTRSREQVTRVFEEFMQGDAEVLKRYLNRLQQIRDTLEISDFFRRHEVIGSSLLFVHDHCHRAGVWLIDFGKTTPLPDGQILDHRRPWEEGNREDGYLLGLDNLIGILANLAER","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":202,"region_id":"DP02461r001","start":185,"term_id":"IDPO:0000002","statement":[{"text":"Residues 185-202 at the N terminus and residue 459 at the C terminus were not seen in electron density and are presumed disordered in this structure.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15350215","version":2,"reference_html":"Crystal structure of the catalytic core of inositol 1,4,5-trisphosphate 3-kinase. <i> Miller GJ, Hurley JH. </i> Mol Cell, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1TZD"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":459,"ncbi_taxon_id":10116,"date":"2019-12-10T11:31:33.159Z","organism":"Rattus norvegicus","features":{"gene3D":[{"start":195,"end":459,"id":"G3DSA:1.10.510.50","name":"G3DSA:1.10.510.50"}],"pfam":[{"id":"PF03770","name":"Inositol polyphosphate kinase","start":243,"end":453}]},"disprot_id":"DP02461","regions_counter":1,"dataset":[],"UniParc":"UPI00001679B7","uniref100":"UniRef100_P17105","uniref90":"UniRef90_P17105","uniref50":"UniRef50_P17105","genes":[{"name":{"value":"Itpka","evidences":[{"code":"ECO:0000312","source":{"name":"RGD","id":"619950","url":"https://rgd.mcw.edu/tools/genes/genes_view.cgi?id=619950"}}]}}],"alphafold_very_low_content":0.3790849673202614,"disorder_content":0.0392156862745098,"disprot_consensus":{"full":[{"start":185,"end":202,"type":"D"}],"Structural state":[{"start":185,"end":202,"type":"D"}]}},{"acc":"Q9NRR4","name":"Ribonuclease 3","sequence":"MMQGNTCHRMSFHPGRGCPRGRGGHGARPSAPSFRPQNLRLLHPQQPPVQYQYEPPSAPSTTFSNSPAPNFLPPRPDFVPFPPPMPPSAQGPLPPCPIRPPFPNHQMRHPFPVPPCFPPMPPPMPCPNNPPVPGAPPGQGTFPFMMPPPSMPHPPPPPVMPQQVNYQYPPGYSHHNFPPPSFNSFQNNPSSFLPSANNSSSPHFRHLPPYPLPKAPSERRSPERLKHYDDHRHRDHSHGRGERHRSLDRRERGRSPDRRRQDSRYRSDYDRGRTPSRHRSYERSRERERERHRHRDNRRSPSLERSYKKEYKRSGRSYGLSVVPEPAGCTPELPGEIIKNTDSWAPPLEIVNHRSPSREKKRARWEEEKDRWSDNQSSGKDKNYTSIKEKEPEETMPDKNEEEEEELLKPVWIRCTHSENYYSSDPMDQVGDSTVVGTSRLRDLYDKFEEELGSRQEKAKAARPPWEPPKTKLDEDLESSSESECESDEDSTCSSSSDSEVFDVIAEIKRKKAHPDRLHDELWYNDPGQMNDGPLCKCSAKARRTGIRHSIYPGEEAIKPCRPMTNNAGRLFHYRITVSPPTNFLTDRPTVIEYDDHEYIFEGFSMFAHAPLTNIPLCKVIRFNIDYTIHFIEEMMPENFCVKGLELFSLFLFRDILELYDWNLKGPLFEDSPPCCPRFHFMPRFVRFLPDGGKEVLSMHQILLYLLRCSKALVPEEEIANMLQWEELEWQKYAEECKGMIVTNPGTKPSSVRIDQLDREQFNPDVITFPIIVHFGIRPAQLSYAGDPQYQKLWKSYVKLRHLLANSPKVKQTDKQKLAQREEALQKIRQKNTMRREVTVELSSQGFWKTGIRSDVCQHAMMLPVLTHHIRYHQCLMHLDKLIGYTFQDRCLLQLAMTHPSHHLNFGMNPDHARNSLSNCGIRQPKYGDRKVHHMHMRKKGINTLINIMSRLGQDDPTPSRINHNERLEFLGDAVVEFLTSVHLYYLFPSLEEGGLATYRTAIVQNQHLAMLAKKLELDRFMLYAHGPDLCRESDLRHAMANCFEALIGAVYLEGSLEEAKQLFGRLLFNDPDLREVWLNYPLHPLQLQEPNTDRQLIETSPVLQKLTEFEEAIGVIFTHVRLLARAFTLRTVGFNHLTLGHNQRMEFLGDSIMQLVATEYLFIHFPDHHEGHLTLLRSSLVNNRTQAKVAEELGMQEYAITNDKTKRPVALRTKTLADLLESFIAALYIDKDLEYVHTFMNVCFFPRLKEFILNQDWNDPKSQLQQCCLTLRTEGKEPDIPLYKTLQTVGPSHARTYTVAVYFKGERIGCGKGPSIQQAEMGAAMDALEKYNFPQMAHQKRFIERKYRQELKEMRWEREHQEREPDETEDIKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":411,"region_id":"DP02463r001","start":390,"term_id":"IDPO:0000002","statement":[{"text":"The final model includes two RIIIDs, dsRBD, and 53% of CED from DROSHA and two G1 helices from DGCR8. The model does not include N-terminal 21 residues, residues 459–521, 668–674, and 712–849 within CED, residues 930–957 in RIIIDa, and C-terminal 32 residues, because their electron densities are unclear or missing.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26748718","version":3,"reference_html":"Structure of Human DROSHA. <i> Kwon SC, Nguyen TA, Choi YG, Jo MH, Hohng S, Kim VN, Woo JS. </i> Cell, 2016","date":"2022-06-28T07:53:21.971Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5B16"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8WYQ5"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T12:16:21.285Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":521,"region_id":"DP02463r002","start":459,"term_id":"IDPO:0000002","statement":[{"text":"The final model includes two RIIIDs, dsRBD, and 53% of CED from DROSHA and two G1 helices from DGCR8. The model does not include N-terminal 21 residues, residues 459–521, 668–674, and 712–849 within CED, residues 930–957 in RIIIDa, and C-terminal 32 residues, because their electron densities are unclear or missing.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26748718","version":3,"reference_html":"Structure of Human DROSHA. <i> Kwon SC, Nguyen TA, Choi YG, Jo MH, Hohng S, Kim VN, Woo JS. </i> Cell, 2016","date":"2022-06-28T07:53:40.272Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5B16"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8WYQ5"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T12:16:35.023Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":849,"region_id":"DP02463r003","start":712,"term_id":"IDPO:0000002","statement":[{"text":"The final model includes two RIIIDs, dsRBD, and 53% of CED from DROSHA and two G1 helices from DGCR8. The model does not include N-terminal 21 residues, residues 459–521, 668–674, and 712–849 within CED, residues 930–957 in RIIIDa, and C-terminal 32 residues, because their electron densities are unclear or missing.","type":"Methods"},{"text":"It is possible that the flexible regions such as PAZ-like domain or MB helix may be located closely to the UG or GHG elements.","type":"Results"},{"text":"The current structure covers most of the conserved regions of DROSHA except for the putative PAZ-like domain (residues 714–849, see below) (Figure 1A), whose electron density was insufficient to build a reliable model probably due to structural flexibility.","type":"Results"}],"curator_id":"fquaglia","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26748718","version":3,"reference_html":"Structure of Human DROSHA. <i> Kwon SC, Nguyen TA, Choi YG, Jo MH, Hohng S, Kim VN, Woo JS. </i> Cell, 2016","date":"2022-06-28T07:54:08.348Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5B16"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8WYQ5"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T12:16:36.223Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":957,"region_id":"DP02463r004","start":930,"term_id":"IDPO:0000002","statement":[{"text":"The final model includes two RIIIDs, dsRBD, and 53% of CED from DROSHA and two G1 helices from DGCR8. The model does not include N-terminal 21 residues, residues 459–521, 668–674, and 712–849 within CED, residues 930–957 in RIIIDa, and C-terminal 32 residues, because their electron densities are unclear or missing.","type":"Methods"},{"text":"It is possible that the flexible regions such as PAZ-like domain or MB helix may be located closely to the UG or GHG elements.","type":"Results"}],"curator_id":"fquaglia","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26748718","version":3,"reference_html":"Structure of Human DROSHA. <i> Kwon SC, Nguyen TA, Choi YG, Jo MH, Hohng S, Kim VN, Woo JS. </i> Cell, 2016","date":"2022-06-28T07:54:19.735Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5B16"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8WYQ5"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T12:16:37.199Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1365,"region_id":"DP02463r005","start":1333,"term_id":"IDPO:0000002","statement":[{"text":"The model does not include N-terminal 21 residues, residues 459–521, 668–674, and 712–849 within CED, residues 930–957 in RIIIDa, and C-terminal 32 residues, because their electron densities are unclear or missing.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26748718","version":3,"reference_html":"Structure of Human DROSHA. <i> Kwon SC, Nguyen TA, Choi YG, Jo MH, Hohng S, Kim VN, Woo JS. </i> Cell, 2016","date":"2022-06-28T07:53:53.153Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5B16"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8WYQ5"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T12:16:38.337Z"}}],"released":"2021_06","length":1374,"ncbi_taxon_id":9606,"date":"2019-12-10T14:29:20.947Z","organism":"Homo sapiens","features":{"gene3D":[{"start":1101,"end":1260,"id":"G3DSA:1.10.1520.10","name":"Ribonuclease III domain"},{"start":1101,"end":1260,"id":"G3DSA:1.10.1520.10","name":"Ribonuclease III domain"}],"pfam":[{"id":"PF00035","name":"Double-stranded RNA binding motif","start":1261,"end":1331},{"id":"PF00636","name":"Ribonuclease III domain","start":1144,"end":1232},{"id":"PF14622","name":"Ribonuclease-III-like","start":963,"end":1070},{"id":"PF26050","name":"Ribonuclease 3, central domain, two antiparallel helical region","start":719,"end":850}]},"disprot_id":"DP02463","regions_counter":5,"dataset":["Cancer-related proteins","RNA-binding proteins","NDDs-related proteins"],"UniParc":"UPI0000163BD8","uniref100":"UniRef100_Q9NRR4","uniref90":"UniRef90_Q9NRR4","uniref50":"UniRef50_Q9NRR4","genes":[{"name":{"value":"DROSHA"},"synonyms":[{"value":"RN3"},{"value":"RNASE3L"},{"value":"RNASEN"}]}],"alphafold_very_low_content":0.30858806404657935,"disorder_content":0.2066957787481805,"disprot_consensus":{"full":[{"start":390,"end":411,"type":"D"},{"start":459,"end":521,"type":"D"},{"start":712,"end":849,"type":"D"},{"start":930,"end":957,"type":"D"},{"start":1333,"end":1365,"type":"D"}],"Structural state":[{"start":390,"end":411,"type":"D"},{"start":459,"end":521,"type":"D"},{"start":712,"end":849,"type":"D"},{"start":930,"end":957,"type":"D"},{"start":1333,"end":1365,"type":"D"}]}},{"acc":"Q12476","name":"Protein AIR2","sequence":"MEKNTAPFVVDTAPTTPPDKLVAPSIEEVNSNPNELRALRGQGRYFGVSDDDKDAIKEAAPKCNNCSQRGHLKKDCPHIICSYCGATDDHYSRHCPKAIQCSKCDEVGHYRSQCPHKWKKVQCTLCKSKKHSKERCPSIWRAYILVDDNEKAKPKVLPFHTIYCYNCGGKGHFGDDCKEKRSSRVPNEDGSAFTGSNLSVELKQEYYRHMNRNSDENEDYQFSESIYDEDPLPRPSHKRHSQNDHSHSGRNKRRASNFHPPPYQKSNVIQPTIRGETLSLNNNISKNSRYQNTKVNVSSISENMYGSRYNPSTYVDNNSISNSSNYRNYNSYQPYRSGTLGKRR","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"creator":"fquaglia","regions":[{"region_id":"DP02464r001","ec_ontology":"ECO","end":159,"term_id":"IDPO:0000002","start":147,"version":2,"statement":[{"text":"Residues 147–159 of Air2p, a portion of the peptide linker between the fourth and fifth zinc knuckles, are disordered and were not modeled.","type":"Results"},{"text":"The linker acts as a spacer, allowing us to delete individual zinc knuckles while not shortening the distance between the remaining ones.","type":"Results"},{"text":"The fourth zinc knuckle (residues 123–136) is tethered to Trf4p via the adjacent linker region but has little direct contact with the surface of Trf4p.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20696927","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3NYB"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structure and function of the polymerase core of TRAMP, a RNA surveillance complex. <i> Hamill S, Wolin SL, Reinisch KM. </i> Proc Natl Acad Sci U S A, 2010","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02464r002","ec_ontology":"ECO","end":159,"term_id":"IDPO:0000033","start":147,"version":3,"statement":[{"text":"Residues 147–159 of Air2p, a portion of the peptide linker between the fourth and fifth zinc knuckles, are disordered and were not modeled.","type":"Results"},{"text":"The linker acts as a spacer, allowing us to delete individual zinc knuckles while not shortening the distance between the remaining ones.","type":"Results"},{"text":"The fourth zinc knuckle (residues 123–136) is tethered to Trf4p via the adjacent linker region but has little direct contact with the surface of Trf4p.","type":"Results"}],"term_name":"flexible linker","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20696927","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3NYB"}],"term_namespace":"Disorder function","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structure and function of the polymerase core of TRAMP, a RNA surveillance complex. <i> Hamill S, Wolin SL, Reinisch KM. </i> Proc Natl Acad Sci U S A, 2010","ec_go":"EXP","disprot_namespace":"Disorder function"},{"region_id":"DP02464r003","ec_ontology":"ECO","end":159,"term_id":"GO:0060090","start":147,"version":3,"statement":[{"text":"Residues 147–159 of Air2p, a portion of the peptide linker between the fourth and fifth zinc knuckles, are disordered and were not modeled.","type":"Results"},{"text":"The linker acts as a spacer, allowing us to delete individual zinc knuckles while not shortening the distance between the remaining ones.","type":"Results"},{"text":"The fourth zinc knuckle (residues 123–136) is tethered to Trf4p via the adjacent linker region but has little direct contact with the surface of Trf4p.","type":"Results"}],"term_name":"molecular adaptor activity","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"20696927","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3NYB"}],"term_namespace":"Molecular function","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structure and function of the polymerase core of TRAMP, a RNA surveillance complex. <i> Hamill S, Wolin SL, Reinisch KM. </i> Proc Natl Acad Sci U S A, 2010","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_12","length":344,"ncbi_taxon_id":559292,"date":"2019-12-10T15:03:09.956Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","features":{"gene3D":[],"pfam":[{"id":"PF00098","name":"Zinc knuckle","start":62,"end":78},{"id":"PF00098","name":"Zinc knuckle","start":100,"end":116},{"id":"PF00098","name":"Zinc knuckle","start":163,"end":179},{"id":"PF21759","name":"AIR2-like, CCHC-type 1 zinc finger 4","start":122,"end":145}]},"disprot_id":"DP02464","regions_counter":3,"dataset":[],"UniParc":"UPI00000530F6","uniref100":"UniRef100_Q12476","uniref90":"UniRef90_Q12476","uniref50":"UniRef50_Q12476","genes":[{"name":{"value":"AIR2"},"olnNames":[{"value":"YDL175C"}]}],"alphafold_very_low_content":0.38953488372093026,"disorder_content":0.0377906976744186,"disprot_consensus":{"full":[{"start":147,"end":159,"type":"D"}],"Structural state":[{"start":147,"end":159,"type":"D"}],"Disorder function":[{"start":147,"end":159,"type":"F"}],"Molecular function":[{"start":147,"end":159,"type":"F"}]}},{"acc":"P07199","name":"Major centromere autoantigen B","sequence":"MGPKRRQLTFREKSRIIQEVEENPDLRKGEIARRFNIPPSTLSTILKNKRAILASERKYGVASTCRKTNKLSPYDKLEGLLIAWFQQIRAAGLPVKGIILKEKALRIAEELGMDDFTASNGWLDRFRRRHGVVSCSGVARARARNAAPRTPAAPASPAAVPSEGSGGSTTGWRAREEQPPSVAEGYASQDVFSATETSLWYDFLPDQAAGLCGGDGRPRQATQRLSVLLCANADGSEKLPPLVAGKSAKPRAGQAGLPCDYTANSKGGVTTQALAKYLKALDTRMAAESRRVLLLAGRLAAQSLDTSGLRHVQLAFFPPGTVHPLERGVVQQVKGHYRQAMLLKAMAALEGQDPSGLQLGLTEALHFVAAAWQAVEPSDIAACFREAGFGGGPNATITTSLKSEGEEEEEEEEEEEEEEGEGEEEEEEGEEEEEEGGEGEELGEEEEVEEEGDVDSDEEEEEDEESSSEGLEAEDWAQGVVEAGGSFGAYGAQEEAQCPTLHFLEGGEDSDSDSEEEDDEEEDDEDEDDDDDEEDGDEVPVPSFGEAMAYFAMVKRYLTSFPIDDRVQSHILHLEHDLVHVTRKNHARQAGVRGLGHQS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":599,"region_id":"DP02465r001","start":583,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The last 16 residues of each CENP-B-(540-599) C terminus, which is the natural C terminus of the full-length CENP-B, are disordered. Therefore, they are not required for dimer formation. This may reflect the flexible nature of the CENP-B C-terminal region, which is rich in glycine residues.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14522975","version":2,"reference_html":"Crystal structure of the human centromere protein B (CENP-B) dimerization domain at 1.65-A resolution. <i> Tawaramoto MS, Park SY, Tanaka Y, Nureki O, Kurumizaka H, Yokoyama S. </i> J Biol Chem, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1UFI"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-26T15:07:42.511Z"}}],"released":"2023_12","length":599,"ncbi_taxon_id":9606,"date":"2019-12-10T15:16:03.696Z","organism":"Homo sapiens","features":{"gene3D":[{"start":539,"end":599,"id":"G3DSA:1.10.287.1090","name":"Dimerisation domain of CENP-B"}],"pfam":[{"id":"PF03184","name":"DDE superfamily endonuclease","start":223,"end":384},{"id":"PF03221","name":"Tc5 transposase DNA-binding domain","start":74,"end":134},{"id":"PF04218","name":"CENP-B N-terminal DNA-binding domain","start":3,"end":55},{"id":"PF09026","name":"Centromere protein B dimerisation domain","start":499,"end":598}]},"disprot_id":"DP02465","regions_counter":3,"dataset":[],"UniParc":"UPI000016A6A2","uniref100":"UniRef100_P07199","uniref90":"UniRef90_P07199","uniref50":"UniRef50_P07199","genes":[{"name":{"value":"CENPB"}}],"alphafold_very_low_content":0.34724540901502504,"disorder_content":0.028380634390651086,"disprot_consensus":{"full":[{"start":583,"end":599,"type":"D"}],"Structural state":[{"start":583,"end":599,"type":"D"}]}},{"acc":"Q12432","name":"Chromatin modification-related protein EAF3","sequence":"MVDLEQEFALGGRCLAFHGPLMYEAKILKIWDPSSKMYTSIPNDKPGGSSQATKEIKPQKLGEDESIPEEIINGKCFFIHYQGWKSSWDEWVGYDRIRAYNEENIAMKKRLANEAKEAKKSLLEQQKKKKLSTSLGGPSNGGKRKGDSRSNASISKSTSQSFLTSSVSGRKSGRSSANSLHPGSSLRSSSDQNGNDDRRRSSSLSPNMLHHIAGYPTPKISLQIPIKLKSVLVDDWEYVTKDKKICRLPADVTVEMVLNKYEHEVSQELESPGSQSQLSEYCAGLKLYFDKCLGNMLLYRLERLQYDELLKKSSKDQKPLVPIRIYGAIHLLRLISVLPELISSTTMDLQSCQLLIKQTEDFLVWLLMHVDEYFNDKDPNRSDDALYVNTSSQYEGVALGM","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":53,"region_id":"DP02466r001","start":44,"term_id":"IDPO:0000002","statement":[{"text":"In the final model, the N-terminal six residues (numbered 1–6) and residues 44–53 were disordered.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18984594","version":2,"reference_html":"Molecular basis of the interaction of Saccharomyces cerevisiae Eaf3 chromo domain with methylated H3K36. <i> Sun B, Hong J, Zhang P, Dong X, Shen X, Lin D, Ding J. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3E9F"},{"db":"PDB","id":"3E9G"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":401,"ncbi_taxon_id":559292,"date":"2019-12-10T16:02:48.291Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","features":{"gene3D":[{"start":216,"end":396,"id":"G3DSA:1.10.274.30","name":"G3DSA:1.10.274.30"}],"pfam":[{"id":"PF05712","name":"MRG","start":216,"end":377},{"id":"PF22732","name":"MSL3 chromodomain-like","start":77,"end":112}]},"disprot_id":"DP02466","regions_counter":1,"dataset":[],"UniParc":"UPI0000052F18","uniref100":"UniRef100_Q12432","uniref90":"UniRef90_Q12432","uniref50":"UniRef50_Q12432","genes":[{"name":{"value":"EAF3"},"orfNames":[{"value":"YP9367.03C"}],"olnNames":[{"value":"YPR023C"}]}],"alphafold_very_low_content":0.24189526184538654,"disorder_content":0.02493765586034913,"disprot_consensus":{"full":[{"start":44,"end":53,"type":"D"}],"Structural state":[{"start":44,"end":53,"type":"D"}]}},{"acc":"P51617","name":"Interleukin-1 receptor-associated kinase 1","sequence":"MAGGPGPGEPAAPGAQHFLYEVPPWVMCRFYKVMDALEPADWCQFAALIVRDQTELRLCERSGQRTASVLWPWINRNARVADLVHILTHLQLLRARDIITAWHPPAPLPSPGTTAPRPSSIPAPAEAEAWSPRKLPSSASTFLSPAFPGSQTHSGPELGLVPSPASLWPPPPSPAPSSTKPGPESSVSLLQGARPFPFCWPLCEISRGTHNFSEELKIGEGGFGCVYRAVMRNTVYAVKRLKENADLEWTAVKQSFLTEVEQLSRFRHPNIVDFAGYCAQNGFYCLVYGFLPNGSLEDRLHCQTQACPPLSWPQRLDILLGTARAIQFLHQDSPSLIHGDIKSSNVLLDERLTPKLGDFGLARFSRFAGSSPSQSSMVARTQTVRGTLAYLPEEYIKTGRLAVDTDTFSFGVVVLETLAGQRAVKTHGARTKYLKDLVEEEAEEAGVALRSTQSTLQAGLAADAWAAPIAMQIYKKHLDPRPGPCPPELGLGLGQLACCCLHRRAKRRPPMTQVYERLEKLQAVVAGVPGHSEAASCIPPSPQENSYVSSTGRAHSGAAPWQPLAAPSGASAQAAEQLQRGPNQPVESDESLGGLSAALRSWHLTPSCPLDPAPLREAGCPQGDTAGESSWGSGPGSRPTAVEGLALGSSASSSSEPPQIIINPARQKMVQKLALYEDGALDSLQLLSSSSLPGLGLEQDRQGPEESDEFQS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":463,"region_id":"DP02467r001","start":449,"term_id":"IDPO:0000002","statement":[{"text":"Three regions are disordered in the structure, residues 243 to 247 in chain A and 244 to 248 in chain B at the loop between β3 and αC, residues 367 to 382 within the activation loop, and residues 449 to 460 in A and 449 to 463 in B at the long insertion between αG and αH (Fig. 3B). Despite being largely disordered, the IRAK1 activation loop is natively phosphorylated at S373, S375, S376, and T381, as shown by liquid chromatography tandem-mass spectrometry (LC/MS/MS) (Fig. S2). It should be noted that the disordered activation loop (residues 367 to 382) situates away from the inhibitor-binding site","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29208712","version":2,"reference_html":"Crystal structure of human IRAK1. <i> Wang L, Qiao Q, Ferrao R, Shen C, Hatcher JM, Buhrlage SJ, Gray NS, Wu H. </i> Proc Natl Acad Sci U S A, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6BFN"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":382,"region_id":"DP02467r002","start":367,"term_id":"IDPO:0000002","statement":[{"text":"Three regions are disordered in the structure, residues 243 to 247 in chain A and 244 to 248 in chain B at the loop between β3 and αC, residues 367 to 382 within the activation loop, and residues 449 to 460 in A and 449 to 463 in B at the long insertion between αG and αH (Fig. 3B). Despite being largely disordered, the IRAK1 activation loop is natively phosphorylated at S373, S375, S376, and T381, as shown by liquid chromatography tandem-mass spectrometry (LC/MS/MS) (Fig. S2). It should be noted that the disordered activation loop (residues 367 to 382) situates away from the inhibitor-binding site","type":"Results"},{"text":"IRAK4 then phosphorylates IRAK1 to first prime its activity, enabling subsequent IRAK1 autophosphorylation in its activation loop to become fully activated","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29208712","version":2,"reference_html":"Crystal structure of human IRAK1. <i> Wang L, Qiao Q, Ferrao R, Shen C, Hatcher JM, Buhrlage SJ, Gray NS, Wu H. </i> Proc Natl Acad Sci U S A, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6BFN"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":382,"region_id":"DP02467r003","start":367,"term_id":"IDPO:0000045","statement":[{"text":"Three regions are disordered in the structure, residues 243 to 247 in chain A and 244 to 248 in chain B at the loop between β3 and αC, residues 367 to 382 within the activation loop, and residues 449 to 460 in A and 449 to 463 in B at the long insertion between αG and αH (Fig. 3B). Despite being largely disordered, the IRAK1 activation loop is natively phosphorylated at S373, S375, S376, and T381, as shown by liquid chromatography tandem-mass spectrometry (LC/MS/MS) (Fig. S2). It should be noted that the disordered activation loop (residues 367 to 382) situates away from the inhibitor-binding site","type":"Results"},{"text":"IRAK4 then phosphorylates IRAK1 to first prime its activity, enabling subsequent IRAK1 autophosphorylation in its activation loop to become fully activated","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29208712","version":2,"reference_html":"Crystal structure of human IRAK1. <i> Wang L, Qiao Q, Ferrao R, Shen C, Hatcher JM, Buhrlage SJ, Gray NS, Wu H. </i> Proc Natl Acad Sci U S A, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"6BFN"}],"term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","length":712,"ncbi_taxon_id":9606,"date":"2019-12-10T17:05:12.262Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":214,"end":514},{"id":"PF00531","name":"Death domain","start":28,"end":102}]},"disprot_id":"DP02467","regions_counter":3,"dataset":[],"UniParc":"UPI0000146573","uniref100":"UniRef100_P51617","uniref90":"UniRef90_P51617","uniref50":"UniRef50_P51617","genes":[{"name":{"value":"IRAK1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6112","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6112"}}]},"synonyms":[{"value":"IRAK"}]}],"alphafold_very_low_content":0.3806179775280899,"disorder_content":0.04353932584269663,"disprot_consensus":{"full":[{"start":367,"end":382,"type":"D"},{"start":449,"end":463,"type":"D"}],"Structural state":[{"start":367,"end":382,"type":"D"},{"start":449,"end":463,"type":"D"}],"Disorder function":[{"start":367,"end":382,"type":"F"}]}},{"acc":"P17480","name":"Nucleolar transcription factor 1","sequence":"MNGEADCPTDLEMAAPKGQDRWSQEDMLTLLECMKNNLPSNDSSKFKTTESHMDWEKVAFKDFSGDMCKLKWVEISNEVRKFRTLTELILDAQEHVKNPYKGKKLKKHPDFPKKPLTPYFRFFMEKRAKYAKLHPEMSNLDLTKILSKKYKELPEKKKMKYIQDFQREKQEFERNLARFREDHPDLIQNAKKSDIPEKPKTPQQLWYTHEKKVYLKVRPDATTKEVKDSLGKQWSQLSDKKRLKWIHKALEQRKEYEEIMRDYIQKHPELNISEEGITKSTLTKAERQLKDKFDGRPTKPPPNSYSLYCAELMANMKDVPSTERMVLCSQQWKLLSQKEKDAYHKKCDQKKKDYEVELLRFLESLPEEEQQRVLGEEKMLNINKKQATSPASKKPAQEGGKGGSEKPKRPVSAMFIFSEEKRRQLQEERPELSESELTRLLARMWNDLSEKKKAKYKAREAALKAQSERKPGGEREERGKLPESPKRAEEIWQQSVIGDYLARFKNDRVKALKAMEMTWNNMEKKEKLMWIKKAAEDQKRYERELSEMRAPPAATNSSKKMKFQGEPKKPPMNGYQKFSQELLSNGELNHLPLKERMVEIGSRWQRISQSQKEHYKKLAEEQQKQYKVHLDLWVKSLSPQDRAAYKEYISNKRKSMTKLRGPNPKSSRTTLQSKSESEEDDEEDEDDEDEDEEEEDDENGDSSEDGGDSSESSSEDESEDGDENEEDDEDEDDDEDDDEDEDNESEGSSSSSSSSGDSSDSDSN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":560,"region_id":"DP02468r001","start":547,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The first two N-terminal residues,including the first plasmid-encoded residue, and the C-terminal residues 547–560 are disordered.","type":"Results"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17505112","version":2,"reference_html":"Structure of human upstream binding factor HMG box 5 and site for binding of the cell-cycle regulatory factor TAF1. <i> Rong H, Li Y, Shi X, Zhang X, Gao Y, Dai H, Teng M, Niu L, Liu Q, Hao Q. </i> Acta Crystallogr D Biol Crystallogr, 2007","date":"2022-08-05T14:15:41.130Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"2HDZ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-08T17:25:24.887Z"}}],"released":"2023_06","length":764,"ncbi_taxon_id":9606,"date":"2019-12-11T10:45:04.442Z","organism":"Homo sapiens","features":{"gene3D":[{"start":555,"end":659,"id":"G3DSA:1.10.30.10","name":"High mobility group box domain"},{"start":555,"end":659,"id":"G3DSA:1.10.30.10","name":"High mobility group box domain"},{"start":555,"end":659,"id":"G3DSA:1.10.30.10","name":"High mobility group box domain"},{"start":555,"end":659,"id":"G3DSA:1.10.30.10","name":"High mobility group box domain"},{"start":555,"end":659,"id":"G3DSA:1.10.30.10","name":"High mobility group box domain"},{"start":555,"end":659,"id":"G3DSA:1.10.30.10","name":"High mobility group box domain"}],"pfam":[{"id":"PF00505","name":"HMG (high mobility group) box","start":112,"end":179},{"id":"PF00505","name":"HMG (high mobility group) box","start":197,"end":263},{"id":"PF00505","name":"HMG (high mobility group) box","start":407,"end":468},{"id":"PF09011","name":"HMG-box domain","start":299,"end":357},{"id":"PF14887","name":"HMG (high mobility group) box 5","start":479,"end":563}]},"disprot_id":"DP02468","regions_counter":2,"dataset":["NDDs-related proteins"],"UniParc":"UPI000013797C","uniref100":"UniRef100_P17480","uniref90":"UniRef90_P17480","uniref50":"UniRef50_P17480","genes":[{"name":{"value":"UBTF"},"synonyms":[{"value":"UBF"},{"value":"UBF1"}]}],"alphafold_very_low_content":0.2094240837696335,"disorder_content":0.01832460732984293,"disprot_consensus":{"full":[{"start":547,"end":560,"type":"D"}],"Structural state":[{"start":547,"end":560,"type":"D"}]}},{"acc":"Q12495","name":"Chromatin assembly factor 1 subunit p90","sequence":"MEQHLKSIPLQDDTKKKGILSFFQNTTTVKSNKFLTKEKDVITLDDPKEDVSGPMIETVKQETMKSINKECADEMKTTPKKANAEDKLLCYKNSPIQSTKYDRNTNKQVPNGNIIAIETKSRSSSPCSKRELSSSKKEEAKREKELKKQQRAEEKHRKELLRQEEKKKKELKVEEERQRRAELKKQKEEEKRRKEEARLEAKRRKEEERLKKEEEIRLKEEAKERAQSRIGNFFKKLSDSNTPVVEKSDYEKFFLPFYAKDGVRVSNKWKLTKVELEGSKRKIDDELLNSKDKTSSDDLLNWLQSRRLPRGHKIKRKAVDVLQQMPLKEKTDDELQSLLAQVPHKYIKFYENVRPPFIGTYSMDFTLPPNDPFSTKGTGFNYDYDSDVEWVNEEEEGEVDNLESGEEEEEEEDDEDVPSEGEFDGFLDSEENSDLDGLPCAKRKFVGPLIPTICLKSNFENLSEENKRYLQQLKAEVIIETDGPIDPFKEPKTSSLPSKRSNSDLQAQTASQSQSPEKKQKAMITDPMDLLRLFDGVQDSTFSLGTVTEIAQKNLPQYNKQTIKNTIKEYAIRSSGKGDLPRKWVIKDAQNWENLRANANMPTPSL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":519,"region_id":"DP02470r001","start":457,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Even though the entire 457–606 protein was present in the crystal (Figure 5A and data not shown), only amino acids 520–600 were visible in our electron density, and the 'wing' (576–581) was disordered.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27690308","version":2,"reference_html":"The Cac1 subunit of histone chaperone CAF-1 organizes CAF-1-H3/H4 architecture and tetramerizes histones. <i> Liu WH, Roemer SC, Zhou Y, Shen ZJ, Dennehey BK, Balsbaugh JL, Liddle JC, Nemkov T, Ahn NG, Hansen KC, Tyler JK, Churchill ME. </i> Elife, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5JBM"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-02T15:53:46.282Z"}}],"released":"2023_12","length":606,"ncbi_taxon_id":559292,"date":"2019-12-11T11:34:19.345Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","features":{"gene3D":[],"pfam":[{"id":"PF11600","name":"Chromatin assembly factor 1 complex p150 subunit, acidic region","start":129,"end":263},{"id":"PF12253","name":"Chromatin assembly factor 1 subunit A dimerization domain","start":345,"end":416},{"id":"PF21796","name":"Chromatin assembly factor 1 subunit Cac1, C-terminal domain","start":530,"end":586}]},"disprot_id":"DP02470","regions_counter":1,"dataset":[],"UniParc":"UPI0000126D75","uniref100":"UniRef100_Q12495","uniref90":"UniRef90_Q12495","uniref50":"UniRef50_Q12495","genes":[{"name":{"value":"RLF2"},"synonyms":[{"value":"CAC1"}],"orfNames":[{"value":"YP9531.12"}],"olnNames":[{"value":"YPR018W"}]}],"alphafold_very_low_content":0.30528052805280526,"disorder_content":0.10396039603960396,"disprot_consensus":{"full":[{"start":457,"end":519,"type":"D"}],"Structural state":[{"start":457,"end":519,"type":"D"}]}},{"acc":"Q96G97","name":"Seipin","sequence":"MVNDPPVPALLWAQEVGQVLAGRARRLLLQFGVLFCTILLLLWVSVFLYGSFYYSYMPTVSHLSPVHFYYRTDCDSSTTSLCSFPVANVSLTKGGRDRVLMYGQPYRVTLELELPESPVNQDLGMFLVTISCYTRGGRIISTSSRSVMLHYRSDLLQMLDTLVFSSLLLFGFAEQKQLLEVELYADYRENSYVPTTGAIIEIHSKRIQLYGAYLRIHAHFTGLRYLLYNFPMTCAFIGVASNFTFLSVIVLFSYMQWVWGGIWPRHRFSLQVNIRKRDNSRKEVQRRISAHQPGPEGQEESTPQSDVTEDGESPEDPSGTEGQLSEEEKPDQQPLSGEEELEPEASDGSGSWEDAALLTEANLPAPAPASASAPVLETLGSSEPAGGALRQRPTCSSS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":60,"region_id":"DP02471r001","start":2,"term_id":"IDPO:0000002","statement":[{"text":"The typical transmembrane region is invisible in the EM map at the first sight. A close examination reveals that the densities of wheel outer ring are discontinuous, indicating that this region represents the TM region, which is invisible due to its flexibility or the C11 symmetry","type":"Results"},{"text":"The atomic model with 159 amino acids (149 amino acids were assigned side chain) was built for this region of each protomer according to the lumenal domain sequence of human SEIPIN. The final model is an undecamer with the lumenal domain alone, whose diameter is 160 Å","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30293840","version":2,"reference_html":"Human SEIPIN Binds Anionic Phospholipids. <i> Yan R, Qian H, Lukmantara I, Gao M, Du X, Yan N, Yang H. </i> Dev Cell, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6DS5"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-05T17:29:07.849Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":398,"region_id":"DP02471r002","start":220,"term_id":"IDPO:0000002","statement":[{"text":"The typical transmembrane region is invisible in the EM map at the first sight. A close examination reveals that the densities of wheel outer ring are discontinuous, indicating that this region represents the TM region, which is invisible due to its flexibility or the C11 symmetry","type":"Results"},{"text":"The atomic model with 159 amino acids (149 amino acids were assigned side chain) was built for this region of each protomer according to the lumenal domain sequence of human SEIPIN. The final model is an undecamer with the lumenal domain alone, whose diameter is 160 Å","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30293840","version":2,"reference_html":"Human SEIPIN Binds Anionic Phospholipids. <i> Yan R, Qian H, Lukmantara I, Gao M, Du X, Yan N, Yang H. </i> Dev Cell, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6DS5"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-05T17:29:08.044Z"}}],"released":"2021_06","length":398,"ncbi_taxon_id":9606,"date":"2019-12-11T11:51:08.373Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF06775","name":"Putative adipose-regulatory protein (Seipin)","start":40,"end":243}]},"disprot_id":"DP02471","regions_counter":2,"dataset":["NDDs-related proteins"],"UniParc":"UPI0000070140","uniref100":"UniRef100_Q96G97","uniref90":"UniRef90_Q96G97","uniref50":"UniRef50_Q96G97","genes":[{"name":{"value":"BSCL2"}}],"alphafold_very_low_content":0.28391959798994976,"disorder_content":0.5979899497487438,"disprot_consensus":{"full":[{"start":2,"end":60,"type":"D"},{"start":220,"end":398,"type":"D"}],"Structural state":[{"start":2,"end":60,"type":"D"},{"start":220,"end":398,"type":"D"}]}},{"acc":"Q3U182","name":"CREB-regulated transcription coactivator 2","sequence":"MATSGANGPGSATASASNPRKFSEKIALQKQRQAEETAAFEEVMMDIGSTRLQAQKLRLAYTRSSHYGGSLPNVNQIGCGLAEFQSPLHSPLDSSRSTRHHGLVERVQRDARRMVSPLRRYPRHIDSSPYSPAYLSPPPESGWRRMMPWGNLPAEKGQLFRLPSALNRTSSDSALHTSVMNPNPQDTYPGPTPPSVLPSRRGGGFLDGEMDAKVPAIEENVVDDKHLLKPWDAKKLSSSSSRPRSCEVPGINIFPSPDQPANVPVLPPAMNTGGSLPDLTNLHFPPPLPTPLDPEETVYPSLSGGNSTTNLTHTMTHLGISGGLGLGPSYDVPGLHSPLSHPSLQSSLSNPNLQASLSSPQPQLQGSHSHPSLPASSLAHHALPTTSLGHPSLSAPALSSSSSSSSTSSPVLSAPPYPASTPGASPRHRRVPLSPLSLPAGPADARRSQQQLPKQFSPTMSPTLSSITQGVPLDTSKLPTDQRLPPYPYSPPSLVIPTHPPTPKSLQQLPSQACLVQPSGGQPPGRQPHYGALYPPGSSGHGQQPYHRPINDFSLGNLEQFNMESPSTSLVLDPPAFSEGPGFLGSEGSMSGPQDPHVLNHQNLTHCSRHGSGPNIILTGDSSPGFSKEIAAALAGVPGFEVSASGLELGLGLEDELRMEPLGLEGLTMLSDPCALLPDPAVEDSFRSDRLQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":14,"region_id":"DP02472r001","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"CRTC2 residues 1–14 and 59–80 and CREB residues 283–284 and 338–341 are included in the expression construct, but are disordered in the structure.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29733854","version":2,"reference_html":"Structural Insights into the CRTC2-CREB Complex Assembly on CRE. <i> Song Y, Zhai L, Valencia Swain J, Chen Y, Wang P, Chen L, Liu Y, Xiang S. </i> J Mol Biol, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5ZKO"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-07T15:46:41.665Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":80,"region_id":"DP02472r002","start":59,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"CRTC2 residues 1–14 and 59–80 and CREB residues 283–284 and 338–341 are included in the expression construct, but are disordered in the structure.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29733854","version":2,"reference_html":"Structural Insights into the CRTC2-CREB Complex Assembly on CRE. <i> Song Y, Zhai L, Valencia Swain J, Chen Y, Wang P, Chen L, Liu Y, Xiang S. </i> J Mol Biol, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5ZKO"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-07T15:46:41.254Z"}}],"released":"2023_12","length":692,"ncbi_taxon_id":10090,"date":"2019-12-11T12:20:17.543Z","organism":"Mus musculus","features":{"gene3D":[],"pfam":[{"id":"PF12884","name":"Transducer of regulated CREB activity, N terminus","start":18,"end":72},{"id":"PF12885","name":"Transducer of regulated CREB activity middle domain","start":168,"end":322},{"id":"PF12886","name":"Transducer of regulated CREB activity, C terminus","start":614,"end":691}]},"disprot_id":"DP02472","regions_counter":2,"dataset":[],"UniParc":"UPI00005ACFD0","uniref100":"UniRef100_Q3U182","uniref90":"UniRef90_Q3U182","uniref50":"UniRef50_Q3U182","genes":[{"name":{"value":"Crtc2"},"synonyms":[{"value":"Torc2"}]}],"alphafold_very_low_content":0.7196531791907514,"disorder_content":0.05202312138728324,"disprot_consensus":{"full":[{"start":1,"end":14,"type":"D"},{"start":59,"end":80,"type":"D"}],"Structural state":[{"start":1,"end":14,"type":"D"},{"start":59,"end":80,"type":"D"}]}},{"acc":"Q15642","name":"Cdc42-interacting protein 4","sequence":"MDWGTELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRPAKDDPESKFSQQQSFVQILQEVNDFAGQRELVAENLSVRVCLELTKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQDINATKADVEKAKQQAHLRSHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELEVVPIIAKCLEGMKVAANAVDPKNDSHVLIELHKSGFARPGDVEFEDFSQPMNRAPSDSSLGTPSDGRPELRGPGRSRTKRWPFGKKNKPRPPPLSPLGGPVPSALPNGPPSPRSGRDPLAILSEISKSVKPRLASFRSLRGSRGTVVTEDFSHLPPEQQRKRLQQQLEERSRELQKEVDQREALKKMKDVYEKTPQMGDPASLEPQIAETLSNIERLKLEVQKYEAWLAEAESRVLSNRGDSLSRHARPPDPPASAPPDSSSNSASQDTKESSEEPPSEESQDTPIYTEFDEDFEEEPTSPIGHCVAIYHFEGSSEGTISMAEGEDLSLMEEDKGDGWTRVRRKEGGEGYVPTSYLRVTLN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":303,"region_id":"DP02473r001","start":289,"term_id":"IDPO:0000002","statement":[{"text":"The models were built for residues 10–56 and 64–288 for EFCΔNCIP4 and residues 1–56 and 64–288 for EFCFBP17. The rest of the residues could not be modeled due to poor/disordered electron densities.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17512409","version":2,"reference_html":"Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis. <i> Shimada A, Niwa H, Tsujita K, Suetsugu S, Nitta K, Hanawa-Suetsugu K, Akasaka R, Nishino Y, Toyama M, Chen L, Liu ZJ, Wang BC, Yamamoto M, Terada T, Miyazawa A, Tanaka A, Sugano S, Shirouzu M, Nagayama K, Takenawa T, Yokoyama S. </i> Cell, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2EFK"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":601,"ncbi_taxon_id":9606,"date":"2019-12-11T12:36:26.255Z","organism":"Homo sapiens","features":{"gene3D":[{"start":1,"end":300,"id":"G3DSA:1.20.1270.60","name":"Arfaptin homology (AH) domain/BAR domain"}],"pfam":[{"id":"PF00018","name":"SH3 domain","start":546,"end":593},{"id":"PF00611","name":"Fes/CIP4, and EFC/F-BAR homology domain","start":10,"end":88},{"id":"PF25610","name":"TOCA family HR1 domain","start":388,"end":474}]},"disprot_id":"DP02473","regions_counter":1,"dataset":[],"UniParc":"UPI000016B11F","uniref100":"UniRef100_Q15642","uniref90":"UniRef90_Q15642","uniref50":"UniRef50_Q15642","genes":[{"name":{"value":"TRIP10"},"synonyms":[{"value":"CIP4"},{"value":"STOT"},{"value":"STP"}]}],"alphafold_very_low_content":0.24792013311148087,"disorder_content":0.024958402662229616,"disprot_consensus":{"full":[{"start":289,"end":303,"type":"D"}],"Structural state":[{"start":289,"end":303,"type":"D"}]}},{"acc":"Q12000","name":"Translation machinery-associated protein 46","sequence":"MPPKKGKQAQAAGKKKDNVDKTFGMKNKNRSTKVQKYIKQVQSQSDPKKEEMRLKKLEEKKRREAEEAERRALFNPVADQRVRAGVDPKSMVCALFKLGNCNKGAKCKFSHDLNVGRRMEKKDLYQDTRSEKENDTMDNWDEEKLRKVILSKHGNPKTTTDKVCKYFIEAVENGKYGWFWICPNGGDKCMYRHSLPEGFVLKTNEQKRLERESLEKQPKITLEEFIETERGKLDKSKLTPITIANFAQWKKDHVIAKINAEKKLSSKRKPTGREIILKMSAENKSFETDNADMPDDVTQGSAWDLTEFTDALKKADHQDDGGIKDYGDGSNPTFDIKKANSATLA","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":319,"region_id":"DP02474r001","start":283,"term_id":"IDPO:0000002","statement":[{"text":"This included 17 groups comprising of Rbg1 (chain A 2–45, 53–125/131–174/233–299, 175–232, 300–369; chain B 2–53, 54–91/98–125/133–174/233–299, 175–232, 300–369) and Tma46 (chain C 214–240, 241–267, 268–282, 302–313, 314–338; chain D 214–240, 241–267, 268–282, 320–336).","type":"Methods"},{"text":"Positions are referred to chain D","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23002146","version":2,"reference_html":"Rbg1-Tma46 dimer structure reveals new functional domains and their role in polysome recruitment. <i> Francis SM, Gas ME, Daugeron MC, Bravo J, Séraphin B. </i> Nucleic Acids Res, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4A9A"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":345,"ncbi_taxon_id":559292,"date":"2019-12-11T12:49:34.742Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","features":{"gene3D":[],"pfam":[{"id":"PF16543","name":"DRG Family Regulatory Proteins, Tma46","start":219,"end":309}]},"disprot_id":"DP02474","regions_counter":1,"dataset":[],"UniParc":"UPI000006C497","uniref100":"UniRef100_Q12000","uniref90":"UniRef90_Q12000","uniref50":"UniRef50_Q12000","genes":[{"name":{"value":"TMA46"},"synonyms":[{"value":"DFRP1"}],"orfNames":[{"value":"YOR3160w"}],"olnNames":[{"value":"YOR091W"}]}],"alphafold_very_low_content":0.04927536231884058,"disorder_content":0.1072463768115942,"disprot_consensus":{"full":[{"start":283,"end":319,"type":"D"}],"Structural state":[{"start":283,"end":319,"type":"D"}]}},{"acc":"Q86UE8","name":"Serine/threonine-protein kinase tousled-like 2","sequence":"MMEELHSLDPRRQELLEARFTGVGVSKGPLNSESSNQSLCSVGSLSDKEVETPEKKQNDQRNRKRKAEPYETSQGKGTPRGHKISDYFEFAGGSAPGTSPGRSVPPVARSSPQHSLSNPLPRRVEQPLYGLDGSAAKEATEEQSALPTLMSVMLAKPRLDTEQLAQRGAGLCFTFVSAQQNSPSSTGSGNTEHSCSSQKQISIQHRQTQSDLTIEKISALENSKNSDLEKKEGRIDDLLRANCDLRRQIDEQQKMLEKYKERLNRCVTMSKKLLIEKSKQEKMACRDKSMQDRLRLGHFTTVRHGASFTEQWTDGYAFQNLIKQQERINSQREEIERQRKMLAKRKPPAMGQAPPATNEQKQRKSKTNGAENETPSSGNTELKDTAPALGAHSLLRLTLAEYHEQEEIFKLRLGHLKKEEAEIQAELERLERVRNLHIRELKRIHNEDNSQFKDHPTLNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKPPIIHYDLKPGNILLVNGTACGEIKITDFGLSKIMDDDSYNSVDGMELTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQENTILKATEVQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLLPHIRKSVSTSSPAGAAIASTSGASNNSSSN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":200,"region_id":"DP02475r001","reference_id":"29955062","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The first 200 amino acids of the N-terminus are predominantly disordered and are predicted to contain a nuclear localization signal (NLS).","type":"Results"}],"curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"author statement used in manual assertion","version":4,"reference_html":"Molecular basis of Tousled-Like Kinase 2 activation. <i> Mortuza GB, Hermida D, Pedersen AK, Segura-Bayona S, López-Méndez B, Redondo P, Rüther P, Pozdnyakova I, Garrote AM, Muñoz IG, Villamor-Payà M, Jauset C, Olsen JV, Stracker TH, Montoya G. </i> Nat Commun, 2018","date":"2023-05-04T20:38:13.414Z","reference_source":"pmid","ec_id":"ECO:0000302","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Biological process","ec_ontology":"ECO","end":190,"region_id":"DP02475r002","reference_id":"29955062","start":1,"term_id":"GO:0051647","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"We next examined the subcellular localization of these mutants and found that with the exception of the [increment]N-TLK2 mutant that contains the putative NLS, all of the mutants showed nuclear localization (Fig. 1f).","type":"Results"},{"text":"Cytoplasmic localization of the [increment]N-TLK2 mutant confirms the presence of the NLS in the N-terminus of the protein.","type":"Figure"}],"curator_id":"vnugnes","released":"2023_06","term_ontology":"GO","curator_name":"Victoria Nugnes","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","version":5,"reference_html":"Molecular basis of Tousled-Like Kinase 2 activation. <i> Mortuza GB, Hermida D, Pedersen AK, Segura-Bayona S, López-Méndez B, Redondo P, Rüther P, Pozdnyakova I, Garrote AM, Muñoz IG, Villamor-Payà M, Jauset C, Olsen JV, Stracker TH, Montoya G. </i> Nat Commun, 2018","date":"2023-05-04T20:53:52.233Z","reference_source":"pmid","ec_id":"ECO:0007089","term_name":"nucleus localization","ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which the nucleus is transported to, and/or maintained in, a specific location within the cell.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":false,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1-Asn190del","start":null,"end":null,"position":null},{"term_id":"MI:0988","term_name":"STREP","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}]}],"released":"2020_06","length":772,"ncbi_taxon_id":9606,"date":"2019-12-18T10:40:59.374Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":464,"end":741}]},"disprot_id":"DP02475","regions_counter":2,"dataset":["NDDs-related proteins"],"UniParc":"UPI000000DAC1","uniref100":"UniRef100_Q86UE8","uniref90":"UniRef90_Q86UE8","uniref50":"UniRef50_Q86UE8","genes":[{"name":{"value":"TLK2"}}],"alphafold_very_low_content":0.3601036269430052,"disorder_content":0.25906735751295334,"disprot_consensus":{"full":[{"start":1,"end":200,"type":"D"}],"Structural state":[{"start":1,"end":200,"type":"D"}],"Biological process":[{"start":1,"end":190,"type":"F"}]}},{"acc":"P36106","name":"Transcription factor BYE1","sequence":"MSVRTSSRSNKGQNKYIEYLLQEETEAPKKKRTKKKVDSAIEKNKKSDSSQEPRKDTENVRTDEVDEADEGYVRCLCGANNENYDAAEYSHGDMVQCDGCDTWQHIKCMTDGKDTIDGLMSEDSKYYCELCDPSLYAHLETSKEAEVSEDEDYHDDVYKPVNDHDDNDADVFLDEESPRKRKRSPDSAKGIHIKSKQVKKSNGSKKRNKSIDAAKSDTAENEMPTRKDFESEKEHKLRYNAEKMFSTLFSKFIVPETIEAKLYELPDGKDVISISQEFAHNLEEELYKACLNVEFGTLDKIYTEKVRSLYSNLKDKKNLELKAHVVEGKLPLNKLVNMNASELANPDLQEFKEKRDKIILENFIVEVPDKPMYVKTHKGDELIEDIAEPQEDILYSKDSIRLHNIDSIDSDKSKIEQTHAISKEPSPSTIINEESLNCAFLYPGLGLEFTGYLNYIGASQKLRRDIFKEAIGDGKLYVEGRLPTTTAAPYLKEISCSRAILVYQLFPSNDSESKTTFADVVDSLENKGRIAGIKPKTRYEKDFYIVPSKGGEIPEILKDILGSHNDERSERFSRMKSDERTLFAFVVVKQEFIH","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":231,"region_id":"DP02476r001","reference_id":"24003114","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"We also included models of the flexible Bye1 SPOC and PHD domains, with the latter positioned on the H3 tail emerging from the core nucleosome particle (Fig. 5C). Although the trajectory of the H3 tail is unclear and although the linkers between the Bye1 domains are flexible, the resulting model explained the position of the ChIP peak with high H3K4me3 occupancy.","type":"Results"},{"text":"In Bye1, the central TFIIS-like domain (TLD, residues 232–365) is flanked by an N-terminal plant homeo domain (PHD) (residues 74–134) and a C-terminal Spen paralogue and orthologue C-terminal (SPOC) domain (residues 447–547)","type":"Article"},{"text":"flexible Bye1 PHD domain position: 74-134","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structures of RNA polymerase II complexes with Bye1, a chromatin-binding PHF3/DIDO homologue. <i> Kinkelin K, Wozniak GG, Rothbart SB, Lidschreiber M, Strahl BD, Cramer P. </i> Proc Natl Acad Sci U S A, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4BY7"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":134,"region_id":"DP02476r002","reference_id":"24003114","start":74,"term_id":"GO:0005515","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"We also included models of the flexible Bye1 SPOC and PHD domains, with the latter positioned on the H3 tail emerging from the core nucleosome particle (Fig. 5C). Although the trajectory of the H3 tail is unclear and although the linkers between the Bye1 domains are flexible, the resulting model explained the position of the ChIP peak with high H3K4me3 occupancy.","type":"Results"},{"text":"In Bye1, the central TFIIS-like domain (TLD, residues 232–365) is flanked by an N-terminal plant homeo domain (PHD) (residues 74–134) and a C-terminal Spen paralogue and orthologue C-terminal (SPOC) domain (residues 447–547)","type":"Article"},{"text":"Bye1 PHD domain contributes to chromatin association by binding trimethylated H3K4 peptides","type":"Results"},{"text":"The Bye1 PHD domain and full-length Bye1 bound specifically to H3K4me3 peptides (Fig. 4A). The high correlation between arrays probed with full-length Bye1 and the isolated PHD domain indicated that the histone-binding potential of Bye1 is harbored within its PHD domain","type":"Results"},{"text":"Additional functional data in vitro and in vivo indicate that Bye1 occupies active genes in their 5′-region and can bind to histone H3 tails with PTMs of active transcription using its PHD domain.","type":"Discussion"},{"text":"the flexible PHD domain is involved in histone-binding","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"x-ray crystallography evidence used in manual assertion","version":4,"reference_html":"Structures of RNA polymerase II complexes with Bye1, a chromatin-binding PHF3/DIDO homologue. <i> Kinkelin K, Wozniak GG, Rothbart SB, Lidschreiber M, Strahl BD, Cramer P. </i> Proc Natl Acad Sci U S A, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4BY7"}],"term_name":"protein binding","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":232,"region_id":"DP02476r004","reference_id":"24003114","start":134,"term_id":"IDPO:0000033","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"We also included models of the flexible Bye1 SPOC and PHD domains, with the latter positioned on the H3 tail emerging from the core nucleosome particle (Fig. 5C). Although the trajectory of the H3 tail is unclear and although the linkers between the Bye1 domains are flexible, the resulting model explained the position of the ChIP peak with high H3K4me3 occupancy.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"x-ray crystallography evidence used in manual assertion","version":4,"reference_html":"Structures of RNA polymerase II complexes with Bye1, a chromatin-binding PHF3/DIDO homologue. <i> Kinkelin K, Wozniak GG, Rothbart SB, Lidschreiber M, Strahl BD, Cramer P. </i> Proc Natl Acad Sci U S A, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4BY7"}],"term_name":"flexible linker","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":447,"region_id":"DP02476r005","reference_id":"24003114","start":366,"term_id":"IDPO:0000033","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"We also included models of the flexible Bye1 SPOC and PHD domains, with the latter positioned on the H3 tail emerging from the core nucleosome particle (Fig. 5C). Although the trajectory of the H3 tail is unclear and although the linkers between the Bye1 domains are flexible, the resulting model explained the position of the ChIP peak with high H3K4me3 occupancy.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"x-ray crystallography evidence used in manual assertion","version":4,"reference_html":"Structures of RNA polymerase II complexes with Bye1, a chromatin-binding PHF3/DIDO homologue. <i> Kinkelin K, Wozniak GG, Rothbart SB, Lidschreiber M, Strahl BD, Cramer P. </i> Proc Natl Acad Sci U S A, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4BY7"}],"term_name":"flexible linker","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":594,"region_id":"DP02476r007","reference_id":"24003114","start":366,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"We also included models of the flexible Bye1 SPOC and PHD domains, with the latter positioned on the H3 tail emerging from the core nucleosome particle (Fig. 5C). Although the trajectory of the H3 tail is unclear and although the linkers between the Bye1 domains are flexible, the resulting model explained the position of the ChIP peak with high H3K4me3 occupancy.","type":"Results"},{"text":"flexible Bye1 SPOC domain position: 447-547","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structures of RNA polymerase II complexes with Bye1, a chromatin-binding PHF3/DIDO homologue. <i> Kinkelin K, Wozniak GG, Rothbart SB, Lidschreiber M, Strahl BD, Cramer P. </i> Proc Natl Acad Sci U S A, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4BY7"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":594,"ncbi_taxon_id":559292,"date":"2019-12-18T11:18:48.768Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","features":{"gene3D":[{"start":59,"end":137,"id":"G3DSA:3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":225,"end":370,"id":"G3DSA:1.10.472.30","name":"Transcription elongation factor S-II, central domain"}],"pfam":[{"id":"PF00628","name":"PHD-finger","start":89,"end":131},{"id":"PF07500","name":"Transcription factor S-II (TFIIS), central domain","start":237,"end":357},{"id":"PF07744","name":"SPOC domain","start":437,"end":588}]},"disprot_id":"DP02476","regions_counter":7,"dataset":[],"UniParc":"UPI000013B6A7","uniref100":"UniRef100_P36106","uniref90":"UniRef90_P36106","uniref50":"UniRef50_P36106","genes":[{"name":{"value":"BYE1"},"orfNames":[{"value":"YKL150"}],"olnNames":[{"value":"YKL005C"}]}],"alphafold_very_low_content":0.3501683501683502,"disorder_content":0.7744107744107744,"disprot_consensus":{"full":[{"start":1,"end":231,"type":"D"},{"start":232,"end":232,"type":"F"},{"start":366,"end":594,"type":"D"}],"Structural state":[{"start":1,"end":231,"type":"D"},{"start":366,"end":594,"type":"D"}],"Molecular function":[{"start":74,"end":134,"type":"F"}],"Disorder function":[{"start":134,"end":232,"type":"F"},{"start":366,"end":447,"type":"F"}]}},{"acc":"Q01970","name":"1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3","sequence":"MAGAQPGVHALQLEPPTVVETLRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNMEVDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDARLEEKLMTVVSGPDPVNTVFLNFMAVQDDTAKVWSEELFKLAMNILAQNASRNTFLRKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYLGGEENGILPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKRHRPSAGGPDSAGRKRPLEQSNSALSESSAATEPSSPQLGSPSSDSCPGLSNGEEVGLEKPSLEPQKSLGDEGLNRGPYVLGPADREDEEEDEEEEEQTDPKKPTTDEGTASSEVNATEEMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVIVDGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEPFDFPKVVLPTLASLRIAAFEEGGKFVGHRILPVSAIRSGYHYVCLRNEANQPLCLPALLIYTEASDYIPDDHQDYAEALINPIKHVSLMDQRARQLAALIGESEAQAGQETCQDTQSQQLGSQPSSNPTPSPLDASPRRPPGPTTSPASTSLSSPGQRDDLIASILSEVAPTPLDELRGHKALVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRLRPGALGGAADVEDTKEGEDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQFKRLKEMNEREKKELQKILDRKRHNSISEAKMRDKHKKEAELTEINRRHITESVNSIRRLEEAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQEIRRSLLGEMPEGLGDGPLVACASNGHAPGSSGHLSGADSESQEENTQL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":572,"region_id":"DP02477r001","reference_id":"23377541","start":471,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Residues 471–572 correspond to a region of the X-Y linker that has low sequence homology and is typically poorly ordered","type":"Methods"},{"text":"separates a triose phosphate isomerase (TIM) barrel-like catalytic domain into X and Y halves","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Full-length Gα(q)-phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil domain. <i> Lyon AM, Dutta S, Boguth CA, Skiniotis G, Tesmer JJ. </i> Nat Struct Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4GNK"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":572,"region_id":"DP02477r002","reference_id":"23377541","start":471,"term_id":"IDPO:0000033","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Residues 471–572 correspond to a region of the X-Y linker that has low sequence homology and is typically poorly ordered","type":"Methods"},{"text":"separates a triose phosphate isomerase (TIM) barrel-like catalytic domain into X and Y halves","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"x-ray crystallography evidence used in manual assertion","version":4,"reference_html":"Full-length Gα(q)-phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil domain. <i> Lyon AM, Dutta S, Boguth CA, Skiniotis G, Tesmer JJ. </i> Nat Struct Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4GNK"}],"term_name":"flexible linker","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":933,"region_id":"DP02477r003","reference_id":"23377541","start":883,"term_id":"IDPO:0000033","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The CTD linker (residues 883–933) is not observed in the structure","type":"Results"},{"text":"The CTD Linker Is Required for Gαq Activation","type":"Results"},{"text":"Because the sequence of the CTD linker is not conserved among PLCβ isozymes, its length and/or flexibility seems to be required for the proximal and distal CTDs to make all the interactions necessary for activation by Gαq.","type":"Results"},{"text":"Furthermore, deletion of the CTD linker leads to complete loss of Gαq activation in our assays","type":"Discussion"},{"text":"PLCβ also has a ~400 amino acid C-terminal extension to the catalytic core that contains the proximal and distal C-terminal domains (CTDs) separated by a non-conserved, low complexity linker of variable length","type":"Article"},{"text":"The distal (purple) and proximal CTDs are connected by the disordered CTD linker","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"x-ray crystallography evidence used in manual assertion","version":4,"reference_html":"Full-length Gα(q)-phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil domain. <i> Lyon AM, Dutta S, Boguth CA, Skiniotis G, Tesmer JJ. </i> Nat Struct Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4GNK"}],"term_name":"flexible linker","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":933,"region_id":"DP02477r004","reference_id":"23377541","start":883,"term_id":"GO:0140677","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The CTD linker (residues 883–933) is not observed in the structure","type":"Results"},{"text":"The CTD Linker Is Required for Gαq Activation","type":"Results"},{"text":"Because the sequence of the CTD linker is not conserved among PLCβ isozymes, its length and/or flexibility seems to be required for the proximal and distal CTDs to make all the interactions necessary for activation by Gαq.","type":"Results"},{"text":"Furthermore, deletion of the CTD linker leads to complete loss of Gαq activation in our assays","type":"Discussion"},{"text":"PLCβ also has a ~400 amino acid C-terminal extension to the catalytic core that contains the proximal and distal C-terminal domains (CTDs) separated by a non-conserved, low complexity linker of variable length","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"x-ray crystallography evidence used in manual assertion","version":4,"reference_html":"Full-length Gα(q)-phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil domain. <i> Lyon AM, Dutta S, Boguth CA, Skiniotis G, Tesmer JJ. </i> Nat Struct Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4GNK"}],"term_name":"molecular function activator activity","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1234,"region_id":"DP02477r005","reference_id":"23377541","start":882,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Electron density was observed for residues 11–470 and 573–881 in chain A of PLCβ3, and 10–196, 199–470, and 575–881 in the second.","type":"Methods"},{"text":"The CTD linker (residues 883–933) is not observed in the structure","type":"Methods"},{"text":"In the distal CTD, the Dα3-Dα4 (residues 1009–1025) and Dα4-Dα5 (residues 1108–1114) loops and C-terminal residues 1193–1234 lacked electron density, consistent with being disordered (Supplementary Fig. 3a).","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Full-length Gα(q)-phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil domain. <i> Lyon AM, Dutta S, Boguth CA, Skiniotis G, Tesmer JJ. </i> Nat Struct Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4GNK"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1192,"region_id":"DP02477r006","reference_id":"23377541","start":934,"term_id":"GO:0060090","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"To elucidate a structural basis for the functional roles of the distal CTD, we used X-ray crystallography and single particle electron cryo-microscopy (cryo EM) to determine the structure of human full-length PLCβ3 in complex with activated Gαq, revealing the distal CTD in the context of a fully functional signaling complex where it forms unanticipated interactions with Gαq and the catalytic core of PLCβ that likely contribute to regulation.","type":"Article"},{"text":"The distal CTD (residues 934–1192) consists of three primarily anti-parallel helical segments that extend nearly the full-length (~140 Å) of the domain (Fig. 1b, ​,2a).2a). The first segment contains the Dα1 (residues 935–946), Dα2 (954–958) and Dα3 (960–1008) helices. Dα3 forms an extended anti-parallel coiled-coil interaction with the Dα4 helix (residues 1027–1107) in the second segment. Dα4 in turn forms an extended anti-parallel coiled-coil interaction with Dα5 (residues 1115–1183) in the third segment. The Dα1 and Dα2 helices at the beginning of the first segment, and Dα6 (residues 1184–1192) at the end of the third segment, form “arms” that cross the same face of the domain and pack against the principal helices of the other two segments","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"x-ray crystallography evidence used in manual assertion","version":4,"reference_html":"Full-length Gα(q)-phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil domain. <i> Lyon AM, Dutta S, Boguth CA, Skiniotis G, Tesmer JJ. </i> Nat Struct Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4GNK"}],"term_name":"molecular adaptor activity","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1192,"region_id":"DP02477r007","reference_id":"23377541","start":934,"term_id":"GO:0060090","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"To elucidate a structural basis for the functional roles of the distal CTD, we used X-ray crystallography and single particle electron cryo-microscopy (cryo EM) to determine the structure of human full-length PLCβ3 in complex with activated Gαq, revealing the distal CTD in the context of a fully functional signaling complex where it forms unanticipated interactions with Gαq and the catalytic core of PLCβ that likely contribute to regulation.","type":"Article"},{"text":"The distal CTD (residues 934–1192) consists of three primarily anti-parallel helical segments that extend nearly the full-length (~140 Å) of the domain (Fig. 1b, ​,2a).2a). The first segment contains the Dα1 (residues 935–946), Dα2 (954–958) and Dα3 (960–1008) helices. Dα3 forms an extended anti-parallel coiled-coil interaction with the Dα4 helix (residues 1027–1107) in the second segment. Dα4 in turn forms an extended anti-parallel coiled-coil interaction with Dα5 (residues 1115–1183) in the third segment. The Dα1 and Dα2 helices at the beginning of the first segment, and Dα6 (residues 1184–1192) at the end of the third segment, form “arms” that cross the same face of the domain and pack against the principal helices of the other two segments","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy evidence used in manual assertion","version":4,"reference_html":"Full-length Gα(q)-phospholipase C-β3 structure reveals interfaces of the C-terminal coiled-coil domain. <i> Lyon AM, Dutta S, Boguth CA, Skiniotis G, Tesmer JJ. </i> Nat Struct Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","term_name":"molecular adaptor activity","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_06","length":1234,"ncbi_taxon_id":9606,"date":"2019-12-19T13:54:29.625Z","organism":"Homo sapiens","features":{"gene3D":[{"start":314,"end":717,"id":"G3DSA:3.20.20.190","name":"Phosphatidylinositol (PI) phosphodiesterase"},{"start":718,"end":886,"id":"G3DSA:2.60.40.150","name":"C2 domain"},{"start":934,"end":1192,"id":"G3DSA:1.20.1230.10","name":"G3DSA:1.20.1230.10"}],"pfam":[{"id":"PF00168","name":"C2 domain","start":727,"end":819},{"id":"PF00387","name":"Phosphatidylinositol-specific phospholipase C, Y domain","start":590,"end":704},{"id":"PF00388","name":"Phosphatidylinositol-specific phospholipase C, X domain","start":319,"end":469},{"id":"PF08703","name":"PLC-beta C terminal","start":944,"end":1200},{"id":"PF17787","name":"PH domain","start":18,"end":146},{"id":"PF22631","name":"Phosphoinositide phospholipase C beta1-4-like EF-hand domain","start":153,"end":221}]},"disprot_id":"DP02477","regions_counter":7,"dataset":[],"UniParc":"UPI000016AECE","uniref100":"UniRef100_Q01970","uniref90":"UniRef90_Q01970","uniref50":"UniRef50_Q01970","genes":[{"name":{"value":"PLCB3","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAA77683.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAA77683.1"}}]}}],"alphafold_very_low_content":0.17585089141004862,"disorder_content":0.3687196110210697,"disprot_consensus":{"full":[{"start":471,"end":572,"type":"D"},{"start":882,"end":1234,"type":"D"}],"Structural state":[{"start":471,"end":572,"type":"D"},{"start":882,"end":1234,"type":"D"}],"Disorder function":[{"start":471,"end":572,"type":"F"},{"start":883,"end":933,"type":"F"}],"Molecular function":[{"start":883,"end":1192,"type":"F"}]}},{"acc":"Q6SJQ7","name":"CMRF35-like molecule 1","sequence":"MHLSLLVPFLFWITGCCTAEDPVTGPEEVSGQEQGSLTVQCRYTSGWKDYKKYWCQGVPQRSCKTLVETDASEQLVKKNRVSIRDNQRDFIFTVTMEDLRMSDAGIYWCGITKGGLDPMFKVTVNIGPAIQVPITVPTMPPITSTTTIFTVTTTVKETSMFPTLTSYYSDNGHGGGDSGGGEDGVGDGFLDLSVLLPVISAVLLLLLLVASLFAWRMVRRQKKAAGPPSEQAQSLEGDLCYADLSLKQPRTSPGSSWKKGSSMSSSGKDHQEEVEYVTMAPFPREEVSYAALTLAGLGQEPTYGNTGCPITHVPRTGLEEETTEYSSIRRPLPAAMP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":330,"region_id":"DP02478r001","reference_id":"29563286","start":132,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In this study, we determined the X-ray crystal structure of the soluble CD300lf (sCD300lf) and the murine norovirus capsid protruding domain complex at a 2.05-Å resolution. ","type":"Abstract"},{"text":"Region adjacent to the crystallized domain sCD300lf characterized by missing electron density.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Atomic Structure of the Murine Norovirus Protruding Domain and Soluble CD300lf Receptor Complex. <i> Kilic T, Koromyslova A, Malak V, Hansman GS. </i> J Virol, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5OR7"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":337,"ncbi_taxon_id":10090,"date":"2019-12-19T15:49:53.656Z","organism":"Mus musculus","features":{"gene3D":[{"start":19,"end":130,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"}],"pfam":[{"id":"PF07686","name":"Immunoglobulin V-set domain","start":25,"end":115},{"id":"PF15330","name":"SHP2-interacting transmembrane adaptor protein, SIT","start":194,"end":299}]},"disprot_id":"DP02478","regions_counter":1,"dataset":[],"UniParc":"UPI0000230BD2","uniref100":"UniRef100_Q6SJQ7","uniref90":"UniRef90_Q6SJQ7","uniref50":"UniRef50_Q6SJQ7","genes":[{"name":{"value":"Cd300lf"},"synonyms":[{"value":"Clm1"},{"value":"Lmir3"}]}],"alphafold_very_low_content":0.35311572700296734,"disorder_content":0.5905044510385756,"disprot_consensus":{"full":[{"start":132,"end":330,"type":"D"}],"Structural state":[{"start":132,"end":330,"type":"D"}]}},{"acc":"O60502","name":"Protein O-GlcNAcase","sequence":"MVQKESQATLEERESELSSNPAASAGASLEPPAAPAPGEDNPAGAGGAAVAGAAGGARRFLCGVVEGFYGRPWVMEQRKELFRRLQKWELNTYLYAPKDDYKHRMFWREMYSVEEAEQLMTLISAAREYEIEFIYAISPGLDITFSNPKEVSTLKRKLDQVSQFGCRSFALLFDDIDHNMCAADKEVFSSFAHAQVSITNEIYQYLGEPETFLFCPTEYCGTFCYPNVSQSPYLRTVGEKLLPGIEVLWTGPKVVSKEIPVESIEEVSKIIKRAPVIWDNIHANDYDQKRLFLGPYKGRSTELIPRLKGVLTNPNCEFEANYVAIHTLATWYKSNMNGVRKDVVMTDSEDSTVSIQIKLENEGSDEDIETDVLYSPQMALKLALTEWLQEFGVPHQYSSRQVAHSGAKASVVDGTPLVAAPSLNATTVVTTVYQEPIMSQGAALSGEPTTLTKEEEKKQPDEEPMDMVVEKQEETDHKNDNQILSEIVEAKMAEELKPMDTDKESIAESKSPEMSMQEDCISDIAPMQTDEQTNKEQFVPGPNEKPLYTAEPVTLEDLQLLADLFYLPYEHGPKGAQMLREFQWLRANSSVVSVNCKGKDSEKIEEWRSRAAKFEEMCGLVMGMFTRLSNCANRTILYDMYSYVWDIKSIMSMVKSFVQWLGCRSHSSAQFLIGDQEPWAFRGGLAGEFQRLLPIDGANDLFFQPPPLTPTSKVYTIRPYFPKDEASVYKICREMYDDGVGLPFQSQPDLIGDKLVGGLLSLSLDYCFVLEDEDGICGYALGTVDVTPFIKKCKISWIPFMQEKYTKPNGDKELSEAEKIMLSFHEEQEVLPETFLANFPSLIKMDIHKKVTDPSVAKSMMACLLSSLKANGSRGAFCEVRPDDKRILEFYSKLGCFEIAKMEGFPKDVVILGRSL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":58,"region_id":"DP02479r001","reference_id":"28346405","start":11,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"OGA-L consists of an N-terminal catalytic domain (GH84), a helical domain, extensive regions predicted as disordered, and a C-terminal domain of unknown function having similarity to histone acetyl transferase (HAT) domains","type":"Article"},{"text":"residues 11-58, 341-370, 535-536, 596-598, 674-675 and 696-706 are disordered","type":"Article"},{"text":"Authors termed “Split1” their construct of OGA comprising amino acids 11-396 (N-terminal fragment) and 535-715 (C-terminal fragment) that yielded crystals suitable for structure determination.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structural and functional insight into human O-GlcNAcase. <i> Roth C, Chan S, Offen WA, Hemsworth GR, Willems LI, King DT, Varghese V, Britton R, Vocadlo DJ, Davies GJ. </i> Nat Chem Biol, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5M7U"},{"db":"PDB","id":"5M7T"},{"db":"PDB","id":"5M7S"},{"db":"PDB","id":"5M7R"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":370,"region_id":"DP02479r002","reference_id":"28346405","start":341,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"OGA-L consists of an N-terminal catalytic domain (GH84), a helical domain, extensive regions predicted as disordered, and a C-terminal domain of unknown function having similarity to histone acetyl transferase (HAT) domains","type":"Article"},{"text":"residues 11-58, 341-370, 535-536, 596-598, 674-675 and 696-706 are disordered","type":"Article"},{"text":"Authors termed “Split1” their construct of OGA comprising amino acids 11-396 (N-terminal fragment) and 535-715 (C-terminal fragment) that yielded crystals suitable for structure determination.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structural and functional insight into human O-GlcNAcase. <i> Roth C, Chan S, Offen WA, Hemsworth GR, Willems LI, King DT, Varghese V, Britton R, Vocadlo DJ, Davies GJ. </i> Nat Chem Biol, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5M7U"},{"db":"PDB","id":"5M7T"},{"db":"PDB","id":"5M7S"},{"db":"PDB","id":"5M7R"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":706,"region_id":"DP02479r003","reference_id":"28346405","start":696,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"OGA-L consists of an N-terminal catalytic domain (GH84), a helical domain, extensive regions predicted as disordered, and a C-terminal domain of unknown function having similarity to histone acetyl transferase (HAT) domains","type":"Article"},{"text":"residues 11-58, 341-370, 535-536, 596-598, 674-675 and 696-706 are disordered","type":"Article"},{"text":"Authors termed “Split1” their construct of OGA comprising amino acids 11-396 (N-terminal fragment) and 535-715 (C-terminal fragment) that yielded crystals suitable for structure determination.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structural and functional insight into human O-GlcNAcase. <i> Roth C, Chan S, Offen WA, Hemsworth GR, Willems LI, King DT, Varghese V, Britton R, Vocadlo DJ, Davies GJ. </i> Nat Chem Biol, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5M7U"},{"db":"PDB","id":"5M7T"},{"db":"PDB","id":"5M7S"},{"db":"PDB","id":"5M7R"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":56,"region_id":"DP02479r004","reference_id":"30644846","start":11,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The residues that were still disordered in monomers A and B were Gly11–Gly56, Ser348–Glu369, Lys535 and Pro707–Tyr715 for monomer B only.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structural studies of a surface-entropy reduction mutant of O-GlcNAcase. <i> Males A, Davies GJ. </i> Acta Crystallogr D Struct Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6HKI"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":369,"region_id":"DP02479r005","reference_id":"30644846","start":348,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The residues that were still disordered in monomers A and B were Gly11–Gly56, Ser348–Glu369, Lys535 and Pro707–Tyr715 for monomer B only.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structural studies of a surface-entropy reduction mutant of O-GlcNAcase. <i> Males A, Davies GJ. </i> Acta Crystallogr D Struct Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6HKI"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":371,"region_id":"DP02479r006","reference_id":"28346407","start":341,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The (β/α)8 barrel includes amino acids 58–340, whereas 341–371 are disordered.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Insights into activity and inhibition from the crystal structure of human O-GlcNAcase. <i> Elsen NL, Patel SB, Ford RE, Hall DL, Hess F, Kandula H, Kornienko M, Reid J, Selnick H, Shipman JM, Sharma S, Lumb KJ, Soisson SM, Klein DJ. </i> Nat Chem Biol, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":372,"region_id":"DP02479r007","reference_id":"28319083","start":335,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode. <i> Li B, Li H, Lu L, Jiang J. </i> Nat Struct Mol Biol, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5TKE"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":916,"ncbi_taxon_id":9606,"date":"2019-12-19T17:32:46.339Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF07555","name":"beta-N-acetylglucosaminidase","start":62,"end":342}]},"disprot_id":"DP02479","regions_counter":7,"dataset":[],"UniParc":"UPI0000073533","uniref100":"UniRef100_O60502","uniref90":"UniRef90_Q8VIJ5","uniref50":"UniRef50_Q8VIJ5","genes":[{"name":{"value":"OGA","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:7056","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:7056"}}]},"synonyms":[{"value":"HEXC"},{"value":"KIAA0679"},{"value":"MEA5"},{"value":"MGEA5"}]}],"alphafold_very_low_content":0.25327510917030566,"disorder_content":0.10589519650655022,"disprot_consensus":{"full":[{"start":11,"end":58,"type":"D"},{"start":335,"end":372,"type":"D"},{"start":696,"end":706,"type":"D"}],"Structural state":[{"start":11,"end":58,"type":"D"},{"start":335,"end":372,"type":"D"},{"start":696,"end":706,"type":"D"}]}},{"acc":"Q12102","name":"Cleavage factor two protein 2","sequence":"MTYKYNCCDDGSGTTVGSVVRFDNVTLLIDPGWNPSKVSYEQCIKYWEKVIPEIDVIILSQPTIECLGAHSLLYYNFTSHFISRIQVYATLPVINLGRVSTIDSYASAGVIGPYDTNKLDLEDIEISFDHIVPLKYSQLVDLRSRYDGLTLLAYNAGVCPGGSIWCISTYSEKLVYAKRWNHTRDNILNAASILDATGKPLSTLMRPSAIITTLDRFGSSQPFKKRSKIFKDTLKKGLSSDGSVIIPVDMSGKFLDLFTQVHELLFESTKINAHTQVPVLILSYARGRTLTYAKSMLEWLSPSLLKTWENRNNTSPFEIGSRIKIIAPNELSKYPGSKICFVSEVGALINEVIIKVGNSEKTTLILTKPSFECASSLDKILEIVEQDERNWKTFPEDGKSFLCDNYISIDTIKEEPLSKEETEAFKVQLKEKKRDRNKKILLVKRESKKLANGNAIIDDTNGERAMRNQDILVENVNGVPPIDHIMGGDEDDDEEEENDNLLNLLKDNSEKSAAKKNTEVPVDIIIQPSAASKHKMFPFNPAKIKKDDYGTVVDFTMFLPDDSDNVNQNSRKRPLKDGAKTTSPVNEEDNKNEEEDGYNMSDPISKRSKHRASRYSGFSGTGEAENFDNLDYLKIDKTLSKRTISTVNVQLKCSVVILNLQSLVDQRSASIIWPSLKSRKIVLSAPKQIQNEEITAKLIKKNIEVVNMPLNKIVEFSTTIKTLDISIDSNLDNLLKWQRISDSYTVATVVGRLVKESLPQVNNHQKTASRSKLVLKPLHGSSRSHKTGALSIGDVRLAQLKKLLTEKNYIAEFKGEGTLVINEKVAVRKINDAETIIDGTPSELFDTVKKLVTDMLAKI","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":625,"region_id":"DP02480r001","reference_id":"17128255","start":423,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Here we report the crystal structures of human CPSF-73 at 2.1 Å resolution, complexed with zinc ions and a sulfate that may mimic the phosphate group of the substrate, and the related yeast protein CPSF-100 (Ydh1p) at 2.5 Å resolution. Both CPSF-73 and CPSF-100 contain two domains, a metallo-β-lactamase domain and a novel β-CASP domain. ","type":"Abstract"},{"text":"There are, however, significant differences in the structures of CPSF-100 and CPSF-73 (Supplemental Fig. 4). Most importantly, motifs for zinc binding in the metallo-β-lactamase domain are missing in CPSF-100 (Supplemental Fig. 2b), and therefore this protein cannot bind zinc and is unlikely to possess nuclease activity. In addition, the β-CASP domain of CPSF-100 (Fig. 2b) is much larger than that of CPSF-73, but contains a highly flexible segment (Supplemental Results and Supplemental Fig. 5).","type":"Article"},{"text":"Several segments of CPSF-73 are disordered in these crystals (1-6, 113-121, 289-299 in the\npresence, and 1-8, 113-121, 184-188, 272-304 in the absence of zinc), as is the case in the\nstructure of yeast CPSF-100 (269-275, 389-396, 423-625).","type":"Supplementary material"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing endonuclease. <i> Mandel CR, Kaneko S, Zhang H, Gebauer D, Vethantham V, Manley JL, Tong L. </i> Nature, 2006","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2I7X"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":859,"ncbi_taxon_id":559292,"date":"2019-12-19T18:15:36.199Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","features":{"gene3D":[{"start":527,"end":717,"id":"G3DSA:3.60.15.10","name":"Ribonuclease Z/Hydroxyacylglutathione hydrolase-like"},{"start":527,"end":717,"id":"G3DSA:3.60.15.10","name":"Ribonuclease Z/Hydroxyacylglutathione hydrolase-like"}],"pfam":[{"id":"PF13299","name":"Cleavage and polyadenylation factor 2 C-terminal","start":728,"end":856},{"id":"PF16661","name":"Metallo-beta-lactamase superfamily domain","start":20,"end":211}]},"disprot_id":"DP02480","regions_counter":1,"dataset":[],"UniParc":"UPI0000052DD6","uniref100":"UniRef100_Q12102","uniref90":"UniRef90_Q12102","uniref50":"UniRef50_Q12102","genes":[{"name":{"value":"CFT2"},"synonyms":[{"value":"YDH1"}],"orfNames":[{"value":"L2946"}],"olnNames":[{"value":"YLR115W"}]}],"alphafold_very_low_content":0.15250291036088476,"disorder_content":0.23632130384167638,"disprot_consensus":{"full":[{"start":423,"end":625,"type":"D"}],"Structural state":[{"start":423,"end":625,"type":"D"}]}},{"acc":"P46674","name":"Nuclear mRNA export protein SAC3","sequence":"MNTSFGSVVPSTNFNFFKGHGNNDNTSANSTVNNSNFFLNSNETKPSKNVFMVHSTSQKKSQQPLQNLSHSPSYTENKPDKKKKYMINDAKTIQLVGPLISSPDNLGFQKRSHKARELPRFLINQEPQLEKRAFVQDPWDKANQEKMISLEESIDDLNELYETLKKMRNTERSIMEEKGLVDKADSAKDLYDAIVFQGTCLDMCPTFERSRRNVEYTVYSYEKNQPNDKKASRTKALKVFARPAAAAAPPLPSDVRPPHILVKTLDYIVDNLLTTLPESEGFLWDRMRSIRQDFTYQNYSGPEAVDCNERIVRIHLLILHIMVKSNVEFSLQQELEQLHKSLITLSEIYDDVRSSGGTCPNEAEFRAYALLSKIRDPQYDENIQRLPKHIFQDKLVQMALCFRRVISNSAYTERGFVKTENCLNFYARFFQLMQSPSLPLLMGFFLQMHLTDIRFYALRALSHTLNKKHKPIPFIYLENMLLFNNRQEIIEFCNYYSIEIINGDAADLKTLQHYSHKLSETQPLKKTYLTCLERRLQKTTYKGLINGGEDNLASSVYVKDPKKDRIPSIADQSFLMENFQNNYNEKLNQNSSVKPQINTSPKRVATRPNHFPFSQESKQLPQISQSHTLSTNPLLTPQVHGDLSEQKQQQIKTVTDGGSPFVFDQSAQNSTVEASKAHMISTTSNGAYDEKLSSEQEEMRKKEEQRIEEEKTQLKKKQENADKQVITEQIANDLVKEVVNSSVISIVKREFSEANYRKDFIDTMTRELYDAFLHERLYLIYMDSRAELKRNSTLKKKFFEKWQASYSQAKKNRILEEKKREEIKLVSHQLGVPGFKKSTCLFRTPYKGNVNSSFMLSSSDKNLIFSPVNDEFNKFATHLTKISKLWRPLEMQSIYYDNLTKKFPSNSLTPANLFIYAKDWTSLSNRWILSKFNLQTAQDSKKFSNNIISSRIICIDDEYEPSDFSDLQLLIFNTGVTNPDIFDLEMKLKDDGEELIKLITGISLNTNICFSLLIIYWESAENTLSESTIKHLLKLNRISKNYSSVIERIDLMNLTEESPHKCLEDKLSEISHSYVYKLTERGKYDKTLRQKRSLAGIHSRSTQLQTTKDIDQKMKKMLEKEKNKYQQQIGERNTYAHLESHIDASPRSKKRKLPILLSTSHSSQFKTPLASRLNTSGSSTSPPLPSHLAMKFRKNSRVTSLHTVLPVSTPSHSNNIPAASFSGNNTTDIQSQQLIENQKSTSVYLNNVSERILGNQEICQTPINPVTPVLDGADQGKEDIPDSILELKILIDSVKKKVNND","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":142,"region_id":"DP02481r001","reference_id":"27422657","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"residues 1–142 showed little potential for forming secondary structure.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"The Sac3 TPR-like region in the Saccharomyces cerevisiae TREX-2 complex is more extensive but independent of the CID region. <i> Aibara S, Bai XC, Stewart M. </i> J Struct Biol, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5L3T"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1301,"region_id":"DP02481r002","reference_id":"27422657","start":551,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"We could not find additional density consistent with residues beyond 551 (connecting the Sac3 M-subcomplex and the Sac3 CID-subcomplex) and so it is likely that this linker is flexible, consistent with the random orientation observed for the CID region relative to the M-region in negatively stained electron micrographs.","type":"Results"},{"text":"No other difference density was observed that could correspond to the CID domain of the complex (containing Sac3 residues 727–805, together with two Sus1 chains and a Cdc31 chain), consistent with the crystals containing only the N-terminal half of Sac3 (up to about residue 555) together with Thp1 and Sem1.","type":"Results"},{"text":"and the CID-subcomplex, consisting of Sac3 residues ∼720–805 bound to Cdc31 and two Sus1 chains and which, in Saccharomyces cerevisiae, binds to the nuclear pore complex (NPC) to tether the complex close to the nuclear basket to facilitate localization of genes such as GAL1","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"The Sac3 TPR-like region in the Saccharomyces cerevisiae TREX-2 complex is more extensive but independent of the CID region. <i> Aibara S, Bai XC, Stewart M. </i> J Struct Biol, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5L3T"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":805,"region_id":"DP02481r003","reference_id":"27422657","start":720,"term_id":"GO:0005515","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"and the CID-subcomplex, consisting of Sac3 residues ∼720–805 bound to Cdc31 and two Sus1 chains and which, in Saccharomyces cerevisiae, binds to the nuclear pore complex (NPC) to tether the complex close to the nuclear basket to facilitate localization of genes such as GAL1","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"The Sac3 TPR-like region in the Saccharomyces cerevisiae TREX-2 complex is more extensive but independent of the CID region. <i> Aibara S, Bai XC, Stewart M. </i> J Struct Biol, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5L3T"},{"db":"PDB","id":"5G5P"}],"term_name":"protein binding","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":805,"region_id":"DP02481r004","reference_id":"27422657","start":720,"term_id":"GO:0060090","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"and the CID-subcomplex, consisting of Sac3 residues ∼720–805 bound to Cdc31 and two Sus1 chains and which, in Saccharomyces cerevisiae, binds to the nuclear pore complex (NPC) to tether the complex close to the nuclear basket to facilitate localization of genes such as GAL1","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"The Sac3 TPR-like region in the Saccharomyces cerevisiae TREX-2 complex is more extensive but independent of the CID region. <i> Aibara S, Bai XC, Stewart M. </i> J Struct Biol, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5L3T"},{"db":"PDB","id":"5G5P"}],"term_name":"molecular adaptor activity","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":719,"region_id":"DP02481r005","reference_id":"27422657","start":551,"term_id":"IDPO:0000033","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"We could not find additional density consistent with residues beyond 551 (connecting the Sac3 M-subcomplex and the Sac3 CID-subcomplex) and so it is likely that this linker is flexible, consistent with the random orientation observed for the CID region relative to the M-region in negatively stained electron micrographs.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"The Sac3 TPR-like region in the Saccharomyces cerevisiae TREX-2 complex is more extensive but independent of the CID region. <i> Aibara S, Bai XC, Stewart M. </i> J Struct Biol, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5L3T"},{"db":"PDB","id":"5G5P"}],"term_name":"flexible linker","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":805,"region_id":"DP02481r006","reference_id":"27422657","start":720,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"There was however, no clear additional density that could be identified with the linkers between these helices or with the CID region of the complex, consistent with the CID region not having a defined orientation relative to the M-region as observed in the negatively-stained material. It is likely that within the cryo-EM micrographs recorded that the CID-subcomplex is also present in random orientations, however since the CID-subcomplex is effectively little more than a single α-helix with small proteins attached, the signal-to-noise is too poor for the particles to be detected with confidence","type":"Results"},{"text":"The structure of the TREX-2 M-region determined by cryo-EM has been deposited in the Electron Microscopy Data Bank (accession No. EMD-3440)","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"The Sac3 TPR-like region in the Saccharomyces cerevisiae TREX-2 complex is more extensive but independent of the CID region. <i> Aibara S, Bai XC, Stewart M. </i> J Struct Biol, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","term_name":"disorder","cross_refs":[{"db":"PDB","id":"5G5P"}],"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":805,"region_id":"DP02481r012","reference_id":"27422657","start":720,"term_id":"GO:0060090","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"CID-subcomplex, consisting of Sac3 residues ∼720–805 bound to Cdc31 and two Sus1 chains and which, in Saccharomyces cerevisiae, binds to the nuclear pore complex (NPC) to tether the complex close to the nuclear basket to facilitate localization of genes such as GAL1","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"The Sac3 TPR-like region in the Saccharomyces cerevisiae TREX-2 complex is more extensive but independent of the CID region. <i> Aibara S, Bai XC, Stewart M. </i> J Struct Biol, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5G5P"},{"db":"PDB","id":"5L3T"}],"term_name":"molecular adaptor activity","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_06","length":1301,"ncbi_taxon_id":559292,"date":"2019-12-20T13:03:38.222Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","features":{"gene3D":[],"pfam":[{"id":"PF03399","name":"SAC3/GANP family","start":203,"end":500},{"id":"PF12209","name":"Leucine permease transcriptional regulator helical domain","start":728,"end":799}]},"disprot_id":"DP02481","regions_counter":12,"dataset":[],"UniParc":"UPI0000168A3F","uniref100":"UniRef100_P46674","uniref90":"UniRef90_P46674","uniref50":"UniRef50_P46674","genes":[{"name":{"value":"SAC3"},"synonyms":[{"value":"LEP1"}],"orfNames":[{"value":"YD8358.13"}],"olnNames":[{"value":"YDR159W"}]}],"alphafold_very_low_content":0.3051498847040738,"disorder_content":0.6863950807071484,"disprot_consensus":{"full":[{"start":1,"end":142,"type":"D"},{"start":551,"end":1301,"type":"D"}],"Structural state":[{"start":1,"end":142,"type":"D"},{"start":551,"end":1301,"type":"D"}],"Molecular function":[{"start":720,"end":805,"type":"F"}],"Disorder function":[{"start":551,"end":719,"type":"F"}]}},{"acc":"Q8ZRP0","name":"Outer membrane protein assembly factor BamA","sequence":"MAMKKLLIASLLFSSATVYGAEGFVVKDIHFEGLQRVAVGAALLSMPVRTGDTVNDEDISNTIRALFATGNFEDVRVLRDGNTLLVQVKERPTIASITFSGNKSVKDDMLKQNLEASGVRVGESLDRTTLSDIEKGLEDFYYSVGKYSASVKAVVTPLPRNRVDLKLVFQEGVSAKIQQINIVGNHAFSTEELISHFQLRDEVPWWNVVGDRKYQKQKLAGDLETLRSYYLDRGYARFNIDSTQVSLTPDKKGIYITVNITEGDQYKLSGVQVSGNLAGHSAEIENLTKIEPGELYNGTKVTKMEDDIKKLLGRYGYAYPRVQSQPEINDADKTVKLRVNVDAGNRFYVRKIRFEGNDTSKDSVLRREMRQMEGAWLGSDLVDQGKERLNRLGFFETVDTDTQRVPGSPDQVDVVYKVKERNTGSFNFGIGYGTESGVSFQAGVQQDNWLGTGYSVGINGTKNDYQTYSELSVTNPYFTVDGVSLGGRIFYNDFQADDADLSDYTNKSYGTDVTLGFPINEYNTLRAGLGYVHNKLSNMQPQIAMDRYLESMGQSADTSSFAADDFTFNYGWTYNKLDRGYFPTDGSRVNLTGKVTIPGSDNEYYKVSLDTATYVPIDNDHKWVVLGRTRWGYGDGLGGKEMPFYENFYAGGSSTVRGFQSNTIGPKAVYKNGAHTSWDDNDDYEDCTQESGCKSDDAVGGNAMAVASLEFITPTPFISEKYANSVRTSFFWDMGTVWDTNWDPSSAPSDVPDYSDPGNIRMSAGIALQWMSPLGPLVFSYAQPFKKYDGDKAEQFQFNIGKTW","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":426,"region_id":"DP02483r001","reference_id":"28974626","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The  crystal  structure  was  determined  by molecular replacement to a resolution of 2.92 Å. Only the BamA barrel domain was found in the structure, indicating that the BamAB complex may be  too flexible to be crystallized,  while  the  BamA  POTRA  domains  and  BamB may  be  cleaved  by contaminant   proteases   during   the   protein   crystallization.","type":"Results"},{"text":"There is one BamA molecule per asymmetric unit. The BamA barrel is formed by 16 β-strands with residues Asn427-Gly801.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"BamA β16C strand and periplasmic turns are critical for outer membrane protein insertion and assembly. <i> Gu Y, Zeng Y, Wang Z, Dong C. </i> Biochem J, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5OR1"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":804,"ncbi_taxon_id":99287,"date":"2019-12-20T16:37:41.024Z","organism":"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","features":{"gene3D":[],"pfam":[{"id":"PF01103","name":"Omp85 superfamily domain","start":448,"end":804},{"id":"PF07244","name":"Surface antigen variable number repeat","start":92,"end":172},{"id":"PF07244","name":"Surface antigen variable number repeat","start":176,"end":263},{"id":"PF07244","name":"Surface antigen variable number repeat","start":266,"end":344},{"id":"PF07244","name":"Surface antigen variable number repeat","start":348,"end":421}]},"disprot_id":"DP02483","regions_counter":1,"dataset":[],"UniParc":"UPI00000CCE5E","uniref100":"UniRef100_Q8ZRP0","uniref90":"UniRef90_Q8ZRP0","uniref50":"UniRef50_D5CHY0","genes":[{"name":{"value":"bamA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01430","url":"https://hamap.expasy.org/unirule/MF_01430"}}]},"synonyms":[{"value":"yaeT"}],"olnNames":[{"value":"STM0224"}]}],"alphafold_very_low_content":0.03109452736318408,"disorder_content":0.5298507462686567,"disprot_consensus":{"full":[{"start":1,"end":426,"type":"D"}],"Structural state":[{"start":1,"end":426,"type":"D"}]}},{"acc":"P0AD27","name":"Inner membrane protein YejM","sequence":"MVTHRQRYREKVSQMVSWGHWFALFNILLSLVIGSRYLFIADWPTTLAGRIYSYVSIIGHFSFLVFATYLLILFPLTFIVGSQRLMRFLSVILATAGMTLLLIDSEVFTRFHLHLNPIVWQLVINPDENEMARDWQLMFISVPVILLLELVFATWSWQKLRSLTRRRRFARPLAAFLFIAFIASHVVYIWADANFYRPITMQRANLPLSYPMTARRFLEKHGLLDAQEYQRRLIEQGNPDAVSVQYPLSELRYRDMGTGQNVLLITVDGLNYSRFEKQMPALAGFAEQNISFTRHMSSGNTTDNGIFGLFYGISPSYMDGILSTRTPAALITALNQQGYQLGLFSSDGFTSPLYRQALLSDFSMPSVRTQSDEQTATQWINWLGRYAQEDNRWFSWVSFNGTNIDDSNQQAFARKYSRAAGNVDDQINRVLNALRDSGKLDNTVVIITAGRGIPLSEEEETFDWSHGHLQVPLVIHWPGTPAQRINALTDHTDLMTTLMQRLLHVSTPASEYSQGQDLFNPQRRHYWVTAADNDTLAITTPKKTLVLNNNGKYRTYNLRGERVKDEKPQLSLLLQVLTDEKRFIAN","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":244,"region_id":"DP02484r001","reference_id":"27487745","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Region 1-244 is not visible in the crystal structure of E. coli YejM","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structural insights into cardiolipin transfer from the Inner membrane to the outer membrane by PbgA in Gram-negative bacteria. <i> Dong H, Zhang Z, Tang X, Huang S, Li H, Peng B, Dong C. </i> Sci Rep, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5I5H"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":586,"ncbi_taxon_id":83333,"date":"2019-12-23T12:23:46.088Z","organism":"Escherichia coli (strain K12)","features":{"gene3D":[{"start":254,"end":570,"id":"G3DSA:3.40.720.10","name":"Alkaline Phosphatase, subunit A"}],"pfam":[{"id":"PF00884","name":"Sulfatase","start":260,"end":501},{"id":"PF11893","name":"Domain of unknown function (DUF3413)","start":6,"end":252}]},"disprot_id":"DP02484","regions_counter":1,"dataset":[],"UniParc":"UPI000013AC7E","uniref100":"UniRef100_P0AD29","uniref90":"UniRef90_P0AD29","uniref50":"UniRef50_P40709","genes":[{"name":{"value":"yejM"},"synonyms":[{"value":"yejN"}],"olnNames":[{"value":"b2188"},{"value":"JW2176"}]}],"alphafold_very_low_content":0.0034129692832764505,"disorder_content":0.41638225255972694,"disprot_consensus":{"full":[{"start":1,"end":244,"type":"D"}],"Structural state":[{"start":1,"end":244,"type":"D"}]}},{"acc":"P40709","name":"Inner membrane protein YejM","sequence":"MVTHRQRYREKVSQMVSWGHWFALFNILLATLLGSRYLFVADWPTTLAGRIYSYLSIVGHFSFLVFATYLLILFPLTFIVMSQRLMRFLSAILATAGMTLLLIDSEVFTRFHLHLNPIVWELVINPDQNEMARDWQLMFISVPVILLIEMLFATWSWQKLRSLTRRRHFARPLAAFFFVSFIASHLIYIWADANFYRPITMQRANLPLSYPMTARRFLEKHGLLDAQEYQRRLVEQGNPEAVSVQYPLSNLHYRDMGTGQNVLLITVDGLNYSRFEKQMPELATFAEQNIDFTRHMSSGNTTDNGIFGLFYGISPGYMDGVLSTRTPAALITALNQQGYQLGLFSSDGFASPLYRQALLSDFSMPAAQTQSDAQTASQWIDWLGRYAQEDNRWFSWISFNGTNIDDSNQKNFVKRYASAASDVDAQINRVLNALREAGKFDNTVVIITAGRGIPLTPEENRFDWSQGHLQVPLVIHWPGTPAQRINVLTDHTDVMTTLMQRLLHVSTPANEYSQGQDIFTVPRRHNWVTAADGSTLAITTPQMTLVLNNNGHYQTYDLHGEKIKDQKPQLSLLLQVLTEEKRFIAN","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":244,"region_id":"DP02485r001","reference_id":"27487745","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"All the proteins were purified, and the PbgA245-586 from S. typhimurium Str. LT2 (StPbgA245-586) and E. coli (EcPbgA245-586) were crystallized","type":"Results"},{"text":"The crystals of StPbgA191-586 belong to the space group P21 with cell dimensions a = 41.49 Å, b = 196.39 Å, c = 45.66 Å, α = γ = 90° and β = 107.53°. The StPbgA191-586 structure was determined by molecular replacement to 2.19 Å resolution; residues 191–245 has no visible electron density so were either disordered or cleaved.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structural insights into cardiolipin transfer from the Inner membrane to the outer membrane by PbgA in Gram-negative bacteria. <i> Dong H, Zhang Z, Tang X, Huang S, Li H, Peng B, Dong C. </i> Sci Rep, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5I5D"},{"db":"PDB","id":"5I5F"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":586,"ncbi_taxon_id":99287,"date":"2019-12-23T12:46:26.364Z","organism":"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","features":{"gene3D":[{"start":254,"end":581,"id":"G3DSA:3.40.720.10","name":"Alkaline Phosphatase, subunit A"}],"pfam":[{"id":"PF00884","name":"Sulfatase","start":260,"end":501},{"id":"PF11893","name":"Domain of unknown function (DUF3413)","start":6,"end":252}]},"disprot_id":"DP02485","regions_counter":1,"dataset":[],"UniParc":"UPI0000059BB0","uniref100":"UniRef100_P40709","uniref90":"UniRef90_P40709","uniref50":"UniRef50_P40709","genes":[{"name":{"value":"yejM"},"olnNames":[{"value":"STM2228"}]}],"alphafold_very_low_content":0.0034129692832764505,"disorder_content":0.41638225255972694,"disprot_consensus":{"full":[{"start":1,"end":244,"type":"D"}],"Structural state":[{"start":1,"end":244,"type":"D"}]}},{"acc":"A7ZUK2","name":"DNA-directed RNA polymerase subunit beta'","sequence":"MKDLLKFLKAQTKTEEFDAIKIALASPDMIRSWSFGEVKKPETINYRTFKPERDGLFCARIFGPVKDYECLCGKYKRLKHRGVICEKCGVEVTQTKVRRERMGHIELASPTAHIWFLKSLPSRIGLLLDMPLRDIERVLYFESYVVIEGGMTNLERQQILTEEQYLDALEEFGDEFDAKMGAEAIQALLKSMDLEQECEQLREELNETNSETKRKKLTKRIKLLEAFVQSGNKPEWMILTVLPVLPPDLRPLVPLDGGRFATSDLNDLYRRVINRNNRLKRLLDLAAPDIIVRNEKRMLQEAVDALLDNGRRGRAITGSNKRPLKSLADMIKGKQGRFRQNLLGKRVDYSGRSVITVGPYLRLHQCGLPKKMALELFKPFIYGKLELRGLATTIKAAKKMVEREEAVVWDILDEVIREHPVLLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCAAYNADFDGDQMAVHVPLTLEAQLEARALMMSTNNILSPANGEPIIVPSQDVVLGLYYMTRDCVNAKGEGMVLTGPKEAERLYRSGLASLHARVKVRITEYEKDANGELVAKTSLKDTTVGRAILWMIVPKGLPYSIVNQALGKKAISKMLNTCYRILGLKPTVIFADQIMYTGFAYAARSGASVGIDDMVIPEKKHEIISEAEAEVAEIQEQFQSGLVTAGERYNKVIDIWAAANDRVSKAMMDNLQTETVINRDGQEEKQVSFNSIYMMADSGARGSAAQIRQLAGMRGLMAKPDGSIIETPITANFREGLNVLQYFISTHGARKGLADTALKTANSGYLTRRLVDVAQDLVVTEDDCGTHEGIMMTPVIEGGDVKEPLRDRVLGRVTAEDVLKPGTADILVPRNTLLHEQWCDLLEENSVDAVKVRSVVSCDTDFGVCAHCYGRDLARGHIINKGEAIGVIAAQSIGEPGTQLTMRTFHIGGAASRAAAESSIQVKNKGSIKLSNVKSVVNSSGKLVITSRNTELKLIDEFGRTKESYKVPYGAVLAKGDGEQVAGGETVANWDPHTMPVITEVSGFVRFTDMIDGQTITRQTDELTGLSSLVVLDSAERTAGGKDLRPALKIVDAQGNDVLIPGTDMPAQYFLPGKAIVQLEDGVQISSGDTLARIPQESGGTKDITGGLPRVADLFEARRPKEPAILAEISGIVSFGKETKGKRRLVITPVDGSDPYEEMIPKWRQLNVFEGERVERGDVISDGPEAPHDILRLRGVHAVTRYIVNEVQDVYRLQGVKINDKHIEVIVRQMLRKATIVNAGSSDFLEGEQVEYSRVKIANRELEANGKVGATYSRDLLGITKASLATESFISAASFQETTRVLTEAAVAGKRDELRGLKENVIVGRLIPAGTGYAYHQDRMRRRAAGEAPAAPQVTAEDASASLAELLNAGLGGSDNE","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1134,"region_id":"DP02486r001","reference_id":"25798859","start":931,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"X-ray crystal structures of Escherichia coli RNA polymerase with switch region binding inhibitors enable rational design of squaramides with an improved fraction unbound to human plasma protein. <i> Molodtsov V, Fleming PR, Eyermann CJ, Ferguson AD, Foulk MA, McKinney DC, Masse CE, Buurman ET, Murakami KS. </i> J Med Chem, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4YFK"},{"db":"PDB","id":"4YFN"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":1407,"ncbi_taxon_id":331111,"date":"2019-12-27T11:17:16.539Z","organism":"Escherichia coli O139:H28 (strain E24377A / ETEC)","features":{"gene3D":[{"start":641,"end":790,"id":"G3DSA:1.10.132.30","name":"G3DSA:1.10.132.30"},{"start":490,"end":640,"id":"G3DSA:1.10.274.100","name":"G3DSA:1.10.274.100"}],"pfam":[{"id":"PF00623","name":"RNA polymerase Rpb1, domain 2","start":392,"end":485},{"id":"PF04983","name":"RNA polymerase Rpb1, domain 3","start":489,"end":644},{"id":"PF04997","name":"RNA polymerase Rpb1, domain 1","start":15,"end":342},{"id":"PF04998","name":"RNA polymerase Rpb1, domain 5","start":766,"end":1315},{"id":"PF05000","name":"RNA polymerase Rpb1, domain 4","start":674,"end":764}]},"disprot_id":"DP02486","regions_counter":1,"dataset":[],"UniParc":"UPI000013471A","uniref100":"UniRef100_A7ZUK2","uniref90":"UniRef90_A7ZUK2","uniref50":"UniRef50_Q9PA87","genes":[{"name":{"value":"rpoC","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01322","url":"https://hamap.expasy.org/unirule/MF_01322"}}]},"olnNames":[{"value":"EcE24377A_4529"}]}],"alphafold_very_low_content":0.02771855010660981,"disorder_content":0.14498933901918976,"disprot_consensus":{"full":[{"start":931,"end":1134,"type":"D"}],"Structural state":[{"start":931,"end":1134,"type":"D"}]}},{"acc":"P22473","name":"Protein P7","sequence":"MSAIVGLCLLSEKVVLSRSLTDEVSKLYKLNRGNVKEPRKYATERMSTQSKPVALQVPVSTIILDYKNEDFIKQNPTYSAMDIIGSPSNTAPQTAFQSIMPSLSALFNTPFIQGAFRHRIISSMGPEISYLVMVIGPPSGFMDTPNVSSAQSSVHTVSNADVDLNDIIAINSTMAKSTKLVSASTLQAMLVNDVYDRCMDLDGILLSQALPFFRNYVNVQSKGSLPPAVAACLNTPIKELFSMGSGKREPLALEFRKDNEGQCIGIVLPKGHEGDTLSSRYPAVFINESEPFSDKERSELSELKRTDSDAYEKLYSETISKHVSDGSYGNRVIISHKMSRLSNGGVKIIGRFKISDFNTVKKNLSSRSGEIDSAKEQWEALSGNGLVTDSNISMLHDKILDTITSNKPGVVLRDGNKKSENIVVCFKNGFPNKKHSLLQLTKNGISVVSLDELTDAGILVESTGPDRVRRSPKVLANKLSSFKGRKVTLDVDNMSTEALIQKLSTL","taxonomy":["Viruses","Riboviria","Orthornavirae","Duplornaviricota","Resentoviricetes","Reovirales","Reoviridae","Sedoreovirinae","Phytoreovirus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":288,"region_id":"DP02487r001","reference_id":"14527391","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The atomic structure of RDV was determined at 3.5 A resolution by X-ray crystallography. ","type":"Abstract"},{"text":"The present model contains two P3 subunits (P3A, residues 50–1016; P3B, residues 1–1019), 13 P8 subunits (PA, residues 1–47 and 55–421; PB, residues 1–48 and 55–421; PC, residues 1–49 and 54–421; QA, residues 1–421; QB, residues 1–421; QC, residues 1–47 and 54–421; RA, residues 1–421; RB, residues 1–48 and 53–421; RC, residues 1–421; SA, residues 1–421; SB, residues 1–50 and 53–421; SC, residues 1–47 and 56–421; T, residues 1–421), and a fragment of P7 (residues 289–300).","type":"Methods"},{"text":"We present here the atomic structure of RDV, determined at 3.5 Å resolution by X-ray crystallography. The model consists of P3 inner capsid proteins, P8 outer capsid proteins, and fragments of P7, the nucleic acid binding protein. The atomic structure suggests a self-assembly mechanism for both homologous and heterologous capsid proteins.","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"The atomic structure of rice dwarf virus reveals the self-assembly mechanism of component proteins. <i> Nakagawa A, Miyazaki N, Taka J, Naitow H, Ogawa A, Fujimoto Z, Mizuno H, Higashi T, Watanabe Y, Omura T, Cheng RH, Tsukihara T. </i> Structure, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1UF2"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":506,"region_id":"DP02487r002","reference_id":"14527391","start":301,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The atomic structure of RDV was determined at 3.5 A resolution by X-ray crystallography.","type":"Abstract"},{"text":"The present model contains two P3 subunits (P3A, residues 50–1016; P3B, residues 1–1019), 13 P8 subunits (PA, residues 1–47 and 55–421; PB, residues 1–48 and 55–421; PC, residues 1–49 and 54–421; QA, residues 1–421; QB, residues 1–421; QC, residues 1–47 and 54–421; RA, residues 1–421; RB, residues 1–48 and 53–421; RC, residues 1–421; SA, residues 1–421; SB, residues 1–50 and 53–421; SC, residues 1–47 and 56–421; T, residues 1–421), and a fragment of P7 (residues 289–300).","type":"Methods"},{"text":"We present here the atomic structure of RDV, determined at 3.5 Å resolution by X-ray crystallography. The model consists of P3 inner capsid proteins, P8 outer capsid proteins, and fragments of P7, the nucleic acid binding protein. The atomic structure suggests a self-assembly mechanism for both homologous and heterologous capsid proteins.","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"The atomic structure of rice dwarf virus reveals the self-assembly mechanism of component proteins. <i> Nakagawa A, Miyazaki N, Taka J, Naitow H, Ogawa A, Fujimoto Z, Mizuno H, Higashi T, Watanabe Y, Omura T, Cheng RH, Tsukihara T. </i> Structure, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1UF2"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":300,"region_id":"DP02487r003","reference_id":"14527391","start":289,"term_id":"IDPO:0000011","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The electron density map clearly shows side chain features, and it allowed us to identify the segment as a fragment of P7 protein (Figure 1D). P7 protein is thought to be a nonspecific nucleic acid binding protein (Ueda et al., 1997\n). This fragment of P7 protein binds tightly to part of P3 protein with a β sheet structure (Figure 1D). This tight interaction between the core and the nucleic acid binding protein P7 might be important for the transport of nucleic acids into viral particles during the process of viral assembly.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"x-ray crystallography evidence used in manual assertion","version":3,"reference_html":"The atomic structure of rice dwarf virus reveals the self-assembly mechanism of component proteins. <i> Nakagawa A, Miyazaki N, Taka J, Naitow H, Ogawa A, Fujimoto Z, Mizuno H, Higashi T, Watanabe Y, Omura T, Cheng RH, Tsukihara T. </i> Structure, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"1UF2"}],"term_name":"disorder to order","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP02487r004","ec_ontology":"ECO","end":300,"term_id":"GO:0005515","start":289,"version":4,"statement":[{"text":"The electron density map clearly shows side chain features, and it allowed us to identify the segment as a fragment of P7 protein (Figure 1D). P7 protein is thought to be a nonspecific nucleic acid binding protein (Ueda et al., 1997\n). This fragment of P7 protein binds tightly to part of P3 protein with a β sheet structure (Figure 1D). This tight interaction between the core and the nucleic acid binding protein P7 might be important for the transport of nucleic acids into viral particles during the process of viral assembly.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P22472","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"14527391","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1UF2"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"fquaglia","reference_html":"The atomic structure of rice dwarf virus reveals the self-assembly mechanism of component proteins. <i> Nakagawa A, Miyazaki N, Taka J, Naitow H, Ogawa A, Fujimoto Z, Mizuno H, Higashi T, Watanabe Y, Omura T, Cheng RH, Tsukihara T. </i> Structure, 2003","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":300,"region_id":"DP02487r005","reference_id":"14527391","start":289,"term_id":"GO:0060090","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The electron density map clearly shows side chain features, and it allowed us to identify the segment as a fragment of P7 protein (Figure 1D). P7 protein is thought to be a nonspecific nucleic acid binding protein (Ueda et al., 1997). This fragment of P7 protein binds tightly to part of P3 protein with a β sheet structure (Figure 1D). This tight interaction between the core and the nucleic acid binding protein P7 might be important for the transport of nucleic acids into viral particles during the process of viral assembly.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"x-ray crystallography evidence used in manual assertion","version":4,"reference_html":"The atomic structure of rice dwarf virus reveals the self-assembly mechanism of component proteins. <i> Nakagawa A, Miyazaki N, Taka J, Naitow H, Ogawa A, Fujimoto Z, Mizuno H, Higashi T, Watanabe Y, Omura T, Cheng RH, Tsukihara T. </i> Structure, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"1UF2"}],"term_name":"molecular adaptor activity","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_06","length":506,"ncbi_taxon_id":142805,"date":"2019-12-27T12:46:31.012Z","organism":"Rice dwarf virus (isolate O)","features":{"gene3D":[],"pfam":[{"id":"PF07236","name":"Phytoreovirus S7 protein","start":1,"end":505}]},"disprot_id":"DP02487","regions_counter":5,"dataset":["Viral proteins"],"UniParc":"UPI0000138C93","uniref100":"UniRef100_P22473","uniref90":"UniRef90_P22473","uniref50":"UniRef50_P22473","genes":[],"disorder_content":0.9762845849802372,"disprot_consensus":{"full":[{"start":1,"end":288,"type":"D"},{"start":289,"end":300,"type":"T"},{"start":301,"end":506,"type":"D"}],"Structural state":[{"start":1,"end":288,"type":"D"},{"start":301,"end":506,"type":"D"}],"Structural transition":[{"start":289,"end":300,"type":"T"}],"Molecular function":[{"start":289,"end":300,"type":"F"}]}},{"acc":"O28769","name":"HAMP domain-containing protein","sequence":"MKLTPQIVLIVVVASLVPLSVLGYLTIAGMTSSAEEAKQGVTTVSQEYLTKAGEEAVRMKAQDLALAVQTYIEAKMKLENKTMLTTFDLIQDPKFRSLGAQRWGAKEYTWVGAGNKVAGRDVAVILTHPAFTGQYEKYLGVDVAMLRWNETMPELYNLLLKITENPEAPKPVCGYYHWDDPETPEKEEIPKYLCHYPTTIKVYDPISKGQLWVVVGTSAYIDGYFQYLTQNPANPAENIASEISKSVEGAIQQVYYALGIAAAIAIVFVIVLAVFTTSTITRPIIELSNTADKIAEGNLEAEVPHQNRADEIGILAKSIERLRRSLKVAMESLEEALK","taxonomy":["Archaea","Euryarchaeota","Archaeoglobi","Archaeoglobales","Archaeoglobaceae","Archaeoglobus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":233,"region_id":"DP02488r001","reference_id":"24568954","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The final model comprises four chains of the fragment N234 to K338.","type":"Methods"},{"text":"When tracing the density it became obvious that there were actually 4 chains in the asymmetric unit, corresponding to the C-terminal fragment spanning residues N234 to K338.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"A soluble mutant of the transmembrane receptor Af1503 features strong changes in coiled-coil periodicity. <i> Hartmann MD, Dunin-Horkawicz S, Hulko M, Martin J, Coles M, Lupas AN. </i> J Struct Biol, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4CQ4"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":338,"ncbi_taxon_id":224325,"date":"2019-12-27T12:56:49.329Z","organism":"Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)","features":{"gene3D":[],"pfam":[{"id":"PF00672","name":"HAMP domain","start":276,"end":327}]},"disprot_id":"DP02488","regions_counter":1,"dataset":[],"UniParc":"UPI0000056CE3","uniref100":"UniRef100_A0A117KMG2","uniref90":"UniRef90_A0A117KMG2","uniref50":"UniRef50_A0A117KMG2","genes":[{"olnNames":[{"value":"AF_1503","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAB89755.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAB89755.1"}}]}]}],"alphafold_very_low_content":0.005917159763313609,"disorder_content":0.6893491124260355,"disprot_consensus":{"full":[{"start":1,"end":233,"type":"D"}],"Structural state":[{"start":1,"end":233,"type":"D"}]}},{"acc":"Q9YIJ1","name":"Capsid protein","sequence":"MSFVDHPPDWLEEVGEGLREFLGLEAGPPKPKPNQQHQDQARGLVLPGYNYLGPGNGLDRGEPVNRADEVAREHDISYNEQLEAGDNPYLKYNHADAEFQEKLADDTSFGGNLGKAVFQAKKRVLEPFGLVEEGAKTAPTGKRIDDHFPKRKKARTEEDSKPSTSSDAEAGPSGSQQLQIPAQPASSLGADTMSAGGGGPLGDNNQGADGVGNASGDWHCDSTWMGDRVVTKSTRTWVLPSYNNHQYREIKSGSVDGSNANAYFGYSTPWGYFDFNRFHSHWSPRDWQRLINNYWGFRPRSLRVKIFNIQVKEVTVQDSTTTIANNLTSTVQVFTDDDYQLPYVVGNGTEGCLPAFPPQVFTLPQYGYATLNRDNTENPTERSSFFCLEYFPSKMLRTGNNFEFTYNFEEVPFHSSFAPSQNLFKLANPLVDQYLYRFVSTNNTGGVQFNKNLAGRYANTYKNWFPGPMGRTQGWNLGSGVNRASVSAFATTNRMELEGASYQVPPQPNGMTNNLQGSNTYALENTMIFNSQPANPGTTATYLEGNMLITSESETQPVNRVAYNVGGQMATNNQSSTTAPATGTYNLQEIVPGSVWMERDVYLQGPIWAKIPETGAHFHPSPAMGGFGLKHPPPMMLIKNTPVPGNITSFSDVPVSSFITQYSTGQVTVEMEWELKKENSKRWNPEIQYTNNYNDPQFVDFAPDSTGEYRTTRPIGTRYLTRPL","taxonomy":["Viruses","Monodnaviria","Shotokuvirae","Cossaviricota","Quintoviricetes","Piccovirales","Parvoviridae","Parvovirinae","Dependoparvovirus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":208,"region_id":"DP02489r001","reference_id":"23926356","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"There was no ordered electron density observed for residues 1 to 208.","type":"Methods"},{"text":"The first 208 amino acids of the VP, comprising the VP1 unique region with a phospholipase A2 domain, the VP1/VP2 common region (residues 137 to 192), and the first 15 residues of VP3, are not observed.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structural insights into adeno-associated virus serotype 5. <i> Govindasamy L, DiMattia MA, Gurda BL, Halder S, McKenna R, Chiorini JA, Muzyczka N, Zolotukhin S, Agbandje-McKenna M. </i> J Virol, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3NTT"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-02T09:16:50.093Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":724,"ncbi_taxon_id":82300,"date":"2019-12-27T13:07:23.397Z","organism":"Adeno-associated virus - 5","features":{"gene3D":[{"start":209,"end":724,"id":"G3DSA:2.170.30.10","name":"Parvovirus coat protein VP1/VP2"}],"pfam":[{"id":"PF00740","name":"Parvovirus coat protein VP1/VP2","start":203,"end":695},{"id":"PF08398","name":"Phospholipase A2-like domain","start":42,"end":121}]},"disprot_id":"DP02489","regions_counter":1,"dataset":["Viral proteins"],"UniParc":"UPI0000042A77","uniref100":"UniRef100_Q9YIJ1","uniref90":"UniRef90_Q9YIJ1","uniref50":"UniRef50_P03135","genes":[{"name":{"value":"cap","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAA77024.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA77024.1"}}]},"synonyms":[{"value":"VP1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAD13756.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD13756.1"}}]}]}],"disorder_content":0.287292817679558,"disprot_consensus":{"full":[{"start":1,"end":208,"type":"D"}],"Structural state":[{"start":1,"end":208,"type":"D"}]}},{"acc":"D1A4G7","name":"ESX secretion system protein EccC","sequence":"MSTVLVRRKERRQPPQMPRGEILLESPPELPEVVTNSFQNVLMYLPMAAGSAAMVFTFLNHRNTLQLVAGGMFALSMFGMMFGQLSQQSGERKTKLNSARRDYLRYLGQVRQRVRKAAKQQREALEWNNPAPGRLWSMVMSPRLWERRSSDADFAQVRIGAGPQRLAVQLIPPETKPVEDLEPMSAGALRRFLRAHSTVPDLPVAISLRSFARILPDGDPKAVYGMVRALIMQLAAFHSPDDVRITVCASRERMPQWQWMKWLPHSLHPTEYDAAGQVRLLTHSLVELESMLGPEIKDRGMFGASRAPAEPFHLVIVDGGQASYDSQIASDGIDGVCVIDLTGSVAETNEATMLRLRVTPERVYVVKRDRAGKEVLSSVGRPDQASIAEAEALARQLAPFRTSAADEPEEDVLSANMTLTSLLHIDNPYNLDPAVLWRPRPQRNRLRVPIGLDADGRPLELDIKESAQGGMGPHGLCIGATGSGKSELLRTLVLALAMTHSPEVLNFVLVDFKGGATFLGMEGLRHVSAIITNLEEELPLVDRMYDALHGEMVRRQEHLRHSGNYASLRDYEKARMEGAPLPPMPTLFIVLDEFSELLSAKPDFAELFVMIGRLGRSLGVHLLLASQRLEEGKLRGLDTHLSYRIGLRTFSAMESRVVLGVPDAYELPPSPGNGYLKFATEPLVRFKAAYVSGPVDEEPQTRSEGPQIVRQVLPYLTDYIRPQVVEQPQPEQRAEENKSSESLFDVVVRQLAGHGPEPHQIWLPPLDVPPTLDELLPPLSPSAAHGYTADGWEWRGRLHAVVGLVDRPFDQRRDPYWLDLSGGAGHVGVAGGPQTGKSTMLRTLITSLALLHTPQEVQFYCLDFGGGTLAGLAELPHVGSVATRLDADRIRRTVAEVSALLEQREQEFTERGIDSMATYRRLRATGEYAGDGFGDVFLVVDNWLTLRQDYEALEDSITQLAARGLGYGIHVVLSSNKWSEFRTSIRDLLGTKLELRLGDPYESEVDRKKAANVPENRPGRGLTRDGYHFLTALPRIDGDTSAETLTEGIATTVKTIREAWHGPTAPPVRMLPNVLPAAQLPSAAESGTRIPIGIDEDSLSPVYLDFNTDPHFLVFGDTECGKSNLLRLITAGIIERYTPQQARLIFIDYSRSLLDVATTEHQIGYAASSTAASSLVRDIKGAMEARLPPPDLTPEQLRSRSWWTGAELFLVVDDYEMVATSDNPLRPLAELLPQARDIGLHLIIARSMGGAGRALYEPIIQRIKEMASPGLVMSGNKDEGILLGNVKPHKLPQGRGYFVERRSGTRLIQTAYRES","taxonomy":["Bacteria","Actinobacteria","Streptosporangiales","Thermomonosporaceae","Thermomonospora"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":413,"region_id":"DP02490r001","reference_id":"25865481","start":200,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Although the full protein is present in the crystal (Figure S3C), the N-terminal “DUF” domain and linker1 are disordered in the structure and could not be modeled","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Substrates Control Multimerization and Activation of the Multi-Domain ATPase Motor of Type VII Secretion. <i> Rosenberg OS, Dovala D, Li X, Connolly L, Bendebury A, Finer-Moore J, Holton J, Cheng Y, Stroud RM, Cox JS. </i> Cell, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4NH0"},{"db":"PDB","id":"4N1A"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Biological process","ec_ontology":"ECO","end":413,"region_id":"DP02490r002","reference_id":"25865481","start":200,"term_id":"GO:0051179","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Although the full protein is present in the crystal (Figure S3C), the N-terminal “DUF” domain and linker1 are disordered in the structure and could not be modeled","type":"Results"},{"text":"The DUF domain, which is required for secretion in vivo","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"x-ray crystallography evidence used in manual assertion","version":4,"reference_html":"Substrates Control Multimerization and Activation of the Multi-Domain ATPase Motor of Type VII Secretion. <i> Rosenberg OS, Dovala D, Li X, Connolly L, Bendebury A, Finer-Moore J, Holton J, Cheng Y, Stroud RM, Cox JS. </i> Cell, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4NH0"},{"db":"PDB","id":"4N1A"}],"term_name":"localization","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2020_06","length":1315,"ncbi_taxon_id":471852,"date":"2019-12-27T13:39:54.873Z","organism":"Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / NBRC 15933 / NCIMB 10081 / Henssen B9)","features":{"gene3D":[],"pfam":[{"id":"PF01580","name":"FtsK/SpoIIIE family","start":443,"end":629},{"id":"PF01580","name":"FtsK/SpoIIIE family","start":804,"end":1036},{"id":"PF01580","name":"FtsK/SpoIIIE family","start":1090,"end":1186}]},"disprot_id":"DP02490","regions_counter":2,"dataset":[],"UniParc":"UPI0001BD160D","uniref100":"UniRef100_D1A4G7","uniref90":"UniRef90_D1A4G7","uniref50":"UniRef50_D1A4G7","genes":[{"name":{"value":"eccC","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"25865481","url":"http://www.ncbi.nlm.nih.gov/pubmed/25865481","alternativeUrl":"https://europepmc.org/abstract/MED/25865481"}}]},"olnNames":[{"value":"Tcur_0607"}]}],"alphafold_very_low_content":0.0311787072243346,"disorder_content":0.16273764258555132,"disprot_consensus":{"full":[{"start":200,"end":413,"type":"D"}],"Structural state":[{"start":200,"end":413,"type":"D"}],"Biological process":[{"start":200,"end":413,"type":"F"}]}},{"acc":"Q9WBP8","name":"Capsid protein","sequence":"MAADGYLPDWLEDNLSEGIREWWDLKPGAPKPKANQQKQDDGRGLVLPGYKYLGPFNGLDKGEPVNAADAAALEHDKAYDQQLKAGDNPYLRYNHADAEFQERLQEDTSFGGNLGRAVFQAKKRVLEPLGLVEEGAKTAPGKKRPVEQSPQEPDSSSGIGKTGQQPAKKRLNFGQTGDSESVPDPQPLGEPPATPAAVGPTTMASGGGAPMADNNEGADGVGNASGNWHCDSTWLGDRVITTSTRTWALPTYNNHLYKQISSASTGASNDNHYFGYSTPWGYFDFNRFHCHFSPRDWQRLINNNWGFRPKRLNFKLFNIQVKEVTTNDGVTTIANNLTSTVQVFSDSEYQLPYVLGSAHQGCLPPFPADVFMIPQYGYLTLNNGSQAVGRSSFYCLEYFPSQMLRTGNNFTFSYTFEEVPFHSSYAHSQSLDRLMNPLIDQYLYYLNRTQNQSGSAQNKDLLFSRGSPAGMSVQPKNWLPGPCYRQQRVSKTKTDNNNSNFTWTGASKYNLNGRESIINPGTAMASHKDDEDKFFPMSGVMIFGKESAGASNTALDNVMITDEEEIKATNPVATERFGTVAVNFQSSSTDPATGDVHAMGALPGMVWQDRDVYLQGPIWAKIPHTDGHFHPSPLMGGFGLKNPPPQILIKNTPVPANPPAEFSATKFASFITQYSTGQVSVEIEWELQKENSKRWNPEVQYTSNYAKSANVDFTVDNNGLYTEPRPIGTRYLTRPL","taxonomy":["Viruses","Monodnaviria","Shotokuvirae","Cossaviricota","Quintoviricetes","Piccovirales","Parvoviridae","Parvovirinae","Dependoparvovirus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":216,"region_id":"DP02491r001","reference_id":"26962225","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"As reported for other AAV structures, the VP was ordered from residue 217 within the VP3 common region, with the VP1u and VP1/2 common regions being disordered ","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"Characterization of the Adeno-Associated Virus 1 and 6 Sialic Acid Binding Site. <i> Huang LY, Patel A, Ng R, Miller EB, Halder S, McKenna R, Asokan A, Agbandje-McKenna M. </i> J Virol, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-06T14:14:23.462Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":127,"end":131,"reference_id":"26962225","reference_source":"pmid","reference_html":"Characterization of the Adeno-Associated Virus 1 and 6 Sialic Acid Binding Site. <i> Huang LY, Patel A, Ng R, Miller EB, Halder S, McKenna R, Asokan A, Agbandje-McKenna M. </i> J Virol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0009293","term_name":"transduction","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP02491r002","statement":[{"text":"Residues 129, 418, and 642 have been reported to play a role in AAV1 and AAV6 transduction (62, 63). Residue 129 is not ordered in the AAV structures, while T502 is at a distance of 38.9 and 35.4 Å from 418 and 642, respectively, located on the interior surface of the capsid. ","type":"Discussion"},{"text":"Annotation pertaining residue Leu129.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-06T14:14:22.559Z"},"term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The transfer of genetic information to a bacterium from a bacteriophage or between bacterial or yeast cells mediated by a phage vector.\" [ISBN:0198506732]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2020_06","length":736,"ncbi_taxon_id":85106,"date":"2019-12-27T14:22:26.327Z","organism":"Adeno-associated virus - 1","features":{"gene3D":[{"start":217,"end":736,"id":"G3DSA:2.170.30.10","name":"Parvovirus coat protein VP1/VP2"}],"pfam":[{"id":"PF00740","name":"Parvovirus coat protein VP1/VP2","start":213,"end":708},{"id":"PF08398","name":"Phospholipase A2-like domain","start":43,"end":122}]},"disprot_id":"DP02491","regions_counter":2,"dataset":["Viral proteins"],"UniParc":"UPI00000F6E15","uniref100":"UniRef100_Q9WBP8","uniref90":"UniRef90_Q1I030","uniref50":"UniRef50_P03135","genes":[],"disorder_content":0.29347826086956524,"disprot_consensus":{"full":[{"start":1,"end":216,"type":"D"}],"Structural state":[{"start":1,"end":216,"type":"D"}],"Biological process":[{"start":127,"end":131,"type":"F"}]}},{"acc":"Q808Y3","name":"Capsid protein","sequence":"MAADGYLPDWLEDNLSEGIREWWDLKPGAPKPKANQQKQDDGRGLVLPGYKYLGPFNGLDKGEPVNAADAAALEHDKAYDQQLKAGDNPYLRYNHADAEFQERLQEDTSFGGNLGRAVFQAKKRVLEPLGLVEEGAKTAPGKKRPVEQSPQEPDSSSGIGKTGQQPAKKRLNFGQTGDSESVPDPQPLGEPPAAPSGLGPNTMASGGGAPMADNNEGADGVGNSSGNWHCDSTWLGDRVITTSTRTWALPTYNNHLYKQISNGTSGGSTNDNTYFGYSTPWGYFDFNRFHCHFSPRDWQRLINNNWGFRPKRLNFKLFNIQVKEVTTNEGTKTIANNLTSTVQVFTDSEYQLPYVLGSAHQGCLPPFPADVFMVPQYGYLTLNNGSQALGRSSFYCLEYFPSQMLRTGNNFQFSYTFEDVPFHSSYAHSQSLDRLMNPLIDQYLYYLVRTQTTGTGGTQTLAFSQAGPSSMANQARNWVPGPCYRQQRVSTTTNQNNNSNFAWTGAAKFKLNGRDSLMNPGVAMASHKDDDDRFFPSSGVLIFGKQGAGNDGVDYSQVLITDEEEIKATNPVATEEYGAVAINNQAANTQAQTGLVHNQGVIPGMVWQNRDVYLQGPIWAKIPHTDGNFHPSPLMGGFGLKHPPPQILIKNTPVPADPPLTFNQAKLNSFITQYSTGQVSVEIEWELQKENSKRWNPEIQYTSNYYKSTNVDFAVNTEGVYSEPRPIGTRYLTRNL","taxonomy":["Viruses","Monodnaviria","Shotokuvirae","Cossaviricota","Quintoviricetes","Piccovirales","Parvoviridae","Parvovirinae","Dependoparvovirus","unclassified Dependoparvovirus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":216,"region_id":"DP02492r001","reference_id":"26334681","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Amino acid residues 1–217, which includes the VP1u (1–137), the VP1/2 common region (138–202), and the first 15 N-terminal residues of VP3 are disordered in the density maps.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structure of neurotropic adeno-associated virus AAVrh.8. <i> Halder S, Van Vliet K, Smith JK, Duong TT, McKenna R, Wilson JM, Agbandje-McKenna M. </i> J Struct Biol, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4RSO"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-02T11:08:39.856Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":736,"ncbi_taxon_id":226582,"date":"2019-12-27T14:34:58.331Z","organism":"Non-human primate Adeno-associated virus","features":{"gene3D":[{"start":217,"end":736,"id":"G3DSA:2.170.30.10","name":"Parvovirus coat protein VP1/VP2"}],"pfam":[{"id":"PF00740","name":"Parvovirus coat protein VP1/VP2","start":213,"end":708},{"id":"PF08398","name":"Phospholipase A2-like domain","start":43,"end":122}]},"disprot_id":"DP02492","regions_counter":1,"dataset":["Viral proteins"],"UniParc":"UPI0000186729","uniref100":"UniRef100_Q808Y3","uniref90":"UniRef90_Q808Y3","uniref50":"UniRef50_P03135","genes":[{"name":{"value":"VP1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAO88183.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAO88183.1"}}]}}],"disorder_content":0.29347826086956524,"disprot_consensus":{"full":[{"start":1,"end":216,"type":"D"}],"Structural state":[{"start":1,"end":216,"type":"D"}]}},{"acc":"P21401","name":"Envelopment polyprotein","sequence":"MYVLLTILTSVLVCEAIIRVSLSSTREETCFGDSTNPEMIEGAWDSLREEEMPEELSCSISGIREVKTSSQELYRALKAIIAADGLNNITCHGKDPEDKISLIKGPPHKKRVGIVRCERRRDAKQIGRKTMAGIAMTVLPALAVFALAPVVFAEDPHLRNRPGKGHNYIDGMTQEDATCKPVTYAGACSSFDVLLEKGKFPLFQSYAHHRTLLEAVHDTIIAKADPPSCDLLSAHGNPCMKEKLVMKTHCPNDYQSAHHLNNDGKMASVKCPPKYELTEDCNFCRQMTGASLKKGSYPLQDLFCQSSEDDGSKLKTKMKGVCEVGVQALKKCDGQLSTAHEVVPFAVFKNSKKVYLDKLDLKTEENLLPDSFVCFEHKGQYKGTMDSGQTKRELKSFDISQCPKIGGHGSKKCTGDAAFCSAYECTAQYANAYCSHANGSGIVQIQVSGVWKKPLCVGYERVVVKRELSAKPIQRVEPCTTCITKCEPHGLVVRSTGFKISSAVACASGVCVTGSQSPSTEITLKYPGISQSSGGDIGVHMAHDDQSVSSKIVAHCPPQDPCLVHDCIVCAHGLINYQCHTALSAFVVVFVFSSIAIICLAILYRVLKCLKIAPRKVLNPLMWITAFIRWIYKKMVARVADNINQVNREIGWMEGGQLVLGNPAPIPRHAPIPRYSTYLMLLLIVSYASACSELIQASSRITTCSTEGVNTKCRLSGTALIRAGSVGAEACLMLKGVKEDQTKFLKLKTVSSELSCREGQSYWTGSFSPKCLSSRRCHLVGECHVNRCLSWRDNETSAEFSFVGESTTMRENKCFEQCGGWGCGCFNVNPSCLFVHTYLQSVRKEALRVFNCIDWVHKLTLEITDFDGSVSTIDLGASSSRFTNWGSVSLSLDAEGISGSNSFSFIESPGKGYAIVDEPFSEIPRQGFLGEIRCNSESSVLSAHESCLRAPNLISYKPMIDQLECTTNLIDPFVVFERGSLPQTRNDKTFAASKGNRGVQAFSKGSVQADLTLMFDNFEVDFVGAAVSCDAAFLNLTGCYSCNAGARVCLSITSTGTGSLSAHNKDGSLHIVLPSENGTKDQCQILHFTVPEVEEEFMYSCDGDERPLLVKGTLIAIDPFDDRREAGGESTVVNPKSGSWNFFDWFSGLMSWFGGPLKTILLICLYVALSIGLFFLLIYLGGTGLSKMWLAATKKAS","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Polyploviricotina","Ellioviricetes","Bunyavirales","Phenuiviridae","Phlebovirus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":370,"region_id":"DP02493r001","reference_id":"30590046","start":154,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Interestingly, only residues constituting domain B were resolved in our crystallographic dataset (residue numbers 370–379 and 397–437). Electron density corresponding to both domain A and the β-ribbon domain of RVFV Gn was not visible and could not be sterically accommodated in the RVFV Gn-Fab RV-Gn1 crystal, indicating that these regions were likely cleaved during crystallogenesis","type":"Results"},{"text":"Previous structural analyses of RVFV Gn have revealed a triangular organization composed of three domains: domain A (residues 154–300), domain B (residues 366–439), and a β-ribbon domain (residues 301–365 and 440–469)","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"A Protective Monoclonal Antibody Targets a Site of Vulnerability on the Surface of Rift Valley Fever Virus. <i> Allen ER, Krumm SA, Raghwani J, Halldorsson S, Elliott A, Graham VA, Koudriakova E, Harlos K, Wright D, Warimwe GM, Brennan B, Huiskonen JT, Dowall SD, Elliott RM, Pybus OG, Burton DR, Hewson R, Doores KJ, Bowden TA. </i> Cell Rep, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6I9I"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":395,"region_id":"DP02493r002","reference_id":"30590046","start":379,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Interestingly, only residues constituting domain B were resolved in our crystallographic dataset (residue numbers 370–379 and 397–437). Electron density corresponding to both domain A and the β-ribbon domain of RVFV Gn was not visible and could not be sterically accommodated in the RVFV Gn-Fab RV-Gn1 crystal, indicating that these regions were likely cleaved during crystallogenesis","type":"Results"},{"text":"Previous structural analyses of RVFV Gn have revealed a triangular organization composed of three domains: domain A (residues 154–300), domain B (residues 366–439), and a β-ribbon domain (residues 301–365 and 440–469)","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"A Protective Monoclonal Antibody Targets a Site of Vulnerability on the Surface of Rift Valley Fever Virus. <i> Allen ER, Krumm SA, Raghwani J, Halldorsson S, Elliott A, Graham VA, Koudriakova E, Harlos K, Wright D, Warimwe GM, Brennan B, Huiskonen JT, Dowall SD, Elliott RM, Pybus OG, Burton DR, Hewson R, Doores KJ, Bowden TA. </i> Cell Rep, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6I9I"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":469,"region_id":"DP02493r003","reference_id":"30590046","start":440,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Interestingly, only residues constituting domain B were resolved in our crystallographic dataset (residue numbers 370–379 and 397–437). Electron density corresponding to both domain A and the β-ribbon domain of RVFV Gn was not visible and could not be sterically accommodated in the RVFV Gn-Fab RV-Gn1 crystal, indicating that these regions were likely cleaved during crystallogenesis","type":"Results"},{"text":"Previous structural analyses of RVFV Gn have revealed a triangular organization composed of three domains: domain A (residues 154–300), domain B (residues 366–439), and a β-ribbon domain (residues 301–365 and 440–469)","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"A Protective Monoclonal Antibody Targets a Site of Vulnerability on the Surface of Rift Valley Fever Virus. <i> Allen ER, Krumm SA, Raghwani J, Halldorsson S, Elliott A, Graham VA, Koudriakova E, Harlos K, Wright D, Warimwe GM, Brennan B, Huiskonen JT, Dowall SD, Elliott RM, Pybus OG, Burton DR, Hewson R, Doores KJ, Bowden TA. </i> Cell Rep, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6I9I"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":1197,"ncbi_taxon_id":11589,"date":"2019-12-27T14:45:13.529Z","organism":"Rift valley fever virus (strain ZH-548 M12)","features":{"gene3D":[],"pfam":[{"id":"PF07243","name":"Phlebovirus glycoprotein G1","start":156,"end":689},{"id":"PF07245","name":"Phlebovirus glycoprotein G2 fusion domain","start":691,"end":1012},{"id":"PF07246","name":"Phlebovirus nonstructural protein NS-M","start":1,"end":90},{"id":"PF07246","name":"Phlebovirus nonstructural protein NS-M","start":92,"end":135},{"id":"PF19019","name":"Phlebovirus glycoprotein G2 C-terminal domain","start":1027,"end":1196}]},"disprot_id":"DP02493","regions_counter":3,"dataset":["Viral proteins"],"UniParc":"UPI0000138747","uniref100":"UniRef100_P21401","uniref90":"UniRef90_P21401","uniref50":"UniRef50_P21401","genes":[{"name":{"value":"GP"}}],"disorder_content":0.22055137844611528,"disprot_consensus":{"full":[{"start":154,"end":370,"type":"D"},{"start":379,"end":395,"type":"D"},{"start":440,"end":469,"type":"D"}],"Structural state":[{"start":154,"end":370,"type":"D"},{"start":379,"end":395,"type":"D"},{"start":440,"end":469,"type":"D"}]}},{"acc":"O56139","name":"Capsid protein VP1","sequence":"MAADGYLPDWLEDNLSEGIREWWALKPGVPQPKANQQHQDNRRGLVLPGYKYLGPGNGLDKGEPVNEADAAALEHDKAYDQQLKAGDNPYLKYNHADAEFQERLQEDTSFGGNLGRAVFQAKKRILEPLGLVEEAAKTAPGKKRPVDQSPQEPDSSSGVGKSGKQPARKRLNFGQTGDSESVPDPQPLGEPPAAPTSLGSNTMASGGGAPMADNNEGADGVGNSSGNWHCDSQWLGDRVITTSTRTWALPTYNNHLYKQISSQSGASNDNHYFGYSTPWGYFDFNRFHCHFSPRDWQRLINNNWGFRPKKLSFKLFNIQVKEVTQNDGTTTIANNLTSTVQVFTDSEYQLPYVLGSAHQGCLPPFPADVFMVPQYGYLTLNNGSQAVGRSSFYCLEYFPSQMLRTGNNFQFSYTFEDVPFHSSYAHSQSLDRLMNPLIDQYLYYLNRTQGTTSGTTNQSRLLFSQAGPQSMSLQARNWLPGPCYRQQRLSKTANDNNNSNFPWTAASKYHLNGRDSLVNPGPAMASHKDDEEKFFPMHGNLIFGKEGTTASNAELDNVMITDEEEIRTTNPVATEQYGTVANNLQSSNTAPTTRTVNDQGALPGMVWQDRDVYLQGPIWAKIPHTDGHFHPSPLMGGFGLKHPPPQIMIKNTPVPANPPTTFSPAKFASFITQYSTGQVSVEIEWELQKENSKRWNPEIQYTSNYNKSVNVDFTVDTNGVYSEPRPIGTRYLTRNL","taxonomy":["Viruses","Monodnaviria","Shotokuvirae","Cossaviricota","Quintoviricetes","Piccovirales","Parvoviridae","Parvovirinae","Dependoparvovirus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":216,"region_id":"DP02494r001","reference_id":"20444480","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The AAV-3B model contains amino acids 217 to 734 (VP1 numbering)","type":"Results"},{"text":"Interpretable density starts at VP3 residue 15 (residue 217 in the conventional VP1 numbering).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"The structure of adeno-associated virus serotype 3B (AAV-3B): insights into receptor binding and immune evasion. <i> Lerch TF, Xie Q, Chapman MS. </i> Virology, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3KIC"},{"db":"PDB","id":"3KIE"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-02T09:19:38.103Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":736,"ncbi_taxon_id":68742,"date":"2019-12-27T15:03:46.530Z","organism":"Adeno-associated virus 3B","features":{"gene3D":[{"start":217,"end":736,"id":"G3DSA:2.170.30.10","name":"Parvovirus coat protein VP1/VP2"}],"pfam":[{"id":"PF00740","name":"Parvovirus coat protein VP1/VP2","start":213,"end":709},{"id":"PF08398","name":"Phospholipase A2-like domain","start":43,"end":122}]},"disprot_id":"DP02494","regions_counter":1,"dataset":["Viral proteins"],"UniParc":"UPI00000F827D","uniref100":"UniRef100_O56139","uniref90":"UniRef90_A0A0K1P7U4","uniref50":"UniRef50_P03135","genes":[],"disorder_content":0.29347826086956524,"disprot_consensus":{"full":[{"start":1,"end":216,"type":"D"}],"Structural state":[{"start":1,"end":216,"type":"D"}]}},{"acc":"Q928V6","name":"Putative integrase [Bacteriophage A118]","sequence":"MKAAIYIRVSTQEQVENYSIQAQTEKLTALCRSKDWDVYDTFIDGGYSGSNMNRPALNEMLSKLHEIDAVVVYRLDRLSRSQKDTITLIEEYFLKNNVEFVSLSETLDTSSPFGRAMIGILSVFAQLERETIRDRMVMGKIKRIEAGLPLTTAKGRTFGYDVIDTKLYINEEEAKQLRLIYDIFEEEQSITFLQKRLKKLGFKVRTYNRYNNWLTNDLYCGYVSYKDKVHVKGIHEPIISEEQFYRVQEIFSRMGKNPNMNKESASLLNNLVVCSKCGLGFVHRRKDTVSRGKKYHYRYYSCKTYKHTHELEKCGNKIWRADKLEELIIDRVNNYSFASRNIDKEDELDSLNEKLKIEHAKKKRLFDLYINGSYEVSELDSMMNDIDAQINYYEAQIEANEELKKNKKIQENLADLATVDFNSLEFREKQLYLKSLINKIYIDGEQVTIEWL","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Listeriaceae","Listeria"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":350,"region_id":"DP02495r001","reference_id":"28549184","start":133,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"We also analyzed the oligomeric properties of the isolated CC domain (residues 345–405). Despite the absence of the remainder of the CTD into which the CC is embedded, the isolated CC polypeptide is soluble and forms stable dimers at >300 μM concentration","type":"Results"},{"text":"The carboxy-terminal domain (CTD) corresponds to region 133-452.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Coiled-coil interactions mediate serine integrase directionality. <i> Gupta K, Sharp R, Yuan JB, Li H, Van Duyne GD. </i> Nucleic Acids Res, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5UDO"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":452,"region_id":"DP02495r002","reference_id":"28549184","start":400,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"We also analyzed the oligomeric properties of the isolated CC domain (residues 345–405). Despite the absence of the remainder of the CTD into which the CC is embedded, the isolated CC polypeptide is soluble and forms stable dimers at >300 μM concentration","type":"Results"},{"text":"The carboxy-terminal domain (CTD) corresponds to region 133-452.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Coiled-coil interactions mediate serine integrase directionality. <i> Gupta K, Sharp R, Yuan JB, Li H, Van Duyne GD. </i> Nucleic Acids Res, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5UDO"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":452,"ncbi_taxon_id":272626,"date":"2019-12-27T15:18:16.562Z","organism":"Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)","features":{"gene3D":[{"start":1,"end":148,"id":"G3DSA:3.40.50.1390","name":"G3DSA:3.40.50.1390"},{"start":133,"end":256,"id":"G3DSA:1.10.10.2600","name":"G3DSA:1.10.10.2600"}],"pfam":[{"id":"PF00239","name":"Resolvase, N terminal domain","start":3,"end":147},{"id":"PF07508","name":"Recombinase","start":171,"end":253},{"id":"PF13408","name":"Recombinase zinc beta ribbon domain","start":267,"end":333}]},"disprot_id":"DP02495","regions_counter":2,"dataset":[],"UniParc":"UPI00000CC874","uniref100":"UniRef100_A0A3T2NB97","uniref90":"UniRef90_Q9T193","uniref50":"UniRef50_Q9T193","genes":[{"name":{"value":"int","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAC97653.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAC97653.1"}}]}}],"alphafold_very_low_content":0.024336283185840708,"disorder_content":0.5995575221238938,"disprot_consensus":{"full":[{"start":133,"end":350,"type":"D"},{"start":400,"end":452,"type":"D"}],"Structural state":[{"start":133,"end":350,"type":"D"},{"start":400,"end":452,"type":"D"}]}},{"acc":"P56926","name":"Glutamine--tRNA ligase","sequence":"MGAFGWEQDRGAPFSGRSPRILTRMTDAPRPTAGADAPARPPAAPLVAPNFITEIIERDLEAGKYPRVVTRFPPDPSGYAHLGHVFASLLDFNTARQYGGQFNLRMDDTNPELARQEYVDSIADDLKWLGLDWGEHFYYASDYFDRYYAYAEQLIRQGDAYVESVSPEELSRLRGNATTPGTPSPYRDRSVEENLDLLRRMKAGEFADGEHVLRAKIDLTAPNMKLRDPVLYRIVNKPHFRTSDEWHIYPAYDFEHPLQDAIEGVTHSMCSLEFVDNRAIYDWLMEKLNFDPRPHQYEFGRRGLEYTITSKRKLRELVQAGRVSGWDDPRMPTLRAQRRLGVTPEAVRAFAAQIGVSRTNRTVDIAVYENAVRDDLNHRAPRVMAVLDPVKVTLTNLDGEKTLSLPYWPHDVVRDSPDGLVGMPGGGRVAPEEAVRDVPLTRELYIERDDFSPAPPKGFKRLTPGGTVRLRGAGIIRADDFGTDEAGQVTHIRATLLGEDAKAAGVIHWVSAERALPAEFRLYDRLFRVPHPEGENADVEDDSAGPAEHEAEPGAGQETAPVSQGFMRYLTPDSLRVLRGYVEPSVAGDPADTRYQFERQGYFWRDPVELERVDSREDALVFGRIITLKDTWGKQGGGTQQKAEGKKRPSTKGRGPDEVRGEGSSSPAKAHAPKAQPLTPEQDAEFTRLLGLGASEGDARTIARDPALLAFVGGAAPGDTFAQVASWTVNELVAGLRAGEVKVRAADLAPLAEGVASGQLSARIAREALARAAASGDAPLTIIEREGLNAGLSAEALQQVVAQVIAANPDKAEAYRGGKTALLGFFTGQVMRATAGKADPQALAAALKDALA","taxonomy":["Bacteria","Deinococcus-Thermus","Deinococci","Deinococcales","Deinococcaceae","Deinococcus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":852,"region_id":"DP02496r001","reference_id":"17284460","start":633,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The structural organization of Dr GlnRS was established by separate multiple sequence alignments. A first alignment of known bacterial GlnRSs shows that Dr GlnRS is highly similar to other bacterial GlnRSs, with the exception of a few insertions (17, 27 and 5 additional residues in the structured region 410–433 and in two loops 535–565 and 610–620, respectively) and the presence of a short N-terminal extension (M1–A43) and a long C-terminal appendix (G633–A862)","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins from an ancient and the modern pathways of aminoacyl-tRNA formation. <i> Deniziak M, Sauter C, Becker HD, Paulus CA, Giegé R, Kern D. </i> Nucleic Acids Res, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2HZ7"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":852,"region_id":"DP02496r002","reference_id":"17284460","start":633,"term_id":"GO:0000049","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The structural organization of Dr GlnRS was established by separate multiple sequence alignments. A first alignment of known bacterial GlnRSs shows that Dr GlnRS is highly similar to other bacterial GlnRSs, with the exception of a few insertions (17, 27 and 5 additional residues in the structured region 410–433 and in two loops 535–565 and 610–620, respectively) and the presence of a short N-terminal extension (M1–A43) and a long C-terminal appendix (G633–A862)","type":"Results"},{"text":"Kinetic investigations and tRNA-binding experiments of full length and Yqey-truncated GlnRSs reveal that the Yqey domain is involved in tRNAGln recognition.","type":"Abstract"},{"text":"Remarkably, the Yqey domain has a disordered orientation in the structure of GlnRS where it acts as a tRNAGln affinity enhancer.","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"x-ray crystallography evidence used in manual assertion","version":4,"reference_html":"Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins from an ancient and the modern pathways of aminoacyl-tRNA formation. <i> Deniziak M, Sauter C, Becker HD, Paulus CA, Giegé R, Kern D. </i> Nucleic Acids Res, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"2HZ7"}],"term_name":"tRNA binding","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a transfer RNA.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":852,"region_id":"DP02496r003","reference_id":"17284460","start":633,"term_id":"GO:0098772","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Remarkably, the Yqey domain has a disordered orientation in the structure of GlnRS where it acts as a tRNAGln affinity enhancer.","type":"Introduction"},{"text":"Taken together, the Yqey flexible module increases the catalytic efficiency of GlnRS for both tRNAGln-dependent Gln activation and tRNAGln charging and is involved in binding of tRNAGln to GlnRS.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"enzymatic activity assay evidence used in manual assertion","version":4,"reference_html":"Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins from an ancient and the modern pathways of aminoacyl-tRNA formation. <i> Deniziak M, Sauter C, Becker HD, Paulus CA, Giegé R, Kern D. </i> Nucleic Acids Res, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005801","cross_refs":[{"db":"PDB","id":"2HZ7"}],"term_name":"molecular function regulator","ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_06","length":852,"ncbi_taxon_id":243230,"date":"2019-12-27T15:55:39.991Z","organism":"Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)","features":{"gene3D":[{"start":69,"end":289,"id":"G3DSA:3.40.50.620","name":"HUPs"},{"start":514,"end":632,"id":"G3DSA:2.40.240.10","name":"Ribosomal Protein L25; Chain P"},{"start":514,"end":632,"id":"G3DSA:2.40.240.10","name":"Ribosomal Protein L25; Chain P"},{"start":301,"end":379,"id":"G3DSA:1.10.1160.10","name":"Glutamyl-trna Synthetase; Domain 2"},{"start":793,"end":852,"id":"G3DSA:1.10.10.410","name":"G3DSA:1.10.10.410"},{"start":680,"end":789,"id":"G3DSA:1.10.150.380","name":"G3DSA:1.10.150.380"}],"pfam":[{"id":"PF00749","name":"tRNA synthetases class I (E and Q), catalytic domain","start":68,"end":376},{"id":"PF02637","name":"GatB domain","start":721,"end":851},{"id":"PF03950","name":"tRNA synthetases class I (E and Q), anti-codon binding domain","start":380,"end":411},{"id":"PF03950","name":"tRNA synthetases class I (E and Q), anti-codon binding domain","start":431,"end":496},{"id":"PF20974","name":"tRNA synthetases class I (E and Q), anti-codon binding domain","start":506,"end":606}]},"disprot_id":"DP02496","regions_counter":3,"dataset":[],"UniParc":"UPI000013661A","uniref100":"UniRef100_P56926","uniref90":"UniRef90_P56926","uniref50":"UniRef50_P56926","genes":[{"name":{"value":"glnS","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00126","url":"https://hamap.expasy.org/unirule/MF_00126"}}]},"olnNames":[{"value":"DR_2611"}]}],"alphafold_very_low_content":0.12441314553990611,"disorder_content":0.25821596244131456,"disprot_consensus":{"full":[{"start":633,"end":852,"type":"D"}],"Structural state":[{"start":633,"end":852,"type":"D"}],"Molecular function":[{"start":633,"end":852,"type":"F"}]}},{"acc":"A7YK37","name":"Capsid protein","sequence":"MRMSDGAAPKANGSEASGQDLVPTAVEQAVPIQPVAGSALAAPAAGQINQIDPWIFQNFVQCPLGEFSISPRNTPGEILFDLALGPGLNPYLAHLSAMYTGWVGNMEVQLVLAGNAFTAGKVVVALVPPYFPKGSLTTAQITCFPHVMCDVRTLEPIQLPLLDVRRVLWHATQDQEESMRLVCMLYTPLRTNSPGDESFVVSGRLLSKPAADFNFVYLTPPIERTIYRMVDLPVLQPRLCTHARWPAPIYGLLVDPSLPSNPQWQNGRVHVDGTLLGTTPVSGSWVSCFAAEAAYEFQSGTGEVATFTLIEQDGSAYVPGDRAAPLGYPDFSGQLEIEVQTETTKTGDKLKVTTFEMILGPTTNVDQAPYQGRVYASLTAVASLDLVDGRVRAVPRSIYGFQDVIPEYNDGLLVPLAPPIGPFLPGEVLLRFRTYMRQLDTADAAAEAIDCALPQEFISWFASNAFTVQSDALLLRYRNTLTGQLLFECKLYSEGYIALSYSGSGPLTFPTDGFFEVVSWVPRLFQLASVGSLTTGRTLKQ","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Picornavirales","Caliciviridae","Norovirus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":227,"region_id":"DP02498r001","reference_id":"29563286","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Similar to the apo CW1 murine norovirus P domain structure (PDB code 3LQ6), the CR10 P domain could be divided into P1-1 (residues 228 to 277), P2 (residues 278 to 416), and P1-2 (residues 417 to 530) subdomains.","type":"Results"},{"text":"No density is visible for residues 1-227 of the capsid protein","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Atomic Structure of the Murine Norovirus Protruding Domain and Soluble CD300lf Receptor Complex. <i> Kilic T, Koromyslova A, Malak V, Hansman GS. </i> J Virol, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5OR7"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-02T11:04:45.329Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":541,"ncbi_taxon_id":463724,"date":"2019-12-27T16:22:41.049Z","organism":"Murine norovirus GV/CR10/2005/USA","features":{"gene3D":[{"start":1,"end":225,"id":"G3DSA:2.60.120.20","name":"G3DSA:2.60.120.20"}],"pfam":[{"id":"PF00915","name":"Calicivirus coat protein","start":20,"end":281},{"id":"PF08435","name":"Calicivirus coat protein C-terminal","start":309,"end":537}]},"disprot_id":"DP02498","regions_counter":1,"dataset":["Viral proteins"],"UniParc":"UPI00015C2043","uniref100":"UniRef100_A7YK37","uniref90":"UniRef90_Q2V8W4","uniref50":"UniRef50_Q2V8W4","genes":[],"disorder_content":0.4195933456561922,"disprot_consensus":{"full":[{"start":1,"end":227,"type":"D"}],"Structural state":[{"start":1,"end":227,"type":"D"}]}},{"acc":"A0KJC7","name":"ImpA-related domain protein","sequence":"MSYQHPWCARLLTSLPDEQIRGAVLADEPRWDYVETELVKLGSLAHSQVDLNAVAEACLGLLESRTKDMRVLAQLLRCLQHPAKATPLGAAISLLEAWIQAYWLLAWPGNASQKQRLMVQIVKRFEGALPRICESASAAELAQLLAQAEQLERVWLAQCPDKGELLDPLVMGLKRAQRQQLAQAEANAAGQPQSSGAAAAGSPASVASTASCAGAMVLSGSAGVDVDSSNDRAWRQTQLKVAELLIERQPEVAVGYRLRRHAVWAGITAVPMSGAGNKTPLAPMSADMVDEYRAAMNAPDQGLWQRIEQSLTLAPYWFEGHRLSAEVAEKLGFGAVAQAIAEELGTFLQRLPALRELAFSDGSPFLSPECSRWLQPAKGGSAGIGEAGLAEEVAQRHGEQGIAAALALLDERIAQLKEPRDRFHALLVQAELLAQEGMEALARQHYQHLWQEASRLGLSHWEPGLVNRLESLAAPLSK","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Aeromonadales","Aeromonadaceae","Aeromonas"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":230,"region_id":"DP02499r001","reference_id":"30420757","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The structure of an Ah TssA2A Nt2 domain construct (D231-L374) was solved to 1.76 Å with four subunits (chains A–D) in the asymmetric unit","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structural insights into the function of type VI secretion system TssA subunits. <i> Dix SR, Owen HJ, Sun R, Ahmad A, Shastri S, Spiewak HL, Mosby DJ, Harris MJ, Batters SL, Brooker TA, Tzokov SB, Sedelnikova SE, Baker PJ, Bullough PA, Rice DW, Thomas MS. </i> Nat Commun, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6G7B"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":478,"ncbi_taxon_id":380703,"date":"2019-12-27T16:27:21.474Z","organism":"Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240)","features":{"gene3D":[],"pfam":[{"id":"PF06812","name":"ImpA, N-terminal, type VI secretion system","start":13,"end":111},{"id":"PF16989","name":"Type VI secretion, EvfE, EvfF, ImpA, BimE, VC_A0119, VasJ","start":229,"end":471}]},"disprot_id":"DP02499","regions_counter":1,"dataset":[],"UniParc":"UPI0000E6920F","uniref100":"UniRef100_A0KJC7","uniref90":"UniRef90_Q0PZG1","uniref50":"UniRef50_A0A0H3I372","genes":[{"olnNames":[{"value":"AHA_1844","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ABK39115.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABK39115.1"}}]}]}],"alphafold_very_low_content":0.09414225941422594,"disorder_content":0.4811715481171548,"disprot_consensus":{"full":[{"start":1,"end":230,"type":"D"}],"Structural state":[{"start":1,"end":230,"type":"D"}]}},{"acc":"Q5A3P6","name":"Serine/threonine-protein kinase PKH2","sequence":"MHKFRYSLHQHYSKRNSSDKSKDSPISQNSNEENDSTKLSSSSLQDLHDDLDDIYNNYTLAQGTNNNSVDTLDSENNQAINKFIDKPPAIHGMEPQLPVMHVSSRLSSLGNTTNETGESIAKSAPGTPLSSHSFDFRPHHPRAVTNSSLNVLLDTPNVSSEFNHLVDQTPPNESVERFDDSNNTVDNTEEEENNDDTDEIPKSETLKQNEENWEKKGAAVKTIKTMDGEMKTIRRNVTDFKFGKELGEGSYSTVILATDKITGKQYAVKVLDKRHIIKEKKVKYVNIEKHALNRLSNRLGVISLYFTFQDKDSLYFVLDYASNGELLTLIKRYNTLNEECTRHFGAQILDAIKYMHDNGVIHRDLKPENILLDDKMRIQITDFGTARLLEKKNDESEEYPVDVRAKSFVGTAEYVSPELLENKYCGKPGDVWAFGCIIYQMIAGKPPFKATNEYLTFQKITKLQFAFSAGFPTIIRDLIKKILVLQPSRRATIPEIQKHYFFQSVDFKDFDSIWLSDPPEIGPYKMTAKSMMKVPELNKAPITTVIKKNVKKSTNSNSNTNNVATAVGGSSSNGHKGSSPTPEKEPSPATINNKSTEKVSAASVAAYVLNKPATNQNSSTSEDSSKRSSNSNETRKLSYSQQDYIPGTNILRPQISTRPSVGSYVKTTPSKDRKTLTKVPSNIHQQQEKVKPKVMEVKPATTLEAAWEPYLTHPDERILRIGPVIAHKEPTEPFEKKNKASLHISPLDINKEQRSRSNTSLLTQIVNEVNNNTSELKKVENADESLAIIEPQYNMKRSPTSDSKKSMDIERSASTSGSRISKKAIFKKLGFSHLEKNDSEESNGPSLTEKPQTCTLVVTTHGRALLFIRNDIESNYLLIAEIKLKYPFIHFQELVISQTKFSKLVPSVGVFVISSIDNSLIFEVEKFEVNQWTEALAKSKYNEIGKR","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Debaryomycetaceae","Candida/Lodderomyces clade","Candida"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":232,"region_id":"DP02500r001","reference_id":"23911092","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Later, crystal structure analysis revealed that one molecule of the catalytic domain (aa 233-521, 33.4 kDa) crystallized per asymmetric unit, corresponding to a V M of 2.26 Å 3 /Da and a solvent content of 46% (v/v).","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"PIF-pocket as a target for C. albicans Pkh selective inhibitors. <i> Pastor-Flores D, Schulze JO, Bahí A, Giacometti R, Ferrer-Dalmau J, Passeron S, Engel M, Süss E, Casamayor A, Biondi RM. </i> ACS Chem Biol, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4C0T"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":944,"region_id":"DP02500r002","reference_id":"23911092","start":522,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Later, crystal structure analysis revealed that one molecule of the catalytic domain (aa 233-521, 33.4 kDa) crystallized per asymmetric unit, corresponding to a V M of 2.26 Å 3 /Da and a solvent content of 46% (v/v).","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"PIF-pocket as a target for C. albicans Pkh selective inhibitors. <i> Pastor-Flores D, Schulze JO, Bahí A, Giacometti R, Ferrer-Dalmau J, Passeron S, Engel M, Süss E, Casamayor A, Biondi RM. </i> ACS Chem Biol, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4C0T"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":947,"ncbi_taxon_id":237561,"date":"2019-12-30T10:27:14.247Z","organism":"Candida albicans (strain SC5314 / ATCC MYA-2876)","features":{"gene3D":[],"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":241,"end":502}]},"disprot_id":"DP02500","regions_counter":2,"dataset":[],"UniParc":"UPI000004FA02","uniref100":"UniRef100_Q5A3P6","uniref90":"UniRef90_Q5A3P6","uniref50":"UniRef50_Q5A3P6","genes":[{"name":{"value":"PKH2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"23911092","url":"http://www.ncbi.nlm.nih.gov/pubmed/23911092","alternativeUrl":"https://europepmc.org/abstract/MED/23911092"}}]},"synonyms":[{"value":"PKH1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"24281718","url":"http://www.ncbi.nlm.nih.gov/pubmed/24281718","alternativeUrl":"https://europepmc.org/abstract/MED/24281718"}}]}],"orfNames":[{"value":"CaO19.12690"},{"value":"CaO19.5224"},{"value":"orf19.5224"}],"olnNames":[{"value":"CAALFM_C112410CA"}]}],"alphafold_very_low_content":0.498416050686378,"disorder_content":0.6916578669482577,"disprot_consensus":{"full":[{"start":1,"end":232,"type":"D"},{"start":522,"end":944,"type":"D"}],"Structural state":[{"start":1,"end":232,"type":"D"},{"start":522,"end":944,"type":"D"}]}},{"acc":"P00800","name":"Thermolysin","sequence":"MKMKMKLASFGLAAGLAAQVFLPYNALASTEHVTWNQQFQTPQFISGDLLKVNGTSPEELVYQYVEKNENKFKFHENAKDTLQLKEKKNDNLGFTFMRFQQTYKGIPVFGAVVTSHVKDGTLTALSGTLIPNLDTKGSLKSGKKLSEKQARDIAEKDLVANVTKEVPEYEQGKDTEFVVYVNGDEASLAYVVNLNFLTPEPGNWLYIIDAVDGKILNKFNQLDAAKPGDVKSITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTLPGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAIRSSVHYSQGYNNAFWNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTDYTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGDSLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTHYGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTSQEVASVKQAFDAVGVK","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Bacillus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":232,"region_id":"DP02501r001","reference_id":"26527148","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"No density is visible for residues 1–232 of Thermolysin","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"MeshAndCollect: an automated multi-crystal data-collection workflow for synchrotron macromolecular crystallography beamlines. <i> Zander U, Bourenkov G, Popov AN, de Sanctis D, Svensson O, McCarthy AA, Round E, Gordeliy V, Mueller-Dieckmann C, Leonard GA. </i> Acta Crystallogr D Biol Crystallogr, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5A3Y"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":548,"ncbi_taxon_id":1427,"date":"2019-12-30T11:15:21.393Z","organism":"Bacillus thermoproteolyticus","features":{"gene3D":[{"start":387,"end":547,"id":"G3DSA:1.10.390.10","name":"Neutral Protease Domain 2"}],"pfam":[{"id":"PF01447","name":"Thermolysin metallopeptidase, catalytic domain","start":240,"end":382},{"id":"PF02868","name":"Thermolysin metallopeptidase, alpha-helical domain","start":385,"end":547},{"id":"PF03413","name":"Peptidase propeptide and YPEB domain","start":144,"end":217},{"id":"PF07504","name":"Fungalysin/Thermolysin Propeptide Motif","start":80,"end":128}]},"disprot_id":"DP02501","regions_counter":1,"dataset":[],"UniParc":"UPI0000D4FECD","uniref100":"UniRef100_P00800","uniref90":"UniRef90_P00800","uniref50":"UniRef50_P05806","genes":[{"name":{"value":"npr"}}],"alphafold_very_low_content":0.058394160583941604,"disorder_content":0.4233576642335766,"disprot_consensus":{"full":[{"start":1,"end":232,"type":"D"}],"Structural state":[{"start":1,"end":232,"type":"D"}]}},{"acc":"A0R1T8","name":"LAO/AO transport system ATPase","sequence":"MPHGVVDVPELITVARGGSMRAVGRLLTLVESDRRGEVLAALGPATPRVIGVTGPPGAGKSTTVGAMVGAYRERGLRVAVLAVDPSSPYSGGALLGDRIRMAAHINDPDVLIRSMAARGHLGGLAAAVPAAIRLLAALSYDLIVLETVGVGQSEIEIAAIADPTVVILNPGAGDAVQAAKAGVLEVADLVVVNKADRDGADQTVRDLRAETDVPVLKLVAAQGDGLHELIEAIEAHQRADTPERRRARARSQILSLAQTLLRNHADLDRLSAAVADGSSDAYTAAERLFAGSVD","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Mycobacteriaceae","Mycolicibacterium"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":238,"region_id":"DP02502r001","reference_id":"30198884","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Several proteolysis sites could result in this 6 kDa fragment. For example, 3C protease was used to remove the N-terminal affinity tag, and aberrant cleavage could have occurred at residue Gln237. Alternatively, cleavage could have occurred at Arg238 by the trypsin-like protease II of E. coli (Strongin et al., 1979 ▸) if this protease were retained in tiny amounts after purification.","type":"Results"},{"text":"N-terminal to the first ordered residue of the dimerization domain is a short linker at residue Arg238 followed by the last α-helix of the GTPase domain, via analogy to other family members. As described above, Gln237 and Arg238 are possible proteolytic sites for the fragment crystallized here.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cleavage assay evidence used in manual assertion","version":3,"reference_html":"Ab initio structure solution of a proteolytic fragment using ARCIMBOLDO. <i> Abendroth J, Sankaran B, Myler PJ, Lorimer DD, Edwards TE. </i> Acta Crystallogr F Struct Biol Commun, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","cross_refs":[{"db":"PDB","id":"6CUM"}],"term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":238,"region_id":"DP02502r002","reference_id":"30198884","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Several proteolysis sites could result in this 6 kDa fragment. For example, 3C protease was used to remove the N-terminal affinity tag, and aberrant cleavage could have occurred at residue Gln237. Alternatively, cleavage could have occurred at Arg238 by the trypsin-like protease II of E. coli (Strongin et al., 1979 ▸) if this protease were retained in tiny amounts after purification.","type":"Results"},{"text":"N-terminal to the first ordered residue of the dimerization domain is a short linker at residue Arg238 followed by the last α-helix of the GTPase domain, via analogy to other family members. As described above, Gln237 and Arg238 are possible proteolytic sites for the fragment crystallized here.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Ab initio structure solution of a proteolytic fragment using ARCIMBOLDO. <i> Abendroth J, Sankaran B, Myler PJ, Lorimer DD, Edwards TE. </i> Acta Crystallogr F Struct Biol Commun, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6CUM"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":294,"ncbi_taxon_id":246196,"date":"2020-01-02T09:39:03.266Z","organism":"Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)","features":{"gene3D":[],"pfam":[{"id":"PF03308","name":"Methylmalonyl Co-A mutase-associated GTPase MeaB","start":24,"end":263}]},"disprot_id":"DP02502","regions_counter":2,"dataset":[],"UniParc":"UPI0000E85B8D","uniref100":"UniRef100_A0A653FJG7","uniref90":"UniRef90_A0A653FJG7","uniref50":"UniRef50_A0A220Y787","genes":[{"olnNames":[{"value":"MSMEG_4869","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ABK74390.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABK74390.1"}}]}]}],"alphafold_very_low_content":0.06802721088435375,"disorder_content":0.8095238095238095,"disprot_consensus":{"full":[{"start":1,"end":238,"type":"D"}],"Structural state":[{"start":1,"end":238,"type":"D"}]}},{"acc":"Q28146","name":"Neurexin-1","sequence":"MGTALLQRGGCFLLCLSLLLLGCWAELGSGLEFPGAEGQWTRFPKWNACCESEMSFQLKTRSARGLVLYFDDEGFCDFLELILTRGGRLQLSFSIFCAEPATLLTDTPVNDGAWHNVRIRRQFRNTTLFIDQVEAKWVEVKSKRRDMTVFSGLFVGGLPPELRAAALKLTLASVREREPFKGWIRDVRVNSSLALPVDSGEVKLDDEPPNSGGGSPCEAGEEGEGGVCLNGGVCSVVDDQAVCDCSRTGFRGKDCSQEDNNVEGLAHLMMGDQGKSKEDNNVEGLAHLMMGDQGKEEYIATFKGSEYFCYDLSQNPIQSSSDEITLSFKTLQRNGLMLHTGKSADYVNLALKNGAVSLVINLGSGAFEALVEPVNGKFNDNAWHDVKVTRNLRQTSGIGHAMVNKLHCSVTISVDGILTTTGYTQEDYTMLGSDDFFYVGGSPSTADLPGSPVSNNFMGCLKEVVYKNNDVRLELSRLAKQGDPKMKIHGVVAFKCENVATLDPITFETPESFISLPKWNAKKTGSISFDFRTTEPNGLILFSHGKPRHQKDAKHPQMIKVDFFAIEMLDGHLYLLLDMGSGTIKIKALQKKVNDGEWYHVDFQRDGRSGTISVNTLRTPYTAPGESQILDLDDELYLGGLPENKAGLVFPTEVWTALLNYGYVGCIRDLFIDGQSKDIRQMAEVQSTAGVKPSCSRETAKPCLSNPCKNNGMCRDGWNRYVCDCSGTGYLGRSCEREATVLSYDGSMFMKIQLPVVMHTEAEDVSLRFRSQRAYGILMATTSRDSADTLRLELDAGRVKLTVNLDCIRINCNSSKGPETLFAGYNLNDNEWHTVRVVRRGKSLKLTVDDQQAMTGQMAGDHTRLEFHNIETGIITERRYLSSVPSNFIGHLQSLTFNGMAYIDLCKNGDIDYCELNARFGFRNIIADPVTFKTKSSYVALATLQAYTSMHLFFQFKTTSLDGLILYNSGDGNDFIVVELVKGYLHYVFDLGNGANLIKGSSNKPLNDNQWHNVMISRDTSNLHTVKIDTKITTQITAGARNLDLKSDLYIGGVAKETYKSLPKLVHAKEGFQGCLASVDLNGRLPDLISDALFCNGQIERGCEGPSTTCQEDSCSNQGVCLQQWDGISCDCSMTSFSGPLCNDPGTTYIFSKGGGQITYKWPPNDRPSTRADRLAIGFSTVQKEAVLVRVDSSSGLGDYLELHIHQGKIGVKFNVGTDDIAIEESNAIINDGKYHVVRFTRSGGNATLQVDSWPVIERYPAGNNDNERLAIARQRIPYRLGRVVDEWLLDKGRQLTIFNSQATIIIGGKEQGQPFQGQLSGLYYNGLKVLNMAAENDANIAIVGNVRLVGEVPSSMTTESTATAMQSEMSTSIMETTTTLATSTARRGKPPTKEPVSQTTDDILVASAECPSDDEDIDPCEPSSGGLANPTRAGGREPYPGSAEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYHVDESRNYISNSAQSNGAVVKEKQPSSAKSANKNKKNKDKEYYV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":280,"region_id":"DP02503r001","reference_id":"21620716","start":31,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The L-shaped molecule can be divided into a flexible repeat I (LNS1-EGF-A-LNS2), a rigid horseshoe-shaped repeat II (LNS3-EGF-B-LNS4) with structural similarity to so-called reelin repeats, and an extended repeat III (LNS5-EGF-B-LNS6) with controlled flexibility.","type":"Abstract"},{"text":"Neurexin repeat I is flexible","type":"Introduction"},{"text":"No electron density is observed for L1 and EGF-A, though present in the crystal, suggesting that these N-terminal modules are disordered and can adopt multiple conformations. Thus, the crystal structure of n1α reveals 7 out of 9 modules (1003 residues per molecule) organized in an L-shaped assembly.","type":"Results"},{"text":"N1α appears increasingly flexible towards its N-terminus","type":"Results"},{"text":"The L1-EGF-A-L2 repeat appears flexible, as L1 and EGF-A are not visible in the crystal structure.","type":"Results"},{"text":"Continuous electron density is visible for L2, L3, EGF-B, L4, L5, EGF-C and L6 (residues Glu281-Val1337), including interconnecting residues.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"The structure of neurexin 1α reveals features promoting a role as synaptic organizer. <i> Chen F, Venugopal V, Murray B, Rudenko G. </i> Structure, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3QCW"},{"db":"PDB","id":"3R05"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":1530,"ncbi_taxon_id":9913,"date":"2020-01-02T10:22:40.059Z","organism":"Bos taurus","features":{"gene3D":[],"pfam":[{"id":"PF00008","name":"EGF-like domain","start":703,"end":730},{"id":"PF01034","name":"Syndecan domain","start":1455,"end":1494},{"id":"PF02210","name":"Laminin G domain","start":58,"end":191},{"id":"PF02210","name":"Laminin G domain","start":328,"end":468},{"id":"PF02210","name":"Laminin G domain","start":531,"end":675},{"id":"PF02210","name":"Laminin G domain","start":769,"end":899},{"id":"PF02210","name":"Laminin G domain","start":956,"end":1084},{"id":"PF02210","name":"Laminin G domain","start":1179,"end":1327}]},"disprot_id":"DP02503","regions_counter":1,"dataset":[],"UniParc":"UPI0000130A9B","uniref100":"UniRef100_Q28146","uniref90":"UniRef90_Q9CS84","uniref50":"UniRef50_Q9CS84","genes":[{"name":{"value":"NRXN1"}}],"alphafold_very_low_content":0.1627450980392157,"disorder_content":0.16339869281045752,"disprot_consensus":{"full":[{"start":31,"end":280,"type":"D"}],"Structural state":[{"start":31,"end":280,"type":"D"}]}},{"acc":"P35828","name":"S-layer protein","sequence":"MAYTTAQLVTAYTNANLGKAPDAATTLTLDAYATQTQTGGLSDAAALTNTLKLVNSTTAVAIQTYQFFTGVAPSAAGLDFLVDSTTNTNDLNDAYYSKFAQENRFINFSINLATGAGAGATAFAAAYTGVSYAQTVATAYDKIIGNAVATAAGVDVAAAVAFLSRQANIDYLTAFVRANTPFTAAADIDLAVKAALIGTILNAATVSGIGGYATATAAMINDLSDGALSTDNAAGVNLFTAYPSSGVSGSTLSLTTGTDTLTGTANNDTFVAGEVAGAATLTVGDTLSGGAGTDVLNWVQAAAVTALPTGVTISGIETMNVTSGAAITLNTSSGVTGLTALNTNTSGAAQTVTAGAGQNLTATTAAQAANNVAVDGGANVTVASTGVTSGTTTVGANSAASGTVSVSVANSSTTTTGAIAVTGGTAVTVAQTAGNAVNTTLTQADVTVTGNSSTTAVTVTQTAAATAGATVAGRVNGAVTITDSAAASATTAGKIATVTLGSFGAATIDSSALTTVNLSGTGTSLGIGRGALTATPTANTLTLNVNGLTTTGAITDSEAAADDGFTTINIAGSTASSTIASLVAADATTLNISGDARVTITSHTAAALTGITVTNSVGATLGAELATGLVFTGGAGADSILLGATTKAIVMGAGDDTVTVSSATLGAGGSVNGGDGTDVLVANVNGSSFSADPAFGGFETLRVAGAAAQGSHNANGFTALQLGATAGATTFTNVAVNVGLTVLAAPTGTTTVTLANATGTSDVFNLTLSSSAALAAGTVALAGVETVNIAATDTNTTAHVDTLTLQATSAKSIVVTGNAGLNLTNTGNTAVTSFDASAVTGTGSAVTFVSANTTVGEVVTIRGGAGADSLTGSATANDTIIGGAGADTLVYTGGTDTFTGGTGADIFDINAIGTSTAFVTITDAAVGDKLDLVGISTNGAIADGAFGAAVTLGAAATLAQYLDAAAAGDGSGTSVAKWFQFGGDTYVVVDSSAGATFVSGADAVIKLTGLVTLTTSAFATEVLTLA","taxonomy":["Bacteria","Proteobacteria","Alphaproteobacteria","Caulobacterales","Caulobacteraceae","Caulobacter"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":248,"region_id":"DP02504r001","reference_id":"28418382","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structure of the hexagonal surface layer on Caulobacter crescentus cells. <i> Bharat TAM, Kureisaite-Ciziene D, Hardy GG, Yu EW, Devant JM, Hagen WJH, Brun YV, Briggs JAG, Löwe J. </i> Nat Microbiol, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"EMDB","id":"3604"}],"term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":248,"region_id":"DP02504r002","reference_id":"28418382","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The N-terminal region of RsaA is a putative LPS binding region (see Figure S2), residues 249-1026 are resolved in the X-ray structure","type":"Figure"},{"text":"RsaA amino acid residues 249-1026 were resolved in the resulting electron density map","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structure of the hexagonal surface layer on Caulobacter crescentus cells. <i> Bharat TAM, Kureisaite-Ciziene D, Hardy GG, Yu EW, Devant JM, Hagen WJH, Brun YV, Briggs JAG, Löwe J. </i> Nat Microbiol, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5N8P"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":256,"region_id":"DP02504r003","reference_id":"28418382","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"At least amino acid residues 256-1026 were still present in the crystallised protein as determined by mass spectrometry after protease cleavage into peptides, a method that does not reveal the exact N- and C-termini of the analysed polypeptide","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cleavage assay evidence used in manual assertion","version":3,"reference_html":"Structure of the hexagonal surface layer on Caulobacter crescentus cells. <i> Bharat TAM, Kureisaite-Ciziene D, Hardy GG, Yu EW, Devant JM, Hagen WJH, Brun YV, Briggs JAG, Löwe J. </i> Nat Microbiol, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","cross_refs":[{"db":"PDB","id":"5N8P"}],"term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2020_06","length":1026,"ncbi_taxon_id":190650,"date":"2020-01-02T10:31:14.816Z","organism":"Caulobacter vibrioides (strain ATCC 19089 / CB15)","features":{"gene3D":[{"start":796,"end":980,"id":"G3DSA:2.150.10.10","name":"Serralysin-like metalloprotease, C-terminal"}],"pfam":[{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":256,"end":273},{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":285,"end":296},{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":860,"end":889},{"id":"PF19198","name":"RsaA N-terminal domain","start":57,"end":245}]},"disprot_id":"DP02504","regions_counter":3,"dataset":[],"UniParc":"UPI0000135A06","uniref100":"UniRef100_P35828","uniref90":"UniRef90_P35828","uniref50":"UniRef50_P35828","genes":[{"name":{"value":"rsaA"},"olnNames":[{"value":"CC_1007"}]}],"alphafold_very_low_content":0.001949317738791423,"disorder_content":0.24951267056530213,"disprot_consensus":{"full":[{"start":1,"end":256,"type":"D"}],"Structural state":[{"start":1,"end":256,"type":"D"}]}},{"acc":"O53168","name":"Peptidoglycan endopeptidase RipA","sequence":"MRRNRRGSPARPAARFVRPAIPSALSVALLVCTPGLATADPQTDTIAALIADVAKANQRLQDLSDEVQAEQESVNKAMVDVETARDNAAAAEDDLEVSQRAVKDANAAIAAAQHRFDTFAAATYMNGPSVSYLSASSPDEIIATVTAAKTLSASSQAVMANLQRARTERVNTESAARLAKQKADKAAADAKASQDAAVAALTETRRKFDEQREEVQRLAAERDAAQARLQAARLVAWSSEGGQGAPPFRMWDPGSGPAGGRAWDGLWDPTLPMIPSANIPGDPIAVVNQVLGISATSAQVTANMGRKFLEQLGILQPTDTGITNAPAGSAQGRIPRVYGRQASEYVIRRGMSQIGVPYSWGGGNAAGPSKGIDSGAGTVGFDCSGLVLYSFAGVGIKLPHYSGSQYNLGRKIPSSQMRRGDVIFYGPNGSQHVTIYLGNGQMLEAPDVGLKVRVAPVRTAGMTPYVVRYIEY","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":262,"region_id":"DP02505r001","reference_id":"25195744","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In a previous study, we determined the crystal structure of a self-inactivated form of RipA in which the catalytic site cleft of the enzyme is physically locked by a pro-domain, and proposed that the activation of the RipA zymogen occurs through proteolytic cleavage (Ruggiero, Marasco et al., 2010). Recent work has confirmed that RipA is proteolytically activated in vivo and that overproduction of activated RipA produces severe growth defects in Mtb (Chao et al., 2013).","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Mutational and structural study of RipA, a key enzyme in Mycobacterium tuberculosis cell division: evidence for the L-to-D inversion of configuration of the catalytic cysteine. <i> Squeglia F, Ruggiero A, Romano M, Vitagliano L, Berisio R. </i> Acta Crystallogr D Biol Crystallogr, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4Q4G"},{"db":"PDB","id":"4Q4T"},{"db":"PDB","id":"4Q4N"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":472,"ncbi_taxon_id":83332,"date":"2020-01-02T15:57:00.243Z","organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","features":{"gene3D":[],"pfam":[{"id":"PF00877","name":"NlpC/P60 family","start":355,"end":469}]},"disprot_id":"DP02505","regions_counter":1,"dataset":[],"UniParc":"UPI000004B723","uniref100":"UniRef100_O53168","uniref90":"UniRef90_O53168","uniref50":"UniRef50_O53168","genes":[{"name":{"value":"ripA"},"olnNames":[{"value":"Rv1477"}]}],"alphafold_very_low_content":0.125,"disorder_content":0.5550847457627118,"disprot_consensus":{"full":[{"start":1,"end":262,"type":"D"}],"Structural state":[{"start":1,"end":262,"type":"D"}]}},{"acc":"Q8A6W3","name":"SusC homolog","sequence":"MPGIMKNKKLLCSVCFLFAFMSALWGQNITVKGNVTSKTDGQPIIGASVVETTATTNGTITDFDGNFTLSVPVNSTLKITYIGYKPVTVKAAAIVNVLLEEDTQMVDEVVVTGYTTQRKADLTGAVSVVKVDEIQKQGENNPVKALQGRVPGMNITADGNPSGSATVRIRGIGTLNNNDPLYIIDGVPTKAGMHELNGNDIESIQVLKDAASASIYGSRAANGVIIITTKQGKKGQIKINFDASVSASMYQSKMNVLNTEQYGRAMWQAYVNDGENPNGNALGYAYNWGYNADGNPVLYGMTLSKYLDSKNTMPVADTDWFDEITRTGVIQQYNLSVSNGSEKGSSFFSLGYYKNLGVIKDTDFDRFSARMNSDYKLIDDILTIGQHFTLNRTSEVQAPGGIIETALDIPSAIPVYASDGSWGGPVGGWPDRRNPRAVLEYNKDNRYTYWRMFGDAYVNLTPFKGFNLRSTFGLDYANKQARYFTYPYQEGTQTNNGKSAVEAKQEHWTKWMWNAIATYQLEVGKHRGDVMIGMELNREDDSHFSGYKEDFSILTPDYMWPDAGSGTAQAYGAGEGYSLVSFFGKMNYSYADRYLLSLTLRRDGSSRFGKNHRYATFPSVSLGWRITQENFMKELTWLDDLKLRASWGQTGNQEISNLARYTIYAPNYGTTDSFGGQSYGTAYDITGSNGGGVLPSGFKRNQIGNDNIKWETTTQTNVGIDFSLFKQSLYGSLEYYYKKATDILTEMAGVGVLGEGGSRWINSGAMKNQGFEFNLGYRNKTAFGLTYDLNGNISTYRNEILELPETVAANGKFGGNGVKSVVGHTYGAQVGYIADGIFKSQDEVDNHATQEGAAVGRIRYRDIDHNGVIDERDQNWIYDPTPSFSYGLNIYLEYKNFDLTMFWQGVQGVDIISDVKKKSDFWSASNVGFLNKGTRLLNAWSPTNPNSDIPALTRSDTNNEQRVSTYFVENGSFLKLRNIQLGYTVPAVISKKMRMDRLRFYCSAQNLLTIKSKNFTGEDPENPNFSYPIPVNITFGLNIGF","taxonomy":["Bacteria","Bacteroidetes","Bacteroidia","Bacteroidales","Bacteroidaceae","Bacteroides"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":235,"region_id":"DP02506r001","reference_id":"28077872","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Region 1-235 is not visible in the crystal structure of SusC homolog","type":"Curator statement"},{"text":"A dataset to 3.1 Å resolution collected on this crystal at DLS beamline I04 generated a definite MR solution with Phaser (RFZ=6.8 TFZ=14.4 PAK=0 LLG=173 TFZ==14.7 RFZ=7.0 TFZ=7.6 PAK=9 LLG=627 TFZ==10.4 LLG=807 TFZ==10.0; space group P21212), using the BT1762 structure and a Sculptor-generated model of BT2264 (21% sequence identity) as search models. In this crystal, there is only one SusC protomer within the asymmetric unit, with the SusC homodimer generated by crystallographic symmetry.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structural basis for nutrient acquisition by dominant members of the human gut microbiota. <i> Glenwright AJ, Pothula KR, Bhamidimarri SP, Chorev DS, Baslé A, Firbank SJ, Zheng H, Robinson CV, Winterhalter M, Kleinekathöfer U, Bolam DN, van den Berg B. </i> Nature, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5T3R"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":1041,"ncbi_taxon_id":226186,"date":"2020-01-07T11:53:33.797Z","organism":"Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)","features":{"gene3D":[{"start":357,"end":1041,"id":"G3DSA:2.40.170.20","name":"TonB-dependent receptor, beta-barrel domain"},{"start":102,"end":229,"id":"G3DSA:2.170.130.10","name":"TonB-dependent receptor, plug domain"}],"pfam":[{"id":"PF00593","name":"TonB dependent receptor-like, beta-barrel","start":425,"end":894},{"id":"PF07715","name":"TonB-dependent Receptor Plug Domain","start":119,"end":224},{"id":"PF13715","name":"CarboxypepD_reg-like domain","start":31,"end":111}]},"disprot_id":"DP02506","regions_counter":1,"dataset":[],"UniParc":"UPI000005B0D9","uniref100":"UniRef100_Q8A6W3","uniref90":"UniRef90_Q8A6W3","uniref50":"UniRef50_Q8A6W3","genes":[{"olnNames":[{"value":"BT_1763","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAO76870.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAO76870.1"}}]}]}],"alphafold_very_low_content":0.01921229586935639,"disorder_content":0.22574447646493756,"disprot_consensus":{"full":[{"start":1,"end":235,"type":"D"}],"Structural state":[{"start":1,"end":235,"type":"D"}]}},{"acc":"Q84852","name":"Spike glycoprotein","sequence":"MKKLFVVLVVMPLIYGDKFPTSVVSNCTDQCASYVANVFTTQPGGFIPSDFSFNNWFLLTNSSTLVSGKLVTKQPLLVNCLWPVPSFEEAASTFCFEGADFDQCNGAVLNNTVDVIRFNLNFTTNVQSGKGATVFSLNTTGGVTLEISCYNDTVSDSSFSSYGEIPFGVTNGPRYCYVLYNGTALKYLGTLPPSVKEIAISKWGHFYINGYNFFSTFPIDCISFNLTTGDSDVFWTIAYTSYTEALVQVENTAITNVTYCNSYVNNIKCSQLTANLNNGFYPVSSSEVGSVNKSVVLLPSFLTHTIVNITIGLGMKRSGYGQPIASTLSNITLPMQDNNTDVYCVRSDQFSVYVHSTCKSALWDNVFKRNCTDVLDATAVIKTGTCPFSFDKLNNYLTFNKFCLSLSPVGANCKFDVAARTRTNEQVVRSLYVIYEEGDSIVGVPSDNSGLHDLSVLHLDSCTDYNIYGRTGVGIIRQTNRTLLSGLYYTSLSGDLLGFKNVSDGVIYSVTPCDVSAQAAVIDGTIVGAITSINSELLGLTHWTITPNFYYYSIYNYTNDKTRGTPIDSNDVGCEPVITYSNIGVCKNGALVFINVTHSDGDVQPISTGNVTIPTNFTISVQVEYIQVYTTPVSIDCSRYVCNGNPRCNKLLTQYVSACQTIEQALAMGARLENMEVDSMLFVSENALKLASVEAFNSSETLDPIYTQWPNIGGFWLEGLKYILPSDNSKRKYRSAIEDLLFSKVVTSGLGTVDEDYKRCTGGYDIADLVCAQYYNGIMVLPGVANADKMTMYTASLAGGITLGAFGGGAVSIPFAVAVQARLNYVALQTDVLNKNQQILASAFNQAIGNITQSFGKVNDAIHQTSRGLTTVAKALAKVQDVVNTQGQALRHLTVQLQNNFQAISSSISDIYNRLDELSADAQVDRLITGRLTALNAFVSQTLTRQAEVRASRQLAKDKVNECVRSQSQRFGFCGNGTHLFSLANAAPNGMIFFHTVLLPTAYETVTAWSGICALDGDRTFGLVVKDVQLTLFRNLDDKFYLTPRTMYQPRVATSSDFVQIEGCDVLFVNTTVSDLPSIIPDYIDINQTVQDILENFRPNWTVPELTLDVFNATYLNLTGEIDDLEFRSEKLHNTTVELAILIDNINNTLVNLEWLNRIETYVKWPWYVWLLIGLVVIFCIPLLLFCCCSTGCCGCIGCLGSCCHSIFSRRQFENYEPIEKVHVH","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Nidovirales","Cornidovirineae","Coronaviridae","Orthocoronavirinae","Alphacoronavirus","Tegacovirus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":299,"region_id":"DP02507r001","reference_id":"22876187","start":17,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The 282 residues N-terminal to the PRCV RBD in the S3H protein were largely disordered or degraded during crystallization, and are absent in the structure.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structural bases of coronavirus attachment to host aminopeptidase N and its inhibition by neutralizing antibodies. <i> Reguera J, Santiago C, Mudgal G, Ordoño D, Enjuanes L, Casasnovas JM. </i> PLoS Pathog, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4F5C"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":1225,"ncbi_taxon_id":11146,"date":"2020-01-07T12:16:14.621Z","organism":"Porcine respiratory coronavirus","features":{"gene3D":[],"pfam":[{"id":"PF01600","name":"Coronavirus spike glycoprotein S1","start":27,"end":445},{"id":"PF01601","name":"Coronavirus spike glycoprotein S2","start":609,"end":1182},{"id":"PF19209","name":"Coronavirus spike glycoprotein S1, C-terminal","start":460,"end":516},{"id":"PF19214","name":"Coronavirus spike glycoprotein S2, intravirion","start":1186,"end":1225}]},"disprot_id":"DP02507","regions_counter":1,"dataset":["Viral proteins"],"UniParc":"UPI00000F8E4F","uniref100":"UniRef100_Q84852","uniref90":"UniRef90_P07946","uniref50":"UniRef50_P07946","genes":[{"name":{"value":"S","evidences":[{"code":"ECO:0000256","source":{"name":"HAMAP-Rule","id":"MF_04200","url":"https://hamap.expasy.org/unirule/MF_04200"}},{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAA46905.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAA46905.1"}}]}}],"disorder_content":0.2310204081632653,"disprot_consensus":{"full":[{"start":17,"end":299,"type":"D"}],"Structural state":[{"start":17,"end":299,"type":"D"}]}},{"acc":"P12537","name":"Pre-hexon-linking protein IIIa","sequence":"MMQDATDPAVRAALQSQPSGLNSTDDWRQVMDRIMSLTARNPDAFRQQPQANRLSAILEAVVPARANPTHEKVLAIVNALAENRAIRPDEAGLVYDALLQRVARYNSGNVQTNLDRLVGDVREAVAQRERAQQQGNLGSMVALNAFLSTQPANVPRGQEDYTNFVSALRLMVTETPQSEVYQSGPDYFFQTSRQGLQTVNLSQAFKNLQGLWGVRAPTGDRATVSSLLTPNSRLLLLLIAPFTDSGSVSRDTYLGHLLTLYREAIGQAHVDEHTFQEITSVSRALGQEDTGSLEATLNYLLTNRRQKIPSLHSLNSEEERILRYVQQSVSLNLMRDGVTPSVALDMTARNMEPGMYASNRPFINRLMDYLHRAAAVNPEYFTNAILNPHWLPPPGFYTGGFEVPEGNDGFLWDDIDDSVFSPQPQTLLELQQREQAEAALRKESFRRPSSLSDLGAAAPRSDASSPFPSLIGSLTSTRTTRPRLLGEEEYLNNSLLQPQREKNLPPAFPNNGIESLVDKMSRWKTYAQEHRDVPGPRPPTRRQRHDRQRGLVWEDDDSADDSSVLDLGGSGNPFAHLRPRLGRMF","taxonomy":["Viruses","Varidnaviria","Bamfordvirae","Preplasmiviricota","Tectiliviricetes","Rowavirales","Adenoviridae","Mastadenovirus"],"creator":"jbergier","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":585,"region_id":"DP02508r001","reference_id":"30121295","start":304,"term_id":"IDPO:0000002","curator_orcid":"0000-0003-2206-9968","statement":[{"text":"The ordered region of IIIa (aa 1–300) is composed of mostly α-helices and organized as two domains: NT domain (NTD; aa 1–134) and middle domain (MDLD; aa 135–300) (Fig. 3c). The CT domain (CTD; aa 400–585), which also contains a few (predicted) helices, is disordered.","type":"Results"},{"text":"From Table 2, 1–303 corresponds to the ordered region of IIIa and 304–585 corresponds to the disordered region of IIIa. Also the PDB show this boundaries as disordered (304-585).","type":"Curator statement"}],"curator_id":"jbergier","released":"2022_03","term_ontology":"IDPO","curator_name":"Julian Bergier","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"Revised Crystal Structure of Human Adenovirus Reveals the Limits on Protein IX Quasi-Equivalence and on Analyzing Large Macromolecular Complexes. <i> Kundhavai Natchiar S, Venkataraman S, Mullen TM, Nemerow GR, Reddy VS. </i> J Mol Biol, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6CGV"},{"db":"EMDB","id":"7034"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-11T09:31:38.606Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":585,"ncbi_taxon_id":28285,"date":"2020-01-07T12:29:15.540Z","organism":"Human adenovirus C serotype 5","features":{"gene3D":[{"start":1,"end":134,"id":"G3DSA:1.20.120.1500","name":"G3DSA:1.20.120.1500"}],"pfam":[{"id":"PF02455","name":"Hexon-associated protein (IIIa)","start":73,"end":582}]},"disprot_id":"DP02508","regions_counter":1,"dataset":["Viral proteins"],"UniParc":"UPI0000170D93","uniref100":"UniRef100_P12537","uniref90":"UniRef90_P12537","uniref50":"UniRef50_P12537","genes":[{"orfNames":[{"value":"L1"}]}],"disorder_content":0.48205128205128206,"disprot_consensus":{"full":[{"start":304,"end":585,"type":"D"}],"Structural state":[{"start":304,"end":585,"type":"D"}]}},{"acc":"P0DOC6","name":"CRISPR-associated endoribonuclease Cas13a","sequence":"MGNLFGHKRWYEVRDKKDFKIKRKVKVKRNYDGNKYILNINENNNKEKIDNNKFIRKYINYKKNDNILKEFTRKFHAGNILFKLKGKEGIIRIENNDDFLETEEVVLYIEAYGKSEKLKALGITKKKIIDEAIRQGITKDDKKIEIKRQENEEEIEIDIRDEYTNKTLNDCSIILRIIENDELETKKSIYEIFKNINMSLYKIIEKIIENETEKVFENRYYEEHLREKLLKDDKIDVILTNFMEIREKIKSNLEILGFVKFYLNVGGDKKKSKNKKMLVEKILNINVDLTVEDIADFVIKELEFWNITKRIEKVKKVNNEFLEKRRNRTYIKSYVLLDKHEKFKIERENKKDKIVKFFVENIKNNSIKEKIEKILAEFKIDELIKKLEKELKKGNCDTEIFGIFKKHYKVNFDSKKFSKKSDEEKELYKIIYRYLKGRIEKILVNEQKVRLKKMEKIEIEKILNESILSEKILKRVKQYTLEHIMYLGKLRHNDIDMTTVNTDDFSRLHAKEELDLELITFFASTNMELNKIFSRENINNDENIDFFGGDREKNYVLDKKILNSKIKIIRDLDFIDNKNNITNNFIRKFTKIGTNERNRILHAISKERDLQGTQDDYNKVINIIQNLKISDEEVSKALNLDVVFKDKKNIITKINDIKISEENNNDIKYLPSFSKVLPEILNLYRNNPKNEPFDTIETEKIVLNALIYVNKELYKKLILEDDLEENESKNIFLQELKKTLGNIDEIDENIIENYYKNAQISASKGNNKAIKKYQKKVIECYIGYLRKNYEELFDFSDFKMNIQEIKKQIKDINDNKTYERITVKTSDKTIVINDDFEYIISIFALLNSNAVINKIRNRFFATSVWLNTSEYQNIIDILDEIMQLNTLRNECITENWNLNLEEFIQKMKEIEKDFDDFKIQTKKEIFNNYYEDIKNNILTEFKDDINGCDVLEKKLEKIVIFDDETKFEIDKKSNILQDEQRKLSNINKKDLKKKVDQYIKDKDQEIKSKILCRIIFNSDFLKKYKKEIDNLIEDMESENENKFQEIYYPKERKNELYIYKKNLFLNIGNPNFDKIYGLISNDIKMADAKFLFNIDGKNIRKNKISEIDAILKNLNDKLNGYSKEYKEKYIKKLKENDDFFAKNIQNKNYKSFEKDYNRVSEYKKIRDLVEFNYLNKIESYLIDINWKLAIQMARFERDMHYIVNGLRELGIIKLSGYNTGISRAYPKRNGSDGFYTTTAYYKFFDEESYKKFEKICYGFGIDLSENSEINKPENESIRNYISHFYIVRNPFADYSIAEQIDRVSNLLSYSTRYNNSTYASVFEVFKKDVNLDYDELKKKFKLIGNNDILERLMKPKKVSVLELESYNSDYIKNLIIELLTKIENTNDTL","taxonomy":["Bacteria","Fusobacteria","Fusobacteriales","Leptotrichiaceae","Leptotrichia"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":174,"region_id":"DP02509r001","start":103,"term_id":"IDPO:0000002","statement":[{"text":"In the LshC2c2-crRNA binary structure, residues 103–174 within the NTD domain and residues 914–1005 within the Linker of LshC2c2 are disordered","type":"Results"},{"text":"The larger subdomain of NTD contains an ordered segment comprising seven α helices, as well as a disordered segment between residues 103–174.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28086085","version":2,"reference_html":"Two Distant Catalytic Sites Are Responsible for C2c2 RNase Activities. <i> Liu L, Li X, Wang J, Wang M, Chen P, Yin M, Li J, Sheng G, Wang Y. </i> Cell, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5WTJ"},{"db":"PDB","id":"5WTK"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1005,"region_id":"DP02509r002","start":914,"term_id":"IDPO:0000002","statement":[{"text":"In the LshC2c2-crRNA binary structure, residues 103–174 within the NTD domain and residues 914–1005 within the Linker of LshC2c2 are disordered","type":"Results"},{"text":"residues 914 to 1005 are disordered","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28086085","version":2,"reference_html":"Two Distant Catalytic Sites Are Responsible for C2c2 RNase Activities. <i> Liu L, Li X, Wang J, Wang M, Chen P, Yin M, Li J, Sheng G, Wang Y. </i> Cell, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5WTJ"},{"db":"PDB","id":"5WTK"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":1005,"region_id":"DP02509r003","start":914,"term_id":"IDPO:0000033","statement":[{"text":"In the LshC2c2-crRNA binary structure, residues 103–174 within the NTD domain and residues 914–1005 within the Linker of LshC2c2 are disordered","type":"Results"},{"text":"residues 914 to 1005 are disordered","type":"Results"},{"text":"the Linker connecting the HEPN1 and HEPN2 domains is partially disordered, in contrast to the ordered structure in the crRNA-free state (discussed further below). Those residues that are ordered in the crRNA-bound structure form eight α helices, while residues 914 to 1005 are disordered.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28086085","version":3,"reference_html":"Two Distant Catalytic Sites Are Responsible for C2c2 RNase Activities. <i> Liu L, Li X, Wang J, Wang M, Chen P, Yin M, Li J, Sheng G, Wang Y. </i> Cell, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5WTJ"},{"db":"PDB","id":"5WTK"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","length":1389,"ncbi_taxon_id":1122172,"date":"2020-01-07T14:03:53.543Z","organism":"Leptotrichia shahii (strain DSM 19757 / CCUG 47503 / CIP 107916 / JCM 16776 / LB37)","features":{"pfam":[{"id":"PF28192","name":"CRISPR-associated endoribonuclease Cas13a","start":9,"end":1170}]},"disprot_id":"DP02509","regions_counter":3,"dataset":[],"UniParc":"UPI00035DCCF4","uniref100":"UniRef100_P0DOC6","uniref90":"UniRef90_P0DOC6","uniref50":"UniRef50_P0DOC6","genes":[{"name":{"value":"cas13a","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"28111461","url":"http://www.ncbi.nlm.nih.gov/pubmed/28111461","alternativeUrl":"https://europepmc.org/abstract/MED/28111461"}}]},"synonyms":[{"value":"c2c2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"26593719","url":"http://www.ncbi.nlm.nih.gov/pubmed/26593719","alternativeUrl":"https://europepmc.org/abstract/MED/26593719"}}]}]}],"alphafold_very_low_content":0.183585313174946,"disorder_content":0.11807055435565154,"disprot_consensus":{"full":[{"start":103,"end":174,"type":"D"},{"start":914,"end":1005,"type":"D"}],"Structural state":[{"start":103,"end":174,"type":"D"},{"start":914,"end":1005,"type":"D"}],"Disorder function":[{"start":914,"end":1005,"type":"F"}]}},{"acc":"P09327","name":"Villin-1","sequence":"MTKLSAQVKGSLNITTPGLQIWRIEAMQMVPVPSSTFGSFFDGDCYIILAIHKTASSLSYDIHYWIGQDSSLDEQGAAAIYTTQMDDFLKGRAVQHREVQGNESEAFRGYFKQGLVIRKGGVASGMKHVETNSYDVQRLLHVKGKRNVVAGEVEMSWKSFNRGDVFLLDLGKLIIQWNGPESTRMERLRGMTLAKEIRDQERGGRTYVGVVDGENELASPKLMEVMNHVLGKRRELKAAVPDTVVEPALKAALKLYHVSDSEGNLVVREVATRPLTQDLLSHEDCYILDQGGLKIYVWKGKKANEQEKKGAMSHALNFIKAKQYPPSTQVEVQNDGAESAVFQQLFQKWTASNRTSGLGKTHTVGSVAKVEQVKFDATSMHVKPQVAAQQKMVDDGSGEVQVWRIENLELVPVDSKWLGHFYGGDCYLLLYTYLIGEKQHYLLYVWQGSQASQDEITASAYQAVILDQKYNGEPVQIRVPMGKEPPHLMSIFKGRMVVYQGGTSRTNNLETGPSTRLFQVQGTGANNTKAFEVPARANFLNSNDVFVLKTQSCCYLWCGKGCSGDEREMAKMVADTISRTEKQVVVEGQEPANFWMALGGKAPYANTKRLQEENLVITPRLFECSNKTGRFLATEIPDFNQDDLEEDDVFLLDVWDQVFFWIGKHANEEEKKAAATTAQEYLKTHPSGRDPETPIIVVKQGHEPPTFTGWFLAWDPFKWSNTKSYEDLKAELGNSRDWSQITAEVTSPKVDVFNANSNLSSGPLPIFPLEQLVNKPVEELPEGVDPSRKEEHLSIEDFTQAFGMTPAAFSALPRWKQQNLKKEKGLF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":613,"region_id":"DP02510r001","reference_id":"19491107","start":360,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"An unambiguous solution showed that the diffraction originated solely from V6, with the V4 and V5 domains and actin not evident.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Helix straightening as an activation mechanism in the gelsolin superfamily of actin regulatory proteins. <i> Wang H, Chumnarnsilpa S, Loonchanta A, Li Q, Kuan YM, Robine S, Larsson M, Mihalek I, Burtnick LD, Robinson RC. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3FG7"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-05T17:34:00.380Z"}}],"released":"2020_06","length":827,"ncbi_taxon_id":9606,"date":"2020-01-07T15:21:52.355Z","organism":"Homo sapiens","features":{"gene3D":[{"start":614,"end":734,"id":"G3DSA:3.40.20.10","name":"Severin"},{"start":614,"end":734,"id":"G3DSA:3.40.20.10","name":"Severin"},{"start":614,"end":734,"id":"G3DSA:3.40.20.10","name":"Severin"},{"start":614,"end":734,"id":"G3DSA:3.40.20.10","name":"Severin"},{"start":614,"end":734,"id":"G3DSA:3.40.20.10","name":"Severin"},{"start":614,"end":734,"id":"G3DSA:3.40.20.10","name":"Severin"},{"start":752,"end":827,"id":"G3DSA:1.10.950.10","name":"Villin headpiece domain"}],"pfam":[{"id":"PF00626","name":"Gelsolin repeat","start":28,"end":108},{"id":"PF00626","name":"Gelsolin repeat","start":147,"end":219},{"id":"PF00626","name":"Gelsolin repeat","start":269,"end":342},{"id":"PF00626","name":"Gelsolin repeat","start":409,"end":489},{"id":"PF00626","name":"Gelsolin repeat","start":532,"end":595},{"id":"PF00626","name":"Gelsolin repeat","start":634,"end":707},{"id":"PF02209","name":"Villin headpiece domain","start":792,"end":827}]},"disprot_id":"DP02510","regions_counter":1,"dataset":["NDDs-related proteins"],"UniParc":"UPI0000138814","uniref100":"UniRef100_P09327","uniref90":"UniRef90_P09327","uniref50":"UniRef50_P09327","genes":[{"name":{"value":"VIL1"},"synonyms":[{"value":"VIL"}]}],"alphafold_very_low_content":0.07980652962515115,"disorder_content":0.30713422007255137,"disprot_consensus":{"full":[{"start":360,"end":613,"type":"D"}],"Structural state":[{"start":360,"end":613,"type":"D"}]}},{"acc":"P02640","name":"Villin-1","sequence":"MVELSKKVTGKLDKTTPGIQIWRIENMEMVPVPTKSYGNFYEGDCYVLLSTRKTGSGFSYNIHYWLGKNSSQDEQGAAAIYTTQMDEYLGSVAVQHREVQGHESETFRAYFKQGLIYKQGGVASGMKHVETNTYNVQRLLHVKGKKNVVAAEVEMSWKSFNLGDVFLLDLGQLIIQWNGPESNRAERLRAMTLAKDIRDRERAGRAKVGVVEGENEAASPELMQALTHVLGEKKNIKAATPDEQVHQALNSALKLYHVSDASGNLVIQEVAIRPLTQDMLQHEDCYILDQAGLKIFVWKGKNANKEEKQQAMSRALGFIKAKNYLASTSVETENDGSESAVFRQLFQKWTVPNQTSGLGKTHTVGKVAKVEQVKFDATTMHVKPEVAAQQKMVDDGSGEAEVWRVENQELVPVEKRWLGHFYGGDCYLVLYTYYVGPKVNRIIYIWQGRHASTDELAASAYQAVFLDQKYNNEPVQVRVTMGKEPAHLMAIFKGKMVVYENGSSRAGGTEPASSTRLFHVHGTNEYNTKAFEVPVRAASLNSNDVFVLKTPSSCYLWYGKGCSGDEREMGKMVADIISKTEKPVVAEGQEPPEFWVALGGKTSYANSKRLQEENPSVPPRLFECSNKTGRFLATEIVDFTQDDLDENDVYLLDTWDQIFFWIGKGANESEKEAAAETAQEYLRSHPGSRDLDTPIIVVKQGFEPPTFTGWFMAWDPLCWSDRKSYDELKAELGDNASIGQLVSGLTSKNEVFTATTTLVPTKLETFPLDVLVNTAAEDLPRGVDPSRKENHLSDEDFKAVFGMTRSAFANLPLWKQQNLKKEKGLF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Phasianinae","Gallus"],"creator":"fquaglia","regions":[{"region_id":"DP02511r001","ec_ontology":"ECO","end":763,"term_id":"IDPO:0000002","start":723,"version":2,"statement":[{"text":"The isolated sixth gelsolin repeat and headpiece domain of villin bundle F-actin in the presence of calcium and are linked by a 40-residue unstructured sequence","type":"Title"},{"text":"D6-HP consists of two structured domains, D6 and HP, separated by an unfolded linker sequence","type":"Results"},{"text":"The linker sequence, positions 105-145, is characterized by the 1HN chemical shift values narrowly clustered between 8.0-8.5 ppm consistent with a random coil, unfolded polypeptide.","type":"Results"},{"text":"The 15N backbone relaxation rates R1 and R2 as well as the {1H-15N}-NOE (Figure 4 A,B,C) indicate three distinct structural entities within D6-HP, namely two structured regions, positions 1-105 and 145-206, and a disordered sequence in between.","type":"Results"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17547371","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"15097"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"fquaglia","reference_html":"The isolated sixth gelsolin repeat and headpiece domain of villin bundle F-actin in the presence of calcium and are linked by a 40-residue unstructured sequence. <i> Smirnov SL, Isern NG, Jiang ZG, Hoyt DW, McKnight CJ. </i> Biochemistry, 2007","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02511r002","ec_ontology":"ECO","end":763,"term_id":"IDPO:0000033","start":723,"version":3,"statement":[{"text":"The isolated sixth gelsolin repeat and headpiece domain of villin bundle F-actin in the presence of calcium and are linked by a 40-residue unstructured sequence","type":"Title"},{"text":"D6-HP consists of two structured domains, D6 and HP, separated by an unfolded linker sequence","type":"Results"},{"text":"The linker sequence, positions 105-145, is characterized by the 1HN chemical shift values narrowly clustered between 8.0-8.5 ppm consistent with a random coil, unfolded polypeptide.","type":"Results"},{"text":"The 15N backbone relaxation rates R1 and R2 as well as the {1H-15N}-NOE (Figure 4 A,B,C) indicate three distinct structural entities within D6-HP, namely two structured regions, positions 1-105 and 145-206, and a disordered sequence in between.","type":"Results"}],"term_name":"flexible linker","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17547371","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"15097"}],"term_namespace":"Disorder function","ec_id":"ECO:0006165","curator_id":"fquaglia","reference_html":"The isolated sixth gelsolin repeat and headpiece domain of villin bundle F-actin in the presence of calcium and are linked by a 40-residue unstructured sequence. <i> Smirnov SL, Isern NG, Jiang ZG, Hoyt DW, McKnight CJ. </i> Biochemistry, 2007","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2020_12","length":826,"ncbi_taxon_id":9031,"date":"2020-01-07T15:35:03.517Z","organism":"Gallus gallus","features":{"gene3D":[{"start":615,"end":733,"id":"G3DSA:3.40.20.10","name":"Severin"},{"start":615,"end":733,"id":"G3DSA:3.40.20.10","name":"Severin"},{"start":615,"end":733,"id":"G3DSA:3.40.20.10","name":"Severin"},{"start":615,"end":733,"id":"G3DSA:3.40.20.10","name":"Severin"},{"start":615,"end":733,"id":"G3DSA:3.40.20.10","name":"Severin"},{"start":615,"end":733,"id":"G3DSA:3.40.20.10","name":"Severin"},{"start":756,"end":826,"id":"G3DSA:1.10.950.10","name":"Villin headpiece domain"}],"pfam":[{"id":"PF00626","name":"Gelsolin repeat","start":27,"end":108},{"id":"PF00626","name":"Gelsolin repeat","start":147,"end":218},{"id":"PF00626","name":"Gelsolin repeat","start":268,"end":343},{"id":"PF00626","name":"Gelsolin repeat","start":408,"end":489},{"id":"PF00626","name":"Gelsolin repeat","start":532,"end":595},{"id":"PF00626","name":"Gelsolin repeat","start":634,"end":707},{"id":"PF02209","name":"Villin headpiece domain","start":791,"end":826}]},"disprot_id":"DP02511","regions_counter":2,"dataset":[],"UniParc":"UPI0000138819","uniref100":"UniRef100_P02640","uniref90":"UniRef90_P02640","uniref50":"UniRef50_P02640","genes":[{"name":{"value":"VIL1"},"synonyms":[{"value":"VIL"}]}],"alphafold_very_low_content":0.07990314769975787,"disorder_content":0.04963680387409201,"disprot_consensus":{"full":[{"start":723,"end":763,"type":"D"}],"Structural state":[{"start":723,"end":763,"type":"D"}],"Disorder function":[{"start":723,"end":763,"type":"F"}]}},{"acc":"Q05022","name":"rRNA biogenesis protein RRP5","sequence":"MVASTKRKRDEDFPLSREDSTKQPSTSSLVRNTEEVSFPRGGASALTPLELKQVANEAASDVLFGNESVKASEPASRPLKKKKTTKKSTSKDSEASSANSDEARAGLIEHVNFKTLKNGSSLLGQISAITKQDLCITFTDGISGYVNLTHISEEFTSILEDLDEDMDSDTDAADEKKSKVEDAEYESSDDEDEKLDKSNELPNLRRYFHIGQWLRCSVIKNTSLEPSTKKSKKKRIELTIEPSSVNIYADEDLVKSTSIQCAVKSIEDHGATLDVGLPGFTGFIAKKDFGNFEKLLPGAVFLGNITKKSDRSIVVNTDFSDKKNKITQISSIDAIIPGQIVDLLCESITKNGIAGKVFGLVSGVVNVSHLRTFSEEDLKHKFVIGSSIRCRIIACLENKSGDKVLILSNLPHILKLEDALRSTEGLDAFPIGYTFESCSIKGRDSEYLYLALDDDRLGKVHSSRVGEIENSENLSSRVLGYSPVDDIYQLSTDPKYLKLKYLRTNDIPIGELLPSCEITSVSSSGIELKIFNGQFKASVPPLHISDTRLVYPERKFKIGSKVKGRVISVNSRGNVHVTLKKSLVNIEDNELPLVSTYENAKNIKEKNEKTLATIQVFKPNGCIISFFGGLSGFLPNSEISEVFVKRPEEHLRLGQTVIVKLLDVDADRRRIIATCKVSNEQAAQQKDTIENIVPGRTIITVHVIEKTKDSVIVEIPDVGLRGVIYVGHLSDSRIEQNRAQLKKLRIGTELTGLVIDKDTRTRVFNMSLKSSLIKDAKKETLPLTYDDVKDLNKDVPMHAYIKSISDKGLFVAFNGKFIGLVLPSYAVDSRDIDISKAFYINQSVTVYLLRTDDKNQKFLLSLKAPKVKEEKKKVESNIEDPVDSSIKSWDDLSIGSIVKAKIKSVKKNQLNVILAANLHGRVDIAEVFDTYEEITDKKQPLSNYKKDDVIKVKIIGNHDVKSHKFLPITHKISKASVLELSMKPSELKSKEVHTKSLEEINIGQELTGFVNNSSGNHLWLTISPVLKARISLLDLADNDSNFSENIESVFPLGSALQVKVASIDREHGFVNAIGKSHVDINMSTIKVGDELPGRVLKIAEKYVLLDLGNKVTGISFITDALNDFSLTLKEAFEDKINNVIPTTVLSVDEQNKKIELSLRPATAKTRSIKSHEDLKQGEIVDGIVKNVNDKGIFVYLSRKVEAFVPVSKLSDSYLKEWKKFYKPMQYVLGKVVTCDEDSRISLTLRESEINGDLKVLKTYSDIKAGDVFEGTIKSVTDFGVFVKLDNTVNVTGLAHITEIADKKPEDLSALFGVGDRVKAIVLKTNPEKKQISLSLKASHFSKEAELASTTTTTTTVDQLEKEDEDEVMADAGFNDSDSESDIGDQNTEVADRKPETSSDGLSLSAGFDWTASILDQAQEEEESDQDQEDFTENKKHKHKRRKENVVQDKTIDINTRAPESVADFERLLIGNPNSSVVWMNYMAFQLQLSEIEKARELAERALKTINFREEAEKLNIWIAMLNLENTFGTEETLEEVFSRACQYMDSYTIHTKLLGIYEISEKFDKAAELFKATAKKFGGEKVSIWVSWGDFLISHNEEQEARTILGNALKALPKRNHIEVVRKFAQLEFAKGDPERGRSLFEGLVADAPKRIDLWNVYVDQEVKAKDKKKVEDLFERIITKKITRKQAKFFFNKWLQFEESEGDEKTIEYVKAKATEYVASHESQKADE","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1408,"region_id":"DP02513r001","reference_id":"28244370","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The density, although weak, was well fitted by the crystal structure of the C-terminal tetratricopeptide repeat (TPR) domain of Rrp5","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Molecular architecture of the 90S small subunit pre-ribosome. <i> Sun Q, Zhu X, Qi J, An W, Lan P, Tan D, Chen R, Wang B, Zheng S, Zhang C, Chen X, Zhang W, Chen J, Dong MQ, Ye K. </i> Elife, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"5WYJ"}],"term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2020_06","length":1729,"ncbi_taxon_id":559292,"date":"2020-01-09T10:43:51.531Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","features":{"gene3D":[{"start":1503,"end":1729,"id":"G3DSA:1.25.40.10","name":"G3DSA:1.25.40.10"}],"pfam":[{"id":"PF00575","name":"S1 RNA binding domain","start":605,"end":676},{"id":"PF00575","name":"S1 RNA binding domain","start":1175,"end":1245},{"id":"PF00575","name":"S1 RNA binding domain","start":1263,"end":1336},{"id":"PF23240","name":"PRP39 N-terminal HAT repeat","start":1622,"end":1709},{"id":"PF29086","name":"Protein RRP5 homolog-like, OB domain","start":878,"end":987}]},"disprot_id":"DP02513","regions_counter":1,"dataset":[],"UniParc":"UPI0000134AD6","uniref100":"UniRef100_Q05022","uniref90":"UniRef90_Q05022","uniref50":"UniRef50_Q05022","genes":[{"name":{"value":"RRP5"},"synonyms":[{"value":"FMI1"}],"orfNames":[{"value":"YM9959.11C"}],"olnNames":[{"value":"YMR229C"}]}],"alphafold_very_low_content":0.13880855986119145,"disorder_content":0.8143435511856565,"disprot_consensus":{"full":[{"start":1,"end":1408,"type":"D"}],"Structural state":[{"start":1,"end":1408,"type":"D"}]}},{"acc":"P36594","name":"DNA-directed RNA polymerase II subunit rpb1","sequence":"MSGIQFSPSSVPLRRVEEVQFGILSPEEIRSMSVAKIEFPETMDESGQRPRVGGLLDPRLGTIDRQFKCQTCGETMADCPGHFGHIELAKPVFHIGFLSKIKKILECVCWNCGKLKIDSSNPKFNDTQRYRDPKNRLNAVWNVCKTKMVCDTGLSAGSDNFDLSNPSANMGHGGCGAAQPTIRKDGLRLWGSWKRGKDESDLPEKRLLSPLEVHTIFTHISSEDLAHLGLNEQYARPDWMIITVLPVPPPSVRPSISVDGTSRGEDDLTHKLSDIIKANANVRRCEQEGAPAHIVSEYEQLLQFHVATYMDNEIAGQPQALQKSGRPLKSIRARLKGKEGRLRGNLMGKRVDFSARTVITGDPNLSLDELGVPRSIAKTLTYPETVTPYNIYQLQELVRNGPDEHPGAKYIIRDTGERIDLRYHKRAGDIPLRYGWRVERHIRDGDVVIFNRQPSLHKMSMMGHRIRVMPYSTFRLNLSVTSPYNADFDGDEMNMHVPQSEETRAEIQEITMVPKQIVSPQSNKPVMGIVQDTLAGVRKFSLRDNFLTRNAVMNIMLWVPDWDGILPPPVILKPKVLWTGKQILSLIIPKGINLIRDDDKQSLSNPTDSGMLIENGEIIYGVVDKKTVGASQGGLVHTIWKEKGPEICKGFFNGIQRVVNYWLLHNGFSIGIGDTIADADTMKEVTRTVKEARRQVAECIQDAQHNRLKPEPGMTLRESFEAKVSRILNQARDNAGRSAEHSLKDSNNVKQMVAAGSKGSFINISQMSACVGQQIVEGKRIPFGFKYRTLPHFPKDDDSPESRGFIENSYLRGLTPQEFFFHAMAGREGLIDTAVKTAETGYIQRRLVKAMEDVMVRYDGTVRNAMGDIIQFAYGEDGLDATLVEYQVFDSLRLSTKQFEKKYRIDLMEDRSLSLYMENSIENDSSVQDLLDEEYTQLVADRELLCKFIFPKGDARWPLPVNVQRIIQNALQIFHLEAKKPTDLLPSDIINGLNELIAKLTIFRGSDRITRDVQNNATLLFQILLRSKFAVKRVIMEYRLNKVAFEWIMGEVEARFQQAVVSPGEMVGTLAAQSIGEPATQMTLNTFHYAGVSSKNVTLGVPRLKEILNVAKNIKTPSLTIYLMPWIAANMDLAKNVQTQIEHTTLSTVTSATEIHYDPDPQDTVIEEDKDFVEAFFAIPDEEVEENLYKQSPWLLRLELDRAKMLDKKLSMSDVAGKIAESFERDLFTIWSEDNADKLIIRCRIIRDDDRKAEDDDNMIEEDVFLKTIEGHMLESISLRGVPNITRVYMMEHKIVRQIEDGTFERADEWVLETDGINLTEAMTVEGVDATRTYSNSFVEILQILGIEATRSALLKELRNVIEFDGSYVNYRHLALLCDVMTSRGHLMAITRHGINRAETGALMRCSFEETVEILMDAAASGEKDDCKGISENIMLGQLAPMGTGAFDIYLDQDMLMNYSLGTAVPTLAGSGMGTSQLPEGAGTPYERSPMVDSGFVGSPDAAAFSPLVQGGSEGREGFGDYGLLGAASPYKGVQSPGYTSPFSSAMSPGYGLTSPSYSPSSPGYSTSPAYMPSSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSATSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPS","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1752,"region_id":"DP02514r001","reference_id":"19458260","start":1498,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The last ordered residue of S. cerevisiae Rpb1 was Leu-1450, whereas the S. pombe chain could be traced as far as residue 1497","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Schizosacharomyces pombe RNA polymerase II at 3.6-A resolution. <i> Spåhr H, Calero G, Bushnell DA, Kornberg RD. </i> Proc Natl Acad Sci U S A, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3H0G"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":1752,"ncbi_taxon_id":284812,"date":"2020-01-09T11:22:32.863Z","organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","features":{"gene3D":[{"start":670,"end":815,"id":"G3DSA:1.10.132.30","name":"G3DSA:1.10.132.30"},{"start":1144,"end":1281,"id":"G3DSA:3.30.1360.140","name":"G3DSA:3.30.1360.140"},{"start":517,"end":669,"id":"G3DSA:1.10.274.100","name":"G3DSA:1.10.274.100"}],"pfam":[{"id":"PF00623","name":"RNA polymerase Rpb1, domain 2","start":348,"end":513},{"id":"PF04983","name":"RNA polymerase Rpb1, domain 3","start":516,"end":675},{"id":"PF04990","name":"RNA polymerase Rpb1, domain 7","start":1144,"end":1280},{"id":"PF04992","name":"RNA polymerase Rpb1, domain 6","start":879,"end":1059},{"id":"PF04997","name":"RNA polymerase Rpb1, domain 1","start":14,"end":346},{"id":"PF04998","name":"RNA polymerase Rpb1, domain 5","start":813,"end":878},{"id":"PF04998","name":"RNA polymerase Rpb1, domain 5","start":1060,"end":1143},{"id":"PF04998","name":"RNA polymerase Rpb1, domain 5","start":1281,"end":1402},{"id":"PF05000","name":"RNA polymerase Rpb1, domain 4","start":700,"end":806},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1579,"end":1592},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1593,"end":1606},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1607,"end":1620},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1621,"end":1634},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1635,"end":1648},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1649,"end":1662},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1663,"end":1676},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1677,"end":1690},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1691,"end":1704},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1712,"end":1725},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1726,"end":1739}]},"disprot_id":"DP02514","regions_counter":2,"dataset":[],"UniParc":"UPI00001345CC","uniref100":"UniRef100_P36594","uniref90":"UniRef90_P36594","uniref50":"UniRef50_P36594","genes":[{"name":{"value":"rpb1"},"orfNames":[{"value":"SPBC28F2.12"}]}],"alphafold_very_low_content":0.18664383561643835,"disorder_content":0.14554794520547945,"disprot_consensus":{"full":[{"start":1498,"end":1752,"type":"D"}],"Structural state":[{"start":1498,"end":1752,"type":"D"}]}},{"acc":"Q13740","name":"CD166 antigen","sequence":"MESKGASSCRLLFCLLISATVFRPGLGWYTVNSAYGDTIIIPCRLDVPQNLMFGKWKYEKPDGSPVFIAFRSSTKKSVQYDDVPEYKDRLNLSENYTLSISNARISDEKRFVCMLVTEDNVFEAPTIVKVFKQPSKPEIVSKALFLETEQLKKLGDCISEDSYPDGNITWYRNGKVLHPLEGAVVIIFKKEMDPVTQLYTMTSTLEYKTTKADIQMPFTCSVTYYGPSGQKTIHSEQAVFDIYYPTEQVTIQVLPPKNAIKEGDNITLKCLGNGNPPPEEFLFYLPGQPEGIRSSNTYTLTDVRRNATGDYKCSLIDKKSMIASTAITVHYLDLSLNPSGEVTRQIGDALPVSCTISASRNATVVWMKDNIRLRSSPSFSSLHYQDAGNYVCETALQEVEGLKKRESLTLIVEGKPQIKMTKKTDPSGLSKTIICHVEGFPKPAIQWTITGSGSVINQTEESPYINGRYYSKIIISPEENVTLTCTAENQLERTVNSLNVSAISIPEHDEADEISDENREKVNDQAKLIVGIVVGLLLAALVAGVVYWLYMKKSKTASKHVNKDLGNMEENKKLEENNHKTEA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":583,"region_id":"DP02515r001","reference_id":"26146185","start":246,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"X-Ray diffraction data for crystals containing CD166 VVC were collected to 1.86 Å and the structure solved by molecular replacement with a search model derived from the second IgSF domain of RAGE (PDB: 3CJJ, 16.4% sequence identity to domain 1 and 30.3% to domain 2; Koch et al., 2010). Only the first two domains could be resolved in the electron density map (Figures 2C and 2D). The crystal lattice did not contain space to accommodate the third domain, suggesting it had been proteolytically cleaved prior to crystal growth.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structures of CD6 and Its Ligand CD166 Give Insight into Their Interaction. <i> Chappell PE, Garner LI, Yan J, Metcalfe C, Hatherley D, Johnson S, Robinson CV, Lea SM, Brown MH. </i> Structure, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5A2F"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":583,"ncbi_taxon_id":9606,"date":"2020-01-09T12:11:12.882Z","organism":"Homo sapiens","features":{"gene3D":[{"start":419,"end":502,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":419,"end":502,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":419,"end":502,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":419,"end":502,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":419,"end":502,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"}],"pfam":[{"id":"PF08205","name":"CD80-like C2-set immunoglobulin domain","start":137,"end":230},{"id":"PF13927","name":"Immunoglobulin domain","start":254,"end":314}]},"disprot_id":"DP02515","regions_counter":1,"dataset":[],"UniParc":"UPI0000126BCA","uniref100":"UniRef100_Q13740","uniref90":"UniRef90_Q13740","uniref50":"UniRef50_Q13740","genes":[{"name":{"value":"ALCAM"},"synonyms":[{"value":"MEMD","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9502422","url":"http://www.ncbi.nlm.nih.gov/pubmed/9502422","alternativeUrl":"https://europepmc.org/abstract/MED/9502422"}}]}]}],"alphafold_very_low_content":0.11320754716981132,"disorder_content":0.5797598627787307,"disprot_consensus":{"full":[{"start":246,"end":583,"type":"D"}],"Structural state":[{"start":246,"end":583,"type":"D"}]}},{"acc":"P56287","name":"Probable translation initiation factor eIF-2B subunit epsilon","sequence":"MPPSKGLNGKLEKPKHALQAIVLSDSYNYRFRPLTLDKPRCLLPLANTPLIEYTFEFLALAGVQEVYVFCCAHAGQIREYIEKSKWNLPSSPFSVNTIVSRESLSVGDALRELDSKQLITSDFILVSGDVVSNVPLNEVLKEHRKRREDDKNAIMTMVVREASPFHRTRARTESSVFVIDKKTSQCVHYQANERGKHYVSMDPEIFNEHEELEVRNDLIDCQIDICSNDVPALFTENFDYQDIRKDFVYGVLTSDLLGKKIHCHVAKENYAARVRSLQTYDAISKDVLSRWVYPFVPDSNLLNQTFSYQRHQIYKEEDVVLARSCIIKARTLIGAYTKVGDASVVANTIIGRNCTIGSNCSIDSAFLWEDVVIGDNCRIGKAILANSVKIGNNCSIEDGAIVAAGVVIGDNTIIEKNKRLTTFESHSQGTLNDPSLVGIGGRGQEYHAEEDSDDEGEFMEASGLIESTNELHLSDSESSETSSSSEEDMEFIPFSARRDSANTINSEDFDEGDFNKEAQQSLERAFEENHQIDIAALELNTLRMAMNANYHEVRSAIVLALLRRIMHLDVSPKEALAKVMTRWGPLLAKLTFSHEEQVDNVLTLQKYCVRLSMTRHFLQLLGYFYQLEIAEENAIQEWYSDPRSSEGELAALRDAGGKQFVDWLNTAESESESEEGSE","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":678,"region_id":"DP02516r001","reference_id":"26901872","start":443,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"the HEAT domains, whose electron densities were not observed in our structure","type":"Figure"},{"text":"We determined the crystal structure of eIF2B at 3.0-Å resolution, and assigned almost all regions except for the ε-subunit HEAT domains","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Crystal structure of eukaryotic translation initiation factor 2B. <i> Kashiwagi K, Takahashi M, Nishimoto M, Hiyama TB, Higo T, Umehara T, Sakamoto K, Ito T, Yokoyama S. </i> Nature, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5B04"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":678,"region_id":"DP02516r002","reference_id":"31048492","start":443,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"missing residues in PDB. Article from the authors that previously identified this region in PMID:26901872","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structural basis for eIF2B inhibition in integrated stress response. <i> Kashiwagi K, Yokoyama T, Nishimoto M, Takahashi M, Sakamoto A, Yonemochi M, Shirouzu M, Ito T. </i> Science, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6JLY"},{"db":"PDB","id":"6JLZ"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":678,"ncbi_taxon_id":284812,"date":"2020-01-09T12:51:58.331Z","organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","features":{"gene3D":[{"start":513,"end":676,"id":"G3DSA:1.25.40.180","name":"G3DSA:1.25.40.180"},{"start":8,"end":360,"id":"G3DSA:3.90.550.10","name":"Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A"}],"pfam":[{"id":"PF00483","name":"Nucleotidyl transferase","start":20,"end":165},{"id":"PF02020","name":"eIF4-gamma/eIF5/eIF2-epsilon","start":596,"end":674},{"id":"PF25084","name":"EIF2B subunit epsilon LbH domain","start":310,"end":413}]},"disprot_id":"DP02516","regions_counter":2,"dataset":[],"UniParc":"UPI0000129AB7","uniref100":"UniRef100_P56287","uniref90":"UniRef90_P56287","uniref50":"UniRef50_P56287","genes":[{"name":{"value":"tif225"},"orfNames":[{"value":"SPAC8C9.15c"}]}],"alphafold_very_low_content":0.10176991150442478,"disorder_content":0.3480825958702065,"disprot_consensus":{"full":[{"start":443,"end":678,"type":"D"}],"Structural state":[{"start":443,"end":678,"type":"D"}]}},{"acc":"Q64487-12","name":"Isoform L of Receptor-type tyrosine-protein phosphatase delta","sequence":"MVPVARPLSLLLTFFLCACAETPPRFTRTPVDQTGVSGGVASFICQATGDPRPKIVWNKKGKKVSNQRFEVIEFDDGSGSVLRIQPLRTPRDEAIYECVASNNVGEISVSTRLTVLREDQIPRGFPTIDMGPQLKVVERTRTATMLCAASGNPDPEITWFKDFLPVDTSNNNGRIKQLRSESIGGTPIRGALQIEQSEESDQGKYECVATNSAGTRYSAPANLYVRELREVRRVPPRFSIPPTNHEIMPGGSVNITCVAVGSPMPYVKWMLGAEDLTPEDDMPIGRNVLELNDVRQSANYTCVAMSTLGVIEAIAQITVKALPKPPGTPVVTESTATSITLTWDSGNPEPVSYYIIQHKPKNSEEPYKEIDGIATTRYSVAGLSPYSDYEFRVVAVNNIGRGPASEPVLTQTSEQAPSSAPRDVQARMLSSTTILVQWKEPEEPNGQIQGYRVYYTMDPTQHVNNWMKHNVADSQITTIGNLVPQKTYSVKVLAFTSIGDGPLSSDIQVITQTGVPGQPLNFKAEPESETSILLSWTPPRSDTIASYELVYRDGDQGEEQRITIEPGTSYRLQGLKPNSLYYFRLSARSPQGLGASTAEISARTMQSMFAKNFHVKAVMKTSVLLSWEIPENYNSAMPFKILYDDGKMVEEVDGRATQKLIVNLKPEKSYSFVLTNRGNSAGGLQHRVTAKTAPDVLRTKPAFIGKTNLDGMITVQLPDVPANENIKGYYIIIVPLKKSRGKFIKPWESPDEMELDELLKEISRKRRSIRYGREVELKPYIAAHFDVLPTEFTLGDDKHYGGFTNKQLQSGQEYVFFVLAVMDHAESKMYATSPYSDPVVSMDLDPQPITDEEEGLIWVVGPVLAVVFIICIVIAILLYKRKRAESESRKSSLPNSKEVPSHHPTDPVELRRLNFQTPGMASHPPIPILELADHIERLKANDNLKFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYVNANYIDGYRKQNAYIATQGSLPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTETHGLVQVTLLDTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCGNTEVPARNLYAYIQKLTQIETGENVTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFLDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGSFDHYAT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":854,"region_id":"DP02517r001","reference_id":"25908590","start":585,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Electron density of the Fn4 domain and subsequent C-terminal region was not visible, likely due to the disorder","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Mechanisms of splicing-dependent trans-synaptic adhesion by PTPδ-IL1RAPL1/IL-1RAcP for synaptic differentiation. <i> Yamagata A, Yoshida T, Sato Y, Goto-Ito S, Uemura T, Maeda A, Shiroshima T, Iwasawa-Okamoto S, Mori H, Mishina M, Fukai S. </i> Nat Commun, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4yh7"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":1501,"ncbi_taxon_id":10090,"date":"2020-01-09T14:24:02.570Z","organism":"Mus musculus","features":{"pfam":[]},"disprot_id":"DP02517","regions_counter":1,"dataset":[],"UniParc":"UPI000258D151","uniref100":"","uniref90":"","uniref50":"","genes":[{"name":{"value":"Ptprd"}}],"disorder_content":0.1798800799467022,"disprot_consensus":{"full":[{"start":585,"end":854,"type":"D"}],"Structural state":[{"start":585,"end":854,"type":"D"}]}},{"acc":"Q8ZRW0","name":"LPS-assembly protein LptD","sequence":"MKKRIPTLLATMIASALYSHQGLAADLASQCMLGVPSYDRPLVKGDTNDLPVTINADNAKGNYPDDAVFTGNVDIMQGNSRLQADEVQLHQKQAEGQPEPVRTVDALGNVHYDDNQVILKGPKGWANLNTKDTNVWEGDYQMVGRQGRGKADLMKQRGENRYTILENGSFTSCLPGSDTWSVVGSEVIHDREEQVAEIWNARFKVGPVPIFYSPYLQLPVGDKRRSGFLIPNAKYTTKNYFEFYLPYYWNIAPNMDATITPHYMHRRGNIMWENEFRYLTQAGEGVMELDYLPSDKVYEDDHPKEGDKHRWLFYWQHSGVMDQVWRFNVDYTKVSDSSYFNDFDSKYGSSTDGYATQKFSVGYAVQNFDATVSTKQFQVFNDQNTSSYSAEPQLDVNYYHNDLGPFDTRIYGQAVHFVNTKDNMPEATRVHLEPTINLPLSNRWGSLNTEAKLMATHYQQTNLDSYNSDPNNKNKLEDSVNRVMPQFKVDGKLIFERDMAMLAPGYTQTLEPRVQYLYVPYRDQSGIYNYDSSLLQSDYNGLFRDRTYGGLDRIASANQVTTGVTTRIYDDAAVERFNVSVGQIYYFTESRTGDDNIKWENDDKTGSLVWAGDTYWRISERWGLRSGVQYDTRLDSVATSSSSLEYRRDQDRLVQLNYRYASPEYIQATLPSYYSTAEQYKNGINQVGAVASWPIADRWSIVGAYYFDTNSSKPADQMLGLQYNSCCYAIRVGYERKLNGWDNDKQHAIYDNAIGFNIELRGLSSNYGLGTQEMLRSNILPYQSSM","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":224,"region_id":"DP02518r001","reference_id":"24990744","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Mass spectrometry confirmed the N-terminal LptD 24–224 amino acids and LptE residues 170–196 were removed by α-chymotrypsin","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structural basis for outer membrane lipopolysaccharide insertion. <i> Dong H, Xiang Q, Gu Y, Wang Z, Paterson NG, Stansfeld PJ, He C, Zhang Y, Wang W, Dong C. </i> Nature, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4N4R"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":224,"region_id":"DP02518r002","reference_id":"24990744","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Mass spectrometry confirmed the N-terminal LptD 24–224 amino acids and LptE residues 170–196 were removed by α-chymotrypsin","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cleavage assay evidence used in manual assertion","version":3,"reference_html":"Structural basis for outer membrane lipopolysaccharide insertion. <i> Dong H, Xiang Q, Gu Y, Wang Z, Paterson NG, Stansfeld PJ, He C, Zhang Y, Wang W, Dong C. </i> Nature, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":224,"region_id":"DP02518r003","reference_id":"24990744","start":24,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Mass spectrometry confirmed the N-terminal LptD 24–224 amino acids and LptE residues 170–196 were removed by α-chymotrypsin","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"spectrometry evidence used in manual assertion","version":3,"reference_html":"Structural basis for outer membrane lipopolysaccharide insertion. <i> Dong H, Xiang Q, Gu Y, Wang Z, Paterson NG, Stansfeld PJ, He C, Zhang Y, Wang W, Dong C. </i> Nature, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007731","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":196,"region_id":"DP02518r004","reference_id":"24990744","start":170,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Mass spectrometry confirmed the N-terminal LptD 24–224 amino acids and LptE residues 170–196 were removed by α-chymotrypsin","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"spectrometry evidence used in manual assertion","version":3,"reference_html":"Structural basis for outer membrane lipopolysaccharide insertion. <i> Dong H, Xiang Q, Gu Y, Wang Z, Paterson NG, Stansfeld PJ, He C, Zhang Y, Wang W, Dong C. </i> Nature, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007731","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":196,"region_id":"DP02518r005","reference_id":"24990744","start":170,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Mass spectrometry confirmed the N-terminal LptD 24–224 amino acids and LptE residues 170–196 were removed by α-chymotrypsin","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cleavage assay evidence used in manual assertion","version":3,"reference_html":"Structural basis for outer membrane lipopolysaccharide insertion. <i> Dong H, Xiang Q, Gu Y, Wang Z, Paterson NG, Stansfeld PJ, He C, Zhang Y, Wang W, Dong C. </i> Nature, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2020_06","length":786,"ncbi_taxon_id":99287,"date":"2020-01-09T14:40:46.752Z","organism":"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","features":{"gene3D":[],"pfam":[{"id":"PF03968","name":"LptA/(LptD N-terminal domain) LPS transport protein","start":53,"end":194},{"id":"PF04453","name":"LPS transport system D","start":309,"end":699}]},"disprot_id":"DP02518","regions_counter":5,"dataset":[],"UniParc":"UPI0000130ED2","uniref100":"UniRef100_Q8ZRW0","uniref90":"UniRef90_P31554","uniref50":"UniRef50_P31554","genes":[{"name":{"value":"lptD","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01411","url":"https://hamap.expasy.org/unirule/MF_01411"}}]},"synonyms":[{"value":"imp"},{"value":"ostA"}],"olnNames":[{"value":"STM0093"}]}],"alphafold_very_low_content":0.01272264631043257,"disorder_content":0.28498727735368956,"disprot_consensus":{"full":[{"start":1,"end":224,"type":"D"}],"Structural state":[{"start":1,"end":224,"type":"D"}]}},{"acc":"Q01080","name":"DNA-directed RNA polymerase I subunit RPA49","sequence":"MSVKRSVSEIEIESVQDQPSVAVGSFFKGFRAPSDTTFDLYKKKKSEKDEFVLHGENERLEYEGYTDSSSQASNQYVVGLFNPEKKSIQLYKAPVLVSKVVSKSSKNLRGPKIKSKSDTRPSALRNALGEAFGTKKAKKAIADLERNRIDSDKLTDSAIDIVDSVRTASKDLPTRAQLDEITSNDRPTPLANIDATDVEQIYPIESIIPKKELQFIRVSSILKEADKEKKLELFPYQNNSKYVAKKLDSLTQPSQMTKLQLLYYLSLLLGVYENRRVNNKTKLLERLNSPPEILVDGILSRFTVIKPGQFGRSKDRSYFIDPQNEDKILCYILAIIMHLDNFIVEITPLAHELNLKPSKVVSLFRVLGAIVKGATVAQAEAFGIPKSTAASYKIATMKVPFKLPEMTRRGRGPRR","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":415,"region_id":"DP02519r001","reference_id":"24153184","start":115,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The C-terminal A49 tWH domain and several other regions are disordered and could not be modelled","type":"Article"},{"text":"A49 tWH domain seems to be mobile in all three crystal forms and thus cannot be modelled","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Crystal structure of the 14-subunit RNA polymerase I. <i> Fernández-Tornero C, Moreno-Morcillo M, Moreno-Morcillo M, Rashid UJ, Taylor NM, Ruiz FM, Gruene T, Legrand P, Steuerwald U, Müller CW. </i> Nature, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4C3J"},{"db":"PDB","id":"4C3H"},{"db":"PDB","id":"4C3I"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":415,"region_id":"DP02519r002","reference_id":"27842382","start":116,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The electron density revealed the downstream DNA, the DNA–RNA hybrid (Fig. 1b), and all Pol I domains with the exception of the flexibly linked C-terminal domain of subunit A49","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structure of RNA polymerase I transcribing ribosomal DNA genes. <i> Neyer S, Kunz M, Geiss C, Hantsche M, Hodirnau VV, Seybert A, Engel C, Scheffer MP, Cramer P, Frangakis AS. </i> Nature, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"5M3F"},{"db":"PDB","id":"5M3M"}],"term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":415,"region_id":"DP02519r003","reference_id":"27867008","start":115,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"the C-terminal tandem winged helix domain (tWH) of A49 was absent in the complex.","type":"Introduction"},{"text":"A49 tWH and A12.2 C-Terminal Domains Are Mobile Elements","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Molecular Structures of Transcribing RNA Polymerase I. <i> Tafur L, Sadian Y, Hoffmann NA, Jakobi AJ, Wetzel R, Hagen WJH, Sachse C, Müller CW. </i> Mol Cell, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"5M5W"},{"db":"PDB","id":"5M5X"}],"term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":415,"region_id":"DP02519r005","reference_id":"27867008","start":115,"term_id":"GO:0003677","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"the C-terminal tandem winged helix domain (tWH) of A49 was absent in the complex.","type":"Introduction"},{"text":"Binding of the tWH to the upstream DNA could stabilize its interaction with the protrusion domain and enforce a closed clamp, thereby enhancing processivity.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy evidence used in manual assertion","version":4,"reference_html":"Molecular Structures of Transcribing RNA Polymerase I. <i> Tafur L, Sadian Y, Hoffmann NA, Jakobi AJ, Wetzel R, Hagen WJH, Sachse C, Müller CW. </i> Mol Cell, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","term_name":"DNA binding","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":403,"region_id":"DP02519r006","reference_id":"27867008","start":182,"term_id":"IDPO:0000011","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Pol I Transition upon DNA Binding","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy evidence used in manual assertion","version":3,"reference_html":"Molecular Structures of Transcribing RNA Polymerase I. <i> Tafur L, Sadian Y, Hoffmann NA, Jakobi AJ, Wetzel R, Hagen WJH, Sachse C, Müller CW. </i> Mol Cell, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","term_name":"disorder to order","ec_go":"IDA","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":415,"region_id":"DP02519r007","reference_id":"27867008","start":115,"term_id":"GO:0098772","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"the C-terminal tandem winged helix domain (tWH) of A49 was absent in the complex.","type":"Introduction"},{"text":"Binding of the tWH to the upstream DNA could stabilize its interaction with the protrusion domain and enforce a closed clamp, thereby enhancing processivity.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy evidence used in manual assertion","version":4,"reference_html":"Molecular Structures of Transcribing RNA Polymerase I. <i> Tafur L, Sadian Y, Hoffmann NA, Jakobi AJ, Wetzel R, Hagen WJH, Sachse C, Müller CW. </i> Mol Cell, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","cross_refs":[{"db":"PDB","id":"5M5X"}],"term_name":"molecular function regulator","ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_06","length":415,"ncbi_taxon_id":559292,"date":"2020-01-09T16:10:34.933Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","features":{"gene3D":[],"pfam":[{"id":"PF06870","name":"A49-like RNA polymerase I associated factor","start":33,"end":404}]},"disprot_id":"DP02519","regions_counter":7,"dataset":[],"UniParc":"UPI0000168AD5","uniref100":"UniRef100_Q01080","uniref90":"UniRef90_Q01080","uniref50":"UniRef50_Q01080","genes":[{"name":{"value":"RPA49"},"synonyms":[{"value":"RRN13"}],"orfNames":[{"value":"N0880"}],"olnNames":[{"value":"YNL248C"}]}],"alphafold_very_low_content":0.02650602409638554,"disorder_content":0.7253012048192771,"disprot_consensus":{"full":[{"start":115,"end":181,"type":"D"},{"start":182,"end":403,"type":"T"},{"start":404,"end":415,"type":"D"}],"Structural state":[{"start":115,"end":415,"type":"D"}],"Molecular function":[{"start":115,"end":415,"type":"F"}],"Structural transition":[{"start":182,"end":403,"type":"T"}]}},{"acc":"G0S3L5","name":"Acetyl-CoA carboxylase-like protein","sequence":"MAEPNGQSAPNGTTSNGRPSYAEKHKLPAHFIGGNRLENAPPSKVKDFVAEHGGHTVITNVLIANNGIAAVKEIRSVRKWAYETFGDERAIKFTVMATPEDLQANADYIRMADHYVEVPGGTNNHNYANVELIVDVAERMDVHAVWAGWGHASENPKLPESLAASPKKIVFIGPPGSAMRSLGDKISSTIVAQHANVPTIPWSGSGVSEVHIDENGIVTVPEEVYLKGCVNSWEEGLEKAREIGFPVMIKASEGGGGKGIRKCMNEDQFEELYKAAAAEIPGSPIFIMKLADSARHLEVQLLADQYGNNISLFGRDCSVQRRHQKIIEEAPVTIASPTTFRAMEEAAVRLGKLVGYVSAGTVEYLYSHADDKFYFLELNPRLQVEHPTTEMVSGVNLPAAQLQIAMGIPLHRIRDIRLLYGVDPKAATEIDFEFKNPESEKTQRRPAPKGHTTACRITSEDPGEGFKPSSGMLQELNFRSSSNVWGYFSVGTAGGIHSFSDSQFGHIFAYGENRAASRKHMIVALKELSIRGDFRTTVEYLIKLLETQAFEENTITTGWLDELISKKLTAERPDTNLAIICGAVIRAHTESEKSLADYRAGLEKGQVPSKDILKTVSSVDFIYEGLRYKFTVTRSSVDTYRLFINGSQCEVGVRTLSDGGLLVLLGGHSHNVYWKDEATGTRISIDGKTCLLEQENDPTQLRTPSPGKLVKYTVESGSHIRAGQTFAEVEVMKMYMPLVAQEDGIVQFIKQPGATLEAGDILGILALDDPSRVKQAQPFVGQLPQYGSPVVVGSKPAQRFAVLYGTMCDILNGYDNQVVMQQKLKEFIEVLRDPKLPYSEFSAQFSALHARMPHKLDAQLTQVLERAQNRGAEFPARQLLKVFNKFLDDNVPNKTDQDLLKSTLEPLTSVLNLYLDGQKARELNLIADLLSMYADVECQFSGRRLQDEEAILKLRDQYKDNIQKVVNTVLSHKNVMSKNSLVLALLDEYRPNKPNVGNVGKHLRPVLRRLTELESRQSAKVSLKAREVLILCALPSLEERTAQMEHILRSSVVQSRYGETGWSHRRPDREVLKEVVDSKYTVFDVLTLFFAHEDPYVALAALEVYVRRAYRAYNLREVRYHDEERPYFIDWDFALRKSGANQTESSMHMQSVVPSSPATPVENDFKRIHSISDMTYLARRTRDEPIRKGVIVPCKDLLDAEEALSRALEVLPLAHKETKDKDRKQQPGIAADLAQRRRPGTPLRLEGIGELSAVVNVAVRDAEGKNDEEILALIKPWVQNSKADLLARRVRRLTFICGRNDGSYPSYYTFRGPDYAEDDSIRHIEPSLAFQLELGRLSKFKLTPVFTQNKNIHVYEAVGRGVETDRRYFTRAVVRPGRLRDEISTAEYLISEADRVVNDIFDALEIIGTNKTDLNHMFINFSHTFQVTADEVAESLQGFLDRFGPRGWRLRVHQVEIRINCMRSDNNDENDTMPLRVIITNTSGFVIQIELYEEKLSEKGEWVYYYVSGNAKIGSMHLLPVSTPYPTKNWLQPKRYKAHILGTQYVYDFPELFRQAIQNSWTEAVKKIPSLAAKQPAIGECIDYNELVLGDQDNLAEVSREPGMNSTGMVGWLINARTPEYPDGRKFIVVANDITFKIGSFGPKEDTFFFKCTELARKMGIPRIYLSANSGARLGLAEELMPHFNVAWNDPAKPEAGFKYLYLSDEAKRRFENEVITEEIVEDGEKRHKIITIVGAEEGLGVECLRGSGLIAGATSRAYNDIFTCTLVTCRSVGIGAYLVRLGQRAVQVEGQPIILTGAPALNSLLGREVYTSNLQLGGTQIMYRNGVSHLTAKDDFDGVTKIVQWLSFIPDQRNNPLPILSPSPDPWDRDVVYTPPYKQTYDVRWMIAGKEDEDGFQPGLFDKDSFVETLGGWARTVVVGRARLGGIPMGVIAVETRTIENITPADPANPDSIEQVTNEAGGVWYPNSAFKTAQAINDFNYGEQLPLMILANWRGFSGGQRDMYNEVLKYGSFIVDALTRFEKPIFIYIPPHGELRGGSWVVVDPTINPASMEMYADEEARGGVLEPEGIIPIKYKKDKQLETMARLDPVYRSLKKEMAKEGLSKEESDNIKKKMQQREELLLPIYHQICVQFADLHDRAGRMKAKGVIRQSLQWRQSRRFFYWRVRRRLIEDDILRRIEEAINPAGKRRHDPENTSLAASPETRSPHLVQLESWVGIPGFKTNDREVVEWYEQNQDRINEKLEKLKKESIADQMRELLRAAESSNPVAAWSGVRDLLRMMPVEEREKVVEYLKQV","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Sordariomycetidae","Sordariales","Chaetomiaceae","Chaetomium"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1185,"region_id":"DP02520r001","reference_id":"27073141","start":1114,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Residues 1,114–1,185, 1,213–1,252, 1,380–1,385, 1,465–1,468 and 2,188–2,195 were disordered in both crystal forms and are not included in the models.","type":"Methods"},{"text":"construct CthCD-CTCter (1,114–2,297)","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"The dynamic organization of fungal acetyl-CoA carboxylase. <i> Hunkeler M, Stuttfeld E, Hagmann A, Imseng S, Maier T. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5I6F"},{"db":"PDB","id":"5I6G"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1252,"region_id":"DP02520r002","reference_id":"27073141","start":1213,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Residues 1,114–1,185, 1,213–1,252, 1,380–1,385, 1,465–1,468 and 2,188–2,195 were disordered in both crystal forms and are not included in the models.","type":"Methods"},{"text":"Residues 1,033–1,035, 1,134–1,152, 1,213–1,252, 1,380–1,385, 1,465–1,468 and 2,188–2,195 were not included in the models.","type":"Methods"},{"text":"In addition, residues 1,032–1,039, 1,134–1,152, 1,213–1,252, 1,380–1,385, 1,465–1,468 and 2,188–2,195 were not included in the model.","type":"Methods"},{"text":"construct CthCD-CTCter (1,114–2,297, PDB:516F and 516G), construct CthCD-CT (788–2,297, PDB:5I6H) and construct CthΔBCCP (1–2,297, Δ700–765, PDB:5I6I)","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"The dynamic organization of fungal acetyl-CoA carboxylase. <i> Hunkeler M, Stuttfeld E, Hagmann A, Imseng S, Maier T. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5I6F"},{"db":"PDB","id":"5I6G"},{"db":"PDB","id":"5I6H"},{"db":"PDB","id":"5I6I"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1152,"region_id":"DP02520r003","reference_id":"27073141","start":1134,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Residues 1,033–1,035, 1,134–1,152, 1,213–1,252, 1,380–1,385, 1,465–1,468 and 2,188–2,195 were not included in the models.","type":"Methods"},{"text":"In addition, residues 1,032–1,039, 1,134–1,152, 1,213–1,252, 1,380–1,385, 1,465–1,468 and 2,188–2,195 were not included in the model.","type":"Curator statement"},{"text":"construct CthCD-CT (788–2,297, PDB:5I6H) and construct CthΔBCCP (1–2,297, Δ700–765, PDB:5I6I)","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"The dynamic organization of fungal acetyl-CoA carboxylase. <i> Hunkeler M, Stuttfeld E, Hagmann A, Imseng S, Maier T. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5I6H"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":699,"region_id":"DP02520r004","reference_id":"27073141","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"To improve crystallizability, we generated ΔBCCP variants of full-length ACC, which, based on SAXS analysis, preserve properties of intact ACC (Supplementary Table 1 and Supplementary Fig. 2a–c). For CthΔBCCP, crystals diffracting to 8.4 Å resolution were obtained. However, molecular replacement did not reveal a unique positioning of the BC domain. Owing to the limited resolution the discussion of structures of CthCD-CT and CthΔBCCP is restricted to the analysis of domain localization. Still, these structures contribute considerably to the visualization of an intrinsically dynamic fungal ACC.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"The dynamic organization of fungal acetyl-CoA carboxylase. <i> Hunkeler M, Stuttfeld E, Hagmann A, Imseng S, Maier T. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5I6I"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":699,"region_id":"DP02520r005","reference_id":"27073141","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"To improve crystallizability, we generated ΔBCCP variants of full-length ACC, which, based on SAXS analysis, preserve properties of intact ACC (Supplementary Table 1 and Supplementary Fig. 2a–c). For CthΔBCCP, crystals diffracting to 8.4 Å resolution were obtained. However, molecular replacement did not reveal a unique positioning of the BC domain. Owing to the limited resolution the discussion of structures of CthCD-CT and CthΔBCCP is restricted to the analysis of domain localization. Still, these structures contribute considerably to the visualization of an intrinsically dynamic fungal ACC.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":3,"reference_html":"The dynamic organization of fungal acetyl-CoA carboxylase. <i> Hunkeler M, Stuttfeld E, Hagmann A, Imseng S, Maier T. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","cross_refs":[{"db":"PDB","id":"5I6I"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":2297,"ncbi_taxon_id":759272,"date":"2020-01-10T10:22:00.731Z","organism":"Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)","features":{"gene3D":[{"start":229,"end":291,"id":"G3DSA:3.30.1490.20","name":"ATP-grasp fold, A domain"}],"pfam":[{"id":"PF00289","name":"Biotin carboxylase, N-terminal domain","start":58,"end":179},{"id":"PF00364","name":"Biotin-requiring enzyme","start":700,"end":764},{"id":"PF01039","name":"Carboxyl transferase domain","start":1619,"end":2171},{"id":"PF02785","name":"Biotin carboxylase C-terminal domain","start":455,"end":562},{"id":"PF02786","name":"Carbamoyl-phosphate synthase L chain, ATP binding domain","start":228,"end":411},{"id":"PF08326","name":"Acetyl-CoA carboxylase, central region","start":766,"end":1517},{"id":"PF21385","name":"Acetyl-CoA carboxylase, BT domain","start":574,"end":693}]},"disprot_id":"DP02520","regions_counter":5,"dataset":[],"UniParc":"UPI000227E158","uniref100":"UniRef100_G0S3L5","uniref90":"UniRef90_G0S3L5","uniref50":"UniRef50_P78820","genes":[{"orfNames":[{"value":"CTHT_0021690","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EGS20342.1","url":"https://www.ebi.ac.uk/ena/browser/view/EGS20342.1"}}]}]}],"disorder_content":0.35306922072268176,"disprot_consensus":{"full":[{"start":1,"end":699,"type":"D"},{"start":1114,"end":1185,"type":"D"},{"start":1213,"end":1252,"type":"D"}],"Structural state":[{"start":1,"end":699,"type":"D"},{"start":1114,"end":1185,"type":"D"},{"start":1213,"end":1252,"type":"D"}]}},{"acc":"A5HC98","sequence":"MDYQEYQQFLARINTARDACVAKDIDVDLLMARHDYFGRELCKSLNIEYRNDVPFIDIILDIRPEVDPLTIDAPHITPDNYLYINNVLYIIDYKVSVSNESSVITYDKYYELTRDISDRLSIPIEIVIIRIDPVSRDLHINSDRFKELYPTIVVDINFNQFFDLKQLLYEKFGDDEEFLLKVAHGDFTLTAPWCKTGCPEFWKHPIYKEFKMSMPVPERRLFEESVKFNAYESERWNTNLVKIREYTKKDYSEHISKSAKNIFLASGFYKQPNKNEISEGWTLMVERVQDQREISKSLHDQKPSIHFIWGAHNPGNSNNATFKLILLSKSLQSIKGISTYTEAFKSLGKMMDIGDKAIEYEEFCMSLKSKARSSWKQIMNKKLEPKQINNALVLWEQQFMINNDLIDKSEKLKLFKNFCGIGKHKQFKNKMLEDLEVSKPKILDFDDANMYLASLTMMEQSKKILSKSNGLKPDNFILNEFGSRIKDANKETYDNMHKIFETGYWQCISDFSTLMKNILSVSQYNRHNTFRIAMCANNNVFAIVFPSADIKTKKATVVYSIIVLHKEEENIFNPGCLHGTFKCMNGYISISRAIRLDKERCQRIVSSPGLFLTTCLLFKHDNPTLVMSDIMNFSIYTSLSITKSVLSLTEPARYMIMNSLAISSNVKDYIAEKFSPYTKTLFSVYMTRLIKNACFDAYDQRQRVQLRDIYLSDYDITQKGIKDNRELTSIWFPGSVTLKEYLTQIYLPFYFNAKGLHEKHHVMVDLAKTILEIECEQRENIKEIWSTNCTKQTVNLKILIHSLCKNLLADTSRHNHLRNRIENRNNFRRSITTISTFTSSKSCLKIGDFRKEKELQSVKQKKILEVQSRKMRLANPMFVTDEQVCLEVGHCNYEMLRNAMPNYTDYISTKVFDRLYELLDKKVLTDKPVIEQIMDMMIDHKKFYFTFFNKGQKTSKDREIFVGEYEAKMCMYAVERIAKERCKLNPDEMISEPGDGKLKVLEQKSEQEIRFLVETTRQKNREIDEAIEALATEGYESNLGKIEKLSLGKAKGLKMEINADMSKWSAQDVFYKYFWLIALDPILYPQEKERILYFMCNYMDKELILPDELLFNLLDQKVAYQNDIIATMTNQLNSNTVLIKRNWLQGNFNYTSSYVHSCAMSVYKEILKEAITLLDGSILVNSLVHSDDNQTSITIVQDKMENDKIIDFAMKEFERACLTFGCQANMKKTYVTNCIKEFVSLFNLYGEPFSIYGRFLLTSVGDCAYIGPYEDLASRISSAQTAIKHGCPPSLAWVSIAISHWMTSLTYNMLPGQSNDPIDYFPAENRKDIPIELNGVLDAPLSMISTVGLESGNLYFLIKLLSKYTPVMQKRESVVNQIAEVKNWKVEDLTDNEIFRLKILRYLVLDAEMDPSDIMGETSDMRGRSILTPRKFTTAGSLRKLYSFSKYQDRLSSPGGMVELFTYLLEKPELLVTKGEDMKDYMESVIFRYNSKRFKESLSIQNPAQLFIEQILFSHKPVIDFSGIRDKYINLHDSRALEKEPDILGKVTFTEAYRLLMRDLSSLELTNDDIQVIYSYIILNDPMMITIANTHILSIYGSPQRRMGMSCSTMPEFRNLKLIHHSPALVLRAYSKNNPDIQGADPTEMARDLVHLKEFVENTNLEEKMKVRIAMNEAEKGQRDIVFELKEMTRFYQVCYEYVKSTEHKIKVFILPAKSYTTTDFCSLMQGNLIKDKEWYTVHYLKQILSGGHKAIMQHNATSEQNIAFECFKLITHFADSFIDSLSRSAFLQLIIDEFSYKDVKVSKLYDIIKNGYNRTDFIPLLFRTGDLRQADLDKYDAMKSHERVTWNDWQTSRHLDMGSINLTITGYNRSITIIGEDNKLTYAELCLTRKTPENITISGRKLLGSRHGLKFENMSKIQTYPGNYYITYRKKDRHQFVYQIHSHESITRRNEEHMAIRTRIYNEITPVCVVNVAEVDGDQRILIRSLDYLNNDIFSLSRIKVGLDEFATIKKAHFSKMVSFEGPPIKTGLLDLTELMKSQDLLNLNYDNIRNSNLISFSKLICCEGSDNINDGLEFLSDDPMNFTEGEAIHSTPIFNIYYSKRGERHMTYRNAIKLLIERETKIFEEAFTFSENGFISPENLGCLEAVVSLIKLLKTNEWSTVIDKCIHICLIKNGMDHMYHSFDVPKCFMGNPITRDINWVMFREFINSLPGTDIPPWNVMTENFKKKCIALINSKFETQRDFSEFTKLMKKEGGRSNIEFD","creator":"fquaglia","dataset":["Viral proteins","RNA-binding proteins"],"date":"2020-01-10T10:59:36.331Z","disprot_id":"DP02521","features":{"gene3D":[],"pfam":[{"id":"PF04196","name":"Bunyavirus RNA dependent RNA polymerase","start":596,"end":1353},{"id":"PF15518","name":"L protein N-terminus","start":5,"end":180},{"id":"PF21561","name":"Virus, RNA-directed RNA polymerase L, thumb ring domain","start":1374,"end":1741}]},"genes":[{"name":{"value":"L","evidences":[],"_id":"685af523b4ac24d5329d9570"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d956f"}],"length":2263,"name":"RNA-directed RNA polymerase L","ncbi_taxon_id":11577,"organism":"Bunyavirus La Crosse","regions_counter":12,"released":"2020_06","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Polyploviricotina","Ellioviricetes","Bunyavirales","Peribunyaviridae","Orthobunyavirus","La Crosse orthobunyavirus"],"UniParc":"UPI000150CB32","uniref100":"UniRef100_A5HC98","uniref50":"UniRef50_A5HC98","uniref90":"UniRef90_A5HC98","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5AMQ","_id":"685af523b4ac24d5329d9537"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":950,"end":959,"interaction_partner":[],"reference_html":"Structural Insights into Bunyavirus Replication and Its Regulation by the vRNA Promoter. <i> Gerlach P, Malet H, Cusack S, Reguera J. </i> Cell, 2015","reference_id":"26004069","region_id":"DP02521r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The L1750 model contains 1652 residues (94.4% complete) with several connecting loops missing, some of which become ordered upon 5′ vRNA binding (Figure 1, Data S1).","_id":"685af523b4ac24d5329d9534"},{"type":"Results","text":"Motif F forms part of the fingertips, the flexible loop between fingers strands β20 and β21 that is only fully ordered when the 5′ vRNA is bound (see above).","_id":"685af523b4ac24d5329d9535"},{"type":"Figure","text":"Upon 5′ vRNA binding (yellow) the backbone interaction with His760 and His761 pulls helix α30 up allowing stabilization of an ordered configuration of the fingertips residues 949–958 (blue sticks).","_id":"685af523b4ac24d5329d9536"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_id":"GO:0003723","term_is_binding":true,"term_is_obsolete":false,"term_name":"RNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-17T09:08:16.674Z","_id":"685af523b4ac24d5329d9538"},"version":5,"_id":"685af523b4ac24d5329d9533","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5AMQ","_id":"685af523b4ac24d5329d953d"},{"db":"PDB","id":"5AMR","_id":"685af523b4ac24d5329d953e"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":950,"end":959,"interaction_partner":[],"reference_html":"Structural Insights into Bunyavirus Replication and Its Regulation by the vRNA Promoter. <i> Gerlach P, Malet H, Cusack S, Reguera J. </i> Cell, 2015","reference_id":"26004069","region_id":"DP02521r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The L1750 model contains 1652 residues (94.4% complete) with several connecting loops missing, some of which become ordered upon 5′ vRNA binding (Figure 1, Data S1).","_id":"685af523b4ac24d5329d953a"},{"type":"Results","text":"Motif F forms part of the fingertips, the flexible loop between fingers strands β20 and β21 that is only fully ordered when the 5′ vRNA is bound (see above).","_id":"685af523b4ac24d5329d953b"},{"type":"Figure","text":"Upon 5′ vRNA binding (yellow) the backbone interaction with His760 and His761 pulls helix α30 up allowing stabilization of an ordered configuration of the fingertips residues 949–958 (blue sticks).","_id":"685af523b4ac24d5329d953c"}],"states_connection":[{"source":"DP02521r008","target":"DP02521r012","_id":"685af523b4ac24d5329d953f"}],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-17T09:08:15.992Z","_id":"685af523b4ac24d5329d9540"},"version":4,"_id":"685af523b4ac24d5329d9539","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5AMQ","_id":"685af523b4ac24d5329d9544"},{"db":"PDB","id":"5AMR","_id":"685af523b4ac24d5329d9545"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":708,"end":717,"interaction_partner":[],"reference_html":"Structural Insights into Bunyavirus Replication and Its Regulation by the vRNA Promoter. <i> Gerlach P, Malet H, Cusack S, Reguera J. </i> Cell, 2015","reference_id":"26004069","region_id":"DP02521r004","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The PDB shows lack of electron densities in this region.","_id":"685af523b4ac24d5329d9542"},{"type":"Results","text":"The L1750 model contains 1652 residues (94.4% complete) with several connecting loops missing, some of which become ordered upon 5′ vRNA binding (Figure 1, Data S1).","_id":"685af523b4ac24d5329d9543"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-17T08:30:30.899Z","_id":"685af523b4ac24d5329d9546"},"version":4,"_id":"685af523b4ac24d5329d9541","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5AMQ","_id":"685af523b4ac24d5329d954a"},{"db":"PDB","id":"5AMR","_id":"685af523b4ac24d5329d954b"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":876,"end":891,"interaction_partner":[],"reference_html":"Structural Insights into Bunyavirus Replication and Its Regulation by the vRNA Promoter. <i> Gerlach P, Malet H, Cusack S, Reguera J. </i> Cell, 2015","reference_id":"26004069","region_id":"DP02521r005","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The PDB shows lack of electron densities in this region.","_id":"685af523b4ac24d5329d9548"},{"type":"Results","text":"The L1750 model contains 1652 residues (94.4% complete) with several connecting loops missing, some of which become ordered upon 5′ vRNA binding (Figure 1, Data S1).","_id":"685af523b4ac24d5329d9549"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-17T08:30:10.231Z","_id":"685af523b4ac24d5329d954c"},"version":4,"_id":"685af523b4ac24d5329d9547","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5AMQ","_id":"685af523b4ac24d5329d9550"},{"db":"PDB","id":"5AMR","_id":"685af523b4ac24d5329d9551"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1408,"end":1424,"interaction_partner":[],"reference_html":"Structural Insights into Bunyavirus Replication and Its Regulation by the vRNA Promoter. <i> Gerlach P, Malet H, Cusack S, Reguera J. </i> Cell, 2015","reference_id":"26004069","region_id":"DP02521r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"A loop (residues 1402 to 1422) at the C-terminal end of the thumb is likely deployed into the polymerase cavity but lacks electron density map, indicating mobility.","_id":"685af523b4ac24d5329d954e"},{"type":"Curator statement","text":"The PDB shows the disordered region 1408-1424.","_id":"685af523b4ac24d5329d954f"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-17T08:29:32.654Z","_id":"685af523b4ac24d5329d9552"},"version":4,"_id":"685af523b4ac24d5329d954d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5AMQ","_id":"685af523b4ac24d5329d9556"},{"db":"PDB","id":"5AMR","_id":"685af523b4ac24d5329d9557"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1532,"end":1543,"interaction_partner":[],"reference_html":"Structural Insights into Bunyavirus Replication and Its Regulation by the vRNA Promoter. <i> Gerlach P, Malet H, Cusack S, Reguera J. </i> Cell, 2015","reference_id":"26004069","region_id":"DP02521r007","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The PDB shows lack of electron densities in this region.","_id":"685af523b4ac24d5329d9554"},{"type":"Results","text":"The L1750 model contains 1652 residues (94.4% complete) with several connecting loops missing, some of which become ordered upon 5′ vRNA binding (Figure 1, Data S1).","_id":"685af523b4ac24d5329d9555"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-17T08:28:30.671Z","_id":"685af523b4ac24d5329d9558"},"version":4,"_id":"685af523b4ac24d5329d9553","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5AMR","_id":"685af523b4ac24d5329d955c"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":950,"end":959,"interaction_partner":[],"reference_html":"Structural Insights into Bunyavirus Replication and Its Regulation by the vRNA Promoter. <i> Gerlach P, Malet H, Cusack S, Reguera J. </i> Cell, 2015","reference_id":"26004069","region_id":"DP02521r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The L1750 model contains 1652 residues (94.4% complete) with several connecting loops missing, some of which become ordered upon 5′ vRNA binding (Figure 1, Data S1).","_id":"685af523b4ac24d5329d955a"},{"type":"Curator statement","text":"The PDB shows lack of electron densities in this region.","_id":"685af523b4ac24d5329d955b"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-17T09:08:12.468Z","_id":"685af523b4ac24d5329d955d"},"version":4,"_id":"685af523b4ac24d5329d9559","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"EMDB","id":"EMD-2930","_id":"685af523b4ac24d5329d9560"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006224","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":185,"end":270,"interaction_partner":[],"reference_html":"Structural Insights into Bunyavirus Replication and Its Regulation by the vRNA Promoter. <i> Gerlach P, Malet H, Cusack S, Reguera J. </i> Cell, 2015","reference_id":"26004069","region_id":"DP02521r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The previously described N-terminal endonuclease domain (residues 1–184) (Reguera et al., 2010) is solvent exposed and differently orientated compared to influenza polymerase (Figure 1C, Figure S4A). However, it is clearly flexibly linked to the central polymerase core, as revealed by its lack of density in one 3D class of the EM map (Figure 2B). An extended linker (residues 185–270), analogous to the influenza PA-linker, that packs on and stabilizes the fingers and palm domains of the RdRp (Figure 1B, Figures S4A and S4B), connects the endonuclease to the PA-C like domain (residues 271–759), which is divided into two lobes (Figures 1A and 1B).","_id":"685af523b4ac24d5329d955f"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-17T08:29:12.719Z","_id":"685af523b4ac24d5329d9561"},"version":3,"_id":"685af523b4ac24d5329d955e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"EMDB","id":"EMD-2930","_id":"685af523b4ac24d5329d9564"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006208","ec_name":"cryogenic electron microscopy evidence used in manual assertion","ec_ontology":"ECO","start":185,"end":270,"interaction_partner":[],"reference_html":"Structural Insights into Bunyavirus Replication and Its Regulation by the vRNA Promoter. <i> Gerlach P, Malet H, Cusack S, Reguera J. </i> Cell, 2015","reference_id":"26004069","region_id":"DP02521r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The previously described N-terminal endonuclease domain (residues 1–184) (Reguera et al., 2010) is solvent exposed and differently orientated compared to influenza polymerase (Figure 1C, Figure S4A). However, it is clearly flexibly linked to the central polymerase core, as revealed by its lack of density in one 3D class of the EM map (Figure 2B). An extended linker (residues 185–270), analogous to the influenza PA-linker, that packs on and stabilizes the fingers and palm domains of the RdRp (Figure 1B, Figures S4A and S4B), connects the endonuclease to the PA-C like domain (residues 271–759), which is divided into two lobes (Figures 1A and 1B).","_id":"685af523b4ac24d5329d9563"}],"states_connection":[],"term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-17T08:31:00.392Z","_id":"685af523b4ac24d5329d9565"},"version":4,"_id":"685af523b4ac24d5329d9562","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5AMQ","_id":"685af523b4ac24d5329d956a"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":950,"end":959,"interaction_partner":[],"reference_html":"Structural Insights into Bunyavirus Replication and Its Regulation by the vRNA Promoter. <i> Gerlach P, Malet H, Cusack S, Reguera J. </i> Cell, 2015","reference_id":"26004069","region_id":"DP02521r012","released":"2022_03","sample":[],"statement":[{"type":"Figure","text":"Upon 5′ vRNA binding (yellow) the backbone interaction with His760 and His761 pulls helix α30 up allowing stabilization of an ordered configuration of the fingertips residues 949–958 (blue sticks).","_id":"685af523b4ac24d5329d956b"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-17T09:08:10.914Z","_id":"685af523b4ac24d5329d956c"},"version":1,"_id":"685af523b4ac24d5329d9569","reference_source":"pmid"}],"__v":0,"disorder_content":0.06672558550596554,"disprot_consensus":{"full":[{"start":185,"end":270,"type":"D"},{"start":708,"end":717,"type":"D"},{"start":876,"end":891,"type":"D"},{"start":950,"end":959,"type":"T"},{"start":1408,"end":1424,"type":"D"},{"start":1532,"end":1543,"type":"D"}],"Structural state":[{"start":185,"end":270,"type":"D"},{"start":708,"end":717,"type":"D"},{"start":876,"end":891,"type":"D"},{"start":950,"end":959,"type":"D"},{"start":1408,"end":1424,"type":"D"},{"start":1532,"end":1543,"type":"D"}],"Molecular function":[{"start":950,"end":959,"type":"F"}],"Structural transition":[{"start":950,"end":959,"type":"T"}],"Disorder function":[{"start":185,"end":270,"type":"F"}]}},{"acc":"Q9BE39","name":"Myosin-7","sequence":"MVDAEMAAFGEAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKEEFVKATILSREGGKVTAETEHGKTVTVKEDQVLQQNPPKFDKIEDMAMLTFLHEPAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKEQATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSSNFQKPRNIKGKPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGFDTPIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERLSRIITRIQAQSRGVLSRMEFKKLLERRDSLLIIQWNIRAFMGVKNWPWMKLYFKIKPLLKSAETEKEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEASLEQEEGKILRAQLEFNQIKAEMERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTKGLNEE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1935,"region_id":"DP02522r001","reference_id":"30275503","start":807,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"structure corresponding to the converter (701–777) and 1st IQ motif (778–806)","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Hypertrophic cardiomyopathy disease results from disparate impairments of cardiac myosin function and auto-inhibition. <i> Robert-Paganin J, Auguin D, Houdusse A. </i> Nat Commun, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6FSA"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":1935,"ncbi_taxon_id":9913,"date":"2020-01-13T12:02:42.969Z","organism":"Bos taurus","features":{"gene3D":[{"start":40,"end":79,"id":"G3DSA:2.30.30.360","name":"Myosin S1 fragment, N-terminal"},{"start":779,"end":837,"id":"G3DSA:4.10.270.10","name":"Myosin, subunit A"},{"start":80,"end":706,"id":"G3DSA:3.40.850.10","name":"Kinesin motor domain"}],"pfam":[{"id":"PF00063","name":"Myosin head (motor domain)","start":88,"end":766},{"id":"PF01576","name":"Myosin tail","start":846,"end":1923},{"id":"PF02736","name":"Myosin N-terminal SH3-like domain","start":23,"end":80}]},"disprot_id":"DP02522","regions_counter":1,"dataset":[],"UniParc":"UPI0000086898","uniref100":"UniRef100_Q9BE39","uniref90":"UniRef90_P12883","uniref50":"UniRef50_P12883","genes":[{"name":{"value":"MYH7"}}],"alphafold_very_low_content":0.047545219638242896,"disorder_content":0.5834625322997417,"disprot_consensus":{"full":[{"start":807,"end":1935,"type":"D"}],"Structural state":[{"start":807,"end":1935,"type":"D"}]}},{"acc":"Q9UKL0","name":"REST corepressor 1","sequence":"MPAMVEKGPEVSGKRRGRNNAAASASAAAASAAASAACASPAATAASGAAASSASAAAASAAAAPNNGQNKSLAAAAPNGNSSSNSWEEGSSGSSSDEEHGGGGMRVGPQYQAVVPDFDPAKLARRSQERDNLGMLVWSPNQNLSEAKLDEYIAIAKEKHGYNMEQALGMLFWHKHNIEKSLADLPNFTPFPDEWTVEDKVLFEQAFSFHGKTFHRIQQMLPDKSIASLVKFYYSWKKTRTKTSVMDRHARKQKREREESEDELEEANGNNPIDIEVDQNKESKKEVPPTETVPQVKKEKHSTQAKNRAKRKPPKGMFLSQEDVEAVSANATAATTVLRQLDMELVSVKRQIQNIKQTNSALKEKLDGGIEPYRLPEVIQKCNARWTTEEQLLAVQAIRKYGRDFQAISDVIGNKSVVQVKNFFVNYRRRFNIDEVLQEWEAEHGKEETNGPSNQKPVKSPDNSIKMPEEEDEAPVLDVRYASAS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":307,"region_id":"DP02523r001","reference_id":"20415477","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Overall  structure  of  the  human  LSD1/CoREST  in  complex  with  14e.  LSD1  (residues 171-836) is in light blue and CoREST (residues 308-440) in blue.","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Biochemical, structural, and biological evaluation of tranylcypromine derivatives as inhibitors of histone demethylases LSD1 and LSD2. <i> Binda C, Valente S, Romanenghi M, Pilotto S, Cirilli R, Karytinos A, Ciossani G, Botrugno OA, Forneris F, Tardugno M, Edmondson DE, Minucci S, Mattevi A, Mai A. </i> J Am Chem Soc, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2XAS"},{"db":"PDB","id":"2XAJ"},{"db":"PDB","id":"2XAH"},{"db":"PDB","id":"2XAG"},{"db":"PDB","id":"2XAQ"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":485,"region_id":"DP02523r002","reference_id":"20415477","start":441,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Overall  structure  of  the  human  LSD1/CoREST  in  complex  with  14e.  LSD1  (residues 171-836) is in light blue and CoREST (residues 308-440) in blue.","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Biochemical, structural, and biological evaluation of tranylcypromine derivatives as inhibitors of histone demethylases LSD1 and LSD2. <i> Binda C, Valente S, Romanenghi M, Pilotto S, Cirilli R, Karytinos A, Ciossani G, Botrugno OA, Forneris F, Tardugno M, Edmondson DE, Minucci S, Mattevi A, Mai A. </i> J Am Chem Soc, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2XAS"},{"db":"PDB","id":"2XAJ"},{"db":"PDB","id":"2XAH"},{"db":"PDB","id":"2XAG"},{"db":"PDB","id":"2XAQ"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":485,"region_id":"DP02523r003","reference_id":"24820421","start":1,"term_id":"GO:0098772","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"CoREST1 showed the highest transcriptional repression among the three proteins.","type":"Results"}],"curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","ec_name":"luciferase reporter gene assay evidence used in manual assertion","version":5,"reference_html":"Differential properties of transcriptional complexes formed by the CoREST family. <i> Barrios ÁP, Gómez AV, Sáez JE, Ciossani G, Toffolo E, Battaglioli E, Mattevi A, Andrés ME. </i> Mol Cell Biol, 2014","date":"2022-03-08T14:51:35.529Z","reference_source":"pmid","ec_id":"ECO:0005648","term_name":"molecular function regulator","ec_go":"IEP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_06","length":485,"ncbi_taxon_id":9606,"date":"2020-01-13T14:15:55.189Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF00249","name":"Myb-like DNA-binding domain","start":194,"end":237},{"id":"PF00249","name":"Myb-like DNA-binding domain","start":385,"end":428},{"id":"PF01448","name":"ELM2 domain","start":105,"end":158},{"id":"PF20878","name":"Helical region in REST corepressor","start":311,"end":374}]},"disprot_id":"DP02523","regions_counter":3,"dataset":[],"UniParc":"UPI0000073120","uniref100":"UniRef100_Q9UKL0","uniref90":"UniRef90_Q9UKL0","uniref50":"UniRef50_Q9UKL0","genes":[{"name":{"value":"RCOR1"},"synonyms":[{"value":"KIAA0071"},{"value":"RCOR"}]}],"alphafold_very_low_content":0.37938144329896906,"disorder_content":0.7257731958762886,"disprot_consensus":{"full":[{"start":1,"end":307,"type":"D"},{"start":308,"end":440,"type":"F"},{"start":441,"end":485,"type":"D"}],"Structural state":[{"start":1,"end":307,"type":"D"},{"start":441,"end":485,"type":"D"}],"Molecular function":[{"start":1,"end":485,"type":"F"}]}},{"acc":"A5YKK6","name":"CCR4-NOT transcription complex subunit 1","sequence":"MNLDSLSLALSQISYLVDNLTKKNYRASQQEIQHIVNRHGPEADRHLLRCLFSHVDFSGDGKSSGKDFHQTQFLIQECALLITKPNFISTLSYAIDNPLHYQKSLKPAPHLFAQLSKVLKLSKVQEVIFGLALLNSSSSDLRGFAAQFIKQKLPDLLRSYIDADVSGNQEGGFQDIAIEVLHLLLSHLLFGQKGAFGVGQEQIDAFLKTLRRDFPQERCPVVLAPLLYPEKRDILMDRILPDSGGVAKTMMESSLADFMQEVGYGFCASIEECRNIIVQFGVREVTAAQVARVLGMMARTHSGLTDGIPLQSISAPGSGIWSDGKDKSDGAQAHTWNVEVLIDVLKELNPSLNFKEVTYELDHPGFQIRDSKGLHNVVYGIQRGLGMEVFPVDLIYRPWKHAEGQLSFIQHSLINPEIFCFADYPCHTVATDILKAPPEDDNREIATWKSLDLIESLLRLAEVGQYEQVKQLFSFPIKHCPDMLVLALLQINTSWHTLRHELISTLMPIFLGNHPNSAIILHYAWHGQGQSPSIRQLIMHAMAEWYMRGEQYDQAKLSRILDVAQDLKALSMLLNGTPFAFVIDLAALASRREYLKLDKWLTDKIREHGEPFIQACMTFLKRRCPSILGGLAPEKDQPKSAQLPPETLATMLACLQACAGSVSQELSETILTMVANCSNVMNKARQPPPGVMPKGRPPSASSLDAISPVQIDPLAGMTSLSIGGSAAPHTQSMQGFPPNLGSAFSTPQSPAKAFPPLSTPNQTTAFSGIGGLSSQLPVGGLGTGSLTGIGTGALGLPAVNNDPFVQRKLGTSGLNQPTFQQSKMKPSDLSQVWPEANQHFSKEIDDEANSYFQRIYNHPPHPTMSVDEVLEMLQRFKDSTIKREREVFNCMLRNLFEEYRFFPQYPDKELHITACLFGGIIEKGLVTYMALGLALRYVLEALRKPFGSKMYYFGIAALDRFKNRLKDYPQYCQHLASISHFMQFPHHLQEYIEYGQQSRDPPVKMQGSITTPGSIALAQAQAQAQVPAKAPLAGQVSTMVTTSTTTTVAKTVTVTRPTGVSFKKDVPPSINTTNIDTLLVATDQTERIVEPPENIQEKIAFIFNNLSQSNMTQKVEELKETVKEEFMPWVSQYLVMKRVSIEPNFHSLYSNFLDTLKNPEFNKMVLNETYRNIKVLLTSDKAAANFSDRSLLKNLGHWLGMITLAKNKPILHTDLDVKSLLLEAYVKGQQELLYVVPFVAKVLESSIRSVVFRPPNPWTMAIMNVLAELHQEHDLKLNLKFEIEVLCKNLALDINELKPGNLLKDKDRLKNLDEQLSAPKKDVKQPEELPPITTTTTSTTPATNTTCTATVPPQPQYSYHDINVYSLAGLAPHITLNPTIPLFQAHPQLKQCVRQAIERAVQELVHPVVDRSIKIAMTTCEQIVRKDFALDSEESRMRIAAHHMMRNLTAGMAMITCREPLLMSISTNLKNSFASALRTASPQQREMMDQAAAQLAQDNCELACCFIQKTAVEKAGPEMDKRLATEFELRKHARQEGRRYCDPVVLTYQAERMPEQIRLKVGGVDPKQLAVYEEFARNVPGFLPTNDLSQPTGFLAQPMKQAWATDDVAQIYDKCITELEQHLHAIPPTLAMNPQAQALRSLLEVVVLSRNSRDAIAALGLLQKAVEGLLDATSGADADLLLRYRECHLLVLKALQDGRAYGSPWCNKQITRCLIECRDEYKYNVEAVELLIRNHLVNMQQYDLHLAQSMENGLNYMAVAFAMQLVKILLVDERSVAHVTEADLFHTIETLMRINAHSRGNAPEGLPQLMEVVRSNYEAMIDRAHGGPNFMMHSGISQASEYDDPPGLREKAEYLLREWVNLYHSAAAGRDSTKAFSAFVGQMHQQGILKTDDLITRFFRLCTEMCVEISYRAQAEQQHNPAANPTMIRAKCYHNLDAFVRLIALLVKHSGEATNTVTKINLLNKVLGIVVGVLLQDHDVRQSEFQQLPYHRIFIMLLLELNAPEHVLETINFQTLTAFCNTFHILRPTKAPGFVYAWLELISHRIFIARMLAHTPQQKGWPMYAQLLIDLFKYLAPFLRNVELTKPMQILYKGTLRVLLVLLHDFPEFLCDYHYGFCDVIPPNCIQLRNLILSAFPRNMRLPDPFTPNLKVDMLSEINIAPRILTNFTGVMPPQFKKDLDSYLKTRSPVTFLSDLRSNLQVSNEPGNRYNLQLINALVLYVGTQAIAHIHNKGSTPSMSTITHSAHMDIFQNLAVDLDTEGRYLFLNAIANQLRYPNSHTHYFSCTMLYLFAEANTEAIQEQITRVLLERLIVNRPHPWGLLITFIELIKNPAFKFWNHEFVHCAPEIEKLFQSVAQCCMGQKQAQQVMEGTGAS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1841,"region_id":"DP02524r002","reference_id":"24121232","start":1565,"term_id":"IDPO:0000002","curator_orcid":"0000-0001-8399-7907","statement":[{"text":"The 3.2-Å-resolution structure of the heterotrimeric complex (Fig. 3, Supplementary Fig. 4c–f and Table 1) contains CNOT1 (1842–2353), CNOT2 (350–540) and CNOT3 (607–748) in a stoichiometry of 1:1:1.","type":"Results"},{"text":"To determine the structure of the CNOT1-C domain, we initially identified a proteolytically stable fragment in CNOT1 (residues 1842–2371; Fig. 1a) that was expressed in a soluble form but failed to crystallize. We then expressed an equivalent fragment of Ct NOT1 (residues 1676–2193; Supplementary Fig. 2), which yielded crystals that diffracted X-rays to 3.2-Å resolution (Table 1).","type":"Results"}],"curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"cleavage assay evidence used in manual assertion","version":4,"reference_html":"Structure and assembly of the NOT module of the human CCR4-NOT complex. <i> Boland A, Chen Y, Raisch T, Jonas S, Kuzuoğlu-Öztürk D, Wohlbold L, Weichenrieder O, Izaurralde E. </i> Nat Struct Mol Biol, 2013","date":"2023-06-05T18:12:56.561Z","reference_source":"pmid","ec_id":"ECO:0007691","cross_refs":[{"db":"PDB","id":"4C0D"}],"term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NZN8"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75175"}]},{"start":1589,"end":1607,"reference_id":"24768540","reference_source":"pmid","reference_html":"A DDX6-CNOT1 complex and W-binding pockets in CNOT9 reveal direct links between miRNA target recognition and silencing. <i> Chen Y, Boland A, Kuzuoğlu-Öztürk D, Bawankar P, Loh B, Chang CT, Weichenrieder O, Izaurralde E. </i> Mol Cell, 2014","date":"2023-06-05T17:55:18.789Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4CRV"},{"db":"PDB","id":"4CRU"}],"region_id":"DP02524r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92600"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6305"}],"statement":[{"text":"Intriguingly, the C-terminal tail of the CN9BD (residues 1,589–1,607) is largely disordered but required for crystallization.","type":"Results"}]}],"released":"2020_06","length":2376,"ncbi_taxon_id":9606,"date":"2020-01-13T14:58:38.471Z","organism":"Homo sapiens","features":{"gene3D":[{"start":1058,"end":1314,"id":"G3DSA:1.25.40.180","name":"G3DSA:1.25.40.180"},{"start":825,"end":1004,"id":"G3DSA:1.25.40.840","name":"G3DSA:1.25.40.840"}],"pfam":[{"id":"PF04054","name":"CCR4-Not complex component, Not1","start":1998,"end":2357},{"id":"PF12842","name":"CCR4-Not complex, Not1 subunit, domain of unknown function DUF3819","start":1387,"end":1534},{"id":"PF16415","name":"CCR4-NOT transcription complex subunit 1 CAF1-binding domain","start":1088,"end":1311},{"id":"PF16417","name":"CCR4-NOT transcription complex subunit 1 TTP binding domain","start":815,"end":1002},{"id":"PF16418","name":"CCR4-NOT transcription complex subunit 1 HEAT repeat","start":500,"end":656},{"id":"PF22940","name":"CCR4-NOT transcription complex subunit 1, N-terminal domain","start":30,"end":227},{"id":"PF23590","name":"CCR4-NOT transcription complex subunit 1, NOT1_connector","start":1610,"end":1814}]},"disprot_id":"DP02524","regions_counter":3,"dataset":["NDDs-related proteins","RNA-binding proteins"],"UniParc":"UPI0001565767","uniref100":"UniRef100_A5YKK6","uniref90":"UniRef90_A5YKK6","uniref50":"UniRef50_A5YKK6","genes":[{"name":{"value":"CNOT1"},"synonyms":[{"value":"CDC39"},{"value":"KIAA1007"},{"value":"NOT1"}],"orfNames":[{"value":"AD-005"}]}],"alphafold_very_low_content":0.15025252525252525,"disorder_content":0.11658249158249158,"disprot_consensus":{"full":[{"start":1565,"end":1841,"type":"D"}],"Structural state":[{"start":1565,"end":1841,"type":"D"}]}},{"acc":"P9WGI1","name":"RNA polymerase sigma factor SigA","sequence":"MAATKASTATDEPVKRTATKSPAASASGAKTGAKRTAAKSASGSPPAKRATKPAARSVKPASAPQDTTTSTIPKRKTRAAAKSAAAKAPSARGHATKPRAPKDAQHEAATDPEDALDSVEELDAEPDLDVEPGEDLDLDAADLNLDDLEDDVAPDADDDLDSGDDEDHEDLEAEAAVAPGQTADDDEEIAEPTEKDKASGDFVWDEDESEALRQARKDAELTASADSVRAYLKQIGKVALLNAEEEVELAKRIEAGLYATQLMTELSERGEKLPAAQRRDMMWICRDGDRAKNHLLEANLRLVVSLAKRYTGRGMAFLDLIQEGNLGLIRAVEKFDYTKGYKFSTYATWWIRQAITRAMADQARTIRIPVHMVEVINKLGRIQRELLQDLGREPTPEELAKEMDITPEKVLEIQQYAREPISLDQTIGDEGDSQLGDFIEDSEAVVAVDAVSFTLLQDQLQSVLDTLSEREAGVVRLRFGLTDGQPRTLDEIGQVYGVTRERIRQIESKTMSKLRHPSRSQVLRDYLD","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":224,"region_id":"DP02525r001","reference_id":"29606590","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Here we report a cryo-EM structure of Mycobacterium tuberculosis RNAP holoenzyme in complex with Lpm at 3.5-Å resolution.","type":"Abstract"},{"text":"For the RNAP β' N and C-termini (residues 1-2 and 1282-1316), the central part of the RNAP β' trigger loop (residues 1014-1022), the RNAP β N and C-termini (residues 1-27 and 1145-1172), the RNAP αI N-terminus and C-terminal domain (residues 1-2 and 227-347), the RNAP αII N-terminus and C-terminal domain (residues 1-2 and 233-347), the RNAP ω N-terminus (residues 1-27), σR1.1 (residues 1-224), and a loop and short extended segment of the σR3-σR4 linker (residues 426-433 and 443-445), density was absent, suggesting very high segmental flexibility; these segments were not fitted.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structural Basis of Transcription Inhibition by Fidaxomicin (Lipiarmycin A3). <i> Lin W, Das K, Degen D, Mazumder A, Duchi D, Wang D, Ebright YW, Ebright RY, Sineva E, Gigliotti M, Srivastava A, Mandal S, Jiang Y, Liu Y, Yin R, Zhang Z, Eng ET, Thomas D, Donadio S, Zhang H, Zhang C, Kapanidis AN, Ebright RH. </i> Mol Cell, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6FBV"}],"term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2020_06","length":528,"ncbi_taxon_id":83332,"date":"2020-01-14T10:37:17.202Z","organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","features":{"gene3D":[{"start":451,"end":528,"id":"G3DSA:1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"start":451,"end":528,"id":"G3DSA:1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}],"pfam":[{"id":"PF00140","name":"Sigma-70 factor, region 1.2","start":226,"end":259},{"id":"PF04539","name":"Sigma-70 region 3","start":374,"end":450},{"id":"PF04542","name":"Sigma-70 region 2","start":295,"end":365},{"id":"PF04545","name":"Sigma-70, region 4","start":463,"end":516}]},"disprot_id":"DP02525","regions_counter":1,"dataset":[],"UniParc":"UPI0000134816","uniref100":"UniRef100_P0A603","uniref90":"UniRef90_P0A603","uniref50":"UniRef50_P0A603","genes":[{"name":{"value":"sigA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00963","url":"https://hamap.expasy.org/unirule/MF_00963"}}]},"synonyms":[{"value":"mysA"},{"value":"rpoD"},{"value":"rpoV"}],"orfNames":[{"value":"MTCY05A6.24"}],"olnNames":[{"value":"Rv2703"}]}],"alphafold_very_low_content":0.3806818181818182,"disorder_content":0.42424242424242425,"disprot_consensus":{"full":[{"start":1,"end":224,"type":"D"}],"Structural state":[{"start":1,"end":224,"type":"D"}]}},{"acc":"C4R4Y0","name":"DNA-directed RNA polymerase subunit","sequence":"MSQFPYSSAPLRSVKEVQFGLLSPEEIRAISVVKIEYPEIMDESRQRPREGGLNDPKLGSIDRNFKCQTCGEGMAECPGHFGHMELAKPVFHIGFIPKIKKVCECICMNCGKLLLDETNPTMAQAIRIRDPKKRFNAVWQLCKTKMVCEADAPVDEYSEQKVVSRGGCGNTQPVVRKDGMKLWGTWKKSGFSDRDAQPERKLLTPGEILNVFKHISPEDCFRLGFNEDYARPEWMIITVLPVPPPQVRPSIAMDETTQGQDDLTHKLSDILKANINVQKLEMDGSPQHIINEVEQLLQFHVATYMDNDIAGQPQALQKSGRPVKAIRARLKGKEGRLRGNLMGKRVDFSARTVISGDPNLELDQVGVPISIAKTLSYPETVTQYNIHRLTEYVRNGPNEHPGAKYVIRDNGDRIDLRYHKRAGDIVLQYGWKVERHLMDDDPVLFNRQPSLHKMSMMAHRVKVMPYSTFRLNLSVTSPYNADFDGDEMNLHVPQSEETRAELSQLCAVPLQIVSPQSNKPVMGIVQDTLCGVRKMTLRDTFIEYEQVMNMLFWVPSWDGVVPQPAILKPKPLWTGKQLLSIAIPSGIHLQRTDGGNSLLSPKDNGMLIVDGKVMFGVVDKKTVGSGGGGLIHTVMREKGPKICAELFGNIQKVVNYWLLHNGFSIGIGDAIADASTMKEITHAISSAKEQVQEIIYKAQHNELELKPGMTLRESFEGEVSRTLNDARDSAGRSAEMNLKDLNNVKQMVSAGSKGSFINIAQMSACVGQQMVEGKRIAFGFADRSLPHFTKDDFSPESKGFVENSYLRGLTPQEFFFHAMAGREGLIDTAVKTAETGYIQRRLVKALEDIMVHYDGTTRNSLGDIIQFLYGEDGLDGTQVERQTIDTIPGSDKAFHKRYYVDLMDEKNSIKPDVIEYAADILGDVELQKELNSEYEQLVSDRKFLREIVFVNGDHNWPLPVNLRRIIQNAQQIFHLDRAKASDLTIPEIIHGVRDLCKKLFVLRGENELIKEAQQNATSLFQCLVRARLATRRILEEFRLNRDAFEWVLGTIEAQFQRSLVHPGEMVGVIAAQSIGEPATQMTLNTFHYAGVSSKNVTLGVPRLKEILNVAKNIKTPALTVYLDREIALDIEKAKVIQSSIEYTTLKNVTSATEIYYDPDPTSTVIEEDFDTVEAYFSIPDEKVEETIDKQSPWLLRLELDRARMLDKQLTMNQVADKISEVFSDDLFVMWSEDNADKLIIRCRVIRDPKAMDEELEAEEDQMLKRIEAHMLDLIALRGIPGISKVYMVKHKVSVPDESGEYKNEELWALETDGINLAEVMAVPGVDSSRTYSNSFVEILSVLGIEATRSSLYKEILNVIAFDGSYVNYRHMALLVDVMTSRGYLMAITRHGINRADTGALMRCSFEETVEILFEAGAAAELDDCRGVSENVMLGQLAPMGTGAFDVMIDEKLLTSLPADYAPTMPLFKGKATQGSATPYDNNAQYDDEFNHDDVADVMFSPMAETGSGDDRSGGLTEYAGIQSPYQPTSPGLSATSPGFAPTSPGFAPTSPRYSPTSPGYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPQYSPTSPQYSPTSPQYSPTSPQYSPTSPQYSPTSPQYSPTSPQYSPTSPQYSPTSPQYSPTSPQYSPTSPQYSPTSPQYSPTSPQYSPTSPQYSPASPQYSPSRHSPNGESKEGE","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Phaffomycetaceae","Komagataella"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1743,"region_id":"DP02526r001","reference_id":"28412353","start":1454,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Region 1454-1743 is invisible in the crystal structure of DNA-directed RNA polymerase subunit.","type":"Curator statement"},{"text":"For the type-2 structure, the stalk was manually fitted to the electron density, and then the clashing residues and the regions with missing electron density were deleted from the structure, using Coot","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Crystal structure of RNA polymerase II from Komagataella pastoris. <i> Ehara H, Umehara T, Sekine SI, Yokoyama S. </i> Biochem Biophys Res Commun, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5X50"},{"db":"PDB","id":"5X51"},{"db":"PDB","id":"5X4Z"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":1743,"ncbi_taxon_id":644223,"date":"2020-01-14T11:21:29.478Z","organism":"Komagataella phaffii (strain GS115 / ATCC 20864)","features":{"gene3D":[{"start":665,"end":810,"id":"G3DSA:1.10.132.30","name":"G3DSA:1.10.132.30"},{"start":1143,"end":1278,"id":"G3DSA:3.30.1360.140","name":"G3DSA:3.30.1360.140"},{"start":512,"end":664,"id":"G3DSA:1.10.274.100","name":"G3DSA:1.10.274.100"}],"pfam":[{"id":"PF00623","name":"RNA polymerase Rpb1, domain 2","start":343,"end":508},{"id":"PF04983","name":"RNA polymerase Rpb1, domain 3","start":511,"end":669},{"id":"PF04990","name":"RNA polymerase Rpb1, domain 7","start":1143,"end":1277},{"id":"PF04992","name":"RNA polymerase Rpb1, domain 6","start":874,"end":1058},{"id":"PF04997","name":"RNA polymerase Rpb1, domain 1","start":12,"end":341},{"id":"PF04998","name":"RNA polymerase Rpb1, domain 5","start":808,"end":873},{"id":"PF04998","name":"RNA polymerase Rpb1, domain 5","start":1059,"end":1142},{"id":"PF04998","name":"RNA polymerase Rpb1, domain 5","start":1278,"end":1399},{"id":"PF05000","name":"RNA polymerase Rpb1, domain 4","start":697,"end":801},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1527,"end":1539},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1541,"end":1553},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1554,"end":1567},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1568,"end":1581},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1582,"end":1595},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1596,"end":1609},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1610,"end":1623},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1624,"end":1637},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1638,"end":1651},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1652,"end":1665},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1666,"end":1679},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1680,"end":1693},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1694,"end":1707},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1708,"end":1721}]},"disprot_id":"DP02526","regions_counter":1,"dataset":[],"UniParc":"UPI0001A4CE88","uniref100":"UniRef100_F2QW17","uniref90":"UniRef90_A0A1B2J8C6","uniref50":"UniRef50_A5DCV3","genes":[{"olnNames":[{"value":"PAS_chr3_0568","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAY70616.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAY70616.1"}}]}]}],"disorder_content":0.1663798049340218,"disprot_consensus":{"full":[{"start":1454,"end":1743,"type":"D"}],"Structural state":[{"start":1454,"end":1743,"type":"D"}]}},{"acc":"P04050","name":"DNA-directed RNA polymerase II subunit RPB1","sequence":"MVGQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETMDETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHFGHIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNELMRQALAIKDSKKRFAAIWTLCKTKMVCETDVPSEDDPTQLVSRGGCGNTQPTIRKDGLKLVGSWKKDRATGDADEPELRVLSTEEILNIFKHISVKDFTSLGFNEVFSRPEWMILTCLPVPPPPVRPSISFNESQRGEDDLTFKLADILKANISLETLEHNGAPHHAIEEAESLLQFHVATYMDNDIAGQPQALQKSGRPVKSIRARLKGKEGRIRGNLMGKRVDFSARTVISGDPNLELDQVGVPKSIAKTLTYPEVVTPYNIDRLTQLVRNGPNEHPGAKYVIRDSGDRIDLRYSKRAGDIQLQYGWKVERHIMDNDPVLFNRQPSLHKMSMMAHRVKVIPYSTFRLNLSVTSPYNADFDGDEMNLHVPQSEETRAELSQLCAVPLQIVSPQSNKPCMGIVQDTLCGIRKLTLRDTFIELDQVLNMLYWVPDWDGVIPTPAIIKPKPLWSGKQILSVAIPNGIHLQRFDEGTTLLSPKDNGMLIIDGQIIFGVVEKKTVGSSNGGLIHVVTREKGPQVCAKLFGNIQKVVNFWLLHNGFSTGIGDTIADGPTMREITETIAEAKKKVLDVTKEAQANLLTAKHGMTLRESFEDNVVRFLNEARDKAGRLAEVNLKDLNNVKQMVMAGSKGSFINIAQMSACVGQQSVEGKRIAFGFVDRTLPHFSKDDYSPESKGFVENSYLRGLTPQEFFFHAMGGREGLIDTAVKTAETGYIQRRLVKALEDIMVHYDNTTRNSLGNVIQFIYGEDGMDAAHIEKQSLDTIGGSDAAFEKRYRVDLLNTDHTLDPSLLESGSEILGDLKLQVLLDEEYKQLVKDRKFLREVFVDGEANWPLPVNIRRIIQNAQQTFHIDHTKPSDLTIKDIVLGVKDLQENLLVLRGKNEIIQNAQRDAVTLFCCLLRSRLATRRVLQEYRLTKQAFDWVLSNIEAQFLRSVVHPGEMVGVLAAQSIGEPATQMTLNTFHFAGVASKKVTSGVPRLKEILNVAKNMKTPSLTVYLEPGHAADQEQAKLIRSAIEHTTLKSVTIASEIYYDPDPRSTVIPEDEEIIQLHFSLLDEEAEQSFDQQSPWLLRLELDRAAMNDKDLTMGQVGERIKQTFKNDLFVIWSEDNDEKLIIRCRVVRPKSLDAETEAEEDHMLKKIENTMLENITLRGVENIERVVMMKYDRKVPSPTGEYVKEPEWVLETDGVNLSEVMTVPGIDPTRIYTNSFIDIMEVLGIEAGRAALYKEVYNVIASDGSYVNYRHMALLVDVMTTQGGLTSVTRHGFNRSNTGALMRCSFEETVEILFEAGASAELDDCRGVSENVILGQMAPIGTGAFDVMIDEESLVKYMPEQKITEIEDGQDGGVTPYSNESGLVNADLDVKDELMFSPLVDSGSNDAMAGGFTAYGGADYGEATSPFGAYGEAPTSPGFGVSSPGFSPTSPTYSPTSPAYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPAYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPSYSPTSPGYSPGSPAYSPKQDEQKHNENENSR","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1716,"region_id":"DP02527r003","reference_id":"28497792","start":1549,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"RNA polymerase II contains a repetitive, intrinsically disordered, C-terminal domain (CTD) composed of heptads of the consensus sequence YSPTSPS. The CTD is heavily phosphorylated and serves as a scaffold, interacting with factors involved in transcription initiation, elongation and termination, RNA processing and chromatin modification.","type":"Abstract"},{"text":"Native gel electrophoresis of the S. cerevisae, D. melanogaster and H. sapiens MBP-CTD fusion proteins, with pIs of 5.57, 5.83, 5.93, respectively. Electrophoretic mobility scales with CTD length, suggesting structural homology.","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","version":3,"reference_html":"Structural heterogeneity in the intrinsically disordered RNA polymerase II C-terminal domain. <i> Portz B, Lu F, Gibbs EB, Mayfield JE, Rachel Mehaffey M, Zhang YJ, Brodbelt JS, Showalter SA, Gilmour DS. </i> Nat Commun, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007689","term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1733,"region_id":"DP02527r004","reference_id":"28300169","start":1456,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Intrinsically disordered CTD of RPB1.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Double-flow focused liquid injector for efficient serial femtosecond crystallography. <i> Oberthuer D, Knoška J, Wiedorn MO, Beyerlein KR, Bushnell DA, Kovaleva EG, Heymann M, Gumprecht L, Kirian RA, Barty A, Mariani V, Tolstikova A, Adriano L, Awel S, Barthelmess M, Dörner K, Xavier PL, Yefanov O, James DR, Nelson G, Wang D, Calvey G, Chen Y, Schmidt A, Szczepek M, Frielingsdorf S, Lenz O, Snell E, Robinson PJ, Šarler B, Belšak G, Maček M, Wilde F, Aquila A, Boutet S, Liang M, Hunter MS, Scheerer P, Lipscomb JD, Weierstall U, Kornberg RD, Spence JC, Pollack L, Chapman HN, Bajt S. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5U5Q"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1733,"region_id":"DP02527r005","reference_id":"26123024","start":1446,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Intrinsically disordered CTD of RPB1.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Molecular basis for 5-carboxycytosine recognition by RNA polymerase II elongation complex. <i> Wang L, Zhou Y, Xu L, Xiao R, Lu X, Chen L, Chong J, Li H, He C, Fu XD, Wang D. </i> Nature, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4Y52"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1733,"region_id":"DP02527r006","reference_id":"21798951","start":1446,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Intrinsically disordered CTD of RPB1.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Initiation complex structure and promoter proofreading. <i> Liu X, Bushnell DA, Silva DA, Huang X, Kornberg RD. </i> Science, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3S16"},{"db":"PDB","id":"3S1N"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1733,"region_id":"DP02527r007","reference_id":"26186291","start":1455,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Intrinsically disordered CTD of RPB1.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Crystal Structure of a Transcribing RNA Polymerase II Complex Reveals a Complete Transcription Bubble. <i> Barnes CO, Calero M, Malik I, Graham BW, Spahr H, Lin G, Cohen AE, Brown IS, Zhang Q, Pullara F, Trakselis MA, Kaplan CD, Calero G. </i> Mol Cell, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5C4X"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":1733,"ncbi_taxon_id":559292,"date":"2020-01-14T13:08:01.269Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","features":{"gene3D":[{"start":664,"end":809,"id":"G3DSA:1.10.132.30","name":"G3DSA:1.10.132.30"},{"start":1141,"end":1275,"id":"G3DSA:3.30.1360.140","name":"G3DSA:3.30.1360.140"},{"start":511,"end":663,"id":"G3DSA:1.10.274.100","name":"G3DSA:1.10.274.100"}],"pfam":[{"id":"PF00623","name":"RNA polymerase Rpb1, domain 2","start":342,"end":507},{"id":"PF04983","name":"RNA polymerase Rpb1, domain 3","start":510,"end":669},{"id":"PF04990","name":"RNA polymerase Rpb1, domain 7","start":1141,"end":1274},{"id":"PF04992","name":"RNA polymerase Rpb1, domain 6","start":873,"end":1056},{"id":"PF04997","name":"RNA polymerase Rpb1, domain 1","start":12,"end":340},{"id":"PF04998","name":"RNA polymerase Rpb1, domain 5","start":807,"end":872},{"id":"PF04998","name":"RNA polymerase Rpb1, domain 5","start":1057,"end":1140},{"id":"PF04998","name":"RNA polymerase Rpb1, domain 5","start":1275,"end":1396},{"id":"PF05000","name":"RNA polymerase Rpb1, domain 4","start":695,"end":800},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1550,"end":1563},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1564,"end":1577},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1585,"end":1598},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1599,"end":1612},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1613,"end":1626},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1627,"end":1640},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1641,"end":1654},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1655,"end":1668},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1669,"end":1682},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1683,"end":1696},{"id":"PF05001","name":"RNA polymerase Rpb1 C-terminal repeat","start":1697,"end":1710}]},"disprot_id":"DP02527","regions_counter":7,"dataset":["Condensates-related proteins"],"UniParc":"UPI0000168E01","uniref100":"UniRef100_P04050","uniref90":"UniRef90_P04050","uniref50":"UniRef50_P04050","genes":[{"name":{"value":"RPO21"},"synonyms":[{"value":"RPB1"},{"value":"RPB220"},{"value":"SUA8"}],"orfNames":[{"value":"D2150"}],"olnNames":[{"value":"YDL140C"}]}],"alphafold_very_low_content":0.16272360069244085,"disorder_content":0.1661858049624928,"disprot_consensus":{"full":[{"start":1446,"end":1733,"type":"D"}],"Structural state":[{"start":1446,"end":1733,"type":"D"}]}},{"acc":"Q80UG2","name":"Plexin-A4","sequence":"MKAMPWNWTCLLSHLLVVGMGSSTLLPRQPPQLSQKPSFVTFRGEPAEGFNHLVVDERTGHIYLGAVNRIYKLSSDLKVLVTHQTGPDEDNPKCYPPRIVQTCNEPLASTNNVNKMLLIDYKENRLIACGSLYQGICKLLRLEDLFKLGEPFHKKEHYLSGVNESGSVFGVIVSYSNFDDKLFIATAVDGKPEYFPTISSRKLTKNSEADGMFAYVFHDEFVASMIKIPSDTFTVIPDFDIYYVYGFSSGNFVYFLTLQPEMVSPPGSTTKEQVYTSKLVRLCKEDTAFNSYVEVPIGCERNGVEYRLLQAAYLSKAGAVLGRTLGVRPDDDLLFTVFSKGQKRKMKSLDESALCIFILKQINDRIKDRLQSCYRGEGTLDLAWLKVKDIPCSSALLTIDDNFCGLDMNAPLGVSEMVRGIPVFTEDRDRMTSVIAYVYKNHSLAFVGTKSGKLKKIRVDGPKGNALQYETVQVVDSGPVLRDMAFSKDHEQLYIMSERQLTRVPVESCGQYRSCGECLGSGDPHCGWCVLHNTCTRKERCERSREPRRFASEMKQCVRLTVHPNNISVSQYNVLLVLETYNVPELSAGVNCTFEDLSEMDGLVIGNQIQCYSPAAKEVPRIITENGDHHVVQLQLKSKETGMTFASTSFVFYNCSVHNSCLSCVESPYRCHWCKYRHVCTHDPNTCSFQEGRVKLPEDCPQLLRVDKILVPVEVIKPITLKAKNLPQPQSGQRGYECILNIQGIEQRVPALRFNSSSVQCQNTSYSYEGMEINNLPVELTVVWNGHFNIDNPAQNKVYLYKCGAMRESCGLCLKADPDFECGWCQSPGQCTLRQHCPAHESRWLELSGANSKCTNPRITEIIPVTGPREGGTKVTIRGENLGLEFRDIASHVKVAGVECSPLVDGYIPAEQIVCEMGEAKPSQHAGFVEICVAVCRPEFMARSSQLYYFMTLTLADLKPNRGPMSGGTQVTITGTNLNAGSNVVVMFGSQPCLFHRRSPSYIICNTTSSEEVLDMKVTVQVDRARIRQDLVFQYVEDPTIVRIEPEWSIVSGNTPIAVWGTHLDLIQNPQIRAKHGGKEHINICEVLNATEMTCQAPALALGPDHQSDLTERPEEFGFILDNVQSLLILNKTNFTYYPNPVFEAFSPSGILELKPGTPIILKGKNLIPPVAGGNVKLNYTVLVGEKPCTVTVSDVQLLCESPNLIGRHKVMARVGGMEYSPGMVYIAPDSPLSLPAIVSIAVAGGLLIIFIVAVLIAYKRKSRESDLTLKRLQMQMDNLESRVALECKEAFAELQTDIHELTSDLDGAGIPFLDYRTYTMRVLFPGIEDHPVLRDLEVPGYRQERVEKGLKLFAQLINNKVFLLSFIRTLESQRSFSMRDRGNVASLIMTVLQSKLEYATDVLKQLLADLIDKNLESKNHPKLLLRRTESVAEKMLTNWFTFLLYKFLKECAGEPLFSLFCAIKQQMEKGPIDAITGEARYSLSEDKLIRQQIEYKTLVLSCVSPDNVNSPEVPVKILNCDTITQVKEKILDAIFKNVPCSHRPKAADMDLEWRQGSGARMILQDEDITTKIENDWKRLNTVAHYQVPDGSVVALVSKQVTAYNAVNNSTVSRTSASKYENMIRYTGSPDSLRSRTPMITPDLESGVKLWHLVKNHEHGDQKEGDRGSKMVSEIYLTRLLATKGTLQKFVDDLFETIFSTAHRGSALPLAIKYMFDFLDEQADKHGIHDPHVRHTWKSNCLPLRFWVNMIKNPQFVFDIHKNSITDACLSVVAQTFMDSCSTSEHRLGKDSPSNKLLYAKDIPSYKNWVERYYSDIGKMPAISDQDMNAYLAEQSRMHMNEFNTMSALSEIFSYVGKYSEEILGPLDHDDQCGKQKLAYKLEQVITLMSLDS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1229,"region_id":"DP02528r001","reference_id":"27397516","start":920,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In five out of 13 full extracellular structures all ten domains are resolved whereas in the other eight structures some of the C-terminal domains were not modeled due to fragmentary or absent electron density. This indicates that some flexibility is present in the extracellular segment of plexins.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structural Basis for Plexin Activation and Regulation. <i> Kong Y, Janssen BJ, Malinauskas T, Vangoor VR, Coles CH, Kaufmann R, Ni T, Gilbert RJ, Padilla-Parra S, Pasterkamp RJ, Jones EY. </i> Neuron, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5L5M"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1229,"region_id":"DP02528r002","reference_id":"27397516","start":1004,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In five out of 13 full extracellular structures all ten domains are resolved whereas in the other eight structures some of the C-terminal domains were not modeled due to fragmentary or absent electron density. This indicates that some flexibility is present in the extracellular segment of plexins.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structural Basis for Plexin Activation and Regulation. <i> Kong Y, Janssen BJ, Malinauskas T, Vangoor VR, Coles CH, Kaufmann R, Ni T, Gilbert RJ, Padilla-Parra S, Pasterkamp RJ, Jones EY. </i> Neuron, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5L5L"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":1893,"ncbi_taxon_id":10090,"date":"2020-01-14T13:12:38.382Z","organism":"Mus musculus","features":{"gene3D":[{"start":1351,"end":1863,"id":"G3DSA:1.10.555.10","name":"Rho GTPase activation protein"},{"start":1129,"end":1221,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":1129,"end":1221,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":1129,"end":1221,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":1129,"end":1221,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":1129,"end":1221,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":40,"end":507,"id":"G3DSA:2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"}],"pfam":[{"id":"PF01403","name":"Sema domain","start":309,"end":486},{"id":"PF01437","name":"Plexin repeat","start":508,"end":557},{"id":"PF01437","name":"Plexin repeat","start":803,"end":854},{"id":"PF01833","name":"IPT/TIG domain","start":857,"end":937},{"id":"PF01833","name":"IPT/TIG domain","start":957,"end":1035},{"id":"PF01833","name":"IPT/TIG domain","start":1039,"end":1114},{"id":"PF01833","name":"IPT/TIG domain","start":1141,"end":1217},{"id":"PF08337","name":"Plexin cytoplasmic RasGAP domain","start":1310,"end":1483},{"id":"PF08337","name":"Plexin cytoplasmic RasGAP domain","start":1597,"end":1863},{"id":"PF17960","name":"TIG domain","start":563,"end":653},{"id":"PF18020","name":"TIG domain found in plexin","start":708,"end":801},{"id":"PF20170","name":"Plexin cytoplasmic RhoGTPase-binding domain","start":1484,"end":1596},{"id":"PF24479","name":"Plexin A/B, PSI domain","start":661,"end":687}]},"disprot_id":"DP02528","regions_counter":2,"dataset":[],"UniParc":"UPI0000001E2C","uniref100":"UniRef100_Q80UG2","uniref90":"UniRef90_Q80UG2","uniref50":"UniRef50_Q80UG2","genes":[{"name":{"value":"Plxna4"},"synonyms":[{"value":"Kiaa1550"}]}],"alphafold_very_low_content":0.058637083993660855,"disorder_content":0.16376122556788167,"disprot_consensus":{"full":[{"start":920,"end":1229,"type":"D"}],"Structural state":[{"start":920,"end":1229,"type":"D"}]}},{"acc":"Q92558","name":"Wiskott-Aldrich syndrome protein family member 1","sequence":"MPLVKRNIDPRHLCHTALPRGIKNELECVTNISLANIIRQLSSLSKYAEDIFGELFNEAHSFSFRVNSLQERVDRLSVSVTQLDPKEEELSLQDITMRKAFRSSTIQDQQLFDRKTLPIPLQETYDVCEQPPPLNILTPYRDDGKEGLKFYTNPSYFFDLWKEKMLQDTEDKRKEKRKQKQKNLDRPHEPEKVPRAPHDRRREWQKLAQGPELAEDDANLLHKHIEVANGPASHFETRPQTYVDHMDGSYSLSALPFSQMSELLTRAEERVLVRPHEPPPPPPMHGAGDAKPIPTCISSATGLIENRPQSPATGRTPVFVSPTPPPPPPPLPSALSTSSLRASMTSTPPPPVPPPPPPPATALQAPAVPPPPAPLQIAPGVLHPAPPPIAPPLVQPSPPVARAAPVCETVPVHPLPQGEVQGLPPPPPPPPLPPPGIRPSSPVTVTALAHPPSGLHPTPSTAPGPHVPLMPPSPPSQVIPASEPKRHPSTLPVISDARSVLLEAIRKGIQLRKVEEQREQEAKHERIENDVATILSRRIAVEYSDSEDDSEFDEVDWLE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":494,"region_id":"DP02529r001","start":185,"term_id":"IDPO:0000002","statement":[{"text":"For this, we determined the 2.43-Å crystal structure of a complex co-crystallized from a variant of the WIRS-containing peptide (WGAERSM*STFGKEKA, M* for selenomethionine, Fig. 1B) and a minimal inhibited WRC, which lacks the C-terminus of Abi and the proline-rich region of WAVE, miniWRC (Fig. 2, Table S1) (Chen et al., 2010).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24439376","version":2,"reference_html":"The WAVE regulatory complex links diverse receptors to the actin cytoskeleton. <i> Chen B, Brinkmann K, Chen Z, Pak CW, Liao Y, Shi S, Henry L, Grishin NV, Bogdan S, Rosen MK. </i> Cell, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4N78"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T13:57:20.532Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":559,"region_id":"DP02529r002","start":545,"term_id":"IDPO:0000002","statement":[{"text":"The A-region of the VCA (residues 545-559) is likely disordered, as it is not observed in the electron density.","type":"Article"}],"curator_id":"vnugnes","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"21107423","version":3,"reference_html":"Structure and control of the actin regulatory WAVE complex. <i> Chen Z, Borek D, Padrick SB, Gomez TS, Metlagel Z, Ismail AM, Umetani J, Billadeau DD, Otwinowski Z, Rosen MK. </i> Nature, 2010","date":"2023-06-13T14:20:13.685Z","reference_source":"pmid","ec_id":"ECO:0006220","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":517,"end":526,"reference_id":"24439376","reference_source":"pmid","reference_html":"The WAVE regulatory complex links diverse receptors to the actin cytoskeleton. <i> Chen B, Brinkmann K, Chen Z, Pak CW, Liao Y, Shi S, Henry L, Grishin NV, Bogdan S, Rosen MK. </i> Cell, 2014","date":"2023-06-13T14:13:23.910Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4N78"}],"region_id":"DP02529r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NYB9"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8WUW1"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y2A7"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q7L576"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9P2E7"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"}],"statement":[{"text":"The crystal structure lacks electron density in this region, indication it is disordered. ","type":"Curator statement"}]},{"start":1,"end":14,"reference_id":"24439376","reference_source":"pmid","reference_html":"The WAVE regulatory complex links diverse receptors to the actin cytoskeleton. <i> Chen B, Brinkmann K, Chen Z, Pak CW, Liao Y, Shi S, Henry L, Grishin NV, Bogdan S, Rosen MK. </i> Cell, 2014","date":"2023-06-13T14:13:38.427Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4N78"}],"region_id":"DP02529r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NYB9"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8WUW1"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y2A7"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q7L576"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9P2E7"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"}],"statement":[{"text":"The crystal structure lacks electron density in this region, indication it is disordered. ","type":"Curator statement"}]},{"start":544,"end":559,"reference_id":"24439376","reference_source":"pmid","reference_html":"The WAVE regulatory complex links diverse receptors to the actin cytoskeleton. <i> Chen B, Brinkmann K, Chen Z, Pak CW, Liao Y, Shi S, Henry L, Grishin NV, Bogdan S, Rosen MK. </i> Cell, 2014","date":"2023-06-13T14:17:19.227Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4N78"}],"region_id":"DP02529r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NYB9"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8WUW1"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y2A7"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q7L576"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9P2E7"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"}],"statement":[{"text":"The crystal structure lacks electron density in this region, indication it is disordered. ","type":"Curator statement"}]}],"released":"2021_06","length":559,"ncbi_taxon_id":9606,"date":"2020-01-23T17:41:08.998Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF02205","name":"WH2 motif","start":495,"end":520},{"id":"PF27569","name":"SCAR helical domain","start":3,"end":180}]},"disprot_id":"DP02529","regions_counter":6,"dataset":["NDDs-related proteins"],"UniParc":"UPI000003AC31","uniref100":"UniRef100_Q92558","uniref90":"UniRef90_Q92558","uniref50":"UniRef50_Q92558","genes":[{"name":{"value":"WASF1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:12732","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:12732"}}]},"synonyms":[{"value":"KIAA0269"},{"value":"SCAR1"},{"value":"WAVE1"}]}],"alphafold_very_low_content":0.334525939177102,"disorder_content":0.6261180679785331,"disprot_consensus":{"full":[{"start":1,"end":14,"type":"D"},{"start":185,"end":494,"type":"D"},{"start":517,"end":526,"type":"D"},{"start":544,"end":559,"type":"D"}],"Structural state":[{"start":1,"end":14,"type":"D"},{"start":185,"end":494,"type":"D"},{"start":517,"end":526,"type":"D"},{"start":544,"end":559,"type":"D"}]}},{"acc":"P18564","name":"Integrin beta-6","sequence":"MGIELLCLFFLFLGRNDHVQGGCALGGAETCEDCLLIGPQCAWCAQENFTHPSGVGERCDTPANLLAKGCQLNFIENPVSQVEILKNKPLSVGRQKNSSDIVQIAPQSLILKLRPGGAQTLQVHVRQTEDYPVDLYYLMDLSASMDDDLNTIKELGSRLSKEMSKLTSNFRLGFGSFVEKPVSPFVKTTPEEIANPCSSIPYFCLPTFGFKHILPLTNDAERFNEIVKNQKISANIDTPEGGFDAIMQAAVCKEKIGWRNDSLHLLVFVSDADSHFGMDSKLAGIVIPNDGLCHLDSKNEYSMSTVLEYPTIGQLIDKLVQNNVLLIFAVTQEQVHLYENYAKLIPGATVGLLQKDSGNILQLIISAYEELRSEVELEVLGDTEGLNLSFTAICNNGTLFQHQKKCSHMKVGDTASFSVTVNIPHCERRSRHIIIKPVGLGDALELLVSPECNCDCQKEVEVNSSKCHHGNGSFQCGVCACHPGHMGPRCECGEDMLSTDSCKEAPDHPSCSGRGDCYCGQCICHLSPYGNIYGPYCQCDNFSCVRHKGLLCGGNGDCDCGECVCRSGWTGEYCNCTTSTDSCVSEDGVLCSGRGDCVCGKCVCTNPGASGPTCERCPTCGDPCNSKRSCIECHLSAAGQAREECVDKCKLAGATISEEEDFSKDGSVSCSLQGENECLITFLITTDNEGKTIIHSINEKDCPKPPNIPMIMLGVSLAILLIGVVLLCIWKLLVSFHDRKEVAKFEAERSKAKWQTGTNPLYRGSTSTFKNVTYKHREKQKVDLSTDC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":788,"region_id":"DP02530r001","reference_id":"25383667","start":492,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Soluble αVβ6 headpiece was prepared similarly as in ref. 33. In brief, the αV headpiece (residues 1–594) with the M400C mutation was followed by a 3C protease site","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structural determinants of integrin β-subunit specificity for latent TGF-β. <i> Dong X, Hudson NE, Lu C, Springer TA. </i> Nat Struct Mol Biol, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4UM8"},{"db":"PDB","id":"4UM9"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":788,"region_id":"DP02530r002","reference_id":"11821050","start":1,"term_id":"GO:0140677","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The integrin alpha v beta 6 binds and activates latent TGF beta 1: a mechanism for regulating pulmonary inflammation and fibrosis.","type":"Title"},{"text":"To demonstrate that full-length α vβ 6 also binds to LAP, we repeated affinity chromatography with unlabeled octylglucoside lysates of β 6-transfected SW480 cells (Figure 1D). A 95 kDa protein corresponding to full-length β 6 was detected by Western blotting in eluted fractions from LAP-Sepharose but not from BSA-Sepharose.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"qualitative western immunoblotting evidence used in manual assertion","version":4,"reference_html":"The integrin alphaVbeta6 binds and activates latent TGFbeta3. <i> Annes JP, Rifkin DB, Munger JS. </i> FEBS Lett, 2002","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000279","term_name":"molecular function activator activity","ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_06","length":788,"ncbi_taxon_id":9606,"date":"2020-01-23T17:51:46.291Z","organism":"Homo sapiens","features":{"gene3D":[{"start":129,"end":373,"id":"G3DSA:3.40.50.410","name":"von Willebrand factor, type A domain"}],"pfam":[{"id":"PF00362","name":"Integrin beta chain VWA domain","start":129,"end":375},{"id":"PF07965","name":"Integrin beta tail domain","start":622,"end":706},{"id":"PF07974","name":"EGF-like domain","start":544,"end":574},{"id":"PF07974","name":"EGF-like domain","start":583,"end":614},{"id":"PF08725","name":"Integrin beta cytoplasmic domain","start":731,"end":774},{"id":"PF17205","name":"Integrin plexin domain","start":28,"end":71},{"id":"PF18372","name":"Integrin beta epidermal growth factor like domain 1","start":456,"end":485},{"id":"PF23105","name":"Integrin EGF domain","start":499,"end":538}]},"disprot_id":"DP02530","regions_counter":2,"dataset":[],"UniParc":"UPI000014BEC0","uniref100":"UniRef100_P18564","uniref90":"UniRef90_P18564","uniref50":"UniRef50_P18564","genes":[{"name":{"value":"ITGB6"}}],"alphafold_very_low_content":0.04568527918781726,"disorder_content":0.3769035532994924,"disprot_consensus":{"full":[{"start":1,"end":491,"type":"F"},{"start":492,"end":788,"type":"D"}],"Structural state":[{"start":492,"end":788,"type":"D"}],"Molecular function":[{"start":1,"end":788,"type":"F"}]}},{"acc":"S6B291","name":"IgG H chain","sequence":"MEFGLSWLFLVAILKGVQCEVQLLESGGDLVQPGGSLRLSCAASGFTFSTYAMSWVRQAPGKGLEWVSGIGDSGHSIYYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCATGSQWPGDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":465,"region_id":"DP02531r001","start":240,"term_id":"IDPO:0000002","statement":[{"text":"The CH1 domain is intrinsically unfolded in the absence of CL and binds to the molecular chaperone BiP. Only when the heavy chain engages the light chain can CH1 be released from BiP to allow a fully assembled IgG molecule to be secreted","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24463572","version":2,"reference_html":"Generation of bispecific IgG antibodies by structure-based design of an orthogonal Fab interface. <i> Lewis SM, Wu X, Pustilnik A, Sereno A, Huang F, Rick HL, Guntas G, Leaver-Fay A, Smith EM, Ho C, Hansen-Estruch C, Chamberlain AK, Truhlar SM, Conner EM, Atwell S, Kuhlman B, Demarest SJ. </i> Nat Biotechnol, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4LLY"},{"db":"PDB","id":"4LLW"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":466,"ncbi_taxon_id":9606,"date":"2020-01-23T18:00:12.752Z","organism":"Homo sapiens","features":{"gene3D":[{"start":357,"end":466,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":357,"end":466,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":357,"end":466,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":357,"end":466,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"}],"pfam":[{"id":"PF07654","name":"Immunoglobulin C1-set domain","start":144,"end":224},{"id":"PF07654","name":"Immunoglobulin C1-set domain","start":259,"end":347},{"id":"PF07654","name":"Immunoglobulin C1-set domain","start":367,"end":451},{"id":"PF07686","name":"Immunoglobulin V-set domain","start":31,"end":134}]},"disprot_id":"DP02531","regions_counter":1,"dataset":[],"UniParc":"UPI00035916D5","uniref100":"UniRef100_S6B291","uniref90":"UniRef90_Q6MZV7","uniref50":"UniRef50_P01857","genes":[],"alphafold_very_low_content":0.04721030042918455,"disorder_content":0.48497854077253216,"disprot_consensus":{"full":[{"start":240,"end":465,"type":"D"}],"Structural state":[{"start":240,"end":465,"type":"D"}]}},{"acc":"Q07866","name":"Kinesin light chain 1","sequence":"MYDNMSTMVYIKEDKLEKLTQDEIISKTKQVIQGLEALKNEHNSILQSLLETLKCLKKDDESNLVEEKSNMIRKSLEMLELGLSEAQVMMALSNHLNAVESEKQKLRAQVRRLCQENQWLRDELANTQQKLQKSEQSVAQLEEEKKHLEFMNQLKKYDDDISPSEDKDTDSTKEPLDDLFPNDEDDPGQGIQQQHSSAAAAAQQGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKDAANLLNDALAIREKTLGKDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKDHPDVAKQLNNLALLCQNQGKYEEVEYYYQRALEIYQTKLGPDDPNVAKTKNNLASCYLKQGKFKQAETLYKEILTRAHEREFGSVDDENKPIWMHAEEREECKGKQKDGTSFGEYGGWYKACKVDSPTVTTTLKNLGALYRRQGKFEAAETLEEAAMRSRKQGLDNVHKQRVAEVLNDPENMEKRRSRESLNVDVVKYESGPDGGEEVSMSVEWNGGVSGRASFCGKRQQQQWPGRRHR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":208,"region_id":"DP02532r001","start":185,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"It should be noted that the 24 N-terminal residues (185–208) from KLC1-TPR[A1-B5], as well as the 21-residue stretch containing the His-tag and the thrombine cleavage site, were not modeled due to electron density absence.","type":"Methods"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29036226","version":2,"reference_html":"Structural plasticity of the N-terminal capping helix of the TPR domain of kinesin light chain. <i> Nguyen TQ, Chenon M, Vilela F, Velours C, Aumont-Nicaise M, Andreani J, Varela PF, Llinas P, Ménétrey J. </i> PLoS One, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5OJ8"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-26T15:50:43.214Z"}}],"released":"2023_12","length":573,"ncbi_taxon_id":9606,"date":"2020-01-30T11:09:26.646Z","organism":"Homo sapiens","features":{"gene3D":[{"start":191,"end":497,"id":"G3DSA:1.25.40.10","name":"G3DSA:1.25.40.10"}],"pfam":[{"id":"PF13374","name":"Tetratricopeptide repeat","start":380,"end":417},{"id":"PF13374","name":"Tetratricopeptide repeat","start":465,"end":498},{"id":"PF13424","name":"Tetratricopeptide repeat","start":213,"end":287},{"id":"PF13424","name":"Tetratricopeptide repeat","start":296,"end":370}]},"disprot_id":"DP02532","regions_counter":1,"dataset":[],"UniParc":"UPI000012DECC","uniref100":"UniRef100_Q07866","uniref90":"UniRef90_Q07866","uniref50":"UniRef50_Q07866","genes":[{"name":{"value":"KLC1"},"synonyms":[{"value":"KLC"},{"value":"KNS2"}]}],"alphafold_very_low_content":0.2705061082024433,"disorder_content":0.041884816753926704,"disprot_consensus":{"full":[{"start":185,"end":208,"type":"D"}],"Structural state":[{"start":185,"end":208,"type":"D"}]}},{"acc":"P56696","name":"Potassium voltage-gated channel subfamily KQT member 4","sequence":"MAEAPPRRLGLGPPPGDAPRAELVALTAVQSEQGEAGGGGSPRRLGLLGSPLPPGAPLPGPGSGSGSACGQRSSAAHKRYRRLQNWVYNVLERPRGWAFVYHVFIFLLVFSCLVLSVLSTIQEHQELANECLLILEFVMIVVFGLEYIVRVWSAGCCCRYRGWQGRFRFARKPFCVIDFIVFVASVAVIAAGTQGNIFATSALRSMRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELITAWYIGFLVLIFASFLVYLAEKDANSDFSSYADSLWWGTITLTTIGYGDKTPHTWLGRVLAAGFALLGISFFALPAGILGSGFALKVQEQHRQKHFEKRRMPAANLIQAAWRLYSTDMSRAYLTATWYYYDSILPSFRELALLFEHVQRARNGGLRPLEVRRAPVPDGAPSRYPPVATCHRPGSTSFCPGESSRMGIKDRIRMGSSQRRTGPSKQHLAPPTMPTSPSSEQVGEATSPTKVQKSWSFNDRTRFRASLRLKPRTSAEDAPSEEVAEEKSYQCELTVDDIMPAVKTVIRSIRILKFLVAKRKFKETLRPYDVKDVIEQYSAGHLDMLGRIKSLQTRVDQIVGRGPGDRKAREKGDKGPSDAEVVDEISMMGRVVKVEKQVQSIEHKLDLLLGFYSRCLRSGTSASLGAVQVPLFDPDITSDYHSPVDHEDISVSAQTLSISRSVSTNMD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":593,"region_id":"DP02533r001","start":550,"term_id":"IDPO:0000002","statement":[{"text":"Residues 524-549 of Kv7.4 and all of CaM except for a few residues at the N-terminus and in the loop interdomain linker (residues 78-82) were resolved. ","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23178170","version":2,"reference_html":"Structure of a Ca(2+)/CaM:Kv7.4 (KCNQ4) B-helix complex provides insight into M current modulation. <i> Xu Q, Chang A, Tolia A, Minor DL. </i> J Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4GOW"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":695,"ncbi_taxon_id":9606,"date":"2020-01-31T08:35:22.064Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF00520","name":"Ion transport protein","start":99,"end":328},{"id":"PF03520","name":"KCNQ voltage-gated potassium channel","start":464,"end":646}]},"disprot_id":"DP02533","regions_counter":1,"dataset":[],"UniParc":"UPI000013D35B","uniref100":"UniRef100_P56696","uniref90":"UniRef90_P56696","uniref50":"UniRef50_P56696","genes":[{"name":{"value":"KCNQ4"}}],"alphafold_very_low_content":0.3856115107913669,"disorder_content":0.06330935251798561,"disprot_consensus":{"full":[{"start":550,"end":593,"type":"D"}],"Structural state":[{"start":550,"end":593,"type":"D"}]}},{"acc":"O70201","name":"Baculoviral IAP repeat-containing protein 5","sequence":"MGAPALPQIWQLYLKNYRIATFKNWPFLEDCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDNPIEEHRKHSPGCAFLTVKKQMEELTVSEFLKLDRQRAKNKIAKETNNKQKEFEETAKTTRQSIEQLAA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":140,"region_id":"DP02534r001","start":123,"term_id":"IDPO:0000002","statement":[{"text":"This helix terminates at residue Lys-120 with residue Asn-122, the last observed in the electron density. The last eighteen residues are not observed in the crystal structure, but these can be accommodated in the solvent continuum.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10949038","version":2,"reference_html":"Crystal structure and mutagenic analysis of the inhibitor-of-apoptosis protein survivin. <i> Muchmore SW, Chen J, Jakob C, Zakula D, Matayoshi ED, Wu W, Zhang H, Li F, Ng SC, Altieri DC. </i> Mol Cell, 2000","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1M4M"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":140,"ncbi_taxon_id":10090,"date":"2020-01-31T09:04:12.131Z","organism":"Mus musculus","features":{"gene3D":[],"pfam":[{"id":"PF00653","name":"Inhibitor of Apoptosis domain","start":18,"end":87}]},"disprot_id":"DP02534","regions_counter":1,"dataset":[],"UniParc":"UPI0000000987","uniref100":"UniRef100_O70201","uniref90":"UniRef90_O70201","uniref50":"UniRef50_O15392-2","genes":[{"name":{"value":"Birc5"},"synonyms":[{"value":"Api4"},{"value":"Iap4"}]}],"alphafold_very_low_content":0.014285714285714285,"disorder_content":0.12857142857142856,"disprot_consensus":{"full":[{"start":123,"end":140,"type":"D"}],"Structural state":[{"start":123,"end":140,"type":"D"}]}},{"acc":"Q8R4T5","name":"General receptor for phosphoinositides 1-associated scaffold protein","sequence":"MTLRRLRKLQQKEEATAAPDLAGRAPDSEAARAAPTPSGPPAAAAPPGAPGDELYAALEDYHPAELYRALAVSGGTLPRRKGSGFRWKNFTQSPEQQRKVLTLEKGDNQTFGFEIQTYGLHHREEQRVEMVTFVCRVHESSPAQLAGLTPGDTIASVNGLNVEGIRHREIVDIIKASGNVLRLETLYGTSIRKAELEARLQYLKQTLYEKWGEYRSLMVQEQRLVHGLVVKDPSIYDTLESVRSCLYGAGLLPGSLPFGPLLAAPGGARGGSRRAKGDTDDAVYHTCFFGGAEPQALPPPPPPARAPGPGSAETPASVLCPAPRATLSRSASVRCAGPGGGGGGGAPGALWTEAREQALCGAGLRKTKYRSFRRRLLKFIPGLNRSLEEEESQL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":130,"region_id":"DP02535r001","start":120,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The blue and magenta dotted lines represent the disordered β2–β3 loops","type":"Figure"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17396155","version":2,"reference_html":"Crystal structures of autoinhibitory PDZ domain of Tamalin: implications for metabotropic glutamate receptor trafficking regulation. <i> Sugi T, Oyama T, Muto T, Nakanishi S, Morikawa K, Jingami H. </i> EMBO J, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2EGN"},{"db":"PDB","id":"2EGK"},{"db":"PDB","id":"2EGO"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":96,"reference_id":"17396155","reference_source":"pmid","reference_html":"Crystal structures of autoinhibitory PDZ domain of Tamalin: implications for metabotropic glutamate receptor trafficking regulation. <i> Sugi T, Oyama T, Muto T, Nakanishi S, Morikawa K, Jingami H. </i> EMBO J, 2007","date":"2022-09-26T19:51:55.673Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02535r002","statement":[{"text":"However, crystallization of the N-terminal region, Tamalin1–189, was unsuccessful. Thus, we performed limited proteolysis to analyze its domain architecture, and expressed the PDZ domain for biochemical characterization.","type":"Results"}]},{"start":1,"end":96,"reference_id":"17396155","reference_source":"pmid","reference_html":"Crystal structures of autoinhibitory PDZ domain of Tamalin: implications for metabotropic glutamate receptor trafficking regulation. <i> Sugi T, Oyama T, Muto T, Nakanishi S, Morikawa K, Jingami H. </i> EMBO J, 2007","date":"2022-09-26T19:53:08.685Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02535r003","statement":[{"text":"To detect intrinsic ligand binding, we expressed high levels of the Tamalin mutant, which lacks the unstructured AR region as shown by circular dichroism spectra (Supplementary Figure 1), and its derivatives.","type":"Results"},{"text":"The difference spectrum (grey)\nbetween Tamalin1-189 (red) and the PDZ domain (blue) is derived from the unstructured AR region. ","type":"Supplementary material"}]}],"released":"2023_12","length":394,"ncbi_taxon_id":10116,"date":"2020-01-31T09:34:03.644Z","organism":"Rattus norvegicus","features":{"gene3D":[{"start":90,"end":190,"id":"G3DSA:2.30.42.10","name":"G3DSA:2.30.42.10"}],"pfam":[{"id":"PF00595","name":"PDZ domain","start":101,"end":184}]},"disprot_id":"DP02535","regions_counter":3,"dataset":[],"UniParc":"UPI00000E753A","uniref100":"UniRef100_Q8R4T5","uniref90":"UniRef90_Q8R4T5","uniref50":"UniRef50_Q8R4T5","genes":[{"name":{"value":"Tamalin","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11850456","url":"http://www.ncbi.nlm.nih.gov/pubmed/11850456","alternativeUrl":"https://europepmc.org/abstract/MED/11850456"}}]},"synonyms":[{"value":"Grasp"}]}],"alphafold_very_low_content":0.43147208121827413,"disorder_content":0.2715736040609137,"disprot_consensus":{"full":[{"start":1,"end":96,"type":"D"},{"start":120,"end":130,"type":"D"}],"Structural state":[{"start":1,"end":96,"type":"D"},{"start":120,"end":130,"type":"D"}]}},{"acc":"P15825","name":"50S ribosomal protein L10","sequence":"MSAESERKTETIPEWKQEEVDAIVEMIESYESVGVVNIAGIPSRQLQDMRRDLHGTAELRVSRNTLLERALDDVDDGLEDLNGYITGQVGLIGTDDNPFSLFQELEASKTPAPIGAGEVAPNDIVIPEGDTGVDPGPFVGELQSVGADARIQEGSIQVLSDSTVLDTGEEVSQELSNVLNELGIEPKEVGLDLRAVFADGVLFEPEELELDIDEYRSDIQAAAGRAFNLSVNADYPTATTAPTMLQSARGNAKSLALQAAIEDPEVVPDLVSKADAQVRALASQIDDEEALPEELQGVEADVATEEPTDDQDDDTASEDDADADDAAEEADDDDDDDEDAGDALGAMF","taxonomy":["Archaea","Euryarchaeota","Stenosarchaea group","Halobacteria","Halobacteriales","Haloarculaceae","Haloarcula"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":348,"region_id":"DP02536r001","reference_id":"11483524","start":74,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In the model of the H.marismortui 50S reported by Ban et al. (2000), L10 was not included because of difficulty in map interpretation in this region. As refinement progressed, map quality improved and small segments of L10 were identified and modeled. Two α‐helices corresponding to residues 12–29 and 63–73 have been included in this model.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"The kink-turn: a new RNA secondary structure motif. <i> Klein DJ, Schmeing TM, Moore PB, Steitz TA. </i> EMBO J, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1JJ2"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":62,"region_id":"DP02536r002","reference_id":"11483524","start":30,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"In the model of the H.marismortui 50S reported by Ban et al. (2000), L10 was not included because of difficulty in map interpretation in this region. As refinement progressed, map quality improved and small segments of L10 were identified and modeled. Two α‐helices corresponding to residues 12–29 and 63–73 have been included in this model.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"The kink-turn: a new RNA secondary structure motif. <i> Klein DJ, Schmeing TM, Moore PB, Steitz TA. </i> EMBO J, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1JJ2"}],"term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","length":348,"ncbi_taxon_id":272569,"date":"2020-02-04T15:42:05.624Z","organism":"Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)","features":{"gene3D":[{"start":12,"end":212,"id":"G3DSA:3.30.70.1730","name":"G3DSA:3.30.70.1730"},{"start":110,"end":189,"id":"G3DSA:3.90.105.20","name":"G3DSA:3.90.105.20"}],"pfam":[{"id":"PF00466","name":"Ribosomal protein L10","start":13,"end":107},{"id":"PF17777","name":"Insertion domain in 60S ribosomal protein L10P","start":116,"end":184}]},"disprot_id":"DP02536","regions_counter":2,"dataset":[],"UniParc":"UPI00001120D1","uniref100":"UniRef100_P15825","uniref90":"UniRef90_P15825","uniref50":"UniRef50_P15825","genes":[{"name":{"value":"rpl10","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00280","url":"https://hamap.expasy.org/unirule/MF_00280"}}]},"synonyms":[{"value":"rpl10e"},{"value":"rplP0","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00280","url":"https://hamap.expasy.org/unirule/MF_00280"}}]}],"olnNames":[{"value":"rrnAC1417"}]}],"alphafold_very_low_content":0.15517241379310345,"disorder_content":0.8850574712643678,"disprot_consensus":{"full":[{"start":30,"end":62,"type":"D"},{"start":74,"end":348,"type":"D"}],"Structural state":[{"start":30,"end":62,"type":"D"},{"start":74,"end":348,"type":"D"}]}},{"acc":"P30130","name":"Outer membrane usher protein FimD","sequence":"MSYLNLRLYQRNTQCLHIRKHRLAGFFVRLVVACAFAAQAPLSSADLYFNPRFLADDPQAVADLSRFENGQELPPGTYRVDIYLNNGYMATRDVTFNTGDSEQGIVPCLTRAQLASMGLNTASVAGMNLLADDACVPLTTMVQDATAHLDVGQQRLNLTIPQAFMSNRARGYIPPELWDPGINAGLLNYNFSGNSVQNRIGGNSHYAYLNLQSGLNIGAWRLRDNTTWSYNSSDRSSGSKNKWQHINTWLERDIIPLRSRLTLGDGYTQGDIFDGINFRGAQLASDDNMLPDSQRGFAPVIHGIARGTAQVTIKQNGYDIYNSTVPPGPFTINDIYAAGNSGDLQVTIKEADGSTQIFTVPYSSVPLLQREGHTRYSITAGEYRSGNAQQEKTRFFQSTLLHGLPAGWTIYGGTQLADRYRAFNFGIGKNMGALGALSVDMTQANSTLPDDSQHDGQSVRFLYNKSLNESGTNIQLVGYRYSTSGYFNFADTTYSRMNGYNIETQDGVIQVKPKFTDYYNLAYNKRGKLQLTVTQQLGRTSTLYLSGSHQTYWGTSNVDEQFQAGLNTAFEDINWTLSYSLTKNAWQKGRDQMLALNVNIPFSHWLRSDSKSQWRHASASYSMSHDLNGRMTNLAGVYGTLLEDNNLSYSVQTGYAGGGDGNSGSTGYATLNYRGGYGNANIGYSHSDDIKQLYYGVSGGVLAHANGVTLGQPLNDTVVLVKAPGAKDAKVENQTGVRTDWRGYAVLPYATEYRENRVALDTNTLADNVDLDNAVANVVPTRGAIVRAEFKARVGIKLLMTLTHNNKPLPFGAMVTSESSQSSGIVADNGQVYLSGMPLAGKVQVKWGEEENAHCVANYQLPPESQQQLLTQLSAECR","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"creator":"rpancsa","regions":[{"region_id":"DP02537r003","unpublished":true,"ec_ontology":"ECO","end":69,"term_id":"GO:0005515","start":46,"version":4,"statement":[{"text":"In this structure, FimF has already polymerized with FimG, and the N-terminal domain of FimD swings over to bind CTD2; the N-terminal domain maintains contact with FimC-FimF, while at the same time permitting access to the C-terminal domains.","type":"Abstract"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P31697","partner_end":null}],"term_name":"protein binding","ec_name":"cryogenic electron microscopy evidence used in manual assertion","released":"2023_12","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"30283140","date":"2022-09-26T20:29:46.735Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6E15"}],"term_namespace":"Molecular function","ec_id":"ECO:0006208","curator_id":"vnugnes","reference_html":"Handover mechanism of the growing pilus by the bacterial outer-membrane usher FimD. <i> Du M, Yuan Z, Yu H, Henderson N, Sarowar S, Zhao G, Werneburg GT, Thanassi DG, Li H. </i> Nature, 2018","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08191"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08190"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08189"}]},{"start":1,"end":46,"reference_id":"30283140","reference_source":"pmid","reference_html":"Handover mechanism of the growing pilus by the bacterial outer-membrane usher FimD. <i> Du M, Yuan Z, Yu H, Henderson N, Sarowar S, Zhao G, Werneburg GT, Thanassi DG, Li H. </i> Nature, 2018","date":"2022-09-26T20:24:40.788Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02537r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08191"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08189"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08190"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P31697"}],"statement":[{"text":"In this conformation, the FimD N-tail is not visible, likely due to flexibility, which is in agreement with previous structures of the disengaged NTD 13,14,20.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"6E14"},{"db":"EMDB","id":"8953"}]},{"start":499,"end":518,"reference_id":"30283140","reference_source":"pmid","reference_html":"Handover mechanism of the growing pilus by the bacterial outer-membrane usher FimD. <i> Du M, Yuan Z, Yu H, Henderson N, Sarowar S, Zhao G, Werneburg GT, Thanassi DG, Li H. </i> Nature, 2018","date":"2022-09-26T20:24:23.400Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02537r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08191"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08189"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08190"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P31697"}],"statement":[{"text":"The electron microscopy evidence in the PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"6E14"},{"db":"EMDB","id":"8953"}]}],"released":"2023_12","length":878,"ncbi_taxon_id":83333,"date":"2020-02-04T16:43:47.985Z","organism":"Escherichia coli (strain K12)","features":{"gene3D":[{"start":46,"end":170,"id":"G3DSA:3.10.20.410","name":"G3DSA:3.10.20.410"},{"start":705,"end":795,"id":"G3DSA:2.60.40.2610","name":"G3DSA:2.60.40.2610"},{"start":796,"end":878,"id":"G3DSA:2.60.40.2070","name":"G3DSA:2.60.40.2070"}],"pfam":[{"id":"PF00577","name":"Outer membrane usher protein","start":208,"end":790},{"id":"PF13953","name":"PapC C-terminal domain","start":799,"end":863},{"id":"PF13954","name":"PapC N-terminal domain","start":48,"end":192}]},"disprot_id":"DP02537","regions_counter":6,"dataset":[],"UniParc":"UPI000016F14E","uniref100":"UniRef100_P30130","uniref90":"UniRef90_P30130","uniref50":"UniRef50_P30130","genes":[{"name":{"value":"fimD"},"olnNames":[{"value":"b4317"},{"value":"JW5780"}]}],"alphafold_very_low_content":0.05011389521640091,"disorder_content":0.07517084282460136,"disprot_consensus":{"full":[{"start":1,"end":46,"type":"D"},{"start":47,"end":69,"type":"F"},{"start":499,"end":518,"type":"D"}],"Structural state":[{"start":1,"end":46,"type":"D"},{"start":499,"end":518,"type":"D"}],"Molecular function":[{"start":46,"end":69,"type":"F"}]}},{"acc":"Q16790","name":"Carbonic anhydrase 9","sequence":"MAPLCPSPWLPLLIPAPAPGLTVQLLLSLLLLVPVHPQRLPRMQEDSPLGGGSSGEDDPLGEEDLPSEEDSPREEDPPGEEDLPGEEDLPGEEDLPEVKPKSEEEGSLKLEDLPTVEAPGDPQEPQNNAHRDKEGDDQSHWRYGGDPPWPRVSPACAGRFQSPVDIRPQLAAFCPALRPLELLGFQLPPLPELRLRNNGHSVQLTLPPGLEMALGPGREYRALQLHLHWGAAGRPGSEHTVEGHRFPAEIHVVHLSTAFARVDEALGRPGGLAVLAAFLEEGPEENSAYEQLLSRLEEIAEEGSETQVPGLDISALLPSDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDTLWGPGDSRLQLNFRATQPLNGRVIEASFPAGVDSSPRAAEPVQLNSCLAAGDILALVFGLLFAVTSVAFLVQMRRQHRRGTKGGVSYRPAEVAETGA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"grivas","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":136,"region_id":"DP02538r001","start":38,"term_id":"IDPO:0000002","statement":[{"text":"in size exclusion chromatography (SEC), PG(38–136) eluted with an anomalous retention\nvolume (10.68 ml), corresponding to an apparent molecular\nmass of 50 kDa much greater than the expected one","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"chromatography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"29564477","version":2,"reference_html":"Biochemical, biophysical and molecular dynamics studies on the proteoglycan-like domain of carbonic anhydrase IX. <i> Langella E, Buonanno M, Vullo D, Dathan N, Leone M, Supuran CT, De Simone G, Monti SM. </i> Cell Mol Life Sci, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:05:14.286Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":136,"region_id":"DP02538r002","start":38,"term_id":"IDPO:0000002","statement":[{"text":"the high number of acidic Glu and Asp residues in the primary sequence caused a scarce denaturation of the protein in SDS [25, 62], which resulted in an aberrant migration on SDS-PAGE, leading to an apparent molecular mass between 15 and 20 kDa instead of the expected 10.8 kDa","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"29564477","version":2,"reference_html":"Biochemical, biophysical and molecular dynamics studies on the proteoglycan-like domain of carbonic anhydrase IX. <i> Langella E, Buonanno M, Vullo D, Dathan N, Leone M, Supuran CT, De Simone G, Monti SM. </i> Cell Mol Life Sci, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007689","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:05:13.149Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":136,"region_id":"DP02538r003","start":38,"term_id":"IDPO:0000002","statement":[{"text":"By DLS analysis, a monodisperse peak (17% of\npolydispersity) was evident, indicative of a species homogeneous in size distribution with a rather large apparent hydrodynamic radius (4.1 nm ± 0.7). ","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"dynamic light scattering assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"29564477","version":2,"reference_html":"Biochemical, biophysical and molecular dynamics studies on the proteoglycan-like domain of carbonic anhydrase IX. <i> Langella E, Buonanno M, Vullo D, Dathan N, Leone M, Supuran CT, De Simone G, Monti SM. </i> Cell Mol Life Sci, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007064","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:05:12.248Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":136,"region_id":"DP02538r004","start":38,"term_id":"IDPO:0000002","statement":[{"text":"In agreement with the hypothesis that PG(38–136) is an IDP, collected spectrum showed a strong negative molar ellipticity value at 198 nm and a negative band between 210 and 230 nm (Fig.  3a), indicative of a protein in a largely disordered conformation.","type":"Results"},{"text":"In conclusion, collected far-UV-CD data give strong evidence that PG (38–136) is an IDP possessing some residues in PPII conformation.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"29564477","version":2,"reference_html":"Biochemical, biophysical and molecular dynamics studies on the proteoglycan-like domain of carbonic anhydrase IX. <i> Langella E, Buonanno M, Vullo D, Dathan N, Leone M, Supuran CT, De Simone G, Monti SM. </i> Cell Mol Life Sci, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:05:11.010Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":136,"region_id":"DP02538r005","start":38,"term_id":"GO:0140677","statement":[{"text":"In the same paper, our finding proved that the PG domain was able to assist the catalysis mediated by the CA domain. ","type":"Results"},{"text":"CA domain was titrated with diferent concentrations of PG (38–136) and the catalytic activity was evaluated. In agreement with the previous results, it was observed that 10 µM PG(38–136) was able to increase the CA catalytic activity of about 63%.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"enzymatic activity assay evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"29564477","version":3,"reference_html":"Biochemical, biophysical and molecular dynamics studies on the proteoglycan-like domain of carbonic anhydrase IX. <i> Langella E, Buonanno M, Vullo D, Dathan N, Leone M, Supuran CT, De Simone G, Monti SM. </i> Cell Mol Life Sci, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005801","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:05:09.351Z","curator_name":"Federica Quaglia"},"term_name":"molecular function activator activity","curator_orcid":"0000-0003-0849-9312","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":136,"region_id":"DP02538r006","start":38,"term_id":"IDPO:0000002","statement":[{"text":"The 1D [1H] NMR spectrum (Fig. S3a) together with the 2D [1H, 1H] TOCSY (Total Correlation Spectroscopy) [32] and 2D [1H, 1H] NOESY (Nuclear Overhauser\nEnhancement Spectroscopy) [33] experiments (Fig. S3b) appear typical of IDPs. In particular, the 1D [1H] (Fig. S3a) and 2D [1H, 1H] TOCSY (Fig. S3b left panel) spectra present low chemical shift dispersion with the backbone amide HN protons resonating in the narrow random coil range between 8 and 8.6 ppm.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"29564477","version":2,"reference_html":"Biochemical, biophysical and molecular dynamics studies on the proteoglycan-like domain of carbonic anhydrase IX. <i> Langella E, Buonanno M, Vullo D, Dathan N, Leone M, Supuran CT, De Simone G, Monti SM. </i> Cell Mol Life Sci, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:05:10.396Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":136,"region_id":"DP02538r007","start":38,"term_id":"IDPO:0000002","statement":[{"text":"The incubation of PG(38–136) with trypsin protease at diferent ratios showed a complete cleavage in the early hours of the reaction.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"29564477","version":2,"reference_html":"Biochemical, biophysical and molecular dynamics studies on the proteoglycan-like domain of carbonic anhydrase IX. <i> Langella E, Buonanno M, Vullo D, Dathan N, Leone M, Supuran CT, De Simone G, Monti SM. </i> Cell Mol Life Sci, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:05:09.762Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2021_06","length":459,"ncbi_taxon_id":9606,"date":"2020-02-05T10:22:16.837Z","organism":"Homo sapiens","features":{"gene3D":[{"start":140,"end":399,"id":"G3DSA:3.10.200.10","name":"Alpha carbonic anhydrase"}],"pfam":[{"id":"PF00194","name":"Eukaryotic-type carbonic anhydrase","start":148,"end":390}]},"disprot_id":"DP02538","regions_counter":15,"dataset":[],"UniParc":"UPI0000047736","uniref100":"UniRef100_Q16790","uniref90":"UniRef90_Q16790","uniref50":"UniRef50_Q16790","genes":[{"name":{"value":"CA9"},"synonyms":[{"value":"G250"},{"value":"MN"}]}],"alphafold_very_low_content":0.3028322440087146,"disorder_content":0.21568627450980393,"disprot_consensus":{"full":[{"start":38,"end":136,"type":"D"}],"Structural state":[{"start":38,"end":136,"type":"D"}],"Molecular function":[{"start":38,"end":136,"type":"F"}]}},{"acc":"Q16611","name":"Bcl-2 homologous antagonist/killer","sequence":"MASGQGPGPPRQECGEPALPSASEEQVAQDTEEVFRSYVFYRHQQEQEAEGVAAPADPEMVTLPLQPSSTMGQVGRQLAIIGDDINRRYDSEFQTMLQHLQPTAENAYEYFTKIATSLFESGINWGRVVALLGFGYRLALHVYQHGLTGFLGQVTRFVVDFMLHHCIARWIAQRGGWVAALNLGNGPILNVLVVLGVVLLGQFVVRRFFKS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":98,"region_id":"DP02539r001","start":64,"term_id":"IDPO:0000002","statement":[{"text":"Circular dichroism (CD) spectra reveal that the BH3 peptides investigated are mainly\ndisordered under our experimental conditions. However, the percentage helicities of the\nBH3 peptides calculated from MRE value at 222 nm19, ranges between approximately 9-\n63%.","type":"Results"},{"text":"These BCL-2 family proteins have a homologous BH3 domain, which is intrinsically disordered in isolation, but form a contiguous helical segment upon binding to its partner BCL-2 proteins","type":"Introduction"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"29654795","version":2,"reference_html":"Promiscuous and Selective: How Intrinsically Disordered BH3 Proteins Interact with Their Pro-survival Partner MCL-1. <i> Dahal L, Kwan TOC, Hollins JJ, Clarke J. </i> J Mol Biol, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":84,"region_id":"DP02539r002","start":75,"term_id":"IDPO:0000011","statement":[{"text":"the Bak peptide adopts an amphipathic alpha helix that interacts with Bcl-xL through hydrophobic and electrostatic interactions","type":"Abstract"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"9020082","version":2,"reference_html":"Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis. <i> Sattler M, Liang H, Nettesheim D, Meadows RP, Harlan JE, Eberstadt M, Yoon HS, Shuker SB, Chang BS, Minn AJ, Thompson CB, Fesik SW. </i> Science, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"1BXL"}],"term_name":"disorder to order","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q07820","partner_end":null}],"ec_ontology":"ECO","end":98,"region_id":"DP02539r003","start":64,"term_id":"GO:0005515","statement":[{"text":"As expected, the effector, pro-apoptotic peptides BAK and BAX bind less tightly\nthan the activator proteins.","type":"Discussion"},{"text":"We show that eight different disordered BH3 proteins all bind to their BCL-2 partner (MCL-1) very rapidly, and that the differences in sequences result in different dissociation rates.","type":"Abstract"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"fluorescence evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"29654795","version":3,"reference_html":"Promiscuous and Selective: How Intrinsically Disordered BH3 Proteins Interact with Their Pro-survival Partner MCL-1. <i> Dahal L, Kwan TOC, Hollins JJ, Clarke J. </i> J Mol Biol, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001249","term_name":"protein binding","curator_orcid":"0000-0003-0849-9312","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":98,"region_id":"DP02539r004","start":64,"term_id":"GO:0098772","statement":[{"text":"As expected, the effector, pro-apoptotic peptides BAK and BAX bind less tightly\nthan the activator proteins.","type":"Discussion"},{"text":"We show that eight different disordered BH3 proteins all bind to their BCL-2 partner (MCL-1) very rapidly, and that the differences in sequences result in different dissociation rates.","type":"Abstract"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"fluorescence evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"29654795","version":3,"reference_html":"Promiscuous and Selective: How Intrinsically Disordered BH3 Proteins Interact with Their Pro-survival Partner MCL-1. <i> Dahal L, Kwan TOC, Hollins JJ, Clarke J. </i> J Mol Biol, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001249","term_name":"molecular function regulator","curator_orcid":"0000-0003-0849-9312","ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":86,"region_id":"DP02539r005","start":69,"term_id":"IDPO:0000011","statement":[{"text":"The BAK segment forms an alpha-helix on the surface of Bcl-xL.","type":"Curator statement"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"27198225","version":2,"reference_html":"Physiological restraint of Bak by Bcl-xL is essential for cell survival. <i> Lee EF, Grabow S, Chappaz S, Dewson G, Hockings C, Kluck RM, Debrincat MA, Gray DH, Witkowski MT, Evangelista M, Pettikiriarachchi A, Bouillet P, Lane RM, Czabotar PE, Colman PM, Smith BJ, Kile BT, Fairlie WD. </i> Genes Dev, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"5FMK"}],"term_name":"disorder to order","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP02539r006","ec_ontology":"ECO","end":86,"term_id":"GO:0005515","start":69,"version":3,"statement":[{"text":"The BAK segment forms an alpha-helix on the surface of Bcl-xL.","type":"Curator statement"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q07817","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"27198225","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5FMK"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"rpancsa","reference_html":"Physiological restraint of Bak by Bcl-xL is essential for cell survival. <i> Lee EF, Grabow S, Chappaz S, Dewson G, Hockings C, Kluck RM, Debrincat MA, Gray DH, Witkowski MT, Evangelista M, Pettikiriarachchi A, Bouillet P, Lane RM, Czabotar PE, Colman PM, Smith BJ, Kile BT, Fairlie WD. </i> Genes Dev, 2016","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","length":211,"ncbi_taxon_id":9606,"date":"2020-02-05T10:53:37.806Z","organism":"Homo sapiens","features":{"gene3D":[{"start":5,"end":193,"id":"G3DSA:1.10.437.10","name":"Blc2-like"}],"pfam":[{"id":"PF00452","name":"Apoptosis regulator proteins, Bcl-2 family","start":78,"end":177}]},"disprot_id":"DP02539","regions_counter":6,"dataset":["Autophagy-related proteins"],"UniParc":"UPI0000126777","uniref100":"UniRef100_Q16611","uniref90":"UniRef90_Q16611","uniref50":"UniRef50_Q16611","genes":[{"name":{"value":"BAK1"},"synonyms":[{"value":"BAK"},{"value":"BCL2L7"},{"value":"CDN1"}]}],"alphafold_very_low_content":0.018957345971563982,"disorder_content":0.16587677725118483,"disprot_consensus":{"full":[{"start":64,"end":68,"type":"D"},{"start":69,"end":86,"type":"T"},{"start":87,"end":98,"type":"D"}],"Structural state":[{"start":64,"end":98,"type":"D"}],"Structural transition":[{"start":69,"end":86,"type":"T"}],"Molecular function":[{"start":64,"end":98,"type":"F"}]}},{"acc":"Q07812","name":"Apoptosis regulator BAX","sequence":"MDGSGEQPRGGGPTSSEQIMKTGALLLQGFIQDRAGRMGGEAPELALDPVPQDASTKKLSECLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNWGRVVALFYFASKLVLKALCTKVPELIRTIMGWTLDFLRERLLGWIQDQGGWDGLLSYFGTPTWQTVTIFVAGVLTASLTIWKKMG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":83,"region_id":"DP02540r001","start":49,"term_id":"IDPO:0000002","statement":[{"text":"Circular dichroism (CD) spectra reveal that the BH3 peptides investigated are mainly\ndisordered under our experimental conditions. However, the percentage helicities of the\nBH3 peptides calculated from MRE value at 222 nm19, ranges between approximately 9-\n63%","type":"Results"},{"text":"These BCL-2 family proteins have a homologous BH3 domain, which is intrinsically disordered in isolation, but form a contiguous helical segment upon binding to its partner BCL-2 proteins","type":"Introduction"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"29654795","version":2,"reference_html":"Promiscuous and Selective: How Intrinsically Disordered BH3 Proteins Interact with Their Pro-survival Partner MCL-1. <i> Dahal L, Kwan TOC, Hollins JJ, Clarke J. </i> J Mol Biol, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"disorder","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-04-07T13:50:58.081Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q07820","partner_end":null}],"ec_ontology":"ECO","end":83,"region_id":"DP02540r002","start":49,"term_id":"GO:0005515","statement":[{"text":"As expected, the effector, pro-apoptotic peptides BAK and BAX bind less tightly\nthan the activator proteins.","type":"Discussion"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"fluorescence evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"29654795","version":3,"reference_html":"Promiscuous and Selective: How Intrinsically Disordered BH3 Proteins Interact with Their Pro-survival Partner MCL-1. <i> Dahal L, Kwan TOC, Hollins JJ, Clarke J. </i> J Mol Biol, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001249","term_name":"protein binding","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-04-07T13:51:05.153Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":83,"region_id":"DP02540r003","start":49,"term_id":"GO:0098772","statement":[{"text":"As expected, the effector, pro-apoptotic peptides BAK and BAX bind less tightly\nthan the activator proteins.","type":"Discussion"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"fluorescence evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"29654795","version":3,"reference_html":"Promiscuous and Selective: How Intrinsically Disordered BH3 Proteins Interact with Their Pro-survival Partner MCL-1. <i> Dahal L, Kwan TOC, Hollins JJ, Clarke J. </i> J Mol Biol, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001249","term_name":"molecular function regulator","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-04-07T13:51:11.504Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":79,"region_id":"DP02540r004","start":55,"term_id":"IDPO:0000011","statement":[{"text":"Here, we describe crystal structures of the pro-survival proteins Mcl-1 and Bcl-x(L) in complex with a 34-mer peptide from Bax that encompasses its BH3 domain. These structures reveal canonical interactions between four signature hydrophobic amino acids from the BaxBH3 domain and the BH3-binding groove of the pro-survival proteins.","type":"Abstract"},{"text":"The boundaries of the helical segment were derived from the PDB file.","type":"Curator statement"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"21199865","version":2,"reference_html":"Mutation to Bax beyond the BH3 domain disrupts interactions with pro-survival proteins and promotes apoptosis. <i> Czabotar PE, Lee EF, Thompson GV, Wardak AZ, Fairlie WD, Colman PM. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"3PK1"}],"term_name":"disorder to order","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-04-07T13:51:03.373Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2021_06","length":192,"ncbi_taxon_id":9606,"date":"2020-02-05T12:10:27.243Z","organism":"Homo sapiens","features":{"gene3D":[{"start":1,"end":191,"id":"G3DSA:1.10.437.10","name":"Blc2-like"}],"pfam":[{"id":"PF00452","name":"Apoptosis regulator proteins, Bcl-2 family","start":63,"end":158}]},"disprot_id":"DP02540","regions_counter":4,"dataset":["Autophagy-related proteins","Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI0000035C7E","uniref100":"UniRef100_Q07812","uniref90":"UniRef90_Q07812","uniref50":"UniRef50_Q07812","genes":[{"name":{"value":"BAX"},"synonyms":[{"value":"BCL2L4"}]}],"alphafold_very_low_content":0.052083333333333336,"disorder_content":0.18229166666666666,"disprot_consensus":{"full":[{"start":49,"end":54,"type":"D"},{"start":55,"end":79,"type":"T"},{"start":80,"end":83,"type":"D"}],"Structural state":[{"start":49,"end":83,"type":"D"}],"Molecular function":[{"start":49,"end":83,"type":"F"}],"Structural transition":[{"start":55,"end":79,"type":"T"}]}},{"acc":"P0ACN7","name":"HTH-type transcriptional repressor CytR","sequence":"MKAKKQETAATMKDVALKAKVSTATVSRALMNPDKVSQATRNRVEKAAREVGYLPQPMGRNVKRNESRTILVIVPDICDPFFSEIIRGIEVTAANHGYLVLIGDCAHQNQQEKTFIDLIITKQIDGMLLLGSRLPFDASIEEQRNLPPMVMANEFAPELELPTVHIDNLTAAFDAVNYLYEQGHKRIGCIAGPEEMPLCHYRLQGYVQALRRCGIMVDPQYIARGDFTFEAGSKAMQQLLDLPQPPTAVFCHSDVMALGALSQAKRQGLKVPEDLSIIGFDNIDLTQFCDPPLTTIAQPRYEIGREAMLLLLDQMQGQHVGSGSRLMDCELIIRGSTRALP","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":67,"region_id":"DP02541r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"We used nuclear magnetic resonance (NMR) spectroscopy to characterize the CytR DBD free in solution and to determine the high-resolution structure of a CytR DBD monomer bound specifically to one DNA half-site of the uridine phosphorylase (udp) operator. We find that the free DBD populates multiple distinct conformations distinguished by up to four sets of NMR peaks per residue.","type":"Abstract"},{"text":"We began our studies of the DBD free state and first assessed the structure and stability of the protein by collecting 15N HSQC NMR spectra over a range of temperatures. As the temperature is increased, the dispersion of the peaks is reduced, indicating that the protein unfolds until only one set of random coil-like signals is obtained at 35 °C","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"21688840","version":2,"reference_html":"Multiple conformations of the cytidine repressor DNA-binding domain coalesce to one upon recognition of a specific DNA surface. <i> Moody CL, Tretyachenko-Ladokhina V, Laue TM, Senear DF, Cocco MJ. </i> Biochemistry, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"2LCV"}],"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:57:51.326Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":55,"region_id":"DP02541r002","start":9,"term_id":"IDPO:0000011","statement":[{"text":"These stable structures coalesce into a single, more stable udp-bound form that features a three-helix bundle containing a canonical helix-turn-helix motif.","type":"Abstract"},{"text":"In the presence of the udp half-site DNA, we find a single set of well-dispersed DBD peaks in the NMR spectrum. This peak pattern exists at 20 °C and remains above 35 °C (Figure 1B). The structural consequences of DNA binding are reversible for DNA substrates; removal of DNA results in the return of the original DBD HSQC spectrum that reflects multiple protein conformations.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"21688840","version":2,"reference_html":"Multiple conformations of the cytidine repressor DNA-binding domain coalesce to one upon recognition of a specific DNA surface. <i> Moody CL, Tretyachenko-Ladokhina V, Laue TM, Senear DF, Cocco MJ. </i> Biochemistry, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"2LCV"}],"term_name":"disorder to order","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:57:59.014Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":67,"region_id":"DP02541r003","start":1,"term_id":"GO:0003677","statement":[{"text":"In the presence of the udp half-site DNA, we find a single set of well-dispersed DBD peaks in the NMR spectrum. This peak pattern exists at 20 °C and remains above 35 °C (Figure 1B). The structural consequences of DNA binding are reversible for DNA substrates; removal of DNA results in the return of the original DBD HSQC spectrum that reflects multiple protein conformations.","type":"Results"},{"text":"When associated with DNA, the DBD is a three-helix bundle containing a canonical helix–turn–helix motif.","type":"Discussion"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"21688840","version":3,"reference_html":"Multiple conformations of the cytidine repressor DNA-binding domain coalesce to one upon recognition of a specific DNA surface. <i> Moody CL, Tretyachenko-Ladokhina V, Laue TM, Senear DF, Cocco MJ. </i> Biochemistry, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"2LCV"}],"term_name":"DNA binding","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:58:08.650Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":67,"region_id":"DP02541r004","start":1,"term_id":"IDPO:0000002","statement":[{"text":"The structure and stability of the free-state DBD were probed further using CD spectroscopy. The far-UV CD spectrum (Figure 2A) indicates primarily α-helix and random coil. The secondary structure composition was estimated using CDSSTR as implemented in CDPro.(22) The reconstructed spectrum that gave the best fit (Figure 2A) predicts a helical content of 22% at 20 °C, with the remainder predicted to be random coil.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"21688840","version":2,"reference_html":"Multiple conformations of the cytidine repressor DNA-binding domain coalesce to one upon recognition of a specific DNA surface. <i> Moody CL, Tretyachenko-Ladokhina V, Laue TM, Senear DF, Cocco MJ. </i> Biochemistry, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:57:49.203Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":67,"region_id":"DP02541r005","start":1,"term_id":"IDPO:0000002","statement":[{"text":"In the case of the free-state DBD, no peaks were detectable in the NMR 15N HSQC spectrum within 10 min of the transfer into D2O, revealing complete amide proton exchange.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"21688840","version":2,"reference_html":"Multiple conformations of the cytidine repressor DNA-binding domain coalesce to one upon recognition of a specific DNA surface. <i> Moody CL, Tretyachenko-Ladokhina V, Laue TM, Senear DF, Cocco MJ. </i> Biochemistry, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006196","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:57:48.224Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":55,"region_id":"DP02541r006","start":9,"term_id":"IDPO:0000011","statement":[{"text":"In the case of the free-state DBD, no peaks were detectable in the NMR 15N HSQC spectrum within 10 min of the transfer into D2O, revealing complete amide proton exchange. In contrast, with the DBD bound to the udp half-site, we find that 30 peaks are present in the NMR spectrum following resuspension in D2O (Figure 1C). These amide protons of the DBD–DNA complex exchange more slowly than those exposed to solvent, suggesting that they are involved in stable secondary structure or are buried within the protein interior or the protein–DNA interface.","type":"Results"},{"text":"The exchange-protected residues of the DNA-bound form reside in this segment of the protein.","type":"Curator statement"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"21688840","version":2,"reference_html":"Multiple conformations of the cytidine repressor DNA-binding domain coalesce to one upon recognition of a specific DNA surface. <i> Moody CL, Tretyachenko-Ladokhina V, Laue TM, Senear DF, Cocco MJ. </i> Biochemistry, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006196","term_name":"disorder to order","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:57:57.055Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":55,"region_id":"DP02541r007","start":9,"term_id":"IDPO:0000011","statement":[{"text":"The reconstructed spectrum that gave the best fit (Figure 2A) predicts a helical content of 22% at 20 °C, with the remainder predicted to be random coil. This is equivalent to only 15 residues in a helical conformation, slightly more than half the number of helical residues that we find in the bound form.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"21688840","version":2,"reference_html":"Multiple conformations of the cytidine repressor DNA-binding domain coalesce to one upon recognition of a specific DNA surface. <i> Moody CL, Tretyachenko-Ladokhina V, Laue TM, Senear DF, Cocco MJ. </i> Biochemistry, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"disorder to order","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:57:55.319Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":67,"region_id":"DP02541r008","start":1,"term_id":"GO:0003677","statement":[{"text":"We used the fluorescence anisotropy of a dye-conjugated (Alexa 532) DNA substrate to monitor the binding of the CytR DBD to DNA. Results of titration experiments (Figure 3) indicate that the CytR DBD binds the udp operator left half-site. We analyzed titration data assuming a 1:1 stoichiometry between monomeric protein and DNA.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"experimental evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"21688840","version":3,"reference_html":"Multiple conformations of the cytidine repressor DNA-binding domain coalesce to one upon recognition of a specific DNA surface. <i> Moody CL, Tretyachenko-Ladokhina V, Laue TM, Senear DF, Cocco MJ. </i> Biochemistry, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000269","term_name":"DNA binding","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:58:06.753Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":67,"region_id":"DP02541r009","start":1,"term_id":"GO:0098772","statement":[{"text":"We used the fluorescence anisotropy of a dye-conjugated (Alexa 532) DNA substrate to monitor the binding of the CytR DBD to DNA. Results of titration experiments (Figure 3) indicate that the CytR DBD binds the udp operator left half-site. We analyzed titration data assuming a 1:1 stoichiometry between monomeric protein and DNA.","type":"Results"},{"text":"The cytidine repressor (CytR) is a member of the LacR family of bacterial repressors with distinct functional features. The Escherichia coli CytR regulon comprises nine operons whose palindromic operators vary in both sequence and, most significantly, spacing between the recognition half-sites.","type":"Abstract"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"experimental evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"21688840","version":3,"reference_html":"Multiple conformations of the cytidine repressor DNA-binding domain coalesce to one upon recognition of a specific DNA surface. <i> Moody CL, Tretyachenko-Ladokhina V, Laue TM, Senear DF, Cocco MJ. </i> Biochemistry, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000269","term_name":"molecular function regulator","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:58:05.113Z"}},{"start":1,"end":66,"reference_id":"37379390","reference_source":"pmid","reference_html":"Functional regulation of an intrinsically disordered protein via a conformationally excited state. <i> Madhurima K, Nandi B, Munshi S, Naganathan AN, Sekhar A. </i> Sci Adv, 2023","date":"2023-08-11T16:29:56.031Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02541r010","statement":[{"text":"The backbone amide resonances of CytRN are dispersed over a narrow chemical shift range between 7.9 and 8.8 ppm in the 1H dimension, and backbone (1HN, 15N, 13C′, 13Cα, 13Cβ, and 1Hα) chemical shifts correlate well with random coil values (fig. S2A), confirming that CytRN is intrinsically disordered. ","type":"Results"},{"text":"Most of the resonances visible in the HSQC spectrum of CytR (Fig. 1D, black contours) overlay very well with matching resonances from CytRN (Fig. 1D, orange contours), indicating that the N-terminal DBD is unstructured in full-length CytR also.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T08:47:35.545Z"}},{"start":35,"end":45,"reference_id":"37379390","reference_source":"pmid","reference_html":"Functional regulation of an intrinsically disordered protein via a conformationally excited state. <i> Madhurima K, Nandi B, Munshi S, Naganathan AN, Sekhar A. </i> Sci Adv, 2023","date":"2023-08-11T16:29:09.301Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02541r011","statement":[{"text":"Residue-specific secondary structure propensity (SSP) (32) scores, calculated using backbone chemical shifts, indicate that native CytRN does not adopt stable secondary structure, although it has up to ~30% residual helicity in regions of the protein that form helices in the DNA-bound conformation (Fig. 1C) (33). This conclusion is consistent with residue-specific patterns in 13Cα and 13C′ secondary chemical shifts that suggest the presence of a low degree of helical content between residues M12-K18 and K35-E45 within an overall disordered ensemble (fig. S2B).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T08:47:17.610Z"}},{"start":11,"end":56,"reference_id":"37379390","reference_source":"pmid","reference_html":"Functional regulation of an intrinsically disordered protein via a conformationally excited state. <i> Madhurima K, Nandi B, Munshi S, Naganathan AN, Sekhar A. </i> Sci Adv, 2023","date":"2023-08-11T16:44:56.504Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02541r012","statement":[{"text":"In contrast, the rest of the protein from T11 to Q56 undergoes sizeable changes in chemical shift upon transitioning to the excited state with an average CSP of 0.59 ± 0.25 ppm over 44 residues, underscoring the fact that disordered native CytR acquires a globally folded structure in the excited state.The magnitude of CSPs plotted on the structure of DNA-bound CytRN (fig. S12) also illustrates that CSPs are not localized to a particular region but are instead distributed across the entire protein sequence from T11 to Q56.","type":"Results"},{"text":"Figure 2G shows the residue-specific S2 values of the excited state evaluated from 15N, 1HN, 13Cα, and 13C′ chemical shift information. S2 values are high in the interior of CytRN and range between 0.60 and 0.88, consistent with the rigidity expected from a globally folded excited state conformation. On the other hand, S2 values drop to less than 0.5 for the flexible terminal residues M1 to M12 and P57 to E66 (Fig. 2G). ","type":"Results"},{"text":"We then acquired CEST data on a sample containing 628 μM 15N-labeled CytRN and 150 μM uridine phosphorylase (udp) half-site double-stranded DNA, which is one of the operator regions specifically recognized by CytRN (33). In the presence of cognate DNA, a distinct third dip in intensity can be clearly discerned in the CEST profile of CytRN D34 at the 15N chemical shift of state B (117.2 ppm) which is the direct result of exchange between free and DNA-bound forms of CytRN (Fig. 4A).","type":"Results"}],"states_connection":[{"source":"DP02541r010","target":"DP02541r013"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T08:47:42.140Z"}},{"start":1,"end":66,"reference_id":"37379390","reference_source":"pmid","reference_html":"Functional regulation of an intrinsically disordered protein via a conformationally excited state. <i> Madhurima K, Nandi B, Munshi S, Naganathan AN, Sekhar A. </i> Sci Adv, 2023","date":"2023-08-11T16:41:10.364Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02541r013","statement":[{"text":"We then calculated the structure of the excited state of CytRN using CS-Rosetta (52, 53) incorporating 119 backbone chemical shifts and 65 15N-1H RDCs as structural restraints (Fig. 3C and Supplementary Text). A well-defined funnel is observed in the energy versus root mean square deviation (RMSD) plot, confirming that the structure calculations have converged (fig. S16).","type":"Results"},{"text":"CytRN adopts a three-helix bundle topology in the excited state, in which helix 3 (H3) docks on to the HTH motif formed by helices 1 (H1) and 2 (H2) (Fig. 3C).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T08:47:15.664Z"}},{"start":1,"end":66,"reference_id":"37379390","reference_source":"pmid","reference_html":"Functional regulation of an intrinsically disordered protein via a conformationally excited state. <i> Madhurima K, Nandi B, Munshi S, Naganathan AN, Sekhar A. </i> Sci Adv, 2023","date":"2023-08-11T16:50:48.414Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","region_id":"DP02541r014","statement":[{"text":"We then acquired CEST data on a sample containing 628 μM 15N-labeled CytRN and 150 μM uridine phosphorylase (udp) half-site double-stranded DNA, which is one of the operator regions specifically recognized by CytRN (33). In the presence of cognate DNA, a distinct third dip in intensity can be clearly discerned in the CEST profile of CytRN D34 at the 15N chemical shift of state B (117.2 ppm) which is the direct result of exchange between free and DNA-bound forms of CytRN (Fig. 4A).","type":"Results"},{"text":"In notable contrast, the exchange broadening incurred by the excited increases by as much as 14 s−1, resulting in substantially larger dispersions in the CPMG profile (Fig. 4F, yellow). CPMG data thus provide a direct validation of the CS-based model, where only the CytRN excited state but not the disordered state binds DNA.","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T08:47:46.963Z"}},{"start":2,"end":65,"reference_id":"35969476","reference_source":"pmid","reference_html":"Flexible Target Recognition of the Intrinsically Disordered DNA-Binding Domain of CytR Monitored by Single-Molecule Fluorescence Spectroscopy. <i> Mitra S, Oikawa H, Rajendran D, Kowada T, Mizukami S, Naganathan AN, Takahashi S. </i> J Phys Chem B, 2022","date":"2023-08-12T10:08:53.045Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"N-terminal"},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"C-terminal"}],"region_id":"DP02541r015","statement":[{"text":"CytR-DBD at low ionic strength conditions and pH 6.0 displays a bimodal behavior, with the major population displaying a peak FRET efficiency at E = 0.47 (implying a relatively expanded structure) and a minor population having a peak FRET efficiency at E = 0.82 (indicating a collapsed structure). This observation clearly demonstrates that the DNA-free CytR-DBD samples a heterogeneous ensemble of conformations in its native ensemble.","type":"Results"},{"text":"The major and minor populations detected in the smFRET efficiency histograms can be assigned to the mostly unfolded state and the compact folded state, respectively.","type":"Results"},{"text":"To further confirm the assignment of the two populations, we examined the effect of denaturant by adding urea (Figure 4A). As the concentration of urea increases, the relative population of the compact form decreases, with a concomitant increase in the expanded state amplitude (Figure 4B). The observation is similar to the standard unfolding transition of two-state proteins and is consistent with the interpretation that the compact and expanded conformations detected in the FRET histograms correspond to the folded-like and unfolded conformations, respectively. ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T08:47:10.866Z"}},{"start":2,"end":65,"reference_id":"35969476","reference_source":"pmid","reference_html":"Flexible Target Recognition of the Intrinsically Disordered DNA-Binding Domain of CytR Monitored by Single-Molecule Fluorescence Spectroscopy. <i> Mitra S, Oikawa H, Rajendran D, Kowada T, Mizukami S, Naganathan AN, Takahashi S. </i> J Phys Chem B, 2022","date":"2023-08-12T10:09:04.287Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"N-terminal"},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"C-terminal"}],"region_id":"DP02541r016","statement":[{"text":"CytR-DBD at low ionic strength conditions and pH 6.0 displays a bimodal behavior, with the major population displaying a peak FRET efficiency at E = 0.47 (implying a relatively expanded structure) and a minor population having a peak FRET efficiency at E = 0.82 (indicating a collapsed structure). This observation clearly demonstrates that the DNA-free CytR-DBD samples a heterogeneous ensemble of conformations in its native ensemble.","type":"Results"},{"text":"The major and minor populations detected in the smFRET efficiency histograms can be assigned to the mostly unfolded state and the compact folded state, respectively.","type":"Results"},{"text":"To further confirm the assignment of the two populations, we examined the effect of denaturant by adding urea (Figure 4A). As the concentration of urea increases, the relative population of the compact form decreases, with a concomitant increase in the expanded state amplitude (Figure 4B). The observation is similar to the standard unfolding transition of two-state proteins and is consistent with the interpretation that the compact and expanded conformations detected in the FRET histograms correspond to the folded-like and unfolded conformations, respectively. ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T08:47:06.604Z"}},{"start":2,"end":65,"reference_id":"35969476","reference_source":"pmid","reference_html":"Flexible Target Recognition of the Intrinsically Disordered DNA-Binding Domain of CytR Monitored by Single-Molecule Fluorescence Spectroscopy. <i> Mitra S, Oikawa H, Rajendran D, Kowada T, Mizukami S, Naganathan AN, Takahashi S. </i> J Phys Chem B, 2022","date":"2023-08-12T10:12:14.394Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"N-terminal"},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"C-terminal"}],"region_id":"DP02541r017","statement":[{"text":"Upon increasing the DNA concentration, the relative abundance of the folded fraction increases monotonically. ","type":"Results"},{"text":"The high FRET efficiency population of CytR-DBD increases in the presence of the varied DNA sequences, in agreement with similar results from ensemble binding isotherms.","type":"Results"},{"text":"Thus, these data provide direct and first evidence that even a random DNA sequence having no similarity with the consensus sequence can induce large structural compaction of the protein.","type":"Results"}],"states_connection":[{"source":"DP02541r010","target":"DP02541r013"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T08:47:40.512Z"}},{"start":2,"end":65,"reference_id":"35969476","reference_source":"pmid","reference_html":"Flexible Target Recognition of the Intrinsically Disordered DNA-Binding Domain of CytR Monitored by Single-Molecule Fluorescence Spectroscopy. <i> Mitra S, Oikawa H, Rajendran D, Kowada T, Mizukami S, Naganathan AN, Takahashi S. </i> J Phys Chem B, 2022","date":"2023-08-12T10:12:41.695Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"N-terminal"},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"C-terminal"}],"ec_go":"IPI","region_id":"DP02541r018","statement":[{"text":"Upon increasing the DNA concentration, the relative abundance of the folded fraction increases monotonically. ","type":"Results"},{"text":"The high FRET efficiency population of CytR-DBD increases in the presence of the varied DNA sequences, in agreement with similar results from ensemble binding isotherms.","type":"Results"},{"text":"Thus, these data provide direct and first evidence that even a random DNA sequence having no similarity with the consensus sequence can induce large structural compaction of the protein.","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T08:47:45.403Z"}}],"released":"2021_06","length":341,"ncbi_taxon_id":83333,"date":"2020-02-05T12:53:35.611Z","organism":"Escherichia coli (strain K12)","features":{"gene3D":[{"start":1,"end":67,"id":"G3DSA:1.10.260.40","name":"lambda repressor-like DNA-binding domains"}],"pfam":[{"id":"PF00356","name":"Bacterial regulatory proteins, lacI family","start":11,"end":56},{"id":"PF13377","name":"Periplasmic binding protein-like domain","start":176,"end":337}]},"disprot_id":"DP02541","regions_counter":18,"dataset":[],"UniParc":"UPI0000128D72","uniref100":"UniRef100_P0ACN9","uniref90":"UniRef90_P0ACN9","uniref50":"UniRef50_P0ACN9","genes":[{"name":{"value":"cytR"},"olnNames":[{"value":"b3934"},{"value":"JW3905"}]}],"alphafold_very_low_content":0.04105571847507331,"disorder_content":0.19648093841642228,"disprot_consensus":{"full":[{"start":1,"end":1,"type":"D"},{"start":2,"end":65,"type":"T"},{"start":66,"end":67,"type":"D"}],"Structural state":[{"start":1,"end":67,"type":"D"}],"Structural transition":[{"start":2,"end":65,"type":"T"}],"Molecular function":[{"start":1,"end":67,"type":"F"}]}},{"acc":"P39061","name":"Collagen alpha-1(XVIII) chain","sequence":"MAPDPSRRLCLLLLLLLSCRLVPASADGNSLSPLNPLVWLWPPKTSDSLEGPVSKPQNSSPVQSTENPTTHVVPQDGLTEQQTTPASSELPPEEEEEEDQKAGQGGSPATPAVPIPLVAPAASPDMKEENVAGVGAKILNVAQGIRSFVQLWDEDSTIGHSAGTEVPDSSIPTVLPSPAELSSAPQGSKTTLWLSSAIPSSPDAQTTEAGTLAVPTQLPPFQSNLQAPLGRPSAPPDFPGRAFLSSSTDQGSSWGNQEPPRQPQHLEGKGFLPMTARSSQQHRHSDVHSDIHGHVPLLPLVTGPLVTASLSVHGLLSVPSSDPSGQLSQVAALPGFPGTWVSHVAPSSGTGLSNDSALAGNGSLTSTSRCLPLPPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCRQFCEALEDECWNYLAGDRLPVVCASLPSQEDGYCVFIGPAAENVAEEVGLLQLLGDPLPEKISQIDDPHVGPAYIFGPDSNSGQVAQYHFPKLFFRDFSLLFHVRPATEAAGVLFAITDAAQVVVSLGVKLSEVRDGQQNISLLYTEPGASQTQTGASFRLPAFVGQWTHFALSVDGGSVALYVDCEEFQRVPFARASQGLELERGAGLFVGQAGTADPDKFQGMISELKVRKTPRVSPVHCLDEEDDDEDRASGDFGSGFEESSKSHKEDTSLLPGLPQPPPVTSPPLAGGSTTEDPRTEETEEDAAVDSIGAETLPGTGSSGAWDEAIQNPGRGLIKGGMKGQKGEPGAQGPPGPAGPQGPAGPVVQSPNSQPVPGAQGPPGPQGPPGKDGTPGRDGEPGDPGEDGRPGDTGPQGFPGTPGDVGPKGEKGDPGIGPRGPPGPPGPPGPSFRQDKLTFIDMEGSGFSGDIESLRGPRGFPGPPGPPGVPGLPGEPGRFGINGSYAPGPAGLPGVPGKEGPPGFPGPPGPPGPPGKEGPPGVAGQKGSVGDVGIPGPKGSKGDLGPIGMPGKSGLAGSPGPVGPPGPPGPPGPPGPGFAAGFDDMEGSGIPLWTTARSSDGLQGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNPGKDGVGRPGLPGPPGPPGPVIYVSSEDKAIVSTPGPEGKPGYAGFPGPAGPKGDLGSKGEQGLPGPKGEKGEPGTIFSPDGRALGHPQKGAKGEPGFRGPPGPYGRPGHKGEIGFPGRPGRPGTNGLKGEKGEPGDASLGFSMRGLPGPPGPPGPPGPPGMPIYDSNAFVESGRPGLPGQQGVQGPSGPKGDKGEVGPPGPPGQFPIDLFHLEAEMKGDKGDRGDAGQKGERGEPGAPGGGFFSSSVPGPPGPPGYPGIPGPKGESIRGPPGPPGPQGPPGIGYEGRQGPPGPPGPPGPPSFPGPHRQTVSVPGPPGPPGPPGPPGAMGASAGQVRIWATYQTMLDKIREVPEGWLIFVAEREELYVRVRNGFRKVLLEARTALPRGTGNEVAALQPPLVQLHEGSPYTRREYSYSTARPWRADDILANPPRLPDRQPYPGVPHHHSSYVHLPPARPTLSLAHTHQDFQPVLHLVALNTPLSGGMRGIRGADFQCFQQARAVGLSGTFRAFLSSRLQDLYSIVRRADRGSVPIVNLKDEVLSPSWDSLFSGSQGQLQPGARIFSFDGRDVLRHPAWPQKSVWHGSDPSGRRLMESYCETWRTETTGATGQASSLLSGRLLEQKAASCHNSYIVLCIENSFMTSFSK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":265,"region_id":"DP02542r001","start":27,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Small-angle  X-ray scattering showed DUF959 to be a highly extended, flexible molecule with a maximum dimension of ~23 nm.","type":"Abstract"},{"text":"The featureless shape of the scattering pattern (Figure 4A), as well as the Kratky plot (Figure 4B) with its lack of any clear maximum, demonstrate the non-globular, flexible and mainly disordered nature of DUF959.","type":"Results"}],"curator_id":"rpancsa","released":"2023_12","ec_name":"small-angle X-ray scattering evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30327321","version":2,"reference_html":"The N-terminal domain of unknown function (DUF959) in collagen XVIII is intrinsically disordered and highly O-glycosylated. <i> Kaur I, Ruskamo S, Koivunen J, Heljasvaara R, Lackman JJ, Izzi V, Petäjä-Repo UE, Kursula P, Pihlajaniemi T. </i> Biochem J, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:07:09.197Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":265,"region_id":"DP02542r002","start":27,"term_id":"IDPO:0000041","unpublished":true,"statement":[{"text":"Glycosidase treatment demonstrated considerable amounts of O-glycosylation, and expression of DUF959 in HEK293 SimpleCells capable of synthesizing only truncated O-glycans confirmed the presence of N-acetylgalactosamine-type O-glycans. The DUF959 sequence is characterized by numerous Ser and Thr residues, and this accounts for the finding that half of the recombinant protein consists of glycans.","type":"Abstract"},{"text":"The DUF959 of ColXVIII is rich in mucin-like O-glycosylation.","type":"Results"}],"curator_id":"rpancsa","released":"2023_12","ec_name":"deglycosylation assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30327321","version":2,"reference_html":"The N-terminal domain of unknown function (DUF959) in collagen XVIII is intrinsically disordered and highly O-glycosylated. <i> Kaur I, Ruskamo S, Koivunen J, Heljasvaara R, Lackman JJ, Izzi V, Petäjä-Repo UE, Kursula P, Pihlajaniemi T. </i> Biochem J, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006291","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:05:53.903Z","curator_name":"Federica Quaglia"},"term_name":"glycosylation display site","curator_orcid":"0000-0003-0849-9312","ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":265,"region_id":"DP02542r003","start":27,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"To characterize the secondary structure content of the DUF959, SRCD spectra were recorded. In this case the spectrum was typical of disordered proteins ,showing a prominent  negative minimum at 198 nm and a relatively low ellipticity near 210 nm  (Figure  3A). No remarkable changes in the secondary structure content  were discovered  when the temperature was increased to 90°C","type":"Results"}],"curator_id":"rpancsa","released":"2023_12","ec_name":"synchrotron radiation circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30327321","version":2,"reference_html":"The N-terminal domain of unknown function (DUF959) in collagen XVIII is intrinsically disordered and highly O-glycosylated. <i> Kaur I, Ruskamo S, Koivunen J, Heljasvaara R, Lackman JJ, Izzi V, Petäjä-Repo UE, Kursula P, Pihlajaniemi T. </i> Biochem J, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006202","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:05:55.717Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":265,"region_id":"DP02542r004","start":27,"term_id":"GO:0098772","unpublished":true,"statement":[{"text":"As intrinsically disordered regions and their post-translational modifications are often involved in protein interactions, our findings may point towards a role of the flexible mucin-like domain of ColXVIII as an interaction hub affecting cell signaling. Moreover, the MUCL-C18 may also serve as a lubricant at cell-extracellular matrix interfaces.","type":"Abstract"},{"text":"DUF959 is a mucin-like domain associated with lipid metabolism and glaucoma in humans.","type":"Figure"},{"text":"It was recently demonstrated that one of the SNPs in the DUF959 region, rs114139997, p.Gly111Arg, is associated with circulating lipid content and coronary artery disease [92], and that in line with this, genetic polymorphism in the FZ18 region of COL18A1 is associated with fat deposition and obesity [93]. Moreover, lack of the Col18a1 medium and long variants in mice results in markedly reduced adiposity and imbalance in circulating triglycerides [8], and lack of all three variants causes hypertriglyceridemia and increases atherosclerosis [94,95], further supporting the role of ColXVIII in regulating lipid metabolism. As mentioned above, site-specific O-glycosylation by GalNAc-T2 is a critical regulator of lipid metabolism, and DUF959 was found among the GalNAc-T2 targets in liver [85], implicating that O-glycosylation of ColXVIII may regulate its ability to control lipid homeostasis.","type":"Discussion"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"30327321","version":3,"reference_html":"The N-terminal domain of unknown function (DUF959) in collagen XVIII is intrinsically disordered and highly O-glycosylated. <i> Kaur I, Ruskamo S, Koivunen J, Heljasvaara R, Lackman JJ, Izzi V, Petäjä-Repo UE, Kursula P, Pihlajaniemi T. </i> Biochem J, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:05:53.319Z","curator_name":"Federica Quaglia"},"term_name":"molecular function regulator","curator_orcid":"0000-0002-0341-4888","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":265,"region_id":"DP02542r005","start":27,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"CD spectroscopy indicates a disordered conformation","type":"Results"},{"text":"To characterize the secondary structure content of the DUF959, SRCD spectra were recorded. In this case, the spectrum was typical of disordered proteins, showing a prominent negative minimum at 198 nm and a relatively low ellipticity near 210 nm (Figure 3A). No remarkable changes in the secondary structure content were discovered when the temperature was increased to 90°C (Figure 3B).","type":"Results"},{"text":"In 50% (v/v) TFE, the CD spectrum of DUF959 showed only minor changes towards helical characteristics, and no significant folding was observed (Figure 3C). We did not detect any conformational changes in DUF959 in the presence of dodecyl phosphocholine micelles, which are commonly used to mimic lipid membrane-binding conditions (data not shown).","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30327321","version":2,"reference_html":"The N-terminal domain of unknown function (DUF959) in collagen XVIII is intrinsically disordered and highly O-glycosylated. <i> Kaur I, Ruskamo S, Koivunen J, Heljasvaara R, Lackman JJ, Izzi V, Petäjä-Repo UE, Kursula P, Pihlajaniemi T. </i> Biochem J, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:05:54.503Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2023_12","length":1774,"ncbi_taxon_id":10090,"date":"2020-02-05T13:48:15.531Z","organism":"Mus musculus","features":{"gene3D":[{"start":1591,"end":1768,"id":"G3DSA:3.10.100.10","name":"Mannose-Binding Protein A, subunit A"},{"start":364,"end":483,"id":"G3DSA:1.10.2000.10","name":"Frizzled cysteine-rich domain"}],"pfam":[{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":823,"end":878},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":953,"end":1007},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":1066,"end":1114},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":1216,"end":1264},{"id":"PF01392","name":"Fz domain","start":376,"end":474},{"id":"PF06121","name":"Domain of Unknown Function (DUF959)","start":16,"end":218},{"id":"PF06482","name":"Collagenase NC10 and Endostatin","start":1600,"end":1769},{"id":"PF13385","name":"Concanavalin A-like lectin/glucanases superfamily","start":540,"end":676},{"id":"PF20010","name":"Collagen trimerization domain","start":1463,"end":1510}]},"disprot_id":"DP02542","regions_counter":5,"dataset":[],"UniParc":"UPI00000279C0","uniref100":"UniRef100_P39061","uniref90":"UniRef90_P39061","uniref50":"UniRef50_P39061","genes":[{"name":{"value":"Col18a1","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:88451","url":"http://www.informatics.jax.org/marker/MGI:88451"}}]}}],"alphafold_very_low_content":0.657271702367531,"disorder_content":0.13472378804960541,"disprot_consensus":{"full":[{"start":27,"end":265,"type":"D"}],"Structural state":[{"start":27,"end":265,"type":"D"}],"Disorder function":[{"start":27,"end":265,"type":"F"}],"Molecular function":[{"start":27,"end":265,"type":"F"}]}},{"acc":"Q9NUM4","name":"Transmembrane protein 106B","sequence":"MGKSLSHLPLHSSKEDAYDGVTSENMRNGLVNSEVHNEDGRNGDVSQFPYVEFTGRDSVTCPTCQGTGRIPRGQENQLVALIPYSDQRLRPRRTKLYVMASVFVCLLLSGLAVFFLFPRSIDVKYIGVKSAYVSYDVQKRTIYLNITNTLNITNNNYYSVEVENITAQVQFSKTVIGKARLNNITIIGPLDMKQIDYTVPTVIAEEMSYMYDFCTLISIKVHNIVLMMQVTVTTTYFGHSEQISQERYQYVDCGRNTTYQLGQSEYLNVLQPQQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"rpancsa","regions":[{"term_namespace":"Molecular function","ec_ontology":"ECO","end":95,"region_id":"DP02543r006","start":1,"term_id":"GO:0060090","unpublished":true,"statement":[{"text":"The N-terminal cytoplasmic domain of TMEM106B has been amazingly implicated in dynamically and transiently interacting with very diverse proteins or complexes, which include endocytic adaptor proteins such as clathrin heavy chain (CLTC) [12]; proteins including CHMP2B of the endosomal sorting complexes required for transport III (ESCRT-III) complex [13); and microtubule-associated protein 6 (Map6) [14].","type":"Introduction"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"30332472","version":3,"reference_html":"TMEM106B, a risk factor for FTLD and aging, has an intrinsically disordered cytoplasmic domain. <i> Kang J, Lim L, Song J. </i> PLoS One, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"molecular adaptor activity","curator_orcid":"0000-0002-0341-4888","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":119,"reference_id":"35477998","reference_source":"pmid","reference_html":"Generic amyloid fibrillation of TMEM106B in patient with Parkinson's disease dementia and normal elders. <i> Fan Y, Zhao Q, Xia W, Tao Y, Yu W, Chen M, Liu Y, Zhao J, Shen Y, Sun Y, Si C, Zhang S, Zhang Y, Li W, Liu C, Wang J, Li D. </i> Cell Res, 2022","date":"2022-09-27T14:32:31.650Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7X83"},{"db":"EMDB","id":"33054"}],"region_id":"DP02543r007","statement":[{"text":"The electron microscopy evidence of the structure of the TMEM106B fibril from normal elder shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":255,"end":274,"reference_id":"35477998","reference_source":"pmid","reference_html":"Generic amyloid fibrillation of TMEM106B in patient with Parkinson's disease dementia and normal elders. <i> Fan Y, Zhao Q, Xia W, Tao Y, Yu W, Chen M, Liu Y, Zhao J, Shen Y, Sun Y, Si C, Zhang S, Zhang Y, Li W, Liu C, Wang J, Li D. </i> Cell Res, 2022","date":"2022-09-27T14:32:46.747Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7X83"},{"db":"EMDB","id":"33054"}],"region_id":"DP02543r008","statement":[{"text":"The electron microscopy evidence of the structure of the TMEM106B fibril from normal elder shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"released":"2023_12","length":274,"ncbi_taxon_id":9606,"date":"2020-02-05T14:10:05.023Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF07092","name":"TM106 protein C-terminal domain","start":118,"end":258},{"id":"PF21002","name":"Transmembrane protein 106 N-terminal region","start":2,"end":95}]},"disprot_id":"DP02543","regions_counter":8,"dataset":["NDDs-related proteins"],"UniParc":"UPI0000073CA6","uniref100":"UniRef100_Q9NUM4","uniref90":"UniRef90_Q9NUM4","uniref50":"UniRef50_Q9NUM4","genes":[{"name":{"value":"TMEM106B"}}],"alphafold_very_low_content":0.21897810218978103,"disorder_content":0.5072992700729927,"disprot_consensus":{"full":[{"start":1,"end":119,"type":"D"},{"start":255,"end":274,"type":"D"}],"Structural state":[{"start":1,"end":119,"type":"D"},{"start":255,"end":274,"type":"D"}],"Molecular function":[{"start":1,"end":95,"type":"F"}]}},{"acc":"Q04410","name":"GRASP65 homolog protein 1","sequence":"MFRIAKNLVRTFEQSVQDTLALSQDSSNLDAFFQSIPPNLLSAQLESPVDAVSEGVKHTNVNETLSGLRIVWVDEMQFQLQSFFDYIVGFNDDPVPVVSNQHGFSYPDYRRITSIFNEHCGRTLKVNIWSAKGGTFRDEYISIISKESDDLDDVSLNHDERRPSSGEAHQFQALGFKVQWTPLIASTFTYHILNVNIPDGPAQSAGLIPDEDYIIGCQDGLLATGGETLLQDIVRSRANYDLVLYVYNKVSDCVRPITVHIGPDGRLGCNVGYGFLHRIPTVKHCPQQAQQQGQDDNPVPVPVPVESETAFVPSAFTAPPVPTKKKSKNKKGTQPLAMDDYFNEGRDKSSTAAKSAESDILAPPPQKQSSSD","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":372,"region_id":"DP02544r002","start":1,"term_id":"IDPO:0000003","unpublished":true,"statement":[{"text":"The theoretical molecular mass of the recombinant Grh1 is 41,119 Da, but SDS-PAGE analysis (Fig. 2B) resulted in an apparent molecular mass of ca. 45,000 Da. This suggests that the amount of hydrophobic aminoacids that compose Grh1 is smaller than expected for well-structured proteins, a phenomenon similar to what was previously observed for other IDPs","type":"Results"}],"curator_id":"rpancsa","released":"2023_12","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30356074","version":2,"reference_html":"The yeast GRASP Grh1 displays a high polypeptide backbone mobility along with an amyloidogenic behavior. <i> Fontana NA, Fonseca-Maldonado R, Mendes LFS, Meleiro LP, Costa-Filho AJ. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007689","term_name":"molten globule","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T17:29:16.716Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":372,"region_id":"DP02544r003","start":1,"term_id":"IDPO:0000003","unpublished":true,"statement":[{"text":"Size exclusion chromatography of the soluble protein on Superdex-200 column, whose result is shown in Fig. 2B, indicates an apparent molecular mass of 45,200 Da. The differences between the expected molecular mass of Grh1 and the values determined from hydrodynamic methods is likely a consequence of the not-fully globular conformation of Grh1 in solution, which has been observed for other proteins rich in disordered regions33, including the GRASP homologue in C. neoformans","type":"Results"}],"curator_id":"rpancsa","released":"2023_12","ec_name":"chromatography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30356074","version":2,"reference_html":"The yeast GRASP Grh1 displays a high polypeptide backbone mobility along with an amyloidogenic behavior. <i> Fontana NA, Fonseca-Maldonado R, Mendes LFS, Meleiro LP, Costa-Filho AJ. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","term_name":"molten globule","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T17:29:15.285Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":372,"region_id":"DP02544r004","start":1,"term_id":"IDPO:0000003","unpublished":true,"statement":[{"text":"The CD spectrum of Grh1 in aqueous solution (Fig. 3) has a minimum around 204 nm and a poorly resolved and lower intensity peak at 222 nm, which are features typical of CD spectra of proteins with a high content of unordered structures19. However, the negative peak at 222 nm is an indication of some ordered elements. Although the intensity ratio of the peaks at 222 nm ([−4,264 deg.cm2.dmol−1) and 200 nm (−6,904 deg.cm2.dmol−1) in the CD spectrum of Grh1 is similar to values observed for other proteins in the pre-molten-globule-like state, according to the “double wavelength” plot, [θ]222 vs. [θ]20019, Grh1 does not fit perfectly as a natively unfolded protein based on the estimation of its secondary structure content (11.5% α-helix, 22.1% β-sheet, 17.4% turns, and 49.8% random coil).","type":"Results"},{"text":"The urea-induced unfolding of Grh1 and DGRASP were analyzed by CD and fluorescence spectroscopies. The unfolding monitored by CD spectroscopy (Fig. 4) is a low cooperative transition as seen in the gradual change of the denatured fraction of the protein (fd) calculated from the molar ellipticity at 222 nm. The sigmoid-like transition is not as abrupt as expected for well-structured proteins of similar size19. The low steepness of the transition curve is typical of native molten globules or native coiled proteins and is due to the low percentage of secondary structure","type":"Results"}],"curator_id":"rpancsa","released":"2023_12","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30356074","version":2,"reference_html":"The yeast GRASP Grh1 displays a high polypeptide backbone mobility along with an amyloidogenic behavior. <i> Fontana NA, Fonseca-Maldonado R, Mendes LFS, Meleiro LP, Costa-Filho AJ. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"molten globule","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T17:29:13.414Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Biological process","ec_ontology":"ECO","end":372,"region_id":"DP02544r005","start":1,"term_id":"GO:1990000","unpublished":true,"statement":[{"text":"We report here our findings on the amyloidogenic behavior of this GRASP. They are derived from CD, fluorescence using a specific dye, and Congo Red absorbance experiments. The results obtained from this wide range of techniques led us to the conclusion that Grh1 can form amyloid-like structures in conditions that could be reasonably found in the cell. Moreover, we showed that the DGRASP, which is the most conserved region along GRASP family, is sufficient for the fiber formation.","type":"Introduction"}],"curator_id":"rpancsa","released":"2023_12","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30356074","version":3,"reference_html":"The yeast GRASP Grh1 displays a high polypeptide backbone mobility along with an amyloidogenic behavior. <i> Fontana NA, Fonseca-Maldonado R, Mendes LFS, Meleiro LP, Costa-Filho AJ. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"amyloid fibril formation","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T17:29:12.034Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2023_12","length":372,"ncbi_taxon_id":559292,"date":"2020-02-05T14:26:01.367Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","features":{"gene3D":[{"start":189,"end":285,"id":"G3DSA:2.30.42.10","name":"G3DSA:2.30.42.10"},{"start":189,"end":285,"id":"G3DSA:2.30.42.10","name":"G3DSA:2.30.42.10"}],"pfam":[{"id":"PF04495","name":"GRASP55/65 PDZ-like domain","start":127,"end":281}]},"disprot_id":"DP02544","regions_counter":5,"dataset":["Condensates-related proteins"],"UniParc":"UPI000006A1E4","uniref100":"UniRef100_Q04410","uniref90":"UniRef90_Q04410","uniref50":"UniRef50_Q04410","genes":[{"name":{"value":"GRH1"},"olnNames":[{"value":"YDR517W"}]}],"alphafold_very_low_content":0.24731182795698925,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":372,"type":"D"}],"Structural state":[{"start":1,"end":372,"type":"D"}],"Biological process":[{"start":1,"end":372,"type":"F"}]}},{"acc":"P07948","name":"Tyrosine-protein kinase Lyn","sequence":"MGCIKSKGKDSLSDDGVDLKTQPVRNTERTIYVRDPTSNKQQRPVPESQLLPGQRFQTKDPEEQGDIVVALYPYDGIHPDDLSFKKGEKMKVLEEHGEWWKAKSLLTKKEGFIPSNYVAKLNTLETEEWFFKDITRKDAERQLLAPGNSAGAFLIRESETLKGSFSLSVRDFDPVHGDVIKHYKIRSLDNGGYYISPRITFPCISDMIKHYQKQADGLCRRLEKACISPKPQKPWDKDAWEIPRESIKLVKRLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTREEPIYIITEYMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGCFTIKSDVWSFGILLYEIVTYGKIPYPGRTNADVMTALSQGYRMPRVENCPDELYDIMKMCWKEKAEERPTFDYLQSVLDDFYTATEGQYQQQP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":62,"region_id":"DP02545r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"The SH4 and UD chemical shifts show the low dispersion typical of disordered regions either alone or when part of the to the USH3 construct.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30360468","version":2,"reference_html":"The Two Isoforms of Lyn Display Different Intramolecular Fuzzy Complexes with the SH3 Domain. <i> Teixeira JMC, Fuentes H, Bielskutė S, Gairi M, Żerko S, Koźmiński W, Pons M. </i> Molecules, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":62,"region_id":"DP02545r002","start":1,"term_id":"GO:0005515","statement":[{"text":"The presence of fuzzy complexes was assessed by chemical shift perturbation, comparing the environment of backbone NH signals from residues in both the SH3 and disordered domains with those of the respective isolated domains. Significant perturbations far from the connecting residues are indicative of interdomain interactions while the retention of low dispersion in the SH4 and UD confirms that these regions remain disordered in the complex.","type":"Results"},{"text":"the initial 18 residues, including the entire SH4 domain, are clearly not affected by the presence of the SH3 domain. Therefore, in the case of Lyn, the fuzzy complex involves only the SH3 and Unique domains.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30360468","version":3,"reference_html":"The Two Isoforms of Lyn Display Different Intramolecular Fuzzy Complexes with the SH3 Domain. <i> Teixeira JMC, Fuentes H, Bielskutė S, Gairi M, Żerko S, Koźmiński W, Pons M. </i> Molecules, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"protein binding","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":62,"region_id":"DP02545r003","start":1,"term_id":"GO:0098772","statement":[{"text":"the evidence presented here support a general universal mechanism in which the Unique domain of the various SFK acts as a reader of the intracellular environment, by using the exquisite plasticity of the disordered regions, and transmit this information to generate the proper kinase response, through the fuzzy complex with the SH3 domain","type":"Discussion"},{"text":"We have used nuclear magnetic resonance (NMR) to show the formation of an intramolecular fuzzy complex in LynA and we show that the 21-residue segment (P23 to R43) that is absent in the LynB isoform contains a specific interaction site with the RT-loop of the SH3 domain, thus making the fuzzy complexes formed by the two isoforms, structurally distinct.","type":"Introduction"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30360468","version":3,"reference_html":"The Two Isoforms of Lyn Display Different Intramolecular Fuzzy Complexes with the SH3 Domain. <i> Teixeira JMC, Fuentes H, Bielskutė S, Gairi M, Żerko S, Koźmiński W, Pons M. </i> Molecules, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"molecular function regulator","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_12","length":512,"ncbi_taxon_id":9606,"date":"2020-02-05T16:08:36.458Z","organism":"Homo sapiens","features":{"gene3D":[{"start":117,"end":267,"id":"G3DSA:3.30.505.10","name":"SH2 domain"}],"pfam":[{"id":"PF00017","name":"SH2 domain","start":129,"end":211},{"id":"PF00018","name":"SH3 domain","start":69,"end":115},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":247,"end":496}]},"disprot_id":"DP02545","regions_counter":3,"dataset":[],"UniParc":"UPI000012EA83","uniref100":"UniRef100_P07948","uniref90":"UniRef90_P07948","uniref50":"UniRef50_P07948","genes":[{"name":{"value":"LYN"},"synonyms":[{"value":"JTK8"}]}],"alphafold_very_low_content":0.14453125,"disorder_content":0.12109375,"disprot_consensus":{"full":[{"start":1,"end":62,"type":"D"}],"Structural state":[{"start":1,"end":62,"type":"D"}],"Molecular function":[{"start":1,"end":62,"type":"F"}]}},{"acc":"P16070","name":"CD44 antigen","sequence":"MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPRIHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSSGSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATTLMSTSATATETATKRQETWDWFSWLFLPSESKNHLHTTTQMAGTSSNTISAGWEPNEENEDERDRHLSFSGSGIDDDEDFISSTISTTPRAFDHTKQNQDWTQWNPSHSNPEVLLQTTTRMTDVDRNGTTAYEGNWNPEAHPPLIHHEHHEEEETPHSTSTIQATPSSTTEETATQKEQWFGNRWHEGYRQTPKEDSHSTTGTAAASAHTSHPMQGRTTPSPEDSSWTDFFNPISHPMGRGHQAGRRMDMDSSHSITLQPTANPNTGLVEDLDRTGPLSMTTQQSNSQSFSTSHEGLEEDKDHPTTSTLTSSNRNDVTGGRRDPNHSEGSTTLLEGYTSHYPHTKESRTFIPVTSAKTGSFGVTAVTVGDSNSNVNRSLSGDQDTFHPSGGSHTTHGSESDGHSHGSQEGGANTTSGPIRTPQIPEWLIILASLLALALILAVCIAVNSRRRCGQKKKLVINSGNGAVEDRKPSGLNGEASKSQEMVHLVNKESSETPDQFMTADETRNLQNVDMKIGV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":742,"region_id":"DP02546r001","start":669,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Here we report the NMR chemical shift assignment of the recombinant intrinsically disordered CD44 cytoplasmic region (669-742)","type":"Abstract"},{"text":"Shown in Fig. 1 is the 1H–15N HSQC spectrum, exhibiting a relatively narrow proton chemical shift dispersion corresponding well with the expected values for an intrinsically disordered protein. Additional evidence for this is provided in Fig. 2b, showing only relatively small deviations from random coil for most parts of the protein.","type":"Results"}],"curator_id":"rpancsa","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30474821","version":2,"reference_html":"<sup>1</sup>H, <sup>15</sup>N, <sup>13</sup>C resonance assignment of the human CD44 cytoplasmic tail (669-742). <i> Frühbauer B, Mateos B, Konrat R. </i> Biomol NMR Assign, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"BMRB","id":"27625"}],"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-27T14:59:02.477Z"}},{"start":153,"end":178,"reference_id":"17085435","reference_source":"pmid","reference_html":"Ligand-induced structural changes of the CD44 hyaluronan-binding domain revealed by NMR. <i> Takeda M, Ogino S, Umemoto R, Sakakura M, Kajiwara M, Sugahara KN, Hayasaka H, Miyasaka M, Terasawa H, Shimada I. </i> J Biol Chem, 2006","date":"2022-09-28T14:46:50.669Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2I83"}],"region_id":"DP02546r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16336","entry_name":"hyaluronic acid"}],"statement":[{"text":"The 10 structures were superposed in a folded region, and residues 21-152 were defined, whereas residues 153-178 were poorly defined.","type":"Results"},{"text":"Residues 153-178 are disordered and are not shown.","type":"Figure"}]},{"start":153,"end":170,"reference_id":"17085435","reference_source":"pmid","reference_html":"Ligand-induced structural changes of the CD44 hyaluronan-binding domain revealed by NMR. <i> Takeda M, Ogino S, Umemoto R, Sakakura M, Kajiwara M, Sugahara KN, Hayasaka H, Miyasaka M, Terasawa H, Shimada I. </i> J Biol Chem, 2006","date":"2022-09-28T14:55:47.580Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2I83"}],"region_id":"DP02546r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16336","entry_name":"hyaluronic acid"}],"statement":[{"text":"A and B, ribbon representations of the unbound (A) and HA-bound (B) states of CD44 HABD. All of the α-helices are colored red. The β-strands are colored cyan and green in the Link module region (residues 32-124) and the lobular region (residues 21-31, 125-178), respectively. The C-terminal unfolded regions (residues 170-178 in A and 153-178 in B) are omitted.","type":"Figure"},{"text":"Comparisons of the structures and the backbone flexibility of CD44 HABD between its unbound and HA-bound states revealed that the C-terminal region of CD44 HABD became disordered upon HA binding.","type":"Article"},{"text":"This ligand-induced order-to-disorder transition of the C terminus of CD44 HABD provides a plausible explanation for the mechanism underlying the HA-induced CD44-mediated cell migration.","type":"Article"}]},{"start":669,"end":742,"reference_id":"30474821","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>15</sup>N, <sup>13</sup>C resonance assignment of the human CD44 cytoplasmic tail (669-742). <i> Frühbauer B, Mateos B, Konrat R. </i> Biomol NMR Assign, 2019","date":"2025-04-25T22:20:17.128Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP02546r007","statement":[{"text":"Here we report the NMR chemical shift assignment of the recombinant intrinsically disordered CD44 cytoplasmic region (669-742)","type":"Abstract"},{"text":"Shown in Fig. 1 is the 1H–15N HSQC spectrum, exhibiting a relatively narrow proton chemical shift dispersion corresponding well with the expected values for an intrinsically disordered protein. Additional evidence for this is provided in Fig. 2b, showing only relatively small deviations from random coil for most parts of the protein.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T22:26:42.779Z"}}],"released":"2023_12","length":742,"ncbi_taxon_id":9606,"date":"2020-02-07T09:14:29.899Z","organism":"Homo sapiens","features":{"gene3D":[{"start":19,"end":171,"id":"G3DSA:3.10.100.10","name":"Mannose-Binding Protein A, subunit A"}],"pfam":[{"id":"PF00193","name":"Extracellular link domain","start":32,"end":119}]},"disprot_id":"DP02546","regions_counter":7,"dataset":[],"UniParc":"UPI000013D3FE","uniref100":"UniRef100_P16070","uniref90":"UniRef90_P16070","uniref50":"UniRef50_P16070","genes":[{"name":{"value":"CD44"},"synonyms":[{"value":"LHR"},{"value":"MDU2"},{"value":"MDU3"},{"value":"MIC4"}]}],"alphafold_very_low_content":0.6981132075471698,"disorder_content":0.1347708894878706,"disprot_consensus":{"full":[{"start":153,"end":170,"type":"T"},{"start":171,"end":178,"type":"D"},{"start":669,"end":742,"type":"D"}],"Structural state":[{"start":153,"end":178,"type":"D"},{"start":669,"end":742,"type":"D"}],"Structural transition":[{"start":153,"end":170,"type":"T"}],"Disorder function":[{"start":669,"end":742,"type":"F"}]}},{"acc":"Q9Y6G9","name":"Cytoplasmic dynein 1 light intermediate chain 1","sequence":"MAAVGRVGSFGSSPPGLSSTYTGGPLGNEIASGNGGAAAGDDEDGQNLWSCILSEVSTRSRSKLPAGKNVLLLGEDGAGKTSLIRKIQGIEEYKKGRGLEYLYLNVHDEDRDDQTRCNVWILDGDLYHKGLLKFSLDAVSLKDTLVMLVVDMSKPWTALDSLQKWASVVREHVDKLKIPPEEMKQMEQKLIRDFQEYVEPGEDFPASPQRRNTASQEDKDDSVVLPLGADTLTHNLGIPVLVVCTKCDAISVLEKEHDYRDEHFDFIQSHIRKFCLQYGAALIYTSVKENKNIDLVYKYIVQKLYGFPYKIPAVVVEKDAVFIPAGWDNDKKIGILHENFQTLKAEDNFEDIITKPPVRKFVHEKEIMAEDDQVFLMKLQSLLAKQPPTAAGRPVDASPRVPGGSPRTPNRSVSSNVASVSPIPAGSKKIDPNMKAGATSEGVLANFFNSLLSKKTGSPGGPGVSGGSPAGGAGGGSSGLPPSTKKSGQKPVLDVHAELDRITRKPVTVSPTTPTSPTEGEAS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":523,"region_id":"DP02547r001","start":388,"term_id":"IDPO:0000002","statement":[{"text":"we first characterized LIC1-C (residues 388–523) by NMR spectroscopy. The 15N-1H heteronuclear single quantum coherence (HSQC) spectrum of LIC1-C at 25°C showed a narrow 7.8 to 8.6 parts per million (ppm) amide-proton chemical shift range, indicating a predominance of structural disorder (Fig 1C). Near-complete backbone resonance assignment was achieved (104 out of the 117 nonproline residues; Fig 1C, S2 Fig). An overlay of 15N-1H HSQC spectra of two smaller constructs, consisting of residues 388–471 and 472–523, reproduced the spectrum obtained from the entire LIC1-C (S2A Fig). This finding indicates that there are no long-range interactions between N- and C-terminal segments of LIC1-C.","type":"Results"},{"text":"the relaxation data show that LIC1-C is intrinsically disordered with large amplitudes of motions faster than nanoseconds. In helix 1 and 2, the amplitudes are smaller and the local reorientation slower but still on the fast timescale. These results support the highly transient character of the helices derived from the SSP score.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30615611","version":2,"reference_html":"A transient helix in the disordered region of dynein light intermediate chain links the motor to structurally diverse adaptors for cargo transport. <i> Celestino R, Henen MA, Gama JB, Carvalho C, McCabe M, Barbosa DJ, Born A, Nichols PJ, Carvalho AX, Gassmann R, Vögeli B. </i> PLoS Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"BMRB","id":"27401"}],"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q96EA4","partner_end":null},{"partner_start":null,"db":"UniProt","id":"Q8TD16","partner_end":null},{"partner_start":null,"db":"UniProt","id":"Q86VS8","partner_end":null}],"ec_ontology":"ECO","end":523,"region_id":"DP02547r002","start":388,"term_id":"GO:0005515","statement":[{"text":"Adaptors known to bind LIC1-C include BICD2 and Spindly (SPDL1), which are likely related [15,16], as well as the structurally distinct adaptors HOOK3, RAB11 family-interacting protein 3 (RAB11FIP3; hereafter referred to as FIP3), and RAB-interacting lysosomal protein (RILP) [12,17].","type":"Introduction"},{"text":"To identify adaptor binding sites in LIC1-C, we recorded 15N-1H HSQC spectra of LIC1-C bound to SPDL1(2–359), BICD2(2–422), and HOOK3(2–239) using molar ratios of 1:0, 1:0.5, and 1:1 (Fig 2A, 2B, 2C and 2D). The spectra obtained from each titration series revealed similar modes of interaction for the three adaptors. Rather than chemical shifts being perturbed, many peaks were significantly attenuated because of binding.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30615611","version":3,"reference_html":"A transient helix in the disordered region of dynein light intermediate chain links the motor to structurally diverse adaptors for cargo transport. <i> Celestino R, Henen MA, Gama JB, Carvalho C, McCabe M, Barbosa DJ, Born A, Nichols PJ, Carvalho AX, Gassmann R, Vögeli B. </i> PLoS Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"protein binding","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":523,"region_id":"DP02547r003","start":388,"term_id":"IDPO:0000002","statement":[{"text":"The spectrum of LIC1-C corresponded largely to structural disorder. However, there were negative values at 208 nm and a negative shoulder at 222 nm. These features are indicative of residual helical structure, in agreement with our findings from NMR spectroscopy.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30615611","version":2,"reference_html":"A transient helix in the disordered region of dynein light intermediate chain links the motor to structurally diverse adaptors for cargo transport. <i> Celestino R, Henen MA, Gama JB, Carvalho C, McCabe M, Barbosa DJ, Born A, Nichols PJ, Carvalho AX, Gassmann R, Vögeli B. </i> PLoS Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":523,"region_id":"DP02547r004","start":388,"term_id":"GO:0060090","statement":[{"text":"the light intermediate chain (LIC) subunit of human dynein uses a short helix in its disordered C-terminal region to bind structurally distinct adaptor proteins that connect the motor to specific cargo.","type":"Abstract"},{"text":"Adaptors known to bind LIC1-C include BICD2 and Spindly (SPDL1), which are likely related [15,16], as well as the structurally distinct adaptors HOOK3, RAB11 family-interacting protein 3 (RAB11FIP3; hereafter referred to as FIP3), and RAB-interacting lysosomal protein (RILP) [12,17].","type":"Introduction"},{"text":"To identify adaptor binding sites in LIC1-C, we recorded 15N-1H HSQC spectra of LIC1-C bound to SPDL1(2–359), BICD2(2–422), and HOOK3(2–239) using molar ratios of 1:0, 1:0.5, and 1:1 (Fig 2A, 2B, 2C and 2D). The spectra obtained from each titration series revealed similar modes of interaction for the three adaptors. Rather than chemical shifts being perturbed, many peaks were significantly attenuated because of binding.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30615611","version":3,"reference_html":"A transient helix in the disordered region of dynein light intermediate chain links the motor to structurally diverse adaptors for cargo transport. <i> Celestino R, Henen MA, Gama JB, Carvalho C, McCabe M, Barbosa DJ, Born A, Nichols PJ, Carvalho AX, Gassmann R, Vögeli B. </i> PLoS Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"molecular adaptor activity","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q96EA4","partner_end":null}],"ec_ontology":"ECO","end":523,"region_id":"DP02547r006","start":388,"term_id":"GO:0005515","statement":[{"text":"the light intermediate chain (LIC) subunit of human dynein uses a short helix in its disordered C-terminal region to bind structurally distinct adaptor proteins that connect the motor to specific cargo.","type":"Abstract"},{"text":"Adaptors known to bind LIC1-C include BICD2 and Spindly (SPDL1), which are likely related [15,16], as well as the structurally distinct adaptors HOOK3, RAB11 family-interacting protein 3 (RAB11FIP3; hereafter referred to as FIP3), and RAB-interacting lysosomal protein (RILP) [12,17].","type":"Introduction"},{"text":"We obtained a KD of 5.7 ± 1.9 μM for the interaction between LIC1(388–523) and SPDL1(2–359) (Fig 2E).","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"surface plasmon resonance evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30615611","version":3,"reference_html":"A transient helix in the disordered region of dynein light intermediate chain links the motor to structurally diverse adaptors for cargo transport. <i> Celestino R, Henen MA, Gama JB, Carvalho C, McCabe M, Barbosa DJ, Born A, Nichols PJ, Carvalho AX, Gassmann R, Vögeli B. </i> PLoS Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001269","term_name":"protein binding","curator_orcid":"0000-0003-0849-9312","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q96EA4","partner_end":null},{"partner_start":null,"db":"UniProt","id":"Q8TD16","partner_end":null}],"ec_ontology":"ECO","end":523,"region_id":"DP02547r007","start":388,"term_id":"GO:0005515","statement":[{"text":"the light intermediate chain (LIC) subunit of human dynein uses a short helix in its disordered C-terminal region to bind structurally distinct adaptor proteins that connect the motor to specific cargo.","type":"Abstract"},{"text":"Adaptors known to bind LIC1-C include BICD2 and Spindly (SPDL1), which are likely related [15,16], as well as the structurally distinct adaptors HOOK3, RAB11 family-interacting protein 3 (RAB11FIP3; hereafter referred to as FIP3), and RAB-interacting lysosomal protein (RILP) [12,17].","type":"Introduction"},{"text":"We also measured binding to fluorescently labeled LIC1(388–523) in microscale thermophoresis (MST) experiments. We obtained KD values of 13.1 ± 0.4 μM and 6.0 ± 1.3 μM for the interaction with SPDL1(2–359) and BICD2(2–422), respectively, which is in reasonable agreement with the SPR analysis","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"microscale thermophoresis evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30615611","version":3,"reference_html":"A transient helix in the disordered region of dynein light intermediate chain links the motor to structurally diverse adaptors for cargo transport. <i> Celestino R, Henen MA, Gama JB, Carvalho C, McCabe M, Barbosa DJ, Born A, Nichols PJ, Carvalho AX, Gassmann R, Vögeli B. </i> PLoS Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006303","term_name":"protein binding","curator_orcid":"0000-0003-0849-9312","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q96NA2","partner_end":null},{"partner_start":null,"db":"UniProt","id":"O75154","partner_end":null},{"partner_start":null,"db":"UniProt","id":"Q96EA4","partner_end":null},{"partner_start":null,"db":"UniProt","id":"Q8TD16","partner_end":null},{"partner_start":null,"db":"UniProt","id":"Q86VS8","partner_end":null}],"ec_ontology":"ECO","end":523,"region_id":"DP02547r008","start":388,"term_id":"GO:0005515","statement":[{"text":"the light intermediate chain (LIC) subunit of human dynein uses a short helix in its disordered C-terminal region to bind structurally distinct adaptor proteins that connect the motor to specific cargo.","type":"Abstract"},{"text":"Adaptors known to bind LIC1-C include BICD2 and Spindly (SPDL1), which are likely related [15,16], as well as the structurally distinct adaptors HOOK3, RAB11 family-interacting protein 3 (RAB11FIP3; hereafter referred to as FIP3), and RAB-interacting lysosomal protein (RILP) [12,17].","type":"Introduction"},{"text":"To directly test whether helix 1 is important for adaptor binding, we performed in vitro pull-down experiments using purified glutathione S-transferase (GST)-tagged versions of LIC1-C (Fig 3A and 3B) and LIC2-C (Fig 4A and 4B) as bait. In addition to BICD2(2–422), SPDL1(2–359), and HOOK3(2–552), we purified full-length versions of RILP (residues 1–401) and FIP3 (residues 2–756), as well as an N-terminal fragment of NIN (residues 1–693) (Fig 3C, S1B Fig). Using Coomassie Blue staining and immunoblotting for the Strep-tag II at the adaptor C terminus, all adaptors were readily detected in GST pull-downs with LIC1(388–523) and LIC1(388–471) (Fig 3D).","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30615611","version":3,"reference_html":"A transient helix in the disordered region of dynein light intermediate chain links the motor to structurally diverse adaptors for cargo transport. <i> Celestino R, Henen MA, Gama JB, Carvalho C, McCabe M, Barbosa DJ, Born A, Nichols PJ, Carvalho AX, Gassmann R, Vögeli B. </i> PLoS Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006077","term_name":"protein binding","curator_orcid":"0000-0003-0849-9312","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","length":523,"ncbi_taxon_id":9606,"date":"2020-02-07T11:42:39.038Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF05783","name":"Dynein light intermediate chain (DLIC)","start":43,"end":511}]},"disprot_id":"DP02547","regions_counter":9,"dataset":[],"UniParc":"UPI000006E91C","uniref100":"UniRef100_Q9Y6G9","uniref90":"UniRef90_Q9Y6G9","uniref50":"UniRef50_Q9Y6G9","genes":[{"name":{"value":"DYNC1LI1"},"synonyms":[{"value":"DNCLI1"}]}],"alphafold_very_low_content":0.40344168260038243,"disorder_content":0.26003824091778205,"disprot_consensus":{"full":[{"start":388,"end":523,"type":"D"}],"Structural state":[{"start":388,"end":523,"type":"D"}],"Molecular function":[{"start":388,"end":523,"type":"F"}]}},{"acc":"P0AES9","name":"Acid stress chaperone HdeA","sequence":"MKKVLGVILGGLLLLPVVSNAADAQKAADNKKPVNSWTCEDFLAVDESFQPTAVGFAEALNNKDKPEDAVLDVQGIATVTPAIVQACTQDKQANFKDKVKGEWDKIKKDM","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"creator":"rpancsa","regions":[{"term_namespace":"Structural transition","ec_ontology":"ECO","end":110,"region_id":"DP02548r001","start":22,"term_id":"IDPO:0000014","statement":[{"text":"One-dimensional 19F NMR spectra were collected at pH 7.0 and 2.0 for all 19F-labeling sites (Fig. S7 and S8), and the results show that the 19F chemical shifts are dispersed over a range of ∼5 ppm (−47.7 to −52.5 ppm) at pH 7 while clustering around −48.3 ppm at pH 2, which is consistent with acid-induced unfolding (see more details in supporting Discussion).","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30573682","version":4,"reference_html":"Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone. <i> Yu XC, Hu Y, Ding J, Li H, Jin C. </i> J Biol Chem, 2019","date":"2026-06-24T15:29:50.890Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"order to disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural transition","conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":2}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-24T15:47:34.853Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":110,"region_id":"DP02548r004","start":22,"term_id":"IDPO:0000002","statement":[{"text":"By using a combination of circular dichroism (CD) and fluorescence measurements, we found that HdeA is only partially unfolded by acid treatment, and it retains significant secondary structure but little tertiary structure in its active form [supporting information (SI) Fig. S1]. ","type":"Results"},{"text":"When we performed the same experiments at pH 2.2, we calculated a distance of 22 ± 1.5 Å (Fig. 5B), in which the partial unfolding of HdeA results in a 2-Å increase in the apparent donor–acceptor distance. Complete unfolding of HdeA in 5 M Gdn yielded an apparent distance of 30 ± 2.8 Å (Fig. 5C). The difference between HdeApH2.2 and completely unfolded HdeA probably reflects the residual secondary structure of HdeA at low pH (Fig. S1A).","type":"Results"},{"text":"During the transit of pathogenic bacteria through the human stomach (pH <3), acidic conditions trigger dimer dissociation and this protein get disordered.","type":"Curator statement"}],"curator_id":"vnugnes","released":"2026_06","ec_name":"fluorescence evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19321422","version":7,"reference_html":"Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding. <i> Tapley TL, Körner JL, Barge MT, Hupfeld J, Schauerte JA, Gafni A, Jakob U, Bardwell JC. </i> Proc Natl Acad Sci U S A, 2009","date":"2026-06-24T14:57:13.327Z","reference_source":"pmid","ec_id":"ECO:0001249","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"IPI","disprot_namespace":"Structural state","conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":2.2}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":110,"region_id":"DP02548r005","start":22,"term_id":"GO:0044183","statement":[{"text":"Our results are consistent with a model in which HdeA stably binds substrates at low pH, thereby preventing their irreversible aggregation. pH neutralization subsequently triggers the slow release of substrate proteins from HdeA, keeping the concentration of aggregation-sensitive intermediates below the threshold where they begin to aggregate. This provides a straightforward and ATP-independent mechanism that allows HdeA to facilitate protein refolding.","type":"Abstract"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"20080625","version":4,"reference_html":"Protein refolding by pH-triggered chaperone binding and release. <i> Tapley TL, Franzmann TM, Chakraborty S, Jakob U, Bardwell JC. </i> Proc Natl Acad Sci U S A, 2010","date":"2026-06-24T17:06:15.462Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"protein folding chaperone","curator_orcid":"0000-0003-0849-9312","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":2}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-24T17:06:19.910Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":110,"region_id":"DP02548r006","start":22,"term_id":"IDPO:0000003","statement":[{"text":"The results indicate that, as the pH transitions to 4.0 and lower (and progressively falls below the pKas for aspartate and glutamate residues), the protein samples a larger range of conformations as a precursor to unfolding and transitioning to the monomer. Based on these results it appears that the dimer interface is one of the first segments within the HdeA dimer to start opening up, as shown by the large loss of solvent protection for helix B at pH 4.0. ","type":"Results"},{"text":"During the transit of pathogenic bacteria through the human stomach (pH <4), acidic conditions trigger dimer dissociation and this protein get disordered.","type":"Curator statement"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"24375557","version":4,"reference_html":"NMR-monitored titration of acid-stress bacterial chaperone HdeA reveals that Asp and Glu charge neutralization produces a loosened dimer structure in preparation for protein unfolding and chaperone activation. <i> Garrison MA, Crowhurst KA. </i> Protein Sci, 2014","date":"2026-06-24T13:55:36.817Z","reference_source":"pmid","ec_id":"ECO:0006196","term_name":"molten globule","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state","conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":3}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-24T14:05:53.647Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":110,"region_id":"DP02548r009","start":22,"term_id":"GO:0044183","statement":[{"text":"A protein aggregation assay was carried out at pH 2 with HDEA (see Materials and Methods). The results illustrated in Figure 1(b) document that HDEA, at the equivalent mass concentration, prevents aggregation of denatured rhodanese under extremely acidic conditions in vitro.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"light scattering evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"10623550","version":4,"reference_html":"HDEA, a periplasmic protein that supports acid resistance in pathogenic enteric bacteria. <i> Gajiwala KS, Burley SK. </i> J Mol Biol, 2000","date":"2026-06-24T16:41:42.090Z","reference_source":"pmid","ec_id":"ECO:0007062","term_name":"protein folding chaperone","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":2}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-24T16:41:47.069Z"}},{"start":22,"end":110,"reference_id":"19321422","reference_source":"pmid","reference_html":"Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding. <i> Tapley TL, Körner JL, Barge MT, Hupfeld J, Schauerte JA, Gafni A, Jakob U, Bardwell JC. </i> Proc Natl Acad Sci U S A, 2009","date":"2026-06-24T14:28:00.963Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0000244","ec_ontology":"ECO","ec_name":"combinatorial evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":3}],"region_id":"DP02548r010","statement":[{"text":"By using a combination of circular dichroism (CD) and fluorescence measurements, we found that HdeA is only partially unfolded by acid treatment, and it retains significant secondary structure but little tertiary structure in its active form [supporting information (SI) Fig. S1]. ","type":"Results"},{"text":"During the transit of pathogenic bacteria through the human stomach (pH <4), acidic conditions trigger dimer dissociation and this protein get disordered.","type":"Curator statement"}]},{"start":22,"end":110,"reference_id":"19321422","reference_source":"pmid","reference_html":"Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding. <i> Tapley TL, Körner JL, Barge MT, Hupfeld J, Schauerte JA, Gafni A, Jakob U, Bardwell JC. </i> Proc Natl Acad Sci U S A, 2009","date":"2026-06-24T16:42:22.958Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0044183","term_name":"protein folding chaperone","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007062","ec_ontology":"ECO","ec_name":"light scattering evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":2.2}],"ec_go":"EXP","region_id":"DP02548r011","statement":[{"text":"We found that upon dilution into low pH buffer, chemically denatured rhodanese undergoes substantial aggregation (initial absorbance ≈0.1; Fig. 3, trace 1) within the time it takes to mix the components and begin the measurement (≈10 s). Importantly, this initial aggregation was suppressed in the presence of fully activated HdeA (initial absorbance ≈0.03; Fig. 3, trace 2). This significant difference in the initial absorbance values allowed us to determine whether a 2-s exposure of HdeA to pH 2.2 is sufficient to activate HdeA fully and to prevent the fast initial aggregation of rhodanese.","type":"Results"},{"text":"These results clearly demonstrate that the rapid pH-induced unfolding and monomerization (as shown in Figs. 1 and 2) fully activate the HdeA chaperone function. This rapid activation makes HdeA ideally suited to bind proteins as they themselves unfold in response to acid, thereby preventing their aggregation.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":22,"end":110,"reference_id":"19321422","reference_source":"pmid","reference_html":"Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding. <i> Tapley TL, Körner JL, Barge MT, Hupfeld J, Schauerte JA, Gafni A, Jakob U, Bardwell JC. </i> Proc Natl Acad Sci U S A, 2009","date":"2026-06-24T14:37:14.250Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007013","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":6}],"region_id":"DP02548r012","statement":[{"text":"By using a combination of circular dichroism (CD) and fluorescence measurements, we found that HdeA is only partially unfolded by acid treatment, and it retains significant secondary structure but little tertiary structure in its active form [supporting information (SI) Fig. S1]. ","type":"Results"},{"text":"As shown in Fig. 1A, we found that the decrease in HdeA fluorescence upon acid-induced partial unfolding occurs very rapidly (kobs = 3.6 s−1) and followed kinetics that were well described by a single exponential function. ","type":"Results"},{"text":"At pH 6 this protein is fully folded. ","type":"Curator statement"}]},{"start":22,"end":110,"reference_id":"30573682","reference_source":"pmid","reference_html":"Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone. <i> Yu XC, Hu Y, Ding J, Li H, Jin C. </i> J Biol Chem, 2019","date":"2026-06-24T16:07:08.354Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7}],"region_id":"DP02548r013","statement":[{"text":"One-dimensional 19F NMR spectra were collected at pH 7.0 and 2.0 for all 19F-labeling sites (Fig. S7 and S8), and the results show that the 19F chemical shifts are dispersed over a range of ∼5 ppm (−47.7 to −52.5 ppm) at pH 7 while clustering around −48.3 ppm at pH 2, which is consistent with acid-induced unfolding (see more details in supporting Discussion).","type":"Results"},{"text":"At pH 2.5, when HdeA is highly activated, over half of the total number of residues show exchanges between folded and unfolded conformations, and the residues are spread out in the protein sequence, suggesting that the exchange process corresponds to a global unfolding of the protein structure.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":22,"end":110,"reference_id":"30573682","reference_source":"pmid","reference_html":"Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone. <i> Yu XC, Hu Y, Ding J, Li H, Jin C. </i> J Biol Chem, 2019","date":"2026-06-24T16:08:03.982Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":2}],"region_id":"DP02548r014","statement":[{"text":"One-dimensional 19F NMR spectra were collected at pH 7.0 and 2.0 for all 19F-labeling sites (Fig. S7 and S8), and the results show that the 19F chemical shifts are dispersed over a range of ∼5 ppm (−47.7 to −52.5 ppm) at pH 7 while clustering around −48.3 ppm at pH 2, which is consistent with acid-induced unfolding (see more details in supporting Discussion).","type":"Results"},{"text":"At pH 2.5, when HdeA is highly activated, over half of the total number of residues show exchanges between folded and unfolded conformations, and the residues are spread out in the protein sequence, suggesting that the exchange process corresponds to a global unfolding of the protein structure.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":49,"end":56,"reference_id":"30573682","reference_source":"pmid","reference_html":"Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone. <i> Yu XC, Hu Y, Ding J, Li H, Jin C. </i> J Biol Chem, 2019","date":"2026-06-24T15:21:30.477Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0044183","term_name":"protein folding chaperone","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":2}],"ec_go":"EXP","region_id":"DP02548r015","statement":[{"text":"Furthermore, comparison of the signal line widths in the free and complexed states at pH 2.0 supports the participation of segments 28–35, 49–55, as well as residue 16 in binding client proteins (Fig. 2C).","type":"Results"},{"text":"Taking all the above factors into consideration, it is clear that the two segments that are rich in hydrophobic residues, namely the 28–35 and 49–55 segments, play central roles in directly binding to unfolded client proteins under acid stress (Fig. 2A).","type":"Results"},{"text":"Taking into account that the 28–35 segment is more deeply buried in the core of the dimer, we herein term the 49–55 segment as client-binding site I and the 28–35 segment as client-binding site II (see below).","type":"Results"},{"text":"Author residue numbering has been mapped to the UniProt canonical sequence.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","term_is_obsolete":false,"term_not_annotate":false},{"start":70,"end":76,"reference_id":"30573682","reference_source":"pmid","reference_html":"Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone. <i> Yu XC, Hu Y, Ding J, Li H, Jin C. </i> J Biol Chem, 2019","date":"2026-06-24T15:22:23.734Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0044183","term_name":"protein folding chaperone","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":2}],"ec_go":"EXP","region_id":"DP02548r016","statement":[{"text":"Furthermore, comparison of the signal line widths in the free and complexed states at pH 2.0 supports the participation of segments 28–35, 49–55, as well as residue 16 in binding client proteins (Fig. 2C).","type":"Results"},{"text":"Taking all the above factors into consideration, it is clear that the two segments that are rich in hydrophobic residues, namely the 28–35 and 49–55 segments, play central roles in directly binding to unfolded client proteins under acid stress (Fig. 2A).","type":"Results"},{"text":"Taking into account that the 28–35 segment is more deeply buried in the core of the dimer, we herein term the 49–55 segment as client-binding site I and the 28–35 segment as client-binding site II (see below).","type":"Results"},{"text":"Author residue numbering has been mapped to the UniProt canonical sequence.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","term_is_obsolete":false,"term_not_annotate":false},{"start":22,"end":32,"reference_id":"30573682","reference_source":"pmid","reference_html":"Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone. <i> Yu XC, Hu Y, Ding J, Li H, Jin C. </i> J Biol Chem, 2019","date":"2026-06-24T16:13:41.289Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006287","ec_ontology":"ECO","ec_name":"electron paramagnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":4}],"region_id":"DP02548r017","statement":[{"text":"The results show that the inactive HdeA dimer structure is relatively compact at pH 6, with the majority of the residues minimally affected by the paramagnetic probes, whereas several regions, including the N and C termini as well as the two client-binding sites, show significantly increased solvent accessibility at pH 4 and 3 (Fig. 4) and is in general agreement with the NMR hydrogen/deuterium (H/D) exchange data previously reported (22).","type":"Results"},{"text":"In contrast, order-to-disorder conformational exchanges occur only at local regions at pH 3.0 and above, and these partially unfolded conformations most probably represent the unfolding intermediates along the pH-induced activation pathway.","type":"Results"}]},{"start":61,"end":76,"reference_id":"30573682","reference_source":"pmid","reference_html":"Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone. <i> Yu XC, Hu Y, Ding J, Li H, Jin C. </i> J Biol Chem, 2019","date":"2026-06-24T16:15:14.867Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006287","ec_ontology":"ECO","ec_name":"electron paramagnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":4}],"region_id":"DP02548r018","statement":[{"text":"The results show that the inactive HdeA dimer structure is relatively compact at pH 6, with the majority of the residues minimally affected by the paramagnetic probes, whereas several regions, including the N and C termini as well as the two client-binding sites, show significantly increased solvent accessibility at pH 4 and 3 (Fig. 4) and is in general agreement with the NMR hydrogen/deuterium (H/D) exchange data previously reported (22).","type":"Results"},{"text":"In contrast, order-to-disorder conformational exchanges occur only at local regions at pH 3.0 and above, and these partially unfolded conformations most probably represent the unfolding intermediates along the pH-induced activation pathway.","type":"Results"}]},{"start":91,"end":110,"reference_id":"30573682","reference_source":"pmid","reference_html":"Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone. <i> Yu XC, Hu Y, Ding J, Li H, Jin C. </i> J Biol Chem, 2019","date":"2026-06-24T16:15:31.153Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006287","ec_ontology":"ECO","ec_name":"electron paramagnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":4}],"region_id":"DP02548r019","statement":[{"text":"The results show that the inactive HdeA dimer structure is relatively compact at pH 6, with the majority of the residues minimally affected by the paramagnetic probes, whereas several regions, including the N and C termini as well as the two client-binding sites, show significantly increased solvent accessibility at pH 4 and 3 (Fig. 4) and is in general agreement with the NMR hydrogen/deuterium (H/D) exchange data previously reported (22).","type":"Results"},{"text":"In contrast, order-to-disorder conformational exchanges occur only at local regions at pH 3.0 and above, and these partially unfolded conformations most probably represent the unfolding intermediates along the pH-induced activation pathway.","type":"Results"}]},{"start":22,"end":110,"reference_id":"30573682","reference_source":"pmid","reference_html":"Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone. <i> Yu XC, Hu Y, Ding J, Li H, Jin C. </i> J Biol Chem, 2019","date":"2026-06-24T16:46:51.437Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0010447","term_name":"response to acidic pH","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007013","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP02548r020","statement":[{"text":"A group of stress-response chaperones in both eubacteria and eukaryotes have been found to adopt well-folded structures under nonstress conditions and become activated via unfolding under stress conditions (5).","type":"Results"},{"text":"Taken together, the acid-induced activation of HdeA is a multistep process, which involves the destabilization of three essential structural locks that inhibit the chaperone activity under nonstress conditions.","type":"Results"},{"text":"Finally, when pH further decreases, the whole-protein structure collapses and becomes fully activated, with both sites exposed for client interactions. In the fully activated state, the N- and C-terminal regions of HdeA form two highly charged, flexible “tails” that help increase the solubility of the HdeA–client complexes, whereas the two essentially hydrophobic client-binding sites are held into a “ring” structure by the strictly conserved disulfide bond (Fig. 6, B and C).","type":"Results"}],"term_comment":"This term should be used to annotate instances where a cell or organism is responding to a chemical that is playing the role of an acid (e.g. proton donor) and therefore lowering the pH. If instead you wish to describe a response to a specific acid as a chemical, such as the anion portion of glutamate, please annotate to the appropriate child of GO:0001101 'response to acid chemical'.","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a pH stimulus with pH < 7. pH is a measure of the acidity or basicity of an aqueous solution.\" [GOC:go_curators, GOC:tb, Wikipedia:PH]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":22,"end":110,"reference_id":"30573682","reference_source":"pmid","reference_html":"Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone. <i> Yu XC, Hu Y, Ding J, Li H, Jin C. </i> J Biol Chem, 2019","date":"2026-06-24T16:46:36.600Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006950","term_name":"response to stress","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007013","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP02548r021","statement":[{"text":"A group of stress-response chaperones in both eubacteria and eukaryotes have been found to adopt well-folded structures under nonstress conditions and become activated via unfolding under stress conditions (5).","type":"Results"},{"text":"Taken together, the acid-induced activation of HdeA is a multistep process, which involves the destabilization of three essential structural locks that inhibit the chaperone activity under nonstress conditions.","type":"Results"},{"text":"Finally, when pH further decreases, the whole-protein structure collapses and becomes fully activated, with both sites exposed for client interactions. In the fully activated state, the N- and C-terminal regions of HdeA form two highly charged, flexible “tails” that help increase the solubility of the HdeA–client complexes, whereas the two essentially hydrophobic client-binding sites are held into a “ring” structure by the strictly conserved disulfide bond (Fig. 6, B and C).","type":"Results"}],"term_comment":"Note that this term is in the subset of terms that should not be used for direct gene product annotation. Instead, select a child term or, if no appropriate child term exists, please request a new term. Direct annotations to this term may be amended during annotation QC.","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a disturbance in organismal or cellular homeostasis, usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation).\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":1,"end":110,"reference_id":"10623550","reference_source":"pmid","reference_html":"HDEA, a periplasmic protein that supports acid resistance in pathogenic enteric bacteria. <i> Gajiwala KS, Burley SK. </i> J Mol Biol, 2000","date":"2026-06-24T16:39:07.189Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990451","term_name":"cellular stress response to acidic pH","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":2}],"ec_go":"IMP","region_id":"DP02548r022","statement":[{"text":"At neutral pH, there is essentially no difference in cell viability. Following exposure to acid (pH 2), however, survival of the hdeA deletion strain is severely compromised. Whereas the wild-type strain recovered after an initial lag of a few hours, the hdeA deletion strain failed to grow even after 72 hours.","type":"Results"}],"term_comment":"An example of this is NOX1 in human (Q9Y5S8) in PMID:10615049.","term_def":"\"Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a disturbance in the homeostasis of organismal or cellular pH (with pH < 7). pH is a measure of the acidity or basicity of an aqueous solution.\" [GOC:BHF, GOC:go_curators, GOC:rl, PMID:10615049]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":22,"end":30,"reference_id":"30573682","reference_source":"pmid","reference_html":"Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone. <i> Yu XC, Hu Y, Ding J, Li H, Jin C. </i> J Biol Chem, 2019","date":"2026-06-24T16:55:03.377Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000059","term_name":"self-inhibition","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7}],"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ala22Lis30del","start":null,"end":null,"position":null}],"region_id":"DP02548r023","statement":[{"text":"In this study, we show direct evidence that the N terminus protects one of the two essential client-binding sites under nonstress conditions.","type":"Results"},{"text":"The self-inhibitory role of the N-terminal region is supported by the observation that an HdeA-NΔ9 mutant with the N-terminal nine residues deleted shows interactions with SurA, another native client of HdeA (13), under elevated pH conditions (Fig. S14, A and B).","type":"Results"},{"text":"The authors refer to the first 9 residues of the mature protein (residues22-30) being involved in the self-inhibition of the chaperone activity.","type":"Curator statement"}]},{"start":22,"end":110,"reference_id":"10623550","reference_source":"pmid","reference_html":"HDEA, a periplasmic protein that supports acid resistance in pathogenic enteric bacteria. <i> Gajiwala KS, Burley SK. </i> J Mol Biol, 2000","date":"2026-06-24T17:02:43.997Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7}],"cross_refs":[{"db":"PDB","id":"1DJ8"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P0AES9","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02548r024","statement":[{"text":"HDEA crystals are composed of symmetric homodimers","type":"Results"},{"text":"We suggest that HDEA dimers dissociate during bacterial passage through the stomach, permitting the hydrophobic HDEA monomers to sequester the exposed non-polar surfaces of the acid-denatured protein in the periplasmic space.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2021_06","length":110,"ncbi_taxon_id":83333,"date":"2020-02-07T14:37:39.290Z","organism":"Escherichia coli (strain K12)","features":{"gene3D":[{"start":22,"end":110,"id":"G3DSA:1.10.890.10","name":"HNS-dependent expression A"}],"pfam":[{"id":"PF06411","name":"HdeA/HdeB family","start":11,"end":96}]},"disprot_id":"DP02548","regions_counter":24,"dataset":["Stress response proteins"],"UniParc":"UPI000012C3B8","uniref100":"UniRef100_P0AET0","uniref90":"UniRef90_P0AET0","uniref50":"UniRef50_P0AET0","genes":[{"name":{"value":"hdeA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00946","url":"https://hamap.expasy.org/unirule/MF_00946"}}]},"synonyms":[{"value":"yhhC"},{"value":"yhiB"}],"olnNames":[{"value":"b3510"},{"value":"JW3478"}]}],"alphafold_very_low_content":0.10909090909090909,"disorder_content":0.8090909090909091,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"F"},{"start":22,"end":110,"type":"T"}],"Structural state":[{"start":22,"end":110,"type":"D"}],"Structural transition":[{"start":22,"end":110,"type":"T"}],"Molecular function":[{"start":22,"end":110,"type":"F"}],"Biological process":[{"start":1,"end":110,"type":"F"}],"Disorder function":[{"start":22,"end":30,"type":"F"}]}},{"acc":"O82775","name":"ATG8-interacting protein 1","sequence":"MANNEEHPPRGNEWEVVSLTSSAYAAAPGPYNVESRDVRKYDAYYGAETSRDLYMSEHFVFPPSEHENLPIDESLFVAEQRKDGRDLMLEGQGLSDQFHYEAGNNQQSIYGESALGSSRHMESFGSESAVYEHGLVDAEGNLDLHSDGEGEKDVKKSTHNLPCEAWWKRRAISMYSRTREANAIWSLFFAAAVTGLVVLGQRWQQERWQVLQLKWQSSISSEKLGRVLEPLSRLKDVIVRSNPQASLVRSGSSSEV","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"creator":"vsagris","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":180,"region_id":"DP02549r001","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"We noticed that the migration rates of ATI1-N and ATI2-N in SDS-PAGE were slower than\nexpected by their molecular weights (MwATI1 -N = 20.46 kDa; MwATI2-N = 21.02 kDa) (Fig. 3A). This simple observation represents a first indication that ATI1 -N and ATI2-N may be intrinsically disordered, because IDRs are typically depleted in hydrophobic residues, and, consequently, tend to bind less SDS, explaining their abnormally slow mobility in SDS-PAGE [37].","type":"Results"}],"curator_id":"rpancsa","released":"2022_06","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30642888","version":2,"reference_html":"The transmembrane autophagy cargo receptors ATI1 and ATI2 interact with ATG8 through intrinsically disordered regions with distinct biophysical properties. <i> Sjøgaard IMZ, Bressendorff S, Prestel A, Kausika S, Oksbjerg E, Kragelund BB, Brodersen P. </i> Biochem J, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007689","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-31T12:41:58.986Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":180,"region_id":"DP02549r002","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Since we cannot exclude that ATI1-N and ATI2-N form folded dimers, we subjected ATI1-N,\nATI2-N and the globular GST to heat treatments for 10 min at 75°C or 5 min at 95°C, and separated\naggregated from soluble protein by centrifugation (Fig. 3C-D). These aggregation tests showed that,\nin contrast to the GST control, ATI1-N and ATI2-N remained soluble upon subjection to elevated\ntemperatures that unfold most globular proteins from non-thermophilic organisms.","type":"Results"}],"curator_id":"fquaglia","released":"2022_06","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30642888","version":3,"reference_html":"The transmembrane autophagy cargo receptors ATI1 and ATI2 interact with ATG8 through intrinsically disordered regions with distinct biophysical properties. <i> Sjøgaard IMZ, Bressendorff S, Prestel A, Kausika S, Oksbjerg E, Kragelund BB, Brodersen P. </i> Biochem J, 2019","date":"2022-05-31T15:20:04.524Z","reference_source":"pmid","ec_id":"ECO:0006317","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-01T08:34:21.867Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":180,"region_id":"DP02549r003","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"We next subjected protein samples of ATI1-N, ATI2-N and the similarly sized, globular prolactin (PRL, 23 kDa) to size-exclusion chromatography in which the elution volume decreases with the Stokes radius of the protein, such that folded proteins elute at larger volumes than IDPs of similar molecular mass. ATI2-N eluted at the smallest volume (67 ml), followed by ATI1-N (75 ml), and finally the globular PRL (85 ml) (Figure 3B), suggesting that the Stokes radii (r) increase in the order r(PRL) < r(ATI1-N) < r(ATI2-N).","type":"Results"}],"curator_id":"fquaglia","released":"2022_06","ec_name":"chromatography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30642888","version":3,"reference_html":"The transmembrane autophagy cargo receptors ATI1 and ATI2 interact with ATG8 through intrinsically disordered regions with distinct biophysical properties. <i> Sjøgaard IMZ, Bressendorff S, Prestel A, Kausika S, Oksbjerg E, Kragelund BB, Brodersen P. </i> Biochem J, 2019","date":"2022-06-04T19:59:42.875Z","reference_source":"pmid","ec_id":"ECO:0007680","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:43:11.178Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":180,"region_id":"DP02549r004","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The CD spectra of both ATI1-N and ATI2-N showed characteristic negative minima ∼200 nm, indicating a low content of secondary structure (Figure 4A). In addition, the broad minima at ∼220 nm may indicate some low (<10%) α-helical content [42], in agreement with the secondary structure prediction obtained utilizing the Psipred tool (Figure 4B) [43,44].","type":"Results"}],"curator_id":"fquaglia","released":"2022_06","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30642888","version":3,"reference_html":"The transmembrane autophagy cargo receptors ATI1 and ATI2 interact with ATG8 through intrinsically disordered regions with distinct biophysical properties. <i> Sjøgaard IMZ, Bressendorff S, Prestel A, Kausika S, Oksbjerg E, Kragelund BB, Brodersen P. </i> Biochem J, 2019","date":"2022-06-04T19:59:03.602Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:43:02.743Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":180,"region_id":"DP02549r005","start":1,"term_id":"IDPO:0000004","unpublished":true,"statement":[{"text":"For ATI1-N, the results are less clear. Although most amide and methyl proton signals collapse, characteristic of IDPs and different from fully folded regions, a broader dispersion of signals both in the methyl region and in the amide region was observed compared to ATI2-N (Fig. 5).","type":"Results"},{"text":"The latter is often observed in disordered regions with transient structure formation and/or transient long-range contacts, consistent with the more compact nature of ATI1-N compared to ATI2-N as suggested by the size exclusion chromatography results.","type":"Results"}],"curator_id":"rpancsa","released":"2022_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30642888","version":2,"reference_html":"The transmembrane autophagy cargo receptors ATI1 and ATI2 interact with ATG8 through intrinsically disordered regions with distinct biophysical properties. <i> Sjøgaard IMZ, Bressendorff S, Prestel A, Kausika S, Oksbjerg E, Kragelund BB, Brodersen P. </i> Biochem J, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"pre-molten globule","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-31T12:47:06.752Z"}},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q8VYK7","partner_end":null}],"ec_ontology":"ECO","end":17,"region_id":"DP02549r007","start":14,"term_id":"GO:0005515","unpublished":true,"statement":[{"text":"We next used the well-resolved indole NH peaks in the 1D 1H NMR spectra to query whether the ATI1-N and ATI2-N were sufficient for ATG8 interaction. First, we expressed wild type and W14A/V17A mutants of ATI1-N and ATI2-N (Figure 6B), and recorded 1D 1H NMR spectra to identify the peak corresponding to the indole NH of W14 in ATI1-N and ATI2-N (Figure 6C). We then recorded spectra in the presence and absence of purified ATG8f expressed in E. coli (Figure 6D,E), and examined the regions of the spectra with chemical shifts from the indole NH protons. This analysis showed clear line broadening of the W14 indole NH signal in the presence of ATG8f (Figure 6E), indicating that binding involves the N-terminal AIM of both ATI1-N and ATI2-N. We conclude that the N-terminal AIMs of ATI1 and ATI2 are necessary and sufficient for binding to ATG8f. We also conclude from the sharp peaks of the indole NH protons in the unbound state that the functional AIMs in both ATI1 and ATI2 reside in regions of high flexibility.","type":"Results"},{"text":"Region including the N-terminal AIM motif (WEVV) at position 14-17.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"30642888","version":4,"reference_html":"The transmembrane autophagy cargo receptors ATI1 and ATI2 interact with ATG8 through intrinsically disordered regions with distinct biophysical properties. <i> Sjøgaard IMZ, Bressendorff S, Prestel A, Kausika S, Oksbjerg E, Kragelund BB, Brodersen P. </i> Biochem J, 2019","date":"2022-06-28T10:42:58.583Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"protein binding","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp14Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val17Ala","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T13:41:39.694Z"}},{"start":14,"end":17,"reference_id":"30642888","reference_source":"pmid","reference_html":"The transmembrane autophagy cargo receptors ATI1 and ATI2 interact with ATG8 through intrinsically disordered regions with distinct biophysical properties. <i> Sjøgaard IMZ, Bressendorff S, Prestel A, Kausika S, Oksbjerg E, Kragelund BB, Brodersen P. </i> Biochem J, 2019","date":"2022-06-28T10:43:12.950Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","region_id":"DP02549r008","statement":[{"text":"We next used the well-resolved indole NH peaks in the 1D 1H NMR spectra to query whether the ATI1-N and ATI2-N were sufficient for ATG8 interaction. First, we expressed wild type and W14A/V17A mutants of ATI1-N and ATI2-N (Figure 6B), and recorded 1D 1H NMR spectra to identify the peak corresponding to the indole NH of W14 in ATI1-N and ATI2-N (Figure 6C). We then recorded spectra in the presence and absence of purified ATG8f expressed in E. coli (Figure 6D,E), and examined the regions of the spectra with chemical shifts from the indole NH protons. This analysis showed clear line broadening of the W14 indole NH signal in the presence of ATG8f (Figure 6E), indicating that binding involves the N-terminal AIM of both ATI1-N and ATI2-N. We conclude that the N-terminal AIMs of ATI1 and ATI2 are necessary and sufficient for binding to ATG8f. We also conclude from the sharp peaks of the indole NH protons in the unbound state that the functional AIMs in both ATI1 and ATI2 reside in regions of high flexibility.","type":"Results"},{"text":"Region including the N-terminal AIM motif (WEVV) at position 14-17.","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp14Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val17Ala","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T13:41:40.252Z"}},{"start":14,"end":17,"reference_id":"30642888","reference_source":"pmid","reference_html":"The transmembrane autophagy cargo receptors ATI1 and ATI2 interact with ATG8 through intrinsically disordered regions with distinct biophysical properties. <i> Sjøgaard IMZ, Bressendorff S, Prestel A, Kausika S, Oksbjerg E, Kragelund BB, Brodersen P. </i> Biochem J, 2019","date":"2022-06-28T10:43:29.762Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","region_id":"DP02549r009","statement":[{"text":"To test directly whether the N-terminal or C-terminal AIMs are functional, we first constructed point mutants in both putative AIMs in ATI2 and performed directed yeast two-hybrid assays with ATG8f. These experiments showed that ATI2 interaction with ATG8f was abolished upon mutation of the putative AIM in the N-terminal IDR, but not upon mutation of the putative AIM in the C-terminal part (Figure 6A). Thus, the N-terminal, but not the C-terminal AIM of ATI2 is necessary for ATG8 interaction in yeast.","type":"Results"},{"text":"Region including the N-terminal AIM motif (WEVV) at position 14-17.","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp14Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val17Ala","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T13:19:01.833Z"}},{"start":14,"end":17,"reference_id":"30642888","reference_source":"pmid","reference_html":"The transmembrane autophagy cargo receptors ATI1 and ATI2 interact with ATG8 through intrinsically disordered regions with distinct biophysical properties. <i> Sjøgaard IMZ, Bressendorff S, Prestel A, Kausika S, Oksbjerg E, Kragelund BB, Brodersen P. </i> Biochem J, 2019","date":"2022-06-28T10:43:20.026Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q8VYK7","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02549r010","statement":[{"text":"To test directly whether the N-terminal or C-terminal AIMs are functional, we first constructed point mutants in both putative AIMs in ATI2 and performed directed yeast two-hybrid assays with ATG8f. These experiments showed that ATI2 interaction with ATG8f was abolished upon mutation of the putative AIM in the N-terminal IDR, but not upon mutation of the putative AIM in the C-terminal part (Figure 6A). Thus, the N-terminal, but not the C-terminal AIM of ATI2 is necessary for ATG8 interaction in yeast.","type":"Results"},{"text":"Region including the N-terminal AIM motif (WEVV) at position 14-17.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp14Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val17Ala","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T13:17:17.352Z"}}],"released":"2022_06","length":256,"ncbi_taxon_id":3702,"date":"2020-02-10T09:41:42.545Z","organism":"Arabidopsis thaliana","features":{"gene3D":[],"pfam":[]},"disprot_id":"DP02549","regions_counter":10,"dataset":["Autophagy-related proteins","Stress response proteins"],"UniParc":"UPI00000AA21E","uniref100":"UniRef100_O82775","uniref90":"UniRef90_O82775","uniref50":"UniRef50_O82775","genes":[{"name":{"value":"ATI1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"22253227","url":"http://www.ncbi.nlm.nih.gov/pubmed/22253227","alternativeUrl":"https://europepmc.org/abstract/MED/22253227"}}]},"olnNames":[{"value":"At2g45980","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT2G45980","url":""}}]}]}],"alphafold_very_low_content":0.29296875,"disorder_content":0.703125,"disprot_consensus":{"full":[{"start":1,"end":180,"type":"D"}],"Structural state":[{"start":1,"end":180,"type":"D"}],"Molecular function":[{"start":14,"end":17,"type":"F"}],"Biological process":[{"start":14,"end":17,"type":"F"}]}},{"acc":"Q8VY98","name":"ATG8-interacting protein 2","sequence":"MADKDEAATRGNDWEVVSLTASAYAAAPGPKPVVDSKDDDHKEVTPCYEAETSHPLYMSRHFVFPPTGQLENTSDLTEASLTGSHCKEGSDLSLKGLDLSDDFGGLEFSEDKGKKEENIYTTAMSSLDDERAIGGSHVYEPVEEPTEPVSPSDVTLDLNPIKDDEVANSPPSEEAWWKRSVASLIAQAKETNTVWSICIAAAVMGIVILGQHWQQERWQILQQKWESSIGNEKAGRLMGPISRLKQAFVGGQRRDSFIRASAQNDR","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":193,"region_id":"DP02550r001","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"We noticed that the migration rates of ATI1-N and ATI2-N in SDS-PAGE were slower than\nexpected by their molecular weights (MwATI1 -N = 20.46 kDa; MwATI2-N = 21.02 kDa) (Fig. 3A). This simple observation represents a first indication that ATI1 -N and ATI2-N may be intrinsically disordered, because IDRs are typically depleted in hydrophobic residues, and, consequently, tend to bind less SDS, explaining their abnormally slow mobility in SDS-PAGE [37]. ","type":"Results"}],"curator_id":"rpancsa","released":"2022_06","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30642888","version":2,"reference_html":"The transmembrane autophagy cargo receptors ATI1 and ATI2 interact with ATG8 through intrinsically disordered regions with distinct biophysical properties. <i> Sjøgaard IMZ, Bressendorff S, Prestel A, Kausika S, Oksbjerg E, Kragelund BB, Brodersen P. </i> Biochem J, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007689","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:48:58.308Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":193,"region_id":"DP02550r002","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Since we cannot exclude that ATI1-N and ATI2-N form folded dimers, we subjected ATI1-N, ATI2-N and the globular GST to heat treatments for 10 min at 75°C or 5 min at 95°C, and separated aggregated from soluble protein by centrifugation (Figure 3C–D). These aggregation tests showed that, in contrast with the GST control, ATI1-N and ATI2-N remained soluble upon subjection to elevated temperatures that unfold most globular proteins from non-thermophilic organisms. ","type":"Results"}],"curator_id":"fquaglia","released":"2022_06","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30642888","version":3,"reference_html":"The transmembrane autophagy cargo receptors ATI1 and ATI2 interact with ATG8 through intrinsically disordered regions with distinct biophysical properties. <i> Sjøgaard IMZ, Bressendorff S, Prestel A, Kausika S, Oksbjerg E, Kragelund BB, Brodersen P. </i> Biochem J, 2019","date":"2022-06-04T19:57:02.326Z","reference_source":"pmid","ec_id":"ECO:0006317","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:48:59.736Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":193,"region_id":"DP02550r003","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"We next subjected protein samples of ATI1-N, ATI2-N and the similarly sized, globular prolactin (PRL, 23 kDa) to size-exclusion chromatography in which the elution volume decreases with the Stokes radius of the protein, such that folded proteins elute at larger volumes than IDPs of similar molecular mass. ATI2-N eluted at the smallest volume (67 ml), followed by ATI1-N (75 ml), and finally the globular PRL (85 ml) (Figure 3B), suggesting that the Stokes radii (r) increase in the order r(PRL) < r(ATI1-N) < r(ATI2-N).\nglobular PRL (85 ml) (Fig. 3B), suggesting that the Stokes radii (r) increase in the order r(PRL) < r(ATI1-N) < r(ATI2-N).","type":"Results"}],"curator_id":"fquaglia","released":"2022_06","ec_name":"chromatography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30642888","version":3,"reference_html":"The transmembrane autophagy cargo receptors ATI1 and ATI2 interact with ATG8 through intrinsically disordered regions with distinct biophysical properties. <i> Sjøgaard IMZ, Bressendorff S, Prestel A, Kausika S, Oksbjerg E, Kragelund BB, Brodersen P. </i> Biochem J, 2019","date":"2022-06-04T19:57:44.202Z","reference_source":"pmid","ec_id":"ECO:0007680","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:49:00.903Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":193,"region_id":"DP02550r004","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The CD spectra of both ATI1-N and ATI2-N showed characteristic negative minima ∼200 nm, indicating a low content of secondary structure (Figure 4A). In addition, the broad minima at ∼220 nm may indicate some low (<10%) α-helical content [42], in agreement with the secondary structure prediction obtained utilizing the Psipred tool (Figure 4B) [43,44].","type":"Results"}],"curator_id":"fquaglia","released":"2022_06","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30642888","version":3,"reference_html":"The transmembrane autophagy cargo receptors ATI1 and ATI2 interact with ATG8 through intrinsically disordered regions with distinct biophysical properties. <i> Sjøgaard IMZ, Bressendorff S, Prestel A, Kausika S, Oksbjerg E, Kragelund BB, Brodersen P. </i> Biochem J, 2019","date":"2022-06-04T19:58:18.582Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:49:02.571Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":193,"region_id":"DP02550r005","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"ATI2-N shows spectral properties of an IDP in all three regions: methyl protons show a narrow dispersion of chemical shifts above 0.8 ppm, amide protons resonate at chemical shifts within the interval 8.0 < δ < 8.7 ppm, and the three tryptophan NHs in ATI2-N give rise to sharp peaks reflecting high conformational flexibility (Fig. 5). Thus, together with the size exclusion chromatography and CD results, we conclude that ATI2-N is a highly disordered IDP with little or no long-range contacts.","type":"Results"}],"curator_id":"rpancsa","released":"2022_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30642888","version":2,"reference_html":"The transmembrane autophagy cargo receptors ATI1 and ATI2 interact with ATG8 through intrinsically disordered regions with distinct biophysical properties. <i> Sjøgaard IMZ, Bressendorff S, Prestel A, Kausika S, Oksbjerg E, Kragelund BB, Brodersen P. </i> Biochem J, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:49:03.642Z"}},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q8VYK7","partner_end":null}],"ec_ontology":"ECO","end":18,"region_id":"DP02550r007","start":13,"term_id":"GO:0005515","unpublished":true,"statement":[{"text":"We next used the well-resolved indole NH peaks in the 1D 1H NMR spectra to query whether the ATI1-N and ATI2-N were sufficient for ATG8 interaction. First, we expressed wild type and W14A/V17A mutants of ATI1-N and ATI2-N (Figure 6B), and recorded 1D 1H NMR spectra to identify the peak corresponding to the indole NH of W14 in ATI1-N and ATI2-N (Figure 6C). We then recorded spectra in the presence and absence of purified ATG8f expressed in E. coli (Figure 6D,E), and examined the regions of the spectra with chemical shifts from the indole NH protons. This analysis showed clear line broadening of the W14 indole NH signal in the presence of ATG8f (Figure 6E), indicating that binding involves the N-terminal AIM of both ATI1-N and ATI2-N. We conclude that the N-terminal AIMs of ATI1 and ATI2 are necessary and sufficient for binding to ATG8f. We also conclude from the sharp peaks of the indole NH protons in the unbound state that the functional AIMs in both ATI1 and ATI2 reside in regions of high flexibility.","type":"Results"},{"text":"Region including the N-terminal AIM motif (WEVV) at position 14-17.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"30642888","version":4,"reference_html":"The transmembrane autophagy cargo receptors ATI1 and ATI2 interact with ATG8 through intrinsically disordered regions with distinct biophysical properties. <i> Sjøgaard IMZ, Bressendorff S, Prestel A, Kausika S, Oksbjerg E, Kragelund BB, Brodersen P. </i> Biochem J, 2019","date":"2022-06-04T20:07:44.849Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"protein binding","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp14Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val17Ala","start":null,"end":null,"position":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:48:51.153Z"}},{"start":13,"end":18,"reference_id":"30642888","reference_source":"pmid","reference_html":"The transmembrane autophagy cargo receptors ATI1 and ATI2 interact with ATG8 through intrinsically disordered regions with distinct biophysical properties. <i> Sjøgaard IMZ, Bressendorff S, Prestel A, Kausika S, Oksbjerg E, Kragelund BB, Brodersen P. </i> Biochem J, 2019","date":"2022-06-04T20:08:46.041Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","region_id":"DP02550r010","statement":[{"text":"We next used the well-resolved indole NH peaks in the 1D 1H NMR spectra to query whether the ATI1-N and ATI2-N were sufficient for ATG8 interaction. First, we expressed wild type and W14A/V17A mutants of ATI1-N and ATI2-N (Figure 6B), and recorded 1D 1H NMR spectra to identify the peak corresponding to the indole NH of W14 in ATI1-N and ATI2-N (Figure 6C). We then recorded spectra in the presence and absence of purified ATG8f expressed in E. coli (Figure 6D,E), and examined the regions of the spectra with chemical shifts from the indole NH protons. This analysis showed clear line broadening of the W14 indole NH signal in the presence of ATG8f (Figure 6E), indicating that binding involves the N-terminal AIM of both ATI1-N and ATI2-N. We conclude that the N-terminal AIMs of ATI1 and ATI2 are necessary and sufficient for binding to ATG8f. We also conclude from the sharp peaks of the indole NH protons in the unbound state that the functional AIMs in both ATI1 and ATI2 reside in regions of high flexibility.","type":"Results"},{"text":"Region including the N-terminal AIM motif (WEVV) at position 14-17.","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp14Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val17Ala","start":null,"end":null,"position":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-07T14:36:39.917Z"}},{"start":13,"end":18,"reference_id":"30642888","reference_source":"pmid","reference_html":"The transmembrane autophagy cargo receptors ATI1 and ATI2 interact with ATG8 through intrinsically disordered regions with distinct biophysical properties. <i> Sjøgaard IMZ, Bressendorff S, Prestel A, Kausika S, Oksbjerg E, Kragelund BB, Brodersen P. </i> Biochem J, 2019","date":"2022-06-04T20:09:08.383Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","region_id":"DP02550r011","statement":[{"text":"To test directly whether the N-terminal or C-terminal AIMs are functional, we first constructed point mutants in both putative AIMs in ATI2 and performed directed yeast two-hybrid assays with ATG8f. These experiments showed that ATI2 interaction with ATG8f was abolished upon mutation of the putative AIM in the N-terminal IDR, but not upon mutation of the putative AIM in the C-terminal part (Figure 6A). Thus, the N-terminal, but not the C-terminal AIM of ATI2 is necessary for ATG8 interaction in yeast.","type":"Results"},{"text":"Region including the N-terminal AIM motif (WEVV) at position 14-17.","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp14Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val17Ala","start":null,"end":null,"position":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-07T14:36:41.837Z"}},{"start":13,"end":18,"reference_id":"30642888","reference_source":"pmid","reference_html":"The transmembrane autophagy cargo receptors ATI1 and ATI2 interact with ATG8 through intrinsically disordered regions with distinct biophysical properties. <i> Sjøgaard IMZ, Bressendorff S, Prestel A, Kausika S, Oksbjerg E, Kragelund BB, Brodersen P. </i> Biochem J, 2019","date":"2022-06-04T20:09:37.230Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q8VYK7","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02550r012","statement":[{"text":"To test directly whether the N-terminal or C-terminal AIMs are functional, we first constructed point mutants in both putative AIMs in ATI2 and performed directed yeast two-hybrid assays with ATG8f. These experiments showed that ATI2 interaction with ATG8f was abolished upon mutation of the putative AIM in the N-terminal IDR, but not upon mutation of the putative AIM in the C-terminal part (Figure 6A). Thus, the N-terminal, but not the C-terminal AIM of ATI2 is necessary for ATG8 interaction in yeast.","type":"Results"},{"text":"Region including the N-terminal AIM motif (WEVV) at position 14-17.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp14Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val17Ala","start":null,"end":null,"position":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:48:55.723Z"}}],"released":"2022_06","length":266,"ncbi_taxon_id":3702,"date":"2020-02-10T10:05:43.859Z","organism":"Arabidopsis thaliana","features":{"gene3D":[],"pfam":[]},"disprot_id":"DP02550","regions_counter":12,"dataset":["Autophagy-related proteins","Stress response proteins"],"UniParc":"UPI00000AC68E","uniref100":"UniRef100_Q8VY98","uniref90":"UniRef90_Q8VY98","uniref50":"UniRef50_Q8VY98","genes":[{"name":{"value":"ATI2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"22253227","url":"http://www.ncbi.nlm.nih.gov/pubmed/22253227","alternativeUrl":"https://europepmc.org/abstract/MED/22253227"}}]},"orfNames":[{"value":"A_IG005I10.20","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAB62839.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAB62839.1"}}]},{"value":"F5I10.20","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAF02797.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF02797.1"}}]}],"olnNames":[{"value":"At4g00355","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT4G00355","url":""}}]}]}],"alphafold_very_low_content":0.2932330827067669,"disorder_content":0.7255639097744361,"disprot_consensus":{"full":[{"start":1,"end":193,"type":"D"}],"Structural state":[{"start":1,"end":193,"type":"D"}],"Molecular function":[{"start":13,"end":18,"type":"F"}],"Biological process":[{"start":13,"end":18,"type":"F"}]}},{"acc":"Q8NBP7","name":"Proprotein convertase subtilisin/kexin type 9","sequence":"MGTVSSRRSWWPLPLLLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLAEAPEHGTTATFHRCAKDPWRLPGTYVVVLKEETHLSQSERTARRLQAQAARRGYLTKILHVFHGLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPPRYRADEYQPPDGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVTAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSQSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAVARCAPDEELLSCSSFSRSGKRRGERMEAQGGKLVCRAHNAFGGEGVYAIARCCLLPQANCSVHTAPPAEASMGTRVHCHQQGHVLTGCSSHWEVEDLGTHKPPVLRPRGQPNQCVGHREASIHASCCHAPGLECKVKEHGIPAPQEQVTVACEEGWTLTGCSALPGTSHVLGAYAVDNTCVVRSRDVSTTGSTSEGAVTAVAICCRSRHLAQASQELQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":60,"region_id":"DP02551r001","start":31,"term_id":"IDPO:0000002","statement":[{"text":"There are 16 PCSK9 crystal structures deposited in the Protein Data Bank (www.rcsb.org; as of July 2018), which used recombinant PCSK9 with an intact prodomain for crystallization (PDB accession codes 2P4E, 3SQO, 4NE9, 5VL7, 5VLA, 5VLH, 5VLL, 5VLP, 2PMW, 3H42, 3P5B, 3P5C, 4NMX, 5VLK, 2QTW, 4K8R). They comprise apo-structures of full length and of C-terminally truncated PCSK9 and of complexes of PCSK9 with antibody Fabs and with peptidic inhibitors. Despite the different PCSK9 forms used and the different space groups, all structures share the common feature in that there is no recognizable electron density for the N-terminal region of the PCSK9 prodomain encompassing residues Q31–T60. This strongly suggests that this segment is in a disordered state.","type":"Introduction"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30653992","version":2,"reference_html":"Identification of a Helical Segment within the Intrinsically Disordered Region of the PCSK9 Prodomain. <i> Ultsch M, Li W, Eigenbrot C, Di Lello P, Lipari MT, Gerhardy S, AhYoung AP, Quinn J, Franke Y, Chen Y, Kong Beltran M, Peterson A, Kirchhofer D. </i> J Mol Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":49,"region_id":"DP02551r002","start":45,"term_id":"IDPO:0000045","statement":[{"text":"The second PTM site is S47, which undergoes phosphorylation [30], [31] mediated by the Golgi casein kinase FAM20C [31], and the S47-phosphorylated PCSK9 was detected in human plasma [30]. The S47 phosphorylation appears to protect the acidic stretch from proteolysis [30].","type":"Introduction"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30653992","version":2,"reference_html":"Identification of a Helical Segment within the Intrinsically Disordered Region of the PCSK9 Prodomain. <i> Ultsch M, Li W, Eigenbrot C, Di Lello P, Lipari MT, Gerhardy S, AhYoung AP, Quinn J, Franke Y, Chen Y, Kong Beltran M, Peterson A, Kirchhofer D. </i> J Mol Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"phosphorylation display site","curator_orcid":"0000-0003-0849-9312","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":53,"region_id":"DP02551r003","start":31,"term_id":"IDPO:0000059","statement":[{"text":"the deletion of the acidic stretch creates a hyperactive PCSK9 displaying enhanced cellular uptake, increased potency of LDLR degradation, and stronger binding to LDLR [8], [37], [46]. This indicates that the acidic stretch has auto-inhibitory activity and functions as a negative regulator of PCSK9. The auto-inhibitory activity is not mediated by specific structural motifs. The acidic stretch could be shortened by a few residues, and up to six glutamic or aspartic acid residues could be charge-neutralized without changes in the auto-inhibitory activity, indicating that activity only depends on a minimal length and a minimal net charge [46].","type":"Introduction"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30653992","version":3,"reference_html":"Identification of a Helical Segment within the Intrinsically Disordered Region of the PCSK9 Prodomain. <i> Ultsch M, Li W, Eigenbrot C, Di Lello P, Lipari MT, Gerhardy S, AhYoung AP, Quinn J, Franke Y, Chen Y, Kong Beltran M, Peterson A, Kirchhofer D. </i> J Mol Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"self-inhibition","curator_orcid":"0000-0003-0849-9312","disprot_namespace":"Disorder function"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":45,"region_id":"DP02551r004","start":36,"term_id":"IDPO:0000011","statement":[{"text":"Solution NMR experiments with peptides spanning the acidic stretch region demonstrated a propensity to adopt an α-helix.","type":"Introduction"},{"text":"The region with α-helical propensity detected by NMR is a close match to the α-helical segment observed in the crystal structures (37DYEELVLAL45)","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30653992","version":2,"reference_html":"Identification of a Helical Segment within the Intrinsically Disordered Region of the PCSK9 Prodomain. <i> Ultsch M, Li W, Eigenbrot C, Di Lello P, Lipari MT, Gerhardy S, AhYoung AP, Quinn J, Franke Y, Chen Y, Kong Beltran M, Peterson A, Kirchhofer D. </i> J Mol Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder to order","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":45,"region_id":"DP02551r005","start":36,"term_id":"IDPO:0000011","statement":[{"text":"This helical conformation is stabilized by binding to antibody 6E2 (Ab6E2), as demonstrated by crystal structures of Fab6E2–peptide complexes. This antibody, which specifically recognizes the helical conformation, bound to both acidic stretch-derived peptides and to intact PCSK9, suggesting that the disorder-to-order transition is a physiological property of PCSK9.","type":"Introduction"},{"text":"The structures of the complexes of Fab6E2–Pep1 (wild-type), Fab6E2–Pep4 (sY38:pS47), and Fab6E2–Pep6 (E32K) were determined at 2.25, 2.20, and 2.10 Å resolution, respectively (see X-ray metrics in Suppl. Table S1). Overall, these complexes are remarkably similar (Fig. 2a–c). The most striking feature in all structures is a well-ordered 2 1/4-turn α-helix formed by the 9-amino-acid central portions of the peptides (37DYEELVLAL45).","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30653992","version":2,"reference_html":"Identification of a Helical Segment within the Intrinsically Disordered Region of the PCSK9 Prodomain. <i> Ultsch M, Li W, Eigenbrot C, Di Lello P, Lipari MT, Gerhardy S, AhYoung AP, Quinn J, Franke Y, Chen Y, Kong Beltran M, Peterson A, Kirchhofer D. </i> J Mol Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"6E4Y"},{"db":"PDB","id":"6E4Z"}],"term_name":"disorder to order","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":53,"region_id":"DP02551r006","start":31,"term_id":"GO:0005515","statement":[{"text":"Immunoblotting of conditioned media demonstrated that Ab6E2 specifically recognized the prodomain of PCSK9 secreted by the three cell lines (Fig. 1a). Furthermore, experiments with the N-terminally truncated PCSK9, in which the acidic stretch residues Q31–A53 were deleted (PCSK9Δ53), indicated that the Ab6E2 binding site is located within the acidic stretch region. First, Ab6E2 did not detect the prodomain band of PCSK9Δ53 in immunoblotting experiments (Fig. 1a). Second, surface plasmon resonance (SPR) experiments demonstrated that Ab6E2 bound to PCSK9 with a KD of 10.5 ± 1.2 nM, but did not interact with PCSK9Δ53 (Fig. 1b, inset).","type":"Results"},{"text":"To investigate whether the region deleted in PCSK9Δ53 (Q31–A53) contains the main antibody epitope, we synthesized a peptide corresponding to this sequence, except that the N-terminal Q31 was omitted. This peptide (Pep1) bound to Ab6E2 with a KD value of 3.8 μM (Table 1), confirming that the antibody epitope lies within the acidic stretch.","type":"Results"},{"text":"Remarkably, Pep2 with the sY38 modification had an approximately 2000-fold increased affinity to Ab6E2 (KD = 1.9 nM)","type":"Results"}],"curator_id":"esalladini","released":"2022_03","ec_name":"surface plasmon resonance evidence used in manual assertion","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"30653992","version":4,"reference_html":"Identification of a Helical Segment within the Intrinsically Disordered Region of the PCSK9 Prodomain. <i> Ultsch M, Li W, Eigenbrot C, Di Lello P, Lipari MT, Gerhardy S, AhYoung AP, Quinn J, Franke Y, Chen Y, Kong Beltran M, Peterson A, Kirchhofer D. </i> J Mol Biol, 2019","date":"2022-03-08T14:28:27.100Z","reference_source":"pmid","ec_id":"ECO:0001269","term_name":"protein binding","curator_orcid":"0000-0002-5152-5953","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"ABCD","id":"ABCD_AQ731","operator":"and","partner_start":null,"partner_end":null}]},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":40,"region_id":"DP02551r007","start":36,"term_id":"IDPO:0000037","statement":[{"text":"The Y38 residue undergoes O-sulfation mediated by the enzyme sulfotransferase [32,33].","type":"Introduction"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30653992","version":2,"reference_html":"Identification of a Helical Segment within the Intrinsically Disordered Region of the PCSK9 Prodomain. <i> Ultsch M, Li W, Eigenbrot C, Di Lello P, Lipari MT, Gerhardy S, AhYoung AP, Quinn J, Franke Y, Chen Y, Kong Beltran M, Peterson A, Kirchhofer D. </i> J Mol Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"molecular recognition display site","curator_orcid":"0000-0003-0849-9312","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":45,"region_id":"DP02551r008","start":37,"term_id":"GO:0098772","statement":[{"text":"There is strong evidence that the acidic stretch is involved in binding interactions. A recent study has implicated the acidic stretch in PCSK9 binding to LDL particles, which seems to regulate the activity of PCSK9 towards LDLR [45].","type":"Introduction"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30653992","version":3,"reference_html":"Identification of a Helical Segment within the Intrinsically Disordered Region of the PCSK9 Prodomain. <i> Ultsch M, Li W, Eigenbrot C, Di Lello P, Lipari MT, Gerhardy S, AhYoung AP, Quinn J, Franke Y, Chen Y, Kong Beltran M, Peterson A, Kirchhofer D. </i> J Mol Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"molecular function regulator","curator_orcid":"0000-0003-0849-9312","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","length":692,"ncbi_taxon_id":9606,"date":"2020-02-10T10:37:46.594Z","organism":"Homo sapiens","features":{"gene3D":[{"start":152,"end":450,"id":"G3DSA:3.40.50.200","name":"Peptidase S8/S53 domain"},{"start":61,"end":148,"id":"G3DSA:3.30.70.80","name":"Peptidase S8 propeptide/proteinase inhibitor I9"}],"pfam":[{"id":"PF00082","name":"Subtilase family","start":181,"end":419},{"id":"PF05922","name":"Peptidase inhibitor I9","start":77,"end":149},{"id":"PF18459","name":"Proprotein convertase subtilisin-like/kexin type 9 C-terminal domain","start":450,"end":531},{"id":"PF18463","name":"Proprotein convertase subtilisin-like/kexin type 9 C-terminal domain","start":602,"end":682},{"id":"PF18464","name":"Proprotein convertase subtilisin-like/kexin type 9 C-terminal domain","start":535,"end":600}]},"disprot_id":"DP02551","regions_counter":8,"dataset":[],"UniParc":"UPI000003B099","uniref100":"UniRef100_Q8NBP7","uniref90":"UniRef90_Q8NBP7","uniref50":"UniRef50_Q8NBP7","genes":[{"name":{"value":"PCSK9"},"synonyms":[{"value":"NARC1"}],"orfNames":[{"value":"PSEC0052"}]}],"alphafold_very_low_content":0.1315028901734104,"disorder_content":0.04335260115606936,"disprot_consensus":{"full":[{"start":31,"end":35,"type":"D"},{"start":36,"end":45,"type":"T"},{"start":46,"end":60,"type":"D"}],"Structural state":[{"start":31,"end":60,"type":"D"}],"Disorder function":[{"start":31,"end":53,"type":"F"}],"Structural transition":[{"start":36,"end":45,"type":"T"}],"Molecular function":[{"start":31,"end":53,"type":"F"}]}},{"acc":"P43629","name":"Killer cell immunoglobulin-like receptor 3DL1","sequence":"MSLMVVSMACVGLFLVQRAGPHMGGQDKPFLSAWPSAVVPRGGHVTLRCHYRHRFNNFMLYKEDRIHIPIFHGRIFQESFNMSPVTTAHAGNYTCRGSHPHSPTGWSAPSNPVVIMVTGNHRKPSLLAHPGPLVKSGERVILQCWSDIMFEHFFLHKEGISKDPSRLVGQIHDGVSKANFSIGPMMLALAGTYRCYGSVTHTPYQLSAPSDPLDIVVTGPYEKPSLSAQPGPKVQAGESVTLSCSSRSSYDMYHLSREGGAHERRLPAVRKVNRTFQADFPLGPATHGGTYRCFGSFRHSPYEWSDPSDPLLVSVTGNPSSSWPSPTEPSSKSGNPRHLHILIGTSVVIILFILLLFFLLHLWCSNKKNAAVMDQEPAGNRTANSEDSDEQDPEEVTYAQLDHCVFTQRKITRPSQRPKTPPTDTILYTELPNAKPRSKVVSCP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":444,"region_id":"DP02552r001","start":361,"term_id":"IDPO:0000002","statement":[{"text":"Consistent with the computer prediction that 3DL1-cyto is disordered, the1H-15N HSQC spectrum (Figure 1B) exhibits limited chemical shift dispersion in the NH dimension (8–8.6ppm).","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30773397","version":2,"reference_html":"Conformational Changes in the Cytoplasmic Region of KIR3DL1 upon Interaction with SHP-2. <i> Cheng H, Schwell V, Curtis BR, Fazlieva R, Roder H, Campbell KS. </i> Structure, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"BMRB","id":"27651"}],"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":385,"region_id":"DP02552r002","start":371,"term_id":"GO:0005515","statement":[{"text":"The CON spectra of unphosphorylated SET-3DL1-cyto complexes with each individual SH2-domain (inmolar ratios of SET-3DL1:N-SH2 or C-SH2 at 1:0.2) show binding-induced reduction of intensities for peaks mainly from residues at or surrounding the N-ITIM (371-DPEEVTYAQLPHCVF-385).","type":"Results"},{"text":"The NMR spectrum of the complex with N-SH2 also shows minor peak intensity reductions for residues 400-PPTDTILYTELPN-412 spanning the C-terminal ITIM (Figures 7A, black andS3A, black to red) that are not evident in complex with C-SH2","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30773397","version":3,"reference_html":"Conformational Changes in the Cytoplasmic Region of KIR3DL1 upon Interaction with SHP-2. <i> Cheng H, Schwell V, Curtis BR, Fazlieva R, Roder H, Campbell KS. </i> Structure, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"BMRB","id":"27651"}],"term_name":"protein binding","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":379,"region_id":"DP02552r003","start":375,"term_id":"IDPO:0000045","statement":[{"text":"3DL1binding to MHC-I ligand results in changes in local electrostatic interactions surrounding the TM and membrane-proximal region of 3DL1-cyto, which induces conformational changes in the N-terminal membrane-proximal region, including loss of transient ahelices, and hence liberating tyrosines from the membrane (Figures 8B and 8C) to be accessible for interaction with the N-SH2 of SHP-2 (Figure 8B) and phosphorylation by Src family PTK (Figure 8C). Phosphorylation of both ITIM tyrosines facilitates high-affinity interaction with both SH2 domains of SHP-2(or SHP-1) to fully activate these PTPs at the plasma membrane.","type":"Discussion"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30773397","version":2,"reference_html":"Conformational Changes in the Cytoplasmic Region of KIR3DL1 upon Interaction with SHP-2. <i> Cheng H, Schwell V, Curtis BR, Fazlieva R, Roder H, Campbell KS. </i> Structure, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"phosphorylation display site","curator_orcid":"0000-0003-0849-9312","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":444,"region_id":"DP02552r004","start":361,"term_id":"GO:0060090","statement":[{"text":"3DL1 binding to MHC-I ligand results in changes in local electrostatic interactions surrounding the TM and membrane-proximal region of 3DL1-cyto, which induces conformational changes in the N-terminal membrane-proximal region, including loss of transient a-helices, and hence liberating tyrosines from the membrane (Figures 8B and 8C) to be accessible for interaction with the N-SH2 of SHP-2 (Figure 8B) and phosphorylation by Src family PTK (Figure 8C). Phosphorylation of both ITIM tyrosines facilitates high-affinity interaction with both SH2 domains of SHP-2(or SHP-1) to fully activate these PTPs at the plasma membrane.","type":"Discussion"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30773397","version":3,"reference_html":"Conformational Changes in the Cytoplasmic Region of KIR3DL1 upon Interaction with SHP-2. <i> Cheng H, Schwell V, Curtis BR, Fazlieva R, Roder H, Campbell KS. </i> Structure, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"molecular adaptor activity","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":409,"region_id":"DP02552r005","start":405,"term_id":"IDPO:0000045","statement":[{"text":"3DL1binding to MHC-I ligand results in changes in local electrostatic interactions surrounding the TM and membrane-proximal region of 3DL1-cyto, which induces conformational changes in the N-terminal membrane-proximal region, including loss of transient ahelices, and hence liberating tyrosines from the membrane (Figures 8B and 8C) to be accessible for interaction with the N-SH2 of SHP-2 (Figure 8B) and phosphorylation by Src family PTK (Figure 8C). Phosphorylation of both ITIM tyrosines facilitates high-affinity interaction with both SH2 domains of SHP-2(or SHP-1) to fully activate these PTPs at the plasma membrane.","type":"Discussion"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30773397","version":2,"reference_html":"Conformational Changes in the Cytoplasmic Region of KIR3DL1 upon Interaction with SHP-2. <i> Cheng H, Schwell V, Curtis BR, Fazlieva R, Roder H, Campbell KS. </i> Structure, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"phosphorylation display site","curator_orcid":"0000-0003-0849-9312","disprot_namespace":"Disorder function"}],"released":"2021_06","length":444,"ncbi_taxon_id":9606,"date":"2020-02-10T11:27:43.083Z","organism":"Homo sapiens","features":{"gene3D":[{"start":220,"end":320,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":220,"end":320,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":220,"end":320,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"}],"pfam":[{"id":"PF00047","name":"Immunoglobulin domain","start":35,"end":107},{"id":"PF00047","name":"Immunoglobulin domain","start":131,"end":207},{"id":"PF00047","name":"Immunoglobulin domain","start":231,"end":305}]},"disprot_id":"DP02552","regions_counter":5,"dataset":[],"UniParc":"UPI000012DB24","uniref100":"UniRef100_P43629","uniref90":"UniRef90_P43629","uniref50":"UniRef50_Q8N743","genes":[{"name":{"value":"KIR3DL1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6338","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6338"}}]},"synonyms":[{"value":"CD158E"},{"value":"NKAT3"},{"value":"NKB1"}]}],"alphafold_very_low_content":0.2725225225225225,"disorder_content":0.1891891891891892,"disprot_consensus":{"full":[{"start":361,"end":444,"type":"D"}],"Structural state":[{"start":361,"end":444,"type":"D"}],"Molecular function":[{"start":361,"end":444,"type":"F"}],"Disorder function":[{"start":375,"end":379,"type":"F"},{"start":405,"end":409,"type":"F"}]}},{"acc":"Q6P5W5","name":"Zinc transporter ZIP4","sequence":"MASLVSLELGLLLAVLVVTATASPPAGLLSLLTSGQGALDQEALGGLLNTLADRVHCANGPCGKCLSVEDALGLGEPEGSGLPPGPVLEARYVARLSAAAVLYLSNPEGTCEDARAGLWASHADHLLALLESPKALTPGLSWLLQRMQARAAGQTPKMACVDIPQLLEEAVGAGAPGSAGGVLAALLDHVRSGSCFHALPSPQYFVDFVFQQHSSEVPMTLAELSALMQRLGVGREAHSDHSHRHRGASSRDPVPLISSSNSSSVWDTVCLSARDVMAAYGLSEQAGVTPEAWAQLSPALLQQQLSGACTSQSRPPVQDQLSQSERYLYGSLATLLICLCAVFGLLLLTCTGCRGVTHYILQTFLSLAVGAVTGDAVLHLTPKVLGLHTHSEEGLSPQPTWRLLAMLAGLYAFFLFENLFNLLLPRDPEDLEDGPCGHSSHSHGGHSHGVSLQLAPSELRQPKPPHEGSRADLVAEESPELLNPEPRRLSPELRLLPYMITLGDAVHNFADGLAVGAAFASSWKTGLATSLAVFCHELPHELGDFAALLHAGLSVRQALLLNLASALTAFAGLYVALAVGVSEESEAWILAVATGLFLYVALCDMLPAMLKVRDPRPWLLFLLHNVGLLGGWTVLLLLSLYEDDITF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":498,"region_id":"DP02554r001","start":424,"term_id":"IDPO:0000002","statement":[{"text":"The 1H‐15N HSQC spectrum of hZIP4 ICL2 measured at 10°C [Fig. 1(c)] displays a narrow chemical shift dispersion in the 1H dimension ranging from 7.8 to 8.8 ppm. Reduced chemical shift dispersion in the 1H dimension is characteristic of IDRs compared to spectra for folded proteins.","type":"Results"},{"text":"Values for secondary chemical shifts were small (Supporting Information Fig. S3), suggesting that the ICL2 protein region exists predominantly as a random coil. Transient secondary structure populations for the disordered hZIP4 ICL2 were assessed using both the secondary structure propensity (SSP) score41 and the δ2D method.42 Both methods (Fig. 2) indicated that the ICL2 protein region is largely random coil with slight tendencies for regions of β‐strand between residues 460–469 and 484–490.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30793391","version":2,"reference_html":"Concomitant disorder and high-affinity zinc binding in the human zinc- and iron-regulated transport protein 4 intracellular loop. <i> Bafaro EM, Maciejewski MW, Hoch JC, Dempski RE. </i> Protein Sci, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":448,"region_id":"DP02554r002","start":431,"term_id":"GO:0046872","statement":[{"text":"Previously, the hZIP4 ICL2 was shown to coordinate two zinc ions with the first zinc binding at a CysHis3 site and the second zinc binding at a His4 site.19 The single cysteine residue (C436) was responsible for the nanomolar binding affinity of zinc to ICL2.","type":"Results"},{"text":"The 1H chemical shift peak dispersion of zinc‐bound ICL2 remained narrow, indicating that the protein remained disordered upon zinc binding. The most prominent change in the spectra upon zinc addition was the disappearance of cross‐peaks. Analysis of the peak heights [Fig. 3(b)] revealed a metal‐dependent signal broadening with cross‐peaks for residues in the histidine‐rich region (residues 431–448), exhibiting ~50% reduction in signal with one zinc bound and complete signal broadening in the presence of two molar equivalents of zinc. ","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30793391","version":3,"reference_html":"Concomitant disorder and high-affinity zinc binding in the human zinc- and iron-regulated transport protein 4 intracellular loop. <i> Bafaro EM, Maciejewski MW, Hoch JC, Dempski RE. </i> Protein Sci, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"metal ion binding","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":448,"region_id":"DP02554r003","start":431,"term_id":"GO:0140486","statement":[{"text":"The largest intracellular loop of ZIP4, ICL2, regulates the plasma membrane levels of the transporter in response to intracellular zinc levels.18 At low intracellular zinc concentrations, ZIP4 undergoes endocytosis from the plasma membrane, and as zinc concentrations increase, ZIP4 is ubiquitinated at the single lysine residue (K463) and proteolytically degraded.","type":"Discussion"},{"text":"The 1H chemical shift peak dispersion of zinc‐bound ICL2 remained narrow, indicating that the protein remained disordered upon zinc binding. The most prominent change in the spectra upon zinc addition was the disappearance of cross‐peaks. Analysis of the peak heights [Fig. 3(b)] revealed a metal‐dependent signal broadening with cross‐peaks for residues in the histidine‐rich region (residues 431–448), exhibiting ~50% reduction in signal with one zinc bound and complete signal broadening in the presence of two molar equivalents of zinc.","type":"Results"}],"curator_id":"fquaglia","released":"2022_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"30793391","version":4,"reference_html":"Concomitant disorder and high-affinity zinc binding in the human zinc- and iron-regulated transport protein 4 intracellular loop. <i> Bafaro EM, Maciejewski MW, Hoch JC, Dempski RE. </i> Protein Sci, 2019","date":"2022-12-06T11:27:47.078Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"zinc ion sequestering activity","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a zinc ion to prevent it from interacting with sensitive components of a biological system.\" [PMID:12050156]","disprot_namespace":"Disorder function","term_is_binding":false},{"term_namespace":"Structural state","ec_ontology":"ECO","end":498,"region_id":"DP02554r004","start":424,"term_id":"IDPO:0000002","statement":[{"text":"Circular dichroism spectroscopy revealed that the M3M4 domain is intrinsically disordered, with only a small structural change induced upon Zn(2+) coordination.","type":"Abstract"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"25882556","version":2,"reference_html":"The large intracellular loop of hZIP4 is an intrinsically disordered zinc binding domain. <i> Bafaro EM, Antala S, Nguyen TV, Dzul SP, Doyon B, Stemmler TL, Dempski RE. </i> Metallomics, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":448,"region_id":"DP02554r005","start":436,"term_id":"GO:0140486","statement":[{"text":"Using a combination of site-directed mutagenesis, metal binding affinity assays, and X-ray absorption spectroscopy, we demonstrated that the two Zn(2+) ions bind sequentially, with the first Zn(2+) binding to a CysHis3 site with a nanomolar binding affinity, and the second Zn(2+) binding to a His4 site with a weaker affinity.","type":"Abstract"},{"text":"Our data supports a model in which the intracellular M3M4 domain senses high cytosolic Zn(2+) concentrations and regulates the plasma membrane levels of the hZIP4 transporter in response to Zn(2+) binding.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_12","ec_name":"mutant phenotype evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"25882556","version":4,"reference_html":"The large intracellular loop of hZIP4 is an intrinsically disordered zinc binding domain. <i> Bafaro EM, Antala S, Nguyen TV, Dzul SP, Doyon B, Stemmler TL, Dempski RE. </i> Metallomics, 2015","date":"2022-12-06T11:27:58.927Z","reference_source":"pmid","ec_id":"ECO:0000315","term_name":"zinc ion sequestering activity","curator_orcid":"0000-0002-0341-4888","ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a zinc ion to prevent it from interacting with sensitive components of a biological system.\" [PMID:12050156]","disprot_namespace":"Disorder function","term_is_binding":false},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":448,"region_id":"DP02554r006","start":436,"term_id":"GO:0008270","statement":[{"text":"Using a combination of site-directed mutagenesis, metal binding affinity assays, and X-ray absorption spectroscopy, we demonstrated that the two Zn(2+) ions bind sequentially, with the first Zn(2+) binding to a CysHis3 site with a nanomolar binding affinity, and the second Zn(2+) binding to a His4 site with a weaker affinity.","type":"Abstract"},{"text":"Our data supports a model in which the intracellular M3M4 domain senses high cytosolic Zn(2+) concentrations and regulates the plasma membrane levels of the hZIP4 transporter in response to Zn(2+) binding.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_12","ec_name":"mutant phenotype evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"25882556","version":4,"reference_html":"The large intracellular loop of hZIP4 is an intrinsically disordered zinc binding domain. <i> Bafaro EM, Antala S, Nguyen TV, Dzul SP, Doyon B, Stemmler TL, Dempski RE. </i> Metallomics, 2015","date":"2022-12-06T11:29:20.841Z","reference_source":"pmid","ec_id":"ECO:0000315","term_name":"zinc ion binding","curator_orcid":"0000-0002-0341-4888","ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a zinc ion (Zn).\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","length":647,"ncbi_taxon_id":9606,"date":"2020-02-10T12:53:15.464Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF02535","name":"ZIP Zinc transporter","start":328,"end":638},{"id":"PF18292","name":"Zinc transporter ZIP4 domain","start":47,"end":196},{"id":"PF21116","name":"Zip protein EF-hand","start":202,"end":308}]},"disprot_id":"DP02554","regions_counter":6,"dataset":[],"UniParc":"UPI00000377A5","uniref100":"UniRef100_Q6P5W5","uniref90":"UniRef90_Q6P5W5","uniref50":"UniRef50_Q6P5W5","genes":[{"name":{"value":"SLC39A4"},"synonyms":[{"value":"ZIP4"}]}],"alphafold_very_low_content":0.1901081916537867,"disorder_content":0.11591962905718702,"disprot_consensus":{"full":[{"start":424,"end":498,"type":"D"}],"Structural state":[{"start":424,"end":498,"type":"D"}],"Molecular function":[{"start":431,"end":448,"type":"F"}]}},{"acc":"Q15109","name":"Advanced glycosylation end product-specific receptor","sequence":"MAAGTAVGAWVLVLSLWGAVVGAQNITARIGEPLVLKCKGAPKKPPQRLEWKLNTGRTEAWKVLSPQGGGPWDSVARVLPNGSLFLPAVGIQDEGIFRCQAMNRNGKETKSNYRVRVYQIPGKPEIVDSASELTAGVPNKVGTCVSEGSYPAGTLSWHLDGKPLVPNEKGVSVKEQTRRHPETGLFTLQSELMVTPARGGDPRPTFSCSFSPGLPRHRALRTAPIQPRVWEPVPLEEVQLVVEPEGGAVAPGGTVTLTCEVPAQPSPQIHWMKDGVPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRAVSISIIEPGEEGPTAGSVGGSGLGTLALALGILGGLGTAALLIGVILWQRRQRRGEERKAPENQEEEEERAELNQSEEPEAGESSTGGP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":404,"region_id":"DP02555r001","start":364,"term_id":"IDPO:0000002","statement":[{"text":"The 2D 1H–15N HSQC spectra of the peptide show a poor spreading of the signals, as commonly observed for unfolded proteins","type":"Results"},{"text":"Secondary structure prediction was carried out with the program TALOS+ (Shen et al. 2009) using the HN, N, C′, Cα, Hα and Cβ chemical shift values as input data. The prediction suggests a random-coil conformation for the whole sequence with all the residues experiencing high mobility. Further and more detailed information on the dynamics of cytRAGE were provided by relaxation data. In particular, the characterization of fast motions occurring on picosecond-nanosecond time scales was performed by exploiting the spin relaxation properties of the amide 15N nuclei through R1, R2, and NOE experiments (see Fig. 3a, c, e). Random-coil polypeptides and flexible protein regions are characterized by fast local motions with NOE values below 0.5 or negative. In our construct of cytRAGE, that includes also three aminoacids of the transmembrane region and two of the thrombin cleavage site, the heteronuclear NOEs for all amino acids are close to zero or even negative at the C-terminal region (Fig. 3e). These NOE values indicate that all the isolated cytRAGE is highly flexible and unfolded in solution.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"23001324","version":2,"reference_html":"NMR characterization of the C-terminal tail of full-length RAGE in a membrane mimicking environment. <i> Borsi V, Cerofolini L, Fragai M, Luchinat C. </i> J Biomol NMR, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P27361","partner_end":null},{"partner_start":null,"db":"UniProt","id":"P58753","partner_end":null},{"partner_start":null,"db":"UniProt","id":"Q99836","partner_end":null}],"ec_ontology":"ECO","end":404,"region_id":"DP02555r002","start":364,"term_id":"GO:0005515","statement":[{"text":"cytRAGE is reported to bind different intracellular proteins such as mDia-1(Rai et al. 2012), ERK-1/2 (Ishihara et al. 2003) and after phosphorylation by PKCξ, TIRAP and MyD88 (Sakaguchi et al. 2011).","type":"Discussion"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"23001324","version":3,"reference_html":"NMR characterization of the C-terminal tail of full-length RAGE in a membrane mimicking environment. <i> Borsi V, Cerofolini L, Fragai M, Luchinat C. </i> J Biomol NMR, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"protein binding","curator_orcid":"0000-0003-0849-9312","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":404,"region_id":"DP02555r003","start":364,"term_id":"GO:0060090","statement":[{"text":"The cytoplasmic domain of RAGE (C-terminal RAGE; ctRAGE) is critical for RAGE-dependent signal transduction. As the most membrane-proximal event, mDia1 binds to ctRAGE, and it is essential for RAGE ligand-stimulated phosphorylation of AKT and cell proliferation/migration. We show that ctRAGE contains an unusual α-turn that mediates the mDia1-ctRAGE interaction and is required for RAGE-dependent signaling.","type":"Abstract"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"22194616","version":3,"reference_html":"Signal transduction in receptor for advanced glycation end products (RAGE): solution structure of C-terminal rage (ctRAGE) and its binding to mDia1. <i> Rai V, Maldonado AY, Burz DS, Reverdatto S, Yan SF, Schmidt AM, Shekhtman A. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"2LMB"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":370,"region_id":"DP02555r004","start":364,"term_id":"GO:0005515","statement":[{"text":"When Arg-5 and Gln-6 are mutated to alanines, the loss of the binding epitope for mDia1 suppresses RAGE ligand-induced downstream phosphorylation of AKT and migration and proliferation of vascular smooth muscle cells (SMCs).","type":"Introduction"},{"text":"To confirm the FH1-ctRAGE interaction surface, we made a ctRAGE double mutant in which residues Arg-5 and Gln-6 were changed to alanine to create R5A/Q6A-ctRAGE (Fig. 1A). Titrating unlabeled FH1 into [U-15N]R5A/Q6A-ctRAGE resulted only in small (<0.02 ppm) changes in the position of one amino acid residue, Arg-10. No other chemical shift changes or substantial broadening of the R5A/Q6A-ctRAGE peaks were observed, suggesting that the double mutant interacts with FH1 very weakly, with a KD well above 1 mm","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"mutant phenotype evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"22194616","version":3,"reference_html":"Signal transduction in receptor for advanced glycation end products (RAGE): solution structure of C-terminal rage (ctRAGE) and its binding to mDia1. <i> Rai V, Maldonado AY, Burz DS, Reverdatto S, Yan SF, Schmidt AM, Shekhtman A. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000315","term_name":"protein binding","curator_orcid":"0000-0003-0849-9312","ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":404,"region_id":"DP02555r005","start":364,"term_id":"IDPO:0000002","statement":[{"text":"The 15N HSQC spectrum of ctRAGE is well resolved but has limited chemical shift dispersion (Fig. 1B), indicating that the majority of the ctRAGE residues are disordered. ","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"22194616","version":2,"reference_html":"Signal transduction in receptor for advanced glycation end products (RAGE): solution structure of C-terminal rage (ctRAGE) and its binding to mDia1. <i> Rai V, Maldonado AY, Burz DS, Reverdatto S, Yan SF, Schmidt AM, Shekhtman A. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":370,"region_id":"DP02555r006","start":364,"term_id":"GO:0005515","statement":[{"text":"Titrating unlabeled FH1 into uniformly 15N-labeled ctRAGE, [U-15N]ctRAGE, resulted in specific changes in the HSQC spectrum of ctRAGE","type":"Results"},{"text":"These changes suggest that residues Gln-3 through Gln-6 participate in the interaction with FH1. Peak broadening is characteristic of slow to intermediate exchange and suggests that the dissociation constant of the interaction Kd is <10 μm","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"22194616","version":3,"reference_html":"Signal transduction in receptor for advanced glycation end products (RAGE): solution structure of C-terminal rage (ctRAGE) and its binding to mDia1. <i> Rai V, Maldonado AY, Burz DS, Reverdatto S, Yan SF, Schmidt AM, Shekhtman A. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"protein binding","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":393,"region_id":"DP02555r007","start":389,"term_id":"IDPO:0000045","statement":[{"text":"the cytoplasmic domain of RAGE is phosphorylated at Ser391 by PKCζ upon binding of ligands. TIRAP and MyD88, which are known to be adaptor proteins for Toll-like receptor-2 and -4 (TLR2/4), bound to the phosphorylated RAGE and transduced a signal to downstream molecules.","type":"Abstract"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"protein kinase assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"21829704","version":2,"reference_html":"TIRAP, an adaptor protein for TLR2/4, transduces a signal from RAGE phosphorylated upon ligand binding. <i> Sakaguchi M, Murata H, Yamamoto K, Ono T, Sakaguchi Y, Motoyama A, Hibino T, Kataoka K, Huh NH. </i> PLoS One, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007687","term_name":"phosphorylation display site","curator_orcid":"0000-0003-0849-9312","ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":404,"region_id":"DP02555r008","start":364,"term_id":"GO:0060090","statement":[{"text":"cytRAGE is reported to bind different intracellular proteins such as mDia-1(Rai et al. 2012), ERK-1/2 (Ishihara et al. 2003) and after phosphorylation by PKCξ, TIRAP and MyD88 (Sakaguchi et al. 2011).","type":"Discussion"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"23001324","version":3,"reference_html":"NMR characterization of the C-terminal tail of full-length RAGE in a membrane mimicking environment. <i> Borsi V, Cerofolini L, Fragai M, Luchinat C. </i> J Biomol NMR, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"molecular adaptor activity","curator_orcid":"0000-0003-0849-9312","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","length":404,"ncbi_taxon_id":9606,"date":"2020-02-10T14:02:25.594Z","organism":"Homo sapiens","features":{"gene3D":[{"start":234,"end":323,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":234,"end":323,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":234,"end":323,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"}],"pfam":[{"id":"PF08205","name":"CD80-like C2-set immunoglobulin domain","start":124,"end":218},{"id":"PF13927","name":"Immunoglobulin domain","start":240,"end":304}]},"disprot_id":"DP02555","regions_counter":8,"dataset":[],"UniParc":"UPI00001330EF","uniref100":"UniRef100_Q15109","uniref90":"UniRef90_Q15109","uniref50":"UniRef50_Q15109","genes":[{"name":{"value":"AGER"},"synonyms":[{"value":"RAGE"}]}],"alphafold_very_low_content":0.12128712871287128,"disorder_content":0.10148514851485149,"disprot_consensus":{"full":[{"start":364,"end":404,"type":"D"}],"Structural state":[{"start":364,"end":404,"type":"D"}],"Molecular function":[{"start":364,"end":404,"type":"F"}],"Disorder function":[{"start":389,"end":393,"type":"F"}]}},{"acc":"P09077","name":"Homeotic protein Sex combs reduced","sequence":"MDPDCFAMSSYQFVNSLASCYPQQMNPQQNHPGAGNSSAGGSGGGAGGSGGVVPSGGTNGGQGSAGAATPGANDYFPAAAAYTPNLYPNTPQAHYANQAAYGGQGNPDMVDYTQLQPQRLLLQQQQQQQQQQHAHAAAAVAAQQQQQLAQQQHPQQQQQQQQANISCKYANDPVTPGGSGGGGVSGSNNNNNSANSNNNNSQSLASPQDLSTRDISPKLSPSSVVESVARSLNKGVLGGSLAAAAAAAGLNNNHSGSGVSGGPGNVNVPMHSPGGGDSDSESDSGNEAGSSQNSGNGKKNPPQIYPWMKRVHLGTSTVNANGETKRQRTSYTRYQTLELEKEFHFNRYLTRRRRIEIAHALCLTERQIKIWFQNRRMKWKKEHKMASMNIVPYHMGPYGHPYHQFDIHPSQFAHLSA","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"creator":"rpancsa","regions":[{"region_id":"DP02556r001","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:10:05.945Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":331,"term_id":"IDPO:0000002","start":298,"version":2,"statement":[{"text":"We have completely assigned the 1H, 13C, and 15N chemical shifts of the backbone atoms of SCRK298–K384 and DFDT337–K426 by solution NMR spectroscopy. Chemical shift-based secondary structure prediction and 15N dynamic studies show that ~ 30 residues in the N-terminus are completely disordered, while the DNA-binding homeodomain is properly folded in both proteins. Reduced spectral density analysis of the 15N dynamics data revealed variations in flexibility in the disordered region.","type":"Introduction"},{"text":"The N-terminal residues of both proteins (SCR: K298 to Y331; DFD: T337 to T374) show lack of secondary structure, highlighting their highly flexible nature.","type":"Results"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2023_12","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30802457","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"27622"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"rpancsa","reference_html":"Dynamic Studies on Intrinsically Disordered Regions of Two Paralogous Transcription Factors Reveal Rigid Segments with Important Biological Functions. <i> Maiti S, Acharya B, Boorla VS, Manna B, Ghosh A, De S. </i> J Mol Biol, 2019","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02556r002","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:10:05.211Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":310,"term_id":"GO:0005515","start":305,"version":3,"statement":[{"text":"Interestingly, one of these segments of rigid residues is conserved in both SCR and DFD, and using NMR titration experiments, we show that this rigid segment is specifically recognized by a co-transcription factor Extradenticle (EXD).","type":"Introduction"},{"text":"Unlabeled homeodomain of EXDA238–I300 (residues A238 toI300) was titrated into15N-labeled SCRK298–K384 or DFDT337–K426, and each titration point was monitored by 15N–1H HSQC experiment (Figs. 6and S4). Consecutive residues Y305 to R310 (P306 lacks backbone NH) in the rigid segment of SCRK298–K384 showed significant chemical shift changes","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P40427","partner_end":null}],"term_name":"protein binding","reference_html":"Dynamic Studies on Intrinsically Disordered Regions of Two Paralogous Transcription Factors Reveal Rigid Segments with Important Biological Functions. <i> Maiti S, Acharya B, Boorla VS, Manna B, Ghosh A, De S. </i> J Mol Biol, 2019","released":"2023_12","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30802457","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"27622"}],"term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"rpancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02556r003","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:10:04.423Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":310,"term_id":"GO:0098772","start":305,"version":3,"statement":[{"text":"Interestingly, one of these segments of rigid residues is conserved in both SCR and DFD, and using NMR titration experiments, we show that this rigid segment is specifically recognized by a co-transcription factor Extradenticle (EXD).","type":"Introduction"},{"text":"Unlabeled homeodomain of EXDA238–I300 (residues A238 toI300) was titrated into15N-labeled SCRK298–K384 or DFDT337–K426, and each titration point was monitored by 15N–1H HSQC experiment (Figs. 6and S4). Consecutive residues Y305 to R310 (P306 lacks backbone NH) in the rigid segment of SCRK298–K384 showed significant chemical shift changes","type":"Results"},{"text":"For SCR, it has been shown that the homeodomain and its preceding~30 residues are sufficient to carry out most of its in vivo functions such as homeotic transformations,transcriptional regulation, and protein–protein interactions[14]. Moreover, these N-terminal 30 residues have been shown to regulate the functional specificities in both SCR and DFD [15].","type":"Introduction"}],"term_name":"molecular function regulator","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2023_12","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30802457","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"27622"}],"term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"rpancsa","reference_html":"Dynamic Studies on Intrinsically Disordered Regions of Two Paralogous Transcription Factors Reveal Rigid Segments with Important Biological Functions. <i> Maiti S, Acharya B, Boorla VS, Manna B, Ghosh A, De S. </i> J Mol Biol, 2019","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2023_12","length":417,"ncbi_taxon_id":7227,"date":"2020-02-10T14:42:03.752Z","organism":"Drosophila melanogaster","features":{"gene3D":[],"pfam":[{"id":"PF00046","name":"Homeodomain","start":325,"end":381}]},"disprot_id":"DP02556","regions_counter":3,"dataset":[],"UniParc":"UPI00001356B3","uniref100":"UniRef100_P09077","uniref90":"UniRef90_P09077","uniref50":"UniRef50_P09077","genes":[{"name":{"value":"Scr"},"orfNames":[{"value":"CG1030"}]}],"alphafold_very_low_content":0.4676258992805755,"disorder_content":0.0815347721822542,"disprot_consensus":{"full":[{"start":298,"end":331,"type":"D"}],"Structural state":[{"start":298,"end":331,"type":"D"}],"Molecular function":[{"start":305,"end":310,"type":"F"}]}},{"acc":"P07548","name":"Homeotic protein deformed","sequence":"MSSFLMGYPHAPHHVQSPMSMGNGLDPKFPPLADDYHHYNGHYSMTASTGHMSGAVGGGAGVGSVGGGGAGGMTGHPHSMHPADMVSDYMAHHHNPHSHSHSHTHSLPHHHSNSAISGHHQASAGGYSSNYANATPPSHPHSHPHAHPHQSLGYYVHHAPEFISAGAVHSDPTNGYGPAANVPNTSNGGGGGGSGAVLGGGAVGGSANGYYGGYGGGYGTANGSVGSTHSQGHSPHSQMMDLPLQCSSTEPPTNTALGLQELGLKLEKRIEEAVPAGQQLQELGMRLRCDDMGSENDDMSEEDRLMLDRSPDELGSNDNDDDLGDSDSDEDLMAETTDGERIIYPWMKKIHVAGVANGSYQPGMEPKRQRTAYTRHQILELEKEFHYNRYLTRRRRIEIAHTLVLSERQIKIWFQNRRMKWKKDNKLPNTKNVRKKTVDANGNPTPVAKKPTKRAASKKQQQAQQQQQSQQQQTQQTPVMNECIRSDSLESIGDVSSSLGNPPYIPAAPETTSSYPGSQQHLSNNNNNGSGNNNNNNNNNNSNLNNNNNNNQMGHTNLHGHLQQQQSDLMTNLQLHIKQDYDLTAL","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"creator":"rpancsa","regions":[{"region_id":"DP02557r001","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:10:27.663Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":374,"term_id":"IDPO:0000002","start":337,"version":2,"statement":[{"text":"We have completely assigned the 1H, 13C, and 15N chemical shifts of the backbone atoms of SCRK298–K384 and DFDT337–K426 by solution NMR spectroscopy. Chemical shift-based secondary structure prediction and 15N dynamic studies show that ~ 30 residues in the N-terminus are completely disordered, while the DNA-binding homeodomain is properly folded in both proteins. Reduced spectral density analysis of the 15N dynamics data revealed variations in flexibility in the disordered region.","type":"Introduction"},{"text":"The N-terminal residues of both proteins (SCR: K298 to Y331; DFD: T337 to T374) show lack of secondary structure, highlighting their highly flexible nature.","type":"Results"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2023_12","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30802457","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"27621"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"rpancsa","reference_html":"Dynamic Studies on Intrinsically Disordered Regions of Two Paralogous Transcription Factors Reveal Rigid Segments with Important Biological Functions. <i> Maiti S, Acharya B, Boorla VS, Manna B, Ghosh A, De S. </i> J Mol Biol, 2019","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02557r002","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:10:28.361Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":349,"term_id":"GO:0005515","start":341,"version":3,"statement":[{"text":"Interestingly, one of these segments of rigid residues is conserved in both SCR and DFD, and using NMR titration experiments, we show that this rigid segment is specifically recognized by a co-transcription factor Extradenticle (EXD).","type":"Introduction"},{"text":"Similarly, the stretch of residues R341 to K349 (P345 lacks backbone NH) in the rigid segment of DFDT337–K426 showed significant chemical shift changes (Fig. 6b). The remaining residues of both SCRK298–K384 and DFDT337–K426 have no significant chemical shift perturbation, indicating a very specific interaction between the rigid segment of the HOX proteins and EXD","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P40427","partner_end":null}],"term_name":"protein binding","reference_html":"Dynamic Studies on Intrinsically Disordered Regions of Two Paralogous Transcription Factors Reveal Rigid Segments with Important Biological Functions. <i> Maiti S, Acharya B, Boorla VS, Manna B, Ghosh A, De S. </i> J Mol Biol, 2019","released":"2023_12","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30802457","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"27621"}],"term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"rpancsa","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02557r003","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:10:29.278Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":349,"term_id":"GO:0060090","start":341,"version":3,"statement":[{"text":"Interestingly, one of these segments of rigid residues is conserved in both SCR and DFD, and using NMR titration experiments, we show that this rigid segment is specifically recognized by a co-transcription factor Extradenticle (EXD).","type":"Introduction"},{"text":"Similarly, the stretch of residues R341 to K349 (P345 lacks backbone NH) in the rigid segment of DFDT337–K426 showed significant chemical shift changes (Fig. 6b). The remaining residues of both SCRK298–K384 and DFDT337–K426 have no significant chemical shift perturbation, indicating a very specific interaction between the rigid segment of the HOX proteins and EXD","type":"Results"}],"term_name":"molecular adaptor activity","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2023_12","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30802457","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"27621"}],"term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"rpancsa","reference_html":"Dynamic Studies on Intrinsically Disordered Regions of Two Paralogous Transcription Factors Reveal Rigid Segments with Important Biological Functions. <i> Maiti S, Acharya B, Boorla VS, Manna B, Ghosh A, De S. </i> J Mol Biol, 2019","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2023_12","length":586,"ncbi_taxon_id":7227,"date":"2020-02-10T14:58:12.257Z","organism":"Drosophila melanogaster","features":{"gene3D":[],"pfam":[{"id":"PF00046","name":"Homeodomain","start":367,"end":423}]},"disprot_id":"DP02557","regions_counter":3,"dataset":[],"UniParc":"UPI000012C9D8","uniref100":"UniRef100_P07548","uniref90":"UniRef90_P07548","uniref50":"UniRef50_P07548","genes":[{"name":{"value":"Dfd"},"orfNames":[{"value":"CG2189"}]}],"alphafold_very_low_content":0.5580204778156996,"disorder_content":0.06484641638225255,"disprot_consensus":{"full":[{"start":337,"end":374,"type":"D"}],"Structural state":[{"start":337,"end":374,"type":"D"}],"Molecular function":[{"start":341,"end":349,"type":"F"}]}},{"acc":"Q9NP70","name":"Ameloblastin","sequence":"MSASKIPLFKMKDLILILCLLEMSFAVPFFPQQSGTPGMASLSLETMRQLGSLQRLNTLSQYSRYGFGKSFNSLWMHGLLPPHSSLPWMRPREHETQQYEYSLPVHPPPLPSQPSLKPQQPGLKPFLQSAAATTNQATALKEALQPPIHLGHLPLQEGELPLVQQQVAPSDKPPKPELPGVDFADPQGPSLPGMDFPDPQGPSLPGLDFADPQGSTIFQIARLISHGPMPQNKQSPLYPGMLYVPFGANQLNAPARLGIMSSEEVAGGREDPMAYGAMFPGFGGMRPGFEGMPHNPAMGGDFTLEFDSPVAATKGPENEEGGAQGSPMPEANPDNLENPAFLTELEPAPHAGLLALPKDDIPGLPRSPSGKMKGLPSVTPAAADPLMTPELADVYRTYDADMTTSVDFQEEATMDTTMAPNSLQTSMPGNKAQEPEMMHDAWHFQEP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":447,"region_id":"DP02558r001","start":223,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The broadest peak (with a half‐width spanning interval of approximately 90 nm), corresponding to hrAMBN‐Cter, illustrates clearly the disordered nature of the C‐terminus and the huge spectrum of its structural forms.","type":"Results"}],"curator_id":"rpancsa","released":"2023_06","ec_name":"dynamic light scattering assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"22243255","version":2,"reference_html":"Biophysical characterization of recombinant human ameloblastin. <i> Wald T, Bednárová L, Osička R, Pachl P, Sulc M, Lyngstadaas SP, Slaby I, Vondrášek J. </i> Eur J Oral Sci, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007064","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:11:44.007Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":62,"end":98,"reference_id":"23782691","reference_source":"pmid","reference_html":"Intrinsically disordered enamel matrix protein ameloblastin forms ribbon-like supramolecular structures via an N-terminal segment encoded by exon 5. <i> Wald T, Osickova A, Sulc M, Benada O, Semeradtova A, Rezabkova L, Veverka V, Bednarova L, Maly J, Macek P, Sebo P, Slaby I, Vondrasek J, Osicka R. </i> J Biol Chem, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP02558r002","statement":[{"text":"no well defined elements of regular secondary structure were observed in the CD spectra of the synthetic peptide encompassing residues 36–72 (peptide 36–72) of AMBN","type":"Results"},{"text":"There is a shift in residue numbering due to the lack of signal peptide of 26 residues in the studied protein construct.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:11:44.701Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":62,"end":98,"reference_id":"23782691","reference_source":"pmid","reference_html":"Intrinsically disordered enamel matrix protein ameloblastin forms ribbon-like supramolecular structures via an N-terminal segment encoded by exon 5. <i> Wald T, Osickova A, Sulc M, Benada O, Semeradtova A, Rezabkova L, Veverka V, Bednarova L, Maly J, Macek P, Sebo P, Slaby I, Vondrasek J, Osicka R. </i> J Biol Chem, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006317","ec_ontology":"ECO","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP02558r003","statement":[{"text":"In addition, thermal denaturation CD experiments with peptide 36–72 showed profiles characteristic for IDPs","type":"Results"},{"text":"There is a shift in residue numbering due to the lack of signal peptide of 26 residues in the studied protein construct.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:11:46.239Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":62,"end":98,"reference_id":"23782691","reference_source":"pmid","reference_html":"Intrinsically disordered enamel matrix protein ameloblastin forms ribbon-like supramolecular structures via an N-terminal segment encoded by exon 5. <i> Wald T, Osickova A, Sulc M, Benada O, Semeradtova A, Rezabkova L, Veverka V, Bednarova L, Maly J, Macek P, Sebo P, Slaby I, Vondrasek J, Osicka R. </i> J Biol Chem, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":3,"region_id":"DP02558r004","statement":[{"text":"Electron microscopy revealed that the AMBN high molecular mass self-assemblies were flat ribbon-like supramolecular structures with an average width of 18 ± 4 nm and with a variable size, ranging from tens to hundreds of nanometers in length","type":"Results"},{"text":"This clearly shows that the segment encompassing residues 36–72 confers the self-assembly capacity of AMBN.","type":"Results"},{"text":"There is a shift in residue numbering due to the lack of signal peptide of 26 residues in the studied protein construct.","type":"Curator statement"},{"text":"Here we observed that AMBN self-associates into ribbon-like supramolecular structures and that this self-assembly process is abolished by the deletion of the 37 residues long segment 36–72 located in the N-terminal portion of the molecule.","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:11:55.759Z"},"ec_go":"IDA","disprot_namespace":"Disorder function"},{"start":27,"end":447,"reference_id":"22243255","reference_source":"pmid","reference_html":"Biophysical characterization of recombinant human ameloblastin. <i> Wald T, Bednárová L, Osička R, Pachl P, Sulc M, Lyngstadaas SP, Slaby I, Vondrášek J. </i> Eur J Oral Sci, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP02558r005","statement":[{"text":"The disordered character of all the studied molecules becomes apparent when compared with the DLS profile of BSA.","type":"Results"},{"text":"One of the studied molecules was full-length ameloblastin, so it is stated to be disordered. Figure 5 shows large difference between the DLS curves of the ameloblastin constructs and that of BSA. Also, Trhoughout the paper the authors emphasize that the disordered, acidic C-terminus has a stronger effect on the structure of the full protein than the slightly more ordered N-terminal half.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:11:47.930Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":220,"end":225,"reference_id":"22243255","reference_source":"pmid","reference_html":"Biophysical characterization of recombinant human ameloblastin. <i> Wald T, Bednárová L, Osička R, Pachl P, Sulc M, Lyngstadaas SP, Slaby I, Vondrášek J. </i> Eur J Oral Sci, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000048","term_name":"limited proteolysis display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP02558r006","statement":[{"text":"All analyses and modelling data were in agreement with earlier experimental  observations  that  tooth-specific  proteases (enamelysin and kallikrein) separate the basic N-terminus from the acidic C-terminal region of the AMBN molecule.","type":"Introduction"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T15:08:34.014Z"},"disprot_namespace":"Disorder function"},{"start":27,"end":447,"reference_id":"22243255","reference_source":"pmid","reference_html":"Biophysical characterization of recombinant human ameloblastin. <i> Wald T, Bednárová L, Osička R, Pachl P, Sulc M, Lyngstadaas SP, Slaby I, Vondrášek J. </i> Eur J Oral Sci, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP02558r007","statement":[{"text":"The CD spectra of all three AMBN molecules at physiological temperature did not provide a clear signal of a dominant and well-profiled structure.","type":"Results"},{"text":"One of the three AMBN constructs studied was the full-lengh protein.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:11:51.175Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2023_06","length":447,"ncbi_taxon_id":9606,"date":"2020-02-10T16:38:15.633Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF05111","name":"Ameloblastin precursor (Amelin)","start":11,"end":191},{"id":"PF05111","name":"Ameloblastin precursor (Amelin)","start":199,"end":447}]},"disprot_id":"DP02558","regions_counter":7,"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000000DCCB","uniref100":"UniRef100_Q9NP70","uniref90":"UniRef90_Q9NP70","uniref50":"UniRef50_Q9NP70","genes":[{"name":{"value":"AMBN"}}],"alphafold_very_low_content":0.8702460850111857,"disorder_content":0.941834451901566,"disprot_consensus":{"full":[{"start":27,"end":447,"type":"D"}],"Structural state":[{"start":27,"end":447,"type":"D"}],"Disorder function":[{"start":62,"end":98,"type":"F"},{"start":220,"end":225,"type":"F"}]}},{"acc":"Q969R2","name":"Oxysterol-binding protein 2","sequence":"MGKAAAPSRGGGCGGRSRGLSSLFTVVPCLSCHTAAPGMSASTSGSGPEPKPQPQPVPEPERGPLSEQVSEAVSEAVPRSEPVSETTSEPEPGAGQPSELLQGSRPGSESSSGVGAGPFTKAASEPLSRAVGSATFLRPESGSLPALKPLPLLRPGQAKTPLGVPMSGTGTTSSAPLALLPLDSFEGWLLKWTNYLKGYQRRWFVLGNGLLSYYRNQGEMAHTCRGTINLSTAHIDTEDSCGILLTSGARSYHLKASSEVDRQQWITALELAKAKAVRVMNTHSDDSGDDDEATTPADKSELHHTLKNLSLKLDDLSTCNDLIAKHGAALQRSLTELDGLKIPSESGEKLKVVNERATLFRITSNAMINACRDFLELAEIHSRKWQRALQYEQEQRVHLEETIEQLAKQHNSLERAFHSAPGRPANPSKSFIEGSLLTPKGEDSEEDEDTEYFDAMEDSTSFITVITEAKEDSRKAEGSTGTSSVDWSSADNVLDGASLVPKGSSKVKRRVRIPNKPNYSLNLWSIMKNCIGRELSRIPMPVNFNEPLSMLQRLTEDLEYHHLLDKAVHCTSSVEQMCLVAAFSVSSYSTTVHRIAKPFNPMLGETFELDRLDDMGLRSLCEQVSHHPPSAAHYVFSKHGWSLWQEITISSKFRGKYISIMPLGAIHLEFQASGNHYVWRKSTSTVHNIIVGKLWIDQSGDIEIVNHKTNDRCQLKFLPYSYFSKEAARKVTGVVSDSQGKAHYVLSGSWDEQMECSKVMHSSPSSPSSDGKQKTVYQTLSAKLLWKKYPLPENAENMYYFSELALTLNEHEEGVAPTDSRLRPDQRLMEKGRWDEANTEKQRLEEKQRLSRRRRLEACGPGSSCSSEEEKEADAYTPLWFEKRLDPLTGEMACVYKGGYWEAKEKQDWHMCPNIF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":184,"region_id":"DP02559r001","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"In all cases, we observed that N-ter had a large impact on protein size, increasing the Stoke’s radius by ∼0.5 to 1 nm for OSBP constructs (OSBP versus ΔN-OSBP, N-PH-FFAT versus PH-FFAT, N-PH-ΔCC-FFAT versus PH-ΔCC-FFAT) and by ∼1.3 nm for ORP4 constructs (N-PH-FFAT versus PH-FFAT) (Figure 1D). This increase was about 2-fold higher than what was expected from the slope of the calibration curve, which was established with folded globular standards.","type":"Results"}],"curator_id":"rpancsa","released":"2023_12","ec_name":"chromatography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30905771","version":2,"reference_html":"An Intrinsically Disordered Region in OSBP Acts as an Entropic Barrier to Control Protein Dynamics and Orientation at Membrane Contact Sites. <i> Jamecna D, Polidori J, Mesmin B, Dezi M, Levy D, Bigay J, Antonny B. </i> Dev Cell, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:10:48.059Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Biological process","ec_ontology":"ECO","end":184,"region_id":"DP02559r002","start":1,"term_id":"GO:0051179","unpublished":true,"statement":[{"text":"ORP4 PH-FFAT showed significantly higher Golgi partitioning than ORP4 N-PH-FFAT (Figure 2B). Thus, the N-ter of OSBP and ORP4 reduce the Golgi membrane partitioning of these proteins.","type":"Results"}],"curator_id":"rpancsa","released":"2023_12","ec_name":"mutant phenotype evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30905771","version":3,"reference_html":"An Intrinsically Disordered Region in OSBP Acts as an Entropic Barrier to Control Protein Dynamics and Orientation at Membrane Contact Sites. <i> Jamecna D, Polidori J, Mesmin B, Dezi M, Levy D, Bigay J, Antonny B. </i> Dev Cell, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000315","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:10:48.572Z","curator_name":"Federica Quaglia"},"term_name":"localization","curator_orcid":"0000-0003-0849-9312","ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2023_12","length":916,"ncbi_taxon_id":9606,"date":"2020-02-10T17:13:07.143Z","organism":"Homo sapiens","features":{"gene3D":[{"start":182,"end":279,"id":"G3DSA:2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"}],"pfam":[{"id":"PF00169","name":"PH domain","start":185,"end":272},{"id":"PF01237","name":"Oxysterol-binding protein","start":522,"end":905}]},"disprot_id":"DP02559","regions_counter":2,"dataset":[],"UniParc":"UPI0000130EB2","uniref100":"UniRef100_Q969R2","uniref90":"UniRef90_Q969R2","uniref50":"UniRef50_Q969R2","genes":[{"name":{"value":"OSBP2"},"synonyms":[{"value":"KIAA1664"},{"value":"ORP4"},{"value":"OSBPL4"}]}],"alphafold_very_low_content":0.2925764192139738,"disorder_content":0.20087336244541484,"disprot_consensus":{"full":[{"start":1,"end":184,"type":"D"}],"Structural state":[{"start":1,"end":184,"type":"D"}],"Biological process":[{"start":1,"end":184,"type":"F"}]}},{"acc":"P60880","name":"Synaptosomal-associated protein 25","sequence":"MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTDLGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":141,"region_id":"DP02561r001","start":83,"term_id":"IDPO:0000002","statement":[{"text":"In general, the SNAP25 loop region is disordered in solution. ","type":"Discussion"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30916996","version":2,"reference_html":"Membrane-mediated disorder-to-order transition of SNAP25 flexible linker facilitates its interaction with syntaxin-1 and SNARE-complex assembly. <i> Jiang X, Zhang Z, Cheng K, Wu Q, Jiang L, Pielak GJ, Liu M, Li C. </i> FASEB J, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T17:32:46.654Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":141,"region_id":"DP02561r002","start":83,"term_id":"IDPO:0000002","statement":[{"text":"The hydrogen-deuterium exchange experiment shows that the hydrogen exchange rate of the residues in the middle part (107–131) is too fast to be detected in both buffer and bicelle. The hydrogen exchange rate of Nterminal residues is barely slower than C-terminal residues in buffer","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30916996","version":2,"reference_html":"Membrane-mediated disorder-to-order transition of SNAP25 flexible linker facilitates its interaction with syntaxin-1 and SNARE-complex assembly. <i> Jiang X, Zhang Z, Cheng K, Wu Q, Jiang L, Pielak GJ, Liu M, Li C. </i> FASEB J, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006196","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:02:28.348Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":110,"region_id":"DP02561r005","start":83,"term_id":"IDPO:0000011","statement":[{"text":"We then expressed the SNAP25 loop region alone to simplify the spectra and acquired the 1H-15N HSQC in buffer and liposomes (Fig. 3 B). Assignments were made by using standard triple resonance experiments (Supplemental Fig. S10 B). In the membrane, many cross peaks from the N-terminal of loop region were broadened beyond detection. The crosspeaks intensity ratios of the SNAP25 loop in buffer and liposomes (Fig. 3 C) also show that the cross-peak intensity decrease caused by membrane binding is localized to the N-terminal of the SNAP25 loop, especially the cysteine rich domain. ","type":"Results"},{"text":"First, membrane binding induces a disorder-to-order conformational transition of the SNAP25 loop involving the formation of an a-helix.","type":"Discussion"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30916996","version":2,"reference_html":"Membrane-mediated disorder-to-order transition of SNAP25 flexible linker facilitates its interaction with syntaxin-1 and SNARE-complex assembly. <i> Jiang X, Zhang Z, Cheng K, Wu Q, Jiang L, Pielak GJ, Liu M, Li C. </i> FASEB J, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder to order","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T17:33:45.235Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":141,"region_id":"DP02561r009","start":111,"term_id":"IDPO:0000045","statement":[{"text":"In this process, phosphorylation of the threonine (T)138 in the C-terminal of the SNAP25 loop influences the electrostatic interaction with syx-1, which explains how phosphorylation T138 mediates SNARE-complex assembly.","type":"Introduction"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30916996","version":2,"reference_html":"Membrane-mediated disorder-to-order transition of SNAP25 flexible linker facilitates its interaction with syntaxin-1 and SNARE-complex assembly. <i> Jiang X, Zhang Z, Cheng K, Wu Q, Jiang L, Pielak GJ, Liu M, Li C. </i> FASEB J, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"phosphorylation display site","curator_orcid":"0000-0003-0849-9312","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T17:36:14.234Z"}},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q16623","partner_end":null}],"ec_ontology":"ECO","end":141,"region_id":"DP02561r010","start":111,"term_id":"GO:0005515","statement":[{"text":"To determine whether the membrane-induced SNAP25 conformational change affects its interaction with syx-1, we acquired 1H-15N HSQC NMR spectra of uniformly enriched SNAP25 loop with or without unenriched syx-1 (1–264) in aqueous buffer and in liposomes (Fig. 6 A, B). Most of the spectrum is unchanged upon addition of syx-1 (1–264) in the buffer, but in liposomes, significant changes in signal intensities were observed in the C-terminal of the SNAP25 loop, and a number of resonances disappeared.","type":"Results"},{"text":"Second, the loop region mediates SNARE complex assembly through its interaction with the syx-1","type":"Discussion"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30916996","version":3,"reference_html":"Membrane-mediated disorder-to-order transition of SNAP25 flexible linker facilitates its interaction with syntaxin-1 and SNARE-complex assembly. <i> Jiang X, Zhang Z, Cheng K, Wu Q, Jiang L, Pielak GJ, Liu M, Li C. </i> FASEB J, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"protein binding","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T17:36:15.186Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":110,"region_id":"DP02561r011","start":83,"term_id":"GO:0008289","statement":[{"text":"We then expressed the SNAP25 loop region alone to simplify the spectra and acquired the 1H-15N HSQC in buffer and liposomes (Fig. 3 B). Assignments were made by using standard triple resonance experiments (Supplemental Fig. S10 B). In the membrane, many cross peaks from the N-terminal of loop region were broadened beyond detection. The crosspeaks intensity ratios of the SNAP25 loop in buffer and liposomes (Fig. 3 C) also show that the cross-peak intensity decrease caused by membrane binding is localized to the N-terminal of the SNAP25 loop, especially the cysteine rich domain.","type":"Results"},{"text":"First, membrane binding induces a disorder-to-order conformational transition of the SNAP25 loop involving the formation of an a-helix.","type":"Discussion"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30916996","version":3,"reference_html":"Membrane-mediated disorder-to-order transition of SNAP25 flexible linker facilitates its interaction with syntaxin-1 and SNARE-complex assembly. <i> Jiang X, Zhang Z, Cheng K, Wu Q, Jiang L, Pielak GJ, Liu M, Li C. </i> FASEB J, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"lipid binding","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T17:31:11.341Z"}}],"released":"2021_06","length":206,"ncbi_taxon_id":9606,"date":"2020-02-11T12:46:07.946Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF00835","name":"SNAP-25 family","start":91,"end":142},{"id":"PF05739","name":"SNARE domain","start":146,"end":202}]},"disprot_id":"DP02561","regions_counter":11,"dataset":["NDDs-related proteins"],"UniParc":"UPI0000001103","uniref100":"UniRef100_P60880","uniref90":"UniRef90_P60880","uniref50":"UniRef50_P60880","genes":[{"name":{"value":"SNAP25"},"synonyms":[{"value":"SNAP"}]}],"alphafold_very_low_content":0.10679611650485436,"disorder_content":0.28640776699029125,"disprot_consensus":{"full":[{"start":83,"end":110,"type":"T"},{"start":111,"end":141,"type":"D"}],"Structural state":[{"start":83,"end":141,"type":"D"}],"Structural transition":[{"start":83,"end":110,"type":"T"}],"Disorder function":[{"start":111,"end":141,"type":"F"}],"Molecular function":[{"start":83,"end":141,"type":"F"}]}},{"acc":"P10081","name":"ATP-dependent RNA helicase eIF4A","sequence":"MSEGITDIEESQIQTNYDKVVYKFDDMELDENLLRGVFGYGFEEPSAIQQRAIMPIIEGHDVLAQAQSGTGKTGTFSIAALQRIDTSVKAPQALMLAPTRELALQIQKVVMALAFHMDIKVHACIGGTSFVEDAEGLRDAQIVVGTPGRVFDNIQRRRFRTDKIKMFILDEADEMLSSGFKEQIYQIFTLLPPTTQVVLLSATMPNDVLEVTTKFMRNPVRILVKKDELTLEGIKQFYVNVEEEEYKYECLTDLYDSISVTQAVIFCNTRRKVEELTTKLRNDKFTVSAIYSDLPQQERDTIMKEFRSGSSRILISTDLLARGIDVQQVSLVINYDLPANKENYIHRIGRGGRFGRKGVAINFVTNEDVGAMRELEKFYSTQIEELPSDIATLLN","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"creator":"fquaglia","regions":[{"region_id":"DP02562r001","ec_ontology":"ECO","end":233,"term_id":"IDPO:0000002","start":223,"version":2,"statement":[{"text":"In these models, the distance from eIF4A residue 223 to residue 233 is  18 –20  Å,  which  can  be  accommodated  readily  by  the  linker polypeptide.","type":"Results"},{"text":"This structure and the intrinsic disorder of the carboxyl-terminal  domain  within  it  suggest  that,  in  solution,eIF4A can be a distended molecule and that the linker between domains  is  relatively  flexible  (although  it  does  not  have  an unusually  high  fraction  of  glycine,  alanine,  or  serine,  which  is characteristic  of  many  flexible  polypeptides).","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11087862","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1FUU"},{"db":"PDB","id":"1FUK"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase. <i> Caruthers JM, Johnson ER, McKay DB. </i> Proc Natl Acad Sci U S A, 2000","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02562r002","ec_ontology":"ECO","end":233,"term_id":"IDPO:0000033","start":223,"version":3,"statement":[{"text":"In these models, the distance from eIF4A residue 223 to residue 233 is  18 –20  Å,  which  can  be  accommodated  readily  by  the  linker polypeptide.","type":"Results"},{"text":"This structure and the intrinsic disorder of the carboxyl-terminal  domain  within  it  suggest  that,  in  solution,eIF4A can be a distended molecule and that the linker between domains  is  relatively  flexible  (although  it  does  not  have  an unusually  high  fraction  of  glycine,  alanine,  or  serine,  which  is characteristic  of  many  flexible  polypeptides).","type":"Results"}],"term_name":"flexible linker","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11087862","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1FUU"},{"db":"PDB","id":"1FUK"}],"term_namespace":"Disorder function","ec_id":"ECO:0005670","curator_id":"fquaglia","reference_html":"Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase. <i> Caruthers JM, Johnson ER, McKay DB. </i> Proc Natl Acad Sci U S A, 2000","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2020_12","length":395,"ncbi_taxon_id":559292,"date":"2020-02-11T16:30:57.949Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","features":{"gene3D":[],"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":47,"end":210},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":247,"end":355}]},"disprot_id":"DP02562","regions_counter":2,"dataset":[],"UniParc":"UPI000012D36B","uniref100":"UniRef100_A6ZQJ1","uniref90":"UniRef90_A6ZQJ1","uniref50":"UniRef50_Q10055","genes":[{"name":{"value":"TIF1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"2648398","url":"http://www.ncbi.nlm.nih.gov/pubmed/2648398","alternativeUrl":"https://europepmc.org/abstract/MED/2648398"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"3057442","url":"http://www.ncbi.nlm.nih.gov/pubmed/3057442","alternativeUrl":"https://europepmc.org/abstract/MED/3057442"}}]},"synonyms":[{"value":"TIF41A"}],"olnNames":[{"value":"YKR059W"}]},{"name":{"value":"TIF2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"2648398","url":"http://www.ncbi.nlm.nih.gov/pubmed/2648398","alternativeUrl":"https://europepmc.org/abstract/MED/2648398"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"3057442","url":"http://www.ncbi.nlm.nih.gov/pubmed/3057442","alternativeUrl":"https://europepmc.org/abstract/MED/3057442"}}]},"synonyms":[{"value":"TIF41B"}],"orfNames":[{"value":"J0660"}],"olnNames":[{"value":"YJL138C"}]}],"alphafold_very_low_content":0.015189873417721518,"disorder_content":0.027848101265822784,"disprot_consensus":{"full":[{"start":223,"end":233,"type":"D"}],"Structural state":[{"start":223,"end":233,"type":"D"}],"Disorder function":[{"start":223,"end":233,"type":"F"}]}},{"acc":"Q15717","name":"ELAV-like protein 1","sequence":"MSNGYEDHMAEDCRGDIGRTNLIVNYLPQNMTQDELRSLFSSIGEVESAKLIRDKVAGHSLGYGFVNYVTAKDAERAINTLNGLRLQSKTIKVSYARPSSEVIKDANLYISGLPRTMTQKDVEDMFSRFGRIINSRVLVDQTTGLSRGVAFIRFDKRSEAEEAITSFNGHKPPGSSEPITVKFAANPNQNKNVALLSQLYHSPARRFGGPVHHQAQRFRFSPMGVDHMSGLSGVNVPGNASSGWCIFIYNLGQDADEGILWQMFGPFGAVTNVKVIRDFNTNKCKGFGFVTMTNYEEAAMAIASLNGYRLGDKILQVSFKTNKSHK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"viglesias","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":19,"region_id":"DP02564r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"The first 19 amino acids form an N-terminal intrinsically disordered region that extends from the canonical RRM fold. The disordered nature of the N-terminal segment is supported by the absence of NOE-derived distances within this region. In addition, chemical shift-based secondary structure propensity analysis revealed no preferential secondary structure propensity","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30535889","version":2,"reference_html":"Oligomeric transition and dynamics of RNA binding by the HuR RRM1 domain in solution. <i> Lixa C, Mujo A, de Magalhães MTQ, Almeida FCL, Lima LMTR, Pinheiro AS. </i> J Biomol NMR, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"5SZW"}],"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-27T15:37:02.430Z"}}],"released":"2021_06","length":326,"ncbi_taxon_id":9606,"date":"2020-02-12T11:47:38.934Z","organism":"Homo sapiens","features":{"gene3D":[{"start":235,"end":326,"id":"G3DSA:3.30.70.330","name":"G3DSA:3.30.70.330"},{"start":235,"end":326,"id":"G3DSA:3.30.70.330","name":"G3DSA:3.30.70.330"},{"start":235,"end":326,"id":"G3DSA:3.30.70.330","name":"G3DSA:3.30.70.330"}],"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":22,"end":92},{"id":"PF00076","name":"RNA recognition motif","start":108,"end":174},{"id":"PF00076","name":"RNA recognition motif","start":246,"end":314}]},"disprot_id":"DP02564","regions_counter":1,"dataset":["Condensates-related proteins","RNA-binding proteins","Cancer-related proteins"],"UniParc":"UPI000004C562","uniref100":"UniRef100_Q15717","uniref90":"UniRef90_Q15717","uniref50":"UniRef50_Q15717","genes":[{"name":{"value":"ELAVL1"},"synonyms":[{"value":"HUR"}]}],"alphafold_very_low_content":0.2116564417177914,"disorder_content":0.05828220858895705,"disprot_consensus":{"full":[{"start":1,"end":19,"type":"D"}],"Structural state":[{"start":1,"end":19,"type":"D"}]}},{"acc":"P01266","name":"Thyroglobulin","sequence":"MALVLEIFTLLASICWVSANIFEYQVDAQPLRPCELQRETAFLKQADYVPQCAEDGSFQTVQCQNDGRSCWCVGANGSEVLGSRQPGRPVACLSFCQLQKQQILLSGYINSTDTSYLPQCQDSGDYAPVQCDVQQVQCWCVDAEGMEVYGTRQLGRPKRCPRSCEIRNRRLLHGVGDKSPPQCSAEGEFMPVQCKFVNTTDMMIFDLVHSYNRFPDAFVTFSSFQRRFPEVSGYCHCADSQGRELAETGLELLLDEIYDTIFAGLDLPSTFTETTLYRILQRRFLAVQSVISGRFRCPTKCEVERFTATSFGHPYVPSCRRNGDYQAVQCQTEGPCWCVDAQGKEMHGTRQQGEPPSCAEGQSCASERQQALSRLYFGTSGYFSQHDLFSSPEKRWASPRVARFATSCPPTIKELFVDSGLLRPMVEGQSQQFSVSENLLKEAIRAIFPSRGLARLALQFTTNPKRLQQNLFGGKFLVNVGQFNLSGALGTRGTFNFSQFFQQLGLASFLNGGRQEDLAKPLSVGLDSNSSTGTPEAAKKDGTMNKPTVGSFGFEINLQENQNALKFLASLLELPEFLLFLQHAISVPEDVARDLGDVMETVLSSQTCEQTPERLFVPSCTTEGSYEDVQCFSGECWCVNSWGKELPGSRVRGGQPRCPTDCEKQRARMQSLMGSQPAGSTLFVPACTSEGHFLPVQCFNSECYCVDAEGQAIPGTRSAIGKPKKCPTPCQLQSEQAFLRTVQALLSNSSMLPTLSDTYIPQCSTDGQWRQVQCNGPPEQVFELYQRWEAQNKGQDLTPAKLLVKIMSYREAASGNFSLFIQSLYEAGQQDVFPVLSQYPSLQDVPLAALEGKRPQPRENILLEPYLFWQILNGQLSQYPGSYSDFSTPLAHFDLRNCWCVDEAGQELEGMRSEPSKLPTCPGSCEEAKLRVLQFIRETEEIVSASNSSRFPLGESFLVAKGIRLRNEDLGLPPLFPPREAFAEQFLRGSDYAIRLAAQSTLSFYQRRRFSPDDSAGASALLRSGPYMPQCDAFGSWEPVQCHAGTGHCWCVDEKGGFIPGSLTARSLQIPQCPTTCEKSRTSGLLSSWKQARSQENPSPKDLFVPACLETGEYARLQASGAGTWCVDPASGEELRPGSSSSAQCPSLCNVLKSGVLSRRVSPGYVPACRAEDGGFSPVQCDQAQGSCWCVMDSGEEVPGTRVTGGQPACESPRCPLPFNASEVVGGTILCETISGPTGSAMQQCQLLCRQGSWSVFPPGPLICSLESGRWESQLPQPRACQRPQLWQTIQTQGHFQLQLPPGKMCSADYADLLQTFQVFILDELTARGFCQIQVKTFGTLVSIPVCNNSSVQVGCLTRERLGVNVTWKSRLEDIPVASLPDLHDIERALVGKDLLGRFTDLIQSGSFQLHLDSKTFPAETIRFLQGDHFGTSPRTWFGCSEGFYQVLTSEASQDGLGCVKCPEGSYSQDEECIPCPVGFYQEQAGSLACVPCPVGRTTISAGAFSQTHCVTDCQRNEAGLQCDQNGQYRASQKDRGSGKAFCVDGEGRRLPWWETEAPLEDSQCLMMQKFEKVPESKVIFDANAPVAVRSKVPDSEFPVMQCLTDCTEDEACSFFTVSTTEPEISCDFYAWTSDNVACMTSDQKRDALGNSKATSFGSLRCQVKVRSHGQDSPAVYLKKGQGSTTTLQKRFEPTGFQNMLSGLYNPIVFSASGANLTDAHLFCLLACDRDLCCDGFVLTQVQGGAIICGLLSSPSVLLCNVKDWMDPSEAWANATCPGVTYDQESHQVILRLGDQEFIKSLTPLEGTQDTFTNFQQVYLWKDSDMGSRPESMGCRKDTVPRPASPTEAGLTTELFSPVDLNQVIVNGNQSLSSQKHWLFKHLFSAQQANLWCLSRCVQEHSFCQLAEITESASLYFTCTLYPEAQVCDDIMESNAQGCRLILPQMPKALFRKKVILEDKVKNFYTRLPFQKLMGISIRNKVPMSEKSISNGFFECERRCDADPCCTGFGFLNVSQLKGGEVTCLTLNSLGIQMCSEENGGAWRILDCGSPDIEVHTYPFGWYQKPIAQNNAPSFCPLVVLPSLTEKVSLDSWQSLALSSVVVDPSIRHFDVAHVSTAATSNFSAVRDLCLSECSQHEACLITTLQTQPGAVRCMFYADTQSCTHSLQGQNCRLLLREEATHIYRKPGISLLSYEASVPSVPISTHGRLLGRSQAIQVGTSWKQVDQFLGVPYAAPPLAERRFQAPEPLNWTGSWDASKPRASCWQPGTRTSTSPGVSEDCLYLNVFIPQNVAPNASVLVFFHNTMDREESEGWPAIDGSFLAAVGNLIVVTASYRVGVFGFLSSGSGEVSGNWGLLDQVAALTWVQTHIRGFGGDPRRVSLAADRGGADVASIHLLTARATNSQLFRRAVLMGGSALSPAAVISHERAQQQAIALAKEVSCPMSSSQEVVSCLRQKPANVLNDAQTKLLAVSGPFHYWGPVIDGHFLREPPARALKRSLWVEVDLLIGSSQDDGLINRAKAVKQFEESRGRTSSKTAFYQALQNSLGGEDSDARVEAAATWYYSLEHSTDDYASFSRALENATRDYFIICPIIDMASAWAKRARGNVFMYHAPENYGHGSLELLADVQFALGLPFYPAYEGQFSLEEKSLSLKIMQYFSHFIRSGNPNYPYEFSRKVPTFATPWPDFVPRAGGENYKEFSELLPNRQGLKKADCSFWSKYISSLKTSADGAKGGQSAESEEEELTAGSGLREDLLSLQEPGSKTYSK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Disorder function","ec_ontology":"ECO","end":620,"region_id":"DP02567r001","start":610,"term_id":"IDPO:0000033","unpublished":true,"statement":[{"text":"In the TG monomer, the globular NTD is connected to the core region via a linker (residues 610–620) that crosses the central dimer interface and is partially flexible","type":"Article"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"cryogenic electron microscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"32025030","version":3,"reference_html":"The structure of human thyroglobulin. <i> Coscia F, Taler-Verčič A, Chang VT, Sinn L, O'Reilly FJ, Izoré T, Renko M, Berger I, Rappsilber J, Turk D, Löwe J. </i> Nature, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","cross_refs":[{"db":"PDB","id":"6SCJ"},{"db":"EMDB","id":"EMD-10141"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-08T17:38:43.056Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":620,"region_id":"DP02567r002","start":610,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"In the TG monomer, the globular NTD is connected to the core region via a linker (residues 610–620) that crosses the central dimer interface and is partially flexible","type":"Article"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"32025030","version":2,"reference_html":"The structure of human thyroglobulin. <i> Coscia F, Taler-Verčič A, Chang VT, Sinn L, O'Reilly FJ, Izoré T, Renko M, Berger I, Rappsilber J, Turk D, Löwe J. </i> Nature, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-08T17:38:38.896Z"}},{"start":1,"end":23,"reference_id":"32025030","reference_source":"pmid","reference_html":"The structure of human thyroglobulin. <i> Coscia F, Taler-Verčič A, Chang VT, Sinn L, O'Reilly FJ, Izoré T, Renko M, Berger I, Rappsilber J, Turk D, Löwe J. </i> Nature, 2020","date":"2022-08-08T17:44:14.996Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6SCJ"},{"db":"EMDB","id":"EMD-10141"}],"region_id":"DP02567r003","statement":[{"text":"The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]},{"start":388,"end":407,"reference_id":"32025030","reference_source":"pmid","reference_html":"The structure of human thyroglobulin. <i> Coscia F, Taler-Verčič A, Chang VT, Sinn L, O'Reilly FJ, Izoré T, Renko M, Berger I, Rappsilber J, Turk D, Löwe J. </i> Nature, 2020","date":"2022-08-08T17:44:27.008Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6SCJ"},{"db":"EMDB","id":"EMD-10141"}],"region_id":"DP02567r004","statement":[{"text":"The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]},{"start":511,"end":546,"reference_id":"32025030","reference_source":"pmid","reference_html":"The structure of human thyroglobulin. <i> Coscia F, Taler-Verčič A, Chang VT, Sinn L, O'Reilly FJ, Izoré T, Renko M, Berger I, Rappsilber J, Turk D, Löwe J. </i> Nature, 2020","date":"2022-08-08T17:44:38.339Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6SCJ"},{"db":"EMDB","id":"EMD-10141"}],"region_id":"DP02567r005","statement":[{"text":"The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]},{"start":830,"end":847,"reference_id":"32025030","reference_source":"pmid","reference_html":"The structure of human thyroglobulin. <i> Coscia F, Taler-Verčič A, Chang VT, Sinn L, O'Reilly FJ, Izoré T, Renko M, Berger I, Rappsilber J, Turk D, Löwe J. </i> Nature, 2020","date":"2022-08-08T17:44:51.805Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6SCJ"},{"db":"EMDB","id":"EMD-10141"}],"region_id":"DP02567r006","statement":[{"text":"The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]},{"start":1010,"end":1020,"reference_id":"32025030","reference_source":"pmid","reference_html":"The structure of human thyroglobulin. <i> Coscia F, Taler-Verčič A, Chang VT, Sinn L, O'Reilly FJ, Izoré T, Renko M, Berger I, Rappsilber J, Turk D, Löwe J. </i> Nature, 2020","date":"2022-08-08T17:45:02.131Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6SCJ"},{"db":"EMDB","id":"EMD-10141"}],"region_id":"DP02567r007","statement":[{"text":"The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]},{"start":1234,"end":1243,"reference_id":"32025030","reference_source":"pmid","reference_html":"The structure of human thyroglobulin. <i> Coscia F, Taler-Verčič A, Chang VT, Sinn L, O'Reilly FJ, Izoré T, Renko M, Berger I, Rappsilber J, Turk D, Löwe J. </i> Nature, 2020","date":"2022-08-08T17:45:14.792Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6SCJ"},{"db":"EMDB","id":"EMD-10141"}],"region_id":"DP02567r008","statement":[{"text":"The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]},{"start":1640,"end":1657,"reference_id":"32025030","reference_source":"pmid","reference_html":"The structure of human thyroglobulin. <i> Coscia F, Taler-Verčič A, Chang VT, Sinn L, O'Reilly FJ, Izoré T, Renko M, Berger I, Rappsilber J, Turk D, Löwe J. </i> Nature, 2020","date":"2022-08-08T17:45:26.196Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6SCJ"},{"db":"EMDB","id":"EMD-10141"}],"region_id":"DP02567r009","statement":[{"text":"The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]},{"start":1802,"end":1814,"reference_id":"32025030","reference_source":"pmid","reference_html":"The structure of human thyroglobulin. <i> Coscia F, Taler-Verčič A, Chang VT, Sinn L, O'Reilly FJ, Izoré T, Renko M, Berger I, Rappsilber J, Turk D, Löwe J. </i> Nature, 2020","date":"2022-08-08T17:45:36.235Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6SCJ"},{"db":"EMDB","id":"EMD-10141"}],"region_id":"DP02567r010","statement":[{"text":"The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]},{"start":2729,"end":2768,"reference_id":"32025030","reference_source":"pmid","reference_html":"The structure of human thyroglobulin. <i> Coscia F, Taler-Verčič A, Chang VT, Sinn L, O'Reilly FJ, Izoré T, Renko M, Berger I, Rappsilber J, Turk D, Löwe J. </i> Nature, 2020","date":"2022-08-08T17:45:48.266Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6SCJ"},{"db":"EMDB","id":"EMD-10141"}],"region_id":"DP02567r011","statement":[{"text":"The PDB shows that this region lacks electron density, indicating that it is disordered.","type":"Curator statement"}]}],"released":"2023_12","length":2768,"ncbi_taxon_id":9606,"date":"2020-02-14T15:30:00.031Z","organism":"Homo sapiens","features":{"gene3D":[{"start":2204,"end":2734,"id":"G3DSA:3.40.50.1820","name":"G3DSA:3.40.50.1820"},{"start":1512,"end":1558,"id":"G3DSA:4.10.800.10","name":"Thyroglobulin type-1"},{"start":1512,"end":1558,"id":"G3DSA:4.10.800.10","name":"Thyroglobulin type-1"},{"start":1512,"end":1558,"id":"G3DSA:4.10.800.10","name":"Thyroglobulin type-1"},{"start":1512,"end":1558,"id":"G3DSA:4.10.800.10","name":"Thyroglobulin type-1"},{"start":1512,"end":1558,"id":"G3DSA:4.10.800.10","name":"Thyroglobulin type-1"},{"start":1512,"end":1558,"id":"G3DSA:4.10.800.10","name":"Thyroglobulin type-1"},{"start":1512,"end":1558,"id":"G3DSA:4.10.800.10","name":"Thyroglobulin type-1"},{"start":1512,"end":1558,"id":"G3DSA:4.10.800.10","name":"Thyroglobulin type-1"},{"start":1512,"end":1558,"id":"G3DSA:4.10.800.10","name":"Thyroglobulin type-1"}],"pfam":[{"id":"PF00086","name":"Thyroglobulin type-1 repeat","start":45,"end":92},{"id":"PF00086","name":"Thyroglobulin type-1 repeat","start":96,"end":160},{"id":"PF00086","name":"Thyroglobulin type-1 repeat","start":312,"end":358},{"id":"PF00086","name":"Thyroglobulin type-1 repeat","start":603,"end":658},{"id":"PF00086","name":"Thyroglobulin type-1 repeat","start":662,"end":724},{"id":"PF00086","name":"Thyroglobulin type-1 repeat","start":750,"end":776},{"id":"PF00086","name":"Thyroglobulin type-1 repeat","start":896,"end":921},{"id":"PF00086","name":"Thyroglobulin type-1 repeat","start":1024,"end":1067},{"id":"PF00086","name":"Thyroglobulin type-1 repeat","start":1091,"end":1141},{"id":"PF00086","name":"Thyroglobulin type-1 repeat","start":1159,"end":1210},{"id":"PF00135","name":"Carboxylesterase family","start":2199,"end":2718},{"id":"PF07699","name":"Tyrosine-protein kinase ephrin type A/B receptor-like","start":1465,"end":1510}]},"disprot_id":"DP02567","regions_counter":11,"dataset":[],"UniParc":"UPI00001734A1","uniref100":"UniRef100_P01266","uniref90":"UniRef90_P01266","uniref50":"UniRef50_P01266","genes":[{"name":{"value":"TG","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11764","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11764"}}]}}],"disorder_content":0.07225433526011561,"disprot_consensus":{"full":[{"start":1,"end":23,"type":"D"},{"start":388,"end":407,"type":"D"},{"start":511,"end":546,"type":"D"},{"start":610,"end":620,"type":"D"},{"start":830,"end":847,"type":"D"},{"start":1010,"end":1020,"type":"D"},{"start":1234,"end":1243,"type":"D"},{"start":1640,"end":1657,"type":"D"},{"start":1802,"end":1814,"type":"D"},{"start":2729,"end":2768,"type":"D"}],"Structural state":[{"start":1,"end":23,"type":"D"},{"start":388,"end":407,"type":"D"},{"start":511,"end":546,"type":"D"},{"start":610,"end":620,"type":"D"},{"start":830,"end":847,"type":"D"},{"start":1010,"end":1020,"type":"D"},{"start":1234,"end":1243,"type":"D"},{"start":1640,"end":1657,"type":"D"},{"start":1802,"end":1814,"type":"D"},{"start":2729,"end":2768,"type":"D"}],"Disorder function":[{"start":610,"end":620,"type":"F"}]}},{"acc":"P04616","sequence":"MAGRSGDSDEDLLKAVRLIKFLYQSNPPPNPEGTRQARRNRRRRWRERQRQIHSISERILSTYLGRSAEPVPLQLPPLERLTLDCNEDCGTSGTQGVGSPQILVESPTVLESGAKE","creator":"fquaglia","dataset":["Viral proteins","RNA-binding proteins"],"date":"2020-02-14T16:16:47.331Z","disprot_id":"DP02568","features":{"gene3D":[],"pfam":[{"id":"PF00424","name":"REV protein (anti-repression trans-activator protein)","start":1,"end":91}]},"genes":[{"name":{"value":"rev","evidences":[{"source":{"id":"MF_04077","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04077","_id":"685af523b4ac24d5329d95b5"},"code":"ECO:0000255","_id":"685af523b4ac24d5329d95b4"}],"_id":"685af523b4ac24d5329d95b6"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d95b3"}],"length":116,"name":"Protein Rev","ncbi_taxon_id":11678,"organism":"Human immunodeficiency virus type 1 group M subtype B (isolate BH10)","regions_counter":16,"released":"2020_12","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"UniParc":"UPI000011F4F3","uniref100":"UniRef100_P04616","uniref50":"UniRef50_P69718","uniref90":"UniRef90_P69718","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2X7L","_id":"685af523b4ac24d5329d9578"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":66,"end":116,"interaction_partner":[],"reference_html":"Implications of the HIV-1 Rev dimer structure at 3.2 A resolution for multimeric binding to the Rev response element. <i> DiMattia MA, Watts NR, Stahl SJ, Rader C, Wingfield PT, Stuart DI, Steven AC, Grimes JM. </i> Proc Natl Acad Sci U S A, 2010","reference_id":"20231488","region_id":"DP02568r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Although full-length Rev is present in the crystals (SDS–PAGE of a crystal showed unaltered Rev mobility, with contaminants at ∼5%) (Fig. S2), only residues 9 to 65—the N-terminal domain (NTD)—were found to be ordered (Fig. 1A).","_id":"685af523b4ac24d5329d9579"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-03T10:16:12.354Z","_id":"685af523b4ac24d5329d957a"},"version":1,"_id":"685af523b4ac24d5329d9577","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":34,"end":50,"interaction_partner":[],"reference_html":"A solution to limited genomic capacity: using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA. <i> Daugherty MD, D'Orso I, Frankel AD. </i> Mol Cell, 2008","reference_id":"18922466","region_id":"DP02568r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"We further characterized the differences in IA and IIB binding modes using amide proton chemical shifts from 15N HSQC NMR spectra to monitor changes in the peptide-RNA interfaces. There is little peak dispersion of peptide resonances in the absence of RNA (Figure 5C), indicative of a largely unstructured molecule.","_id":"685af523b4ac24d5329d957c"},{"type":"Curator statement","text":"Protein used in this publication is from Human immunodeficiency virus type 1 group M subtype B (isolate HXB3). IDR has 100% identity to this Uniprot.","_id":"685af523b4ac24d5329d957d"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:49:19.099Z","_id":"685af523b4ac24d5329d957e"},"version":1,"_id":"685af523b4ac24d5329d957b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":34,"end":50,"interaction_partner":[],"reference_html":"A solution to limited genomic capacity: using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA. <i> Daugherty MD, D'Orso I, Frankel AD. </i> Mol Cell, 2008","reference_id":"18922466","region_id":"DP02568r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"We further characterized the differences in IA and IIB binding modes using amide proton chemical shifts from 15N HSQC NMR spectra to monitor changes in the peptide-RNA interfaces. There is little peak dispersion of peptide resonances in the absence of RNA (Figure 5C), indicative of a largely unstructured molecule. However, we observe substantial amide peak dispersion in the presence of either IIB (red) or IA (blue) RNAs (Figure 5C), including the Hε protons of arginine side chains (Figure 5C inset). The overall upfield shifts observed in both 1H and 15N dimensions is consistent with stabilization of peptide α-helical structure upon binding (Wang and Jardetzky, 2002).","_id":"685af523b4ac24d5329d9580"},{"type":"Curator statement","text":"Protein used in this publication is from Human immunodeficiency virus type 1 group M subtype B (isolate HXB3). IDR has 100% identity to this Uniprot.","_id":"685af523b4ac24d5329d9581"}],"states_connection":[{"source":"DP02568r004","target":"DP02568r006","_id":"685af523b4ac24d5329d9582"}],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:49:41.643Z","_id":"685af523b4ac24d5329d9583"},"version":1,"_id":"685af523b4ac24d5329d957f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":34,"end":50,"interaction_partner":[],"reference_html":"A solution to limited genomic capacity: using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA. <i> Daugherty MD, D'Orso I, Frankel AD. </i> Mol Cell, 2008","reference_id":"18922466","region_id":"DP02568r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The overall upfield shifts observed in both 1H and 15N dimensions is consistent with stabilization of peptide α-helical structure upon binding (Wang and Jardetzky, 2002).","_id":"685af523b4ac24d5329d9585"},{"type":"Curator statement","text":"Protein used in this publication is from Human immunodeficiency virus type 1 group M subtype B (isolate HXB3). IDR has 100% identity to this Uniprot.","_id":"685af523b4ac24d5329d9586"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:48:18.995Z","_id":"685af523b4ac24d5329d9587"},"version":1,"_id":"685af523b4ac24d5329d9584","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":34,"end":50,"interaction_partner":[],"reference_html":"A solution to limited genomic capacity: using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA. <i> Daugherty MD, D'Orso I, Frankel AD. </i> Mol Cell, 2008","reference_id":"18922466","region_id":"DP02568r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Given, the purine-rich internal loop of IA, we asked if this amino acid also is essential for IA binding. Interestingly, mutation of Asn40 had no effect on IA binding. Conversely, mutation of Arg41, which does not affect IIB binding (Tan et al., 1993), showed a reproducible 2-fold decrease in IA affinity (Figure 5A). R38A and R46A mutants showed similar 2-fold reductions in IA affinity but had no effect on IIB, while R43A, R44A, and W45A mutants bound IA like the wild type peptide. Helical wheel projections clearly show that different surfaces of the helix are used to recognize IIB and IA RNAs (Figure 5B).","_id":"685af523b4ac24d5329d9589"},{"type":"Curator statement","text":"Protein used in this publication is from Human immunodeficiency virus type 1 group M subtype B (isolate HXB3). IDR has 100% identity to this Uniprot.","_id":"685af523b4ac24d5329d958a"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_go_domain":"F","term_id":"GO:0003723","term_is_binding":true,"term_is_obsolete":false,"term_name":"RNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:52:49.356Z","_id":"685af523b4ac24d5329d958b"},"version":1,"_id":"685af523b4ac24d5329d9588","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":34,"end":50,"interaction_partner":[],"reference_html":"The arginine-rich RNA-binding motif of HIV-1 Rev is intrinsically disordered and folds upon RRE binding. <i> Casu F, Duggan BM, Hennig M. </i> Biophys J, 2013","reference_id":"23972852","region_id":"DP02568r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"CD spectra of the Rev ARM peptide in physiological buffer exhibited a minimum around 200 nm, typical of an unfolded state (Fig. 1 A).","_id":"685af523b4ac24d5329d958d"},{"type":"Curator statement","text":"Protein used in this publication is from Human immunodeficiency virus type 1 group M subtype B (isolate HXB3). IDR has 100% identity to this Uniprot.","_id":"685af523b4ac24d5329d958e"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:47:56.694Z","_id":"685af523b4ac24d5329d958f"},"version":1,"_id":"685af523b4ac24d5329d958c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":34,"end":50,"interaction_partner":[],"reference_html":"The arginine-rich RNA-binding motif of HIV-1 Rev is intrinsically disordered and folds upon RRE binding. <i> Casu F, Duggan BM, Hennig M. </i> Biophys J, 2013","reference_id":"23972852","region_id":"DP02568r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"To obtain residue-specific information regarding the Rev ARM peptide, we recorded 1HN,15N-HSQC spectra (Fig. 2). In aqueous solution, the peptide shows little dispersion of the resonances (Fig. 2 B), indicative of an unfolded peptide and in accordance with the CD data.","_id":"685af523b4ac24d5329d9591"},{"type":"Curator statement","text":"Protein used in this publication is from Human immunodeficiency virus type 1 group M subtype B (isolate HXB3). IDR has 100% identity to this Uniprot.","_id":"685af523b4ac24d5329d9592"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:47:38.722Z","_id":"685af523b4ac24d5329d9593"},"version":1,"_id":"685af523b4ac24d5329d9590","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":34,"end":50,"interaction_partner":[],"reference_html":"The arginine-rich RNA-binding motif of HIV-1 Rev is intrinsically disordered and folds upon RRE binding. <i> Casu F, Duggan BM, Hennig M. </i> Biophys J, 2013","reference_id":"23972852","region_id":"DP02568r010","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Fig. 5 B shows that the [1HN],15N hetNOE values for Rev ARM in aqueous solution at pH 7.4 average 0.47 for residues T34–R50, consistent with a disordered peptide. In contrast, the hetNOEs of the Rev ARM peptide in complex with RRE StemIIB average 0.83 for residues T34–R50, and in 50% TFE average 0.77 for residues T34–R50. These higher hetNOE values indicate higher backbone rigidity and are typical of a well-ordered secondary structure.","_id":"685af523b4ac24d5329d9595"},{"type":"Curator statement","text":"RRE StemIIB it's the RNA binding Rev ARM.","_id":"685af523b4ac24d5329d9596"},{"type":"Curator statement","text":"Protein used in this publication is from Human immunodeficiency virus type 1 group M subtype B (isolate HXB3). IDR has 100% identity to this Uniprot.","_id":"685af523b4ac24d5329d9597"}],"states_connection":[{"source":"DP02568r009","target":"DP02568r011","_id":"685af523b4ac24d5329d9598"}],"term_go_domain":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:49:38.373Z","_id":"685af523b4ac24d5329d9599"},"version":1,"_id":"685af523b4ac24d5329d9594","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":34,"end":50,"interaction_partner":[],"reference_html":"The arginine-rich RNA-binding motif of HIV-1 Rev is intrinsically disordered and folds upon RRE binding. <i> Casu F, Duggan BM, Hennig M. </i> Biophys J, 2013","reference_id":"23972852","region_id":"DP02568r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In contrast, the hetNOEs of the Rev ARM peptide in complex with RRE StemIIB average 0.83 for residues T34–R50, and in 50% TFE average 0.77 for residues T34–R50. These higher hetNOE values indicate higher backbone rigidity and are typical of a well-ordered secondary structure.","_id":"685af523b4ac24d5329d959b"},{"type":"Curator statement","text":"RRE StemIIB it's the RNA binding Rev ARM.","_id":"685af523b4ac24d5329d959c"},{"type":"Curator statement","text":"Protein used in this publication is from Human immunodeficiency virus type 1 group M subtype B (isolate HXB3). IDR has 100% identity to this Uniprot.","_id":"685af523b4ac24d5329d959d"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T12:51:05.205Z","_id":"685af523b4ac24d5329d959e"},"version":1,"_id":"685af523b4ac24d5329d959a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":34,"end":50,"interaction_partner":[],"reference_html":"The arginine-rich RNA-binding motif of HIV-1 Rev is intrinsically disordered and folds upon RRE binding. <i> Casu F, Duggan BM, Hennig M. </i> Biophys J, 2013","reference_id":"23972852","region_id":"DP02568r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Fig. 5 B shows that the [1HN],15N hetNOE values for Rev ARM in aqueous solution at pH 7.4 average 0.47 for residues T34–R50, consistent with a disordered peptide. In contrast, the hetNOEs of the Rev ARM peptide in complex with RRE StemIIB average 0.83 for residues T34–R50, and in 50% TFE average 0.77 for residues T34–R50. These higher hetNOE values indicate higher backbone rigidity and are typical of a well-ordered secondary structure.\" Curator statement \"RRE StemIIB it's the RNA binding Rev ARM.","_id":"685af523b4ac24d5329d95a0"},{"type":"Curator statement","text":"RRE StemIIB it's the RNA binding Rev ARM.","_id":"685af523b4ac24d5329d95a1"},{"type":"Curator statement","text":"Protein used in this publication is from Human immunodeficiency virus type 1 group M subtype B (isolate HXB3). IDR has 100% identity to this Uniprot.","_id":"685af523b4ac24d5329d95a2"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_go_domain":"F","term_id":"GO:0003723","term_is_binding":true,"term_is_obsolete":false,"term_name":"RNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:52:37.769Z","_id":"685af523b4ac24d5329d95a3"},"version":1,"_id":"685af523b4ac24d5329d959f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007106","ec_name":"green fluorescent protein fusion protein localization evidence used in manual assertion","ec_ontology":"ECO","start":35,"end":50,"interaction_partner":[],"reference_html":"Analysis of nuclear targeting activities of transport signals in the human immunodeficiency virus Rev protein. <i> Demart S, Ceccherini-Silberstein F, Schlicht S, Walcher S, Wolff H, Neumann M, Erfle V, Brack-Werner R. </i> Exp Cell Res, 2003","reference_id":"14644169","region_id":"DP02568r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Rev–GFP showed typical predominantly nuclear localization (>80% of fluorescence) (Fig. 2A). In contrast, RevM5–GFP fluorescence was apparent mainly in the cytoplasm, with less than 22% of total fluorescence in the nucleus (Fig. 2A).","_id":"685af523b4ac24d5329d95a5"},{"type":"Curator statement","text":"RevM5 has a mutation in this IDR.","_id":"685af523b4ac24d5329d95a6"}],"states_connection":[],"term_comment":"","term_def":"\"The directed movement of a protein from the nucleus into the cytoplasm.\" [GOC:jl]","term_go_domain":"P","term_id":"GO:0006611","term_is_binding":false,"term_is_obsolete":false,"term_name":"protein export from nucleus","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:53:19.029Z","_id":"685af523b4ac24d5329d95a7"},"version":1,"_id":"685af523b4ac24d5329d95a4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007106","ec_name":"green fluorescent protein fusion protein localization evidence used in manual assertion","ec_ontology":"ECO","start":76,"end":80,"interaction_partner":[],"reference_html":"Analysis of nuclear targeting activities of transport signals in the human immunodeficiency virus Rev protein. <i> Demart S, Ceccherini-Silberstein F, Schlicht S, Walcher S, Wolff H, Neumann M, Erfle V, Brack-Werner R. </i> Exp Cell Res, 2003","reference_id":"14644169","region_id":"DP02568r014","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Analysis of the nuclear translocation activity of NES mutant peptides demonstrated that peptides with PAAAA instead of PPLER were defective in both nuclear import (Fig. 8A) and export (Fig. 9), indicating involvement of this sequence in a bidirectional transport activity of the Rev–NES.","_id":"685af523b4ac24d5329d95a9"}],"states_connection":[],"term_comment":"","term_def":"\"The directed movement of a protein from the nucleus into the cytoplasm.\" [GOC:jl]","term_go_domain":"P","term_id":"GO:0006611","term_is_binding":false,"term_is_obsolete":false,"term_name":"protein export from nucleus","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:53:14.494Z","_id":"685af523b4ac24d5329d95aa"},"version":1,"_id":"685af523b4ac24d5329d95a8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-08T14:27:13.311Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001807","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","ec_ontology":"ECO","start":35,"end":46,"interaction_partner":[{"db":"Rfam","id":"RF00036","operator":"and","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d95ad"}],"reference_html":"Interactions between HIV Rev and nuclear import and export factors: the Rev nuclear localisation signal mediates specific binding to human importin-beta. <i> Henderson BR, Percipalle P. </i> J Mol Biol, 1997","reference_id":"9405152","region_id":"DP02568r015","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As shown in a gel mobility shift assay (Figure 2), the addition of Rev normally leads to formation of multimeric complexes with 35S-labelled RRE.","_id":"685af523b4ac24d5329d95ac"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_go_domain":"F","term_id":"GO:0003723","term_is_binding":true,"term_is_obsolete":false,"term_name":"RNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-08-09T18:34:56.295Z","_id":"685af523b4ac24d5329d95ae"},"version":2,"_id":"685af523b4ac24d5329d95ab","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007688","ec_name":"gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":35,"end":46,"interaction_partner":[],"reference_html":"Interactions between HIV Rev and nuclear import and export factors: the Rev nuclear localisation signal mediates specific binding to human importin-beta. <i> Henderson BR, Percipalle P. </i> J Mol Biol, 1997","reference_id":"9405152","region_id":"DP02568r016","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The experiment demonstrates the specificity of the Rev-importin-β interaction, as importin-β did not bind to the GST-Rev NLS mutant, or to GST protein. This was an unexpected finding, and identifies Rev as the first protein known to contain an NLS specific for the 97 kDa importin-β receptor, and not importin-α.","_id":"685af523b4ac24d5329d95b0"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-02T10:52:26.575Z","_id":"685af523b4ac24d5329d95b1"},"version":1,"_id":"685af523b4ac24d5329d95af","reference_source":"pmid"}],"__v":0,"disorder_content":0.5862068965517241,"disprot_consensus":{"full":[{"start":34,"end":50,"type":"T"},{"start":66,"end":116,"type":"D"}],"Structural state":[{"start":34,"end":50,"type":"D"},{"start":66,"end":116,"type":"D"}],"Structural transition":[{"start":34,"end":50,"type":"T"}],"Molecular function":[{"start":34,"end":50,"type":"F"}],"Biological process":[{"start":35,"end":50,"type":"F"},{"start":76,"end":80,"type":"F"}]}},{"acc":"Q8R1S4","name":"Protein MTSS 1","sequence":"MEAVIEKECSALGGLFQTIISDMKGSYPVWEDFINKAGKLQSQLRTTVVAAAAFLDAFQKVADMATNTRGGTREIGSALTRMCMRHRSIEAKLRQFSSALIDCLINPLQEQMEEWKKVANQLDKDHAKEYKKARQEIKNKSSDTLKLQKKAKKVDAQGRGDIQPQLDSALQDVNDKYLLLEETEKQAVRKALIEERGRFCTFISMLRPVIEEEISMLGEITHLQTISEDLKSLTMDPHKLPSSSEQVILDLKGSDYSWSYQTPPSSPSTTMSRKSSVCSSLNSVNSSDSRSSGSHSHSPSSHYRYRSSNLAQQAPVRLSSVSSHDSGFISQDAFQSKSPSPMPPEAANQLSNGFSHCSLSSESHAGPVGAGPFPHCLPASRLLPRVTSVHLPDYAHYYTIGPGMFPSSQIPSWKDWAKPGPYDQPLVNTLQRRKEKREPDSNGGGPTTTGGPPAGAEEAQRPRSMTVSAATRPGEEMAACEELTLALSRGLQLDVQRSSRDSLQCSSGYSTQTTTPCCSEDTIPSQVSDYDYFSVSGDQEAEQQEFDKSSTIPRNSDISQSYRRMFQAKRPASTAGLPTTLGPAMVTPGVATIRRTPSTKPSVRRGTIGAGPIPIKTPVIPVKTPTVPDLPGVLPSPPDGPEERGEHSPESPSAGEGPQGVSNIPSSLWSGQAPVNPPLPGPKPSIPEEHRQAIPESEAEDQERDPPSATVSPGPIPESDPADLSPRESPQGEDMLNAIRRGVKLKKTTTNDRSAPRFS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":168,"region_id":"DP02569r001","start":155,"term_id":"IDPO:0000002","statement":[{"text":"In the structure of MIM’s IMD, only one turn of this α-helix is observed for chain A, whereas the helix is fully missing in chain B, possibly due to local disorder in the structure","type":"Results"},{"text":"The crystal structure of the IMD of MIM (N-terminal 250 amino acids) was determined to 1.85 Å resolution, using the single anomalous dispersion method and X-ray data collected from a Se-Met-substituted crystal (Experimental Procedures and Table 1). The IMD forms a dimer (Figure 1B). The structure is well defined in the electron density map, except for three areas, which are disordered: the last six amino acids of chain A, the last eight amino acids of chain B, and amino acids Asp 155 to Ser 168 of chain B.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17292833","version":2,"reference_html":"Structural basis for the actin-binding function of missing-in-metastasis. <i> Lee SH, Kerff F, Chereau D, Ferron F, Klug A, Dominguez R. </i> Structure, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2D1L"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":759,"ncbi_taxon_id":10090,"date":"2020-02-18T14:22:20.180Z","organism":"Mus musculus","features":{"gene3D":[{"start":1,"end":252,"id":"G3DSA:1.20.1270.60","name":"Arfaptin homology (AH) domain/BAR domain"}],"pfam":[{"id":"PF02205","name":"WH2 motif","start":729,"end":755},{"id":"PF08397","name":"IRSp53/MIM homology domain","start":16,"end":241}]},"disprot_id":"DP02569","regions_counter":1,"dataset":[],"UniParc":"UPI0000006909","uniref100":"UniRef100_Q8R1S4","uniref90":"UniRef90_Q8R1S4","uniref50":"UniRef50_Q8R1S4","genes":[{"name":{"value":"Mtss1","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:2384818","url":"http://www.informatics.jax.org/marker/MGI:2384818"}}]},"synonyms":[{"value":"Mim"}]}],"alphafold_very_low_content":0.5480895915678524,"disorder_content":0.01844532279314888,"disprot_consensus":{"full":[{"start":155,"end":168,"type":"D"}],"Structural state":[{"start":155,"end":168,"type":"D"}]}},{"acc":"Q8BPB0","name":"MOB kinase activator 1B","sequence":"MSFLFGSRSSKTFKPKKNIPEGSHQYELLKHAEATLGSGNLRMAVMLPEGEDLNEWVAVNTVDFFNQINMLYGTITDFCTEESCPVMSAGPKYEYHWADGTNIKKPIKCSAPKYIDYLMTWVQDQLDDETLFPSKIGVPFPKNFMSVAKTILKRLFRVYAHIYHQHFDPVIQLQEEAHLNTSFKHFIFFVQEFNLIDRRELAPLQELIEKLTSKDR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":23,"region_id":"DP02570r001","start":11,"term_id":"IDPO:0000002","statement":[{"text":"The overall structure adopts a globular shape comprising the MOB core domain made of nine α-helices (H1-H9) with the N-terminal extension, which forms a β-strand (the SN strand, residues 5-9) at the N-terminal segment of FLFGSRSS (residues 3-10) and a newly formed 4-turn α-helix (residues 24-38, hereafter referred to as the Switch helix), whereas the 10-residue linker between the SN strand and the Switch helix were poorly defined on the current map. Notably, the SN strand forms a β-sheet with the S2 strand (residues 95-98)","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27335147","version":2,"reference_html":"Structural basis for autoinhibition and its relief of MOB1 in the Hippo pathway. <i> Kim SY, Tachioka Y, Mori T, Hakoshima T. </i> Sci Rep, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5B6B"},{"db":"PDB","id":"5B5W"},{"db":"PDB","id":"5B5V"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":23,"region_id":"DP02570r002","start":11,"term_id":"IDPO:0000033","statement":[{"text":"The overall structure adopts a globular shape comprising the MOB core domain made of nine α-helices (H1-H9) with the N-terminal extension, which forms a β-strand (the SN strand, residues 5-9) at the N-terminal segment of FLFGSRSS (residues 3-10) and a newly formed 4-turn α-helix (residues 24-38, hereafter referred to as the Switch helix), whereas the 10-residue linker between the SN strand and the Switch helix were poorly defined on the current map. Notably, the SN strand forms a β-sheet with the S2 strand (residues 95-98)","type":"Results"},{"text":"In the autoinhibited form of MOB1, the N-terminal extension forms the very N-terminal β-strand, the SN strand (residues 5-9), forming a β-sheet with the S2 strand, followed by a conformationally flexible linker and the Switch helix bound to the LATS1-binding site. The flexible linker runs along the LATS1-binding surface with electrostatic interactions. Thr12 is located at the conformationally flexible linker and Thr35 is located at the Switch helix.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27335147","version":3,"reference_html":"Structural basis for autoinhibition and its relief of MOB1 in the Hippo pathway. <i> Kim SY, Tachioka Y, Mori T, Hakoshima T. </i> Sci Rep, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5B6B"},{"db":"PDB","id":"5B5W"},{"db":"PDB","id":"5B5V"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","length":216,"ncbi_taxon_id":10090,"date":"2020-02-18T14:44:14.103Z","organism":"Mus musculus","features":{"gene3D":[{"start":1,"end":216,"id":"G3DSA:1.20.140.30","name":"MOB kinase activator"}],"pfam":[{"id":"PF03637","name":"Mob1/phocein family","start":33,"end":204}]},"disprot_id":"DP02570","regions_counter":2,"dataset":[],"UniParc":"UPI00000742E9","uniref100":"UniRef100_Q7L9L4","uniref90":"UniRef90_Q7L9L4","uniref50":"UniRef50_Q7L9L4","genes":[{"name":{"value":"Mob1b"},"synonyms":[{"value":"Mobkl1a"}]}],"alphafold_very_low_content":0.06018518518518518,"disorder_content":0.06018518518518518,"disprot_consensus":{"full":[{"start":11,"end":23,"type":"D"}],"Structural state":[{"start":11,"end":23,"type":"D"}],"Disorder function":[{"start":11,"end":23,"type":"F"}]}},{"acc":"P80192","name":"Mitogen-activated protein kinase kinase kinase 9","sequence":"MEPSRALLGCLASAAAAAPPGEDGAGAGAEEEEEEEEEAAAAVGPGELGCDAPLPYWTAVFEYEAAGEDELTLRLGDVVEVLSKDSQVSGDEGWWTGQLNQRVGIFPSNYVTPRSAFSSRCQPGGEDPSCYPPIQLLEIDFAELTLEEIIGIGGFGKVYRAFWIGDEVAVKAARHDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARGGPLNRVLSGKRIPPDILVNWAVQIARGMNYLHDEAIVPIIHRDLKSSNILILQKVENGDLSNKILKITDFGLAREWHRTTKMSAAGTYAWMAPEVIRASMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKLALPIPSTCPEPFAKLMEDCWNPDPHSRPSFTNILDQLTTIEESGFFEMPKDSFHCLQDNWKHEIQEMFDQLRAKEKELRTWEEELTRAALQQKNQEELLRRREQELAEREIDILERELNIIIHQLCQEKPRVKKRKGKFRKSRLKLKDGNRISLPSDFQHKFTVQASPTMDKRKSLINSRSSPPASPTIIPRLRAIQLTPGESSKTWGRSSVVPKEEGEEEEKRAPKKKGRTWGPGTLGQKELASGDEGSPQRREKANGLSTPSESPHFHLGLKSLVDGYKQWSSSAPNLVKGPRSSPALPGFTSLMEMEDEDSEGPGSGESRLQHSPSQSYLCIPFPRGEDGDGPSSDGIHEEPTPVNSATSTPQLTPTNSLKRGGAHHRRCEVALLGCGAVLAATGLGFDLLEAGKCQLLPLEEPEPPAREEKKRREGLFQRSSRPRRSTSPPSRKLFKKEEPMLLLGDPSASLTLLSLSSISECNSTRSLLRSDSDEIVVYEMPVSPVEAPPLSPCTHNPLVNVRVERFKRDPNQSLTPTHVTLTTPSQPSSHRRTPSDGALKPETLLASRSPSSNGLSPSPGAGMLKTPSPSRDPGEFPRLPDPNVVFPPTPRRWNTQQDSTLERPKTLEFLPRPRPSANRQRLDPWWFVSPSHARSTSPANSSSTETPSNLDSCFASSSSTVEERPGLPALLPFQAGPLPPTERTLLDLDAEGQSQDSTVPLCRAELNTHRPAPYEIQQEFWS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":310,"region_id":"DP02571r001","start":298,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"This DFG-in structure had no density in the loop between strand β and helix αC (chain segment 174−180) in the C-terminal domain and in part of the activation loop (294−319) chain segment 296−309.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18714982","version":2,"reference_html":"Mixed-lineage kinase 1 and mixed-lineage kinase 3 subtype-selective dihydronaphthyl[3,4-a]pyrrolo[3,4-c]carbazole-5-ones: optimization, mixed-lineage kinase 1 crystallography, and oral in vivo activity in 1-methyl-4-phenyltetrahydropyridine models. <i> Hudkins RL, Diebold JL, Tao M, Josef KA, Park CH, Angeles TS, Aimone LD, Husten J, Ator MA, Meyer SL, Holskin BP, Durkin JT, Fedorov AA, Fedorov EV, Almo SC, Mathiasen JR, Bozyczko-Coyne D, Saporito MS, Scott RW, Mallamo JP. </i> J Med Chem, 2008","date":"2022-08-05T14:17:25.322Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3DTC"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-08T17:49:50.266Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":310,"region_id":"DP02571r002","start":298,"term_id":"GO:0140677","unpublished":true,"statement":[{"text":"This DFG-in structure had no density in the loop between strand β and helix αC (chain segment 174−180) in the C-terminal domain and in part of the activation loop (294−319) chain segment 296−309.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18714982","version":3,"reference_html":"Mixed-lineage kinase 1 and mixed-lineage kinase 3 subtype-selective dihydronaphthyl[3,4-a]pyrrolo[3,4-c]carbazole-5-ones: optimization, mixed-lineage kinase 1 crystallography, and oral in vivo activity in 1-methyl-4-phenyltetrahydropyridine models. <i> Hudkins RL, Diebold JL, Tao M, Josef KA, Park CH, Angeles TS, Aimone LD, Husten J, Ator MA, Meyer SL, Holskin BP, Durkin JT, Fedorov AA, Fedorov EV, Almo SC, Mathiasen JR, Bozyczko-Coyne D, Saporito MS, Scott RW, Mallamo JP. </i> J Med Chem, 2008","date":"2022-08-05T14:18:42.648Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3DTC"}],"term_name":"molecular function activator activity","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-08T17:49:52.202Z"}},{"start":173,"end":183,"reference_id":"18714982","reference_source":"pmid","reference_html":"Mixed-lineage kinase 1 and mixed-lineage kinase 3 subtype-selective dihydronaphthyl[3,4-a]pyrrolo[3,4-c]carbazole-5-ones: optimization, mixed-lineage kinase 1 crystallography, and oral in vivo activity in 1-methyl-4-phenyltetrahydropyridine models. <i> Hudkins RL, Diebold JL, Tao M, Josef KA, Park CH, Angeles TS, Aimone LD, Husten J, Ator MA, Meyer SL, Holskin BP, Durkin JT, Fedorov AA, Fedorov EV, Almo SC, Mathiasen JR, Bozyczko-Coyne D, Saporito MS, Scott RW, Mallamo JP. </i> J Med Chem, 2008","date":"2022-08-05T14:18:31.087Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3DTC"}],"region_id":"DP02571r003","statement":[{"text":"Missing electron density region in PDB:3DTC.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-08T17:49:44.087Z"}}],"released":"2023_12","length":1104,"ncbi_taxon_id":9606,"date":"2020-02-19T10:30:31.682Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":144,"end":403},{"id":"PF14604","name":"Variant SH3 domain","start":59,"end":112}]},"disprot_id":"DP02571","regions_counter":3,"dataset":["Stress response proteins"],"UniParc":"UPI0000052A4B","uniref100":"UniRef100_P80192","uniref90":"UniRef90_P80192","uniref50":"UniRef50_P80192","genes":[{"name":{"value":"MAP3K9"},"synonyms":[{"value":"MLK1"},{"value":"PRKE1"}]}],"alphafold_very_low_content":0.5788043478260869,"disorder_content":0.021739130434782608,"disprot_consensus":{"full":[{"start":173,"end":183,"type":"D"},{"start":298,"end":310,"type":"D"}],"Structural state":[{"start":173,"end":183,"type":"D"},{"start":298,"end":310,"type":"D"}],"Molecular function":[{"start":298,"end":310,"type":"F"}]}},{"acc":"P55042","name":"GTP-binding protein RAD","sequence":"MTLNGGGSGAGGSRGGGQERERRRGSTPWGPAPPLHRRSMPVDERDLQAALTPGALTAAAAGTGTQGPRLDWPEDSEDSLSSGGSDSDESVYKVLLLGAPGVGKSALARIFGGVEDGPEAEAAGHTYDRSIVVDGEEASLMVYDIWEQDGGRWLPGHCMAMGDAYVIVYSVTDKGSFEKASELRVQLRRARQTDDVPIILVGNKSDLVRSREVSVDEGRACAVVFDCKFIETSAALHHNVQALFEGVVRQIRLRRDSKEANARRQAGTRRRESLGKKAKRFLGRIVARNSRKMAFRAKSKSCHDLSVL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":125,"region_id":"DP02572r001","start":116,"term_id":"IDPO:0000002","statement":[{"text":"Second, the subtle but important switch I conformational switch that reads out the bound GTP in Ras is completely missing in the RGK proteins as they are not observed in the electron density in both Rad and Rem2","type":"Results"},{"text":"Specifically, switch I is disordered in both nucleotide states for both Rad and Rem2, without any detectable interactions between protein and nucleotide.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21903096","version":2,"reference_html":"RGK family G-domain:GTP analog complex structures and nucleotide-binding properties. <i> Sasson Y, Navon-Perry L, Huppert D, Hirsch JA. </i> J Mol Biol, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3Q72"},{"db":"PDB","id":"3Q7P"},{"db":"PDB","id":"3Q7Q"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":160,"region_id":"DP02572r002","start":149,"term_id":"IDPO:0000002","statement":[{"text":"For the RGK proteins, in the Rad:GDP crystal structure and particularly in the Rad:GNP crystal structure, switch II is largely characterized by static disorder.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21903096","version":2,"reference_html":"RGK family G-domain:GTP analog complex structures and nucleotide-binding properties. <i> Sasson Y, Navon-Perry L, Huppert D, Hirsch JA. </i> J Mol Biol, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3Q72"},{"db":"PDB","id":"3Q7P"},{"db":"PDB","id":"3Q7Q"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":308,"ncbi_taxon_id":9606,"date":"2020-02-19T10:55:55.923Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF00071","name":"Ras family","start":93,"end":252}]},"disprot_id":"DP02572","regions_counter":2,"dataset":[],"UniParc":"UPI00001330D1","uniref100":"UniRef100_P55042","uniref90":"UniRef90_P55042","uniref50":"UniRef50_P55042","genes":[{"name":{"value":"RRAD"},"synonyms":[{"value":"RAD"}]}],"alphafold_very_low_content":0.288961038961039,"disorder_content":0.07142857142857142,"disprot_consensus":{"full":[{"start":116,"end":125,"type":"D"},{"start":149,"end":160,"type":"D"}],"Structural state":[{"start":116,"end":125,"type":"D"},{"start":149,"end":160,"type":"D"}]}},{"acc":"Q8VEL9","name":"GTP-binding protein REM 2","sequence":"MHTDLDTDMDMDTETVALCSSSSRQASPLGTPTPEADTTLLKQKPEKLLAELDLSGPPPAPGVPRRRGSMPVPYKHQLRRAQAVDELDWPPQASPSGSSDSLGSGEAALTQKDGVFKVMLVGESGVGKSTLAGTFGGLQGDHAHEMENSEDTYERRIMVDKEEVTLIVYDIWEQGDAGGWLQDHCLQTGDAFLIVFSVTDRRGFSKVPETLLRLRAGRPHHDLPVILVGNKSDLARSREVSLEEGRHLAGTLSCKHIETSAALHHNTRELFEGAVRQIRLRRGRGHAGGQRPEPSSPDGPAPPTRRESLTKKAKRFLANLVPRNAKFFKQRSRSCHDLSVL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":151,"region_id":"DP02573r001","start":140,"term_id":"IDPO:0000002","statement":[{"text":"Specifically, switch I is disordered in both nucleotide states for both Rad and Rem2, without any detectable interactions between protein and nucleotide.","type":"Discussion"},{"text":"Second, the subtle but important switch I conformational switch that reads out the bound GTP in Ras is completely missing in the RGK proteins as they are not observed in the electron density in both Rad and Rem2","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21903096","version":2,"reference_html":"RGK family G-domain:GTP analog complex structures and nucleotide-binding properties. <i> Sasson Y, Navon-Perry L, Huppert D, Hirsch JA. </i> J Mol Biol, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3Q85"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":341,"ncbi_taxon_id":10090,"date":"2020-02-19T11:15:33.836Z","organism":"Mus musculus","features":{"gene3D":[],"pfam":[{"id":"PF00071","name":"Ras family","start":117,"end":279}]},"disprot_id":"DP02573","regions_counter":1,"dataset":[],"UniParc":"UPI0000021E22","uniref100":"UniRef100_Q8VEL9","uniref90":"UniRef90_Q8VEL9","uniref50":"UniRef50_Q8VEL9","genes":[{"name":{"value":"Rem2"}}],"alphafold_very_low_content":0.33724340175953077,"disorder_content":0.03519061583577713,"disprot_consensus":{"full":[{"start":140,"end":151,"type":"D"}],"Structural state":[{"start":140,"end":151,"type":"D"}]}},{"acc":"P39905","name":"Glial cell line-derived neurotrophic factor","sequence":"MKLWDVVAVCLVLLHTASAFPLPAGKRPPEAPAEDRSLGRRRAPFALSSDSNMPEDYPDQFDDVMDFIQATIKRLKRSPDKQMAVLPRRERNRQAAAANPENSRGKGRRGQRGKNRGCVLTAIHLNVTDLGLGYETKEELIFRYCSGSCDAAETTYDKILKNLSRNRRLVSDKVGQACCRPIAFDDDLSFLDDNLVYHILRKHSAKRCGCI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":117,"region_id":"DP02574r001","start":78,"term_id":"IDPO:0000002","statement":[{"text":"The N-­terminal region (residues 1–39 in chain B and 1–31 in chain D) of GDNF was dis­ordered.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19478429","version":2,"reference_html":"Comparison of GFL-GFRalpha complexes: further evidence relating GFL bend angle to RET signalling. <i> Parkash V, Goldman A. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3FUB"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":211,"ncbi_taxon_id":9606,"date":"2020-02-19T12:17:19.271Z","organism":"Homo sapiens","features":{"gene3D":[{"start":114,"end":211,"id":"G3DSA:2.10.90.10","name":"Cystine-knot cytokines"}],"pfam":[{"id":"PF00019","name":"Transforming growth factor beta like domain","start":118,"end":210}]},"disprot_id":"DP02574","regions_counter":1,"dataset":["Extracellular matrix proteins"],"UniParc":"UPI00000326A1","uniref100":"UniRef100_P39905","uniref90":"UniRef90_P39905","uniref50":"UniRef50_P39905","genes":[{"name":{"value":"GDNF"}}],"alphafold_very_low_content":0.1895734597156398,"disorder_content":0.1895734597156398,"disprot_consensus":{"full":[{"start":78,"end":117,"type":"D"}],"Structural state":[{"start":78,"end":117,"type":"D"}]}},{"acc":"P83755","name":"Photosystem II protein D1","sequence":"MTAILERRESESLWGRFCNWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIISGAIIPTSAAIGLHFYPIWEAASVDEWLYNGGPYELIVLHFLLGVACYMGREWELSFRLGMRPWIAVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANEGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLAAVEAPSTNG","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":344,"region_id":"DP02575r001","start":335,"term_id":"IDPO:0000002","statement":[{"text":"But the carboxy (C) terminus of PsbA (amino acids 335–344), important for the binding of the manganese cluster, appears to be disordered, as there is no density present in that region.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28604725","version":2,"reference_html":"Subunit and chlorophyll organization of the plant photosystem II supercomplex. <i> van Bezouwen LS, Caffarri S, Kale RS, Kouřil R, Thunnissen AWH, Oostergetel GT, Boekema EJ. </i> Nat Plants, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"5MDX"},{"db":"EMDB","id":"EMD-3491"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":344,"region_id":"DP02575r002","start":335,"term_id":"GO:0046872","statement":[{"text":"But the carboxy (C) terminus of PsbA (amino acids 335–344), important for the binding of the manganese cluster, appears to be disordered, as there is no density present in that region.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"28604725","version":3,"reference_html":"Subunit and chlorophyll organization of the plant photosystem II supercomplex. <i> van Bezouwen LS, Caffarri S, Kale RS, Kouřil R, Thunnissen AWH, Oostergetel GT, Boekema EJ. </i> Nat Plants, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","cross_refs":[{"db":"PDB","id":"5MDX"},{"db":"EMDB","id":"EMD-3491"}],"term_name":"metal ion binding","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","length":353,"ncbi_taxon_id":3702,"date":"2020-02-19T14:43:55.171Z","organism":"Arabidopsis thaliana","features":{"gene3D":[{"start":12,"end":343,"id":"G3DSA:1.20.85.10","name":"Photosystem II protein D1-like"}],"pfam":[{"id":"PF00124","name":"Photosynthetic reaction centre protein","start":28,"end":327}]},"disprot_id":"DP02575","regions_counter":3,"dataset":[],"UniParc":"UPI000006175B","uniref100":"UniRef100_P83755","uniref90":"UniRef90_P83755","uniref50":"UniRef50_P83755","genes":[{"name":{"value":"psbA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01379","url":"https://hamap.expasy.org/unirule/MF_01379"}}]},"olnNames":[{"value":"AtCg00020"}]}],"alphafold_very_low_content":0.0226628895184136,"disorder_content":0.028328611898016998,"disprot_consensus":{"full":[{"start":335,"end":344,"type":"D"}],"Structural state":[{"start":335,"end":344,"type":"D"}],"Molecular function":[{"start":335,"end":344,"type":"F"}]}},{"acc":"P56777","name":"Photosystem II CP47 reaction center protein","sequence":"MGLPWYRVHTVVLNDPGRLLAVHIMHTALVAGWAGSMALYELAVFDPSDPVLDPMWRQGMFVIPFMTRLGITNSWGGWNITGGTITNPGLWSYEGVAGAHIVFSGLCFLAAIWHWVYWDLEIFCDERTGKPSLDLPKIFGIHLFLSGVACFGFGAFHVTGLYGPGIWVSDPYGLTGKVQPVNPAWGVEGFDPFVPGGIASHHIAAGTLGILAGLFHLSVRPPQRLYKGLRMGNIETVLSSSIAAVFFAAFVVAGTMWYGSATTPIELFGPTRYQWDQGYFQQEIYRRVSAGLAENQSLSEAWAKIPEKLAFYDYIGNNPAKGGLFRAGSMDNGDGIAVGWLGHPVFRNKEGRELFVRRMPTFFETFPVVLVDGDGIVRADVPFRRAESKYSVEQVGVTVEFYGGELNGVSYSDPATVKKYARRAQLGEIFELDRATLKSDGVFRSSPRGWFTFGHASFALLFFFGHIWHGARTLFRDVFAGIDPDLDAQVEFGAFQKLGDPTTKRQAV","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":508,"region_id":"DP02576r001","start":480,"term_id":"IDPO:0000002","statement":[{"text":"In the cryo-EM density map all the transmembrane helices of PsbA, PsbB, PsbC and PsbD are clearly visible and well defined. Whereas the helices are clearly visible, the termini are more difficult to assign.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28604725","version":2,"reference_html":"Subunit and chlorophyll organization of the plant photosystem II supercomplex. <i> van Bezouwen LS, Caffarri S, Kale RS, Kouřil R, Thunnissen AWH, Oostergetel GT, Boekema EJ. </i> Nat Plants, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"EMDB","id":"EMD-3491"},{"db":"PDB","id":"5MDX"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2021_06","length":508,"ncbi_taxon_id":3702,"date":"2020-02-19T14:51:32.512Z","organism":"Arabidopsis thaliana","features":{"gene3D":[],"pfam":[{"id":"PF00421","name":"Photosystem II protein","start":1,"end":500}]},"disprot_id":"DP02576","regions_counter":1,"dataset":[],"UniParc":"UPI0000132608","uniref100":"UniRef100_P56777","uniref90":"UniRef90_P56777","uniref50":"UniRef50_P56777","genes":[{"name":{"value":"psbB","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01495","url":"https://hamap.expasy.org/unirule/MF_01495"}}]},"olnNames":[{"value":"AtCg00680"}]}],"alphafold_very_low_content":0,"disorder_content":0.05708661417322835,"disprot_consensus":{"full":[{"start":480,"end":508,"type":"D"}],"Structural state":[{"start":480,"end":508,"type":"D"}]}},{"acc":"P23321","name":"Oxygen-evolving enhancer protein 1-1, chloroplastic","sequence":"MAASLQSTATFLQSAKIATAPSRGSSHLRSTQAVGKSFGLETSSARLTCSFQSDFKDFTGKCSDAVKIAGFALATSALVVSGASAEGAPKRLTYDEIQSKTYMEVKGTGTANQCPTIDGGSETFSFKPGKYAGKKFCFEPTSFTVKADSVSKNAPPEFQNTKLMTRLTYTLDEIEGPFEVASDGSVNFKEEDGIDYAAVTVQLPGGERVPFLFTVKQLDASGKPDSFTGKFLVPSYRGSSFLDPKGRGGSTGYDNAVALPAGGRGDEEELVKENVKNTAASVGEITLKVTKSKPETGEVIGVFESLQPSDTDLGAKVPKDVKIQGVWYGQLE","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":281,"region_id":"DP02577r001","start":240,"term_id":"IDPO:0000002","statement":[{"text":"For the extrinsic subunits the density for PsbO has been assigned. The β-barrel is well organized, but for the loops not all densities are resolved.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28604725","version":2,"reference_html":"Subunit and chlorophyll organization of the plant photosystem II supercomplex. <i> van Bezouwen LS, Caffarri S, Kale RS, Kouřil R, Thunnissen AWH, Oostergetel GT, Boekema EJ. </i> Nat Plants, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"EMDB","id":"EMD-3491"},{"db":"PDB","id":"5MDX"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2020_12","length":332,"ncbi_taxon_id":3702,"date":"2020-02-19T15:00:42.446Z","organism":"Arabidopsis thaliana","features":{"gene3D":[],"pfam":[{"id":"PF01716","name":"Manganese-stabilising protein / photosystem II polypeptide","start":99,"end":331}]},"disprot_id":"DP02577","regions_counter":1,"dataset":[],"UniParc":"UPI000016DB97","uniref100":"UniRef100_P23321","uniref90":"UniRef90_P23321","uniref50":"UniRef50_P23321","genes":[{"name":{"value":"PSBO1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11719511","url":"http://www.ncbi.nlm.nih.gov/pubmed/11719511","alternativeUrl":"https://europepmc.org/abstract/MED/11719511"}}]},"synonyms":[{"value":"OEC33","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11826309","url":"http://www.ncbi.nlm.nih.gov/pubmed/11826309","alternativeUrl":"https://europepmc.org/abstract/MED/11826309"}}]},{"value":"PSBO","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9802567","url":"http://www.ncbi.nlm.nih.gov/pubmed/9802567","alternativeUrl":"https://europepmc.org/abstract/MED/9802567"}}]}],"orfNames":[{"value":"K1F13.25","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"BAB10933.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAB10933.1"}}]}],"olnNames":[{"value":"At5g66570","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT5G66570","url":""}}]}]}],"alphafold_very_low_content":0.24397590361445784,"disorder_content":0.12650602409638553,"disprot_consensus":{"full":[{"start":240,"end":281,"type":"D"}],"Structural state":[{"start":240,"end":281,"type":"D"}]}},{"acc":"Q16647","name":"Prostacyclin synthase","sequence":"MAWAALLGLLAALLLLLLLSRRRTRRPGEPPLDLGSIPWLGYALDFGKDAASFLTRMKEKHGDIFTILVGGRYVTVLLDPHSYDAVVWEPRTRLDFHAYAIFLMERIFDVQLPHYSPSDEKARMKLTLLHRELQALTEAMYTNLHAVLLGDATEAGSGWHEMGLLDFSYSFLLRAGYLTLYGIEALPRTHESQAQDRVHSADVFHTFRQLDRLLPKLARGSLSVGDKDHMCSVKSRLWKLLSPARLARRAHRSKWLESYLLHLEEMGVSEEMQARALVLQLWATQGNMGPAAFWLLLFLLKNPEALAAVRGELESILWQAEQPVSQTTTLPQKVLDSTPVLDSVLSESLRLTAAPFITREVVVDLAMPMADGREFNLRRGDRLLLFPFLSPQRDPEIYTDPEVFKYNRFLNPDGSEKKDFYKDGKRLKNYNMPWGAGHNHCLGRSYAVNSIKQFVFLVLVHLDLELINADVEIPEFDLSRYGFGLMQPEHDVPVRYRIRP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":330,"region_id":"DP02578r001","start":319,"term_id":"IDPO:0000002","statement":[{"text":"No electron density is associated with residues 320–327 of chain A or residues 319–330 of chain B, and these regions were omitted from the model.","type":"Table"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17020766","version":2,"reference_html":"Crystal structure of the human prostacyclin synthase. <i> Chiang CW, Yeh HC, Wang LH, Chan NL. </i> J Mol Biol, 2006","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2IAG"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":500,"ncbi_taxon_id":9606,"date":"2020-02-19T15:15:02.155Z","organism":"Homo sapiens","features":{"gene3D":[{"start":15,"end":500,"id":"G3DSA:1.10.630.10","name":"Cytochrome P450"}],"pfam":[{"id":"PF00067","name":"Cytochrome P450","start":269,"end":491}]},"disprot_id":"DP02578","regions_counter":1,"dataset":[],"UniParc":"UPI00001328DF","uniref100":"UniRef100_Q16647","uniref90":"UniRef90_Q16647","uniref50":"UniRef50_Q16647","genes":[{"name":{"value":"PTGIS"},"synonyms":[{"value":"CYP8"},{"value":"CYP8A1"}]}],"alphafold_very_low_content":0,"disorder_content":0.024,"disprot_consensus":{"full":[{"start":319,"end":330,"type":"D"}],"Structural state":[{"start":319,"end":330,"type":"D"}]}},{"acc":"Q8VDQ1","name":"Prostaglandin reductase 2","sequence":"MIIQRVVLNSRPGKNGNPVAENFRVEEFSLPDALNEGQVQVRTLYLSVDPYMRCKMNEDTGTDYLAPWQLAQVADGGGIGVVEESKHQKLTKGDFVTSFYWPWQTKAILDGNGLEKVDPQLVDGHLSYFLGAIGMPGLTSLIGVQEKGHISAGSNQTMVVSGAAGACGSLAGQIGHLLGCSRVVGICGTQEKCLFLTSELGFDAAVNYKTGNVAEQLREACPGGVDVYFDNVGGDISNAVISQMNENSHIILCGQISQYSNDVPYPPPLPPAVEAIRKERNITRERFTVLNYKDKFEPGILQLSQWFKEGKLKVKETMAKGLENMGVAFQSMMTGGNVGKQIVCISEDSSL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":265,"region_id":"DP02579r001","start":254,"term_id":"IDPO:0000002","statement":[{"text":"No electron density was observed for residues 254–265.","type":"Article"},{"text":"The present structure does not contain a bound nucleotide, which is most likely the reason for the observed disorder in one of the nucleotide‐recognition loops (residues 254–265).","type":"Article"},{"text":"The Tyr64 side‐chain is disordered in the 18204011 structure, which is most likely due to lack of any bound NADPH.","type":"Article"},{"text":"No electron density was observed for residues 254–265, the side‐chain atoms of D32, Y64, E115, E191, N212, R286, E297, K320, E347, or the rest of the expression and purification tag.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15229897","version":2,"reference_html":"Crystal structure of a putative NADPH-dependent oxidoreductase (GI: 18204011) from mouse at 2.10 A resolution. <i> Levin I, Schwarzenbacher R, McMullan D, Abdubek P, Ambing E, Biorac T, Cambell J, Canaves JM, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hampton E, Jaroszewski L, Karlak C, Klock HE, Koesema E, Kreusch A, Kuhn P, Lesley SA, McPhillips TM, Miller MD, Morse A, Moy K, Ouyang J, Page R, Quijano K, Reyes R, Robb A, Sims E, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, von Delft F, Wang X, West B, Wolf G, Xu Q, Hodgson KO, Wooley J, Wilson IA. </i> Proteins, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1VJ1"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":265,"region_id":"DP02579r002","start":254,"term_id":"GO:0098772","statement":[{"text":"No electron density was observed for residues 254–265.","type":"Article"},{"text":"The present structure does not contain a bound nucleotide, which is most likely the reason for the observed disorder in one of the nucleotide‐recognition loops (residues 254–265).","type":"Article"},{"text":"The disordered loop between residues Cys253 and Pro266 comprises a conserved GxxS motif, which stabilizes both the adenine and nicotinamide moieties of the cofactor in the NADPH‐bound form of quinone oxidoreductase.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15229897","version":3,"reference_html":"Crystal structure of a putative NADPH-dependent oxidoreductase (GI: 18204011) from mouse at 2.10 A resolution. <i> Levin I, Schwarzenbacher R, McMullan D, Abdubek P, Ambing E, Biorac T, Cambell J, Canaves JM, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Godzik A, Grittini C, Grzechnik SK, Hampton E, Jaroszewski L, Karlak C, Klock HE, Koesema E, Kreusch A, Kuhn P, Lesley SA, McPhillips TM, Miller MD, Morse A, Moy K, Ouyang J, Page R, Quijano K, Reyes R, Robb A, Sims E, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, von Delft F, Wang X, West B, Wolf G, Xu Q, Hodgson KO, Wooley J, Wilson IA. </i> Proteins, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1VJ1"}],"term_name":"molecular function regulator","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","length":351,"ncbi_taxon_id":10090,"date":"2020-02-19T15:20:18.779Z","organism":"Mus musculus","features":{"gene3D":[],"pfam":[{"id":"PF00107","name":"Zinc-binding dehydrogenase","start":168,"end":269},{"id":"PF16884","name":"N-terminal domain of oxidoreductase","start":5,"end":117}]},"disprot_id":"DP02579","regions_counter":2,"dataset":[],"UniParc":"UPI00000E6424","uniref100":"UniRef100_Q8VDQ1","uniref90":"UniRef90_Q8VDQ1","uniref50":"UniRef50_Q8VDQ1","genes":[{"name":{"value":"Ptgr2","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:1916372","url":"http://www.informatics.jax.org/marker/MGI:1916372"}}]},"synonyms":[{"value":"Zadh1"}]}],"alphafold_very_low_content":0,"disorder_content":0.03418803418803419,"disprot_consensus":{"full":[{"start":254,"end":265,"type":"D"}],"Structural state":[{"start":254,"end":265,"type":"D"}],"Molecular function":[{"start":254,"end":265,"type":"F"}]}},{"acc":"P28827","name":"Receptor-type tyrosine-protein phosphatase mu","sequence":"MRGLGTCLATLAGLLLTAAGETFSGGCLFDEPYSTCGYSQSEGDDFNWEQVNTLTKPTSDPWMPSGSFMLVNASGRPEGQRAHLLLPQLKENDTHCIDFHYFVSSKSNSPPGLLNVYVKVNNGPLGNPIWNISGDPTRTWNRAELAISTFWPNFYQVIFEVITSGHQGYLAIDEVKVLGHPCTRTPHFLRIQNVEVNAGQFATFQCSAIGRTVAGDRLWLQGIDVRDAPLKEIKVTSSRRFIASFNVVNTTKRDAGKYRCMIRTEGGVGISNYAELVVKEPPVPIAPPQLASVGATYLWIQLNANSINGDGPIVAREVEYCTASGSWNDRQPVDSTSYKIGHLDPDTEYEISVLLTRPGEGGTGSPGPALRTRTKCADPMRGPRKLEVVEVKSRQITIRWEPFGYNVTRCHSYNLTVHYCYQVGGQEQVREEVSWDTENSHPQHTITNLSPYTNVSVKLILMNPEGRKESQELIVQTDEDLPGAVPTESIQGSTFEEKIFLQWREPTQTYGVITLYEITYKAVSSFDPEIDLSNQSGRVSKLGNETHFLFFGLYPGTTYSFTIRASTAKGFGPPATNQFTTKISAPSMPAYELETPLNQTDNTVTVMLKPAHSRGAPVSVYQIVVEEERPRRTKKTTEILKCYPVPIHFQNASLLNSQYYFAAEFPADSLQAAQPFTIGDNKTYNGYWNTPLLPYKSYRIYFQAASRANGETKIDCVQVATKGAATPKPVPEPEKQTDHTVKIAGVIAGILLFVIIFLGVVLVMKKRKLAKKRKETMSSTRQEMTVMVNSMDKSYAEQGTNCDEAFSFMDTHNLNGRSVSSPSSFTMKTNTLSTSVPNSYYPDETHTMASDTSSLVQSHTYKKREPADVPYQTGQLHPAIRVADLLQHITQMKCAEGYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQTIEGDTNSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPSAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACLCGDTSVPASQVRSLYYDMNKLDPQTNSSQIKEEFRTLNMVTPTLRVEDCSIALLPRNHEKNRCMDILPPDRCLPFLITIDGESSNYINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSVVMLNDVDPAQLCPQYWPENGVHRHGPIQVEFVSADLEEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNGGGRSGTFCAISIVCEMLRHQRTVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALEYLNSG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":742,"region_id":"DP02580r001","start":589,"term_id":"IDPO:0000002","statement":[{"text":"The electron density for the fourth FN domain, although sufficient to indicate its approximate position, remained largely disordered throughout refinement; therefore, this domain was not included in the final model (fig. S2, A and B).","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17761881","version":3,"reference_html":"Structure of a tyrosine phosphatase adhesive interaction reveals a spacer-clamp mechanism. <i> Aricescu AR, Siebold C, Choudhuri K, Chang VT, Lu W, Davis SJ, van der Merwe PA, Jones EY. </i> Science, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2V5Y"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-29T07:28:57.910Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":1452,"ncbi_taxon_id":9606,"date":"2020-02-19T15:53:40.923Z","organism":"Homo sapiens","features":{"gene3D":[{"start":489,"end":588,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":489,"end":588,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":489,"end":588,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":489,"end":588,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":877,"end":1452,"id":"G3DSA:3.90.190.10","name":"Protein tyrosine phosphatase superfamily"}],"pfam":[{"id":"PF00041","name":"Fibronectin type III domain","start":498,"end":577},{"id":"PF00047","name":"Immunoglobulin domain","start":192,"end":269},{"id":"PF00102","name":"Protein-tyrosine phosphatase","start":923,"end":1153},{"id":"PF00102","name":"Protein-tyrosine phosphatase","start":1213,"end":1447},{"id":"PF00629","name":"MAM domain, meprin/A5/mu","start":27,"end":182},{"id":"PF23144","name":"Receptor-type tyrosine-protein phosphatase U Fn3 domain","start":583,"end":724}]},"disprot_id":"DP02580","regions_counter":3,"dataset":[],"UniParc":"UPI0000132997","uniref100":"UniRef100_P28827","uniref90":"UniRef90_P28827","uniref50":"UniRef50_P28827","genes":[{"name":{"value":"PTPRM"},"synonyms":[{"value":"PTPRL1"}]}],"alphafold_very_low_content":0.10674931129476584,"disorder_content":0.10606060606060606,"disprot_consensus":{"full":[{"start":589,"end":742,"type":"D"}],"Structural state":[{"start":589,"end":742,"type":"D"}]}},{"acc":"F1RAX4","name":"Receptor for retinol uptake stra6","sequence":"MSAETVNNYDYSDWYENAAPTKAPVEVIPPCDPTADEGLFHICIAAISLVVMLVLAILARRQKLSDNQRGLTGLLSPVNFLDHTQHKGLAVAVYGVLFCKLVGMVLSHHPLPFTKEVANKEFWMILALLYYPALYYPLLACGTLHNKVGYVLGSLLSWTHFGILVWQKVDCPKTPQIYKYYALFGSLPQIACLAFLSFQYPLLLFKGLQNTETANASEDLSSSYYRDYVKKILKKKKPTKISSSTSKPKLFDRLRDAVKSYIYTPEDVFRFPLKLAISVVVAFIALYQMALLLISGVLPTLHIVRRGVDENIAFLLAGFNIILSNDRQEVVRIVVYYLWCVEICYVSAVTLSCLVNLLMLMRSMVLHRSNLKGLYRGDSLNVFNCHRSIRPSRPALVCWMGFTSYQAAFLCLGMAIQTLVFFICILFAVFLIIIPILWGTNLMLFHIIGNLWPFWLTLVLAALIQHVASRFLFIRKDGGTRDLNNRGSLFLLSYILFLVNVMIGVVLGIWRVVITALFNIVHLGRLDISLLNRNVEAFDPGYRCYSHYLKIEVSQSHPVMKAFCGLLLQSSGQDGLSAQRIRDAEEGIQLVQQEKKQNKVSNAKRARAHWQLLYTLVNNPSLVGSRKHFQCQSSESFINGALSRTSKEGSKKDGSVNEPSKEAESAAASN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Actinopterygii","Neopterygii","Teleostei","Ostariophysi","Cypriniformes","Danionidae","Danioninae","Danio"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":597,"region_id":"DP02583r001","start":575,"term_id":"IDPO:0000002","statement":[{"text":"Two C-terminal CaM-binding helices (CaMBP1 and CaMBP2) follow, linked by a disordered segment (Fig. 1, D and E).","type":"Article"},{"text":"The disordered CaMBP1-CaMBP2 linker is conserved in sequence for its central and acidic motif, EEGIQLV in zebrafish STRA6, with the Glu-Gly segment invariant across STRA6 orthologs","type":"Article"},{"text":"CaMBP1 and CaMBP2 are connected by a linker, that is disordered in the structure and that contains a conserved sequence motif (EEGIQLV; fig. S7) similar to the box2 motif of cytokine receptors, which is known to mediate recruitment of JAK family members through their FERM and SH2 domains","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27563101","version":2,"reference_html":"Structure of the STRA6 receptor for retinol uptake. <i> Chen Y, Clarke OB, Kim J, Stowe S, Kim YK, Assur Z, Cavalier M, Godoy-Ruiz R, von Alpen DC, Manzini C, Blaner WS, Frank J, Quadro L, Weber DJ, Shapiro L, Hendrickson WA, Mancia F. </i> Science, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"5SY1"},{"db":"PDB","id":"5K8Q"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":597,"region_id":"DP02583r002","start":575,"term_id":"IDPO:0000033","statement":[{"text":"Two C-terminal CaM-binding helices (CaMBP1 and CaMBP2) follow, linked by a disordered segment (Fig. 1, D and E).","type":"Article"},{"text":"The disordered CaMBP1-CaMBP2 linker is conserved in sequence for its central and acidic motif, EEGIQLV in zebrafish STRA6, with the Glu-Gly segment invariant across STRA6 orthologs","type":"Article"},{"text":"CaMBP1 and CaMBP2 are connected by a linker, that is disordered in the structure and that contains a conserved sequence motif (EEGIQLV; fig. S7) similar to the box2 motif of cytokine receptors, which is known to mediate recruitment of JAK family members through their FERM and SH2 domains","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27563101","version":3,"reference_html":"Structure of the STRA6 receptor for retinol uptake. <i> Chen Y, Clarke OB, Kim J, Stowe S, Kim YK, Assur Z, Cavalier M, Godoy-Ruiz R, von Alpen DC, Manzini C, Blaner WS, Frank J, Quadro L, Weber DJ, Shapiro L, Hendrickson WA, Mancia F. </i> Science, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","cross_refs":[{"db":"PDB","id":"5SY1"},{"db":"PDB","id":"5K8Q"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":591,"region_id":"DP02583r003","start":585,"term_id":"GO:0060090","statement":[{"text":"CaMBP1 and CaMBP2 are connected by a linker, that is disordered in the structure and that contains a conserved sequence motif (EEGIQLV; fig. S7) similar to the box2 motif of cytokine receptors, which is known to mediate recruitment of JAK family members through their FERM and SH2 domains","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"27563101","version":3,"reference_html":"Structure of the STRA6 receptor for retinol uptake. <i> Chen Y, Clarke OB, Kim J, Stowe S, Kim YK, Assur Z, Cavalier M, Godoy-Ruiz R, von Alpen DC, Manzini C, Blaner WS, Frank J, Quadro L, Weber DJ, Shapiro L, Hendrickson WA, Mancia F. </i> Science, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","cross_refs":[{"db":"PDB","id":"5SY1"},{"db":"PDB","id":"5K8Q"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_12","length":670,"ncbi_taxon_id":7955,"date":"2020-02-20T12:09:47.840Z","organism":"Danio rerio","features":{"gene3D":[],"pfam":[{"id":"PF14752","name":"Retinol binding protein receptor","start":29,"end":628}]},"disprot_id":"DP02583","regions_counter":3,"dataset":[],"UniParc":"UPI000151DFE9","uniref100":"UniRef100_F1RAX4","uniref90":"UniRef90_F1RAX4","uniref50":"UniRef50_F1RAX4","genes":[{"name":{"value":"stra6","evidences":[{"code":"ECO:0000312","source":{"name":"Ensembl","id":"ENSDARP00000067478","url":"https://www.ensembl.org/id/ENSDARP00000067478"}},{"code":"ECO:0000312","source":{"name":"ZFIN","id":"ZDB-GENE-060616-252","url":"http://zfin.org/cgi-bin/webdriver?MIval=aa-markerview.apg&OID=ZDB-GENE-060616-252"}}]}}],"alphafold_very_low_content":0.08656716417910448,"disorder_content":0.034328358208955224,"disprot_consensus":{"full":[{"start":575,"end":597,"type":"D"}],"Structural state":[{"start":575,"end":597,"type":"D"}],"Disorder function":[{"start":575,"end":597,"type":"F"}],"Molecular function":[{"start":585,"end":591,"type":"F"}]}},{"acc":"F1QGH7","name":"Catenin beta-1","sequence":"MATQSDLMELEMAMDPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEDDDVDNQVLYEWEQGFNQSFNQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDSAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTSGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQDAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDIHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMTWNETGDLGLDIGAQGEPLGYRQDDPSYRSFHSGGYGQDAMGMDPMMEHEMAGHHPGPDYPVDGLPDLGHTQDLIDGLPPGDSNQLAWFDTDL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Actinopterygii","Neopterygii","Teleostei","Ostariophysi","Cypriniformes","Danionidae","Danioninae","Danio"],"creator":"fquaglia","regions":[{"region_id":"DP02584r001","ec_ontology":"ECO","end":126,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"No clear electron density was observed for the two terminal domains except for the helix C in the C-terminal domain and an additional α helix flanking the N terminus of armadillo repeat 1.","type":"Results"},{"text":"The final crystal structure obtained from full-length zebrafish β-catenin protein crystals contains residues 126–681","type":"Results"},{"text":"Our crystal structures demonstrate that the N- and C-terminal domains of β-catenin are structurally flexible and clearly do not interact with the armadillo repeat domain with a static conformation.","type":"Results"},{"text":"In our crystal structures, the N- and the C-terminal tails are disordered despite the presence of intact β-catenin R1C and full-length β-catenin in respective crystals. Therefore, we conclude that the N- and C-terminal tails do not interact with the armadillo repeat domain with a specific conformation.","type":"Discussion"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18334222","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2Z6G"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Crystal structure of a full-length beta-catenin. <i> Xing Y, Takemaru K, Liu J, Berndt JD, Zheng JJ, Moon RT, Xu W. </i> Structure, 2008","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02584r002","ec_ontology":"ECO","end":780,"term_id":"IDPO:0000002","start":680,"version":2,"statement":[{"text":"No clear electron density was observed for the two terminal domains except for the helix C in the C-terminal domain and an additional α helix flanking the N terminus of armadillo repeat 1.","type":"Results"},{"text":"The final crystal structure obtained from full-length zebrafish β-catenin protein crystals contains residues 126–681","type":"Results"},{"text":"Our crystal structures demonstrate that the N- and C-terminal domains of β-catenin are structurally flexible and clearly do not interact with the armadillo repeat domain with a static conformation.","type":"Results"},{"text":"In our crystal structures, the N- and the C-terminal tails are disordered despite the presence of intact β-catenin R1C and full-length β-catenin in respective crystals. Therefore, we conclude that the N- and C-terminal tails do not interact with the armadillo repeat domain with a specific conformation.","type":"Discussion"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18334222","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2Z6G"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Crystal structure of a full-length beta-catenin. <i> Xing Y, Takemaru K, Liu J, Berndt JD, Zheng JJ, Moon RT, Xu W. </i> Structure, 2008","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":780,"ncbi_taxon_id":7955,"date":"2020-02-20T14:30:40.910Z","organism":"Danio rerio","features":{"gene3D":[{"start":132,"end":685,"id":"G3DSA:1.25.10.10","name":"Leucine-rich Repeat Variant"}],"pfam":[{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":228,"end":261},{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":350,"end":389},{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":431,"end":472},{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":584,"end":621}]},"disprot_id":"DP02584","regions_counter":2,"dataset":[],"UniParc":"UPI000024D4A9","uniref100":"UniRef100_F1QGH7","uniref90":"UniRef90_Q02248","uniref50":"UniRef50_Q02248","genes":[{"name":{"value":"ctnnb1","evidences":[{"code":"ECO:0000312","source":{"name":"ZFIN","id":"ZDB-GENE-980526-362","url":"http://zfin.org/cgi-bin/webdriver?MIval=aa-markerview.apg&OID=ZDB-GENE-980526-362"}}]}}],"alphafold_very_low_content":0.2153846153846154,"disorder_content":0.29102564102564105,"disprot_consensus":{"full":[{"start":1,"end":126,"type":"D"},{"start":680,"end":780,"type":"D"}],"Structural state":[{"start":1,"end":126,"type":"D"},{"start":680,"end":780,"type":"D"}]}},{"acc":"Q9H900","name":"Protein zwilch homolog","sequence":"MWERLNCAAEDFYSRLLQKFNEEKKGIRKDPFLYEADVQVQLISKGQPNPLKNILNENDIVFIVEKVPLEKEETSHIEELQSEETAISDFSTGENVGPLALPVGKARQLIGLYTMAHNPNMTHLKINLPVTALPPLWVRCDSSDPEGTCWLGAELITTNNSITGIVLYVVSCKADKNYSVNLENLKNLHKKRHHLSTVTSKGFAQYELFKSSALDDTITASQTAIALDISWSPVDEILQIPPLSSTATLNIKVESGEPRGPLNHLYRELKFLLVLADGLRTGVTEWLEPLEAKSAVELVQEFLNDLNKLDGFGDSTKKDTEVETLKHDTAAVDRSVKRLFKVRSDLDFAEQLWCKMSSSVISYQDLVKCFTLIIQSLQRGDIQPWLHSGSNSLLSKLIHQSYHGTMDTVSLSGTIPVQMLLEIGLDKLKKDYISFFIGQELASLNHLEYFIAPSVDIQEQVYRVQKLHHILEILVSCMPFIKSQHELLFSLTQICIKYYKQNPLDEQHIFQLPVRPTAVKNLYQSEKPQKWRVEIYSGQKKIKTVWQLSDSSPIDHLNFHKPDFSELTLNGSLEERIFFTNMVTCSQVHFK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":263,"region_id":"DP02585r001","start":253,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Domain 1 is connected to domain 2 (residues 264–505) through a flexible connector (residues 253–263) that is invisible in the electron density.","type":"Results"},{"text":"The final model includes residues 1–68, 99–211, 222–252, 264–309, 339–560, and 576–590 as well as five additional residues at the N terminus left after the removal of the tag.","type":"Methods"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20462495","version":2,"reference_html":"Structural analysis of the RZZ complex reveals common ancestry with multisubunit vesicle tethering machinery. <i> Civril F, Wehenkel A, Giorgi FM, Santaguida S, Di Fonzo A, Grigorean G, Ciccarelli FD, Musacchio A. </i> Structure, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3IF8"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-05T13:48:36.459Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":263,"region_id":"DP02585r002","start":253,"term_id":"IDPO:0000033","unpublished":true,"statement":[{"text":"Domain 1 is connected to domain 2 (residues 264–505) through a flexible connector (residues 253–263) that is invisible in the electron density.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20462495","version":3,"reference_html":"Structural analysis of the RZZ complex reveals common ancestry with multisubunit vesicle tethering machinery. <i> Civril F, Wehenkel A, Giorgi FM, Santaguida S, Di Fonzo A, Grigorean G, Ciccarelli FD, Musacchio A. </i> Structure, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3IF8"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-05T13:56:34.222Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":98,"region_id":"DP02585r003","start":69,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The final model includes residues 1–68, 99–211, 222–252, 264–309, 339–560, and 576–590 as well as five additional residues at the N terminus left after the removal of the tag.","type":"Methods"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20462495","version":2,"reference_html":"Structural analysis of the RZZ complex reveals common ancestry with multisubunit vesicle tethering machinery. <i> Civril F, Wehenkel A, Giorgi FM, Santaguida S, Di Fonzo A, Grigorean G, Ciccarelli FD, Musacchio A. </i> Structure, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3IF8"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-05T13:47:05.239Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":221,"region_id":"DP02585r004","start":212,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The final model includes residues 1–68, 99–211, 222–252, 264–309, 339–560, and 576–590 as well as five additional residues at the N terminus left after the removal of the tag.","type":"Methods"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20462495","version":2,"reference_html":"Structural analysis of the RZZ complex reveals common ancestry with multisubunit vesicle tethering machinery. <i> Civril F, Wehenkel A, Giorgi FM, Santaguida S, Di Fonzo A, Grigorean G, Ciccarelli FD, Musacchio A. </i> Structure, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3IF8"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-05T13:47:48.605Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":338,"region_id":"DP02585r005","start":310,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The final model includes residues 1–68, 99–211, 222–252, 264–309, 339–560, and 576–590 as well as five additional residues at the N terminus left after the removal of the tag.","type":"Methods"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20462495","version":2,"reference_html":"Structural analysis of the RZZ complex reveals common ancestry with multisubunit vesicle tethering machinery. <i> Civril F, Wehenkel A, Giorgi FM, Santaguida S, Di Fonzo A, Grigorean G, Ciccarelli FD, Musacchio A. </i> Structure, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3IF8"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-05T13:49:54.390Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":575,"region_id":"DP02585r006","start":561,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The final model includes residues 1–68, 99–211, 222–252, 264–309, 339–560, and 576–590 as well as five additional residues at the N terminus left after the removal of the tag.","type":"Methods"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20462495","version":2,"reference_html":"Structural analysis of the RZZ complex reveals common ancestry with multisubunit vesicle tethering machinery. <i> Civril F, Wehenkel A, Giorgi FM, Santaguida S, Di Fonzo A, Grigorean G, Ciccarelli FD, Musacchio A. </i> Structure, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3IF8"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-05T13:50:24.980Z"}}],"released":"2023_12","length":591,"ncbi_taxon_id":9606,"date":"2020-02-20T14:43:38.960Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF09817","name":"RZZ complex, subunit zwilch","start":31,"end":572}]},"disprot_id":"DP02585","regions_counter":7,"dataset":[],"UniParc":"UPI0000070024","uniref100":"UniRef100_Q9H900","uniref90":"UniRef90_Q9H900","uniref50":"UniRef50_Q9H900","genes":[{"name":{"value":"ZWILCH"}}],"alphafold_very_low_content":0.12521150592216582,"disorder_content":0.16074450084602368,"disprot_consensus":{"full":[{"start":69,"end":98,"type":"D"},{"start":212,"end":221,"type":"D"},{"start":253,"end":263,"type":"D"},{"start":310,"end":338,"type":"D"},{"start":561,"end":575,"type":"D"}],"Structural state":[{"start":69,"end":98,"type":"D"},{"start":212,"end":221,"type":"D"},{"start":253,"end":263,"type":"D"},{"start":310,"end":338,"type":"D"},{"start":561,"end":575,"type":"D"}],"Disorder function":[{"start":253,"end":263,"type":"F"}]}},{"acc":"P10761","name":"Zona pellucida sperm-binding protein 3","sequence":"MASSYFLFLCLLLCGGPELCNSQTLWLLPGGTPTPVGSSSPVKVECLEAELVVTVSRDLFGTGKLVQPGDLTLGSEGCQPRVSVDTDVVRFNAQLHECSSRVQMTKDALVYSTFLLHDPRPVSGLSILRTNRVEVPIECRYPRQGNVSSHPIQPTWVPFRATVSSEEKLAFSLRLMEENWNTEKSAPTFHLGEVAHLQAEVQTGSHLPLQLFVDHCVATPSPLPDPNSSPYHFIVDFHGCLVDGLSESFSAFQVPRPRPETLQFTVDVFHFANSSRNTLYITCHLKVAPANQIPDKLNKACSFNKTSQSWLPVEGDADICDCCSHGNCSNSSSSQFQIHGPRQWSKLVSRNRRHVTDEADVTVGPLIFLGKANDQTVEGWTASAQTSVALGLGLATVAFLTLAAIVLAVTRKCHSSSYLVSLPQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":131,"region_id":"DP02586r001","start":119,"term_id":"IDPO:0000002","statement":[{"text":"No electron density could be observed for FG loop residues Pro 119–Asn 131 in the P21212 map.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19052627","version":2,"reference_html":"Crystal structure of the ZP-N domain of ZP3 reveals the core fold of animal egg coats. <i> Monné M, Han L, Schwend T, Burendahl S, Jovine L. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3D4C"},{"db":"PDB","id":"3EF7"},{"db":"PDB","id":"3D4G"},{"db":"PDB","id":"5OSQ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":424,"ncbi_taxon_id":10090,"date":"2020-02-20T16:40:48.211Z","organism":"Mus musculus","features":{"gene3D":[],"pfam":[{"id":"PF00100","name":"ZP-C domain","start":166,"end":302},{"id":"PF23344","name":"ZP-N domain","start":46,"end":142}]},"disprot_id":"DP02586","regions_counter":1,"dataset":[],"UniParc":"UPI0000027910","uniref100":"UniRef100_P10761","uniref90":"UniRef90_P10761","uniref50":"UniRef50_P21754","genes":[{"name":{"value":"Zp3"},"synonyms":[{"value":"Zp-3"},{"value":"Zpc"}]}],"alphafold_very_low_content":0.21462264150943397,"disorder_content":0.030660377358490566,"disprot_consensus":{"full":[{"start":119,"end":131,"type":"D"}],"Structural state":[{"start":119,"end":131,"type":"D"}]}},{"acc":"Q96PM5","name":"RING finger and CHY zinc finger domain-containing protein 1","sequence":"MAATAREDGASGQERGQRGCEHYDRGCLLKAPCCDKLYTCRLCHDNNEDHQLDRFKVKEVQCINCEKIQHAQQTCEECSTLFGEYYCDICHLFDKDKKQYHCENCGICRIGPKEDFFHCLKCNLCLAMNLQGRHKCIENVSRQNCPICLEDIHTSRVVAHVLPCGHLLHRTCYEEMLKEGYRCPLCMHSALDMTRYWRQLDDEVAQTPMPSEYQNMTVDILCNDCNGRSTVQFHILGMKCKICESYNTAQAGGRRISLDQQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":215,"region_id":"DP02587r001","start":187,"term_id":"IDPO:0000002","statement":[{"text":"The structure of the Pirh2 CTD consists of a 30-residue disordered loop (residues 187–215) followed by a compact, globular fold that incorporates a single zinc ion with four cysteine thiol groups (residues Cys222, Cys225, Cys240 and Cys243) forming a tetrahedral zinc coordination (Fig. 2c). Residues 198 to 205 within the unstructured region showed some α-helical propensity based on their backbone NMR resonances.","type":"Results"},{"text":"In contrast, the 30 amino-acid linker between the RING and the CTD (~30 residues) gives Pirh2 great flexibility to bring together the ubiquitin-charged E2 enzyme with substrates.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19043414","version":2,"reference_html":"Molecular basis of Pirh2-mediated p53 ubiquitylation. <i> Sheng Y, Laister RC, Lemak A, Wu B, Tai E, Duan S, Lukin J, Sunnerhagen M, Srisailam S, Karra M, Benchimol S, Arrowsmith CH. </i> Nat Struct Mol Biol, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"2K2D"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":215,"region_id":"DP02587r002","start":187,"term_id":"IDPO:0000033","statement":[{"text":"The structure of the Pirh2 CTD consists of a 30-residue disordered loop (residues 187–215) followed by a compact, globular fold that incorporates a single zinc ion with four cysteine thiol groups (residues Cys222, Cys225, Cys240 and Cys243) forming a tetrahedral zinc coordination (Fig. 2c). Residues 198 to 205 within the unstructured region showed some α-helical propensity based on their backbone NMR resonances.","type":"Results"},{"text":"In contrast, the 30 amino-acid linker between the RING and the CTD (~30 residues) gives Pirh2 great flexibility to bring together the ubiquitin-charged E2 enzyme with substrates.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19043414","version":3,"reference_html":"Molecular basis of Pirh2-mediated p53 ubiquitylation. <i> Sheng Y, Laister RC, Lemak A, Wu B, Tai E, Duan S, Lukin J, Sunnerhagen M, Srisailam S, Karra M, Benchimol S, Arrowsmith CH. </i> Nat Struct Mol Biol, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"2K2D"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","length":261,"ncbi_taxon_id":9606,"date":"2020-02-20T17:11:35.783Z","organism":"Homo sapiens","features":{"gene3D":[{"start":138,"end":189,"id":"G3DSA:3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"}],"pfam":[{"id":"PF05495","name":"CHY zinc finger","start":20,"end":85},{"id":"PF13639","name":"Ring finger domain","start":144,"end":186},{"id":"PF14599","name":"Zinc-ribbon","start":191,"end":248}]},"disprot_id":"DP02587","regions_counter":2,"dataset":[],"UniParc":"UPI000013C366","uniref100":"UniRef100_Q96PM5","uniref90":"UniRef90_Q96PM5","uniref50":"UniRef50_Q96PM5","genes":[{"name":{"value":"RCHY1"},"synonyms":[{"value":"ARNIP"},{"value":"CHIMP"},{"value":"PIRH2"},{"value":"RNF199"},{"value":"ZNF363"}]}],"alphafold_very_low_content":0.06130268199233716,"disorder_content":0.1111111111111111,"disprot_consensus":{"full":[{"start":187,"end":215,"type":"D"}],"Structural state":[{"start":187,"end":215,"type":"D"}],"Disorder function":[{"start":187,"end":215,"type":"F"}]}},{"acc":"P47273","name":"Uncharacterized protein MG027","sequence":"MAITVKGLTNKLTRTQRRIAVVEFIFSLLFFLPKEAEVIQADFLEYDTKERQLNEWQKLIVKAFSENIFSFQKKIEEQQLKNQLEIQTKYNKISGKKIDLLTTAVVLCALSEQKAHNTDKPLLISEALLIMDHYSQGAEKKQTHALLDKLL","taxonomy":["Bacteria","Tenericutes","Mollicutes","Mycoplasmataceae","Mycoplasma"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":99,"region_id":"DP02588r001","start":78,"term_id":"IDPO:0000002","statement":[{"text":"In MG027, the loop region (between residue 78 to 99) that connects H4 and H5 is much longer than the corresponding loop in mt‐nusB (between residue 76 to 86) and other nusB proteins (Fig. 3). This loop is mostly exposed in the solvent region and is disordered in MG027 structure.","type":"Results"},{"text":"No density was visible for the first 11 N‐terminal amino acids and part of the loop region that connects α‐helix 4 (H4) and α‐helix 5 (H5)","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15146506","version":2,"reference_html":"A conserved hypothetical protein from Mycoplasma genitalium shows structural homology to nusb proteins. <i> Liu J, Yokota H, Kim R, Kim SH. </i> Proteins, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1Q8C"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":11,"region_id":"DP02588r002","start":1,"term_id":"IDPO:0000002","statement":[{"text":"In MG027, the loop region (between residue 78 to 99) that connects H4 and H5 is much longer than the corresponding loop in mt‐nusB (between residue 76 to 86) and other nusB proteins (Fig. 3). This loop is mostly exposed in the solvent region and is disordered in MG027 structure.","type":"Results"},{"text":"No density was visible for the first 11 N‐terminal amino acids and part of the loop region that connects α‐helix 4 (H4) and α‐helix 5 (H5)","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15146506","version":2,"reference_html":"A conserved hypothetical protein from Mycoplasma genitalium shows structural homology to nusb proteins. <i> Liu J, Yokota H, Kim R, Kim SH. </i> Proteins, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1Q8C"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":151,"ncbi_taxon_id":243273,"date":"2020-02-20T17:53:25.391Z","organism":"Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195)","features":{"gene3D":[{"start":1,"end":151,"id":"G3DSA:1.10.940.10","name":"NusB-like"}],"pfam":[{"id":"PF09185","name":"Domain of unknown function (DUF1948)","start":12,"end":151}]},"disprot_id":"DP02588","regions_counter":2,"dataset":[],"UniParc":"UPI0000139129","uniref100":"UniRef100_P47273","uniref90":"UniRef90_P47273","uniref50":"UniRef50_P47273","genes":[{"olnNames":[{"value":"MG027"}]}],"alphafold_very_low_content":0.06622516556291391,"disorder_content":0.2185430463576159,"disprot_consensus":{"full":[{"start":1,"end":11,"type":"D"},{"start":78,"end":99,"type":"D"}],"Structural state":[{"start":1,"end":11,"type":"D"},{"start":78,"end":99,"type":"D"}]}},{"acc":"Q05080","name":"Cytokinesis protein 2","sequence":"MSYSYEACFWDPNDNGVNILLGHISQGIRSCDSMILFFKQRSELEKDYARRLGAITGKLDKDIGTNMDYGKLNETFNVVLSVEKARAQSHSKQSEILFRQIYTDTKAFAANLQARYTTLSGKIERLRMDKFNKKKGCEVLQKKLQDAQIRFRDLQLNENNMIGAKRVEHNKRELLKWESNSQEYKVQLDVLKQEYKASQKFWIHEWAQLSCELQEMENARISFLQSKLQQFATSSMETYILEQTKMDMLTNHLNSFTAADEISTFSKENGTGRLKHKTSKGDMNSSANWAQMSSISTTSKKTESYMDNIRKLSSQLKETENKRKLASIDKYEKPLPSPEVTMATQFRNSTPVIRNETKVVANPTLSLRSSPVQLQSNVDDSVLRQKPDKPRPIVGEEQLKPDEDSKNPDEKGLMVHKRNQSLSSPSESSSSNPTDFSHIKKRQSMESMTTSVSSMANSIDDSQRFAKSWNSSNRKRKSMSHLQVPSSASSRSDDGGRTPNSAHNLNEDDYNTRRDTSTSTILFKPPVAVRGTSRGHTHRQSMIMQDSSNPIEDALYEMERIQSSSKPGTKTGNIMDERGVVRDRGITVTLPIVTSEGFPVIEYAKAMYPLIGNEAPGLANFHKGDYLLITEIVNKDWYKGEVYDNDRIDRNHRIGLIPYNFIQLLHQGL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":300,"region_id":"DP02589r001","start":276,"term_id":"IDPO:0000002","statement":[{"text":"An unstructured carboxy-terminal region follows helix α5 in each monomer and also packs against its dimerization partner.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"25620000","version":2,"reference_html":"Comparison of Saccharomyces cerevisiae F-BAR domain structures reveals a conserved inositol phosphate binding site. <i> Moravcevic K, Alvarado D, Schmitz KR, Kenniston JA, Mendrola JM, Ferguson KM, Lemmon MA. </i> Structure, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4WPE"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":669,"ncbi_taxon_id":559292,"date":"2020-02-27T08:43:33.581Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","features":{"gene3D":[{"start":1,"end":275,"id":"G3DSA:1.20.1270.60","name":"Arfaptin homology (AH) domain/BAR domain"}],"pfam":[{"id":"PF00611","name":"Fes/CIP4, and EFC/F-BAR homology domain","start":16,"end":92}]},"disprot_id":"DP02589","regions_counter":1,"dataset":[],"UniParc":"UPI0000128C32","uniref100":"UniRef100_Q05080","uniref90":"UniRef90_Q05080","uniref50":"UniRef50_Q05080","genes":[{"name":{"value":"HOF1"},"synonyms":[{"value":"CYK2"}],"orfNames":[{"value":"YM9973.05"}],"olnNames":[{"value":"YMR032W"}]}],"alphafold_very_low_content":0.3796711509715994,"disorder_content":0.03736920777279522,"disprot_consensus":{"full":[{"start":276,"end":300,"type":"D"}],"Structural state":[{"start":276,"end":300,"type":"D"}]}},{"acc":"P47523","name":"Uncharacterized protein MG281","sequence":"MQFKKHKNSVKFKRKLFWTIGVLGAGALTTFSAVMITNLVNQSGYALVASGRSGNLGFKLFSTQSPSAEVKLKSLSLNDGSYQSEIDLSGGANFREKFRNFANELSEAITNSPKGLDRPVPKTEISGLIKTGDNFITPSFKAGYYDHVASDGSLLSYYQSTEYFNNRVLMPILQTTNGTLMANNRGYDDVFRQVPSFSGWSNTKATTVSTSNNLTYDKWTYFAAKGSPLYDSYPNHFFEDVKTLAIDAKDISALKTTIDSEKPTYLIIRGLSGNGSQLNELQLPESVKKVSLYGDYTGVNVAKQIFANVVELEFYSTSKANSFGFNPLVLGSKTNVIYDLFASKPFTHIDLTQVTLQNSDNSAIDANKLKQAVGDIYNYRRFERQFQGYFAGGYIDKYLVKNVNTNKDSDDDLVYRSLKELNLHLEEAYREGDNTYYRVNENYYPGASIYENERASRDSEFQNEILKRAEQNGVTFDENIKRITASGKYSVQFQKLENDTDSSLERMTKAVEGLVTVIGEEKFETVDITGVSSDTNEVKSLAKELKTNALGVKLKL","taxonomy":["Bacteria","Tenericutes","Mollicutes","Mycoplasmataceae","Mycoplasma"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":74,"region_id":"DP02590r001","start":37,"term_id":"IDPO:0000002","statement":[{"text":"The N- and C-terminal fragments (residues 37 to 74 and residues 469 to 556), which were truncated in Protein M TD as compared with Protein M, are likely disordered because the three-dimensional reconstructions of a Fab in complex with Protein M and Protein M TD by using negative-stain electron microscopy are nearly identical","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24503852","version":2,"reference_html":"A structurally distinct human mycoplasma protein that generically blocks antigen-antibody union. <i> Grover RK, Zhu X, Nieusma T, Jones T, Boreo I, MacLeod AS, Mark A, Niessen S, Kim HJ, Kong L, Assad-Garcia N, Kwon K, Chesi M, Smider VV, Salomon DR, Jelinek DF, Kyle RA, Pyles RB, Glass JI, Ward AB, Wilson IA, Lerner RA. </i> Science, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4NZT"},{"db":"PDB","id":"4NZR"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":468,"region_id":"DP02590r002","start":455,"term_id":"IDPO:0000002","statement":[{"text":"Residues 455 to 468 in domain II of Protein M TD were flexible and not modeled.","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24503852","version":2,"reference_html":"A structurally distinct human mycoplasma protein that generically blocks antigen-antibody union. <i> Grover RK, Zhu X, Nieusma T, Jones T, Boreo I, MacLeod AS, Mark A, Niessen S, Kim HJ, Kong L, Assad-Garcia N, Kwon K, Chesi M, Smider VV, Salomon DR, Jelinek DF, Kyle RA, Pyles RB, Glass JI, Ward AB, Wilson IA, Lerner RA. </i> Science, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4NZT"},{"db":"PDB","id":"4NZR"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":74,"region_id":"DP02590r003","start":37,"term_id":"IDPO:0000002","statement":[{"text":"The N- and C-terminal fragments (residues 37 to 74 and residues 469 to 556), which were truncated in Protein M TD as compared with Protein M, are likely disordered because the three-dimensional reconstructions of a Fab in complex with Protein M and Protein M TD by using negative-stain electron microscopy are nearly identical","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"microscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24503852","version":2,"reference_html":"A structurally distinct human mycoplasma protein that generically blocks antigen-antibody union. <i> Grover RK, Zhu X, Nieusma T, Jones T, Boreo I, MacLeod AS, Mark A, Niessen S, Kim HJ, Kong L, Assad-Garcia N, Kwon K, Chesi M, Smider VV, Salomon DR, Jelinek DF, Kyle RA, Pyles RB, Glass JI, Ward AB, Wilson IA, Lerner RA. </i> Science, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001232","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":556,"region_id":"DP02590r004","start":469,"term_id":"IDPO:0000002","statement":[{"text":"The N- and C-terminal fragments (residues 37 to 74 and residues 469 to 556), which were truncated in Protein M TD as compared with Protein M, are likely disordered because the three-dimensional reconstructions of a Fab in complex with Protein M and Protein M TD by using negative-stain electron microscopy are nearly identical","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"microscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24503852","version":2,"reference_html":"A structurally distinct human mycoplasma protein that generically blocks antigen-antibody union. <i> Grover RK, Zhu X, Nieusma T, Jones T, Boreo I, MacLeod AS, Mark A, Niessen S, Kim HJ, Kong L, Assad-Garcia N, Kwon K, Chesi M, Smider VV, Salomon DR, Jelinek DF, Kyle RA, Pyles RB, Glass JI, Ward AB, Wilson IA, Lerner RA. </i> Science, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001232","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":556,"region_id":"DP02590r005","start":469,"term_id":"IDPO:0000031","statement":[{"text":"The N- and C-terminal fragments (residues 37 to 74 and residues 469 to 556), which were truncated in Protein M TD as compared with Protein M, are likely disordered because the three-dimensional reconstructions of a Fab in complex with Protein M and Protein M TD by using negative-stain electron microscopy are nearly identical","type":"Article"},{"text":"These structural studies suggested that Protein M should preclude the ability of the antibody to bind to its antigen because it displaces or distorts the CDRs and/or may use its C-terminal domain to sterically block entrance to the antibody-combining site","type":"Article"},{"text":"Protein M blocks antibody-antigen union, likely because of its large C-terminal domain extending over the antibody-combining site, blocking entry to large antigens.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"microscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24503852","version":3,"reference_html":"A structurally distinct human mycoplasma protein that generically blocks antigen-antibody union. <i> Grover RK, Zhu X, Nieusma T, Jones T, Boreo I, MacLeod AS, Mark A, Niessen S, Kim HJ, Kong L, Assad-Garcia N, Kwon K, Chesi M, Smider VV, Salomon DR, Jelinek DF, Kyle RA, Pyles RB, Glass JI, Ward AB, Wilson IA, Lerner RA. </i> Science, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001232","term_name":"flexible C-terminal tail","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Disorder function"}],"released":"2021_06","length":556,"ncbi_taxon_id":243273,"date":"2020-03-02T11:01:11.637Z","organism":"Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195)","features":{"gene3D":[],"pfam":[{"id":"PF20757","name":"Protein M, large region","start":79,"end":440},{"id":"PF22805","name":"Protein M, smaller domain","start":441,"end":468},{"id":"PF22806","name":"Protein M, C-terminal","start":469,"end":556}]},"disprot_id":"DP02590","regions_counter":5,"dataset":[],"UniParc":"UPI0000139579","uniref100":"UniRef100_P47523","uniref90":"UniRef90_P47523","uniref50":"UniRef50_P47523","genes":[{"olnNames":[{"value":"MG281"}]}],"alphafold_very_low_content":0.18884892086330934,"disorder_content":0.2517985611510791,"disprot_consensus":{"full":[{"start":37,"end":74,"type":"D"},{"start":455,"end":556,"type":"D"}],"Structural state":[{"start":37,"end":74,"type":"D"},{"start":455,"end":556,"type":"D"}],"Disorder function":[{"start":469,"end":556,"type":"F"}]}},{"acc":"P78362","name":"SRSF protein kinase 2","sequence":"MSVNSEKSSSSERPEPQQKAPLVPPPPPPPPPPPPPLPDPTPPEPEEEILGSDDEEQEDPADYCKGGYHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQLIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYVRRMAAEATEWQKAGAPPPSGSAVSTAPQQKPIGKISKNKKKKLKKKQKRQAELLEKRLQEIEELEREAERKIIEENITSAAPSNDQDGEYCPEVKLKTTGLEEAAEAETAKDNGEAEDQEEKEDAEKENIEKDEDDVDQELANIDPTWIESPKTNGHIENGPFSLEQQLDDEDDDEEDCPNPEEYNLDEPNAESDYTYSSSYEQFNGELPNGRHKIPESQFPEFSTSLFSGSLEPVACGSVLSEGSPLTEQEESSPSHDRSRTVSASSTGDLPKAKTRAADLLVNPLDPRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGEDYSRDEDHIAHIIELLGSIPRHFALSGKYSREFFNRRGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFTDFLIPMLEMVPEKRASAGECLRHPWLNS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":80,"region_id":"DP02591r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"a comparison between ΔNΔS-SRPK2 (4.5 mg/mL black line) and SRPK2 (0.16 mg/mL blue line) samples indicates that the polydisperse full-length version in solution contains disordered regions, which are the ones that lack in the truncated version.","type":"Figure"},{"text":"The scattering adjustment and pair-distribution function (Fig. 5) clearly depicts an elongated molecule profile in solution, because of the left side shift of the peak, as well as the tail on the q higher values [38]. The molecular dimensions RG (radius of gyration) and Dmax (maximum dimension) agree with each other between Guinier fit and p(r) calculations (Table 3). This elongated profile may suggest the contribution of the intrinsically unstructured regions SID and N-terminal for the oligomer formation.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31229549","version":2,"reference_html":"Insights into the full-length SRPK2 structure and its hydrodynamic behavior. <i> Barbosa ÉAA, Seraphim TV, Gandin CA, Teixeira LF, da Silva RAG, Righetto GL, Goncalves KA, Vasconcellos RS, Almeida MR, Silva Júnior A, Fietto JLR, Kobarg J, Gileadi C, Massirer KB, Borges JC, de Oliveira Neto M, Bressan GC. </i> Int J Biol Macromol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":511,"region_id":"DP02591r002","start":231,"term_id":"IDPO:0000002","statement":[{"text":"a comparison between ΔNΔS-SRPK2 (4.5 mg/mL black line) and SRPK2 (0.16 mg/mL blue line) samples indicates that the polydisperse full-length version in solution contains disordered regions, which are the ones that lack in the truncated version.","type":"Figure"},{"text":"The scattering adjustment and pair-distribution function (Fig. 5) clearly depicts an elongated molecule profile in solution, because of the left side shift of the peak, as well as the tail on the q higher values [38]. The molecular dimensions RG (radius of gyration) and Dmax (maximum dimension) agree with each other between Guinier fit and p(r) calculations (Table 3). This elongated profile may suggest the contribution of the intrinsically unstructured regions SID and N-terminal for the oligomer formation.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31229549","version":2,"reference_html":"Insights into the full-length SRPK2 structure and its hydrodynamic behavior. <i> Barbosa ÉAA, Seraphim TV, Gandin CA, Teixeira LF, da Silva RAG, Righetto GL, Goncalves KA, Vasconcellos RS, Almeida MR, Silva Júnior A, Fietto JLR, Kobarg J, Gileadi C, Massirer KB, Borges JC, de Oliveira Neto M, Bressan GC. </i> Int J Biol Macromol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":511,"region_id":"DP02591r003","start":231,"term_id":"IDPO:0000002","statement":[{"text":"CD analysis (Fig. 4C, Table 2) also revealed that SRPK2 is composed of random structure with some content of regular secondary structure. These data agree with a model where the bi-lobed folded kinase domain somehow coexists with the intrinsically unstructured segments","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31229549","version":2,"reference_html":"Insights into the full-length SRPK2 structure and its hydrodynamic behavior. <i> Barbosa ÉAA, Seraphim TV, Gandin CA, Teixeira LF, da Silva RAG, Righetto GL, Goncalves KA, Vasconcellos RS, Almeida MR, Silva Júnior A, Fietto JLR, Kobarg J, Gileadi C, Massirer KB, Borges JC, de Oliveira Neto M, Bressan GC. </i> Int J Biol Macromol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":80,"region_id":"DP02591r004","start":1,"term_id":"IDPO:0000002","statement":[{"text":"CD analysis (Fig. 4C, Table 2) also revealed that SRPK2 is composed of random structure with some content of regular secondary structure. These data agree with a model where the bi-lobed folded kinase domain somehow coexists with the intrinsically unstructured segments","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31229549","version":2,"reference_html":"Insights into the full-length SRPK2 structure and its hydrodynamic behavior. <i> Barbosa ÉAA, Seraphim TV, Gandin CA, Teixeira LF, da Silva RAG, Righetto GL, Goncalves KA, Vasconcellos RS, Almeida MR, Silva Júnior A, Fietto JLR, Kobarg J, Gileadi C, Massirer KB, Borges JC, de Oliveira Neto M, Bressan GC. </i> Int J Biol Macromol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":511,"region_id":"DP02591r005","start":231,"term_id":"GO:0140677","statement":[{"text":"the bi-lobed folded kinase domain somehow coexists with the intrinsically unstructured segments, which act as binding regions for other proteins [19] and contribute to the kinase processive activity over its substrates [18,41]. It is worth mentioning that the full-length kinase was quite active under in vitro experiments in our hands (data not shown).","type":"Results"},{"text":"In addition, together with an also intrinsically unstructured N-terminal extension, SID plays a critical role in the kinase processivity ability. This is mainly reached due to the N-terminal and SID nucleotide release factor action, which favors the ADP release from the active site during the catalysis [21].","type":"Introduction"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31229549","version":3,"reference_html":"Insights into the full-length SRPK2 structure and its hydrodynamic behavior. <i> Barbosa ÉAA, Seraphim TV, Gandin CA, Teixeira LF, da Silva RAG, Righetto GL, Goncalves KA, Vasconcellos RS, Almeida MR, Silva Júnior A, Fietto JLR, Kobarg J, Gileadi C, Massirer KB, Borges JC, de Oliveira Neto M, Bressan GC. </i> Int J Biol Macromol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"molecular function activator activity","curator_orcid":"0000-0003-0849-9312","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":80,"region_id":"DP02591r006","start":1,"term_id":"GO:0140677","statement":[{"text":"the bi-lobed folded kinase domain somehow coexists with the intrinsically unstructured segments, which act as binding regions for other proteins [19] and contribute to the kinase processive activity over its substrates [18,41]. It is worth mentioning that the full-length kinase was quite active under in vitro experiments in our hands (data not shown).","type":"Results"},{"text":"In addition, together with an also intrinsically unstructured N-terminal extension, SID plays a critical role in the kinase processivity ability. This is mainly reached due to the N-terminal and SID nucleotide release factor action, which favors the ADP release from the active site during the catalysis [21].","type":"Introduction"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31229549","version":3,"reference_html":"Insights into the full-length SRPK2 structure and its hydrodynamic behavior. <i> Barbosa ÉAA, Seraphim TV, Gandin CA, Teixeira LF, da Silva RAG, Righetto GL, Goncalves KA, Vasconcellos RS, Almeida MR, Silva Júnior A, Fietto JLR, Kobarg J, Gileadi C, Massirer KB, Borges JC, de Oliveira Neto M, Bressan GC. </i> Int J Biol Macromol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"molecular function activator activity","curator_orcid":"0000-0003-0849-9312","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":80,"region_id":"DP02591r007","start":1,"term_id":"IDPO:0000002","statement":[{"text":"In the aSEC experiments (Fig. 8A), the full-length SRPK2 was eluted with 11.5 mL, which is consistent with an apparent molecular mass equal to 220 ± 10 kDa. This value indicates species ranging between dimer and trimer species. The RS was determined to be 50 ± 1 Å, which yielded an f/f0 of 1.7 ± 0.1 (considering a monomeric form for SRPK2), indicating a highly elongated particle [46]. This shape could be due to the presence of unstructured regions in the full-length recombinant protein. The RG/RS ranging from 1.3 to 1.5 also suggests the presence of unstructured regions [37].","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"chromatography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31229549","version":2,"reference_html":"Insights into the full-length SRPK2 structure and its hydrodynamic behavior. <i> Barbosa ÉAA, Seraphim TV, Gandin CA, Teixeira LF, da Silva RAG, Righetto GL, Goncalves KA, Vasconcellos RS, Almeida MR, Silva Júnior A, Fietto JLR, Kobarg J, Gileadi C, Massirer KB, Borges JC, de Oliveira Neto M, Bressan GC. </i> Int J Biol Macromol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":511,"region_id":"DP02591r008","start":231,"term_id":"IDPO:0000002","statement":[{"text":"In the aSEC experiments (Fig. 8A), the full-length SRPK2 was eluted with 11.5 mL, which is consistent with an apparent molecular mass equal to 220 ± 10 kDa. This value indicates species ranging between dimer and trimer species. The RS was determined to be 50 ± 1 Å, which yielded an f/f0 of 1.7 ± 0.1 (considering a monomeric form for SRPK2), indicating a highly elongated particle [46]. This shape could be due to the presence of unstructured regions in the full-length recombinant protein. The RG/RS ranging from 1.3 to 1.5 also suggests the presence of unstructured regions [37].","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"chromatography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31229549","version":2,"reference_html":"Insights into the full-length SRPK2 structure and its hydrodynamic behavior. <i> Barbosa ÉAA, Seraphim TV, Gandin CA, Teixeira LF, da Silva RAG, Righetto GL, Goncalves KA, Vasconcellos RS, Almeida MR, Silva Júnior A, Fietto JLR, Kobarg J, Gileadi C, Massirer KB, Borges JC, de Oliveira Neto M, Bressan GC. </i> Int J Biol Macromol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":511,"region_id":"DP02591r009","start":231,"term_id":"IDPO:0000002","statement":[{"text":"The f/f0 values were calculated to be 1.64 ± 0.03 for the monomer and 1.51 ± 0.04 for the dimer, which corroborates the hypothesis that SRPK2, either the monomer or the dimer, presents an elongated shape [32], likely due to the unstructured regions, as indicated by the aSEC experiments.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"analytical ultracentrifugation evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31229549","version":2,"reference_html":"Insights into the full-length SRPK2 structure and its hydrodynamic behavior. <i> Barbosa ÉAA, Seraphim TV, Gandin CA, Teixeira LF, da Silva RAG, Righetto GL, Goncalves KA, Vasconcellos RS, Almeida MR, Silva Júnior A, Fietto JLR, Kobarg J, Gileadi C, Massirer KB, Borges JC, de Oliveira Neto M, Bressan GC. </i> Int J Biol Macromol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006275","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":80,"region_id":"DP02591r010","start":1,"term_id":"IDPO:0000002","statement":[{"text":"The f/f0 values were calculated to be 1.64 ± 0.03 for the monomer and 1.51 ± 0.04 for the dimer, which corroborates the hypothesis that SRPK2, either the monomer or the dimer, presents an elongated shape [32], likely due to the unstructured regions, as indicated by the aSEC experiments.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"analytical ultracentrifugation evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31229549","version":2,"reference_html":"Insights into the full-length SRPK2 structure and its hydrodynamic behavior. <i> Barbosa ÉAA, Seraphim TV, Gandin CA, Teixeira LF, da Silva RAG, Righetto GL, Goncalves KA, Vasconcellos RS, Almeida MR, Silva Júnior A, Fietto JLR, Kobarg J, Gileadi C, Massirer KB, Borges JC, de Oliveira Neto M, Bressan GC. </i> Int J Biol Macromol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006275","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":688,"ncbi_taxon_id":9606,"date":"2020-03-02T14:22:11.909Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":81,"end":223},{"id":"PF00069","name":"Protein kinase domain","start":523,"end":686}]},"disprot_id":"DP02591","regions_counter":10,"dataset":[],"UniParc":"UPI000006D371","uniref100":"UniRef100_P78362","uniref90":"UniRef90_P78362","uniref50":"UniRef50_P78362","genes":[{"name":{"value":"SRPK2","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAH68547.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAH68547.1"}}]}}],"alphafold_very_low_content":0.3386627906976744,"disorder_content":0.5247093023255814,"disprot_consensus":{"full":[{"start":1,"end":80,"type":"D"},{"start":231,"end":511,"type":"D"}],"Structural state":[{"start":1,"end":80,"type":"D"},{"start":231,"end":511,"type":"D"}],"Molecular function":[{"start":1,"end":80,"type":"F"},{"start":231,"end":511,"type":"F"}]}},{"acc":"Q9H8Y8","name":"Golgi reassembly-stacking protein 2","sequence":"MGSSQSVEIPGGGTEGYHVLRVQENSPGHRAGLEPFFDFIVSINGSRLNKDNDTLKDLLKANVEKPVKMLIYSSKTLELRETSVTPSNLWGGQGLLGVSIRFCSFDGANENVWHVLEVESNSPAALAGLRPHSDYIIGADTVMNESEDLFSLIETHEAKPLKLYVYNTDTDNCREVIITPNSAWGGEGSLGCGIGYGYLHRIPTRPFEEGKKISLPGQMAGTPITPLKDGFTEVQLSSVNPPSLSPPGTTGIEQSLTGLSISSTPPAVSSVLSTGVPTVPLLPPQVNQSLTSVPPMNPATTLPGLMPLPAGLPNLPNLNLNLPAPHIMPGVGLPELVNPGLPPLPSMPPRNLPGIAPLPLPSEFLPSFPLVPESSSAASSGELLSSLPPTSNAPSDPATTTAKADAASSLTVDVTPPTAKAPTTVEDRVGDSTPVSEKPVSAAVDANASESP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":452,"region_id":"DP02592r001","start":209,"term_id":"IDPO:0000002","statement":[{"text":"The spectrum showed that the GRASP55 exhibited broad bands at ~203 and ~222 nm, suggesting the presence of the disordered as well as ordered secondary structure elements in the protein. The CD spectrum was further analyzed via CDSSTR routine using a set of various databases at Dichroweb server [33,34]. The results from CDSSTR deconvolution showed that fulllength GRASP55 has ~21% of α-helix, ~20% of β-sheet, ~17% of turns, and ~42% of disordered regions with the normalized root mean square deviation (NRMSD) of 0.19, which indicates, as already mentioned above, the presence of multiple disorder sites alongside well-structured regions. In addition, the protein family database analysis showed that the\nfull-length GRASP55 consists, as expected, of two domains: the GRASP (residues 1 –208) [17], including the two PDZ subdomains, and the SPR (residues 209 –452). Furthermore, the sequence-based prediction of protein disorder suggested that the C-terminal (SPR) domain of\nfull-length GRASP55 has high propensity of intrinsic disorder (Fig. 2), which is similar to the SPR domains of the CnGRASP and ScGRASP [29,30].","type":"Results"},{"text":"Based on these values, GRASP55 has Rh (measured from SEC-MALS) of the pre-molten globular conformation state. However, the far-UV CD studies and the crystal structure of the GRASP55 domain [17] showed that GRASP55 has a significant content of secondary structure in the native state. Moreover, the urea-induced denaturation studies showed that GRASP55\nunfolds at high concentration (4 M) in a cooperative manner. These observations together suggest GRASP55 would not likely form a pre-molten globular conformation in the native conditions. It would rather either form a complex elongated conformation and/or its PDZ domains, influenced by the hydrophobic disordered Cterminal domain, would not fold properly.","type":"Discussion"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31102680","version":2,"reference_html":"Exploring structural aspects of the human Golgi matrix protein GRASP55 in solution. <i> Reddy ST, Mendes LFS, Fontana NA, Costa-Filho AJ. </i> Int J Biol Macromol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":452,"region_id":"DP02592r002","start":209,"term_id":"IDPO:0000002","statement":[{"text":"Furthermore, the obtained Rh value of GRASP55 is much higher than what is expected for\na ~47 kDa protein (~3 nm) [40,41 ] based on the relation between Rh and molecular mass of different standard proteins. This is another indication that GRASP55 exhibits intrinsically disorder (ID) behavior in solution and agrees with our findings mentioned above. The ID behavior previously observed for lower eukaryotic GRASPs [29,30] thus seems to be a general property of GRASPs, spanning from lower to higher eukaryotes.","type":"Results"},{"text":"Based on these values, GRASP55 has Rh (measured from SEC-MALS) of the pre-molten globular conformation state. However, the far-UV CD studies and the crystal structure of the GRASP55 domain [17] showed that GRASP55 has a significant content of secondary structure in the native state. Moreover, the urea-induced denaturation studies showed that GRASP55\nunfolds at high concentration (4 M) in a cooperative manner. These observations together suggest GRASP55 would not likely form a pre-molten globular conformation in the native conditions. It would rather either form a complex elongated conformation and/or its PDZ domains, influenced by the hydrophobic disordered Cterminal domain, would not fold properly.","type":"Discussion"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"chromatography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31102680","version":2,"reference_html":"Exploring structural aspects of the human Golgi matrix protein GRASP55 in solution. <i> Reddy ST, Mendes LFS, Fontana NA, Costa-Filho AJ. </i> Int J Biol Macromol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":452,"region_id":"DP02592r003","start":209,"term_id":"IDPO:0000045","statement":[{"text":"Golgi structure formation is regulated by phosphorylation during the cell cycle. GRASP65 is a major target of mitotic kinases on the Golgi (Wang et al., 2003); the SPR domain contains multiple phosphorylation sites that are phosphorylated by Cdk1 and Plk in mitosis (Tang et al., 2012), which inhibits GRASP oligomerization and results in Golgi disassembly (Wang et al., 2005). At the end of mitosis, GRASP65 dephosphorylation by PP2A (Tang et al., 2008) allows the reformation of GRASP trans-oligomers and restacking of newly formed cisternae (Tang et al., 2010). GRASP55 is regulated in a similar way (Xiang and Wang, 2010), though phosphorylated by the MAP kinase ERKs instead (Jesch et al., 2001; Feinstein and Linstedt, 2007; Duran et al., 2008).","type":"Article"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"26779480","version":2,"reference_html":"GRASPs in Golgi Structure and Function. <i> Zhang X, Wang Y. </i> Front Cell Dev Biol, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"phosphorylation display site","curator_orcid":"0000-0003-0849-9312","disprot_namespace":"Disorder function"}],"released":"2021_06","length":452,"ncbi_taxon_id":9606,"date":"2020-03-02T15:06:39.953Z","organism":"Homo sapiens","features":{"gene3D":[{"start":1,"end":208,"id":"G3DSA:2.30.42.10","name":"G3DSA:2.30.42.10"}],"pfam":[{"id":"PF04495","name":"GRASP55/65 PDZ-like domain","start":69,"end":204}]},"disprot_id":"DP02592","regions_counter":3,"dataset":[],"UniParc":"UPI0000070B86","uniref100":"UniRef100_Q9H8Y8","uniref90":"UniRef90_Q9H8Y8","uniref50":"UniRef50_Q9H8Y8","genes":[{"name":{"value":"GORASP2"},"synonyms":[{"value":"GOLPH6"}]}],"alphafold_very_low_content":0.5066371681415929,"disorder_content":0.5398230088495575,"disprot_consensus":{"full":[{"start":209,"end":452,"type":"D"}],"Structural state":[{"start":209,"end":452,"type":"D"}],"Disorder function":[{"start":209,"end":452,"type":"F"}]}},{"acc":"Q9ESJ0","name":"Exportin-4","sequence":"MMAAALGPPEVIAQLENAAKVLMAPPSMVSNEQRQHAEHIFLSFRKSKSPFAVCRHILETSKVDYVLFQAATAIMEAVVREWVLLEKGSIESLRTFLLTYVLQRPNLQKYVREQILLAVAVIVKRGSLDKSIDCKSIFHEVSQLISSGNPTVQTLACSILTALLSEFSSSSKTSNIGLSMEFHGNCKRVFQEEDLRQIFMLTVGVLQEFSRRENLSAQMSSVFQRYLALANQVLSWNFLPPKLGRHYIAMFESSQNVLLKPTESWREALLDSRVMELFFTVHRKIREDSDMAQDSLQCLAQLASLHGPIFPDEGSQVDYLAHFIEGLLNTINGIEIEDSEAVGISSIISNLITVFPRNVLTAIPSELFSSFVNCLTHLTCSFGRSAALEEVLDKDDMVYMEAYDKLLESWLTLVRDDKHFHKGFFTQHAVQVFNSYIQCHLAAPDGTRNLTANGVASREEEEISELQEDDRDQFSDQLASVGMLGRIAAEHCMPLLTSLLEERVTRLHGQLQRHQQQFLASPGSSTIDNKMLDDLYEDIHWLILVTGYLLADDTQGETPLIPPEIMEYSIKHSSEVDINTTLQILGSPGEKASSIPGYSRTDSVIRLLSAVLRVSEVESRAIRADLTHLLSPQMGKDIVWFLKRWAKTYLLVDEKLYDQISLPLSTAFGADTEGSQWIIGYLLQKVISNLSVWSSEQDLANDTVQLLVTLVERRERANLVIQCENWWNLAKQFASRSPPLNFLSSPVQRTLMKALVLGGFAHMDTETKQQYWTEVLQPLQQRFLRVINQENFQQMCQQEEVKQEITATLEALCGIAEATQIDNVAILFNFLMDFLNNCIGLMEVYKNTPETVNLIIEVFVEVAHKQICYLGESKAMHLYEACLTLLQVYSKNNLGRQRIDVTAEEEQYQDLLLIMELLTNLLSKEFIDFSDTDEVFRGHEPGQAAGRSVSAADVVLYGVNLILPLMSQDLLKFPTLCNQYYKLITFICEIFPEKIPQLPEDLFKSLMYSLELGMTSMSSEVCQLCLEALTPLAEQCAKAQETDSPLFLATRHFLKLVFDMLVLQKHNTEMTTAAGEAFYTLVCLHQAEYSELVETLLSSQQDPVIYQRLADAFNKLTASSTPPALDRKQKMAFLKSLEEFMANVGGLLCVK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":260,"region_id":"DP02593r001","start":241,"term_id":"IDPO:0000002","statement":[{"text":"Limited proteolysis by trypsin or chymotrypsin did not compromise the integrity of the heterotrimeric complex (Fig. 1b). It also left eIF5A and Ran intact, but cleaved Xpo4 within two poorly conserved loops comprising residues 241–260 and 931–948, respectively","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27306458","version":2,"reference_html":"Structure of the exportin Xpo4 in complex with RanGTP and the hypusine-containing translation factor eIF5A. <i> Aksu M, Trakhanov S, Görlich D. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","cross_refs":[{"db":"PDB","id":"5DLQ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":948,"region_id":"DP02593r002","start":931,"term_id":"IDPO:0000002","statement":[{"text":"Limited proteolysis by trypsin or chymotrypsin did not compromise the integrity of the heterotrimeric complex (Fig. 1b). It also left eIF5A and Ran intact, but cleaved Xpo4 within two poorly conserved loops comprising residues 241–260 and 931–948, respectively","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27306458","version":2,"reference_html":"Structure of the exportin Xpo4 in complex with RanGTP and the hypusine-containing translation factor eIF5A. <i> Aksu M, Trakhanov S, Görlich D. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","cross_refs":[{"db":"PDB","id":"5DLQ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":181,"region_id":"DP02593r003","start":170,"term_id":"IDPO:0000002","statement":[{"text":"The final model includes residues 7–179 of Ran and 15–152 of eIF5A. We modelled 1,052 of 1,113 residues of Xpo4, with a few residues missing from N- and C-terminus as well as from several loop regions between the HEAT repeats.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27306458","version":2,"reference_html":"Structure of the exportin Xpo4 in complex with RanGTP and the hypusine-containing translation factor eIF5A. <i> Aksu M, Trakhanov S, Görlich D. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5DLQ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":530,"region_id":"DP02593r004","start":507,"term_id":"IDPO:0000002","statement":[{"text":"The final model includes residues 7–179 of Ran and 15–152 of eIF5A. We modelled 1,052 of 1,113 residues of Xpo4, with a few residues missing from N- and C-terminus as well as from several loop regions between the HEAT repeats.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27306458","version":2,"reference_html":"Structure of the exportin Xpo4 in complex with RanGTP and the hypusine-containing translation factor eIF5A. <i> Aksu M, Trakhanov S, Görlich D. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5DLQ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":771,"region_id":"DP02593r005","start":761,"term_id":"IDPO:0000002","statement":[{"text":"The final model includes residues 7–179 of Ran and 15–152 of eIF5A. We modelled 1,052 of 1,113 residues of Xpo4, with a few residues missing from N- and C-terminus as well as from several loop regions between the HEAT repeats.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27306458","version":2,"reference_html":"Structure of the exportin Xpo4 in complex with RanGTP and the hypusine-containing translation factor eIF5A. <i> Aksu M, Trakhanov S, Görlich D. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5DLQ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1046,"region_id":"DP02593r006","start":1034,"term_id":"IDPO:0000002","statement":[{"text":"The final model includes residues 7–179 of Ran and 15–152 of eIF5A. We modelled 1,052 of 1,113 residues of Xpo4, with a few residues missing from N- and C-terminus as well as from several loop regions between the HEAT repeats.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27306458","version":2,"reference_html":"Structure of the exportin Xpo4 in complex with RanGTP and the hypusine-containing translation factor eIF5A. <i> Aksu M, Trakhanov S, Görlich D. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5DLQ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":1046,"region_id":"DP02593r007","start":1034,"term_id":"IDPO:0000033","statement":[{"text":"The final model includes residues 7–179 of Ran and 15–152 of eIF5A. We modelled 1,052 of 1,113 residues of Xpo4, with a few residues missing from N- and C-terminus as well as from several loop regions between the HEAT repeats.","type":"Article"},{"text":"disordered region connecting repeats HEAT18B and HEAT19A","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27306458","version":3,"reference_html":"Structure of the exportin Xpo4 in complex with RanGTP and the hypusine-containing translation factor eIF5A. <i> Aksu M, Trakhanov S, Görlich D. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5DLQ"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":771,"region_id":"DP02593r008","start":761,"term_id":"IDPO:0000033","statement":[{"text":"The final model includes residues 7–179 of Ran and 15–152 of eIF5A. We modelled 1,052 of 1,113 residues of Xpo4, with a few residues missing from N- and C-terminus as well as from several loop regions between the HEAT repeats.","type":"Article"},{"text":"disordered region connecting repeats HEAT13B and HEAT14A","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27306458","version":3,"reference_html":"Structure of the exportin Xpo4 in complex with RanGTP and the hypusine-containing translation factor eIF5A. <i> Aksu M, Trakhanov S, Görlich D. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5DLQ"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":530,"region_id":"DP02593r009","start":507,"term_id":"IDPO:0000033","statement":[{"text":"The final model includes residues 7–179 of Ran and 15–152 of eIF5A. We modelled 1,052 of 1,113 residues of Xpo4, with a few residues missing from N- and C-terminus as well as from several loop regions between the HEAT repeats.","type":"Article"},{"text":"disordered region connecting repeats HEAT10A and HEAT10B","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27306458","version":3,"reference_html":"Structure of the exportin Xpo4 in complex with RanGTP and the hypusine-containing translation factor eIF5A. <i> Aksu M, Trakhanov S, Görlich D. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5DLQ"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":181,"region_id":"DP02593r010","start":170,"term_id":"IDPO:0000033","statement":[{"text":"The final model includes residues 7–179 of Ran and 15–152 of eIF5A. We modelled 1,052 of 1,113 residues of Xpo4, with a few residues missing from N- and C-terminus as well as from several loop regions between the HEAT repeats.","type":"Article"},{"text":"disordered region connecting repeats HEAT4B and HEAT5A","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27306458","version":3,"reference_html":"Structure of the exportin Xpo4 in complex with RanGTP and the hypusine-containing translation factor eIF5A. <i> Aksu M, Trakhanov S, Görlich D. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5DLQ"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","length":1151,"ncbi_taxon_id":10090,"date":"2020-03-02T15:37:25.320Z","organism":"Mus musculus","features":{"gene3D":[{"start":698,"end":1145,"id":"G3DSA:1.25.10.10","name":"Leucine-rich Repeat Variant"}],"pfam":[{"id":"PF28490","name":"Exportin-4","start":29,"end":1148}]},"disprot_id":"DP02593","regions_counter":10,"dataset":[],"UniParc":"UPI00015DEDC1","uniref100":"UniRef100_Q9ESJ0","uniref90":"UniRef90_Q9C0E2","uniref50":"UniRef50_Q9C0E2","genes":[{"name":{"value":"Xpo4","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"27306458","url":"http://www.ncbi.nlm.nih.gov/pubmed/27306458","alternativeUrl":"https://europepmc.org/abstract/MED/27306458"}},{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:1888526","url":"http://www.informatics.jax.org/marker/MGI:1888526"}}]},"synonyms":[{"value":"Kiaa1721","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"14621295","url":"http://www.ncbi.nlm.nih.gov/pubmed/14621295","alternativeUrl":"https://europepmc.org/abstract/MED/14621295"}}]}]}],"alphafold_very_low_content":0.023457862728062554,"disorder_content":0.08514335360556038,"disprot_consensus":{"full":[{"start":170,"end":181,"type":"D"},{"start":241,"end":260,"type":"D"},{"start":507,"end":530,"type":"D"},{"start":761,"end":771,"type":"D"},{"start":931,"end":948,"type":"D"},{"start":1034,"end":1046,"type":"D"}],"Structural state":[{"start":170,"end":181,"type":"D"},{"start":241,"end":260,"type":"D"},{"start":507,"end":530,"type":"D"},{"start":761,"end":771,"type":"D"},{"start":931,"end":948,"type":"D"},{"start":1034,"end":1046,"type":"D"}],"Disorder function":[{"start":170,"end":181,"type":"F"},{"start":507,"end":530,"type":"F"},{"start":761,"end":771,"type":"F"},{"start":1034,"end":1046,"type":"F"}]}},{"acc":"P63241","name":"Eukaryotic translation initiation factor 5A-1","sequence":"MADDLDFETGDAGASATFPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRNDFQLIGIQDGYLSLLQDSGEVREDLRLPEGDLGKEIEQKYDCGEEILITVLSAMTEEAAVAIKAMAK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":14,"region_id":"DP02594r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"Even though this complex was stable and monodisperse, it did not crystallize–apparently because of disordered loops and termini: Indeed, the 14 N-terminal probably disordered residues of eIF5A (refs 36, 37, 53) not only turned out to be dispensable for complex formation (Fig. 1a), but also, their deletion allowed the RanGTP·Xpo4·eIF5A complex to crystallize in needle clusters.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27306458","version":2,"reference_html":"Structure of the exportin Xpo4 in complex with RanGTP and the hypusine-containing translation factor eIF5A. <i> Aksu M, Trakhanov S, Görlich D. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5DLQ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T14:24:55.995Z"}}],"released":"2021_06","length":154,"ncbi_taxon_id":9606,"date":"2020-03-02T18:19:02.561Z","organism":"Homo sapiens","features":{"gene3D":[{"start":1,"end":83,"id":"G3DSA:2.30.30.30","name":"G3DSA:2.30.30.30"}],"pfam":[{"id":"PF01287","name":"Eukaryotic elongation factor 5A hypusine, DNA-binding OB fold","start":83,"end":150},{"id":"PF21485","name":"Translation initiation factor 5A-like, N-terminal","start":15,"end":77}]},"disprot_id":"DP02594","regions_counter":1,"dataset":["NDDs-related proteins","RNA-binding proteins"],"UniParc":"UPI0000006BEE","uniref100":"UniRef100_P63241","uniref90":"UniRef90_P63241","uniref50":"UniRef50_P63241","genes":[{"name":{"value":"EIF5A"}}],"alphafold_very_low_content":0.06493506493506493,"disorder_content":0.09090909090909091,"disprot_consensus":{"full":[{"start":1,"end":14,"type":"D"}],"Structural state":[{"start":1,"end":14,"type":"D"}]}},{"acc":"P25490","name":"Transcriptional repressor protein YY1","sequence":"MASGDTLYIATDGSEMPAEIVELHEIEVETIPVETIETTVVGEEEEEDDDDEDGGGGDHGGGGGHGHAGHHHHHHHHHHHPPMIALQPLVTDDPTQVHHHQEVILVQTREEVVGGDDSDGLRAEDGFEDQILIPVPAPAGGDDDYIEQTLVTVAAAGKSGGGGSSSSGGGRVKKGGGKKSGKKSYLSGGAGAAGGGGADPGNKKWEQKQVQIKTLEGEFSVTMWSSDEKKDIDHETVVEEQIIGENSPPDYSEYMTGKKLPPGGIPGIDLSDPKQLAEFARMKPRKIKEDDAPRTIACPHKGCTKMFRDNSAMRKHLHTHGPRVHVCAECGKAFVESSKLKRHQLVHTGEKPFQCTFEGCGKRFSLDFNLRTHVRIHTGDRPYVCPFDGCNKKFAQSTNLKSHILTHAKAKNNQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"rpancsa","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":295,"region_id":"DP02595r001","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The discrepancy between the formula and SDS-PAGE-determined molecular masses suggests that YY1 belongs to the group of Intrinsically Disordered Proteins (IDPs). In general, the apparent molecular masses of IDPs determined by SDSPAGE are 1.2 – 1.8 times higher than the results expected from sequence data or measured by mass spectrometry.45 The retarded IDP mobility by SDS-PAGE results from IDPs binding less SDS than globular proteins because of their decreased hydrophobic residue content.\nAnalogous calculations conducted for the DBD showed migration typical for a globular protein (the formula and apparent molecular masses calculated from electrophoresis are 14,053.9 Da and 14 kDa, respectively). Furthermore, considering that the apparent molecular masses of full-length YY1 and its N-terminal fragment were 1.23 and 1.38 times higher, respectively, than their formula masses, the studied proteins appear to have strongly heterogeneous and complex structures, and the intrinsically disordered properties are primarily in the N-terminal fragment of the protein. This observation justifies the division of the YY1 protein into N- and C-terminal fragments around the 295 residue and also justifies studying them separately.","type":"Results"}],"curator_id":"rpancsa","released":"2023_06","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"25963536","version":2,"reference_html":"Intrinsic disorder of human Yin Yang 1 protein. <i> Górecki A, Bonarek P, Górka AK, Figiel M, Wilamowski M, Dziedzicka-Wasylewska M. </i> Proteins, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007689","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-29T15:53:09.308Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":295,"region_id":"DP02595r002","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"YY1, the NTF and casein were efficiently digested by both enzymes under moderate conditions (30 min at 25 8C at 1:500 protease/substrate ratio), whereas the DBD and\nBSA were not. The NTF exhibited the greatest susceptibility to proteolysis, and the process was almost complete with the use of proteinase K.","type":"Results"}],"curator_id":"rpancsa","released":"2023_06","ec_name":"cleavage assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"25963536","version":2,"reference_html":"Intrinsic disorder of human Yin Yang 1 protein. <i> Górecki A, Bonarek P, Górka AK, Figiel M, Wilamowski M, Dziedzicka-Wasylewska M. </i> Proteins, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-29T15:51:59.366Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":295,"region_id":"DP02595r003","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"According to the presented data, the DBD can be classified as a globular protein or molten globule (Rs 5 20.5 A˚ 34), and the NTF (Rs 5 46.8 A˚ ) can be classified as a random coil under native conditions. Surprisingly, the hydrodynamic radius of full-length YY1\n(Rs 5 46.5 A˚ ) is slightly lower than that of its N-terminal part and may indicate a pre-molten globule or random coil state under native conditions. ","type":"Results"}],"curator_id":"rpancsa","released":"2023_06","ec_name":"chromatography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"25963536","version":2,"reference_html":"Intrinsic disorder of human Yin Yang 1 protein. <i> Górecki A, Bonarek P, Górka AK, Figiel M, Wilamowski M, Dziedzicka-Wasylewska M. </i> Proteins, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-29T15:51:11.578Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":295,"region_id":"DP02595r004","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The spectrum registered for the DBD is typical for C2H2-type zinc finger structures ligated with Zn21,62,63 and the spectra obtained for YY1 and its N-terminal\nfragment are typical for proteins with a low content of stable secondary structures, that is, for IDPs.38,64","type":"Results"}],"curator_id":"rpancsa","released":"2023_06","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"25963536","version":2,"reference_html":"Intrinsic disorder of human Yin Yang 1 protein. <i> Górecki A, Bonarek P, Górka AK, Figiel M, Wilamowski M, Dziedzicka-Wasylewska M. </i> Proteins, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-29T15:48:01.499Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":295,"region_id":"DP02595r005","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Similar conclusions can be drawn from the analysis of the fluorescence spectra recorded for two tryptophan residues present in the protein (W205 and W225). Under native conditions, the maximum fluorescence emission wavelength was approximately 340 nm (Fig. 7), compared with the range of 346–350 nm for water-exposed tryptophan residues in proteins (Class III, according to tryptophan residue classification).67","type":"Results"}],"curator_id":"rpancsa","released":"2023_06","ec_name":"fluorescence evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"25963536","version":2,"reference_html":"Intrinsic disorder of human Yin Yang 1 protein. <i> Górecki A, Bonarek P, Górka AK, Figiel M, Wilamowski M, Dziedzicka-Wasylewska M. </i> Proteins, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001249","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-29T15:47:18.816Z"}}],"released":"2023_06","length":414,"ncbi_taxon_id":9606,"date":"2020-03-02T22:29:19.577Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF00096","name":"Zinc finger, C2H2 type","start":298,"end":320},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":325,"end":347},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":353,"end":377},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":383,"end":407}]},"disprot_id":"DP02595","regions_counter":9,"dataset":["NDDs-related proteins"],"UniParc":"UPI00001378FC","uniref100":"UniRef100_P25490","uniref90":"UniRef90_P25490","uniref50":"UniRef50_P25490","genes":[{"name":{"value":"YY1"},"synonyms":[{"value":"INO80S"}]}],"alphafold_very_low_content":0.6521739130434783,"disorder_content":0.7125603864734299,"disprot_consensus":{"full":[{"start":1,"end":295,"type":"D"}],"Structural state":[{"start":1,"end":295,"type":"D"}]}},{"acc":"Q04866","name":"Chain length determinant protein","sequence":"MTVDSNTSSGRGNDPEQIDLIELLLQLWRGKMTIIVAVIIAILLAVGYLMIAKEKWTSTAIITQPDAAQVATYTNALNVLYGGNAPKISEVQANFISRFSSAFSALSEVLDNQKEREKLTIEQSVKGQALPLSVSYVSTTAEGAQRRLAEYIQQVDEEVAKELEVDLKDNITLQTKTLQESLETQEVVAQEQKDLRIKQIEEALRYADEAKITQPQIQQTQDVTQDTMFLLGSDALKSMIQNEATRPLVFSPAYYQTKQTLLDIKNLKVTADTVHVYRYVMKPTLPVRRDSPKTAITLVLAVLLGGMIGAGIVLGRNALRSYKPKAL","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":249,"region_id":"DP02596r001","start":206,"term_id":"IDPO:0000002","statement":[{"text":"The loop connecting helices α6 and α7, the loop between helices α4 and α5, and the loop that connects the β2-β3 strands each have disordered segments in one or more of the structures.","type":"Results"},{"text":"Region 206-249 of WzzB from Salmonella typhimurium connects helices α6 and α8 of the protein and corresponds to a disordered region not visible in the electron density (see Supplementary Figure S1)","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18204465","version":2,"reference_html":"Bacterial polysaccharide co-polymerases share a common framework for control of polymer length. <i> Tocilj A, Munger C, Proteau A, Morona R, Purins L, Ajamian E, Wagner J, Papadopoulos M, Van Den Bosch L, Rubinstein JL, Féthière J, Matte A, Cygler M. </i> Nat Struct Mol Biol, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3B8P"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":327,"ncbi_taxon_id":99287,"date":"2020-03-03T09:44:57.081Z","organism":"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","features":{"gene3D":[],"pfam":[{"id":"PF02706","name":"Chain length determinant protein","start":16,"end":121}]},"disprot_id":"DP02596","regions_counter":1,"dataset":[],"UniParc":"UPI0000138FBD","uniref100":"UniRef100_Q04866","uniref90":"UniRef90_Q04866","uniref50":"UniRef50_P76372","genes":[{"name":{"value":"wzzB"},"synonyms":[{"value":"cld"},{"value":"rol"}],"olnNames":[{"value":"STM2079"}]}],"alphafold_very_low_content":0.06116207951070336,"disorder_content":0.1345565749235474,"disprot_consensus":{"full":[{"start":206,"end":249,"type":"D"}],"Structural state":[{"start":206,"end":249,"type":"D"}]}},{"acc":"O49195","name":"Vegetative storage protein 1","sequence":"MKILSLSLLLLLAATVSHVQSSASVPGLIELLESNTIFGNEAELLEKEGLSINYPNCRSWHLGVETSNIINFDTVPANCKAYVEDYLITSKQYQYDSKTVNKEAYFYAKGLALKNDTVNVWIFDLDDTLLSSIPYYAKYGYGTENTAPGAYWSWLESGESTPGLPETLHLYENLLELGIEPIIISDRWKKLSEVTVENLKAVGVTKWKHLILKPNGSKLTQVVYKSKVRNSLVKKGYNIVGNIGDQWADLVEDTPGRVFKLPNPLYYVPS","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":48,"region_id":"DP02597r001","start":16,"term_id":"IDPO:0000002","statement":[{"text":"In the final model, the electron density of residues Val16-Glu48 was invisible, and therefore, these residues were excluded.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23166664","version":2,"reference_html":"The crystal structure of Arabidopsis VSP1 reveals the plant class C-like phosphatase structure of the DDDD superfamily of phosphohydrolases. <i> Chen Y, Wei J, Wang M, Shi Z, Gong W, Zhang M. </i> PLoS One, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4FYP"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":270,"ncbi_taxon_id":3702,"date":"2020-03-03T09:59:41.646Z","organism":"Arabidopsis thaliana","features":{"gene3D":[{"start":51,"end":270,"id":"G3DSA:3.40.50.1000","name":"HAD superfamily/HAD-like"}],"pfam":[{"id":"PF03767","name":"HAD superfamily, subfamily IIIB (Acid phosphatase)","start":43,"end":268}]},"disprot_id":"DP02597","regions_counter":1,"dataset":[],"UniParc":"UPI0000001429","uniref100":"UniRef100_O49195","uniref90":"UniRef90_O49195","uniref50":"UniRef50_O82122","genes":[{"name":{"value":"VSP1"},"orfNames":[{"value":"T4C12"}],"olnNames":[{"value":"At5g24780"}]}],"alphafold_very_low_content":0.1259259259259259,"disorder_content":0.12222222222222222,"disprot_consensus":{"full":[{"start":16,"end":48,"type":"D"}],"Structural state":[{"start":16,"end":48,"type":"D"}]}},{"acc":"Q96H20","name":"Vacuolar-sorting protein SNF8","sequence":"MHRRGVGAGAIAKKKLAEAKYKERGTVLAEDQLAQMSKQLDMFKTNLEEFASKHKQEIRKNPEFRVQFQDMCATIGVDPLASGKGFWSEMLGVGDFYYELGVQIIEVCLALKHRNGGLITLEELHQQVLKGRGKFAQDVSQDDLIRAIKKLKALGTGFGIIPVGGTYLIQSVPAELNMDHTVVLQLAEKNGYVTVSEIKASLKWETERARQVLEHLLKEGLAWLDLQAPGEAHYWLPALFTDLYSQEITAEEAREALP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":25,"region_id":"DP02598r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"Residues 149–169 from VPS36 and residues 1–25 from VPS22 are present in construct a, but could not be visualized in electron density and are presumed to be disordered.","type":"Methods"},{"text":"Authors of the publication refer to the N-terminal 25 residues of VPS22 as VPS22-H0","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18539118","version":2,"reference_html":"Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex. <i> Im YJ, Hurley JH. </i> Dev Cell, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2ZME"},{"db":"PDB","id":"3CUQ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":25,"region_id":"DP02598r002","start":1,"term_id":"GO:0008289","statement":[{"text":"Authors of the publication refer to the N-terminal 25 residues of VPS22 as VPS22-H0","type":"Curator statement"},{"text":"The observation that both the Vps36 GLUE domain and the Vps22 H0 contribute to lipid binding in vitro suggested to us that a combinatorial mechanism evolved to drive high-affinity membrane targeting of ESCRT-II","type":"Discussion"},{"text":"The purified pseudo-intact ESCRT-II showed strong binding to liposomes made of synthetic lipids composed of phosphatidylcholine (PC), phosphatidylethanolamine (PE), and phosphoinositides (PIPs) (Fig. 4D–K), and bound weakly to PC:PE and PC:PE:phosphatidylinositol (PI) liposomes (Fig. 4B, C, K).","type":"Results"}],"curator_id":"esalladini","released":"2022_03","ec_name":"co-sedimentation assay evidence used in manual assertion","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"18539118","version":4,"reference_html":"Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex. <i> Im YJ, Hurley JH. </i> Dev Cell, 2008","date":"2022-03-09T10:49:48.317Z","reference_source":"pmid","ec_id":"ECO:0001164","term_name":"lipid binding","curator_orcid":"0000-0002-5152-5953","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"ChEBI","id":"49183","operator":"and","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"16038","operator":"and","partner_start":null,"partner_end":null}]},{"term_namespace":"Biological process","ec_ontology":"ECO","end":25,"region_id":"DP02598r003","start":1,"term_id":"GO:0051179","statement":[{"text":"Authors of the publication refer to the N-terminal 25 residues of VPS22 as VPS22-H0","type":"Curator statement"},{"text":"We have now found that the most N-terminal predicted helix of the core of each subunit (H0) is flexibly attached to the core assembly. We have been able to assign functions to each of these two regions. The VPS22-H0 participates in membrane binding, while the VPS36-H0 interacts with ESCRT-I.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"microscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18539118","version":3,"reference_html":"Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex. <i> Im YJ, Hurley JH. </i> Dev Cell, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001232","cross_refs":[{"db":"PDB","id":"2ZME"},{"db":"PDB","id":"3CUQ"}],"term_name":"localization","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2021_06","length":258,"ncbi_taxon_id":9606,"date":"2020-03-03T10:48:50.498Z","organism":"Homo sapiens","features":{"gene3D":[{"start":173,"end":258,"id":"G3DSA:1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"start":173,"end":258,"id":"G3DSA:1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}],"pfam":[{"id":"PF04157","name":"EAP30/Vps36 family","start":6,"end":225}]},"disprot_id":"DP02598","regions_counter":3,"dataset":[],"UniParc":"UPI0000071826","uniref100":"UniRef100_Q96H20","uniref90":"UniRef90_Q96H20","uniref50":"UniRef50_Q96H20","genes":[{"name":{"value":"SNF8"},"synonyms":[{"value":"EAP30"}]}],"alphafold_very_low_content":0.027131782945736434,"disorder_content":0.09689922480620156,"disprot_consensus":{"full":[{"start":1,"end":25,"type":"D"}],"Structural state":[{"start":1,"end":25,"type":"D"}],"Molecular function":[{"start":1,"end":25,"type":"F"}],"Biological process":[{"start":1,"end":25,"type":"F"}]}},{"acc":"Q86VN1","name":"Vacuolar protein-sorting-associated protein 36","sequence":"MDRFVWTSGLLEINETLVIQQRGVRIYDGEEKIKFDAGTLLLSTHRLIWRDQKNHECCMAILLSQIVFIEEQAAGIGKSAKIVVHLHPAPPNKEPGPFQSSKNSYIKLSFKEHGQIEFYRRLSEEMTQRRWENMPVSQSLQTNRGPQPGRIRAVGIVGIERKLEEKRKETDKNISEAFEDLSKLMIKAKEMVELSKSIANKIKDKQGDITEDETIRFKSYLLSMGIANPVTRETYGSGTQYHMQLAKQLAGILQVPLEERGGIMSLTEVYCLVNRARGMELLSPEDLVNACKMLEALKLPLRLRVFDSGVMVIELQSHKEEEMVASALETVSEKGSLTSEEFAKLVGMSVLLAKERLLLAEKMGHLCRDDSVEGLRFYPNLFMTQS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":169,"region_id":"DP02599r001","start":149,"term_id":"IDPO:0000002","statement":[{"text":"The linker between the GLUE domain and the C-terminal core of VPS36 (residues 140–169) also contains a predicted α helix, which we refer to as VPS36-H0","type":"Results"},{"text":"The VPS22-H0, VPS36-H0, and adjoining residues were disordered.","type":"Results"},{"text":"Residues 149–169 from VPS36 and residues 1–25 from VPS22 are present in construct a, but could not be visualized in electron density and are presumed to be disordered.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18539118","version":2,"reference_html":"Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex. <i> Im YJ, Hurley JH. </i> Dev Cell, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2ZME"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":169,"region_id":"DP02599r002","start":149,"term_id":"IDPO:0000033","statement":[{"text":"The linker between the GLUE domain and the C-terminal core of VPS36 (residues 140–169) also contains a predicted α helix, which we refer to as VPS36-H0","type":"Results"},{"text":"The VPS22-H0, VPS36-H0, and adjoining residues were disordered.","type":"Results"},{"text":"Residues 149–169 from VPS36 and residues 1–25 from VPS22 are present in construct a, but could not be visualized in electron density and are presumed to be disordered.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18539118","version":3,"reference_html":"Integrated structural model and membrane targeting mechanism of the human ESCRT-II complex. <i> Im YJ, Hurley JH. </i> Dev Cell, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2ZME"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","length":386,"ncbi_taxon_id":9606,"date":"2020-03-03T11:31:57.777Z","organism":"Homo sapiens","features":{"gene3D":[{"start":1,"end":138,"id":"G3DSA:2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":317,"end":386,"id":"G3DSA:1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"start":317,"end":386,"id":"G3DSA:1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}],"pfam":[{"id":"PF04157","name":"EAP30/Vps36 family","start":154,"end":370},{"id":"PF11605","name":"Vacuolar protein sorting protein 36 Vps36","start":6,"end":87}]},"disprot_id":"DP02599","regions_counter":2,"dataset":[],"UniParc":"UPI000013CFE6","uniref100":"UniRef100_Q86VN1","uniref90":"UniRef90_Q86VN1","uniref50":"UniRef50_Q86VN1","genes":[{"name":{"value":"VPS36"},"synonyms":[{"value":"C13orf9"},{"value":"EAP45"}],"orfNames":[{"value":"CGI-145"}]}],"alphafold_very_low_content":0.06735751295336788,"disorder_content":0.054404145077720206,"disprot_consensus":{"full":[{"start":149,"end":169,"type":"D"}],"Structural state":[{"start":149,"end":169,"type":"D"}],"Disorder function":[{"start":149,"end":169,"type":"F"}]}},{"acc":"P35916","name":"Vascular endothelial growth factor receptor 3","sequence":"MQRGAALCLRLWLCLGLLDGLVSGYSMTPPTLNITEESHVIDTGDSLSISCRGQHPLEWAWPGAQEAPATGDKDSEDTGVVRDCEGTDARPYCKVLLLHEVHANDTGSYVCYYKYIKARIEGTTAASSYVFVRDFEQPFINKPDTLLVNRKDAMWVPCLVSIPGLNVTLRSQSSVLWPDGQEVVWDDRRGMLVSTPLLHDALYLQCETTWGDQDFLSNPFLVHITGNELYDIQLLPRKSLELLVGEKLVLNCTVWAEFNSGVTFDWDYPGKQAERGKWVPERRSQQTHTELSSILTIHNVSQHDLGSYVCKANNGIQRFRESTEVIVHENPFISVEWLKGPILEATAGDELVKLPVKLAAYPPPEFQWYKDGKALSGRHSPHALVLKEVTEASTGTYTLALWNSAAGLRRNISLELVVNVPPQIHEKEASSPSIYSRHSRQALTCTAYGVPLPLSIQWHWRPWTPCKMFAQRSLRRRQQQDLMPQCRDWRAVTTQDAVNPIESLDTWTEFVEGKNKTVSKLVIQNANVSAMYKCVVSNKVGQDERLIYFYVTTIPDGFTIESKPSEELLEGQPVLLSCQADSYKYEHLRWYRLNLSTLHDAHGNPLLLDCKNVHLFATPLAASLEEVAPGARHATLSLSIPRVAPEHEGHYVCEVQDRRSHDKHCHKKYLSVQALEAPRLTQNLTDLLVNVSDSLEMQCLVAGAHAPSIVWYKDERLLEEKSGVDLADSNQKLSIQRVREEDAGRYLCSVCNAKGCVNSSASVAVEGSEDKGSMEIVILVGTGVIAVFFWVLLLLIFCNMRRPAHADIKTGYLSIIMDPGEVPLEEQCEYLSYDASQWEFPRERLHLGRVLGYGAFGKVVEASAFGIHKGSSCDTVAVKMLKEGATASEHRALMSELKILIHIGNHLNVVNLLGACTKPQGPLMVIVEFCKYGNLSNFLRAKRDAFSPCAEKSPEQRGRFRAMVELARLDRRRPGSSDRVLFARFSKTEGGARRASPDQEAEDLWLSPLTMEDLVCYSFQVARGMEFLASRKCIHRDLAARNILLSESDVVKICDFGLARDIYKDPDYVRKGSARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQINEEFCQRLRDGTRMRAPELATPAIRRIMLNCWSGDPKARPAFSELVEILGDLLQGRGLQEEEEVCMAPRSSQSSEEGSFSQVSTMALHIAQADAEDSPPSLQRHSLAARYYNWVSFPGCLARGAETRGSSRMKTFEEFPMTPTTYKGSVDNQTDSGMVLASEEFEQIESRHRQESGFSCKGPGQNVAVTRAHPDSQGRRRRPERGARGGQVFYNSEYGELSEPSEEDHCSPSARVTFFTDNSY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"region_id":"DP02600r001","ec_ontology":"ECO","end":483,"term_id":"IDPO:0000002","start":470,"version":2,"statement":[{"text":"The structure of the VEGFR-3 D4-5 homodimer suggests that proteolytic cleavage did not introduce significant changes in the D5 conformation, because it occurred in the C-D loop, which is disordered in the Cys466/Cys486 disulfide bridge","type":"Discussion"},{"text":"Residues 470–483 in the C-D loop were disordered and thus were omitted from the final model. VEGFR-3 D4-5 has an overall extended structure connected by the linker peptide, a salt bridge between Glu344 and Lys539, and a hydrogen bond between Glu391 and Tyr448","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23878260","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4BSJ"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structural and mechanistic insights into VEGF receptor 3 ligand binding and activation. <i> Leppänen VM, Tvorogov D, Kisko K, Prota AE, Jeltsch M, Anisimov A, Markovic-Mueller S, Stuttfeld E, Goldie KN, Ballmer-Hofer K, Alitalo K. </i> Proc Natl Acad Sci U S A, 2013","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T18:30:50.356Z"}},{"region_id":"DP02600r002","ec_ontology":"ECO","end":483,"term_id":"IDPO:0000033","start":470,"version":3,"statement":[{"text":"The structure of the VEGFR-3 D4-5 homodimer suggests that proteolytic cleavage did not introduce significant changes in the D5 conformation, because it occurred in the C-D loop, which is disordered in the Cys466/Cys486 disulfide bridge","type":"Discussion"},{"text":"Residues 470–483 in the C-D loop were disordered and thus were omitted from the final model. VEGFR-3 D4-5 has an overall extended structure connected by the linker peptide, a salt bridge between Glu344 and Lys539, and a hydrogen bond between Glu391 and Tyr448","type":"Results"}],"term_name":"flexible linker","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23878260","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4BSJ"}],"term_namespace":"Disorder function","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structural and mechanistic insights into VEGF receptor 3 ligand binding and activation. <i> Leppänen VM, Tvorogov D, Kisko K, Prota AE, Jeltsch M, Anisimov A, Markovic-Mueller S, Stuttfeld E, Goldie KN, Ballmer-Hofer K, Alitalo K. </i> Proc Natl Acad Sci U S A, 2013","ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T18:30:50.131Z"}},{"region_id":"DP02600r003","ec_ontology":"ECO","end":89,"term_id":"IDPO:0000002","start":77,"version":3,"statement":[{"text":"On the other hand, VEGFR-3 D1 has large disordered regions in the ligand complex, suggesting that it may interact with other binding partners in vivo, such as neuropilin-2 or the large N- and C-terminal propeptides of VEGF-C and VEGF-D.","type":"Discussion"},{"text":"Residues 28–134 of D1 are largely disordered, and we could build only the core of the apparent I-type Ig domain using KIT D1 (PDB ID code 2E9W) as a model.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_06","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23878260","date":"2022-06-28T07:50:24.058Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4BSK"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structural and mechanistic insights into VEGF receptor 3 ligand binding and activation. <i> Leppänen VM, Tvorogov D, Kisko K, Prota AE, Jeltsch M, Anisimov A, Markovic-Mueller S, Stuttfeld E, Goldie KN, Ballmer-Hofer K, Alitalo K. </i> Proc Natl Acad Sci U S A, 2013","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P49767"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T12:15:54.665Z"}},{"region_id":"DP02600r004","ec_ontology":"ECO","end":123,"term_id":"IDPO:0000002","start":114,"version":3,"statement":[{"text":"On the other hand, VEGFR-3 D1 has large disordered regions in the ligand complex, suggesting that it may interact with other binding partners in vivo, such as neuropilin-2 or the large N- and C-terminal propeptides of VEGF-C and VEGF-D.","type":"Discussion"},{"text":"Residues 28–134 of D1 are largely disordered, and we could build only the core of the apparent I-type Ig domain using KIT D1 (PDB ID code 2E9W) as a model.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_06","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23878260","date":"2022-06-28T07:50:12.002Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4BSK"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structural and mechanistic insights into VEGF receptor 3 ligand binding and activation. <i> Leppänen VM, Tvorogov D, Kisko K, Prota AE, Jeltsch M, Anisimov A, Markovic-Mueller S, Stuttfeld E, Goldie KN, Ballmer-Hofer K, Alitalo K. </i> Proc Natl Acad Sci U S A, 2013","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P49767"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T12:15:56.835Z"}}],"released":"2020_12","length":1363,"ncbi_taxon_id":9606,"date":"2020-03-03T13:35:37.850Z","organism":"Homo sapiens","features":{"gene3D":[{"start":668,"end":775,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":668,"end":775,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":668,"end":775,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":668,"end":775,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":668,"end":775,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":668,"end":775,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"}],"pfam":[{"id":"PF07679","name":"Immunoglobulin I-set domain","start":678,"end":765},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":845,"end":1169},{"id":"PF13927","name":"Immunoglobulin domain","start":236,"end":314},{"id":"PF17988","name":"VEGFR-2 Transmembrane domain","start":770,"end":804},{"id":"PF21339","name":"Vascular endothelial growth factor receptor 1-like, Ig-like domain","start":145,"end":223},{"id":"PF22854","name":"VEGFR1-3, N-terminal Ig-like domain","start":29,"end":141},{"id":"PF22971","name":"VEGFR-1-like, immunoglobulin-like domain","start":419,"end":553}]},"disprot_id":"DP02600","regions_counter":4,"dataset":["Cancer-related proteins"],"UniParc":"UPI000003CA99","uniref100":"UniRef100_P35916","uniref90":"UniRef90_P35916","uniref50":"UniRef50_P35916","genes":[{"name":{"value":"FLT4"},"synonyms":[{"value":"VEGFR3"}]}],"alphafold_very_low_content":0.23404255319148937,"disorder_content":0.02714600146735143,"disprot_consensus":{"full":[{"start":77,"end":89,"type":"D"},{"start":114,"end":123,"type":"D"},{"start":470,"end":483,"type":"D"}],"Structural state":[{"start":77,"end":89,"type":"D"},{"start":114,"end":123,"type":"D"},{"start":470,"end":483,"type":"D"}],"Disorder function":[{"start":470,"end":483,"type":"F"}]}},{"acc":"Q96NW4","name":"Ankyrin repeat domain-containing protein 27","sequence":"MALYDEDLLKNPFYLALQKCRPDLCSKVAQIHGIVLVPCKGSLSSSIQSTCQFESYILIPVEEHFQTLNGKDVFIQGNRIKLGAGFACLLSVPILFEETFYNEKEESFSILCIAHPLEKRESSEEPLAPSDPFSLKTIEDVREFLGRHSERFDRNIASFHRTFRECERKSLRHHIDSANALYTKCLQQLLRDSHLKMLAKQEAQMNLMKQAVEIYVHHEIYNLIFKYVGTMEASEDAAFNKITRSLQDLQQKDIGVKPEFSFNIPRAKRELAQLNKCTSPQQKLVCLRKVVQLITQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSLAKDELGYCLTSFEAAIEYIRQGSLSAKPPESEGFGDRLFLKQRMSLLSQMTSSPTDCLFKHIASGNQKEVERLLSQEDHDKDTVQKMCHPLCFCDDCEKLVSGRLNDPSVVTPFSRDDRGHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALVYYDVESCRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSVMEAYHLSFERRQKSSEAPVQSPQRSVDSISQESSTSSFSSMSASSRQEETKKDYREVEKLLRAVADGDLEMVRYLLEWTEEDLEDAEDTVSAADPEFCHPLCQCPKCAPAQKRLAKVPASGLGVNVTSQDGSSPLHVAALHGRADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKCLLDSNAKPNKKDLSGNTPLIYACSGGHHELVALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASVQVLNKRQRTAVDCAEQNSKIMELLQVVPSCVASLDDVAETDRKEYVTVKIRKKWNSKLYDLPDEPFTRQFYFVHSAGQFKGKTSREIMARDRSVPNLTEGSLHEPGRQSVTLRQNNLPAQSGSHAAEKGNSDWPERPGLTQTGPGHRRMLRRHTVEDAVVSQGPEAAGPLSTPQEVSASRS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":732,"region_id":"DP02601r001","start":693,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The first ankyrin repeat (coloured cyan in all figures), although separated from the next five repeats by a disordered region (residues 694–729) for which there is no electron density, contacts the second ankyrin repeat through an extensive and tightly packed hydrophobic interface (Figure 3).","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23104059","version":2,"reference_html":"The binding of Varp to VAMP7 traps VAMP7 in a closed, fusogenically inactive conformation. <i> Schäfer IB, Hesketh GG, Bright NA, Gray SR, Pryor PR, Evans PR, Luzio JP, Owen DJ. </i> Nat Struct Mol Biol, 2012","date":"2022-08-05T14:22:01.186Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4B93"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-08T17:50:36.262Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":732,"region_id":"DP02601r002","start":693,"term_id":"IDPO:0000033","unpublished":true,"statement":[{"text":"The first ankyrin repeat (coloured cyan in all figures), although separated from the next five repeats by a disordered region (residues 694–729) for which there is no electron density, contacts the second ankyrin repeat through an extensive and tightly packed hydrophobic interface (Figure 3).","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23104059","version":3,"reference_html":"The binding of Varp to VAMP7 traps VAMP7 in a closed, fusogenically inactive conformation. <i> Schäfer IB, Hesketh GG, Bright NA, Gray SR, Pryor PR, Evans PR, Luzio JP, Owen DJ. </i> Nat Struct Mol Biol, 2012","date":"2022-08-05T14:22:16.970Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4B93"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-08T17:50:34.906Z"}},{"start":619,"end":640,"reference_id":"24856514","reference_source":"pmid","reference_html":"VARP is recruited on to endosomes by direct interaction with retromer, where together they function in export to the cell surface. <i> Hesketh GG, Pérez-Dorado I, Jackson LP, Wartosch L, Schäfer IB, Gray SR, McCoy AJ, Zeldin OB, Garman EF, Harbour ME, Evans PR, Seaman MNJ, Luzio JP, Owen DJ. </i> Dev Cell, 2014","date":"2022-09-30T14:05:34.024Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"Crystals of VARP451–640His6: Rab321–225(Q85L) were grown by sitting drop vapor diffusion at 18°C against well solutions containing 14%–19% (w/v) of polyethylene glycol 3350 and 200 mM sodium citrate, pH 8.0, at an initial complex concentration of 2.5 mg/ml. "}]}],"cross_refs":[{"db":"PDB","id":"4CYM"}],"region_id":"DP02601r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q13637","statements":[{"type":"Methods","text":"Crystals of VARP451–640His6: Rab321–225(Q85L) were grown by sitting drop vapor diffusion at 18°C against well solutions containing 14%–19% (w/v) of polyethylene glycol 3350 and 200 mM sodium citrate, pH 8.0, at an initial complex concentration of 2.5 mg/ml. "}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"1963","entry_name":"guanosine 5'-[beta,gamma-methylene]triphosphate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"}],"sequence_construct":"GPLGSMDPSVVTPFSRDDRGHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALVYYDVESCRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSVMEAYHLSFERRQKSSEAPVQSPQRSVDHHHHHH","statement":[{"text":" The final model comprises three molecules of the complex in the asymmetric unit, where VARP (residues 452–618), Rab32 (residues 22–198), and Rab32’s bound GppCp:Mg2+ are well defined in the electron density map (Figures S1C and S1D).","type":"Results"}]}],"released":"2023_12","length":1050,"ncbi_taxon_id":9606,"date":"2020-03-03T15:27:37.286Z","organism":"Homo sapiens","features":{"gene3D":[{"start":665,"end":895,"id":"G3DSA:1.25.40.20","name":"Ankyrin repeat-containing domain"},{"start":665,"end":895,"id":"G3DSA:1.25.40.20","name":"Ankyrin repeat-containing domain"},{"start":133,"end":378,"id":"G3DSA:1.20.1050.80","name":"G3DSA:1.20.1050.80"}],"pfam":[{"id":"PF00023","name":"Ankyrin repeat","start":463,"end":493},{"id":"PF02204","name":"Vacuolar sorting protein 9 (VPS9) domain","start":266,"end":364},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":513,"end":594},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":734,"end":807},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":808,"end":871}]},"disprot_id":"DP02601","regions_counter":4,"dataset":[],"UniParc":"UPI000006D08A","uniref100":"UniRef100_Q96NW4","uniref90":"UniRef90_Q96NW4","uniref50":"UniRef50_Q96NW4","genes":[{"name":{"value":"ANKRD27"},"orfNames":[{"value":"PP12899"}]}],"alphafold_very_low_content":0.24952380952380954,"disorder_content":0.05904761904761905,"disprot_consensus":{"full":[{"start":619,"end":640,"type":"D"},{"start":693,"end":732,"type":"D"}],"Structural state":[{"start":619,"end":640,"type":"D"},{"start":693,"end":732,"type":"D"}],"Disorder function":[{"start":693,"end":732,"type":"F"}]}},{"acc":"P70280","name":"Vesicle-associated membrane protein 7","sequence":"MAILFAVVARGTTILAKHAWCGGNFLEVTEQILAKIPSENNKLTYSHGNYLFHYICQDRIVYLCITDDDFERSRAFSFLNEVKKRFQTTYGSRAQTALPYAMNSEFSSVLAAQLKHHSENKSLDKVMETQAQVDELKGIMVRNIDLVAQRGERLELLIDKTENLVDSSVTFKTTSRNLARAMCMKNIKLTIIIIIVSIVFIYIIVSLLCGGFTWPNCVKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":188,"region_id":"DP02602r001","start":164,"term_id":"IDPO:0000002","statement":[{"text":"In the Varp–VAMP7 complex, the final 24 residues of the VAMP7 cytosolic region (164–188), which are dispensable for binding to Varp (Fig. 1 and Supplementary Fig. 6), are not visible in the structure.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23104059","version":2,"reference_html":"The binding of Varp to VAMP7 traps VAMP7 in a closed, fusogenically inactive conformation. <i> Schäfer IB, Hesketh GG, Bright NA, Gray SR, Pryor PR, Evans PR, Luzio JP, Owen DJ. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4B93"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":220,"ncbi_taxon_id":10090,"date":"2020-03-03T15:34:07.292Z","organism":"Mus musculus","features":{"gene3D":[],"pfam":[{"id":"PF00957","name":"Synaptobrevin","start":125,"end":205},{"id":"PF13774","name":"Regulated-SNARE-like domain","start":15,"end":110}]},"disprot_id":"DP02602","regions_counter":2,"dataset":[],"UniParc":"UPI0000022697","uniref100":"UniRef100_P70280","uniref90":"UniRef90_P70280","uniref50":"UniRef50_P70280","genes":[{"name":{"value":"Vamp7"},"synonyms":[{"value":"Sybl1"}]}],"alphafold_very_low_content":0.02727272727272727,"disorder_content":0.11363636363636363,"disprot_consensus":{"full":[{"start":164,"end":188,"type":"D"}],"Structural state":[{"start":164,"end":188,"type":"D"}]}},{"acc":"P20020-1","name":"Isoform D of Plasma membrane calcium-transporting ATPase 1","sequence":"MGDMANNSVAYSGVKNSLKEANHDGDFGITLAELRALMELRSTDALRKIQESYGDVYGICTKLKTSPNEGLSGNPADLERREAVFGKNFIPPKKPKTFLQLVWEALQDVTLIILEIAAIVSLGLSFYQPPEGDNALCGEVSVGEEEGEGETGWIEGAAILLSVVCVVLVTAFNDWSKEKQFRGLQSRIEQEQKFTVIRGGQVIQIPVADITVGDIAQVKYGDLLPADGILIQGNDLKIDESSLTGESDHVKKSLDKDPLLLSGTHVMEGSGRMVVTAVGVNSQTGIIFTLLGAGGEEEEKKDEKKKEKKNKKQDGAIENRNKAKAQDGAAMEMQPLKSEEGGDGDEKDKKKANLPKKEKSVLQGKLTKLAVQIGKAGLLMSAITVIILVLYFVIDTFWVQKRPWLAECTPIYIQYFVKFFIIGVTVLVVAVPEGLPLAVTISLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTMNRMTVVQAYINEKHYKKVPEPEAIPPNILSYLVTGISVNCAYTSKILPPEKEGGLPRHVGNKTECALLGLLLDLKRDYQDVRNEIPEEALYKVYTFNSVRKSMSTVLKNSDGSYRIFSKGASEIILKKCFKILSANGEAKVFRPRDRDDIVKTVIEPMASEGLRTICLAFRDFPAGEPEPEWDNENDIVTGLTCIAVVGIEDPVRPEVPDAIKKCQRAGITVRMVTGDNINTARAIATKCGILHPGEDFLCLEGKDFNRRIRNEKGEIEQERIDKIWPKLRVLARSSPTDKHTLVKGIIDSTVSDQRQVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVKAVMWGRNVYDSISKFLQFQLTVNVVAVIVAFTGACITQDSPLKAVQMLWVNLIMDTLASLALATEPPTESLLLRKPYGRNKPLISRTMMKNILGHAFYQLVVVFTLLFAGEKFFDIDSGRNAPLHAPPSEHYTIVFNTFVLMQLFNEINARKIHGERNVFEGIFNNAIFCTIVLGTFVVQIIIVQFGGKPFSCSELSIEQWLWSIFLGMGTLLWGQLISTIPTSRLKFLKEAGHGTQKEEIPEEELAEDVEEIDHAERELRRGQILWFRGLNRIQTQMDVVNAFQSGSSIQGALRRQPSIASQHHDVTNISTPTHIRVVNAFRSSLYEGLEKPESRSSIHNFMTHPEFRIEDSEPHIPLIDDTDAEDDAPTKRNSSPPPSPNKNNNAVDSGIHLTIEMNKSATSSSPGSPLHSLETSL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1258,"region_id":"DP02604r001","start":1063,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The C-terminal autoinhibitory domain and the phospholipid-binding domain in the first cytosolic loop of the PMCAs are not resolved, suggesting structural flexibility in these regions.","type":"Results"},{"text":"PMCAs have a unique autoinhibitory domain at N terminus (in plants) or C terminus (in mammals)","type":"Introduction"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30190470","version":2,"reference_html":"Structure of the human plasma membrane Ca<sup>2+</sup>-ATPase 1 in complex with its obligatory subunit neuroplastin. <i> Gong D, Chi X, Ren K, Huang G, Zhou G, Yan N, Lei J, Zhou Q. </i> Nat Commun, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6A69"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1258,"region_id":"DP02604r002","start":1063,"term_id":"GO:0140678","unpublished":true,"statement":[{"text":"The C-terminal autoinhibitory domain and the phospholipid-binding domain in the first cytosolic loop of the PMCAs are not resolved, suggesting structural flexibility in these regions.","type":"Results"},{"text":"PMCAs have a unique autoinhibitory domain at N terminus (in plants) or C terminus (in mammals)","type":"Introduction"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"cryogenic electron microscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"30190470","version":3,"reference_html":"Structure of the human plasma membrane Ca<sup>2+</sup>-ATPase 1 in complex with its obligatory subunit neuroplastin. <i> Gong D, Chi X, Ren K, Huang G, Zhou G, Yan N, Lei J, Zhou Q. </i> Nat Commun, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","cross_refs":[{"db":"PDB","id":"6A69"}],"term_name":"molecular function inhibitor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2023_12","length":1258,"ncbi_taxon_id":9606,"date":"2020-03-03T16:08:28.720Z","organism":"Homo sapiens","features":{"pfam":[]},"disprot_id":"DP02604","regions_counter":2,"dataset":[],"UniParc":"UPI00001261E9","uniref100":"","uniref90":"","uniref50":"","genes":[{"name":{"value":"ATP2B1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:814","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:814"}}]},"synonyms":[{"value":"PMCA1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8396145","url":"http://www.ncbi.nlm.nih.gov/pubmed/8396145","alternativeUrl":"https://europepmc.org/abstract/MED/8396145"}}]}]}],"disorder_content":0.15580286168521462,"disprot_consensus":{"full":[{"start":1063,"end":1258,"type":"D"}],"Structural state":[{"start":1063,"end":1258,"type":"D"}],"Molecular function":[{"start":1063,"end":1258,"type":"F"}]}},{"acc":"P02533","name":"Keratin, type I cytoskeletal 14","sequence":"MTTCSRQFTSSSSMKGSCGIGGGIGGGSSRISSVLAGGSCRAPSTYGGGLSVSSSRFSSGGACGLGGGYGGGFSSSSSSFGSGFGGGYGGGLGAGLGGGFGGGFAGGDGLLVGSEKVTMQNLNDRLASYLDKVRALEEANADLEVKIRDWYQRQRPAEIKDYSPYFKTIEDLRNKILTATVDNANVLLQIDNARLAADDFRTKYETELNLRMSVEADINGLRRVLDELTLARADLEMQIESLKEELAYLKKNHEEEMNALRGQVGGDVNVEMDAAPGVDLSRILNEMRDQYEKMAEKNRKDAEEWFFTKTEELNREVATNSELVQSGKSEISELRRTMQNLEIELQSQLSMKASLENSLEETKGRYCMQLAQIQEMIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAHLSSSQFSSGSQSSRDVTSSSRQIRTKVMDVHDGKVVSTHEQVLRTKN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":331,"region_id":"DP02605r001","start":295,"term_id":"IDPO:0000002","statement":[{"text":"We crystallized a complex of K5 L2-2B and K14 L2-2B (Fig. 1a), which behaves as a functional assembly intermediate in vitro and in vivo (Supplementary Fig. 1a–c). The resulting structure includes residues Thr382– Gly476 of K5 and Ser332–Gly421 of K14 (Supplementary Fig. 1d). The L2 region and N-terminal end of the 2B domains of K5 and K14 are not well ordered in the crystal, and we did not model them.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22705788","version":2,"reference_html":"Structural basis for heteromeric assembly and perinuclear organization of keratin filaments. <i> Lee CH, Kim MS, Chung BM, Leahy DJ, Coulombe PA. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3TNU"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":331,"region_id":"DP02605r002","start":295,"term_id":"IDPO:0000033","statement":[{"text":"We crystallized a complex of K5 L2-2B and K14 L2-2B (Fig. 1a), which behaves as a functional assembly intermediate in vitro and in vivo (Supplementary Fig. 1a–c). The resulting structure includes residues Thr382– Gly476 of K5 and Ser332–Gly421 of K14 (Supplementary Fig. 1d). The L2 region and N-terminal end of the 2B domains of K5 and K14 are not well ordered in the crystal, and we did not model them.","type":"Results"},{"text":"Although variable in size (40–240 kDa) and primary structure, all intermediate filament proteins feature a central α-helical rod domain of conserved length and substructure comprising four heptad repeat– containing segments (1A, 1B, 2A and 2B) interrupted by three short linker sequences (L1, L12 and L2) at conserved locations","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22705788","version":3,"reference_html":"Structural basis for heteromeric assembly and perinuclear organization of keratin filaments. <i> Lee CH, Kim MS, Chung BM, Leahy DJ, Coulombe PA. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3TNU"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2020_12","length":472,"ncbi_taxon_id":9606,"date":"2020-03-03T16:49:13.011Z","organism":"Homo sapiens","features":{"gene3D":[{"start":149,"end":265,"id":"G3DSA:1.20.5.1160","name":"Vasodilator-stimulated phosphoprotein"}],"pfam":[{"id":"PF00038","name":"Intermediate filament protein","start":114,"end":424}]},"disprot_id":"DP02605","regions_counter":2,"dataset":[],"UniParc":"UPI000000D9D9","uniref100":"UniRef100_P02533","uniref90":"UniRef90_P02533","uniref50":"UniRef50_P02533","genes":[{"name":{"value":"KRT14"}}],"alphafold_very_low_content":0.3072033898305085,"disorder_content":0.07838983050847458,"disprot_consensus":{"full":[{"start":295,"end":331,"type":"D"}],"Structural state":[{"start":295,"end":331,"type":"D"}],"Disorder function":[{"start":295,"end":331,"type":"F"}]}},{"acc":"P13647","name":"Keratin, type II cytoskeletal 5","sequence":"MSRQSSVSFRSGGSRSFSTASAITPSVSRTSFTSVSRSGGGGGGGFGRVSLAGACGVGGYGSRSLYNLGGSKRISISTSGGSFRNRFGAGAGGGYGFGGGAGSGFGFGGGAGGGFGLGGGAGFGGGFGGPGFPVCPPGGIQEVTVNQSLLTPLNLQIDPSIQRVRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRQNLEPLFEQYINNLRRQLDSIVGERGRLDSELRNMQDLVEDFKNKYEDEINKRTTAENEFVMLKKDVDAAYMNKVELEAKVDALMDEINFMKMFFDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIANRSRTEAESWYQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRAEIDNVKKQCANLQNAIADAEQRGELALKDARNKLAELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEGEECRLSGEGVGPVNISVVTSSVSSGYGSGSGYGGGLGGGLGGGLGGGLAGGSSGSYYSSSSGGVGLGGGLSVGGSGFSASSGRGLGVGFGSGGGSSSSVKFVSTTSSSRKSFKS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":381,"region_id":"DP02606r001","start":350,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"We crystallized a complex of K5 L2-2B and K14 L2-2B (Fig. 1a), which behaves as a functional assembly intermediate in vitro and in vivo (Supplementary Fig. 1a–c). The resulting structure includes residues Thr382– Gly476 of K5 and Ser332–Gly421 of K14 (Supplementary Fig. 1d). The L2 region and N-terminal end of the 2B domains of K5 and K14 are not well ordered in the crystal, and we did not model them. X-ray data collection and refinement statistics are reported in Table 1. The structure of the 2B domain of K5–K14 reveals a typical left-handed coiled-coil dimer, with the two α-helices oriented in parallel and in register (Fig. 1b) and one coiled-coil heterodimer of K5–K14 2B domains per asymmetric unit.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22705788","version":2,"reference_html":"Structural basis for heteromeric assembly and perinuclear organization of keratin filaments. <i> Lee CH, Kim MS, Chung BM, Leahy DJ, Coulombe PA. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3TNU"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":381,"region_id":"DP02606r002","start":350,"term_id":"IDPO:0000033","unpublished":true,"statement":[{"text":"We crystallized a complex of K5 L2-2B and K14 L2-2B (Fig. 1a), which behaves as a functional assembly intermediate in vitro and in vivo (Supplementary Fig. 1a–c). The resulting structure includes residues Thr382– Gly476 of K5 and Ser332–Gly421 of K14 (Supplementary Fig. 1d). The L2 region and N-terminal end of the 2B domains of K5 and K14 are not well ordered in the crystal, and we did not model them. X-ray data collection and refinement statistics are reported in Table 1. The structure of the 2B domain of K5–K14 reveals a typical left-handed coiled-coil dimer, with the two α-helices oriented in parallel and in register (Fig. 1b) and one coiled-coil heterodimer of K5–K14 2B domains per asymmetric unit.","type":"Results"},{"text":"Although variable in size (40–240 kDa) and primary structure, all intermediate filament proteins feature a central α-helical rod domain of conserved length and substructure comprising four heptad repeat– containing segments (1A, 1B, 2A and 2B) interrupted by three short linker sequences (L1, L12 and L2) at conserved locations","type":"Article"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22705788","version":3,"reference_html":"Structural basis for heteromeric assembly and perinuclear organization of keratin filaments. <i> Lee CH, Kim MS, Chung BM, Leahy DJ, Coulombe PA. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3TNU"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":1,"end":167,"reference_id":"26231765","reference_source":"pmid","reference_html":"Order and disorder in intermediate filament proteins. <i> Kornreich M, Avinery R, Malka-Gibor E, Laser-Azogui A, Beck R. </i> FEBS Lett, 2015","date":"2022-09-30T15:15:30.225Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02606r003","statement":[{"text":"All IF proteins share a common tripartite structure consisting of a central α-helical rod domain, and disordered N-terminal head and C-terminal tail domains.","type":"Introduction"},{"text":"The rod domain corresponds to the 168-481 region.","type":"Curator statement"}]},{"start":482,"end":590,"reference_id":"26231765","reference_source":"pmid","reference_html":"Order and disorder in intermediate filament proteins. <i> Kornreich M, Avinery R, Malka-Gibor E, Laser-Azogui A, Beck R. </i> FEBS Lett, 2015","date":"2022-09-30T15:15:12.482Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02606r004","statement":[{"text":"All IF proteins share a common tripartite structure consisting of a central α-helical rod domain, and disordered N-terminal head and C-terminal tail domains.","type":"Introduction"},{"text":"The rod domain corresponds to the 168-481 region.","type":"Curator statement"}]},{"start":1,"end":167,"reference_id":"26181054","reference_source":"pmid","reference_html":"Complete Structure of an Epithelial Keratin Dimer: Implications for Intermediate Filament Assembly. <i> Bray DJ, Walsh TR, Noro MG, Notman R. </i> PLoS One, 2015","date":"2022-09-30T15:23:01.448Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02606r005","statement":[{"text":"Current understanding on the head and tail domains indicates that these correspond with intrinsically-disordered regions of the keratin protein [21].","type":"Introduction"},{"text":"The head domain corresponds to the 1-167 region.","type":"Curator statement"}]},{"start":478,"end":590,"reference_id":"26181054","reference_source":"pmid","reference_html":"Complete Structure of an Epithelial Keratin Dimer: Implications for Intermediate Filament Assembly. <i> Bray DJ, Walsh TR, Noro MG, Notman R. </i> PLoS One, 2015","date":"2022-09-30T15:24:12.326Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02606r006","statement":[{"text":"Current understanding on the head and tail domains indicates that these correspond with intrinsically-disordered regions of the keratin protein [21].","type":"Introduction"},{"text":"The tail domain corresponds to the 478-590 region.","type":"Curator statement"}]}],"released":"2023_12","length":590,"ncbi_taxon_id":9606,"date":"2020-03-03T16:53:33.278Z","organism":"Homo sapiens","features":{"gene3D":[{"start":203,"end":320,"id":"G3DSA:1.20.5.1160","name":"Vasodilator-stimulated phosphoprotein"}],"pfam":[{"id":"PF00038","name":"Intermediate filament protein","start":167,"end":480},{"id":"PF16208","name":"Keratin type II head","start":16,"end":164}]},"disprot_id":"DP02606","regions_counter":6,"dataset":[],"UniParc":"UPI000012DB0D","uniref100":"UniRef100_P13647","uniref90":"UniRef90_P13647","uniref50":"UniRef50_P13647","genes":[{"name":{"value":"KRT5"}}],"alphafold_very_low_content":0.4542372881355932,"disorder_content":0.5288135593220339,"disprot_consensus":{"full":[{"start":1,"end":167,"type":"D"},{"start":350,"end":381,"type":"D"},{"start":478,"end":590,"type":"D"}],"Structural state":[{"start":1,"end":167,"type":"D"},{"start":350,"end":381,"type":"D"},{"start":478,"end":590,"type":"D"}],"Disorder function":[{"start":350,"end":381,"type":"F"}]}},{"acc":"Q9UNA0","name":"A disintegrin and metalloproteinase with thrombospondin motifs 5","sequence":"MLLGWASLLLCAFRLPLAAVGPAATPAQDKAGQPPTAAAAAQPRRRQGEEVQERAEPPGHPHPLAQRRRSKGLVQNIDQLYSGGGKVGYLVYAGGRRFLLDLERDGSVGIAGFVPAGGGTSAPWRHRSHCFYRGTVDGSPRSLAVFDLCGGLDGFFAVKHARYTLKPLLRGPWAEEEKGRVYGDGSARILHVYTREGFSFEALPPRASCETPASTPEAHEHAPAHSNPSGRAALASQLLDQSALSPAGGSGPQTWWRRRRRSISRARQVELLLVADASMARLYGRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLGDKDKSLEVSKNAATTLKNFCKWQHQHNQLGDDHEEHYDAAILFTREDLCGHHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDSKFCEETFGSTEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLLDLPRKQILGPEELPGQTYDATQQCNLTFGPEYSVCPGMDVCARLWCAVVRQGQMVCLTKKLPAVEGTPCGKGRICLQGKCVDKTKKKYYSTSSHGNWGSWGSWGQCSRSCGGGVQFAYRHCNNPAPRNNGRYCTGKRAIYRSCSLMPCPPNGKSFRHEQCEAKNGYQSDAKGVKTFVEWVPKYAGVLPADVCKLTCRAKGTGYYVVFSPKVTDGTECRLYSNSVCVRGKCVRTGCDGIIGSKLQYDKCGVCGGDNSSCTKIVGTFNKKSKGYTDVVRIPEGATHIKVRQFKAKDQTRFTAYLALKKKNGEYLINGKYMISTSETIIDINGTVMNYSGWSHRDDFLHGMGYSATKEILIVQILATDPTKPLDVRYSFFVPKKSTPKVNSVTSHGSNKVGSHTSQPQWVTGPWLACSRTCDTGWHTRTVQCQDGNRKLAKGCPLSQRPSAFKQCLLKKC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":628,"region_id":"DP02607r001","start":557,"term_id":"IDPO:0000002","statement":[{"text":"Although the amino acid sequence of the crystallized protein encompasses three domains—catalytic, disintegrin-like domain, and thrombospondin-like domain—the latter domain, residues 557–628, has no supporting electron density, presumably because of disorder.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18042673","version":2,"reference_html":"Crystal structures of the two major aggrecan degrading enzymes, ADAMTS4 and ADAMTS5. <i> Mosyak L, Georgiadis K, Shane T, Svenson K, Hebert T, McDonagh T, Mackie S, Olland S, Lin L, Zhong X, Kriz R, Reifenberg EL, Collins-Racie LA, Corcoran C, Freeman B, Zollner R, Marvell T, Vera M, Sum PE, Lavallie ER, Stahl M, Somers W. </i> Protein Sci, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2RJQ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":628,"region_id":"DP02607r002","start":557,"term_id":"GO:0098772","statement":[{"text":"Although the amino acid sequence of the crystallized protein encompasses three domains—catalytic, disintegrin-like domain, and thrombospondin-like domain—the latter domain, residues 557–628, has no supporting electron density, presumably because of disorder.","type":"Methods"},{"text":"In combination with the thrombospondin type I domain, the disintegrin-like domain was proposed to play an important role in recognition of substrate folding topology (Lauer-Fields et al. 2007).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18042673","version":3,"reference_html":"Crystal structures of the two major aggrecan degrading enzymes, ADAMTS4 and ADAMTS5. <i> Mosyak L, Georgiadis K, Shane T, Svenson K, Hebert T, McDonagh T, Mackie S, Olland S, Lin L, Zhong X, Kriz R, Reifenberg EL, Collins-Racie LA, Corcoran C, Freeman B, Zollner R, Marvell T, Vera M, Sum PE, Lavallie ER, Stahl M, Somers W. </i> Protein Sci, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","cross_refs":[{"db":"PDB","id":"2RJQ"}],"term_name":"molecular function regulator","curator_orcid":"0000-0002-0341-4888","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","length":930,"ncbi_taxon_id":9606,"date":"2020-03-03T17:01:23.948Z","organism":"Homo sapiens","features":{"gene3D":[{"start":264,"end":480,"id":"G3DSA:3.40.390.10","name":"Collagenase (Catalytic Domain)"},{"start":876,"end":930,"id":"G3DSA:2.20.100.10","name":"Thrombospondin type-1 (TSP1) repeat"},{"start":876,"end":930,"id":"G3DSA:2.20.100.10","name":"Thrombospondin type-1 (TSP1) repeat"}],"pfam":[{"id":"PF00090","name":"Thrombospondin type 1 domain","start":572,"end":621},{"id":"PF01421","name":"Reprolysin (M12B) family zinc metalloprotease","start":269,"end":476},{"id":"PF05986","name":"ADAM-TS Spacer 1","start":734,"end":852},{"id":"PF17771","name":"ADAMTS cysteine-rich domain 2","start":487,"end":554},{"id":"PF19030","name":"Thrombospondin type 1 domain","start":879,"end":930},{"id":"PF19236","name":"ADAMTS cysteine-rich domain","start":628,"end":731}]},"disprot_id":"DP02607","regions_counter":2,"dataset":["Extracellular matrix proteins"],"UniParc":"UPI00001AEAC2","uniref100":"UniRef100_Q9UNA0","uniref90":"UniRef90_Q9UNA0","uniref50":"UniRef50_Q9UNA0","genes":[{"name":{"value":"ADAMTS5"},"synonyms":[{"value":"ADAMTS11"},{"value":"ADMP2"}]}],"alphafold_very_low_content":0.1827956989247312,"disorder_content":0.07741935483870968,"disprot_consensus":{"full":[{"start":557,"end":628,"type":"D"}],"Structural state":[{"start":557,"end":628,"type":"D"}],"Molecular function":[{"start":557,"end":628,"type":"F"}]}},{"acc":"Q8IUQ4","name":"E3 ubiquitin-protein ligase SIAH1","sequence":"MSRQTATALPTGTSKCPPSQRVPALTGTTASNNDLASLFECPVCFDYVLPPILQCQSGHLVCSNCRPKLTCCPTCRGPLGSIRNLAMEKVANSVLFPCKYASSGCEITLPHTEKADHEELCEFRPYSCPCPGASCKWQGSLDAVMPHLMHQHKSITTLQGEDIVFLATDINLPGAVDWVMMQSCFGFHFMLVLEKQEKYDGHQQFFAIVQLIGTRKQAENFAYRLELNGHRRRLTWEATPRSIHEGIATAIMNSDCLVFDTSIAQLFAENGNLGINVTISMC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":124,"region_id":"DP02608r001","start":90,"term_id":"IDPO:0000002","statement":[{"text":"No electron density was observed for residues 90-124.","type":"Methods"}],"curator_id":"vnugnes","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"16085652","version":3,"reference_html":"Structural analysis of Siah1-Siah-interacting protein interactions and insights into the assembly of an E3 ligase multiprotein complex. <i> Santelli E, Leone M, Li C, Fukushima T, Preece NE, Olson AJ, Ely KR, Reed JC, Pellecchia M, Liddington RC, Matsuzawa S. </i> J Biol Chem, 2005","date":"2023-06-13T14:31:02.257Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2A25"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9HB71"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"}]}],"released":"2021_06","length":282,"ncbi_taxon_id":9606,"date":"2020-03-03T17:18:01.797Z","organism":"Homo sapiens","features":{"gene3D":[{"start":93,"end":282,"id":"G3DSA:2.60.210.10","name":"Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A"},{"start":26,"end":127,"id":"G3DSA:3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"}],"pfam":[{"id":"PF03145","name":"Sina, TRAF-like domain","start":182,"end":278},{"id":"PF21361","name":"Sina, zinc finger","start":89,"end":165},{"id":"PF21362","name":"E3 ubiquitin-protein ligase sina/sinah, RING finger","start":41,"end":75}]},"disprot_id":"DP02608","regions_counter":1,"dataset":["NDDs-related proteins"],"UniParc":"UPI0000073CF6","uniref100":"UniRef100_Q8IUQ4","uniref90":"UniRef90_Q8IUQ4","uniref50":"UniRef50_Q8IUQ4","genes":[{"name":{"value":"SIAH1"},"synonyms":[{"value":"HUMSIAH"}]}],"alphafold_very_low_content":0.09219858156028368,"disorder_content":0.12411347517730496,"disprot_consensus":{"full":[{"start":90,"end":124,"type":"D"}],"Structural state":[{"start":90,"end":124,"type":"D"}]}},{"acc":"Q96PY5","name":"Formin-like protein 2","sequence":"MGNAGSMDSQQTDFRAHNVPLKLPMPEPGELEERFAIVLNAMNLPPDKARLLRQYDNEKKWELICDQERFQVKNPPHTYIQKLKGYLDPAVTRKKFRRRVQESTQVLRELEISLRTNHIGWVREFLNEENKGLDVLVEYLSFAQYAVTFDFESVESTVESSVDKSKPWSRSIEDLHRGSNLPSPVGNSVSRSGRHSALRYNTLPSRRTLKNSRLVSKKDDVHVCIMCLRAIMNYQYGFNMVMSHPHAVNEIALSLNNKNPRTKALVLELLAAVCLVRGGHEIILSAFDNFKEVCGEKQRFEKLMEHFRNEDNNIDFMVASMQFINIVVHSVEDMNFRVHLQYEFTKLGLDEYLDKLKHTESDKLQVQIQAYLDNVFDVGALLEDAETKNAALERVEELEENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKMVKEKEEAIQRQSTLEKKIHELEKQGTIKIQKKGDGDIAILPVVASGTLSMGSEVVAGNSVGPTMGAASSGPLPPPPPPLPPSSDTPETVQNGPVTPPMPPPPPPPPPPPPPPPPPPPPPLPGPAAETVPAPPLAPPLPSAPPLPGTSSPTVVFNSGLAAVKIKKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERILEDLNVDEFEEIFKTKAQGPAIDLSSSKQKIPQKGSNKVTLLEANRAKNLAITLRKAGKTADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERERKPLENLSDEDRFMMQFSKIERLMQKMTIMAFIGNFAESIQMLTPQLHAIIAASVSIKSSQKLKKILEIILALGNYMNSSKRGAVYGFKLQSLDLLLDTKSTDRKQTLLHYISNVVKEKYHQVSLFYNELHYVEKAAAVSLENVLLDVKELQRGMDLTKREYTMHDHNTLLKEFILNNEGKLKKLQDDAKIAQDAFDDVVKYFGENPKTTPPSVFFPVFVRFVKAYKQAEEENELRKKQEQALMEKLLEQEALMEQQDPKSPSHKSKRQQQELIAELRRRQVKDNRHVYEGKDGAIEDIITVLKTVPFTARTAKRGSRFFCEPVLTEEYHY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":204,"region_id":"DP02609r001","start":150,"term_id":"IDPO:0000002","statement":[{"text":"The flexible loop of 55 residues that is not resolved in the electron density map of the FMNL2N–Cdc42 structure is directly preceding the second basic helix α9. Interestingly, this loop is missing in one splice variant of FMNL3, isoform 2, but otherwise conserved in all FMNLs","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"25963737","version":2,"reference_html":"The structure of FMNL2-Cdc42 yields insights into the mechanism of lamellipodia and filopodia formation. <i> Kühn S, Erdmann C, Kage F, Block J, Schwenkmezger L, Steffen A, Rottner K, Geyer M. </i> Nat Commun, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4YC7"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":204,"region_id":"DP02609r002","start":150,"term_id":"IDPO:0000033","statement":[{"text":"The flexible loop of 55 residues that is not resolved in the electron density map of the FMNL2N–Cdc42 structure is directly preceding the second basic helix α9. Interestingly, this loop is missing in one splice variant of FMNL3, isoform 2, but otherwise conserved in all FMNLs","type":"Results"},{"text":"Proteomic analyses identified a phosphorylation site for S171 (ref. 41), which is in the centre of the flexible loop preceding helix α9 (Supplementary Fig. 4) and not resolved in the crystal structure.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"25963737","version":3,"reference_html":"The structure of FMNL2-Cdc42 yields insights into the mechanism of lamellipodia and filopodia formation. <i> Kühn S, Erdmann C, Kage F, Block J, Schwenkmezger L, Steffen A, Rottner K, Geyer M. </i> Nat Commun, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4YC7"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"region_id":"DP02609r003","ec_ontology":"ECO","end":173,"term_id":"IDPO:0000045","start":169,"version":2,"statement":[{"text":"The flexible loop of 55 residues that is not resolved in the electron density map of the FMNL2N–Cdc42 structure is directly preceding the second basic helix α9. Interestingly, this loop is missing in one splice variant of FMNL3, isoform 2, but otherwise conserved in all FMNLs","type":"Results"},{"text":"Proteomic analyses identified a phosphorylation site for S171 (ref. 41), which is in the centre of the flexible loop preceding helix α9 (Supplementary Fig. 4) and not resolved in the crystal structure.","type":"Results"}],"term_name":"phosphorylation display site","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"25963737","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4YC7"}],"term_namespace":"Disorder function","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"The structure of FMNL2-Cdc42 yields insights into the mechanism of lamellipodia and filopodia formation. <i> Kühn S, Erdmann C, Kage F, Block J, Schwenkmezger L, Steffen A, Rottner K, Geyer M. </i> Nat Commun, 2015","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2020_12","length":1086,"ncbi_taxon_id":9606,"date":"2020-03-03T17:29:02.971Z","organism":"Homo sapiens","features":{"gene3D":[{"start":608,"end":994,"id":"G3DSA:1.20.58.2220","name":"G3DSA:1.20.58.2220"}],"pfam":[{"id":"PF02181","name":"Formin Homology 2 Domain","start":617,"end":982},{"id":"PF06367","name":"Diaphanous FH3 Domain","start":280,"end":470},{"id":"PF06371","name":"Diaphanous GTPase-binding Domain","start":24,"end":143},{"id":"PF06371","name":"Diaphanous GTPase-binding Domain","start":217,"end":275}]},"disprot_id":"DP02609","regions_counter":3,"dataset":[],"UniParc":"UPI00000717E2","uniref100":"UniRef100_Q96PY5","uniref90":"UniRef90_Q96PY5","uniref50":"UniRef50_Q96PY5","genes":[{"name":{"value":"FMNL2"},"synonyms":[{"value":"FHOD2"},{"value":"KIAA1902"}]}],"alphafold_very_low_content":0.2302025782688766,"disorder_content":0.05064456721915286,"disprot_consensus":{"full":[{"start":150,"end":204,"type":"D"}],"Structural state":[{"start":150,"end":204,"type":"D"}],"Disorder function":[{"start":150,"end":204,"type":"F"}]}},{"acc":"P22449","name":"Hepatocyte nuclear factor 4-alpha","sequence":"MRLSKTLADMDMADYSAALDPAYTTLEFENVQVLTMGNDTSPSEGANLNSSNSLGVSALCAICGDRATGKHYGASSCDGCKGFFRRSVRKNHMYSCRFSRQCVVDKDKRNQCRYCRLKKCFRAGMKKEAVQNERDRISTRRSSYEDSSLPSINALLQAEVLSQQITSPISGINGDIRAKKIANITDVCESMKEQLLVLVEWAKYIPAFCELLLDDQVALLRAHAGEHLLLGATKRSMVFKDVLLLGNDYIVPRHCPELAEMSRVSIRILDELVLPFQELQIDDNEYACLKAIIFFDPDAKGLSDPGKIKRLRSQVQVSLEDYINDRQYDSRGRFGELLLLLPTLQSITWQMIEQIQFIKLFGMAKIDNLLQEMLLGGSASDAPHAHHPLHPHLMQEHMGTNVIVANTMPSHLSNGQMCEWPRPRGQAATPETPQPSPPSGSGSESYKLLPGAITTIVKPPSAIPQPTITKQEAI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"creator":"fquaglia","regions":[{"region_id":"DP02610r001","ec_ontology":"ECO","end":382,"term_id":"IDPO:0000002","start":368,"version":2,"statement":[{"text":"Electron density is apparent for all residues except those at the amino (133–140) and carboxyl (368–382) termini of the domain and within the loop between α helices 1 and 3 (the 1/3 loop, residues 157–165).","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12193589","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1M7W"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Crystal structure of the HNF4 alpha ligand binding domain in complex with endogenous fatty acid ligand. <i> Dhe-Paganon S, Duda K, Iwamoto M, Chi YI, Shoelson SE. </i> J Biol Chem, 2002","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":474,"ncbi_taxon_id":10116,"date":"2020-03-04T09:09:23.809Z","organism":"Rattus norvegicus","features":{"gene3D":[{"start":49,"end":140,"id":"G3DSA:3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A"},{"start":126,"end":391,"id":"G3DSA:1.10.565.10","name":"Retinoid X Receptor"}],"pfam":[{"id":"PF00104","name":"Ligand-binding domain of nuclear hormone receptor","start":175,"end":361},{"id":"PF00105","name":"Double treble clef zinc finger, C4 type","start":59,"end":127}]},"disprot_id":"DP02610","regions_counter":1,"dataset":[],"UniParc":"UPI00001709AB","uniref100":"UniRef100_P22449","uniref90":"UniRef90_P22449","uniref50":"UniRef50_P41235","genes":[{"name":{"value":"Hnf4a"},"synonyms":[{"value":"Hnf-4"},{"value":"Hnf4"},{"value":"Nr2a1"},{"value":"Tcf14"}]}],"alphafold_very_low_content":0.3227848101265823,"disorder_content":0.03164556962025317,"disprot_consensus":{"full":[{"start":368,"end":382,"type":"D"}],"Structural state":[{"start":368,"end":382,"type":"D"}]}},{"acc":"Q8N1G2","name":"Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1","sequence":"MKRRTDPECTAPIKKQKKRVAELALSLSSTSDDEPPSSVSHGAKASTTSLSGSDSETEGKQHSSDSFDDAFKADSLVEGTSSRYSMYNSVSQKLMAKMGFREGEGLGKYSQGRKDIVEASSQKGRRGLGLTLRGFDQELNVDWRDEPEPSACEQVSWFPECTTEIPDTQEMSDWMVVGKRKMIIEDETEFCGEELLHSVLQCKSVFDVLDGEEMRRARTRANPYEMIRGVFFLNRAAMKMANMDFVFDRMFTNPRDSYGKPLVKDREAELLYFADVCAGPGGFSEYVLWRKKWHAKGFGMTLKGPNDFKLEDFYSASSELFEPYYGEGGIDGDGDITRPENISAFRNFVLDNTDRKGVHFLMADGGFSVEGQENLQEILSKQLLLCQFLMALSIVRTGGHFICKTFDLFTPFSVGLVYLLYCCFERVCLFKPITSRPANSERYVVCKGLKVGIDDVRDYLFAVNIKLNQLRNTDSDVNLVVPLEVIKGDHEFTDYMIRSNESHCSLQIKALAKIHAFVQDTTLSEPRQAEIRKECLRLWGIPDQARVAPSSSDPKSKFFELIQGTEIDIFSYKPTLLTSKTLEKIRPVFDYRCMVSGSEQKFLIGLGKSQIYTWDGRQSDRWIKLDLKTELPRDTLLSVEIVHELKGEGKAQRKISAIHILDVLVLNGTDVREQHFNQRIQLAEKFVKAVSKPSRPDMNPIRVKEVYRLEEMEKIFVRLEMKIIKGSSGTPKLSYTGRDDRHFVPMGLYIVRTVNEPWTMGFSKSFKKKFFYNKKTKDSTFDLPADSIAPFHICYYGRLFWEWGDGIRVHDSQKPQDQDKLSKEDVLSFIQMHRA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":140,"region_id":"DP02611r001","start":126,"term_id":"IDPO:0000002","statement":[{"text":"The figure-of-merit after phasing (before solvent modification) was 0.4, and the resulting experimental electron density maps were well defined, allowing the tracing of a model that consisted of residues 141–544 of the protein.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24402442","version":2,"reference_html":"Structural analysis of human 2'-O-ribose methyltransferases involved in mRNA cap structure formation. <i> Smietanski M, Werner M, Purta E, Kaminska KH, Stepinski J, Darzynkiewicz E, Nowotny M, Bujnicki JM. </i> Nat Commun, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4N4A"},{"db":"PDB","id":"4N48"},{"db":"PDB","id":"4N49"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":835,"ncbi_taxon_id":9606,"date":"2020-03-04T09:14:54.193Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF01585","name":"G-patch domain","start":88,"end":130},{"id":"PF01728","name":"FtsJ-like methyltransferase","start":233,"end":448}]},"disprot_id":"DP02611","regions_counter":1,"dataset":[],"UniParc":"UPI00000700C2","uniref100":"UniRef100_Q8N1G2","uniref90":"UniRef90_Q8N1G2","uniref50":"UniRef50_Q8N1G2","genes":[{"name":{"value":"CMTR1"},"synonyms":[{"value":"FTSJD2"},{"value":"KIAA0082"},{"value":"MTR1"}]}],"alphafold_very_low_content":0.09700598802395209,"disorder_content":0.017964071856287425,"disprot_consensus":{"full":[{"start":126,"end":140,"type":"D"}],"Structural state":[{"start":126,"end":140,"type":"D"}]}},{"acc":"Q9Y6D6","name":"Brefeldin A-inhibited guanine nucleotide-exchange protein 1","sequence":"MYEGKKTKNMFLTRALEKILADKEVKKAHHSQLRKACEVALEEIKAETEKQSPPHGEAKAGSSTLPPVKSKTNFIEADKYFLPFELACQSKCPRIVSTSLDCLQKLIAYGHLTGNAPDSTTPGKKLIDRIIETICGCFQGPQTDEGVQLQIIKALLTAVTSQHIEIHEGTVLQAVRTCYNIYLASKNLINQTTAKATLTQMLNVIFARMENQALQEAKQMEKERHRQHHHLLQSPVSHHEPESPQLRYLPPQTVDHISQEHEGDLDLHTNDVDKSLQDDTEPENGSDISSAENEQTEADQATAAETLSKNEVLYDGENHDCEEKPQDIVQNIVEEMVNIVVGDMGEGTTINASADGNIGTIEDGSDSENIQANGIPGTPISVAYTPSLPDDRLSVSSNDTQESGNSSGPSPGAKFSHILQKDAFLVFRSLCKLSMKPLSDGPPDPKSHELRSKILSLQLLLSILQNAGPIFRTNEMFINAIKQYLCVALSKNGVSSVPEVFELSLSIFLTLLSNFKTHLKMQIEVFFKEIFLYILETSTSSFDHKWMVIQTLTRICADAQSVVDIYVNYDCDLNAANIFERLVNDLSKIAQGRGSQELGMSNVQELSLRKKGLECLVSILKCMVEWSKDQYVNPNSQTTLGQEKPSEQEMSEIKHPETINRYGSLNSLESTSSSGIGSYSTQMSGTDNPEQFEVLKQQKEIIEQGIDLFNKKPKRGIQYLQEQGMLGTTPEDIAQFLHQEERLDSTQVGEFLGDNDKFNKEVMYAYVDQHDFSGKDFVSALRMFLEGFRLPGEAQKIDRLMEKFAARYLECNQGQTLFASADTAYVLAYSIIMLTTDLHSPQVKNKMTKEQYIKMNRGINDSKDLPEEYLSAIYNEIAGKKISMKETKELTIPTKSSKQNVASEKQRRLLYNLEMEQMAKTAKALMEAVSHVQAPFTSATHLEHVRPMFKLAWTPFLAAFSVGLQDCDDTEVASLCLEGIRCAIRIACIFSIQLERDAYVQALARFTLLTVSSGITEMKQKNIDTIKTLITVAHTDGNYLGNSWHEILKCISQLELAQLIGTGVKPRYISGTVRGREGSLTGTKDQAPDEFVGLGLVGGNVDWKQIASIQESIGETSSQSVVVAVDRIFTGSTRLDGNAIVDFVRWLCAVSMDELLSTTHPRMFSLQKIVEISYYNMGRIRLQWSRIWEVIGDHFNKVGCNPNEDVAIFAVDSLRQLSMKFLEKGELANFRFQKDFLRPFEHIMKRNRSPTIRDMVVRCIAQMVNSQAANIRSGWKNIFSVFHLAASDQDESIVELAFQTTGHIVTLVFEKHFPATIDSFQDAVKCLSEFACNAAFPDTSMEAIRLIRHCAKYVSDRPQAFKEYTSDDMNVAPEDRVWVRGWFPILFELSCIINRCKLDVRTRGLTVMFEIMKTYGHTYEKHWWQDLFRIVFRIFDNMKLPEQQTEKAEWMTTTCNHALYAICDVFTQYLEVLSDVLLDDIFAQLYWCVQQDNEQLARSGTNCLENVVILNGEKFTLEIWDKTCNCTLDIFKTTIPHALLTWRPNSGETAPPPPSPVSEKPLDTISQKSVDIHDSIQPRSVDNRPQAPLVSASAVNEEVSKIKSTAKFPEQKLFAALLIKCVVQLELIQTIDNIVFFPATSKKEDAENLAAAQRDAVDFDVRVDTQDQGMYRFLTSQQLFKLLDCLLESHRFAKAFNSNNEQRTALWKAGFKGKSKPNLLKQETSSLACGLRILFRMYMDESRVSAWEEVQQRLLNVCSEALSYFLTLTSESHREAWTNLLLLFLTKVLKISDNRFKAHASFYYPLLCEIMQFDLIPELRAVLRRFFLRIGVVFQISQPPEQELGINKQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":63,"region_id":"DP02612r001","start":50,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"We then determined the crystal structure of Arl1-GTP–DCB at 3.4 Å resolution (Supplementary Table S1). In the structure, each asymmetric unit contains one Arl1 (residues 17–181) bound with a GTP and a Mg2+ ion at the active site and one DCB domain (residues 14–49 and 64–221) (Figure 1B).","type":"Article"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27436755","version":2,"reference_html":"Structural basis for targeting BIG1 to Golgi apparatus through interaction of its DCB domain with Arl1. <i> Wang R, Wang Z, Wang K, Zhang T, Ding J. </i> J Mol Cell Biol, 2016","date":"2022-08-05T14:24:25.605Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5J5C"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-08T17:52:37.968Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":63,"region_id":"DP02612r002","start":50,"term_id":"IDPO:0000033","unpublished":true,"statement":[{"text":"We then determined the crystal structure of Arl1-GTP–DCB at 3.4 Å resolution (Supplementary Table S1). In the structure, each asymmetric unit contains one Arl1 (residues 17–181) bound with a GTP and a Mg2+ ion at the active site and one DCB domain (residues 14–49 and 64–221)","type":"Article"},{"text":"The DCB domain consists of eight α-helices forming four HEAT (Huntingtin, Elongation factor 3, protein phosphatase 2A, and the yeast kinase TOR1) repeats, and each repeat comprises of a pair of antiparallel α-helices connected by a flexible linker, resembling that in Thielavia terrestris Sec7 protein (Richardson et al., 2016) (Supplementary Figure S4A).","type":"Article"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27436755","version":3,"reference_html":"Structural basis for targeting BIG1 to Golgi apparatus through interaction of its DCB domain with Arl1. <i> Wang R, Wang Z, Wang K, Zhang T, Ding J. </i> J Mol Cell Biol, 2016","date":"2022-08-05T14:24:54.796Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5J5C"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P40616"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-08T17:53:29.390Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":13,"region_id":"DP02612r003","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"We then determined the crystal structure of Arl1-GTP–DCB at 3.4 Å resolution (Supplementary Table S1). In the structure, each asymmetric unit contains one Arl1 (residues 17–181) bound with a GTP and a Mg2+ ion at the active site and one DCB domain (residues 14–49 and 64–221) (Figure 1B).","type":"Article"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27436755","version":2,"reference_html":"Structural basis for targeting BIG1 to Golgi apparatus through interaction of its DCB domain with Arl1. <i> Wang R, Wang Z, Wang K, Zhang T, Ding J. </i> J Mol Cell Biol, 2016","date":"2022-08-05T14:24:19.628Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5J5C"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-08T17:52:39.035Z"}}],"released":"2023_06","length":1849,"ncbi_taxon_id":9606,"date":"2020-03-04T09:34:37.353Z","organism":"Homo sapiens","features":{"gene3D":[{"start":773,"end":891,"id":"G3DSA:1.10.1000.11","name":"Arf Nucleotide-binding Site Opener,domain 2"}],"pfam":[{"id":"PF01369","name":"Sec7 domain","start":698,"end":882},{"id":"PF09324","name":"Mon2/Sec7/BIG1-like, HDS","start":1220,"end":1301},{"id":"PF12783","name":"Mon2/Sec7/BIG1-like, HUS domain","start":420,"end":578},{"id":"PF16213","name":"Mon2/Sec7/BIG1-like, dimerisation and cyclophilin-binding domain","start":29,"end":212},{"id":"PF20252","name":"BIG2 C-terminal domain","start":1622,"end":1827}]},"disprot_id":"DP02612","regions_counter":7,"dataset":["NDDs-related proteins"],"UniParc":"UPI0000126939","uniref100":"UniRef100_Q9Y6D6","uniref90":"UniRef90_Q9Y6D6","uniref50":"UniRef50_Q9Y6D6","genes":[{"name":{"value":"ARFGEF1"},"synonyms":[{"value":"ARFGEP1"},{"value":"BIG1"}]}],"alphafold_very_low_content":0.20497566252028124,"disorder_content":0.014602487831260141,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"D"},{"start":50,"end":63,"type":"D"}],"Structural state":[{"start":1,"end":13,"type":"D"},{"start":50,"end":63,"type":"D"}],"Disorder function":[{"start":50,"end":63,"type":"F"}]}},{"acc":"Q8K368","name":"Fanconi anemia group I protein homolog","sequence":"MDLKILSLATDKTTDKLQEFLQTLKDDDLASLLQNQAVKGRAVGTLLRAVLKGSPCSEEDGALRRYKIYSCCIQLVESGDLQQDVASEIIGLLMLEVHHFPGPLLVDLASDFVGAVREDRLVNGKSLELLPIILTALATKKEVLACGKGDLNGEEYKRQLIDTLCSVRWPQRYMIQLTSVFKDVCLTPEEMNLVVAKVLTMFSKLNLQEIPPLVYQLLVLSSKGSRRSVLDGIIAFFRELDKQHREEQSSDELSELITAPADELYHVEGTVILHIVFAIKLDCELGRELLKHLKAGQQGDPSKCLCPFSIALLLSLTRIQRFEEQVFDLLKTSVVKSFKDLQLLQGSKFLQTLVPQRTCVSTMILEVVRNSVHSWDHVTQGLIEFGFILMDSYGPKKILDGKAVEIGTSLSKMTNQHACKLGANILLETFKIHEMIRQEILEQVLNRVVTRTSSPINHFLDLFSDIIMYAPLILQNCSKVTETFDYLTFLPLQTVQGLLKAVQPLLKISMSMRDSLILVLRKAMFASQLDARKSAVAGFLLLLKNFKVLGSLPSSQCTQSIGVTQVRVDVHSRYSAVANETFCLEIIDSLKRSLGQQADIRLMLYDGFYDVLRRNSQLASSIMQTLFSQLKQFYEPEPDLLPPLKLGACVLTQGSQIFLQEPLDHLLSCIQHCLAWYKSRVVPLQQGDEGEEEEEELYSELDDMLESITVRMIKSELEDFELDKSADFSQNTNVGIKNNICACLIMGVCEVLMEYNFSISNFSKSKFEEILSLFTCYKKFSDILSEKAGKGKAKMTSKVSDSLLSLKFVSDLLTALFRDSIQSHEESLSVLRSSGEFMHYAVNVTLQKIQQLIRTGHVSGPDGQNPDKIFQNLCDITRVLLWRYTSIPTSVEESGKKEKGKSISLLCLEGLQKTFSVVLQFYQPKVQQFLQALDVMGTEEEEAGVTVTQRASFQIRQFQRSLLNLLSSEEDDFNSKEALLLIAVLSTLSRLLEPTSPQFVQMLSWTSKICKEYSQEDASFCKSLMNLFFSLHVLYKSPVTLLRDLSQDIHGQLGDIDQDVEIEKTDHFAVVNLRTAAPTVCLLVLSQAEKVLEEVDWLIAKIKGSANQETLSDKVTPEDASSQAVPPTLLIEKAIVMQLGTLVTFFHELVQTALPSGSCVDTLLKGLSKIYSTLTAFVKYYLQVCQSSRGIPNTVEKLVKLSGSHLTPVCYSFISYVQNKSSDAPKCSEKEKAAVSTTMAKVLRETKPIPNLVFAIEQYEKFLIQLSKKSKVNLMQHMKLSTSRDFKIKGSVLDMVLREDEEDENEEGTASAHTQQDREPAKKRRKKCLS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":563,"region_id":"DP02613r001","start":554,"term_id":"IDPO:0000002","statement":[{"text":"In free FANCI, it forms the β3-β4 sheet and part of it is disordered.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21764741","version":2,"reference_html":"Structure of the FANCI-FANCD2 complex: insights into the Fanconi anemia DNA repair pathway. <i> Joo W, Xu G, Persky NS, Smogorzewska A, Rudge DG, Buzovetsky O, Elledge SJ, Pavletich NP. </i> Science, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3S51"},{"db":"PDB","id":"3S4Z"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":563,"region_id":"DP02613r002","start":554,"term_id":"IDPO:0000011","statement":[{"text":"This region undergoes a complete conformational change on FANCD2 binding. In free FANCI, it forms the β3-β4 sheet and part of it is disordered.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21764741","version":2,"reference_html":"Structure of the FANCI-FANCD2 complex: insights into the Fanconi anemia DNA repair pathway. <i> Joo W, Xu G, Persky NS, Smogorzewska A, Rudge DG, Buzovetsky O, Elledge SJ, Pavletich NP. </i> Science, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"3S4W"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":563,"region_id":"DP02613r003","start":554,"term_id":"IDPO:0000045","statement":[{"text":"These three sites map to the 37-amino acid FANCI-specific HD2 insertion at the I-D interface. This region undergoes a complete conformational change on FANCD2 binding. In free FANCI, it forms the β3-β4 sheet and part of it is disordered.","type":"Article"},{"text":"The five FANCI phosphorylation sites cluster at HD2, at and near the I-D interface. Only three of these sites have the ATM/ATR kinase consensus and are also conserved in vertebrates (Ser555, Thr558, Thr564 in mouse FANCI).","type":"Supplementary material"},{"text":"In the ID complex it instead forms two new helices (α26b and α26c) and a 10-residue extension to α27, becoming ordered in its entirety (Fig. 3C). This changes entirely the structural context of the phosphorylation sites. In free FANCI, they map to the disordered segment where they can be readily phosphorylated. In the complex, they end up at the start, middle and immediately after the α26c helix. Their side chains are embedded in hydrogen bond networks that anchor α26c in the FANCI structure and also contact FANCD2 (Fig. 3D and Fig. 2B bottom panel). The structure suggests that their phosphorylation may augment the intramolecular hydrogen bond networks, stabilizing the FANCD2-bound conformation of this region, and may also result in new FANCD2 contacts","type":"Article"},{"text":"Phosphorylation sites map to a disordered region that undergoes a disorder to order transition upon binding of FANCD2","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21764741","version":2,"reference_html":"Structure of the FANCI-FANCD2 complex: insights into the Fanconi anemia DNA repair pathway. <i> Joo W, Xu G, Persky NS, Smogorzewska A, Rudge DG, Buzovetsky O, Elledge SJ, Pavletich NP. </i> Science, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3S4W"}],"term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":563,"region_id":"DP02613r004","start":554,"term_id":"GO:0005515","statement":[{"text":"These three sites map to the 37-amino acid FANCI-specific HD2 insertion at the I-D interface. This region undergoes a complete conformational change on FANCD2 binding. In free FANCI, it forms the β3-β4 sheet and part of it is disordered.","type":"Article"},{"text":"In the ID complex it instead forms two new helices (α26b and α26c) and a 10-residue extension to α27, becoming ordered in its entirety (Fig. 3C). This changes entirely the structural context of the phosphorylation sites. In free FANCI, they map to the disordered segment where they can be readily phosphorylated. In the complex, they end up at the start, middle and immediately after the α26c helix. Their side chains are embedded in hydrogen bond networks that anchor α26c in the FANCI structure and also contact FANCD2 (Fig. 3D and Fig. 2B bottom panel). The structure suggests that their phosphorylation may augment the intramolecular hydrogen bond networks, stabilizing the FANCD2-bound conformation of this region, and may also result in new FANCD2 contacts","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"21764741","version":3,"reference_html":"Structure of the FANCI-FANCD2 complex: insights into the Fanconi anemia DNA repair pathway. <i> Joo W, Xu G, Persky NS, Smogorzewska A, Rudge DG, Buzovetsky O, Elledge SJ, Pavletich NP. </i> Science, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"3S4W"}],"term_name":"protein binding","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":563,"region_id":"DP02613r005","start":554,"term_id":"GO:0098772","statement":[{"text":"Our data implicate the ID complex in recognizing DNA structures that result from the encounter of replication forks with an ICL. The complex may function in stabilizing and protecting these DNA structures, and also in providing specificity for the initial incisions around the ICL by directing the FA-associated nuclease to these sites.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"21764741","version":3,"reference_html":"Structure of the FANCI-FANCD2 complex: insights into the Fanconi anemia DNA repair pathway. <i> Joo W, Xu G, Persky NS, Smogorzewska A, Rudge DG, Buzovetsky O, Elledge SJ, Pavletich NP. </i> Science, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","term_name":"molecular function regulator","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_12","length":1330,"ncbi_taxon_id":10090,"date":"2020-03-04T10:06:14.511Z","organism":"Mus musculus","features":{"gene3D":[],"pfam":[{"id":"PF14674","name":"FANCI solenoid 1 cap","start":1,"end":53},{"id":"PF14675","name":"FANCI solenoid 1","start":64,"end":280},{"id":"PF14676","name":"FANCI solenoid 2","start":378,"end":540},{"id":"PF14677","name":"FANCI solenoid 3","start":803,"end":1028},{"id":"PF14678","name":"FANCI solenoid 4","start":1041,"end":1292},{"id":"PF14679","name":"FANCI helical domain 1","start":284,"end":370},{"id":"PF14680","name":"FANCI helical domain 2","start":554,"end":784}]},"disprot_id":"DP02613","regions_counter":5,"dataset":[],"UniParc":"UPI000002885E","uniref100":"UniRef100_Q8K368","uniref90":"UniRef90_Q8K368","uniref50":"UniRef50_Q9NVI1","genes":[{"name":{"value":"Fanci"}}],"alphafold_very_low_content":0.08721804511278196,"disorder_content":0.007518796992481203,"disprot_consensus":{"full":[{"start":554,"end":563,"type":"T"}],"Structural state":[{"start":554,"end":563,"type":"D"}],"Structural transition":[{"start":554,"end":563,"type":"T"}],"Disorder function":[{"start":554,"end":563,"type":"F"}],"Molecular function":[{"start":554,"end":563,"type":"F"}]}},{"acc":"Q3MIT2","name":"Putative tRNA pseudouridine synthase Pus10","sequence":"MFPLTEENKHVAQLLLNTGTCPRCIFRFCGVDFHAPYKLPYKELLNELQKFLETEKDELILEVMNPPPKKIRLQELEDSIDNLSQNGEGRISVSHVGSTASKNSNLNVCNVCLGILQEFCEKDFIKKVCQKVEASGFEFTSLVFSVSFPPQLSVREHAAWLLVKQEMGKQSLSLGRDDIVQLKEAYKWITHPLFSEELGVPIDGKSLFEVSVVFAHPETVEDCHFLAAICPDCFKPAKNKQSVFTRMAVMKALNKIKEEDFLKQFPCPPNSPKAVCAVLEIECAHGAVFVAGRYNKYSRNLPQTPWIIDGERKLESSVEELISDHLLAVFKAESFNFSSSGREDVDVRTLGNGRPFAIELVNPHRVHFTSQEIKELQQKINNSSNKIQVRDLQLVTREAIGHMKEGEEEKTKTYSALIWTNKAIQKKDIEFLNDIKDLKIDQKTPLRVLHRRPLAVRARVIHFMETQYVDEHHFRLHLKTQAGTYIKEFVHGDFGRTKPNIGSLMNVTADILELDVESVDVDWPPALDD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":243,"region_id":"DP02614r001","start":234,"term_id":"IDPO:0000002","statement":[{"text":"The location of the The model also places the tRNA acceptor stem next to a predominantly basic loop, Phe234–Val243, which is disordered in our structure. loop 234–243 is marked by an arrow","type":"Results"},{"text":"The model also places the tRNA acceptor stem next to a predominantly basic loop, Phe234–Val243, which is disordered in our structure. This loop may become ordered upon RNA binding to provide further stabilizing interactions, clamping the RNA substrate.","type":"Results"},{"text":"The final model has one molecule in the asymmetric unit with residues Glu55-Glu62, Leu76–Leu106 and Phe234–Val243 disordered in our crystals","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17900615","version":2,"reference_html":"Crystal structure of human Pus10, a novel pseudouridine synthase. <i> McCleverty CJ, Hornsby M, Spraggon G, Kreusch A. </i> J Mol Biol, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2V9K"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":55,"end":106,"reference_id":"17900615","reference_source":"pmid","reference_html":"Crystal structure of human Pus10, a novel pseudouridine synthase. <i> McCleverty CJ, Hornsby M, Spraggon G, Kreusch A. </i> J Mol Biol, 2007","date":"2024-05-06T16:33:52.301Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP02614r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"42334","entry_name":null}],"statement":[{"text":"Residues Glu55–Leu106 connecting α3 and α4 are disordered in our structure. A metal bound in between helix α2 and the loop preceding helix α4 is identified as zinc from a fluorescence scan of the crystal.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"2V9K"}]}],"released":"2021_06","length":529,"ncbi_taxon_id":9606,"date":"2020-03-04T16:14:23.903Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF21237","name":"Eukaryotic Pus10, N-terminal","start":109,"end":283},{"id":"PF21238","name":"Pus10, C-terminal","start":289,"end":520}]},"disprot_id":"DP02614","regions_counter":5,"dataset":["RNA-binding proteins"],"UniParc":"UPI000013E1F4","uniref100":"UniRef100_Q3MIT2","uniref90":"UniRef90_Q3MIT2","uniref50":"UniRef50_Q3MIT2","genes":[{"name":{"value":"PUS10","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:26505","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:26505"}}]},"synonyms":[{"value":"CCDC139","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:26505","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:26505"}}]},{"value":"DOBI","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"19712588","url":"http://www.ncbi.nlm.nih.gov/pubmed/19712588","alternativeUrl":"https://europepmc.org/abstract/MED/19712588"}}]}]}],"alphafold_very_low_content":0.09262759924385633,"disorder_content":0.11720226843100189,"disprot_consensus":{"full":[{"start":55,"end":106,"type":"D"},{"start":234,"end":243,"type":"D"}],"Structural state":[{"start":55,"end":106,"type":"D"},{"start":234,"end":243,"type":"D"}]}},{"acc":"O75817","name":"Ribonuclease P protein subunit p20","sequence":"MAENREPRGAVEAELDPVEYTLRKRLPSRLPRRPNDIYVNMKTDFKAQLARCQKLLDGGARGQNACSEIYIHGLGLAINRAINIALQLQAGSFGSLQVAANTSTVELVDELEPETDTREPLTRIRNNSAIHIRVFRVTPK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":28,"region_id":"DP02615r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"The final model of Rpp20/Rpp25 (R/Rfree = 0.20/0.24) was obtained from data to 2.25 Å and, as a result of disordered regions in both the N- and C-termini and between the β3 and β4 antiparallel beta strands, consisted of residues 29 to 59, 63 to 114, and 119 to 140 of Rpp20 and residues 22 to 109 and 125 to 157 of Rpp25","type":"Results"},{"text":"Since the N- and C-terminal regions of both Rpp20 and Rpp25 were disordered in the crystals and our initial datasets were limited in resolution to approximately 3.0 Å, it was difficult to establish the correct amino acid register of the protein models","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29625199","version":2,"reference_html":"Crystal Structure of Human Rpp20/Rpp25 Reveals Quaternary Level Adaptation of the Alba Scaffold as Structural Basis for Single-stranded RNA Binding. <i> Chan CW, Kiesel BR, Mondragón A. </i> J Mol Biol, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6CWX"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":140,"ncbi_taxon_id":9606,"date":"2020-03-04T17:19:37.044Z","organism":"Homo sapiens","features":{"gene3D":[{"start":19,"end":136,"id":"G3DSA:3.30.110.20","name":"Alba-like domain"}],"pfam":[{"id":"PF12328","name":"Rpp20 subunit of nuclear RNase MRP and P","start":33,"end":133}]},"disprot_id":"DP02615","regions_counter":1,"dataset":[],"UniParc":"UPI0000131F3B","uniref100":"UniRef100_O75817","uniref90":"UniRef90_O75817","uniref50":"UniRef50_O75817","genes":[{"name":{"value":"POP7"},"synonyms":[{"value":"RPP20","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"20215441","url":"http://www.ncbi.nlm.nih.gov/pubmed/20215441","alternativeUrl":"https://europepmc.org/abstract/MED/20215441"}}]}]}],"alphafold_very_low_content":0.08571428571428572,"disorder_content":0.2,"disprot_consensus":{"full":[{"start":1,"end":28,"type":"D"}],"Structural state":[{"start":1,"end":28,"type":"D"}]}},{"acc":"Q9BUL9","name":"Ribonuclease P protein subunit p25","sequence":"MENFRKVRSEEAPAGCGAEGGGPGSGPFADLAPGAVHMRVKEGSKIRNLMAFATASMAQPATRAIVFSGCGRATTKTVTCAEILKRRLAGLHQVTRLRYRSVREVWQSLPPGPTQGQTPGEPAASLSVLKNVPGLAILLSKDALDPRQPGYQPPNPHPGPSSPPAAPASKRSLGEPAAGEGSAKRSQPEPGVADEDQTA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"region_id":"DP02616r001","ec_ontology":"ECO","end":21,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"The final model of Rpp20/Rpp25 (R/Rfree = 0.20/0.24) was obtained from data to 2.25 Å and, as a result of disordered regions in both the N- and C-termini and between the β3 and β4 antiparallel beta strands, consisted of residues 29 to 59, 63 to 114, and 119 to 140 of Rpp20 and residues 22 to 109 and 125 to 157 of Rpp25","type":"Results"},{"text":"Since the N- and C-terminal regions of both Rpp20 and Rpp25 were disordered in the crystals and our initial datasets were limited in resolution to approximately 3.0 Å, it was difficult to establish the correct amino acid register of the protein models.","type":"Methods"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29625199","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6CWX"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Crystal Structure of Human Rpp20/Rpp25 Reveals Quaternary Level Adaptation of the Alba Scaffold as Structural Basis for Single-stranded RNA Binding. <i> Chan CW, Kiesel BR, Mondragón A. </i> J Mol Biol, 2018","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":199,"region_id":"DP02616r002","start":158,"term_id":"IDPO:0000002","statement":[{"text":"The final model of Rpp20/Rpp25 (R/Rfree = 0.20/0.24) was obtained from data to 2.25 Å and, as a result of disordered regions in both the N- and C-termini and between the β3 and β4 antiparallel beta strands, consisted of residues 29 to 59, 63 to 114, and 119 to 140 of Rpp20 and residues 22 to 109 and 125 to 157 of Rpp25","type":"Results"},{"text":"Since the N- and C-terminal regions of both Rpp20 and Rpp25 were disordered in the crystals and our initial datasets were limited in resolution to approximately 3.0 Å, it was difficult to establish the correct amino acid register of the protein models.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29625199","version":2,"reference_html":"Crystal Structure of Human Rpp20/Rpp25 Reveals Quaternary Level Adaptation of the Alba Scaffold as Structural Basis for Single-stranded RNA Binding. <i> Chan CW, Kiesel BR, Mondragón A. </i> J Mol Biol, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6CWX"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":199,"ncbi_taxon_id":9606,"date":"2020-03-04T17:21:51.543Z","organism":"Homo sapiens","features":{"gene3D":[{"start":34,"end":143,"id":"G3DSA:3.30.110.20","name":"Alba-like domain"}],"pfam":[{"id":"PF01918","name":"Alba","start":37,"end":100}]},"disprot_id":"DP02616","regions_counter":2,"dataset":[],"UniParc":"UPI0000072730","uniref100":"UniRef100_Q9BUL9","uniref90":"UniRef90_Q9BUL9","uniref50":"UniRef50_Q9BUL9","genes":[{"name":{"value":"RPP25"}}],"alphafold_very_low_content":0.1407035175879397,"disorder_content":0.3165829145728643,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"},{"start":158,"end":199,"type":"D"}],"Structural state":[{"start":1,"end":21,"type":"D"},{"start":158,"end":199,"type":"D"}]}},{"acc":"P21575","name":"Dynamin-1","sequence":"MGNRGMEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNSTTEYAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSDLANSDALKIAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLPGLRNKLQSQLLSIEKEVDEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSGDQIDTYELSGGARINRIFHERFPFELVKMEFDEKELRREISYAIKNIHGIRTGLFTPDLAFEATVKKQVQKLKEPSIKCVDMVVSELTSTIRKCSEKLQQYPRLREEMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQRSNQMNKKKTSGNQDEILVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDYRQLELACETQEEVDSWKASFLRAGVYPERVGDKEKASETEENGSDSFMHSMDPQLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHALKEALSIIGDINTTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRSGQASPSRPESPRPPFDL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":517,"region_id":"DP02617r001","start":497,"term_id":"IDPO:0000002","statement":[{"text":"Linkers connecting the MD to the PH and the PH to the GED are disordered, indicating a flexibly tethered PH","type":"Article"},{"text":"Linker connecting MD to PH","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21927001","version":2,"reference_html":"The crystal structure of dynamin. <i> Ford MG, Jenni S, Nunnari J. </i> Nature, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3ZVR"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":517,"region_id":"DP02617r002","start":497,"term_id":"IDPO:0000033","statement":[{"text":"Linkers connecting the MD to the PH and the PH to the GED are disordered, indicating a flexibly tethered PH","type":"Article"},{"text":"Linker connecting MD to PH","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21927001","version":3,"reference_html":"The crystal structure of dynamin. <i> Ford MG, Jenni S, Nunnari J. </i> Nature, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3ZVR"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":652,"region_id":"DP02617r003","start":629,"term_id":"IDPO:0000002","statement":[{"text":"Linkers connecting the MD to the PH and the PH to the GED are disordered, indicating a flexibly tethered PH","type":"Article"},{"text":"Linker connecting PH to GED","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21927001","version":2,"reference_html":"The crystal structure of dynamin. <i> Ford MG, Jenni S, Nunnari J. </i> Nature, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3ZVR"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":652,"region_id":"DP02617r004","start":629,"term_id":"IDPO:0000033","statement":[{"text":"Linkers connecting the MD to the PH and the PH to the GED are disordered, indicating a flexibly tethered PH","type":"Article"},{"text":"Linker connecting PH to GED","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21927001","version":3,"reference_html":"The crystal structure of dynamin. <i> Ford MG, Jenni S, Nunnari J. </i> Nature, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3ZVR"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","length":864,"ncbi_taxon_id":10116,"date":"2020-03-04T17:55:05.783Z","organism":"Rattus norvegicus","features":{"gene3D":[{"start":496,"end":656,"id":"G3DSA:2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"}],"pfam":[{"id":"PF00169","name":"PH domain","start":520,"end":621},{"id":"PF00350","name":"Dynamin family","start":34,"end":207},{"id":"PF01031","name":"Dynamin central region","start":215,"end":501},{"id":"PF02212","name":"Dynamin GTPase effector domain","start":656,"end":744}]},"disprot_id":"DP02617","regions_counter":4,"dataset":[],"UniParc":"UPI0000129A1F","uniref100":"UniRef100_P21575","uniref90":"UniRef90_P21575","uniref50":"UniRef50_P21575","genes":[{"name":{"value":"Dnm1"},"synonyms":[{"value":"Dnm"}]}],"alphafold_very_low_content":0.16319444444444445,"disorder_content":0.052083333333333336,"disprot_consensus":{"full":[{"start":497,"end":517,"type":"D"},{"start":629,"end":652,"type":"D"}],"Structural state":[{"start":497,"end":517,"type":"D"},{"start":629,"end":652,"type":"D"}],"Disorder function":[{"start":497,"end":517,"type":"F"},{"start":629,"end":652,"type":"F"}]}},{"acc":"Q0WYX8","name":"MAM domain-containing glycosylphosphatidylinositol anchor protein 1","sequence":"MEMICVLFLSLVPAYSRGQGVYAPAQAQIIHAGQACVVKEDNISERVYTIREGDTLVLQCLVTGHPRPQVRWTKTAGSASDKFQETSVLNETLRIEKIQRLQGGRYYCKAENGVGVPAIRSIRVDVQYLDEPVLTVHQTISDVRGSFYQEKTVFLRCTVNSNPPARFIWKRGAETLSHSQDNGVDIYEPLYTQGETKVLKLKNLRPQDYASYTCQVSVRNVCSIPDKSITFQLTNTTAPPALKLSVNETLVVNPGDNVTMQCSLTGGDPQPEVLWSHSPGPLPPNSLVQGGNLTIWRIRVEDSGYYNCTAINNVGNPAKKTVNLLVRSMKNATFQITPDVIKESETIQLGQDLKLSCHVDAVPQEKVVYSWYKNGKPARFSDRLLITRNDPELPPVTCSLEIIDLRFSDYGTYLCVATFQGAPIPDLSVEVNISSETVPPTISVPKGQSTITVREGSRAELQCEVRGKPKPPIIWSRVDKETPMPSGTMTVETYDGKLRLESVSRDMSGTYKCQTARYNGFNIRPREALVQLNVQFPPVVEPAFQDVRQGMGRSVTLRCTMLKGSPMKVATSVWRFNGTLLAQPPAEQQDYSELKVDSVSRETSGSYECSISNDVGVSACLFQVSAKAYSPEFYYDTPNPTLSQKQSKNYSYILQWTQKEPDAVDPILKYRLEVRQLAQRNTIQTFIPVQKMEKGLLLEHILPNLKVPQSYEVRLTPITSFGAGDMAARIIRYMEPINYPSPTDNTCRFEDEKICGFVQDKMDNFDWTRQNALTQNPKRTVNTGPPTDISGTPEGYYMFIEASRPRVTGDKARLISPLYNITAKYYCVSFYYHMYGKHIGSLNLLVRVRNKRAIDTQVWSLSGNRGNMWQQAHVPINPPGPFQIIFEGVRGTSYEGDIAIDDVTLKKGDCPRKPIGPNKAVALPGSGVSAQHGPCLCGPLTFFLYVLLR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Phasianinae","Gallus"],"creator":"fquaglia","regions":[{"region_id":"DP02619r001","ec_ontology":"ECO","end":920,"term_id":"IDPO:0000002","start":736,"version":2,"statement":[{"text":"Seven domains (Ig1-6 to FnIII7) could be unequivocally resolved in the electron density maps; however, the C-terminal MAM8 domain was not visible and most likely highly mobile and accommodated in the solvent channels of the crystal.","type":"Results"},{"text":"The MAM8 domain was not visible in the electron density maps, probably due to a flexible FnIII7-MAM8 linker.","type":"Figure"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28817804","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5OJ2"},{"db":"PDB","id":"5OJ6"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structural Mechanism for Modulation of Synaptic Neuroligin-Neurexin Signaling by MDGA Proteins. <i> Elegheert J, Cvetkovska V, Clayton AJ, Heroven C, Vennekens KM, Smukowski SN, Regan MC, Jia W, Smith AC, Furukawa H, Savas JN, de Wit J, Begbie J, Craig AM, Aricescu AR. </i> Neuron, 2017","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":949,"ncbi_taxon_id":9031,"date":"2020-03-05T14:17:25.404Z","organism":"Gallus gallus","features":{"gene3D":[{"start":636,"end":730,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":636,"end":730,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":636,"end":730,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":636,"end":730,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":636,"end":730,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":636,"end":730,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":636,"end":730,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"}],"pfam":[{"id":"PF00629","name":"MAM domain, meprin/A5/mu","start":747,"end":911},{"id":"PF13927","name":"Immunoglobulin domain","start":46,"end":112},{"id":"PF13927","name":"Immunoglobulin domain","start":132,"end":217},{"id":"PF13927","name":"Immunoglobulin domain","start":239,"end":312},{"id":"PF13927","name":"Immunoglobulin domain","start":342,"end":418},{"id":"PF13927","name":"Immunoglobulin domain","start":439,"end":514},{"id":"PF13927","name":"Immunoglobulin domain","start":537,"end":613}]},"disprot_id":"DP02619","regions_counter":1,"dataset":[],"UniParc":"UPI0000DB4FCC","uniref100":"UniRef100_Q0WYX8","uniref90":"UniRef90_Q0WYX8","uniref50":"UniRef50_Q0WYX8","genes":[{"name":{"value":"MDGA1","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"BAE98269.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAE98269.1"}}]}}],"alphafold_very_low_content":0.08008429926238145,"disorder_content":0.19494204425711276,"disprot_consensus":{"full":[{"start":736,"end":920,"type":"D"}],"Structural state":[{"start":736,"end":920,"type":"D"}]}},{"acc":"Q14194","name":"Dihydropyrimidinase-related protein 1","sequence":"MSYQGKKSIPHITSDRLLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPSQGMTAADDFFQGTRAALVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEVLVQDKGVNSFQVYMAYKDVYQMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVYITKVMSKSAADIIALARKKGPLVFGEPIAASLGTDGTHYWSKNWAKAAAFVTSPPLSPDPTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNINVNKGMGRFIPRKAFPEHLYQRVKIRNKVFGLQGVSRGMYDGPVYEVPATPKYATPAPSAKSSPSKHQPPPIRNLHQSNFSLSGAQIDDNNPRRTGHRIVAPPGGRSNITSLG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":14,"region_id":"DP02620r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"As no electron density was detectable for residues 1–14 and 497–572 they were excluded from the final model.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26249678","version":2,"reference_html":"Structure of human collapsin response mediator protein 1: a possible role of its C-terminal tail. <i> Liu SH, Huang SF, Hsu YL, Pan SH, Chen YJ, Lin YH. </i> Acta Crystallogr F Struct Biol Commun, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4B3Z"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":572,"region_id":"DP02620r002","start":497,"term_id":"IDPO:0000002","statement":[{"text":"As no electron density was detectable for residues 1–14 and 497–572 they were excluded from the final model.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26249678","version":2,"reference_html":"Structure of human collapsin response mediator protein 1: a possible role of its C-terminal tail. <i> Liu SH, Huang SF, Hsu YL, Pan SH, Chen YJ, Lin YH. </i> Acta Crystallogr F Struct Biol Commun, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4B3Z"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":572,"region_id":"DP02620r003","start":497,"term_id":"IDPO:0000045","statement":[{"text":"Analysis of the oligomerization and structural states after the deletion of residues 472–572 by thrombin in vitro revealed discernible differences which, in addition to protein phosphorylation or dephosphorylation events, might be crucial to regulate the function of CRMP and its interaction with other signalling proteins.","type":"Introduction"},{"text":"Collapsin response mediator proteins (CRMPs) are a family of cytosolic phosphoproteins that were originally investigated as signalling mediators of semaphorin 3A","type":"Introduction"},{"text":"Several phosphorylation sites are localized in the C-terminal disordered region of CRMP, i.e. a phosphotyrosine at residue 504, a phosphothreonine at residue 509 and phosphoserines at residues 521, 522, 537, 540 and 542 (PTM-sites position as reported in UniProt).","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26249678","version":2,"reference_html":"Structure of human collapsin response mediator protein 1: a possible role of its C-terminal tail. <i> Liu SH, Huang SF, Hsu YL, Pan SH, Chen YJ, Lin YH. </i> Acta Crystallogr F Struct Biol Commun, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","cross_refs":[{"db":"PDB","id":"4B3Z"}],"term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","disprot_namespace":"Disorder function"}],"released":"2021_06","length":572,"ncbi_taxon_id":9606,"date":"2020-03-05T14:46:17.710Z","organism":"Homo sapiens","features":{"gene3D":[{"start":15,"end":482,"id":"G3DSA:2.30.40.10","name":"Urease, subunit C, domain 1"}],"pfam":[{"id":"PF01979","name":"Amidohydrolase family","start":64,"end":453}]},"disprot_id":"DP02620","regions_counter":3,"dataset":[],"UniParc":"UPI0000047FA2","uniref100":"UniRef100_Q14194","uniref90":"UniRef90_Q14194","uniref50":"UniRef50_Q14194","genes":[{"name":{"value":"CRMP1"},"synonyms":[{"value":"DPYSL1"},{"value":"ULIP3"}]}],"alphafold_very_low_content":0.08741258741258741,"disorder_content":0.15734265734265734,"disprot_consensus":{"full":[{"start":1,"end":14,"type":"D"},{"start":497,"end":572,"type":"D"}],"Structural state":[{"start":1,"end":14,"type":"D"},{"start":497,"end":572,"type":"D"}],"Disorder function":[{"start":497,"end":572,"type":"F"}]}},{"acc":"P97427","name":"Dihydropyrimidinase-related protein 1","sequence":"MSHQGKKSIPHITSDRLLIRGGRIINDDQSFYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPSQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEVLVQDKGVNSFQVYMAYKDLYQMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAIAIAGRINCPVYITKVMSKSAADIIALARKKGPLVFGEPIAASLGTDGTHYWSKNWAKAAAFVTSPPLSPDPTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPDKMKTITAKSHKSTVEYNIFEGMECHGSPLVVISQGKIVFEDGNISVSKGMGRFIPRKPFPEHLYQRVRIRSKVFGLHSVSRGMYDGPVYEVPATPKHAAPAPSAKSSPSKHQPPPIRNLHQSNFSLSGAQIDDNNPRRTGHRIVAPPGGRSNITSLG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":525,"region_id":"DP02621r001","start":491,"term_id":"IDPO:0000002","statement":[{"text":"To characterize the bases of CRMP action, we determined the X‐ray structure of murine CRMP1. Limited proteolysis of CRMP1 (residues 8–572) demonstrated that the C‐terminal segment (approximately 75 amino acids) is proteolytically susceptible (data not shown).","type":"Results"},{"text":"Electron density was visible for residues 15–490, consistent with the proteolysis results described above.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14685275","version":2,"reference_html":"Structural bases for CRMP function in plexin-dependent semaphorin3A signaling. <i> Deo RC, Schmidt EF, Elhabazi A, Togashi H, Burley SK, Strittmatter SM. </i> EMBO J, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1KCX"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":525,"region_id":"DP02621r002","start":491,"term_id":"IDPO:0000045","statement":[{"text":"Collapsin response mediator proteins (CRMPs) are cytosolic phosphoproteins involved in neuronal differentiation and axonal guidance.","type":"Abstract"},{"text":"Phosphorylation sites are localized in the ID region","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14685275","version":2,"reference_html":"Structural bases for CRMP function in plexin-dependent semaphorin3A signaling. <i> Deo RC, Schmidt EF, Elhabazi A, Togashi H, Burley SK, Strittmatter SM. </i> EMBO J, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","cross_refs":[{"db":"PDB","id":"1KCX"}],"term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","disprot_namespace":"Disorder function"}],"released":"2021_06","length":572,"ncbi_taxon_id":10090,"date":"2020-03-05T15:22:56.325Z","organism":"Mus musculus","features":{"gene3D":[{"start":15,"end":482,"id":"G3DSA:2.30.40.10","name":"Urease, subunit C, domain 1"}],"pfam":[{"id":"PF01979","name":"Amidohydrolase family","start":64,"end":453}]},"disprot_id":"DP02621","regions_counter":2,"dataset":[],"UniParc":"UPI000000151F","uniref100":"UniRef100_P97427","uniref90":"UniRef90_Q14194","uniref50":"UniRef50_Q14194","genes":[{"name":{"value":"Crmp1"},"synonyms":[{"value":"Dpysl1"},{"value":"Ulip3"}]}],"alphafold_very_low_content":0.08216783216783216,"disorder_content":0.06118881118881119,"disprot_consensus":{"full":[{"start":491,"end":525,"type":"D"}],"Structural state":[{"start":491,"end":525,"type":"D"}],"Disorder function":[{"start":491,"end":525,"type":"F"}]}},{"acc":"Q15113","name":"Procollagen C-endopeptidase enhancer 1","sequence":"MLPAATASLLGPLLTACALLPFAQGQTPNYTRPVFLCGGDVKGESGYVASEGFPNLYPPNKECIWTITVPEGQTVSLSFRVFDLELHPACRYDALEVFAGSGTSGQRLGRFCGTFRPAPLVAPGNQVTLRMTTDEGTGGRGFLLWYSGRATSGTEHQFCGGRLEKAQGTLTTPNWPESDYPPGISCSWHIIAPPDQVIALTFEKFDLEPDTYCRYDSVSVFNGAVSDDSRRLGKFCGDAVPGSISSEGNELLVQFVSDLSVTADGFSASYKTLPRGTAKEGQGPGPKRGTEPKVKLPPKSQPPEKTEESPSAPDAPTCPKQCRRTGTLQSNFCASSLVVTATVKSMVREPGEGLAVTVSLIGAYKTGGLDLPSPPTGASLKFYVPCKQCPPMKKGVSYLLMGQVEENRGPVLPPESFVVLHRPNQDQILTNLSKRKCPSQPVRAAASQD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":200,"region_id":"DP02622r001","start":189,"term_id":"IDPO:0000002","statement":[{"text":"The CPIII-Long:C1C2 structure is isomorphous with the CPIII-His:C1C2 structure, but nearly half of CUB2 could not be modeled due to disorder (missing residues: 133–144, 164–175, 195–208, 217–227).","type":"Results"},{"text":"Region boundaries of the disordered region within CUB2 according to the canonical sequence in UniProt","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30078642","version":2,"reference_html":"Structural Basis for the Acceleration of Procollagen Processing by Procollagen C-Proteinase Enhancer-1. <i> Pulido D, Sharma U, Vadon-Le Goff S, Hussain SA, Cordes S, Mariano N, Bettler E, Moali C, Aghajari N, Hohenester E, Hulmes DJS. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6FZW"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-10T14:02:49.039Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":233,"region_id":"DP02622r002","start":220,"term_id":"IDPO:0000002","statement":[{"text":"The CPIII-Long:C1C2 structure is isomorphous with the CPIII-His:C1C2 structure, but nearly half of CUB2 could not be modeled due to disorder (missing residues: 133–144, 164–175, 195–208, 217–227).","type":"Results"},{"text":"Region boundaries of the disordered region within CUB2 according to the canonical sequence in UniProt","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30078642","version":2,"reference_html":"Structural Basis for the Acceleration of Procollagen Processing by Procollagen C-Proteinase Enhancer-1. <i> Pulido D, Sharma U, Vadon-Le Goff S, Hussain SA, Cordes S, Mariano N, Bettler E, Moali C, Aghajari N, Hohenester E, Hulmes DJS. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6FZW"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-10T14:02:47.848Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":252,"region_id":"DP02622r003","start":241,"term_id":"IDPO:0000002","statement":[{"text":"The CPIII-Long:C1C2 structure is isomorphous with the CPIII-His:C1C2 structure, but nearly half of CUB2 could not be modeled due to disorder (missing residues: 133–144, 164–175, 195–208, 217–227).","type":"Results"},{"text":"Region boundaries of the disordered region within CUB2 according to the canonical sequence in UniProt","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30078642","version":2,"reference_html":"Structural Basis for the Acceleration of Procollagen Processing by Procollagen C-Proteinase Enhancer-1. <i> Pulido D, Sharma U, Vadon-Le Goff S, Hussain SA, Cordes S, Mariano N, Bettler E, Moali C, Aghajari N, Hohenester E, Hulmes DJS. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6FZW"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-10T14:02:47.093Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":169,"region_id":"DP02622r004","start":151,"term_id":"IDPO:0000002","statement":[{"text":"When compared with the relatively elongated low-resolution structure of full-length PCPE-1 in solution (Bernocco et al., 2003, Kronenberg et al., 2009), the ability of CUB1 and CUB2 to interact in this way in the complex confirms that there is considerable flexibility in the inter-domain linker.","type":"Results"},{"text":"Inter-domain linker connecting CUB1 and CUB2","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30078642","version":2,"reference_html":"Structural Basis for the Acceleration of Procollagen Processing by Procollagen C-Proteinase Enhancer-1. <i> Pulido D, Sharma U, Vadon-Le Goff S, Hussain SA, Cordes S, Mariano N, Bettler E, Moali C, Aghajari N, Hohenester E, Hulmes DJS. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6FZW"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-10T14:02:45.836Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":165,"region_id":"DP02622r005","start":151,"term_id":"IDPO:0000033","statement":[{"text":"When compared with the relatively elongated low-resolution structure of full-length PCPE-1 in solution (Bernocco et al., 2003, Kronenberg et al., 2009), the ability of CUB1 and CUB2 to interact in this way in the complex confirms that there is considerable flexibility in the inter-domain linker.","type":"Results"},{"text":"Inter-domain linker connecting CUB1 and CUB2","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30078642","version":3,"reference_html":"Structural Basis for the Acceleration of Procollagen Processing by Procollagen C-Proteinase Enhancer-1. <i> Pulido D, Sharma U, Vadon-Le Goff S, Hussain SA, Cordes S, Mariano N, Bettler E, Moali C, Aghajari N, Hohenester E, Hulmes DJS. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6FZW"}],"term_name":"flexible linker","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-10T14:02:49.727Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":269,"end":278,"reference_id":"30078642","reference_source":"pmid","reference_html":"Structural Basis for the Acceleration of Procollagen Processing by Procollagen C-Proteinase Enhancer-1. <i> Pulido D, Sharma U, Vadon-Le Goff S, Hussain SA, Cordes S, Mariano N, Bettler E, Moali C, Aghajari N, Hohenester E, Hulmes DJS. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6FZW"}],"region_id":"DP02622r006","statement":[{"text":"The CPIII-Long:C1C2 structure is isomorphous with the CPIII-His:C1C2 structure, but nearly half of CUB2 could not be modeled due to disorder (missing residues: 133–144, 164–175, 195–208, 217–227).","type":"Results"},{"text":"Region boundaries of the disordered region within CUB2 according to the canonical sequence in UniProt.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-10T14:02:44.983Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":449,"ncbi_taxon_id":9606,"date":"2020-03-05T16:05:07.684Z","organism":"Homo sapiens","features":{"gene3D":[{"start":312,"end":442,"id":"G3DSA:2.40.50.120","name":"G3DSA:2.40.50.120"},{"start":151,"end":273,"id":"G3DSA:2.60.120.290","name":"Spermadhesin, CUB domain"},{"start":151,"end":273,"id":"G3DSA:2.60.120.290","name":"Spermadhesin, CUB domain"}],"pfam":[{"id":"PF00431","name":"CUB domain","start":37,"end":146},{"id":"PF00431","name":"CUB domain","start":159,"end":270},{"id":"PF01759","name":"UNC-6/NTR/C345C module","start":331,"end":433}]},"disprot_id":"DP02622","regions_counter":6,"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000161B54","uniref100":"UniRef100_Q15113","uniref90":"UniRef90_Q15113","uniref50":"UniRef50_Q15113","genes":[{"name":{"value":"PCOLCE"},"synonyms":[{"value":"PCPE1"}]}],"alphafold_very_low_content":0.17817371937639198,"disorder_content":0.1492204899777283,"disprot_consensus":{"full":[{"start":151,"end":169,"type":"D"},{"start":189,"end":200,"type":"D"},{"start":220,"end":233,"type":"D"},{"start":241,"end":252,"type":"D"},{"start":269,"end":278,"type":"D"}],"Structural state":[{"start":151,"end":169,"type":"D"},{"start":189,"end":200,"type":"D"},{"start":220,"end":233,"type":"D"},{"start":241,"end":252,"type":"D"},{"start":269,"end":278,"type":"D"}],"Disorder function":[{"start":151,"end":165,"type":"F"}]}},{"acc":"P42003","name":"Protein mothers against dpp","sequence":"MDTDDVESNTSSAMSTLGSLFSFTSPAVKKLLGWKQGDEEEKWAEKAVDSLVKKLKKRKGAIEELERALSCPGQPSKCVTIPRSLDGRLQVSHRKGLPHVIYCRVWRWPDLQSHHELKPLELCQYPFSAKQKEVCINPYHYKRVESPVLPPVLVPRHSEFAPGHSMLQFNHVAEPSMPHNVSYSNSGFNSHSLSTSNTSVGSPSSVNSNPNSPYDSLAGTPPPAYSPSEDGNSNNPNDGGQLLDAQMGDVAQVSYSEPAFWASIAYYELNCRVGEVFHCNNNSVIVDGFTNPSNNSDRCCLGQLSNVNRNSTIENTRRHIGKGVHLYYVTGEVYAECLSDSAIFVQSRNCNYHHGFHPSTVCKIPPGCSLKIFNNQEFAQLLSQSVNNGFEAVYELTKMCTIRMSFVKGWGAEYHRQDVTSTPCWIEIHLHGPLQWLDKVLTQMGSPHNAISSVS","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":256,"region_id":"DP02623r001","start":215,"term_id":"IDPO:0000002","statement":[{"text":"Unfortunately,  the  linker  region  (215—256)  was  flexible  and  disordered  in  the  present  Mad  structure,  indicating  that  there  is  no  observable  contact  between  the  linker  and  MH2  domain.","type":"Results"},{"text":"Flexible linker connecting domains MH1 and MH2","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19557331","version":2,"reference_html":"Crystal structure of the MH2 domain of Drosophila Mad. <i> WANG C, CHEN L, WANG L, WU J. </i> Sci China C Life Sci, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3GMJ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":256,"region_id":"DP02623r002","start":215,"term_id":"IDPO:0000033","statement":[{"text":"Unfortunately,  the  linker  region  (215—256)  was  flexible  and  disordered  in  the  present  Mad  structure,  indicating  that  there  is  no  observable  contact  between  the  linker  and  MH2  domain.","type":"Results"},{"text":"Flexible linker connecting domains MH1 and MH2","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19557331","version":3,"reference_html":"Crystal structure of the MH2 domain of Drosophila Mad. <i> WANG C, CHEN L, WANG L, WU J. </i> Sci China C Life Sci, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3GMJ"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2020_12","length":455,"ncbi_taxon_id":7227,"date":"2020-03-05T16:38:09.993Z","organism":"Drosophila melanogaster","features":{"gene3D":[{"start":257,"end":455,"id":"G3DSA:2.60.200.10","name":"G3DSA:2.60.200.10"},{"start":17,"end":158,"id":"G3DSA:3.90.520.10","name":"SMAD MH1 domain"}],"pfam":[{"id":"PF03165","name":"MH1 domain","start":45,"end":145},{"id":"PF03166","name":"MH2 domain","start":260,"end":431}]},"disprot_id":"DP02623","regions_counter":2,"dataset":[],"UniParc":"UPI000000C4C1","uniref100":"UniRef100_P42003","uniref90":"UniRef90_P42003","uniref50":"UniRef50_P42003","genes":[{"name":{"value":"Mad"},"orfNames":[{"value":"CG12399"}]}],"alphafold_very_low_content":0.2021978021978022,"disorder_content":0.09230769230769231,"disprot_consensus":{"full":[{"start":215,"end":256,"type":"D"}],"Structural state":[{"start":215,"end":256,"type":"D"}],"Disorder function":[{"start":215,"end":256,"type":"F"}]}},{"acc":"P04775","name":"Sodium channel protein type 2 subunit alpha","sequence":"MARSVLVPPGPDSFRFFTRESLAAIEQRIAEEKAKRPKQERKDEDDENGPKPNSDLEAGKSLPFIYGDIPPEMVSEPLEDLDPYYINKKTFIVLNKGKAISRFSATSALYILTPFNPIRKLAIKILVHSLFNVLIMCTILTNCVFMTMSNPPDWTKNVEYTFTGIYTFESLIKILARGFCLEDFTFLRNPWNWLDFTVITFAYVTEFVNLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCLQWPPDNSTFEINITSFFNNSLDWNGTAFNRTVNMFNWDEYIEDKSHFYFLEGQNDALLCGNSSDAGQCPEGYICVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDFWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLINLILAVVAMAYEEQNQATLEEAEQKEAEFQQMLEQLKKQQEEAQAAAAAASAESRDFSGAGGIGVFSESSSVASKLSSKSEKELKNRRKKKKQKEQAGEEEKEDAVRKSASEDSIRKKGFQFSLEGSRLTYEKRFSSPHQSLLSIRGSLFSPRRNSRASLFNFKGRVKDIGSENDFADDEHSTFEDNDSRRDSLFVPHRHGERRPSNVSQASRASRGIPTLPMNGKMHSAVDCNGVVSLVGGPSALTSPVGQLLPEGTTTETEIRKRRSSSYHVSMDLLEDPSRQRAMSMASILTNTMEELEESRQKCPPCWYKFANMCLIWDCCKPWLKVKHVVNLVVMDPFVDLAITICIVLNTLFMAMEHYPMTEQFSSVLSVGNLVFTGIFTAEMFLKIIAMDPYYYFQEGWNIFDGFIVSLSLMELGLANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKISNDCELPRWHMHHFFHSFLIVFRVLCGEWIETMWDCMEVAGQTMCLTVFMMVMVIGNLVVLNLFLALLLSSFSSDNLAATDDDNEMNNLQIAVGRMQKGIDFVKRKIREFIQKAFVRKQKALDEIKPLEDLNNKKDSCISNHTTIEIGKDLNYLKDGNGTTSGIGSSVEKYVVDESDYMSFINNPSLTVTVPIALGESDFENLNTEEFSSESDMEESKEKLNATSSSEGSTVDIGAPAEGEQPEAEPEESLEPEACFTEDCVRKFKCCQISIEEGKGKLWWNLRKTCYKIVEHNWFETFIVFMILLSSGALAFEDIYIEQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGFQMYFTNAWCWLDFLIVDVSLVSLTANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALLGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCINYTTGEMFDVSVVNNYSECQALIESNQTARWKNVKVNFDNVGLGYLSLLQVATFKGWMDIMYAAVDSRNVELQPKYEDNLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPANKFQGMVFDFVTKQVFDISIMILICLNMVTMMVETDDQSQEMTNILYWINLVFIVLFTGECVLKLISLRHYYFTIGWNIFDFVVVILSIVGMFLAELIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKREVGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSGPPDCDPEKDHPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFIEFCKLSDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEERFMASNPSKVSYEPITTTLKRKQEEVSAIVIQRAYRRYLLKQKVKKVSSIYKKDKGKEDEGTPIKEDIITDKLNENSTPEKTDVTPSTTSPPSYDSVTKPEKEKFEKDKSEKEDKGKDIRESKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1486,"region_id":"DP02624r001","start":1474,"term_id":"IDPO:0000002","statement":[{"text":"Although the termini are mobile and flexible with negative hNOE values, residues in the central portion of the inactivation gate peptide have positive hNOEs indicative of stable structure.","type":"Results"},{"text":"The glycine- and proline-rich regions flanking the folded core are unstructured in both peptide constructs, consistent with their proposed role as hinges in the intact channel","type":"Results"},{"text":"The structured subdomain contains residues functionally implicated in mediating and regulating inactivation and is flanked by regions proposed to serve as hinge regions for the inactivation gate.","type":"Results"},{"text":"The NMR solution structure of the isolated inactivation gate reveals a stably folded core comprised of an α-helix capped by an N-terminal turn, supporting a model in which the tightly folded core containing the latch motif pivots on a more flexible hinge region to occlude the pore during inactivation.","type":"Abstract"},{"text":"The stably folded core (1487 - 1506) is flanked by N-terminal (1474-1486) and C-terminal (1507-1526) disordered regions that occlude the pore and serve as hinge regions for the inactivation gate","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9893979","version":2,"reference_html":"Solution structure of the sodium channel inactivation gate. <i> Rohl CA, Boeckman FA, Baker C, Scheuer T, Catterall WA, Klevit RE. </i> Biochemistry, 1999","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"1BYY"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":1486,"region_id":"DP02624r002","start":1474,"term_id":"IDPO:0000030","statement":[{"text":"Although the termini are mobile and flexible with negative hNOE values, residues in the central portion of the inactivation gate peptide have positive hNOEs indicative of stable structure.","type":"Results"},{"text":"The glycine- and proline-rich regions flanking the folded core are unstructured in both peptide constructs, consistent with their proposed role as hinges in the intact channel","type":"Results"},{"text":"The structured subdomain contains residues functionally implicated in mediating and regulating inactivation and is flanked by regions proposed to serve as hinge regions for the inactivation gate.","type":"Results"},{"text":"The NMR solution structure of the isolated inactivation gate reveals a stably folded core comprised of an α-helix capped by an N-terminal turn, supporting a model in which the tightly folded core containing the latch motif pivots on a more flexible hinge region to occlude the pore during inactivation.","type":"Abstract"},{"text":"The stably folded core (1487 - 1506) is flanked by N-terminal (1474-1486) and C-terminal (1507-1526) disordered regions that occlude the pore and serve as hinge regions for the inactivation gate","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9893979","version":3,"reference_html":"Solution structure of the sodium channel inactivation gate. <i> Rohl CA, Boeckman FA, Baker C, Scheuer T, Catterall WA, Klevit RE. </i> Biochemistry, 1999","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"1BYY"}],"term_name":"entropic chain","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":1526,"region_id":"DP02624r003","start":1507,"term_id":"IDPO:0000030","statement":[{"text":"Although the termini are mobile and flexible with negative hNOE values, residues in the central portion of the inactivation gate peptide have positive hNOEs indicative of stable structure.","type":"Results"},{"text":"The glycine- and proline-rich regions flanking the folded core are unstructured in both peptide constructs, consistent with their proposed role as hinges in the intact channel","type":"Results"},{"text":"The structured subdomain contains residues functionally implicated in mediating and regulating inactivation and is flanked by regions proposed to serve as hinge regions for the inactivation gate.","type":"Results"},{"text":"The stably folded core (1487 - 1506) is flanked by N-terminal (1474-1486) and C-terminal (1507-1526) disordered regions that occlude the pore and serve as hinge regions for the inactivation gate","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9893979","version":3,"reference_html":"Solution structure of the sodium channel inactivation gate. <i> Rohl CA, Boeckman FA, Baker C, Scheuer T, Catterall WA, Klevit RE. </i> Biochemistry, 1999","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"1BYY"}],"term_name":"entropic chain","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1526,"region_id":"DP02624r004","start":1507,"term_id":"IDPO:0000002","statement":[{"text":"Although the termini are mobile and flexible with negative hNOE values, residues in the central portion of the inactivation gate peptide have positive hNOEs indicative of stable structure.","type":"Results"},{"text":"The glycine- and proline-rich regions flanking the folded core are unstructured in both peptide constructs, consistent with their proposed role as hinges in the intact channel","type":"Results"},{"text":"The structured subdomain contains residues functionally implicated in mediating and regulating inactivation and is flanked by regions proposed to serve as hinge regions for the inactivation gate.","type":"Results"},{"text":"The stably folded core (1487 - 1506) is flanked by N-terminal (1474-1486) and C-terminal (1507-1526) disordered regions that occlude the pore and serve as hinge regions for the inactivation gate","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9893979","version":2,"reference_html":"Solution structure of the sodium channel inactivation gate. <i> Rohl CA, Boeckman FA, Baker C, Scheuer T, Catterall WA, Klevit RE. </i> Biochemistry, 1999","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"1BYY"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":2005,"ncbi_taxon_id":10116,"date":"2020-03-05T17:25:48.967Z","organism":"Rattus norvegicus","features":{"gene3D":[{"start":1522,"end":1643,"id":"G3DSA:1.20.120.350","name":"Voltage-gated potassium channels. Chain C"},{"start":1522,"end":1643,"id":"G3DSA:1.20.120.350","name":"Voltage-gated potassium channels. Chain C"},{"start":1522,"end":1643,"id":"G3DSA:1.20.120.350","name":"Voltage-gated potassium channels. Chain C"},{"start":1522,"end":1643,"id":"G3DSA:1.20.120.350","name":"Voltage-gated potassium channels. Chain C"}],"pfam":[{"id":"PF00520","name":"Ion transport protein","start":128,"end":434},{"id":"PF00520","name":"Ion transport protein","start":759,"end":990},{"id":"PF00520","name":"Ion transport protein","start":1207,"end":1482},{"id":"PF00520","name":"Ion transport protein","start":1531,"end":1786},{"id":"PF06512","name":"Sodium ion transport-associated","start":997,"end":1203},{"id":"PF11933","name":"Cytoplasmic domain of voltage-gated Na+ ion channel","start":558,"end":709},{"id":"PF24609","name":"SCN5A-like, C-terminal IQ motif","start":1898,"end":1930}]},"disprot_id":"DP02624","regions_counter":4,"dataset":[],"UniParc":"UPI00001279CA","uniref100":"UniRef100_P04775","uniref90":"UniRef90_P04775","uniref50":"UniRef50_P04775","genes":[{"name":{"value":"Scn2a"},"synonyms":[{"value":"Scn2a1"}]}],"alphafold_very_low_content":0.2598503740648379,"disorder_content":0.016458852867830425,"disprot_consensus":{"full":[{"start":1474,"end":1486,"type":"D"},{"start":1507,"end":1526,"type":"D"}],"Structural state":[{"start":1474,"end":1486,"type":"D"},{"start":1507,"end":1526,"type":"D"}],"Disorder function":[{"start":1474,"end":1486,"type":"F"},{"start":1507,"end":1526,"type":"F"}]}},{"acc":"Q920Q2","name":"DNA repair protein REV1","sequence":"MRRGGWRKRTENDGWEKWGGYMAAKVQKLEEQFRTDAANQKDGTASAIFSGVAIYVNGYTDPSAEELRNLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLLSSAPYQLYTKPSAAQKSLNFNPVCKPEDPGPGPSNRAKQLNNRVNHIIKKIETESEVKANGLSSWNEDGVNDDFSFEDLEHTFPGRKQNGVMHPRDTAVIFNGHTHSSNGALKTQDCLVPVGNSVASRLSLDSTQEEKRAEKSNADFRDCTVQHLQHSTRSADALRSPHRTNSLSPSLHSNTKINGAHHSTVQGPSSTKSTSVLTLSKVAPSVPSKPSDCNFISDFYSRSRLHHISTWKCELTEFVNTLQRQSSGIFPGREKLKKVKTGRSSLVVTDTGTMSVLSSPRHQSCVMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGTAPLRPGANPQLEWQYYQNRALRGKAADIPDSSVWENQDSTQTNGIDSVLSKAEIASCSYEARQVGIKNGMFFGYAKQLCPNLQAVPYDFHACREVAQAMYETLASYTHSIEAVSCDEALIDVTDILAETKLSPEEFAAALRIEIKDKTKCAASVGIGSNILLARMATKKAKPDGQYHLQPDEVDDFIRGQLVTNLPGVGRSMESKLASLGIKTCGDLQCLTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEAAGMKGKRLTLKIMVRKPGAPIETAKFGGHGICDNIARTVTLDQATDSAKIIGKATLNMFHTMKLNISDMRGVGIQVNQLVPANSNLSTCSSRPSAQSSLFSGRPHSVRDLFQLQKAKKPTEEEHKEVFLAAVDLEVSSTSRACGLLSPLSAHLAASVSPDTNSGECSRKWNGLHSPVSGQSRLNLSIEVPSPSQIDQSVLEALPLDLREQIEQVCAAQQGEPRGKKKEPVNGCSSGVLPHPVGTVLLQIPEPQEPCNSDSKISVIALPAFSQVDPDVFAALPAELQKELKAAYDQRQRQGEDTTHQQPTSTSVPKNPLLQLKPPAMKDKRNKRKNLIGSPRKSPLKNKLLSSPAKTLPGAYGSPQKLMDGFLQHEGMASERPLEEVSASTPGAQDLSSLLPGQSSCFRPAAPNLAGAVEFSDVKTLLKEWITTISDPMEEDILQVVRYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNVQVVLQQTYGSTLKVT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1152,"region_id":"DP02625r001","start":1135,"term_id":"IDPO:0000002","statement":[{"text":"With the exception of disordered residues at the N terminus, the mRev1 CTD is well structured, with mean pairwise r.m.s.d. of 0.47 and 0.94 Å for the backbone and heavy atoms, respectively","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22700975","version":2,"reference_html":"Multifaceted recognition of vertebrate Rev1 by translesion polymerases ζ and κ. <i> Wojtaszek J, Liu J, D'Souza S, Wang S, Xue Y, Walker GC, Zhou P. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"BMRB","id":"18433"},{"db":"PDB","id":"2LSJ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":1249,"ncbi_taxon_id":10090,"date":"2020-03-05T17:48:19.701Z","organism":"Mus musculus","features":{"gene3D":[{"start":31,"end":133,"id":"G3DSA:3.40.50.10190","name":"BRCT domain"},{"start":706,"end":831,"id":"G3DSA:3.30.1490.100","name":"DNA polymerase, Y-family, little finger domain"},{"start":1142,"end":1240,"id":"G3DSA:1.20.58.1280","name":"G3DSA:1.20.58.1280"},{"start":536,"end":629,"id":"G3DSA:3.30.70.270","name":"G3DSA:3.30.70.270"},{"start":536,"end":629,"id":"G3DSA:3.30.70.270","name":"G3DSA:3.30.70.270"}],"pfam":[{"id":"PF00817","name":"impB/mucB/samB family","start":420,"end":449},{"id":"PF00817","name":"impB/mucB/samB family","start":504,"end":620},{"id":"PF11799","name":"impB/mucB/samB family C-terminal domain","start":707,"end":827},{"id":"PF14377","name":"Ubiquitin binding region","start":933,"end":954},{"id":"PF14377","name":"Ubiquitin binding region","start":1013,"end":1042},{"id":"PF16589","name":"BRCT domain","start":48,"end":129},{"id":"PF16727","name":"DNA repair protein REV1 C-terminal domain","start":1165,"end":1246},{"id":"PF21999","name":"DNA polymerase-iota, thumb domain","start":645,"end":697}]},"disprot_id":"DP02625","regions_counter":1,"dataset":[],"UniParc":"UPI00000227C8","uniref100":"UniRef100_Q920Q2","uniref90":"UniRef90_Q920Q2","uniref50":"UniRef50_Q9UBZ9","genes":[{"name":{"value":"Rev1"},"synonyms":[{"value":"Rev1l"}]}],"alphafold_very_low_content":0.4099279423538831,"disorder_content":0.014411529223378704,"disprot_consensus":{"full":[{"start":1135,"end":1152,"type":"D"}],"Structural state":[{"start":1135,"end":1152,"type":"D"}]}},{"acc":"Q9QUG2","name":"DNA polymerase kappa","sequence":"MDNTKEKDNFKDDLLLRMGLNDNKAGMEGLDKEKINKIIMEATKGSRFYGNELKKEKQVNQRIENMMQQKAQITSQQLRKAQLQVDKFAMELERNRNLNNTIVHVDMDAFYAAVEMRDNPELKDKPIAVGSMSMLATSNYHARRFGVRAAMPGFIAKRLCPQLIIVPPNFDKYRAVSKEVKEILAEYDPNFMAMSLDEAYLNITQHLQERQDWPEDKRRYFIKMGNYLKIDTPRQEANELTEYERSISPLLFEDSPPDLQPQGSPFQLNSEEQNNPQIAQNSVVFGTSAEEVVKEIRFRIEQKTTLTASAGIAPNTMLAKVCSDKNKPNGQYQILPSRSAVMDFIKDLPIRKVSGIGKVTEKMLMALGIVTCTELYQQRALLSLLFSETSWHYFLHIALGLGSTDLARDGERKSMSVERTFSEISKTEEQYSLCQELCAELAHDLQKEGLKGRTVTIKLKNVNFEVKTRASTVPAAISTAEEIFAIAKELLRTEVNVGSPHPLRLRLMGVRMSTFSSEDDRKHQQRSIIGFLQAGNQALSSTGDSLDKTDKTELAKPLEMSHKKSFFDKKRSERISNCQDTSRCKTAGQQALQILEPSQALKKLSESFETSENSNDCQTFICPVCFREQEGVSLEAFNEHVDECLDGPSTSENSKISCYSHASSADIGQKEDVHPSIPLCEKRGHENGEITLVDGVDLTGTEDRSLKAARMDTLENNRSKEECPDIPDKSCPISLENETISTLSRQDSVQPCTDEVVTGRALVCPVCNLEQETSDLTLFNIHVDICLNKGIIQELRNSEGNSVKQPKESSRSTDRLQKASGRTKRPGTKTKSSTLKKTKPRDPRHTLDGFFK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":616,"region_id":"DP02626r001","start":546,"term_id":"IDPO:0000002","statement":[{"text":"The mPol κ RIR(546–616) displays a typical 1H-15N HSQC spectrum of a disordered peptide, with amide resonances showing a narrow chemical shift distribution.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22700975","version":2,"reference_html":"Multifaceted recognition of vertebrate Rev1 by translesion polymerases ζ and κ. <i> Wojtaszek J, Liu J, D'Souza S, Wang S, Xue Y, Walker GC, Zhou P. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"2LSJ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02626r002","ec_ontology":"ECO","end":582,"term_id":"GO:0005515","start":560,"version":3,"statement":[{"text":"The mPol κ RIR(546–616) displays a typical 1H-15N HSQC spectrum of a disordered peptide, with amide resonances showing a narrow chemical shift distribution.","type":"Results"},{"text":"By analyzing mPol κ RIR amide resonances that experience substantial perturbations upon binding to the mRev1 CTD, we have identified a 23-residue RIR peptide of mPol κ(560–582) that not only binds to the mRev1 CTD tightly but also causes identical resonance perturbations for the mRev1 CTD as the longer peptide. This 23-residue peptide was subsequently used to investigate the mRev1 CTD-Pol κ RIR interaction.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q920Q2","partner_end":null}],"term_name":"protein binding","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"22700975","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2LSJ"}],"term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"fquaglia","reference_html":"Multifaceted recognition of vertebrate Rev1 by translesion polymerases ζ and κ. <i> Wojtaszek J, Liu J, D'Souza S, Wang S, Xue Y, Walker GC, Zhou P. </i> J Biol Chem, 2012","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":575,"region_id":"DP02626r003","start":566,"term_id":"IDPO:0000011","statement":[{"text":"The mPol κ RIR(546–616) displays a typical 1H-15N HSQC spectrum of a disordered peptide, with amide resonances showing a narrow chemical shift distribution.","type":"Results"},{"text":"The binding of the mRev1 CTD similarly induces folding of the disordered Pol κ RIR into a three-turn α-helix, starting from Phe566 and ending at Ile575","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22700975","version":2,"reference_html":"Multifaceted recognition of vertebrate Rev1 by translesion polymerases ζ and κ. <i> Wojtaszek J, Liu J, D'Souza S, Wang S, Xue Y, Walker GC, Zhou P. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"2LSJ"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":582,"region_id":"DP02626r004","start":560,"term_id":"GO:0060090","statement":[{"text":"The eukaryotic Y-family polymerase Rev1 is an essential scaffolding protein in translesion synthesis. Its C-terminal domain (CTD), which interacts with translesion polymerase ζ through the Rev7 subunit and with polymerases κ, ι, and η in vertebrates through the Rev1-interacting region (RIR), is absolutely required for function.","type":"Abstract"},{"text":"Our combined structural and biochemical studies reveal two distinct surfaces of the Rev1 CTD that separately mediate the assembly of extension and insertion translesion polymerase complexes and provide a molecular framework for developing novel cancer therapeutics to inhibit translesion synthesis.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"22700975","version":3,"reference_html":"Multifaceted recognition of vertebrate Rev1 by translesion polymerases ζ and κ. <i> Wojtaszek J, Liu J, D'Souza S, Wang S, Xue Y, Walker GC, Zhou P. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"molecular adaptor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","length":852,"ncbi_taxon_id":10090,"date":"2020-03-05T17:56:55.807Z","organism":"Mus musculus","features":{"gene3D":[{"start":411,"end":525,"id":"G3DSA:3.30.1490.100","name":"DNA polymerase, Y-family, little finger domain"},{"start":259,"end":330,"id":"G3DSA:3.30.70.270","name":"G3DSA:3.30.70.270"},{"start":259,"end":330,"id":"G3DSA:3.30.70.270","name":"G3DSA:3.30.70.270"}],"pfam":[{"id":"PF00817","name":"impB/mucB/samB family","start":105,"end":324},{"id":"PF11798","name":"IMS family HHH motif","start":339,"end":369},{"id":"PF11799","name":"impB/mucB/samB family C-terminal domain","start":412,"end":521}]},"disprot_id":"DP02626","regions_counter":4,"dataset":[],"UniParc":"UPI0000021C98","uniref100":"UniRef100_Q9QUG2","uniref90":"UniRef90_Q9QUG2","uniref50":"UniRef50_Q9UBT6","genes":[{"name":{"value":"Polk"},"synonyms":[{"value":"Dinb1"}]}],"alphafold_very_low_content":0.35563380281690143,"disorder_content":0.08333333333333333,"disprot_consensus":{"full":[{"start":546,"end":565,"type":"D"},{"start":566,"end":575,"type":"T"},{"start":576,"end":616,"type":"D"}],"Structural state":[{"start":546,"end":616,"type":"D"}],"Molecular function":[{"start":560,"end":582,"type":"F"}],"Structural transition":[{"start":566,"end":575,"type":"T"}]}},{"acc":"Q8TEP8","name":"Centrosomal protein of 192 kDa","sequence":"MEDFRGIAEESFPSFLTNSLFGNSGILENVTLSSNLGLPVAVSTLARDRSSTDNRYPDIQASYLVEGRFSVPSGSSPGSQSDAEPRERLQLSFQDDDSISRKKSYVESQRLSNALSKQSALQMETAGPEEEPAGATESLQGQDLFNRASPLEQAQDSPIDFHLQSWMNNKEPKIVVLDAGKHFEDKTLKSDLSHTSLLENEKLILPTSLEDSSDDDIDDEMFYDDHLEAYFEQLAIPGMIYEDLEGPEPPEKGFKLPTNGLRQANENGSLNCKFQSENNSSLISLDSHSSETTHKESEESQVICLPGTSNSIGTGDSRRYTDGMLPFSSGTWGTEKEIENLKGIVPDLNSECASKDVLVKTLRAIDVKLNSDNFHDANANRGGFDLTDPVKQGAECPHQNKTVLHMDGCLDTETPTVSIQENVDVASLKPISDSGINFTDAIWSPTCERRTCECHESIEKNKDKTDLPQSVVYQNEEGRWVTDLAYYTSFNSKQNLNVSLSDEMNEDFRSGSEAFDLIAQDEEEFNKEHQFIQEENIDAHNTSVALGDTSWGATINYSLLRKSRSTSDLDKDDASYLRLSLGEFFAQRSEALGCLGGGNNVKRPSFGYFIRSPEKREPIALIRKSDVSRGNLEKEMAHLNHDLYSGDLNEQSQAQLSEGSITLQVEAVESTSQVDENDVTLTADKGKTEDTFFMSNKPQRYKDKLPDSGDSMLRISTIASAIAEASVNTDPSQLAAMIKALSNKTRDKTFQEDEKQKDYSHVRHFLPNDLEKSNGSNALDMEKYLKKTEVSRYESALENFSRASMSDTWDLSLPKEQTTQDIHPVDLSATSVSVRAPEENTAAIVYVENGESENQESFRTINSSNSVTNRENNSAVVDVKTCSIDNKLQDVGNDEKATSISTPSDSYSSVRNPRITSLCLLKDCEEIRDNRENQRQNECVSEISNSEKHVTFENHRIVSPKNSDLKNTSPEHGGRGSEDEQESFRPSTSPLSHSSPSEISGTSSSGCALESFGSAAQQQQPPCEQELSPLVCSPAGVSRLTYVSEPESSYPTTATDDALEDRKSDITSELSTTIIQGSPAALEERAMEKLREKVPFQNRGKGTLSSIIQNNSDTRKATETTSLSSKPEYVKPDFRWSKDPSSKSGNLLETSEVGWTSNPEELDPIRLALLGKSGLSCQVGSATSHPVSCQEPIDEDQRISPKDKSTAGREFSGQVSHQTTSENQCTPIPSSTVHSSVADMQNMPAAVHALLTQPSLSAAPFAQRYLGTLPSTGSTTLPQCHAGNATVCGFSGGLPYPAVAGEPVQNSVAVGICLGSNIGSGWMGTSSLCNPYSNTLNQNLLSTTKPFPVPSVGTNCGIEPWDSGVTSGLGSVRVPEELKLPHACCVGIASQTLLSVLNPTDRWLQVSIGVLSISVNGEKVDLSTYRCLVFKNKAIIRPHATEEIKVLFIPSSPGVFRCTFSVASWPCSTDAETIVQAEALASTVTLTAIAESPVIEVETEKKDVLDFGDLTYGGWKALPLKLINRTHATVPIRLIINANAVAWRCFTFSKESVRAPVEVAPCADVVTRLAGPSVVNHMMPASYDGQDPEFLMIWVLFHSPKKQISSSDILDSAEEFSAKVDIEVDSPNPTPVLRSVSLRARAGIARIHAPRDLQTMHFLAKVASSRKQHLPLKNAGNIEVYLDIKVPEQGSHFSVDPKNLLLKPGEEHEVIVSFTPKDPEACEERILKIFVQPFGPQYEVVLKGEVISSGSKPLSPGPCLDIPSILSNKQFLAWGGVPLGRTQLQKLALRNNSASTTQHLRLLIRGQDQDCFQLQNTFGSEQRLTSNCEIRIHPKEDIFISVLFAPTRLSCMLARLEIKQLGNRSQPGIKFTIPLSGYGGTSNLILEGVKKLSDSYMVTVNGLVPGKESKIVFSVRNTGSRAAFVKAVGFKDSQKKVLLDPKVLRIFPDKFVLKERTQENVTLIYNPSDRGINNKTATELSTVYLFGGDEISRQQYRRALLHKPEMIKQILPEHSVLQNINFVEAFQDELLVTEVYDLPQRPNDVQLFYGSMCKIILSVIGEFRDCISSREFLQPSSKASLESTSDLGASGKHGGNVSLDVLPVKGPQGSPLLSRAARPPLDQLASEEPWTVLPEHLILVAPSPCDMAKTGRFQIVNNSVRLLRFELCWPAHCLTVTPQHGCVAPESKLQILVSPNSSLSTKQSMFPWSGLIYIHCDDGQKKIVKVQIREDLTQVELLTRLTSKPFGILSPVSEPSVSHLVKPMTKPPSTKVEIRNKSITFPTTEPGETSESCLELENHGTTDVKWHLSSLAPPYVKGVDESGDVFRATYAAFRCSPISGLLESHGIQKVSITFLPRGRGDYAQFWDVECHPLKEPHMKHTLRFQLSGQSIEAENEPENACLSTDSLIKIDHLVKPRRQAVSEASARIPEQLDVTARGVYAPEDVYRFRPTSVGESRTLKVNLRNNSFITHSLKFLSPREPFYVKHSKYSLRAQHYINMPVQFKPKSAGKFEALLVIQTDEGKSIAIRLIGEALGKN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":214,"region_id":"DP02627r001","start":201,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The N-termini and C-termini of both Cep192 -58mer (201–214 and 242–258) and Cep152-60mer (1–15 and 47–60) were disordered, suggesting that these regions are highly flexible upon binding to CPB.","type":"Methods"},{"text":"Cep192-58mer corresponds to Cep192 (201–258) fragment","type":"Curator statement"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24997597","version":2,"reference_html":"Molecular basis for unidirectional scaffold switching of human Plk4 in centriole biogenesis. <i> Park SY, Park JE, Kim TS, Kim JH, Kwak MJ, Ku B, Tian L, Murugan RN, Ahn M, Komiya S, Hojo H, Kim NH, Kim BY, Bang JK, Erikson RL, Lee KW, Kim SJ, Oh BH, Yang W, Lee KS. </i> Nat Struct Mol Biol, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4N7Z"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":258,"region_id":"DP02627r002","start":242,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The N-termini and C-termini of both Cep192 -58mer (201–214 and 242–258) and Cep152-60mer (1–15 and 47–60) were disordered, suggesting that these regions are highly flexible upon binding to CPB.","type":"Methods"},{"text":"Cep192-58mer corresponds to Cep192 (201–258) fragment","type":"Curator statement"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24997597","version":2,"reference_html":"Molecular basis for unidirectional scaffold switching of human Plk4 in centriole biogenesis. <i> Park SY, Park JE, Kim TS, Kim JH, Kwak MJ, Ku B, Tian L, Murugan RN, Ahn M, Komiya S, Hojo H, Kim NH, Kim BY, Bang JK, Erikson RL, Lee KW, Kim SJ, Oh BH, Yang W, Lee KS. </i> Nat Struct Mol Biol, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4N7Z"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":258,"region_id":"DP02627r003","start":242,"term_id":"IDPO:0000014","unpublished":true,"statement":[{"text":"The N-termini and C-termini of both Cep192 -58mer (201–214 and 242–258) and Cep152-60mer (1–15 and 47–60) were disordered, suggesting that these regions are highly flexible upon binding to CPB.","type":"Methods"},{"text":"Cep192-58mer corresponds to Cep192 (201–258) fragment","type":"Curator statement"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24997597","version":2,"reference_html":"Molecular basis for unidirectional scaffold switching of human Plk4 in centriole biogenesis. <i> Park SY, Park JE, Kim TS, Kim JH, Kwak MJ, Ku B, Tian L, Murugan RN, Ahn M, Komiya S, Hojo H, Kim NH, Kim BY, Bang JK, Erikson RL, Lee KW, Kim SJ, Oh BH, Yang W, Lee KS. </i> Nat Struct Mol Biol, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4N7Z"}],"term_name":"order to disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":214,"region_id":"DP02627r006","start":201,"term_id":"IDPO:0000014","unpublished":true,"statement":[{"text":"The N-termini and C-termini of both Cep192 -58mer (201–214 and 242–258) and Cep152-60mer (1–15 and 47–60) were disordered, suggesting that these regions are highly flexible upon binding to CPB.","type":"Methods"},{"text":"Cep192-58mer corresponds to Cep192 (201–258) fragment","type":"Curator statement"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24997597","version":2,"reference_html":"Molecular basis for unidirectional scaffold switching of human Plk4 in centriole biogenesis. <i> Park SY, Park JE, Kim TS, Kim JH, Kwak MJ, Ku B, Tian L, Murugan RN, Ahn M, Komiya S, Hojo H, Kim NH, Kim BY, Bang JK, Erikson RL, Lee KW, Kim SJ, Oh BH, Yang W, Lee KS. </i> Nat Struct Mol Biol, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4N7Z"}],"term_name":"order to disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2023_12","length":2537,"ncbi_taxon_id":9606,"date":"2020-03-06T09:27:40.168Z","organism":"Homo sapiens","features":{"gene3D":[{"start":2436,"end":2535,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":2436,"end":2535,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":2436,"end":2535,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"}],"pfam":[{"id":"PF22060","name":"Cep192 domain 1","start":1369,"end":1490},{"id":"PF22064","name":"Cep192 domain 2","start":1492,"end":1645},{"id":"PF22065","name":"Cep192 domain 7","start":2268,"end":2391},{"id":"PF22066","name":"Cep192 domain 8","start":2436,"end":2534},{"id":"PF22067","name":"Cep192 domain 3","start":1648,"end":1746},{"id":"PF22073","name":"Cep192 domain 4","start":1763,"end":1880},{"id":"PF22074","name":"Cep192 domain 5","start":1886,"end":2061},{"id":"PF22076","name":"Cep192 domain 6","start":2128,"end":2229},{"id":"PF25763","name":"CEP192 Aurora A binding region","start":469,"end":533},{"id":"PF25765","name":"CEP192, PLK4 binding region","start":202,"end":243}]},"disprot_id":"DP02627","regions_counter":8,"dataset":[],"UniParc":"UPI000006D5E6","uniref100":"UniRef100_Q8TEP8","uniref90":"UniRef90_Q8TEP8","uniref50":"UniRef50_Q8TEP8","genes":[{"name":{"value":"CEP192","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:25515","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:25515"}}]},"synonyms":[{"value":"KIAA1569"}],"orfNames":[{"value":"PP8407"}]}],"alphafold_very_low_content":0.5916436736302719,"disorder_content":0.012219156484036263,"disprot_consensus":{"full":[{"start":201,"end":214,"type":"T"},{"start":242,"end":258,"type":"T"}],"Structural state":[{"start":201,"end":214,"type":"D"},{"start":242,"end":258,"type":"D"}],"Structural transition":[{"start":201,"end":214,"type":"T"},{"start":242,"end":258,"type":"T"}]}},{"acc":"O94986","name":"Centrosomal protein of 152 kDa","sequence":"MSLDFGSVALPVQNEDEEYDEEDYEREKELQQLLTDLPHDMLDDDLSSPELQYSDCSEDGTDGQPHHPEQLEMSWNEQMLPKSQSVNGYNEIQSLYAGEKCGNVWEENRSKTEDRHPVYHPEEGGDEGGSGYSPPSKCEQTDLYHLPENFRPYTNGQKQEFNNQATNVIKFSDPQWNHFQGPSCQGLEPYNKVTYKPYQSSAQNNGSPAQEITGSDTFEGLQQQFLGANENSAENMQIIQLQVLNKAKERQLENLIEKLNESERQIRYLNHQLVIIKDEKDGLTLSLRESQKLFQNGKEREIQLEAQIKALETQIQALKVNEEQMIKKSRTTEMALESLKQQLVDLHHSESLQRAREQHESIVMGLTKKYEEQVLSLQKNLDATVTALKEQEDICSRLKDHVKQLERNQEAIKLEKTEIINKLTRSLEESQKQCAHLLQSGSVQEVAQLQFQLQQAQKAHAMSANMNKALQEELTELKDEISLYESAAKLGIHPSDSEGELNIELTESYVDLGIKKVNWKKSKVTSIVQEEDPNEELSKDEFILKLKAEVQRLLGSNSMKRHLVSQLQNDLKDCHKKIEDLHQVKKDEKSIEVETKTDTSEKPKNQLWPESSTSDVVRDDILLLKNEIQVLQQQNQELKETEGKLRNTNQDLCNQMRQMVQDFDHDKQEAVDRCERTYQQHHEAMKTQIRESLLAKHALEKQQLFEAYERTHLQLRSELDKLNKEVTAVQECYLEVCREKDNLELTLRKTTEKEQQTQEKIKEKLIQQLEKEWQSKLDQTIKAMKKKTLDCGSQTDQVTTSDVISKKEMAIMIEEQKCTIQQNLEQEKDIAIKGAMKKLEIELELKHCENITKQVEIAVQNAHQRWLGELPELAEYQALVKAEQKKWEEQHEVSVNKRISFAVSEAKEKWKSELENMRKNILPGKELEEKIHSLQKELELKNEEVPVVIRAELAKARSEWNKEKQEEIHRIQEQNEQDYRQFLDDHRNKINEVLAAAKEDFMKQKTELLLQKETELQTCLDQSRREWTMQEAKRIQLEIYQYEEDILTVLGVLLSDTQKEHISDSEDKQLLEIMSTCSSKWMSVQYFEKLKGCIQKAFQDTLPLLVENADPEWKKRNMAELSKDSASQGTGQGDPGPAAGHHAQPLALQATEAEADKKKVLEIKDLCCGHCFQELEKAKQECQDLKGKLEKCCRHLQHLERKHKAVVEKIGEENNKVVEELIEENNDMKNKLEELQTLCKTPPRSLSAGAIENACLPCSGGALEELRGQYIKAVKKIKCDMLRYIQESKERAAEMVKAEVLRERQETARKMRKYYLICLQQILQDDGKEGAEKKIMNAASKLATMAKLLETPISSKSQSKTTQSALPLTSEMLIAVKKSKRNDVNQKIPCCIESKSNSVNTITRTLCEQAPKRRAACNLQRLLENSEHQSIKHVGSKETHLEFQFGDGSCKHLNSLPRNVSPEFVPCEGEGGFGLHKKKDLLSDNGSESLPHSAAYPFLGTLGNKPSPRCTPGPSESGCMHITFRDSNERLGLKVYKCNPLMESENAASEKSQGLDVQEPPVKDGGDLSDCLGWPSSSATLSFDSREASFVHGRPQGTLEIPSESVKSKQFSPSGYLSDTEESNMICQTMKCQRYQTPYLSEETTYLEPGKISVNCGHPSRHKADRLKSDFKKLSSTLPSSVCQQPSRKLIVPLSSQQDSGFDSPFVNLD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":15,"region_id":"DP02628r001","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The N-termini and C-termini of both Cep192 -58mer (201–214 and 242–258) and Cep152-60mer (1–15 and 47–60) were disordered, suggesting that these regions are highly flexible upon binding to CPB.","type":"Methods"},{"text":"Cep152-60mer corresponds to Cep152 (1–60) fragment","type":"Curator statement"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24997597","version":2,"reference_html":"Molecular basis for unidirectional scaffold switching of human Plk4 in centriole biogenesis. <i> Park SY, Park JE, Kim TS, Kim JH, Kwak MJ, Ku B, Tian L, Murugan RN, Ahn M, Komiya S, Hojo H, Kim NH, Kim BY, Bang JK, Erikson RL, Lee KW, Kim SJ, Oh BH, Yang W, Lee KS. </i> Nat Struct Mol Biol, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4N7V"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-14T11:42:23.591Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":60,"region_id":"DP02628r002","start":47,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The N-termini and C-termini of both Cep192 -58mer (201–214 and 242–258) and Cep152-60mer (1–15 and 47–60) were disordered, suggesting that these regions are highly flexible upon binding to CPB.","type":"Methods"},{"text":"Cep152-60mer corresponds to Cep152 (1–60) fragment","type":"Curator statement"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24997597","version":2,"reference_html":"Molecular basis for unidirectional scaffold switching of human Plk4 in centriole biogenesis. <i> Park SY, Park JE, Kim TS, Kim JH, Kwak MJ, Ku B, Tian L, Murugan RN, Ahn M, Komiya S, Hojo H, Kim NH, Kim BY, Bang JK, Erikson RL, Lee KW, Kim SJ, Oh BH, Yang W, Lee KS. </i> Nat Struct Mol Biol, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4N7V"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-14T11:42:22.646Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2023_06","length":1710,"ncbi_taxon_id":9606,"date":"2020-03-06T09:32:16.424Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF25769","name":"CEP152, PLK4 binding region","start":1,"end":58},{"id":"PF25770","name":"CEP152, CEP63 binding coiled coil","start":1263,"end":1313},{"id":"PF30816","name":"CEP152 first coiled-coil region","start":216,"end":774},{"id":"PF30819","name":"CEP152 second coiled-coil region","start":831,"end":1225}]},"disprot_id":"DP02628","regions_counter":9,"dataset":["NDDs-related proteins","Condensates-related proteins"],"UniParc":"UPI000006FDC0","uniref100":"UniRef100_O94986","uniref90":"UniRef90_O94986","uniref50":"UniRef50_O94986","genes":[{"name":{"value":"CEP152","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:29298","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:29298"}}]},"synonyms":[{"value":"KIAA0912"}]}],"alphafold_very_low_content":0.4298245614035088,"disorder_content":0.01695906432748538,"disprot_consensus":{"full":[{"start":1,"end":15,"type":"D"},{"start":47,"end":60,"type":"D"}],"Structural state":[{"start":1,"end":15,"type":"D"},{"start":47,"end":60,"type":"D"}]}},{"acc":"O14958","name":"Calsequestrin-2","sequence":"MKRTHLFIVGIYFLSSCRAEEGLNFPTYDGKDRVVSLSEKNFKQVLKKYDLLCLYYHEPVSSDKVTQKQFQLKEIVLELVAQVLEHKAIGFVMVDAKKEAKLAKKLGFDEEGSLYILKGDRTIEFDGEFAADVLVEFLLDLIEDPVEIISSKLEVQAFERIEDYIKLIGFFKSEDSEYYKAFEEAAEHFQPYIKFFATFDKGVAKKLSLKMNEVDFYEPFMDEPIAIPNKPYTEEELVEFVKEHQRPTLRRLRPEEMFETWEDDLNGIHIVAFAEKSDPDGYEFLEILKQVARDNTDNPDLSILWIDPDDFPLLVAYWEKTFKIDLFRPQIGVVNVTDADSVWMEIPDDDDLPTAEELEDWIEDVLSGKINTEDDDEDDDDDDNSDEEDNDDSDDDDDE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":399,"region_id":"DP02630r001","start":371,"term_id":"IDPO:0000002","statement":[{"text":"In the crystal structure, two N-terminal residues and 29 C-terminal residues starting from N371 are disordered and the corresponding electron densities for these regions are not visible","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17881003","version":2,"reference_html":"Characterization of human cardiac calsequestrin and its deleterious mutants. <i> Kim E, Youn B, Kemper L, Campbell C, Milting H, Varsanyi M, Kang C. </i> J Mol Biol, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2VAF"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-06T12:55:20.039Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":399,"region_id":"DP02630r002","start":371,"term_id":"IDPO:0000045","statement":[{"text":"Therefore, Ser385 and Ser393, which had been confirmed by the mass spectroscopy as the phosphorylation sites, were mutated to aspartic acids to mimic the charge and length of the phosphoserine residue.","type":"Results"},{"text":"However, the MALDI mass spectroscopy data have indicated, without ambiguity, that the phosphorylation sites on hCASQ2 are Ser385 and Ser393, but not Thr372.","type":"Discussion"},{"text":"In addition, the back-to-back interface has the polyanionic C-terminal disordered tail in it, which is composed of residues from 371 to 399 in the case of hCASQ2. Thus, this disordered tail contains both phosphorylation sites, Ser385 and Ser393 (Fig. 7). The twenty-six out of twenty-nine residues in the disordered C-terminus of hCASQ2 are acidic residues.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"protein mass spectrometry evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21416293","version":2,"reference_html":"Phosphorylation of human calsequestrin: implications for calcium regulation. <i> Sanchez EJ, Munske GR, Criswell A, Milting H, Dunker AK, Kang C. </i> Mol Cell Biochem, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007184","term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-21T15:01:47.055Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":399,"region_id":"DP02630r003","start":371,"term_id":"IDPO:0000011","statement":[{"text":"In addition, small angle X-ray scattering determined that in high concentrations of Ca2+, S385D:S393D exists in more compact forms of oligomer than those of unphosphorylated hCASQ2 (Fig. 5a, b). Therefore, the disorder-order transition through phosphorylation-induced helix formation delays Ca2+-dependent aggregation probably through providing more stable back-to-back interface.","type":"Discussion"},{"text":"Therefore, phosphorylation of two serine residues in the highly acidic C-terminal tail increases not only the negative charge in the back-to-back interface, but also establishes a disorder-order transition through the formation of extra-helices and tight interaction with existing positive patches.","type":"Discussion"},{"text":"The authors report the exact phosphorylation sites of hCASQ2 for the first time. It was also showed that phosphoserine mimicking double mutant of hCASQ2 has a substantial increase in its Ca2+ binding capacity, solubility and α-helix content, probably due to the extra negative charge and order-disorder transition in the back-to-back interface.","type":"Conclusion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21416293","version":2,"reference_html":"Phosphorylation of human calsequestrin: implications for calcium regulation. <i> Sanchez EJ, Munske GR, Criswell A, Milting H, Dunker AK, Kang C. </i> Mol Cell Biochem, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-06T13:12:55.583Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":399,"region_id":"DP02630r004","start":371,"term_id":"GO:0140314","statement":[{"text":"In the crystal structures of both CASQ1 and CASQ2 from various species [20, 39, 46], two distinct dimerization contacts are observed: front-to-front and back-to-back, which involve the N-terminal and C-terminal residues, respectively. Those interfaces form the basis of dimer, tetramer, and possibly further polymers of CASQ. Not only do the observed polymers have the morphology inferred for the physiologically relevant aggregation [23], but these two interfaces also provide the basis for a mechanism to couple Ca2+-binding and polymerization","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_12","ec_name":"enzymatic activity assay evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"21416293","version":4,"reference_html":"Phosphorylation of human calsequestrin: implications for calcium regulation. <i> Sanchez EJ, Munske GR, Criswell A, Milting H, Dunker AK, Kang C. </i> Mol Cell Biochem, 2011","date":"2022-12-06T10:42:09.275Z","reference_source":"pmid","ec_id":"ECO:0005801","term_name":"calcium ion sequestering activity","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a calcium ion to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-20T20:41:51.976Z"}},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"ChEBI","id":"29108","partner_end":null}],"ec_ontology":"ECO","end":399,"region_id":"DP02630r006","start":371,"term_id":"GO:0005509","statement":[{"text":"In the crystal structures of both CASQ1 and CASQ2 from various species [20, 39, 46], two distinct dimerization contacts are observed: front-to-front and back-to-back, which involve the N-terminal and C-terminal residues, respectively. Those interfaces form the basis of dimer, tetramer, and possibly further polymers of CASQ. Not only do the observed polymers have the morphology inferred for the physiologically relevant aggregation [23], but these two interfaces also provide the basis for a mechanism to couple Ca2+-binding and polymerization","type":"Discussion"},{"text":"In addition, the experimental approach with equilibrium dialysis and atomic absorption spectroscopy shows that the hCASQ2 double mutant shows a similar Ca2+ binding capacity up to a Ca2+-concentration of ~6–7 mM (Fig. 6). Above this Ca2+ concentration, S385D:S393D displays significantly increased Ca2+-binding capacity (Fig. 6). Coincidently, the bifurcation point of Ca2+ concentration between double mutant and others in turbidity assay (Fig. 4) is similar to that of Ca2+-binding capacity curve","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"enzymatic activity assay evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"21416293","version":4,"reference_html":"Phosphorylation of human calsequestrin: implications for calcium regulation. <i> Sanchez EJ, Munske GR, Criswell A, Milting H, Dunker AK, Kang C. </i> Mol Cell Biochem, 2011","date":"2026-01-07T15:30:57.190Z","reference_source":"pmid","ec_id":"ECO:0005801","term_name":"calcium ion binding","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-01-07T15:31:07.390Z"}}],"released":"2021_06","length":399,"ncbi_taxon_id":9606,"date":"2020-03-06T18:17:07.175Z","organism":"Homo sapiens","features":{"gene3D":[{"start":248,"end":387,"id":"G3DSA:3.40.30.10","name":"Glutaredoxin"},{"start":248,"end":387,"id":"G3DSA:3.40.30.10","name":"Glutaredoxin"},{"start":248,"end":387,"id":"G3DSA:3.40.30.10","name":"Glutaredoxin"}],"pfam":[{"id":"PF01216","name":"Calsequestrin","start":2,"end":381}]},"disprot_id":"DP02630","regions_counter":6,"dataset":[],"UniParc":"UPI0000161BE0","uniref100":"UniRef100_O14958","uniref90":"UniRef90_O14958","uniref50":"UniRef50_O14958","genes":[{"name":{"value":"CASQ2"}}],"alphafold_very_low_content":0.08270676691729323,"disorder_content":0.07268170426065163,"disprot_consensus":{"full":[{"start":371,"end":399,"type":"T"}],"Structural state":[{"start":371,"end":399,"type":"D"}],"Disorder function":[{"start":371,"end":399,"type":"F"}],"Structural transition":[{"start":371,"end":399,"type":"T"}],"Molecular function":[{"start":371,"end":399,"type":"F"}]}},{"acc":"Q39026","name":"Mitogen-activated protein kinase 6","sequence":"MDGGSGQPAADTEMTEAPGGFPAAAPSPQMPGIENIPATLSHGGRFIQYNIFGNIFEVTAKYKPPIMPIGKGAYGIVCSAMNSETNESVAIKKIANAFDNKIDAKRTLREIKLLRHMDHENIVAIRDIIPPPLRNAFNDVYIAYELMDTDLHQIIRSNQALSEEHCQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARVTSESDFMTEYVVTRWYRAPELLLNSSDYTAAIDVWSVGCIFMELMDRKPLFPGRDHVHQLRLLMELIGTPSEEELEFLNENAKRYIRQLPPYPRQSITDKFPTVHPLAIDLIEKMLTFDPRRRITVLDALAHPYLNSLHDISDEPECTIPFNFDFENHALSEEQMKELIYREALAFNPEYQQ","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":224,"region_id":"DP02631r001","start":215,"term_id":"IDPO:0000002","statement":[{"text":"The MPK6 crystals contain two protein chains in the asymmetric unit. Amino acid residues 70–75 (part of the glycine-rich loop), 213–214 (part of the phosphorylation lip), and 366–374 (part of the L16 loop) in chain A and amino acid residues 215–224 (phosphorylation lip) and 285–287 (part of the MAPK insert) in chain B were not resolved in the electron density maps.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27160427","version":2,"reference_html":"Analysis of crystal structure of Arabidopsis MPK6 and generation of its mutants with higher activity. <i> Wang B, Qin X, Wu J, Deng H, Li Y, Yang H, Chen Z, Liu G, Ren D. </i> Sci Rep, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5CI6"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":224,"region_id":"DP02631r002","start":215,"term_id":"IDPO:0000045","statement":[{"text":"The MPK6 crystals contain two protein chains in the asymmetric unit. Amino acid residues 70–75 (part of the glycine-rich loop), 213–214 (part of the phosphorylation lip), and 366–374 (part of the L16 loop) in chain A and amino acid residues 215–224 (phosphorylation lip) and 285–287 (part of the MAPK insert) in chain B were not resolved in the electron density maps.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27160427","version":2,"reference_html":"Analysis of crystal structure of Arabidopsis MPK6 and generation of its mutants with higher activity. <i> Wang B, Qin X, Wu J, Deng H, Li Y, Yang H, Chen Z, Liu G, Ren D. </i> Sci Rep, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5CI6"}],"term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","length":395,"ncbi_taxon_id":3702,"date":"2020-03-09T09:01:32.844Z","organism":"Arabidopsis thaliana","features":{"gene3D":[],"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":68,"end":348}]},"disprot_id":"DP02631","regions_counter":2,"dataset":["Stress response proteins"],"UniParc":"UPI00000014BF","uniref100":"UniRef100_Q39026","uniref90":"UniRef90_Q39026","uniref50":"UniRef50_Q39026","genes":[{"name":{"value":"MPK6","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8282107","url":"http://www.ncbi.nlm.nih.gov/pubmed/8282107","alternativeUrl":"https://europepmc.org/abstract/MED/8282107"}}]},"orfNames":[{"value":"F18O19.10","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAB64027.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAB64027.1"}}]}],"olnNames":[{"value":"At2g43790","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT2G43790","url":""}}]}]}],"alphafold_very_low_content":0.07088607594936709,"disorder_content":0.02531645569620253,"disprot_consensus":{"full":[{"start":215,"end":224,"type":"D"}],"Structural state":[{"start":215,"end":224,"type":"D"}],"Disorder function":[{"start":215,"end":224,"type":"F"}]}},{"acc":"P31321","name":"cAMP-dependent protein kinase type I-beta regulatory subunit","sequence":"MASPPACPSEEDESLKGCELYVQLHGIQQVLKDCIVHLCISKPERPMKFLREHFEKLEKEENRQILARQKSNSQSDSHDEEVSPTPPNPVVKARRRRGGVSAEVYTEEDAVSYVRKVIPKDYKTMTALAKAISKNVLFAHLDDNERSDIFDAMFPVTHIAGETVIQQGNEGDNFYVVDQGEVDVYVNGEWVTNISEGGSFGELALIYGTPRAATVKAKTDLKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLQRRSPNEEYVEVGRLGPSDYFGEIALLLNRPRAATVVARGPLKCVKLDRPRFERVLGPCSEILKRNIQRYNSFISLTV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":81,"region_id":"DP02632r001","start":59,"term_id":"IDPO:0000002","statement":[{"text":"Although 21 residues of the linker region between the D/D domain and the CNB-A domain of each R-subunit (residues 59–81) are still missing in our structure, several features are clear.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22797896","version":2,"reference_html":"Localization and quaternary structure of the PKA RIβ holoenzyme. <i> Ilouz R, Bubis J, Wu J, Yim YY, Deal MS, Kornev AP, Ma Y, Blumenthal DK, Taylor SS. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4DIN"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T14:36:18.728Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":81,"region_id":"DP02632r002","start":59,"term_id":"IDPO:0000033","statement":[{"text":"Although 21 residues of the linker region between the D/D domain and the CNB-A domain of each R-subunit (residues 59–81) are still missing in our structure, several features are clear.","type":"Results"},{"text":"The unusual feature of our structure was that we were capable to visualize both the D/D domain and the CNB domains simultaneously. Structures of these domains for different R-subunits were solved previously only separately. The extended flexible linker between these domains prevented crystallization of the full length R-subunits. ","type":"Results"},{"text":"The entire linker segment that joins the D/D domain to CNB-A is classified as an intrinsic disordered region, and embedded within this segment is the inhibitor site (IS) that docks to the active site cleft of the C-subunit in the holoenzyme. ","type":"Results"}],"curator_id":"vnugnes","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"22797896","version":4,"reference_html":"Localization and quaternary structure of the PKA RIβ holoenzyme. <i> Ilouz R, Bubis J, Wu J, Yim YY, Deal MS, Kornev AP, Ma Y, Blumenthal DK, Taylor SS. </i> Proc Natl Acad Sci U S A, 2012","date":"2023-06-13T14:42:37.293Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4DIN"}],"term_name":"flexible linker","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Disorder function","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P05132 "},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5957"}]},{"start":1,"end":13,"reference_id":"22797896","reference_source":"pmid","reference_html":"Localization and quaternary structure of the PKA RIβ holoenzyme. <i> Ilouz R, Bubis J, Wu J, Yim YY, Deal MS, Kornev AP, Ma Y, Blumenthal DK, Taylor SS. </i> Proc Natl Acad Sci U S A, 2012","date":"2023-06-13T14:38:56.854Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4DIN"}],"region_id":"DP02632r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5957"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P05132"}],"statement":[{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"released":"2020_12","length":381,"ncbi_taxon_id":9606,"date":"2020-03-09T10:42:59.563Z","organism":"Homo sapiens","features":{"gene3D":[{"start":238,"end":381,"id":"G3DSA:2.60.120.10","name":"Jelly Rolls"},{"start":238,"end":381,"id":"G3DSA:2.60.120.10","name":"Jelly Rolls"}],"pfam":[{"id":"PF00027","name":"Cyclic nucleotide-binding domain","start":160,"end":236},{"id":"PF00027","name":"Cyclic nucleotide-binding domain","start":274,"end":359},{"id":"PF02197","name":"Regulatory subunit of type II PKA R-subunit","start":25,"end":61}]},"disprot_id":"DP02632","regions_counter":4,"dataset":["NDDs-related proteins"],"UniParc":"UPI00001724F4","uniref100":"UniRef100_P31321","uniref90":"UniRef90_P31321","uniref50":"UniRef50_P31321","genes":[{"name":{"value":"PRKAR1B"}}],"alphafold_very_low_content":0.06299212598425197,"disorder_content":0.09448818897637795,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"D"},{"start":59,"end":81,"type":"D"}],"Structural state":[{"start":1,"end":13,"type":"D"},{"start":59,"end":81,"type":"D"}],"Disorder function":[{"start":59,"end":81,"type":"F"}]}},{"acc":"P22605","name":"Retinoic acid receptor beta","sequence":"MSTSSHACPVPAVRGHMTHYPAAPYPLLFPPVIRGLSLPPLHGLHGHPPPSGCSTPSPASVGQACQRTTGGSQFAASTKWTPSLNAAIETQSTSSEELVPSPPSPLPPPRVYKPCFVCQDKSSGYHYGVSACEGCKGFFRRSIQKNMIYTCHRDKNCVINKVTRNRCQYCRLQKCFEVGMSKESVRNDRNKKKKEPSKQECTESYEMTAELDDLTEKIRKAHQETFPSLCQLGKYTTNSSADHRVRLDLGLWDKFSELATKCIIKIVEFAKRLPGFTGLTIADQITLLKAACLDILILRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFTFANQLLPLEMDDTETGLLSAICLICGDRQDLEEPTKVDKLQEPLLEALKIYIRKRRPSKPHMFPKILMKITDLRSISAKGAERVITLKMEIPGSMPPLIQEMLENSEGHEPLTPSSSGNIAEHSPSVSPSSVENSGVSQSPLLQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":481,"region_id":"DP02633r001","start":454,"term_id":"IDPO:0000002","statement":[{"text":"Electron density was observed for only 10 residues (out of 40) of the RARβ C-terminal F region.","type":"Results"},{"text":"Like other members of the nuclear receptor superfamily, retinoid receptors are modular and include an N-terminal A/B activation domain, a central DNA-binding domain (region C), a linker region D, a ligand-binding domain (region E), and a C-terminal region F of unknown structure and function.","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15528208","version":2,"reference_html":"Characterization of the interaction between retinoic acid receptor/retinoid X receptor (RAR/RXR) heterodimers and transcriptional coactivators through structural and fluorescence anisotropy studies. <i> Pogenberg V, Guichou JF, Vivat-Hannah V, Kammerer S, Pérez E, Germain P, de Lera AR, Gronemeyer H, Royer CA, Bourguet W. </i> J Biol Chem, 2005","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1XDK"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":209,"region_id":"DP02633r002","start":180,"term_id":"IDPO:0000002","statement":[{"text":"Electron density was observed for only 10 residues (out of 40) of the RARβ C-terminal F region.","type":"Results"},{"text":"Like other members of the nuclear receptor superfamily, retinoid receptors are modular and include an N-terminal A/B activation domain, a central DNA-binding domain (region C), a linker region D, a ligand-binding domain (region E), and a C-terminal region F of unknown structure and function.","type":"Introduction"},{"text":"Helix H2, the connection between H2 and H3 in RXRα, the D-region and the last 30 residues of the F-region in RARβ, could not be modeled due to poor electron density in these regions.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15528208","version":2,"reference_html":"Characterization of the interaction between retinoic acid receptor/retinoid X receptor (RAR/RXR) heterodimers and transcriptional coactivators through structural and fluorescence anisotropy studies. <i> Pogenberg V, Guichou JF, Vivat-Hannah V, Kammerer S, Pérez E, Germain P, de Lera AR, Gronemeyer H, Royer CA, Bourguet W. </i> J Biol Chem, 2005","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1XDK"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":209,"region_id":"DP02633r003","start":180,"term_id":"IDPO:0000033","statement":[{"text":"Electron density was observed for only 10 residues (out of 40) of the RARβ C-terminal F region.","type":"Results"},{"text":"Like other members of the nuclear receptor superfamily, retinoid receptors are modular and include an N-terminal A/B activation domain, a central DNA-binding domain (region C), a linker region D, a ligand-binding domain (region E), and a C-terminal region F of unknown structure and function.","type":"Introduction"},{"text":"Helix H2, the connection between H2 and H3 in RXRα, the D-region and the last 30 residues of the F-region in RARβ, could not be modeled due to poor electron density in these regions.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15528208","version":3,"reference_html":"Characterization of the interaction between retinoic acid receptor/retinoid X receptor (RAR/RXR) heterodimers and transcriptional coactivators through structural and fluorescence anisotropy studies. <i> Pogenberg V, Guichou JF, Vivat-Hannah V, Kammerer S, Pérez E, Germain P, de Lera AR, Gronemeyer H, Royer CA, Bourguet W. </i> J Biol Chem, 2005","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1XDK"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","length":482,"ncbi_taxon_id":10090,"date":"2020-03-09T11:15:36.470Z","organism":"Mus musculus","features":{"gene3D":[{"start":109,"end":209,"id":"G3DSA:3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A"},{"start":164,"end":448,"id":"G3DSA:1.10.565.10","name":"Retinoid X Receptor"}],"pfam":[{"id":"PF00104","name":"Ligand-binding domain of nuclear hormone receptor","start":254,"end":426},{"id":"PF00105","name":"Double treble clef zinc finger, C4 type","start":114,"end":182}]},"disprot_id":"DP02633","regions_counter":3,"dataset":[],"UniParc":"UPI0000021521","uniref100":"UniRef100_P22605","uniref90":"UniRef90_P10826","uniref50":"UniRef50_P10826","genes":[{"name":{"value":"Rarb"},"synonyms":[{"value":"Nr1b2"}]}],"alphafold_very_low_content":0.2946058091286307,"disorder_content":0.12033195020746888,"disprot_consensus":{"full":[{"start":180,"end":209,"type":"D"},{"start":454,"end":481,"type":"D"}],"Structural state":[{"start":180,"end":209,"type":"D"},{"start":454,"end":481,"type":"D"}],"Disorder function":[{"start":180,"end":209,"type":"F"}]}},{"acc":"Q9UBV7","name":"Beta-1,4-galactosyltransferase 7","sequence":"MFPSRRKAAQLPWEDGRSGLLSGGLPRKCSVFHLFVACLSLGFFSLLWLQLSCSGDVARAVRGQGQETSGPPRACPPEPPPEHWEEDASWGPHRLAVLVPFRERFEELLVFVPHMRRFLSRKKIRHHIYVLNQVDHFRFNRAALINVGFLESSNSTDYIAMHDVDLLPLNEELDYGFPEAGPFHVASPELHPLYHYKTYVGGILLLSKQHYRLCNGMSNRFWGWGREDDEFYRRIKGAGLQLFRPSGITTGYKTFRHLHDPAWRKRDQKRIAAQKQEQFKVDREGGLNTVKYHVASRTALSVGGAPCTVLNIMLDCDKTATPWCTFS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":285,"region_id":"DP02634r001","start":260,"term_id":"IDPO:0000002","statement":[{"text":"In B, the long loop region, residues 260–285, invisible in the open conformation, is highlighted in red.","type":"Figure"},{"text":"In the open conformation crystal structure (Fig. 1A), no electron density was observed for a region encompassing residues 260–278, and only weak backbone electron density could be traced for residues 278–284. ","type":"Results"},{"text":"In the crystal structures of human β4GalT7, the missing and weak electron\ndensity from residues 260–284, together with the presence of the Trp224 side chain rotamers in the open conformation (data not shown), suggest structural flexibility in this region.","type":"Discussion"},{"text":"In the open conformation (A), the electron density was visible up to His259 , and the clear electron density appeared again at Gly285 (blue sphere). ","type":"Figure"}],"curator_id":"maspromonte","released":"2022_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Maria Cristina Aspromonte","reference_id":"24052259","version":3,"reference_html":"Crystal structures of β-1,4-galactosyltransferase 7 enzyme reveal conformational changes and substrate binding. <i> Tsutsui Y, Ramakrishnan B, Qasba PK. </i> J Biol Chem, 2013","date":"2022-10-17T16:13:27.837Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4IRP"}],"term_name":"disorder","curator_orcid":"0000-0002-4937-6952","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17659","statements":[{"type":"Methods","text":"The tetragonal crystal was soaked in the same pH 6.5 reservoir solution containing 15% 2-methy-2,4-pentanediol (MPD) at 18 °C for 20 h followed by a brief soak in 100 mM Tris (pH 8.0), 750 mM sodium acetate, 15% MPD, 5 mM MnCl2, and 5 mM UDP-Gal at room temperature."}],"entry_name":"UDP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29035","statements":[{"type":"Methods","text":"One manganese ion and one UDP molecule are located in the catalytic pocket of each protein molecule."}],"entry_name":"manganese(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30089","statements":[{"type":"Methods","text":"The purified β4GalT7Δ81 (15 mg/ml) was readily crystallized using the hanging drop vapor diffusion method with 100 mM imidazole (pH 6.5) and 750 mM sodium acetate as a reservoir solution in the presence of 5 mM MnCl2 at 18 °C. The addition of MnCl2 was necessary for growing a larger, 0.1– 0.2 mm crystal."}],"entry_name":"acetate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"50059","statements":[{"type":"Methods","text":"The purified β4GalT7Δ81 (15 mg/ml) was readily crystallized using the hanging drop vapor diffusion method with 100 mM imidazole (pH 6.5) and 750 mM sodium acetate as a reservoir solution in the presence of 5 mM MnCl2 at 18 °C. The addition of MnCl2 was necessary for growing a larger, 0.1– 0.2 mm crystal."}],"entry_name":"imidazolium cation"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T13:12:38.409Z"}},{"start":260,"end":285,"reference_id":"24052259","reference_source":"pmid","reference_html":"Crystal structures of β-1,4-galactosyltransferase 7 enzyme reveal conformational changes and substrate binding. <i> Tsutsui Y, Ramakrishnan B, Qasba PK. </i> J Biol Chem, 2013","date":"2022-10-21T08:55:29.336Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"4IRP"},{"db":"PDB","id":"4IRQ"}],"region_id":"DP02634r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17659","statements":[{"type":"Methods","text":"The tetragonal crystal was soaked in the same pH 6.5 reservoir solution containing 15% 2-methy-2,4-pentanediol (MPD) at 18 °C for 20 h followed by a brief soak in 100 mM Tris (pH 8.0), 750 mM sodium acetate, 15% MPD, 5 mM MnCl2, and 5 mM UDP-Gal at room temperature."}],"entry_name":"UDP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29035","statements":[{"type":"Methods","text":"One manganese ion and one UDP molecule are located in the catalytic pocket of each protein molecule."}],"entry_name":"manganese(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30089","statements":[{"type":"Methods","text":"The purified β4GalT7Δ81 (15 mg/ml) was readily crystallized using the hanging drop vapor diffusion method with 100 mM imidazole (pH 6.5) and 750 mM sodium acetate as a reservoir solution in the presence of 5 mM MnCl2 at 18 °C. The addition of MnCl2 was necessary for growing a larger, 0.1–0.2 mm crystal."}],"entry_name":"acetate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"50059","statements":[{"type":"Methods","text":"The purified β4GalT7Δ81 (15 mg/ml) was readily crystallized using the hanging drop vapor diffusion method with 100 mM imidazole (pH 6.5) and 750 mM sodium acetate as a reservoir solution in the presence of 5 mM MnCl2 at 18 °C. The addition of MnCl2 was necessary for growing a larger, 0.1–0.2 mm crystal."}],"entry_name":"imidazolium cation"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46097","statements":[{"type":"Methods","text":"The tetragonal crystal was soaked in the same pH 6.5 reservoir solution containing 15% 2-methy-2,4-pentanediol (MPD) at 18 °C for 20 h followed by a brief soak in 100 mM Tris (pH 8.0), 750 mM sodium acetate, 15% MPD, 5 mM MnCl2, and 5 mM UDP-Gal at room temperature."}],"entry_name":"Htris"}],"statement":[{"text":"In the open conformation crystal structure (Fig. 1A), no electron density was observed for a region encompassing residues 260–278, and only weak backbone electron density could be traced for residues 278–284. In contrast, the same region in the closed conformation had clear electron density corresponding to a long loop, residues 260–285 (Fig. 1B). The appearance of the long loop coincides with the change in the orientation of the Trp224 side chain, from pointing away to pointing toward the binding pocket, forming a hydrogen bond with the β-phosphate oxygen atom of the bound UDP (Fig. 1B).","type":"Results"},{"text":"In the open conformation (A), the electron density was visible up to His259 , and the clear electron density appeared again at Gly285 (blue sphere). The His257 -X-His259 motif, Trp224 , and the N and C termini are indicated. A disulfide bond is shown in a ball-and-stick format, with the yellow spheres indicating sulfur atoms. In B, the long loop region, residues 260 –285, invisible in the open conformation, is highlighted in red.","type":"Figure"}],"states_connection":[{"source":"DP02634r001","target":"DP02634r010"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T13:12:37.214Z"}},{"start":260,"end":285,"reference_id":"24052259","reference_source":"pmid","reference_html":"Crystal structures of β-1,4-galactosyltransferase 7 enzyme reveal conformational changes and substrate binding. <i> Tsutsui Y, Ramakrishnan B, Qasba PK. </i> J Biol Chem, 2013","date":"2022-10-21T08:56:06.502Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"4IRP"}],"region_id":"DP02634r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17659","statements":[{"type":"Methods","text":"The tetragonal crystal was soaked in the same pH 6.5 reservoir solution containing 15% 2-methy-2,4-pentanediol (MPD) at 18 °C for 20 h followed by a brief soak in 100 mM Tris (pH 8.0), 750 mM sodium acetate, 15% MPD, 5 mM MnCl2, and 5 mM UDP-Gal at room temperature."}],"entry_name":"UDP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29035","statements":[{"type":"Methods","text":"One manganese ion and one UDP molecule are located in the catalytic pocket of each protein molecule."}],"entry_name":"manganese(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30089","statements":[{"type":"Methods","text":"The purified β4GalT7Δ81 (15 mg/ml) was readily crystallized using the hanging drop vapor diffusion method with 100 mM imidazole (pH 6.5) and 750 mM sodium acetate as a reservoir solution in the presence of 5 mM MnCl2 at 18 °C. The addition of MnCl2 was necessary for growing a larger, 0.1–0.2 mm crystal."}],"entry_name":"acetate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"50059","statements":[{"type":"Methods","text":"The purified β4GalT7Δ81 (15 mg/ml) was readily crystallized using the hanging drop vapor diffusion method with 100 mM imidazole (pH 6.5) and 750 mM sodium acetate as a reservoir solution in the presence of 5 mM MnCl2 at 18 °C. The addition of MnCl2 was necessary for growing a larger, 0.1–0.2 mm crystal."}],"entry_name":"imidazolium cation"}],"statement":[{"text":"We present here the crystal structures of human β4GalT7 in open and closed conformations. A comparison of these crystal structures shows that, upon\nmanganese and UDP or UDP-Gal binding, the enzyme undergoes conformational changes involving a small and a long loop.","type":"Abstract"},{"text":"In the open conformation crystal structure (Fig. 1A), no electron density was observed for a region encompassing residues 260–278, and only weak backbone electron density could be traced for residues 278–284. In contrast, the same region in the closed conformation had clear electron density corresponding to a long loop, residues 260–285 (Fig. 1B). The appearance of the long loop coincides with the change in the orientation of the Trp224 side chain, from pointing away to pointing toward the binding pocket, forming a hydrogen bond with the β-phosphate oxygen atom of the bound UDP (Fig. 1B).","type":"Results"},{"text":"The present human β4GalT7 crystal structures show that the β4GalT7 enzyme undergoes conformational changes upon binding with manganese and UDP or UDP-Gal. This conformational change involves small and long loops containing residues Gly223-Trp224 and His259 to Gly284, respectively.","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T13:12:34.939Z"}},{"start":260,"end":285,"reference_id":"24052259","reference_source":"pmid","reference_html":"Crystal structures of β-1,4-galactosyltransferase 7 enzyme reveal conformational changes and substrate binding. <i> Tsutsui Y, Ramakrishnan B, Qasba PK. </i> J Biol Chem, 2013","date":"2022-10-17T16:19:09.286Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"4IRQ"}],"region_id":"DP02634r010","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17659","statements":[{"type":"Methods","text":"The tetragonal crystal was soaked in the same pH 6.5 reservoir solution containing 15% 2-methy-2,4-pentanediol (MPD) at 18 °C for 20 h followed by a brief soak in 100 mM Tris (pH 8.0), 750 mM sodium acetate, 15% MPD, 5 mM MnCl2, and 5 mM UDP-Gal at room temperature."}],"entry_name":"UDP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29035","statements":[{"type":"Methods","text":"One manganese ion and one UDP molecule are located in the catalytic pocket of each protein molecule."}],"entry_name":"manganese(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46097","statements":[{"type":"Methods","text":"The tetragonal crystal was soaked in the same pH 6.5 reservoir solution containing 15% 2-methy-2,4-pentanediol (MPD) at 18 °C for 20 h followed by a brief soak in 100 mM Tris (pH 8.0), 750 mM sodium acetate, 15% MPD, 5 mM MnCl2, and 5 mM UDP-Gal at room temperature."}],"entry_name":"Htris"}],"statement":[{"text":"In the open conformation crystal structure (Fig. 1A), no electron density was observed for a region encompassing residues 260–278, and only weak backbone electron density could be traced for residues 278–284. In contrast, the same region in the closed conformation had clear electron density corresponding to a long loop, residues 260–285 (Fig. 1B). The appearance of the long loop coincides with the change in the orientation of the Trp224 side chain, from pointing away to pointing toward the binding pocket, forming a hydrogen bond with the β-phosphate oxygen atom of the bound UDP (Fig. 1B).","type":"Results"},{"text":"In the crystal structures of human β4GalT7, the missing and weak electron density from residues 260 –284, together with the presence of the Trp224 side chain rotamers in the open conformation (data not shown), suggest structural flexibility in this region.","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-20T15:32:46.304Z"}}],"released":"2021_06","length":327,"ncbi_taxon_id":9606,"date":"2020-03-09T11:58:38.120Z","organism":"Homo sapiens","features":{"gene3D":[{"start":47,"end":327,"id":"G3DSA:3.90.550.10","name":"Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A"}],"pfam":[{"id":"PF02709","name":"N-terminal domain of galactosyltransferase","start":182,"end":257},{"id":"PF13733","name":"N-terminal region of glycosyl transferase group 7","start":84,"end":175}]},"disprot_id":"DP02634","regions_counter":10,"dataset":["NDDs-related proteins"],"UniParc":"UPI00000361E1","uniref100":"UniRef100_Q9UBV7","uniref90":"UniRef90_Q9UBV7","uniref50":"UniRef50_Q9UBV7","genes":[{"name":{"value":"B4GALT7"},"synonyms":[{"value":"XGALT1"}],"orfNames":[{"value":"UNQ748/PRO1478"}]}],"alphafold_very_low_content":0.08868501529051988,"disorder_content":0.07951070336391437,"disprot_consensus":{"full":[{"start":260,"end":285,"type":"T"}],"Structural state":[{"start":260,"end":285,"type":"D"}],"Structural transition":[{"start":260,"end":285,"type":"T"}],"Disorder function":[{"start":260,"end":285,"type":"F"}]}},{"acc":"Q9ERE3","name":"Serine/threonine-protein kinase Sgk3","sequence":"MQRDCIMDYKESCPSVSIPSSDEHREKKKRFTVYKVLVSVGRSEWFVFRRYAEFDKLYNSLKKQFPAMALKIPAKRIFGDNFDPDFIKQRRAGLNEFIQNLVRYPELYNHPDVRAFLQMDSPRHQSDPSEDEDERSTSKPHSTSRNINLGPTGNPHAKPTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGELFFHLQRERSFPEPRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSMGHVVLTDFGLCKEGIAISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLNLRPGVSLTAWSILEELLEKNRQNRLGAKEDFLEIQNHPFFESLSWTDLVQKKIPPPFNPNVAGPDDIRNFDAVFTEETVPYSVCVSSDYSIVNASVLEADDAFVGFSYAPPSEDLFL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"region_id":"DP02635r001","ec_ontology":"ECO","end":160,"term_id":"IDPO:0000002","start":126,"version":2,"statement":[{"text":"Two CISK-PX fragments were used for the crystallographic studies. One contained the PX domain (short-PX, residues 7–126) and another contained both the PX domain and the linker between the PX domain and kinase domain (long-PX, residues 7–160)","type":"Methods"},{"text":"The density for this linker region, however, cannot be observed in the electron density map, which indicates that the linker region is much more dynamic compared with the PX domain in the crystallized CISK fragment. Our DLS data on different fragments of CISK-PX have shown that the fragment containing only the PX domain (residues 7–126, 14.34 kDa) is monomeric (DLS molecular mass, 16.68 kDa), whereas the fragment containing the PX domain and the linker region (residues 7–160, 18.00 kDa) is in an oligomeric form with DLS molecular weight around a dimer (35.14 kDa).","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15126499","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1XTE"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structural basis of membrane targeting by the Phox homology domain of cytokine-independent survival kinase (CISK-PX). <i> Xing Y, Liu D, Zhang R, Joachimiak A, Songyang Z, Xu W. </i> J Biol Chem, 2004","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02635r002","ec_ontology":"ECO","end":160,"term_id":"IDPO:0000033","start":126,"version":3,"statement":[{"text":"Two CISK-PX fragments were used for the crystallographic studies. One contained the PX domain (short-PX, residues 7–126) and another contained both the PX domain and the linker between the PX domain and kinase domain (long-PX, residues 7–160)","type":"Methods"},{"text":"The density for this linker region, however, cannot be observed in the electron density map, which indicates that the linker region is much more dynamic compared with the PX domain in the crystallized CISK fragment. Our DLS data on different fragments of CISK-PX have shown that the fragment containing only the PX domain (residues 7–126, 14.34 kDa) is monomeric (DLS molecular mass, 16.68 kDa), whereas the fragment containing the PX domain and the linker region (residues 7–160, 18.00 kDa) is in an oligomeric form with DLS molecular weight around a dimer (35.14 kDa).","type":"Results"},{"text":"Nevertheless, the high tendency for CISK-PX to dimerize in the presence of the linker region implies that dimerization may play an important role in CISK membrane localization and regulation.","type":"Results"},{"text":"Furthermore, biochemical studies reveal that CISK-PX dimerizes in the presence of the linker between the PX domain and kinase domain, suggesting a multivalent mechanism in membrane localization of CISK.","type":"Abstract"}],"term_name":"flexible linker","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15126499","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1XTE"}],"term_namespace":"Disorder function","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structural basis of membrane targeting by the Phox homology domain of cytokine-independent survival kinase (CISK-PX). <i> Xing Y, Liu D, Zhang R, Joachimiak A, Songyang Z, Xu W. </i> J Biol Chem, 2004","ec_go":"EXP","disprot_namespace":"Disorder function"},{"region_id":"DP02635r003","ec_ontology":"ECO","end":160,"term_id":"GO:0060090","start":126,"version":3,"statement":[{"text":"Furthermore, biochemical studies reveal that CISK-PX dimerizes in the presence of the linker between the PX domain and kinase domain, suggesting a multivalent mechanism in membrane localization of CISK.","type":"Abstract"},{"text":"The density for this linker region, however, cannot be observed in the electron density map, which indicates that the linker region is much more dynamic compared with the PX domain in the crystallized CISK fragment. Our DLS data on different fragments of CISK-PX have shown that the fragment containing only the PX domain (residues 7–126, 14.34 kDa) is monomeric (DLS molecular mass, 16.68 kDa), whereas the fragment containing the PX domain and the linker region (residues 7–160, 18.00 kDa) is in an oligomeric form with DLS molecular weight around a dimer (35.14 kDa).","type":"Results"},{"text":"Nevertheless, the high tendency for CISK-PX to dimerize in the presence of the linker region implies that dimerization may play an important role in CISK membrane localization and regulation.","type":"Results"},{"text":"In addition to the linker region, the PX domain itself might also contribute to part of the dimer interface. At least two models exist for the dimeric state of CISK-PX. In the first model, the linker facilitates the dimerization via linker-linker interaction; in the other model, the linker from one CISK molecule interacts with another CISK-PX domain","type":"Results"}],"term_name":"molecular adaptor activity","ec_name":"dynamic light scattering assay evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15126499","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1XTE"}],"term_namespace":"Molecular function","ec_id":"ECO:0007064","curator_id":"fquaglia","reference_html":"Structural basis of membrane targeting by the Phox homology domain of cytokine-independent survival kinase (CISK-PX). <i> Xing Y, Liu D, Zhang R, Joachimiak A, Songyang Z, Xu W. </i> J Biol Chem, 2004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02635r004","ec_ontology":"ECO","end":160,"term_id":"GO:0051179","start":126,"version":3,"statement":[{"text":"Furthermore, biochemical studies reveal that CISK-PX dimerizes in the presence of the linker between the PX domain and kinase domain, suggesting a multivalent mechanism in membrane localization of CISK.","type":"Abstract"},{"text":"Nevertheless, the high tendency for CISK-PX to dimerize in the presence of the linker region implies that dimerization may play an important role in CISK membrane localization and regulation.","type":"Results"}],"term_name":"localization","ec_name":"dynamic light scattering assay evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15126499","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1XTE"}],"term_namespace":"Biological process","ec_id":"ECO:0007064","curator_id":"fquaglia","reference_html":"Structural basis of membrane targeting by the Phox homology domain of cytokine-independent survival kinase (CISK-PX). <i> Xing Y, Liu D, Zhang R, Joachimiak A, Songyang Z, Xu W. </i> J Biol Chem, 2004","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2020_12","length":496,"ncbi_taxon_id":10090,"date":"2020-03-09T14:36:25.836Z","organism":"Mus musculus","features":{"gene3D":[{"start":7,"end":125,"id":"G3DSA:3.30.1520.10","name":"Phox-like domain"}],"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":163,"end":419},{"id":"PF00433","name":"Protein kinase C terminal domain","start":440,"end":487},{"id":"PF00787","name":"PX domain","start":42,"end":119}]},"disprot_id":"DP02635","regions_counter":4,"dataset":[],"UniParc":"UPI000002273E","uniref100":"UniRef100_Q9ERE3","uniref90":"UniRef90_Q96BR1","uniref50":"UniRef50_O00141","genes":[{"name":{"value":"Sgk3"},"synonyms":[{"value":"Cisk"},{"value":"Sgkl"}]}],"alphafold_very_low_content":0.11693548387096774,"disorder_content":0.07056451612903226,"disprot_consensus":{"full":[{"start":126,"end":160,"type":"D"}],"Structural state":[{"start":126,"end":160,"type":"D"}],"Disorder function":[{"start":126,"end":160,"type":"F"}],"Molecular function":[{"start":126,"end":160,"type":"F"}],"Biological process":[{"start":126,"end":160,"type":"F"}]}},{"acc":"O88393","name":"Transforming growth factor beta receptor type 3","sequence":"MAVTSHHMVPVFVLMSACLATAGPEPSTRCELSPISASHPVQALMESFTVLSGCASRGTTGLPREVHILNLRSTDQGLGQPQREVTLHLNPIASVHTHHKPVVFLLNSPQPLVWHVKTERLAAGVPRLFLVSEGSVVQFSSGNFSLTAETEERSFPQENEHLLHWAQKEYGAVTSFTELKIARNIYIKVGEDQVFPPTCNIGKNFLSLNYLAEYLQPKAAEGCVLASQPHEKEVHIIELISPNSNPYSTFQVDIIIDIRPAREDPEVVKNLVLILKCKKSVNWVIKSFDVKGNLKVIAPDSIGFGKESERSMTVTKLVRNDYPSTQENLMKWALDNGYSPVTSYTIAPVANRFHLRLENNEEMRDEEVHTIPPELRILLGPDHLPALDSPPFQGEIPNGGFPFPFPDIPRRGWKEGEDRIPRPKEPIIPRVQLLPDHREPEEVQGGVNIALSVKCDNEKMVVAVDKDSFQTNGYSGMELTLLDPSCKAKMNGTHFVLESPLNGCGTRHRRSAPDGVVYYNSIVVQAPSPGDSSGWPDGYEDLESGDNGFPGDTDEGETAPLSRAGVVVFNCSLRQLRSPSGFQDQLDGNATFNMELYNTDLFLVPSPGVFSVAENEHVYVEVSVTKADQDLGFAIQTCFISPYSNPDRMSDYTIIENICPKDDSVKFYSSKRVHFPIPHAEVDKKRFSFVFKSVFNTSLLFLHCELTLCSRNKGSQKLPKCVTPDDACTSLDATMIWTMMQNKKTFTKPLAVVLQVDYKENVPNMKESSPVPPPPQIFHGLDTLTVMGIAFAAFVIGALLTGALWYIYSHTGETARRQQVPTSPPASENSSAAHSIGSTQSTPCSSSSTA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":744,"region_id":"DP02636r001","start":730,"term_id":"IDPO:0000002","statement":[{"text":"In the murine 2.7 Å crystal structure that we are presenting here, the FG-loop is disordered, however, well-ordered in a recently reported homologous rat ZP-C structure.","type":"Abstract"},{"text":"Such a flexible and temporarily-modulated association of the EHP segment with the ZP domain has been proposed to control the polymerization of ZP domain-containing proteins. Our findings suggest that this flexibility also extends to the ZP domain of TGFR-3 and might facilitate co-receptor ligand interaction and presentation via the adjacent FG-loop.","type":"Abstract"},{"text":"In all ZP structures solved to date, the EHP segment folds back onto the ZP-C subdomain via a flexible FG-loop","type":"Introduction"},{"text":"In case of the bridging residues 730 to 744 in the FG loop we observe residual, however non-interpretable, difference density hinting that this segment remained largely intact in the crystals and that the lack of defined electron density is caused by conformational disorder in this segment","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23826237","version":2,"reference_html":"Identification of a Novel TGF-β-Binding Site in the Zona Pellucida C-terminal (ZP-C) Domain of TGF-β-Receptor-3 (TGFR-3). <i> Diestel U, Resch M, Meinhardt K, Weiler S, Hellmann TV, Mueller TD, Nickel J, Eichler J, Muller YA. </i> PLoS One, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4AJV"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":744,"region_id":"DP02636r002","start":730,"term_id":"IDPO:0000033","statement":[{"text":"In the murine 2.7 Å crystal structure that we are presenting here, the FG-loop is disordered, however, well-ordered in a recently reported homologous rat ZP-C structure.","type":"Abstract"},{"text":"Such a flexible and temporarily-modulated association of the EHP segment with the ZP domain has been proposed to control the polymerization of ZP domain-containing proteins. Our findings suggest that this flexibility also extends to the ZP domain of TGFR-3 and might facilitate co-receptor ligand interaction and presentation via the adjacent FG-loop.","type":"Abstract"},{"text":"In all ZP structures solved to date, the EHP segment folds back onto the ZP-C subdomain via a flexible FG-loop","type":"Introduction"},{"text":"In case of the bridging residues 730 to 744 in the FG loop we observe residual, however non-interpretable, difference density hinting that this segment remained largely intact in the crystals and that the lack of defined electron density is caused by conformational disorder in this segment","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23826237","version":3,"reference_html":"Identification of a Novel TGF-β-Binding Site in the Zona Pellucida C-terminal (ZP-C) Domain of TGF-β-Receptor-3 (TGFR-3). <i> Diestel U, Resch M, Meinhardt K, Weiler S, Hellmann TV, Mueller TD, Nickel J, Eichler J, Muller YA. </i> PLoS One, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4AJV"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2020_12","length":850,"ncbi_taxon_id":10090,"date":"2020-03-09T14:53:45.721Z","organism":"Mus musculus","features":{"gene3D":[],"pfam":[{"id":"PF00100","name":"ZP-C domain","start":588,"end":721},{"id":"PF23344","name":"ZP-N domain","start":455,"end":528},{"id":"PF26060","name":"TGFBR3-like, N-terminal domain","start":47,"end":214},{"id":"PF26060","name":"TGFBR3-like, N-terminal domain","start":218,"end":362}]},"disprot_id":"DP02636","regions_counter":2,"dataset":[],"UniParc":"UPI0000029689","uniref100":"UniRef100_O88393","uniref90":"UniRef90_O88393","uniref50":"UniRef50_O88393","genes":[{"name":{"value":"Tgfbr3"}}],"alphafold_very_low_content":0.27058823529411763,"disorder_content":0.01764705882352941,"disprot_consensus":{"full":[{"start":730,"end":744,"type":"D"}],"Structural state":[{"start":730,"end":744,"type":"D"}],"Disorder function":[{"start":730,"end":744,"type":"F"}]}},{"acc":"P07237","name":"Protein disulfide-isomerase","sequence":"MLRRALLCLAVAALVRADAPEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDSAKQFLQAAEAIDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESEELTAERITEFCHRFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFEDVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGDDDDLEDLEEAEEPDMEEDDDQKAVKDEL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":334,"region_id":"DP02637r001","start":323,"term_id":"IDPO:0000002","statement":[{"text":"The residues corresponding to the β5 strand and the following β5–α4 loop are absent from the electron density map due to disorder.","type":"Results"},{"text":"No electron density was observed for P135, E348–S357 (the x‐linker), the N‐terminal GPLGS cloning linker and, additionally, residues E323–L334 for chain A and E322–A336 for chain B that correspond to the strand β5 and β5–α4 loop in the b′x crystal structure.","type":"Results"},{"text":"The β5 strand, which normally forms β‐sheet with the β4 strand, is disordered in the dimeric structure.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24549644","version":2,"reference_html":"Structural insight into the dimerization of human protein disulfide isomerase. <i> Bastos-Aristizabal S, Kozlov G, Gehring K. </i> Protein Sci, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4JU5"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-13T20:38:03.607Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":357,"region_id":"DP02637r002","start":348,"term_id":"IDPO:0000002","statement":[{"text":"PDI, also known as PDIA1, is the founding member and the most studied protein in the PDI family. PDI contains four thioredoxin‐like domains abb′a′, where a denotes catalytic domains containing CxxC motifs and b stands for non‐catalytic domains, with a 20‐residue x‐linker between b′ and a′ domain and a C‐terminal acidic tail.","type":"Introduction"},{"text":"The construct (residues 135–357) includes the bb′ domains and half of the x‐linker and yields high‐quality NMR spectra that were used to determine the NMR solution structure of the monomeric form","type":"Results"},{"text":"No electron density was observed for P135, E348–S357 (the x‐linker), the N‐terminal GPLGS cloning linker and, additionally, residues E323–L334 for chain A and E322–A336 for chain B that correspond to the strand β5 and β5–α4 loop in the b′x crystal structure.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24549644","version":2,"reference_html":"Structural insight into the dimerization of human protein disulfide isomerase. <i> Bastos-Aristizabal S, Kozlov G, Gehring K. </i> Protein Sci, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4JU5"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-13T20:38:04.501Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":357,"region_id":"DP02637r003","start":348,"term_id":"IDPO:0000033","statement":[{"text":"PDI, also known as PDIA1, is the founding member and the most studied protein in the PDI family. PDI contains four thioredoxin‐like domains abb′a′, where a denotes catalytic domains containing CxxC motifs and b stands for non‐catalytic domains, with a 20‐residue x‐linker between b′ and a′ domain and a C‐terminal acidic tail.","type":"Introduction"},{"text":"The construct (residues 135–357) includes the bb′ domains and half of the x‐linker and yields high‐quality NMR spectra that were used to determine the NMR solution structure of the monomeric form","type":"Results"},{"text":"No electron density was observed for P135, E348–S357 (the x‐linker), the N‐terminal GPLGS cloning linker and, additionally, residues E323–L334 for chain A and E322–A336 for chain B that correspond to the strand β5 and β5–α4 loop in the b′x crystal structure.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24549644","version":3,"reference_html":"Structural insight into the dimerization of human protein disulfide isomerase. <i> Bastos-Aristizabal S, Kozlov G, Gehring K. </i> Protein Sci, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4JU5"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-13T20:38:03.351Z"}},{"start":479,"end":508,"reference_id":"36265586","reference_source":"pmid","reference_html":"Crystal structure of the collagen prolyl 4-hydroxylase (C-P4H) catalytic domain complexed with PDI: Toward a model of the C-P4H α<sub>2</sub>β<sub>2</sub> tetramer. <i> Murthy AV, Sulu R, Lebedev A, Salo AM, Korhonen K, Venkatesan R, Tu H, Bergmann U, Jänis J, Laitaoja M, Ruddock LW, Myllyharju J, Koski MK, Wierenga RK. </i> J Biol Chem, 2022","date":"2023-12-13T20:33:12.129Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7ZSC"}],"region_id":"DP02637r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O15460"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"}],"statement":[{"text":"The highly acidic C-terminal region of PDI (residues 477–498) is also completely disordered and not seen in the electron density maps.","type":"Results"}]}],"released":"2021_06","length":508,"ncbi_taxon_id":9606,"date":"2020-03-09T15:11:56.808Z","organism":"Homo sapiens","features":{"gene3D":[{"start":362,"end":479,"id":"G3DSA:3.40.30.10","name":"Glutaredoxin"},{"start":362,"end":479,"id":"G3DSA:3.40.30.10","name":"Glutaredoxin"},{"start":362,"end":479,"id":"G3DSA:3.40.30.10","name":"Glutaredoxin"}],"pfam":[{"id":"PF00085","name":"Thioredoxin","start":26,"end":131},{"id":"PF00085","name":"Thioredoxin","start":369,"end":471},{"id":"PF13848","name":"Thioredoxin-like domain","start":161,"end":344}]},"disprot_id":"DP02637","regions_counter":4,"dataset":["Autophagy-related proteins","Condensates-related proteins"],"UniParc":"UPI000016AF0F","uniref100":"UniRef100_P07237","uniref90":"UniRef90_P07237","uniref50":"UniRef50_P07237","genes":[{"name":{"value":"P4HB"},"synonyms":[{"value":"ERBA2L"},{"value":"PDI"},{"value":"PDIA1"},{"value":"PO4DB"}]}],"alphafold_very_low_content":0.09055118110236221,"disorder_content":0.10236220472440945,"disprot_consensus":{"full":[{"start":323,"end":334,"type":"D"},{"start":348,"end":357,"type":"D"},{"start":479,"end":508,"type":"D"}],"Structural state":[{"start":323,"end":334,"type":"D"},{"start":348,"end":357,"type":"D"},{"start":479,"end":508,"type":"D"}],"Disorder function":[{"start":348,"end":357,"type":"F"}]}},{"acc":"Q6ZPF4","name":"Formin-like protein 3","sequence":"MGNLESTDGGPGEPPSVPLLLPPGKTPMPEPCELEERFALVLSSMNLPPDKARLLRQYDNEKKWDLICDQERFQVKNPPHTYIQKLQSFLDPNVTRKKFRRRVQESTKVLRELEISLRTNHIGWVREFLNDENKGLDVLVDYLSFAQCSVMFDFEGLESGDDGAFDKLRSWSRSIEDLQPPNALSAPFTNSLARSARQSVLRYSTLPGRRALKNSRLVSQKDDVHVCILCLRAIMNYQYGFNLVMSHPHAVNEIALSLNNKNPRTKALVLELLAAVCLVRGGHEIILAAFDNFKEVCKELHRFEKLMEYFRNEDSNIDFMVACMQFINIVVHSVEDMNFRVHLQYEFTKLGLEEFLQKSRHTESEKLQVQIQAYLDNVFDVGGLLEDAETKNVALEKVEELEEHVSHLTEKLLDLENENMMRVAELEKQLLQREKELESIKETYENTSNQVHTLRRLIKEKEEAFQRRCHLEPSARGLESMGGEALARVGPTELTEGIPPSDLDLLAPAPPTEETLPLPPPPAPPLPPPPPPLPDKCPPAPPLPGAAPSVVLTVGLSAIRIKKPIKTKFRLPVFNWTALKPNQINGTVFSELDDEKILEDLDLDRFEELFKTKAQGPALDLICSKNKTAQKAASKVTLLEANRAKNLAITLRKAGRSAEEICRAIHTFDLQTLPVDFVECLMRFLPTEAEVKLLRQYERERQPLEELAAEDRFMLLFSKVERLTQRMAGMAFLGNFQDNLQMLTPQLNAIIAASASVKSSQKLKQMLEIILALGNYMNSSKRGAVYGFKLQSLDLLLDTKSTDRKMTLLHFIALTVKEKYPELANFWQELHFVEKAAAVSLENVLLDVKELGRGMELIRRECSIHDNSVLRNFLSTNEGKLDKLQRDAKTAEEAYNAVVRYFGESPKTTPPSVFFPVFVRFIRSYKEAEQENEARKKQEEVMREKQLAQEAKKLDAKTPSQRNKWQQQELIAELRRRQAKEHRPVYEGKDGTIEDIITVLKSVPFTARTAKRGSRFFCDAAHHDESNC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":634,"region_id":"DP02638r001","start":615,"term_id":"IDPO:0000002","statement":[{"text":"A flexible linker of varying length allows considerable flexibility in orientation of the subunits","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23222643","version":2,"reference_html":"FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation. <i> Thompson ME, Heimsath EG, Gauvin TJ, Higgs HN, Kull FJ. </i> Nat Struct Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4EAH"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":634,"region_id":"DP02638r002","start":615,"term_id":"IDPO:0000033","statement":[{"text":"A flexible linker of varying length allows considerable flexibility in orientation of the subunits","type":"Article"},{"text":"The separation of actin subunits in the FMNL3–actin structure shows that each actin monomer can be held in place only through interactions with FH2 subunits, which suggests that flexibility in the FH2 linker region could allow the actin subunits to remain in contact with the FH2 domains while sliding past one another during elongation","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23222643","version":3,"reference_html":"FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation. <i> Thompson ME, Heimsath EG, Gauvin TJ, Higgs HN, Kull FJ. </i> Nat Struct Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4EAH"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","length":1028,"ncbi_taxon_id":10090,"date":"2020-03-09T15:22:09.324Z","organism":"Mus musculus","features":{"gene3D":[{"start":554,"end":938,"id":"G3DSA:1.20.58.2220","name":"G3DSA:1.20.58.2220"}],"pfam":[{"id":"PF02181","name":"Formin Homology 2 Domain","start":562,"end":926},{"id":"PF06367","name":"Diaphanous FH3 Domain","start":283,"end":472},{"id":"PF06371","name":"Diaphanous GTPase-binding Domain","start":28,"end":144},{"id":"PF06371","name":"Diaphanous GTPase-binding Domain","start":220,"end":278}]},"disprot_id":"DP02638","regions_counter":2,"dataset":[],"UniParc":"UPI00001D4B76","uniref100":"UniRef100_Q6ZPF4","uniref90":"UniRef90_Q8IVF7-2","uniref50":"UniRef50_Q8IVF7","genes":[{"name":{"value":"Fmnl3"},"synonyms":[{"value":"Frl2"},{"value":"Kiaa2014"}]}],"alphafold_very_low_content":0.20038910505836577,"disorder_content":0.019455252918287938,"disprot_consensus":{"full":[{"start":615,"end":634,"type":"D"}],"Structural state":[{"start":615,"end":634,"type":"D"}],"Disorder function":[{"start":615,"end":634,"type":"F"}]}},{"acc":"P78330","name":"Phosphoserine phosphatase","sequence":"MVSHSELRKLFYSADAVCFDVDSTVIREEGIDELAKICGVEDAVSEMTRRAMGGAVPFKAALTERLALIQPSREQVQRLIAEQPPHLTPGIRELVSRLQERNVQVFLISGGFRSIVEHVASKLNIPATNVFANRLKFYFNGEYAGFDETQPTAESGGKGKVIKLLKEKFHFKKIIMIGDGATDMEACPPADAFIGFGGNVIRQQVKDNAKWYITDFVELLGELEE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":56,"region_id":"DP02639r001","start":45,"term_id":"IDPO:0000002","statement":[{"text":"For another 12 amino acids in MolA (45–56) and another ten amino acids in MolB (47–56), there is no visible density in the electron-density maps. As will be discussed later, this unfolded region coincides with the region that discriminates between the open and closed conformation.","type":"Results"},{"text":"Helix α3, connecting helix α2 to helix α4 in the closed conformation (not shown), is completely disordered in the open conformation and is therefore not visible.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12777757","version":2,"reference_html":"High-resolution structure of human phosphoserine phosphatase in open conformation. <i> Peeraer Y, Rabijns A, Verboven C, Collet JF, Van Schaftingen E, De Ranter C. </i> Acta Crystallogr D Biol Crystallogr, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1NNL"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T14:58:03.798Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":56,"region_id":"DP02639r002","start":45,"term_id":"IDPO:0000002","statement":[{"text":"For another 12 amino acids in MolA (45–56) and another ten amino acids in MolB (47–56), there is no visible density in the electron-density maps. As will be discussed later, this unfolded region coincides with the region that discriminates between the open and closed conformation.","type":"Results"},{"text":"The B-factor plot of the main-chain atoms, shown in Fig. 2, clearly indicates that the missing residues are located in a region of higher than average B factors.","type":"Results"}],"curator_id":"vnugnes","released":"2023_06","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"12777757","version":3,"reference_html":"High-resolution structure of human phosphoserine phosphatase in open conformation. <i> Peeraer Y, Rabijns A, Verboven C, Collet JF, Van Schaftingen E, De Ranter C. </i> Acta Crystallogr D Biol Crystallogr, 2003","date":"2023-06-13T14:57:47.898Z","reference_source":"pmid","ec_id":"ECO:0006222","cross_refs":[{"db":"PDB","id":"1NNL"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val2Ile","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271"}]}],"released":"2021_06","length":225,"ncbi_taxon_id":9606,"date":"2020-03-12T08:44:00.811Z","organism":"Homo sapiens","features":{"gene3D":[{"start":30,"end":146,"id":"G3DSA:1.10.150.210","name":"Phosphoserine phosphatase; domain 2"},{"start":16,"end":213,"id":"G3DSA:3.40.50.1000","name":"HAD superfamily/HAD-like"}],"pfam":[{"id":"PF00702","name":"haloacid dehalogenase-like hydrolase","start":15,"end":187}]},"disprot_id":"DP02639","regions_counter":5,"dataset":["NDDs-related proteins"],"UniParc":"UPI0000135875","uniref100":"UniRef100_P78330","uniref90":"UniRef90_P78330","uniref50":"UniRef50_P78330","genes":[{"name":{"value":"PSPH","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9577","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9577"}}]}}],"alphafold_very_low_content":0.0044444444444444444,"disorder_content":0.05333333333333334,"disprot_consensus":{"full":[{"start":45,"end":56,"type":"D"}],"Structural state":[{"start":45,"end":56,"type":"D"}]}},{"acc":"Q4F883","name":"Senescence-associated carboxylesterase 101","sequence":"MESSSSLKGSALGKLVVTSGLLHSSWSKILEIHNPPYSNHDPGLQVSKKKKDSGLEFQIHREEKFTLVVFSAPPICRSSSSDSTLLHVKDKENPFPFLCSENNPSFSLHTPAFNLFTSASTSLTYLKSELLQTLKSEKPVIITGAALGGSVASLYTLWLLETIEPTLKRPLCITFGSPLIGDASLQQILENSVRNSCFLHVVSAQTRIKMDFFKPFGTFLICFDSGCVCIEDHVAVTELLNGVHDSGLVDYSQVLNRLDQSMLSLADSRLIPEDVIKGIEKRAEMKNLRFDMMFKKLNDMKISMAYIEWYKKKCKEVKIGYYDRFKTQLAFPSKEFDINIKNHHKSELNRFWKSVVEEVERRPQSDASILKRRFLFSGNNYRRMIEPLDIAEYYLEGRKEYRTTGRSHHYVMLEKWFGMESILIEKERCKKRDLSDLLTFDSCFWAEVEDSLIVINQLNTTVGMRDDVREVLTRKLVEFEGYVWEIITKREVSPEIFLEESSFMKWWKEYKKIKGFNSSYLTEFMNTRKYESYGKSQ","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":52,"region_id":"DP02640r001","start":35,"term_id":"IDPO:0000002","statement":[{"text":"A flexible SAG101 segment between P35 and D52 is represented as a dotted line.","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24331460","version":2,"reference_html":"Structural basis for signaling by exclusive EDS1 heteromeric complexes with SAG101 or PAD4 in plant innate immunity. <i> Wagner S, Stuttmann J, Rietz S, Guerois R, Brunstein E, Bautor J, Niefind K, Parker JE. </i> Cell Host Microbe, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4NFU"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":52,"region_id":"DP02640r002","start":35,"term_id":"IDPO:0000033","statement":[{"text":"A flexible SAG101 segment between P35 and D52 is represented as a dotted line.","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24331460","version":3,"reference_html":"Structural basis for signaling by exclusive EDS1 heteromeric complexes with SAG101 or PAD4 in plant innate immunity. <i> Wagner S, Stuttmann J, Rietz S, Guerois R, Brunstein E, Bautor J, Niefind K, Parker JE. </i> Cell Host Microbe, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4NFU"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","length":537,"ncbi_taxon_id":3702,"date":"2020-03-12T08:55:27.179Z","organism":"Arabidopsis thaliana","features":{"gene3D":[{"start":56,"end":206,"id":"G3DSA:3.40.50.1820","name":"G3DSA:3.40.50.1820"}],"pfam":[{"id":"PF01764","name":"Lipase (class 3)","start":109,"end":202},{"id":"PF18117","name":"Enhanced disease susceptibility 1 protein EP domain","start":306,"end":518}]},"disprot_id":"DP02640","regions_counter":2,"dataset":[],"UniParc":"UPI00001624A1","uniref100":"UniRef100_Q4F883","uniref90":"UniRef90_Q4F883","uniref50":"UniRef50_Q4F883","genes":[{"name":{"value":"SAG101"},"orfNames":[{"value":"F2G14.50"}],"olnNames":[{"value":"At5g14930"}]}],"alphafold_very_low_content":0.0260707635009311,"disorder_content":0.0335195530726257,"disprot_consensus":{"full":[{"start":35,"end":52,"type":"D"}],"Structural state":[{"start":35,"end":52,"type":"D"}],"Disorder function":[{"start":35,"end":52,"type":"F"}]}},{"acc":"Q8GY88","name":"Shikimate kinase 2, chloroplastic","sequence":"MEAATVQRFQYSSWNDLRNFEGKPRGSLRYNTQRIKEDKRFRVVALTLDKRRDHRLRSVSDKNSSALLETGSLLHSPFDEEQQILKKKAEEVKPYLNGRSMYLVGMMGSGKTTVGKIMARSLGYTFFDCDTLIEQAMKGTSVAEIFEHFGESVFREKETEALKKLSLMYHQVVVSTGGGAVIRPINWKYMHKGISIWLDVPLEALAHRIAAVGTGSRPLLHDDESGDTYTAALNRLSTIWDARGEAYTKASARVSLENITLKLGYRSVSDLTPAEIAIEAFEQVQSYLEKEDGMARPDGL","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":81,"region_id":"DP02641r001","start":55,"term_id":"IDPO:0000002","statement":[{"text":"There are 28 residues preceding α-helix 1, which were not built in the AtSK2 structure due to a lack of corresponding electron density","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21520319","version":2,"reference_html":"Structural and biochemical investigation of two Arabidopsis shikimate kinases: the heat-inducible isoform is thermostable. <i> Fucile G, Garcia C, Carlsson J, Sunnerhagen M, Christendat D. </i> Protein Sci, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3NWJ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":227,"region_id":"DP02641r002","start":212,"term_id":"IDPO:0000002","statement":[{"text":"Most of the AtSK2 LID domain between α-helix 7 and α-helix 8 (residues 212-227) was not modeled in the AtSK2 crystal structure due to a lack of corresponding electron density. This region contains the substrate binding and putatively catalytic arginine (Arg117) of the LID domain","type":"Results"},{"text":"The apo-AtSK2 structure adopts the open conformation, as indicated by the orientation of the disordered LID domain away from the active site and the spacing of the ESB and NB domains away from the RC domain relative to the closed conformation MtSK structure.","type":"Results"},{"text":"The AtSK2 structure can be divided into four domains [Fig. 2(B)]: the reduced CORE (RC) domain comprising the central β-sheet and flanking α-helices, the nucleotide binding (NB) domain, which includes the phosphate binding loop (P-loop/Walker-A motif), the disordered LID domain, which contains catalytic and substrate binding residues, and the extended shikimate binding (ESB) domain, which includes a modified SK-type Walker B motif and several other substrate binding residues.","type":"Results"},{"text":"The extended loop region of the LID domain was not modeled in the AtSK2 structure.","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21520319","version":2,"reference_html":"Structural and biochemical investigation of two Arabidopsis shikimate kinases: the heat-inducible isoform is thermostable. <i> Fucile G, Garcia C, Carlsson J, Sunnerhagen M, Christendat D. </i> Protein Sci, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3NWJ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":227,"region_id":"DP02641r003","start":212,"term_id":"GO:0005515","statement":[{"text":"Most of the AtSK2 LID domain between α-helix 7 and α-helix 8 (residues 212-227) was not modeled in the AtSK2 crystal structure due to a lack of corresponding electron density. This region contains the substrate binding and putatively catalytic arginine (Arg117) of the LID domain","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"21520319","version":3,"reference_html":"Structural and biochemical investigation of two Arabidopsis shikimate kinases: the heat-inducible isoform is thermostable. <i> Fucile G, Garcia C, Carlsson J, Sunnerhagen M, Christendat D. </i> Protein Sci, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","cross_refs":[{"db":"PDB","id":"3NWJ"}],"term_name":"protein binding","curator_orcid":"0000-0002-0341-4888","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":227,"region_id":"DP02641r004","start":212,"term_id":"GO:0098772","statement":[{"text":"Most of the AtSK2 LID domain between α-helix 7 and α-helix 8 (residues 212-227) was not modeled in the AtSK2 crystal structure due to a lack of corresponding electron density. This region contains the substrate binding and putatively catalytic arginine (Arg117) of the LID domain","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"21520319","version":3,"reference_html":"Structural and biochemical investigation of two Arabidopsis shikimate kinases: the heat-inducible isoform is thermostable. <i> Fucile G, Garcia C, Carlsson J, Sunnerhagen M, Christendat D. </i> Protein Sci, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","cross_refs":[{"db":"PDB","id":"3NWJ"}],"term_name":"molecular function regulator","curator_orcid":"0000-0002-0341-4888","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","length":300,"ncbi_taxon_id":3702,"date":"2020-03-12T09:17:37.663Z","organism":"Arabidopsis thaliana","features":{"gene3D":[],"pfam":[{"id":"PF01202","name":"Shikimate kinase","start":107,"end":261}]},"disprot_id":"DP02641","regions_counter":4,"dataset":[],"UniParc":"UPI000000C5CE","uniref100":"UniRef100_Q8GY88","uniref90":"UniRef90_Q8GY88","uniref50":"UniRef50_Q8GY88","genes":[{"name":{"value":"SK2"},"orfNames":[{"value":"F23K16.170"}],"olnNames":[{"value":"At4g39540"}]}],"alphafold_very_low_content":0.25666666666666665,"disorder_content":0.14333333333333334,"disprot_consensus":{"full":[{"start":55,"end":81,"type":"D"},{"start":212,"end":227,"type":"D"}],"Structural state":[{"start":55,"end":81,"type":"D"},{"start":212,"end":227,"type":"D"}],"Molecular function":[{"start":212,"end":227,"type":"F"}]}},{"acc":"P53780","name":"Cystathionine beta-lyase, chloroplastic","sequence":"MTSSLSLHSSFVPSFADLSDRGLISKNSPTSVSISKVPTWEKKQISNRNSFKLNCVMEKSVDGQTHSTVNNTTDSLNTMNIKEEASVSTLLVNLDNKFDPFDAMSTPLYQTATFKQPSAIENGPYDYTRSGNPTRDALESLLAKLDKADRAFCFTSGMAALSAVTHLIKNGEEIVAGDDVYGGSDRLLSQVVPRSGVVVKRVNTTKLDEVAAAIGPQTKLVWLESPTNPRQQISDIRKISEMAHAQGALVLVDNSIMSPVLSRPLELGADIVMHSATKFIAGHSDVMAGVLAVKGEKLAKEVYFLQNSEGSGLAPFDCWLCLRGIKTMALRIEKQQENARKIAMYLSSHPRVKKVYYAGLPDHPGHHLHFSQAKGAGSVFSFITGSVALSKHLVETTKYFSIAVSFGSVKSLISMPCFMSHASIPAEVREARGLTEDLVRISAGIEDVDDLISDLDIAFKTFPL","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":84,"region_id":"DP02642r001","start":57,"term_id":"IDPO:0000002","statement":[{"text":"The N-terminal domain (residues 57–131) is only partially defined (residues 57–84 are flexible) and interacts with the active site of the neighboring monomer.","type":"Results"},{"text":"hree stretches of the polypeptide chain were invisible in the electron density maps; the N-terminal part, i.e. residues 57 to 84; the region between residues 418 to 433; and the 11 amino acids of the C-terminalStrep-tag","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11402193","version":2,"reference_html":"The three-dimensional structure of cystathionine beta-lyase from Arabidopsis and its substrate specificity. <i> Breitinger U, Clausen T, Ehlert S, Huber R, Laber B, Schmidt F, Pohl E, Messerschmidt A. </i> Plant Physiol, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1IBJ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":84,"region_id":"DP02642r002","start":57,"term_id":"GO:0060090","statement":[{"text":"The N-terminal domain (residues 57–131) is only partially defined (residues 57–84 are flexible) and interacts with the active site of the neighboring monomer.","type":"Results"},{"text":"Three stretches of the polypeptide chain were invisible in the electron density maps; the N-terminal part, i.e. residues 57 to 84; the region between residues 418 to 433; and the 11 amino acids of the C-terminalStrep-tag","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11402193","version":3,"reference_html":"The three-dimensional structure of cystathionine beta-lyase from Arabidopsis and its substrate specificity. <i> Breitinger U, Clausen T, Ehlert S, Huber R, Laber B, Schmidt F, Pohl E, Messerschmidt A. </i> Plant Physiol, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"1IBJ"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","length":464,"ncbi_taxon_id":3702,"date":"2020-03-12T15:27:16.536Z","organism":"Arabidopsis thaliana","features":{"gene3D":[{"start":85,"end":328,"id":"G3DSA:3.40.640.10","name":"Type I PLP-dependent aspartate aminotransferase-like (Major domain)"},{"start":329,"end":464,"id":"G3DSA:3.90.1150.10","name":"Aspartate Aminotransferase, domain 1"}],"pfam":[{"id":"PF01053","name":"Cys/Met metabolism PLP-dependent enzyme","start":88,"end":460}]},"disprot_id":"DP02642","regions_counter":2,"dataset":[],"UniParc":"UPI0000036A1A","uniref100":"UniRef100_P53780","uniref90":"UniRef90_P53780","uniref50":"UniRef50_P53780","genes":[{"orfNames":[{"value":"F24I3.130"}],"olnNames":[{"value":"At3g57050"}]}],"alphafold_very_low_content":0.17025862068965517,"disorder_content":0.0603448275862069,"disprot_consensus":{"full":[{"start":57,"end":84,"type":"D"}],"Structural state":[{"start":57,"end":84,"type":"D"}],"Molecular function":[{"start":57,"end":84,"type":"F"}]}},{"acc":"Q9MAB9","name":"Membrane-anchored ubiquitin-fold protein 1","sequence":"MAEVHNQLEIKFRLTDGSDIGPKAFPDATTVSALKETVISEWPREKENGPKTVKEVKLISAGKVLENSKTVKDYRSPVSNLAGAVTTMHVIIQAPVTEKEKKPKGDPKMNKCVCSVM","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":116,"region_id":"DP02643r001","start":101,"term_id":"IDPO:0000002","statement":[{"text":"Disordered residues 101–116 of the C terminus have been omitted for clarity","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15782178","version":2,"reference_html":"Cell-free protein production and labeling protocol for NMR-based structural proteomics. <i> Vinarov DA, Lytle BL, Peterson FC, Tyler EM, Volkman BF, Markley JL. </i> Nat Methods, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"1SE9"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":117,"ncbi_taxon_id":3702,"date":"2020-03-12T15:48:00.552Z","organism":"Arabidopsis thaliana","features":{"gene3D":[],"pfam":[{"id":"PF13881","name":"Ubiquitin-2 like Rad60 SUMO-like","start":7,"end":115}]},"disprot_id":"DP02643","regions_counter":1,"dataset":[],"UniParc":"UPI00000A6052","uniref100":"UniRef100_Q9MAB9","uniref90":"UniRef90_Q9MAB9","uniref50":"UniRef50_Q8LCS8","genes":[{"name":{"value":"MUB1"},"orfNames":[{"value":"T4P13.27"}],"olnNames":[{"value":"At3g01050"}]}],"alphafold_very_low_content":0.1111111111111111,"disorder_content":0.13675213675213677,"disprot_consensus":{"full":[{"start":101,"end":116,"type":"D"}],"Structural state":[{"start":101,"end":116,"type":"D"}]}},{"acc":"Q9SUM3","name":"NADPH--cytochrome P450 reductase 2","sequence":"MSSSSSSSTSMIDLMAAIIKGEPVIVSDPANASAYESVAAELSSMLIENRQFAMIVTTSIAVLIGCIVMLVWRRSGSGNSKRVEPLKPLVIKPREEEIDDGRKKVTIFFGTQTGTAEGFAKALGEEAKARYEKTRFKIVDLDDYAADDDEYEEKLKKEDVAFFFLATYGDGEPTDNAARFYKWFTEGNDRGEWLKNLKYGVFGLGNRQYEHFNKVAKVVDDILVEQGAQRLVQVGLGDDDQCIEDDFTAWREALWPELDTILREEGDTAVATPYTAAVLEYRVSIHDSEDAKFNDINMANGNGYTVFDAQHPYKANVAVKRELHTPESDRSCIHLEFDIAGSGLTYETGDHVGVLCDNLSETVDEALRLLDMSPDTYFSLHAEKEDGTPISSSLPPPFPPCNLRTALTRYACLLSSPKKSALVALAAHASDPTEAERLKHLASPAGKDEYSKWVVESQRSLLEVMAEFPSAKPPLGVFFAGVAPRLQPRFYSISSSPKIAETRIHVTCALVYEKMPTGRIHKGVCSTWMKNAVPYEKSENCSSAPIFVRQSNFKLPSDSKVPIIMIGPGTGLAPFRGFLQERLALVESGVELGPSVLFFGCRNRRMDFIYEEELQRFVESGALAELSVAFSREGPTKEYVQHKMMDKASDIWNMISQGAYLYVCGDAKGMARDVHRSLHTIAQEQGSMDSTKAEGFVKNLQTSGRYLRDVW","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":303,"region_id":"DP02644r001","start":263,"term_id":"IDPO:0000002","statement":[{"text":"A hinge region links the N‐terminal FMN‐binding domain to the rest of CPR.","type":"Introduction"},{"text":"Two forms of ATR2 exist in the crystal. Form A (chain A) has the electron density for all four domains except a 43‐residue fragment of the hinge region; Form B (chain B) has the electron density for three domains, but lacks that for the FMN‐binding domain (Fig. 2A). The structure of ATR2 is described based on Form A unless noted otherwise.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28103421","version":2,"reference_html":"Structure of the Arabidopsis thaliana NADPH-cytochrome P450 reductase 2 (ATR2) provides insight into its function. <i> Niu G, Zhao S, Wang L, Dong W, Liu L, He Y. </i> FEBS J, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5GXU"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":303,"region_id":"DP02644r002","start":263,"term_id":"IDPO:0000033","statement":[{"text":"A hinge region links the N‐terminal FMN‐binding domain to the rest of CPR.","type":"Introduction"},{"text":"Two forms of ATR2 exist in the crystal. Form A (chain A) has the electron density for all four domains except a 43‐residue fragment of the hinge region; Form B (chain B) has the electron density for three domains, but lacks that for the FMN‐binding domain (Fig. 2A). The structure of ATR2 is described based on Form A unless noted otherwise.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28103421","version":3,"reference_html":"Structure of the Arabidopsis thaliana NADPH-cytochrome P450 reductase 2 (ATR2) provides insight into its function. <i> Niu G, Zhao S, Wang L, Dong W, Liu L, He Y. </i> FEBS J, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5GXU"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":303,"region_id":"DP02644r003","start":73,"term_id":"IDPO:0000002","statement":[{"text":"Two forms of ATR2 exist in the crystal. Form A (chain A) has the electron density for all four domains except a 43‐residue fragment of the hinge region; Form B (chain B) has the electron density for three domains, but lacks that for the FMN‐binding domain (Fig. 2A). The structure of ATR2 is described based on Form A unless noted otherwise.","type":"Results"},{"text":"Disordered region in chain B that includes FMN-binding domain, solved in chain A, and hinge region (263-303) that is disordered in both chains","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28103421","version":2,"reference_html":"Structure of the Arabidopsis thaliana NADPH-cytochrome P450 reductase 2 (ATR2) provides insight into its function. <i> Niu G, Zhao S, Wang L, Dong W, Liu L, He Y. </i> FEBS J, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5GXU"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":711,"ncbi_taxon_id":3702,"date":"2020-03-12T16:28:24.290Z","organism":"Arabidopsis thaliana","features":{"gene3D":[{"start":356,"end":487,"id":"G3DSA:1.20.990.10","name":"NADPH-cytochrome p450 Reductase; Chain A, domain 3"},{"start":91,"end":274,"id":"G3DSA:3.40.50.360","name":"G3DSA:3.40.50.360"},{"start":552,"end":711,"id":"G3DSA:3.40.50.80","name":"Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module"}],"pfam":[{"id":"PF00175","name":"Oxidoreductase NAD-binding domain","start":565,"end":675},{"id":"PF00258","name":"Flavodoxin","start":107,"end":250},{"id":"PF00667","name":"FAD binding domain","start":307,"end":528}]},"disprot_id":"DP02644","regions_counter":3,"dataset":[],"UniParc":"UPI000009D6FE","uniref100":"UniRef100_Q9SUM3","uniref90":"UniRef90_Q9SUM3","uniref50":"UniRef50_Q9SUM3","genes":[{"name":{"value":"ATR2"},"synonyms":[{"value":"AR2"}],"orfNames":[{"value":"F9N11.60"}],"olnNames":[{"value":"At4g30210"}]}],"alphafold_very_low_content":0.0829817158931083,"disorder_content":0.32489451476793246,"disprot_consensus":{"full":[{"start":73,"end":303,"type":"D"}],"Structural state":[{"start":73,"end":303,"type":"D"}],"Disorder function":[{"start":263,"end":303,"type":"F"}]}},{"acc":"Q9HC35","name":"Echinoderm microtubule-associated protein-like 4","sequence":"MDGFAGSLDDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKKSVSSKGQPSPRAVIPMSCITNGSGANRKPSHTSAVSIAGKETLSSAAKSGTEKKKEKPQGQREKKEESHSNDQSPQIRASPSPQPSSQPLQIHRQTPESKNATPTKSIKRPSPAEKSHNSWENSDDSRNKLSKIPSTPKLIPKVTKTADKHKDVIINQEGEYIKMFMRGRPITMFIPSDVDNYDDIRTELPPEKLKLEWAYGYRGKDCRANVYLLPTGKIVYFIASVVVLFNYEERTQRHYLGHTDCVKCLAIHPDKIRIATGQIAGVDKDGRPLQPHVRVWDSVTLSTLQIIGLGTFERGVGCLDFSKADSGVHLCIIDDSNEHMLTVWDWQKKAKGAEIKTTNEVVLAVEFHPTDANTIITCGKSHIFFWTWSGNSLTRKQGIFGKYEKPKFVQCLAFLGNGDVLTGDSGGVMLIWSKTTVEPTPGKGPKGVYQISKQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDHDLNPEREIEVPDQYGTIRAVAEGKADQFLVGTSRNFILRGTFNDGFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCLWNSMEHRLEWTRLVDEPGHCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSIDGTFLAVGSHDNFIYLYVVSENGRKYSRYGRCTGHSSYITHLDWSPDNKYIMSNSGDYEILYWDIPNGCKLIRNRSDCKDIDWTTYTCVLGFQVFGVWPEGSDGTDINALVRSHNRKVIAVADDFCKVHLFQYPCSKAKAPSHKYSAHSSHVTNVSFTHNDSHLISTGGKDMSIIQWKLVEKLSLPQNETVADTTLTKAPVSSTESVIQSNTPTPPPSQPLNETAEEESRISSSPTLLENSLEQTVEPSEDHSEEESEEGSGDLGEPLYEEPCNEISKEQAKATLLEDQQDPSPSS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":64,"region_id":"DP02645r001","start":45,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Only residues 14–44 were visible in the electron density map but most strikingly they formed a trimeric coiled-coil.","type":"Results"}],"curator_id":"vnugnes","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"25740311","version":3,"reference_html":"Microtubule association of EML proteins and the EML4-ALK variant 3 oncoprotein require an N-terminal trimerization domain. <i> Richards MW, O'Regan L, Roth D, Montgomery JM, Straube A, Fry AM, Bayliss R. </i> Biochem J, 2015","date":"2022-06-15T20:56:00.238Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4CGC"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":38,"end":38,"position":"Specific residue"}]}],"released":"2022_06","length":981,"ncbi_taxon_id":9606,"date":"2020-03-13T14:59:21.880Z","organism":"Homo sapiens","features":{"gene3D":[{"start":255,"end":863,"id":"G3DSA:2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"}],"pfam":[{"id":"PF03451","name":"HELP motif","start":255,"end":293},{"id":"PF23409","name":"Echinoderm microtubule-associated protein first beta-propeller","start":301,"end":578},{"id":"PF23414","name":"Echinoderm microtubule-associated protein second beta-propeller","start":595,"end":864}]},"disprot_id":"DP02645","regions_counter":1,"dataset":["Cancer-related proteins"],"UniParc":"UPI000052BFE0","uniref100":"UniRef100_Q9HC35","uniref90":"UniRef90_Q9HC35","uniref50":"UniRef50_Q9HC35","genes":[{"name":{"value":"EML4"},"synonyms":[{"value":"C2orf2"},{"value":"EMAPL4"}]}],"alphafold_very_low_content":0.2803261977573904,"disorder_content":0.020387359836901122,"disprot_consensus":{"full":[{"start":45,"end":64,"type":"D"}],"Structural state":[{"start":45,"end":64,"type":"D"}]}},{"acc":"P23457","name":"3-alpha-hydroxysteroid dehydrogenase","sequence":"MDSISLRVALNDGNFIPVLGFGTTVPEKVAKDEVIKATKIAIDNGFRHFDSAYLYEVEEEVGQAIRSKIEDGTVKREDIFYTSKLWSTFHRPELVRTCLEKTLKSTQLDYVDLYIIHFPMALQPGDIFFPRDEHGKLLFETVDICDTWEAMEKCKDAGLAKSIGVSNFNCRQLERILNKPGLKYKPVCNQVECHLYLNQSKMLDYCKSKDIILVSYCTLGSSRDKTWVDQKSPVLLDDPVLCAIAKKYKQTPALVALRYQLQRGVVPLIRSFNAKRIKELTQVFEFQLASEDMKALDGLNRNFRYNNAKYFDDHPNHPFTDE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":322,"region_id":"DP02646r001","start":312,"term_id":"IDPO:0000002","statement":[{"text":"The final model contains 305 (residues 1−26, 30−221, and 225−311) out of 322 residues in the protein.","type":"Methods"},{"text":"A β-hairpin seals the N-terminal end of the barrel (residues 7−17), while the C-terminus is a 23-residue coil, of which the last 11 residues are disordered.","type":"Results"},{"text":"Although chain breaks are not shown, portions of two loops (residues 27−29 and 222−224) are disordered, as are the C-terminal residues 312−322","type":"Figure"},{"text":"Portions of two loops (residues 27−29 and 222−224) and the C-terminus (residues 312−322) were classified as disordered, and these residues were not included in the model.","type":"Results"},{"text":"Residues 27−29, 222−224, and 312−322 are disordered and were not included in the model.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"8718859","version":2,"reference_html":"Structure of 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase complexed with NADP+. <i> Bennett MJ, Schlegel BP, Jez JM, Penning TM, Lewis M. </i> Biochemistry, 1996","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1LWI"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":322,"ncbi_taxon_id":10116,"date":"2020-03-13T16:53:05.987Z","organism":"Rattus norvegicus","features":{"gene3D":[{"start":1,"end":322,"id":"G3DSA:3.20.20.100","name":"NADP-dependent oxidoreductase domain"}],"pfam":[{"id":"PF00248","name":"Aldo/keto reductase family","start":19,"end":300}]},"disprot_id":"DP02646","regions_counter":1,"dataset":[],"UniParc":"UPI000011251F","uniref100":"UniRef100_P23457","uniref90":"UniRef90_P23457","uniref50":"UniRef50_Q91WR5","genes":[{"name":{"value":"Akr1c9"}}],"alphafold_very_low_content":0.003105590062111801,"disorder_content":0.034161490683229816,"disprot_consensus":{"full":[{"start":312,"end":322,"type":"D"}],"Structural state":[{"start":312,"end":322,"type":"D"}]}},{"acc":"O95278","name":"Laforin","sequence":"MRFRFGVVVPPAVAGARPELLVVGSRPELGRWEPRGAVRLRPAGTAAGDGALALQEPGLWLGEVELAAEEAAQDGAEPGRVDTFWYKFLKREPGGELSWEGNGPHHDRCCTYNENNLVDGVYCLPIGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYSRILPNIWLGSCPRQVEHVTIKLKHELGITAVMNFQTEWDIVQNSSGCNRYPEPMTPDTMIKLYREEGLAYIWMPTPDMSTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAVYIDEEALARAQEDFFQKFGKVRSSVCSL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":79,"region_id":"DP02647r001","start":69,"term_id":"IDPO:0000002","statement":[{"text":"Residues 69–79 were 100% deuterated throughout the DXMS experiment, and these residues were disordered and not modeled in the structure (labeled disordered loop)","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"25544560","version":2,"reference_html":"Structural mechanism of laforin function in glycogen dephosphorylation and lafora disease. <i> Raththagala M, Brewer MK, Parker MW, Sherwood AR, Wong BK, Hsu S, Bridges TM, Paasch BC, Hellman LM, Husodo S, Meekins DA, Taylor AO, Turner BD, Auger KD, Dukhande VV, Chakravarthy S, Sanz P, Woods VL, Li S, Vander Kooi CW, Gentry MS. </i> Mol Cell, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4RKK"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":331,"ncbi_taxon_id":9606,"date":"2020-03-13T17:14:46.841Z","organism":"Homo sapiens","features":{"gene3D":[{"start":5,"end":118,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":137,"end":329,"id":"G3DSA:3.90.190.10","name":"Protein tyrosine phosphatase superfamily"}],"pfam":[{"id":"PF00686","name":"Starch binding domain","start":19,"end":105},{"id":"PF00782","name":"Dual specificity phosphatase, catalytic domain","start":176,"end":303}]},"disprot_id":"DP02647","regions_counter":1,"dataset":["Age-related disorders proteins"],"UniParc":"UPI00004FD228","uniref100":"UniRef100_O95278","uniref90":"UniRef90_O95278","uniref50":"UniRef50_O95278","genes":[{"name":{"value":"EPM2A"}}],"alphafold_very_low_content":0.015105740181268883,"disorder_content":0.03323262839879154,"disprot_consensus":{"full":[{"start":69,"end":79,"type":"D"}],"Structural state":[{"start":69,"end":79,"type":"D"}]}},{"acc":"Q8GXX0","name":"FAD-linked sulfhydryl oxidase ERV1","sequence":"MGEKPWQPLLQSFEKLSNCVQTHLSNFIGIKNTPPSSQSTIQNPIISLDSSPPIATNSSSLQKLPLKDKSTGPVTKEDLGRATWTFLHTLAAQYPEKPTRQQKKDVKELMTILSRMYPCRECADHFKEILRSNPAQAGSQEEFSQWLCHVHNTVNRSLGKLVFPCERVDARWGKLECEQKSCDLHGTSMDF","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":191,"region_id":"DP02648r001","start":174,"term_id":"IDPO:0000002","statement":[{"text":"The flexibility of the carboxy-terminal tail of AtErv1 in the crystal structure and the requirement for the shuttle disulfide in activity assays led us to speculate that the shuttle disulfide region may be modular and sufficient for substrate recognition.","type":"Results"},{"text":"When the carboxy-terminal 18 residues of AtErv1 were not seen in the electron density maps, we sought to determine if they were present in the crystals or if the protein had suffered proteolytic degradation during crystallization.","type":"Results"},{"text":"Nevertheless, the AtErv1 crystal structure provides further support for the general flexibility of shuttle disulfide regions of eukaryotic sulfhydryl oxidases and, coupled with mutagenesis, confirms that dynamic polypeptide segments determine the substrate specificities and reaction rates of the ERV/ALR sulfhydryl oxidases.","type":"Discussion"},{"text":"In addition, both have a second disulfide bond on a flexible loop or tail of the protein, positioned so that it can either approach the active-site disulfide or extend into solvent.","type":"Introduction"},{"text":"The AtErv1 shuttle disulfide is in a region of the structure that is disordered and thus apparently mobile and exposed. This feature may facilitate access of protein substrates to the shuttle disulfide.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16893552","version":2,"reference_html":"Gain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering of the shuttle disulfide. <i> Vitu E, Bentzur M, Lisowsky T, Kaiser CA, Fass D. </i> J Mol Biol, 2006","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2HJ3"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":191,"region_id":"DP02648r002","start":174,"term_id":"GO:0098772","statement":[{"text":"The flexibility of the carboxy-terminal tail of AtErv1 in the crystal structure and the requirement for the shuttle disulfide in activity assays led us to speculate that the shuttle disulfide region may be modular and sufficient for substrate recognition.","type":"Results"},{"text":"When the carboxy-terminal 18 residues of AtErv1 were not seen in the electron density maps, we sought to determine if they were present in the crystals or if the protein had suffered proteolytic degradation during crystallization.","type":"Results"},{"text":"Nevertheless, the AtErv1 crystal structure provides further support for the general flexibility of shuttle disulfide regions of eukaryotic sulfhydryl oxidases and, coupled with mutagenesis, confirms that dynamic polypeptide segments determine the substrate specificities and reaction rates of the ERV/ALR sulfhydryl oxidases.","type":"Discussion"},{"text":"The shuttle disulfide is required for oxidation of protein substrates by AtErv1","type":"Results"},{"text":"Although the location and context of this \"shuttle\" disulfide differs among family members, it is proposed to perform the same basic function of mediating electron transfer from substrate to the enzyme active site. We have determined by X-ray crystallography the structure of AtErv1, an ERV/ALR enzyme that contains a Cys-X4-Cys shuttle disulfide and oxidizes thioredoxin in vitro, and compared it to ScErv2, which has a Cys-X-Cys shuttle and does not oxidize thioredoxin at an appreciable rate. The AtErv1 shuttle disulfide is in a region of the structure that is disordered and thus apparently mobile and exposed. This feature may facilitate access of protein substrates to the shuttle disulfide. To test whether the shuttle disulfide region is modular and can confer on other enzymes oxidase activity toward new substrates, we generated chimeric enzyme variants combining shuttle disulfide and core elements from AtErv1 and ScErv2 and monitored oxidation of thioredoxin by the chimeras. We found that the AtErv1 shuttle disulfide region could indeed confer thioredoxin oxidase activity on the ScErv2 core. ","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16893552","version":3,"reference_html":"Gain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering of the shuttle disulfide. <i> Vitu E, Bentzur M, Lisowsky T, Kaiser CA, Fass D. </i> J Mol Biol, 2006","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2HJ3"}],"term_name":"molecular function regulator","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","length":191,"ncbi_taxon_id":3702,"date":"2020-03-13T17:42:21.824Z","organism":"Arabidopsis thaliana","features":{"gene3D":[{"start":59,"end":183,"id":"G3DSA:1.20.120.310","name":"ERV/ALR sulfhydryl oxidase domain"}],"pfam":[{"id":"PF04777","name":"Erv1 / Alr family","start":81,"end":172}]},"disprot_id":"DP02648","regions_counter":2,"dataset":[],"UniParc":"UPI000000C122","uniref100":"UniRef100_Q8GXX0","uniref90":"UniRef90_Q8GXX0","uniref50":"UniRef50_Q8GXX0","genes":[{"name":{"value":"ERV1"},"orfNames":[{"value":"F10F5.3"}],"olnNames":[{"value":"At1g49880"}]}],"alphafold_very_low_content":0.18324607329842932,"disorder_content":0.09424083769633508,"disprot_consensus":{"full":[{"start":174,"end":191,"type":"D"}],"Structural state":[{"start":174,"end":191,"type":"D"}],"Molecular function":[{"start":174,"end":191,"type":"F"}]}},{"acc":"P01023","name":"Alpha-2-macroglobulin","sequence":"MGKNKLLHPSLVLLLLVLLPTDASVSGKPQYMVLVPSLLHTETTEKGCVLLSYLNETVTVSASLESVRGNRSLFTDLEAENDVLHCVAFAVPKSSSNEEVMFLTVQVKGPTQEFKKRTTVMVKNEDSLVFVQTDKSIYKPGQTVKFRVVSMDENFHPLNELIPLVYIQDPKGNRIAQWQSFQLEGGLKQFSFPLSSEPFQGSYKVVVQKKSGGRTEHPFTVEEFVLPKFEVQVTVPKIITILEEEMNVSVCGLYTYGKPVPGHVTVSICRKYSDASDCHGEDSQAFCEKFSGQLNSHGCFYQQVKTKVFQLKRKEYEMKLHTEAQIQEEGTVVELTGRQSSEITRTITKLSFVKVDSHFRQGIPFFGQVRLVDGKGVPIPNKVIFIRGNEANYYSNATTDEHGLVQFSINTTNVMGTSLTVRVNYKDRSPCYGYQWVSEEHEEAHHTAYLVFSPSKSFVHLEPMSHELPCGHTQTVQAHYILNGGTLLGLKKLSFYYLIMAKGGIVRTGTHGLLVKQEDMKGHFSISIPVKSDIAPVARLLIYAVLPTGDVIGDSAKYDVENCLANKVDLSFSPSQSLPASHAHLRVTAAPQSVCALRAVDQSVLLMKPDAELSASSVYNLLPEKDLTGFPGPLNDQDNEDCINRHNVYINGITYTPVSSTNEKDMYSFLEDMGLKAFTNSKIRKPKMCPQLQQYEMHGPEGLRVGFYESDVMGRGHARLVHVEEPHTETVRKYFPETWIWDLVVVNSAGVAEVGVTVPDTITEWKAGAFCLSEDAGLGISSTASLRAFQPFFVELTMPYSVIRGEAFTLKATVLNYLPKCIRVSVQLEASPAFLAVPVEKEQAPHCICANGRQTVSWAVTPKSLGNVNFTVSAEALESQELCGTEVPSVPEHGRKDTVIKPLLVEPEGLEKETTFNSLLCPSGGEVSEELSLKLPPNVVEESARASVSVLGDILGSAMQNTQNLLQMPYGCGEQNMVLFAPNIYVLDYLNETQQLTPEIKSKAIGYLNTGYQRQLNYKHYDGSYSTFGERYGRNQGNTWLTAFVLKTFAQARAYIFIDEAHITQALIWLSQRQKDNGCFRSSGSLLNNAIKGGVEDEVTLSAYITIALLEIPLTVTHPVVRNALFCLESAWKTAQEGDHGSHVYTKALLAYAFALAGNQDKRKEVLKSLNEEAVKKDNSVHWERPQKPKAPVGHFYEPQAPSAEVEMTSYVLLAYLTAQPAPTSEDLTSATNIVKWITKQQNAQGGFSSTQDTVVALHALSKYGAATFTRTGKAAQVTIQSSGTFSSKFQVDNNNRLLLQQVSLPELPGEYSMKVTGEGCVYLQTSLKYNILPEKEEFPFALGVQTLPQTCDEPKAHTSFQISLSVSYTGSRSASNMAIVDVKMVSGFIPLKPTVKMLERSNHVSRTEVSSNHVLIYLDKVSNQTLSLFFTVLQDVPVRDLKPAIVKVYDYYETDEFAIAEYNAPCSKDLGNA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":728,"region_id":"DP02649r001","start":690,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"At this point, the polypeptide enters the 39‐residue bait‐region segment (P690–T728), which is disordered.","type":"Article"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22290936","version":2,"reference_html":"The crystal structure of human α2-macroglobulin reveals a unique molecular cage. <i> Marrero A, Duquerroy S, Trapani S, Goulas T, Guevara T, Andersen GR, Navaza J, Sottrup-Jensen L, Gomis-Rüth FX. </i> Angew Chem Int Ed Engl, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4ACQ"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-04T10:07:57.336Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":728,"region_id":"DP02649r003","start":690,"term_id":"GO:0098772","unpublished":true,"statement":[{"text":"At this point, the polypeptide enters the 39‐residue bait‐region segment (P690–T728), which is disordered.","type":"Article"},{"text":"This intrinsic flexibility is in accordance with a function as a universal bait for endopeptidases that must be freely accessible and prepared to adapt to different types of active‐site cleft.","type":"Article"},{"text":"The α2M tetramer operates through a unique irreversible “venus flytrap” mechanism (Supporting Information, Figure S1a), which “entraps” proteinases in the inhibitor tetramer that remain still active against small substrates or inhibitors.1, 2 Entrapping results from large conformational changes elicited upon cleavage by the proteinase within a multitarget “bait region” and exposition of a buried cysteine–glutamine thioester bond located within a “thioester domain” (TED).","type":"Article"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"22290936","version":3,"reference_html":"The crystal structure of human α2-macroglobulin reveals a unique molecular cage. <i> Marrero A, Duquerroy S, Trapani S, Goulas T, Guevara T, Andersen GR, Navaza J, Sottrup-Jensen L, Gomis-Rüth FX. </i> Angew Chem Int Ed Engl, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"molecular function regulator","curator_orcid":"0000-0002-0341-4888","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-04T12:08:34.500Z"},"term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":683,"end":700,"reference_id":"2476433","reference_source":"pmid","reference_html":"The alpha-macroglobulin bait region. Sequence diversity and localization of cleavage sites for proteinases in five mammalian alpha-macroglobulins. <i> Sottrup-Jensen L, Sand O, Kristensen L, Fey GH. </i> J Biol Chem, 1989","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP02649r004","statement":[{"text":"The α-macroglobulin bait region is located equivalently with resi\ndues 666-706 in human α2-macroglobulin.","type":"Abstract"},{"text":"Upon incubation with chymotryspin two new NH2-terminal sequences, 1 (minor) and 2 (major) were seen (Table 2A). In an experiment where the incubation period was 5 min only sequence 2 was found (not shown), demonstrating that chymotrypsin primarly cleaves at Tyr(682)-Gly (numbering of human α2M), and that cleavage at Tyr(700)-Asn is secondary. As described above secondary cleavages were also identified at Tyr(693)-Val and at Leu(705)-Asn.","type":"Results"},{"text":"Although restrictions in motility do exist, residues 683-700 appear to constitute a highly flexible surface loop","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:04:55.716Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":683,"end":700,"reference_id":"2476433","reference_source":"pmid","reference_html":"The alpha-macroglobulin bait region. Sequence diversity and localization of cleavage sites for proteinases in five mammalian alpha-macroglobulins. <i> Sottrup-Jensen L, Sand O, Kristensen L, Fey GH. </i> J Biol Chem, 1989","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000048","term_name":"limited proteolysis display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP02649r005","statement":[{"text":"The α-macroglobulin bait region is located equivalently with resi\ndues 666-706 in human α2-macroglobulin.","type":"Abstract"},{"text":"Although restrictions in motility do exist, residues 683-700 appear to constitute a highly flexible surface loop","type":"Discussion"},{"text":"The partial bait region sequence determined earlier (Sottrup-Jensen et al., 1984c) was completed by analyzing overlapping CNBr fragments and tryptic peptides obtained from PZP or the PZP-chymotrypsin complex (Figs.1-3 and Table 1)","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:04:57.084Z"},"ec_go":"IDA","disprot_namespace":"Disorder function"}],"released":"2023_06","length":1474,"ncbi_taxon_id":9606,"date":"2020-03-16T09:56:47.007Z","organism":"Homo sapiens","features":{"gene3D":[{"start":789,"end":906,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":789,"end":906,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":1337,"end":1474,"id":"G3DSA:2.60.40.690","name":"Alpha-macroglobulin, receptor-binding domain"}],"pfam":[{"id":"PF00207","name":"Alpha-2-macroglobulin family","start":738,"end":828},{"id":"PF01835","name":"MG2 domain","start":129,"end":221},{"id":"PF07677","name":"A-macroglobulin receptor binding domain","start":1375,"end":1464},{"id":"PF07678","name":"A-macroglobulin TED domain","start":948,"end":1264},{"id":"PF07703","name":"Alpha-2-macroglobulin bait region domain","start":459,"end":607},{"id":"PF17789","name":"Macroglobulin domain MG4","start":350,"end":445},{"id":"PF17791","name":"Macroglobulin domain MG3","start":223,"end":312}]},"disprot_id":"DP02649","regions_counter":5,"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000155718","uniref100":"UniRef100_P01023","uniref90":"UniRef90_P01023","uniref50":"UniRef50_P01023","genes":[{"name":{"value":"A2M"},"synonyms":[{"value":"CPAMD5"}],"orfNames":[{"value":"FWP007"}]}],"alphafold_very_low_content":0.05223880597014925,"disorder_content":0.031207598371777476,"disprot_consensus":{"full":[{"start":683,"end":728,"type":"D"}],"Structural state":[{"start":683,"end":728,"type":"D"}],"Molecular function":[{"start":690,"end":728,"type":"F"}],"Disorder function":[{"start":683,"end":700,"type":"F"}]}},{"acc":"P30542","name":"Adenosine receptor A1","sequence":"MPPSISAFQAAYIGIEVLIALVSVPGNVLVIWAVKVNQALRDATFCFIVSLAVADVAVGALVIPLAILINIGPQTYFHTCLMVACPVLILTQSSILALLAIAVDRYLRVKIPLRYKMVVTPRRAAVAIAGCWILSFVVGLTPMFGWNNLSAVERAWAANGSMGEPVIKCEFEKVISMEYMVYFNFFVWVLPPLLLMVLIYLEVFYLIRKQLNKKVSASSGDPQKYYGKELKIAKSLALILFLFALSWLPLHILNCITLFCPSCHKPSILTYIAIFLTHGNSAMNPIVYAFRIQKFRVTFLKIWNDHFRCQPAPPIDEDLPEERPDD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":326,"region_id":"DP02651r001","start":301,"term_id":"IDPO:0000002","statement":[{"text":"The A1R transmembrane domain regions and extracellular and intracellular loops (ECL and ICL, respectively) are well defined, with the exception of 7 residues in ICL3 and the last 25 residues of helix 8.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29925945","version":2,"reference_html":"Structure of the adenosine-bound human adenosine A<sub>1</sub> receptor-G<sub>i</sub> complex. <i> Draper-Joyce CJ, Khoshouei M, Thal DM, Liang YL, Nguyen ATN, Furness SGB, Venugopal H, Baltos JA, Plitzko JM, Danev R, Baumeister W, May LT, Wootten D, Sexton PM, Glukhova A, Christopoulos A. </i> Nature, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6D9H"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2020_12","length":326,"ncbi_taxon_id":9606,"date":"2020-03-16T10:22:11.917Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF00001","name":"7 transmembrane receptor (rhodopsin family)","start":26,"end":288}]},"disprot_id":"DP02651","regions_counter":1,"dataset":["Age-related disorders proteins"],"UniParc":"UPI00000503E1","uniref100":"UniRef100_P30542","uniref90":"UniRef90_P30542","uniref50":"UniRef50_P30542","genes":[{"name":{"value":"ADORA1"}}],"alphafold_very_low_content":0.006134969325153374,"disorder_content":0.07975460122699386,"disprot_consensus":{"full":[{"start":301,"end":326,"type":"D"}],"Structural state":[{"start":301,"end":326,"type":"D"}]}},{"acc":"Q96FQ6","name":"Protein S100-A16","sequence":"MSDCYTELEKAVIVLVENFYKYVSKYSLVKNKISKSSFREMLQKELNHMLSDTGNRKAADKLIQNLDANHDGRISFDEYWTLIGGITGPIAKLIHEQEQQSSS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":71,"region_id":"DP02652r001","start":51,"term_id":"IDPO:0000002","statement":[{"text":"The structure generally shows a well-defined electron density map for the four helices of the two EF-hand motifs of each subunit except for residues from 51 to 71 of monomer D, comprising helix III and part of the loop between helix III and IV. This is consistent with a very high degree of mobility of these regions in the crystal lattice, as also indicated by the B factors.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21046186","version":2,"reference_html":"Structural characterization of human S100A16, a low-affinity calcium binder. <i> Babini E, Bertini I, Borsi V, Calderone V, Hu X, Luchinat C, Parigi G. </i> J Biol Inorg Chem, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3NXA"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":71,"region_id":"DP02652r002","start":51,"term_id":"IDPO:0000002","statement":[{"text":"The structure generally shows a well-defined electron density map for the four helices of the two EF-hand motifs of each subunit except for residues from 51 to 71 of monomer D, comprising helix III and part of the loop between helix III and IV. This is consistent with a very high degree of mobility of these regions in the crystal lattice, as also indicated by the B factors.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21046186","version":2,"reference_html":"Structural characterization of human S100A16, a low-affinity calcium binder. <i> Babini E, Bertini I, Borsi V, Calderone V, Hu X, Luchinat C, Parigi G. </i> J Biol Inorg Chem, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3NXA"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":103,"ncbi_taxon_id":9606,"date":"2020-03-16T10:53:10.438Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF01023","name":"S-100/ICaBP type calcium binding domain","start":8,"end":52}]},"disprot_id":"DP02652","regions_counter":2,"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000135414","uniref100":"UniRef100_Q96FQ6","uniref90":"UniRef90_Q96FQ6","uniref50":"UniRef50_Q96FQ6","genes":[{"name":{"value":"S100A16","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:20441","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:20441"}}]},"synonyms":[{"value":"S100F"}],"orfNames":[{"value":"AAG13"}]}],"alphafold_very_low_content":0,"disorder_content":0.20388349514563106,"disprot_consensus":{"full":[{"start":51,"end":71,"type":"D"}],"Structural state":[{"start":51,"end":71,"type":"D"}]}},{"acc":"P61765","name":"Syntaxin-binding protein 1","sequence":"MAPIGLKAVVGEKIMHDVIKKVKKKGEWKVLVVDQLSMRMLSSCCKMTDIMTEGITIVEDINKRREPLPSLEAVYLITPSEKSVHSLISDFKDPPTAKYRAAHVFFTDSCPDALFNELVKSRAAKVIKTLTEINIAFLPYESQVYSLDSADSFQSFYSPHKAQMKNPILERLAEQIATLCATLKEYPAVRYRGEYKDNALLAQLIQDKLDAYKADDPTMGEGPDKARSQLLILDRGFDPSSPVLHELTFQAMSYDLLPIENDVYKYETSGIGEARVKEVLLDEDDDLWIALRHKHIAEVSQEVTRSLKDFSSSKRMNTGEKTTMRDLSQMLKKMPQYQKELSKYSTHLHLAEDCMKHYQGTVDKLCRVEQDLAMGTDAEGEKIKDPMRAIVPILLDANVSTYDKIRIILLYIFLKNGITEENLNKLIQHAQIPPEDSEIITNMAHLGVPIVTDSTLRRRSKPERKERISEQTYQLSRWTPIIKDIMEDTIEDKLDTKHYPYISTRSSASFSTTAVSARYGHWHKNKAPGEYRSGPRLIIFILGGVSLNEMRCAYEVTQANGKWEVLIGSTHILTPQKLLDTLKKLNKTDEEISS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural transition","ec_ontology":"ECO","end":358,"region_id":"DP02653r001","start":295,"term_id":"IDPO:0000011","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"We identified a conformational change in Munc18-1 domain 3a (residues 295–358); these residues form the predominant interaction site with Sx1 helices H3 and Hc in the Munc18-1–Sx1 closed structure (6). In that structure, Munc18-1 residues 295–358 form a bent hairpin, but in the Munc18-1 structure reported here the hairpin is unfurled, involving a 180° rotation and > 25 Å translation of backbone residues to form an extended antiparallel helical hairpin.","type":"Results"},{"text":"Munc18-1 domain 3a may be flexible in the unbound solution state and adopt an ordered conformation upon interaction with binding partners. We showed that a domain 3a peptide interacts with preformed SNARE complex, as evidenced by an increase in helicity consistent with coiled-coil formation.","type":"Discussion"},{"text":"Domain 3a variability suggests this region may be unstructured in the unbound solution state and possibly adopts a helical structure upon interaction with partners","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21193638","version":2,"reference_html":"Possible roles for Munc18-1 domain 3a and Syntaxin1 N-peptide and C-terminal anchor in SNARE complex formation. <i> Hu SH, Christie MP, Saez NJ, Latham CF, Jarrott R, Lua LH, Collins BM, Martin JL. </i> Proc Natl Acad Sci U S A, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006200","term_name":"disorder to order","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":358,"region_id":"DP02653r002","start":295,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Munc18-1 domain 3a may be flexible in the unbound solution state and adopt an ordered conformation upon interaction with binding partners. We showed that a domain 3a peptide interacts with preformed SNARE complex, as evidenced by an increase in helicity consistent with coiled-coil formation.","type":"Discussion"},{"text":"Domain 3a variability suggests this region may be unstructured in the unbound solution state and possibly adopts a helical structure upon interaction with partners","type":"Results"},{"text":"We used CD spectroscopy to analyze whether a peptide corresponding to this region of Munc18-1 (residues 326–359) could interact with the SNARE ternary complex (formed from Sx1 H3 helix, His-SNAP25, and VAMP2). The CD spectrum from the mixture of peptide and SNARE complex (Fig. 4D) reveals an increase in helicity of about 8% in comparison with the SNARE complex. We would expect an increase in helicity of 11% if all 34 peptide residues form coiled-coil interactions with the helical residues of the SNARE complex. These results indicate that the isolated domain 3a peptide interacts with the SNARE complex and that this interaction induces coiled-coil formation in the peptide.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21193638","version":2,"reference_html":"Possible roles for Munc18-1 domain 3a and Syntaxin1 N-peptide and C-terminal anchor in SNARE complex formation. <i> Hu SH, Christie MP, Saez NJ, Latham CF, Jarrott R, Lua LH, Collins BM, Martin JL. </i> Proc Natl Acad Sci U S A, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006200","term_name":"disorder","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":358,"region_id":"DP02653r003","start":295,"term_id":"GO:0005515","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Munc18-1 domain 3a may be flexible in the unbound solution state and adopt an ordered conformation upon interaction with binding partners. We showed that a domain 3a peptide interacts with preformed SNARE complex, as evidenced by an increase in helicity consistent with coiled-coil formation.","type":"Discussion"},{"text":"Domain 3a variability suggests this region may be unstructured in the unbound solution state and possibly adopts a helical structure upon interaction with partners","type":"Results"},{"text":"We identified a conformational change in Munc18-1 domain 3a (residues 295–358); these residues form the predominant interaction site with Sx1 helices H3 and Hc in the Munc18-1–Sx1 closed structure (6). In that structure, Munc18-1 residues 295–358 form a bent hairpin, but in the Munc18-1 structure reported here the hairpin is unfurled, involving a 180° rotation and > 25 Å translation of backbone residues to form an extended antiparallel helical hairpin.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"circular dichroism evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"21193638","version":3,"reference_html":"Possible roles for Munc18-1 domain 3a and Syntaxin1 N-peptide and C-terminal anchor in SNARE complex formation. <i> Hu SH, Christie MP, Saez NJ, Latham CF, Jarrott R, Lua LH, Collins BM, Martin JL. </i> Proc Natl Acad Sci U S A, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006200","term_name":"protein binding","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":358,"region_id":"DP02653r004","start":295,"term_id":"GO:0060090","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Munc18-1 domain 3a may be flexible in the unbound solution state and adopt an ordered conformation upon interaction with binding partners. We showed that a domain 3a peptide interacts with preformed SNARE complex, as evidenced by an increase in helicity consistent with coiled-coil formation.","type":"Discussion"},{"text":"Domain 3a variability suggests this region may be unstructured in the unbound solution state and possibly adopts a helical structure upon interaction with partners","type":"Results"},{"text":"We identified a conformational change in Munc18-1 domain 3a (residues 295–358); these residues form the predominant interaction site with Sx1 helices H3 and Hc in the Munc18-1–Sx1 closed structure (6). In that structure, Munc18-1 residues 295–358 form a bent hairpin, but in the Munc18-1 structure reported here the hairpin is unfurled, involving a 180° rotation and > 25 Å translation of backbone residues to form an extended antiparallel helical hairpin.","type":"Results"},{"text":"The structure of N-peptide bound rat Munc18-1 adopts an extended domain 3a conformation that may preclude closed Sx1 binding yet remain compatible with binding open Sx1 and SNARE complexes.","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"circular dichroism evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"21193638","version":3,"reference_html":"Possible roles for Munc18-1 domain 3a and Syntaxin1 N-peptide and C-terminal anchor in SNARE complex formation. <i> Hu SH, Christie MP, Saez NJ, Latham CF, Jarrott R, Lua LH, Collins BM, Martin JL. </i> Proc Natl Acad Sci U S A, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006200","term_name":"molecular adaptor activity","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_12","length":594,"ncbi_taxon_id":10116,"date":"2020-03-16T11:09:45.972Z","organism":"Rattus norvegicus","features":{"gene3D":[{"start":135,"end":584,"id":"G3DSA:3.40.50.1910","name":"G3DSA:3.40.50.1910"},{"start":246,"end":359,"id":"G3DSA:3.90.830.10","name":"Syntaxin Binding Protein 1; Chain A, domain 2"},{"start":4,"end":132,"id":"G3DSA:3.40.50.2060","name":"G3DSA:3.40.50.2060"}],"pfam":[{"id":"PF00995","name":"Sec1 family","start":29,"end":580}]},"disprot_id":"DP02653","regions_counter":4,"dataset":[],"UniParc":"UPI0000000ED9","uniref100":"UniRef100_P61764","uniref90":"UniRef90_P61764","uniref50":"UniRef50_P61764","genes":[{"name":{"value":"Stxbp1"},"synonyms":[{"value":"Unc18a"}]}],"alphafold_very_low_content":0.04208754208754209,"disorder_content":0.10774410774410774,"disprot_consensus":{"full":[{"start":295,"end":358,"type":"T"}],"Structural state":[{"start":295,"end":358,"type":"D"}],"Structural transition":[{"start":295,"end":358,"type":"T"}],"Molecular function":[{"start":295,"end":358,"type":"F"}]}},{"acc":"Q9H5I1","name":"Histone-lysine N-methyltransferase SUV39H2","sequence":"MAAVGAEARGAWCVPCLVSLDTLQELCRKEKLTCKSIGITKRNLNNYEVEYLCDYKVVKDMEYYLVKWKGWPDSTNTWEPLQNLKCPLLLQQFSNDKHNYLSQVKKGKAITPKDNNKTLKPAIAEYIVKKAKQRIALQRWQDELNRRKNHKGMIFVENTVDLEGPPSDFYYINEYKPAPGISLVNEATFGCSCTDCFFQKCCPAEAGVLLAYNKNQQIKIPPGTPIYECNSRCQCGPDCPNRIVQKGTQYSLCIFRTSNGRGWGVKTLVKIKRMSFVMEYVGEVITSEEAERRGQFYDNKGITYLFDLDYESDEFTVDAARYGNVSHFVNHSCDPNLQVFNVFIDNLDTRLPRIALFSTRTINAGEELTFDYQMKGSGDISSDSIDHSPAKKRVRTVCKCGAVTCRGYLN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":392,"region_id":"DP02654r001","start":379,"term_id":"IDPO:0000002","statement":[{"text":"Post-SET is fully structured only when bound to the substrate peptide (Figure 2A), or to a small molecule inhibitor [32], but the density is incomplete otherwise (Figure 2B–D). This implies that Post-SET is naturally flexible, which may be important for peptide turn-over, as recently proposed ","type":"Results"},{"text":"A flexible or even disordered state when no co-factor or peptide is bound.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20084102","version":2,"reference_html":"Structural biology of human H3K9 methyltransferases. <i> Wu H, Min J, Lunin VV, Antoshenko T, Dombrovski L, Zeng H, Allali-Hassani A, Campagna-Slater V, Vedadi M, Arrowsmith CH, Plotnikov AN, Schapira M. </i> PLoS One, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2R3A"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":410,"ncbi_taxon_id":9606,"date":"2020-03-16T12:13:41.297Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF00385","name":"Chromo (CHRromatin Organisation MOdifier) domain","start":47,"end":94},{"id":"PF00856","name":"SET domain","start":262,"end":373},{"id":"PF05033","name":"Pre-SET motif","start":148,"end":242}]},"disprot_id":"DP02654","regions_counter":1,"dataset":[],"UniParc":"UPI0000136177","uniref100":"UniRef100_Q9H5I1","uniref90":"UniRef90_Q9H5I1","uniref50":"UniRef50_Q9H5I1","genes":[{"name":{"value":"SUV39H2"},"synonyms":[{"value":"KMT1B"}]}],"alphafold_very_low_content":0.05853658536585366,"disorder_content":0.03414634146341464,"disprot_consensus":{"full":[{"start":379,"end":392,"type":"D"}],"Structural state":[{"start":379,"end":392,"type":"D"}]}},{"acc":"Q8ZQC8","name":"Secreted effector protein sopD2","sequence":"MPVTLSFGNRHNYEINHSRLARLMSPDKEEALYMGVWDRFKDCFRTHKKQEVLEVLYTLIHGCERENQAELNVDITGMEKIHAFTQLKEYANPSQQDRFVMRFDMNQTQVLFEIDGKVIDKCNLHRLLNVSENCIFKVMEEDEEELFLKICIKYGEKISRYPELLEGFANKLKDAVNEDDDVKDEVYKLMRSGEDRKMECVEWNGTLTEEEKNKLRCLQMGSFNITTQFFKIGYWELEGEVLFDMVHPTLSYLLQAYKPSLSSDLIETNTMLFSDVLNKDYDDYQNNKREIDAILRRIYRSHNNTLFISEKSSCRNMLI","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":35,"region_id":"DP02655r001","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Note that the electron density for the first 75 residues in both proteins is not contiguous and only several helical segments could be modeled","type":"Supplementary material"},{"text":"The residues of the N-terminal segmentare not well defined displaying high flexibility","type":"Supplementary material"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26299973","version":2,"reference_html":"Salmonella Disrupts Host Endocytic Trafficking by SopD2-Mediated Inhibition of Rab7. <i> D'Costa VM, Braun V, Landekic M, Shi R, Proteau A, McDonald L, Cygler M, Grinstein S, Brumell JH. </i> Cell Rep, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5CQ9"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-10T15:38:21.409Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":74,"region_id":"DP02655r002","start":64,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Note that the electron density for the first 75 residues in both proteins is not contiguous and only several helical segments could be modeled","type":"Supplementary material"},{"text":"The residues of the N-terminal segmentare not well defined displaying high flexibility","type":"Supplementary material"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26299973","version":2,"reference_html":"Salmonella Disrupts Host Endocytic Trafficking by SopD2-Mediated Inhibition of Rab7. <i> D'Costa VM, Braun V, Landekic M, Shi R, Proteau A, McDonald L, Cygler M, Grinstein S, Brumell JH. </i> Cell Rep, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5CQ9"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-10T15:38:21.084Z"}}],"released":"2021_12","length":319,"ncbi_taxon_id":99287,"date":"2020-03-16T12:30:20.107Z","organism":"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","features":{"gene3D":[],"pfam":[{"id":"PF11047","name":"Salmonella outer protein D","start":1,"end":319}]},"disprot_id":"DP02655","regions_counter":2,"dataset":["Bacterial virulence-related proteins"],"UniParc":"UPI00000CCFC7","uniref100":"UniRef100_Q8ZQC8","uniref90":"UniRef90_Q8ZQC8","uniref50":"UniRef50_Q8ZQC8","genes":[{"name":{"value":"sopD2"},"olnNames":[{"value":"STM0972"}]}],"alphafold_very_low_content":0.003134796238244514,"disorder_content":0.14420062695924765,"disprot_consensus":{"full":[{"start":1,"end":35,"type":"D"},{"start":64,"end":74,"type":"D"}],"Structural state":[{"start":1,"end":35,"type":"D"},{"start":64,"end":74,"type":"D"}]}},{"acc":"P08294","name":"Extracellular superoxide dismutase [Cu-Zn]","sequence":"MLALLCSCLLLAAGASDAWTGEDSAEPNSDSAEWIRDMYAKVTEIWQEVMQRRDDDGALHAACQVQPSATLDAAQPRVTGVVLFRQLAPRAKLDAFFALEGFPTEPNSSSRAIHVHQFGDLSQGCESTGPHYNPLAVPHPQHPGDFGNFAVRDGSLWRYRAGLAASLAGPHSIVGRAVVVHAGEDDLGRGGNQASVENGNAGRRLACCVVGVCGPGLWERQAREHSERKKRRRESECKAA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":54,"region_id":"DP02656r001","start":19,"term_id":"IDPO:0000002","statement":[{"text":"The N- and C-terminal end regions required for tetramerisation and heparin binding, respectively, are highly flexible.","type":"Abstract"},{"text":"Both the N- and the C-terminal ends are incomplete in the structural model reported here, as there is weak electron density corresponding to these regions (modelling at 0.7σ contour level was not reliable), signifying either a greater flexibility for these parts of the molecule or the possibility that the protein has partially degraded during crystallisation.","type":"Results"},{"text":"The functionally important C- and N-terminal end regions are found to be highly flexible and are not fully visible in the electron density.","type":"Conclusion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19289127","version":2,"reference_html":"The structure of human extracellular copper-zinc superoxide dismutase at 1.7 A resolution: insights into heparin and collagen binding. <i> Antonyuk SV, Strange RW, Marklund SL, Hasnain SS. </i> J Mol Biol, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2JLP"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":54,"region_id":"DP02656r002","start":19,"term_id":"GO:0060090","statement":[{"text":"The N- and C-terminal end regions required for tetramerisation and heparin binding, respectively, are highly flexible.","type":"Abstract"},{"text":"Both the N- and the C-terminal ends are incomplete in the structural model reported here, as there is weak electron density corresponding to these regions (modelling at 0.7σ contour level was not reliable), signifying either a greater flexibility for these parts of the molecule or the possibility that the protein has partially degraded during crystallisation.","type":"Results"},{"text":"The functionally important C- and N-terminal end regions are found to be highly flexible and are not fully visible in the electron density.","type":"Conclusion"},{"text":"Among the missing residues at the N-terminus is Val24, which is known to be involved in oligomerisation of SOD3; in particular, the mutation Val to Asp in tetrameric mouse SOD3 causes it to become dimeric, while the reverse mutation in natively dimeric rat SOD3 converts it to a tetramer","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19289127","version":3,"reference_html":"The structure of human extracellular copper-zinc superoxide dismutase at 1.7 A resolution: insights into heparin and collagen binding. <i> Antonyuk SV, Strange RW, Marklund SL, Hasnain SS. </i> J Mol Biol, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2JLP"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":240,"region_id":"DP02656r004","start":224,"term_id":"GO:0005515","statement":[{"text":"The N- and C-terminal end regions required for tetramerisation and heparin binding, respectively, are highly flexible.","type":"Abstract"},{"text":"Both the N- and the C-terminal ends are incomplete in the structural model reported here, as there is weak electron density corresponding to these regions (modelling at 0.7σ contour level was not reliable), signifying either a greater flexibility for these parts of the molecule or the possibility that the protein has partially degraded during crystallisation.","type":"Results"},{"text":"The functionally important C- and N-terminal end regions are found to be highly flexible and are not fully visible in the electron density.","type":"Conclusion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19289127","version":3,"reference_html":"The structure of human extracellular copper-zinc superoxide dismutase at 1.7 A resolution: insights into heparin and collagen binding. <i> Antonyuk SV, Strange RW, Marklund SL, Hasnain SS. </i> J Mol Biol, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2JLP"}],"term_name":"protein binding","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":240,"region_id":"DP02656r005","start":224,"term_id":"IDPO:0000002","statement":[{"text":"The N- and C-terminal end regions required for tetramerisation and heparin binding, respectively, are highly flexible.","type":"Abstract"},{"text":"Both the N- and the C-terminal ends are incomplete in the structural model reported here, as there is weak electron density corresponding to these regions (modelling at 0.7σ contour level was not reliable), signifying either a greater flexibility for these parts of the molecule or the possibility that the protein has partially degraded during crystallisation.","type":"Results"},{"text":"The functionally important C- and N-terminal end regions are found to be highly flexible and are not fully visible in the electron density.","type":"Conclusion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19289127","version":2,"reference_html":"The structure of human extracellular copper-zinc superoxide dismutase at 1.7 A resolution: insights into heparin and collagen binding. <i> Antonyuk SV, Strange RW, Marklund SL, Hasnain SS. </i> J Mol Biol, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2JLP"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":240,"ncbi_taxon_id":9606,"date":"2020-03-16T14:34:40.239Z","organism":"Homo sapiens","features":{"gene3D":[{"start":57,"end":235,"id":"G3DSA:2.60.40.200","name":"Superoxide dismutase, copper/zinc binding domain"}],"pfam":[{"id":"PF00080","name":"Copper/zinc superoxide dismutase (SODC)","start":78,"end":210}]},"disprot_id":"DP02656","regions_counter":5,"dataset":[],"UniParc":"UPI0000000DE0","uniref100":"UniRef100_P08294","uniref90":"UniRef90_P08294","uniref50":"UniRef50_P08294","genes":[{"name":{"value":"SOD3"}}],"alphafold_very_low_content":0.1,"disorder_content":0.22083333333333333,"disprot_consensus":{"full":[{"start":19,"end":54,"type":"D"},{"start":224,"end":240,"type":"D"}],"Structural state":[{"start":19,"end":54,"type":"D"},{"start":224,"end":240,"type":"D"}],"Molecular function":[{"start":19,"end":54,"type":"F"},{"start":224,"end":240,"type":"F"}]}},{"acc":"O88483","name":"[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial","sequence":"MPAPTQLFFPLVRNCELSRIYGTACYCHHKHLCCSPPYIPQNRLRYTPHPAYATFCRPRENWWQYTQGRRYASTPQKFYLTPPQVNSILKANEYSFKVPEFDGKNVSSILGFDSNQLPANAPIEDRRSAATCLQTRGMLLGVFDGHAGCACSQAVSERLFYYIAVSLLPHETLLEIENAVESGRALLPILQWHKHPNDYFSKEASKLYFNSLRTYWQELIDLNTGESADIDVKEALINAFKRLDNDISLEAQVGDPNSFLNYLVLRVAFSGATACVAHVDGVDLHVANTGDSRAMLGVQEEDGSWSAVTLSNDHNAQNERELERLKLEHPKNEAKSVVKQDRLLGLLMPFRAFGDVKFKWSIDLQKRVIESGPDQLNDNEYTKFIPPNYHTPPYLTAEPEVTYHRLRPQDKFLVLATDGLWETMHRQDVVRIVGEYLTGMHHQQPIAVGGYKVTLGQMHGLLTERRAKMSSVFEDQNAATHLIRHAVGNNEFGAVDHERLSKMLSLPEELARMYRDDITIIVVQFNSHVVGAYQNQEQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":385,"region_id":"DP02657r001","start":375,"term_id":"IDPO:0000002","statement":[{"text":"Some of the solvent-exposed parts of the PDP1c molecule are disordered and not included in the model. These are the residues 111–114, 152–157, 304–314, 374–404 and 418–442 that probably form flexible loops in the PDP1c molecule.","type":"Article"},{"text":"Region 304-314 missing from the model corresponds to region 375-385 of the sequence","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17532339","version":2,"reference_html":"Crystal structure of pyruvate dehydrogenase phosphatase 1 and its functional implications. <i> Vassylyev DG, Symersky J. </i> J Mol Biol, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2PNQ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":475,"region_id":"DP02657r002","start":445,"term_id":"IDPO:0000002","statement":[{"text":"Some of the solvent-exposed parts of the PDP1c molecule are disordered and not included in the model. These are the residues 111–114, 152–157, 304–314, 374–404 and 418–442 that probably form flexible loops in the PDP1c molecule.","type":"Article"},{"text":"Region 374-404 missing from the model corresponds to region 445-475 of the sequence","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17532339","version":2,"reference_html":"Crystal structure of pyruvate dehydrogenase phosphatase 1 and its functional implications. <i> Vassylyev DG, Symersky J. </i> J Mol Biol, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2PNQ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":538,"ncbi_taxon_id":10116,"date":"2020-03-16T15:08:58.626Z","organism":"Rattus norvegicus","features":{"gene3D":[{"start":120,"end":526,"id":"G3DSA:3.60.40.10","name":"PPM-type phosphatase domain"}],"pfam":[{"id":"PF00481","name":"Protein phosphatase 2C","start":203,"end":441}]},"disprot_id":"DP02657","regions_counter":2,"dataset":[],"UniParc":"UPI00001314D1","uniref100":"UniRef100_O88483","uniref90":"UniRef90_O88483","uniref50":"UniRef50_O88483","genes":[{"name":{"value":"Pdp1"},"synonyms":[{"value":"Ppm2c"}]}],"alphafold_very_low_content":0.1449814126394052,"disorder_content":0.07806691449814127,"disprot_consensus":{"full":[{"start":375,"end":385,"type":"D"},{"start":445,"end":475,"type":"D"}],"Structural state":[{"start":375,"end":385,"type":"D"},{"start":445,"end":475,"type":"D"}]}},{"acc":"Q8N807","name":"Protein disulfide-isomerase-like protein of the testis","sequence":"MDLLWMPLLLVAACVSAVHSSPEVNAGVSSIHITKPVHILEERSLLVLTPAGLTQMLNQTRFLMVLFHNPSSKQSRNLAEELGKAVEIMGKGKNGIGFGKVDITIEKELQQEFGITKAPELKLFFEGNRSEPISCKGVVESAALVVWLRRQISQKAFLFNSSEQVAEFVISRPLVIVGFFQDLEEEVAELFYDVIKDFPELTFGVITIGNVIGRFHVTLDSVLVFKKGKIVNRQKLINDSTNKQELNRVIKQHLTDFVIEYNTENKDLISELHIMSHMLLFVSKSSESYGIIIQHYKLASKEFQNKILFILVDADEPRNGRVFKYFRVTEVDIPSVQILNLSSDARYKMPSDDITYESLKKFGRSFLSKNATKHQSSEEIPKYWDQGLVKQLVGKNFNVVVFDKEKDVFVMFYAPWSKKCKMLFPLLEELGRKYQNHSTIIIAKIDVTANDIQLMYLDRYPFFRLFPSGSQQAVLYKGEHTLKGFSDFLESHIKTKIEDEDELLSVEQNEVIEEEVLAEEKEVPMMRKGLPEQQSPELENMTKYVSKLEEPAGKKKTSEEVVVVVAKPKGPPVQKKKPKVKEEL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":31,"region_id":"DP02658r001","start":21,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Although we used recombinant hPDILT protein consisting of amino acids Ser-21–Val-580 for crystal growth (Fig. 2A), only amino acids Ser-32–Lys-495 are clearly distinguished in the final electron density map, covering parts of the N-terminal loop, four thioredoxin-like domains (a, b, b′, and a′), and the x-linker (Fig. 2B).","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29203529","version":2,"reference_html":"Crystal and solution structures of human protein-disulfide isomerase-like protein of the testis (PDILT) provide insight into its chaperone activity. <i> Li H, Yang K, Wang W, Niu Y, Li J, Dong Y, Liu Y, Wang CC, Wang L, Liang H. </i> J Biol Chem, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5XF7"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-03T19:45:46.121Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":44,"region_id":"DP02658r002","start":21,"term_id":"GO:0044183","unpublished":true,"statement":[{"text":"Although we used recombinant hPDILT protein consisting of amino acids Ser-21–Val-580 for crystal growth (Fig. 2A), only amino acids Ser-32–Lys-495 are clearly distinguished in the final electron density map, covering parts of the N-terminal loop, four thioredoxin-like domains (a, b, b′, and a′), and the x-linker (Fig. 2B).","type":"Results"},{"text":"The full-length hPDILT consisting of 584 amino acids divided into 9 regions, including the signal peptide (Met-1–Ser-20), N-terminal loop (Ser-21–Ser-44), a domain (Leu-45–Lys-155), b domain (Ala-156–Thr-255), b′ domain (Asp-256–Lys-369), x-linker (Asn-370–Leu-388), a′ domain (Val-389–Lys-496), C-terminal tail (Ile-497–Val-580), and the ER retrieval peptide KEEL (Lys-581–Leu-584) (Fig. 1A).","type":"Results"},{"text":"Thus, the N-terminal loop and the C-terminal tails are important for the chaperone activity. ","type":"Discussion"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"29203529","version":3,"reference_html":"Crystal and solution structures of human protein-disulfide isomerase-like protein of the testis (PDILT) provide insight into its chaperone activity. <i> Li H, Yang K, Wang W, Niu Y, Li J, Dong Y, Liu Y, Wang CC, Wang L, Liang H. </i> J Biol Chem, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5XF7"}],"term_name":"protein folding chaperone","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-03T19:45:16.694Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":580,"region_id":"DP02658r003","start":496,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Although we used recombinant hPDILT protein consisting of amino acids Ser-21–Val-580 for crystal growth (Fig. 2A), only amino acids Ser-32–Lys-495 are clearly distinguished in the final electron density map, covering parts of the N-terminal loop, four thioredoxin-like domains (a, b, b′, and a′), and the x-linker (Fig. 2B).","type":"Results"},{"text":"The full-length hPDILT consisting of 584 amino acids divided into 9 regions, including the signal peptide (Met-1–Ser-20), N-terminal loop (Ser-21–Ser-44), a domain (Leu-45–Lys-155), b domain (Ala-156–Thr-255), b′ domain (Asp-256–Lys-369), x-linker (Asn-370–Leu-388), a′ domain (Val-389–Lys-496), C-terminal tail (Ile-497–Val-580), and the ER retrieval peptide KEEL (Lys-581–Leu-584) (Fig. 1A).","type":"Results"},{"text":"This result suggests that the C-terminal tail of hPDILT is flexible in the crystal structure.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29203529","version":2,"reference_html":"Crystal and solution structures of human protein-disulfide isomerase-like protein of the testis (PDILT) provide insight into its chaperone activity. <i> Li H, Yang K, Wang W, Niu Y, Li J, Dong Y, Liu Y, Wang CC, Wang L, Liang H. </i> J Biol Chem, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5XF7"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-03T19:45:50.215Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":580,"region_id":"DP02658r004","start":496,"term_id":"GO:0044183","unpublished":true,"statement":[{"text":"Although we used recombinant hPDILT protein consisting of amino acids Ser-21–Val-580 for crystal growth (Fig. 2A), only amino acids Ser-32–Lys-495 are clearly distinguished in the final electron density map, covering parts of the N-terminal loop, four thioredoxin-like domains (a, b, b′, and a′), and the x-linker (Fig. 2B).","type":"Results"},{"text":"The full-length hPDILT consisting of 584 amino acids divided into 9 regions, including the signal peptide (Met-1–Ser-20), N-terminal loop (Ser-21–Ser-44), a domain (Leu-45–Lys-155), b domain (Ala-156–Thr-255), b′ domain (Asp-256–Lys-369), x-linker (Asn-370–Leu-388), a′ domain (Val-389–Lys-496), C-terminal tail (Ile-497–Val-580), and the ER retrieval peptide KEEL (Lys-581–Leu-584) (Fig. 1A).","type":"Results"},{"text":"This result suggests that the C-terminal tail of hPDILT is flexible in the crystal structure.","type":"Results"},{"text":"Thus, the N-terminal loop and the C-terminal tails are important for the chaperone activity.","type":"Discussion"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"29203529","version":3,"reference_html":"Crystal and solution structures of human protein-disulfide isomerase-like protein of the testis (PDILT) provide insight into its chaperone activity. <i> Li H, Yang K, Wang W, Niu Y, Li J, Dong Y, Liu Y, Wang CC, Wang L, Liang H. </i> J Biol Chem, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5XF7"}],"term_name":"protein folding chaperone","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-03T19:45:37.469Z"}}],"released":"2023_12","length":584,"ncbi_taxon_id":9606,"date":"2020-03-16T15:28:44.388Z","organism":"Homo sapiens","features":{"gene3D":[{"start":382,"end":498,"id":"G3DSA:3.40.30.10","name":"Glutaredoxin"},{"start":382,"end":498,"id":"G3DSA:3.40.30.10","name":"Glutaredoxin"},{"start":382,"end":498,"id":"G3DSA:3.40.30.10","name":"Glutaredoxin"}],"pfam":[{"id":"PF00085","name":"Thioredoxin","start":48,"end":149},{"id":"PF00085","name":"Thioredoxin","start":389,"end":490},{"id":"PF13848","name":"Thioredoxin-like domain","start":180,"end":362}]},"disprot_id":"DP02658","regions_counter":4,"dataset":[],"UniParc":"UPI000006DBC2","uniref100":"UniRef100_Q8N807","uniref90":"UniRef90_Q8N807","uniref50":"UniRef50_Q8N807","genes":[{"name":{"value":"PDILT"}}],"alphafold_very_low_content":0.15753424657534246,"disorder_content":0.1643835616438356,"disprot_consensus":{"full":[{"start":21,"end":31,"type":"D"},{"start":32,"end":44,"type":"F"},{"start":496,"end":580,"type":"D"}],"Structural state":[{"start":21,"end":31,"type":"D"},{"start":496,"end":580,"type":"D"}],"Molecular function":[{"start":21,"end":44,"type":"F"},{"start":496,"end":580,"type":"F"}]}},{"acc":"Q91ZW2","name":"GDP-fucose protein O-fucosyltransferase 1","sequence":"MGAAAWAPPHLLLRASFLLLLLLLPLRGRSAGSWDLAGYLLYCPCMGRFGNQADHFLGSLAFAKLLNRTLAVPPWIEYQHHKPPFTNLHVSYQKYFKLEPLQAYHRVVSLEDFMENLAPSHWPPEKRVAYCFEVAAQRSPDKKTCPMKEGNPFGPFWDQFHVSFNKSELFTGISFSASYKEQWTQRFPAKEHPVLALPGAPAQFPVLEEHRELQKYMVWSDEMVRTGEALISAHLVRPYVGIHLRIGSDWKNACAMLKDGTAGSHFMASPQCVGYSRSTATPLTMTMCLPDLKEIQRAVTLWVRALNARSVYIATDSESYVSEIQQLFKDKVRVVSLKPEVAQIDLYILGQADHFIGNCVSSFTAFVKRERDLHGRQSSFFGMDRPSQLRDEF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":267,"region_id":"DP02659r001","start":255,"term_id":"IDPO:0000002","statement":[{"text":"Twenty-nine POFUT1 residues belonging to three segments (79–87, 255–267, and 275–281) flanking the binding groove are disordered in the POFUT1–GDP binary complex, but ordered, to different degrees, upon EGF-LD binding.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28530709","version":2,"reference_html":"Recognition of EGF-like domains by the Notch-modifying O-fucosyltransferase POFUT1. <i> Li Z, Han K, Pak JE, Satkunarajah M, Zhou D, Rini JM. </i> Nat Chem Biol, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5KY0"},{"db":"PDB","id":"5KXH"},{"db":"PDB","id":"5KY3"},{"db":"PDB","id":"5KY4"},{"db":"PDB","id":"5KY7"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":393,"ncbi_taxon_id":10090,"date":"2020-03-16T16:00:58.449Z","organism":"Mus musculus","features":{"gene3D":[],"pfam":[{"id":"PF10250","name":"GDP-fucose protein O-fucosyltransferase","start":39,"end":373}]},"disprot_id":"DP02659","regions_counter":1,"dataset":[],"UniParc":"UPI000000B9A1","uniref100":"UniRef100_Q91ZW2","uniref90":"UniRef90_Q91ZW2","uniref50":"UniRef50_Q9H488","genes":[{"name":{"value":"Pofut1"}}],"alphafold_very_low_content":0.061068702290076333,"disorder_content":0.03307888040712468,"disprot_consensus":{"full":[{"start":255,"end":267,"type":"D"}],"Structural state":[{"start":255,"end":267,"type":"D"}]}},{"acc":"Q9SKB2","name":"Leucine-rich repeat receptor-like serine/threonine/tyrosine-protein kinase SOBIR1","sequence":"MAVPTGSANLFLRPLILAVLSFLLLSSFVSSVEWLDIDSSDLKALQVIETELGVNSQRSSASDVNPCGRRGVFCERRHSATTGEYVLRVTRLVYRSRSLTGTISPVIGMLSELKELTLSNNQLVNAVPVDILSCKQLEVLDLRKNRFSGQIPGNFSSLSRLRILDLSSNKLSGNLNFLKNLRNLENLSVANNLFSGKIPEQIVSFHNLRFFDFSGNRYLEGPAPVMSSIKLQTSPHQTRHILAETPTSSPTNKPNNSTTSKAPKGAPKPGKLKKKKKKSKKKKVAAWILGFVVGAIGGTISGFVFSVLFKLIIQAIRGSEKPPGPSIFSPLIKKAEDLAFLENEEALASLEIIGRGGCGEVFKAELPGSNGKIIAVKKVIQPPKDADELTDEDSKFLNKKMRQIRSEINTVGHIRHRNLLPLLAHVSRPECHYLVYEYMEKGSLQDILTDVQAGNQELMWPARHKIALGIAAGLEYLHMDHNPRIIHRDLKPANVLLDDDMEARISDFGLAKAMPDAVTHITTSHVAGTVGYIAPEFYQTHKFTDKCDIYSFGVILGILVIGKLPSDEFFQHTDEMSLIKWMRNIITSENPSLAIDPKLMDQGFDEQMLLVLKIACYCTLDDPKQRPNSKDVRTMLSQIKH","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":270,"region_id":"DP02660r001","start":225,"term_id":"IDPO:0000002","statement":[{"text":"The C-terminal cap features a highly positively charged linear motif which was found to be largely disordered in this structure.","type":"Abstract"},{"text":"In line with this, the C-terminal capping domain, which in plant LRR-RKs is normally terminated by a well defined disulfide bond (Hohmann et al., 2017), is found to be largely disordered in our SOBIR1 structure","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"31063151","version":2,"reference_html":"Crystal structure of the leucine-rich repeat ectodomain of the plant immune receptor kinase SOBIR1. <i> Hohmann U, Hothorn M. </i> Acta Crystallogr D Struct Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6R1H"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":641,"ncbi_taxon_id":3702,"date":"2020-03-16T18:41:41.951Z","organism":"Arabidopsis thaliana","features":{"gene3D":[{"start":38,"end":242,"id":"G3DSA:3.80.10.10","name":"Ribonuclease Inhibitor"}],"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":350,"end":632},{"id":"PF00560","name":"Leucine Rich Repeat","start":183,"end":202},{"id":"PF13855","name":"Leucine rich repeat","start":112,"end":171}]},"disprot_id":"DP02660","regions_counter":1,"dataset":[],"UniParc":"UPI0000052A13","uniref100":"UniRef100_Q9SKB2","uniref90":"UniRef90_Q9SKB2","uniref50":"UniRef50_Q9SKB2","genes":[{"name":{"value":"SOBIR1"},"synonyms":[{"value":"EVR"}],"orfNames":[{"value":"F20M17.8"}],"olnNames":[{"value":"At2g31880"}]}],"alphafold_very_low_content":0.11544461778471139,"disorder_content":0.0717628705148206,"disprot_consensus":{"full":[{"start":225,"end":270,"type":"D"}],"Structural state":[{"start":225,"end":270,"type":"D"}]}},{"acc":"Q6ZVN8","name":"Hemojuvelin","sequence":"MGEPGQSPSPRSSHGSPPTLSTLTLLLLLCGHAHSQCKILRCNAEYVSSTLSLRGGGSSGALRGGGGGGRGGGVGSGGLCRALRSYALCTRRTARTCRGDLAFHSAVHGIEDLMIQHNCSRQGPTAPPPPRGPALPGAGSGLPAPDPCDYEGRFSRLHGRPPGFLHCASFGDPHVRSFHHHFHTCRVQGAWPLLDNDFLFVQATSSPMALGANATATRKLTIIFKNMQECIDQKVYQAEVDNLPVAFEDGSINGGDRPGGSSLSIQTANPGNHVEIQAAYIGTTIIIRQTAGQLSFSIKVAEDVAMAFSAEQDLQLCVGGCPPSQRLSRSERNRRGAITIDTARRLCKEGLPVEDAYFHSCVFDVLISGDPNFTVAAQAALEDARAFLPDLEKLHLFPSDAGVPLSSATLLAPLLSGLFVLWLCIQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":145,"region_id":"DP02661r001","start":130,"term_id":"IDPO:0000002","statement":[{"text":"This resulted in a well-defined model for the RGMCND–BMP2 complex that included two molecules of RGMC (residues Q36–P129) bound to a disulfide linked BMP2 dimer (residues K293–R396)","type":"Methods"},{"text":"Each RGMBND is connected to the RGMB C-terminal domain (RGMBCD) via a disordered 15 amino acid linker not visible in the electron density map.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"25938661","version":2,"reference_html":"Repulsive guidance molecule is a structural bridge between neogenin and bone morphogenetic protein. <i> Healey EG, Bishop B, Elegheert J, Bell CH, Padilla-Parra S, Siebold C. </i> Nat Struct Mol Biol, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4UI1"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":145,"region_id":"DP02661r002","start":130,"term_id":"IDPO:0000033","statement":[{"text":"Each RGMBND is connected to the RGMB C-terminal domain (RGMBCD) via a disordered 15 amino acid linker not visible in the electron density map.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"25938661","version":3,"reference_html":"Repulsive guidance molecule is a structural bridge between neogenin and bone morphogenetic protein. <i> Healey EG, Bishop B, Elegheert J, Bell CH, Padilla-Parra S, Siebold C. </i> Nat Struct Mol Biol, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4UI1"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","length":426,"ncbi_taxon_id":9606,"date":"2020-03-16T19:20:01.827Z","organism":"Homo sapiens","features":{"gene3D":[{"start":173,"end":326,"id":"G3DSA:3.40.1000.10","name":"Mog1/PsbP, alpha/beta/alpha sandwich"}],"pfam":[{"id":"PF06534","name":"Repulsive guidance molecule (RGM) C-terminal domain","start":164,"end":389},{"id":"PF06535","name":"Repulsive guidance molecule (RGM) N-terminal domain","start":37,"end":121}]},"disprot_id":"DP02661","regions_counter":2,"dataset":[],"UniParc":"UPI000013EB58","uniref100":"UniRef100_Q6ZVN8","uniref90":"UniRef90_Q6ZVN8","uniref50":"UniRef50_Q6ZVN8","genes":[{"name":{"value":"HJV","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4887","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4887"}}]},"synonyms":[{"value":"HFE2"},{"value":"RGMC"}]}],"alphafold_very_low_content":0.16901408450704225,"disorder_content":0.03755868544600939,"disprot_consensus":{"full":[{"start":130,"end":145,"type":"D"}],"Structural state":[{"start":130,"end":145,"type":"D"}],"Disorder function":[{"start":130,"end":145,"type":"F"}]}},{"acc":"Q9VXJ0","name":"Peroxisomal multifunctional enzyme type 2","sequence":"MSSSDGKLRYDGRVAVVTGAGAGLGREYALLFAERGAKVVVNDLGGTHSGDGASQRAADIVVDEIRKAGGEAVADYNSVIDGAKVIETAIKAFGRVDILVNNAGILRDRSLVKTSEQDWNLVNDVHLKGSFKCTQAAFPYMKKQNYGRIIMTSSNSGIYGNFGQVNYTAAKMGLIGLANTVAIEGARNNVLCNVIVPTAASRMTEGILPDILFNELKPKLIAPVVAYLCHESCEDNGSYIESAAGWATKLHMVRGKGAVLRPSLDDPVTIEYVKDVWSNVTDMSKAKHLGAIAEASGTLLEVLEKLKEGGGDAIEDAFEFNSKELITYALGIGASVKNAKDMRFLYENDADFAAIPTFFVLPGLLLQMSTDKLLSKALPNSQVDFSNILHGEQYLEIVDDLPTSGTLLTNGKVFDVMDKGSGAVVVTNSESFDESGRLLVRNQSTTFIVGAGKFGGKKDPIAGVVPLQPAPNRQPDATVQYTTSEDQAALYRLSGDKNPLHIDPQMALLAGFKTPILHGLCTLGFSVRAVLAQFADNNPALFKAVKVRFSGPVIPGQTLRVDLWKQGTRINFRTVVVETGKEVISGAYVDLKSSQAKL","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":55,"region_id":"DP02662r001","start":44,"term_id":"IDPO:0000002","statement":[{"text":"In total, 80% of the total sequence was comprised of the clear density that initially enabled the tracking of the correct position of the atoms in the main chain; however, the density was poor in some areas of the map that are known to contain flexible regions in the homologous structures. The missing polypeptide fragments included regions 1–6, 44–55, 88–98 and 200–204 in the dehydrogenase domain, and 373–387, 451–457 and 593–598 in the hydratase domain.","type":"Results"},{"text":"missing region inside the dehydrogenase domain (1–307)","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21320074","version":2,"reference_html":"Peroxisomal multifunctional enzyme type 2 from the fruitfly: dehydrogenase and hydratase act as separate entities, as revealed by structure and kinetics. <i> Haataja TJ, Koski MK, Hiltunen JK, Glumoff T. </i> Biochem J, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3OML"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":98,"region_id":"DP02662r002","start":88,"term_id":"IDPO:0000002","statement":[{"text":"In total, 80% of the total sequence was comprised of the clear density that initially enabled the tracking of the correct position of the atoms in the main chain; however, the density was poor in some areas of the map that are known to contain flexible regions in the homologous structures. The missing polypeptide fragments included regions 1–6, 44–55, 88–98 and 200–204 in the dehydrogenase domain, and 373–387, 451–457 and 593–598 in the hydratase domain.","type":"Results"},{"text":"missing region inside the dehydrogenase domain (1–307)","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21320074","version":2,"reference_html":"Peroxisomal multifunctional enzyme type 2 from the fruitfly: dehydrogenase and hydratase act as separate entities, as revealed by structure and kinetics. <i> Haataja TJ, Koski MK, Hiltunen JK, Glumoff T. </i> Biochem J, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3OML"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":387,"region_id":"DP02662r003","start":373,"term_id":"IDPO:0000002","statement":[{"text":"In total, 80% of the total sequence was comprised of the clear density that initially enabled the tracking of the correct position of the atoms in the main chain; however, the density was poor in some areas of the map that are known to contain flexible regions in the homologous structures. The missing polypeptide fragments included regions 1–6, 44–55, 88–98 and 200–204 in the dehydrogenase domain, and 373–387, 451–457 and 593–598 in the hydratase domain.","type":"Results"},{"text":"missing region inside the hydratase domain (314–598)","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21320074","version":2,"reference_html":"Peroxisomal multifunctional enzyme type 2 from the fruitfly: dehydrogenase and hydratase act as separate entities, as revealed by structure and kinetics. <i> Haataja TJ, Koski MK, Hiltunen JK, Glumoff T. </i> Biochem J, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3OML"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":598,"ncbi_taxon_id":7227,"date":"2020-03-17T09:45:08.035Z","organism":"Drosophila melanogaster","features":{"gene3D":[],"pfam":[{"id":"PF00106","name":"short chain dehydrogenase","start":13,"end":199},{"id":"PF01575","name":"MaoC like domain","start":468,"end":585},{"id":"PF22622","name":"MFE-2 hydratase 2 N-terminal domain","start":318,"end":450}]},"disprot_id":"DP02662","regions_counter":3,"dataset":[],"UniParc":"UPI0000076289","uniref100":"UniRef100_Q9VXJ0","uniref90":"UniRef90_Q9VXJ0","uniref50":"UniRef50_Q9VXJ0","genes":[{"name":{"value":"Mfe2","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0030731","url":"http://flybase.org/reports/FBgn0030731.html"}}]},"orfNames":[{"value":"CG3415"}]}],"alphafold_very_low_content":0.010033444816053512,"disorder_content":0.06354515050167224,"disprot_consensus":{"full":[{"start":44,"end":55,"type":"D"},{"start":88,"end":98,"type":"D"},{"start":373,"end":387,"type":"D"}],"Structural state":[{"start":44,"end":55,"type":"D"},{"start":88,"end":98,"type":"D"},{"start":373,"end":387,"type":"D"}]}},{"acc":"P0A9Q9","name":"Aspartate-semialdehyde dehydrogenase","sequence":"MKNVGFIGWRGMVGSVLMQRMVEERDFDAIRPVFFSTSQLGQAAPSFGGTTGTLQDAFDLEALKALDIIVTCQGGDYTNEIYPKLRESGWQGYWIDAASSLRMKDDAIIILDPVNQDVITDGLNNGIRTFVGGNCTVSLMLMSLGGLFANDLVDWVSVATYQAASGGGARHMRELLTQMGHLYGHVADELATPSSAILDIERKVTTLTRSGELPVDNFGVPLAGSLIPWIDKQLDNGQSREEWKGQAETNKILNTSSVIPVDGLCVRVGALRCHSQAFTIKLKKDVSIPTVEELLAAHNPWAKVVPNDREITMRELTPAAVTGTLTTPVGRLRKLNMGPEFLSAFTVGDQLLWGAAEPLRRMLRQLA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":242,"region_id":"DP02663r001","start":232,"term_id":"IDPO:0000002","statement":[{"text":"The structure is too disordered to model from residues 232 to 242 in subunit A, from  residues 232 to 241 in subunit B, and from residues 233 to 240 in subunit C","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10369777","version":2,"reference_html":"Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis. <i> Hadfield A, Kryger G, Ouyang J, Petsko GA, Ringe D, Viola R. </i> J Mol Biol, 1999","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1BRM"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":367,"ncbi_taxon_id":83333,"date":"2020-03-17T10:11:21.837Z","organism":"Escherichia coli (strain K12)","features":{"gene3D":[],"pfam":[{"id":"PF01118","name":"Semialdehyde dehydrogenase, NAD binding domain","start":3,"end":120},{"id":"PF02774","name":"Semialdehyde dehydrogenase, dimerisation domain","start":144,"end":353}]},"disprot_id":"DP02663","regions_counter":1,"dataset":[],"UniParc":"UPI0000000EAE","uniref100":"UniRef100_P0A9R0","uniref90":"UniRef90_Q8FCR6","uniref50":"UniRef50_Q51344","genes":[{"name":{"value":"asd","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_02121","url":"https://hamap.expasy.org/unirule/MF_02121"}}]},"synonyms":[{"value":"hom"}],"olnNames":[{"value":"b3433"},{"value":"JW3396"}]}],"alphafold_very_low_content":0,"disorder_content":0.02997275204359673,"disprot_consensus":{"full":[{"start":232,"end":242,"type":"D"}],"Structural state":[{"start":232,"end":242,"type":"D"}]}},{"acc":"Q81G39","name":"D-alanine--D-alanyl carrier protein ligase","sequence":"MKLLEQIEKWAAETPDQTAFVWRDAKITYKQLKEDSDALAHWISSEYPDDRSPIMVYGHMQPEMIINFLGCVKAGHAYIPVDLSIPADRVQRIAENSGAKLLLSATAVTVTDLPVRIVSEDNLKDIFFTHKGNTPNPEHAVKGDENFYIIYTSGSTGNPKGVQITYNCLVSFTKWAVEDFNLQTGQVFLNQAPFSFDLSVMDIYPSLVTGGTLWAIDKDMIARPKDLFASLEQSDIQVWTSTPSFAEMCLMEASFSESMLPNMKTFLFCGEVLPNEVARKLIERFPKATIMNTYGPTEATVAVTGIHVTEEVLDQYKSLPVGYCKSDCRLLIMKEDGTIAPDGEKGEIVIVGPSVSVGYLGSPELTEKAFTMIDGERAYKTGDAGYVENGLLFYNGRLDFQIKLHGYRMELEEIEHHLRACSYVEGAVIVPIKKGEKYDYLLAVVVPGEHSFEKEFKLTSAIKKELNERLPNYMIPRKFMYQSSIPMTPNGKVDRKKLLSEVTA","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Bacillus","Bacillus cereus group"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":413,"region_id":"DP02664r001","start":397,"term_id":"IDPO:0000002","statement":[{"text":"The crystal structure of DltA in the absence of any substrate was observed to have a noticeably more disordered pocket for ATP which would explain why DltA has relatively low affinity for ATP in the absence of any D-alanyl carrier.","type":"Abstract"},{"text":"We also determined the structure of BcDltA in the absence of any substrate. This structure is noticeably more disordered than previously reported DltA structures, which may explain the enzyme’s lower affinity to ATP in the absence of the other two substrates.","type":"Introduction"},{"text":"The electron density map indicated several disordered regions (Ser-153 to Pro-159, Pro-363 to Glu-367, Arg-397 to Glu-413, Lys-433 to Tyr-440) with the corresponding regions in the starting model highlighted in magenta in Figure 2B.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"25285205","version":2,"reference_html":"Thiolation-enhanced substrate recognition by D-alanyl carrier protein ligase DltA from Bacillus cereus. <i> Du L, Luo Y. </i> F1000Res, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4PZP"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":413,"region_id":"DP02664r002","start":397,"term_id":"IDPO:0000033","statement":[{"text":"The electron density map indicated several disordered regions (Ser-153 to Pro-159, Pro-363 to Glu-367, Arg-397 to Glu-413, Lys-433 to Tyr-440) with the corresponding regions in the starting model highlighted in magenta in Figure 2B.","type":"Results"},{"text":"The C-terminal part of this flexible inter-domain region also contains a β-hairpin which has been observed to interact with CoA in homologous acetyl-CoA synthetase","type":"Results"},{"text":"The longest such disordered region is between Arg-397 and Glu-413, which contains the inter-domain hinge residue Asp-399, interacts with β-phosphate of ATP, and forms the pantetheine channel. Possibly, this important region remains disordered in the presence of saturating D-alanine, therefore providing an explanation for the similar values between the above mentioned K D (0.43 mM) and the K M (0.46 mM) for ATP, in the presence of saturating D-alanine but in absence of CoA.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"25285205","version":3,"reference_html":"Thiolation-enhanced substrate recognition by D-alanyl carrier protein ligase DltA from Bacillus cereus. <i> Du L, Luo Y. </i> F1000Res, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4PZP"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","length":504,"ncbi_taxon_id":226900,"date":"2020-03-17T10:26:18.545Z","organism":"Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)","features":{"gene3D":[{"start":1,"end":397,"id":"G3DSA:3.40.50.12780","name":"G3DSA:3.40.50.12780"}],"pfam":[{"id":"PF00501","name":"AMP-binding enzyme","start":8,"end":360},{"id":"PF13193","name":"AMP-binding enzyme C-terminal domain","start":413,"end":492}]},"disprot_id":"DP02664","regions_counter":2,"dataset":[],"UniParc":"UPI000018E0EF","uniref100":"UniRef100_B7HHC6","uniref90":"UniRef90_A7GMR0","uniref50":"UniRef50_Q65DH1","genes":[{"name":{"value":"dltA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00593","url":"https://hamap.expasy.org/unirule/MF_00593"}}]},"olnNames":[{"value":"BC_1372"}]}],"alphafold_very_low_content":0,"disorder_content":0.03373015873015873,"disprot_consensus":{"full":[{"start":397,"end":413,"type":"D"}],"Structural state":[{"start":397,"end":413,"type":"D"}],"Disorder function":[{"start":397,"end":413,"type":"F"}]}},{"acc":"Q9Y5C1","name":"Angiopoietin-related protein 3","sequence":"MFTIKLLLFIVPLVISSRIDQDNSSFDSLSPEPKSRFAMLDDVKILANGLLQLGHGLKDFVHKTKGQINDIFQKLNIFDQSFYDLSLQTSEIKEEEKELRRTTYKLQVKNEEVKNMSLELNSKLESLLEEKILLQQKVKYLEEQLTNLIQNQPETPEHPEVTSLKTFVEKQDNSIKDLLQTVEDQYKQLNQQHSQIKEIENQLRRTSIQEPTEISLSSKPRAPRTTPFLQLNEIRNVKHDGIPAECTTIYNRGEHTSGMYAIRPSNSQVFHVYCDVISGSPWTLIQHRIDGSQNFNETWENYKYGFGRLDGEFWLGLEKIYSIVKQSNYVLRIELEDWKDNKHYIEYSFYLGNHETNYTLHLVAITGNVPNAIPENKDLVFSTWDHKAKGHFNCPEGYSGGWWWHDECGENNLNGKYNKPRAKSKPERRRGLSWKSQNGRLYSIKSTKMLIHPTDSESFE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":429,"region_id":"DP02665r001","start":420,"term_id":"IDPO:0000002","statement":[{"text":"There are 3 monomers of Angptl3 in the asymmetric unit. The N-terminal His-tag as well as the C-terminal 6 amino acids are not visible. In addition, there are two regions within the fibrinogen-like domain (Lys389 - His391 and Pro420 - Arg429 in the A-chain) for which the electron density is either missing or not of sufficient quality to allow tracing of the chain, suggesting the presence of flexible loops.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29713054","version":2,"reference_html":"Structures of Angptl3 and Angptl4, modulators of triglyceride levels and coronary artery disease. <i> Biterova E, Esmaeeli M, Alanen HI, Saaranen M, Ruddock LW. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6EUA"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":460,"ncbi_taxon_id":9606,"date":"2020-03-17T11:00:54.930Z","organism":"Homo sapiens","features":{"gene3D":[],"pfam":[{"id":"PF00147","name":"Fibrinogen beta and gamma chains, C-terminal globular domain","start":243,"end":453},{"id":"PF28904","name":"Angiopoietin-like protein 8","start":43,"end":206}]},"disprot_id":"DP02665","regions_counter":1,"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000003722C","uniref100":"UniRef100_Q9Y5C1","uniref90":"UniRef90_Q9Y5C1","uniref50":"UniRef50_Q9Y5C1","genes":[{"name":{"value":"ANGPTL3"},"synonyms":[{"value":"ANGPT5"}],"orfNames":[{"value":"UNQ153/PRO179"}]}],"alphafold_very_low_content":0.15,"disorder_content":0.021739130434782608,"disprot_consensus":{"full":[{"start":420,"end":429,"type":"D"}],"Structural state":[{"start":420,"end":429,"type":"D"}]}},{"acc":"P41780","name":"FAD:protein FMN transferase","sequence":"MKMTFCRAVCLAAAFLLMGCDEAPETTTASPAAQVLEGKTMGTLWRVSVVGIDAKRAAELQTKIQTQLDADDWLLSTYKNDSALMRFNHSRSLAPWPVSEAMADIVTSALRIGAKTDGAMDITVGPLVNLWGFGPDRQPLHIPTPAQIDAAKAKTGLQHLQVIDRAGHQFLQKDLPDLYVDLSTVGEGYAADHLARLMEQEGIARYLVSVGGALSSRGMNAQGQPWRVAIQKPTDRENAVQAIVDINGHGISTSGSYRNYYELDGKRVSHVIDPQTGRPIEHNLVSVTVIAPTALEADGWDTGLMVLGTQKAQEVVRREGLAVFMIMKEGEGFKTWMSPQFKTFLVSDKN","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":31,"region_id":"DP02667r001","start":20,"term_id":"IDPO:0000002","statement":[{"text":"Residues not included due to the absence of any electron density include chain A (20-31, 349-356), chain B (20-32, 234-240, 349-356), chain C (20-25, 349-356), and chain D (20-32, 235-240, 350-356).","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21148731","version":2,"reference_html":"FAD binding by ApbE protein from Salmonella enterica: a new class of FAD-binding proteins. <i> Boyd JM, Endrizzi JA, Hamilton TL, Christopherson MR, Mulder DW, Downs DM, Peters JW. </i> J Bacteriol, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3PND"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":350,"ncbi_taxon_id":99287,"date":"2020-03-17T11:13:39.577Z","organism":"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","features":{"gene3D":[{"start":20,"end":350,"id":"G3DSA:3.10.520.20","name":"G3DSA:3.10.520.20"}],"pfam":[{"id":"PF02424","name":"ApbE family","start":41,"end":324}]},"disprot_id":"DP02667","regions_counter":1,"dataset":[],"UniParc":"UPI0000125C14","uniref100":"UniRef100_P41780","uniref90":"UniRef90_P41780","uniref50":"UniRef50_P41780","genes":[{"name":{"value":"apbE","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9473043","url":"http://www.ncbi.nlm.nih.gov/pubmed/9473043","alternativeUrl":"https://europepmc.org/abstract/MED/9473043"}}]},"olnNames":[{"value":"STM2266"}]}],"alphafold_very_low_content":0.08571428571428572,"disorder_content":0.03428571428571429,"disprot_consensus":{"full":[{"start":20,"end":31,"type":"D"}],"Structural state":[{"start":20,"end":31,"type":"D"}]}},{"acc":"Q44522","name":"6b protein","sequence":"MTVPTWQVRDLRRILRVSELSQHLRQARTDFRSTLSQLVYFNRSVVNPNEYDDEYLLSDQRLTYVYVDEVTAQLCGLNRLLPSNSPAFGTVATAMPPWLLDPQEMNAILQQSCGQGGFVNYHHGPSTNGFFLAILMSQLFIRIRTDVIRGQGYGWYARQGNYVEEGEDNEGIENEEEEEETREFQLSDLIHYPIVALGSCHLTR","taxonomy":["Bacteria","Proteobacteria","Alphaproteobacteria","Rhizobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":179,"region_id":"DP02668r001","start":167,"term_id":"IDPO:0000002","statement":[{"text":"The disordered region—including loop segment 166–182 (AK6b), 167–179 (AB6b), or 70–76 (AtARF)—was not included in the model.","type":"Methods"},{"text":"The acidic loop (residues 164–184), which may serve as a structural scaffold for protein–protein or protein–nucleic acid interaction, is disordered in both the AK6b and AB6b structures.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21156810","version":2,"reference_html":"Molecular insights into plant cell proliferation disturbance by Agrobacterium protein 6b. <i> Wang M, Soyano T, Machida S, Yang JY, Jung C, Chua NH, Yuan YA. </i> Genes Dev, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3AQ2"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":204,"ncbi_taxon_id":373,"date":"2020-03-17T11:25:30.838Z","organism":"Agrobacterium vitis","features":{"gene3D":[],"pfam":[{"id":"PF02027","name":"RolB/RolC glucosidase family","start":1,"end":200}]},"disprot_id":"DP02668","regions_counter":1,"dataset":[],"UniParc":"UPI00000B98AB","uniref100":"UniRef100_Q44522","uniref90":"UniRef90_A0A1B9UDL6","uniref50":"UniRef50_P0A3T1","genes":[{"name":{"value":"6b","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAA54541.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA54541.1"}}]},"orfNames":[{"value":"GN325_27015","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"MVB05405.1","url":"https://www.ebi.ac.uk/ena/browser/view/MVB05405.1"}}]}]}],"alphafold_very_low_content":0.9705882352941176,"disorder_content":0.06372549019607843,"disprot_consensus":{"full":[{"start":167,"end":179,"type":"D"}],"Structural state":[{"start":167,"end":179,"type":"D"}]}},{"acc":"Q57530","name":"6b protein","sequence":"MTVPTWQVRDLRRILRVSELRQHLRQARTDFRSTLSQFVYFNRSVVNPNAYDDEYLLSDQRLTYVYVDEVTAQLCGLNRLLPSNSPAFGTVATAMPPWLLDPQEMNAILQQSCGQGGFVNYHHGPSTNSFFLAILMSQLFIRIRTDVIRGQGYGWYARLGNYVEEGEDNEGIENEEEEEEEEEETREFQLSDLIHYPIVALGSCHLTR","taxonomy":["Bacteria","Proteobacteria","Alphaproteobacteria","Rhizobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":182,"region_id":"DP02669r001","start":166,"term_id":"IDPO:0000002","statement":[{"text":"The disordered region—including loop segment 166–182 (AK6b), 167–179 (AB6b), or 70–76 (AtARF)—was not included in the model.","type":"Methods"},{"text":"The acidic loop (residues 164–184), which may serve as a structural scaffold for protein–protein or protein–nucleic acid interaction, is disordered in both the AK6b and AB6b structures.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21156810","version":2,"reference_html":"Molecular insights into plant cell proliferation disturbance by Agrobacterium protein 6b. <i> Wang M, Soyano T, Machida S, Yang JY, Jung C, Chua NH, Yuan YA. </i> Genes Dev, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3AQ3"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":184,"region_id":"DP02669r005","start":164,"term_id":"GO:0098772","statement":[{"text":"Acidic Region of the 6b Protein Is Required for Callus Formation and Shoot Regeneration on Hormone-Free Medium","type":"Results"},{"text":"The Acidic Region of the 6b Protein Is Essential for the Hormone-Independent Formation of Callus and the Interaction with NtSIP1","type":"Figure"},{"text":"Analysis of the Role of the Acidic Region of 6b in the Interaction of 6b with NtSIP1 Using the Yeast Two-Hybrid System.","type":"Figure"},{"text":"These results showed that the GALDBD-6b protein was capable of activating transcription and that the acidic region of 6b was required for activation","type":"Results"},{"text":"6b Protein Affects the Transcription of Plant Genes","type":"Discussion"},{"text":"The  6b  protein  did  not  include  any  obvious  DNA  binding motif, but it did include an acidic region that is required for its  interaction  with  NtSIP1  and  for  the  activation  of  transcription by 6b. Thus, 6b might function as a transcriptional coactivator/mediator  by  interacting  with  other  proteins  in the  transcriptional  machinery.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"immunodetection assay evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11884686","version":3,"reference_html":"The protein encoded by oncogene 6b from Agrobacterium tumefaciens interacts with a nuclear protein of tobacco. <i> Kitakura S, Fujita T, Ueno Y, Terakura S, Wabiko H, Machida Y. </i> Plant Cell, 2002","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","term_name":"molecular function regulator","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q8W3M8","partner_end":null}],"ec_ontology":"ECO","end":184,"region_id":"DP02669r006","start":164,"term_id":"GO:0005515","statement":[{"text":"The Acidic Region of the 6b Protein Is Essential for the Hormone-Independent Formation of Callus and the Interaction with NtSIP1","type":"Figure"},{"text":"Analysis of the Role of the Acidic Region of 6b in the Interaction of 6b with NtSIP1 Using the Yeast Two-Hybrid System.","type":"Figure"},{"text":"The  6b  protein  did  not  include  any  obvious  DNA  binding motif, but it did include an acidic region that is required for its  interaction  with  NtSIP1  and  for  the  activation  of  transcription by 6b. Thus, 6b might function as a transcriptional coactivator/mediator  by  interacting  with  other  proteins  in the  transcriptional  machinery.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"yeast 2-hybrid evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11884686","version":3,"reference_html":"The protein encoded by oncogene 6b from Agrobacterium tumefaciens interacts with a nuclear protein of tobacco. <i> Kitakura S, Fujita T, Ueno Y, Terakura S, Wabiko H, Machida Y. </i> Plant Cell, 2002","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005805","term_name":"protein binding","curator_orcid":"0000-0002-0341-4888","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q8W3M8","partner_end":null}],"ec_ontology":"ECO","end":184,"region_id":"DP02669r007","start":164,"term_id":"GO:0005515","statement":[{"text":"The Acidic Region of the 6b Protein Is Essential for the Hormone-Independent Formation of Callus and the Interaction with NtSIP1","type":"Figure"},{"text":"NtSIP1 Interacts with 6b in Vitro","type":"Results"},{"text":"The  6b  protein  did  not  include  any  obvious  DNA  binding motif, but it did include an acidic region that is required for its  interaction  with  NtSIP1  and  for  the  activation  of  transcription by 6b. Thus, 6b might function as a transcriptional coactivator/mediator  by  interacting  with  other  proteins  in the  transcriptional  machinery.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"immunodetection assay evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11884686","version":3,"reference_html":"The protein encoded by oncogene 6b from Agrobacterium tumefaciens interacts with a nuclear protein of tobacco. <i> Kitakura S, Fujita T, Ueno Y, Terakura S, Wabiko H, Machida Y. </i> Plant Cell, 2002","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","term_name":"protein binding","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"B1B5X5","partner_end":null}],"ec_ontology":"ECO","end":184,"region_id":"DP02669r008","start":164,"term_id":"GO:0005515","statement":[{"text":"In this study, we report that 6b interacts with the tobacco nuclear protein NtSIP2, whose predicted sequence is significantly similar to that of the TNP1 protein, which is encoded by the transposable element Tam1 of Antirrhinum majus. Most NtSIP2 localizes to the nucleoli, and 6b localizes to a subnucleolar region as well as the nucleoplasm, suggesting their functions in the nucleolus; 6b could act as a histone chaperone similar to the nucleolar histone chaperones of animal cells, nucleophosmin/B23 and nucleolin.","type":"Introduction"},{"text":"Mutant AK6bΔA that lacked the acidic region did not bind NtSIP2 (unpublished data).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18463947","version":3,"reference_html":"Interaction between Agrobacterium tumefaciens oncoprotein 6b and a tobacco nucleolar protein that is homologous to TNP1 encoded by a transposable element of Antirrhinum majus. <i> Kitakura S, Terakura S, Yoshioka Y, Machida C, Machida Y. </i> J Plant Res, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007689","term_name":"protein binding","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Biological process","ec_ontology":"ECO","end":184,"region_id":"DP02669r009","start":164,"term_id":"GO:0051179","statement":[{"text":"In this study, we report that 6b interacts with the tobacco nuclear protein NtSIP2, whose predicted sequence is significantly similar to that of the TNP1 protein, which is encoded by the transposable element Tam1 of Antirrhinum majus. Most NtSIP2 localizes to the nucleoli, and 6b localizes to a subnucleolar region as well as the nucleoplasm, suggesting their functions in the nucleolus; 6b could act as a histone chaperone similar to the nucleolar histone chaperones of animal cells, nucleophosmin/B23 and nucleolin.","type":"Introduction"},{"text":"Mutant AK6bΔA that lacked the acidic region did not bind NtSIP2 (unpublished data).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"fluorescence evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18463947","version":3,"reference_html":"Interaction between Agrobacterium tumefaciens oncoprotein 6b and a tobacco nucleolar protein that is homologous to TNP1 encoded by a transposable element of Antirrhinum majus. <i> Kitakura S, Terakura S, Yoshioka Y, Machida C, Machida Y. </i> J Plant Res, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001249","term_name":"localization","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":184,"region_id":"DP02669r010","start":164,"term_id":"GO:0044183","statement":[{"text":"Protein 6b Has Histone Chaperone–Like Activity","type":"Results"},{"text":"To examine the putative histone chaperone activity of 6b, we first performed supercoiling assays with relaxed and closed-circular DNA, recombinant 6b (or human NAP-1 [hNAP-1]) that had been purified from E. coli, and core histones prepared from HeLa cells.","type":"Results"},{"text":"Our observations indicated that 6b had histone chaperone–like activity in vitro but that the activity of 6b was lower than that of hNAP-1 in our assay system.","type":"Results"},{"text":"As shown in Figure 5C, the mutant derivatives of AK6bΔA and AK6bΔC, which lacked tumorigenic activity (Figure 1B), had no histone chaperone–like activity.","type":"Results"},{"text":"In the AK6bΔA sequence (the 564-bp sequence), the 63-bp sequence corresponding to the entire acidic region of 6b (amino acid residues 164 to 184) was deleted from the 6b coding sequence (the 627-bp sequence corresponding to 208–amino acid residues plus the termination codon).","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"enzymatic activity assay evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"17890376","version":3,"reference_html":"An oncoprotein from the plant pathogen agrobacterium has histone chaperone-like activity. <i> Terakura S, Ueno Y, Tagami H, Kitakura S, Machida C, Wabiko H, Aiba H, Otten L, Tsukagoshi H, Nakamura K, Machida Y. </i> Plant Cell, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005801","term_name":"protein folding chaperone","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","length":208,"ncbi_taxon_id":358,"date":"2020-03-17T11:28:04.366Z","organism":"Rhizobium radiobacter","features":{"gene3D":[],"pfam":[{"id":"PF02027","name":"RolB/RolC glucosidase family","start":1,"end":204}]},"disprot_id":"DP02669","regions_counter":10,"dataset":[],"UniParc":"UPI00000BEEC9","uniref100":"UniRef100_Q57530","uniref90":"UniRef90_A0A1B9UDL6","uniref50":"UniRef50_P0A3T1","genes":[{"name":{"value":"A6b","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAA06313.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAA06313.1"}}]},"synonyms":[{"value":"6b","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAA52221.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA52221.1"}}]}]}],"alphafold_very_low_content":0.052884615384615384,"disorder_content":0.08173076923076923,"disprot_consensus":{"full":[{"start":164,"end":165,"type":"F"},{"start":166,"end":182,"type":"D"},{"start":183,"end":184,"type":"F"}],"Structural state":[{"start":166,"end":182,"type":"D"}],"Molecular function":[{"start":164,"end":184,"type":"F"}],"Biological process":[{"start":164,"end":184,"type":"F"}]}},{"acc":"P15848","name":"Arylsulfatase B","sequence":"MGPRGAASLPRGPGPRRLLLPVVLPLLLLLLLAPPGSGAGASRPPHLVFLLADDLGWNDVGFHGSRIRTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPSCVPLDEKLLPQLLKEAGYTTHMVGKWHLGMYRKECLPTRRGFDTYFGYLLGSEDYYSHERCTLIDALNVTRCALDFRDGEEVATGYKNMYSTNIFTKRAIALITNHPPEKPLFLYLALQSVHEPLQVPEEYLKPYDFIQDKNRHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGQTLAGGNNWPLRGRKWSLWEGGVRGVGFVASPLLKQKGVKNRELIHISDWLPTLVKLARGHTNGTKPLDGFDVWKTISEGSPSPRIELLHNIDPNFVDSSPCPRNSMAPAKDDSSLPEYSAFNTSVHAAIRHGNWKLLTGYPGCGYWFPPPSQYNVSEIPSSDPPTKTLWLFDIDRDPEERHDLSREYPHIVTKLLSRLQFYHKHSVPVYFPAQDPRCDPKATGVWGPWM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":422,"region_id":"DP02670r001","start":406,"term_id":"IDPO:0000002","statement":[{"text":"Although there is up to 20% of the mature form of the protein in the crystals, the invisibility of this loop is probably due to its flexibility in both the precursor and mature forms of the enzyme, since the loop would be visible if it were ordered only in the precursor form.","type":"Results"},{"text":"In the crystal structure of 4-S, the loop from residues 407 to 422, which is anchored at one end by a disulfide bridge (Cys405– Cys447) and terminates at one of the cleavage sites, is not readily visible in the electron density.","type":"Results"}],"curator_id":"fquaglia","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9032078","version":3,"reference_html":"Structure of a human lysosomal sulfatase. <i> Bond CS, Clements PR, Ashby SJ, Collyer CA, Harrop SJ, Hopwood JJ, Guss JM. </i> Structure, 1997","date":"2022-05-13T15:14:45.308Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1FSU"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":533,"ncbi_taxon_id":9606,"date":"2020-03-17T11:42:47.695Z","organism":"Homo sapiens","features":{"gene3D":[{"start":43,"end":531,"id":"G3DSA:3.40.720.10","name":"Alkaline Phosphatase, subunit A"}],"pfam":[{"id":"PF00884","name":"Sulfatase","start":45,"end":361}]},"disprot_id":"DP02670","regions_counter":1,"dataset":["Autophagy-related proteins"],"UniParc":"UPI00001260A3","uniref100":"UniRef100_P15848","uniref90":"UniRef90_P15848","uniref50":"UniRef50_P15848","genes":[{"name":{"value":"ARSB"}}],"alphafold_very_low_content":0.054409005628517824,"disorder_content":0.03189493433395872,"disprot_consensus":{"full":[{"start":406,"end":422,"type":"D"}],"Structural state":[{"start":406,"end":422,"type":"D"}]}},{"acc":"P38111","name":"Serine/threonine-protein kinase MEC1","sequence":"MESHVKYLDELILAIKDLNSGVDSKVQIKKVPTDPSSSQEYAKSLKILNTLIRNLKDQRRNNIMKNDTIFSKTVSALALLLEYNPFLLVMKDSNGNFEIQRLIDDFLNISVLNYDNYHRIWFMRRKLGSWCKACVEFYGKPAKFQLTAHFENTMNLYEQALTEVLLGKTELLKFYDTLKGLYILLYWFTSEYSTFGNSIAFLDSSLGFTKFDFNFQRLIRIVLYVFDSCELAALEYAEIQLKYISLVVDYVCNRTISTALDAPALVCCEQLKFVLTTMHHFLDNKYGLLDNDPTMAKGILRLYSLCISNDFSKCFVDHFPIDQWADFSQSEHFPFTQLTNKALSIVYFDLKRRSLPVEALKYDNKFNIWVYQSEPDSSLKNVTSPFDDRYKQLEKLRLLVLKKFNKTERGTLLKYRVNQLSPGFFQRAGNDFKLILNEASVSIQTCFKTNNITRLTSWTVILGRLACLESEKFSGTLPNSTKDMDNWYVCHLCDIEKTGNPFVRINPNRPEAAGKSEIFRILHSNFLSHPNIDEFSESLLSGILFSLHRIFSHFQPPKLTDGNGQINKSFKLVQKCFMNSNRYLRLLSTRIIPLFNISDSHNSEDEHTATLIKFLQSQKLPVVKENLVIAWTQLTLTTSNDVFDTLLLKLIDIFNSDDYSLRIMMTLQIKNMAKILKKTPYQLLSPILPVLLRQLGKNLVERKVGFQNLIELLGYSSKTILDIFQRYIIPYAIIQYKSDVLSEIAKIMCDGDTSLINQMKVNLLKKNSRQIFAVALVKHGLFSLDILETLFLNRAPTFDKGYITAYLPDYKTLAEITKLYKNSVTKDASDSENANMILCSLRFLITNFEKDKRHGSKYKNINNWTDDQEQAFQKKLQDNILGIFQVFSSDIHDVEGRTTYYEKLRVINGISFLIIYAPKKSIISALAQISICLQTGLGLKEVRYEAFRCWHLLVRHLNDEELSTVIDSLIAFILQKWSEFNGKLRNIVYSILDTLIKEKSDLILKLKPYTTLALVGKPELGILARDGQFARMVNKIRSTTDLIPIFANNLKSSNKYVINQNLDDIEVYLRRKQTERSIDFTPKKVGQTSDITLVLGALLDTSHKFRNLDKDLCEKCAKCISMIGVLDVTKHEFKRTTYSENEVYDLNDSVQTIKFLIWVINDILVPAFWQSENPSKQLFVALVIQESLKYCGLSSESWDMNHKELYPNEAKLWEKFNSVSKTTIYPLLSSLYLAQSWKEYVPLKYPSNNFKEGYKIWVKRFTLDLLKTGTTENHPLHVFSSLIREDDGSLSNFLLPYISLDIIIKAEKGTPYADILNGIIIEFDSIFTCNLEGMNNLQVDSLRMCYESIFRVFEYCKKWATEFKQNYSKLHGTFIIKDTKTTNMLLRIDEFLRTTPSDLLAQRSLETDSFERSALYLEQCYRQNPHDKNQNGQLLKNLQITYEEIGDIDSLDGVLRTFATGNLVSKIEELQYSENWKLAQDCFNVLGKFSDDPKTTTRMLKSMYDHQLYSQIISNSSFHSSDGKISLSPDVKEWYSIGLEAANLEGNVQTLKNWVEQIESLRNIDDREVLLQYNIAKALIAISNEDPLRTQKYIHNSFRLIGTNFITSSKETTLLKKQNLLMKLHSLYDLSFLSSAKDKFEYKSNTTILDYRMERIGADFVPNHYILSMRKSFDQLKMNEQADADLGKTFFTLAQLARNNARLDIASESLMHCLERRLPQAELEFAEILWKQGENDRALKIVQEIHEKYQENSSVNARDRAAVLLKFTEWLDLSNNSASEQIIKQYQDIFQIDSKWDKPYYSIGLYYSRLLERKKAEGYITNGRFEYRAISYFLLAFEKNTAKVRENLPKVITFWLDIAAASISEAPGNRKEMLSKATEDICSHVEEALQHCPTYIWYFVLTQLLSRLLHSHQSSAQIIMHILLSLAVEYPSHILWYITALVNSNSSKRVLRGKHILEKYRQHSQNPHDLVSSALDLTKALTRVCLQDVKSITSRSGKSLEKDFKFDMNVAPSAMVVPVRKNLDIISPLESNSMRGYQPFRPVVSIIRFGSSYKVFSSLKKPKQLNIIGSDGNIYGIMCKKEDVRQDNQYMQFATTMDFLLSKDIASRKRSLGINIYSVLSLREDCGILEMVPNVVTLRSILSTKYESLKIKYSLKSLHDRWQHTAVDGKLEFYMEQVDKFPPILYQWFLENFPDPINWFNARNTYARSYAVMAMVGHILGLGDRHCENILLDIQTGKVLHVDFDCLFEKGKRLPVPEIVPFRLTPNLLDALGIIGTEGTFKKSSEVTLALMRKNEVALMNVIETIMYDRNMDHSIQKALKVLRNKIRGIDPQDGLVLSVAGQTETLIQEATSEDNLSKMYIGWLPFW","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":235,"region_id":"DP02671r001","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The Mec1 N terminus is highly flexible, with more than 200 amino acids (residues 1 to 235) invisible in the structure.","type":"Article"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29191911","version":2,"reference_html":"3.9 Å structure of the yeast Mec1-Ddc2 complex, a homolog of human ATR-ATRIP. <i> Wang X, Ran T, Zhang X, Xin J, Zhang Z, Wu T, Wang W, Cai G. </i> Science, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"5X6O"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"start":33,"end":43,"reference_id":"33169019","reference_source":"pmid","reference_html":"Mechanism of auto-inhibition and activation of Mec1<sup>ATR</sup> checkpoint kinase. <i> Tannous EA, Yates LA, Zhang X, Burgers PM. </i> Nat Struct Mol Biol, 2021","date":"2022-10-03T20:07:42.999Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"11055"},{"db":"PDB","id":"6Z3A"}],"region_id":"DP02671r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q04377"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:33113"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"The electron microscopy evidence of the Mec1-Ddc2 in complex with AMP-PNP shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":1,"end":32,"reference_id":"33169019","reference_source":"pmid","reference_html":"Mechanism of auto-inhibition and activation of Mec1<sup>ATR</sup> checkpoint kinase. <i> Tannous EA, Yates LA, Zhang X, Burgers PM. </i> Nat Struct Mol Biol, 2021","date":"2022-10-03T20:09:20.213Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"11055"},{"db":"PDB","id":"6Z3A"}],"region_id":"DP02671r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q04377"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:33113"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"The electron microscopy evidence of the Mec1-Ddc2 shows this region is ordered when interacting with AMP-PNP.","type":"Curator statement"}]},{"start":44,"end":235,"reference_id":"33169019","reference_source":"pmid","reference_html":"Mechanism of auto-inhibition and activation of Mec1<sup>ATR</sup> checkpoint kinase. <i> Tannous EA, Yates LA, Zhang X, Burgers PM. </i> Nat Struct Mol Biol, 2021","date":"2022-10-03T20:09:37.709Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"11055"},{"db":"PDB","id":"6Z3A"}],"region_id":"DP02671r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q04377"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:33113"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"The electron microscopy evidence of the Mec1-Ddc2 shows this region is ordered when interacting with AMP-PNP.","type":"Curator statement"}]},{"start":1991,"end":2003,"reference_id":"33169019","reference_source":"pmid","reference_html":"Mechanism of auto-inhibition and activation of Mec1<sup>ATR</sup> checkpoint kinase. <i> Tannous EA, Yates LA, Zhang X, Burgers PM. </i> Nat Struct Mol Biol, 2021","date":"2022-10-03T20:10:46.646Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"11055"},{"db":"PDB","id":"6Z3A"}],"region_id":"DP02671r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q04377"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:33113"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"The electron microscopy evidence of the Mec1-Ddc2 in complex with AMP-PNP shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"released":"2023_12","length":2368,"ncbi_taxon_id":559292,"date":"2020-03-17T17:03:47.507Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","features":{"gene3D":[{"start":1666,"end":1924,"id":"G3DSA:1.25.40.10","name":"G3DSA:1.25.40.10"},{"start":2176,"end":2353,"id":"G3DSA:1.10.1070.11","name":"Phosphatidylinositol 3-/4-kinase, catalytic domain"}],"pfam":[{"id":"PF00454","name":"Phosphatidylinositol 3- and 4-kinase","start":2075,"end":2315},{"id":"PF02259","name":"FAT domain","start":1571,"end":1853},{"id":"PF02260","name":"FATC domain","start":2338,"end":2368},{"id":"PF08064","name":"UME (NUC010) domain","start":876,"end":977},{"id":"PF23593","name":"Serine/threonine-protein kinase ATR-like, HEAT repeats","start":1880,"end":1978},{"id":"PF25030","name":"Serine/threonine-protein kinase ATR, M-HEAT region","start":1242,"end":1470},{"id":"PF25385","name":"MEC1-like, HEAT repeats","start":1,"end":725}]},"disprot_id":"DP02671","regions_counter":5,"dataset":[],"UniParc":"UPI000012A1D6","uniref100":"UniRef100_P38111","uniref90":"UniRef90_P38111","uniref50":"UniRef50_P38111","genes":[{"name":{"value":"MEC1"},"synonyms":[{"value":"ESR1"},{"value":"SAD3"}],"orfNames":[{"value":"YBR1012"}],"olnNames":[{"value":"YBR136W"}]}],"alphafold_very_low_content":0.008868243243243243,"disorder_content":0.10472972972972973,"disprot_consensus":{"full":[{"start":1,"end":32,"type":"T"},{"start":33,"end":43,"type":"D"},{"start":44,"end":235,"type":"T"},{"start":1991,"end":2003,"type":"D"}],"Structural state":[{"start":1,"end":235,"type":"D"},{"start":1991,"end":2003,"type":"D"}],"Structural transition":[{"start":1,"end":32,"type":"T"},{"start":44,"end":235,"type":"T"}]}},{"acc":"O35484","name":"Antizyme inhibitor 1","sequence":"MKGFIDDANYSVGLLDEGTNLGNVIDNYVYEHTLTGKNAFFVGDLGKIVKKHSQWQTVVAQIKPFYTVKCNSTPAVLEILAALGTGFACSSKNEMALVQELGVSPENIIFTSPCKQVSQIKYAAKVGVNIMTCDNEIELKKIARNHPNAKVLLHIATEDNIGGEDGNMKFGTTLKNCRHLLECAKELDVQIIGVKFHVSSACKEYQVYVHALSDARCVFDMAGEFGFTMNMLDIGGGFTGTEIQLEEVNHVISPLLDIYFPEGSGIQIISEPGSYYVSSAFTLAVNIIAKKVVENDKFSSGVEKNGSDEPAFVYYMNDGVYGSFASKLSEDLNTIPEVHKKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPAIYFMMSFSDWYEMQDAGITSDAMMKNFFFAPSCIQLSQEDSFSTEA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":448,"region_id":"DP02672r001","start":436,"term_id":"IDPO:0000002","statement":[{"text":"The structure of AzI has several disordered regions. These include the first seven residues at the N terminus, the last 13 residues at the C terminus, and three disordered loops: amino acids 160–167, which connect β7 to α7; 294–310, connecting β11 to β12; and 330–334 between η3 to β13.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18369191","version":2,"reference_html":"Crystallographic and biochemical studies revealing the structural basis for antizyme inhibitor function. <i> Albeck S, Dym O, Unger T, Snapir Z, Bercovich Z, Kahana C. </i> Protein Sci, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3BTN"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":310,"region_id":"DP02672r002","start":294,"term_id":"IDPO:0000002","statement":[{"text":"The structure of AzI has several disordered regions. These include the first seven residues at the N terminus, the last 13 residues at the C terminus, and three disordered loops: amino acids 160–167, which connect β7 to α7; 294–310, connecting β11 to β12; and 330–334 between η3 to β13.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18369191","version":2,"reference_html":"Crystallographic and biochemical studies revealing the structural basis for antizyme inhibitor function. <i> Albeck S, Dym O, Unger T, Snapir Z, Bercovich Z, Kahana C. </i> Protein Sci, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3BTN"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":448,"ncbi_taxon_id":10090,"date":"2020-03-17T18:19:49.347Z","organism":"Mus musculus","features":{"gene3D":[{"start":20,"end":416,"id":"G3DSA:2.40.37.10","name":"Lyase, Ornithine Decarboxylase; Chain A, domain 1"},{"start":44,"end":280,"id":"G3DSA:3.20.20.10","name":"Alanine racemase"}],"pfam":[{"id":"PF02784","name":"Pyridoxal-dependent decarboxylase, pyridoxal binding domain","start":45,"end":278}]},"disprot_id":"DP02672","regions_counter":2,"dataset":[],"UniParc":"UPI00000040A2","uniref100":"UniRef100_O35484","uniref90":"UniRef90_O35484","uniref50":"UniRef50_O35484","genes":[{"name":{"value":"Azin1"},"synonyms":[{"value":"Oazi"},{"value":"Oazin"}]}],"alphafold_very_low_content":0.08258928571428571,"disorder_content":0.06696428571428571,"disprot_consensus":{"full":[{"start":294,"end":310,"type":"D"},{"start":436,"end":448,"type":"D"}],"Structural state":[{"start":294,"end":310,"type":"D"},{"start":436,"end":448,"type":"D"}]}},{"acc":"P11926","name":"Ornithine decarboxylase","sequence":"MNNFGNEEFDCHFLDEGFTAKDILDQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALPRVTPFYAVKCNDSKAIVKTLAATGTGFDCASKTEIQLVQSLGVPPERIIYANPCKQVSQIKYAANNGVQMMTFDSEVELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLRTSRLLLERAKELNIDVVGVSFHVGSGCTDPETFVQAISDARCVFDMGAEVGFSMYLLDIGGGFPGSEDVKLKFEEITGVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKIVLKEQTGSDDEDESSEQTFMYYVNDGVYGSFNCILYDHAHVKPLLQKRPKPDEKYYSSSIWGPTCDGLDRIVERCDLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPTIYYVMSGPAWQLMQQFQNPDFPPEVEEQDASTLPVSCAWESGMKRHRAACASASINV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":461,"region_id":"DP02673r002","start":422,"term_id":"IDPO:0000002","statement":[{"text":"The following residues lacked discernible electron density: 1–18, 31–36, 161–163, 303–308, 345–347, 393–394, and 422–461 in ODC and 220–228 in Az95–2281.","type":"Methods"},{"text":"X-ray crystallography failed to provide structural information about the ODC C-tail because this region is disordered in the structures of both the ODC–Az95–2281 heterodimer and the ODC homodimers","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26305948","version":2,"reference_html":"Structural basis of antizyme-mediated regulation of polyamine homeostasis. <i> Wu HY, Chen SF, Hsieh JY, Chou F, Wang YH, Lin WT, Lee PY, Yu YJ, Lin LY, Lin TS, Lin CL, Liu GY, Tzeng SR, Hung HC, Chan NL. </i> Proc Natl Acad Sci U S A, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4ZGY"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T09:03:42.418Z"}},{"region_id":"DP02673r005","ec_ontology":"ECO","end":18,"term_id":"IDPO:0000014","start":1,"version":2,"statement":[{"text":"This N-terminal segment of ODC (residues 1∼16) is hereafter referred to as the N-latch (Fig. S4 and Fig. 1A), whose conformation is locked in the ODC homodimer by binding across the barrel and sheet domains to mask a prospective proteasome-interacting surface. Az1 binding causes both significant repositioning of the two domains of ODC and rearrangement of the interface contacts (Fig. 2 B and C), which disrupt their interactions with the N-latch and lead to its displacement.","type":"Results"},{"text":"Intriguingly, in ODC–Az95–2281, the fragment becomes fully exposed and thus appears to be suitable for mediating proteasome association due to the disruption of the homodimer interface and an Az1-induced structural transition of the ODC N terminus, which becomes disordered and invisible in the electron density map upon Az1 binding","type":"Results"},{"text":"The N-terminal fragment (residues 1–16, enclosed by black box), which undergoes an order-to-disorder transition upon Az1 binding, is referred to as the N-latch.","type":"Figure"}],"term_name":"order to disorder","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26305948","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4ZGY"}],"term_namespace":"Structural transition","ec_id":"ECO:0005670","curator_id":"fquaglia","reference_html":"Structural basis of antizyme-mediated regulation of polyamine homeostasis. <i> Wu HY, Chen SF, Hsieh JY, Chou F, Wang YH, Lin WT, Lee PY, Yu YJ, Lin LY, Lin TS, Lin CL, Liu GY, Tzeng SR, Hung HC, Chan NL. </i> Proc Natl Acad Sci U S A, 2015","ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T09:05:01.421Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":18,"region_id":"DP02673r006","start":1,"term_id":"IDPO:0000002","statement":[{"text":"MALDI-TOF mass spectrometry and N-terminal sequencing analysis using an ODC protein sample retrieved from dissolved ODC–Az95–2281 crystals both show the intactness of the ODC N terminus (Fig. S3), providing convincing evidence that the exposure of this presumably proteasome-interacting surface of ODC is caused by an Az1-induced order-to-disorder transition of the ODC N-terminal segment (Fig. 2), rather than by an experimental artifact that resulted from nonspecific proteolysis during sample preparation and crystallization.","type":"Results"},{"text":"Intriguingly, in ODC–Az95–2281, the fragment becomes fully exposed and thus appears to be suitable for mediating proteasome association due to the disruption of the homodimer interface and an Az1-induced structural transition of the ODC N terminus, which becomes disordered and invisible in the electron density map upon Az1 binding","type":"Results"},{"text":"The following residues lacked discernible electron density: 1–18, 31–36, 161–163, 303–308, 345–347, 393–394, and 422–461 in ODC and 220–228 in Az95–2281.","type":"Methods"}],"curator_id":"vnugnes","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"26305948","version":3,"reference_html":"Structural basis of antizyme-mediated regulation of polyamine homeostasis. <i> Wu HY, Chen SF, Hsieh JY, Chou F, Wang YH, Lin WT, Lee PY, Yu YJ, Lin LY, Lin TS, Lin CL, Liu GY, Tzeng SR, Hung HC, Chan NL. </i> Proc Natl Acad Sci U S A, 2015","date":"2023-06-14T09:04:21.436Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4ZGY"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P54368"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":461,"region_id":"DP02673r007","start":422,"term_id":"IDPO:0000002","statement":[{"text":"Comparing the spectra of the full-length and truncated homodimers showed that the ODC C-tail is indeed unstructured, being highly flexible and solvent exposed, which gives rise to well-resolved NMR peaks. Moreover, the signals that correspond to the ODC C-tail remained unchanged in the presence of Az95–2281 (Fig. 3B), suggesting that heterodimerization most likely has no effect on the properties of this region.","type":"Results"}],"curator_id":"vnugnes","released":"2023_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"26305948","version":3,"reference_html":"Structural basis of antizyme-mediated regulation of polyamine homeostasis. <i> Wu HY, Chen SF, Hsieh JY, Chou F, Wang YH, Lin WT, Lee PY, Yu YJ, Lin LY, Lin TS, Lin CL, Liu GY, Tzeng SR, Hung HC, Chan NL. </i> Proc Natl Acad Sci U S A, 2015","date":"2023-06-14T08:58:08.173Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":461,"ncbi_taxon_id":9606,"date":"2020-03-17T19:01:36.074Z","organism":"Homo sapiens","features":{"gene3D":[{"start":17,"end":424,"id":"G3DSA:2.40.37.10","name":"Lyase, Ornithine Decarboxylase; Chain A, domain 1"},{"start":44,"end":283,"id":"G3DSA:3.20.20.10","name":"Alanine racemase"}],"pfam":[{"id":"PF00278","name":"Pyridoxal-dependent decarboxylase, C-terminal sheet domain","start":40,"end":44},{"id":"PF00278","name":"Pyridoxal-dependent decarboxylase, C-terminal sheet domain","start":282,"end":387},{"id":"PF02784","name":"Pyridoxal-dependent decarboxylase, pyridoxal binding domain","start":45,"end":281}]},"disprot_id":"DP02673","regions_counter":7,"dataset":["NDDs-related proteins"],"UniParc":"UPI0000156A46","uniref100":"UniRef100_P11926","uniref90":"UniRef90_P11926","uniref50":"UniRef50_P11926","genes":[{"name":{"value":"ODC1"}}],"alphafold_very_low_content":0.10845986984815618,"disorder_content":0.12581344902386118,"disprot_consensus":{"full":[{"start":1,"end":18,"type":"T"},{"start":422,"end":461,"type":"D"}],"Structural state":[{"start":1,"end":18,"type":"D"},{"start":422,"end":461,"type":"D"}],"Structural transition":[{"start":1,"end":18,"type":"T"}]}},{"acc":"P54368","name":"Ornithine decarboxylase antizyme 1","sequence":"MVKSSLQRILNSHCFAREKEGDKPSATIHASRTMPLLSLHSRGGSSSESSRVSLHCCSNPGPGPRWCSDAPHPPLKIPGGRGNSQRDHNLSANLFYSDDRLNVTEELTSNDKTRILNVQSRLTDAKRINWRTVLSGGSLYIEIPGGALPEGSKDSFAVLLEFAEEQLRADHVFICFHKNREDRAALLRTFSFLGFEIVRPGHPLVPKRPDACFMAYTFERESSGEEEE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":125,"region_id":"DP02674r001","start":110,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The following residues were missing in the structure: 1–9, 161–167, 294–310, 342–346, and 433–448 in AzIN and 110–125 and 220–228 in Az1 110–228. ","type":"Methods"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26305948","version":2,"reference_html":"Structural basis of antizyme-mediated regulation of polyamine homeostasis. <i> Wu HY, Chen SF, Hsieh JY, Chou F, Wang YH, Lin WT, Lee PY, Yu YJ, Lin LY, Lin TS, Lin CL, Liu GY, Tzeng SR, Hung HC, Chan NL. </i> Proc Natl Acad Sci U S A, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4ZGZ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":69,"end":92,"reference_id":"26443277","reference_source":"pmid","reference_html":"Structural basis of Ornithine Decarboxylase inactivation and accelerated degradation by polyamine sensor Antizyme1. <i> Wu D, Kaan HY, Zheng X, Tang X, He Y, Vanessa Tan Q, Zhang N, Song H. </i> Sci Rep, 2015","date":"2022-10-03T21:02:12.269Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02674r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P11926"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1051"}],"statement":[{"text":"The PDB of the crystal structure of ODC-PLP-AZ1 ternary complex shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"released":"2023_12","length":228,"ncbi_taxon_id":9606,"date":"2020-03-17T19:20:23.290Z","organism":"Homo sapiens","features":{"gene3D":[{"start":93,"end":228,"id":"G3DSA:3.40.630.60","name":"G3DSA:3.40.630.60"}],"pfam":[{"id":"PF02100","name":"Ornithine decarboxylase antizyme","start":136,"end":216}]},"disprot_id":"DP02674","regions_counter":2,"dataset":[],"UniParc":"UPI0000161BAA","uniref100":"UniRef100_P54368","uniref90":"UniRef90_P54368","uniref50":"UniRef50_P54368","genes":[{"name":{"value":"OAZ1"},"synonyms":[{"value":"OAZ"}]}],"alphafold_very_low_content":0.22807017543859648,"disorder_content":0.17543859649122806,"disprot_consensus":{"full":[{"start":69,"end":92,"type":"D"},{"start":110,"end":125,"type":"D"}],"Structural state":[{"start":69,"end":92,"type":"D"},{"start":110,"end":125,"type":"D"}]}},{"acc":"O14977","name":"Antizyme inhibitor 1","sequence":"MKGFIDDANYSVGLLDEGTNLGNVIDNYVYEHTLTGKNAFFVGDLGKIVKKHSQWQNVVAQIKPFYTVKCNSAPAVLEILAALGTGFACSSKNEMALVQELGVPPENIIYISPCKQVSQIKYAAKVGVNILTCDNEIELKKIARNHPNAKVLLHIATEDNIGGEEGNMKFGTTLKNCRHLLECAKELDVQIIGVKFHVSSACKESQVYVHALSDARCVFDMAGEIGFTMNMLDIGGGFTGTEFQLEEVNHVISPLLDIYFPEGSGVKIISEPGSYYVSSAFTLAVNIIAKKVVENDKFPSGVEKTGSDEPAFMYYMNDGVYGSFASKLSEDLNTIPEVHKKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPAIYYMMSFSDWYEMQDAGITSDSMMKNFFFVPSCIQLSQEDSFSAEA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"creator":"fquaglia","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":310,"region_id":"DP02675r001","start":294,"term_id":"IDPO:0000002","statement":[{"text":"The following residues were missing in the structure: 1–9, 161–167, 294–310, 342–346, and 433–448 in AzIN and 110–125 and 220–228 in Az1 110–228.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26305948","version":2,"reference_html":"Structural basis of antizyme-mediated regulation of polyamine homeostasis. <i> Wu HY, Chen SF, Hsieh JY, Chou F, Wang YH, Lin WT, Lee PY, Yu YJ, Lin LY, Lin TS, Lin CL, Liu GY, Tzeng SR, Hung HC, Chan NL. </i> Proc Natl Acad Sci U S A, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4ZGZ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":448,"region_id":"DP02675r002","start":433,"term_id":"IDPO:0000002","statement":[{"text":"The following residues were missing in the structure: 1–9, 161–167, 294–310, 342–346, and 433–448 in AzIN and 110–125 and 220–228 in Az1 110–228.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26305948","version":2,"reference_html":"Structural basis of antizyme-mediated regulation of polyamine homeostasis. <i> Wu HY, Chen SF, Hsieh JY, Chou F, Wang YH, Lin WT, Lee PY, Yu YJ, Lin LY, Lin TS, Lin CL, Liu GY, Tzeng SR, Hung HC, Chan NL. </i> Proc Natl Acad Sci U S A, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4ZGZ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","length":448,"ncbi_taxon_id":9606,"date":"2020-03-17T19:23:06.345Z","organism":"Homo sapiens","features":{"gene3D":[{"start":20,"end":416,"id":"G3DSA:2.40.37.10","name":"Lyase, Ornithine Decarboxylase; Chain A, domain 1"},{"start":44,"end":280,"id":"G3DSA:3.20.20.10","name":"Alanine racemase"}],"pfam":[{"id":"PF02784","name":"Pyridoxal-dependent decarboxylase, pyridoxal binding domain","start":45,"end":278}]},"disprot_id":"DP02675","regions_counter":2,"dataset":[],"UniParc":"UPI0000130BCC","uniref100":"UniRef100_O14977","uniref90":"UniRef90_O14977","uniref50":"UniRef50_O14977","genes":[{"name":{"value":"AZIN1"},"synonyms":[{"value":"OAZI"},{"value":"OAZIN"}]}],"alphafold_very_low_content":0.060267857142857144,"disorder_content":0.07366071428571429,"disprot_consensus":{"full":[{"start":294,"end":310,"type":"D"},{"start":433,"end":448,"type":"D"}],"Structural state":[{"start":294,"end":310,"type":"D"},{"start":433,"end":448,"type":"D"}]}},{"acc":"Q9HD36","features":{"gene3D":[{"start":5,"end":195,"id":"G3DSA:1.10.437.10","name":"Blc2-like"}],"pfam":[{"id":"PF00452","name":"Apoptosis regulator proteins, Bcl-2 family","start":49,"end":163}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MVDQLRERTTMADPLRERTELLLADYLGYCAREPGTPEPAPSTPEAAVLRSAAARLRQIHRSFFSAYLGYPGNRFELVALMADSVLSDSPGPTWGRVVTLVTFAGTLLERGPLVTARWKKWGFQPRLKEQEGDVARDCQRLVALLSSRLMGQHRAWLQAQGGWDGFCHFFRTPFPLAFWRKQLVQAFLSCLLTTAFIYLWTRLL","length":204,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":121,"region_id":"DP02676r001","start":107,"term_id":"IDPO:0000002","statement":[{"text":"Bcl-B is distinguished from other Bcl-2 family members through an insertion of an unstructured loop between helices α5 and α6.","type":"Abstract"},{"text":"Residues 107–121 are absent from the electron density for Bcl-B, indicating their flexibility.","type":"Results"},{"text":"A point of similarity between Bcl-B and Boo, which differentiates them both from other Bcl-2 proteins, is the presence of the unstructured α5–α6 loop.","type":"Results"},{"text":"Clear and continuous electron density was obtained for residues 2–106, and 122–164 of Bcl-B and 53–76 of Bim, whereas the residues constituting the α5–α6 loop (residues 107–121) lack clear electron density and were presumed disordered.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23235460","version":2,"reference_html":"The restricted binding repertoire of Bcl-B leaves Bim as the universal BH3-only prosurvival Bcl-2 protein antagonist. <i> Rautureau GJ, Yabal M, Yang H, Huang DC, Kvansakul M, Hinds MG. </i> Cell Death Dis, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4B4S"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02676","date":"2020-03-18T11:53:17.629Z","organism":"Homo sapiens","regions_counter":1,"name":"Bcl-2-like protein 10","dataset":[],"UniParc":"UPI000013D0DA","uniref100":"UniRef100_Q9HD36","uniref90":"UniRef90_Q9HD36","uniref50":"UniRef50_Q9HD36","genes":[{"name":{"value":"BCL2L10","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"17532299","url":"http://www.ncbi.nlm.nih.gov/pubmed/17532299","alternativeUrl":"https://europepmc.org/abstract/MED/17532299"}}]},"synonyms":[{"value":"BCL-B","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"22498477","url":"http://www.ncbi.nlm.nih.gov/pubmed/22498477","alternativeUrl":"https://europepmc.org/abstract/MED/22498477"}}]},{"value":"BCLB","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"22233804","url":"http://www.ncbi.nlm.nih.gov/pubmed/22233804","alternativeUrl":"https://europepmc.org/abstract/MED/22233804"}}]},{"value":"BOO","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:993","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:993"}}]},{"value":"DIVA","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:993","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:993"}}]}]}],"alphafold_very_low_content":0.029411764705882353,"disorder_content":0.07352941176470588,"disprot_consensus":{"full":[{"start":107,"end":121,"type":"D"}],"Structural state":[{"start":107,"end":121,"type":"D"}]}},{"acc":"O75936","features":{"gene3D":[{"start":1,"end":97,"id":"G3DSA:3.30.2020.30","name":"G3DSA:3.30.2020.30"},{"start":98,"end":387,"id":"G3DSA:3.60.130.10","name":"Clavaminate synthase-like"}],"pfam":[{"id":"PF02668","name":"Taurine catabolism dioxygenase TauD, TfdA family","start":114,"end":366},{"id":"PF06155","name":"Gamma-butyrobetaine hydroxylase-like, N-terminal","start":15,"end":91}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MACTIQKAEALDGAHLMQILWYDEEESLYPAVWLRDNCPCSDCYLDSAKARKLLVEALDVNIGIKGLIFDRKKVYITWPDEHYSEFQADWLKKRCFSKQARAKLQRELFFPECQYWGSELQLPTLDFEDVLRYDEHAYKWLSTLKKVGIVRLTGASDKPGEVSKLGKRMGFLYLTFYGHTWQVQDKIDANNVAYTTGKLSFHTDYPALHHPPGVQLLHCIKQTVTGGDSEIVDGFNVCQKLKKNNPQAFQILSSTFVDFTDIGVDYCDFSVQSKHKIIELDDKGQVVRINFNNATRDTIFDVPVERVQPFYAALKEFVDLMNSKESKFTFKMNPGDVITFDNWRLLHGRRSYEAGTEISRHLEGAYADWDVVMSRLRILRQRVENGN","length":387,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":198,"region_id":"DP02678r001","start":188,"term_id":"IDPO:0000002","statement":[{"text":"The model was built for all residues except disordered loop regions, which include residues 188–198, 223–227, 351–359 and two C-terminal residues.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20599753","version":2,"reference_html":"Crystal structure of human gamma-butyrobetaine hydroxylase. <i> Tars K, Rumnieks J, Zeltins A, Kazaks A, Kotelovica S, Leonciks A, Sharipo J, Viksna A, Kuka J, Liepinsh E, Dambrova M. </i> Biochem Biophys Res Commun, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3N6W"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","ncbi_taxon_id":9606,"disprot_id":"DP02678","date":"2020-03-18T14:36:43.159Z","organism":"Homo sapiens","regions_counter":1,"name":"Gamma-butyrobetaine dioxygenase","dataset":[],"UniParc":"UPI0000126A4C","uniref100":"UniRef100_O75936","uniref90":"UniRef90_O75936","uniref50":"UniRef50_O75936","genes":[{"name":{"value":"BBOX1"},"synonyms":[{"value":"BBH"},{"value":"BBOX"}]}],"alphafold_very_low_content":0.002583979328165375,"disorder_content":0.028423772609819122,"disprot_consensus":{"full":[{"start":188,"end":198,"type":"D"}],"Structural state":[{"start":188,"end":198,"type":"D"}]}},{"acc":"Q8R464","features":{"gene3D":[{"start":223,"end":308,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":223,"end":308,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":223,"end":308,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"}],"pfam":[{"id":"PF07686","name":"Immunoglobulin V-set domain","start":30,"end":122},{"id":"PF08205","name":"CD80-like C2-set immunoglobulin domain","start":130,"end":206},{"id":"PF13927","name":"Immunoglobulin domain","start":224,"end":295}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MGRARRFQWPLLLLWAAAAGPGTGQEVQTENVTVAEGGVAEITCRLHQYDGSIVVIQNPARQTLFFNGTRALKDERFQLEEFSPRRVRIRLSDARLEDEGGYFCQLYTEDTHHQIATLTVLVAPENPVVEVREQAVEGGEVELSCLVPRSRPAAVLRWYRDRKELKGVSSGQENGKVWSVASTVRFRVDRKDDGGIVICEAQNQALPSGHSKQTQYVLDVQYSPTARIHASQAVVREGDTLVLTCAVTGNPRPNQIRWNRGNESLPERAEAVGETLTLPGLVSADNGTYTCEAANKHGHARALYVLVVYDPGAVVEAQTSVPYAIVGGILALLVFLIICVLVGMVWCSVRQKGSYLTHEASGLDEQGEAREAFLNGGDGHKRKEEFFI","length":388,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":120,"region_id":"DP02679r001","start":25,"term_id":"IDPO:0000002","statement":[{"text":"The Ig1 domain of one mNecl-4 ectodomain (chain C) interacts with mNecl-1 whereas the electron-density of the Ig1 domain of the other mNecl-4 ectodomain (chain A) was essentially missing, indicating that this domain is highly flexible, likely due to the lack of contacts with other molecules in the crystal.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30674679","version":2,"reference_html":"Structure of the heterophilic interaction between the nectin-like 4 and nectin-like 1 molecules. <i> Liu X, An T, Li D, Fan Z, Xiang P, Li C, Ju W, Li J, Hu G, Qin B, Yin B, Wojdyla JA, Wang M, Yuan J, Qiang B, Shu P, Cui S, Peng X. </i> Proc Natl Acad Sci U S A, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5ZO2"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":10090,"disprot_id":"DP02679","date":"2020-03-18T15:25:07.488Z","organism":"Mus musculus","regions_counter":1,"name":"Cell adhesion molecule 4","dataset":[],"UniParc":"UPI0000028443","uniref100":"UniRef100_Q8R464","uniref90":"UniRef90_Q8R464","uniref50":"UniRef50_Q8R464","genes":[{"name":{"value":"Cadm4"},"synonyms":[{"value":"Igsf4c"},{"value":"Necl4"},{"value":"Tsll2"}]}],"alphafold_very_low_content":0.14432989690721648,"disorder_content":0.24742268041237114,"disprot_consensus":{"full":[{"start":25,"end":120,"type":"D"}],"Structural state":[{"start":25,"end":120,"type":"D"}]}},{"acc":"P23280","features":{"gene3D":[{"start":20,"end":280,"id":"G3DSA:3.10.200.10","name":"Alpha carbonic anhydrase"}],"pfam":[{"id":"PF00194","name":"Eukaryotic-type carbonic anhydrase","start":31,"end":278}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MRALVLLLSLFLLGGQAQHVSDWTYSEGALDEAHWPQHYPACGGQRQSPINLQRTKVRYNPSLKGLNMTGYETQAGEFPMVNNGHTVQISLPSTMRMTVADGTVYIAQQMHFHWGGASSEISGSEHTVDGIRHVIEIHIVHYNSKYKSYDIAQDAPDGLAVLAAFVEVKNYPENTYYSNFISHLANIKYPGQRTTLTGLDVQDMLPRNLQHYYTYHGSLTTPPCTENVHWFVLADFVKLSRTQVWKLENSLLDHRNKTIHNDYRRTQPLNHRVVESNFPNQEYTLGSEFQFYLHKIEEILDYLRRALN","length":308,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":31,"region_id":"DP02680r001","start":21,"term_id":"IDPO:0000002","statement":[{"text":"The final model includes aa 32-279, while aa 21-31 are disordered.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22366092","version":2,"reference_html":"Crystal structure of the secretory isozyme of mammalian carbonic anhydrases CA VI: implications for biological assembly and inhibitor development. <i> Pilka ES, Kochan G, Oppermann U, Yue WW. </i> Biochem Biophys Res Commun, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3FE4"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T15:15:24.219Z"}}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02680","date":"2020-03-18T16:04:51.691Z","organism":"Homo sapiens","regions_counter":1,"name":"Carbonic anhydrase 6","dataset":["NDDs-related proteins"],"UniParc":"UPI0000161B17","uniref100":"UniRef100_P23280","uniref90":"UniRef90_P23280","uniref50":"UniRef50_P23280","genes":[{"name":{"value":"CA6"}}],"alphafold_very_low_content":0.06818181818181818,"disorder_content":0.03571428571428571,"disprot_consensus":{"full":[{"start":21,"end":31,"type":"D"}],"Structural state":[{"start":21,"end":31,"type":"D"}]}},{"acc":"B8ZXI1","features":{"gene3D":[{"start":1,"end":415,"id":"G3DSA:3.20.20.105","name":"Queuine tRNA-ribosyltransferase-like"}],"pfam":[{"id":"PF01702","name":"Queuine tRNA-ribosyltransferase","start":13,"end":414}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MKLSLIKVVNGCRLGKIQNLGKAGDCTVDIPGCLLYTRTGSAPHLTHQTLRNIHGVPGIAQLTLSSLAEHHEVLAEYKKGVGSFIGMPESLFYCSLHDPVTPGPAGYVTSKSVSVWGFGGRVEMTVSKFMAIQEALQPDWFQCLSDGEASCAETTSIKRARKSVDRSLLFLDSCLRLQEESEVLQKSVIIGVIEGGDVMEERLRSARETAKRPVGGFLLDGFQGDPAVTETRLHLLSSVTAELPEDKPRLICGVSRPDEVLECIERGVDLFESFFPYQVTERGCALTFTFDCQLNPEETLLQQNGIQEKIKGLDQAKKIEATGCNQEMTSFEINLKEKKYQEDFDPLVRGCSCYCCKNHTRAYIHHLLMTNELLAGVLLMMHNFEHYFGFFCSIREALKNDTLAQLKELICRQMF","length":415,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":326,"region_id":"DP02681r001","start":292,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"In both polypeptide chains, an expanded segment comprising Cys292–Gln326 obviously is disordered, as no corresponding electron density is visible in the map.","type":"Results"},{"text":"A short turn (Thr295–Gly298) connecting strands βG and βH in bacterial TGT is replaced by an extended putative loop comprising 45 residues (Thr287–Phe331) in QTRT2.","type":"Results"},{"text":"Loop βGβH of QTRT2","type":"Curator statement"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29862811","version":2,"reference_html":"Homodimer Architecture of QTRT2, the Noncatalytic Subunit of the Eukaryotic tRNA-Guanine Transglycosylase. <i> Behrens C, Biela I, Petiot-Bécard S, Botzanowski T, Cianférani S, Sager CP, Klebe G, Heine A, Reuter K. </i> Biochemistry, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6FV5"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-04T13:07:03.526Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":326,"region_id":"DP02681r002","start":292,"term_id":"IDPO:0000033","unpublished":true,"statement":[{"text":"In both polypeptide chains, an expanded segment comprising Cys292–Gln326 obviously is disordered, as no corresponding electron density is visible in the map.","type":"Results"},{"text":"A short turn (Thr295–Gly298) connecting strands βG and βH in bacterial TGT is replaced by an extended putative loop comprising 45 residues (Thr287–Phe331) in QTRT2.","type":"Results"},{"text":"Loop βGβH of QTRT2","type":"Curator statement"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29862811","version":3,"reference_html":"Homodimer Architecture of QTRT2, the Noncatalytic Subunit of the Eukaryotic tRNA-Guanine Transglycosylase. <i> Behrens C, Biela I, Petiot-Bécard S, Botzanowski T, Cianférani S, Sager CP, Klebe G, Heine A, Reuter K. </i> Biochemistry, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6FV5"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-04T13:07:08.146Z"}}],"released":"2023_12","ncbi_taxon_id":10090,"disprot_id":"DP02681","date":"2020-03-18T16:40:07.497Z","organism":"Mus musculus","regions_counter":2,"name":"Queuine tRNA-ribosyltransferase accessory subunit 2","dataset":[],"UniParc":"UPI0001B30122","uniref100":"UniRef100_B8ZXI1","uniref90":"UniRef90_B8ZXI1","uniref50":"UniRef50_B8ZXI1","genes":[{"name":{"value":"Qtrt2","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03043","url":"https://hamap.expasy.org/unirule/MF_03043"}}]},"synonyms":[{"value":"Qtrtd1","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03043","url":"https://hamap.expasy.org/unirule/MF_03043"}}]}]}],"alphafold_very_low_content":0.060240963855421686,"disorder_content":0.08433734939759036,"disprot_consensus":{"full":[{"start":292,"end":326,"type":"D"}],"Structural state":[{"start":292,"end":326,"type":"D"}],"Disorder function":[{"start":292,"end":326,"type":"F"}]}},{"acc":"P13797","features":{"gene3D":[{"start":113,"end":624,"id":"G3DSA:1.10.418.10","name":"Calponin-like domain"}],"pfam":[{"id":"PF00307","name":"Calponin homology (CH) domain","start":124,"end":237},{"id":"PF00307","name":"Calponin homology (CH) domain","start":268,"end":378},{"id":"PF00307","name":"Calponin homology (CH) domain","start":399,"end":505},{"id":"PF00307","name":"Calponin homology (CH) domain","start":521,"end":626},{"id":"PF13499","name":"EF-hand domain pair","start":15,"end":82}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MDEMATTQISKDELDELKEAFAKVDLNSNGFICDYELHELFKEANMPLPGYKVREIIQKLMLDGDRNKDGKISFDEFVYIFQEVKSSDIAKTFRKAINRKEGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDERAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELSRNEALAALLRDGETLEELMKLSPEELLLRWANFHLENSGWQKINNFSADIKDSKAYFHLLNQIAPKGQKEGEPRIDINMSGFNETDDLKRAESMLQQADKLGCRQFVTPADVVSGNPKLNLAFVANLFNKYPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLYADLQDALVILQLYERIKVPVDWSKVNKPPYPKLGANMKKLENCNYAVELGKHPAKFSLVGIGGQDLNDGNQTLTLALVWQLMRRYTLNVLEDLGDGQKANDDIIVNWVNRTLSEAGKSTSIQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNLTEDDKHNNAKYAVSMARRIGARVYALPEDLVEVKPKMVMTVFACLMGRGMKRV","length":630,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":20,"region_id":"DP02682r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"The final structure contains 247 residues, with the N-terminal 20 and eight residues in a mobile loop not visible, and 20 water molecules.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9302997","version":2,"reference_html":"The structure of an actin-crosslinking domain from human fimbrin. <i> Goldsmith SC, Pokala N, Shen W, Fedorov AA, Matsudaira P, Almo SC. </i> Nat Struct Biol, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1AOA"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02682","date":"2020-03-19T10:45:55.502Z","organism":"Homo sapiens","regions_counter":1,"name":"Plastin-3","dataset":[],"UniParc":"UPI000016AEC5","uniref100":"UniRef100_P13797","uniref90":"UniRef90_P13797","uniref50":"UniRef50_P13797","genes":[{"name":{"value":"PLS3"}}],"alphafold_very_low_content":0.03968253968253968,"disorder_content":0.031746031746031744,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"D"}],"Structural state":[{"start":1,"end":20,"type":"D"}]}},{"acc":"Q9DBG5","features":{"gene3D":[],"pfam":[{"id":"PF03036","name":"Perilipin family","start":22,"end":428}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MSSNGTDAPAEAQAAMEEPVVQPSVVDRVAGLPLISSTYGMVSAAYTSTKENYPHVRTVCDVAEKGVKTLTTAAVSTAQPILSKLEPQIATASEYAHRGLDRLQESLPILQQPTEKVLADTKELVSSTVSGAQEMVSSSVSSAKETVATRVTGAVDVTLGAVQNSVDKTKSAMTSGVQSVMGSRVGQMVISGVDRVLVKSEAWADNRLPLTEAELALIATPPEDSDMASLQQQRQEQNYFVRLGSLSERLRNHAYEHSLGKLQNARQKAQETLQQLTSVLGLMESVKQGVDQRLGEGQEKLHQMWLSWNQKTPQDAEKDPAKPEQVEARALSMFRDITQQLQSMCVALGASIQGLPSHVREQAQQARSQVNDLQATFSGIHSFQDLSAGVLAQTRERIARAREALDNTVEYVAQNTPAMWLVGPFAPGITEKTPEGK","length":437,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":205,"region_id":"DP02683r001","start":191,"term_id":"IDPO:0000002","statement":[{"text":"Residues 191–205, 289–320, and 432–437 could not be located in the electron density and are presumed disordered.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15242596","version":2,"reference_html":"Structure of a lipid droplet protein; the PAT family member TIP47. <i> Hickenbottom SJ, Kimmel AR, Londos C, Hurley JH. </i> Structure, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1SZI"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":320,"region_id":"DP02683r002","start":289,"term_id":"IDPO:0000002","statement":[{"text":"Residues 191–205, 289–320, and 432–437 could not be located in the electron density and are presumed disordered.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15242596","version":2,"reference_html":"Structure of a lipid droplet protein; the PAT family member TIP47. <i> Hickenbottom SJ, Kimmel AR, Londos C, Hurley JH. </i> Structure, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1SZI"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":10090,"disprot_id":"DP02683","date":"2020-03-19T10:56:20.899Z","organism":"Mus musculus","regions_counter":2,"name":"Perilipin-3","dataset":[],"UniParc":"UPI00000216F5","uniref100":"UniRef100_Q9DBG5","uniref90":"UniRef90_Q9DBG5","uniref50":"UniRef50_Q9DBG5","genes":[{"name":{"value":"Plin3"},"synonyms":[{"value":"M6prbp1"},{"value":"Tip47","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15242596","url":"http://www.ncbi.nlm.nih.gov/pubmed/15242596","alternativeUrl":"https://europepmc.org/abstract/MED/15242596"}}]}]}],"alphafold_very_low_content":0.2654462242562929,"disorder_content":0.10755148741418764,"disprot_consensus":{"full":[{"start":191,"end":205,"type":"D"},{"start":289,"end":320,"type":"D"}],"Structural state":[{"start":191,"end":205,"type":"D"},{"start":289,"end":320,"type":"D"}]}},{"acc":"P53816","features":{"gene3D":[],"pfam":[{"id":"PF04970","name":"Lecithin retinol acyltransferase","start":7,"end":125}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MRAPIPEPKPGDLIEIFRPFYRHWAIYVGDGYVVHLAPPSEVAGAGAASVMSALTDKAIVKKELLYDVAGSDKYQVNNKHDDKYSPLPCSKIIQRAEELVGQEVLYKLTSENCEHFVNELRYGVARSDQVRDVIIAASVAGMGLAAMSLIGVMFSRNKRQKQ","length":162,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":57,"region_id":"DP02684r001","start":40,"term_id":"IDPO:0000002","statement":[{"text":"Residues 1–5, 40–57, and 126–140 were not modeled because of the weak or absent electron density of these regions.","type":"Methods"},{"text":"Region 40-57 corresponds to a disordered loop between β3 and β4","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22605381","version":2,"reference_html":"Structural basis for the acyltransferase activity of lecithin:retinol acyltransferase-like proteins. <i> Golczak M, Kiser PD, Sears AE, Lodowski DT, Blaner WS, Palczewski K. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4DOT"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":57,"region_id":"DP02684r002","start":40,"term_id":"GO:0008289","statement":[{"text":"Residues 1–5, 40–57, and 126–140 were not modeled because of the weak or absent electron density of these regions.","type":"Methods"},{"text":"A region that contributes to the HRASLS2 and HRASLS3 membrane interaction is the 40–57-amino acid segment between β3 and β4.","type":"Results"},{"text":"Thus, the reason for the disorder observed in this particular region could stem from the lack of a proper interfacial environment in the protein crystal, as lipid membrane interactions have been shown to stabilize amphiphilic helices","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"22605381","version":3,"reference_html":"Structural basis for the acyltransferase activity of lecithin:retinol acyltransferase-like proteins. <i> Golczak M, Kiser PD, Sears AE, Lodowski DT, Blaner WS, Palczewski K. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4DOT"}],"term_name":"lipid binding","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Biological process","ec_ontology":"ECO","end":57,"region_id":"DP02684r004","start":40,"term_id":"GO:0051179","statement":[{"text":"A region that contributes to the HRASLS2 and HRASLS3 membrane interaction is the 40–57-amino acid segment between β3 and β4","type":"Results"},{"text":"This in turn suggested an amphiphilic helix with a hydrophobic interface mainly composed of Val-50, Met-51, and Leu-54 in HRASLS3 and Val-50, Leu-51, and Leu-54 in HRASLS2 that could interact with the nonpolar core of a bilayer","type":"Results"},{"text":"The authors suggest that interaction of this region with a lipid bilayer could promote its re-folding as documented for many other amphiphilic helices, although they don't test this hypothesis","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"22605381","version":3,"reference_html":"Structural basis for the acyltransferase activity of lecithin:retinol acyltransferase-like proteins. <i> Golczak M, Kiser PD, Sears AE, Lodowski DT, Blaner WS, Palczewski K. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4DOT"}],"term_name":"localization","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02684","date":"2020-03-19T11:31:21.690Z","organism":"Homo sapiens","regions_counter":4,"name":"Phospholipase A and acyltransferase 3","dataset":[],"UniParc":"UPI00001539AB","uniref100":"UniRef100_P53816","uniref90":"UniRef90_P53816","uniref50":"UniRef50_P53816","genes":[{"name":{"value":"PLAAT3","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:17825","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:17825"}}]},"synonyms":[{"value":"HRASLS3","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"22605381","url":"http://www.ncbi.nlm.nih.gov/pubmed/22605381","alternativeUrl":"https://europepmc.org/abstract/MED/22605381"}}]},{"value":"HREV107","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9771974","url":"http://www.ncbi.nlm.nih.gov/pubmed/9771974","alternativeUrl":"https://europepmc.org/abstract/MED/9771974"}}]},{"value":"PLA2G16"}]}],"alphafold_very_low_content":0.32098765432098764,"disorder_content":0.1111111111111111,"disprot_consensus":{"full":[{"start":40,"end":57,"type":"D"}],"Structural state":[{"start":40,"end":57,"type":"D"}],"Molecular function":[{"start":40,"end":57,"type":"F"}],"Biological process":[{"start":40,"end":57,"type":"F"}]}},{"acc":"P40999","features":{"gene3D":[],"pfam":[{"id":"PF00145","name":"C-5 cytosine-specific DNA methylase","start":8,"end":322}]},"creator":"fquaglia","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"sequence":"MLSTKRLRVLELYSGIGGMHYALNLANIPADIVCAIDINPQANEIYNLNHGKLAKHMDISTLTAKDFDAFDCKLWTMSPSCQPFTRIGNRKDILDPRSQAFLNILNVLPHVNNLPEYILIENVQGFEESKAAEECRKVLRNCGYNLIEGILSPNQFNIPNSRSRWYGLARLNFKGEWSIDDVFQFSEVAQKEGEVKRIRDYLEIERDWSSYMVLESVLNKWGHQFDIVKPDSSSCCCFTRGYTHLVQGAGSILQMSDHENTHEQFERNRMALQLRYFTAREVARLMGFPESLEWSKSNVTEKCMYRLLGNSINVKVVSYLISLLLEPLNF","length":330,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":95,"region_id":"DP02685r001","start":84,"term_id":"IDPO:0000002","statement":[{"text":"This loop is presumably unstructured in solution as the electron density for the corresponding amino acids was only observed for one of the four Dnmt2 molecules in the asymmetric unit, and this loop adopted a defined conformation due to formation of crystal contacts with another Dnmt2 molecule in the crystal lattice.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29892076","version":2,"reference_html":"Structural insights into the stimulation of S. pombe Dnmt2 catalytic efficiency by the tRNA nucleoside queuosine. <i> Johannsson S, Neumann P, Wulf A, Welp LM, Gerber HD, Krull M, Diederichsen U, Urlaub H, Ficner R. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6FDF"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":284812,"disprot_id":"DP02685","date":"2020-03-19T12:02:27.738Z","organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","regions_counter":1,"name":"tRNA (cytosine(38)-C(5))-methyltransferase","dataset":[],"UniParc":"UPI0000131CFF","uniref100":"UniRef100_P40999","uniref90":"UniRef90_P40999","uniref50":"UniRef50_P40999","genes":[{"name":{"value":"pmt1"},"orfNames":[{"value":"SPBC19C2.02"}]}],"alphafold_very_low_content":0.015151515151515152,"disorder_content":0.03636363636363636,"disprot_consensus":{"full":[{"start":84,"end":95,"type":"D"}],"Structural state":[{"start":84,"end":95,"type":"D"}]}},{"acc":"Q6XHB2","features":{"gene3D":[{"start":1547,"end":1718,"id":"G3DSA:2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"},{"start":1547,"end":1718,"id":"G3DSA:2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"},{"start":165,"end":358,"id":"G3DSA:3.80.10.10","name":"Ribonuclease Inhibitor"}],"pfam":[{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":1026,"end":1289},{"id":"PF08477","name":"Ras of Complex, Roc, domain of DAPkinase","start":372,"end":490},{"id":"PF16095","name":"C-terminal of Roc, COR-A domain","start":592,"end":717},{"id":"PF25497","name":"C-terminal of Roc, COR-B domain","start":746,"end":804},{"id":"PF25497","name":"C-terminal of Roc, COR-B domain","start":910,"end":1007}]},"creator":"fquaglia","taxonomy":["Eukaryota","Amoebozoa","Evosea","Eumycetozoa","Dictyostelia","Dictyosteliales","Dictyosteliaceae","Dictyostelium"],"sequence":"MDSSQQLQESQQLQQQYTRVGIDVIGPMKDLIISVMNSLDTTFKIINETYRIVYFDTDETKLTSSNLDSDDEEFESDDDADEEADLQIQASCNLYTFDGKNRQSVDEIKRIVQHLNETQSQQNDNQAVPVIPTFFVVVNIGVGPSFVSEIKSAAGTTQFIEWIVNDQASKEVFKVSTNLLSHHKKQIELTHACTVGDVNYLDQIILSGVSTDQLKEAHKAGHAIVFDSLLTHNSNSLVVTGTMALLGAIVENGDRKGKRLSLSRSNLSRFPMSITQMCTHLVELDLSDNKITELPKDIQLLKSLRILILRGNLLEDIPLEICYLGDLKILELQENPLNNFPLSVVQSGTKNLLLFCKNILERKKSETWNKVKLMFVGQEGVGKTSLCQALKGSKKKKAELQVTGDTVSTEGVKIQNIKNKKVEFHAWDFGGQQVFYPTHQFFLTTHALYLVVFKLTDPNFAERVNYWVRQVKSNSSGAVPAIFLVGTHSDVCTPEQLQEAESILKANFVKYSRVKENTINFVCCATGKGIKELKKRLIHEAEKSHLIKKDIPGNYMVLEARLTNRGANPGRMAVSGSPIGGGSSAQLSSNAINSQKERYIDYDDYMNECKLSHLQPEEIKGATDFLHNLGIILHFDTPTLKNLVVLDPQWLADVMSSLITFSHNWIKRGILNHSELVAVWGGKYDQSLWPLLLKLLEKFEVSYELPNIAKSLIPSLLPEDAEGEISTIKDREWVTLPQAIESGRCQVFGCDYNFDFMPLGFFARLLLRILLISGVEVRTYWRNGVLLDILTPEQVKLQQSKQQQLQQQQQQQNNNESNDSSVNNNNNNNNNNNNNNIINSSSSSSLNLTQTSTSTSPSKLSLNNSQINNSNSTLNSQQLINPSVSPLSSTTPRHQALITFIKKKSFESKDKDSYKLNIEVRSFNTTIEKDHSASLFFQQILFTIDTLLASSYVGLEITRMIPCIHCVQKNPRADPYYFDFSSCISALQDGKPHLFCRNDPSIPVRIDYIAPDLCLKKVPTLADNEIEYEKQIGKGGFGLVHKGRLVKDKSVVAIKSLILGDSEGETEMIEKFQEFQREVFIMSNLNHPNIVKLYGLMHNPPRMVMEFVPCGDLYHRLLDKAHPIKWSVKLRLMLDIALGIEYMQNQNPPIVHRDLRSPNIFLQSLDENAPVCAKVADFGLSQQSVHSVSGLLGNFQWMAPETIGAEEESYTEKADTYSFAMILYTILTGEGPFDEYSYGKIKFINMIREEGLRPTIPEDCPPRLRNVIELCWSGDPKKRPHFSYIVKELSELRNGNTTSTTTNTSSTTNNLNSANVSIASTSSNADDGSQTNNNNNNNNNNNNNNNNNSGSSIALSPSRSFEQQTTTTTTTTTSPSSPSTSFINSSGSYNTESYSVASSSTTNLLNTLNNANQPVNFIGTASVHKKMEVLAGVEAGETVWTKSADSSLCFWSTKKGHLINELKCPHTVATTMMIKVGKYIWEATNSNGIYIWDMGTMTIVQQLTTPHKGDVCLHFVEYGDNNGVWSGGSEGTVCLWDMQTFEKKHSFSLESAITAMSYFGNNTLYIASGSHIVVFKTKTLLMNVNQNWKHSTGSITSILAMKDEVWSGGSDGRIYIWKVKNEFELQKVQSLEAHHEKITSLIHLEDNVLSGSTDKCISLFKISDPKKPFTTQEHHKQGVTSIVKVQSHIVWAITSDTTTPLVLWNIPQKWEKKTANGILPRLKFFR","length":1726,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1193,"region_id":"DP02686r001","start":1180,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Because of its flexibility, the activation loop is not visible in the structure of dephosphorylated Roco4, and in the active form only the main chain can be traced.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22689969","version":2,"reference_html":"Roco kinase structures give insights into the mechanism of Parkinson disease-related leucine-rich-repeat kinase 2 mutations. <i> Gilsbach BK, Ho FY, Vetter IR, van Haastert PJ, Wittinghofer A, Kortholt A. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4F0G"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":1193,"region_id":"DP02686r002","start":1180,"term_id":"IDPO:0000045","unpublished":true,"statement":[{"text":"Because of its flexibility, the activation loop is not visible in the structure of dephosphorylated Roco4, and in the active form only the main chain can be traced.","type":"Results"},{"text":"Phosphorylation of serine and threonine residues in kinase-activation loops is important for regulating kinase activity in many protein kinases (22–25). Because the Roco4 kinase becomes autophosphorylated during kinase assays, it is technically difficult to measure the difference in kinase activity in the phosphorylated and dephosphorylated protein. In autophosphorylation assays Roco4 incorporates maximally 2.04 ± 0.33 mol (n = 5) of phosphate per mole of protein. Roco4 kinase contains four putative phosphorylation sites in the activation loop: S1181, S1184, S1187, and S1189","type":"Results"},{"text":"In many kinases, the activation loop is a highly flexible element and contains the primary activity-related phosphorylation sites. In the unphosphorylated, inactive state, this loop often is disordered, but upon phosphorylation it reorients into an ordered, active conformation","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"enzymatic activity assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22689969","version":2,"reference_html":"Roco kinase structures give insights into the mechanism of Parkinson disease-related leucine-rich-repeat kinase 2 mutations. <i> Gilsbach BK, Ho FY, Vetter IR, van Haastert PJ, Wittinghofer A, Kortholt A. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005801","cross_refs":[{"db":"PDB","id":"4F0G"}],"term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Disorder function"}],"released":"2023_12","ncbi_taxon_id":44689,"disprot_id":"DP02686","date":"2020-03-19T12:18:04.636Z","organism":"Dictyostelium discoideum","regions_counter":2,"name":"Probable serine/threonine-protein kinase roco4","dataset":[],"UniParc":"UPI00001BDD55","uniref100":"UniRef100_Q6XHB2","uniref90":"UniRef90_Q6XHB2","uniref50":"UniRef50_Q8SSS9","genes":[{"name":{"value":"roco4"},"orfNames":[{"value":"DDB_G0288251"}]}],"alphafold_very_low_content":0.19235225955967555,"disorder_content":0.008111239860950173,"disprot_consensus":{"full":[{"start":1180,"end":1193,"type":"D"}],"Structural state":[{"start":1180,"end":1193,"type":"D"}],"Disorder function":[{"start":1180,"end":1193,"type":"F"}]}},{"acc":"P24005","features":{"gene3D":[],"pfam":[{"id":"PF18060","name":"F actin bundling C terminal","start":187,"end":255}]},"creator":"fquaglia","taxonomy":["Eukaryota","Amoebozoa","Evosea","Eumycetozoa","Dictyostelia","Dictyosteliales","Dictyosteliaceae","Dictyostelium"],"sequence":"MAETKVAPNLTGIEQTKAGQSFTEKLSAEAMEFFCNVAKLPFSQQAVHFLNAYWAEVSKEAEFIYSVGWETIKYADMHCKGIQLVFKYDEGNDLDFDIALYFYEQLCKFCEDPKNKNYATTYPISQPQMLTALKRKQELREKVDVNFDGRVSFLEYLLYQYKDFANPADFCTRSMNHDEHPEIKKARLALEEVNKRIRAYEEEKARLTEESKIPGVKGLGATNMLAQIDSGPLKEQLNFALISAEAAVRTASKKYGGAAYSGGAGDAGAGSSAGAIWWMNRDLEEKKKRYGPQKK","length":295,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":269,"region_id":"DP02687r001","start":257,"term_id":"IDPO:0000002","statement":[{"text":"Residues 1–24 and 257–269 could not be built into the final refined model owing to a lack of electron density, implying that the extreme N-terminal region and the loop connecting α11 and α12 are highly flexible.","type":"Results"},{"text":"Although localised in the C-terminal actin-binding domain (C-domain; residues 181–295), this disordered region is not directly involved in the binding of actin since the actin-binding sites are at amino acids 1–123 (ABS1), 193–254 (ABS2) and 279–295 (ABS3)","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26327373","version":2,"reference_html":"Structure of the 34 kDa F-actin-bundling protein ABP34 from Dictyostelium discoideum. <i> Kim MK, Kim JH, Kim JS, Kang SO. </i> Acta Crystallogr D Biol Crystallogr, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4X3N"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":24,"region_id":"DP02687r002","start":1,"term_id":"IDPO:0000002","statement":[{"text":"Residues 1–24 and 257–269 could not be built into the final refined model owing to a lack of electron density, implying that the extreme N-terminal region and the loop connecting α11 and α12 are highly flexible.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26327373","version":2,"reference_html":"Structure of the 34 kDa F-actin-bundling protein ABP34 from Dictyostelium discoideum. <i> Kim MK, Kim JH, Kim JS, Kang SO. </i> Acta Crystallogr D Biol Crystallogr, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4X3N"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":44689,"disprot_id":"DP02687","date":"2020-03-19T14:56:08.086Z","organism":"Dictyostelium discoideum","regions_counter":2,"name":"Calcium-regulated actin-bundling protein","dataset":[],"UniParc":"UPI0000125439","uniref100":"UniRef100_P24005","uniref90":"UniRef90_P24005","uniref50":"UniRef50_P24005","genes":[{"name":{"value":"abpB"},"orfNames":[{"value":"DDB_G0279081"}]}],"alphafold_very_low_content":0.0576271186440678,"disorder_content":0.12542372881355932,"disprot_consensus":{"full":[{"start":1,"end":24,"type":"D"},{"start":257,"end":269,"type":"D"}],"Structural state":[{"start":1,"end":24,"type":"D"},{"start":257,"end":269,"type":"D"}]}},{"acc":"O96759","features":{"gene3D":[{"start":547,"end":587,"id":"G3DSA:1.10.45.10","name":"Vanillyl-alcohol Oxidase; Chain A, domain 4"}],"pfam":[{"id":"PF01565","name":"FAD binding domain","start":141,"end":279},{"id":"PF02913","name":"FAD linked oxidases, C-terminal domain","start":318,"end":586}]},"creator":"fquaglia","taxonomy":["Eukaryota","Amoebozoa","Evosea","Eumycetozoa","Dictyostelia","Dictyosteliales","Dictyosteliaceae","Dictyostelium"],"sequence":"MSGEKKEYPKEHIDLYQQIKWNGWGDTRKFLHQLKPSGTIAMTTPEVSSVPLPSLRGFIKKELTLPGEEDKPFVLDETPALQIENIHVDPPKQYPEFVRELKAFFLPDQLKDDKLARITHTFGKSLRDLIRVRIGQVKNAPDLIVLPHSHEEVERLVQLAHKYNVVIIPMGGGSNIVGAIEPVSNERFTVSIDMRRMNKVLWVDRREMTACIQVGIMGPELEKQLHKQGVSLGHDPDSFEFSTLGGWLATCSSGHQSDKYGDIEDMAVSFRTVTPTGTLELRNGARSGAGINYKHIILGSEGTLGIITEAVMKVHAVPQAVEYYGFLFPTFAHAVSALQQIRSSEVIPTMIRVYDPEETQLSFAWKPSKGAVSEFTSAMVKKYLHYIRSFDFKNVCLSIIGFEGPKKVVDFHRTSVFDILSKNAAFGLGSAPGKTWAEKRYDLPYIRDFLLDHNMWVDVAETTVSYANLQTLWKDAKQTFVKHFKDQGIPAWICAHISHTYTNGVCLYFIFASKQNENKDMAQYIEAKKLMTDIIFKYGGSLSHHHGVGYEHVPWMTRYATRGWINVYRSLKETIDPKDICNPRKLIPTIKEENNKEPFLFDVVNVKYPKL","length":611,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":562,"region_id":"DP02688r001","start":543,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Another disordered loop is close to the C terminus between helices α17 and α18 (residues 543–562). We will refer to it as the “HHH loop” (Figure 2B) because it contains three well-conserved histidines that have a role in substrate binding and/or activity","type":"Results"},{"text":"Inspection of the B factor values of the helix residues reveals a steady increase from the N terminus to the C terminus, the average B factor being 20–30 Å2 higher on the C-terminal helical end. This observation is consistent with the idea that the C-terminal residues of the gating helix can be quite flexible, as suggested by the fact that the helix adopts different conformations in the various protein chains.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17562315","version":2,"reference_html":"The crucial step in ether phospholipid biosynthesis: structural basis of a noncanonical reaction associated with a peroxisomal disorder. <i> Razeto A, Mattiroli F, Carpanelli E, Aliverti A, Pandini V, Coda A, Mattevi A. </i> Structure, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2UUV"},{"db":"PDB","id":"2UUU"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":562,"region_id":"DP02688r003","start":543,"term_id":"IDPO:0000030","unpublished":true,"statement":[{"text":"Another disordered loop is close to the C terminus between helices α17 and α18 (residues 543–562). We will refer to it as the “HHH loop” (Figure 2B) because it contains three well-conserved histidines that have a role in substrate binding and/or activity","type":"Results"},{"text":"Access to the tunnel is controlled by a flexible loop and a gating helix at the protein-membrane interface.","type":"Abstract"},{"text":"The tunnel is accessible from the flavin si face as a consequence of HHH loop disorder","type":"Results"},{"text":"The negatively charged phosphate moiety of the acyl-DHAP substrate might interact with the histidine cluster so that substrate binding might trigger closure of the HHH loop, shielding the active site from solvent.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17562315","version":3,"reference_html":"The crucial step in ether phospholipid biosynthesis: structural basis of a noncanonical reaction associated with a peroxisomal disorder. <i> Razeto A, Mattiroli F, Carpanelli E, Aliverti A, Pandini V, Coda A, Mattevi A. </i> Structure, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2UUV"},{"db":"PDB","id":"2UUU"}],"term_name":"entropic chain","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2023_12","ncbi_taxon_id":44689,"disprot_id":"DP02688","date":"2020-03-19T15:31:19.693Z","organism":"Dictyostelium discoideum","regions_counter":3,"name":"Alkyldihydroxyacetonephosphate synthase","dataset":[],"UniParc":"UPI00001254E7","uniref100":"UniRef100_O96759","uniref90":"UniRef90_O96759","uniref50":"UniRef50_O96759","genes":[{"name":{"value":"eapA"},"orfNames":[{"value":"DDB_G0286183"}]}],"alphafold_very_low_content":0.014729950900163666,"disorder_content":0.03273322422258593,"disprot_consensus":{"full":[{"start":543,"end":562,"type":"D"}],"Structural state":[{"start":543,"end":562,"type":"D"}],"Disorder function":[{"start":543,"end":562,"type":"F"}]}},{"acc":"Q54BW5","features":{"gene3D":[{"start":35,"end":176,"id":"G3DSA:2.70.40.10","name":"G3DSA:2.70.40.10"}],"pfam":[{"id":"PF00692","name":"dUTPase","start":46,"end":174}]},"creator":"fquaglia","taxonomy":["Eukaryota","Amoebozoa","Evosea","Eumycetozoa","Dictyostelia","Dictyosteliales","Dictyosteliaceae","Dictyostelium"],"sequence":"MPIEQKYFSLFSNLFKRLTTNNNNNNYLKMAPPNFETFKVKKLSDKAIIPQRGSKGAAGYDLSSAHELVVPAHGKALAMTDLQIAIPDGTYGRIAPRSGLAWKNFIDCGAGVIDSDYRGNVGVVLFNHSDVDFKVAVGDRVAQLIFERIVTPEPLEVDEIDETQRGAGGFGSTGVKVQN","length":179,"regions":[{"region_id":"DP02689r001","ec_ontology":"ECO","end":179,"term_id":"IDPO:0000002","start":164,"version":2,"statement":[{"text":"Crystallographic analyses of the core enzyme indicated that the C-termini, normally flexible, were constrained by interactions with the shortened N-termini that arose from the loss of residues 1-37.","type":"Abstract"},{"text":"Homotrimeric structure of D. discoideum dUTPase where the flexible C-terminus of chain A interacts with the N-terminus of chain B and the flexible C-terminus of chain C interacts with the N-terminus of chain A.","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"31910901","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5F9K"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Mitochondrial localization of Dictyostelium discoideum dUTPase mediated by its N-terminus. <i> Chia CP, Inoguchi N, Varon KC, Bartholomai BM, Moriyama H. </i> BMC Res Notes, 2020","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","ncbi_taxon_id":44689,"disprot_id":"DP02689","date":"2020-03-19T16:46:58.859Z","organism":"Dictyostelium discoideum","regions_counter":1,"name":"Deoxyuridine 5'-triphosphate nucleotidohydrolase","dataset":[],"UniParc":"UPI00004E54B4","uniref100":"UniRef100_Q54BW5","uniref90":"UniRef90_Q54BW5","uniref50":"UniRef50_Q54BW5","genes":[{"name":{"value":"dut"},"orfNames":[{"value":"DDB_G0293374"}]}],"alphafold_very_low_content":0.05027932960893855,"disorder_content":0.0893854748603352,"disprot_consensus":{"full":[{"start":164,"end":179,"type":"D"}],"Structural state":[{"start":164,"end":179,"type":"D"}]}},{"acc":"F4JL28","features":{"gene3D":[{"start":136,"end":210,"id":"G3DSA:3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":6,"end":135,"id":"G3DSA:2.30.30.490","name":"G3DSA:2.30.30.490"}],"pfam":[{"id":"PF01426","name":"BAH domain","start":31,"end":142},{"id":"PF30811","name":"UBR7-like PHD finger","start":147,"end":197}]},"creator":"fquaglia","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"sequence":"MAKTRPGVASKIKTGRKELDSYTIKGTNKVVRAGDCVLMRPSDAGKPPYVARVEKIEADARNNVKVHCRWYYRPEESLGGRRQFHGAKELFLSDHFDVQSAHTIEGKCIVHTFKNYTRLENVGAEDYYCRFEYKAATGAFTPDRVAVYCKCEMPYNPDDLMVQCEGCKDWYHPACVGMTIEEAKKLDHFVCAECSSDDDVKKSQNGFTSSPADDVKVRLSLFSHLLYRCSITYL","length":234,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":208,"region_id":"DP02690r001","start":195,"term_id":"IDPO:0000002","statement":[{"text":"However, we failed to obtain crystals of full-length EBS in complex with H3K4me2 or H3K4me3 peptides.","type":"Article"},{"text":"Missing density region in the C-terminal loop (197-234) of the protein","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30082787","version":2,"reference_html":"EBS is a bivalent histone reader that regulates floral phase transition in Arabidopsis. <i> Yang Z, Qian S, Scheid RN, Lu L, Chen X, Liu R, Du X, Lv X, Boersma MD, Scalf M, Smith LM, Denu JM, Du J, Zhong X. </i> Nat Genet, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5Z8L"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":234,"region_id":"DP02690r002","start":221,"term_id":"IDPO:0000002","statement":[{"text":"However, we failed to obtain crystals of full-length EBS in complex with H3K4me2 or H3K4me3 peptides.","type":"Article"},{"text":"Missing density region in the C-terminal loop (197-234) of the protein","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30082787","version":2,"reference_html":"EBS is a bivalent histone reader that regulates floral phase transition in Arabidopsis. <i> Yang Z, Qian S, Scheid RN, Lu L, Chen X, Liu R, Du X, Lv X, Boersma MD, Scalf M, Smith LM, Denu JM, Du J, Zhong X. </i> Nat Genet, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5Z8L"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":234,"region_id":"DP02690r004","start":200,"term_id":"GO:0140678","statement":[{"text":"Notably, EBS adopted an autoinhibition mode to mediate its switch in binding preference between H3K27me3 and H3K4me3.","type":"Abstract"},{"text":"To investigate the in vivo relevance of the C-terminal autoinhibition loop, we generated a C-terminal deletion mutant and found that it failed to complement the early flowering of ebs (n = 6 independent transgenic lines; Fig. 4a,​,bb and Supplementary Fig. 6d), despite having a much higher protein level than wild-type EBS","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"deletion mutation phenotypic evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"30082787","version":3,"reference_html":"EBS is a bivalent histone reader that regulates floral phase transition in Arabidopsis. <i> Yang Z, Qian S, Scheid RN, Lu L, Chen X, Liu R, Du X, Lv X, Boersma MD, Scalf M, Smith LM, Denu JM, Du J, Zhong X. </i> Nat Genet, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001175","term_name":"molecular function inhibitor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_12","ncbi_taxon_id":3702,"disprot_id":"DP02690","date":"2020-03-19T17:22:21.755Z","organism":"Arabidopsis thaliana","regions_counter":4,"name":"Chromatin remodeling protein EBS","dataset":[],"UniParc":"UPI00005DC255","uniref100":"UniRef100_F4JL28","uniref90":"UniRef90_F4JL28","uniref50":"UniRef50_F4JL28","genes":[{"name":{"value":"EBS","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11340178","url":"http://www.ncbi.nlm.nih.gov/pubmed/11340178","alternativeUrl":"https://europepmc.org/abstract/MED/11340178"}}]},"orfNames":[{"value":"F1N20.240","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"CAA18117.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA18117.1"}}]}],"olnNames":[{"value":"At4g22140","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AEE84562.1","url":"https://www.ebi.ac.uk/ena/browser/view/AEE84562.1"}}]}]}],"alphafold_very_low_content":0.12393162393162394,"disorder_content":0.11965811965811966,"disprot_consensus":{"full":[{"start":195,"end":208,"type":"D"},{"start":209,"end":220,"type":"F"},{"start":221,"end":234,"type":"D"}],"Structural state":[{"start":195,"end":208,"type":"D"},{"start":221,"end":234,"type":"D"}],"Molecular function":[{"start":200,"end":234,"type":"F"}]}},{"acc":"Q92608","features":{"gene3D":[{"start":423,"end":617,"id":"G3DSA:2.60.40.150","name":"C2 domain"},{"start":81,"end":177,"id":"G3DSA:1.20.1270.350","name":"G3DSA:1.20.1270.350"},{"start":1188,"end":1337,"id":"G3DSA:1.25.40.410","name":"G3DSA:1.25.40.410"},{"start":1493,"end":1622,"id":"G3DSA:1.20.58.740","name":"G3DSA:1.20.58.740"}],"pfam":[{"id":"PF06920","name":"DHR-2, Lobe A","start":1205,"end":1334},{"id":"PF07653","name":"Variant SH3 domain","start":12,"end":63},{"id":"PF14429","name":"C2 domain in Dock180 and Zizimin proteins","start":419,"end":615},{"id":"PF16172","name":"DOCK N-terminus","start":72,"end":414},{"id":"PF20421","name":"DHR-2, Lobe C","start":1514,"end":1615},{"id":"PF20422","name":"DHR-2, Lobe B","start":1395,"end":1473},{"id":"PF23554","name":"Dedicator of cytokinesis (DOCK) TPR region","start":626,"end":1156}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MAPWRKADKERHGVAIYNFQGSGAPQLSLQIGDVVRIQETCGDWYRGYLIKHKMLQGIFPKSFIHIKEVTVEKRRNTENIIPAEIPLAQEVTTTLWEWGSIWKQLYVASKKERFLQVQSMMYDLMEWRSQLLSGTLPKDELKELKQKVTSKIDYGNKILELDLIVRDEDGNILDPDNTSVISLFHAHEEATDKITERIKEEMSKDQPDYAMYSRISSSPTHSLYVFVRNFVCRIGEDAELFMSLYDPNKQTVISENYLVRWGSRGFPKEIEMLNNLKVVFTDLGNKDLNRDKIYLICQIVRVGKMDLKDTGAKKCTQGLRRPFGVAVMDITDIIKGKAESDEEKQHFIPFHPVTAENDFLHSLLGKVIASKGDSGGQGLWVTMKMLVGDIIQIRKDYPHLVDRTTVVARKLGFPEIIMPGDVRNDIYITLLQGDFDKYNKTTQRNVEVIMCVCAEDGKTLPNAICVGAGDKPMNEYRSVVYYQVKQPRWMETVKVAVPIEDMQRIHLRFMFRHRSSLESKDKGEKNFAMSYVKLMKEDGTTLHDGFHDLVVLKGDSKKMEDASAYLTLPSYRHHVENKGATLSRSSSSVGGLSVSSRDVFSISTLVCSTKLTQNVGLLGLLKWRMKPQLLQENLEKLKIVDGEEVVKFLQDTLDALFNIMMEHSQSDEYDILVFDALIYIIGLIADRKFQHFNTVLEAYIQQHFSATLAYKKLMTVLKTYLDTSSRGEQCEPILRTLKALEYVFKFIVRSRTLFSQLYEGKEQMEFEESMRRLFESINNLMKSQYKTTILLQVAALKYIPSVLHDVEMVFDAKLLSQLLYEFYTCIPPVKLQKQKVQSMNEIVQSNLFKKQECRDILLPVITKELKELLEQKDDMQHQVLERKYCVELLNSILEVLSYQDAAFTYHHIQEIMVQLLRTVNRTVITMGRDHILISHFVACMTAILNQMGDQHYSFYIETFQTSSELVDFLMETFIMFKDLIGKNVYPGDWMAMSMVQNRVFLRAINKFAETMNQKFLEHTNFEFQLWNNYFHLAVAFITQDSLQLEQFSHAKYNKILNKYGDMRRLIGFSIRDMWYKLGQNKICFIPGMVGPILEMTLIPEAELRKATIPIFFDMMLCEYQRSGDFKKFENEIILKLDHEVEGGRGDEQYMQLLESILMECAAEHPTIAKSVENFVNLVKGLLEKLLDYRGVMTDESKDNRMSCTVNLLNFYKDNNREEMYIRYLYKLRDLHLDCDNYTEAAYTLLLHTWLLKWSDEQCASQVMQTGQQHPQTHRQLKETLYETIIGYFDKGKMWEEAISLCKELAEQYEMEIFDYELLSQNLIQQAKFYESIMKILRPKPDYFAVGYYGQGFPSFLRNKVFIYRGKEYERREDFQMQLMTQFPNAEKMNTTSAPGDDVKNAPGQYIQCFTVQPVLDEHPRFKNKPVPDQIINFYKSNYVQRFHYSRPVRRGTVDPENEFASMWIERTSFVTAYKLPGILRWFEVVHMSQTTISPLENAIETMSTANEKILMMINQYQSDETLPINPLSMLLNGIVDPAVMGGFAKYEKAFFTEEYVRDHPEDQDKLTHLKDLIAWQIPFLGAGIKIHEKRVSDNLRPFHDRMEECFKNLKMKVEKEYGVREMPDFDDRRVGRPRSMLRSYRQMSIISLASMNSDCSTPSKPTSESFDLELASPKTPRVEQEEPISPGSTLPEVKLRRSKKRTKRSSVVFADEKAAAESDLKRLSRKHEFMSDTNLSEHAAIPLKASVLSQMSFASQSMPTIPALALSVAGIPGLDEANTSPRLSQTFLQLSDGDKKTLTRKKVNQFFKTMLASKSAEEGKQIPDSLSTDL","length":1830,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":80,"region_id":"DP02691r001","start":70,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The DOCK2 structure is composed of the N-terminal SH3 domain (residues 1–69) and a three-helix bundle domain (residues 81–167; Dα1–3). The electron density of the 11-residue region connecting the two domains was not observed.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22331897","version":2,"reference_html":"Structural basis for mutual relief of the Rac guanine nucleotide exchange factor DOCK2 and its partner ELMO1 from their autoinhibited forms. <i> Hanawa-Suetsugu K, Kukimoto-Niino M, Mishima-Tsumagari C, Akasaka R, Ohsawa N, Sekine S, Ito T, Tochio N, Koshiba S, Kigawa T, Terada T, Shirouzu M, Nishikimi A, Uruno T, Katakai T, Kinashi T, Kohda D, Fukui Y, Yokoyama S. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3A98"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":80,"region_id":"DP02691r002","start":70,"term_id":"IDPO:0000033","unpublished":true,"statement":[{"text":"The DOCK2 structure is composed of the N-terminal SH3 domain (residues 1–69) and a three-helix bundle domain (residues 81–167; Dα1–3). The electron density of the 11-residue region connecting the two domains was not observed.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22331897","version":3,"reference_html":"Structural basis for mutual relief of the Rac guanine nucleotide exchange factor DOCK2 and its partner ELMO1 from their autoinhibited forms. <i> Hanawa-Suetsugu K, Kukimoto-Niino M, Mishima-Tsumagari C, Akasaka R, Ohsawa N, Sekine S, Ito T, Tochio N, Koshiba S, Kigawa T, Terada T, Shirouzu M, Nishikimi A, Uruno T, Katakai T, Kinashi T, Kohda D, Fukui Y, Yokoyama S. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3A98"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":1621,"end":1830,"reference_id":"32651375","reference_source":"pmid","reference_html":"Structure of the DOCK2-ELMO1 complex provides insights into regulation of the auto-inhibited state. <i> Chang L, Yang J, Jo CH, Boland A, Zhang Z, McLaughlin SH, Abu-Thuraia A, Killoran RC, Smith MJ, Côté JF, Barford D. </i> Nat Commun, 2020","date":"2022-10-04T14:20:17.331Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"10498"},{"db":"PDB","id":"6TGC"},{"db":"PDB","id":"6TGB"},{"db":"EMDB","id":"10497"}],"region_id":"DP02691r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92556"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63000"}],"statement":[{"text":"The polybasic region C-terminal of DOCK2DHR2 (Fig. 1a) is disordered.","type":"Results"}]},{"start":70,"end":80,"reference_id":"32651375","reference_source":"pmid","reference_html":"Structure of the DOCK2-ELMO1 complex provides insights into regulation of the auto-inhibited state. <i> Chang L, Yang J, Jo CH, Boland A, Zhang Z, McLaughlin SH, Abu-Thuraia A, Killoran RC, Smith MJ, Côté JF, Barford D. </i> Nat Commun, 2020","date":"2022-10-04T14:27:29.438Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"10498"},{"db":"PDB","id":"6TGC"},{"db":"PDB","id":"6TGB"},{"db":"EMDB","id":"10497"}],"region_id":"DP02691r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92556"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63000"}],"statement":[{"text":"The electron microscopy evidence of the binary DOCK2-ELMO1 complex and ternary DOCK2-ELMO1-RAC1 complex, show this region lacks electron density indicating it is disordered.","type":"Curator statement"}]},{"start":578,"end":589,"reference_id":"32651375","reference_source":"pmid","reference_html":"Structure of the DOCK2-ELMO1 complex provides insights into regulation of the auto-inhibited state. <i> Chang L, Yang J, Jo CH, Boland A, Zhang Z, McLaughlin SH, Abu-Thuraia A, Killoran RC, Smith MJ, Côté JF, Barford D. </i> Nat Commun, 2020","date":"2022-10-04T14:27:45.775Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"10498"},{"db":"PDB","id":"6TGC"},{"db":"PDB","id":"6TGB"},{"db":"EMDB","id":"10497"}],"region_id":"DP02691r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92556"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63000"}],"statement":[{"text":"The electron microscopy evidence of the binary DOCK2-ELMO1 complex and ternary DOCK2-ELMO1-RAC1 complex, show this region lacks electron density indicating it is disordered.","type":"Curator statement"}]},{"start":1257,"end":1270,"reference_id":"32651375","reference_source":"pmid","reference_html":"Structure of the DOCK2-ELMO1 complex provides insights into regulation of the auto-inhibited state. <i> Chang L, Yang J, Jo CH, Boland A, Zhang Z, McLaughlin SH, Abu-Thuraia A, Killoran RC, Smith MJ, Côté JF, Barford D. </i> Nat Commun, 2020","date":"2022-10-04T14:29:07.544Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"10498"},{"db":"PDB","id":"6TGC"},{"db":"PDB","id":"6TGB"},{"db":"EMDB","id":"10497"}],"region_id":"DP02691r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92556"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63000"}],"statement":[{"text":"The electron microscopy evidence of the binary DOCK2-ELMO1 complex and ternary DOCK2-ELMO1-RAC1 complex, show this region lacks electron density indicating it is disordered.","type":"Curator statement"}]}],"released":"2023_12","ncbi_taxon_id":9606,"disprot_id":"DP02691","date":"2020-03-19T17:43:40.376Z","organism":"Homo sapiens","regions_counter":6,"name":"Dedicator of cytokinesis protein 2","dataset":[],"UniParc":"UPI000006CED8","uniref100":"UniRef100_Q92608","uniref90":"UniRef90_Q92608","uniref50":"UniRef50_Q92608","genes":[{"name":{"value":"DOCK2"},"synonyms":[{"value":"KIAA0209"}]}],"alphafold_very_low_content":0.12459016393442623,"disorder_content":0.13497267759562842,"disprot_consensus":{"full":[{"start":70,"end":80,"type":"D"},{"start":578,"end":589,"type":"D"},{"start":1257,"end":1270,"type":"D"},{"start":1621,"end":1830,"type":"D"}],"Structural state":[{"start":70,"end":80,"type":"D"},{"start":578,"end":589,"type":"D"},{"start":1257,"end":1270,"type":"D"},{"start":1621,"end":1830,"type":"D"}],"Disorder function":[{"start":70,"end":80,"type":"F"}]}},{"acc":"Q6R327","features":{"gene3D":[],"pfam":[{"id":"PF14663","name":"Rapamycin-insensitive companion of mTOR RasGEF_N domain","start":747,"end":852},{"id":"PF14664","name":"Rapamycin-insensitive companion of mTOR, N-term","start":58,"end":439},{"id":"PF14665","name":"Rapamycin-insensitive companion of mTOR, phosphorylation-site","start":1085,"end":1188},{"id":"PF14666","name":"Rapamycin-insensitive companion of mTOR, middle domain","start":641,"end":740},{"id":"PF14668","name":"Rapamycin-insensitive companion of mTOR, domain 5","start":922,"end":991}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MAAIGRGRSLKNLRVRGRNDSGEENVPLDLTREPSDNLREILQNVARLQGVSNMRKLGHLNNFTKLLCDIGHSEEKLGFHYEDIIICLRLALLNEAKEVRAAGLRALRYLIQDSSILQKVLKLKVDYLIARCIDIQQSNEVERTQALRLVRKMITVNASLFPSSVTNSLIAVGNDGLQERDRMVRACIAIICELALQNPEVVALRGGLNTILKNVIDCQLSRINEALITTILHLLNHPKTRQYVRADVELERILAPYTDFHYRHSPDTAEGQLKEDREARFLASKMGIIATFRSWAGIINLCKPGNSGIQSLIGVLCIPNMEIRRGLLEVLYDIFRLPLPVVTEEFIEALLSVDPGRFQDSWRLSDGFVAAEAKTILPHRARSRPDLMDNYLALILSAFIRNGLLEGLVEVITNSDDHISVRATILLGELLHMANTILPHSHSHHLHCLPTLMNMAASFDIPKEKRLRASAALNCLKRFHEMKKRGPKPYSLHLDHIIQKAIATHQKRDQYLRVQKDIFILKDTEEALLINLRDSQVLQHKENLEWNWNLIGTILKWPNVNLRNYKDEQLHRFVRRLLYFYKPSSKLYANLDLDFAKAKQLTVVGCQFTEFLLESEEDGQGYLEDLVKDIVQWLNASSGMKPERSLQNNGLLTTLSQHYFLFIGTLSCHPHGVKMLEKCSVFQCLLNLCSLKNQDHLLKLTVSSLDYSRDGLARVILSKILTAATDACRLYATKHLRVLLRANVEFFNNWGIELLVTQLHDKNKTISSEALDILDEACEDKANLHALIQMKPALSHLGDKGLLLLLRFLSIPKGFSYLNERGYVAKQLEKWHREYNSKYVDLIEEQLNEALTTYRKPVDGDNYVRRSNQRLQRPHVYLPIHLYGQLVHHKTGCHLLEVQNIITELCRNVRTPDLDKWEEIKKLKASLWALGNIGSSNWGLNLLQEENVIPDILKLAKQCEVLSIRGTCVYVLGLIAKTKQGCDILKCHNWDAVRHSRKHLWPVVPDDVEQLCNELSSIPSTLSLNSESTSSRHNSESESVPSSMFILEDDRFGSSSTSTFFLDINEDTEPTFYDRSGPIKDKNSFPFFASSKLVKNRILNSLTLPNKKHRSSSDPKGGKLSSESKTSNRRIRTLTEPSVDFNHSDDFTPISTVQKTLQLETSFMGNKHIEDTGSTPSIGENDLKFTKNFGTENHRENTSRERLVVESSTSSHMKIRSQSFNTDTTTSGISSMSSSPSRETVGVDATTMDTDCGSMSTVVSTKTIKTSHYLTPQSNHLSLSKSNSVSLVPPGSSHTLPRRAQSLKAPSIATIKSLADCNFSYTSSRDAFGYATLKRLQQQRMHPSLSHSEALASPAKDVLFTDTITMKANSFESRLTPSRFMKALSYASLDKEDLLSPINQNTLQRSSSVRSMVSSATYGGSDDYIGLALPVDINDIFQVKDIPYFQTKNIPPHDDRGARAFAHDAGGLPSGTGGLVKNSFHLLRQQMSLTEIMNSIHSDASLFLESTEDTGLQEHTDDNCLYCVCIEILGFQPSNQLSAICSHSDFQDIPYSDWCEQTIHNPLEVVPSKFSGISGCSDGVSQEGSASSTKSTELLLGVKTIPDDTPMCRILLRKEVLRLVINLSSSVSTKCHETGLLTIKEKYPQTFDDICLYSEVSHLLSHCTFRLPCRRFIQELFQDVQFLQMHEEAEAVLATPPKQPIVDTSAES","length":1708,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":191,"region_id":"DP02692r001","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"According to the 4.9 Å EM map, we could only build poly-Alanine chains for N-terminal portion of Rictor and five α-helices of mSin1. The rest portions are invisible in the EM map possibly due to their intrinsic flexibility, which is consistent with secondary structure prediction","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29567957","version":2,"reference_html":"Cryo-EM structure of human mTOR complex 2. <i> Chen X, Liu M, Tian Y, Li J, Qi Y, Zhao D, Wu Z, Huang M, Wong CCL, Wang HW, Wang J, Yang H, Xu Y. </i> Cell Res, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"EMDB","id":"EMD-6913"},{"db":"PDB","id":"5ZCS"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1610,"region_id":"DP02692r002","start":1017,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"According to the 4.9 Å EM map, we could only build poly-Alanine chains for N-terminal portion of Rictor and five α-helices of mSin1. The rest portions are invisible in the EM map possibly due to their intrinsic flexibility, which is consistent with secondary structure prediction","type":"Discussion"},{"text":"Rictor has an N-terminal armadillo (ARM) repeat cluster (~900 residues), followed by a large unstructured region","type":"Results"},{"text":"The C-terminal half of Rictor and most of the mSin1 portion are invisible in the EM map, which might result from their intrinsic flexibility.","type":"Results"},{"text":"The C-terminal portion of Rictor could not be assigned in the EM map possibly due to its flexibility.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29567957","version":2,"reference_html":"Cryo-EM structure of human mTOR complex 2. <i> Chen X, Liu M, Tian Y, Li J, Qi Y, Zhao D, Wu Z, Huang M, Wong CCL, Wang HW, Wang J, Yang H, Xu Y. </i> Cell Res, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"EMDB","id":"EMD-6913"},{"db":"PDB","id":"5ZCS"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP02692r004","unpublished":true,"ec_ontology":"ECO","end":595,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"Moreover, mSin1N could bind to the Rictor N-terminal portions containing residues 1–595 or 1–905 and C-terminal portion containing residues 905–1708","type":"Results"},{"text":"Two C-terminal truncations and an N-terminal truncation of Rictor could bind to mTOR","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9BPZ7","partner_end":null},{"partner_start":null,"db":"UniProt","id":"P42345","partner_end":null}],"term_name":"protein binding","ec_name":"co-immunoprecipitation evidence used in manual assertion","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"29567957","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"EMDB","id":"EMD-6913"},{"db":"PDB","id":"5ZCS"}],"term_namespace":"Molecular function","ec_id":"ECO:0006030","curator_id":"fquaglia","reference_html":"Cryo-EM structure of human mTOR complex 2. <i> Chen X, Liu M, Tian Y, Li J, Qi Y, Zhao D, Wu Z, Huang M, Wong CCL, Wang HW, Wang J, Yang H, Xu Y. </i> Cell Res, 2018","curator_orcid":"0000-0002-0341-4888","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02692r005","unpublished":true,"ec_ontology":"ECO","end":905,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"Moreover, mSin1N could bind to the Rictor N-terminal portions containing residues 1–595 or 1–905 and C-terminal portion containing residues 905–1708","type":"Results"},{"text":"Two C-terminal truncations and an N-terminal truncation of Rictor could bind to mTOR","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9BPZ7","partner_end":null},{"partner_start":null,"db":"UniProt","id":"P42345","partner_end":null}],"term_name":"protein binding","ec_name":"co-immunoprecipitation evidence used in manual assertion","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"29567957","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"EMDB","id":"EMD-6913"},{"db":"PDB","id":"5ZCS"}],"term_namespace":"Molecular function","ec_id":"ECO:0006030","curator_id":"fquaglia","reference_html":"Cryo-EM structure of human mTOR complex 2. <i> Chen X, Liu M, Tian Y, Li J, Qi Y, Zhao D, Wu Z, Huang M, Wong CCL, Wang HW, Wang J, Yang H, Xu Y. </i> Cell Res, 2018","curator_orcid":"0000-0002-0341-4888","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02692r006","unpublished":true,"ec_ontology":"ECO","end":1708,"term_id":"GO:0005515","start":905,"version":3,"statement":[{"text":"Moreover, mSin1N could bind to the Rictor N-terminal portions containing residues 1–595 or 1–905 and C-terminal portion containing residues 905–1708","type":"Results"},{"text":"Two C-terminal truncations and an N-terminal truncation of Rictor could bind to mTOR","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9BPZ7","partner_end":null},{"partner_start":null,"db":"UniProt","id":"P42345","partner_end":null}],"term_name":"protein binding","ec_name":"co-immunoprecipitation evidence used in manual assertion","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"29567957","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"EMDB","id":"EMD-6913"},{"db":"PDB","id":"5ZCS"}],"term_namespace":"Molecular function","ec_id":"ECO:0006030","curator_id":"fquaglia","reference_html":"Cryo-EM structure of human mTOR complex 2. <i> Chen X, Liu M, Tian Y, Li J, Qi Y, Zhao D, Wu Z, Huang M, Wong CCL, Wang HW, Wang J, Yang H, Xu Y. </i> Cell Res, 2018","curator_orcid":"0000-0002-0341-4888","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1708,"region_id":"DP02692r007","start":1,"term_id":"GO:0060090","unpublished":true,"statement":[{"text":"The functional core complex consists of mTOR, mLST8, and two mTORC2-specific components, Rictor and mSin1.","type":"Results"},{"text":"Our biochemical and structural analyses demonstrate that Rictor and mSin1 interact with each other and together make multiple contacts with mTOR-mLST8.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"29567957","version":3,"reference_html":"Cryo-EM structure of human mTOR complex 2. <i> Chen X, Liu M, Tian Y, Li J, Qi Y, Zhao D, Wu Z, Huang M, Wong CCL, Wang HW, Wang J, Yang H, Xu Y. </i> Cell Res, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","cross_refs":[{"db":"EMDB","id":"EMD-6913"},{"db":"PDB","id":"5ZCS"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_12","ncbi_taxon_id":9606,"disprot_id":"DP02692","date":"2020-03-20T09:53:06.897Z","organism":"Homo sapiens","regions_counter":9,"name":"Rapamycin-insensitive companion of mTOR","dataset":[],"UniParc":"UPI00003529F3","uniref100":"UniRef100_Q6R327","uniref90":"UniRef90_Q6R327","uniref50":"UniRef50_Q6R327","genes":[{"name":{"value":"RICTOR","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"EAW55980.1","url":"https://www.ebi.ac.uk/ena/browser/view/EAW55980.1"}}]},"synonyms":[{"value":"KIAA1999","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"BAC02708.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAC02708.1"}}]}]}],"alphafold_very_low_content":0.35655737704918034,"disorder_content":0.4596018735362998,"disprot_consensus":{"full":[{"start":1,"end":191,"type":"D"},{"start":192,"end":1016,"type":"F"},{"start":1017,"end":1610,"type":"D"},{"start":1611,"end":1708,"type":"F"}],"Structural state":[{"start":1,"end":191,"type":"D"},{"start":1017,"end":1610,"type":"D"}],"Molecular function":[{"start":1,"end":1708,"type":"F"}]}},{"acc":"Q9BPZ7","features":{"gene3D":[{"start":369,"end":493,"id":"G3DSA:2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"}],"pfam":[{"id":"PF05422","name":"Stress-activated map kinase interacting protein 1 (SIN1)","start":18,"end":128},{"id":"PF16978","name":"SAPK-interacting protein 1 (Sin1), middle CRIM domain","start":139,"end":267},{"id":"PF16979","name":"SAPK-interacting protein 1 (Sin1), Pleckstrin-homology","start":382,"end":487},{"id":"PF25322","name":"SIN1 Ras-binding domain","start":287,"end":353}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MAFLDNPTIILAHIRQSHVTSDDTGMCEMVLIDHDVDLEKIHPPSMPGDSGSEIQGSNGETQGYVYAQSVDITSSWDFGIRRRSNTAQRLERLRKERQNQIKCKNIQWKERNSKQSAQELKSLFEKKSLKEKPPISGKQSILSVRLEQCPLQLNNPFNEYSKFDGKGHVGTTATKKIDVYLPLHSSQDRLLPMTVVTMASARVQDLIGLICWQYTSEGREPKLNDNVSAYCLHIAEDDGEVDTDFPPLDSNEPIHKFGFSTLALVEKYSSPGLTSKESLFVRINAAHGFSLIQVDNTKVTMKEILLKAVKRRKGSQKVSGPQYRLEKQSEPNVAVDLDSTLESQSAWEFCLVRENSSRADGVFEEDSQIDIATVQDMLSSHHYKSFKVSMIHRLRFTTDVQLGISGDKVEIDPVTNQKASTKFWIKQKPISIDSDLLCACDLAEEKSPSHAIFKLTYLSNHDYKHLYFESDAATVNEIVLKVNYILESRASTARADYFAQKQRKLNRRTSFSFQKEKKSGQQ","length":522,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":522,"region_id":"DP02693r001","start":248,"term_id":"IDPO:0000002","statement":[{"text":"The C-terminal half of Rictor and most of the mSin1 portion are invisible in the EM map, which might result from their intrinsic flexibility.","type":"Results"},{"text":"According to the 4.9 Å EM map, we could only build poly-Alanine chains for N-terminal portion of Rictor and five α-helices of mSin1. The rest portions are invisible in the EM map possibly due to their intrinsic flexibility, which is consistent with secondary structure prediction","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29567957","version":2,"reference_html":"Cryo-EM structure of human mTOR complex 2. <i> Chen X, Liu M, Tian Y, Li J, Qi Y, Zhao D, Wu Z, Huang M, Wong CCL, Wang HW, Wang J, Yang H, Xu Y. </i> Cell Res, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"EMDB","id":"EMD-6913"},{"db":"PDB","id":"5ZCS"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":522,"region_id":"DP02693r002","start":1,"term_id":"GO:0060090","statement":[{"text":"The functional core complex consists of mTOR, mLST8, and two mTORC2-specific components, Rictor and mSin1.","type":"Abstract"},{"text":"mSin1 binds Rictor, MSLT8 and mTOR and is involved in the formation of the complex ","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"29567957","version":3,"reference_html":"Cryo-EM structure of human mTOR complex 2. <i> Chen X, Liu M, Tian Y, Li J, Qi Y, Zhao D, Wu Z, Huang M, Wong CCL, Wang HW, Wang J, Yang H, Xu Y. </i> Cell Res, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","cross_refs":[{"db":"EMDB","id":"EMD-6913"},{"db":"PDB","id":"5ZCS"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":522,"region_id":"DP02693r003","start":1,"term_id":"GO:0060090","statement":[{"text":"The functional core complex consists of mTOR, mLST8, and two mTORC2-specific components, Rictor and mSin1.","type":"Abstract"},{"text":"mSin1 binds Rictor, MSLT8 and mTOR and is involved in the formation of the complex ","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"co-immunoprecipitation evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"29567957","version":3,"reference_html":"Cryo-EM structure of human mTOR complex 2. <i> Chen X, Liu M, Tian Y, Li J, Qi Y, Zhao D, Wu Z, Huang M, Wong CCL, Wang HW, Wang J, Yang H, Xu Y. </i> Cell Res, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006030","cross_refs":[{"db":"EMDB","id":"EMD-6913"},{"db":"PDB","id":"5ZCS"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02693r004","ec_ontology":"ECO","end":522,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"Full-length mSin1 bound to the N-terminal portion (residues 1–905) or C-terminal portion (residues 905–1708) of Rictor","type":"Results"},{"text":"The ProA-tagged mSin1 could pull out endogenous mTOR, indicating a direct interaction (Supplementary information, Figure S2b, lanes 1, 3, 4, and 7). Full-length mSin1 and two C-terminal truncations could also pull out the endogenous mTOR in the presence of Rictor","type":"Results"},{"text":"mSin1 bound to mLST8 (lane 4) and the interaction was enhanced when mTOR was overexpressed (lane 6).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q6R327","partner_end":null},{"partner_start":null,"db":"UniProt","id":"P42345","partner_end":null},{"partner_start":null,"db":"UniProt","id":"Q9BVC4","partner_end":null}],"term_name":"protein binding","ec_name":"co-immunoprecipitation evidence used in manual assertion","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"29567957","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"EMDB","id":"EMD-6913"},{"db":"PDB","id":"5ZCS"}],"term_namespace":"Molecular function","ec_id":"ECO:0006030","curator_id":"fquaglia","reference_html":"Cryo-EM structure of human mTOR complex 2. <i> Chen X, Liu M, Tian Y, Li J, Qi Y, Zhao D, Wu Z, Huang M, Wong CCL, Wang HW, Wang J, Yang H, Xu Y. </i> Cell Res, 2018","curator_orcid":"0000-0002-0341-4888","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":522,"region_id":"DP02693r005","start":360,"term_id":"GO:0140678","statement":[{"text":"The PH domain of mSin1 inhibits mTORC2 activity and this autoinhibition is released in the presence of phosphatidylinositol (3,4,5)-trisphosphate (PIP3)","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"29567957","version":3,"reference_html":"Cryo-EM structure of human mTOR complex 2. <i> Chen X, Liu M, Tian Y, Li J, Qi Y, Zhao D, Wu Z, Huang M, Wong CCL, Wang HW, Wang J, Yang H, Xu Y. </i> Cell Res, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","cross_refs":[{"db":"EMDB","id":"EMD-6913"},{"db":"PDB","id":"5ZCS"}],"term_name":"molecular function inhibitor activity","curator_orcid":"0000-0002-0341-4888","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02693","date":"2020-03-20T10:10:43.458Z","organism":"Homo sapiens","regions_counter":5,"name":"Target of rapamycin complex 2 subunit MAPKAP1","dataset":["Stress response proteins"],"UniParc":"UPI000002B3BD","uniref100":"UniRef100_Q9BPZ7","uniref90":"UniRef90_Q9BPZ7","uniref50":"UniRef50_Q9BPZ7","genes":[{"name":{"value":"MAPKAP1"},"synonyms":[{"value":"MIP1"},{"value":"SIN1"}]}],"alphafold_very_low_content":0.15134099616858238,"disorder_content":0.5268199233716475,"disprot_consensus":{"full":[{"start":1,"end":247,"type":"F"},{"start":248,"end":522,"type":"D"}],"Structural state":[{"start":248,"end":522,"type":"D"}],"Molecular function":[{"start":1,"end":522,"type":"F"}]}},{"acc":"Q8WUN7","features":{"gene3D":[{"start":46,"end":123,"id":"G3DSA:1.20.225.20","name":"G3DSA:1.20.225.20"}],"pfam":[{"id":"PF00240","name":"Ubiquitin family","start":156,"end":224},{"id":"PF16455","name":"Ubiquitin-binding domain","start":29,"end":132}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MGGCVGAQHDSSGSLNENSEGTGVALGRNQPLKKEKPKWKSDYPMTDGQLRSKRDEFWDTAPAFEGRKEIWDALKAAAHAFESNDHELAQAIIDGANITLPHGALTECYDELGNRYQLPVYCLAPPINMIEEKSDIETLDIPEPPPNSGYECQLRLRLSTGKDLKLVVRSTDTVFHMKRRLHAAEGVEPGSQRWFFSGRPLTDKMKFEELKIPKDYVVQVIVSQPVQNPTPVEN","length":234,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":20,"region_id":"DP02694r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"Moreover, both termini (residues Met1–Ser20 and Pro101–Asn106) are not included in the structural calculation process for their conformational flexibility.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15987890","version":2,"reference_html":"Solution structure of the ubiquitin-like domain of human DC-UbP from dendritic cells. <i> Gao YG, Song AX, Shi YH, Chang YG, Liu SX, Yu YZ, Cao XT, Lin DH, Hu HY. </i> Protein Sci, 2005","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"1TTN"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02694","date":"2020-03-20T12:01:33.832Z","organism":"Homo sapiens","regions_counter":1,"name":"Ubiquitin domain-containing protein 2","dataset":[],"UniParc":"UPI00000733F2","uniref100":"UniRef100_Q8WUN7","uniref90":"UniRef90_Q8WUN7","uniref50":"UniRef50_Q9HAC8","genes":[{"name":{"value":"UBTD2"},"synonyms":[{"value":"DCUBP"}],"orfNames":[{"value":"SB72"}]}],"alphafold_very_low_content":0.2094017094017094,"disorder_content":0.08547008547008547,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"D"}],"Structural state":[{"start":1,"end":20,"type":"D"}]}},{"acc":"Q9JIP3","features":{"gene3D":[{"start":7,"end":174,"id":"G3DSA:2.60.40.2160","name":"G3DSA:2.60.40.2160"},{"start":176,"end":268,"id":"G3DSA:2.60.40.2150","name":"G3DSA:2.60.40.2150"}],"pfam":[{"id":"PF08357","name":"SEFIR domain","start":329,"end":476},{"id":"PF16556","name":"IL17RA/B, N-terminal domain","start":32,"end":163},{"id":"PF16578","name":"IL17RD, second fnIII domain","start":176,"end":265}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MLLVLLILAASCRSALPREPTIQCGSETGPSPEWMVQHTLTPGDLRDLQVELVKTSVAAEEFSILMNISWILRADASIRLLKATKICVSGKNNMNSYSCVRCNYTEAFQSQTRPSGGKWTFSYVGFPVELSTLYLISAHNIPNANMNEDSPSLSVNFTSPGCLNHVMKYKKQCTEAGSLWDPDITACKKNEKMVEVNFTTNPLGNRYTILIQRDTTLGFSRVLENKLMRTSVAIPVTEESEGAVVQLTPYLHTCGNDCIRREGTVVLCSETSAPIPPDDNRRMLGGWLPLFLVLLVAVWVLAAGIYLTWRQGRSTKTSFPISTMLLPLIKVLVVYPSEICFHHTVCRFTDFLQNYCRSEVILEKWQKKKIAEMGPVQWLTTQKQAADKVVFLLPSDVPTLCDSACGHNEGSARENSQDLFPLAFNLFCSDFSSQTHLHKYLVVYLGGADLKGDYNALSVCPQYHLMKDATAFHTELLKATQSMSVKKRSQACHDSCSPL","length":499,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":416,"region_id":"DP02695r001","start":396,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The structure is well defined except for a 20 amino acids (A.A.) region connecting strand βC and helix αC (residues 396–416, we named as CC′ segment), the electron density of which is not observable.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23355738","version":2,"reference_html":"Crystal structure of IL-17 receptor B SEFIR domain. <i> Zhang B, Liu C, Qian W, Han Y, Li X, Deng J. </i> J Immunol, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3VBC"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-04T14:38:29.483Z"}}],"released":"2023_12","ncbi_taxon_id":10090,"disprot_id":"DP02695","date":"2020-03-20T13:51:40.720Z","organism":"Mus musculus","regions_counter":1,"name":"Interleukin-17 receptor B","dataset":[],"UniParc":"UPI0000001A0E","uniref100":"UniRef100_Q9JIP3","uniref90":"UniRef90_Q9JIP3","uniref50":"UniRef50_Q9NRM6","genes":[{"name":{"value":"Il17rb"},"synonyms":[{"value":"Evi27"},{"value":"Il17br"}]}],"alphafold_very_low_content":0.11623246492985972,"disorder_content":0.04208416833667335,"disprot_consensus":{"full":[{"start":396,"end":416,"type":"D"}],"Structural state":[{"start":396,"end":416,"type":"D"}]}},{"acc":"Q9FLN8","features":{"gene3D":[],"pfam":[{"id":"PF03492","name":"SAM dependent carboxyl methyltransferase","start":17,"end":370}]},"creator":"fquaglia","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"sequence":"MGSKGDNVAVCNMKLERLLSMKGGKGQDSYANNSQAQAMHARSMLHLLEETLENVHLNSSASPPPFTAVDLGCSSGANTVHIIDFIVKHISKRFDAAGIDPPEFTAFFSDLPSNDFNTLFQLLPPLVSNTCMEECLAADGNRSYFVAGVPGSFYRRLFPARTIDFFHSAFSLHWLSQVPESVTDRRSAAYNRGRVFIHGAGEKTTTAYKRQFQADLAEFLRARAAEVKRGGAMFLVCLGRTSVDPTDQGGAGLLFGTHFQDAWDDLVREGLVAAEKRDGFNIPVYAPSLQDFKEVVDANGSFAIDKLVVYKGGSPLVVNEPDDASEVGRAFASSCRSVAGVLVEAHIGEELSNKLFSRVESRATSHAKDVLVNLQFFHIVASLSFT","length":386,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":24,"region_id":"DP02696r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"The first 49 residues of AtIAMT1 in this particular set of crystal structures form a mobile loop. In fact, recognizable electron density attributable to residues 1 to 24 is noticeably absent from the refined AtIAMT1 crystal structure, which also lacks a bound IAA substrate.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18162595","version":2,"reference_html":"Structural, biochemical, and phylogenetic analyses suggest that indole-3-acetic acid methyltransferase is an evolutionarily ancient member of the SABATH family. <i> Zhao N, Ferrer JL, Ross J, Guan J, Yang Y, Pichersky E, Noel JP, Chen F. </i> Plant Physiol, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3B5I"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":3702,"disprot_id":"DP02696","date":"2020-03-20T14:35:48.880Z","organism":"Arabidopsis thaliana","regions_counter":1,"name":"Indole-3-acetate O-methyltransferase 1","dataset":[],"UniParc":"UPI0000048C70","uniref100":"UniRef100_Q9FLN8","uniref90":"UniRef90_Q9FLN8","uniref50":"UniRef50_Q9FLN8","genes":[{"name":{"value":"IAMT1"},"orfNames":[{"value":"MCO15.20"}],"olnNames":[{"value":"At5g55250"}]}],"alphafold_very_low_content":0.03626943005181347,"disorder_content":0.06217616580310881,"disprot_consensus":{"full":[{"start":1,"end":24,"type":"D"}],"Structural state":[{"start":1,"end":24,"type":"D"}]}},{"acc":"Q02363","features":{"gene3D":[{"start":30,"end":97,"id":"G3DSA:4.10.280.10","name":"Helix-loop-helix DNA-binding domain"}],"pfam":[{"id":"PF00010","name":"Helix-loop-helix DNA-binding domain","start":37,"end":76}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MKAFSPVRSVRKNSLSDHSLGISRSKTPVDDPMSLLYNMNDCYSKLKELVPSIPQNKKVSKMEILQHVIDYILDLQIALDSHPTIVSLHHQRPGQNQASRTPLTTLNTDISILSLQASEFPSELMSNDSKALCG","length":134,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":23,"region_id":"DP02697r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"We have solved the structure of the ID2 homodimer HLH domain (residues 24–82) at a 2.1Å resolution, coupled to a stabilizing 14 amino acid linker region (LKPSFLVQSGDIAS).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23119064","version":2,"reference_html":"A divalent ion is crucial in the structure and dominant-negative function of ID proteins, a class of helix-loop-helix transcription regulators. <i> Wong MV, Jiang S, Palasingam P, Kolatkar PR. </i> PLoS One, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4AYA"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02697","date":"2020-03-20T14:57:19.368Z","organism":"Homo sapiens","regions_counter":1,"name":"DNA-binding protein inhibitor ID-2","dataset":[],"UniParc":"UPI00000012EE","uniref100":"UniRef100_Q02363","uniref90":"UniRef90_Q02363","uniref50":"UniRef50_Q02363","genes":[{"name":{"value":"ID2"},"synonyms":[{"value":"BHLHB26"}]}],"alphafold_very_low_content":0.14925373134328357,"disorder_content":0.17164179104477612,"disprot_consensus":{"full":[{"start":1,"end":23,"type":"D"}],"Structural state":[{"start":1,"end":23,"type":"D"}]}},{"acc":"P54687","features":{"gene3D":[{"start":46,"end":381,"id":"G3DSA:3.30.470.10","name":"G3DSA:3.30.470.10"},{"start":194,"end":373,"id":"G3DSA:3.20.10.10","name":"D-amino Acid Aminotransferase, subunit A, domain 2"}],"pfam":[{"id":"PF01063","name":"Amino-transferase class IV","start":94,"end":343}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MKDCSNGCSAECTGEGGSKEVVGTFKAKDLIVTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGEDHQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVTRRCILDLAHQWGEFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPKLASRILSKLTDIQYGREESDWTIVLS","length":386,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":21,"region_id":"DP02698r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"The final model of hBCATc-ox·4MeVA comprises 358 residues (22-45, 47-193, and 199-385) for subunit 1, 358 residues (24-194 and 199-385) for subunit 2, 2 PLPs, 4MeVAs, and 351 water molecules. The average thermal factor of the main-chain atoms is 24.3 Å2. No interpretable electron density was observed for the residues that are not listed above.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16141215","version":2,"reference_html":"Structural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentin. <i> Goto M, Miyahara I, Hirotsu K, Conway M, Yennawar N, Islam MM, Hutson SM. </i> J Biol Chem, 2005","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2COI"},{"db":"PDB","id":"2COJ"},{"db":"PDB","id":"2COG"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","ncbi_taxon_id":9606,"disprot_id":"DP02698","date":"2020-03-24T13:11:08.788Z","organism":"Homo sapiens","regions_counter":1,"name":"Branched-chain-amino-acid aminotransferase, cytosolic","dataset":[],"UniParc":"UPI00001267D1","uniref100":"UniRef100_P54687","uniref90":"UniRef90_P54687","uniref50":"UniRef50_P54687","genes":[{"name":{"value":"BCAT1"},"synonyms":[{"value":"BCT1"},{"value":"ECA39"}]}],"alphafold_very_low_content":0.04404145077720207,"disorder_content":0.054404145077720206,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"}],"Structural state":[{"start":1,"end":21,"type":"D"}]}},{"acc":"Q6V1X1","features":{"gene3D":[{"start":632,"end":889,"id":"G3DSA:3.40.50.1820","name":"G3DSA:3.40.50.1820"},{"start":91,"end":614,"id":"G3DSA:2.140.10.30","name":"G3DSA:2.140.10.30"}],"pfam":[{"id":"PF00326","name":"Prolyl oligopeptidase family","start":687,"end":890},{"id":"PF00930","name":"Dipeptidyl peptidase IV (DPP IV) N-terminal region","start":175,"end":594},{"id":"PF19520","name":"Dipeptidyl peptidase 8 and 9 N-terminal","start":9,"end":162}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MWKRSEQMKIKSGKCNMAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQLKKLLADTRKYHGYMMAKAPHDFMFVKRNDPDGPHSDRIYYLAMSGENRENTLFYSEIPKTINRAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIGTVGIASYDYHQGSGTFLFQAGSGIYHVKDGGPQGFTQQPLRPNLVETSCPNIRMDPKLCPADPDWIAFIHSNDIWISNIVTREERRLTYVHNELANMEEDARSAGVATFVLQEEFDRYSGYWWCPKAETTPSGGKILRILYEENDESEVEIIHVTSPMLETRRADSFRYPKTGTANPKVTFKMSEIMIDAEGRIIDVIDKELIQPFEILFEGVEYIARAGWTPEGKYAWSILLDRSQTRLQIVLISPELFIPVEDDVMERQRLIESVPDSVTPLIIYEETTDIWINIHDIFHVFPQSHEEEIEFIFASECKTGFRHLYKITSILKESKYKRSSGGLPAPSDFKCPIKEEIAITSGEWEVLGRHGSNIQVDEVRRLVYFEGTKDSPLEHHLYVVSYVNPGEVTRLTDRGYSHSCCISQHCDFFISKYSNQKNPHCVSLYKLSSPEDDPTCKTKEFWATILDSAGPLPDYTPPEIFSFESTTGFTLYGMLYKPHDLQPGKKYPTVLFIYGGPQVQLVNNRFKGVKYFRLNTLASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEIDDQVEGLQYLASRYDFIDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLWIFYDTGYTERYMGHPDQNEQGYYLGSVAMQAEKFPSEPNRLLLLHGFLDENVHFAHTSILLSFLVRAGKPYDLQIYPQERHSIRVPESGEHYELHLLHYLQENLGSRIAALKVI","length":898,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":164,"region_id":"DP02699r001","start":138,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The DPP8 unliganded form has interpretable electron density from residues 48–70, 77–105, 109–137, and 165–897, while in DPP8 in complex with SLRFLYEG, residues 48–105, 109–139, and 148–897 are well ordered. ","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29382749","version":2,"reference_html":"Structures and mechanism of dipeptidyl peptidases 8 and 9, important players in cellular homeostasis and cancer. <i> Ross B, Krapp S, Augustin M, Kierfersauer R, Arciniega M, Geiss-Friedlander R, Huber R. </i> Proc Natl Acad Sci U S A, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6EOS"},{"db":"PDB","id":"6EOO"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-02T17:49:21.861Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":164,"region_id":"DP02699r002","start":148,"term_id":"IDPO:0000011","unpublished":true,"statement":[{"text":"The DPP8 unliganded form has interpretable electron density from residues 48–70, 77–105, 109–137, and 165–897, while in DPP8 in complex with SLRFLYEG, residues 48–105, 109–139, and 148–897 are well ordered. ","type":"Results"},{"text":"In intriguing contrast to DPP4, where liganded and unliganded forms are closely similar, ligand binding to DPP8/9 induces an extensive rearrangement at the active site through a disorder-order transition of a 26-residue loop segment, which partially folds into an α-helix (R-helix), including R160/133, a key residue for substrate binding.","type":"Abstract"},{"text":"Part of this segment folds into the R-helix, which harbors the arginine residues at its C termini. The R-helix becomes ordered upon substrate binding but is mostly disordered in the unliganded forms (Fig. 2 B, D, and E)","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29382749","version":2,"reference_html":"Structures and mechanism of dipeptidyl peptidases 8 and 9, important players in cellular homeostasis and cancer. <i> Ross B, Krapp S, Augustin M, Kierfersauer R, Arciniega M, Geiss-Friedlander R, Huber R. </i> Proc Natl Acad Sci U S A, 2018","date":"2022-08-04T08:16:15.698Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6EOT"},{"db":"PDB","id":"6EOP"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-04T14:47:10.930Z"}},{"start":1,"end":47,"reference_id":"29382749","reference_source":"pmid","reference_html":"Structures and mechanism of dipeptidyl peptidases 8 and 9, important players in cellular homeostasis and cancer. <i> Ross B, Krapp S, Augustin M, Kierfersauer R, Arciniega M, Geiss-Friedlander R, Huber R. </i> Proc Natl Acad Sci U S A, 2018","date":"2022-08-02T17:49:05.636Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6EOS"},{"db":"PDB","id":"6EOO"}],"region_id":"DP02699r003","statement":[{"text":"The DPP8 unliganded form has interpretable electron density from residues 48–70, 77–105, 109–137, and 165–897, while in DPP8 in complex with SLRFLYEG, residues 48–105, 109–139, and 148–897 are well ordered.","type":"Results"}]}],"released":"2023_12","ncbi_taxon_id":9606,"disprot_id":"DP02699","date":"2020-03-24T13:24:42.581Z","organism":"Homo sapiens","regions_counter":3,"name":"Dipeptidyl peptidase 8","dataset":[],"UniParc":"UPI00001BFAFE","uniref100":"UniRef100_Q6V1X1","uniref90":"UniRef90_Q6V1X1","uniref50":"UniRef50_Q6V1X1","genes":[{"name":{"value":"DPP8","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11012666","url":"http://www.ncbi.nlm.nih.gov/pubmed/11012666","alternativeUrl":"https://europepmc.org/abstract/MED/11012666"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:16490","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:16490"}}]},"synonyms":[{"value":"DPRP1"}],"orfNames":[{"value":"MSTP097"},{"value":"MSTP135"},{"value":"MSTP141"}]}],"alphafold_very_low_content":0.04788418708240535,"disorder_content":0.08240534521158129,"disprot_consensus":{"full":[{"start":1,"end":47,"type":"D"},{"start":138,"end":147,"type":"D"},{"start":148,"end":164,"type":"T"}],"Structural state":[{"start":1,"end":47,"type":"D"},{"start":138,"end":164,"type":"D"}],"Structural transition":[{"start":148,"end":164,"type":"T"}]}},{"acc":"P0A8S9","features":{"gene3D":[{"start":1,"end":116,"id":"G3DSA:1.10.4000.10","name":"Flagellar transcriptional activator FlhD"}],"pfam":[{"id":"PF05247","name":"Flagellar transcriptional activator (FlhD)","start":1,"end":100}]},"creator":"fquaglia","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"sequence":"MHTSELLKHIYDINLSYLLLAQRLIVQDKASAMFRLGINEEMATTLAALTLPQMVKLAETNQLVCHFRFDSHQTITQLTQDSRVDDLQQIHTGIMLSTRLLNDVNQPEEALRKKRA","length":116,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":116,"region_id":"DP02700r001","start":83,"term_id":"IDPO:0000002","statement":[{"text":"The C-termini of both FlhD monomers (residues 83-116) are completely disrupted by crystal packing, implying that this region of FlhD is highly flexible.","type":"Abstract"},{"text":"Residues 83–116 in both chains were not interpretable and were not initially modelled.","type":"Results"},{"text":"Protruding from the core are two flexible arms, each composed of ≈ 34 residues of the C‐terminus of each monomer","type":"Results"},{"text":"Thus, our model suggests that the entire C‐terminal sequence (83–116) of each chain is mobile and flexible in the FlhD dimer, so much so that its folding energy is less than the energy necessary to crystallize the protein.","type":"Results"},{"text":"Also, residues 83–116 in chain B and residues 99–116 in chain A are disrupted by crystal packing and cannot be modelled. Thus, this part of the FlhD dimer must be highly flexible in solution and, therefore, its structure should be malleable","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11169099","version":2,"reference_html":"Crystal structure of the global regulator FlhD from Escherichia coli at 1.8 A resolution. <i> Campos A, Zhang RG, Alkire RW, Matsumura P, Westbrook EM. </i> Mol Microbiol, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1G8E"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":116,"region_id":"DP02700r002","start":83,"term_id":"IDPO:0000031","statement":[{"text":"The C-termini of both FlhD monomers (residues 83-116) are completely disrupted by crystal packing, implying that this region of FlhD is highly flexible.","type":"Abstract"},{"text":"Thus, our model suggests that the entire C‐terminal sequence (83–116) of each chain is mobile and flexible in the FlhD dimer, so much so that its folding energy is less than the energy necessary to crystallize the protein.","type":"Results"},{"text":"Thus, the unusually tight packing of protein in this crystal form prevents both C‐termini from adopting a well‐defined structure. The implication is that the C‐terminus is very flexible: sufficiently flexible that the forces involved in crystal packing are greater than the forces folding this region of the FlhD protein.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11169099","version":3,"reference_html":"Crystal structure of the global regulator FlhD from Escherichia coli at 1.8 A resolution. <i> Campos A, Zhang RG, Alkire RW, Matsumura P, Westbrook EM. </i> Mol Microbiol, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1G8E"}],"term_name":"flexible C-terminal tail","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":83333,"disprot_id":"DP02700","date":"2020-03-24T14:04:27.245Z","organism":"Escherichia coli (strain K12)","regions_counter":2,"name":"Flagellar transcriptional regulator FlhD","dataset":[],"UniParc":"UPI0000113055","uniref100":"UniRef100_B7MCF4","uniref90":"UniRef90_B7MCF4","uniref50":"UniRef50_O85806","genes":[{"name":{"value":"flhD"},"synonyms":[{"value":"flbB"}],"olnNames":[{"value":"b1892"},{"value":"JW1881"}]}],"alphafold_very_low_content":0.02586206896551724,"disorder_content":0.29310344827586204,"disprot_consensus":{"full":[{"start":83,"end":116,"type":"D"}],"Structural state":[{"start":83,"end":116,"type":"D"}],"Disorder function":[{"start":83,"end":116,"type":"F"}]}},{"acc":"Q15631","features":{"gene3D":[{"start":1,"end":132,"id":"G3DSA:1.20.58.190","name":"Translin; domain 1"},{"start":133,"end":228,"id":"G3DSA:1.20.58.200","name":"Translin; domain 2"}],"pfam":[{"id":"PF01997","name":"Translin family","start":19,"end":216}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MSVSEIFVELQGFLAAEQDIREEIRKVVQSLEQTAREILTLLQGVHQGAGFQDIPKRCLKAREHFGTVKTHLTSLKTKFPAEQYYRFHEHWRFVLQRLVFLAAFVVYLETETLVTREAVTEILGIEPDREKGFHLDVEDYLSGVLILASELSRLSVNSVTAGDYSRPLHISTFINELDSGFRLLNLKNDSLRKRYDGLKYDVKKVEEVVYDLSIRGFNKETAAACVEK","length":228,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":228,"region_id":"DP02701r001","start":218,"term_id":"IDPO:0000002","statement":[{"text":"In the orthorhombic crystal structure, the first 11 residues, including the His tag  and the spacer sequence before Met1,and the last 11 resides (residues 218-228) are invisible, probably owing to disorder.","type":"Methods"},{"text":"The C-terminal segment from residue 218 to the end was poorly defined in each monomer and was not included in the atomic model.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15039555","version":2,"reference_html":"Structure of human translin at 2.2 A resolution. <i> Sugiura I, Sasaki C, Hasegawa T, Kohno T, Sugio S, Moriyama H, Kasai M, Matsuzaki T. </i> Acta Crystallogr D Biol Crystallogr, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1J1J"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02701","date":"2020-03-24T15:38:32.929Z","organism":"Homo sapiens","regions_counter":1,"name":"Translin","dataset":[],"UniParc":"UPI0000000C3D","uniref100":"UniRef100_Q15631","uniref90":"UniRef90_Q15631","uniref50":"UniRef50_Q15631","genes":[{"name":{"value":"TSN"}}],"alphafold_very_low_content":0.03508771929824561,"disorder_content":0.04824561403508772,"disprot_consensus":{"full":[{"start":218,"end":228,"type":"D"}],"Structural state":[{"start":218,"end":228,"type":"D"}]}},{"acc":"Q14995","features":{"gene3D":[{"start":94,"end":187,"id":"G3DSA:3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A"},{"start":379,"end":578,"id":"G3DSA:1.10.565.10","name":"Retinoid X Receptor"}],"pfam":[{"id":"PF00104","name":"Ligand-binding domain of nuclear hormone receptor","start":403,"end":577},{"id":"PF00105","name":"Double treble clef zinc finger, C4 type","start":102,"end":171}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MEVNAGGVIAYISSSSSASSPASCHSEGSENSFQSSSSSVPSSPNSSNSDTNGNPKNGDLANIEGILKNDRIDCSMKTSKSSAPGMTKSHSGVTKFSGMVLLCKVCGDVASGFHYGVHACEGCKGFFRRSIQQNIQYKKCLKNENCSIMRMNRNRCQQCRFKKCLSVGMSRDAVRFGRIPKREKQRMLIEMQSAMKTMMNSQFSGHLQNDTLVEHHEQTALPAQEQLRPKPQLEQENIKSSSPPSSDFAKEEVIGMVTRAHKDTFMYNQEQQENSAESMQPQRGERIPKNMEQYNLNHDHCGNGLSSHFPCSESQQHLNGQFKGRNIMHYPNGHAICIANGHCMNFSNAYTQRVCDRVPIDGFSQNENKNSYLCNTGGRMHLVCPMSKSPYVDPHKSGHEIWEEFSMSFTPAVKEVVEFAKRIPGFRDLSQHDQVNLLKAGTFEVLMVRFASLFDAKERTVTFLSGKKYSVDDLHSMGAGDLLNSMFEFSEKLNALQLSDEEMSLFTAVVLVSADRSGIENVNSVEALQETLIRALRTLIMKNHPNEASIFTKLLLKLPDLRSLNNMHSEELLAFKVHP","length":579,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":395,"region_id":"DP02702r001","start":386,"term_id":"IDPO:0000002","statement":[{"text":"The current atomic model of Rev-erbβ contains residues (396–476) with disordered N and C-terminal tails (residues 386–395 and 477–479).","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17870090","version":2,"reference_html":"Structural insight into the constitutive repression function of the nuclear receptor Rev-erbbeta. <i> Woo EJ, Jeong DG, Lim MY, Jun Kim S, Kim KJ, Yoon SM, Park BC, Ryu SE. </i> J Mol Biol, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2V0V"},{"db":"PDB","id":"2V7C"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":479,"region_id":"DP02702r002","start":470,"term_id":"IDPO:0000002","statement":[{"text":"Careful examination of the structure shows that the region corresponding to the disordered region 470–479 in molecule A exhibits relatively high thermal displacement parameters in all other molecules in both crystal forms, indicating structural mobility of this region","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17870090","version":2,"reference_html":"Structural insight into the constitutive repression function of the nuclear receptor Rev-erbbeta. <i> Woo EJ, Jeong DG, Lim MY, Jun Kim S, Kim KJ, Yoon SM, Park BC, Ryu SE. </i> J Mol Biol, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2V0V"},{"db":"PDB","id":"2V7C"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","ncbi_taxon_id":9606,"disprot_id":"DP02702","date":"2020-03-24T16:09:41.311Z","organism":"Homo sapiens","regions_counter":2,"name":"Nuclear receptor subfamily 1 group D member 2","dataset":[],"UniParc":"UPI0000209A6C","uniref100":"UniRef100_Q14995","uniref90":"UniRef90_Q14995","uniref50":"UniRef50_Q14995","genes":[{"name":{"value":"NR1D2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:7963","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:7963"}}]}}],"alphafold_very_low_content":0.43350604490500866,"disorder_content":0.03454231433506045,"disprot_consensus":{"full":[{"start":386,"end":395,"type":"D"},{"start":470,"end":479,"type":"D"}],"Structural state":[{"start":386,"end":395,"type":"D"},{"start":470,"end":479,"type":"D"}]}},{"acc":"O00411","features":{"gene3D":[{"start":207,"end":356,"id":"G3DSA:1.25.40.10","name":"G3DSA:1.25.40.10"},{"start":551,"end":699,"id":"G3DSA:1.10.1320.10","name":"DNA-directed RNA polymerase, N-terminal domain"}],"pfam":[{"id":"PF00940","name":"DNA-dependent RNA polymerase","start":831,"end":1205},{"id":"PF14700","name":"DNA-directed RNA polymerase N-terminal","start":428,"end":704}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MSALCWGRGAAGLKRALRPCGRPGLPGKEGTAGGVCGPRRSSSASPQEQDQDRRKDWGHVELLEVLQARVRQLQAESVSEVVVNRVDVARLPECGSGDGSLQPPRKVQMGAKDATPVPCGRWAKILEKDKRTQQMRMQRLKAKLQMPFQSGEFKALTRRLQVEPRLLSKQMAGCLEDCTRQAPESPWEEQLARLLQEAPGKLSLDVEQAPSGQHSQAQLSGQQQRLLAFFKCCLLTDQLPLAHHLLVVHHGQRQKRKLLTLDMYNAVMLGWARQGAFKELVYVLFMVKDAGLTPDLLSYAAALQCMGRQDQDAGTIERCLEQMSQEGLKLQALFTAVLLSEEDRATVLKAVHKVKPTFSLPPQLPPPVNTSKLLRDVYAKDGRVSYPKLHLPLKTLQCLFEKQLHMELASRVCVVSVEKPTLPSKEVKHARKTLKTLRDQWEKALCRALRETKNRLEREVYEGRFSLYPFLCLLDEREVVRMLLQVLQALPAQGESFTTLARELSARTFSRHVVQRQRVSGQVQALQNHYRKYLCLLASDAEVPEPCLPRQYWEELGAPEALREQPWPLPVQMELGKLLAEMLVQATQMPCSLDKPHRSSRLVPVLYHVYSFRNVQQIGILKPHPAYVQLLEKAAEPTLTFEAVDVPMLCPPLPWTSPHSGAFLLSPTKLMRTVEGATQHQELLETCPPTALHGALDALTQLGNCAWRVNGRVLDLVLQLFQAKGCPQLGVPAPPSEAPQPPEAHLPHSAAPARKAELRRELAHCQKVAREMHSLRAEALYRLSLAQHLRDRVFWLPHNMDFRGRTYPCPPHFNHLGSDVARALLEFAQGRPLGPHGLDWLKIHLVNLTGLKKREPLRKRLAFAEEVMDDILDSADQPLTGRKWWMGAEEPWQTLACCMEVANAVRASDPAAYVSHLPVHQDGSCNGLQHYAALGRDSVGAASVNLEPSDVPQDVYSGVAAQVEVFRRQDAQRGMRVAQVLEGFITRKVVKQTVMTVVYGVTRYGGRLQIEKRLRELSDFPQEFVWEASHYLVRQVFKSLQEMFSGTRAIQHWLTESARLISHMGSVVEWVTPLGVPVIQPYRLDSKVKQIGGGIQSITYTHNGDISRKPNTRKQKNGFPPNFIHSLDSSHMMLTALHCYRKGLTFVSVHDCYWTHAADVSVMNQVCREQFVRLHSEPILQDLSRFLVKRFCSEPQKILEASQLKETLQAVPKPGAFDLEQVKRSTYFFS","length":1230,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":217,"region_id":"DP02703r001","start":105,"term_id":"IDPO:0000002","statement":[{"text":"Here we report the X-ray structure of human mtRNAP at 2.5 Å resolution, which reveals a T7-like catalytic carboxy-terminal domain, an amino-terminal domain that remotely resembles the T7 promoter-binding domain, a novel pentatricopeptide repeat domain, and a flexible N-terminal extension.","type":"Abstract"},{"text":"The refined structure includes residues 218–591, 603–611, 616–735, 770–1085 and 1109–1230.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21947009","version":2,"reference_html":"Structure of human mitochondrial RNA polymerase. <i> Ringel R, Sologub M, Morozov YI, Litonin D, Cramer P, Temiakov D. </i> Nature, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3SPA"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T15:20:23.033Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":602,"region_id":"DP02703r002","start":592,"term_id":"IDPO:0000002","statement":[{"text":"The refined structure includes residues 218–591, 603–611, 616–735, 770–1085 and 1109–1230.","type":"Methods"},{"text":"Disordered region inside the intercalating hairpin","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21947009","version":2,"reference_html":"Structure of human mitochondrial RNA polymerase. <i> Ringel R, Sologub M, Morozov YI, Litonin D, Cramer P, Temiakov D. </i> Nature, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3SPA"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T15:20:01.581Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":769,"region_id":"DP02703r003","start":734,"term_id":"IDPO:0000002","statement":[{"text":"The refined structure includes residues 218–591, 603–611, 616–735, 770–1085 and 1109–1230.","type":"Methods"},{"text":"Disordered region inside the \"thumb\" of the protein","type":"Curator statement"},{"text":"A portion of the thumb (residues 736–769) and the flexible specificity loop (residues 1086–1105) are not visible in the structure, but adjacent elements occupy almost identical positions in T7 RNAP, indicating that these elements have similar orientations and functions.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21947009","version":2,"reference_html":"Structure of human mitochondrial RNA polymerase. <i> Ringel R, Sologub M, Morozov YI, Litonin D, Cramer P, Temiakov D. </i> Nature, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3SPA"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T15:19:42.043Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1108,"region_id":"DP02703r004","start":1086,"term_id":"IDPO:0000002","statement":[{"text":"The refined structure includes residues 218–591, 603–611, 616–735, 770–1085 and 1109–1230.","type":"Methods"},{"text":"Disordered region corresponding to the \"specificity loop\" of the protein","type":"Curator statement"},{"text":"A portion of the thumb (residues 736–769) and the flexible specificity loop (residues 1086–1105) are not visible in the structure, but adjacent elements occupy almost identical positions in T7 RNAP, indicating that these elements have similar orientations and functions.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21947009","version":2,"reference_html":"Structure of human mitochondrial RNA polymerase. <i> Ringel R, Sologub M, Morozov YI, Litonin D, Cramer P, Temiakov D. </i> Nature, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3SPA"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T15:19:17.000Z"}},{"start":39,"end":218,"reference_id":"35662414","reference_source":"pmid","reference_html":"Non-coding 7S RNA inhibits transcription via mitochondrial RNA polymerase dimerization. <i> Zhu X, Xie X, Das H, Tan BG, Shi Y, Al-Behadili A, Peter B, Motori E, Valenzuela S, Posse V, Gustafsson CM, Hällberg BM, Falkenberg M. </i> Cell, 2022","date":"2023-06-13T15:26:59.587Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7PZR"}],"region_id":"DP02703r005","statement":[{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":592,"end":602,"reference_id":"35662414","reference_source":"pmid","reference_html":"Non-coding 7S RNA inhibits transcription via mitochondrial RNA polymerase dimerization. <i> Zhu X, Xie X, Das H, Tan BG, Shi Y, Al-Behadili A, Peter B, Motori E, Valenzuela S, Posse V, Gustafsson CM, Hällberg BM, Falkenberg M. </i> Cell, 2022","date":"2023-06-13T15:27:15.645Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7PZR"}],"region_id":"DP02703r006","statement":[{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":736,"end":769,"reference_id":"35662414","reference_source":"pmid","reference_html":"Non-coding 7S RNA inhibits transcription via mitochondrial RNA polymerase dimerization. <i> Zhu X, Xie X, Das H, Tan BG, Shi Y, Al-Behadili A, Peter B, Motori E, Valenzuela S, Posse V, Gustafsson CM, Hällberg BM, Falkenberg M. </i> Cell, 2022","date":"2023-06-13T15:27:30.742Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7PZR"}],"region_id":"DP02703r007","statement":[{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":1086,"end":1108,"reference_id":"35662414","reference_source":"pmid","reference_html":"Non-coding 7S RNA inhibits transcription via mitochondrial RNA polymerase dimerization. <i> Zhu X, Xie X, Das H, Tan BG, Shi Y, Al-Behadili A, Peter B, Motori E, Valenzuela S, Posse V, Gustafsson CM, Hällberg BM, Falkenberg M. </i> Cell, 2022","date":"2023-06-13T15:27:52.378Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7PZR"}],"region_id":"DP02703r008","statement":[{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02703","date":"2020-03-24T17:26:34.775Z","organism":"Homo sapiens","regions_counter":8,"name":"DNA-directed RNA polymerase, mitochondrial","dataset":["NDDs-related proteins"],"UniParc":"UPI00001347BF","uniref100":"UniRef100_O00411","uniref90":"UniRef90_O00411","uniref50":"UniRef50_O00411","genes":[{"name":{"value":"POLRMT","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9200","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9200"}}]}}],"alphafold_very_low_content":0.11463414634146342,"disorder_content":0.2032520325203252,"disprot_consensus":{"full":[{"start":39,"end":218,"type":"D"},{"start":592,"end":602,"type":"D"},{"start":734,"end":769,"type":"D"},{"start":1086,"end":1108,"type":"D"}],"Structural state":[{"start":39,"end":218,"type":"D"},{"start":592,"end":602,"type":"D"},{"start":734,"end":769,"type":"D"},{"start":1086,"end":1108,"type":"D"}]}},{"acc":"P41214","features":{"gene3D":[{"start":375,"end":474,"id":"G3DSA:1.10.245.10","name":"SWIB/MDM2 domain"},{"start":100,"end":181,"id":"G3DSA:2.30.130.10","name":"PUA domain"}],"pfam":[{"id":"PF01253","name":"Translation initiation factor SUI1","start":490,"end":565},{"id":"PF17832","name":"Pre-PUA-like domain","start":2,"end":90},{"id":"PF25304","name":"eIF2D winged helix domain","start":265,"end":346},{"id":"PF26291","name":"eIF2D, SWIB domain","start":385,"end":467},{"id":"PF26292","name":"elF2D, PUA domain","start":93,"end":175}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MFAKAFRVKSNTAIKGSDRRKLRADVTTAFPTLGTDQVSELVPGKEELNIVKLYAHKGDAVTVYVSGGNPILFELEKNLYPTVYTLWSYPDLLPTFTTWPLVLEKLVGGADLMLPGLVMPPAGLPQVQKGDLCAISLVGNRAPVAIGVAAMSTAEMLTSGLKGRGFSVLHTYQDHLWRSGNKSSPPSIAPLALDSADLSEEKGSVQMDSTLQGDMRHMTLEGEEENGEVHQAREDKSLSEAPEDTSTRGLNQDSTDSKTLQEQMDELLQQCFLHALKCRVKKADLPLLTSTFLGSHMFSCCPEGRQLDIKKSSYKKLSKFLQQMQQEQIIQVKELSKGVESIVAVDWKHPRITSFVIPEPSPTSQTIQEGSREQPYHPPDIKPLYCVPASMTLLFQESGHKKGSFLEGSEVRTIVINYAKKNDLVDADNKNLVRLDPILCDCILEKNEQHTVMKLPWDSLLTRCLEKLQPAYQVTLPGQEPIVKKGRICPIDITLAQRASNKKVTVVRNLEAYGLDPYSVAAILQQRCQASTTVNPAPGAKDSLQVQIQGNQVHHLGWLLLEEYQLPRKHIQGLEKALKPGKKK","length":584,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":259,"region_id":"DP02704r001","start":184,"term_id":"IDPO:0000002","statement":[{"text":"The structures, supported by biochemical experiments, reveal how eIF2D emulates the function of several canonical translation initiation factors by using three independent, flexibly connected RNA binding domains to simultaneously monitor codon-anticodon interactions in the ribosomal P-site and position the initiator tRNA.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28732596","version":2,"reference_html":"Structural and Functional Insights into Human Re-initiation Complexes. <i> Weisser M, Schäfer T, Leibundgut M, Böhringer D, Aylett CHS, Ban N. </i> Mol Cell, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"5OA3"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":373,"region_id":"DP02704r002","start":348,"term_id":"IDPO:0000002","statement":[{"text":"The structures, supported by biochemical experiments, reveal how eIF2D emulates the function of several canonical translation initiation factors by using three independent, flexibly connected RNA binding domains to simultaneously monitor codon-anticodon interactions in the ribosomal P-site and position the initiator tRNA.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28732596","version":2,"reference_html":"Structural and Functional Insights into Human Re-initiation Complexes. <i> Weisser M, Schäfer T, Leibundgut M, Böhringer D, Aylett CHS, Ban N. </i> Mol Cell, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"5OA3"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":373,"region_id":"DP02704r003","start":348,"term_id":"IDPO:0000033","statement":[{"text":"The structures, supported by biochemical experiments, reveal how eIF2D emulates the function of several canonical translation initiation factors by using three independent, flexibly connected RNA binding domains to simultaneously monitor codon-anticodon interactions in the ribosomal P-site and position the initiator tRNA.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28732596","version":3,"reference_html":"Structural and Functional Insights into Human Re-initiation Complexes. <i> Weisser M, Schäfer T, Leibundgut M, Böhringer D, Aylett CHS, Ban N. </i> Mol Cell, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","cross_refs":[{"db":"PDB","id":"5OA3"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":259,"region_id":"DP02704r004","start":184,"term_id":"IDPO:0000033","statement":[{"text":"The structures, supported by biochemical experiments, reveal how eIF2D emulates the function of several canonical translation initiation factors by using three independent, flexibly connected RNA binding domains to simultaneously monitor codon-anticodon interactions in the ribosomal P-site and position the initiator tRNA.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28732596","version":3,"reference_html":"Structural and Functional Insights into Human Re-initiation Complexes. <i> Weisser M, Schäfer T, Leibundgut M, Böhringer D, Aylett CHS, Ban N. </i> Mol Cell, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","cross_refs":[{"db":"PDB","id":"5OA3"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02704","date":"2020-03-24T17:52:23.320Z","organism":"Homo sapiens","regions_counter":4,"name":"Eukaryotic translation initiation factor 2D","dataset":[],"UniParc":"UPI000006CDB6","uniref100":"UniRef100_P41214","uniref90":"UniRef90_P41214","uniref50":"UniRef50_P41214","genes":[{"name":{"value":"EIF2D"},"synonyms":[{"value":"HCA56"},{"value":"LGTN"}]}],"alphafold_very_low_content":0.1523972602739726,"disorder_content":0.17465753424657535,"disprot_consensus":{"full":[{"start":184,"end":259,"type":"D"},{"start":348,"end":373,"type":"D"}],"Structural state":[{"start":184,"end":259,"type":"D"},{"start":348,"end":373,"type":"D"}],"Disorder function":[{"start":184,"end":259,"type":"F"},{"start":348,"end":373,"type":"F"}]}},{"acc":"P45379","features":{"gene3D":[{"start":173,"end":298,"id":"G3DSA:1.20.5.350","name":"G3DSA:1.20.5.350"}],"pfam":[{"id":"PF00992","name":"Troponin","start":103,"end":240}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MSDIEEVVEEYEEEEQEEAAVEEEEDWREDEDEQEEAAEEDAEAEAETEETRAEEDEEEEEAKEAEDGPMEESKPKPRSFMPNLVPPKIPDGERVDFDDIHRKRMEKDLNELQALIEAHFENRKKEEEELVSLKDRIERRRAERAEQQRIRNEREKERQNRLAEERARREEEENRRKAEDEARKKKALSNMMHFGGYIQKQAQTERKSGKRQTEREKKKKILAERRKVLAIDHLNEDQLREKAKELWQSIYNLEAEKFDLQEKFKQQKYEINVLRNRINDNQKVSKTRGKAKVTGRWK","length":298,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":212,"region_id":"DP02705r001","start":193,"term_id":"IDPO:0000002","statement":[{"text":"Further upstream of H1(T2), residues 183–202 of TnT were not defined in the electron density map.","type":"Article"},{"text":"IDR corresponding to region 193-212 on the amino acid sequence.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12840750","version":2,"reference_html":"Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form. <i> Takeda S, Yamashita A, Maeda K, Maéda Y. </i> Nature, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1J1E"},{"db":"PDB","id":"1J1D"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":288,"region_id":"DP02705r002","start":272,"term_id":"IDPO:0000002","statement":[{"text":"The C terminus of TnT (denoted as C-TnT, residues 272–288), which has been shown to bind to tropomyosin is not always defined in the crystal (the residues down to 276 are defined in Tn52KB)","type":"Article"},{"text":"As described above, most of the electron densities associated with the potential actin–tropomyosin interfaces are ambiguous. These include the inhibitory region (residues 137–148) and the C-terminus of TnI (residues 163–210 in Tn52KA and 192–210 in Tn52KB), and the C-TnT (residues 272–288).","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12840750","version":2,"reference_html":"Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form. <i> Takeda S, Yamashita A, Maeda K, Maéda Y. </i> Nature, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1J1E"},{"db":"PDB","id":"1J1D"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":66,"reference_id":"https://mobidb.org/P45379","reference_source":"mobidb","reference_html":"An Entry Referenced from MobiDB","date":"2022-02-14T09:00:00.000Z","curator_id":"amonzon","curator_name":"Alex Monzon","curator_orcid":"0000-0003-0362-8218","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007759","ec_ontology":"ECO","ec_name":"curator inference from database used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP02705r004","statement":[{"text":"This poly-E region is inferred by the curator to be disordered, based on MobiDB-Lite and according to experimental evidence demonstrating that poly-E repeats display random-coil-like conformation (PMID:16949547)","type":"Curator statement"}],"ec_go":"IC","disprot_namespace":"Structural state"}],"released":"2020_12","ncbi_taxon_id":9606,"disprot_id":"DP02705","date":"2020-03-24T18:24:01.542Z","organism":"Homo sapiens","regions_counter":4,"name":"Troponin T, cardiac muscle","dataset":[],"UniParc":"UPI0000137657","uniref100":"UniRef100_P45379","uniref90":"UniRef90_P45379","uniref50":"UniRef50_P45379","genes":[{"name":{"value":"TNNT2"}}],"alphafold_very_low_content":0.10067114093959731,"disorder_content":0.34563758389261745,"disprot_consensus":{"full":[{"start":1,"end":66,"type":"D"},{"start":193,"end":212,"type":"D"},{"start":272,"end":288,"type":"D"}],"Structural state":[{"start":1,"end":66,"type":"D"},{"start":193,"end":212,"type":"D"},{"start":272,"end":288,"type":"D"}]}},{"acc":"Q9NXV2","features":{"gene3D":[],"pfam":[{"id":"PF02214","name":"BTB/POZ domain","start":46,"end":134},{"id":"PF31093","name":"KCTD2/KCTD5/KCTD17 C-terminal domain","start":155,"end":209}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MAENHCELLSPARGGIGAGLGGGLCRRCSAGLGALAQRPGSVSKWVRLNVGGTYFLTTRQTLCRDPKSFLYRLCQADPDLDSDKDETGAYLIDRDPTYFGPVLNYLRHGKLVINKDLAEEGVLEEAEFYNITSLIKLVKDKIRERDSKTSQVPVKHVYRVLQCQEEELTQMVSTMSDGWKFEQLVSIGSSYNYGNEDQAEFLCVVSKELHNTPYGTASEPSEKAKILQERGSRM","length":234,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":234,"region_id":"DP02706r001","start":212,"term_id":"IDPO:0000002","statement":[{"text":"C-terminal residues 212–234 were not visible in electron density maps. Residues 34–43 adopt different conformations in high- and low-salt crystals. Other flexible regions include residues 77–82 near the α2-helix and residues 188–200 near theβ5-β6 loops.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19361449","version":2,"reference_html":"Pentameric assembly of potassium channel tetramerization domain-containing protein 5. <i> Dementieva IS, Tereshko V, McCrossan ZA, Solomaha E, Araki D, Xu C, Grigorieff N, Goldstein SA. </i> J Mol Biol, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3DRZ"},{"db":"PDB","id":"3DRX"},{"db":"PDB","id":"3DRY"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":200,"region_id":"DP02706r002","start":188,"term_id":"IDPO:0000002","statement":[{"text":"C-terminal residues 212–234 were not visible in electron density maps. Residues 34–43 adopt different conformations in high- and low-salt crystals. Other flexible regions include residues 77–82 near the α2-helix and residues 188–200 near theβ5-β6 loops.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19361449","version":2,"reference_html":"Pentameric assembly of potassium channel tetramerization domain-containing protein 5. <i> Dementieva IS, Tereshko V, McCrossan ZA, Solomaha E, Araki D, Xu C, Grigorieff N, Goldstein SA. </i> J Mol Biol, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3DRZ"},{"db":"PDB","id":"3DRX"},{"db":"PDB","id":"3DRY"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02706","date":"2020-03-24T19:17:18.762Z","organism":"Homo sapiens","regions_counter":2,"name":"BTB/POZ domain-containing protein KCTD5","dataset":[],"UniParc":"UPI0000073110","uniref100":"UniRef100_Q9NXV2","uniref90":"UniRef90_Q9NXV2","uniref50":"UniRef50_Q9NXV2","genes":[{"name":{"value":"KCTD5"}}],"alphafold_very_low_content":0.21794871794871795,"disorder_content":0.15384615384615385,"disprot_consensus":{"full":[{"start":188,"end":200,"type":"D"},{"start":212,"end":234,"type":"D"}],"Structural state":[{"start":188,"end":200,"type":"D"},{"start":212,"end":234,"type":"D"}]}},{"acc":"P25891","features":{"gene3D":[{"start":22,"end":209,"id":"G3DSA:3.40.420.10","name":"Ricin (A subunit), domain 1"},{"start":210,"end":286,"id":"G3DSA:4.10.470.10","name":"Ricin (A Subunit), domain 2"}],"pfam":[{"id":"PF00161","name":"Ribosome inactivating protein","start":33,"end":248}]},"creator":"fquaglia","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","PACMAD clade","Panicoideae","Andropogonodae","Andropogoneae","Tripsacinae","Zea"],"sequence":"MAEITLEPSDLMAQTNKRIVPKFTEIFPVEDANYPYSAFIASVRKDVIKHCTDHKGIFQPVLPPEKKVPELWLYTELKTRTSSITLAIRMDNLYLVGFRTPGGVWWEFGKDGDTHLLGDNPRWLGFGGRYQDLIGNKGLETVTMGRAEMTRAVNDLAKKKKMATLEEEEVQMQMQMPEAADLAAAAAADPQADTKSKLVKLVVMVCEGLRFNTVSRTVDAGFNSQHGVTLTVTQGKQVQKWDRISKAAFEWADHPTAVIPDMQKLGIKDKNEAARIVALVKNQTTACATAASADNDDDEA","length":300,"dataset":[],"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":179,"region_id":"DP02707r001","start":163,"term_id":"IDPO:0000002","statement":[{"text":"In Pro-RIP, the internal inactivating region Ala163–Asp189 is very rich in acidic residues. Our structure shows that the internal inactivating region consists of a flexible loop (Ala163–Ala179) and a long α-helix (Ala180–Ala188)","type":"Discussion"},{"text":"In the precursor, the inactivation region is found on the protein surface and consists of a flexible loop followed by a long alpha-helix. This region diminished both the interaction with ribosome and cytotoxicity, but not cellular uptake.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17855394","version":2,"reference_html":"Structure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active site. <i> Mak AN, Wong YT, An YJ, Cha SS, Sze KH, Au SW, Wong KB, Shaw PC. </i> Nucleic Acids Res, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2PQG"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":179,"region_id":"DP02707r002","start":163,"term_id":"GO:0098772","statement":[{"text":"In Pro-RIP, the internal inactivating region Ala163–Asp189 is very rich in acidic residues. Our structure shows that the internal inactivating region consists of a flexible loop (Ala163–Ala179) and a long α-helix (Ala180–Ala188)","type":"Discussion"},{"text":"In the precursor, the inactivation region is found on the protein surface and consists of a flexible loop followed by a long alpha-helix. This region diminished both the interaction with ribosome and cytotoxicity, but not cellular uptake.","type":"Abstract"},{"text":"Among the sequences to be removed during the activation of maize RIP, the 25 aa internal region (known as internal inactivation region) is the most crucial, as removal of this region increases the activity by at least 600-fold, whereas removal of the N- or C-terminal region only increases the activity by 6- or 5-fold, respectively","type":"Introduction"},{"text":"These indicated that the internal inactivation region of Pro-RIP might obstruct the protein to dock onto the ribosome.","type":"Results"},{"text":"Therefore, the internal inactivation region may serve the purpose of preventing the maize RIP from attacking its cognate ribosomes in vivo.","type":"Results"},{"text":"The internal inactivation region is removed in the active form","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"17855394","version":3,"reference_html":"Structure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active site. <i> Mak AN, Wong YT, An YJ, Cha SS, Sze KH, Au SW, Wong KB, Shaw PC. </i> Nucleic Acids Res, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2PQG"}],"term_name":"molecular function regulator","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":4577,"disprot_id":"DP02707","date":"2020-03-24T19:29:20.854Z","organism":"Zea mays","regions_counter":2,"name":"Ribosome-inactivating protein 3","UniParc":"UPI0000034B75","uniref100":"UniRef100_P25891","uniref90":"UniRef90_P25891","uniref50":"UniRef50_P10593","genes":[{"name":{"value":"CRIP3"}}],"alphafold_very_low_content":0.09333333333333334,"disorder_content":0.056666666666666664,"disprot_consensus":{"full":[{"start":163,"end":179,"type":"D"}],"Structural state":[{"start":163,"end":179,"type":"D"}],"Molecular function":[{"start":163,"end":179,"type":"F"}]}},{"acc":"P04035","features":{"gene3D":[{"start":587,"end":703,"id":"G3DSA:3.30.70.420","name":"G3DSA:3.30.70.420"},{"start":537,"end":858,"id":"G3DSA:3.90.770.10","name":"3-hydroxy-3-methylglutaryl-coenzyme A Reductase; Chain A, domain 2"},{"start":449,"end":536,"id":"G3DSA:1.10.3270.10","name":"HMGR, N-terminal domain"}],"pfam":[{"id":"PF00368","name":"Hydroxymethylglutaryl-coenzyme A reductase","start":492,"end":871},{"id":"PF12349","name":"Sterol-sensing domain of SREBP cleavage-activation","start":87,"end":222}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MLSRLFRMHGLFVASHPWEVIVGTVTLTICMMSMNMFTGNNKICGWNYECPKFEEDVLSSDIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTGLNEALPFFLLLIDLSRASTLAKFALSSNSQDEVRENIARGMAILGPTFTLDALVECLVIGVGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFARVLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADPSPQNSTADTSKVSLGLDENVSKRIEPSVSLWQFYLSKMISMDIEQVITLSLALLLAVKYIFFEQTETESTLSLKNPITSPVVTQKKVPDNCCRREPMLVRNNQKCDSVEEETGINRERKVEVIKPLVAETDTPNRATFVVGNSSLLDTSSVLVTQEPEIELPREPRPNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYKLETLMETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGVAGPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRACDSAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMISKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREVLKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAAGHLVKSHMIHNRSKINLQDLQGACTKKTA","length":888,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":888,"region_id":"DP02709r001","start":861,"term_id":"IDPO:0000002","statement":[{"text":"Near the carboxyl terminus of HMGR, several catalytically relevant residues are disordered in the enzyme-statin complexes. If these residues were not flexible, they would sterically hinder statin binding.","type":"Abstract"},{"text":"In the electron-density maps of the statin-complex structures, residues COOH-terminal to Gly860 are missing.","type":"Article"},{"text":"In the statin-bound structures, these residues are disordered, revealing a shallow hydrophobic groove that accommodates the hydrophobic moieties of the statins.","type":"Article"},{"text":"The structurally diverse, rigid hydrophobic groups of the statins are accommodated in a shallow non-polar groove that is present only when COOH-terminal residues of HMGR are disordered.","type":"Article"},{"text":"Statins are HMGR inhibitors. Here HMGR is complexed with six different statins: rosuvastatin (PDB:1hwl), cerivastatin (PDB:1hwj), fluvastatin (PDB:1hwi), mevastatin (PDB:1hw8), atorvastatin (PDB:1hwk), simvastatin (PDB:1hw9).","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11349148","version":2,"reference_html":"Structural mechanism for statin inhibition of HMG-CoA reductase. <i> Istvan ES, Deisenhofer J. </i> Science, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1HWL"},{"db":"PDB","id":"1HWJ"},{"db":"PDB","id":"1HWI"},{"db":"PDB","id":"1HW8"},{"db":"PDB","id":"1HWK"},{"db":"PDB","id":"1HW9"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":888,"region_id":"DP02709r002","start":861,"term_id":"IDPO:0000031","statement":[{"text":"Near the carboxyl terminus of HMGR, several catalytically relevant residues are disordered in the enzyme-statin complexes. If these residues were not flexible, they would sterically hinder statin binding.","type":"Abstract"},{"text":"In the electron-density maps of the statin-complex structures, residues COOH-terminal to Gly860 are missing.","type":"Article"},{"text":"In the statin-bound structures, these residues are disordered, revealing a shallow hydrophobic groove that accommodates the hydrophobic moieties of the statins.","type":"Article"},{"text":"The structurally diverse, rigid hydrophobic groups of the statins are accommodated in a shallow non-polar groove that is present only when COOH-terminal residues of HMGR are disordered.","type":"Article"},{"text":"It appears that the innate flexibility of the COOH-terminal region of HMGR is fortuitously exploited by statins to create a binding site for the inhibitor molecules.","type":"Article"},{"text":"Statins exploit the conformational flexibility of HMGR to create a hydrophobic binding pocket near the active site.","type":"Figure"},{"text":"Statins are HMGR inhibitors. Here HMGR is complexed with six different statins: rosuvastatin (PDB:1hwl), cerivastatin (PDB:1hwj), fluvastatin (PDB:1hwi), mevastatin (PDB:1hw8), atorvastatin (PDB:1hwk), simvastatin (PDB:1hw9).","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11349148","version":3,"reference_html":"Structural mechanism for statin inhibition of HMG-CoA reductase. <i> Istvan ES, Deisenhofer J. </i> Science, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1HWL"},{"db":"PDB","id":"1HWJ"},{"db":"PDB","id":"1HWI"},{"db":"PDB","id":"1HW8"},{"db":"PDB","id":"1HWK"},{"db":"PDB","id":"1HW9"}],"term_name":"flexible C-terminal tail","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":888,"region_id":"DP02709r003","start":861,"term_id":"GO:0098772","statement":[{"text":"Near the carboxyl terminus of HMGR, several catalytically relevant residues are disordered in the enzyme-statin complexes. If these residues were not flexible, they would sterically hinder statin binding.","type":"Abstract"},{"text":"In the electron-density maps of the statin-complex structures, residues COOH-terminal to Gly860 are missing.","type":"Article"},{"text":"In the statin-bound structures, these residues are disordered, revealing a shallow hydrophobic groove that accommodates the hydrophobic moieties of the statins.","type":"Article"},{"text":"The structurally diverse, rigid hydrophobic groups of the statins are accommodated in a shallow non-polar groove that is present only when COOH-terminal residues of HMGR are disordered.","type":"Article"},{"text":"It appears that the innate flexibility of the COOH-terminal region of HMGR is fortuitously exploited by statins to create a binding site for the inhibitor molecules.","type":"Article"},{"text":"Statins exploit the conformational flexibility of HMGR to create a hydrophobic binding pocket near the active site.","type":"Figure"},{"text":"Statins are HMGR inhibitors. Here HMGR is complexed with six different statins: rosuvastatin (PDB:1hwl), cerivastatin (PDB:1hwj), fluvastatin (PDB:1hwi), mevastatin (PDB:1hw8), atorvastatin (PDB:1hwk), simvastatin (PDB:1hw9).","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11349148","version":3,"reference_html":"Structural mechanism for statin inhibition of HMG-CoA reductase. <i> Istvan ES, Deisenhofer J. </i> Science, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1HWL"},{"db":"PDB","id":"1HWJ"},{"db":"PDB","id":"1HWI"},{"db":"PDB","id":"1HW8"},{"db":"PDB","id":"1HWK"},{"db":"PDB","id":"1HW9"}],"term_name":"molecular function regulator","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02709","date":"2020-03-25T09:49:35.080Z","organism":"Homo sapiens","regions_counter":3,"name":"3-hydroxy-3-methylglutaryl-coenzyme A reductase","dataset":["Age-related disorders proteins"],"UniParc":"UPI000012C9E2","uniref100":"UniRef100_P04035","uniref90":"UniRef90_P04035","uniref50":"UniRef50_P04035","genes":[{"name":{"value":"HMGCR","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:5006","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:5006"}}]}}],"alphafold_very_low_content":0.19594594594594594,"disorder_content":0.03153153153153153,"disprot_consensus":{"full":[{"start":861,"end":888,"type":"D"}],"Structural state":[{"start":861,"end":888,"type":"D"}],"Disorder function":[{"start":861,"end":888,"type":"F"}],"Molecular function":[{"start":861,"end":888,"type":"F"}]}},{"acc":"Q9BQ50","features":{"gene3D":[{"start":7,"end":222,"id":"G3DSA:3.30.420.10","name":"Ribonuclease H-like superfamily/Ribonuclease H"}],"pfam":[]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MSEAPRAETFVFLDLEATGLPSVEPEIAELSLFAVHRSSLENPEHDESGALVLPRVLDKLTLCMCPERPFTAKASEITGLSSEGLARCRKAGFDGAVVRTLQAFLSRQAGPICLVAHNGFDYDFPLLCAELRRLGARLPRDTVCLDTLPALRGLDRAHSHGTRARGRQGYSLGSLFHRYFRAEPSAAHSAEGDVHTLLLIFLHRAAELLAWADEQARGWAHIEPMYLPPDDPSLEA","length":236,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":168,"region_id":"DP02710r001","start":159,"term_id":"IDPO:0000002","statement":[{"text":"Three segments spanning residues 159–168, 185–187, and 229–236 were disordered in both monomers and omitted from the crystallographic model.","type":"Results"},{"text":"Adjacent to each active site is a flexible region containing three arginines positioned appropriately to bind DNA and to control its entry into the active site.","type":"Abstract"},{"text":"This loop is largely disordered, indicating that it is somewhat mobile, and it contains the positively charged arginines at positions 163, 165, and 167. ","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15661738","version":2,"reference_html":"The human TREX2 3' -> 5'-exonuclease structure suggests a mechanism for efficient nonprocessive DNA catalysis. <i> Perrino FW, Harvey S, McMillin S, Hollis T. </i> J Biol Chem, 2005","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1Y97"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":168,"region_id":"DP02710r002","start":159,"term_id":"GO:0003677","statement":[{"text":"Three segments spanning residues 159–168, 185–187, and 229–236 were disordered in both monomers and omitted from the crystallographic model.","type":"Results"},{"text":"Adjacent to each active site is a flexible region containing three arginines positioned appropriately to bind DNA and to control its entry into the active site.","type":"Abstract"},{"text":"This loop is largely disordered, indicating that it is somewhat mobile, and it contains the positively charged arginines at positions 163, 165, and 167. ","type":"Results"},{"text":"Arginines 163, 165, and 167 within the loop are unique to TREX2 and strongly contribute to its high affinity for DNA","type":"Figure"},{"text":"The position of the active sites in the TREX2 dimer and the adjacent flexible region provides an explanation for the tight DNA binding and robust catalytic activity of the TREX2 enzyme.","type":"Introduction"},{"text":"Involvement of all three of the arginines positioned at 163, 165, and 167 on the flexible loop is supported by additional mutagenesis studies that demonstrate contributions to DNA binding by each of the individual arginines in TREX2.","type":"Discussion"},{"text":"These data suggest a model for TREX2 catalysis in which the negatively charged phosphodiester backbone of DNA is first bound by the positively charged arginine residues present on this flexible loop, and the DNA is subsequently moved into the active site for catalysis.","type":"Discussion"},{"text":"Together, the efficient excision of 3′-terminal nucleotides facilitated by a presumed two-metal ion mechanism of phosphodiester bond cleavage similar to that proposed for the exonuclease of E. coli DNA polymerase I and the efficient binding and movement of the DNA substrate into the active site by the α6–α7 flexible loop can account for the robust nature of the TREX2 enzyme.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15661738","version":3,"reference_html":"The human TREX2 3' -> 5'-exonuclease structure suggests a mechanism for efficient nonprocessive DNA catalysis. <i> Perrino FW, Harvey S, McMillin S, Hollis T. </i> J Biol Chem, 2005","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1Y97"}],"term_name":"DNA binding","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":168,"region_id":"DP02710r003","start":159,"term_id":"GO:0060090","statement":[{"text":"Adjacent to each active site is a flexible region containing three arginines positioned appropriately to bind DNA and to control its entry into the active site.","type":"Abstract"},{"text":"These data suggest a model for TREX2 catalysis in which the negatively charged phosphodiester backbone of DNA is first bound by the positively charged arginine residues present on this flexible loop, and the DNA is subsequently moved into the active site for catalysis.","type":"Discussion"},{"text":"Together, the efficient excision of 3′-terminal nucleotides facilitated by a presumed two-metal ion mechanism of phosphodiester bond cleavage similar to that proposed for the exonuclease of E. coli DNA polymerase I and the efficient binding and movement of the DNA substrate into the active site by the α6–α7 flexible loop can account for the robust nature of the TREX2 enzyme.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15661738","version":3,"reference_html":"The human TREX2 3' -> 5'-exonuclease structure suggests a mechanism for efficient nonprocessive DNA catalysis. <i> Perrino FW, Harvey S, McMillin S, Hollis T. </i> J Biol Chem, 2005","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1Y97"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":168,"region_id":"DP02710r004","start":159,"term_id":"GO:0098772","statement":[{"text":"Adjacent to each active site is a flexible region containing three arginines positioned appropriately to bind DNA and to control its entry into the active site.","type":"Abstract"},{"text":"These data suggest a model for TREX2 catalysis in which the negatively charged phosphodiester backbone of DNA is first bound by the positively charged arginine residues present on this flexible loop, and the DNA is subsequently moved into the active site for catalysis.","type":"Discussion"},{"text":"Together, the efficient excision of 3′-terminal nucleotides facilitated by a presumed two-metal ion mechanism of phosphodiester bond cleavage similar to that proposed for the exonuclease of E. coli DNA polymerase I and the efficient binding and movement of the DNA substrate into the active site by the α6–α7 flexible loop can account for the robust nature of the TREX2 enzyme.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15661738","version":3,"reference_html":"The human TREX2 3' -> 5'-exonuclease structure suggests a mechanism for efficient nonprocessive DNA catalysis. <i> Perrino FW, Harvey S, McMillin S, Hollis T. </i> J Biol Chem, 2005","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1Y97"}],"term_name":"molecular function regulator","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02710","date":"2020-03-25T10:56:51.076Z","organism":"Homo sapiens","regions_counter":5,"name":"Three prime repair exonuclease 2","dataset":[],"UniParc":"UPI000006ECFE","uniref100":"UniRef100_Q9BQ50","uniref90":"UniRef90_Q9BQ50","uniref50":"UniRef50_Q9BQ50","genes":[{"name":{"value":"TREX2"}}],"alphafold_very_low_content":0.029661016949152543,"disorder_content":0.0423728813559322,"disprot_consensus":{"full":[{"start":159,"end":168,"type":"D"}],"Structural state":[{"start":159,"end":168,"type":"D"}],"Molecular function":[{"start":159,"end":168,"type":"F"}]}},{"acc":"Q9V6K1","features":{"gene3D":[{"start":110,"end":620,"id":"G3DSA:3.40.50.200","name":"Peptidase S8/S53 domain"}],"pfam":[{"id":"PF00082","name":"Subtilase family","start":122,"end":600},{"id":"PF12580","name":"Tripeptidyl peptidase II","start":892,"end":1076},{"id":"PF12583","name":"Tripeptidyl peptidase II, C-terminal","start":1181,"end":1248},{"id":"PF21223","name":"Tripeptidyl-peptidase II, first Ig-like domain","start":622,"end":738},{"id":"PF21316","name":"TPPII, galactose-binding domain-like","start":765,"end":856}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"sequence":"MFNRFRLVHKQLRLYKNFGLLGQKASVGLTLPIISLSRPYMAYMGTERSVVMITAPATKEFAESSERSNSSKKTTNKEQSDKSAESRMATSGIVESFPTGALVPKAETGVLNFLQKYPEYDGRDVTIAIFDSGVDPRATGLETLCDGKTVKVIERYDCSGCGDVDMKKKVTPDENGNIKGLSGNSLKLSPELMALNTDPEKAVRVGLKSFSDLLPSKVRNNIVAQAKLKHWDKPHKTATANASRKIVEFESQNPGEASKLPWDKKILKENLDFELEMLNSYEKVYGDIKTSYDCILFPTADGWLTIVDTTEQGDLDQALRIGEYSRTHETRNVDDFLSISVNVHDEGNVLEVVGMSSPHGTHVSSIASGNHSSRDVDGVAPNAKIVSMTIGDGRLGSMETGTALVRAMTKVMELCRDGRRIDVINMSYGEHANWSNSGRIGELMNEVVNKYGVVWVASAGNHGPALCTVGTPPDISQPSLIGVGAYVSPQMMEAEYAMREKLPGNVYTWTSRDPCIDGGQGVTVCAPGGAIASVPQFTMSKSQLMNGTSMAAPHVAGAVALLISGLKQQNIEYSPYSIKRAISVTATKLGYVDPFAQGHGLLNVEKAFEHLTEHRQSKDNMLRFSVRVGNNADKGIHLRQGVQRNSIDYNVYIEPIFYNDKEADPKDKFNFNVRLNLIASQPWVQCGAFLDLSYGTRSIAVRVDPTGLQPGVHSAVIRAYDTDCVQKGSLFEIPVTVVQPHVLESDQNTPVFEPASSKGDNSVEFQPNTIQRDFILVPERATWAELRMRITDPNRGEDIGKFFVHTNQLLPKQSCRKLETMKIVSVGSENESIMAFKVKSGRILELCIAKYWSNYGQSHLKYSLRFRGVEAHNPNAYVMHAGRGIHKLEIEALVAEDVQPQLQLKNAEVVLKPTEAKISPLSATRDVIPDGRQVYQNLLAFNLNVAKAADVSIYAPIFNDLLYEAEFESQMWMLFDANKALVATGDAHSHTSFTKLDKGEYTIRLQVRHEKRDLLEKISEANLVASFKLTSPLTLDFYENYNQCIVGGRKYVSSPLRLSTRVLYIAPITQERLTKANLPAQCAWLSGNLVFPQDEVGRRVAQHPFTYILNPAEKKSHTNGSSNGSSAAGSTATAAAVTTANGAKPKAPATPQAATSVTNPAAGDGISVQNDPPVDSSGSPASPKKGKANADDYAESFRDFQCSQIVKCELEMAEKIYNDVVAAHPKHLQANLLLIQNIESNQLKSQLPLTFVNAQKTSPPEAGESADKQKEDQKKVRSALERIVKLADKVIQETDSEALLSYYGLKNDTRADAAKIKTNMDKQKNTLIEALSKKGIAVAKLAVLDDCIKDSLAEINELYTEIIKFVDANDSKAIQFALWHAYAHGHYGRMYKYVVKLIEEKRTRDHFVELAAINGALGHEHIRTVINRMMITAFPSSFRLF","length":1441,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":417,"region_id":"DP02711r001","start":408,"term_id":"IDPO:0000002","statement":[{"text":"Furthermore, the structure suggests a model for activation of TPP II involving the relocation of a flexible loop and a repositioning of the active–site serine, coupling it to holocomplex assembly and active site sequestration.","type":"Abstract"},{"text":"Density for most of the structure was observed; the disordered regions were limited to a few predicted loop regions, which were not modelled due to lack of density or weak density (Fig. 1a, c). These loops include residues Asn90–Pro112, loop “L1” (Glu408–Gly417), which is highly conserved and unique to the TPP II family, residues Gly442–Gln456 of loop “L2” (Gly441–Gly460), which is likewise highly conserved and contains active–site residue Ser462 at its C–terminal side, and loop “L3” (Lys1027–Lys1098) which is substantially shorter in human TPP II and is prone to nicking in both purified Drosophila and human TPP II with no observable effect on activity.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20676100","version":2,"reference_html":"Hybrid molecular structure of the giant protease tripeptidyl peptidase II. <i> Chuang CK, Rockel B, Seyit G, Walian PJ, Schönegge AM, Peters J, Zwart PH, Baumeister W, Jap BK. </i> Nat Struct Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3LXU"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":456,"region_id":"DP02711r002","start":442,"term_id":"IDPO:0000002","statement":[{"text":"Furthermore, the structure suggests a model for activation of TPP II involving the relocation of a flexible loop and a repositioning of the active–site serine, coupling it to holocomplex assembly and active site sequestration.","type":"Abstract"},{"text":"Density for most of the structure was observed; the disordered regions were limited to a few predicted loop regions, which were not modelled due to lack of density or weak density (Fig. 1a, c). These loops include residues Asn90–Pro112, loop “L1” (Glu408–Gly417), which is highly conserved and unique to the TPP II family, residues Gly442–Gln456 of loop “L2” (Gly441–Gly460), which is likewise highly conserved and contains active–site residue Ser462 at its C–terminal side, and loop “L3” (Lys1027–Lys1098) which is substantially shorter in human TPP II and is prone to nicking in both purified Drosophila and human TPP II with no observable effect on activity.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20676100","version":2,"reference_html":"Hybrid molecular structure of the giant protease tripeptidyl peptidase II. <i> Chuang CK, Rockel B, Seyit G, Walian PJ, Schönegge AM, Peters J, Zwart PH, Baumeister W, Jap BK. </i> Nat Struct Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3LXU"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1098,"region_id":"DP02711r003","start":1027,"term_id":"IDPO:0000002","statement":[{"text":"Furthermore, the structure suggests a model for activation of TPP II involving the relocation of a flexible loop and a repositioning of the active–site serine, coupling it to holocomplex assembly and active site sequestration.","type":"Abstract"},{"text":"Density for most of the structure was observed; the disordered regions were limited to a few predicted loop regions, which were not modelled due to lack of density or weak density (Fig. 1a, c). These loops include residues Asn90–Pro112, loop “L1” (Glu408–Gly417), which is highly conserved and unique to the TPP II family, residues Gly442–Gln456 of loop “L2” (Gly441–Gly460), which is likewise highly conserved and contains active–site residue Ser462 at its C–terminal side, and loop “L3” (Lys1027–Lys1098) which is substantially shorter in human TPP II and is prone to nicking in both purified Drosophila and human TPP II with no observable effect on activity.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20676100","version":2,"reference_html":"Hybrid molecular structure of the giant protease tripeptidyl peptidase II. <i> Chuang CK, Rockel B, Seyit G, Walian PJ, Schönegge AM, Peters J, Zwart PH, Baumeister W, Jap BK. </i> Nat Struct Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3LXU"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":7227,"disprot_id":"DP02711","date":"2020-03-25T11:30:38.128Z","organism":"Drosophila melanogaster","regions_counter":3,"name":"Tripeptidyl-peptidase 2","dataset":[],"UniParc":"UPI0000083289","uniref100":"UniRef100_Q9V6K1","uniref90":"UniRef90_Q9V6K1","uniref50":"UniRef50_Q9V6K1","genes":[{"name":{"value":"TppII"},"orfNames":[{"value":"CG3991"}]}],"alphafold_very_low_content":0.1179736294240111,"disorder_content":0.06731436502428868,"disprot_consensus":{"full":[{"start":408,"end":417,"type":"D"},{"start":442,"end":456,"type":"D"},{"start":1027,"end":1098,"type":"D"}],"Structural state":[{"start":408,"end":417,"type":"D"},{"start":442,"end":456,"type":"D"},{"start":1027,"end":1098,"type":"D"}]}},{"acc":"Q9H3P2","features":{"gene3D":[],"pfam":[{"id":"PF23553","name":"NELF-A N-terminal domain","start":8,"end":153}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MASMRESDTGLWLHNKLGATDELWAPPSIASLLTAAVIDNIRLCFHGLSSAVKLKLLLGTLHLPRRTVDEMKGALMEIIQLASLDSDPWVLMVADILKSFPDTGSLNLELEEQNPNVQDILGELREKVGECEASAMLPLECQYLNKNALTTLAGPLTPPVKHFQLKRKPKSATLRAELLQKSTETAQQLKRSAGVPFHAKGRGLLRKMDTTTPLKGIPKQAPFRSPTAPSVFSPTGNRTPIPPSRTLLRKERGVKLLDISELDMVGAGREAKRRRKTLDAEVVEKPAKEETVVENATPDYAAGLVSTQKLGSLNNEPALPSTSYLPSTPSVVPASSYIPSSETPPAPSSREASRPPEEPSAPSPTLPAQFKQRAPMYNSGLSPATPTPAAPTSPLTPTTPPAVAPTTQTPPVAMVAPQTQAPAQQQPKKNLSLTREQMFAAQEMFKTANKVTRPEKALILGFMAGSRENPCQEQGDVIQIKLSEHTEDLPKADGQGSTTMLVDTVFEMNYATGQWTRFKKYKPMTNVS","length":528,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":528,"region_id":"DP02712r001","start":189,"term_id":"IDPO:0000002","statement":[{"text":"Additionally, NELF possesses two flexible 'tentacles' that can contact DSIF and exiting RNA.","type":"Abstract"},{"text":"It also unveiled that NELF comprises three structured lobes and two flexible tentacles that approach DSIF and exiting RNA.","type":"Discussion"},{"text":"Residues 189-528 of NELF-A form a flexible tentacle that binds Pol II and DSIF.","type":"Figure"},{"text":"Negative elongation factor (NELF), is composed of the four subunits NELF-A, -B, -C (or isoform NELF-D that lacks the first nine NELF-C residues), and -E. One of the two flexible \"tentacles\" is in NELF-A, the other flexible \"tentacle\" is in NELF-E. They contact DSIF, composed of SPT5 and SPT4","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30135580","version":2,"reference_html":"Structure of paused transcription complex Pol II-DSIF-NELF. <i> Vos SM, Farnung L, Urlaub H, Cramer P. </i> Nature, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6GML"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP02712r002","ec_ontology":"ECO","end":528,"term_id":"GO:0005515","start":189,"version":3,"statement":[{"text":"Additionally, NELF possesses two flexible 'tentacles' that can contact DSIF and exiting RNA.","type":"Abstract"},{"text":"It also unveiled that NELF comprises three structured lobes and two flexible tentacles that approach DSIF and exiting RNA.","type":"Discussion"},{"text":"Residues 189-528 of NELF-A form a flexible tentacle that binds Pol II and DSIF.","type":"Figure"},{"text":"Negative elongation factor (NELF), is composed of the four subunits NELF-A, -B, -C (or isoform NELF-D that lacks the first nine NELF-C residues), and -E. One of the two flexible \"tentacles\" is in NELF-A, the other flexible \"tentacle\" is in NELF-E. They contact DSIF, composed of SPT5 and SPT4","type":"Curator statement"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P63272","partner_end":null},{"partner_start":null,"db":"UniProt","id":"O00267","partner_end":null},{"partner_start":null,"db":"UniProt","id":"P60899","partner_end":null},{"partner_start":null,"db":"UniProt","id":"I3LGP4","partner_end":null},{"partner_start":null,"db":"UniProt","id":"I3LJR4","partner_end":null}],"term_name":"protein binding","ec_name":"cryogenic electron microscopy evidence used in manual assertion","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"30135580","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6GML"}],"term_namespace":"Molecular function","ec_id":"ECO:0006208","curator_id":"fquaglia","reference_html":"Structure of paused transcription complex Pol II-DSIF-NELF. <i> Vos SM, Farnung L, Urlaub H, Cramer P. </i> Nature, 2018","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":528,"region_id":"DP02712r003","start":189,"term_id":"GO:0060090","statement":[{"text":"Additionally, NELF possesses two flexible 'tentacles' that can contact DSIF and exiting RNA.","type":"Abstract"},{"text":"It also unveiled that NELF comprises three structured lobes and two flexible tentacles that approach DSIF and exiting RNA.","type":"Discussion"},{"text":"Residues 189-528 of NELF-A form a flexible tentacle that binds Pol II and DSIF.","type":"Figure"},{"text":"Negative elongation factor (NELF), is composed of the four subunits NELF-A, -B, -C (or isoform NELF-D that lacks the first nine NELF-C residues), and -E. One of the two flexible \"tentacles\" is in NELF-A, the other flexible \"tentacle\" is in NELF-E. They contact DSIF, composed of SPT5 and SPT4","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"30135580","version":3,"reference_html":"Structure of paused transcription complex Pol II-DSIF-NELF. <i> Vos SM, Farnung L, Urlaub H, Cramer P. </i> Nature, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","cross_refs":[{"db":"PDB","id":"6GML"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":528,"region_id":"DP02712r004","start":189,"term_id":"GO:0060090","statement":[{"text":"Additionally, NELF possesses two flexible 'tentacles' that can contact DSIF and exiting RNA.","type":"Abstract"},{"text":"It also unveiled that NELF comprises three structured lobes and two flexible tentacles that approach DSIF and exiting RNA.","type":"Discussion"},{"text":"Residues 189-528 of NELF-A form a flexible tentacle that binds Pol II and DSIF.","type":"Figure"},{"text":"Crosslinking data indicate that the NELF-A flexible \"tentacle\" reach the DSIF DNA clamp, in particular SPT4 and the SPT5 NGN domain, and is involved in the binding of Pol II subunits RBP1, RBP2, RBP9 ","type":"Curator statement"},{"text":"Negative elongation factor (NELF), is composed of the four subunits NELF-A, -B, -C (or isoform NELF-D that lacks the first nine NELF-C residues), and -E. One of the two flexible \"tentacles\" is in NELF-A, the other flexible \"tentacle\" is in NELF-E. They contact DSIF, composed of SPT5 and SPT4","type":"Curator statement"}],"curator_id":"esalladini","released":"2022_03","ec_name":"cross-linking evidence used in manual assertion","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"30135580","version":4,"reference_html":"Structure of paused transcription complex Pol II-DSIF-NELF. <i> Vos SM, Farnung L, Urlaub H, Cramer P. </i> Nature, 2018","date":"2022-03-08T14:24:18.227Z","reference_source":"pmid","ec_id":"ECO:0001170","cross_refs":[{"db":"PDB","id":"6GML"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0002-5152-5953","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"I3LJR4","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"I3LGP4","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P60899","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"O00267","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63272","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T11:44:09.299Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":528,"region_id":"DP02712r005","start":189,"term_id":"GO:0060090","statement":[{"text":"Additionally, NELF possesses two flexible 'tentacles' that can contact DSIF and exiting RNA.","type":"Abstract"},{"text":"It also unveiled that NELF comprises three structured lobes and two flexible tentacles that approach DSIF and exiting RNA.","type":"Discussion"},{"text":"Residues 189-528 of NELF-A form a flexible tentacle that binds Pol II and DSIF.","type":"Figure"},{"text":"Crosslinking data indicate that the NELF-A flexible \"tentacle\" reach the DSIF DNA clamp, in particular SPT4 and the SPT5 NGN domain, and is involved in the binding of Pol II subunits RBP1, RBP2, RBP9 ","type":"Curator statement"},{"text":"Negative elongation factor (NELF), is composed of the four subunits NELF-A, -B, -C (or isoform NELF-D that lacks the first nine NELF-C residues), and -E. One of the two flexible \"tentacles\" is in NELF-A, the other flexible \"tentacle\" is in NELF-E. They contact DSIF, composed of SPT5 and SPT4","type":"Curator statement"}],"curator_id":"esalladini","released":"2022_03","ec_name":"cross-linking evidence used in manual assertion","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"30135580","version":4,"reference_html":"Structure of paused transcription complex Pol II-DSIF-NELF. <i> Vos SM, Farnung L, Urlaub H, Cramer P. </i> Nature, 2018","date":"2022-03-08T14:22:43.786Z","reference_source":"pmid","ec_id":"ECO:0001170","cross_refs":[{"db":"PDB","id":"6GML"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0002-5152-5953","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P63272","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"O00267","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P60899","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"I3LGP4","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"I3LJR4","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T11:44:11.471Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":528,"region_id":"DP02712r006","start":189,"term_id":"GO:0060090","statement":[{"text":"Additionally, NELF possesses two flexible 'tentacles' that can contact DSIF and exiting RNA.","type":"Abstract"},{"text":"It also unveiled that NELF comprises three structured lobes and two flexible tentacles that approach DSIF and exiting RNA.","type":"Discussion"},{"text":"Residues 189-528 of NELF-A form a flexible tentacle that binds Pol II and DSIF.","type":"Figure"},{"text":"Crosslinking data indicate that the NELF-A flexible \"tentacle\" reach the DSIF DNA clamp, in particular SPT4 and the SPT5 NGN domain, and is involved in the binding of Pol II subunits RBP1, RBP2, RBP9 ","type":"Curator statement"},{"text":"Negative elongation factor (NELF), is composed of the four subunits NELF-A, -B, -C (or isoform NELF-D that lacks the first nine NELF-C residues), and -E. One of the two flexible \"tentacles\" is in NELF-A, the other flexible \"tentacle\" is in NELF-E. They contact DSIF, composed of SPT5 and SPT4","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"30135580","version":3,"reference_html":"Structure of paused transcription complex Pol II-DSIF-NELF. <i> Vos SM, Farnung L, Urlaub H, Cramer P. </i> Nature, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","cross_refs":[{"db":"PDB","id":"6GML"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02712","date":"2020-03-25T13:50:33.018Z","organism":"Homo sapiens","regions_counter":7,"name":"Negative elongation factor A","dataset":["Condensates-related proteins"],"UniParc":"UPI000006DE29","uniref100":"UniRef100_Q9H3P2","uniref90":"UniRef90_Q9H3P2","uniref50":"UniRef50_Q9H3P2","genes":[{"name":{"value":"NELFA"},"synonyms":[{"value":"WHSC2"}],"orfNames":[{"value":"P/OKcl.15"}]}],"alphafold_very_low_content":0.42613636363636365,"disorder_content":0.6439393939393939,"disprot_consensus":{"full":[{"start":189,"end":528,"type":"D"}],"Structural state":[{"start":189,"end":528,"type":"D"}],"Molecular function":[{"start":189,"end":528,"type":"F"}]}},{"acc":"P18615","features":{"gene3D":[{"start":257,"end":343,"id":"G3DSA:3.30.70.330","name":"G3DSA:3.30.70.330"}],"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":269,"end":323}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MLVIPPGLSEEEEALQKKFNKLKKKKKALLALKKQSSSSTTSQGGVKRSLSEQPVMDTATATEQAKQLVKSGAISAIKAETKNSGFKRSRTLEGKLKDPEKGPVPTFQPFQRSISADDDLQESSRRPQRKSLYESFVSSSDRLRELGPDGEEAEGPGAGDGPPRSFDWGYEERSGAHSSASPPRSRSRDRSHERNRDRDRDRERDRDRDRDRDRERDRDRDRDRDRDRERDRDRERDRDRDREGPFRRSDSFPERRAPRKGNTLYVYGEDMTPTLLRGAFSPFGNIIDLSMDPPRNCAFVTYEKMESADQAVAELNGTQVESVQLKVNIARKQPMLDAATGKSVWGSLAVQNSPKGCHRDKRTQIVYSDDVYKENLVDGF","length":380,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":363,"region_id":"DP02713r001","start":139,"term_id":"IDPO:0000002","statement":[{"text":"Residues 139-363 of NELF-E form a flexible tentacle that extends over DSIF near exiting RNA.","type":"Figure"},{"text":"Density for NELF-E was largely lacking except for the N-terminal helix α1.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30135580","version":2,"reference_html":"Structure of paused transcription complex Pol II-DSIF-NELF. <i> Vos SM, Farnung L, Urlaub H, Cramer P. </i> Nature, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6GML"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-05T19:19:29.178Z"}}],"released":"2020_12","ncbi_taxon_id":9606,"disprot_id":"DP02713","date":"2020-03-25T15:42:42.186Z","organism":"Homo sapiens","regions_counter":3,"name":"Negative elongation factor E","dataset":["Condensates-related proteins","RNA-binding proteins"],"UniParc":"UPI000016AF7C","uniref100":"UniRef100_P18615","uniref90":"UniRef90_P18615","uniref50":"UniRef50_P18615","genes":[{"name":{"value":"NELFE"},"synonyms":[{"value":"RD","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"14701750","url":"http://www.ncbi.nlm.nih.gov/pubmed/14701750","alternativeUrl":"https://europepmc.org/abstract/MED/14701750"}}]},{"value":"RDBP"}]}],"alphafold_very_low_content":0.22631578947368422,"disorder_content":0.5921052631578947,"disprot_consensus":{"full":[{"start":139,"end":363,"type":"D"}],"Structural state":[{"start":139,"end":363,"type":"D"}]}},{"acc":"O60880","features":{"gene3D":[{"start":1,"end":104,"id":"G3DSA:3.30.505.10","name":"SH2 domain"}],"pfam":[{"id":"PF00017","name":"SH2 domain","start":7,"end":86}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MDAVAVYHGKISRETGEKLLLATGLDGSYLLRDSESVPGVYCLCVLYHGYIYTYRVSQTETGSWSAETAPGVHKRYFRKIKNLISAFQKPDQGIVIPLQYPVEKKSSARSTQGTTGIREDPDVCLKAP","length":128,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":128,"region_id":"DP02714r001","start":103,"term_id":"IDPO:0000002","statement":[{"text":"The C-terminal 25 residues of SAP/SH2D1A were unstructured in both complexes. The 1H–15N HSQC cross-peaks corresponding to this region of the protein were very narrow and intense, indicative of rapid and unhindered tumbling in solution (Li et al., 1999). Moreover, no intermediate- or long-range nuclear Overhauser effects (NOEs) could be observed beyond residue 105. Consequently, only residues 1–107, corresponding essentially to the SH2 domain region of the protein (residues 6–102)","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11823424","version":2,"reference_html":"A \"three-pronged\" binding mechanism for the SAP/SH2D1A SH2 domain: structural basis and relevance to the XLP syndrome. <i> Hwang PM, Li C, Morra M, Lillywhite J, Muhandiram DR, Gertler F, Terhorst C, Kay LE, Pawson T, Forman-Kay JD, Li SC. </i> EMBO J, 2002","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"1KA6"},{"db":"PDB","id":"1KA7"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02714","date":"2020-03-25T17:35:10.747Z","organism":"Homo sapiens","regions_counter":1,"name":"SH2 domain-containing protein 1A","dataset":[],"UniParc":"UPI0000000D0B","uniref100":"UniRef100_O60880","uniref90":"UniRef90_O60880","uniref50":"UniRef50_O60880","genes":[{"name":{"value":"SH2D1A"},"synonyms":[{"value":"DSHP"},{"value":"SAP"}]}],"alphafold_very_low_content":0.0859375,"disorder_content":0.203125,"disprot_consensus":{"full":[{"start":103,"end":128,"type":"D"}],"Structural state":[{"start":103,"end":128,"type":"D"}]}},{"acc":"P00452","features":{"gene3D":[],"pfam":[{"id":"PF00317","name":"Ribonucleotide reductase, all-alpha domain","start":142,"end":219},{"id":"PF02867","name":"Ribonucleotide reductase, barrel domain","start":223,"end":731},{"id":"PF03477","name":"ATP cone domain","start":6,"end":92}]},"creator":"fquaglia","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"sequence":"MNQNLLVTKRDGSTERINLDKIHRVLDWAAEGLHNVSISQVELRSHIQFYDGIKTSDIHETIIKAAADLISRDAPDYQYLAARLAIFHLRKKAYGQFEPPALYDHVVKMVEMGKYDNHLLEDYTEEEFKQMDTFIDHDRDMTFSYAAVKQLEGKYLVQNRVTGEIYESAQFLYILVAACLFSNYPRETRLQYVKRFYDAVSTFKISLPTPIMSGVRTPTRQFSSCVLIECGDSLDSINATSSAIVKYVSQRAGIGINAGRIRALGSPIRGGEAFHTGCIPFYKHFQTAVKSCSQGGVRGGAATLFYPMWHLEVESLLVLKNNRGVEGNRVRHMDYGVQINKLMYTRLLKGEDITLFSPSDVPGLYDAFFADQEEFERLYTKYEKDDSIRKQRVKAVELFSLMMQERASTGRIYIQNVDHCNTHSPFDPAIAPVRQSNLCLEIALPTKPLNDVNDENGEIALCTLSAFNLGAINNLDELEELAILAVRALDALLDYQDYPIPAAKRGAMGRRTLGIGVINFAYYLAKHGKRYSDGSANNLTHKTFEAIQYYLLKASNELAKEQGACPWFNETTYAKGILPIDTYKKDLDTIANEPLHYDWEALRESIKTHGLRNSTLSALMPSETSSQISNATNGIEPPRGYVSIKASKDGILRQVVPDYEHLHDAYELLWEMPGNDGYLQLVGIMQKFIDQSISANTNYDPSRFPSGKVPMQQLLKDLLTAYKFGVKTLYYQNTRDGAEDAQDDLVPSIQDDGCESGACKI","length":761,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":761,"region_id":"DP02715r001","start":737,"term_id":"IDPO:0000002","statement":[{"text":"The last 24 residues at the carboxyl end, which includes these two cysteines, are not visible in the electron density map.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"8052308","version":2,"reference_html":"Structure of ribonucleotide reductase protein R1. <i> Uhlin U, Eklund H. </i> Nature, 1994","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1RLR"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":761,"region_id":"DP02715r002","start":737,"term_id":"GO:0044183","statement":[{"text":"The last 24 residues at the carboxyl end, which includes these two cysteines, are not visible in the electron density map.","type":"Article"},{"text":"Ribonucleotide reductase is the only enzyme that catalyses de novo formation of deoxyribonucleotides and is thus a key enzyme in DNA synthesis. The radical-based reaction involves five cysteins. Two redox-active cysteines are located at adjacent antiparallel strands in a new type of ten-stranded alpha/beta-barrel, and two others at the carboxyl end in a flexible arm.","type":"Abstract"},{"text":"Together with the disordered carboxyl end of the peptide this provides strong support for the theory of a  flexible tail that transfers reducing equivalents from the surface to the active site by a thiol exchange reaction.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"8052308","version":3,"reference_html":"Structure of ribonucleotide reductase protein R1. <i> Uhlin U, Eklund H. </i> Nature, 1994","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1RLR"}],"term_name":"protein folding chaperone","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":83333,"disprot_id":"DP02715","date":"2020-03-25T20:11:58.107Z","organism":"Escherichia coli (strain K12)","regions_counter":2,"name":"Ribonucleoside-diphosphate reductase 1 subunit alpha","dataset":[],"UniParc":"UPI0000112BE0","uniref100":"UniRef100_P00452","uniref90":"UniRef90_P00452","uniref50":"UniRef50_P00452","genes":[{"name":{"value":"nrdA"},"synonyms":[{"value":"dnaF"}],"olnNames":[{"value":"b2234"},{"value":"JW2228"}]}],"alphafold_very_low_content":0.0328515111695138,"disorder_content":0.0328515111695138,"disprot_consensus":{"full":[{"start":737,"end":761,"type":"D"}],"Structural state":[{"start":737,"end":761,"type":"D"}],"Molecular function":[{"start":737,"end":761,"type":"F"}]}},{"acc":"P0A873","features":{"gene3D":[{"start":161,"end":255,"id":"G3DSA:1.10.1270.20","name":"tRNA(m1g37)methyltransferase, domain 2"},{"start":1,"end":160,"id":"G3DSA:3.40.1280.10","name":"G3DSA:3.40.1280.10"}],"pfam":[{"id":"PF01746","name":"tRNA (Guanine-1)-methyltransferase TrmD","start":1,"end":225}]},"creator":"fquaglia","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"sequence":"MWIGIISLFPEMFRAITDYGVTGRAVKNGLLSIQSWSPRDFTHDRHRTVDDRPYGGGPGMLMMVQPLRDAIHAAKAAAGEGAKVIYLSPQGRKLDQAGVSELATNQKLILVCGRYEGIDERVIQTEIDEEWSIGDYVLSGGELPAMTLIDSVSRFIPGVLGHEASATEDSFAEGLLDCPHYTRPEVLEGMEVPPVLLSGNHAEIRRWRLKQSLGRTWLRRPELLENLALTEEQARLLAEFKTEHAQQQHKHDGMA","length":255,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":172,"region_id":"DP02716r001","start":162,"term_id":"IDPO:0000002","statement":[{"text":"Each monomer consists of a C-terminal domain connected by a flexible linker to an N-terminal AdoMet-binding domain.","type":"Abstract"},{"text":"The monomer of TrmD consists of two discrete domains connected by an extended flexible linker region of 11 residues ","type":"Results"},{"text":"A disordered peptide linker spans the 23 Å distance between residues 161 and 173.","type":"Results"},{"text":"The disordered linker peptide that connects the two domains is expected to be in an extended conformation to span the available distance and must lie in and along one edge of the groove passing over the AdoHcy-binding site.","type":"Results"},{"text":"We have previously indicated that an unstructured peptide linker exists spanning residues 162 to 172 and running over the cofactor-binding site in the extended cleft formed by the monomer–monomer interface.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14583191","version":2,"reference_html":"Insights into catalysis by a knotted TrmD tRNA methyltransferase. <i> Elkins PA, Watts JM, Zalacain M, van Thiel A, Vitazka PR, Redlak M, Andraos-Selim C, Rastinejad F, Holmes WM. </i> J Mol Biol, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1P9P"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":172,"region_id":"DP02716r002","start":162,"term_id":"IDPO:0000033","statement":[{"text":"Each monomer consists of a C-terminal domain connected by a flexible linker to an N-terminal AdoMet-binding domain.","type":"Abstract"},{"text":"The monomer of TrmD consists of two discrete domains connected by an extended flexible linker region of 11 residues ","type":"Results"},{"text":"A disordered peptide linker spans the 23 Å distance between residues 161 and 173.","type":"Results"},{"text":"The disordered linker peptide that connects the two domains is expected to be in an extended conformation to span the available distance and must lie in and along one edge of the groove passing over the AdoHcy-binding site.","type":"Results"},{"text":"We have previously indicated that an unstructured peptide linker exists spanning residues 162 to 172 and running over the cofactor-binding site in the extended cleft formed by the monomer–monomer interface.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14583191","version":3,"reference_html":"Insights into catalysis by a knotted TrmD tRNA methyltransferase. <i> Elkins PA, Watts JM, Zalacain M, van Thiel A, Vitazka PR, Redlak M, Andraos-Selim C, Rastinejad F, Holmes WM. </i> J Mol Biol, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1P9P"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":83333,"disprot_id":"DP02716","date":"2020-03-26T09:40:36.716Z","organism":"Escherichia coli (strain K12)","regions_counter":2,"name":"tRNA (guanine-N(1)-)-methyltransferase","dataset":[],"UniParc":"UPI0000137412","uniref100":"UniRef100_A7ZQ47","uniref90":"UniRef90_A4WDH2","uniref50":"UniRef50_Q7MBD6","genes":[{"name":{"value":"trmD"},"olnNames":[{"value":"b2607"},{"value":"JW2588"}]}],"alphafold_very_low_content":0.00392156862745098,"disorder_content":0.043137254901960784,"disprot_consensus":{"full":[{"start":162,"end":172,"type":"D"}],"Structural state":[{"start":162,"end":172,"type":"D"}],"Disorder function":[{"start":162,"end":172,"type":"F"}]}},{"acc":"O95071","features":{"gene3D":[{"start":361,"end":496,"id":"G3DSA:2.130.10.30","name":"Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II"}],"pfam":[{"id":"PF00632","name":"HECT-domain (ubiquitin-transferase)","start":2501,"end":2798},{"id":"PF00658","name":"MLLE domain","start":2392,"end":2449},{"id":"PF11547","name":"E3 ubiquitin ligase EDD","start":179,"end":230},{"id":"PF30802","name":"UBR box","start":1175,"end":1241},{"id":"PF30806","name":"UBR5 first HEAT repeat domain","start":872,"end":1163},{"id":"PF30807","name":"UBR5 second HEAT repeat domain","start":1248,"end":2206}]},"creator":"xcastro","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MTSIHFVVHPLPGTEDQLNDRLREVSEKLNKYNLNSHPPLNVLEQATIKQCVVGPNHAAFLLEDGRVCRIGFSVQPDRLELGKPDNNDGSKLNSNSGAGRTSRPGRTSDSPWFLSGSETLGRLAGNTLGSRWSSGVGGSGGGSSGRSSAGARDSRRQTRVIRTGRDRGSGLLGSQPQPVIPASVIPEELISQAQVVLQGKSRSVIIRELQRTNLDVNLAVNNLLSRDDEDGDDGDDTASESYLPGEDLMSLLDADIHSAHPSVIIDADAMFSEDISYFGYPSFRRSSLSRLGSSRVLLLPLERDSELLRERESVLRLRERRWLDGASFDNERGSTSKEGEPNLDKKNTPVQSPVSLGEDLQWWPDKDGTKFICIGALYSELLAVSSKGELYQWKWSESEPYRNAQNPSLHHPRATFLGLTNEKIVLLSANSIRATVATENNKVATWVDETLSSVASKLEHTAQTYSELQGERIVSLHCCALYTCAQLENSLYWWGVVPFSQRKKMLEKARAKNKKPKSSAGISSMPNITVGTQVCLRNNPLYHAGAVAFSISAGIPKVGVLMESVWNMNDSCRFQLRSPESLKNMEKASKTTEAKPESKQEPVKTEMGPPPSPASTCSDASSIASSASMPYKRRRSTPAPKEEEKVNEEQWSLREVVFVEDVKNVPVGKVLKVDGAYVAVKFPGTSSNTNCQNSSGPDADPSSLLQDCRLLRIDELQVVKTGGTPKVPDCFQRTPKKLCIPEKTEILAVNVDSKGVHAVLKTGNWVRYCIFDLATGKAEQENNFPTSSIAFLGQNERNVAIFTAGQESPIILRDGNGTIYPMAKDCMGGIRDPDWLDLPPISSLGMGVHSLINLPANSTIKKKAAVIIMAVEKQTLMQHILRCDYEACRQYLMNLEQAVVLEQNLQMLQTFISHRCDGNRNILHACVSVCFPTSNKETKEEEEAERSERNTFAERLSAVEAIANAISVVSSNGPGNRAGSSSSRSLRLREMMRRSLRAAGLGRHEAGASSSDHQDPVSPPIAPPSWVPDPPAMDPDGDIDFILAPAVGSLTTAATGTGQGPSTSTIPGPSTEPSVVESKDRKANAHFILKLLCDSVVLQPYLRELLSAKDARGMTPFMSAVSGRAYPAAITILETAQKIAKAEISSSEKEEDVFMGMVCPSGTNPDDSPLYVLCCNDTCSFTWTGAEHINQDIFECRTCGLLESLCCCTECARVCHKGHDCKLKRTSPTAYCDCWEKCKCKTLIAGQKSARLDLLYRLLTATNLVTLPNSRGEHLLLFLVQTVARQTVEHCQYRPPRIREDRNRKTASPEDSDMPDHDLEPPRFAQLALERVLQDWNALKSMIMFGSQENKDPLSASSRIGHLLPEEQVYLNQQSGTIRLDCFTHCLIVKCTADILLLDTLLGTLVKELQNKYTPGRREEAIAVTMRFLRSVARVFVILSVEMASSKKKNNFIPQPIGKCKRVFQALLPYAVEELCNVAESLIVPVRMGIARPTAPFTLASTSIDAMQGSEELFSVEPLPPRPSSDQSSSSSQSQSSYIIRNPQQRRISQSQPVRGRDEEQDDIVSADVEEVEVVEGVAGEEDHHDEQEEHGEENAEAEGQHDEHDEDGSDMELDLLAAAETESDSESNHSNQDNASGRRSVVTAATAGSEAGASSVPAFFSEDDSQSNDSSDSDSSSSQSDDIEQETFMLDEPLERTTNSSHANGAAQAPRSMQWAVRNTQHQRAASTAPSSTSTPAASSAGLIYIDPSNLRRSGTISTSAAAAAAALEASNASSYLTSASSLARAYSIVIRQISDLMGLIPKYNHLVYSQIPAAVKLTYQDAVNLQNYVEEKLIPTWNWMVSIMDSTEAQLRYGSALASAGDPGHPNHPLHASQNSARRERMTAREEASLRTLEGRRRATLLSARQGMMSARGDFLNYALSLMRSHNDEHSDVLPVLDVCSLKHVAYVFQALIYWIKAMNQQTTLDTPQLERKRTRELLELGIDNEDSEHENDDDTNQSATLNDKDDDSLPAETGQNHPFFRRSDSMTFLGCIPPNPFEVPLAEAIPLADQPHLLQPNARKEDLFGRPSQGLYSSSASSGKCLMEVTVDRNCLEVLPTKMSYAANLKNVMNMQNRQKKEGEEQPVLPEETESSKPGPSAHDLAAQLKSSLLAEIGLTESEGPPLTSFRPQCSFMGMVISHDMLLGRWRLSLELFGRVFMEDVGAEPGSILTELGGFEVKESKFRREMEKLRNQQSRDLSLEVDRDRDLLIQQTMRQLNNHFGRRCATTPMAVHRVKVTFKDEPGEGSGVARSFYTAIAQAFLSNEKLPNLECIQNANKGTHTSLMQRLRNRGERDREREREREMRRSSGLRAGSRRDRDRDFRRQLSIDTRPFRPASEGNPSDDPEPLPAHRQALGERLYPRVQAMQPAFASKITGMLLELSPAQLLLLLASEDSLRARVDEAMELIIAHGRENGADSILDLGLVDSSEKVQQENRKRHGSSRSVVDMDLDDTDDGDDNAPLFYQPGKRGFYTPRPGKNTEARLNCFRNIGRILGLCLLQNELCPITLNRHVIKVLLGRKVNWHDFAFFDPVMYESLRQLILASQSSDADAVFSAMDLAFAIDLCKEEGGGQVELIPNGVNIPVTPQNVYEYVRKYAEHRMLVVAEQPLHAMRKGLLDVLPKNSLEDLTAEDFRLLVNGCGEVNVQMLISFTSFNDESGENAEKLLQFKRWFWSIVEKMSMTERQDLVYFWTSSPSLPASEEGFQPMPSITIRPPDDQHLPTANTCISRLYVPLYSSKQILKQKLLLAIKTKNFGFV","length":2799,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":2747,"region_id":"DP02717r001","start":2738,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The structure also features three loops, L1 (seven residues), L2 (17 residues) and L3 (seven residues); the longest loop L2 is disordered and is absent from the density map","type":"Results"},{"text":"The final structure does not include 19 of the 113 residues, including the seven last C-­terminal residues, as these regions were disordered in the crystal.","type":"Results"},{"text":"This disordered region correspond to 12 aa of the L2 loop","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23027739","version":2,"reference_html":"Structure of the HECT C-lobe of the UBR5 E3 ubiquitin ligase. <i> Matta-Camacho E, Kozlov G, Menade M, Gehring K. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012","date":"2022-06-28T07:49:41.491Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3PT3"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-28T12:15:15.144Z"}}],"released":"2022_06","ncbi_taxon_id":9606,"disprot_id":"DP02717","date":"2020-03-26T10:01:16.045Z","organism":"Homo sapiens","regions_counter":17,"name":"E3 ubiquitin-protein ligase UBR5","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI0000129BCB","uniref100":"UniRef100_O95071","uniref90":"UniRef90_O95071","uniref50":"UniRef50_O95071","genes":[{"name":{"value":"UBR5"},"synonyms":[{"value":"EDD"},{"value":"EDD1"},{"value":"HYD"},{"value":"KIAA0896"}]}],"disorder_content":0.0035727045373347625,"disprot_consensus":{"full":[{"start":2738,"end":2747,"type":"D"}],"Structural state":[{"start":2738,"end":2747,"type":"D"}]}},{"acc":"Q8ST83","features":{"gene3D":[],"pfam":[{"id":"PF00096","name":"Zinc finger, C2H2 type","start":386,"end":408},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":414,"end":438},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":444,"end":468}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"sequence":"MAYERFGIILQSEQYDEDIGNTKVNQKMNEGNHYDLHRKNAFDRIIHSESKKGDNVINYNIHENDKIKAADNIFSSKLKMNPNMSYEMNINCFKNIGYGENQETSKVLTNSLSNNDINTEESGVVDKNSPFLTLGTTILNSNGKSRRWEQKLVHIKTMEGEFSVTMWASGISDDEYSGSDQIVGASDLLKGKEEFGIDGFTSQQNKEYQKMESKFTNAQTLEMPHPISSVQIMDHLIKERGNLSQENNISERILSKTTLSFEEPILLPDSSSIELVNETAAMTINNHRTLSNHTGNTGDLHALPSSVPFRIGLHEGQVNDCLSTISQSTHQDNTDSTGCGEMNLSEVTVSYTNDKKIACPHKGCNKHFRDSSAMRKHLHTHGPRVHVCAECGKAFVESSKLKRHQLVHTGEKPFQCTFEGCGKRFSLDFNLRTHVRIHTGDRPFVCPFDACNKKFAQSTNLKSHILTHAKAKRNTSISGKSGCSNAESNSQSEDTSANYVKVELQDSVTENHVPFVVYAD","length":520,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":144,"region_id":"DP02718r001","start":116,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Pho regions flanking the spacer and connecting it to the DNA-binding domain are predicted to be disordered","type":"Figure"},{"text":"In crystal form P3121, a longer Pho construct comprising 131 amino acid residues was used for cocrystallization (Supplemental Table 1), but only electron density corresponding to the Pho spacer peptide was visible.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24186981","version":2,"reference_html":"Structural basis for targeting the chromatin repressor Sfmbt to Polycomb response elements. <i> Alfieri C, Gambetta MC, Matos R, Glatt S, Sehr P, Fraterman S, Wilm M, Müller J, Müller CW. </i> Genes Dev, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4C5G"},{"db":"PDB","id":"4C5H"},{"db":"PDB","id":"4C5E"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":246,"region_id":"DP02718r002","start":171,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Pho regions flanking the spacer and connecting it to the DNA-binding domain are predicted to be disordered","type":"Figure"},{"text":"In crystal form P3121, a longer Pho construct comprising 131 amino acid residues was used for cocrystallization (Supplemental Table 1), but only electron density corresponding to the Pho spacer peptide was visible.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24186981","version":2,"reference_html":"Structural basis for targeting the chromatin repressor Sfmbt to Polycomb response elements. <i> Alfieri C, Gambetta MC, Matos R, Glatt S, Sehr P, Fraterman S, Wilm M, Müller J, Müller CW. </i> Genes Dev, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4C5G"},{"db":"PDB","id":"4C5H"},{"db":"PDB","id":"4C5E"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":246,"region_id":"DP02718r003","start":171,"term_id":"IDPO:0000033","unpublished":true,"statement":[{"text":"Pho regions flanking the spacer and connecting it to the DNA-binding domain are predicted to be disordered","type":"Figure"},{"text":"The spacer region of Pho, separated from the DNA-binding domain by a long flexible linker, forms a tight complex with the four malignant brain tumor (4MBT) domain of Sfmbt.","type":"Abstract"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24186981","version":3,"reference_html":"Structural basis for targeting the chromatin repressor Sfmbt to Polycomb response elements. <i> Alfieri C, Gambetta MC, Matos R, Glatt S, Sehr P, Fraterman S, Wilm M, Müller J, Müller CW. </i> Genes Dev, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4C5G"},{"db":"PDB","id":"4C5H"},{"db":"PDB","id":"4C5E"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2023_12","ncbi_taxon_id":7227,"disprot_id":"DP02718","date":"2020-03-26T10:22:18.657Z","organism":"Drosophila melanogaster","regions_counter":3,"name":"Polycomb protein PHO","dataset":[],"UniParc":"UPI000008014A","uniref100":"UniRef100_Q8ST83","uniref90":"UniRef90_Q8ST83","uniref50":"UniRef50_Q8ST83","genes":[{"name":{"value":"pho"},"orfNames":[{"value":"CG17743"}]}],"alphafold_very_low_content":0.7423076923076923,"disorder_content":0.20192307692307693,"disprot_consensus":{"full":[{"start":116,"end":144,"type":"D"},{"start":171,"end":246,"type":"D"}],"Structural state":[{"start":116,"end":144,"type":"D"},{"start":171,"end":246,"type":"D"}],"Disorder function":[{"start":171,"end":246,"type":"F"}]}},{"acc":"Q53FT3","features":{"gene3D":[],"pfam":[{"id":"PF05603","name":"Hikeshi-like, N-terminal domain","start":6,"end":128},{"id":"PF21057","name":"Hikeshi-like, C-terminal domain","start":136,"end":196}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MFGCLVAGRLVQTAAQQVAEDKFVFDLPDYESINHVVVFMLGTIPFPEGMGGSVYFSYPDSNGMPVWQLLGFVTNGKPSAIFKISGLKSGEGSQHPFGAMNIVRTPSVAQIGISVELLDSMAQQTPVGNAAVSSVDSFTQFTQKMLDNFYNFASSFAVSQAQMTPSPSEMFIPANVVLKWYENFQRRLAQNPLFWKT","length":197,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":106,"region_id":"DP02719r001","start":88,"term_id":"IDPO:0000002","statement":[{"text":"The E-loop of Phe97Ala mutant was largely disordered","type":"Figure"},{"text":"The E-loop containing the Phe97Ala mutation was largely disordered in both monomers, in contrast to the same loop of the wt (Fig. 4c), indicating that Phe97 was responsible for the decreased flexibility of the E-loop as an anchor point (see §4).","type":"Results"}],"curator_id":"vnugnes","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"25760597","version":3,"reference_html":"Structural and functional analysis of Hikeshi, a new nuclear transport receptor of Hsp70s. <i> Song J, Kose S, Watanabe A, Son SY, Choi S, Hong H, Yamashita E, Park IY, Imamoto N, Lee SJ. </i> Acta Crystallogr D Biol Crystallogr, 2015","date":"2023-06-14T09:20:13.317Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3WW0"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe97Ala","start":null,"end":null,"position":null}]}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02719","date":"2020-03-26T11:40:46.719Z","organism":"Homo sapiens","regions_counter":4,"name":"Protein Hikeshi","dataset":["NDDs-related proteins"],"UniParc":"UPI000050A8EF","uniref100":"UniRef100_Q53FT3","uniref90":"UniRef90_Q53FT3","uniref50":"UniRef50_Q53FT3","genes":[{"name":{"value":"HIKESHI","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:26938","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:26938"}}]},"synonyms":[{"value":"C11orf73"}],"orfNames":[{"value":"HSPC138"},{"value":"HSPC179"},{"value":"HSPC248"}]}],"alphafold_very_low_content":0.01015228426395939,"disorder_content":0.09644670050761421,"disprot_consensus":{"full":[{"start":88,"end":106,"type":"D"}],"Structural state":[{"start":88,"end":106,"type":"D"}]}},{"acc":"P32357","features":{"gene3D":[{"start":144,"end":355,"id":"G3DSA:1.25.40.550","name":"G3DSA:1.25.40.550"},{"start":1,"end":143,"id":"G3DSA:2.60.34.20","name":"G3DSA:2.60.34.20"}],"pfam":[{"id":"PF05282","name":"AAR2 C-terminal repeat region","start":179,"end":303},{"id":"PF20981","name":"AAR2 N-terminal domain","start":6,"end":129}]},"creator":"fquaglia","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"sequence":"MNTVPFTSAPIEVTIGIDQYSFNVKENQPFHGIKDIPIGHVHVIHFQHADNSSMRYGYWFDCRMGNFYIQYDPKDGLYKMMEERDGAKFENIVHNFKERQMMVSYPKIDEDDTWYNLTEFVQMDKIRKIVRKDENQFSYVDSSMTTVQENELLKSSLQKAGSKMEAKNEDDPAHSLNYTVINFKSREAIRPGHEMEDFLDKSYYLNTVMLQGIFKNSSNYFGELQFAFLNAMFFGNYGSSLQWHAMIELICSSATVPKHMLDKLDEILYYQIKTLPEQYSDILLNERVWNICLYSSFQKNSLHNTEKIMENKYPELLGKDNEDDALIYGISDEERDDEDDEHNPTIVGGLYYQRP","length":355,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":171,"region_id":"DP02721r001","start":153,"term_id":"IDPO:0000002","statement":[{"text":"Aar2pSub is organized in two globular domains, connected via a flexible loop between residues 153 and 171, part of which was cleaved during subtilisin treatment","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21764848","version":2,"reference_html":"Mechanism for Aar2p function as a U5 snRNP assembly factor. <i> Weber G, Cristão VF, de L Alves F, Santos KF, Holton N, Rappsilber J, Beggs JD, Wahl MC. </i> Genes Dev, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3SBT"},{"db":"PDB","id":"3SBS"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":171,"region_id":"DP02721r002","start":153,"term_id":"IDPO:0000033","statement":[{"text":"Aar2pSub is organized in two globular domains, connected via a flexible loop between residues 153 and 171, part of which was cleaved during subtilisin treatment","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21764848","version":3,"reference_html":"Mechanism for Aar2p function as a U5 snRNP assembly factor. <i> Weber G, Cristão VF, de L Alves F, Santos KF, Holton N, Rappsilber J, Beggs JD, Wahl MC. </i> Genes Dev, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3SBT"},{"db":"PDB","id":"3SBS"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":559292,"disprot_id":"DP02721","date":"2020-03-26T12:11:48.224Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":2,"name":"A1 cistron-splicing factor AAR2","dataset":[],"UniParc":"UPI0000053112","uniref100":"UniRef100_P32357","uniref90":"UniRef90_P32357","uniref50":"UniRef50_P32357","genes":[{"name":{"value":"AAR2"},"orfNames":[{"value":"YBL06.06"},{"value":"YBL0611"}],"olnNames":[{"value":"YBL074C"}]}],"alphafold_very_low_content":0.08450704225352113,"disorder_content":0.05352112676056338,"disprot_consensus":{"full":[{"start":153,"end":171,"type":"D"}],"Structural state":[{"start":153,"end":171,"type":"D"}],"Disorder function":[{"start":153,"end":171,"type":"F"}]}},{"acc":"P33334","features":{"gene3D":[{"start":1257,"end":1375,"id":"G3DSA:1.20.58.1750","name":"G3DSA:1.20.58.1750"},{"start":1833,"end":1993,"id":"G3DSA:3.30.420.230","name":"G3DSA:3.30.420.230"},{"start":1994,"end":2092,"id":"G3DSA:1.20.80.40","name":"G3DSA:1.20.80.40"}],"pfam":[{"id":"PF08082","name":"PRO8NT (NUC069), PrP8 N-terminal domain","start":131,"end":282},{"id":"PF08083","name":"PROCN (NUC071) domain","start":472,"end":874},{"id":"PF08084","name":"PROCT (NUC072) domain","start":2289,"end":2410},{"id":"PF10596","name":"U6-snRNA interacting domain of PrP8","start":1514,"end":1671},{"id":"PF10597","name":"U5-snRNA binding site 2 of PrP8","start":1308,"end":1444},{"id":"PF10598","name":"RNA recognition motif of the spliceosomal PrP8","start":1059,"end":1149},{"id":"PF12134","name":"PRP8 domain IV core","start":1832,"end":2060}]},"creator":"bjuhasz","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"sequence":"MSGLPPPPPGFEEDSDLALPPPPPPPPGYEIEELDNPMVPSSVNEDTFLPPPPPPPSNFEINAEEIVDFTLPPPPPPPGLDELETKAEKKVELHGKRKLDIGKDTFVTRKSRKRAKKMTKKAKRSNLYTPKAEMPPEHLRKIINTHSDMASKMYNTDKKAFLGALKYLPHAILKLLENMPHPWEQAKEVKVLYHTSGAITFVNETPRVIEPVYTAQWSATWIAMRREKRDRTHFKRMRFPPFDDDEPPLSYEQHIENIEPLDPINLPLDSQDDEYVKDWLYDSRPLEEDSKKVNGTSYKKWSFDLPEMSNLYRLSTPLRDEVTDKNYYYLFDKKSFFNGKALNNAIPGGPKFEPLYPREEEEDYNEFNSIDRVIFRVPIRSEYKVAFPHLYNSRPRSVRIPWYNNPVSCIIQNDEEYDTPALFFDPSLNPIPHFIDNNSSLNVSNTKENGDFTLPEDFAPLLAEEEELILPNTKDAMSLYHSPFPFNRTKGKMVRAQDVALAKKWFLQHPDEEYPVKVKVSYQKLLKNYVLNELHPTLPTNHNKTKLLKSLKNTKYFQQTTIDWVEAGLQLCRQGHNMLNLLIHRKGLTYLHLDYNFNLKPTKTLTTKERKKSRLGNSFHLMRELLKMMKLIVDTHVQFRLGNVDAFQLADGIHYILNHIGQLTGIYRYKYKVMHQIRACKDLKHIIYYKFNKNLGKGPGCGFWQPAWRVWLNFLRGTIPLLERYIGNLITRQFEGRSNEIVKTTTKQRLDAYYDLELRNSVMDDILEMMPESIRQKKARTILQHLSEAWRCWKANIPWDVPGMPAPIKKIIERYIKSKADAWVSAAHYNRERIKRGAHVEKTMVKKNLGRLTRLWIKNEQERQRQIQKNGPEITPEEATTIFSVMVEWLESRSFSPIPFPPLTYKNDTKILVLALEDLKDVYASKVRLNASEREELALIEEAYDNPHDTLNRIKKYLLTQRVFKPVDITMMENYQNISPVYSVDPLEKITDAYLDQYLWYEADQRKLFPNWIKPSDSEIPPLLVYKWTQGINNLSEIWDVSRGQSAVLLETTLGEMAEKIDFTLLNRLLRLIVDPNIADYITAKNNVVINFKDMSHVNKYGLIRGLKFASFIFQYYGLVIDLLLLGQERATDLAGPANNPNEFMQFKSKEVEKAHPIRLYTRYLDRIYMLFHFEEDEGEELTDEYLAENPDPNFENSIGYNNRKCWPKDSRMRLIRQDVNLGRAVFWEIQSRVPTSLTSIKWENAFVSVYSKNNPNLLFSMCGFEVRILPRQRMEEVVSNDEGVWDLVDERTKQRTAKAYLKVSEEEIKKFDSRIRGILMASGSTTFTKVAAKWNTSLISLFTYFREAIVATEPLLDILVKGETRIQNRVKLGLNSKMPTRFPPAVFYTPKELGGLGMISASHILIPASDLSWSKQTDTGITHFRAGMTHEDEKLIPTIFRYITTWENEFLDSQRVWAEYATKRQEAIQQNRRLAFEELEGSWDRGIPRISTLFQRDRHTLAYDRGHRIRREFKQYSLERNSPFWWTNSHHDGKLWNLNAYRTDVIQALGGIETILEHTLFKGTGFNSWEGLFWEKASGFEDSMQFKKLTHAQRTGLSQIPNRRFTLWWSPTINRANVYVGFLVQLDLTGIFLHGKIPTLKISLIQIFRAHLWQKIHESIVFDICQILDGELDVLQIESVTKETVHPRKSYKMNSSAADITMESVHEWEVSKPSLLHETNDSFKGLITNKMWFDVQLRYGDYDSHDISRYVRAKFLDYTTDNVSMYPSPTGVMIGIDLAYNMYDAYGNWFNGLKPLIQNSMRTIMKANPALYVLRERIRKGLQIYQSSVQEPFLNSSNYAELFNNDIKLFVDDTNVYRVTVHKTFEGNVATKAINGCIFTLNPKTGHLFLKIIHTSVWAGQKRLSQLAKWKTAEEVSALVRSLPKEEQPKQIIVTRKAMLDPLEVHMLDFPNIAIRPTELRLPFSAAMSIDKLSDVVMKATEPQMVLFNIYDDWLDRISSYTAFSRLTLLLRALKTNEESAKMILLSDPTITIKSYHLWPSFTDEQWITIESQMRDLILTEYGRKYNVNISALTQTEIKDIILGQNIKAPSVKRQKMAELEAARSEKQNDEEAAGASTVMKTKTINAQGEEIVVVASADYESQTFSSKNEWRKSAIANTLLYLRLKNIYVSADDFVEEQNVYVLPKNLLKKFIEISDVKIQVAAFIYGMSAKDHPKVKEIKTVVLVPQLGHVGSVQISNIPDIGDLPDTEGLELLGWIHTQTEELKFMAASEVATHSKLFADKKRDCIDISIFSTPGSVSLSAYNLTDEGYQWGEENKDIMNVLSEGFEPTFSTHAQLLLSDRITGNFIIPSGNVWNYTFMGTAFNQEGDYNFKYGIPLEFYNEMHRPVHFLQFSELAGDEELEAEQIDVFS","length":2413,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":2147,"region_id":"DP02722r001","start":2087,"term_id":"IDPO:0000002","statement":[{"text":"Prp8pCTF* lacked 16 amino acids at the C terminus compared with Prp8pCTF. In that structure, a 60-residue linker between the domains lacked electron density, demonstrating its intrinsic flexibility","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21764848","version":2,"reference_html":"Mechanism for Aar2p function as a U5 snRNP assembly factor. <i> Weber G, Cristão VF, de L Alves F, Santos KF, Holton N, Rappsilber J, Beggs JD, Wahl MC. </i> Genes Dev, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3SBG"},{"db":"PDB","id":"3SBT"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":2147,"region_id":"DP02722r002","start":2087,"term_id":"IDPO:0000033","statement":[{"text":"Prp8pCTF* lacked 16 amino acids at the C terminus compared with Prp8pCTF. In that structure, a 60-residue linker between the domains lacked electron density, demonstrating its intrinsic flexibility","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21764848","version":3,"reference_html":"Mechanism for Aar2p function as a U5 snRNP assembly factor. <i> Weber G, Cristão VF, de L Alves F, Santos KF, Holton N, Rappsilber J, Beggs JD, Wahl MC. </i> Genes Dev, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3SBG"},{"db":"PDB","id":"3SBT"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":559292,"disprot_id":"DP02722","date":"2020-03-26T12:17:14.893Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":2,"name":"Pre-mRNA-splicing factor 8","dataset":["RNA-binding proteins"],"UniParc":"UPI000013213D","uniref100":"UniRef100_P33334","uniref90":"UniRef90_P33334","uniref50":"UniRef50_P33334","genes":[{"name":{"value":"PRP8"},"synonyms":[{"value":"DBF3"},{"value":"DNA39"},{"value":"RNA8"},{"value":"SLT21"},{"value":"USA2"}],"olnNames":[{"value":"YHR165C"}]}],"alphafold_very_low_content":0.0820555325321177,"disorder_content":0.025279734769995857,"disprot_consensus":{"full":[{"start":2087,"end":2147,"type":"D"}],"Structural state":[{"start":2087,"end":2147,"type":"D"}],"Disorder function":[{"start":2087,"end":2147,"type":"F"}]}},{"acc":"Q8VDP3","features":{"gene3D":[{"start":85,"end":466,"id":"G3DSA:3.50.50.60","name":"FAD/NAD(P)-binding domain"},{"start":388,"end":615,"id":"G3DSA:1.10.418.10","name":"Calponin-like domain"}],"pfam":[{"id":"PF00307","name":"Calponin homology (CH) domain","start":511,"end":611},{"id":"PF01494","name":"FAD binding domain","start":85,"end":122},{"id":"PF12130","name":"Bivalent Mical/EHBP Rab binding domain","start":918,"end":1046},{"id":"PF25413","name":"Mical, Rossman domain","start":236,"end":365}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MASPASTNPAHDHFETFVQAQLCQDVLSSFQGLCRALGVESGGGLSQYHKIKAQLNYWSAKSLWAKLDKRASQPVYQQGQACTNTKCLVVGAGPCGLRAAVELALLGARVVLVEKRIKFSRHNVLHLWPFTIHDLRALGAKKFYGRFCTGTLDHISIRQLQLLLLKVALLLGVEIHWGVKFTGLQPPPRKGSGWRAQLQPNPPAQLASYEFDVLISAAGGKFVPEGFTIREMRGKLAIGITANFVNGRTVEETQVPEISGVARIYNQKFFQSLLKATGIDLENIVYYKDETHYFVMTAKKQCLLRLGVLRQDLSETDQLLGKANVVPEALQRFARAAADFATHGKLGKLEFAQDARGRPDVAAFDFTSMMRAESSARVQEKHGARLLLGLVGDCLVEPFWPLGTGVARGFLAAFDAAWMVKRWAEGAGPLEVLAERESLYQLLSQTSPENMHRNVAQYGLDPATRYPNLNLRAVTPNQVQDLYDMMDKEHAQRKSDEPDSRKTTTGSAGTEELLHWCQEQTAGFPGVHVTDFSSSWADGLALCALVHHLQPGLLEPSELQGMGALEATTWALRVAEHELGITPVLSAQAVMAGSDPLGLIAYLSHFHSAFKNTSHSSGLVSQPSGTPSAILFLGKLQRSLQRTRAKVDEETPSTEEPPVSEPSMSPNTPELSEHQEAGAEELCELCGKHLYILERFCVDGHFFHRSCFCCHTCEATLWPGGYGQHPGDGHFYCLQHLPQEDQKEADNNGSLESQELPTPGDSNMQPDPSSPPVTRVSPVPSPSQPARRLIRLSSLERLRLSSLNIIPDSGAEPPPKPPRSCSDLARESLKSSFVGWGVPVQAPQVPEAIEKGDDEEEEEEEEEEEEEPLPPLEPELEQTLLTLAKNPGAMTKYPTWRRTLMRRAKEEEMKRFCKAQAIQRRLNEIEATMRELEAEGTKLELALRKESSSPEQQKKLWLDQLLRLIQKKNSLVTEEAELMITVQELDLEEKQRQLDHELRGYMNREETMKTEADLQSENQVLRKLLEVVNQRDALIQFQEERRLREMPA","length":1048,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":505,"region_id":"DP02723r001","start":487,"term_id":"IDPO:0000002","statement":[{"text":"Our results suggest that the CH domain, which is loosely connected to the MO domain by a flexible linker and is far away from the catalytic site, couples F-actin to the enhancement of redox activity of MICALMO-CH by a cooperative mechanism involving a trans interaction between adjacently bound molecules.","type":"Abstract"},{"text":"The structures of two crystal forms, native 1 and 2 (Table 1), show electron density for residues 8–486 of the MO domain and residues 506–554 and 562–614 of the CH domain (Fig. 1).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26935886","version":2,"reference_html":"Modulation of MICAL Monooxygenase Activity by its Calponin Homology Domain: Structural and Mechanistic Insights. <i> Alqassim SS, Urquiza M, Borgnia E, Nagib M, Amzel LM, Bianchet MA. </i> Sci Rep, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4TXI"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":505,"region_id":"DP02723r002","start":487,"term_id":"IDPO:0000033","statement":[{"text":"Our results suggest that the CH domain, which is loosely connected to the MO domain by a flexible linker and is far away from the catalytic site, couples F-actin to the enhancement of redox activity of MICALMO-CH by a cooperative mechanism involving a trans interaction between adjacently bound molecules.","type":"Abstract"},{"text":"The structures of two crystal forms, native 1 and 2 (Table 1), show electron density for residues 8–486 of the MO domain and residues 506–554 and 562–614 of the CH domain (Fig. 1).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26935886","version":3,"reference_html":"Modulation of MICAL Monooxygenase Activity by its Calponin Homology Domain: Structural and Mechanistic Insights. <i> Alqassim SS, Urquiza M, Borgnia E, Nagib M, Amzel LM, Bianchet MA. </i> Sci Rep, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4TXI"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":10090,"disprot_id":"DP02723","date":"2020-03-26T12:42:40.873Z","organism":"Mus musculus","regions_counter":2,"name":"[F-actin]-monooxygenase MICAL1","dataset":[],"UniParc":"UPI00000E6848","uniref100":"UniRef100_Q8VDP3","uniref90":"UniRef90_Q8VDP3","uniref50":"UniRef50_Q8TDZ2-2","genes":[{"name":{"value":"Mical1"},"synonyms":[{"value":"Mical"},{"value":"Nical"}]}],"alphafold_very_low_content":0.21660305343511452,"disorder_content":0.01812977099236641,"disprot_consensus":{"full":[{"start":487,"end":505,"type":"D"}],"Structural state":[{"start":487,"end":505,"type":"D"}],"Disorder function":[{"start":487,"end":505,"type":"F"}]}},{"acc":"Q13838","features":{"gene3D":[],"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":70,"end":235},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":274,"end":382}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MAENDVDNELLDYEDDEVETAAGGDGAEAPAKKDVKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQLEPVTGQVSVLVMCHTRELAFQISKEYERFSKYMPNVKVAVFFGGLSIKKDEEVLKKNCPHIVVGTPGRILALARNKSLNLKHIKHFILDECDKMLEQLDMRRDVQEIFRMTPHEKQVMMFSATLSKEIRPVCRKFMQDPMEIFVDDETKLTLHGLQQYYVKLKDNEKNRKLFDLLDVLEFNQVVIFVKSVQRCIALAQLLVEQNFPAIAIHRGMPQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIAFNYDMPEDSDTYLHRVARAGRFGTKGLAITFVSDENDAKILNDVQDRFEVNISELPDEIDISSYIEQTR","length":428,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":44,"region_id":"DP02724r001","start":34,"term_id":"IDPO:0000002","statement":[{"text":"The corresponding residues in the N terminus of UAP56 (residues 34–44) are disordered, consistent with the limited proteolysis result.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15296731","version":2,"reference_html":"Crystal structure of UAP56, a DExD/H-box protein involved in pre-mRNA splicing and mRNA export. <i> Zhao R, Shen J, Green MR, MacMorris M, Blumenthal T. </i> Structure, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1T6N"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":44,"region_id":"DP02724r002","start":34,"term_id":"IDPO:0000002","statement":[{"text":"The corresponding residues in the N terminus of UAP56 (residues 34–44) are disordered, consistent with the limited proteolysis result.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15296731","version":2,"reference_html":"Crystal structure of UAP56, a DExD/H-box protein involved in pre-mRNA splicing and mRNA export. <i> Zhao R, Shen J, Green MR, MacMorris M, Blumenthal T. </i> Structure, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","cross_refs":[{"db":"PDB","id":"1T6N"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02724","date":"2020-03-27T09:41:23.972Z","organism":"Homo sapiens","regions_counter":2,"name":"Spliceosome RNA helicase DDX39B","dataset":[],"UniParc":"UPI0000001D0B","uniref100":"UniRef100_Q13838","uniref90":"UniRef90_Q13838","uniref50":"UniRef50_Q13838","genes":[{"name":{"value":"DDX39B","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:13917","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:13917"}}]},"synonyms":[{"value":"BAT1"},{"value":"UAP56"}]}],"alphafold_very_low_content":0.102803738317757,"disorder_content":0.02570093457943925,"disprot_consensus":{"full":[{"start":34,"end":44,"type":"D"}],"Structural state":[{"start":34,"end":44,"type":"D"}]}},{"acc":"Q42521","features":{"gene3D":[{"start":66,"end":360,"id":"G3DSA:3.40.640.10","name":"Type I PLP-dependent aspartate aminotransferase-like (Major domain)"}],"pfam":[{"id":"PF00282","name":"Pyridoxal-dependent decarboxylase conserved domain","start":33,"end":381}]},"creator":"fquaglia","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"sequence":"MVLSHAVSESDVSVHSTFASRYVRTSLPRFKMPENSIPKEAAYQIINDELMLDGNPRLNLASFVTTWMEPECDKLIMSSINKNYVDMDEYPVTTELQNRCVNMIAHLFNAPLEEAETAVGVGTVGSSEAIMLAGLAFKRKWQNKRKAEGKPVDKPNIVTGANVQVCWEKFARYFEVELKEVKLSEGYYVMDPQQAVDMVDENTICVAAILGSTLNGEFEDVKLLNDLLVEKNKETGWDTPIHVDAASGGFIAPFLYPELEWDFRLPLVKSINVSGHKYGLVYAGIGWVIWRNKEDLPEELIFHINYLGADQPTFTLNFSKGSSQVIAQYYQLIRLGHEGYRNVMENCRENMIVLREGLEKTERFNIVSKDEGVPLVAFSLKDSSCHTEFEISDMLRRYGWIVPAYTMPPNAQHITVLRVVIREDFSRTLAERLVIDIEKVMRELDELPSRVIHKISLGQEKSESNSDNLMVTVKKSDIDKQRDIITGWKKFVADRKKTSGIC","length":502,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":11,"region_id":"DP02726r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"The first 11 N-terminal residues are disordered, while residues 12–20 assume a conformation resembling that found in the low-pH structure of GadB (1PMM).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19580813","version":2,"reference_html":"A common structural basis for pH- and calmodulin-mediated regulation in plant glutamate decarboxylase. <i> Gut H, Dominici P, Pilati S, Astegno A, Petoukhov MV, Svergun DI, Grütter MG, Capitani G. </i> J Mol Biol, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3HBX"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":502,"region_id":"DP02726r002","start":449,"term_id":"IDPO:0000002","statement":[{"text":"Residues 449–502 are disordered in the Gad1 crystal structure at pH 5.5. This C-terminal domain consists of a linker of varying lengths in different plant Gads (residues 449–470 in Gad1, Fig. 3), followed by the well-characterized and conserved CaMBD (residues 471 – 502).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19580813","version":2,"reference_html":"A common structural basis for pH- and calmodulin-mediated regulation in plant glutamate decarboxylase. <i> Gut H, Dominici P, Pilati S, Astegno A, Petoukhov MV, Svergun DI, Grütter MG, Capitani G. </i> J Mol Biol, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3HBX"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":470,"region_id":"DP02726r003","start":449,"term_id":"IDPO:0000033","statement":[{"text":"Residues 449–502 are disordered in the Gad1 crystal structure at pH 5.5. This C-terminal domain consists of a linker of varying lengths in different plant Gads (residues 449–470 in Gad1, Fig. 3), followed by the well-characterized and conserved CaMBD (residues 471 – 502).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19580813","version":3,"reference_html":"A common structural basis for pH- and calmodulin-mediated regulation in plant glutamate decarboxylase. <i> Gut H, Dominici P, Pilati S, Astegno A, Petoukhov MV, Svergun DI, Grütter MG, Capitani G. </i> J Mol Biol, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3HBX"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":502,"region_id":"DP02726r004","start":471,"term_id":"GO:0005515","statement":[{"text":"Residues 449–502 are disordered in the Gad1 crystal structure at pH 5.5. This C-terminal domain consists of a linker of varying lengths in different plant Gads (residues 449–470 in Gad1, Fig. 3), followed by the well-characterized and conserved CaMBD (residues 471 – 502).","type":"Results"},{"text":"The CaMBD is located at the C-terminus of the protein and is preceded by a flexible stretch of ∼20 residues. This results in the highly flexible binding mode for attached CaM molecules.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"static light scattering assay evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19580813","version":3,"reference_html":"A common structural basis for pH- and calmodulin-mediated regulation in plant glutamate decarboxylase. <i> Gut H, Dominici P, Pilati S, Astegno A, Petoukhov MV, Svergun DI, Grütter MG, Capitani G. </i> J Mol Biol, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007066","cross_refs":[{"db":"PDB","id":"3HBX"}],"term_name":"protein binding","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":502,"region_id":"DP02726r005","start":471,"term_id":"GO:0005515","statement":[{"text":"Residues 449–502 are disordered in the Gad1 crystal structure at pH 5.5. This C-terminal domain consists of a linker of varying lengths in different plant Gads (residues 449–470 in Gad1, Fig. 3), followed by the well-characterized and conserved CaMBD (residues 471 – 502).","type":"Results"},{"text":"The CaMBD is located at the C-terminus of the protein and is preceded by a flexible stretch of ∼20 residues. This results in the highly flexible binding mode for attached CaM molecules.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19580813","version":3,"reference_html":"A common structural basis for pH- and calmodulin-mediated regulation in plant glutamate decarboxylase. <i> Gut H, Dominici P, Pilati S, Astegno A, Petoukhov MV, Svergun DI, Grütter MG, Capitani G. </i> J Mol Biol, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","cross_refs":[{"db":"PDB","id":"3HBX"}],"term_name":"protein binding","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":57,"region_id":"DP02726r006","start":1,"term_id":"GO:0060090","statement":[{"text":"The N-terminal domain (residues 1–57, Fig. 1 and see Fig. 6) has an important role in the formation and stabilization of the dimer and hexamer.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19580813","version":3,"reference_html":"A common structural basis for pH- and calmodulin-mediated regulation in plant glutamate decarboxylase. <i> Gut H, Dominici P, Pilati S, Astegno A, Petoukhov MV, Svergun DI, Grütter MG, Capitani G. </i> J Mol Biol, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3HBX"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":502,"region_id":"DP02726r007","start":471,"term_id":"GO:0098772","statement":[{"text":"CaM activates Gad1 in a unique way by relieving two C-terminal autoinhibition domains of adjacent active sites, forming a 393 kDa Gad1–CaM complex with an unusual 1:3 stoichiometry.","type":"Abstract"},{"text":"Many plant species like soybean, tobacco, petunia and Arabidopsis, express Gad proteins containing a 30 – 50 residue C-terminal extension compared to the bacterial enzyme sequence. The additional domain has been identified as a CaMBD15 and autoinhibits the Gad protein in the absence of Ca2+/CaM, whereas Gad activity is upregulated upon addition of Ca2+/CaM.","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19580813","version":3,"reference_html":"A common structural basis for pH- and calmodulin-mediated regulation in plant glutamate decarboxylase. <i> Gut H, Dominici P, Pilati S, Astegno A, Petoukhov MV, Svergun DI, Grütter MG, Capitani G. </i> J Mol Biol, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","cross_refs":[{"db":"PDB","id":"3HBX"}],"term_name":"molecular function regulator","curator_orcid":"0000-0002-0341-4888","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":3702,"disprot_id":"DP02726","date":"2020-03-27T10:20:40.723Z","organism":"Arabidopsis thaliana","regions_counter":7,"name":"Glutamate decarboxylase 1","dataset":[],"UniParc":"UPI000016DA16","uniref100":"UniRef100_Q42521","uniref90":"UniRef90_Q42521","uniref50":"UniRef50_Q42521","genes":[{"name":{"value":"GAD1"},"synonyms":[{"value":"GAD"},{"value":"GDH1"}],"orfNames":[{"value":"MKP11.30"},{"value":"MKP11_18"}],"olnNames":[{"value":"At5g17330"}]}],"alphafold_very_low_content":0.0697211155378486,"disorder_content":0.1294820717131474,"disprot_consensus":{"full":[{"start":1,"end":11,"type":"D"},{"start":12,"end":57,"type":"F"},{"start":449,"end":502,"type":"D"}],"Structural state":[{"start":1,"end":11,"type":"D"},{"start":449,"end":502,"type":"D"}],"Disorder function":[{"start":449,"end":470,"type":"F"}],"Molecular function":[{"start":1,"end":57,"type":"F"},{"start":471,"end":502,"type":"F"}]}},{"acc":"Q13526","features":{"gene3D":[],"pfam":[{"id":"PF00397","name":"WW domain","start":7,"end":37},{"id":"PF00639","name":"PPIC-type PPIASE domain","start":59,"end":162}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MADEEKLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGNSSSGGKNGQGEPARVRCSHLLVKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE","length":163,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":50,"region_id":"DP02727r001","start":39,"term_id":"IDPO:0000002","statement":[{"text":"Pin1 contains an N-terminal WW domain and a C-terminal peptidyl-prolyl cis-trans isomerase (PPIase) domain connected by a flexible linker.","type":"Article"},{"text":"residues 39–50 are disordered","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10932246","version":2,"reference_html":"Structural basis for phosphoserine-proline recognition by group IV WW domains. <i> Verdecia MA, Bowman ME, Lu KP, Hunter T, Noel JP. </i> Nat Struct Biol, 2000","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1F8A"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":50,"region_id":"DP02727r002","start":39,"term_id":"IDPO:0000033","statement":[{"text":"Pin1 contains an N-terminal WW domain and a C-terminal peptidyl-prolyl cis-trans isomerase (PPIase) domain connected by a flexible linker.","type":"Article"},{"text":"residues 39–50 are disordered","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10932246","version":3,"reference_html":"Structural basis for phosphoserine-proline recognition by group IV WW domains. <i> Verdecia MA, Bowman ME, Lu KP, Hunter T, Noel JP. </i> Nat Struct Biol, 2000","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1F8A"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2020_12","ncbi_taxon_id":9606,"disprot_id":"DP02727","date":"2020-03-27T19:02:47.551Z","organism":"Homo sapiens","regions_counter":2,"name":"Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1","dataset":[],"UniParc":"UPI000004062D","uniref100":"UniRef100_Q13526","uniref90":"UniRef90_Q13526","uniref50":"UniRef50_Q13526","genes":[{"name":{"value":"PIN1"}}],"alphafold_very_low_content":0.05521472392638037,"disorder_content":0.0736196319018405,"disprot_consensus":{"full":[{"start":39,"end":50,"type":"D"}],"Structural state":[{"start":39,"end":50,"type":"D"}],"Disorder function":[{"start":39,"end":50,"type":"F"}]}},{"acc":"P42166","features":{"gene3D":[{"start":103,"end":159,"id":"G3DSA:1.10.720.40","name":"G3DSA:1.10.720.40"},{"start":103,"end":159,"id":"G3DSA:1.10.720.40","name":"G3DSA:1.10.720.40"}],"pfam":[{"id":"PF03020","name":"LEM domain","start":111,"end":155},{"id":"PF08198","name":"Thymopoietin protein","start":2,"end":49},{"id":"PF11560","name":"Lamina-associated polypeptide 2 alpha","start":461,"end":693}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MPEFLEDPSVLTKDKLKSELVANNVTLPAGEQRKDVYVQLYLQHLTARNRPPLPAGTNSKGPPDFSSDEEREPTPVLGSGAAAAGRSRAAVGRKATKKTDKPRQEDKDDLDVTELTNEDLLDQLVKYGVNPGPIVGTTRKLYEKKLLKLREQGTESRSSTPLPTISSSAENTRQNGSNDSDRYSDNEEGKKKEHKKVKSTRDIVPFSELGTTPSGGGFFQGISFPEISTRPPLGSTELQAAKKVHTSKGDLPREPLVATNLPGRGQLQKLASERNLFISCKSSHDRCLEKSSSSSSQPEHSAMLVSTAASPSLIKETTTGYYKDIVENICGREKSGIQPLCPERSHISDQSPLSSKRKALEESESSQLISPPLAQAIRDYVNSLLVQGGVGSLPGTSNSMPPLDVENIQKRIDQSKFQETEFLSPPRKVPRLSEKSVEERDSGSFVAFQNIPGSELMSSFAKTVVSHSLTTLGLEVAKQSQHDKIDASELSFPFHESILKVIEEEWQQVDRQLPSLACKYPVSSREATQILSVPKVDDEILGFISEATPLGGIQAASTESCNQQLDLALCRAYEAAASALQIATHTAFVAKAMQADISQAAQILSSDPSRTHQALGILSKTYDAASYICEAAFDEVKMAAHTMGNATVGRRYLWLKDCKINLASKNKLASTPFKGGTLFGGEVCKVIKKRGNKH","length":694,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":110,"region_id":"DP02728r001","start":51,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Human LAP2(1-168) has two structurally independent, non-interacting domains located at residues 1-50 ('LAP2-N') and residues 111-152 (LEM-domain), connected by an approximately 60-residue flexible linker.","type":"Abstract"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11500367","version":2,"reference_html":"Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: one binds BAF and the other binds DNA. <i> Cai M, Huang Y, Ghirlando R, Wilson KL, Craigie R, Clore GM. </i> EMBO J, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"1GJJ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-04T15:13:10.401Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":110,"region_id":"DP02728r002","start":51,"term_id":"IDPO:0000033","unpublished":true,"statement":[{"text":"Human LAP2(1-168) has two structurally independent, non-interacting domains located at residues 1-50 ('LAP2-N') and residues 111-152 (LEM-domain), connected by an approximately 60-residue flexible linker.","type":"Abstract"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11500367","version":3,"reference_html":"Solution structure of the constant region of nuclear envelope protein LAP2 reveals two LEM-domain structures: one binds BAF and the other binds DNA. <i> Cai M, Huang Y, Ghirlando R, Wilson KL, Craigie R, Clore GM. </i> EMBO J, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"1GJJ"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-04T15:13:12.383Z"}}],"released":"2023_12","ncbi_taxon_id":9606,"disprot_id":"DP02728","date":"2020-03-27T19:19:07.009Z","organism":"Homo sapiens","regions_counter":2,"name":"Lamina-associated polypeptide 2, isoform alpha","dataset":[],"UniParc":"UPI000013D709","uniref100":"UniRef100_P42166","uniref90":"UniRef90_P42166","uniref50":"UniRef50_P42166","genes":[{"name":{"value":"TMPO"},"synonyms":[{"value":"LAP2"}]}],"alphafold_very_low_content":0.49135446685878964,"disorder_content":0.08645533141210375,"disprot_consensus":{"full":[{"start":51,"end":110,"type":"D"}],"Structural state":[{"start":51,"end":110,"type":"D"}],"Disorder function":[{"start":51,"end":110,"type":"F"}]}},{"acc":"Q96EP1","features":{"gene3D":[{"start":276,"end":397,"id":"G3DSA:3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"}],"pfam":[{"id":"PF00498","name":"FHA domain","start":38,"end":105},{"id":"PF13923","name":"Zinc finger, C3HC4 type (RING finger)","start":304,"end":342},{"id":"PF17979","name":"Cysteine rich domain with multizinc binding regions","start":466,"end":620}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MERPEEGKQSPPPQPWGRLLRLGAEEGEPHVLLRKREWTIGRRRGCDLSFPSNKLVSGDHCRIVVDEKSGQVTLEDTSTSGTVINKLKVVKKQTCPLQTGDVIYLVYRKNEPEHNVAYLYESLSEKQGMTQESFEANKENVFHGTKDTSGAGAGRGADPRVPPSSPATQVCFEEPQPSTSTSDLFPTASASSTEPSPAGRERSSSCGSGGGGISPKGSGPSVASDEVSSFASALPDRKTASFSSLEPQDQEDLEPVKKKMRGDGDLDLNGQLLVAQPRRNAQTVHEDVRAAAGKPDKMEETLTCIICQDLLHDCVSLQPCMHTFCAACYSGWMERSSLCPTCRCPVERICKNHILNNLVEAYLIQHPDKSRSEEDVQSMDARNKITQDMLQPKVRRSFSDEEGSSEDLLELSDVDSESSDISQPYVVCRQCPEYRRQAAQPPHCPAPEGEPGAPQALGDAPSTSVSLTTAVQDYVCPLQGSHALCTCCFQPMPDRRAEREQDPRVAPQQCAVCLQPFCHLYWGCTRTGCYGCLAPFCELNLGDKCLDGVLNNNSYESDILKNYLATRGLTWKNMLTESLVALQRGVFLLSDYRVTGDTVLCYCCGLRSFRELTYQYRQNIPASELPVAVTSRPDCYWGRNCRTQVKAHHAMKFNHICEQTRFKN","length":664,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":472,"region_id":"DP02729r001","start":446,"term_id":"IDPO:0000002","statement":[{"text":"In both structures, residues 425–445 and 473–663 are modeled, whereas no ordered electron density was observed for residues 446–472.","type":"Results"},{"text":"This incompatibility and the observation that the C terminus of CHFR and the phosphate and ribose groups of the ligand are only ordered in the CHFR-C·AMP2 structure suggest that one molecule of the AMP2 is bound to the protein, with the caveat that we were not able to model the entire ligand linker motif, presumably due to its flexibility.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20880844","version":2,"reference_html":"Structural basis of poly(ADP-ribose) recognition by the multizinc binding domain of checkpoint with forkhead-associated and RING Domains (CHFR). <i> Oberoi J, Richards MW, Crumpler S, Brown N, Blagg J, Bayliss R. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2XOZ"},{"db":"PDB","id":"2XOC"},{"db":"PDB","id":"2XOY"},{"db":"PDB","id":"2XP0"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":472,"region_id":"DP02729r002","start":446,"term_id":"IDPO:0000033","statement":[{"text":"In both structures, residues 425–445 and 473–663 are modeled, whereas no ordered electron density was observed for residues 446–472.","type":"Results"},{"text":"This incompatibility and the observation that the C terminus of CHFR and the phosphate and ribose groups of the ligand are only ordered in the CHFR-C·AMP2 structure suggest that one molecule of the AMP2 is bound to the protein, with the caveat that we were not able to model the entire ligand linker motif, presumably due to its flexibility.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20880844","version":3,"reference_html":"Structural basis of poly(ADP-ribose) recognition by the multizinc binding domain of checkpoint with forkhead-associated and RING Domains (CHFR). <i> Oberoi J, Richards MW, Crumpler S, Brown N, Blagg J, Bayliss R. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2XOZ"},{"db":"PDB","id":"2XOC"},{"db":"PDB","id":"2XOY"},{"db":"PDB","id":"2XP0"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02729","date":"2020-03-31T08:43:38.476Z","organism":"Homo sapiens","regions_counter":2,"name":"E3 ubiquitin-protein ligase CHFR","dataset":[],"UniParc":"UPI000006EA87","uniref100":"UniRef100_Q96EP1","uniref90":"UniRef90_Q96EP1","uniref50":"UniRef50_Q96EP1","genes":[{"name":{"value":"CHFR"},"synonyms":[{"value":"RNF196"}]}],"alphafold_very_low_content":0.338855421686747,"disorder_content":0.04066265060240964,"disprot_consensus":{"full":[{"start":446,"end":472,"type":"D"}],"Structural state":[{"start":446,"end":472,"type":"D"}],"Disorder function":[{"start":446,"end":472,"type":"F"}]}},{"acc":"Q6P1M3","features":{"gene3D":[{"start":19,"end":173,"id":"G3DSA:2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"}],"pfam":[{"id":"PF00400","name":"WD domain, G-beta repeat","start":432,"end":451},{"id":"PF08366","name":"LLGL2","start":273,"end":372}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MRRFLRPGHDPVRERLKRDLFQFNKTVEHGFPHQPSALGYSPSLRILAIGTRSGAIKLYGAPGVEFMGLHQENNAVTQIHLLPGQCQLVTLLDDNSLHLWSLKVKGGASELQEDESFTLRGPPGAAPSATQITVVLPHSSCELLYLGTESGNVFVVQLPAFRALEDRTISSDAVLQRLPEEARHRRVFEMVEALQEHPRDPNQILIGYSRGLVVIWDLQGSRVLYHFLSSQQLENIWWQRDGRLLVSCHSDGSYCQWPVSSEAQQPEPLRSLVPYGPFPCKAITRILWLTTRQGLPFTIFQGGMPRASYGDRHCISVIHDGQQTAFDFTSRVIGFTVLTEADPAATFDDPYALVVLAEEELVVIDLQTAGWPPVQLPYLASLHCSAITCSHHVSNIPLKLWERIIAAGSRQNAHFSTMEWPIDGGTSLTPAPPQRDLLLTGHEDGTVRFWDASGVCLRLLYKLSTVRVFLTDTDPNENFSAQGEDEWPPLRKVGSFDPYSDDPRLGIQKIFLCKYSGYLAVAGTAGQVLVLELNDEAAEQAVEQVEADLLQDQEGYRWKGHERLAARSGPVRFEPGFQPFVLVQCQPPAVVTSLALHSEWRLVAFGTSHGFGLFDHQQRRQVFVKCTLHPSDQLALEGPLSRVKSLKKSLRQSFRRMRRSRVSSRKRHPAGPPGEAQEGSAKAERPGLQNMELAPVQRKIEARSAEDSFTGFVRTLYFADTYLKDSSRHCPSLWAGTNGGTIYAFSLRVPPAERRMDEPVRAEQAKEIQLMHRAPVVGILVLDGHSVPLPEPLEVAHDLSKSPDMQGSHQLLVVSEEQFKVFTLPKVSAKLKLKLTALEGSRVRRVSVAHFGSRRAEDYGEHHLAVLTNLGDIQVVSLPLLKPQVRYSCIRREDVSGIASCVFTKYGQGFYLISPSEFERFSLSTKWLVEPRCLVDSAETKNHRPGNGAGPKKAPSRARNSGTQSDGEEKQPGLVMERALLSDERVLKEIQSTLEGDRGSGNWRSHRAAVGCSLSNGGAE","length":1020,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":484,"region_id":"DP02730r001","start":471,"term_id":"IDPO:0000002","statement":[{"text":"The crystal form 1 Lgl2 structure includes 827 of 979 amino acids of the Lgl2 protein construct; there was no electron density for residues 13–17, 471–484, 635–707, and 853–858.","type":"Results"},{"text":"Crystal structure of the human cell polarity protein Lethal Giant Larvae 2 (Lgl2). Unphosphorylated, crystal form 1.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"31088962","version":2,"reference_html":"Structural insights into the aPKC regulatory switch mechanism of the human cell polarity protein lethal giant larvae 2. <i> Almagor L, Ufimtsev IS, Ayer A, Li J, Weis WI. </i> Proc Natl Acad Sci U S A, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6N8P"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":708,"region_id":"DP02730r002","start":631,"term_id":"IDPO:0000002","statement":[{"text":"The crystal form 1 Lgl2 structure includes 827 of 979 amino acids of the Lgl2 protein construct; there was no electron density for residues 13–17, 471–484, 635–707, and 853–858.","type":"Results"},{"text":"Crystal structure of the human cell polarity protein Lethal Giant Larvae 2 (Lgl2). Unphosphorylated, crystal form 1.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"31088962","version":2,"reference_html":"Structural insights into the aPKC regulatory switch mechanism of the human cell polarity protein lethal giant larvae 2. <i> Almagor L, Ufimtsev IS, Ayer A, Li J, Weis WI. </i> Proc Natl Acad Sci U S A, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6N8P"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":708,"region_id":"DP02730r003","start":631,"term_id":"IDPO:0000033","statement":[{"text":"The crystal form 1 Lgl2 structure includes 827 of 979 amino acids of the Lgl2 protein construct; there was no electron density for residues 13–17, 471–484, 635–707, and 853–858.","type":"Results"},{"text":"Both the unphosphorylated and phosphorylated form 2 structures are missing residues 261–263, 472–485, and 631–708, and the loop residues 554–555 are missing in the unphosphorylated form 2 structure.","type":"Results"},{"text":"Linker separating WD40 repeats 9 and 10","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"31088962","version":3,"reference_html":"Structural insights into the aPKC regulatory switch mechanism of the human cell polarity protein lethal giant larvae 2. <i> Almagor L, Ufimtsev IS, Ayer A, Li J, Weis WI. </i> Proc Natl Acad Sci U S A, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6N8P"},{"db":"PDB","id":"6N8R"},{"db":"PDB","id":"6N8S"},{"db":"PDB","id":"6N8Q"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":484,"region_id":"DP02730r004","start":471,"term_id":"IDPO:0000033","statement":[{"text":"The crystal form 1 Lgl2 structure includes 827 of 979 amino acids of the Lgl2 protein construct; there was no electron density for residues 13–17, 471–484, 635–707, and 853–858.","type":"Results"},{"text":"Both the unphosphorylated and phosphorylated form 2 structures are missing residues 261–263, 472–485, and 631–708, and the loop residues 554–555 are missing in the unphosphorylated form 2 structure.","type":"Results"},{"text":"Linker separating WD40 repeats 8 and 9","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"31088962","version":3,"reference_html":"Structural insights into the aPKC regulatory switch mechanism of the human cell polarity protein lethal giant larvae 2. <i> Almagor L, Ufimtsev IS, Ayer A, Li J, Weis WI. </i> Proc Natl Acad Sci U S A, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6N8P"},{"db":"PDB","id":"6N8R"},{"db":"PDB","id":"6N8S"},{"db":"PDB","id":"6N8Q"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":708,"region_id":"DP02730r005","start":631,"term_id":"IDPO:0000045","statement":[{"text":"We examined the phosphorylation of purified Lgl2 treated with purified aPKCι by mass spectrometry (the same sample that was used for crystallization), and found seven phosphorylated serine residues on the 10–11 loop (S641, S645, S649, S653, S660, S663, and S680), which include the previously reported sites","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"mass spectrometry evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"31088962","version":2,"reference_html":"Structural insights into the aPKC regulatory switch mechanism of the human cell polarity protein lethal giant larvae 2. <i> Almagor L, Ufimtsev IS, Ayer A, Li J, Weis WI. </i> Proc Natl Acad Sci U S A, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001230","cross_refs":[{"db":"PDB","id":"6N8R"},{"db":"PDB","id":"6N8S"}],"term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02730","date":"2020-03-31T09:42:19.759Z","organism":"Homo sapiens","regions_counter":6,"name":"LLGL scribble cell polarity complex component 2","dataset":[],"UniParc":"UPI0000232A48","uniref100":"UniRef100_Q6P1M3","uniref90":"UniRef90_Q6P1M3","uniref50":"UniRef50_Q6P1M3","genes":[{"name":{"value":"LLGL2"}}],"alphafold_very_low_content":0.1450980392156863,"disorder_content":0.09019607843137255,"disprot_consensus":{"full":[{"start":471,"end":484,"type":"D"},{"start":631,"end":708,"type":"D"}],"Structural state":[{"start":471,"end":484,"type":"D"},{"start":631,"end":708,"type":"D"}],"Disorder function":[{"start":471,"end":484,"type":"F"},{"start":631,"end":708,"type":"F"}]}},{"acc":"Q5U651","features":{"gene3D":[],"pfam":[{"id":"PF00788","name":"Ras association (RalGDS/AF-6) domain","start":145,"end":258},{"id":"PF01843","name":"DIL domain","start":770,"end":875}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MLSGERKEGGSPRFGKLHLPVGLWINSPRKQLAKLGRRWPSAASVKSSSSDTGSRSSEPLPPPPPHVELRRVGAVKAAGGASGSRAKRISQLFRGSGTGTTGSSGAGGPGTPGGAQRWASEKKLPELAAGVAPEPPLATRATAPPGVLKIFGAGLASGANYKSVLATARSTARELVAEALERYGLAGSPGGGPGESSCVDAFALCDALGRPAAAGVGSGEWRAEHLRVLGDSERPLLVQELWRARPGWARRFELRGREEARRLEQEAFGAADSEGTGAPSWRPQKNRSRAASGGAALASPGPGTGSGAPAGSGGKERSENLSLRRSVSELSLQGRRRRQQERRQQALSMAPGAADAQIGTADPGDFDQLTQCLIQAPSNRPYFLLLQGYQDAQDFVVYVMTREQHVFGRGGNSSGRGGSPAPYVDTFLNAPDILPRHCTVRAGPEHPAMVRPSRGAPVTHNGCLLLREAELHPGDLLGLGEHFLFMYKDPRTGGSGPARPPWLPARPGATPPGPGWAFSCRLCGRGLQERGEALAAYLDGREPVLRFRPREEEALLGEIVRAAAAGSGDLPPLGPATLLALCVQHSARELELGHLPRLLGRLARLIKEAVWEKIKEIGDRQPENHPEGVPEVPLTPEAVSVELRPLMLWMANTTELLSFVQEKVLEMEKEADQEDPQLCNDLELCDEAMALLDEVIMCTFQQSVYYLTKTLYSTLPALLDSNPFTAGAELPGPGAELGAMPPGLRPTLGVFQAALELTSQCELHPDLVSQTFGYLFFFSNASLLNSLMERGQGRPFYQWSRAVQIRTNLDLVLDWLQGAGLGDIATEFFRKLSMAVNLLCVPRTSLLKASWSSLRTDHPTLTPAQLHHLLSHYQLGPGRGPPAAWDPPPAEREAVDTGDIFESFSSHPPLILPLGSSRLRLTGPVTDDALHRELRRLRRLLWDLEQQELPANYRHGPPVATSP","length":963,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":197,"region_id":"DP02731r001","start":187,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The current RRA model excludes many residues; 141–142 (N terminus), 154–158 (loop β1-β2), 187–197 (loop α1-β3), 212–220 (loop β3-β4), and 268–285 (C terminus, not part of the RRA) as highlighted in Figures 2A and 2C, and many side chains were also poorly defined in the electron density map.","type":"Results"},{"text":"Similar to the free RA domain structure, the current Rasip1 RA domain model excludes many residues, 141–142 (N terminus), 186–195 (loop α1-β3), 212–220 (loop β3-β4), and 268–285 (C terminus), and many side chains were also poorly defined in the electron density map.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27839947","version":2,"reference_html":"Structural Basis of Dimeric Rasip1 RA Domain Recognition of the Ras Subfamily of GTP-Binding Proteins. <i> Gingras AR, Puzon-McLaughlin W, Bobkov AA, Ginsberg MH. </i> Structure, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5KHQ"},{"db":"PDB","id":"5KHO"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":285,"region_id":"DP02731r002","start":268,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The current RRA model excludes many residues; 141–142 (N terminus), 154–158 (loop β1-β2), 187–197 (loop α1-β3), 212–220 (loop β3-β4), and 268–285 (C terminus, not part of the RRA) as highlighted in Figures 2A and 2C, and many side chains were also poorly defined in the electron density map.","type":"Results"},{"text":"Similar to the free RA domain structure, the current Rasip1 RA domain model excludes many residues, 141–142 (N terminus), 186–195 (loop α1-β3), 212–220 (loop β3-β4), and 268–285 (C terminus), and many side chains were also poorly defined in the electron density map.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27839947","version":2,"reference_html":"Structural Basis of Dimeric Rasip1 RA Domain Recognition of the Ras Subfamily of GTP-Binding Proteins. <i> Gingras AR, Puzon-McLaughlin W, Bobkov AA, Ginsberg MH. </i> Structure, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5KHQ"},{"db":"PDB","id":"5KHO"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":285,"region_id":"DP02731r003","start":268,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The current RRA model excludes many residues; 141–142 (N terminus), 154–158 (loop β1-β2), 187–197 (loop α1-β3), 212–220 (loop β3-β4), and 268–285 (C terminus, not part of the RRA) as highlighted in Figures 2A and 2C, and many side chains were also poorly defined in the electron density map.","type":"Results"},{"text":"Similar to the free RA domain structure, the current Rasip1 RA domain model excludes many residues, 141–142 (N terminus), 186–195 (loop α1-β3), 212–220 (loop β3-β4), and 268–285 (C terminus), and many side chains were also poorly defined in the electron density map.","type":"Results"},{"text":"This observation was in agreement with the NMR spectrum of the complex, which showed that most of the sharp peaks remained sharp when in complex with Rap1; this suggested that the unstructured loops remained unstructured in the complex.","type":"Results"},{"text":"The Rasip1 RA domain contains many unstructured loops as demonstrated by both the presence of many sharp peaks in the NMR sfHMQC and the absence of electron density in the crystal structure.","type":"Discussion"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27839947","version":2,"reference_html":"Structural Basis of Dimeric Rasip1 RA Domain Recognition of the Ras Subfamily of GTP-Binding Proteins. <i> Gingras AR, Puzon-McLaughlin W, Bobkov AA, Ginsberg MH. </i> Structure, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"5KHQ"},{"db":"PDB","id":"5KHO"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":197,"region_id":"DP02731r004","start":187,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The current RRA model excludes many residues; 141–142 (N terminus), 154–158 (loop β1-β2), 187–197 (loop α1-β3), 212–220 (loop β3-β4), and 268–285 (C terminus, not part of the RRA) as highlighted in Figures 2A and 2C, and many side chains were also poorly defined in the electron density map.","type":"Results"},{"text":"Similar to the free RA domain structure, the current Rasip1 RA domain model excludes many residues, 141–142 (N terminus), 186–195 (loop α1-β3), 212–220 (loop β3-β4), and 268–285 (C terminus), and many side chains were also poorly defined in the electron density map.","type":"Results"},{"text":"This observation was in agreement with the NMR spectrum of the complex, which showed that most of the sharp peaks remained sharp when in complex with Rap1; this suggested that the unstructured loops remained unstructured in the complex.","type":"Results"},{"text":"The Rasip1 RA domain contains many unstructured loops as demonstrated by both the presence of many sharp peaks in the NMR sfHMQC and the absence of electron density in the crystal structure.","type":"Discussion"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27839947","version":2,"reference_html":"Structural Basis of Dimeric Rasip1 RA Domain Recognition of the Ras Subfamily of GTP-Binding Proteins. <i> Gingras AR, Puzon-McLaughlin W, Bobkov AA, Ginsberg MH. </i> Structure, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"5KHQ"},{"db":"PDB","id":"5KHO"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2023_12","ncbi_taxon_id":9606,"disprot_id":"DP02731","date":"2020-03-31T14:00:21.803Z","organism":"Homo sapiens","regions_counter":4,"name":"Ras-interacting protein 1","dataset":[],"UniParc":"UPI000020283D","uniref100":"UniRef100_Q5U651","uniref90":"UniRef90_Q5U651","uniref50":"UniRef50_Q5U651","genes":[{"name":{"value":"RASIP1"}}],"alphafold_very_low_content":0.2782969885773624,"disorder_content":0.030114226375908618,"disprot_consensus":{"full":[{"start":187,"end":197,"type":"D"},{"start":268,"end":285,"type":"D"}],"Structural state":[{"start":187,"end":197,"type":"D"},{"start":268,"end":285,"type":"D"}]}},{"acc":"Q8IWJ2","features":{"gene3D":[],"pfam":[{"id":"PF01465","name":"GRIP domain","start":1614,"end":1656},{"id":"PF16704","name":"Rab binding domain","start":1548,"end":1612}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MEDLVQDGVASPATPGTGKSKLETLPKEDLIKFAKKQMMLIQKAKSRCTELEKEIEELRSKPVTEGTGDIIKALTERLDALLLEKAETEQQCLSLKKENIKMKQEVEDSVTKMGDAHKELEQSHINYVKEIENLKNELMAVRSKYSEDKANLQKQLEEAMNTQLELSEQLKFQNNSEDNVKKLQEEIEKIRPGFEEQILYLQKQLDATTDEKKETVTQLQNIIEANSQHYQKNINSLQEELLQLKAIHQEEVKELMCQIEASAKEHEAEINKLNELKENLVKQCEASEKNIQKKYECELENLRKATSNANQDNQICSILLQENTFVEQVVNEKVKHLEDTLKELESQHSILKDEVTYMNNLKLKLEMDAQHIKDEFFHEREDLEFKINELLLAKEEQGCVIEKLKSELAGLNKQFCYTVEQHNREVQSLKEQHQKEISELNETFLSDSEKEKLTLMFEIQGLKEQCENLQQEKQEAILNYESLREIMEILQTELGESAGKISQEFESMKQQQASDVHELQQKLRTAFTEKDALLETVNRLQGENEKLLSQQELVPELENTIKNLQEKNGVYLLSLSQRDTMLKELEGKINSLTEEKDDFINKLKNSHEEMDNFHKKCEREERLILELGKKVEQTIQYNSELEQKVNELTGGLEETLKEKDQNDQKLEKLMVQMKVLSEDKEVLSAEVKSLYEENNKLSSEKKQLSRDLEVFLSQKEDVILKEHITQLEKKLQLMVEEQDNLNKLLENEQVQKLFVKTQLYGFLKEMGSEVSEDSEEKDVVNVLQAVGESLAKINEEKCNLAFQRDEKVLELEKEIKCLQEESVVQCEELKSLLRDYEQEKVLLRKELEEIQSEKEALQSDLLEMKNANEKTRLENQNLLIQVEEVSQTCSKSEIHNEKEKCFIKEHENLKPLLEQKELRDRRAELILLKDSLAKSPSVKNDPLSSVKELEEKIENLEKECKEKEEKINKIKLVAVKAKKELDSSRKETQTVKEELESLRSEKDQLSASMRDLIQGAESYKNLLLEYEKQSEQLDVEKERANNFEHRIEDLTRQLRNSTLQCETINSDNEDLLARIETLQSNAKLLEVQILEVQRAKAMVDKELEAEKLQKEQKIKEHATTVNELEELQVQLQKQKKQLQKTMQELELVKKDAQQTTLMNMEIADYERLMKELNQKLTNKNNKIEDLEQEIKIQKQKQETLQEEITSLQSSVQQYEEKNTKIKQLLVKTKKELADSKQAETDHLILQASLKGELEASQQQVEVYKIQLAEITSEKHKIHEHLKTSAEQHQRTLSAYQQRVTALQEECRAAKAEQATVTSEFESYKVRVHNVLKQQKNKSMSQAETEGAKQEREHLEMLIDQLKIKLQDSQNNLQINVSELQTLQSEHDTLLERHNKMLQETVSKEAELREKLCSIQSENMMMKSEHTQTVSQLTSQNEVLRNSFRDQVRHLQEEHRKTVETLQQQLSKMEAQLFQLKNEPTTRSPVSSQQSLKNLRERRNTDLPLLDMHTVTREEGEGMETTDTESVSSASTYTQSLEQLLNSPETKLEPPLWHAEFTKEELVQKLSSTTKSADHLNGLLRETEATNAILMEQIKLLKSEIRRLERNQEREKSAANLEYLKNVLLQFIFLKPGSERERLLPVINTMLQLSPEEKGKLAAVAQGEEENASRSSGWASYLHSWSGLR","length":1684,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1569,"region_id":"DP02732r001","start":1547,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"In addition, flexible regions were detected downstream of the GRIP domain (∼20 residues), and spanning ∼40 residues upstream of residue 1527","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18243103","version":2,"reference_html":"Rab and Arl GTPase family members cooperate in the localization of the golgin GCC185. <i> Burguete AS, Fenn TD, Brunger AT, Pfeffer SR. </i> Cell, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3BBP"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-13T20:40:59.137Z"}}],"released":"2024_06","ncbi_taxon_id":9606,"disprot_id":"DP02732","date":"2020-03-31T14:39:42.684Z","organism":"Homo sapiens","regions_counter":1,"name":"GRIP and coiled-coil domain-containing protein 2","dataset":["Condensates-related proteins"],"UniParc":"UPI00000744D3","uniref100":"UniRef100_Q8IWJ2","uniref90":"UniRef90_Q8IWJ2","uniref50":"UniRef50_Q8IWJ2","genes":[{"name":{"value":"GCC2"},"synonyms":[{"value":"KIAA0336"},{"value":"RANBP2L4"}]}],"alphafold_very_low_content":0.13657957244655583,"disorder_content":0.013657957244655582,"disprot_consensus":{"full":[{"start":1547,"end":1569,"type":"D"}],"Structural state":[{"start":1547,"end":1569,"type":"D"}]}},{"acc":"P20340","features":{"gene3D":[],"pfam":[{"id":"PF00071","name":"Ras family","start":15,"end":173}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MSTGGDFGNPLRKFKLVFLGEQSVGKTSLITRFMYDSFDNTYQATIGIDFLSKTMYLEDRTVRLQLWDTAGQERFRSLIPSYIRDSTVAVVVYDITNVNSFQQTTKWIDDVRTERGSDVIIMLVGNKTDLADKRQVSIEEGERKAKELNVMFIETSAKAGYNVKQLFRRVAAALPGMESTQDRSREDMIDIKLEKPQEQPVSEGGCSC","length":208,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":206,"region_id":"DP02733r001","start":175,"term_id":"IDPO:0000002","statement":[{"text":"We present a structure-derived model for dual GTPase membrane attachment that highlights the potential ability of Rab GTPases to reach binding partners at a significant distance from the membrane via their unstructured and membrane-anchored, hypervariable domains.","type":"Abstract"},{"text":"An important aspect of our model is the possibility that Rab proteins may reach some distance from the membrane (up to ∼10nm) to bind to an effector protein, due to the unstructured nature of a Rab protein's ∼30 residue, membrane anchored, C-terminal hypervariable domain","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18243103","version":2,"reference_html":"Rab and Arl GTPase family members cooperate in the localization of the golgin GCC185. <i> Burguete AS, Fenn TD, Brunger AT, Pfeffer SR. </i> Cell, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3BBP"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Biological process","ec_ontology":"ECO","end":206,"region_id":"DP02733r002","start":175,"term_id":"GO:0051179","statement":[{"text":"We present a structure-derived model for dual GTPase membrane attachment that highlights the potential ability of Rab GTPases to reach binding partners at a significant distance from the membrane via their unstructured and membrane-anchored, hypervariable domains.","type":"Abstract"},{"text":"An important aspect of our model is the possibility that Rab proteins may reach some distance from the membrane (up to ∼10nm) to bind to an effector protein, due to the unstructured nature of a Rab protein's ∼30 residue, membrane anchored, C-terminal hypervariable domain","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18243103","version":3,"reference_html":"Rab and Arl GTPase family members cooperate in the localization of the golgin GCC185. <i> Burguete AS, Fenn TD, Brunger AT, Pfeffer SR. </i> Cell, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3BBP"}],"term_name":"localization","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02733","date":"2020-03-31T14:56:18.159Z","organism":"Homo sapiens","regions_counter":2,"name":"Ras-related protein Rab-6A","dataset":[],"UniParc":"UPI0000037BDB","uniref100":"UniRef100_P20340","uniref90":"UniRef90_P20340","uniref50":"UniRef50_P20340","genes":[{"name":{"value":"RAB6A"},"synonyms":[{"value":"RAB6"}]}],"alphafold_very_low_content":0.16346153846153846,"disorder_content":0.15384615384615385,"disprot_consensus":{"full":[{"start":175,"end":206,"type":"D"}],"Structural state":[{"start":175,"end":206,"type":"D"}],"Biological process":[{"start":175,"end":206,"type":"F"}]}},{"acc":"P21517","features":{"gene3D":[{"start":525,"end":603,"id":"G3DSA:2.60.40.1180","name":"Golgi alpha-mannosidase II"}],"pfam":[{"id":"PF00128","name":"Alpha amylase, catalytic domain","start":127,"end":284},{"id":"PF00128","name":"Alpha amylase, catalytic domain","start":294,"end":530},{"id":"PF02903","name":"Alpha amylase, N-terminal ig-like domain","start":3,"end":105}]},"creator":"fquaglia","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"sequence":"MLNAWHLPVPPFVKQSKDQLLITLWLTGEDPPQRIMLRTEHDNEEMSVPMHKQRSQPQPGVTAWRAAIDLSSGQPRRRYSFKLLWHDRQRWFTPQGFSRMPPARLEQFAVDVPDIGPQWAADQIFYQIFPDRFARSLPREAEQDHVYYHHAAGQEIILRDWDEPVTAQAGGSTFYGGDLDGISEKLPYLKKLGVTALYLNPVFKAPSVHKYDTEDYRHVDPQFGGDGALLRLRHNTQQLGMRLVLDGVFNHSGDSHAWFDRHNRGTGGACHNPESPWRDWYSFSDDGTALDWLGYASLPKLDYQSESLVNEIYRGEDSIVRHWLKAPWNMDGWRLDVVHMLGEAGGARNNMQHVAGITEAAKETQPEAYIVGEHFGDARQWLQADVEDAAMNYRGFTFPLWGFLANTDISYDPQQIDAQTCMAWMDNYRAGLSHQQQLRMFNQLDSHDTARFKTLLGRDIARLPLAVVWLFTWPGVPCIYYGDEVGLDGKNDPFCRKPFPWQVEKQDTALFALYQRMIALRKKSQALRHGGCQVLYAEDNVVVFVRVLNQQRVLVAINRGEACEVVLPASPFLNAVQWQCKEGHGQLTDGILALPAISATVWMN","length":604,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":131,"region_id":"DP02734r001","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Based on the crystallographic structure, it has been interpreted that the N-terminal region of the enzyme (Met1-Phe131) might be unstructured or flexible.","type":"Abstract"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27317979","version":2,"reference_html":"Role of N-terminal region of Escherichia coli maltodextrin glucosidase in folding and function of the protein. <i> Pastor A, Singh AK, Shukla PK, Equbal MJ, Malik ST, Singh TP, Chaudhuri TK. </i> Biochim Biophys Acta, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5BN7"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-05T15:46:47.808Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":131,"region_id":"DP02734r002","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Based on the crystallographic structure, it has been interpreted that the N-terminal region of the enzyme (Met1-Phe131) might be unstructured or flexible.","type":"Abstract"},{"text":"The native and functional state of MalZ was subjected to limited proteolysis by trypsin (Fig. 5a) as well as proteinase K (Fig. 5b).","type":"Results"},{"text":"The gel run after proteolysis for different time durations show a prominent band at 54 kDa, which is expected to be remaining after a truncation of about 130 amino acids. This was analysed by the molecular weight analysis program Image lab of Bio-rad.","type":"Results"},{"text":"These results confirmed that the N-terminal is getting digested during limited proteolysis. This supports our assumption that the N-terminal domain is either flexible or unstructured.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"cleavage assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27317979","version":2,"reference_html":"Role of N-terminal region of Escherichia coli maltodextrin glucosidase in folding and function of the protein. <i> Pastor A, Singh AK, Shukla PK, Equbal MJ, Malik ST, Singh TP, Chaudhuri TK. </i> Biochim Biophys Acta, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","cross_refs":[{"db":"PDB","id":"5BN7"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":131,"region_id":"DP02734r003","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The CD spectra of N-terminal hence show that although β-strands are predominant, the region is somewhat unstructured with almost half of the region showing random coil structures.","type":"Results"},{"text":"The CD spectra of MalZ N terminal domain, the secondary structure prediction suggests that almost half of the N-terminal region consists of random coil and loop regions.","type":"Figure"},{"text":"The circular dichroism spectra was recorded in the range of 200–300 nm on a Jasco J-815 CD polarimeter.","type":"Methods"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27317979","version":2,"reference_html":"Role of N-terminal region of Escherichia coli maltodextrin glucosidase in folding and function of the protein. <i> Pastor A, Singh AK, Shukla PK, Equbal MJ, Malik ST, Singh TP, Chaudhuri TK. </i> Biochim Biophys Acta, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006200","cross_refs":[{"db":"PDB","id":"5BN7"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":430,"region_id":"DP02734r005","start":419,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The density for residues 419–430 was also not observed.","type":"Figure"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27317979","version":2,"reference_html":"Role of N-terminal region of Escherichia coli maltodextrin glucosidase in folding and function of the protein. <i> Pastor A, Singh AK, Shukla PK, Equbal MJ, Malik ST, Singh TP, Chaudhuri TK. </i> Biochim Biophys Acta, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5BN7"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-05T15:46:36.213Z"}}],"released":"2023_12","ncbi_taxon_id":83333,"disprot_id":"DP02734","date":"2020-03-31T15:36:32.668Z","organism":"Escherichia coli (strain K12)","regions_counter":5,"name":"Maltodextrin glucosidase","dataset":[],"UniParc":"UPI000016F2CF","uniref100":"UniRef100_P21517","uniref90":"UniRef90_P21517","uniref50":"UniRef50_P21517","genes":[{"name":{"value":"malZ"},"olnNames":[{"value":"b0403"},{"value":"JW0393"}]}],"alphafold_very_low_content":0,"disorder_content":0.2367549668874172,"disprot_consensus":{"full":[{"start":1,"end":131,"type":"D"},{"start":419,"end":430,"type":"D"}],"Structural state":[{"start":1,"end":131,"type":"D"},{"start":419,"end":430,"type":"D"}]}},{"acc":"P07355","features":{"gene3D":[{"start":17,"end":339,"id":"G3DSA:1.10.220.10","name":"Annexin"}],"pfam":[{"id":"PF00191","name":"Annexin","start":38,"end":102},{"id":"PF00191","name":"Annexin","start":109,"end":174},{"id":"PF00191","name":"Annexin","start":193,"end":259},{"id":"PF00191","name":"Annexin","start":269,"end":334}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MSTVHEILCKLSLEGDHSTPPSAYGSVKAYTNFDAERDALNIETAIKTKGVDEVTIVNILTNRSNAQRQDIAFAYQRRTKKELASALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVPKWISIMTERSVPHLQKVFDRYKSYSPYDMLESIRKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQQDTKGDYQKALLYLCGGDD","length":339,"regions":[{"region_id":"DP02735r001","ec_ontology":"ECO","end":33,"term_id":"IDPO:0000002","start":2,"version":2,"statement":[{"text":"Annexin A2 (ANXA2) has a versatile role in membrane-associated functions including membrane aggregation, endo- and exocytosis, and it is regulated by post-translational modifications and protein-protein interactions through the unstructured N-terminal domain (NTD).","type":"Abstract"},{"text":"Annexins consist of a disordered N-terminal domain (NTD, ANXA2 residues 2–33) (Figure 1A) followed by a conserved C-terminal core domain (CTD, ANXA2 residues 34–339) comprising four annexin repeats","type":"Introduction"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28669632","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5LQ0"},{"db":"PDB","id":"5LPX"},{"db":"PDB","id":"5LQ2"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Regulation of the Equilibrium between Closed and Open Conformations of Annexin A2 by N-Terminal Phosphorylation and S100A4-Binding. <i> Ecsédi P, Kiss B, Gógl G, Radnai L, Buday L, Koprivanacz K, Liliom K, Leveles I, Vértessy B, Jeszenői N, Hetényi C, Schlosser G, Katona G, Nyitray L. </i> Structure, 2017","validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-04-23T10:16:57.156Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":26,"region_id":"DP02735r002","start":22,"term_id":"IDPO:0000045","statement":[{"text":"Phosphorylation of Tyr24 anchors the NTD to the core and inhibits membrane aggregation","type":"Article"},{"text":"In contrast, pTyr24 anchors the NTD to the CTD and hampers the membrane-bridging function.","type":"Abstract"},{"text":"LUV aggregation induced by wild-type ANXA2, ANXA2DNTD, ANXA2S26E, and ANXA2S12E-S26E was similar, while the amplitude of the turbidity change caused by ANXA2pY24 was 11-fold smaller than that caused by native ANXA2","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"mass spectrometry evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28669632","version":3,"reference_html":"Regulation of the Equilibrium between Closed and Open Conformations of Annexin A2 by N-Terminal Phosphorylation and S100A4-Binding. <i> Ecsédi P, Kiss B, Gógl G, Radnai L, Buday L, Koprivanacz K, Liliom K, Leveles I, Vértessy B, Jeszenői N, Hetényi C, Schlosser G, Katona G, Nyitray L. </i> Structure, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001230","cross_refs":[{"db":"PDB","id":"5LQ0"},{"db":"PDB","id":"5LPX"},{"db":"PDB","id":"5LQ2"}],"term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-04-23T15:25:28.050Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"region_id":"DP02735r004","ec_ontology":"ECO","end":33,"term_id":"IDPO:0000011","start":2,"version":2,"statement":[{"text":"The unstructured N-terminal domain (NTD) is visible in complex with S100A4","type":"Curator statement"},{"text":"Furthermore, it was shown that S100A4 binding requires the entire NTD","type":"Results"}],"term_name":"disorder to order","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28669632","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5LPU"}],"term_namespace":"Structural transition","ec_id":"ECO:0005670","curator_id":"fquaglia","reference_html":"Regulation of the Equilibrium between Closed and Open Conformations of Annexin A2 by N-Terminal Phosphorylation and S100A4-Binding. <i> Ecsédi P, Kiss B, Gógl G, Radnai L, Buday L, Koprivanacz K, Liliom K, Leveles I, Vértessy B, Jeszenői N, Hetényi C, Schlosser G, Katona G, Nyitray L. </i> Structure, 2017","validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-04-23T10:16:59.204Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP02735r005","ec_ontology":"ECO","end":33,"term_id":"GO:0005515","start":2,"version":3,"statement":[{"text":"The unstructured N-terminal domain (NTD) is visible in complex with S100A4","type":"Curator statement"},{"text":"Furthermore, it was shown that S100A4 binding requires the entire NTD","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P26447","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","reference_html":"Regulation of the Equilibrium between Closed and Open Conformations of Annexin A2 by N-Terminal Phosphorylation and S100A4-Binding. <i> Ecsédi P, Kiss B, Gógl G, Radnai L, Buday L, Koprivanacz K, Liliom K, Leveles I, Vértessy B, Jeszenői N, Hetényi C, Schlosser G, Katona G, Nyitray L. </i> Structure, 2017","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"28669632","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5LPU"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"fquaglia","curator_orcid":"0000-0002-0341-4888","validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-04-23T10:17:12.385Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":15,"region_id":"DP02735r006","start":2,"term_id":"GO:0005515","statement":[{"text":"One of the most extensively characterized properties of ANXA2 is its interaction with S100A10 forming a heterotetrameric complex (calpactin I).","type":"Results"},{"text":"To evaluate quantitatively the interaction of S100A4 with ANXA2, we performed fluorescence polarization (FP) binding studies using Fl-ANXA22−15 and Fl-ANXA22−33 fragments, as well as full-length Fl-ANXA2 variants","type":"Results"},{"text":"As expected, S100A10 bound tightly to both NTD fragments, as well as all ANXA2 constructs, with a Kd of 10–40 nM","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"fluorescence polarization evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"28669632","version":4,"reference_html":"Regulation of the Equilibrium between Closed and Open Conformations of Annexin A2 by N-Terminal Phosphorylation and S100A4-Binding. <i> Ecsédi P, Kiss B, Gógl G, Radnai L, Buday L, Koprivanacz K, Liliom K, Leveles I, Vértessy B, Jeszenői N, Hetényi C, Schlosser G, Katona G, Nyitray L. </i> Structure, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006277","term_name":"protein binding","curator_orcid":"0000-0002-0341-4888","interaction_partner":[{"db":"UniProt","id":"P60903","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-04-23T15:29:28.246Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P26447","partner_end":null}],"ec_ontology":"ECO","end":33,"region_id":"DP02735r007","start":2,"term_id":"GO:0005515","statement":[{"text":"The results of the label-free isothermal titration calorimetry measurements confirmed that S100A4 binds to ANXA2 with moderate affinity (Kd ≈ 11 and 8 μM for the NTD and full-length ANXA2, respectively) and with a stoichiometry of one ANXA2 chain to an S100A4 dimer (Figures 3F and 3G).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"isothermal titration calorimetry evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"28669632","version":3,"reference_html":"Regulation of the Equilibrium between Closed and Open Conformations of Annexin A2 by N-Terminal Phosphorylation and S100A4-Binding. <i> Ecsédi P, Kiss B, Gógl G, Radnai L, Buday L, Koprivanacz K, Liliom K, Leveles I, Vértessy B, Jeszenői N, Hetényi C, Schlosser G, Katona G, Nyitray L. </i> Structure, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005647","term_name":"protein binding","validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-04-23T10:17:22.690Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":33,"region_id":"DP02735r008","start":2,"term_id":"GO:0098772","statement":[{"text":"We also studied the effect of S100 binding and/or protein phosphorylation on ANXA2-mediated liposome aggregation. We found that Tyr24 phosphorylation reduced the conformational fluctuation of the C-NTD and it hampers the ability of ANXA2 to aggregate phosphatidylserine-containing large unilamellar vesicles (LUVs).","type":"Introduction"},{"text":"Modulation of ANXA2-Mediated Liposome Aggregation by Protein Phosphorylation and S100 Binding","type":"Figure"},{"text":"Since we demonstrated that the pTyr24 side chain clamps the C-NTD to the CTD, a possible explanation for the tyrosine phosphorylation-mediated inhibition of LUV aggregation is that the concave side of ANXA2, which is supposedly responsible for ANXA2-ANXA2 interactions during membrane bridging, is masked by the C-NTD in the membrane-bound form as well (Figure 6B).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cell aggregation evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"28669632","version":3,"reference_html":"Regulation of the Equilibrium between Closed and Open Conformations of Annexin A2 by N-Terminal Phosphorylation and S100A4-Binding. <i> Ecsédi P, Kiss B, Gógl G, Radnai L, Buday L, Koprivanacz K, Liliom K, Leveles I, Vértessy B, Jeszenői N, Hetényi C, Schlosser G, Katona G, Nyitray L. </i> Structure, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006319","term_name":"molecular function regulator","validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-04-23T11:58:30.554Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":33,"region_id":"DP02735r009","start":2,"term_id":"GO:0098772","statement":[{"text":"C-NTD Phosphorylation Modulates ANXA2 Stability","type":"Results"},{"text":"Based on our crystal structures, MD simulations, and LP and DSF experiments we can conclude that the flexibility of the C-NTD and the stability of the CTD are clearly interrelated and oppositely regulated by Tyr24 phosphorylation and Ser26Glu phosphomimicking mutation.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"28669632","version":3,"reference_html":"Regulation of the Equilibrium between Closed and Open Conformations of Annexin A2 by N-Terminal Phosphorylation and S100A4-Binding. <i> Ecsédi P, Kiss B, Gógl G, Radnai L, Buday L, Koprivanacz K, Liliom K, Leveles I, Vértessy B, Jeszenői N, Hetényi C, Schlosser G, Katona G, Nyitray L. </i> Structure, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006317","term_name":"molecular function regulator","validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-04-23T11:58:28.931Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_12","ncbi_taxon_id":9606,"disprot_id":"DP02735","date":"2020-03-31T16:49:43.108Z","organism":"Homo sapiens","regions_counter":9,"name":"Annexin A2","dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000125B76","uniref100":"UniRef100_P07355","uniref90":"UniRef90_P07355","uniref50":"UniRef50_P07355","genes":[{"name":{"value":"ANXA2"},"synonyms":[{"value":"ANX2"},{"value":"ANX2L4"},{"value":"CAL1H"},{"value":"LPC2D"}]}],"alphafold_very_low_content":0.04129793510324484,"disorder_content":0.0943952802359882,"disprot_consensus":{"full":[{"start":2,"end":33,"type":"T"}],"Structural state":[{"start":2,"end":33,"type":"D"}],"Disorder function":[{"start":22,"end":26,"type":"F"}],"Structural transition":[{"start":2,"end":33,"type":"T"}],"Molecular function":[{"start":2,"end":33,"type":"F"}]}},{"acc":"Q04049","features":{"gene3D":[{"start":391,"end":513,"id":"G3DSA:3.30.1490.100","name":"DNA polymerase, Y-family, little finger domain"},{"start":2,"end":295,"id":"G3DSA:3.30.70.270","name":"G3DSA:3.30.70.270"}],"pfam":[{"id":"PF00817","name":"impB/mucB/samB family","start":29,"end":276},{"id":"PF11799","name":"impB/mucB/samB family C-terminal domain","start":393,"end":506}]},"creator":"fquaglia","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"sequence":"MSKFTWKELIQLGSPSKAYESSLACIAHIDMNAFFAQVEQMRCGLSKEDPVVCVQWNSIIAVSYAARKYGISRMDTIQEALKKCSNLIPIHTAVFKKGEDFWQYHDGCGSWVQDPAKQISVEDHKVSLEPYRRESRKALKIFKSACDLVERASIDEVFLDLGRICFNMLMFDNEYELTGDLKLKDALSNIREAFIGGNYDINSHLPLIPEKIKSLKFEGDVFNPEGRDLITDWDDVILALGSQVCKGIRDSIKDILGYTTSCGLSSTKNVCKLASNYKKPDAQTIVKNDCLLDFLDCGKFEITSFWTLGGVLGKELIDVLDLPHENSIKHIRETWPDNAGQLKEFLDAKVKQSDYDRSTSNIDPLKTADLAEKLFKLSRGRYGLPLSSRPVVKSMMSNKNLRGKSCNSIVDCISWLEVFCAELTSRIQDLEQEYNKIVIPRTVSISLKTKSYEVYRKSGPVAYKGINFQSHELLKVGIKFVTDLDIKGKNKSYYPLTKLSMTITNFDIIDLQKTVVDMFGNQVHTFKSSAGKEDEEKTTSSKADEKTPKLECCKYQVTFTDQKALQEHADYHLALKLSEGLNGAEESSKNLSFGEKRLLFSRKRPNSQHTATPQKKQVTSSKNILSFFTRKK","length":632,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":528,"region_id":"DP02736r001","start":510,"term_id":"IDPO:0000002","statement":[{"text":"There was no clear electron density beyond residue 509 indicating that this putative α helix does not have a unique position and is not part of the little finger sub-domain.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29385534","version":2,"reference_html":"The C-terminal region of translesion synthesis DNA polymerase η is partially unstructured and has high conformational flexibility. <i> Powers KT, Elcock AH, Washington MT. </i> Nucleic Acids Res, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5VTP"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":632,"region_id":"DP02736r002","start":510,"term_id":"IDPO:0000002","statement":[{"text":"Langevin dynamics simulations, and small-angle X-ray scattering-we show that the C-terminal region is partially unstructured and has high conformational flexibility.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29385534","version":2,"reference_html":"The C-terminal region of translesion synthesis DNA polymerase η is partially unstructured and has high conformational flexibility. <i> Powers KT, Elcock AH, Washington MT. </i> Nucleic Acids Res, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","cross_refs":[{"db":"PDB","id":"5VTP"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":632,"region_id":"DP02736r003","start":510,"term_id":"GO:0060090","statement":[{"text":"Langevin dynamics simulations, and small-angle X-ray scattering-we show that the C-terminal region is partially unstructured and has high conformational flexibility.","type":"Abstract"},{"text":"The C-terminal region mediates interactions with proliferating cell nuclear antigen (PCNA) and other translesion synthesis proteins such as Rev1. This region contains a ubiquitin-binding/zinc-binding (UBZ) motif and a PCNA-interacting protein (PIP) motif.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"29385534","version":3,"reference_html":"The C-terminal region of translesion synthesis DNA polymerase η is partially unstructured and has high conformational flexibility. <i> Powers KT, Elcock AH, Washington MT. </i> Nucleic Acids Res, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","cross_refs":[{"db":"PDB","id":"5VTP"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0002-0341-4888","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":559292,"disprot_id":"DP02736","date":"2020-03-31T17:42:38.259Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":3,"name":"DNA polymerase eta","dataset":[],"UniParc":"UPI000006B8F4","uniref100":"UniRef100_Q04049","uniref90":"UniRef90_Q04049","uniref50":"UniRef50_Q04049","genes":[{"name":{"value":"RAD30"},"synonyms":[{"value":"DBH1"}],"olnNames":[{"value":"YDR419W"}]}],"alphafold_very_low_content":0.1060126582278481,"disorder_content":0.19462025316455697,"disprot_consensus":{"full":[{"start":510,"end":632,"type":"D"}],"Structural state":[{"start":510,"end":632,"type":"D"}],"Molecular function":[{"start":510,"end":632,"type":"F"}]}},{"acc":"Q9NWW9","features":{"gene3D":[],"pfam":[{"id":"PF04970","name":"Lecithin retinol acyltransferase","start":7,"end":125}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MALARPRPRLGDLIEISRFGYAHWAIYVGDGYVVHLAPASEIAGAGAASVLSALTNKAIVKKELLSVVAGGDNYRVNNKHDDRYTPLPSNKIVKRAEELVGQELPYSLTSDNCEHFVNHLRYGVSRSDQVTGAVTTVGVAAGLLAAASLVGILLARSKRERQ","length":162,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":51,"region_id":"DP02737r001","start":40,"term_id":"IDPO:0000002","statement":[{"text":"A region that contributes to the HRASLS2 and HRASLS3 membrane interaction is the 40–57-amino acid segment between β3 and β4","type":"Results"},{"text":"This in turn suggested an amphiphilic helix with a hydrophobic interface mainly composed of Val-50, Met-51, and Leu-54 in HRASLS3 and Val-50, Leu-51, and Leu-54 in HRASLS2 that could interact with the nonpolar core of a bilayer","type":"Results"},{"text":"Thus, the reason for the disorder observed in this particular region could stem from the lack of a proper interfacial environment in the protein crystal, as lipid membrane interactions have been shown to stabilize amphiphilic helices","type":"Results"},{"text":"The authors suggest that interaction of this region with a lipid bilayer could promote its re-folding as documented for many other amphiphilic helices, although they don't test this hypothesis","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22605381","version":2,"reference_html":"Structural basis for the acyltransferase activity of lecithin:retinol acyltransferase-like proteins. <i> Golczak M, Kiser PD, Sears AE, Lodowski DT, Blaner WS, Palczewski K. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4DPZ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Biological process","ec_ontology":"ECO","end":51,"region_id":"DP02737r002","start":40,"term_id":"GO:0051179","statement":[{"text":"A region that contributes to the HRASLS2 and HRASLS3 membrane interaction is the 40–57-amino acid segment between β3 and β4","type":"Results"},{"text":"This in turn suggested an amphiphilic helix with a hydrophobic interface mainly composed of Val-50, Met-51, and Leu-54 in HRASLS3 and Val-50, Leu-51, and Leu-54 in HRASLS2 that could interact with the nonpolar core of a bilayer","type":"Results"},{"text":"Thus, the reason for the disorder observed in this particular region could stem from the lack of a proper interfacial environment in the protein crystal, as lipid membrane interactions have been shown to stabilize amphiphilic helices","type":"Results"},{"text":"The authors suggest that interaction of this region with a lipid bilayer could promote its re-folding as documented for many other amphiphilic helices, although they don't test this hypothesis","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"22605381","version":3,"reference_html":"Structural basis for the acyltransferase activity of lecithin:retinol acyltransferase-like proteins. <i> Golczak M, Kiser PD, Sears AE, Lodowski DT, Blaner WS, Palczewski K. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4DPZ"}],"term_name":"localization","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02737","date":"2020-04-06T08:52:58.057Z","organism":"Homo sapiens","regions_counter":2,"name":"Phospholipase A and acyltransferase 2","dataset":[],"UniParc":"UPI000012CBE3","uniref100":"UniRef100_Q9NWW9","uniref90":"UniRef90_Q9NWW9","uniref50":"UniRef50_Q9NWW9","genes":[{"name":{"value":"PLAAT2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:17824","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:17824"}}]},"synonyms":[{"value":"HRASLS2"}]}],"alphafold_very_low_content":0.22839506172839505,"disorder_content":0.07407407407407407,"disprot_consensus":{"full":[{"start":40,"end":51,"type":"D"}],"Structural state":[{"start":40,"end":51,"type":"D"}],"Biological process":[{"start":40,"end":51,"type":"F"}]}},{"acc":"P08581","features":{"gene3D":[{"start":657,"end":744,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":657,"end":744,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":42,"end":531,"id":"G3DSA:2.130.10.10","name":"YVTN repeat-like/Quinoprotein amine dehydrogenase"}],"pfam":[{"id":"PF01403","name":"Sema domain","start":317,"end":491},{"id":"PF01437","name":"Plexin repeat","start":520,"end":561},{"id":"PF01833","name":"IPT/TIG domain","start":563,"end":654},{"id":"PF01833","name":"IPT/TIG domain","start":657,"end":728},{"id":"PF01833","name":"IPT/TIG domain","start":742,"end":817},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":1078,"end":1336}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MKAPAVLAPGILVLLFTLVQRSNGECKEALAKSEMNVNMKYQLPNFTAETPIQNVILHEHHIFLGATNYIYVLNEEDLQKVAEYKTGPVLEHPDCFPCQDCSSKANLSGGVWKDNINMALVVDTYYDDQLISCGSVNRGTCQRHVFPHNHTADIQSEVHCIFSPQIEEPSQCPDCVVSALGAKVLSSVKDRFINFFVGNTINSSYFPDHPLHSISVRRLKETKDGFMFLTDQSYIDVLPEFRDSYPIKYVHAFESNNFIYFLTVQRETLDAQTFHTRIIRFCSINSGLHSYMEMPLECILTEKRKKRSTKKEVFNILQAAYVSKPGAQLARQIGASLNDDILFGVFAQSKPDSAEPMDRSAMCAFPIKYVNDFFNKIVNKNNVRCLQHFYGPNHEHCFNRTLLRNSSGCEARRDEYRTEFTTALQRVDLFMGQFSEVLLTSISTFIKGDLTIANLGTSEGRFMQVVVSRSGPSTPHVNFLLDSHPVSPEVIVEHTLNQNGYTLVITGKKITKIPLNGLGCRHFQSCSQCLSAPPFVQCGWCHDKCVRSEECLSGTWTQQICLPAIYKVFPNSAPLEGGTRLTICGWDFGFRRNNKFDLKKTRVLLGNESCTLTLSESTMNTLKCTVGPAMNKHFNMSIIISNGHGTTQYSTFSYVDPVITSISPKYGPMAGGTLLTLTGNYLNSGNSRHISIGGKTCTLKSVSNSILECYTPAQTISTEFAVKLKIDLANRETSIFSYREDPIVYEIHPTKSFISGGSTITGVGKNLNSVSVPRMVINVHEAGRNFTVACQHRSNSEIICCTTPSLQQLNLQLPLKTKAFFMLDGILSKYFDLIYVHNPVFKPFEKPVMISMGNENVLEIKGNDIDPEAVKGEVLKVGNKSCENIHLHSEAVLCTVPNDLLKLNSELNIEWKQAISSTVLGKVIVQPDQNFTGLIAGVVSISTALLLLLGFFLWLKKRKQIKDLGSELVRYDARVHTPHLDRLVSARSVSPTTEMVSNESVDYRATFPEDQFPNSSQNGSCRQVQYPLTDMSPILTSGDSDISSPLLQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDNDGKKIHCAVKSLNRITDIGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYLASKKFVHRDLAARNCMLDEKFTVKVADFGLARDMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFSELVSRISAIFSTFIGEHYVHVNATYVNVKCVAPYPSLLSSEDNADDEVDTRPASFWETS","length":1390,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1244,"region_id":"DP02738r001","start":1225,"term_id":"IDPO:0000002","statement":[{"text":"Electron density for the activation loop between the DFG motif and Leu-1245 is not visible in the structure, suggesting that residues 1225–1244 of the activation loop are disordered following phosphorylation.","type":"Results"},{"text":"The crystal structure of the unbound kinase domain phosphorylated at Tyr-1234 and Tyr-1235 shows that activation loop phosphorylation leads to the ejection and disorder of the activation loop and rearrangement of helix αC and the G loop to generate a viable active site.","type":"Abstract"},{"text":"Upon phosphorylation, the G loop adopts an extended conformation (blue) that requires ejection of the activation loop (gray) and reveals the ATP-binding site.","type":"Figure"}],"curator_id":"vnugnes","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"21247903","version":3,"reference_html":"Structural basis for selective small molecule kinase inhibition of activated c-Met. <i> Rickert KW, Patel SB, Allison TJ, Byrne NJ, Darke PL, Ford RE, Guerin DJ, Hall DL, Kornienko M, Lu J, Munshi SK, Reid JC, Shipman JM, Stanton EF, Wilson KJ, Young JR, Soisson SM, Lumb KJ. </i> J Biol Chem, 2011","date":"2022-06-16T19:43:40.348Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3Q6U"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1234,"end":1234,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1235,"end":1235,"position":"Specific residue"}],"sequence_construct":"MQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDNDGKKIHCAVKSLNRITDIGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYLASKKFVHRDLAARNCMLDEKFTVKVADFGLARDMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFSELVSRISAIFSTFIGEHHHHHHH"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":1239,"region_id":"DP02738r002","start":1225,"term_id":"IDPO:0000014","statement":[{"text":"The crystal structure of the unbound kinase domain phosphorylated at Tyr-1234 and Tyr-1235 shows that activation loop phosphorylation leads to the ejection and disorder of the activation loop and rearrangement of helix αC and the G loop to generate a viable active site.","type":"Abstract"},{"text":"Upon phosphorylation, the G loop adopts an extended conformation (blue) that requires ejection of the activation loop (gray) and reveals the ATP-binding site.","type":"Figure"},{"text":"One of the more striking differences observed between the unbound, phosphorylated c-Met structure and the structure observed in the presence of compound 1 is the nearly complete ordering of the activation loop, including the phosphate groups of Tyr(P)-1234 and Tyr(P)-1235 (Fig. 5). Only a short region of the activation loop remains disordered (residues 1240–1243). Upon loop stabilization, the phosphotyrosine residues form electrostatic interactions: Tyr(P)-1234 interacts with Lys-1232 and Lys-1253, and Tyr(P)-1235 interacts with Arg-1227 and His-1238","type":"Results"},{"text":"Upon phosphorylation and ejection of the activation loop, the G loop adopts a remarkably different conformation that involves a movement of 9–11 Å for the Cβ atoms of Arg-1086, His-1088, and Phe-1089 (Fig. 3A). The extended β-hairpin conformation of the G loop is incompatible with the presence of the activation loop in the unphosphorylated state. This structural transition removes the active site obstruction seen in the unphosphorylated structure by the G loop side chains of Arg-1086, His-1088, and His-1089 and thus relieves an autoinhibitory feature of the unphosphorylated kinase.","type":"Results"}],"curator_id":"vnugnes","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"21247903","version":3,"reference_html":"Structural basis for selective small molecule kinase inhibition of activated c-Met. <i> Rickert KW, Patel SB, Allison TJ, Byrne NJ, Darke PL, Ford RE, Guerin DJ, Hall DL, Kornienko M, Lu J, Munshi SK, Reid JC, Shipman JM, Stanton EF, Wilson KJ, Young JR, Soisson SM, Lumb KJ. </i> J Biol Chem, 2011","date":"2022-06-16T19:45:24.698Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3Q6U"},{"db":"PDB","id":"3Q6W"},{"db":"PDB","id":"3R7O"}],"term_name":"order to disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural transition","construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1324,"end":1324,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":135,"end":135,"position":"Specific residue"}],"sequence_construct":"MQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDNDGKKIHCAVKSLNRITDIGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYLASKKFVHRDLAARNCMLDEKFTVKVADFGLARDMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFSELVSRISAIFSTFIGEHHHHHHH"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":1244,"region_id":"DP02738r003","start":1225,"term_id":"IDPO:0000045","statement":[{"text":"The crystal structure of the unbound kinase domain phosphorylated at Tyr-1234 and Tyr-1235 shows that activation loop phosphorylation leads to the ejection and disorder of the activation loop and rearrangement of helix αC and the G loop to generate a viable active site.","type":"Abstract"},{"text":"Upon phosphorylation, the G loop adopts an extended conformation (blue) that requires ejection of the activation loop (gray) and reveals the ATP-binding site.","type":"Figure"},{"text":"One of the more striking differences observed between the unbound, phosphorylated c-Met structure and the structure observed in the presence of compound 1 is the nearly complete ordering of the activation loop, including the phosphate groups of Tyr(P)-1234 and Tyr(P)-1235 (Fig. 5). Only a short region of the activation loop remains disordered (residues 1240–1243). Upon loop stabilization, the phosphotyrosine residues form electrostatic interactions: Tyr(P)-1234 interacts with Lys-1232 and Lys-1253, and Tyr(P)-1235 interacts with Arg-1227 and His-1238","type":"Results"},{"text":"Upon phosphorylation and ejection of the activation loop, the G loop adopts a remarkably different conformation that involves a movement of 9–11 Å for the Cβ atoms of Arg-1086, His-1088, and Phe-1089 (Fig. 3A). The extended β-hairpin conformation of the G loop is incompatible with the presence of the activation loop in the unphosphorylated state. This structural transition removes the active site obstruction seen in the unphosphorylated structure by the G loop side chains of Arg-1086, His-1088, and His-1089 and thus relieves an autoinhibitory feature of the unphosphorylated kinase.","type":"Results"}],"curator_id":"vnugnes","released":"2022_06","ec_name":"enzymatic activity assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"21247903","version":3,"reference_html":"Structural basis for selective small molecule kinase inhibition of activated c-Met. <i> Rickert KW, Patel SB, Allison TJ, Byrne NJ, Darke PL, Ford RE, Guerin DJ, Hall DL, Kornienko M, Lu J, Munshi SK, Reid JC, Shipman JM, Stanton EF, Wilson KJ, Young JR, Soisson SM, Lumb KJ. </i> J Biol Chem, 2011","date":"2022-06-16T19:47:20.878Z","reference_source":"pmid","ec_id":"ECO:0005801","cross_refs":[{"db":"PDB","id":"3Q6U"},{"db":"PDB","id":"3Q6W"},{"db":"PDB","id":"3R7O"}],"term_name":"phosphorylation display site","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","disprot_namespace":"Disorder function","construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1234,"end":1234,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1235,"end":1235,"position":"Specific residue"}],"sequence_construct":"MQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDNDGKKIHCAVKSLNRITDIGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYLASKKFVHRDLAARNCMLDEKFTVKVADFGLARDMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFSELVSRISAIFSTFIGEHHHHHHH"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1244,"region_id":"DP02738r004","start":1225,"term_id":"GO:0140677","statement":[{"text":"The crystal structure of the unbound kinase domain phosphorylated at Tyr-1234 and Tyr-1235 shows that activation loop phosphorylation leads to the ejection and disorder of the activation loop and rearrangement of helix αC and the G loop to generate a viable active site.","type":"Abstract"},{"text":"Upon phosphorylation, the G loop adopts an extended conformation (blue) that requires ejection of the activation loop (gray) and reveals the ATP-binding site.","type":"Figure"},{"text":"One of the more striking differences observed between the unbound, phosphorylated c-Met structure and the structure observed in the presence of compound 1 is the nearly complete ordering of the activation loop, including the phosphate groups of Tyr(P)-1234 and Tyr(P)-1235 (Fig. 5). Only a short region of the activation loop remains disordered (residues 1240–1243). Upon loop stabilization, the phosphotyrosine residues form electrostatic interactions: Tyr(P)-1234 interacts with Lys-1232 and Lys-1253, and Tyr(P)-1235 interacts with Arg-1227 and His-1238","type":"Results"},{"text":"Upon phosphorylation and ejection of the activation loop, the G loop adopts a remarkably different conformation that involves a movement of 9–11 Å for the Cβ atoms of Arg-1086, His-1088, and Phe-1089 (Fig. 3A). The extended β-hairpin conformation of the G loop is incompatible with the presence of the activation loop in the unphosphorylated state. This structural transition removes the active site obstruction seen in the unphosphorylated structure by the G loop side chains of Arg-1086, His-1088, and His-1089 and thus relieves an autoinhibitory feature of the unphosphorylated kinase.","type":"Results"}],"curator_id":"vnugnes","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"21247903","version":4,"reference_html":"Structural basis for selective small molecule kinase inhibition of activated c-Met. <i> Rickert KW, Patel SB, Allison TJ, Byrne NJ, Darke PL, Ford RE, Guerin DJ, Hall DL, Kornienko M, Lu J, Munshi SK, Reid JC, Shipman JM, Stanton EF, Wilson KJ, Young JR, Soisson SM, Lumb KJ. </i> J Biol Chem, 2011","date":"2022-06-16T19:46:49.384Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3Q6U"},{"db":"PDB","id":"3Q6W"},{"db":"PDB","id":"3R7O"}],"term_name":"molecular function activator activity","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1234,"end":1234,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":1235,"end":1235,"position":"Specific residue"}],"sequence_construct":"MQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDNDGKKIHCAVKSLNRITDIGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFIRNETHNPTVKDLIGFGLQVAKGMKYLASKKFVHRDLAARNCMLDEKFTVKVADFGLARDMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFSELVSRISAIFSTFIGEHHHHHHH"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02738","date":"2020-04-06T09:51:31.068Z","organism":"Homo sapiens","regions_counter":4,"name":"Hepatocyte growth factor receptor","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI000016AD2F","uniref100":"UniRef100_P08581","uniref90":"UniRef90_P08581","uniref50":"UniRef50_P08581","genes":[{"name":{"value":"MET"}}],"alphafold_very_low_content":0.1316546762589928,"disorder_content":0.014388489208633094,"disprot_consensus":{"full":[{"start":1225,"end":1239,"type":"T"},{"start":1240,"end":1244,"type":"D"}],"Structural state":[{"start":1225,"end":1244,"type":"D"}],"Structural transition":[{"start":1225,"end":1239,"type":"T"}],"Disorder function":[{"start":1225,"end":1244,"type":"F"}],"Molecular function":[{"start":1225,"end":1244,"type":"F"}]}},{"acc":"P45352","features":{"gene3D":[{"start":20,"end":307,"id":"G3DSA:3.30.572.10","name":"Thymidylate synthase/dCMP hydroxymethylase domain"}],"pfam":[{"id":"PF00303","name":"Thymidylate synthase","start":26,"end":307}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"sequence":"MLVEGSELQSGAQQPRTEAPQHGELQYLRQVEHIMRCGFKKEDRTGTGTLSVFGMQARYSLRDEFPLLTTKRVFWKGVLEELLWFIKGSTNAKELSSKGVRIWDANGSRDFLDSLGFSARQEGDLGPVYGFQWRHFGADYKDMDSDYSGQGVDQLQKVIDTIKTNPDDRRIIMCAWNPKDLPLMALPPCHALCQFYVVNGELSCQLYQRSGDMGLGVPFNIASYALLTYMIAHITGLQPGDFVHTLGDAHIYLNHIEPLKIQLQREPRPFPKLRILRKVETIDDFKVEDFQIEGYNPHPTIKMEMAV","length":307,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":20,"region_id":"DP02739r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"Two insertions in the rat protein are clearly seen, but the N-termini (residues 1−20) and C-termini (residues 301−307) are disordered in both crystal forms.","type":"Abstract"},{"text":"Both the N- and C-termini were disordered in the first rTS structure, and residues r1−r20 and r301−r307 were therefore left out of the final model.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9894005","version":2,"reference_html":"Crystal structures of rat thymidylate synthase inhibited by Tomudex, a potent anticancer drug. <i> Sotelo-Mundo RR, Ciesla J, Dzik JM, Rode W, Maley F, Maley GF, Hardy LW, Montfort WR. </i> Biochemistry, 1999","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1RTS"},{"db":"PDB","id":"2TSR"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","ncbi_taxon_id":10116,"disprot_id":"DP02739","date":"2020-04-06T16:43:21.296Z","organism":"Rattus norvegicus","regions_counter":1,"name":"Thymidylate synthase","dataset":[],"UniParc":"UPI0000112C76","uniref100":"UniRef100_P45352","uniref90":"UniRef90_P04818-2","uniref50":"UniRef50_P04818-2","genes":[{"name":{"value":"Tyms"}}],"alphafold_very_low_content":0.029315960912052116,"disorder_content":0.06514657980456026,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"D"}],"Structural state":[{"start":1,"end":20,"type":"D"}]}},{"acc":"P08179","features":{"gene3D":[],"pfam":[{"id":"PF00551","name":"Formyl transferase","start":1,"end":181}]},"creator":"fquaglia","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"sequence":"MNIVVLISGNGSNLQAIIDACKTNKIKGTVRAVFSNKADAFGLERARQAGIATHTLIASAFDSREAYDRELIHEIDMYAPDVVVLAGFMRILSPAFVSHYAGRLLNIHPSLLPKYPGLHTHRQALENGDEEHGTSVHFVTDELDGGPVILQAKVPVFAGDSEDDITARVQTQEHAIYPLVISWFADGRLKMHENAAWLDGQRLPPQGYAADE","length":212,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":132,"region_id":"DP02740r001","start":110,"term_id":"IDPO:0000002","statement":[{"text":"The structure is a modified doubly wound alpha/beta sheet with flexibility in the active site, including a disordered loop in the apo structure, which is ordered in the ternary complex structure.","type":"Abstract"},{"text":"The apo models include all protein atoms for residues 1-109 and 133-212, whereas the ternary model includes residues 1-209.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"1631098","version":2,"reference_html":"Structures of apo and complexed Escherichia coli glycinamide ribonucleotide transformylase. <i> Almassy RJ, Janson CA, Kan CC, Hostomska Z. </i> Proc Natl Acad Sci U S A, 1992","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1CDD"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":132,"region_id":"DP02740r002","start":110,"term_id":"IDPO:0000011","statement":[{"text":"The structure is a modified doubly wound alpha/beta sheet with flexibility in the active site, including a disordered loop in the apo structure, which is ordered in the ternary complex structure.","type":"Abstract"},{"text":"The apo models include all protein atoms for residues 1-109 and 133-212, whereas the ternary model includes residues 1-209.","type":"Methods"},{"text":"The disordered loop at position 110-132 in the apo structure (PDB:1CDD) becomes ordered in the ternary complex structure with the substrate glycinamide ribonucleotide and a folate inhibitor (PDB:1CDE)","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"1631098","version":2,"reference_html":"Structures of apo and complexed Escherichia coli glycinamide ribonucleotide transformylase. <i> Almassy RJ, Janson CA, Kan CC, Hostomska Z. </i> Proc Natl Acad Sci U S A, 1992","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1CDD"},{"db":"PDB","id":"1CDE"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2021_06","ncbi_taxon_id":83333,"disprot_id":"DP02740","date":"2020-04-07T13:27:08.830Z","organism":"Escherichia coli (strain K12)","regions_counter":2,"name":"Phosphoribosylglycinamide formyltransferase","dataset":[],"UniParc":"UPI0000110B1A","uniref100":"UniRef100_P08179","uniref90":"UniRef90_P08179","uniref50":"UniRef50_P08179","genes":[{"name":{"value":"purN","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01930","url":"https://hamap.expasy.org/unirule/MF_01930"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"3301838","url":"http://www.ncbi.nlm.nih.gov/pubmed/3301838","alternativeUrl":"https://europepmc.org/abstract/MED/3301838"}}]},"olnNames":[{"value":"b2500"},{"value":"JW2485"}]}],"alphafold_very_low_content":0.0047169811320754715,"disorder_content":0.10849056603773585,"disprot_consensus":{"full":[{"start":110,"end":132,"type":"T"}],"Structural state":[{"start":110,"end":132,"type":"D"}],"Structural transition":[{"start":110,"end":132,"type":"T"}]}},{"acc":"P09951","features":{"gene3D":[{"start":248,"end":307,"id":"G3DSA:3.30.1490.20","name":"ATP-grasp fold, A domain"}],"pfam":[{"id":"PF02078","name":"Synapsin pre-ATP-grasp domain","start":113,"end":212},{"id":"PF02750","name":"Synapsin, ATP binding domain","start":214,"end":416},{"id":"PF10581","name":"Synapsin N-terminal domain","start":1,"end":25}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"sequence":"MNYLRRRLSDSNFMANLPNGYMTDLQRPQPPPPPPSAASPGATPGSAAASAERASTAAPVASPAAPSPGSSGGGGFFSSLSNAVKQTTAAAAATFSEQVGGGSGGAGRGGAAARVLLVIDEPHTDWAKYFKGKKIHGEIDIKVEQAEFSDLNLVAHANGGFSVDMEVLRNGVKVVRSLKPDFVLIRQHAFSMARNGDYRSLVIGLQYAGIPSVNSLHSVYNFCDKPWVFAQMVRLHKKLGTEEFPLIDQTFYPNHKEMLSSTTYPVVVKMGHAHSGMGKVKVDNQHDFQDIASVVALTKTYATAEPFIDAKYDVRVQKIGQNYKAYMRTSVSGNWKTNTGSAMLEQIAMSDRYKLWVDTCSEIFGGLDICAVEALHGKDGRDHIIEVVGSSMPLIGDHQDEDKQLIVELVVNKMTQALPRQRDASPGRGSHSQTPSPGALPLGRQTSQQPAGPPAQQRPPPQGGPPQPGPGPQRQGPPLQQRPPPQGQQHLSGLGPPAGSPLPQRLPSPTAAPQQSASQATPMTQGQGRQSRPVAGGPGAPPAARPPASPSPQRQAGPPQATRQASISGPAPPKVSGASPGGQQRQGPPQKPPGPAGPIRQASQAGPGPRTGPPTTQQPRPSGPGPAGRPTKPQLAQKPSQDVPPPIIAAAGGPPHPQLNKSQSLTNAFNLPEPAPPRPSLSQDEVKAETIRSLRKSFASLFSD","length":704,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":111,"region_id":"DP02741r001","start":2,"term_id":"IDPO:0000002","statement":[{"text":"The evidence supports a view of synapsin I as an ATP-utilizing, tetrameric protein made up of monomers that have a flexible, extended N terminus.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14688264","version":2,"reference_html":"Tetramerization and ATP binding by a protein comprising the A, B, and C domains of rat synapsin I. <i> Brautigam CA, Chelliah Y, Deisenhofer J. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1PX2"},{"db":"PDB","id":"1PK8"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":11,"region_id":"DP02741r002","start":7,"term_id":"IDPO:0000045","statement":[{"text":"Only two domains are conserved in all synapsins: a short N-terminal A domain with a single phosphorylation site for cAMP-dependent protein kinase (PKA) and CaM Kinase I, and a large central C domain that binds ATP and may be enzymatic. We now demonstrate that synapsin phosphorylation in the A domain, at the only phosphorylation site shared by all synapsins, dissociates synapsins from synaptic vesicles. Furthermore, we show that the A domain binds phospholipids and is inhibited by phosphorylation. Our results suggest a novel mechanism by which proteins reversibly bind to membranes using a phosphorylation-dependent phospholipid-binding domain. The dynamic association of synapsins with synaptic vesicles correlates with their role in activity-dependent plasticity.","type":"Abstract"},{"text":"The phosphorylated site corresponds to Ser9 of Synaptin I.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10571231","version":2,"reference_html":"A phospho-switch controls the dynamic association of synapsins with synaptic vesicles. <i> Hosaka M, Hammer RE, Südhof TC. </i> Neuron, 1999","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007689","term_name":"phosphorylation display site","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-14T11:16:29.020Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":58,"region_id":"DP02741r004","start":53,"term_id":"IDPO:0000041","statement":[{"text":"Here, we identified seven in vivo O-GlcNAcylation sites on synapsin I by analysis of HPLC-purified digests of rat brain synapsin I. The seven O-GlcNAcylation sites (Ser55, Thr56, Thr87, Ser516, Thr524, Thr562, and Ser576) in synapsin I are clustered around its five phosphorylation sites in domains B and D.","type":"Abstract"},{"text":"The glycosylated sites correspond to Ser55 and Thr56.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"chromatography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10386995","version":2,"reference_html":"Glycosylation sites flank phosphorylation sites on synapsin I: O-linked N-acetylglucosamine residues are localized within domains mediating synapsin I interactions. <i> Cole RN, Hart GW. </i> J Neurochem, 1999","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","term_name":"glycosylation display site","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-14T10:52:37.418Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":89,"region_id":"DP02741r005","start":85,"term_id":"IDPO:0000041","statement":[{"text":"Here, we identified seven in vivo O-GlcNAcylation sites on synapsin I by analysis of HPLC-purified digests of rat brain synapsin I. The seven O-GlcNAcylation sites (Ser55, Thr56, Thr87, Ser516, Thr524, Thr562, and Ser576) in synapsin I are clustered around its five phosphorylation sites in domains B and D.","type":"Abstract"},{"text":"The glycosylated site correspond to Thr87.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"chromatography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10386995","version":2,"reference_html":"Glycosylation sites flank phosphorylation sites on synapsin I: O-linked N-acetylglucosamine residues are localized within domains mediating synapsin I interactions. <i> Cole RN, Hart GW. </i> J Neurochem, 1999","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","term_name":"glycosylation display site","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-14T10:52:36.635Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":10116,"disprot_id":"DP02741","date":"2020-04-07T17:23:44.475Z","organism":"Rattus norvegicus","regions_counter":5,"name":"Synapsin-1","dataset":[],"UniParc":"UPI000004368E","uniref100":"UniRef100_P09951","uniref90":"UniRef90_O88935","uniref50":"UniRef50_O88935","genes":[{"name":{"value":"Syn1"}}],"alphafold_very_low_content":0.42329545454545453,"disorder_content":0.15625,"disprot_consensus":{"full":[{"start":2,"end":111,"type":"D"}],"Structural state":[{"start":2,"end":111,"type":"D"}],"Disorder function":[{"start":7,"end":11,"type":"F"},{"start":53,"end":58,"type":"F"},{"start":85,"end":89,"type":"F"}]}},{"acc":"P06756","features":{"gene3D":[{"start":31,"end":468,"id":"G3DSA:2.130.10.130","name":"Integrin alpha, N-terminal"}],"pfam":[{"id":"PF00357","name":"Integrin alpha cytoplasmic region","start":1017,"end":1031},{"id":"PF01839","name":"FG-GAP repeat","start":253,"end":286},{"id":"PF01839","name":"FG-GAP repeat","start":306,"end":347},{"id":"PF01839","name":"FG-GAP repeat","start":370,"end":406},{"id":"PF08441","name":"Integrin alpha Ig-like domain 1","start":467,"end":625},{"id":"PF20805","name":"Integrin alpha Ig-like domain 2","start":626,"end":764},{"id":"PF20806","name":"Integrin alpha Ig-like domain 3","start":772,"end":983}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MAFPPRRRLRLGPRGLPLLLSGLLLPLCRAFNLDVDSPAEYSGPEGSYFGFAVDFFVPSASSRMFLLVGAPKANTTQPGIVEGGQVLKCDWSSTRRCQPIEFDATGNRDYAKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSQDIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQGQLISDQVAEIVSKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIDDFVSGVPRAARTLGMVYIYDGKNMSSLYNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQRASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGIVYIFNGRSTGLNAVPSQILEGQWAARSMPPSFGYSMKGATDIDKNGYPDLIVGAFGVDRAILYRARPVITVNAGLEVYPSILNQDNKTCSLPGTALKVSCFNVRFCLKADGKGVLPRKLNFQVELLLDKLKQKGAIRRALFLYSRSPSHSKNMTISRGGLMQCEELIAYLRDESEFRDKLTPITIFMEYRLDYRTAADTTGLQPILNQFTPANISRQAHILLDCGEDNVCKPKLEVSVDSDQKKIYIGDDNPLTLIVKAQNQGEGAYEAELIVSIPLQADFIGVVRNNEALARLSCAFKTENQTRQVVCDLGNPMKAGTQLLAGLRFSVHQQSEMDTSVKFDLQIQSSNLFDKVSPVVSHKVDLAVLAAVEIRGVSSPDHVFLPIPNWEHKENPETEEDVGPVVQHIYELRNNGPSSFSKAMLHLQWPYKYNNNTLLYILHYDIDGPMNCTSDMEINPLRIKISSLQTTEKNDTVAGQGERDHLITKRDLALSEGDIHTLGCGVAQCLKIVCQVGRLDRGKSAILYVKSLLWTETFMNKENQNHSYSLKSSASFNVIEFPYKNLPIEDITNSTLVTTNVTWGIQPAPMPVPVWVIILAVLAGLLLLAVLVFVMYRMGFFKRVRPPQEEQEREQLQPHENGEGNSET","length":1048,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":897,"region_id":"DP02742r001","start":868,"term_id":"IDPO:0000002","statement":[{"text":"No electron density was observed for TM residues and much of the α(V) linker. α(V)β(3)-AB and α(V)β(3)-1TM demonstrate flexibility in the linker between their extracellular and TM domains, rather than the previously proposed rigid linkage.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23106217","version":3,"reference_html":"α(V)β(3) integrin crystal structures and their functional implications. <i> Dong X, Mi LZ, Zhu J, Wang W, Hu P, Luo BH, Springer TA. </i> Biochemistry, 2012","date":"2022-06-27T16:31:00.192Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4G1M"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T16:33:39.233Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":897,"region_id":"DP02742r002","start":868,"term_id":"IDPO:0000033","statement":[{"text":"No electron density was observed for TM residues and much of the α(V) linker. α(V)β(3)-AB and α(V)β(3)-1TM demonstrate flexibility in the linker between their extracellular and TM domains, rather than the previously proposed rigid linkage.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23106217","version":4,"reference_html":"α(V)β(3) integrin crystal structures and their functional implications. <i> Dong X, Mi LZ, Zhu J, Wang W, Hu P, Luo BH, Springer TA. </i> Biochemistry, 2012","date":"2022-06-27T16:33:20.001Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4G1M"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T16:33:36.408Z"}}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02742","date":"2020-04-07T18:18:20.167Z","organism":"Homo sapiens","regions_counter":2,"name":"Integrin alpha-V","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI000013D12E","uniref100":"UniRef100_P06756","uniref90":"UniRef90_P06756","uniref50":"UniRef50_P06756","genes":[{"name":{"value":"ITGAV","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6150","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6150"}}]},"synonyms":[{"value":"MSK8","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6150","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6150"}}]},{"value":"VNRA","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6150","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6150"}}]},{"value":"VTNR","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6150","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6150"}}]}]}],"alphafold_very_low_content":0.07633587786259542,"disorder_content":0.02862595419847328,"disprot_consensus":{"full":[{"start":868,"end":897,"type":"D"}],"Structural state":[{"start":868,"end":897,"type":"D"}],"Disorder function":[{"start":868,"end":897,"type":"F"}]}},{"acc":"P97675","features":{"gene3D":[{"start":148,"end":868,"id":"G3DSA:3.40.720.10","name":"Alkaline Phosphatase, subunit A"}],"pfam":[{"id":"PF01033","name":"Somatomedin B domain","start":54,"end":92},{"id":"PF01033","name":"Somatomedin B domain","start":97,"end":137},{"id":"PF01663","name":"Type I phosphodiesterase / nucleotide pyrophosphatase","start":162,"end":486}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"sequence":"MDSRLALATEEPIKKDSLKRYKILCAVLLALLVIVSLGLGLGLGLRKPEEHIGSCRKKCFDSSHRGLEGCRCDSGCTDRGDCCWDFEDTCVKSTQIWTCNSFRCGETRLEAALCSCADDCLQRKDCCTDYKAVCQGEVPWVTEACASSQEPQCPEGFDQPPVILFSMDGFRAEYLQTWSTLLPNINKLKTCGLHSKYMRAMYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVYLNKNFSLSSVEKSNPAWWSGQPIWLTAMYQGLKAASYYWPGSDVAVNGSFPNIYRNYSNSVPYESRIATLLQWLDLPKAERPSFYTIYVEEPDSAGHKSGPVSAGVIKALQLVDDAFGMLMEGLKQRNLHNCVNIIVLADHGMDQTSCDRVEYMTDYFPEINFYMYQGPAPRIRTRNIPQDFFTFNSEEIVRDLSCRKSDQHFKPYLTPDLPKRLHYAKNVRIDKVHLMVDRQWLAYRNKGSSNCEGGTHGYNNEFKSMEAIFLAHGPSFKEKTVIEPFENIEVYNLLCDLLHIQPAPNNGSHGSLNHLLKAPFYQPSHAEELSKSAGCGFTTPLPKDSLNCSCLALQTSGQEEQVNQRLNLSGGEVSATEKTNLPFGRPRVIQKNKDHCLLYHREYVSGFGKAMKMPMWSSYTVPKPGDTSSLPPTVPDCLRADVRVDPSESQKCSFYLADQNIDHGFLYPPAIKGNNESQYDALITSNLVPMYKEFKKMWDYFHKVLLIKYAIERNGVNVVSGPIFDYNYDGHFDAPDEITNYVAGTDVPVPTHYFVVLTSCKNKTHTPDSCPGWLDVLPFVVPHRPTNVESCPENKAEDLWVEERFKAHIARVRDVELLTGLDFYQEKTQPVSEILQLKTYLPTFETII","length":875,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":336,"region_id":"DP02743r001","start":324,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Its structure at 2.77 Å resolution reveals that the active-site zinc ions are missing and a large part of the active site and the surrounding residues are flexible.","type":"Abstract"},{"text":"However, owing to significant disorder and the low resolution of the data, model building and refinement of the NPP 349–875 structure reported here was only possible using the superimposed PDE and nuclease domains of the refined NPP3 140–875 structure as a starting point.","type":"Methods"},{"text":"In all four chains of the NPP 349–875 structure the following regions of the PDE domain have no density owing to flexibility: 168–181, 324–336 and 473–492 (Fig. 2b).","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30387774","version":2,"reference_html":"Crystallization of ectonucleotide phosphodiesterase/pyrophosphatase-3 and orientation of the SMB domains in the full-length ectodomain. <i> Döhler C, Zebisch M, Krinke D, Robitzki A, Sträter N. </i> Acta Crystallogr F Struct Biol Commun, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6G4G"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":492,"region_id":"DP02743r002","start":473,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Its structure at 2.77 Å resolution reveals that the active-site zinc ions are missing and a large part of the active site and the surrounding residues are flexible.","type":"Abstract"},{"text":"However, owing to significant disorder and the low resolution of the data, model building and refinement of the NPP 349–875 structure reported here was only possible using the superimposed PDE and nuclease domains of the refined NPP3 140–875 structure as a starting point.","type":"Methods"},{"text":"In all four chains of the NPP 349–875 structure the following regions of the PDE domain have no density owing to flexibility: 168–181, 324–336 and 473–492 (Fig. 2b).","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30387774","version":2,"reference_html":"Crystallization of ectonucleotide phosphodiesterase/pyrophosphatase-3 and orientation of the SMB domains in the full-length ectodomain. <i> Döhler C, Zebisch M, Krinke D, Robitzki A, Sträter N. </i> Acta Crystallogr F Struct Biol Commun, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6G4G"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2023_12","ncbi_taxon_id":10116,"disprot_id":"DP02743","date":"2020-04-07T22:04:55.767Z","organism":"Rattus norvegicus","regions_counter":2,"name":"Ectonucleotide pyrophosphatase/phosphodiesterase family member 3","dataset":[],"UniParc":"UPI0000167A5C","uniref100":"UniRef100_P97675","uniref90":"UniRef90_P97675","uniref50":"UniRef50_O14638","genes":[{"name":{"value":"Enpp3"},"synonyms":[{"value":"Pdnp3"}]}],"alphafold_very_low_content":0.022857142857142857,"disorder_content":0.037714285714285714,"disprot_consensus":{"full":[{"start":324,"end":336,"type":"D"},{"start":473,"end":492,"type":"D"}],"Structural state":[{"start":324,"end":336,"type":"D"},{"start":473,"end":492,"type":"D"}]}},{"acc":"Q92574","features":{"gene3D":[],"pfam":[{"id":"PF04388","name":"Hamartin, N-terminal domain","start":7,"end":275},{"id":"PF30391","name":"TSC1, coiled-coil","start":347,"end":719}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MAQQANVGELLAMLDSPMLGVRDDVTAVFKENLNSDRGPMLVNTLVDYYLETSSQPALHILTTLQEPHDKHLLDRINEYVGKAATRLSILSLLGHVIRLQPSWKHKLSQAPLLPSLLKCLKMDTDVVVLTTGVLVLITMLPMIPQSGKQHLLDFFDIFGRLSSWCLKKPGHVAEVYLVHLHASVYALFHRLYGMYPCNFVSFLRSHYSMKENLETFEEVVKPMMEHVRIHPELVTGSKDHELDPRRWKRLETHDVVIECAKISLDPTEASYEDGYSVSHQISARFPHRSADVTTSPYADTQNSYGCATSTPYSTSRLMLLNMPGQLPQTLSSPSTRLITEPPQATLWSPSMVCGMTTPPTSPGNVPPDLSHPYSKVFGTTAGGKGTPLGTPATSPPPAPLCHSDDYVHISLPQATVTPPRKEERMDSARPCLHRQHHLLNDRGSEEPPGSKGSVTLSDLPGFLGDLASEEDSIEKDKEEAAISRELSEITTAEAEPVVPRGGFDSPFYRDSLPGSQRKTHSAASSSQGASVNPEPLHSSLDKLGPDTPKQAFTPIDLPCGSADESPAGDRECQTSLETSIFTPSPCKIPPPTRVGFGSGQPPPYDHLFEVALPKTAHHFVIRKTEELLKKAKGNTEEDGVPSTSPMEVLDRLIQQGADAHSKELNKLPLPSKSVDWTHFGGSPPSDEIRTLRDQLLLLHNQLLYERFKRQQHALRNRRLLRKVIKAAALEEHNAAMKDQLKLQEKDIQMWKVSLQKEQARYNQLQEQRDTMVTKLHSQIRQLQHDREEFYNQSQELQTKLEDCRNMIAELRIELKKANNKVCHTELLLSQVSQKLSNSESVQQQMEFLNRQLLVLGEVNELYLEQLQNKHSDTTKEVEMMKAAYRKELEKNRSHVLQQTQRLDTSQKRILELESHLAKKDHLLLEQKKYLEDVKLQARGQLQAAESRYEAQKRITQVFELEILDLYGRLEKDGLLKKLEEEKAEAAEAAEERLDCCNDGCSDSMVGHNEEASGHNGETKTPRPSSARGSSGSRGGGGSSSSSSELSTPEKPPHQRAGPFSSRWETTMGEASASIPTTVGSLPSSKSFLGMKARELFRNKSESQCDEDGMTSSLSESLKTELGKDLGVEAKIPLNLDGPHPSPPTPDSVGQLHIMDYNETHHEHS","length":1164,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":992,"region_id":"DP02744r001","start":978,"term_id":"IDPO:0000002","statement":[{"text":"The first 39 residues of each TSC1 helix (residues 939–977) formed a single helix, whereas the last 15 residues were not visible in our electron density map.","type":"Results"}],"curator_id":"vnugnes","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"26893383","version":3,"reference_html":"Structural Basis of the Interaction between Tuberous Sclerosis Complex 1 (TSC1) and Tre2-Bub2-Cdc16 Domain Family Member 7 (TBC1D7). <i> Qin J, Wang Z, Hoogeveen-Westerveld M, Shen G, Gong W, Nellist M, Xu W. </i> J Biol Chem, 2016","date":"2022-06-16T19:57:04.358Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5EJC"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9P0N9"}]},{"region_id":"DP02744r002","ec_ontology":"ECO","end":992,"term_id":"GO:0005515","start":939,"version":3,"statement":[{"text":"To reveal how TBC1D7 interacts with TSC1, we determined the crystal structure of the TSC1 TBC1D7-binding domain (residues 939–992) in complex with near full-length TBC1D7(19–293), using the Se-Met single wavelength anomalous dispersion method","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9P0N9","partner_end":null}],"term_name":"protein binding","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"26893383","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5EJC"}],"term_namespace":"Molecular function","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structural Basis of the Interaction between Tuberous Sclerosis Complex 1 (TSC1) and Tre2-Bub2-Cdc16 Domain Family Member 7 (TBC1D7). <i> Qin J, Wang Z, Hoogeveen-Westerveld M, Shen G, Gong W, Nellist M, Xu W. </i> J Biol Chem, 2016","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T16:18:44.405Z"}},{"region_id":"DP02744r003","ec_ontology":"ECO","end":992,"term_id":"GO:0005515","start":939,"version":4,"statement":[{"text":"ITC showed that full-length TBC1D7 and N-terminal truncated TBC1D7 (residues 19–293) interacted with TSC1(939–992) with comparable affinities: 0.4 and 0.2 μm, respectively","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9P0N9","partner_end":null}],"term_name":"protein binding","ec_name":"isothermal titration calorimetry evidence used in manual assertion","released":"2022_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"26893383","date":"2022-06-16T20:00:55.726Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"vnugnes","reference_html":"Structural Basis of the Interaction between Tuberous Sclerosis Complex 1 (TSC1) and Tre2-Bub2-Cdc16 Domain Family Member 7 (TBC1D7). <i> Qin J, Wang Z, Hoogeveen-Westerveld M, Shen G, Gong W, Nellist M, Xu W. </i> J Biol Chem, 2016","curator_orcid":"0000-0001-8399-7907","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02744r004","ec_ontology":"ECO","end":992,"term_id":"GO:0005515","start":939,"version":4,"statement":[{"text":"Pulldown experiments using the purified proteins showed that TSC1(939–992) was sufficient for interacting with TBC1D7 (Fig. 1a). TBC1D7 and TSC1(939–992) formed a stable complex and co-migrated in SEC.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9P0N9","partner_end":null}],"term_name":"protein binding","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","released":"2022_06","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"26893383","date":"2022-06-16T20:00:35.961Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006077","curator_id":"vnugnes","reference_html":"Structural Basis of the Interaction between Tuberous Sclerosis Complex 1 (TSC1) and Tre2-Bub2-Cdc16 Domain Family Member 7 (TBC1D7). <i> Qin J, Wang Z, Hoogeveen-Westerveld M, Shen G, Gong W, Nellist M, Xu W. </i> J Biol Chem, 2016","curator_orcid":"0000-0001-8399-7907","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Cellular component","ec_ontology":"ECO","end":992,"region_id":"DP02744r005","start":939,"term_id":"GO:0033596","statement":[{"text":"The TSC1-TBC1D7 interaction is important for the stability and activity of the TSC complex, a crucial regulator of the mTORC1 pathway that controls cell growth (25). Here we reveal the structural basis of the TSC1-TBC1D7 interaction.","type":"Discussion"}],"curator_id":"vnugnes","released":"2022_06","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"26893383","version":4,"reference_html":"Structural Basis of the Interaction between Tuberous Sclerosis Complex 1 (TSC1) and Tre2-Bub2-Cdc16 Domain Family Member 7 (TBC1D7). <i> Qin J, Wang Z, Hoogeveen-Westerveld M, Shen G, Gong W, Nellist M, Xu W. </i> J Biol Chem, 2016","date":"2022-06-16T20:00:11.912Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"5EJC"}],"term_name":"TSC1-TSC2 complex","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A protein complex consisting of at least tumerin and hamartin; its formation may regulate hamartin homomultimer formation. The complex acts as a GTPase activating protein (GAP) for the small GTPase (Rheb), and inhibits the TOR signaling pathway.\" [PMID:10585443, PMID:17121544, PMID:9580671]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02744","date":"2020-04-08T23:08:07.447Z","organism":"Homo sapiens","regions_counter":7,"name":"Hamartin","dataset":["Autophagy-related proteins","Cancer-related proteins","NDDs-related proteins","Age-related disorders proteins"],"UniParc":"UPI000016A7B6","uniref100":"UniRef100_Q92574","uniref90":"UniRef90_Q92574","uniref50":"UniRef50_Q92574","genes":[{"name":{"value":"TSC1"},"synonyms":[{"value":"KIAA0243"},{"value":"TSC"}]}],"alphafold_very_low_content":0.4424398625429553,"disorder_content":0.01288659793814433,"disprot_consensus":{"full":[{"start":939,"end":977,"type":"F"},{"start":978,"end":992,"type":"D"}],"Structural state":[{"start":978,"end":992,"type":"D"}],"Molecular function":[{"start":939,"end":992,"type":"F"}],"Cellular component":[{"start":939,"end":992,"type":"F"}]}},{"acc":"P05231","features":{"gene3D":[],"pfam":[{"id":"PF00489","name":"Interleukin-6/G-CSF/MGF family","start":27,"end":212}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MNSFSTSAFGPVAFSLGLLLVLPAAFPAPVPPGEDSKDVAAPHRQPLTSSERIDKQIRYILDGISALRKETCNKSNMCESSKEALAENNLNLPKMAEKDGCFQSGFNEETCLVKIITGLLEFEVYLEYLQNRFESSEEQARAVQMSTKVLIQFLQKKAKNLDAITTPDPTTNASLLTKLQAQNQWLQDMTTHLILRSFKEFLQSSLRALRQM","length":212,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":46,"region_id":"DP02745r001","start":28,"term_id":"IDPO:0000002","statement":[{"text":"Although the amino-terminal 19 amino acids are disordered in solution, the remainder of the molecule has a well defined structure that shares many features displayed by other long-chain four-helix bundle cytokines.","type":"Abstract"},{"text":"Essentially all restraints are localized to residues 20 to 185; we have reported that the amino-terminal 19 residues of IL-6 are extremely flexible, as evidenced by observed 15N T2 values (Xu et al., 1996), and thus fail to yield any restraints useful for 3D structure determination.","type":"Results"},{"text":"The disordered N-terminal 19 residues correspond to the region 28-46 of the protein, since the authors cloned the gene lacking its signal peptide.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9159484","version":2,"reference_html":"Solution structure of recombinant human interleukin-6. <i> Xu GY, Yu HA, Hong J, Stahl M, McDonagh T, Kay LE, Cumming DA. </i> J Mol Biol, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"1IL6"},{"db":"PDB","id":"2IL6"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T11:13:58.550Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":28,"end":46,"reference_id":"9118960","reference_source":"pmid","reference_html":"1.9 A crystal structure of interleukin 6: implications for a novel mode of receptor dimerization and signaling. <i> Somers W, Stahl M, Seehra JS. </i> EMBO J, 1997","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1ALU"}],"region_id":"DP02745r002","statement":[{"text":"The N-termini of IL-6 and G-CSF are disordered so that the crystal structures of both begin at the start of helix A, whereas the N-terminal residues of hGH are ordered and are involved in receptor binding.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-29T18:47:47.744Z"}}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02745","date":"2020-04-08T23:39:16.558Z","organism":"Homo sapiens","regions_counter":2,"name":"Interleukin-6","dataset":["Extracellular matrix proteins"],"UniParc":"UPI000002C4A6","uniref100":"UniRef100_P05231","uniref90":"UniRef90_P05231","uniref50":"UniRef50_P05231","genes":[{"name":{"value":"IL6","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6018","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6018"}}]},"synonyms":[{"value":"IFNB2"}]}],"alphafold_very_low_content":0.0330188679245283,"disorder_content":0.08962264150943396,"disprot_consensus":{"full":[{"start":28,"end":46,"type":"D"}],"Structural state":[{"start":28,"end":46,"type":"D"}]}},{"acc":"Q14565","features":{"gene3D":[],"pfam":[{"id":"PF08423","name":"Rad51","start":94,"end":338},{"id":"PF14520","name":"SAM-like Helix-hairpin-helix tandem","start":25,"end":79}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MKEDQVVAEEPGFQDEEESLFQDIDLLQKHGINVADIKKLKSVGICTIKGIQMTTRRALCNVKGLSEAKVDKIKEAANKLIEPGFLTAFEYSEKRKMVFHITTGSQEFDKLLGGGIESMAITEAFGEFRTGKTQLSHTLCVTAQLPGAGGYPGGKIIFIDTENTFRPDRLRDIADRFNVDHDAVLDNVLYARAYTSEHQMELLDYVAAKFHEEAGIFKLLIIDSIMALFRVDFSGRGELAERQQKLAQMLSRLQKISEEYNVAVFVTNQMTADPGATMTFQADPKKPIGGHILAHASTTRISLRKGRGELRIAKIYDSPEMPENEATFAITAGGIGDAKE","length":340,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":289,"region_id":"DP02746r001","start":271,"term_id":"IDPO:0000002","statement":[{"text":"In the L2 regions (shown in blue in Fig. 1 [triangle]), the full-length HsDMC1 structure has a slightly larger section of disordered amino-acid residues (residues 271–289).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23545642","version":2,"reference_html":"Structure of a filament of stacked octamers of human DMC1 recombinase. <i> Du L, Luo Y. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4HYY"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":289,"region_id":"DP02746r002","start":271,"term_id":"IDPO:0000002","statement":[{"text":"About 30% of the Dmc1 protein (the N-terminal region, Dmc11–82, and the putative DNA binding region (Loop 2), Dmc1 271–289) was uninterpretable from the calculated electron density maps, suggesting that these regions are either highly flexible or have multiple conformations.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15125839","version":2,"reference_html":"Structural basis for octameric ring formation and DNA interaction of the human homologous-pairing protein Dmc1. <i> Kinebuchi T, Kagawa W, Enomoto R, Tanaka K, Miyagawa K, Shibata T, Kurumizaka H, Yokoyama S. </i> Mol Cell, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1V5W"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":82,"region_id":"DP02746r003","start":1,"term_id":"IDPO:0000002","statement":[{"text":"About 30% of the Dmc1 protein (the N-terminal region, Dmc1 1–82, and the putative DNA binding region (Loop 2), Dmc1 271–289) was uninterpretable from the calculated electron density maps, suggesting that these regions are either highly flexible or have multiple conformations.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15125839","version":2,"reference_html":"Structural basis for octameric ring formation and DNA interaction of the human homologous-pairing protein Dmc1. <i> Kinebuchi T, Kagawa W, Enomoto R, Tanaka K, Miyagawa K, Shibata T, Kurumizaka H, Yokoyama S. </i> Mol Cell, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1V5W"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","ncbi_taxon_id":9606,"disprot_id":"DP02746","date":"2020-04-08T23:58:29.672Z","organism":"Homo sapiens","regions_counter":3,"name":"Meiotic recombination protein DMC1/LIM15 homolog","dataset":[],"UniParc":"UPI000016AAAD","uniref100":"UniRef100_Q14565","uniref90":"UniRef90_Q14565","uniref50":"UniRef50_Q14565","genes":[{"name":{"value":"DMC1"},"synonyms":[{"value":"DMC1H"},{"value":"LIM15"}]}],"alphafold_very_low_content":0.05,"disorder_content":0.29705882352941176,"disprot_consensus":{"full":[{"start":1,"end":82,"type":"D"},{"start":271,"end":289,"type":"D"}],"Structural state":[{"start":1,"end":82,"type":"D"},{"start":271,"end":289,"type":"D"}]}},{"acc":"Q9GZN7","features":{"gene3D":[],"pfam":[{"id":"PF10259","name":"Rogdi leucine zipper containing protein","start":18,"end":275}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MATVMAATAAERAVLEEEFRWLLHDEVHAVLKQLQDILKEASLRFTLPGSGTEGPAKQENFILGSCGTDQVKGVLTLQGDALSQADVNLKMPRNNQLLHFAFREDKQWKLQQIQDARNHVSQAIYLLTSRDQSYQFKTGAEVLKLMDAVMLQLTRARNRLTTPATLTLPEIAASGLTRMFAPALPSDLLVNVYINLNKLCLTVYQLHALQPNSTKNFRPAGGAVLHSPGAMFEWGSQRLEVSHVHKVECVIPWLNDALVYFTVSLQLCQQLKDKISVFSSYWSYRPF","length":287,"regions":[{"start":47,"end":56,"reference_id":"28638151","reference_source":"pmid","reference_html":"The crystal structure of human Rogdi provides insight into the causes of Kohlschutter-Tönz Syndrome. <i> Lee H, Jeong H, Choe J, Jun Y, Lim C, Lee C. </i> Sci Rep, 2017","date":"2023-05-03T20:41:35.498Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5XQH"}],"region_id":"DP02747r004","statement":[{"text":"Residues 11 to 23, 47 to 56, 64 to 68, 92 to 96, 130 to 138, and 266 were not modelled due to weak electron density.","type":"Results"}]}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02747","date":"2020-04-09T09:47:07.186Z","organism":"Homo sapiens","regions_counter":4,"name":"Protein rogdi homolog","dataset":["NDDs-related proteins"],"UniParc":"UPI0000037B8E","uniref100":"UniRef100_Q9GZN7","uniref90":"UniRef90_Q9GZN7","uniref50":"UniRef50_Q9GZN7","genes":[{"name":{"value":"ROGDI"}}],"alphafold_very_low_content":0.04878048780487805,"disorder_content":0.03484320557491289,"disprot_consensus":{"full":[{"start":47,"end":56,"type":"D"}],"Structural state":[{"start":47,"end":56,"type":"D"}]}},{"acc":"P36871","features":{"gene3D":[],"pfam":[{"id":"PF02878","name":"Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I","start":15,"end":157},{"id":"PF02879","name":"Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II","start":194,"end":301},{"id":"PF02880","name":"Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III","start":307,"end":420},{"id":"PF24947","name":"Phosphoglucomutase-1, C-terminal domain","start":422,"end":559}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MVKIVTVKTQAYQDQKPGTSGLRKRVKVFQSSANYAENFIQSIISTVEPAQRQEATLVVGGDGRFYMKEAIQLIARIAAANGIGRLVIGQNGILSTPAVSCIIRKIKAIGGIILTASHNPGGPNGDFGIKFNISNGGPAPEAITDKIFQISKTIEEYAVCPDLKVDLGVLGKQQFDLENKFKPFTVEIVDSVEAYATMLRSIFDFSALKELLSGPNRLKIRIDAMHGVVGPYVKKILCEELGAPANSAVNCVPLEDFGGHHPDPNLTYAADLVETMKSGEHDFGAAFDGDGDRNMILGKHGFFVNPSDSVAVIAANIFSIPYFQQTGVRGFARSMPTSGALDRVASATKIALYETPTGWKFFGNLMDASKLSLCGEESFGTGSDHIREKDGLWAVLAWLSILATRKQSVEDILKDHWQKYGRNFFTRYDYEEVEAEGANKMMKDLEALMFDRSFVGKQFSANDKVYTVEKADNFEYSDPVDGSISRNQGLRLIFTDGSRIVFRLSGTGSAGATIRLYIDSYEKDVAKINQDPQVMLAPLISIALKVSQLQERTGRTAPTVIT","length":562,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":267,"region_id":"DP02748r001","start":256,"term_id":"IDPO:0000002","statement":[{"text":"In an apparent series of propagated changes, several other nearby loops are also disordered, including another in D1 (residues 64–65) and a larger region in D2 (residues 256–267). In total, 23 residues in two domains are affected by induced disorder in the structure of G291R mutant","type":"Results"},{"text":"Through comparison with the high-resolution crystal structure of wild-type (WT) human PGM1, also reported here, we find that both mutant enzymes suffer from regions of induced structural disorder and other effects resulting from the dramatic change in physicochemical characteristics at the site of mutation.","type":"Introduction"},{"text":"Two independent glycine to arginine substitutions (G121R and G291R), both affecting key active site loops of PGM1, are found to induce regions of structural disorder, as evidenced by a nearly complete loss of electron density for as many as 23 amino acids.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26972339","version":2,"reference_html":"Induced Structural Disorder as a Molecular Mechanism for Enzyme Dysfunction in Phosphoglucomutase 1 Deficiency. <i> Stiers KM, Kain BN, Graham AC, Beamer LJ. </i> J Mol Biol, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5HSH"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02748","date":"2020-04-09T13:04:02.952Z","organism":"Homo sapiens","regions_counter":1,"name":"Phosphoglucomutase-1","dataset":[],"UniParc":"UPI0000131860","uniref100":"UniRef100_P36871","uniref90":"UniRef90_P36871","uniref50":"UniRef50_P36871","genes":[{"name":{"value":"PGM1"}}],"alphafold_very_low_content":0,"disorder_content":0.021352313167259787,"disprot_consensus":{"full":[{"start":256,"end":267,"type":"D"}],"Structural state":[{"start":256,"end":267,"type":"D"}]}},{"acc":"P09041","features":{"gene3D":[{"start":76,"end":416,"id":"G3DSA:3.40.50.1260","name":"G3DSA:3.40.50.1260"},{"start":76,"end":416,"id":"G3DSA:3.40.50.1260","name":"G3DSA:3.40.50.1260"}],"pfam":[{"id":"PF00162","name":"Phosphoglycerate kinase","start":9,"end":406}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MALSAKLTLDKVDLKGKRVIMRVDFNVPMKNNQITNNQRIKAAIPSIKHCLDNGAKSVVLMSHLGRPDGIPMPDKYSLEPVADELKSLLNKDVIFLKDCVGPEVEQACANPDNGSIILLENLRFHVEEEGKGKDSSGKKISADPAKVEAFQASLSKLGDVYVNDAFGTAHRAHSSTVGVNLPQKASGFLMKKELDYFSKALEKPERPFLAILGGAKVKDKIQLIKNMLDKVNFMIIGGGMAYTFLKELKNMQIGASLFDEEGATIVKEIMEKAEKNGVKIVFPVDFVTGDKFDENAKVGQATIESGIPSGWMGLDCGPESIKINAQIVAQAKLIVWNGPIGVFEWDAFAKGTKALMDEVVKATSNGCVTIIGGGDTATCCAKWGTEDKVSHVSTGGGASLELLEGKILPGVEALSNM","length":417,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":386,"region_id":"DP02749r001","start":372,"term_id":"IDPO:0000002","statement":[{"text":"Binding 3PG causes a 13 degree rotation that partially closes the structure and causes helix 13, which is disordered in the unliganded structure, to stabilize.","type":"Abstract"},{"text":"Residues 372–386 are disordered in the monomer bound with 3PG, similar to the unliganded PGK2 structure; however, these residues are clearly ordered, forming a helix, in the monomer with ATP bound.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18004764","version":2,"reference_html":"X-ray analysis of phosphoglycerate kinase 2, a sperm-specific isoform from Mus musculus. <i> Sawyer GM, Monzingo AF, Poteet EC, O'Brien DA, Robertus JD. </i> Proteins, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2P9Q"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":386,"region_id":"DP02749r002","start":372,"term_id":"IDPO:0000011","statement":[{"text":"Binding 3PG causes a 13 degree rotation that partially closes the structure and causes helix 13, which is disordered in the unliganded structure, to stabilize.","type":"Abstract"},{"text":"Binding ATP leaves the protein in the open configuration but also causes helix 13 to be ordered.","type":"Abstract"},{"text":"Residues 372–386 are disordered in the monomer bound with 3PG, similar to the unliganded PGK2 structure; however, these residues are clearly ordered, forming a helix, in the monomer with ATP bound.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18004764","version":2,"reference_html":"X-ray analysis of phosphoglycerate kinase 2, a sperm-specific isoform from Mus musculus. <i> Sawyer GM, Monzingo AF, Poteet EC, O'Brien DA, Robertus JD. </i> Proteins, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2PAA"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2021_06","ncbi_taxon_id":10090,"disprot_id":"DP02749","date":"2020-04-09T13:19:14.257Z","organism":"Mus musculus","regions_counter":2,"name":"Phosphoglycerate kinase 2","dataset":[],"UniParc":"UPI0000161CF4","uniref100":"UniRef100_P09041","uniref90":"UniRef90_P09041","uniref50":"UniRef50_P09041","genes":[{"name":{"value":"Pgk2"},"synonyms":[{"value":"Pgk-2"}]}],"alphafold_very_low_content":0,"disorder_content":0.03597122302158273,"disprot_consensus":{"full":[{"start":372,"end":386,"type":"T"}],"Structural state":[{"start":372,"end":386,"type":"D"}],"Structural transition":[{"start":372,"end":386,"type":"T"}]}},{"acc":"P17109","features":{"gene3D":[],"pfam":[{"id":"PF02775","name":"Thiamine pyrophosphate enzyme, C-terminal TPP binding domain","start":422,"end":534},{"id":"PF02776","name":"Thiamine pyrophosphate enzyme, N-terminal TPP binding domain","start":10,"end":118},{"id":"PF16582","name":"Middle domain of thiamine pyrophosphate","start":184,"end":388}]},"creator":"fquaglia","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"sequence":"MSVSAFNRRWAAVILEALTRHGVRHICIAPGSRSTPLTLAAAENSAFIHHTHFDERGLGHLALGLAKVSKQPVAVIVTSGTAVANLYPALIEAGLTGEKLILLTADRPPELIDCGANQAIRQPGMFASHPTHSISLPRPTQDIPARWLVSTIDHALGTLHAGGVHINCPFAEPLYGEMDDTGLSWQQRLGDWWQDDKPWLREAPRLESEKQRDWFFWRQKRGVVVAGRMSAEEGKKVALWAQTLGWPLIGDVLSQTGQPLPCADLWLGNAKATSELQQAQIVVQLGSSLTGKRLLQWQASCEPEEYWIVDDIEGRLDPAHHRGRRLIANIADWLELHPAEKRQPWCVEIPRLAEQAMQAVIARRDAFGEAQLAHRICDYLPEQGQLFVGNSLVVRLIDALSQLPAGYPVYSNRGASGIDGLLSTAAGVQRASGKPTLAIVGDLSALYDLNALALLRQVSAPLVLIVVNNNGGQIFSLLPTPQSERERFYLMPQNVHFEHAAAMFELKYHRPQNWQELETAFADAWRTPTTTVIEMVVNDTDGAQTLQQLLAQVSHL","length":556,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":488,"region_id":"DP02750r001","start":472,"term_id":"IDPO:0000002","statement":[{"text":"The residues Gly472 to Phe488 of the active site region are either disordered, or in an open conformation in the MenD oxoglutarate complex structure, but adopt a closed conformation in the MenD ThDP complex structure.","type":"Abstract"},{"text":"The most significant difference between the oxoglutarate complex and the ThDP complex structure, presumably caused by the binding of ThDP, is the movement of the loop (Tyr489 to Asn494) and the disorder region Gly472 to Phe488","type":"Results"},{"text":"Active site pocket of EcMenD anchoring ThDP and Mg2+ shows a disordered region in the apo and oxoglutarate complex structures, and an ordered region in the ThDP complex structure.","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19703421","version":2,"reference_html":"Structural and functional analysis of Vitamin K2 synthesis protein MenD. <i> Priyadarshi A, Kim EE, Hwang KY. </i> Biochem Biophys Res Commun, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3HWW"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":488,"region_id":"DP02750r002","start":472,"term_id":"IDPO:0000011","statement":[{"text":"The residues Gly472 to Phe488 of the active site region are either disordered, or in an open conformation in the MenD oxoglutarate complex structure, but adopt a closed conformation in the MenD ThDP complex structure.","type":"Abstract"},{"text":"Active site pocket of EcMenD anchoring ThDP and Mg2+ shows a disordered region in the apo and oxoglutarate complex structures, and an ordered region in the ThDP complex structure.","type":"Figure"},{"text":"The most significant difference between the oxoglutarate complex and the ThDP complex structure, presumably caused by the binding of ThDP, is the movement of the loop (Tyr489 to Asn494) and the disorder region Gly472 to Phe488","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19703421","version":2,"reference_html":"Structural and functional analysis of Vitamin K2 synthesis protein MenD. <i> Priyadarshi A, Kim EE, Hwang KY. </i> Biochem Biophys Res Commun, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3HWX"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":488,"region_id":"DP02750r003","start":472,"term_id":"IDPO:0000002","statement":[{"text":"The region between β15 and α21, residue 472–488 (A chain) and residue 471–493 (B chain) is found disorder or have a weak density map, corresponding to the high flexible loop binding region for the cofactor ThDP.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19338755","version":2,"reference_html":"Structural insights of the MenD from Escherichia coli reveal ThDP affinity. <i> Priyadarshi A, Saleem Y, Nam KH, Kim KS, Park SY, Kim EE, Hwang KY. </i> Biochem Biophys Res Commun, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3FLM"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":83333,"disprot_id":"DP02750","date":"2020-04-14T09:13:12.797Z","organism":"Escherichia coli (strain K12)","regions_counter":3,"name":"2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase","dataset":[],"UniParc":"UPI000016F2E6","uniref100":"UniRef100_C4ZUA7","uniref90":"UniRef90_Q8XDX8","uniref50":"UniRef50_Q8XDX8","genes":[{"name":{"value":"menD","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01659","url":"https://hamap.expasy.org/unirule/MF_01659"}}]},"olnNames":[{"value":"b2264"},{"value":"JW5374"}]}],"alphafold_very_low_content":0,"disorder_content":0.030575539568345324,"disprot_consensus":{"full":[{"start":472,"end":488,"type":"T"}],"Structural state":[{"start":472,"end":488,"type":"D"}],"Structural transition":[{"start":472,"end":488,"type":"T"}]}},{"acc":"Q03653","features":{"gene3D":[],"pfam":[{"id":"PF21072","name":"EFR3 protein","start":12,"end":556}]},"creator":"fquaglia","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"sequence":"MQLSMRMMFTPKHQKLVNQCYPTGRTTDKKPKSSETSYLLYYVNSRRSKLEKVSTYLIKRSTSDLNHRRIGNIAVTLDLMNKIVLHCKENLNVFVKDFLYIMNKVLSNNNFNNDVSVVELIELAFSSICQNLDDVLCNGDMEFVQLYQNFVDLFFKIVTERIHNDDMLLKCCIDISNTNSVSSNPQLNHFVSKSVAYTISKFQERNPKFKTLSLEAALESNLGKRLSRTQTRTIGLDKAAEDNHDLSVKALQSYFNTTETDKLNLSIRTLLRCLQSTPNKELLEFVCNGIPVQLRYIVILLLVRQLSDKDKNVNPIVSLKLMSSLLVSDVSIVGLSVLDIMRKLLNFQLKNATNKEVVAQSCITMTDLNHKTYYAEQTSDMLYELLLKLKSDTVKDVEKNAVVEDIDFLVEHITQPSISLELFIDLAHYMKNHIICLFNIVETEVPSSILFSKLYSLLRELDSHGVQKEMMEEIFDKYGKMALLSGLNYFLENVSEPEYTYYSYHLQAANFLKLNDYKSQTEYKMQTRTLFTKEDLLSYYSDTGSNKYSKKGAQILLSRDNQISTSDLLSDSQVRTTPLEYKNVPNAIFSNGKAVYDNNDFAAKQNKFDNSIDDNIEEANDTVISDANAKGSIYRFVAEDARSWKTMRATAPKVSDLKKTMNEKNIPNNMKRDGSFRGSQSVKSRVTNITFLLNELKTFSDDANKIKDPDEENIVGLDKIDVARSNSLRLAPISSLSDRSSIGNRKSFLQKTATGENQNDDFKDANEDLHSLSSRGKIFSST","length":782,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":232,"region_id":"DP02751r001","start":217,"term_id":"IDPO:0000002","statement":[{"text":"The final model, which includes residues 9–562 of Efr3-N8–562 except for a disordered loop comprising residues 217–232, was refined to Rwork = 23.11% and Rfree = 25.56% with good geometry","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24360784","version":2,"reference_html":"Structural insights into assembly and regulation of the plasma membrane phosphatidylinositol 4-kinase complex. <i> Wu X, Chi RJ, Baskin JM, Lucast L, Burd CG, De Camilli P, Reinisch KM. </i> Dev Cell, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4N5A"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":559292,"disprot_id":"DP02751","date":"2020-04-14T09:54:46.472Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":1,"name":"Protein EFR3","dataset":[],"UniParc":"UPI000013B910","uniref100":"UniRef100_Q03653","uniref90":"UniRef90_Q03653","uniref50":"UniRef50_Q03653","genes":[{"name":{"value":"EFR3"},"orfNames":[{"value":"YM8261.06C"}],"olnNames":[{"value":"YMR212C"}]}],"alphafold_very_low_content":0.2851662404092072,"disorder_content":0.020460358056265986,"disprot_consensus":{"full":[{"start":217,"end":232,"type":"D"}],"Structural state":[{"start":217,"end":232,"type":"D"}]}},{"acc":"P46951","features":{"gene3D":[{"start":664,"end":807,"id":"G3DSA:1.25.40.10","name":"G3DSA:1.25.40.10"},{"start":664,"end":807,"id":"G3DSA:1.25.40.10","name":"G3DSA:1.25.40.10"}],"pfam":[{"id":"PF29148","name":"YPP1 N-terminal domain","start":15,"end":199},{"id":"PF29151","name":"YPP1 middle domain","start":239,"end":677},{"id":"PF29158","name":"YPP1 C-terminal domain","start":691,"end":817}]},"creator":"fquaglia","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"sequence":"MPNSNVRIPPTVPSKIIDVVDQALRARLLGGSTFNSGFDSLDSVLNLQFRLHYHVIGSNGPAKPVCDVLLKESQNLEKNMSMMEELNDYPEITKLVEKILFNCLGILFFHRGQFQESQRCLLHSLKIHNNTASQKTALMEQYDRYLIVENLYYRGLVSQDINIMQNVFYKELLAHVDTIPPESNGLLFEYISLIVAKLRFNQIQDLAENFKTTVENPFILFLYMIKKFQSPLKKHIDNDDLYLKFGQNVLLKAKFPTASETNDEALEHFNVFLQYYFKFTHIKKIKVNPSWYNFIISSMEKTFQSIEVSKTAMFLFQNLSDNSNDEIKKKTFKRESILNFVNFVKYNDKYYQLHDNSHRDIISFIDAYSFILQNSSKTDSIENVFDYDNTVSTFATSLNSFYKEYNLPLMSQSESLDWLENSTRCVYPGNISKVLTNAWSTLYEIRKYQLDFLVSNNLTSYLCNAMMLSTKEKDNADVEEQEEGEEEKALRELQFKYSYTLAQQRHIETAIKTLESLILSKNPNYYKAWHLLALCRSVQEDKEMSYKIVCSVLEAMNESLQNNTLLLNDRWQFIHLKLTQLALIEEIFGTLEALETLPEVFELYATLFPDSQPELNSMGPKYSQTKEYLLQMVWIFAANMYMRTKDNDEDAKAAIKEASNVESKFKNLNCNIANGYLSIIKDEPGVALKEFETVLYYDENNLDALVGFAELIFPEELGVEETNLERYYTLSLDKKPGKRAKLTFVNDTDRSAAYARLKFLLECAILESIEAYYSPEVWWYLSLIYEKYQDDEYKNSLLKCIKYQELNPIRSLRYCNY","length":817,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":483,"region_id":"DP02752r001","start":470,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Ypp1 structure comprises residues 12–817, except for disordered loops spanning residues 131–134, 470–483, 714–741, and 788–790. Residues in several additional loops (residues 608–617, 661–666, and 680–683) could not be modeled in some of the other Ypp1 molecules within the unit cell. The structure was refined to Rwork = 23.98% and Rfree = 27.72% with good geometry","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24360784","version":2,"reference_html":"Structural insights into assembly and regulation of the plasma membrane phosphatidylinositol 4-kinase complex. <i> Wu X, Chi RJ, Baskin JM, Lucast L, Burd CG, De Camilli P, Reinisch KM. </i> Dev Cell, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4N5C"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-05T14:34:29.897Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":741,"region_id":"DP02752r002","start":714,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Ypp1 structure comprises residues 12–817, except for disordered loops spanning residues 131–134, 470–483, 714–741, and 788–790. Residues in several additional loops (residues 608–617, 661–666, and 680–683) could not be modeled in some of the other Ypp1 molecules within the unit cell. The structure was refined to Rwork = 23.98% and Rfree = 27.72% with good geometry","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24360784","version":2,"reference_html":"Structural insights into assembly and regulation of the plasma membrane phosphatidylinositol 4-kinase complex. <i> Wu X, Chi RJ, Baskin JM, Lucast L, Burd CG, De Camilli P, Reinisch KM. </i> Dev Cell, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4N5C"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-05T14:34:31.027Z"}}],"released":"2023_12","ncbi_taxon_id":559292,"disprot_id":"DP02752","date":"2020-04-14T10:07:18.350Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":4,"name":"Cargo-transport protein YPP1","dataset":[],"UniParc":"UPI000013AF9E","uniref100":"UniRef100_P46951","uniref90":"UniRef90_P46951","uniref50":"UniRef50_P46951","genes":[{"name":{"value":"YPP1"},"orfNames":[{"value":"G7594"}],"olnNames":[{"value":"YGR198W"}]}],"alphafold_very_low_content":0.056303549571603426,"disorder_content":0.051407588739290085,"disprot_consensus":{"full":[{"start":470,"end":483,"type":"D"},{"start":714,"end":741,"type":"D"}],"Structural state":[{"start":470,"end":483,"type":"D"},{"start":714,"end":741,"type":"D"}]}},{"acc":"Q13617","features":{"gene3D":[],"pfam":[{"id":"PF00888","name":"Cullin alpha solenoid domain","start":14,"end":487},{"id":"PF10557","name":"Cullin protein neddylation domain","start":675,"end":735},{"id":"PF26557","name":"Cullin alpha+beta domain","start":511,"end":644}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MSLKPRVVDFDETWNKLLTTIKAVVMLEYVERATWNDRFSDIYALCVAYPEPLGERLYTETKIFLENHVRHLHKRVLESEEQVLVMYHRYWEEYSKGADYMDCLYRYLNTQFIKKNKLTEADLQYGYGGVDMNEPLMEIGELALDMWRKLMVEPLQAILIRMLLREIKNDRGGEDPNQKVIHGVINSFVHVEQYKKKFPLKFYQEIFESPFLTETGEYYKQEASNLLQESNCSQYMEKVLGRLKDEEIRCRKYLHPSSYTKVIHECQQRMVADHLQFLHAECHNIIRQEKKNDMANMYVLLRAVSTGLPHMIQELQNHIHDEGLRATSNLTQENMPTLFVESVLEVHGKFVQLINTVLNGDQHFMSALDKALTSVVNYREPKSVCKAPELLAKYCDNLLKKSAKGMTENEVEDRLTSFITVFKYIDDKDVFQKFYARMLAKRLIHGLSMSMDSEEAMINKLKQACGYEFTSKLHRMYTDMSVSADLNNKFNNFIKNQDTVIDLGISFQIYVLQAGAWPLTQAPSSTFAIPQELEKSVQMFELFYSQHFSGRKLTWLHYLCTGEVKMNYLGKPYVAMVTTYQMAVLLAFNNSETVSYKELQDSTQMNEKELTKTIKSLLDVKMINHDSEKEDIDAESSFSLNMNFSSKRTKFKITTSMQKDTPQEMEQTRSAVDEDRKMYLQAAIVRIMKARKVLRHNALIQEVISQSRARFNPSISMIKKCIEVLIDKQYIERSQASADEYSYVA","length":745,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":134,"region_id":"DP02753r001","start":117,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Structural comparison of Cul2 with other cullin proteins reveals that they share a conserved cullin repeat structure and contain flexible N termini which play different roles in CRL formation","type":"Results"},{"text":"To investigate how VHL recruits Cul2, we co-expressed VHL (residues 1–213), EloB (residues 1–118), EloC (residues 17–112) and an N-terminal segment of Cul2 (Cul2N) spanning the first cullin repeat (residues 1–163), the minimal domain required for binding to VHL","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"25661653","version":2,"reference_html":"Insights into Cullin-RING E3 ubiquitin ligase recruitment: structure of the VHL-EloBC-Cul2 complex. <i> Nguyen HC, Yang H, Fribourgh JL, Wolfe LS, Xiong Y. </i> Structure, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4WQO"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-05T15:01:21.130Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":134,"region_id":"DP02753r004","start":117,"term_id":"IDPO:0000002","unpublished":true,"curator_id":"esalladini","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Edoardo Salladini","reference_id":"28591624","version":3,"reference_html":"Crystal Structure of the Cul2-Rbx1-EloBC-VHL Ubiquitin Ligase Complex. <i> Cardote TAF, Gadd MS, Ciulli A. </i> Structure, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5N4W"}],"term_name":"disorder","curator_orcid":"0000-0002-5152-5953","statement":[{"text":"These residues could not be modeled, but was not mention in the text.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-05T14:57:58.698Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":634,"region_id":"DP02753r005","start":625,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"In our structure, some residues at the CTD (625–634 and 645–660) were disordered and could not be modeled.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28591624","version":2,"reference_html":"Crystal Structure of the Cul2-Rbx1-EloBC-VHL Ubiquitin Ligase Complex. <i> Cardote TAF, Gadd MS, Ciulli A. </i> Structure, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5N4W"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-05T14:59:38.118Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":660,"region_id":"DP02753r006","start":645,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"In our structure, some residues at the CTD (625–634 and 645–660) were disordered and could not be modeled.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28591624","version":2,"reference_html":"Crystal Structure of the Cul2-Rbx1-EloBC-VHL Ubiquitin Ligase Complex. <i> Cardote TAF, Gadd MS, Ciulli A. </i> Structure, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5N4W"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-05T14:59:37.219Z"}}],"released":"2023_12","ncbi_taxon_id":9606,"disprot_id":"DP02753","date":"2020-04-14T11:22:25.544Z","organism":"Homo sapiens","regions_counter":6,"name":"Cullin-2","dataset":[],"UniParc":"UPI0000154743","uniref100":"UniRef100_Q13617","uniref90":"UniRef90_Q13617","uniref50":"UniRef50_Q13617","genes":[{"name":{"value":"CUL2"}}],"alphafold_very_low_content":0.012080536912751677,"disorder_content":0.05906040268456376,"disprot_consensus":{"full":[{"start":117,"end":134,"type":"D"},{"start":625,"end":634,"type":"D"},{"start":645,"end":660,"type":"D"}],"Structural state":[{"start":117,"end":134,"type":"D"},{"start":625,"end":634,"type":"D"},{"start":645,"end":660,"type":"D"}]}},{"acc":"Q9S7B5","features":{"gene3D":[{"start":60,"end":520,"id":"G3DSA:3.40.50.1100","name":"G3DSA:3.40.50.1100"}],"pfam":[{"id":"PF00291","name":"Pyridoxal-phosphate dependent enzyme","start":165,"end":472}]},"creator":"fquaglia","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"sequence":"MASSCLFNASVSSLNPKQDPIRRHRSTSLLRHRPVVISCTADGNNIKAPIETAVKPPHRTEDNIRDEARRNRSNAVNPFSAKYVPFNAAPGSTESYSLDEIVYRSRSGGLLDVEHDMEALKRFDGAYWRDLFDSRVGKSTWPYGSGVWSKKEWVLPEIDDDDIVSAFEGNSNLFWAERFGKQFLGMNDLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMKRPVVGVGCASTGDTSAALSAYCASAGIPSIVFLPANKISMAQLVQPIANGAFVLSIDTDFDGCMKLIREITAELPIYLANSLNSLRLEGQKTAAIEILQQFDWQVPDWVIVPGGNLGNIYAFYKGFKMCQELGLVDRIPRMVCAQAANANPLYLHYKSGWKDFKPMTASTTFASAIQIGDPVSIDRAVYALKKCNGIVEEATEEELMDAMAQADSTGMFICPHTGVALTALFKLRNQGVIAPTDRTVVVSTAHGLKFTQSKIDYHSNAIPDMACRFSNPPVDVKADFGAVMDVLKSYLGSNTLTS","length":526,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":363,"region_id":"DP02754r001","start":347,"term_id":"IDPO:0000002","statement":[{"text":"In addition, a loop between residues 347 and 363 is disordered.","type":"Results"},{"text":"Apart from the disordered area (loop 347–363), this region in TS has the same fold as in the other enzymes.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11344332","version":2,"reference_html":"Crystal structure of threonine synthase from Arabidopsis thaliana. <i> Thomazeau K, Curien G, Dumas R, Biou V. </i> Protein Sci, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1E5X"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":3702,"disprot_id":"DP02754","date":"2020-04-14T11:52:14.482Z","organism":"Arabidopsis thaliana","regions_counter":1,"name":"Threonine synthase 1, chloroplastic","dataset":[],"UniParc":"UPI0000048A1F","uniref100":"UniRef100_Q9S7B5","uniref90":"UniRef90_Q9S7B5","uniref50":"UniRef50_Q9S7B5","genes":[{"name":{"value":"TS1"},"synonyms":[{"value":"MTO2"}],"orfNames":[{"value":"F27B13.80"}],"olnNames":[{"value":"At4g29840"}]}],"alphafold_very_low_content":0.11026615969581749,"disorder_content":0.03231939163498099,"disprot_consensus":{"full":[{"start":347,"end":363,"type":"D"}],"Structural state":[{"start":347,"end":363,"type":"D"}]}},{"acc":"Q69ZK9","features":{"gene3D":[{"start":41,"end":617,"id":"G3DSA:3.40.50.1820","name":"G3DSA:3.40.50.1820"}],"pfam":[{"id":"PF00135","name":"Carboxylesterase family","start":42,"end":601}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MWLLALCLVGLAGAQRGGGGPGGGAPGGPGLGLGSLGEERFPVVNTAYGRVRGVRRELNNEILGPVVQFLGVPYATPPLGARRFQPPEAPASWPGVRNATTLPPACPQNLHGALPAIMLPVWFTDNLEAAATYVQNQSEDCLYLNLYVPTEDGPLTKKRDEATLNPPDTDIRDSGKKPVMLFLHGGSYMEGTGNMFDGSVLAAYGNVIVVTLNYRLGVLGFLSTGDQAAKGNYGLLDQIQALRWLSENIAHFGGDPERITIFGSGAGASCVNLLILSHHSEGLFQKAIAQSGTAISSWSVNYQPLKYTRLLAAKVGCDREDSTEAVECLRRKSSRELVDQDVQPARYHIAFGPVVDGDVVPDDPEILMQQGEFLNYDMLIGVNQGEGLKFVEDSAESEDGVSASAFDFTVSNFVDNLYGYPEGKDVLRETIKFMYTDWADRDNGEMRRKTLLALFTDHQWVAPAVATAKLHADYQSPVYFYTFYHHCQAEGRPEWADAAHGDELPYVFGVPMVGATDLFPCNFSKNDVMLSAVVMTYWTNFAKTGDPNQPVPQDTKFIHTKPNRFEEVVWSKFNSKEKQYLHIGLKPRVRDNYRANKVAFWLELVPHLHNLHTELFTTTTRLPPYATRWPPRTPGPGTSGTRRPPPPATLPPESDIDLGPRAYDRFPGDSRDYSTELSVTVAVGASLLFLNILAFAALYYKRDRRQELRCRRLSPPGGSGSGVPGGGPLLPTAGRELPPEEELVSLQLKRGGGVGADPAEALRPACPPDYTLALRRAPDDVPLLAPGALTLLPSGLGPPPPPPPPSLHPFGPFPPPPPTATSHNNTLPHPHSTTRV","length":836,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":172,"region_id":"DP02755r001","start":159,"term_id":"IDPO:0000002","statement":[{"text":"The crystal structure of NL2A reveals that the A splice insertion, which encompasses residues 152–169, is positioned in the β6–β7 loop. The inserted sequence is mostly disordered in the structure; electron density is observed only for residues 152–158 in one protomer and is entirely absent in the other","type":"Results"},{"text":"In the NL2A structure, the majority of the 17 residues inserted at the A site are disordered, making it difficult to predict the potential contribution of the A insert to NRX binding at this time.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18250328","version":2,"reference_html":"Crystal structure of the extracellular cholinesterase-like domain from neuroligin-2. <i> Koehnke J, Jin X, Budreck EC, Posy S, Scheiffele P, Honig B, Shapiro L. </i> Proc Natl Acad Sci U S A, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3BL8"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","ncbi_taxon_id":10090,"disprot_id":"DP02755","date":"2020-04-14T12:07:11.428Z","organism":"Mus musculus","regions_counter":1,"name":"Neuroligin-2","dataset":[],"UniParc":"UPI00003FEFDD","uniref100":"UniRef100_Q69ZK9","uniref90":"UniRef90_Q69ZK9","uniref50":"UniRef50_Q69ZK9","genes":[{"name":{"value":"Nlgn2"},"synonyms":[{"value":"Kiaa1366"}]}],"alphafold_very_low_content":0.2679425837320574,"disorder_content":0.01674641148325359,"disprot_consensus":{"full":[{"start":159,"end":172,"type":"D"}],"Structural state":[{"start":159,"end":172,"type":"D"}]}},{"acc":"P21447","features":{"gene3D":[{"start":694,"end":1013,"id":"G3DSA:1.20.1560.10","name":"ABC transporter type 1, transmembrane domain"},{"start":694,"end":1013,"id":"G3DSA:1.20.1560.10","name":"ABC transporter type 1, transmembrane domain"}],"pfam":[{"id":"PF00005","name":"ABC transporter","start":406,"end":555},{"id":"PF00005","name":"ABC transporter","start":1049,"end":1200},{"id":"PF00664","name":"ABC transporter transmembrane region","start":50,"end":339},{"id":"PF00664","name":"ABC transporter transmembrane region","start":708,"end":982}]},"creator":"zkalman","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MELEEDLKGRADKNFSKMGKKSKKEKKEKKPAVSVLTMFRYAGWLDRLYMLVGTLAAIIHGVALPLMMLIFGDMTDSFASVGNVSKNSTNMSEADKRAMFAKLEEEMTTYAYYYTGIGAGVLIVAYIQVSFWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELHAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYSIGQVLTVFFSVLIGAFSVGQASPNIEAFANARGAAYEVFKIIDNKPSIDSFSKSGHKPDNIQGNLEFKNIHFSYPSRKEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLDGMVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQTAGNEIELGNEACKSKDEIDNLDMSSKDSGSSLIRRRSTRKSICGPHDQDRKLSTKEALDEDVPPASFWRILKLNSTEWPYFVVGIFCAIINGGLQPAFSVIFSKVVGVFTNGGPPETQRQNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDVSWFDDPKNTTGALTTRLANDAAQVKGATGSRLAVIFQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVTQQLMTFENVLLVFSAIVFGAMAVGQVSSFAPDYAKATVSASHIIRIIEKTPEIDSYSTQGLKPNMLEGNVQFSGVVFNYPTRPSIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSRVVSYEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGKVKEHGTHQQLLAQKGIYFSMVSVQAGAKRS","length":1276,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":686,"region_id":"DP02756r001","start":627,"term_id":"IDPO:0000002","statement":[{"text":"The function of P-gp requires the flexibility of its two halves, which are joined by a mobile linker that is disordered in all mP-gp structures reported so far.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27864369","version":2,"reference_html":"Structures of the Multidrug Transporter P-glycoprotein Reveal Asymmetric ATP Binding and the Mechanism of Polyspecificity. <i> Esser L, Zhou F, Pluchino KM, Shiloach J, Ma J, Tang WK, Gutierrez C, Zhang A, Shukla S, Madigan JP, Zhou T, Kwong PD, Ambudkar SV, Gottesman MM, Xia D. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5KPI"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":686,"region_id":"DP02756r002","start":627,"term_id":"IDPO:0000033","statement":[{"text":"The function of P-gp requires the flexibility of its two halves, which are joined by a mobile linker that is disordered in all mP-gp structures reported so far.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27864369","version":3,"reference_html":"Structures of the Multidrug Transporter P-glycoprotein Reveal Asymmetric ATP Binding and the Mechanism of Polyspecificity. <i> Esser L, Zhou F, Pluchino KM, Shiloach J, Ma J, Tang WK, Gutierrez C, Zhang A, Shukla S, Madigan JP, Zhou T, Kwong PD, Ambudkar SV, Gottesman MM, Xia D. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5KPI"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":683,"region_id":"DP02756r003","start":627,"term_id":"IDPO:0000002","statement":[{"text":"The linker (residues 627–683) between NBD1 and TM7 is not observed and presumed to be disordered. Residues 1–33 and 1272–1276 at the N- and C- termini are also not observed.","type":"Results"},{"text":"The N-terminal half of the protein (blue) and the C-terminal half (yellow) are connected by a flexible linker region (black dashed line) that is disordered in the structure.","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23901103","version":2,"reference_html":"Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain. <i> Ward AB, Szewczyk P, Grimard V, Lee CW, Martinez L, Doshi R, Caya A, Villaluz M, Pardon E, Cregger C, Swartz DJ, Falson PG, Urbatsch IL, Govaerts C, Steyaert J, Chang G. </i> Proc Natl Acad Sci U S A, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4KSC"},{"db":"PDB","id":"4KSB"},{"db":"PDB","id":"4KSD"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":683,"region_id":"DP02756r004","start":627,"term_id":"IDPO:0000033","statement":[{"text":"The linker (residues 627–683) between NBD1 and TM7 is not observed and presumed to be disordered. Residues 1–33 and 1272–1276 at the N- and C- termini are also not observed.","type":"Results"},{"text":"The N-terminal half of the protein (blue) and the C-terminal half (yellow) are connected by a flexible linker region (black dashed line) that is disordered in the structure.","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23901103","version":3,"reference_html":"Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain. <i> Ward AB, Szewczyk P, Grimard V, Lee CW, Martinez L, Doshi R, Caya A, Villaluz M, Pardon E, Cregger C, Swartz DJ, Falson PG, Urbatsch IL, Govaerts C, Steyaert J, Chang G. </i> Proc Natl Acad Sci U S A, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4KSC"},{"db":"PDB","id":"4KSB"},{"db":"PDB","id":"4KSD"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":10090,"disprot_id":"DP02756","date":"2020-04-14T13:10:12.292Z","organism":"Mus musculus","regions_counter":4,"name":"ATP-dependent translocase ABCB1","dataset":[],"UniParc":"UPI000016CFAF","uniref100":"UniRef100_P21447","uniref90":"UniRef90_P21447","uniref50":"UniRef50_P21447","genes":[{"name":{"value":"Abcb1a","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:97570","url":"http://www.informatics.jax.org/marker/MGI:97570"}}]},"synonyms":[{"value":"Abcb4"},{"value":"Mdr1a"},{"value":"Mdr3"},{"value":"Pgy-3"},{"value":"Pgy3"}]}],"alphafold_very_low_content":0.07053291536050156,"disorder_content":0.047021943573667714,"disprot_consensus":{"full":[{"start":627,"end":686,"type":"D"}],"Structural state":[{"start":627,"end":686,"type":"D"}],"Disorder function":[{"start":627,"end":686,"type":"F"}]}},{"acc":"Q9GZU1","features":{"gene3D":[],"pfam":[{"id":"PF08016","name":"Polycystin cation channel","start":385,"end":524},{"id":"PF21381","name":"Mucolipin, extracytosolic domain","start":91,"end":285}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MTAPAGPRGSETERLLTPNPGYGTQAGPSPAPPTPPEEEDLRRRLKYFFMSPCDKFRAKGRKPCKLMLQVVKILVVTVQLILFGLSNQLAVTFREENTIAFRHLFLLGYSDGADDTFAAYTREQLYQAIFHAVDQYLALPDVSLGRYAYVRGGGDPWTNGSGLALCQRYYHRGHVDPANDTFDIDPMVVTDCIQVDPPERPPPPPSDDLTLLESSSSYKNLTLKFHKLVNVTIHFRLKTINLQSLINNEIPDCYTFSVLITFDNKAHSGRIPISLETQAHIQECKHPSVFQHGDNSFRLLFDVVVILTCSLSFLLCARSLLRGFLLQNEFVGFMWRQRGRVISLWERLEFVNGWYILLVTSDVLTISGTIMKIGIEAKNLASYDVCSILLGTSTLLVWVGVIRYLTFFHNYNILIATLRVALPSVMRFCCCVAVIYLGYCFCGWIVLGPYHVKFRSLSMVSECLFSLINGDDMFVTFAAMQAQQGRSSLVWLFSQLYLYSFISLFIYMVLSLFIALITGAYDTIKHPGGAGAEESELQAYIAQCQDSPTSGKFRRGSGSACSLLCCCGRDPSEEHSLLVN","length":580,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":59,"region_id":"DP02757r001","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The electron density is clearly resolved for residues 60–526 in the apo TRPML1 and residues 38–526 in the ML-SA1-bound TRPML1 (Extended Data Fig. 4), with the exception of a short linker in the luminal domain (amino acids 206–215).","type":"Results"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29019983","version":2,"reference_html":"Human TRPML1 channel structures in open and closed conformations. <i> Schmiege P, Fine M, Blobel G, Li X. </i> Nature, 2017","date":"2022-08-04T08:23:08.115Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"5WJ5"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-04T14:49:27.190Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":215,"region_id":"DP02757r002","start":206,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The electron density is clearly resolved for residues 60–526 in the apo TRPML1 and residues 38–526 in the ML-SA1-bound TRPML1 (Extended Data Fig. 4), with the exception of a short linker in the luminal domain (amino acids 206–215).","type":"Results"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29019983","version":2,"reference_html":"Human TRPML1 channel structures in open and closed conformations. <i> Schmiege P, Fine M, Blobel G, Li X. </i> Nature, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"5WJ5"},{"db":"PDB","id":"5WJ9"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-02T18:20:49.369Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":580,"region_id":"DP02757r003","start":527,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The electron density is clearly resolved for residues 60–526 in the apo TRPML1 and residues 38–526 in the ML-SA1-bound TRPML1 (Extended Data Fig. 4), with the exception of a short linker in the luminal domain (amino acids 206–215).","type":"Results"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29019983","version":2,"reference_html":"Human TRPML1 channel structures in open and closed conformations. <i> Schmiege P, Fine M, Blobel G, Li X. </i> Nature, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"5WJ5"},{"db":"PDB","id":"5WJ9"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-02T18:22:03.220Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":215,"region_id":"DP02757r004","start":206,"term_id":"IDPO:0000033","unpublished":true,"statement":[{"text":"The electron density is clearly resolved for residues 60–526 in the apo TRPML1 and residues 38–526 in the ML-SA1-bound TRPML1 (Extended Data Fig. 4), with the exception of a short linker in the luminal domain (amino acids 206–215).","type":"Results"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"cryogenic electron microscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29019983","version":3,"reference_html":"Human TRPML1 channel structures in open and closed conformations. <i> Schmiege P, Fine M, Blobel G, Li X. </i> Nature, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","cross_refs":[{"db":"PDB","id":"5WJ5"},{"db":"PDB","id":"5WJ9"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-02T18:22:22.802Z"}},{"term_namespace":"Biological process","ec_ontology":"ECO","end":578,"region_id":"DP02757r005","start":573,"term_id":"GO:0051179","unpublished":true,"statement":[{"text":"We have also found that the C-terminal tail of mucolipin-1 is palmitoylated and that this modification might regulate the efficiency of endocytosis. Finally, the mutagenesis of both di-leucine motifs abrogated lysosomal accumulation and resulted in cell-surface redistribution of mucolipin-1. Taken together, these results reveal novel information regarding the motifs that regulate mucolipin-1 trafficking and suggest a role for palmitoylation in protein sorting.","type":"Abstract"},{"text":"These data indicate that the E573EHSLL sequence is an essential component of the endosomal targeting signal in mucolipin-1 cytoplasmic tail.","type":"Results"},{"text":"A di-leucine motif located at C-terminal tail of mucolipin-1 mediates internalization of Tac-MLN-CTail chimera.","type":"Figure"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"immunodetection assay evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16497227","version":3,"reference_html":"Two di-leucine motifs regulate trafficking of mucolipin-1 to lysosomes. <i> Vergarajauregui S, Puertollano R. </i> Traffic, 2006","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","term_name":"localization","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-05T19:14:38.667Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":568,"region_id":"DP02757r006","start":564,"term_id":"IDPO:0000044","unpublished":true,"statement":[{"text":"We have also found that the C-terminal tail of mucolipin-1 is palmitoylated and that this modification might regulate the efficiency of endocytosis. Finally, the mutagenesis of both di-leucine motifs abrogated lysosomal accumulation and resulted in cell-surface redistribution of mucolipin-1. Taken together, these results reveal novel information regarding the motifs that regulate mucolipin-1 trafficking and suggest a role for palmitoylation in protein sorting.","type":"Abstract"},{"text":"Palmitoylation mediates the association of the C-terminal tail of mucolipin-1 with membranes","type":"Results"},{"text":"These data suggest that the C565CC sequence is required for palmitoylation and subsequent association with membranes although the acidic di-leucine motif mediates localization at endosomes.","type":"Results"},{"text":"Together, our results suggest that the palmitoylation of the C-terminal tail of mucolipin-1 may play a role in regulating its trafficking possibly through bringing the endocytic signal closer to the plasma membrane, thus increasing the efficiency of endocytosis.","type":"Results"},{"text":"Therefore, we conclude that mucolipin-1 is palmitoylated in vivo and that Cys565, Cys566 and Cys567 account for the total palmitoylation of the protein.","type":"Results"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"enzymatic activity assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16497227","version":2,"reference_html":"Two di-leucine motifs regulate trafficking of mucolipin-1 to lysosomes. <i> Vergarajauregui S, Puertollano R. </i> Traffic, 2006","date":"2022-08-04T08:17:18.778Z","reference_source":"pmid","ec_id":"ECO:0005801","term_name":"palmitoylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-05T19:13:50.253Z"}},{"start":48,"end":59,"reference_id":"29019983","reference_source":"pmid","reference_html":"Human TRPML1 channel structures in open and closed conformations. <i> Schmiege P, Fine M, Blobel G, Li X. </i> Nature, 2017","date":"2022-08-04T08:29:37.193Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5WJ9"}],"region_id":"DP02757r007","statement":[{"text":"The apo TRPML1 at pH 7.0 was determined at 3.7 Å, representing a closed conformation; the ML-SA1-bound TRPML1 at pH 6.0 was determined at 3.5 Å, representing an open conformation (Extended Data Figs 2b, ​,33 and Extended Data Table 1).","type":"Results"},{"text":"The electron density is clearly resolved for residues 60–526 in the apo TRPML1 and residues 38–526 in the ML-SA1-bound TRPML1 (Extended Data Fig. 4), with the exception of a short linker in the luminal domain (amino acids 206–215).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-04T14:49:37.514Z"}}],"released":"2023_06","ncbi_taxon_id":9606,"disprot_id":"DP02757","date":"2020-04-14T13:39:59.648Z","organism":"Homo sapiens","regions_counter":7,"name":"Mucolipin-1","dataset":["NDDs-related proteins"],"UniParc":"UPI00000377A2","uniref100":"UniRef100_Q9GZU1","uniref90":"UniRef90_Q9GZU1","uniref50":"UniRef50_Q9GZU1","genes":[{"name":{"value":"MCOLN1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:13356","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:13356"}}]},"synonyms":[{"value":"ML4"},{"value":"TRPML1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"27623384","url":"http://www.ncbi.nlm.nih.gov/pubmed/27623384","alternativeUrl":"https://europepmc.org/abstract/MED/27623384"}}]}],"orfNames":[{"value":"MSTP080"}]}],"alphafold_very_low_content":0.12586206896551724,"disorder_content":0.2120689655172414,"disprot_consensus":{"full":[{"start":1,"end":47,"type":"D"},{"start":48,"end":59,"type":"T"},{"start":206,"end":215,"type":"D"},{"start":527,"end":580,"type":"D"}],"Structural state":[{"start":1,"end":59,"type":"D"},{"start":206,"end":215,"type":"D"},{"start":527,"end":580,"type":"D"}],"Disorder function":[{"start":206,"end":215,"type":"F"},{"start":564,"end":568,"type":"F"}],"Biological process":[{"start":573,"end":578,"type":"F"}],"Structural transition":[{"start":48,"end":59,"type":"T"}]}},{"acc":"Q13563","features":{"gene3D":[{"start":468,"end":540,"id":"G3DSA:1.20.120.350","name":"Voltage-gated potassium channels. Chain C"}],"pfam":[{"id":"PF08016","name":"Polycystin cation channel","start":464,"end":687},{"id":"PF18109","name":"Ferredoxin I 4Fe-4S cluster domain","start":834,"end":868},{"id":"PF20519","name":"Polycystin domain","start":269,"end":463}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MVNSSRVQPQQPGDAKRPPAPRAPDPGRLMAGCAAVGASLAAPGGLCEQRGLEIEMQRIRQAAARDPPAGAAASPSPPLSSCSRQAWSRDNPGFEAEEEEEEVEGEEGGMVVEMDVEWRPGSRRSAASSAVSSVGARSRGLGGYHGAGHPSGRRRRREDQGPPCPSPVGGGDPLHRHLPLEGQPPRVAWAERLVRGLRGLWGTRLMEESSTNREKYLKSVLRELVTYLLFLIVLCILTYGMMSSNVYYYTRMMSQLFLDTPVSKTEKTNFKTLSSMEDFWKFTEGSLLDGLYWKMQPSNQTEADNRSFIFYENLLLGVPRIRQLRVRNGSCSIPQDLRDEIKECYDVYSVSSEDRAPFGPRNGTAWIYTSEKDLNGSSHWGIIATYSGAGYYLDLSRTREETAAQVASLKKNVWLDRGTRATFIDFSVYNANINLFCVVRLLVEFPATGGVIPSWQFQPLKLIRYVTTFDFFLAACEIIFCFFIFYYVVEEILEIRIHKLHYFRSFWNCLDVVIVVLSVVAIGINIYRTSNVEVLLQFLEDQNTFPNFEHLAYWQIQFNNIAAVTVFFVWIKLFKFINFNRTMSQLSTTMSRCAKDLFGFAIMFFIIFLAYAQLAYLVFGTQVDDFSTFQECIFTQFRIILGDINFAEIEEANRVLGPIYFTTFVFFMFFILLNMFLAIINDTYSEVKSDLAQQKAEMELSDLIRKGYHKALVKLKLKKNTVDDISESLRQGGGKLNFDELRQDLKGKGHTDAEIEAIFTKYDQDGDQELTEHEHQQMRDDLEKEREDLDLDHSSLPRPMSSRSFPRSLDDSEEDDDEDSGHSSRRRGSISSGVSYEEFQVLVRRVDRMEHSIGSIVSKIDAVIVKLEIMERAKLKRREVLGRLLDGVAEDERLGRDSEIHREQMERLVREELERWESDDAASQISHGLGTPVGLNGQPRPRSSRPSSSQSTEGMEGAGGNGSSNVHV","length":968,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":215,"region_id":"DP02758r001","start":198,"term_id":"IDPO:0000002","statement":[{"text":"At 3.0 Å resolution, the cryo-EM map was of sufficient quality for de novo atomic model building in Coot (Emsley et al., 2010) except for the disordered N terminus (198–215), a loop (296–301) within the extracellular polycystin domain, S2–S3 loop (494–503), and C terminus (695–703).","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27768895","version":2,"reference_html":"The Structure of the Polycystic Kidney Disease Channel PKD2 in Lipid Nanodiscs. <i> Shen PS, Yang X, DeCaen PG, Liu X, Bulkley D, Clapham DE, Cao E. </i> Cell, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"5T4D"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":503,"region_id":"DP02758r002","start":494,"term_id":"IDPO:0000002","statement":[{"text":"At 3.0 Å resolution, the cryo-EM map was of sufficient quality for de novo atomic model building in Coot (Emsley et al., 2010) except for the disordered N terminus (198–215), a loop (296–301) within the extracellular polycystin domain, S2–S3 loop (494–503), and C terminus (695–703).","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27768895","version":2,"reference_html":"The Structure of the Polycystic Kidney Disease Channel PKD2 in Lipid Nanodiscs. <i> Shen PS, Yang X, DeCaen PG, Liu X, Bulkley D, Clapham DE, Cao E. </i> Cell, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"5T4D"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02758","date":"2020-04-14T13:52:17.941Z","organism":"Homo sapiens","regions_counter":2,"name":"Polycystin-2","dataset":[],"UniParc":"UPI0000131B69","uniref100":"UniRef100_Q13563","uniref90":"UniRef90_Q13563","uniref50":"UniRef50_Q13563","genes":[{"name":{"value":"PKD2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9009","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9009"}}]},"synonyms":[{"value":"TRPP2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"19556541","url":"http://www.ncbi.nlm.nih.gov/pubmed/19556541","alternativeUrl":"https://europepmc.org/abstract/MED/19556541"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9009","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9009"}}]}]}],"alphafold_very_low_content":0.29132231404958675,"disorder_content":0.028925619834710745,"disprot_consensus":{"full":[{"start":198,"end":215,"type":"D"},{"start":494,"end":503,"type":"D"}],"Structural state":[{"start":198,"end":215,"type":"D"},{"start":494,"end":503,"type":"D"}]}},{"acc":"Q14181","features":{"gene3D":[{"start":1,"end":78,"id":"G3DSA:1.10.8.530","name":"G3DSA:1.10.8.530"}],"pfam":[{"id":"PF04042","name":"DNA polymerase alpha/epsilon subunit B","start":342,"end":549},{"id":"PF08418","name":"DNA polymerase alpha subunit B N-terminal","start":6,"end":72},{"id":"PF22062","name":"DNA polymerase alpha subunit B, OB domain","start":217,"end":322}]},"creator":"lchemes","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MSASAQQLAEELQIFGLDCEEALIEKLVELCVQYGQNEEGMVGELIAFCTSTHKVGLTSEILNSFEHEFLSKRLSKARHSTCKDSGHAGARDIVSIQELIEVEEEEEILLNSYTTPSKGSQKRAISTPETPLTKRSVSTRSPHQLLSPSSFSPSATPSQKYNSRSNRGEVVTSFGLAQGVSWSGRGGAGNISLKVLGCPEALTGSYKSMFQKLPDIREVLTCKIEELGSELKEHYKIEAFTPLLAPAQEPVTLLGQIGCDSNGKLNNKSVILEGDREHSSGAQIPVDLSELKEYSLFPGQVVIMEGINTTGRKLVATKLYEGVPLPFYQPTEEDADFEQSMVLVACGPYTTSDSITYDPLLDLIAVINHDRPDVCILFGPFLDAKHEQVENCLLTSPFEDIFKQCLRTIIEGTRSSGSHLVFVPSLRDVHHEPVYPQPPFSYSDLSREDKKQVQFVSEPCSLSINGVIFGLTSTDLLFHLGAEEISSSSGTSDRFSRILKHILTQRSYYPLYPPQEDMAIDYESFYVYAQLPVTPDVLIIPSELRYFVKDVLGCVCVNPGRLTKGQVGGTFARLYLRRPAADGAERQSPCIAVQVVRI","length":598,"regions":[{"region_id":"DP02759r001","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:38:01.758Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":156,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"Both the NTD and an extended linker (residues 79–156) between the NTD and the PDE are not visible in crystal formation, pointing to the absence of stabilizing interactions with the PDE, the OB, and p180C. The only exception is molecule 2 residues 151–156 that are stabilized by interactions with the neighboring molecule","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2023_12","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"25847248","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4Y97"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lchemes","reference_html":"Crystal Structure of the Human Pol α B Subunit in Complex with the C-terminal Domain of the Catalytic Subunit. <i> Suwa Y, Gu J, Baranovskiy AG, Babayeva ND, Pavlov YI, Tahirov TH. </i> J Biol Chem, 2015","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02759r002","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:38:02.722Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":156,"term_id":"IDPO:0000033","start":79,"version":3,"statement":[{"text":"The N-terminal domain and the linker connecting it to the PDE domain are disordered in the reported crystal structure. ","type":"Abstract"},{"text":"Both the NTD and an extended linker (residues 79–156) between the NTD and the PDE are not visible in crystal formation, pointing to the absence of stabilizing interactions with the PDE, the OB, and p180C. The only exception is molecule 2 residues 151–156 that are stabilized by interactions with the neighboring molecule","type":"Results"},{"text":"In Prim-Pol α, the CTD-B subunit complex plays an additional and unique role by tethering two catalytic domains and regulating their activities (53).","type":"Discussion"}],"term_name":"flexible linker","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2023_12","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"25847248","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4Y97"}],"term_namespace":"Disorder function","ec_id":"ECO:0006220","curator_id":"lchemes","reference_html":"Crystal Structure of the Human Pol α B Subunit in Complex with the C-terminal Domain of the Catalytic Subunit. <i> Suwa Y, Gu J, Baranovskiy AG, Babayeva ND, Pavlov YI, Tahirov TH. </i> J Biol Chem, 2015","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2023_12","ncbi_taxon_id":9606,"disprot_id":"DP02759","date":"2020-04-14T20:58:17.251Z","organism":"Homo sapiens","regions_counter":3,"name":"DNA polymerase alpha subunit B","dataset":[],"UniParc":"UPI000012977B","uniref100":"UniRef100_Q14181","uniref90":"UniRef90_Q14181","uniref50":"UniRef50_Q14181","genes":[{"name":{"value":"POLA2"}}],"alphafold_very_low_content":0.09531772575250837,"disorder_content":0.2608695652173913,"disprot_consensus":{"full":[{"start":1,"end":156,"type":"D"}],"Structural state":[{"start":1,"end":156,"type":"D"}],"Disorder function":[{"start":79,"end":156,"type":"F"}]}},{"acc":"P76216","features":{"gene3D":[{"start":1,"end":447,"id":"G3DSA:3.75.10.20","name":"Succinylarginine dihydrolase"}],"pfam":[{"id":"PF04996","name":"Succinylarginine dihydrolase","start":3,"end":440}]},"creator":"lchemes","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"sequence":"MNAWEVNFDGLVGLTHHYAGLSFGNEASTRHRFQVSNPRLAAKQGLLKMKALADAGFPQAVIPPHERPFIPVLRQLGFSGSDEQVLEKVARQAPHWLSSVSSASPMWVANAATIAPSADTLDGKVHLTVANLNNKFHRSLEAPVTESLLKAIFNDEEKFSVHSALPQVALLGDEGAANHNRLGGHYGEPGMQLFVYGREEGNDTRPSRYPARQTREASEAVARLNQVNPQQVIFAQQNPDVIDQGVFHNDVIAVSNRQVLFCHQQAFARQSQLLANLRARVNGFMAIEVPATQVSVSDTVSTYLFNSQLLSRDDGSMMLVLPQECREHAGVWGYLNELLAADNPISELKVFDLRESMANGGGPACLRLRVVLTEEERRAVNPAVMMNDTLFNALNDWVDRYYRDRLTAADLADPQLLREGREALDVLSQLLNLGSVYPFQREGGGNG","length":447,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":34,"region_id":"DP02760r001","start":19,"term_id":"IDPO:0000002","statement":[{"text":"The only significant difference between the molecules is the conformation of a loop, Ala19–Gln34, which is largely disordered in the apo protein but becomes well ordered in the presence of bound substrate or product.","type":"Results"}],"curator_id":"vnugnes","released":"2025_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15703173","version":3,"reference_html":"Crystal structure of N-succinylarginine dihydrolase AstB, bound to substrate and product, an enzyme from the arginine catabolic pathway of Escherichia coli. <i> Tocilj A, Schrag JD, Li Y, Schneider BL, Reitzer L, Matte A, Cygler M. </i> J Biol Chem, 2005","date":"2025-11-19T18:35:44.270Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1YNF"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":49,"end":49,"position":"Specific residue","statements":[{"type":"Methods","text":"Selenomethionine-labeled protein was prepared by transforming the E. coli methionine auxotroph DL41(DE3) with the plasmid DNA, and the cells were grown in LeMaster medium supplemented with 25 mg/liter of l-selenomethionine for selenomethionine labeling (13)."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":106,"end":106,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":191,"end":191,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":285,"end":285,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":317,"end":317,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":318,"end":318,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":357,"end":357,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":385,"end":385,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":386,"end":386,"position":"Specific residue"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29103","entry_name":null}]},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":34,"region_id":"DP02760r002","start":19,"term_id":"IDPO:0000011","statement":[{"text":"Like other members of the AT superfamily of enzymes, AstB possesses a flexible loop that is disordered in the absence of substrate and assumes an ordered conformation upon substrate binding, shielding the ligand from the bulk solvent, thereby controlling substrate access and product release.","type":"Abstract"},{"text":"The only significant difference between the molecules is the conformation of a loop, Ala19–Gln34, which is largely disordered in the apo protein but becomes well ordered in the presence of bound substrate or product.","type":"Results"},{"text":"An electron density map calculated from diffraction data collected from this crystal revealed a well defined substrate molecule bound in the active site (Fig. 3a). As a result of substrate binding, all of the residues in the Ala19–Arg32 loop, which were disordered in the native crystal structures, were now clearly defined in electron density.","type":"Results"}],"curator_id":"vnugnes","released":"2025_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"15703173","version":3,"reference_html":"Crystal structure of N-succinylarginine dihydrolase AstB, bound to substrate and product, an enzyme from the arginine catabolic pathway of Escherichia coli. <i> Tocilj A, Schrag JD, Li Y, Schneider BL, Reitzer L, Matte A, Cygler M. </i> J Biol Chem, 2005","date":"2025-11-19T18:40:09.640Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1YNI"},{"db":"PDB","id":"1YNH"},{"db":"PDB","id":"1YNF"}],"term_name":"disorder to order","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29103","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"27574","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17705","entry_name":null}],"states_connection":[{"source":"DP02760r001","target":"DP02760r004"}]},{"start":19,"end":34,"reference_id":"15703173","reference_source":"pmid","reference_html":"Crystal structure of N-succinylarginine dihydrolase AstB, bound to substrate and product, an enzyme from the arginine catabolic pathway of Escherichia coli. <i> Tocilj A, Schrag JD, Li Y, Schneider BL, Reitzer L, Matte A, Cygler M. </i> J Biol Chem, 2005","date":"2025-11-19T18:39:42.023Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"PDB","id":"1YNI"},{"db":"PDB","id":"1YNH"}],"region_id":"DP02760r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29103","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"27574","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17705","entry_name":null}],"statement":[{"text":"An electron density map calculated from diffraction data collected from this crystal revealed a well defined substrate molecule bound in the active site (Fig. 3a). As a result of substrate binding, all of the residues in the Ala19–Arg32 loop, which were disordered in the native crystal structures, were now clearly defined in electron density.","type":"Results"}]}],"released":"2021_06","ncbi_taxon_id":83333,"disprot_id":"DP02760","date":"2020-04-15T05:03:56.200Z","organism":"Escherichia coli (strain K12)","regions_counter":4,"name":"N-succinylarginine dihydrolase","dataset":["Stress response proteins"],"UniParc":"UPI000003EB36","uniref100":"UniRef100_C4ZZA1","uniref90":"UniRef90_Q32G87","uniref50":"UniRef50_Q32G87","genes":[{"name":{"value":"astB"},"synonyms":[{"value":"ydjT"}],"olnNames":[{"value":"b1745"},{"value":"JW1734"}]}],"alphafold_very_low_content":0.008948545861297539,"disorder_content":0.035794183445190156,"disprot_consensus":{"full":[{"start":19,"end":34,"type":"T"}],"Structural state":[{"start":19,"end":34,"type":"D"}],"Structural transition":[{"start":19,"end":34,"type":"T"}]}},{"acc":"P25299","features":{"gene3D":[{"start":15,"end":111,"id":"G3DSA:3.30.70.330","name":"G3DSA:3.30.70.330"},{"start":253,"end":290,"id":"G3DSA:1.10.20.70","name":"G3DSA:1.10.20.70"}],"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":20,"end":90},{"id":"PF14304","name":"Transcription termination and cleavage factor C-terminal","start":254,"end":291}]},"creator":"lchemes","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"sequence":"MNRQSGVNAGVQNNPPSRVVYLGSIPYDQTEEQILDLCSNVGPVINLKMMFDPQTGRSKGYAFIEFRDLESSASAVRNLNGYQLGSRFLKCGYSSNSDISGVSQQQQQQYNNINGNNNNNGNNNNNSNGPDFQNSGNANFLSQKFPELPSGIDVNINMTTPAMMISSELAKKPKEVQLKFLQKFQEWTRAHPEDAVSLLELCPQLSFVTAELLLTNGICKVDDLIPLASRPQEEASATNNNSVNEVVDPAVLNKQKELLKQVLQLNDSQISILPDDERMAIWDLKQKALRGEFGAF","length":296,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":232,"region_id":"DP02761r001","start":127,"term_id":"IDPO:0000002","statement":[{"text":"By CD spectroscopy, each of these isolated peptides is minimally folded (Figure 1B), with only minor indication of a thermal denaturation unfolding transition for His6-Rna15p(127–232). NMR spectroscopy data are also consistent with peptides that are either unfolded or in a heterogeneous molten-globule state (Figure 1C). This is evident by the poor dispersion in the 1H chemical shift values as is seen with disordered peptides","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"21481776","version":2,"reference_html":"Locked tether formation by cooperative folding of Rna14p monkeytail and Rna15p hinge domains in the yeast CF IA complex. <i> Moreno-Morcillo M, Moreno-Morcillo M, Minvielle-Sébastia L, Fribourg S, Mackereth CD. </i> Structure, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"2L9B"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":232,"region_id":"DP02761r002","start":127,"term_id":"IDPO:0000002","statement":[{"text":"By CD spectroscopy, each of these isolated peptides is minimally folded (Figure 1B), with only minor indication of a thermal denaturation unfolding transition for His6-Rna15p(127–232). NMR spectroscopy data are also consistent with peptides that are either unfolded or in a heterogeneous molten-globule state (Figure 1C). This is evident by the poor dispersion in the 1H chemical shift values as is seen with disordered peptides","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"21481776","version":2,"reference_html":"Locked tether formation by cooperative folding of Rna14p monkeytail and Rna15p hinge domains in the yeast CF IA complex. <i> Moreno-Morcillo M, Moreno-Morcillo M, Minvielle-Sébastia L, Fribourg S, Mackereth CD. </i> Structure, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","cross_refs":[{"db":"PDB","id":"2L9B"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":232,"region_id":"DP02761r003","start":127,"term_id":"IDPO:0000011","statement":[{"text":"The C-terminal monkeytail domain from Rna14p and the hinge region from Rna15p display a coupled binding and folding mechanism, where both peptides are initially disordered. ","type":"Abstract"},{"text":"Excellent stability and evidence of a single well-folded complex by nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy is seen with samples from bacterially coexpressed Rna14p(626–677)/Rna15p(127–232)","type":"Results"},{"text":"The authors show that while the individual Rna15p and Rna14p proteins are disordered and show low NMR dispersion, the co-expressed complex is folded and has a highly dispersed spectrum (Figure 1C)","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"21481776","version":2,"reference_html":"Locked tether formation by cooperative folding of Rna14p monkeytail and Rna15p hinge domains in the yeast CF IA complex. <i> Moreno-Morcillo M, Moreno-Morcillo M, Minvielle-Sébastia L, Fribourg S, Mackereth CD. </i> Structure, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"2L9B"}],"term_name":"disorder to order","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":232,"region_id":"DP02761r004","start":127,"term_id":"GO:0005515","statement":[{"text":"Excellent stability and evidence of a single well-folded complex by nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy is seen with samples from bacterially coexpressed Rna14p(626–677)/Rna15p(127–232)","type":"Results"},{"text":"The authors show that while the individual Rna15p and Rna14p proteins are disordered and show low NMR dispersion, the co-expressed complex is folded and has a highly dispersed spectrum (Figure 1C)","type":"Curator statement"},{"text":"Genetic data confirm that mutation of residues within the minimal heterodimer region inhibit association of full-length Rna14p and Rna15p.","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"21481776","version":3,"reference_html":"Locked tether formation by cooperative folding of Rna14p monkeytail and Rna15p hinge domains in the yeast CF IA complex. <i> Moreno-Morcillo M, Moreno-Morcillo M, Minvielle-Sébastia L, Fribourg S, Mackereth CD. </i> Structure, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"2L9B"}],"term_name":"protein binding","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":232,"region_id":"DP02761r005","start":127,"term_id":"GO:0060090","statement":[{"text":"Mutants with destabilized monkeytail-hinge interactions prevent association of Rna15p within CF IA. Conservation of interdomain residues reveals that the structural tethering is preserved in the homologous mammalian ... proteins of the CstF complex.","type":"Abstract"},{"text":"The interaction between the monkeytail and hinge domains creates a high affinity link that joins Rna14p and Rna15p together in a tight complex, and from sequence analysis a similar tether is likely formed between the metazoan orthologs","type":"Discussion"},{"text":"Using TAP-tag purification we have found that the loss of this tether specifically results in a separation of Rna15p from CF IA.","type":"Discussion"},{"text":"Most importantly, without Rna15p the RRM domain is no longer present in the CF IA complex, causing loss of specific RNA-binding for CF IA, even though the RRM domain itself is not directly affected by either mutation.","type":"Discussion"}],"curator_id":"lchemes","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"21481776","version":3,"reference_html":"Locked tether formation by cooperative folding of Rna14p monkeytail and Rna15p hinge domains in the yeast CF IA complex. <i> Moreno-Morcillo M, Moreno-Morcillo M, Minvielle-Sébastia L, Fribourg S, Mackereth CD. </i> Structure, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"2L9B"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":559292,"disprot_id":"DP02761","date":"2020-04-15T06:25:05.610Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":5,"name":"mRNA 3'-end-processing protein RNA15","dataset":[],"UniParc":"UPI0000052DDF","uniref100":"UniRef100_P25299","uniref90":"UniRef90_P25299","uniref50":"UniRef50_P25299","genes":[{"name":{"value":"RNA15"},"olnNames":[{"value":"YGL044C"}]}],"alphafold_very_low_content":0.20608108108108109,"disorder_content":0.3581081081081081,"disprot_consensus":{"full":[{"start":127,"end":232,"type":"T"}],"Structural state":[{"start":127,"end":232,"type":"D"}],"Structural transition":[{"start":127,"end":232,"type":"T"}],"Molecular function":[{"start":127,"end":232,"type":"F"}]}},{"acc":"Q9VI75","features":{"gene3D":[{"start":1,"end":161,"id":"G3DSA:1.25.40.90","name":"G3DSA:1.25.40.90"},{"start":160,"end":308,"id":"G3DSA:1.20.58.150","name":"G3DSA:1.20.58.150"}],"pfam":[{"id":"PF07651","name":"ANTH domain","start":24,"end":297}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"sequence":"MTMAGQTINDRLLAARHSLAGQGLAKSVCKATTEECIGPKKKHLDYLVHCTNEPNVSIPHLANLLIERSQNANWVVVYKSLITTHHLMAYGNERFMQYLASSNSTFNLSSFLDKGTVQDGGMGVPGGRMGYDMSPFIRRYAKYLNEKSLSYRAMAFDFCKVKRGKEEGSLRSMNAEKLLKTLPVLQAQLDALLEFDCQSNDLSNGVINMSFMLLFRDLIRLFACYNDGIINLLEKYFDMNKKHARDALDLYKKFLVRMDRVGEFLKVAENVGIDKGDIPDLTKAPSSLLDALEQHLATLEGRKVSAANTPTQSSSSAFGTAAASSKFDTTNGIDEQLKAQVLAEEEAAMNQYKSKVSSPTSSGAAGASAALTNPFLSSPPAAQAGQPIVDLFGAASAQPAAAAAATKASDDLLQLGNPFADMFDASGGGAAAVGATGNAGDGTAKYDGGAGSSPFDWGATDDDGGAAQ","length":468,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":21,"region_id":"DP02763r001","start":4,"term_id":"IDPO:0000002","statement":[{"text":"As the residues in segments at the N-terminal end (4–21) and in two long loops (117–119 and 163–166) and the last two residues have weak or uninterpretable densities, they were assumed to be flexible.","type":"Methods"},{"text":"The crystal structure of the NAP domain (residues 4–301) was determined by the multiple anomalous dispersion (MAD) phasing technique (Experimental Procedures and Table 1) . The structure, missing the first eighteen disordered residues, is composed entirely of ten α helices and connecting loops, all of varying lengths.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11239400","version":2,"reference_html":"A novel all helix fold of the AP180 amino-terminal domain for phosphoinositide binding and clathrin assembly in synaptic vesicle endocytosis. <i> Mao Y, Chen J, Maynard JA, Zhang B, Quiocho FA. </i> Cell, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1HX8"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","ncbi_taxon_id":7227,"disprot_id":"DP02763","date":"2020-04-15T09:14:17.201Z","organism":"Drosophila melanogaster","regions_counter":2,"name":"Phosphatidylinositol-binding clathrin assembly protein LAP","dataset":[],"UniParc":"UPI000007F038","uniref100":"UniRef100_Q9VI75","uniref90":"UniRef90_Q9VI75","uniref50":"UniRef50_Q9VI75","genes":[{"name":{"value":"lap"},"orfNames":[{"value":"CG2520"}]}],"alphafold_very_low_content":0.32264957264957267,"disorder_content":0.038461538461538464,"disprot_consensus":{"full":[{"start":4,"end":21,"type":"D"}],"Structural state":[{"start":4,"end":21,"type":"D"}]}},{"acc":"Q13162","features":{"gene3D":[{"start":75,"end":271,"id":"G3DSA:3.40.30.10","name":"Glutaredoxin"}],"pfam":[{"id":"PF00578","name":"AhpC/TSA family","start":82,"end":213},{"id":"PF10417","name":"C-terminal domain of 1-Cys peroxiredoxin","start":234,"end":261}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MEALPLLAATTPDHGRHRRLLLLPLLLFLLPAGAVQGWETEERPRTREEECHFYAGGQVYPGEASRVSVADHSLHLSKAKISKPAPYWEGTAVIDGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRLEEFRSINTEVVACSVDSQFTHLAWINTPRRQGGLGPIRIPLLSDLTHQISKDYGVYLEDSGHTLRGLFIIDDKGILRQITLNDLPVGRSVDETLRLVQAFQYTDKHGEVCPAGWKPGSETIIPDPAGKLKYFDKLN","length":271,"regions":[{"term_namespace":"Molecular function","ec_ontology":"ECO","end":75,"region_id":"DP02764r001","start":1,"term_id":"GO:0060090","statement":[{"text":"However, in the full-length Prx4 structure, the N-terminal 1–37 residues were invisible (which was not due to degradation; results not shown) and residues 38–46 adopt an unwound loop. Thus this region was proposed to be flexible and exposed to the solvent.","type":"Results"},{"text":"In contrast, oxidized Prx4 exists in a rather stable decameric form, probably stabilized by its unique flexible N-terminal region.","type":"Discussion"},{"text":"The mutant Prx4-ΔN, lacking the N-terminal 46 residues, was predominantly a decamer in a reduced state, but partially dissociated into dimers especially at lower concentrations after reaction with H2O2, suggesting that the flexible N-terminal region may play a role in stabilization of the Prx4 decamer in the oxidized state.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"21916849","version":3,"reference_html":"Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4. <i> Wang X, Wang L, Wang X, Sun F, Wang CC. </i> Biochem J, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3TKQ"},{"db":"PDB","id":"3TKP"},{"db":"PDB","id":"3TKS"},{"db":"PDB","id":"3TKR"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":75,"region_id":"DP02764r002","start":1,"term_id":"IDPO:0000002","statement":[{"text":"However, in the full-length Prx4 structure, the N-terminal 1–37 residues were invisible (which was not due to degradation; results not shown) and residues 38–46 adopt an unwound loop. Thus this region was proposed to be flexible and exposed to the solvent.","type":"Results"},{"text":"In contrast, oxidized Prx4 exists in a rather stable decameric form, probably stabilized by its unique flexible N-terminal region.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21916849","version":2,"reference_html":"Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4. <i> Wang X, Wang L, Wang X, Sun F, Wang CC. </i> Biochem J, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3TKQ"},{"db":"PDB","id":"3TKP"},{"db":"PDB","id":"3TKS"},{"db":"PDB","id":"3TKR"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":271,"region_id":"DP02764r003","start":1,"term_id":"GO:0140313","statement":[{"text":"The second-order rate constant for the reaction of Prx4 with H2O2 was determined to be 2.2 × 107 M−1·s−1 (Figure 6A), indicating that Prx4 can remove H2O2 as efficiently as haem or selenium peroxidases and other Prxs do.","type":"Results"},{"text":"The peroxidase activity was also monitored in a reaction coupled to NADPH oxidation (Figure 6B). NADPH was oxidized with an initial reaction rate of ~1 μM·s−1 in the presence of 2.5 μM Prx4 and 50 μM H2O2, the minimal amount for quantitatively monitoring the reaction in practice. When the H2O2 concentrations increased, the oxidation rate of NADPH decreased, indicating loss of peroxidase activity of Prx4.","type":"Results"},{"text":"Overoxidation of wild-type Prx4 intensified with increasing H2O2 concentrations, whereas the overoxidation of Prx4-ΔC and Prx4-T118E remained negligible, with a faint increase only at 500 μM H2O2.","type":"Results"},{"text":"Prx4 (peroxiredoxin 4) is the only peroxiredoxin located in the ER (endoplasmic reticulum) and a proposed scavenger for H2O2. In the present study, we solved crystal structures of human Prx4 in three different redox forms and characterized the reaction features of Prx4 with H2O2.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"enzymatic activity assay evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"21916849","version":3,"reference_html":"Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4. <i> Wang X, Wang L, Wang X, Sun F, Wang CC. </i> Biochem J, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005801","term_name":"molecular sequestering activity","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02764","date":"2020-04-15T10:52:12.261Z","organism":"Homo sapiens","regions_counter":3,"name":"Peroxiredoxin-4","dataset":[],"UniParc":"UPI00001314E8","uniref100":"UniRef100_Q13162","uniref90":"UniRef90_Q13162","uniref50":"UniRef50_Q13162","genes":[{"name":{"value":"PRDX4"}}],"alphafold_very_low_content":0.22140221402214022,"disorder_content":0.2767527675276753,"disprot_consensus":{"full":[{"start":1,"end":75,"type":"D"},{"start":76,"end":271,"type":"F"}],"Structural state":[{"start":1,"end":75,"type":"D"}],"Molecular function":[{"start":1,"end":271,"type":"F"}]}},{"acc":"Q14118","features":{"gene3D":[{"start":492,"end":603,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":492,"end":603,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":181,"end":315,"id":"G3DSA:3.30.70.1040","name":"Dystroglycan, domain 2"}],"pfam":[{"id":"PF05345","name":"Putative Ig domain","start":62,"end":140},{"id":"PF05454","name":"Dystroglycan domain 4","start":607,"end":715},{"id":"PF18424","name":"Alpha-Dystroglycan N-terminal domain 2","start":182,"end":304},{"id":"PF29962","name":"Alpha-Dystroglycan third Ig-like domain","start":493,"end":596}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MRMSVGLSLLLPLSGRTFLLLLSVVMAQSHWPSEPSEAVRDWENQLEASMHSVLSDLHEAVPTVVGIPDGTAVVGRSFRVTIPTDLIASSGDIIKVSAAGKEALPSWLHWDSQSHTLEGLPLDTDKGVHYISVSATRLGANGSHIPQTSSVFSIEVYPEDHSELQSVRTASPDPGEVVSSACAADEPVTVLTVILDADLTKMTPKQRIDLLHRMRSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQNSVPDIHGVEAPAREGAMSAQLGYPVVGWHIANKKPPLPKRVRRQIHATPTPVTAIGPPTTAIQEPPSRIVPTPTSPAIAPPTETMAPPVRDPVPGKPTVTIRTRGAIIQTPTLGPIQPTRVSEAGTTVPGQIRPTMTIPGYVEPTAVATPPTTTTKKPRVSTPKPATPSTDSTTTTTRRPTKKPRTPRPVPRVTTKVSITRLETASPPTRIRTTTSGVPRGGEPNQRPELKNHIDRVDAWVGTYFEVKIPSDTFYDHEDTTTDKLKLTLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFMHATDKGGLSAVDAFEIHVHRRPQGDRAPARFKAKFVGDPALVLNDIHKKIALVKKLAFAFGDRNCSTITLQNITRGSIVVEWTNNTLPLEPCPKEQIAGLSRRIAEDDGKPRPAFSNALEPDFKATSITVTGSGSCRHLQFIPVVPPRRVPSEAPPTEVPDRDPEKSSEDDVYLHTVIPAVVVAAILLIAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSVPETTPLNQDTMGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP","length":895,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":179,"region_id":"DP02765r001","start":163,"term_id":"IDPO:0000002","statement":[{"text":"Upon completion of the crystallographic refinement, the final R‐factor was 0.163 (R‐free = 0.195), with residues 52–60, 163–179, and 305–315 missing in the final model as no reliable electron density could be detected for these regions.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28781947","version":2,"reference_html":"Structural flexibility of human α-dystroglycan. <i> Covaceuszach S, Bozzi M, Bigotti MG, Sciandra F, Konarev PV, Brancaccio A, Cassetta A. </i> FEBS Open Bio, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5LLK"}],"term_name":"disorder","validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-04-26T16:22:10.323Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":179,"region_id":"DP02765r002","start":163,"term_id":"IDPO:0000033","statement":[{"text":"Upon completion of the crystallographic refinement, the final R‐factor was 0.163 (R‐free = 0.195), with residues 52–60, 163–179, and 305–315 missing in the final model as no reliable electron density could be detected for these regions.","type":"Results"},{"text":"The hα‐DG‐Nt and mα‐DG‐Nt crystal structures display the most significant structural differences in the flexible linker (see Fig. S2A,B) connecting the Ig‐like and S6 domains.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28781947","version":4,"reference_html":"Structural flexibility of human α-dystroglycan. <i> Covaceuszach S, Bozzi M, Bigotti MG, Sciandra F, Konarev PV, Brancaccio A, Cassetta A. </i> FEBS Open Bio, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5LLK"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-14T08:13:15.076Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":305,"end":315,"reference_id":"28781947","reference_source":"pmid","reference_html":"Structural flexibility of human α-dystroglycan. <i> Covaceuszach S, Bozzi M, Bigotti MG, Sciandra F, Konarev PV, Brancaccio A, Cassetta A. </i> FEBS Open Bio, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5LLK"}],"region_id":"DP02765r003","statement":[{"text":"Upon completion of the crystallographic refinement, the final R‐factor was 0.163 (R‐free = 0.195), with residues 52–60, 163–179, and 305–315 missing in the final model as no reliable electron density could be detected for these regions.","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-14T08:11:46.660Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":163,"end":179,"reference_id":"28781947","reference_source":"pmid","reference_html":"Structural flexibility of human α-dystroglycan. <i> Covaceuszach S, Bozzi M, Bigotti MG, Sciandra F, Konarev PV, Brancaccio A, Cassetta A. </i> FEBS Open Bio, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP02765r004","statement":[{"text":"The Rg distributions of these ensembles (Fig. 7, solid lines) are very similar to each other and nearly as broad as the distribution of randomly generated models (Fig. 7, dashed lines), supporting the hypothesis of a certain degree of interdomain flexibility.","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-14T08:13:54.537Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":163,"end":179,"reference_id":"28781947","reference_source":"pmid","reference_html":"Structural flexibility of human α-dystroglycan. <i> Covaceuszach S, Bozzi M, Bigotti MG, Sciandra F, Konarev PV, Brancaccio A, Cassetta A. </i> FEBS Open Bio, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP02765r005","statement":[{"text":"The Rg distributions of these ensembles (Fig. 7, solid lines) are very similar to each other and nearly as broad as the distribution of randomly generated models (Fig. 7, dashed lines), supporting the hypothesis of a certain degree of interdomain flexibility.","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-14T08:13:56.356Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2020_12","ncbi_taxon_id":9606,"disprot_id":"DP02765","date":"2020-04-15T11:44:05.074Z","organism":"Homo sapiens","regions_counter":5,"name":"Dystroglycan","dataset":["Extracellular matrix proteins","NDDs-related proteins"],"UniParc":"UPI000013EDAE","uniref100":"UniRef100_Q14118","uniref90":"UniRef90_Q14118","uniref50":"UniRef50_Q14118","genes":[{"name":{"value":"DAG1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:2666","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:2666"}}]}}],"alphafold_very_low_content":0.358659217877095,"disorder_content":0.03128491620111732,"disprot_consensus":{"full":[{"start":163,"end":179,"type":"D"},{"start":305,"end":315,"type":"D"}],"Structural state":[{"start":163,"end":179,"type":"D"},{"start":305,"end":315,"type":"D"}],"Disorder function":[{"start":163,"end":179,"type":"F"}]}},{"acc":"P15442","features":{"gene3D":[{"start":1,"end":138,"id":"G3DSA:3.10.110.10","name":"Ubiquitin Conjugating Enzyme"},{"start":1388,"end":1493,"id":"G3DSA:3.40.50.800","name":"Anticodon-binding domain"}],"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":299,"end":526},{"id":"PF00069","name":"Protein kinase domain","start":599,"end":669},{"id":"PF00069","name":"Protein kinase domain","start":748,"end":981},{"id":"PF05773","name":"RWD domain","start":13,"end":125},{"id":"PF12745","name":"Anticodon binding domain of tRNAs","start":1387,"end":1657},{"id":"PF13393","name":"Histidyl-tRNA synthetase","start":1075,"end":1356}]},"creator":"fquaglia","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"sequence":"MSLSHLTLDQYYEIQCNELEAIRSIYMDDFTDLTKRKSSWDKQPQIIFEITLRSVDKEPVESSITLHFAMTPMYPYTAPEIEFKNVQNVMDSQLQMLKSEFKKIHNTSRGQEIIFEITSFTQEKLDEFQNVVNTQSLEDDRLQRIKETKEQLEKEEREKQQETIKKRSDEQRRIDEIVQRELEKRQDDDDDLLFNRTTQLDLQPPSEWVASGEAIVFSKTIKAKLPNNSMFKFKAVVNPKPIKLTSDIFSFSKQFLVKPYIPPESPLADFLMSSEMMENFYYLLSEIELDNSYFNTSNGKKEIANLEKELETVLKAKHDNVNRLFGYTVERMGRNNATFVWKIRLLTEYCNYYPLGDLIQSVGFVNLATARIWMIRLLEGLEAIHKLGIVHKCINLETVILVKDADFGSTIPKLVHSTYGYTVLNMLSRYPNKNGSSVELSPSTWIAPELLKFNNAKPQRLTDIWQLGVLFIQIISGSDIVMNFETPQEFLDSTSMDETLYDLLSKMLNNDPKKRLGTLELLPMKFLRTNIDSTINRFNLVSESVNSNSLELTPGDTITVRGNGGRTLSQSSIRRRSFNVGSRFSSINPATRSRYASDFEEIAVLGQGAFGQVVKARNALDSRYYAIKKIRHTEEKLSTILSEVMLLASLNHQYVVRYYAAWLEEDSMDENVFESTDEESDLSESSSDFEENDLLDQSSIFKNRTNHDLDNSNWDFISGSGYPDIVFENSSRDDENEDLDHDTSSTSSSESQDDTDKESKSIQNVPRRRNFVKPMTAVKKKSTLFIQMEYCENRTLYDLIHSENLNQQRDEYWRLFRQILEALSYIHSQGIIHRDLKPMNIFIDESRNVKIGDFGLAKNVHRSLDILKLDSQNLPGSSDNLTSAIGTAMYVATEVLDGTGHYNEKIDMYSLGIIFFEMIYPFSTGMERVNILKKLRSVSIEFPPDFDDNKMKVEKKIIRLLIDHDPNKRPGARTLLNSGWLPVKHQDEVIKEALKSLSNPSSPWQQQVRESLFNQSYSLTNDILFDNSVPTSTPFANILRSQMTEEVVKIFRKHGGIENNAPPRIFPKAPIYGTQNVYEVLDKGGTVLQLQYDLTYPMARYLSKNPSLISKQYRMQHVYRPPDHSRSSLEPRKFGEIDFDIISKSSSESGFYDAESLKIIDEILTVFPVFEKTNTFFILNHADILESVFNFTNIDKAQRPLVSRMLSQVGFARSFKEVKNELKAQLNISSTALNDLELFDFRLDFEAAKKRLYKLMIDSPHLKKIEDSLSHISKVLSYLKPLEVARNVVISPLSNYNSAFYKGGIMFHAVYDDGSSRNMIAAGGRYDTLISFFARPSGKKSSNTRKAVGFNLAWETIFGIAQNYFKLASGNRIKKRNRFLKDTAVDWKPSRCDVLISSFSNSLLDTIGVTILNTLWKQNIKADMLRDCSSVDDVVTGAQQDGIDWILLIKQQAYPLTNHKRKYKPLKIKKLSTNVDIDLDLDEFLTLYQQETGNKSLINDSLTLGDKADEFKRWDENSSAGSSQEGDIDDVVAGSTNNQKVIYVPNMATRSKKANKREKWVYEDAARNSSNMILHNLSNAPIITVDALRDETLEIISITSLAQKEEWLRKVFGSGNNSTPRSFATSIYNNLSKEAHKGNRWAILYCHKTGKSSVIDLQR","length":1659,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":951,"region_id":"DP02767r001","start":921,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"A segment between αF and αH (residues 921-951) exhibits high B-factors, consistent with disorder.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15964839","version":2,"reference_html":"Structural basis for autoinhibition and mutational activation of eukaryotic initiation factor 2alpha protein kinase GCN2. <i> Padyana AK, Qiu H, Roll-Mecak A, Hinnebusch AG, Burley SK. </i> J Biol Chem, 2005","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-06T14:07:09.448Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":882,"region_id":"DP02767r004","start":861,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Approximately 22 residues at the center of the activation loop (residues 861-882) appear disordered and are invisible in experimental electron density maps (Figs. 1b and 2a). ","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15964839","version":2,"reference_html":"Structural basis for autoinhibition and mutational activation of eukaryotic initiation factor 2alpha protein kinase GCN2. <i> Padyana AK, Qiu H, Roll-Mecak A, Hinnebusch AG, Burley SK. </i> J Biol Chem, 2005","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1ZYD"},{"db":"PDB","id":"1ZYC"},{"db":"PDB","id":"1ZY5"},{"db":"PDB","id":"1ZY4"},{"db":"PDB","id":"1ZXE"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-06T14:02:20.014Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":882,"region_id":"DP02767r005","start":861,"term_id":"IDPO:0000045","unpublished":true,"statement":[{"text":"Approximately 22 residues at the center of the activation loop (residues 861-882) appear disordered and are invisible in experimental electron density maps (Figs. 1b and 2a). ","type":"Results"},{"text":"Autophosphorylation sites within the activation segment, Thr887 and Thr882 (42), are not phosphorylated in any of the purified proteins used for crystallization","type":"Results"},{"text":"The activating mutations R794G and F842L lead to increased autophosphorylation of the GCN2 activation loop (Fig. 4a), and there is genetic evidence that phosphorylation of both Thr887 and Thr882 in this loop is required for full activity even in the presence of these GCN2c mutations","type":"Discussion"},{"text":"Subsequent autophosphorylation of the activation loop is predicted to facilitate an additional realignment of active site residues necessary for substrate phosphorylation.","type":"Introduction"}],"curator_id":"fquaglia","released":"2024_06","ec_name":"protein kinase assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15964839","version":3,"reference_html":"Structural basis for autoinhibition and mutational activation of eukaryotic initiation factor 2alpha protein kinase GCN2. <i> Padyana AK, Qiu H, Roll-Mecak A, Hinnebusch AG, Burley SK. </i> J Biol Chem, 2005","date":"2024-03-04T15:39:12.901Z","reference_source":"pmid","ec_id":"ECO:0007687","term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-04T15:41:57.290Z"}},{"start":1519,"end":1537,"reference_id":"24719324","reference_source":"pmid","reference_html":"Crystal structures of GCN2 protein kinase C-terminal domains suggest regulatory differences in yeast and mammals. <i> He H, Singh I, Wek SA, Dey S, Baird TD, Wek RC, Georgiadis MM. </i> J Biol Chem, 2014","date":"2022-10-06T14:19:25.143Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02767r006","statement":[{"text":"The mCTD structural model includes residues 1530–1648 for the A chain and 1526–1648 for the B chain; the yCTD includes residues 1537–1549 and 1559–1659 for the A chain and residues 1538–1555 and 1560–1659 for the B chain. Missing residues in yCTD are disordered and correspond to the connecting loop region between the N-terminal β-strand and α-helix.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"4OTM"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-04T15:41:38.112Z"}},{"start":1519,"end":1537,"reference_id":"24719324","reference_source":"pmid","reference_html":"Crystal structures of GCN2 protein kinase C-terminal domains suggest regulatory differences in yeast and mammals. <i> He H, Singh I, Wek SA, Dey S, Baird TD, Wek RC, Georgiadis MM. </i> J Biol Chem, 2014","date":"2022-10-06T14:19:59.114Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4OTM"}],"region_id":"DP02767r007","statement":[{"text":"The mCTD structural model includes residues 1530–1648 for the A chain and 1526–1648 for the B chain; the yCTD includes residues 1537–1549 and 1559–1659 for the A chain and residues 1538–1555 and 1560–1659 for the B chain. Missing residues in yCTD are disordered and correspond to the connecting loop region between the N-terminal β-strand and α-helix.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-04T15:41:43.070Z"}},{"start":665,"end":767,"reference_id":"15964839","reference_source":"pmid","reference_html":"Structural basis for autoinhibition and mutational activation of eukaryotic initiation factor 2alpha protein kinase GCN2. <i> Padyana AK, Qiu H, Roll-Mecak A, Hinnebusch AG, Burley SK. </i> J Biol Chem, 2005","date":"2022-10-06T14:33:25.017Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001191","ec_ontology":"ECO","ec_name":"in vitro cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02767r008","statement":[{"text":"The GCN2 fragment (from S. cerevisiae) encompassing residues 594-997 with deleted segment 665-767, and the same fragments bearing the D835N or R794G mutations, were expressed in Escherichia coli BL21(DE3*) cells as N-terminal His6-Smt3 fusion proteins (26) using a pET26b-derived expression vector (both S- and Se-methionine forms).","type":"Methods"},{"text":"Limited proteolysis/mass spectrometry studies of the GCN2 PK domain (residues 593-998) confirmed the presence of a large (102 residue) proteolytically sensitive insert that is poorly conserved among GCN2 homologs (Fig. 1b).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-04T15:41:40.903Z"}}],"released":"2023_12","ncbi_taxon_id":559292,"disprot_id":"DP02767","date":"2020-04-15T13:25:38.939Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":8,"name":"eIF-2-alpha kinase GCN2","dataset":["RNA-binding proteins","Stress response proteins"],"UniParc":"UPI000012B2E6","uniref100":"UniRef100_P15442","uniref90":"UniRef90_P15442","uniref50":"UniRef50_P15442","genes":[{"name":{"value":"GCN2","evidences":[{"code":"ECO:0000312","source":{"name":"SGD","id":"S000002691","url":"https://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000002691"}}]},"synonyms":[{"value":"AAS1","evidences":[{"code":"ECO:0000312","source":{"name":"SGD","id":"S000002691","url":"https://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000002691"}}]}],"olnNames":[{"value":"YDR283C"}]}],"alphafold_very_low_content":0.1723930078360458,"disorder_content":0.10548523206751055,"disprot_consensus":{"full":[{"start":665,"end":767,"type":"D"},{"start":861,"end":882,"type":"D"},{"start":921,"end":951,"type":"D"},{"start":1519,"end":1537,"type":"D"}],"Structural state":[{"start":665,"end":767,"type":"D"},{"start":861,"end":882,"type":"D"},{"start":921,"end":951,"type":"D"},{"start":1519,"end":1537,"type":"D"}],"Disorder function":[{"start":861,"end":882,"type":"F"},{"start":1519,"end":1537,"type":"F"}]}},{"acc":"P09950","features":{"gene3D":[{"start":130,"end":386,"id":"G3DSA:3.40.640.10","name":"Type I PLP-dependent aspartate aminotransferase-like (Major domain)"},{"start":84,"end":476,"id":"G3DSA:3.90.1150.10","name":"Aspartate Aminotransferase, domain 1"}],"pfam":[{"id":"PF00155","name":"Aminotransferase class I and II","start":114,"end":479}]},"creator":"fquaglia","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"sequence":"MQRSIFARFGNSSAAVSTLNRLSTTAAPHAKNGYATATGAGAAAATATASSTHAAAAAAAAANHSTQESGFDYEGLIDSELQKKRLDKSYRYFNNINRLAKEFPLAHRQREADKVTVWCSNDYLALSKHPEVLDAMHKTIDKYGCGAGGTRNIAGHNIPTLNLEAELATLHKKEGALVFSSCYVANDAVLSLLGQKMKDLVIFSDELNHASMIVGIKHANVKKHIFKHNDLNELEQLLQSYPKSVPKLIAFESVYSMAGSVADIEKICDLADKYGALTFLDEVHAVGLYGPHGAGVAEHCDFESHRASGIATPKTNDKGGAKTVMDRVDMITGTLGKSFGSVGGYVAASRKLIDWFRSFAPGFIFTTTLPPSVMAGATAAIRYQRCHIDLRTSQQKHTMYVKKAFHELGIPVIPNPSHIVPVLIGNADLAKQASDILINKHQIYVQAINFPTVARGTERLRITPTPGHTNDLSDILINAVDDVFNELQLPRVRDWESQGGLLGVGESGFVEESNLWTSSQLSLTNDDLNPNVRDPIVKQLEVSSGIKQ","length":548,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":71,"region_id":"DP02768r001","start":58,"term_id":"IDPO:0000002","statement":[{"text":"The variant used for crystallization lacked the mitochondrial targeting sequence (residues 1–57, (Vogtle et al., 2009)), and the first 13 residues of the mature N-terminus were disordered in the final refined structure.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29551290","version":2,"reference_html":"Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme. <i> Brown BL, Kardon JR, Sauer RT, Baker TA. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5TXT"},{"db":"PDB","id":"5TXR"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":113,"region_id":"DP02768r002","start":83,"term_id":"IDPO:0000002","statement":[{"text":"NT (near the mature N-terminus, residues 83–113) was only ordered in subunit B. NTB includes part of helix α1, an extended loop, strand β1, and the loop leading to β2.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29551290","version":2,"reference_html":"Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme. <i> Brown BL, Kardon JR, Sauer RT, Baker TA. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5TXT"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":113,"region_id":"DP02768r003","start":83,"term_id":"IDPO:0000011","statement":[{"text":"NT (near the mature N-terminus, residues 83–113) was only ordered in subunit B. NTB includes part of helix α1, an extended loop, strand β1, and the loop leading to β2.","type":"Results"},{"text":"PLP binding is coupled to disorder-order transitions in three distinct regions of ALAS","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29551290","version":2,"reference_html":"Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme. <i> Brown BL, Kardon JR, Sauer RT, Baker TA. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5TXT"},{"db":"PDB","id":"5TXR"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":156,"region_id":"DP02768r004","start":147,"term_id":"IDPO:0000011","statement":[{"text":"GR, which overlaps with a conserved glycine-rich motif (Gong and Ferreira, 1995), by contrast, was ordered only in the A subunit and consists of residues 147–156. The ordered GRA element packs against the PLP cofactor-binding pocket that was in the B subunit.","type":"Results"},{"text":"PLP binding is coupled to disorder-order transitions in three distinct regions of ALAS","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29551290","version":2,"reference_html":"Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme. <i> Brown BL, Kardon JR, Sauer RT, Baker TA. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5TXT"},{"db":"PDB","id":"5TXR"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":156,"region_id":"DP02768r005","start":147,"term_id":"IDPO:0000002","statement":[{"text":"GR, which overlaps with a conserved glycine-rich motif (Gong and Ferreira, 1995), by contrast, was ordered only in the A subunit and consists of residues 147–156. The ordered GRA element packs against the PLP cofactor-binding pocket that was in the B subunit.","type":"Results"},{"text":"PLP binding is coupled to disorder-order transitions in three distinct regions of ALAS","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29551290","version":2,"reference_html":"Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme. <i> Brown BL, Kardon JR, Sauer RT, Baker TA. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5TXT"},{"db":"PDB","id":"5TXR"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":548,"region_id":"DP02768r006","start":538,"term_id":"IDPO:0000002","statement":[{"text":"CT is comprised of residues 538–548, the last 11 residues of the eukaryote-specific C-terminal extension in ALASSc. The ordered CTA element from the PLP-free subunit also contributed to the assembled active site of the opposite B subunit.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29551290","version":2,"reference_html":"Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme. <i> Brown BL, Kardon JR, Sauer RT, Baker TA. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5TXT"},{"db":"PDB","id":"5TXR"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":548,"region_id":"DP02768r007","start":538,"term_id":"IDPO:0000011","statement":[{"text":"CT is comprised of residues 538–548, the last 11 residues of the eukaryote-specific C-terminal extension in ALASSc. The ordered CTA element from the PLP-free subunit also contributed to the assembled active site of the opposite B subunit.","type":"Results"},{"text":"PLP binding is coupled to disorder-order transitions in three distinct regions of ALAS","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29551290","version":2,"reference_html":"Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme. <i> Brown BL, Kardon JR, Sauer RT, Baker TA. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5TXT"},{"db":"PDB","id":"5TXR"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2021_06","ncbi_taxon_id":559292,"disprot_id":"DP02768","date":"2020-04-15T13:58:56.799Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":7,"name":"5-aminolevulinate synthase, mitochondrial","dataset":[],"UniParc":"UPI000012C441","uniref100":"UniRef100_P09950","uniref90":"UniRef90_P09950","uniref50":"UniRef50_P09950","genes":[{"name":{"value":"HEM1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"3516694","url":"http://www.ncbi.nlm.nih.gov/pubmed/3516694","alternativeUrl":"https://europepmc.org/abstract/MED/3516694"}}]},"synonyms":[{"value":"CYD1"}],"orfNames":[{"value":"YD9934.16"}],"olnNames":[{"value":"YDR232W","evidences":[{"code":"ECO:0000312","source":{"name":"SGD","id":"S000002640","url":"https://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000002640"}}]}]}],"alphafold_very_low_content":0.10948905109489052,"disorder_content":0.12043795620437957,"disprot_consensus":{"full":[{"start":58,"end":71,"type":"D"},{"start":83,"end":113,"type":"T"},{"start":147,"end":156,"type":"T"},{"start":538,"end":548,"type":"T"}],"Structural state":[{"start":58,"end":71,"type":"D"},{"start":83,"end":113,"type":"D"},{"start":147,"end":156,"type":"D"},{"start":538,"end":548,"type":"D"}],"Structural transition":[{"start":83,"end":113,"type":"T"},{"start":147,"end":156,"type":"T"},{"start":538,"end":548,"type":"T"}]}},{"acc":"P06782","features":{"gene3D":[],"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":55,"end":306},{"id":"PF08587","name":"Ubiquitin associated domain (UBA)","start":344,"end":389},{"id":"PF16579","name":"Adenylate sensor of SNF1-like protein kinase","start":504,"end":626}]},"creator":"lchemes","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"sequence":"MSSNNNTNTAPANANSSHHHHHHHHHHHHHGHGGSNSTLNNPKSSLADGAHIGNYQIVKTLGEGSFGKVKLAYHTTTGQKVALKIINKKVLAKSDMQGRIEREISYLRLLRHPHIIKLYDVIKSKDEIIMVIEYAGNELFDYIVQRDKMSEQEARRFFQQIISAVEYCHRHKIVHRDLKPENLLLDEHLNVKIADFGLSNIMTDGNFLKTSCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYVMLCRRLPFDDESIPVLFKNISNGVYTLPKFLSPGAAGLIKRMLIVNPLNRISIHEIMQDDWFKVDLPEYLLPPDLKPHPEEENENNDSKKDGSSPDNDEIDDNLVNILSSTMGYEKDEIYESLESSEDTPAFNEIRDAYMLIKENKSLIKDMKANKSVSDELDTFLSQSPPTFQQQSKSHQKSQVDHETAKQHARRMASAITQQRTYHQSPFMDQYKEEDSTVSILPTSLPQIHRANMLAQGSPAASKISPLVTKKSKTRWHFGIRSRSYPLDVMGEIYIALKNLGAEWAKPSEEDLWTIKLRWKYDIGNKTNTNEKIPDLMKMVIQLFQIETNNYLVDFKFDGWESSYGDDTTVSNISEDEMSTFSAYPFLHLTTKLIMELAVNSQSN","length":633,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":214,"region_id":"DP02769r001","start":200,"term_id":"IDPO:0000002","statement":[{"text":"The activation loop of the kinase (residues 200-215) enclosed between the highly conserved DFG and APE motifs (Fig. 1B) is disordered in the current structure\"...\"The current structure of Snf1-KD is in the unphosphorylated form. It has been reported that mutating the Thr residue in the activation loop to an Asp residue can confer partial activity to AMPK [18,19]. We have therefore produced crystals of the T210D mutant of yeast Snf1-KD and determined its structure at 2.7 A˚ resolution. This structure showed that the activation loop is still disordered in the T210D mutant\n","type":"Results"},{"text":"This structure corresponds to an unphosphorylated state and also the T210D phspophomimetic mutant","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"16236260","version":2,"reference_html":"Crystal structure of the protein kinase domain of yeast AMP-activated protein kinase Snf1. <i> Rudolph MJ, Amodeo GA, Bai Y, Tong L. </i> Biochem Biophys Res Commun, 2005","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3HYH"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":212,"region_id":"DP02769r002","start":197,"term_id":"IDPO:0000002","statement":[{"text":"Snf1-pKD displays a ‘closed’ conformation, although the phosphorylated Thr 210 is invisible,\n","type":"Results"},{"text":"This structure corresponds to an active form that is phosphorylated on the activation loop residue T210 (this is part of the disordered region)","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"19474788","version":2,"reference_html":"Structural insight into the autoinhibition mechanism of AMP-activated protein kinase. <i> Chen L, Jiao ZH, Zheng LS, Zhang YY, Xie ST, Wang ZX, Wu JW. </i> Nature, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3DAE"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":212,"region_id":"DP02769r003","start":197,"term_id":"GO:0140677","statement":[{"text":"A new inhibited conformation of the KD is observed in a DFG-out conformation and with the glycine-rich loop adopting a structure that blocks ATP binding to the active site.","type":"Abstract"},{"text":"A large part of the activation segment of the KD, including Thr210 that is phosphorylated for activation, is ordered in the new structure. These residues are positioned far from the rest of the KD (Fig. 1  c). ","type":"Results"},{"text":"This region corresponds to the activation loop that contains T210. This structure reports an unphosphorylated and inactive form of the enzyme. Phosphorylation at T210 leads to disorder in a larger region of the activation loop (197-212) and when the domain is in the unphosphorylated inhibited conformation, structuring is observed and only residues 199-205 remain disordered. ","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"20823513","version":3,"reference_html":"An inhibited conformation for the protein kinase domain of the Saccharomyces cerevisiae AMPK homolog Snf1. <i> Rudolph MJ, Amodeo GA, Tong L. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"3MN3"}],"term_name":"molecular function activator activity","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":559292,"disprot_id":"DP02769","date":"2020-04-15T18:01:35.525Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":3,"name":"Carbon catabolite-derepressing protein kinase","dataset":[],"UniParc":"UPI0000052F22","uniref100":"UniRef100_P06782","uniref90":"UniRef90_P06782","uniref50":"UniRef50_P06782","genes":[{"name":{"value":"SNF1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"6366512","url":"http://www.ncbi.nlm.nih.gov/pubmed/6366512","alternativeUrl":"https://europepmc.org/abstract/MED/6366512"}}]},"synonyms":[{"value":"CAT1"},{"value":"CCR1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"1944227","url":"http://www.ncbi.nlm.nih.gov/pubmed/1944227","alternativeUrl":"https://europepmc.org/abstract/MED/1944227"}}]},{"value":"GLC2"},{"value":"PAS14"}],"orfNames":[{"value":"D8035.20"}],"olnNames":[{"value":"YDR477W"}]}],"alphafold_very_low_content":0.2527646129541864,"disorder_content":0.02843601895734597,"disprot_consensus":{"full":[{"start":197,"end":214,"type":"D"}],"Structural state":[{"start":197,"end":214,"type":"D"}],"Molecular function":[{"start":197,"end":212,"type":"F"}]}},{"acc":"P01127","features":{"gene3D":[{"start":21,"end":188,"id":"G3DSA:2.10.90.10","name":"Cystine-knot cytokines"}],"pfam":[{"id":"PF00341","name":"PDGF/VEGF domain","start":97,"end":180},{"id":"PF04692","name":"Platelet-derived growth factor, N terminal region","start":21,"end":92}]},"creator":"lchemes","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MNRCWALFLSLCCYLRLVSAEGDPIPEELYEMLSDHSIRSFDDLQRLLHGDPGEEDGAELDLNMTRSHSGGELESLARGRRSLGSLTIAEPAMIAECKTRTEVFEISRRLIDRTNANFLVWPPCVEVQRCSGCCNNRNVQCRPTQVQLRPVQVRKIEIVRKKPIFKKATVTLEDHLACKCETVAAARPVTRSPGGSQEQRAKTPQTRVTIRTVRVRRPPKGKHRKFKHTHDKTALKETLGA","length":241,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":119,"region_id":"DP02770r001","start":106,"term_id":"IDPO:0000002","statement":[{"text":"The strand connections, denoted as loops I, II and III, range from residues Ile25-Leu38, Cys53-Val58 and Val78 -Lys81, respectively, are exposed to solvent and show partial disorder in all three independent monomers","type":"Results"},{"text":"Because processing removes residues 1-81 from the mature protein form, the L1 loop residue numbering and boundaries are as follows: residue Ile25 named by the authors corresponds to Ile 106 in the UNIPROT entry, and Leu 38 named by the authors corresponds to Leu 119.","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"1396586","version":2,"reference_html":"Crystal structure of human platelet-derived growth factor BB. <i> Oefner C, D'Arcy A, Winkler FK, Eggimann B, Hosang M. </i> EMBO J, 1992","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1PDG"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T16:18:00.921Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":119,"region_id":"DP02770r002","start":106,"term_id":"IDPO:0000011","statement":[{"text":"A large-scale structural organization and rearrangement is observed for PDGF-B upon receptor binding, in which the PDGF-B L1 loop, disordered in the structure of the free form, adopts a highly specific conformation to form hydrophobic interactions with the third Ig domain of PDGFRbeta","type":"Abstract"},{"text":"The loop itself is exquisitely configured in the complex, with the aromatic ring of Phe37 at the center of the hydrophobic core, and numerous intraloop hydrogen bonds to maintain main chain peptide conformation (Fig. 3C). Therefore, this loop has an intrinsic propensity to fold into the observed conformation. In support of this notion, the L1 loop of the propeptide-bound PDGF-A, which is only marginally stabilized at its base by the interaction with the propeptide, is ordered and adopts a similar conformation to PDGF-B (Fig. S3D). Hence, the free PDGF-B L1 loop, which was disordered in that structure, may exist in equilibrium between folded and unfolded states, the former only selected by receptor binding.","type":"Results"},{"text":"Figure 4 Legend: Comparison between the free PDGF-B (PDB code 1PDG) dimer (red) and the PDGFRβ-bound PDGF-B dimer (cyan for the protruding protomer and green for the receding protomer) shows that PDGFRβ-binding induces the structural organization of the previously disordered large L1 loop","type":"Figure"},{"text":"Because processing removes residues 1-81 from the mature protein form, the L1 loop residue numbering and boundaries are as follows: residue Ile25 named by the authors corresponds to Ile 106 in the UNIPROT entry, and Leu 38 named by the authors corresponds to Leu 119. The Phe 37 residue named by the authors corresponds to Phe 118 in the UNIPROT entry","type":"Curator statement"}],"curator_id":"vnugnes","released":"2022_06","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"20534510","version":3,"reference_html":"Structures of a platelet-derived growth factor/propeptide complex and a platelet-derived growth factor/receptor complex. <i> Shim AH, Liu H, Focia PJ, Chen X, Lin PC, He X. </i> Proc Natl Acad Sci U S A, 2010","date":"2022-06-16T19:52:23.202Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"3MJG"}],"term_name":"disorder to order","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P09619"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"44278","entry_name":"N-acetyl-alpha-D-glucosamine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"506227","entry_name":"N-acetyl-D-glucosamine"}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":119,"region_id":"DP02770r003","start":106,"term_id":"GO:0005161","statement":[{"text":"A large-scale structural organization and rearrangement is observed for PDGF-B upon receptor binding, in which the PDGF-B L1 loop, disordered in the structure of the free form, adopts a highly specific conformation to form hydrophobic interactions with the third Ig domain of PDGFRbeta","type":"Abstract"},{"text":"Because processing removes residues 1-81 from the mature protein form, the L1 loop residue numbering and boundaries are as follows: residue Ile25 named by the authors corresponds to Ile 106 in the UNIPROT entry, and Leu 38 named by the authors corresponds to Leu 119. The Phe 37 residue named by the authors corresponds to Phe 118 in the UNIPROT entry","type":"Curator statement"},{"text":"Figure 4 Legend: Comparison between the free PDGF-B (PDB code 1PDG) dimer (red) and the PDGFRβ-bound PDGF-B dimer (cyan for the protruding protomer and green for the receding protomer) shows that PDGFRβ-binding induces the structural organization of the previously disordered large L1 loop","type":"Figure"},{"text":"The L1 loop becomes ordered as a part of the recognition of the receptor PDGFRbeta","type":"Curator statement"}],"curator_id":"vnugnes","released":"2022_06","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"20534510","version":4,"reference_html":"Structures of a platelet-derived growth factor/propeptide complex and a platelet-derived growth factor/receptor complex. <i> Shim AH, Liu H, Focia PJ, Chen X, Lin PC, He X. </i> Proc Natl Acad Sci U S A, 2010","date":"2022-06-16T19:54:19.613Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"3MJG"}],"term_name":"platelet-derived growth factor receptor binding","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a platelet-derived growth factor receptor.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P09619","operator":null,"partner_start":null,"partner_end":null}]}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02770","date":"2020-04-15T19:21:15.915Z","organism":"Homo sapiens","regions_counter":3,"name":"Platelet-derived growth factor subunit B","dataset":["Cancer-related proteins","Extracellular matrix proteins","NDDs-related proteins"],"UniParc":"UPI000004110E","uniref100":"UniRef100_P01127","uniref90":"UniRef90_P01127","uniref50":"UniRef50_P01127","genes":[{"name":{"value":"PDGFB"},"synonyms":[{"value":"PDGF2"},{"value":"SIS"}]}],"alphafold_very_low_content":0.18672199170124482,"disorder_content":0.058091286307053944,"disprot_consensus":{"full":[{"start":106,"end":119,"type":"T"}],"Structural state":[{"start":106,"end":119,"type":"D"}],"Structural transition":[{"start":106,"end":119,"type":"T"}],"Molecular function":[{"start":106,"end":119,"type":"F"}]}},{"acc":"P0DTC2","name":"Spike glycoprotein","sequence":"MFVFLVLLPLVSSQCVNLTTRTQLPPAYTNSFTRGVYYPDKVFRSSVLHSTQDLFLPFFSNVTWFHAIHVSGTNGTKRFDNPVLPFNDGVYFASTEKSNIIRGWIFGTTLDSKTQSLLIVNNATNVVIKVCEFQFCNDPFLGVYYHKNNKSWMESEFRVYSSANNCTFEYVSQPFLMDLEGKQGNFKNLREFVFKNIDGYFKIYSKHTPINLVRDLPQGFSALEPLVDLPIGINITRFQTLLALHRSYLTPGDSSSGWTAGAAAYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCTLKSFTVEKGIYQTSNFRVQPTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNFNFNGLTGTGVLTESNKKFLPFQQFGRDIADTTDAVRDPQTLEILDITPCSFGGVSVITPGTNTSNQVAVLYQDVNCTEVPVAIHADQLTPTWRVYSTGSNVFQTRAGCLIGAEHVNNSYECDIPIGAGICASYQTQTNSPRRARSVASQSIIAYTMSLGAENSVAYSNNSIAIPTNFTISVTTEILPVSMTKTSVDCTMYICGDSTECSNLLLQYGSFCTQLNRALTGIAVEQDKNTQEVFAQVKQIYKTPPIKDFGGFNFSQILPDPSKPSKRSFIEDLLFNKVTLADAGFIKQYGDCLGDIAARDLICAQKFNGLTVLPPLLTDEMIAQYTSALLAGTITSGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKLIANQFNSAIGKIQDSLSSTASALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQSAPHGVVFLHVTYVPAQEKNFTTAPAICHDGKAHFPREGVFVSNGTHWFVTQRNFYEPQIITTDNTFVSGNCDVVIGIVNNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKWPWYIWLGFIAGLIAIVMVTIMLCCMTSCCSCLKGCCSCGSCCKFDEDDSEPVLKGVKLHYT","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Nidovirales","Cornidovirineae","Coronaviridae","Orthocoronavirinae","Betacoronavirus","Sarbecovirus"],"creator":"xcastro","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":79,"region_id":"DP02772r001","reference_id":"32155444","start":70,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The atomic model comprises residues 27-1147, with internal breaks corresponding to flexible regions (including part of the RBM), and lacks the C-terminal most segment (including the heptad repeat 2) that is not visible in the map, as is the case for all S structures determined to date.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. <i> Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D. </i> Cell, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6VYB"},{"db":"PDB","id":"6VXX"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:21:55.761Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":164,"region_id":"DP02772r002","reference_id":"32155444","start":144,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The atomic model comprises residues 27-1147, with internal breaks corresponding to flexible regions (including part of the RBM), and lacks the C-terminal most segment (including the heptad repeat 2) that is not visible in the map, as is the case for all S structures determined to date.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. <i> Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D. </i> Cell, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6VYB"},{"db":"PDB","id":"6VXX"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:21:36.344Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":185,"region_id":"DP02772r003","reference_id":"32155444","start":173,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The atomic model comprises residues 27-1147, with internal breaks corresponding to flexible regions (including part of the RBM), and lacks the C-terminal most segment (including the heptad repeat 2) that is not visible in the map, as is the case for all S structures determined to date.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. <i> Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D. </i> Cell, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6VYB"},{"db":"PDB","id":"6VXX"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:21:18.273Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":262,"region_id":"DP02772r004","reference_id":"32155444","start":246,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The atomic model comprises residues 27-1147, with internal breaks corresponding to flexible regions (including part of the RBM), and lacks the C-terminal most segment (including the heptad repeat 2) that is not visible in the map, as is the case for all S structures determined to date.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. <i> Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D. </i> Cell, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6VYB"},{"db":"PDB","id":"6VXX"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:19:07.166Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":488,"region_id":"DP02772r005","reference_id":"32155444","start":469,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The atomic model comprises residues 27-1147, with internal breaks corresponding to flexible regions (including part of the RBM), and lacks the C-terminal most segment (including the heptad repeat 2) that is not visible in the map, as is the case for all S structures determined to date.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. <i> Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D. </i> Cell, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6VYB"},{"db":"PDB","id":"6VXX"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:16:21.771Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":640,"region_id":"DP02772r006","reference_id":"32155444","start":621,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The atomic model comprises residues 27-1147, with internal breaks corresponding to flexible regions (including part of the RBM), and lacks the C-terminal most segment (including the heptad repeat 2) that is not visible in the map, as is the case for all S structures determined to date.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. <i> Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D. </i> Cell, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6VYB"},{"db":"PDB","id":"6VXX"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:15:56.088Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":687,"region_id":"DP02772r007","reference_id":"32155444","start":677,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The atomic model comprises residues 27-1147, with internal breaks corresponding to flexible regions (including part of the RBM), and lacks the C-terminal most segment (including the heptad repeat 2) that is not visible in the map, as is the case for all S structures determined to date.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. <i> Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D. </i> Cell, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6VYB"},{"db":"PDB","id":"6VXX"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:15:10.391Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":853,"region_id":"DP02772r008","reference_id":"32155444","start":828,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The atomic model comprises residues 27-1147, with internal breaks corresponding to flexible regions (including part of the RBM), and lacks the C-terminal most segment (including the heptad repeat 2) that is not visible in the map, as is the case for all S structures determined to date.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. <i> Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D. </i> Cell, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6VYB"},{"db":"PDB","id":"6VXX"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:13:29.787Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1273,"region_id":"DP02772r009","reference_id":"32155444","start":1148,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The atomic model comprises residues 27-1147, with internal breaks corresponding to flexible regions (including part of the RBM), and lacks the C-terminal most segment (including the heptad repeat 2) that is not visible in the map, as is the case for all S structures determined to date.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. <i> Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D. </i> Cell, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6VYB"},{"db":"PDB","id":"6VXX"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:12:40.481Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":26,"region_id":"DP02772r010","reference_id":"32075877","start":1,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Our final model spans S residues 27 to 1146, with several flexible loops omitted. Like all previously reported coronavirus S ectodomain structures, the density for 2019-nCoV S begins to fade after the connector domain, reflecting the flexibility of the heptad repeat 2 domain in the prefusion conformation.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. <i> Wrapp D, Wang N, Corbett KS, Goldsmith JA, Hsieh CL, Abiona O, Graham BS, McLellan JS. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6VSB"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T08:59:40.571Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":80,"region_id":"DP02772r011","reference_id":"32075877","start":67,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Our final model spans S residues 27 to 1146, with several flexible loops omitted. Like all previously reported coronavirus S ectodomain structures, the density for 2019-nCoV S begins to fade after the connector domain, reflecting the flexibility of the heptad repeat 2 domain in the prefusion conformation.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. <i> Wrapp D, Wang N, Corbett KS, Goldsmith JA, Hsieh CL, Abiona O, Graham BS, McLellan JS. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6VSB"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T08:59:31.901Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":154,"region_id":"DP02772r012","reference_id":"32075877","start":142,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Our final model spans S residues 27 to 1146, with several flexible loops omitted. Like all previously reported coronavirus S ectodomain structures, the density for 2019-nCoV S begins to fade after the connector domain, reflecting the flexibility of the heptad repeat 2 domain in the prefusion conformation.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. <i> Wrapp D, Wang N, Corbett KS, Goldsmith JA, Hsieh CL, Abiona O, Graham BS, McLellan JS. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6VSB"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T08:59:11.563Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":262,"region_id":"DP02772r013","reference_id":"32075877","start":246,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Our final model spans S residues 27 to 1146, with several flexible loops omitted. Like all previously reported coronavirus S ectodomain structures, the density for 2019-nCoV S begins to fade after the connector domain, reflecting the flexibility of the heptad repeat 2 domain in the prefusion conformation.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. <i> Wrapp D, Wang N, Corbett KS, Goldsmith JA, Hsieh CL, Abiona O, Graham BS, McLellan JS. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6VSB"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T08:58:50.191Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":490,"region_id":"DP02772r014","reference_id":"32075877","start":455,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Our final model spans S residues 27 to 1146, with several flexible loops omitted. Like all previously reported coronavirus S ectodomain structures, the density for 2019-nCoV S begins to fade after the connector domain, reflecting the flexibility of the heptad repeat 2 domain in the prefusion conformation.","type":"Article"},{"text":"This disordered region corresponds to the so called RBM or Receptor Binding Motif, a long flexible loop that is disordered and flexible in the unbound conformation, but becomes ordered in the ACE2-bound form","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. <i> Wrapp D, Wang N, Corbett KS, Goldsmith JA, Hsieh CL, Abiona O, Graham BS, McLellan JS. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6VSB"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T08:58:09.866Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":637,"region_id":"DP02772r015","reference_id":"32075877","start":621,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Our final model spans S residues 27 to 1146, with several flexible loops omitted. Like all previously reported coronavirus S ectodomain structures, the density for 2019-nCoV S begins to fade after the connector domain, reflecting the flexibility of the heptad repeat 2 domain in the prefusion conformation.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. <i> Wrapp D, Wang N, Corbett KS, Goldsmith JA, Hsieh CL, Abiona O, Graham BS, McLellan JS. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6VSB"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T08:57:52.639Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":686,"region_id":"DP02772r016","reference_id":"32075877","start":673,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Our final model spans S residues 27 to 1146, with several flexible loops omitted. Like all previously reported coronavirus S ectodomain structures, the density for 2019-nCoV S begins to fade after the connector domain, reflecting the flexibility of the heptad repeat 2 domain in the prefusion conformation.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. <i> Wrapp D, Wang N, Corbett KS, Goldsmith JA, Hsieh CL, Abiona O, Graham BS, McLellan JS. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6VSB"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T08:57:09.461Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":852,"region_id":"DP02772r017","reference_id":"32075877","start":829,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Our final model spans S residues 27 to 1146, with several flexible loops omitted. Like all previously reported coronavirus S ectodomain structures, the density for 2019-nCoV S begins to fade after the connector domain, reflecting the flexibility of the heptad repeat 2 domain in the prefusion conformation.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. <i> Wrapp D, Wang N, Corbett KS, Goldsmith JA, Hsieh CL, Abiona O, Graham BS, McLellan JS. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6VSB"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T08:57:06.163Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1208,"region_id":"DP02772r018","reference_id":"32075877","start":1147,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Our final model spans S residues 27 to 1146, with several flexible loops omitted. Like all previously reported coronavirus S ectodomain structures, the density for 2019-nCoV S begins to fade after the connector domain, reflecting the flexibility of the heptad repeat 2 domain in the prefusion conformation.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. <i> Wrapp D, Wang N, Corbett KS, Goldsmith JA, Hsieh CL, Abiona O, Graham BS, McLellan JS. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6VSB"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T08:56:31.207Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":332,"region_id":"DP02772r019","reference_id":"32225176","start":319,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The final model contains residues Thr333 to Gly526 of the SARS-CoV-2 RBD, residues Ser19 to Asp615 of the ACE2 N-terminal peptidase domain, one zinc ion, four NAG glycans linked to ACE2 Asn90, Asn322 and Asn546 and to RBD Asn343, as well as 80 water molecules.","type":"Article"},{"text":"Receptor-binding domain (RBD, 319-542) of the Spike glycoprotein","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor. <i> Lan J, Ge J, Yu J, Shan S, Zhou H, Fan S, Zhang Q, Shi X, Wang Q, Zhang L, Wang X. </i> Nature, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6M0J"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:43:57.870Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":541,"region_id":"DP02772r020","reference_id":"32225176","start":527,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"The final model contains residues Thr333 to Gly526 of the SARS-CoV-2 RBD, residues Ser19 to Asp615 of the ACE2 N-terminal peptidase domain, one zinc ion, four NAG glycans linked to ACE2 Asn90, Asn322 and Asn546 and to RBD Asn343, as well as 80 water molecules.","type":"Article"},{"text":"Receptor-binding domain (RBD, 319-542) of the Spike glycoprotein","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor. <i> Lan J, Ge J, Yu J, Shan S, Zhou H, Fan S, Zhang Q, Shi X, Wang Q, Zhang L, Wang X. </i> Nature, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6M0J"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:43:56.519Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":332,"region_id":"DP02772r021","reference_id":"32245784","start":319,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Missing electron density region identified upon visual inspection of the structure inside the receptor-binding domain (RBD, 319-542) of the Spike glycoprotein","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV. <i> Yuan M, Wu NC, Zhu X, Lee CD, So RTY, Lv H, Mok CKP, Wilson IA. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6W41"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:43:54.789Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":541,"region_id":"DP02772r022","reference_id":"32245784","start":527,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Missing electron density region identified upon visual inspection of the structure inside the receptor-binding domain (RBD, 319-542) of the Spike glycoprotein","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV. <i> Yuan M, Wu NC, Zhu X, Lee CD, So RTY, Lv H, Mok CKP, Wilson IA. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6W41"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:43:53.811Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP02772r028","ec_ontology":"ECO","end":541,"term_id":"GO:0005515","start":319,"version":4,"statement":[{"text":"Here, we present cryo-electron microscopy structures of full-length human ACE2 in the presence of the neutral amino acid transporter B0AT1 with or without the receptor binding domain (RBD) of the surface spike glycoprotein (S protein) of SARS-CoV-2, both at an overall resolution of 2.9 angstroms, with a local resolution of 3.5 angstroms at the ACE2-RBD interface.","type":"Abstract"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9BYF1","partner_end":null}],"term_name":"protein binding","ec_name":"cryogenic electron microscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"32132184","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6M17"},{"db":"EMDB","id":"30039"},{"db":"EMDB","id":"30046"}],"term_namespace":"Molecular function","ec_id":"ECO:0006208","curator_id":"fquaglia","reference_html":"Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2. <i> Yan R, Zhang Y, Li Y, Xia L, Guo Y, Zhou Q. </i> Science, 2020","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:27:42.024Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":335,"region_id":"DP02772r029","reference_id":"32132184","start":319,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Here, we present cryo-electron microscopy structures of full-length human ACE2 in the presence of the neutral amino acid transporter B0AT1 with or without the receptor binding domain (RBD) of the surface spike glycoprotein (S protein) of SARS-CoV-2, both at an overall resolution of 2.9 angstroms, with a local resolution of 3.5 angstroms at the ACE2-RBD interface.","type":"Abstract"},{"text":"Missing electron density region identified upon visual inspection of the structure.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2. <i> Yan R, Zhang Y, Li Y, Xia L, Guo Y, Zhou Q. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6M17"},{"db":"EMDB","id":"30039"},{"db":"EMDB","id":"30046"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:43:52.812Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":541,"region_id":"DP02772r030","reference_id":"32132184","start":519,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Here, we present cryo-electron microscopy structures of full-length human ACE2 in the presence of the neutral amino acid transporter B0AT1 with or without the receptor binding domain (RBD) of the surface spike glycoprotein (S protein) of SARS-CoV-2, both at an overall resolution of 2.9 angstroms, with a local resolution of 3.5 angstroms at the ACE2-RBD interface.","type":"Abstract"},{"text":"Missing electron density region identified upon visual inspection of the structure.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":4,"reference_html":"Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2. <i> Yan R, Zhang Y, Li Y, Xia L, Guo Y, Zhou Q. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6M17"},{"db":"EMDB","id":"30039"},{"db":"EMDB","id":"30046"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:43:51.892Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":685,"region_id":"DP02772r031","reference_id":"32057769","start":680,"term_id":"IDPO:0000048","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Despite a high similarity with the genome sequence of SARS-CoV and SARS-like CoVs, we identified a peculiar furin-like cleavage site in the Spike protein of the 2019-nCoV, lacking in the other SARS-like CoVs.","type":"Abstract"},{"text":"In this article, we focus on a specific furin-like protease recognition pattern present in the vicinity of one of the maturation sites of the S protein (Fig. 1B) that may have significant functional implications for virus entry.","type":"Article"},{"text":"For instance, the pathogenesis of some CoV has been previously related to the presence of a furin-like cleavage site in the S-protein sequence. For example, the insertion of a similar cleavage site in the infectious bronchitis virus (IBV) S-protein results in higher pathogenicity, pronounced neural symptoms and neurotropism in infected chickens (Cheng et al., 2019).","type":"Article"},{"text":"Similarly, in the case of influenza virus, low-pathogenicity forms of influenza virus contain a single basic residue at the cleavage site, which is cleaved by trypsin-like proteases and the tissue distribution of the activating protease(s) typically restricts infections to the respiratory and/or intestinal organs (Sun et al., 2010). Conversely, the highly pathogenic forms of influenza have a furin-like cleavage site cleaved by different cellular proteases, including furin, which are expressed in a wide variety of cell types allowing a widening of the cell tropism of the virus (Kido et al., 2012).","type":"Article"},{"text":"This furin-like cleavage site, is supposed to be cleaved during virus egress (Mille and Whittaker, 2014) for S-protein “priming” and may provide a gain-of-function to the 2019-nCoV for efficient spreading in the human population compared to other lineage b betacoronaviruses.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","version":4,"reference_html":"The spike glycoprotein of the new coronavirus 2019-nCoV contains a furin-like cleavage site absent in CoV of the same clade. <i> Coutard B, Valle C, de Lamballerie X, Canard B, Seidah NG, Decroly E. </i> Antiviral Res, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"limited proteolysis display site","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:47:15.293Z"},"term_xref":"GO:0098772","disprot_namespace":"Disorder function"},{"term_namespace":"Biological process","ec_ontology":"ECO","end":686,"region_id":"DP02772r032","reference_id":"32142651","start":681,"term_id":"GO:0046598","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Cell entry of coronaviruses depends on binding of the viral spike (S) proteins to cellular receptors and on S protein priming by host cell proteases.","type":"Abstract"},{"text":"Here, we demonstrate that SARS-CoV-2 uses the SARS-CoV receptor ACE2 for entry and the serine protease TMPRSS2 for S protein priming.","type":"Abstract"},{"text":"The present study provides evidence that host cell entry of SARS-CoV-2 depends on the SARS-CoV receptor ACE2 and can be blocked by a clinically proven inhibitor of the cellular serine protease TMPRSS2, which is employed by SARS-CoV-2 for S protein priming.","type":"Discussion"},{"text":"These results suggest efficient proteolytic processing of SARS-2-S in human cells, in keeping with the presence of several arginine residues at the S1/S2 cleavage site of SARS-2-S but not SARS-S.","type":"Results"}],"curator_id":"fquaglia","released":"2024_06","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"immunodetection assay evidence used in manual assertion","version":5,"reference_html":"SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor. <i> Hoffmann M, Kleine-Weber H, Schroeder S, Krüger N, Herrler T, Erichsen S, Schiergens TS, Herrler G, Wu NH, Nitsche A, Müller MA, Drosten C, Pöhlmann S. </i> Cell, 2020","date":"2024-02-29T14:28:25.839Z","reference_source":"pmid","ec_id":"ECO:0007719","term_name":"positive regulation of viral entry into host cell","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of the introduction of viral entry into the host cell.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-02-29T14:29:07.711Z"}},{"term_namespace":"Biological process","ec_ontology":"ECO","end":508,"region_id":"DP02772r033","reference_id":"32142651","start":437,"term_id":"GO:0046598","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Cell entry of coronaviruses depends on binding of the viral spike (S) proteins to cellular receptors and on S protein priming by host cell proteases.","type":"Abstract"},{"text":"Here, we demonstrate that SARS-CoV-2 uses the SARS-CoV receptor ACE2 for entry and the serine protease TMPRSS2 for S protein priming.","type":"Abstract"},{"text":"Moreover, antiserum raised against human ACE2 blocked SARS-S- and SARS-2-S- but not VSV-G- or MERS-S-driven entry (Figure 3B). Finally, authentic SARS-CoV-2 infected BHK-21 cells transfected to express ACE2 cells but not parental BHK-21 cells with high efficiency (Figure 3C), indicating that SARS-2-S, like SARS-S, uses ACE2 for cellular entry.","type":"Discussion"}],"curator_id":"fquaglia","released":"2024_06","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"immunodetection assay evidence used in manual assertion","version":5,"reference_html":"SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor. <i> Hoffmann M, Kleine-Weber H, Schroeder S, Krüger N, Herrler T, Erichsen S, Schiergens TS, Herrler G, Wu NH, Nitsche A, Müller MA, Drosten C, Pöhlmann S. </i> Cell, 2020","date":"2024-02-29T14:28:38.166Z","reference_source":"pmid","ec_id":"ECO:0007719","term_name":"positive regulation of viral entry into host cell","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of the introduction of viral entry into the host cell.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-02-29T14:29:09.324Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":686,"region_id":"DP02772r034","reference_id":"32142651","start":681,"term_id":"IDPO:0000048","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Cell entry of coronaviruses depends on binding of the viral spike (S) proteins to cellular receptors and on S protein priming by host cell proteases.","type":"Abstract"},{"text":"Here, we demonstrate that SARS-CoV-2 uses the SARS-CoV receptor ACE2 for entry and the serine protease TMPRSS2 for S protein priming.","type":"Abstract"},{"text":"The present study provides evidence that host cell entry of SARS-CoV-2 depends on the SARS-CoV receptor ACE2 and can be blocked by a clinically proven inhibitor of the cellular serine protease TMPRSS2, which is employed by SARS-CoV-2 for S protein priming.","type":"Discussion"},{"text":"These results suggest efficient proteolytic processing of SARS-2-S in human cells, in keeping with the presence of several arginine residues at the S1/S2 cleavage site of SARS-2-S but not SARS-S.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"immunodetection assay evidence used in manual assertion","version":3,"reference_html":"SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor. <i> Hoffmann M, Kleine-Weber H, Schroeder S, Krüger N, Herrler T, Erichsen S, Schiergens TS, Herrler G, Wu NH, Nitsche A, Müller MA, Drosten C, Pöhlmann S. </i> Cell, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","term_name":"limited proteolysis display site","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:45:02.417Z"},"ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":21,"region_id":"DP02772r035","reference_id":"32366695","start":16,"term_id":"IDPO:0000041","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"To determine the site-specific glycosylation of SARS-CoV-2 S, we employed trypsin, chymotrypsin, and alphalytic protease to generate three glycopeptide samples. These proteases were selected to generate glycopeptides that contain a single N-linked glycan sequon. The glycopeptides were analyzed by liquid-chromatography-mass spectrometry (LC-MS), and the glycan compositions were determined for all 22 N-linked glycan sites (Fig. 2). Although unoccupied glycosylation sites were detected on SARS-CoV-2 S, when quantified they were revealed to form a very minor component of the total peptide pool (table S2).","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"mass spectrometry evidence used in manual assertion","version":4,"reference_html":"Site-specific glycan analysis of the SARS-CoV-2 spike. <i> Watanabe Y, Allen JD, Wrapp D, McLellan JS, Crispin M. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001230","term_name":"glycosylation display site","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:44:15.747Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":335,"region_id":"DP02772r036","reference_id":"32366695","start":330,"term_id":"IDPO:0000041","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"To determine the site-specific glycosylation of SARS-CoV-2 S, we employed trypsin, chymotrypsin, and alphalytic protease to generate three glycopeptide samples. These proteases were selected to generate glycopeptides that contain a single N-linked glycan sequon. The glycopeptides were analyzed by liquid-chromatography-mass spectrometry (LC-MS), and the glycan compositions were determined for all 22 N-linked glycan sites (Fig. 2). Although unoccupied glycosylation sites were detected on SARS-CoV-2 S, when quantified they were revealed to form a very minor component of the total peptide pool (table S2).","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"mass spectrometry evidence used in manual assertion","version":4,"reference_html":"Site-specific glycan analysis of the SARS-CoV-2 spike. <i> Watanabe Y, Allen JD, Wrapp D, McLellan JS, Crispin M. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001230","term_name":"glycosylation display site","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:44:14.103Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":78,"region_id":"DP02772r037","reference_id":"32366695","start":73,"term_id":"IDPO:0000041","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"To determine the site-specific glycosylation of SARS-CoV-2 S, we employed trypsin, chymotrypsin, and alphalytic protease to generate three glycopeptide samples. These proteases were selected to generate glycopeptides that contain a single N-linked glycan sequon. The glycopeptides were analyzed by liquid-chromatography-mass spectrometry (LC-MS), and the glycan compositions were determined for all 22 N-linked glycan sites (Fig. 2). Although unoccupied glycosylation sites were detected on SARS-CoV-2 S, when quantified they were revealed to form a very minor component of the total peptide pool (table S2).","type":"Article"},{"text":"We characterized the N-linked glycans on extended flexible loop structures (N74 and N149) and at the membrane-proximal C terminus (N1158, N1173, N1194) that were not resolved in the cryo-EM maps (4) These were determined to be complex-type glycans, consistent with steric accessibility of these residues.","type":"Article"},{"text":"Legend Fig 3. Note that the flexible loops on which N74 and N149 glycan sites reside are represented as dashed lines with glycan sites on the loops mapped at their approximate regions.\n","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"mass spectrometry evidence used in manual assertion","version":4,"reference_html":"Site-specific glycan analysis of the SARS-CoV-2 spike. <i> Watanabe Y, Allen JD, Wrapp D, McLellan JS, Crispin M. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001230","term_name":"glycosylation display site","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:44:11.755Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":153,"region_id":"DP02772r038","reference_id":"32366695","start":148,"term_id":"IDPO:0000041","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"To determine the site-specific glycosylation of SARS-CoV-2 S, we employed trypsin, chymotrypsin, and alphalytic protease to generate three glycopeptide samples. These proteases were selected to generate glycopeptides that contain a single N-linked glycan sequon. The glycopeptides were analyzed by liquid-chromatography-mass spectrometry (LC-MS), and the glycan compositions were determined for all 22 N-linked glycan sites (Fig. 2). Although unoccupied glycosylation sites were detected on SARS-CoV-2 S, when quantified they were revealed to form a very minor component of the total peptide pool (table S2).","type":"Article"},{"text":"We characterized the N-linked glycans on extended flexible loop structures (N74 and N149) and at the membrane-proximal C terminus (N1158, N1173, N1194) that were not resolved in the cryo-EM maps (4) These were determined to be complex-type glycans, consistent with steric accessibility of these residues.","type":"Article"},{"text":"Legend Fig 3. Note that the flexible loops on which N74 and N149 glycan sites reside are represented as dashed lines with glycan sites on the loops mapped at their approximate regions.\n","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"mass spectrometry evidence used in manual assertion","version":4,"reference_html":"Site-specific glycan analysis of the SARS-CoV-2 spike. <i> Watanabe Y, Allen JD, Wrapp D, McLellan JS, Crispin M. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001230","term_name":"glycosylation display site","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:44:10.084Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":1162,"region_id":"DP02772r039","reference_id":"32366695","start":1157,"term_id":"IDPO:0000041","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"To determine the site-specific glycosylation of SARS-CoV-2 S, we employed trypsin, chymotrypsin, and alphalytic protease to generate three glycopeptide samples. These proteases were selected to generate glycopeptides that contain a single N-linked glycan sequon. The glycopeptides were analyzed by liquid-chromatography-mass spectrometry (LC-MS), and the glycan compositions were determined for all 22 N-linked glycan sites (Fig. 2). Although unoccupied glycosylation sites were detected on SARS-CoV-2 S, when quantified they were revealed to form a very minor component of the total peptide pool (table S2).","type":"Article"},{"text":"We characterized the N-linked glycans on extended flexible loop structures (N74 and N149) and at the membrane-proximal C terminus (N1158, N1173, N1194) that were not re-solved in the cryo-EM maps (4) These were determined to be complex-type glycans, consistent with steric accessibility of these residues.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"mass spectrometry evidence used in manual assertion","version":4,"reference_html":"Site-specific glycan analysis of the SARS-CoV-2 spike. <i> Watanabe Y, Allen JD, Wrapp D, McLellan JS, Crispin M. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001230","term_name":"glycosylation display site","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:44:08.916Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":1177,"region_id":"DP02772r040","reference_id":"32366695","start":1172,"term_id":"IDPO:0000041","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"To determine the site-specific glycosylation of SARS-CoV-2 S, we employed trypsin, chymotrypsin, and alphalytic protease to generate three glycopeptide samples. These proteases were selected to generate glycopeptides that contain a single N-linked glycan sequon. The glycopeptides were analyzed by liquid-chromatography-mass spectrometry (LC-MS), and the glycan compositions were determined for all 22 N-linked glycan sites (Fig. 2). Although unoccupied glycosylation sites were detected on SARS-CoV-2 S, when quantified they were revealed to form a very minor component of the total peptide pool (table S2).","type":"Article"},{"text":"We characterized the N-linked glycans on extended flexible loop structures (N74 and N149) and at the membrane-proximal C terminus (N1158, N1173, N1194) that were not re-solved in the cryo-EM maps (4) These were determined to be complex-type glycans, consistent with steric accessibility of these residues.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"mass spectrometry evidence used in manual assertion","version":4,"reference_html":"Site-specific glycan analysis of the SARS-CoV-2 spike. <i> Watanabe Y, Allen JD, Wrapp D, McLellan JS, Crispin M. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001230","term_name":"glycosylation display site","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:44:07.784Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":1198,"region_id":"DP02772r041","reference_id":"32366695","start":1194,"term_id":"IDPO:0000041","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"To determine the site-specific glycosylation of SARS-CoV-2 S, we employed trypsin, chymotrypsin, and alphalytic protease to generate three glycopeptide samples. These proteases were selected to generate glycopeptides that contain a single N-linked glycan sequon. The glycopeptides were analyzed by liquid-chromatography-mass spectrometry (LC-MS), and the glycan compositions were determined for all 22 N-linked glycan sites (Fig. 2). Although unoccupied glycosylation sites were detected on SARS-CoV-2 S, when quantified they were revealed to form a very minor component of the total peptide pool (table S2).","type":"Article"},{"text":"We characterized the N-linked glycans on extended flexible loop structures (N74 and N149) and at the membrane-proximal C terminus (N1158, N1173, N1194) that were not re-solved in the cryo-EM maps (4) These were determined to be complex-type glycans, consistent with steric accessibility of these residues.","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"mass spectrometry evidence used in manual assertion","version":4,"reference_html":"Site-specific glycan analysis of the SARS-CoV-2 spike. <i> Watanabe Y, Allen JD, Wrapp D, McLellan JS, Crispin M. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001230","term_name":"glycosylation display site","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:44:06.781Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":319,"end":541,"reference_id":"32132184","reference_source":"pmid","reference_html":"Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2. <i> Yan R, Zhang Y, Li Y, Xia L, Guo Y, Zhou Q. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6M17"},{"db":"EMDB","id":"30039"},{"db":"EMDB","id":"30046"}],"region_id":"DP02772r043","statement":[{"text":"Here, we present cryo-electron microscopy structures of full-length human ACE2 in the presence of the neutral amino acid transporter B0AT1 with or without the receptor binding domain (RBD) of the surface spike glycoprotein (S protein) of SARS-CoV-2, both at an overall resolution of 2.9 angstroms, with a local resolution of 3.5 angstroms at the ACE2-RBD interface.","type":"Abstract"},{"text":"The region corresponds to the so called RBM or Receptor Binding Motif, a region that is a flexible and disordered loop in the unbound state, and becomes ordered in all the available ACE2-bound SARS-CoV-2 Spike structures. Flexibility in the unbound state can be observed in PDB:6VSB [PMID: 32075877] and PDB:6VYB [PMID: 32155444] and the ordering that occurs in the ACE-2 bound form can be seen in PDB: 6M17 [PMID: 32132184] and PDB: 6MOJ [PMID: 32225176]","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T09:44:03.459Z"},"ec_go":"IDA","disprot_namespace":"Structural transition"}],"released":"2020_06","length":1273,"ncbi_taxon_id":2697049,"date":"2020-04-15T21:05:10.000Z","organism":"Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2)","features":{"gene3D":[{"start":1165,"end":1212,"id":"G3DSA:1.20.5.790","name":"Single helix bin"}],"pfam":[{"id":"PF01601","name":"Coronavirus spike glycoprotein S2","start":711,"end":1232},{"id":"PF09408","name":"Betacoronavirus spike glycoprotein S1, receptor binding","start":349,"end":526},{"id":"PF16451","name":"Betacoronavirus-like spike glycoprotein S1, N-terminal","start":33,"end":337},{"id":"PF19209","name":"Coronavirus spike glycoprotein S1, C-terminal","start":536,"end":592}]},"disprot_id":"DP02772","regions_counter":49,"dataset":["Viral proteins"],"UniParc":"UPI00131F240A","uniref100":"UniRef100_P0DTC2","uniref90":"UniRef90_P0DTC2","uniref50":"UniRef50_P0DTC2","genes":[{"name":{"value":"S","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04099","url":"https://hamap.expasy.org/unirule/MF_04099"}}]},"orfNames":[{"value":"2"}]}],"disorder_content":0.28043990573448546,"disprot_consensus":{"full":[{"start":1,"end":26,"type":"D"},{"start":67,"end":80,"type":"D"},{"start":142,"end":164,"type":"D"},{"start":173,"end":185,"type":"D"},{"start":246,"end":262,"type":"D"},{"start":319,"end":541,"type":"T"},{"start":621,"end":640,"type":"D"},{"start":673,"end":687,"type":"D"},{"start":828,"end":853,"type":"D"},{"start":1147,"end":1273,"type":"D"}],"Structural state":[{"start":1,"end":26,"type":"D"},{"start":67,"end":80,"type":"D"},{"start":142,"end":164,"type":"D"},{"start":173,"end":185,"type":"D"},{"start":246,"end":262,"type":"D"},{"start":319,"end":335,"type":"D"},{"start":455,"end":490,"type":"D"},{"start":519,"end":541,"type":"D"},{"start":621,"end":640,"type":"D"},{"start":673,"end":687,"type":"D"},{"start":828,"end":853,"type":"D"},{"start":1147,"end":1273,"type":"D"}],"Molecular function":[{"start":319,"end":541,"type":"F"}],"Disorder function":[{"start":16,"end":21,"type":"F"},{"start":73,"end":78,"type":"F"},{"start":148,"end":153,"type":"F"},{"start":330,"end":335,"type":"F"},{"start":680,"end":686,"type":"F"},{"start":1157,"end":1162,"type":"F"},{"start":1172,"end":1177,"type":"F"},{"start":1194,"end":1198,"type":"F"}],"Biological process":[{"start":437,"end":508,"type":"F"},{"start":681,"end":686,"type":"F"}],"Structural transition":[{"start":319,"end":541,"type":"T"}]}},{"acc":"Q9UPY3","features":{"gene3D":[{"start":1659,"end":1853,"id":"G3DSA:1.10.1520.10","name":"Ribonuclease III domain"},{"start":1659,"end":1853,"id":"G3DSA:1.10.1520.10","name":"Ribonuclease III domain"},{"start":625,"end":725,"id":"G3DSA:3.30.160.380","name":"G3DSA:3.30.160.380"}],"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":46,"end":209},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":499,"end":553},{"id":"PF00636","name":"Ribonuclease III domain","start":1313,"end":1396},{"id":"PF00636","name":"Ribonuclease III domain","start":1702,"end":1824},{"id":"PF02170","name":"PAZ domain","start":917,"end":1062},{"id":"PF03368","name":"Dicer dimerisation domain","start":630,"end":718},{"id":"PF20930","name":"Dicer, partner-binding domain","start":268,"end":366},{"id":"PF20931","name":"Dicer, platform domain","start":761,"end":886},{"id":"PF20932","name":"Dicer, dsRNA-binding domain","start":1830,"end":1918}]},"creator":"lchemes","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MKSPALQPLSMAGLQLMTPASSPMGPFFGLPWQQEAIHDNIYTPRKYQVELLEAALDHNTIVCLNTGSGKTFIAVLLTKELSYQIRGDFSRNGKRTVFLVNSANQVAQQVSAVRTHSDLKVGEYSNLEVNASWTKERWNQEFTKHQVLIMTCYVALNVLKNGYLSLSDINLLVFDECHLAILDHPYREIMKLCENCPSCPRILGLTASILNGKCDPEELEEKIQKLEKILKSNAETATDLVVLDRYTSQPCEIVVDCGPFTDRSGLYERLLMELEEALNFINDCNISVHSKERDSTLISKQILSDCRAVLVVLGPWCADKVAGMMVRELQKYIKHEQEELHRKFLLFTDTFLRKIHALCEEHFSPASLDLKFVTPKVIKLLEILRKYKPYERQQFESVEWYNNRNQDNYVSWSDSEDDDEDEEIEEKEKPETNFPSPFTNILCGIIFVERRYTAVVLNRLIKEAGKQDPELAYISSNFITGHGIGKNQPRNKQMEAEFRKQEEVLRKFRAHETNLLIATSIVEEGVDIPKCNLVVRFDLPTEYRSYVQSKGRARAPISNYIMLADTDKIKSFEEDLKTYKAIEKILRNKCSKSVDTGETDIDPVMDDDDVFPPYVLRPDDGGPRVTINTAIGHINRYCARLPSDPFTHLAPKCRTRELPDGTFYSTLYLPINSPLRASIVGPPMSCVRLAERVVALICCEKLHKIGELDDHLMPVGKETVKYEEELDLHDEEETSVPGRPGSTKRRQCYPKAIPECLRDSYPRPDQPCYLYVIGMVLTTPLPDELNFRRRKLYPPEDTTRCFGILTAKPIPQIPHFPVYTRSGEVTISIELKKSGFMLSLQMLELITRLHQYIFSHILRLEKPALEFKPTDADSAYCVLPLNVVNDSSTLDIDFKFMEDIEKSEARIGIPSTKYTKETPFVFKLEDYQDAVIIPRYRNFDQPHRFYVADVYTDLTPLSKFPSPEYETFAEYYKTKYNLDLTNLNQPLLDVDHTSSRLNLLTPRHLNQKGKALPLSSAEKRKAKWESLQNKQILVPELCAIHPIPASLWRKAVCLPSILYRLHCLLTAEELRAQTASDAGVGVRSLPADFRYPNLDFGWKKSIDSKSFISISNSSSAENDNYCKHSTIVPENAAHQGANRTSSLENHDQMSVNCRTLLSESPGKLHVEVSADLTAINGLSYNQNLANGSYDLANRDFCQGNQLNYYKQEIPVQPTTSYSIQNLYSYENQPQPSDECTLLSNKYLDGNANKSTSDGSPVMAVMPGTTDTIQVLKGRMDSEQSPSIGYSSRTLGPNPGLILQALTLSNASDGFNLERLEMLGDSFLKHAITTYLFCTYPDAHEGRLSYMRSKKVSNCNLYRLGKKKGLPSRMVVSIFDPPVNWLPPGYVVNQDKSNTDKWEKDEMTKDCMLANGKLDEDYEEEDEEEESLMWRAPKEEADYEDDFLEYDQEHIRFIDNMLMGSGAFVKKISLSPFSTTDSAYEWKMPKKSSLGSMPFSSDFEDFDYSSWDAMCYLDPSKAVEEDDFVVGFWNPSEENCGVDTGKQSISYDLHTEQCIADKSIADCVEALLGCYLTSCGERAAQLFLCSLGLKVLPVIKRTDREKALCPTRENFNSQQKNLSVSCAAASVASSRSSVLKDSEYGCLKIPPRCMFDHPDADKTLNHLISGFENFEKKINYRFKNKAYLLQAFTHASYHYNTITDCYQRLEFLGDAILDYLITKHLYEDPRQHSPGVLTDLRSALVNNTIFASLAVKYDYHKYFKAVSPELFHVIDDFVQFQLEKNEMQGMDSELRRSEEDEEKEEDIEVPKAMGDIFESLAGAIYMDSGMSLETVWQVYYPMMRPLIEKFSANVPRSPVRELLEMEPETAKFSPAERTYDGKVRVTVEVVGKGKFKGVGRSYRIAKSAAARRALRSLKANQPQVPNS","length":1922,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1029,"region_id":"DP02781r001","start":1003,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Surprisingly, the hDicer-specific-segment, that forms the ‘hDicer-specific helix’ in the structure of hDicer PAZ cassette-siRNA 12-mer complex (Figure 1D) is melted/disordered (spanning residues 1005-1019) in the hDicer PAZ cassette-siRNA 16-mer complex (Figure 6B, dotted red line).","type":"Results"},{"text":"Due to a shift in the numbering used by the authors, the missing residues correspond to UNIPROT numbering 1003-1029","type":"Curator statement"},{"text":"The authors mention only the disordering of the specific helix (1015-1029), but in the structure the preceding loop (1003-1014) is also disordered, so in this structure both the loop and helix are disordered. This is the 16-mer siRNA bound enzyme and represents the cleavage competent state","type":"Curator statement"},{"text":"We propose that our structure of the hDicer PAZ cassette-siRNA 16-mer complex (Figure 6B), where the Dicer-specific segment is disordered/melted, likely reflects the cleavage-competent conformation.","type":"Discussion"}],"curator_id":"vnugnes","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24486018","version":3,"reference_html":"A phosphate-binding pocket within the platform-PAZ-connector helix cassette of human Dicer. <i> Tian Y, Simanshu DK, Ma JB, Park JE, Heo I, Kim VN, Patel DJ. </i> Mol Cell, 2014","date":"2022-06-16T20:12:55.647Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4NHA"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":777,"end":777,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":839,"end":839,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":844,"end":844,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":899,"end":899,"position":"Specific residue"}],"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting RNA sequence 5' GCGUUGGCCAACGCUU."}]}],"sequence_construct":"SDQPCYLYVIGMVLTTPLPDELNFRRRKLYPPEDTTRCFGILTAKPIPQIPHFPVYTRSGEVTISIELKKSGFMLSLQMLELITRLHQYIFSHILRLEKPALEFKPTDADSAYCVLPLNVVNDSSTLDIDFKFMEDIEKSEARIGIPSTKYTKETPFVFKLEDYQDAVIIPRYRNFDQPHRFYVADVYTDLTPLSKFPSPEYETFAEYYKTKYNLDLTNLNQPLLDVDHTSSRLNLLTPRHLNQKGKALPLSSAEKRKAKWESLQNKQILVPELCAIHPIPASLWRKAVCLPSILYRLHCLL"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1013,"region_id":"DP02781r002","start":1003,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"One of the unexpected features of the structure of the hDicer PAZ cassette-siRNA 12-mer complex is the identification of a disordered segment (993-1003), followed by an α-helical segment (1006-1020), with the latter designated the ‘hDicer-specific helix’. This helix extends out from the surface of the protein in a knob-like manner (Figure 1D, E), and in turn orients the bound siRNA duplex at an angle (approximately 60°) away from the surface of the protein","type":"Results"},{"text":"We postulate that the knob-like orientation of the hDicer-specific helix in hDicer PAZ cassette-siRNA 12-mer complex, wherein the bound siRNA is aligned at approximately 60° to the flat surface of the hDicer PAZ cassette, may represent the conformation associated with product release/transfer (Figure 7B)","type":"Discussion"},{"text":"The numbering used by authors is shifted by 10. The disordered segment (993-1003 by the authors) corresponds to residues 1003-1013 in the UNIPROT numbering. In this structure of hDICER with a 12-mer siRNA, the loop preceding the terminal helix (1003-1013) is disordered. This is the 12-mer siRNA bound enzyme and represents the product/release state","type":"Curator statement"}],"curator_id":"vnugnes","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24486018","version":3,"reference_html":"A phosphate-binding pocket within the platform-PAZ-connector helix cassette of human Dicer. <i> Tian Y, Simanshu DK, Ma JB, Park JE, Heo I, Kim VN, Patel DJ. </i> Mol Cell, 2014","date":"2022-06-16T20:03:46.861Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4NGD"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting RNA sequence 5'GCGAAUUCGCUU."}]}]},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":1029,"region_id":"DP02781r003","start":1013,"term_id":"IDPO:0000011","unpublished":true,"statement":[{"text":"One of the unexpected features of the structure of the hDicer PAZ cassette-siRNA 12-mer complex is the identification of a disordered segment (993-1003), followed by an α-helical segment (1006-1020), with the latter designated the ‘hDicer-specific helix’. This helix extends out from the surface of the protein in a knob-like manner (Figure 1D, E), and in turn orients the bound siRNA duplex at an angle (approximately 60°) away from the surface of the protein","type":"Results"},{"text":"Surprisingly, the hDicer-specific-segment, that forms the ‘hDicer-specific helix’ in the structure of hDicer PAZ cassette-siRNA 12-mer complex (Figure 1D) is melted/disordered (spanning residues 1005-1019) in the hDicer PAZ cassette-siRNA 16-mer complex (Figure 6B, dotted red line).","type":"Results"},{"text":"The numbering used by authors is shifted by 10. In the hDICER bound to the 12-mer siRNA, the disordered segment (993-1003 by the authors) corresponds to residues 1003-1013 in the UNIPROT numbering. In the hDICER structure bound to 16-mer siRNA, the disordered segment extends to include the terminal helix (residues 1003-1029) and therefore residues 1014-1029 corresponding to the terminal helix become ordered.","type":"Curator statement"}],"curator_id":"vnugnes","released":"2022_06","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"24486018","version":3,"reference_html":"A phosphate-binding pocket within the platform-PAZ-connector helix cassette of human Dicer. <i> Tian Y, Simanshu DK, Ma JB, Park JE, Heo I, Kim VN, Patel DJ. </i> Mol Cell, 2014","date":"2022-06-16T20:13:34.927Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4NGD"},{"db":"PDB","id":"4NHA"}],"term_name":"disorder to order","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting RNAs sequences 5'GCGAAUUCGCUU and 5' GCGUUGGCCAACGCUU"}]}]}],"released":"2022_06","ncbi_taxon_id":9606,"disprot_id":"DP02781","date":"2020-04-16T00:08:34.685Z","organism":"Homo sapiens","regions_counter":4,"name":"Endoribonuclease Dicer","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI0000044294","uniref100":"UniRef100_Q9UPY3","uniref90":"UniRef90_Q9UPY3","uniref50":"UniRef50_Q8R418","genes":[{"name":{"value":"DICER1"},"synonyms":[{"value":"DICER"},{"value":"HERNA"},{"value":"KIAA0928"}]}],"alphafold_very_low_content":0.2892819979188345,"disorder_content":0.01404786680541103,"disprot_consensus":{"full":[{"start":1003,"end":1012,"type":"D"},{"start":1013,"end":1029,"type":"T"}],"Structural state":[{"start":1003,"end":1029,"type":"D"}],"Structural transition":[{"start":1013,"end":1029,"type":"T"}]}},{"acc":"Q9NPI8","features":{"gene3D":[{"start":151,"end":357,"id":"G3DSA:1.25.40.490","name":"G3DSA:1.25.40.490"}],"pfam":[{"id":"PF11107","name":"Fanconi anemia group F protein (FANCF)","start":1,"end":354}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MESLLQHLDRFSELLAVSSTTYVSTWDPATVRRALQWARYLRHIHRRFGRHGPIRTALERRLHNQWRQEGGFGRGPVPGLANFQALGHCDVLLSLRLLENRALGDAARYHLVQQLFPGPGVRDADEETLQESLARLARRRSAVHMLRFNGYRENPNLQEDSLMKTQAELLLERLQEVGKAEAERPARFLSSLWERLPQNNFLKVIAVALLQPPLSRRPQEELEPGIHKSPGEGSQVLVHWLLGNSEVFAAFCRALPAGLLTLVTSRHPALSPVYLGLLTDWGQRLHYDLQKGIWVGTESQDVPWEELHNRFQSLCQAPPPLKDKVLTALETCKAQDGDFEVPGLSIWTDLLLALRSGAFRKRQVLGLSAGLSSV","length":374,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":234,"region_id":"DP02782r001","start":211,"term_id":"IDPO:0000002","statement":[{"text":"The capping helix α1 is linked to the first hairpin (HP1: helices α2 and α3) through an 11-residue loop that is disordered in the crystals. Hairpins HP1 and HP2 are connected by a highly charged, 23-residue loop L2 (residues 211-234) that is also disordered in the crystals.","type":"Results"},{"text":"The C-terminal domain, CTD, spans residues 156-357 of of FANCF","type":"Curator statement"}],"curator_id":"vnugnes","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"17082180","version":3,"reference_html":"Structural determinants of human FANCF protein that function in the assembly of a DNA damage signaling complex. <i> Kowal P, Gurtan AM, Stuckert P, D'Andrea AD, Ellenberger T. </i> J Biol Chem, 2007","date":"2022-06-16T20:56:41.404Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2IQC"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16793","entry_name":"mercury(2+)"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-27T16:29:44.338Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":188,"region_id":"DP02782r002","start":177,"term_id":"IDPO:0000002","statement":[{"text":"The capping helix α1 is linked to the first hairpin (HP1: helices α2 and α3) through an 11-residue loop that is disordered in the crystals. Hairpins HP1 and HP2 are connected by a highly charged, 23-residue loop L2 (residues 211-234) that is also disordered in the crystals.","type":"Results"},{"text":"The C-terminal domain, CTD, spans residues 156-357 of of FANCF","type":"Curator statement"}],"curator_id":"vnugnes","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"17082180","version":3,"reference_html":"Structural determinants of human FANCF protein that function in the assembly of a DNA damage signaling complex. <i> Kowal P, Gurtan AM, Stuckert P, D'Andrea AD, Ellenberger T. </i> J Biol Chem, 2007","date":"2022-06-16T20:57:01.228Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2IQC"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16793","entry_name":"mercury(2+)"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-27T16:29:43.038Z"}}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02782","date":"2020-04-16T16:47:46.556Z","organism":"Homo sapiens","regions_counter":3,"name":"Fanconi anemia group F protein","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI000012A4CA","uniref100":"UniRef100_Q9NPI8","uniref90":"UniRef90_Q9NPI8","uniref50":"UniRef50_Q9NPI8","genes":[{"name":{"value":"FANCF"}}],"alphafold_very_low_content":0.11497326203208556,"disorder_content":0.0962566844919786,"disprot_consensus":{"full":[{"start":177,"end":188,"type":"D"},{"start":211,"end":234,"type":"D"}],"Structural state":[{"start":177,"end":188,"type":"D"},{"start":211,"end":234,"type":"D"}]}},{"acc":"P49189","features":{"gene3D":[{"start":1,"end":256,"id":"G3DSA:3.40.605.10","name":"Aldehyde Dehydrogenase; Chain A, domain 1"},{"start":257,"end":492,"id":"G3DSA:3.40.309.10","name":"Aldehyde Dehydrogenase; Chain A, domain 2"}],"pfam":[{"id":"PF00171","name":"Aldehyde dehydrogenase family","start":27,"end":483}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MSTGTFVVSQPLNYRGGARVEPADASGTEKAFEPATGRVIATFTCSGEKEVNLAVQNAKAAFKIWSQKSGMERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFKPSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGSVPTGMKIMEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEILDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIYVPEDPKLKDGYYMRPCVLTNCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLAAGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRENGRVTIEYYSQLKTVCVEMGDVESAF","length":494,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":255,"region_id":"DP02783r001","start":232,"term_id":"IDPO:0000002","statement":[{"text":"Moreover, the αβE region consisting of an α-helix and a β-strand of the coenzyme domain at the dimer interface are disordered, likely due to the loss of interactions with the inter-domain linker, which leads to incomplete β-nicotinamide adenine dinucleotide (NAD+) binding pocket.","type":"Abstract"},{"text":"Although the enzyme was co-crystallized with the β-nicotinamide adenine dinucleotide (NAD+) coenzyme, all structures, which are very similar, are devoid of NAD+ and display the same disordered region forming the coenzyme binding site.","type":"Introduction"},{"text":"The αβE region is not visible in the electron density maps thus is highly mobile (Figure 3C,D). The αE helix delineates the coenzyme cavity and possesses conserved residues known to bind the pyrophosphate moiety such as Ser233 and Thr236 (Ser242 and Thr245 in GmALDH9A2). ","type":"Results"},{"text":"This region interacts with the bound NAD+ when present in ALDH structures, and the absence of a bound NAD+ in the HsALDH9A1 structure is in agreement with this largely disordered region.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30914451","version":2,"reference_html":"Kinetic and structural analysis of human ALDH9A1. <i> Končitíková R, Vigouroux A, Kopečná M, Šebela M, Moréra S, Kopečný D. </i> Biosci Rep, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6QAO"},{"db":"PDB","id":"6QAK"},{"db":"PDB","id":"6QAP"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-01-07T15:49:14.988Z"}},{"start":232,"end":257,"reference_id":"32717224","reference_source":"pmid","reference_html":"Inhibition, crystal structures, and in-solution oligomeric structure of aldehyde dehydrogenase 9A1. <i> Wyatt JW, Korasick DA, Qureshi IA, Campbell AC, Gates KS, Tanner JJ. </i> Arch Biochem Biophys, 2020","date":"2026-01-07T16:20:20.637Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"6VR6"}],"region_id":"DP02783r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15846","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"86195","statements":[{"type":"Results","text":"Two structures of ALDH9A1 complexed with NAD+ were determined. A 2.5 Å resolution structure with space group P1 was obtained using enzyme that had been incubated with both NAD+ and DEAB (Table 1)."}],"entry_name":null}],"statement":[{"text":"The αE-βE region of the Rossmann fold (residues 232 – 258) exhibits a well-defined conformation in the P1 NAD+ complex, in contrast to the C222 NAD+-complex and apo enzyme structures in which these residues are disordered.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":232,"end":257,"reference_id":"32717224","reference_source":"pmid","reference_html":"Inhibition, crystal structures, and in-solution oligomeric structure of aldehyde dehydrogenase 9A1. <i> Wyatt JW, Korasick DA, Qureshi IA, Campbell AC, Gates KS, Tanner JJ. </i> Arch Biochem Biophys, 2020","date":"2026-01-07T16:41:09.372Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"6VR6"}],"region_id":"DP02783r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15846","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"86195","statements":[{"type":"Results","text":"Two structures of ALDH9A1 complexed with NAD+ were determined. A 2.5 Å resolution structure with space group P1 was obtained using enzyme that had been incubated with both NAD+ and DEAB (Table 1)."}],"entry_name":null}],"statement":[{"text":"The αE-βE region of the Rossmann fold (residues 232 – 258) exhibits a well-defined conformation in the P1 NAD+ complex, in contrast to the C222 NAD+-complex and apo enzyme structures in which these residues are disordered.","type":"Results"},{"text":"The ordering of αE-βE and the remodeling of the inter-domain linker result in the formation of new tertiary and quaternary structural interactions (Fig. 7).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","states_connection":[{"source":"DP02783r001","target":"DP02783r003"}]},{"start":232,"end":257,"reference_id":"32717224","reference_source":"pmid","reference_html":"Inhibition, crystal structures, and in-solution oligomeric structure of aldehyde dehydrogenase 9A1. <i> Wyatt JW, Korasick DA, Qureshi IA, Campbell AC, Gates KS, Tanner JJ. </i> Arch Biochem Biophys, 2020","date":"2026-01-07T16:18:40.282Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"6VR6"}],"region_id":"DP02783r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15846","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"86195","statements":[{"type":"Results","text":"Two structures of ALDH9A1 complexed with NAD+ were determined. A 2.5 Å resolution structure with space group P1 was obtained using enzyme that had been incubated with both NAD+ and DEAB (Table 1)."}],"entry_name":null}],"statement":[{"text":"The ordering of αE-βE and the remodeling of the inter-domain linker result in the formation of new tertiary and quaternary structural interactions (Fig. 7). For example, βE makes three main chain hydrogen bonds with the inter-domain linker to form a two-stranded anti-parallel β-sheet structure (Fig. 7A).","type":"Results"},{"text":"This interface involves the nonpolar face of αE, which includes Met238, Met241, Ala245, and Ile248. Also, Phe465 of the linker intercalates between the βE strands of two adjacent protomers, forming intermolecular nonpolar contacts with Ile248 and Pro250 (Fig. 7B). In summary, the isomerization of the αE-βE region and the inter-domain linker into their canonical conformations results in the formation of many noncovalent interactions that stabilize the active form of ALDH9A1.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":232,"end":236,"reference_id":"32717224","reference_source":"pmid","reference_html":"Inhibition, crystal structures, and in-solution oligomeric structure of aldehyde dehydrogenase 9A1. <i> Wyatt JW, Korasick DA, Qureshi IA, Campbell AC, Gates KS, Tanner JJ. </i> Arch Biochem Biophys, 2020","date":"2026-01-07T16:18:55.843Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0070403","term_name":"NAD+ binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"6VR6"}],"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"15846","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02783r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"86195","statements":[{"type":"Results","text":"Two structures of ALDH9A1 complexed with NAD+ were determined. A 2.5 Å resolution structure with space group P1 was obtained using enzyme that had been incubated with both NAD+ and DEAB (Table 1)."}],"entry_name":null}],"statement":[{"text":"NAD+ binds in the expected site at the C-termini of the β-strands of the Rossmann fold. NAD+ forms several electrostatic interactions with the protein (Fig. 4A). The adenine ribose hydrogen bonds with Lys180. The pyrophosphate interacts with Trp156, Ser233, and Thr236.","type":"Results"}],"term_comment":"","term_def":"\"Binding to the oxidized form, NAD, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02783","date":"2020-04-16T17:20:42.844Z","organism":"Homo sapiens","regions_counter":6,"name":"4-trimethylaminobutyraldehyde dehydrogenase","dataset":[],"UniParc":"UPI000016A525","uniref100":"UniRef100_P49189","uniref90":"UniRef90_P49189","uniref50":"UniRef50_P49189","genes":[{"name":{"value":"ALDH9A1"},"synonyms":[{"value":"ALDH4"},{"value":"ALDH7"},{"value":"ALDH9","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8786138","url":"http://www.ncbi.nlm.nih.gov/pubmed/8786138","alternativeUrl":"https://europepmc.org/abstract/MED/8786138"}}]}]}],"alphafold_very_low_content":0,"disorder_content":0.05263157894736842,"disprot_consensus":{"full":[{"start":232,"end":257,"type":"T"}],"Structural state":[{"start":232,"end":255,"type":"D"},{"start":256,"end":257,"type":"S"}],"Structural transition":[{"start":232,"end":257,"type":"T"}],"Disorder function":[{"start":232,"end":257,"type":"F"}],"Molecular function":[{"start":232,"end":236,"type":"F"}]}},{"acc":"P16892","features":{"gene3D":[],"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":13,"end":309}]},"creator":"fquaglia","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"sequence":"MPKRIVYNISSDFQLKSLLGEGAYGVVCSATHKPTGEIVAIKKIEPFDKPLFALRTLREIKILKHFKHENIITIFNIQRPDSFENFNEVYIIQELMQTDLHRVISTQMLSDDHIQYFIYQTLRAVKVLHGSNVIHRDLKPSNLLINSNCDLKVCDFGLARIIDESAADNSEPTGQQSGMTEYVATRWYRAPEVMLTSAKYSRAMDVWSCGCILAELFLRRPIFPGRDYRHQLLLIFGIIGTPHSDNDLRCIESPRAREYIKSLPMYPAAPLEKMFPRVNPKGIDLLQRMLVFDPAKRITAKEALEHPYLQTYHDPNDEPEGEPIPPSFFEFDHYKEALTTKDLKKLIWNEIFS","length":353,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":179,"region_id":"DP02784r001","start":164,"term_id":"IDPO:0000002","statement":[{"text":"The final models of npFus3, Fus3VF, Fus3/Ste7_pep1, Fus3/Msg5_pep, and Fus3/Far1_pep contain a full-length model of Fus3 (1–353) interspersed with a flexible segment encompassing part of the activation loop (164–179). This region appears to be flexible and invisible in all the structures.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16364919","version":2,"reference_html":"The role of docking interactions in mediating signaling input, output, and discrimination in the yeast MAPK network. <i> Reményi A, Good MC, Bhattacharyya RP, Lim WA. </i> Mol Cell, 2005","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2B9J"},{"db":"PDB","id":"2B9F"},{"db":"PDB","id":"2B9H"},{"db":"PDB","id":"2B9I"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":559292,"disprot_id":"DP02784","date":"2020-04-16T17:47:46.360Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":1,"name":"Mitogen-activated protein kinase FUS3","dataset":[],"UniParc":"UPI000012AD91","uniref100":"UniRef100_P16892","uniref90":"UniRef90_P16892","uniref50":"UniRef50_P16892","genes":[{"name":{"value":"FUS3"},"synonyms":[{"value":"DAC2"}],"orfNames":[{"value":"YBL03.21"},{"value":"YBL0303"}],"olnNames":[{"value":"YBL016W"}]}],"alphafold_very_low_content":0.04815864022662889,"disorder_content":0.0453257790368272,"disprot_consensus":{"full":[{"start":164,"end":179,"type":"D"}],"Structural state":[{"start":164,"end":179,"type":"D"}]}},{"acc":"P16278","features":{"gene3D":[{"start":306,"end":649,"id":"G3DSA:2.60.120.260","name":"Galactose-binding domain-like"}],"pfam":[{"id":"PF01301","name":"Glycosyl hydrolases family 35","start":40,"end":356},{"id":"PF21317","name":"Beta-galactosidase, first all-beta domain","start":403,"end":515},{"id":"PF21467","name":"Beta-galactosidase, galactose-binding domain","start":549,"end":610}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MPGFLVRILPLLLVLLLLGPTRGLRNATQRMFEIDYSRDSFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLNAIQTYVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVILRPGPYICAEWEMGGLPAWLLEKESILLRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPVITVQVENEYGSYFACDFDYLRFLQKRFRHHLGDDVVLFTTDGAHKTFLKCGALQGLYTTVDFGTGSNITDAFLSQRKCEPKGPLINSEFYTGWLDHWGQPHSTIKTEAVASSLYDILARGASVNLYMFIGGTNFAYWNGANSPYAAQPTSYDYDAPLSEAGDLTEKYFALRNIIQKFEKVPEGPIPPSTPKFAYGKVTLEKLKTVGAALDILCPSGPIKSLYPLTFIQVKQHYGFVLYRTTLPQDCSNPAPLSSPLNGVHDRAYVAVDGIPQGVLERNNVITLNITGKAGATLDLLVENMGRVNYGAYINDFKGLVSNLTLSSNILTDWTIFPLDTEDAVRSHLGGWGHRDSGHHDEAWAHNSSNYTLPAFYMGNFSIPSGIPDLPQDTFIQFPGWTKGQVWINGFNLGRYWPARGPQLTLFVPQHILMTSAPNTITVLELEWAPCSSDDPELCAVTFVDRPVIGSSVTYDHPSKPVEKRLMPPPPQKNKDSWLDHV","length":677,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":544,"region_id":"DP02785r001","start":531,"term_id":"IDPO:0000002","statement":[{"text":"Residues 531–544 were not visible in the electron density maps of the four β-Gal monomers in asymmetric units; therefore, these residues were not modeled.","type":"Results"},{"text":"The crystal structure showed that Arg-530 and Asn545 are separated by about 40 Å, and they point in opposite directions. Therefore, it seems that these residues were connected by a flexible loop before trypsinization. ","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22128166","version":2,"reference_html":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases. <i> Ohto U, Usui K, Ochi T, Yuki K, Satow Y, Shimizu T. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3THC"},{"db":"PDB","id":"3THD"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-03T21:00:23.669Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":544,"region_id":"DP02785r002","start":531,"term_id":"IDPO:0000033","statement":[{"text":"Residues 531–544 were not visible in the electron density maps of the four β-Gal monomers in asymmetric units; therefore, these residues were not modeled.","type":"Results"},{"text":"The crystal structure showed that Arg-530 and Asn545 are separated by about 40 Å, and they point in opposite directions. Therefore, it seems that these residues were connected by a flexible loop before trypsinization. ","type":"Results"},{"text":"Flexible linker connecting β-domain 1 (residues 397–514) and β-domain 2 (residues 545–647)","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22128166","version":3,"reference_html":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases. <i> Ohto U, Usui K, Ochi T, Yuki K, Satow Y, Shimizu T. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3THC"},{"db":"PDB","id":"3THD"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-03T21:00:23.480Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":677,"region_id":"DP02785r003","start":648,"term_id":"IDPO:0000002","statement":[{"text":"Residues after Ser-647 were not visible in the electron density map.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22128166","version":2,"reference_html":"Crystal structure of human β-galactosidase: structural basis of Gm1 gangliosidosis and morquio B diseases. <i> Ohto U, Usui K, Ochi T, Yuki K, Satow Y, Shimizu T. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3THC"},{"db":"PDB","id":"3THD"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-03T20:58:31.492Z"}}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02785","date":"2020-04-16T18:10:18.978Z","organism":"Homo sapiens","regions_counter":3,"name":"Beta-galactosidase","dataset":["NDDs-related proteins"],"UniParc":"UPI0000E9BBE7","uniref100":"UniRef100_P16278","uniref90":"UniRef90_P16278","uniref50":"UniRef50_P16278","genes":[{"name":{"value":"GLB1"},"synonyms":[{"value":"ELNR1"}]}],"alphafold_very_low_content":0.10487444608567208,"disorder_content":0.06499261447562776,"disprot_consensus":{"full":[{"start":531,"end":544,"type":"D"},{"start":648,"end":677,"type":"D"}],"Structural state":[{"start":531,"end":544,"type":"D"},{"start":648,"end":677,"type":"D"}],"Disorder function":[{"start":531,"end":544,"type":"F"}]}},{"acc":"Q9Y823","features":{"gene3D":[{"start":24,"end":300,"id":"G3DSA:3.20.20.70","name":"Aldolase class I"}],"pfam":[{"id":"PF00682","name":"HMGL-like","start":35,"end":294},{"id":"PF22617","name":"Homocitrate synthase post-HMGL domain-like","start":308,"end":388}]},"creator":"fquaglia","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"sequence":"MSVSEANGTETIKPPMNGNPYGPNPSDFLSRVNNFSIIESTLREGEQFANAFFDTEKKIQIAKALDNFGVDYIELTSPVASEQSRQDCEAICKLGLKCKILTHIRCHMDDARVAVETGVDGVDVVIGTSQYLRKYSHGKDMTYIIDSATEVINFVKSKGIEVRFSSEDSFRSDLVDLLSLYKAVDKIGVNRVGIADTVGCATPRQVYDLIRTLRGVVSCDIECHFHNDTGMAIANAYCALEAGATHIDTSILGIGERNGITPLGALLARMYVTDREYITHKYKLNQLRELENLVADAVEVQIPFNNYITGMCAFTHKAGIHAKAILANPSTYEILKPEDFGMSRYVHVGSRLTGWNAIKSRAEQLNLHLTDAQAKELTVRIKKLADVRTLAMDDVDRVLREYHADLSDADRITKEASA","length":418,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":418,"region_id":"DP02786r001","start":406,"term_id":"IDPO:0000002","statement":[{"text":"Subdomain II (residues 351–405) consists of a three-helix bundle composed of α11-α13. The residues after the α13 helix are disordered in SpHCS structures and are not reported here.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19776021","version":2,"reference_html":"Crystal structure and functional analysis of homocitrate synthase, an essential enzyme in lysine biosynthesis. <i> Bulfer SL, Scott EM, Couture JF, Pillus L, Trievel RC. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3IVT"},{"db":"PDB","id":"3IVS"},{"db":"PDB","id":"3IVU"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":141,"region_id":"DP02786r002","start":129,"term_id":"IDPO:0000002","statement":[{"text":"Although the overall alterations between the catalytic domains of the apoenzyme and 2-OG complex are relatively modest (root mean square deviation value of 1.25 Å for all aligned atoms), pronounced structural changes occur in the linker between β4 and α4 that is disordered in the apoenzyme. Binding of 2-OG induces ordering of the linker, resulting in the formation of the 3104 helix and the β4.1-β4.2 hairpin. RES","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19776021","version":2,"reference_html":"Crystal structure and functional analysis of homocitrate synthase, an essential enzyme in lysine biosynthesis. <i> Bulfer SL, Scott EM, Couture JF, Pillus L, Trievel RC. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3IVS"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":141,"region_id":"DP02786r003","start":129,"term_id":"IDPO:0000011","statement":[{"text":"Although the overall alterations between the catalytic domains of the apoenzyme and 2-OG complex are relatively modest (root mean square deviation value of 1.25 Å for all aligned atoms), pronounced structural changes occur in the linker between β4 and α4 that is disordered in the apoenzyme. Binding of 2-OG induces ordering of the linker, resulting in the formation of the 3104 helix and the β4.1-β4.2 hairpin. RES","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19776021","version":2,"reference_html":"Crystal structure and functional analysis of homocitrate synthase, an essential enzyme in lysine biosynthesis. <i> Bulfer SL, Scott EM, Couture JF, Pillus L, Trievel RC. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3IVS"},{"db":"PDB","id":"3IVT"},{"db":"PDB","id":"3IVU"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":333,"region_id":"DP02786r004","start":320,"term_id":"IDPO:0000002","statement":[{"text":"In the structures of the HCS apoenzyme and one of the 2-OG binary complexes, a lid motif from the C-terminal domain occludes the entrance to the active site of the neighboring monomer, whereas in the second 2-OG complex the lid is disordered, suggesting that it regulates substrate access to the active site through its apparent flexibility.","type":"Abstract"},{"text":"In the course of screening crystals of the SpHCS·2-OG complex, we identified two different conformations of the lid motif (residues 320–333) that encloses the entrance to the active site, which we term the closed and open conformations. In the closed lid complex (2.67 Å resolution), the lid motif is clearly visible in the electron density map and obstructs the entrance to the active site, whereas in the open complex (2.72 Å resolution), density for the lid is absent, resulting in a solvent-exposed active site.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19776021","version":2,"reference_html":"Crystal structure and functional analysis of homocitrate synthase, an essential enzyme in lysine biosynthesis. <i> Bulfer SL, Scott EM, Couture JF, Pillus L, Trievel RC. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3IVU"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":333,"region_id":"DP02786r005","start":320,"term_id":"IDPO:0000011","statement":[{"text":"In the structures of the HCS apoenzyme and one of the 2-OG binary complexes, a lid motif from the C-terminal domain occludes the entrance to the active site of the neighboring monomer, whereas in the second 2-OG complex the lid is disordered, suggesting that it regulates substrate access to the active site through its apparent flexibility.","type":"Abstract"},{"text":"In the course of screening crystals of the SpHCS·2-OG complex, we identified two different conformations of the lid motif (residues 320–333) that encloses the entrance to the active site, which we term the closed and open conformations. In the closed lid complex (2.67 Å resolution), the lid motif is clearly visible in the electron density map and obstructs the entrance to the active site, whereas in the open complex (2.72 Å resolution), density for the lid is absent, resulting in a solvent-exposed active site.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19776021","version":2,"reference_html":"Crystal structure and functional analysis of homocitrate synthase, an essential enzyme in lysine biosynthesis. <i> Bulfer SL, Scott EM, Couture JF, Pillus L, Trievel RC. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3IVU"},{"db":"PDB","id":"3IVT"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":333,"region_id":"DP02786r006","start":320,"term_id":"IDPO:0000030","statement":[{"text":"In the structures of the HCS apoenzyme and one of the 2-OG binary complexes, a lid motif from the C-terminal domain occludes the entrance to the active site of the neighboring monomer, whereas in the second 2-OG complex the lid is disordered, suggesting that it regulates substrate access to the active site through its apparent flexibility.","type":"Abstract"},{"text":"In the course of screening crystals of the SpHCS·2-OG complex, we identified two different conformations of the lid motif (residues 320–333) that encloses the entrance to the active site, which we term the closed and open conformations. In the closed lid complex (2.67 Å resolution), the lid motif is clearly visible in the electron density map and obstructs the entrance to the active site, whereas in the open complex (2.72 Å resolution), density for the lid is absent, resulting in a solvent-exposed active site.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19776021","version":3,"reference_html":"Crystal structure and functional analysis of homocitrate synthase, an essential enzyme in lysine biosynthesis. <i> Bulfer SL, Scott EM, Couture JF, Pillus L, Trievel RC. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3IVU"},{"db":"PDB","id":"3IVT"},{"db":"PDB","id":"3IVS"}],"term_name":"entropic chain","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":284812,"disprot_id":"DP02786","date":"2020-04-16T18:39:28.478Z","organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","regions_counter":6,"name":"Homocitrate synthase, mitochondrial","dataset":[],"UniParc":"UPI000006C25C","uniref100":"UniRef100_Q9Y823","uniref90":"UniRef90_Q9Y823","uniref50":"UniRef50_P48570","genes":[{"name":{"value":"lys4"},"orfNames":[{"value":"SPBC1105.02c"}]}],"alphafold_very_low_content":0.04066985645933014,"disorder_content":0.09569377990430622,"disprot_consensus":{"full":[{"start":129,"end":141,"type":"T"},{"start":320,"end":333,"type":"T"},{"start":406,"end":418,"type":"D"}],"Structural state":[{"start":129,"end":141,"type":"D"},{"start":320,"end":333,"type":"D"},{"start":406,"end":418,"type":"D"}],"Structural transition":[{"start":129,"end":141,"type":"T"},{"start":320,"end":333,"type":"T"}],"Disorder function":[{"start":320,"end":333,"type":"F"}]}},{"acc":"P45523","features":{"gene3D":[{"start":26,"end":143,"id":"G3DSA:1.10.287.460","name":"Peptidyl-prolyl cis-trans isomerase, FKBP-type, N-terminal domain"}],"pfam":[{"id":"PF00254","name":"FKBP-type peptidyl-prolyl cis-trans isomerase","start":159,"end":246},{"id":"PF01346","name":"Domain amino terminal to FKBP-type peptidyl-prolyl isomerase","start":46,"end":152}]},"creator":"fquaglia","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"sequence":"MKSLFKVTLLATTMAVALHAPITFAAEAAKPATAADSKAAFKNDDQKSAYALGASLGRYMENSLKEQEKLGIKLDKDQLIAGVQDAFADKSKLSDQEIEQTLQAFEARVKSSAQAKMEKDAADNEAKGKEYREKFAKEKGVKTSSTGLVYQVVEAGKGEAPKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPPNSTLVFDVELLDVKPAPKADAKPEADAKAADSAKK","length":270,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":39,"region_id":"DP02787r001","start":26,"term_id":"IDPO:0000002","statement":[{"text":"The N and C termini of the FkpA polypeptide chain have peptide segments of 14 (in all three structures) and 18 residues (in full-length FkpA), respectively, which could not be identified in the electron density maps of the crystal structures.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14672666","version":2,"reference_html":"Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity. <i> Saul FA, Arié JP, Vulliez-le Normand B, Kahn R, Betton JM, Bentley GA. </i> J Mol Biol, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1Q6I"},{"db":"PDB","id":"1Q6H"},{"db":"PDB","id":"1Q6U"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":114,"region_id":"DP02787r002","start":15,"term_id":"GO:0044183","statement":[{"text":"These results suggest that the chaperone and catalytic activities reside in the N and C-terminal domains, respectively.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"14672666","version":3,"reference_html":"Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity. <i> Saul FA, Arié JP, Vulliez-le Normand B, Kahn R, Betton JM, Bentley GA. </i> J Mol Biol, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1Q6I"},{"db":"PDB","id":"1Q6H"},{"db":"PDB","id":"1Q6U"}],"term_name":"protein folding chaperone","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":270,"region_id":"DP02787r003","start":253,"term_id":"IDPO:0000002","statement":[{"text":"The N and C termini of the FkpA polypeptide chain have peptide segments of 14 (in all three structures) and 18 residues (in full-length FkpA), respectively, which could not be identified in the electron density maps of the crystal structures.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14672666","version":2,"reference_html":"Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity. <i> Saul FA, Arié JP, Vulliez-le Normand B, Kahn R, Betton JM, Bentley GA. </i> J Mol Biol, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1Q6U"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":270,"region_id":"DP02787r004","start":253,"term_id":"IDPO:0000011","statement":[{"text":"The N and C termini of the FkpA polypeptide chain have peptide segments of 14 (in all three structures) and 18 residues (in full-length FkpA), respectively, which could not be identified in the electron density maps of the crystal structures.","type":"Results"},{"text":"Accordingly, the observed mobility of the C-terminal domains of the dimeric molecule could effectively adapt these two independent folding functions of FkpA to polypeptide substrates.","type":"Abstract"},{"text":"The C-domain (residues 115–224) belongs to the FKBP family. This domain has an FK506-binding site characteristic of this protein family, fixing the ligand in the same manner as observed in other FKBP structures that have been determined.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14672666","version":2,"reference_html":"Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity. <i> Saul FA, Arié JP, Vulliez-le Normand B, Kahn R, Betton JM, Bentley GA. </i> J Mol Biol, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1Q6U"},{"db":"PDB","id":"1Q6I"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2021_06","ncbi_taxon_id":83333,"disprot_id":"DP02787","date":"2020-04-16T22:28:46.104Z","organism":"Escherichia coli (strain K12)","regions_counter":4,"name":"FKBP-type peptidyl-prolyl cis-trans isomerase FkpA","dataset":[],"UniParc":"UPI000012A826","uniref100":"UniRef100_P45523","uniref90":"UniRef90_P45523","uniref50":"UniRef50_P45523","genes":[{"name":{"value":"fkpA"},"synonyms":[{"value":"yzzS"}],"olnNames":[{"value":"b3347"},{"value":"JW3309"}]}],"alphafold_very_low_content":0.14814814814814814,"disorder_content":0.11851851851851852,"disprot_consensus":{"full":[{"start":15,"end":25,"type":"F"},{"start":26,"end":39,"type":"D"},{"start":40,"end":114,"type":"F"},{"start":253,"end":270,"type":"T"}],"Structural state":[{"start":26,"end":39,"type":"D"},{"start":253,"end":270,"type":"D"}],"Molecular function":[{"start":15,"end":114,"type":"F"}],"Structural transition":[{"start":253,"end":270,"type":"T"}]}},{"acc":"Q62902","features":{"gene3D":[],"pfam":[{"id":"PF03388","name":"Legume-like lectin family","start":51,"end":281}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"sequence":"MAVSRRRGPQAGAQSFFCALLLSFSQFVGSDGMGGDAAAPGAAGTQAELPHRRFEYKYSFKGPHLVQSDGTVPFWAHAGNAIPSADQIRIAPSLKSQRGSVWTKTKAAFENWEVEVTFRVTGRGRIGADGLAIWYTENQGLDGPVFGSADMWNGVGIFFDSFDNDGKKNNPAIVVVGNNGQINYDHQNDGATQALASCQRDFRNKPYPVRAKITYYQKTLTVMINNGFTPDKNDYEFCAKVENMVIPTQGHFGISAATGGLADDHDVLSFLTFQLTEPGKEPPTPEKDISEKEKEKYQEEFEHFQQELDKKKEEFQKGHPDLQGQPADDIFESIGDRELRQVFEGQNRIHLEIKQLNRQLDMILDEQRRYVSSLTEEISRRGAGTPGQPGQVSQQELDTVVRTQLEILRQVNEMKNSMRETMRLVSGVQHPGSAGVYETTQHFMDIKEHLHIVKRDIDSLAQRSMSSNEKPKCPDLPAFPSCLSTVHFVIFIVVQTVLFIGYIMYRTQQEAAAKKFF","length":517,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":49,"region_id":"DP02789r001","start":31,"term_id":"IDPO:0000002","statement":[{"text":"Residues 31–49 and the 6xHis tag inserted between residues 34 and 35 (23) are not visible in the electron density maps.","type":"Results"},{"text":"The final model contains residues 50–277 of p58, 197 water molecules and 2 sulfate ions.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11850423","version":2,"reference_html":"Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum. <i> Velloso LM, Svensson K, Schneider G, Pettersson RF, Lindqvist Y. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1GV9"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","ncbi_taxon_id":10116,"disprot_id":"DP02789","date":"2020-04-17T09:37:14.209Z","organism":"Rattus norvegicus","regions_counter":1,"name":"Protein ERGIC-53","dataset":[],"UniParc":"UPI00000E5B96","uniref100":"UniRef100_Q62902","uniref90":"UniRef90_Q62902","uniref50":"UniRef50_Q62902","genes":[{"name":{"value":"Lman1"},"synonyms":[{"value":"Ergic53"}]}],"alphafold_very_low_content":0.15860735009671179,"disorder_content":0.0367504835589942,"disprot_consensus":{"full":[{"start":31,"end":49,"type":"D"}],"Structural state":[{"start":31,"end":49,"type":"D"}]}},{"acc":"Q8BTI9","features":{"gene3D":[{"start":317,"end":500,"id":"G3DSA:2.60.40.150","name":"C2 domain"},{"start":850,"end":1054,"id":"G3DSA:1.10.1070.11","name":"Phosphatidylinositol 3-/4-kinase, catalytic domain"},{"start":116,"end":694,"id":"G3DSA:1.25.40.70","name":"G3DSA:1.25.40.70"}],"pfam":[{"id":"PF00454","name":"Phosphatidylinositol 3- and 4-kinase","start":794,"end":1010},{"id":"PF00613","name":"Phosphoinositide 3-kinase family, accessory domain (PIK domain)","start":526,"end":703},{"id":"PF00792","name":"Phosphoinositide 3-kinase C2","start":344,"end":459},{"id":"PF00794","name":"PI3-kinase family, ras-binding domain","start":176,"end":281},{"id":"PF02192","name":"PI3-kinase family, p85-binding domain","start":36,"end":110}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MPPAMADNLDIWAVDSQIASDGAISVDFLLPTGIYIQLEVPREATISYIKQMLWKQVHNYPMFNLLMDIDSYMFACVNQTAVYEELEDETRRLCDVRPFLPVLKLVTRSCDPAEKLDSKIGVLIGKGLHEFDALKDPEVNEFRRKMRKFSEAKIQSLVGLSWIDWLKHTYPPEHEPSVLENLEDKLYGGKLVVAVHFENSQDVFSFQVSPNLNPIKINELAIQKRLTIRGKEDEASPCDYVLQVSGRVEYVFGDHPLIQFQYIRNCVMNRTLPHFILVECCKIKKMYEQEMIAIEAAINRNSSNLPLPLPPKKTRVISHIWDNNNPFQITLVKGNKLNTEETVKVHVRAGLFHGTELLCKTVVSSEISGKNDHIWNEQLEFDINICDLPRMARLCFAVYAVLDKVKTKKSTKTINPSKYQTIRKAGKVHYPVAWVNTMVFDFKGQLRSGDVILHSWSSFPDELEEMLNPMGTVQTNPYAENATALHITFPENKKQPCYYPPFDKIIEKAAELASGDSANVSSRGGKKFLAVLKEILDRDPLSQLCENEMDLIWTLRQDCRENFPQSLPKLLLSIKWNKLEDVAQLQALLQIWPKLPPREALELLDFNYPDQYVREYAVGCLRQMSDEELSQYLLQLVQVLKYEPFLDCALSRFLLERALDNRRIGQFLFWHLRSEVHTPAVSVQFGVILEAYCRGSVGHMKVLSKQVEALNKLKTLNSLIKLNAVKLSRAKGKEAMHTCLKQSAYREALSDLQSPLNPCVILSELYVEKCKYMDSKMKPLWLVYSSRAFGEDSVGVIFKNGDDLRQDMLTLQMLRLMDLLWKEAGLDLRMLPYGCLATGDRSGLIEVVSTSETIADIQLNSSNVAATAAFNKDALLNWLKEYNSGDDLDRAIEEFTLSCAGYCVASYVLGIGDRHSDNIMVKKTGQLFHIDFGHILGNFKSKFGIKRERVPFILTYDFIHVIQQGKTGNTEKFGRFRQCCEDAYLILRRHGNLFITLFALMLTAGLPELTSVKDIQYLKDSLALGKSEEEALKQFKQKFDEALRESWTTKVNWMAHTVRKDYRS","length":1064,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":12,"region_id":"DP02790r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"The structure of p110β has residues 1-12, 228-234, 299-319, 402-431, 514-524 and 1058-1064 disordered.","type":"Supplementary material"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21362552","version":2,"reference_html":"Structure of lipid kinase p110β/p85β elucidates an unusual SH2-domain-mediated inhibitory mechanism. <i> Zhang X, Vadas O, Perisic O, Anderson KE, Clark J, Hawkins PT, Stephens LR, Williams RL. </i> Mol Cell, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2Y3A"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":319,"region_id":"DP02790r002","start":299,"term_id":"IDPO:0000002","statement":[{"text":"The structure of p110β has residues 1-12, 228-234, 299-319, 402-431, 514-524 and 1058-1064 disordered.","type":"Supplementary material"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21362552","version":2,"reference_html":"Structure of lipid kinase p110β/p85β elucidates an unusual SH2-domain-mediated inhibitory mechanism. <i> Zhang X, Vadas O, Perisic O, Anderson KE, Clark J, Hawkins PT, Stephens LR, Williams RL. </i> Mol Cell, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2Y3A"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":431,"region_id":"DP02790r003","start":402,"term_id":"IDPO:0000002","statement":[{"text":"The structure of p110β has residues 1-12, 228-234, 299-319, 402-431, 514-524 and 1058-1064 disordered.","type":"Supplementary material"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21362552","version":2,"reference_html":"Structure of lipid kinase p110β/p85β elucidates an unusual SH2-domain-mediated inhibitory mechanism. <i> Zhang X, Vadas O, Perisic O, Anderson KE, Clark J, Hawkins PT, Stephens LR, Williams RL. </i> Mol Cell, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2Y3A"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":524,"region_id":"DP02790r004","start":514,"term_id":"IDPO:0000002","statement":[{"text":"The structure of p110β has residues 1-12, 228-234, 299-319, 402-431, 514-524 and 1058-1064 disordered.","type":"Supplementary material"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21362552","version":2,"reference_html":"Structure of lipid kinase p110β/p85β elucidates an unusual SH2-domain-mediated inhibitory mechanism. <i> Zhang X, Vadas O, Perisic O, Anderson KE, Clark J, Hawkins PT, Stephens LR, Williams RL. </i> Mol Cell, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2Y3A"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":319,"region_id":"DP02790r005","start":299,"term_id":"IDPO:0000033","statement":[{"text":"Flexible linker connecting RBD domain and C2 domain","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21362552","version":3,"reference_html":"Structure of lipid kinase p110β/p85β elucidates an unusual SH2-domain-mediated inhibitory mechanism. <i> Zhang X, Vadas O, Perisic O, Anderson KE, Clark J, Hawkins PT, Stephens LR, Williams RL. </i> Mol Cell, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2Y3A"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":10090,"disprot_id":"DP02790","date":"2020-04-17T09:44:41.065Z","organism":"Mus musculus","regions_counter":5,"name":"Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform","dataset":[],"UniParc":"UPI00000EAB6E","uniref100":"UniRef100_Q8BTI9","uniref90":"UniRef90_P42338","uniref50":"UniRef50_P42338","genes":[{"name":{"value":"Pik3cb"}}],"alphafold_very_low_content":0.042293233082706765,"disorder_content":0.06954887218045112,"disprot_consensus":{"full":[{"start":1,"end":12,"type":"D"},{"start":299,"end":319,"type":"D"},{"start":402,"end":431,"type":"D"},{"start":514,"end":524,"type":"D"}],"Structural state":[{"start":1,"end":12,"type":"D"},{"start":299,"end":319,"type":"D"},{"start":402,"end":431,"type":"D"},{"start":514,"end":524,"type":"D"}],"Disorder function":[{"start":299,"end":319,"type":"F"}]}},{"acc":"O08908","features":{"gene3D":[{"start":110,"end":292,"id":"G3DSA:1.10.555.10","name":"Rho GTPase activation protein"},{"start":608,"end":722,"id":"G3DSA:3.30.505.10","name":"SH2 domain"},{"start":608,"end":722,"id":"G3DSA:3.30.505.10","name":"SH2 domain"}],"pfam":[{"id":"PF00017","name":"SH2 domain","start":324,"end":399},{"id":"PF00017","name":"SH2 domain","start":616,"end":690},{"id":"PF00620","name":"RhoGAP domain","start":125,"end":258},{"id":"PF16454","name":"Phosphatidylinositol 3-kinase regulatory subunit P85 inter-SH2 domain","start":422,"end":590}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MAGAEGFQYRAVYPFRRERPEDLELLPGDLLVVSRVALQALGVADGGERCPHNVGWMPGFNERTRQRGDFPGTYVEFLGPVALARPGPRPRGPRPLPARPLDGSSESGHILPDLAEQFSPPDPAPPILVKLVEAIEQAELDSECYSKPELPATRTDWSLSDLEQWDRTALYDAVKGFLLALPAAVVTPEAAAEAYRALREVAGPVGLVLEPPTLPLHQALTLRFLLQHLGRVARRAPSPDTAVHALASAFGPLLLRIPPSGGEGDGSEPVPDFPVLLLERLVQEHVEEQDAAPPALPPKPSKAKPAPTALANGGSPPSLQDAEWYWGDISREEVNERLRDTPDGTFLVRDASSKIQGEYTLTLRKGGNNKLIKVFHRDGHYGFSEPLTFCSVVELISHYRHESLAQYNAKLDTRLLYPVSKYQQDQVVKEDSIEAVGAQLKVYHQQYQDKSREYDQLYEEYTRTSQELQMKRTAIEAFNETIKIFEEQGQTQEKCSKEYLERFRREGNEKEMQRILLNSERLKSRIAEIHESRTKLEQDLRAQASDNREIDKRMNSLKPDLMQLRKIRDQYLVWLTQKGARQRKINEWLGIKNETEDQYSLMEDEDALPHHEERTWYVGKINRTQAEEMLSGKRDGTFLIRESSQRGCYACSVVVDGDTKHCVIYRTATGFGFAEPYNLYGSLKELVLHYQHASLVQHNDALTVTLAHPVRAPGPGPPSAAR","length":722,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":440,"region_id":"DP02791r001","start":423,"term_id":"IDPO:0000002","statement":[{"text":"The regulatory p85β structure has residues 423-440, 501-507, 576-607 and 715-722 disordered.","type":"Supplementary material"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21362552","version":2,"reference_html":"Structure of lipid kinase p110β/p85β elucidates an unusual SH2-domain-mediated inhibitory mechanism. <i> Zhang X, Vadas O, Perisic O, Anderson KE, Clark J, Hawkins PT, Stephens LR, Williams RL. </i> Mol Cell, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2Y3A"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":607,"region_id":"DP02791r002","start":576,"term_id":"IDPO:0000002","statement":[{"text":"The regulatory p85β structure has residues 423-440, 501-507, 576-607 and 715-722 disordered.","type":"Supplementary material"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21362552","version":2,"reference_html":"Structure of lipid kinase p110β/p85β elucidates an unusual SH2-domain-mediated inhibitory mechanism. <i> Zhang X, Vadas O, Perisic O, Anderson KE, Clark J, Hawkins PT, Stephens LR, Williams RL. </i> Mol Cell, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2Y3A"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":440,"region_id":"DP02791r003","start":423,"term_id":"IDPO:0000033","statement":[{"text":"Flexible linker connecting nSH2 domain and iSH2 domain","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21362552","version":3,"reference_html":"Structure of lipid kinase p110β/p85β elucidates an unusual SH2-domain-mediated inhibitory mechanism. <i> Zhang X, Vadas O, Perisic O, Anderson KE, Clark J, Hawkins PT, Stephens LR, Williams RL. </i> Mol Cell, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2Y3A"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":607,"region_id":"DP02791r004","start":576,"term_id":"IDPO:0000033","statement":[{"text":"Flexible linker connecting iSH2 domain and cSH2 domain","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21362552","version":3,"reference_html":"Structure of lipid kinase p110β/p85β elucidates an unusual SH2-domain-mediated inhibitory mechanism. <i> Zhang X, Vadas O, Perisic O, Anderson KE, Clark J, Hawkins PT, Stephens LR, Williams RL. </i> Mol Cell, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2Y3A"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":607,"region_id":"DP02791r005","start":576,"term_id":"IDPO:0000045","statement":[{"text":"Another conserved Tyr modified by phosphorylation is in the iSH2-cSH2 linker\n(Tyr607-Hsp85α, Tyr605-Hsp85β, Tyr341-Hsp55γ, Tyr599-Mmp85β).","type":"Supplementary material"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21362552","version":2,"reference_html":"Structure of lipid kinase p110β/p85β elucidates an unusual SH2-domain-mediated inhibitory mechanism. <i> Zhang X, Vadas O, Perisic O, Anderson KE, Clark J, Hawkins PT, Stephens LR, Williams RL. </i> Mol Cell, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2Y3A"}],"term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2020_12","ncbi_taxon_id":10090,"disprot_id":"DP02791","date":"2020-04-17T10:14:01.780Z","organism":"Mus musculus","regions_counter":5,"name":"Phosphatidylinositol 3-kinase regulatory subunit beta","dataset":["Stress response proteins"],"UniParc":"UPI000024DFD5","uniref100":"UniRef100_O08908","uniref90":"UniRef90_O08908","uniref50":"UniRef50_O00459","genes":[{"name":{"value":"Pik3r2"}}],"alphafold_very_low_content":0.11911357340720222,"disorder_content":0.06925207756232687,"disprot_consensus":{"full":[{"start":423,"end":440,"type":"D"},{"start":576,"end":607,"type":"D"}],"Structural state":[{"start":423,"end":440,"type":"D"},{"start":576,"end":607,"type":"D"}],"Disorder function":[{"start":423,"end":440,"type":"F"},{"start":576,"end":607,"type":"F"}]}},{"acc":"P42337","features":{"gene3D":[{"start":853,"end":1068,"id":"G3DSA:1.10.1070.11","name":"Phosphatidylinositol 3-/4-kinase, catalytic domain"}],"pfam":[{"id":"PF00454","name":"Phosphatidylinositol 3- and 4-kinase","start":798,"end":1015},{"id":"PF00613","name":"Phosphoinositide 3-kinase family, accessory domain (PIK domain)","start":520,"end":703},{"id":"PF00792","name":"Phosphoinositide 3-kinase C2","start":351,"end":483},{"id":"PF00794","name":"PI3-kinase family, ras-binding domain","start":174,"end":291},{"id":"PF02192","name":"PI3-kinase family, p85-binding domain","start":32,"end":107}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MPPRPSSGELWGIHLMPPRILVECLLPNGMIVTLECLREATLVTIKHELFREARKYPLHQLLQDETSYIFVSVTQEAEREEFFDETRRLCDLRLFQPFLKVIEPVGNREEKILNREIGFVIGMPVCEFDMVKDPEVQDFRRNILNVCKEAVDLRDLNSPHSRAMYVYPPNVESSPELPKHIYNKLDKGQIIVVIWVIVSPNNDKQKYTLKINHDCVPEQVIAEAIRKKTRSMLLSSEQLKLCVLEYQGKYILKVCGCDEYFLEKYPLSQYKYIRSCIMLGRMPNLMLMAKESLYSQLPIDSFTMPSYSRRISTATPYMNGETSTKSLWVINSALRIKILCATYVNVNIRDIDKIYVRTGIYHGGEPLCDNVNTQRVPCSNPRWNEWLNYDIYIPDLPRAARLCLSICSVKGRKGAKEEHCPLAWGNINLFDYTDTLVSGKMALNLWPVPHGLEDLLNPIGVTGSNPNKETPCLELEFDWFSSVVKFPDMSVIEEHANWSVSREAGFSYSHTGLSNRLARDNELRENDKEQLRALCTRDPLSEITEQEKDFLWSHRHYCVTIPEILPKLLLSVKWNSRDEVAQMYCLVKDWPPIKPEQAMELLDCNYPDPMVRSFAVRCLEKYLTDDKLSQYLIQLVQVLKYEQYLDNLLVRFLLKKALTNQRIGHFFFWHLKSEMHNKTVSQRFGLLLESYCRACGMYLKHLNRQVEAMEKLINLTDILKQEKKDETQKVQMKFLVEQMRQPDFMDALQGFLSPLNPAHQLGNLRLEECRIMSSAKRPLWLNWENPDIMSELLFQNNEIIFKNGDDLRQDMLTLQIIRIMENIWQNQGLDLRMLPYGCLSIGDCVGLIEVVRNSHTIMQIQCKGGLKGALQFNSHTLHQWLKDKNKGEIYDAAIDLFTRSCAGYCVATFILGIGDRHNSNIMVKDDGQLFHIDFGHFLDHKKKKFGYKRERVPFVLTQDFLIVISKGAQEYTKTREFERFQEMCYKAYLAIRQHANLFINLFSMMLGSGMPELQSFDDIAYIRKTLALDKTEQEALEYFTKQMNDAHHGGWTTKMDWIFHTIKQHALN","length":1068,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":322,"region_id":"DP02792r001","start":310,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Flexible linker between RBD domain and C2 domain","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22120714","version":2,"reference_html":"Regulation of lipid binding underlies the activation mechanism of class IA PI3-kinases. <i> Hon WC, Berndt A, Williams RL. </i> Oncogene, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4A55"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":322,"region_id":"DP02792r002","start":310,"term_id":"IDPO:0000033","unpublished":true,"statement":[{"text":"Flexible linker between RBD domain and C2 domain","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22120714","version":3,"reference_html":"Regulation of lipid binding underlies the activation mechanism of class IA PI3-kinases. <i> Hon WC, Berndt A, Williams RL. </i> Oncogene, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4A55"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":525,"region_id":"DP02792r003","start":501,"term_id":"IDPO:0000033","unpublished":true,"statement":[{"text":"Flexible linker between C2 domain and PIK domain","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22120714","version":3,"reference_html":"Regulation of lipid binding underlies the activation mechanism of class IA PI3-kinases. <i> Hon WC, Berndt A, Williams RL. </i> Oncogene, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4A55"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":525,"region_id":"DP02792r004","start":501,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Flexible linker between C2 domain and PIK domain","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22120714","version":2,"reference_html":"Regulation of lipid binding underlies the activation mechanism of class IA PI3-kinases. <i> Hon WC, Berndt A, Williams RL. </i> Oncogene, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4A55"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_12","ncbi_taxon_id":10090,"disprot_id":"DP02792","date":"2020-04-17T11:27:28.950Z","organism":"Mus musculus","regions_counter":4,"name":"Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform","dataset":[],"UniParc":"UPI0000027AB6","uniref100":"UniRef100_P42337","uniref90":"UniRef90_P42336","uniref50":"UniRef50_P42336","genes":[{"name":{"value":"Pik3ca"}}],"alphafold_very_low_content":0.016853932584269662,"disorder_content":0.035580524344569285,"disprot_consensus":{"full":[{"start":310,"end":322,"type":"D"},{"start":501,"end":525,"type":"D"}],"Structural state":[{"start":310,"end":322,"type":"D"},{"start":501,"end":525,"type":"D"}],"Disorder function":[{"start":310,"end":322,"type":"F"},{"start":501,"end":525,"type":"F"}]}},{"acc":"Q63716","features":{"gene3D":[{"start":3,"end":199,"id":"G3DSA:3.40.30.10","name":"Glutaredoxin"}],"pfam":[{"id":"PF00578","name":"AhpC/TSA family","start":8,"end":141},{"id":"PF10417","name":"C-terminal domain of 1-Cys peroxiredoxin","start":162,"end":197}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"sequence":"MSSGNAKIGHPAPSFKATAVMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAWINTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITINDLPVGRSVDEILRLVQAFQFTDKHGEVCPAGWKPGSDTIKPDVNKSKEYFSKQK","length":199,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":199,"region_id":"DP02793r001","start":176,"term_id":"IDPO:0000002","statement":[{"text":"The C-terminal ≈20 residues of HBP23 corresponding to the N-terminal half of this ORF6 subdomain are disordered in the crystal as described.","type":"Results"},{"text":"The current structure of HBP23 consists of 173 residues (3–175); the N-terminal 2 and the C-terminal 24 residues (176–199) are not included in the model because of their weak electron densities.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10535922","version":2,"reference_html":"Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product. <i> Hirotsu S, Abe Y, Okada K, Nagahara N, Hori H, Nishino T, Hakoshima T. </i> Proc Natl Acad Sci U S A, 1999","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1QQ2"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","ncbi_taxon_id":10116,"disprot_id":"DP02793","date":"2020-04-17T14:58:24.048Z","organism":"Rattus norvegicus","regions_counter":1,"name":"Peroxiredoxin-1","dataset":[],"UniParc":"UPI00001314E2","uniref100":"UniRef100_Q63716","uniref90":"UniRef90_Q06830","uniref50":"UniRef50_Q06830","genes":[{"name":{"value":"Prdx1"},"synonyms":[{"value":"Tdpx2"}]}],"alphafold_very_low_content":0,"disorder_content":0.12060301507537688,"disprot_consensus":{"full":[{"start":176,"end":199,"type":"D"}],"Structural state":[{"start":176,"end":199,"type":"D"}]}},{"acc":"P22234","features":{"gene3D":[{"start":265,"end":423,"id":"G3DSA:3.40.50.7700","name":"PurE domain"}],"pfam":[{"id":"PF00731","name":"AIR carboxylase","start":267,"end":404},{"id":"PF01259","name":"SAICAR synthetase","start":12,"end":238}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MATAEVLNIGKKLYEGKTKEVYELLDSPGKVLLQSKDQITAGNAARKNHLEGKAAISNKITSCIFQLLQEAGIKTAFTRKCGETAFIAPQCEMIPIEWVCRRIATGSFLKRNPGVKEGYKFYPPKVELFFKDDANNDPQWSEEQLIAAKFCFAGLLIGQTEVDIMSHATQAIFEILEKSWLPQNCTLVDMKIEFGVDVTTKEIVLADVIDNDSWRLWPSGDRSQQKDKQSYRDLKEVTPEGLQMVKKNFEWVAERVELLLKSESQCRVVVLMGSTSDLGHCEKIKKACGNFGIPCELRVTSAHKGPDETLRIKAEYEGDGIPTVFVAVAGRSNGLGPVMSGNTAYPVISCPPLTPDWGVQDVWSSLRLPSGLGCSTVLSPEGSAQFAAQIFGLSNHLVWSKLRASILNTWISLKQADKKIRECNL","length":425,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":51,"region_id":"DP02794r001","start":37,"term_id":"IDPO:0000002","statement":[{"text":"Several regions of the polypeptide chain, including residues Met1–Val6, Asp37–Glu51, and Asp221–Thr238, were not visible in the electron density map and assumed being disordered in the crystal.","type":"Results"},{"text":"All three above-mentioned disordered regions in the PAICS crystal structure are located in the SAICARs domain.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17224163","version":2,"reference_html":"Octameric structure of the human bifunctional enzyme PAICS in purine biosynthesis. <i> Li SX, Tong YP, Xie XC, Wang QH, Zhou HN, Han Y, Zhang ZY, Gao W, Li SG, Zhang XC, Bi RC. </i> J Mol Biol, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2H31"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":238,"region_id":"DP02794r002","start":221,"term_id":"IDPO:0000002","statement":[{"text":"Several regions of the polypeptide chain, including residues Met1–Val6, Asp37–Glu51, and Asp221–Thr238, were not visible in the electron density map and assumed being disordered in the crystal.","type":"Results"},{"text":"All three above-mentioned disordered regions in the PAICS crystal structure are located in the SAICARs domain.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17224163","version":2,"reference_html":"Octameric structure of the human bifunctional enzyme PAICS in purine biosynthesis. <i> Li SX, Tong YP, Xie XC, Wang QH, Zhou HN, Han Y, Zhang ZY, Gao W, Li SG, Zhang XC, Bi RC. </i> J Mol Biol, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2H31"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02794","date":"2020-04-17T15:35:10.416Z","organism":"Homo sapiens","regions_counter":2,"name":"Multifunctional protein ADE2","dataset":[],"UniParc":"UPI000042AB67","uniref100":"UniRef100_P22234","uniref90":"UniRef90_P22234","uniref50":"UniRef50_P22234","genes":[{"name":{"value":"PAICS","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:8587","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8587"}}]},"synonyms":[{"value":"ADE2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"2253271","url":"http://www.ncbi.nlm.nih.gov/pubmed/2253271","alternativeUrl":"https://europepmc.org/abstract/MED/2253271"}}]},{"value":"AIRC"},{"value":"PAIS"}]}],"alphafold_very_low_content":0.007058823529411765,"disorder_content":0.07764705882352942,"disprot_consensus":{"full":[{"start":37,"end":51,"type":"D"},{"start":221,"end":238,"type":"D"}],"Structural state":[{"start":37,"end":51,"type":"D"},{"start":221,"end":238,"type":"D"}]}},{"acc":"Q9NV23","features":{"gene3D":[{"start":7,"end":265,"id":"G3DSA:3.40.50.1820","name":"G3DSA:3.40.50.1820"}],"pfam":[{"id":"PF00975","name":"Thioesterase domain","start":28,"end":252}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MERGDQPKRTRNENIFNCLYKNPEATFKLICFPWMGGGSTHFAKWGQDTHDLLEVHSLRLPGRESRVEEPLENDISQLVDEVVCALQPVIQDKPFAFFGHSMGSYIAFRTALGLKENNQPEPLHLFLSSATPVHSKAWHRIPKDDELSEEQISHYLMEFGGTPKHFAEAKEFVKQCSPIIRADLNIVRSCTSNVPSKAVLSCDLTCFVGSEDIAKDMEAWKDVTSGNAKIYQLPGGHFYLLDPANEKLIKNYIIKCLEVSSISNF","length":265,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":24,"region_id":"DP02795r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"The final model only contained residues 25–58, 77–158, and 166–265.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26663084","version":2,"reference_html":"Crystal Structure and Substrate Specificity of Human Thioesterase 2: INSIGHTS INTO THE MOLECULAR BASIS FOR THE MODULATION OF FATTY ACID SYNTHASE. <i> Ritchie MK, Johnson LC, Clodfelter JE, Pemble CW, Fulp BE, Furdui CM, Kridel SJ, Lowther WT. </i> J Biol Chem, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4XJV"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":76,"region_id":"DP02795r002","start":59,"term_id":"IDPO:0000002","statement":[{"text":"The final model only contained residues 25–58, 77–158, and 166–265.","type":"Results"},{"text":"The remaining coil and short helical sections of the capping domain and the backside of the molecule exhibit 2–3-fold higher B-values or are missing in the electron density (residues 59–76 and 159–165).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26663084","version":2,"reference_html":"Crystal Structure and Substrate Specificity of Human Thioesterase 2: INSIGHTS INTO THE MOLECULAR BASIS FOR THE MODULATION OF FATTY ACID SYNTHASE. <i> Ritchie MK, Johnson LC, Clodfelter JE, Pemble CW, Fulp BE, Furdui CM, Kridel SJ, Lowther WT. </i> J Biol Chem, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4XJV"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":76,"region_id":"DP02795r003","start":59,"term_id":"IDPO:0000002","statement":[{"text":"The final model only contained residues 25–58, 77–158, and 166–265.","type":"Results"},{"text":"The remaining coil and short helical sections of the capping domain and the backside of the molecule exhibit 2–3-fold higher B-values or are missing in the electron density (residues 59–76 and 159–165).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26663084","version":2,"reference_html":"Crystal Structure and Substrate Specificity of Human Thioesterase 2: INSIGHTS INTO THE MOLECULAR BASIS FOR THE MODULATION OF FATTY ACID SYNTHASE. <i> Ritchie MK, Johnson LC, Clodfelter JE, Pemble CW, Fulp BE, Furdui CM, Kridel SJ, Lowther WT. </i> J Biol Chem, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4XJV"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","ncbi_taxon_id":9606,"disprot_id":"DP02795","date":"2020-04-17T15:54:22.701Z","organism":"Homo sapiens","regions_counter":3,"name":"S-acyl fatty acid synthase thioesterase, medium chain","dataset":[],"UniParc":"UPI0000047465","uniref100":"UniRef100_Q9NV23","uniref90":"UniRef90_Q9NV23","uniref50":"UniRef50_P08635","genes":[{"name":{"value":"OLAH","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:25625","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:25625"}}]},"synonyms":[{"value":"THEDC1"}]}],"alphafold_very_low_content":0.04150943396226415,"disorder_content":0.15849056603773584,"disprot_consensus":{"full":[{"start":1,"end":24,"type":"D"},{"start":59,"end":76,"type":"D"}],"Structural state":[{"start":1,"end":24,"type":"D"},{"start":59,"end":76,"type":"D"}]}},{"acc":"Q56026","features":{"gene3D":[{"start":36,"end":343,"id":"G3DSA:1.20.1710.10","name":"IpaD-like"}],"pfam":[{"id":"PF06511","name":"Type III secretion systems tip complex components","start":5,"end":341}]},"creator":"fquaglia","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"],"sequence":"MLNIQNYSASPHPGIVAERPQTPSASEHVETAVVPSTTEHRGTDIISLSQAATKIHQAQQTLQSTPPISEENNDERTLARQQLTSSLNALAKSGVSLSAEQNENLRSAFSAPTSALFSASPMAQPRTTISDAEIWDMVSQNISAIGDSYLGVYENVVAVYTDFYQAFSDILSKMGGWLLPGKDGNTVKLDVTSLKNDLNSLVNKYNQINSNTVLFPAQSGSGVKVATEAEARQWLSELNLPNSCLKSYGSGYVVTVDLTPLQKMVQDIDGLGAPGKDSKLEMDNAKYQAWQSGFKAQEENMKTTLQTLTQKYSNANSLYDNLVKVLSSTISSSLETAKSFLQG","length":343,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":131,"region_id":"DP02796r001","start":111,"term_id":"IDPO:0000002","statement":[{"text":"The crystal structures of SipD in the apo and bound forms are nearly identical (Fig. 1 and Supporting Information Fig. S2). For the SipD-deoxycholate crystal (Fig. 1), the final model includes residues 39-342 for molecule A and 46-336 for molecule B. However, residues 110-132 in molecule A and residues 92-94 and 118-134 in molecule B can not be fit to the electron density due to disorder.","type":"Results"}],"curator_id":"vnugnes","released":"2025_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"21031487","version":3,"reference_html":"The crystal structures of the Salmonella type III secretion system tip protein SipD in complex with deoxycholate and chenodeoxycholate. <i> Chatterjee S, Zhong D, Nordhues BA, Battaile KP, Lovell S, De Guzman RN. </i> Protein Sci, 2011","date":"2025-02-10T15:46:06.275Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3NZZ"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":21,"reference_id":"21829362","reference_source":"pmid","reference_html":"Crystal structure of PrgI-SipD: insight into a secretion competent state of the type three secretion system needle tip and its interaction with host ligands. <i> Lunelli M, Hurwitz R, Lambers J, Kolbe M. </i> PLoS Pathog, 2011","date":"2025-02-10T15:49:53.484Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP02796r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":"glycerol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"In SipD crystals, as in the crystal structures of IpaD [16] and BipD [17], the N-terminal 31, 38 or 29 amino acids, respectively, were not defined.","type":"Results"}]},{"start":1,"end":21,"reference_id":"21829362","reference_source":"pmid","reference_html":"Crystal structure of PrgI-SipD: insight into a secretion competent state of the type three secretion system needle tip and its interaction with host ligands. <i> Lunelli M, Hurwitz R, Lambers J, Kolbe M. </i> PLoS Pathog, 2011","date":"2025-02-10T15:50:01.712Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP02796r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":"glycerol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"In SipD crystals, as in the crystal structures of IpaD [16] and BipD [17], the N-terminal 31, 38 or 29 amino acids, respectively, were not defined.","type":"Results"}]}],"released":"2025_06","ncbi_taxon_id":99287,"disprot_id":"DP02796","date":"2020-04-17T22:21:00.948Z","organism":"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","regions_counter":3,"name":"Cell invasion protein SipD","dataset":["Bacterial virulence-related proteins"],"UniParc":"UPI00000D0143","uniref100":"UniRef100_Q56026","uniref90":"UniRef90_Q56026","uniref50":"UniRef50_Q56026","genes":[{"name":{"value":"sipD"},"synonyms":[{"value":"sspD"}],"olnNames":[{"value":"STM2883"}]}],"alphafold_very_low_content":0.12244897959183673,"disorder_content":0.12244897959183673,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"},{"start":111,"end":131,"type":"D"}],"Structural state":[{"start":1,"end":21,"type":"D"},{"start":111,"end":131,"type":"D"}],"Disorder function":[{"start":1,"end":21,"type":"F"}]}},{"acc":"P20061","features":{"gene3D":[],"pfam":[{"id":"PF01122","name":"Eukaryotic cobalamin-binding protein","start":9,"end":328},{"id":"PF14478","name":"Domain of unknown function (DUF4430)","start":355,"end":432}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MRQSHQLPLVGLLLFSFIPSQLCEICEVSEENYIRLKPLLNTMIQSNYNRGTSAVNVVLSLKLVGIQIQTLMQKMIQQIKYNVKSRLSDVSSGELALIILALGVCRNAEENLIYDYHLIDKLENKFQAEIENMEAHNGTPLTNYYQLSLDVLALCLFNGNYSTAEVVNHFTPENKNYYFGSQFSVDTGAMAVLALTCVKKSLINGQIKADEGSLKNISIYTKSLVEKILSEKKENGLIGNTFSTGEAMQALFVSSDYYNENDWNCQQTLNTVLTEISQGAFSNPNAAAQVLPALMGKTFLDINKDSSCVSASGNFNISADEPITVTPPDSQSYISVNYSVRINETYFTNVTVLNGSVFLSVMEKAQKMNDTIFGFTMEERSWGPYITCIQGLCANNNDRTYWELLSGGEPLSQGAGSYVVRNGENLEVRWSKY","length":433,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":330,"region_id":"DP02797r001","start":318,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"In contrast to the crystal structure of human TC, the HC linker does not participate in crystal contacts over its full length and is largely disordered (residues 296–307).","type":"Results"},{"text":"It comprises two globular domains, the N-terminal α-domain (residues 1–287) and the C-terminal β-domain (residues 309–410), which are connected by a flexible linker","type":"Results"},{"text":"Flexible linker between cobalamin binding domain and globular c-terminal beta domain. Residue numbers in the publication refer to multiple sequence alignment in Figure 2 and not to the protein sequence.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23846701","version":2,"reference_html":"Structural basis for universal corrinoid recognition by the cobalamin transport protein haptocorrin. <i> Furger E, Frei DC, Schibli R, Fischer E, Prota AE. </i> J Biol Chem, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4KKJ"},{"db":"PDB","id":"4KKI"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-06T14:47:45.655Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":330,"region_id":"DP02797r002","start":318,"term_id":"IDPO:0000033","unpublished":true,"statement":[{"text":"In contrast to the crystal structure of human TC, the HC linker does not participate in crystal contacts over its full length and is largely disordered (residues 296–307).","type":"Results"},{"text":"It comprises two globular domains, the N-terminal α-domain (residues 1–287) and the C-terminal β-domain (residues 309–410), which are connected by a flexible linker","type":"Results"},{"text":"Flexible linker between cobalamin binding domain and globular c-terminal beta domain. Residue numbers in the publication refer to multiple sequence alignment of Figure 2 and not to the protein sequence.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23846701","version":3,"reference_html":"Structural basis for universal corrinoid recognition by the cobalamin transport protein haptocorrin. <i> Furger E, Frei DC, Schibli R, Fischer E, Prota AE. </i> J Biol Chem, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4KKJ"},{"db":"PDB","id":"4KKI"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-06T14:47:46.033Z"}},{"start":1,"end":23,"reference_id":"23846701","reference_source":"pmid","reference_html":"Structural basis for universal corrinoid recognition by the cobalamin transport protein haptocorrin. <i> Furger E, Frei DC, Schibli R, Fischer E, Prota AE. </i> J Biol Chem, 2013","date":"2022-10-06T14:46:40.677Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4KKJ"},{"db":"PDB","id":"4KKI"}],"region_id":"DP02797r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"506227","entry_name":"N-acetyl-D-glucosamine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"141013","entry_name":"cob(II)inamide"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17514","entry_name":"cyanide"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46807","entry_name":"diethylene glycol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17439","entry_name":"cyanocob(III)alamin"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"released":"2023_12","ncbi_taxon_id":9606,"disprot_id":"DP02797","date":"2020-04-17T22:55:15.736Z","organism":"Homo sapiens","regions_counter":3,"name":"Transcobalamin-1","dataset":[],"UniParc":"UPI0000136AE1","uniref100":"UniRef100_P20061","uniref90":"UniRef90_P20061","uniref50":"UniRef50_P20061","genes":[{"name":{"value":"TCN1"},"synonyms":[{"value":"TC1"}]}],"alphafold_very_low_content":0.07159353348729793,"disorder_content":0.08314087759815242,"disprot_consensus":{"full":[{"start":1,"end":23,"type":"D"},{"start":318,"end":330,"type":"D"}],"Structural state":[{"start":1,"end":23,"type":"D"},{"start":318,"end":330,"type":"D"}],"Disorder function":[{"start":318,"end":330,"type":"F"}]}},{"acc":"P23771","features":{"gene3D":[{"start":307,"end":370,"id":"G3DSA:3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A"},{"start":307,"end":370,"id":"G3DSA:3.30.50.10","name":"Erythroid Transcription Factor GATA-1, subunit A"}],"pfam":[{"id":"PF00320","name":"GATA zinc finger","start":263,"end":296},{"id":"PF00320","name":"GATA zinc finger","start":317,"end":349}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MEVTADQPRWVSHHHPAVLNGQHPDTHHPGLSHSYMDAAQYPLPEEVDVLFNIDGQGNHVPPYYGNSVRATVQRYPPTHHGSQVCRPPLLHGSLPWLDGGKALGSHHTASPWNLSPFSKTSIHHGSPGPLSVYPPASSSSLSGGHASPHLFTFPPTPPKDVSPDPSLSTPGSAGSARQDEKECLKYQVPLPDSMKLESSHSRGSMTALGGASSSTHHPITTYPPYVPEYSSGLFPPSSLLGGSPTGFGCKSRPKARSSTGRECVNCGATSTPLWRRDGTGHYLCNACGLYHKMNGQNRPLIKPKRRLSAARRAGTSCANCQTTTTTLWRRNANGDPVCNACGLYYKLHNINRPLTMKKEGIQTRNRKMSSKSKKCKKVHDSLEDFPKNSSFNPAALSRHMSSLSHISPFSHSSHMLTTPTPMHPPSSLSFGPHHPSSMVTAMG","length":443,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":314,"region_id":"DP02798r001","start":304,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The linker region in all three crystal structures shows a large flexibility as evident by high B-factors and a weak electron density.","type":"Results"}],"curator_id":"vnugnes","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"23142663","version":3,"reference_html":"DNA binding by GATA transcription factor suggests mechanisms of DNA looping and long-range gene regulation. <i> Chen Y, Bates DL, Dey R, Chen PH, Machado AC, Laird-Offringa IA, Rohs R, Chen L. </i> Cell Rep, 2012","date":"2022-06-16T21:00:20.746Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4HCA"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:55:38.613Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":314,"region_id":"DP02798r002","start":304,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The linker region in all three crystal structures shows a large flexibility as evident by high B-factors and a weak electron density.","type":"Results"}],"curator_id":"vnugnes","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"23142663","version":3,"reference_html":"DNA binding by GATA transcription factor suggests mechanisms of DNA looping and long-range gene regulation. <i> Chen Y, Bates DL, Dey R, Chen PH, Machado AC, Laird-Offringa IA, Rohs R, Chen L. </i> Cell Rep, 2012","date":"2022-06-16T20:59:53.687Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4HCA"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:55:40.378Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":314,"region_id":"DP02798r003","start":304,"term_id":"IDPO:0000033","unpublished":true,"statement":[{"text":"The linker region in all three crystal structures shows a large flexibility as evident by high B-factors and a weak electron density.","type":"Results"},{"text":"These structural analyses suggest that the linker region between the N-finger and the C-finger in GATA3 does not appear to have any conformational limitations. One of its functional roles appears to be providing a constraint on the spacing of the palindromic sites and the geometric distance between the DNA molecules bridged by GATA, while the flexibility of the linker region allows a wide variety of orientations of the bridged DNA molecules.","type":"Results"}],"curator_id":"vnugnes","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"23142663","version":4,"reference_html":"DNA binding by GATA transcription factor suggests mechanisms of DNA looping and long-range gene regulation. <i> Chen Y, Bates DL, Dey R, Chen PH, Machado AC, Laird-Offringa IA, Rohs R, Chen L. </i> Cell Rep, 2012","date":"2022-06-16T21:00:32.628Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4HCA"}],"term_name":"flexible linker","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Disorder function","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:55:41.754Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":314,"region_id":"DP02798r004","start":304,"term_id":"IDPO:0000033","unpublished":true,"statement":[{"text":"The linker region in all three crystal structures shows a large flexibility as evident by high B-factors and a weak electron density.","type":"Results"}],"curator_id":"vnugnes","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"23142663","version":4,"reference_html":"DNA binding by GATA transcription factor suggests mechanisms of DNA looping and long-range gene regulation. <i> Chen Y, Bates DL, Dey R, Chen PH, Machado AC, Laird-Offringa IA, Rohs R, Chen L. </i> Cell Rep, 2012","date":"2022-06-16T21:00:45.193Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4HCA"}],"term_name":"flexible linker","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Disorder function","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:55:43.511Z"}}],"released":"2022_06","ncbi_taxon_id":9606,"disprot_id":"DP02798","date":"2020-04-17T23:28:58.950Z","organism":"Homo sapiens","regions_counter":4,"name":"Trans-acting T-cell-specific transcription factor GATA-3","dataset":["Cancer-related proteins","Condensates-related proteins","NDDs-related proteins"],"UniParc":"UPI000004904B","uniref100":"UniRef100_P23771","uniref90":"UniRef90_P23772","uniref50":"UniRef50_P23772","genes":[{"name":{"value":"GATA3"}}],"alphafold_very_low_content":0.5282167042889391,"disorder_content":0.024830699774266364,"disprot_consensus":{"full":[{"start":304,"end":314,"type":"D"}],"Structural state":[{"start":304,"end":314,"type":"D"}],"Disorder function":[{"start":304,"end":314,"type":"F"}]}},{"acc":"P34257","features":{"gene3D":[{"start":60,"end":104,"id":"G3DSA:1.10.10.10","name":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"}],"pfam":[{"id":"PF11427","name":"Tc3 transposase","start":3,"end":52},{"id":"PF13358","name":"DDE superfamily endonuclease","start":140,"end":287},{"id":"PF21517","name":"Transposable element Tc3 transposase, HTH","start":64,"end":103}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"sequence":"MPRGSALSDTERAQLDVMKLLNVSLHEMSRKISRSRHCIREYLKDPVSYGTSKRAPRRKALSVRDERNVIRAASNSCKTARDIRNELQLSASKRTILNVIKRSGVIVRQKLRPAPLLSADHKLKRLEFAKNNMGTNWSKVVFSDEKKFNLDGPDGCRYYWRDLRKEPMVFSRRNFGGGTVMVWGAFTEKKKLEIQFVSSKMNSTDYQNVLELELSKYLRHYSRKDFRFQQDNATIHVSNSTRDYFKLKKINLLDWPARSPDLNPIENLWGILVRIVYAQNKTYPTVASLKQGILDAWKSIPDNQLKSLVRSMEDRLIEIIRTQGNPINY","length":329,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":135,"region_id":"DP02799r001","start":104,"term_id":"IDPO:0000002","statement":[{"text":"All DNA bases and amino acid residues 2–103 were defined in electron density, but electron density for amino acid residues 1 and 104–135, and the C-terminal His-tag is missing.","type":"Results"},{"text":"The structure reveals two helix–turn–helix (HTH) protein domains separated by a linker of 18 amino acids, binding to the 26mer duplex of DNA, as shown in Figure ​Figure2.2. All DNA bases and amino acid residues 2–103 were defined in electron density, but electron density for amino acid residues 1 and 104–135, and the C-terminal His-tag is missing. It is probable that the N-terminal methionine was removed from the protein, as shown for the earlier construct (17). The C-terminal residues are not visible in the electron density, probably due to the flexibility of these amino acids in the absence of the catalytic domain.","type":"Results"},{"text":"The limited resolution, the high B-factor of the data and the missing C-terminal amino acids result in a relatively high R-factor (23.3%) and free R-factor (27.3%).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15304566","version":2,"reference_html":"Structural analysis of the bipartite DNA-binding domain of Tc3 transposase bound to transposon DNA. <i> Watkins S, van Pouderoyen G, Sixma TK. </i> Nucleic Acids Res, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1U78"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":135,"region_id":"DP02799r002","start":104,"term_id":"IDPO:0000002","statement":[{"text":"All DNA bases and amino acid residues 2–103 were defined in electron density, but electron density for amino acid residues 1 and 104–135, and the C-terminal His-tag is missing.","type":"Results"},{"text":"The structure reveals two helix–turn–helix (HTH) protein domains separated by a linker of 18 amino acids, binding to the 26mer duplex of DNA, as shown in Figure ​Figure2.2. All DNA bases and amino acid residues 2–103 were defined in electron density, but electron density for amino acid residues 1 and 104–135, and the C-terminal His-tag is missing. It is probable that the N-terminal methionine was removed from the protein, as shown for the earlier construct (17). The C-terminal residues are not visible in the electron density, probably due to the flexibility of these amino acids in the absence of the catalytic domain.","type":"Results"},{"text":"The limited resolution, the high B-factor of the data and the missing C-terminal amino acids result in a relatively high R-factor (23.3%) and free R-factor (27.3%).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15304566","version":2,"reference_html":"Structural analysis of the bipartite DNA-binding domain of Tc3 transposase bound to transposon DNA. <i> Watkins S, van Pouderoyen G, Sixma TK. </i> Nucleic Acids Res, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1U78"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":6239,"disprot_id":"DP02799","date":"2020-04-20T09:42:37.732Z","organism":"Caenorhabditis elegans","regions_counter":2,"name":"Transposable element Tc3 transposase","dataset":[],"UniParc":"UPI0000136AB1","uniref100":"UniRef100_P34257","uniref90":"UniRef90_P34257","uniref50":"UniRef50_P34257","genes":[{"name":{"value":"tc3a"},"orfNames":[{"value":"B0303.5"}]}],"alphafold_very_low_content":0.0060790273556231,"disorder_content":0.0972644376899696,"disprot_consensus":{"full":[{"start":104,"end":135,"type":"D"}],"Structural state":[{"start":104,"end":135,"type":"D"}]}},{"acc":"P63028","features":{"gene3D":[{"start":1,"end":172,"id":"G3DSA:2.170.150.10","name":"Metal Binding Protein, Guanine Nucleotide Exchange Factor; Chain A"}],"pfam":[{"id":"PF00838","name":"Translationally controlled tumour protein","start":1,"end":168}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MIIYRDLISHDELFSDIYKIREIADGLCLEVEGKMVSRTEGAIDDSLIGGNASAEGPEGEGTESTVVTGVDIVMNHHLQETSFTKEAYKKYIKDYMKSLKGKLEEQKPERVKPFMTGAAEQIKHILANFNNYQFFIGENMNPDGMVALLDYREDGVTPFMIFFKDGLEMEKC","length":172,"regions":[{"region_id":"DP02800r001","ec_ontology":"ECO","end":66,"term_id":"IDPO:0000002","start":39,"version":2,"statement":[{"text":"Residues 1–38 and 68–170, and 1–41 and 67–170 were modeled for chains A and B, respectively; similar to other crystal structures of HRF (Vedadi et al., 2007, Susini et al., 2008, Dong et al., 2009, Eichhorn et al., 2013), the mobile loop region (residues Thr39-Val66) was disordered.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29216544","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5O9K"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Crystal structures of murine and human Histamine-Releasing Factor (HRF/TCTP) and a model for HRF dimerisation in mast cell activation. <i> Doré KA, Kashiwakura JI, McDonnell JM, Gould HJ, Kawakami T, Sutton BJ, Davies AM. </i> Mol Immunol, 2018","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02800r002","ec_ontology":"ECO","end":66,"term_id":"GO:0098772","start":39,"version":3,"statement":[{"text":"HRF crystal and solution structures have provided little insight into either the formation of disulphide-linked HRF dimers or the ability of HRF to activate mast cells.","type":"Abstract"},{"text":"The current model for the activity of HRF in mast cell activation involves cross-linking of FcεRI-bound IgE by dimeric HRF, mediated by interactions between HRF and the Fab regions of IgE","type":"Introduction"}],"term_name":"molecular function regulator","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"29216544","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5O9K"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"fquaglia","reference_html":"Crystal structures of murine and human Histamine-Releasing Factor (HRF/TCTP) and a model for HRF dimerisation in mast cell activation. <i> Doré KA, Kashiwakura JI, McDonnell JM, Gould HJ, Kawakami T, Sutton BJ, Davies AM. </i> Mol Immunol, 2018","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_12","ncbi_taxon_id":10090,"disprot_id":"DP02800","date":"2020-04-20T10:06:21.550Z","organism":"Mus musculus","regions_counter":2,"name":"Translationally-controlled tumor protein","dataset":[],"UniParc":"UPI00000233A4","uniref100":"UniRef100_P63028","uniref90":"UniRef90_P63028","uniref50":"UniRef50_P63028","genes":[{"name":{"value":"Tpt1"},"synonyms":[{"value":"Trt"}]}],"alphafold_very_low_content":0.029069767441860465,"disorder_content":0.16279069767441862,"disprot_consensus":{"full":[{"start":39,"end":66,"type":"D"}],"Structural state":[{"start":39,"end":66,"type":"D"}],"Molecular function":[{"start":39,"end":66,"type":"F"}]}},{"acc":"P05452","features":{"gene3D":[{"start":66,"end":202,"id":"G3DSA:3.10.100.10","name":"Mannose-Binding Protein A, subunit A"}],"pfam":[{"id":"PF00059","name":"Lectin C-type domain","start":88,"end":199}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MELWGAYLLLCLFSLLTQVTTEPPTQKPKKIVNAKKDVVNTKMFEELKSRLDTLAQEVALLKEQQALQTVCLKGTKVHMKCFLAFTQTKTFHEASEDCISRGGTLGTPQTGSENDALYEYLRQSVGNEAEIWLGLNDMAAEGTWVDMTGARIAYKNWETEITAQPDGGKTENCAVLSGAANGKWFDKRCRDQLPYICQFGIV","length":202,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":46,"region_id":"DP02801r001","start":22,"term_id":"IDPO:0000002","statement":[{"text":"The N‐terminal 25 residues can not be located in the electron density maps, indicating disorder in the N‐terminal part of TN.","type":"Results"},{"text":"The disordered segment at the N-terminal region of the protein correspond to residues 22-46, since region 1-21 is the signal peptide","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"9256258","version":2,"reference_html":"Crystal structure of tetranectin, a trimeric plasminogen-binding protein with an alpha-helical coiled coil. <i> Nielsen BB, Kastrup JS, Rasmussen H, Holtet TL, Graversen JH, Graversen JH, Etzerodt M, Thøgersen HC, Larsen IK. </i> FEBS Lett, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1HTN"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02801r002","ec_ontology":"ECO","end":49,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"The close structural resemblance of TN to the neck and CRD part of the MBPs, where carbohydrate‐binding is conferred to the CRD, whereas other additional domains provide the diversity of functions of these proteins, indicate that the kringle 4‐binding site resides within residues 1–49 of the TN sequence. This is supported by the observation that only the full‐length protein and not the isolated CRD binds to immobilized kringle 4 (Holtet, T.L., unpublished). ","type":"Results"},{"text":"However, the observations that TN binds to the kringle 4 domain of plasminogen [1, 10], interacts in a calcium‐dependent manner with sulfated polysaccharides [11] and fibrin [12], binds to immobilized fucoidan (Graversen, J.H., unpublished), as well as the presence of two characteristic calcium sites in the TN structure, suggest that one function of the protein is to target plasminogen to specific carbohydrate ligands on cell surfaces, in the extracellular matrix or to fibrin.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P00747","partner_end":null}],"term_name":"protein binding","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"9256258","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1HTN"}],"term_namespace":"Molecular function","ec_id":"ECO:0006218","curator_id":"fquaglia","reference_html":"Crystal structure of tetranectin, a trimeric plasminogen-binding protein with an alpha-helical coiled coil. <i> Nielsen BB, Kastrup JS, Rasmussen H, Holtet TL, Graversen JH, Graversen JH, Etzerodt M, Thøgersen HC, Larsen IK. </i> FEBS Lett, 1997","curator_orcid":"0000-0002-0341-4888","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Biological process","ec_ontology":"ECO","end":49,"region_id":"DP02801r003","start":1,"term_id":"GO:0051179","statement":[{"text":"The close structural resemblance of TN to the neck and CRD part of the MBPs, where carbohydrate‐binding is conferred to the CRD, whereas other additional domains provide the diversity of functions of these proteins, indicate that the kringle 4‐binding site resides within residues 1–49 of the TN sequence. This is supported by the observation that only the full‐length protein and not the isolated CRD binds to immobilized kringle 4 (Holtet, T.L., unpublished). ","type":"Results"},{"text":"However, the observations that TN binds to the kringle 4 domain of plasminogen [1, 10], interacts in a calcium‐dependent manner with sulfated polysaccharides [11] and fibrin [12], binds to immobilized fucoidan (Graversen, J.H., unpublished), as well as the presence of two characteristic calcium sites in the TN structure, suggest that one function of the protein is to target plasminogen to specific carbohydrate ligands on cell surfaces, in the extracellular matrix or to fibrin.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"9256258","version":3,"reference_html":"Crystal structure of tetranectin, a trimeric plasminogen-binding protein with an alpha-helical coiled coil. <i> Nielsen BB, Kastrup JS, Rasmussen H, Holtet TL, Graversen JH, Graversen JH, Etzerodt M, Thøgersen HC, Larsen IK. </i> FEBS Lett, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","cross_refs":[{"db":"PDB","id":"1HTN"}],"term_name":"localization","curator_orcid":"0000-0002-0341-4888","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02801","date":"2020-04-20T10:28:00.100Z","organism":"Homo sapiens","regions_counter":3,"name":"Tetranectin","dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000174155","uniref100":"UniRef100_P05452","uniref90":"UniRef90_P05452","uniref50":"UniRef50_P05452","genes":[{"name":{"value":"CLEC3B"},"synonyms":[{"value":"TNA"}]}],"alphafold_very_low_content":0.12871287128712872,"disorder_content":0.12376237623762376,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"F"},{"start":22,"end":46,"type":"D"},{"start":47,"end":49,"type":"F"}],"Structural state":[{"start":22,"end":46,"type":"D"}],"Molecular function":[{"start":1,"end":49,"type":"F"}],"Biological process":[{"start":1,"end":49,"type":"F"}]}},{"acc":"Q921Z5","features":{"gene3D":[{"start":13,"end":198,"id":"G3DSA:1.20.1440.160","name":"G3DSA:1.20.1440.160"}],"pfam":[{"id":"PF05527","name":"Tumor necrosis factor alpha-induced protein 8-like","start":16,"end":196}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MLSEAEEPREVATDVFNSKNLAVQAQKKILGKMVSKSIATTLIDDTSSEVLDELYRVTKEYTQNKKEAERVIKNLIKTVIKLAVLHRNNQFNQDELALMEKFKKKVHQLAMTVVSFHQVEYTFDRNVLSRLLNECRELLHEIIQRHLTAKSHGRVNNVFDHFSDCDFLAALYNPFGKFKPHLQKLCDGINKMLDEENI","length":198,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":12,"region_id":"DP02802r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"Except for 12 flexible N-terminal residues (Met1-Ala12), all other amino acids are defined in the electron density map.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28740220","version":2,"reference_html":"The Tnfaip8-PE complex is a novel upstream effector in the anti-autophagic action of insulin. <i> Kim JS, Park J, Kim MS, Ha JY, Jang YW, Shin DH, Son JH. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5JXD"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":12,"region_id":"DP02802r002","start":1,"term_id":"GO:0036094","statement":[{"text":"Our structural analysis suggests that the flexibility of the N-terminal domain together with the described positively charged surface (Fig. 4) may be important for the biological functions of mTnfaip8 and hTIPE3 probably assisting in the uptake and release of phosphoglycerides.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"protein mass spectrometry evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"28740220","version":3,"reference_html":"The Tnfaip8-PE complex is a novel upstream effector in the anti-autophagic action of insulin. <i> Kim JS, Park J, Kim MS, Ha JY, Jang YW, Shin DH, Son JH. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007184","cross_refs":[{"db":"PDB","id":"5JXD"}],"term_name":"small molecule binding","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":12,"region_id":"DP02802r003","start":1,"term_id":"GO:0140313","statement":[{"text":"Our structural analysis suggests that the flexibility of the N-terminal domain together with the described positively charged surface (Fig. 4) may be important for the biological functions of mTnfaip8 and hTIPE3 probably assisting in the uptake and release of phosphoglycerides.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"protein mass spectrometry evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"28740220","version":3,"reference_html":"The Tnfaip8-PE complex is a novel upstream effector in the anti-autophagic action of insulin. <i> Kim JS, Park J, Kim MS, Ha JY, Jang YW, Shin DH, Son JH. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007184","cross_refs":[{"db":"PDB","id":"5JXD"}],"term_name":"molecular sequestering activity","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":10090,"disprot_id":"DP02802","date":"2020-04-20T10:58:22.473Z","organism":"Mus musculus","regions_counter":3,"name":"Tumor necrosis factor alpha-induced protein 8","dataset":[],"UniParc":"UPI00000289AE","uniref100":"UniRef100_Q921Z5","uniref90":"UniRef90_Q921Z5","uniref50":"UniRef50_Q8WVP5","genes":[{"name":{"value":"Tnfaip8"}}],"alphafold_very_low_content":0.015151515151515152,"disorder_content":0.06060606060606061,"disprot_consensus":{"full":[{"start":1,"end":12,"type":"D"}],"Structural state":[{"start":1,"end":12,"type":"D"}],"Molecular function":[{"start":1,"end":12,"type":"F"}]}},{"acc":"Q96Q11","features":{"gene3D":[{"start":28,"end":179,"id":"G3DSA:3.30.460.10","name":"Beta Polymerase, domain 2"}],"pfam":[{"id":"PF01743","name":"Poly A polymerase head domain","start":59,"end":182},{"id":"PF12627","name":"Probable RNA and SrmB- binding site of polymerase A","start":216,"end":266}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MLRCLYHWHRPVLNRRWSRLCLPKQYLFTMKLQSPEFQSLFTEGLKSLTELFVKENHELRIAGGAVRDLLNGVKPQDIDFATTATPTQMKEMFQSAGIRMINNRGEKHGTITARLHEENFEITTLRIDVTTDGRHAEVEFTTDWQKDAERRDLTINSMFLGFDGTLFDYFNGYEDLKNKKVRFVGHAKQRIQEDYLRILRYFRFYGRIVDKPGDHDPETLEAIAENAKGLAGISGERIWVELKKILVGNHVNHLIHLIYDLDVAPYIGLPANASLEEFDKVSKNVDGFSPKPVTLLASLFKVQDDVTKLDLRLKIAKEEKNLGLFIVKNRKDLIKATDSSDPLKPYQDFIIDSREPDATTRVCELLKYQGEHCLLKEMQQWSIPPFPVSGHDIRKVGISSGKEIGALLQQLREQWKKSGYQMEKDELLSYIKKT","length":434,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":139,"region_id":"DP02803r001","start":128,"term_id":"IDPO:0000002","statement":[{"text":"The tail domain of hmtCCase (residues 355–405) as well as a stretch of 11 amino acid residues (99–110) within the head domain are completely disordered in the structure.","type":"Results"},{"text":"This IDR corresponds to the stretch of 11 amino acid residues, whose numbering in the publication is referred to the multiple sequence alignment of Figure 1.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12729736","version":2,"reference_html":"Crystal structure of the human CCA-adding enzyme: insights into template-independent polymerization. <i> Augustin MA, Reichert AS, Betat H, Huber R, Mörl M, Steegborn C. </i> J Mol Biol, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1OU5"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-03T21:03:02.207Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":434,"region_id":"DP02803r002","start":384,"term_id":"IDPO:0000002","statement":[{"text":"The tail domain of hmtCCase (residues 355–405) as well as a stretch of 11 amino acid residues (99–110) within the head domain are completely disordered in the structure.","type":"Results"},{"text":"This IDR corresponds to the tail domain of hmtCCase, whose numbering in the publication is referred to the multiple sequence alignment of Figure 1.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12729736","version":2,"reference_html":"Crystal structure of the human CCA-adding enzyme: insights into template-independent polymerization. <i> Augustin MA, Reichert AS, Betat H, Huber R, Mörl M, Steegborn C. </i> J Mol Biol, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1OU5"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-03T21:03:02.477Z"}}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02803","date":"2020-04-20T11:35:18.857Z","organism":"Homo sapiens","regions_counter":3,"name":"CCA tRNA nucleotidyltransferase 1, mitochondrial","dataset":["NDDs-related proteins"],"UniParc":"UPI000013CD08","uniref100":"UniRef100_Q96Q11","uniref90":"UniRef90_Q96Q11","uniref50":"UniRef50_Q96Q11","genes":[{"name":{"value":"TRNT1"},"orfNames":[{"value":"CGI-47"}]}],"alphafold_very_low_content":0.06221198156682028,"disorder_content":0.14516129032258066,"disprot_consensus":{"full":[{"start":128,"end":139,"type":"D"},{"start":384,"end":434,"type":"D"}],"Structural state":[{"start":128,"end":139,"type":"D"},{"start":384,"end":434,"type":"D"}]}},{"acc":"P61587","features":{"gene3D":[],"pfam":[{"id":"PF00071","name":"Ras family","start":25,"end":193}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MKERRASQKLSSKSIMDPNQNVKCKIVVVGDSQCGKTALLHVFAKDCFPENYVPTVFENYTASFEIDTQRIELSLWDTSGSPYYDNVRPLSYPDSDAVLICFDISRPETLDSVLKKWKGEIQEFCPNTKMLLVGCKSDLRTDVSTLVELSNHRQTPVSYDQGANMAKQIGAATYIECSALQSENSVRDIFHVATLACVNKTNKNVKRNKSQRATKRISHMPSRPELSAVATDLRKDKAKSCTVM","length":244,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":19,"region_id":"DP02804r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"In RhoE, electron density is well defined for residues Gln20 to Lys200, whereas in ROCK-I residues 6–404 are similarly well resolved.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18946488","version":2,"reference_html":"Mechanism of multi-site phosphorylation from a ROCK-I:RhoE complex structure. <i> Komander D, Garg R, Wan PT, Ridley AJ, Barford D. </i> EMBO J, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2V55"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":19,"region_id":"DP02804r002","start":1,"term_id":"IDPO:0000045","statement":[{"text":"ROCK-I phosphorylates the unconventional G-protein RhoE on multiple N- and C-terminal sites. These phosphorylation events stabilise RhoE, which functions to antagonise RhoA-induced stress fibre assembly.","type":"Abstract"},{"text":"Importantly, Ser7 and Ser11 of RhoE are sites of ROCK-I phosphorylation (Riento et al, 2005a).","type":"Results"},{"text":"Within the context of the crystal structure, the two ROCK-I phosphorylation sites present in RhoE (Ser7 and Ser11) are likely interchanging at the catalytic (primary binding) site, with resultant low substrate occupancy and consequently disordered and poorly resolved electron density.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18946488","version":2,"reference_html":"Mechanism of multi-site phosphorylation from a ROCK-I:RhoE complex structure. <i> Komander D, Garg R, Wan PT, Ridley AJ, Barford D. </i> EMBO J, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2V55"}],"term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"region_id":"DP02804r003","ec_ontology":"ECO","end":19,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"The interaction of RhoE with ROCK-I positions RhoE to present both its N and C termini in close proximity to the kinase catalytic site cleft (Figure 5A). The visible N and C termini of RhoE (residues 20 and 200, respectively) are located some 20 Å from the kinase phosphoacceptor-binding site.","type":"Results"},{"text":"Model building studies, extending the polypeptide chain N-terminal from Gln20, and with reference to the position of the GSK3β peptide bound to PKBβ (Yang et al, 2002), indicate that both N-terminal phosphorylation sites, Ser7 and Ser11, are within reach of the catalytic site (Figure 5A).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q13464","partner_end":null}],"term_name":"protein binding","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"18946488","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2V55"}],"term_namespace":"Molecular function","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Mechanism of multi-site phosphorylation from a ROCK-I:RhoE complex structure. <i> Komander D, Garg R, Wan PT, Ridley AJ, Barford D. </i> EMBO J, 2008","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02804","date":"2020-04-20T22:14:46.016Z","organism":"Homo sapiens","regions_counter":3,"name":"Rho-related GTP-binding protein RhoE","dataset":[],"UniParc":"UPI0000003FE9","uniref100":"UniRef100_P61587","uniref90":"UniRef90_P61587","uniref50":"UniRef50_P61587","genes":[{"name":{"value":"RND3"},"synonyms":[{"value":"ARHE"},{"value":"RHO8"},{"value":"RHOE"}]}],"alphafold_very_low_content":0.2336065573770492,"disorder_content":0.0778688524590164,"disprot_consensus":{"full":[{"start":1,"end":19,"type":"D"}],"Structural state":[{"start":1,"end":19,"type":"D"}],"Disorder function":[{"start":1,"end":19,"type":"F"}],"Molecular function":[{"start":1,"end":19,"type":"F"}]}},{"acc":"Q91WA6","features":{"gene3D":[{"start":1,"end":126,"id":"G3DSA:2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"}],"pfam":[{"id":"PF16764","name":"Sharpin PH domain","start":14,"end":126},{"id":"PF25393","name":"LUBAC thetering domain","start":171,"end":212}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MSPPAGGAAVAADPASPVVLLAVHAAVRPLGAGQDAEAQPRKLQLIADPERPGRFRLGLLGTEPGAVSLEWPLEAICYTVRGPNQHELQPPPGGPGTFSVHFLDPEEAQQWAALVRDATAEGQNGSGSPAPAPAPAMCPISPPCSSMAQIPKATQPEVDLPQSSGNFKKEELATRLSQAIAGGDEKAAAQVAAVLAQHHVALNVQLMEAWFPPGPIRLQVTVEDATSVLSSSSSAHVSLKIHPHCSIAALQDQVFSEFGFPPAVQRWVIGRCLCMPERSLASYGVSQDGDPAFLYLLSAPREVSGQSLQNSKMDRKLGLFPQSLGLPHDLQPSSSSLPSPSQPGWSCPSCTFINASNRPGCEMCSTQRPCAWDPLAAAST","length":380,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":341,"region_id":"DP02805r001","start":301,"term_id":"IDPO:0000002","statement":[{"text":"Flexible linker connecting the UBL and NZF domains, as shown in Figure 3A","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29694895","version":2,"reference_html":"Cooperative Domain Formation by Homologous Motifs in HOIL-1L and SHARPIN Plays A Crucial Role in LUBAC Stabilization. <i> Fujita H, Tokunaga A, Shimizu S, Whiting AL, Aguilar-Alonso F, Takagi K, Walinda E, Sasaki Y, Shimokawa T, Mizushima T, Ohki I, Ariyoshi M, Tochio H, Bernal F, Shirakawa M, Iwai K. </i> Cell Rep, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5Y3T"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":341,"region_id":"DP02805r002","start":301,"term_id":"IDPO:0000033","statement":[{"text":"Flexible linker connecting the UBL and NZF domains, as shown in Figure 3A","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29694895","version":3,"reference_html":"Cooperative Domain Formation by Homologous Motifs in HOIL-1L and SHARPIN Plays A Crucial Role in LUBAC Stabilization. <i> Fujita H, Tokunaga A, Shimizu S, Whiting AL, Aguilar-Alonso F, Takagi K, Walinda E, Sasaki Y, Shimokawa T, Mizushima T, Ohki I, Ariyoshi M, Tochio H, Bernal F, Shirakawa M, Iwai K. </i> Cell Rep, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5Y3T"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":10090,"disprot_id":"DP02805","date":"2020-04-20T22:46:24.033Z","organism":"Mus musculus","regions_counter":2,"name":"Sharpin","dataset":[],"UniParc":"UPI000002935E","uniref100":"UniRef100_Q91WA6","uniref90":"UniRef90_Q91WA6","uniref50":"UniRef50_Q9H0F6","genes":[{"name":{"value":"Sharpin"},"synonyms":[{"value":"Cpdm"},{"value":"Sipl1"}]}],"alphafold_very_low_content":0.25263157894736843,"disorder_content":0.10789473684210527,"disprot_consensus":{"full":[{"start":301,"end":341,"type":"D"}],"Structural state":[{"start":301,"end":341,"type":"D"}],"Disorder function":[{"start":301,"end":341,"type":"F"}]}},{"acc":"P0CY08","features":{"gene3D":[],"pfam":[{"id":"PF00046","name":"Homeodomain","start":134,"end":188}]},"creator":"lchemes","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"sequence":"MNKIPIKDLLNPQITDEFKSSILDINKKLFSICCNLPKLPESVTTEEEVELRDILGFLSRANKNRKISDEEKKLLQTTSQLTTTITVLLKEMRSIENDRSNYQLTQKNKSADGLVFNVVTQDMINKSTKPYRGHRFTKENVRILESWFAKNIENPYLDTKGLENLMKNTSLSRIQIKNWVSNRRRKEKTITIAPELADLLSGEPLAKKKE","length":210,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":132,"region_id":"DP02806r001","start":103,"term_id":"IDPO:0000002","statement":[{"text":"Cleavage of the purified al protein with chymotrypsin generates two major fragments...This analysis showed that the larger fragment consists of amino acids 1-102 and the smaller fragment consists of amino acids 132-210 of al (210 residues total).","type":"Results"},{"text":"The limited proteolysis experiments identify residues 103-131 as the flexible linker","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"3061876","version":2,"reference_html":"Flexibility of the yeast alpha 2 repressor enables it to occupy the ends of its operator, leaving the center free. <i> Sauer RT, Smith DL, Johnson AD. </i> Genes Dev, 1988","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":132,"region_id":"DP02806r002","start":113,"term_id":"IDPO:0000011","statement":[{"text":"The otherwise flexible amino-terminal extension of the MATalpha2 homeodomain forms a beta-hairpin that grips the MCM1 surface through parallel beta-strand hydrogen bonds and close-packed, predominantly hydrophobic, side chains.....An unusual feature of the complex is that an eight-amino-acid sequence adopts an alpha-helical conformation in one of two copies of the MATalpha2 monomer and a beta-strand conformation in the other. This 'chameleon' sequence of MATalpha2 may be important for recognizing natural operator sites.","type":"Abstract"},{"text":"The structure shows that α2 uses a short eight-amino-acid module in the linker region to bind MCM1 via parallel β-strands. This recognition strand is tethered to the α2 homeodomain by a segment of unusual conformational flexibility. ","type":"Introduction"},{"text":"The cis copy of the α2 flexible linker implicated in the interaction with MCM1 (refs 23,26) forms a β-hairpin with a type-I turn.","type":"Results"},{"text":"The results compared to the flexible region identified by proteolysis, indicate that residues 113-132 become ordered upon binding MCM1 and DNA. This structure consists of a beta strand (113-120) involved in MCM1 binding, plus a \"chameleon\" region (121-128) that can be either a beta strand or a helix","type":"Curator statement"},{"text":"The α2 residues 121–128, QDMINKST, have the unusual property of forming either an α-helix or a β-strand. ","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"9490409","version":2,"reference_html":"Crystal structure of the yeast MATalpha2/MCM1/DNA ternary complex. <i> Tan S, Richmond TJ. </i> Nature, 1998","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"1MNM"}],"term_name":"disorder to order","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":132,"region_id":"DP02806r003","start":103,"term_id":"IDPO:0000033","statement":[{"text":"The α2 residues 121–128, QDMINKST, have the unusual property of forming either an α-helix or a β-strand. ","type":"Results"},{"text":"This paper demonstrates the two domains are joined by a flexible linker","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"3061876","version":3,"reference_html":"Flexibility of the yeast alpha 2 repressor enables it to occupy the ends of its operator, leaving the center free. <i> Sauer RT, Smith DL, Johnson AD. </i> Genes Dev, 1988","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","term_name":"flexible linker","curator_orcid":"0000-0003-0192-9906","ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":128,"region_id":"DP02806r004","start":110,"term_id":"GO:0005515","statement":[{"text":"An a2 fragment beginning with residue 120 retains partial cooperative binding with MCMl , and a fragment that starts with residue 128 fails to show strong cooperative binding with MCMl. These results suggest that approximately 20 residues (110-l 28) adjacent to the homeodomain are required for cooperative binding with MCMl. ","type":"Results"},{"text":"This paper demonstrates the linker region is required for cooperative MCM1 binding","type":"Curator statement"}],"curator_id":"esalladini","released":"2022_03","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"8422672","version":4,"reference_html":"A short, disordered protein region mediates interactions between the homeodomain of the yeast alpha 2 protein and the MCM1 protein. <i> Vershon AK, Johnson AD. </i> Cell, 1993","date":"2022-03-08T14:17:51.614Z","reference_source":"pmid","ec_id":"ECO:0001807","term_name":"protein binding","curator_orcid":"0000-0002-5152-5953","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P11746","operator":"and","partner_start":null,"partner_end":null}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":128,"region_id":"DP02806r005","start":110,"term_id":"GO:0098772","statement":[{"text":"An a2 fragment beginning with residue 120 retains partial cooperative binding with MCMl , and a fragment that starts with residue 128 fails to show strong cooperative binding with MCMl. These results suggest that approximately 20 residues (110-l 28) adjacent to the homeodomain are required for cooperative binding with MCMl. ","type":"Results"},{"text":"This paper demonstrates the linker region is required for cooperative MCM1 binding, it is a protein protein interaction that regulates DNA operator recognition","type":"Curator statement"}],"curator_id":"esalladini","released":"2022_03","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"8422672","version":4,"reference_html":"A short, disordered protein region mediates interactions between the homeodomain of the yeast alpha 2 protein and the MCM1 protein. <i> Vershon AK, Johnson AD. </i> Cell, 1993","date":"2022-03-08T14:17:43.489Z","reference_source":"pmid","ec_id":"ECO:0001807","term_name":"molecular function regulator","curator_orcid":"0000-0002-5152-5953","ec_go":"IPI","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P11746","operator":"and","partner_start":null,"partner_end":null}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":121,"region_id":"DP02806r006","start":114,"term_id":"GO:0098772","statement":[{"text":"The structure shows that α2 uses a short eight-amino-acid module in the linker region to bind MCM1 via parallel β-strands. ","type":"Introduction"},{"text":"The otherwise flexible amino-terminal extension of the MATalpha2 homeodomain forms a beta-hairpin that grips the MCM1 surface through parallel beta-strand hydrogen bonds and close-packed, predominantly hydrophobic, side chains","type":"Results"},{"text":"With the exception of Val 119, each of the α2 residues between Leu 114 and Gln 121 (LVFNVVTQ) makes van der Waals contacts with MCM1 residues. ","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"9490409","version":3,"reference_html":"Crystal structure of the yeast MATalpha2/MCM1/DNA ternary complex. <i> Tan S, Richmond TJ. </i> Nature, 1998","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","term_name":"molecular function regulator","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":210,"region_id":"DP02806r007","start":190,"term_id":"IDPO:0000002","statement":[{"text":"The a2 fragment used in our crystallographic study extends to the C-terminal end of a2 and therefore contains an additional 22 residues following the C-terminus of the homeodomain. This C-terminal tail may mediate the interaction between a2 and al (A. Mak and A. D. J., unpublished data; see also Strathern et al., 1988). We do not see clear electron density for this region and presume that it is disordered in the crystal. ","type":"Results"},{"text":"The region actually corresponds to 21 residues 190-210 as shown by the crystal structure","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"1682054","version":2,"reference_html":"Crystal structure of a MAT alpha 2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions. <i> Wolberger C, Vershon AK, Liu B, Johnson AD, Pabo CO. </i> Cell, 1991","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1APL"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":203,"region_id":"DP02806r008","start":193,"term_id":"GO:0098772","statement":[{"text":"We found that the a1 homeodomain perturbs the resonances of only the C-terminal tail of a2; moreover, contact with a1 converts a portion of this tail (residues 193-203) from its unstructured state to an a-helix, as determined by J coupling and NOE measurements","type":"Abstract"},{"text":"These NOE cross peak volume data suggest that residues 194-200 are helical. ","type":"Results"},{"text":"Binding to MAT alpha 1 structures the C terminal tail into a helix as shown by NMR","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"8049230","version":3,"reference_html":"Heterodimerization of the yeast homeodomain transcriptional regulators alpha 2 and a1 induces an interfacial helix in alpha 2. <i> Phillips CL, Stark MR, Johnson AD, Dahlquist FW. </i> Biochemistry, 1994","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"molecular function regulator","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":203,"region_id":"DP02806r009","start":193,"term_id":"IDPO:0000011","statement":[{"text":"We found that the a1 homeodomain perturbs the resonances of only the C-terminal tail of a2; moreover, contact with a1 converts a portion of this tail (residues 193-203) from its unstructured state to an a-helix, as determined by J coupling and NOE measurements","type":"Abstract"},{"text":"These NOE cross peak volume data suggest that residues 194-200 are helical. ","type":"Results"},{"text":"Binding to MAT alpha 1 structures the C terminal tail into a helix as shown by NMR","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"8049230","version":2,"reference_html":"Heterodimerization of the yeast homeodomain transcriptional regulators alpha 2 and a1 induces an interfacial helix in alpha 2. <i> Phillips CL, Stark MR, Johnson AD, Dahlquist FW. </i> Biochemistry, 1994","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder to order","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":205,"region_id":"DP02806r010","start":190,"term_id":"IDPO:0000011","statement":[{"text":"The a1 and a2 homeodomains bind in a head-to-tail orientation, with heterodimer contacts mediated by a 16-residue tail located carboxyl-terminal to the a2 homeodomain. This tail becomes ordered in the presence of al, part of it forming a short amphipathic helix that packs against the a1 horneodomain between helices 1 and 2","type":"Abstract"},{"text":"The a2 protein contacts the a1 homeodomain with a peptide tail located COOHterminal to the a2 homeodomain. As compared with the structure of a2 alone bound to DNA, an additional 16 residues are ordered in the ternary complex. This COOHterminal tail, consisting of residues 59 to 74","type":"Results"},{"text":"Numbering is shifted by 131 residues according to UNIPROT accession, and the region corresponds to residues 190-205 of the UNIPROT sequence","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"7569974","version":2,"reference_html":"Crystal structure of the MATa1/MAT alpha 2 homeodomain heterodimer bound to DNA. <i> Li T, Stark MR, Johnson AD, Wolberger C. </i> Science, 1995","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"1YRN"}],"term_name":"disorder to order","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":205,"region_id":"DP02806r011","start":190,"term_id":"GO:0098772","statement":[{"text":"The a1 and a2 homeodomains bind in a head-to-tail orientation, with heterodimer contacts mediated by a 16-residue tail located carboxyl-terminal to the a2 homeodomain. This tail becomes ordered in the presence of al, part of it forming a short amphipathic helix that packs against the a1 horneodomain between helices 1 and 2","type":"Abstract"},{"text":"The a2 protein contacts the a1 homeodomain with a peptide tail located COOHterminal to the a2 homeodomain. As compared with the structure of a2 alone bound to DNA, an additional 16 residues are ordered in the ternary complex. This COOHterminal tail, consisting of residues 59 to 74","type":"Results"},{"text":"Numbering is shifted by 131 residues according to UNIPROT accession, and the region corresponds to residues 190-205 of the UNIPROT sequence. Function of this region is binding to MAT 1 alpha","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"7569974","version":3,"reference_html":"Crystal structure of the MATa1/MAT alpha 2 homeodomain heterodimer bound to DNA. <i> Li T, Stark MR, Johnson AD, Wolberger C. </i> Science, 1995","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"1YRN"}],"term_name":"molecular function regulator","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":559292,"disprot_id":"DP02806","date":"2020-04-21T20:04:48.848Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":11,"name":"Mating-type protein ALPHA2","dataset":[],"UniParc":"UPI000012EBF8","uniref100":"UniRef100_P0CY09","uniref90":"UniRef90_P0CY09","uniref50":"UniRef50_P0CY09","genes":[{"name":{"value":"MATALPHA2"},"synonyms":[{"value":"ALPHA-2"},{"value":"MAT2A"},{"value":"MATAL2"}],"orfNames":[{"value":"YCR39C"}],"olnNames":[{"value":"YCR039C"}]}],"alphafold_very_low_content":0.0380952380952381,"disorder_content":0.24285714285714285,"disprot_consensus":{"full":[{"start":103,"end":112,"type":"D"},{"start":113,"end":132,"type":"T"},{"start":190,"end":205,"type":"T"},{"start":206,"end":210,"type":"D"}],"Structural state":[{"start":103,"end":132,"type":"D"},{"start":190,"end":210,"type":"D"}],"Structural transition":[{"start":113,"end":132,"type":"T"},{"start":190,"end":205,"type":"T"}],"Disorder function":[{"start":103,"end":132,"type":"F"}],"Molecular function":[{"start":110,"end":128,"type":"F"},{"start":190,"end":205,"type":"F"}]}},{"acc":"P53927","features":{"gene3D":[{"start":3,"end":175,"id":"G3DSA:3.30.70.330","name":"G3DSA:3.30.70.330"}],"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":93,"end":162}]},"creator":"lchemes","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"sequence":"MVKSTSKTSTKETVTKQPTEEKPIQEKEELALETSSSSSDEEDEKDEDEIEGLAASDDEQSGTHKIKRLNPKKQANEKKSKDKKTLEEYSGIIYVSRLPHGFHEKELSKYFAQFGDLKEVRLARNKKTGNSRHYGFLEFVNKEDAMIAQESMNNYLLMGHLLQVRVLPKGAKIEKLYKYKKRVLVEKGITKPVKQLKDNMKQKHEERIKKLAKSGIEFKW","length":220,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":191,"region_id":"DP02808r001","start":179,"term_id":"IDPO:0000002","statement":[{"text":"Figure 1. Helices α4 and αC are not visible in the Nop15 crystal structure (chain A) and are drawn with dotted lines","type":"Results"},{"text":"The missing residues in the crystal structure correspond to residues 179-191","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"27789691","version":2,"reference_html":"Structural analysis reveals the flexible C-terminus of Nop15 undergoes rearrangement to recognize a pre-ribosomal RNA folding intermediate. <i> Zhang J, Gonzalez LE, Hall TMT. </i> Nucleic Acids Res, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5T9P"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":220,"region_id":"DP02808r002","start":181,"term_id":"IDPO:0000002","statement":[{"text":"NMR: The average intensity of the C-terminal resonances was 4 times higher than those of the central RRM domain (P < 0.0001). Therefore, our NMR results indicate that the C-terminal region tumbles as a flexible moiety at a rate faster than the core RRM domain (Figure (Figure4D4D).","type":"Results"},{"text":"The flexible residues from NMR analysis correspond to residues 181-220","type":"Curator statement"},{"text":"Small-angle X-ray scattering, NMR and RNA-binding analyses further reveal that the C-terminal residues of Nop15 are highly flexible","type":"Abstract"}],"curator_id":"lchemes","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"27789691","version":2,"reference_html":"Structural analysis reveals the flexible C-terminus of Nop15 undergoes rearrangement to recognize a pre-ribosomal RNA folding intermediate. <i> Zhang J, Gonzalez LE, Hall TMT. </i> Nucleic Acids Res, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":220,"region_id":"DP02808r003","start":181,"term_id":"IDPO:0000002","statement":[{"text":"SAXS: we used SAXS to study Nop1581–220 (Figure (Figure4A,4A, Supplementary Table S3). We evaluated the SAXS data using the EOM, which allows fitting of an ensemble of structures for flexible protein regions. The selected set of three conformers that optimally fit the SAXS data indicated that the C-terminal residues (181–220) are highly flexible, widely sampling around the core RRM domain (Figure (Figure4A4A and B).","type":"Results"},{"text":"The flexible residues from SAXS analysis correspond to residues 181-220","type":"Curator statement"},{"text":"Small-angle X-ray scattering, NMR and RNA-binding analyses further reveal that the C-terminal residues of Nop15 are highly flexible","type":"Abstract"}],"curator_id":"lchemes","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"27789691","version":2,"reference_html":"Structural analysis reveals the flexible C-terminus of Nop15 undergoes rearrangement to recognize a pre-ribosomal RNA folding intermediate. <i> Zhang J, Gonzalez LE, Hall TMT. </i> Nucleic Acids Res, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":220,"region_id":"DP02808r004","start":181,"term_id":"IDPO:0000011","statement":[{"text":"Small-angle X-ray scattering, NMR and RNA-binding analyses further reveal that the C-terminal residues of Nop15 are highly flexible, but essential for tight RNA binding. Moreover, comparison with a recently reported cryo-electron microscopy structure indicates that dramatic rearrangement of the C-terminal region of Nop15 in the pre-ribosome exposes the RNA-binding surface to recognize the base of its stem-loop target RNA","type":"Abstract"},{"text":"Comparing our crystal structure with Nop15 in a cryo-EM model of the pre-60S ribosome (17) indicates that the α-helical region is dramatically refolded, which releases the classical RNA-binding residues for interaction at the base of an ITS2 stem-loop and allows interaction of the C-terminal residues near the distal loop of the stem-loop.","type":"Introduction"},{"text":"The disorder to order transition is deduced from the comparison of the results of this paper with those of CryoEM structures where the same region is folded","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"27789691","version":2,"reference_html":"Structural analysis reveals the flexible C-terminus of Nop15 undergoes rearrangement to recognize a pre-ribosomal RNA folding intermediate. <i> Zhang J, Gonzalez LE, Hall TMT. </i> Nucleic Acids Res, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","term_name":"disorder to order","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":220,"region_id":"DP02808r005","start":181,"term_id":"IDPO:0000011","statement":[{"text":"The disorder to order transition is deduced from the comparison of the results of this paper (region folded) with those of Crystal structures where the same region is unfolded or flexible","type":"Curator statement"},{"text":"\nHowever, states A–C already contain a hallmark structure typically seen on Arx1 or Nog2 particles, termed the “foot,” which is formed by ITS2 rRNA and its associated “A3” cluster factors Cic1/Nsa3, Nop7, Nop15, and Rlp7\n","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"cryogenic electron microscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"27251291","version":2,"reference_html":"Diverse roles of assembly factors revealed by structures of late nuclear pre-60S ribosomes. <i> Wu S, Tutuncuoglu B, Yan K, Brown H, Zhang Y, Tan D, Gamalinda M, Yuan Y, Li Z, Jakovljevic J, Ma C, Lei J, Dong MQ, Woolford JL, Gao N. </i> Nature, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","cross_refs":[{"db":"PDB","id":"3JCT"}],"term_name":"disorder to order","curator_orcid":"0000-0003-0192-9906","ec_go":"IDA","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":87,"region_id":"DP02808r006","start":1,"term_id":"IDPO:0000002","statement":[{"text":"There is no statement in the paper but residues 1-87 are disordered ","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"27251291","version":2,"reference_html":"Diverse roles of assembly factors revealed by structures of late nuclear pre-60S ribosomes. <i> Wu S, Tutuncuoglu B, Yan K, Brown H, Zhang Y, Tan D, Gamalinda M, Yuan Y, Li Z, Jakovljevic J, Ma C, Lei J, Dong MQ, Woolford JL, Gao N. </i> Nature, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"3JCT"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":220,"region_id":"DP02808r007","start":181,"term_id":"GO:0098772","statement":[{"text":"Small-angle X-ray scattering, NMR and RNA-binding analyses further reveal that the C-terminal residues of Nop15 are highly flexible, but essential for tight RNA binding. Moreover, comparison with a recently reported cryo-electron microscopy structure indicates that dramatic rearrangement of the C-terminal region of Nop15 in the pre-ribosome exposes the RNA-binding surface to recognize the base of its stem-loop target RNA","type":"Abstract"},{"text":"Comparing our crystal structure with Nop15 in a cryo-EM model of the pre-60S ribosome (17) indicates that the α-helical region is dramatically refolded, which releases the classical RNA-binding residues for interaction at the base of an ITS2 stem-loop and allows interaction of the C-terminal residues near the distal loop of the stem-loop.","type":"Introduction"},{"text":"Our binding assays indicate that the residues of Nop15 C-terminal to the α3/α4 helices (181–220) are important for RNA binding","type":"Results"},{"text":"Moreover, removal of an additional 12 residues from the C-terminus (Nop1581–180) further weakened RNA-binding affinity to 30-fold weaker than Nop15 81–220. Together these results indicate that the C-terminal residues are paradoxically important for RNA recognition, despite sequestering the classical RNA-binding residues.","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"experimental evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"27789691","version":3,"reference_html":"Structural analysis reveals the flexible C-terminus of Nop15 undergoes rearrangement to recognize a pre-ribosomal RNA folding intermediate. <i> Zhang J, Gonzalez LE, Hall TMT. </i> Nucleic Acids Res, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000269","term_name":"molecular function regulator","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":220,"region_id":"DP02808r008","start":181,"term_id":"GO:0003723","statement":[{"text":"Small-angle X-ray scattering, NMR and RNA-binding analyses further reveal that the C-terminal residues of Nop15 are highly flexible, but essential for tight RNA binding. Moreover, comparison with a recently reported cryo-electron microscopy structure indicates that dramatic rearrangement of the C-terminal region of Nop15 in the pre-ribosome exposes the RNA-binding surface to recognize the base of its stem-loop target RNA","type":"Abstract"},{"text":"Comparing our crystal structure with Nop15 in a cryo-EM model of the pre-60S ribosome (17) indicates that the α-helical region is dramatically refolded, which releases the classical RNA-binding residues for interaction at the base of an ITS2 stem-loop and allows interaction of the C-terminal residues near the distal loop of the stem-loop.","type":"Introduction"},{"text":"Our binding assays indicate that the residues of Nop15 C-terminal to the α3/α4 helices (181–220) are important for RNA binding","type":"Results"},{"text":"Moreover, removal of an additional 12 residues from the C-terminus (Nop1581–180) further weakened RNA-binding affinity to 30-fold weaker than Nop15 81–220. Together these results indicate that the C-terminal residues are paradoxically important for RNA recognition, despite sequestering the classical RNA-binding residues.","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"experimental evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"27789691","version":3,"reference_html":"Structural analysis reveals the flexible C-terminus of Nop15 undergoes rearrangement to recognize a pre-ribosomal RNA folding intermediate. <i> Zhang J, Gonzalez LE, Hall TMT. </i> Nucleic Acids Res, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000269","term_name":"RNA binding","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":80,"region_id":"DP02808r009","start":1,"term_id":"GO:0003723","statement":[{"text":"Deletion of the N-terminal region that was not included in our crystal structure (residues 1–80) increased RNA-binding affinity 8 fold (Kd = 35.4 nM for Nop1581–220) (Figure ​(Figure2C2C and D, Table ​Table1).1).","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"experimental evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"27789691","version":3,"reference_html":"Structural analysis reveals the flexible C-terminus of Nop15 undergoes rearrangement to recognize a pre-ribosomal RNA folding intermediate. <i> Zhang J, Gonzalez LE, Hall TMT. </i> Nucleic Acids Res, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000269","term_name":"RNA binding","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":559292,"disprot_id":"DP02808","date":"2020-04-22T02:59:53.136Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":9,"name":"Ribosome biogenesis protein 15","dataset":[],"UniParc":"UPI0000053239","uniref100":"UniRef100_P53927","uniref90":"UniRef90_P53927","uniref50":"UniRef50_P53927","genes":[{"name":{"value":"NOP15","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11583614","url":"http://www.ncbi.nlm.nih.gov/pubmed/11583614","alternativeUrl":"https://europepmc.org/abstract/MED/11583614"}}]},"orfNames":[{"value":"N1954"}],"olnNames":[{"value":"YNL110C"}]}],"alphafold_very_low_content":0.22727272727272727,"disorder_content":0.5863636363636363,"disprot_consensus":{"full":[{"start":1,"end":87,"type":"D"},{"start":179,"end":180,"type":"D"},{"start":181,"end":220,"type":"T"}],"Structural state":[{"start":1,"end":87,"type":"D"},{"start":179,"end":220,"type":"D"}],"Structural transition":[{"start":181,"end":220,"type":"T"}],"Molecular function":[{"start":1,"end":80,"type":"F"},{"start":181,"end":220,"type":"F"}]}},{"acc":"P53193","features":{"gene3D":[{"start":93,"end":182,"id":"G3DSA:1.20.1280.20","name":"HscB, C-terminal domain"},{"start":3,"end":96,"id":"G3DSA:1.10.287.110","name":"DnaJ domain"}],"pfam":[{"id":"PF00226","name":"DnaJ domain","start":32,"end":78},{"id":"PF07743","name":"HSCB C-terminal oligomerisation domain","start":101,"end":170}]},"creator":"fquaglia","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"sequence":"MLKYLVQRRFTSTFYELFPKTFPKKLPIWTIDQSRLRKEYRQLQAQHHPDMAQQGSEQSSTLNQAYHTLKDPLRRSQYMLKLLRNIDLTQEQTSNEVTTSDPQLLLKVLDIHDELSQMDDEAGVKLLEKQNKERIQDIEAQLGQCYNDKDYAAAVKLTVELKYWYNLAKAFKDWAPGKQLEMNH","length":184,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":60,"region_id":"DP02809r001","start":47,"term_id":"IDPO:0000002","statement":[{"text":"The best results were obtained for variant Jac1-C2 (residues 5–182). Similar to Jac1-C1, Jac1-C2 crystallized with two molecules (A and B) in the asymmetric unit and diffracted X-rays to 1.85 Å resolution. The structure was determined for residues 8–181 (A) and 12–176 (B), but segments consisting of residues 47–60 and 95–98 (B) were not resolved.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22306468","version":2,"reference_html":"Interaction of J-protein co-chaperone Jac1 with Fe-S scaffold Isu is indispensable in vivo and conserved in evolution. <i> Ciesielski SJ, Schilke BA, Osipiuk J, Bigelow L, Mulligan R, Majewska J, Joachimiak A, Marszalek J, Craig EA, Dutkiewicz R. </i> J Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3UO3"},{"db":"PDB","id":"3UO2"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":100,"region_id":"DP02809r002","start":91,"term_id":"IDPO:0000002","statement":[{"text":"The structure of Jac1 is L-shaped and consists of 2 distinct α-helical domains (Fig. 1); the N-terminal J-domain (residues 11–84) and the C-terminal Isu binding C-domain (residues 101–184). These two domains are connected by a flexible linker (residues 85–100). ","type":"Results"},{"text":"Interestingly, the linker helix is ordered in molecule A of both Jac1 structures and disordered in molecule B, suggesting intrinsic flexibility of this region.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22306468","version":2,"reference_html":"Interaction of J-protein co-chaperone Jac1 with Fe-S scaffold Isu is indispensable in vivo and conserved in evolution. <i> Ciesielski SJ, Schilke BA, Osipiuk J, Bigelow L, Mulligan R, Majewska J, Joachimiak A, Marszalek J, Craig EA, Dutkiewicz R. </i> J Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3UO2"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":100,"region_id":"DP02809r003","start":91,"term_id":"IDPO:0000033","statement":[{"text":"The structure of Jac1 is L-shaped and consists of 2 distinct α-helical domains (Fig. 1); the N-terminal J-domain (residues 11–84) and the C-terminal Isu binding C-domain (residues 101–184). These two domains are connected by a flexible linker (residues 85–100). ","type":"Results"},{"text":"Interestingly, the linker helix is ordered in molecule A of both Jac1 structures and disordered in molecule B, suggesting intrinsic flexibility of this region.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22306468","version":3,"reference_html":"Interaction of J-protein co-chaperone Jac1 with Fe-S scaffold Isu is indispensable in vivo and conserved in evolution. <i> Ciesielski SJ, Schilke BA, Osipiuk J, Bigelow L, Mulligan R, Majewska J, Joachimiak A, Marszalek J, Craig EA, Dutkiewicz R. </i> J Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"3UO2"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":559292,"disprot_id":"DP02809","date":"2020-04-22T15:37:39.278Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":3,"name":"J-type co-chaperone JAC1, mitochondrial","dataset":["Stress response proteins"],"UniParc":"UPI000013B023","uniref100":"UniRef100_P53193","uniref90":"UniRef90_P53193","uniref50":"UniRef50_P53193","genes":[{"name":{"value":"JAC1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11171977","url":"http://www.ncbi.nlm.nih.gov/pubmed/11171977","alternativeUrl":"https://europepmc.org/abstract/MED/11171977"}},{"code":"ECO:0000312","source":{"name":"SGD","id":"S000002986","url":"https://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000002986"}}]},"synonyms":[{"value":"SEO2"}],"olnNames":[{"value":"YGL018C"}]}],"alphafold_very_low_content":0.05434782608695652,"disorder_content":0.13043478260869565,"disprot_consensus":{"full":[{"start":47,"end":60,"type":"D"},{"start":91,"end":100,"type":"D"}],"Structural state":[{"start":47,"end":60,"type":"D"},{"start":91,"end":100,"type":"D"}],"Disorder function":[{"start":91,"end":100,"type":"F"}]}},{"acc":"P02469","features":{"gene3D":[{"start":19,"end":273,"id":"G3DSA:2.60.120.1490","name":"G3DSA:2.60.120.1490"}],"pfam":[{"id":"PF00053","name":"Laminin EGF domain","start":271,"end":324},{"id":"PF00053","name":"Laminin EGF domain","start":398,"end":455},{"id":"PF00053","name":"Laminin EGF domain","start":458,"end":507},{"id":"PF00053","name":"Laminin EGF domain","start":510,"end":548},{"id":"PF00053","name":"Laminin EGF domain","start":773,"end":818},{"id":"PF00053","name":"Laminin EGF domain","start":821,"end":864},{"id":"PF00053","name":"Laminin EGF domain","start":917,"end":973},{"id":"PF00053","name":"Laminin EGF domain","start":976,"end":1025},{"id":"PF00053","name":"Laminin EGF domain","start":1028,"end":1081},{"id":"PF00053","name":"Laminin EGF domain","start":1084,"end":1126},{"id":"PF00053","name":"Laminin EGF domain","start":1132,"end":1172},{"id":"PF00055","name":"Laminin N-terminal (Domain VI)","start":35,"end":269},{"id":"PF21199","name":"Laminin IV type B domain","start":553,"end":764},{"id":"PF23219","name":"LAMB1-4 helical domain","start":1472,"end":1555},{"id":"PF24973","name":"Laminin/attractin EGF domain","start":335,"end":387},{"id":"PF24973","name":"Laminin/attractin EGF domain","start":867,"end":909}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MGLLQVFAFGVLALWGTRVCAQEPEFSYGCAEGSCYPATGDLLIGRAQKLSVTSTCGLHKPEPYCIVSHLQEDKKCFICDSRDPYHETLNPDSHLIENVVTTFAPNRLKIWWQSENGVENVTIQLDLEAEFHFTHLIMTFKTFRPAAMLIERSSDFGKAWGVYRYFAYDCESSFPGISTGPMKKVDDIICDSRYSDIEPSTEGEVIFRALDPAFKIEDPYSPRIQNLLKITNLRIKFVKLHTLGDNLLDSRMEIREKYYYAVYDMVVRGNCFCYGHASECAPVDGVNEEVEGMVHGHCMCRHNTKGLNCELCMDFYHDLPWRPAEGRNSNACKKCNCNEHSSSCHFDMAVFLATGNVSGGVCDNCQHNTMGRNCEQCKPFYFQHPERDIRDPNLCEPCTCDPAGSENGGICDGYTDFSVGLIAGQCRCKLHVEGERCDVCKEGFYDLSAEDPYGCKSCACNPLGTIPGGNPCDSETGYCYCKRLVTGQRCDQCLPQHWGLSNDLDGCRPCDCDLGGALNNSCSEDSGQCSCLPHMIGRQCNEVESGYYFTTLDHYIYEAEEANLGPGVIVVERQYIQDRIPSWTGPGFVRVPEGAYLEFFIDNIPYSMEYEILIRYEPQLPDHWEKAVITVQRPGKIPASSRCGNTVPDDDNQVVSLSPGSRYVVLPRPVCFEKGMNYTVRLELPQYTASGSDVESPYTFIDSLVLMPYCKSLDIFTVGGSGDGEVTNSAWETFQRYRCLENSRSVVKTPMTDVCRNIIFSISALIHQTGLACECDPQGSLSSVCDPNGGQCQCRPNVVGRTCNRCAPGTFGFGPNGCKPCDCHLQGSASAFCDAITGQCHCFQGIYARQCDRCLPGYWGFPSCQPCQCNGHALDCDTVTGECLSCQDYTTGHNCERCLAGYYGDPIIGSGDHCRPCPCPDGPDSGRQFARSCYQDPVTLQLACVCDPGYIGSRCDDCASGFFGNPSDFGGSCQPCQCHHNIDTTDPEACDKETGRCLKCLYHTEGDHCQLCQYGYYGDALRQDCRKCVCNYLGTVKEHCNGSDCHCDKATGQCSCLPNVIGQNCDRCAPNTWQLASGTGCGPCNCNAAHSFGPSCNEFTGQCQCMPGFGGRTCSECQELFWGDPDVECRACDCDPRGIETPQCDQSTGQCVCVEGVEGPRCDKCTRGYSGVFPDCTPCHQCFALWDAIIGELTNRTHKFLEKAKALKISGVIGPYRETVDSVEKKVNEIKDILAQSPAAEPLKNIGILFEEAEKLTKDVTEKMAQVEVKLTDTASQSNSTAGELGALQAEAESLDKTVKELAEQLEFIKNSDIQGALDSITKYFQMSLEAEKRVNASTTDPNSTVEQSALTRDRVEDLMLERESPFKEQQEEQARLLDELAGKLQSLDLSAVAQMTCGTPPGADCSESECGGPNCRTDEGEKKCGGPGCGGLVTVAHSAWQKAMDFDRDVLSALAEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQIRNFLTEDSADLDSIEAVANEVLKMEMPSTPQQLQNLTEDIRERVETLSQVEVILQQSAADIARAELLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEAEYIEKVVYSVKQNADDVKKTLDGELDEKYKKVESLIAQKTEESADARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISEKVAVYSTCL","length":1786,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":540,"region_id":"DP02810r002","start":494,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The partial LEa domain at the C-terminus is disordered and the structure is therefore referred to as β1 LN-LEa1–4 in this report.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22860131","version":2,"reference_html":"Crystal structures of the network-forming short-arm tips of the laminin β1 and γ1 chains. <i> Carafoli F, Hussain SA, Hohenester E. </i> PLoS One, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4AQS"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-06T14:57:15.336Z"}}],"released":"2023_12","ncbi_taxon_id":10090,"disprot_id":"DP02810","date":"2020-04-22T16:18:04.528Z","organism":"Mus musculus","regions_counter":2,"name":"Laminin subunit beta-1","dataset":[],"UniParc":"UPI000016CE91","uniref100":"UniRef100_P02469","uniref90":"UniRef90_P02469","uniref50":"UniRef50_P07942","genes":[{"name":{"value":"Lamb1"},"synonyms":[{"value":"Lamb-1"},{"value":"Lamb1-1"}]}],"alphafold_very_low_content":0.07390817469204927,"disorder_content":0.02631578947368421,"disprot_consensus":{"full":[{"start":494,"end":540,"type":"D"}],"Structural state":[{"start":494,"end":540,"type":"D"}]}},{"acc":"Q8K419","features":{"gene3D":[],"pfam":[{"id":"PF00337","name":"Galactoside-binding lectin","start":18,"end":149},{"id":"PF00337","name":"Galactoside-binding lectin","start":197,"end":326}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MAYVPAPGYQPTYNPTLPYKRPIPGGLSVGMSVYIQGMAKENMRRFHVNFAVGQDDGADVAFHFNPRFDGWDKVVFNTMQSGQWGKEEKKKSMPFQKGKHFELVFMVMPEHYKVVVNGNSFYEYGHRLPVQMVTHLQVDGDLELQSINFLGGQPAAAPYPGAMTIPAYPAGSPGYNPPQMNTLPVMTGPPVFNPRVPYVGALQGGLTVRRTIIIKGYVLPTARNFVINFKVGSSGDIALHLNPRIGDSVVRNSFMNGSWGAEERKVAYNPFGPGQFFDLSIRCGMDRFKVFANGQHLFDFSHRFQAFQMVDTLEINGDITLSYVQI","length":326,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":12,"region_id":"DP02811r001","start":2,"term_id":"IDPO:0000002","statement":[{"text":"The final crystallographic model consisted of 140 protein residues (corresponding to residues 12–164 of the mGal sequence deposited in GenBank as AAC27245.1), one lactose molecule, two glycerol molecules, part of a polyethylene glycol molecule (comprising two ethylene glycol units), one sodium cation and 189 water molecules.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21358051","version":2,"reference_html":"Structure of the mouse galectin-4 N-terminal carbohydrate-recognition domain reveals the mechanism of oligosaccharide recognition. <i> Krejčiříková V, Pachl P, Fábry M, Malý P, Rezáčová P, Brynda J. </i> Acta Crystallogr D Biol Crystallogr, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3I8T"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":10090,"disprot_id":"DP02811","date":"2020-04-22T16:35:31.341Z","organism":"Mus musculus","regions_counter":1,"name":"Galectin-4","dataset":[],"UniParc":"UPI00000E61A0","uniref100":"UniRef100_Q8K419","uniref90":"UniRef90_Q8K419","uniref50":"UniRef50_P56470","genes":[{"name":{"value":"Lgals4"}}],"alphafold_very_low_content":0.07975460122699386,"disorder_content":0.03374233128834356,"disprot_consensus":{"full":[{"start":2,"end":12,"type":"D"}],"Structural state":[{"start":2,"end":12,"type":"D"}]}},{"acc":"A6NI73","features":{"gene3D":[{"start":138,"end":237,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"},{"start":138,"end":237,"id":"G3DSA:2.60.40.10","name":"Immunoglobulins"}],"pfam":[{"id":"PF13895","name":"Immunoglobulin domain","start":48,"end":135}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MAPWSHPSAQLQPVGGDAVSPALMVLLCLGLSLGPRTHVQAGNLSKATLWAEPGSVISRGNSVTIRCQGTLEAQEYRLVKEGSPEPWDTQNPLEPKNKARFSIPSMTEHHAGRYRCYYYSPAGWSEPSDPLELVVTGFYNKPTLSALPSPVVTSGENVTLQCGSRLRFDRFILTEEGDHKLSWTLDSQLTPSGQFQALFPVGPVTPSHRWMLRCYGSRRHILQVWSEPSDLLEIPVSGAADNLSPSQNKSDSGTASHLQDYAVENLIRMGMAGLILVVLGILIFQDWHSQRSPQAAAGR","length":299,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":157,"region_id":"DP02812r001","start":147,"term_id":"IDPO:0000002","statement":[{"text":"Residues 1 and 2, 106-116, and 136-138 were disordered. 91.8% of total residues were in the most favored regions, and 0% were in the disallowed regions of the Ramachandran plot.","type":"Methods"},{"text":"The AB (residues 106-116) and CC′ (residues 136-138) loops of D2 were disordered (Fig. 1, A and C).","type":"Results"},{"text":"However, residues 106-116 of D2, which corresponds to the A′ strand of D1 in the other LRC receptors, was disordered.","type":"Results"},{"text":"Disordered residue 106-116 of the crystal structure corresponds to sequence residues 147-157","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16675463","version":2,"reference_html":"Crystal structure of the human monocyte-activating receptor, \"Group 2\" leukocyte Ig-like receptor A5 (LILRA5/LIR9/ILT11). <i> Shiroishi M, Kajikawa M, Kuroki K, Ose T, Kohda D, Maenaka K. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2D3V"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":157,"region_id":"DP02812r002","start":147,"term_id":"IDPO:0000002","statement":[{"text":"The average B-factor of D2 (46.0 Å2) was higher than that of domain 1 (D1) (24.3 Å2), which may be due to the relatively loose packing of D2 in the crystal.","type":"Results"},{"text":"Disordered residue 106-116 of the crystal structure corresponds to sequence residues 147-157","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16675463","version":2,"reference_html":"Crystal structure of the human monocyte-activating receptor, \"Group 2\" leukocyte Ig-like receptor A5 (LILRA5/LIR9/ILT11). <i> Shiroishi M, Kajikawa M, Kuroki K, Ose T, Kohda D, Maenaka K. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2D3V"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":157,"region_id":"DP02812r003","start":147,"term_id":"IDPO:0000041","statement":[{"text":"Thus, this loop is more flexible than the equivalent region in the other LRC receptors. Since the predicted N-linked glycosylation site (Asn116) was located on the disordered AB loop in D2, the attached sugar moiety might be expected to be very mobile","type":"Results"},{"text":"Disordered residue 106-116 of the crystal structure corresponds to sequence residues 147-157, therefore the glycosylated residue is Asn157","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16675463","version":2,"reference_html":"Crystal structure of the human monocyte-activating receptor, \"Group 2\" leukocyte Ig-like receptor A5 (LILRA5/LIR9/ILT11). <i> Shiroishi M, Kajikawa M, Kuroki K, Ose T, Kohda D, Maenaka K. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2D3V"}],"term_name":"glycosylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02812","date":"2020-04-22T16:52:49.122Z","organism":"Homo sapiens","regions_counter":3,"name":"Leukocyte immunoglobulin-like receptor subfamily A member 5","dataset":[],"UniParc":"UPI0000034C06","uniref100":"UniRef100_A6NI73","uniref90":"UniRef90_A6NI73","uniref50":"UniRef50_A6NI73","genes":[{"name":{"value":"LILRA5"},"synonyms":[{"value":"ILT11"},{"value":"LILRB7"},{"value":"LIR9"}]}],"alphafold_very_low_content":0.15384615384615385,"disorder_content":0.03678929765886288,"disprot_consensus":{"full":[{"start":147,"end":157,"type":"D"}],"Structural state":[{"start":147,"end":157,"type":"D"}],"Disorder function":[{"start":147,"end":157,"type":"F"}]}},{"acc":"P62330","features":{"gene3D":[],"pfam":[{"id":"PF00025","name":"ADP-ribosylation factor family","start":2,"end":172}]},"creator":"lchemes","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MGKVLSKIFGNKEMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTYKNVKFNVWDVGGQDKIRPLWRHYYTGTQGLIFVVDCADRDRIDEARQELHRIINDREMRDAIILIFANKQDLPDAMKPHEIQEKLGLTRIRDRNWYVQPSCATSGDGLYEGLTWLTSNYKS","length":175,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":56,"region_id":"DP02815r001","start":34,"term_id":"IDPO:0000002","statement":[{"text":"The crystal structure of Δ13Arf6-GDP reveals an unprecedented unfolding of the GTPase core β-strands, which is fully accounted for by small-angle X-ray scattering data in solution and by ab initio three-dimensional envelope calculation. NMR chemical shifts identify this structural disorder in Δ13Arf6-GDP, ","type":"Abstract"},{"text":"The structure of Δ13Arf6-GDP in the crystal and in solution was analyzed by the combination of structural and biophysical methods, revealing a partial unfolding of the switch 1 and interswitch regions unique to this small GTPase. ","type":"Abstract"},{"text":"Residues affected by structural changes extend from Lys34 in strand β1′, which corresponds to switch 1 in Arf-GDP structures, to Asn56 after strand β2 (interswitch) in the central β-sheet. The β1′–β2 region is essentially disordered in one Δ13Arf6-GDP subunit of the asymmetric unit, while in the other subunit, β1′–β2","type":"Results"},{"text":"strands β1′ and β2, which form switch 1 and part of the interswitch in Arf6-GDPFL, are relocated as far as 47 Å away from their original positions, yielding a flexible loop that protrudes from the small GTPase core","type":"Discussion"}],"curator_id":"lchemes","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"20709080","version":2,"reference_html":"SAXS and X-ray crystallography suggest an unfolding model for the GDP/GTP conformational switch of the small GTPase Arf6. <i> Biou V, Aizel K, Roblin P, Thureau A, Jacquet E, Hansson S, Guibert B, Guittet E, van Heijenoort C, Zeghouf M, Perez J, Cherfils J. </i> J Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3N5C"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":56,"region_id":"DP02815r002","start":34,"term_id":"IDPO:0000002","statement":[{"text":"The crystal structure of Δ13Arf6-GDP reveals an unprecedented unfolding of the GTPase core β-strands, which is fully accounted for by small-angle X-ray scattering data in solution and by ab initio three-dimensional envelope calculation. NMR chemical shifts identify this structural disorder in Δ13Arf6-GDP, ","type":"Abstract"},{"text":"The structure of Δ13Arf6-GDP in the crystal and in solution was analyzed by the combination of structural and biophysical methods, revealing a partial unfolding of the switch 1 and interswitch regions unique to this small GTPase. ","type":"Abstract"},{"text":"NMR: NMR chemical shifts provide a powerful means of detecting local disorder in proteins…It features a significant number of peaks that are too broad to be resolved individually, and a paucity of peaks in the ranges 8.5–10 ppm (1 H) and 123– 133 ppm (15N), which generally correspond to βsheet structures….fully consistent with the unfolding of β-strands and with the enrichment in flexible structures, as seen in the Δ13Arf6-GDP crystal","type":"Results"},{"text":"strands β1′ and β2, which form switch 1 and part of the interswitch in Arf6-GDPFL, are relocated as far as 47 Å away from their original positions, yielding a flexible loop that protrudes from the small GTPase core","type":"Discussion"}],"curator_id":"lchemes","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"20709080","version":2,"reference_html":"SAXS and X-ray crystallography suggest an unfolding model for the GDP/GTP conformational switch of the small GTPase Arf6. <i> Biou V, Aizel K, Roblin P, Thureau A, Jacquet E, Hansson S, Guibert B, Guittet E, van Heijenoort C, Zeghouf M, Perez J, Cherfils J. </i> J Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"3N5C"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":56,"region_id":"DP02815r003","start":34,"term_id":"IDPO:0000002","statement":[{"text":"The crystal structure of Δ13Arf6-GDP reveals an unprecedented unfolding of the GTPase core β-strands, which is fully accounted for by small-angle X-ray scattering data in solution and by ab initio three-dimensional envelope calculation. NMR chemical shifts identify this structural disorder in Δ13Arf6-GDP, ","type":"Abstract"},{"text":"The structure of Δ13Arf6-GDP in the crystal and in solution was analyzed by the combination of structural and biophysical methods, revealing a partial unfolding of the switch 1 and interswitch regions unique to this small GTPase. ","type":"Abstract"},{"text":"SAXS: The SAXS envelope of Arf6- GDPFL was essentially globular and superimposed very well with the crystal structure of Arf6-GDPFL (Fig. 3c). In contrast, the Δ13Arf6-GDP SAXS envelope displayed a large protrusion (Fig. 3d). Remarkably, the protrusion readily accommodated the partially unfolded β1′–β2 strands from the Δ13Arf6-GDP crystal structure (Fig. 3d), suggesting that a similar unfolding takes place in solution","type":"Results"},{"text":"strands β1′ and β2, which form switch 1 and part of the interswitch in Arf6-GDPFL, are relocated as far as 47 Å away from their original positions, yielding a flexible loop that protrudes from the small GTPase core","type":"Discussion"}],"curator_id":"lchemes","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"20709080","version":2,"reference_html":"SAXS and X-ray crystallography suggest an unfolding model for the GDP/GTP conformational switch of the small GTPase Arf6. <i> Biou V, Aizel K, Roblin P, Thureau A, Jacquet E, Hansson S, Guibert B, Guittet E, van Heijenoort C, Zeghouf M, Perez J, Cherfils J. </i> J Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","cross_refs":[{"db":"PDB","id":"3N5C"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":56,"region_id":"DP02815r004","start":34,"term_id":"IDPO:0000011","statement":[{"text":"The crystal structure of Δ13Arf6-GDP reveals an unprecedented unfolding of the GTPase core β-strands, which is fully accounted for by small-angle X-ray scattering data in solution and by ab initio three-dimensional envelope calculation. NMR chemical shifts identify this structural disorder in Δ13Arf6-GDP, ","type":"Abstract"},{"text":"The structure of Δ13Arf6-GDP in the crystal and in solution was analyzed by the combination of structural and biophysical methods, revealing a partial unfolding of the switch 1 and interswitch regions unique to this small GTPase. ","type":"Abstract"},{"text":"Altogether, this is one of the largest conformational departures from the classical fold of a small GTPase....This indicates that the local disorder in Δ13Arf6- GDP is not an intrinsic property of Δ13Arf6, but is specific for its GDP-bound form\n\n","type":"Results"},{"text":"strands β1′ and β2, which form switch 1 and part of the interswitch in Arf6-GDPFL, are relocated as far as 47 Å away from their original positions, yielding a flexible loop that protrudes from the small GTPase core","type":"Discussion"}],"curator_id":"lchemes","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"20709080","version":2,"reference_html":"SAXS and X-ray crystallography suggest an unfolding model for the GDP/GTP conformational switch of the small GTPase Arf6. <i> Biou V, Aizel K, Roblin P, Thureau A, Jacquet E, Hansson S, Guibert B, Guittet E, van Heijenoort C, Zeghouf M, Perez J, Cherfils J. </i> J Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"3N5C"}],"term_name":"disorder to order","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":56,"region_id":"DP02815r005","start":34,"term_id":"GO:0098772","statement":[{"text":"The crystal structure of Δ13Arf6-GDP reveals an unprecedented unfolding of the GTPase core β-strands, which is fully accounted for by small-angle X-ray scattering data in solution and by ab initio three-dimensional envelope calculation. NMR chemical shifts identify this structural disorder in Δ13Arf6-GDP [...] Taken together, these experiments suggest an unfolding model for the nucleotide switch of Arf6 and shed new light on its biochemical differences with Arf1.","type":"Abstract"},{"text":"The structure of Δ13Arf6-GDP in the crystal and in solution was analyzed by the combination of structural and biophysical methods, revealing a partial unfolding of the switch 1 and interswitch regions unique to this small GTPase. \n","type":"Abstract"},{"text":"Altogether, this is one of the largest conformational departures from the classical fold of a small GTPase [...] the 1 H–15N HSQC spectrum of Δ13Arf6-GTP is very well defined and is representative of a well-ordered conformation (Fig. 2, blue). This indicates that the local disorder in Δ13Arf6- GDP is not an intrinsic property of Δ13Arf6, but is specific for its GDP-bound form\n\n","type":"Results"},{"text":"Altogether, our results suggest that the GDP/GTP structural switch of Arf6 may follow a structural route different from that of Arf1. The interswitch toggle of Arf6 may proceed through a local unfolding of the interswitch, possibly via a GEFbound intermediate in which Arf6 resembles the Δ13Arf6-GDP structure (Fig. 5d)","type":"Discussion"},{"text":"The conformational switch is proposed to participate in the nucleotide exchange (GTP/GDP) function of Arf6","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"20709080","version":3,"reference_html":"SAXS and X-ray crystallography suggest an unfolding model for the GDP/GTP conformational switch of the small GTPase Arf6. <i> Biou V, Aizel K, Roblin P, Thureau A, Jacquet E, Hansson S, Guibert B, Guittet E, van Heijenoort C, Zeghouf M, Perez J, Cherfils J. </i> J Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"3N5C"}],"term_name":"molecular function regulator","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02815","date":"2020-04-22T18:33:44.955Z","organism":"Homo sapiens","regions_counter":5,"name":"ADP-ribosylation factor 6","dataset":[],"UniParc":"UPI0000027915","uniref100":"UniRef100_P62330","uniref90":"UniRef90_P62330","uniref50":"UniRef50_P62330","genes":[{"name":{"value":"ARF6","evidences":[{"code":"ECO:0000303","source":{"name":"Citation","id":"Ref.6","url":"https://www.uniprot.org/uniprot/null#ref6"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:659","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:659"}}]}}],"alphafold_very_low_content":0.005714285714285714,"disorder_content":0.13142857142857142,"disprot_consensus":{"full":[{"start":34,"end":56,"type":"T"}],"Structural state":[{"start":34,"end":56,"type":"D"}],"Structural transition":[{"start":34,"end":56,"type":"T"}],"Molecular function":[{"start":34,"end":56,"type":"F"}]}},{"acc":"P48740-3","features":{"pfam":[]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MRWLLLYYALCFSLSKASAHTVELNNMFGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGSFMSITFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVECSDNLFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDIFDIEDHPEVPCPYDYIKIKVGPKVLGPFCGEKAPEPISTQSHSVLILFHSDNSGENRGWRLSYRAAGNECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDTFQIECLKDGTWSNKIPTCKKNEIDLESELKSEQVTE","length":380,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":380,"region_id":"DP02816r001","start":364,"term_id":"IDPO:0000002","statement":[{"text":"The 17 C-terminal residues that are unique to MAP-1 are disordered in the crystal. ","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22854970","version":2,"reference_html":"Crystal structure and functional characterization of the complement regulator mannose-binding lectin (MBL)/ficolin-associated protein-1 (MAP-1). <i> Skjoedt MO, Roversi P, Hummelshøj T, Palarasah Y, Rosbjerg A, Johnson S, Lea SM, Garred P. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02816","date":"2020-04-22T18:34:19.507Z","organism":"Homo sapiens","regions_counter":1,"name":"Isoform 3 of Mannan-binding lectin serine protease 1","dataset":[],"UniParc":"UPI000020A983","uniref100":"","uniref90":"","uniref50":"","genes":[{"name":{"value":"MASP1"},"synonyms":[{"value":"CRARF"},{"value":"CRARF1"},{"value":"PRSS5"}]}],"disorder_content":0.04473684210526316,"disprot_consensus":{"full":[{"start":364,"end":380,"type":"D"}],"Structural state":[{"start":364,"end":380,"type":"D"}]}},{"acc":"Q64373","features":{"gene3D":[{"start":1,"end":209,"id":"G3DSA:1.10.437.10","name":"Blc2-like"}],"pfam":[{"id":"PF00452","name":"Apoptosis regulator proteins, Bcl-2 family","start":90,"end":188},{"id":"PF02180","name":"Bcl-2 homology region 4","start":1,"end":26}]},"creator":"lchemes","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEETEAERETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIASWMATYLNDHLEPWIQENGGWDTFVDLYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK","length":233,"regions":[{"region_id":"DP02817r001","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T12:43:43.546Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":81,"term_id":"IDPO:0000002","start":28,"version":2,"statement":[{"text":"When Bcl-xl F105A (form II) and Bcl-xl F105A (form I) were superposed for 142 Ca (except for Ser28 to Ile81), the overlay, with an RMSD of 0.43 Å, suggested that they were very similar overall\n\n","type":"Results"},{"text":"During the course of determining the three-dimensional structure of Bcl-xl, a large region of Bcl-xl was found to be unstructured in the wild type and Y101A and F105A mutant forms, as determined by previous NMR and X-ray crystallographic techniques [3–6,9]. ","type":"Discussion"},{"text":"This and previous structures show that the region 28-81 is disordered with missing electron density","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"20206602","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3IHC"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lchemes","reference_html":"Structural insights into mouse anti-apoptotic Bcl-xl reveal affinity for Beclin 1 and gossypol. <i> Priyadarshi A, Roy A, Kim KS, Kim EE, Hwang KY. </i> Biochem Biophys Res Commun, 2010","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":81,"region_id":"DP02817r002","start":28,"term_id":"IDPO:0000037","statement":[{"text":"The rate of nonenzymatic deamidation of two asparagines in the antiapoptotic protein Bcl-xL is accelerated by this increase in pH. Deamidation of these asparagines is a signal for the degradation of Bcl-xL, which is a component of the apoptotic response to DNA damage […]we present evidence that deamidation of human Bcl-xL is intramolecularly catalyzed in a manner that is dependent upon these histidines. Further, we present evidence that these histidines act as a pH-sensitive switch that enhances the effect of the increase in pH on the rate of Bcl-xL deamidation","type":"Abstract"},{"text":"We have previously demonstrated that the antiapoptotic Bcl-2 family member Bcl-xL undergoes deamidation at Asn 52 and Asn 66 when susceptible tumor cells are treated with DNAdamaging antineoplastic agents [...] We now report that human Bcl-xL contains histidines in close proximity to each of its two deamidation sites and that such histidines are conserved throughout the Bcl-xL p\nIndeed, we show here that deamidation of human Bcl-xL is intramolecularly catalyzed in a manner that involves these highly conserved histidines and that treatment of susceptible tumor cells with DNA-damaging agents increases the catalytic activity.\n","type":"Introduction"},{"text":"Additionally, we consistently found that total Bcl-xL(H58A/H71A) is markedly increased relative to total wild-type Bcl-xL in cisplatin-treated cells (Fig. 5A). Finally, we found that Bcl-xL(H58A/H71A) is deamidated at a slower rate than wild-type Bcl-xL in cells treated with cycloheximide (Fig. 5B)","type":"Results"},{"text":"All residues that are deamidated (N52 and N66) as well as the catalytic histidines (H58 and H71) are within the IDP region","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"immunodetection assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"29694915","version":2,"reference_html":"Bcl-xL deamidation is regulated by multiple ion transporters and is intramolecularly catalyzed. <i> Dho SH, Manson SR, Jung SH, Lim JC, Weintraub SJ. </i> Biochim Biophys Acta Mol Cell Res, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007719","term_name":"molecular recognition display site","curator_orcid":"0000-0003-0192-9906","ec_go":"IDA","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":10090,"disprot_id":"DP02817","date":"2020-04-22T19:24:17.749Z","organism":"Mus musculus","regions_counter":2,"name":"Bcl-2-like protein 1","dataset":[],"UniParc":"UPI000002103C","uniref100":"UniRef100_Q64373","uniref90":"UniRef90_Q64373","uniref50":"UniRef50_Q64373","genes":[{"name":{"value":"Bcl2l1"},"synonyms":[{"value":"Bcl2l"},{"value":"Bclx"}]}],"alphafold_very_low_content":0.2832618025751073,"disorder_content":0.2317596566523605,"disprot_consensus":{"full":[{"start":28,"end":81,"type":"D"}],"Structural state":[{"start":28,"end":81,"type":"D"}],"Disorder function":[{"start":28,"end":81,"type":"F"}]}},{"acc":"Q07157","features":{"gene3D":[{"start":410,"end":518,"id":"G3DSA:2.30.42.10","name":"G3DSA:2.30.42.10"},{"start":410,"end":518,"id":"G3DSA:2.30.42.10","name":"G3DSA:2.30.42.10"},{"start":410,"end":518,"id":"G3DSA:2.30.42.10","name":"G3DSA:2.30.42.10"}],"pfam":[{"id":"PF00595","name":"PDZ domain","start":23,"end":106},{"id":"PF00595","name":"PDZ domain","start":187,"end":261},{"id":"PF00595","name":"PDZ domain","start":428,"end":499},{"id":"PF00625","name":"Guanylate kinase","start":691,"end":792},{"id":"PF00791","name":"ZU5 domain","start":1637,"end":1720},{"id":"PF07653","name":"Variant SH3 domain","start":520,"end":582}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MSARAAAAKSTAMEETAIWEQHTVTLHRAPGFGFGIAISGGRDNPHFQSGETSIVISDVLKGGPAEGQLQENDRVAMVNGVSMDNVEHAFAVQQLRKSGKNAKITIRRKKKVQIPVSRPDPEPVSDNEEDSYDEEIHDPRSGRSGVVNRRSEKIWPRDRSASRERSLSPRSDRRSVASSQPAKPTKVTLVKSRKNEEYGLRLASHIFVKEISQDSLAARDGNIQEGDVVLKINGTVTENMSLTDAKTLIERSKGKLKMVVQRDERATLLNVPDLSDSIHSANASERDDISEIQSLASDHSGRSHDRPPRRSRSRSPDQRSEPSDHSRHSPQQPSNGSLRSRDEERISKPGAVSTPVKHADDHTPKTVEEVTVERNEKQTPSLPEPKPVYAQVGQPDVDLPVSPSDGVLPNSTHEDGILRPSMKLVKFRKGDSVGLRLAGGNDVGIFVAGVLEDSPAAKEGLEEGDQILRVNNVDFTNIIREEAVLFLLDLPKGEEVTILAQKKKDVYRRIVESDVGDSFYIRTHFEYEKESPYGLSFNKGEVFRVVDTLYNGKLGSWLAIRIGKNHKEVERGIIPNKNRAEQLASVQYTLPKTAGGDRADFWRFRGLRSSKRNLRKSREDLSAQPVQTKFPAYERVVLREAGFLRPVTIFGPIADVAREKLAREEPDIYQIAKSEPRDAGTDQRSSGIIRLHTIKQIIDQDKHALLDVTPNAVDRLNYAQWYPIVVFLNPDSKQGVKTMRMRLCPESRKSARKLYERSHKLRKNNHHLFTTTINLNSMNDGWYGALKEAIQQQQNQLVWVSEGKADGATSDDLDLHDDRLSYLSAPGSEYSMYSTDSRHTSDYEDTDTEGGAYTDQELDETLNDEVGTPPESAITRSSEPVREDSSGMHHENQTYPPYSPQAQPQPIHRIDSPGFKPASQQKAEASSPVPYLSPETNPASSTSAVNHNVNLTNVRLEEPTPAPSTSYSPQADSLRTPSTEAAHIMLRDQEPSLSSHVDPTKVYRKDPYPEEMMRQNHVLKQPAVSHPGHRPDKEPNLTYEPQLPYVEKQASRDLEQPTYRYESSSYTDQFSRNYEHRLRYEDRVPMYEEQWSYYDDKQPYPSRPPFDNQHSQDLDSRQHPEESSERGYFPRFEEPAPLSYDSRPRYEQAPRASALRHEEQPAPGYDTHGRLRPEAQPHPSAGPKPAESKQYFEQYSRSYEQVPPQGFTSRAGHFEPLHGAAAVPPLIPSSQHKPEALPSNTKPLPPPPTQTEEEEDPAMKPQSVLTRVKMFENKRSASLETKKDVNDTGSFKPPEVASKPSGAPIIGPKPTSQNQFSEHDKTLYRIPEPQKPQLKPPEDIVRSNHYDPEEDEEYYRKQLSYFDRRSFENKPPAHIAASHLSEPAKPAHSQNQSNFSSYSSKGKPPEADGVDRSFGEKRYEPIQATPPPPPLPSQYAQPSQPVTSASLHIHSKGAHGEGNSVSLDFQNSLVSKPDPPPSQNKPATFRPPNREDTAQAAFYPQKSFPDKAPVNGTEQTQKTVTPAYNRFTPKPYTSSARPFERKFESPKFNHNLLPSETAHKPDLSSKTPTSPKTLVKSHSLAQPPEFDSGVETFSIHAEKPKYQINNISTVPKAIPVSPSAVEEDEDEDGHTVVATARGIFNSNGGVLSSIETGVSIIIPQGAIPEGVEQEIYFKVCRDNSILPPLDKEKGETLLSPLVMCGPHGLKFLKPVELRLPHCDPKTWQNKCLPGDPNYLVGANCVSVLIDHF","length":1748,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":627,"region_id":"DP02818r001","start":589,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The previous structures of the SG domains of ZO proteins revealed flexibility between the SH3 and GUK domains (that is, the structure of each individual domain is rather rigid, but the relative domain-domain conformation is variable).","type":"Results"},{"text":"The U5 region is a variable surface loop sequence near the C-terminal part of the SH3 domain. It is present in the PSG construct but did not show any traceable electron density.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22030391","version":2,"reference_html":"The Src homology 3 domain is required for junctional adhesion molecule binding to the third PDZ domain of the scaffolding protein ZO-1. <i> Nomme J, Fanning AS, Caffrey M, Lye MF, Anderson JM, Lavie A. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3TSZ"},{"db":"PDB","id":"3TSW"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-10-31T19:20:04.753Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":627,"region_id":"DP02818r002","start":589,"term_id":"IDPO:0000033","unpublished":true,"statement":[{"text":"The previous structures of the SG domains of ZO proteins revealed flexibility between the SH3 and GUK domains (that is, the structure of each individual domain is rather rigid, but the relative domain-domain conformation is variable).","type":"Results"},{"text":"The U5 region is a variable surface loop sequence near the C-terminal part of the SH3 domain. It is present in the PSG construct but did not show any traceable electron density.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22030391","version":3,"reference_html":"The Src homology 3 domain is required for junctional adhesion molecule binding to the third PDZ domain of the scaffolding protein ZO-1. <i> Nomme J, Fanning AS, Caffrey M, Lye MF, Anderson JM, Lavie A. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"3TSZ"},{"db":"PDB","id":"3TSW"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-10-31T19:20:05.698Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":687,"region_id":"DP02818r003","start":675,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Final built models comprised the following residues: PSG 417–587, 629–674, and 688–803. Residue Lys629 was modeled as an alanine (residues: 588–628 (U5) and 675–687 were lacking unambiguous electron density); PSG+JAM-A 421–588, 628–684, and 687–802 (residues: 417–420, 589–627 (U5), 685, 686, and 803 were lacking unambiguous electron density); PDZ3 420–512 (residues: 417–419 and 513–516 were lacking unambiguous electron density).","type":"Methods"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22030391","version":2,"reference_html":"The Src homology 3 domain is required for junctional adhesion molecule binding to the third PDZ domain of the scaffolding protein ZO-1. <i> Nomme J, Fanning AS, Caffrey M, Lye MF, Anderson JM, Lavie A. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3TSW"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-10-31T19:20:04.500Z"}},{"start":265,"end":420,"reference_id":"30354300","reference_source":"pmid","reference_html":"Whole-Exome Sequencing Identifies Pathogenic Variants in TJP1 Gene Associated With Arrhythmogenic Cardiomyopathy. <i> De Bortoli M, Postma AV, Poloni G, Calore M, Minervini G, Mazzotti E, Rigato I, Ebert M, Lorenzon A, Vazza G, Cipriani A, Bariani R, Perazzolo Marra M, Husser D, Thiene G, Daliento L, Corrado D, Basso C, Tosatto SCE, Bauce B, van Tintelen JP, Rampazzo A. </i> Circ Genom Precis Med, 2018","date":"2022-11-10T19:01:54.171Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02818r004","statement":[{"text":"All 4 TJP1 variants are predicted to be deleterious and affect highly conserved amino acids, either at the GUK (guanylate kinase)–like domain (p.(Y669C)) or at the disordered region of the protein between the PDZ2 and PDZ3 domains (p.(R265W), p.(S329L), and p.(D360V)).","type":"Abstract"},{"text":"Since the PDZ2 domain comprises the 186-264 region, and the PDZ3 domain comprises the 421-502 region, the authors are referring to the 265-420 region as disordered.","type":"Curator statement"}]},{"start":795,"end":1631,"reference_id":"33806674","reference_source":"pmid","reference_html":"NMR-Guided Repositioning of Non-Steroidal Anti-Inflammatory Drugs into Tight Junction Modulators.  <i> Tenno T, Kataoka K, Goda N, Hiroaki H. </i> Int J Mol Sci, 2021","date":"2022-11-10T19:58:37.996Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02818r005","statement":[{"text":"ZO-1/2 harbors three consecutive PSD-95/Discs large/and ZO-1 (PDZ) domains at the N-terminus of the protein. They follow a Src homology domain, the guanylate kinase (GUK) domain, and a long intrinsically disordered region that contains the actin-binding site (Figure 1c).","type":"Introduction"},{"text":"In the Figure 1c the authors shows the IDR spans between the GUK domain (606-794) and the ZU5 domain (1632-1748).","type":"Curator statement"}]}],"released":"2023_12","ncbi_taxon_id":9606,"disprot_id":"DP02818","date":"2020-04-23T14:21:04.297Z","organism":"Homo sapiens","regions_counter":5,"name":"Tight junction protein ZO-1","dataset":["Condensates-related proteins"],"UniParc":"UPI000013C445","uniref100":"UniRef100_Q07157","uniref90":"UniRef90_Q07157","uniref50":"UniRef50_Q07157","genes":[{"name":{"value":"TJP1"},"synonyms":[{"value":"ZO1"}]}],"alphafold_very_low_content":0.6332951945080092,"disorder_content":0.5978260869565217,"disprot_consensus":{"full":[{"start":265,"end":420,"type":"D"},{"start":589,"end":627,"type":"D"},{"start":675,"end":687,"type":"D"},{"start":795,"end":1631,"type":"D"}],"Structural state":[{"start":265,"end":420,"type":"D"},{"start":589,"end":627,"type":"D"},{"start":675,"end":687,"type":"D"},{"start":795,"end":1631,"type":"D"}],"Disorder function":[{"start":589,"end":627,"type":"F"}]}},{"acc":"Q62420","features":{"gene3D":[{"start":1,"end":247,"id":"G3DSA:1.20.1270.60","name":"Arfaptin homology (AH) domain/BAR domain"}],"pfam":[{"id":"PF00018","name":"SH3 domain","start":296,"end":340},{"id":"PF03114","name":"BAR domain","start":6,"end":241}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MSVAGLKKQFHKATQKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRLEERIRQASSQPRREYQPKPRMSLEFATGDSTQPNGGLSHTGTPKPPGVQMDQPCCRALYDFEPENEGELGFKEGDIITLTNQIDENWYEGMLHGQSGFFPINYVEILVALPH","length":352,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":26,"region_id":"DP02819r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"Residues 1–26 are disordered at the N termini, which both point in the direction of the distal ends of the crescent-shaped dimer.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16023669","version":2,"reference_html":"Crystal structure of the endophilin-A1 BAR domain. <i> Weissenhorn W. </i> J Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1ZWW"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":86,"region_id":"DP02819r002","start":67,"term_id":"IDPO:0000002","statement":[{"text":"Residues 67–86 (in the second protomer, residues 70–84) are disordered in the structure and they could extend either sideward or perpendicularly to the concave surface.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"16023669","version":2,"reference_html":"Crystal structure of the endophilin-A1 BAR domain. <i> Weissenhorn W. </i> J Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1ZWW"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":86,"region_id":"DP02819r003","start":67,"term_id":"GO:0098772","statement":[{"text":"Here, we present the 2.3 A crystal structure of the endophilin-A1 BAR domain, which has been suggested to function in inducing and sensing membrane curvature at the site of endocytosis.","type":"Abstract"},{"text":"The endophilin-1A BAR domain thus constitutes a new variant of a BAR domain, and it may link endophilin-1A BAR function to calcium regulation of endocytosis.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"16023669","version":3,"reference_html":"Crystal structure of the endophilin-A1 BAR domain. <i> Weissenhorn W. </i> J Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"1ZWW"}],"term_name":"molecular function regulator","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":10090,"disprot_id":"DP02819","date":"2020-04-23T15:36:33.663Z","organism":"Mus musculus","regions_counter":3,"name":"Endophilin-A1","dataset":[],"UniParc":"UPI0000029023","uniref100":"UniRef100_Q62420","uniref90":"UniRef90_O35179","uniref50":"UniRef50_O35179","genes":[{"name":{"value":"Sh3gl2"},"synonyms":[{"value":"Een1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"21849472","url":"http://www.ncbi.nlm.nih.gov/pubmed/21849472","alternativeUrl":"https://europepmc.org/abstract/MED/21849472"}}]},{"value":"Sh3d2a"}]}],"alphafold_very_low_content":0.10227272727272728,"disorder_content":0.13068181818181818,"disprot_consensus":{"full":[{"start":1,"end":26,"type":"D"},{"start":67,"end":86,"type":"D"}],"Structural state":[{"start":1,"end":26,"type":"D"},{"start":67,"end":86,"type":"D"}],"Molecular function":[{"start":67,"end":86,"type":"F"}]}},{"acc":"Q62264","features":{"gene3D":[],"pfam":[{"id":"PF07084","name":"Thyroid hormone-inducible hepatic protein Spot 14","start":1,"end":148}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MQVLTKRYPKNCLLTVMDRYSAVVRNMEQVVMIPSLLRDVQLSGPGGSVQDGAPDLYTYFTMLKSICVEVDHGLLPREEWQAKVAGNETSEAENDAAETEEAEEDRISEELDLEAQFHLHFCSLHHILTHLTRKAQEVTRKYQEMTGQVL","length":150,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":104,"region_id":"DP02820r001","start":77,"term_id":"IDPO:0000002","statement":[{"text":"The model spans residues 8–149, although residues 46–48 and 77–104 are poorly ordered and were not placed in the electron density.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20952656","version":2,"reference_html":"Crystal structure of Spot 14, a modulator of fatty acid synthesis. <i> Colbert CL, Kim CW, Moon YA, Henry L, Palnitkar M, McKean WB, Fitzgerald K, Deisenhofer J, Horton JD, Kwon HJ. </i> Proc Natl Acad Sci U S A, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3ONT"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9CQ20","partner_end":null}],"ec_ontology":"ECO","end":150,"region_id":"DP02820r002","start":1,"term_id":"GO:0005515","statement":[{"text":"Interaction of S14 and MIG12 in Cultured Cells.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"co-immunoprecipitation evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"20952656","version":3,"reference_html":"Crystal structure of Spot 14, a modulator of fatty acid synthesis. <i> Colbert CL, Kim CW, Moon YA, Henry L, Palnitkar M, McKean WB, Fitzgerald K, Deisenhofer J, Horton JD, Kwon HJ. </i> Proc Natl Acad Sci U S A, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006030","term_name":"protein binding","curator_orcid":"0000-0002-0341-4888","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":150,"region_id":"DP02820r003","start":1,"term_id":"GO:0140678","statement":[{"text":"The structure of S14 suggests a mechanism whereby heterodimer formation with MIG12 attenuates the ability of MIG12 to activate ACC.","type":"Abstract"},{"text":"S14 Knockdown Increases ACC Polymerization and Activity in Vivo.","type":"Results"},{"text":"Increasing S14 levels resulted in reduced ACC polymerization (Fig. 5A) and less MIG12 incorporation into ACC polymers","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"20952656","version":3,"reference_html":"Crystal structure of Spot 14, a modulator of fatty acid synthesis. <i> Colbert CL, Kim CW, Moon YA, Henry L, Palnitkar M, McKean WB, Fitzgerald K, Deisenhofer J, Horton JD, Kwon HJ. </i> Proc Natl Acad Sci U S A, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007689","cross_refs":[{"db":"PDB","id":"3ONT"}],"term_name":"molecular function inhibitor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":10090,"disprot_id":"DP02820","date":"2020-04-23T16:06:02.862Z","organism":"Mus musculus","regions_counter":3,"name":"Thyroid hormone-inducible hepatic protein","dataset":[],"UniParc":"UPI00000040AA","uniref100":"UniRef100_Q62264","uniref90":"UniRef90_Q62264","uniref50":"UniRef50_Q62264","genes":[{"name":{"value":"Thrsp"},"synonyms":[{"value":"S14"}]}],"alphafold_very_low_content":0.18,"disorder_content":0.18666666666666668,"disprot_consensus":{"full":[{"start":1,"end":76,"type":"F"},{"start":77,"end":104,"type":"D"},{"start":105,"end":150,"type":"F"}],"Structural state":[{"start":77,"end":104,"type":"D"}],"Molecular function":[{"start":1,"end":150,"type":"F"}]}},{"acc":"Q8IVH8","features":{"gene3D":[],"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":16,"end":273},{"id":"PF00780","name":"CNH domain","start":572,"end":860}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MNPGFDLSRRNPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDCKHPNIVAYFGSYLRRDKLWICMEFCGGGSLQDIYHVTGPLSELQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKRKSFIGTPYWMAPEVAAVERKGGYNQLCDLWAVGITAIELAELQPPMFDLHPMRALFLMTKSNFQPPKLKDKMKWSNSFHHFVKMALTKNPKKRPTAEKLLQHPFVTQHLTRSLAIELLDKVNNPDHSTYHDFDDDDPEPLVAVPHRIHSTSRNVREEKTRSEITFGQVKFDPPLRKETEPHHELPDSDGFLDSSEEIYYTARSNLDLQLEYGQGHQGGYFLGANKSLLKSVEEELHQRGHVAHLEDDEGDDDESKHSTLKAKIPPPLPPKPKSIFIPQEMHSTEDENQGTIKRCPMSGSPAKPSQVPPRPPPPRLPPHKPVALGNGMSSFQLNGERDGSLCQQQNEHRGTNLSRKEKKDVPKPISNGLPPTPKVHMGACFSKVFNGCPLKIHCASSWINPDTRDQYLIFGAEEGIYTLNLNELHETSMEQLFPRRCTWLYVMNNCLLSISGKASQLYSHNLPGLFDYARQMQKLPVAIPAHKLPDRILPRKFSVSAKIPETKWCQKCCVVRNPYTGHKYLCGALQTSIVLLEWVEPMQKFMLIKHIDFPIPCPLRMFEMLVVPEQEYPLVCVGVSRGRDFNQVVRFETVNPNSTSSWFTESDTPQTNVTHVTQLERDTILVCLDCCIKIVNLQGRLKSSRKLSSELTFDFQIESIVCLQDSVLAFWKHGMQGRSFRSNEVTQEISDSTRIFRLLGSDRVVVLESRPTDNPTANSNLYILAGHENSY","length":894,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":380,"region_id":"DP02822r001","start":315,"term_id":"IDPO:0000002","statement":[{"text":"The density for the compound was clearly distinct, as was in general the backbone density for residues between 13 and 314 (the site of Clostripain cleavage in solution), but the residues that follow were disordered.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27727493","version":2,"reference_html":"Germinal-center kinase-like kinase co-crystal structure reveals a swapped activation loop and C-terminal extension. <i> Marcotte D, Rushe M, M Arduini R, Lukacs C, Atkins K, Sun X, Little K, Cullivan M, Paramasivam M, Patterson TA, Hesson T, D McKee T, May-Dracka TL, Xin Z, Bertolotti-Ciarlet A, Bhisetti GR, Lyssikatos JP, Silvian LF. </i> Protein Sci, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5J5T"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":380,"region_id":"DP02822r002","start":315,"term_id":"IDPO:0000045","statement":[{"text":"Phosphomapping of the isolated protein band (MS Bioworks) demonstrated that several sites were phosphorylated, namely: Thr38, Thr145, Thr164, Ser170, Thr227, Ser280, Thr327, Ser329, Thr332, and Tyr379. Because GLK is a Ser/Thr kinase, we reasoned that the Tyr379 phosphorylation must have been the result of another kinase acting on GLK as a substrate. The phosphorylation at Ser170 is likely due to autophosphorylation.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"chromatography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27727493","version":2,"reference_html":"Germinal-center kinase-like kinase co-crystal structure reveals a swapped activation loop and C-terminal extension. <i> Marcotte D, Rushe M, M Arduini R, Lukacs C, Atkins K, Sun X, Little K, Cullivan M, Paramasivam M, Patterson TA, Hesson T, D McKee T, May-Dracka TL, Xin Z, Bertolotti-Ciarlet A, Bhisetti GR, Lyssikatos JP, Silvian LF. </i> Protein Sci, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","cross_refs":[{"db":"PDB","id":"5J5T"}],"term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":380,"region_id":"DP02822r003","start":315,"term_id":"IDPO:0000033","statement":[{"text":"The disordered region is localized between the kinase domain and the CNH domain","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27727493","version":3,"reference_html":"Germinal-center kinase-like kinase co-crystal structure reveals a swapped activation loop and C-terminal extension. <i> Marcotte D, Rushe M, M Arduini R, Lukacs C, Atkins K, Sun X, Little K, Cullivan M, Paramasivam M, Patterson TA, Hesson T, D McKee T, May-Dracka TL, Xin Z, Bertolotti-Ciarlet A, Bhisetti GR, Lyssikatos JP, Silvian LF. </i> Protein Sci, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"5J5T"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02822","date":"2020-04-23T17:02:18.554Z","organism":"Homo sapiens","regions_counter":3,"name":"Mitogen-activated protein kinase kinase kinase kinase 3","dataset":[],"UniParc":"UPI00000747E6","uniref100":"UniRef100_Q8IVH8","uniref90":"UniRef90_Q8IVH8","uniref50":"UniRef50_Q8IVH8","genes":[{"name":{"value":"MAP4K3"},"synonyms":[{"value":"RAB8IPL1"}]}],"alphafold_very_low_content":0.2986577181208054,"disorder_content":0.0738255033557047,"disprot_consensus":{"full":[{"start":315,"end":380,"type":"D"}],"Structural state":[{"start":315,"end":380,"type":"D"}],"Disorder function":[{"start":315,"end":380,"type":"F"}]}},{"acc":"Q9UKY0","features":{"gene3D":[{"start":50,"end":154,"id":"G3DSA:1.10.790.10","name":"Prion/Doppel protein, beta-ribbon domain"}],"pfam":[{"id":"PF00377","name":"Prion/Doppel alpha-helical domain","start":63,"end":176},{"id":"PF11466","name":"Prion-like protein Doppel","start":1,"end":30}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MRKHLSWWWLATVCMLLFSHLSAVQTRGIKHRIKWNRKALPSTAQITEAQVAENRPGAFIKQGRKLDIDFGAEGNRYYEANYWQFPDGIHYNGCSEANVTKEAFVTGCINATQAANQGEFQKPDNKLHQQVLWRLVQELCSLKHCEFWLERGAGLRVTMHQPVLLCLLALIWLTVK","length":176,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":51,"region_id":"DP02823r001","start":24,"term_id":"IDPO:0000002","statement":[{"text":"The NMR structure of the recombinant human doppel protein, hDpl(24-152), contains a flexibly disordered \"tail\" comprising residues 24-51, and a globular domain extending from residues 52 to 149 for which a detailed structure was obtained.","type":"Abstract"},{"text":"The structure of hDpl(24–152) (Figure 1) contains a well defined globular domain and a flexibly disordered tail of residues 24–50, as is seen readily from the relative intensities of the 15N{1H}-NOEs (Supplementary Material, Figure S2a).","type":"Results"},{"text":"When compared to the remainder of the globular domain, there is a low propensity of medium-range and long-range NOE constraints in this region (Supplementary Material, Figure S2b), but the observation of positive 15N{1H}-NOEs for all amide moieties that were assigned in this region indicates that there is static disorder rather than increased intramolecular mobility.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12595265","version":2,"reference_html":"NMR structure of the human doppel protein. <i> Lührs T, Riek R, Güntert P, Wüthrich K. </i> J Mol Biol, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"1LG4"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02823","date":"2020-04-23T18:09:07.405Z","organism":"Homo sapiens","regions_counter":1,"name":"Prion-like protein doppel","dataset":[],"UniParc":"UPI000000DA73","uniref100":"UniRef100_Q9UKY0","uniref90":"UniRef90_Q9UKY0","uniref50":"UniRef50_Q9UKY0","genes":[{"name":{"value":"PRND"},"synonyms":[{"value":"DPL"}],"orfNames":[{"value":"UNQ1830/PRO3443"}]}],"alphafold_very_low_content":0.09659090909090909,"disorder_content":0.1590909090909091,"disprot_consensus":{"full":[{"start":24,"end":51,"type":"D"}],"Structural state":[{"start":24,"end":51,"type":"D"}]}},{"acc":"Q14019","features":{"gene3D":[{"start":1,"end":142,"id":"G3DSA:3.40.20.10","name":"Severin"}],"pfam":[{"id":"PF00241","name":"Cofilin/tropomyosin-type actin-binding protein","start":4,"end":130}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MATKIDKEACRAAYNLVRDDGSAVIWVTFKYDGSTIVPGEQGAEYQHFIQQCTDDVRLFAFVRFTTGDAMSKRSKFALITWIGENVSGLQRAKTGTDKTLVKEVVQNFAKEFVISDRKELEEDFIKSELKKAGGANYDAQTE","length":142,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":142,"region_id":"DP02824r001","start":132,"term_id":"IDPO:0000002","statement":[{"text":"The final model fits the electron density map very well with good geometry. The model includes 131 residues of CLP (of a total of 142 residues).","type":"Methods"},{"text":"N-terminal residues (3–0) are extended straight from β1 while C-terminal residues after Lys 131 cannot be defined by the electron density map.","type":"Results"},{"text":"The flexible C-terminal tail for CLP is 11 residues in length, while those for actophorin and yeast cofilin are 3 and 5, respectively.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15459340","version":2,"reference_html":"Crystal structure of human coactosin-like protein at 1.9 A resolution. <i> Li X, Liu X, Lou Z, Duan X, Wu H, Liu Y, Rao Z. </i> Protein Sci, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1VFQ"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":142,"region_id":"DP02824r002","start":132,"term_id":"GO:0060090","statement":[{"text":"LP also has a long flexible C terminus composed of 11 residues: AGGANYDAQTE. The first four residues form a hinge region, while the last seven make a good combination for molecular recognition. This flexible C terminus is sited not far from the region containing α1–β2, α4–β5 and β4–β5 loops. As a consequence, the flexible C terminus of CLP may be used to bind F-actin and/or other proteins.","type":"Results"},{"text":"Its long flexible C-terminal arm may help CLP binding other molecules.","type":"Figure"},{"text":"In the CLP–F-actin contact surface, besides the complementary morphology of the two polymers, their flexible C-terminal tails could assist the CLP polymer to bind to F-actin.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"15459340","version":3,"reference_html":"Crystal structure of human coactosin-like protein at 1.9 A resolution. <i> Li X, Liu X, Lou Z, Duan X, Wu H, Liu Y, Rao Z. </i> Protein Sci, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","cross_refs":[{"db":"PDB","id":"1VFQ"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0002-0341-4888","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02824","date":"2020-04-24T08:56:15.626Z","organism":"Homo sapiens","regions_counter":2,"name":"Coactosin-like protein","dataset":[],"UniParc":"UPI0000505468","uniref100":"UniRef100_Q14019","uniref90":"UniRef90_Q14019","uniref50":"UniRef50_Q14019","genes":[{"name":{"value":"COTL1"},"synonyms":[{"value":"CLP"}]}],"alphafold_very_low_content":0.056338028169014086,"disorder_content":0.07746478873239436,"disprot_consensus":{"full":[{"start":132,"end":142,"type":"D"}],"Structural state":[{"start":132,"end":142,"type":"D"}],"Molecular function":[{"start":132,"end":142,"type":"F"}]}},{"acc":"P31153","features":{"gene3D":[],"pfam":[{"id":"PF00438","name":"S-adenosylmethionine synthetase, N-terminal domain","start":18,"end":115},{"id":"PF02772","name":"S-adenosylmethionine synthetase, central domain","start":129,"end":250},{"id":"PF02773","name":"S-adenosylmethionine synthetase, C-terminal domain","start":252,"end":388}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MNGQLNGFHEAFIEEGTFLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVAKTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDSSKGFDYKTCNVLVALEQQSPDIAQGVHLDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPWLRPDSKTQVTVQYMQDRGAVLPIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRFVIGGPQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFHYGTSQKSERELLEIVKKNFDLRPGVIVRDLDLKKPIYQRTAAYGHFGRDSFPWEVPKKLKY","length":395,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":126,"region_id":"DP02825r001","start":116,"term_id":"IDPO:0000002","statement":[{"text":"The structure of (PPNP-bound) MATα2 has a disordered gating loop, providing direct evidence against the idea that it provides the energy for the opening of the gate.","type":"Results"},{"text":"The two ordered sites contain SAMe, PPNP, Mg2+, and K+, whereas the disordered sites contain only an ethylene glycol molecule as a result of the cryoprotection. The structure of (PPNP-bound) MATα2 has a disordered gating loop, and a comparison of the PPNP-bound, MAT(α2)4(βV2)2, and SAMe+ADO+MET+PPNP structures shows that the gate is open when active site is occupied by PPNP.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26858410","version":2,"reference_html":"Crystallography captures catalytic steps in human methionine adenosyltransferase enzymes. <i> Murray B, Antonyuk SV, Marina A, Lu SC, Mato JM, Hasnain SS, Rojas AL. </i> Proc Natl Acad Sci U S A, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5A19"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-01-07T16:54:46.417Z"}},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":126,"region_id":"DP02825r004","start":116,"term_id":"IDPO:0000011","statement":[{"text":"The structure of (PPNP-bound) MATα2 has a disordered gating loop, providing direct evidence against the idea that it provides the energy for the opening of the gate.","type":"Results"},{"text":"The two ordered sites contain SAMe, PPNP, Mg2+, and K+, whereas the disordered sites contain only an ethylene glycol molecule as a result of the cryoprotection. The structure of (PPNP-bound) MATα2 has a disordered gating loop, and a comparison of the PPNP-bound, MAT(α2)4(βV2)2, and SAMe+ADO+MET+PPNP structures shows that the gate is open when active site is occupied by PPNP.","type":"Results"},{"text":"It has been suggested that when the active site is occupied, the loop is closed like a gate, but when the active site is empty, the loop becomes invisible in the structure, presumably resulting from an open dynamic gate.","type":"Introduction"},{"text":"The active site gating loop gains order and closes upon substrate binding.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26858410","version":2,"reference_html":"Crystallography captures catalytic steps in human methionine adenosyltransferase enzymes. <i> Murray B, Antonyuk SV, Marina A, Lu SC, Mato JM, Hasnain SS, Rojas AL. </i> Proc Natl Acad Sci U S A, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"5A19"},{"db":"PDB","id":"5A1G"},{"db":"PDB","id":"5A1I"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-01-07T16:54:59.232Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":129,"region_id":"DP02825r005","start":117,"term_id":"IDPO:0000002","statement":[{"text":"The structure lacked  substrates  or  products;  therefore,  the  Mat2A  gating  loop (Mat2A residues 109–140), which closes upon substrate binding, was disordered and not observed.","type":"Results"},{"text":"Numbering is referred to chain A of the PDB","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"28553945","version":2,"reference_html":"Targeting S-adenosylmethionine biosynthesis with a novel allosteric inhibitor of Mat2A. <i> Quinlan CL, Kaiser SE, Bolaños B, Nowlin D, Grantner R, Karlicek-Bryant S, Feng JL, Jenkinson S, Freeman-Cook K, Dann SG, Wang X, Wells PA, Fantin VR, Stewart AE, Grant SK. </i> Nat Chem Biol, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5UGH"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-01-07T16:34:17.244Z"}}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02825","date":"2020-04-24T09:21:28.736Z","organism":"Homo sapiens","regions_counter":5,"name":"S-adenosylmethionine synthase isoform type-2","dataset":[],"UniParc":"UPI0000000C32","uniref100":"UniRef100_P31153","uniref90":"UniRef90_P31153","uniref50":"UniRef50_P31153","genes":[{"name":{"value":"MAT2A"},"synonyms":[{"value":"AMS2"},{"value":"MATA2"}]}],"alphafold_very_low_content":0.007594936708860759,"disorder_content":0.035443037974683546,"disprot_consensus":{"full":[{"start":116,"end":126,"type":"T"},{"start":127,"end":129,"type":"D"}],"Structural state":[{"start":116,"end":129,"type":"D"}],"Structural transition":[{"start":116,"end":126,"type":"T"}]}},{"acc":"P40344","features":{"gene3D":[],"pfam":[{"id":"PF03987","name":"Autophagocytosis associated protein, active-site domain","start":32,"end":305}]},"creator":"vsagris","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"sequence":"MIRSTLSSWREYLTPITHKSTFLTTGQITPEEFVQAGDYLCHMFPTWKWNEESSDISYRDFLPKNKQFLIIRKVPCDKRAEQCVEVEGPDVIMKGFAEDGDEDDVLEYIGSETEHVQSTPAGGTKDSSIDDIDELIQDMEIKEEDENDDTEEFNAKGGLAKDMAQERYYDLYIAYSTSYRVPKMYIVGFNSNGSPLSPEQMFEDISADYRTKTATIEKLPFYKNSVLSVSIHPCKHANVMKILLDKVRVVRQRRRKELQEEQELDGVGDWEDLQDDIDDSLRVDQYLIVFLKFITSVTPSIQHDYTMEGW","length":310,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":20,"region_id":"DP02826r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"The 20 amino-terminal and 4 carboxyl-terminal residues as well as three regions corresponding to residues 84–128, 143–162, and 271–278 lacked defined electron density and were omitted from the model.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17227760","version":2,"reference_html":"The crystal structure of Atg3, an autophagy-related ubiquitin carrier protein (E2) enzyme that mediates Atg8 lipidation. <i> Yamada Y, Suzuki NN, Hanada T, Ichimura Y, Kumeta H, Fujioka Y, Ohsumi Y, Inagaki F. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2DYT"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-14T13:38:43.723Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":128,"region_id":"DP02826r002","start":84,"term_id":"IDPO:0000002","statement":[{"text":"The 20 amino-terminal and 4 carboxyl-terminal residues as well as three regions corresponding to residues 84–128, 143–162, and 271–278 lacked defined electron density and were omitted from the model.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17227760","version":2,"reference_html":"The crystal structure of Atg3, an autophagy-related ubiquitin carrier protein (E2) enzyme that mediates Atg8 lipidation. <i> Yamada Y, Suzuki NN, Hanada T, Ichimura Y, Kumeta H, Fujioka Y, Ohsumi Y, Inagaki F. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2DYT"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-14T13:38:55.724Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":162,"region_id":"DP02826r003","start":143,"term_id":"IDPO:0000002","statement":[{"text":"The 20 amino-terminal and 4 carboxyl-terminal residues as well as three regions corresponding to residues 84–128, 143–162, and 271–278 lacked defined electron density and were omitted from the model.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17227760","version":2,"reference_html":"The crystal structure of Atg3, an autophagy-related ubiquitin carrier protein (E2) enzyme that mediates Atg8 lipidation. <i> Yamada Y, Suzuki NN, Hanada T, Ichimura Y, Kumeta H, Fujioka Y, Ohsumi Y, Inagaki F. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2DYT"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-14T13:39:13.149Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":162,"region_id":"DP02826r004","start":84,"term_id":"IDPO:0000002","statement":[{"text":"Because most residues of FR are disordered in the crystal, we could not obtain further structural information on FR from the crystal structure.To obtain structural information on FR in solution, we expressed the FR moiety of Atg3 (83–162) in E. coli, purified it,and analyzed it by NMR spectroscopy. Fig. 3A shows the 1H-15N HSQC spectrum of the FR moiety of Atg3.","type":"Results"},{"text":"Intriguingly, the spectrum of full-length Atg3 was strikingly similar to that of FR, suggesting that most observed signals for full-length Atg3 were derived from the FR moiety. This observation indicates that the mobility of FR is much higher than that of other regions of Atg3 because the residues located at the flexible regions give strong NMR signals because of long T2 relaxation times compared with those located at the rigid regions.","type":"Results"},{"text":"These results suggest that the FR moiety of Atg3 has a random coil structure and is highly mobile in solution, not only in the isolated state but also in intact Atg3. Although residues 129–142 of FR have a helical structure in the crystal (Fig. 1,A and B), they may have a more flexible conformation in solution.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17227760","version":2,"reference_html":"The crystal structure of Atg3, an autophagy-related ubiquitin carrier protein (E2) enzyme that mediates Atg8 lipidation. <i> Yamada Y, Suzuki NN, Hanada T, Ichimura Y, Kumeta H, Fujioka Y, Ohsumi Y, Inagaki F. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":162,"region_id":"DP02826r005","start":84,"term_id":"GO:0005515","statement":[{"text":"Furthermore,in vitro pull down assays showed that FR of Atg3 mediated the binding of Atg7.","type":"Discussion"}],"curator_id":"esalladini","released":"2022_03","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"17227760","version":4,"reference_html":"The crystal structure of Atg3, an autophagy-related ubiquitin carrier protein (E2) enzyme that mediates Atg8 lipidation. <i> Yamada Y, Suzuki NN, Hanada T, Ichimura Y, Kumeta H, Fujioka Y, Ohsumi Y, Inagaki F. </i> J Biol Chem, 2007","date":"2022-03-08T14:17:10.611Z","reference_source":"pmid","ec_id":"ECO:0006077","term_name":"protein binding","curator_orcid":"0000-0002-5152-5953","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P38862","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-05-26T10:28:00.486Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":142,"region_id":"DP02826r006","start":129,"term_id":"IDPO:0000003","statement":[{"text":"The conformation of residues 129–142, which are modeled as helix C, also seems to be flexible because the average B-factor of these residues is rather high (89.9 and 54.0 Å2 for helix C and all Atg3 residues, respectively). ","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17227760","version":2,"reference_html":"The crystal structure of Atg3, an autophagy-related ubiquitin carrier protein (E2) enzyme that mediates Atg8 lipidation. <i> Yamada Y, Suzuki NN, Hanada T, Ichimura Y, Kumeta H, Fujioka Y, Ohsumi Y, Inagaki F. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2DYT"}],"term_name":"molten globule","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":20,"region_id":"DP02826r008","start":1,"term_id":"IDPO:0000002","statement":[{"text":"Otherwise, several loops in Atg7, Atg3, and Atg10, and the BMOE crosslink not visible in the electron density were not modeled in the structures.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23142976","version":2,"reference_html":"Noncanonical E2 recruitment by the autophagy E1 revealed by Atg7-Atg3 and Atg7-Atg10 structures. <i> Kaiser SE, Mao K, Taherbhoy AM, Yu S, Olszewski JL, Duda DM, Kurinov I, Deng A, Fenn TD, Klionsky DJ, Schulman BA. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4GSL"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-17T13:51:16.695Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":128,"region_id":"DP02826r009","start":84,"term_id":"IDPO:0000002","statement":[{"text":"Otherwise, several loops in Atg7, Atg3, and Atg10, and the BMOE crosslink not visible in the electron density were not modeled in the structures.","type":"Methods"},{"text":"In both the free and Atg7-bound Atg3 structures, the majority of the FR is disordered, except for a small helical segment.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23142976","version":2,"reference_html":"Noncanonical E2 recruitment by the autophagy E1 revealed by Atg7-Atg3 and Atg7-Atg10 structures. <i> Kaiser SE, Mao K, Taherbhoy AM, Yu S, Olszewski JL, Duda DM, Kurinov I, Deng A, Fenn TD, Klionsky DJ, Schulman BA. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4GSL"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-17T13:53:21.395Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":162,"region_id":"DP02826r010","start":142,"term_id":"IDPO:0000002","statement":[{"text":"Otherwise, several loops in Atg7, Atg3, and Atg10, and the BMOE crosslink not visible in the electron density were not modeled in the structures.","type":"Methods"},{"text":"In both the free and Atg7-bound Atg3 structures, the majority of the FR is disordered, except for a small helical segment.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23142976","version":2,"reference_html":"Noncanonical E2 recruitment by the autophagy E1 revealed by Atg7-Atg3 and Atg7-Atg10 structures. <i> Kaiser SE, Mao K, Taherbhoy AM, Yu S, Olszewski JL, Duda DM, Kurinov I, Deng A, Fenn TD, Klionsky DJ, Schulman BA. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4GSL"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-17T13:53:17.897Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":280,"region_id":"DP02826r011","start":247,"term_id":"IDPO:0000002","statement":[{"text":"Otherwise, several loops in Atg7, Atg3, and Atg10, and the BMOE crosslink not visible in the electron density were not modeled in the structures.","type":"Methods"},{"text":"IDR inside the ‘handle region’ (HR) of Atg3.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23142976","version":2,"reference_html":"Noncanonical E2 recruitment by the autophagy E1 revealed by Atg7-Atg3 and Atg7-Atg10 structures. <i> Kaiser SE, Mao K, Taherbhoy AM, Yu S, Olszewski JL, Duda DM, Kurinov I, Deng A, Fenn TD, Klionsky DJ, Schulman BA. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4GSL"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-17T13:52:21.270Z"}},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P38182","partner_end":null}],"ec_ontology":"ECO","end":273,"region_id":"DP02826r012","start":270,"term_id":"GO:0005515","statement":[{"text":"Here, we show by NMR spectroscopy that Atg3 directly interacts with Atg8 through the WEDL sequence in HR and that the interaction is quite similar to Atg8-Atg19AIM and LC3-p62AIM interactions. Thus, the WEDL sequence of Atg3 is a canonical AIM.","type":"Introduction"},{"text":"The region includes the canonical LIR motif \"WEDL\".","type":"Curator statement"}],"curator_id":"vsagris","released":"2022_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Vasileios Sagris","reference_id":"20615880","version":4,"reference_html":"Autophagy-related protein 8 (Atg8) family interacting motif in Atg3 mediates the Atg3-Atg8 interaction and is crucial for the cytoplasm-to-vacuole targeting pathway. <i> Yamaguchi M, Noda NN, Nakatogawa H, Kumeta H, Ohsumi Y, Inagaki F. </i> J Biol Chem, 2010","date":"2022-06-22T15:35:23.059Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"protein binding","curator_orcid":"0000-0001-6587-8357","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-26T20:06:14.888Z"}},{"start":270,"end":273,"reference_id":"20615880","reference_source":"pmid","reference_html":"Autophagy-related protein 8 (Atg8) family interacting motif in Atg3 mediates the Atg3-Atg8 interaction and is crucial for the cytoplasm-to-vacuole targeting pathway. <i> Yamaguchi M, Noda NN, Nakatogawa H, Kumeta H, Ohsumi Y, Inagaki F. </i> J Biol Chem, 2010","date":"2022-06-22T15:36:14.792Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":1,"ec_go":"EXP","region_id":"DP02826r014","statement":[{"text":"Here, we show by NMR spectroscopy that Atg3 directly interacts with Atg8 through the WEDL sequence in HR and that the interaction is quite similar to Atg8-Atg19AIM and LC3-p62AIM interactions. Thus, the WEDL sequence of Atg3 is a canonical AIM.","type":"Introduction"},{"text":"The region includes the canonical LIR motif \"WEDL\".","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-26T20:06:15.852Z"}},{"start":82,"end":165,"reference_id":"24879155","reference_source":"pmid","reference_html":"Identification of Atg3 as an intrinsically disordered polypeptide yields insights into the molecular dynamics of autophagy-related proteins in yeast. <i> Popelka H, Uversky VN, Klionsky DJ. </i> Autophagy, 2014","date":"2022-06-10T19:53:49.942Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP02826r015","statement":[{"text":"As expected, the log(Rh) vs. log(Mw) dependency for Atg3FR was significantly displaced from the linear dependency log(Rh) vs. log(Mw) of standard globular proteins, and its experimental hydrodynamic radius exceeds the calculated hydrodynamic radius of both a native-coil-like IDP and a GdmCl-unfolded globular protein with comparable molecular mass (Table 1). This suggests that Atg3FR adopts a conformation even more disordered than that of the full-length Atg3.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-13T09:09:58.820Z"}},{"start":82,"end":165,"reference_id":"24879155","reference_source":"pmid","reference_html":"Identification of Atg3 as an intrinsically disordered polypeptide yields insights into the molecular dynamics of autophagy-related proteins in yeast. <i> Popelka H, Uversky VN, Klionsky DJ. </i> Autophagy, 2014","date":"2022-06-10T19:56:53.533Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006200","ec_ontology":"ECO","ec_name":"circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP02826r016","statement":[{"text":" In comparison, the far-UV CD spectrum of Atg3FR (Fig. 3B) did resemble the spectrum of unordered structures with a negative minimum at approximately 200 nm,38,39 indicating that the secondary structure is missing in Atg3FR.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-13T09:10:03.802Z"}},{"start":82,"end":165,"reference_id":"24879155","reference_source":"pmid","reference_html":"Identification of Atg3 as an intrinsically disordered polypeptide yields insights into the molecular dynamics of autophagy-related proteins in yeast. <i> Popelka H, Uversky VN, Klionsky DJ. </i> Autophagy, 2014","date":"2022-06-10T19:57:44.918Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP02826r017","statement":[{"text":"Atg3FR, which behaved as an extended random-coil-like protein (Fig. 2; Fig. 3), has a predicted molecular mass of 10 kDa, but migrated at the position of a polypeptide twice as large (Fig. 4A; Table 2).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-13T09:10:08.818Z"}}],"released":"2021_06","ncbi_taxon_id":559292,"disprot_id":"DP02826","date":"2020-04-24T10:57:25.089Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":17,"name":"Autophagy-related protein 3","dataset":["Autophagy-related proteins"],"UniParc":"UPI0000052F5F","uniref100":"UniRef100_A6ZS81","uniref90":"UniRef90_A6ZS81","uniref50":"UniRef50_W0TEF9","genes":[{"name":{"value":"ATG3"},"synonyms":[{"value":"APG3"},{"value":"AUT1"}],"orfNames":[{"value":"N2040"}],"olnNames":[{"value":"YNR007C"}]}],"alphafold_very_low_content":0.25806451612903225,"disorder_content":0.44516129032258067,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"D"},{"start":82,"end":165,"type":"D"},{"start":247,"end":280,"type":"D"}],"Structural state":[{"start":1,"end":20,"type":"D"},{"start":82,"end":165,"type":"D"},{"start":247,"end":280,"type":"D"}],"Molecular function":[{"start":84,"end":162,"type":"F"},{"start":270,"end":273,"type":"F"}],"Biological process":[{"start":270,"end":273,"type":"F"}]}},{"acc":"P22523","sequence":"MIERGKFRSLTLINWNGFFARTFDLDELVTTLSGGNGAGKSTTMAAFVTALIPDLTLLHFRNTTEAGATSGSRDKGLHGKLKAGVCYSMLDTINSRHQRVVVGVRLQQVAGRDRKVDIKPFAIQGLPMSVQPTQLVTETLNERQARVLPLNELKDKLEAMEGVQFKQFNSITDYHSLMFDLGIIARRLRSASDRSKFYRLIEASLYGGISSAITRSLRDYLLPENSGVRKAFQDMEAALRENRMTLEAIRVTQSDRDLFKHLISEATNYVAADYMRHANERRVHLDKALEFRRELHTSRQQLAAEQYKHVDMARELAEHNGAEGDLEADYQAASDHLNLVQTALRQQEKIERYEADLDELQIRLEEQNEVVAEAIERQQENEARAEAAELEVDELKSQLADYQQALDVQQTRAIQYNQAIAALNRAKELCHLPDLTADCAAEWLETFQAKELEATEKMLSLEQKMSMAQTAHSQFEQAYQLVVAINGPLARNEAWDVARELLREGVDQRHLAEQVQPLRMRLSELEQRLREQQEAERLLADFCKRQGKNFDIDELEALHQELEARIASLSDSVSNAREERMALRQEQEQLQSRIQSLMQRAPVWLAAQNSLNQLSEQCGEEFTSSQDVTEYLQQLLEREREAIVERDEVGARKNAVDEEIERLSQPGGSEDQRLNALAERFGGVLLSEIYDDVSLEDAPYFSALYGPSRHAIVVPDLSQVTEHLEGLTDCPEDLYLIEGDPQSFDDSVFSVDELEKAVVVKIADRQWRYSRFPEVPLFGRAARESRIESLHAEREVLSERFATLSFDVQKTQRLHQAFSRFIGSHLAVAFESDPEAEIRQLNSRRVELERALSNHENDNQQQRIQFEQAKEGVTALNRILPRLNLLADDSLADRVDEIRERLDEAQEAARFVQQFGNQLAKLEPIVSVLQSDPEQFEQLKEDYAYSQQMQRDARQQAFALTEVVQRRAHFSYSDSAEMLSGNSDLNEKLRERLEQAEAERTRAREALRGHAAQLSQYNQVLASLKSSYDTKKELLNDLQRELQDIGVRADSGAEERARIRRDELHAQLSNNRSRRNQLEKALTFCEAEMDNLTRKLRKLERDYFEMREQVVTAKAGWCAVMRMVKDNGVERRLHRRELAYLSADDLRSMSDKALGALRLAVADNEHLRDVLRMSEDPKRPERKIQFFVAVYQHLRERIRQDIIRTDDPVEAIEQMEIELSRLTEELTSREQKLAISSRSVANIIRKTIQREQNRIRMLNQGLQNVSFGQVNSVRLNVNVRETHAMLLDVLSEQHEQHQDLFNSNRLTFSEALAKLYQRLNPQIDMGQRTPQTIGEELLDYRNYLEMEVEVNRGSDGWLRAESGALSTGEAIGTGMSILVMVVQSWEDESRRLRGKDISPCRLLFLDEAARLDARSIATLFELCERLQMQLIIAAPENISPEKGTTYKLVRKVFQNTEHVHVVGLRGFAPQLPETLPGTDEAPSQAS","alphafold_very_low_content":"0.026244952893674293","creator":"fquaglia","dataset":[],"date":"2020-04-24T14:42:41.968Z","disprot_id":"DP02827","features":{"gene3D":[{"start":667,"end":778,"id":"G3DSA:1.20.1060.30","name":"G3DSA:1.20.1060.30","_id":"685af523b4ac24d5329d95b7"}],"pfam":[{"id":"PF04310","name":"MukB N-terminal","start":2,"end":227},{"id":"PF13558","name":"SbcC/RAD50-like, Walker B motif","start":1336,"end":1424},{"id":"PF16330","name":"MukB hinge domain","start":645,"end":810},{"id":"PF30340","name":"Chromosome partition protein MukB, C-terminal domain","start":1116,"end":1229}]},"genes":[{"name":{"value":"mukB","evidences":[],"_id":"685af523b4ac24d5329d95c3"},"synonyms":[],"olnNames":[{"value":"b0924","evidences":[],"_id":"685af523b4ac24d5329d95c4"},{"value":"JW0907","evidences":[],"_id":"685af523b4ac24d5329d95c5"}],"orfNames":[],"_id":"685af523b4ac24d5329d95c2"}],"length":1486,"name":"Chromosome partition protein MukB","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions_counter":2,"released":"2023_12","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"UniParc":"UPI000016F30F","uniref100":"UniRef100_C4ZQ50","uniref50":"UniRef50_Q935S7","uniref90":"UniRef90_B5QZC8","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1QHL","_id":"685af523b4ac24d5329d95bc"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":59,"end":76,"interaction_partner":[],"reference_html":"Crystal structure of the N-terminal domain of MukB: a protein involved in chromosome partitioning. <i> van den Ent F, Lockhart A, Kendrick-Jones J, Löwe J. </i> Structure, 1999","reference_id":"10545328","region_id":"DP02827r001","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"The second helix H2 is connected to strand S3 by a long, mostly flexible loop. Residues 59 to 76 are disordered in the crystal.","_id":"685af523b4ac24d5329d95bb"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-10-06T15:09:12.016Z","_id":"685af523b4ac24d5329d95bd"},"version":2,"_id":"685af523b4ac24d5329d95ba","reference_source":"pmid"}],"__v":0,"disorder_content":0.012113055181695828,"disprot_consensus":{"full":[{"start":59,"end":76,"type":"D"}],"Structural state":[{"start":59,"end":76,"type":"D"}]}},{"acc":"Q9W058","features":{"gene3D":[],"pfam":[{"id":"PF01144","name":"Coenzyme A transferase","start":37,"end":265},{"id":"PF01144","name":"Coenzyme A transferase","start":299,"end":496}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"sequence":"MLCRLVGNRSLGARYTASIKAIACYSTSGKQRNGKIYESAIDAVADVQDGAQILFGGFGICGIPEKMINALKQKGVKNITGVSNNGGVDDTGLGVLIKQKQVSKVIGSYVGENTELVRQYLEGELAVELTPQGTLAEKIRAGGAGIPAFYTPTGYATLVQEGGAPIKYSKDGKVEISSEKKPVKEFNGKNYVMEESIFADFAFVKAQKADPLGNLVFNKAARNFNAPMCRAAKITVAEVEEIVPIGALSPDEIHVPGIYINRIFKGTNYNKRVERLRITEPKDPSKPAPPPNPAQVLRERIARRVALEFHDGMYANLGIGIPVLSSNYIPKGMNVMLQSENGILGLGPFPTKDKVDPDLINAGKESVTVVPGASYFGSDDSFAMIRGGHVDITILGAMEVSATGDLANWMIPGKLVKGMGGAMDLVAAPGTKVIITMEHNARDGSPKILDTCSLPLTGKGVIDMIISEKAVFTVEKGVGLTLIEVAEGYTVDDIIASTGAKFTVSPNLKKMGQIPV","length":516,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":291,"region_id":"DP02828r001","start":281,"term_id":"IDPO:0000002","statement":[{"text":"Residues 250–­257 in the hydrophilic linker, which is absent in the bacterial homologues, are invisible in the electron-density maps. The region consisting of residues 373–383 is also disordered in the DmSCOT structure.","type":"Results"},{"text":"Residue numbering reported by the authors of the publication refers to the PDB structure. The interdomain flexible linker corresponds to region 281-291.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24100554","version":2,"reference_html":"Structure of succinyl-CoA:3-ketoacid CoA transferase from Drosophila melanogaster. <i> Zhang M, Xu HY, Wang YC, Shi ZB, Zhang NN. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4KGB"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":291,"region_id":"DP02828r002","start":281,"term_id":"IDPO:0000033","statement":[{"text":"Residues 250–­257 in the hydrophilic linker, which is absent in the bacterial homologues, are invisible in the electron-density maps. The region consisting of residues 373–383 is also disordered in the DmSCOT structure.","type":"Results"},{"text":"Residue numbering reported by the authors of the publication refers to the PDB structure. The interdomain flexible linker corresponds to region 281-291.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24100554","version":3,"reference_html":"Structure of succinyl-CoA:3-ketoacid CoA transferase from Drosophila melanogaster. <i> Zhang M, Xu HY, Wang YC, Shi ZB, Zhang NN. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":7227,"disprot_id":"DP02828","date":"2020-04-24T18:30:08.828Z","organism":"Drosophila melanogaster","regions_counter":2,"name":"Succinyl-CoA:3-ketoacid-coenzyme A transferase, mitochondrial","dataset":[],"UniParc":"UPI000007C5E1","uniref100":"UniRef100_Q9W058","uniref90":"UniRef90_Q9W058","uniref50":"UniRef50_Q9W058","genes":[{"name":{"value":"SCOT","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"24100554","url":"http://www.ncbi.nlm.nih.gov/pubmed/24100554","alternativeUrl":"https://europepmc.org/abstract/MED/24100554"}}]},"orfNames":[{"value":"CG1140","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0035298","url":"http://flybase.org/reports/FBgn0035298.html"}}]}]}],"alphafold_very_low_content":0.03875968992248062,"disorder_content":0.02131782945736434,"disprot_consensus":{"full":[{"start":281,"end":291,"type":"D"}],"Structural state":[{"start":281,"end":291,"type":"D"}],"Disorder function":[{"start":281,"end":291,"type":"F"}]}},{"acc":"P46379","features":{"gene3D":[],"pfam":[{"id":"PF00240","name":"Ubiquitin family","start":19,"end":87},{"id":"PF12057","name":"BCL2-associated athanogene 6","start":277,"end":391},{"id":"PF20960","name":"Bag6, BAG-similar domain","start":1059,"end":1111}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MEPNDSTSTAVEEPDSLEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNVGGKVIHLVERAPPQTHLPSGASSGTGSASATHGGGSPPGTRGPGASVHDRNANSYVMVGTFNLPSDGSAVDVHINMEQAPIQSEPRVRLVMAQHMIRDIQTLLSRMETLPYLQCRGGPQPQHSQPPPQPPAVTPEPVALSSQTSEPVESEAPPREPMEAEEVEERAPAQNPELTPGPAPAGPTPAPETNAPNHPSPAEYVEVLQELQRLESRLQPFLQRYYEVLGAAATTDYNNNHEGREEDQRLINLVGESLRLLGNTFVALSDLRCNLACTPPRHLHVVRPMSHYTTPMVLQQAAIPIQINVGTTVTMTGNGTRPPPTPNAEAPPPGPGQASSVAPSSTNVESSAEGAPPPGPAPPPATSHPRVIRISHQSVEPVVMMHMNIQDSGTQPGGVPSAPTGPLGPPGHGQTLGQQVPGFPTAPTRVVIARPTPPQARPSHPGGPPVSGTLQGAGLGTNASLAQMVSGLVGQLLMQPVLVAQGTPGMAPPPAPATASASAGTTNTATTAGPAPGGPAQPPPTPQPSMADLQFSQLLGNLLGPAGPGAGGSGVASPTITVAMPGVPAFLQGMTDFLQATQTAPPPPPPPPPPPPAPEQQTMPPPGSPSGGAGSPGGLGLESLSPEFFTSVVQGVLSSLLGSLGARAGSSESIAAFIQRLSGSSNIFEPGADGALGFFGALLSLLCQNFSMVDVVMLLHGHFQPLQRLQPQLRSFFHQHYLGGQEPTPSNIRMATHTLITGLEEYVRESFSLVQVQPGVDIIRTNLEFLQEQFNSIAAHVLHCTDSGFGARLLELCNQGLFECLALNLHCLGGQQMELAAVINGRIRRMSRGVNPSLVSWLTTMMGLRLQVVLEHMPVGPDAILRYVRRVGDPPQPLPEEPMEVQGAERASPEPQRENASPAPGTTAEEAMSRGPPPAPEGGSRDEQDGASAETEPWAAAVPPEWVPIIQQDIQSQRKVKPQPPLSDAYLSGMPAKRRKTMQGEGPQLLLSEAVSRAAKAAGARPLTSPESLSRDLEAPEVQESYRQQLRSDIQKRLQEDPNYSPQRFPNAQRAFADDP","length":1132,"regions":[{"term_namespace":"Structural transition","ec_ontology":"ECO","end":1112,"region_id":"DP02829r001","start":1057,"term_id":"IDPO:0000011","unpublished":true,"statement":[{"text":"The x-ray crystal structure of the complex was determined at 1.85 Å resolution. Unambiguous electron density allowed modeling of residues 1058–1112 of BAG6 BAGS and 94–143 of Ubl4a TUGS.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"25713138","version":2,"reference_html":"Structure of a BAG6 (Bcl-2-associated athanogene 6)-Ubl4a (ubiquitin-like protein 4a) complex reveals a novel binding interface that functions in tail-anchored protein biogenesis. <i> Kuwabara N, Minami R, Yokota N, Matsumoto H, Senda T, Kawahara H, Kato R. </i> J Biol Chem, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4X86"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP02829r002","unpublished":true,"ec_ontology":"ECO","end":1123,"term_id":"GO:0005515","start":1048,"version":3,"statement":[{"text":"The x-ray crystal structure of the complex was determined at 1.85 Å resolution. Unambiguous electron density allowed modeling of residues 1058–1112 of BAG6 BAGS and 94–143 of Ubl4a TUGS.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P11441","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2023_12","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"25713138","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4X86"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"fquaglia","reference_html":"Structure of a BAG6 (Bcl-2-associated athanogene 6)-Ubl4a (ubiquitin-like protein 4a) complex reveals a novel binding interface that functions in tail-anchored protein biogenesis. <i> Kuwabara N, Minami R, Yokota N, Matsumoto H, Senda T, Kawahara H, Kato R. </i> J Biol Chem, 2015","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1123,"region_id":"DP02829r003","start":1048,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"On the other hand, the profile of BAG6 BAGS exhibited a large negative value at 200 nm but a small negative value at 222 nm, suggesting that it is almost unstructured; the α-helical content was estimated as 14% from the value at 222 nm.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"25713138","version":2,"reference_html":"Structure of a BAG6 (Bcl-2-associated athanogene 6)-Ubl4a (ubiquitin-like protein 4a) complex reveals a novel binding interface that functions in tail-anchored protein biogenesis. <i> Kuwabara N, Minami R, Yokota N, Matsumoto H, Senda T, Kawahara H, Kato R. </i> J Biol Chem, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":1123,"region_id":"DP02829r004","start":1048,"term_id":"IDPO:0000011","unpublished":true,"statement":[{"text":"When BAG6 BAGS and Ubl4a were mixed, the profile revealed a typical α-helical structure whose intensity was greater than that of Ubl4a or BAG6 BAGS alone; the α-helical content was estimated to be 38% from the value at 222 nm. The secondary structure content was calculated using the K2D3 software (31). The α-helix and β-sheet contents were estimated to be 26 and 18% (Ubl4a), 19 and 16% (BAG6 BAGS), and 43 and 10% (BAG6 BAGS + Ubl4a), respectively. Thus, α-helical content increased upon complex formation. The change in β-sheet content was smaller than the change in α-helical content, and β-sheet contents were less than 20% in all cases. Thus, we suspect that the BAG6 BAGS fragment is disordered and/or non-helical in its monomeric form but forms helical structures upon Ubl4a binding.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"25713138","version":2,"reference_html":"Structure of a BAG6 (Bcl-2-associated athanogene 6)-Ubl4a (ubiquitin-like protein 4a) complex reveals a novel binding interface that functions in tail-anchored protein biogenesis. <i> Kuwabara N, Minami R, Yokota N, Matsumoto H, Senda T, Kawahara H, Kato R. </i> J Biol Chem, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P11441","partner_end":null}],"ec_ontology":"ECO","end":1123,"region_id":"DP02829r005","start":1048,"term_id":"GO:0005515","unpublished":true,"statement":[{"text":"We used SAXS to show that the BAG6 BAGS-Ubl4a TUGS complex exists as a heterodimer in solution.","type":"Discussion"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"small-angle X-ray scattering evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"25713138","version":3,"reference_html":"Structure of a BAG6 (Bcl-2-associated athanogene 6)-Ubl4a (ubiquitin-like protein 4a) complex reveals a novel binding interface that functions in tail-anchored protein biogenesis. <i> Kuwabara N, Minami R, Yokota N, Matsumoto H, Senda T, Kawahara H, Kato R. </i> J Biol Chem, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","term_name":"protein binding","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1123,"region_id":"DP02829r006","start":1048,"term_id":"GO:0140677","unpublished":true,"statement":[{"text":"Furthermore, the tight association of BAG6 and Ubl4a resulted in modulation of Ubl4a protein stability in cells. ","type":"Abstract"},{"text":"The structure of Ubl4a, which interacts with BAG6, is similar to the yeast homologue Get5, which forms a homodimer. These observations indicate that the BAGS domain of BAG6 promotes the TA protein biogenesis pathway in mammals by the interaction with Ubl4a.","type":"Abstract"},{"text":"BAG6 association stabilizes the Ubl4a protein. A, Ubl4a protein is destabilized by loss of its C-terminal BAG6 binding region. ","type":"Figure"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"qualitative western immunoblotting evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"25713138","version":3,"reference_html":"Structure of a BAG6 (Bcl-2-associated athanogene 6)-Ubl4a (ubiquitin-like protein 4a) complex reveals a novel binding interface that functions in tail-anchored protein biogenesis. <i> Kuwabara N, Minami R, Yokota N, Matsumoto H, Senda T, Kawahara H, Kato R. </i> J Biol Chem, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000279","term_name":"molecular function activator activity","curator_orcid":"0000-0002-0341-4888","ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1123,"region_id":"DP02829r007","start":1048,"term_id":"GO:0060090","unpublished":true,"statement":[{"text":"In this study, we obtained evidence that the C terminus of BAG6 (previously designated as a BAG domain) is essential for tethering the C-terminal conserved stretch of Ubl4a, designated here as the TUGS (tethering Ubl4a to BAGS) domain. ","type":"Introduction"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"25713138","version":3,"reference_html":"Structure of a BAG6 (Bcl-2-associated athanogene 6)-Ubl4a (ubiquitin-like protein 4a) complex reveals a novel binding interface that functions in tail-anchored protein biogenesis. <i> Kuwabara N, Minami R, Yokota N, Matsumoto H, Senda T, Kawahara H, Kato R. </i> J Biol Chem, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","term_name":"molecular adaptor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P11441","partner_end":null}],"ec_ontology":"ECO","end":1123,"region_id":"DP02829r008","start":1048,"term_id":"GO:0005515","unpublished":true,"statement":[{"text":"Using the bacterially expressed BAGS domain of BAG6 (residues 1048–1123) and the C-terminal region of Ubl4a (residues 95–147), we characterized the BAG6-Ubl4a interaction. To measure the affinity between BAG6 BAGS and Ubl4a TUGS, we carried out SPR experiments (Fig. 3A). Surprisingly, the calculated overall dissociation constant was very small, 2.2 ± 0.5 nm, suggesting that these two proteins form a very tight complex.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"surface plasmon resonance evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"25713138","version":3,"reference_html":"Structure of a BAG6 (Bcl-2-associated athanogene 6)-Ubl4a (ubiquitin-like protein 4a) complex reveals a novel binding interface that functions in tail-anchored protein biogenesis. <i> Kuwabara N, Minami R, Yokota N, Matsumoto H, Senda T, Kawahara H, Kato R. </i> J Biol Chem, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001269","term_name":"protein binding","curator_orcid":"0000-0002-0341-4888","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":395,"end":1029,"reference_id":"34523930","reference_source":"pmid","reference_html":"Regulation of Fibroblast Activation Protein-α Expression: Focus on Intracellular Protein Interactions. <i> Juillerat-Jeanneret L, Tafelmeyer P, Golshayan D. </i> J Med Chem, 2021","date":"2022-11-16T19:46:45.587Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02829r009","statement":[{"text":"The protein structure of BAG6/BAT3 can be subdivided in three parts: a N-terminal region (aa1–aa474) comprising an ubiquitin-like domain (UBL, aa13–aa87), a central domain comprising a long disordered Pro-rich domain (aa395–aa1029) bearing short polyPro and polyGly sequences which may be involved in inter- and intramolecular protein–protein interactions, a zinc-finger domain (aa851–aa884) and a C-terminal region (aa1030–aa1132), comprising the nuclear localization sequence (NLS, aa1030–aa1055), and the BAG domain (aa1000–aa1111).","type":"Introduction"}]}],"released":"2023_12","ncbi_taxon_id":9606,"disprot_id":"DP02829","date":"2020-04-27T08:49:10.782Z","organism":"Homo sapiens","regions_counter":9,"name":"Large proline-rich protein BAG6","dataset":[],"UniParc":"UPI00001267A0","uniref100":"UniRef100_P46379","uniref90":"UniRef90_P46379","uniref50":"UniRef50_P46379","genes":[{"name":{"value":"BAG6","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:13919","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:13919"}}]},"synonyms":[{"value":"BAT3","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"2156268","url":"http://www.ncbi.nlm.nih.gov/pubmed/2156268","alternativeUrl":"https://europepmc.org/abstract/MED/2156268"}}]},{"value":"G3"}]}],"alphafold_very_low_content":0.519434628975265,"disorder_content":0.6280918727915195,"disprot_consensus":{"full":[{"start":395,"end":1029,"type":"D"},{"start":1048,"end":1123,"type":"T"}],"Structural state":[{"start":395,"end":1029,"type":"D"},{"start":1048,"end":1123,"type":"D"}],"Structural transition":[{"start":1048,"end":1123,"type":"T"}],"Molecular function":[{"start":1048,"end":1123,"type":"F"}]}},{"acc":"Q91YD9","features":{"gene3D":[{"start":5,"end":147,"id":"G3DSA:2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":428,"end":489,"id":"G3DSA:3.90.810.10","name":"CRIB domain"},{"start":428,"end":489,"id":"G3DSA:3.90.810.10","name":"CRIB domain"}],"pfam":[{"id":"PF00568","name":"WH1 domain","start":28,"end":133},{"id":"PF00786","name":"P21-Rho-binding domain","start":199,"end":257},{"id":"PF02205","name":"WH2 motif","start":398,"end":423},{"id":"PF02205","name":"WH2 motif","start":427,"end":446}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MSSGQQPPRRVTNVGSLLLTPQENESLFSFLGKKCVTMSSAVVQLYAADRNCMWAKKCSGVACLVKDNPQRSYFLRIFDIKDGKLLWEQELYNNFVYNSPRGYFHTFAGDTCQVALNFANEEEAKKFRKAVTDLLGRRQRKSEKRRDAPNGPNLPMATVDIKNPEITTNRFYGSQVNNISHTKEKKKGKAKKKRLTKADIGTPSNFQHIGHVGWDPNTGFDLNNLDPELKNLFDMCGISEAQLKDRETSKVIYDFIEKTGGVEAVKNELRRQAPPPPPPSRGGPPPPPPPPHSSGPPPPPARGRGAPPPPPSRAPTAAPPPPPPSRPGVVVPPPPPNRMYPPPPPALPSSAPSGPPPPPPPSMAGSTAPPPPPPPPPPPGPPPPPGLPSDGDHQVPAPSGNKAALLDQIREGAQLKKVEQNSRPVSCSGRDALLDQIRQGIQLKSVSDGQESTPPTPAPTSGIVGALMEVMQKRSKAIHSSDEDEDDDDEEDFEDDDEWED","length":501,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":428,"region_id":"DP02830r001","start":419,"term_id":"IDPO:0000002","statement":[{"text":"The limitations, however, are that individual atomic positions cannot be refined and the inter-W linkers cannot be visualized.","type":"Results"},{"text":"Flexible linker connecting WH2 1 domain and WH2 2 domain.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20804767","version":2,"reference_html":"Structure of a longitudinal actin dimer assembled by tandem w domains: implications for actin filament nucleation. <i> Rebowski G, Namgoong S, Boczkowska M, Leavis PC, Navaza J, Dominguez R. </i> J Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3M3N"}],"term_name":"disorder","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:42:31.902Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":428,"region_id":"DP02830r002","start":419,"term_id":"IDPO:0000033","statement":[{"text":"The limitations, however, are that individual atomic positions cannot be refined and the inter-W linkers cannot be visualized.","type":"Results"},{"text":"Flexible linker connecting WH2 1 domain and WH2 2 domain.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20804767","version":3,"reference_html":"Structure of a longitudinal actin dimer assembled by tandem w domains: implications for actin filament nucleation. <i> Rebowski G, Namgoong S, Boczkowska M, Leavis PC, Navaza J, Dominguez R. </i> J Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"3M3N"}],"term_name":"flexible linker","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:42:32.761Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2020_12","ncbi_taxon_id":10090,"disprot_id":"DP02830","date":"2020-04-27T09:25:32.363Z","organism":"Mus musculus","regions_counter":2,"name":"Neural Wiskott-Aldrich syndrome protein","dataset":[],"UniParc":"UPI000002967C","uniref100":"UniRef100_Q91YD9","uniref90":"UniRef90_O08816","uniref50":"UniRef50_O00401","genes":[{"name":{"value":"Wasl"}}],"alphafold_very_low_content":0.21756487025948104,"disorder_content":0.01996007984031936,"disprot_consensus":{"full":[{"start":419,"end":428,"type":"D"}],"Structural state":[{"start":419,"end":428,"type":"D"}],"Disorder function":[{"start":419,"end":428,"type":"F"}]}},{"acc":"Q13164","features":{"gene3D":[],"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":55,"end":347}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MAEPLKEEDGEDGSAEPPGPVKAEPAHTAASVAAKNLALLKARSFDVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYGEFKSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDCAPPFDFAFDREALTRERIKEAIVAEIEDFHARREGIRQQIRFQPSLQPVASEPGCPDVEMPSPWAPSGDCAMESPPPAPPPCPGPAPDTIDLTLQPPPPVSEPAPPKKDGAISDNTKAALKAALLKSLRSRLRDGPSAPLEAPEPRKPVTAQERQREREEKRRRRQERAKEREKRRQERERKERGAGASGGPSTDPLAGLVLSDNDRSLLERWTRMARPAAPALTSVPAPAPAPTPTPTPVQPTSPPPGPVAQPTGPQPQSAGSTSGPVPQPACPPPGPAPHPTGPPGPIPVPAPPQIATSTSLLAAQSLVPPPGLPGSSTPGVLPYFPPGLPPPDAGGAPQSSMSESPDVNLVTQQLSKSQVEDPLPPVFSGTPKGSGAGYGVGFDLEEFLNQSFDMGVADGPQDGQADSASLSASLLADWLEGHGMNPADIESLQREIQMDSPMLLADLPDLQDP","length":816,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":46,"region_id":"DP02831r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"ERK5 residues 47–393 were resolved in the electron density with the exception of the activation loop residues 208–214, which were disordered (Figure ​1), and residues 288–292, which form a short loop in the CMGC-specific insert. In o","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23656407","version":2,"reference_html":"X-ray crystal structure of ERK5 (MAPK7) in complex with a specific inhibitor. <i> Elkins JM, Wang J, Deng X, Pattison MJ, Arthur JS, Erazo T, Gomez N, Lizcano JM, Gray NS, Knapp S. </i> J Med Chem, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4B99"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Biological process","ec_ontology":"ECO","end":46,"region_id":"DP02831r002","start":1,"term_id":"GO:0051179","statement":[{"text":"ERK5 residues 47–393 were resolved in the electron density with the exception of the activation loop residues 208–214, which were disordered (Figure ​1), and residues 288–292, which form a short loop in the CMGC-specific insert. In o","type":"Results"},{"text":"The region N-terminal to the kinase domain contains sequences for targeting to the cytoplasm, while in the C-terminal region there is a nuclear localization sequence (residues 505–539). ERK5 is found in both cytoplasmic and nuclear locations.","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"23656407","version":3,"reference_html":"X-ray crystal structure of ERK5 (MAPK7) in complex with a specific inhibitor. <i> Elkins JM, Wang J, Deng X, Pattison MJ, Arthur JS, Erazo T, Gomez N, Lizcano JM, Gray NS, Knapp S. </i> J Med Chem, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","cross_refs":[{"db":"PDB","id":"4B99"}],"term_name":"localization","curator_orcid":"0000-0002-0341-4888","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2020_12","ncbi_taxon_id":9606,"disprot_id":"DP02831","date":"2020-04-27T09:39:19.253Z","organism":"Homo sapiens","regions_counter":2,"name":"Mitogen-activated protein kinase 7","dataset":[],"UniParc":"UPI000012F179","uniref100":"UniRef100_Q13164","uniref90":"UniRef90_Q13164","uniref50":"UniRef50_Q13164","genes":[{"name":{"value":"MAPK7"},"synonyms":[{"value":"BMK1"},{"value":"ERK5"},{"value":"PRKM7"}]}],"alphafold_very_low_content":0.4227941176470588,"disorder_content":0.056372549019607844,"disprot_consensus":{"full":[{"start":1,"end":46,"type":"D"}],"Structural state":[{"start":1,"end":46,"type":"D"}],"Biological process":[{"start":1,"end":46,"type":"F"}]}},{"acc":"Q7L2J0","features":{"gene3D":[],"pfam":[{"id":"PF06859","name":"Bicoid-interacting protein 3 (Bin3)","start":575,"end":683}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MIEMAAEKEPFLVPAPPPPLKDESGGGGGPTVPPHQEAASGELRGGTERGPGRCAPSAGSPAAAVGRESPGAAATSSSGPQAQQHRGGGPQAQSHGEARLSDPPGRAAPPDVGEERRGGGGTELGPPAPPRPRNGYQPHRPPGGGGGKRRNSCNVGGGGGGFKHPAFKRRRRVNSDCDSVLPSNFLLGGNIFDPLNLNSLLDEEVSRTLNAETPKSSPLPAKGRDPVEILIPKDITDPLSLNTCTDEGHVVLASPLKTGRKRHRHRGQHHQQQQAAGGSESHPVPPTAPLTPLLHGEGASQQPRHRGQNRDAPQPYELNTAINCRDEVVSPLPSALQGPSGSLSAPPAASVISAPPSSSSRHRKRRRTSSKSEAGARGGGQGSKEKGRGSWGGRHHHHHPLPAAGFKKQQRKFQYGNYCKYYGYRNPSCEDGRLRVLKPEWFRGRDVLDLGCNVGHLTLSIACKWGPSRMVGLDIDSRLIHSARQNIRHYLSEELRLPPQTLEGDPGAEGEEGTTTVRKRSCFPASLTASRGPIAAPQVPLDGADTSVFPNNVVFVTGNYVLDRDDLVEAQTPEYDVVLCLSLTKWVHLNWGDEGLKRMFRRIYRHLRPGGILVLEPQPWSSYGKRKTLTETIYKNYYRIQLKPEQFSSYLTSPDVGFSSYELVATPHNTSKGFQRPVYLFHKARSPSH","length":689,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":545,"region_id":"DP02832r001","start":492,"term_id":"IDPO:0000002","statement":[{"text":"Electron density not visible for the residues between the two regions involved in cofactor (SAM/SAH) binding ","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30559425","version":2,"reference_html":"Structural basis of 7SK RNA 5'-γ-phosphate methylation and retention by MePCE. <i> Yang Y, Eichhorn CD, Wang Y, Cascio D, Feigon J. </i> Nat Chem Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6DCB"},{"db":"PDB","id":"6DCC"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":689,"region_id":"DP02832r002","start":400,"term_id":"GO:0003723","statement":[{"text":"MePCE binds tightly to capped RNA.","type":"Results"},{"text":"5′ capping is a tightly regulated step in RNA processing that is required for RNA stability, localization, and function.","type":"Introduction"},{"text":"The MePCE region used for ITC experiments corresponds to MTase domain (residues 400–689)","type":"Curator statement"}],"curator_id":"esalladini","released":"2022_03","ec_name":"isothermal titration calorimetry evidence used in manual assertion","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"30559425","version":4,"reference_html":"Structural basis of 7SK RNA 5'-γ-phosphate methylation and retention by MePCE. <i> Yang Y, Eichhorn CD, Wang Y, Cascio D, Feigon J. </i> Nat Chem Biol, 2019","date":"2022-03-08T14:15:31.780Z","reference_source":"pmid","ec_id":"ECO:0005647","term_name":"RNA binding","curator_orcid":"0000-0002-5152-5953","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"RNAcentral","id":"URS0000734D8F_9606","operator":"and","partner_start":null,"partner_end":null}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":689,"region_id":"DP02832r003","start":400,"term_id":"GO:0098772","statement":[{"text":"MePCE binds tightly to capped RNA.","type":"Results"},{"text":"5′ capping is a tightly regulated step in RNA processing that is required for RNA stability, localization, and function.","type":"Introduction"},{"text":"The MePCE region used for ITC experiments corresponds to MTase domain (residues 400–689)","type":"Curator statement"}],"curator_id":"esalladini","released":"2022_03","ec_name":"isothermal titration calorimetry evidence used in manual assertion","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"30559425","version":4,"reference_html":"Structural basis of 7SK RNA 5'-γ-phosphate methylation and retention by MePCE. <i> Yang Y, Eichhorn CD, Wang Y, Cascio D, Feigon J. </i> Nat Chem Biol, 2019","date":"2022-03-08T14:15:22.008Z","reference_source":"pmid","ec_id":"ECO:0005647","term_name":"molecular function regulator","curator_orcid":"0000-0002-5152-5953","ec_go":"IPI","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"RNAcentral","id":"URS0000734D8F_9606","operator":"and","partner_start":null,"partner_end":null}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":431,"region_id":"DP02832r004","start":418,"term_id":"IDPO:0000002","statement":[{"text":"In the absence of RNA, the N-terminus (residues 418–431) and C-terminal β6-β7 loop (residues 665–676) are partially disordered (Fig. 2c,f), while in the presence of meSL1p, a helix α0 forms near the N-terminus, loop residues that connect to α1 become ordered, and the β6-β7 loop adopts an ordered structure with a short helix α7 in the middle.","type":"Results"},{"text":"Based on studies indicating that MePCE binds the proximal end of the 7SK SL1 and adjacent ssRNA in vivo (Fig. 1c), we designed and synthesized an RNA hairpin-ssRNA construct comprising the 5′-end of 7SK SL1 with a UUCG tetraloop and an eight nucleotide ssRNA 3′ overhang (SL1p).","type":"Results"},{"text":"The structures of MePCE–SAH in the absence and presence of SL1p are globally similar (all atom RMSD 0.29 Å), but there are major differences around the active site and RNA-protein interface (Fig. 2e,f). In the absence of RNA, the N-terminus (residues 418–431) and C-terminal β6-β7 loop (residues 665–676) are partially disordered (Fig. 2c,f), while in the presence of meSL1p, a helix α0 forms near the N-terminus, loop residues that connect to α1 become ordered, and the β6-β7 loop adopts an ordered structure with a short helix α7 in the middle (Fig. 2b,e).","type":"Results"},{"text":"Authors of the publication compare their crystal structures of MePCE-MT bound to SL1p (PDB: 6dcb, 6dcc) to an unpublished structure of unbound MePCE-MT (PDB:5UNA), to highlights the conformational changes in MePCEMT that occur on RNA binding.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30559425","version":2,"reference_html":"Structural basis of 7SK RNA 5'-γ-phosphate methylation and retention by MePCE. <i> Yang Y, Eichhorn CD, Wang Y, Cascio D, Feigon J. </i> Nat Chem Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":431,"region_id":"DP02832r005","start":418,"term_id":"IDPO:0000011","statement":[{"text":"In the absence of RNA, the N-terminus (residues 418–431) and C-terminal β6-β7 loop (residues 665–676) are partially disordered (Fig. 2c,f), while in the presence of meSL1p, a helix α0 forms near the N-terminus, loop residues that connect to α1 become ordered, and the β6-β7 loop adopts an ordered structure with a short helix α7 in the middle.","type":"Results"},{"text":"Based on studies indicating that MePCE binds the proximal end of the 7SK SL1 and adjacent ssRNA in vivo (Fig. 1c), we designed and synthesized an RNA hairpin-ssRNA construct comprising the 5′-end of 7SK SL1 with a UUCG tetraloop and an eight nucleotide ssRNA 3′ overhang (SL1p).","type":"Results"},{"text":"The structures of MePCE–SAH in the absence and presence of SL1p are globally similar (all atom RMSD 0.29 Å), but there are major differences around the active site and RNA-protein interface (Fig. 2e,f). In the absence of RNA, the N-terminus (residues 418–431) and C-terminal β6-β7 loop (residues 665–676) are partially disordered (Fig. 2c,f), while in the presence of meSL1p, a helix α0 forms near the N-terminus, loop residues that connect to α1 become ordered, and the β6-β7 loop adopts an ordered structure with a short helix α7 in the middle (Fig. 2b,e).","type":"Results"},{"text":"Authors of the publication compare their crystal structures of MePCE-MT bound to SL1p (PDB: 6dcb, 6dcc) to an unpublished structure of unbound MePCE-MT (PDB:5UNA), to highlights the conformational changes in MePCEMT that occur on RNA binding.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30559425","version":2,"reference_html":"Structural basis of 7SK RNA 5'-γ-phosphate methylation and retention by MePCE. <i> Yang Y, Eichhorn CD, Wang Y, Cascio D, Feigon J. </i> Nat Chem Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"6DCB"},{"db":"PDB","id":"6DCC"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":676,"region_id":"DP02832r006","start":665,"term_id":"IDPO:0000011","statement":[{"text":"In the absence of RNA, the N-terminus (residues 418–431) and C-terminal β6-β7 loop (residues 665–676) are partially disordered (Fig. 2c,f), while in the presence of meSL1p, a helix α0 forms near the N-terminus, loop residues that connect to α1 become ordered, and the β6-β7 loop adopts an ordered structure with a short helix α7 in the middle.","type":"Results"},{"text":"Based on studies indicating that MePCE binds the proximal end of the 7SK SL1 and adjacent ssRNA in vivo (Fig. 1c), we designed and synthesized an RNA hairpin-ssRNA construct comprising the 5′-end of 7SK SL1 with a UUCG tetraloop and an eight nucleotide ssRNA 3′ overhang (SL1p).","type":"Results"},{"text":"The structures of MePCE–SAH in the absence and presence of SL1p are globally similar (all atom RMSD 0.29 Å), but there are major differences around the active site and RNA-protein interface (Fig. 2e,f). In the absence of RNA, the N-terminus (residues 418–431) and C-terminal β6-β7 loop (residues 665–676) are partially disordered (Fig. 2c,f), while in the presence of meSL1p, a helix α0 forms near the N-terminus, loop residues that connect to α1 become ordered, and the β6-β7 loop adopts an ordered structure with a short helix α7 in the middle (Fig. 2b,e).","type":"Results"},{"text":"Authors of the publication compare their crystal structures of MePCE-MT bound to SL1p (PDB: 6dcb, 6dcc) to an unpublished structure of unbound MePCE-MT (PDB:5UNA), to highlights the conformational changes in MePCEMT that occur on RNA binding.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30559425","version":2,"reference_html":"Structural basis of 7SK RNA 5'-γ-phosphate methylation and retention by MePCE. <i> Yang Y, Eichhorn CD, Wang Y, Cascio D, Feigon J. </i> Nat Chem Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"6DCB"},{"db":"PDB","id":"6DCC"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":676,"region_id":"DP02832r007","start":665,"term_id":"IDPO:0000002","statement":[{"text":"In the absence of RNA, the N-terminus (residues 418–431) and C-terminal β6-β7 loop (residues 665–676) are partially disordered (Fig. 2c,f), while in the presence of meSL1p, a helix α0 forms near the N-terminus, loop residues that connect to α1 become ordered, and the β6-β7 loop adopts an ordered structure with a short helix α7 in the middle.","type":"Results"},{"text":"Based on studies indicating that MePCE binds the proximal end of the 7SK SL1 and adjacent ssRNA in vivo (Fig. 1c), we designed and synthesized an RNA hairpin-ssRNA construct comprising the 5′-end of 7SK SL1 with a UUCG tetraloop and an eight nucleotide ssRNA 3′ overhang (SL1p).","type":"Results"},{"text":"The structures of MePCE–SAH in the absence and presence of SL1p are globally similar (all atom RMSD 0.29 Å), but there are major differences around the active site and RNA-protein interface (Fig. 2e,f). In the absence of RNA, the N-terminus (residues 418–431) and C-terminal β6-β7 loop (residues 665–676) are partially disordered (Fig. 2c,f), while in the presence of meSL1p, a helix α0 forms near the N-terminus, loop residues that connect to α1 become ordered, and the β6-β7 loop adopts an ordered structure with a short helix α7 in the middle (Fig. 2b,e).","type":"Results"},{"text":"Authors of the publication compare their crystal structures of MePCE-MT bound to SL1p (PDB: 6dcb, 6dcc) to an unpublished structure of unbound MePCE-MT (PDB:5UNA), to highlights the conformational changes in MePCEMT that occur on RNA binding.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30559425","version":2,"reference_html":"Structural basis of 7SK RNA 5'-γ-phosphate methylation and retention by MePCE. <i> Yang Y, Eichhorn CD, Wang Y, Cascio D, Feigon J. </i> Nat Chem Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02832","date":"2020-04-27T10:10:09.300Z","organism":"Homo sapiens","regions_counter":7,"name":"7SK snRNA methylphosphate capping enzyme","dataset":[],"UniParc":"UPI0000227DFA","uniref100":"UniRef100_Q7L2J0","uniref90":"UniRef90_Q7L2J0","uniref50":"UniRef50_Q7L2J0","genes":[{"name":{"value":"MEPCE","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"30559425","url":"http://www.ncbi.nlm.nih.gov/pubmed/30559425","alternativeUrl":"https://europepmc.org/abstract/MED/30559425"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:20247","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:20247"}}]},"synonyms":[{"value":"BCDIN3","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"17643375","url":"http://www.ncbi.nlm.nih.gov/pubmed/17643375","alternativeUrl":"https://europepmc.org/abstract/MED/17643375"}}]}]}],"alphafold_very_low_content":0.5094339622641509,"disorder_content":0.11611030478955008,"disprot_consensus":{"full":[{"start":400,"end":417,"type":"F"},{"start":418,"end":431,"type":"T"},{"start":432,"end":491,"type":"F"},{"start":492,"end":545,"type":"D"},{"start":546,"end":664,"type":"F"},{"start":665,"end":676,"type":"T"},{"start":677,"end":689,"type":"F"}],"Structural state":[{"start":418,"end":431,"type":"D"},{"start":492,"end":545,"type":"D"},{"start":665,"end":676,"type":"D"}],"Molecular function":[{"start":400,"end":689,"type":"F"}],"Structural transition":[{"start":418,"end":431,"type":"T"},{"start":665,"end":676,"type":"T"}]}},{"acc":"Q9Y4F1","features":{"gene3D":[{"start":931,"end":1034,"id":"G3DSA:2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":931,"end":1034,"id":"G3DSA:2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":119,"end":223,"id":"G3DSA:1.20.80.10","name":"G3DSA:1.20.80.10"},{"start":537,"end":750,"id":"G3DSA:1.20.900.10","name":"Dbl homology (DH) domain"}],"pfam":[{"id":"PF00169","name":"PH domain","start":762,"end":855},{"id":"PF00169","name":"PH domain","start":935,"end":1028},{"id":"PF00373","name":"FERM central domain","start":125,"end":230},{"id":"PF00621","name":"RhoGEF domain","start":544,"end":727},{"id":"PF08736","name":"FERM adjacent (FA)","start":330,"end":369},{"id":"PF09379","name":"FERM N-terminal domain","start":44,"end":106},{"id":"PF09380","name":"FERM C-terminal PH-like domain","start":234,"end":323}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MGEIEQRPTPGSRLGAPENSGISTLERGQKPPPTPSGKLVSIKIQMLDDTQEAFEVPQRAPGKVLLDAVCNHLNLVEGDYFGLEFPDHKKITVWLDLLKPIVKQIRRPKHVVVKFVVKFFPPDHTQLQEELTRYLFALQVKQDLAQGRLTCNDTSAALLISHIVQSEIGDFDEALDREHLAKNKYIPQQDALEDKIVEFHHNHIGQTPAESDFQLLEIARRLEMYGIRLHPAKDREGTKINLAVANTGILVFQGFTKINAFNWAKVRKLSFKRKRFLIKLRPDANSAYQDTLEFLMASRDFCKSFWKICVEHHAFFRLFEEPKPKPKPVLFSRGSSFRFSGRTQKQVLDYVKEGGHKKVQFERKHSKIHSIRSLASQPTELNSEVLEQSQQSTSLTFGEGAESPGGQSCRRGKEPKVSAGEPGSHPSPAPRRSPAGNKQADGAASAPTEEEEEVVKDRTQQSKPQPPQPSTGSLTGSPHLSELSVNSQGGVAPANVTLSPNLSPDTKQASPLISPLLNDQACPRTDDEDEGRRKRFPTDKAYFIAKEVSTTERTYLKDLEVITSWFQSTVSKEDAMPEALKSLIFPNFEPLHKFHTNFLKEIEQRLALWEGRSNAQIRDYQRIGDVMLKNIQGMKHLAAHLWKHSEALEALENGIKSSRRLENFCRDFELQKVCYLPLNTFLLRPLHRLMHYKQVLERLCKHHPPSHADFRDCRAALAEITEMVAQLHGTMIKMENFQKLHELKKDLIGIDNLVVPGREFIRLGSLSKLSGKGLQQRMFFLFNDVLLYTSRGLTASNQFKVHGQLPLYGMTIEESEDEWGVPHCLTLRGQRQSIIVAASSRSEMEKWVEDIQMAIDLAEKSSSPAPEFLASSPPDNKSPDEATAADQESEDDLSASRTSLERQAPHRGNTMVHVCWHRNTSVSMVDFSIAVENQLSGNLLRKFKNSNGWQKLWVVFTNFCLFFYKSHQDNHPLASLPLLGYSLTIPSESENIQKDYVFKLHFKSHVYYFRAESEYTFERWMEVIRSATSSASRPHVLSHKESLVY","length":1045,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":909,"region_id":"DP02833r001","start":862,"term_id":"IDPO:0000002","statement":[{"text":"They also have a second PH domain (referred to as PH2), which is connected to the first PH domain (PH1) by a ~70-residue linker.","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23375260","version":2,"reference_html":"Structural basis for autoinhibition of the guanine nucleotide exchange factor FARP2. <i> He X, Kuo YC, Rosche TJ, Zhang X. </i> Structure, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4H6Y"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:42:10.016Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":909,"region_id":"DP02833r002","start":862,"term_id":"IDPO:0000033","statement":[{"text":"They also have a second PH domain (referred to as PH2), which is connected to the first PH domain (PH1) by a ~70-residue linker.","type":"Introduction"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23375260","version":3,"reference_html":"Structural basis for autoinhibition of the guanine nucleotide exchange factor FARP2. <i> He X, Kuo YC, Rosche TJ, Zhang X. </i> Structure, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:42:10.679Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02833","date":"2020-04-27T11:29:13.954Z","organism":"Homo sapiens","regions_counter":2,"name":"FERM, ARHGEF and pleckstrin domain-containing protein 1","dataset":[],"UniParc":"UPI000007052C","uniref100":"UniRef100_Q9Y4F1","uniref90":"UniRef90_Q9Y4F1","uniref50":"UniRef50_F1LYQ8","genes":[{"name":{"value":"FARP1"},"synonyms":[{"value":"CDEP"},{"value":"PLEKHC2"}]}],"alphafold_very_low_content":0.2555023923444976,"disorder_content":0.045933014354066985,"disprot_consensus":{"full":[{"start":862,"end":909,"type":"D"}],"Structural state":[{"start":862,"end":909,"type":"D"}],"Disorder function":[{"start":862,"end":909,"type":"F"}]}},{"acc":"Q9Y2Z0","features":{"gene3D":[{"start":165,"end":276,"id":"G3DSA:2.60.40.790","name":"G3DSA:2.60.40.790"},{"start":19,"end":120,"id":"G3DSA:1.25.40.10","name":"G3DSA:1.25.40.10"}],"pfam":[{"id":"PF04969","name":"CS domain","start":173,"end":248},{"id":"PF05002","name":"SGS domain","start":285,"end":365},{"id":"PF13432","name":"Tetratricopeptide repeat","start":59,"end":104}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MAAAAAGTATSQRFFQSFSDALIDEDPQAALEELTKALEQKPDDAQYYCQRAYCHILLGNYCVAVADAKKSLELNPNNSTAMLRKGICEYHEKNYAAALETFTEGQKLDIETGFHRVGQAGLQLLTSSDPPALDSQSAGITGADANFSVWIKRCQEAQNGSESEVWTHQSKIKYDWYQTESQVVITLMIKNVQKNDVNVEFSEKELSALVKLPSGEDYNLKLELLHPIIPEQSTFKVLSTKIEIKLKKPEAVRWEKLEGQGDVPTPKQFVADVKNLYPSSSPYTRNWDKLVGEIKEEEKNEKLEGDAALNRLFQQIYSDGSDEVKRAMNKSFMESGGTVLSTNWSDVGKRKVEINPPDDMEWKKY","length":365,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":276,"region_id":"DP02834r001","start":262,"term_id":"IDPO:0000002","statement":[{"text":"The line-widths of the peaks in the spectrum of intact Sgt1 are smaller than expected for a single domain molecule over 30 kDa, strongly implying that the linkers between the domains are flexible and that any contacts between domains are not long-lived. Hence, the domains probably function in a coordinated but not necessarily cooperative manner.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14761955","version":2,"reference_html":"Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain. <i> Lee YT, Jacob J, Michowski W, Nowotny M, Kuznicki J, Chazin WJ. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":276,"region_id":"DP02834r002","start":262,"term_id":"IDPO:0000002","statement":[{"text":"Missing residues in the crystal structure of human Sgt1 corresponds to the region connecting CS domain and SGS domain.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14761955","version":2,"reference_html":"Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain. <i> Lee YT, Jacob J, Michowski W, Nowotny M, Kuznicki J, Chazin WJ. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1RL1"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":276,"region_id":"DP02834r003","start":262,"term_id":"IDPO:0000033","statement":[{"text":"Missing residues in the crystal structure of human Sgt1 corresponds to the region connecting CS domain and SGS domain.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14761955","version":3,"reference_html":"Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain. <i> Lee YT, Jacob J, Michowski W, Nowotny M, Kuznicki J, Chazin WJ. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"1RL1"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":276,"region_id":"DP02834r004","start":262,"term_id":"IDPO:0000033","statement":[{"text":"The line-widths of the peaks in the spectrum of intact Sgt1 are smaller than expected for a single domain molecule over 30 kDa, strongly implying that the linkers between the domains are flexible and that any contacts between domains are not long-lived. Hence, the domains probably function in a coordinated but not necessarily cooperative manner.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14761955","version":3,"reference_html":"Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain. <i> Lee YT, Jacob J, Michowski W, Nowotny M, Kuznicki J, Chazin WJ. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"1RL1"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02834","date":"2020-04-27T22:38:47.940Z","organism":"Homo sapiens","regions_counter":4,"name":"Protein SGT1 homolog","dataset":[],"UniParc":"UPI00001CDFF4","uniref100":"UniRef100_Q9Y2Z0","uniref90":"UniRef90_Q9Y2Z0","uniref50":"UniRef50_Q9Y2Z0","genes":[{"name":{"value":"SUGT1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:16987","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:16987"}}]}}],"alphafold_very_low_content":0.12602739726027398,"disorder_content":0.0410958904109589,"disprot_consensus":{"full":[{"start":262,"end":276,"type":"D"}],"Structural state":[{"start":262,"end":276,"type":"D"}],"Disorder function":[{"start":262,"end":276,"type":"F"}]}},{"acc":"Q14849","features":{"gene3D":[{"start":216,"end":444,"id":"G3DSA:3.30.530.20","name":"G3DSA:3.30.530.20"}],"pfam":[{"id":"PF01852","name":"START domain","start":240,"end":443},{"id":"PF10457","name":"Cholesterol-capturing domain","start":47,"end":213}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MSKLPRELTRDLERSLPAVASLGSSLSHSQSLSSHLLPPPEKRRAISDVRRTFCLFVTFDLLFISLLWIIELNTNTGIRKNLEQEIIQYNFKTSFFDIFVLAFFRFSGLLLGYAVLRLRHWWVIAVTTLVSSAFLIVKVILSELLSKGAFGYLLPIVSFVLAWLETWFLDFKVLPQEAEEERWYLAAQVAVARGPLLFSGALSEGQFYSPPESFAGSDNESDEEVAGKKSFSAQEREYIRQGKEATAVVDQILAQEENWKFEKNNEYGDTVYTIEVPFHGKTFILKTFLPCPAELVYQEVILQPERMVLWNKTVTACQILQRVEDNTLISYDVSAGAAGGVVSPRDFVNVRRIERRRDRYLSSGIATSHSAKPPTHKYVRGENGPGGFIVLKSASNPRVCTFVWILNTDLKGRLPRYLIHQSLAATMFEFAFHLRQRISELGARA","length":445,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":230,"region_id":"DP02835r001","start":216,"term_id":"IDPO:0000002","statement":[{"text":"The final structural model includes residues 231–444 of StARD3 (the coordinates for residues 216–230 were omitted because no electron density was observed), 224 water molecules, three molecules of ethylene glycol, one sulfate ion and one molecule of l-(+)-tartaric acid.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27487925","version":2,"reference_html":"Structure of the lutein-binding domain of human StARD3 at 1.74 Å resolution and model of a complex with lutein. <i> Horvath MP, George EW, Tran QT, Baumgardner K, Zharov G, Lee S, Sharifzadeh H, Shihab S, Mattinson T, Li B, Bernstein PS. </i> Acta Crystallogr F Struct Biol Commun, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5I9J"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02835r002","ec_ontology":"ECO","end":230,"term_id":"IDPO:0000033","start":216,"version":3,"statement":[{"text":"The final structural model includes residues 231–444 of StARD3 (the coordinates for residues 216–230 were omitted because no electron density was observed), 224 water molecules, three molecules of ethylene glycol, one sulfate ion and one molecule of l-(+)-tartaric acid.","type":"Results"},{"text":"Missing residues in the crystal structure corresponds to the IDR connecting the MENTAL domain to the SMART domain.","type":"Curator statement"}],"term_name":"flexible linker","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27487925","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Disorder function","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Structure of the lutein-binding domain of human StARD3 at 1.74 Å resolution and model of a complex with lutein. <i> Horvath MP, George EW, Tran QT, Baumgardner K, Zharov G, Lee S, Sharifzadeh H, Shihab S, Mattinson T, Li B, Bernstein PS. </i> Acta Crystallogr F Struct Biol Commun, 2016","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02835","date":"2020-04-27T22:49:50.808Z","organism":"Homo sapiens","regions_counter":2,"name":"StAR-related lipid transfer protein 3","dataset":[],"UniParc":"UPI000012F1BC","uniref100":"UniRef100_Q14849","uniref90":"UniRef90_Q14849","uniref50":"UniRef50_Q14849","genes":[{"name":{"value":"STARD3","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:17579","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:17579"}}]},"synonyms":[{"value":"CAB1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9270027","url":"http://www.ncbi.nlm.nih.gov/pubmed/9270027","alternativeUrl":"https://europepmc.org/abstract/MED/9270027"}}]},{"value":"MLN64","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11053434","url":"http://www.ncbi.nlm.nih.gov/pubmed/11053434","alternativeUrl":"https://europepmc.org/abstract/MED/11053434"}}]}]}],"alphafold_very_low_content":0.16404494382022472,"disorder_content":0.033707865168539325,"disprot_consensus":{"full":[{"start":216,"end":230,"type":"D"}],"Structural state":[{"start":216,"end":230,"type":"D"}],"Disorder function":[{"start":216,"end":230,"type":"F"}]}},{"acc":"P24785","features":{"gene3D":[],"pfam":[{"id":"PF00035","name":"Double-stranded RNA binding motif","start":4,"end":68},{"id":"PF00035","name":"Double-stranded RNA binding motif","start":171,"end":239},{"id":"PF00270","name":"DEAD/DEAH box helicase","start":392,"end":543},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":640,"end":772},{"id":"PF04408","name":"Helicase associated domain (HA2), winged-helix","start":836,"end":864},{"id":"PF07717","name":"Oligonucleotide/oligosaccharide-binding (OB)-fold","start":1002,"end":1079},{"id":"PF21010","name":"Helicase associated domain (HA2), ratchet-like","start":865,"end":945}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"sequence":"MDIKSFLYQFCAKSQIEPKFDIRQTGPKNRQRFLCEVRVEPNTYIGVGNSTNKKDAEKNACRDFVNYLVRVGKLNTNDVPADAGASGGGPRTGLEGAGMAGGSGQQKRVFDGQSGPQDLGEAYRPLNHDGGDGGNRYSVIDRIQEQRDMNEAEAFDVNAAIHGNWTIENAKERLNIYKQTNNIRDDYKYTPVGPEHARSFLAELSIYVPALNRTVTARESGSNKKSASKSCALSLVRQLFHLNVIEPFSGTLKKKKDEQLKPYPVKLSPNLINKIDEVIKGLDLPVVNPRNIKIELDGPPIPLIVNLSRIDSSQQDGEKRQESSVIPWAPPQANWNTWHACNIDEGELATTSIDDLSMDYERSLRDRRQNDNEYRQFLEFREKLPIAAMRSEILTAINDNPVVIIRGNTGCGKTTQIAQYILDDYICSGQGGYANIYVTQPRRISAISVAERVARERCEQLGDTVGYSVRFESVFPRPYGAILFCTVGVLLRKLEAGLRGVSHIIVDEIHERDVNSDFLLVILRDMVDTYPDLHVILMSATIDTTKFSKYFGICPVLEVPGRAFPVQQFFLEDIIQMTDFVPSAESRRKRKEVEDEEQLLSEDKDEAEINYNKVCEDKYSQKTRNAMAMLSESDVSFELLEALLMHIKSKNIPGAILVFLPGWNLIFALMKFLQNTNIFGDTSQYQILPCHSQIPRDEQRKVFEPVPEGVTKIILSTNIAETSITIDDIVFVIDICKARMKLFTSHNNLTSYATVWASKTNLEQRKGRAGRVRPGFCFTLCSRARFQALEDNLTPEMFRTPLHEMALTIKLLRLGSIHHFLSKALEPPPVDAVIEAEVLLREMRCLDANDELTPLGRLLARLPIEPRLGKMMVLGAVFGCADLMAIMASYSSTFSEVFSLDIGQRRLANHQKALSGTKCSDHVAMIVASQMWRREKQRGEHMEARFCDWKGLQMSTMNVIWDAKQQLLDLLQQAGFPEECMISHEVDERIDGDDPVLDVSLALLCLGLYPNICVHKEKRKVLTTESKAALLHKTSVNCSNLAVTFPYPFFVFGEKIRTRAVSCKQLSMVSPLQVILFGSRKIDLAANNIVRVDNWLNFDIEPELAAKIGALKPALEDLITVACDNPSDILRLEEPYAQLVKVVKDLCVKSAGDFGLQRESGILPHQSRQFSDGGGPPKRGRFETGRFTNSSFGRRGNGRTFGGGYGNNGGGYGNNGGGYGNIGGGYGNNAGGYGNNGGYGNNGGGYRNNGGGYGNNGGGYGNKRGGFGDSFESNRGSGGGFRNGDQGGRWGNF","length":1293,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":164,"region_id":"DP02836r001","start":81,"term_id":"IDPO:0000002","statement":[{"text":"Only individual dsRBDs, consisting of residues 1–80 of dsRBD1 (Figure ​2B) and residues 165–247 of dsRBD2 (Figure ​2C), were visible in the electron density map. The linker region connecting the two domains is not visible, which is consistent with the hypothesis that this linker is normally disordered (Figure ​2A).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30649456","version":2,"reference_html":"Structural insights reveal the specific recognition of roX RNA by the dsRNA-binding domains of the RNA helicase MLE and its indispensable role in dosage compensation in Drosophila. <i> Lv M, Yao Y, Li F, Xu L, Yang L, Gong Q, Xu YZ, Shi Y, Fan YJ, Tang Y. </i> Nucleic Acids Res, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5ZTM"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":164,"region_id":"DP02836r002","start":81,"term_id":"IDPO:0000033","statement":[{"text":"Only individual dsRBDs, consisting of residues 1–80 of dsRBD1 (Figure ​2B) and residues 165–247 of dsRBD2 (Figure ​2C), were visible in the electron density map. The linker region connecting the two domains is not visible, which is consistent with the hypothesis that this linker is normally disordered (Figure ​2A).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30649456","version":3,"reference_html":"Structural insights reveal the specific recognition of roX RNA by the dsRNA-binding domains of the RNA helicase MLE and its indispensable role in dosage compensation in Drosophila. <i> Lv M, Yao Y, Li F, Xu L, Yang L, Gong Q, Xu YZ, Shi Y, Fan YJ, Tang Y. </i> Nucleic Acids Res, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"5ZTM"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":142,"region_id":"DP02836r003","start":1,"term_id":"IDPO:0000002","statement":[{"text":"For each copy, well-defined electron density is present for residues 143–1158 of MLE (with the exception of a loop 311–321), as well as for ADP-AlF4, a magnesium ion, and 10 ribonucleotides (Table 1).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26545078","version":2,"reference_html":"Structure of the RNA Helicase MLE Reveals the Molecular Mechanisms for Uridine Specificity and RNA-ATP Coupling. <i> Prabu JR, Müller M, Thomae AW, Schüssler S, Bonneau F, Becker PB, Conti E. </i> Mol Cell, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5AOR"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":321,"region_id":"DP02836r004","start":311,"term_id":"IDPO:0000002","statement":[{"text":"For each copy, well-defined electron density is present for residues 143–1158 of MLE (with the exception of a loop 311–321), as well as for ADP-AlF4, a magnesium ion, and 10 ribonucleotides (Table 1).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26545078","version":2,"reference_html":"Structure of the RNA Helicase MLE Reveals the Molecular Mechanisms for Uridine Specificity and RNA-ATP Coupling. <i> Prabu JR, Müller M, Thomae AW, Schüssler S, Bonneau F, Becker PB, Conti E. </i> Mol Cell, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5AOR"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1293,"region_id":"DP02836r005","start":1159,"term_id":"IDPO:0000002","statement":[{"text":"For each copy, well-defined electron density is present for residues 143–1158 of MLE (with the exception of a loop 311–321), as well as for ADP-AlF4, a magnesium ion, and 10 ribonucleotides (Table 1).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26545078","version":2,"reference_html":"Structure of the RNA Helicase MLE Reveals the Molecular Mechanisms for Uridine Specificity and RNA-ATP Coupling. <i> Prabu JR, Müller M, Thomae AW, Schüssler S, Bonneau F, Becker PB, Conti E. </i> Mol Cell, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5AOR"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":104,"region_id":"DP02836r006","start":1,"term_id":"IDPO:0000002","statement":[{"text":"Proteolysis of MLEΔC resulted in a stable 120 kDa fragment lacking dsRBD1 but containing dsRBD2 (MLE105-1158, referred to as MLEcore) (Figure S1A).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26545078","version":2,"reference_html":"Structure of the RNA Helicase MLE Reveals the Molecular Mechanisms for Uridine Specificity and RNA-ATP Coupling. <i> Prabu JR, Müller M, Thomae AW, Schüssler S, Bonneau F, Becker PB, Conti E. </i> Mol Cell, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","cross_refs":[{"db":"PDB","id":"5AOR"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":7227,"disprot_id":"DP02836","date":"2020-04-28T09:00:55.520Z","organism":"Drosophila melanogaster","regions_counter":6,"name":"Dosage compensation regulator","dataset":[],"UniParc":"UPI000012F1F4","uniref100":"UniRef100_P24785","uniref90":"UniRef90_P24785","uniref50":"UniRef50_P24785","genes":[{"name":{"value":"mle","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0002774","url":"http://flybase.org/reports/FBgn0002774.html"}}]},"synonyms":[{"value":"nap","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0002774","url":"http://flybase.org/reports/FBgn0002774.html"}}]}],"orfNames":[{"value":"CG11680","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0002774","url":"http://flybase.org/reports/FBgn0002774.html"}}]}]}],"alphafold_very_low_content":0.14617169373549885,"disorder_content":0.2397525135344161,"disprot_consensus":{"full":[{"start":1,"end":164,"type":"D"},{"start":311,"end":321,"type":"D"},{"start":1159,"end":1293,"type":"D"}],"Structural state":[{"start":1,"end":164,"type":"D"},{"start":311,"end":321,"type":"D"},{"start":1159,"end":1293,"type":"D"}],"Disorder function":[{"start":81,"end":164,"type":"F"}]}},{"acc":"Q9QXN5","features":{"gene3D":[],"pfam":[{"id":"PF05153","name":"Myo-inositol oxygenase","start":38,"end":285}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MKVDVGPDPSLVYRPDVDPEMAKSKDSFRNYTSGPLLDRVFTTYKLMHTHQTVDFVSRKRIQYGSFSYKKMTIMEAVGMLDDLVDESDPDVDFPNSFHAFQTAEGIRKAHPDKDWFHLVGLLHDLGKIMALWGEPQWAVVGDTFPVGCRPQASVVFCDSTFQDNPDLQDPRYSTELGMYQPHCGLENVLMSWGHDEYLYQMMKFNKFSLPSEAFYMIRFHSFYPWHTGGDYRQLCSQQDLDMLPWVQEFNKFDLYTKCPDLPDVESLRPYYQGLIDKYCPGTLSW","length":285,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":28,"region_id":"DP02837r001","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"No electron density was found for the N-terminal residues 1–28. An N-terminal 3-kDa fragment is readily lost by proteolysis (15), but SDS/PAGE analysis of dissolved crystals (23) showed that the molecule was intact; these residues are assumed to be disordered in the crystal structure. The putative NADPH-binding motif identified by Yang et al. (19) is in this disordered region; we find no evidence of NADPH binding (data not shown). ","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17012379","version":2,"reference_html":"Crystal structure of a substrate complex of myo-inositol oxygenase, a di-iron oxygenase with a key role in inositol metabolism. <i> Brown PM, Caradoc-Davies TT, Dickson JM, Cooper GJ, Loomes KM, Baker EN. </i> Proc Natl Acad Sci U S A, 2006","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2HUO"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2023_12","ncbi_taxon_id":10090,"disprot_id":"DP02837","date":"2020-04-28T11:07:23.461Z","organism":"Mus musculus","regions_counter":1,"name":"Inositol oxygenase","dataset":[],"UniParc":"UPI0000029CB4","uniref100":"UniRef100_Q9QXN5","uniref90":"UniRef90_Q9QXN5","uniref50":"UniRef50_Q9QXN5","genes":[{"name":{"value":"Miox"},"synonyms":[{"value":"Aldrl6"},{"value":"Rsor"}]}],"alphafold_very_low_content":0.017543859649122806,"disorder_content":0.09824561403508772,"disprot_consensus":{"full":[{"start":1,"end":28,"type":"D"}],"Structural state":[{"start":1,"end":28,"type":"D"}]}},{"acc":"P20807","features":{"gene3D":[],"pfam":[{"id":"PF00648","name":"Calpain family cysteine protease","start":75,"end":415},{"id":"PF01067","name":"Calpain large subunit, domain III","start":435,"end":574},{"id":"PF13833","name":"EF-hand domain pair","start":665,"end":723},{"id":"PF16648","name":"Unstructured region on Calpain-3","start":583,"end":636},{"id":"PF21875","name":"Calpain-13-like, C-terminal EF-hand","start":729,"end":796}]},"creator":"lchemes","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MPTVISASVAPRTAAEPRSPGPVPHPAQSKATEAGGGNPSGIYSAIISRNFPIIGVKEKTFEQLHKKCLEKKVLYVDPEFPPDETSLFYSQKFPIQFVWKRPPEICENPRFIIDGANRTDICQGELGDCWFLAAIACLTLNQHLLFRVIPHDQSFIENYAGIFHFQFWRYGEWVDVVIDDCLPTYNNQLVFTKSNHRNEFWSALLEKAYAKLHGSYEALKGGNTTEAMEDFTGGVAEFFEIRDAPSDMYKIMKKAIERGSLMGCSIDDGTNMTYGTSPSGLNMGELIARMVRNMDNSLLQDSDLDPRGSDERPTRTIIPVQYETRMACGLVRGHAYSVTGLDEVPFKGEKVKLVRLRNPWGQVEWNGSWSDRWKDWSFVDKDEKARLQHQVTEDGEFWMSYEDFIYHFTKLEICNLTADALQSDKLQTWTVSVNEGRWVRGCSAGGCRNFPDTFWTNPQYRLKLLEEDDDPDDSEVICSFLVALMQKNRRKDRKLGASLFTIGFAIYEVPKEMHGNKQHLQKDFFLYNASKARSKTYINMREVSQRFRLPPSEYVIVPSTYEPHQEGEFILRVFSEKRNLSEEVENTISVDRPVKKKKTKPIIFVSDRANSNKELGVDQESEEGKGKTSPDKQKQSPQPQPGSSDQESEEQQQFRNIFKQIAGDDMEICADELKKVLNTVVNKHKDLKTHGFTLESCRSMIALMDTDGSGKLNLQEFHHLWNKIKAWQKIFKHYDTDQSGTINSYEMRNAVNDAGFHLNNQLYDIITMRYADKHMNIDFDSFICCFVRLEGMFRAFHAFDKDGDGIIKLNVLEWLQLTMYA","length":821,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":320,"region_id":"DP02838r001","start":269,"term_id":"IDPO:0000002","statement":[{"text":"Following the clear continuing electron density from the N terminus of IS1 (Asp268), eight residues were manually built in molecule B, and seven residues in molecules C and D, but only three residues could be traced in molecule A due to insignificant electron density thereafter. The C-terminal end of IS1 is missing, and electron density is not traceable until partway into PC2 at Pro319 in molecule B, Val320 in molecule C, Gln321 in molecule D, and Glu323 in molecule A. The missing portion of IS1 lies between the 1b and 2b autolysis sites (25, 26).","type":"Results"},{"text":"The limits of the disordered segment vary slightly in each structure, and are determined to be 269-320","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"29382717","version":2,"reference_html":"Structures of human calpain-3 protease core with and without bound inhibitor reveal mechanisms of calpain activation. <i> Ye Q, Campbell RL, Davies PL. </i> J Biol Chem, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6BJD"},{"db":"PDB","id":"6BGP"},{"db":"PDB","id":"6BDT"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":320,"region_id":"DP02838r002","start":269,"term_id":"IDPO:0000002","statement":[{"text":"Both methods showed only 26- and 13-kDa species present. The former matched in size the ΔNS core up to the 1b IS1 cleavage site in PC2, and the latter matched the remainder of PC2 from the 2b IS1 cleavage site onward. These results from the C129S crystals are in agreement with a previous experiment using the Cys129 protease core (25) over a much shorter time frame. It suggests that IS1 of the C129S crystals was indeed autoproteolyzed during crystallization [...] Although there was no autolysis of C129A, most of IS1 still could not be built due to poor quality or missing electron density.\n","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"29382717","version":2,"reference_html":"Structures of human calpain-3 protease core with and without bound inhibitor reveal mechanisms of calpain activation. <i> Ye Q, Campbell RL, Davies PL. </i> J Biol Chem, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","cross_refs":[{"db":"PDB","id":"6BJD"},{"db":"PDB","id":"6BGP"},{"db":"PDB","id":"6BDT"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":320,"region_id":"DP02838r003","start":269,"term_id":"IDPO:0000002","statement":[{"text":"Small-angle X-ray scattering (SAXS) analysis of the C129A mutant suggested that IS1 is disordered and mobile enough to occupy several locations.","type":"Abstract"},{"text":"Therefore, the missing IS1 region was built in using the ensemble optimization method (EOM) (33). A large conformational pool (10,000 possibilities) was generated using sequence information and the crystal structure of Ca2+-bound calpain-3 C129S core as a template but with PC1 and PC2 unfixed and, therefore, free to rotate. However, only those conformers that were consistent with the SAXS experimental scattering data were retained. The final ensemble of conformers of the calpain-3 core with the IS1 structural model inserted was in excellent agreement with both sets of experimental scattering data,","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"29382717","version":2,"reference_html":"Structures of human calpain-3 protease core with and without bound inhibitor reveal mechanisms of calpain activation. <i> Ye Q, Campbell RL, Davies PL. </i> J Biol Chem, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","cross_refs":[{"db":"PDB","id":"6BJD"},{"db":"PDB","id":"6BGP"},{"db":"PDB","id":"6BDT"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":320,"region_id":"DP02838r004","start":269,"term_id":"IDPO:0000059","statement":[{"text":"IS1, interrupts the protease core and must be cleaved for activation and substrate binding","type":"Abstract"},{"text":"the first cleavage as an essential step to activation through removal of an internal propeptide that otherwise blocks substrate access to the catalytic cleft (25).","type":"Introduction"},{"text":"But in addition to the metal ion requirement, it is known that calpain-3 has an additional inhibitory feature, which is IS1 acting as an internal autoinhibitory propeptide to block the enzyme's active site (25). Although in the Ca2+-bound crystal structure, most of IS1 is not visible, what can be seen of IS1 in the active site cleft supports the autoinhibition role. First, the N-terminal segment of IS1 (Met272-Thr273-Tyr274-Gly275) protrudes into the active-site cleft through the S3, S2, S1, and S1′ subsites and makes extensive contacts with residues on either side of the catalytic cleft (Fig. 8). (See detailed description below). Second, residues Val320-Gln321-Tyr322 located just beyond the C terminus of IS1 are part of PC2 that lies on the top of the active site, in which Val320 forms an interaction with residue Glu125 OE2 of PC1 (2.9 Å). Furthermore, an extended hydrophobic patch is formed\nThis region of IS1 that occupies the active-site cleft is perfectly conserved in the comparison of the IS1 sequences from 22 different mammals, which reinforces its functional importance (Fig. S3)","type":"Results"},{"text":"The flexible region occludes the active site, preventing rearrangements necessary for catalytic activity. It needs to undergo auto proteolysis to allow enzyme activation","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"29382717","version":3,"reference_html":"Structures of human calpain-3 protease core with and without bound inhibitor reveal mechanisms of calpain activation. <i> Ye Q, Campbell RL, Davies PL. </i> J Biol Chem, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"6BJD"},{"db":"PDB","id":"6BGP"},{"db":"PDB","id":"6BDT"}],"term_name":"self-inhibition","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02838","date":"2020-04-29T14:43:29.736Z","organism":"Homo sapiens","regions_counter":4,"name":"Calpain-3","dataset":[],"UniParc":"UPI000000103F","uniref100":"UniRef100_P20807","uniref90":"UniRef90_P20807","uniref50":"UniRef50_P20807","genes":[{"name":{"value":"CAPN3","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:1480","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:1480"}}]},"synonyms":[{"value":"CANP3"},{"value":"CANPL3"},{"value":"NCL1"}]}],"alphafold_very_low_content":0.16930572472594396,"disorder_content":0.06333739342265529,"disprot_consensus":{"full":[{"start":269,"end":320,"type":"D"}],"Structural state":[{"start":269,"end":320,"type":"D"}],"Disorder function":[{"start":269,"end":320,"type":"F"}]}},{"acc":"O43070","features":{"gene3D":[{"start":117,"end":217,"id":"G3DSA:3.40.50.10190","name":"BRCT domain"}],"pfam":[{"id":"PF00498","name":"FHA domain","start":23,"end":94}]},"creator":"lchemes","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"sequence":"MWIIEAEGDILKGKSRILFPGTYIVGRNVSDDSSHIQVISKSISKRHARFTILTPSEKDYFTGGPCEFEVKDLDTKFGTKVNEKVVGQNGDSYKEKDLKIQLGKCPFTINAYWRSMCIQFDNPEMLSQWASNLNLLGIPTGLRDSDATTHFVMNRQAGSSITVGTMYAFLKKTVIIDDSYLQYLSTVKESVIEDASLMPDALECFKNIIKNNDQFPSSPEDCINSLEGFSCAMLNTSSESHHLLELLGLRISTFMSLGDIDKELISKTDFVVLNNAVYDSEKISFPEGIFCLTIEQLWKIIIERNSRELISKEIERLKYATASNSTPQKIIQPQRHIQKNIVDDLFSVKKPLPCSPKSKRVKTLENLSIMDFVQPKQMFGKEPEGYLSNQSNNGSAQNKKSGDNSEKTKNSLKSSSKKSANTGSGQGKTKVEYVSYNSVDKGNSSPFKPLELNVVGEKKANAEVDSLPSENVQESEDDKAFEENRRLRNLGSVEYIRIMSSEKSNANSRHTSKYYSGRKNFKKFQKKASQKAPLQAFLSLSEHKKTEVFDQDDTDLEPVPRLMSKVESIPAGASSDKSGKSSISKKSSNSFKELSPKTNNDEDDEFNDLKFHF","length":613,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":553,"region_id":"DP02839r001","start":330,"term_id":"IDPO:0000002","statement":[{"text":"Nbs1 cardinal features: fused, extended, FHA-BRCT(1)-BRCT(2) domains flexibly linked to C-terminal Mre11- and ATM-binding motifs. ","type":"Abstract"},{"text":"To define functional Nbs1 regions, we expressed a series of truncated S. pombe Nbs1 (spNbs1) proteins and mapped structured domains with proteolysis\nTrypsin degradation of Nbs1-ΔAT reveals a stable 37kDa folded core (Nbs1-fc, residues 1-329) encompassing the Nbs1 FHA domain and its two BRCT domains (Figures 1A and 1B). N-terminal sequencing of smaller transiently stable trypsin products maps three additional cleavage sites to a divergent sequence linking BRCT2 and the MB motif. Thus, the N-terminal 55% of spNbs1 comprises a composite FHA-BRCT1-BRCT2 folded Nbs1-fc that is linked to the C-terminal Mre11 and ATM binding regions via a protease-sensitive linker peptide.\n","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"19804755","version":2,"reference_html":"Nbs1 flexibly tethers Ctp1 and Mre11-Rad50 to coordinate DNA double-strand break processing and repair. <i> Williams RS, Dodson GE, Limbo O, Yamada Y, Williams JS, Guenther G, Classen S, Glover JN, Iwasaki H, Russell P, Tainer JA. </i> Cell, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":553,"region_id":"DP02839r002","start":330,"term_id":"IDPO:0000002","statement":[{"text":"Nbs1 cardinal features: fused, extended, FHA-BRCT(1)-BRCT(2) domains flexibly linked to C-terminal Mre11- and ATM-binding motifs. ","type":"Abstract"},{"text":"While spNbs1-fc SAXS closely matches the X-ray structure, the maximum particle dimension (Dmax) for spNbs1-ΔAT is much larger (~175 Å), indicating a very elongated structure (Figures 7A and 7B). Consistent with an unstructured Nbs1 C-terminus, the spNbs1-ΔAT Kratky plot is intermediate between parabolic and asymptotic curves, while spNbs1-fc has a parabolic plot showing spNbs1-fc is folded consistent with proteolysis and crystal structures (Figure 7C).\nAlthough its C-terminus may undergo disorder-to-order transitions upon binding Mre11 and ATM, we do not see stable domains (>10 kDa) when Nbs1 is trypsin digested while in complex with Mre11 (Figure S9). Thus, C-terminal Mre11 and ATM interacting regions may be peptide interaction motifs, rather than globular domains.","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"19804755","version":2,"reference_html":"Nbs1 flexibly tethers Ctp1 and Mre11-Rad50 to coordinate DNA double-strand break processing and repair. <i> Williams RS, Dodson GE, Limbo O, Yamada Y, Williams JS, Guenther G, Classen S, Glover JN, Iwasaki H, Russell P, Tainer JA. </i> Cell, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":286,"region_id":"DP02839r003","start":275,"term_id":"IDPO:0000002","statement":[{"text":"Nbs1 cardinal features: fused, extended, FHA-BRCT(1)-BRCT(2) domains flexibly linked to C-terminal Mre11- and ATM-binding motifs. ","type":"Abstract"},{"text":"While no mention is specifically made in text, the region corresponds to a loop that contains a conserved phosphorylation site in both human and yeast Nbs1, and the site is validated in the human protein. both are exposed flexible loops in the structure","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"19804755","version":2,"reference_html":"Nbs1 flexibly tethers Ctp1 and Mre11-Rad50 to coordinate DNA double-strand break processing and repair. <i> Williams RS, Dodson GE, Limbo O, Yamada Y, Williams JS, Guenther G, Classen S, Glover JN, Iwasaki H, Russell P, Tainer JA. </i> Cell, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3HUE"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":553,"region_id":"DP02839r004","start":330,"term_id":"GO:0060090","statement":[{"text":"Tethering of Ctp1 to a flexible Nbs1 arm suggests a mechanism for restricting DNA end processing and homologous recombination activities of Sae2/Ctp1/CtIP to the immediate vicinity of DSBs","type":"Abstract"},{"text":"Nbs1 emerges as an extended, flexible binding nexus coordinating interactions between the Mre11-Rad50 core, the checkpoint kinase ATM/Tel1, and the DNA end-processing factor Ctp1.","type":"Introduction"},{"text":"Flexible Nbs1 molecular associations may accommodate large-scale MRN complex conformational changes, proposed to regulate ATM activation and dimer-to-monomer transitions","type":"Discussion"}],"curator_id":"lchemes","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"19804755","version":3,"reference_html":"Nbs1 flexibly tethers Ctp1 and Mre11-Rad50 to coordinate DNA double-strand break processing and repair. <i> Williams RS, Dodson GE, Limbo O, Yamada Y, Williams JS, Guenther G, Classen S, Glover JN, Iwasaki H, Russell P, Tainer JA. </i> Cell, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","cross_refs":[{"db":"PDB","id":"3HUE"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":531,"region_id":"DP02839r005","start":474,"term_id":"IDPO:0000002","statement":[{"text":"Figure S2 Legend: Shown are the chromatogram and the SDS–PAGE of fractions containing the Mre11–Nbs1 complex and free Nbs1. The elution volumes and sizes of proteins from a gel filtration standard (Bio–Rad) are noted on top of the chromatogram. ","type":"Supplementary material"},{"text":"The SDS-PAGE and SEC profiles shown in Figure S2 indicate that the fragment is disordered in isolation. It has an anomalous migration profile in SDS-PAGE and elutes as a peak of large Rh compared to its MW. The structures also show poor density in the complex with Mre11 at residues: 474-483 and 497-531","type":"Curator statement"},{"text":"Flexible Nbs1 molecular associations may accommodate large-scale MRN complex conformational changes, proposed to regulate ATM activation and dimer-to-monomer transitions","type":"Discussion"}],"curator_id":"lchemes","released":"2022_03","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"22705791","version":2,"reference_html":"Structure of Mre11-Nbs1 complex yields insights into ataxia-telangiectasia-like disease mutations and DNA damage signaling. <i> Schiller CB, Lammens K, Guerini I, Coordes B, Feldmann H, Schlauderer F, Möckel C, Schele A, Strässer K, Jackson SP, Hopfner KP. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007689","cross_refs":[{"db":"PDB","id":"4FBQ"},{"db":"PDB","id":"4FBK"},{"db":"PDB","id":"4FBW"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":526,"region_id":"DP02839r006","start":477,"term_id":"IDPO:0000011","statement":[{"text":"Two Nbs1 subunits stretch around the outside of the nuclease domains of Mre11, with one subunit additionally bridging and locking the Mre11 dimer via a highly conserved asymmetrical binding motif.","type":"Abstract"},{"text":"Two Nbs1mir molecules wrap around the outside of the two Mre11 phosphodiesterase domains, each binding in a highly extended conformation via a α–helix–β strand motif (Interaction region 1). However, one of the two Nbs1mir molecules additionally binds across the Mre11 dimer interface, forming a second interaction opposite the nuclease cleft (Interaction region 2) (Fig. 2a,b). Consequently, a highly conserved “NFKxFxK motif” (residues 518–526) from one Nbs1mir bridges both copies of the eukaryote–specific loop insertion in the Mre11 dimer.","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"22705791","version":2,"reference_html":"Structure of Mre11-Nbs1 complex yields insights into ataxia-telangiectasia-like disease mutations and DNA damage signaling. <i> Schiller CB, Lammens K, Guerini I, Coordes B, Feldmann H, Schlauderer F, Möckel C, Schele A, Strässer K, Jackson SP, Hopfner KP. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4FBQ"},{"db":"PDB","id":"4FBK"},{"db":"PDB","id":"4FBW"}],"term_name":"disorder to order","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":526,"region_id":"DP02839r007","start":477,"term_id":"GO:0005515","statement":[{"text":"Two Nbs1 subunits stretch around the outside of the nuclease domains of Mre11, with one subunit additionally bridging and locking the Mre11 dimer via a highly conserved asymmetrical binding motif.","type":"Abstract"},{"text":"Two Nbs1mir molecules wrap around the outside of the two Mre11 phosphodiesterase domains, each binding in a highly extended conformation via a α–helix–β strand motif (Interaction region 1). However, one of the two Nbs1mir molecules additionally binds across the Mre11 dimer interface, forming a second interaction opposite the nuclease cleft (Interaction region 2) (Fig. 2a,b). Consequently, a highly conserved “NFKxFxK motif” (residues 518–526) from one Nbs1mir bridges both copies of the eukaryote–specific loop insertion in the Mre11 dimer.","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"22705791","version":3,"reference_html":"Structure of Mre11-Nbs1 complex yields insights into ataxia-telangiectasia-like disease mutations and DNA damage signaling. <i> Schiller CB, Lammens K, Guerini I, Coordes B, Feldmann H, Schlauderer F, Möckel C, Schele A, Strässer K, Jackson SP, Hopfner KP. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4FBQ"},{"db":"PDB","id":"4FBK"},{"db":"PDB","id":"4FBW"}],"term_name":"protein binding","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":526,"region_id":"DP02839r008","start":477,"term_id":"GO:0060090","statement":[{"text":"Two Nbs1 subunits stretch around the outside of the nuclease domains of Mre11, with one subunit additionally bridging and locking the Mre11 dimer via a highly conserved asymmetrical binding motif.","type":"Abstract"},{"text":"Two Nbs1mir molecules wrap around the outside of the two Mre11 phosphodiesterase domains, each binding in a highly extended conformation via a α–helix–β strand motif (Interaction region 1). However, one of the two Nbs1mir molecules additionally binds across the Mre11 dimer interface, forming a second interaction opposite the nuclease cleft (Interaction region 2) (Fig. 2a,b). Consequently, a highly conserved “NFKxFxK motif” (residues 518–526) from one Nbs1mir bridges both copies of the eukaryote–specific loop insertion in the Mre11 dimer.","type":"Results"},{"text":"While the mechanistic link between Rad50 and DNA binding to Mre11 requires further studies, our data suggest that Mre11 dimer flexibility and its control by Nbs1 could be an important part of MRN function.","type":"Discussion"}],"curator_id":"lchemes","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"22705791","version":3,"reference_html":"Structure of Mre11-Nbs1 complex yields insights into ataxia-telangiectasia-like disease mutations and DNA damage signaling. <i> Schiller CB, Lammens K, Guerini I, Coordes B, Feldmann H, Schlauderer F, Möckel C, Schele A, Strässer K, Jackson SP, Hopfner KP. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4FBQ"},{"db":"PDB","id":"4FBK"},{"db":"PDB","id":"4FBW"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":284812,"disprot_id":"DP02839","date":"2020-04-29T15:24:09.849Z","organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","regions_counter":8,"name":"DNA repair and telomere maintenance protein nbs1","dataset":[],"UniParc":"UPI00001620EC","uniref100":"UniRef100_O43070","uniref90":"UniRef90_O43070","uniref50":"UniRef50_O43070","genes":[{"name":{"value":"nbs1"},"orfNames":[{"value":"SPBC6B1.09c"}]}],"alphafold_very_low_content":0.2838499184339315,"disorder_content":0.38499184339314846,"disprot_consensus":{"full":[{"start":275,"end":286,"type":"D"},{"start":330,"end":476,"type":"D"},{"start":477,"end":526,"type":"T"},{"start":527,"end":553,"type":"D"}],"Structural state":[{"start":275,"end":286,"type":"D"},{"start":330,"end":553,"type":"D"}],"Molecular function":[{"start":330,"end":553,"type":"F"}],"Structural transition":[{"start":477,"end":526,"type":"T"}]}},{"acc":"O60934","features":{"gene3D":[{"start":111,"end":189,"id":"G3DSA:3.40.50.10190","name":"BRCT domain"},{"start":211,"end":326,"id":"G3DSA:3.40.50.10980","name":"G3DSA:3.40.50.10980"}],"pfam":[{"id":"PF00498","name":"FHA domain","start":24,"end":100},{"id":"PF00533","name":"BRCA1 C Terminus (BRCT) domain","start":116,"end":179},{"id":"PF08599","name":"DNA damage repair protein Nbs1","start":683,"end":746},{"id":"PF16508","name":"Second BRCT domain on Nijmegen syndrome breakage protein","start":216,"end":325}]},"creator":"lchemes","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MWKLLPAAGPAGGEPYRLLTGVEYVVGRKNCAILIENDQSISRNHAVLTANFSVTNLSQTDEIPVLTLKDNSKYGTFVNEEKMQNGFSRTLKSGDGITFGVFGSKFRIEYEPLVACSSCLDVSGKTALNQAILQLGGFTVNNWTEECTHLVMVSVKVTIKTICALICGRPIVKPEYFTEFLKAVESKKQPPQIESFYPPLDEPSIGSKNVDLSGRQERKQIFKGKTFIFLNAKQHKKLSSAVVFGGGEARLITEENEEEHNFFLAPGTCVVDTGITNSQTLIPDCQKKWIQSIMDMLQRQGLRPIPEAEIGLAVIFMTTKNYCDPQGHPSTGLKTTTPGPSLSQGVSVDEKLMPSAPVNTTTYVADTESEQADTWDLSERPKEIKVSKMEQKFRMLSQDAPTVKESCKTSSNNNSMVSNTLAKMRIPNYQLSPTKLPSINKSKDRASQQQQTNSIRNYFQPSTKKRERDEENQEMSSCKSARIETSCSLLEQTQPATPSLWKNKEQHLSENEPVDTNSDNNLFTDTDLKSIVKNSASKSHAAEKLRSNKKREMDDVAIEDEVLEQLFKDTKPELEIDVKVQKQEEDVNVRKRPRMDIETNDTFSDEAVPESSKISQENEIGKKRELKEDSLWSAKEISNNDKLQDDSEMLPKKLLLTEFRSLVIKNSTSRNPSGINDDYGQLKNFKKFKKVTYPGAGKLPHIIGGSDLIAHHARKNTELEEWLRQEMEVQNQHAKEESLADDLFRYNPYLKRRR","length":754,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":295,"region_id":"DP02840r002","start":272,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Yet, structure-based sequence alignments show an insertion missing in the spNbs1-fc model corresponds to an α-helix usually found between the third and fourth BRCT domain β-strands (β17 and β18 of BRCT2), that is linked to an hNbs1 Ser278 phosphorylation site loop (human Nbs1 residues 272–295) (Figure S3). To model these missing regions of hNbs1-fc, we generated 100 hNbs1-fc models based on the spNbs1 structure using MODELLER, and evaluated models by fit to the SAXS data. This approach identified 12 models with superior χ2 fits (χ2<1.3, best model χ2=1.25) that all bear extended accessible pSer278 loop conformations (Figures 2B and 2C). Thus, the overall spNbs1-fc fold is maintained in hNbs1-fc, but is decorated with a solvent-accessible phosphorylated loop. ","type":"Results"},{"text":"(C) Superposition of 12 homology hNbs1 models with SAXS scattering χ2 fits better than 1.3. ATM Phosphorylation sites in hNbs1 map to surface accessible loops with observed conformational variability between models. Ser278 phosphorylation could mediate auto-regulatory BRCT peptide binding in cis through an interaction with the phosphoprotein-binding cleft.","type":"Figure"},{"text":"The flexible region includes pSer278 which is a validated site","type":"Curator statement"}],"curator_id":"vnugnes","released":"2023_06","ec_name":"small-angle X-ray scattering evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"19804755","version":3,"reference_html":"Nbs1 flexibly tethers Ctp1 and Mre11-Rad50 to coordinate DNA double-strand break processing and repair. <i> Williams RS, Dodson GE, Limbo O, Yamada Y, Williams JS, Guenther G, Classen S, Glover JN, Iwasaki H, Russell P, Tainer JA. </i> Cell, 2009","date":"2023-06-21T10:02:10.168Z","reference_source":"pmid","ec_id":"ECO:0006210","term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":280,"region_id":"DP02840r003","start":276,"term_id":"IDPO:0000045","unpublished":true,"statement":[{"text":"Here we show that phosphorylation of NBS1, induced by ionizing radiation, requires catalytically active ATM. Complexes containing ATM and NBS1 exist in vivo in both untreated cells and cells treated with ionizing radiation. We have identified two residues of NBS1, Ser 278 and Ser 343 that are phosphorylated in vitro by ATM and whose modification in vivo is essential for the cellular response to DNA damage.","type":"Abstract"},{"text":"To determine whether Ser 278 and Ser 343 of NBS1 are phosphorylated in vivo, NBS1-LBI, a T-antigen immortalized NBS cell line established from a patient carrying the common founder mutation 657del5 (ref. 23) in NBS1, was transfected with plasmids encoding wild-type NBS1 (pCMV-NBS1wt); NBS1S278A (pCMV–NBS1S278A), NBS1S343A (pCMV–NBS1S343A) or NBS1S278A/S343A (pCMV–NBS1S278A/S343A).","type":"Results"},{"text":"Upon treatment with ionizing radiation, the mobility of NBS1wt, but not NBS1S278A, NBS1S343A or NBS1S278A/S343A, was altered ( Fig. 3b, compare lanes 5 and 6 with lanes 3 and 4 and 7–10). These data indicate that Ser 278 and Ser 343 are phosphorylated in vivo.","type":"Results"},{"text":"The pSer278 site is phosphorylated by ATM","type":"Curator statement"}],"curator_id":"vnugnes","released":"2023_06","ec_name":"protein kinase assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"10839544","version":3,"reference_html":"Functional link between ataxia-telangiectasia and Nijmegen breakage syndrome gene products. <i> Zhao S, Weng YC, Yuan SS, Lin YT, Hsu HC, Lin SC, Gerbino E, Song MH, Zdzienicka MZ, Gatti RA, Shay JW, Ziv Y, Shiloh Y, Lee EY. </i> Nature, 2000","date":"2023-06-21T10:03:33.751Z","reference_source":"pmid","ec_id":"ECO:0007687","term_name":"phosphorylation display site","curator_orcid":"0000-0001-8399-7907","ec_go":"IDA","disprot_namespace":"Disorder function"},{"start":335,"end":392,"reference_id":"19804755","reference_source":"pmid","reference_html":"Nbs1 flexibly tethers Ctp1 and Mre11-Rad50 to coordinate DNA double-strand break processing and repair. <i> Williams RS, Dodson GE, Limbo O, Yamada Y, Williams JS, Guenther G, Classen S, Glover JN, Iwasaki H, Russell P, Tainer JA. </i> Cell, 2009","date":"2023-05-15T16:14:16.902Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP02840r004","statement":[{"text":"To better understand NBS mutations, we analyzed the human Nbs1-fc structure with SAXS and proteolysis. Human Nbs1 (hNbs1) forms a trypsin-stable composite FHA-BRCT1-BRCT2 core (hNbs1-fc, residues 1-334) similar to spNbs1-fc (Figure 2A)","type":"Results"},{"text":"(A) Trypsin degradation produces a stable hNbs1 folded core (hNbs1-fc, residues 1-334).","type":"Figure"}]}],"released":"2022_06","ncbi_taxon_id":9606,"disprot_id":"DP02840","date":"2020-04-29T17:54:21.968Z","organism":"Homo sapiens","regions_counter":4,"name":"Nibrin","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI0000073BF4","uniref100":"UniRef100_O60934","uniref90":"UniRef90_O60934","uniref50":"UniRef50_O60934","genes":[{"name":{"value":"NBN"},"synonyms":[{"value":"NBS"},{"value":"NBS1"},{"value":"P95"}]}],"alphafold_very_low_content":0.4403183023872679,"disorder_content":0.10875331564986737,"disprot_consensus":{"full":[{"start":272,"end":295,"type":"D"},{"start":335,"end":392,"type":"D"}],"Structural state":[{"start":272,"end":295,"type":"D"},{"start":335,"end":392,"type":"D"}],"Disorder function":[{"start":276,"end":280,"type":"F"}]}},{"acc":"Q09683","features":{"gene3D":[{"start":5,"end":310,"id":"G3DSA:3.60.21.10","name":"G3DSA:3.60.21.10"},{"start":311,"end":419,"id":"G3DSA:3.30.110.110","name":"G3DSA:3.30.110.110"}],"pfam":[{"id":"PF00149","name":"Calcineurin-like phosphoesterase","start":18,"end":254},{"id":"PF04152","name":"Mre11 DNA-binding presumed domain","start":299,"end":467}]},"creator":"lchemes","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"sequence":"MPNDPSDMNNELHNENTIRILISSDPHVGYGEKDPVRGNDSFVSFNEILEIARERDVDMILLGGDIFHDNKPSRKALYQALRSLRLNCLGDKPCELELLSDTSLTTGDTAVCNINYLDPNINVAIPVFSIHGNHDDPSGDGRYSALDILQVTGLVNYFGRVPENDNIVVSPILLQKGFTKLALYGISNVRDERLYHSFRENKVKFLRPDLYRDEWFNLLTVHQNHSAHTPTSYLPESFIQDFYDFVLWGHEHECLIDGSYNPTQKFTVVQPGSTIATSLSPGETAPKHCGILNITGKDFHLEKIRLRTVRPFIMKDIILSEVSSIPPMVENKKEVLTYLISKVEEAITEANAQWYEAQGTVPVVENEKPPLPLIRLRVDYTGGYQTENPQRFSNRFVGRVANATDVVQFYLKKKYTRSKRNDGLYTSAVEDIKINSLRVESLVNEYLKTNRLECLPEDSLGEAVVNFVEKDDRDAIKECVETQLNKQINLLVKKRVTEENLEQEISSIINDLPKISTTKRKDYEELPEEVSETSINIAEHTPVLKHTSSLLDHHSPLATSSSEHEMEATPSPALLKKTNKRRELPSSLTKKNTRTPQRSKEVKKVPARKLSQSTKKSDKNTQSTLLFYDPSSTTEAQYLDNEDDEILDD","length":649,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":116,"region_id":"DP02842r001","start":101,"term_id":"IDPO:0000002","statement":[{"text":"Binding of the NFKxFxK motif at the Mre11 dimer interface is mediated by the eukaryote–specific insertion loops (one from each Mre11 protomer). As a result, these loops undergo a substantial structural change and a disorder to order transition, leading us to name these as “latching loops”. ","type":"Results"},{"text":"In the free state Mre11, residues 101-116 from the \"latching loop\" are disordered","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"22705791","version":2,"reference_html":"Structure of Mre11-Nbs1 complex yields insights into ataxia-telangiectasia-like disease mutations and DNA damage signaling. <i> Schiller CB, Lammens K, Guerini I, Coordes B, Feldmann H, Schlauderer F, Möckel C, Schele A, Strässer K, Jackson SP, Hopfner KP. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4FCX"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":116,"region_id":"DP02842r002","start":101,"term_id":"IDPO:0000011","statement":[{"text":"Binding of the NFKxFxK motif at the Mre11 dimer interface is mediated by the eukaryote–specific insertion loops (one from each Mre11 protomer). As a result, these loops undergo a substantial structural change and a disorder to order transition, leading us to name these as “latching loops”. \nThe second part, unique to eukaryotic Mre11, comprises the latching loops that interact with each other via an extended loop in the presence (but not absence) of Nbs1. As seen from the structures of Nbs1mir–Mre11cd and apo–Mre11cd, Nbs1 induces a disorder–to–order transition and geometric rearrangement of the latching loops (Fig. 4b–d), flipping them almost 180° towards the basal phosphodiesterase core.","type":"Results"},{"text":"In the free state Mre11 (4FCX), residues 101-116 from the \"latching loop\" are disordered. In the complex (4FBQ), only residues 103-108 remain disordered","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"22705791","version":2,"reference_html":"Structure of Mre11-Nbs1 complex yields insights into ataxia-telangiectasia-like disease mutations and DNA damage signaling. <i> Schiller CB, Lammens K, Guerini I, Coordes B, Feldmann H, Schlauderer F, Möckel C, Schele A, Strässer K, Jackson SP, Hopfner KP. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4FCX"},{"db":"PDB","id":"4FBQ"}],"term_name":"disorder to order","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":116,"region_id":"DP02842r003","start":101,"term_id":"GO:0098772","statement":[{"text":"Binding of the NFKxFxK motif at the Mre11 dimer interface is mediated by the eukaryote–specific insertion loops (one from each Mre11 protomer). As a result, these loops undergo a substantial structural change and a disorder to order transition, leading us to name these as “latching loops”. \nThe second part, unique to eukaryotic Mre11, comprises the latching loops that interact with each other via an extended loop in the presence (but not absence) of Nbs1. As seen from the structures of Nbs1mir–Mre11cd and apo–Mre11cd, Nbs1 induces a disorder–to–order transition and geometric rearrangement of the latching loops (Fig. 4b–d), flipping them almost 180° towards the basal phosphodiesterase core.","type":"Results"},{"text":"In the free state Mre11 (4FCX), residues 101-116 from the \"latching loop\" are disordered. In the complex (4FBQ), only residues 103-108 remain disordered","type":"Curator statement"},{"text":"In contrast, our data suggest that telomere maintenance depends on a stable interaction between the NFKxFxK motif of Xrs2/Nbs1 and the latching loops of Mre11 [...] The asymmetric bridging of Mre11 dimers by a single Nbs1 subunit, paired with the uncovered intrinsic flexibility of the eukaryotic Mre11 dimer, is perhaps the most significant and unexpected finding of our structural and functional analyses. ","type":"Discussion"}],"curator_id":"lchemes","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"22705791","version":3,"reference_html":"Structure of Mre11-Nbs1 complex yields insights into ataxia-telangiectasia-like disease mutations and DNA damage signaling. <i> Schiller CB, Lammens K, Guerini I, Coordes B, Feldmann H, Schlauderer F, Möckel C, Schele A, Strässer K, Jackson SP, Hopfner KP. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4FCX"},{"db":"PDB","id":"4FBQ"}],"term_name":"molecular function regulator","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":284812,"disprot_id":"DP02842","date":"2020-04-30T01:14:42.176Z","organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","regions_counter":3,"name":"DNA repair protein rad32","dataset":[],"UniParc":"UPI0000133025","uniref100":"UniRef100_Q09683","uniref90":"UniRef90_Q09683","uniref50":"UniRef50_Q09683","genes":[{"name":{"value":"rad32"},"orfNames":[{"value":"SPAC13C5.07"}]}],"alphafold_very_low_content":0.26348228043143296,"disorder_content":0.02465331278890601,"disprot_consensus":{"full":[{"start":101,"end":116,"type":"T"}],"Structural state":[{"start":101,"end":116,"type":"D"}],"Structural transition":[{"start":101,"end":116,"type":"T"}],"Molecular function":[{"start":101,"end":116,"type":"F"}]}},{"acc":"P47110","features":{"pfam":[]},"creator":"lchemes","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"sequence":"MDQKASYFINEKLFTEVKPVLFTDLIHHLKIGPSMAKKLMFDYYKQTTNAKYNCVVICCYKDQTIKIIHDLSNIPQQDSIIDCFIYAFNPMDSFIPYYDIIDQKDCLTIKNSYELKVSESSKIIERTKTLEEKSKPLVRPTARSKTTPEETTGRKSKSKDMGLRSTALLAKMKKDRDDKETSRQNELRKRKEENLQKINKQNPEREAQMKELNNLFVEDDLDTEEVNGGSKPNSPKETDSNDKDKNNDDLEDLLETTAEDSLMDVPKIQQTKPSETEHSKEPKSEEEPSSFIDEDGYIVTKRPATSTPPRKPSPVVKRALSSSKKQETPSSNKRLKKQGTLESFFKRKAK","length":350,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":350,"region_id":"DP02847r001","start":117,"term_id":"IDPO:0000002","statement":[{"text":"Pol32C harboring the C-terminus PIP motif is disordered, but the spatial position of Pol32N is such that it would allow for the PIP motif of Pol32C to extend to the downstream portion of the DNA duplex for interactions with PCNA (Fig. 1a and Supplementary Fig. 3).","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"31582849","version":2,"reference_html":"Cryo-EM structure and dynamics of eukaryotic DNA polymerase δ holoenzyme. <i> Jain R, Rice WJ, Malik R, Johnson RE, Prakash L, Prakash S, Ubarretxena-Belandia I, Aggarwal AK. </i> Nat Struct Mol Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6P1H"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":345,"region_id":"DP02847r002","start":337,"term_id":"GO:0005515","statement":[{"text":"To analyze the roles of PIP motifs individually, we purified Polδ complexes that carry either (1) the F1002A, I1003A mutations in the Pol3 PIP, (2) the Y327A, F328A mutations in the Pol31 PIP, or (3) where the PIP of Pol32 had been inactivated by deleting C-terminal residues 337–350 of the protein (1–336) or by changing the conserved F344, F345 residues to alanines (Fig. 3B). As shown in Fig. 3C, Polδ harboring a mutation in the Pol3 PIP (lane 5) or lacking the Pol32 PIP (lane 9) exhibits a reduction in PCNA-stimulated DNA synthesis and the formation of fully extended product was impaired by these mutations, similar to that observed for mutations in the Pol31 PIP (lane 7). Thus PCNA binding motifs in all three subunits affect Polδ’s ability to synthesize DNA with PCNA, and they all appear to affect it to about the same degree.","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"experimental phenotypic evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"22003126","version":3,"reference_html":"PCNA binding domains in all three subunits of yeast DNA polymerase δ modulate its function in DNA replication. <i> Acharya N, Klassen R, Johnson RE, Prakash L, Prakash S. </i> Proc Natl Acad Sci U S A, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007634","term_name":"protein binding","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":345,"region_id":"DP02847r003","start":337,"term_id":"GO:0098772","statement":[{"text":"To analyze the roles of PIP motifs individually, we purified Polδ complexes that carry either (1) the F1002A, I1003A mutations in the Pol3 PIP, (2) the Y327A, F328A mutations in the Pol31 PIP, or (3) where the PIP of Pol32 had been inactivated by deleting C-terminal residues 337–350 of the protein (1–336) or by changing the conserved F344, F345 residues to alanines (Fig. 3B). As shown in Fig. 3C, Polδ harboring a mutation in the Pol3 PIP (lane 5) or lacking the Pol32 PIP (lane 9) exhibits a reduction in PCNA-stimulated DNA synthesis and the formation of fully extended product was impaired by these mutations, similar to that observed for mutations in the Pol31 PIP (lane 7). Thus PCNA binding motifs in all three subunits affect Polδ’s ability to synthesize DNA with PCNA, and they all appear to affect it to about the same degree.","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"experimental phenotypic evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"22003126","version":3,"reference_html":"PCNA binding domains in all three subunits of yeast DNA polymerase δ modulate its function in DNA replication. <i> Acharya N, Klassen R, Johnson RE, Prakash L, Prakash S. </i> Proc Natl Acad Sci U S A, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007634","term_name":"molecular function regulator","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":345,"region_id":"DP02847r004","start":337,"term_id":"GO:0098772","statement":[{"text":"This is a PCNA interacting PIP Box motif\n","type":"Curator statement"},{"text":"The observed defects in mutagenesis were less severe with pol32– 10, a C-terminal 7 aa truncation (F344FKRKAK), than with the internal deletion mutant pol32–9 deleting aa 310–343 which include QGTLES343 of the motif, suggesting the existence of residual interactions between Pol32–10 and PCNA in vivo.\n\n","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"mutant phenotype evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"14594808","version":3,"reference_html":"The Pol32 subunit of DNA polymerase delta contains separable domains for processive replication and proliferating cell nuclear antigen (PCNA) binding. <i> Johansson E, Garg P, Burgers PM. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000315","term_name":"molecular function regulator","curator_orcid":"0000-0003-0192-9906","ec_go":"IMP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":559292,"disprot_id":"DP02847","date":"2020-04-30T20:56:53.166Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":4,"name":"DNA polymerase delta subunit 3","dataset":[],"UniParc":"UPI0000129740","uniref100":"UniRef100_P47110","uniref90":"UniRef90_P47110","uniref50":"UniRef50_P47110","genes":[{"name":{"value":"POL32"},"orfNames":[{"value":"J1626"}],"olnNames":[{"value":"YJR043C"}]}],"alphafold_very_low_content":0.26,"disorder_content":0.6685714285714286,"disprot_consensus":{"full":[{"start":117,"end":350,"type":"D"}],"Structural state":[{"start":117,"end":350,"type":"D"}],"Molecular function":[{"start":337,"end":345,"type":"F"}]}},{"acc":"P15436","features":{"gene3D":[{"start":586,"end":817,"id":"G3DSA:3.90.1600.10","name":"Palm domain of DNA polymerase"},{"start":316,"end":544,"id":"G3DSA:3.30.420.10","name":"Ribonuclease H-like superfamily/Ribonuclease H"},{"start":834,"end":985,"id":"G3DSA:1.10.132.60","name":"G3DSA:1.10.132.60"}],"pfam":[{"id":"PF00136","name":"DNA polymerase family B","start":546,"end":973},{"id":"PF03104","name":"DNA polymerase family B, exonuclease domain","start":248,"end":482},{"id":"PF14260","name":"C4-type zinc-finger of DNA polymerase delta","start":1009,"end":1080},{"id":"PF24055","name":"DNA polymerase delta catalytic subunit-like, N-terminal domain","start":159,"end":225}]},"creator":"lchemes","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"sequence":"MSEKRSLPMVDVKIDDEDTPQLEKKIKRQSIDHGVGSEPVSTIEIIPSDSFRKYNSQGFKAKDTDLMGTQLESTFEQELSQMEHDMADQEEHDLSSFERKKLPTDFDPSLYDISFQQIDAEQSVLNGIKDENTSTVVRFFGVTSEGHSVLCNVTGFKNYLYVPAPNSSDANDQEQINKFVHYLNETFDHAIDSIEVVSKQSIWGYSGDTKLPFWKIYVTYPHMVNKLRTAFERGHLSFNSWFSNGTTTYDNIAYTLRLMVDCGIVGMSWITLPKGKYSMIEPNNRVSSCQLEVSINYRNLIAHPAEGDWSHTAPLRIMSFDIECAGRIGVFPEPEYDPVIQIANVVSIAGAKKPFIRNVFTLNTCSPITGSMIFSHATEEEMLSNWRNFIIKVDPDVIIGYNTTNFDIPYLLNRAKALKVNDFPYFGRLKTVKQEIKESVFSSKAYGTRETKNVNIDGRLQLDLLQFIQREYKLRSYTLNAVSAHFLGEQKEDVHYSIISDLQNGDSETRRRLAVYCLKDAYLPLRLMEKLMALVNYTEMARVTGVPFSYLLARGQQIKVVSQLFRKCLEIDTVIPNMQSQASDDQYEGATVIEPIRGYYDVPIATLDFNSLYPSIMMAHNLCYTTLCNKATVERLNLKIDEDYVITPNGDYFVTTKRRRGILPIILDELISARKRAKKDLRDEKDPFKRDVLNGRQLALKISANSVYGFTGATVGKLPCLAISSSVTAYGRTMILKTKTAVQEKYCIKNGYKHDAVVVYGDTDSVMVKFGTTDLKEAMDLGTEAAKYVSTLFKHPINLEFEKAYFPYLLINKKRYAGLFWTNPDKFDKLDQKGLASVRRDSCSLVSIVMNKVLKKILIERNVDGALAFVRETINDILHNRVDISKLIISKTLAPNYTNPQPHAVLAERMKRREGVGPNVGDRVDYVIIGGNDKLYNRAEDPLFVLENNIQVDSRYYLTNQLQNPIISIVAPIIGDKQANGMFVVKSIKINTGSQKGGLMSFIKKVEACKSCKGPLRKGEGPLCSNCLARSGELYIKALYDVRDLEEKYSRLWTQCQRCAGNLHSEVLCSNKNCDIFYMRVKVKKELQEKVEQLSKW","length":1097,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1051,"region_id":"DP02848r001","start":1007,"term_id":"IDPO:0000002","statement":[{"text":"Polδ CysAD is disordered, suggestive of a flexible region that may only become ordered when it interacts with other components of the replication fork, including PCNA18 (Supplementary Fig. 3)[...]The paucity of interactions between the catalytic and regulatory modules behooves a relatively flexible complex able to accommodate changes in DNA direction. In a previous low resolution SAXS analysis of the Polδ holoenzyme in the absence of DNA, we observed significant flexibility between the catalytic and regulatory modules35. From the current cryo-EM analysis, flexibility between the modules appears to be a feature even when Polδ is complexed to DNA. ","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"31582849","version":2,"reference_html":"Cryo-EM structure and dynamics of eukaryotic DNA polymerase δ holoenzyme. <i> Jain R, Rice WJ, Malik R, Johnson RE, Prakash L, Prakash S, Ubarretxena-Belandia I, Aggarwal AK. </i> Nat Struct Mol Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6P1H"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1051,"region_id":"DP02848r002","start":1007,"term_id":"GO:0060090","statement":[{"text":"Polδ CysAD is disordered, suggestive of a flexible region that may only become ordered when it interacts with other components of the replication fork, including PCNA18 (Supplementary Fig. 3)[...]The paucity of interactions between the catalytic and regulatory modules behooves a relatively flexible complex able to accommodate changes in DNA direction. In a previous low resolution SAXS analysis of the Polδ holoenzyme in the absence of DNA, we observed significant flexibility between the catalytic and regulatory modules35. From the current cryo-EM analysis, flexibility between the modules appears to be a feature even when Polδ is complexed to DNA. ","type":"Results"},{"text":"From the structure, the interface between the catalytic and regulatory modules is relatively sparse and suggestive of a relatively flexible complex able to accommodate changes in DNA direction.\n\nFlexibility between the regulatory and catalytic modules, coupled with the proximity of the regulatory module to the exo and thumb domains, appears to be important for the 3′→5′ exonuclease activity of Polδ\n\nLocal flexibility between the catalytic and regulatory modules may also facilitate the binding of various DNA substrates in these diverse pathways.\n\n","type":"Discussion"}],"curator_id":"lchemes","released":"2022_03","ec_name":"cryogenic electron microscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"31582849","version":3,"reference_html":"Cryo-EM structure and dynamics of eukaryotic DNA polymerase δ holoenzyme. <i> Jain R, Rice WJ, Malik R, Johnson RE, Prakash L, Prakash S, Ubarretxena-Belandia I, Aggarwal AK. </i> Nat Struct Mol Biol, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","cross_refs":[{"db":"PDB","id":"6P1H"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0003-0192-9906","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":559292,"disprot_id":"DP02848","date":"2020-05-01T00:59:42.423Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":2,"name":"DNA polymerase delta catalytic subunit","dataset":[],"UniParc":"UPI0000168B4F","uniref100":"UniRef100_P15436","uniref90":"UniRef90_P15436","uniref50":"UniRef50_P15436","genes":[{"name":{"value":"POL3"},"synonyms":[{"value":"CDC2"},{"value":"TEX1"}],"orfNames":[{"value":"D2366"}],"olnNames":[{"value":"YDL102W"}]}],"alphafold_very_low_content":0.07474931631722881,"disorder_content":0.04102096627164995,"disprot_consensus":{"full":[{"start":1007,"end":1051,"type":"D"}],"Structural state":[{"start":1007,"end":1051,"type":"D"}],"Molecular function":[{"start":1007,"end":1051,"type":"F"}]}},{"acc":"O43521","features":{"gene3D":[],"pfam":[{"id":"PF06773","name":"Bim protein N-terminus","start":4,"end":40},{"id":"PF08945","name":"Bcl-x interacting, BH3 domain","start":136,"end":166}]},"creator":"bjuhasz","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MAKQPSDVSSECDREGRQLQPAERPPQLRPGAPTSLQTEPQGNPEGNHGGEGDSCPHGSPQGPLAPPASPGPFATRSPLFIFMRRSSLLSRSSSGYFSFDTDRSPAPMSCDKSTQTPSPPCQAFNHYLSAMASMRQAEPADMRPEIWIAQELRRIGDEFNAYYARRVFLNNYQAAEDHPRMVILRLLRYIVRLVWRMH","length":198,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":41,"region_id":"DP02849r001","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets","type":"Title"},{"text":"We show, using spectroscopic methods, that the BH3-only proteins Bim, Bad and Bmf are unstructured in the absence of binding partners. Detailed sequence analyses are consistent with this observation and suggest that most BH3-only proteins are unstructured","type":"Abstract"},{"text":"The CD spectra obtained for BimLDC27 over the range 5–651C is characteristic of an unstructured protein, although the slight inflection near 222nm may indicate some residual a-helical structure","type":"Results"}],"curator_id":"lchemes","released":"2023_12","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"16645638","version":2,"reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:25:26.098Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":41,"region_id":"DP02849r002","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets","type":"Title"},{"text":"We show, using spectroscopic methods, that the BH3-only proteins Bim, Bad and Bmf are unstructured in the absence of binding partners. Detailed sequence analyses are consistent with this observation and suggest that most BH3-only proteins are unstructured","type":"Abstract"},{"text":"Analysis of NMR spectra for BimLDC27 support this conclusion (Figure 2c). In the 1H-15N-HSQC spectrum (Figure 2c), the backbone amide resonances fall between 8.0 and 8.5 p.p.m., and there is little dispersion in the aliphatic region in the 1D 1H NMR spectrum (data not shown). The sharp resonances and lack of chemical shift dispersion reflect the intrinsic mobility and lack of long-range order in BimLDC27. The absence of stable tertiary structure is supported by the complete absence of any HN–HN cross peaks in both proton 2D NOESY and a three-dimensional (3D) 15N-NOESY spectra (data not shown). In heteronuclear\n{1H}15N, NOEs spectra, most of the resonances were of negative intensity (data not shown), indicating mobility on the ps–ns time scale, features typical of IUPs.28\n","type":"Results"}],"curator_id":"lchemes","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"16645638","version":2,"reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:25:24.609Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":41,"region_id":"DP02849r003","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets","type":"Title"},{"text":"We show, using spectroscopic methods, that the BH3-only proteins Bim, Bad and Bmf are unstructured in the absence of binding partners. Detailed sequence analyses are consistent with this observation and suggest that most BH3-only proteins are unstructured","type":"Abstract"},{"text":"\nDuring purification, BimLDC27 was observed to be highly protease sensitive and behaved as a larger protein, migrating in sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PAGE) as an approximately 16 kDa protein and eluting from gel filtration columns with an apparent molecular weight of B25 kDa (see Figure 3a). However, when analyzed by sedimentation\nvelocity centrifugation and evaluated in terms of a single class of noninteracting solute, a molecular mass (Mr) of 13.2 kDa was obtained (Figure 2a).\n","type":"Results"}],"curator_id":"lchemes","released":"2023_12","ec_name":"chromatography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"16645638","version":2,"reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:25:23.472Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":164,"region_id":"DP02849r004","start":97,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets","type":"Title"},{"text":"We show, using spectroscopic methods, that the BH3-only proteins Bim, Bad and Bmf are unstructured in the absence of binding partners. Detailed sequence analyses are consistent with this observation and suggest that most BH3-only proteins are unstructured","type":"Abstract"},{"text":"During purification, BimLDC27 was observed to be highly protease sensitive and behaved as a larger protein, migrating in sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PAGE) as an approximately 16 kDa protein and eluting from gel filtration columns with an apparent molecular weight of B25 kDa (see Figure 3a). However, when analyzed by sedimentation velocity centrifugation and evaluated in terms of a single class of noninteracting solute, a molecular mass (Mr) of 13.2 kDa was obtained (Figure 2a).\n","type":"Results"}],"curator_id":"lchemes","released":"2023_12","ec_name":"chromatography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"16645638","version":2,"reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:25:22.363Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":164,"region_id":"DP02849r005","start":97,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets","type":"Title"},{"text":"We show, using spectroscopic methods, that the BH3-only proteins Bim, Bad and Bmf are unstructured in the absence of binding partners. Detailed sequence analyses are consistent with this observation and suggest that most BH3-only proteins are unstructured","type":"Abstract"},{"text":"Analysis of NMR spectra for BimLDC27 support this conclusion (Figure 2c). In the 1H-15N-HSQC spectrum (Figure 2c), the backbone amide resonances fall between 8.0 and 8.5 p.p.m., and there is little dispersion in the aliphatic region in the 1D 1H NMR spectrum (data not shown). The sharp resonances and lack of chemical shift dispersion reflect the intrinsic mobility and lack of long-range order in BimLDC27. The absence of stable tertiary structure is supported by the complete absence of any HN–HN cross peaks in both proton 2D NOESY and a three-dimensional (3D) 15N-NOESY spectra (data not shown). In heteronuclear\n","type":"Results"}],"curator_id":"lchemes","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"16645638","version":2,"reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:25:21.482Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":164,"region_id":"DP02849r006","start":97,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets","type":"Title"},{"text":"We show, using spectroscopic methods, that the BH3-only proteins Bim, Bad and Bmf are unstructured in the absence of binding partners. Detailed sequence analyses are consistent with this observation and suggest that most BH3-only proteins are unstructured","type":"Abstract"},{"text":"\nThe CD spectra obtained for BimLDC27 over the range 5–651C is characteristic of an unstructured protein, although the slight inflection near 222nm may indicate some residual a-helical structure","type":"Results"}],"curator_id":"lchemes","released":"2023_12","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"16645638","version":2,"reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:25:20.314Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":164,"region_id":"DP02849r007","start":142,"term_id":"IDPO:0000011","unpublished":true,"statement":[{"text":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets","type":"Title"},{"text":"We show, using spectroscopic methods, that the BH3-only proteins Bim, Bad and Bmf are unstructured in the absence of binding partners. Detailed sequence analyses are consistent with this observation and suggest that most BH3-only proteins are unstructured. When Bim binds and inactivates prosurvival proteins, most residues remain disordered, only the BH3 element becomes structured, and the short ahelical molecular recognition element can be considered to behave as a ‘bead on a string’. Coupled folding and binding is typical of many IUPs that have important signaling roles, such as BH3-only proteins, as the inherent structural plasticity favors interaction with multiple targets.","type":"Abstract"},{"text":"Partial proteolysis experiments were used to further evaluate the conformational changes associated with complex formation. When treated with trypsin, BimLDC27 was rapidly degraded to small peptides (Figure 3b, lanes 3 and 4), whereas Bcl-w was relatively resistant although after 60 min digestion. When Bcl-wDC10 and BimLDC27 were mixed before trypsin digestion, a different proteolytic profile was obtained (Figure 3b, lanes 8 and 9). Mass spectrometry analysis of the peptide mixtures revealed changes consistent with complex formation […] The mass of the new peptide corresponds to that expected for a peptide derived from the C-terminus of BimLDC27 (sequence shown at the bottom of Figure 3b). This peptide includes the BH3 domain and suggests that interaction with the hydrophobic binding groove protects the BH3 domain and the hydrophobic groove of Bcl-w from proteolysis","type":"Results"},{"text":"The curator assigns the residues based on the known crystal structures","type":"Curator statement"}],"curator_id":"lchemes","released":"2023_12","ec_name":"cleavage assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"16645638","version":2,"reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:25:16.746Z","curator_name":"Federica Quaglia"},"term_name":"disorder to order","curator_orcid":"0000-0003-0192-9906","ec_go":"IDA","disprot_namespace":"Structural transition"},{"region_id":"DP02849r008","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:25:14.447Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":165,"term_id":"GO:0005515","start":143,"version":3,"statement":[{"text":"We report the crystal structure of human Mcl-1 bound to a BH3 peptide derived from human Bim and the structures for three complexes that accommodate large physicochemical changes at conserved Bim sites.","type":"Abstract"},{"text":"To provide a structural context for interpreting changes in binding, we solved the structure of human Mcl-1, consisting of residues corresponding to the Bcl-2 fold without the PEST or transmembrane domains, in complex with a peptide consisting of the BH3 region from human Bim. Single-wavelength anomolous diffraction (SAD) phasing using a selenomethionine derivative provided the native structure at a resolution of 2.0 Å, with an Rfree of 0.23. The model includes residues 172–197, 203–321 of Mcl-1, and 0–22 of Bim.","type":"Results"},{"text":"Residues 0-22  mentioned by the authors correspond to residues 143-165 of the uniprot entry","type":"Curator statement"}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2023_12","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"20066663","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3KJ0"},{"db":"PDB","id":"3KJ1"},{"db":"PDB","id":"3KJ2"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"lchemes","reference_html":"Mcl-1-Bim complexes accommodate surprising point mutations via minor structural changes. <i> Fire E, Gullá SV, Grant RA, Keating AE. </i> Protein Sci, 2010","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02849r009","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:25:12.780Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":165,"term_id":"GO:0098772","start":143,"version":3,"statement":[{"text":"We report the crystal structure of human Mcl-1 bound to a BH3 peptide derived from human Bim and the structures for three complexes that accommodate large physicochemical changes at conserved Bim sites.","type":"Abstract"},{"text":"To provide a structural context for interpreting changes in binding, we solved the structure of human Mcl-1, consisting of residues corresponding to the Bcl-2 fold without the PEST or transmembrane domains, in complex with a peptide consisting of the BH3 region from human Bim. Single-wavelength anomolous diffraction (SAD) phasing using a selenomethionine derivative provided the native structure at a resolution of 2.0 Å, with an Rfree of 0.23. The model includes residues 172–197, 203–321 of Mcl-1, and 0–22 of Bim.","type":"Results"},{"text":"Residues 0-22  mentioned by the authors correspond to residues 143-165 of the uniprot entry","type":"Curator statement"}],"term_name":"molecular function regulator","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2023_12","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"20066663","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3KJ0"},{"db":"PDB","id":"3KJ1"},{"db":"PDB","id":"3KJ2"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"lchemes","reference_html":"Mcl-1-Bim complexes accommodate surprising point mutations via minor structural changes. <i> Fire E, Gullá SV, Grant RA, Keating AE. </i> Protein Sci, 2010","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":165,"region_id":"DP02849r010","start":142,"term_id":"GO:0005515","unpublished":true,"statement":[{"text":"We report the crystal structure of human Mcl-1 bound to a BH3 peptide derived from human Bim and the structures for three complexes that accommodate large physicochemical changes at conserved Bim sites.","type":"Abstract"},{"text":"Fluorescence spectroscopy\nThe BH3 region of Bim has been used extensively for studies exploring the relationship between sequence, structure, and binding in the Bcl-2 family.23–25 This work focused on the analysis of two positions in Bim that have the potential to influence binding specificity. As defined in Table TableI,I, these are positions 2d (isoleucine) and 4a (phenylalanine). \n","type":"Results"},{"text":"Table I: Binding Affinity of Bim Peptides for Mcl-1 and Bcl-xL\nreveals the affinity of the wild type sequence is < 2nM for both Mcl-1 and Bcl-XL\n","type":"Table"}],"curator_id":"lchemes","released":"2023_12","ec_name":"experimental evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"20066663","version":3,"reference_html":"Mcl-1-Bim complexes accommodate surprising point mutations via minor structural changes. <i> Fire E, Gullá SV, Grant RA, Keating AE. </i> Protein Sci, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000269","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:25:13.515Z","curator_name":"Federica Quaglia"},"term_name":"protein binding","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":165,"region_id":"DP02849r011","start":141,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The study strategy is twofold: while BAX oligomerization was monitored through spectral changes of spin-labeled BAX, the binding kinetics was studied by observing time-dependent changes of spin-labeled BimBH3. Meanwhile, conformational transition between the unstructured and structured BimBH3 was measured. We show that helical propensity of the BimBH3 is increased upon binding to BAX but is then reduced after being released from the activated BAX;\n","type":"Abstract"},{"text":"BH3 domain of Bim is an IDP. […]From the spectra of circular dichroism (CD) spectroscopy, the studied peptides are largely disordered, having very low α- helicity relative to the CD spectrum of the BimBH3 in 90/10 (v/v) TFE/PB solvent (Fig. 1C). The CD result is consistent with the low predicted helicity (ca. 1 − 3%) of the peptides (Fig. 1D)","type":"Results"},{"text":"Legand Fig 1. (C) CD spectra of the BimBH3 mutants. BimBH3 and its mutants are largely disordered compared to BimBH3-C in 90/10 (v/v) TFE/PB buffer.\n","type":"Figure"}],"curator_id":"lchemes","released":"2023_12","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"26913490","version":2,"reference_html":"Evidence for an Induced-Fit Process Underlying the Activation of Apoptotic BAX by an Intrinsically Disordered BimBH3 Peptide. <i> Jhong SR, Li CY, Sung TC, Lan YJ, Chang KJ, Chiang YW. </i> J Phys Chem B, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:25:19.026Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":165,"region_id":"DP02849r012","start":141,"term_id":"IDPO:0000011","unpublished":true,"statement":[{"text":"Here we study the interaction of BAX with an intrinsically\ndisordered BH3 motif of Bim protein (BimBH3) using ESR techniques. Upon incubation with\nBAX, BimBH3 binds to BAX at helices 1/6 trigger site to initiate conformational changes of\nBAX, which in turn promotes the formation of BAX oligomers. Study strategy is two-fold: while\nBAX oligomerization was monitored through spectral changes of spin-labeled BAX, the binding\nkinetics was studied by observing time-dependent changes of spin-labeled BimBH3. Meanwhile,\nconformational transition between the unstructured and structured BimBH3 was measured. We\nshow that helical propensity of the BimBH3 is increased upon binding to BAX, but is then\nreduced after being released from the activated BAX;","type":"Introduction"},{"text":"This comparison indicates that the helicity of the peptides is not a prerequisite for the binding to BAX. Taken together, it suggests that BAX oligomerization can be initiated either by the binding of the structured BimBH3 (i.e., Bim SAHB) through a conformational selection mechanism or by the interaction of the unstructured BimBH3 through an induced-fit mechanism.\nSpecifically, the results from the present study i) reveal new insights into how the induced-fit reaction of an IDP triggers the oligomerization of BAX, ii) report BAX oligomerization can be initiated by BimBH3 through an induced-fit mechanism, and iii) provide a tool to design experiments that can discriminate between the different functional states of an IDP.\n","type":"Discussion"}],"curator_id":"lchemes","released":"2023_12","ec_name":"electron paramagnetic resonance evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"26913490","version":2,"reference_html":"Evidence for an Induced-Fit Process Underlying the Activation of Apoptotic BAX by an Intrinsically Disordered BimBH3 Peptide. <i> Jhong SR, Li CY, Sung TC, Lan YJ, Chang KJ, Chiang YW. </i> J Phys Chem B, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006287","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:25:15.460Z","curator_name":"Federica Quaglia"},"term_name":"disorder to order","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2023_12","ncbi_taxon_id":9606,"disprot_id":"DP02849","date":"2020-05-04T18:43:14.359Z","organism":"Homo sapiens","regions_counter":14,"name":"Bcl-2-like protein 11","dataset":[],"UniParc":"UPI0000033ABA","uniref100":"UniRef100_O43521","uniref90":"UniRef90_O43521","uniref50":"UniRef50_O43521","genes":[{"name":{"value":"BCL2L11"},"synonyms":[{"value":"BIM"}]}],"alphafold_very_low_content":0.36363636363636365,"disorder_content":0.5555555555555556,"disprot_consensus":{"full":[{"start":1,"end":41,"type":"D"},{"start":97,"end":140,"type":"D"},{"start":141,"end":165,"type":"T"}],"Structural state":[{"start":1,"end":41,"type":"D"},{"start":97,"end":165,"type":"D"}],"Structural transition":[{"start":141,"end":165,"type":"T"}],"Molecular function":[{"start":142,"end":165,"type":"F"}]}},{"acc":"O60239","features":{"gene3D":[],"pfam":[{"id":"PF05276","name":"SH3 domain-binding protein 5 (SH3BP5)","start":39,"end":266}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MDAALKRSRSEEPAEILPPARDEEEEEEEGMEQGLEEEEEVDPRIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELVKKIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLTLAKGEYKMALKNLEMISDEIHERRRSSAMGPRGCGVGAEGSSTSVEDLPGSKPEPDAISVASEAFEDDSCSNFVSEDDSETQSVSSFSSGPTSPSEMPDQFPAVVRPGSLDLPSPVSLSEFGMMFPVLGPRSECSGASSPECEVERGDRAEGAENKTSDKANNNRGLSSSSGSGGSSKSQSSTSPEGQALENRMKQLSLQCSKGRDGIIADIKMVQIG","length":455,"regions":[{"region_id":"DP02850r001","ec_ontology":"ECO","end":452,"term_id":"IDPO:0000002","start":266,"version":2,"statement":[{"text":"To define the dynamics of the full-length SH3BP5 protein, we used hydrogen deuterium exchange mass spectrometry (HDX-MS).","type":"Results"},{"text":"We carried out HDX experiments with a short pulse of deuterium exposure (3 s at 1 °C) for the full-length SH3BP5, with both the N terminus and C terminus of SH3BP5 having > 50% deuterium incorporation, indicating limited secondary structure (Supplementary Figure 3a). HDX-MS results were used to generate a crystal construct of SH3BP5, with all of the C-terminal disordered region removed (SH3BP5 1–265).","type":"Results"}],"term_name":"disorder","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30217979","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6DJL"}],"term_namespace":"Structural state","ec_id":"ECO:0006236","curator_id":"fquaglia","reference_html":"Structural determinants of Rab11 activation by the guanine nucleotide exchange factor SH3BP5. <i> Jenkins ML, Margaria JP, Stariha JTB, Hoffmann RM, McPhail JA, Hamelin DJ, Boulanger MJ, Hirsch E, Burke JE. </i> Nat Commun, 2018","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","ncbi_taxon_id":9606,"disprot_id":"DP02850","date":"2020-05-08T09:02:39.648Z","organism":"Homo sapiens","regions_counter":1,"name":"SH3 domain-binding protein 5","dataset":[],"UniParc":"UPI0000124ED9","uniref100":"UniRef100_O60239","uniref90":"UniRef90_O60239","uniref50":"UniRef50_O60239","genes":[{"name":{"value":"SH3BP5"},"synonyms":[{"value":"SAB"}]}],"alphafold_very_low_content":0.3516483516483517,"disorder_content":0.41098901098901097,"disprot_consensus":{"full":[{"start":266,"end":452,"type":"D"}],"Structural state":[{"start":266,"end":452,"type":"D"}]}},{"acc":"Q5FWF5","features":{"gene3D":[],"pfam":[{"id":"PF13878","name":"zinc-finger of acetyl-transferase ESCO","start":604,"end":643},{"id":"PF13880","name":"ESCO1/2 acetyl-transferase","start":763,"end":831}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MMSIQEKSKENSSKVTKKSDDKNSETEIQDSQKNLAKKSGPKETIKSQAKSSSESKINQPELETRMSTRSSKAASNDKATKSINKNTVTVRGYSQESTKKKLSQKKLVHENPKANEQLNRRSQRLQQLTEVSRRSLRSREIQGQVQAVKQSLPPTKKEQCSSTQSKSNKTSQKHVKRKVLEVKSDSKEDENLVINEVINSPKGKKRKVEHQTACACSSQCTQGSEKCPQKTTRRDETKPVPVTSEVKRSKMATSVVPKKNEMKKSVHTQVNTNTTLPKSPQPSVPEQSDNELEQAGKSKRGSILQLCEEIAGEIESDNVEVKKESSQMESVKEEKPTEIKLEETSVERQILHQKETNQDVQCNRFFPSRKTKPVKCILNGINSSAKKNSNWTKIKLSKFNSVQHNKLDSQVSPKLGLLRTSFSPPALEMHHPVTQSTFLGTKLHDRNITCQQEKMKEINSEEVKINDITVEINKTTERAPENCHLANEIKPSDPPLDNQMKHSFDSASNKNFSQCLESKLENSPVENVTAASTLLSQAKIDTGENKFPGSAPQQHSILSNQTSKSSDNRETPRNHSLPKCNSHLEITIPKDLKLKEAEKTDEKQLIIDAGQKRFGAVSCNVCGMLYTASNPEDETQHLLFHNQFISAVKYVGWKKERILAEYPDGRIIMVLPEDPKYALKKVDEIREMVDNDLGFQQAPLMCYSRTKTLLFISNDKKVVGCLIAEHIQWGYRVIEEKLPVIRSEEEKVRFERQKAWCCSTLPEPAICGISRIWVFSMMRRKKIASRMIECLRSNFIYGSYLSKEEIAFSDPTPDGKLFATQYCGTGQFLVYNFINGQNST","length":840,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":753,"region_id":"DP02851r001","start":740,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Notably, the segment of the loop connecting these strands (residues 740–753) could not be traced in the electron density map and is presumably disordered.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"27803161","version":2,"reference_html":"Molecular Basis for Cohesin Acetylation by Establishment of Sister Chromatid Cohesion N-Acetyltransferase ESCO1. <i> Rivera-Colón Y, Maguire A, Liszczak GP, Olia AS, Marmorstein R. </i> J Biol Chem, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5T53"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-05T15:12:43.042Z"}},{"start":1,"end":15,"reference_id":"27803161","reference_source":"pmid","reference_html":"Molecular Basis for Cohesin Acetylation by Establishment of Sister Chromatid Cohesion N-Acetyltransferase ESCO1. <i> Rivera-Colón Y, Maguire A, Liszczak GP, Olia AS, Marmorstein R. </i> J Biol Chem, 2016","date":"2022-08-05T15:13:35.536Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5T53"}],"region_id":"DP02851r002","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"released":"2023_12","ncbi_taxon_id":9606,"disprot_id":"DP02851","date":"2020-05-08T10:06:12.208Z","organism":"Homo sapiens","regions_counter":2,"name":"N-acetyltransferase ESCO1","dataset":[],"UniParc":"UPI00004C96E2","uniref100":"UniRef100_Q5FWF5","uniref90":"UniRef90_Q5FWF5","uniref50":"UniRef50_Q5FWF5","genes":[{"name":{"value":"ESCO1"},"synonyms":[{"value":"EFO1"},{"value":"KIAA1911"}]}],"alphafold_very_low_content":0.6761904761904762,"disorder_content":0.034523809523809526,"disprot_consensus":{"full":[{"start":1,"end":15,"type":"D"},{"start":740,"end":753,"type":"D"}],"Structural state":[{"start":1,"end":15,"type":"D"},{"start":740,"end":753,"type":"D"}]}},{"acc":"P55197","features":{"gene3D":[{"start":120,"end":201,"id":"G3DSA:3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"start":120,"end":201,"id":"G3DSA:3.30.40.10","name":"Zinc/RING finger domain, C3HC4 (zinc finger)"}],"pfam":[{"id":"PF13831","name":"PHD-finger","start":37,"end":72},{"id":"PF13832","name":"PHD-zinc-finger like domain","start":81,"end":197}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MVSSDRPVSLEDEVSHSMKEMIGGCCVCSDERGWAENPLVYCDGHGCSVAVHQACYGIVQVPTGPWFCRKCESQERAARVRCELCPHKDGALKRTDNGGWAHVVCALYIPEVQFANVSTMEPIVLQSVPHDRYNKTCYICDEQGRESKAATGACMTCNKHGCRQAFHVTCAQFAGLLCEEEGNGADNVQYCGYCKYHFSKLKKSKRGSNRSYDQSLSDSSSHSQDKHHEKEKKKYKEKDKHKQKHKKQPEPSPALVPSLTVTTEKTYTSTSNNSISGSLKRLEDTTARFTNANFQEVSAHTSSGKDVSETRGSEGKGKKSSAHSSGQRGRKPGGGRNPGTTVSAASPFPQGSFSGTPGSVKSSSGSSVQSPQDFLSFTDSDLRNDSYSHSQQSSATKDVHKGESGSQEGGVNSFSTLIGLPSTSAVTSQPKSFENSPGDLGNSSLPTAGYKRAQTSGIEEETVKEKKRKGNKQSKHGPGRPKGNKNQENVSHLSVSSASPTSSVASAAGSITSSSLQKSPTLLRNGSLQSLSVGSSPVGSEISMQYRHDGACPTTTFSELLNAIHNGIYNSNDVAVSFPNVVSGSGSSTPVSSSHLPQQSSGHLQQVGALSPSAVSSAAPAVATTQANTLSGSSLSQAPSHMYGNRSNSSMAALIAQSENNQTDQDLGDNSRNLVGRGSSPRGSLSPRSPVSSLQIRYDQPGNSSLENLPPVAASIEQLLERQWSEGQQFLLEQGTPSDILGMLKSLHQLQVENRRLEEQIKNLTAKKERLQLLNAQLSVPFPTITANPSPSHQIHTFSAQTAPTTDSLNSSKSPHIGNSFLPDNSLPVLNQDLTSSGQSTSSSSALSTPPPAGQSPAQQGSGVSGVQQVNGVTVGALASGMQPVTSTIPAVSAVGGIIGALPGNQLAINGIVGALNGVMQTPVTMSQNPTPLTHTTVPPNATHPMPATLTNSASGLGLLSDQQRQILIHQQQFQQLLNSQQLTPEQHQAFLYQLMQHHHQQHHQPELQQLQIPGPTQIPINNLLAGTQAPPLHTATTNPFLTIHGDNASQKVARLSDKTGPVAQEKS","length":1068,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":188,"region_id":"DP02852r001","start":179,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The first PHD finger adopts a mixed α/β fold characteristic of canonical PHD fingers, while PHD finger 2 is atypical and is composed solely of six α-helical segments with a disordered segment spanning residues 179–188 (Figure S2A).","type":"Results"},{"text":"A segment within PHD finger 2 of AF10PZP, that spans amino acids 179-188, is disordered in the 1.60 Å structure in the free state (Figure S2A). Upon complex formation with H3(1-36) peptide, this region becomes ordered to form an anti-parallel β-sheet (Figure 2I, marked by arrow; free and bound structures superimposition shown in Figure S2D). This dynamic β-sheet forms part of the binding channel wall within the PZP domain and contributes to the alignment of the bound H3 peptide with residue E179, which emanates from this β-sheet platform, directly involved in recognition of the ε-NH3+ group of K23 (Figure 2E).","type":"Results"}],"curator_id":"fquaglia","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26439302","version":2,"reference_html":"The PZP Domain of AF10 Senses Unmodified H3K27 to Regulate DOT1L-Mediated Methylation of H3K79. <i> Chen S, Yang Z, Wilkinson AW, Deshpande AJ, Sidoli S, Krajewski K, Strahl BD, Garcia BA, Armstrong SA, Patel DJ, Gozani O. </i> Mol Cell, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5DAG"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-24T18:40:05.584Z"}},{"region_id":"DP02852r002","unpublished":true,"ec_ontology":"ECO","end":190,"term_id":"GO:0005515","start":179,"version":3,"statement":[{"text":"The first PHD finger adopts a mixed α/β fold characteristic of canonical PHD fingers, while PHD finger 2 is atypical and is composed solely of six α-helical segments with a disordered segment spanning residues 179–188 (Figure S2A).","type":"Results"},{"text":"A segment within PHD finger 2 of AF10PZP, that spans amino acids 179-188, is disordered in the 1.60 Å structure in the free state (Figure S2A). Upon complex formation with H3(1-36) peptide, this region becomes ordered to form an anti-parallel β-sheet (Figure 2I, marked by arrow; free and bound structures superimposition shown in Figure S2D). This dynamic β-sheet forms part of the binding channel wall within the PZP domain and contributes to the alignment of the bound H3 peptide with residue E179, which emanates from this β-sheet platform, directly involved in recognition of the ε-NH3+ group of K23 (Figure 2E).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P68431","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_06","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"26439302","date":"2022-06-26T16:32:20.892Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5DAH"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"fquaglia","reference_html":"The PZP Domain of AF10 Senses Unmodified H3K27 to Regulate DOT1L-Mediated Methylation of H3K79. <i> Chen S, Yang Z, Wilkinson AW, Deshpande AJ, Sidoli S, Krajewski K, Strahl BD, Garcia BA, Armstrong SA, Patel DJ, Gozani O. </i> Mol Cell, 2015","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T12:48:13.130Z"}},{"term_namespace":"Biological process","ec_ontology":"ECO","end":190,"region_id":"DP02852r004","start":179,"term_id":"GO:0070734","unpublished":true,"statement":[{"text":"The first PHD finger adopts a mixed α/β fold characteristic of canonical PHD fingers, while PHD finger 2 is atypical and is composed solely of six α-helical segments with a disordered segment spanning residues 179–188 (Figure S2A).","type":"Results"},{"text":"A segment within PHD finger 2 of AF10PZP, that spans amino acids 179-188, is disordered in the 1.60 Å structure in the free state (Figure S2A). Upon complex formation with H3(1-36) peptide, this region becomes ordered to form an anti-parallel β-sheet (Figure 2I, marked by arrow; free and bound structures superimposition shown in Figure S2D). This dynamic β-sheet forms part of the binding channel wall within the PZP domain and contributes to the alignment of the bound H3 peptide with residue E179, which emanates from this β-sheet platform, directly involved in recognition of the ε-NH3+ group of K23 (Figure 2E).","type":"Results"},{"text":"In cells, PZP recognition of H3 is required for H3K79 dimethylation, expression of DOT1L-target genes, and proliferation of DOT1L-addicted leukemic cells. Together, our results uncover a pivotal role for H3K27-via readout by the AF10 PZP domain-in regulating the cancer-associated enzyme DOT1L.","type":"Abstract"}],"curator_id":"fquaglia","released":"2022_06","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"26439302","version":3,"reference_html":"The PZP Domain of AF10 Senses Unmodified H3K27 to Regulate DOT1L-Mediated Methylation of H3K79. <i> Chen S, Yang Z, Wilkinson AW, Deshpande AJ, Sidoli S, Krajewski K, Strahl BD, Garcia BA, Armstrong SA, Patel DJ, Gozani O. </i> Mol Cell, 2015","date":"2022-06-26T16:32:54.101Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"5DAH"}],"term_name":"histone H3-K27 methylation","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The modification of histone H3 by addition of one or more methyl groups to lysine at position 27 of the histone.\" [GOC:mah, GOC:pr]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T12:48:03.257Z"}},{"start":1,"end":23,"reference_id":"26439302","reference_source":"pmid","reference_html":"The PZP Domain of AF10 Senses Unmodified H3K27 to Regulate DOT1L-Mediated Methylation of H3K79. <i> Chen S, Yang Z, Wilkinson AW, Deshpande AJ, Sidoli S, Krajewski K, Strahl BD, Garcia BA, Armstrong SA, Patel DJ, Gozani O. </i> Mol Cell, 2015","date":"2022-06-26T16:31:50.226Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5DAG"}],"region_id":"DP02852r005","statement":[{"text":"Missing electron density region at the N-terminus of the protein.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T12:46:41.616Z"}},{"start":179,"end":188,"reference_id":"26439302","reference_source":"pmid","reference_html":"The PZP Domain of AF10 Senses Unmodified H3K27 to Regulate DOT1L-Mediated Methylation of H3K79. <i> Chen S, Yang Z, Wilkinson AW, Deshpande AJ, Sidoli S, Krajewski K, Strahl BD, Garcia BA, Armstrong SA, Patel DJ, Gozani O. </i> Mol Cell, 2015","date":"2022-06-27T13:27:11.458Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP02852r006","statement":[{"text":"A segment within PHD finger 2 of AF10PZP, that spans amino acids 179-188, is disordered in the 1.60 Å structure in the free state (Figure S2A). Upon complex formation with H3(1-36) peptide, this region becomes ordered to form an anti-parallel β-sheet (Figure 2I, marked by arrow; free and bound structures superimposition shown in Figure S2D).","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P68431"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T13:27:39.743Z"}}],"released":"2022_06","ncbi_taxon_id":9606,"disprot_id":"DP02852","date":"2020-05-08T14:09:36.479Z","organism":"Homo sapiens","regions_counter":6,"name":"Protein AF-10","dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI000012564D","uniref100":"UniRef100_P55197","uniref90":"UniRef90_P55197","uniref50":"UniRef50_P55197","genes":[{"name":{"value":"MLLT10","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:16063","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:16063"}}]},"synonyms":[{"value":"AF10","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10860745","url":"http://www.ncbi.nlm.nih.gov/pubmed/10860745","alternativeUrl":"https://europepmc.org/abstract/MED/10860745"}}]}]}],"alphafold_very_low_content":0.7209737827715356,"disorder_content":0.03089887640449438,"disprot_consensus":{"full":[{"start":1,"end":23,"type":"D"},{"start":179,"end":188,"type":"T"},{"start":189,"end":190,"type":"F"}],"Structural state":[{"start":1,"end":23,"type":"D"},{"start":179,"end":188,"type":"D"}],"Molecular function":[{"start":179,"end":190,"type":"F"}],"Biological process":[{"start":179,"end":190,"type":"F"}],"Structural transition":[{"start":179,"end":188,"type":"T"}]}},{"acc":"Q99P68","features":{"gene3D":[{"start":71,"end":167,"id":"G3DSA:2.10.90.10","name":"Cystine-knot cytokines"}],"pfam":[{"id":"PF05463","name":"Sclerostin (SOST)","start":1,"end":208}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MQPSLAPCLICLLVHAAFCAVEGQGWQAFRNDATEVIPGLGEYPEPPPENNQTMNRAENGGRPPHHPYDAKDVSEYSCRELHYTRFLTDGPCRSAKPVTELVCSGQCGPARLLPNAIGRVKWWRPNGPDFRCIPDRYRAQRVQLLCPGGAAPRSRKVRLVASCKCKRLTRFHNQSELKDFGPETARPQKGRKPRPGARGAKANQAELENAY","length":211,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":51,"region_id":"DP02853r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"In this study we present the structure of murine Sclerostin by solution NMR spectroscopy revealing that only the cystin-knot motif is structured.","type":"Article"},{"text":"N- and C-termini of Sclerostin are flexible","type":"Results"},{"text":"We initially prepared full-length murine Sclerostin (mSOST) in Sf9 cells (Fig. 1A). The protein comprising Gln1 to Tyr188 could be obtained from the supernatant of Sf9 cells. Staining via the Periodic Schiff Acid method confirmed the presence of glycosylation; mass spectrometry subsequently showed both N-glycosylation sites, Asn28 and Asn150, to be linked to carbohydrates. Storage of full-length mSOST over several weeks at 4 °C resulted in partial proteolysis although the protein solution had a purity of ⩾95%. Thus residual protease activity cleaves mSOST indicating the presence of flexible regions. The largest fragment showed an apparent molecular weight of roughly 10–12 kDa in a SDS–PAGE analysis (Fig. 1B). Mass spectrometry gave a molecular weight of 10,254 Da, which corresponds to a fragment comprising Glu52 to Cys142.","type":"Results"},{"text":"To additionally test our hypothesis that the N- and C-terminus are highly flexible and unstructured we compared the 2D 1H–15N HSQC spectra of uniformly 15N-labeled full-length mSOST and mSOSTΔNC. Residues located in the termini of mSOST exhibit amide proton chemical shift values between 7.5 and 8.5 ppm indicative for random coil conformation (Supplementary Fig. 2).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19166819","version":2,"reference_html":"NMR structure of the Wnt modulator protein Sclerostin. <i> Weidauer SE, Schmieder P, Beerbaum M, Schmitz W, Oschkinat H, Mueller TD. </i> Biochem Biophys Res Commun, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":211,"region_id":"DP02853r004","start":143,"term_id":"IDPO:0000002","statement":[{"text":"In this study we present the structure of murine Sclerostin by solution NMR spectroscopy revealing that only the cystin-knot motif is structured.","type":"Article"},{"text":"N- and C-termini of Sclerostin are flexible","type":"Results"},{"text":"We initially prepared full-length murine Sclerostin (mSOST) in Sf9 cells (Fig. 1A). The protein comprising Gln1 to Tyr188 could be obtained from the supernatant of Sf9 cells. Staining via the Periodic Schiff Acid method confirmed the presence of glycosylation; mass spectrometry subsequently showed both N-glycosylation sites, Asn28 and Asn150, to be linked to carbohydrates. Storage of full-length mSOST over several weeks at 4 °C resulted in partial proteolysis although the protein solution had a purity of ⩾95%. Thus residual protease activity cleaves mSOST indicating the presence of flexible regions. The largest fragment showed an apparent molecular weight of roughly 10–12 kDa in a SDS–PAGE analysis (Fig. 1B). Mass spectrometry gave a molecular weight of 10,254 Da, which corresponds to a fragment comprising Glu52 to Cys142.","type":"Results"},{"text":"To additionally test our hypothesis that the N- and C-terminus are highly flexible and unstructured we compared the 2D 1H–15N HSQC spectra of uniformly 15N-labeled full-length mSOST and mSOSTΔNC. Residues located in the termini of mSOST exhibit amide proton chemical shift values between 7.5 and 8.5 ppm indicative for random coil conformation (Supplementary Fig. 2).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19166819","version":2,"reference_html":"NMR structure of the Wnt modulator protein Sclerostin. <i> Weidauer SE, Schmieder P, Beerbaum M, Schmitz W, Oschkinat H, Mueller TD. </i> Biochem Biophys Res Commun, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":51,"region_id":"DP02853r005","start":1,"term_id":"IDPO:0000002","statement":[{"text":"In this study we present the structure of murine Sclerostin by solution NMR spectroscopy revealing that only the cystin-knot motif is structured.","type":"Article"},{"text":"N- and C-termini of Sclerostin are flexible","type":"Results"},{"text":"We initially prepared full-length murine Sclerostin (mSOST) in Sf9 cells (Fig. 1A). The protein comprising Gln1 to Tyr188 could be obtained from the supernatant of Sf9 cells. Staining via the Periodic Schiff Acid method confirmed the presence of glycosylation; mass spectrometry subsequently showed both N-glycosylation sites, Asn28 and Asn150, to be linked to carbohydrates. Storage of full-length mSOST over several weeks at 4 °C resulted in partial proteolysis although the protein solution had a purity of ⩾95%. Thus residual protease activity cleaves mSOST indicating the presence of flexible regions. The largest fragment showed an apparent molecular weight of roughly 10–12 kDa in a SDS–PAGE analysis (Fig. 1B). Mass spectrometry gave a molecular weight of 10,254 Da, which corresponds to a fragment comprising Glu52 to Cys142.","type":"Results"},{"text":"To additionally test our hypothesis that the N- and C-terminus are highly flexible and unstructured we compared the 2D 1H–15N HSQC spectra of uniformly 15N-labeled full-length mSOST and mSOSTΔNC. Residues located in the termini of mSOST exhibit amide proton chemical shift values between 7.5 and 8.5 ppm indicative for random coil conformation (Supplementary Fig. 2).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19166819","version":2,"reference_html":"NMR structure of the Wnt modulator protein Sclerostin. <i> Weidauer SE, Schmieder P, Beerbaum M, Schmitz W, Oschkinat H, Mueller TD. </i> Biochem Biophys Res Commun, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007689","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":211,"region_id":"DP02853r006","start":143,"term_id":"IDPO:0000002","statement":[{"text":"In this study we present the structure of murine Sclerostin by solution NMR spectroscopy revealing that only the cystin-knot motif is structured.","type":"Article"},{"text":"N- and C-termini of Sclerostin are flexible","type":"Results"},{"text":"We initially prepared full-length murine Sclerostin (mSOST) in Sf9 cells (Fig. 1A). The protein comprising Gln1 to Tyr188 could be obtained from the supernatant of Sf9 cells. Staining via the Periodic Schiff Acid method confirmed the presence of glycosylation; mass spectrometry subsequently showed both N-glycosylation sites, Asn28 and Asn150, to be linked to carbohydrates. Storage of full-length mSOST over several weeks at 4 °C resulted in partial proteolysis although the protein solution had a purity of ⩾95%. Thus residual protease activity cleaves mSOST indicating the presence of flexible regions. The largest fragment showed an apparent molecular weight of roughly 10–12 kDa in a SDS–PAGE analysis (Fig. 1B). Mass spectrometry gave a molecular weight of 10,254 Da, which corresponds to a fragment comprising Glu52 to Cys142.","type":"Results"},{"text":"To additionally test our hypothesis that the N- and C-terminus are highly flexible and unstructured we compared the 2D 1H–15N HSQC spectra of uniformly 15N-labeled full-length mSOST and mSOSTΔNC. Residues located in the termini of mSOST exhibit amide proton chemical shift values between 7.5 and 8.5 ppm indicative for random coil conformation (Supplementary Fig. 2).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19166819","version":2,"reference_html":"NMR structure of the Wnt modulator protein Sclerostin. <i> Weidauer SE, Schmieder P, Beerbaum M, Schmitz W, Oschkinat H, Mueller TD. </i> Biochem Biophys Res Commun, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007689","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":30,"region_id":"DP02853r008","start":26,"term_id":"IDPO:0000041","statement":[{"text":"Staining via the Periodic Schiff Acid method confirmed the presence of glycosylation; mass spectrometry subsequently showed both N-glycosylation sites, Asn28 and Asn150, to be linked to carbohydrates.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"mass spectrometry evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19166819","version":2,"reference_html":"NMR structure of the Wnt modulator protein Sclerostin. <i> Weidauer SE, Schmieder P, Beerbaum M, Schmitz W, Oschkinat H, Mueller TD. </i> Biochem Biophys Res Commun, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001230","term_name":"glycosylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":152,"region_id":"DP02853r009","start":148,"term_id":"IDPO:0000041","statement":[{"text":"Staining via the Periodic Schiff Acid method confirmed the presence of glycosylation; mass spectrometry subsequently showed both N-glycosylation sites, Asn28 and Asn150, to be linked to carbohydrates.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"mass spectrometry evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19166819","version":2,"reference_html":"NMR structure of the Wnt modulator protein Sclerostin. <i> Weidauer SE, Schmieder P, Beerbaum M, Schmitz W, Oschkinat H, Mueller TD. </i> Biochem Biophys Res Commun, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001230","term_name":"glycosylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2020_12","ncbi_taxon_id":10090,"disprot_id":"DP02853","date":"2020-05-08T15:19:42.087Z","organism":"Mus musculus","regions_counter":9,"name":"Sclerostin","dataset":[],"UniParc":"UPI00000284D2","uniref100":"UniRef100_Q99P68","uniref90":"UniRef90_Q99P68","uniref50":"UniRef50_Q9BQB4","genes":[{"name":{"value":"Sost","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:1921749","url":"http://www.informatics.jax.org/marker/MGI:1921749"}}]}}],"alphafold_very_low_content":0.037914691943127965,"disorder_content":0.5687203791469194,"disprot_consensus":{"full":[{"start":1,"end":51,"type":"D"},{"start":143,"end":211,"type":"D"}],"Structural state":[{"start":1,"end":51,"type":"D"},{"start":143,"end":211,"type":"D"}],"Disorder function":[{"start":26,"end":30,"type":"F"},{"start":148,"end":152,"type":"F"}]}},{"acc":"Q9BYF1","features":{"gene3D":[],"pfam":[{"id":"PF01401","name":"Angiotensin-converting enzyme","start":21,"end":606},{"id":"PF16959","name":"Renal amino acid transporter","start":617,"end":770}]},"creator":"lchemes","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MSSSSWLLLSLVAVTAAQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLYEEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDFRILMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKSIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNKNSFVGWSTDWSPYADQSIKVRISLKSALGDKAYEWNDNEMYLFRSSVAYAMRQYFLKVKNQMILFGEEDVRVANLKPRISFNFFVTAPKNVSDIIPRTEVEKAIRMSRSRINDAFRLNDNSLEFLGIQPTLGPPNQPPVSIWLIVFGVVMGVIVVGIVILIFTGIRDRKKKNKARSGENPYASIDISKGENNPGFQNTDDVQTSF","length":805,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":805,"region_id":"DP02854r001","reference_id":"32132184","start":769,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Full-length ACE2 consists of an Nterminal PD and a C-terminal collectrin-like domain (CLD) that ends with a single transmembrane helix and a ~40-residue intracellular segment (15, 21).","type":"Article"},{"text":"The high resolution supported reliable model building. For ACE2, side chains could be assigned to residues 19 to 768, which contain the PD (residues 19 to 615) and the CLD (residues 616 to 768), which consists of a small extracellular domain, a long linker, and the single TM helix (Fig. 1C).","type":"Article"},{"text":"The C-terminal tail starting on residue 769 has no density in the structure and is therefore disordered","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2. <i> Yan R, Zhang Y, Li Y, Xia L, Guo Y, Zhou Q. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6M1D"},{"db":"PDB","id":"6M17"},{"db":"PDB","id":"6M18"}],"term_name":"disorder","ec_go":"IDA","disprot_namespace":"Structural state"},{"start":779,"end":783,"reference_id":"23882028","reference_source":"pmid","reference_html":"Development of a 5-plex SILAC method tuned for the quantitation of tyrosine phosphorylation dynamics. <i> Tzouros M, Golling S, Avila D, Lamerz J, Berrera M, Ebeling M, Langen H, Augustin A. </i> Mol Cell Proteomics, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001254","ec_ontology":"ECO","ec_name":"radioisotope assay evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP02854r003","statement":[{"text":"Using this new labeling strategy specifically tailored for phosphotyrosines, it was possible to generate the time profiles for 318 unique phosphopeptides belonging to 215 proteins from an erlotinib-treated breast cancer cell line model.","type":"Abstract"}],"ec_go":"IDA","disprot_namespace":"Disorder function"}],"released":"2020_06","ncbi_taxon_id":9606,"disprot_id":"DP02854","date":"2020-05-08T17:02:06.414Z","organism":"Homo sapiens","regions_counter":3,"name":"Angiotensin-converting enzyme 2","dataset":[],"UniParc":"UPI000006D4E0","uniref100":"UniRef100_Q9BYF1","uniref90":"UniRef90_Q9BYF1","uniref50":"UniRef50_Q9BYF1","genes":[{"name":{"value":"ACE2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:13557","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:13557"}}]},"orfNames":[{"value":"UNQ868/PRO1885"}]}],"alphafold_very_low_content":0.04720496894409938,"disorder_content":0.04596273291925466,"disprot_consensus":{"full":[{"start":769,"end":805,"type":"D"}],"Structural state":[{"start":769,"end":805,"type":"D"}],"Disorder function":[{"start":779,"end":783,"type":"F"}]}},{"acc":"P11166","features":{"gene3D":[],"pfam":[{"id":"PF00083","name":"Sugar (and other) transporter","start":19,"end":466}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MEPSSKKLTGRLMLAVGGAVLGSLQFGYNTGVINAPQKVIEEFYNQTWVHRYGESILPTTLTTLWSLSVAIFSVGGMIGSFSVGLFVNRFGRRNSMLMMNLLAFVSAVLMGFSKLGKSFEMLILGRFIIGVYCGLTTGFVPMYVGEVSPTALRGALGTLHQLGIVVGILIAQVFGLDSIMGNKDLWPLLLSIIFIPALLQCIVLPFCPESPRFLLINRNEENRAKSVLKKLRGTADVTHDLQEMKEESRQMMREKKVTILELFRSPAYRQPILIAVVLQLSQQLSGINAVFYYSTSIFEKAGVQQPVYATIGSGIVNTAFTVVSLFVVERAGRRTLHLIGLAGMAGCAILMTIALALLEQLPWMSYLSIVAIFGFVAFFEVGPGPIPWFIVAELFSQGPRPAAIAVAGFSNWTSNFIVGMCFQYVEQLCGPYVFIIFTVLLVLFFIFTYFKVPETKGRTFDEIASGFRQGGASQSDKTPEELFHPLGADSQV","length":492,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":492,"region_id":"DP02855r001","start":456,"term_id":"IDPO:0000002","statement":[{"text":"In the GLUT1 structure, residues 9–455 constitute the canonical MFS fold whereas the C-terminal segment was invisible probably due to its inherent flexibility in this conformation (Fig. 1).","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24847886","version":2,"reference_html":"Crystal structure of the human glucose transporter GLUT1. <i> Deng D, Xu C, Sun P, Wu J, Yan C, Hu M, Yan N. </i> Nature, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4PYP"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T12:58:44.017Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":456,"end":492,"reference_id":"27078104","reference_source":"pmid","reference_html":"Mechanism of inhibition of human glucose transporter GLUT1 is conserved between cytochalasin B and phenylalanine amides. <i> Kapoor K, Finer-Moore JS, Pedersen BP, Caboni L, Waight A, Hillig RC, Bringmann P, Heisler I, Müller T, Siebeneicher H, Stroud RM. </i> Proc Natl Acad Sci U S A, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5EQG"},{"db":"PDB","id":"5EQH"},{"db":"PDB","id":"5EQI"}],"region_id":"DP02855r002","statement":[{"text":"As in 4PYP, residues 1–8 and 456–504 were not visible in density maps and are not part of our structures.","type":"Methods"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-24T15:05:44.278Z"}}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02855","date":"2020-05-08T17:19:12.324Z","organism":"Homo sapiens","regions_counter":2,"name":"Solute carrier family 2, facilitated glucose transporter member 1","dataset":["NDDs-related proteins","Age-related disorders proteins"],"UniParc":"UPI000004F0B2","uniref100":"UniRef100_P11166","uniref90":"UniRef90_P11166","uniref50":"UniRef50_P11166","genes":[{"name":{"value":"SLC2A1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11005","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11005"}}]},"synonyms":[{"value":"GLUT1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"18245775","url":"http://www.ncbi.nlm.nih.gov/pubmed/18245775","alternativeUrl":"https://europepmc.org/abstract/MED/18245775"}}]}]}],"alphafold_very_low_content":0.04878048780487805,"disorder_content":0.07520325203252033,"disprot_consensus":{"full":[{"start":456,"end":492,"type":"D"}],"Structural state":[{"start":456,"end":492,"type":"D"}]}},{"acc":"P83916","features":{"gene3D":[],"pfam":[{"id":"PF00385","name":"Chromo (CHRromatin Organisation MOdifier) domain","start":21,"end":69},{"id":"PF01393","name":"Chromo shadow domain","start":113,"end":172}]},"creator":"lchemes","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MGKKQNKKKVEEVLEEEEEEYVVEKVLDRRVVKGKVEYLLKWKGFSDEDNTWEPEENLDCPDLIAEFLQSQKTAHETDKSEGGKRKADSDSEDKGEESKPKKKKEESEKPRGFARGLEPERIIGATDSSGELMFLMKWKNSDEADLVPAKEANVKCPQVVISFYEERLTWHSYPSEDDDKKDDKN","length":185,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":107,"region_id":"DP02856r001","start":73,"term_id":"IDPO:0000002","statement":[{"text":"Here, we used NMR spectroscopy in combination with small angle X-ray scattering and dynamic light scattering to characterize the dynamic and structural properties of full-length human HP1β (hHP1β) in solution. We show that the hinge region is highly flexible and enables a largely unrestricted spatial search by the two globular domains for their binding partners","type":"Abstract"},{"text":"Besides the two structurally related CD (21–71) and CSD (110–170), the remainder of the protein, which accounts for more than one third of the sequence, has a non-globular character with a high percentage of charged residues. The non-globular nature of the hinge region and the N- and C-terminal tails lead to severe signal overlap between 8 and 8.5 ppm in the 1H dimension and a large dynamic range of peak intensities.","type":"Results"},{"text":"For most residues in the tails and the hinge region the absolute values of Cα secondary chemical shifts were below 0.3 ppm (figure 2C and, for the combined secondary chemical shifts see figure S1), supporting their intrinsically disordered nature. In the hinge region a weak helical tendency expands the α-helix of the CD beyond residue 70 up to 73. In addition, a continuous stretch of small negative Cα secondary shifts in proximity to residue 20 points to a propensity for extended conformations in the N-terminal tail. \n\nAccording to 15N spin relaxation rates the backbone outside of CD and CSD is highly mobile (figure 3).","type":"Results"},{"text":"The limits of the region are determined from the NMR data in Figures 2, 3 and 4","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"23585859","version":2,"reference_html":"Structural plasticity in human heterochromatin protein 1β. <i> Munari F, Rezaei-Ghaleh N, Xiang S, Fischle W, Zweckstetter M. </i> PLoS One, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T17:21:49.801Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":107,"region_id":"DP02856r002","start":73,"term_id":"IDPO:0000002","statement":[{"text":"Here, we used NMR spectroscopy in combination with small angle X-ray scattering and dynamic light scattering to characterize the dynamic and structural properties of full-length human HP1β (hHP1β) in solution. We show that the hinge region is highly flexible and enables a largely unrestricted spatial search by the two globular domains for their binding partners","type":"Abstract"},{"text":"Comparison of the R g distribution derived from the optimized ensembles with that obtained from a pool of randomly generated models is shown in figure 1D. The R g distribution of the selected ensemble is nearly as broad as the one from the initial random pool, with the maximum shifted towards longer distances, indicating that the hinge region is highly flexible with a preference for more extended conformations.","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"23585859","version":2,"reference_html":"Structural plasticity in human heterochromatin protein 1β. <i> Munari F, Rezaei-Ghaleh N, Xiang S, Fischle W, Zweckstetter M. </i> PLoS One, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T17:21:39.150Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":107,"region_id":"DP02856r003","start":73,"term_id":"IDPO:0000002","statement":[{"text":"Here, we used NMR spectroscopy in combination with small angle X-ray scattering and dynamic light scattering to characterize the dynamic and structural properties of full-length human HP1β (hHP1β) in solution. We show that the hinge region is highly flexible and enables a largely unrestricted spatial search by the two globular domains for their binding partners","type":"Abstract"},{"text":"Dynamic light scattering measurements resulted in a well-defined monodisperse peak with a hydrodynamic radius of 4.4±0.1 nm (figure 1A). The value is in agreement with the results from pulse field gradient NMR (figure 1B) and indicates that the protein does not assume a compact state in solution.","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"dynamic light scattering assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"23585859","version":2,"reference_html":"Structural plasticity in human heterochromatin protein 1β. <i> Munari F, Rezaei-Ghaleh N, Xiang S, Fischle W, Zweckstetter M. </i> PLoS One, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007064","term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T17:20:50.731Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":185,"region_id":"DP02856r004","start":176,"term_id":"IDPO:0000002","statement":[{"text":"Here, we used NMR spectroscopy in combination with small angle X-ray scattering and dynamic light scattering to characterize the dynamic and structural properties of full-length human HP1β (hHP1β) in solution. We show that the hinge region is highly flexible and enables a largely unrestricted spatial search by the two globular domains for their binding partners","type":"Abstract"},{"text":"The N- and C-terminal tails as well as the hinge region showed much smaller J(0) and bigger J(0.87ωH) than the two globular domains, indicating a very slow decay of their spectral density function characteristic of fast tumbling molecules with high internal mobility.","type":"Results"},{"text":"The J(0.87ωH) profile demonstrated that the N-terminal tail experiences smaller internal dynamics when compared to the hinge region, with the C-terminal tail being the most flexible part among the disordered domains (figure S3A).","type":"Results"},{"text":"The limits of the region are determined from the NMR data in Figures 2, 3 and 4","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"23585859","version":2,"reference_html":"Structural plasticity in human heterochromatin protein 1β. <i> Munari F, Rezaei-Ghaleh N, Xiang S, Fischle W, Zweckstetter M. </i> PLoS One, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T17:20:22.508Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":185,"region_id":"DP02856r005","start":176,"term_id":"IDPO:0000002","statement":[{"text":"No specific mention in text, but the region 176-185 is missing in the electron density","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"21346195","version":2,"reference_html":"Mitotic centromeric targeting of HP1 and its binding to Sgo1 are dispensable for sister-chromatid cohesion in human cells. <i> Kang J, Chaudhary J, Dong H, Kim S, Brautigam CA, Yu H. </i> Mol Biol Cell, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3Q6S"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-15T17:19:02.338Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":107,"region_id":"DP02856r008","start":73,"term_id":"IDPO:0000033","statement":[{"text":"We show that the hinge region is highly flexible and enables a largely unrestricted spatial search by the two globular domains for their binding partners.","type":"Abstract"}],"curator_id":"vnugnes","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"23585859","version":4,"reference_html":"Structural plasticity in human heterochromatin protein 1β. <i> Munari F, Rezaei-Ghaleh N, Xiang S, Fischle W, Zweckstetter M. </i> PLoS One, 2013","date":"2023-12-15T17:39:07.454Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"flexible linker","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02856","date":"2020-05-08T19:16:04.609Z","organism":"Homo sapiens","regions_counter":9,"name":"Chromobox protein homolog 1","dataset":["Condensates-related proteins"],"UniParc":"UPI0000021A5B","uniref100":"UniRef100_P83916","uniref90":"UniRef90_P83916","uniref50":"UniRef50_P83916","genes":[{"name":{"value":"CBX1"},"synonyms":[{"value":"CBX"}]}],"alphafold_very_low_content":0.12972972972972974,"disorder_content":0.24324324324324326,"disprot_consensus":{"full":[{"start":73,"end":107,"type":"D"},{"start":176,"end":185,"type":"D"}],"Structural state":[{"start":73,"end":107,"type":"D"},{"start":176,"end":185,"type":"D"}],"Disorder function":[{"start":73,"end":107,"type":"F"}]}},{"acc":"P18206-2","features":{"pfam":[]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVAAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVQAAQMLQSDPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNSKNQGIEEALKNRNFTVEKMSAEINEIIRVLQLTSWDEDAWASKDTEAMKRALASIDSKLNQAKGWLRDPSASPGDAGEQAIRQILDEAGKVGELCAGKERREILGTCKMLGQMTDQVADLRARGQGSSPVAMQKAQQVSQGLDVLTAKVENAARKLEAMTNSKQSIAKKIDAAQNWLADPNGGPEGEEQIRGALAEARKIAELCDDPKERDDILRSLGEISALTSKLADLRRQGKGDSPEARALAKQVATALQNLQTKTNRAVANSRPAKAAVHLEGKIEQAQRWIDNPTVDDRGVGQAAIRGLVAEGHRLANVMMGPYRQDLLAKCDRVDQLTAQLADLAARGEGESPQARALASQLQDSLKDLKARMQEAMTQEVSDVFSDTTTPIKLLAVAATAPPDAPNREEVFDERAANFENHSGKLGATAEKAAAVGTANKSTVEGIQASVKTARELTPQVVSAARILLRNPGNQAAYEHFETMKNQWIDNVEKMTGLVDEAIDTKSLLDASEEAIKKDLDKCKVAMANIQPQMLVAGATSIARRANRILLVAKREVENSEDPKFREAVKAASDELSKTISPMVMDAKAVAGNISDPGLQKSFLDSGYRILGAVAKVREAFQPQEPDFPPPPPDLEQLRLTDELAPPKPPLPEGEVPPPRPPPPEEKDEEFPEQKAGEVINQPMMMAARQLHDEARKWSSKGNDIIAAAKRMALLMAEMSRLVRGGSGTKRALIQCAKDIAKASDEVTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKILSTVKATMLGRTNISDEESEQATEMLVHNAQNLMQSVKETVREAEAASIKIRTDAGFTLRWVRKTPWYQ","length":1066,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":876,"region_id":"DP02858r001","start":844,"term_id":"IDPO:0000002","statement":[{"text":"The asymmetric unit contains two copies of the vinculin monomer and the proline-rich linker, speculated to function as a hinge for the protein Price et al. 1989, Brindle et al. 1996, was largely disordered.","type":"Results"},{"text":"The N- and C-terminal helical bundles are indicated. In one monomer in the asymmetric unit residues 853–872 are disordered, while residues 853-878 are disordered in the other monomer in the asymmetric unit. These residues span vinculin's proline-rich linker. For clarity, all figures of full-length vinculin show residues 1–840 and 879–1066.","type":"Figure"},{"text":"However, disordered regions were difficult to parameterize in terms of multiple conformations at the given resolution, which led to relatively high B factor and R factor statistics for the single-conformation models used, and did limit the scope of reliably assigning bound water molecules.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15242595","version":2,"reference_html":"Crystal structure of human vinculin. <i> Borgon RA, Vonrhein C, Bricogne G, Bois PR, Izard T. </i> Structure, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1TR2"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9BX66","partner_end":null}],"ec_ontology":"ECO","end":879,"region_id":"DP02858r002","start":857,"term_id":"GO:0005515","statement":[{"text":"As shown in Fig. 2B and C, similar dissociation constants (Kd) were obtained for vin857 (1.08 μM) and vin837 (1.16 μM) with the tandem SH3 domains, and the stoichiometries of vin857 and vin837 were both determined to be 1, indicating that vin857 is sufficient for the interaction.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"isothermal titration calorimetry evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"24878663","version":3,"reference_html":"Structural investigation of the interaction between the tandem SH3 domains of c-Cbl-associated protein and vinculin. <i> Zhao D, Wang X, Peng J, Wang C, Li F, Sun Q, Zhang Y, Zhang J, Cai G, Zuo X, Wu J, Shi Y, Zhang Z, Gong Q. </i> J Struct Biol, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005647","term_name":"protein binding","curator_orcid":"0000-0002-0341-4888","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9BX66","partner_end":null}],"ec_ontology":"ECO","end":879,"region_id":"DP02858r003","start":857,"term_id":"GO:0005515","statement":[{"text":"Because no inter-domain NOEs are observed between the SH3a and SH3b domains after their binding to vin857 (data not shown), the enhanced binding affinity is most likely caused by the flexible linker, which tethers both the SH3a and SH3b domains and restricts the dissociation ability of the individual SH3 domains from the substrate.","type":"Discussion"},{"text":"Additionally, almost the same NMR chemical shift perturbations were observed in the 15N-HSQC spectra of the tandem SH3 domains upon titration with the vin837 and vin857 peptides (Fig. S3), consistent with the above-mentioned ITC results.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"24878663","version":3,"reference_html":"Structural investigation of the interaction between the tandem SH3 domains of c-Cbl-associated protein and vinculin. <i> Zhao D, Wang X, Peng J, Wang C, Li F, Sun Q, Zhang Y, Zhang J, Cai G, Zuo X, Wu J, Shi Y, Zhang Z, Gong Q. </i> J Struct Biol, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"protein binding","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02858r004","ec_ontology":"ECO","end":867,"term_id":"GO:0005515","start":857,"version":3,"statement":[{"text":"In this study, we first determined the solution structure of the tandem SH3 domains of CAP and further analyzed its complex structure with the proline-rich linker of vinculin using ITC, NMR, and X-ray crystallography.","type":"Discussion"},{"text":"The binding motif of the SH3 domain of Vinculin (857-879) is composed of two short proline-rich regions (prr): prr1 (N- LAPPKPPLPE -C), corresponding to PDB:4ln2, and prr2 (N- VPPPRPPPPE -C), corresponding to PDB:4lnp.","type":"Curator statement"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9BX66","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"24878663","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4ln2"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"fquaglia","reference_html":"Structural investigation of the interaction between the tandem SH3 domains of c-Cbl-associated protein and vinculin. <i> Zhao D, Wang X, Peng J, Wang C, Li F, Sun Q, Zhang Y, Zhang J, Cai G, Zuo X, Wu J, Shi Y, Zhang Z, Gong Q. </i> J Struct Biol, 2014","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02858r005","ec_ontology":"ECO","end":879,"term_id":"GO:0005515","start":870,"version":3,"statement":[{"text":"In this study, we first determined the solution structure of the tandem SH3 domains of CAP and further analyzed its complex structure with the proline-rich linker of vinculin using ITC, NMR, and X-ray crystallography.","type":"Discussion"},{"text":"The binding motif of the SH3 domain of Vinculin (857-879) is composed of two short proline-rich regions (prr): prr1 (N- LAPPKPPLPE -C), corresponding to PDB:4ln2, and prr2 (N- VPPPRPPPPE -C), corresponding to PDB:4lnp.","type":"Curator statement"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9BX66","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"24878663","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4lnp"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"fquaglia","reference_html":"Structural investigation of the interaction between the tandem SH3 domains of c-Cbl-associated protein and vinculin. <i> Zhao D, Wang X, Peng J, Wang C, Li F, Sun Q, Zhang Y, Zhang J, Cai G, Zuo X, Wu J, Shi Y, Zhang Z, Gong Q. </i> J Struct Biol, 2014","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":879,"region_id":"DP02858r006","start":870,"term_id":"IDPO:0000011","statement":[{"text":"In this study, we first determined the solution structure of the tandem SH3 domains of CAP and further analyzed its complex structure with the proline-rich linker of vinculin using ITC, NMR, and X-ray crystallography.","type":"Discussion"},{"text":"The binding motif of the SH3 domain of Vinculin (857-879) is composed of two short proline-rich regions (prr): prr1 (N- LAPPKPPLPE -C), corresponding to PDB:4ln2, and prr2 (N- VPPPRPPPPE -C), corresponding to PDB:4lnp.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24878663","version":2,"reference_html":"Structural investigation of the interaction between the tandem SH3 domains of c-Cbl-associated protein and vinculin. <i> Zhao D, Wang X, Peng J, Wang C, Li F, Sun Q, Zhang Y, Zhang J, Cai G, Zuo X, Wu J, Shi Y, Zhang Z, Gong Q. </i> J Struct Biol, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4lnp"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":867,"region_id":"DP02858r007","start":857,"term_id":"IDPO:0000011","statement":[{"text":"In this study, we first determined the solution structure of the tandem SH3 domains of CAP and further analyzed its complex structure with the proline-rich linker of vinculin using ITC, NMR, and X-ray crystallography.","type":"Discussion"},{"text":"The binding motif of the SH3 domain of Vinculin (857-879) is composed of two short proline-rich regions (prr): prr1 (N- LAPPKPPLPE -C), corresponding to PDB:4ln2, and prr2 (N- VPPPRPPPPE -C), corresponding to PDB:4lnp.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24878663","version":2,"reference_html":"Structural investigation of the interaction between the tandem SH3 domains of c-Cbl-associated protein and vinculin. <i> Zhao D, Wang X, Peng J, Wang C, Li F, Sun Q, Zhang Y, Zhang J, Cai G, Zuo X, Wu J, Shi Y, Zhang Z, Gong Q. </i> J Struct Biol, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4ln2"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":879,"region_id":"DP02858r008","start":857,"term_id":"GO:0060090","statement":[{"text":"In this study, we first determined the solution structure of the tandem SH3 domains of CAP and further analyzed its complex structure with the proline-rich linker of vinculin using ITC, NMR, and X-ray crystallography.","type":"Discussion"},{"text":"Because no inter-domain NOEs are observed between the SH3a and SH3b domains after their binding to vin857 (data not shown), the enhanced binding affinity is most likely caused by the flexible linker, which tethers both the SH3a and SH3b domains and restricts the dissociation ability of the individual SH3 domains from the substrate.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"24878663","version":3,"reference_html":"Structural investigation of the interaction between the tandem SH3 domains of c-Cbl-associated protein and vinculin. <i> Zhao D, Wang X, Peng J, Wang C, Li F, Sun Q, Zhang Y, Zhang J, Cai G, Zuo X, Wu J, Shi Y, Zhang Z, Gong Q. </i> J Struct Biol, 2014","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"molecular adaptor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_12","ncbi_taxon_id":9606,"disprot_id":"DP02858","date":"2020-05-11T09:14:54.150Z","organism":"Homo sapiens","regions_counter":11,"name":"Isoform 1 of Vinculin","dataset":[],"UniParc":"UPI00000424F8","uniref100":"","uniref90":"","uniref50":"","genes":[{"name":{"value":"VCL"}}],"disorder_content":0.03095684803001876,"disprot_consensus":{"full":[{"start":844,"end":856,"type":"D"},{"start":857,"end":867,"type":"T"},{"start":868,"end":869,"type":"D"},{"start":870,"end":879,"type":"T"}],"Structural state":[{"start":844,"end":876,"type":"D"}],"Molecular function":[{"start":857,"end":879,"type":"F"}],"Structural transition":[{"start":857,"end":867,"type":"T"},{"start":870,"end":879,"type":"T"}]}},{"acc":"P55211","features":{"gene3D":[],"pfam":[{"id":"PF00619","name":"Caspase recruitment domain","start":6,"end":90},{"id":"PF00656","name":"Caspase domain","start":161,"end":412}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MDEADRRLLRRCRLRLVEELQVDQLWDALLSRELFRPHMIEDIQRAGSGSRRDQARQLIIDLETRGSQALPLFISCLEDTGQDMLASFLRTNRQAAKLSKPTLENLTPVVLRPEIRKPEVLRPETPRPVDIGSGGFGDVGALESLRGNADLAYILSMEPCGHCLIINNVNFCRESGLRTRTGSNIDCEKLRRRFSSLHFMVEVKGDLTAKKMVLALLELAQQDHGALDCCVVVILSHGCQASHLQFPGAVYGTDGCPVSVEKIVNIFNGTSCPSLGGKPKLFFIQACGGEQKDHGFEVASTSPEDESPGSNPEPDATPFQEGLRTFDQLDAISSLPTPSDIFVSYSTFPGFVSWRDPKSGSWYVETLDDIFEQWAHSEDLQSLLLRVANAVSVKGIYKQMPGCFNFLRKKLFFKTS","length":416,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":334,"region_id":"DP02860r001","start":289,"term_id":"IDPO:0000002","statement":[{"text":"The final refined atomic model contains residues 140–288 and 335–416 for chains A and C, and 140–289 and 337–416 for chains B and D, respectively.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"15941357","version":2,"reference_html":"Engineering a dimeric caspase-9: a re-evaluation of the induced proximity model for caspase activation. <i> Chao Y, Shiozaki EN, Srinivasula SM, Rigotti DJ, Fairman R, Shi Y. </i> PLoS Biol, 2005","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2AR9"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-24T18:33:31.977Z"}},{"region_id":"DP02860r002","ec_ontology":"ECO","end":321,"term_id":"GO:0005515","start":316,"version":3,"statement":[{"text":"In order to help elucidate the molecular mechanisms of cIAP1 activity and to explore the possibility of targeting cIAP1 activity with small molecules, we have determined the crystal structures of the BIR3 domain of cIAP1 in complex with N-terminal hexapeptides of the activated (cleaved) forms of both SMAC and caspase-9. ","type":"Introduction"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q13490","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19153467","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3D9T"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"fquaglia","reference_html":"The structure of the BIR3 domain of cIAP1 in complex with the N-terminal peptides of SMAC and caspase-9. <i> Kulathila R, Vash B, Sage D, Cornell-Kennon S, Wright K, Koehn J, Stams T, Clark K, Price A. </i> Acta Crystallogr D Biol Crystallogr, 2009","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-24T18:36:39.078Z"}},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q13490","partner_end":null}],"ec_ontology":"ECO","end":321,"region_id":"DP02860r003","start":316,"term_id":"GO:0005515","statement":[{"text":"The caspase-9 peptide (ATPFQE) binds to the BIR3 domain of cIAP2 with an affinity of 48 ± 2nM, whereas the SMAC peptide (AVPIAQ) binds with an affinity of 85 ± 8nM.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"surface plasmon resonance evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19153467","version":3,"reference_html":"The structure of the BIR3 domain of cIAP1 in complex with the N-terminal peptides of SMAC and caspase-9. <i> Kulathila R, Vash B, Sage D, Cornell-Kennon S, Wright K, Koehn J, Stams T, Clark K, Price A. </i> Acta Crystallogr D Biol Crystallogr, 2009","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001269","term_name":"protein binding","curator_orcid":"0000-0002-0341-4888","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-24T18:36:00.164Z"}}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02860","date":"2020-05-11T13:49:42.312Z","organism":"Homo sapiens","regions_counter":3,"name":"Caspase-9","dataset":["Cancer-related proteins"],"UniParc":"UPI000003AEFF","uniref100":"UniRef100_P55211","uniref90":"UniRef90_P55211","uniref50":"UniRef50_P55211","genes":[{"name":{"value":"CASP9"},"synonyms":[{"value":"MCH6"}]}],"alphafold_very_low_content":0.17548076923076922,"disorder_content":0.11057692307692307,"disprot_consensus":{"full":[{"start":289,"end":334,"type":"D"}],"Structural state":[{"start":289,"end":334,"type":"D"}],"Molecular function":[{"start":316,"end":321,"type":"F"}]}},{"acc":"P08670","features":{"gene3D":[{"start":134,"end":251,"id":"G3DSA:1.20.5.1160","name":"Vasodilator-stimulated phosphoprotein"}],"pfam":[{"id":"PF00038","name":"Intermediate filament protein","start":102,"end":410},{"id":"PF04732","name":"Intermediate filament head (DNA binding) region","start":7,"end":101}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MSTRSVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYASSPGGVYATRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNLDSLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE","length":466,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":144,"region_id":"DP02862r001","start":99,"term_id":"IDPO:0000002","statement":[{"text":"Surprisingly, a clear electron density is only observed starting from residues 144 and 149 in chains A and B, respectively. Moreover, SDS-PAGE analysis of the crystals confirmed that the fragment was intact (mass 11.1 kDa). In addition, first few traceable residues in each chain are mobile, as evident from increased B-factors. Both the coil 1A and most of the linker L1 are therefore completely disordered in this crystal structure.","type":"Results"},{"text":"With the exception of residues 144 to 149 (shown in orange) in chain A, the rest of the linker L1 and coil 1A is disordered in the crystals.","type":"Results"},{"text":"Although the presence of the nonhelical head domains is essential for proper tetramer stabilization, the precise alignment of the dimers forming the tetramer appears to depend on the complementarity of their surface charge distribution patterns, while the structural plasticity of linker L1 and coil 1A plays a role in the subsequent IF assembly process.","type":"Abstract"},{"text":"Coil 1A corresponds to region 99-139 and linker L1 corresponds to region 140-147.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22869704","version":2,"reference_html":"Atomic structure of the vimentin central α-helical domain and its implications for intermediate filament assembly. <i> Chernyatina AA, Nicolet S, Aebi U, Herrmann H, Strelkov SV. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3SSU"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":144,"region_id":"DP02862r002","start":99,"term_id":"IDPO:0000002","statement":[{"text":"Surprisingly, a clear electron density is only observed starting from residues 144 and 149 in chains A and B, respectively. Moreover, SDS-PAGE analysis of the crystals confirmed that the fragment was intact (mass 11.1 kDa). In addition, first few traceable residues in each chain are mobile, as evident from increased B-factors. Both the coil 1A and most of the linker L1 are therefore completely disordered in this crystal structure.","type":"Results"},{"text":"With the exception of residues 144 to 149 (shown in orange) in chain A, the rest of the linker L1 and coil 1A is disordered in the crystals.","type":"Results"},{"text":"Although the presence of the nonhelical head domains is essential for proper tetramer stabilization, the precise alignment of the dimers forming the tetramer appears to depend on the complementarity of their surface charge distribution patterns, while the structural plasticity of linker L1 and coil 1A plays a role in the subsequent IF assembly process.","type":"Abstract"},{"text":"Coil 1A corresponds to region 99-139 and linker L1 corresponds to region 140-147.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22869704","version":2,"reference_html":"Atomic structure of the vimentin central α-helical domain and its implications for intermediate filament assembly. <i> Chernyatina AA, Nicolet S, Aebi U, Herrmann H, Strelkov SV. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3SSU"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":144,"region_id":"DP02862r003","start":99,"term_id":"IDPO:0000002","statement":[{"text":"Surprisingly, a clear electron density is only observed starting from residues 144 and 149 in chains A and B, respectively. Moreover, SDS-PAGE analysis of the crystals confirmed that the fragment was intact (mass 11.1 kDa). In addition, first few traceable residues in each chain are mobile, as evident from increased B-factors. Both the coil 1A and most of the linker L1 are therefore completely disordered in this crystal structure.","type":"Results"},{"text":"With the exception of residues 144 to 149 (shown in orange) in chain A, the rest of the linker L1 and coil 1A is disordered in the crystals.","type":"Results"},{"text":"Although the presence of the nonhelical head domains is essential for proper tetramer stabilization, the precise alignment of the dimers forming the tetramer appears to depend on the complementarity of their surface charge distribution patterns, while the structural plasticity of linker L1 and coil 1A plays a role in the subsequent IF assembly process.","type":"Abstract"},{"text":"Coil 1A corresponds to region 99-139 and linker L1 corresponds to region 140-147.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22869704","version":2,"reference_html":"Atomic structure of the vimentin central α-helical domain and its implications for intermediate filament assembly. <i> Chernyatina AA, Nicolet S, Aebi U, Herrmann H, Strelkov SV. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007689","cross_refs":[{"db":"PDB","id":"3SSU"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":144,"region_id":"DP02862r004","start":99,"term_id":"GO:0060090","statement":[{"text":"Surprisingly, a clear electron density is only observed starting from residues 144 and 149 in chains A and B, respectively. Moreover, SDS-PAGE analysis of the crystals confirmed that the fragment was intact (mass 11.1 kDa). In addition, first few traceable residues in each chain are mobile, as evident from increased B-factors. Both the coil 1A and most of the linker L1 are therefore completely disordered in this crystal structure.","type":"Results"},{"text":"With the exception of residues 144 to 149 (shown in orange) in chain A, the rest of the linker L1 and coil 1A is disordered in the crystals.","type":"Results"},{"text":"Although the presence of the nonhelical head domains is essential for proper tetramer stabilization, the precise alignment of the dimers forming the tetramer appears to depend on the complementarity of their surface charge distribution patterns, while the structural plasticity of linker L1 and coil 1A plays a role in the subsequent IF assembly process.","type":"Abstract"},{"text":"Coil 1A corresponds to region 99-139 and linker L1 corresponds to region 140-147.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"22869704","version":3,"reference_html":"Atomic structure of the vimentin central α-helical domain and its implications for intermediate filament assembly. <i> Chernyatina AA, Nicolet S, Aebi U, Herrmann H, Strelkov SV. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"3SSU"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_12","ncbi_taxon_id":9606,"disprot_id":"DP02862","date":"2020-05-11T17:20:42.990Z","organism":"Homo sapiens","regions_counter":4,"name":"Vimentin","dataset":[],"UniParc":"UPI0000465140","uniref100":"UniRef100_P08670","uniref90":"UniRef90_P08670","uniref50":"UniRef50_P08670","genes":[{"name":{"value":"VIM"}}],"alphafold_very_low_content":0.2317596566523605,"disorder_content":0.09871244635193133,"disprot_consensus":{"full":[{"start":99,"end":144,"type":"D"}],"Structural state":[{"start":99,"end":144,"type":"D"}],"Molecular function":[{"start":99,"end":144,"type":"F"}]}},{"acc":"P62558","features":{"gene3D":[],"pfam":[{"id":"PF18090","name":"Centromere-binding protein HTH domain","start":158,"end":232}]},"creator":"fquaglia","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"sequence":"MKRAPVIPKHTLNTQPVEDTSLSTPAAPMVDSLIARVGVMARGNAITLPVCGRDVKFTLEVLRGDSVEKTSRVWSGNERDQELLTEDALDDLIPSFLLTGQQTPAFGRRVSGVIEIADGSRRRKAAALTESDYRVLVGELDDEQMAALSRLGNDYRPTSAYERGQRYASRLQNEFAGNISALADAENISRKIITRCINTAKLPKSVVALFSHPGELSARSGDALQKAFTDKEELLKQQASNLHEQKKAGVIFEAEEVITLLTSVLKTSSASRTSLSSRHQFAPGATVLYKGDKMVLNLDRSRVPTECIEKIEAILKELEKPAP","length":323,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":323,"region_id":"DP02863r001","start":272,"term_id":"IDPO:0000002","statement":[{"text":"SopB is a multidomain protein, which like P1 ParB contains an all-helical DNA-binding domain that is flexibly attached to a compact (β3–α)2 dimer-domain.","type":"Abstract"},{"text":"However, density was only observed for SopB residues 157–271 from one subunit and 157–270 of the second subunit. These residues contain all the determinants required for sequence specific binding to the sopC consensus site (36). The absence of density for the SopB N- and C-terminal regions suggested that either these regions were highly flexible or were proteolysed during crystallization. Consistent with the former possibility, the first and last residues observed, 157 and 271, each face into large solvent channels, which could easily accommodate the disordered or flexibly attached domains.","type":"Results"},{"text":"The structure indicates that SopB consists of three main regions: 1–155, 155–272 and 272–323 that are flexibly linked.","type":"Results"},{"text":"The fact that the N- and C-terminal regions are not visible in the FL SopB-18mer structure indicates that these three principal regions of SopB are flexibly attached.","type":"Results"},{"text":"The C-terminal dimerization domain of SopB is highly flexible.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20236989","version":2,"reference_html":"Insight into F plasmid DNA segregation revealed by structures of SopB and SopB-DNA complexes. <i> Schumacher MA, Piro KM, Xu W. </i> Nucleic Acids Res, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3MKY"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":323,"region_id":"DP02863r002","start":275,"term_id":"IDPO:0000011","statement":[{"text":"Previous studies suggest that SopB residues 275–323 are involved in dimer formation and therefore must form a folded domain, consistent with our CD studies (36). Thus, we next produced and crystallized SopB(275–323).","type":"Results"},{"text":"The structure revealed that, indeed, residues 275–323 form a highly intertwined dimer composed of 3 β-strands and 1 α-helix with topology (β1; 276–281, β2; 284–289, β3; 292–298 α1; 306–318) (Figure 2A–D). The dimer is stabilized almost entirely by backbone, β-strand hydrogen bonds. The interface of the dimer buries an extensive 5990 Å2 of protein surface from solvent, consistent with it forming the primary dimerization domain of SopB, which anchors the SopB subunits on a palindromic DNA site (see Figure 3). That the C-domain is a physiologically relevant oligomer is also supported by the finding that the identical dimer is observed twice in the crystal (the dimers overlay with an RMSD of 0.6 Å) and size exclusion chromatography data providing a MW of 13 kDa for SopB(275–323) [compared to a calculated MW of 11.2 kDa for a SopB(275–323) dimer].","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20236989","version":2,"reference_html":"Insight into F plasmid DNA segregation revealed by structures of SopB and SopB-DNA complexes. <i> Schumacher MA, Piro KM, Xu W. </i> Nucleic Acids Res, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"3KZ5"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":323,"region_id":"DP02863r003","start":275,"term_id":"IDPO:0000011","statement":[{"text":"Previous studies suggest that SopB residues 275–323 are involved in dimer formation and therefore must form a folded domain, consistent with our CD studies (36). Thus, we next produced and crystallized SopB(275–323).","type":"Results"},{"text":"The structure revealed that, indeed, residues 275–323 form a highly intertwined dimer composed of 3 β-strands and 1 α-helix with topology (β1; 276–281, β2; 284–289, β3; 292–298 α1; 306–318) (Figure 2A–D). The dimer is stabilized almost entirely by backbone, β-strand hydrogen bonds. The interface of the dimer buries an extensive 5990 Å2 of protein surface from solvent, consistent with it forming the primary dimerization domain of SopB, which anchors the SopB subunits on a palindromic DNA site (see Figure 3). That the C-domain is a physiologically relevant oligomer is also supported by the finding that the identical dimer is observed twice in the crystal (the dimers overlay with an RMSD of 0.6 Å) and size exclusion chromatography data providing a MW of 13 kDa for SopB(275–323) [compared to a calculated MW of 11.2 kDa for a SopB(275–323) dimer].","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"chromatography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20236989","version":2,"reference_html":"Insight into F plasmid DNA segregation revealed by structures of SopB and SopB-DNA complexes. <i> Schumacher MA, Piro KM, Xu W. </i> Nucleic Acids Res, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","cross_refs":[{"db":"PDB","id":"3KZ5"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":323,"region_id":"DP02863r004","start":275,"term_id":"IDPO:0000060","statement":[{"text":"Previous studies suggest that SopB residues 275–323 are involved in dimer formation and therefore must form a folded domain, consistent with our CD studies (36). Thus, we next produced and crystallized SopB(275–323).","type":"Results"},{"text":"The structure revealed that, indeed, residues 275–323 form a highly intertwined dimer composed of 3 β-strands and 1 α-helix with topology (β1; 276–281, β2; 284–289, β3; 292–298 α1; 306–318) (Figure 2A–D). The dimer is stabilized almost entirely by backbone, β-strand hydrogen bonds. The interface of the dimer buries an extensive 5990 Å2 of protein surface from solvent, consistent with it forming the primary dimerization domain of SopB, which anchors the SopB subunits on a palindromic DNA site (see Figure 3). That the C-domain is a physiologically relevant oligomer is also supported by the finding that the identical dimer is observed twice in the crystal (the dimers overlay with an RMSD of 0.6 Å) and size exclusion chromatography data providing a MW of 13 kDa for SopB(275–323) [compared to a calculated MW of 11.2 kDa for a SopB(275–323) dimer].","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20236989","version":3,"reference_html":"Insight into F plasmid DNA segregation revealed by structures of SopB and SopB-DNA complexes. <i> Schumacher MA, Piro KM, Xu W. </i> Nucleic Acids Res, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"3KZ5"}],"term_name":"self-assembly","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2020_12","ncbi_taxon_id":83333,"disprot_id":"DP02863","date":"2020-05-11T17:51:19.117Z","organism":"Escherichia coli (strain K12)","regions_counter":4,"name":"Protein SopB","dataset":[],"UniParc":"UPI0000001013","uniref100":"UniRef100_P62559","uniref90":"UniRef90_P62559","uniref50":"UniRef50_P62559","genes":[{"name":{"value":"sopB"},"synonyms":[{"value":"B"}],"olnNames":[{"value":"ECOK12F047"}]}],"alphafold_very_low_content":0.08668730650154799,"disorder_content":0.1609907120743034,"disprot_consensus":{"full":[{"start":272,"end":274,"type":"D"},{"start":275,"end":323,"type":"T"}],"Structural state":[{"start":272,"end":323,"type":"D"}],"Structural transition":[{"start":275,"end":323,"type":"T"}],"Disorder function":[{"start":275,"end":323,"type":"F"}]}},{"acc":"P83917","features":{"gene3D":[],"pfam":[{"id":"PF00385","name":"Chromo (CHRromatin Organisation MOdifier) domain","start":21,"end":69},{"id":"PF01393","name":"Chromo shadow domain","start":113,"end":172}]},"creator":"lchemes","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MGKKQNKKKVEEVLEEEEEEYVVEKVLDRRVVKGKVEYLLKWKGFSDEDNTWEPEENLDCPDLIAEFLQSQKTAHETDKSEGGKRKADSDSEDKGEESKPKKKKEESEKPRGFARGLEPERIIGATDSSGELMFLMKWKNSDEADLVPAKEANVKCPQVVISFYEERLTWHSYPSEDDDKKDDKN","length":185,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":103,"region_id":"DP02864r001","start":79,"term_id":"IDPO:0000002","statement":[{"text":"Limited proteolysis of MoMOD1 revealed two regions that are resistant to digestion, these correspond to the conserved sequences in the HP1-like proteins[…] The results suggest that the MoMOD1 protein consists of two structural domains, residues 10-78 and 104-171, connected by an exposed linker.","type":"Discussion"}],"curator_id":"lchemes","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"9171360","version":2,"reference_html":"Structure of the chromatin binding (chromo) domain from mouse modifier protein 1. <i> Ball LJ, Murzina NV, Broadhurst RW, Raine AR, Archer SJ, Stott FJ, Murzin AG, Singh PB, Domaille PJ, Laue ED. </i> EMBO J, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":103,"region_id":"DP02864r002","start":79,"term_id":"IDPO:0000033","statement":[{"text":"Limited proteolysis of MoMOD1 revealed two regions that are resistant to digestion, these correspond to the conserved sequences in the HP1-like proteins[…] The results suggest that the MoMOD1 protein consists of two structural domains, residues 10-78 and 104-171, connected by an exposed linker.","type":"Discussion"}],"curator_id":"lchemes","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"9171360","version":3,"reference_html":"Structure of the chromatin binding (chromo) domain from mouse modifier protein 1. <i> Ball LJ, Murzina NV, Broadhurst RW, Raine AR, Archer SJ, Stott FJ, Murzin AG, Singh PB, Domaille PJ, Laue ED. </i> EMBO J, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","term_name":"flexible linker","curator_orcid":"0000-0003-0192-9906","ec_go":"IDA","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":10090,"disprot_id":"DP02864","date":"2020-05-11T20:47:13.256Z","organism":"Mus musculus","regions_counter":2,"name":"Chromobox protein homolog 1","dataset":[],"UniParc":"UPI0000021A5B","uniref100":"UniRef100_P83916","uniref90":"UniRef90_P83916","uniref50":"UniRef50_P83916","genes":[{"name":{"value":"Cbx1"},"synonyms":[{"value":"Cbx"}]}],"alphafold_very_low_content":0.13513513513513514,"disorder_content":0.13513513513513514,"disprot_consensus":{"full":[{"start":79,"end":103,"type":"D"}],"Structural state":[{"start":79,"end":103,"type":"D"}],"Disorder function":[{"start":79,"end":103,"type":"F"}]}},{"acc":"P05205","features":{"gene3D":[],"pfam":[{"id":"PF00385","name":"Chromo (CHRromatin Organisation MOdifier) domain","start":24,"end":72},{"id":"PF01393","name":"Chromo shadow domain","start":143,"end":202}]},"creator":"lchemes","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"sequence":"MGKKIDNPESSAKVSDAEEEEEEYAVEKIIDRRVRKGKVEYYLKWKGYPETENTWEPENNLDCQDLIQQYEASRKDEEKSAASKKDRPSSSAKAKETQGRASSSTSTASKRKSEEPTAPSGNKSKRTTDAEQDTIPVSGSTGFDRGLEAEKILGASDNNGRLTFLIQFKGVDQAEMVPSSVANEKIPRMVIHFYEERLSWYSDNED","length":206,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":140,"region_id":"DP02865r001","start":131,"term_id":"IDPO:0000002","statement":[{"text":" By combining results of NMR and crystallography, we conclude that the CSD module is made up of residues 141 through 201 in the HP1a.","type":"Results"}],"curator_id":"vnugnes","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"21472955","version":3,"reference_html":"The HP1a disordered C terminus and chromo shadow domain cooperate to select target peptide partners. <i> Mendez DL, Kim D, Chruszcz M, Stephens GE, Minor W, Khorasanizadeh S, Elgin SC. </i> Chembiochem, 2011","date":"2023-12-13T20:51:50.911Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3P7J"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-14T15:11:28.720Z"}},{"start":131,"end":140,"reference_id":"21472955","reference_source":"pmid","reference_html":"The HP1a disordered C terminus and chromo shadow domain cooperate to select target peptide partners. <i> Mendez DL, Kim D, Chruszcz M, Stephens GE, Minor W, Khorasanizadeh S, Elgin SC. </i> Chembiochem, 2011","date":"2023-12-13T20:48:57.323Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02865r002","statement":[{"text":"By measuring the heteronuclear NOE (Nuclear Overhauser Effect) data for backbone amides, we identified disordered regions, which exist at the N-terminus (residues 131 to 140 of intact HP1a), and the CTE (residues 202 to 206), as well as segments within the CSD module (residues 158–159, 162, 170, and 172–173) (Figure 3A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-14T15:11:38.604Z"}}],"released":"2021_06","ncbi_taxon_id":7227,"disprot_id":"DP02865","date":"2020-05-11T21:09:05.525Z","organism":"Drosophila melanogaster","regions_counter":2,"name":"Heterochromatin protein 1","dataset":["Condensates-related proteins"],"UniParc":"UPI000016BB1F","uniref100":"UniRef100_P05205","uniref90":"UniRef90_P05205","uniref50":"UniRef50_P05205","genes":[{"name":{"value":"Su(var)205"},"synonyms":[{"value":"HP1"}],"orfNames":[{"value":"CG8409"}]}],"alphafold_very_low_content":0.1262135922330097,"disorder_content":0.04854368932038835,"disprot_consensus":{"full":[{"start":131,"end":140,"type":"D"}],"Structural state":[{"start":131,"end":140,"type":"D"}]}},{"acc":"A1Z9S6","features":{"pfam":[]},"creator":"lchemes","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"sequence":"MEDIEYLDEYKDLVLPGIKSSAPTASSAGVPRQRRISSDSSNSSSIDADIFQKLFHGKYLDDELLKEGSGSKSQDRRRRPPSPSSSDESNDALEALFCGKSSQSKLSKRRERYESFDSVDDLGEALMRPSHRLTVPKPSTSQAGSKKSQDAAPHRSISNSSSSNIAMSSGQTYACPKNKKTNSVANKTAVSANGDKWASGKNKTVTIVKPQKTDLRPSRLEPKTDPLNLGDLYGDSDSDSSYEYESDFYGDQDSDEEDEPVIDISTDTSRTTSVADTVTPVVSDDEGQEPQSELNQRHANDQESFLSSTYERLQSYLSNLSSAEPPPIYKKQNSARKSRSNEKKPSSSQQVKHANEQSAASDKEANKKERDLEPPEASSSAKSSASKASGSRKLYDVANNATLEAVERMSLDLAEQIMEIDVERSYEFEKRSASKSRSLSRSKIPADSSTSQLGHVRKLTYSSERLDQPEPLGTQLRRSKSESLPKRGRPRGQKQRKNRGATMEEKSANCRDGEGEPVKRKRGRPRKIIPKEEAKTAETENTIESLNTNVPLSIDTSKENPETETVNLEVPIKQDELVSDLDNAKELTGSTNLPQDDIEMASNHQETDLKCAPDRVALDKSESTPKVEEEQLCKVDTPSDTALDESKVSESAKNHIELEDKDKDKEETQKESPNGNSKETNENSVIVTNEVELPAKKAEAKAEAGNIVEESDSQLAEDFKLAEEILAAEVGKGVEANEVSVTSVQGEQNPVIEIVKELEQETISEVVPAQNDQSSVEDQTLADKENPVEKPSPVKAPSSSKDEPPAEENLPAPDQDPIEQQKTPVAKNQQHDKEHNEAPKAESLSVSDIPSSSVTPSKKRNHSSPANTPKKSKEIEALQSSVPRRALRSDKATPQNLRESRSKRTLKTELTLLMDDTMRRSSPRLGRSPAESHSSHERSPMEKKVTVSKLAKDLITIDKEKEIELKSLPDASETKDVKITKTTTASDTSILTDENPSSSKTEMKKLKGKPLKAKKMSRTSETEVKKAIADSNEDIPSIFSIKCVEEHLTSSESEQKDEKEELLCPKPQIDCTNTDLEQSTAIETDTEQVEEKRSNRRKSRRIRNEKFKTETDTLSDHLDAKKAENASLEISMRPKCTLETQQSDPVTAKNKRNSGRLSRKEKSVINAAKSEKDKSPSAISQSTERKQLLNENPSKKDKKTEQSGNKKEAVVGPLDKTETSSSTNIIDKKSNESFDSAMQPSDRLNQKESAFTKLSSISSPKKIMKDQDKDLDALSKGGDSNPTIRDTGEDSRQTDKKHQENDTKHEEEDSSKLKANIDETKSSSEKDAEPISKDSSQDSAKPRLSKPKSRNKRKKNEKKPNDSIAESDIEGGFQVNTETVQATCSTPSESNKKDMVKSDETNEEPNLSETEIGRIRKRGQAFHIENPKDDLHITPQNENQSIAGVNFEKQVPLPESVESDTPIMKIPTKTYLMCTKNKTSLLSASEDPDIVLEPQKLITTSKGDSNPDLDNANNLETSSTQDPKEHEFSDQTFTDNSDIIPSCTKKSQIVFPTTPTKSSDQTKNSFITPNRSPKSKRNVSKEAKRLDNSFEESQNAASESSASKVQKELRTPTASCRKLRVLIKRTPTSSLPTNSRKSIFKKTPAKSKRLTKILESMEKTPSREPSVSLGEVNPDSDPVAAESVAVLHESDRDLESNEIPNEEVFEDTEEASAEDTDNKLKKKEDDHELEVNDICAASKNPITDDSTKDASSNKSTDSDVLQETKDELSNSLINATQGEDTPIKELTEEEVPNNKTVEDESKKQEILKDLEPDNAALEEDTASTAKAAEEMDLYIKEKSNVKSVLAEPETDVTDDEELAQSPIPNSSETTSVTDDPEPSTSSVVKRSLRKREADSSQPDEAAKRKQRQDVEKSLTGKKEQVKPARRRQLAEVEERPSLKRSKTESEAKSTVQGKYISIIGNETIMSSTTAPIRETNREAASTSPSARKSAVQEAKHVETTKHIILGPPGKKLLHSDSPAAEVKKPMVQTLLSSTLSLQKPSTLDDGSPLKIRKSLKKSIADENIDGDQSIFSSSSVLNKNTSVVAPRKVNISVSLLQSKDTQVETAASSSETPILTKKEKLKTQKSTKKPEGNKKTESKKKSLVQGPQMKTQKSEEAVSGPKILNKYLKSETESSRKTVSTVTGRKQIGQLEVLKKPESRKSEESLVEAISRKKQSQVQRLSKIDGRKSEGTSLPQPDVSKSETALKAALPKETEFPVQDAEIEKMSKGRGHQNAVKNTKTEQPKSKPKTEVRSLQAEAATELMDSMDSQSDVSDIRATFPESQGIFNVPGHMTRAISSNRSLAPTPTPMSDSQRNASKERFTPVSDQKKPIRESQTLSKRRARGGRNQPLVSKRKAGEAEDGTAVINPKRPREMDEEDHPQQNDHVQESAFAAFPVKITAASSVIPQVVRSTGNTVPQNISPRKLCVKINRRPYNKWLRSTQERNEEQEGSRNVTSLPLLGETSETDSAAESMSESILQSQVQSEPAIQPLPASQPDSCTLQASDLRIRESSAQLAPIAAYDSPAANDSSTSPALDIAPESAQTAKATLNTALCPSTEKHLPDEPTLLESSKKVAEPQKLQTFQAKCLPVPIPEVKSEPEDIMDEHSPNEPMPMVAAAPATPQPHAITEDAGPDTIQVNTLGVSTSSRPLELHSIPSASDPDGNPNAIGQTKMYSFLYPKRYKQSYDDVGLDFCCPNLDGPMRAIDFTRLHSKAEVPVLEIPQFLVITTKFISKADKNMPSKVRAKLELLDKSKERDSSKLTPTATTPTADPTGPSSFSPAPASVGPATQPFPSIIQNLLSAPLPDPGLFNHPTTVDPSTSTPVVSGSSSSTTISADLDSLSKQLPRGTKLIKKSVQQVATNPSLAGTSMVINASPSFIQLPPICPNDKQRVELQARVQMFDLVLQTLSRRAANLSVAERQRTIEEIVRTSSLMAIDVDVGTKLLENYVHYLNKATSTMTPLTPAQINSSLGASTSSTLSKSIATSDIPQQGKKISADHAQQRSSLPATIPLYDGGRNTLGFPYSCSKSTAGRKSSYVATSTPVKASTSQAAAAAALGNAQPRSTLGIPKSVREDASQFVNLNTTVCMPAPRTNAKKKPGTSGPLKSMNSSPAVQKPALCKQQTAPARTLSKSTVSSVARAKSTGSLSAVLGETPADEFVSPAGMSLSTTGNPNVFIINHAVQSEESILPDSNSSVGHMETTVIKGELDDSAEIII","length":3257,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":2512,"region_id":"DP02866r001","start":2415,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"we identified an LCVKI motif in HP2 that binds to the HP1a CSD. The binding affinity of the HP2 fragment is approximately two orders of magnitude higher than that of peptides from PIWI (with a PRVKV motif), AF10 (with a PLVVL motif), or CG15356 (with LYPLL and LSIVA motifs). ","type":"Abstract"},{"text":"To investigate the hypothesis that tertiary structure in HP2 [10] is required for binding, we performed the reciprocal experiment, examining the 2D [15N-1H] HSQC spectrum of the 15N labeled HP2 fragment in the presence of unlabeled CSD (Figure 1C). We find that in the absence of the CSD the HP2 fragment is disordered. Both 1D 1H and 2D [15N-1H] HSQC spectra lack chemical shift dispersion. In the presence of the CSD, a limited set of resonances become perturbed (Figure 1C)","type":"Results"}],"curator_id":"lchemes","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"21472955","version":2,"reference_html":"The HP1a disordered C terminus and chromo shadow domain cooperate to select target peptide partners. <i> Mendez DL, Kim D, Chruszcz M, Stephens GE, Minor W, Khorasanizadeh S, Elgin SC. </i> Chembiochem, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:30:21.260Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":2512,"region_id":"DP02866r002","start":2415,"term_id":"GO:0005515","unpublished":true,"statement":[{"text":"we identified an LCVKI motif in HP2 that binds to the HP1a CSD. The binding affinity of the HP2 fragment is approximately two orders of magnitude higher than that of peptides from PIWI (with a PRVKV motif), AF10 (with a PLVVL motif), or CG15356 (with LYPLL and LSIVA motifs). ","type":"Abstract"},{"text":"To investigate the hypothesis that tertiary structure in HP2 [10] is required for binding, we performed the reciprocal experiment, examining the 2D [15N-1H] HSQC spectrum of the 15N labeled HP2 fragment in the presence of unlabeled CSD (Figure 1C). We find that in the absence of the CSD the HP2 fragment is disordered. Both 1D 1H and 2D [15N-1H] HSQC spectra lack chemical shift dispersion. In the presence of the CSD, a limited set of resonances become perturbed (Figure 1C)","type":"Results"}],"curator_id":"lchemes","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"21472955","version":3,"reference_html":"The HP1a disordered C terminus and chromo shadow domain cooperate to select target peptide partners. <i> Mendez DL, Kim D, Chruszcz M, Stephens GE, Minor W, Khorasanizadeh S, Elgin SC. </i> Chembiochem, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:30:22.757Z","curator_name":"Federica Quaglia"},"term_name":"protein binding","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":2512,"region_id":"DP02866r003","start":2415,"term_id":"GO:0098772","unpublished":true,"statement":[{"text":"we identified an LCVKI motif in HP2 that binds to the HP1a CSD. The binding affinity of the HP2 fragment is approximately two orders of magnitude higher than that of peptides from PIWI (with a PRVKV motif), AF10 (with a PLVVL motif), or CG15356 (with LYPLL and LSIVA motifs). ","type":"Abstract"},{"text":"To investigate the hypothesis that tertiary structure in HP2 [10] is required for binding, we performed the reciprocal experiment, examining the 2D [15N-1H] HSQC spectrum of the 15N labeled HP2 fragment in the presence of unlabeled CSD (Figure 1C). We find that in the absence of the CSD the HP2 fragment is disordered. Both 1D 1H and 2D [15N-1H] HSQC spectra lack chemical shift dispersion. In the presence of the CSD, a limited set of resonances become perturbed (Figure 1C)","type":"Results"}],"curator_id":"lchemes","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"21472955","version":3,"reference_html":"The HP1a disordered C terminus and chromo shadow domain cooperate to select target peptide partners. <i> Mendez DL, Kim D, Chruszcz M, Stephens GE, Minor W, Khorasanizadeh S, Elgin SC. </i> Chembiochem, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:30:10.668Z","curator_name":"Federica Quaglia"},"term_name":"molecular function regulator","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":2512,"region_id":"DP02866r004","start":2415,"term_id":"GO:0098772","unpublished":true,"statement":[{"text":"we identified an LCVKI motif in HP2 that binds to the HP1a CSD. The binding affinity of the HP2 fragment is approximately two orders of magnitude higher than that of peptides from PIWI (with a PRVKV motif), AF10 (with a PLVVL motif), or CG15356 (with LYPLL and LSIVA motifs). ","type":"Abstract"},{"text":"To determine the affinity of HP2 for the HP1a CSD we performed fluorescence polarization assays. We designed a short HP2 peptide (22 aa) with the critical valine residue near the center […] Using this assay, we observed that both HP2 and PIWI binding are shifted to the millimolar range by I191E and W200A mutations in HP1a. Thus, both peptides bind using a similar mechanism; they bind to the CSD dimer and require the PXVXL platform (Figure 4A).","type":"Results"}],"curator_id":"lchemes","released":"2023_12","ec_name":"fluorescence polarization evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"21472955","version":3,"reference_html":"The HP1a disordered C terminus and chromo shadow domain cooperate to select target peptide partners. <i> Mendez DL, Kim D, Chruszcz M, Stephens GE, Minor W, Khorasanizadeh S, Elgin SC. </i> Chembiochem, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006277","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:30:10.055Z","curator_name":"Federica Quaglia"},"term_name":"molecular function regulator","curator_orcid":"0000-0003-0192-9906","ec_go":"IPI","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2023_12","ncbi_taxon_id":7227,"disprot_id":"DP02866","date":"2020-05-11T21:21:41.676Z","organism":"Drosophila melanogaster","regions_counter":5,"name":"Su(Var)2-HP2, isoform A","dataset":[],"UniParc":"UPI000007BADC","uniref100":"UniRef100_A1Z9S6","uniref90":"UniRef90_A1Z9S6","uniref50":"UniRef50_A1Z9S6","genes":[{"name":{"value":"Su(var)2-HP2","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF58230.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF58230.1"}},{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0026427","url":"http://flybase.org/reports/FBgn0026427.html"}}]},"synonyms":[{"value":"Dmel\\CG12864","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF58230.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF58230.1"}}]},{"value":"HP2","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF58230.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF58230.1"}}]},{"value":"Hp2","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF58230.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF58230.1"}}]},{"value":"SU(VAR)2-HP2","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF58230.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF58230.1"}}]}],"orfNames":[{"value":"CG12864","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF58230.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF58230.1"}},{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0026427","url":"http://flybase.org/reports/FBgn0026427.html"}}]},{"value":"Dmel_CG12864","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF58230.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF58230.1"}}]}]}],"disorder_content":0.030089038992938286,"disprot_consensus":{"full":[{"start":2415,"end":2512,"type":"D"}],"Structural state":[{"start":2415,"end":2512,"type":"D"}],"Molecular function":[{"start":2415,"end":2512,"type":"F"}]}},{"acc":"P40381","features":{"gene3D":[],"pfam":[{"id":"PF00385","name":"Chromo (CHRromatin Organisation MOdifier) domain","start":81,"end":133},{"id":"PF01393","name":"Chromo shadow domain","start":275,"end":327}]},"creator":"lchemes","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"sequence":"MKKGGVRSYRRSSTSKRSVIDDDSEPELPSMTKEAIASHKADSGSSDNEVESDHESKSSSKKLKENAKEEEGGEEEEEDEYVVEKVLKHRMARKGGGYEYLLKWEGYDDPSDNTWSSEADCSGCKQLIEAYWNEHGGRPEPSKRKRTARPKKPEAKEPSPKSRKTDEDKHDKDSNEKIEDVNEKTIKFADKSQEEFNENGPPSGQPNGHIESDNESKSPSQKESNESEDIQIAETPSNVTPKKKPSPEVPKLPDNRELTVKQVENYDSWEDLVSSIDTIERKDDGTLEIYLTWKNGAISHHPSTITNKKCPQKMLQFYESHLTFRENE","length":328,"regions":[{"start":1,"end":74,"reference_id":"22683269","reference_source":"pmid","reference_html":"HP1(Swi6) mediates the recognition and destruction of heterochromatic RNA transcripts. <i> Keller C, Adaixo R, Stunnenberg R, Woolcock KJ, Hiller S, Bühler M. </i> Mol Cell, 2012","date":"2022-11-15T15:00:14.200Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02867r005","statement":[{"text":"HP1Swi6 consists of four domains: An N-terminal domain (NTD, residues 1–74), which is presumably flexibly disordered; a chromodomain (CD, residues 75–139), which binds K9-methylated histone tails (Bannister et al., 2001); a hinge region (H, residues 140–264); and a C-terminal chromo shadow domain (CSD, residues 265–328) (Cowieson et al., 2000).","type":"Results"},{"text":"The chemical shift dispersion and intensities of the resonances in full-length HP1Swi6 indicated the CD and the CSD to be folded domains and the NTD and the hinge region to be flexibly unfolded polypeptide segments, as expected from predictions of the secondary structure.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:54:54.644Z"}},{"start":140,"end":264,"reference_id":"22683269","reference_source":"pmid","reference_html":"HP1(Swi6) mediates the recognition and destruction of heterochromatic RNA transcripts. <i> Keller C, Adaixo R, Stunnenberg R, Woolcock KJ, Hiller S, Bühler M. </i> Mol Cell, 2012","date":"2022-11-15T15:01:36.567Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02867r006","statement":[{"text":"HP1Swi6 consists of four domains: An N-terminal domain (NTD, residues 1–74), which is presumably flexibly disordered; a chromodomain (CD, residues 75–139), which binds K9-methylated histone tails (Bannister et al., 2001); a hinge region (H, residues 140–264); and a C-terminal chromo shadow domain (CSD, residues 265–328) (Cowieson et al., 2000).","type":"Results"},{"text":"The chemical shift dispersion and intensities of the resonances in full-length HP1Swi6 indicated the CD and the CSD to be folded domains and the NTD and the hinge region to be flexibly unfolded polypeptide segments, as expected from predictions of the secondary structure. ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:54:56.335Z"}},{"start":140,"end":264,"reference_id":"22683269","reference_source":"pmid","reference_html":"HP1(Swi6) mediates the recognition and destruction of heterochromatic RNA transcripts. <i> Keller C, Adaixo R, Stunnenberg R, Woolcock KJ, Hiller S, Bühler M. </i> Mol Cell, 2012","date":"2022-11-15T15:06:44.502Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","region_id":"DP02867r007","statement":[{"text":"By using NMR chemical shift titrations monitored on amide resonances in the flexible hinge region, we determined the binding constant of full-length HP1Swi6 to a 20-mer RNA as 38 ± 13 μM (Figure 3C). These results demonstrate that HP1Swi6 is able to bind RNA alone and that the hinge region is substantially involved in this binding interaction.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:54:58.146Z"}},{"start":140,"end":264,"reference_id":"22683269","reference_source":"pmid","reference_html":"HP1(Swi6) mediates the recognition and destruction of heterochromatic RNA transcripts. <i> Keller C, Adaixo R, Stunnenberg R, Woolcock KJ, Hiller S, Bühler M. </i> Mol Cell, 2012","date":"2022-11-15T15:07:44.575Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","region_id":"DP02867r008","statement":[{"text":"To test whether the hinge region also confers RNA binding properties to HP1Swi6, we purified recombinant CD, hinge, and CSD. In contrast to the CD and the CSD, the isolated hinge region was sufficient for strong RNA binding (Figure 3B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T11:45:44.956Z"}}],"released":"2023_12","ncbi_taxon_id":284812,"disprot_id":"DP02867","date":"2020-05-12T00:19:18.597Z","organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","regions_counter":8,"name":"Chromatin-associated protein swi6","dataset":["Condensates-related proteins","RNA-binding proteins"],"UniParc":"UPI00001362A2","uniref100":"UniRef100_P40381","uniref90":"UniRef90_P40381","uniref50":"UniRef50_P40381","genes":[{"name":{"value":"swi6"},"orfNames":[{"value":"SPAC664.01c"},{"value":"SPAC824.10c"}]}],"alphafold_very_low_content":0.27134146341463417,"disorder_content":0.6067073170731707,"disprot_consensus":{"full":[{"start":1,"end":74,"type":"D"},{"start":140,"end":264,"type":"D"}],"Structural state":[{"start":1,"end":74,"type":"D"},{"start":140,"end":264,"type":"D"}],"Molecular function":[{"start":140,"end":264,"type":"F"}]}},{"acc":"Q9Y5S9","features":{"gene3D":[{"start":1,"end":168,"id":"G3DSA:3.30.70.330","name":"G3DSA:3.30.70.330"}],"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":75,"end":144}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MADVLDLHEAGGEDFAMDEDGDESIHKLKEKAKKRKGRGFGSEEGSRARMREDYDSVEQDGDEPGPQRSVEGWILFVTGVHEEATEEDIHDKFAEYGEIKNIHLNLDRRTGYLKGYTLVEYETYKEAQAAMEGLNGQDLMGQPISVDWCFVRGPPKGKRRGGRRRSRSPDRRRR","length":174,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":63,"region_id":"DP02868r001","start":50,"term_id":"IDPO:0000002","statement":[{"text":"Although Y14 residues 50–168 are present in the Y14t-Magoh complex crystals, only residues 64–165 are sufficiently well ordered to be visualized in the electron density.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12781131","version":2,"reference_html":"Structure of the Y14-Magoh core of the exon junction complex. <i> Lau CK, Diem MD, Dreyfuss G, Van Duyne GD. </i> Curr Biol, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1P27"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-08-19T12:55:39.254Z"}}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02868","date":"2020-05-12T08:55:06.174Z","organism":"Homo sapiens","regions_counter":1,"name":"RNA-binding protein 8A","dataset":[],"UniParc":"UPI0000004160","uniref100":"UniRef100_Q9Y5S9","uniref90":"UniRef90_Q9Y5S9","uniref50":"UniRef50_Q9Y5S9","genes":[{"name":{"value":"RBM8A"},"synonyms":[{"value":"RBM8"}],"orfNames":[{"value":"HSPC114"},{"value":"MDS014"}]}],"alphafold_very_low_content":0.07471264367816093,"disorder_content":0.08045977011494253,"disprot_consensus":{"full":[{"start":50,"end":63,"type":"D"}],"Structural state":[{"start":50,"end":63,"type":"D"}]}},{"acc":"Q16630","features":{"gene3D":[{"start":81,"end":172,"id":"G3DSA:3.30.70.330","name":"G3DSA:3.30.70.330"}],"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":83,"end":152},{"id":"PF25524","name":"CPSF6-like, RSLD domain, N-terminal region","start":412,"end":514}]},"creator":"ireményi","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MADGVDHIDIYADVGEEFNQEAEYGGHDQIDLYDDVISPSANNGDAPEDRDYMDTLPPTVGDDVGKGAAPNVVYTYTGKRIALYIGNLTWWTTDEDLTEAVHSLGVNDILEIKFFENRANGQSKGFALVGVGSEASSKKLMDLLPKRELHGQNPVVTPCNKQFLSQFEMQSRKTTQSGQMSGEGKAGPPGGSSRAAFPQGGRGRGRFPGAVPGGDRFPGPAGPGGPPPPFPAGQTPPRPPLGPPGPPGPPGPPPPGQVLPPPLAGPPNRGDRPPPPVLFPGQPFGQPPLGPLPPGPPPPVPGYGPPPGPPPPQQGPPPPPGPFPPRPPGPLGPPLTLAPPPHLPGPPPGAPPPAPHVNPAFFPPPTNSGMPTSDSRGPPPTDPYGRPPPYDRGDYGPPGREMDTARTPLSEAEFEEIMNRNRAISSSAISRAVSDASAGDYGSAIETLVTAISLIKQSKVSADDRCKVLISSLQDCLHGIESKSYGSGSRRERSRERDHSRSREKSRRHKSRSRDRHDDYYRERSRERERHRDRDRDRDRERDREREYRHR","length":551,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":80,"region_id":"DP02869r001","start":13,"term_id":"IDPO:0000002","statement":[{"text":"Although diffraction data were collected from a complex containing residues 13-235 of CFIm68 (Figure S2B), the refined electron density map showed interpretable density only for residues 81-172, a segment which comprises the entire RRM domain (residues 81-160).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21295486","version":2,"reference_html":"Crystal structure of a human cleavage factor CFI(m)25/CFI(m)68/RNA complex provides an insight into poly(A) site recognition and RNA looping. <i> Yang Q, Coseno M, Gilmartin GM, Doublié S. </i> Structure, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3Q2S"},{"db":"PDB","id":"3Q2T"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":235,"region_id":"DP02869r002","start":173,"term_id":"IDPO:0000002","statement":[{"text":"Although diffraction data were collected from a complex containing residues 13-235 of CFIm68 (Figure S2B), the refined electron density map showed interpretable density only for residues 81-172, a segment which comprises the entire RRM domain (residues 81-160).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21295486","version":2,"reference_html":"Crystal structure of a human cleavage factor CFI(m)25/CFI(m)68/RNA complex provides an insight into poly(A) site recognition and RNA looping. <i> Yang Q, Coseno M, Gilmartin GM, Doublié S. </i> Structure, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3Q2S"},{"db":"PDB","id":"3Q2T"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":519,"region_id":"DP02869r003","start":481,"term_id":"IDPO:0000002","statement":[{"text":"Similar to the TNPO3-SRSF1 co-crystal structure, only a fraction of the input CPSF6 RSLD (9 of the 70 residues) was ordered in the density map.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30916345","version":2,"reference_html":"Differential role for phosphorylation in alternative polyadenylation function versus nuclear import of SR-like protein CPSF6. <i> Jang S, Cook NJ, Pye VE, Bedwell GJ, Dudek AM, Singh PK, Cherepanov P, Engelman AN. </i> Nucleic Acids Res, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6GX9"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":550,"region_id":"DP02869r004","start":531,"term_id":"IDPO:0000002","statement":[{"text":"Similar to the TNPO3-SRSF1 co-crystal structure, only a fraction of the input CPSF6 RSLD (9 of the 70 residues) was ordered in the density map.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30916345","version":2,"reference_html":"Differential role for phosphorylation in alternative polyadenylation function versus nuclear import of SR-like protein CPSF6. <i> Jang S, Cook NJ, Pye VE, Bedwell GJ, Dudek AM, Singh PK, Cherepanov P, Engelman AN. </i> Nucleic Acids Res, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6GX9"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":496,"region_id":"DP02869r005","start":492,"term_id":"IDPO:0000045","statement":[{"text":"Four sites in the RSLD, Ser494, Ser500, Ser511 and Ser513, were phosphorylated in both endogenous CPSF6 and exogenously expressed CPSF6[551] protein.","type":"Results"},{"text":"Includes the phosphorylated Ser494.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"mass spectrometry evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30916345","version":2,"reference_html":"Differential role for phosphorylation in alternative polyadenylation function versus nuclear import of SR-like protein CPSF6. <i> Jang S, Cook NJ, Pye VE, Bedwell GJ, Dudek AM, Singh PK, Cherepanov P, Engelman AN. </i> Nucleic Acids Res, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001230","term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":502,"region_id":"DP02869r006","start":498,"term_id":"IDPO:0000045","statement":[{"text":"Four sites in the RSLD, Ser494, Ser500, Ser511 and Ser513, were phosphorylated in both endogenous CPSF6 and exogenously expressed CPSF6[551] protein.","type":"Results"},{"text":"Includes the phosphorylated Ser500.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"mass spectrometry evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30916345","version":2,"reference_html":"Differential role for phosphorylation in alternative polyadenylation function versus nuclear import of SR-like protein CPSF6. <i> Jang S, Cook NJ, Pye VE, Bedwell GJ, Dudek AM, Singh PK, Cherepanov P, Engelman AN. </i> Nucleic Acids Res, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001230","term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":515,"region_id":"DP02869r007","start":509,"term_id":"IDPO:0000045","statement":[{"text":"Four sites in the RSLD, Ser494, Ser500, Ser511 and Ser513, were phosphorylated in both endogenous CPSF6 and exogenously expressed CPSF6[551] protein.","type":"Results"},{"text":"Includes the phosphorylated Ser511 and Ser513.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"mass spectrometry evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30916345","version":2,"reference_html":"Differential role for phosphorylation in alternative polyadenylation function versus nuclear import of SR-like protein CPSF6. <i> Jang S, Cook NJ, Pye VE, Bedwell GJ, Dudek AM, Singh PK, Cherepanov P, Engelman AN. </i> Nucleic Acids Res, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001230","term_name":"phosphorylation display site","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Biological process","ec_ontology":"ECO","end":551,"region_id":"DP02869r008","start":481,"term_id":"GO:0051179","statement":[{"text":"The RSLD confers CPSF6 nuclear import without any contribution from PY-NLS","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"microscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"30916345","version":3,"reference_html":"Differential role for phosphorylation in alternative polyadenylation function versus nuclear import of SR-like protein CPSF6. <i> Jang S, Cook NJ, Pye VE, Bedwell GJ, Dudek AM, Singh PK, Cherepanov P, Engelman AN. </i> Nucleic Acids Res, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001232","term_name":"localization","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02869","date":"2020-05-12T09:57:17.659Z","organism":"Homo sapiens","regions_counter":11,"name":"Cleavage and polyadenylation specificity factor subunit 6","dataset":["RNA-binding proteins"],"UniParc":"UPI000006D566","uniref100":"UniRef100_Q16630","uniref90":"UniRef90_Q16630","uniref50":"UniRef50_Q16630","genes":[{"name":{"value":"CPSF6","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:13871","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:13871"}}]},"synonyms":[{"value":"CFIM68","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9659921","url":"http://www.ncbi.nlm.nih.gov/pubmed/9659921","alternativeUrl":"https://europepmc.org/abstract/MED/9659921"}}]}]}],"alphafold_very_low_content":0.33212341197822143,"disorder_content":0.3448275862068966,"disprot_consensus":{"full":[{"start":13,"end":80,"type":"D"},{"start":173,"end":235,"type":"D"},{"start":481,"end":519,"type":"D"},{"start":520,"end":530,"type":"F"},{"start":531,"end":550,"type":"D"},{"start":551,"end":551,"type":"F"}],"Structural state":[{"start":13,"end":80,"type":"D"},{"start":173,"end":235,"type":"D"},{"start":481,"end":519,"type":"D"},{"start":531,"end":550,"type":"D"}],"Disorder function":[{"start":492,"end":496,"type":"F"},{"start":498,"end":502,"type":"F"},{"start":509,"end":515,"type":"F"}],"Biological process":[{"start":481,"end":551,"type":"F"}]}},{"acc":"P22893","features":{"gene3D":[],"pfam":[{"id":"PF00642","name":"Zinc finger C-x8-C-x5-C-x3-H type (and similar)","start":96,"end":121},{"id":"PF00642","name":"Zinc finger C-x8-C-x5-C-x3-H type (and similar)","start":134,"end":160}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MDLSAIYESLQSMSHDLSSDHGGTESLGGLWNINSDSIPSGVTSRLTGRSTSLVEGRSCGWVPPPPGFAPLAPRPGPELSPSPTSPTATPTTSSRYKTELCRTYSESGRCRYGAKCQFAHGLGELRQANRHPKYKTELCHKFYLQGRCPYGSRCHFIHNPTEDLALPGQPHVLRQSISFSGLPSGRRSSPPPPGFSGPSLSSCSFSPSSSPPPPGDLPLSPSAFSAAPGTPVTRRDPNQACCPSCRRSTTPSTIWGPLGGLARSPSAHSLGSDPDDYASSGSSLGGSDSPVFEAGVFGPPQTPAPPRRLPIFNRISVSE","length":319,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":163,"region_id":"DP02870r001","start":129,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The solution structure of Nup475(Y143K) was solved with use of a combination of 2D and 3D experiments on nonlabeled, 15N-labeled, and 15N/13C-labeled protein samples. Although the fragment was 77 amino acids in length, intraresidue NOEs were observed only for residues 9−42, and resonance assignments are reported for residues 5−42. This region has the amino acid sequence -T5TSSRYKTELC15RTYSESGRC24RYGAKC30QFAH34GLGELRQA42- and corresponds to residues 91−128 in the murine protein. The assigned 15N HSQC of the peptide demonstrates that nearly all of the shifted resonances correspond to the well-structured domain, while the unassigned resonances are sharp, poorly dispersed, and occur in the region of the spectrum normally associated with unstructured elements (Figure 1).","type":"Results"},{"text":"The overlap introduced by the peaks due to the unstructured domain made the 13C/15N HSQC-NOESY and TOCSY spectra difficult to assign unambiguously.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"12515557","version":2,"reference_html":"A Cys3His zinc-binding domain from Nup475/tristetraprolin: a novel fold with a disklike structure. <i> Amann BT, Worthington MT, Berg JM. </i> Biochemistry, 2003","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"1M9O"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2023_12","ncbi_taxon_id":10090,"disprot_id":"DP02870","date":"2020-05-12T11:02:37.976Z","organism":"Mus musculus","regions_counter":1,"name":"mRNA decay activator protein ZFP36","dataset":[],"UniParc":"UPI00000019A3","uniref100":"UniRef100_P22893","uniref90":"UniRef90_P22893","uniref50":"UniRef50_P26651","genes":[{"name":{"value":"Zfp36","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"7559666","url":"http://www.ncbi.nlm.nih.gov/pubmed/7559666","alternativeUrl":"https://europepmc.org/abstract/MED/7559666"}},{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:99180","url":"http://www.informatics.jax.org/marker/MGI:99180"}}]},"synonyms":[{"value":"Nup475","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"1699942","url":"http://www.ncbi.nlm.nih.gov/pubmed/1699942","alternativeUrl":"https://europepmc.org/abstract/MED/1699942"}}]},{"value":"Tis11","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"2915901","url":"http://www.ncbi.nlm.nih.gov/pubmed/2915901","alternativeUrl":"https://europepmc.org/abstract/MED/2915901"}}]},{"value":"Tis11a"},{"value":"Ttp","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"2204625","url":"http://www.ncbi.nlm.nih.gov/pubmed/2204625","alternativeUrl":"https://europepmc.org/abstract/MED/2204625"}}]}]}],"alphafold_very_low_content":0.34169278996865204,"disorder_content":0.109717868338558,"disprot_consensus":{"full":[{"start":129,"end":163,"type":"D"}],"Structural state":[{"start":129,"end":163,"type":"D"}]}},{"acc":"Q5D1E7","features":{"gene3D":[],"pfam":[{"id":"PF11977","name":"Zc3h12a-like Ribonuclease NYN domain","start":135,"end":289},{"id":"PF18039","name":"UBA-like domain","start":49,"end":89},{"id":"PF18561","name":"Endoribonuclease Regnase 1/ ZC3H12 C-terminal domain","start":547,"end":590}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MSDPCGTKPVQESNPTMSLWSLEDRHSSQGRPQPDQDPVAKEAPTSELQMKVDFFRKLGYSSSEIHSVLQKLGVQADTNTVLGELVKHGSATERECQALTAPSPQPPLVPRGGSTPKPSTLEPSLPEEDREGSDLRPVVIDGSNVAMSHGNKEVFSCRGILLAVNWFLERGHTDITVFVPSWRKEQPRPDVPITDQHILRELEKKKILVFTPSRRVGGKRVVCYDDRFIVKLAFESDGVVVSNDTYRDLQGERQEWKRFIEERLLMYSFVNDKFMPPDDPLGRHGPSLDNFLRKKPLPSEHRKQPCPYGKKCTYGIKCRFFHPERPSRPQRSVADELRANALLSPPRTPVKDKSSQRPSPASQSSSVSLEAEPGSLDGKKLGARSSPGPHREGSPQTCAPAGRSLPVSGGSFGPTEWLAHTQDSLPYTSQECLDSGIGSLESQMSELWGVRGGSPGESGPTRGPYAGYHSYGSKVPAAPSFSPFRPAMGAGHFSVPTDYVPPPPTYPSREYWSEPYPLPPPTPVLQEPQRPSPGAGGGPWGRVGDLAKERAGVYTKLCGVFPPHLVEAVMRRFPQLLDPQQLAAEILSYKSQHLSE","length":596,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":339,"region_id":"DP02871r001","start":296,"term_id":"IDPO:0000002","statement":[{"text":"We analyzed Rengase-1 derived from Mus musculus and solved the structures of the four domains; NTD, PIN, ZF, and CTD individually by X-ray crystallography or NMR (Fig. 1a–e). X-ray crystallography was attempted for the fragment containing both the PIN and ZF domains, however, electron density was observed only for the PIN domain (Fig. 1c), consistent with a previous report on Regnase-1 derived from Homo sapiens11.","type":"Results"},{"text":"A Regnase-1 construct consisting of PIN and ZF domains derived from Mus musculus was crystallized; however, the electron density of the ZF domain was low, indicating that the ZF domain is highly mobile in the absence of target mRNA or possibly other protein-protein interactions.","type":"Discussion"}],"curator_id":"vnugnes","released":"2025_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"26927947","version":3,"reference_html":"Structural basis for the regulation of enzymatic activity of Regnase-1 by domain-domain interactions. <i> Yokogawa M, Tsushima T, Noda NN, Kumeta H, Enokizono Y, Yamashita K, Standley DM, Takeuchi O, Akira S, Inagaki F. </i> Sci Rep, 2016","date":"2025-10-15T14:17:31.530Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5H9W"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29101","entry_name":null}]},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":326,"region_id":"DP02871r002","start":301,"term_id":"GO:0003729","statement":[{"text":"Our NMR experiments confirmed direct binding of the ZF domain to IL-6 mRNA with a Kd of 10 ± 1.1 μM. Furthermore, an in vitro gel shift assay indicated that Regnase-1 containing the ZF domain enhanced target mRNA-binding, but the protein-RNA complex remained in the bottom of the well without entering into the polyacrylamide gel. These results indicate that Regnase-1 directly binds to RNA and precipitates under such experimental conditions.","type":"Discussion"}],"curator_id":"esalladini","released":"2022_03","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"26927947","version":4,"reference_html":"Structural basis for the regulation of enzymatic activity of Regnase-1 by domain-domain interactions. <i> Yokogawa M, Tsushima T, Noda NN, Kumeta H, Enokizono Y, Yamashita K, Standley DM, Takeuchi O, Akira S, Inagaki F. </i> Sci Rep, 2016","date":"2022-03-08T14:12:10.926Z","reference_source":"pmid","ec_id":"ECO:0001807","term_name":"mRNA binding","curator_orcid":"0000-0002-5152-5953","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns.\" [GOC:kmv, GOC:pr, SO:0000234]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"NCBIgene","id":"NM_031168.2","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-15T14:33:12.868Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":326,"region_id":"DP02871r003","start":301,"term_id":"GO:0003729","statement":[{"text":"Our NMR experiments confirmed direct binding of the ZF domain to IL-6 mRNA with a Kd of 10 ± 1.1 μM. Furthermore, an in vitro gel shift assay indicated that Regnase-1 containing the ZF domain enhanced target mRNA-binding, but the protein-RNA complex remained in the bottom of the well without entering into the polyacrylamide gel. These results indicate that Regnase-1 directly binds to RNA and precipitates under such experimental conditions.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"26927947","version":3,"reference_html":"Structural basis for the regulation of enzymatic activity of Regnase-1 by domain-domain interactions. <i> Yokogawa M, Tsushima T, Noda NN, Kumeta H, Enokizono Y, Yamashita K, Standley DM, Takeuchi O, Akira S, Inagaki F. </i> Sci Rep, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"mRNA binding","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns.\" [GOC:kmv, GOC:pr, SO:0000234]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-15T14:33:08.747Z"}},{"start":306,"end":322,"reference_id":"26927947","reference_source":"pmid","reference_html":"Structural basis for the regulation of enzymatic activity of Regnase-1 by domain-domain interactions. <i> Yokogawa M, Tsushima T, Noda NN, Kumeta H, Enokizono Y, Yamashita K, Standley DM, Takeuchi O, Akira S, Inagaki F. </i> Sci Rep, 2016","date":"2025-10-15T14:30:26.813Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008270","term_name":"zinc ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"BMRB","id":"25719"},{"db":"PDB","id":"2N5K"}],"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"29105","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP02871r006","statement":[{"text":"Three Cys residues and one His residue responsible for Zn2+-binding were shown in sticks.","type":"Figure"},{"text":"NMR data shows the residues Cys306, Cys312, Cys318 and His322 bind to a Zn+2 ion. ","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a zinc ion (Zn).\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2021_06","ncbi_taxon_id":10090,"disprot_id":"DP02871","date":"2020-05-12T11:26:59.620Z","organism":"Mus musculus","regions_counter":6,"name":"Endoribonuclease ZC3H12A","dataset":["Stress response proteins"],"UniParc":"UPI00004E153C","uniref100":"UniRef100_Q5D1E7","uniref90":"UniRef90_Q5D1E7","uniref50":"UniRef50_Q5D1E8","genes":[{"name":{"value":"Zc3h12a","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"19322177","url":"http://www.ncbi.nlm.nih.gov/pubmed/19322177","alternativeUrl":"https://europepmc.org/abstract/MED/19322177"}},{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:2385891","url":"http://www.informatics.jax.org/marker/MGI:2385891"}}]},"synonyms":[{"value":"Mcpip","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16574901","url":"http://www.ncbi.nlm.nih.gov/pubmed/16574901","alternativeUrl":"https://europepmc.org/abstract/MED/16574901"}}]},{"value":"Mcpip1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"19666473","url":"http://www.ncbi.nlm.nih.gov/pubmed/19666473","alternativeUrl":"https://europepmc.org/abstract/MED/19666473"}}]}]}],"alphafold_very_low_content":0.4463087248322148,"disorder_content":0.0738255033557047,"disprot_consensus":{"full":[{"start":296,"end":339,"type":"D"}],"Structural state":[{"start":296,"end":339,"type":"D"}],"Molecular function":[{"start":301,"end":326,"type":"F"}]}},{"acc":"Q8N5H7","features":{"gene3D":[{"start":203,"end":323,"id":"G3DSA:3.30.505.10","name":"SH2 domain"},{"start":540,"end":860,"id":"G3DSA:1.10.840.10","name":"Ras guanine-nucleotide exchange factors catalytic domain"}],"pfam":[{"id":"PF00017","name":"SH2 domain","start":220,"end":300},{"id":"PF00617","name":"RasGEF domain","start":635,"end":712}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MTEGTKKTSKKFKFFKFKGFGSLSNLPRSFTLRRSSASISRQSHLEPDTFEATQDDMVTVPKSPPAYARSSDMYSHMGTMPRPSIKKAQNSQAARQAQEAGPKPNLVPGGVPDPPGLEAAKEVMVKATGPLEDTPAMEPNPSAVEVDPIRKPEVPTGDVEEERPPRDVHSERAAGEPEAGSDYVKFSKEKYILDSSPEKLHKELEEELKLSSTDLRSHAWYHGRIPREVSETLVQRNGDFLIRDSLTSLGDYVLTCRWRNQALHFKINKVVVKAGESYTHIQYLFEQESFDHVPALVRYHVGSRKAVSEQSGAIIYCPVNRTFPLRYLEASYGLGQGSSKPASPVSPSGPKGSHMKRRSVTMTDGLTADKVTRSDGCPTSTSLPRPRDSIRSCALSMDQIPDLHSPMSPISESPSSPAYSTVTRVHAAPAAPSATALPASPVARRSSEPQLCPGSAPKTHGESDKGPHTSPSHTLGKASPSPSLSSYSDPDSGHYCQLQPPVRGSREWAATETSSQQARSYGERLKELSENGAPEGDWGKTFTVPIVEVTSSFNPATFQSLLIPRDNRPLEVGLLRKVKELLAEVDARTLARHVTKVDCLVARILGVTKEMQTLMGVRWGMELLTLPHGRQLRLDLLERFHTMSIMLAVDILGCTGSAEERAALLHKTIQLAAELRGTMGNMFSFAAVMGALDMAQISRLEQTWVTLRQRHTEGAILYEKKLKPFLKSLNEGKEGPPLSNTTFPHVLPLITLLECDSAPPEGPEPWGSTEHGVEVVLAHLEAARTVAHHGGLYHTNAEVKLQGFQARPELLEVFSTEFQMRLLWGSQGASSSQARRYEKFDKVLTALSHKLEPAVRSSEL","length":860,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":769,"region_id":"DP02872r001","start":756,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"curator_id":"vnugnes","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"22081014","version":3,"reference_html":"NSP-Cas protein structures reveal a promiscuous interaction module in cell signaling. <i> Mace PD, Wallez Y, Dobaczewska MK, Lee JJ, Robinson H, Pasquale EB, Riedl SJ. </i> Nat Struct Mol Biol, 2011","date":"2022-08-04T14:52:36.072Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3T6G"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2023_12","ncbi_taxon_id":9606,"disprot_id":"DP02872","date":"2020-05-12T11:45:44.450Z","organism":"Homo sapiens","regions_counter":1,"name":"SH2 domain-containing protein 3C","dataset":[],"UniParc":"UPI000006EC87","uniref100":"UniRef100_Q8N5H7","uniref90":"UniRef90_Q8N5H7","uniref50":"UniRef50_Q9QZS8","genes":[{"name":{"value":"SH2D3C"},"synonyms":[{"value":"NSP3"}],"orfNames":[{"value":"UNQ272/PRO309/PRO34088"}]}],"alphafold_very_low_content":0.46744186046511627,"disorder_content":0.01627906976744186,"disprot_consensus":{"full":[{"start":756,"end":769,"type":"D"}],"Structural state":[{"start":756,"end":769,"type":"D"}]}},{"acc":"P97465","features":{"gene3D":[{"start":149,"end":257,"id":"G3DSA:2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":149,"end":257,"id":"G3DSA:2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"}],"pfam":[{"id":"PF00169","name":"PH domain","start":5,"end":117},{"id":"PF02174","name":"PTB domain (IRS-1 type)","start":160,"end":252}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MDGAVMEGPLFLQSQRFGTKRWRKTWAVLYPASPHGVARLEFFDHKGSSSRGGRGGSRRLDCKMIRLAECVSVVPVTVESPPEPGAVAFRLDTAQRSHLLAADAVSSTAWVQTLCRTAFPKGGWALAQTENQPKFSALEMLENSLYSPTWEGSQFWVTSQKTEASERCGLQGSYILRVEAEKLTLLTLGAQSQILEPLLFWPYTLLRRYGRDKVMFSFEAGRRCPSGPGTFTFQTSQGNDIFQAVEAAIQQQKAQGKVGQAQDILRTDSHDGETEGKTVPPPVPQDPLGSPPALYAEPLDSLRIPPGPSQDSVYSDPLGSTPAGAGEGVHSKKPLYWDLYGHVQQQLLKTKLTDSKEDPIYDEPEGLAPAPPRGLYDLPQEPRDAWWCQARLKEEGYELPYNPATDDYAVPPPRSPKPAPAPKPQGLILPESGTTRGSGSKGFSSDTALYSQVQKSGTSGAWDCGLSKVGNDRAGVKSEGST","length":482,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":266,"region_id":"DP02873r001","start":257,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The electron density was of good quality and well defined for most of the structure. The final model consists of residues 154-256 of mouse Dok1 in chain A, residues 154-254 in chain B, and 16 water molecules.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"14607833","version":2,"reference_html":"Structural basis for the specific recognition of RET by the Dok1 phosphotyrosine binding domain. <i> Shi N, Ye S, Bartlam M, Yang M, Wu J, Liu Y, Sun F, Han X, Peng X, Qiang B, Yuan J, Rao Z. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1UEF"},{"db":"PDB","id":"1P5T"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-10T16:38:14.333Z"}}],"released":"2023_12","ncbi_taxon_id":10090,"disprot_id":"DP02873","date":"2020-05-12T11:53:34.524Z","organism":"Mus musculus","regions_counter":1,"name":"Docking protein 1","dataset":[],"UniParc":"UPI000052927B","uniref100":"UniRef100_P97465","uniref90":"UniRef90_P97465","uniref50":"UniRef50_P97465","genes":[{"name":{"value":"Dok1"},"synonyms":[{"value":"Dok"}]}],"alphafold_very_low_content":0.34647302904564314,"disorder_content":0.02074688796680498,"disprot_consensus":{"full":[{"start":257,"end":266,"type":"D"}],"Structural state":[{"start":257,"end":266,"type":"D"}]}},{"acc":"Q61033","features":{"gene3D":[{"start":102,"end":158,"id":"G3DSA:1.10.720.40","name":"G3DSA:1.10.720.40"},{"start":102,"end":158,"id":"G3DSA:1.10.720.40","name":"G3DSA:1.10.720.40"}],"pfam":[{"id":"PF03020","name":"LEM domain","start":110,"end":154},{"id":"PF08198","name":"Thymopoietin protein","start":2,"end":49},{"id":"PF11560","name":"Lamina-associated polypeptide 2 alpha","start":459,"end":692}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MPEFLEDPSVLTKDKLKSELVANNVTLPAGEQRKDVYVQLYLQHLTARNRPPLAAGANSKGPPDFSSDEEREPTPVLGSGASVGRGRGAVGRKATKKTDKPRLEDKDDLDVTELSNEELLDQLVRYGVNPGPIVGTTRKLYEKKLLKLREQGTESRSSTPLPTVSSSAENTRQNGSNDSDRYSDNDEGKKKEHKKVKSARDCVPFSELASTPSGAFFQGISFPEISTRPPLGRTELQAAKKVQTTKRDPPRETCTDTALPGKGQTHKLAPGRSLFIPSESSYDRCVEKSSSPSSQREFAARLVSAAASPSLIRETTTTYSKDIVENICRGGKSRAQPLRAEEPGVSDQSVFSSEREVLQESERSQVISPPLAQAIRDYVNSLLVQGGVGSLPGTSDSVPTLDVENICKRLSQSSYQDSESLSPPRKVPRLSEKPARGGDSGSCVAFQNTPGSEHRSSFAKSVVSHSLTTLGVEVSKPPPQHDKIEASEPSFPLHESILKVVEEEWQQIDRQLPSVACRYPVSSIEAARILSVPKVDDEILGFISEATPRAATQASSTESCDKHLDLALCRSYEAAASALQIAAHTAFVAKSLQADISQAAQIINSDPSDAQQALRILNRTYDAASYLCDAAFDEVRMSACAMGSSTMGRRYLWLKDCKISPASKNKLTVAPFKGGTLFGGEVHKVIKKRGNKQ","length":693,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":491,"region_id":"DP02874r001","start":472,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"LAP2α-CTD forms an elongated dimer that is ∼94 Å long and 54 Å wide (Figure 3). In one monomer (orange in Figure 3), the current model contains amino acid residues His465–Gly471 and Pro492–Arg689. In the other monomer (green in Figure 3), the model contains residues His465–Glu473, Pro489–Ser544, and Ser556–Val685. The missing parts were disordered and did not have interpretable electron density.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"17562312","version":2,"reference_html":"Structural basis for dimerization of LAP2alpha, a component of the nuclear lamina. <i> Bradley CM, Jones S, Huang Y, Suzuki Y, Kvaratskhelia M, Hickman AB, Craigie R, Dyda F. </i> Structure, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2V0X"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":51,"end":110,"reference_id":"17562312","reference_source":"pmid","reference_html":"Structural basis for dimerization of LAP2alpha, a component of the nuclear lamina. <i> Bradley CM, Jones S, Huang Y, Suzuki Y, Kvaratskhelia M, Hickman AB, Craigie R, Dyda F. </i> Structure, 2007","date":"2022-11-10T15:25:15.494Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02874r003","statement":[{"text":"The constant region (residues 1–186) consists of a LEM-like domain (residues 1–50) connected by a flexible tether to a LEM domain between residues 111 and 153 (Cai et al., 2001). ","type":"Figure"}]},{"start":51,"end":110,"reference_id":"17562312","reference_source":"pmid","reference_html":"Structural basis for dimerization of LAP2alpha, a component of the nuclear lamina. <i> Bradley CM, Jones S, Huang Y, Suzuki Y, Kvaratskhelia M, Hickman AB, Craigie R, Dyda F. </i> Structure, 2007","date":"2022-11-10T15:36:36.746Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02874r004","statement":[{"text":"The constant region (residues 1–186) consists of a LEM-like domain (residues 1–50) connected by a flexible tether to a LEM domain between residues 111 and 153 (Cai et al., 2001). ","type":"Figure"}]}],"released":"2023_12","ncbi_taxon_id":10090,"disprot_id":"DP02874","date":"2020-05-12T15:54:24.195Z","organism":"Mus musculus","regions_counter":4,"name":"Lamina-associated polypeptide 2, isoforms alpha/zeta","dataset":[],"UniParc":"UPI00000290E5","uniref100":"UniRef100_Q61033","uniref90":"UniRef90_Q61033","uniref50":"UniRef50_P42166","genes":[{"name":{"value":"Tmpo"},"synonyms":[{"value":"Lap2"}]}],"alphafold_very_low_content":0.481962481962482,"disorder_content":0.11544011544011544,"disprot_consensus":{"full":[{"start":51,"end":110,"type":"D"},{"start":472,"end":491,"type":"D"}],"Structural state":[{"start":51,"end":110,"type":"D"},{"start":472,"end":491,"type":"D"}],"Disorder function":[{"start":51,"end":110,"type":"F"}]}},{"acc":"P55789","features":{"gene3D":[{"start":81,"end":205,"id":"G3DSA:1.20.120.310","name":"ERV/ALR sulfhydryl oxidase domain"}],"pfam":[{"id":"PF04777","name":"Erv1 / Alr family","start":104,"end":196}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MAAPGERGRFHGGNLFFLPGGARSEMMDDLATDARGRGAGRRDAAASASTPAQAPTSDSPVAEDASRRRPCRACVDFKTWMRTQQKRDTKFREDCPPDREELGRHSWAVLHTLAAYYPDLPTPEQQQDMAQFIHLFSKFYPCEECAEDLRKRLCRNHPDTRTRACFTQWLCHLHNEVNRKLGKPDFDCSKVDERWRDGWKDGSCD","length":205,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":93,"region_id":"DP02875r001","start":81,"term_id":"IDPO:0000002","statement":[{"text":"The N-terminus of each subunit was disordered, with the final model including residues 94–205 from each subunit.","type":"Methods"},{"text":"In all subunits, the first 27 N-terminal residues of the sfALR construct (Figure S1; comprising 14 residues of the tag and linker, followed by 13 residues from the N-terminus of the cytokine form of ALR) were disordered.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20593814","version":2,"reference_html":"Structure of the human sulfhydryl oxidase augmenter of liver regeneration and characterization of a human mutation causing an autosomal recessive myopathy . <i> Daithankar VN, Schaefer SA, Dong M, Bahnson BJ, Thorpe C. </i> Biochemistry, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3MBG"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-03T20:25:49.640Z"}}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02875","date":"2020-05-12T16:12:09.078Z","organism":"Homo sapiens","regions_counter":1,"name":"FAD-linked sulfhydryl oxidase ALR","dataset":["NDDs-related proteins"],"UniParc":"UPI0000140A12","uniref100":"UniRef100_P55789","uniref90":"UniRef90_P55789","uniref50":"UniRef50_P55789","genes":[{"name":{"value":"GFER"},"synonyms":[{"value":"ALR"},{"value":"HERV1"},{"value":"HPO"}]}],"alphafold_very_low_content":0.22439024390243903,"disorder_content":0.06341463414634146,"disprot_consensus":{"full":[{"start":81,"end":93,"type":"D"}],"Structural state":[{"start":81,"end":93,"type":"D"}]}},{"acc":"Q8N884","features":{"gene3D":[],"pfam":[{"id":"PF03281","name":"Mab-21 protein nucleotidyltransferase domain","start":214,"end":389},{"id":"PF20266","name":"Mab-21 protein HhH/H2TH-like domain","start":405,"end":509}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MQPWHGKAMQRASEAGATAPKASARNARGAPMDPTESPAAPEAALPKAGKFGPARKSGSRQKKSAPDTQERPPVRATGARAKKAPQRAQDTQPSDATSAPGAEGLEPPAAREPALSRAGSCRQRGARCSTKPRPPPGPWDVPSPGLPVSAPILVRRDAAPGASKLRAVLEKLKLSRDDISTAAGMVKGVVDHLLLRLKCDSAFRGVGLLNTGSYYEHVKISAPNEFDVMFKLEVPRIQLEEYSNTRAYYFVKFKRNPKENPLSQFLEGEILSASKMLSKFRKIIKEEINDIKDTDVIMKRKRGGSPAVTLLISEKISVDITLALESKSSWPASTQEGLRIQNWLSAKVRKQLRLKPFYLVPKHAKEGNGFQEETWRLSFSHIEKEILNNHGKSKTCCENKEEKCCRKDCLKLMKYLLEQLKERFKDKKHLDKFSSYHVKTAFFHVCTQNPQDSQWDRKDLGLCFDNCVTYFLQCLRTEKLENYFIPEFNLFSSNLIDKRSKEFLTKQIEYERNNEFPVFDEF","length":522,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":305,"region_id":"DP02876r001","start":289,"term_id":"IDPO:0000002","statement":[{"text":"The final model of human cGAS, except for the disordered regions (residues 218-222, 255-260, 289-305, 363-370 and 426-427), was refined to an R-factor of 20.6% (R free = 25.2%).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24116191","version":2,"reference_html":"Structural and functional analyses of DNA-sensing and immune activation by human cGAS. <i> Kato K, Ishii R, Goto E, Ishitani R, Tokunaga F, Nureki O. </i> PLoS One, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4MKP"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-10-31T19:17:42.482Z"}}],"released":"2020_12","ncbi_taxon_id":9606,"disprot_id":"DP02876","date":"2020-05-12T16:40:00.997Z","organism":"Homo sapiens","regions_counter":1,"name":"Cyclic GMP-AMP synthase","dataset":["Condensates-related proteins"],"UniParc":"UPI000006DE5D","uniref100":"UniRef100_Q8N884","uniref90":"UniRef90_Q8N884","uniref50":"UniRef50_Q8N884","genes":[{"name":{"value":"CGAS","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"23258413","url":"http://www.ncbi.nlm.nih.gov/pubmed/23258413","alternativeUrl":"https://europepmc.org/abstract/MED/23258413"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:21367","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:21367"}}]},"synonyms":[{"value":"C6orf150","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:21367","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:21367"}}]},{"value":"MB21D1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:21367","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:21367"}}]}]}],"alphafold_very_low_content":0.2988505747126437,"disorder_content":0.032567049808429116,"disprot_consensus":{"full":[{"start":289,"end":305,"type":"D"}],"Structural state":[{"start":289,"end":305,"type":"D"}]}},{"acc":"Q8XAD5","features":{"pfam":[{"id":"PF21217","name":"Stability determinant","start":16,"end":45}]},"creator":"lchemes","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"sequence":"MNRALSPMVSEFETIEQENSYNEWLRAKVATSLADPRPAIPHDEVERRMAERFAKMRKERSKQ","length":63,"dataset":["Unicellular toxins and antitoxins"],"regions":[{"region_id":"DP02878r002","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:37:39.662Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":63,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"Here, we present a combination of SAXS and NMR data to describe the conformational ensemble of the PaaA2 antitoxin from the human pathogen E. coli O157","type":"Abstract"},{"text":"We show that the conformational ensemble of PaaA2 is highly compact and that the protein exists in solution as two preformed helices, connected by a flexible linker, that probably act as molecular recognition elements for toxin inhibition.","type":"Abstract"},{"text":"The structural properties of PaaA2 in solution were further investigated by SAXS measurements (Figure 3A and Table S2). The SAXS data also indicate that PaaA2 is an IDP-like protein as the normalized Kratky plot displays the behavior of a highly flexible biomolecule (Figure 3A, inset).","type":"Results"},{"text":"comparison of the experimentally determined Rg of PaaA2 with the values expected for an IDP of similar length (63 amino acids) or a globular protein with a similar molecular mass (∼8.5 kDa) suggests that the behavior of PaaA2 in solution most resembles that of an IDP and not of a globular protein (Figure 3B).","type":"Results"},{"text":"Altogether, these findings reveal that, in the absence of its cognate binding partner ParE2, the PaaA2 antitoxin in solution harbors two α helices connected by a flexible linker","type":"Results"},{"text":"Although PaaA2 may assume a certain level of compactness, it is clear that the protein neither adopts a globular conformation nor contains a hydrophobic core. Although the former is supported by the analytical SEC and DLS experiments, the latter is evidenced by the thermal unfolding data","type":"Discussion"},{"text":" Second, the structural study of PaaA2 reveals that the antitoxin is a monomer composed of two α helices connected by a highly flexible linker. Interestingly, these pre-existing α helices align well with the toxin-binding elements of the archetypal RelB antitoxins. Therefore, we hypothesize that these helices act as molecular recognition elements that allow PaaA2 to efficiently bind the ParE2 toxin. Given that the helices are preformed, PaaA2 probably interacts with its cognate toxin through the mechanism of conformational selection","type":"Discussion"}],"term_name":"disorder","ec_name":"small-angle X-ray scattering evidence used in manual assertion","reference_html":"Small-angle X-ray scattering- and nuclear magnetic resonance-derived conformational ensemble of the highly flexible antitoxin PaaA2. <i> Sterckx YG, Volkov AN, Vranken WF, Kragelj J, Jensen MR, Buts L, Garcia-Pino A, Jové T, Van Melderen L, Blackledge M, van Nuland NA, Loris R. </i> Structure, 2014","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"24768114","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3ZBE"}],"term_namespace":"Structural state","ec_id":"ECO:0006210","curator_id":"lchemes","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02878r003","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:37:40.754Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":63,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"Here, we present a combination of SAXS and NMR data to describe the conformational ensemble of the PaaA2 antitoxin from the human pathogen E. coli O157","type":"Abstract"},{"text":"\nWe show that the conformational ensemble of PaaA2 is highly compact and that the protein exists in solution as two preformed helices, connected by a flexible linker, that probably act as molecular recognition elements for toxin inhibition.","type":"Abstract"},{"text":"Estimation of the antitoxin’s secondary structure content based on the analysis of the CD spectrum reveals that PaaA2 consists of random coil with a significant amount of α helices (∼35% α helicity; Figure 2A and Table S1)","type":"Results"},{"text":"it is noteworthy that the denaturation is fully reversible (Figure S2) and that the thermal profile is not sigmoidal, suggesting that the unfolding event occurs through a noncooperative process.\n","type":"Results"},{"text":"Altogether, these findings reveal that, in the absence of its cognate binding partner ParE2, the PaaA2 antitoxin in solution harbors two α helices connected by a flexible linker","type":"Results"},{"text":"Although PaaA2 may assume a certain level of compactness, it is clear that the protein neither adopts a globular conformation nor contains a hydrophobic core. Although the former is supported by the analytical SEC and DLS experiments, the latter is evidenced by the thermal unfolding data","type":"Discussion"},{"text":"Second, the structural study of PaaA2 reveals that the antitoxin is a monomer composed of two α helices connected by a highly flexible linker. Interestingly, these pre-existing α helices align well with the toxin-binding elements of the archetypal RelB antitoxins. Therefore, we hypothesize that these helices act as molecular recognition elements that allow PaaA2 to efficiently bind the ParE2 toxin. Given that the helices are preformed, PaaA2 probably interacts with its cognate toxin through the mechanism of conformational selection","type":"Discussion"},{"text":"Although the whole protein is overall disordered, NMR reveals that regions 16-28 and 42-57 are preformed helices","type":"Curator statement"}],"term_name":"disorder","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"24768114","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006204","curator_id":"lchemes","reference_html":"Small-angle X-ray scattering- and nuclear magnetic resonance-derived conformational ensemble of the highly flexible antitoxin PaaA2. <i> Sterckx YG, Volkov AN, Vranken WF, Kragelj J, Jensen MR, Buts L, Garcia-Pino A, Jové T, Van Melderen L, Blackledge M, van Nuland NA, Loris R. </i> Structure, 2014","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02878r004","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:37:42.040Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":63,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"Here, we present a combination of SAXS and NMR data to describe the conformational ensemble of the PaaA2 antitoxin from the human pathogen E. coli O157","type":"Abstract"},{"text":"\nWe show that the conformational ensemble of PaaA2 is highly compact and that the protein exists in solution as two preformed helices, connected by a flexible linker, that probably act as molecular recognition elements for toxin inhibition.","type":"Abstract"},{"text":"The analytical SEC and DLS experiments indicate that PaaA2 displays IDP-like features and adopts an extended, nonglobular conformation (Figures 2B and 2C). The ratios between the apparent and theoretical values for molecular mass (Mr,app/Mr,theor) and hydrodynamic radius (Rh,app/Rh,theor) are 2.2–2.8 and 1.3–1.6, respectively, which is a typical trait for IDPs","type":"Results"},{"text":"Altogether, these findings reveal that, in the absence of its cognate binding partner ParE2, the PaaA2 antitoxin in solution harbors two α helices connected by a flexible linker","type":"Results"},{"text":"\nAlthough PaaA2 may assume a certain level of compactness, it is clear that the protein neither adopts a globular conformation nor contains a hydrophobic core. Although the former is supported by the analytical SEC and DLS experiments, the latter is evidenced by the thermal unfolding data.\n","type":"Discussion"},{"text":"econd, the structural study of PaaA2 reveals that the antitoxin is a monomer composed of two α helices connected by a highly flexible linker. Interestingly, these pre-existing α helices align well with the toxin-binding elements of the archetypal RelB antitoxins. Therefore, we hypothesize that these helices act as molecular recognition elements that allow PaaA2 to efficiently bind the ParE2 toxin. Given that the helices are preformed, PaaA2 probably interacts with its cognate toxin through the mechanism of conformational selection","type":"Discussion"}],"term_name":"disorder","ec_name":"chromatography evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"24768114","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0007680","curator_id":"lchemes","reference_html":"Small-angle X-ray scattering- and nuclear magnetic resonance-derived conformational ensemble of the highly flexible antitoxin PaaA2. <i> Sterckx YG, Volkov AN, Vranken WF, Kragelj J, Jensen MR, Buts L, Garcia-Pino A, Jové T, Van Melderen L, Blackledge M, van Nuland NA, Loris R. </i> Structure, 2014","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02878r005","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:37:43.392Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":63,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"Here, we present a combination of SAXS and NMR data to describe the conformational ensemble of the PaaA2 antitoxin from the human pathogen E. coli O157.","type":"Abstract"},{"text":"We show that the conformational ensemble of PaaA2 is highly compact and that the protein exists in solution as two preformed helices, connected by a flexible linker, that probably act as molecular recognition elements for toxin inhibition.\n","type":"Abstract"},{"text":"The analytical SEC and DLS experiments indicate that PaaA2 displays IDP-like features and adopts an extended, nonglobular conformation (Figures 2B and 2C). The ratios between the apparent and theoretical values for molecular mass (Mr,app/Mr,theor) and hydrodynamic radius (Rh,app/Rh,theor) are 2.2–2.8 and 1.3–1.6, respectively, which is a typical trait for IDPs\n","type":"Results"},{"text":"Altogether, these findings reveal that, in the absence of its cognate binding partner ParE2, the PaaA2 antitoxin in solution harbors two α helices connected by a flexible linker","type":"Results"},{"text":"Although PaaA2 may assume a certain level of compactness, it is clear that the protein neither adopts a globular conformation nor contains a hydrophobic core. Although the former is supported by the analytical SEC and DLS experiments, the latter is evidenced by the thermal unfolding data.","type":"Discussion"},{"text":"Second, the structural study of PaaA2 reveals that the antitoxin is a monomer composed of two α helices connected by a highly flexible linker. Interestingly, these pre-existing α helices align well with the toxin-binding elements of the archetypal RelB antitoxins. Therefore, we hypothesize that these helices act as molecular recognition elements that allow PaaA2 to efficiently bind the ParE2 toxin. Given that the helices are preformed, PaaA2 probably interacts with its cognate toxin through the mechanism of conformational selection","type":"Discussion"}],"term_name":"disorder","ec_name":"dynamic light scattering assay evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"24768114","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0007064","curator_id":"lchemes","reference_html":"Small-angle X-ray scattering- and nuclear magnetic resonance-derived conformational ensemble of the highly flexible antitoxin PaaA2. <i> Sterckx YG, Volkov AN, Vranken WF, Kragelj J, Jensen MR, Buts L, Garcia-Pino A, Jové T, Van Melderen L, Blackledge M, van Nuland NA, Loris R. </i> Structure, 2014","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02878r006","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:37:53.972Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":41,"term_id":"IDPO:0000033","start":29,"version":3,"statement":[{"text":"Here, we present a combination of SAXS and NMR data to describe the conformational ensemble of the PaaA2 antitoxin from the human pathogen E. coli O157","type":"Abstract"},{"text":"\nWe show that the conformational ensemble of PaaA2 is highly compact and that the protein exists in solution as two preformed helices, connected by a flexible linker, that probably act as molecular recognition elements for toxin inhibition.","type":"Abstract"},{"text":"The fully assigned 1H-15N HSQC spectrum of PaaA2 shows that most of the backbone amide resonances are confined to a narrow spectral region (Figure 4A), typical for IDPs or proteins with a high α-helical content (Wüthrich, 1986,  Wishart et al., 1991). On the other hand, δ2D (Camilloni et al., 2012), which is benchmarked for IDPs, identifies two stable cores existing in an α-helical conformation for more than 80% of the time: residues Asn22 to Arg26 and Glu46 to Glu51 for helices 1 and 2, respectively (Figure 4C). These core regions coincide with the predicted α helices and contain flanking regions with percentages of α helicity between 15% and 80% (Figure 4C), which is overall in agreement with the CD data (Table S1). All of the other residues are predicted to adopt a coil-like conformation. In agreement with these predictions, the NOE spectroscopy (NOESY) spectra indicate the absence of β sheet signatures and contain peaks characteristic of α helices.","type":"Results"},{"text":"Altogether, these findings reveal that, in the absence of its cognate binding partner ParE2, the PaaA2 antitoxin in solution harbors two α helices connected by a flexible linker","type":"Results"},{"text":"Although PaaA2 may assume a certain level of compactness, it is clear that the protein neither adopts a globular conformation nor contains a hydrophobic core. Although the former is supported by the analytical SEC and DLS experiments, the latter is evidenced by the thermal unfolding data.","type":"Discussion"},{"text":"Second, the structural study of PaaA2 reveals that the antitoxin is a monomer composed of two α helices connected by a highly flexible linker. Interestingly, these pre-existing α helices align well with the toxin-binding elements of the archetypal RelB antitoxins. Therefore, we hypothesize that these helices act as molecular recognition elements that allow PaaA2 to efficiently bind the ParE2 toxin. Given that the helices are preformed, PaaA2 probably interacts with its cognate toxin through the mechanism of conformational selection","type":"Discussion"}],"term_name":"flexible linker","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"24768114","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Disorder function","ec_id":"ECO:0006165","curator_id":"lchemes","reference_html":"Small-angle X-ray scattering- and nuclear magnetic resonance-derived conformational ensemble of the highly flexible antitoxin PaaA2. <i> Sterckx YG, Volkov AN, Vranken WF, Kragelj J, Jensen MR, Buts L, Garcia-Pino A, Jové T, Van Melderen L, Blackledge M, van Nuland NA, Loris R. </i> Structure, 2014","ec_go":"EXP","disprot_namespace":"Disorder function"},{"region_id":"DP02878r007","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:37:50.789Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":34,"term_id":"GO:0005515","start":15,"version":3,"statement":[{"text":"The antitoxin EcPaaA2 is characterized by tha helices (H1 ans H2) that serve as molecular recognition elements to wrap itself around EcParE2","type":"Abstract"},{"text":"In this antitoxin-toxin heterodimer, the EcPaaA2 completely wraps itself around EcParE2 in an all alpha helical conformation and covers an accessible surface area of around 1500 A2 on EcParE2","type":"Results"},{"text":"The EcPaaA2 antitoxin was recently found to be an intrinsically disordered protein with a broad conformational ensemble but containing two alpha helices. When bound to its cognate toxin these two transient helices stabilize and extend to encompass residues I15-A34 and H42-S61 (H1 and H2), the remaining aminoacids adopt defined loop conformations","type":"Results"}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","reference_html":"A unique hetero-hexadecameric architecture displayed by the Escherichia coli O157 PaaA2-ParE2 antitoxin-toxin complex. <i> Sterckx YG, Jové T, Shkumatov AV, Garcia-Pino A, Geerts L, De Kerpel M, Lah J, De Greve H, Van Melderen L, Loris R. </i> J Mol Biol, 2016","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"26996937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5CW7"},{"db":"PDB","id":"5CZF"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"lchemes","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02878r008","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:37:55.812Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":34,"term_id":"GO:0098772","start":15,"version":3,"statement":[{"text":"The antitoxin EcPaaA2 is characterized by tha helices (H1 ans H2) that serve as molecular recognition elements to wrap itself around EcParE2","type":"Abstract"},{"text":"In this antitoxin-toxin heterodimer, the EcPaaA2 completely wraps itself around EcParE2 in an all alpha helical conformation and covers an accessible surface area of around 1500 A2 on EcParE2","type":"Results"},{"text":"The EcPaaA2 antitoxin was recently found to be an intrinsically disordered protein with a broad conformational ensemble but containing two alpha helices. When bound to its cognate toxin these two transient helices stabilize and extend to encompass residues I15-A34 and H42-S61 (H1 and H2), the remaining aminoacids adopt defined loop conformations","type":"Results"}],"term_name":"molecular function regulator","ec_name":"x-ray crystallography evidence used in manual assertion","reference_html":"A unique hetero-hexadecameric architecture displayed by the Escherichia coli O157 PaaA2-ParE2 antitoxin-toxin complex. <i> Sterckx YG, Jové T, Shkumatov AV, Garcia-Pino A, Geerts L, De Kerpel M, Lah J, De Greve H, Van Melderen L, Loris R. </i> J Mol Biol, 2016","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"26996937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5CW7"},{"db":"PDB","id":"5CZF"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"lchemes","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02878r009","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:37:56.714Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":61,"term_id":"GO:0098772","start":42,"version":3,"statement":[{"text":"The antitoxin EcPaaA2 is characterized by tha helices (H1 ans H2) that serve as molecular recognition elements to wrap itself around EcParE2","type":"Abstract"},{"text":"In this antitoxin-toxin heterodimer, the EcPaaA2 completely wraps itself around EcParE2 in an all alpha helical conformation and covers an accessible surface area of around 1500 A2 on EcParE2","type":"Results"},{"text":"The EcPaaA2 antitoxin was recently found to be an intrinsically disordered protein with a broad conformational ensemble but containing two alpha helices. When bound to its cognate toxin these two transient helices stabilize and extend to encompass residues I15-A34 and H42-S61 (H1 and H2), the remaining aminoacids adopt defined loop conformations","type":"Results"}],"term_name":"molecular function regulator","ec_name":"x-ray crystallography evidence used in manual assertion","reference_html":"A unique hetero-hexadecameric architecture displayed by the Escherichia coli O157 PaaA2-ParE2 antitoxin-toxin complex. <i> Sterckx YG, Jové T, Shkumatov AV, Garcia-Pino A, Geerts L, De Kerpel M, Lah J, De Greve H, Van Melderen L, Loris R. </i> J Mol Biol, 2016","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"26996937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5CW7"},{"db":"PDB","id":"5CZF"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"lchemes","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02878r010","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:37:52.387Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":61,"term_id":"GO:0005515","start":42,"version":3,"statement":[{"text":"The antitoxin EcPaaA2 is characterized by tha helices (H1 ans H2) that serve as molecular recognition elements to wrap itself around EcParE2","type":"Abstract"},{"text":"In this antitoxin-toxin heterodimer, the EcPaaA2 completely wraps itself around EcParE2 in an all alpha helical conformation and covers an accessible surface area of around 1500 A2 on EcParE2","type":"Results"},{"text":"The EcPaaA2 antitoxin was recently found to be an intrinsically disordered protein with a broad conformational ensemble but containing two alpha helices. When bound to its cognate toxin these two transient helices stabilize and extend to encompass residues I15-A34 and H42-S61 (H1 and H2), the remaining aminoacids adopt defined loop conformations","type":"Results"}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","reference_html":"A unique hetero-hexadecameric architecture displayed by the Escherichia coli O157 PaaA2-ParE2 antitoxin-toxin complex. <i> Sterckx YG, Jové T, Shkumatov AV, Garcia-Pino A, Geerts L, De Kerpel M, Lah J, De Greve H, Van Melderen L, Loris R. </i> J Mol Biol, 2016","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"26996937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5CW7"},{"db":"PDB","id":"5CZF"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"lchemes","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02878r011","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:37:48.646Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":49,"term_id":"IDPO:0000011","start":5,"version":2,"statement":[{"text":"The antitoxin EcPaaA2 is characterized by tha helices (H1 ans H2) that serve as molecular recognition elements to wrap itself around EcParE2","type":"Abstract"},{"text":"In this antitoxin-toxin heterodimer, the EcPaaA2 completely wraps itself around EcParE2 in an all alpha helical conformation and covers an accessible surface area of around 1500 A2 on EcParE2","type":"Results"},{"text":"The EcPaaA2 antitoxin was recently found to be an intrinsically disordered protein with a broad conformational ensemble but containing two alpha helices. When bound to its cognate toxin these two transient helices stabilize and extend to encompass residues I15-A34 and H42-S61 (H1 and H2), the remaining aminoacids adopt defined loop conformations","type":"Results"}],"term_name":"disorder to order","ec_name":"x-ray crystallography evidence used in manual assertion","reference_html":"A unique hetero-hexadecameric architecture displayed by the Escherichia coli O157 PaaA2-ParE2 antitoxin-toxin complex. <i> Sterckx YG, Jové T, Shkumatov AV, Garcia-Pino A, Geerts L, De Kerpel M, Lah J, De Greve H, Van Melderen L, Loris R. </i> J Mol Biol, 2016","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"26996937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5CW7"},{"db":"PDB","id":"5CZF"}],"term_namespace":"Structural transition","ec_id":"ECO:0005670","curator_id":"lchemes","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP02878r012","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:37:58.428Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":12,"term_id":"GO:0060090","start":1,"version":3,"statement":[{"text":"The antitoxin EcPaaA2 is characterized by tha helices (H1 ans H2) that serve as molecular recognition elements to wrap itself around EcParE2","type":"Abstract"},{"text":"The N-terminus of EcxPaaA2 is important for the assembly of the hetero-hexadecamer","type":"Results"},{"text":"Solution studies reveal that the removal of the first 12 residues  of the EcPaaA2 antitoxin generates a toxin-antitoxin complex which has all the hallmarks of a heterodimer","type":"Curator statement"},{"text":"The N terminal region is neccessary for formation of the higher order hetero-hexadecamer assembly","type":"Curator statement"}],"term_name":"molecular adaptor activity","ec_name":"x-ray crystallography evidence used in manual assertion","reference_html":"A unique hetero-hexadecameric architecture displayed by the Escherichia coli O157 PaaA2-ParE2 antitoxin-toxin complex. <i> Sterckx YG, Jové T, Shkumatov AV, Garcia-Pino A, Geerts L, De Kerpel M, Lah J, De Greve H, Van Melderen L, Loris R. </i> J Mol Biol, 2016","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"26996937","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5CW7"},{"db":"PDB","id":"5CZF"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"lchemes","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02878r013","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:37:44.917Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":15,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"Here, we present a combination of SAXS and NMR data to describe the conformational ensemble of the PaaA2 antitoxin from the human pathogen E. coli O157","type":"Abstract"},{"text":"We show that the conformational ensemble of PaaA2 is highly compact and that the protein exists in solution as two preformed helices, connected by a flexible linker, that probably act as molecular recognition elements for toxin inhibition","type":"Abstract"},{"text":"The fully assigned 1H-15N HSQC spectrum of PaaA2 shows that most of the backbone amide resonances are confined to a narrow spectral region (Figure 4A), typical for IDPs or proteins with a high α-helical content ","type":"Results"},{"text":"Chemical shift-based secondary structure predictions with DANGLE and TALOS+ suggest the presence of two a helices (residues Glu16 to Lys28 and His42 to Arg57), connected by a linker segment (Figure 4B), which is in agreement with our bioinformatics analysis.","type":"Results"},{"text":"On the other hand, δ2D (Camilloni et al., 2012), which is benchmarked for IDPs, identifies two stable cores existing in an α-helical conformation for more than 80% of the time: residues Asn22 to Arg26 and Glu46 to Glu51 for helices 1 and 2, respectively (Figure 4C). These core regions coincide with the predicted α helices and contain flanking regions with percentages of α helicity between 15% and 80% (Figure 4C), which is overall in agreement with the CD data (Table S1). All of the other residues are predicted to adopt a coil-like conformation. In agreement with these predictions, the NOE spectroscopy (NOESY) spectra indicate the absence of β sheet signatures and contain peaks characteristic of α helices.","type":"Results"},{"text":"Altogether, these findings reveal that, in the absence of its cognate binding partner ParE2, the PaaA2 antitoxin in solution harbors two α helices connected by a flexible linker","type":"Results"},{"text":"Although PaaA2 may assume a certain level of compactness, it is clear that the protein neither adopts a globular conformation nor contains a hydrophobic core. Although the former is supported by the analytical SEC and DLS experiments, the latter is evidenced by the thermal unfolding data.","type":"Discussion"},{"text":"Second, the structural study of PaaA2 reveals that the antitoxin is a monomer composed of two α helices connected by a highly flexible linker. Interestingly, these pre-existing α helices align well with the toxin-binding elements of the archetypal RelB antitoxins. Therefore, we hypothesize that these helices act as molecular recognition elements that allow PaaA2 to efficiently bind the ParE2 toxin. Given that the helices are preformed, PaaA2 probably interacts with its cognate toxin through the mechanism of conformational selection","type":"Discussion"},{"text":"The entire protein is an IDP, but regions 16-28 and 42-57 are in a helical conformation, constituting two preformed helices. The boundaries of these helices are not strictly defined as the core region is helical >80% of the time and the flanking regions have decreasing fraction of helicity as the helical content is highly dynamic in the ensemble. The boundary established by the authors in the text is taken, which is highly coincident with the models deposited in the PDB where the helices range from residues 14-29 and 43-57","type":"Curator statement"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"24768114","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3ZBE"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"lchemes","reference_html":"Small-angle X-ray scattering- and nuclear magnetic resonance-derived conformational ensemble of the highly flexible antitoxin PaaA2. <i> Sterckx YG, Volkov AN, Vranken WF, Kragelj J, Jensen MR, Buts L, Garcia-Pino A, Jové T, Van Melderen L, Blackledge M, van Nuland NA, Loris R. </i> Structure, 2014","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02878r014","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T17:37:46.704Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":41,"term_id":"IDPO:0000002","start":29,"version":2,"statement":[{"text":"Here, we present a combination of SAXS and NMR data to describe the conformational ensemble of the PaaA2 antitoxin from the human pathogen E. coli O157","type":"Abstract"},{"text":"We show that the conformational ensemble of PaaA2 is highly compact and that the protein exists in solution as two preformed helices, connected by a flexible linker, that probably act as molecular recognition elements for toxin inhibition","type":"Abstract"},{"text":"The fully assigned 1H-15N HSQC spectrum of PaaA2 shows that most of the backbone amide resonances are confined to a narrow spectral region (Figure 4A), typical for IDPs or proteins with a high α-helical content ","type":"Results"},{"text":"Chemical shift-based secondary structure predictions with DANGLE and TALOS+ suggest the presence of two a helices (residues Glu16 to Lys28 and His42 to Arg57), connected by a linker segment (Figure 4B), which is in agreement with our bioinformatics analysis.","type":"Results"},{"text":"On the other hand, δ2D (Camilloni et al., 2012), which is benchmarked for IDPs, identifies two stable cores existing in an α-helical conformation for more than 80% of the time: residues Asn22 to Arg26 and Glu46 to Glu51 for helices 1 and 2, respectively (Figure 4C). These core regions coincide with the predicted α helices and contain flanking regions with percentages of α helicity between 15% and 80% (Figure 4C), which is overall in agreement with the CD data (Table S1). All of the other residues are predicted to adopt a coil-like conformation. In agreement with these predictions, the NOE spectroscopy (NOESY) spectra indicate the absence of β sheet signatures and contain peaks characteristic of α helices.","type":"Results"},{"text":"Altogether, these findings reveal that, in the absence of its cognate binding partner ParE2, the PaaA2 antitoxin in solution harbors two α helices connected by a flexible linker","type":"Results"},{"text":"Although PaaA2 may assume a certain level of compactness, it is clear that the protein neither adopts a globular conformation nor contains a hydrophobic core. Although the former is supported by the analytical SEC and DLS experiments, the latter is evidenced by the thermal unfolding data.","type":"Discussion"},{"text":"Second, the structural study of PaaA2 reveals that the antitoxin is a monomer composed of two α helices connected by a highly flexible linker. Interestingly, these pre-existing α helices align well with the toxin-binding elements of the archetypal RelB antitoxins. Therefore, we hypothesize that these helices act as molecular recognition elements that allow PaaA2 to efficiently bind the ParE2 toxin. Given that the helices are preformed, PaaA2 probably interacts with its cognate toxin through the mechanism of conformational selection","type":"Discussion"},{"text":"The entire protein is an IDP, but regions 16-28 and 42-57 are in a helical conformation, constituting two preformed helices. The boundaries of these helices are not strictly defined as the core region is helical >80% of the time and the flanking regions have decreasing fraction of helicity as the helical content is highly dynamic in the ensemble. The boundary established by the authors in the text is taken, which is highly coincident with the models deposited in the PDB where the helices range from residues 14-29 and 43-57","type":"Curator statement"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"24768114","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3ZBE"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"lchemes","reference_html":"Small-angle X-ray scattering- and nuclear magnetic resonance-derived conformational ensemble of the highly flexible antitoxin PaaA2. <i> Sterckx YG, Volkov AN, Vranken WF, Kragelj J, Jensen MR, Buts L, Garcia-Pino A, Jové T, Van Melderen L, Blackledge M, van Nuland NA, Loris R. </i> Structure, 2014","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","ncbi_taxon_id":83334,"disprot_id":"DP02878","date":"2020-05-15T14:19:38.843Z","organism":"Escherichia coli O157:H7","regions_counter":14,"name":"Stability determinant","UniParc":"UPI00001657D9","uniref100":"UniRef100_A0A1Q6B310","uniref90":"UniRef90_A7ZKN8","uniref50":"UniRef50_N6VGU1","genes":[{"orfNames":[{"value":"ECs_2280","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAB35703.2","url":"https://www.ebi.ac.uk/ena/browser/view/BAB35703.2"}}]}]}],"alphafold_very_low_content":0.015873015873015872,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":4,"type":"D"},{"start":5,"end":49,"type":"T"},{"start":50,"end":63,"type":"D"}],"Structural state":[{"start":1,"end":63,"type":"D"}],"Disorder function":[{"start":29,"end":41,"type":"F"}],"Molecular function":[{"start":1,"end":12,"type":"F"},{"start":15,"end":34,"type":"F"},{"start":42,"end":61,"type":"F"}],"Structural transition":[{"start":5,"end":49,"type":"T"}]}},{"acc":"P59594","sequence":"MFIFLLFLTLTSGSDLDRCTTFDDVQAPNYTQHTSSMRGVYYPDEIFRSDTLYLTQDLFLPFYSNVTGFHTINHTFGNPVIPFKDGIYFAATEKSNVVRGWVFGSTMNNKSQSVIIINNSTNVVIRACNFELCDNPFFAVSKPMGTQTHTMIFDNAFNCTFEYISDAFSLDVSEKSGNFKHLREFVFKNKDGFLYVYKGYQPIDVVRDLPSGFNTLKPIFKLPLGINITNFRAILTAFSPAQDIWGTSAAAYFVGYLKPTTFMLKYDENGTITDAVDCSQNPLAELKCSVKSFEIDKGIYQTSNFRVVPSGDVVRFPNITNLCPFGEVFNATKFPSVYAWERKKISNCVADYSVLYNSTFFSTFKCYGVSATKLNDLCFSNVYADSFVVKGDDVRQIAPGQTGVIADYNYKLPDDFMGCVLAWNTRNIDATSTGNYNYKYRYLRHGKLRPFERDISNVPFSPDGKPCTPPALNCYWPLNDYGFYTTTGIGYQPYRVVVLSFELLNAPATVCGPKLSTDLIKNQCVNFNFNGLTGTGVLTPSSKRFQPFQQFGRDVSDFTDSVRDPKTSEILDISPCSFGGVSVITPGTNASSEVAVLYQDVNCTDVSTAIHADQLTPAWRIYSTGNNVFQTQAGCLIGAEHVDTSYECDIPIGAGICASYHTVSLLRSTSQKSIVAYTMSLGADSSIAYSNNTIAIPTNFSISITTEVMPVSMAKTSVDCNMYICGDSTECANLLLQYGSFCTQLNRALSGIAAEQDRNTREVFAQVKQMYKTPTLKYFGGFNFSQILPDPLKPTKRSFIEDLLFNKVTLADAGFMKQYGECLGDINARDLICAQKFNGLTVLPPLLTDDMIAAYTAALVSGTATAGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKQIANQFNKAISQIQESLTTTSTALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDKVEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQAAPHGVVFLHVTYVPSQERNFTTAPAICHEGKAYFPREGVFVFNGTSWFITQRNFFSPQIITTDNTFVSGNCDVVIGIINNTVYDPLQPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKWPWYVWLGFIAGLIAIVMVTILLCCMTSCCSCLKGACSCGSCCKFDEDDSEPVLKGVKLHYT","creator":"fquaglia","dataset":["Viral proteins"],"date":"2020-05-18T08:34:37.386Z","disprot_id":"DP02879","features":{"gene3D":[{"start":1147,"end":1194,"id":"G3DSA:1.20.5.790","name":"Single helix bin","_id":"685af523b4ac24d5329d95c6"}],"pfam":[{"id":"PF01601","name":"Coronavirus spike glycoprotein S2","start":693,"end":1214},{"id":"PF09408","name":"Betacoronavirus spike glycoprotein S1, receptor binding","start":335,"end":512},{"id":"PF16451","name":"Betacoronavirus-like spike glycoprotein S1, N-terminal","start":33,"end":324},{"id":"PF19209","name":"Coronavirus spike glycoprotein S1, C-terminal","start":522,"end":578}]},"genes":[{"name":{"value":"S","evidences":[{"source":{"id":"MF_04099","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04099","_id":"685af523b4ac24d5329d9601"},"code":"ECO:0000255","_id":"685af523b4ac24d5329d9600"}],"_id":"685af523b4ac24d5329d9602"},"synonyms":[],"olnNames":[],"orfNames":[{"value":"2","evidences":[],"_id":"685af523b4ac24d5329d9603"}],"_id":"685af523b4ac24d5329d95ff"}],"length":1255,"name":"Spike glycoprotein","ncbi_taxon_id":694009,"organism":"Human SARS coronavirus","regions_counter":11,"released":"2020_06","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Nidovirales","Cornidovirineae","Coronaviridae","Orthocoronavirinae","Betacoronavirus","Sarbecovirus"],"UniParc":"UPI000018FE19","uniref100":"UniRef100_P59594","uniref50":"UniRef50_P0DTC2","uniref90":"UniRef90_P59594","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6ACC","_id":"685af523b4ac24d5329d95cc"},{"db":"PDB","id":"6ACD","_id":"685af523b4ac24d5329d95cd"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006224","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":17,"interaction_partner":[],"reference_html":"Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2. <i> Song W, Gui M, Wang X, Xiang Y. </i> PLoS Pathog, 2018","reference_id":"30102747","region_id":"DP02879r001","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"Flexible region in the structrures of ACE2-free SARS-CoV spike glycoprotein with three RBD in down conformation (PDB:6ACC) and with one RBD in up conformation (PDB:6ACD), and in the SARS-CoV spike glycoprotein and ACE2 complex, ACE2-bound conformation 1 (PDB:6acg), conformation 2 (PDB:6acj) and conformation 3 (PDB:6ack).","_id":"685af523b4ac24d5329d95cb"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T09:56:37.503Z","_id":"685af523b4ac24d5329d95ce"},"version":3,"_id":"685af523b4ac24d5329d95ca","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6ACC","_id":"685af523b4ac24d5329d95d1"},{"db":"PDB","id":"6ACD","_id":"685af523b4ac24d5329d95d2"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006224","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":661,"end":673,"interaction_partner":[],"reference_html":"Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2. <i> Song W, Gui M, Wang X, Xiang Y. </i> PLoS Pathog, 2018","reference_id":"30102747","region_id":"DP02879r002","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"Flexible region in the structrures of ACE2-free SARS-CoV spike glycoprotein with three RBD in down conformation (PDB:6ACC) and with one RBD in up conformation (PDB:6ACD), and in the SARS-CoV spike glycoprotein and ACE2 complex, ACE2-bound conformation 1 (PDB:6acg), conformation 2 (PDB:6acj) and conformation 3 (PDB:6ack).","_id":"685af523b4ac24d5329d95d0"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T09:56:36.584Z","_id":"685af523b4ac24d5329d95d3"},"version":3,"_id":"685af523b4ac24d5329d95cf","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6ACC","_id":"685af523b4ac24d5329d95d6"},{"db":"PDB","id":"6ACD","_id":"685af523b4ac24d5329d95d7"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006224","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":812,"end":831,"interaction_partner":[],"reference_html":"Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2. <i> Song W, Gui M, Wang X, Xiang Y. </i> PLoS Pathog, 2018","reference_id":"30102747","region_id":"DP02879r003","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"Flexible region in the structrures of ACE2-free SARS-CoV spike glycoprotein with three RBD in down conformation (PDB:6ACC) and with one RBD in up conformation (PDB:6ACD), and in the SARS-CoV spike glycoprotein and ACE2 complex, ACE2-bound conformation 1 (PDB:6acg), conformation 2 (PDB:6acj) and conformation 3 (PDB:6ack).","_id":"685af523b4ac24d5329d95d5"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T09:56:35.166Z","_id":"685af523b4ac24d5329d95d8"},"version":3,"_id":"685af523b4ac24d5329d95d4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6ACC","_id":"685af523b4ac24d5329d95db"},{"db":"PDB","id":"6ACD","_id":"685af523b4ac24d5329d95dc"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006224","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1120,"end":1196,"interaction_partner":[],"reference_html":"Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2. <i> Song W, Gui M, Wang X, Xiang Y. </i> PLoS Pathog, 2018","reference_id":"30102747","region_id":"DP02879r004","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"Flexible region in the structrures of ACE2-free SARS-CoV spike glycoprotein with three RBD in down conformation (PDB:6ACC) and with one RBD in up conformation (PDB:6ACD), and in the SARS-CoV spike glycoprotein and ACE2 complex, ACE2-bound conformation 1 (PDB:6acg), conformation 2 (PDB:6acj) and conformation 3 (PDB:6ack).","_id":"685af523b4ac24d5329d95da"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T09:56:33.888Z","_id":"685af523b4ac24d5329d95dd"},"version":3,"_id":"685af523b4ac24d5329d95d9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6ACC","_id":"685af523b4ac24d5329d95e0"},{"db":"PDB","id":"6ACD","_id":"685af523b4ac24d5329d95e1"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006208","ec_name":"cryogenic electron microscopy evidence used in manual assertion","ec_ontology":"ECO","start":661,"end":673,"interaction_partner":[],"reference_html":"Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2. <i> Song W, Gui M, Wang X, Xiang Y. </i> PLoS Pathog, 2018","reference_id":"30102747","region_id":"DP02879r005","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"The S1/S2 cleavage site is located in a flexible loop of residues 660–675 that is completely exposed in the prefusion S1-S2 trimer spike. The S2’ cleavage site of the SARS-CoV S glycoprotein is highly conserved among coronaviruses and is completely buried in the prefusion SARS-CoV S glycoprotein","_id":"685af523b4ac24d5329d95df"}],"states_connection":[],"term_id":"IDPO:0000048","term_name":"limited proteolysis display site","term_namespace":"Disorder function","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T09:50:24.011Z","_id":"685af523b4ac24d5329d95e2"},"version":3,"_id":"685af523b4ac24d5329d95de","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":661,"end":673,"interaction_partner":[],"reference_html":"Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2. <i> Song W, Gui M, Wang X, Xiang Y. </i> PLoS Pathog, 2018","reference_id":"30102747","region_id":"DP02879r006","released":"2022_03","sample":[],"statement":[{"type":"Introduction","text":"The S1/S2 cleavage site is located in a flexible loop of residues 660–675 that is completely exposed in the prefusion S1-S2 trimer spike. The S2’ cleavage site of the SARS-CoV S glycoprotein is highly conserved among coronaviruses and is completely buried in the prefusion SARS-CoV S glycoprotein","_id":"685af523b4ac24d5329d95e4"}],"states_connection":[],"term_id":"IDPO:0000048","term_name":"limited proteolysis display site","term_namespace":"Disorder function","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T09:50:21.730Z","_id":"685af523b4ac24d5329d95e5"},"version":4,"_id":"685af523b4ac24d5329d95e3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5WRG","_id":"685af523b4ac24d5329d95ee"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006224","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":661,"end":674,"interaction_partner":[],"reference_html":"Cryo-electron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding. <i> Gui M, Song W, Zhou H, Xu J, Chen S, Xiang Y, Wang X. </i> Cell Res, 2017","reference_id":"28008928","region_id":"DP02879r008","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Here we report the ectodomain structures of the SARS-CoV surface spike trimer in different conformational states determined by single-particle cryo-electron microscopy. The conformation 1 determined at 4.3 Å resolution is three-fold symmetric and has all the three receptor-binding C-terminal domain 1 (CTD1s) of the S1 subunits in “down” positions. The binding of the “down” CTD1s to the SARS-CoV receptor ACE2 is not possible due to steric clashes, suggesting that the conformation 1 represents a receptor-binding inactive state.","_id":"685af523b4ac24d5329d95ec"},{"type":"Curator statement","text":"Conformation 1 determined at 4.3 Å resolution corresponds to PDB:5WRG.","_id":"685af523b4ac24d5329d95ed"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T09:56:32.681Z","_id":"685af523b4ac24d5329d95ef"},"version":3,"_id":"685af523b4ac24d5329d95eb","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5WRG","_id":"685af523b4ac24d5329d95f3"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006224","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1059,"end":1196,"interaction_partner":[],"reference_html":"Cryo-electron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding. <i> Gui M, Song W, Zhou H, Xu J, Chen S, Xiang Y, Wang X. </i> Cell Res, 2017","reference_id":"28008928","region_id":"DP02879r009","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Here we report the ectodomain structures of the SARS-CoV surface spike trimer in different conformational states determined by single-particle cryo-electron microscopy. The conformation 1 determined at 4.3 Å resolution is three-fold symmetric and has all the three receptor-binding C-terminal domain 1 (CTD1s) of the S1 subunits in “down” positions. The binding of the “down” CTD1s to the SARS-CoV receptor ACE2 is not possible due to steric clashes, suggesting that the conformation 1 represents a receptor-binding inactive state.","_id":"685af523b4ac24d5329d95f1"},{"type":"Curator statement","text":"Conformation 1 determined at 4.3 Å resolution corresponds to PDB:5WRG.","_id":"685af523b4ac24d5329d95f2"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T09:56:31.437Z","_id":"685af523b4ac24d5329d95f4"},"version":3,"_id":"685af523b4ac24d5329d95f0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5X5B","_id":"685af523b4ac24d5329d95f7"},{"db":"PDB","id":"5X58","_id":"685af523b4ac24d5329d95f8"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006224","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":810,"end":830,"interaction_partner":[],"reference_html":"Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains. <i> Yuan Y, Cao D, Zhang Y, Ma J, Qi J, Wang Q, Lu G, Wu Y, Yan J, Shi Y, Zhang X, Gao GF. </i> Nat Commun, 2017","reference_id":"28393837","region_id":"DP02879r010","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"Flexible region in prefusion structure of SARS-CoV spike glycoprotein, conformation 1 (PDB:5x58) and conformation 2 (PDB:5x5b).","_id":"685af523b4ac24d5329d95f6"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T09:56:29.648Z","_id":"685af523b4ac24d5329d95f9"},"version":3,"_id":"685af523b4ac24d5329d95f5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5X5B","_id":"685af523b4ac24d5329d95fc"},{"db":"PDB","id":"5X58","_id":"685af523b4ac24d5329d95fd"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006224","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1105,"end":1193,"interaction_partner":[],"reference_html":"Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains. <i> Yuan Y, Cao D, Zhang Y, Ma J, Qi J, Wang Q, Lu G, Wu Y, Yan J, Shi Y, Zhang X, Gao GF. </i> Nat Commun, 2017","reference_id":"28393837","region_id":"DP02879r011","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"Flexible region in prefusion structure of SARS-CoV spike glycoprotein, conformation 1 (PDB:5x58) and conformation 2 (PDB:5x5b).","_id":"685af523b4ac24d5329d95fb"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-20T09:56:28.592Z","_id":"685af523b4ac24d5329d95fe"},"version":3,"_id":"685af523b4ac24d5329d95fa","reference_source":"pmid"}],"__v":0,"disorder_content":0.15219123505976095,"disprot_consensus":{"full":[{"start":1,"end":17,"type":"D"},{"start":661,"end":674,"type":"D"},{"start":810,"end":831,"type":"D"},{"start":1059,"end":1196,"type":"D"}],"Structural state":[{"start":1,"end":17,"type":"D"},{"start":661,"end":674,"type":"D"},{"start":810,"end":831,"type":"D"},{"start":1059,"end":1196,"type":"D"}],"Disorder function":[{"start":661,"end":673,"type":"F"}]}},{"acc":"K9N5Q8","features":{"gene3D":[{"start":1248,"end":1295,"id":"G3DSA:1.20.5.790","name":"Single helix bin"}],"pfam":[{"id":"PF01601","name":"Coronavirus spike glycoprotein S2","start":780,"end":1314},{"id":"PF09408","name":"Betacoronavirus spike glycoprotein S1, receptor binding","start":394,"end":527},{"id":"PF16451","name":"Betacoronavirus-like spike glycoprotein S1, N-terminal","start":49,"end":383},{"id":"PF19214","name":"Coronavirus spike glycoprotein S2, intravirion","start":1316,"end":1353}]},"creator":"fquaglia","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Nidovirales","Cornidovirineae","Coronaviridae","Orthocoronavirinae","Betacoronavirus","Merbecovirus"],"sequence":"MIHSVFLLMFLLTPTESYVDVGPDSVKSACIEVDIQQTFFDKTWPRPIDVSKADGIIYPQGRTYSNITITYQGLFPYQGDHGDMYVYSAGHATGTTPQKLFVANYSQDVKQFANGFVVRIGAAANSTGTVIISPSTSATIRKIYPAFMLGSSVGNFSDGKMGRFFNHTLVLLPDGCGTLLRAFYCILEPRSGNHCPAGNSYTSFATYHTPATDCSDGNYNRNASLNSFKEYFNLRNCTFMYTYNITEDEILEWFGITQTAQGVHLFSSRYVDLYGGNMFQFATLPVYDTIKYYSIIPHSIRSIQSDRKAWAAFYVYKLQPLTFLLDFSVDGYIRRAIDCGFNDLSQLHCSYESFDVESGVYSVSSFEAKPSGSVVEQAEGVECDFSPLLSGTPPQVYNFKRLVFTNCNYNLTKLLSLFSVNDFTCSQISPAAIASNCYSSLILDYFSYPLSMKSDLSVSSAGPISQFNYKQSFSNPTCLILATVPHNLTTITKPLKYSYINKCSRFLSDDRTEVPQLVNANQYSPCVSIVPSTVWEDGDYYRKQLSPLEGGGWLVASGSTVAMTEQLQMGFGITVQYGTDTNSVCPKLEFANDTKIASQLGNCVEYSLYGVSGRGVFQNCTAVGVRQQRFVYDAYQNLVGYYSDDGNYYCLRACVSVPVSVIYDKETKTHATLFGSVACEHISSTMSQYSRSTRSMLKRRDSTYGPLQTPVGCVLGLVNSSLFVEDCKLPLGQSLCALPDTPSTLTPRSVRSVPGEMRLASIAFNHPIQVDQLNSSYFKLSIPTNFSFGVTQEYIQTTIQKVTVDCKQYVCNGFQKCEQLLREYGQFCSKINQALHGANLRQDDSVRNLFASVKSSQSSPIIPGFGGDFNLTLLEPVSISTGSRSARSAIEDLLFDKVTIADPGYMQGYDDCMQQGPASARDLICAQYVAGYKVLPPLMDVNMEAAYTSSLLGSIAGVGWTAGLSSFAAIPFAQSIFYRLNGVGITQQVLSENQKLIANKFNQALGAMQTGFTTTNEAFHKVQDAVNNNAQALSKLASELSNTFGAISASIGDIIQRLDVLEQDAQIDRLINGRLTTLNAFVAQQLVRSESAALSAQLAKDKVNECVKAQSKRSGFCGQGTHIVSFVVNAPNGLYFMHVGYYPSNHIEVVSAYGLCDAANPTNCIAPVNGYFIKTNNTRIVDEWSYTGSSFYAPEPITSLNTKYVAPQVTYQNISTNLPPPLLGNSTGIDFQDELDEFFKNVSTSIPNFGSLTQINTTLLDLTYEMLSLQQVVKALNESYIDLKELGNYTYYNKWPWYIWLGFIAGLVALALCVFFILCCTGCGTNCMGKLKCNRCCDRYEEYDLEPHKVHVH","length":1353,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":709,"region_id":"DP02880r001","reference_id":"28393837","start":699,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"An atomic model of the cleaved MERS-CoV S1/S2 trimer was built de novo using the 3.7 Å map, except for the flexible regions of S1 CTD and part of S1 NTD, which were fitted by crystal structures. The final model includes residues 18–1,206, with several small breaks due to the poor densities.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains. <i> Yuan Y, Cao D, Zhang Y, Ma J, Qi J, Wang Q, Lu G, Wu Y, Yan J, Shi Y, Zhang X, Gao GF. </i> Nat Commun, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"5X5F"},{"db":"PDB","id":"5X59"},{"db":"PDB","id":"5X5C"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T08:40:55.306Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":756,"region_id":"DP02880r002","reference_id":"28393837","start":745,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"An atomic model of the cleaved MERS-CoV S1/S2 trimer was built de novo using the 3.7 Å map, except for the flexible regions of S1 CTD and part of S1 NTD, which were fitted by crystal structures. The final model includes residues 18–1,206, with several small breaks due to the poor densities.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains. <i> Yuan Y, Cao D, Zhang Y, Ma J, Qi J, Wang Q, Lu G, Wu Y, Yan J, Shi Y, Zhang X, Gao GF. </i> Nat Commun, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"5X5F"},{"db":"PDB","id":"5X59"},{"db":"PDB","id":"5X5C"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T08:40:53.393Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":1294,"region_id":"DP02880r003","reference_id":"28393837","start":1207,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"An atomic model of the cleaved MERS-CoV S1/S2 trimer was built de novo using the 3.7 Å map, except for the flexible regions of S1 CTD and part of S1 NTD, which were fitted by crystal structures. The final model includes residues 18–1,206, with several small breaks due to the poor densities.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains. <i> Yuan Y, Cao D, Zhang Y, Ma J, Qi J, Wang Q, Lu G, Wu Y, Yan J, Shi Y, Zhang X, Gao GF. </i> Nat Commun, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"5X5F"},{"db":"PDB","id":"5X59"},{"db":"PDB","id":"5X5C"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T08:40:37.555Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":379,"region_id":"DP02880r004","reference_id":"29514901","start":367,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Flexible region in the crystal structure of MERS-CoV S1 RBD in complex with neutralizing antibody CDC2-C2.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Importance of Neutralizing Monoclonal Antibodies Targeting Multiple Antigenic Sites on the Middle East Respiratory Syndrome Coronavirus Spike Glycoprotein To Avoid Neutralization Escape. <i> Wang L, Shi W, Chappell JD, Joyce MG, Zhang Y, Kanekiyo M, Becker MM, van Doremalen N, Fischer R, Wang N, Corbett KS, Choe M, Mason RD, Van Galen JG, Zhou T, Saunders KO, Tatti KM, Haynes LM, Kwong PD, Modjarrad K, Kong WP, McLellan JS, Denison MR, Munster VJ, Mascola JR, Graham BS. </i> J Virol, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6C6Z"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T08:35:34.464Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":437,"region_id":"DP02880r005","reference_id":"29514901","start":427,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Flexible region in the crystal structure of MERS-CoV S1 RBD in complex with neutralizing antibody CDC2-C2.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Importance of Neutralizing Monoclonal Antibodies Targeting Multiple Antigenic Sites on the Middle East Respiratory Syndrome Coronavirus Spike Glycoprotein To Avoid Neutralization Escape. <i> Wang L, Shi W, Chappell JD, Joyce MG, Zhang Y, Kanekiyo M, Becker MM, van Doremalen N, Fischer R, Wang N, Corbett KS, Choe M, Mason RD, Van Galen JG, Zhou T, Saunders KO, Tatti KM, Haynes LM, Kwong PD, Modjarrad K, Kong WP, McLellan JS, Denison MR, Munster VJ, Mascola JR, Graham BS. </i> J Virol, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6C6Z"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T08:35:29.831Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":589,"region_id":"DP02880r006","reference_id":"29514901","start":579,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Flexible region in the crystal structure of MERS-CoV S1 RBD in complex with neutralizing antibody CDC2-C2.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Importance of Neutralizing Monoclonal Antibodies Targeting Multiple Antigenic Sites on the Middle East Respiratory Syndrome Coronavirus Spike Glycoprotein To Avoid Neutralization Escape. <i> Wang L, Shi W, Chappell JD, Joyce MG, Zhang Y, Kanekiyo M, Becker MM, van Doremalen N, Fischer R, Wang N, Corbett KS, Choe M, Mason RD, Van Galen JG, Zhou T, Saunders KO, Tatti KM, Haynes LM, Kwong PD, Modjarrad K, Kong WP, McLellan JS, Denison MR, Munster VJ, Mascola JR, Graham BS. </i> J Virol, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6C6Z"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T08:35:28.048Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":380,"region_id":"DP02880r007","reference_id":"28472421","start":366,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Flexible region in the crystal structure of MERS-CoV S1 RBD in complex with a fully human antibody MCA1.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Human Neutralizing Monoclonal Antibody Inhibition of Middle East Respiratory Syndrome Coronavirus Replication in the Common Marmoset. <i> Chen Z, Bao L, Chen C, Zou T, Xue Y, Li F, Lv Q, Gu S, Gao X, Cui S, Wang J, Qin C, Jin Q. </i> J Infect Dis, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5GMQ"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T08:25:03.057Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":380,"region_id":"DP02880r008","reference_id":"26370782","start":367,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Flexible region in the crystal structure of MERS-CoV S1 RBD in complex with neutralizing antibody m336.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Junctional and allele-specific residues are critical for MERS-CoV neutralization by an exceptionally potent germline-like antibody. <i> Ying T, Prabakaran P, Du L, Shi W, Feng Y, Wang Y, Wang L, Li W, Jiang S, Dimitrov DS, Zhou T. </i> Nat Commun, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4XAK"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T08:24:33.191Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":601,"region_id":"DP02880r009","reference_id":"26370782","start":591,"term_id":"IDPO:0000002","curator_orcid":"0000-0002-0341-4888","statement":[{"text":"Flexible region in the crystal structure of MERS-CoV S1 RBD in complex with neutralizing antibody m336.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"reference_html":"Junctional and allele-specific residues are critical for MERS-CoV neutralization by an exceptionally potent germline-like antibody. <i> Ying T, Prabakaran P, Du L, Shi W, Feng Y, Wang Y, Wang L, Li W, Jiang S, Dimitrov DS, Zhou T. </i> Nat Commun, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4XAK"}],"term_name":"disorder","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T08:24:25.295Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_06","ncbi_taxon_id":1263720,"disprot_id":"DP02880","date":"2020-05-18T08:36:41.227Z","organism":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012)","regions_counter":9,"name":"Spike glycoprotein","dataset":["Viral proteins"],"UniParc":"UPI00029EDFAA","uniref100":"UniRef100_K9N5Q8","uniref90":"UniRef90_K9N5Q8","uniref50":"UniRef50_K9N5Q8","genes":[{"name":{"value":"S","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04099","url":"https://hamap.expasy.org/unirule/MF_04099"}}]},"orfNames":[{"value":"3"}]}],"disorder_content":0.11751662971175167,"disprot_consensus":{"full":[{"start":366,"end":380,"type":"D"},{"start":427,"end":437,"type":"D"},{"start":579,"end":589,"type":"D"},{"start":591,"end":601,"type":"D"},{"start":699,"end":709,"type":"D"},{"start":745,"end":756,"type":"D"},{"start":1207,"end":1294,"type":"D"}],"Structural state":[{"start":366,"end":380,"type":"D"},{"start":427,"end":437,"type":"D"},{"start":579,"end":589,"type":"D"},{"start":591,"end":601,"type":"D"},{"start":699,"end":709,"type":"D"},{"start":745,"end":756,"type":"D"},{"start":1207,"end":1294,"type":"D"}]}},{"acc":"Q09428","features":{"gene3D":[{"start":978,"end":1325,"id":"G3DSA:1.20.1560.10","name":"ABC transporter type 1, transmembrane domain"},{"start":978,"end":1325,"id":"G3DSA:1.20.1560.10","name":"ABC transporter type 1, transmembrane domain"}],"pfam":[{"id":"PF00005","name":"ABC transporter","start":696,"end":856},{"id":"PF00005","name":"ABC transporter","start":1361,"end":1509},{"id":"PF00664","name":"ABC transporter transmembrane region","start":304,"end":590},{"id":"PF00664","name":"ABC transporter transmembrane region","start":1014,"end":1292}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MPLAFCGSENHSAAYRVDQGVLNNGCFVDALNVVPHVFLLFITFPILFIGWGSQSSKVHIHHSTWLHFPGHNLRWILTFMLLFVLVCEIAEGILSDGVTESHHLHLYMPAGMAFMAAVTSVVYYHNIETSNFPKLLIALLVYWTLAFITKTIKFVKFLDHAIGFSQLRFCLTGLLVILYGMLLLVEVNVIRVRRYIFFKTPREVKPPEDLQDLGVRFLQPFVNLLSKGTYWWMNAFIKTAHKKPIDLRAIGKLPIAMRALTNYQRLCEAFDAQVRKDIQGTQGARAIWQALSHAFGRRLVLSSTFRILADLLGFAGPLCIFGIVDHLGKENDVFQPKTQFLGVYFVSSQEFLANAYVLAVLLFLALLLQRTFLQASYYVAIETGINLRGAIQTKIYNKIMHLSTSNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAIYTSISIFMNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKLSEFLSSAEIREEQCAPHEPTPQGPASKYQAVPLRVVNRKRPAREDCRGLTGPLQSLVPSADGDADNCCVQIMGGYFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDPSPERETATDLDIRKRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSECQLFEHWKTLMNRQDQELEKETVTERKATEPPQGLSRAMSSRDGLLQDEEEEEEEAAESEEDDNLSSMLHQRAEIPWRACAKYLSSAGILLLSLLVFSQLLKHMVLVAIDYWLAKWTDSALTLTPAARNCSLSQECTLDQTVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAVTSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIHGLLKTEAESYEGLLAPSLIPKNWPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSVFASFVRADK","length":1581,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":676,"region_id":"DP02881r001","start":621,"term_id":"IDPO:0000002","statement":[{"text":"Flexible linker connecting the ABC transporter transmembrane region domain and ABC transporter 1 domain.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29286281","version":2,"reference_html":"Molecular structure of human KATP in complex with ATP and ADP. <i> Lee KPK, Chen J, MacKinnon R. </i> Elife, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6C3P"},{"db":"PDB","id":"6C3O"}],"term_name":"disorder","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:41:59.714Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":676,"region_id":"DP02881r002","start":621,"term_id":"IDPO:0000033","statement":[{"text":"Flexible linker connecting the ABC transporter transmembrane region domain and ABC transporter 1 domain.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29286281","version":4,"reference_html":"Molecular structure of human KATP in complex with ATP and ADP. <i> Lee KPK, Chen J, MacKinnon R. </i> Elife, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:42:00.504Z"},"ec_go":"IDA","disprot_namespace":"Disorder function"}],"released":"2020_12","ncbi_taxon_id":9606,"disprot_id":"DP02881","date":"2020-05-26T09:59:10.646Z","organism":"Homo sapiens","regions_counter":2,"name":"ATP-binding cassette sub-family C member 8","dataset":[],"UniParc":"UPI000016B078","uniref100":"UniRef100_Q09428","uniref90":"UniRef90_Q09428","uniref50":"UniRef50_Q09428","genes":[{"name":{"value":"ABCC8"},"synonyms":[{"value":"HRINS"},{"value":"SUR"},{"value":"SUR1"}]}],"alphafold_very_low_content":0.08855154965211891,"disorder_content":0.03542061986084757,"disprot_consensus":{"full":[{"start":621,"end":676,"type":"D"}],"Structural state":[{"start":621,"end":676,"type":"D"}],"Disorder function":[{"start":621,"end":676,"type":"F"}]}},{"acc":"Q6A070","features":{"gene3D":[{"start":1542,"end":1772,"id":"G3DSA:1.25.10.10","name":"Leucine-rich Repeat Variant"},{"start":1542,"end":1772,"id":"G3DSA:1.25.10.10","name":"Leucine-rich Repeat Variant"},{"start":1542,"end":1772,"id":"G3DSA:1.25.10.10","name":"Leucine-rich Repeat Variant"},{"start":1542,"end":1772,"id":"G3DSA:1.25.10.10","name":"Leucine-rich Repeat Variant"}],"pfam":[]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MAAAPSELLPLPPPATPGSYRLLSRCRPYAPGTDGRRSGGTMRGEKNYYCRGAAGDHGSCPATPSPLASTLLLPAEAVSTSWSGPGSGLSGGDEEETRLLQLLRTAPDPSEAFQALQAALPRRGGRLGFPRRKEALYRALGRVLVEGGSEEKRLCLQLLSDVLRGQGEAGQLEEAFSLALLPQLVVSLREDNPALRKDALQILHICLRRSSGQVLRTLIQGLESPDARLRASTALLLPILFTPEDLLQGLDLTEVIISLARKLGDQEMEEESETAFSSLQQIGERLGQERFHSYISRLPSALRRHYNRRLESQYGSQVPYYLELEASGFSEDAAPCVVNLSSSNLKFEIIPQELHARLLDQEDYKNRTQAVEELKQLLGKFNPSSTPHASLVGFISLLYNLLDDSNFKVVHGTLQVLHLLVIRLGEQVQQFLGPVIAASVKVLADNKLVIKQEYMKIFLKLMKEVGPQRVLSLLLENLKHKHSRVREEVVNICICSLLTYPSEDFDLPKLSFDLAPALVDSKRRVRQAALEAFAVLASSMGSGKTNVLFKAVDTVELQDNGDGVMNAVQARLARKTLPRLTEQGFVEYAILMPSSAQGRSSHLAHGADTDWLMSGNRTQSAHCYCGDHTRDSMQLYGSYSPTICTRRVLSAGKGKNKLPWENEQPGVMGENQTSNSKDIKDTEQFSAHDLIPSPKLKPSQGMPASDDLCFSKKRSSRNLFQSSRDFNSESVPTCGAGNTADLQTNLPGKCGQLGLSQIGCRTGSVGSDLQFLGTANGHQDKVYASIDFGSKTQQTFGSQSERTSSYSGSNASPGSFILPSYPLASPRTSPKHTSPLSVAPKKSQDNSISFSNSWPLKSFEGLSKPSPQKKLANQKSSDPTGENFQEKTTAVQLTPALVRSPSSRRGLNGTKPVPPIPRGINLLPDKADLSTMGHMKKQPDDIWKSEKDNLTIDLSELNFRDKDLDQEEMHSSLRSLRNSAAKKRAKLSGSSSTSDVDSPDSAMKLELTIDSPSRASSPNISSYSESGVYSQESLTSSLSTTPQGKRIMSDIFPTFGSKPCSTRLSSAKKTSHAAEQSPSAGFTRSSNLQQISSFDFTSTNTLSEDSVVIVGKGVFGNPNSAPTTCSQPVISSVESEDTFPVKPSIEPPSGVYGRAVQHNAPLYPEVENDKDTKVSIAKSTYEKMRQKRKEEKELLDAKDCERKETNPWERIKHLGSEKMTSENEPSSGVIPQYKERMSSVTHSPEIMDSLELRPFSKPDIALTEALRLLADEDWEKKMEGLNFVRCLAAFHSDLLNTKLHETTFAVVQEVKNLRSGVSRAAVVCLGDLFTYLKKSMDQELDSAVRALLHKAGESNTFIREDVDKALKAMVNNVTPARAVTSLINGGQSHLHIAVRRCTAQHLADVVECMDPERISSGTKDMADRLLPAAAKFAQDSSQETRYYGRKMLFLMMGHPNFEKLLEKYIPSKDLPYIKESVKNLRLKGLGEIPLDTASAKGRRSHPGSVGNTRSSSVSRDAFSSSEREVTEVREVPRKSAPRNSLESAEYIKVITGLLNAKDFRDRINGIKQLLSDTENNQELVVGNIVKIFDAFKSRLHDSNSKVNLVALETMHKMIPLLRDNLSPIINMLIPAIVDNNLNSKNPGIYAAATNVVHALSQHVDNYLLLQPFCTKAQFLNGKAKQDMTEKLADIVTELYQRKPHATEQKVLVVLWHLLGNMTHSGSLPGAGGNIRTATAKLSKALFTQMGQNLLNQAASQPPHIKKSLEELLDVTVLSEL","length":1776,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":620,"region_id":"DP02882r001","start":595,"term_id":"IDPO:0000002","statement":[{"text":"No clear electron density was evident for N-terminal residues 332–344, HR A loops residues 361–365, HR F residues 558–562, and the C-terminal residues 595–620.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26378256","version":2,"reference_html":"Crescerin uses a TOG domain array to regulate microtubules in the primary cilium. <i> Das A, Dickinson DJ, Wood CC, Goldstein B, Slep KC. </i> Mol Biol Cell, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5DN7"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","ncbi_taxon_id":10090,"disprot_id":"DP02882","date":"2020-05-27T08:23:15.603Z","organism":"Mus musculus","regions_counter":1,"name":"TOG array regulator of axonemal microtubules protein 1","dataset":[],"UniParc":"UPI00003FEF0B","uniref100":"UniRef100_Q6A070","uniref90":"UniRef90_Q6A070","uniref50":"UniRef50_Q6A070","genes":[{"name":{"value":"Togaram1"},"synonyms":[{"value":"Fam179b"},{"value":"Kiaa0423"}]}],"alphafold_very_low_content":0.4358108108108108,"disorder_content":0.01463963963963964,"disprot_consensus":{"full":[{"start":595,"end":620,"type":"D"}],"Structural state":[{"start":595,"end":620,"type":"D"}]}},{"acc":"F1QR43","features":{"gene3D":[],"pfam":[{"id":"PF06662","name":"D-glucuronyl C5-epimerase C-terminus","start":385,"end":576},{"id":"PF21174","name":"D-glucuronyl C5-epimerase, beta-sandwich domain","start":237,"end":356}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Actinopterygii","Neopterygii","Teleostei","Ostariophysi","Cypriniformes","Danionidae","Danioninae","Danio"],"sequence":"MMRCLAARVHYKTLIVICALLSLLTVLLWNKCTSEKALRFLPRHPQPPPSPKIDSHPQQPQPPEPPPVVGGVRYEEIDCLINDDATIKGRREGSEVYMPFSWMEKYFEVYGKVVQYDGYDRFEFSHSYSKVYAQREQYHPNGVFMSFEGYNVEVRDRVKCISGVEGVPLSTQWGPQGYFYAIQIAQYGLSHYSKNLTERPPHVEVYDTAEERDSRSSAWTVPKGCSLTRVYDKTRATSVRQFSAPENSEGVSLPLGNTKDFIISFDLKFTSNGSVSVILETTEKGPPFVIHYVTTTQLILLKDRDITYGIGPRTTWTTVTRDLLTDLRKGIGLSNTKAVKATKTMPRRVVKLVVHGTGTIDNITISTTSHMAAFYAASDWLVRNQDERGGWPIMVTRKLGEGFRALEPGWYSAMAQGQAMSTLVRAYLMTKDDTYLKAALRATGPFKLPSEQHGVKAVFMNKYDWYEEYPTIPSSFVLNGFIYSLIGLFDLAQTAGEKLGRDAGQLYSKGMESLKVMLPLYDTGSGTIYDLRHFILGTAPNLARWDYHTTHINQLQLLGTIDNSPIFRDSVKRWKSYLKGGRAKHN","length":586,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":72,"region_id":"DP02883r001","start":51,"term_id":"IDPO:0000002","statement":[{"text":"The final model has excellent density for most residues except for the N-terminal flexible loop (Pro50–Val71) and a small internal loop (Asp212–Ser215).","type":"Methods"},{"text":"the N-terminal flexible loop at Pro50–Val71 corresponds to Pro51-Val72.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"25568314","version":2,"reference_html":"Structural and functional study of D-glucuronyl C5-epimerase. <i> Qin Y, Ke J, Gu X, Fang J, Wang W, Cong Q, Li J, Tan J, Brunzelle JS, Zhang C, Jiang Y, Melcher K, Li JP, Xu HE, Ding K. </i> J Biol Chem, 2015","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4PXQ"},{"db":"PDB","id":"4PW2"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-27T18:18:46.857Z"}}],"released":"2021_06","ncbi_taxon_id":7955,"disprot_id":"DP02883","date":"2020-05-27T09:21:01.939Z","organism":"Danio rerio","regions_counter":1,"name":"D-glucuronyl C5-epimerase B","dataset":[],"UniParc":"UPI0000EB6EB1","uniref100":"UniRef100_F1QR43","uniref90":"UniRef90_F1QR43","uniref50":"UniRef50_O94923","genes":[{"name":{"value":"glceb","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16156897","url":"http://www.ncbi.nlm.nih.gov/pubmed/16156897","alternativeUrl":"https://europepmc.org/abstract/MED/16156897"}},{"code":"ECO:0000312","source":{"name":"ZFIN","id":"ZDB-GENE-040630-8","url":"http://zfin.org/cgi-bin/webdriver?MIval=aa-markerview.apg&OID=ZDB-GENE-040630-8"}}]}}],"alphafold_very_low_content":0.06484641638225255,"disorder_content":0.03754266211604096,"disprot_consensus":{"full":[{"start":51,"end":72,"type":"D"}],"Structural state":[{"start":51,"end":72,"type":"D"}]}},{"acc":"F1RE08","features":{"gene3D":[{"start":12,"end":480,"id":"G3DSA:1.10.630.10","name":"Cytochrome P450"}],"pfam":[{"id":"PF00067","name":"Cytochrome P450","start":33,"end":466}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Actinopterygii","Neopterygii","Teleostei","Ostariophysi","Cypriniformes","Danionidae","Danioninae","Danio"],"sequence":"MMWTALLLVGLSILVIVLYGRRTRRRNEPPLDKGMIPWLGHALEFGKDAAKFLTRMKEKHGDIFTVRAAGLYITVLLDSNCYDAVLSDVASLDQTSYAQVLMKRIFNMILPSHNPESEKKRAEMHFQGASLTQLSNSMQNNLRLLMTPSEMGLKTSEWKKDGLFNLCYSLLFKTGYLTVFGAENNDSAALTQIYEEFRRFDKLLPKLARTTINKEEKQIASAAREKLWKWLTPSGLDRKPREQSWLGSYVKQLQDEGIDAEMQRRAMLLQLWVTQGNAGPAAFWVMGYLLTHPEALRAVREEIQGGKHLRLEERQKNTPVFDSVLWETLRLTAAALITRDVTQDKKIRLSNGQEYHLRRGDRLCVFPFISPQMDPQIHQQPEMFQFDRFLNADRTEKKDFFKNGARVKYPSVPWGTEDNLCPGRHFAVHAIKELVFTILTRFDVELCDKNATVPLVDPSRYGFGILQPAGDLEIRYRIRF","length":480,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":316,"region_id":"DP02884r001","start":305,"term_id":"IDPO:0000002","statement":[{"text":"No electron density is associated with residues 305–316 of chain A and 155–157, 183–186, 232–243, and 305–316 of chain B, so these regions were omitted from the model.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18032380","version":2,"reference_html":"Structures of prostacyclin synthase and its complexes with substrate analog and inhibitor reveal a ligand-specific heme conformation change. <i> Li YC, Chiang CW, Yeh HC, Hsu PY, Whitby FG, Wang LH, Chan NL. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3B98"},{"db":"PDB","id":"3B99"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":243,"region_id":"DP02884r002","start":232,"term_id":"IDPO:0000002","statement":[{"text":"No electron density is associated with residues 305–316 of chain A and 155–157, 183–186, 232–243, and 305–316 of chain B, so these regions were omitted from the model.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18032380","version":2,"reference_html":"Structures of prostacyclin synthase and its complexes with substrate analog and inhibitor reveal a ligand-specific heme conformation change. <i> Li YC, Chiang CW, Yeh HC, Hsu PY, Whitby FG, Wang LH, Chan NL. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3B98"},{"db":"PDB","id":"3B99"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":7955,"disprot_id":"DP02884","date":"2020-05-27T09:29:39.550Z","organism":"Danio rerio","regions_counter":2,"name":"Prostacyclin synthase","dataset":[],"UniParc":"UPI00015A7684","uniref100":"UniRef100_F1RE08","uniref90":"UniRef90_F1RE08","uniref50":"UniRef50_F1RE08","genes":[{"name":{"value":"ptgis","evidences":[{"code":"ECO:0000312","source":{"name":"ZFIN","id":"ZDB-GENE-070116-1","url":"http://zfin.org/cgi-bin/webdriver?MIval=aa-markerview.apg&OID=ZDB-GENE-070116-1"}}]},"synonyms":[{"value":"ptgisl","evidences":[{"code":"ECO:0000312","source":{"name":"ZFIN","id":"ZDB-GENE-070116-1","url":"http://zfin.org/cgi-bin/webdriver?MIval=aa-markerview.apg&OID=ZDB-GENE-070116-1"}}]}]}],"alphafold_very_low_content":0.00625,"disorder_content":0.05,"disprot_consensus":{"full":[{"start":232,"end":243,"type":"D"},{"start":305,"end":316,"type":"D"}],"Structural state":[{"start":232,"end":243,"type":"D"},{"start":305,"end":316,"type":"D"}]}},{"acc":"Q10589","features":{"gene3D":[],"pfam":[{"id":"PF16716","name":"Bone marrow stromal antigen 2","start":49,"end":136}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MASTSYDYCRVPMEDGDKRCKLLLGIGILVLLIIVILGVPLIIFTIKANSEACRDGLRAVMECRNVTHLLQQELTEAQKGFQDVEAQAATCNHTVMALMASLDAEKAQGQKKVEELEGEITTLNHKLQDASAEVERLRRENQVLSVRIADKKYYPSSQDSSSAAAPQLLIVLLGLSALLQ","length":180,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":89,"region_id":"DP02885r001","start":79,"term_id":"IDPO:0000002","statement":[{"text":"This might be due to flexibility within the region (residues 79 to 89) connecting the N-terminal and coiled-coil domains as documented by the sensitivity to proteolysis and the absence of an ordered structure for residues 80 to 88.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20399176","version":2,"reference_html":"Structural basis of HIV-1 tethering to membranes by the BST-2/tetherin ectodomain. <i> Hinz A, Miguet N, Natrajan G, Usami Y, Yamanaka H, Renesto P, Hartlieb B, McCarthy AA, Simorre JP, Göttlinger H, Weissenhorn W. </i> Cell Host Microbe, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":89,"region_id":"DP02885r002","start":79,"term_id":"IDPO:0000033","statement":[{"text":"This might be due to flexibility within the region (residues 79 to 89) connecting the N-terminal and coiled-coil domains as documented by the sensitivity to proteolysis and the absence of an ordered structure for residues 80 to 88.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20399176","version":3,"reference_html":"Structural basis of HIV-1 tethering to membranes by the BST-2/tetherin ectodomain. <i> Hinz A, Miguet N, Natrajan G, Usami Y, Yamanaka H, Renesto P, Hartlieb B, McCarthy AA, Simorre JP, Göttlinger H, Weissenhorn W. </i> Cell Host Microbe, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02885","date":"2020-05-27T10:41:38.938Z","organism":"Homo sapiens","regions_counter":2,"name":"Bone marrow stromal antigen 2","dataset":[],"UniParc":"UPI000004494D","uniref100":"UniRef100_Q10589","uniref90":"UniRef90_Q10589","uniref50":"UniRef50_Q10589","genes":[{"name":{"value":"BST2"}}],"alphafold_very_low_content":0.06666666666666667,"disorder_content":0.06111111111111111,"disprot_consensus":{"full":[{"start":79,"end":89,"type":"D"}],"Structural state":[{"start":79,"end":89,"type":"D"}],"Disorder function":[{"start":79,"end":89,"type":"F"}]}},{"acc":"Q5QGG3","features":{"gene3D":[{"start":93,"end":235,"id":"G3DSA:3.30.62.10","name":"Nef Regulatory Factor"}],"pfam":[{"id":"PF00469","name":"Negative factor, (F-Protein) or Nef","start":2,"end":234}]},"creator":"lchemes","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"sequence":"MGGAISMRRSRPSGDLRQRLLRARGETYGRLLGEVEDGYSQSPGGLDKGLSSLSCEGQKYNQGQYMNTPWRNPAEEREKLAYRKQNMDDIDEZDDDLVGVSVRPKVPLRTMSYKLAIDMSHFIKEKGGLEGIYYSARRHRILDIYLEKEEGIIPDWQDYTSGPGIRYPKTFGWLWKLVPVNVSDEAQEDEEHYLMHPAQTSQWDDPWGEVLAWKFDPTLAYTYEAYVRYPEEFGSKSGLSEEEVRRRLTARGLLNMADKKETR","length":263,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":202,"region_id":"DP02886r001","start":184,"term_id":"IDPO:0000002","statement":[{"text":"Here, we determine the structure of SIVmac239 Nef bound to the ExxxLM motif of another Nef molecule at 2.5 Å resolution. This provides a basis for a structural model, where a hydrophobic crevice in simian immunodeficiency virus (SIV) Nef targets a dileucine motif in CD4 and a tyrosine-based motif in CD3","type":"Introduction"},{"text":"The model contains residues 103–233 of SIV Nef and residues 80–134 of the SH3 domain, whereas no electron density was identified for the CD4 peptide (Fig. 1a). ","type":"Results"},{"text":"Residues 66-102 (PDB 5nuh) and 87-106 (5nui) are disordered in all structures, and Residues 184-202 containing the ExxxLL sorting motif (5nui) are disordered in the unbound state","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"28874665","version":2,"reference_html":"Endocytic sorting motif interactions involved in Nef-mediated downmodulation of CD4 and CD3. <i> Manrique S, Sauter D, Horenkamp FA, Lülf S, Yu H, Hotter D, Anand K, Kirchhoff F, Geyer M. </i> Nat Commun, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5NUI"},{"db":"PDB","id":"5NUH"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":102,"region_id":"DP02886r002","start":66,"term_id":"IDPO:0000002","statement":[{"text":"Here, we determine the structure of SIVmac239 Nef bound to the ExxxLM motif of another Nef molecule at 2.5 Å resolution. This provides a basis for a structural model, where a hydrophobic crevice in simian immunodeficiency virus (SIV) Nef targets a dileucine motif in CD4 and a tyrosine-based motif in CD3","type":"Introduction"},{"text":"The model contains residues 103–233 of SIV Nef and residues 80–134 of the SH3 domain, whereas no electron density was identified for the CD4 peptide (Fig. 1a). ","type":"Results"},{"text":"Residues 66-102 (PDB 5nuh) and 87-106 (5nui) are disordered in all structures, and Residues 184-202 containing the ExxxLL sorting motif (5nui) are disordered in the unbound state","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"28874665","version":2,"reference_html":"Endocytic sorting motif interactions involved in Nef-mediated downmodulation of CD4 and CD3. <i> Manrique S, Sauter D, Horenkamp FA, Lülf S, Yu H, Hotter D, Anand K, Kirchhoff F, Geyer M. </i> Nat Commun, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5NUI"},{"db":"PDB","id":"5NUH"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":106,"region_id":"DP02886r003","start":87,"term_id":"IDPO:0000011","statement":[{"text":"Here, we determine the structure of SIVmac239 Nef bound to the ExxxLM motif of another Nef molecule at 2.5 Å resolution. This provides a basis for a structural model, where a hydrophobic crevice in simian immunodeficiency virus (SIV) Nef targets a dileucine motif in CD4 and a tyrosine-based motif in CD3","type":"Abstract"},{"text":"Nef… contains an N-terminal membrane anchor domain of 60–120 amino acids length followed by a core domain of 130–150 amino acids, containing a highly conserved dileucine-based sorting motif at the center of a C-terminal flexible loop27. This exposed sorting motif enables Nef to interact with AP2 and to induce the internalization of its target receptors. ","type":"Introduction"},{"text":"Residues 66-102 (PDB 5nuh) and 87-106 (5nui) are disordered in all structures, and Residues 184-202 containing the ExxxLL sorting motif (5nui) are disordered in the unbound state [...] At the contact interfaces a three-fold rotational symmetry appears with each C-terminal flexible loop of Nef contacting the sorting motif recognition site of the neighboring Nef–SH3 heterodimer (Fig. 1a). In this crystallographic assembly, the EEHYLM sorting motif of the C-terminal flexible loop interacts with the hydrophobic crevice [...] Again, the sorting motif of one Nef molecule in the asymmetric units contacts the hydrophobic crevice of another Nef molecule (Fig. 1b). In this structure, the electron density map was visible for all residues in the dileucine-based sorting motif, providing detailed molecular insights into the interaction of Nef with endocytic sorting motifs (Fig. 1c). ","type":"Results"},{"text":"The region encompassing the ExxxLL sorting motif (5nui) becomes ordered in the Nef-bound state, emulating its interaction with the AP2 adaptor complex","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"28874665","version":2,"reference_html":"Endocytic sorting motif interactions involved in Nef-mediated downmodulation of CD4 and CD3. <i> Manrique S, Sauter D, Horenkamp FA, Lülf S, Yu H, Hotter D, Anand K, Kirchhoff F, Geyer M. </i> Nat Commun, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"5NUI"},{"db":"PDB","id":"5NUH"}],"term_name":"disorder to order","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":106,"region_id":"DP02886r004","start":87,"term_id":"GO:0005515","statement":[{"text":"Here, we determine the structure of SIVmac239 Nef bound to the ExxxLM motif of another Nef molecule at 2.5 Å resolution. This provides a basis for a structural model, where a hydrophobic crevice in simian immunodeficiency virus (SIV) Nef targets a dileucine motif in CD4 and a tyrosine-based motif in CD3","type":"Abstract"},{"text":"Nef… contains an N-terminal membrane anchor domain of 60–120 amino acids length followed by a core domain of 130–150 amino acids, containing a highly conserved dileucine-based sorting motif at the center of a C-terminal flexible loop27. This exposed sorting motif enables Nef to interact with AP2 and to induce the internalization of its target receptors. ","type":"Introduction"},{"text":"Residues 66-102 (PDB 5nuh) and 87-106 (5nui) are disordered in all structures, and Residues 184-202 containing the ExxxLL sorting motif (5nui) are disordered in the unbound state [...] At the contact interfaces a three-fold rotational symmetry appears with each C-terminal flexible loop of Nef contacting the sorting motif recognition site of the neighboring Nef–SH3 heterodimer (Fig. 1a). In this crystallographic assembly, the EEHYLM sorting motif of the C-terminal flexible loop interacts with the hydrophobic crevice [...] Again, the sorting motif of one Nef molecule in the asymmetric units contacts the hydrophobic crevice of another Nef molecule (Fig. 1b). In this structure, the electron density map was visible for all residues in the dileucine-based sorting motif, providing detailed molecular insights into the interaction of Nef with endocytic sorting motifs (Fig. 1c). ","type":"Results"},{"text":"The region encompassing the ExxxLL sorting motif (5nui) becomes ordered in the Nef-bound state, emulating its interaction with the AP2 adaptor complex","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"28874665","version":3,"reference_html":"Endocytic sorting motif interactions involved in Nef-mediated downmodulation of CD4 and CD3. <i> Manrique S, Sauter D, Horenkamp FA, Lülf S, Yu H, Hotter D, Anand K, Kirchhoff F, Geyer M. </i> Nat Commun, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"5NUI"},{"db":"PDB","id":"5NUH"}],"term_name":"protein binding","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Biological process","ec_ontology":"ECO","end":106,"region_id":"DP02886r005","start":87,"term_id":"GO:0019065","statement":[{"text":"Here, we determine the structure of SIVmac239 Nef bound to the ExxxLM motif of another Nef molecule at 2.5 Å resolution. This provides a basis for a structural model, where a hydrophobic crevice in simian immunodeficiency virus (SIV) Nef targets a dileucine motif in CD4 and a tyrosine-based motif in CD3","type":"Abstract"},{"text":"Nef… contains an N-terminal membrane anchor domain of 60–120 amino acids length followed by a core domain of 130–150 amino acids, containing a highly conserved dileucine-based sorting motif at the center of a C-terminal flexible loop27. This exposed sorting motif enables Nef to interact with AP2 and to induce the internalization of its target receptors. ","type":"Introduction"},{"text":"Again, the sorting motif of one Nef molecule in the asymmetric units contacts the hydrophobic crevice of another Nef molecule (Fig. 1b). In this structure, the electron density map was visible for all residues in the dileucine-based sorting motif, providing detailed molecular insights into the interaction of Nef with endocytic sorting motifs (Fig. 1c). ","type":"Results"},{"text":"We find that Nef is indeed able to act like an adapter by binding to dileucine-based sorting motifs embedded in the plasma membrane while simultaneously exposing its own dileucine motif within the C-terminal flexible loop to the cytosol. This is possible by a dipolar electrostatic surface charge character of Nef. The hydrophobic crevice that interacts with the dileucine motifs is surrounded by positively charged residues, whereas the C-terminal flexible loop with the ExxxLL sorting motif in its center is largely negatively charged. This enables Nef to pick up the cytosolic tail sequences of T cell surface receptors at the plasma membrane and couple them to the endocytic adapter protein machinery. ","type":"Discussion"}],"curator_id":"lchemes","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"28874665","version":3,"reference_html":"Endocytic sorting motif interactions involved in Nef-mediated downmodulation of CD4 and CD3. <i> Manrique S, Sauter D, Horenkamp FA, Lülf S, Yu H, Hotter D, Anand K, Kirchhoff F, Geyer M. </i> Nat Commun, 2017","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"5NUI"},{"db":"PDB","id":"5NUH"}],"term_name":"receptor-mediated endocytosis of virus by host cell","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any receptor-mediated endocytosis that is involved in the uptake of a virus into a host cell; successive instances of virus endocytosis result in the accumulation of virus particles within the cell.\" [GOC:bf, GOC:jl, ISBN:0781702534]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2020_12","ncbi_taxon_id":11723,"disprot_id":"DP02886","date":"2020-05-28T22:51:00.891Z","organism":"Simian immunodeficiency virus","regions_counter":5,"name":"Protein Nef","dataset":["Viral proteins"],"UniParc":"UPI000048E2E2","uniref100":"UniRef100_Q5QGG3","uniref90":"UniRef90_P31818","uniref50":"UniRef50_P18092","genes":[{"name":{"value":"nef","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAV65326.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAV65326.1"}}]}}],"disorder_content":0.21292775665399238,"disprot_consensus":{"full":[{"start":66,"end":86,"type":"D"},{"start":87,"end":106,"type":"T"},{"start":184,"end":202,"type":"D"}],"Structural state":[{"start":66,"end":102,"type":"D"},{"start":184,"end":202,"type":"D"}],"Structural transition":[{"start":87,"end":106,"type":"T"}],"Molecular function":[{"start":87,"end":106,"type":"F"}],"Biological process":[{"start":87,"end":106,"type":"F"}]}},{"acc":"P62944","features":{"gene3D":[{"start":1,"end":591,"id":"G3DSA:1.25.10.10","name":"Leucine-rich Repeat Variant"},{"start":822,"end":937,"id":"G3DSA:3.30.310.10","name":"TATA-Binding Protein"},{"start":705,"end":821,"id":"G3DSA:2.60.40.1150","name":"G3DSA:2.60.40.1150"}],"pfam":[{"id":"PF01602","name":"Adaptin N terminal region","start":12,"end":533},{"id":"PF02883","name":"Adaptin C-terminal domain","start":712,"end":817},{"id":"PF09066","name":"Beta2-adaptin appendage, C-terminal sub-domain","start":827,"end":935}]},"creator":"lchemes","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"sequence":"MTDSKYFTTNKKGEIFELKAELNNEKKEKRKEAVKKVIAAMTVGKDVSSLFPDVVNCMQTDNLELKKLVYLYLMNYAKSQPDMAIMAVNSFVKDCEDPNPLIRALAVRTMGCIRVDKITEYLCEPLRKCLKDEDPYVRKTAAVCVAKLHDINAQMVEDQGFLDSLRDLIADSNPMVVANAVAALSEISESHPNSNLLDLNPQNINKLLTALNECTEWGQIFILDCLSNYNPKDDREAQSICERVTPRLSHANSAVVLSAVKVLMKFLELLPKDSDYYNMLLKKLAPPLVTLLSGEPEVQYVALRNINLIVQKRPEILKQEIKVFFVKYNDPIYVKLEKLDIMIRLASQANIAQVLAELKEYATEVDVDFVRKAVRAIGRCAIKVEQSAERCVSTLLDLIQTKVNYVVQEAIVVIRDIFRKYPNKYESIIATLCENLDSLDEPDARAAMIWIVGEYAERIDNADELLESFLEGFHDESTQVQLTLLTAIVKLFLKKPSETQELVQQVLSLATQDSDNPDLRDRGYIYWRLLSTDPVTAKEVVLSEKPLISEETDLIEPTLLDELICHIGSLASVYHKPPNAFVEGSHGIHRKHLPIHHGSTDAGDSPVGTTTATNLEQPQVIPSQGDLLGDLLNLDLGPPVNVPQVSSMQMGAVDLLGGGLDSLVGQSFIPSSVPATFAPSPTPAVVSSGLNDLFELSTGIGMAPGGYVAPKAVWLPAVKAKGLEISGTFTHRQGHIYMEMNFTNKALQHMTDFAIQFNKNSFGVIPSTPLAIHTPLMPNQSIDVSLPLNTLGPVMKMEPLNNLQVAVKNNIDVFYFSCLIPLNVLFVEDGKMERQVFLATWKDIPNENELQFQIKECHLNADTVSSKLQNNNVYTIAKRNVEGQDMLYQSLKLTNGIWILAELRIQPGNPNYTLSLKCRAPEVSQYIYQVYDSILKN","length":937,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":18,"region_id":"DP02887r001","start":7,"term_id":"IDPO:0000002","statement":[{"text":"We show by cryoelectron microscopy (cryo-EM) and allied methods that simian tetherin is targeted in a unique way by the induced refolding of the b subunit of AP-2 from an a-helix to a b-hairpin, creating a binding site for the (G/D)DIWK motif in a crevice between the new b-hairpin and Nef","type":"Abstract"},{"text":"However, when bound to both tetherin and Nef, b2 (peptide 7–18) underwent 40% less HD exchange (30 s) (Figures 4C and S4A). Slower deuteration was also seen in a and s2 residues in SIVsmm Nef binding regions (Figures S4B and S4C), as expected. The finding that protection from amide HD exchange in the b2 N terminus depends on the presence of both SIVsmm Nef and tetherin strongly supports the conclusions drawn from the cryo-EM structure, which shows that the presence of these two molecules together is required for refolding of this region","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"31447307","version":2,"reference_html":"Structural Basis for Tetherin Antagonism as a Barrier to Zoonotic Lentiviral Transmission. <i> Buffalo CZ, Stürzel CM, Heusinger E, Kmiec D, Kirchhoff F, Hurley JH, Ren X. </i> Cell Host Microbe, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006236","term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":18,"region_id":"DP02887r002","start":7,"term_id":"IDPO:0000011","statement":[{"text":"We show by cryoelectron microscopy (cryo-EM) and allied methods that simian tetherin is targeted in a unique way by the induced refolding of the b subunit of AP-2 from an a-helix to a b-hairpin, creating a binding site for the (G/D)DIWK motif in a crevice between the new b-hairpin and Nef","type":"Abstract"},{"text":"However, when bound to both tetherin and Nef, b2 (peptide 7–18) underwent 40% less HD exchange (30 s) (Figures 4C and S4A). Slower deuteration was also seen in a and s2 residues in SIVsmm Nef binding regions (Figures S4B and S4C), as expected. The finding that protection from amide HD exchange in the b2 N terminus depends on the presence of both SIVsmm Nef and tetherin strongly supports the conclusions drawn from the cryo-EM structure, which shows that the presence of these two molecules together is required for refolding of this region","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"31447307","version":2,"reference_html":"Structural Basis for Tetherin Antagonism as a Barrier to Zoonotic Lentiviral Transmission. <i> Buffalo CZ, Stürzel CM, Heusinger E, Kmiec D, Kirchhoff F, Hurley JH, Ren X. </i> Cell Host Microbe, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006236","term_name":"disorder to order","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":18,"region_id":"DP02887r003","start":7,"term_id":"GO:0005515","statement":[{"text":"We show by cryoelectron microscopy (cryo-EM) and allied methods that simian tetherin is targeted in a unique way by the induced refolding of the b subunit of AP-2 from an a-helix to a b-hairpin, creating a binding site for the (G/D)DIWK motif in a crevice between the new b-hairpin and Nef","type":"Abstract"},{"text":"However, when bound to both tetherin and Nef, b2 (peptide 7–18) underwent 40% less HD exchange (30 s) (Figures 4C and S4A). Slower deuteration was also seen in a and s2 residues in SIVsmm Nef binding regions (Figures S4B and S4C), as expected. The finding that protection from amide HD exchange in the b2 N terminus depends on the presence of both SIVsmm Nef and tetherin strongly supports the conclusions drawn from the cryo-EM structure, which shows that the presence of these two molecules together is required for refolding of this region","type":"Results"},{"text":"We used fluorescence polarization (FP) to determine that Alexa488-tetherin tail bound to AP2DmC and SIVsmm Nef with Kd = 2.7 mM ± 0.1 mM (Figures 1C and 1D), while binding to the separate components or to AP2hemi was undetectable. These data indicate that simian tetherin binds to the AP-2 core and SIVsmm Nef in a cooperative and high-affinity ternary complex that requires elements of the full AP-2 tetramer","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"31447307","version":3,"reference_html":"Structural Basis for Tetherin Antagonism as a Barrier to Zoonotic Lentiviral Transmission. <i> Buffalo CZ, Stürzel CM, Heusinger E, Kmiec D, Kirchhoff F, Hurley JH, Ren X. </i> Cell Host Microbe, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006236","cross_refs":[{"db":"PDB","id":"6OWT"}],"term_name":"protein binding","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":18,"region_id":"DP02887r004","start":7,"term_id":"GO:0098772","statement":[{"text":"We show by cryoelectron microscopy (cryo-EM) and allied methods that simian tetherin is targeted in a unique way by the induced refolding of the b subunit of AP-2 from an a-helix to a b-hairpin, creating a binding site for the (G/D)DIWK motif in a crevice between the new b-hairpin and Nef","type":"Abstract"},{"text":"However, when bound to both tetherin and Nef, b2 (peptide 7–18) underwent 40% less HD exchange (30 s) (Figures 4C and S4A). Slower deuteration was also seen in a and s2 residues in SIVsmm Nef binding regions (Figures S4B and S4C), as expected. The finding that protection from amide HD exchange in the b2 N terminus depends on the presence of both SIVsmm Nef and tetherin strongly supports the conclusions drawn from the cryo-EM structure, which shows that the presence of these two molecules together is required for refolding of this region","type":"Results"},{"text":"We used fluorescence polarization (FP) to determine that Alexa488-tetherin tail bound to AP2DmC and SIVsmm Nef with Kd = 2.7 mM ± 0.1 mM (Figures 1C and 1D), while binding to the separate components or to AP2hemi was undetectable. These data indicate that simian tetherin binds to the AP-2 core and SIVsmm Nef in a cooperative and high-affinity ternary complex that requires elements of the full AP-2 tetramer","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"31447307","version":3,"reference_html":"Structural Basis for Tetherin Antagonism as a Barrier to Zoonotic Lentiviral Transmission. <i> Buffalo CZ, Stürzel CM, Heusinger E, Kmiec D, Kirchhoff F, Hurley JH, Ren X. </i> Cell Host Microbe, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006236","term_name":"molecular function regulator","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":18,"region_id":"DP02887r005","start":7,"term_id":"GO:0098772","statement":[{"text":"We show by cryoelectron microscopy (cryo-EM) and allied methods that simian tetherin is targeted in a unique way by the induced refolding of the b subunit of AP-2 from an a-helix to a b-hairpin, creating a binding site for the (G/D)DIWK motif in a crevice between the new b-hairpin and Nef","type":"Abstract"},{"text":"However, when bound to both tetherin and Nef, b2 (peptide 7–18) underwent 40% less HD exchange (30 s) (Figures 4C and S4A). Slower deuteration was also seen in a and s2 residues in SIVsmm Nef binding regions (Figures S4B and S4C), as expected. The finding that protection from amide HD exchange in the b2 N terminus depends on the presence of both SIVsmm Nef and tetherin strongly supports the conclusions drawn from the cryo-EM structure, which shows that the presence of these two molecules together is required for refolding of this region","type":"Results"},{"text":"We used fluorescence polarization (FP) to determine that Alexa488-tetherin tail bound to AP2DmC and SIVsmm Nef with Kd = 2.7 mM ± 0.1 mM (Figures 1C and 1D), while binding to the separate components or to AP2hemi was undetectable. These data indicate that simian tetherin binds to the AP-2 core and SIVsmm Nef in a cooperative and high-affinity ternary complex that requires elements of the full AP-2 tetramer","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"experimental evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"31447307","version":3,"reference_html":"Structural Basis for Tetherin Antagonism as a Barrier to Zoonotic Lentiviral Transmission. <i> Buffalo CZ, Stürzel CM, Heusinger E, Kmiec D, Kirchhoff F, Hurley JH, Ren X. </i> Cell Host Microbe, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000269","term_name":"molecular function regulator","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":18,"region_id":"DP02887r006","start":7,"term_id":"GO:0098772","statement":[{"text":"We show by cryoelectron microscopy (cryo-EM) and allied methods that simian tetherin is targeted in a unique way by the induced refolding of the b subunit of AP-2 from an a-helix to a b-hairpin, creating a binding site for the (G/D)DIWK motif in a crevice between the new b-hairpin and Nef","type":"Abstract"},{"text":"However, when bound to both tetherin and Nef, b2 (peptide 7–18) underwent 40% less HD exchange (30 s) (Figures 4C and S4A). Slower deuteration was also seen in a and s2 residues in SIVsmm Nef binding regions (Figures S4B and S4C), as expected. The finding that protection from amide HD exchange in the b2 N terminus depends on the presence of both SIVsmm Nef and tetherin strongly supports the conclusions drawn from the cryo-EM structure, which shows that the presence of these two molecules together is required for refolding of this region","type":"Results"},{"text":"We used fluorescence polarization (FP) to determine that Alexa488-tetherin tail bound to AP2DmC and SIVsmm Nef with Kd = 2.7 mM ± 0.1 mM (Figures 1C and 1D), while binding to the separate components or to AP2hemi was undetectable. These data indicate that simian tetherin binds to the AP-2 core and SIVsmm Nef in a cooperative and high-affinity ternary complex that requires elements of the full AP-2 tetramer","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"cryogenic electron microscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"31447307","version":3,"reference_html":"Structural Basis for Tetherin Antagonism as a Barrier to Zoonotic Lentiviral Transmission. <i> Buffalo CZ, Stürzel CM, Heusinger E, Kmiec D, Kirchhoff F, Hurley JH, Ren X. </i> Cell Host Microbe, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","cross_refs":[{"db":"PDB","id":"6OWT"}],"term_name":"molecular function regulator","curator_orcid":"0000-0003-0192-9906","ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":18,"region_id":"DP02887r007","start":7,"term_id":"GO:0005515","statement":[{"text":"We show by cryoelectron microscopy (cryo-EM) and allied methods that simian tetherin is targeted in a unique way by the induced refolding of the b subunit of AP-2 from an a-helix to a b-hairpin, creating a binding site for the (G/D)DIWK motif in a crevice between the new b-hairpin and Nef","type":"Abstract"},{"text":"However, when bound to both tetherin and Nef, b2 (peptide 7–18) underwent 40% less HD exchange (30 s) (Figures 4C and S4A). Slower deuteration was also seen in a and s2 residues in SIVsmm Nef binding regions (Figures S4B and S4C), as expected. The finding that protection from amide HD exchange in the b2 N terminus depends on the presence of both SIVsmm Nef and tetherin strongly supports the conclusions drawn from the cryo-EM structure, which shows that the presence of these two molecules together is required for refolding of this region","type":"Results"},{"text":"We used fluorescence polarization (FP) to determine that Alexa488-tetherin tail bound to AP2DmC and SIVsmm Nef with Kd = 2.7 mM ± 0.1 mM (Figures 1C and 1D), while binding to the separate components or to AP2hemi was undetectable. These data indicate that simian tetherin binds to the AP-2 core and SIVsmm Nef in a cooperative and high-affinity ternary complex that requires elements of the full AP-2 tetramer","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"cryogenic electron microscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"31447307","version":3,"reference_html":"Structural Basis for Tetherin Antagonism as a Barrier to Zoonotic Lentiviral Transmission. <i> Buffalo CZ, Stürzel CM, Heusinger E, Kmiec D, Kirchhoff F, Hurley JH, Ren X. </i> Cell Host Microbe, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","cross_refs":[{"db":"PDB","id":"6OWT"}],"term_name":"protein binding","curator_orcid":"0000-0003-0192-9906","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":10116,"disprot_id":"DP02887","date":"2020-05-29T04:12:59.257Z","organism":"Rattus norvegicus","regions_counter":7,"name":"AP-2 complex subunit beta","dataset":[],"UniParc":"UPI0000125012","uniref100":"UniRef100_P63010","uniref90":"UniRef90_P63010","uniref50":"UniRef50_P63010","genes":[{"name":{"value":"Ap2b1"},"synonyms":[{"value":"Clapb1"}]}],"alphafold_very_low_content":0.12593383137673425,"disorder_content":0.012806830309498399,"disprot_consensus":{"full":[{"start":7,"end":18,"type":"T"}],"Structural state":[{"start":7,"end":18,"type":"D"}],"Structural transition":[{"start":7,"end":18,"type":"T"}],"Molecular function":[{"start":7,"end":18,"type":"F"}]}},{"acc":"Q70627","features":{"gene3D":[{"start":2,"end":57,"id":"G3DSA:4.10.890.10","name":"HIV 1 nef anchor domain"},{"start":56,"end":206,"id":"G3DSA:3.30.62.10","name":"Nef Regulatory Factor"}],"pfam":[{"id":"PF00469","name":"Negative factor, (F-Protein) or Nef","start":2,"end":205}]},"creator":"lchemes","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"sequence":"MGGKWSKSSVIGWPTVRERMRRAEPAADGVGAASQDLEKHGAITSSNTAATNADCAWLEAQEEEEVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGIRYPLTFGWCYKLVPVEPEKLEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC","length":206,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":71,"region_id":"DP02888r001","start":60,"term_id":"IDPO:0000002","statement":[{"text":"Significant internal motions on the ps to ns time scale are detected for residues 60 to 71 and for residues 149 to 180, which form solvent-exposed loops.","type":"Abstract"}],"curator_id":"vnugnes","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"9194185","version":3,"reference_html":"Refined solution structure and backbone dynamics of HIV-1 Nef. <i> Grzesiek S, Bax A, Hu JS, Kaufman J, Palmer I, Stahl SJ, Tjandra N, Wingfield PT. </i> Protein Sci, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"2NEF"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T11:29:45.904Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":180,"region_id":"DP02888r002","start":149,"term_id":"IDPO:0000002","statement":[{"text":"Significant internal motions on the ps to ns time scale are detected for residues 60 to 71 and for residues 149 to 180, which form solvent-exposed loops.","type":"Abstract"}],"curator_id":"vnugnes","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"9194185","version":3,"reference_html":"Refined solution structure and backbone dynamics of HIV-1 Nef. <i> Grzesiek S, Bax A, Hu JS, Kaufman J, Palmer I, Stahl SJ, Tjandra N, Wingfield PT. </i> Protein Sci, 1997","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"2NEF"}],"term_name":"disorder","curator_orcid":"0000-0001-8399-7907","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T11:29:44.810Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":82834,"disprot_id":"DP02888","date":"2020-05-29T04:49:07.876Z","organism":"Human immunodeficiency virus type 1 group M subtype B (isolate LW123)","regions_counter":2,"name":"Protein Nef","dataset":["Viral proteins"],"UniParc":"UPI000012FF02","uniref100":"UniRef100_Q70627","uniref90":"UniRef90_Q70627","uniref50":"UniRef50_P03406","genes":[{"name":{"value":"nef","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04078","url":"https://hamap.expasy.org/unirule/MF_04078"}}]}}],"disorder_content":0.21359223300970873,"disprot_consensus":{"full":[{"start":60,"end":71,"type":"D"},{"start":149,"end":180,"type":"D"}],"Structural state":[{"start":60,"end":71,"type":"D"},{"start":149,"end":180,"type":"D"}]}},{"acc":"P03407","sequence":"MGGKWSKRSMGGWSAIRERMRRAEPRAEPAADGVGAVSRDLEKHGAITSSNTAATNADCAWLEAQEEEEVGFPVRPQVPLRPMTYKAALDISHFLKEKGGLEGLIWSQRRQEILDLWIYHTQGYFPDWQNYTPGPGIRYPLTFGWCFKLVPVEPEKVEEANEGENNSLLHPMSLHGMEDAEKEVLVWRFDSKLAFHHMARELHPEYYKDC","creator":"jbergier","dataset":["Viral proteins"],"date":"2020-05-29T05:04:38.276Z","disprot_id":"DP02889","features":{"gene3D":[{"start":2,"end":61,"id":"G3DSA:4.10.890.10","name":"HIV 1 nef anchor domain","_id":"685af523b4ac24d5329d9604"},{"start":60,"end":210,"id":"G3DSA:3.30.62.10","name":"Nef Regulatory Factor","_id":"685af523b4ac24d5329d9605"}],"pfam":[{"id":"PF00469","name":"Negative factor, (F-Protein) or Nef","start":2,"end":209}]},"genes":[{"name":{"value":"nef","evidences":[{"source":{"id":"MF_04078","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04078","_id":"685af523b4ac24d5329d963d"},"code":"ECO:0000255","_id":"685af523b4ac24d5329d963c"}],"_id":"685af523b4ac24d5329d963e"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d963b"}],"length":210,"name":"Protein Nef","ncbi_taxon_id":11685,"organism":"Human immunodeficiency virus type 1 group M subtype B (isolate ARV2/SF2)","regions_counter":12,"released":"2021_06","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"UniParc":"UPI000012FEFA","uniref100":"UniRef100_P03407","uniref50":"UniRef50_P03407","uniref90":"UniRef90_P03407","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3REB","_id":"685af523b4ac24d5329d9613"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":155,"end":179,"interaction_partner":[],"reference_html":"Molecular design, functional characterization and structural basis of a protein inhibitor against the HIV-1 pathogenicity factor Nef. <i> Breuer S, Schievink SI, Schulte A, Blankenfeldt W, Fackler OT, Geyer M. </i> PLoS One, 2011","reference_id":"21625496","region_id":"DP02889r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The C-terminal flexible loop of Nef that contained the endocytic dileucine motif was partly truncated in the crystallized complex, nonetheless no electron density was observed starting from residues 155 to 179, in line with the assumption of a flexible loop section (Figure 5A).","_id":"685af523b4ac24d5329d9612"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-04T12:58:23.498Z","_id":"685af523b4ac24d5329d9614"},"version":3,"_id":"685af523b4ac24d5329d9611","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"4U5W","_id":"685af523b4ac24d5329d9617"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":155,"end":181,"interaction_partner":[],"reference_html":"Interaction with the Src homology (SH3-SH2) region of the Src-family kinase Hck structures the HIV-1 Nef dimer for kinase activation and effector recruitment. <i> Alvarado JJ, Tarafdar S, Yeh JI, Smithgall TE. </i> J Biol Chem, 2014","reference_id":"25122770","region_id":"DP02889r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Models of x-ray structures and electron density were produced using PyMOL (Schrodinger). The final structure includes Nef-SF2core residues 72–161 and 183–208 for chain A, residues 71–154 and 182–208 for chain C, Hck32 residues 83–246 for chain B, and residues 83–176 and 182–246 for chain D.","_id":"685af523b4ac24d5329d9616"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-04T13:19:15.055Z","_id":"685af523b4ac24d5329d9618"},"version":3,"_id":"685af523b4ac24d5329d9615","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3RBB","_id":"685af523b4ac24d5329d9624"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":157,"end":179,"interaction_partner":[],"reference_html":"Conformation of the dileucine-based sorting motif in HIV-1 Nef revealed by intermolecular domain assembly. <i> Horenkamp FA, Breuer S, Schulte A, Lülf S, Weyand M, Saksela K, Geyer M. </i> Traffic, 2011","reference_id":"21477083","region_id":"DP02889r007","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"In this study we determined a structural conformation of the dileucine-based sorting motif in the C-terminal flexible loop of Nef.","_id":"685af523b4ac24d5329d9623"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-04T13:18:55.047Z","_id":"685af523b4ac24d5329d9625"},"version":3,"_id":"685af523b4ac24d5329d9622","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3RBB","_id":"685af523b4ac24d5329d9628"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":157,"end":179,"interaction_partner":[],"reference_html":"Conformation of the dileucine-based sorting motif in HIV-1 Nef revealed by intermolecular domain assembly. <i> Horenkamp FA, Breuer S, Schulte A, Lülf S, Weyand M, Saksela K, Geyer M. </i> Traffic, 2011","reference_id":"21477083","region_id":"DP02889r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In the crystal structure, two Nef–HckSH3-B6 complexes form symmetrical contacts by mutual interactions of the 33 residues encompassing C-terminal flexible loop with the core domain structure of the opposing Nef molecule (Figure 3A). These contacts are mediated by residues V152-P154, followed by E164, N165 and S167-D179 as well as V184 of the loop region. They interact with residues in the range of F94 to T121 of the Nef core domain, completed by V70-R75 of the PxxP loop and V186 of the terminal β-strand β5.","_id":"685af523b4ac24d5329d9627"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-04T13:18:53.733Z","_id":"685af523b4ac24d5329d9629"},"version":4,"_id":"685af523b4ac24d5329d9626","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3RBB","_id":"685af523b4ac24d5329d962c"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":157,"end":179,"interaction_partner":[],"reference_html":"Conformation of the dileucine-based sorting motif in HIV-1 Nef revealed by intermolecular domain assembly. <i> Horenkamp FA, Breuer S, Schulte A, Lülf S, Weyand M, Saksela K, Geyer M. </i> Traffic, 2011","reference_id":"21477083","region_id":"DP02889r009","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"In this study we determined a structural conformation of the dileucine-based sorting motif in the C-terminal flexible loop of Nef. The Nef protein of primate lentiviruses HIV and SIV is the only non-transmembrane protein known to traffic via a dileucine motif 36. This endocytic sorting signal is required for the stimulated internalization of T-cell receptor molecules from the surface of an infected cell by Nef and a key factor for the pathogenicity of HIV.","_id":"685af523b4ac24d5329d962b"}],"states_connection":[],"term_comment":"","term_def":"\"Any endocytosis that is involved in the uptake of a virus into a host cell.\" [GOC:bf, GOC:jl, VZ:977]","term_id":"GO:0075509","term_is_binding":false,"term_is_obsolete":false,"term_name":"endocytosis involved in viral entry into host cell","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-04T13:18:50.787Z","_id":"685af523b4ac24d5329d962d"},"version":4,"_id":"685af523b4ac24d5329d962a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3RBB","_id":"685af523b4ac24d5329d9634"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0001171","ec_name":"crystallography evidence used in manual assertion","ec_ontology":"ECO","start":157,"end":179,"interaction_partner":[],"reference_html":"Conformation of the dileucine-based sorting motif in HIV-1 Nef revealed by intermolecular domain assembly. <i> Horenkamp FA, Breuer S, Schulte A, Lülf S, Weyand M, Saksela K, Geyer M. </i> Traffic, 2011","reference_id":"21477083","region_id":"DP02889r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In the crystal structure, two Nef–HckSH3-B6 complexes form symmetrical contacts by mutual interactions of the 33 residues encompassing C-terminal flexible loop with the core domain structure of the opposing Nef molecule (Figure 3A). These contacts are mediated by residues V152-P154, followed by E164, N165 and S167-D179 as well as V184 of the loop region. They interact with residues in the range of F94 to T121 of the Nef core domain, completed by V70-R75 of the PxxP loop and V186 of the terminal β-strand β5.","_id":"685af523b4ac24d5329d9633"}],"states_connection":[],"term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-04T13:18:51.853Z","_id":"685af523b4ac24d5329d9635"},"version":1,"_id":"685af523b4ac24d5329d9632","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6B72","_id":"685af523b4ac24d5329d9637"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":154,"end":180,"interaction_partner":[],"reference_html":"A single β-octyl glucoside molecule induces HIV-1 Nef dimer formation in the absence of partner protein binding. <i> Wu M, Alvarado JJ, Augelli-Szafran CE, Ptak RG, Smithgall TE. </i> PLoS One, 2018","reference_id":"29415006","region_id":"DP02889r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Electron density for the flexible central loop (150–176) was not observed, consistent with the disordered nature of this region in the absence of a binding partner.","_id":"685af523b4ac24d5329d9638"},{"type":"Curator statement","text":"The flexible central loop corresponds to 154-180 region of the Nef protein according to the PDB.","_id":"685af523b4ac24d5329d9639"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-04T13:19:24.473Z","_id":"685af523b4ac24d5329d963a"},"version":1,"_id":"685af523b4ac24d5329d9636","reference_source":"pmid"}],"__v":0,"disorder_content":0.13333333333333333,"disprot_consensus":{"full":[{"start":154,"end":156,"type":"D"},{"start":157,"end":179,"type":"T"},{"start":180,"end":181,"type":"D"}],"Structural state":[{"start":154,"end":181,"type":"D"}],"Structural transition":[{"start":157,"end":179,"type":"T"}],"Molecular function":[{"start":157,"end":179,"type":"F"}],"Biological process":[{"start":157,"end":179,"type":"F"}],"Disorder function":[{"start":157,"end":179,"type":"F"}]}},{"acc":"Q7K5N4","features":{"gene3D":[{"start":36,"end":279,"id":"G3DSA:3.40.532.10","name":"Peptidase C12, ubiquitin carboxyl-terminal hydrolase"}],"pfam":[{"id":"PF01088","name":"Ubiquitin carboxyl-terminal hydrolase, family 1","start":46,"end":258},{"id":"PF18031","name":"Ubiquitin carboxyl-terminal hydrolases","start":348,"end":393}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"sequence":"MNAAGGGSGAQAAAVAAGNNSLSHNALLSTASGATTMPMAQLADGWLELESDPGLFTLLLKDFGCHDVQVEEVYDLQKPIESPYGFIFLFRWIEERRARRKIVETTAEIFVKDEEAISSIFFAQQVVPNSCATHALLSVLLNCNENNLQLGDTLSRLKTHTKGMSPENKGLAIGNTPELACAHNSHAMPQARRRLERTGAGVSSCRFTGEAFHFVSFVPINGQLFELDGLKPYPMNHGGWEDSEDWTDKFRRVMAERLGIATGEQDIRFNLMAVVPDRRIAITHKLKMLRTNQAIVSGTLQKLLKADEQGESGNGDSQRPDTPTTLLEPSAFTARDLQSLLKNLDTEIAINEQHLADENDRRHMFKVDASRRTHNYDKFICTFLSMLAHQGVLGELVSQHLLPSKKVSGQGAANRISKQSTTASAGGSTAAGTASTPKTQQQQAAAAKNGKSPSKTPGRRRKGRNKCRKRK","length":471,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":210,"region_id":"DP02890r001","start":195,"term_id":"IDPO:0000002","statement":[{"text":"Disordered region inside the crossover-loop of Calypso.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30258054","version":2,"reference_html":"A bidentate Polycomb Repressive-Deubiquitinase complex is required for efficient activity on nucleosomes. <i> Foglizzo M, Middleton AJ, Burgess AE, Crowther JM, Dobson RCJ, Murphy JM, Day CL, Mace PD. </i> Nat Commun, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6CGA"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":334,"region_id":"DP02890r002","start":304,"term_id":"IDPO:0000002","statement":[{"text":"Disordered region corresponding to an insertion of 41 aa in the ULD domain of Calypso.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30258054","version":2,"reference_html":"A bidentate Polycomb Repressive-Deubiquitinase complex is required for efficient activity on nucleosomes. <i> Foglizzo M, Middleton AJ, Burgess AE, Crowther JM, Dobson RCJ, Murphy JM, Day CL, Mace PD. </i> Nat Commun, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6CGA"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":7227,"disprot_id":"DP02890","date":"2020-05-29T11:00:18.181Z","organism":"Drosophila melanogaster","regions_counter":2,"name":"Ubiquitin carboxyl-terminal hydrolase calypso","dataset":[],"UniParc":"UPI00000820FC","uniref100":"UniRef100_Q7K5N4","uniref90":"UniRef90_Q7K5N4","uniref50":"UniRef50_Q7K5N4","genes":[{"name":{"value":"calypso"},"orfNames":[{"value":"CG8445"}]}],"alphafold_very_low_content":0.27388535031847133,"disorder_content":0.09978768577494693,"disprot_consensus":{"full":[{"start":195,"end":210,"type":"D"},{"start":304,"end":334,"type":"D"}],"Structural state":[{"start":195,"end":210,"type":"D"},{"start":304,"end":334,"type":"D"}]}},{"acc":"Q9V727","features":{"gene3D":[],"pfam":[{"id":"PF13919","name":"Asx homology domain","start":198,"end":335},{"id":"PF13922","name":"PHD domain of transcriptional enhancer, Asx","start":1602,"end":1668}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"sequence":"MKTITPDTTTTTSSQHQQLLIPQADQHHQPMLQQQSLLAAPPPTMIMEHVNLVDDDEKDPLALEQLEVSPSTKHTHSLRRHLPRIIVKPIPPEKKPMAPSEEAAVSTAPAPPTRLICSRRIQQQQQVKAAAAAAAAAAAAAAAAAAAAQAQATSSYPSAISPGSKAGTSQASTMREVLASIPGFSVKPRRRSNKKLTTAAQIEQTKDGKIDLETPDSILASTNLRALLNKQTFSLLPPLYQYNLIQLLPSVDREASELEQPSSSASGGSPSEAIRLSASCLNNEFFARACLEWRERLSEGEFTPENQLKLKTEAEREKNKLDPWKLKHFEPFWGEKNSRGKDKDKLESDCKNQKLSASIKSEPKPPATSQQKPLQQATCDNETELKFDLSTKCETTSAKTTVAVAVADKSSTFPPTGSQNNVLNEQQRRVLKRPSSSPSQRKQAPTTIATINLDDDLDELPSTSKDSKQPKMDEIVPNASGNVVAAPMVDVVDHSAVEMKIKDEQQHQRQHQPLINSTCDKIEPSECSKEMIVAMKQVDSKEDVDSIASAAAMPAIAAVTPHTPKPEALAPNPDVANQFVSYLQNVELAAETKAPLDNSNEADITTGTNSHDFVFSDTIDHAYFQEHQSTINHNFFTSSSSSNTATTAANKLEEHSDKPEDSPLPIASSISGSTPASSITSTSCTSSSSSSASMSSSCSSSNSGSTTTAPTTSSSAGAPTAPLTLAAAAETTLANVQAMLSTVAKLQQQQQELPVELNSNEMYQHVQHDWNFGDIKLSSSQSSGDQQRNLSHEAIDLMDVVQDADVIDDIMHNDVCHDVLGDEDEGDQEEDEDDEVVECMTEEQQLIDEDSEAVREIVDKLQQHQQQQNQQQHHQQLHIQDVVQLAQHSFMPQAHSEFGNDIGQEMLCDAVPMSAAEMEVSSTVITNSSNSNDSSNNISLCSSTNSLTINQMPHQASQQPQQNAQSNAQQQRQILVDSNGQIIGNFLLQQQRQQQQQQLLQQFTLQAAAAQQQQQQQQQHQQQQQQQQQATSSNSLGKTLPVALRNGTQQFLSPNLIAQQHQQQQQQQLEQHQQQATAQQKHQQIQQFALQQAQLHQRQLLAQAANNNLLQQQQQQQQNVALPTTQAKFIAKPLNIISMTRPANASPTTAATTANTASIPSAYANVVAVTGAQQQQSPPVPAPQQQTVQQQQLANHNSNMQQLPNVLTMKTLPPSGVPTTIAQQRLQPKMPTGKGRKATSNRLPPGAVNLERSYQICQAVIQNSPNRENLKAQLRPPAAILNQHQPTTTTAPAPINPVTLNVSTVAATPMSNITTATGSMAAAVAAAPPQNVLKQEELLVSGAVGAGALPAGLPPNVMGVGRPGVYKVIGPRMSGFPRKKYVQRKPSPTTLIRHVFSPGPGGATATAQQLQMLQQHHQSTTSPVPVQNPQQPAPEQLIHQNGNGQYVLVHRANVGAADNQAPRASSAPPMHQNQFVTVQNPLHSINGIPMGGRGRPASVDTTAGSGNVIAPPISATDALHHHHHEMQQQQQHQQPQPLGNVGAAANIVRRNIAAGPNIAYIDGSNTNSSAVALMEAGNNYIVTTNASPTAAPSPINQQPQSQPTGTQHQHPLLQLHQTGENTPPGNEATATANNCACSLNAMVICQQCGAFCHDDCIGAAKLCVACVIR","length":1669,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":340,"region_id":"DP02891r001","start":310,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"It is possible that in situ proteolysis used during crystal growth may have removed residues 310–340 of the ASX Deubad, or that the remaining residues of the ASX Deubad adopt alternate conformations in the crystal. Either scenario would suggest a degree of conformational flexibility in the C-terminal region of ASX Deubad.","type":"Results"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30258054","version":2,"reference_html":"A bidentate Polycomb Repressive-Deubiquitinase complex is required for efficient activity on nucleosomes. <i> Foglizzo M, Middleton AJ, Burgess AE, Crowther JM, Dobson RCJ, Murphy JM, Day CL, Mace PD. </i> Nat Commun, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6CGA"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-02T19:31:55.591Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":273,"region_id":"DP02891r002","start":254,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Flexible region inside the ASX Deubad domain, invisible in the crystal structure.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"30258054","version":2,"reference_html":"A bidentate Polycomb Repressive-Deubiquitinase complex is required for efficient activity on nucleosomes. <i> Foglizzo M, Middleton AJ, Burgess AE, Crowther JM, Dobson RCJ, Murphy JM, Day CL, Mace PD. </i> Nat Commun, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"6CGA"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-02T19:31:40.513Z"}}],"released":"2023_12","ncbi_taxon_id":7227,"disprot_id":"DP02891","date":"2020-05-29T11:06:02.628Z","organism":"Drosophila melanogaster","regions_counter":2,"name":"Polycomb protein Asx","dataset":[],"UniParc":"UPI000007D103","uniref100":"UniRef100_Q9V727","uniref90":"UniRef90_Q9V727","uniref50":"UniRef50_Q9V727","genes":[{"name":{"value":"Asx"},"orfNames":[{"value":"CG8787"}]}],"alphafold_very_low_content":0.7579388855602157,"disorder_content":0.03055721989215099,"disprot_consensus":{"full":[{"start":254,"end":273,"type":"D"},{"start":310,"end":340,"type":"D"}],"Structural state":[{"start":254,"end":273,"type":"D"},{"start":310,"end":340,"type":"D"}]}},{"acc":"Q3UND0","features":{"gene3D":[{"start":111,"end":218,"id":"G3DSA:2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"}],"pfam":[{"id":"PF00018","name":"SH3 domain","start":312,"end":349},{"id":"PF00169","name":"PH domain","start":117,"end":216}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MPNPSCTSSPGPLPEEIRNLLADVETFVADTLKGENLSKKAKEKRESLIKKIKDVKSVYLQEFQDKGDAEDGDEYDDPFAGPADTISLASERYDKDDDGPSDGNQFPPIAAQDLPFVIKAGYLEKRRKDHSFLGFEWQKRWCALSKTVFYYYGSDKDKQQKGEFAIDGYDVRMNNTLRKDGKKDCCFEICAPDKRIYQFTAASPKDAEEWVQQLKFILQDLGSDVIPEDDEERGELYDDVDHPAAVSSPQRSQPIDDEIYEELPEEEEDTASVKMDEQGKGSRDSVHHTSGDKSTDYANFYQGLWDCTGALSDELSFKRGDVIYILSKEYNRYGWWVGEMKGAIGLVPKAYLMEMYDI","length":358,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":105,"region_id":"DP02892r001","start":65,"term_id":"IDPO:0000002","statement":[{"text":"The linker region between the DM and PH domains (residues 65–109) is disordered.","type":"Results"},{"text":"Flexible linker connecting the homodimerization (DM) and PH domain of Skap2.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19026786","version":2,"reference_html":"The Skap-hom dimerization and PH domains comprise a 3'-phosphoinositide-gated molecular switch. <i> Swanson KD, Tang Y, Ceccarelli DF, Poy F, Sliwa JP, Neel BG, Eck MJ. </i> Mol Cell, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2OTX"}],"term_name":"disorder","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:41:47.482Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":105,"region_id":"DP02892r002","start":65,"term_id":"IDPO:0000033","statement":[{"text":"The linker region between the DM and PH domains (residues 65–109) is disordered.","type":"Results"},{"text":"Flexible linker connecting the homodimerization (DM) and PH domain of Skap2.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19026786","version":3,"reference_html":"The Skap-hom dimerization and PH domains comprise a 3'-phosphoinositide-gated molecular switch. <i> Swanson KD, Tang Y, Ceccarelli DF, Poy F, Sliwa JP, Neel BG, Eck MJ. </i> Mol Cell, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"2OTX"}],"term_name":"flexible linker","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:41:48.208Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2020_12","ncbi_taxon_id":10090,"disprot_id":"DP02892","date":"2020-05-29T11:27:08.869Z","organism":"Mus musculus","regions_counter":2,"name":"Src kinase-associated phosphoprotein 2","dataset":[],"UniParc":"UPI00005AC2C6","uniref100":"UniRef100_Q3UND0","uniref90":"UniRef90_Q3UND0","uniref50":"UniRef50_Q3UND0","genes":[{"name":{"value":"Skap2"},"synonyms":[{"value":"Prap"},{"value":"Ra70"},{"value":"Saps"},{"value":"Scap2"},{"value":"Skap55r"}]}],"alphafold_very_low_content":0.2430167597765363,"disorder_content":0.11452513966480447,"disprot_consensus":{"full":[{"start":65,"end":105,"type":"D"}],"Structural state":[{"start":65,"end":105,"type":"D"}],"Disorder function":[{"start":65,"end":105,"type":"F"}]}},{"acc":"Q9BZZ5-2","features":{"pfam":[]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MPTVEELYRNYGILADATEQVGQHKDAYQVILDGVKGGTKEKRLAAQFIPKFFKHFPELADSAINAQLDLCEDEDVSIRRQAIKELPQFATGENLPRVADILTQLLQTDDSAEFNLVNNALLSIFKMDAKGTLGGLFSQILQGEDIVRERAIKFLSTKLKTLPDEVLTKEVEELILTESKKVLEDVTGEEFVLFMKILSGLKSLQTVSGRQQLVELVAEQADLEQTFNPSDPDCVDRLLQCTRQAVPLFSKNVHSTRFVTYFCEQVLPNLGTLTTPVEGLDIQLEVLKLLAEMSSFCGDMEKLETNLRKLFDKLLEYMPLPPEEAENGENAGNEEPKLQFSYVECLLYSFHQLGRKLPDFLTAKLNAEKLKDFKIRLQYFARGLQVYIRQLRLALQGKTGEALKTEENKIKVVALKITNNINVLIKDLFHIPPSYKSTVTLSWKPVQKVEIGQKRASEDTTSGSPPKKSSAGPKRDARQIYNPPSGKYSSNLGNFNYERSLQGK","length":504,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":335,"region_id":"DP02894r001","start":322,"term_id":"IDPO:0000002","statement":[{"text":"Residues 277–278, 322–335, 365–366, 430–431, and 447–454, as well as the four extra N-terminal residues (Gly-Ser-His-Met), artificially added by cloning into pET-28b, were disordered in the crystal.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22334682","version":2,"reference_html":"Helical repeat structure of apoptosis inhibitor 5 reveals protein-protein interaction modules. <i> Han BG, Kim KH, Lee SJ, Jeong KC, Cho JW, Noh KH, Kim TW, Kim SJ, Yoon HJ, Suh SW, Lee S, Lee BI. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3U0R"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":504,"region_id":"DP02894r002","start":455,"term_id":"IDPO:0000002","statement":[{"text":"The C-terminal region of API5 (residues 455–504), which contains a nuclear localization signal (Fig. 2) between residues 454–475 and is predicted to be disordered by IUPRED (33), was readily removed by trypsin.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22334682","version":2,"reference_html":"Helical repeat structure of apoptosis inhibitor 5 reveals protein-protein interaction modules. <i> Han BG, Kim KH, Lee SJ, Jeong KC, Cho JW, Noh KH, Kim TW, Kim SJ, Yoon HJ, Suh SW, Lee S, Lee BI. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3U0R"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":504,"region_id":"DP02894r003","start":455,"term_id":"IDPO:0000002","statement":[{"text":"The C-terminal region of API5 (residues 455–504), which contains a nuclear localization signal (Fig. 2) between residues 454–475 and is predicted to be disordered by IUPRED (33), was readily removed by trypsin.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22334682","version":2,"reference_html":"Helical repeat structure of apoptosis inhibitor 5 reveals protein-protein interaction modules. <i> Han BG, Kim KH, Lee SJ, Jeong KC, Cho JW, Noh KH, Kim TW, Kim SJ, Yoon HJ, Suh SW, Lee S, Lee BI. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","cross_refs":[{"db":"PDB","id":"3U0R"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Biological process","ec_ontology":"ECO","end":475,"region_id":"DP02894r004","start":455,"term_id":"GO:0051179","statement":[{"text":"The C-terminal region of API5 (residues 455–504), which contains a nuclear localization signal (Fig. 2) between residues 454–475 and is predicted to be disordered by IUPRED (33), was readily removed by trypsin.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"22334682","version":3,"reference_html":"Helical repeat structure of apoptosis inhibitor 5 reveals protein-protein interaction modules. <i> Han BG, Kim KH, Lee SJ, Jeong KC, Cho JW, Noh KH, Kim TW, Kim SJ, Yoon HJ, Suh SW, Lee S, Lee BI. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"3U0R"}],"term_name":"localization","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02894","date":"2020-05-29T12:31:03.101Z","organism":"Homo sapiens","regions_counter":4,"name":"Isoform 2 of Apoptosis inhibitor 5","dataset":[],"UniParc":"UPI000007086D","uniref100":"","uniref90":"","uniref50":"","genes":[{"name":{"value":"API5","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:594","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:594"}}]},"orfNames":[{"value":"MIG8"}]}],"disorder_content":0.12698412698412698,"disprot_consensus":{"full":[{"start":322,"end":335,"type":"D"},{"start":455,"end":504,"type":"D"}],"Structural state":[{"start":322,"end":335,"type":"D"},{"start":455,"end":504,"type":"D"}],"Biological process":[{"start":455,"end":475,"type":"F"}]}},{"acc":"Q96E14","features":{"gene3D":[],"pfam":[{"id":"PF16100","name":"RecQ-mediated genome instability protein 2","start":21,"end":143}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MAAAADSFSGGPAGVRLPRSPPLKVLAEQLRRDAEGGPGAWRLSRAAAGRGPLDLAAVWMQGRVVMADRGEARLRDPSGDFSVRGLERVPRGRPCLVPGKYVMVMGVVQACSPEPCLQAVKMTDLSDNPIHESMWELEVEDLHRNIP","length":147,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":16,"region_id":"DP02895r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"Electron density defining the N-terminus of RMI2 was missing, which could indicate that this region of the domain is structurally dynamic.","type":"Results"}],"curator_id":"fquaglia","released":"2022_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20826341","version":3,"reference_html":"Structure and cellular roles of the RMI core complex from the bloom syndrome dissolvasome. <i> Hoadley KA, Xu D, Xue Y, Satyshur KA, Wang W, Keck JL. </i> Structure, 2010","date":"2022-06-25T20:40:18.959Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3MXN"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9H9A7"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T12:46:07.913Z"}}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02895","date":"2020-05-29T12:38:54.042Z","organism":"Homo sapiens","regions_counter":1,"name":"RecQ-mediated genome instability protein 2","dataset":["Cancer-related proteins"],"UniParc":"UPI000006EA0A","uniref100":"UniRef100_Q96E14","uniref90":"UniRef90_Q96E14","uniref50":"UniRef50_Q96E14","genes":[{"name":{"value":"RMI2"},"synonyms":[{"value":"C16orf75"}]}],"alphafold_very_low_content":0.08843537414965986,"disorder_content":0.10884353741496598,"disprot_consensus":{"full":[{"start":1,"end":16,"type":"D"}],"Structural state":[{"start":1,"end":16,"type":"D"}]}},{"acc":"Q91VS8","features":{"gene3D":[{"start":929,"end":1032,"id":"G3DSA:2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":929,"end":1032,"id":"G3DSA:2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":929,"end":1032,"id":"G3DSA:2.30.29.30","name":"Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)"},{"start":125,"end":228,"id":"G3DSA:1.20.80.10","name":"G3DSA:1.20.80.10"},{"start":533,"end":749,"id":"G3DSA:1.20.900.10","name":"Dbl homology (DH) domain"}],"pfam":[{"id":"PF00169","name":"PH domain","start":760,"end":854},{"id":"PF00169","name":"PH domain","start":933,"end":1026},{"id":"PF00373","name":"FERM central domain","start":127,"end":234},{"id":"PF00621","name":"RhoGEF domain","start":542,"end":726},{"id":"PF08736","name":"FERM adjacent (FA)","start":334,"end":375},{"id":"PF09379","name":"FERM N-terminal domain","start":48,"end":110},{"id":"PF09380","name":"FERM C-terminal PH-like domain","start":238,"end":327}]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MGEIEGTYRALPTSGTRLGGQTAIGVSTLEPEQSLSPRMQEKHMRIRVKLLDSTVELFDIEPKCDGQVLLTQVWKHLNLIECDYFGLEFKNVQSYWIWLEPMKPIIRQVRKPKNAVLRLAVKFFPPDPGQLQEEYTRYLFALQLKRDLLEERLTCTANTAALLISHLLQSEIGDYDETLDREHLKANEYLPNQEKSLEKILDFHQRHTGQTPAESDFQVLEIARKLEMYGIRFHMASDREGTKINLAVSHMGVLVFQGTTKINTFNWSKVRKLSFKRKRFLIKLHPEVHGPYQDTLEFLLGSRDECKNFWKICVEYHTFFRLSDQPKPKAKAVFFSRGSSFRYSGRTQKQLVDYVKDGGMKRIPYERRHSKTRTSLHALTVDLPKQSVSFTDGLRTSASLSSANVSFYPPPSSSLSPPGLPNLKDSSSSLVDPQAPVIKSTAAERSSGPSSSDGPSTQSAHLPGPPVLRPGPGFSMDSPQPSPSSLKSHLSLCPELQAALSTAEQGASPVLSPVLSGAGTARMDNQEEQKHKHMPEDEAYFIAKEILATERTYLKDLEVITVWFRSVLIKEEAMPAALMALLFSNIDPVYEFHRGFLHEVEQRLALWEGPSSAHLKGDHQRIGDILLRNMRQLKEFTSYFQRHDEVLTELEKATKHCKKLEAVYKEFELQKVCYLPLNTFLLKPVQRLVHYRLLLSRLCAHYSPGHRDYADCHEALKAITEVTTELQQSLTRLENLQKLTELQRDLVGVENLIAPGREFIREGCLHKLTKKGLQQRMFFLFSDMLLYTSKSVTGASHFRIRGFLPLRGMLVEESENEWSVPHCFTIYAAQKTIVVAASTRLEKEKWMQDLNAAIQAAKTIGDSPPVLLGGPVYTRTPRSSDEVSLEESEDGRGNRGSLEGNSQHRANTTMHVCWYRNTSVSRADHSAAVENQLSGYLLRKFKNSNGWQKLWVVFTNFCLFFYKTHQDDYPLASLPLLGYSVSLPREADSIHKDYVFKLQFKSHVYFFRAESKYTFERWMDVIKRASSSPGRPPSFTQDCSHHSPGLEAEIREKEACPSPCLDKNL","length":1065,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":906,"region_id":"DP02896r001","start":869,"term_id":"IDPO:0000002","statement":[{"text":"The ~70-residue PH1-PH2 linker is disordered except for the 864–868 and the 907–931 segments.","type":"Results"},{"text":"Flexible linker connecting PH1 and PH2 domain corresponds to region 869-906 of the amino acid sequence.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23375260","version":2,"reference_html":"Structural basis for autoinhibition of the guanine nucleotide exchange factor FARP2. <i> He X, Kuo YC, Rosche TJ, Zhang X. </i> Structure, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4GZU"}],"term_name":"disorder","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:41:35.099Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":906,"region_id":"DP02896r002","start":869,"term_id":"IDPO:0000033","statement":[{"text":"The ~70-residue PH1-PH2 linker is disordered except for the 864–868 and the 907–931 segments.","type":"Results"},{"text":"Flexible linker connecting PH1 and PH2 domain corresponds to region 869-906 of the amino acid sequence.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23375260","version":3,"reference_html":"Structural basis for autoinhibition of the guanine nucleotide exchange factor FARP2. <i> He X, Kuo YC, Rosche TJ, Zhang X. </i> Structure, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4GZU"}],"term_name":"flexible linker","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:41:36.078Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":10090,"disprot_id":"DP02896","date":"2020-05-29T12:45:47.913Z","organism":"Mus musculus","regions_counter":2,"name":"FERM, ARHGEF and pleckstrin domain-containing protein 2","dataset":[],"UniParc":"UPI0000029239","uniref100":"UniRef100_Q91VS8","uniref90":"UniRef90_Q91VS8","uniref50":"UniRef50_Q91VS8","genes":[{"name":{"value":"Farp2"},"synonyms":[{"value":"Kiaa0793"}]}],"alphafold_very_low_content":0.27605633802816903,"disorder_content":0.03568075117370892,"disprot_consensus":{"full":[{"start":869,"end":906,"type":"D"}],"Structural state":[{"start":869,"end":906,"type":"D"}],"Disorder function":[{"start":869,"end":906,"type":"F"}]}},{"acc":"Q90VU7","sequence":"MGGKWSKSSVIGWPAVRERMRRAEPAADGVGAVSRDLEKHGAITSSNTAANNAACAWLEAQEEEEVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGVRYPLTFGWCYKLVPVEPDKVEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC","creator":"jbergier","dataset":["Viral proteins"],"date":"2020-05-30T00:17:04.285Z","disprot_id":"DP02897","features":{"gene3D":[{"start":2,"end":57,"id":"G3DSA:4.10.890.10","name":"HIV 1 nef anchor domain","_id":"685af523b4ac24d5329d963f"},{"start":56,"end":206,"id":"G3DSA:3.30.62.10","name":"Nef Regulatory Factor","_id":"685af523b4ac24d5329d9640"}],"pfam":[{"id":"PF00469","name":"Negative factor, (F-Protein) or Nef","start":2,"end":205}]},"genes":[{"name":{"value":"nef","evidences":[{"source":{"id":"MF_04078","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04078","_id":"685af523b4ac24d5329d9667"},"code":"ECO:0000256","_id":"685af523b4ac24d5329d9666"},{"source":{"id":"AAB60579.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/AAB60579.1","_id":"685af523b4ac24d5329d9669"},"code":"ECO:0000313","_id":"685af523b4ac24d5329d9668"}],"_id":"685af523b4ac24d5329d966a"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d9665"}],"length":206,"name":"Protein Nef","ncbi_taxon_id":11676,"organism":"Human immunodeficiency virus 1","regions_counter":6,"released":"2020_12","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"UniParc":"UPI000010C120","uniref100":"UniRef100_Q90VU7","uniref50":"UniRef50_P03407","uniref90":"UniRef90_Q90VU7","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"4EMZ","_id":"685af523b4ac24d5329d9645"},{"db":"PDB","id":"4EN2","_id":"685af523b4ac24d5329d9646"}],"curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":27,"end":56,"interaction_partner":[],"reference_html":"Structural basis of evasion of cellular adaptive immunity by HIV-1 Nef. <i> Jia X, Singh R, Homann S, Yang H, Guatelli J, Xiong Y. </i> Nat Struct Mol Biol, 2012","reference_id":"22705789","region_id":"DP02897r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Much of the Nef N- and C-terminal loops (residues 27–56 and 162–174, respectively) are disordered and not seen in the structure","_id":"685af523b4ac24d5329d9644"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2020-12-02T14:33:29.369Z","_id":"685af523b4ac24d5329d9643"},"version":2,"_id":"685af523b4ac24d5329d9642","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"4EMZ","_id":"685af523b4ac24d5329d964a"},{"db":"PDB","id":"4EN2","_id":"685af523b4ac24d5329d964b"}],"curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":162,"end":174,"interaction_partner":[],"reference_html":"Structural basis of evasion of cellular adaptive immunity by HIV-1 Nef. <i> Jia X, Singh R, Homann S, Yang H, Guatelli J, Xiong Y. </i> Nat Struct Mol Biol, 2012","reference_id":"22705789","region_id":"DP02897r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Much of the Nef N- and C-terminal loops (residues 27–56 and 162–174, respectively) are disordered and not seen in the structure","_id":"685af523b4ac24d5329d9649"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2020-12-02T14:33:28.170Z","_id":"685af523b4ac24d5329d9648"},"version":2,"_id":"685af523b4ac24d5329d9647","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6D83","_id":"685af523b4ac24d5329d9650"},{"db":"PDB","id":"6CM9","_id":"685af523b4ac24d5329d9651"}],"curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"IDA","ec_id":"ECO:0006208","ec_name":"cryogenic electron microscopy evidence used in manual assertion","ec_ontology":"ECO","start":158,"end":168,"interaction_partner":[],"reference_html":"HIV-1 Nefs Are Cargo-Sensitive AP-1 Trimerization Switches in Tetherin Downregulation. <i> Morris KL, Buffalo CZ, Stürzel CM, Heusinger E, Kirchhoff F, Ren X, Hurley JH. </i> Cell, 2018","reference_id":"30053425","region_id":"DP02897r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The Nef LL motif is well-defined in density and engages the γ-σ1 (Figure 2C) in trans with respect to the μ1 interaction. The Nef sequences 149–157 and 168–179 are disordered over gaps of 22 and 25 Å, respectively between the LL motif and the Nef core","_id":"685af523b4ac24d5329d964e"},{"type":"Figure","text":"Fig 2 legend. (C) The ExxxLL motif of Nef binds to AP-1σ1 (D) These binding regions of Nef are found on the unstructured loops L1 and L4 but are stabilized in the trimeric assembly","_id":"685af523b4ac24d5329d964f"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2020-12-02T14:33:27.468Z","_id":"685af523b4ac24d5329d964d"},"version":2,"_id":"685af523b4ac24d5329d964c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6D83","_id":"685af523b4ac24d5329d9656"},{"db":"PDB","id":"6CM9","_id":"685af523b4ac24d5329d9657"}],"curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006208","ec_name":"cryogenic electron microscopy evidence used in manual assertion","ec_ontology":"ECO","start":160,"end":165,"interaction_partner":[],"reference_html":"HIV-1 Nefs Are Cargo-Sensitive AP-1 Trimerization Switches in Tetherin Downregulation. <i> Morris KL, Buffalo CZ, Stürzel CM, Heusinger E, Kirchhoff F, Ren X, Hurley JH. </i> Cell, 2018","reference_id":"30053425","region_id":"DP02897r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The Nef LL motif is well-defined in density and engages the γ-σ1 (Figure 2C) in trans with respect to the μ1 interaction. The Nef sequences 149–157 and 168–179 are disordered over gaps of 22 and 25 Å, respectively between the LL motif and the Nef core","_id":"685af523b4ac24d5329d9654"},{"type":"Figure","text":"Fig 2 legend. (C) The ExxxLL motif of Nef binds to AP-1σ1 (D) These binding regions of Nef are found on the unstructured loops L1 and L4 but are stabilized in the trimeric assembly","_id":"685af523b4ac24d5329d9655"}],"states_connection":[],"term_comment":"","term_def":"\"The formation of a protein trimer, a macromolecular structure consisting of three noncovalently associated identical or nonidentical subunits.\" [GOC:hjd]","term_id":"GO:0070206","term_is_binding":false,"term_is_obsolete":false,"term_name":"protein trimerization","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2020-12-02T14:33:26.871Z","_id":"685af523b4ac24d5329d9653"},"version":3,"_id":"685af523b4ac24d5329d9652","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6CM9","_id":"685af523b4ac24d5329d965f"},{"db":"PDB","id":"6D83","_id":"685af523b4ac24d5329d9660"},{"db":"EMDB","id":"EMD-7453","_id":"685af523b4ac24d5329d9661"},{"db":"EMDB","id":"EMD-7457","_id":"685af523b4ac24d5329d9662"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006208","ec_name":"cryogenic electron microscopy evidence used in manual assertion","ec_ontology":"ECO","start":168,"end":179,"interaction_partner":[],"reference_html":"HIV-1 Nefs Are Cargo-Sensitive AP-1 Trimerization Switches in Tetherin Downregulation. <i> Morris KL, Buffalo CZ, Stürzel CM, Heusinger E, Kirchhoff F, Ren X, Hurley JH. </i> Cell, 2018","reference_id":"30053425","region_id":"DP02897r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The Nef sequences 149–157 and 168–179 are disordered over gaps of 22 and 25 Å, respectively between the LL motif and the Nef core.","_id":"685af523b4ac24d5329d9663"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-30T09:31:23.539Z","_id":"685af523b4ac24d5329d9664"},"version":1,"_id":"685af523b4ac24d5329d965e","reference_source":"pmid"}],"__v":0,"disorder_content":0.23300970873786409,"disprot_consensus":{"full":[{"start":27,"end":56,"type":"D"},{"start":158,"end":168,"type":"T"},{"start":169,"end":179,"type":"D"}],"Structural state":[{"start":27,"end":56,"type":"D"},{"start":162,"end":179,"type":"D"}],"Structural transition":[{"start":158,"end":168,"type":"T"}],"Biological process":[{"start":160,"end":165,"type":"F"}]}},{"acc":"P35585","features":{"gene3D":[],"pfam":[{"id":"PF00928","name":"Adaptor complexes medium subunit family","start":157,"end":422},{"id":"PF01217","name":"Clathrin adaptor complex small chain","start":5,"end":133}]},"creator":"lchemes","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MSASAVYVLDLKGKVLICRNYRGDVDMSEVEHFMPILMEKEEEGMLSPILAHGGVRFMWIKHNNLYLVATSKKNACVSLVFSFLYKVVQVFSEYFKELEEESIRDNFVIIYELLDELMDFGYPQTTDSKILQEYITQEGHKLETGAPRPPATVTNAVSWRSEGIKYRKNEVFLDVIEAVNLLVSANGNVLRSEIVGSIKMRVFLSGMPELRLGLNDKVLFDNTGRGKSKSVELEDVKFHQCVRLSRFENDRTISFIPPDGEFELMSYRLNTHVKPLIWIESVIEKHSHSRIEYMVKAKSQFKRRSTANNVEIHIPVPNDADSPKFKTTVGSVKWVPENSEIVWSVKSFPGGKEYLMRAHFGLPSVEAEDKEGKPPISVKFEIPYFTTSGIQVRYLKIIEKSGYQALPWVRYITQNGDYQLRTQ","length":423,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":231,"region_id":"DP02898r001","start":219,"term_id":"IDPO:0000002","statement":[{"text":"By combining information about the sequence at the μ2 cleavage site (31) with knowledge of the μ2 structure, we can identify the protease-sensitive segment as a disordered loop around residue 224 (not, as one might have expected, the interdomain linker). The same loop is present and disordered in μ1","type":"Results"},{"text":"The disordered region corresponds to residues 219-231","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"15377783","version":2,"reference_html":"Crystal structure of the clathrin adaptor protein 1 core. <i> Heldwein EE, Macia E, Wang J, Yin HL, Kirchhausen T, Harrison SC. </i> Proc Natl Acad Sci U S A, 2004","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1W63"}],"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":231,"region_id":"DP02898r002","start":218,"term_id":"IDPO:0000011","statement":[{"text":"An unstructured region of μ1 (residues 218–231) becomes ordered to interact with both Nef and the MHC-I CD [...] Residues 215–233 of μ1 rearrange from a disordered loop in the crystal structure of the AP1 core into a helix-turn motif when in complex with the MHC-I CD and Nef. ","type":"Results"},{"text":"The region becomes ordered upon binding to MHC-I","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"22705789","version":2,"reference_html":"Structural basis of evasion of cellular adaptive immunity by HIV-1 Nef. <i> Jia X, Singh R, Homann S, Yang H, Guatelli J, Xiong Y. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4EMZ"},{"db":"PDB","id":"4EN2"}],"term_name":"disorder to order","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP02898r003","ec_ontology":"ECO","end":231,"term_id":"GO:0005515","start":218,"version":3,"statement":[{"text":"An unstructured region of μ1 (residues 218–231) becomes ordered to interact with both Nef and the MHC-I CD [...] Residues 215–233 of μ1 rearrange from a disordered loop in the crystal structure of the AP1 core into a helix-turn motif when in complex with the MHC-I CD and Nef. ","type":"Results"},{"text":"The region becomes ordered upon binding to MHC-I","type":"Curator statement"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P04439","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"22705789","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4EMZ"},{"db":"PDB","id":"4EN2"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"lchemes","reference_html":"Structural basis of evasion of cellular adaptive immunity by HIV-1 Nef. <i> Jia X, Singh R, Homann S, Yang H, Guatelli J, Xiong Y. </i> Nat Struct Mol Biol, 2012","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":231,"region_id":"DP02898r004","start":218,"term_id":"GO:0098772","statement":[{"text":"An unstructured region of μ1 (residues 218–231) becomes ordered to interact with both Nef and the MHC-I CD [...] Residues 215–233 of μ1 rearrange from a disordered loop in the crystal structure of the AP1 core into a helix-turn motif when in complex with the MHC-I CD and Nef. ","type":"Results"},{"text":"The region becomes ordered upon binding to MHC-I","type":"Curator statement"}],"curator_id":"lchemes","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"22705789","version":3,"reference_html":"Structural basis of evasion of cellular adaptive immunity by HIV-1 Nef. <i> Jia X, Singh R, Homann S, Yang H, Guatelli J, Xiong Y. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"4EMZ"},{"db":"PDB","id":"4EN2"}],"term_name":"molecular function regulator","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":10090,"disprot_id":"DP02898","date":"2020-05-30T01:55:51.235Z","organism":"Mus musculus","regions_counter":4,"name":"AP-1 complex subunit mu-1","dataset":[],"UniParc":"UPI00006842B0","uniref100":"UniRef100_P35585","uniref90":"UniRef90_Q9BXS5","uniref50":"UniRef50_Q9BXS5","genes":[{"name":{"value":"Ap1m1"},"synonyms":[{"value":"Cltnm"}]}],"alphafold_very_low_content":0.014184397163120567,"disorder_content":0.030732860520094562,"disprot_consensus":{"full":[{"start":218,"end":231,"type":"T"}],"Structural state":[{"start":219,"end":231,"type":"D"}],"Structural transition":[{"start":218,"end":231,"type":"T"}],"Molecular function":[{"start":218,"end":231,"type":"F"}]}},{"acc":"P23873","features":{"gene3D":[{"start":1,"end":88,"id":"G3DSA:1.10.260.40","name":"lambda repressor-like DNA-binding domains"}],"pfam":[{"id":"PF01381","name":"Helix-turn-helix","start":18,"end":69}]},"creator":"lchemes","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"sequence":"MMSFQKIYSPTQLANAMKLVRQQNGWTQSELAKKIGIKQATISNFENNPDNTTLTTFFKILQSLELSMTLCDAKNASPESTEQQNLEW","length":88,"dataset":["Unicellular toxins and antitoxins"],"regions":[{"region_id":"DP02899r001","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T18:36:35.672Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":88,"term_id":"IDPO:0000002","start":73,"version":2,"statement":[{"text":"The first three and last 16 residues of each HipB subunit are disordered and located near a small β-sheet, that is composed of β1 and β1′ (from the other subunit) and forms a “β–lid” (Fig. 2A).","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Molecular mechanisms of HipA-mediated multidrug tolerance and its neutralization by HipB. <i> Schumacher MA, Piro KM, Xu W, Hansen S, Lewis K, Brennan RG. </i> Science, 2009","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"19150849","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3HZI"},{"db":"PDB","id":"3DNV"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lchemes","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02899r002","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T18:36:54.248Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":88,"term_id":"IDPO:0000048","start":73,"version":3,"statement":[{"text":"To test the hypothesis that the 16 residue C-terminal stretch is critical for degradation, we cloned a truncated HipB (HipB72) lacking the last 16 residues of HipB into pBR creating pBRhipB72. We measured the rate of in vivo degradation of HipB72 in wild type and Δlon (KLE905 and KLE906, respectively) (Fig. 4). Interestingly, HipB72 is indeed substantially more stabile (t1/2>200 min) than full length HipB in wild type indicating that the unstructured C terminus of HipB is essential for degradation by Lon protease (Fig. 4A). As expected, full length HipB72 is also stable in Δlon background. We purified the truncated HipB (His6-HipB72) and tested it in the Lon in vitro degradation assay. The effect was also noticeable though less pronounced in vitro. The half-life time of HipB changed from 74 min for full length HipB to 130 min in the mutant (Fig. 4B).","type":"Results"},{"text":"Our data show that a disordered C-terminus of HipB serves as a degradation signal for the Lon protease.","type":"Discussion"}],"term_name":"limited proteolysis display site","ec_name":"mutant phenotype evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"22720069","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Disorder function","ec_id":"ECO:0000315","curator_id":"rpancsa","reference_html":"Regulation of the Escherichia coli HipBA toxin-antitoxin system by proteolysis. <i> Hansen S, Vulić M, Min J, Yen TJ, Schumacher MA, Brennan RG, Lewis K. </i> PLoS One, 2012","ec_go":"IMP","disprot_namespace":"Disorder function"}],"released":"2020_12","ncbi_taxon_id":83333,"disprot_id":"DP02899","date":"2020-05-30T06:14:58.188Z","organism":"Escherichia coli (strain K12)","regions_counter":2,"name":"Antitoxin HipB","UniParc":"UPI000012C72A","uniref100":"UniRef100_P23873","uniref90":"UniRef90_P23873","uniref50":"UniRef50_P23873","genes":[{"name":{"value":"hipB"},"olnNames":[{"value":"b1508"},{"value":"JW1501"}]}],"alphafold_very_low_content":0.07954545454545454,"disorder_content":0.18181818181818182,"disprot_consensus":{"full":[{"start":73,"end":88,"type":"D"}],"Structural state":[{"start":73,"end":88,"type":"D"}],"Disorder function":[{"start":73,"end":88,"type":"F"}]}},{"acc":"P0A968","features":{"gene3D":[],"pfam":[{"id":"PF00313","name":"'Cold-shock' DNA-binding domain","start":3,"end":65}]},"creator":"lchemes","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"sequence":"MEKGTVKWFNNAKGFGFICPEGGGEDIFAHYSTIQMDGYRTLKAGQSVQFDVHQGPKGNHASVIVPVEVEAAVA","length":74,"dataset":["Unicellular toxins and antitoxins","RNA-binding proteins"],"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":74,"region_id":"DP02900r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"Here we report that CspD is subject to proteolysis by the Lon protease both in vivo and in vitro.","type":"Abstract"},{"text":"To analyse the stability of CspD, in vivo degradation experiments in E. coli MC4100 were performed as described in Experimental procedures . Western blot analysis revealed that CspD indeed is an instable protein (Fig. 2A). ","type":"Results"}],"curator_id":"lchemes","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"21435040","version":2,"reference_html":"The Escherichia coli replication inhibitor CspD is subject to growth-regulated degradation by the Lon protease. <i> Langklotz S, Narberhaus F. </i> Mol Microbiol, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:33:48.648Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0192-9906","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2020_12","ncbi_taxon_id":83333,"disprot_id":"DP02900","date":"2020-05-30T06:23:53.535Z","organism":"Escherichia coli (strain K12)","regions_counter":2,"name":"Cold shock-like protein CspD","UniParc":"UPI0000128582","uniref100":"UniRef100_P0A970","uniref90":"UniRef90_P0A970","uniref50":"UniRef50_P0A970","genes":[{"name":{"value":"cspD"},"synonyms":[{"value":"cspH"},{"value":"ybjA"}],"olnNames":[{"value":"b0880"},{"value":"JW0864"}]}],"alphafold_very_low_content":0.05405405405405406,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":74,"type":"D"}],"Structural state":[{"start":1,"end":74,"type":"D"}]}},{"acc":"J7QA90","features":{"gene3D":[],"pfam":[{"id":"PF08681","name":"Antitoxin TacA 1-like","start":8,"end":86}]},"creator":"lchemes","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"sequence":"MSAVKKQRIDLRLTDDDKSMIEEAAAISNQSVSQFMLNSASQRAAEVIEQHRRVILNEESWTRVMDALSNPPSPGEKLKRAAKRLQGM","length":88,"dataset":["Unicellular toxins and antitoxins"],"regions":[{"region_id":"DP02901r001","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T18:37:28.383Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":88,"term_id":"IDPO:0000002","start":73,"version":2,"statement":[{"text":"In the repressor complex, AtaR intrinsically disordered region interacts with AtaT at two different sites, folding into different structures, that are involved in two separate functional roles, toxin neutralization and placing the DNA-binding domains of AtaR in a binding-compatible orientation. \n\n","type":"Abstract"},{"text":"The antitoxin AtaR binds and neutralizes AtaT via its intrinsically disordered C-terminal region (IDR), sufficient to counteract the action of AtaT in vivo\n","type":"Introduction"},{"text":"The structure of AtaR shows the RHH dimer adopts an elongated conformation (Fig. 2a). The second α-helix of each monomer extends toward the C terminus from V32 to S69 (S73 to M88 are not visible and are presumably disordered)","type":"Results"},{"text":"While the region with missing residues in the PDB 6GTO is from residues 71-88, the authors limit the region to residues 73-88.","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","reference_html":"Mechanism of regulation and neutralization of the AtaR-AtaT toxin-antitoxin system. <i> Jurėnas D, Van Melderen L, Garcia-Pino A. </i> Nat Chem Biol, 2019","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"30718814","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6GTO"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lchemes","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02901r002","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T10:54:57.183Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":88,"term_id":"IDPO:0000002","start":44,"version":3,"statement":[{"text":"On its own, the C-terminal region of AtaR (AtaRA44–M88) or shorter versions from S60 to M88 (AtaRS60–M88) are largely disordered in solution as shown by circular dichroism spectroscopy (Supplementary Fig. 3b). The circular dichroism spectra of both, AtaRA44–M88 and AtaRS60–M88, show a lack of secondary structure and a distinctive minimum at 205nm typical of disordered proteins. Moreover, AtaRA44–M88 lacks an observable transition from native to denatured state, also a signature feature of IDRs (Supplementary Fig. 3b).","type":"Results"}],"term_name":"disorder","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30718814","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006204","curator_id":"rpancsa","reference_html":"Mechanism of regulation and neutralization of the AtaR-AtaT toxin-antitoxin system. <i> Jurėnas D, Van Melderen L, Garcia-Pino A. </i> Nat Chem Biol, 2019","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02901r003","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T18:37:25.915Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":88,"term_id":"IDPO:0000011","start":44,"version":2,"statement":[{"text":"In the repressor complex, AtaR intrinsically disordered region interacts with AtaT at two different sites, folding into different structures, that are involved in two separate functional roles, toxin neutralization and placing the DNA-binding domains of AtaR in a binding-compatible orientation. [...] The antitoxin AtaR binds and neutralizes AtaT via its intrinsically disordered C-terminal region (IDR), sufficient to counteract the action of AtaT in vivo10\n\n","type":"Abstract"},{"text":"The structure AtaRA44–M88 in complex with AtaTY144F (Fig. 3a and Supplementary Fig. 3d) showed the intrinsically disordered AtaRA44–M88 wrapped around AtaTY144F (encompassing a large interface of ~1,500Å2 ). AtaRA44–M88 is anchored to the surface of AtaT via four structural motifs—mt1 (β-strand), mt2 (α-helix), a proline-rich fragment (P-rich) and mt3 (α-helix) (Fig. 3a–g)","type":"Results"},{"text":"Evidence is in PDB 6gtr","type":"Curator statement"}],"term_name":"disorder to order","ec_name":"x-ray crystallography evidence used in manual assertion","reference_html":"Mechanism of regulation and neutralization of the AtaR-AtaT toxin-antitoxin system. <i> Jurėnas D, Van Melderen L, Garcia-Pino A. </i> Nat Chem Biol, 2019","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"30718814","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6GTS"},{"db":"PDB","id":"6GTQ"},{"db":"PDB","id":"6GTR"}],"term_namespace":"Structural transition","ec_id":"ECO:0005670","curator_id":"lchemes","curator_orcid":"0000-0003-0192-9906","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP02901r004","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T18:37:24.572Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":88,"term_id":"GO:0005515","start":44,"version":4,"statement":[{"text":"In the repressor complex, AtaR intrinsically disordered region interacts with AtaT at two different sites, folding into different structures, that are involved in two separate functional roles, toxin neutralization and placing the DNA-binding domains of AtaR in a binding-compatible orientation.\n\n","type":"Abstract"},{"text":"The structure AtaRA44–M88 in complex with AtaTY144F (Fig. 3a and Supplementary Fig. 3d) showed the intrinsically disordered AtaRA44–M88 wrapped around AtaTY144F (encompassing a large interface of ~1,500Å2 ). AtaRA44–M88 is anchored to the surface of AtaT via four structural motifs—mt1 (β-strand), mt2 (α-helix), a proline-rich fragment (P-rich) and mt3 (α-helix) (Fig. 3a–g)","type":"Results"},{"text":"Evidence is in PDB 6gtr","type":"Curator statement"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"A0A1V3CQ74","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","reference_html":"Mechanism of regulation and neutralization of the AtaR-AtaT toxin-antitoxin system. <i> Jurėnas D, Van Melderen L, Garcia-Pino A. </i> Nat Chem Biol, 2019","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30718814","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6GTS"},{"db":"PDB","id":"6GTQ"},{"db":"PDB","id":"6GTR"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"rpancsa","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02901r005","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T18:37:23.903Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":88,"term_id":"GO:0005515","start":44,"version":4,"statement":[{"text":"We used AtaR A44–M88 to gain further insights into the mechanism of AtaT neutralization. AtaT Y144F interacts with AtaR A44–M88 with an affinity of 367nM, lower than the affinity for the full length AtaR (Kd=29nM) (Supplementary Fig. 2g,h and Supplementary Table 1).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"A0A1V3CQ74","partner_end":null}],"term_name":"protein binding","ec_name":"isothermal titration calorimetry evidence used in manual assertion","reference_html":"Mechanism of regulation and neutralization of the AtaR-AtaT toxin-antitoxin system. <i> Jurėnas D, Van Melderen L, Garcia-Pino A. </i> Nat Chem Biol, 2019","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30718814","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"rpancsa","curator_orcid":"0000-0003-0849-9312","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02901r007","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T10:57:01.339Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":88,"term_id":"GO:0097351","start":44,"version":4,"statement":[{"text":"The antitoxin AtaR binds and neutralizes AtaT via its intrinsically disordered C-terminal region (IDR), sufficient to counteract the action of AtaT in vivo10\n\n","type":"Abstract"},{"text":"Removing the last six residues of AtaR (K83 to M88) has a strong effect on growth and when this is extended to nine residues (R80 to M88) neutralization severely drops. These results indicate the neutralization region of AtaR involves almost entirely the IDR.","type":"Results"},{"text":"AtaR neutralizes AtaT via four functional domains located mainly in the C-terminal IDR","type":"Discussion"}],"term_name":"toxin sequestering activity","ec_name":"experimental phenotypic evidence used in manual assertion","reference_html":"Mechanism of regulation and neutralization of the AtaR-AtaT toxin-antitoxin system. <i> Jurėnas D, Van Melderen L, Garcia-Pino A. </i> Nat Chem Biol, 2019","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"30718814","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6GTO"},{"db":"PDB","id":"6GTS"},{"db":"PDB","id":"6GTQ"},{"db":"PDB","id":"6GTR"}],"term_namespace":"Molecular function","ec_id":"ECO:0007634","curator_id":"rpancsa","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a toxic protein, disabling its function. There may be more than one antitoxin to a toxic protein. Instances of this activity are known only in prokaryotes, where the toxic protein may be a ribonuclease, a DNA gyrase, or other.\" [GOC:rs, PMID:19143615, PMID:19325885, PMID:21819231, PMID:22545240, PMID:24806488, Wikipedia:Toxin-antitoxin_system#Type_II]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_12","ncbi_taxon_id":562,"disprot_id":"DP02901","date":"2020-05-30T19:23:18.899Z","organism":"Escherichia coli","regions_counter":7,"name":"DUF1778 domain-containing protein","UniParc":"UPI00000D0B2F","uniref100":"UniRef100_J7QA90","uniref90":"UniRef90_J7QA90","uniref50":"UniRef50_J7QA90","genes":[{"orfNames":[{"value":"A9X72_01425","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AVU64007.1","url":"https://www.ebi.ac.uk/ena/browser/view/AVU64007.1"}}]},{"value":"AAG43_001902","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EFL6008478.1","url":"https://www.ebi.ac.uk/ena/browser/view/EFL6008478.1"}}]},{"value":"ACN81_27750","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"OKU12987.1","url":"https://www.ebi.ac.uk/ena/browser/view/OKU12987.1"}}]},{"value":"BANRA_04607","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"VCV62499.1","url":"https://www.ebi.ac.uk/ena/browser/view/VCV62499.1"}}]},{"value":"BF481_000881","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EFI1480547.1","url":"https://www.ebi.ac.uk/ena/browser/view/EFI1480547.1"}}]},{"value":"BHS81_20640","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ORJ74380.1","url":"https://www.ebi.ac.uk/ena/browser/view/ORJ74380.1"}}]},{"value":"BK292_07330","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"OJM96857.1","url":"https://www.ebi.ac.uk/ena/browser/view/OJM96857.1"}}]},{"value":"BMT50_11545","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"OKB73359.1","url":"https://www.ebi.ac.uk/ena/browser/view/OKB73359.1"}}]},{"value":"BN17_33961","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CCJ46076.1","url":"https://www.ebi.ac.uk/ena/browser/view/CCJ46076.1"}}]},{"value":"BOH76_21075","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TEY97339.1","url":"https://www.ebi.ac.uk/ena/browser/view/TEY97339.1"}}]},{"value":"BON67_16110","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TEZ18500.1","url":"https://www.ebi.ac.uk/ena/browser/view/TEZ18500.1"}}]},{"value":"BON68_09795","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TEZ33383.1","url":"https://www.ebi.ac.uk/ena/browser/view/TEZ33383.1"}}]},{"value":"BON69_15975","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TEZ31271.1","url":"https://www.ebi.ac.uk/ena/browser/view/TEZ31271.1"}}]},{"value":"BON70_07290","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TEZ36924.1","url":"https://www.ebi.ac.uk/ena/browser/view/TEZ36924.1"}}]},{"value":"BON71_12410","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TEZ48313.1","url":"https://www.ebi.ac.uk/ena/browser/view/TEZ48313.1"}}]},{"value":"BON72_01915","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TEZ56812.1","url":"https://www.ebi.ac.uk/ena/browser/view/TEZ56812.1"}}]},{"value":"BON76_01280","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TEZ74177.1","url":"https://www.ebi.ac.uk/ena/browser/view/TEZ74177.1"}}]},{"value":"BON94_28105","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TFA47341.1","url":"https://www.ebi.ac.uk/ena/browser/view/TFA47341.1"}}]},{"value":"BvCmsHHP019_01674","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"GCP93102.1","url":"https://www.ebi.ac.uk/ena/browser/view/GCP93102.1"}}]},{"value":"C9160_12820","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TJH21183.1","url":"https://www.ebi.ac.uk/ena/browser/view/TJH21183.1"}}]},{"value":"C9E67_02045","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"QCL46073.1","url":"https://www.ebi.ac.uk/ena/browser/view/QCL46073.1"}}]},{"value":"CCS08_20675","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"OWW53234.1","url":"https://www.ebi.ac.uk/ena/browser/view/OWW53234.1"}}]},{"value":"CR538_01655","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AUJ99219.1","url":"https://www.ebi.ac.uk/ena/browser/view/AUJ99219.1"}}]},{"value":"DAH19_17150","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGG54002.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGG54002.1"}}]},{"value":"DAH20_09975","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGG69631.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGG69631.1"}}]},{"value":"DAH23_09180","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGG41890.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGG41890.1"}}]},{"value":"DAH24_08965","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGG14368.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGG14368.1"}}]},{"value":"DAH25_09555","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGJ92561.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGJ92561.1"}}]},{"value":"DAH26_09190","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGG29287.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGG29287.1"}}]},{"value":"DAH29_13330","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGG04776.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGG04776.1"}}]},{"value":"DAH30_05715","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGF95915.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGF95915.1"}}]},{"value":"DAH31_09755","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGF96940.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGF96940.1"}}]},{"value":"DAH42_06460","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGF44049.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGF44049.1"}}]},{"value":"DAH43_06950","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGF22036.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGF22036.1"}}]},{"value":"DAH45_07300","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGF31294.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGF31294.1"}}]},{"value":"DAH46_06945","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGF14347.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGF14347.1"}}]},{"value":"DAH47_06190","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGF31670.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGF31670.1"}}]},{"value":"DAH48_06575","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGF07713.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGF07713.1"}}]},{"value":"DAH49_06925","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGF15990.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGF15990.1"}}]},{"value":"DEN87_09685","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TFY43683.1","url":"https://www.ebi.ac.uk/ena/browser/view/TFY43683.1"}}]},{"value":"DEN88_06875","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TFY38808.1","url":"https://www.ebi.ac.uk/ena/browser/view/TFY38808.1"}}]},{"value":"DEN89_12920","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TFY32675.1","url":"https://www.ebi.ac.uk/ena/browser/view/TFY32675.1"}}]},{"value":"DEN90_11110","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TFY26548.1","url":"https://www.ebi.ac.uk/ena/browser/view/TFY26548.1"}}]},{"value":"DEN91_13510","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TFY08219.1","url":"https://www.ebi.ac.uk/ena/browser/view/TFY08219.1"}}]},{"value":"DEN92_11790","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TFY23523.1","url":"https://www.ebi.ac.uk/ena/browser/view/TFY23523.1"}}]},{"value":"DEN95_20050","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TFX85834.1","url":"https://www.ebi.ac.uk/ena/browser/view/TFX85834.1"}}]},{"value":"DEO04_12010","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TFX44578.1","url":"https://www.ebi.ac.uk/ena/browser/view/TFX44578.1"}}]},{"value":"DEO05_11020","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TFX58678.1","url":"https://www.ebi.ac.uk/ena/browser/view/TFX58678.1"}}]},{"value":"DEO06_11255","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TFX43010.1","url":"https://www.ebi.ac.uk/ena/browser/view/TFX43010.1"}}]},{"value":"DEO07_11670","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TFX51024.1","url":"https://www.ebi.ac.uk/ena/browser/view/TFX51024.1"}}]},{"value":"DEO08_08190","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TFX26072.1","url":"https://www.ebi.ac.uk/ena/browser/view/TFX26072.1"}}]},{"value":"DEO09_11685","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TFX34170.1","url":"https://www.ebi.ac.uk/ena/browser/view/TFX34170.1"}}]},{"value":"DEO10_12650","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TFX21844.1","url":"https://www.ebi.ac.uk/ena/browser/view/TFX21844.1"}}]},{"value":"DEO11_11680","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TFX32486.1","url":"https://www.ebi.ac.uk/ena/browser/view/TFX32486.1"}}]},{"value":"DEO18_07855","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TFW86965.1","url":"https://www.ebi.ac.uk/ena/browser/view/TFW86965.1"}}]},{"value":"DEO20_22645","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TFW71260.1","url":"https://www.ebi.ac.uk/ena/browser/view/TFW71260.1"}}]},{"value":"DS732_25100","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AXO09360.1","url":"https://www.ebi.ac.uk/ena/browser/view/AXO09360.1"}}]},{"value":"E0I42_12085","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TZF12933.1","url":"https://www.ebi.ac.uk/ena/browser/view/TZF12933.1"}}]},{"value":"E2113_17730","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TEW40430.1","url":"https://www.ebi.ac.uk/ena/browser/view/TEW40430.1"}}]},{"value":"E2117_15630","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TEW24404.1","url":"https://www.ebi.ac.uk/ena/browser/view/TEW24404.1"}}]},{"value":"E5M02_05865","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGI17841.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGI17841.1"}}]},{"value":"E5P24_11930","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGJ48607.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGJ48607.1"}}]},{"value":"E5P25_18400","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGJ34641.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGJ34641.1"}}]},{"value":"E5P33_10590","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGJ10738.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGJ10738.1"}}]},{"value":"E5P39_05805","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGI88114.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGI88114.1"}}]},{"value":"E5P41_10150","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGI75703.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGI75703.1"}}]},{"value":"E5P42_15500","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGI85014.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGI85014.1"}}]},{"value":"E5P43_02700","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGI68718.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGI68718.1"}}]},{"value":"E5P44_18685","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGI52740.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGI52740.1"}}]},{"value":"E5P45_04330","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGI52856.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGI52856.1"}}]},{"value":"E5P46_15485","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGI50626.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGI50626.1"}}]},{"value":"E5P47_14950","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGI36486.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGI36486.1"}}]},{"value":"E5P48_01580","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGI41660.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGI41660.1"}}]},{"value":"E5P49_04010","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGI45130.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGI45130.1"}}]},{"value":"E5P50_07270","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGI28574.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGI28574.1"}}]},{"value":"E5P52_06600","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGI22885.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGI22885.1"}}]},{"value":"E5S34_11300","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGH99944.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGH99944.1"}}]},{"value":"E5S37_09185","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGI01477.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGI01477.1"}}]},{"value":"E5S39_09190","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGH86596.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGH86596.1"}}]},{"value":"E5S42_08280","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGH76119.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGH76119.1"}}]},{"value":"E5S44_11235","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGH71312.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGH71312.1"}}]},{"value":"E5S45_10170","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGH16988.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGH16988.1"}}]},{"value":"E5S54_06815","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGH49139.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGH49139.1"}}]},{"value":"E5S61_12055","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TGH02972.1","url":"https://www.ebi.ac.uk/ena/browser/view/TGH02972.1"}}]},{"value":"EBP16_11825","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"MLY01084.1","url":"https://www.ebi.ac.uk/ena/browser/view/MLY01084.1"}}]},{"value":"GAJ26_06090","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EFH6212603.1","url":"https://www.ebi.ac.uk/ena/browser/view/EFH6212603.1"}}]},{"value":"GKF89_26985","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"MSD77464.1","url":"https://www.ebi.ac.uk/ena/browser/view/MSD77464.1"}}]},{"value":"GRW57_20865","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"MXH42725.1","url":"https://www.ebi.ac.uk/ena/browser/view/MXH42725.1"}}]},{"value":"GUC01_13975","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"NAG20118.1","url":"https://www.ebi.ac.uk/ena/browser/view/NAG20118.1"}}]},{"value":"HHH44_000669","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"HAH1417320.1","url":"https://www.ebi.ac.uk/ena/browser/view/HAH1417320.1"}}]},{"value":"J4S20_001276","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"HBA5962167.1","url":"https://www.ebi.ac.uk/ena/browser/view/HBA5962167.1"}}]},{"value":"NCTC10418_00491","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"STE82860.1","url":"https://www.ebi.ac.uk/ena/browser/view/STE82860.1"}}]},{"value":"NCTC10865_00468","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"STI15260.1","url":"https://www.ebi.ac.uk/ena/browser/view/STI15260.1"}}]},{"value":"NCTC13127_00609","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"STI62953.1","url":"https://www.ebi.ac.uk/ena/browser/view/STI62953.1"}}]}]}],"alphafold_very_low_content":0.011363636363636364,"disorder_content":0.5113636363636364,"disprot_consensus":{"full":[{"start":44,"end":88,"type":"T"}],"Structural state":[{"start":44,"end":88,"type":"D"}],"Structural transition":[{"start":44,"end":88,"type":"T"}],"Molecular function":[{"start":44,"end":88,"type":"F"}]}},{"acc":"P78953","features":{"pfam":[],"gene3D":[]},"creator":"rpancsa","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"sequence":"MKEQEFSYREAKDVSLDSKGLENSFLSSPNREKTPLFFEGNSNETSGYDQTKNFTHGDGDMSLGNLSELNVATDLLESLDLRSMYMHGYGHLDSSFSSQHSPDNRKRMSSTSVFKRINSEEEGRIPSLTYSAGTMNSTSSSTASLKGADIVADYETFNPDQNLAELSFDRSKSSRKRAVEVAEFSRAKTMSPLEYTVQHPYQSHNELSTNPARARAGSVPNLARIPSDVKPVPPAHLSASSTVGPRILPSLPKDTTEDNPALERVETTASLDMDYKPLEPLAPIQEAPVEDTSEPFSSVPEATLDDSDISTESLRKKVLAKMEAKRISSGSSYASTLRKVYDFSELSLPTNGKDYDELYLQSSRNSEPEISTIINDSLQQENMDEDISATSIPKSQAAYGHGSVTYHEVPRYNLTSASVGYSISSQRGRIKSSSTIDNLSAILSSEDLRHPSMQPVPGTKRTYSNYCENEPNKSSQSLVSSESHNVEGWNYSETGTVGFYDPSAEISASIDELRQSTPVARDSELLSRAHSFDLNRLDLPSQDKSTSYEVPNGTENQSPRPVTSLGFVNETFFEEKPKAPLPLGRFYIHLNSILNISISEVHSPIKIIVNTPTQNMQLPWQAVNGNNRLDHDFAFHVDDNFKVSFMFLDIPIEDKSNGSKGVSATKDVSNGKPAETKSKARKFFDKLFNRRKKRKLNKAAAVENSKAKKSVVIKKVSGTATLNLGNVKDSCFGKAFNVEIPIISRGFLEAIPVKINSIGKRTLGNLTLTCLYIPELSVPEQELPFTLEQATMDLRHVRSNYLYNEGYLYRLEDSSIRRRFVVLRSKQLNFYAEKGGQYLDTFQLSKTVVSIPMVNFSEAVSNLGLVAGILATSVDRRHVQLFADSKKVCQKWLQVMNSRSFALDRGTEKLWLQEYVNFMA","length":920,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":452,"region_id":"DP02903r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"The low sedimentation coefficient and large Stokes radius are consistent with Mid1p-N452 purified with phosphatase inhibitors being disordered.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"chromatography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31243991","version":2,"reference_html":"The Functionally Important N-Terminal Half of Fission Yeast Mid1p Anillin Is Intrinsically Disordered and Undergoes Phase Separation. <i> Chatterjee M, Pollard TD. </i> Biochemistry, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","term_name":"disorder","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T17:17:01.125Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":452,"region_id":"DP02903r002","start":1,"term_id":"IDPO:0000002","statement":[{"text":"The low sedimentation coefficient and large Stokes radius are consistent with Mid1p-N452 purified with phosphatase inhibitors being disordered.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"analytical ultracentrifugation evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31243991","version":2,"reference_html":"The Functionally Important N-Terminal Half of Fission Yeast Mid1p Anillin Is Intrinsically Disordered and Undergoes Phase Separation. <i> Chatterjee M, Pollard TD. </i> Biochemistry, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006275","term_name":"disorder","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T17:17:01.852Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":452,"region_id":"DP02903r003","start":1,"term_id":"IDPO:0000002","statement":[{"text":"The low sedimentation coefficient and large Stokes radius are consistent with Mid1p-N452 purified with phosphatase inhibitors being disordered.","type":"Results"},{"text":"Static light scattering analysis of the peak of Mid1p-N452 gave a molecular weight of 60 kDa (Figure 3A), which is slightly larger than the molecular weight of 52.7 kDa based on the sequence. Therefore, Mid1pN452 is a monomer with a large hydrodynamic radius.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"static light scattering assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31243991","version":2,"reference_html":"The Functionally Important N-Terminal Half of Fission Yeast Mid1p Anillin Is Intrinsically Disordered and Undergoes Phase Separation. <i> Chatterjee M, Pollard TD. </i> Biochemistry, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007066","term_name":"disorder","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T17:17:08.646Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":308,"region_id":"DP02903r004","start":1,"term_id":"IDPO:0000002","statement":[{"text":"After uniform labeling of Mid1p-N308 with 15N in bacteria and purification, we recorded 1H −15N HSQC NMR spectra. The peaks in the two-dimensional NMR spectra overlapped and were characterized by limited 1H chemical shift dispersion. These features are characteristic of intrinsically disordered proteins (IDPs) where conformational\naveraging within the rapidly interconvertible ensembles results in poor dispersion. Flexibility allows significant chemical exchange of 15N with bulk water, resulting in decreases in 1H −15N signal intensities and a poor signal-to-noise ratio.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31243991","version":2,"reference_html":"The Functionally Important N-Terminal Half of Fission Yeast Mid1p Anillin Is Intrinsically Disordered and Undergoes Phase Separation. <i> Chatterjee M, Pollard TD. </i> Biochemistry, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T17:17:21.424Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":452,"region_id":"DP02903r005","start":1,"term_id":"IDPO:0000002","statement":[{"text":"The CD spectrum of Mid1p-N452 purified from insect cells with phosphatase inhibitors (Figure 5C) was typical of a disordered protein53 with a minimum at 205 nm and a shoulder at 220 nm.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31243991","version":2,"reference_html":"The Functionally Important N-Terminal Half of Fission Yeast Mid1p Anillin Is Intrinsically Disordered and Undergoes Phase Separation. <i> Chatterjee M, Pollard TD. </i> Biochemistry, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"disorder","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T17:17:22.123Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":452,"region_id":"DP02903r006","start":1,"term_id":"GO:0140693","statement":[{"text":"Differential interference contrast microscopy at room temperature (DIC) revealed that Mid1p-N452 at concentrations from 3.8 to 23 μM formed droplets, which increased in size over time.","type":"Results"},{"text":"Like the wild type protein, Mid1p constructs consisting of residues 1 −50649 or 1 −45220 exit the nucleus during interphase and accumulate in cortical nodes that mature to form cytokinetic nodes and assemble functional contractile rings during mitosis.","type":"Discussion"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"microscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31243991","version":3,"reference_html":"The Functionally Important N-Terminal Half of Fission Yeast Mid1p Anillin Is Intrinsically Disordered and Undergoes Phase Separation. <i> Chatterjee M, Pollard TD. </i> Biochemistry, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001232","term_name":"molecular condensate scaffold activity","curator_orcid":"0000-0003-0849-9312","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-12T14:40:49.009Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9USI6","partner_end":null}],"ec_ontology":"ECO","end":452,"region_id":"DP02903r007","start":1,"term_id":"GO:0005515","statement":[{"text":"Mid1p immunoprecipitates with overexpressed full-length Myo2, but not with a construct lacking 132 residues from C-terminus.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"co-immunoprecipitation evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31243991","version":3,"reference_html":"The Functionally Important N-Terminal Half of Fission Yeast Mid1p Anillin Is Intrinsically Disordered and Undergoes Phase Separation. <i> Chatterjee M, Pollard TD. </i> Biochemistry, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006030","term_name":"protein binding","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T17:17:23.675Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9USI6","partner_end":null}],"ec_ontology":"ECO","end":452,"region_id":"DP02903r008","start":1,"term_id":"GO:0005515","statement":[{"text":"Hence, we assessed the binding of purified Mid1p-N452 to GST-Myo2-tail, a fusion of\nGST to Myo2p residues 1441 −1526 that we immobilized on glutathione beads. Mid1p-N452 bound to GST-Myo2 tail (1441 −1526) with a Kd of ∼2 μM (n = 2; 1.9 and 2.2).","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31243991","version":3,"reference_html":"The Functionally Important N-Terminal Half of Fission Yeast Mid1p Anillin Is Intrinsically Disordered and Undergoes Phase Separation. <i> Chatterjee M, Pollard TD. </i> Biochemistry, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006077","term_name":"protein binding","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T17:17:24.541Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":284812,"disprot_id":"DP02903","date":"2020-06-15T08:17:26.375Z","organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","regions_counter":8,"name":"Division mal foutue 1 protein","dataset":["Condensates-related proteins"],"UniParc":"UPI00001294D8","uniref100":"UniRef100_P78953","uniref90":"UniRef90_P78953","uniref50":"UniRef50_P78953","genes":[{"name":{"value":"mid1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8946912","url":"http://www.ncbi.nlm.nih.gov/pubmed/8946912","alternativeUrl":"https://europepmc.org/abstract/MED/8946912"}}]},"synonyms":[{"value":"dmf1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8946912","url":"http://www.ncbi.nlm.nih.gov/pubmed/8946912","alternativeUrl":"https://europepmc.org/abstract/MED/8946912"}}]}],"orfNames":[{"value":"SPCC4B3.15"}]}],"alphafold_very_low_content":0.6695652173913044,"disorder_content":0.49130434782608695,"disprot_consensus":{"full":[{"start":1,"end":452,"type":"D"}],"Structural state":[{"start":1,"end":452,"type":"D"}],"Molecular function":[{"start":1,"end":452,"type":"F"}]}},{"acc":"Q8NBI3","features":{"pfam":[{"id":"PF15550","name":"Draxin","start":38,"end":349}],"gene3D":[]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MAGPAIHTAPMLFLVLLLPLELSLAGALAPGTPARNLPENHIDLPGPALWTPQASHHRRRGPGKKEWGPGLPSQAQDGAVVTATRQASRLPEAEGLLPEQSPAGLLQDKDLLLGLALPYPEKENRPPGWERTRKRSREHKRRRDRLRLHQGRALVRGPSSLMKKAELSEAQVLDAAMEESSTSLAPTMFFLTTFEAAPATEESLILPVTSLRPQQAQPRSDGEVMPTLDMALFDWTDYEDLKPDGWPSAKKKEKHRGKLSSDGNETSPAEGEPCDHHQDCLPGTCCDLREHLCTPHNRGLNNKCFDDCMCVEGLRCYAKFHRNRRVTRRKGRCVEPETANGDQGSFINV","length":349,"regions":[{"region_id":"DP02904r001","unpublished":true,"ec_ontology":"ECO","end":243,"term_id":"GO:0005515","start":225,"version":3,"statement":[{"text":"Crystal structure of Netrin-1 in complex with a Draxin fragment","type":"Article"},{"text":"We show that Draxin is largely unstructured, but that it uses a small C-terminal domain (Draxin-C) to bind DCC N-terminal Ig domains and an upstream conserved peptide motif (Draxin-22) to bind Netrin-1.","type":"Introduction"},{"text":"Draxin also contains a Netrin-1 binding site, just 20 amino acids N-terminal to Draxin-C, the DCC binding domain. It covers a 22-residue region that is evolutionary conserved, but is intrinsically unstructured.","type":"Discussion"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"O95631","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2023_12","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"29503192","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6FKQ"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"fquaglia","reference_html":"Structural Basis for Draxin-Modulated Axon Guidance and Fasciculation by Netrin-1 through DCC. <i> Liu Y, Bhowmick T, Liu Y, Gao X, Mertens HDT, Svergun DI, Xiao J, Zhang Y, Wang JH, Meijers R. </i> Neuron, 2018","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":243,"region_id":"DP02904r002","start":225,"term_id":"IDPO:0000011","unpublished":true,"statement":[{"text":"Crystal structure of Netrin-1 in complex with a Draxin fragment","type":"Article"},{"text":"We show that Draxin is largely unstructured, but that it uses a small C-terminal domain (Draxin-C) to bind DCC N-terminal Ig domains and an upstream conserved peptide motif (Draxin-22) to bind Netrin-1.","type":"Introduction"},{"text":"Draxin also contains a Netrin-1 binding site, just 20 amino acids N-terminal to Draxin-C, the DCC binding domain. It covers a 22-residue region that is evolutionary conserved, but is intrinsically unstructured.","type":"Discussion"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29503192","version":2,"reference_html":"Structural Basis for Draxin-Modulated Axon Guidance and Fasciculation by Netrin-1 through DCC. <i> Liu Y, Bhowmick T, Liu Y, Gao X, Mertens HDT, Svergun DI, Xiao J, Zhang Y, Wang JH, Meijers R. </i> Neuron, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"6FKQ"}],"term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":245,"region_id":"DP02904r003","start":25,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Draxin is predicted to consist of a signal peptide for secretion, an unstructured region covering residues 25 to 245, and a C-terminal domain","type":"Results"},{"text":"Dimensionless Kratky plot of the SAXS data demonstrating the partially folded nature of hDraxin in solution. Theoretical Kratky representations for compact folded (dotted black line), fully unfolded (solid black line), and the experimentally derived full-length human Draxin (solid red line) are shown.","type":"Figure"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"small-angle X-ray scattering evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29503192","version":2,"reference_html":"Structural Basis for Draxin-Modulated Axon Guidance and Fasciculation by Netrin-1 through DCC. <i> Liu Y, Bhowmick T, Liu Y, Gao X, Mertens HDT, Svergun DI, Xiao J, Zhang Y, Wang JH, Meijers R. </i> Neuron, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","cross_refs":[{"db":"SASBDB","id":"SASDBZ6"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":243,"region_id":"DP02904r004","start":225,"term_id":"GO:0060090","unpublished":true,"statement":[{"text":"Draxin tethers Netrin-1 and DCC together to promote fasciculation","type":"Article"},{"text":"The relatively strong Draxin/Netrin-1 complex can build a bridge between two axons decorated with DCC, initiating adhesion and therefore fasciculation between the axons. ","type":"Discussion"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"29503192","version":3,"reference_html":"Structural Basis for Draxin-Modulated Axon Guidance and Fasciculation by Netrin-1 through DCC. <i> Liu Y, Bhowmick T, Liu Y, Gao X, Mertens HDT, Svergun DI, Xiao J, Zhang Y, Wang JH, Meijers R. </i> Neuron, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"6FKQ"}],"term_name":"molecular adaptor activity","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":243,"region_id":"DP02904r005","start":225,"term_id":"GO:0098772","unpublished":true,"statement":[{"text":"Draxin tethers Netrin-1 and DCC together to promote fasciculation","type":"Article"},{"text":"The relatively strong Draxin/Netrin-1 complex can build a bridge between two axons decorated with DCC, initiating adhesion and therefore fasciculation between the axons.","type":"Discussion"}],"curator_id":"fquaglia","released":"2023_12","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"29503192","version":3,"reference_html":"Structural Basis for Draxin-Modulated Axon Guidance and Fasciculation by Netrin-1 through DCC. <i> Liu Y, Bhowmick T, Liu Y, Gao X, Mertens HDT, Svergun DI, Xiao J, Zhang Y, Wang JH, Meijers R. </i> Neuron, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"6FKQ"}],"term_name":"molecular function regulator","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2023_12","ncbi_taxon_id":9606,"disprot_id":"DP02904","date":"2020-06-15T08:40:46.498Z","organism":"Homo sapiens","regions_counter":5,"name":"Draxin","dataset":[],"UniParc":"UPI000013E16C","uniref100":"UniRef100_Q8NBI3","uniref90":"UniRef90_Q8NBI3","uniref50":"UniRef50_Q8NBI3","genes":[{"name":{"value":"DRAXIN","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03060","url":"https://hamap.expasy.org/unirule/MF_03060"}}]},"synonyms":[{"value":"C1orf187"}],"orfNames":[{"value":"PSEC0258"},{"value":"UNQ3119/PRO10268"}]}],"alphafold_very_low_content":0.47564469914040114,"disorder_content":0.6332378223495702,"disprot_consensus":{"full":[{"start":25,"end":224,"type":"D"},{"start":225,"end":243,"type":"T"},{"start":244,"end":245,"type":"D"}],"Structural state":[{"start":25,"end":245,"type":"D"}],"Molecular function":[{"start":225,"end":243,"type":"F"}],"Structural transition":[{"start":225,"end":243,"type":"T"}]}},{"acc":"P53853","features":{"pfam":[{"id":"PF00956","name":"Nucleosome assembly protein (NAP)","start":37,"end":174}],"gene3D":[]},"creator":"rpancsa","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"sequence":"MMSDQENENEHAKAFLGLAKCEEEVDAIEREVELYRLNKMKPVYEKRDAYIDEIAEFWKIVLSQHVSFANYIRASDFKYIDTIDKIKVEWLALESEMYDTRDFSITFHFHGIEGDFKEQQVTKVFQIKKGKDDQEDGILTSEPVPIEWPQSYDSINPDLIKDKRSPEGKKKYRQGMKTIFGWFRWTGLKPGKEFPHGDSLASLFSEEIYPFCVKYYAEAQRDLEDEEGESGLSADGDSEDDDGSLGEVDLPLSDEEPSSKKRKV","length":264,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":264,"region_id":"DP02908r001","start":226,"term_id":"IDPO:0000002","statement":[{"text":"TALOS-N CS analysis of Vps75226–264 in the context of full-length Vps752 shows that the Vps75 tail is disordered. The same narrow CS dispersion is observed in the full complex.","type":"Figure"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31387991","version":2,"reference_html":"Histone chaperone exploits intrinsic disorder to switch acetylation specificity. <i> Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T. </i> Nat Commun, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02908r002","ec_ontology":"ECO","end":264,"term_id":"GO:0005515","start":226,"version":3,"statement":[{"text":"When we compared the 1H-15N CSPs of the Vps75 CTAD in the Asf1–H3:H4–Rtt109–Vps752 and the Asf1–H329–135:H4–Rtt109–Vps752 complexes (relative to free Vps752), we observed that the CSPs of residues 234–246 in the complex assembled with N-terminally truncated H3 were smaller than in that assembled with full-length H3 (Fig. 5b), confirming the interaction between the Vps75 CTAD and the H3 tail. Despite binding to each other, both the H3 N-terminal domain and the Vps75 CTAD remain disordered (Figs. 4b, ​,5c5c and Supplementary Fig. 9), hence conserving a substantial portion of their free-form conformational entropy. In agreement with the structural data, the removal of the Vps75 CTAD severely impacts H3-K9ac, but has no effect on H3-K56ac.","type":"Results"},{"text":"We compared the 2D 1H-15N NMR spectrum of H3 in the free histone dimer H3:H4 with those of H3 in the Asf1–H3:H4 complex and after addition of one equivalent of either Vps752 or Vps7521–225. In the presence of Vps752, the chemical shifts of H3 residues 7–37 differed from those measured in either H3:H4 or Asf1–H3:H4, while in the presence of the C-terminally truncated Vps7521–225, the chemical shifts of the H3 tail were identical to those of the free histone dimer (Fig. 4b). This result demonstrates that the H3 tail interacts with the Vps75 CTAD.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P61830","partner_end":null}],"term_name":"protein binding","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31387991","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6O22"}],"term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"rpancsa","reference_html":"Histone chaperone exploits intrinsic disorder to switch acetylation specificity. <i> Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T. </i> Nat Commun, 2019","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":264,"region_id":"DP02908r003","start":226,"term_id":"GO:0044183","statement":[{"text":"We show that Vps75 promotes K9-acetylation by engaging the H3 N-terminal tail in fuzzy electrostatic interactions with its disordered C-terminal domain, thereby confining the H3 tail to a wide central cavity faced by the Rtt109 active site. These fuzzy interactions between disordered domains achieve localization of lysine residues in the H3 tail to the catalytic site with minimal loss of entropy","type":"Abstract"},{"text":"The histone chaperone Vps75 belongs to the nucleosome assembly protein (NAP-1) family, which can bind to the four core histones (H2A, H2B, H3, and H4)25. Like Asf1, Vps75 stimulates acetylation of H3 by Rtt10910; however, unlike Asf1, it is critical for H3-K9ac but not for H3-K56ac, and can also facilitate acetylation of K23 and K27.","type":"Introduction"},{"text":"Vps75 promotes acetylation of K9 via a two-fold mechanism, which differs from a classical interaction between folded and unfolded protein domains. First, the Vps75 dimer acts as a binding platform for both the Asf1–H3:H4 substrate and the Rtt109 enzyme, building a doughnut-like structure with a 25-Å-wide central cavity faced by the Rtt109 catalytic site. Second, the unstructured C-terminal tail of Vps75 (C-terminal acidic domain, CTAD) recruits the similarly unstructured H3 N-terminal tail, containing K9, to this cavity via fuzzy electrostatic interactions. Both the Vps75 CTAD and the H3 N-terminal domain remain disordered, allowing confinement of the H3 tail in proximity to the enzyme active site with minimal entropic penalty.","type":"Introduction"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31387991","version":3,"reference_html":"Histone chaperone exploits intrinsic disorder to switch acetylation specificity. <i> Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T. </i> Nat Commun, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"protein folding chaperone","curator_orcid":"0000-0003-0849-9312","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":559292,"disprot_id":"DP02908","date":"2020-06-15T11:44:35.884Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":3,"name":"Vacuolar protein sorting-associated protein 75","dataset":[],"UniParc":"UPI000013BBD6","uniref100":"UniRef100_P53853","uniref90":"UniRef90_P53853","uniref50":"UniRef50_P53853","genes":[{"name":{"value":"VPS75"},"orfNames":[{"value":"N0890"}],"olnNames":[{"value":"YNL246W"}]}],"alphafold_very_low_content":0.08333333333333333,"disorder_content":0.14772727272727273,"disprot_consensus":{"full":[{"start":226,"end":264,"type":"D"}],"Structural state":[{"start":226,"end":264,"type":"D"}],"Molecular function":[{"start":226,"end":264,"type":"F"}]}},{"acc":"P28023","features":{"pfam":[{"id":"PF01302","name":"CAP-Gly domain","start":29,"end":93},{"id":"PF12455","name":"Dynein associated protein","start":526,"end":804},{"id":"PF26666","name":"Domain of unknown function (DUF8221)","start":948,"end":1033}],"gene3D":[]},"creator":"rpancsa","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"sequence":"MAQSKRHMYNRTPSGSRMSTEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKILKREGADAAAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGPSSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRDQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEAKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGGDHDCVLVLLLMPRLICKAELIRKQAQEKFDLSENCSERPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDVYKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEESTMQLADHIKFTQSALDCMSVEVGRLRAFLQGGQEATDIALLLRDLETSCSDIRQFCKKIRRRMPGTDAPGIPAALAFGSQVSDTLLDCRKHLTWVVAVLQEVAAAAAQLIAPLAENEGLPVAALEELAFKASEQIYGSPSSSPYECLRQSCSILISTMNKLATAMQEGEYDAERPPSKPPPVEPWPAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLEETQTLLRKKEKEFEETMDALQADIDQLEAEKTELKQRLNSQSKRTIEGLRGPPPSGIATLVSGIAGEEQQRGGTPGQAPGALPGPGPVKDSPLLLQQISAMRLHISQLQHENSILRGAQMKASLAALPPLHVAKFSLPPHEGPGGNLLSGALYRKTSQLLEKLNQLSTYTHVVDITRSSPACKSPSAQLMEQVAQLKSLSDTIEKLKDEVLKETVTQRPGATVPTDFATFPSSAFLRAKEEQQDDTVYMGKVTFSCAAGLGQRHRLVLTQEQLHQLHGRLIS","length":1280,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":191,"region_id":"DP02910r001","start":108,"term_id":"IDPO:0000002","statement":[{"text":"In contrast to the CAP-Gly domain, the signals of other domains in the protein are poorly dispersed. This is an indication that the extended region of p150Glued(1–191) comprising the basic and SP-rich domains is much less structured than the CAP-Gly domain and may have a substantial proportion of random coil. ","type":"Results"},{"text":"Our results thus indicate that despite the presence of some secondary structures in these segments, the basic and SP-rich domains are intrinsically disordered and unfolded in\nfree state in solution.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31445682","version":2,"reference_html":"Conformational Flexibility of p150<sup>Glued</sup>(1-191) Subunit of Dynactin Assembled with Microtubules. <i> Guo C, Williams JC, Polenova T. </i> Biophys J, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":191,"region_id":"DP02910r002","start":108,"term_id":"GO:0005515","statement":[{"text":"The binding affinity of monomeric p150Glued(1–191) to polymerized MTs was assessed by co-sedimentation assay (Fig. 1 C). More than 98% of p150Glued(1–191) binds to\nMTs when equivalent molar concentrations of the protein and the tubulin dimer were used (Fig. 1 C). In comparison, as we and others reported previously, under the identical\nconditions, less than half of the CAP-Gly domain protein encompassing residues 19–107 (CAP-Gly19–107) binds to MTs (15). Thus, the binding affinity of p150Glued(1–191) to MTs is significantly higher than that of CAP-Gly(19–107). Th is result validates that p150Glued(1–191) contains a second MT-binding domain other than CAP-Gly, and the\nextended region comprised of the basic domain and SP-rich domain assists the interactions between the p150Glued and MTs.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"co-sedimentation assay evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31445682","version":3,"reference_html":"Conformational Flexibility of p150<sup>Glued</sup>(1-191) Subunit of Dynactin Assembled with Microtubules. <i> Guo C, Williams JC, Polenova T. </i> Biophys J, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001164","term_name":"protein binding","curator_orcid":"0000-0003-0849-9312","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":191,"region_id":"DP02910r003","start":108,"term_id":"GO:0005515","statement":[{"text":"Our results thus indicate that the rigid segments in the basic domain of p150Glued(1–191), S112–R119, A124–R132, and T141–T146, likely comprise most of the residues at the intermolecular interface with MTs (Fig. 7 C). Together with the CAP-Gly domain, they appear to be responsible for the MT-binding interactions of the p150Glued subunit. This finding is consistent with previous studies demonstrating that the basic domain is the second MT-binding segment of p150Glued ","type":"Results"},{"text":"Residues 108–191 of p150Glued(1–191) enhance the binding affinity and contain a second MT-binding region, albeit it is largely unstructured in solution and dynamic upon binding to MTs. Three short and rigid segments in the basic domain, S111–I116, A124–R132, and K144–T146, are predicted to form a-helical and b-sheet structures and are likely to encompass the MT-binding site.","type":"Discussion"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31445682","version":3,"reference_html":"Conformational Flexibility of p150<sup>Glued</sup>(1-191) Subunit of Dynactin Assembled with Microtubules. <i> Guo C, Williams JC, Polenova T. </i> Biophys J, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"protein binding","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":145,"region_id":"DP02910r004","start":115,"term_id":"GO:0060090","statement":[{"text":"As reported previously, the basic domain of p150Glued (residues 115–145) has the ability to bind with MTs in the absence of CAP-Gly domain and to independently skate along MTs in the absence of dynein (16). In addition, this domain enhances dynein processivity\nby fourfold and is responsible for the long-range motility of dynein and its long-time interactions with MTs (16).","type":"Introduction"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31445682","version":3,"reference_html":"Conformational Flexibility of p150<sup>Glued</sup>(1-191) Subunit of Dynactin Assembled with Microtubules. <i> Guo C, Williams JC, Polenova T. </i> Biophys J, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"molecular adaptor activity","curator_orcid":"0000-0003-0849-9312","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":152,"region_id":"DP02910r005","start":132,"term_id":"GO:0098772","statement":[{"text":"More specifically, the K-rich domain (132–152) antagonizes the inhibitory effect of the coiled-coil 1 domain (CC1) (residues 214–547) in the MT-binding affinity of p150Glued (17).","type":"Introduction"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31445682","version":3,"reference_html":"Conformational Flexibility of p150<sup>Glued</sup>(1-191) Subunit of Dynactin Assembled with Microtubules. <i> Guo C, Williams JC, Polenova T. </i> Biophys J, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"molecular function regulator","curator_orcid":"0000-0003-0849-9312","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":18,"region_id":"DP02910r006","start":1,"term_id":"IDPO:0000002","statement":[{"text":"In contrast to the CAP-Gly domain, the signals of other domains in the protein are poorly dispersed. This is an indication that the extended region of p150Glued(1–191) comprising the basic and SP-rich domains is much less structured than the CAP-Gly domain and may have a substantial proportion of random coil.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31445682","version":2,"reference_html":"Conformational Flexibility of p150<sup>Glued</sup>(1-191) Subunit of Dynactin Assembled with Microtubules. <i> Guo C, Williams JC, Polenova T. </i> Biophys J, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":18,"region_id":"DP02910r007","start":1,"term_id":"GO:0060090","statement":[{"text":"We also speculate that the N-terminal tail (1–25) of p150Glued(1–191) may contain\nan anchoring point at residue R11 for interacting with the tubulin’s C-terminal tail (Fig. 7). In a previous study, the N-terminal segment 1–25 has been proposed to secure the\nbinding of CAP-Gly to MTs by wrapping around tubulin’s E-hook (13). According to our results, R11 is the only residue that is detected at 4\u0001C and exhibits strong peak intensity in the segment 1–25, indicating that R11 is possibly involved in binding interactions with tubulin.","type":"Results"},{"text":"In the N-terminal segment of p150Glued (residues 1–144), the N-terminal tail (residues 1–25) and the basic patch (residues 106–144) greatly increase the binding affinity of the\nsegment to MTs, and these patches affect the lateral associations of tubulins by interacting with the tubulin’s E-hook(13).","type":"Introduction"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31445682","version":3,"reference_html":"Conformational Flexibility of p150<sup>Glued</sup>(1-191) Subunit of Dynactin Assembled with Microtubules. <i> Guo C, Williams JC, Polenova T. </i> Biophys J, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"molecular adaptor activity","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":18,"region_id":"DP02910r008","start":1,"term_id":"GO:0005515","statement":[{"text":"We also speculate that the N-terminal tail (1–25) of p150Glued(1–191) may contain\nan anchoring point at residue R11 for interacting with the tubulin’s C-terminal tail (Fig. 7). In a previous study, the N-terminal segment 1–25 has been proposed to secure the\nbinding of CAP-Gly to MTs by wrapping around tubulin’s E-hook (13). According to our results, R11 is the only residue that is detected at 4\u0001C and exhibits strong peak intensity in the segment 1–25, indicating that R11 is possibly involved in binding interactions with tubulin.","type":"Results"},{"text":"In the N-terminal segment of p150Glued (residues 1–144), the N-terminal tail (residues 1–25) and the basic patch (residues 106–144) greatly increase the binding affinity of the\nsegment to MTs, and these patches affect the lateral associations of tubulins by interacting with the tubulin’s E-hook(13).","type":"Introduction"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31445682","version":3,"reference_html":"Conformational Flexibility of p150<sup>Glued</sup>(1-191) Subunit of Dynactin Assembled with Microtubules. <i> Guo C, Williams JC, Polenova T. </i> Biophys J, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"protein binding","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":10116,"disprot_id":"DP02910","date":"2020-06-15T14:06:11.284Z","organism":"Rattus norvegicus","regions_counter":8,"name":"Dynactin subunit 1","dataset":[],"UniParc":"UPI0000129A27","uniref100":"UniRef100_P28023","uniref90":"UniRef90_Q14203-6","uniref50":"UniRef50_Q14203","genes":[{"name":{"value":"Dctn1"}}],"alphafold_very_low_content":0.1609375,"disorder_content":0.0796875,"disprot_consensus":{"full":[{"start":1,"end":18,"type":"D"},{"start":108,"end":191,"type":"D"}],"Structural state":[{"start":1,"end":18,"type":"D"},{"start":108,"end":191,"type":"D"}],"Molecular function":[{"start":1,"end":18,"type":"F"},{"start":108,"end":191,"type":"F"}]}},{"acc":"Q8N3V7","features":{"pfam":[],"gene3D":[]},"creator":"rpancsa","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MLGPHLPPPPLAPSEGRPTPCAFQIPDGSYRCLALEAEESSGEEGLQGEVGPTDLEEDEGVSRSGDDSACRVTQGTPQLPKALGIQPPSCSREEQGASQHDDRASQDWDVVKAGQMMTASPSPGPGPRVAQKPALGRSTSLTEKDLKEAKARSQQIAAQLTTPPSSNSRGVQLFNRRRQRVNEFTLESHGQRGQKPSQESLRVLPSSLPGHAPGLSLSSTSLPEPGPPRHPSPQSPDRGVPGHSMEGYSEEASLLRHLEKVASEEEEVPLVVYLKENAALLTANGLHLSQNREAQQSSPAPPPAEVHSPAADVNQNLASPSATLTTPTSNSSHNPPATDVNQNPPATVVPQSLPLSSIQQNSSEAQLPSNGTGPASKPSTLCADGQPQAPAEEVRCSTLLIDKVSTPATTTSTFSREATLIPSSRPPASDFMSSSLLIDIQPNTLVVSADQEMSGRAAATTPTKVYSEVHFTLAKPPSVVNRTARPFGIQAPGGTSQMERSPMLERRHFGEKAPAPQPPSLPDRSPRPQRHIMSRSPMVERRMMGQRSPASERRPLGNFTAPPTYTETLSTAPLASWVRSPPSYSVLYPSSDPKSSHLKGQAVPASKTGILEESMARRGSRKSMFTFVEKPKVTPNPDLLDLVQTADEKRRQRDQGEVGVEEEPFALGAEASNFQQEPAPRDRASPAAAEEVVPEWASCLKSPRIQAKPKPKPNQNLSEASGKGAELYARRQSRMEKYVIESSSHTPELARCPSPTMSLPSSWKYPTNAPGAFRVASRSPARTPPASLYHGYLPENGVLRPEPTKQPPYQLRPSLFVLSPIKEPAKVSPRAASPAKPSSLDLVPNLPKGALPPSPALPRPSRSSPGLYTSPGQDSLQPTAVSPPYGGDISPVSPSRAWSPRAKQAPRPSFSTRNAGIEAQVWKPSFCFK","length":929,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":613,"region_id":"DP02911r001","start":545,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"To determine if SYNPO545-613 is disordered as predicted, we used far UV CD and NMR spectroscopy to investigate the solution structure of the polypeptide. A strong negative\nsignal at 200 nm in the far UV CD spectrum (Fig. 1B) and limited dispersion in the amide proton region of the 1H-15N HSQC spectrum (Fig. 1C) are consistent with a primarily disordered protein.","type":"Results"}],"curator_id":"rpancsa","released":"2023_12","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31597702","version":2,"reference_html":"Intrinsic disorder and amino acid specificity modulate binding of the WW2 domain in kidney and brain protein (KIBRA) to synaptopodin. <i> Kwok E, Rodriguez DJ, Kremerskothen J, Nyarko A. </i> J Biol Chem, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:34:06.995Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":613,"region_id":"DP02911r002","start":545,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"To determine if SYNPO545-613 is disordered as predicted, we used far UV CD and NMR spectroscopy to investigate the solution structure of the polypeptide. A strong negative\nsignal at 200 nm in the far UV CD spectrum (Fig. 1B) and limited dispersion in the amide proton region of the 1H-15N HSQC spectrum (Fig. 1C) are consistent with a primarily disordered protein.","type":"Results"}],"curator_id":"rpancsa","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31597702","version":2,"reference_html":"Intrinsic disorder and amino acid specificity modulate binding of the WW2 domain in kidney and brain protein (KIBRA) to synaptopodin. <i> Kwok E, Rodriguez DJ, Kremerskothen J, Nyarko A. </i> J Biol Chem, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:34:07.949Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02911r003","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:34:17.467Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":613,"term_id":"GO:0005515","start":545,"version":3,"statement":[{"text":"Isothermal titration calorimetry and CD experiments revealed that the interactions of the disordered WW2 domain with SYNPO are significantly weaker than SYNPO's interactions with the well-folded WW1 domain and that an I81W substitution in the WW2 domain neither enhances binding affinity nor induces substantial WW2 domain folding.","type":"Abstract"},{"text":"These analyses also disclosed that SYNPO binds the tandem WW domain polypeptide in an antiparallel manner, that is, the WW1 domain binds the second PPXY motif of SYNPO.","type":"Abstract"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q8IX03","partner_end":null}],"term_name":"protein binding","ec_name":"isothermal titration calorimetry evidence used in manual assertion","released":"2023_12","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31597702","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"rpancsa","reference_html":"Intrinsic disorder and amino acid specificity modulate binding of the WW2 domain in kidney and brain protein (KIBRA) to synaptopodin. <i> Kwok E, Rodriguez DJ, Kremerskothen J, Nyarko A. </i> J Biol Chem, 2019","curator_orcid":"0000-0003-0849-9312","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":929,"reference_id":"28510039","reference_source":"pmid","reference_html":"Synaptopodin family of natively unfolded, actin binding proteins: physical properties and potential biological functions. <i> Chalovich JM, Schroeter MM. </i> Biophys Rev, 2010","date":"2022-11-07T19:18:06.732Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP02911r005","statement":[{"text":"Synaptopodin family of natively unfolded, actin binding proteins: physical properties and potential biological functions","type":"Title"},{"text":"Critical to the understanding of the function of synaptopodin’s is the appreciation of the fact that they have little secondary or tertiary structure under native conditions.","type":"Article"}]}],"released":"2023_12","ncbi_taxon_id":9606,"disprot_id":"DP02911","date":"2020-06-15T16:34:18.747Z","organism":"Homo sapiens","regions_counter":5,"name":"Synaptopodin","dataset":[],"UniParc":"UPI000006CF19","uniref100":"UniRef100_Q8N3V7","uniref90":"UniRef90_Q8N3V7","uniref50":"UniRef50_Q8CC35","genes":[{"name":{"value":"SYNPO"},"synonyms":[{"value":"KIAA1029"}]}],"alphafold_very_low_content":0.6340150699677072,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":929,"type":"D"}],"Structural state":[{"start":1,"end":929,"type":"D"}],"Molecular function":[{"start":545,"end":613,"type":"F"}]}},{"acc":"P04004","features":{"pfam":[{"id":"PF00045","name":"Hemopexin","start":161,"end":203},{"id":"PF00045","name":"Hemopexin","start":206,"end":251},{"id":"PF00045","name":"Hemopexin","start":267,"end":289},{"id":"PF00045","name":"Hemopexin","start":432,"end":472},{"id":"PF01033","name":"Somatomedin B domain","start":22,"end":60}],"gene3D":[]},"creator":"rpancsa","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MAPLRPLLILALLAWVALADQESCKGRCTEGFNVDKKCQCDELCSYYQSCCTDYTAECKPQVTRGDVFTMPEDEYTVYDDGEEKNNATVHEQVGGPSLTSDLQAQSKGNPEQTPVLKPEEEAPAPEVGASKPEGIDSRPETLHPGRPQPPAEEELCSGKPFDAFTDLKNGSLFAFRGQYCYELDEKAVRPGYPKLIRDVWGIEGPIDAAFTRINCQGKTYLFKGSQYWRFEDGVLDPDYPRNISDGFDGIPDNVDAALALPAHSYSGRERVYFFKGKQYWEYQFQHQPSQEECEGSSLSAVFEHFAMMQRDSWEDIFELLFWGRTSAGTRQPQFISRDWHGVPGQVDAAMAGRIYISGMAPRPSLAKKQRFRHRNRKGYRSQRGHSRGRNQNSRRPSRATWLSLFSSEESNLGANNYDDYRMDWLVPATCEPIQSVFFFSGDKYYRVNLRTRRVDTVDPPYPRSIAQYWLGCPAPGHL","length":478,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":130,"region_id":"DP02913r001","start":48,"term_id":"IDPO:0000002","statement":[{"text":"We utilized far-UV CD to study the effect of osmotic pressure on secondary structure within the IDD. Ethylene glycol (EG) and polyethylene glycol (PEG)-400 were employed to test for structural changes within the IDD that may be induced by changes in osmotic pressure. The results indicated that the SMBIDD fragment alone exhibited ellipticity characteristic of a protein fold devoid of classical secondary structure elements (Figure 2a).","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31793295","version":2,"reference_html":"Characterization of an Extensive Interface on Vitronectin for Binding to Plasminogen Activator Inhibitor-1: Adoption of Structure in an Intrinsically Disordered Region. <i> Puster LO, Stanley CB, Uversky VN, Curtis JE, Krueger S, Chu Y, Peterson CB. </i> Biochemistry, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"disorder","validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-05-03T14:59:53.506Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":130,"region_id":"DP02913r002","start":1,"term_id":"IDPO:0000002","statement":[{"text":"This analysis indicates that the isolated SMB-IDD is a significantly flexible structure, existing over a relatively broad Rg range of ~20-55 Å","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"small-angle neutron scattering evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31793295","version":2,"reference_html":"Characterization of an Extensive Interface on Vitronectin for Binding to Plasminogen Activator Inhibitor-1: Adoption of Structure in an Intrinsically Disordered Region. <i> Puster LO, Stanley CB, Uversky VN, Curtis JE, Krueger S, Chu Y, Peterson CB. </i> Biochemistry, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006214","term_name":"disorder","validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-05-03T15:02:10.913Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":130,"region_id":"DP02913r003","start":1,"term_id":"GO:0060090","statement":[{"text":"Our prior work using hydrodynamic methods with PAI-1 and full-length vitronectin demonstrated that there is a 2:1 (PAI-1:vitronectin) stoichiometry of interaction that leads to assembly of higher-order oligomeric complexes via a prominent intermediate containing four PAI-1 and two vitronectin molecules.","type":"Results"},{"text":"Calculated structures for the PAI-1:SMBIDD complex suggest that the IDD provides an interaction surface outside of the primary PAI-1-binding site located within the SMB domain; this binding is proposed to lead to the assembly of higher-order structures of vitronectin and PAI-1 commonly found in tissues.","type":"Abstract"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31793295","version":3,"reference_html":"Characterization of an Extensive Interface on Vitronectin for Binding to Plasminogen Activator Inhibitor-1: Adoption of Structure in an Intrinsically Disordered Region. <i> Puster LO, Stanley CB, Uversky VN, Curtis JE, Krueger S, Chu Y, Peterson CB. </i> Biochemistry, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"molecular adaptor activity","validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-05-03T15:06:22.501Z"},"curator_orcid":"0000-0003-0849-9312","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":130,"region_id":"DP02913r004","start":1,"term_id":"GO:0005515","statement":[{"text":"Analysis of the SANS data using the Ensemble Optimization Method confirms that the SMBIDD adopts a more compact configuration when bound to PAI-1. Calculated structures for the PAI-1:SMBIDD complex suggest that the IDD provides an interaction surface outside of the primary PAI-1-binding site located within the SMB domain","type":"Abstract"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"small-angle neutron scattering evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31793295","version":3,"reference_html":"Characterization of an Extensive Interface on Vitronectin for Binding to Plasminogen Activator Inhibitor-1: Adoption of Structure in an Intrinsically Disordered Region. <i> Puster LO, Stanley CB, Uversky VN, Curtis JE, Krueger S, Chu Y, Peterson CB. </i> Biochemistry, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006214","term_name":"protein binding","validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-05-03T15:05:53.560Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":130,"region_id":"DP02913r005","start":1,"term_id":"IDPO:0000011","statement":[{"text":"Analysis of the SANS data using the Ensemble Optimization Method confirms that the SMBIDD adopts a more compact configuration when bound to PAI-1. ","type":"Abstract"},{"text":"We compared the Rg values for free vs. bound SMB-IDD and observed that PAI-1 binding yields a shift in the Rg range for the SMB-IDD to predominantly lower values, consistent with a solution structure for the IDD that is restricted in conformation upon binding","type":"Results"},{"text":"In a series of SANS experiments to test for structural changes in the SMB-IDD, it was observed that PAI-1 binding led to structural reorganization of the IDD into a more compact structure. This result localizes an additional binding site for PAI-1 to the linker region in vitronectin.","type":"Discussion"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"small-angle neutron scattering evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31793295","version":2,"reference_html":"Characterization of an Extensive Interface on Vitronectin for Binding to Plasminogen Activator Inhibitor-1: Adoption of Structure in an Intrinsically Disordered Region. <i> Puster LO, Stanley CB, Uversky VN, Curtis JE, Krueger S, Chu Y, Peterson CB. </i> Biochemistry, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006214","term_name":"disorder to order","validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-05-03T15:03:48.278Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":71,"region_id":"DP02913r006","start":1,"term_id":"GO:0005515","statement":[{"text":"To localize the putative binding site, we constructed a truncated form of vitronectin containing 71 amino acids from the N-terminus, including the SMB domain and an additional 24 amino acids from the IDD region. This portion of the IDD is rich in acidic amino acids, which are hypothesized to be complementary to several basic residues identified within an extensive vitronectin-binding site mapped on PAI-1 (Schar, Jensen, Christensen, Blouse, Andreasen, Peterson. J Biol Chem. 2008;283:10297-10309). Steady-state and stopped-flow fluorescence measurements demonstrate that the truncated form of vitronectin exhibits the same rapid biphasic association as full-length vitronectin and that the IDD hosts the elusive second PAI-1 binding site that lies external to the SMB domain of vitronectin. ","type":"Abstract"}],"curator_id":"esalladini","released":"2022_03","ec_name":"fluorescence polarization evidence used in manual assertion","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"31682300","version":4,"reference_html":"Identification of a PAI-1-binding site within an intrinsically disordered region of vitronectin. <i> Chu Y, Bucci JC, Peterson CB. </i> Protein Sci, 2020","date":"2022-03-08T14:11:03.795Z","reference_source":"pmid","ec_id":"ECO:0006277","term_name":"protein binding","curator_orcid":"0000-0002-5152-5953","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P05121","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-08T18:11:40.021Z"}},{"start":59,"end":70,"reference_id":"12808446","reference_source":"pmid","reference_html":"How vitronectin binds PAI-1 to modulate fibrinolysis and cell migration. <i> Zhou A, Huntington JA, Pannu NS, Carrell RW, Read RJ. </i> Nat Struct Biol, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1OC0"}],"region_id":"DP02913r007","statement":[{"text":"Dashed lines indicate disordered residues in the reactive center loop (RCL) of PAI-1 and residues leading to the RGD sequence of somatomedin B.","type":"Figure"},{"text":"The final model includes residues 6–337 and 348–379 of PAI-1 and 3–39 of SMB.","type":"Methods"},{"text":"In a complex with PAI-1, the RGD sequence (residues 45–47 of the somatomedin B domain, Fig. 1b,c) will be positioned close to PAI-1, together with the rest of the large vitronectin molecule, leaving insufficient room for the RGD sequence to bind to integrins in the manner seen in the recent crystal structure of the integrin–RGD ligand complex","type":"Discussion"},{"text":"The numbering of the IDR that includes the RGD motif (64-66) of vitronectin, correspond to region 59-70 of the associated UniProt sequence, since PDB:1OC0 spans residues 20-70 of the protein.","type":"Curator statement"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-04-30T08:53:15.132Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":22,"end":58,"reference_id":"12808446","reference_source":"pmid","reference_html":"How vitronectin binds PAI-1 to modulate fibrinolysis and cell migration. <i> Zhou A, Huntington JA, Pannu NS, Carrell RW, Read RJ. </i> Nat Struct Biol, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"1OC0"}],"interaction_partner":[{"db":"UniProt","id":"P05121","partner_start":null,"partner_end":null}],"region_id":"DP02913r008","statement":[{"text":"The interaction of the plasma protein vitronectin with plasminogen activator inhibitor-1 (PAI-1) is central to human health. Vitronectin binding extends the lifetime of active PAI-1, which controls hemostasis by inhibiting fibrinolysis and has also been implicated in angiogenesis. The PAI-1–vitronectin binding interaction also affects cell adhesion and motility. For these reasons, elevated PAI-1 activities are associated both with coronary thrombosis and with a poor prognosis in many cancers. Here we show the crystal structure at a resolution of 2.3 Å of the complex of the somatomedin B domain of vitronectin with PAI-1. The structure of the complex explains how vitronectin binds to and stabilizes the active conformation of PAI-1. It also explains the tissue effects of PAI-1, as PAI-1 competes for and sterically blocks the interaction of vitronectin with cell surface receptors and integrins.","type":"Abstract"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-05-03T14:32:04.314Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":22,"end":58,"reference_id":"12808446","reference_source":"pmid","reference_html":"How vitronectin binds PAI-1 to modulate fibrinolysis and cell migration. <i> Zhou A, Huntington JA, Pannu NS, Carrell RW, Read RJ. </i> Nat Struct Biol, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1OC0"}],"region_id":"DP02913r009","statement":[{"text":"The interaction of the plasma protein vitronectin with plasminogen activator inhibitor-1 (PAI-1) is central to human health. Vitronectin binding extends the lifetime of active PAI-1, which controls hemostasis by inhibiting fibrinolysis and has also been implicated in angiogenesis. The PAI-1–vitronectin binding interaction also affects cell adhesion and motility. For these reasons, elevated PAI-1 activities are associated both with coronary thrombosis and with a poor prognosis in many cancers. Here we show the crystal structure at a resolution of 2.3 Å of the complex of the somatomedin B domain of vitronectin with PAI-1. The structure of the complex explains how vitronectin binds to and stabilizes the active conformation of PAI-1. It also explains the tissue effects of PAI-1, as PAI-1 competes for and sterically blocks the interaction of vitronectin with cell surface receptors and integrins.","type":"Abstract"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-05-03T14:31:07.459Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":22,"end":58,"reference_id":"12808446","reference_source":"pmid","reference_html":"How vitronectin binds PAI-1 to modulate fibrinolysis and cell migration. <i> Zhou A, Huntington JA, Pannu NS, Carrell RW, Read RJ. </i> Nat Struct Biol, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP02913r010","statement":[{"text":"The interaction of the plasma protein vitronectin with plasminogen activator inhibitor-1 (PAI-1) is central to human health. Vitronectin binding extends the lifetime of active PAI-1, which controls hemostasis by inhibiting fibrinolysis and has also been implicated in angiogenesis. The PAI-1–vitronectin binding interaction also affects cell adhesion and motility. For these reasons, elevated PAI-1 activities are associated both with coronary thrombosis and with a poor prognosis in many cancers. Here we show the crystal structure at a resolution of 2.3 Å of the complex of the somatomedin B domain of vitronectin with PAI-1. The structure of the complex explains how vitronectin binds to and stabilizes the active conformation of PAI-1. It also explains the tissue effects of PAI-1, as PAI-1 competes for and sterically blocks the interaction of vitronectin with cell surface receptors and integrins.","type":"Abstract"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-05-03T14:32:11.215Z"},"ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02913","date":"2020-06-15T17:21:41.004Z","organism":"Homo sapiens","regions_counter":10,"name":"Vitronectin","dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000138E65","uniref100":"UniRef100_P04004","uniref90":"UniRef90_P04004","uniref50":"UniRef50_P04004","genes":[{"name":{"value":"VTN"}}],"alphafold_very_low_content":0.3075313807531381,"disorder_content":0.2719665271966527,"disprot_consensus":{"full":[{"start":1,"end":130,"type":"T"}],"Structural state":[{"start":1,"end":130,"type":"D"}],"Molecular function":[{"start":1,"end":130,"type":"F"}],"Structural transition":[{"start":1,"end":130,"type":"T"}]}},{"acc":"P48443","features":{"pfam":[{"id":"PF00104","name":"Ligand-binding domain of nuclear hormone receptor","start":258,"end":442},{"id":"PF00105","name":"Double treble clef zinc finger, C4 type","start":138,"end":206},{"id":"PF11825","name":"Nuclear/hormone receptor activator site AF-1","start":25,"end":134}],"gene3D":[]},"creator":"rpancsa","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MYGNYSHFMKFPAGYGGSPGHTGSTSMSPSAALSTGKPMDSHPSYTDTPVSAPRTLSAVGTPLNALGSPYRVITSAMGPPSGALAAPPGINLVAPPSSQLNVVNSVSSSEDIKPLPGLPGIGNMNYPSTSPGSLVKHICAICGDRSSGKHYGVYSCEGCKGFFKRTIRKDLIYTCRDNKDCLIDKRQRNRCQYCRYQKCLVMGMKREAVQEERQRSRERAESEAECATSGHEDMPVERILEAELAVEPKTESYGDMNMENSTNDPVTNICHAADKQLFTLVEWAKRIPHFSDLTLEDQVILLRAGWNELLIASFSHRSVSVQDGILLATGLHVHRSSAHSAGVGSIFDRVLTELVSKMKDMQMDKSELGCLRAIVLFNPDAKGLSNPSEVETLREKVYATLEAYTKQKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLETPLQIT","length":463,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":127,"region_id":"DP02915r001","start":2,"term_id":"IDPO:0000002","statement":[{"text":"The obtained  CD  spectrum  of AB_hRXG is  typical for proteins  containing  disordered  regions (Figure 4A). It is characterized by a deep minimum at 200 nm and a lack of distinct minima at 208 nm and 222 nm, with only a shallow minimum at 222 nm, which suggests the existence of  some secondary structure.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31881311","version":2,"reference_html":"Ordered structure-forming properties of the intrinsically disordered AB region of hRXRγ and its ability to promote liquid-liquid phase separation. <i> Sołtys K, Ożyhar A. </i> J Steroid Biochem Mol Biol, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:44:45.516Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":127,"region_id":"DP02915r002","start":2,"term_id":"IDPO:0000002","statement":[{"text":"The remarkably bigger experimental Rs in comparison to the theoretical value places AB_hRXG on the  log (Rs)  versus  log (M)  plot  in the  area for IDPs with  PMG-like  properties (Figure 5B).","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"chromatography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31881311","version":2,"reference_html":"Ordered structure-forming properties of the intrinsically disordered AB region of hRXRγ and its ability to promote liquid-liquid phase separation. <i> Sołtys K, Ożyhar A. </i> J Steroid Biochem Mol Biol, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:44:44.484Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":127,"region_id":"DP02915r003","start":2,"term_id":"IDPO:0000004","statement":[{"text":"The remarkably bigger experimental Rs in comparison to the theoretical value places AB_hRXG on the  log (Rs)  versus  log (M)  plot  in the  area for IDPs with  PMG-like  properties (Figure 5B).","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"chromatography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31881311","version":2,"reference_html":"Ordered structure-forming properties of the intrinsically disordered AB region of hRXRγ and its ability to promote liquid-liquid phase separation. <i> Sołtys K, Ożyhar A. </i> J Steroid Biochem Mol Biol, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:44:43.907Z","curator_name":"Federica Quaglia"},"term_name":"pre-molten globule","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":127,"region_id":"DP02915r004","start":2,"term_id":"IDPO:0000004","statement":[{"text":"The estimated molecular mass (13 490 Da, 13 260 Da and 13108  Da)  was  close  to the  theoretical  value  (14054Da)  and the  c(s)  distribution obtained for different protein concentration overlaps, indicating that AB_hRXG is a monomer with a highly  extended  conformation. The  obtained  Stokes  radii  (Rs)  for the different concentrations  of AB_hRXG (28.6  Å)  were in good  agreement  with the SEC  data  (27.5  Å).","type":"Results"},{"text":"The calculated f/f0ratio for AB_hRXG is 1.8 (Table 2), which indicates an extended conformation and again classifies AB_hRXGto the PMG-like IDPs.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"analytical ultracentrifugation evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31881311","version":2,"reference_html":"Ordered structure-forming properties of the intrinsically disordered AB region of hRXRγ and its ability to promote liquid-liquid phase separation. <i> Sołtys K, Ożyhar A. </i> J Steroid Biochem Mol Biol, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006275","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:44:43.060Z","curator_name":"Federica Quaglia"},"term_name":"pre-molten globule","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":127,"region_id":"DP02915r005","start":2,"term_id":"IDPO:0000002","statement":[{"text":"AB_hRXG in the absence of osmolyte appearedto be very sensitive to trypsin (Figure 7;  lines  6,  10  and  14)  and  proteinase  K  digestion","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"cleavage assay evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31881311","version":2,"reference_html":"Ordered structure-forming properties of the intrinsically disordered AB region of hRXRγ and its ability to promote liquid-liquid phase separation. <i> Sołtys K, Ożyhar A. </i> J Steroid Biochem Mol Biol, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:44:42.401Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":127,"region_id":"DP02915r006","start":2,"term_id":"GO:0140693","statement":[{"text":"Taken  together,  the  data  show  that  AB_hRXG exhibits the ability  to  promote the formation of LLPS and that the process is concentration-and temperature-dependent.","type":"Results"},{"text":"To observe the formation of liquid droplets, a concentration of around 3 mg/ml and higher was needed.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"microscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31881311","version":3,"reference_html":"Ordered structure-forming properties of the intrinsically disordered AB region of hRXRγ and its ability to promote liquid-liquid phase separation. <i> Sołtys K, Ożyhar A. </i> J Steroid Biochem Mol Biol, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001232","validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:44:41.907Z","curator_name":"Federica Quaglia"},"term_name":"molecular condensate scaffold activity","curator_orcid":"0000-0003-0849-9312","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02915","date":"2020-06-16T07:13:24.386Z","organism":"Homo sapiens","regions_counter":6,"name":"Retinoic acid receptor RXR-gamma","dataset":["Condensates-related proteins"],"UniParc":"UPI000004989F","uniref100":"UniRef100_P48443","uniref90":"UniRef90_P48443","uniref50":"UniRef50_P48443","genes":[{"name":{"value":"RXRG"},"synonyms":[{"value":"NR2B3"}]}],"alphafold_very_low_content":0.31533477321814257,"disorder_content":0.27213822894168466,"disprot_consensus":{"full":[{"start":2,"end":127,"type":"D"}],"Structural state":[{"start":2,"end":127,"type":"D"}],"Molecular function":[{"start":2,"end":127,"type":"F"}]}},{"acc":"Q14444","features":{"pfam":[{"id":"PF12287","name":"Cytoplasmic activation/proliferation-associated protein-1 C term","start":359,"end":685},{"id":"PF18293","name":"Caprin-1 dimerization domain","start":132,"end":247}],"gene3D":[]},"creator":"rpancsa","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MPSATSHSGSGSKSSGPPPPSGSSGSEAAAGAGAAAPASQHPATGTGAVQTEAMKQILGVIDKKLRNLEKKKGKLDDYQERMNKGERLNQDQLDAVSKYQEVTNNLEFAKELQRSFMALSQDIQKTIKKTARREQLMREEAEQKRLKTVLELQYVLDKLGDDEVRTDLKQGLNGVPILSEEELSLLDEFYKLVDPERDMSLRLNEQYEHASIHLWDLLEGKEKPVCGTTYKVLKEIVERVFQSNYFDSTHNHQNGLCEEEEAASAPAVEDQVPEAEPEPAEEYTEQSEVESTEYVNRQFMAETQFTSGEKEQVDEWTVETVEVVNSLQQQPQAASPSVPEPHSLTPVAQADPLVRRQRVQDLMAQMQGPYNFIQDSMLDFENQTLDPAIVSAQPMNPTQNMDMPQLVCPPVHSESRLAQPNQVPVQPEATQVPLVSSTSEGYTASQPLYQPSHATEQRPQKEPIDQIQATISLNTDQTTASSSLPAASQPQVFQAGTSKPLHSSGINVNAAPFQSMQTVFNMNAPVPPVNEPETLKQQNQYQASYNQSFSSQPHQVEQTELQQEQLQTVVGTYHGSPDQSHQVTGNHQQPPQQNTGFPRSNQPYYNSRGVSRGGSRGARGLMNGYRGPANGFRGGYDGYRPSFSNTPNSGYTQSQFSAPRDYSGYQRDGYQQNFKRGSGQSGPRGAPRGRGGPPRPNRGMPQMNTQQVN","length":709,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":709,"region_id":"DP02916r001","start":607,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"To address these questions, we first reconstituted a model biomolecular condensate containing the intrinsically disordered C-terminal regions of FMRP (445–632, hereafter referredto as FMRP) and CAPRIN1 (607–709, hereafter referred to as CAPRIN1) for biophysical studies.","type":"Introduction"},{"text":"Figure 2  Solution-state NMR spectra of [13C,15N]CAPRIN1 inFMRP or pFMRP condensed phases. Disordered nature inferred from figure by the annotator.","type":"Figure"}],"curator_id":"rpancsa","released":"2023_06","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31439799","version":2,"reference_html":"Phospho-dependent phase separation of FMRP and CAPRIN1 recapitulates regulation of translation and deadenylation. <i> Kim TH, Tsang B, Vernon RM, Sonenberg N, Kay LE, Forman-Kay JD. </i> Science, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T17:21:29.963Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":709,"region_id":"DP02916r002","start":607,"term_id":"GO:0140693","unpublished":true,"statement":[{"text":"Phosphorylation acts as switch for FMRP-CAPRIN1 co–phase separation and a determinant of subcompartmentalization with RNA.(A) Phase diagram for FMRP andpYCAPRIN1 co–phase separation","type":"Figure"},{"text":"Phase diagram for co–phaseseparation of pFMRP and CAPRIN1. Teal dots represent conditions with observable droplet formation.","type":"Figure"},{"text":"The Tyr residues in these regions of CAPRIN1 are known to be phosphorylated in vivo (22), which is suggestive of their regulatory function. When we Tyr-phosphorylated CAPRIN1 in vitro (pYCAPRIN1;fig. S3, C and D), we found that pYCAPRIN1co–phase-separates with FMRP but not with pFMRP","type":"Results"},{"text":"Overlay of CON spectra of [13C,15N]CAPRIN1 in FMRP (green) or in pFMRP (purple) condensed phases. (C) Examples of reduced intensities or small CSPs of arginine (1, 2) and aromatic (3) residues from the CON spectra","type":"Results"}],"curator_id":"rpancsa","released":"2023_06","ec_name":"fluorescence microscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31439799","version":3,"reference_html":"Phospho-dependent phase separation of FMRP and CAPRIN1 recapitulates regulation of translation and deadenylation. <i> Kim TH, Tsang B, Vernon RM, Sonenberg N, Kay LE, Forman-Kay JD. </i> Science, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006323","term_name":"molecular condensate scaffold activity","curator_orcid":"0000-0003-0849-9312","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-12T14:41:00.951Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q06787","partner_end":null}],"ec_ontology":"ECO","end":709,"region_id":"DP02916r003","start":607,"term_id":"GO:0005515","unpublished":true,"statement":[{"text":" CAPRIN1 binds pFMRP with a medium(~5) and high (~9) number of phosphorylation sites with apparent affinities of 16.1 ± 4.4mMand 5.8 ± 0.4mM, respectively. Error bars denote SD. (C) Phase diagram for co–phaseseparation of pFMRP and CAPRIN1","type":"Figure"}],"curator_id":"rpancsa","released":"2023_06","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31439799","version":3,"reference_html":"Phospho-dependent phase separation of FMRP and CAPRIN1 recapitulates regulation of translation and deadenylation. <i> Kim TH, Tsang B, Vernon RM, Sonenberg N, Kay LE, Forman-Kay JD. </i> Science, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001183","term_name":"protein binding","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T17:21:31.829Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q06787","partner_end":null}],"ec_ontology":"ECO","end":709,"region_id":"DP02916r004","start":607,"term_id":"GO:0005515","unpublished":true,"statement":[{"text":"Using isothermal titration calorimetry (ITC), we detected no FMRP-CAPRIN1 interaction; however,after in vitro phosphorylation of FMRP (pFMRP;fig. S3, A and B) by casein kinase II (CK2), a known kinase that Ser/Thr-phosphorylates FMRP in vivo (22,23), we observed an effective 1 micromolar CAPRIN1-pFMRP binding affinity.","type":"Results"}],"curator_id":"rpancsa","released":"2023_06","ec_name":"isothermal titration calorimetry evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31439799","version":3,"reference_html":"Phospho-dependent phase separation of FMRP and CAPRIN1 recapitulates regulation of translation and deadenylation. <i> Kim TH, Tsang B, Vernon RM, Sonenberg N, Kay LE, Forman-Kay JD. </i> Science, 2019","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005647","term_name":"protein binding","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T17:21:32.849Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2023_06","ncbi_taxon_id":9606,"disprot_id":"DP02916","date":"2020-06-16T08:06:04.576Z","organism":"Homo sapiens","regions_counter":4,"name":"Caprin-1","dataset":["NDDs-related proteins","Condensates-related proteins"],"UniParc":"UPI0000130F9E","uniref100":"UniRef100_Q14444","uniref90":"UniRef90_Q14444","uniref50":"UniRef50_Q14444","genes":[{"name":{"value":"CAPRIN1"},"synonyms":[{"value":"GPIAP1"},{"value":"GPIP137"},{"value":"M11S1"},{"value":"RNG105"}]}],"alphafold_very_low_content":0.6276445698166432,"disorder_content":0.14527503526093088,"disprot_consensus":{"full":[{"start":607,"end":709,"type":"D"}],"Structural state":[{"start":607,"end":709,"type":"D"}],"Molecular function":[{"start":607,"end":709,"type":"F"}]}},{"acc":"Q02521","features":{"pfam":[{"id":"PF12656","name":"G-patch domain","start":93,"end":152}],"gene3D":[]},"creator":"rpancsa","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"sequence":"MSKFSLKLGSKTLKKNISKKTKKKNSLQKANLFDWDDAETASLSHKPQSKIKIQSIDKFDLDEESSSKKKLVIKLSENADTKKNDAPLVEYVTEKEYNEVPVEEFGDALLRGMGWESDSEQDSKGDKTQSRNKDVSNVSQIHPDGLGIGAKLNKAINVEEASFMPVVKIDKITGTKVDDDKKNKS","length":185,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":185,"region_id":"DP02917r001","start":10,"term_id":"IDPO:0000002","statement":[{"text":"Size exclusion chromatography of scSpp2(10–185) resulted in an apparent molecular mass of approximately 65 kDa, roughly three times higher than the calculated molecular mass of scSpp2(10–185). In contrast, multiangle light scattering identified this truncated Spp2 as a monomer, indicating that the protein behaves like a partially or fully unfolded protein.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"chromatography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31974312","version":2,"reference_html":"Structural analysis of the intrinsically disordered splicing factor Spp2 and its binding to the DEAH-box ATPase Prp2. <i> Hamann F, Schmitt A, Favretto F, Hofele R, Neumann P, Xiang S, Urlaub H, Zweckstetter M, Ficner R. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":150,"region_id":"DP02917r002","start":10,"term_id":"IDPO:0000002","statement":[{"text":"In addition, CD measurements were performed with scSpp2(10–150) as well as with the further truncated version scSpp2(100–150) containing only the G-patch region. The CD spectra clearly show the absence of stable secondary structure elements for both samples","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"far-UV circular dichroism evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31974312","version":2,"reference_html":"Structural analysis of the intrinsically disordered splicing factor Spp2 and its binding to the DEAH-box ATPase Prp2. <i> Hamann F, Schmitt A, Favretto F, Hofele R, Neumann P, Xiang S, Urlaub H, Zweckstetter M, Ficner R. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":185,"region_id":"DP02917r003","start":10,"term_id":"IDPO:0000002","statement":[{"text":"To study the properties of scSpp2 in more detail, a heteronuclear singular quantum coherence (HSQC) NMR spectrum of 15N-labeled scSpp2(10–185) was recorded (Fig. 1C). The NMR spectrum was of high quality with a narrow distribution of the cross peaks around 8 ppm of the 1H frequency, which is typical for the spectra of intrinsically disordered proteins.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31974312","version":2,"reference_html":"Structural analysis of the intrinsically disordered splicing factor Spp2 and its binding to the DEAH-box ATPase Prp2. <i> Hamann F, Schmitt A, Favretto F, Hofele R, Neumann P, Xiang S, Urlaub H, Zweckstetter M, Ficner R. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":150,"region_id":"DP02917r004","start":100,"term_id":"GO:0005515","statement":[{"text":"Authors performed and infer information on binding using a homologous protein!","type":"Curator statement"},{"text":"Binding experiments of different truncated versions of ctSpp2G-patch show that this N-terminal helix is sufficient for binding to the DEAH-box ATPase and thus likely displays the major anchor point of the G-patch motif.","type":"Discussion"},{"text":"In particular, glycines 223, 226, and 230 of ctSpp2 exhibit conformations allowed only for glycine residues, and mutation to serine strongly weakens the binding of the ctSpp2G-patch to ctPrp2 (SI Appendix, Fig. S7).","type":"Discussion"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31974312","version":3,"reference_html":"Structural analysis of the intrinsically disordered splicing factor Spp2 and its binding to the DEAH-box ATPase Prp2. <i> Hamann F, Schmitt A, Favretto F, Hofele R, Neumann P, Xiang S, Urlaub H, Zweckstetter M, Ficner R. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"protein binding","curator_orcid":"0000-0003-0849-9312","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":150,"region_id":"DP02917r005","start":100,"term_id":"GO:0140677","statement":[{"text":"The Prp2-specific cofactor Spp2 belongs to the family of G-patch–containing proteins. The name-giving glycine-rich patch (G-patch) consists of at least six conserved glycines and was first identified in RNA-associated proteins by bioinformatic analysis (20).","type":"Introduction"},{"text":"Spp2, which stimulates only the RNA-dependent ATPase activity of isolated Prp2 and not any helicase activity (24). Actually, no helicase activity could be observed for isolated Prp2 or the Prp2-Spp2 complex within the spliceosome (25, 26).","type":"Introduction"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"31974312","version":3,"reference_html":"Structural analysis of the intrinsically disordered splicing factor Spp2 and its binding to the DEAH-box ATPase Prp2. <i> Hamann F, Schmitt A, Favretto F, Hofele R, Neumann P, Xiang S, Urlaub H, Zweckstetter M, Ficner R. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006218","term_name":"molecular function activator activity","curator_orcid":"0000-0003-0849-9312","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":110,"region_id":"DP02917r006","start":100,"term_id":"IDPO:0000011","statement":[{"text":"Spp2G-patch is unfolded in solution and only transiently samples an α-helical conformation in its N-terminal part. This N-terminal amphipathic helix stably binds Prp2 mainly via hydrophobic interactions with a conserved hydrophobic patch at the winged-helix (WH) domain. The C-terminal part binds to the RecA2 domain and can adopt two alternative conformations.","type":"Introduction"},{"text":"In all crystal forms of the ctPrp2-ctSpp2211–254 complex, the N-terminal residues 212 to 222 of the G-patch domain form an amphipathic α-helix that is bound to the WH domain (Fig. 2A). The α-helix is terminated by a sharp kink, followed by a region exhibiting an extended conformation reaching the β-hairpin of the RecA2 domain. The C-terminal part of the ctSpp2 G-patch adopts two alternative conformations in the five different crystal structures.","type":"Results"},{"text":"The transition was observed for a homologous protein!","type":"Curator statement"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31974312","version":2,"reference_html":"Structural analysis of the intrinsically disordered splicing factor Spp2 and its binding to the DEAH-box ATPase Prp2. <i> Hamann F, Schmitt A, Favretto F, Hofele R, Neumann P, Xiang S, Urlaub H, Zweckstetter M, Ficner R. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","term_name":"disorder to order","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2021_06","ncbi_taxon_id":559292,"disprot_id":"DP02917","date":"2020-06-16T08:44:17.941Z","organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":6,"name":"Pre-mRNA-splicing factor SPP2","dataset":[],"UniParc":"UPI0000135E65","uniref100":"UniRef100_Q02521","uniref90":"UniRef90_Q02521","uniref50":"UniRef50_Q02521","genes":[{"name":{"value":"SPP2"},"olnNames":[{"value":"YOR148C"}]}],"alphafold_very_low_content":0.10810810810810811,"disorder_content":0.9513513513513514,"disprot_consensus":{"full":[{"start":10,"end":99,"type":"D"},{"start":100,"end":110,"type":"T"},{"start":111,"end":185,"type":"D"}],"Structural state":[{"start":10,"end":185,"type":"D"}],"Molecular function":[{"start":100,"end":150,"type":"F"}],"Structural transition":[{"start":100,"end":110,"type":"T"}]}},{"acc":"P17947","features":{"pfam":[{"id":"PF00178","name":"Ets-domain","start":169,"end":253}],"gene3D":[]},"creator":"rpancsa","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MLQACKMEGFPLVPPPSEDLVPYDTDLYQRQTHEYYPYLSSDGESHSDHYWDFHPHHVHSEFESFAENNFTELQSVQPPQLQQLYRHMELEQMHVLDTPMVPPHPSLGHQVSYLPRMCLQYPSLSPAQPSSDEEEGERQSPPLEVSDGEADGLEPGPGLLPGETGSKKKIRLYQFLLDLLRSGDMKDSIWWVDKDKGTFQFSSKHKEALAHRWGIQKGNRKKMTYQKMARALRNYGKTGEVKKVKKKLTYQFSGEVLGRGGLAERRHPPH","length":270,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":165,"region_id":"DP02918r001","start":118,"term_id":"IDPO:0000002","statement":[{"text":"In 1:1-bound ΔN165, whose resonances were well resolved, 88 of the 95 assigned residues overlapped with ΔN117, with all PEST residues clustered around 8.2 ± 0.2 parts per million (ppm) on the 1H dimension, a chemical shift characteristic of disordered structures.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"32128405","version":2,"reference_html":"Intrinsic disorder controls two functionally distinct dimers of the master transcription factor PU.1. <i> Xhani S, Lee S, Kim HM, Wang S, Esaki S, Ha VLT, Khanezarrin M, Fernandez GL, Albrecht AV, Aramini JM, Germann MW, Poon GMK. </i> Sci Adv, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-02T14:33:34.216Z"}},{"start":1,"end":168,"reference_id":"32128405","reference_source":"pmid","reference_html":"Intrinsic disorder controls two functionally distinct dimers of the master transcription factor PU.1. <i> Xhani S, Lee S, Kim HM, Wang S, Esaki S, Ha VLT, Khanezarrin M, Fernandez GL, Albrecht AV, Aramini JM, Germann MW, Poon GMK. </i> Sci Adv, 2020","date":"2024-12-02T14:27:03.284Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP02918r007","statement":[{"text":"The remaining ~170 and 12 residues that flank N- and C-terminally, respectively, are intrinsically disordered sequences. The extended N-terminal IDR consists of an acidic transactivation domain (human residues 1 to 80), a Q-rich domain (residues 81 to 116), and a highly negatively charged PEST domain (residues 117 to 165), all of which are characteristic disordered regions in eukaryotic factors (9).","type":"Introduction"},{"text":"The DNA binding (ETS) domain of PU.1 represents its only structured domain, whose 1:1 complex with cognate DNA (Fig. 1A) is structurally conserved in this family of transcription factors.","type":"Results"}]},{"start":258,"end":270,"reference_id":"32128405","reference_source":"pmid","reference_html":"Intrinsic disorder controls two functionally distinct dimers of the master transcription factor PU.1. <i> Xhani S, Lee S, Kim HM, Wang S, Esaki S, Ha VLT, Khanezarrin M, Fernandez GL, Albrecht AV, Aramini JM, Germann MW, Poon GMK. </i> Sci Adv, 2020","date":"2024-12-02T14:27:22.289Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP02918r008","statement":[{"text":"The remaining ~170 and 12 residues that flank N- and C-terminally, respectively, are intrinsically disordered sequences. The extended N-terminal IDR consists of an acidic transactivation domain (human residues 1 to 80), a Q-rich domain (residues 81 to 116), and a highly negatively charged PEST domain (residues 117 to 165), all of which are characteristic disordered regions in eukaryotic factors (9).","type":"Introduction"},{"text":"The DNA binding (ETS) domain of PU.1 represents its only structured domain, whose 1:1 complex with cognate DNA (Fig. 1A) is structurally conserved in this family of transcription factors.","type":"Results"}]},{"start":118,"end":165,"reference_id":"32128405","reference_source":"pmid","reference_html":"Intrinsic disorder controls two functionally distinct dimers of the master transcription factor PU.1. <i> Xhani S, Lee S, Kim HM, Wang S, Esaki S, Ha VLT, Khanezarrin M, Fernandez GL, Albrecht AV, Aramini JM, Germann MW, Poon GMK. </i> Sci Adv, 2020","date":"2024-12-02T14:42:27.155Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP02918r009","statement":[{"text":"To gain insight into the conformational structure of the free PU.1 dimer, we interrogated ΔN165 and ΔN117 by circular dichroism (CD) and NMR spectroscopy. At an identically low concentration (25 μM), a net contribution of coil content due to the PEST domain was apparent (Fig. 3C). ","type":"Results"}]}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02918","date":"2020-06-16T11:01:05.835Z","organism":"Homo sapiens","regions_counter":9,"name":"Transcription factor PU.1","dataset":["Age-related disorders proteins"],"UniParc":"UPI00001329E8","uniref100":"UniRef100_P17947","uniref90":"UniRef90_P17947","uniref50":"UniRef50_P17947","genes":[{"name":{"value":"SPI1"}}],"alphafold_very_low_content":0.3925925925925926,"disorder_content":0.6703703703703704,"disprot_consensus":{"full":[{"start":1,"end":168,"type":"D"},{"start":258,"end":270,"type":"D"}],"Structural state":[{"start":1,"end":168,"type":"D"},{"start":258,"end":270,"type":"D"}]}},{"acc":"Q9SQK3","features":{"pfam":[{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":199,"end":280}],"gene3D":[]},"creator":"rpancsa","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"sequence":"MVSSVLSIPPQTCLLPRLPISDSVNCKSKIVYCLSTSVRGSSVKRQSTARTRSFTETNRRTPSVQSKHEFWEDPDDGSDSENEYEGEEEDGIGNDLDNESDWEDDSRVQKLTTTDNYEEELAKEVEQLLEPEERVILQQNEKPNLKMISTKSWKPLQTLALSMQIQLMDNLIENGLDIDDVDKDNQTALHKAIIGKKEAVISHLLRKGANPHLQDRDGAAPIHYAVQVGALQTVKLLFKYNVDVNVADNEGWTPLHIAVQSRNRDITKILLTNGADKTRRTKDGKLALDLALCFGRDFKSYDLVKLLKIMPTGDI","length":315,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":112,"region_id":"DP02919r001","start":40,"term_id":"IDPO:0000002","statement":[{"text":"The crystal structure of the STT hetero-dimer complex from Arabidopsis was determined at 2.2 A˚ resolution (Table S1 ). Because the IDRs of STT1 and STT2 are highly mobile, residues 40–112 of STT1 and residues 37–231 of STT2 could not be accurately modeled into the electron density.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"32169217","version":2,"reference_html":"Liquid-Liquid Phase Transition Drives Intra-chloroplast Cargo Sorting. <i> Ouyang M, Li X, Zhang J, Feng P, Pu H, Kong L, Bai Z, Rong L, Xu X, Chi W, Wang Q, Chen F, Lu C, Shen J, Zhang L. </i> Cell, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","term_name":"disorder","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T17:22:41.003Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q42029","partner_end":null}],"ec_ontology":"ECO","end":112,"region_id":"DP02919r002","start":40,"term_id":"GO:0005515","statement":[{"text":"Moreover, deletion of IDRs of either STT1 or STT2 substantially impacts binding of OE23 to the STT complex as revealed by pull-down assays.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"32169217","version":3,"reference_html":"Liquid-Liquid Phase Transition Drives Intra-chloroplast Cargo Sorting. <i> Ouyang M, Li X, Zhang J, Feng P, Pu H, Kong L, Bai Z, Rong L, Xu X, Chi W, Wang Q, Chen F, Lu C, Shen J, Zhang L. </i> Cell, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006077","term_name":"protein binding","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T17:22:43.018Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q42029","partner_end":null}],"ec_ontology":"ECO","end":112,"region_id":"DP02919r003","start":40,"term_id":"GO:0005515","statement":[{"text":"the STT complex was able to bind the LMNG-solubilized synthetic transit peptide of OE23 (KD =8 mM) at an approximately 1:1 protein: peptide ratio","type":"Results"},{"text":"ITC-based titration assays also demonstrated that deletion of the IDRs of either STT1 or STT2 substantially impaired binding of cpTat transit peptide to the STT complex, showing an 20-fold and 10-fold higher KD, respectively","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"isothermal titration calorimetry evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"32169217","version":3,"reference_html":"Liquid-Liquid Phase Transition Drives Intra-chloroplast Cargo Sorting. <i> Ouyang M, Li X, Zhang J, Feng P, Pu H, Kong L, Bai Z, Rong L, Xu X, Chi W, Wang Q, Chen F, Lu C, Shen J, Zhang L. </i> Cell, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005647","term_name":"protein binding","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T17:22:50.926Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":112,"region_id":"DP02919r004","start":40,"term_id":"GO:0140693","statement":[{"text":"Our results showed that 0.5 mM in vitro-translated OE23 precursor could also induce the STTs (2.5 mM) phase separation (Figure 4B).","type":"Results"},{"text":"Substitution of the residues of the LTP binding motif within the STTs prevented phase separation (Figure S4A). Thus, besides formation of STT oligomers, the STTs-LTP binding reaction is also required for this phase separation.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"microscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"32169217","version":3,"reference_html":"Liquid-Liquid Phase Transition Drives Intra-chloroplast Cargo Sorting. <i> Ouyang M, Li X, Zhang J, Feng P, Pu H, Kong L, Bai Z, Rong L, Xu X, Chi W, Wang Q, Chen F, Lu C, Shen J, Zhang L. </i> Cell, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001232","term_name":"molecular condensate scaffold activity","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T17:23:41.298Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":3702,"disprot_id":"DP02919","date":"2020-06-17T12:17:55.539Z","organism":"Arabidopsis thaliana","regions_counter":4,"name":"Ankyrin repeat domain-containing protein EMB506, chloroplastic","dataset":["Condensates-related proteins"],"UniParc":"UPI00000A02A1","uniref100":"UniRef100_Q9SQK3","uniref90":"UniRef90_Q9SQK3","uniref50":"UniRef50_Q9SQK3","genes":[{"name":{"value":"EMB506"},"orfNames":[{"value":"MSN9.60"}],"olnNames":[{"value":"At5g40160"}]}],"alphafold_very_low_content":0.2984126984126984,"disorder_content":0.23174603174603176,"disprot_consensus":{"full":[{"start":40,"end":112,"type":"D"}],"Structural state":[{"start":40,"end":112,"type":"D"}],"Molecular function":[{"start":40,"end":112,"type":"F"}]}},{"acc":"Q05753","features":{"pfam":[{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":308,"end":389},{"id":"PF13637","name":"Ankyrin repeats (many copies)","start":264,"end":303}],"gene3D":[]},"creator":"rpancsa","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"sequence":"MQSLSTPHTISLLLPRTSPSRLSPSLHSLAFPTRLRSLSYSSQTSILPDAGDDFIVGDCLVYEDGVFEDPYLDKEVTQVAKQERKKNRRGGAKRLDESEIEPENLVPEEWRDIQAEVNLTKKDKRKIAQEMEFGVRVEKKRQGLIPLRKVDLNDFLTYKEAKLAQLRPVILDKPGNFSDDSGASSDGETAVSSPSERVAPKNPRWAVYGKGFDHVAKFFNSDKYDPSDKKSDGPRKLLSKEEKFMLNSRNPDLAVATSKKWLPLHTLAACGEFYLVDSLLKHNLDINATDVGGLTVLHRAIIGKKQAITNYLLRESANPFVLDDEGATLMHYAVQTASAPTIKLLLLYNADINAQDRDGWTPLHVAVQARRSDIVKLLLIKGADIEVKNKDGLTPLGLCLYLGREIRTYEVMKLLKEFPLSRHKKRLVTTDEDIE","length":435,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":231,"region_id":"DP02920r001","start":37,"term_id":"IDPO:0000002","statement":[{"text":"The crystal structure of the STT hetero-dimer complex from Arabidopsis was determined at 2.2 A˚ resolution (Table S1 ). Because the IDRs of STT1 and STT2 are highly mobile, residues 40–112 of STT1 and residues 37–231 of STT2 could not be accurately modeled into the electron density.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"32169217","version":2,"reference_html":"Liquid-Liquid Phase Transition Drives Intra-chloroplast Cargo Sorting. <i> Ouyang M, Li X, Zhang J, Feng P, Pu H, Kong L, Bai Z, Rong L, Xu X, Chi W, Wang Q, Chen F, Lu C, Shen J, Zhang L. </i> Cell, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","term_name":"disorder","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T17:24:13.486Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q42029","partner_end":null}],"ec_ontology":"ECO","end":231,"region_id":"DP02920r002","start":37,"term_id":"GO:0005515","statement":[{"text":"Moreover, deletion of IDRs of either STT1 or STT2 substantially impacts binding of OE23 to the STT complex as revealed by pull-down assays","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"32169217","version":3,"reference_html":"Liquid-Liquid Phase Transition Drives Intra-chloroplast Cargo Sorting. <i> Ouyang M, Li X, Zhang J, Feng P, Pu H, Kong L, Bai Z, Rong L, Xu X, Chi W, Wang Q, Chen F, Lu C, Shen J, Zhang L. </i> Cell, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006077","term_name":"protein binding","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T17:24:14.642Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q42029","partner_end":null}],"ec_ontology":"ECO","end":231,"region_id":"DP02920r003","start":37,"term_id":"GO:0005515","statement":[{"text":"the STT complex was able to bind the LMNG-solubilized synthetic transit peptide of OE23 (KD = 8 mM) at an approximately 1:1 protein: peptide ratio. ","type":"Results"},{"text":"ITC-based titration assays also demonstrated that deletion of the IDRs of either STT1 or STT2 substantially impaired binding of cpTat transit peptide to the STT complex, showing an 20-fold and 10-fold higher KD, respectively","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"isothermal titration calorimetry evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"32169217","version":3,"reference_html":"Liquid-Liquid Phase Transition Drives Intra-chloroplast Cargo Sorting. <i> Ouyang M, Li X, Zhang J, Feng P, Pu H, Kong L, Bai Z, Rong L, Xu X, Chi W, Wang Q, Chen F, Lu C, Shen J, Zhang L. </i> Cell, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005647","term_name":"protein binding","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T17:24:15.400Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":231,"region_id":"DP02920r004","start":37,"term_id":"GO:0140693","statement":[{"text":"Our results showed that 0.5 mM in vitro-translated OE23 precursor could also induce the STTs (2.5 mM) phase separation (Figure 4B).","type":"Results"},{"text":"Substitution of the residues of the LTP binding motif within the STTs prevented phase separation (Figure S4A). Thus, besides formation of STT oligomers, the STTs-LTP binding reaction is also required for this phase separation. ","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"microscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"32169217","version":3,"reference_html":"Liquid-Liquid Phase Transition Drives Intra-chloroplast Cargo Sorting. <i> Ouyang M, Li X, Zhang J, Feng P, Pu H, Kong L, Bai Z, Rong L, Xu X, Chi W, Wang Q, Chen F, Lu C, Shen J, Zhang L. </i> Cell, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001232","term_name":"molecular condensate scaffold activity","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-03-09T17:24:16.116Z"},"curator_orcid":"0000-0003-0849-9312","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_06","ncbi_taxon_id":3702,"disprot_id":"DP02920","date":"2020-06-17T12:38:51.398Z","organism":"Arabidopsis thaliana","regions_counter":4,"name":"Ankyrin repeat domain-containing protein, chloroplastic","dataset":["Condensates-related proteins"],"UniParc":"UPI000016DB5F","uniref100":"UniRef100_Q05753","uniref90":"UniRef90_Q05753","uniref50":"UniRef50_Q05753","genes":[{"name":{"value":"AKRP"},"synonyms":[{"value":"AKR"},{"value":"EMB2036"}],"orfNames":[{"value":"K2A18.13"}],"olnNames":[{"value":"At5g66055"}]}],"alphafold_very_low_content":0.24597701149425288,"disorder_content":0.4482758620689655,"disprot_consensus":{"full":[{"start":37,"end":231,"type":"D"}],"Structural state":[{"start":37,"end":231,"type":"D"}],"Molecular function":[{"start":37,"end":231,"type":"F"}]}},{"acc":"P26368","features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":151,"end":224},{"id":"PF00076","name":"RNA recognition motif","start":261,"end":330},{"id":"PF00076","name":"RNA recognition motif","start":400,"end":459}],"gene3D":[]},"creator":"rpancsa","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MSDFDEFERQLNENKQERDKENRHRKRSHSRSRSRDRKRRSRSRDRRNRDQRSASRDRRRRSKPLTRGAKEEHGGLIRSPRHEKKKKVRKYWDVPPPGFEHITPMQYKAMQAAGQIPATALLPTMTPDGLAVTPTPVPVVGSQMTRQARRLYVGNIPFGITEEAMMDFFNAQMRLGGLTQAPGNPVLAVQINQDKNFAFLEFRSVDETTQAMAFDGIIFQGQSLKIRRPHDYQPLPGMSENPSVYVPGVVSTVVPDSAHKLFIGGLPNYLNDDQVKELLTSFGPLKAFNLVKDSATGLSKGYAFCEYVDINVTDQAIAGLNGMQLGDKKLLVQRASVGAKNATLVSPPSTINQTPVTLQVPGLMSSQVQMGGHPTEVLCLMNMVLPEELLDDEEYEEIVEDVRDECSKYGLVKSIEIPRPVDGVEVPGCGKIFVEFTSVFDCQKAMQGLTGRKFANRVVVTKYCDPDSYHRRDFW","length":475,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":258,"region_id":"DP02921r001","start":231,"term_id":"IDPO:0000002","statement":[{"text":"Previous studies on the RNA binding of U2AF2mostly focused on RRM1 and RRM2, but suggested a potential role of the intervening linker region (residues 231 to 258) for regulating the dynamic RNA recognition by U2AF2","type":"Results"},{"text":"The RRM1–RRM2 linker is flexible, as indicated by low heteronuclear NOE values. The highest flexibility is ob-served for the N-terminal region of the linker (residues 235 to249), beyond the residues (D231/Y232) that stabilize helixα0.Consistently, NMR signals corresponding to these N-terminal linker residues (residues 235 to 245) in NMR spectra of the constructs, RRM1–linker and linker–RRM2, superimpose well with those in the spectrum of RRM1,2, indicative of their intrinsically disordered nature and absence of contacts to RRM1or RRM2","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"32188783","version":2,"reference_html":"An autoinhibitory intramolecular interaction proof-reads RNA recognition by the essential splicing factor U2AF2. <i> Kang HS, Sánchez-Rico C, Ebersberger S, Sutandy FXR, Busch A, Welte T, Stehle R, Hipp C, Schulz L, Buchbender A, Zarnack K, König J, Sattler M. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T16:03:55.091Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":259,"region_id":"DP02921r002","start":250,"term_id":"GO:0005515","statement":[{"text":"Indeed, our experimental heteronuclear NOEvalues display a gradual increase in the C-terminal region of the linker (residues 250 to 258) toward the RRM2 domain, indicative of limited flexibility (Fig. 1C). This is consistent with the interaction of the C-terminal region of the RRM1–RRM2 linker with the RNA binding interface of RRM2, as seen in our structure (Fig. 1B), although in a dynamic manner.","type":"Results"},{"text":" the C-terminal region of the linker (residues 250 to 259) adopts a well-defined conformation in the solution structure and binds to RRM2, supported by 84 distance restraints derived from proton–proton nuclear Overhauser enhancements (NOEs) between the linker and RRM2. In detail, three residues (V250/S251/T252) are packed against to the N-terminal end of strandβ2 in RRM2 (K286/A288/F288) in an antiparallel manner, while the rest of this region (residues 253 to259) interacts with residues in the RRM2β-sheet.","type":"Results"}],"curator_id":"rpancsa","released":"2023_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"32188783","version":4,"reference_html":"An autoinhibitory intramolecular interaction proof-reads RNA recognition by the essential splicing factor U2AF2. <i> Kang HS, Sánchez-Rico C, Ebersberger S, Sutandy FXR, Busch A, Welte T, Stehle R, Hipp C, Schulz L, Buchbender A, Zarnack K, König J, Sattler M. </i> Proc Natl Acad Sci U S A, 2020","date":"2023-12-07T09:55:58.507Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"protein binding","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"6TR0"}],"interaction_partner":[{"db":"UniProt","id":"P26368","operator":"and","partner_start":261,"partner_end":330}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T11:39:46.267Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":235,"region_id":"DP02921r003","start":231,"term_id":"GO:0005515","statement":[{"text":"First, two additional short helices form at the N terminus of RRM1, helixα0, and at the C terminus of RRM2, helixαC (Fig. 1B). In particular, the orientation of the N-terminal helix is stabilized by interactions with residues at the N-terminal region of the RRM1–RRM2 linker(D231/Y232)","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"32188783","version":3,"reference_html":"An autoinhibitory intramolecular interaction proof-reads RNA recognition by the essential splicing factor U2AF2. <i> Kang HS, Sánchez-Rico C, Ebersberger S, Sutandy FXR, Busch A, Welte T, Stehle R, Hipp C, Schulz L, Buchbender A, Zarnack K, König J, Sattler M. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"protein binding","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T11:39:49.979Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":258,"region_id":"DP02921r004","start":231,"term_id":"GO:0140678","statement":[{"text":"The Linker Plays an Autoinhibitory Role in Py-Tract RNA Binding.The interaction with the RNA binding interface of RRM2 suggests a potential role of the RRM1–RRM2 linker in regulating RNA binding. To further explore this, we removed the linker/RRM2contacts by replacing the core linker region (residues 233 to 257)with Gly-Gly-Ser repeats of the same length","type":"Results"},{"text":"RRM1,2-GS comprises two functional RRM domains butlacks the contacts of the RRM1,2 linker to RRM2.","type":"Results"},{"text":"the competition of linker and RNA for RRM2favors binding of strong over weak Py-tracts.","type":"Results"},{"text":"These data further corroborate the autoinhibitory role of the linker, and show that the dynamic linker/RRM2 interaction reduces the RNA binding affinity of RRM1,2. The linker thereby proofreads against the binding of weak RNA ligands by directly competing for the RNA binding interface on the RRM2. Of note, the autoinhibitory role of the linker is also recapitulated in the context of the minimal U2AFheterodimer (SI Appendix,Fig.S6B), indicating that the presence of the small subunit U2AF1 does not affect or modulate theRRM2/linker interaction.","type":"Results"}],"curator_id":"rpancsa","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Rita Pancsa","reference_id":"32188783","version":3,"reference_html":"An autoinhibitory intramolecular interaction proof-reads RNA recognition by the essential splicing factor U2AF2. <i> Kang HS, Sánchez-Rico C, Ebersberger S, Sutandy FXR, Busch A, Welte T, Stehle R, Hipp C, Schulz L, Buchbender A, Zarnack K, König J, Sattler M. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"molecular function inhibitor activity","curator_orcid":"0000-0003-0849-9312","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T16:05:12.034Z"}},{"start":231,"end":258,"reference_id":"32188783","reference_source":"pmid","reference_html":"An autoinhibitory intramolecular interaction proof-reads RNA recognition by the essential splicing factor U2AF2. <i> Kang HS, Sánchez-Rico C, Ebersberger S, Sutandy FXR, Busch A, Welte T, Stehle R, Hipp C, Schulz L, Buchbender A, Zarnack K, König J, Sattler M. </i> Proc Natl Acad Sci U S A, 2020","date":"2023-12-07T10:05:20.456Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6TR0"}],"region_id":"DP02921r005","statement":[{"text":"Previous studies on the RNA binding of U2AF2mostly focused on RRM1 and RRM2, but suggested a potential role of the intervening linker region (residues 231 to 258) for regulating the dynamic RNA recognition by U2AF2","type":"Results"},{"text":"The RRM1–RRM2 linker is flexible, as indicated by low heteronuclear NOE values. The highest flexibility is ob-served for the N-terminal region of the linker (residues 235 to249), beyond the residues (D231/Y232) that stabilize helixα0. Consistently, NMR signals corresponding to these N-terminal linker residues (residues 235 to 245) in NMR spectra of the constructs, RRM1–linker and linker–RRM2, superimpose well with those in the spectrum of RRM1,2, indicative of their intrinsically disordered nature and absence of contacts to RRM1or RRM2","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T11:39:54.286Z"}}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02921","date":"2020-06-17T14:26:30.338Z","organism":"Homo sapiens","regions_counter":5,"name":"Splicing factor U2AF 65 kDa subunit","dataset":["Condensates-related proteins"],"UniParc":"UPI000017A38C","uniref100":"UniRef100_P26368","uniref90":"UniRef90_P26368","uniref50":"UniRef50_P26368","genes":[{"name":{"value":"U2AF2"},"synonyms":[{"value":"U2AF65"}]}],"alphafold_very_low_content":0.21894736842105264,"disorder_content":0.05894736842105263,"disprot_consensus":{"full":[{"start":231,"end":258,"type":"D"},{"start":259,"end":259,"type":"F"}],"Structural state":[{"start":231,"end":258,"type":"D"}],"Molecular function":[{"start":231,"end":259,"type":"F"}],"Disorder function":[{"start":231,"end":258,"type":"F"}]}},{"acc":"P01215","features":{"pfam":[{"id":"PF00236","name":"Glycoprotein hormone","start":28,"end":115}],"gene3D":[]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MDYYRKYAAIFLVTLSVFLHVLHSAPDVQDCPECTLQENPFFSQPGAPILQCMGCCFSRAYPTPLRSKKTMLVQKNVTSESTCCVAKSYNRVTVMGGFKVENHTACHCSTCYYHKS","length":116,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":57,"region_id":"DP02922r001","start":33,"term_id":"IDPO:0000002","statement":[{"text":"The solution structure of dg-alpha hCG is represented by an ensemble of 27 structures. In comparison to the crystal structure of the dimer, the solution structure of free dg-alpha hCG exhibits: (a) an increased structural disorder (residues 33-57); (b) a different backbone conformation near Val76 and Glu77; and (c) a larger flexibility.","type":"Abstract"},{"text":"The disorder present in the segment comprising residues 33–57 reflects the absence of medium‐and long‐range NOEs. This is in good agreement with the random coil 1H chemical shifts of the corresponding residues","type":"Results"},{"text":"The two hairpins are connected by a disordered loop consisting of the residues 33–57.","type":"Results"},{"text":"From Fig. 6 it is obvious that free dg‐αhCG is a rather flexible molecule. This is reflected by the disorder we observed for the loop comprising residues α33–57, and also by the conformational heterogeneity of the hairpin loop α70–74 and the tight turn α20–23. ","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10095786","version":2,"reference_html":"Solution structure of the alpha-subunit of human chorionic gonadotropin. <i> Erbel PJ, Karimi-Nejad Y, De Beer T, Boelens R, Kamerling JP, Vliegenthart JF. </i> Eur J Biochem, 1999","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"1DZ7"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":10,"region_id":"DP02922r002","start":1,"term_id":"IDPO:0000002","statement":[{"text":"The N‐ and C‐terminal segments, comprising residues 1–10 and 85–92, respectively, are also disordered and stick out into the solution like two arms.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"10095786","version":2,"reference_html":"Solution structure of the alpha-subunit of human chorionic gonadotropin. <i> Erbel PJ, Karimi-Nejad Y, De Beer T, Boelens R, Kamerling JP, Vliegenthart JF. </i> Eur J Biochem, 1999","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","cross_refs":[{"db":"PDB","id":"1DZ7"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":9606,"disprot_id":"DP02922","date":"2020-06-20T23:05:02.721Z","organism":"Homo sapiens","regions_counter":2,"name":"Glycoprotein hormones alpha chain","dataset":[],"UniParc":"UPI000003FF94","uniref100":"UniRef100_P01215","uniref90":"UniRef90_P01215","uniref50":"UniRef50_P01215","genes":[{"name":{"value":"CGA"}}],"alphafold_very_low_content":0,"disorder_content":0.3017241379310345,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"},{"start":33,"end":57,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":33,"end":57,"type":"D"}]}},{"acc":"P33128","features":{"pfam":[{"id":"PF00345","name":"Pili and flagellar-assembly chaperone, PapD N-terminal domain","start":27,"end":152},{"id":"PF02753","name":"Pili assembly chaperone PapD, C-terminal domain","start":158,"end":243}],"gene3D":[]},"creator":"fquaglia","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"sequence":"MFFNTKHTTALCFVTCMAFSSSSIADIVISGTRVIYKSDQKSVNVRLENKGNNPLLVQSWLDTGDDNAEPGSITVPFTATPPVSRIDAKRGQTIKLMYTASTSLPKDRESVFWFNVLEVPPKPDAEKVANQSLLQLAFRTRIKLFYRPDGLKGNPSEAPLALKWFWSGSEGKASLRVTNPTPYYVSFSSGDLEASGKRYPIDVKMIAPFSDEVMKVNGLNGKANSAKVHFYAINDFGGAIEGNARL","length":246,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":132,"region_id":"DP02923r001","start":122,"term_id":"IDPO:0000002","statement":[{"text":"The residues 42-49, 98-108, 146, and 147 of the protein were not observed in the electron density map, which appears to be highly flexible.","type":"Results"},{"text":"The highly flexible region 98-108 corresponds to region 122-132 on the protein sequence, since region 1-25 of the protein was excluded from the crystal structure as it corresponds to a signal peptide.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"32649775","version":2,"reference_html":"Crystal structure of the usher chaperone YadV reveals a monomer with the proline lock in closed conformation suggestive of an intermediate state. <i> Pandey NK, Verma G, Kushwaha GS, Suar M, Suar M, Bhavesh NS. </i> FEBS Lett, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5ghu"}],"term_name":"disorder","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:41:21.256Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":132,"region_id":"DP02923r002","start":122,"term_id":"IDPO:0000033","statement":[{"text":"The residues 42-49, 98-108, 146, and 147 of the protein were not observed in the electron density map, which appears to be highly flexible.","type":"Results"},{"text":"The  polypeptide  chain  may  be  divided  into  two  major domains, the N-terminal domain (residues, 1-123) has immunoglobulin (Ig) like fold whereas the C-terminal  domain  has  β-barrel  fold  (residues,  130-222).","type":"Results"},{"text":"The highly flexible region 98-108 corresponds to region 122-132 on the protein sequence, since region 1-25 of the protein was excluded from the crystal structure as it corresponds to a signal peptide.","type":"Curator statement"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"32649775","version":3,"reference_html":"Crystal structure of the usher chaperone YadV reveals a monomer with the proline lock in closed conformation suggestive of an intermediate state. <i> Pandey NK, Verma G, Kushwaha GS, Suar M, Suar M, Bhavesh NS. </i> FEBS Lett, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","cross_refs":[{"db":"PDB","id":"5ghu"}],"term_name":"flexible linker","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:41:22.428Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":83333,"disprot_id":"DP02923","date":"2020-07-17T09:33:12.066Z","organism":"Escherichia coli (strain K12)","regions_counter":2,"name":"Probable fimbrial chaperone YadV","dataset":["Stress response proteins"],"UniParc":"UPI000016F0FB","uniref100":"UniRef100_P33128","uniref90":"UniRef90_P33128","uniref50":"UniRef50_P33128","genes":[{"name":{"value":"yadV"},"synonyms":[{"value":"ecpD"}],"olnNames":[{"value":"b0140"},{"value":"JW0136"}]}],"alphafold_very_low_content":0.0040650406504065045,"disorder_content":0.044715447154471545,"disprot_consensus":{"full":[{"start":122,"end":132,"type":"D"}],"Structural state":[{"start":122,"end":132,"type":"D"}],"Disorder function":[{"start":122,"end":132,"type":"F"}]}},{"acc":"P0C6X7","features":{"pfam":[{"id":"PF00680","name":"Viral RNA-dependent RNA polymerase","start":4866,"end":5140},{"id":"PF01661","name":"Macro domain","start":1036,"end":1143},{"id":"PF05409","name":"Coronavirus endopeptidase C30","start":3269,"end":3551},{"id":"PF06460","name":"Coronavirus 2'-O-methyltransferase","start":6777,"end":7072},{"id":"PF06471","name":"Coronavirus proofreading exoribonuclease","start":5906,"end":6426},{"id":"PF06478","name":"Coronavirus RNA-dependent RNA polymerase, N-terminal","start":4384,"end":4735},{"id":"PF08710","name":"Coronavirus replicase NSP9","start":4118,"end":4230},{"id":"PF08715","name":"Coronavirus papain-like peptidase","start":1541,"end":1859},{"id":"PF08716","name":"Coronavirus replicase NSP7","start":3837,"end":3919},{"id":"PF08717","name":"Coronavirus replicase NSP8","start":3920,"end":4117},{"id":"PF09401","name":"Coronavirus RNA synthesis protein NSP10","start":4240,"end":4361},{"id":"PF11501","name":"Betacoronavirus replicase NSP1","start":9,"end":131},{"id":"PF11633","name":"Betacoronavirus single-stranded poly(A) binding domain","start":1327,"end":1469},{"id":"PF12124","name":"Betacoronavirus SUD-C domain","start":1473,"end":1538},{"id":"PF12379","name":"Betacoronavirus replicase NSP3, N-terminal","start":881,"end":1029},{"id":"PF13087","name":"AAA domain","start":5739,"end":5876},{"id":"PF16251","name":"Betacoronavirus nucleic acid-binding (NAB)","start":1876,"end":2007},{"id":"PF16348","name":"Coronavirus replicase NSP4, C-terminal","start":3144,"end":3240},{"id":"PF19211","name":"Coronavirus replicase NSP2, N-terminal","start":184,"end":423},{"id":"PF19213","name":"Coronavirus replicase NSP6","start":3576,"end":3836}],"gene3D":[]},"creator":"fquaglia","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Nidovirales","Cornidovirineae","Coronaviridae","Orthocoronavirinae","Betacoronavirus","Sarbecovirus"],"sequence":"MESLVLGVNEKTHVQLSLPVLQVRDVLVRGFGDSVEEALSEAREHLKNGTCGLVELEKGVLPQLEQPYVFIKRSDALSTNHGHKVVELVAEMDGIQYGRSGITLGVLVPHVGETPIAYRNVLLRKNGNKGAGGHSYGIDLKSYDLGDELGTDPIEDYEQNWNTKHGSGALRELTRELNGGAVTRYVDNNFCGPDGYPLDCIKDFLARAGKSMCTLSEQLDYIESKRGVYCCRDHEHEIAWFTERSDKSYEHQTPFEIKSAKKFDTFKGECPKFVFPLNSKVKVIQPRVEKKKTEGFMGRIRSVYPVASPQECNNMHLSTLMKCNHCDEVSWQTCDFLKATCEHCGTENLVIEGPTTCGYLPTNAVVKMPCPACQDPEIGPEHSVADYHNHSNIETRLRKGGRTRCFGGCVFAYVGCYNKRAYWVPRASADIGSGHTGITGDNVETLNEDLLEILSRERVNINIVGDFHLNEEVAIILASFSASTSAFIDTIKSLDYKSFKTIVESCGNYKVTKGKPVKGAWNIGQQRSVLTPLCGFPSQAAGVIRSIFARTLDAANHSIPDLQRAAVTILDGISEQSLRLVDAMVYTSDLLTNSVIIMAYVTGGLVQQTSQWLSNLLGTTVEKLRPIFEWIEAKLSAGVEFLKDAWEILKFLITGVFDIVKGQIQVASDNIKDCVKCFIDVVNKALEMCIDQVTIAGAKLRSLNLGEVFIAQSKGLYRQCIRGKEQLQLLMPLKAPKEVTFLEGDSHDTVLTSEEVVLKNGELEALETPVDSFTNGAIVGTPVCVNGLMLLEIKDKEQYCALSPGLLATNNVFRLKGGAPIKGVTFGEDTVWEVQGYKNVRITFELDERVDKVLNEKCSVYTVESGTEVTEFACVVAEAVVKTLQPVSDLLTNMGIDLDEWSVATFYLFDDAGEENFSSRMYCSFYPPDEEEEDDAECEEEEIDETCEHEYGTEDDYQGLPLEFGASAETVRVEEEEEEDWLDDTTEQSEIEPEPEPTPEEPVNQFTGYLKLTDNVAIKCVDIVKEAQSANPMVIVNAANIHLKHGGGVAGALNKATNGAMQKESDDYIKLNGPLTVGGSCLLSGHNLAKKCLHVVGPNLNAGEDIQLLKAAYENFNSQDILLAPLLSAGIFGAKPLQSLQVCVQTVRTQVYIAVNDKALYEQVVMDYLDNLKPRVEAPKQEEPPNTEDSKTEEKSVVQKPVDVKPKIKACIDEVTTTLEETKFLTNKLLLFADINGKLYHDSQNMLRGEDMSFLEKDAPYMVGDVITSGDITCVVIPSKKAGGTTEMLSRALKKVPVDEYITTYPGQGCAGYTLEEAKTALKKCKSAFYVLPSEAPNAKEEILGTVSWNLREMLAHAEETRKLMPICMDVRAIMATIQRKYKGIKIQEGIVDYGVRFFFYTSKEPVASIITKLNSLNEPLVTMPIGYVTHGFNLEEAARCMRSLKAPAVVSVSSPDAVTTYNGYLTSSSKTSEEHFVETVSLAGSYRDWSYSGQRTELGVEFLKRGDKIVYHTLESPVEFHLDGEVLSLDKLKSLLSLREVKTIKVFTTVDNTNLHTQLVDMSMTYGQQFGPTYLDGADVTKIKPHVNHEGKTFFVLPSDDTLRSEAFEYYHTLDESFLGRYMSALNHTKKWKFPQVGGLTSIKWADNNCYLSSVLLALQQLEVKFNAPALQEAYYRARAGDAANFCALILAYSNKTVGELGDVRETMTHLLQHANLESAKRVLNVVCKHCGQKTTTLTGVEAVMYMGTLSYDNLKTGVSIPCVCGRDATQYLVQQESSFVMMSAPPAEYKLQQGTFLCANEYTGNYQCGHYTHITAKETLYRIDGAHLTKMSEYKGPVTDVFYKETSYTTTIKPVSYKLDGVTYTEIEPKLDGYYKKDNAYYTEQPIDLVPTQPLPNASFDNFKLTCSNTKFADDLNQMTGFTKPASRELSVTFFPDLNGDVVAIDYRHYSASFKKGAKLLHKPIVWHINQATTKTTFKPNTWCLRCLWSTKPVDTSNSFEVLAVEDTQGMDNLACESQQPTSEEVVENPTIQKEVIECDVKTTEVVGNVILKPSDEGVKVTQELGHEDLMAAYVENTSITIKKPNELSLALGLKTIATHGIAAINSVPWSKILAYVKPFLGQAAITTSNCAKRLAQRVFNNYMPYVFTLLFQLCTFTKSTNSRIRASLPTTIAKNSVKSVAKLCLDAGINYVKSPKFSKLFTIAMWLLLLSICLGSLICVTAAFGVLLSNFGAPSYCNGVRELYLNSSNVTTMDFCEGSFPCSICLSGLDSLDSYPALETIQVTISSYKLDLTILGLAAEWVLAYMLFTKFFYLLGLSAIMQVFFGYFASHFISNSWLMWFIISIVQMAPVSAMVRMYIFFASFYYIWKSYVHIMDGCTSSTCMMCYKRNRATRVECTTIVNGMKRSFYVYANGGRGFCKTHNWNCLNCDTFCTGSTFISDEVARDLSLQFKRPINPTDQSSYIVDSVAVKNGALHLYFDKAGQKTYERHPLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCDESASKSASVYYSQLMCQPILLLDQALVSDVGDSTEVSVKMFDAYVDTFSATFSVPMEKLKALVATAHSELAKGVALDGVLSTFVSAARQGVVDTDVDTKDVIECLKLSHHSDLEVTGDSCNNFMLTYNKVENMTPRDLGACIDCNARHINAQVAKSHNVSLIWNVKDYMSLSEQLRKQIRSAAKKNNIPFRLTCATTRQVVNVITTKISLKGGKIVSTCFKLMLKATLLCVLAALVCYIVMPVHTLSIHDGYTNEIIGYKAIQDGVTRDIISTDDCFANKHAGFDAWFSQRGGSYKNDKSCPVVAAIITREIGFIVPGLPGTVLRAINGDFLHFLPRVFSAVGNICYTPSKLIEYSDFATSACVLAAECTIFKDAMGKPVPYCYDTNLLEGSISYSELRPDTRYVLMDGSIIQFPNTYLEGSVRVVTTFDAEYCRHGTCERSEVGICLSTSGRWVLNNEHYRALSGVFCGVDAMNLIANIFTPLVQPVGALDVSASVVAGGIIAILVTCAAYYFMKFRRVFGEYNHVVAANALLFLMSFTILCLVPAYSFLPGVYSVFYLYLTFYFTNDVSFLAHLQWFAMFSPIVPFWITAIYVFCISLKHCHWFFNNYLRKRVMFNGVTFSTFEEAALCTFLLNKEMYLKLRSETLLPLTQYNRYLALYNKYKYFSGALDTTSYREAACCHLAKALNDFSNSGADVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDTVYCPRHVICTAEDMLNPNYEDLLIRKSNHSFLVQAGNVQLRVIGHSMQNCLLRLKVDTSNPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNHTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGKFYGPFVDRQTAQAAGTDTTITLNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCAALKELLQNGMNGRTILGSTILEDEFTPFDVVRQCSGVTFQGKFKKIVKGTHHWMLLTFLTSLLILVQSTQWSLFFFVYENAFLPFTLGIMAIAACAMLLVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLELADTSLSGYRLKDCVMYASALVLLILMTARTVYDDAARRVWTLMNVITLVYKVYYGNALDQAISMWALVISVTSNYSGVVTTIMFLARAIVFVCVEYYPLLFITGNTLQCIMLVYCFLGYCCCCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKSSIDAFKLNIKLLGIGGKPCIKVATVQSKMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQGAVDINRLCEEMLDNRATLQAIASEFSSLPSYAAYATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRKLEKMADQAMTQMYKQARSEDKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVVPDYGTYKNTCDGNTFTYASALWEIQQVVDADSKIVQLSEINMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNNSKGGRFVLALLSDHQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQAGNATEVPANSTVLSFCAFAVDPAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHPNPKGFCDLKGKYVQIPTTCANDPVGFTLRNTVCTVCGMWKGYGCSCDQLREPLMQSADASTFLNRVCGVSAARLTPCGTGTSTDVVYRAFDIYNEKVAGFAKFLKTNCCRFQEKDEEGNLLDSYFVVKRHTMSNYQHEETIYNLVKDCPAVAVHDFFKFRVDGDMVPHISRQRLTKYTMADLVYALRHFDEGNCDTLKEILVTYNCCDDDYFNKKDWYDFVENPDILRVYANLGERVRQSLLKTVQFCDAMRDAGIVGVLTLDNQDLNGNWYDFGDFVQVAPGCGVPIVDSYYSLLMPILTLTRALAAESHMDADLAKPLIKWDLLKYDFTEERLCLFDRYFKYWDQTYHPNCINCLDDRCILHCANFNVLFSTVFPPTSFGPLVRKIFVDGVPFVVSTGYHFRELGVVHNQDVNLHSSRLSFKELLVYAADPAMHAASGNLLLDKRTTCFSVAALTNNVAFQTVKPGNFNKDFYDFAVSKGFFKEGSSVELKHFFFAQDGNAAISDYDYYRYNLPTMCDIRQLLFVVEVVDKYFDCYDGGCINANQVIVNNLDKSAGFPFNKWGKARLYYDSMSYEDQDALFAYTKRNVIPTITQMNLKYAISAKNRARTVAGVSICSTMTNRQFHQKLLKSIAATRGATVVIGTSKFYGGWHNMLKTVYSDVETPHLMGWDYPKCDRAMPNMLRIMASLVLARKHNTCCNLSHRFYRLANECAQVLSEMVMCGGSLYVKPGGTSSGDATTAYANSVFNICQAVTANVNALLSTDGNKIADKYVRNLQHRLYECLYRNRDVDHEFVDEFYAYLRKHFSMMILSDDAVVCYNSNYAAQGLVASIKNFKAVLYYQNNVFMSEAKCWTETDLTKGPHEFCSQHTMLVKQGDDYVYLPYPDPSRILGAGCFVDDIVKTDGTLMIERFVSLAIDAYPLTKHPNQEYADVFHLYLQYIRKLHDELTGHMLDMYSVMLTNDNTSRYWEPEFYEAMYTPHTVLQAVGACVLCNSQTSLRCGACIRRPFLCCKCCYDHVISTSHKLVLSVNPYVCNAPGCDVTDVTQLYLGGMSYYCKSHKPPISFPLCANGQVFGLYKNTCVGSDNVTDFNAIATCDWTNAGDYILANTCTERLKLFAAETLKATEETFKLSYGIATVREVLSDRELHLSWEVGKPRPPLNRNYVFTGYRVTKNSKVQIGEYTFEKGDYGDAVVYRGTTTYKLNVGDYFVLTSHTVMPLSAPTLVPQEHYVRITGLYPTLNISDEFSSNVANYQKVGMQKYSTLQGPPGTGKSHFAIGLALYYPSARIVYTACSHAAVDALCEKALKYLPIDKCSRIIPARARVECFDKFKVNSTLEQYVFCTVNALPETTADIVVFDEISMATNYDLSVVNARLRAKHYVYIGDPAQLPAPRTLLTKGTLEPEYFNSVCRLMKTIGPDMFLGTCRRCPAEIVDTVSALVYDNKLKAHKDKSAQCFKMFYKGVITHDVSSAINRPQIGVVREFLTRNPAWRKAVFISPYNSQNAVASKILGLPTQTVDSSQGSEYDYVIFTQTTETAHSCNVNRFNVAITRAKIGILCIMSDRDLYDKLQFTSLEIPRRNVATLQAENVTGLFKDCSKIITGLHPTQAPTHLSVDIKFKTEGLCVDIPGIPKDMTYRRLISMMGFKMNYQVNGYPNMFITREEAIRHVRAWIGFDVEGCHATRDAVGTNLPLQLGFSTGVNLVAVPTGYVDTENNTEFTRVNAKPPPGDQFKHLIPLMYKGLPWNVVRIKIVQMLSDTLKGLSDRVVFVLWAHGFELTSMKYFVKIGPERTCCLCDKRATCFSTSSDTYACWNHSVGFDYVYNPFMIDVQQWGFTGNLQSNHDQHCQVHGNAHVASCDAIMTRCLAVHECFVKRVDWSVEYPIIGDELRVNSACRKVQHMVVKSALLADKFPVLHDIGNPKAIKCVPQAEVEWKFYDAQPCSDKAYKIEELFYSYATHHDKFTDGVCLFWNCNVDRYPANAIVCRFDTRVLSNLNLPGCDGGSLYVNKHAFHTPAFDKSAFTNLKQLPFFYYSDSPCESHGKQVVSDIDYVPLKSATCITRCNLGGAVCRHHANEYRQYLDAYNMMISAGFSLWIYKQFDTYNLWNTFTRLQSLENVAYNVVNKGHFDGHAGEAPVSIINNAVYTKVDGIDVEIFENKTTLPVNVAFELWAKRNIKPVPEIKILNNLGVDIAANTVIWDYKREAPAHVSTIGVCTMTDIAKKPTESACSSLTVLFDGRVEGQVDLFRNARNGVLITEGSVKGLTPSKGPAQASVNGVTLIGESVKTQFNYFKKVDGIIQQLPETYFTQSRDLEDFKPRSQMETDFLELAMDEFIQRYKLEGYAFEHIVYGDFSHGQLGGLHLMIGLAKRSQDSPLKLEDFIPMDSTVKNYFITDAQTGSSKCVCSVIDLLLDDFVEIIKSQDLSVISKVVKVTIDYAEISFMLWCKDGHVETFYPKLQASQAWQPGVAMPNLYKMQRMLLEKCDLQNYGENAVIPKGIMMNVAKYTQLCQYLNTLTLAVPYNMRVIHFGAGSDKGVAPGTAVLRQWLPTGTLLVDSDLNDFVSDADSTLIGDCATVHTANKWDLIISDMYDPRTKHVTKENDSKEGFFTYLCGFIKQKLALGGSIAVKITEHSWNADLYKLMGHFSWWTAFVTNVNASSSEAFLIGANYLGKPKEQIDGYTMHANYIFWRNTNPIQLSSYSLFDMSKFPLKLRGTAVMSLKENQINDMIYSLLEKGRLIIRENNRVVVSSDILVNN","length":7073,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":12,"region_id":"DP02924r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"We further characterized the full-length 179-residue protein and show that the polypeptide segments of residues 1 to 12 and 129 to 179 are flexibly disordered.","type":"Abstract"},{"text":"However, the presence of flexibly disordered regions in the protein identified by 1H NMR spectroscopy (see “Characterization of the full-length SARS-CoV nsp1” below) was consistent with the results of secondary structure prediction, which indicated that a few residues at the N terminus, as well as a greater number of residues in the C-terminal one-third of the protein, would not adopt regular secondary structure.","type":"Results"},{"text":"The structure of intact nsp1 includes a globular domain of residues 13 to 121 and the disordered regions of residues 1 to 12 and 122 to 179 (Fig. 1b).","type":"Results"},{"text":"Most of the resonances in full-length nsp1 that are not present in nsp1(13-128) have either small positive or negative 15N{1H} NOEs (Fig. 5c), showing that the polypeptide segments of residues 1 to 12 and 129 to 179 are best described as a short N-terminal and a long C-terminal flexibly disordered tail, respectively (Fig. ​1b).","type":"Results"}],"curator_id":"jbergier","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Julian Bergier","reference_id":"17202208","version":3,"reference_html":"Novel beta-barrel fold in the nuclear magnetic resonance structure of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus. <i> Almeida MS, Johnson MA, Herrmann T, Geralt M, Wüthrich K. </i> J Virol, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0003-2206-9968","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-20T09:12:10.141Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":179,"region_id":"DP02924r002","start":129,"term_id":"IDPO:0000002","statement":[{"text":"We further characterized the full-length 179-residue protein and show that the polypeptide segments of residues 1 to 12 and 129 to 179 are flexibly disordered.","type":"Abstract"},{"text":"However, the presence of flexibly disordered regions in the protein identified by 1H NMR spectroscopy (see “Characterization of the full-length SARS-CoV nsp1” below) was consistent with the results of secondary structure prediction, which indicated that a few residues at the N terminus, as well as a greater number of residues in the C-terminal one-third of the protein, would not adopt regular secondary structure.","type":"Results"},{"text":"The structure of intact nsp1 includes a globular domain of residues 13 to 121 and the disordered regions of residues 1 to 12 and 122 to 179 (Fig. 1b).","type":"Results"},{"text":"Most of the resonances in full-length nsp1 that are not present in nsp1(13-128) have either small positive or negative 15N{1H} NOEs (Fig. 5c), showing that the polypeptide segments of residues 1 to 12 and 129 to 179 are best described as a short N-terminal and a long C-terminal flexibly disordered tail, respectively (Fig. ​1b).","type":"Results"}],"curator_id":"jbergier","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Julian Bergier","reference_id":"17202208","version":3,"reference_html":"Novel beta-barrel fold in the nuclear magnetic resonance structure of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus. <i> Almeida MS, Johnson MA, Herrmann T, Geralt M, Wüthrich K. </i> J Virol, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0003-2206-9968","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-20T09:12:08.893Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":87,"region_id":"DP02924r003","start":75,"term_id":"IDPO:0000002","statement":[{"text":"Increased flexibility of the polypeptide chain that causes reduced NOE intensities is found in the disordered loop between residues 75 and 87 and in the region of residues 94 to 103, which forms nonregular secondary structure with one γ-turn of residues 97 to 99 and a type II β-turn of residues 98 to 101 ​(Fig.1). ","type":"Results"}],"curator_id":"jbergier","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Julian Bergier","reference_id":"17202208","version":3,"reference_html":"Novel beta-barrel fold in the nuclear magnetic resonance structure of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus. <i> Almeida MS, Johnson MA, Herrmann T, Geralt M, Wüthrich K. </i> J Virol, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0003-2206-9968","cross_refs":[{"db":"BMRB","id":"7014"},{"db":"PDB","id":"2GDT"},{"db":"PDB","id":"2HSX"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-20T09:12:08.894Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":694009,"disprot_id":"DP02924","date":"2020-09-17T09:36:27.391Z","organism":"Human SARS coronavirus","regions_counter":4,"name":"Replicase polyprotein 1ab","dataset":["Viral proteins","RNA-binding proteins"],"UniParc":"UPI000019098F","uniref100":"UniRef100_P0C6X7","uniref90":"UniRef90_P0C6X7","uniref50":"UniRef50_P0C6X7","genes":[{"name":{"value":"rep"},"orfNames":[{"value":"1a-1b"}]}],"disorder_content":0.010745086950374664,"disprot_consensus":{"full":[{"start":1,"end":12,"type":"D"},{"start":75,"end":87,"type":"D"},{"start":129,"end":179,"type":"D"}],"Structural state":[{"start":1,"end":12,"type":"D"},{"start":75,"end":87,"type":"D"},{"start":129,"end":179,"type":"D"}]}},{"acc":"P0DTD1","sequence":"MESLVPGFNEKTHVQLSLPVLQVRDVLVRGFGDSVEEVLSEARQHLKDGTCGLVEVEKGVLPQLEQPYVFIKRSDARTAPHGHVMVELVAELEGIQYGRSGETLGVLVPHVGEIPVAYRKVLLRKNGNKGAGGHSYGADLKSFDLGDELGTDPYEDFQENWNTKHSSGVTRELMRELNGGAYTRYVDNNFCGPDGYPLECIKDLLARAGKASCTLSEQLDFIDTKRGVYCCREHEHEIAWYTERSEKSYELQTPFEIKLAKKFDTFNGECPNFVFPLNSIIKTIQPRVEKKKLDGFMGRIRSVYPVASPNECNQMCLSTLMKCDHCGETSWQTGDFVKATCEFCGTENLTKEGATTCGYLPQNAVVKIYCPACHNSEVGPEHSLAEYHNESGLKTILRKGGRTIAFGGCVFSYVGCHNKCAYWVPRASANIGCNHTGVVGEGSEGLNDNLLEILQKEKVNINIVGDFKLNEEIAIILASFSASTSAFVETVKGLDYKAFKQIVESCGNFKVTKGKAKKGAWNIGEQKSILSPLYAFASEAARVVRSIFSRTLETAQNSVRVLQKAAITILDGISQYSLRLIDAMMFTSDLATNNLVVMAYITGGVVQLTSQWLTNIFGTVYEKLKPVLDWLEEKFKEGVEFLRDGWEIVKFISTCACEIVGGQIVTCAKEIKESVQTFFKLVNKFLALCADSIIIGGAKLKALNLGETFVTHSKGLYRKCVKSREETGLLMPLKAPKEIIFLEGETLPTEVLTEEVVLKTGDLQPLEQPTSEAVEAPLVGTPVCINGLMLLEIKDTEKYCALAPNMMVTNNTFTLKGGAPTKVTFGDDTVIEVQGYKSVNITFELDERIDKVLNEKCSAYTVELGTEVNEFACVVADAVIKTLQPVSELLTPLGIDLDEWSMATYYLFDESGEFKLASHMYCSFYPPDEDEEEGDCEEEEFEPSTQYEYGTEDDYQGKPLEFGATSAALQPEEEQEEDWLDDDSQQTVGQQDGSEDNQTTTIQTIVEVQPQLEMELTPVVQTIEVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYDKLVSSFLEMKSEKQVEQKIAEIPKEEVKPFITESKPSVEQRKQDDKKIKACVEEVTTTLEETKFLTENLLLYIDINGNLHPDSATLVSDIDITFLKKDAPYIVGDVVQEGVLTAVVIPTKKAGGTTEMLAKALRKVPTDNYITTYPGQGLNGYTVEEAKTVLKKCKSAFYILPSIISNEKQEILGTVSWNLREMLAHAEETRKLMPVCVETKAIVSTIQRKYKGIKIQEGVVDYGARFYFYTSKTTVASLINTLNDLNETLVTMPLGYVTHGLNLEEAARYMRSLKVPATVSVSSPDAVTAYNGYLTSSSKTPEEHFIETISLAGSYKDWSYSGQSTQLGIEFLKRGDKSVYYTSNPTTFHLDGEVITFDNLKTLLSLREVRTIKVFTTVDNINLHTQVVDMSMTYGQQFGPTYLDGADVTKIKPHNSHEGKTFYVLPNDDTLRVEAFEYYHTTDPSFLGRYMSALNHTKKWKYPQVNGLTSIKWADNNCYLATALLTLQQIELKFNPPALQDAYYRARAGEAANFCALILAYCNKTVGELGDVRETMSYLFQHANLDSCKRVLNVVCKTCGQQQTTLKGVEAVMYMGTLSYEQFKKGVQIPCTCGKQATKYLVQQESPFVMMSAPPAQYELKHGTFTCASEYTGNYQCGHYKHITSKETLYCIDGALLTKSSEYKGPITDVFYKENSYTTTIKPVTYKLDGVVCTEIDPKLDNYYKKDNSYFTEQPIDLVPNQPYPNASFDNFKFVCDNIKFADDLNQLTGYKKPASRELKVTFFPDLNGDVVAIDYKHYTPSFKKGAKLLHKPIVWHVNNATNKATYKPNTWCIRCLWSTKPVETSNSFDVLKSEDAQGMDNLACEDLKPVSEEVVENPTIQKDVLECNVKTTEVVGDIILKPANNSLKITEEVGHTDLMAAYVDNSSLTIKKPNELSRVLGLKTLATHGLAAVNSVPWDTIANYAKPFLNKVVSTTTNIVTRCLNRVCTNYMPYFFTLLLQLCTFTRSTNSRIKASMPTTIAKNTVKSVGKFCLEASFNYLKSPNFSKLINIIIWFLLLSVCLGSLIYSTAALGVLMSNLGMPSYCTGYREGYLNSTNVTIATYCTGSIPCSVCLSGLDSLDTYPSLETIQITISSFKWDLTAFGLVAEWFLAYILFTRFFYVLGLAAIMQLFFSYFAVHFISNSWLMWLIINLVQMAPISAMVRMYIFFASFYYVWKSYVHVVDGCNSSTCMMCYKRNRATRVECTTIVNGVRRSFYVYANGGKGFCKLHNWNCVNCDTFCAGSTFISDEVARDLSLQFKRPINPTDQSSYIVDSVTVKNGSIHLYFDKAGQKTYERHSLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCEESSAKSASVYYSQLMCQPILLLDQALVSDVGDSAEVAVKMFDAYVNTFSSTFNVPMEKLKTLVATAEAELAKNVSLDNVLSTFISAARQGFVDSDVETKDVVECLKLSHQSDIEVTGDSCNNYMLTYNKVENMTPRDLGACIDCSARHINAQVAKSHNIALIWNVKDFMSLSEQLRKQIRSAAKKNNLPFKLTCATTRQVVNVVTTKIALKGGKIVNNWLKQLIKVTLVFLFVAAIFYLITPVHVMSKHTDFSSEIIGYKAIDGGVTRDIASTDTCFANKHADFDTWFSQRGGSYTNDKACPLIAAVITREVGFVVPGLPGTILRTTNGDFLHFLPRVFSAVGNICYTPSKLIEYTDFATSACVLAAECTIFKDASGKPVPYCYDTNVLEGSVAYESLRPDTRYVLMDGSIIQFPNTYLEGSVRVVTTFDSEYCRHGTCERSEAGVCVSTSGRWVLNNDYYRSLPGVFCGVDAVNLLTNMFTPLIQPIGALDISASIVAGGIVAIVVTCLAYYFMRFRRAFGEYSHVVAFNTLLFLMSFTVLCLTPVYSFLPGVYSVIYLYLTFYLTNDVSFLAHIQWMVMFTPLVPFWITIAYIICISTKHFYWFFSNYLKRRVVFNGVSFSTFEEAALCTFLLNKEMYLKLRSDVLLPLTQYNRYLALYNKYKYFSGAMDTTSYREAACCHLAKALNDFSNSGSDVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQSAVKRTIKGTHHWLLLTILTSLLVLVQSTQWSLFFFLYENAFLPFAMGIIAMSAFAMMFVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLDMVDTSLSGFKLKDCVMYASAVVLLILMTARTVYDDGARRVWTLMNVLTLVYKVYYGNALDQAISMWALIISVTSNYSGVVTTVMFLARGIVFMCVEYCPIFFITGNTLQCIMLVYCFLGYFCTCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKNSIDAFKLNIKLLGVGGKPCIKVATVQSKMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQGAVDINKLCEEMLDNRATLQAIASEFSSLPSYAAFATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRKLEKMADQAMTQMYKQARSEDKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVIPDYNTYKNTCDGTTFTYASALWEIQQVVDADSKIVQLSEISMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNTTKGGRFVLALLSDLQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQAGNATEVPANSTVLSFCAFAVDAAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHPNPKGFCDLKGKYVQIPTTCANDPVGFTLKNTVCTVCGMWKGYGCSCDQLREPMLQSADAQSFLNRVCGVSAARLTPCGTGTSTDVVYRAFDIYNDKVAGFAKFLKTNCCRFQEKDEDDNLIDSYFVVKRHTFSNYQHEETIYNLLKDCPAVAKHDFFKFRIDGDMVPHISRQRLTKYTMADLVYALRHFDEGNCDTLKEILVTYNCCDDDYFNKKDWYDFVENPDILRVYANLGERVRQALLKTVQFCDAMRNAGIVGVLTLDNQDLNGNWYDFGDFIQTTPGSGVPVVDSYYSLLMPILTLTRALTAESHVDTDLTKPYIKWDLLKYDFTEERLKLFDRYFKYWDQTYHPNCVNCLDDRCILHCANFNVLFSTVFPPTSFGPLVRKIFVDGVPFVVSTGYHFRELGVVHNQDVNLHSSRLSFKELLVYAADPAMHAASGNLLLDKRTTCFSVAALTNNVAFQTVKPGNFNKDFYDFAVSKGFFKEGSSVELKHFFFAQDGNAAISDYDYYRYNLPTMCDIRQLLFVVEVVDKYFDCYDGGCINANQVIVNNLDKSAGFPFNKWGKARLYYDSMSYEDQDALFAYTKRNVIPTITQMNLKYAISAKNRARTVAGVSICSTMTNRQFHQKLLKSIAATRGATVVIGTSKFYGGWHNMLKTVYSDVENPHLMGWDYPKCDRAMPNMLRIMASLVLARKHTTCCSLSHRFYRLANECAQVLSEMVMCGGSLYVKPGGTSSGDATTAYANSVFNICQAVTANVNALLSTDGNKIADKYVRNLQHRLYECLYRNRDVDTDFVNEFYAYLRKHFSMMILSDDAVVCFNSTYASQGLVASIKNFKSVLYYQNNVFMSEAKCWTETDLTKGPHEFCSQHTMLVKQGDDYVYLPYPDPSRILGAGCFVDDIVKTDGTLMIERFVSLAIDAYPLTKHPNQEYADVFHLYLQYIRKLHDELTGHMLDMYSVMLTNDNTSRYWEPEFYEAMYTPHTVLQAVGACVLCNSQTSLRCGACIRRPFLCCKCCYDHVISTSHKLVLSVNPYVCNAPGCDVTDVTQLYLGGMSYYCKSHKPPISFPLCANGQVFGLYKNTCVGSDNVTDFNAIATCDWTNAGDYILANTCTERLKLFAAETLKATEETFKLSYGIATVREVLSDRELHLSWEVGKPRPPLNRNYVFTGYRVTKNSKVQIGEYTFEKGDYGDAVVYRGTTTYKLNVGDYFVLTSHTVMPLSAPTLVPQEHYVRITGLYPTLNISDEFSSNVANYQKVGMQKYSTLQGPPGTGKSHFAIGLALYYPSARIVYTACSHAAVDALCEKALKYLPIDKCSRIIPARARVECFDKFKVNSTLEQYVFCTVNALPETTADIVVFDEISMATNYDLSVVNARLRAKHYVYIGDPAQLPAPRTLLTKGTLEPEYFNSVCRLMKTIGPDMFLGTCRRCPAEIVDTVSALVYDNKLKAHKDKSAQCFKMFYKGVITHDVSSAINRPQIGVVREFLTRNPAWRKAVFISPYNSQNAVASKILGLPTQTVDSSQGSEYDYVIFTQTTETAHSCNVNRFNVAITRAKVGILCIMSDRDLYDKLQFTSLEIPRRNVATLQAENVTGLFKDCSKVITGLHPTQAPTHLSVDTKFKTEGLCVDIPGIPKDMTYRRLISMMGFKMNYQVNGYPNMFITREEAIRHVRAWIGFDVEGCHATREAVGTNLPLQLGFSTGVNLVAVPTGYVDTPNNTDFSRVSAKPPPGDQFKHLIPLMYKGLPWNVVRIKIVQMLSDTLKNLSDRVVFVLWAHGFELTSMKYFVKIGPERTCCLCDRRATCFSTASDTYACWHHSIGFDYVYNPFMIDVQQWGFTGNLQSNHDLYCQVHGNAHVASCDAIMTRCLAVHECFVKRVDWTIEYPIIGDELKINAACRKVQHMVVKAALLADKFPVLHDIGNPKAIKCVPQADVEWKFYDAQPCSDKAYKIEELFYSYATHSDKFTDGVCLFWNCNVDRYPANSIVCRFDTRVLSNLNLPGCDGGSLYVNKHAFHTPAFDKSAFVNLKQLPFFYYSDSPCESHGKQVVSDIDYVPLKSATCITRCNLGGAVCRHHANEYRLYLDAYNMMISAGFSLWVYKQFDTYNLWNTFTRLQSLENVAFNVVNKGHFDGQQGEVPVSIINNTVYTKVDGVDVELFENKTTLPVNVAFELWAKRNIKPVPEVKILNNLGVDIAANTVIWDYKRDAPAHISTIGVCSMTDIAKKPTETICAPLTVFFDGRVDGQVDLFRNARNGVLITEGSVKGLQPSVGPKQASLNGVTLIGEAVKTQFNYYKKVDGVVQQLPETYFTQSRNLQEFKPRSQMEIDFLELAMDEFIERYKLEGYAFEHIVYGDFSHSQLGGLHLLIGLAKRFKESPFELEDFIPMDSTVKNYFITDAQTGSSKCVCSVIDLLLDDFVEIIKSQDLSVVSKVVKVTIDYTEISFMLWCKDGHVETFYPKLQSSQAWQPGVAMPNLYKMQRMLLEKCDLQNYGDSATLPKGIMMNVAKYTQLCQYLNTLTLAVPYNMRVIHFGAGSDKGVAPGTAVLRQWLPTGTLLVDSDLNDFVSDADSTLIGDCATVHTANKWDLIISDMYDPKTKNVTKENDSKEGFFTYICGFIQQKLALGGSVAIKITEHSWNADLYKLMGHFAWWTAFVTNVNASSSEAFLIGCNYLGKPREQIDGYVMHANYIFWRNTNPIQLSSYSLFDMSKFPLKLRGTAVMSLKEGQINDMILSLLSKGRLIIRENNRVVISSDVLVNN","creator":"grivas","dataset":["Viral proteins","Condensates-related proteins","RNA-binding proteins"],"date":"2020-09-17T11:03:53.862Z","disprot_id":"DP02925","features":{"pfam":[{"id":"PF00680","name":"Viral RNA-dependent RNA polymerase","start":4889,"end":5173},{"id":"PF01661","name":"Macro domain","start":1058,"end":1164},{"id":"PF05409","name":"Coronavirus endopeptidase C30","start":3292,"end":3575},{"id":"PF06460","name":"Coronavirus 2'-O-methyltransferase","start":6800,"end":7095},{"id":"PF06471","name":"Coronavirus proofreading exoribonuclease","start":5929,"end":6449},{"id":"PF06478","name":"Coronavirus RNA-dependent RNA polymerase, N-terminal","start":4407,"end":4758},{"id":"PF08710","name":"Coronavirus replicase NSP9","start":4141,"end":4253},{"id":"PF08715","name":"Coronavirus papain-like peptidase","start":1564,"end":1882},{"id":"PF08716","name":"Coronavirus replicase NSP7","start":3860,"end":3942},{"id":"PF08717","name":"Coronavirus replicase NSP8","start":3943,"end":4140},{"id":"PF09401","name":"Coronavirus RNA synthesis protein NSP10","start":4263,"end":4384},{"id":"PF11501","name":"Betacoronavirus replicase NSP1","start":9,"end":131},{"id":"PF11633","name":"Betacoronavirus single-stranded poly(A) binding domain","start":1351,"end":1493},{"id":"PF12124","name":"Betacoronavirus SUD-C domain","start":1498,"end":1561},{"id":"PF12379","name":"Betacoronavirus replicase NSP3, N-terminal","start":880,"end":1050},{"id":"PF13087","name":"AAA domain","start":5762,"end":5899},{"id":"PF16251","name":"Betacoronavirus nucleic acid-binding (NAB)","start":1899,"end":2029},{"id":"PF16348","name":"Coronavirus replicase NSP4, C-terminal","start":3166,"end":3263},{"id":"PF19211","name":"Coronavirus replicase NSP2, N-terminal","start":184,"end":423},{"id":"PF19213","name":"Coronavirus replicase NSP6","start":3599,"end":3859}],"gene3D":[]},"genes":[{"name":{"value":"rep","evidences":[],"_id":"685af523b4ac24d5329d96f7"},"synonyms":[],"olnNames":[],"orfNames":[{"value":"1a-1b","evidences":[],"_id":"685af523b4ac24d5329d96f8"}],"_id":"685af523b4ac24d5329d96f6"}],"length":7096,"name":"Replicase polyprotein 1ab","ncbi_taxon_id":2697049,"organism":"Severe acute respiratory syndrome coronavirus 2","regions_counter":40,"released":"2020_12","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Nidovirales","Cornidovirineae","Coronaviridae","Orthocoronavirinae","Betacoronavirus","Sarbecovirus"],"UniParc":"UPI00131F162F","uniref100":"UniRef100_P0DTD1","uniref50":"UniRef50_P0C6X7","uniref90":"UniRef90_P0DTD1","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6YVA","_id":"685af523b4ac24d5329d966d"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1782,"end":1796,"interaction_partner":[],"reference_html":"Papain-like protease regulates SARS-CoV-2 viral spread and innate immunity. <i> Shin D, Mukherjee R, Grewe D, Bojkova D, Baek K, Bhattacharya A, Schulz L, Widera M, Mehdipour AR, Tascher G, Geurink PP, Wilhelm A, van der Heden van Noort GJ, Ovaa H, Müller S, Knobeloch KP, Rajalingam K, Schulman BA, Cinatl J, Hummer G, Ciesek S, Dikic I. </i> Nature, 2020","reference_id":"32726803","region_id":"DP02925r003","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"Unstructured region belonging to the Papain-like proteinase (PL-PRO)","_id":"685af523b4ac24d5329d966c"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-07-27T13:34:40.164Z","_id":"685af523b4ac24d5329d966e"},"version":2,"_id":"685af523b4ac24d5329d966b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"7C2J","_id":"685af523b4ac24d5329d9672"},{"db":"PDB","id":"7C2I","_id":"685af523b4ac24d5329d9673"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":4254,"end":4270,"interaction_partner":[],"reference_html":"Crystal structure of SARS-CoV-2 nsp10/nsp16 2'-O-methylase and its implication on antiviral drug design. <i> Lin S, Chen H, Ye F, Chen Z, Yang F, Zheng Y, Cao Y, Qiao J, Yang S, Lu G. </i> Signal Transduct Target Ther, 2020","reference_id":"32728018","region_id":"DP02925r004","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"In addition, the α1′-helix of nsp10 was completely density-untraceable in our structure, which can be clearly observed in both SARS-CoV and MERS-CoV nsp10 (Fig. ​(Fig.1b1b).","_id":"685af523b4ac24d5329d9670"},{"type":"Curator statement","text":"Unstructured region belonging to the RNA-directed RNA polymerase (Pol/RdRp)","_id":"685af523b4ac24d5329d9671"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-07-27T13:32:53.999Z","_id":"685af523b4ac24d5329d9674"},"version":2,"_id":"685af523b4ac24d5329d966f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6M71","_id":"685af523b4ac24d5329d9677"},{"db":"PDB","id":"7BTF","_id":"685af523b4ac24d5329d9678"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006224","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":3931,"end":3942,"interaction_partner":[],"reference_html":"Structure of the RNA-dependent RNA polymerase from COVID-19 virus. <i> Gao Y, Yan L, Huang Y, Liu F, Zhao Y, Cao L, Wang T, Sun Q, Ming Z, Zhang L, Ge J, Zheng L, Zhang Y, Wang H, Zhu Y, Zhu C, Hu T, Hua T, Zhang B, Yang X, Li J, Yang H, Liu Z, Xu W, Guddat LW, Wang Q, Lou Z, Rao Z. </i> Science, 2020","reference_id":"32277040","region_id":"DP02925r005","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The defined region relies on examining the missing coordinates in both reported cryo-EM structures attached to the publication (7btf and 6m71) and it belongs to Non-structural protein 7 (nsp7).","_id":"685af523b4ac24d5329d9676"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-07-27T13:28:50.093Z","_id":"685af523b4ac24d5329d9679"},"version":2,"_id":"685af523b4ac24d5329d9675","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"7C2K","_id":"685af523b4ac24d5329d967c"},{"db":"PDB","id":"7BZF","_id":"685af523b4ac24d5329d967d"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006224","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":3932,"end":3942,"interaction_partner":[],"reference_html":"Structural Basis for RNA Replication by the SARS-CoV-2 Polymerase. <i> Wang Q, Wu J, Wang H, Gao Y, Liu Q, Mu A, Ji W, Yan L, Zhu Y, Zhu C, Fang X, Yang X, Huang Y, Gao H, Liu F, Ge J, Sun Q, Yang X, Xu W, Liu Z, Yang H, Lou Z, Jiang B, Guddat LW, Gong P, Rao Z. </i> Cell, 2020","reference_id":"32526208","region_id":"DP02925r006","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The defined region relies on examining the missing coordinates in both reported cryo-EM structures attached to the publication (7c2k and 7bzf) and it belongs to Non-structural protein 7 (nsp7).","_id":"685af523b4ac24d5329d967b"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-07-27T13:28:48.836Z","_id":"685af523b4ac24d5329d967e"},"version":2,"_id":"685af523b4ac24d5329d967a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"7BZF","_id":"685af523b4ac24d5329d9681"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006224","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":3943,"end":4020,"interaction_partner":[],"reference_html":"Structural Basis for RNA Replication by the SARS-CoV-2 Polymerase. <i> Wang Q, Wu J, Wang H, Gao Y, Liu Q, Mu A, Ji W, Yan L, Zhu Y, Zhu C, Fang X, Yang X, Huang Y, Gao H, Liu F, Ge J, Sun Q, Yang X, Xu W, Liu Z, Yang H, Lou Z, Jiang B, Guddat LW, Gong P, Rao Z. </i> Cell, 2020","reference_id":"32526208","region_id":"DP02925r007","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The defined region relies on examining the missing coordinates in the reported cryo-EM structure of the RNA-dependent RNA polymerase post-translocated catalytic complex - attached to the publication - and it belongs to Non-structural protein 8 (nsp8).","_id":"685af523b4ac24d5329d9680"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-07-27T13:20:44.162Z","_id":"685af523b4ac24d5329d9682"},"version":2,"_id":"685af523b4ac24d5329d967f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"7BZF","_id":"685af523b4ac24d5329d9685"},{"db":"PDB","id":"7C2K","_id":"685af523b4ac24d5329d9686"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"IDA","ec_id":"ECO:0006208","ec_name":"cryogenic electron microscopy evidence used in manual assertion","ec_ontology":"ECO","start":3995,"end":4020,"interaction_partner":[],"reference_html":"Structural Basis for RNA Replication by the SARS-CoV-2 Polymerase. <i> Wang Q, Wu J, Wang H, Gao Y, Liu Q, Mu A, Ji W, Yan L, Zhu Y, Zhu C, Fang X, Yang X, Huang Y, Gao H, Liu F, Ge J, Sun Q, Yang X, Xu W, Liu Z, Yang H, Lou Z, Jiang B, Guddat LW, Gong P, Rao Z. </i> Cell, 2020","reference_id":"32526208","region_id":"DP02925r008","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The defined region relies on examining the missing coordinates in both reported cryo-EM structures of the RNA-dependent RNA polymerase of the pre-translocated and post-translocated catalytic complex - attached to the publication - and it belongs to Non-structural protein 8 (nsp8).","_id":"685af523b4ac24d5329d9684"}],"states_connection":[],"term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-07-27T13:40:12.769Z","_id":"685af523b4ac24d5329d9687"},"version":2,"_id":"685af523b4ac24d5329d9683","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6YYT","_id":"685af523b4ac24d5329d968a"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006224","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":3932,"end":3942,"interaction_partner":[],"reference_html":"Structure of replicating SARS-CoV-2 polymerase. <i> Hillen HS, Kokic G, Farnung L, Dienemann C, Tegunov D, Cramer P. </i> Nature, 2020","reference_id":"32438371","region_id":"DP02925r009","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The defined region relies on examining the missing coordinates in the reported cryo-EM structure of replicating SARS-CoV-2 polymerase - attached to the publication - and it belongs to Non-structural protein 7 (nsp7).","_id":"685af523b4ac24d5329d9689"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-07-27T13:24:40.103Z","_id":"685af523b4ac24d5329d968b"},"version":2,"_id":"685af523b4ac24d5329d9688","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6YYT","_id":"685af523b4ac24d5329d9690"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006208","ec_name":"cryogenic electron microscopy evidence used in manual assertion","ec_ontology":"ECO","start":3982,"end":4007,"interaction_partner":[],"reference_html":"Structure of replicating SARS-CoV-2 polymerase. <i> Hillen HS, Kokic G, Farnung L, Dienemann C, Tegunov D, Cramer P. </i> Nature, 2020","reference_id":"32438371","region_id":"DP02925r010","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"The protruding, exiting RNA duplex is flanked by long α-helical extensions that are formed by the highly conserved17 N-terminal regions in the two nsp8 subunits (Figs. 2, 3). These prominent nsp8 extensions reach up to 28 base pairs away from the active site and use positively charged residues that are positioned to interact with the RNA backbones (Fig. 3).","_id":"685af523b4ac24d5329d968d"},{"type":"Article","text":"The two nsp8 extensions differ with respect to their RNA interactions, which also argues for sequence-independent binding. The two nsp8 copies adopt different structures in the RdRp complex, and interact differently with nsp7 and nsp12 subdomains (Extended Data Fig. 3c). The nsp8 extensions also adopt different structures in crystals of nsp8–nsp7 complexes17,18, and are mobile in free RdRp15,16. This indicates that the nsp8 extensions are flexible in the RdRp complex and become ordered when an RNA duplex exits the enzyme.","_id":"685af523b4ac24d5329d968e"},{"type":"Curator statement","text":"The defined binding region mainly composed by positively charged residues relies on examining the reported cryo-EM structure attached to the publication along with Figure 3. ","_id":"685af523b4ac24d5329d968f"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_id":"GO:0003723","term_is_binding":true,"term_is_obsolete":false,"term_name":"RNA binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-07-27T13:37:58.907Z","_id":"685af523b4ac24d5329d9691"},"version":3,"_id":"685af523b4ac24d5329d968c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6YYT","_id":"685af523b4ac24d5329d9695"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"IDA","ec_id":"ECO:0006208","ec_name":"cryogenic electron microscopy evidence used in manual assertion","ec_ontology":"ECO","start":3948,"end":4020,"interaction_partner":[],"reference_html":"Structure of replicating SARS-CoV-2 polymerase. <i> Hillen HS, Kokic G, Farnung L, Dienemann C, Tegunov D, Cramer P. </i> Nature, 2020","reference_id":"32438371","region_id":"DP02925r011","released":"2022_03","sample":[],"statement":[{"type":"Article","text":"The protruding, exiting RNA duplex is flanked by long α-helical extensions that are formed by the highly conserved17 N-terminal regions in the two nsp8 subunits (Figs. 2, 3). These prominent nsp8 extensions reach up to 28 base pairs away from the active site and use positively charged residues that are positioned to interact with the RNA backbones (Fig. 3).","_id":"685af523b4ac24d5329d9693"},{"type":"Article","text":"The two nsp8 extensions differ with respect to their RNA interactions, which also argues for sequence-independent binding. The two nsp8 copies adopt different structures in the RdRp complex, and interact differently with nsp7 and nsp12 subdomains (Extended Data Fig. 3c). The nsp8 extensions also adopt different structures in crystals of nsp8–nsp7 complexes17,18, and are mobile in free RdRp15,16. This indicates that the nsp8 extensions are flexible in the RdRp complex and become ordered when an RNA duplex exits the enzyme.","_id":"685af523b4ac24d5329d9694"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-07-27T13:35:55.788Z","_id":"685af523b4ac24d5329d9696"},"version":2,"_id":"685af523b4ac24d5329d9692","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6ZOK","_id":"685af523b4ac24d5329d969b"},{"db":"PDB","id":"6ZOJ","_id":"685af523b4ac24d5329d969c"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006224","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":147,"interaction_partner":[],"reference_html":"SARS-CoV-2 Nsp1 binds the ribosomal mRNA channel to inhibit translation. <i> Schubert K, Karousis ED, Jomaa A, Scaiola A, Echeverria B, Gurzeler LA, Leibundgut M, Thiel V, Mühlemann O, Ban N. </i> Nat Struct Mol Biol, 2020","reference_id":"32908316","region_id":"DP02925r012","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"This may correspond to the flexibly disposed N-terminal domain of Nsp1 considering the 20-amino acid unstructured linker between the N- and C-terminal domains (Fig. 2e and Supplementary Fig. 1).","_id":"685af523b4ac24d5329d9698"},{"type":"Figure","text":"The C-terminal domain of Nsp1 binds to the mRNA entry site of 40S (red), while the N-terminal domain (gray) is flexibly disposed.","_id":"685af523b4ac24d5329d9699"},{"type":"Results","text":"These results also agree with our structural findings that the C-terminal domain of Nsp1 is responsible for specific contacts with the ribosome, whereas the N-terminal domain is flexibly disposed.","_id":"685af523b4ac24d5329d969a"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-07T10:13:09.549Z","_id":"685af523b4ac24d5329d969d"},"version":3,"_id":"685af523b4ac24d5329d9697","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"6ZOK","_id":"685af523b4ac24d5329d96a1"},{"db":"PDB","id":"6ZOJ","_id":"685af523b4ac24d5329d96a2"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006208","ec_name":"cryogenic electron microscopy evidence used in manual assertion","ec_ontology":"ECO","start":129,"end":147,"interaction_partner":[],"reference_html":"SARS-CoV-2 Nsp1 binds the ribosomal mRNA channel to inhibit translation. <i> Schubert K, Karousis ED, Jomaa A, Scaiola A, Echeverria B, Gurzeler LA, Leibundgut M, Thiel V, Mühlemann O, Ban N. </i> Nat Struct Mol Biol, 2020","reference_id":"32908316","region_id":"DP02925r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"This may correspond to the flexibly disposed N-terminal domain of Nsp1 considering the 20-amino acid unstructured linker between the N- and C-terminal domains (Fig. 2e and Supplementary Fig. 1).","_id":"685af523b4ac24d5329d969f"},{"type":"Curator statement","text":"Region 129-147 correspond to the flexible linker connecting the unstructured N-terminal domain of Nsp1 and its C-terminal domain, as also shown in Fig. 2e. ","_id":"685af523b4ac24d5329d96a0"}],"states_connection":[],"term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-07T10:13:58.724Z","_id":"685af523b4ac24d5329d96a3"},"version":4,"_id":"685af523b4ac24d5329d969e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"7C2J","_id":"685af523b4ac24d5329d96bf"},{"db":"PDB","id":"7C2I","_id":"685af523b4ac24d5329d96c0"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":4254,"end":4271,"interaction_partner":[],"reference_html":"Crystal structure of SARS-CoV-2 nsp10/nsp16 2'-O-methylase and its implication on antiviral drug design. <i> Lin S, Chen H, Ye F, Chen Z, Yang F, Zheng Y, Cao Y, Qiao J, Yang S, Lu G. </i> Signal Transduct Target Ther, 2020","reference_id":"32728018","region_id":"DP02925r018","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The defined region relies on examining the missing coordinates in both reported X-ray structures attached to the publication (7C2J and 7C2I) and it is also missing in other unpublished structures of the Non-structural protein 10 (nsp10).","_id":"685af523b4ac24d5329d96be"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-07-27T10:02:27.654Z","_id":"685af523b4ac24d5329d96c1"},"version":2,"_id":"685af523b4ac24d5329d96bd","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"50337","_id":"685af523b4ac24d5329d96c3"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":3837,"end":3846,"interaction_partner":[],"reference_html":"<sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N backbone and side chain chemical shift assignments of the SARS-CoV-2 non-structural protein 7. <i> Tonelli M, Rienstra C, Anderson TK, Kirchdoerfer R, Henzler-Wildman K. </i> Biomol NMR Assign, 2021","reference_id":"33219414","region_id":"DP02925r019","released":"2022_03","sample":[],"statement":[{"type":"Curator statement","text":"The region is disordered based upon Fig.2.","_id":"685af523b4ac24d5329d96c4"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-12-07T09:30:37.963Z","_id":"685af523b4ac24d5329d96c5"},"version":1,"_id":"685af523b4ac24d5329d96c2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","date":"2022-04-06T14:39:56.058Z","disprot_namespace":"Structural state","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":3660,"end":3681,"interaction_partner":[],"reference_html":"Investigating the conformational dynamics of SARS-CoV-2 NSP6 protein with emphasis on non-transmembrane 91-112 & 231-290 regions. <i> Kumar A, Kumar P, Saumya KU, Giri R. </i> Microb Pathog, 2021","reference_id":"34648928","region_id":"DP02925r020","released":"2022_06","sample":[],"statement":[{"type":"Results","text":"Circular dichroism spectroscopy was used to monitor the conformational dynamics of NSP6 (91–112). In physiological pH buffer conditions, the peptide showed strong negative ellipticity at 198 nm, characteristic of random coil conformations (Fig. 4A).","_id":"685af523b4ac24d5329d96c7"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2022-04-07T08:01:30.806Z","_id":"685af523b4ac24d5329d96c8"},"version":0,"_id":"685af523b4ac24d5329d96c6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","date":"2022-04-07T16:26:12.838Z","disprot_namespace":"Structural transition","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":3660,"end":3681,"interaction_partner":[],"reference_html":"Investigating the conformational dynamics of SARS-CoV-2 NSP6 protein with emphasis on non-transmembrane 91-112 & 231-290 regions. <i> Kumar A, Kumar P, Saumya KU, Giri R. </i> Microb Pathog, 2021","reference_id":"34648928","region_id":"DP02925r021","released":"2022_06","sample":[{"db":"ChEBI","deviation":"not relevant","entry_name":"2,2,2-trifluoroethanol","id":"42330","statements":[{"type":"Methods","text":"The peptide was kept in organic solvents (TFE) with increasing concentration from 0 to 50%, and far-UV (190–240 nm) spectra were recorded in 1 mm quartz cuvette.","_id":"685af523b4ac24d5329d96cd"}],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d96cc"},{"db":"ChEBI","deviation":"not relevant","entry_name":"sodium dodecyl sulfate","id":"8984","statements":[{"type":"Figure","text":"In the presence of SDS (B) and TFE (C) peptide gained helical conformation at 208 nm and 222 nm.","_id":"685af523b4ac24d5329d96cf"}],"term_id":"IDPO:00488","term_name":"interacting lipid","unit_id":"UO:0000063","unit_name":"mM","value":1,"_id":"685af523b4ac24d5329d96ce"},{"db":"ChEBI","deviation":"not relevant","entry_name":"1,2-dioleoyl-sn-glycero-3-phospho-L-serine","id":"60568","statements":[{"type":"Figure","text":"The negatively charged liposome DOPS induces partial helical conformation in the peptide.","_id":"685af523b4ac24d5329d96d1"}],"term_id":"IDPO:00488","term_name":"interacting lipid","unit_id":"UO:0000063","unit_name":"mM","value":7.5,"_id":"685af523b4ac24d5329d96d0"}],"statement":[{"type":"Results","text":"Interestingly, in the presence of organic solvent (TFE) and SDS, peptide showed negative ellipticity at 208 nm and 222 nm, which showed a gain in the helical conformation of peptide (Fig. 4B & C). The results showed that the surrounding environment has a strong role in conformational dynamics of NSP6 91–112 region. Organic solvent and SDS are well-acknowledged for their hydrophobic and biological membrane mimic properties, respectively","_id":"685af523b4ac24d5329d96ca"},{"type":"Results","text":"to see the impact of membrane-mediated environment on the NSP6 91–112 region, we have used DOPS liposome. The NSP6 91–112 region acquires partial helical conformation in the presence of DOPS (Fig. 4D).","_id":"685af523b4ac24d5329d96cb"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2022-04-08T07:18:02.462Z","_id":"685af523b4ac24d5329d96d2"},"version":0,"_id":"685af523b4ac24d5329d96c9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","date":"2022-04-07T16:29:50.195Z","disprot_namespace":"Structural transition","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":3660,"end":3681,"interaction_partner":[],"reference_html":"Investigating the conformational dynamics of SARS-CoV-2 NSP6 protein with emphasis on non-transmembrane 91-112 & 231-290 regions. <i> Kumar A, Kumar P, Saumya KU, Giri R. </i> Microb Pathog, 2021","reference_id":"34648928","region_id":"DP02925r022","released":"2022_06","sample":[{"db":"ChEBI","deviation":"not relevant","entry_name":"2,2,2-trifluoroethanol","id":"42330","statements":[{"type":"Figure","text":" In the presence of SDS (E) and TFE (F) peptide showed significant blue shift under the influence of hydrophobic environment.","_id":"685af523b4ac24d5329d96d7"}],"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"685af523b4ac24d5329d96d6"},{"db":"ChEBI","deviation":"not relevant","entry_name":"sodium dodecyl sulfate","id":"8984","statements":[{"type":"Figure","text":" In the presence of SDS (E) and TFE (F) peptide showed significant blue shift under the influence of hydrophobic environment.","_id":"685af523b4ac24d5329d96d9"}],"term_id":"IDPO:00488","term_name":"interacting lipid","unit_id":"UO:0000063","unit_name":"mM","value":1,"_id":"685af523b4ac24d5329d96d8"}],"statement":[{"type":"Results","text":"we have used the intrinsic tryptophan present in this peptide as a fluorescence probe to monitor the tertiary structure changes in the presence of SDS and TFE (Fig. 4E & F). Trp in the presence of non-polar/hydrophobic environment gives rise to a significant blue shift [33]. Furthermore, we have observed that in the presence of TFE and SDS peptide showed blue shift, which again confirms the tertiary structural changes are happening to the peptide in these conditions and following the results obtained from the CD spectroscopy.","_id":"685af523b4ac24d5329d96d4"},{"type":"Figure","text":"In the presence of SDS (E) and TFE (F) peptide showed significant blue shift under the influence of hydrophobic environment.","_id":"685af523b4ac24d5329d96d5"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2022-04-08T07:18:11.878Z","_id":"685af523b4ac24d5329d96da"},"version":0,"_id":"685af523b4ac24d5329d96d3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","date":"2022-04-06T15:30:05.717Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":3660,"end":3681,"interaction_partner":[{"db":"ChEBI","id":"8984","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d96dc"}],"reference_html":"Investigating the conformational dynamics of SARS-CoV-2 NSP6 protein with emphasis on non-transmembrane 91-112 & 231-290 regions. <i> Kumar A, Kumar P, Saumya KU, Giri R. </i> Microb Pathog, 2021","reference_id":"34648928","region_id":"DP02925r023","released":"2022_06","sample":[],"statement":[{"type":"Results","text":"we have used the intrinsic tryptophan present in this peptide as a fluorescence probe to monitor the tertiary structure changes in the presence of SDS and TFE (Fig. 4E & F). Trp in the presence of non-polar/hydrophobic environment gives rise to a significant blue shift [33]. Furthermore, we have observed that in the presence of TFE and SDS peptide showed blue shift, which again confirms the tertiary structural changes are happening to the peptide in these conditions and following the results obtained from the CD spectroscopy.","_id":"685af523b4ac24d5329d96dd"},{"type":"Figure","text":"In the presence of SDS (E) and TFE (F) peptide showed significant blue shift under the influence of hydrophobic environment.","_id":"685af523b4ac24d5329d96de"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_id":"GO:0008289","term_is_obsolete":false,"term_name":"lipid binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2022-04-07T08:03:03.076Z","_id":"685af523b4ac24d5329d96df"},"version":0,"_id":"685af523b4ac24d5329d96db","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","date":"2022-04-06T15:36:03.640Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":3660,"end":3681,"interaction_partner":[{"db":"ChEBI","id":"8984","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d96e1"},{"db":"ChEBI","id":"60568","operator":"or","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d96e2"}],"reference_html":"Investigating the conformational dynamics of SARS-CoV-2 NSP6 protein with emphasis on non-transmembrane 91-112 & 231-290 regions. <i> Kumar A, Kumar P, Saumya KU, Giri R. </i> Microb Pathog, 2021","reference_id":"34648928","region_id":"DP02925r024","released":"2022_06","sample":[],"statement":[{"type":"Results","text":"Interestingly, in the presence of organic solvent (TFE) and SDS, peptide showed negative ellipticity at 208 nm and 222 nm, which showed a gain in the helical conformation of peptide (Fig. 4B & C). The results showed that the surrounding environment has a strong role in conformational dynamics of NSP6 91–112 region. Organic solvent and SDS are well-acknowledged for their hydrophobic and biological membrane mimic properties, respectively","_id":"685af523b4ac24d5329d96e3"},{"type":"Results","text":"to see the impact of membrane-mediated environment on the NSP6 91–112 region, we have used DOPS liposome. The NSP6 91–112 region acquires partial helical conformation in the presence of DOPS (Fig. 4D).","_id":"685af523b4ac24d5329d96e4"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_id":"GO:0008289","term_is_obsolete":false,"term_name":"lipid binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2022-04-07T08:02:57.415Z","_id":"685af523b4ac24d5329d96e5"},"version":0,"_id":"685af523b4ac24d5329d96e0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-21T12:34:04.896Z","disprot_namespace":"Structural state","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":148,"end":180,"interaction_partner":[],"reference_html":"Copper(II) Binding to the Intrinsically Disordered C-Terminal Peptide of SARS-CoV-2 Virulence Factor Nsp1. <i> Morales M, Ravanfar R, Oyala PH, Gray HB, Winkler JR. </i> Inorg Chem, 2022","reference_id":"35658408","region_id":"DP02925r025","released":"2022_06","sample":[],"statement":[{"type":"Article","text":"The far-UV circular dichroism (CD) spectrum of Nsp1-CT features a negative ellipticity minimum at 200 nm and a negative ellipticity shoulder near 230 nm (Figure S1). The molar ellipticity minimum at 200 nm is about 40% of that expected for a random coil, suggesting an offsetting positive contribution from β-sheet or turn structures. (23) Decomposition of the spectrum into three components (α-helix, β-sheet, and random coil) indicates that the peptide adopts a dominant random coil configuration with an admixture of β-sheet and minimal (<5%) α-helix.","_id":"685af523b4ac24d5329d96e7"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-21T13:40:13.553Z","_id":"685af523b4ac24d5329d96e8"},"version":0,"_id":"685af523b4ac24d5329d96e6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-16T19:31:49.012Z","disprot_namespace":"Structural state","ec_id":"ECO:0001183","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","ec_ontology":"ECO","start":148,"end":180,"interaction_partner":[],"reference_html":"Copper(II) Binding to the Intrinsically Disordered C-Terminal Peptide of SARS-CoV-2 Virulence Factor Nsp1. <i> Morales M, Ravanfar R, Oyala PH, Gray HB, Winkler JR. </i> Inorg Chem, 2022","reference_id":"35658408","region_id":"DP02925r026","released":"2022_06","sample":[],"statement":[{"type":"Article","text":"Employing laser spectroscopy, including time-resolved fluorescence energy transfer (TR-FRET), we have obtained nanosecond snapshots of rapidly fluctuating conformations in the Nsp1 C-terminal peptide (Nsp1-CT).","_id":"685af523b4ac24d5329d96ea"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-17T06:46:46.840Z","_id":"685af523b4ac24d5329d96eb"},"version":0,"_id":"685af523b4ac24d5329d96e9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"position":null,"statements":[],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.His165Ala","_id":"685af523b4ac24d5329d96ef"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-16T19:34:19.330Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001183","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","ec_ontology":"ECO","start":163,"end":167,"interaction_partner":[{"db":"ChEBI","id":"29036","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d96ed"}],"reference_html":"Copper(II) Binding to the Intrinsically Disordered C-Terminal Peptide of SARS-CoV-2 Virulence Factor Nsp1. <i> Morales M, Ravanfar R, Oyala PH, Gray HB, Winkler JR. </i> Inorg Chem, 2022","reference_id":"35658408","region_id":"DP02925r027","released":"2022_06","sample":[],"sequence_construct":"ELGTDPYEDFQENWNTKASSGVTRELMRELNGG","statement":[{"type":"Article","text":"Nsp1-CT W161 fluorescence is sensitive to low concentrations of Cu(II). At 30 μM peptide concentration, addition of 1 mol equiv of aquo Cu(II) leads to an ∼25% reduction in W161 fluorescence intensity. Cu(II) also produces a systematic reduction in the effective W161 fluorescence lifetime. Treating the reduction in ⟨τ⟩ with a single Cu-binding-site model leads to a dissociation constant of 9.7 μM (pH 6.5) (Figure 3). *W161 fluorescence in an Nsp1 variant in which H165 is replaced by alanine (Nsp1-CT(H165A)) is only weakly quenched by Cu(II) with an apparent dissociation constant of 106 μM (Figure S2). This result is consistent with the relative Cu(II) binding constants of imidazole (104.02 M–1) and a carboxylate (acetate, 101.82 M–1). (16) Importantly, the *W161 quenching data clearly implicate H165 as the site of Cu(II) coordination to Nsp1-CT.","_id":"685af523b4ac24d5329d96ee"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a copper (Cu) ion.\" [GOC:ai]","term_id":"GO:0005507","term_is_obsolete":false,"term_name":"copper ion binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-17T06:45:12.308Z","_id":"685af523b4ac24d5329d96f0"},"version":0,"_id":"685af523b4ac24d5329d96ec","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[{"start":null,"end":null,"position":null,"statements":[],"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.His165Ala","_id":"685af523b4ac24d5329d96f2"}],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-06-21T12:39:04.236Z","disprot_namespace":"Disorder function","ec_go":"IMP","ec_id":"ECO:0000315","ec_name":"mutant phenotype evidence used in manual assertion","ec_ontology":"ECO","start":163,"end":167,"interaction_partner":[{"db":"ChEBI","id":"29036","operator":null,"partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d96f3"}],"reference_html":"Copper(II) Binding to the Intrinsically Disordered C-Terminal Peptide of SARS-CoV-2 Virulence Factor Nsp1. <i> Morales M, Ravanfar R, Oyala PH, Gray HB, Winkler JR. </i> Inorg Chem, 2022","reference_id":"35658408","region_id":"DP02925r028","released":"2022_06","sample":[],"sequence_construct":"ELGTDPYEDFQENWNTKASSGVTRELMRELNGG","statement":[{"type":"Results","text":"Nsp1-CT W161 fluorescence is sensitive to low concentrations of Cu(II). At 30 μM peptide concentration, addition of 1 mol equiv of aquo Cu(II) leads to an ∼25% reduction in W161 fluorescence intensity. Cu(II) also produces a systematic reduction in the effective W161 fluorescence lifetime. Treating the reduction in ⟨τ⟩ with a single Cu-binding-site model leads to a dissociation constant of 9.7 μM (pH 6.5) (Figure 3). *W161 fluorescence in an Nsp1 variant in which H165 is replaced by alanine (Nsp1-CT(H165A)) is only weakly quenched by Cu(II) with an apparent dissociation constant of 106 μM (Figure S2). This result is consistent with the relative Cu(II) binding constants of imidazole (104.02 M–1) and a carboxylate (acetate, 101.82 M–1). (16) Importantly, the *W161 quenching data clearly implicate H165 as the site of Cu(II) coordination to Nsp1-CT.","_id":"685af523b4ac24d5329d96f4"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a copper (Cu) ion.\" [GOC:ai]","term_id":"GO:0005507","term_is_obsolete":false,"term_name":"copper ion binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-21T13:40:17.907Z","_id":"685af523b4ac24d5329d96f5"},"version":0,"_id":"685af523b4ac24d5329d96f1","reference_source":"pmid"}],"__v":0,"disorder_content":0.04720969560315671,"disprot_consensus":{"full":[{"start":1,"end":180,"type":"D"},{"start":1782,"end":1796,"type":"D"},{"start":3660,"end":3681,"type":"T"},{"start":3837,"end":3846,"type":"D"},{"start":3931,"end":3947,"type":"D"},{"start":3948,"end":4020,"type":"T"},{"start":4254,"end":4271,"type":"D"}],"Structural state":[{"start":1,"end":180,"type":"D"},{"start":1782,"end":1796,"type":"D"},{"start":3660,"end":3681,"type":"D"},{"start":3837,"end":3846,"type":"D"},{"start":3931,"end":4020,"type":"D"},{"start":4254,"end":4271,"type":"D"}],"Structural transition":[{"start":3660,"end":3681,"type":"T"},{"start":3948,"end":4020,"type":"T"}],"Molecular function":[{"start":163,"end":167,"type":"F"},{"start":3660,"end":3681,"type":"F"},{"start":3982,"end":4007,"type":"F"}],"Disorder function":[{"start":129,"end":147,"type":"F"}]}},{"acc":"A8BB85","features":{"pfam":[{"id":"PF00696","name":"Amino acid kinase family","start":5,"end":294}],"gene3D":[]},"creator":"fquaglia","taxonomy":["Eukaryota","Metamonada","Diplomonadida","Hexamitidae","Giardiinae","Giardia"],"sequence":"MSAGKTVVIALGGNAMLQAKEKGDYDTQRKNVEIAASEIYKIHKAGYKVVLTSGNGPQVGAIKLQNQAAAGVSPEMPLHVCGAMSQGFIGYMMSQAMDNVFCANNEPANCVTCVTQTLVDPKDQAFTNPTKPVGRFYTEQEAKDLMAANPGKILREDAGRGWRVVVPSPRPLEIVEYGVIKTLIDNNVLVICTNGGGIPCKRENKVISGVDAVIDKDLATSLLAKTLNSDYLMILTDVLNACINYKKPDERKLEEIKLSEILALEKDGHFAAGSMGPKVRAAIEFTQATGKMSIITSLSTAVDALNGKCGTRIIKD","length":316,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":160,"region_id":"DP02926r001","start":135,"term_id":"IDPO:0000002","statement":[{"text":"In addition, no electron density is associated with the following surface residues: 18–19, 135–160 and 272–273 in molecule A, 138–152, 244–245 and 271–272 in molecule B, 138–161 and 247–250 in molecule C, and 140–152, 243–249 and 271–272 in molecule D.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20383005","version":2,"reference_html":"X-ray structure and characterization of carbamate kinase from the human parasite Giardia lamblia. <i> Galkin A, Kulakova L, Wu R, Nash TE, Dunaway-Mariano D, Herzberg O. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3KZF"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_06","ncbi_taxon_id":184922,"disprot_id":"DP02926","date":"2020-09-23T13:43:02.840Z","organism":"Giardia intestinalis (strain ATCC 50803 / WB clone C6)","regions_counter":1,"name":"Carbamate kinase","dataset":[],"UniParc":"UPI000018BF46","uniref100":"UniRef100_A8BB85","uniref90":"UniRef90_O97438","uniref50":"UniRef50_O97438","genes":[{"orfNames":[{"value":"GL50803_0016453","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"KAE8302059.1","url":"https://www.ebi.ac.uk/ena/browser/view/KAE8302059.1"}}]},{"value":"GL50803_16453","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EDO80558.1","url":"https://www.ebi.ac.uk/ena/browser/view/EDO80558.1"}}]}]}],"alphafold_very_low_content":0,"disorder_content":0.08227848101265822,"disprot_consensus":{"full":[{"start":135,"end":160,"type":"D"}],"Structural state":[{"start":135,"end":160,"type":"D"}]}},{"acc":"Q26997","features":{"pfam":[{"id":"PF00156","name":"Phosphoribosyl transferase domain","start":49,"end":207}],"gene3D":[]},"creator":"fquaglia","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Conoidasida","Coccidia","Eucoccidiorida","Eimeriorina","Sarcocystidae","Toxoplasma"],"sequence":"MASKPIEDYGKGKGRIEPMYIPDNTFYNADDFLVPPHCKPYIDKILLPGGLVKDRVEKLAYDIHRTYFGEELHIICILKGSRGFFNLLIDYLATIQKYSGRESSVPPFFEHYVRLKSYQNDNSTGQLTVLSDDLSIFRDKHVLIVEDIVDTGFTLTEFGERLKAVGPKSMRIATLVEKRTDRSNSLKGDFVGFSIEDVWIVGCCYDFNEMFRDFDHVAVLSDAARKKFEK","length":230,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":126,"region_id":"DP02927r001","start":116,"term_id":"IDPO:0000002","statement":[{"text":"In the structure of the enzyme bound to its product, a long flexible loop (residues 115-126) is located away from the active site.","type":"Abstract"},{"text":"There is no density for residues 116-126 in subunits B, C and D, indicating that these residues are disordered.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"8836106","version":2,"reference_html":"Crystal structures of Toxoplasma gondii HGXPRTase reveal the catalytic role of a long flexible loop. <i> Schumacher MA, Carter D, Roos DS, Ullman B, Brennan RG. </i> Nat Struct Biol, 1996","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"1DBR"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","ncbi_taxon_id":5811,"disprot_id":"DP02927","date":"2020-09-23T14:06:49.626Z","organism":"Toxoplasma gondii","regions_counter":1,"name":"Hypoxanthine-guanine-xanthine phosphoribosyltransferase","dataset":[],"UniParc":"UPI0000000538","uniref100":"UniRef100_Q26997","uniref90":"UniRef90_Q26997","uniref50":"UniRef50_Q26997","genes":[{"name":{"value":"HPRT"}}],"alphafold_very_low_content":0.017391304347826087,"disorder_content":0.04782608695652174,"disprot_consensus":{"full":[{"start":116,"end":126,"type":"D"}],"Structural state":[{"start":116,"end":126,"type":"D"}]}},{"acc":"A0A220GHA5","features":{"pfam":[],"gene3D":[]},"creator":"fquaglia","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Uroviricota","Caudoviricetes","Caudovirales","Siphoviridae","Moineauvirus","unclassified Moineauvirus"],"sequence":"MAYGKSRYNSYRKRSFNRSNKQRREYAQEMDRLEKAFENLDGWYLSSMKDSAYKDFGKYEIRLSNHSADNKYHDLENGRLIVNIKASKLNFVDIIENKLDKIIEKIDKLDLDKYRFINATNLEHDIKCYYKGFKTKKEVI","length":140,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":22,"region_id":"DP02928r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"Here, we report the solution structure of AcrIIA5, which features a novel α/β fold connected to an N-terminal intrinsically disordered region (IDR).","type":"Abstract"},{"text":"Here, we show that AcrIIA5 adopts a novel α/β fold preceded by an intrinsically disordered region (IDR).","type":"Introduction"},{"text":"AcrIIA5 comprises seven β-strands and two α-helices, preceded by an extended N-terminal disordered region (Figure 1B).","type":"Results"},{"text":"We note that the N-terminal 22 residues of AcrIIA5 display largely disordered backbone conformations (Figure 2A).","type":"Results"},{"text":"In addition, the N-terminal tail region exhibited a narrow dispersion of backbone chemical shifts, which is typically observed in unfolded proteins (Supplementary Figure S1B).","type":"Results"},{"text":"Heteronuclear NOEs are sensitive to fast internal dynamics, and thus can discriminate flexible loop and tail regions from rigid secondary structures. Residues in the folded region of AcrIIA5 showed large 1H–15N heteronuclear NOE values (>0.8), whereas the N-terminal disordered region exhibited significantly reduced NOE values (<0.6), a signature of conformational flexibility (Figure 2B).","type":"Results"},{"text":"AcrIIA5 is unique among known Acr proteins in that it contains a long unstructured tail region at the N-terminus. The 22-residue tail also possesses an amino acid composition biased toward disorder, including three lysine, four arginine, and four serine residues","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"32544231","version":3,"reference_html":"Intrinsic disorder is essential for Cas9 inhibition of anti-CRISPR AcrIIA5. <i> An SY, Ka D, Kim I, Kim EH, Kim NK, Bae E, Suh JY. </i> Nucleic Acids Res, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","cross_refs":[{"db":"PDB","id":"6LKF"},{"db":"BMRB","id":"50185"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-06T14:07:17.632Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":22,"region_id":"DP02928r002","start":1,"term_id":"GO:0140678","statement":[{"text":"Remarkably, truncation of the N-terminal IDR abrogates the inhibitory activity against Cas9, revealing that the IDR is essential for Cas9 inhibition by AcrIIA5.","type":"Abstract"},{"text":"N-terminal disorder is essential for Cas9 inhibition by AcrIIA5","type":"Results"},{"text":"We employed the N-terminal truncated AcrIIA5Δ20 to examine whether the IDR was dispensable for Cas9 inhibition by AcrIIA5. Remarkably, AcrIIA5Δ20 completely lost its ability to inhibit Cas9, revealing that the N-terminal disordered region is essential for Acr activity (Figure 3C).","type":"Results"},{"text":"Truncation of the first 5 N-terminal residues (AcrIIA5Δ5) showed a ∼40% reduction of Cas9 inhibition, and further truncations abolished the Acr activity (Figure 3E). Thus, the length of the IDR was important for Cas9 inhibition of AcrIIA5, such that an IDR length of >20 residues was required to maintain the maximal inhibitory activity against Cas9.","type":"Results"},{"text":"The IDR peptide alone (residues 1–20) failed to show any inhibitory activity against Cas9, indicating that the IDR functions in Cas9 inhibition only in concert with the folded region of AcrIIA5 (Figure 3G).","type":"Results"},{"text":"Taken together, the Cas9 inhibition of AcrIIA5 requires an IDR sequence that is covalently linked to the structured region.","type":"Results"},{"text":"Specifically, the length of the IDR provides a scaffold for association between AcrIIA5 and Cas9–sgRNA, while the positive charges of the IDR serve as a regulatory switch that hinders Cas9 function upon binding.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"deletion mutation phenotypic evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"32544231","version":3,"reference_html":"Intrinsic disorder is essential for Cas9 inhibition of anti-CRISPR AcrIIA5. <i> An SY, Ka D, Kim I, Kim EH, Kim NK, Bae E, Suh JY. </i> Nucleic Acids Res, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001175","term_name":"molecular function inhibitor activity","curator_orcid":"0000-0002-0341-4888","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-05T07:40:00.467Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":22,"region_id":"DP02928r003","start":1,"term_id":"GO:0003723","statement":[{"text":"The IDR mediates direct interaction between AcrIIA5 and Cas9–sgRNA","type":"Results"},{"text":"Taken together, AcrIIA5 selectively binds to sgRNA-loaded Cas9 and inhibits the nuclease activity without competing with target DNA binding, which is unique among Cas9 inhibitors.","type":"Results"},{"text":"The size and sequence of the IDR modulate AcrIIA5 binding to Cas9 and inhibition of the nuclease activity.","type":"Discussion"}],"curator_id":"esalladini","released":"2022_03","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"32544231","version":4,"reference_html":"Intrinsic disorder is essential for Cas9 inhibition of anti-CRISPR AcrIIA5. <i> An SY, Ka D, Kim I, Kim EH, Kim NK, Bae E, Suh JY. </i> Nucleic Acids Res, 2020","date":"2022-03-08T14:10:30.723Z","reference_source":"pmid","ec_id":"ECO:0001807","term_name":"RNA binding","curator_orcid":"0000-0002-5152-5953","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"RNAcentral","id":"URS00021ED9AA_1314","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-12T13:41:19.019Z"}}],"released":"2021_06","ncbi_taxon_id":2006928,"disprot_id":"DP02928","date":"2020-09-23T14:42:09.976Z","organism":"Streptococcus phage D4276","regions_counter":3,"name":"AcrIIA5","dataset":["Viral proteins","RNA-binding proteins"],"UniParc":"UPI000B94BE49","uniref100":"UniRef100_A0A220GHA5","uniref90":"UniRef90_A0A220GHA5","uniref50":"UniRef50_A0A220GHA5","genes":[{"orfNames":[{"value":"D4276_028","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ASD50988.1","url":"https://www.ebi.ac.uk/ena/browser/view/ASD50988.1"}}]}]}],"disorder_content":0.15714285714285714,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"}],"Structural state":[{"start":1,"end":22,"type":"D"}],"Molecular function":[{"start":1,"end":22,"type":"F"}]}},{"acc":"P0A2N1","features":{"pfam":[{"id":"PF03536","name":"OspF/SpvC","start":2,"end":241}],"gene3D":[]},"creator":"fquaglia","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"],"sequence":"MPINRPNLNLNIPPLNIVAAYDGAEIPSTNKHLKNNFNSLHNQMRKMPVSHFKEALDVPDYSGMRQSGFFAMSQGFQLNNHGYDVFIHARRESPQSQGKFAGDKFHISVLRDMVPQAFQALSGLLFSEDSPVDKWKVTDMEKVVQQARVSLGAQFTLYIKPDQENSQYSASFLHKTRQFIECLESRLSENGVISGQCPESDVHPENWKYLSYRNELRSGRDGGEMQRQALREEPFYRLMTE","length":241,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":26,"region_id":"DP02929r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"The final model of the native structure contains residues 28–241 and misses residues 1–27, 66–67, 95, and 218–225 due to the lack of electron density. Two regions (residues 1–26 and 95–98) are disordered in the structure of the SpvC/phosphopeptide complex.","type":"Results"},{"text":"The N-terminal 26 residues are disordered in both the native SpvC structure and its complex with the peptide substrate (Figures 2A and 2B).","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18060821","version":2,"reference_html":"Structural insights into the enzymatic mechanism of the pathogenic MAPK phosphothreonine lyase. <i> Zhu Y, Li H, Long C, Hu L, Xu H, Liu L, Chen S, Wang DC, Shao F. </i> Mol Cell, 2007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2Q8Y"},{"db":"PDB","id":"2P1W"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-10T15:54:42.895Z"}}],"released":"2021_06","ncbi_taxon_id":149539,"disprot_id":"DP02929","date":"2020-09-23T15:15:13.692Z","organism":"Salmonella enteritidis","regions_counter":1,"name":"MAPK phosphothreonine lyase","dataset":["Bacterial virulence-related proteins"],"UniParc":"UPI0000138D6F","uniref100":"UniRef100_P0A2N0","uniref90":"UniRef90_P0A2N0","uniref50":"UniRef50_Q8VSP9","genes":[{"name":{"value":"spvC"},"synonyms":[{"value":"mkaD"},{"value":"vsdD"}]}],"alphafold_very_low_content":0.058091286307053944,"disorder_content":0.1078838174273859,"disprot_consensus":{"full":[{"start":1,"end":26,"type":"D"}],"Structural state":[{"start":1,"end":26,"type":"D"}]}},{"acc":"Q9Y6I3","features":{"pfam":[{"id":"PF01417","name":"ENTH domain","start":17,"end":140}],"gene3D":[]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MSTSSLRRQMKNIVHNYSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMIWKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKENMYAVQTLKDFQYVDRDGKDQGVNVREKAKQLVALLRDEDRLREERAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQSSGEEELQLQLALAMSKEEADQPPSCGPEDDAQLQLALSLSREEHDKEERIRRGDDLRLQMAIEESKRETGGKEESSLMDLADVFTAPAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPPVPPAADPWGGPAPTPASGDPWRPAAPAGPSVDPWGGTPAPAAGEGPTPDPWGSSDGGVPVSGPSASDPWTPAPAFSDPWGGSPAKPSTNGTTAAGGFDTEPDEFSDFDRLRTALPTSGSSAGELELLAGEVPARSPGAFDMSGVRGSLAEAVGSPPPAATPTPTPPTRKTPESFLGPNAALVDLDSLVSRPGPTPPGAKASNPFLPGGGPATGPSVTNPFQPAPPATLTLNQLRLSPVPPVPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL","length":576,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":18,"region_id":"DP02930r001","start":1,"term_id":"IDPO:0000002","statement":[{"text":"Mapping of the changes in the chemical shift onto the three-dimensional structure showed that the most perturbed residues are localized at three sites: the NH2-terminal unstructured region (site 1), the solvent-exposed surface of the first helix (site 2), and the region around loop 1 (loop connecting helices 1 and 2) and loop 3 (loop connecting helices 3 and 4) and helix 4 (site 3) (Fig. 2, A and B).","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11161217","version":2,"reference_html":"Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis. <i> Itoh T, Koshiba S, Kigawa T, Kikuchi A, Yokoyama S, Takenawa T. </i> Science, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","interaction_partner":[{"partner_start":null,"db":"ChEBI","id":"CHEBI:18348","partner_end":null}],"ec_ontology":"ECO","end":18,"region_id":"DP02930r002","start":1,"term_id":"GO:0036094","statement":[{"text":"Results suggest that site 1, the NH2-terminal unstructured region, was necessary for binding and adopted a specific conformation upon binding to PtdIns(4,5)P2.","type":"Article"},{"text":"Many residues in site 1 showed large chemical shift changes, suggesting a large structural change upon phosphoinositide binding (Fig. 2A). Deletion of the entire site 1 region (NH2-terminal, 18 residues) resulted in a complete loss of PtdIns(4,5)P2binding (Fig. 2F).","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"co-sedimentation assay evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11161217","version":3,"reference_html":"Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis. <i> Itoh T, Koshiba S, Kigawa T, Kikuchi A, Yokoyama S, Takenawa T. </i> Science, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001164","term_name":"small molecule binding","curator_orcid":"0000-0002-0341-4888","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":18,"region_id":"DP02930r003","start":1,"term_id":"IDPO:0000011","statement":[{"text":"Results suggest that site 1, the NH2-terminal unstructured region, was necessary for binding and adopted a specific conformation upon binding to PtdIns(4,5)P2.","type":"Article"},{"text":"Many residues in site 1 showed large chemical shift changes, suggesting a large structural change upon phosphoinositide binding (Fig. 2A). Deletion of the entire site 1 region (NH2-terminal, 18 residues) resulted in a complete loss of PtdIns(4,5)P2binding (Fig. 2F).","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"11161217","version":2,"reference_html":"Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis. <i> Itoh T, Koshiba S, Kigawa T, Kikuchi A, Yokoyama S, Takenawa T. </i> Science, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder to order","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":18,"region_id":"DP02930r004","start":1,"term_id":"GO:0140313","statement":[{"text":"Results suggest that site 1, the NH2-terminal unstructured region, was necessary for binding and adopted a specific conformation upon binding to PtdIns(4,5)P2.","type":"Article"},{"text":"Many residues in site 1 showed large chemical shift changes, suggesting a large structural change upon phosphoinositide binding (Fig. 2A). Deletion of the entire site 1 region (NH2-terminal, 18 residues) resulted in a complete loss of PtdIns(4,5)P2binding (Fig. 2F).","type":"Article"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"11161217","version":3,"reference_html":"Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis. <i> Itoh T, Koshiba S, Kigawa T, Kikuchi A, Yokoyama S, Takenawa T. </i> Science, 2001","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"molecular sequestering activity","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":18,"region_id":"DP02930r005","start":1,"term_id":"GO:0140313","statement":[{"text":"Results suggest that site 1, the NH2-terminal unstructured region, was necessary for binding and adopted a specific conformation upon binding to PtdIns(4,5)P2.","type":"Article"},{"text":"Many residues in site 1 showed large chemical shift changes, suggesting a large structural change upon phosphoinositide binding (Fig. 2A). Deletion of the entire site 1 region (NH2-terminal, 18 residues) resulted in a complete loss of PtdIns(4,5)P2binding (Fig. 2F).","type":"Article"}],"curator_id":"esalladini","released":"2022_03","ec_name":"co-sedimentation assay evidence used in manual assertion","term_ontology":"GO","curator_name":"Edoardo Salladini","reference_id":"11161217","version":4,"reference_html":"Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis. <i> Itoh T, Koshiba S, Kigawa T, Kikuchi A, Yokoyama S, Takenawa T. </i> Science, 2001","date":"2022-03-08T14:09:55.201Z","reference_source":"pmid","ec_id":"ECO:0001164","term_name":"molecular sequestering activity","curator_orcid":"0000-0002-5152-5953","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"ChEBI","id":"18348","operator":"and","partner_start":null,"partner_end":null}]}],"released":"2020_12","ncbi_taxon_id":9606,"disprot_id":"DP02930","date":"2020-09-24T15:02:59.634Z","organism":"Homo sapiens","regions_counter":5,"name":"Epsin-1","dataset":[],"UniParc":"UPI0000070B74","uniref100":"UniRef100_Q9Y6I3","uniref90":"UniRef90_Q9Y6I3","uniref50":"UniRef50_O88339","genes":[{"name":{"value":"EPN1"}}],"alphafold_very_low_content":0.4027777777777778,"disorder_content":0.03125,"disprot_consensus":{"full":[{"start":1,"end":18,"type":"T"}],"Structural state":[{"start":1,"end":18,"type":"D"}],"Molecular function":[{"start":1,"end":18,"type":"F"}],"Structural transition":[{"start":1,"end":18,"type":"T"}]}},{"acc":"Q9RQJ2","features":{"pfam":[{"id":"PF04371","name":"Porphyromonas-type peptidyl-arginine deiminase","start":77,"end":355}],"gene3D":[]},"creator":"fquaglia","taxonomy":["Bacteria","Bacteroidetes","Bacteroidia","Bacteroidales","Porphyromonadaceae","Porphyromonas"],"sequence":"MKKLLQAKALILALGLFQLPAIAQTQMQADRTNGQFATEEMQRAFQETNPPAGPVRAIAEYERSAAVLVRYPFGIPMELIKELAKNDKVITIVASESQKNTVITQYTQSGVNLSNCDFIIAKTDSYWTRDYTGWFAMYDTNKVGLVDFIYNRPRPNDDEFPKYEAQYLGIEMFGMKLKQTGGNYMTDGYGSAVQSHIAYTENSSLSQAQVNQKMKDYLGITHHDVVQDPNGEYINHVDCWGKYLAPNKILIRKVPDNHPQHQALEDMAAYFAAQTCAWGTKYEVYRALATNEQPYTNSLILNNRVFVPVNGPASVDNDALNVYKTAMPGYEIIGVKGASGTPWLGTDALHCRTHEVADKGYLYIKHYPILGEQAGPDYKIEADVVSCANATISPVQCYYRINGSGSFKAADMTMESTGHYTYSFTGLNKNDKVEYYISAADNSGRKETYPFIGEPDPFKFTCMNETNTCTVTGAAKALRAWFNAGRSELAVSVSLNIAGTYRIKLYNTAGEEVAAMTKELVAGTSVFSMDVYSQAPGTYVLVVEGNGIRETMKILK","length":556,"dataset":[],"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":484,"region_id":"DP02931r001","start":464,"term_id":"IDPO:0000002","statement":[{"text":"The crystallised tPPADWT and tPPADC351A constructs include residues aa464–484, with no visible electron density.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26209657","version":2,"reference_html":"Crystal structure of Porphyromonas gingivalis peptidylarginine deiminase: implications for autoimmunity in rheumatoid arthritis. <i> Montgomery AB, Kopec J, Shrestha L, Thezenas ML, Burgess-Brown NA, Fischer R, Yue WW, Venables PJ. </i> Ann Rheum Dis, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"5AK7"},{"db":"PDB","id":"5AK8"}],"term_name":"disorder","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:41:03.279Z"},"curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":484,"region_id":"DP02931r002","start":464,"term_id":"IDPO:0000033","statement":[{"text":"The crystallised tPPADWT and tPPADC351A constructs include residues aa464–484, with no visible electron density. This region represents a flexible linker connecting the IgLF and CTD in the full-length polypeptide, and its flexibility likely caused disorder in the crystal.","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"x-ray crystallography evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"26209657","version":3,"reference_html":"Crystal structure of Porphyromonas gingivalis peptidylarginine deiminase: implications for autoimmunity in rheumatoid arthritis. <i> Montgomery AB, Kopec J, Shrestha L, Thezenas ML, Burgess-Brown NA, Fischer R, Yue WW, Venables PJ. </i> Ann Rheum Dis, 2016","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:41:04.290Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_06","ncbi_taxon_id":242619,"disprot_id":"DP02931","date":"2020-09-24T17:05:44.950Z","organism":"Porphyromonas gingivalis (strain ATCC BAA-308 / W83)","regions_counter":2,"name":"Peptidylarginine deiminase","UniParc":"UPI00000B9D30","uniref100":"UniRef100_Q9RQJ2","uniref90":"UniRef90_Q9RQJ2","uniref50":"UniRef50_Q9RQJ2","genes":[{"olnNames":[{"value":"PG_1424"}]}],"alphafold_very_low_content":0.08992805755395683,"disorder_content":0.03776978417266187,"disprot_consensus":{"full":[{"start":464,"end":484,"type":"D"}],"Structural state":[{"start":464,"end":484,"type":"D"}],"Disorder function":[{"start":464,"end":484,"type":"F"}]}},{"acc":"Q9KRE7","features":{"pfam":[{"id":"PF01226","name":"Formate/nitrite transporter","start":13,"end":275}],"gene3D":[]},"creator":"fquaglia","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Vibrionales","Vibrionaceae","Vibrio"],"sequence":"MEHNQFDSLLPPQMAERAAITGEGKAKKAAYKSFLLAISAGIQIGIAFVFYTVVTTGAHDMPYGVTKLLGGLAFSLGLILVVITGGELFTSSVLILVAKASGKISWKELVRNWTVVYFGNLCGSIILVFIMLATRQFMEDGGQLGLNAMAISQHKLHHTFLQAFALGLMCNILVCLAVWMTFSARSLTDKVMVLILPVAMFVSSGFEHCIANMFQVPMAIGIKYFAPESFWAMTGANIAQYADLNFVNFIVNNLIPVTLGNIVGGGVFVGMWYWLIYLKD","length":280,"dataset":[],"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":21,"region_id":"DP02933r001","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Whereas the construct used for crystallization contained the entire 280 amino acid sequence, the first 22 amino acids at the N-terminus and the last three at the C-terminus are disordered in the crystal.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"20010838","version":2,"reference_html":"Structure and mechanism of a pentameric formate channel. <i> Waight AB, Love J, Wang DN. </i> Nat Struct Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3KLZ"},{"db":"PDB","id":"3KLY"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-27T14:20:15.273Z"}}],"released":"2021_12","ncbi_taxon_id":243277,"disprot_id":"DP02933","date":"2020-09-25T14:22:39.971Z","organism":"Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)","regions_counter":1,"name":"Formate transporter 1, putative","UniParc":"UPI00000C3097","uniref100":"UniRef100_A0A7U8WTD5","uniref90":"UniRef90_A0A271VRL5","uniref50":"UniRef50_A0A395TNN1","genes":[{"olnNames":[{"value":"VC_1695","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF94845.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF94845.1"}}]}]}],"alphafold_very_low_content":0.007142857142857143,"disorder_content":0.075,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"}],"Structural state":[{"start":1,"end":21,"type":"D"}]}},{"acc":"Q8I2X3","features":{"pfam":[{"id":"PF00149","name":"Calcineurin-like phosphoesterase","start":28,"end":257}],"gene3D":[]},"creator":"fquaglia","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"sequence":"MNYCKTTFHIFFFVLFFITIYEIKCQLRFASLGDWGKDTKGQILNAKYFKQFIKNERVTFIVSPGSNFIDGVKGLNDPAWKNLYEDVYSEEKGDMYMPFFTVLGTRDWTGNYNAQLLKGQGIYIEKNGETSIEKDADATNYPKWIMPNYWYHYFTHFTVSSGPSIVKTGHKDLAAAFIFIDTWVLSSNFPYKKIHEKAWNDLKSQLSVAKKIADFIIVVGDQPIYSSGYSRGSSYLAYYLLPLLKDAEVDLYISGHDNNMEVIEDNDMAHITCGSGSMSQGKSGMKNSKSLFFSSDIGFCVHELSNNGIVTKFVSSKKGEVIYTHKLNIKKKKTLDKVNALQHFAALPNVELTDVPSSGPMGNKDTFVRVVGTIGILIGSVIVFIGASSFLSKNMK","length":396,"dataset":[],"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":136,"region_id":"DP02934r001","start":122,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"Two loops comprising residues 122 to 136 and 161 to 169, were disordered and therefore not included in the structure.","type":"Methods"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"22387043","version":2,"reference_html":"Crystal structure of GAP50, the anchor of the invasion machinery in the inner membrane complex of Plasmodium falciparum. <i> Bosch J, Paige MH, Vaidya AB, Bergman LW, Hol WG. </i> J Struct Biol, 2012","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3TGH"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_12","ncbi_taxon_id":36329,"disprot_id":"DP02934","date":"2020-09-25T15:23:26.102Z","organism":"Plasmodium falciparum (isolate 3D7)","regions_counter":1,"name":"Acid phosphatase","UniParc":"UPI0000086295","uniref100":"UniRef100_W7JYT7","uniref90":"UniRef90_A0A060RXN4","uniref50":"UniRef50_A0A653HHM8","genes":[{"orfNames":[{"value":"PF3D7_0918000","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAD51862.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAD51862.1"}}]}]}],"alphafold_very_low_content":0.07323232323232323,"disorder_content":0.03787878787878788,"disprot_consensus":{"full":[{"start":122,"end":136,"type":"D"}],"Structural state":[{"start":122,"end":136,"type":"D"}]}},{"acc":"A0A0H3MCR9","features":{"pfam":[{"id":"PF17435","name":"CT_584-like","start":1,"end":183}],"gene3D":[]},"creator":"fquaglia","taxonomy":["Bacteria","Chlamydiae","Chlamydiales","Chlamydiaceae","Chlamydia/Chlamydophila group","Chlamydia"],"sequence":"MTTKPKTLEIDNNTFLLLEGNLKRIFATPIGYTTFREFQNVVFNCAQGQQELANFLFEMLINGKLLQELPAGQKQSAQSLIVQFMMPIRVAKDIHERGEFINFITSDMLAQQERCVFLNRLSRVDGQEFLLMTDVQNTCHLIRHLLSRLLEAQKNPIGEKNLQEIQEDLDSLRAHFEELTKSV","length":183,"dataset":["Neglected tropical diseases proteins"],"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":13,"region_id":"DP02937r001","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"In addition, potentially owing to the use of limited proteolysis in order to crystallize CT548, residues at both the amino-terminus (Met1–Asn13) and carboxy-terminus (Lys181–Val183) could not be modeled due to poor electron density.","type":"Methods"}],"curator_id":"fquaglia","released":"2023_06","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24192348","version":2,"reference_html":"Structure of CT584 from Chlamydia trachomatis refined to 3.05 Å resolution. <i> Barta ML, Hickey J, Kemege KE, Lovell S, Battaile KP, Hefty PS. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"4MLK"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-16T15:27:22.677Z"}}],"released":"2023_06","ncbi_taxon_id":471472,"disprot_id":"DP02937","date":"2020-09-29T10:27:53.436Z","organism":"Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B)","regions_counter":1,"name":"Uncharacterized protein","UniParc":"UPI0000139AE0","uniref100":"UniRef100_O84588","uniref90":"UniRef90_Q9PJF6","uniref50":"UniRef50_Q9Z7A3","genes":[{"olnNames":[{"value":"CTL0847","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAP04284.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAP04284.1"}}]}]}],"alphafold_very_low_content":0.0273224043715847,"disorder_content":0.07103825136612021,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"D"}],"Structural state":[{"start":1,"end":13,"type":"D"}]}},{"acc":"O61130","features":{"pfam":[{"id":"PF02430","name":"Apical membrane antigen 1","start":55,"end":520}],"gene3D":[]},"creator":"bmesza","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Plasmodium)"],"sequence":"MNKIYYIIFLSAQCLVHIGKCGRNQKPSRLTRSANNVLLEKGPTVERSTRMSNPWKAFMEKYDIERTHSSGVRVDLGEDAEVENAKYRIPAGRCPVFGKGIVIENSDVSFLRPVATGDQKLKDGGFAFPNANDHISPMTLANLKERYKDNVEMMKLNDIALCRTHAASFVMAGDQNSSYRHPAVYDEKEKTCHMLYLSAQENMGPRYCSPDAQNRDAVFCFKPDKNESFENLVYLSKNVRNDWDKKCPRKNLGNAKFGLWVDGNCEEIPYVKEVEAEDLRECNRIVFGASASDQPTQYEEEMTDYQKIQQGFRQNNREMIKSAFLPVGAFNSDNFKSKGRGFNWANFDSVKKKCYIFNTKPTCLINDKNFIATTALSHPQEVDLEFPCSIYKDEIEREIKKQSRNMNLYSVDGERIVLPRIFISNDKESIKCPCEPERISNSTCNFYVCNCVEKRAEIKENNQVVIKEEFRDYYENGEEKSNKQMLLIIIGITGGVCVVALASMAYFRKKANNDKYDKMDQAEGYGKPTTRKDEMLDPEASFWGEDKRASHTTPVLMEKPYY","length":562,"regions":[{"region_id":"DP02939r001","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:48:35.427Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":334,"term_id":"IDPO:0000002","start":297,"version":2,"statement":[{"text":"Several breaks occur in the main-chain tracing of all three domains as a result of absent or poorly defined electron density; these regions correspond to 15% of the polypeptide chain (fig. S2). Of particular note, no electron density was present for the 40-residue segment 295 to 334 in domain II, showing that this region is disordered or mobile. We refer to this region as the domain II loop.","type":"Results"},{"text":"The defined region relies on examining the missing coordinates in both reported X-ray structures attached to the publication (1w8k and 1w81), therefore the exact boundaries might be slightly different from the ones reported in the paper.","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"15731407","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1W8K"},{"db":"PDB","id":"1W81"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"bmesza","reference_html":"Crystal structure of the malaria vaccine candidate apical membrane antigen 1. <i> Pizarro JC, Vulliez-Le Normand B, Chesne-Seck ML, Collins CR, Withers-Martinez C, Hackett F, Blackman MJ, Faber BW, Remarque EJ, Kocken CH, Thomas AW, Bentley GA. </i> Science, 2005","curator_orcid":"0000-0003-0919-4449","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02939r002","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:48:36.103Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":215,"term_id":"IDPO:0000002","start":205,"version":2,"statement":[{"text":"Several breaks occur in the main-chain tracing of all three domains as a result of absent or poorly defined electron density; these regions correspond to 15% of the polypeptide chain (fig. S2). Of particular note, no electron density was present for the 40-residue segment 295 to 334 in domain II, showing that this region is disordered or mobile. We refer to this region as the domain II loop.","type":"Results"},{"text":"The region is defined based on missing coordinates in the two structures reported in the publication (1w8k and 1w81).","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"15731407","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1W8K"},{"db":"PDB","id":"1W81"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"bmesza","reference_html":"Crystal structure of the malaria vaccine candidate apical membrane antigen 1. <i> Pizarro JC, Vulliez-Le Normand B, Chesne-Seck ML, Collins CR, Withers-Martinez C, Hackett F, Blackman MJ, Faber BW, Remarque EJ, Kocken CH, Thomas AW, Bentley GA. </i> Science, 2005","curator_orcid":"0000-0003-0919-4449","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02939r003","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T14:48:39.104Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":412,"term_id":"IDPO:0000002","start":403,"version":2,"statement":[{"text":"Several breaks occur in the main-chain tracing of all three domains as a result of absent or poorly defined electron density; these regions correspond to 15% of the polypeptide chain (fig. S2). Of particular note, no electron density was present for the 40-residue segment 295 to 334 in domain II, showing that this region is disordered or mobile. We refer to this region as the domain II loop.","type":"Results"},{"text":"The region is defined based on missing coordinates in the two structures reported in the publication (1w8k and 1w81).","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"15731407","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1W8K"},{"db":"PDB","id":"1W81"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"bmesza","reference_html":"Crystal structure of the malaria vaccine candidate apical membrane antigen 1. <i> Pizarro JC, Vulliez-Le Normand B, Chesne-Seck ML, Collins CR, Withers-Martinez C, Hackett F, Blackman MJ, Faber BW, Remarque EJ, Kocken CH, Thomas AW, Bentley GA. </i> Science, 2005","curator_orcid":"0000-0003-0919-4449","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_12","ncbi_taxon_id":5855,"disprot_id":"DP02939","date":"2020-10-01T13:03:23.556Z","organism":"Plasmodium vivax","regions_counter":3,"name":"Apical merozoite antigen 1","dataset":[],"UniParc":"UPI00000777E0","uniref100":"UniRef100_A5K4Z2","uniref90":"UniRef90_C6L651","uniref50":"UniRef50_P22621","genes":[{"name":{"value":"AMA1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAC16731.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAC16731.1"}}]}}],"alphafold_very_low_content":0.20284697508896798,"disorder_content":0.10498220640569395,"disprot_consensus":{"full":[{"start":205,"end":215,"type":"D"},{"start":297,"end":334,"type":"D"},{"start":403,"end":412,"type":"D"}],"Structural state":[{"start":205,"end":215,"type":"D"},{"start":297,"end":334,"type":"D"},{"start":403,"end":412,"type":"D"}]}},{"acc":"P07749","features":{"pfam":[{"id":"PF13499","name":"EF-hand domain pair","start":131,"end":193},{"id":"PF22592","name":"FCaBP EF-hand domain","start":34,"end":126}],"gene3D":[]},"creator":"fquaglia","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Trypanosoma","Schizotrypanum"],"sequence":"MGACGSKGSTSDKGLASDKDGKKAKDRKEAWERIRQAIPREKTAEAKQRRIELFKKFDKNETGKLCYDEVHSGCLEVLKLDEFTPRVRDITKRAFDKARALGSKLENKGSEDFVEFLEFRLMLCYIYDFFELTVMFDEIDASGNMLVDEEELKRAVPKLEAWGAKVEDPAALFKELDKNGTGSVTFDEFAAWASAVKLDADGDPDNVPESA","length":211,"dataset":["Neglected tropical diseases proteins"],"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":17,"region_id":"DP02940r001","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"The first 17 residues from the N terminus appear unstructured and solvent-exposed.","type":"Abstract"},{"text":"The unstructured N-terminal region of FCaBP suggests that its covalently attached myristoyl group at the N terminus may be solvent-exposed, in contrast to the highly sequestered myristoyl group seen in recoverin and GCAP1. NMR analysis demonstrates that the myristoyl group attached to FCaBP is indeed solvent-exposed in both the Ca2+-free and Ca2+-bound states, and myristoylation has no effect on protein structure and folding stability.","type":"Abstract"},{"text":"In each crystal form, the first 17 residues from the N terminus appear disordered.","type":"Results"},{"text":"High temperature factors for the N-terminal residues suggest they may be dynamically disordered.","type":"Results"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18559337","version":2,"reference_html":"Structural insights into membrane targeting by the flagellar calcium-binding protein (FCaBP), a myristoylated and palmitoylated calcium sensor in Trypanosoma cruzi. <i> Wingard JN, Ladner J, Vanarotti M, Fisher AJ, Robinson H, Buchanan KT, Engman DM, Ames JB. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3CS1"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-16T15:25:29.991Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":17,"region_id":"DP02940r002","start":1,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"NMR relaxation studies and heteronuclear 15N nuclear Overhauser effect (NOE) analysis on FCaBP also confirms that the first 17 N-terminal residues are indeed unstructured (data not shown) and the N-terminal myristoyl group is solvent-exposed (see below). ","type":"Results"},{"text":"The absence of detectable electron density from the first 17 residues of FCaBP suggested that the N-terminal region and myristoyl group may be structurally disordered.","type":"Results"}],"curator_id":"fquaglia","released":"2022_12","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18559337","version":3,"reference_html":"Structural insights into membrane targeting by the flagellar calcium-binding protein (FCaBP), a myristoylated and palmitoylated calcium sensor in Trypanosoma cruzi. <i> Wingard JN, Ladner J, Vanarotti M, Fisher AJ, Robinson H, Buchanan KT, Engman DM, Ames JB. </i> J Biol Chem, 2008","date":"2022-09-16T15:01:42.484Z","reference_source":"pmid","ec_id":"ECO:0006165","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-16T15:08:23.474Z"}}],"released":"2021_12","ncbi_taxon_id":5693,"disprot_id":"DP02940","date":"2020-10-02T08:57:08.687Z","organism":"Trypanosoma cruzi","regions_counter":2,"name":"Flagellar calcium-binding protein","UniParc":"UPI000012A58E","uniref100":"UniRef100_P07749","uniref90":"UniRef90_P07749","uniref50":"UniRef50_P07749","genes":[{"name":{"value":"FCABP"}}],"alphafold_very_low_content":0.10426540284360189,"disorder_content":0.08056872037914692,"disprot_consensus":{"full":[{"start":1,"end":17,"type":"D"}],"Structural state":[{"start":1,"end":17,"type":"D"}]}},{"acc":"P50490","features":{"pfam":[{"id":"PF02430","name":"Apical membrane antigen 1","start":110,"end":580}],"gene3D":[]},"creator":"viglesias","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"sequence":"MRKLYCVLLLSAFEFTYMINFGRGQNYWEHPYQKSGVYHPINEHREHPKEYEYPLHQEHTYQQEDSGEDENTLQHAYPIDHEGAEPAPQEQNLFSSIEIVERSNYMGNPWTEYMAKYDIEEVHGSGIRVDLGEDAEVAGTQYRLPSGKCPVFGKGIIIENSNTTFLKPVATGNQDLKDGGFAFPPTNPLISPMTLNGMRDFYKNNEYVKNLDELTLCSRHAGNMNPDNDKNSNYKYPAVYDYNDKKCHILYIAAQENNGPRYCNKDQSKRNSMFCFRPAKDKLFENYTYLSKNVVDNWEEVCPRKNLENAKFGLWVDGNCEDIPHVNEFSANDLFECNKLVFELSASDQPKQYEQHLTDYEKIKEGFKNKNASMIKSAFLPTGAFKADRYKSHGKGYNWGNYNRETQKCEIFNVKPTCLINNSSYIATTALSHPIEVEHNFPCSLYKDEIKKEIERESKRIKLNDNDDEGNKKIIAPRIFISDDKDSLKCPCDPEMVSNSTCRFFVCKCVERRAEVTSNNEVVVKEEYKDEYADIPEHKPTYDNMKIIIASSAAVAVLATILMVYLYKRKGNAEKYDKMDQPQHYGKSTSRNDEMLDPEASFWGEEKRASHTTPVLMEKPYY","length":622,"dataset":[],"regions":[{"start":258,"end":273,"reference_id":"25360546","reference_source":"pmid","reference_html":"Structure and dynamics of apical membrane antigen 1 from Plasmodium falciparum FVO. <i> Lim SS, Yang W, Krishnarjuna B, Kannan Sivaraman K, Chandrashekaran IR, Kass I, MacRaild CA, Devine SM, Debono CO, Anders RF, Scanlon MJ, Scammells PJ, Norton RS, McGowan S. </i> Biochemistry, 2014","date":"2025-03-25T09:57:36.296Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"4R1A"}],"region_id":"DP02941r003","statement":[{"text":"The structure of FVO PfAMA1 showed numerous disordered loops in both domains. In DI, the disordered residues not observed in the density (160–163, 173–176, 226–232, and 258–273) correspond to loops Ib and If and part of the Ie loop (Figure 1A). There are 38 residues missing in DII [351–388 (Figure 1A)], which correspond to most of the loop DII structure found in the 3D7 PfAMA1 structure (Figure 1B).","type":"Results"},{"text":"This analysis showed that loops Ib and If (polymorphic cluster C3) are highly flexible regions in all three structures (Figure 2 and Table S2 of the Supporting Information). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-08T16:02:37.294Z"}},{"start":351,"end":388,"reference_id":"25360546","reference_source":"pmid","reference_html":"Structure and dynamics of apical membrane antigen 1 from Plasmodium falciparum FVO. <i> Lim SS, Yang W, Krishnarjuna B, Kannan Sivaraman K, Chandrashekaran IR, Kass I, MacRaild CA, Devine SM, Debono CO, Anders RF, Scanlon MJ, Scammells PJ, Norton RS, McGowan S. </i> Biochemistry, 2014","date":"2025-03-25T10:05:15.860Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"4R1A"}],"region_id":"DP02941r004","statement":[{"text":"The structure of FVO PfAMA1 showed numerous disordered loops in both domains. In DI, the disordered residues not observed in the density (160–163, 173–176, 226–232, and 258–273) correspond to loops Ib and If and part of the Ie loop (Figure 1A). There are 38 residues missing in DII [351–388 (Figure 1A)], which correspond to most of the loop DII structure found in the 3D7 PfAMA1 structure (Figure 1B).","type":"Results"},{"text":"The DII loop in both P. vivax AMA1 and our FVO PfAMA1 (Figure 1A) structure is disordered. ","type":"Results"},{"text":"The FVO PfAMA1 DII loop is disordered in the absence of crystal packing (PDB ID 4R1A); no residues were found within 4 Å of the DII loops. There appears to be sufficient space in the lattice for the DII loop to adopt a closed conformation as in 3D7 PfAMA1 (PDB ID: 1Z40) if this were its preferred conformation in FVO PfAMA1.","type":"Supplementary material"},{"text":"Unlike the published structures of 3D7 PfAMA1 and one 1F9–3D7 PfAMA1 complex (PDB entries 1Z40 and 2Q8A, respectively), in which the conserved DII loop is partially ordered, the DII loop of FVO PfAMA1 is completely disordered. ","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-08T16:02:32.527Z"}}],"released":"2021_12","ncbi_taxon_id":5838,"disprot_id":"DP02941","date":"2020-10-02T13:10:27.579Z","organism":"Plasmodium falciparum (isolate FCR-3 / Gambia)","regions_counter":4,"name":"Apical membrane antigen 1","UniParc":"UPI000012593A","uniref100":"UniRef100_P50490","uniref90":"UniRef90_P22621","uniref50":"UniRef50_P22621","genes":[{"name":{"value":"AMA-1"},"synonyms":[{"value":"PF83"}]}],"alphafold_very_low_content":0.25884244372990356,"disorder_content":0.08681672025723473,"disprot_consensus":{"full":[{"start":258,"end":273,"type":"D"},{"start":351,"end":388,"type":"D"}],"Structural state":[{"start":258,"end":273,"type":"D"},{"start":351,"end":388,"type":"D"}]}},{"acc":"P63101","features":{"pfam":[{"id":"PF00244","name":"14-3-3 protein","start":9,"end":229}],"gene3D":[]},"creator":"msalas","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQPESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAGEGGEN","length":245,"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":245,"region_id":"DP02943r001","start":234,"term_id":"IDPO:0000002","statement":[{"text":"1H-NMR spectroscopy revealed the presence of a flexible and unstructured C-terminal extension, 12 amino acids in length, which protrudes from the domain core of 14-3-3ζ and is similar in structure and length to the C-terminal extension of mammalian sHsps. The extension stabilizes 14-3-3ζ","type":"Abstract"},{"text":"It has been proposed that the C-terminus of 14-3-3ζ (Asp231–Asn245) adopts a poorly ordered conformation","type":"Introduction"},{"text":"Taken together these results indicated that the strongest cross-peaks in the two-dimensional NMR spectra of full-length 14-3-3ζ were attributable to the 12 amino acid residues at the extreme C-terminus of the 14-3-3ζ dimer (i.e. from Gly234 to Asn245), with no cross-peaks being observed for residues preceding Gly234","type":"Results"},{"text":"thus 14-3-3ζ has a flexible C-terminal extension encompassing its last 12 amino acids that is directly comparable with the C-terminal extension of mammalian sHsps in terms of its polar nature and conformational flexibility","type":"Results"},{"text":"Consistent with folding prediction algorithms, the NMR data indicate that the last 12 C-terminal amino acids of 14-3-3ζ (Gly234–Asp245) are solvent-exposed and exhibit flexibility that is independent of the domain core of the protein, while adopting no preferred secondary structure","type":"Discussion"},{"text":"Therefore it is concluded that 14-3-3ζ, and by analogy all other 14-3-3 proteins, have a flexible C-terminal extension.","type":"Discussion"}],"curator_id":"msalas","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Martin Salas","reference_id":"21554249","version":2,"reference_html":"NMR spectroscopy of 14-3-3ζ reveals a flexible C-terminal extension: differentiation of the chaperone and phosphoserine-binding activities of 14-3-3ζ. <i> Williams DM, Ecroyd H, Goodwin KL, Dai H, Fu H, Woodcock JM, Zhang L, Carver JA. </i> Biochem J, 2011","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","validated":{"curator_id":"fquaglia","timestamp":"2020-11-25T16:18:52.006Z","curator_name":"Federica Quaglia"},"term_name":"disorder","curator_orcid":"0000-0001-6352-1282","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","ncbi_taxon_id":10090,"disprot_id":"DP02943","date":"2020-10-09T17:47:54.819Z","organism":"Mus musculus","regions_counter":1,"name":"14-3-3 protein zeta/delta","dataset":[],"UniParc":"UPI0000004169","uniref100":"UniRef100_P63101","uniref90":"UniRef90_P63101","uniref50":"UniRef50_P63101","genes":[{"name":{"value":"Ywhaz"}}],"alphafold_very_low_content":0.04081632653061224,"disorder_content":0.04897959183673469,"disprot_consensus":{"full":[{"start":234,"end":245,"type":"D"}],"Structural state":[{"start":234,"end":245,"type":"D"}]}},{"acc":"Q96RD7","features":{"pfam":[{"id":"PF00876","name":"Innexin","start":47,"end":236}],"gene3D":[]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MAIAQLATEYVFSDFLLKEPTEPKFKGLRLELAVDKMVTCIAVGLPLLLISLAFAQEISIGTQISCFSPSSFSWRQAAFVDSYCWAAVQQKNSLQSESGNLPLWLHKFFPYILLLFAILLYLPPLFWRFAAAPHICSDLKFIMEELDKVYNRAIKAAKSARDLDMRDGACSVPGVTENLGQSLWEVSESHFKYPIVEQYLKTKKNSNNLIIKYISCRLLTLIIILLACIYLGYYFSLSSLSDEFVCSIKSGILRNDSTVPDQFQCKLIAVGIFQLLSVINLVVYVLLAPVVVYTLFVPFRQKTDVLKVYEILPTFDVLHFKSEGYNDLSLYNLFLEENISEVKSYKCLKVLENIKSSGQGIDPMLLLTNLGMIKMDVVDGKTPMSAEMREEQGNQTAELQGMNIDSETKANNGEKNARQRLLDSSC","length":426,"dataset":[],"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":190,"region_id":"DP02945r001","start":163,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"We were able to model most of PANX1 except for the linker connecting the intracellular helices IH1 and IH2 (residues 163–190), and the CTT (residues 374–426).","type":"Methods"},{"text":"The disordered IH1–IH2 linker (residues 163–190) and the CTT (residues after 373) are indicated by dashed lines","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"32494015","version":2,"reference_html":"Structures of human pannexin 1 reveal ion pathways and mechanism of gating. <i> Ruan Z, Orozco IJ, Du J, Lü W. </i> Nature, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","cross_refs":[{"db":"PDB","id":"6WBF"}],"term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-27T15:38:04.321Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":190,"region_id":"DP02945r002","start":163,"term_id":"IDPO:0000033","unpublished":true,"statement":[{"text":"We were able to model most of PANX1 except for the linker connecting the intracellular helices IH1 and IH2 (residues 163–190), and the CTT (residues 374–426).","type":"Methods"},{"text":"The disordered IH1–IH2 linker (residues 163–190) and the CTT (residues after 373) are indicated by dashed lines","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"32494015","version":3,"reference_html":"Structures of human pannexin 1 reveal ion pathways and mechanism of gating. <i> Ruan Z, Orozco IJ, Du J, Lü W. </i> Nature, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","cross_refs":[{"db":"PDB","id":"6WBF"}],"term_name":"flexible linker","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-27T15:38:03.793Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":426,"region_id":"DP02945r003","start":374,"term_id":"IDPO:0000002","unpublished":true,"statement":[{"text":"We were able to model most of PANX1 except for the linker connecting the intracellular helices IH1 and IH2 (residues 163–190), and the CTT (residues 374–426).","type":"Methods"},{"text":"The disordered IH1–IH2 linker (residues 163–190) and the CTT (residues after 373) are indicated by dashed lines","type":"Figure"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"32494015","version":2,"reference_html":"Structures of human pannexin 1 reveal ion pathways and mechanism of gating. <i> Ruan Z, Orozco IJ, Du J, Lü W. </i> Nature, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006224","term_name":"disorder","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-27T14:56:21.303Z"}},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":426,"region_id":"DP02945r004","start":374,"term_id":"IDPO:0000031","unpublished":true,"statement":[{"text":"The PANX1 channel forms a heptamer that contains (from top to bottom) an extracellular domain (ECD), a transmembrane domain (TMD) and an intracellular domain (ICD), with the unstructured CTT blocking the ICD entrance to the ion pathway along the symmetry axis (referred to as the main pore) (Fig. 1a, b).","type":"Article"},{"text":"Although we were unable to model the CTT owing to its intrinsically disordered nature, we have defined its key role in caspase-dependent channel gating (see ‘Ion pathways and channel gating’).","type":"Article"},{"text":"Instead, we observed that the intracellular entry was blocked by the unstructured CTT, and this blockage was released upon removal of the CTT by caspase 7, opening the main pore (Fig. 1c).","type":"Article"},{"text":"Under normal physiological conditions, the intracellular entrance of the main pore is blocked by the unstructured CTT, so anions—but not ATP—can move through the side tunnels, which explains why PANX1 currents can be evoked with a voltage clamp, during which there is no ATP release","type":"Discussion"}],"curator_id":"fquaglia","released":"2022_03","ec_name":"cryogenic electron microscopy evidence used in manual assertion","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"32494015","version":3,"reference_html":"Structures of human pannexin 1 reveal ion pathways and mechanism of gating. <i> Ruan Z, Orozco IJ, Du J, Lü W. </i> Nature, 2020","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006208","term_name":"flexible C-terminal tail","curator_orcid":"0000-0002-0341-4888","ec_go":"IDA","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-27T14:56:30.920Z"}}],"released":"2021_12","ncbi_taxon_id":9606,"disprot_id":"DP02945","date":"2020-10-14T15:39:57.663Z","organism":"Homo sapiens","regions_counter":4,"name":"Pannexin-1","UniParc":"UPI0000169BEA","uniref100":"UniRef100_Q96RD7","uniref90":"UniRef90_Q96RD7","uniref50":"UniRef50_Q96RD7","genes":[{"name":{"value":"PANX1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:8599","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8599"}}]},"synonyms":[{"value":"MRS1"}],"orfNames":[{"value":"UNQ2529/PRO6028"}]}],"alphafold_very_low_content":0.176056338028169,"disorder_content":0.19014084507042253,"disprot_consensus":{"full":[{"start":163,"end":190,"type":"D"},{"start":374,"end":426,"type":"D"}],"Structural state":[{"start":163,"end":190,"type":"D"},{"start":374,"end":426,"type":"D"}],"Disorder function":[{"start":163,"end":190,"type":"F"},{"start":374,"end":426,"type":"F"}]}},{"acc":"Q2VL32","features":{"pfam":[{"id":"PF13678","name":"NFkB-p65-degrading zinc protease","start":22,"end":270}],"gene3D":[]},"creator":"fquaglia","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Vibrionales","Vibrionaceae","Photobacterium"],"sequence":"MTAIFSLAINSNFVLANNDKPDASDDKYADYVVRLGSEHPLNHTQIIELSSAVSRAVLLSYPNIIDRYTAAATEYTVIDALFHSPTFRHIVSFGLHNQQENLGHIRYTNEYEINNNREDEFSLVSEVSYDDIKSSNAQQVPLVAFYEAREDRATGTPIVNMGVAPSLFSGRYSWWQEALIHEIVHHVTGSSDTHEENKQGPTEILAQMVAAELHWAIPTFKGYSDPARVEAIQERDFHSLLNMFQRHGSELGFLFTRLATIAKGKKASPDFGTLTSFCSEGISSFPKYPDHDDDFNGGGAFFLPSASADSSVECTFDVLNRIEPVDDSIKFEGGNLLIKNDFKNLNLRVAQLSFLNAKKGSGFYRKNWDSWKSWYQASSWKNGLNSGLYGYGHDESEGNLIYSPYGITFNDGSFSIGFSSRKHINDNTKDDNFVKLNNANWSSFYYAGQMFFDKNKRPVALVITEPLNAAFGAGWSYIYKDGKWHYEAQDDWDQRLFKDSTLSLDPHAPQFIN","length":513,"dataset":["Unicellular toxins and antitoxins"],"regions":[{"region_id":"DP02946r001","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T17:44:12.925Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":314,"term_id":"IDPO:0000002","start":278,"version":2,"statement":[{"text":"The primary structure of AIP56 suggests that this toxin comprises two functional domains and could be an A-B toxin with its two moieties linked by a single disulphide bond (Figure S1) [23]. Therefore, in order to define domain boundaries within the toxin, limited proteolysis experiments were performed. SDS-PAGE analysis of AIP56 digested with chymotrypsin, trypsin or proteinase K revealed that the toxin is highly resistant to trypsin digestion, whereas chymotrypsin and proteinase K cleaved AIP56 into two major fragments with approximately 32 and 24 kDa (Figure 2A). These two fragments were only detected upon treatment with the reducing agent DTT, suggesting that they are linked by a disulphide bridge (Figure 2B). N-terminal Edman sequencing revealed that chymotrypsin cleavage occurred between Phe285 and Phe286, in the amino-acid stretch flanked by the two unique cysteine residues (Cys262 and Cys298) of AIP56 (Figure 2C). Altogether, these results indicate that AIP56 is composed of two domains linked by a disulphide bridge.","type":"Results"},{"text":"The region described in the publication, spanning residues Cys262 to Cys298, corresponds to region Cys278-Cys314 of the associated UniProt sequence as AIP56 was synthesized as a precursor protein with a cleavable N-terminal signal peptide that was removed during secretion, originating a 497-amino acid mature toxin.","type":"Curator statement"}],"term_name":"disorder","ec_name":"cleavage assay evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23468618","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0007691","curator_id":"fquaglia","reference_html":"The apoptogenic toxin AIP56 is a metalloprotease A-B toxin that cleaves NF-κb P65. <i> Silva DS, Silva DS, Pereira LM, Moreira AR, Ferreira-da-Silva F, Brito RM, Faria TQ, Zornetta I, Montecucco C, Oliveira P, Azevedo JE, Pereira PJ, Macedo-Ribeiro S, do Vale A, dos Santos NM. </i> PLoS Pathog, 2013","ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP02946r002","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T17:44:13.644Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":314,"term_id":"IDPO:0000033","start":278,"version":3,"statement":[{"text":"The primary structure of AIP56 suggests that this toxin comprises two functional domains and could be an A-B toxin with its two moieties linked by a single disulphide bond (Figure S1) [23]. Therefore, in order to define domain boundaries within the toxin, limited proteolysis experiments were performed. SDS-PAGE analysis of AIP56 digested with chymotrypsin, trypsin or proteinase K revealed that the toxin is highly resistant to trypsin digestion, whereas chymotrypsin and proteinase K cleaved AIP56 into two major fragments with approximately 32 and 24 kDa (Figure 2A). These two fragments were only detected upon treatment with the reducing agent DTT, suggesting that they are linked by a disulphide bridge (Figure 2B). N-terminal Edman sequencing revealed that chymotrypsin cleavage occurred between Phe285 and Phe286, in the amino-acid stretch flanked by the two unique cysteine residues (Cys262 and Cys298) of AIP56 (Figure 2C). Altogether, these results indicate that AIP56 is composed of two domains linked by a disulphide bridge.","type":"Results"},{"text":"AIP56 toxicity requires integrity of the linker but the disulfide bridge is dispensable for intoxication.","type":"Figure"},{"text":"The region described in the publication, spanning residues Cys262 to Cys298, corresponds to region Cys278-Cys314 of the associated UniProt sequence as AIP56 was synthesized as a precursor protein with a cleavable N-terminal signal peptide that was removed during secretion, originating a 497-amino acid mature toxin.","type":"Curator statement"}],"term_name":"flexible linker","ec_name":"cleavage assay evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"23468618","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Disorder function","ec_id":"ECO:0007691","curator_id":"fquaglia","reference_html":"The apoptogenic toxin AIP56 is a metalloprotease A-B toxin that cleaves NF-κb P65. <i> Silva DS, Silva DS, Pereira LM, Moreira AR, Ferreira-da-Silva F, Brito RM, Faria TQ, Zornetta I, Montecucco C, Oliveira P, Azevedo JE, Pereira PJ, Macedo-Ribeiro S, do Vale A, dos Santos NM. </i> PLoS Pathog, 2013","ec_go":"IDA","disprot_namespace":"Disorder function"},{"region_id":"DP02946r003","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T17:44:15.198Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":314,"term_id":"GO:0051179","start":278,"version":3,"statement":[{"text":"Translocation of AIP56 requires integrity of the Cys262-Cys298 linker but the disulphide bridge is not an absolute requirement for toxicity","type":"Results"},{"text":"These results suggest that the integrity of the linker region between the two cysteine residues is needed for toxin internalization, in contrast to what is known for the diphtheria, tetanus and botulinum toxins, where nicking of the inter-cysteine loop is required for toxicity","type":"Results"},{"text":"In contrast, we have found that the AIP56 N-terminal metalloprotease can only act when linked to a C-terminal binding domain that, by analogy with other A-B toxins, may assist the protease domain in its membrane translocation into the cytosol","type":"Discussion"},{"text":"The region described in the publication, spanning residues Cys262 to Cys298, corresponds to region Cys278-Cys314 of the associated UniProt sequence as AIP56 was synthesized as a precursor protein with a cleavable N-terminal signal peptide that was removed during secretion, originating a 497-amino acid mature toxin.","type":"Curator statement"}],"term_name":"localization","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"23468618","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Biological process","ec_id":"ECO:0007689","curator_id":"fquaglia","reference_html":"The apoptogenic toxin AIP56 is a metalloprotease A-B toxin that cleaves NF-κb P65. <i> Silva DS, Silva DS, Pereira LM, Moreira AR, Ferreira-da-Silva F, Brito RM, Faria TQ, Zornetta I, Montecucco C, Oliveira P, Azevedo JE, Pereira PJ, Macedo-Ribeiro S, do Vale A, dos Santos NM. </i> PLoS Pathog, 2013","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2020_12","ncbi_taxon_id":38294,"disprot_id":"DP02946","date":"2020-10-19T10:33:04.883Z","organism":"Photobacterium damsela subsp. piscicida","regions_counter":3,"name":"Aip56","UniParc":"UPI000059665F","uniref100":"UniRef100_Q2VL32","uniref90":"UniRef90_Q2VL32","uniref50":"UniRef50_A0A1S6HW48","genes":[{"name":{"value":"aip56","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ABA00995.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABA00995.1"}}]},"orfNames":[{"value":"E4T25_16935","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TFZ50892.1","url":"https://www.ebi.ac.uk/ena/browser/view/TFZ50892.1"}}]}]}],"alphafold_very_low_content":0.08187134502923976,"disorder_content":0.07212475633528265,"disprot_consensus":{"full":[{"start":278,"end":314,"type":"D"}],"Structural state":[{"start":278,"end":314,"type":"D"}],"Disorder function":[{"start":278,"end":314,"type":"F"}],"Biological process":[{"start":278,"end":314,"type":"F"}]}},{"acc":"A7L035","features":{"pfam":[{"id":"PF28873","name":"CaTX-A toxin domain","start":28,"end":248}],"gene3D":[]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Cnidaria","Cubozoa","Chirodropida","Chirodropidae","Chironex"],"sequence":"MVKMLFFAFLPLLFMTGIAAESTISSGLNSLKTKIDAKMPSGKQLFDKVVEMQKQIDAKFSNDDERAKVMGAIGSLSTAVGKFQSGDPAKIASGCLDILVGISSVLKDFAKFSPIFSILSLVVGLFSGTKAEESVGSVVKKAVQEQSDQELQEALYGVKREYAVSKAFLDGVRNETSDLSPTEVSALAANVPIYQGVRFIAMVVQRIKYIKPKTESEIKRMLTMLELFTDLCSLRDLILLDLYQLVATPGHSPNIASGIKEVSNLGREEYKKVFEDLLKNDDKETYLFLSYLYPREKNEQSRKIFNFFDLMKVKYDDRLKQDLTGVKIFSNVHWPNYFMCSSNDYLALICTKPYGSLKLDKLNDGYYSIKTTQHDPKICHRYGNYILFTHKRNDDLEKFNFVPVKLEKREIYLLSSKESPNKFAYVPQNADGALFFVDGIPSKVGYGNQGYFTLVE","length":456,"dataset":[],"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":47,"term_name":"disorder","reference_id":"29880743","released":"2023_12","term_id":"IDPO:0000002","unpublished":true,"curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","start":22,"term_ontology":"IDPO","version":2,"curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Here we have synthesized peptides corresponding to these regions and analyzed their structures using NMR spectroscopy. The peptide corresponding to the predicted N-terminal amphiphilic helix appears unstructured in aqueous solution.","type":"Abstract"},{"text":"The locations of Asn21 and Pro22 (corresponding to Asn42 and Pro94 in the full-length protein) are labeled in CfTX-122–47 and CfTX-173–100, respectively, and correspond to the start of the C-terminal tails that are more disordered than the helical regions.","type":"Figure"},{"text":"The NMR data for CfTX-122–47 solubilized in water is consistent with the PrDOS results, which indicated that the respective sequence is unstructured.","type":"Results"},{"text":"Secondary α-proton shifts for CfTX-122–47 in H2O (black bars) and in 100 mM SDS (grey bars with black border). Secondary shift values of CfTX-122–47 in an aqueous environment are generally within ±0.1, indicating lack of structure; whereas the values of CfTX-122–47 in SDS are lower than −0.1 ppm between residues 4 and 19 (corresponding to residues 25 and 40 in the full-length protein), indicating an α-helical structure in this environment.","type":"Figure"},{"text":"The region predicted to form an amphiphilic α-helix in CfTX-1 (residues 25–32) appears to be disordered in aqueous solution based on the chemical shift analysis of CfTX-122–47.","type":"Discussion"}],"reference_html":"Structural Characterisation of Predicted Helical Regions in the <i>Chironex fleckeri</i> CfTX-1 Toxin. <i> Andreosso A, Bansal PS, Smout MJ, Wilson D, Seymour JE, Daly NL. </i> Mar Drugs, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP02947r001","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":47,"term_name":"disorder to order","reference_id":"29880743","released":"2023_12","term_id":"IDPO:0000011","unpublished":true,"curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","start":22,"term_ontology":"IDPO","version":2,"curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Secondary α-proton shifts for CfTX-122–47 in H2O (black bars) and in 100 mM SDS (grey bars with black border). Secondary shift values of CfTX-122–47 in an aqueous environment are generally within ±0.1, indicating lack of structure; whereas the values of CfTX-122–47 in SDS are lower than −0.1 ppm between residues 4 and 19 (corresponding to residues 25 and 40 in the full-length protein), indicating an α-helical structure in this environment.","type":"Figure"},{"text":"By contrast, the chemical shift analysis in the presence of 100 mM SDS has several consecutive negative shifts, consistent with helical structure. This helical structure was confirmed by determination of the three-dimensional structure (Figure 2).","type":"Discussion"},{"text":"The transition of unstructured to helical structure in the presence of membranes or membrane-mimicking environments has previously been shown for other peptides, such as the antimicrobial peptides MSI-78 and magainin-2","type":"Discussion"}],"reference_html":"Structural Characterisation of Predicted Helical Regions in the <i>Chironex fleckeri</i> CfTX-1 Toxin. <i> Andreosso A, Bansal PS, Smout MJ, Wilson D, Seymour JE, Daly NL. </i> Mar Drugs, 2018","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP02947r002","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2023_12","ncbi_taxon_id":45396,"disprot_id":"DP02947","date":"2020-10-19T10:52:42.349Z","organism":"Chironex fleckeri","regions_counter":2,"name":"Toxin CfTX-1","UniParc":"UPI000159392A","uniref100":"UniRef100_A7L035","uniref90":"UniRef90_A7L035","uniref50":"UniRef50_P58762","genes":[],"alphafold_very_low_content":0.05701754385964912,"disorder_content":0.05701754385964912,"disprot_consensus":{"full":[{"start":22,"end":47,"type":"T"}],"Structural state":[{"start":22,"end":47,"type":"D"}],"Structural transition":[{"start":22,"end":47,"type":"T"}]}},{"acc":"J7JU64","features":{"pfam":[],"gene3D":[]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Spiralia","Lophotrochozoa","Mollusca","Gastropoda","Caenogastropoda","Neogastropoda","Conoidea","Conidae","Conus","Rhizoconus"],"sequence":"METLTLLWRASSSCLLVVLSHSLLRLLGVRCLEKSGAQPNKLFRPPCCQKGPSFARHSRCVYYTQSRE","length":68,"dataset":[],"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":68,"term_name":"disorder","reference_id":"23382933","released":"2023_12","term_id":"IDPO:0000002","unpublished":true,"curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","start":29,"term_ontology":"IDPO","version":2,"curator_name":"Federica Quaglia","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"The 1D 1H NMR spectra of αB-VxXXIVA isomers in phosphate buffer at pH 5.8 show that the majority of the amide protons fall within the 8.0–9.0 ppm range (Fig. 6); the lack of chemical shift dispersion here and elsewhere in the spectrum indicates that these isomers lack any significant tertiary structure. The same was true at pH 7.0 (Fig. S1, S2, S3). NMR spectra were also acquired in the presence of 3–10 mM CaCl2 to ascertain whether calcium had any effect on their conformation, but no change in chemical shift dispersion was observed","type":"Results"}],"reference_html":"A novel inhibitor of α9α10 nicotinic acetylcholine receptors from Conus vexillum delineates a new conotoxin superfamily. <i> Luo S, Christensen S, Zhangsun D, Wu Y, Hu Y, Zhu X, Chhabra S, Norton RS, McIntosh JM. </i> PLoS One, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP02948r001","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-27T19:53:50.971Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":68,"term_name":"disorder","reference_id":"23382933","released":"2023_12","term_id":"IDPO:0000002","unpublished":true,"curator_orcid":"0000-0002-0341-4888","curator_id":"fquaglia","start":29,"term_ontology":"IDPO","version":2,"curator_name":"Federica Quaglia","ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"CD spectra were acquired on all threeαB-VxXXIVA isomers in phosphate buffer. All peptide isomers exhibited minima at around 200 nm (Fig. 7A), indicative of a random coil conformation with no α-helical and β-sheet content, and consistent with our NMR results.","type":"Results"}],"reference_html":"A novel inhibitor of α9α10 nicotinic acetylcholine receptors from Conus vexillum delineates a new conotoxin superfamily. <i> Luo S, Christensen S, Zhangsun D, Wu Y, Hu Y, Zhu X, Chhabra S, Norton RS, McIntosh JM. </i> PLoS One, 2013","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","region_id":"DP02948r002","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-27T19:53:42.071Z"}}],"released":"2023_12","ncbi_taxon_id":89431,"disprot_id":"DP02948","date":"2020-10-19T11:05:20.530Z","organism":"Conus vexillum","regions_counter":2,"name":"Alpha-conotoxin VxXXIVA","UniParc":"UPI00027EF45C","uniref100":"UniRef100_J7JU64","uniref90":"UniRef90_J7JU64","uniref50":"UniRef50_J7JU64","genes":[],"alphafold_very_low_content":0.5735294117647058,"disorder_content":0.5882352941176471,"disprot_consensus":{"full":[{"start":29,"end":68,"type":"D"}],"Structural state":[{"start":29,"end":68,"type":"D"}]}},{"acc":"O25555","features":{"pfam":[],"gene3D":[]},"creator":"fquaglia","taxonomy":["Bacteria","Proteobacteria","Epsilonproteobacteria","Campylobacterales","Helicobacteraceae","Helicobacter"],"sequence":"MPNTTAKKDYTKYSKKQLFNLIHQLERKIKKMQNDRISFKEKMAKELEKRDQNFKDKIDALNELLQKISQAFDDKRDCCLGHEIPNIETQQAMRDVGNKETDLIVEDFSSYSNERKRALGVEAQS","length":125,"dataset":["Unicellular toxins and antitoxins"],"regions":[{"region_id":"DP02949r001","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T17:27:54.168Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":125,"term_id":"IDPO:0000002","start":96,"version":2,"statement":[{"text":"However, another CD analysis (supplemental Fig. S6C) indicated that the 30-residue HP0895Ctp is unstructured.","type":"Results"}],"term_name":"disorder","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21123184","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006204","curator_id":"fquaglia","reference_html":"Functional identification of toxin-antitoxin molecules from Helicobacter pylori 26695 and structural elucidation of the molecular interactions. <i> Han KD, Matsuura A, Ahn HC, Kwon AR, Min YH, Park HJ, Won HS, Park SJ, Kim DY, Lee BJ. </i> J Biol Chem, 2011","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02949r002","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T17:28:51.574Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":125,"term_id":"GO:0005515","start":96,"version":3,"statement":[{"text":"In contrast, the unstructured C-terminal region of HP0895 was responsible for binding to HP0894 and underwent a conformational change in the process.","type":"Abstract"},{"text":"Based on these results, and to confirm the binding of this C-terminal region of HP0895 with HP0894, we synthesized a 30-residue peptide, HP0895Ctp (Val96–Ser125), corresponding to the C-terminal region of HP0895 and investigated the interaction between this peptide and HP0894. A series of two-dimensional [1H-15N] TROSY spectra of 15N-labeled HP0894 was recorded with successive additions of unlabeled HP0895Ctp (0, 0.5, 1, and 2 molar equivalents). As shown in Fig. 2C, obvious chemical shift changes in the slow exchange mode on the NMR time scale were observed for a lot of the residues of HP0894, and some other residues showed chemical shift changes in fast exchange mode. Chemical shift changes from the residues in the slow exchange mode were completed with equimolar HP0895Ctp, whereas fast exchange mode chemical shift changes continued above 1:1 molar ratio in an HP0895Ctp concentration-dependent manner. These results indicate that the dissociation constants (Kd) of HP0895Ctp (and consequently HP0895) with HP0894 are relatively small (∼10−8 m or smaller) (27). Thus, HP0894-HP0895 binding is strong. In addition, these results confirmed that HP0895 binds to HP0894 via its C-terminal region with a binding stoichiometry of 1:1.","type":"Results"},{"text":"Our results show that the cellular level functioning of HP0894 is inactivated by binding with HP0895. The direct interaction of these two proteins occurs mainly between the 30-residue C-terminal tail of HP0895 and the N-terminal secondary structure elements and an adjacent C-terminal β-strand of HP0894. Upon binding to HP0894, that unstructured C terminus tail of HP0895 seems to be transformed into structured form.","type":"Discussion"},{"text":"Taken together, it is concluded that the HP0894-HP0895 protein couple is a TA system in H. pylori, where HP0894 is a toxin with an RNase function, whereas HP0895 is an antitoxin functioning by binding to both the toxin and DNA.","type":"Abstract"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"O25554","partner_end":null}],"term_name":"protein binding","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Functional identification of toxin-antitoxin molecules from Helicobacter pylori 26695 and structural elucidation of the molecular interactions. <i> Han KD, Matsuura A, Ahn HC, Kwon AR, Min YH, Park HJ, Won HS, Park SJ, Kim DY, Lee BJ. </i> J Biol Chem, 2011","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"21123184","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"fquaglia","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02949r003","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T17:28:17.416Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":125,"term_id":"IDPO:0000011","start":96,"version":2,"statement":[{"text":"In contrast, the unstructured C-terminal region of HP0895 was responsible for binding to HP0894 and underwent a conformational change in the process.","type":"Abstract"},{"text":"Thus, the unstructured HP0895 C-terminal region transforms into a structured form upon binding to HP0894. Furthermore, far-UV CD titrations of HP0894 with HP0895ctp yield a 1:1 stoichiometry with Kd of ∼10−8 M","type":"Results"},{"text":"Our results show that the cellular level functioning of HP0894 is inactivated by binding with HP0895. The direct interaction of these two proteins occurs mainly between the 30-residue C-terminal tail of HP0895 and the N-terminal secondary structure elements and an adjacent C-terminal β-strand of HP0894. Upon binding to HP0894, that unstructured C terminus tail of HP0895 seems to be transformed into structured form.","type":"Discussion"}],"term_name":"disorder to order","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"21123184","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural transition","ec_id":"ECO:0006204","curator_id":"fquaglia","reference_html":"Functional identification of toxin-antitoxin molecules from Helicobacter pylori 26695 and structural elucidation of the molecular interactions. <i> Han KD, Matsuura A, Ahn HC, Kwon AR, Min YH, Park HJ, Won HS, Park SJ, Kim DY, Lee BJ. </i> J Biol Chem, 2011","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP02949r004","validated":{"curator_id":"bmesza","timestamp":"2020-12-12T20:48:21.756Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":125,"term_id":"GO:0097351","start":96,"version":3,"statement":[{"text":"Taken together, it is concluded that the HP0894-HP0895 protein couple is a TA system in H. pylori, where HP0894 is a toxin with an RNase function, whereas HP0895 is an antitoxin functioning by binding to both the toxin and DNA.","type":"Abstract"},{"text":"HP0894 has RNase activity on mRNA, and HP0895 inhibits the decay of mRNA by HP0894. Moreover, HP0894 expression has a toxic effect on E. coli cell growth, but the co-expression of HP0895 neutralizes that HP0894 toxicity.","type":"Discussion"},{"text":"Our results show that the cellular level functioning of HP0894 is inactivated by binding with HP0895. The direct interaction of these two proteins occurs mainly between the 30-residue C-terminal tail of HP0895 and the N-terminal secondary structure elements and an adjacent C-terminal β-strand of HP0894. Upon binding to HP0894, that unstructured C terminus tail of HP0895 seems to be transformed into structured form.","type":"Discussion"}],"term_name":"toxin sequestering activity","ec_name":"experimental phenotypic evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"21123184","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0007634","curator_id":"fquaglia","reference_html":"Functional identification of toxin-antitoxin molecules from Helicobacter pylori 26695 and structural elucidation of the molecular interactions. <i> Han KD, Matsuura A, Ahn HC, Kwon AR, Min YH, Park HJ, Won HS, Park SJ, Kim DY, Lee BJ. </i> J Biol Chem, 2011","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a toxic protein, disabling its function. There may be more than one antitoxin to a toxic protein. Instances of this activity are known only in prokaryotes, where the toxic protein may be a ribonuclease, a DNA gyrase, or other.\" [GOC:rs, PMID:19143615, PMID:19325885, PMID:21819231, PMID:22545240, PMID:24806488, Wikipedia:Toxin-antitoxin_system#Type_II]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_12","ncbi_taxon_id":85962,"disprot_id":"DP02949","date":"2020-10-19T11:14:37.778Z","organism":"Helicobacter pylori (strain ATCC 700392 / 26695)","regions_counter":4,"name":"Uncharacterized protein","UniParc":"UPI00000C08BA","uniref100":"UniRef100_O25555","uniref90":"UniRef90_O25555","uniref50":"UniRef50_O25555","genes":[{"olnNames":[{"value":"HP_0895","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAD07949.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD07949.1"}}]}]}],"alphafold_very_low_content":0.016,"disorder_content":0.24,"disprot_consensus":{"full":[{"start":96,"end":125,"type":"T"}],"Structural state":[{"start":96,"end":125,"type":"D"}],"Molecular function":[{"start":96,"end":125,"type":"F"}],"Structural transition":[{"start":96,"end":125,"type":"T"}]}},{"acc":"P0C079","features":{"pfam":[{"id":"PF04221","name":"RelB antitoxin","start":1,"end":79}],"gene3D":[]},"creator":"fquaglia","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"sequence":"MGSINLRIDDELKARSYAALEKMGVTPSEALRLMLEYIADNERLPFKQTLLSDEDAELVEIVKERLRNPKPVRVTLDEL","length":79,"dataset":["Unicellular toxins and antitoxins","Stress response proteins"],"regions":[{"region_id":"DP02950r001","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T12:54:37.776Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":65,"term_id":"IDPO:0000002","start":43,"version":2,"statement":[{"text":"The following part (Arg43 to Arg65) is largely unstructured as evidenced by random CSI values and low heteronuclei (1H–15N) nuclear Overhauser enhancement (NOE) values (Fig. S2d and e).","type":"Results"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18501926","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"fquaglia","reference_html":"Structural mechanism of transcriptional autorepression of the Escherichia coli RelB/RelE antitoxin/toxin module. <i> Li GY, Zhang Y, Inouye M, Ikura M. </i> J Mol Biol, 2008","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02950r002","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T12:54:49.593Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":79,"term_id":"IDPO:0000002","start":43,"version":2,"statement":[{"text":"In summary, antitoxin RelB possesses a well-folded core domain (Met1–Glu42) at its N-terminus followed by a flexible region (Arg43–Leu79) at its C-terminus, a modular pattern typical of many other antitoxins.","type":"Results"}],"term_name":"disorder","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18501926","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006204","curator_id":"fquaglia","reference_html":"Structural mechanism of transcriptional autorepression of the Escherichia coli RelB/RelE antitoxin/toxin module. <i> Li GY, Zhang Y, Inouye M, Ikura M. </i> J Mol Biol, 2008","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02950r003","validated":{"curator_id":"bmesza","timestamp":"2020-12-12T20:49:46.477Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":79,"term_id":"GO:0005515","start":52,"version":3,"statement":[{"text":"To determine the region within RelB that is responsible for RelB−RelE interaction and antitoxic activity, full-length RelB (RelB1-79) and two N-terminus-truncated antitoxin sequences (RelB36-79 and RelB52-79) were coexpressed with RelE toxin in a single operon using the pBAD promoter control. E. coli strain TOP10 cells, carrying the plasmids, were grown in LB medium, and 0.2% arabinose was added at time zero. The growth rate observed for RelB36-79:RelE- or RelB52-79:RelE-expressing bacteria was indifferent from that of the full-length-RelB:RelE-expressing bacteria (Figure 6A). As a positive control, expression of the RelE toxin using the same pBAD system led to significant growth arrest. The result suggests that RelB interacts and neutralizes RelE toxicity via its C-terminal region. The exact binding domain should be therefore located in the last 28 residues of RelB.","type":"Results"},{"text":"We showed evidence that (i) RelB possesses a high content of α-helical and flexible regions and exhibits a conformationally induced fit upon toxin binding, as many proteins featuring disordered regions do, (ii) RelE is a well-folded protein, displaying a high content of antiparallel β-sheets and β-turns, (iii) RelB, RelE, and the RelBE complex display considerably different thermodynamic stabilities that most likely serve as an important functional basis that regulates the activity of the system under different conditions, (iv) the C-terminal part of RelB is responsible for RelB−RelE interaction, and (iv) the C-terminal part of RelB is likely to be unfolded due to high sensitivity to protease activity and this part interacts with RelE to become more resistant to degradation.","type":"Conclusion"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P0C077","partner_end":null}],"term_name":"protein binding","ec_name":"experimental phenotypic evidence used in manual assertion","reference_html":"Structural and thermodynamic characterization of the Escherichia coli RelBE toxin-antitoxin system: indication for a functional role of differential stability. <i> Cherny I, Overgaard M, Borch J, Bram Y, Gerdes K, Gazit E. </i> Biochemistry, 2007","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"17924660","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0007634","curator_id":"fquaglia","curator_orcid":"0000-0002-0341-4888","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02950r005","validated":{"curator_id":"bmesza","timestamp":"2020-12-12T20:49:59.957Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":79,"term_id":"GO:0097351","start":52,"version":3,"statement":[{"text":"The RelE and RelB proteins constitute the RNA interferase (toxin) and its cognate inhibitor (antitoxin) components of the Escherichia coli relBE toxin−antitoxin system.","type":"Abstract"},{"text":"To determine the region within RelB that is responsible for RelB−RelE interaction and antitoxic activity, full-length RelB (RelB1-79) and two N-terminus-truncated antitoxin sequences (RelB36-79 and RelB52-79) were coexpressed with RelE toxin in a single operon using the pBAD promoter control. E. coli strain TOP10 cells, carrying the plasmids, were grown in LB medium, and 0.2% arabinose was added at time zero. The growth rate observed for RelB36-79:RelE- or RelB52-79:RelE-expressing bacteria was indifferent from that of the full-length-RelB:RelE-expressing bacteria (Figure 6A). As a positive control, expression of the RelE toxin using the same pBAD system led to significant growth arrest. The result suggests that RelB interacts and neutralizes RelE toxicity via its C-terminal region. The exact binding domain should be therefore located in the last 28 residues of RelB.","type":"Results"}],"term_name":"toxin sequestering activity","ec_name":"experimental phenotypic evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"17924660","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0007634","curator_id":"fquaglia","reference_html":"Structural and thermodynamic characterization of the Escherichia coli RelBE toxin-antitoxin system: indication for a functional role of differential stability. <i> Cherny I, Overgaard M, Borch J, Bram Y, Gerdes K, Gazit E. </i> Biochemistry, 2007","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a toxic protein, disabling its function. There may be more than one antitoxin to a toxic protein. Instances of this activity are known only in prokaryotes, where the toxic protein may be a ribonuclease, a DNA gyrase, or other.\" [GOC:rs, PMID:19143615, PMID:19325885, PMID:21819231, PMID:22545240, PMID:24806488, Wikipedia:Toxin-antitoxin_system#Type_II]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02950r006","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T16:42:18.003Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":79,"term_id":"IDPO:0000002","start":47,"version":2,"statement":[{"text":"A 1H-15N HSQC spectrum of 15N,13C-labeled RelBC alone displays poor dispersion of NH resonance (7.9-8.5 ppm), indicating that this C-terminal region of RelB is largely unstructured in its free state (Fig. 2B).","type":"Results"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19297318","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"fquaglia","reference_html":"Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module involves a helix displacement near an mRNA interferase active site. <i> Li GY, Zhang Y, Inouye M, Ikura M. </i> J Biol Chem, 2009","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02950r007","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T16:42:48.846Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":79,"term_id":"IDPO:0000011","start":47,"version":2,"statement":[{"text":"Titration of labeled RelBC with unlabeled RelER81A/R83A shows dramatic chemical shift changes in a similar slow exchange regime (Fig. 2, B and D). The well dispersed spectrum of RelBC in the bound state suggests that RelER81A/R83A binding induces the folding of RelBC.","type":"Results"},{"text":"The chemical shift index analysis (30) of RelBC peptide in both free and bound states revealed a disordered-to-ordered conformation change upon the complex formation (supplemental Fig. S3, A and B).","type":"Results"}],"term_name":"disorder to order","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"19297318","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2KC8"}],"term_namespace":"Structural transition","ec_id":"ECO:0006165","curator_id":"fquaglia","reference_html":"Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module involves a helix displacement near an mRNA interferase active site. <i> Li GY, Zhang Y, Inouye M, Ikura M. </i> J Biol Chem, 2009","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP02950r008","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T16:43:03.746Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":79,"term_id":"GO:0005515","start":47,"version":3,"statement":[{"text":"Titration of labeled RelBC with unlabeled RelER81A/R83A shows dramatic chemical shift changes in a similar slow exchange regime (Fig. 2, B and D). The well dispersed spectrum of RelBC in the bound state suggests that RelER81A/R83A binding induces the folding of RelBC.","type":"Results"},{"text":"The chemical shift index analysis (30) of RelBC peptide in both free and bound states revealed a disordered-to-ordered conformation change upon the complex formation (supplemental Fig. S3, A and B).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P0C077","partner_end":null}],"term_name":"protein binding","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19297318","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2KC8"}],"term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"fquaglia","reference_html":"Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module involves a helix displacement near an mRNA interferase active site. <i> Li GY, Zhang Y, Inouye M, Ikura M. </i> J Biol Chem, 2009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02950r009","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T16:43:16.857Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":79,"term_id":"GO:0097351","start":47,"version":3,"statement":[{"text":"The residual activity of RelER81A/R83A is completely abolished by the addition of the C-terminal domain of RelB antitoxin, RelBC (residues Lys47 to Leu79) (Fig. 1, A-C).","type":"Results"},{"text":"Our structures indicate that RelB counteracts the toxic activity of RelE by displacing alpha4 helix from the catalytically competent position found in the free RelE structure.","type":"Abstract"}],"term_name":"toxin sequestering activity","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"19297318","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2KC8"}],"term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"fquaglia","reference_html":"Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module involves a helix displacement near an mRNA interferase active site. <i> Li GY, Zhang Y, Inouye M, Ikura M. </i> J Biol Chem, 2009","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a toxic protein, disabling its function. There may be more than one antitoxin to a toxic protein. Instances of this activity are known only in prokaryotes, where the toxic protein may be a ribonuclease, a DNA gyrase, or other.\" [GOC:rs, PMID:19143615, PMID:19325885, PMID:21819231, PMID:22545240, PMID:24806488, Wikipedia:Toxin-antitoxin_system#Type_II]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02950r010","validated":{"curator_id":"bmesza","timestamp":"2020-12-12T20:49:19.690Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":79,"term_id":"IDPO:0000002","start":47,"version":2,"statement":[{"text":"The apparent melting temperature of RelBC was estimated to be below 10 °C (Fig. 1b). In summary, antitoxin RelB possesses a well-folded core domain (Met1–Glu42) at its N-terminus followed by a flexible region (Arg43–Leu79) at its C-terminus, a modular pattern typical of many other antitoxins.","type":"Results"}],"term_name":"disorder","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18501926","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006317","curator_id":"fquaglia","reference_html":"Structural mechanism of transcriptional autorepression of the Escherichia coli RelB/RelE antitoxin/toxin module. <i> Li GY, Zhang Y, Inouye M, Ikura M. </i> J Mol Biol, 2008","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02950r011","validated":{"curator_id":"bmesza","timestamp":"2020-12-12T20:49:34.683Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":79,"term_id":"IDPO:0000002","start":47,"version":2,"statement":[{"text":"Firstly, size-exclusion analysis of RelB (9.38 kDa) yielded an apparent molecular mass (66.9 kDa) that is significantly larger than that of a dimer (as exhibited by many other antitoxin dimers) and closer to that of a septamer. Since the determination of molecular mass by SEC is related to the shape of the molecule, it is less accurate with nonglobular proteins. It is likely that the SEC method overestimates the size of RelB because the unstructured C-terminal region does not fold into a compact globular conformation.","type":"Results"}],"term_name":"disorder","ec_name":"chromatography evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"18501926","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0007680","curator_id":"fquaglia","reference_html":"Structural mechanism of transcriptional autorepression of the Escherichia coli RelB/RelE antitoxin/toxin module. <i> Li GY, Zhang Y, Inouye M, Ikura M. </i> J Mol Biol, 2008","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","ncbi_taxon_id":83333,"disprot_id":"DP02950","date":"2020-10-19T11:30:39.064Z","organism":"Escherichia coli (strain K12)","regions_counter":11,"name":"Antitoxin RelB","UniParc":"UPI0000133664","uniref100":"UniRef100_P0C079","uniref90":"UniRef90_P0C079","uniref50":"UniRef50_P0C079","genes":[{"name":{"value":"relB"},"olnNames":[{"value":"b1564"},{"value":"JW1556"}]}],"alphafold_very_low_content":0,"disorder_content":0.46835443037974683,"disprot_consensus":{"full":[{"start":43,"end":46,"type":"D"},{"start":47,"end":79,"type":"T"}],"Structural state":[{"start":43,"end":79,"type":"D"}],"Molecular function":[{"start":47,"end":79,"type":"F"}],"Structural transition":[{"start":47,"end":79,"type":"T"}]}},{"acc":"P01501","features":{"pfam":[{"id":"PF01372","name":"Melittin","start":44,"end":69}],"gene3D":[]},"creator":"fquaglia","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Hymenoptera","Apocrita","Aculeata","Apoidea","Apidae","Apis"],"sequence":"MKFLVNVALVFMVVYISYIYAAPEPEPAPEPEAEADAEADPEAGIGAVLKVLTTGLPALISWIKRKRQQG","length":70,"dataset":[],"regions":[{"region_id":"DP02951r001","unpublished":true,"validated":{"curator_id":"bmesza","timestamp":"2020-11-27T14:34:55.423Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":70,"term_id":"IDPO:0000002","start":44,"version":2,"statement":[{"text":"Analysis of chemical shifts and steady state heteronuclear nuclear Overhauser effect (NOE) patterns indicated that melittin is unstructured without TFE, but assumes stable helical conformation above a certain TFE concentration threshold.","type":"Introduction"},{"text":"The 15N-HSQC spectrum of melittin in aqueous solution at pH 7.0 without TFE (Figure 2B) showed a limited chemical shift dispersion along the 1H dimension indicative of an unstructured form.","type":"Results"},{"text":"It is known that melittin is unstructured at low concentrations in aqueous solutions, and more structured when bound to lipids, cell-surface GAGs, and proteins.","type":"Discussion"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"29668274","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"fquaglia","reference_html":"Nuclear Magnetic Resonance-Based Structural Characterization and Backbone Dynamics of Recombinant Bee Venom Melittin. <i> Ramirez L, Shekhtman A, Pande J. </i> Biochemistry, 2018","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02951r002","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-11-27T15:15:26.516Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":70,"term_id":"IDPO:0000011","start":44,"version":2,"statement":[{"text":"At 30% TFE (Figure 4B), there is an overall reduction in flexibility manifested by the higher positive heteronuclear NOEs. In general, the trans conformer was less flexible than the cis, and the difference is more pronounced for residues 15-17, and 19-21. The trans conformer has large positive heteronuclear NOEs (0.57 - 0.94 for residues 4-24) throughout the chain, and this is consistent with the formation of stable helices.","type":"Results"}],"term_name":"disorder to order","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0919-4449","released":"2022_03","term_ontology":"IDPO","curator_name":"Bálint Mészáros","reference_id":"29668274","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural transition","ec_id":"ECO:0006165","curator_id":"bmesza","reference_html":"Nuclear Magnetic Resonance-Based Structural Characterization and Backbone Dynamics of Recombinant Bee Venom Melittin. <i> Ramirez L, Shekhtman A, Pande J. </i> Biochemistry, 2018","ec_go":"EXP","disprot_namespace":"Structural transition"},{"region_id":"DP02951r003","unpublished":true,"ec_ontology":"ECO","end":63,"term_id":"GO:0005515","start":58,"version":3,"statement":[{"text":"We identified the amino acids in melittinimportant for binding to HAA by saturation-transfer difference (STD) nuclearmagnetic resonance (NMR) experiments, and analysis of NMR line broadening upon titration of melittin with HAA. Our results suggest that hydrophobic resi-dues Ile17 and Ile20 on the C-terminal region of melittin are in close contactwith HAA in the melittin-HAA complex.","type":"Abstract"},{"text":"The melittin residues that showed the highest signal broadening upon addition of HAA were Ile17, and Ile20, with above 60% decrease in peak intensity (Figure 2). Next to these are Leu13, Ala15, Leu16, Ser18, and Trp19, which showed at least 50% decrease in peak amplitude. It is important to note that most of these residues have hydrophobic side chains, thus suggesting that hydrophobic interaction between HAA and melittin drives the binding event, consistent with our ITC findings.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P02489","partner_end":null}],"term_name":"protein binding","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"31762096","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006165","curator_id":"fquaglia","reference_html":"Hydrophobic residues of melittin mediate its binding to αA-crystallin. <i> Ramirez LM, Shekhtman A, Pande J. </i> Protein Sci, 2020","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-28T19:50:48.008Z"}},{"region_id":"DP02951r004","unpublished":true,"ec_ontology":"ECO","end":69,"term_id":"GO:0005515","start":44,"version":3,"statement":[{"text":"We characterized the thermodynamic parameters of the binding process between melittin and HAA through isothermal titration calorimetry (ITC), and found the binding tobe endothermic and entropy-driven.","type":"Abstract"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P02489","partner_end":null}],"term_name":"protein binding","ec_name":"isothermal titration calorimetry evidence used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","reference_id":"31762096","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"fquaglia","reference_html":"Hydrophobic residues of melittin mediate its binding to αA-crystallin. <i> Ramirez LM, Shekhtman A, Pande J. </i> Protein Sci, 2020","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-28T18:56:17.859Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":68,"term_name":"lipid binding","reference_html":"Honeybee venom and melittin suppress growth factor receptor activation in HER2-enriched and triple-negative breast cancer. <i> Duffy C, Sorolla A, Wang E, Golden E, Woodward E, Davern K, Ho D, Johnstone E, Pfleger K, Redfern A, Iyer KS, Baer B, Blancafort P. </i> NPJ Precis Oncol, 2020","start":63,"region_id":"DP02951r005","term_id":"GO:0008289","unpublished":true,"version":3,"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"enzymatic activity assay evidence used in manual assertion","statement":[{"text":"To assess the functional role of the positive (K21RKR24) sequence in the C-terminus of melittin, we designed a negatively charged melittin peptide (D21EDE24-melittin). These negative residues were predicted to disrupt the binding of melittin with the plasma membrane.","type":"Results"},{"text":"These data demonstrate that residues required for melittin activity include those residing in the C-terminal α-helix, comprising several key positively charged residues necessary for interaction with the plasma membrane.","type":"Results"}],"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005801","reference_id":"32923684","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-28T18:56:18.000Z"}},{"term_namespace":"Biological process","ec_ontology":"ECO","end":68,"term_name":"localization","reference_html":"Honeybee venom and melittin suppress growth factor receptor activation in HER2-enriched and triple-negative breast cancer. <i> Duffy C, Sorolla A, Wang E, Golden E, Woodward E, Davern K, Ho D, Johnstone E, Pfleger K, Redfern A, Iyer KS, Baer B, Blancafort P. </i> NPJ Precis Oncol, 2020","start":63,"region_id":"DP02951r006","term_id":"GO:0051179","unpublished":true,"version":3,"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"enzymatic activity assay evidence used in manual assertion","statement":[{"text":"To assess the functional role of the positive (K21RKR24) sequence in the C-terminus of melittin, we designed a negatively charged melittin peptide (D21EDE24-melittin). These negative residues were predicted to disrupt the binding of melittin with the plasma membrane.","type":"Results"},{"text":"These data demonstrate that residues required for melittin activity include those residing in the C-terminal α-helix, comprising several key positively charged residues necessary for interaction with the plasma membrane.","type":"Results"}],"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005801","reference_id":"32923684","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-28T18:05:13.782Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":70,"term_name":"molecular function inhibitor activity","reference_html":"Honeybee venom and melittin suppress growth factor receptor activation in HER2-enriched and triple-negative breast cancer. <i> Duffy C, Sorolla A, Wang E, Golden E, Woodward E, Davern K, Ho D, Johnstone E, Pfleger K, Redfern A, Iyer KS, Baer B, Blancafort P. </i> NPJ Precis Oncol, 2020","start":44,"region_id":"DP02951r007","term_id":"GO:0140678","unpublished":true,"version":3,"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"qualitative western immunoblotting evidence used in manual assertion","statement":[{"text":"Honeybee venom and melittin suppress the activation of EGFR and HER2 by interfering with the phosphorylation of these receptors in the plasma membrane of breast carcinoma cells.","type":"Abstract"},{"text":"Honeybee venom and melittin suppress the phosphorylation of EGFR and HER2.","type":"Figure"},{"text":"Here, we show that honeybee venom and melittin suppress the ligand-induced phosphorylation of EGFR and HER2, dynamically modulating downstream signaling pathways in breast cancer cells.","type":"Discussion"}],"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000279","reference_id":"32923684","ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-28T18:05:08.563Z"}}],"released":"2021_12","ncbi_taxon_id":7460,"disprot_id":"DP02951","date":"2020-10-19T15:20:21.247Z","organism":"Apis mellifera","regions_counter":7,"name":"Melittin","UniParc":"UPI000012EED4","uniref100":"UniRef100_P01501","uniref90":"UniRef90_P01501","uniref50":"UniRef50_P01501","genes":[{"name":{"value":"MELT"}}],"alphafold_very_low_content":0.18571428571428572,"disorder_content":0.38571428571428573,"disprot_consensus":{"full":[{"start":44,"end":70,"type":"T"}],"Structural state":[{"start":44,"end":70,"type":"D"}],"Structural transition":[{"start":44,"end":70,"type":"T"}],"Molecular function":[{"start":44,"end":70,"type":"F"}],"Biological process":[{"start":63,"end":68,"type":"F"}]}},{"acc":"P08572","features":{"pfam":[{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":61,"end":116},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":184,"end":232},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":293,"end":347},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":423,"end":482},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":494,"end":549},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":684,"end":738},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":780,"end":837},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":920,"end":978},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":1033,"end":1088},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":1101,"end":1159},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":1182,"end":1233},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":1332,"end":1389},{"id":"PF01413","name":"C-terminal tandem repeated domain in type 4 procollagen","start":1491,"end":1594},{"id":"PF01413","name":"C-terminal tandem repeated domain in type 4 procollagen","start":1599,"end":1710}],"gene3D":[]},"creator":"gpozzati","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MGRDQRAVAGPALRRWLLLGTVTVGFLAQSVLAGVKKFDVPCGGRDCSGGCQCYPEKGGRGQPGPVGPQGYNGPPGLQGFPGLQGRKGDKGERGAPGVTGPKGDVGARGVSGFPGADGIPGHPGQGGPRGRPGYDGCNGTQGDSGPQGPPGSEGFTGPPGPQGPKGQKGEPYALPKEERDRYRGEPGEPGLVGFQGPPGRPGHVGQMGPVGAPGRPGPPGPPGPKGQQGNRGLGFYGVKGEKGDVGQPGPNGIPSDTLHPIIAPTGVTFHPDQYKGEKGSEGEPGIRGISLKGEEGIMGFPGLRGYPGLSGEKGSPGQKGSRGLDGYQGPDGPRGPKGEAGDPGPPGLPAYSPHPSLAKGARGDPGFPGAQGEPGSQGEPGDPGLPGPPGLSIGDGDQRRGLPGEMGPKGFIGDPGIPALYGGPPGPDGKRGPPGPPGLPGPPGPDGFLFGLKGAKGRAGFPGLPGSPGARGPKGWKGDAGECRCTEGDEAIKGLPGLPGPKGFAGINGEPGRKGDRGDPGQHGLPGFPGLKGVPGNIGAPGPKGAKGDSRTITTKGERGQPGVPGVPGMKGDDGSPGRDGLDGFPGLPGPPGDGIKGPPGDPGYPGIPGTKGTPGEMGPPGLGLPGLKGQRGFPGDAGLPGPPGFLGPPGPAGTPGQIDCDTDVKRAVGGDRQEAIQPGCIGGPKGLPGLPGPPGPTGAKGLRGIPGFAGADGGPGPRGLPGDAGREGFPGPPGFIGPRGSKGAVGLPGPDGSPGPIGLPGPDGPPGERGLPGEVLGAQPGPRGDAGVPGQPGLKGLPGDRGPPGFRGSQGMPGMPGLKGQPGLPGPSGQPGLYGPPGLHGFPGAPGQEGPLGLPGIPGREGLPGDRGDPGDTGAPGPVGMKGLSGDRGDAGFTGEQGHPGSPGFKGIDGMPGTPGLKGDRGSPGMDGFQGMPGLKGRPGFPGSKGEAGFFGIPGLKGLAGEPGFKGSRGDPGPPGPPPVILPGMKDIKGEKGDEGPMGLKGYLGAKGIQGMPGIPGLSGIPGLPGRPGHIKGVKGDIGVPGIPGLPGFPGVAGPPGITGFPGFIGSRGDKGAPGRAGLYGEIGATGDFGDIGDTINLPGRPGLKGERGTTGIPGLKGFFGEKGTEGDIGFPGITGVTGVQGPPGLKGQTGFPGLTGPPGSQGELGRIGLPGGKGDDGWPGAPGLPGFPGLRGIRGLHGLPGTKGFPGSPGSDIHGDPGFPGPPGERGDPGEANTLPGPVGVPGQKGDQGAPGERGPPGSPGLQGFPGITPPSNISGAPGDKGAPGIFGLKGYRGPPGPPGSAALPGSKGDTGNPGAPGTPGTKGWAGDSGPQGRPGVFGLPGEKGPRGEQGFMGNTGPTGAVGDRGPKGPKGDPGFPGAPGTVGAPGIAGIPQKIAVQPGTVGPQGRRGPPGAPGEMGPQGPPGEPGFRGAPGKAGPQGRGGVSAVPGFRGDEGPIGHQGPIGQEGAPGRPGSPGLPGMPGRSVSIGYLLVKHSQTDQEPMCPVGMNKLWSGYSLLYFEGQEKAHNQDLGLAGSCLARFSTMPFLYCNPGDVCYYASRNDKSYWLSTTAPLPMMPVAEDEIKPYISRCSVCEAPAIAIAVHSQDVSIPHCPAGWRSLWIGYSFLMHTAAGDEGGGQSLVSPGSCLEDFRATPFIECNGGRGTCHYYANKYSFWLTTIPEQSFQGSPSADTLKAGLIRTHISRCQVCMKNL","name":"Collagen alpha-2(IV) chain","regions":[{"region_id":"DP02953r001","unpublished":true,"validated":{"curator_id":"bmesza","timestamp":"2020-11-27T13:41:23.123Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":1638,"term_id":"IDPO:0000002","start":1629,"version":2,"statement":[{"text":"These hairpins (residues 37–45 in the case of SM1 and\nresidues 144–154 in the case of SM1') were not visible in the\nstructure of a2NC1 homo (Fig. 3), as would be expected if they\nwere disordered in this noncanonical homo-octamer.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-4303-9939","released":"2023_06","term_ontology":"IDPO","curator_name":"Gabriele Pozzati","reference_id":"30443360","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5NB2"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"gpozzati","reference_html":"Structures of collagen IV globular domains: insight into associated pathologies, folding and network assembly. <i> Casino P, Gozalbo-Rovira R, Rodríguez-Díaz J, Banerjee S, Boutaud A, Rubio V, Hudson BG, Saus J, Cervera J, Marina A. </i> IUCrJ, 2018","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02953r003","unpublished":true,"validated":{"curator_id":"bmesza","timestamp":"2020-11-27T13:41:24.023Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":1696,"term_id":"IDPO:0000002","start":1680,"version":2,"statement":[{"text":"SM3' was disordered and was not visible in either a2NC1 homo\nor a4NC1 homo (Fig. 3)","type":"Results"},{"text":"a2NC1 domain is crystallized in 5NB2 while a4NC1 is crystallized in 5NB1 (however such PDB is not associated to this UniprotID)","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-4303-9939","released":"2023_06","term_ontology":"IDPO","curator_name":"Gabriele Pozzati","reference_id":"30443360","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5NB2"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"gpozzati","reference_html":"Structures of collagen IV globular domains: insight into associated pathologies, folding and network assembly. <i> Casino P, Gozalbo-Rovira R, Rodríguez-Díaz J, Banerjee S, Boutaud A, Rubio V, Hudson BG, Saus J, Cervera J, Marina A. </i> IUCrJ, 2018","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1680,"end":1696,"reference_id":"30443360","reference_source":"pmid","reference_html":"Structures of collagen IV globular domains: insight into associated pathologies, folding and network assembly. <i> Casino P, Gozalbo-Rovira R, Rodríguez-Díaz J, Banerjee S, Boutaud A, Rubio V, Hudson BG, Saus J, Cervera J, Marina A. </i> IUCrJ, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"gpozzati","curator_name":"Gabriele Pozzati","curator_orcid":"0000-0002-4303-9939","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"cross_refs":[{"db":"PDB","id":"5NB2"},{"db":"PDB","id":"5NAX"}],"region_id":"DP02953r006","statement":[{"text":"Here, we define three structural motifs in sheet II (Fig. 3), SM1 (hairpin b3–b4), SM2 (hairpin b6–b7) and SM3 (b9 and the preceding loop), and their homologous counterparts in sheet II0, SM1’ (hairpin b3’–b4’), SM2’ (hairpin b6’–b7’) and SM3’ (b9’ and the preceding loop) (Figs. 3a and 3b).","type":"Results"},{"text":"The comparison between the structure of the a2NC1 domain in its noncanonical homohexamer and the same domain in a121NC1 (a2NC1a121) revealed that there are conformational differences that might explain the greater number of subunits (Fig. 2, Supplementary Fig. S6).","type":"Results"},{"text":"Overall, a comparison of noncanonical and canonical oligomers (Figs. 3a and 3b) revealed that the SM1, SM1’ and SM2 flexible regions are key determinants in protomer formation, while the loops connecting these motifs, Lb7b8 (motif ClA), Lb70b80 and SM3’, are needed to establish the protomer–protomer interactions that generate the hexamer.","type":"Results"},{"text":"Indeed, previous work with the natural a121NC1 heterohexamer has reported structural inter-chain variability in the conformations of these loops (Sundaramoorthy et al., 2002; Than et al., 2002).","type":"Results"},{"text":"Proposed model for canonical hexamer assembly. Individual monomers (a) start to nucleate a protomer via\n\nb-sheets I/I0 (b). Next, the SM1/1’ and SM2/SM2’ flexible regions from b-sheets II/II0 are stabilized in the nascent protomer, resulting in favoured additional intersubunit interactions within the protomer (c). Final stabilization is attained with the proper folding of SM3’ and of the ClA and ClB motifs that allow the binding of chloride ions (green spheres) (d). The two protomers in the hexamer are now ready to be joined by sulfilimine bonds (red lines).","type":"Figure"},{"text":"Our findings of noncanonical assemblies for a2NC1 and a4NC1 homo-oligomers and the structural changes observed in the chains forming these noncanonical protomers in comparison to a2NC1_121 and to the chains in a1NC1homo, a3NC1homo and a5NC1homo could imply that chain folding is closely related to protomer assembly. It is unlikely that a2NC1homo and a4NC1homo could represent stable physiological assemblies, but the structures of the individual chains in these noncanonical oligomers might provide a frozen glimpse of transient conformational states in the process of NC1 folding and hexamer building.","type":"Discussion"},{"text":"The disordered loops are present in the noncanonical octamer (5NB2_B), while the same loops are ordered when the a2NC1 chain is assembled into the canonical a2NC1_121 hexamer (5NAX).","type":"Curator statement"}],"validated":{"curator_name":"Lucia Chemes","curator_id":"lchemes","timestamp":"2021-06-15T21:00:38.787Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":1629,"end":1638,"reference_id":"30443360","reference_source":"pmid","reference_html":"Structures of collagen IV globular domains: insight into associated pathologies, folding and network assembly. <i> Casino P, Gozalbo-Rovira R, Rodríguez-Díaz J, Banerjee S, Boutaud A, Rubio V, Hudson BG, Saus J, Cervera J, Marina A. </i> IUCrJ, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"gpozzati","curator_name":"Gabriele Pozzati","curator_orcid":"0000-0002-4303-9939","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"cross_refs":[{"db":"PDB","id":"5NB2"},{"db":"PDB","id":"5NAX"}],"region_id":"DP02953r007","statement":[{"text":"Here, we define three structural motifs in sheet II (Fig. 3), SM1 (hairpin b3–b4), SM2 (hairpin b6–b7) and SM3 (b9 and the preceding loop), and their homologous counterparts in sheet II0, SM1’ (hairpin b3’–b4’), SM2’ (hairpin b6’–b7’) and SM3’ (b9’ and the preceding loop) (Figs. 3a and 3b).","type":"Results"},{"text":"The comparison between the structure of the a2NC1 domain in its noncanonical homohexamer and the same domain in a121NC1 (a2NC1a121) revealed that there are conformational differences that might explain the greater number of subunits (Fig. 2, Supplementary Fig. S6).","type":"Results"},{"text":"As can be seen in the canonical structures, SM1 and SM1’ (Fig. 3b) face the central tunnel, creating a closed ‘barrel’-like arrangement of six alternating b4 and b40 strands, which allows compact intertwining of three monomers (Than et al., 2002). These hairpins (residues 37–45 in the case of SM1 and residues 144–154 in the case of SM10) were not visible in the structure of a2NC1homo (Fig. 3), as would be expected if they were disordered in this noncanonical homo-octamer. On the other hand, they were visible in a4NC1homo but with a different conformation to that in a2NC1121 (Fig. 3). These changes are expected to decrease the strength of the association of the subunits into the protomer.","type":"Results"},{"text":"Overall, a comparison of noncanonical and canonical oligomers (Figs. 3a and 3b) revealed that the SM1, SM1’ and SM2 flexible regions are key determinants in protomer formation, while the loops connecting these motifs, Lb7b8 (motif ClA), Lb70b80 and SM3’, are needed to establish the protomer–protomer interactions that generate the hexamer.","type":"Results"},{"text":"Indeed, previous work with the natural a121NC1 heterohexamer has reported structural inter-chain variability in the conformations of these loops (Sundaramoorthy et al., 2002; Than et al., 2002).","type":"Results"},{"text":"Proposed model for canonical hexamer assembly. Individual monomers (a) start to nucleate a protomer via\n\nb-sheets I/I0 (b). Next, the SM1/1’ and SM2/SM2’ flexible regions from b-sheets II/II0 are stabilized in the nascent protomer, resulting in favoured additional intersubunit interactions within the protomer (c). Final stabilization is attained with the proper folding of SM3’ and of the ClA and ClB motifs that allow the binding of chloride ions (green spheres) (d). The two protomers in the hexamer are now ready to be joined by sulfilimine bonds (red lines).","type":"Figure"},{"text":"Our findings of noncanonical assemblies for a2NC1 and a4NC1 homo-oligomers and the structural changes observed in the chains forming these noncanonical protomers in comparison to a2NC1_121 and to the chains in a1NC1homo, a3NC1homo and a5NC1homo could imply that chain folding is closely related to protomer assembly. It is unlikely that a2NC1homo and a4NC1homo could represent stable physiological assemblies, but the structures of the individual chains in these noncanonical oligomers might provide a frozen glimpse of transient conformational states in the process of NC1 folding and hexamer building.","type":"Discussion"},{"text":"The disordered loops are present in the noncanonical octamer (5NB2_B), while the same loops are ordered when the a2NC1 chain is assembled into the canonical a2NC1_121 hexamer (5NAX).","type":"Curator statement"}],"validated":{"curator_name":"Lucia Chemes","curator_id":"lchemes","timestamp":"2021-06-15T21:00:32.272Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":1629,"end":1638,"reference_id":"30443360","reference_source":"pmid","reference_html":"Structures of collagen IV globular domains: insight into associated pathologies, folding and network assembly. <i> Casino P, Gozalbo-Rovira R, Rodríguez-Díaz J, Banerjee S, Boutaud A, Rubio V, Hudson BG, Saus J, Cervera J, Marina A. </i> IUCrJ, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"gpozzati","curator_name":"Gabriele Pozzati","curator_orcid":"0000-0002-4303-9939","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":3,"cross_refs":[{"db":"PDB","id":"5NB2"},{"db":"PDB","id":"5NAX"}],"region_id":"DP02953r009","statement":[{"text":"Overall, a comparison of noncanonical and canonical oligomers (Figs. 3a and 3b) revealed that the SM1, SM1’ and SM2 flexible regions are key determinants in protomer formation, while the loops connecting these motifs, Lb7b8 (motif ClA), Lb70b80 and SM3’, are needed to establish the protomer–protomer interactions that generate the hexamer.","type":"Results"},{"text":"Proposed model for canonical hexamer assembly. Individual monomers (a) start to nucleate a protomer via\n\nb-sheets I/I0 (b). Next, the SM1/1’ and SM2/SM2’ flexible regions from b-sheets II/II0 are stabilized in the nascent protomer, resulting in favoured additional intersubunit interactions within the protomer (c). Final stabilization is attained with the proper folding of SM3’ and of the ClA and ClB motifs that allow the binding of chloride ions (green spheres) (d). The two protomers in the hexamer are now ready to be joined by sulfilimine bonds (red lines).","type":"Figure"},{"text":"Our findings of noncanonical assemblies for a2NC1 and a4NC1 homo-oligomers and the structural changes observed in the chains forming these noncanonical protomers in comparison to a2NC1_121 and to the chains in a1NC1homo, a3NC1homo and a5NC1homo could imply that chain folding is closely related to protomer assembly. It is unlikely that a2NC1homo and a4NC1homo could represent stable physiological assemblies, but the structures of the individual chains in these noncanonical oligomers might provide a frozen glimpse of transient conformational states in the process of NC1 folding and hexamer building.","type":"Discussion"},{"text":"The disordered loops are present in the noncanonical octamer (5NB2_B), while the same loops are ordered when the a2NC1 chain is assembled into the canonical a2NC1_121 hexamer (5NAX).","type":"Curator statement"}],"validated":{"curator_name":"Lucia Chemes","curator_id":"lchemes","timestamp":"2021-06-16T12:33:16.032Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":1680,"end":1696,"reference_id":"30443360","reference_source":"pmid","reference_html":"Structures of collagen IV globular domains: insight into associated pathologies, folding and network assembly. <i> Casino P, Gozalbo-Rovira R, Rodríguez-Díaz J, Banerjee S, Boutaud A, Rubio V, Hudson BG, Saus J, Cervera J, Marina A. </i> IUCrJ, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"gpozzati","curator_name":"Gabriele Pozzati","curator_orcid":"0000-0002-4303-9939","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":3,"cross_refs":[{"db":"PDB","id":"5NB2"},{"db":"PDB","id":"5NAX"}],"region_id":"DP02953r010","statement":[{"text":"Overall, a comparison of noncanonical and canonical oligomers (Figs. 3a and 3b) revealed that the SM1, SM1’ and SM2 flexible regions are key determinants in protomer formation, while the loops connecting these motifs, Lb7b8 (motif ClA), Lb70b80 and SM3’, are needed to establish the protomer–protomer interactions that generate the hexamer.","type":"Results"},{"text":"Proposed model for canonical hexamer assembly. Individual monomers (a) start to nucleate a protomer via\n\nb-sheets I/I0 (b). Next, the SM1/1’ and SM2/SM2’ flexible regions from b-sheets II/II0 are stabilized in the nascent protomer, resulting in favoured additional intersubunit interactions within the protomer (c). Final stabilization is attained with the proper folding of SM3’ and of the ClA and ClB motifs that allow the binding of chloride ions (green spheres) (d). The two protomers in the hexamer are now ready to be joined by sulfilimine bonds (red lines).","type":"Figure"},{"text":"Our findings of noncanonical assemblies for a2NC1 and a4NC1 homo-oligomers and the structural changes observed in the chains forming these noncanonical protomers in comparison to a2NC1_121 and to the chains in a1NC1homo, a3NC1homo and a5NC1homo could imply that chain folding is closely related to protomer assembly. It is unlikely that a2NC1homo and a4NC1homo could represent stable physiological assemblies, but the structures of the individual chains in these noncanonical oligomers might provide a frozen glimpse of transient conformational states in the process of NC1 folding and hexamer building.","type":"Discussion"},{"text":"The disordered loops are present in the noncanonical octamer (5NB2_B), while the same loops are ordered when the a2NC1 chain is assembled into the canonical a2NC1_121 hexamer (5NAX).","type":"Curator statement"}],"validated":{"curator_name":"Lucia Chemes","curator_id":"lchemes","timestamp":"2021-06-16T12:33:12.453Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2023_06","length":1712,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP02953","date":"2020-10-28T14:26:27.139Z","regions_counter":10,"dataset":["NDDs-related proteins","Extracellular matrix proteins"],"UniParc":"UPI0000126D42","uniref100":"UniRef100_P08572","uniref90":"UniRef90_P08572","uniref50":"UniRef50_P08572","genes":[{"name":{"value":"COL4A2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:2203","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:2203"}}]}}],"alphafold_very_low_content":0.7710280373831776,"disorder_content":0.015771028037383176,"disprot_consensus":{"full":[{"start":1629,"end":1638,"type":"T"},{"start":1680,"end":1696,"type":"T"}],"Structural state":[{"start":1629,"end":1638,"type":"D"},{"start":1680,"end":1696,"type":"D"}],"Structural transition":[{"start":1629,"end":1638,"type":"T"},{"start":1680,"end":1696,"type":"T"}],"Disorder function":[{"start":1629,"end":1638,"type":"F"}],"Molecular function":[{"start":1680,"end":1696,"type":"F"}]}},{"acc":"Q12888","features":{"pfam":[{"id":"PF09038","name":"Tumour suppressor p53-binding protein-1 Tudor","start":1483,"end":1604},{"id":"PF18428","name":"BRCA1 C Terminus (BRCT) domain","start":1867,"end":1969}],"gene3D":[]},"creator":"zskalman","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MDPTGSQLDSDFSQQDTPCLIIEDSQPESQVLEDDSGSHFSMLSRHLPNLQTHKENPVLDVVSNPEQTAGEERGDGNSGFNEHLKENKVADPVDSSNLDTCGSISQVIEQLPQPNRTSSVLGMSVESAPAVEEEKGEELEQKEKEKEEDTSGNTTHSLGAEDTASSQLGFGVLELSQSQDVEENTVPYEVDKEQLQSVTTNSGYTRLSDVDANTAIKHEEQSNEDIPIAEQSSKDIPVTAQPSKDVHVVKEQNPPPARSEDMPFSPKASVAAMEAKEQLSAQELMESGLQIQKSPEPEVLSTQEDLFDQSNKTVSSDGCSTPSREEGGCSLASTPATTLHLLQLSGQRSLVQDSLSTNSSDLVAPSPDAFRSTPFIVPSSPTEQEGRQDKPMDTSVLSEEGGEPFQKKLQSGEPVELENPPLLPESTVSPQASTPISQSTPVFPPGSLPIPSQPQFSHDIFIPSPSLEEQSNDGKKDGDMHSSSLTVECSKTSEIEPKNSPEDLGLSLTGDSCKLMLSTSEYSQSPKMESLSSHRIDEDGENTQIEDTEPMSPVLNSKFVPAENDSILMNPAQDGEVQLSQNDDKTKGDDTDTRDDISILATGCKGREETVAEDVCIDLTCDSGSQAVPSPATRSEALSSVLDQEEAMEIKEHHPEEGSSGSEVEEIPETPCESQGEELKEENMESVPLHLSLTETQSQGLCLQKEMPKKECSEAMEVETSVISIDSPQKLAILDQELEHKEQEAWEEATSEDSSVVIVDVKEPSPRVDVSCEPLEGVEKCSDSQSWEDIAPEIEPCAENRLDTKEEKSVEYEGDLKSGTAETEPVEQDSSQPSLPLVRADDPLRLDQELQQPQTQEKTSNSLTEDSKMANAKQLSSDAEAQKLGKPSAHASQSFCESSSETPFHFTLPKEGDIIPPLTGATPPLIGHLKLEPKRHSTPIGISNYPESTIATSDVMSESMVETHDPILGSGKGDSGAAPDVDDKLCLRMKLVSPETEASEESLQFNLEKPATGERKNGSTAVAESVASPQKTMSVLSCICEARQENEARSEDPPTTPIRGNLLHFPSSQGEEEKEKLEGDHTIRQSQQPMKPISPVKDPVSPASQKMVIQGPSSPQGEAMVTDVLEDQKEGRSTNKENPSKALIERPSQNNIGIQTMECSLRVPETVSAATQTIKNVCEQGTSTVDQNFGKQDATVQTERGSGEKPVSAPGDDTESLHSQGEEEFDMPQPPHGHVLHRHMRTIREVRTLVTRVITDVYYVDGTEVERKVTEETEEPIVECQECETEVSPSQTGGSSGDLGDISSFSSKASSLHRTSSGTSLSAMHSSGSSGKGAGPLRGKTSGTEPADFALPSSRGGPGKLSPRKGVSQTGTPVCEEDGDAGLGIRQGGKAPVTPRGRGRRGRPPSRTTGTRETAVPGPLGIEDISPNLSPDDKSFSRVVPRVPDSTRRTDVGAGALRRSDSPEIPFQAAAGPSDGLDASSPGNSFVGLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDILLCDPIPLDTEVTALSEDEYFSAGVVKGHRKESGELYYSIEKEGQRKWYKRMAVILSLEQGNRLREQYGLGPYEAVTPLTKAADISLDNLVEGKRKRRSNVSSPATPTASSSSSTTPTRKITESPRASMGVLSGKRKLITSEEERSPAKRGRKSATVKPGAVGAGEFVSPCESGDNTGEPSALEEQRGPLPLNKTLFLGYAFLLTMATTSDKLASRSKLPDGPTGSSEEEEEFLEIPPFNKQYTESQLRAGAGYILEDFNEAQCNTAYQCLLIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHANQLQNYRNYLLPAGYSLEEQRILDWQPRENPFQNLKVLLVSDQQQNFLELWSEILMTGGAASVKQHHSSAHNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEWVIQCLIVGERIGFKQHPKYKHDYVSH","name":"TP53-binding protein 1","regions":[{"region_id":"DP02954r001","validated":{"curator_id":"bmesza","timestamp":"2020-11-27T14:09:58.332Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":1768,"term_id":"IDPO:0000002","start":1750,"version":2,"statement":[{"text":"The N-terminal BRCT domain of BP1 contains a unique large insertion of 29 residues (1741-1769) rich in polar and charged residues between b1 and a1 that are not found in BRCA1 or other BRCTs. In our structure, this region is very disordered, probably indicating that it is highly fexible. However, in the first copy of BP1, some broken electron density is interpretable for residues 1741-1750 and there is good indication from model\nbuilding that these residues form an a-helical structure (a-I) that extends from the surface of the N-terminal BRCT domain into the solvent (Figure 1).","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-4303-9939","released":"2022_03","term_ontology":"IDPO","curator_name":"Gabriele Pozzati","reference_id":"12110597","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1GZH"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"gpozzati","reference_html":"Crystal structure of human 53BP1 BRCT domains bound to p53 tumour suppressor. <i> Derbyshire DJ, Basu BP, Serpell LC, Joo WS, Date T, Iwabuchi K, Doherty AJ. </i> EMBO J, 2002","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1741,"end":1767,"reference_id":"11877378","reference_source":"pmid","reference_html":"Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure. <i> Joo WS, Jeffrey PD, Cantor SB, Finnin MS, Livingston DM, Pavletich NP. </i> Genes Dev, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"ashenoy","curator_name":"Aditi Shenoy","curator_orcid":"0000-0001-7748-2501","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1KZY"}],"region_id":"DP02954r003","statement":[{"text":"An N-terminal fragment (residues 1702–1713) and the region between β1A and α1A (residues 1741–1769) do not have interpretable electron density, and we presume are disordered. Residues 1741–1769 correspond to a 29 amino acid insertion that is not found in other BRCT repeats and is rich in polar and charged residues.","type":"Methods"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-28T13:53:35.963Z"}},{"start":1,"end":1483,"reference_id":"28188027","reference_source":"pmid","reference_html":"A New Mode of Mitotic Surveillance. <i> Lambrus BG, Holland AJ. </i> Trends Cell Biol, 2017","date":"2022-12-28T14:57:17.874Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP02954r004","statement":[{"text":"(B) Diagram of the domain structure of 53BP1. The N-terminal region of 53BP1 is a disordered region containing multiple ATM phosphorylation sites while the C-terminal half contains the following domains: dynein light chain 8 (LC8) binding, oligomerization, glycine–arginine rich (GAR), tandem Tudor (recognizes methylated residues), ubiquitination-dependent recruitment (UDR), nuclear localization signal (NLS), and tandem BRCT.","type":"Figure"},{"text":"The unstructured N-terminal half of 53BP1 contains 28 S/TQ sites that are phosphorylated by ATM following DNA damage and are required for its recruitment of NHEJ-promoting factors.","type":"Article"},{"text":"Following the unstructured region the first structured region is the tudor-like domain, which spans the 1484-1603 region according to UniProt.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-06T16:35:59.767Z"}},{"start":1140,"end":1225,"reference_id":"36335430","reference_source":"pmid","reference_html":"Multivalent binding of the hub protein LC8 at a newly discovered site in 53BP1. <i> Howe J, Weeks A, Reardon P, Barbar E. </i> Biophys J, 2022","date":"2024-05-03T08:32:27.081Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":null}],"region_id":"DP02954r005","sequence_construct":"SKALIERPSQNNIGIQTMECSLRVPETVSAATQTIKNVCEQGTSTVDQNFGKQDATVQTERGSGEKPVSAPGDDTESLHSQGEEEF","statement":[{"text":"Far-UV circular dichroism shows a spectrum with a strong negative ellipticity at 200 nm, which is consistent with a primarily disordered structure (Fig. 2 A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:56:20.610Z"}},{"start":1140,"end":1225,"reference_id":"36335430","reference_source":"pmid","reference_html":"Multivalent binding of the hub protein LC8 at a newly discovered site in 53BP1. <i> Howe J, Weeks A, Reardon P, Barbar E. </i> Biophys J, 2022","date":"2024-05-03T08:33:47.665Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":null}],"region_id":"DP02954r006","sequence_construct":"SKALIERPSQNNIGIQTMECSLRVPETVSAATQTIKNVCEQGTSTVDQNFGKQDATVQTERGSGEKPVSAPGDDTESLHSQGEEEF","statement":[{"text":"The lack of contiguous regions with deviation from Cα-Cβ shifts from expected values indicates that the 53BP1 LBD is dynamic and disordered, consistent with the prediction. 15N relaxation experiments confirm that the 53BP1 LBD is disordered with little evidence of restricted motion across the chain (Fig. 2 C). ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:56:17.819Z"}},{"start":1150,"end":1157,"reference_id":"36335430","reference_source":"pmid","reference_html":"Multivalent binding of the hub protein LC8 at a newly discovered site in 53BP1. <i> Howe J, Weeks A, Reardon P, Barbar E. </i> Biophys J, 2022","date":"2024-05-03T08:37:57.925Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q96FJ2","operator":null,"partner_start":1,"partner_end":89}],"region_id":"DP02954r007","statement":[{"text":"The presence of three LC8 binding sites in 53BP1 is supported by the loss of resonances for residues between 1144 and 1211.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:56:38.998Z"}},{"start":1167,"end":1174,"reference_id":"36335430","reference_source":"pmid","reference_html":"Multivalent binding of the hub protein LC8 at a newly discovered site in 53BP1. <i> Howe J, Weeks A, Reardon P, Barbar E. </i> Biophys J, 2022","date":"2024-05-03T08:38:29.520Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q96FJ2","operator":null,"partner_start":1,"partner_end":89}],"region_id":"DP02954r008","statement":[{"text":"The presence of three LC8 binding sites in 53BP1 is supported by the loss of resonances for residues between 1144 and 1211.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:56:37.009Z"}},{"start":1192,"end":1199,"reference_id":"36335430","reference_source":"pmid","reference_html":"Multivalent binding of the hub protein LC8 at a newly discovered site in 53BP1. <i> Howe J, Weeks A, Reardon P, Barbar E. </i> Biophys J, 2022","date":"2024-05-03T08:38:41.863Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q96FJ2","operator":null,"partner_start":1,"partner_end":89}],"region_id":"DP02954r009","statement":[{"text":"The presence of three LC8 binding sites in 53BP1 is supported by the loss of resonances for residues between 1144 and 1211.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:56:35.487Z"}}],"released":"2020_12","length":1972,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP02954","date":"2020-10-28T16:45:03.957Z","regions_counter":9,"dataset":["Condensates-related proteins"],"UniParc":"UPI000016A0A6","uniref100":"UniRef100_Q12888","uniref90":"UniRef90_Q12888","uniref50":"UniRef50_Q12888","genes":[{"name":{"value":"TP53BP1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11999","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11999"}}]}}],"alphafold_very_low_content":0.7936105476673428,"disorder_content":0.7662271805273834,"disprot_consensus":{"full":[{"start":1,"end":1483,"type":"D"},{"start":1741,"end":1768,"type":"D"}],"Structural state":[{"start":1,"end":1483,"type":"D"},{"start":1741,"end":1768,"type":"D"}],"Molecular function":[{"start":1150,"end":1157,"type":"F"},{"start":1167,"end":1174,"type":"F"},{"start":1192,"end":1199,"type":"F"}]}},{"acc":"O70200","features":{"pfam":[{"id":"PF21008","name":"Allograft inflammatory factor 1","start":8,"end":147}],"gene3D":[]},"creator":"msalas","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MSQSRDLQGGKAFGLLKAQQEERLEGINKQFLDDPKYSNDEDLPSKLEAFKVKYMEFDLNGNGDIDIMSLKRMLEKLGVPKTHLELKRLIREVSSGSEETFSYSDFLRMMLGKRSAILRMILMYEEKNKEHKRPTGPPAKKAISELP","name":"Allograft inflammatory factor 1","regions":[{"region_id":"DP02956r001","validated":{"curator_id":"fquaglia","timestamp":"2020-11-25T16:19:04.034Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":16,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"The residues invisible in electron density are indicated by gray shading","type":"Figure"},{"text":"The residues Met1 to Leu16 and Tyr124 to Pro147 in HIba1, and Met1 to Leu16 and Asn128 to Pro147 inMIba1 were invisible in the final electron density map, as indicated by gray in Figure1","type":"Results"},{"text":"The mass spectrum of purified samples showed that there are truncated proteins with molecular masses of 13,234 Da for H-Iba1 (VM=1.82 Å3/Da) and 14,486 Da for M-Iba1 (VM=1.92 Å3/Da), respectively, suggesting that from eight to 13 amino acid residues are possibly disorderd in crystals ","type":"Results"},{"text":"Both of the highly mobile N-terminal and C-terminal regions protrude from the upper surface, as labeled in Figure 6 (middle)","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-6352-1282","released":"2022_03","term_ontology":"IDPO","curator_name":"Martin Salas","reference_id":"17011575","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1WY9"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"msalas","reference_html":"X-ray structures of the microglia/macrophage-specific protein Iba1 from human and mouse demonstrate novel molecular conformation change induced by calcium binding. <i> Yamada M, Ohsawa K, Imai Y, Kohsaka S, Kamitori S. </i> J Mol Biol, 2006","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02956r002","validated":{"curator_id":"fquaglia","timestamp":"2020-11-25T16:19:04.964Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":147,"term_id":"IDPO:0000002","start":124,"version":2,"statement":[{"text":"The residues invisible in electron density are indicated by gray shading","type":"Figure"},{"text":"The residues Met1 to Leu16 and Tyr124 to Pro147 in HIba1, and Met1 to Leu16 and Asn128 to Pro147 inMIba1 were invisible in the final electron density map, as indicated by gray in Figure1","type":"Results"},{"text":"The mass spectrum of purified samples showed that there are truncated proteins with molecular masses of 13,234 Da for H-Iba1 (VM=1.82 Å3/Da) and 14,486 Da for M-Iba1 (VM=1.92 Å3/Da), respectively, suggesting that from eight to 13 amino acid residues are possibly disorderd in crystals","type":"Results"},{"text":"Both of the highly mobile N-terminal and C-terminal regions protrude from the upper surface, as labeled in Figure 6 (middle)","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-6352-1282","released":"2022_03","term_ontology":"IDPO","curator_name":"Martin Salas","reference_id":"17011575","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1WY9"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"msalas","reference_html":"X-ray structures of the microglia/macrophage-specific protein Iba1 from human and mouse demonstrate novel molecular conformation change induced by calcium binding. <i> Yamada M, Ohsawa K, Imai Y, Kohsaka S, Kamitori S. </i> J Mol Biol, 2006","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":147,"ncbi_taxon_id":10090,"organism":"Mus musculus","disprot_id":"DP02956","date":"2020-11-05T18:03:56.778Z","regions_counter":2,"dataset":[],"UniParc":"UPI0000022332","uniref100":"UniRef100_O70200","uniref90":"UniRef90_O70200","uniref50":"UniRef50_O70200","genes":[{"name":{"value":"Aif1"},"synonyms":[{"value":"Iba1"}]}],"alphafold_very_low_content":0.047619047619047616,"disorder_content":0.272108843537415,"disprot_consensus":{"full":[{"start":1,"end":16,"type":"D"},{"start":124,"end":147,"type":"D"}],"Structural state":[{"start":1,"end":16,"type":"D"},{"start":124,"end":147,"type":"D"}]}},{"acc":"P47992","features":{"pfam":[{"id":"PF00048","name":"Small cytokines (intecrine/chemokine), interleukin-8 like","start":32,"end":82}],"gene3D":[]},"creator":"msalas","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MRLLILALLGICSLTAYIVEGVGSEVSDKRTCVSLTTQRLPVSRIKTYTITEGSLRAVIFITKRGLKVCADPQATWVRDVVRSMDRKSNTRNNMIQTKPTGTQQSTNTAVTLTG","name":"Lymphotactin","regions":[{"region_id":"DP02957r001","validated":{"curator_id":"fquaglia","timestamp":"2020-11-25T16:19:21.767Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":114,"term_id":"IDPO:0000002","start":90,"version":2,"statement":[{"text":"Two regions are dynamically disordered as evidenced by 1H and 13C chemical shifts and {15N}-1H NOEs: residues 1–9 of the amino terminus and residues 69-93 of the C-terminal extension.","type":"Abstract"},{"text":"A steady decline is seen in the heteronuclear NOE values for the unstructured residues approaching the ends of the N- and C-termini with negative NOE values observed for residues near each terminus; these values are consistent with large-amplitude motions on the picosecond to nanosecond time scale and a complete lack of stable secondary or tertiary structure.","type":"Results"},{"text":"No long-range NOEs were observed for the 9 N-terminal and 26 C-terminal residues.","type":"Results"},{"text":"Residues 1–8 and 69–93 are highly disordered.","type":"Results"},{"text":"Residues comprising the unique C-terminal sequence of hLtn are entirely disordered in solution (Figures 4 and 5), but residues 9–68 adopt the conserved fold observed for all other chemokines (Figure 6).","type":"Discussion"},{"text":"The IDR characterized in the publication and spanning residues 69-93 corresponds to region 90-114 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-21) that is cleaved in the mature secreted protein.","type":"Curator statement"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0001-6352-1282","released":"2022_03","term_ontology":"IDPO","curator_name":"Martin Salas","reference_id":"11601972","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1J8I"},{"db":"PDB","id":"1J9O"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"msalas","reference_html":"Monomeric solution structure of the prototypical 'C' chemokine lymphotactin. <i> Kuloglu ES, McCaslin DR, Kitabwalla M, Pauza CD, Markley JL, Volkman BF. </i> Biochemistry, 2001","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02957r002","validated":{"curator_id":"fquaglia","timestamp":"2020-11-25T16:19:21.050Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":114,"term_id":"IDPO:0000002","start":90,"version":2,"statement":[{"text":"The IDR characterized in the publication and spanning residues 69-93 corresponds to region 90-114 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-21) that is cleaved in the mature secreted protein.","type":"Curator statement"},{"text":"The C-terminal α-helix observed at 10 °C and 200 mM NaCl, which is conserved in other chemokines, is absent at 45 °C and no salt, and the last 38 residues of the protein are completely disordered, as indicated by heteronuclear 15N-1H NOEs. ","type":"Abstract"},{"text":"Under these conditions, hLtn adopted the conserved chemokine fold consisting of three antiparallel β-strands and a C-terminal α-helix with unstructured N- (1–9) and C-terminal (69–93) residues.","type":"Results"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0001-6352-1282","released":"2022_03","term_ontology":"IDPO","curator_name":"Martin Salas","reference_id":"11889129","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"5251"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"msalas","reference_html":"Structural rearrangement of human lymphotactin, a C chemokine, under physiological solution conditions. <i> Kuloğlu ES, McCaslin DR, Markley JL, Volkman BF. </i> J Biol Chem, 2002","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02957r003","validated":{"curator_id":"fquaglia","timestamp":"2020-11-25T16:19:20.387Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":114,"term_id":"IDPO:0000002","start":97,"version":2,"statement":[{"text":"The IDR characterized in the publication and spanning residues 76-93 corresponds to region 97-114  of the amino acid sequence, since the the Ltn expression construct described in the paper lacks the N-terminal Val-1 residue and the resulting protein therefore corresponds to Ltn (2–93). In addition the natural precursor form of the protein contains a signal peptide (1-21) that is cleaved in the mature secreted protein.","type":"Curator statement"},{"text":"Completely disordered residues 76–93 were not included in water refinement calculations, thus the ensemble of CC3 NMR structures deposited in the PDB contains only residues 1–75.","type":"Methods"},{"text":"Backbone r.m.s.d. (Figure 3B) and 15N-1H heteronuclear NOE (Figure 3C) values confirm that residues 1–10 and 69–93 are dynamically disordered in solution, as observed with the Ltn10 structure (4). ","type":"Results"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0001-6352-1282","released":"2022_03","term_ontology":"IDPO","curator_name":"Martin Salas","reference_id":"17302442","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2HDM"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"msalas","reference_html":"An engineered second disulfide bond restricts lymphotactin/XCL1 to a chemokine-like conformation with XCR1 agonist activity. <i> Tuinstra RL, Peterson FC, Elgin ES, Pelzek AJ, Volkman BF. </i> Biochemistry, 2007","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02957r004","validated":{"curator_id":"fquaglia","timestamp":"2020-11-25T16:19:19.565Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":114,"term_id":"IDPO:0000002","start":82,"version":2,"statement":[{"text":"The IDR characterized in the publication and spanning residues 61-93 corresponds to region 82-114 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-21) that is cleaved in the mature secreted protein.","type":"Curator statement"},{"text":"Disordered N- and C-terminal residues (residues 1–7 and 53–93) are not shown.","type":"Figure"},{"text":"Completely disordered residues 61–93 were not included in water refinement calculations, thus the ensemble of Ltn40 NMR structures deposited in the Protein Data Bank contains only residues 1–60. NMR structure refinement statistics are provided in Table S1.","type":"Methods"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0001-6352-1282","released":"2022_03","term_ontology":"IDPO","curator_name":"Martin Salas","reference_id":"18364395","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2JP1"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"msalas","reference_html":"Interconversion between two unrelated protein folds in the lymphotactin native state. <i> Tuinstra RL, Peterson FC, Kutlesa S, Elgin ES, Kron MA, Volkman BF. </i> Proc Natl Acad Sci U S A, 2008","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":114,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP02957","date":"2020-11-10T17:59:24.267Z","regions_counter":4,"dataset":[],"UniParc":"UPI000013633F","uniref100":"UniRef100_P47992","uniref90":"UniRef90_P47992","uniref50":"UniRef50_P47992","genes":[{"name":{"value":"XCL1"},"synonyms":[{"value":"LTN"},{"value":"SCYC1"}]}],"alphafold_very_low_content":0.02631578947368421,"disorder_content":0.2894736842105263,"disprot_consensus":{"full":[{"start":82,"end":114,"type":"D"}],"Structural state":[{"start":82,"end":114,"type":"D"}]}},{"acc":"Q55DL0","features":{"pfam":[{"id":"PF01979","name":"Amidohydrolase family","start":58,"end":446}],"gene3D":[]},"creator":"ashenoy","taxonomy":["Eukaryota","Amoebozoa","Evosea","Eumycetozoa","Dictyostelia","Dictyosteliales","Dictyosteliaceae","Dictyostelium"],"sequence":"MLRVDQTGTILIKNGTVVNDDRYFKSDVLVENGIIKEISKNIEPKEGIKVVDATDKLLLPGGIDTHTHFQLPFMGTVSVDDFDIGTQAAVAGGTTFIIDFVIPTRGQSLLEAYDQWKKWADEKVNCDYSLHVAITWWSEQVSREMEILVKERGVNSFKCFMAYKNSFMVTDQEMYHIFKRCKELGAIAQVHAENGDMVFEGQKKMLEMGITGPEGHELSRPEALEAEATNRAIVIADSVCTPVYIVHVQSIGAADVICKHRKEGVRVYGEPIAAGLGVDGSHMWNHDWRHAAAFVMGPPIRPDPRTKGVLMDYLARGDLDCVGTDNCTFCADQKAMGKDDFTKIPNGVNGVEDRMSIVWENGVNTGKLTWCQFVRATSSEAARIFNIYPRKGRIDVGCDGDIVIWDPNQSKTISKDTHHHAVDFNIFEGIKVTGIAVTTIVAGNIVWSDNKLSCVKGSGRFVPRPPFGPVFDGIEQRDKVRNELLRKVDRKPYEDDNTKNSSK","name":"Dihydropyrimidinase","regions":[{"region_id":"DP02958r001","validated":{"curator_id":"bmesza","timestamp":"2020-11-30T10:47:42.446Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":503,"term_id":"IDPO:0000002","start":491,"version":2,"statement":[{"text":"Only residues 7–490 could be traced; 5 amino acids at the N terminus, the 13C-terminal residues, and the polyhistidine tag are not visible in the electron density map because of structural flexibility.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-7748-2501","released":"2022_03","term_ontology":"IDPO","curator_name":"Aditi Shenoy","reference_id":"16517602","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2FTW"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"ashenoy","reference_html":"The crystal structures of dihydropyrimidinases reaffirm the close relationship between cyclic amidohydrolases and explain their substrate specificity. <i> Lohkamp B, Andersen B, Piškur J, Dobritzsch D. </i> J Biol Chem, 2006","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":503,"ncbi_taxon_id":44689,"organism":"Dictyostelium discoideum","disprot_id":"DP02958","date":"2020-11-11T10:50:26.880Z","regions_counter":1,"dataset":[],"UniParc":"UPI00004E4BBE","uniref100":"UniRef100_Q55DL0","uniref90":"UniRef90_Q55DL0","uniref50":"UniRef50_Q55DL0","genes":[{"name":{"value":"pyd2"},"orfNames":[{"value":"DDB_G0269246"}]}],"alphafold_very_low_content":0.007952286282306162,"disorder_content":0.02584493041749503,"disprot_consensus":{"full":[{"start":491,"end":503,"type":"D"}],"Structural state":[{"start":491,"end":503,"type":"D"}]}},{"acc":"P42527","features":{"pfam":[{"id":"PF00400","name":"WD domain, G-beta repeat","start":860,"end":897},{"id":"PF00400","name":"WD domain, G-beta repeat","start":902,"end":936},{"id":"PF00400","name":"WD domain, G-beta repeat","start":945,"end":980},{"id":"PF00400","name":"WD domain, G-beta repeat","start":993,"end":1021},{"id":"PF00400","name":"WD domain, G-beta repeat","start":1028,"end":1061},{"id":"PF00400","name":"WD domain, G-beta repeat","start":1066,"end":1101},{"id":"PF00400","name":"WD domain, G-beta repeat","start":1106,"end":1141},{"id":"PF02816","name":"Alpha-kinase family","start":634,"end":800}],"gene3D":[]},"creator":"ashenoy","taxonomy":["Eukaryota","Amoebozoa","Evosea","Eumycetozoa","Dictyostelia","Dictyosteliales","Dictyosteliaceae","Dictyostelium"],"sequence":"MFNIKKRKESITGIPPINVNSPQSVPLSGTLQSPLITPNSPNFVSRQCPFKKFGCSSFLVSKAEFDNHLKDDAQFHLQLAVEKFDHQFDLHTQLMAHFTEQMEDQLEKTMKVVRNHTDSLGGNVQTKLDEGIEKCMAFAKKVEQQQQQLAKRLITQQIQEKKSTSSPLVKGGISGGGGSGGDDSFDGANISSMSTSKQELQQELQSLSIKMKKELTELSDELSQKLERSTGNIDIKIKRIEGEVNEKIDKRQLVSTIDDSIGKKTDSIGYTLESSIIKKVEEKEKKKSEQNQLLFDSKIESLKDKIKIIETQQLDTSSEVRKLKLESTSSGNLMAGLNGTSGRPSSSSHFIPSSVSAAANNINKNEIMEEVKKVEEKLQKKIREEIDNTKSELSKVERSVKDNRSEIEGLEKDCKNQFDKQDNKIKQVEDDLKKSDSLLLLMQNNLKKYNEFVDRERDRESERLKLQDSIKRLEQNQKKIEAEIQEGNEQVERVLREEASISPISSVPKSPITTKRSSIILNSPPMTSQQSSPKIQDLLSSSGSSSVSGINISSETGEMGILWEFDPIINKWIRLSMKLKVERKPFAEGALREAYHTVSLGVGTDENYPLGTTTKLFPPIEMISPISKNNEAMTQLKNGTKFVLKLYKKEAEQQASRELYFEDVKMQMVCRDWGNKFNQKKPPKKIEFLMSWVVELIDRSPSSNGQPILCSIEPLLVGEFKKNNSNYGAVLTNRSTPQAFSHFTYELSNKQMIVVDIQGVDDLYTDPQIHTPDGKGFGLGNLGKAGINKFITTHKCNAVCALLDLDVKLGGVLSGNNKKQLQQGTMVMPDILPELMPSDNTIKVGAKQLPKAEFSKKDLKCVSTIQSFRERVNSIAFFDNQKLLCAGYGDGTYRVFDVNDNWKCLYTVNGHRKSIESIACNSNYIFTSSPDNTIKVHIIRSGNTKCIETLVGHTGEVNCVVANEKYLFSCSYDKTIKVWDLSTFKEIKSFEGVHTKYIKTLALSGRYLFSGGNDQIIYVWDTETLSMLFNMQGHEDWVLSLHCTASYLFSTSKDNVIKIWDLSNFSCIDTLKGHWNSVSSCVVKDRYLYSGSEDNSIKVWDLDTLECVYTIPKSHSLGVKCLMVFNNQIISAAFDGSIKVWEWQSK","name":"Myosin heavy chain kinase A","regions":[{"region_id":"DP02959r001","unpublished":true,"validated":{"curator_id":"bmesza","timestamp":"2020-11-30T11:37:22.577Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":841,"term_id":"IDPO:0000002","start":810,"version":2,"statement":[{"text":"An intramolecular ligand for the Pi-pocket can be generated by the auto-phosphorylation of a conserved threonine residue (Thr825 in MHCK-A; Thr348 in eEF2K) in the unstructured linker C-terminal to the α -kinase domain.","type":"Article"},{"text":"Region 810-841 is a flexible linker connecting the α-kinase domain and the WD repeat domain.","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-7748-2501","released":"2023_12","term_ontology":"IDPO","curator_name":"Aditi Shenoy","reference_id":"27211275","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5E4H"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"ashenoy","reference_html":"Structure of the Dictyostelium Myosin-II Heavy Chain Kinase A (MHCK-A) α-kinase domain apoenzyme reveals a novel autoinhibited conformation. <i> Ye Q, Yang Y, van Staalduinen L, Crawley SW, Liu L, Brennan S, Côté GP, Jia Z. </i> Sci Rep, 2016","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":841,"term_name":"flexible linker","reference_html":"Structure of the Dictyostelium Myosin-II Heavy Chain Kinase A (MHCK-A) α-kinase domain apoenzyme reveals a novel autoinhibited conformation. <i> Ye Q, Yang Y, van Staalduinen L, Crawley SW, Liu L, Brennan S, Côté GP, Jia Z. </i> Sci Rep, 2016","start":810,"region_id":"DP02959r002","term_id":"IDPO:0000033","unpublished":true,"version":3,"curator_id":"ashenoy","released":"2023_12","term_ontology":"IDPO","curator_name":"Aditi Shenoy","ec_name":"x-ray crystallography evidence used in manual assertion","statement":[{"text":"An intramolecular ligand for the Pi-pocket can be generated by the auto-phosphorylation of a conserved threonine residue (Thr825 in MHCK-A; Thr348 in eEF2K) in the unstructured linker C-terminal to the α -kinase domain.","type":"Article"},{"text":"Region 810-841 is a flexible linker connecting the α-kinase domain and the WD repeat domain.","type":"Curator statement"}],"curator_orcid":"0000-0001-7748-2501","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","reference_id":"27211275","validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-07T18:37:15.941Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":841,"term_name":"phosphorylation display site","reference_html":"Autophosphorylation activates Dictyostelium myosin II heavy chain kinase A by providing a ligand for an allosteric binding site in the alpha-kinase domain. <i> Crawley SW, Gharaei MS, Ye Q, Yang Y, Raveh B, London N, Schueler-Furman O, Jia Z, Côté GP. </i> J Biol Chem, 2011","start":806,"region_id":"DP02959r003","term_id":"IDPO:0000045","unpublished":true,"version":2,"curator_id":"ashenoy","released":"2023_12","term_ontology":"IDPO","curator_name":"Aditi Shenoy","ec_name":"x-ray crystallography evidence used in manual assertion","statement":[{"text":"The key residue in the C-tail was identified as Thr825, which was found to be constitutively autophosphorylated.","type":"Abstract"},{"text":"The residue in the C-tail which regulates autophosphorylation is found within the disorder region","type":"Curator statement"}],"curator_orcid":"0000-0001-7748-2501","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","reference_id":"21071445","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T10:29:25.483Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":830,"term_name":"molecular function regulator","reference_html":"Structure of the Dictyostelium Myosin-II Heavy Chain Kinase A (MHCK-A) α-kinase domain apoenzyme reveals a novel autoinhibited conformation. <i> Ye Q, Yang Y, van Staalduinen L, Crawley SW, Liu L, Brennan S, Côté GP, Jia Z. </i> Sci Rep, 2016","start":822,"region_id":"DP02959r004","term_id":"GO:0098772","unpublished":true,"version":3,"curator_id":"ashenoy","released":"2023_12","term_ontology":"GO","curator_name":"Aditi Shenoy","ec_name":"enzymatic activity assay evidence used in manual assertion","statement":[{"text":"Similar to results reported previously, the QQG(p)TMVMPD peptide restored ~60% of kinase activity with a Kd of 38 ± 12 μM29. The QQG(p)TMSMPD peptide was less effective, yielding a Kd of 98 ± 20 μM and a maximal kinase activity of ~50%. The results are consistent with the conclusion that a hydrophobic residue at the +2 position following the phosphothreonine enhances binding to the Pi-pocket.","type":"Results"}],"curator_orcid":"0000-0001-7748-2501","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005801","reference_id":"27211275","validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-07T18:36:27.337Z"},"ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":827,"term_name":"phosphorylation display site","reference_html":"Autophosphorylation activates Dictyostelium myosin II heavy chain kinase A by providing a ligand for an allosteric binding site in the alpha-kinase domain. <i> Crawley SW, Gharaei MS, Ye Q, Yang Y, Raveh B, London N, Schueler-Furman O, Jia Z, Côté GP. </i> J Biol Chem, 2011","start":823,"region_id":"DP02959r005","term_id":"IDPO:0000045","unpublished":true,"version":2,"curator_id":"ashenoy","released":"2023_12","term_ontology":"IDPO","curator_name":"Aditi Shenoy","ec_name":"enzymatic activity assay evidence used in manual assertion","statement":[{"text":"Incubation of A-CAT-5xA with [γ-32P]ATP resulted in the incorporation of less than 0.1 mol of phosphate/mol (Fig. 3A). The amount of phosphate incorporated into A-CAT-5xA increased to 0.2 mol/mol after a 1-h treatment with calf intestinal alkaline phosphatase and to 0.33 mol/mol after a 5-h treatment with SAP (Fig. 3A). We interpret these results to indicate that Thr825 is nearly fully phosphorylated in bacterially expressed A-CAT-5xA and that it is only partially dephosphorylated even after extensive phosphatase treatment.","type":"Results"}],"curator_orcid":"0000-0001-7748-2501","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005801","reference_id":"21071445","validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-07T18:38:35.394Z"},"ec_go":"IDA","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":831,"term_name":"self-activation","reference_html":"Autophosphorylation activates Dictyostelium myosin II heavy chain kinase A by providing a ligand for an allosteric binding site in the alpha-kinase domain. <i> Crawley SW, Gharaei MS, Ye Q, Yang Y, Raveh B, London N, Schueler-Furman O, Jia Z, Côté GP. </i> J Biol Chem, 2011","start":823,"region_id":"DP02959r006","term_id":"IDPO:0000058","unpublished":true,"version":3,"curator_id":"ashenoy","released":"2023_12","term_ontology":"IDPO","curator_name":"Aditi Shenoy","ec_name":"enzymatic activity assay evidence used in manual assertion","statement":[{"text":"In contrast, mutation of Thr825 to alanine decreased kinase and ATPase activities by 95% (Fig. 2B). This result suggests that autophosphorylation of Thr825 is critical for the activity of A-CAT.","type":"Results"}],"curator_orcid":"0000-0001-7748-2501","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005801","reference_id":"21071445","validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-07T18:39:08.932Z"},"ec_go":"IDA","disprot_namespace":"Disorder function"}],"released":"2023_12","length":1146,"ncbi_taxon_id":44689,"organism":"Dictyostelium discoideum","disprot_id":"DP02959","date":"2020-11-11T11:09:33.423Z","regions_counter":7,"dataset":[],"UniParc":"UPI000012DEFB","uniref100":"UniRef100_P42527","uniref90":"UniRef90_P42527","uniref50":"UniRef50_P42527","genes":[{"name":{"value":"mhkA"},"synonyms":[{"value":"mhckA"}],"orfNames":[{"value":"DDB_G0291231"}]}],"alphafold_very_low_content":0.29930191972076786,"disorder_content":0.027923211169284468,"disprot_consensus":{"full":[{"start":806,"end":809,"type":"F"},{"start":810,"end":841,"type":"D"}],"Structural state":[{"start":810,"end":841,"type":"D"}],"Disorder function":[{"start":806,"end":841,"type":"F"}],"Molecular function":[{"start":822,"end":830,"type":"F"}]}},{"acc":"P00880","features":{"pfam":[{"id":"PF00016","name":"Ribulose bisphosphate carboxylase large chain, catalytic domain","start":151,"end":459},{"id":"PF02788","name":"Ribulose bisphosphate carboxylase large chain, N-terminal domain","start":21,"end":140}],"gene3D":[]},"creator":"jssuarez","taxonomy":["Bacteria","Cyanobacteria","Synechococcales","Synechococcaceae","Synechococcus"],"sequence":"MPKTQSAAGYKAGVKDYKLTYYTPDYTPKDTDLLAAFRFSPQPGVPADEAGAAIAAESSTGTWTTVWTDLLTDMDRYKGKCYHIEPVQGEENSYFAFIAYPLDLFEEGSVTNILTSIVGNVFGFKAIRSLRLEDIRFPVALVKTFQGPPHGIQVERDLLNKYGRPMLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENINSQPFQRWRDRFLFVADAIHKSQAETGEIKGHYLNVTAPTCEEMMKRAEFAKELGMPIIMHDFLTAGFTANTTLAKWCRDNGVLLHIHRAMHAVIDRQRNHGIHFRVLAKCLRLSGGDHLHSGTVVGKLEGDKASTLGFVDLMREDHIEADRSRGVFFTQDWASMPGVLPVASGGIHVWHMPALVEIFGDDSVLQFGGGTLGHPWGNAPGATANRVALEACVQARNEGRDLYREGGDILREAGKWSPELAAALDLWKEIKFEFETMDKL","name":"Ribulose bisphosphate carboxylase large chain","regions":[{"region_id":"DP02960r001","validated":{"curator_id":"bmesza","timestamp":"2020-12-03T17:58:58.123Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":472,"term_id":"IDPO:0000002","start":410,"version":2,"statement":[{"text":"Fitting of the RbcL8 core from the crystal structure showed that density accommodating the ∼60 C-terminal residues (residues 413–475) of the RbcL subunits was missing in the cryo-EM density map (Fig. 3c, d), indicating that this segment is disordered.","type":"Results"},{"text":"Residues 413 and 475 correspond to residues 410 and 472 (respectively) in the Uniprot and PDB associated sequences.","type":"Curator statement"}],"term_name":"disorder","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"20075914","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006224","curator_id":"jssuarez","reference_html":"Coupled chaperone action in folding and assembly of hexadecameric Rubisco. <i> Liu C, Young AL, Starling-Windhof A, Bracher A, Saschenbrecker S, Rao BV, Rao KV, Berninghausen O, Mielke T, Hartl FU, Beckmann R, Hayer-Hartl M. </i> Nature, 2010","ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP02960r002","validated":{"curator_id":"bmesza","timestamp":"2020-12-01T11:35:38.933Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":472,"term_id":"IDPO:0000011","start":410,"version":2,"statement":[{"text":"On RbcX2 binding, the previously ‘free’ C-terminal segment of RbcL seems to be pulled back towards the main body of the subunit and becomes tethered via the interaction of the ultimate C terminus with the central crevice of RbcX2. This RbcX2-mediated ordering of the RbcL C termini may also provide a platform for RbcS docking. ","type":"Results"},{"text":"Residues 413 and 475 correspond to residues 410 and 472 respectively.","type":"Curator statement"}],"term_name":"disorder to order","ec_name":"cryogenic electron microscopy evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"20075914","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2WVW"}],"term_namespace":"Structural transition","ec_id":"ECO:0006208","curator_id":"jssuarez","reference_html":"Coupled chaperone action in folding and assembly of hexadecameric Rubisco. <i> Liu C, Young AL, Starling-Windhof A, Bracher A, Saschenbrecker S, Rao BV, Rao KV, Berninghausen O, Mielke T, Hartl FU, Beckmann R, Hayer-Hartl M. </i> Nature, 2010","ec_go":"IDA","disprot_namespace":"Structural transition"},{"region_id":"DP02960r003","validated":{"curator_id":"bmesza","timestamp":"2020-12-01T11:36:04.922Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":472,"term_id":"GO:0005515","start":410,"version":3,"statement":[{"text":"On RbcX2 binding, the previously ‘free’ C-terminal segment of RbcL seems to be pulled back towards the main body of the subunit and becomes tethered via the interaction of the ultimate C terminus with the central crevice of RbcX2.","type":"Results"},{"text":"These interactions with RbcX2 may exert a stabilizing effect on the N-terminal domain, as indicated by the partial protease protection of the N-terminal ∼60 residues of RbcL by RbcX2 (data not shown).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q44212","partner_end":null}],"term_name":"protein binding","ec_name":"cryogenic electron microscopy evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"GO","curator_name":"Jaime Santos Suárez","reference_id":"20075914","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2WVW"}],"term_namespace":"Molecular function","ec_id":"ECO:0006208","curator_id":"jssuarez","reference_html":"Coupled chaperone action in folding and assembly of hexadecameric Rubisco. <i> Liu C, Young AL, Starling-Windhof A, Bracher A, Saschenbrecker S, Rao BV, Rao KV, Berninghausen O, Mielke T, Hartl FU, Beckmann R, Hayer-Hartl M. </i> Nature, 2010","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02960r005","validated":{"curator_id":"bmesza","timestamp":"2020-12-03T17:59:36.276Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":472,"term_id":"GO:0005515","start":410,"version":3,"statement":[{"text":"Raf1 fulfills a role similar to that of the assembly chaperone RbcX, thus suggesting that functionally redundant factors ensure efficient Rubisco biogenesis.","type":"Abstract"},{"text":"The resulting tentative model for the RbcL8–Raf14 complex (Fig. 5g,h) is consistent with a role of Raf1 in stabilizing RbcL2 and allowing its assembly into the RbcL8 core complex.","type":"Results"},{"text":" Thus, it seems plausible that the C-terminal residues of RbcL are also ordered in the complex with Raf1","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9SR19","partner_end":null}],"term_name":"protein binding","ec_name":"cross-linking evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"GO","curator_name":"Jaime Santos Suárez","reference_id":"26237510","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001170","curator_id":"jssuarez","reference_html":"Structure and mechanism of the Rubisco-assembly chaperone Raf1. <i> Hauser T, Bhat JY, Miličić G, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M. </i> Nat Struct Mol Biol, 2015","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02960r006","validated":{"curator_id":"bmesza","timestamp":"2020-12-03T18:02:23.783Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":472,"term_id":"GO:0005515","start":410,"version":3,"statement":[{"text":"To elucidate how Raf1 mediates Rubisco assembly, we obtained a higher-resolution structure of the Syn7942 RbcL-Raf1 supercomplex expressed in Escherichia coli using cryo-EM (SI Appendix, Fig. S2).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9SR19","partner_end":null}],"term_name":"protein binding","ec_name":"cryogenic electron microscopy evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"GO","curator_name":"Jaime Santos Suárez","reference_id":"32636267","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006208","curator_id":"jssuarez","reference_html":"Rubisco accumulation factor 1 (Raf1) plays essential roles in mediating Rubisco assembly and carboxysome biogenesis. <i> Huang F, Kong WW, Sun Y, Chen T, Dykes GF, Jiang YL, Liu LN. </i> Proc Natl Acad Sci U S A, 2020","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02960r007","validated":{"curator_id":"bmesza","timestamp":"2020-12-01T11:36:46.349Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":472,"term_id":"GO:0098772","start":410,"version":3,"statement":[{"text":"\"This movement could in turn destabilize the interaction of the RbcL C terminus with RbcX2, thus triggering RbcX2 release and final maturation of the Rubisco holoenzyme.\"","type":"Results"},{"text":"On RbcX2 binding, the previously ‘free’ C-terminal segment of RbcL seems to be pulled back towards the main body of the subunit and becomes tethered via the interaction of the ultimate C terminus with the central crevice of RbcX2. This RbcX2-mediated ordering of the RbcL C termini may also provide a platform for RbcS docking.","type":"Results"}],"term_name":"molecular function regulator","ec_name":"cryogenic electron microscopy evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"GO","curator_name":"Jaime Santos Suárez","reference_id":"20075914","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2WVW"}],"term_namespace":"Molecular function","ec_id":"ECO:0006208","curator_id":"jssuarez","reference_html":"Coupled chaperone action in folding and assembly of hexadecameric Rubisco. <i> Liu C, Young AL, Starling-Windhof A, Bracher A, Saschenbrecker S, Rao BV, Rao KV, Berninghausen O, Mielke T, Hartl FU, Beckmann R, Hayer-Hartl M. </i> Nature, 2010","ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02960r010","validated":{"curator_id":"bmesza","timestamp":"2020-12-03T18:02:31.616Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":466,"term_id":"GO:0005515","start":461,"version":3,"statement":[{"text":"Binding of Syn6301-RbcX2(FLAG), AnaCA-RbcX2(FLAG) and Syn7002-RbcX2 to an array of dodecapeptides, with a 10 residue overlap, covering the sequence of the last 40 amino-acids of Syn7002-RbcL, Syn6301-RbcL and Ana7120-RbcL (shown on top)","type":"Supplementary material"},{"text":"The consensus motif for RbcX2 binding inferred by this analysis corresponds to residues 461 to 466 (EIKFEF).","type":"Curator statement"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q44212","partner_end":null}],"term_name":"protein binding","ec_name":"physical interaction evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"GO","curator_name":"Jaime Santos Suárez","reference_id":"20075914","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0000353","curator_id":"jssuarez","reference_html":"Coupled chaperone action in folding and assembly of hexadecameric Rubisco. <i> Liu C, Young AL, Starling-Windhof A, Bracher A, Saschenbrecker S, Rao BV, Rao KV, Berninghausen O, Mielke T, Hartl FU, Beckmann R, Hayer-Hartl M. </i> Nature, 2010","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02960r013","validated":{"curator_id":"bmesza","timestamp":"2020-12-03T18:02:37.853Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":470,"term_id":"GO:0005515","start":460,"version":3,"statement":[{"text":"Isothermal titration calorimetry confirmed that Syn6301-RbcX2 bound the C-terminal sequence of RbcL (KEIKFEFETMD) with low affinity (Kd ∼105 µM) (Supplementary Fig. 3a, b).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q44212","partner_end":null}],"term_name":"protein binding","ec_name":"isothermal titration calorimetry evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"GO","curator_name":"Jaime Santos Suárez","reference_id":"20075914","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"jssuarez","reference_html":"Coupled chaperone action in folding and assembly of hexadecameric Rubisco. <i> Liu C, Young AL, Starling-Windhof A, Bracher A, Saschenbrecker S, Rao BV, Rao KV, Berninghausen O, Mielke T, Hartl FU, Beckmann R, Hayer-Hartl M. </i> Nature, 2010","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_12","length":472,"ncbi_taxon_id":269084,"organism":"Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)","disprot_id":"DP02960","date":"2020-11-11T15:49:00.550Z","regions_counter":13,"dataset":[],"UniParc":"UPI0000133360","uniref100":"UniRef100_Q31NB3","uniref90":"UniRef90_Q31NB3","uniref50":"UniRef50_P04717","genes":[{"name":{"value":"cbbL"},"synonyms":[{"value":"rbcA"},{"value":"rbcL"}],"olnNames":[{"value":"syc0130_c"}]}],"alphafold_very_low_content":0.012711864406779662,"disorder_content":0.13347457627118645,"disprot_consensus":{"full":[{"start":410,"end":472,"type":"T"}],"Structural state":[{"start":410,"end":472,"type":"D"}],"Structural transition":[{"start":410,"end":472,"type":"T"}],"Molecular function":[{"start":410,"end":472,"type":"F"}]}},{"acc":"Q9SR19","features":{"pfam":[{"id":"PF18087","name":"Rubisco Assembly chaperone C-terminal domain","start":288,"end":435},{"id":"PF18578","name":"Rubisco accumulation factor 1 alpha helical domain","start":155,"end":264},{"id":"PF18579","name":"Rubisco accumulation factor 1 helix turn helix domain","start":85,"end":142}],"gene3D":[]},"creator":"jssuarez","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"sequence":"MFSLKSLISSPFTQSTTHGLFTNPITRPVNPLPRTVSFTVTASMIPKRSSANMIPKNPPARQQLYQPFRPPSSPIPTQFRSLDSAGKIEILAGRMALWFEYAPLISSLYTDGFTPPTIEELTGISSIEQNRLIVGAQVRDSILQSIHEPELISAFDTGGAELLYEIRLLSTTQRVAAATFIIDRNIDSKGAQDLARAIKDYPNRRGDVGWLDFDYNLPGDCLSFLYYRQSRENKNPSDQRTSMLLQALGVAESEKAKNRLNTELYGDKEAEKEKEKKKKEEEVKAIRIPVVRLKFGEVAEATSVVVLPVCKAEEGEKKILEAPMEIIAGGDFKVVEAEKGWKRWVVLPSWNPVAAIGKGGVAVSFRDDRKVLPWDGKEEPLLVVADRVRNVVEADDGYYLVVAENGLKLEKGSDLKAREVKESLGMVVLVVRPPREDDDDWQTSHQNWD","name":"Rubisco accumulation factor 1.2, chloroplastic","regions":[{"region_id":"DP02961r001","validated":{"curator_id":"bmesza","timestamp":"2020-12-17T10:28:28.229Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":449,"term_id":"IDPO:0000002","start":438,"version":2,"statement":[{"text":"The C-terminal 12 residues were disordered in all\ncrystal lattices.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"26237510","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4WT4"},{"db":"PDB","id":"4WT5"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"jssuarez","reference_html":"Structure and mechanism of the Rubisco-assembly chaperone Raf1. <i> Hauser T, Bhat JY, Miličić G, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M. </i> Nat Struct Mol Biol, 2015","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02961r002","validated":{"curator_id":"bmesza","timestamp":"2020-12-17T10:28:29.202Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":285,"term_id":"IDPO:0000002","start":270,"version":2,"statement":[{"text":"The Dmax of the full-length AtRaf1.2 dimer was ∼208 Å, and the radius of gyration (Rg) was 52 Å; we obtained similar values for Syn7942-Raf1. This suggested that the highly charged, flexible linker allows dynamic movements of the Raf1α domains relative to the β-domain dimer, as supported by an ensemble model of the AtRaf1.2 structure (Supplementary Fig. 3e).","type":"Results"},{"text":"The limits of the disordered region were further verified from the structural data on the domain limits and supported by MS analysis.","type":"Curator statement"}],"term_name":"disorder","ec_name":"small-angle X-ray scattering evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"26237510","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006210","curator_id":"jssuarez","reference_html":"Structure and mechanism of the Rubisco-assembly chaperone Raf1. <i> Hauser T, Bhat JY, Miličić G, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M. </i> Nat Struct Mol Biol, 2015","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":449,"ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","disprot_id":"DP02961","date":"2020-11-11T16:41:18.730Z","regions_counter":2,"dataset":[],"UniParc":"UPI00000A4430","uniref100":"UniRef100_Q9SR19","uniref90":"UniRef90_Q9SR19","uniref50":"UniRef50_Q9SR19","genes":[{"name":{"value":"RAF1.2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"22942379","url":"http://www.ncbi.nlm.nih.gov/pubmed/22942379","alternativeUrl":"https://europepmc.org/abstract/MED/22942379"}}]},"orfNames":[{"value":"F7O18.2","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAF04886.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF04886.1"}}]}],"olnNames":[{"value":"At3g04550","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT3G04550","url":""}}]}]}],"alphafold_very_low_content":0.2026726057906459,"disorder_content":0.062360801781737196,"disprot_consensus":{"full":[{"start":270,"end":285,"type":"D"},{"start":438,"end":449,"type":"D"}],"Structural state":[{"start":270,"end":285,"type":"D"},{"start":438,"end":449,"type":"D"}]}},{"acc":"Q9SN68","features":{"pfam":[{"id":"PF00071","name":"Ras family","start":12,"end":171}],"gene3D":[]},"creator":"jssuarez","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"sequence":"MAAAGNKSINAKLVLLGDVGAGKSSLVLRFVKDQFVEFQESTIGAAFFSQTLAVNDATVKFEIWDTAGQERYHSLAPMYYRGAAAAIIVFDVTNQASFERAKKWVQELQAQGNPNMVMALAGNKSDLLDARKVTAEDAQTYAQENGLFFMETSAKTATNVKEIFYEIARRLPRVQPTENPTGMVLPDRAMDRAVSSSCCA","name":"Ras-related protein RABF2b","regions":[{"region_id":"DP02962r001","validated":{"curator_id":"bmesza","timestamp":"2020-12-01T13:29:15.781Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":44,"term_id":"IDPO:0000002","start":32,"version":2,"statement":[{"text":"Missing electron density in the nucleotide-free state and in the VPS9a mutant (D185N) GDP-bound form.","type":"Curator statement"},{"text":"Switch I of ARA7 (residues 32-44) in ARA7-GDP/VPS9a(D185N) is disordered and indicated as transparent green dots. ","type":"Supplementary material"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"20833725","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2EFD"},{"db":"PDB","id":"2EFH"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"jssuarez","reference_html":"GDP-bound and nucleotide-free intermediates of the guanine nucleotide exchange in the Rab5·Vps9 system. <i> Uejima T, Ihara K, Goh T, Ito E, Sunada M, Ueda T, Nakano A, Wakatsuki S. </i> J Biol Chem, 2010","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02962r002","validated":{"curator_id":"bmesza","timestamp":"2020-12-03T18:25:16.418Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":44,"term_id":"GO:0140313","start":32,"version":3,"statement":[{"text":"Involved in nucleotide binding (GDP) and exchange","type":"Curator statement"}],"term_name":"molecular sequestering activity","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"GO","curator_name":"Jaime Santos Suárez","reference_id":"20833725","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2EFC"},{"db":"PDB","id":"2EFE"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"jssuarez","reference_html":"GDP-bound and nucleotide-free intermediates of the guanine nucleotide exchange in the Rab5·Vps9 system. <i> Uejima T, Ihara K, Goh T, Ito E, Sunada M, Ueda T, Nakano A, Wakatsuki S. </i> J Biol Chem, 2010","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02962r003","validated":{"curator_id":"bmesza","timestamp":"2020-12-03T18:25:36.315Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":44,"term_id":"GO:0036094","start":32,"version":3,"statement":[{"text":"Involved in nucleotide binding (GDP) and exchange","type":"Curator statement"}],"term_name":"small molecule binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"GO","curator_name":"Jaime Santos Suárez","reference_id":"20833725","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2EFC"},{"db":"PDB","id":"2EFE"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"jssuarez","reference_html":"GDP-bound and nucleotide-free intermediates of the guanine nucleotide exchange in the Rab5·Vps9 system. <i> Uejima T, Ihara K, Goh T, Ito E, Sunada M, Ueda T, Nakano A, Wakatsuki S. </i> J Biol Chem, 2010","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02962r004","validated":{"curator_id":"bmesza","timestamp":"2020-12-03T18:25:54.460Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":44,"term_id":"IDPO:0000011","start":32,"version":2,"statement":[{"text":"After GTP coming into the binary complex of Rab/Vps9 domain, the conformational change is occurred in switch I and II of Rab and Rab is re-orientated to the compacted form. ","type":"Supplementary material"}],"term_name":"disorder to order","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"20833725","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2EFC"},{"db":"PDB","id":"2EFE"},{"db":"PDB","id":"2EFH"},{"db":"PDB","id":"2EFD"}],"term_namespace":"Structural transition","ec_id":"ECO:0005670","curator_id":"jssuarez","reference_html":"GDP-bound and nucleotide-free intermediates of the guanine nucleotide exchange in the Rab5·Vps9 system. <i> Uejima T, Ihara K, Goh T, Ito E, Sunada M, Ueda T, Nakano A, Wakatsuki S. </i> J Biol Chem, 2010","ec_go":"EXP","disprot_namespace":"Structural transition"}],"released":"2020_12","length":200,"ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","disprot_id":"DP02962","date":"2020-11-11T17:15:41.824Z","regions_counter":4,"dataset":[],"UniParc":"UPI000009F109","uniref100":"UniRef100_Q9SN68","uniref90":"UniRef90_Q9SN68","uniref50":"UniRef50_Q9SN68","genes":[{"name":{"value":"RABF2B","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12644670","url":"http://www.ncbi.nlm.nih.gov/pubmed/12644670","alternativeUrl":"https://europepmc.org/abstract/MED/12644670"}}]},"synonyms":[{"value":"ARA-7","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11532937","url":"http://www.ncbi.nlm.nih.gov/pubmed/11532937","alternativeUrl":"https://europepmc.org/abstract/MED/11532937"}}]},{"value":"RAB5B","evidences":[{"code":"ECO:0000305","source":{"name":"PubMed","id":"12644670","url":"http://www.ncbi.nlm.nih.gov/pubmed/12644670","alternativeUrl":"https://europepmc.org/abstract/MED/12644670"}}]}],"orfNames":[{"value":"F24J7.190","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"CAA16940.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA16940.1"}}]}],"olnNames":[{"value":"At4g19640","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT4G19640","url":""}}]}]}],"alphafold_very_low_content":0.125,"disorder_content":0.065,"disprot_consensus":{"full":[{"start":32,"end":44,"type":"T"}],"Structural state":[{"start":32,"end":44,"type":"D"}],"Molecular function":[{"start":32,"end":44,"type":"F"}],"Structural transition":[{"start":32,"end":44,"type":"T"}]}},{"acc":"F6IAY2","features":{"pfam":[{"id":"PF02365","name":"No apical meristem (NAM) protein","start":23,"end":148}],"gene3D":[]},"creator":"jssuarez","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","BOP clade","Pooideae","Triticodae","Triticeae","Hordeinae","Hordeum"],"sequence":"MSEVSVINQATEVEDAAAGLDLPPGFRFHPTDEEIISHYLTPKALDHRFCSGVIGEVDLNKCEPWHLPGKAKMGEKEWYFFCHKDRKYPTGTRTNRATMSGYWKATGKDKEIFRGRGILVGMKKTLVFYLGRAPRGEKTGWVMHEFRLEGRLPHPLPRSAKDEWAVSKVFNKELTATNGAMATAMAAAPDAGIERVSSFGFISDHFLDAGELPPLMDPPLGGDVDQVIDFNSNSAYATGGRSGSGLEVKMEQHMPPHMMYSSPYFSLPAANSGDLSPAIRRYCKAEQVSGQTSALSPSRDTGLSTDPNAAGCAEISSAPTPSSHNQDFLDHLDEYPALNLADIWKY","name":"NAC transcription factor","regions":[{"region_id":"DP02965r001","validated":{"curator_id":"bmesza","timestamp":"2020-12-02T13:10:21.522Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":346,"term_id":"IDPO:0000002","start":177,"version":2,"statement":[{"text":"The far-UV CD spectra showed a strong negative absorbance at 200 nm for His6-HvNAC005(173–355), His6-HvNAC013(177–346), and HvNAC013(177–346) with little ellipticity around 220 nm indicating lack of a significant amount of secondary structure and highly characteristic of unstructured proteins (Figs. 6, A and B, and ​77B).","type":"Results"},{"text":"HvNAC013 correspond to Hordeum vulgare NAC transcription factor.","type":"Curator statement"}],"term_name":"disorder","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"21856750","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006204","curator_id":"jssuarez","reference_html":"Senescence-associated barley NAC (NAM, ATAF1,2, CUC) transcription factor interacts with radical-induced cell death 1 through a disordered regulatory domain. <i> Kjaersgaard T, Jensen MK, Christiansen MW, Gregersen P, Kragelund BB, Skriver K. </i> J Biol Chem, 2011","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02965r002","validated":{"curator_id":"bmesza","timestamp":"2020-12-02T13:10:34.777Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":346,"term_id":"IDPO:0000004","start":177,"version":2,"statement":[{"text":"This aspect of HvNAC013(177–346) was analyzed using size exclusion chromatography. The calculated molecular mass of HvNAC013(177–346) is 18.0 kDa, corresponding to a Stokes radius of 20.5 Å for a globular protein. However, HvNAC013(177–346) eluted in a volume corresponding to a molecular mass of 41.5 kDa and a Stokes radius of 28.01 Å (Fig. 6C). This suggested that HvNAC013(177–346) exists in a pre-molten globule-like state (Fig. 6C).","type":"Results"},{"text":"HvNAC013 correspond to Hordeum vulgare NAC transcription factor.","type":"Curator statement"}],"term_name":"pre-molten globule","ec_name":"chromatography evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"21856750","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0007680","curator_id":"jssuarez","reference_html":"Senescence-associated barley NAC (NAM, ATAF1,2, CUC) transcription factor interacts with radical-induced cell death 1 through a disordered regulatory domain. <i> Kjaersgaard T, Jensen MK, Christiansen MW, Gregersen P, Kragelund BB, Skriver K. </i> J Biol Chem, 2011","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02965r003","validated":{"curator_id":"bmesza","timestamp":"2020-12-02T14:05:54.913Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":346,"term_id":"IDPO:0000002","start":177,"version":2,"statement":[{"text":"NMR experiments using 15N-labeled HvNAC013(177–346) were also performed to examine for both the secondary structure and oligomeric state of HvNAC013(177–346). The HSQC spectrum showed a clustering of signals with low dispersion in the proton dimension (Fig. 6D) suggesting that HvNAC013(177–346) is highly unfolded.","type":"Results"},{"text":"HvNAC013 correspond to Hordeum vulgare NAC transcription factor.","type":"Curator statement"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"21856750","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"jssuarez","reference_html":"Senescence-associated barley NAC (NAM, ATAF1,2, CUC) transcription factor interacts with radical-induced cell death 1 through a disordered regulatory domain. <i> Kjaersgaard T, Jensen MK, Christiansen MW, Gregersen P, Kragelund BB, Skriver K. </i> J Biol Chem, 2011","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02965r004","validated":{"curator_id":"bmesza","timestamp":"2020-12-03T18:27:13.339Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":346,"term_id":"GO:0005515","start":177,"version":3,"statement":[{"text":"A directed yeast two-hybrid assay using full-length HvNAC013 and HvRCD1 as bait and prey, respectively, suggested that the proteins interacted (Fig. 8B). Similar results were obtained when HvRCD1 acted as bait and HvNAC013 as prey (Fig. 8C). Analysis of the ability of the isolated domains of HvNAC013 to interact with HvRCD1 showed that the interaction was mediated by the TRD of HvNAC013 (Fig. 8D). ","type":"Results"},{"text":"HvNAC013 correspond to Hordeum vulgare NAC transcription factor.","type":"Curator statement"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"F8KA94","partner_end":null}],"term_name":"protein binding","ec_name":"yeast 2-hybrid evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"GO","curator_name":"Jaime Santos Suárez","reference_id":"21856750","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005805","curator_id":"jssuarez","reference_html":"Senescence-associated barley NAC (NAM, ATAF1,2, CUC) transcription factor interacts with radical-induced cell death 1 through a disordered regulatory domain. <i> Kjaersgaard T, Jensen MK, Christiansen MW, Gregersen P, Kragelund BB, Skriver K. </i> J Biol Chem, 2011","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02965r005","validated":{"curator_id":"bmesza","timestamp":"2020-12-03T18:27:14.123Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":346,"term_id":"GO:0005515","start":177,"version":3,"statement":[{"text":"Recombinant versions of the HvNAC013 TRD and HvRCD1 RST domains, His6-HvNAC013(177–346) and GST-HvRCD1(485–579), were produced and used for in vitro pulldown assays (Fig. 8E). Western blot analysis showed that His6-HvNAC013(177–346) bound to immobilized GST-HvRCD1(485–579), but not to GST.","type":"Results"},{"text":"HvNAC013 correspond to Hordeum vulgare NAC transcription factor.","type":"Curator statement"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"F8KA94","partner_end":null}],"term_name":"protein binding","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"GO","curator_name":"Jaime Santos Suárez","reference_id":"21856750","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006077","curator_id":"jssuarez","reference_html":"Senescence-associated barley NAC (NAM, ATAF1,2, CUC) transcription factor interacts with radical-induced cell death 1 through a disordered regulatory domain. <i> Kjaersgaard T, Jensen MK, Christiansen MW, Gregersen P, Kragelund BB, Skriver K. </i> J Biol Chem, 2011","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02965r006","validated":{"curator_id":"bmesza","timestamp":"2020-12-03T18:27:14.858Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":346,"term_id":"GO:0005515","start":250,"version":3,"statement":[{"text":"In contrast to full-length HvNAC013 and its TRD, HvNAC013(1–250), lacking the 96 C-terminal amino acid residues of HvNAC013, did not interact with HvRCD1. In contrast, mutation of the conserved aspartate (D217A) and leucine (L212A) of the LP motif had no effect on the interaction. In conclusion, the ability of the HvNAC013 TRD to interact with RCD1 resides within the 96 C-terminal amino acid residues of HvNAC013, and no interaction was detected between the LP motif","type":"Results"},{"text":"HvNAC013 correspond to Hordeum vulgare NAC transcription factor.","type":"Curator statement"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"F8KA94","partner_end":null}],"term_name":"protein binding","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"GO","curator_name":"Jaime Santos Suárez","reference_id":"21856750","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0007089","curator_id":"jssuarez","reference_html":"Senescence-associated barley NAC (NAM, ATAF1,2, CUC) transcription factor interacts with radical-induced cell death 1 through a disordered regulatory domain. <i> Kjaersgaard T, Jensen MK, Christiansen MW, Gregersen P, Kragelund BB, Skriver K. </i> J Biol Chem, 2011","ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02965r007","validated":{"curator_id":"bmesza","timestamp":"2020-12-02T13:04:31.912Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":346,"term_id":"GO:0098772","start":250,"version":3,"statement":[{"text":"HvNAC013 interacted with barley radical-induced cell death 1 (RCD1) via the very C-terminal part of its TRD, outside of the region containing the LP motif. ","type":"Abstract"},{"text":"In conclusion, the ability of the HvNAC013 TRD to interact with RCD1 resides within the 96 C-terminal amino acid residues of HvNAC013.","type":"Results"},{"text":"The indispensability of the 96 C-terminal amino acid residues of HvNAC013 for the interaction with HvRCD1 together with the predicted structure for the last 24 residues of HvNAC013 (Fig. 4) may suggest that a MoRF is present in this part of HvNAC013 (6, 7).","type":"Discussion"},{"text":"HvNAC013 correspond to Hordeum vulgare NAC transcription factor.","type":"Curator statement"}],"term_name":"molecular function regulator","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"GO","curator_name":"Jaime Santos Suárez","reference_id":"21856750","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0007089","curator_id":"jssuarez","reference_html":"Senescence-associated barley NAC (NAM, ATAF1,2, CUC) transcription factor interacts with radical-induced cell death 1 through a disordered regulatory domain. <i> Kjaersgaard T, Jensen MK, Christiansen MW, Gregersen P, Kragelund BB, Skriver K. </i> J Biol Chem, 2011","ec_go":"IMP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02965r008","validated":{"curator_id":"bmesza","timestamp":"2020-12-02T13:05:57.634Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":346,"term_id":"GO:0140677","start":177,"version":3,"statement":[{"text":"Coding regions of HvNAC005 and HvNAC013 were fused to yeast GAL4 DBD (Fig. 5A) and analyzed for their ability to activate transcription and promote yeast growth in the absence of histidine and adenine. Murine tumor suppressor p53 (pVA3-1) and SV40 large antigen (pTD1-1) were included as positive controls for transformation and activity dependent selective growth (38). Full-length HvNAC013 was able to activate transcription, and the activation potential resided in the C terminus (residues 177–346), whereas the N-terminal NAC domain (residues 1–176) was unable to activate reporter genes (Fig. 5C).","type":"Results"},{"text":"HvNAC013 correspond to Hordeum vulgare NAC transcription factor.","type":"Curator statement"}],"term_name":"molecular function activator activity","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"GO","curator_name":"Jaime Santos Suárez","reference_id":"21856750","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0007089","curator_id":"jssuarez","reference_html":"Senescence-associated barley NAC (NAM, ATAF1,2, CUC) transcription factor interacts with radical-induced cell death 1 through a disordered regulatory domain. <i> Kjaersgaard T, Jensen MK, Christiansen MW, Gregersen P, Kragelund BB, Skriver K. </i> J Biol Chem, 2011","ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02965r009","validated":{"curator_id":"bmesza","timestamp":"2020-12-03T18:28:10.717Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":346,"term_id":"GO:0098772","start":177,"version":3,"statement":[{"text":"The CD spectrum of interacting HvNAC013(177–346) and His6-HvRCD1(485–579) seemed to be dominated by the HvNAC013 structure (Fig. 9D). A change in absorbance at both 222 and 208 nm was observed for mixed compared with individual proteins suggesting a shift toward a more unfolded state or more extended structure within the complex (Fig. 9D). This is a strong indication that HvNAC013 and HvRCD1 do not interact through a coupled binding and folding mechanism, but rather through a slight reorientation of the conformational ensemble of either or both proteins, possibly involving extended structure formation.","type":"Results"}],"term_name":"molecular function regulator","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"GO","curator_name":"Jaime Santos Suárez","reference_id":"21856750","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006204","curator_id":"jssuarez","reference_html":"Senescence-associated barley NAC (NAM, ATAF1,2, CUC) transcription factor interacts with radical-induced cell death 1 through a disordered regulatory domain. <i> Kjaersgaard T, Jensen MK, Christiansen MW, Gregersen P, Kragelund BB, Skriver K. </i> J Biol Chem, 2011","ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02965r010","validated":{"curator_id":"bmesza","timestamp":"2020-12-03T18:27:51.468Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":346,"term_id":"GO:0005515","start":177,"version":3,"statement":[{"text":"The CD spectrum of interacting HvNAC013(177–346) and His6-HvRCD1(485–579) seemed to be dominated by the HvNAC013 structure (Fig. 9D). A change in absorbance at both 222 and 208 nm was observed for mixed compared with individual proteins suggesting a shift toward a more unfolded state or more extended structure within the complex (Fig. 9D). This is a strong indication that HvNAC013 and HvRCD1 do not interact through a coupled binding and folding mechanism, but rather through a slight reorientation of the conformational ensemble of either or both proteins, possibly involving extended structure formation.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"F8KA94","partner_end":null}],"term_name":"protein binding","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"GO","curator_name":"Jaime Santos Suárez","reference_id":"21856750","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006204","curator_id":"jssuarez","reference_html":"Senescence-associated barley NAC (NAM, ATAF1,2, CUC) transcription factor interacts with radical-induced cell death 1 through a disordered regulatory domain. <i> Kjaersgaard T, Jensen MK, Christiansen MW, Gregersen P, Kragelund BB, Skriver K. </i> J Biol Chem, 2011","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02965r011","validated":{"curator_id":"bmesza","timestamp":"2020-12-03T18:28:02.123Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":346,"term_id":"GO:0005515","start":177,"version":3,"statement":[{"text":"Spectra of individual proteins and mixed HvNAC013(177–346) and His6-HvRCD1(485–579) were recorded (Fig. 9, A and B). The sum of the spectra of individual proteins was used as reference for noninteracting proteins. Δλmax was calculated and a minor change of 4.5 and 3.0 nm in fluorescence λmax upon mixing of the two proteins was observed from the excitation wavelengths. This suggested that the environment around the aromatic residues changed to more hydrophobic upon interaction (Fig. 9B).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"F8KA94","partner_end":null}],"term_name":"protein binding","ec_name":"fluorescence evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"GO","curator_name":"Jaime Santos Suárez","reference_id":"21856750","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001249","curator_id":"jssuarez","reference_html":"Senescence-associated barley NAC (NAM, ATAF1,2, CUC) transcription factor interacts with radical-induced cell death 1 through a disordered regulatory domain. <i> Kjaersgaard T, Jensen MK, Christiansen MW, Gregersen P, Kragelund BB, Skriver K. </i> J Biol Chem, 2011","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02965r012","validated":{"curator_id":"bmesza","timestamp":"2020-12-03T18:28:11.456Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":346,"term_id":"GO:0098772","start":177,"version":3,"statement":[{"text":"Spectra of individual proteins and mixed HvNAC013(177–346) and His6-HvRCD1(485–579) were recorded (Fig. 9, A and B). The sum of the spectra of individual proteins was used as reference for noninteracting proteins. Δλmax was calculated and a minor change of 4.5 and 3.0 nm in fluorescence λmax upon mixing of the two proteins was observed from the excitation wavelengths. This suggested that the environment around the aromatic residues changed to more hydrophobic upon interaction (Fig. 9B).","type":"Results"}],"term_name":"molecular function regulator","ec_name":"fluorescence evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"GO","curator_name":"Jaime Santos Suárez","reference_id":"21856750","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001249","curator_id":"jssuarez","reference_html":"Senescence-associated barley NAC (NAM, ATAF1,2, CUC) transcription factor interacts with radical-induced cell death 1 through a disordered regulatory domain. <i> Kjaersgaard T, Jensen MK, Christiansen MW, Gregersen P, Kragelund BB, Skriver K. </i> J Biol Chem, 2011","ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2020_12","length":346,"ncbi_taxon_id":112509,"organism":"Hordeum vulgare subsp. vulgare","disprot_id":"DP02965","date":"2020-11-12T15:55:28.246Z","regions_counter":12,"dataset":[],"UniParc":"UPI0002116FAE","uniref100":"UniRef100_F6IAY2","uniref90":"UniRef90_F6IAY2","uniref50":"UniRef50_T1NW97","genes":[{"name":{"value":"NAC013","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CBZ39283.1","url":"https://www.ebi.ac.uk/ena/browser/view/CBZ39283.1"}}]}}],"alphafold_very_low_content":0.49421965317919075,"disorder_content":0.4913294797687861,"disprot_consensus":{"full":[{"start":177,"end":346,"type":"D"}],"Structural state":[{"start":177,"end":346,"type":"D"}],"Molecular function":[{"start":177,"end":346,"type":"F"}]}},{"acc":"Q9SU24","features":{"pfam":[{"id":"PF00004","name":"ATPase family associated with various cellular activities (AAA)","start":467,"end":613},{"id":"PF00628","name":"PHD-finger","start":169,"end":212},{"id":"PF01426","name":"BAH domain","start":250,"end":342},{"id":"PF09079","name":"CDC6, C terminal winged helix domain","start":708,"end":799},{"id":"PF17872","name":"AAA lid domain","start":641,"end":676}],"gene3D":[]},"creator":"jssuarez","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"sequence":"MASTPRAKTFKSPTKTPSNIYRKSYLSPSSTSHTPQTPETHTPLRRSARHVSRKIDLGNDPIDAPGNDPIEGMNLIRKRERAPRKPTTDVVPSKSKKTETPKKKKKIDSFTPVSPIRSETIKKTKKKKRVYYNKVEFDETEFEIGDDVYVKRREDSNSDEEEDPEIEDCQICFKSDTNIMIECDDCLGGFHLKCLKPPLKEVPEGDWICQFCEVKKSGQSQTLDLPKPPEGKKLARTMREKLLSGDLWAARIDKLWKEVDDGVYWIRARWYMIPEETVSGRQPHNLKRELYLTNDFADIEMECILRHCSVKCPKEFSKASNDGDDVFLCEYEYDVHWRSFKRLAELADGDSDSDQEWNGRKEEEVDDSDEEMELDDEVLKSKRGGLTSARGGANSRKGRFFGVEKVGMKLIPEHVRCHKQSELEKAKATLLLATRPKSLPCRSKEMEEITSFIKGSISDDQCLGRCMYIHGVPGTGKTISVLSVMKNLKAEVEEGSVSPYCFVEINGLKLASPENIYSVIYEALSGHRVGWKKALQCLNERFAEGKRIGKEDEKPCILLIDELDLLVTRNQSVLYNILDWPTKPNSKLVVLGIANTMDLPEKLLPRISSRMGIQRLCFGPYNHTQLQEIISTRLNGIDAFEKTAIEFASRKVAAISGDARRALEICRRAAEVADHRLNTNKSAKNQLVIMADVEAAIQEMFQAPHIQVMKSVSKLSKIFLTAMVHELYKTGMAETTFDRVATTVSSICLTNGEAFPGWDILLKIGCDLGECRIILCEPGEKHRLQKLQLNFPSDDVAFALKDNKDLPWLANYL","name":"Origin of replication complex subunit 1B","regions":[{"region_id":"DP02966r001","validated":{"curator_id":"bmesza","timestamp":"2020-12-02T14:41:28.556Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":234,"term_id":"IDPO:0000002","start":216,"version":2,"statement":[{"text":"The two linker regions on both sides of PHD finger that are connected to the BAH domain (residues 156–161 and 216–234) are disordered and were not built into the final model (Figure 1D).","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"26876097","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5HH7"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"jssuarez","reference_html":"Structural Basis for the Unique Multivalent Readout of Unmodified H3 Tail by Arabidopsis ORC1b BAH-PHD Cassette. <i> Li S, Yang Z, Du X, Liu R, Wilkinson AW, Gozani O, Jacobsen SE, Patel DJ, Du J. </i> Structure, 2016","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02966r002","validated":{"curator_id":"bmesza","timestamp":"2020-12-02T14:41:27.576Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":234,"term_id":"IDPO:0000033","start":216,"version":3,"statement":[{"text":"The two linker regions on both sides of PHD finger that are connected to the BAH domain (residues 156–161 and 216–234) are disordered and were not built into the final model (Figure 1D).","type":"Results"}],"term_name":"flexible linker","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"26876097","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5HH7"}],"term_namespace":"Disorder function","ec_id":"ECO:0005670","curator_id":"jssuarez","reference_html":"Structural Basis for the Unique Multivalent Readout of Unmodified H3 Tail by Arabidopsis ORC1b BAH-PHD Cassette. <i> Li S, Yang Z, Du X, Liu R, Wilkinson AW, Gozani O, Jacobsen SE, Patel DJ, Du J. </i> Structure, 2016","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2020_12","length":813,"ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","disprot_id":"DP02966","date":"2020-11-12T19:09:16.264Z","regions_counter":2,"dataset":[],"UniParc":"UPI00000A52D7","uniref100":"UniRef100_Q9SU24","uniref90":"UniRef90_Q9SU24","uniref50":"UniRef50_Q9SU24","genes":[{"name":{"value":"ORC1B","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16179646","url":"http://www.ncbi.nlm.nih.gov/pubmed/16179646","alternativeUrl":"https://europepmc.org/abstract/MED/16179646"}}]},"synonyms":[{"value":"UNE13","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15634699","url":"http://www.ncbi.nlm.nih.gov/pubmed/15634699","alternativeUrl":"https://europepmc.org/abstract/MED/15634699"}}]}],"orfNames":[{"value":"T1P17.210","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"CAB53755.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAB53755.1"}}]}],"olnNames":[{"value":"At4g12620","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT4G12620","url":""}}]}]}],"alphafold_very_low_content":0.2570725707257073,"disorder_content":0.023370233702337023,"disprot_consensus":{"full":[{"start":216,"end":234,"type":"D"}],"Structural state":[{"start":216,"end":234,"type":"D"}],"Disorder function":[{"start":216,"end":234,"type":"F"}]}},{"acc":"Q05128","features":{"pfam":[{"id":"PF07447","name":"Matrix protein VP40","start":27,"end":295}],"gene3D":[]},"name":"Matrix protein VP40","creator":"gpozzati","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Filoviridae","Ebolavirus"],"sequence":"MRRVILPTAPPEYMEAIYPVRSNSTIARGGNSNTGFLTPESVNGDTPSNPLRPIADDTIDHASHTPGSVSSAFILEAMVNVISGPKVLMKQIPIWLPLGVADQKTYSFDSTTAAIMLASYTITHFGKATNPLVRVNRLGPGIPDHPLRLLRIGNQAFLQEFVLPPVQLPQYFTFDLTALKLITQPLPAATWTDDTPTGSNGALRPGISFHPKLRPILLPNKSGKKGNSADLTSPEKIQAIMTSLQDFKIVPIDPTKNIMGIEVPETLVHKLTGKKVTSKNGQPIIPVLLPKYIGLDPVAPGDLTMVITQDCDTCHSPASLPAVIEK","dataset":["Viral proteins"],"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":231,"term_name":"disorder","reference_html":"Ebola and Marburg virus matrix layers are locally ordered assemblies of VP40 dimers. <i> Wan W, Clarke M, Norris MJ, Kolesnikova L, Koehler A, Bornholdt ZA, Becker S, Saphire EO, Briggs JA. </i> Elife, 2020","start":219,"region_id":"DP02967r002","term_id":"IDPO:0000002","unpublished":true,"version":3,"curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","statement":[{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"curator_orcid":"0000-0001-8399-7907","date":"2022-12-28T15:24:36.191Z","reference_source":"pmid","ec_id":"ECO:0006220","reference_id":"33016878","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"7JZT"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":326,"term_name":"disorder","reference_html":"Ebola and Marburg virus matrix layers are locally ordered assemblies of VP40 dimers. <i> Wan W, Clarke M, Norris MJ, Kolesnikova L, Koehler A, Bornholdt ZA, Becker S, Saphire EO, Briggs JA. </i> Elife, 2020","start":309,"region_id":"DP02967r005","term_id":"IDPO:0000002","unpublished":true,"version":3,"curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","statement":[{"text":"The core of the linear hexamer consists of four NTDs from which the linked CTDs are disordered or ‘sprung’ and not resolved.","type":"Introduction"}],"curator_orcid":"0000-0001-8399-7907","date":"2022-12-28T15:22:49.335Z","reference_source":"pmid","ec_id":"ECO:0006220","reference_id":"33016878","ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"7JZT"}]}],"released":"2021_12","length":326,"ncbi_taxon_id":128952,"organism":"Zaire ebolavirus (strain Mayinga-76)","disprot_id":"DP02967","date":"2020-11-13T16:28:17.433Z","regions_counter":5,"UniParc":"UPI000000135F","uniref100":"UniRef100_Q77DJ6","uniref90":"UniRef90_Q77DJ6","uniref50":"UniRef50_Q2PDK5","genes":[{"name":{"value":"VP40"}}],"disorder_content":0.0950920245398773,"disprot_consensus":{"full":[{"start":219,"end":231,"type":"D"},{"start":309,"end":326,"type":"D"}],"Structural state":[{"start":219,"end":231,"type":"D"},{"start":309,"end":326,"type":"D"}]}},{"acc":"Q44177","features":{"pfam":[{"id":"PF02341","name":"RbcX protein","start":1,"end":111}],"gene3D":[]},"creator":"jssuarez","taxonomy":["Bacteria","Cyanobacteria","Synechococcales","Synechococcaceae","Synechococcus","unclassified Synechococcus"],"sequence":"MEFKKVAKETAITLQSYLTYQAVRLISQQLSETNPGQAIWLGEFSKRHPIQESDLYLEAMMLENKELVLRILTVRENLAEGVLEFLPEMVLSQIKQSNGNHRRSLLERLTQVDSSSTDQTEPNPGESDTSEDSE","name":"ORF134","regions":[{"region_id":"DP02968r001","validated":{"curator_id":"bmesza","timestamp":"2020-12-03T18:37:47.295Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":134,"term_id":"IDPO:0000002","start":115,"version":2,"statement":[{"text":"Residues 115 to 134 were not resolved in any of the RbcX peptide chains.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"17574029","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2PEN"},{"db":"PDB","id":"2PEQ"},{"db":"PDB","id":"2PEI"},{"db":"PDB","id":"2PEM"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"jssuarez","reference_html":"Structure and function of RbcX, an assembly chaperone for hexadecameric Rubisco. <i> Saschenbrecker S, Bracher A, Rao KV, Rao BV, Hartl FU, Hayer-Hartl M. </i> Cell, 2007","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02968r003","validated":{"curator_id":"bmesza","timestamp":"2020-12-03T18:37:59.269Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":134,"term_id":"IDPO:0000002","start":110,"version":2,"statement":[{"text":"Indeed, limited proteolysis of RbcX resulted in the removal of the poorly conserved 25 C-terminal residues (Figure S3), leaving a stable core domain of residues 1–109 (RbcX(ΔC25)) which was active in Rubisco assembly (Figure S4).","type":"Results"}],"term_name":"disorder","ec_name":"cleavage assay evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"17574029","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0007691","curator_id":"jssuarez","reference_html":"Structure and function of RbcX, an assembly chaperone for hexadecameric Rubisco. <i> Saschenbrecker S, Bracher A, Rao KV, Rao BV, Hartl FU, Hayer-Hartl M. </i> Cell, 2007","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2020_12","length":134,"ncbi_taxon_id":32049,"organism":"Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6)","disprot_id":"DP02968","date":"2020-11-13T16:52:25.467Z","regions_counter":3,"dataset":[],"UniParc":"UPI00000BBF19","uniref100":"UniRef100_Q44177","uniref90":"UniRef90_Q44177","uniref50":"UniRef50_Q44177","genes":[{"name":{"value":"rbcX","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00855","url":"https://hamap.expasy.org/unirule/MF_00855"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"15564522","url":"http://www.ncbi.nlm.nih.gov/pubmed/15564522","alternativeUrl":"https://europepmc.org/abstract/MED/15564522"}}]},"synonyms":[{"value":"orf134","evidences":[{"code":"ECO:0000303","source":{"name":"Citation","id":"Ref.1","url":"https://www.uniprot.org/uniprot/null#ref1"}}]}],"olnNames":[{"value":"SYNPCC7002_A1797"}]}],"alphafold_very_low_content":0.05970149253731343,"disorder_content":0.1865671641791045,"disprot_consensus":{"full":[{"start":110,"end":134,"type":"D"}],"Structural state":[{"start":110,"end":134,"type":"D"}]}},{"acc":"O80837","features":{"pfam":[{"id":"PF03763","name":"Remorin, C-terminal region","start":80,"end":184},{"id":"PF03766","name":"Remorin, N-terminal region","start":30,"end":76}],"gene3D":[]},"creator":"jssuarez","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"sequence":"MAEEQKTSKVDVESPAVLAPAKEPTPAPVEVADEKIHNPPPVESKALAVVEKPIEEHTPKKASSGSADRDVILADLEKEKKTSFIKAWEESEKSKAENRAQKKISDVHAWENSKKAAVEAQLRKIEEKLEKKKAQYGEKMKNKVAAIHKLAEEKRAMVEAKKGEELLKAEEMGAKYRATGVVPKATCGCF","name":"Remorin","regions":[{"region_id":"DP02969r001","unpublished":true,"validated":{"curator_id":"bmesza","timestamp":"2020-12-17T12:44:09.290Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":77,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"In contrast, AtREM1.3-N showed low ellipticity at 190 nm and a minimum ellipticity at 200 nm, the characteristic pattern of a disordered conformation (57% random coil) (Fig. 1E, table).","type":"Results"}],"term_name":"disorder","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2023_12","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"23027878","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006204","curator_id":"jssuarez","reference_html":"The intrinsically disordered N-terminal region of AtREM1.3 remorin protein mediates protein-protein interactions. <i> Marín M, Thallmair V, Ott T. </i> J Biol Chem, 2012","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02969r002","unpublished":true,"validated":{"curator_id":"bmesza","timestamp":"2020-12-17T12:43:43.102Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":77,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"The abnormally slow migration of AtREM1.3-N supports the presence of intrinsic disorder within this region (32, 33).","type":"Results"}],"term_name":"disorder","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2023_12","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"23027878","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0007689","curator_id":"jssuarez","reference_html":"The intrinsically disordered N-terminal region of AtREM1.3 remorin protein mediates protein-protein interactions. <i> Marín M, Thallmair V, Ott T. </i> J Biol Chem, 2012","ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP02969r003","unpublished":true,"validated":{"curator_id":"bmesza","timestamp":"2020-12-17T12:44:53.668Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":61,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"Incubation of purified AtREM1.3 with increasing concentrations of PK led to the accumulation of a stable fragment migrating at 17 kDa (Fig. 1F). Sequence determination by mass spectrometry of the proteolysis-resistant fragment resulted in the identification of residues 62–176, representing the majority of the C-terminal region.","type":"Results"}],"term_name":"disorder","ec_name":"cleavage assay evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2023_12","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"23027878","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0007691","curator_id":"jssuarez","reference_html":"The intrinsically disordered N-terminal region of AtREM1.3 remorin protein mediates protein-protein interactions. <i> Marín M, Thallmair V, Ott T. </i> J Biol Chem, 2012","ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP02969r004","unpublished":true,"validated":{"curator_id":"bmesza","timestamp":"2020-12-17T12:45:16.639Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":190,"term_id":"IDPO:0000002","start":177,"version":2,"statement":[{"text":"Incubation of purified AtREM1.3 with increasing concentrations of PK led to the accumulation of a stable fragment migrating at 17 kDa (Fig. 1F). Sequence determination by mass spectrometry of the proteolysis-resistant fragment resulted in the identification of residues 62–176, representing the majority of the C-terminal region.","type":"Results"}],"term_name":"disorder","ec_name":"cleavage assay evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2023_12","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"23027878","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0007691","curator_id":"jssuarez","reference_html":"The intrinsically disordered N-terminal region of AtREM1.3 remorin protein mediates protein-protein interactions. <i> Marín M, Thallmair V, Ott T. </i> J Biol Chem, 2012","ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":77,"term_name":"molecular function regulator","reference_html":"The intrinsically disordered N-terminal region of AtREM1.3 remorin protein mediates protein-protein interactions. <i> Marín M, Thallmair V, Ott T. </i> J Biol Chem, 2012","start":1,"region_id":"DP02969r005","term_id":"GO:0098772","unpublished":true,"version":3,"curator_id":"jssuarez","released":"2023_12","term_ontology":"GO","curator_name":"Jaime Santos Suárez","ec_name":"GAL4-VP16 functional complementation evidence used in manual assertion","statement":[{"text":"For this, different truncated AtREM1.3 variants were co-expressed with AtIMPa1, AtIMPa2, AtIMPa3, and AtIMPa6 using the GAL4 system.","type":"Results"},{"text":"Deletion of the N-terminal region led to a significant reduction in the interaction strength with AtIMPa1 and AtIMpa2 in the quantitative β-galactosidase assay (Fig. 5, B and D), indicating that the ID N-terminal region also contributed to interaction with the importin α proteins.","type":"Results"}],"curator_orcid":"0000-0001-9045-7765","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006297","reference_id":"23027878","validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-15T09:36:25.996Z"},"ec_go":"IPI","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP02969r007","unpublished":true,"validated":{"curator_id":"bmesza","timestamp":"2020-12-17T13:11:56.060Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":68,"term_id":"IDPO:0000045","start":64,"version":2,"statement":[{"text":"Phosphorylation of Ser-66 in the intrinsically disordered N-terminal region decreases the interaction strength with the importin α proteins.","type":"Abstract"},{"text":"Furthermore, constitutive phosphorylation of Ser-66 decreases the interaction with importin α proteins, implying that phosphorylation of AtREM1.3 in its ID N-terminal domain could be a mechanism of controlling protein interactions with cytosolic proteins.","type":"Discussion"},{"text":"Phosphoablative (AtREM1.3-S66A) and phosphomimetic (AtREM1.3-S66D) mutant variants of Ser-66 were created and used to assess the possible impact of phosphorylation within the ID N-terminal domain in the interaction with importin α proteins. Quantitative β-galactosidase assays showed a tendency to reduced interaction strength of AtIMpa1 and AtIMpa2 with the phosphomimetic variant. ","type":"Results"}],"term_name":"phosphorylation display site","ec_name":"mutant phenotype evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2023_12","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"23027878","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Disorder function","ec_id":"ECO:0000315","curator_id":"jssuarez","reference_html":"The intrinsically disordered N-terminal region of AtREM1.3 remorin protein mediates protein-protein interactions. <i> Marín M, Thallmair V, Ott T. </i> J Biol Chem, 2012","ec_go":"IMP","disprot_namespace":"Disorder function"},{"start":64,"end":68,"reference_id":"23027878","reference_source":"pmid","reference_html":"The intrinsically disordered N-terminal region of AtREM1.3 remorin protein mediates protein-protein interactions. <i> Marín M, Thallmair V, Ott T. </i> J Biol Chem, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006297","ec_ontology":"ECO","ec_name":"GAL4-VP16 functional complementation evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP02969r008","statement":[{"text":"Phosphoablative (AtREM1.3-S66A) and phosphomimetic (AtREM1.3-S66D) mutant variants of Ser-66 were created and used to assess the possible impact of phosphorylation within the ID N-terminal domain in the interaction with importin α proteins. Quantitative β-galactosidase assays showed a tendency to reduced interaction strength of AtIMpa1 and AtIMpa2 with the phosphomimetic variant. Interestingly, this reduction is comparable with the reduction observed in the variant devoid of the N-terminal domain (Fig. 5, B and D).","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-15T09:37:25.724Z"},"ec_go":"IPI","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2023_12","length":190,"ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","disprot_id":"DP02969","date":"2020-11-13T17:33:44.947Z","regions_counter":8,"dataset":[],"UniParc":"UPI00000AAA09","uniref100":"UniRef100_O80837","uniref90":"UniRef90_O80837","uniref50":"UniRef50_O80837","genes":[{"name":{"value":"DBP"},"orfNames":[{"value":"F4I18.20"}],"olnNames":[{"value":"At2g45820"}]}],"alphafold_very_low_content":0.23157894736842105,"disorder_content":0.4789473684210526,"disprot_consensus":{"full":[{"start":1,"end":77,"type":"D"},{"start":177,"end":190,"type":"D"}],"Structural state":[{"start":1,"end":77,"type":"D"},{"start":177,"end":190,"type":"D"}],"Molecular function":[{"start":1,"end":77,"type":"F"}],"Disorder function":[{"start":64,"end":68,"type":"F"}]}},{"acc":"Q5JRX3","features":{"pfam":[{"id":"PF00675","name":"Insulinase (Peptidase family M16)","start":96,"end":177},{"id":"PF05193","name":"Peptidase M16 inactive domain","start":245,"end":429},{"id":"PF08367","name":"Peptidase M16C associated","start":504,"end":752},{"id":"PF22516","name":"PreP C-terminal domain","start":856,"end":1001}],"gene3D":[]},"creator":"jssuarez","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MWRCGGRQGLCVLRRLSGGHAHHRAWRWNSNRACERALQYKLGDKIHGFTVNQVTSVPELFLTAVKLTHDDTGARYLHLAREDTNNLFSVQFRTTPMDSTGVPHILEHTVLCGSQKYPCRDPFFKMLNRSLSTFMNAFTASDYTLYPFSTQNPKDFQNLLSVYLDATFFPCLRELDFWQEGWRLEHENPSDPQTPLVFKGVVFNEMKGAFTDNERIFSQHLQNRLLPDHTYSVVSGGDPLCIPELTWEQLKQFHATHYHPSNARFFTYGNFPLEQHLKQIHEEALSKFQKIEPSTVVPAQTPWDKPREFQITCGPDSFATDPSKQTTISVSFLLPDITDTFEAFTLSLLSSLLTSGPNSPFYKALIESGLGTDFSPDVGYNGYTREAYFSVGLQGIAEKDIETVRSLIDRTIDEVVEKGFEDDRIEALLHKIEIQMKHQSTSFGLMLTSYIASCWNHDGDPVELLKLGNQLAKFRQCLQENPKFLQEKVKQYFKNNQHKLTLSMRPDDKYHEKQAQVEATKLKQKVEALSPGDRQQIYEKGLELRSQQSKPQDASCLPALKVSDIEPTIPVTELDVVLTAGDIPVQYCAQPTNGMVYFRAFSSLNTLPEELRPYVPLFCSVLTKLGCGLLDYREQAQQIELKTGGMSASPHVLPDDSHMDTYEQGVLFSSLCLDRNLPDMMQLWSEIFNNPCFEEEEHFKVLVKMTAQELANGIPDSGHLYASIRAGRTLTPAGDLQETFSGMDQVRLMKRIAEMTDIKPILRKLPRIKKHLLNGDNMRCSVNATPQQMPQTEKAVEDFLRSIGRSKKERRPVRPHTVEKPVPSSSGGDAHVPHGSQVIRKLVMEPTFKPWQMKTHFLMPFPVNYVGECIRTVPYTDPDHASLKILARLMTAKFLHTEIREKGGAYGGGAKLSHNGIFTLYSYRDPNTIETLQSFGKAVDWAKSGKFTQQDIDEAKLSVFSTVDAPVAPSDKGMDHFLYGLSDEMKQAHREQLFAVSHDKLLAVSDRYLGTGKSTHGLAILGPENPKIAKDPSWIIQ","name":"Presequence protease, mitochondrial","regions":[{"start":774,"end":787,"reference_id":"24931469","reference_source":"pmid","reference_html":"Molecular basis of substrate recognition and degradation by human presequence protease. <i> King JV, Liang WG, Scherpelz KP, Schilling AB, Meredith SC, Tang WJ. </i> Structure, 2014","date":"2022-08-02T19:58:44.720Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4L3T"}],"region_id":"DP02971r003","statement":[{"text":"The PDB shows this region lacks electron density, indicating it's disordered.","type":"Curator statement"}]}],"released":"2023_06","length":1037,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP02971","date":"2020-11-13T19:11:01.866Z","regions_counter":3,"dataset":["NDDs-related proteins"],"UniParc":"UPI000013C859","uniref100":"UniRef100_Q5JRX3","uniref90":"UniRef90_Q5JRX3","uniref50":"UniRef50_Q5JRX3","genes":[{"name":{"value":"PITRM1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:17663","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:17663"}}]},"synonyms":[{"value":"KIAA1104","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"BAA83056.2","url":"https://www.ebi.ac.uk/ena/browser/view/BAA83056.2"}}]},{"value":"MP1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10360838","url":"http://www.ncbi.nlm.nih.gov/pubmed/10360838","alternativeUrl":"https://europepmc.org/abstract/MED/10360838"}}]},{"value":"PREP","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16849325","url":"http://www.ncbi.nlm.nih.gov/pubmed/16849325","alternativeUrl":"https://europepmc.org/abstract/MED/16849325"}}]}]}],"alphafold_very_low_content":0.03857280617164899,"disorder_content":0.013500482160077145,"disprot_consensus":{"full":[{"start":774,"end":787,"type":"D"}],"Structural state":[{"start":774,"end":787,"type":"D"}]}},{"acc":"P06734","features":{"pfam":[{"id":"PF00059","name":"Lectin C-type domain","start":181,"end":283}],"gene3D":[]},"creator":"gpozzati","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MEEGQYSEIEELPRRRCCRRGTQIVLLGLVTAALWAGLLTLLLLWHWDTTQSLKQLEERAARNVSQVSKNLESHHGDQMAQKSQSTQISQELEELRAEQQRLKSQDLELSWNLNGLQADLSSFKSQELNERNEASDLLERLREEVTKLRMELQVSSGFVCNTCPEKWINFQRKCYYFGKGTKQWVHARYACDDMEGQLVSIHSPEEQDFLTKHASHTGSWIGLRNLDLKGEFIWVDGSHVDYSNWAPGEPTSRSQGEDCVMMRGSGRWNDAFCDRKLGAWVCDRLATCTPPASEGSAESMGPDSRPDPDGRLPTPSAPLHS","name":"Low affinity immunoglobulin epsilon Fc receptor","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":159,"term_name":"disorder","start":150,"region_id":"DP02975r002","term_id":"IDPO:0000002","unpublished":true,"reference_html":"Structural changes in the lectin domain of CD23, the low-affinity IgE receptor, upon calcium binding. <i> Wurzburg BA, Tarchevskaya SS, Jardetzky TS. </i> Structure, 2006","curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-12-28T13:46:46.806Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2H2T"}],"reference_id":"16765898","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"The final model includes residues 160–288 of CD23, 1 calcium ion, and 173 water molecules. The model is missing 13 N-terminal residues, 33 C-terminal residues (289–321), and internal residues 253–257.","type":"Results"}]},{"term_namespace":"Structural state","ec_ontology":"ECO","end":321,"term_name":"disorder","start":293,"region_id":"DP02975r003","term_id":"IDPO:0000002","unpublished":true,"reference_html":"Structural changes in the lectin domain of CD23, the low-affinity IgE receptor, upon calcium binding. <i> Wurzburg BA, Tarchevskaya SS, Jardetzky TS. </i> Structure, 2006","curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-12-28T13:41:04.638Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2H2R"},{"db":"PDB","id":"2H2T"}],"reference_id":"16765898","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"Electron density for the 30 C-terminal residues (292–321) of the construct is not observed, and these residues are not part of the predicted lectin domain.","type":"Results"}]},{"region_id":"DP02975r005","unpublished":true,"ec_ontology":"ECO","end":258,"term_id":"IDPO:0000002","start":244,"version":3,"statement":[{"text":"In the absence of Ca2+ binding to CD23, as in the complex presented here, the loop including Asp258 is found to be partially flexible","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-8399-7907","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","reference_id":"28361904","date":"2022-12-28T13:32:22.499Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5LGK"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"vnugnes","reference_html":"IgE binds asymmetrically to its B cell receptor CD23. <i> Dhaliwal B, Pang MO, Keeble AH, James LK, Gould HJ, McDonnell JM, Sutton BJ, Beavil AJ. </i> Sci Rep, 2017","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P01854"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"506227","entry_name":"N-acetyl-D-glucosamine"}]}],"released":"2021_12","length":321,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP02975","date":"2020-11-16T10:59:38.206Z","regions_counter":9,"dataset":[],"UniParc":"UPI000002BEF3","uniref100":"UniRef100_P06734","uniref90":"UniRef90_P06734","uniref50":"UniRef50_P06734","genes":[{"name":{"value":"FCER2"},"synonyms":[{"value":"CD23A"},{"value":"CLEC4J"},{"value":"FCE2"},{"value":"IGEBF"}]}],"alphafold_very_low_content":0.059190031152647975,"disorder_content":0.16822429906542055,"disprot_consensus":{"full":[{"start":150,"end":159,"type":"D"},{"start":244,"end":258,"type":"D"},{"start":293,"end":321,"type":"D"}],"Structural state":[{"start":150,"end":159,"type":"D"},{"start":244,"end":258,"type":"D"},{"start":293,"end":321,"type":"D"}]}},{"acc":"Q05193","features":{"pfam":[{"id":"PF00169","name":"PH domain","start":520,"end":621},{"id":"PF00350","name":"Dynamin family","start":34,"end":207},{"id":"PF01031","name":"Dynamin central region","start":215,"end":501},{"id":"PF02212","name":"Dynamin GTPase effector domain","start":656,"end":744}],"gene3D":[]},"creator":"tszani","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MGNRGMEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNATTEYAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSDLANSDALKVAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLPGLRNKLQSQLLSIEKEVEEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSGDQIDTYELSGGARINRIFHERFPFELVKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLREEMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQRSNQMNKKKTSGNQDEILVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDYRQLELACETQEEVDSWKASFLRAGVYPERVGDKEKASETEENGSDSFMHSMDPQLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHALKEALSIIGDINTTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRSGQASPSRPESPRPPFDL","name":"Dynamin-1","regions":[{"region_id":"DP02976r001","validated":{"curator_id":"fquaglia","timestamp":"2020-11-25T16:19:55.266Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":356,"term_id":"IDPO:0000002","start":347,"version":2,"statement":[{"text":"Residues 63–64, 110–112, 143–149, 347–356, 394–404, 446–447, 500–517, 534–537, 578–581 and 632–652 are disordered. ","type":"Methods"},{"text":"α1S in dynamin 1 is subdivided into α1NS, α1MS and α1CS by two disordered loops, L1NS and L1CS, compared to a single break of the corresponding helix in MxA.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-3130-9284","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamás Szaniszló","reference_id":"21927000","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3SNH"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"tszani","reference_html":"Crystal structure of nucleotide-free dynamin. <i> Faelber K, Posor Y, Gao S, Held M, Roske Y, Schulze D, Haucke V, Noé F, Daumke O. </i> Nature, 2011","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02976r002","validated":{"curator_id":"fquaglia","timestamp":"2020-11-25T16:19:59.583Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":517,"term_id":"IDPO:0000033","start":500,"version":3,"statement":[{"text":"Residues 63–64, 110–112, 143–149, 347–356, 394–404, 446–447, 500–517, 534–537, 578–581 and 632–652 are disordered. ","type":"Methods"},{"text":"The PH domain is interconnected between α3S and α4S of the stalk by two disordered loops, L1SP and L2SP, and shows only minor deviations from the isolated PH domain of dynamin 1 (refs 14, 15; r.m.s.d. of 0.8 Å for 102 Cα atoms).","type":"Results"},{"text":"The IDR spanning residues 500-517 is a flexible linker connecting the Stalk in the middle domain (MD) and the PH domain as shown in Fig 1.","type":"Curator statement"}],"term_name":"flexible linker","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0002-3130-9284","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamás Szaniszló","reference_id":"21927000","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3SNH"}],"term_namespace":"Disorder function","ec_id":"ECO:0005670","curator_id":"tszani","reference_html":"Crystal structure of nucleotide-free dynamin. <i> Faelber K, Posor Y, Gao S, Held M, Roske Y, Schulze D, Haucke V, Noé F, Daumke O. </i> Nature, 2011","ec_go":"EXP","disprot_namespace":"Disorder function"},{"region_id":"DP02976r003","validated":{"curator_id":"fquaglia","timestamp":"2020-11-25T16:20:00.595Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":652,"term_id":"IDPO:0000033","start":632,"version":3,"statement":[{"text":"Residues 63–64, 110–112, 143–149, 347–356, 394–404, 446–447, 500–517, 534–537, 578–581 and 632–652 are disordered. ","type":"Methods"},{"text":"The PH domain is interconnected between α3S and α4S of the stalk by two disordered loops, L1SP and L2SP, and shows only minor deviations from the isolated PH domain of dynamin 1 (refs 14, 15; r.m.s.d. of 0.8 Å for 102 Cα atoms).  ","type":"Results"},{"text":"The IDR spanning residues 632-652  is a flexible linker connecting the PH domain and the Stalk of the GTPase effector domain (GED) as shown in Fig 1.","type":"Curator statement"}],"term_name":"flexible linker","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0002-3130-9284","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamás Szaniszló","reference_id":"21927000","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3SNH"}],"term_namespace":"Disorder function","ec_id":"ECO:0005670","curator_id":"tszani","reference_html":"Crystal structure of nucleotide-free dynamin. <i> Faelber K, Posor Y, Gao S, Held M, Roske Y, Schulze D, Haucke V, Noé F, Daumke O. </i> Nature, 2011","ec_go":"EXP","disprot_namespace":"Disorder function"},{"region_id":"DP02976r004","validated":{"curator_id":"fquaglia","timestamp":"2020-11-25T16:19:55.981Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":404,"term_id":"IDPO:0000002","start":394,"version":2,"statement":[{"text":"Residues 63–64, 110–112, 143–149, 347–356, 394–404, 446–447, 500–517, 534–537, 578–581 and 632–652 are disordered. ","type":"Methods"},{"text":"α1S in dynamin 1 is subdivided into α1NS, α1MS and α1CS by two disordered loops, L1NS and L1CS, compared to a single break of the corresponding helix in MxA.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-3130-9284","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamás Szaniszló","reference_id":"21927000","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3SNH"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"tszani","reference_html":"Crystal structure of nucleotide-free dynamin. <i> Faelber K, Posor Y, Gao S, Held M, Roske Y, Schulze D, Haucke V, Noé F, Daumke O. </i> Nature, 2011","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02976r005","validated":{"curator_id":"fquaglia","timestamp":"2020-11-25T16:19:57.187Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":517,"term_id":"IDPO:0000002","start":500,"version":2,"statement":[{"text":"Residues 63–64, 110–112, 143–149, 347–356, 394–404, 446–447, 500–517, 534–537, 578–581 and 632–652 are disordered.","type":"Methods"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-3130-9284","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamás Szaniszló","reference_id":"21927000","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3SNH"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"tszani","reference_html":"Crystal structure of nucleotide-free dynamin. <i> Faelber K, Posor Y, Gao S, Held M, Roske Y, Schulze D, Haucke V, Noé F, Daumke O. </i> Nature, 2011","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02976r006","validated":{"curator_id":"fquaglia","timestamp":"2020-11-25T16:19:58.197Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":652,"term_id":"IDPO:0000002","start":632,"version":2,"statement":[{"text":"Residues 63–64, 110–112, 143–149, 347–356, 394–404, 446–447, 500–517, 534–537, 578–581 and 632–652 are disordered.","type":"Methods"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-3130-9284","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamás Szaniszló","reference_id":"21927000","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3SNH"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"tszani","reference_html":"Crystal structure of nucleotide-free dynamin. <i> Faelber K, Posor Y, Gao S, Held M, Roske Y, Schulze D, Haucke V, Noé F, Daumke O. </i> Nature, 2011","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":864,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP02976","date":"2020-11-16T12:52:30.706Z","regions_counter":6,"dataset":["NDDs-related proteins"],"UniParc":"UPI0000129A1E","uniref100":"UniRef100_Q05193","uniref90":"UniRef90_P21575","uniref50":"UniRef50_P21575","genes":[{"name":{"value":"DNM1"},"synonyms":[{"value":"DNM"}]}],"alphafold_very_low_content":0.16203703703703703,"disorder_content":0.06944444444444445,"disprot_consensus":{"full":[{"start":347,"end":356,"type":"D"},{"start":394,"end":404,"type":"D"},{"start":500,"end":517,"type":"D"},{"start":632,"end":652,"type":"D"}],"Structural state":[{"start":347,"end":356,"type":"D"},{"start":394,"end":404,"type":"D"},{"start":500,"end":517,"type":"D"},{"start":632,"end":652,"type":"D"}],"Disorder function":[{"start":500,"end":517,"type":"F"},{"start":632,"end":652,"type":"F"}]}},{"acc":"O75962","features":{"pfam":[{"id":"PF00018","name":"SH3 domain","start":1662,"end":1713},{"id":"PF00069","name":"Protein kinase domain","start":2796,"end":3050},{"id":"PF00435","name":"Spectrin repeat","start":341,"end":444},{"id":"PF00435","name":"Spectrin repeat","start":570,"end":670},{"id":"PF00435","name":"Spectrin repeat","start":909,"end":1006},{"id":"PF00435","name":"Spectrin repeat","start":1140,"end":1243},{"id":"PF00621","name":"RhoGEF domain","start":1296,"end":1464},{"id":"PF00621","name":"RhoGEF domain","start":1973,"end":2143},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":2685,"end":2776},{"id":"PF13716","name":"Divergent CRAL/TRIO domain","start":84,"end":211},{"id":"PF16609","name":"SH3-RhoGEF linking unstructured region","start":1715,"end":1972},{"id":"PF22697","name":"SOS1/NGEF-like PH domain","start":1480,"end":1589},{"id":"PF22697","name":"SOS1/NGEF-like PH domain","start":2159,"end":2269},{"id":"PF23323","name":"Kalirin-like, spectrin repeats","start":787,"end":896},{"id":"PF23587","name":"Kalirin, SH3","start":2546,"end":2614}],"gene3D":[]},"creator":"gpozzati","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MSGSSGGAAAPAASSGPAAAASAAGSGCGGGAGEGAEEAAKDLADIAAFFRSGFRKNDEMKAMDVLPILKEKVAYLSGGRDKRGGPILTFPARSNHDRIRQEDLRRLISYLACIPSEEVCKRGFTVIVDMRGSKWDSIKPLLKILQESFPCCIHVALIIKPDNFWQKQRTNFGSSKFEFETNMVSLEGLTKVVDPSQLTPEFDGCLEYNHEEWIEIRVAFEDYISNATHMLSRLEELQDILAKKELPQDLEGARNMIEEHSQLKKKVIKAPIEDLDLEGQKLLQRIQSSESFPKKNSGSGNADLQNLLPKVSTMLDRLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWITHNKGLFLNSYTEIGTSHPHAMELQTQHNHFAMNCMNVYVNINRIMSVANRLVESGHYASQQIRQIASQLEQEWKAFAAALDERSTLLDMSSIFHQKAEKYMSNVDSWCKACGEVDLPSELQDLEDAIHHHQGIYEHITLAYSEVSQDGKSLLDKLQRPLTPGSSDSLTASANYSKAVHHVLDVIHEVLHHQRQLENIWQHRKVRLHQRLQLCVFQQDVQQVLDWIENHGEAFLSKHTGVGKSLHRARALQKRHEDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYQAAHQLEDRIQDFVRRVEQRKILLDMSVSFHTHVKELWTWLEELQKELLDDVYAESVEAVQDLIKRFGQQQQTTLQVTVNVIKEGEDLIQQLRDSAISSNKTPHNSSINHIETVLQQLDEAQSQMEELFQERKIKLELFLQLRIFERDAIDIISDLESWNDELSQQMNDFDTEDLTIAEQRLQHHADKALTMNNLTFDVIHQGQDLLQYVNEVQASGVELLCDRDVDMATRVQDLLEFLHEKQQELDLAAEQHRKHLEQCVQLRHLQAEVKQVLGWIRNGESMLNAGLITASSLQEAEQLQREHEQFQHAIEKTHQSALQVQQKAEAMLQANHYDMDMIRDCAEKVASHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVLESLEQEYKREEDWCGGADKLGPNSETDHVTPMISKHLEQKEAFLKACTLARRNADVFLKYLHRNSVNMPGMVTHIKAPEQQVKNILNELFQRENRVLHYWTMRKRRLDQCQQYVVFERSAKQALEWIHDNGEFYLSTHTSTGSSIQHTQELLKEHEEFQITAKQTKERVKLLIQLADGFCEKGHAHAAEIKKCVTAVDKRYRDFSLRMEKYRTSLEKALGISSDSNKSSKSLQLDIIPASIPGSEVKLRDAAHELNEEKRKSARRKEFIMAELIQTEKAYVRDLRECMDTYLWEMTSGVEEIPPGIVNKELIIFGNMQEIYEFHNNIFLKELEKYEQLPEDVGHCFVTWADKFQMYVTYCKNKPDSTQLILEHAGSYFDEIQQRHGLANSISSYLIKPVQRITKYQLLLKELLTCCEEGKGEIKDGLEVMLSVPKRANDAMHLSMLEGFDENIESQGELILQESFQVWDPKTLIRKGRERHLFLFEMSLVFSKEVKDSSGRSKYLYKSKLFTSELGVTEHVEGDPCKFALWVGRTPTSDNKIVLKASSIENKQDWIKHIREVIQERTIHLKGALKEPIHIPKTAPATRQKGRRDGEDLDSQGDGSSQPDTISIASRTSQNTLDSDKLSGGCELTVVIHDFTACNSNELTIRRGQTVEVLERPHDKPDWCLVRTTDRSPAAEGLVPCGSLCIAHSRSSMEMEGIFNHKDSLSVSSNDASPPASVASLQPHMIGAQSSPGPKRPGNTLRKWLTSPVRRLSSGKADGHVKKLAHKHKKSREVRKSADAGSQKDSDDSAATPQDETVEERGRNEGLSSGTLSKSSSSGMQSCGEEEGEEGADAVPLPPPMAIQQHSLLQPDSQDDKASSRLLVRPTSSETPSAAELVSAIEELVKSKMALEDRPSSLLVDQGDSSSPSFNPSDNSLLSSSSPIDEMEERKSSSLKRRHYVLQELVETERDYVRDLGYVVEGYMALMKEDGVPDDMKGKDKIVFGNIHQIYDWHRDFFLGELEKCLEDPEKLGSLFVKHERRLHMYIAYCQNKPKSEHIVSEYIDTFFEDLKQRLGHRLQLTDLLIKPVQRIMKYQLLLKDFLKYSKKASLDTSELERAVEVMCIVPRRCNDMMNVGRLQGFDGKIVAQGKLLLQDTFLVTDQDAGLLPRCRERRIFLFEQIVIFSEPLDKKKGFSMPGFLFKNSIKVSCLCLEENVENDPCKFALTSRTGDVVETFILHSSSPSVRQTWIHEINQILENQRNFLNALTSPIEYQRNHSGGGGGGGSGGSGGGGGSGGGGAPSGGSGHSGGPSSCGGAPSTSRSRPSRIPQPVRHHPPVLVSSAASSQAEADKMSGTSTPGPSLPPPGAAPEAGPSAPSRRPPGADAEGSEREAEPIPKMKVLESPRKGAANASGSSPDAPAKDARASLGTLPLGKPRAGAASPLNSPLSSAVPSLGKEPFPPSSPLQKGGSFWSSIPASPASRPGSFTFPGDSDSLQRQTPRHAAPGKDTDRMSTCSSASEQSVQSTQSNGSESSSSSNISTMLVTHDYTAVKEDEINVYQGEVVQILASNQQNMFLVFRAATDQCPAAEGWIPGFVLGHTSAVIVENPDGTLKKSTSWHTALRLRKKSEKKDKDGKREGKLENGYRKSREGLSNKVSVKLLNPNYIYDVPPEFVIPLSEVTCETGETVVLRCRVCGRPKASITWKGPEHNTLNNDGHYSISYSDLGEATLKIVGVTTEDDGIYTCIAVNDMGSASSSASLRVLGPGMDGIMVTWKDNFDSFYSEVAELGRGRFSVVKKCDQKGTKRAVATKFVNKKLMKRDQVTHELGILQSLQHPLLVGLLDTFETPTSYILVLEMADQGRLLDCVVRWGSLTEGKIRAHLGEVLEAVRYLHNCRIAHLDLKPENILVDESLAKPTIKLADFGDAVQLNTTYYIHQLLGNPEFAAPEIILGNPVSLTSDTWSVGVLTYVLLSGVSPFLDDSVEETCLNICRLDFSFPDDYFKGVSQKAKEFVCFLLQEDPAKRPSAALALQEQWLQAGNGRSTGVLDTSRLTSFIERRKHQNDVRPIRSIKNFLQSRLLPRV","name":"Triple functional domain protein","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1507,"term_name":"disorder","start":1494,"region_id":"DP02977r001","term_id":"IDPO:0000002","unpublished":true,"reference_html":"The DH and PH domains of Trio coordinately engage Rho GTPases for their efficient activation. <i> Chhatriwala MK, Betts L, Worthylake DK, Sondek J. </i> J Mol Biol, 2007","curator_id":"vnugnes","released":"2023_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-08-05T15:31:34.500Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"2NZ8"}],"reference_id":"17391702","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63000"}]}],"released":"2023_06","length":3097,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP02977","date":"2020-11-17T09:18:09.022Z","regions_counter":1,"dataset":["NDDs-related proteins"],"UniParc":"UPI0000049BA9","uniref100":"UniRef100_O75962","uniref90":"UniRef90_O75962","uniref50":"UniRef50_O75962","genes":[{"name":{"value":"TRIO"}}],"disorder_content":0.004520503713270907,"disprot_consensus":{"full":[{"start":1494,"end":1507,"type":"D"}],"Structural state":[{"start":1494,"end":1507,"type":"D"}]}},{"acc":"Q9BSQ5","features":{"pfam":[{"id":"PF16545","name":"Cerebral cavernous malformation protein, harmonin-homology","start":287,"end":387}],"gene3D":[]},"creator":"gpozzati","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MEEEGKKGKKPGIVSPFKRVFLKGEKSRDKKAHEKVTERRPLHTVVLSLPERVEPDRLLSDYIEKEVKYLGQLTSIPGYLNPSSRTEILHFIDNAKRAHQLPGHLTQEHDAVLSLSAYNVKLAWRDGEDIILRVPIHDIAAVSYVRDDAAHLVVLKTAQDPGISPSQSLCAESSRGLSAGSLSESAVGPVEACCLVILAAESKVAAEELCCLLGQVFQVVYTESTIDFLDRAIFDGASTPTHHLSLHSDDSSTKVDIKETYEVEASTFCFPESVDVGGASPHSKTISESELSASATELLQDYMLTLRTKLSSQEIQQFAALLHEYRNGASIHEFCINLRQLYGDSRKFLLLGLRPFIPEKDSQHFENFLETIGVKDGRGIITDSFGRHRRALSTTSSSTTNGNRATGSSDDRSAPSEGDEWDRMISDISSDIEALGCSMDQDSA","name":"Cerebral cavernous malformations 2 protein","regions":[{"region_id":"DP02978r001","unpublished":true,"ec_ontology":"ECO","end":190,"term_id":"IDPO:0000002","start":160,"version":2,"statement":[{"text":"Based on our crystal structure, CCM2PTB comprises residues Ser60–Tyr221 with a 32-residue flexible loop (loop β6/β7) inserted between strands β6 and β7 (residues Asp160–Glu191), for which we do not observe density in any of the four copies of CCM2PTB","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-4303-9939","released":"2022_03","term_ontology":"IDPO","curator_name":"Gabriele Pozzati","reference_id":"25525273","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4WJ7"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"gpozzati","reference_html":"Structural basis for the disruption of the cerebral cavernous malformations 2 (CCM2) interaction with Krev interaction trapped 1 (KRIT1) by disease-associated mutations. <i> Fisher OS, Liu W, Zhang R, Stiegler AL, Ghedia S, Weber JL, Boggon TJ. </i> J Biol Chem, 2015","validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-15T16:35:56.519Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02978r003","unpublished":true,"ec_ontology":"ECO","end":420,"term_id":"IDPO:0000002","start":377,"version":2,"statement":[{"text":"The long loop (residues 377–420) connecting CCM2cts and CCM2-chelix, and the remaining residues beyond α6, are omitted in the final model due to the lack of interpretable electron density, indicative of their high intrinsic flexibility.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-4303-9939","released":"2022_03","term_ontology":"IDPO","curator_name":"Gabriele Pozzati","reference_id":"25982527","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4YKC"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"gpozzati","reference_html":"Structural Insights into the Molecular Recognition between Cerebral Cavernous Malformation 2 and Mitogen-Activated Protein Kinase Kinase Kinase 3. <i> Wang X, Hou Y, Deng K, Zhang Y, Wang DC, Ding J. </i> Structure, 2015","validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-15T16:56:59.291Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_12","length":444,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP02978","date":"2020-11-17T10:09:14.202Z","regions_counter":3,"dataset":[],"UniParc":"UPI000006CE51","uniref100":"UniRef100_Q9BSQ5","uniref90":"UniRef90_Q9BSQ5","uniref50":"UniRef50_Q9BSQ5","genes":[{"name":{"value":"CCM2"},"synonyms":[{"value":"C7orf22"}],"orfNames":[{"value":"PP10187"}]}],"alphafold_very_low_content":0.3400900900900901,"disorder_content":0.16891891891891891,"disprot_consensus":{"full":[{"start":160,"end":190,"type":"D"},{"start":377,"end":420,"type":"D"}],"Structural state":[{"start":160,"end":190,"type":"D"},{"start":377,"end":420,"type":"D"}]}},{"acc":"Q4V8K1","features":{"pfam":[{"id":"PF01794","name":"Ferric reductase like transmembrane component","start":249,"end":394},{"id":"PF03807","name":"NADP oxidoreductase coenzyme F420-dependent","start":22,"end":107}],"gene3D":[]},"creator":"ashenoy","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"sequence":"MEKTCADEFPLTVDSSEKQGVVCIFGTGDFGKSLGLKMLQCGYSVVFGSRNPQVSSLLPRGAEVLCYSEAASRSDVIVLAVHREHYDFLAELADSLKGRVLIDVSNNQKMNQYPESNAEYLAQLVPGAHVVKAFNTISAWALQSGTLDASRQVFVCGNDSKAKDRVMDIARTLGLTPLDQGSLVAAKEIENYPLQLFPMWRFPFYLSSGLCVFFFVYCAIREVIYPYVTGKTDSTYRLVVSIPNRVFPITALTLLALVYLPGILAAILQLYRGTKYRRFPNWLDHWMLCRKQLGLVALGFAFLHAIYTLVIPIRYYVRWRLRNATITQALTNKDSPFSSSTAWLSDSYLALGILGFFLFLLLGITSLPSVSNMVNWREFRFVQSKLGYLTLVLCTAHTLVYGGKRFLSPSILIWSLPSAYILALIIPCTVLVMKFILIMPCIDKTLTRIRQGWERKSKYAQSTLNGKSDI","name":"Metalloreductase STEAP4","regions":[{"region_id":"DP02980r001","unpublished":true,"ec_ontology":"ECO","end":18,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"These are as follows: first, a short loop between α5 and β7 (residues 147–149), which is also poorly ordered in Steap3 (residues 157–162); second, the N-terminal 18 residues are also disordered.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-7748-2501","released":"2022_03","term_ontology":"IDPO","curator_name":"Aditi Shenoy","reference_id":"23733181","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2YJZ"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"ashenoy","reference_html":"The crystal structure of six-transmembrane epithelial antigen of the prostate 4 (Steap4), a ferri/cuprireductase, suggests a novel interdomain flavin-binding site. <i> Gauss GH, Kleven MD, Sendamarai AK, Fleming MD, Lawrence CM. </i> J Biol Chem, 2013","validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-15T17:16:53.174Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_12","length":470,"ncbi_taxon_id":10116,"organism":"Rattus norvegicus","disprot_id":"DP02980","date":"2020-11-19T16:07:31.307Z","regions_counter":1,"dataset":[],"UniParc":"UPI0000520BA1","uniref100":"UniRef100_Q4V8K1","uniref90":"UniRef90_Q4V8K1","uniref50":"UniRef50_Q4V8K1","genes":[{"name":{"value":"Steap4"}}],"alphafold_very_low_content":0.05531914893617021,"disorder_content":0.03829787234042553,"disprot_consensus":{"full":[{"start":1,"end":18,"type":"D"}],"Structural state":[{"start":1,"end":18,"type":"D"}]}},{"acc":"P04275","features":{"pfam":[{"id":"PF00092","name":"von Willebrand factor type A domain","start":1277,"end":1449},{"id":"PF00092","name":"von Willebrand factor type A domain","start":1498,"end":1647},{"id":"PF00092","name":"von Willebrand factor type A domain","start":1691,"end":1860},{"id":"PF00093","name":"von Willebrand factor type C domain","start":2431,"end":2494},{"id":"PF00093","name":"von Willebrand factor type C domain","start":2582,"end":2644},{"id":"PF00094","name":"von Willebrand factor type D domain","start":35,"end":179},{"id":"PF00094","name":"von Willebrand factor type D domain","start":388,"end":540},{"id":"PF00094","name":"von Willebrand factor type D domain","start":867,"end":1011},{"id":"PF00094","name":"von Willebrand factor type D domain","start":1950,"end":2102},{"id":"PF01826","name":"Trypsin Inhibitor like cysteine rich domain","start":295,"end":348},{"id":"PF01826","name":"Trypsin Inhibitor like cysteine rich domain","start":652,"end":707},{"id":"PF08742","name":"C8 domain","start":224,"end":292},{"id":"PF08742","name":"C8 domain","start":584,"end":649},{"id":"PF08742","name":"C8 domain","start":1060,"end":1127},{"id":"PF08742","name":"C8 domain","start":2138,"end":2200},{"id":"PF16164","name":"VWA N-terminal","start":1198,"end":1276},{"id":"PF23244","name":"Von Willebrand factor-like domain","start":834,"end":860},{"id":"PF25962","name":"Otogelin-like/Mucin TIL domain","start":1142,"end":1196}],"gene3D":[]},"creator":"msalas","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MIPARFAGVLLALALILPGTLCAEGTRGRSSTARCSLFGSDFVNTFDGSMYSFAGYCSYLLAGGCQKRSFSIIGDFQNGKRVSLSVYLGEFFDIHLFVNGTVTQGDQRVSMPYASKGLYLETEAGYYKLSGEAYGFVARIDGSGNFQVLLSDRYFNKTCGLCGNFNIFAEDDFMTQEGTLTSDPYDFANSWALSSGEQWCERASPPSSSCNISSGEMQKGLWEQCQLLKSTSVFARCHPLVDPEPFVALCEKTLCECAGGLECACPALLEYARTCAQEGMVLYGWTDHSACSPVCPAGMEYRQCVSPCARTCQSLHINEMCQERCVDGCSCPEGQLLDEGLCVESTECPCVHSGKRYPPGTSLSRDCNTCICRNSQWICSNEECPGECLVTGQSHFKSFDNRYFTFSGICQYLLARDCQDHSFSIVIETVQCADDRDAVCTRSVTVRLPGLHNSLVKLKHGAGVAMDGQDVQLPLLKGDLRIQHTVTASVRLSYGEDLQMDWDGRGRLLVKLSPVYAGKTCGLCGNYNGNQGDDFLTPSGLAEPRVEDFGNAWKLHGDCQDLQKQHSDPCALNPRMTRFSEEACAVLTSPTFEACHRAVSPLPYLRNCRYDVCSCSDGRECLCGALASYAAACAGRGVRVAWREPGRCELNCPKGQVYLQCGTPCNLTCRSLSYPDEECNEACLEGCFCPPGLYMDERGDCVPKAQCPCYYDGEIFQPEDIFSDHHTMCYCEDGFMHCTMSGVPGSLLPDAVLSSPLSHRSKRSLSCRPPMVKLVCPADNLRAEGLECTKTCQNYDLECMSMGCVSGCLCPPGMVRHENRCVALERCPCFHQGKEYAPGETVKIGCNTCVCQDRKWNCTDHVCDATCSTIGMAHYLTFDGLKYLFPGECQYVLVQDYCGSNPGTFRILVGNKGCSHPSVKCKKRVTILVEGGEIELFDGEVNVKRPMKDETHFEVVESGRYIILLLGKALSVVWDRHLSISVVLKQTYQEKVCGLCGNFDGIQNNDLTSSNLQVEEDPVDFGNSWKVSSQCADTRKVPLDSSPATCHNNIMKQTMVDSSCRILTSDVFQDCNKLVDPEPYLDVCIYDTCSCESIGDCACFCDTIAAYAHVCAQHGKVVTWRTATLCPQSCEERNLRENGYECEWRYNSCAPACQVTCQHPEPLACPVQCVEGCHAHCPPGKILDELLQTCVDPEDCPVCEVAGRRFASGKKVTLNPSDPEHCQICHCDVVNLTCEACQEPGGLVVPPTDAPVSPTTLYVEDISEPPLHDFYCSRLLDLVFLLDGSSRLSEAEFEVLKAFVVDMMERLRISQKWVRVAVVEYHDGSHAYIGLKDRKRPSELRRIASQVKYAGSQVASTSEVLKYTLFQIFSKIDRPEASRITLLLMASQEPQRMSRNFVRYVQGLKKKKVIVIPVGIGPHANLKQIRLIEKQAPENKAFVLSSVDELEQQRDEIVSYLCDLAPEAPPPTLPPDMAQVTVGPGLLGVSTLGPKRNSMVLDVAFVLEGSDKIGEADFNRSKEFMEEVIQRMDVGQDSIHVTVLQYSYMVTVEYPFSEAQSKGDILQRVREIRYQGGNRTNTGLALRYLSDHSFLVSQGDREQAPNLVYMVTGNPASDEIKRLPGDIQVVPIGVGPNANVQELERIGWPNAPILIQDFETLPREAPDLVLQRCCSGEGLQIPTLSPAPDCSQPLDVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITTIDVPWNVVPEKAHLLSLVDVMQREGGPSQIGDALGFAVRYLTSEMHGARPGASKAVVILVTDVSVDSVDAAADAARSNRVTVFPIGIGDRYDAAQLRILAGPAGDSNVVKLQRIEDLPTMVTLGNSFLHKLCSGFVRICMDEDGNEKRPGDVWTLPDQCHTVTCQPDGQTLLKSHRVNCDRGLRPSCPNSQSPVKVEETCGCRWTCPCVCTGSSTRHIVTFDGQNFKLTGSCSYVLFQNKEQDLEVILHNGACSPGARQGCMKSIEVKHSALSVELHSDMEVTVNGRLVSVPYVGGNMEVNVYGAIMHEVRFNHLGHIFTFTPQNNEFQLQLSPKTFASKTYGLCGICDENGANDFMLRDGTVTTDWKTLVQEWTVQRPGQTCQPILEEQCLVPDSSHCQVLLLPLFAECHKVLAPATFYAICQQDSCHQEQVCEVIASYAHLCRTNGVCVDWRTPDFCAMSCPPSLVYNHCEHGCPRHCDGNVSSCGDHPSEGCFCPPDKVMLEGSCVPEEACTQCIGEDGVQHQFLEAWVPDHQPCQICTCLSGRKVNCTTQPCPTAKAPTCGLCEVARLRQNADQCCPEYECVCDPVSCDLPPVPHCERGLQPTLTNPGECRPNFTCACRKEECKRVSPPSCPPHRLPTLRKTQCCDEYECACNCVNSTVSCPLGYLASTATNDCGCTTTTCLPDKVCVHRSTIYPVGQFWEEGCDVCTCTDMEDAVMGLRVAQCSQKPCEDSCRSGFTYVLHEGECCGRCLPSACEVVTGSPRGDSQSSWKSVGSQWASPENPCLINECVRVKEEVFIQQRNVSCPQLEVPVCPSGFQLSCKTSACCPSCRCERMEACMLNGTVIGPGKTVMIDVCTTCRCMVQVGVISGFKLECRKTTCNPCPLGYKEENNTGECCGRCLPTACTIQLRGGQIMTLKRDETLQDGCDTHFCKVNERGEYFWEKRVTGCPPFDEHKCLAEGGKIMKIPGTCCDTCEEPECNDITARLQYVKVGSCKSEVEVDIHYCQGKCASKAMYSIDINDVQDQCSCCSPTRTEPMQVALHCTNGSVVYHEVLNAMECKCSPRKCSK","name":"von Willebrand factor","regions":[{"region_id":"DP02981r001","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-11-25T15:41:14.328Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":1493,"term_id":"IDPO:0000002","start":1478,"version":2,"statement":[{"text":"The crystal asymmetric unit contains three A2 molecules that are essentially identical and comprise residues 1,478–1,674; we do not observe interpretable density for amino-terminal residues 1,478–1,493, most likely because of flexibility.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-6352-1282","released":"2022_03","term_ontology":"IDPO","curator_name":"Martin Salas","reference_id":"21750539","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3ZQK"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"msalas","reference_html":"Calcium modulates force sensing by the von Willebrand factor A2 domain. <i> Jakobi AJ, Mashaghi A, Tans SJ, Huizinga EG. </i> Nat Commun, 2011","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_12","length":2813,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP02981","date":"2020-11-24T22:04:40.025Z","regions_counter":1,"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000046823","uniref100":"UniRef100_P04275","uniref90":"UniRef90_P04275","uniref50":"UniRef50_P04275","genes":[{"name":{"value":"VWF"},"synonyms":[{"value":"F8VWF"}]}],"disorder_content":0.005687877710629221,"disprot_consensus":{"full":[{"start":1478,"end":1493,"type":"D"}],"Structural state":[{"start":1478,"end":1493,"type":"D"}]}},{"acc":"O01479","features":{"pfam":[{"id":"PF03250","name":"Tropomodulin","start":33,"end":182},{"id":"PF27087","name":"TMOD/LMOD Leucine-rich domain","start":220,"end":379}],"gene3D":[]},"creator":"spenadias","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"sequence":"MSQAKTDYYSEEKTFSAPSANSQQGTQLPSKVYNKGLKDLEDNDIEGLLSSLSIDELEDLNNDFDPDNSMLPPSQRCRDQTDKEPTGPYKRDNLLKFLEDKAKTEKDWEDVCPYTPGQKRGKVYDSDSGRNSEEPENGKMEMPIEIDLDDDEEELECALVTAPEKDLVDLAGILGMHNVLNQPQYYNALKGKTQDESTGTTFNGIMQSYVPRIVPDEPDNDTDVESCINRLREDDTDLKEVNINNMKRVSKERIRSLIEAACNSKHIEKFSLANTAISDSEARGLIELIETSPSLRVLNVESNFLTPELLARLLRSTLVTQSIVEFKADNQRQSVLGNQVEMDMMMAIEENESLLRVGISFASMEARHRVSEALERNYERVRLRRLGKDPNV","name":"Tropomodulin","regions":[{"region_id":"DP02982r001","validated":{"curator_id":"fquaglia","timestamp":"2020-11-25T16:23:01.585Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":221,"term_id":"IDPO:0000002","start":196,"version":2,"statement":[{"text":"A large part of the N-terminus, including residues 196–221, is completely disordered, which was also observed in the homologous structure 1IO0","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-2902-823X","released":"2022_03","term_ontology":"IDPO","curator_name":"Samuel Peña Díaz","reference_id":"15211521","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1PGV"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"spenadias","reference_html":"Structural genomics of Caenorhabditis elegans: crystal structure of the tropomodulin C-terminal domain. <i> Lu S, Symersky J, Li S, Carson M, Chen L, Meehan E, Luo M. </i> Proteins, 2004","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":392,"ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","disprot_id":"DP02982","date":"2020-11-25T11:55:37.432Z","regions_counter":1,"dataset":[],"UniParc":"UPI00000749DC","uniref100":"UniRef100_O01479","uniref90":"UniRef90_O01479","uniref50":"UniRef50_O01479","genes":[{"name":{"value":"unc-94"},"synonyms":[{"value":"tmd-1"}],"orfNames":[{"value":"C06A5.7"}]}],"alphafold_very_low_content":0.1096938775510204,"disorder_content":0.0663265306122449,"disprot_consensus":{"full":[{"start":196,"end":221,"type":"D"}],"Structural state":[{"start":196,"end":221,"type":"D"}]}},{"acc":"Q9DEA6","features":{"pfam":[{"id":"PF03250","name":"Tropomodulin","start":1,"end":129},{"id":"PF27087","name":"TMOD/LMOD Leucine-rich domain","start":165,"end":324}],"gene3D":[]},"creator":"spenadias","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Phasianinae","Gallus"],"sequence":"EDKILGALTEEELRKLENELEELDPDNALLPAGLRQRDQTQKPPTGPFKREELMAHLEQQAKDIKDREDLVPFTGEKRGKAWIPKQKPMDPVLESVTLEPELEEALANASDAELCDIAAILGMHTLMSNQQYYEALGSSTIVNKEGLNSVIKPTKYKPVPDEEPNSTDVEETLKRIQNNDPDLEEVNLNNIMNIPVPTLKACAEALKTNTYVKKFSIVGTRSNDPVAFALAEMLKVNNTLKSLNVESNFISGSGILALVEALQSNTSLIELRIDNQSQPLGNNVEMEIANMLEKNTTLLKFGYHFTQQGPRLRASNAMMNNNDLVRKRRLAELNGPIFPKCRTGV","name":"Tropomodulin","regions":[{"region_id":"DP02983r001","validated":{"curator_id":"fquaglia","timestamp":"2020-11-25T16:21:58.637Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":164,"term_id":"IDPO:0000002","start":146,"version":2,"statement":[{"text":"The first N-terminal 19 residues, Gly160–Pro178, do not give any clear electron density, and these are likely to be flexible and disordered.","type":"Results"},{"text":"Gly160 and Pro178 in this construct correspond to Gly146 and Pro164 in Tropomodulin real sequence.","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-2902-823X","released":"2022_03","term_ontology":"IDPO","curator_name":"Samuel Peña Díaz","reference_id":"12414704","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1IO0"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"spenadias","reference_html":"Crystal structure of the C-terminal half of tropomodulin and structural basis of actin filament pointed-end capping. <i> Krieger I, Kostyukova A, Yamashita A, Nitanai Y, Maéda Y. </i> Biophys J, 2002","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":345,"ncbi_taxon_id":9031,"organism":"Gallus gallus","disprot_id":"DP02983","date":"2020-11-25T12:20:19.951Z","regions_counter":1,"dataset":[],"UniParc":"UPI00000FCBBA","uniref100":"UniRef100_Q9DEA6","uniref90":"UniRef90_F1NY71","uniref50":"UniRef50_F1NY71","genes":[{"name":{"value":"E-Tmod","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAB18913.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAB18913.1"}}]}}],"alphafold_very_low_content":0.017391304347826087,"disorder_content":0.05507246376811594,"disprot_consensus":{"full":[{"start":146,"end":164,"type":"D"}],"Structural state":[{"start":146,"end":164,"type":"D"}]}},{"acc":"P09446","features":{"pfam":[{"id":"PF00012","name":"Hsp70 protein","start":6,"end":613}],"gene3D":[]},"creator":"spenadias","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"sequence":"MSKHNAVGIDLGTTYSCVGVFMHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPHNTVFDAKRLIGRKFDDPAVQSDMKHWPFKVISAEGAKPKVQVEYKGENKIFTPEEISSMVLLKMKETAEAFLGTTVKDAVVTVPAYFNDSQRQATKDAGAIAGLNVLRIINEPTAAAIAYGLDKKGHGERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFCAEFKRKHKKDLASNPRALRRLRTACERAKRTLSSSSQASIEIDSLFEGIDFYTNITRARFEELCADLFRSTMDPVEKSLRDAKMDKSQVHDIVLVGGSTRIPKVQKLLSDLFSGKELNKSINPDEAVAYGAAVQAAILSGDKSEAVQDLLLLDVAPLSLGIETAGGVMTALIKRNTTIPTKTAQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELSGIPPAPRGVPQIEVTFDIDANGILNVSATDKSTGKQNKITITNDKGRLSKDDIERMVNEAEKYKADDEAQKDRIGAKNGLESYAFNLKQTIEDEKLKDKISPEDKKKIEDKCDEILKWLDSNQTAEKEEFEHQQKDLEGLANPIISKLYQSAGGAPPGAAPGGAAGGAGGPTIEEVD","name":"Heat shock protein hsp-1","regions":[{"region_id":"DP02984r001","validated":{"curator_id":"fquaglia","timestamp":"2020-11-25T16:35:37.808Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":640,"term_id":"IDPO:0000002","start":615,"version":2,"statement":[{"text":"In accordance with solution studies of E. coli DnaK [16] and the crystal structure of rat Hsc70 [14], the final 26 C terminal residues were found to be disordered","type":"Results"},{"text":"The complete sequence of the construct used was mgsshhhhhhssGLVPRGSHMASGLESYAFNLKQTIEDEKLKDKISPEDKKKIEDKCDEILKWLDSNQTAEKEEFEHQQKDLEGLANPIISKLYQSaggappgaapggaaggaggptieevd; recombinant tag residues in italic, disordered residues in lowercase.","type":"Figure"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-2902-823X","released":"2022_03","term_ontology":"IDPO","curator_name":"Samuel Peña Díaz","reference_id":"17407764","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2P32"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"spenadias","reference_html":"Crystal structure of the C-terminal three-helix bundle subdomain of C. elegans Hsp70. <i> Worrall LJ, Walkinshaw MD. </i> Biochem Biophys Res Commun, 2007","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":640,"ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","disprot_id":"DP02984","date":"2020-11-25T14:47:27.861Z","regions_counter":1,"dataset":["Stress response proteins"],"UniParc":"UPI000012CC87","uniref100":"UniRef100_P09446","uniref90":"UniRef90_P09446","uniref50":"UniRef50_P09446","genes":[{"name":{"value":"hsp-1","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"F26D10.3","url":"https://www.wormbase.org/db/seq/sequence?name=F26D10.3;class=Transcript"}}]},"synonyms":[{"value":"hsp70a","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"2841196","url":"http://www.ncbi.nlm.nih.gov/pubmed/2841196","alternativeUrl":"https://europepmc.org/abstract/MED/2841196"}}]}],"orfNames":[{"value":"F26D10.3","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"F26D10.3","url":"https://www.wormbase.org/db/seq/sequence?name=F26D10.3;class=Transcript"}}]}]}],"alphafold_very_low_content":0.05,"disorder_content":0.040625,"disprot_consensus":{"full":[{"start":615,"end":640,"type":"D"}],"Structural state":[{"start":615,"end":640,"type":"D"}]}},{"acc":"P0A6Y8","features":{"pfam":[{"id":"PF00012","name":"Hsp70 protein","start":4,"end":602}],"gene3D":[]},"creator":"spenadias","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"sequence":"MGKIIGIDLGTTNSCVAIMDGTTPRVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQRDVSIMPFKIIAADNGDAWVEVKGQKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGLEVKRIINEPTAAALAYGLDKGTGNRTIAVYDLGGGTFDISIIEIDEVDGEKTFEVLATNGDTHLGGEDFDSRLINYLVEEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDLVNRSIEPLKVALQDAGLSVSDIDDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTGDVKDVLLLDVTPLSLGIETMGGVMTTLIAKNTTIPTKHSQVFSTAEDNQSAVTIHVLQGERKRAADNKSLGQFNLDGINPAPRGMPQIEVTFDIDADGILHVSAKDKNSGKEQKITIKASSGLNEDEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPADDKTAIESALTALETALKGEDKAAIEAKMQELAQVSQKLMEIAQQQHAQQQTAGADASANNAKDDDVVDAEFEEVKDKK","name":"Chaperone protein DnaK","regions":[{"region_id":"DP02985r001","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T15:39:51.053Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":638,"term_id":"IDPO:0000002","start":606,"version":2,"statement":[{"text":"The domain was shown to be comprised of a rigid structure consisting of four helices and a flexible C-terminal subdomain of approximately 33 amino acids. The mobility of the flexible region is maintained in the context of the full-length protein and does not appear to be modulated by the nucleotide state.","type":"Abstract"},{"text":"In addition, the last 33 amino acids constitute a highly flexible subdomain of the molecule.","type":"Introduction"},{"text":"In contrast to the apparently rigid structure of the helical portion of the molecule, the carboxy-terminal 33 residues are highly flexible.","type":"Discussion"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0002-2902-823X","released":"2022_03","term_ontology":"IDPO","curator_name":"Samuel Peña Díaz","reference_id":"10048327","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"spenadias","reference_html":"Topology and dynamics of the 10 kDa C-terminal domain of DnaK in solution. <i> Bertelsen EB, Zhou H, Lowry DF, Flynn GC, Dahlquist FW. </i> Protein Sci, 1999","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":638,"ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","disprot_id":"DP02985","date":"2020-11-25T15:56:50.784Z","regions_counter":1,"dataset":["Stress response proteins"],"UniParc":"UPI00001295C4","uniref100":"UniRef100_A7ZHA4","uniref90":"UniRef90_A7MIK5","uniref50":"UniRef50_Q5ZTY3","genes":[{"name":{"value":"dnaK"},"synonyms":[{"value":"groP"},{"value":"grpF"},{"value":"seg"}],"olnNames":[{"value":"b0014"},{"value":"JW0013"}]}],"alphafold_very_low_content":0.03134796238244514,"disorder_content":0.05172413793103448,"disprot_consensus":{"full":[{"start":606,"end":638,"type":"D"}],"Structural state":[{"start":606,"end":638,"type":"D"}]}},{"acc":"P63018","features":{"pfam":[{"id":"PF00012","name":"Hsp70 protein","start":6,"end":612}],"gene3D":[]},"creator":"tcordero","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"sequence":"MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIISWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD","name":"Heat shock cognate 71 kDa protein","regions":[{"region_id":"DP02986r001","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T15:40:34.721Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":646,"term_id":"IDPO:0000002","start":622,"version":2,"statement":[{"text":"The remaining residues of the four molecules, A621–A646, B619–B646, C622–C646, and D615–D646, could not be traced due to their poor electron density maps.","type":"Methods"},{"text":"The numbering of the IDR refers to chain C","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-2902-823X","released":"2022_03","term_ontology":"IDPO","curator_name":"Samuel Peña Díaz","reference_id":"12773536","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1UD0"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"spenadias","reference_html":"Crystal structure of the C-terminal 10-kDa subdomain of Hsc70. <i> Chou CC, Forouhar F, Yeh YH, Shr HL, Wang C, Hsiao CD. </i> J Biol Chem, 2003","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":622,"end":646,"reference_id":"12773536","reference_source":"pmid","reference_html":"Crystal structure of the C-terminal 10-kDa subdomain of Hsc70. <i> Chou CC, Forouhar F, Yeh YH, Shr HL, Wang C, Hsiao CD. </i> J Biol Chem, 2003","date":"2026-05-12T15:05:09.789Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":549,"end":549,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":617,"end":617,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":621,"end":621,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"1UD0"}],"region_id":"DP02986r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29101","entry_name":null}],"statement":[{"text":"he remaining residues of the four molecules, A621–A646, B619–B646, C622–C646, and D615–D646, could not be traced due to their poor electron density maps.","type":"Methods"}]}],"released":"2020_12","length":646,"ncbi_taxon_id":10116,"organism":"Rattus norvegicus","disprot_id":"DP02986","date":"2020-11-25T18:38:56.056Z","regions_counter":4,"dataset":["Stress response proteins"],"UniParc":"UPI00000018A6","uniref100":"UniRef100_P63017","uniref90":"UniRef90_P63017","uniref50":"UniRef50_P0DMV8","genes":[{"name":{"value":"Hspa8","evidences":[{"code":"ECO:0000312","source":{"name":"RGD","id":"621725","url":"https://rgd.mcw.edu/tools/genes/genes_view.cgi?id=621725"}}]},"synonyms":[{"value":"Hsc70"},{"value":"Hsc73"}]}],"alphafold_very_low_content":0.05263157894736842,"disorder_content":0.03869969040247678,"disprot_consensus":{"full":[{"start":622,"end":646,"type":"D"}],"Structural state":[{"start":622,"end":646,"type":"D"}],"Disorder function":[{"start":622,"end":646,"type":"F"}]}},{"acc":"Q22942","features":{"pfam":[{"id":"PF01633","name":"Choline/ethanolamine kinase","start":78,"end":416}],"gene3D":[]},"creator":"spenadias","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"sequence":"MSSRKVSRAHYDEDELASAANMSLVAEGHFRGMKELLSTMDLDTDANTIPELKERAHMLCARFLGGAWKTVPLEHLRISRIKGGMSNMLFLCRLSEVYPPIRNEPNKVLLRVYFNPETESHLVAESVIFTLLSERHLGPKLYGIFSGGRLEEYIPSRPLSCHEISLAHMSTKIAKRVAKVHQLEVPIWKEPDYLCEALQRWLKQLTGTVDAEHRFDLPEECGVSSVNCLDLARELEFLRAHISLSKSPVTFCHNDLQEGNILLPKASSGNIRMPSLSDETQALGNSLSAFNPADPRLVLIDFEYASYNYRAFDFANHFIEWTIDYDIDEAPFYKIQTENFPENDQMLEFFLNYLREQGNTRENELYKKSEDLVQETLPFVPVSHFFWGVWGLLQVELSPVGFGFADYGRDRLSLYFKHKQLLKNLASHQ","name":"Choline kinase A2","regions":[{"region_id":"DP02987r001","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T15:16:25.757Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":31,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"The N terminus of the protein begins with 31 unobserved and presumably disordered residues, followed by a small subdomain that contains two helices","type":"Results"},{"text":"The final model includes residues 32–265 and residues 296–426 for subunit A, residues 40–265 and residues 296–426 for subunit B, one calcium ion for each subunit, and a total of 342 water molecules. Residues not included in the model are Caenorhabditis elegans: cloning, expression, purification, and those that are not visible and assumed to be disordered.","type":"Methods"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-2902-823X","released":"2022_03","term_ontology":"IDPO","curator_name":"Samuel Peña Díaz","reference_id":"12791258","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1NW1"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"spenadias","reference_html":"The crystal structure of choline kinase reveals a eukaryotic protein kinase fold. <i> Peisach D, Gee P, Kent C, Xu Z. </i> Structure, 2003","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02987r002","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T15:16:27.274Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":296,"term_id":"IDPO:0000002","start":265,"version":2,"statement":[{"text":"In addition, strands 10 and 11 are connected by a long stretch of sequence (residues 265– 296) that appears to extend away from the core structure. Since there is no electron density observed for this sequence, it is assumed to be disordered","type":"Results"},{"text":"The final model includes residues 32–265 and residues 296–426 for subunit A, residues 40–265 and residues 296–426 for subunit B, one calcium ion for each subunit, and a total of 342 water molecules. Residues not included in the model are Caenorhabditis elegans: cloning, expression, purification, and those that are not visible and assumed to be disordered.","type":"Methods"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-2902-823X","released":"2022_03","term_ontology":"IDPO","curator_name":"Samuel Peña Díaz","reference_id":"12791258","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1NW1"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"spenadias","reference_html":"The crystal structure of choline kinase reveals a eukaryotic protein kinase fold. <i> Peisach D, Gee P, Kent C, Xu Z. </i> Structure, 2003","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":429,"ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","disprot_id":"DP02987","date":"2020-11-26T07:49:55.030Z","regions_counter":2,"dataset":[],"UniParc":"UPI000017B85E","uniref100":"UniRef100_Q22942","uniref90":"UniRef90_Q22942","uniref50":"UniRef50_Q22942","genes":[{"name":{"value":"cka-2","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"C52B9.1a","url":"https://www.wormbase.org/db/seq/sequence?name=C52B9.1a;class=Transcript"}}]},"orfNames":[{"value":"C52B9.1","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"C52B9.1a","url":"https://www.wormbase.org/db/seq/sequence?name=C52B9.1a;class=Transcript"}}]}]}],"alphafold_very_low_content":0.10256410256410256,"disorder_content":0.14685314685314685,"disprot_consensus":{"full":[{"start":1,"end":31,"type":"D"},{"start":265,"end":296,"type":"D"}],"Structural state":[{"start":1,"end":31,"type":"D"},{"start":265,"end":296,"type":"D"}]}},{"acc":"P34704","features":{"pfam":[{"id":"PF09232","name":"Caenorhabditis elegans Her-1","start":22,"end":165}],"gene3D":[]},"creator":"spenadias","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"sequence":"MRYLPIFVFLGSFGYTETTLTKELIKDAAEKCCTRNRQECCIEIMKFGTPIRCGYDRDPKLPGYVYKCLQNVLFAKEPKKKINLDDSVCCSVFGNDQNDSGRRCENRCKNLMTSPSIDAATRLDSIKSCSLLDNVLYKCFEKCRSLRKDGIKIEVLQFEEYCNATFIQKRTFRGV","name":"Protein her-1","regions":[{"region_id":"DP02988r001","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T14:56:27.870Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":175,"term_id":"IDPO:0000002","start":165,"version":2,"statement":[{"text":"The final model includes all of the HER-1GM sequence except 11 C-terminal residues (165–175) for which electron density was not interpretable.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-2902-823X","released":"2022_03","term_ontology":"IDPO","curator_name":"Samuel Peña Díaz","reference_id":"15289613","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1SZH"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"spenadias","reference_html":"Crystal structure of Caenorhabditis elegans HER-1 and characterization of the interaction between HER-1 and TRA-2A. <i> Hamaoka BY, Dann CE, Geisbrecht BV, Leahy DJ. </i> Proc Natl Acad Sci U S A, 2004","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":175,"ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","disprot_id":"DP02988","date":"2020-11-26T09:11:42.084Z","regions_counter":1,"dataset":[],"UniParc":"UPI000012C613","uniref100":"UniRef100_P34704","uniref90":"UniRef90_P34704","uniref50":"UniRef50_P34704","genes":[{"name":{"value":"her-1"},"orfNames":[{"value":"ZK287.8"}]}],"alphafold_very_low_content":0.08571428571428572,"disorder_content":0.06285714285714286,"disprot_consensus":{"full":[{"start":165,"end":175,"type":"D"}],"Structural state":[{"start":165,"end":175,"type":"D"}]}},{"acc":"Q03611","features":{"pfam":[{"id":"PF00027","name":"Cyclic nucleotide-binding domain","start":512,"end":602},{"id":"PF00520","name":"Ion transport protein","start":122,"end":419},{"id":"PF16526","name":"C-terminal leucine zipper domain of cyclic nucleotide-gated channels","start":609,"end":675}],"gene3D":[]},"creator":"spenadias","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"sequence":"MSTAEPAPDPTNPSTSGLAPTTNGIGSPPPTASAATKFSILTKFLRRKNQVHTTTAQQNEFMQKYMPNGNSNAVQPAATGGQPASSDGGSAIEVPPPKESYAVRIRKYLANYTQDPSTDNFYYWTCVVTVAYIYNLLFVIARQVFNDLIGPSSQSLCRFYNGTLNSTTQVECTYNMLTNMKEMPTYSQYPDLGWSKYWHFRMLWVFFDLLMDCVYLIDTFLNYRMGYMDQGLVVREAEKVTKAYWQSKQYRIDGISLIPLDYILGWPIPYINWRGLPILRLNRLIRYKRVRNCLERTETRSSMPNAFRVVVVVWYIVIIIHWNACLYFWISEWIGLGTDAWVYGHLNKQSLPDDITDTLLRRYVYSFYWSTLILTTIGEVPSPVRNIEYAFVTLDLMCGVLIFATIVGNVGSMISNMSAARTEFQNKMDGIKQYMELRKVSKQLEIRVIKWFDYLWTNKQSLSDQQVLKVLPDKLQAEIAMQVHFETLRKVRIFQDCEAGLLAELVLKLQLQVFSPGDFICKKGDIGREMYIVKRGRLQVVDDDGKKVFVTLQEGSVFGELSILNIAGSKNGNRRTANVRSVGYTDLFVLSKTDLWNALREYPDARKLLLAKGREILKKDNLLDENAPEEQKTVEEIAEHLNNAVKVLQTRMARLIVEHSSTEGKLMKRIEMLEKHLSRYKALARRQKTMHGVSIDGGDISTDGVDERVRPPRLRQTKTIDLPTGTESESLLK","name":"Cyclic nucleotide-gated cation channel","regions":[{"region_id":"DP02989r001","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T15:02:53.575Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":105,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"Residues M1 to I105 and N621 to K733, which constitute most of the amino terminus and the distal C terminus beyond the CNBD, respectively, were not modelled because their densities were weak or missing.","type":"Results"},{"text":"The density of residues 1–105 was missing in the map","type":"Methods"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-2902-823X","released":"2022_03","term_ontology":"IDPO","curator_name":"Samuel Peña Díaz","reference_id":"28099415","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5H3O"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"spenadias","reference_html":"Structure of a eukaryotic cyclic-nucleotide-gated channel. <i> Li M, Zhou X, Wang S, Michailidis I, Gong Y, Su D, Li H, Li X, Yang J. </i> Nature, 2017","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02989r002","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T15:02:54.868Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":733,"term_id":"IDPO:0000002","start":621,"version":2,"statement":[{"text":"Residues M1 to I105 and N621 to K733, which constitute most of the amino terminus and the distal C terminus beyond the CNBD, respectively, were not modelled because their densities were weak or missing.","type":"Results"},{"text":"Residues 621–733 were not visible in the density map. There was weak density under the C-linker/CNBD region. This density could represent the coiled coil region, but it was too weak for model building.","type":"Methods"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-2902-823X","released":"2022_03","term_ontology":"IDPO","curator_name":"Samuel Peña Díaz","reference_id":"28099415","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5H3O"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"spenadias","reference_html":"Structure of a eukaryotic cyclic-nucleotide-gated channel. <i> Li M, Zhou X, Wang S, Michailidis I, Gong Y, Su D, Li H, Li X, Yang J. </i> Nature, 2017","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02989r003","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T14:59:45.758Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":103,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"Residues M1 to V103 (N terminus), G162 to L164, and D620 to K733 (distal C terminus) were not modeled because of weak or missing densities.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-2902-823X","released":"2022_03","term_ontology":"IDPO","curator_name":"Samuel Peña Díaz","reference_id":"32483338","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6WEL"},{"db":"PDB","id":"6WEJ"},{"db":"PDB","id":"6WEK"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"spenadias","reference_html":"Mechanism of ligand activation of a eukaryotic cyclic nucleotide-gated channel. <i> Zheng X, Fu Z, Su D, Zhang Y, Li M, Pan Y, Li H, Li S, Grassucci RA, Ren Z, Hu Z, Li X, Zhou M, Li G, Frank J, Yang J. </i> Nat Struct Mol Biol, 2020","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02989r004","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T14:59:46.956Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":733,"term_id":"IDPO:0000002","start":620,"version":2,"statement":[{"text":"Residues M1 to V103 (N terminus), G162 to L164, and D620 to K733 (distal C terminus) were not modeled because of weak or missing densities.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-2902-823X","released":"2022_03","term_ontology":"IDPO","curator_name":"Samuel Peña Díaz","reference_id":"32483338","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6WEL"},{"db":"PDB","id":"6WEJ"},{"db":"PDB","id":"6WEK"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"spenadias","reference_html":"Mechanism of ligand activation of a eukaryotic cyclic nucleotide-gated channel. <i> Zheng X, Fu Z, Su D, Zhang Y, Li M, Pan Y, Li H, Li S, Grassucci RA, Ren Z, Hu Z, Li X, Zhou M, Li G, Frank J, Yang J. </i> Nat Struct Mol Biol, 2020","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":733,"ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","disprot_id":"DP02989","date":"2020-11-26T09:20:57.437Z","regions_counter":4,"dataset":[],"UniParc":"UPI0000127C24","uniref100":"UniRef100_Q03611","uniref90":"UniRef90_Q03611","uniref50":"UniRef50_Q03611","genes":[{"name":{"value":"tax-4"},"orfNames":[{"value":"ZC84.2"}]}],"alphafold_very_low_content":0.1869031377899045,"disorder_content":0.2987721691678035,"disprot_consensus":{"full":[{"start":1,"end":105,"type":"D"},{"start":620,"end":733,"type":"D"}],"Structural state":[{"start":1,"end":105,"type":"D"},{"start":620,"end":733,"type":"D"}]}},{"acc":"Q9U489","features":{"pfam":[{"id":"PF00630","name":"Filamin/ABP280 repeat","start":694,"end":813},{"id":"PF01436","name":"NHL repeat","start":845,"end":872},{"id":"PF01436","name":"NHL repeat","start":892,"end":919},{"id":"PF01436","name":"NHL repeat","start":939,"end":966},{"id":"PF01436","name":"NHL repeat","start":987,"end":1013},{"id":"PF01436","name":"NHL repeat","start":1035,"end":1062},{"id":"PF01436","name":"NHL repeat","start":1120,"end":1147}],"gene3D":[]},"creator":"spenadias","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"sequence":"MATIVPCSLEKEEGAPSGPRRLQTEIDVDANDSGNELSMGGSSSEGDSMSHHRGEHSPNHHHQDNHLGSGPPPPQFTGSLFDTPPSMIQSPQQQPQFQFNTGFGLGLPQDSFRCSVCSKSSTIGVLPFVCAHKTCQSCYQMTPSSYDRRACKLCGAVSTATANFTSQMYLSPTLPSPPRGALMSDCSTPTMNNHINSSTPLHQPRAFSFSLSGMPGSPSPVMGARMPSSAGGLMMRPIGFPDSDSSLTSWSPLQQPSQLSINNLSSIGGHQQQSPMLMQNVFDSLAVNDDTPVFSPLSPTNTSMHMPPSLMASPDVPKHSATIAPPRNSMCSTPRLQLATPMSSQSQQTFPIPSPLGSQPQQQQPMGPIQCQGCESKISFAYCMQCQEALCIHCVQAHQRVRATKQHAFVELQQLMATLMSRAVQPQQAQQYTQNVGGSVRQALGSVGSGDVFFSGHVSGVENDSIGSGESSPRSSSVCGTHDSVIIGICENCPHSVLLCAICVAQHPGKHRVQPLGDIRVAVGEVVNESQLLQWQCEKTGDTIKQIIDGIVTNATTAENEIRAAFDTHVNALEERRKELLKRVETVKNLKLSVLISQAESLQSKQIDLQQAIQTATKLMDSSDCDEMVLRQVFEKLASCQMGNEGTEPNNNILNVLMLACQVNEDDRLKFTAPQDGILLNKARQFGNIESGPCAKNSSIVGDSFKKAIRERQTVIYVQLRDACGDLLSSSIAATQPTSQALLPHQEPHSHLEQAMPTSDVQAFVISPDGSTVEVTMTPRENGIVALSYYPSIEGSYTLNILVKGTPISGCPTTMDIRRGRNYDEIAAKGPILTFGKEGSGDGELCRPWGICVDQRGRVIVADRSNNRVQIFDKDGNFISKFGTSGNRPGQFDRPAGITTNSLNNIVVADKDNHRVQVFDENGMFLLKFGDRGRAVGYFNYPWGVATNSHNAIAVSDTRNHRVQIFTPQGQFVRKCGFDSAYFFKNLDSPRGLCYLPDGQLLITDFNNHRLAVLSPRNMSEMKVYGSEGDGDGMFVRPQGVVIDPEGHILVCDSRNNRVQVFASDDMRFIGSFGLGPVPNSGFQMPQELPAPYSSLGGPFGAPAFSSAPTPLTPSPRQLLDRPTDLAVGPDGRIYVVDFGNNCIRVF","name":"Protein lin-41","regions":[{"region_id":"DP02990r001","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T15:14:45.937Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":757,"term_id":"IDPO:0000002","start":730,"version":2,"statement":[{"text":"The final crystallographic model encompasses residues 691–729 and 758–820, whereas a long insert (730–757) that is only found in Caenorhabditis LIN-41 protein sequences could not be built due to high flexibility.","type":"Results"},{"text":"The disordered sequence stretch 730–757 which is not included in the model is displayed as grey dots.","type":"Figure"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-2902-823X","released":"2022_03","term_ontology":"IDPO","curator_name":"Samuel Peña Díaz","reference_id":"25167051","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4UMG"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"spenadias","reference_html":"The TRIM-NHL protein LIN-41 controls the onset of developmental plasticity in Caenorhabditis elegans. <i> Tocchini C, Keusch JJ, Miller SB, Finger S, Gut H, Stadler MB, Ciosk R. </i> PLoS Genet, 2014","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":1147,"ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","disprot_id":"DP02990","date":"2020-11-26T09:37:45.624Z","regions_counter":1,"dataset":["RNA-binding proteins"],"UniParc":"UPI0000075D8E","uniref100":"UniRef100_Q9U489","uniref90":"UniRef90_Q9U489","uniref50":"UniRef50_Q9U489","genes":[{"name":{"value":"lin-41","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"C12C8.3a","url":"https://www.wormbase.org/db/seq/sequence?name=C12C8.3a;class=Transcript"}}]},"orfNames":[{"value":"C12C8.3","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"C12C8.3a","url":"https://www.wormbase.org/db/seq/sequence?name=C12C8.3a;class=Transcript"}}]}]}],"alphafold_very_low_content":0.4350479511769834,"disorder_content":0.024411508282476024,"disprot_consensus":{"full":[{"start":730,"end":757,"type":"D"}],"Structural state":[{"start":730,"end":757,"type":"D"}]}},{"acc":"Q9XTW2","features":{"pfam":[{"id":"PF06702","name":"Golgi casein kinase, C-terminal, Fam20","start":132,"end":477}],"gene3D":[]},"creator":"spenadias","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"sequence":"MRCNIKRLFTLAIGVFAATLVIISFSKDNYEREWKQGPQSNEARAVGHQSPDLFPVGQNSLPHQPIPPSLGEKDLSDPFNFLFSSNKITLRKLYDLTKNVDFDQLRQNECKKNITLSKFWEKSEQRNVPEDDNWERFYSNIGSCSVYSDDQMIDNLLHDLNTSPIKHVHIMDGGTQVKFVFTFKNDKQAVFKPMRFGRDYESDPNHFYFSDFERHHAEIATFHLDRVLGFRRAIPTVGRVLNMTTELFEKAEKKLKKTFFFSPAKNFCFVSRCDYYCDTTHAICGLPDMKEGSVQVFLPDESAVPRKHNRSPYRRTYSKKNQVAEWQSSMNYCTDKVKTKRQYAHGRRLLDLVDIHILDYLIGNQDRHHFESFNVFNDLPSYAIHLDHGRAFGRSDFDDDDIILPLRQCCILRPSTFQTLMNFYSTPKSLTKALHESLSKDPAHPILAYKHYPAMERRLAKIMSHILECFESRGVAEVLVAEYNNPDVSDAEQNDEEQSEEHQDKKDDKKTV","name":"Extracellular serine/threonine protein kinase CeFam20","regions":[{"region_id":"DP02991r001","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T15:07:59.326Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":129,"term_id":"IDPO:0000002","start":120,"version":2,"statement":[{"text":"The C-terminal 25 residues are missing from all four molecules and are presumably disordered. Residues 120–129 have poor electron densities and are built in only one molecule","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-2902-823X","released":"2022_03","term_ontology":"IDPO","curator_name":"Samuel Peña Díaz","reference_id":"23754375","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4KQB"},{"db":"PDB","id":"4KQA"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"spenadias","reference_html":"Crystal structure of the Golgi casein kinase. <i> Xiao J, Tagliabracci VS, Wen J, Kim SA, Dixon JE. </i> Proc Natl Acad Sci U S A, 2013","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02991r002","validated":{"curator_id":"fquaglia","timestamp":"2020-11-26T15:08:00.044Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":512,"term_id":"IDPO:0000002","start":488,"version":2,"statement":[{"text":"The C-terminal 25 residues are missing from all four molecules and are presumably disordered. Residues 120–129 have poor electron densities and are built in only one molecule","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-2902-823X","released":"2022_03","term_ontology":"IDPO","curator_name":"Samuel Peña Díaz","reference_id":"23754375","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4KQB"},{"db":"PDB","id":"4KQA"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"spenadias","reference_html":"Crystal structure of the Golgi casein kinase. <i> Xiao J, Tagliabracci VS, Wen J, Kim SA, Dixon JE. </i> Proc Natl Acad Sci U S A, 2013","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":512,"ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","disprot_id":"DP02991","date":"2020-11-26T10:46:08.774Z","regions_counter":2,"dataset":[],"UniParc":"UPI000004E688","uniref100":"UniRef100_Q9XTW2","uniref90":"UniRef90_Q9XTW2","uniref50":"UniRef50_Q9XTW2","genes":[{"name":{"value":"famk-1","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"H03A11.1","url":"https://www.wormbase.org/db/seq/sequence?name=H03A11.1;class=Transcript"}}]},"orfNames":[{"value":"H03A11.1","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"H03A11.1","url":"https://www.wormbase.org/db/seq/sequence?name=H03A11.1;class=Transcript"}}]}]}],"alphafold_very_low_content":0.107421875,"disorder_content":0.068359375,"disprot_consensus":{"full":[{"start":120,"end":129,"type":"D"},{"start":488,"end":512,"type":"D"}],"Structural state":[{"start":120,"end":129,"type":"D"},{"start":488,"end":512,"type":"D"}]}},{"acc":"Q9RFD6","features":{"pfam":[{"id":"PF00142","name":"4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family","start":34,"end":294}],"gene3D":[]},"creator":"jssuarez","taxonomy":["Bacteria","Proteobacteria","Alphaproteobacteria","Rhodobacterales","Rhodobacteraceae","Luteovulum"],"sequence":"MSPKDLTIPTGADGEGSVQVHLDEADKITGAKVFAVYGKGGIGKSTTSSNLSAAFSILGKRVLQIGCDPKHDSTFTLTGSLVPTVIDVLKDVDFHPEELRPEDFVFEGFNGVMCVEAGGPPAGTGCGGYVVGQTVKLLKQHHLLDDTDVVIFDVLGDVVCGGFAAPLQHADQAVVVTANDFDSIYAMNRIIAAVQAKSKNYKVRLAGCVANRSRATDEVDRFCKETNFRRLAHMPDLDAIRRSRLKKKTLFEMDEDQDVLAARAEYIRLAESLWRGLDPIDPHSLPDRDIFELLGFD","name":"Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein","regions":[{"region_id":"DP02993r001","unpublished":true,"ec_ontology":"ECO","end":29,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"The N-terminus (1-29)\non both the subunits was not resolved in electron density\nmaps even after several rounds of refinement. ","type":"Methods"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"19006326","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3FWY"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"jssuarez","reference_html":"Crystal structure of the L protein of Rhodobacter sphaeroides light-independent protochlorophyllide reductase with MgADP bound: a homologue of the nitrogenase Fe protein. <i> Sarma R, Barney BM, Hamilton TL, Jones A, Seefeldt LC, Peters JW. </i> Biochemistry, 2008","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":29,"term_name":"disorder to order","reference_html":"The flexible N-terminus of BchL autoinhibits activity through interaction with its [4Fe-4S] cluster and released upon ATP binding. <i> Corless EI, Saad Imran SM, Watkins MB, Bacik JP, Mattice JR, Patterson A, Danyal K, Soffe M, Kitelinger R, Seefeldt LC, Origanti S, Bennett B, Bothner B, Ando N, Antony E. </i> J Biol Chem, 2021","start":16,"region_id":"DP02993r002","term_id":"IDPO:0000011","unpublished":true,"version":2,"curator_id":"jssuarez","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","ec_name":"x-ray crystallography evidence used in manual assertion","statement":[{"text":"Unexpectedly, although the N-terminus is disordered in previous DPOR L-protein structures (residues 1-29 in 3FWY and\nresidues 1-27 in 2YNM), we observe electron\ndensity at the N-terminus of chain C in our\nnucleotide-free structure, which we were able\nto model as residues 16 to 29 (Supplemental\nFig. 1b).","type":"Results"},{"text":"Interestingly, in chain C, we observe\nthe flexible N-terminus bound across the\n[4Fe-4S] cluster (Fig. 2a, dark blue) covering\na surface that is normally used to interface\nwith BchNB (Fig. 2c, purple).","type":"Results"}],"curator_orcid":"0000-0001-9045-7765","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","reference_id":"33219127","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":29,"term_name":"self-inhibition","reference_html":"The flexible N-terminus of BchL autoinhibits activity through interaction with its [4Fe-4S] cluster and released upon ATP binding. <i> Corless EI, Saad Imran SM, Watkins MB, Bacik JP, Mattice JR, Patterson A, Danyal K, Soffe M, Kitelinger R, Seefeldt LC, Origanti S, Bennett B, Bothner B, Ando N, Antony E. </i> J Biol Chem, 2021","start":16,"region_id":"DP02993r003","term_id":"IDPO:0000059","unpublished":true,"version":3,"curator_id":"jssuarez","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","ec_name":"x-ray crystallography evidence used in manual assertion","statement":[{"text":"The position and specific interactions of the N-terminal residues in our\nnucleotide-free structure suggests a possible\nauto-inhibitory role by forming a barrier to\ndocking and shielding the [4Fe-4S] cluster of\nBchL.","type":"Results"},{"text":"The masking of the [4Fe-4S] cluster by the flexible N-terminal region and the\nassociated inhibition of activity is a novel\nmechanism of regulation in metalloproteins.","type":"Abstract"}],"curator_orcid":"0000-0001-9045-7765","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0005670","reference_id":"33219127","ec_go":"EXP","disprot_namespace":"Disorder function"},{"term_namespace":"Structural transition","ec_ontology":"ECO","end":29,"term_name":"order to disorder","reference_html":"The flexible N-terminus of BchL autoinhibits activity through interaction with its [4Fe-4S] cluster and released upon ATP binding. <i> Corless EI, Saad Imran SM, Watkins MB, Bacik JP, Mattice JR, Patterson A, Danyal K, Soffe M, Kitelinger R, Seefeldt LC, Origanti S, Bennett B, Bothner B, Ando N, Antony E. </i> J Biol Chem, 2021","start":16,"region_id":"DP02993r004","term_id":"IDPO:0000014","unpublished":true,"version":2,"curator_id":"jssuarez","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","statement":[{"text":"Hydrogen deuterium exchange mass spectrometry shows that ATPbinding to BchL produces specific conformational changes leading to release of the flexible N-terminus from the docking interface. ","type":"Abstract"},{"text":"The HDX data suggest a direct path\nof communication between the N-terminal\nflexible region and the ATP binding pocket.\nPerturbations in the N-terminal flexible region allosterically modulates changes in the\nATP-binding pocket (and vice versa).","type":"Results"}],"curator_orcid":"0000-0001-9045-7765","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006196","reference_id":"33219127","ec_go":"EXP","disprot_namespace":"Structural transition"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":29,"term_name":"self-inhibition","reference_html":"The flexible N-terminus of BchL autoinhibits activity through interaction with its [4Fe-4S] cluster and released upon ATP binding. <i> Corless EI, Saad Imran SM, Watkins MB, Bacik JP, Mattice JR, Patterson A, Danyal K, Soffe M, Kitelinger R, Seefeldt LC, Origanti S, Bennett B, Bothner B, Ando N, Antony E. </i> J Biol Chem, 2021","start":1,"region_id":"DP02993r005","term_id":"IDPO:0000059","unpublished":true,"version":3,"curator_id":"jssuarez","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","ec_name":"mutant phenotype evidence used in manual assertion","statement":[{"text":"We show that amino acid\nsubstitutions within this flexible N-terminal\nregion enhance the kinetics of Pchlide reduction, pointing to a functionally auto-inhibitory role.","type":"Introduction"},{"text":" Both BchLS17A and\nBchL4A are active for Pchlide reduction and\nshow Chlide formation rates ~2 fold higher\nthan that of wild type BchL (kobs= 0.026 ±\n0.002, 0.041 ± 0.008, and 0.045 ± 0.007 min1\nfor BchL, BchLS17A and BchL4A, respectively; Fig. 3b). ","type":"Results"}],"curator_orcid":"0000-0001-9045-7765","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000315","reference_id":"33219127","ec_go":"IMP","disprot_namespace":"Disorder function"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":29,"term_name":"self-inhibition","reference_html":"The flexible N-terminus of BchL autoinhibits activity through interaction with its [4Fe-4S] cluster and released upon ATP binding. <i> Corless EI, Saad Imran SM, Watkins MB, Bacik JP, Mattice JR, Patterson A, Danyal K, Soffe M, Kitelinger R, Seefeldt LC, Origanti S, Bennett B, Bothner B, Ando N, Antony E. </i> J Biol Chem, 2021","start":1,"region_id":"DP02993r006","term_id":"IDPO:0000059","unpublished":true,"version":3,"curator_id":"jssuarez","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","statement":[{"text":"The HDX data suggest a direct path of communication between the N-terminal flexible region and the ATP binding pocket. Perturbations in the N-terminal flexible region allosterically modulates changes in the ATP-binding pocket (and vice versa).","type":"Results"},{"text":"The HDX-MS data support an elegant\nallosteric mechanism for the ATP-binding\ndriven release of autoinhibition, as helix 8\nphysically connects the DFD patch and the\nflexible N-terminal region (Supplemental\nFig. 6b-c).","type":"Discussion"}],"curator_orcid":"0000-0001-9045-7765","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006196","reference_id":"33219127","ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_12","length":297,"ncbi_taxon_id":272943,"organism":"Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)","disprot_id":"DP02993","date":"2020-11-26T17:07:52.864Z","regions_counter":6,"dataset":[],"UniParc":"UPI0000126810","uniref100":"UniRef100_Q9RFD6","uniref90":"UniRef90_Q9RFD6","uniref50":"UniRef50_Q9RFD6","genes":[{"name":{"value":"bchL","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00355","url":"https://hamap.expasy.org/unirule/MF_00355"}}]},"orfNames":[{"value":"RSP_0288"}],"olnNames":[{"value":"RHOS4_18930"}]}],"alphafold_very_low_content":0.04713804713804714,"disorder_content":0.09764309764309764,"disprot_consensus":{"full":[{"start":1,"end":15,"type":"D"},{"start":16,"end":29,"type":"T"}],"Structural state":[{"start":1,"end":29,"type":"D"}],"Structural transition":[{"start":16,"end":29,"type":"T"}],"Disorder function":[{"start":1,"end":29,"type":"F"}]}},{"acc":"Q84MC7","features":{"pfam":[{"id":"PF10604","name":"Polyketide cyclase / dehydrase and lipid transport","start":39,"end":178}],"gene3D":[]},"creator":"jssuarez","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"sequence":"MMDGVEGGTAMYGGLETVQYVRTHHQHLCRENQCTSALVKHIKAPLHLVWSLVRRFDQPQKYKPFVSRCTVIGDPEIGSLREVNVKSGLPATTSTERLELLDDEEHILGIKIIGGDHRLKNYSSILTVHPEIIEGRAGTMVIESFVVDVPQGNTKDETCYFVEALIRCNLKSLADVSERLASQDITQ","name":"Abscisic acid receptor PYL9","regions":[{"region_id":"DP02995r001","unpublished":true,"ec_ontology":"ECO","end":12,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"The map obtained showed clear electron density for most of the protein residues and the ABA–bound molecule, whereas no models were built for 12 N‐terminal and 5 C‐terminal residues, which were not observed in the electron density map.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"24645846","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3W9R"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"jssuarez","reference_html":"Mechanism of high-affinity abscisic acid binding to PYL9/RCAR1. <i> Nakagawa M, Kagiyama M, Shibata N, Hirano Y, Hakoshima T. </i> Genes Cells, 2014","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-01-25T16:46:20.348Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":17,"term_name":"disorder","start":1,"region_id":"DP02995r002","term_id":"IDPO:0000002","unpublished":true,"reference_html":"Structural insights into the abscisic acid stereospecificity by the ABA receptors PYR/PYL/RCAR. <i> Zhang X, Jiang L, Wang G, Yu L, Zhang Q, Xin Q, Wu W, Gong Z, Chen Z. </i> PLoS One, 2013","curator_id":"vnugnes","released":"2024_06","term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2024-01-25T16:48:21.454Z","reference_source":"pmid","ec_id":"ECO:0006220","cross_refs":[{"db":"PDB","id":"3OQU"}],"reference_id":"23844015","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5280896"}],"statement":[{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"released":"2021_12","length":187,"ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","disprot_id":"DP02995","date":"2020-11-26T19:59:51.539Z","regions_counter":2,"dataset":[],"UniParc":"UPI0000162BE3","uniref100":"UniRef100_Q84MC7","uniref90":"UniRef90_Q84MC7","uniref50":"UniRef50_Q84MC7","genes":[{"name":{"value":"PYL9"},"synonyms":[{"value":"RCAR1"}],"orfNames":[{"value":"F6F3.16"}],"olnNames":[{"value":"At1g01360"}]}],"alphafold_very_low_content":0.06951871657754011,"disorder_content":0.09090909090909091,"disprot_consensus":{"full":[{"start":1,"end":17,"type":"D"}],"Structural state":[{"start":1,"end":17,"type":"D"}]}},{"acc":"O85041","features":{"pfam":[{"id":"PF12288","name":"Carboxysome shell peptide mid-region","start":17,"end":140},{"id":"PF12288","name":"Carboxysome shell peptide mid-region","start":173,"end":533}],"gene3D":[]},"creator":"jssuarez","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Chromatiales","Halothiobacillaceae","Halothiobacillus"],"sequence":"MPSQSGMNPADLSGLSGKELARARRAALSKQGKAAVSNKTASVNRSTKQAASSINTNQVRSSVNEVPTDYQMADQLCSTIDHADFGTESNRVRDLCRQRREALSTIGKKAAKTTGKPSGRVRPQQSVVHNDAMIENAGDTNQSSSTSLNNELSEICSIADDMPERFGSQAKTVRDICRARRQALSERGTRAVPPKPQSQGGPGRNGYQIDGYLDTALHGRDAAKRHREMLCQYGRGTAPSCKPTGRVKNSVQSGNAAPKKVETGHTLSGGSVTGTQVDRKSHVTGNEPGTCRAVTGTEYVGTEQFTSFCNTSPKPNATKVNVTTTARGRPVSGTEVSRTEKVTGNESGVCRNVTGTEYMSNEAHFSLCGTAAKPSQADKVMFGATARTHQVVSGSDEFRPSSVTGNESGAKRTITGSQYADEGLARLTINGAPAKVARTHTFAGSDVTGTEIGRSTRVTGDESGSCRSISGTEYLSNEQFQSFCDTKPQRSPFKVGQDRTNKGQSVTGNLVDRSELVTGNEPGSCSRVTGSQYGQSKICGGGVGKVRSMRTLRGTSVSGQQLDHAPKMSGDERGGCMPVTGNEYYGREHFEPFCTSTPEPEAQSTEQSLTCEGQIISGTSVDASDLVTGNEIGEQQLISGDAYVGAQQTGCLPTSPRFNQTGNVQSMGFKNTNQPEQNFAPGEVMPTDFSIQTPARSAQNRITGNDIAPSGRITGPGMLATGLITGTPEFRHAARELVGSPQPMAMAMANRNKAAQAPVVQPEVVATQEKPELVCAPRSDQMDRVSGEGKERCHITGDDWSVNKHITGTAGQWASGRNPSMRGNARVVETSAFANRNVPKPEKPGSKITGSSGNDTQGSLITYSGGARG","name":"Carboxysome shell polypeptide","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":603,"term_name":"disorder","reference_html":"Multivalent interactions between CsoS2 and Rubisco mediate α-carboxysome formation. <i> Oltrogge LM, Chaijarasphong T, Chen AW, Bolin ER, Marqusee S, Savage DF. </i> Nat Struct Mol Biol, 2020","start":260,"region_id":"DP02996r001","term_id":"IDPO:0000002","unpublished":true,"version":2,"curator_id":"jssuarez","released":"2023_12","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"Circular dichroism (CD) spectra indicated that only the NTD has α-helical content (Fig. 1b).","type":"Results"}],"curator_orcid":"0000-0001-9045-7765","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","reference_id":"32123388","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T09:23:07.059Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":839,"term_name":"disorder","reference_html":"Multivalent interactions between CsoS2 and Rubisco mediate α-carboxysome formation. <i> Oltrogge LM, Chaijarasphong T, Chen AW, Bolin ER, Marqusee S, Savage DF. </i> Nat Struct Mol Biol, 2020","start":604,"region_id":"DP02996r002","term_id":"IDPO:0000002","unpublished":true,"version":2,"curator_id":"jssuarez","released":"2023_12","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"Circular dichroism (CD) spectra indicated that only the NTD has α-helical content (Fig. 1b).","type":"Results"}],"curator_orcid":"0000-0001-9045-7765","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","reference_id":"32123388","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T09:23:06.168Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2023_12","length":869,"ncbi_taxon_id":927,"organism":"Halothiobacillus neapolitanus","disprot_id":"DP02996","date":"2020-11-27T12:14:47.145Z","regions_counter":2,"dataset":[],"UniParc":"UPI00000B6577","uniref100":"UniRef100_O85041","uniref90":"UniRef90_O85041","uniref50":"UniRef50_O85041","genes":[{"name":{"value":"csoS2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9696760","url":"http://www.ncbi.nlm.nih.gov/pubmed/9696760","alternativeUrl":"https://europepmc.org/abstract/MED/9696760"}}]},"olnNames":[{"value":"Hneap_0920"}]}],"alphafold_very_low_content":0.3037974683544304,"disorder_content":0.667433831990794,"disprot_consensus":{"full":[{"start":260,"end":839,"type":"D"}],"Structural state":[{"start":260,"end":839,"type":"D"}]}},{"acc":"P34808","features":{"pfam":[{"id":"PF00004","name":"ATPase family associated with various cellular activities (AAA)","start":229,"end":361},{"id":"PF17862","name":"AAA+ lid domain","start":384,"end":417}],"gene3D":[]},"creator":"spenadias","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"sequence":"MNGDVQSVIRGYLERAQVAKTMSDAGRWNEAGDLLRQLMTDVKSCKISASNRDEHDARNTFLRALEANLKLVQQNVRDEDDLHEAMTRQSGSPEPPADPDVWSKPSPPLPSSSKFGATKKGVGAAGPRPREISKSTSSMSTNPADVKPANPTQGILPQNSAGDSFDASAYDAYIVQAVRGTMATNTENTMSLDDIIGMHDVKQVLHEAVTLPLLVPEFFQGLRSPWKAMVLAGPPGTGKTLIARAIASESSSTFFTVSSTDLSSKWRGDSEKIVRLLFELARFYAPSIIFIDEIDTLGGQRGNSGEHEASRRVKSEFLVQMDGSQNKFDSRRVFVLAATNIPWELDEALRRRFEKRIFIPLPDIDARKKLIEKSMEGTPKSDEINYDDLAARTEGFSGADVVSLCRTAAINVLRRYDTKSLRGGELTAAMESLKAELVRNIDFEAALQAVSPSAGPDTMLKCKEWCDSFGAM","name":"Meiotic spindle formation protein mei-1","regions":[{"region_id":"DP02999r001","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-01T15:40:40.061Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":172,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"Six regions of the polypeptide chain (residues 1–172, 186–190, 263–269, 297–306,\n324–332, 467–472) are not well resolved and presumed disordered","type":"Methods"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-2902-823X","released":"2022_03","term_ontology":"IDPO","curator_name":"Samuel Peña Díaz","reference_id":"28783150","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5WCB"},{"db":"PDB","id":"5WC0"},{"db":"PDB","id":"5WC1"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"spenadias","reference_html":"Katanin spiral and ring structures shed light on power stroke for microtubule severing. <i> Zehr E, Szyk A, Piszczek G, Szczesna E, Zuo X, Roll-Mecak A. </i> Nat Struct Mol Biol, 2017","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02999r002","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-01T15:40:39.116Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":306,"term_id":"IDPO:0000002","start":297,"version":2,"statement":[{"text":"Six regions of the polypeptide chain (residues 1–172, 186–190, 263–269, 297–306,\n324–332, 467–472) are not well resolved and presumed disordered","type":"Methods"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-2902-823X","released":"2022_03","term_ontology":"IDPO","curator_name":"Samuel Peña Díaz","reference_id":"28783150","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5WCB"},{"db":"PDB","id":"5WC0"},{"db":"PDB","id":"5WC1"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"spenadias","reference_html":"Katanin spiral and ring structures shed light on power stroke for microtubule severing. <i> Zehr E, Szyk A, Piszczek G, Szczesna E, Zuo X, Roll-Mecak A. </i> Nat Struct Mol Biol, 2017","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP02999r003","unpublished":true,"ec_ontology":"ECO","end":140,"term_id":"IDPO:0000033","start":85,"version":3,"statement":[{"text":"Domain diagram of katanin p60; MIT, microtubule interacting and trafficking domain, yellow; flexible linker, pink; AAA domain, gray; fishhook-shaped linker element, light blue; α1, dark blue; α12 and C-terminal residues 468–472, dark orange. NBD and HBD are highlighted by light green and dark green hatches, respectively. Residue numbers for C. elegans katanin.","type":"Figure"},{"text":"Pink region in figure 1D is comprised between residues 85-140","type":"Curator statement"},{"text":"This region connects microtubule interacting and trafficking (MIT) domain to the AAA ATPase domain","type":"Curator statement"}],"term_name":"flexible linker","ec_name":"small-angle X-ray scattering evidence used in manual assertion","curator_orcid":"0000-0002-2902-823X","released":"2022_03","term_ontology":"IDPO","curator_name":"Samuel Peña Díaz","reference_id":"28783150","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5WCB"},{"db":"PDB","id":"5WC0"},{"db":"PDB","id":"5WC1"}],"term_namespace":"Disorder function","ec_id":"ECO:0006210","curator_id":"spenadias","reference_html":"Katanin spiral and ring structures shed light on power stroke for microtubule severing. <i> Zehr E, Szyk A, Piszczek G, Szczesna E, Zuo X, Roll-Mecak A. </i> Nat Struct Mol Biol, 2017","ec_go":"EXP","disprot_namespace":"Disorder function"},{"region_id":"DP02999r004","unpublished":true,"ec_ontology":"ECO","end":156,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"Disordered segments not visible in reconstruction marked with hatches. Residue numbers for C. elegans katanin.","type":"Figure"},{"text":"Hatched regions are comprised between residues 1-156 in Figure 2E","type":"Curator statement"},{"text":"No density was visible for the rest of the linker and the MIT domain, consistent with their flexibility as previously shown (Zehr et al., 2017).\" ","type":"Results"}],"term_name":"disorder","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-2902-823X","released":"2022_03","term_ontology":"IDPO","curator_name":"Samuel Peña Díaz","reference_id":"31735665","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6UGD"},{"db":"PDB","id":"6UGF"},{"db":"PDB","id":"6UGE"}],"term_namespace":"Structural state","ec_id":"ECO:0006224","curator_id":"spenadias","reference_html":"Katanin Grips the β-Tubulin Tail through an Electropositive Double Spiral to Sever Microtubules. <i> Zehr EA, Szyk A, Szczesna E, Roll-Mecak A. </i> Dev Cell, 2020","ec_go":"IDA","disprot_namespace":"Structural state"},{"start":1,"end":172,"reference_id":"31735665","reference_source":"pmid","reference_html":"Katanin Grips the β-Tubulin Tail through an Electropositive Double Spiral to Sever Microtubules. <i> Zehr EA, Szyk A, Szczesna E, Roll-Mecak A. </i> Dev Cell, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"6UGF"},{"db":"PDB","id":"6UGE"},{"db":"PDB","id":"6UGD"}],"region_id":"DP02999r005","statement":[{"text":"A disordered region outside the AAA core anchors katanin to the microtubule while the AAA motor exerts the forces that extract tubulin dimers and sever the microtubule","type":"Abstract"},{"text":"Thus, our structural and functional work reveals how tubulin tails template the assembly and ATPase activation of the katanin hexamer, and shows how katanin uses complex multivalent interactions with the microtubule through flexible and intrinsically disordered elements to generate the forces needed to extract tubulin subunits out of the microtubule","type":"Introduction"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":84,"reference_id":"31735665","reference_source":"pmid","reference_html":"Katanin Grips the β-Tubulin Tail through an Electropositive Double Spiral to Sever Microtubules. <i> Zehr EA, Szyk A, Szczesna E, Roll-Mecak A. </i> Dev Cell, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"6UGF"},{"db":"PDB","id":"6UGE"},{"db":"PDB","id":"6UGD"}],"region_id":"DP02999r006","statement":[{"text":"Our structural and functional work shows that katanin, unlike other AAA ATPases characterized so far, uses a double-spiral system to coordinate the tubulin tail through the central pore and multivalent contacts through a low complexity disordered region outside the ordered AAA core to anchor the enzyme to the microtubule","type":"Discussion"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":85,"end":172,"reference_id":"31735665","reference_source":"pmid","reference_html":"Katanin Grips the β-Tubulin Tail through an Electropositive Double Spiral to Sever Microtubules. <i> Zehr EA, Szyk A, Szczesna E, Roll-Mecak A. </i> Dev Cell, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"6UGF"},{"db":"PDB","id":"6UGE"},{"db":"PDB","id":"6UGD"}],"region_id":"DP02999r007","statement":[{"text":"A Positively Charged Disordered Linker Region Is Critical for Severing","type":"Results"},{"text":"Mutation of the equivalent Ser to a phosphomimetic residue (Ser135Glu) in C. elegans katanin causes a ∼50% decrease in ATPase (Figure 5A) as well as microtubule severing and nanodamage activity (Figures 5B, 5D, 5E, and S7A). Thus, the introduction of negative charges in this linker region inhibits katanin","type":"Results"},{"text":"Our results indicate that both microtubule binding and mechanochemical coupling are impaired when positively charged residues are mutated in the linker, with K119 and K120 having the most drastic effect. Thus, elements outside the structured AAA and MIT domains are critical for severing","type":"Results"},{"text":"Our functional work reveals that clusters of positively charged residues in the disordered linker connecting the AAA and MIT domains are required for katanin microtubule binding and severing","type":"Discussion"},{"text":"High-affinity microtubule binding requires the disordered linker (Eckert et al., 2012, Jiang et al., 2017), consistent with our finding that positively charged linker residues are critical for katanin severing","type":"Discussion"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_12","length":472,"ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","disprot_id":"DP02999","date":"2020-11-30T15:28:50.103Z","regions_counter":7,"dataset":[],"UniParc":"UPI000012EEBA","uniref100":"UniRef100_P34808","uniref90":"UniRef90_P34808","uniref50":"UniRef50_P34808","genes":[{"name":{"value":"mei-1","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03023","url":"https://hamap.expasy.org/unirule/MF_03023"}}]},"orfNames":[{"value":"T01G9.5"}]}],"alphafold_very_low_content":0.1440677966101695,"disorder_content":0.3855932203389831,"disprot_consensus":{"full":[{"start":1,"end":172,"type":"D"},{"start":297,"end":306,"type":"D"}],"Structural state":[{"start":1,"end":172,"type":"D"},{"start":297,"end":306,"type":"D"}],"Disorder function":[{"start":85,"end":140,"type":"F"}],"Molecular function":[{"start":1,"end":172,"type":"F"}]}},{"acc":"Q997F2","features":{"pfam":[{"id":"PF13008","name":"Zinc-binding domain of Paramyxoviridae V protein","start":413,"end":455},{"id":"PF14313","name":"N-terminal region of Paramyxovirinae phosphoprotein (P)","start":5,"end":52},{"id":"PF14320","name":"Phosphoprotein P region PNT disordered","start":71,"end":351}],"gene3D":[]},"creator":"ewagner","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Paramyxoviridae","Orthoparamyxovirinae","Henipavirus"],"sequence":"MDKLELVNDGLNIIDFIQKNQKEIQKTYGRSSIQQPSIKDQTKAWEDFLQCTSGESEQVEGGMSKDDGDVERRNLEDLSSTSPTDGTIGKRVSNTRDWAEGSDDIQLDPVVTDVVYHDHGGECTGYGFTSSPERGWSDYTSGANNGNVCLVSDAKMLSYAPEIAVSKEDRETDLVHLENKLSTTGLNPTAVPFTLRNLSDPAKDSPVIAEHYYGLGVKEQNVGPQTSRNVNLDSIKLYTSDDEEADQLEFEDEFAGSSSEVIVGISPEDEEPSSVGGKPNESIGRTIEGQSIRDNLQAKDNKSTDVPGAGPKDSAVKEEPPQKRLPMLAEEFECSGSEDPIIRELLKENSLINCQQGKDAQPPYHWSIERSISPDKTEIVNGAVQTADRQRPGTPMPKSRGIPIKKGHRREISICWDGKRAWVEEWCNPACSRITPLPRRQECQCGECPTECFHCG","name":"Non-structural protein V","regions":[{"region_id":"DP03000r001","unpublished":true,"ec_ontology":"ECO","end":456,"term_id":"IDPO:0000002","start":1,"version":3,"statement":[{"text":"This aberrant migration during electrophoresis is a hallmark of intrinsically disordered proteins (IDPs) and is often due to their typically high content of acidic residues35 and/or low compaction.","type":"Results"}],"term_name":"disorder","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","curator_orcid":"0000-0003-2206-9968","released":"2023_06","term_ontology":"IDPO","curator_name":"Julian Bergier","reference_id":"28972216","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0007689","curator_id":"jbergier","reference_html":"The Henipavirus V protein is a prevalently unfolded protein with a zinc-finger domain involved in binding to DDB1. <i> Salladini E, Delauzun V, Longhi S. </i> Mol Biosyst, 2017","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-22T13:41:00.885Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP03000r002","unpublished":true,"ec_ontology":"ECO","end":456,"term_id":"IDPO:0000004","start":1,"version":3,"statement":[{"text":"The experimentally observed values of the Rs are very close to the values expected for a PMG form (i.e. an extended conformation possessing nevertheless some residual structure38) (∼45 Å) (see Table 1).","type":"Results"}],"term_name":"pre-molten globule","ec_name":"chromatography evidence used in manual assertion","curator_orcid":"0000-0003-2206-9968","released":"2023_06","term_ontology":"IDPO","curator_name":"Julian Bergier","reference_id":"28972216","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0007680","curator_id":"jbergier","reference_html":"The Henipavirus V protein is a prevalently unfolded protein with a zinc-finger domain involved in binding to DDB1. <i> Salladini E, Delauzun V, Longhi S. </i> Mol Biosyst, 2017","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-22T13:40:55.573Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP03000r003","unpublished":true,"ec_ontology":"ECO","end":456,"term_id":"IDPO:0000004","start":1,"version":3,"statement":[{"text":"The spectra are typical of proteins predominantly unfolded, as judged from their large negative ellipticity at 200 nm, low amplitude in the 210–230 nm region, and low ellipticity at 190 nm (Fig. 3A).","type":"Results"},{"text":"As shown in the inset of Fig. 3A, HeV and NiV V fall closer to the PMG-like region than to the RC-like region.","type":"Results"}],"term_name":"pre-molten globule","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0003-2206-9968","released":"2023_06","term_ontology":"IDPO","curator_name":"Julian Bergier","reference_id":"28972216","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006204","curator_id":"jbergier","reference_html":"The Henipavirus V protein is a prevalently unfolded protein with a zinc-finger domain involved in binding to DDB1. <i> Salladini E, Delauzun V, Longhi S. </i> Mol Biosyst, 2017","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-22T13:40:49.859Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP03000r005","unpublished":true,"ec_ontology":"ECO","end":456,"term_id":"IDPO:0000002","start":1,"version":3,"statement":[{"text":"The strong discrepancy between the experimentally observed Rg values and those expected for a globular/spherical form, together with the fact that they are even larger than the values expected for IDPs indicate that the V proteins are highly disordered.","type":"Results"}],"term_name":"disorder","ec_name":"small-angle X-ray scattering evidence used in manual assertion","curator_orcid":"0000-0003-2206-9968","released":"2023_06","term_ontology":"IDPO","curator_name":"Julian Bergier","reference_id":"28972216","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006210","curator_id":"jbergier","reference_html":"The Henipavirus V protein is a prevalently unfolded protein with a zinc-finger domain involved in binding to DDB1. <i> Salladini E, Delauzun V, Longhi S. </i> Mol Biosyst, 2017","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-22T13:40:39.755Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP03000r006","unpublished":true,"ec_ontology":"ECO","end":456,"term_id":"GO:0005515","start":1,"version":4,"statement":[{"text":"In an attempt at quantifying the V-DDB1 binding affinity, we used microscale thermophoresis (MST). Labeled DDB1 was then titrated with unlabeled V. Results allowed us to infer an equilibrium dissociation constant (KD) of 32 ± 6 nM for HeV V and of 35 ± 3 nM for NiV V (Fig. 6C and D). ","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q16531","partner_end":null}],"term_name":"protein binding","ec_name":"microscale thermophoresis evidence used in manual assertion","curator_orcid":"0000-0003-2206-9968","released":"2023_06","term_ontology":"GO","curator_name":"Julian Bergier","reference_id":"28972216","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006303","curator_id":"jbergier","reference_html":"The Henipavirus V protein is a prevalently unfolded protein with a zinc-finger domain involved in binding to DDB1. <i> Salladini E, Delauzun V, Longhi S. </i> Mol Biosyst, 2017","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-22T13:41:08.974Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":406,"reference_id":"33177626","reference_source":"pmid","reference_html":"Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS. <i> Schiavina M, Salladini E, Murrali MG, Tria G, Felli IC, Pierattelli R, Longhi S. </i> Sci Rep, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"cross_refs":[{"db":"SASBDB","id":"SASDJB5"}],"region_id":"DP03000r007","statement":[{"text":"The flexible nature of NiV PNT was qualitatively assessed by using the normalized Kratky plot, where the absence of a well-defined bell shape indicates a protein with intrinsically disordered regions (Fig. 4C).","type":"Results"},{"text":"The resulting final Rg distribution, broader than the one generated from the NMR-based pool, indicates that NiV PNT exists in solution as a randomly distributed ensemble of non-compact and highly flexible conformations.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-11-22T14:28:24.286Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":406,"reference_id":"33177626","reference_source":"pmid","reference_html":"Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS. <i> Schiavina M, Salladini E, Murrali MG, Tria G, Felli IC, Pierattelli R, Longhi S. </i> Sci Rep, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"cross_refs":[{"db":"BMRB","id":"50370"}],"region_id":"DP03000r008","statement":[{"text":"NiV PNT is a very large intrinsically disordered protein (412 residues including the C-terminal His tag and the initial methionine), as can be inferred by inspection of the two 2D spectra, the 1H–15N HSQC (Fig. 2A) and the 13C′–15N CON (Fig. 2B).","type":"Results"},{"text":"The relaxation rates show an overall trend consistent with the considerably disordered conformation of PNT. 1H–15N NOE values are all well below 0.5, indicating high flexibility of the backbone (Supplementary Figure S1A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-11-22T14:29:08.955Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":456,"reference_id":"28972216","reference_source":"pmid","reference_html":"The Henipavirus V protein is a prevalently unfolded protein with a zinc-finger domain involved in binding to DDB1. <i> Salladini E, Delauzun V, Longhi S. </i> Mol Biosyst, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006206","ec_ontology":"ECO","ec_name":"near-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03000r009","statement":[{"text":"The near-UV CD spectra of the V proteins are rather smooth suggesting a predominantly disordered nature (Fig. 3B).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-22T13:40:26.267Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":409,"end":456,"reference_id":"29769705","reference_source":"pmid","reference_html":"Possible role of the Nipah virus V protein in the regulation of the interferon beta induction by interacting with UBX domain-containing protein1. <i> Uchida S, Horie R, Sato H, Kai C, Yoneda M. </i> Sci Rep, 2018","date":"2024-04-09T08:25:13.933Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0522","term_name":"myc","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"To identify host proteins that specifically interact with the unique C-terminal domain of NiV V, which is not shared with the P or W protein, myc-tagged wild-type NiV V and a mutant lacking the C-terminal domain (ΔCT) were expressed in HEK293T cells and immunoprecipitated with an anti-myc antibody. "}]}],"ec_go":"IPI","region_id":"DP03000r011","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"},{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0045","entry_name":"Human Embryonic Kidney 293"}],"statement":[{"text":"To confirm the result of the mass-spectrometric analysis, the same immunoprecipitation assay was followed by western blotting with an anti-myc antibody and an anti-UBXN1 antibody. UBXN1 was detected as the protein binding to wild-type NiV V, but not to ΔCT (Fig. 1B). The interaction was also verified by the coimmunoprecipitation of NiV V with the endogenous UBXN1 (Fig. 1C). In HeLa cells, UBXN1 was also coimmunoprecipitated with NiV V, indicating that UBXN1 is a binding partner of NiV V in various cell types (Fig. 1D). ","type":"Results"},{"text":"The wild-type NiV V, but not ΔCT, was coimmunoprecipitated with UBXN1 (Fig. 1E).","type":"Results"},{"text":"Two protein bands coimmunoprecipitated with wild-type NiV V, but not with ΔCT were detected (Supplementary Fig. 1A). One of the proteins with a mass of approximately 42.56 kDa was identified as UBX domain-containing protein 1 (UBXN1) by a mass-spectrometric analysis (Fig. 1A).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"Q04323","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-09T13:23:14.363Z"}},{"start":1,"end":456,"reference_id":"29769705","reference_source":"pmid","reference_html":"Possible role of the Nipah virus V protein in the regulation of the interferon beta induction by interacting with UBX domain-containing protein1. <i> Uchida S, Horie R, Sato H, Kai C, Yoneda M. </i> Sci Rep, 2018","date":"2024-04-09T08:25:49.310Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005601","ec_ontology":"ECO","ec_name":"immunofluorescence confocal microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0522","term_name":"myc","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"To identify host proteins that specifically interact with the unique C-terminal domain of NiV V, which is not shared with the P or W protein, myc-tagged wild-type NiV V and a mutant lacking the C-terminal domain (ΔCT) were expressed in HEK293T cells and immunoprecipitated with an anti-myc antibody. "}]}],"ec_go":"IDA","region_id":"DP03000r012","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0045","entry_name":"Human Embryonic Kidney 293"}],"statement":[{"text":"To confirm their intracellular interaction, an immunofluorescence assay was also performed after NiV V or UBXN1 was expressed in HEK293T cells. As previously reported, NiV V was mainly localized in cytoplasm (Fig. 1F, upper lane)24. UBXN1 was also localized in cytoplasm, and formed spot-like structures (Fig. 1F, middle lane), which is reportedly attributable to its association with the ubiquitin–proteasome system27,28. The coexpression of both proteins caused the accumulation of UBXN1 in the cytoplasm, and its signal localized strongly with that of the V protein (Fig. 1F, lower lane). Furthermore, NiV V was co-localized with endogenous UBXN1 in the cytoplasm (Fig. 1G). These results suggest that V protein interacts intracellularly with UBXN1.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"Q04323","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-09T13:23:27.892Z"}},{"start":409,"end":426,"reference_id":"29769705","reference_source":"pmid","reference_html":"Possible role of the Nipah virus V protein in the regulation of the interferon beta induction by interacting with UBX domain-containing protein1. <i> Uchida S, Horie R, Sato H, Kai C, Yoneda M. </i> Sci Rep, 2018","date":"2024-04-08T08:08:44.910Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0050821","term_name":"protein stabilization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006081","ec_ontology":"ECO","ec_name":"far-Western blotting evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0522","term_name":"myc","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"To identify host proteins that specifically interact with the unique C-terminal domain of NiV V, which is not shared with the P or W protein, myc-tagged wild-type NiV V and a mutant lacking the C-terminal domain (ΔCT) were expressed in HEK293T cells and immunoprecipitated with an anti-myc antibody. "}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q04323","operator":null,"partner_start":211,"partner_end":293}],"region_id":"DP03000r013","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0045","entry_name":"Human Embryonic Kidney 293"}],"statement":[{"text":"When NiV V was expressed together with UBXN1, the degradation of UBXN1 was inhibited (Fig. 3E,F). This result suggests that NiV V increases the stability of UBXN1, causing its intracellular accumulation.","type":"Results"},{"text":"The mutants containing Domain1 (Del1, -2 and -5) clearly increased the expression level of UBXN1, whereas the others did not (Fig. 4A).","type":"Results"},{"text":"These results indicate that the stabilization of UBXN1 requires Domain1 of NiV V and the UBX domain of UBXN1, which are identical to the domains required for the interaction of the two proteins (Fig. 2C,E). Therefore, we infer that the stabilization of UBXN1 is caused by its interaction with NiV V.","type":"Results"}],"term_comment":"","term_def":"\"Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-08T17:21:55.213Z"}},{"start":412,"end":426,"reference_id":"29769705","reference_source":"pmid","reference_html":"Possible role of the Nipah virus V protein in the regulation of the interferon beta induction by interacting with UBX domain-containing protein1. <i> Uchida S, Horie R, Sato H, Kai C, Yoneda M. </i> Sci Rep, 2018","date":"2024-04-09T09:05:57.868Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0050821","term_name":"protein stabilization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0522","term_name":"myc","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"To identify host proteins that specifically interact with the unique C-terminal domain of NiV V, which is not shared with the P or W protein, myc-tagged wild-type NiV V and a mutant lacking the C-terminal domain (ΔCT) were expressed in HEK293T cells and immunoprecipitated with an anti-myc antibody. "}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly418Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys419Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg420Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu424Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu425Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp426Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile412Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser413Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile414Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys415Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp416Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp417Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala421Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp422Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val423Ala","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q04323","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03000r014","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0045","entry_name":"Human Embryonic Kidney 293"}],"statement":[{"text":"To confirm the stabilization of UBXN1 by the myc-tagged alanine-substitution mutants of NiV V, these mutants were coexpressed with HA-tagged UBXN1. RRE stabilized UBXN1 as effectively as did wild-type NiV V, but GKR and EEW stabilized it less effectively, and ISI, CWD, and AWV did not stabilize it at all (Fig. 5C). Therefore, residues ISI, CWD, and AWV are important for UBXN1 stabilization.","type":"Results"}],"term_comment":"","term_def":"\"Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-09T13:23:58.144Z"}},{"start":409,"end":423,"reference_id":"29769705","reference_source":"pmid","reference_html":"Possible role of the Nipah virus V protein in the regulation of the interferon beta induction by interacting with UBX domain-containing protein1. <i> Uchida S, Horie R, Sato H, Kai C, Yoneda M. </i> Sci Rep, 2018","date":"2024-04-08T08:36:44.922Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0522","term_name":"myc","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"To identify host proteins that specifically interact with the unique C-terminal domain of NiV V, which is not shared with the P or W protein, myc-tagged wild-type NiV V and a mutant lacking the C-terminal domain (ΔCT) were expressed in HEK293T cells and immunoprecipitated with an anti-myc antibody. "}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg409Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg410Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu411Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile412Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser413Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile414Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala421Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp422Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val423Ala","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q9BYX4","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03000r015","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"The alanine-substitution mutants CWD, GKR, and EEW reduced the activity of MDA5 as strongly as did wild-type NiV V, whereas the interference activities of RRE, ISI, and AWV were weaker than that of wild-type NiV V (Fig. 5D). These results suggest that MDA5 and UBXN1 share the amino acid residues in ISI and AWV to interact with NiV V.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-08T17:30:48.425Z"}},{"start":1,"end":456,"reference_id":"29769705","reference_source":"pmid","reference_html":"Possible role of the Nipah virus V protein in the regulation of the interferon beta induction by interacting with UBX domain-containing protein1. <i> Uchida S, Horie R, Sato H, Kai C, Yoneda M. </i> Sci Rep, 2018","date":"2024-04-05T16:04:30.161Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0030430","term_name":"host cell cytoplasm","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005601","ec_ontology":"ECO","ec_name":"immunofluorescence confocal microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0522","term_name":"myc","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IDA","region_id":"DP03000r017","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0045","entry_name":"Human Embryonic Kidney 293"}],"statement":[{"text":"As previously reported, NiV V was mainly localized in cytoplasm (Fig. 1F, upper lane)24.","type":"Results"}],"term_comment":"","term_def":"\"The cytoplasm of a host cell.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":412,"end":423,"reference_id":"29769705","reference_source":"pmid","reference_html":"Possible role of the Nipah virus V protein in the regulation of the interferon beta induction by interacting with UBX domain-containing protein1. <i> Uchida S, Horie R, Sato H, Kai C, Yoneda M. </i> Sci Rep, 2018","date":"2024-04-05T16:54:25.875Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0522","term_name":"myc","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile412Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser413Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile414Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys415Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp416Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp417Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly418Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys419Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg420Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp422Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val423Ala","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q04323","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03000r018","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0045","entry_name":"Human Embryonic Kidney 293"}],"statement":[{"text":"The mutants were expressed in HEK293T cells and an immunoprecipitation assay was performed. Mutants RRE and EEW maintained the interaction with UBXN1, although it was weaker than that of intact NiV V. However, the interactions of mutants ISI, CWD, GKR, and AWV were eliminated (Fig. 5B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":456,"reference_id":"29769705","reference_source":"pmid","reference_html":"Possible role of the Nipah virus V protein in the regulation of the interferon beta induction by interacting with UBX domain-containing protein1. <i> Uchida S, Horie R, Sato H, Kai C, Yoneda M. </i> Sci Rep, 2018","date":"2024-12-17T14:12:03.363Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0039502","term_name":"suppression by virus of host type I interferon-mediated signaling pathway","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005648","ec_ontology":"ECO","ec_name":"luciferase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"ec_go":"IEP","region_id":"DP03000r019","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0045","entry_name":"Human Embryonic Kidney 293"}],"statement":[{"text":"MDA5 induced the activation of the IFNB promoter, and wild-type NiV V interrupted MDA5 activity (Fig. 5D).","type":"Results"},{"text":"HEK293T cells were transfected with an IFNβ reporter vector together with vectors expressing FLAG-tagged MDA5 and wild-type NiV V or its alanine-substitution mutants.","type":"Figure"}],"term_comment":"","term_def":"\"Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of type I interferon-mediated signaling in the host organism. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.\" [GOC:add, GOC:bf, GOC:sp, UniProtKB-KW:KW-1114, VZ:883]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":456,"reference_id":"29769705","reference_source":"pmid","reference_html":"Possible role of the Nipah virus V protein in the regulation of the interferon beta induction by interacting with UBX domain-containing protein1. <i> Uchida S, Horie R, Sato H, Kai C, Yoneda M. </i> Sci Rep, 2018","date":"2024-12-17T14:08:26.621Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0052170","term_name":"suppression by symbiont of host innate immune response","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005648","ec_ontology":"ECO","ec_name":"luciferase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"ec_go":"IEP","region_id":"DP03000r020","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0045","entry_name":"Human Embryonic Kidney 293"}],"statement":[{"text":"MDA5 induced the activation of the IFNB promoter, and wild-type NiV V interrupted MDA5 activity (Fig. 5D).","type":"Results"},{"text":"HEK293T cells were transfected with an IFNβ reporter vector together with vectors expressing FLAG-tagged MDA5 and wild-type NiV V or its alanine-substitution mutants.","type":"Figure"}],"term_comment":"","term_def":"\"Any process in which a symbiont stops, prevents, or reduces the frequency, rate or extent of the innate immune response of the host organism, the host's first line of defense against infection. The host is defined as the larger of the organisms involved in a symbiotic interaction.\" [GOC:mtg_pamgo_17jul06]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":456,"reference_id":"29769705","reference_source":"pmid","reference_html":"Possible role of the Nipah virus V protein in the regulation of the interferon beta induction by interacting with UBX domain-containing protein1. <i> Uchida S, Horie R, Sato H, Kai C, Yoneda M. </i> Sci Rep, 2018","date":"2024-04-05T17:19:08.922Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006309","ec_ontology":"ECO","ec_name":"competitive binding evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0522","term_name":"myc","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q04323","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9BYX4","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP03000r021","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0045","entry_name":"Human Embryonic Kidney 293"}],"statement":[{"text":"Although the coimmunoprecipitation of UBXN1 and MDA5 was slightly decreased in the competitive binding, both proteins were coimmunoprecipitated with NiV V together (Fig. 5E). These results indicated that the binding sites of NiV V to MDA5 and UBXN1 were close but not identical, and NiV V could interact with both proteins together.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":456,"reference_id":"29769705","reference_source":"pmid","reference_html":"Possible role of the Nipah virus V protein in the regulation of the interferon beta induction by interacting with UBX domain-containing protein1. <i> Uchida S, Horie R, Sato H, Kai C, Yoneda M. </i> Sci Rep, 2018","date":"2024-04-05T17:36:48.597Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0075111","term_name":"suppression by symbiont of host receptor-mediated signal transduction","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005648","ec_ontology":"ECO","ec_name":"luciferase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IEP","region_id":"DP03000r022","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0045","entry_name":"Human Embryonic Kidney 293"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q04323"}],"statement":[{"text":"The coexpression of UBXN1 increased MDA5-suppression activity of NiV V, depending on the expression level (Fig. 6A). To examine whether RIG-I signaling was suppressed by the stabilized UBXN1, the constitutively activated RIG-I (RIG-IΔ) was expressed with NiV V and UBXN1, and IFN reporter assay was performed. As previously reported19, NiV V did not suppress RIG-I signaling directly (Fig. 6B). However, when coexpressed with UBXN1, NiV V suppressed RIG-I signaling depending on the expression level (Fig. 6B). This suppression effect of NiV V was also observed in 293UBXN1- cells, indicating that it is not due to the artifacts derived from a high amount UBXN1 (Fig. 6C).","type":"Results"}],"term_comment":"Note that this term is used to annotate gene products of the symbiont. To annotate host gene products, consider the biological process term \"negative regulation by host of symbiont receptor-mediated signal transduction ; GO:0075080\".","term_def":"\"Any process in which the symbiont stops, prevents, or reduces the frequency, rate or extent of receptor-mediated signal transduction in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.\" [GOC:pamgo_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":456,"reference_id":"29769705","reference_source":"pmid","reference_html":"Possible role of the Nipah virus V protein in the regulation of the interferon beta induction by interacting with UBX domain-containing protein1. <i> Uchida S, Horie R, Sato H, Kai C, Yoneda M. </i> Sci Rep, 2018","date":"2024-12-17T14:09:36.416Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0052170","term_name":"suppression by symbiont of host innate immune response","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2025_06","version":1,"region_id":"DP03000r023","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0045","entry_name":"Human Embryonic Kidney 293"}],"statement":[{"text":"Furthermore, NiV V suppressed RIG-I and MDA5-dependent interferon signaling by stabilizing UBXN1 and increasing the interaction between MAVS and UBXN1 in addition to directly interrupting the activation of MDA5. Our results suggest a novel molecular mechanism by which the induction of interferon is potentially suppressed by NiV V protein via UBXN1.","type":"Results"}],"term_comment":"","term_def":"\"Any process in which a symbiont stops, prevents, or reduces the frequency, rate or extent of the innate immune response of the host organism, the host's first line of defense against infection. The host is defined as the larger of the organisms involved in a symbiotic interaction.\" [GOC:mtg_pamgo_17jul06]","term_is_obsolete":false,"term_not_annotate":false}],"released":"2023_06","length":456,"ncbi_taxon_id":121791,"organism":"Nipah virus","disprot_id":"DP03000","date":"2020-12-02T09:49:37.548Z","regions_counter":24,"dataset":["Viral proteins"],"UniParc":"UPI00000F8868","uniref100":"UniRef100_Q997F2","uniref90":"UniRef90_Q997F2","uniref50":"UniRef50_Q997F2","genes":[{"name":{"value":"P/V/C"}}],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":456,"type":"D"}],"Structural state":[{"start":1,"end":456,"type":"D"}],"Molecular function":[{"start":1,"end":456,"type":"F"}],"Biological process":[{"start":1,"end":456,"type":"F"}],"Cellular component":[{"start":1,"end":456,"type":"F"}]}},{"acc":"O55777","features":{"pfam":[{"id":"PF13008","name":"Zinc-binding domain of Paramyxoviridae V protein","start":411,"end":454},{"id":"PF14313","name":"N-terminal region of Paramyxovirinae phosphoprotein (P)","start":5,"end":51},{"id":"PF14320","name":"Phosphoprotein P region PNT disordered","start":71,"end":381}],"gene3D":[]},"creator":"ewagner","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Paramyxoviridae","Orthoparamyxovirinae","Henipavirus"],"sequence":"MDKLDLVNDGLDIIDFIQKNQKEIQKTYGRSSIQQPSTKDRTRAWEDFLQSTSGEHEQAEGGMPKNDGGTEGRNVEDLSSVTSSDGTIGQRVSNTRAWAEDPDDIQLDPMVTDVVYHDHGGECTGHGPSSSPERGWSYHMSGTHDGNVRAVPDTKVLPNAPKTTVPEEVREIDLIGLEDKFASAGLNPAAVPFVPKNQSTPTEEPPVIPEYYYGSGRRGDLSKSPPRGNVNLDSIKIYTSDDEDENQLEYEDEFAKSSSEVVIDTTPEDNDSINQEEVVGDPSDQGLEHPFPLGKFPEKEETPDVRRKDSLMQDSCKRGGVPKRLPMLSEEFECSGSDDPIIQELEREGSHPGGSLRLREPPQSSGNSRNQPDRQLKTGDAASPGGVQRPGTPMPKSRIMPIKKGHRREVSICWDGRRAWVEEWCNPVCSRITPQPRKQECYCGECPTECSQCCHEE","name":"Non-structural protein V","regions":[{"region_id":"DP03001r001","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T15:04:12.324Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":457,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"This aberrant migration during electrophoresis is a hallmark of intrinsically disordered proteins (IDPs) and is often due to their typically high content of acidic residues and/or low compaction.","type":"Results"}],"term_name":"disorder","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2023_06","term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"28972216","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0007689","curator_id":"tlazar","reference_html":"The Henipavirus V protein is a prevalently unfolded protein with a zinc-finger domain involved in binding to DDB1. <i> Salladini E, Delauzun V, Longhi S. </i> Mol Biosyst, 2017","ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP03001r002","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T15:04:11.689Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":457,"term_id":"IDPO:0000004","start":1,"version":2,"statement":[{"text":"The experimentally observed values of the Rs are very close to the values expected for a PMG form (i.e. an extended conformation possessing nevertheless some residual structure","type":"Results"}],"term_name":"pre-molten globule","ec_name":"chromatography evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2023_06","term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"28972216","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0007680","curator_id":"tlazar","reference_html":"The Henipavirus V protein is a prevalently unfolded protein with a zinc-finger domain involved in binding to DDB1. <i> Salladini E, Delauzun V, Longhi S. </i> Mol Biosyst, 2017","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP03001r003","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T15:04:11.142Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":457,"term_id":"IDPO:0000004","start":1,"version":2,"statement":[{"text":"The spectra are typical of proteins predominantly unfolded","type":"Results"},{"text":"HeV and NiV V fall closer to the PMG-like region than to the RC-like region","type":"Results"}],"term_name":"pre-molten globule","ec_name":"far-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2023_06","term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"28972216","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006204","curator_id":"tlazar","reference_html":"The Henipavirus V protein is a prevalently unfolded protein with a zinc-finger domain involved in binding to DDB1. <i> Salladini E, Delauzun V, Longhi S. </i> Mol Biosyst, 2017","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP03001r004","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T15:04:10.424Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":457,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"The near-UV CD spectra of the V proteins are rather smooth suggesting a predominantly disordered nature.","type":"Results"}],"term_name":"disorder","ec_name":"near-UV circular dichroism evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2023_06","term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"28972216","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006206","curator_id":"tlazar","reference_html":"The Henipavirus V protein is a prevalently unfolded protein with a zinc-finger domain involved in binding to DDB1. <i> Salladini E, Delauzun V, Longhi S. </i> Mol Biosyst, 2017","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP03001r005","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T15:04:09.856Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":457,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"observed Rg values and those expected for a globular/spherical form, together with the fact that they are even larger than the values expected for IDPs indicate that the V proteins are highly disordered","type":"Results"}],"term_name":"disorder","ec_name":"small-angle X-ray scattering evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2023_06","term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"28972216","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006210","curator_id":"tlazar","reference_html":"The Henipavirus V protein is a prevalently unfolded protein with a zinc-finger domain involved in binding to DDB1. <i> Salladini E, Delauzun V, Longhi S. </i> Mol Biosyst, 2017","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP03001r006","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T15:04:09.255Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":457,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"Labeled DDB1 was then titrated with unlabeled V. Results allowed us to infer an equilibrium dissociation constant (KD) of 32 +/- 6 nM for HeV V","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q16531","partner_end":null}],"term_name":"protein binding","ec_name":"microscale thermophoresis evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2023_06","term_ontology":"GO","curator_name":"Tamas Lazar","reference_id":"28972216","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006303","curator_id":"tlazar","reference_html":"The Henipavirus V protein is a prevalently unfolded protein with a zinc-finger domain involved in binding to DDB1. <i> Salladini E, Delauzun V, Longhi S. </i> Mol Biosyst, 2017","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":173,"end":178,"reference_id":"29321677","reference_source":"pmid","reference_html":"Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V. <i> Atkinson SC, Audsley MD, Lieu KG, Marsh GA, Thomas DR, Heaton SM, Paxman JJ, Wagstaff KM, Buckle AM, Moseley GW, Jans DA, Borg NA. </i> Sci Rep, 2018","date":"2024-03-06T15:14:21.638Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0075733","term_name":"intracellular transport of virus","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu177Ala","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP03001r007","statement":[{"text":"In untreated cells the HeV V double leucine mutant (VL174A/L177A) showed a significant increase (p < 0.0001) in nuclear localization compared to wild-type V (Fig. 1c,d), suggesting loss of exportin-1-mediated nuclear export of V. Consistent with this, HeV VL174A/L177A nuclear localization was not strongly affected by LMB treatment (Fig. 1c,d). Together, these data indicate that exportin-1-mediated nuclear export of HeV V is dependent on residues L174 and L177, and that the NES from NiV V is conserved in HeV V.\n\n","type":"Results"}],"term_comment":"","term_def":"\"The directed movement of a virus, or part of a virus, within the host cell.\" [GOC:ai, GOC:bf, GOC:jl, PMID:11733033]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-07T13:47:14.792Z"}},{"start":173,"end":178,"reference_id":"29321677","reference_source":"pmid","reference_html":"Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V. <i> Atkinson SC, Audsley MD, Lieu KG, Marsh GA, Thomas DR, Heaton SM, Paxman JJ, Wagstaff KM, Buckle AM, Moseley GW, Jans DA, Borg NA. </i> Sci Rep, 2018","date":"2024-03-07T14:54:30.900Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu174Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu177Ala","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"O14980","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P62826","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP03001r008","statement":[{"text":"As expected, the absence of a larger sedimenting species when VL174A/L177A was incubated with exportin-1/Ran-GTP (Fig. 3c) confirmed that L174 and L177 within the HeV V NES are critical to exportin-1/Ran-GTP binding.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-08T14:52:08.874Z"}},{"start":173,"end":178,"reference_id":"29321677","reference_source":"pmid","reference_html":"Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V. <i> Atkinson SC, Audsley MD, Lieu KG, Marsh GA, Thomas DR, Heaton SM, Paxman JJ, Wagstaff KM, Buckle AM, Moseley GW, Jans DA, Borg NA. </i> Sci Rep, 2018","date":"2024-03-07T14:53:37.845Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0031267","term_name":"small GTPase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu174Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu177Ala","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P62826","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03001r010","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O14980"}],"statement":[{"text":"As expected, the absence of a larger sedimenting species when VL174A/L177A was incubated with exportin-1/Ran-GTP (Fig. 3c) confirmed that L174 and L177 within the HeV V NES are critical to exportin-1/Ran-GTP binding.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a small monomeric GTPase.\" [GOC:mah, PMID:27218782]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-08T14:52:16.347Z"}},{"start":1,"end":457,"reference_id":"29321677","reference_source":"pmid","reference_html":"Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V. <i> Atkinson SC, Audsley MD, Lieu KG, Marsh GA, Thomas DR, Heaton SM, Paxman JJ, Wagstaff KM, Buckle AM, Moseley GW, Jans DA, Borg NA. </i> Sci Rep, 2018","date":"2024-03-07T14:53:03.267Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P52293","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P70168","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P62826","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"O1498","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP03001r011","statement":[{"text":"The formation of a larger sedimenting species when HeV V was incubated with equimolar concentrations of importin α2/β1 (8.1 S) or exportin-1/Ran-GTP (6.7 S) confirmed HeV V bound either importin α2/β1 and exportin-1/Ran-GTP directly (Fig. 3a,b and Supplementary Table 1).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-08T14:52:29.968Z"}},{"start":1,"end":457,"reference_id":"29321677","reference_source":"pmid","reference_html":"Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V. <i> Atkinson SC, Audsley MD, Lieu KG, Marsh GA, Thomas DR, Heaton SM, Paxman JJ, Wagstaff KM, Buckle AM, Moseley GW, Jans DA, Borg NA. </i> Sci Rep, 2018","date":"2024-03-07T14:52:43.339Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0031267","term_name":"small GTPase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P62826","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03001r012","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O14980"}],"statement":[{"text":"The formation of a larger sedimenting species when HeV V was incubated with equimolar concentrations of importin α2/β1 (8.1 S) or exportin-1/Ran-GTP (6.7 S) confirmed HeV V bound either importin α2/β1 and exportin-1/Ran-GTP directly (Fig. 3a,b and Supplementary Table 1).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a small monomeric GTPase.\" [GOC:mah, PMID:27218782]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-08T14:52:32.752Z"}},{"start":1,"end":457,"reference_id":"29321677","reference_source":"pmid","reference_html":"Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V. <i> Atkinson SC, Audsley MD, Lieu KG, Marsh GA, Thomas DR, Heaton SM, Paxman JJ, Wagstaff KM, Buckle AM, Moseley GW, Jans DA, Borg NA. </i> Sci Rep, 2018","date":"2024-03-07T14:52:16.217Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0061676","term_name":"importin-alpha family protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P52293","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03001r013","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P70168"}],"statement":[{"text":"The formation of a larger sedimenting species when HeV V was incubated with equimolar concentrations of importin α2/β1 (8.1 S) or exportin-1/Ran-GTP (6.7 S) confirmed HeV V bound either importin α2/β1 and exportin-1/Ran-GTP directly (Fig. 3a,b and Supplementary Table 1).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a member of the importin-alpha family.\" [PMID:15350979, PMID:17170104, PMID:23734157]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-08T14:52:37.873Z"}},{"start":51,"end":405,"reference_id":"29321677","reference_source":"pmid","reference_html":"Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V. <i> Atkinson SC, Audsley MD, Lieu KG, Marsh GA, Thomas DR, Heaton SM, Paxman JJ, Wagstaff KM, Buckle AM, Moseley GW, Jans DA, Borg NA. </i> Sci Rep, 2018","date":"2024-03-07T14:51:04.770Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P62826 ","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"O14980","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP03001r014","statement":[{"text":"In contrast, binding was observed when both V1-405 (Fig. 3e) or V51-457 (Fig. 3g) were mixed with exportin-1/Ran-GTP, indicating that neither the C-terminal region (residues 406–457) nor N-terminal 50 residues of V are critical for exportin-1/Ran-GTP binding.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-08T14:53:12.033Z"}},{"start":51,"end":405,"reference_id":"29321677","reference_source":"pmid","reference_html":"Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V. <i> Atkinson SC, Audsley MD, Lieu KG, Marsh GA, Thomas DR, Heaton SM, Paxman JJ, Wagstaff KM, Buckle AM, Moseley GW, Jans DA, Borg NA. </i> Sci Rep, 2018","date":"2024-03-07T14:50:01.649Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0031267","term_name":"small GTPase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P62826","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03001r016","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O14980"}],"statement":[{"text":"In contrast, binding was observed when both V1-405 (Fig. 3e) or V51-457 (Fig. 3g) were mixed with exportin-1/Ran-GTP, indicating that neither the C-terminal region (residues 406–457) nor N-terminal 50 residues of V are critical for exportin-1/Ran-GTP binding.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a small monomeric GTPase.\" [GOC:mah, PMID:27218782]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-08T14:53:33.196Z"}},{"start":1,"end":50,"reference_id":"29321677","reference_source":"pmid","reference_html":"Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V. <i> Atkinson SC, Audsley MD, Lieu KG, Marsh GA, Thomas DR, Heaton SM, Paxman JJ, Wagstaff KM, Buckle AM, Moseley GW, Jans DA, Borg NA. </i> Sci Rep, 2018","date":"2024-03-06T15:32:18.606Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0061676","term_name":"importin-alpha family protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P52293","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03001r017","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P70168"}],"statement":[{"text":"Similarly, we observed binding when V1–405 was incubated with importin α2/β1 (Fig. 3f), but not upon incubation of V51-457 with importin α2/β1 (Fig. 3h). This suggests that the first 50 residues of V are required for interaction with importin α2/β1.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a member of the importin-alpha family.\" [PMID:15350979, PMID:17170104, PMID:23734157]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-07T13:56:02.716Z"}},{"start":1,"end":457,"reference_id":"29321677","reference_source":"pmid","reference_html":"Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V. <i> Atkinson SC, Audsley MD, Lieu KG, Marsh GA, Thomas DR, Heaton SM, Paxman JJ, Wagstaff KM, Buckle AM, Moseley GW, Jans DA, Borg NA. </i> Sci Rep, 2018","date":"2024-03-07T14:48:30.763Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0075733","term_name":"intracellular transport of virus","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007060","ec_ontology":"ECO","ec_name":"confocal laser scanning microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IDA","region_id":"DP03001r020","statement":[{"text":"In untreated cells, HeV P and V were excluded from the nucleus, whereas W showed strong nuclear localization, but was excluded from structures consistent with nucleoli (Fig. 1a,b). Following LMB treatment HeV V showed a marked increase in nuclear localization (p < 0.0001), but remained excluded from nucleoli (Fig. 1a,b), providing the first empirical evidence that HeV V undergoes exportin-1-dependent nuclear export.","type":"Results"}],"term_comment":"","term_def":"\"The directed movement of a virus, or part of a virus, within the host cell.\" [GOC:ai, GOC:bf, GOC:jl, PMID:11733033]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-08T14:54:22.117Z"}},{"start":1,"end":457,"reference_id":"29321677","reference_source":"pmid","reference_html":"Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V. <i> Atkinson SC, Audsley MD, Lieu KG, Marsh GA, Thomas DR, Heaton SM, Paxman JJ, Wagstaff KM, Buckle AM, Moseley GW, Jans DA, Borg NA. </i> Sci Rep, 2018","date":"2024-03-06T15:39:11.885Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0075733","term_name":"intracellular transport of virus","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001585","ec_ontology":"ECO","ec_name":"small interfering RNA knockdown evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IMP","region_id":"DP03001r021","statement":[{"text":"A significant (p < 0.0001) increase in the extent of nuclear accumulation of wild-type HeV V was observed in cells transfected with XPO1 siRNA, compared to mock-treated cells and those transfected with Scr siRNA (Fig. 1f,g).","type":"Results"}],"term_comment":"","term_def":"\"The directed movement of a virus, or part of a virus, within the host cell.\" [GOC:ai, GOC:bf, GOC:jl, PMID:11733033]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-07T14:04:31.805Z"}},{"start":1,"end":405,"reference_id":"29321677","reference_source":"pmid","reference_html":"Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V. <i> Atkinson SC, Audsley MD, Lieu KG, Marsh GA, Thomas DR, Heaton SM, Paxman JJ, Wagstaff KM, Buckle AM, Moseley GW, Jans DA, Borg NA. </i> Sci Rep, 2018","date":"2024-03-07T09:37:30.180Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP03001r022","statement":[{"text":"Using CD we observed full-length HeV V displayed a single minimum at around 200 nm, which is indicative of a largely unstructured protein. Also apparent was broad but weak negative ellipticity between 215 and 235 nm, indicative of a small proportion of residual secondary structure that is absent in the CD spectra of V1-405. Based on this data we concur HeV V1-405 is predominantly intrinsically disordered (Supplementary Fig. 7a).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-07T14:04:59.242Z"}},{"start":1,"end":50,"reference_id":"29321677","reference_source":"pmid","reference_html":"Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V. <i> Atkinson SC, Audsley MD, Lieu KG, Marsh GA, Thomas DR, Heaton SM, Paxman JJ, Wagstaff KM, Buckle AM, Moseley GW, Jans DA, Borg NA. </i> Sci Rep, 2018","date":"2024-03-07T14:46:01.603Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP03001r027","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O14980"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62826"}],"statement":[{"text":"In contrast, V structural gain was negligible upon mixing VL174/L177A or V51-457 with equimolar exportin-1/Ran-GTP (Fig. 4c,g magenta vs gray). This was expected for VL174/L177A since it does not bind to exportin-1/Ran-GTP (Fig. 3c), but not for V51-457, since the first 50 residues are dispensable for exportin-1/Ran-GTP binding (Fig. 3g). These studies suggest that HeV V residues 1–50, which are the only residues with predicted secondary structure in the shared P/V/W-N-terminal region, are critical to the disorder-to-order transition of V upon binding to exportin-1/Ran-GTP.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-08T14:55:19.798Z"}},{"start":1,"end":457,"reference_id":"29321677","reference_source":"pmid","reference_html":"Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V. <i> Atkinson SC, Audsley MD, Lieu KG, Marsh GA, Thomas DR, Heaton SM, Paxman JJ, Wagstaff KM, Buckle AM, Moseley GW, Jans DA, Borg NA. </i> Sci Rep, 2018","date":"2024-03-05T14:12:53.124Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP03001r029","statement":[{"text":"In contrast, the Kratky plot of V (Fig. 5e,f, black) lacked a well-defined peak and plateaued at high s values, as is typical of an unfolded protein. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-06T16:51:26.961Z"}},{"start":1,"end":457,"reference_id":"29321677","reference_source":"pmid","reference_html":"Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V. <i> Atkinson SC, Audsley MD, Lieu KG, Marsh GA, Thomas DR, Heaton SM, Paxman JJ, Wagstaff KM, Buckle AM, Moseley GW, Jans DA, Borg NA. </i> Sci Rep, 2018","date":"2024-04-08T17:38:18.656Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1901344","term_name":"response to leptomycin B","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007060","ec_ontology":"ECO","ec_name":"confocal laser scanning microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IDA","region_id":"DP03001r030","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0059","entry_name":"Verda reno"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"52646","entry_name":"leptomycin B"}],"statement":[{"text":"In untreated cells, HeV P and V were excluded from the nucleus, whereas W showed strong nuclear localization, but was excluded from structures consistent with nucleoli (Fig. 1a,b). Following LMB treatment HeV V showed a marked increase in nuclear localization (p < 0.0001), but remained excluded from nucleoli (Fig. 1a,b), providing the first empirical evidence that HeV V undergoes exportin-1-dependent nuclear export.","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a leptomycin B stimulus.\" [GOC:TermGenie]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":457,"reference_id":"29321677","reference_source":"pmid","reference_html":"Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V. <i> Atkinson SC, Audsley MD, Lieu KG, Marsh GA, Thomas DR, Heaton SM, Paxman JJ, Wagstaff KM, Buckle AM, Moseley GW, Jans DA, Borg NA. </i> Sci Rep, 2018","date":"2024-03-06T15:11:28.372Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0520","term_name":"HA","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"O14980","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03001r031","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"statement":[{"text":"Consistent with the above results, coimmunoprecipitation revealed endogenous exportin-1 could readily interact with HA-fused wild-type HeV V, but the interaction with HA-tagged VL174A/L177A appeared reduced in comparison (Fig. 1h, Supplementary Fig. 4).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":457,"reference_id":"29321677","reference_source":"pmid","reference_html":"Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V. <i> Atkinson SC, Audsley MD, Lieu KG, Marsh GA, Thomas DR, Heaton SM, Paxman JJ, Wagstaff KM, Buckle AM, Moseley GW, Jans DA, Borg NA. </i> Sci Rep, 2018","date":"2024-03-06T15:13:28.740Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0061676","term_name":"importin-alpha family protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P52292","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03001r032","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"statement":[{"text":"Consistent with this result, GFP-fused V coimmunoprecipitated endogenous importin α1 to levels comparable to those of a GFP-fusion protein containing the prototypic importin α/β1-recognized NLS from simian virus (SV40) large tumour antigen GFP-T-Ag NLS (Fig. 2e, Supplementary Fig. 6).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a member of the importin-alpha family.\" [PMID:15350979, PMID:17170104, PMID:23734157]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":457,"reference_id":"29321677","reference_source":"pmid","reference_html":"Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V. <i> Atkinson SC, Audsley MD, Lieu KG, Marsh GA, Thomas DR, Heaton SM, Paxman JJ, Wagstaff KM, Buckle AM, Moseley GW, Jans DA, Borg NA. </i> Sci Rep, 2018","date":"2024-03-06T15:14:46.255Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0075733","term_name":"intracellular transport of virus","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP03001r033","statement":[{"text":"Taken together, results suggest HeV V shuttles dynamically between the host cell nucleus and cytosol, accessing the nucleus by subverting importin α1 of the host nuclear transport system.","type":"Results"}],"term_comment":"","term_def":"\"The directed movement of a virus, or part of a virus, within the host cell.\" [GOC:ai, GOC:bf, GOC:jl, PMID:11733033]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":457,"reference_id":"29321677","reference_source":"pmid","reference_html":"Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V. <i> Atkinson SC, Audsley MD, Lieu KG, Marsh GA, Thomas DR, Heaton SM, Paxman JJ, Wagstaff KM, Buckle AM, Moseley GW, Jans DA, Borg NA. </i> Sci Rep, 2018","date":"2024-04-08T17:58:16.279Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0030430","term_name":"host cell cytoplasm","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005589","ec_ontology":"ECO","ec_name":"confocal microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP03001r034","statement":[{"text":"In untreated cells, HeV P and V were excluded from the nucleus, whereas W showed strong nuclear localization, but was excluded from structures consistent with nucleoli (Fig. 1a,b).","type":"Results"},{"text":"Despite the fact that P, V and W share the exportin-1 recognized NES shown to be active for V here, there are inherent differences in the steady-state localization of the P-gene encoded products, whereby V is predominantly cytoplasmic and W is predominantly nuclear, implying the unique C-terminal regions of these proteins contribute strongly to nucleocytoplasmic trafficking (see16,33).","type":"Discussion"}],"term_comment":"","term_def":"\"The cytoplasm of a host cell.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IDA","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0059","entry_name":"Verda reno"}]}],"released":"2023_06","length":457,"ncbi_taxon_id":928303,"organism":"Hendra virus (isolate Horse/Autralia/Hendra/1994)","disprot_id":"DP03001","date":"2020-12-02T10:03:53.502Z","regions_counter":34,"dataset":["Viral proteins"],"UniParc":"UPI00000F0415","uniref100":"UniRef100_O55777","uniref90":"UniRef90_O55777","uniref50":"UniRef50_Q997F2","genes":[{"name":{"value":"P/V/C"}}],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":50,"type":"T"},{"start":51,"end":457,"type":"D"}],"Structural state":[{"start":1,"end":457,"type":"D"}],"Molecular function":[{"start":1,"end":457,"type":"F"}],"Biological process":[{"start":1,"end":457,"type":"F"}],"Structural transition":[{"start":1,"end":50,"type":"T"}],"Cellular component":[{"start":1,"end":457,"type":"F"}]}},{"acc":"P59636","features":{"pfam":[{"id":"PF09399","name":"Betacoronavirus lipid binding protein","start":1,"end":98}],"gene3D":[]},"creator":"tlazar","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Nidovirales","Cornidovirineae","Coronaviridae","Orthocoronavirinae","Betacoronavirus","Sarbecovirus"],"sequence":"MDPNQTNVVPPALHLVDPQIQLTITRMEDAMGQGQNSADPKVYPIILRLGSQLSLSMARRNLDSLEARAFQSTPIVVQMTKLATTEELPDEFVVVTAK","name":"ORF9b protein","regions":[{"region_id":"DP03002r001","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-02T15:00:46.313Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":37,"term_id":"IDPO:0000002","start":26,"version":2,"statement":[{"text":"in the electron density map, two regions near the N terminus (residues 1–8 and 26–37) are not resolved. Both of these disordered segments are located on the periphery of the structure, whereas the inner core of the protein is reasonably well ordered.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2022_03","term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"16843897","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2CME"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"tlazar","reference_html":"The crystal structure of ORF-9b, a lipid binding protein from the SARS coronavirus. <i> Meier C, Aricescu AR, Assenberg R, Aplin RT, Gilbert RJ, Grimes JM, Stuart DI. </i> Structure, 2006","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_12","length":98,"ncbi_taxon_id":694009,"organism":"Severe acute respiratory syndrome coronavirus","disprot_id":"DP03002","date":"2020-12-02T12:29:46.921Z","regions_counter":1,"dataset":["Viral proteins"],"UniParc":"UPI000018DB78","uniref100":"UniRef100_P59636","uniref90":"UniRef90_P59636","uniref50":"UniRef50_P59636","genes":[{"orfNames":[{"value":"9b"}]}],"disorder_content":0.12244897959183673,"disprot_consensus":{"full":[{"start":26,"end":37,"type":"D"}],"Structural state":[{"start":26,"end":37,"type":"D"}]}},{"acc":"P0DTC3","features":{"pfam":[{"id":"PF11289","name":"Betacoronavirus viroporin","start":1,"end":274}],"gene3D":[]},"name":"ORF3a protein","creator":"esalladini","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Nidovirales","Cornidovirineae","Coronaviridae","Orthocoronavirinae","Betacoronavirus","Sarbecovirus"],"sequence":"MDLFMRIFTIGTVTLKQGEIKDATPSDFVRATATIPIQASLPFGWLIVGVALLAVFQSASKIITLKKRWQLALSKGVHFVCNLLLLFVTVYSHLLLVAAGLEAPFLYLYALVYFLQSINFVRIIMRLWLCWKCRSKNPLLYDANYFLCWHTNCYDYCIPYNSVTSSIVITSGDGTTSPISEHDYQIGGYTEKWESGVKDCVVLHSYFTSDYYQLYSTQLSTDTGVEHVTFFIYNKIVDEPEEHVQIHTIDGSSGVVNPVMEPIYDEPTTTTSVPL","dataset":["Viral proteins"],"regions":[{"region_id":"DP03003r001","ec_ontology":"ECO","end":39,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"The N-terminus (amino acids 1–39), C-terminus (amino acids 239–275), and a short cytoplasmic loop (amino acids 175–180) are either not observed or weakly resolved in the density map, presumably due to conformational differences between particles or because they are disordered.","type":"Results"}],"term_name":"disorder","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"32587976","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"7KJR"},{"db":"PDB","id":"6XDC"}],"term_namespace":"Structural state","ec_id":"ECO:0006224","curator_id":"fquaglia","reference_html":"","validated":{"curator_name":"Attila Meszaros","curator_id":"ameszaros","timestamp":"2021-07-01T09:40:08.755Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP03003r002","ec_ontology":"ECO","end":275,"term_id":"IDPO:0000002","start":239,"version":2,"statement":[{"text":"The N-terminus (amino acids 1–39), C-terminus (amino acids 239–275), and a short cytoplasmic loop (amino acids 175–180) are either not observed or weakly resolved in the density map, presumably due to conformational differences between particles or because they are disordered.","type":"Results"}],"term_name":"disorder","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"32587976","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"7KJR"},{"db":"PDB","id":"6XDC"}],"term_namespace":"Structural state","ec_id":"ECO:0006224","curator_id":"fquaglia","reference_html":"","validated":{"curator_name":"Attila Meszaros","curator_id":"ameszaros","timestamp":"2021-07-01T09:40:06.509Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Cellular component","ec_ontology":"ECO","end":41,"term_name":"cytoplasmic side of plasma membrane","reference_html":"Cryo-EM structure of the SARS-CoV-2 3a ion channel in lipid nanodiscs.  <i> Kern DM, Sorum B, Mali SS, Mali SS, Hoel CM, Sridharan S, Remis JP, Toso DB, Kotecha A, Bautista DM, Brohawn SG. </i> bioRxiv, 2021","start":1,"region_id":"DP03003r003","term_id":"GO:0009898","version":4,"curator_id":"vnugnes","released":"2023_12","term_ontology":"GO","curator_name":"Victoria Nugnes","ec_name":"fluorescence microscopy evidence used in manual assertion","statement":[{"text":"The 3a N-terminus is involved in subcellular localization","type":"Results"},{"text":"These results are consistent with the N-terminal region of 3a being a determinant of its subcellular localization without influencing channel properties.","type":"Results"},{"text":"The N-terminal ~41 residues of each chain constitute the majority of the extracellularly or lumenally exposed 3a protein and thus could be involved in retention of 3a to internal membranes in cultured cells. To test this, we generated an N-terminal deletion construct lacking the first 41 amino acids (3aΔN) and compared its localization to wild-type 3a in HEK cells. Indeed, 3aΔN-EGFP shows reduced localization to internal membranes and bright foci and increased plasma membrane expression (Fig. 4A, S12). While we were unable to model the N-terminal 39 residues of 3a, we note an unassigned density feature in the cryo-EM maps that stretches between subunits just above the extracellular entrance to the pore that could correspond to a portion of these unmodeled N-terminal residues (Fig. 4B). We speculated that if the N-terminal region was stably positioned above the mouth of the pore it could influence channel properties.","type":"Results"}],"curator_orcid":"0000-0001-8399-7907","date":"2023-08-22T14:01:15.083Z","reference_source":"pmid","ec_id":"ECO:0006323","reference_id":"32587976","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The leaflet the plasma membrane that faces the cytoplasm and any proteins embedded or anchored in it or attached to its surface.\" [GOC:dos, GOC:tb]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-26T15:28:07.121Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":40,"term_name":"molecular function activator activity","reference_html":"Severe acute respiratory syndrome coronavirus ORF3a protein activates the NLRP3 inflammasome by promoting TRAF3-dependent ubiquitination of ASC. <i> Siu KL, Yuen KS, Castaño-Rodriguez C, Ye ZW, Yeung ML, Fung SY, Yuan S, Chan CP, Yuen KY, Enjuanes L, Jin DY. </i> FASEB J, 2019","start":36,"region_id":"DP03003r004","term_id":"GO:0140677","version":4,"curator_id":"fquaglia","released":"2022_03","term_ontology":"GO","curator_name":"Federica Quaglia","ec_name":"mutant phenotype evidence used in manual assertion","statement":[{"text":"Definition of a TRAF binding domain in ORF3a required for activation of NF-κB and IL-1β secretion.","type":"Results"},{"text":"A TRAF-binding motif, PLQAS, consistent with the consensus sequence PxQx(T/S/D) in which x could be any residue, was located at aa 36–40 of ORF3a. To define their necessity for the NF-κB- and inflammasome-activating activity of ORF3a, 3 point mutants designated M-T, M-I, and M-C were created to disrupt the TRAF binding, ion channel, and caveolin binding domains, respectively (Fig. 4A). In M-T, 3 conserved residues (P, Q, and S) in the TRAF-binding motif were changed into A. In M-I, 3 conserved C residues required for ion channel activity (14, 24) were changed into S. Finally, 3 conserved Y residues in the caveolin-binding motif were changed into A in M-C.","type":"Results"},{"text":"Interestingly, the M-C and M-I mutants were fully competent in the activation of NF-κB and the NLRP3 inflammasome (Fig. 4B, bars 5–8 vs. 3 and 4; Fig. 4C, lanes 2 and 3 vs. 1). In sharp contrast, the M-T mutant lost its ability to activate either IL-8–Luc or IL-1β secretion (Fig. 4B, bars 9 and 10 vs. 3 and 4; Fig. 4C, lane 4 vs. 1). In other words, TRAF binding was essential for NF-κB and NLRP3 inflammasome activation by ORF3a. Surprisingly, neither caveolin binding nor the ion channel was required for this activity.","type":"Results"}],"curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0000315","reference_id":"31034780","validated":{"curator_name":"Attila Meszaros","curator_id":"ameszaros","timestamp":"2021-07-02T09:26:35.958Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":40,"term_name":"protein binding","reference_html":"Severe acute respiratory syndrome coronavirus ORF3a protein activates the NLRP3 inflammasome by promoting TRAF3-dependent ubiquitination of ASC. <i> Siu KL, Yuen KS, Castaño-Rodriguez C, Ye ZW, Yeung ML, Fung SY, Yuan S, Chan CP, Yuen KY, Enjuanes L, Jin DY. </i> FASEB J, 2019","start":36,"region_id":"DP03003r005","term_id":"GO:0005515","version":4,"curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","ec_name":"co-immunoprecipitation evidence used in manual assertion","statement":[{"text":"When we immunoprecipitated TRAF2, 3, and 6 with an anti-FLAG antibody, ORF3a but not its M-T mutant was detected in the precipitate (Fig. 5A, lanes 1, 3, and 5 vs. 2, 4, and 6). These results indicated that ORF3a was capable of interacting with TRAF2, 3, and 6, but this ability was abrogated in the M-T mutant.","type":"Results"},{"text":"The TRAF binding domain is required for the association of ORF3a with TRAF2, 3, and 6 and ASC.","type":"Figure"}],"curator_orcid":"0000-0002-5152-5953","date":"2022-03-08T14:08:03.982Z","reference_source":"pmid","ec_id":"ECO:0006030","reference_id":"31034780","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q12933","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q13114","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q13114","operator":"or","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-12T14:21:50.242Z"}},{"start":36,"end":40,"reference_id":"31034780","reference_source":"pmid","reference_html":"Severe acute respiratory syndrome coronavirus ORF3a protein activates the NLRP3 inflammasome by promoting TRAF3-dependent ubiquitination of ASC. <i> Siu KL, Yuen KS, Castaño-Rodriguez C, Ye ZW, Yeung ML, Fung SY, Yuan S, Chan CP, Yuen KY, Enjuanes L, Jin DY. </i> FASEB J, 2019","date":"2022-03-08T14:08:38.200Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","released":"2022_03","version":4,"region_id":"DP03003r006","statement":[{"text":"A TRAF-binding motif, PLQAS, consistent with the consensus sequence PxQx(T/S/D) in which x could be any residue, was located at aa 36–40 of ORF3a. To define their necessity for the NF-κB- and inflammasome-activating activity of ORF3a, 3 point mutants designated M-T, M-I, and M-C were created to disrupt the TRAF binding, ion channel, and caveolin binding domains, respectively (Fig. 4A). In M-T, 3 conserved residues (P, Q, and S) in the TRAF-binding motif were changed into A. In M-I, 3 conserved C residues required for ion channel activity (14, 24) were changed into S. Finally, 3 conserved Y residues in the caveolin-binding motif were changed into A in M-C.","type":"Results"},{"text":"Interestingly, the M-C and M-I mutants were fully competent in the activation of NF-κB and the NLRP3 inflammasome (Fig. 4B, bars 5–8 vs. 3 and 4; Fig. 4C, lanes 2 and 3 vs. 1). In sharp contrast, the M-T mutant lost its ability to activate either IL-8–Luc or IL-1β secretion (Fig. 4B, bars 9 and 10 vs. 3 and 4; Fig. 4C, lane 4 vs. 1). In other words, TRAF binding was essential for NF-κB and NLRP3 inflammasome activation by ORF3a. Surprisingly, neither caveolin binding nor the ion channel was required for this activity.","type":"Results"}],"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q12933","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q13114","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9Y4K3","operator":"or","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-12T14:21:50.723Z"}}],"released":"2020_12","length":275,"ncbi_taxon_id":2697049,"organism":"Severe acute respiratory syndrome coronavirus 2","disprot_id":"DP03003","date":"2020-12-03T11:03:17.250Z","regions_counter":7,"UniParc":"UPI00131EFFEB","uniref100":"UniRef100_P0DTC3","uniref90":"UniRef90_P0DTC3","uniref50":"UniRef50_P59632","genes":[{"orfNames":[{"value":"3a"}]}],"disorder_content":0.27636363636363637,"disprot_consensus":{"full":[{"start":1,"end":39,"type":"D"},{"start":40,"end":41,"type":"F"},{"start":239,"end":275,"type":"D"}],"Structural state":[{"start":1,"end":39,"type":"D"},{"start":239,"end":275,"type":"D"}],"Cellular component":[{"start":1,"end":41,"type":"F"}],"Molecular function":[{"start":36,"end":40,"type":"F"}]}},{"acc":"P58004","features":{"pfam":[{"id":"PF04636","name":"PA26 p53-induced protein (sestrin)","start":44,"end":479}],"gene3D":[]},"creator":"ldobson","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MIVADSECRAELKDYLRFAPGGVGDSGPGEEQRESRARRGPRGPSAFIPVEEVLREGAESLEQHLGLEALMSSGRVDNLAVVMGLHPDYFTSFWRLHYLLLHTDGPLASSWRHYIAIMAAARHQCSYLVGSHMAEFLQTGGDPEWLLGLHRAPEKLRKLSEINKLLAHRPWLITKEHIQALLKTGEHTWSLAELIQALVLLTHCHSLSSFVFGCGILPEGDADGSPAPQAPTPPSEQSSPPSRDPLNNSGGFESARDVEALMERMQQLQESLLRDEGTSQEEMESRFELEKSESLLVTPSADILEPSPHPDMLCFVEDPTFGYEDFTRRGAQAPPTFRAQDYTWEDHGYSLIQRLYPEGGQLLDEKFQAAYSLTYNTIAMHSGVDTSVLRRAIWNYIHCVFGIRYDDYDYGEVNQLLERNLKVYIKTVACYPEKTTRRMYNLFWRHFRHSEKVHVNLLLLEARMQAALLYALRAITRYMT","name":"Sestrin-2","regions":[{"region_id":"DP03004r003","unpublished":true,"ec_ontology":"ECO","end":309,"term_id":"IDPO:0000033","start":296,"version":3,"statement":[{"text":"Sestrin2 is a 55 kDa, monomeric, all α-helical, globular protein that contains distinct N-terminal [NTD, residues 66–220] and C-terminal [CTD, residues 339–480] domains connected by a partially disordered, partially helical linker region [Linker, residues 221–338] ","type":"Results"},{"text":"Disordered residues not present in the crystal structure (1 to 65, 242 to 255, 272 to 280, 296 to 309) are shown as dashed lines","type":"Figure"}],"term_name":"flexible linker","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-2765-3872","released":"2022_03","term_ontology":"IDPO","curator_name":"László Dobson","reference_id":"26586190","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5DJ4"}],"term_namespace":"Disorder function","ec_id":"ECO:0006220","curator_id":"ldobson","reference_html":"Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway. <i> Saxton RA, Knockenhauer KE, Wolfson RL, Chantranupong L, Pacold ME, Wang T, Schwartz TU, Sabatini DM. </i> Science, 2016","validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-07T18:30:33.313Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"region_id":"DP03004r005","unpublished":true,"ec_ontology":"ECO","end":255,"term_id":"IDPO:0000033","start":240,"version":3,"statement":[{"text":"Region 240-255 is intrinsically disordered and is a flexible linker connecting Sesn-B and Sesn-C domains","type":"Curator statement"},{"text":"The overall structure is well-defined except for residues 1–65, 221–224, 240–255, 272–279, 295–307, 329–332 and 479–480","type":"Figure"},{"text":"\"The structure of full-length hSesn2 indicates that the protein contains three domains separated by two unstructured flexible linker regions (Fig. 1b)\"","type":"Results"}],"term_name":"flexible linker","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-2765-3872","released":"2022_03","term_ontology":"IDPO","curator_name":"László Dobson","reference_id":"26612684","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5CUF"}],"term_namespace":"Disorder function","ec_id":"ECO:0006220","curator_id":"ldobson","reference_html":"Janus-faced Sestrin2 controls ROS and mTOR signalling through two separate functional domains. <i> Kim H, An S, Ro SH, Teixeira F, Park GJ, Kim C, Cho CS, Kim JS, Jakob U, Lee JH, Cho US. </i> Nat Commun, 2015","validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-07T18:34:06.425Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"region_id":"DP03004r007","unpublished":true,"ec_ontology":"ECO","end":307,"term_id":"IDPO:0000033","start":295,"version":3,"statement":[{"text":"Region 295-307 is intrinsically disordered and is a flexible linker connecting Sesn-A and Sesn-B domains","type":"Curator statement"},{"text":"The overall structure is well-defined except for residues 1–65, 221–224, 240–255, 272–279, 295–307, 329–332 and 479–480.","type":"Figure"},{"text":"\"The structure of full-length hSesn2 indicates that the protein contains three domains separated by two unstructured flexible linker regions (Fig. 1b)\"","type":"Results"}],"term_name":"flexible linker","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-2765-3872","released":"2022_03","term_ontology":"IDPO","curator_name":"László Dobson","reference_id":"26612684","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5CUF"}],"term_namespace":"Disorder function","ec_id":"ECO:0006220","curator_id":"ldobson","reference_html":"Janus-faced Sestrin2 controls ROS and mTOR signalling through two separate functional domains. <i> Kim H, An S, Ro SH, Teixeira F, Park GJ, Kim C, Cho CS, Kim JS, Jakob U, Lee JH, Cho US. </i> Nat Commun, 2015","validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-07T18:34:07.201Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":1,"end":65,"reference_id":"26586190","reference_source":"pmid","reference_html":"Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway. <i> Saxton RA, Knockenhauer KE, Wolfson RL, Chantranupong L, Pacold ME, Wang T, Schwartz TU, Sabatini DM. </i> Science, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5DJ4"}],"region_id":"DP03004r013","statement":[{"text":"Disordered residues not present in the crystal structure (1 to 65, 242 to 255, 272 to 280, 296 to 309) are shown as dashed line","type":"Figure"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-07T18:28:53.806Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":241,"end":255,"reference_id":"26586190","reference_source":"pmid","reference_html":"Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway. <i> Saxton RA, Knockenhauer KE, Wolfson RL, Chantranupong L, Pacold ME, Wang T, Schwartz TU, Sabatini DM. </i> Science, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5DJ4"}],"region_id":"DP03004r014","statement":[{"text":"Disordered residues not present in the crystal structure (1 to 65, 242 to 255, 272 to 280, 296 to 309) are shown as dashed line","type":"Figure"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-07T18:28:53.018Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":296,"end":309,"reference_id":"26586190","reference_source":"pmid","reference_html":"Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway. <i> Saxton RA, Knockenhauer KE, Wolfson RL, Chantranupong L, Pacold ME, Wang T, Schwartz TU, Sabatini DM. </i> Science, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5DJ4"}],"region_id":"DP03004r015","statement":[{"text":"Disordered residues not present in the crystal structure (1 to 65, 242 to 255, 272 to 280, 296 to 309) are shown as dashed line","type":"Figure"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-07T18:28:52.135Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":222,"end":232,"reference_id":"26586190","reference_source":"pmid","reference_html":"Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway. <i> Saxton RA, Knockenhauer KE, Wolfson RL, Chantranupong L, Pacold ME, Wang T, Schwartz TU, Sabatini DM. </i> Science, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5DJ4"}],"region_id":"DP03004r016","statement":[{"text":"Disordered residues not present in the crystal structure (1 to 65, 242 to 255, 272 to 280, 296 to 309) are shown as dashed line","type":"Figure"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-07T18:28:51.308Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":222,"end":232,"reference_id":"26586190","reference_source":"pmid","reference_html":"Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway. <i> Saxton RA, Knockenhauer KE, Wolfson RL, Chantranupong L, Pacold ME, Wang T, Schwartz TU, Sabatini DM. </i> Science, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"5DJ4"}],"region_id":"DP03004r017","statement":[{"text":"\"Sestrin2 is a 55 kDa, monomeric, all α-helical, globular protein that contains distinct N-terminal [NTD, residues 66–220] and C-terminal [CTD, residues 339–480] domains connected by a partially disordered, partially helical linker region [Linker, residues 221–338] \"","type":"Results"},{"text":"\"Disordered residues not present in the crystal structure (1 to 65, 242 to 255, 272 to 280, 296 to 309) are shown as dashed lines\"","type":"Figure"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-07T18:30:51.773Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":241,"end":255,"reference_id":"26586190","reference_source":"pmid","reference_html":"Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway. <i> Saxton RA, Knockenhauer KE, Wolfson RL, Chantranupong L, Pacold ME, Wang T, Schwartz TU, Sabatini DM. </i> Science, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"5DJ4"}],"region_id":"DP03004r018","statement":[{"text":"\"Sestrin2 is a 55 kDa, monomeric, all α-helical, globular protein that contains distinct N-terminal [NTD, residues 66–220] and C-terminal [CTD, residues 339–480] domains connected by a partially disordered, partially helical linker region [Linker, residues 221–338] \"","type":"Results"},{"text":"\"Disordered residues not present in the crystal structure (1 to 65, 242 to 255, 272 to 280, 296 to 309) are shown as dashed lines\"","type":"Figure"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-07T18:31:04.590Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":295,"end":307,"reference_id":"26612684","reference_source":"pmid","reference_html":"Janus-faced Sestrin2 controls ROS and mTOR signalling through two separate functional domains. <i> Kim H, An S, Ro SH, Teixeira F, Park GJ, Kim C, Cho CS, Kim JS, Jakob U, Lee JH, Cho US. </i> Nat Commun, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5CUF"}],"region_id":"DP03004r019","statement":[{"text":"\"The overall structure is well-defined except for residues 1–65, 221–224, 240–255, 272–279, 295–307, 329–332 and 479–480\"","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-07T18:33:38.332Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":240,"end":255,"reference_id":"26612684","reference_source":"pmid","reference_html":"Janus-faced Sestrin2 controls ROS and mTOR signalling through two separate functional domains. <i> Kim H, An S, Ro SH, Teixeira F, Park GJ, Kim C, Cho CS, Kim JS, Jakob U, Lee JH, Cho US. </i> Nat Commun, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5CUF"}],"region_id":"DP03004r020","statement":[{"text":"\"The overall structure is well-defined except for residues 1–65, 221–224, 240–255, 272–279, 295–307, 329–332 and 479–480\"","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-07T18:33:39.143Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":65,"reference_id":"26612684","reference_source":"pmid","reference_html":"Janus-faced Sestrin2 controls ROS and mTOR signalling through two separate functional domains. <i> Kim H, An S, Ro SH, Teixeira F, Park GJ, Kim C, Cho CS, Kim JS, Jakob U, Lee JH, Cho US. </i> Nat Commun, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5CUF"}],"region_id":"DP03004r021","statement":[{"text":"\"The overall structure is well-defined except for residues 1–65, 221–224, 240–255, 272–279, 295–307, 329–332 and 479–480\"","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-07T18:33:28.641Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_12","length":480,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP03004","date":"2020-12-03T12:15:34.701Z","regions_counter":21,"dataset":["Autophagy-related proteins"],"UniParc":"UPI0000001C01","uniref100":"UniRef100_P58004","uniref90":"UniRef90_P58004","uniref50":"UniRef50_P58004","genes":[{"name":{"value":"SESN2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:20746","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:20746"}}]},"synonyms":[{"value":"Hi95","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12203114","url":"http://www.ncbi.nlm.nih.gov/pubmed/12203114","alternativeUrl":"https://europepmc.org/abstract/MED/12203114"}}]},{"value":"SEST2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12607115","url":"http://www.ncbi.nlm.nih.gov/pubmed/12607115","alternativeUrl":"https://europepmc.org/abstract/MED/12607115"}}]}]}],"alphafold_very_low_content":0.1625,"disorder_content":0.22291666666666668,"disprot_consensus":{"full":[{"start":1,"end":65,"type":"D"},{"start":222,"end":232,"type":"D"},{"start":240,"end":255,"type":"D"},{"start":295,"end":309,"type":"D"}],"Structural state":[{"start":1,"end":65,"type":"D"},{"start":222,"end":232,"type":"D"},{"start":240,"end":255,"type":"D"},{"start":295,"end":309,"type":"D"}],"Disorder function":[{"start":222,"end":232,"type":"F"},{"start":240,"end":255,"type":"F"},{"start":295,"end":309,"type":"F"}]}},{"acc":"Q53TN4","features":{"pfam":[{"id":"PF03188","name":"Eukaryotic cytochrome b561","start":49,"end":185}],"gene3D":[]},"creator":"zskalman","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MAMEGYWRFLALLGSALLVGFLSVIFALVWVLHYREGLGWDGSALEFNWHPVLMVTGFVFIQGIAIIVYRLPWTWKCSKLLMKSIHAGLNAVAAILAIISVVAVFENHNVNNIANMYSLHSWVGLIAVICYLLQLLSGFSVFLLPWAPLSLRAFLMPIHVYSGIVIFGTVIATALMGLTEKLIFSLRDPAYSTFPPEGVFVNTLGLLILVFGALIFWIVTRPQWKRPKEPNSTILHPNGGTEQGARGSMPAYSGNNMDKSDSELNSEVAARKRNLALDEAGQRSTM","name":"Cytochrome b reductase 1","regions":[{"region_id":"DP03005r001","validated":{"curator_id":"fquaglia","timestamp":"2020-12-03T15:31:05.340Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":286,"term_id":"IDPO:0000002","start":231,"version":2,"statement":[{"text":"Although full-length Dcytb (residues 1–286) was used for crystallization, the atomic model includes only residues 6–230 because the electron density map for the five N-terminal residues and the 56 C-terminal residues was disordered.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-4634-0433","released":"2022_03","term_ontology":"IDPO","curator_name":"Zsófia Kálmán","reference_id":"30272000","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5ZLG"},{"db":"PDB","id":"5ZLE"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"zskalman","reference_html":"Structural basis for promotion of duodenal iron absorption by enteric ferric reductase with ascorbate. <i> Ganasen M, Togashi H, Takeda H, Asakura H, Tosha T, Yamashita K, Hirata K, Nariai Y, Urano T, Yuan X, Hamza I, Mauk AG, Shiro Y, Sugimoto H, Sawai H. </i> Commun Biol, 2018","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":286,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP03005","date":"2020-12-03T12:47:12.306Z","regions_counter":1,"dataset":[],"UniParc":"UPI0000140B22","uniref100":"UniRef100_Q53TN4","uniref90":"UniRef90_Q53TN4","uniref50":"UniRef50_Q53TN4","genes":[{"name":{"value":"CYBRD1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:20797","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:20797"}}]},"synonyms":[{"value":"DCYTB","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12949720","url":"http://www.ncbi.nlm.nih.gov/pubmed/12949720","alternativeUrl":"https://europepmc.org/abstract/MED/12949720"}}]},{"value":"FRRS3"}]}],"alphafold_very_low_content":0.11538461538461539,"disorder_content":0.1958041958041958,"disprot_consensus":{"full":[{"start":231,"end":286,"type":"D"}],"Structural state":[{"start":231,"end":286,"type":"D"}]}},{"acc":"O95843","features":{"pfam":[{"id":"PF13202","name":"EF hand","start":63,"end":78},{"id":"PF13499","name":"EF-hand domain pair","start":90,"end":159}],"gene3D":[]},"creator":"zskalman","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MGNGKSIAGDQKAVPTQETHVWYRTFMMEYPSGLQTLHEFKTLLGLQGLNQKANKHIDQVYNTFDTNKDGFVDFLEFIAAVNLIMQEKMEQKLKWYFKLYDADGNGSIDKNELLDMFMAVQALNGQQTLSPEEFINLVFHKIDINNDGELTLEEFINGMAKDQDLLEIVYKSFDFSNVLRVICNGKQPDMETDSSKSPDKAGLGKVKMK","name":"Guanylyl cyclase-activating protein 3","regions":[{"start":186,"end":209,"reference_id":"16626734","reference_source":"pmid","reference_html":"The crystal structure of GCAP3 suggests molecular mechanism of GCAP-linked cone dystrophies. <i> Stephen R, Palczewski K, Sousa MC. </i> J Mol Biol, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2GGZ"}],"region_id":"DP03006r003","statement":[{"text":"In both molecules, and in spite of different packing contacts, 19 amino acids from the N–terminus and 24 from the C– terminus could not be traced, presumably due to conformational flexibility.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":22,"reference_id":"16626734","reference_source":"pmid","reference_html":"The crystal structure of GCAP3 suggests molecular mechanism of GCAP-linked cone dystrophies. <i> Stephen R, Palczewski K, Sousa MC. </i> J Mol Biol, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2GGZ"}],"region_id":"DP03006r004","statement":[{"text":"In both molecules, and in spite of different packing contacts, 19 amino acids from the N–terminus and 24 from the C– terminus could not be traced, presumably due to conformational flexibility.","type":"Results"},{"text":"\nThe region with missing residues in the PDB structure has a different numbering in UniProt and the publication, the region defined here follows the UniProt numbering.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":209,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP03006","date":"2020-12-03T14:50:03.219Z","regions_counter":4,"dataset":[],"UniParc":"UPI000013D131","uniref100":"UniRef100_O95843","uniref90":"UniRef90_O95843","uniref50":"UniRef50_O95843","genes":[{"name":{"value":"GUCA1C"},"synonyms":[{"value":"GCAP3"}]}],"alphafold_very_low_content":0.13875598086124402,"disorder_content":0.22009569377990432,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"},{"start":186,"end":209,"type":"D"}],"Structural state":[{"start":1,"end":22,"type":"D"},{"start":186,"end":209,"type":"D"}]}},{"acc":"P97784","features":{"pfam":[{"id":"PF00875","name":"DNA photolyase","start":5,"end":164},{"id":"PF03441","name":"FAD binding domain of DNA photolyase","start":288,"end":486}],"gene3D":[]},"creator":"vsagris","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MGVNAVHWFRKGLRLHDNPALKECIQGADTIRCVYILDPWFAGSSNVGINRWRFLLQCLEDLDANLRKLNSRLFVIRGQPADVFPRLFKEWNITKLSIEYDSEPFGKERDAAIKKLATEAGVEVIVRISHTLYDLDKIIELNGGQPPLTYKRFQTLVSKMEPLEMPADTITSDVIGKCMTPLSDDHDEKYGVPSLEELGFDTDGLSSAVWPGGETEALTRLERHLERKAWVANFERPRMNANSLLASPTGLSPYLRFGCLSCRLFYFKLTDLYKKVKKNSSPPLSLYGQLLWREFFYTAATNNPRFDKMEGNPICVQIPWDKNPEALAKWAEGRTGFPWIDAIMTQLRQEGWIHHLARHAVACFLTRGDLWISWEEGMKVFEELLLDADWSINAGSWMWLSCSSFFQQFFHCYCPVGFGRRTDPNGDYIRRYLPVLRGFPAKYIYDPWNAPEGIQKVAKCLIGVNYPKPMVNHAEASRLNIERMKQIYQQLSRYRGLGLLASVPSNSNGNGGLMGYAPGENVPSCSSSGNGGLMGYAPGENVPSCSGGNCSQGSGILHYAHGDSQQTHSLKQGRSSAGTGLSSGKRPSQEEDAQSVGPKVQRQSSN","name":"Cryptochrome-1","regions":[{"region_id":"DP03007r001","unpublished":true,"ec_ontology":"ECO","end":177,"term_id":"IDPO:0000002","start":167,"version":2,"statement":[{"text":"The extended loop between helices α6 and α8 (Met160mCRY1 to Gly213mCRY1) is partly disordered in mCRY1 (missing residues 167 to 177 and 203/204), and the region between Cys178mCRY1 and α8 significantly differs from dCRY (Figure 3A). ","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"23746849","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4K0R"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"jssuarez","reference_html":"Structures of Drosophila cryptochrome and mouse cryptochrome1 provide insight into circadian function. <i> Czarna A, Berndt A, Singh HR, Grudziecki A, Ladurner AG, Timinszky G, Kramer A, Wolf E. </i> Cell, 2013","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T10:00:48.186Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP03007r002","unpublished":true,"ec_ontology":"ECO","end":606,"term_id":"IDPO:0000002","start":498,"version":2,"statement":[{"text":"The full-length mCRY1 protein was spontaneously proteolysed to a mCRY1[1-497] fragment corresponding to the photolyase homology region (PHR).","type":"Methods"}],"term_name":"disorder","ec_name":"cleavage assay evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","reference_id":"23746849","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4K0R"}],"term_namespace":"Structural state","ec_id":"ECO:0007691","curator_id":"jssuarez","reference_html":"Structures of Drosophila cryptochrome and mouse cryptochrome1 provide insight into circadian function. <i> Czarna A, Berndt A, Singh HR, Grudziecki A, Ladurner AG, Timinszky G, Kramer A, Wolf E. </i> Cell, 2013","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T10:00:18.327Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":606,"term_name":"disorder","reference_html":"Quantitative analyses of cryptochrome-mBMAL1 interactions: mechanistic insights into the transcriptional regulation of the mammalian circadian clock. <i> Czarna A, Breitkreuz H, Mahrenholz CC, Arens J, Strauss HM, Wolf E. </i> J Biol Chem, 2011","start":471,"region_id":"DP03007r004","term_id":"IDPO:0000002","unpublished":true,"version":2,"curator_id":"jssuarez","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","ec_name":"analytical ultracentrifugation evidence used in manual assertion","statement":[{"text":"The hydrodynamic (Stokes) radii determined by AUC analyses (Table 1) suggest that the mCRY and mBMAL1 proteins have somewhat elongated shapes and might be at least partially unstructured.","type":"Results"}],"curator_orcid":"0000-0001-9045-7765","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006275","reference_id":"21521686","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T09:42:57.152Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":591,"term_name":"disorder","reference_html":"Quantitative analyses of cryptochrome-mBMAL1 interactions: mechanistic insights into the transcriptional regulation of the mammalian circadian clock. <i> Czarna A, Breitkreuz H, Mahrenholz CC, Arens J, Strauss HM, Wolf E. </i> J Biol Chem, 2011","start":564,"region_id":"DP03007r005","term_id":"IDPO:0000002","unpublished":true,"version":2,"curator_id":"jssuarez","released":"2022_03","term_ontology":"IDPO","curator_name":"Jaime Santos Suárez","ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"To quantify the contributions of the two mBMAL1 binding epitopes of mCRY1 and to find out which epitope is responsible for the different binding affinities of mCRY1 to mBMAL1-(577–625), mBMAL1-(490–625), and mBMAL1-(490–625)K537Q, we have synthesized peptides comprising mCRY1 residues Asn-472 to Ser-505 corresponding to the predicted coiled coil region (peptide P1) as well as residues Ser-564 to Glu-591 within the mCRY1 tail region (peptide P2). CD spectroscopy showed that peptide P1 has a high α-helical content (as predicted), whereas peptide P2 is mostly disordered (Table 2 and supplemental Fig. S3B). ","type":"Results"}],"curator_orcid":"0000-0001-9045-7765","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","reference_id":"21521686","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T09:36:06.164Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":595,"term_name":"molecular function regulator","reference_html":"Quantitative analyses of cryptochrome-mBMAL1 interactions: mechanistic insights into the transcriptional regulation of the mammalian circadian clock. <i> Czarna A, Breitkreuz H, Mahrenholz CC, Arens J, Strauss HM, Wolf E. </i> J Biol Chem, 2011","start":565,"region_id":"DP03007r012","term_id":"GO:0098772","unpublished":true,"version":3,"curator_id":"jssuarez","released":"2022_03","term_ontology":"GO","curator_name":"Jaime Santos Suárez","ec_name":"fluorescence evidence used in manual assertion","statement":[{"text":"To determine which mCRY residues are most critical for the mBMAL1 interaction, we have SPOT-synthesized peptides including the conserved mCRY coiled coil epitope (mCRY1 sequence 473HAEASRLNIERMKQIYQQLSRYRGLGLLASVP504) and the major part of the mCRY1 tail epitope (565QQTHSLKQGRSSAGTGLSSGKRPSQEEDAQS595). We have exchanged each amino acid in the mCRY peptides to alanine and measured the binding of the modified peptides to Cy3.5 fluorescently labeled mBMAL1-(577–625) (Fig. 4D). his experiment showed that single alanine mutations of the negatively charged residues Glu-590, Glu-591, or Asp-592 in the mCRY1 tail peptide raise its affinity to mBMAL1 drastically, whereas the exchange of any single lysine or arginine to alanine lowers it.","type":"Results"}],"curator_orcid":"0000-0001-9045-7765","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0001249","reference_id":"21521686","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T09:53:31.685Z"},"ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP03007r013","unpublished":true,"ec_ontology":"ECO","end":595,"term_id":"GO:0005515","start":565,"version":3,"statement":[{"text":"To determine which mCRY residues are most critical for the mBMAL1 interaction, we have SPOT-synthesized peptides including the conserved mCRY coiled coil epitope (mCRY1 sequence 473HAEASRLNIERMKQIYQQLSRYRGLGLLASVP504) and the major part of the mCRY1 tail epitope (565QQTHSLKQGRSSAGTGLSSGKRPSQEEDAQS595). We have exchanged each amino acid in the mCRY peptides to alanine and measured the binding of the modified peptides to Cy3.5 fluorescently labeled mBMAL1-(577–625) (Fig. 4D). his experiment showed that single alanine mutations of the negatively charged residues Glu-590, Glu-591, or Asp-592 in the mCRY1 tail peptide raise its affinity to mBMAL1 drastically, whereas the exchange of any single lysine or arginine to alanine lowers it.","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9WTL8","partner_end":null}],"term_name":"protein binding","ec_name":"fluorescence evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"GO","curator_name":"Jaime Santos Suárez","reference_id":"21521686","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0001249","curator_id":"jssuarez","reference_html":"Quantitative analyses of cryptochrome-mBMAL1 interactions: mechanistic insights into the transcriptional regulation of the mammalian circadian clock. <i> Czarna A, Breitkreuz H, Mahrenholz CC, Arens J, Strauss HM, Wolf E. </i> J Biol Chem, 2011","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T09:44:56.839Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP03007r014","unpublished":true,"ec_ontology":"ECO","end":591,"term_id":"GO:0005515","start":564,"version":3,"statement":[{"text":"Peptide P2, however, binds to mBMAL1-(577–625) and to the mBMAL1-(490–625)K537Q mutant fragment with an affinity of ∼3 μm but to the wild-type mBMAL1-(490–625) fragment with a lower affinity of ∼8 μm (Table 3 and Fig. 5, B–D). In contrast to all other mCRY-mBMAL1 interactions that we have analyzed by ITC, the interaction of peptide P2 with mBMAL1-(490–625)K537Q is exothermic and enthalpically as well as entropically favored (Fig. 5D, Table 3). This indicates that the P2-mBMAL1-(490–625)K537Q complex involves a larger number of polar contacts (e.g. hydrogen bonds) than the other mCRY-BMAL1 interactions, which are entropically but not enthalpically favored (30).","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9WTL8","partner_end":null}],"term_name":"protein binding","ec_name":"isothermal titration calorimetry evidence used in manual assertion","curator_orcid":"0000-0001-9045-7765","released":"2022_03","term_ontology":"GO","curator_name":"Jaime Santos Suárez","reference_id":"21521686","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0005647","curator_id":"jssuarez","reference_html":"Quantitative analyses of cryptochrome-mBMAL1 interactions: mechanistic insights into the transcriptional regulation of the mammalian circadian clock. <i> Czarna A, Breitkreuz H, Mahrenholz CC, Arens J, Strauss HM, Wolf E. </i> J Biol Chem, 2011","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T09:43:57.197Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":591,"term_name":"molecular function regulator","reference_html":"Quantitative analyses of cryptochrome-mBMAL1 interactions: mechanistic insights into the transcriptional regulation of the mammalian circadian clock. <i> Czarna A, Breitkreuz H, Mahrenholz CC, Arens J, Strauss HM, Wolf E. </i> J Biol Chem, 2011","start":564,"region_id":"DP03007r015","term_id":"GO:0098772","unpublished":true,"version":4,"curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","ec_name":"isothermal titration calorimetry evidence used in manual assertion","statement":[{"text":"Peptide P2, however, binds to mBMAL1-(577–625) and to the mBMAL1-(490–625)K537Q mutant fragment with an affinity of ∼3 μm but to the wild-type mBMAL1-(490–625) fragment with a lower affinity of ∼8 μm (Table 3 and Fig. 5, B–D). In contrast to all other mCRY-mBMAL1 interactions that we have analyzed by ITC, the interaction of peptide P2 with mBMAL1-(490–625)K537Q is exothermic and enthalpically as well as entropically favored (Fig. 5D, Table 3). This indicates that the P2-mBMAL1-(490–625)K537Q complex involves a larger number of polar contacts (e.g. hydrogen bonds) than the other mCRY-BMAL1 interactions, which are entropically but not enthalpically favored (30).","type":"Results"}],"curator_orcid":"0000-0002-5152-5953","date":"2022-03-08T14:07:24.699Z","reference_source":"pmid","ec_id":"ECO:0005647","reference_id":"21521686","ec_go":"IPI","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q9WTL8","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-26T15:15:45.164Z"}},{"start":494,"end":497,"reference_id":"29937374","reference_source":"pmid","reference_html":"Autophagy Regulates the Liver Clock and Glucose Metabolism by Degrading CRY1. <i> Toledo M, Batista-Gonzalez A, Merheb E, Aoun ML, Tarabra E, Feng D, Sarparanta J, Merlo P, Botrè F, Schwartz GJ, Pessin JE, Singh R. </i> Cell Metab, 2018","date":"2022-06-20T20:17:25.709Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","region_id":"DP03007r020","statement":[{"text":"We then determined the role of each LIR motif in degradation of CRY1 by expressing FLAG-tagged WT-CRY1 plasmid and each CRY1 mutant LIR plasmid (mLIR1, mLIR2, mLIR3, and mLIR4 as in Figure 5B) in liver via tail vein injections using the jet-PEI in vivo transfection system (Chang et al., 2014) (Figure S5A).","type":"Results"},{"text":"Strikingly, mLIR1-CRY1 and mLIR4-CRY1 accumulated significantly more than mLIR2-CRY1 and mLIR3-CRY1 or WT-CRY1. Levels of mLIR2 and mLIR3 CRY1 were moderately higher than WT-CRY1, but differences between these groups remained statistically insignificant (Figure 5C). These results indicate that LIR1 (271DLYKKV276) and LIR4 (492SRYRGL497) are required for degradation of CRY1\nby autophagy. Accumulation of mLIR1-CRY1 and mLIR4-CRY1 did not occur from reduced autophagy per se, indicated by equivalent LC3-II flux in livers injected with WT or mLIR-CRY1 plasmids (Figure 5D), or from changes in transfection\ndetermined by qPCR showing equivalent Cry1 expression in\nlivers injected with WT and mLIR-CRY1 plasmids (Figure S5E).","type":"Results"},{"text":"CoIP in 293T cells confirmed that interactions of mLIR1-CRY1\nand mLIR4-CRY1 with GFP-tagged LC3 were remarkably\nreduced compared with WT-CRY1, mLIR2-CRY1, or mLIR3-\nCRY1 (Figure S5F). These results are consistent with significant\naccumulation of mLIR1-CRY1 and mLIR4-CRY1 and moderate\naccumulation of mLIR2 and mLIR3 CRY1 in liver compared\nwith WT-CRY1 (Figure 5C). Consistent with our observation that accumulation of CRY1 in Atg7KO mice associates with\ndecreased BMAL1 levels (Figure 2J), accumulation of mLIR1-\nCRY1 or mLIR4-CRY1 each associated with reduced BMAL1\nlevels (Figure 5E), indicating that expressing autophagy-resistant\nforms of CRY1 is sufficient to disrupt the liver clock.","type":"Results"},{"text":"In the article, the functional LIR motif YRGL in positions 494-497 corresponds to LIR4.","type":"Curator statement"},{"text":"The non-functional LIR motif YQQL in positions 488-491, and the functional LIR motif YRGL in positions 494-497, are both incorporated inside the disordered region fragment in positions 471-606.","type":"Curator statement"},{"text":"mLIR4-CRY1 (492SRARGA497)","type":"Table"},{"text":"Figure 5. LIR Motifs Determine CRY1 Degradation and Regulation of Gluconeogenesis\n(A) Murine CRY1 has 13 LIR motifs (green).\n(B) Inactivation of selected LIR motifs (mLIR1-4) on CRY1 via mutagenesis of tyrosine (Y), valine (V), or leucine (L) residues (green) to alanine (A) (red).\n(C) IB for FLAG in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 plasmid or each FLAG-tagged CRY1 LIR mutant plasmid (mLIR1–4); n = 12.\n(D) IB for LC3 in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 or each CRY1 LIR mutant (mLIR1–4) and cultured in presence or absence of\nLys Inh for 2 hr; n = 7–10.\n(E and F) IB for BMAL1 and G6P in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 plasmid or each CRY1 LIR mutant plasmid (mLIR1–4);\nn = 8–12.","type":"Figure"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T13:10:20.112Z"}},{"start":494,"end":497,"reference_id":"29937374","reference_source":"pmid","reference_html":"Autophagy Regulates the Liver Clock and Glucose Metabolism by Degrading CRY1. <i> Toledo M, Batista-Gonzalez A, Merheb E, Aoun ML, Tarabra E, Feng D, Sarparanta J, Merlo P, Botrè F, Schwartz GJ, Pessin JE, Singh R. </i> Cell Metab, 2018","date":"2022-06-28T10:52:00.029Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_06","version":2,"ec_go":"IPI","region_id":"DP03007r021","statement":[{"text":"We then determined the role of each LIR motif in degradation of CRY1 by expressing FLAG-tagged WT-CRY1 plasmid and each CRY1 mutant LIR plasmid (mLIR1, mLIR2, mLIR3, and mLIR4 as in Figure 5B) in liver via tail vein injections using the jet-PEI in vivo transfection system (Chang et al., 2014) (Figure S5A).","type":"Results"},{"text":"Strikingly, mLIR1-CRY1 and mLIR4-CRY1 accumulated significantly more than mLIR2-CRY1 and mLIR3-CRY1 or WT-CRY1. Levels of mLIR2 and mLIR3 CRY1 were moderately higher than WT-CRY1, but differences between these groups remained statistically insignificant (Figure 5C). These results indicate that LIR1 (271DLYKKV276) and LIR4 (492SRYRGL497) are required for degradation of CRY1\nby autophagy. Accumulation of mLIR1-CRY1 and mLIR4-CRY1 did not occur from reduced autophagy per se, indicated by equivalent LC3-II flux in livers injected with WT or mLIR-CRY1 plasmids (Figure 5D), or from changes in transfection\ndetermined by qPCR showing equivalent Cry1 expression in\nlivers injected with WT and mLIR-CRY1 plasmids (Figure S5E).","type":"Results"},{"text":"CoIP in 293T cells confirmed that interactions of mLIR1-CRY1\nand mLIR4-CRY1 with GFP-tagged LC3 were remarkably\nreduced compared with WT-CRY1, mLIR2-CRY1, or mLIR3-\nCRY1 (Figure S5F). These results are consistent with significant\naccumulation of mLIR1-CRY1 and mLIR4-CRY1 and moderate\naccumulation of mLIR2 and mLIR3 CRY1 in liver compared\nwith WT-CRY1 (Figure 5C). Consistent with our observation that accumulation of CRY1 in Atg7KO mice associates with\ndecreased BMAL1 levels (Figure 2J), accumulation of mLIR1-\nCRY1 or mLIR4-CRY1 each associated with reduced BMAL1\nlevels (Figure 5E), indicating that expressing autophagy-resistant\nforms of CRY1 is sufficient to disrupt the liver clock.","type":"Results"},{"text":"In the article, the functional LIR motif YRGL in positions 494-497 corresponds to LIR4.","type":"Curator statement"},{"text":"The non-functional LIR motif YQQL in positions 488-491, and the functional LIR motif YRGL in positions 494-497, are both incorporated inside the disordered region fragment in positions 471-606.","type":"Curator statement"},{"text":"mLIR4-CRY1 (492SRARGA497)","type":"Table"},{"text":"Figure 5. LIR Motifs Determine CRY1 Degradation and Regulation of Gluconeogenesis\n(A) Murine CRY1 has 13 LIR motifs (green).\n(B) Inactivation of selected LIR motifs (mLIR1-4) on CRY1 via mutagenesis of tyrosine (Y), valine (V), or leucine (L) residues (green) to alanine (A) (red).\n(C) IB for FLAG in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 plasmid or each FLAG-tagged CRY1 LIR mutant plasmid (mLIR1–4); n = 12.\n(D) IB for LC3 in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 or each CRY1 LIR mutant (mLIR1–4) and cultured in presence or absence of\nLys Inh for 2 hr; n = 7–10.\n(E and F) IB for BMAL1 and G6P in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 plasmid or each CRY1 LIR mutant plasmid (mLIR1–4);\nn = 8–12.","type":"Figure"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"Q9CQV6","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T13:10:22.678Z"}},{"start":494,"end":497,"reference_id":"29937374","reference_source":"pmid","reference_html":"Autophagy Regulates the Liver Clock and Glucose Metabolism by Degrading CRY1. <i> Toledo M, Batista-Gonzalez A, Merheb E, Aoun ML, Tarabra E, Feng D, Sarparanta J, Merlo P, Botrè F, Schwartz GJ, Pessin JE, Singh R. </i> Cell Metab, 2018","date":"2022-06-21T15:28:34.586Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_06","version":1,"ec_go":"IPI","region_id":"DP03007r022","statement":[{"text":"We then determined the role of each LIR motif in degradation of CRY1 by expressing FLAG-tagged WT-CRY1 plasmid and each CRY1 mutant LIR plasmid (mLIR1, mLIR2, mLIR3, and mLIR4 as in Figure 5B) in liver via tail vein injections using the jet-PEI in vivo transfection system (Chang et al., 2014) (Figure S5A).","type":"Results"},{"text":"Strikingly, mLIR1-CRY1 and mLIR4-CRY1 accumulated significantly more than mLIR2-CRY1 and mLIR3-CRY1 or WT-CRY1. Levels of mLIR2 and mLIR3 CRY1 were moderately higher than WT-CRY1, but differences between these groups remained statistically insignificant (Figure 5C). These results indicate that LIR1 (271DLYKKV276) and LIR4 (492SRYRGL497) are required for degradation of CRY1\nby autophagy. Accumulation of mLIR1-CRY1 and mLIR4-CRY1 did not occur from reduced autophagy per se, indicated by equivalent LC3-II flux in livers injected with WT or mLIR-CRY1 plasmids (Figure 5D), or from changes in transfection\ndetermined by qPCR showing equivalent Cry1 expression in\nlivers injected with WT and mLIR-CRY1 plasmids (Figure S5E).","type":"Results"},{"text":"CoIP in 293T cells confirmed that interactions of mLIR1-CRY1\nand mLIR4-CRY1 with GFP-tagged LC3 were remarkably\nreduced compared with WT-CRY1, mLIR2-CRY1, or mLIR3-\nCRY1 (Figure S5F). These results are consistent with significant\naccumulation of mLIR1-CRY1 and mLIR4-CRY1 and moderate\naccumulation of mLIR2 and mLIR3 CRY1 in liver compared\nwith WT-CRY1 (Figure 5C). Consistent with our observation that accumulation of CRY1 in Atg7KO mice associates with\ndecreased BMAL1 levels (Figure 2J), accumulation of mLIR1-\nCRY1 or mLIR4-CRY1 each associated with reduced BMAL1\nlevels (Figure 5E), indicating that expressing autophagy-resistant\nforms of CRY1 is sufficient to disrupt the liver clock.","type":"Results"},{"text":"In the article, the functional LIR motif YRGL in positions 494-497 corresponds to LIR4.","type":"Curator statement"},{"text":"The non-functional LIR motif YQQL in positions 488-491, and the functional LIR motif YRGL in positions 494-497, are both incorporated inside the disordered region fragment in positions 471-606.","type":"Curator statement"},{"text":"mLIR4-CRY1 (492SRARGA497)","type":"Table"},{"text":"Figure 5. LIR Motifs Determine CRY1 Degradation and Regulation of Gluconeogenesis\n(A) Murine CRY1 has 13 LIR motifs (green).\n(B) Inactivation of selected LIR motifs (mLIR1-4) on CRY1 via mutagenesis of tyrosine (Y), valine (V), or leucine (L) residues (green) to alanine (A) (red).\n(C) IB for FLAG in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 plasmid or each FLAG-tagged CRY1 LIR mutant plasmid (mLIR1–4); n = 12.\n(D) IB for LC3 in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 or each CRY1 LIR mutant (mLIR1–4) and cultured in presence or absence of\nLys Inh for 2 hr; n = 7–10.\n(E and F) IB for BMAL1 and G6P in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 plasmid or each CRY1 LIR mutant plasmid (mLIR1–4);\nn = 8–12.","type":"Figure"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"Q9CQV6","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T13:10:28.228Z"}},{"start":494,"end":497,"reference_id":"29937374","reference_source":"pmid","reference_html":"Autophagy Regulates the Liver Clock and Glucose Metabolism by Degrading CRY1. <i> Toledo M, Batista-Gonzalez A, Merheb E, Aoun ML, Tarabra E, Feng D, Sarparanta J, Merlo P, Botrè F, Schwartz GJ, Pessin JE, Singh R. </i> Cell Metab, 2018","date":"2022-06-20T21:14:21.871Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","region_id":"DP03007r023","statement":[{"text":"We then determined the role of each LIR motif in degradation of CRY1 by expressing FLAG-tagged WT-CRY1 plasmid and each CRY1 mutant LIR plasmid (mLIR1, mLIR2, mLIR3, and mLIR4 as in Figure 5B) in liver via tail vein injections using the jet-PEI in vivo transfection system (Chang et al., 2014) (Figure S5A).","type":"Results"},{"text":"Strikingly, mLIR1-CRY1 and mLIR4-CRY1 accumulated significantly more than mLIR2-CRY1 and mLIR3-CRY1 or WT-CRY1. Levels of mLIR2 and mLIR3 CRY1 were moderately higher than WT-CRY1, but differences between these groups remained statistically insignificant (Figure 5C). These results indicate that LIR1 (271DLYKKV276) and LIR4 (492SRYRGL497) are required for degradation of CRY1\nby autophagy. Accumulation of mLIR1-CRY1 and mLIR4-CRY1 did not occur from reduced autophagy per se, indicated by equivalent LC3-II flux in livers injected with WT or mLIR-CRY1 plasmids (Figure 5D), or from changes in transfection\ndetermined by qPCR showing equivalent Cry1 expression in\nlivers injected with WT and mLIR-CRY1 plasmids (Figure S5E).","type":"Results"},{"text":"CoIP in 293T cells confirmed that interactions of mLIR1-CRY1\nand mLIR4-CRY1 with GFP-tagged LC3 were remarkably\nreduced compared with WT-CRY1, mLIR2-CRY1, or mLIR3-\nCRY1 (Figure S5F). These results are consistent with significant\naccumulation of mLIR1-CRY1 and mLIR4-CRY1 and moderate\naccumulation of mLIR2 and mLIR3 CRY1 in liver compared\nwith WT-CRY1 (Figure 5C). Consistent with our observation that accumulation of CRY1 in Atg7KO mice associates with\ndecreased BMAL1 levels (Figure 2J), accumulation of mLIR1-\nCRY1 or mLIR4-CRY1 each associated with reduced BMAL1\nlevels (Figure 5E), indicating that expressing autophagy-resistant\nforms of CRY1 is sufficient to disrupt the liver clock.","type":"Results"},{"text":"In the article, the functional LIR motif YRGL in positions 494-497 corresponds to LIR4.","type":"Curator statement"},{"text":"The non-functional LIR motif YQQL in positions 488-491, and the functional LIR motif YRGL in positions 494-497, are both incorporated inside the disordered region fragment in positions 471-606.","type":"Curator statement"},{"text":"mLIR4-CRY1 (492SRARGA497)","type":"Table"},{"text":"Figure 5. LIR Motifs Determine CRY1 Degradation and Regulation of Gluconeogenesis\n(A) Murine CRY1 has 13 LIR motifs (green).\n(B) Inactivation of selected LIR motifs (mLIR1-4) on CRY1 via mutagenesis of tyrosine (Y), valine (V), or leucine (L) residues (green) to alanine (A) (red).\n(C) IB for FLAG in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 plasmid or each FLAG-tagged CRY1 LIR mutant plasmid (mLIR1–4); n = 12.\n(D) IB for LC3 in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 or each CRY1 LIR mutant (mLIR1–4) and cultured in presence or absence of\nLys Inh for 2 hr; n = 7–10.\n(E and F) IB for BMAL1 and G6P in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 plasmid or each CRY1 LIR mutant plasmid (mLIR1–4);\nn = 8–12.","type":"Figure"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T13:11:46.884Z"}},{"start":494,"end":497,"reference_id":"29937374","reference_source":"pmid","reference_html":"Autophagy Regulates the Liver Clock and Glucose Metabolism by Degrading CRY1. <i> Toledo M, Batista-Gonzalez A, Merheb E, Aoun ML, Tarabra E, Feng D, Sarparanta J, Merlo P, Botrè F, Schwartz GJ, Pessin JE, Singh R. </i> Cell Metab, 2018","date":"2022-06-20T20:25:55.144Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0006111","term_name":"regulation of gluconeogenesis","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","region_id":"DP03007r024","statement":[{"text":"LIR Motifs Link CRY1 Degradation to Regulation of Gluconeogenesis\nSince increases in hepatocellular CRY1 protein inhibit gluconeo￾genesis, we next tested whether accumulation of mLIR1-CRY1 or mLIR4-CRY1 was sufficient to suppress hepatic glucose production/blood glucose levels. Indeed, mice injected with mLIR1-CRY1 or mLIR4-CRY1, but not mLIR2-CRY1 and mLIR3-CRY1 constructs, displayed reduced G6P protein levels (Figure 5F) and decreased blood glucose levels at 7 p.m. (Figures 5G–5J). Furthermore, mLIR1-CRY1- or mLIR4-CRY1-injected mice, and not the mLIR2-CRY1- and mLIR3-CRY1-injected mice, exhibited less glucose production when subjected to PTTs (Figure 5K), indicating that LIR motifs 271DLYKKV276 and 492SRYRGL497 link CRY1 turnover by autophagy to regulation\nof gluconeogenesis. Most surprisingly, CRY1 LIR2 (285SLYGQL290) and LIR4 (492SRYRGL497) are also required for degradation of SCF components Skp1 and FBXL3 by autophagy, since livers injected with mLIR2-CRY1, mLIR3-CRY1, and\nmLIR4-CRY1 each showed accumulation of these proteins compared with WT-CRY1 or mLIR1-CRY1 (Figure S5G). These data suggest that SCF components Skp1 and Fbxl3 are likely tar￾geted for autophagic degradation via their association with CRY1 (Xing et al., 2013), which, in turn, binds to LC3 via its LIR motifs.","type":"Results"},{"text":"In the article, the functional LIR motif YRGL in positions 494-497 corresponds to LIR4.","type":"Curator statement"},{"text":"The non-functional LIR motif YQQL in positions 488-491, and the functional LIR motif YRGL in positions 494-497, are both incorporated inside the disordered region fragment in positions 471-606.","type":"Curator statement"},{"text":"mLIR4-CRY1 (492SRARGA497)","type":"Table"},{"text":"Figure 5. LIR Motifs Determine CRY1 Degradation and Regulation of Gluconeogenesis (A) Murine CRY1 has 13 LIR motifs (green). (B) Inactivation of selected LIR motifs (mLIR1-4) on CRY1 via mutagenesis of tyrosine (Y), valine (V), or leucine (L) residues (green) to alanine (A) (red). (C) IB for FLAG in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 plasmid or each FLAG-tagged CRY1 LIR mutant plasmid (mLIR1–4); n = 12. (D) IB for LC3 in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 or each CRY1 LIR mutant (mLIR1–4) and cultured in presence or absence of Lys Inh for 2 hr; n = 7–10. (E and F) IB for BMAL1 and G6P in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 plasmid or each CRY1 LIR mutant plasmid (mLIR1–4); n = 8–12.","type":"Figure"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of gluconeogenesis, the formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T13:11:51.244Z"}},{"start":494,"end":497,"reference_id":"29937374","reference_source":"pmid","reference_html":"Autophagy Regulates the Liver Clock and Glucose Metabolism by Degrading CRY1. <i> Toledo M, Batista-Gonzalez A, Merheb E, Aoun ML, Tarabra E, Feng D, Sarparanta J, Merlo P, Botrè F, Schwartz GJ, Pessin JE, Singh R. </i> Cell Metab, 2018","date":"2022-06-20T20:26:48.333Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0006111","term_name":"regulation of gluconeogenesis","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IEP","region_id":"DP03007r025","statement":[{"text":"LIR Motifs Link CRY1 Degradation to Regulation of Gluconeogenesis\nSince increases in hepatocellular CRY1 protein inhibit gluconeo￾genesis, we next tested whether accumulation of mLIR1-CRY1 or mLIR4-CRY1 was sufficient to suppress hepatic glucose production/blood glucose levels. Indeed, mice injected with mLIR1-CRY1 or mLIR4-CRY1, but not mLIR2-CRY1 and mLIR3-CRY1 constructs, displayed reduced G6P protein levels (Figure 5F) and decreased blood glucose levels at 7 p.m. (Figures 5G–5J). Furthermore, mLIR1-CRY1- or mLIR4-CRY1-injected mice, and not the mLIR2-CRY1- and mLIR3-CRY1-injected mice, exhibited less glucose production when subjected to PTTs (Figure 5K), indicating that LIR motifs 271DLYKKV276 and 492SRYRGL497 link CRY1 turnover by autophagy to regulation\nof gluconeogenesis. Most surprisingly, CRY1 LIR2 (285SLYGQL290) and LIR4 (492SRYRGL497) are also required for degradation of SCF components Skp1 and FBXL3 by autophagy, since livers injected with mLIR2-CRY1, mLIR3-CRY1, and\nmLIR4-CRY1 each showed accumulation of these proteins compared with WT-CRY1 or mLIR1-CRY1 (Figure S5G). These data suggest that SCF components Skp1 and Fbxl3 are likely tar￾geted for autophagic degradation via their association with CRY1 (Xing et al., 2013), which, in turn, binds to LC3 via its LIR motifs.","type":"Results"},{"text":"In the article, the functional LIR motif YRGL in positions 494-497 corresponds to LIR4.","type":"Curator statement"},{"text":"The non-functional LIR motif YQQL in positions 488-491, and the functional LIR motif YRGL in positions 494-497, are both incorporated inside the disordered region fragment in positions 471-606.","type":"Curator statement"},{"text":"mLIR4-CRY1 (492SRARGA497)","type":"Table"},{"text":"Figure 5. LIR Motifs Determine CRY1 Degradation and Regulation of Gluconeogenesis (A) Murine CRY1 has 13 LIR motifs (green). (B) Inactivation of selected LIR motifs (mLIR1-4) on CRY1 via mutagenesis of tyrosine (Y), valine (V), or leucine (L) residues (green) to alanine (A) (red). (C) IB for FLAG in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 plasmid or each FLAG-tagged CRY1 LIR mutant plasmid (mLIR1–4); n = 12. (D) IB for LC3 in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 or each CRY1 LIR mutant (mLIR1–4) and cultured in presence or absence of Lys Inh for 2 hr; n = 7–10. (E and F) IB for BMAL1 and G6P in livers from male mice at 7 p.m. expressing FLAG-tagged WT-CRY1 plasmid or each CRY1 LIR mutant plasmid (mLIR1–4); n = 8–12.","type":"Figure"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of gluconeogenesis, the formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T13:11:55.430Z"}},{"start":494,"end":497,"reference_id":"29937374","reference_source":"pmid","reference_html":"Autophagy Regulates the Liver Clock and Glucose Metabolism by Degrading CRY1. <i> Toledo M, Batista-Gonzalez A, Merheb E, Aoun ML, Tarabra E, Feng D, Sarparanta J, Merlo P, Botrè F, Schwartz GJ, Pessin JE, Singh R. </i> Cell Metab, 2018","date":"2022-06-21T18:17:53.619Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0045722","term_name":"positive regulation of gluconeogenesis","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001218","ec_ontology":"ECO","ec_name":"in vivo protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IDA","region_id":"DP03007r028","statement":[{"text":"LIR motifs link CRY1 degradation to regulation of glucose homeostasis","type":"Article"},{"text":"LIR motifs on CRY1 determine their degradation and regulation of gluconeogenesis","type":"Figure"},{"text":"Since increases in hepatocellular CRY1 protein inhibit gluconeogenesis, we next tested whether accumulation of mLIR1-CRY1 or mLIR4-CRY1 was sufficient to suppress hepatic glucose production/blood glucose levels. Indeed, mice injected with mLIR1-CRY1 or mLIR4-CRY1, but not mLIR2-CRY1 and mLIR3-CRY1 constructs, displayed reduced G6P protein levels (Fig. 5F) and decreased blood glucose levels at 7pm (Fig. 5G–5J). Furthermore, mLIR1-CRY1 or mLIR4-CRY1-injected mice, and not the mLIR2-CRY1 and mLIR3-CRY1-injected mice, exhibited less glucose production when subjected to PTTs (Fig. 5K) – indicating that LIR motifs 271DLYKKV276 and 492SRYRGL497 link CRY1 turnover by autophagy to regulation of gluconeogenesis.","type":"Results"},{"text":"The non-functional LIR motif YQQL in positions 488-491, and the functional LIR motif YRGL in positions 494-497, are both incorporated inside the disordered region fragment in positions 471-606.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of gluconeogenesis.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T13:12:02.468Z"}}],"released":"2021_12","length":606,"ncbi_taxon_id":10090,"organism":"Mus musculus","disprot_id":"DP03007","date":"2020-12-03T17:48:48.386Z","regions_counter":28,"dataset":["Autophagy-related proteins"],"UniParc":"UPI000002950C","uniref100":"UniRef100_P97784","uniref90":"UniRef90_P97784","uniref50":"UniRef50_P97784","genes":[{"name":{"value":"Cry1"}}],"alphafold_very_low_content":0.1848184818481848,"disorder_content":0.24257425742574257,"disprot_consensus":{"full":[{"start":167,"end":177,"type":"D"},{"start":471,"end":606,"type":"D"}],"Structural state":[{"start":167,"end":177,"type":"D"},{"start":471,"end":606,"type":"D"}],"Molecular function":[{"start":494,"end":497,"type":"F"},{"start":564,"end":595,"type":"F"}],"Biological process":[{"start":494,"end":497,"type":"F"}]}},{"acc":"P53104","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":24,"end":322},{"id":"PF12063","name":"Atg1-like, MIT domain 1","start":592,"end":763},{"id":"PF21127","name":"ATG1-like, MIT domain 2","start":784,"end":893}],"gene3D":[]},"creator":"tlazar","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"sequence":"MGDIKNKDHTTSVNHNLMASAGNYTAEKEIGKGSFATVYRGHLTSDKSQHVAIKEVSRAKLKNKKLLENLEIEIAILKKIKHPHIVGLIDCERTSTDFYLIMEYCALGDLTFLLKRRKELMENHPLLRTVFEKYPPPSENHNGLHRAFVLSYLQQLASALKFLRSKNLVHRDIKPQNLLLSTPLIGYHDSKSFHELGFVGIYNLPILKIADFGFARFLPNTSLAETLCGSPLYMAPEILNYQKYNAKADLWSVGTVVFEMCCGTPPFRASNHLELFKKIKRANDVITFPSYCNIEPELKELICSLLTFDPAQRIGFEEFFANKVVNEDLSSYELEDDLPELESKSKGIVESNMFVSEYLSKQPKSPNSNLAGHQSMADNPAELSDALKNSNILTAPAVKTDHTQAVDKKASNNKYHNSLVSDRSFEREYVVVEKKSVEVNSLADEVAQAGFNPNPIKHPTSTQNQNVLLNEQFSPNNQQYFQNQGENPRLLRATSSSSGGSDGSRRPSLVDRRLSISSLNPSNALSRALGIASTRLFGGANQQQQQQQITSSPPYSQTLLNSQLFHELTENIILRIDHLQHPETLKLDNTNIVSILESLAAKAFVVYSYAEVKFSQIVPLSTTLKGMANFENRRSMDSNAIAEEQDSDDAEEEDETLKKYKEDCLSTKTFGKGRTLSATSQLSATFNKLPRSEMILLCNEAIVLYMKALSILSKSMQVTSNWWYESQEKSCSLRVNVLVQWLREKFNECLEKADFLRLKINDLRFKHASEVAENQTLEEKGSSEEPVYLEKLLYDRALEISKMAAHMELKGENLYNCELAYATSLWMLETSLDDDDFTNAYGDYPFKTNIHLKSNDVEDKEKYHSVLDENDRIIIRKYIDSIANRLKILRQKMNHQN","name":"Serine/threonine-protein kinase ATG1","regions":[{"region_id":"DP03008r001","unpublished":true,"validated":{"curator_id":"fquaglia","timestamp":"2020-12-04T11:45:47.943Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":586,"term_id":"IDPO:0000002","start":332,"version":2,"statement":[{"text":"The IDR of Atg1 (D211A) showed a double-Gaussian distribution of R_2D, suggesting interactions between the IDR and the dead kinase domain, in agreement with phosphorylation of the IDR by the N-terminal kinase domain of the WT protein","type":"Results"}],"term_name":"disorder","ec_name":"atomic force microscopy evidence used in manual assertion","curator_orcid":"0000-0001-7496-6711","released":"2023_12","term_ontology":"IDPO","curator_name":"Tamas Lazar","reference_id":"33230318","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0001591","curator_id":"tlazar","reference_html":"Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy. <i> Kodera N, Noshiro D, Dora SK, Mori T, Habchi J, Blocquel D, Gruet A, Dosnon M, Salladini E, Bignon C, Fujioka Y, Oda T, Noda NN, Sato M, Lotti M, Mizuguchi M, Longhi S, Ando T. </i> Nat Nanotechnol, 2021","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2023_12","length":897,"ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","disprot_id":"DP03008","date":"2020-12-04T10:14:13.712Z","regions_counter":1,"dataset":["Condensates-related proteins"],"UniParc":"UPI0000125C5E","uniref100":"UniRef100_A6ZU07","uniref90":"UniRef90_A6ZU07","uniref50":"UniRef50_Q75CH3","genes":[{"name":{"value":"ATG1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"14536056","url":"http://www.ncbi.nlm.nih.gov/pubmed/14536056","alternativeUrl":"https://europepmc.org/abstract/MED/14536056"}}]},"synonyms":[{"value":"APG1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9169869","url":"http://www.ncbi.nlm.nih.gov/pubmed/9169869","alternativeUrl":"https://europepmc.org/abstract/MED/9169869"}}]},{"value":"AUT3","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9190802","url":"http://www.ncbi.nlm.nih.gov/pubmed/9190802","alternativeUrl":"https://europepmc.org/abstract/MED/9190802"}}]},{"value":"CVT10","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8663607","url":"http://www.ncbi.nlm.nih.gov/pubmed/8663607","alternativeUrl":"https://europepmc.org/abstract/MED/8663607"}}]}],"orfNames":[{"value":"G1615"}],"olnNames":[{"value":"YGL180W","evidences":[{"code":"ECO:0000312","source":{"name":"SGD","id":"S000003148","url":"https://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000003148"}}]}]}],"alphafold_very_low_content":0.3857302118171683,"disorder_content":0.2842809364548495,"disprot_consensus":{"full":[{"start":332,"end":586,"type":"D"}],"Structural state":[{"start":332,"end":586,"type":"D"}]}},{"acc":"Q5D1E8","features":{"pfam":[{"id":"PF11977","name":"Zc3h12a-like Ribonuclease NYN domain","start":135,"end":289},{"id":"PF18039","name":"UBA-like domain","start":49,"end":89},{"id":"PF18561","name":"Endoribonuclease Regnase 1/ ZC3H12 C-terminal domain","start":550,"end":593}],"gene3D":[]},"creator":"zskalman","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MSGPCGEKPVLEASPTMSLWEFEDSHSRQGTPRPGQELAAEEASALELQMKVDFFRKLGYSSTEIHSVLQKLGVQADTNTVLGELVKHGTATERERQTSPDPCPQLPLVPRGGGTPKAPNLEPPLPEEEKEGSDLRPVVIDGSNVAMSHGNKEVFSCRGILLAVNWFLERGHTDITVFVPSWRKEQPRPDVPITDQHILRELEKKKILVFTPSRRVGGKRVVCYDDRFIVKLAYESDGIVVSNDTYRDLQGERQEWKRFIEERLLMYSFVNDKFMPPDDPLGRHGPSLDNFLRKKPLTLEHRKQPCPYGRKCTYGIKCRFFHPERPSCPQRSVADELRANALLSPPRAPSKDKNGRRPSPSSQSSSLLTESEQCSLDGKKLGAQASPGSRQEGLTQTYAPSGRSLAPSGGSGSSFGPTDWLPQTLDSLPYVSQDCLDSGIGSLESQMSELWGVRGGGPGEPGPPRAPYTGYSPYGSELPATAAFSAFGRAMGAGHFSVPADYPPAPPAFPPREYWSEPYPLPPPTSVLQEPPVQSPGAGRSPWGRAGSLAKEQASVYTKLCGVFPPHLVEAVMGRFPQLLDPQQLAAEILSYKSQHPSE","name":"Endoribonuclease ZC3H12A","regions":[{"start":297,"end":334,"reference_id":"22561375","reference_source":"pmid","reference_html":"Structural study of MCPIP1 N-terminal conserved domain reveals a PIN-like RNase. <i> Xu J, Peng W, Sun Y, Wang X, Xu Y, Li X, Gao G, Rao Z. </i> Nucleic Acids Res, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3V33"}],"region_id":"DP03010r002","statement":[{"text":"The CCCH zinc-finger motif (297–334) was totally disordered in our structure of NCD-ZF, although SDS–PAGE analysis confirmed that the CCCH zinc finger was not degraded in the crystal.","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-07T18:23:11.128Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":112,"end":133,"reference_id":"22561375","reference_source":"pmid","reference_html":"Structural study of MCPIP1 N-terminal conserved domain reveals a PIN-like RNase. <i> Xu J, Peng W, Sun Y, Wang X, Xu Y, Li X, Gao G, Rao Z. </i> Nucleic Acids Res, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3V33"},{"db":"PDB","id":"3V34"},{"db":"PDB","id":"3V32"}],"region_id":"DP03010r003","statement":[{"text":"The N-terminal 22 residues (i.e. 112–133) and residues 216–222 are missing in the final model due to the absence of interpretable electron density.","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-07T18:23:24.423Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_12","length":599,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP03010","date":"2020-12-04T13:36:50.790Z","regions_counter":3,"dataset":["RNA-binding proteins","Stress response proteins"],"UniParc":"UPI000004D30E","uniref100":"UniRef100_Q5D1E8","uniref90":"UniRef90_Q5D1E8","uniref50":"UniRef50_Q5D1E8","genes":[{"name":{"value":"ZC3H12A","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:26259","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:26259"}}]},"synonyms":[{"value":"MCPIP","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16574901","url":"http://www.ncbi.nlm.nih.gov/pubmed/16574901","alternativeUrl":"https://europepmc.org/abstract/MED/16574901"}}]},{"value":"MCPIP1"}]}],"alphafold_very_low_content":0.44073455759599334,"disorder_content":0.1001669449081803,"disprot_consensus":{"full":[{"start":112,"end":133,"type":"D"},{"start":297,"end":334,"type":"D"}],"Structural state":[{"start":112,"end":133,"type":"D"},{"start":297,"end":334,"type":"D"}]}},{"acc":"P51787","features":{"pfam":[{"id":"PF00520","name":"Ion transport protein","start":124,"end":358},{"id":"PF03520","name":"KCNQ voltage-gated potassium channel","start":505,"end":617}],"gene3D":[]},"creator":"ldobson","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MAAASSPPRAERKRWGWGRLPGARRGSAGLAKKCPFSLELAEGGPAGGALYAPIAPGAPGPAPPASPAAPAAPPVASDLGPRPPVSLDPRVSIYSTRRPVLARTHVQGRVYNFLERPTGWKCFVYHFAVFLIVLVCLIFSVLSTIEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGCRSKYVGLWGRLRFARKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRVEFGSYADALWWGVVTVTTIGYGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASLIQTAWRCYAAENPDSSTWKIYIRKAPRSHTLLSPSPKPKKSVVVKKKKFKLDKDNGVTPGEKMLTVPHITCDPPEERRLDHFSVDGYDSSVRKSPTLLEVSMPHFMRTNSFAEDLDLEGETLLTPITHISQLREHHRATIKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMVRIKELQRRLDQSIGKPSLFISVSEKSKDRGSNTIGARLNRVEDKVTQLDQRLALITDMLHQLLSLHGGSTPGSGGPPREGGAHITQPCGSGGSVDPELFLPSNTLPTYEQLTVPRRGPDEGS","name":"Potassium voltage-gated channel subfamily KQT member 1","regions":[{"start":574,"end":584,"reference_id":"18165683","reference_source":"pmid","reference_html":"The KCNQ1 (Kv7.1) COOH terminus, a multitiered scaffold for subunit assembly and protein interaction. <i> Wiener R, Haitin Y, Shamgar L, Fernández-Alonso MC, Martos A, Chomsky-Hecht O, Rivas G, Attali B, Hirsch JA. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3BJ4"}],"region_id":"DP03011r002","statement":[{"text":"\"Residues 574-584 are not observed and must be disordered\"","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-07T18:27:15.977Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":676,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP03011","date":"2020-12-05T09:36:29.276Z","regions_counter":2,"dataset":[],"UniParc":"UPI0000030D13","uniref100":"UniRef100_P51787","uniref90":"UniRef90_P51787","uniref50":"UniRef50_P51787","genes":[{"name":{"value":"KCNQ1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6294","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6294"}}]},"synonyms":[{"value":"KCNA8","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6294","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6294"}}]},{"value":"KCNA9","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6294","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6294"}}]},{"value":"KVLQT1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9312006","url":"http://www.ncbi.nlm.nih.gov/pubmed/9312006","alternativeUrl":"https://europepmc.org/abstract/MED/9312006"}}]}]}],"alphafold_very_low_content":0.3757396449704142,"disorder_content":0.016272189349112426,"disprot_consensus":{"full":[{"start":574,"end":584,"type":"D"}],"Structural state":[{"start":574,"end":584,"type":"D"}]}},{"acc":"P40818","features":{"pfam":[{"id":"PF00443","name":"Ubiquitin carboxyl-terminal hydrolase","start":777,"end":1106},{"id":"PF00581","name":"Rhodanese-like domain","start":184,"end":305},{"id":"PF08969","name":"USP8 dimerisation domain","start":8,"end":115},{"id":"PF20625","name":"USP8 WW domain","start":648,"end":680}],"gene3D":[]},"creator":"zskalman","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MPAVASVPKELYLSSSLKDLNKKTEVKPEKISTKSYVHSALKIFKTAEECRLDRDEERAYVLYMKYVTVYNLIKKRPDFKQQQDYFHSILGPGNIKKAVEEAERLSESLKLRYEEAEVRKKLEEKDRQEEAQRLQQKRQETGREDGGTLAKGSLENVLDSKDKTQKSNGEKNEKCETKEKGAITAKELYTMMTDKNISLIIMDARRMQDYQDSCILHSLSVPEEAISPGVTASWIEAHLPDDSKDTWKKRGNVEYVVLLDWFSSAKDLQIGTTLRSLKDALFKWESKTVLRNEPLVLEGGYENWLLCYPQYTTNAKVTPPPRRQNEEVSISLDFTYPSLEESIPSKPAAQTPPASIEVDENIELISGQNERMGPLNISTPVEPVAASKSDVSPIIQPVPSIKNVPQIDRTKKPAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKPVVFSPTLMLTDEEKARIHAETALLMEKNKQEKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAKEEMEKKESEQAKKEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGDVPHTSVTGDSGSGKPFKIKGQPESGILRTGTFREDTDDTERNKAQREPLTRARSEEMGRIVPGLPSGWAKFLDPITGTFRYYHSPTNTVHMYPPEMAPSSAPPSTPPTHKAKPQIPAERDREPSKLKRSYSSPDITQAIQEEEKRKPTVTPTVNRENKPTCYPKAEISRLSASQIRNLNPVFGGSGPALTGLRNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHKGEVAEEFGIIMKALWTGQYRYISPKDFKITIGKINDQFAGYSQQDSQELLLFLMDGLHEDLNKADNRKRYKEENNDHLDDFKAAEHAWQKHKQLNESIIVALFQGQFKSTVQCLTCHKKSRTFEAFMYLSLPLASTSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKRFSYDGRWKQKLQTSVDFPLENLDLSQYVIGPKNNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHEVSDISVSSVKSSAAYILFYTSLGPRVTDVAT","name":"Ubiquitin carboxyl-terminal hydrolase 8","regions":[{"start":888,"end":898,"reference_id":"17035239","reference_source":"pmid","reference_html":"Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8). <i> Avvakumov GV, Walker JR, Xue S, Finerty PJ, Mackenzie F, Newman EM, Dhe-Paganon S. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2GFO"}],"region_id":"DP03012r002","statement":[{"text":"Residues 888– 898, which run antiparallel to helix 9, are disordered.","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-07T18:24:37.928Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":734,"end":761,"reference_id":"17035239","reference_source":"pmid","reference_html":"Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8). <i> Avvakumov GV, Walker JR, Xue S, Finerty PJ, Mackenzie F, Newman EM, Dhe-Paganon S. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2GFO"}],"region_id":"DP03012r003","statement":[{"text":"Based on the statement \"USP8 Catalytic Domain—At the carboxyl terminus of the\nmolecule, a 376-residue fragment containing the catalytic\ndomain of USP8 was crystallized (Fig. 4).\" and the missing electron density for this region this segment can considered as disordered.","type":"Curator statement"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-07T18:25:47.612Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_12","length":1118,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP03012","date":"2020-12-05T09:36:58.587Z","regions_counter":3,"dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI0000030306","uniref100":"UniRef100_P40818","uniref90":"UniRef90_P40818","uniref50":"UniRef50_P40818","genes":[{"name":{"value":"USP8","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:12631","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:12631"}}]},"synonyms":[{"value":"KIAA0055"},{"value":"UBPY"}]}],"alphafold_very_low_content":0.30590339892665475,"disorder_content":0.03488372093023256,"disprot_consensus":{"full":[{"start":734,"end":761,"type":"D"},{"start":888,"end":898,"type":"D"}],"Structural state":[{"start":734,"end":761,"type":"D"},{"start":888,"end":898,"type":"D"}]}},{"acc":"Q16821","features":{"pfam":[{"id":"PF03370","name":"Carbohydrate/starch-binding module (family 21)","start":123,"end":229}],"gene3D":[]},"creator":"ldobson","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MEPSEVPSQISKDNFLEVPNLSDSLCEDEEVTFQPGFSPQPSRRGSDSSEDIYLDTPSSGTRRVSFADSFGFNLVSVKEFDCWELPSASTTFDLGTDIFHTEEYVLAPLFDLPSSKEDLMQQLQIQKAILESTESLLGSTSIKGIIRVLNVSFEKLVYVRMSLDDWQTHYDILAEYVPNSCDGETDQFSFKIVLVPPYQKDGSKVEFCIRYETSVGTFWSNNNGTNYTFICQKKEQEPEPVKPWKEVPNRQIKGCLKVKSSKEESSVTSEENNFENPKNTDTYIPTIICSHEDKEDLEASNRNVKDVNREHDEHNEKELELMINQHLIRTRSTASRDERNTFSTDPVNFPNKAEGLEKKQIHGEICTDLFQRSLSPSSSAESSVKGDFYCNEKYSSGDDCTHQPSEETTSNMGEIKPSLGDTSSDELVQLHTGSKEVLDDNANPAHGNGTVQIPCPSSDQLMAGNLNKKHEGGAKNIEVKDLGCLRRDFHSDTSACLKESTEEGSSKEDYYGNGKDDEEQRIYLGVNEKQRKNFQTILHDQERKMGNPKISVAGIGASNRDLATLLSEHTAIPTRAITADVSHSPRTNLSWEEAVLTPEHHHLTSEGSALGGITGQVCSSRTGNVLRNDYLFQVEEKSGGINSEDQDNSPQHKQSWNVLESQGKSRENKTNITEHIKGQTDCEDVWGKRDNTRSLKATTEELFTCQETVCCELSSLADHGITEKAEAGTAYIIKTTSESTPESMSAREKAIIAKLPQETARSDRPIEVKETAFDPHEGRNDDSHYTLCQRDTVGVIYDNDFEKESRLGICNVRVDEMEKEETMSMYNPRKTHDREKCGTGNITSVEESSWVITEYQKATSKLDLQLGMLPTDKTVFSENRDLRQVQELSKKTDSDAIVHSAFNSDTNRAPQNSSPFSKHHTEISVSTNEQAIAVENAVTTMASQPISTKSENICNSTREIQGIEKHPYPESKPEEVSRSSGIVTSGSRKERCIGQIFQTEEYSVEKSLGPMILINKPLENMEEARHENEGLVSSGQSLYTSGEKESDSSASTSLPVEESQAQGNESLFSKYTNSKIPYFLLFLIFLITVYHYDLMIGLTFYVLSLSWLSWEEGRQKESVKKK","name":"Protein phosphatase 1 regulatory subunit 3A","regions":[{"region_id":"DP03013r001","unpublished":true,"ec_ontology":"ECO","end":60,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"SDS/PAGE analysis of the crystal revealed no obvious degradation of GM (Fig. 1E), therefore GM residues 1–60 and 82–99 included in the crystalized complex but not observed in the electron density map are most likely disordered","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-2765-3872","released":"2023_12","term_ontology":"IDPO","curator_name":"László Dobson","reference_id":"30422398","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5ZQV"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"ldobson","reference_html":"Structural basis for protein phosphatase 1 recruitment by glycogen-targeting subunits. <i> Yu J, Deng T, Xiang S. </i> FEBS J, 2018","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-08T18:58:51.295Z"}},{"region_id":"DP03013r002","unpublished":true,"ec_ontology":"ECO","end":99,"term_id":"IDPO:0000002","start":83,"version":2,"statement":[{"text":"SDS/PAGE analysis of the crystal revealed no obvious degradation of GM (Fig. 1E), therefore GM residues 1–60 and 82–99 included in the crystalized complex but not observed in the electron density map are most likely disordered","type":"Results"},{"text":"Cys82 is missing from the PDB, unclear if this affects the C-terminal disordered region","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-2765-3872","released":"2023_12","term_ontology":"IDPO","curator_name":"László Dobson","reference_id":"30422398","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5ZQV"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"ldobson","reference_html":"Structural basis for protein phosphatase 1 recruitment by glycogen-targeting subunits. <i> Yu J, Deng T, Xiang S. </i> FEBS J, 2018","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-08T18:58:50.947Z"}}],"released":"2023_12","length":1122,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP03013","date":"2020-12-05T10:11:01.934Z","regions_counter":2,"dataset":[],"UniParc":"UPI000013DDAA","uniref100":"UniRef100_Q16821","uniref90":"UniRef90_Q16821","uniref50":"UniRef50_Q16821","genes":[{"name":{"value":"PPP1R3A"},"synonyms":[{"value":"PP1G"}]}],"alphafold_very_low_content":0.7878787878787878,"disorder_content":0.06862745098039216,"disprot_consensus":{"full":[{"start":1,"end":60,"type":"D"},{"start":83,"end":99,"type":"D"}],"Structural state":[{"start":1,"end":60,"type":"D"},{"start":83,"end":99,"type":"D"}]}},{"acc":"P62137","features":{"pfam":[{"id":"PF00149","name":"Calcineurin-like phosphoesterase","start":59,"end":251},{"id":"PF16891","name":"Serine-threonine protein phosphatase N-terminal domain","start":9,"end":56}],"gene3D":[]},"creator":"ldobson","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIRYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPADKNKGKYGQFSGLNPGGRPITPPRNSAKAKK","name":"Serine/threonine-protein phosphatase PP1-alpha catalytic subunit","regions":[{"region_id":"DP03014r001","unpublished":true,"ec_ontology":"ECO","end":330,"term_id":"IDPO:0000002","start":300,"version":2,"statement":[{"text":"Similarly, PP1Cα residues 300–330 that are disordered in the crystal probably do not contribute to binding GM","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-2765-3872","released":"2022_03","term_ontology":"IDPO","curator_name":"László Dobson","reference_id":"30422398","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5ZQV"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"ldobson","reference_html":"Structural basis for protein phosphatase 1 recruitment by glycogen-targeting subunits. <i> Yu J, Deng T, Xiang S. </i> FEBS J, 2018","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_12","length":330,"ncbi_taxon_id":10090,"organism":"Mus musculus","disprot_id":"DP03014","date":"2020-12-05T10:13:55.620Z","regions_counter":1,"dataset":[],"UniParc":"UPI00000262E8","uniref100":"UniRef100_P62137","uniref90":"UniRef90_P62137","uniref50":"UniRef50_P62137","genes":[{"name":{"value":"Ppp1ca"},"synonyms":[{"value":"Ppp1a"}]}],"alphafold_very_low_content":0.09696969696969697,"disorder_content":0.09393939393939393,"disprot_consensus":{"full":[{"start":300,"end":330,"type":"D"}],"Structural state":[{"start":300,"end":330,"type":"D"}]}},{"acc":"Q86XI6","features":{"pfam":[{"id":"PF03370","name":"Carbohydrate/starch-binding module (family 21)","start":128,"end":232}],"gene3D":[]},"creator":"ldobson","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MMAVDIEYRYNCMAPSLRQERFAFKISPKPSKPLRPCIQLSSKNEASGMVAPAVQEKKVKKRVSFADNQGLALTMVKVFSEFDDPLDMPFNITELLDNIVSLTTAESESFVLDFSQPSADYLDFRNRLQADHVCLENCVLKDKAIAGTVKVQNLAFEKTVKIRMTFDTWKSYTDFPCQYVKDTYAGSDRDTFSFDISLPEKIQSYERMEFAVYYECNGQTYWDSNRGKNYRIIRAELKSTQGMTKPHSGPDLGISFDQFGSPRCSYGLFPEWPSYLGYEKLGPYY","name":"Protein phosphatase 1 regulatory subunit 3B","regions":[{"region_id":"DP03015r001","unpublished":true,"ec_ontology":"ECO","end":58,"term_id":"IDPO:0000002","start":31,"version":2,"statement":[{"text":"To test this, we reconstituted a PP1 complex containing PP1Cα (7–300) and the human GL residues 31–105 [referred to as GL (31–105) hereafter] and crystallized it.   ","type":"Results"},{"text":"The final model containing PP1Cα residues 7–299 and GL residues 59–77 (Figs. 3B) was refined to a resolution of 3.32 Å, and agrees well with the diffraction data and expected geometric values (Table 2)","type":"Results"},{"text":"Statement in the paper only describes that after crystallization of the N-terminal 31-105 residues, residues 59-77 are present. To assign this IDR region I considered that the original publication \nI) also crystallized the homologous N-terminal of Q16821 (PDB: 5ZQV), where 1-60 and 78-98 residues were described as disordered (see DP03014 - Statement: SDS/PAGE analysis of the crystal revealed no obvious degradation of GM (Fig. 1E), therefore GM residues 1–60 and 82–99 included in the crystalized complex but not observed in the electron density map are most likely disordered) AND II) Missing X-ray coordinates (PDB: 5ZT0) indeed support this region is disordered","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-2765-3872","released":"2022_03","term_ontology":"IDPO","curator_name":"László Dobson","reference_id":"30422398","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5ZT0"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"ldobson","reference_html":"Structural basis for protein phosphatase 1 recruitment by glycogen-targeting subunits. <i> Yu J, Deng T, Xiang S. </i> FEBS J, 2018","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP03015r002","unpublished":true,"ec_ontology":"ECO","end":105,"term_id":"IDPO:0000002","start":78,"version":2,"statement":[{"text":"To test this, we reconstituted a PP1 complex containing PP1Cα (7–300) and the human GL residues 31–105 [referred to as GL (31–105) hereafter] and crystallized it.   ","type":"Results"},{"text":"The final model containing PP1Cα residues 7–299 and GL residues 59–77 (Figs. 3B) was refined to a resolution of 3.32 Å, and agrees well with the diffraction data and expected geometric values (Table 2)\n","type":"Results"},{"text":"Statement in the paper only describes that after crystallization of the N-terminal 31-105 residues, residues 59-77 are present. To assign this IDR region I considered that the original publication \nI) also crystallized the homologous N-terminal of Q16821 (PDB: 5ZQV), where 1-60 and 78-98 residues were described as disordered (see DP03014 - Statement: SDS/PAGE analysis of the crystal revealed no obvious degradation of GM (Fig. 1E), therefore GM residues 1–60 and 82–99 included in the crystalized complex but not observed in the electron density map are most likely disordered) AND II) Missing X-ray coordinates (PDB: 5ZT0) indeed support this region is disordered","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-2765-3872","released":"2022_03","term_ontology":"IDPO","curator_name":"László Dobson","reference_id":"30422398","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5ZT0"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"ldobson","reference_html":"Structural basis for protein phosphatase 1 recruitment by glycogen-targeting subunits. <i> Yu J, Deng T, Xiang S. </i> FEBS J, 2018","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_12","length":285,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP03015","date":"2020-12-05T10:25:01.030Z","regions_counter":2,"dataset":[],"UniParc":"UPI000000DA40","uniref100":"UniRef100_Q86XI6","uniref90":"UniRef90_Q86XI6","uniref50":"UniRef50_Q86XI6","genes":[{"name":{"value":"PPP1R3B"},"synonyms":[{"value":"PPP1R4"}]}],"alphafold_very_low_content":0.24210526315789474,"disorder_content":0.19649122807017544,"disprot_consensus":{"full":[{"start":31,"end":58,"type":"D"},{"start":78,"end":105,"type":"D"}],"Structural state":[{"start":31,"end":58,"type":"D"},{"start":78,"end":105,"type":"D"}]}},{"acc":"P11274","features":{"pfam":[{"id":"PF00168","name":"C2 domain","start":913,"end":1007},{"id":"PF00620","name":"RhoGAP domain","start":1068,"end":1215},{"id":"PF00621","name":"RhoGEF domain","start":503,"end":689},{"id":"PF09036","name":"Bcr-Abl oncoprotein oligomerisation domain","start":3,"end":75},{"id":"PF19057","name":"PH domain","start":703,"end":775}],"gene3D":[]},"creator":"zskalman","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MVDPVGFAEAWKAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRWGFRRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGEGSPGKARPGTARRPGAAASGERDDRGPPASVAALRSNFERIRKGHGQPGADAEKPFYVNVEFHHERGLVKVNDKEVSDRISSLGSQAMQMERKKSQHGAGSSVGDASRPPYRGRSSESSCGVDGDYEDAELNPRFLKDNLIDANGGSRPPWPPLEYQPYQSIYVGGMMEGEGKGPLLRSQSTSEQEKRLTWPRRSYSPRSFEDCGGGYTPDCSSNENLTSSEEDFSSGQSSRVSPSPTTYRMFRDKSRSPSQNSQQSFDSSSPPTPQCHKRHRHCPVVVSEATIVGVRKTGQIWPNDGEGAFHGDADGSFGTPPGYGCAADRAEEQRRHQDGLPYIDDSPSSSPHLSSKGRGSRDALVSGALESTKASELDLEKGLEMRKWVLSGILASEETYLSHLEALLLPMKPLKAAATTSQPVLTSQQIETIFFKVPELYEIHKEFYDGLFPRVQQWSHQQRVGDLFQKLASQLGVYRAFVDNYGVAMEMAEKCCQANAQFAEISENLRARSNKDAKDPTTKNSLETLLYKPVDRVTRSTLVLHDLLKHTPASHPDHPLLQDALRISQNFLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVEGARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLSFQMVDELEAVPNIPLVPDEELDALKIKISQIKNDIQREKRANKGSKATERLKKKLSEQESLLLLMSPSMAFRVHSRNGKSYTFLISSDYERAEWRENIREQQKKCFRSFSLTSVELQMLTNSCVKLQTVHSIPLTINKEDDESPGLYGFLNVIVHSATGFKQSSNLYCTLEVDSFGYFVNKAKTRVYRDTAEPNWNEEFEIELEGSQTLRILCYEKCYNKTKIPKEDGESTDRLMGKGQVQLDPQALQDRDWQRTVIAMNGIEVKLSVKFNSREFSLKRMPSRKQTGVFGVKIAVVTKRERSKVPYIVRQCVEEIERRGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLFTDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSLHNLATVFGPTLLRPSEKESKLPANPSQPITMTDSWSLEVMSQVQVLLYFLQLEAIPAPDSKRQSILFSTEV","name":"Breakpoint cluster region protein","regions":[{"region_id":"DP03016r001","unpublished":true,"ec_ontology":"ECO","end":638,"term_id":"IDPO:0000002","start":622,"version":2,"statement":[{"text":"The α4–α5 loop of the Bcr-Abl DH domain is very dynamic and does not adopt a preferred conformation (Fig. 2a).","type":"Results"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-4634-0433","released":"2022_06","term_ontology":"IDPO","curator_name":"Zsófia Kálmán","reference_id":"29235475","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5N6R"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"zskalman","reference_html":"Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase. <i> Reckel S, Gehin C, Tardivon D, Georgeon S, Kükenshöner T, Löhr F, Koide A, Buchner L, Panjkovich A, Reynaud A, Pinho S, Gerig B, Svergun D, Pojer F, Güntert P, Dötsch V, Koide S, Gavin AC, Hantschel O. </i> Nat Commun, 2017","validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-15T11:10:07.215Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":624,"end":637,"reference_id":"29235475","reference_source":"pmid","reference_html":"Structural and functional dissection of the DH and PH domains of oncogenic Bcr-Abl tyrosine kinase. <i> Reckel S, Gehin C, Tardivon D, Georgeon S, Kükenshöner T, Löhr F, Koide A, Buchner L, Panjkovich A, Reynaud A, Pinho S, Gerig B, Svergun D, Pojer F, Güntert P, Dötsch V, Koide S, Gavin AC, Hantschel O. </i> Nat Commun, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":2,"cross_refs":[{"db":"PDB","id":"5N7E"}],"region_id":"DP03016r002","statement":[{"text":"No electron density was observed for the extended flexible α4–α5\nloop region seen in the NMR structure, so this loop was not\nincluded in the crystallographic model.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2022_06","length":1271,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP03016","date":"2020-12-05T10:38:17.108Z","regions_counter":2,"dataset":["Cancer-related proteins"],"UniParc":"UPI0000126848","uniref100":"UniRef100_P11274","uniref90":"UniRef90_P11274","uniref50":"UniRef50_P11274","genes":[{"name":{"value":"BCR","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:1014","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:1014"}}]},"synonyms":[{"value":"BCR1"},{"value":"D22S11"}]}],"alphafold_very_low_content":0.38630999213217937,"disorder_content":0.013375295043273014,"disprot_consensus":{"full":[{"start":622,"end":638,"type":"D"}],"Structural state":[{"start":622,"end":638,"type":"D"}]}},{"acc":"P10565","features":{"pfam":[],"gene3D":[]},"name":"Binary larvicide subunit BinB","creator":"lchemes","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Lysinibacillus"],"sequence":"MCDSKDNSGVSEKCGKKFTNYPLNTTPTSLNYNLPEISKKFYNLKNKYSRNGYGLSKTEFPSSIENCPSNEYSIMYDNKDPRFLIRFLLDDGRYIIADRDDGEVFDEAPTYLDNNNHPIISRHYTGEERQKFEQVGSGDYITGEQFFQFYTQNKTRVLSNCRALDSRTILLSTAKIFPIYPPASETQLTAFVNSSFYAAAIPQLPQTSLLENIPEPTSLDDSGVLPKDAVRAVKGSALLPCIIVHDPNLNNSDKMKFNTYYLLEYKEYWHQLWSQIIPAHQTVKIQERTGISEVVQNSMIEDLNMYIGADFGMLFYFRSSGFKEQITRGLNRPLSQTTTQLGERVEEMEYYNSNDLDVRYVKYALAREFTLKRVNGEIVKNWVAVDYRLAGIQSYPNAPITNPLTLTKHTIIRCENSYDGHIFKTPLIFKNGEVIVKTNEELIPKINQ","dataset":["Unicellular toxins and antitoxins","Bacterial virulence-related proteins"],"regions":[{"region_id":"DP03018r001","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T11:02:02.994Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":34,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"Residues 1-11 of BinA and residues 1-34 of BinB were disordered in the electron density map and therefore not included in the model (crystallization at pH 7.0)","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"27680699","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5FOZ"},{"db":"PDB","id":"5FOY"},{"db":"PDB","id":"5G37"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lchemes","reference_html":"De novo phasing with X-ray laser reveals mosquito larvicide BinAB structure. <i> Colletier JP, Sawaya MR, Gingery M, Rodriguez JA, Cascio D, Brewster AS, Michels-Clark T, Hice RH, Coquelle N, Boutet S, Williams GJ, Messerschmidt M, DePonte DP, Sierra RG, Laksmono H, Koglin JE, Hunter MS, Park HW, Uervirojnangkoorn M, Bideshi DK, Brunger AT, Federici BA, Sauter NK, Eisenberg DS. </i> Nature, 2016","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":448,"ncbi_taxon_id":1421,"organism":"Lysinibacillus sphaericus","disprot_id":"DP03018","date":"2020-12-06T23:12:42.592Z","regions_counter":1,"UniParc":"UPI0000128363","uniref100":"UniRef100_P10565","uniref90":"UniRef90_P18568","uniref50":"UniRef50_P18568","genes":[{"name":{"value":"binB"},"synonyms":[{"value":"sph04"}]}],"alphafold_very_low_content":0.11607142857142858,"disorder_content":0.07589285714285714,"disprot_consensus":{"full":[{"start":1,"end":34,"type":"D"}],"Structural state":[{"start":1,"end":34,"type":"D"}]}},{"acc":"P30996","features":{"pfam":[{"id":"PF01742","name":"Clostridial neurotoxin zinc protease","start":4,"end":409},{"id":"PF07951","name":"Clostridium neurotoxin, C-terminal receptor binding","start":1083,"end":1274},{"id":"PF07952","name":"Clostridium neurotoxin, Translocation domain","start":538,"end":847},{"id":"PF07953","name":"Clostridium neurotoxin, N-terminal receptor binding","start":877,"end":1074}],"gene3D":[]},"name":"Botulinum neurotoxin type F","creator":"lchemes","taxonomy":["Bacteria","Firmicutes","Clostridia","Eubacteriales","Clostridiaceae","Clostridium"],"sequence":"MPVAINSFNYNDPVNDDTILYMQIPYEEKSKKYYKAFEIMRNVWIIPERNTIGTNPSDFDPPASLKNGSSAYYDPNYLTTDAEKDRYLKTTIKLFKRINSNPAGKVLLQEISYAKPYLGNDHTPIDEFSPVTRTTSVNIKLSTNVESSMLLNLLVLGAGPDIFESCCYPVRKLIDPDVVYDPSNYGFGSINIVTFSPEYEYTFNDISGGHNSSTESFIADPAISLAHELIHALHGLYGARGVTYEETIEVKQAPLMIAEKPIRLEEFLTFGGQDLNIITSAMKEKIYNNLLANYEKIATRLSEVNSAPPEYDINEYKDYFQWKYGLDKNADGSYTVNENKFNEIYKKLYSFTESDLANKFKVKCRNTYFIKYEFLKVPNLLDDDIYTVSEGFNIGNLAVNNRGQSIKLNPKIIDSIPDKGLVEKIVKFCKSVIPRKGTKAPPRLCIRVNNSELFFVASESSYNENDINTPKEIDDTTNLNNNYRNNLDEVILDYNSQTIPQISNRTLNTLVQDNSYVPRYDSNGTSEIEEYDVVDFNVFFYLHAQKVPEGETNISLTSSIDTALLEESKDIFFSSEFIDTINKPVNAALFIDWISKVIRDFTTEATQKSTVDKIADISLIVPYVGLALNIIIEAEKGNFEEAFELLGVGILLEFVPELTIPVILVFTIKSYIDSYENKNKAIKAINNSLIEREAKWKEIYSWIVSNWLTRINTQFNKRKEQMYQALQNQVDAIKTAIEYKYNNYTSDEKNRLESEYNINNIEEELNKKVSLAMKNIERFMTESSISYLMKLINEAKVGKLKKYDNHVKSDLLNYILDHRSILGEQTNELSDLVTSTLNSSIPFELSSYTNDKILIIYFNRLYKKIKDSSILDMRYENNKFIDISGYGSNISINGNVYIYSTNRNQFGIYNSRLSEVNIAQNNDIIYNSRYQNFSISFWVRIPKHYKPMNHNREYTIINCMGNNNSGWKISLRTVRDCEIIWTLQDTSGNKENLIFRYEELNRISNYINKWIFVTITNNRLGNSRIYINGNLIVEKSISNLGDIHVSDNILFKIVGCDDETYVGIRYFKVFNTELDKTEIETLYSNEPDPSILKNYWGNYLLYNKKYYLFNLLRKDKYITLNSGILNINQQRGVTEGSVFLNYKLYEGVEVIIRKNGPIDISNTDNFVRKNDLAYINVVDRGVEYRLYADTKSEKEKIIRTSNLNDSLGQIIVMDSIGNNCTMNFQNNNGSNIGLLGFHSNNLVASSWYYNNIRRNTSSNGCFWSSISKENGWKE","dataset":["Unicellular toxins and antitoxins","Bacterial virulence-related proteins"],"regions":[{"region_id":"DP03019r001","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T11:17:33.999Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":214,"term_id":"IDPO:0000002","start":205,"version":2,"statement":[{"text":"The loop region Asp205-Thr214 is disordered and not modeled in both structures. Loop Glu249-Ile262 disordered and hence not modeled in form I is ordered in the form II crystal. The C-terminal residues (Val422- Lys439) are not modeled due to poor electron density in both structures. The absence of the C-terminal residues and the disordered region (Glu249-Ile262) is not due to autolysis as shown by SDS-PAGE analysis on crystals of both forms (data not shown) (24, 25).”","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"16128577","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2A97"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lchemes","reference_html":"Structural analysis of botulinum neurotoxin serotype F light chain: implications on substrate binding and inhibitor design. <i> Agarwal R, Binz T, Swaminathan S. </i> Biochemistry, 2005","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP03019r002","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T11:17:34.795Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":260,"term_id":"IDPO:0000002","start":249,"version":2,"statement":[{"text":"The loop region Asp205-Thr214 is disordered and not modeled in both structures. Loop Glu249-Ile262 disordered and hence not modeled in form I is ordered in the form II crystal. The C-terminal residues (Val422- Lys439) are not modeled due to poor electron density in both structures. The absence of the C-terminal residues and the disordered region (Glu249-Ile262) is not due to autolysis as shown by SDS-PAGE analysis on crystals of both forms (data not shown) (24, 25).”","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"16128577","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2A97"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lchemes","reference_html":"Structural analysis of botulinum neurotoxin serotype F light chain: implications on substrate binding and inhibitor design. <i> Agarwal R, Binz T, Swaminathan S. </i> Biochemistry, 2005","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP03019r003","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T11:16:28.539Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":439,"term_id":"IDPO:0000002","start":416,"version":2,"statement":[{"text":"The loop region Asp205-Thr214 is disordered and not modeled in both structures. Loop Glu249-Ile262 disordered and hence not modeled in form I is ordered in the form II crystal. The C-terminal residues (Val422- Lys439) are not modeled due to poor electron density in both structures. The absence of the C-terminal residues and the disordered region (Glu249-Ile262) is not due to autolysis as shown by SDS-PAGE analysis on crystals of both forms (data not shown) (24, 25).”","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"16128577","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2A97"},{"db":"PDB","id":"2A8A"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lchemes","reference_html":"Structural analysis of botulinum neurotoxin serotype F light chain: implications on substrate binding and inhibitor design. <i> Agarwal R, Binz T, Swaminathan S. </i> Biochemistry, 2005","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":1274,"ncbi_taxon_id":1491,"organism":"Clostridium botulinum","disprot_id":"DP03019","date":"2020-12-06T23:17:35.056Z","regions_counter":3,"UniParc":"UPI0000126B8A","uniref100":"UniRef100_P30996","uniref90":"UniRef90_P30996","uniref50":"UniRef50_A7GBG3","genes":[{"name":{"value":"botF"}}],"alphafold_very_low_content":0.018838304552590265,"disorder_content":0.03610675039246468,"disprot_consensus":{"full":[{"start":205,"end":214,"type":"D"},{"start":249,"end":260,"type":"D"},{"start":416,"end":439,"type":"D"}],"Structural state":[{"start":205,"end":214,"type":"D"},{"start":249,"end":260,"type":"D"},{"start":416,"end":439,"type":"D"}]}},{"acc":"O06522","features":{"pfam":[{"id":"PF03498","name":"Cytolethal distending toxin A/C domain","start":77,"end":220}],"gene3D":[]},"name":"Cytolethal distending toxin subunit A","creator":"lchemes","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Pasteurellales","Pasteurellaceae","Haemophilus"],"sequence":"MKKFLPSLLLMGSVACSSNQRMNDYSQPESQSDLAPKSSTIQPQPQPLLSKTPSMSLNLLSSSGPNRQVLPSEPSNFMTLMGQNGALLTVWALAKRNWLWAYPNIYSQDFGNIRNWKMEPGKHREYFRFVNQSLGTCVEAYGNGLIHDICSLDKLAQEFELLPTDSGAVVIKSVSQGRCVTYNPVSTTFYSTVTLSVCDGATEPSRDQTWYLAPPVLEATAVN","dataset":["Unicellular toxins and antitoxins","Bacterial virulence-related proteins"],"regions":[{"region_id":"DP03020r001","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T15:17:11.644Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":56,"term_id":"IDPO:0000002","start":18,"version":2,"statement":[{"text":"The N-terminal 38 residues (18–56) of the crystallized construct of CdtA are not visible in the electron density, nor are residues 183–185 of CdtB (internal loop). \n","type":"Results"},{"text":"It is probable, therefore, that residues 18–67 are normally disordered in the complex, but a fortuitous crystal-packing arrangement allowed for the region between 56 and 67 to become ordered","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"15164065","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1SR4"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lchemes","reference_html":"Assembly and function of a bacterial genotoxin. <i> Nesić D, Hsu Y, Stebbins CE. </i> Nature, 2004","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":223,"ncbi_taxon_id":233412,"organism":"Haemophilus ducreyi (strain 35000HP / ATCC 700724)","disprot_id":"DP03020","date":"2020-12-06T23:20:36.444Z","regions_counter":1,"UniParc":"UPI000012746D","uniref100":"UniRef100_O06522","uniref90":"UniRef90_O06522","uniref50":"UniRef50_O06522","genes":[{"name":{"value":"cdtA"},"olnNames":[{"value":"HD_0902"}]}],"alphafold_very_low_content":0.17937219730941703,"disorder_content":0.17488789237668162,"disprot_consensus":{"full":[{"start":18,"end":56,"type":"D"}],"Structural state":[{"start":18,"end":56,"type":"D"}]}},{"acc":"F2WK69","features":{"pfam":[{"id":"PF04829","name":"Pre-toxin domain with VENN motif","start":38,"end":87},{"id":"PF21111","name":"CDI toxin restriction endonuclease-like domain","start":252,"end":374},{"id":"PF21483","name":"Toxin CdiA-like, helical domain","start":166,"end":220}],"gene3D":[]},"name":"Toxin CdiA","creator":"lchemes","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"sequence":"MVNATLSVVQKNSAFVGSATGELAARAIGMLYPGVKQSDLSEEQKQTISTLATVSAGLAGGLTGSSTASAAVGAQSGKNAVENNYLSTNQSLTFDKELSDCRKSGGNCQDIIDKWEKISDEQSAEIDQKLKDNPLEAQVIDKEVAKGGYDMTQRPGWLGNIGVEVMTSDEAKAYVQKWNGRDLTKIDVNSPEWTKFAVFASDPENQAMLVSGGLLVKDITKAAISFMSRNTATATVNASEVGMQWGQGNMKQGMPWEDYVGKSLPADARLPKNFKIFDYYDGATKTATSVKSIDTQTMAKLANPNQVYSSIKGNIDAAAKFKEYALSGRELTSSMISNREIQLAIPADTTKTQWAEINRAIEYGKSQGVKVTVTQVK","dataset":["Unicellular toxins and antitoxins","Bacterial virulence-related proteins"],"regions":[{"region_id":"DP03021r001","validated":{"curator_id":"fquaglia","timestamp":"2020-12-10T15:19:55.467Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":164,"term_id":"IDPO:0000002","start":88,"version":2,"statement":[{"text":"The structural model contains CdiA-CTo11 EC869 residues Val85 – Lys297 (numbered from Val1 of the VENN motif) and Ala2 – Arg164 of CdiIo11 EC869","type":"Results"},{"text":"In contrast, the CdiA-CT N-terminal regions are not fully resolved in the structures and their functional significance remains unclear. The N-terminal regions are exceptionally labile to proteolysis, suggesting these domains are flexible and perhaps partially disordered. Intrinsically flexible domains are critical for colicin toxin import (23, 24), so perhaps the N-terminal region mediates CdiA-CT transport across the target cell envelope","type":"Results"},{"text":"Residue V85 mentioned by the authors, refers to residue V165 of the UNIPROT sequence and residue K297 corresponds to residue K377 of the UNIPROT sequence","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"23236156","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4G6U"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lchemes","reference_html":"Structural basis of toxicity and immunity in contact-dependent growth inhibition (CDI) systems. <i> Morse RP, Nikolakakis KC, Willett JL, Gerrick E, Low DA, Hayes CS, Goulding CW. </i> Proc Natl Acad Sci U S A, 2012","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":377,"ncbi_taxon_id":83334,"organism":"Escherichia coli O157:H7","disprot_id":"DP03021","date":"2020-12-06T23:22:51.859Z","regions_counter":1,"UniParc":"UPI00016C8341","uniref100":"UniRef100_B3BM80","uniref90":"UniRef90_B3BM80","uniref50":"UniRef50_B3BM80","genes":[],"alphafold_very_low_content":0.41909814323607425,"disorder_content":0.20424403183023873,"disprot_consensus":{"full":[{"start":88,"end":164,"type":"D"}],"Structural state":[{"start":88,"end":164,"type":"D"}]}},{"acc":"I1WVY3","features":{"pfam":[{"id":"PF05594","name":"Haemagglutinin repeat","start":337,"end":422},{"id":"PF05594","name":"Haemagglutinin repeat","start":510,"end":587},{"id":"PF05594","name":"Haemagglutinin repeat","start":748,"end":805},{"id":"PF05594","name":"Haemagglutinin repeat","start":1122,"end":1178},{"id":"PF05594","name":"Haemagglutinin repeat","start":1190,"end":1239},{"id":"PF05594","name":"Haemagglutinin repeat","start":1790,"end":1845},{"id":"PF05860","name":"TPS secretion domain","start":80,"end":330},{"id":"PF13018","name":"Extended Signal Peptide of Type V secretion system","start":1,"end":50},{"id":"PF13332","name":"Hemagglutinin repeat","start":1947,"end":2084},{"id":"PF13332","name":"Hemagglutinin repeat","start":2094,"end":2252},{"id":"PF13332","name":"Hemagglutinin repeat","start":2331,"end":2500},{"id":"PF18451","name":"Contact-dependent growth inhibition CdiA C-terminal domain","start":3036,"end":3114}],"gene3D":[]},"name":"tRNA nuclease CdiA-2","creator":"lchemes","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Burkholderia","pseudomallei group"],"sequence":"MNKNRYRVVFNRARGALMVVQENGRASHGSGSRDARAGVVPAWLSLSPFALRHVALAVLVAAGVVPIWVNAQVVAGGAHAPSVIQTQNGLQQVNINRPGASGVSMNTYNQFDVPKPGIILNNSPINVQTQLGGIIGGNPNFQAGDAARLIVNQVNSNNPSFIRGKVEIGGAAAQLVIANQAGLVVDGGGFLNTSRATLTTGNPNFGPDGSLTGFNVNQGLISVVGAGLDTANVDQVDLLARAVQINAKAYAKTLNVVAGSNQVDYNTLNATPIAANGPAPTIAIDVSQLGGMYANRVFLVSSENGVGVANAGDIAAQAGDLTLQANGRLVLSGHTNAAGNMSLSASGGIQNSGVTYGKQSVTITTGADLTNSGALTAQQNLTANVGSLNSTGTLGAGINVDSTVGTSGDLNVTSSGQLTATGTNSAAGNATFTGSGVNLSNSATAANGNLALTATAGDVNLAGSTVSAKGAVNAQASGTVVNDRGNLSSGAGMTLGGGSLSNQGGRANSQGPLSVQMAGTVSNQNGMLSSQSTADVRGSAIQNNAGLIQSAGKQTIAGASIDNSAGRLISLNADGLSVTATGALTNAAGANVSGDPGGVIGGKGDVTVQGNTVTNSGSMSADATLHVIGQSVDNGNGALHAGQTTTVDAGNHLSNAGGRVEGQSAVLNGATLDNSQGTVNAATVSLNGTTLLNHGGTVTQTGTGPMTVAITDTLDNSNNGLIQTRSTDLSLTSTTLINDNGGTITHVGPGTLTVGNGSGTVSNKAGAIASNGRTVLQGKTIDNSAGSASGQTGLSVNAADSITNLGGKLTSNANVDVTAGGALVNDGGELGSKTAATTIHSASLSNLNGKIVSPTLTATVAGLLDNSQNGDFEANQLALTAANLKNQGGHISQWQSGPTTLAVSGTLDNSNGGVIQTNSTDLTLAPAVLDNSKGTITHGGTGTLTLTPGNGAGALQNTGGTIGTNGQAIVKAGSLDNGSGVIAAKLGLSATIAGAMNNTQGLMRSNAALSIISNGALSNHQGHIEAGTPGDTSTLSIQAASIDNTDGAVHDFGTGKMTVQGGSQIVNSHAGGVDGMGQMTGQGDVTIGAASISNTQGGQLMGANLLIQGATLDNSGGQVGNVANATGDVNVAMSGAVTNTNGSITSTRDLSVAASTLLGGGAYSAARDAAINLQGDFTTTPQTQFNIGRDLTFTLPGTFANSANLQSVHNLTVNAGNIVNTGAMTAGSLLSTHSGDLTNYGAMVGGSVAIQASGTVSNLGPVALIGASDTSGLLEIVAHDIENRDDTTLGDSMPTTTIFGLGKVALAGGKDANGNYTNAALINNSSAAIQSGASMELHADKVTNTRRVMQTSGNTSQVDPALLQQLGISMSGCAAYYIAACSGQDVHWINLFHDPNYPDYDPAPIIAALKLQPGGVFTVPPNGGQWNSGYQYTTYEGKATANTVTKLSPGAQIASGGDLDASTVKTFQNYWSSVTAAGNIKQPASLDMDGWGATGQQAPGVTVVYSGYYHYNNYDNSEHNWTLPFGDKPFVGGPGGYTQAAPADVRQYSLPDYRSTWGANGTISGNGVSVNNTAANATIPSLGLLPGQAVPGLTIGTVSGNASGTQSGAAAIKGGTPTWVDPVIASATAVNVLSNLTIPQGGLYRPNSAPNPTYLIETNPAFTRMNNFLSSDYYLNQIGVNPLTTEKRLGDGFYEQQLVRNQVTQLTGKAVLGPYTDLQGMYQSLMLAGAEWSKSLNLPLGMSLSAQQVAALTTNVIIMQTETVGGQQVLVPVVYLAKADQQNANGPLITAGNIDLKNTQVFTNSGTVKADTTLALQGKQIDNAFGALQSGGLTSLDTTGNVDLTSANVKAGSLDLNAGNKLILDTATQTTHQVSRDGATSDKTTLGPAANLNVAGDASIKTGGDFQQNAGNLNVGGNLNANIGGNWNLGVQQTGEHKVVQRANGVSDTDLNSATGSTVNVGGKSAIGVGGDLTAQGARLDFGQGGTVAAKGNVTFGAASTTSTINANSSGDQGNRSYAETRHGSDQALTGTTVKGGDTLNVVSGKDINVIGSTIDLKKGDANLLAAGDVNVGAVTERHVYNSRETHSRSGVVSGTKIASSQDATSTVANGSLISADGVSIGSGKDINVQGSTVVGTHDVALNAAHDVNITTSQDTSQSSTTYQEQHSGLMSGGGLSFSVGNSKLAQQNQSSSVTNNASTVGSVDGNLTVNAGNTLHVKGSDLVAGKDVTGTAANIVVDSATDTTRQAQQQQTSKSGLTVGLSGSVGDAINNAISETQAARESAKDSNGRASALHSIAAAGDVAFGGLGAKALLDGAKGPQAPSIGVQVSVGSSHSSMQSSEDQTIQRGSSINAGGNAKLIATGNGTPKDGNITIAGSNVNAANVALIANNQVNLVNTTDTDKTQSSNSSSGSSVGVSIGTNGIGVSASMQRAHGDGNSDAAIQNNTHINASQTATIVSGGDTNVIGANVNANKVVADVGGNLNVASVQDTTVSAAHQSSAGGGFTISQTGGGASFSAQNGHADGNYAGVNEQAGIQAGSGGFDVTVKGNTDLKGAYIASTADASKNSLTTGTLTTSDIENHSHYSANSAGFSAGASVGVSTKAVGPSSVSGSGGVTPMVFQNDSGDQSATTKSAVSAGAINITKPGEQTQDVANLNRDATNLNGTVSKTPDVQKMLSQQADTMNAAQAAGQTVSQGIGLYADGKRKDAIDAAKAAYERGDLVAMQSYIDQAKSWDEGGASRAGLQATGGALIGGLGGGSVLTAIGGAAGAGTSSLLAGQAEKISKSVGDMTGSSLVGNIAANVAATVGGALVGGSAGAAMASNVELYNAGNDPQKTDDRATIAGLQGLLNQAVAAGAKGLSTIANARNAIGNAISGALDSAADQFGTLMKRDAEGKMSQSPAELVSQGVANGINTVLGSKGGEPPLAGPSAVAVDSLTGQAANAALGATDRTPPSNAILSNSNSDNNSTQGSQSGTVTKTPNPEATGSLSGKPTQIPPLSDEVTTRSLIRENQSAVTLANKGYDVVQNPEVLGPKNPDYTINGQVFDNYAPATGNVRNIATTISNKVSSGQASNIVVNLADSSASPAAIEAQINSYPIPGLGKVIVIDKLGNITIIKPKGN","dataset":["Unicellular toxins and antitoxins","RNA-binding proteins","Bacterial virulence-related proteins"],"regions":[{"region_id":"DP03022r002","validated":{"curator_id":"bmesza","timestamp":"2020-12-14T10:51:13.212Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":2987,"term_id":"IDPO:0000002","start":2948,"version":2,"statement":[{"text":"The structural model contains CdiA-CTII Bp1026b residues Gly163 – Pro294 and residues Ala2 – Arg101 of CdiIII Bp1026b","type":"Results"},{"text":"The CdiA-CTo11 EC869/CdiIo11 EC869 complex was stable; however, the N-terminus of the CdiA-CTII Bp1026b showed significant degradation after purification, suggesting that this region is sensitive to proteolysis","type":"Results"},{"text":"In contrast, the CdiA-CT N-terminal regions are not fully resolved in the structures and their functional significance remains unclear. The N-terminal regions are exceptionally labile to proteolysis, suggesting these domains are flexible and perhaps partially disordered. Intrinsically flexible domains are critical for colicin toxin import (23, 24), so perhaps the N-terminal region mediates CdiA-CT transport across the target cell envelope.","type":"Results"},{"text":"Residue G163 mentioned by the authors, refers to residue G2988 of the UNIPROT sequence and P294 refers to residue 3119 of the UNIPROT sequence","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"23236156","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4G6V"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lchemes","reference_html":"Structural basis of toxicity and immunity in contact-dependent growth inhibition (CDI) systems. <i> Morse RP, Nikolakakis KC, Willett JL, Gerrick E, Low DA, Hayes CS, Goulding CW. </i> Proc Natl Acad Sci U S A, 2012","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":3122,"ncbi_taxon_id":884204,"organism":"Burkholderia pseudomallei (strain 1026b)","disprot_id":"DP03022","date":"2020-12-06T23:24:41.109Z","regions_counter":2,"UniParc":"UPI00025C30BF","uniref100":"UniRef100_I1WVY3","uniref90":"UniRef90_I1WVY3","uniref50":"UniRef50_I1WVY3","genes":[{"name":{"value":"cdiA2"},"olnNames":[{"value":"BP1026B_II2207"}]}],"disorder_content":0.012812299807815503,"disprot_consensus":{"full":[{"start":2948,"end":2987,"type":"D"}],"Structural state":[{"start":2948,"end":2987,"type":"D"}]}},{"acc":"P43528","features":{"pfam":[{"id":"PF01375","name":"Heat-labile enterotoxin alpha chain","start":2,"end":263}],"gene3D":[]},"name":"Heat-labile enterotoxin IIB, A chain","creator":"lchemes","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"sequence":"MAKVISFFISLFLISFPLYANDYFRADSRTPDEVRRSGGLIPRGQDEAYERGTPININLYDHARGTATGNTRYNDGYVSTTTTLRQAHFLGQNMLGGYNEYYIYVVAAAPNLFDVNGVLGRYSPYPSENEYAALGGIPLSQIIGWYRVSFGAIEGGMHRNRDYRRDLFRGLSAAPNEDGYRIAGFPDGFPAWEEVPWREFAPNSCLPNNKASSDTTCASLTNKLSQHDLADFKKYIKRKFTLMTLLSINNDGFFSNNGGKDEL","dataset":["Unicellular toxins and antitoxins","Bacterial virulence-related proteins"],"regions":[{"region_id":"DP03023r001","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T11:22:27.899Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":263,"term_id":"IDPO:0000002","start":251,"version":2,"statement":[{"text":"However, the A2 linkers share only 38% sequence identity between LT-IIa and LT-IIb and have only 21% sequence\nidentity with LT-I [10,11].”\n","type":"Introduction"},{"text":"In addition, the C-terminal residues 231–243 of the A2 chain could not be traced. However, substantial yet uninterpretable electron density in the pore persists in Fo–Fc maps contoured at the 2s level, indicating a partially disordered conformation for these terminal residues","type":"Results"},{"text":"The residues referred to by the authors as 231-243 correspond to UNIPROT entry residues 251-263","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"8805549","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1TII"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lchemes","reference_html":"Crystal structure of a new heat-labile enterotoxin, LT-IIb. <i> van den Akker F, Sarfaty S, Twiddy EM, Connell TD, Holmes RK, Hol WG. </i> Structure, 1996","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP03023r002","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T11:23:59.536Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":263,"term_id":"GO:0005515","start":251,"version":3,"statement":[{"text":"The lower part of the pore holds the remaining 13 C-terminal residues, for which some electron density is present. Since the last interpretable residue (Asn230) is already two-thirds of the way down the 30 Å long pore (Fig. 8), it seems likely that not all 13 remaining residues will fit inside the lower part of the pore. The four C-terminal residues lysine, aspartate, glutamate, leucine (KDEL) in the A2 fragment of LT-IIb, being an endoplasmic reticulum (ER) retention signal [48], will thus most likely extend outside the pore, similar to the arginine, aspartate, glutamate, leucine (RDEL) terminus in LT-I [3,4].\n","type":"Results"},{"text":"In LT-IIb, residue 230 is not part of the helix and residues 231–243 could not be fit in the uninterpretable electron density present in the lower half of the pore. The interactions between A2 and the B pentamer in the upper part of the pore are entirely hydrophobic in nature by means of Phe220, Thr221, Leu222, Met223, Thr224, Leu225, Leu226, and Ile228 of A2 interacting with Met69, Ala70, Leu73 and the Cb of Ser74 of each of the B subunits. In fact, upon A2–B5 association, a surface of 1127 Å2 is buried, of which 869 Å2 is hydrophobic.","type":"Curator statement"},{"text":"\nThe residues referred to by the authors as 231-243 correspond to UNIPROT entry residues 251-263","type":"Curator statement"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"P43529","partner_end":null}],"term_name":"protein binding","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"8805549","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1TII"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"lchemes","reference_html":"Crystal structure of a new heat-labile enterotoxin, LT-IIb. <i> van den Akker F, Sarfaty S, Twiddy EM, Connell TD, Holmes RK, Hol WG. </i> Structure, 1996","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP03023r003","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T11:24:00.229Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":263,"term_id":"GO:0060090","start":251,"version":3,"statement":[{"text":"The lower part of the pore holds the remaining 13 C-terminal residues, for which some electron density is present. Since the last interpretable residue (Asn230) is already two-thirds of the way down the 30 Å long pore (Fig. 8), it seems likely that not all 13 remaining residues will fit inside the lower part of the pore. The four C-terminal residues lysine, aspartate, glutamate, leucine (KDEL) in the A2 fragment of LT-IIb, being an endoplasmic reticulum (ER) retention signal [48], will thus most likely extend outside the pore, similar to the arginine, aspartate, glutamate, leucine (RDEL) terminus in LT-I [3,4].\n","type":"Results"},{"text":"In LT-IIb, residue 230 is not part of the helix and residues 231–243 could not be fit in the uninterpretable electron density present in the lower half of the pore. The interactions between A2 and the B pentamer in the upper part of the pore are entirely hydrophobic in nature by means of Phe220, Thr221, Leu222, Met223, Thr224, Leu225, Leu226, and Ile228 of A2 interacting with Met69, Ala70, Leu73 and the Cb of Ser74 of each of the B subunits. In fact, upon A2–B5 association, a surface of 1127 Å2 is buried, of which 869 Å2 is hydrophobic.","type":"Curator statement"},{"text":"\nThe residues referred to by the authors as 231-243 correspond to UNIPROT entry residues 251-263","type":"Curator statement"}],"term_name":"molecular adaptor activity","ec_name":"x-ray crystallography evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"8805549","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1TII"}],"term_namespace":"Molecular function","ec_id":"ECO:0005670","curator_id":"lchemes","reference_html":"Crystal structure of a new heat-labile enterotoxin, LT-IIb. <i> van den Akker F, Sarfaty S, Twiddy EM, Connell TD, Holmes RK, Hol WG. </i> Structure, 1996","ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP03023r004","validated":{"curator_id":"fquaglia","timestamp":"2020-12-12T09:44:27.662Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":263,"term_id":"GO:0051179","start":258,"version":3,"statement":[{"text":"The four C-terminal residues lysine, aspartate, glutamate, leucine (KDEL) in the A2 fragment of LT-IIb, being an endoplasmic reticulum (ER) retention signal [48], will thus most likely extend outside the pore, similar to the arginine, aspartate, glutamate, leucine (RDEL) terminus in LT-I [3,4].","type":"Results"},{"text":"The involvement of the ER retention signal in LT intoxication has been postulated. However, recent studies have reached different conclusions concerning the role of RDEL/KDEL-dependent retrograde transport through the Golgi-ER during intoxication by CT and LT-I [49,50]","type":"Results"}],"term_name":"localization","ec_name":"author inference used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"GO","curator_name":"Lucia Chemes","reference_id":"8805549","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1TII"}],"term_namespace":"Biological process","ec_id":"ECO:0006216","curator_id":"lchemes","reference_html":"Crystal structure of a new heat-labile enterotoxin, LT-IIb. <i> van den Akker F, Sarfaty S, Twiddy EM, Connell TD, Holmes RK, Hol WG. </i> Structure, 1996","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false}],"released":"2020_12","length":263,"ncbi_taxon_id":562,"organism":"Escherichia coli","disprot_id":"DP03023","date":"2020-12-06T23:28:11.640Z","regions_counter":4,"UniParc":"UPI00024F0FEE","uniref100":"UniRef100_P43528","uniref90":"UniRef90_P43528","uniref50":"UniRef50_P43528","genes":[],"alphafold_very_low_content":0.09885931558935361,"disorder_content":0.049429657794676805,"disprot_consensus":{"full":[{"start":251,"end":263,"type":"D"}],"Structural state":[{"start":251,"end":263,"type":"D"}],"Molecular function":[{"start":251,"end":263,"type":"F"}],"Biological process":[{"start":258,"end":263,"type":"F"}]}},{"acc":"Q7B8V4","features":{"pfam":[{"id":"PF01742","name":"Clostridial neurotoxin zinc protease","start":4,"end":410},{"id":"PF07951","name":"Clostridium neurotoxin, C-terminal receptor binding","start":1088,"end":1293},{"id":"PF07952","name":"Clostridium neurotoxin, Translocation domain","start":549,"end":866},{"id":"PF07953","name":"Clostridium neurotoxin, N-terminal receptor binding","start":886,"end":1079}],"gene3D":[]},"name":"BoNT/A","creator":"lchemes","taxonomy":["Bacteria","Firmicutes","Clostridia","Eubacteriales","Clostridiaceae","Clostridium"],"sequence":"MPFVNKQFNYKDPVNGVDIAYIKIPNAGQMQPVKAFKIHNKIWVIPERDTFTNPEEGDLNPPPEAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYSTDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGSYRSEELNLVIIGPSADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLEVDTNPLLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNRVFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAKSIVGTTASLQYMKNVFKEKYLLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVKFFKVLNRKTYLNFDKAVFKINIVPKVNYTIYDGFNLRNTNLAANFNGQNTEINNMNFTKLKNFTGLFEFYKLLCVRGIITSKTKSLDKGYNKALNDLCIKVNNWDLFFSPSEDNFTNDLNKGEEITSDTNIEAAEENISLDLIQQYYLTFNFDNEPENISIENLSSDIIGQLELMPNIERFPNGKKYELDKYTMFHYLRAQEFEHGKSRIALTNSVNEALLNPSRVYTFFSSDYVKKVNKATEAAMFLGWVEQLVYDFTDETSEVSTTDKIADITIIIPYIGPALNIGNMLYKDDFVGALIFSGAVILLEFIPEIAIPVLGTFALVSYIANKVLTVQTIDNALSKRNEKWDEVYKYIVTNWLAKVNTQIDLIRKKMKEALENQAEATKAIINYQYNQYTEEEKNNINFNIDDLSSKLNESINKAMININKFLNQCSVSYLMNSMIPYGVKRLEDFDASLKDALLKYIYDNRGTLIGQVDRLKDKVNNTLSTDIPFQLSKYVDNQRLLSTFTEYIKNIINTSILNLRYESNHLIDLSRYASKINIGSKVNFDPIDKNQIQLFNLESSKIEVILKNAIVYNSMYENFSTSFWIRIPKYFNSISLNNEYTIINCMENNSGWKVSLNYGEIIWTLQDTQEIKQRVVFKYSQMINISDYINRWIFVTITNNRLNNSKIYINGRLIDQKPISNLGNIHASNNIMFKLDGCRDTHRYIWIKYFNLFDKELNEKEIKDLYDNQSNSGILKDFWGDYLQYDKPYYMLNLYDPNKYVDVNNVGIRGYMYLKGPRGSVMTTNIYLNSSLYRGTKFIIKKYASGNKDNIVRNNDRVYINVVVKNKEYRLATNASQAGVEKILSALEIPDVGNLSQVVVMKSKNDQGITNKCKMNLQDNNGNDIGFIGFHQFNNIAKLVASNWYNRQIERSSRTLGCSWEFIPVDDGWGERPL","dataset":["Unicellular toxins and antitoxins","Bacterial virulence-related proteins"],"regions":[{"region_id":"DP03024r001","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T11:26:10.819Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":210,"term_id":"IDPO:0000002","start":199,"version":2,"statement":[{"text":"Our structure further demonstrates the remarkable plasticity of the substrate binding cleft of the BoNT/\nA LC protease and provides a paradigm for iterative structure-based design and development of BoNT/A LC inhibitors\n","type":"Abstract"},{"text":"residues 199-210 are disordered in the structure","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"20614028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3NF3"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lchemes","reference_html":"Iterative structure-based peptide-like inhibitor design against the botulinum neurotoxin serotype A. <i> Zuniga JE, Hammill JT, Drory O, Nuss JE, Burnett JC, Gussio R, Wipf P, Bavari S, Brunger AT. </i> PLoS One, 2010","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP03024r002","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T11:26:11.475Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":255,"term_id":"IDPO:0000002","start":245,"version":2,"statement":[{"text":"Our structure further demonstrates the remarkable plasticity of the substrate binding cleft of the BoNT/\nA LC protease and provides a paradigm for iterative structure-based design and development of BoNT/A LC inhibitors\n","type":"Abstract"},{"text":"Electron density for the 250 loop of the BoNT/A LC is only observed for structures of the LC complexed with PLMs containing either no side chain (i.e. a Gly component) or an Ala in the P29 position (Figure 7C). In contrast, no electron density is observed for various residues within this loop for either the unbound form of the BoNT/A LC, or when bound to arginine hydroxamate (ArgHX) (residues 245–256), I1 (residues 250–253), or JTH-NB72-39 (residues 247–255) (Figure 7C). In all BoNT/A LC:inhibitor complexes described","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"20614028","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3NF3"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lchemes","reference_html":"Iterative structure-based peptide-like inhibitor design against the botulinum neurotoxin serotype A. <i> Zuniga JE, Hammill JT, Drory O, Nuss JE, Burnett JC, Gussio R, Wipf P, Bavari S, Brunger AT. </i> PLoS One, 2010","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":1296,"ncbi_taxon_id":1491,"organism":"Clostridium botulinum","disprot_id":"DP03024","date":"2020-12-07T02:41:18.900Z","regions_counter":2,"UniParc":"UPI0000001386","uniref100":"UniRef100_P0DPI1","uniref90":"UniRef90_P0DPI0","uniref50":"UniRef50_P0DPI0","genes":[{"name":{"value":"a","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAM75961.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAM75961.1"}}]},"synonyms":[{"value":"A","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ABD65472.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABD65472.1"}}]},{"value":"boNT","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ABD65472.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABD65472.1"}}]},{"value":"bont","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAM75961.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAM75961.1"}}]},{"value":"bonta","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ABO68833.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABO68833.1"}}]}]}],"disorder_content":0.017746913580246913,"disprot_consensus":{"full":[{"start":199,"end":210,"type":"D"},{"start":245,"end":255,"type":"D"}],"Structural state":[{"start":199,"end":210,"type":"D"},{"start":245,"end":255,"type":"D"}]}},{"acc":"A0A384E149","features":{"pfam":[{"id":"PF01742","name":"Clostridial neurotoxin zinc protease","start":5,"end":402}],"gene3D":[]},"name":"Catalytic domain of botulinum neurotoxin X","creator":"lchemes","taxonomy":["Bacteria","Firmicutes","Clostridia","Eubacteriales","Clostridiaceae","Clostridium"],"sequence":"MKLEINKFNYNDPIDGINVITMRPPRHSDKINKGKGPFKAFQVIKNIWIVPERYNFTNNTNDLNIPSEPIMEADAIYNPNYLNTPSEKDEFLQGVIKVLERIKSKPEGEKLLELISSSIPLPLVSNGALTLSDNETIAYQENNNIVSNLQANLVIYGPGPDIANNATYGLYSTPISNGEGTLSEVSFSPFYLKPFDESYGNYRSLVNIVNKFVKREFAPDPASTLMHELVHVTHNLYGISNRNFYYNFDTGKIETSRQQNSLIFEELLTFGGIDSKAISSLIIKKIIETAKNNYTTLISERLNTVTVENDLLKYIKNKIPVQGRLGNFKLDTAEFEKKLNTILFVLNESNLAQRFSILVRKHYLKERPIDPIYVNILDDNSYSTLEGFNISSQGSNDFQGQLLESSYFEKIESNALRAFIKICPRNGLLYNAIYRNSKN","dataset":["Unicellular toxins and antitoxins"],"regions":[{"region_id":"DP03026r001","validated":{"curator_id":"fquaglia","timestamp":"2020-12-10T12:25:30.422Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":439,"term_id":"IDPO:0000002","start":414,"version":2,"statement":[{"text":"Residues 1–413 were clearly defined, however no electron density was observed for the N-terminal tag and the C-terminal end (414–439), all in solvent-accessible areas","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"29540745","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6F47"},{"db":"PDB","id":"6F4E"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lchemes","reference_html":"Structural characterisation of the catalytic domain of botulinum neurotoxin X - high activity and unique substrate specificity. <i> Masuyer G, Zhang S, Barkho S, Shen Y, Henriksson L, Košenina S, Dong M, Stenmark P. </i> Sci Rep, 2018","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":439,"ncbi_taxon_id":1491,"organism":"Clostridium botulinum","disprot_id":"DP03026","date":"2020-12-07T04:16:23.376Z","regions_counter":1,"UniParc":"UPI000DC0F250","uniref100":"UniRef100_P0DPK1","uniref90":"UniRef90_P0DPK1","uniref50":"UniRef50_P0DPK1","genes":[],"alphafold_very_low_content":0.029612756264236904,"disorder_content":0.05922551252847381,"disprot_consensus":{"full":[{"start":414,"end":439,"type":"D"}],"Structural state":[{"start":414,"end":439,"type":"D"}]}},{"acc":"Q81AN8","features":{"pfam":[{"id":"PF07968","name":"Leukocidin/Hemolysin toxin family","start":62,"end":313}],"gene3D":[]},"name":"Hemolysin II","creator":"lchemes","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Bacillus","Bacillus cereus group"],"sequence":"MKKAKEIAKCVAVASVIMSGSFGLQATSAFADSKGTVENLQNGGKVYNSFKTTYDMKQNIKNSIKVSFIEDPYADKKIAIVTTDGSNIDAKYTINSGYYNAGLKWPSAYHTEAEITSGDSAQFHKAAPVNTMTSAKVTSEVGYTLGGSVKVGVNDKGPNADASITGSFAWKESVSYDQVDYKTVLETHTDKKLNWKVGFQSFNFPEWGIYNRDSFNTFYGNQLFMKSRSYNEGTNNFVSKDTVPALTGYGFSPNVVAVITADKTETTSDLKITNRRISDQYNIEWVSSKWWGTNNKDTYNEFFTNHYKLDWKNHQVTLDNQKALEEQMNSINSVNDKLNKGKGKLSLSMNGNQLKATSSNAGYGISYEDKNWGIFVNGEKVYTFNEKSTVGNISNDINKLNIKGPYIEIKQI","dataset":["Unicellular toxins and antitoxins"],"regions":[{"region_id":"DP03027r003","validated":{"curator_id":"bmesza","timestamp":"2020-12-12T20:54:41.242Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":329,"term_id":"IDPO:0000002","start":319,"version":2,"statement":[{"text":"In the WT domain, dynamic flexibility occurs at the N-terminus and the first α-helix that connects the HlyIIC domain to the HlyII-core structure. In the destabilizing P405M mutant, increased flexibility is evident throughout the first subdomain\n","type":"Abstract"},{"text":"As shown in Fig. 4A, most residues in the regular secondary structure HlyIIC have S 2 order parameters in the rigid limit. Low S2 order parameters indicative of dynamic flexibility occur for the N-terminal segment that connects HlyIIC to the rest of the HlyII protein, the N-terminal α-helix (αA), and the loops between secondary structure units - in particular the loop between helix αB and strand β5 that includes the site of the P405M mutation. The dynamic nature of the N-terminal linker segment corresponding to the first 11 amino acids of HlyIIC appears to be conserved in the full-length HlyII toxin, in as much as HlyIIC can be proteolytically cleaved from HlyII","type":"Results"},{"text":"The non-zero R2ex terms are due to conformational exchange on the µs-ms timescale. The majority of residues that experience R2ex contributions are in the two helices αA and αB","type":"Results"},{"text":"Figure 1 legend: The first 11 residues at the disordered N-terminus are not shown.","type":"Figure"},{"text":"The region is a linker between two ordered domains, and the BMRB code attached is for the P405M mutant, for which the 3D structure was calculated and the relaxation data was measured.","type":"Curator statement"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"28607368","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2N67"},{"db":"BMRB","id":"19463"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"lchemes","reference_html":"NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold. <i> Kaplan AR, Kaus K, De S, Olson R, Alexandrescu AT. </i> Sci Rep, 2017","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP03027r004","validated":{"curator_id":"bmesza","timestamp":"2020-12-12T20:54:42.689Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":329,"term_id":"IDPO:0000002","start":319,"version":2,"statement":[{"text":"In the WT domain, dynamic flexibility occurs at the N-terminus and the first α-helix that connects the HlyIIC domain to the HlyII-core structure. In the destabilizing P405M mutant, increased flexibility is evident throughout the first subdomain\n","type":"Abstract"},{"text":"Backbone amide proton protection factors in WT-HlyIIC are uniformly large for residues in regular secondary structure. The exception is helix αA, where only a single residue shows weak protection (Fig. 5B,D). In the P405M mutant (Fig. 5C), the largest protection factors are reduced about 2.5-fold compared to WT, consistent with the lower stability of the mutant to unfolding (Fig. 3B). A much more dramatic change is seen when the structure distribution of protection factors in the P405M mutant is considered. The amide protons from subdomain 2 in the second half of the molecule are protected but only two amide protons from subdomain 1 show measurable protection, at the beginning of strand β2 (Fig. 5C,E)","type":"Results"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"28607368","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2N67"}],"term_namespace":"Structural state","ec_id":"ECO:0006196","curator_id":"lchemes","reference_html":"NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold. <i> Kaplan AR, Kaus K, De S, Olson R, Alexandrescu AT. </i> Sci Rep, 2017","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP03027r005","validated":{"curator_id":"bmesza","timestamp":"2020-12-12T20:54:44.242Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":329,"term_id":"IDPO:0000033","start":319,"version":3,"statement":[{"text":"In the WT domain, dynamic flexibility occurs at the N-terminus and the first α-helix that connects the HlyIIC domain to the HlyII-core structure. In the destabilizing P405M mutant, increased flexibility is evident throughout the first subdomain\n","type":"Abstract"},{"text":"Backbone amide proton protection factors in WT-HlyIIC are uniformly large for residues in regular secondary structure. The exception is helix αA, where only a single residue shows weak protection (Fig. 5B,D). In the P405M mutant (Fig. 5C), the largest protection factors are reduced about 2.5-fold compared to WT, consistent with the lower stability of the mutant to unfolding (Fig. 3B). A much more dramatic change is seen when the structure distribution of protection factors in the P405M mutant is considered. The amide protons from subdomain 2 in the second half of the molecule are protected but only two amide protons from subdomain 1 show measurable protection, at the beginning of strand β2 (Fig. 5C,E)","type":"Results"},{"text":"The dynamic nature of the N-terminal linker segment corresponding to the first 11 amino acids of HlyIIC appears to be conserved in the full-length HlyII toxin, in as much as HlyIIC can be proteolytically cleaved from HlyII","type":"Results"},{"text":"In the monomer model (Fig. 6A), the HlyIIC domain extends from the toxin core at an edge of the β-sandwich structure opposite that of the stem loop, so that an interaction between the two segments is highly unlikely. Fig. 6B and C show the homology model of the heptameric membrane-spanning pore complex. Even with a fully extended linker, the domain appears to be too far away to interact with the pore component of the structure (Fig. 6B and C), in agreement with experimental results that indicate HlyIIC does not obstruct the toxin pore in voltage gating experiments","type":"Discussion"},{"text":"The linker segment between the N-terminus of HlyIIC domain and the C-terminus of the HlyII core is highly flexible and can be proteolytically cleaved","type":"Discussion"}],"term_name":"flexible linker","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"28607368","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2N67"}],"term_namespace":"Disorder function","ec_id":"ECO:0006165","curator_id":"lchemes","reference_html":"NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold. <i> Kaplan AR, Kaus K, De S, Olson R, Alexandrescu AT. </i> Sci Rep, 2017","ec_go":"EXP","disprot_namespace":"Disorder function"},{"region_id":"DP03027r006","validated":{"curator_id":"bmesza","timestamp":"2020-12-12T20:54:45.816Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":329,"term_id":"IDPO:0000033","start":319,"version":3,"statement":[{"text":"Limited proteolysis of the oligomers formed by HlyII and HlyII(ΔCT) on red cell membranes showed that the C‐terminal extension is sensitive to digestion, while HlyII(ΔCT) is protease resistant and migrates with an electrophoretic mobility similar to that of digested HlyII\n","type":"Abstract"},{"text":"multiple proteolytic fragments at low protease concentrations (5 μg mL−1; Fig. 3, lane 2). In contrast, the oligomeric form of HlyII(ΔCT), like the αHL heptamer, was protease resistant. At the highest concentration of proteinase K (500 μg mL−1), a protease‐resistant, SDS‐stable form of oligomeric HlyII was formed, which migrated in SDS gels with a similar mobility to oligomers formed from the genetically truncated HlyII(ΔCT) (Fig. 3). These results suggest that the C‐terminal extension either has a structure with pronounced sensitivity to proteolytic cleavage, or that the extension is connected to the rest of the protein through a readily accessible linker. The former is favored because the C terminus (TL, see below) expressed as a separate domain is protease sensitive (data not shown)","type":"Results"},{"text":"In the monomer model (Fig. 6A), the HlyIIC domain extends from the toxin core at an edge of the β-sandwich structure opposite that of the stem loop, so that an interaction between the two segments is highly unlikely. Fig. 6B and C show the homology model of the heptameric membrane-spanning pore complex. Even with a fully extended linker, the domain appears to be too far away to interact with the pore component of the structure (Fig. 6B and C), in agreement with experimental results that indicate HlyIIC does not obstruct the toxin pore in voltage gating experiments","type":"Discussion"},{"text":"The N terminal domain is defined between residues 1-288 in this paper, which corresponds to residues 31 to 318 of the Uniprot entry, and the C terminal domain is defined in this paper as residues 289-382, which corresponds to residues 319-412 of the Uniprot entry. This is consistent with the presence of the signal peptide in the Uniprot entry and the fact that this is a secreted protein.","type":"Curator statement"}],"term_name":"flexible linker","ec_name":"cleavage assay evidence used in manual assertion","curator_orcid":"0000-0003-0192-9906","released":"2022_03","term_ontology":"IDPO","curator_name":"Lucia Chemes","reference_id":"12070333","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Disorder function","ec_id":"ECO:0007691","curator_id":"lchemes","reference_html":"Properties of Bacillus cereus hemolysin II: a heptameric transmembrane pore. <i> Miles G, Bayley H, Cheley S. </i> Protein Sci, 2002","ec_go":"IDA","disprot_namespace":"Disorder function"}],"released":"2020_12","length":412,"ncbi_taxon_id":226900,"organism":"Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)","disprot_id":"DP03027","date":"2020-12-07T04:47:14.855Z","regions_counter":6,"UniParc":"UPI000018E8FD","uniref100":"UniRef100_A0A164S515","uniref90":"UniRef90_A0A0G8CGU1","uniref50":"UniRef50_A0A0G8F2B8","genes":[{"olnNames":[{"value":"BC_3523","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAP10457.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAP10457.1"}}]}]}],"alphafold_very_low_content":0.08009708737864078,"disorder_content":0.02669902912621359,"disprot_consensus":{"full":[{"start":319,"end":329,"type":"D"}],"Structural state":[{"start":319,"end":329,"type":"D"}],"Disorder function":[{"start":319,"end":329,"type":"F"}]}},{"acc":"A0A0H3GD84","features":{"pfam":[{"id":"PF01289","name":"Thiol-activated cytolysin","start":60,"end":414},{"id":"PF17440","name":"Thiol-activated cytolysin beta sandwich domain","start":418,"end":519}],"gene3D":[]},"name":"Thiol-activated cytolysin","creator":"fquaglia","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Listeriaceae","Listeria"],"sequence":"MKKIMLVFITLILVSLPIAQQTEAKDASAFNKENSISSMAPPASPPASPKTPIEKKHADEIDKYIQGLDYNKNNVLVYHGDAVTNVPPRKGYKDGNEYIVVEKKKKSINQNNADIQVVNAISSLTYPGALVKANSELVENQPDVLPVKRDSLTLSIDLPGMTNQDNKIVVKNATKSNVNNAVNTLVERWNEKYAQAYPNVSAKIDYDDEMAYSESQLIAKFGTAFKAVNNSLNVNFGAISEGKMQEEVISFKQIYYNVNVNEPTRPSRFFGKAVTKEQLQALGVNAENPPAYISSVAYGRQVYLKLSTNSHSTKVKAAFDAAVSGKSVSGDVELTNIIKNSSFKAVIYGGSAKDEVQIIDGNLGDLRDILKKGATFNRETPGVPIAYTTNFLKDNELAVIKNNSEYIETTSKAYTDGKINIDHSGGYVAQFNISWDEVNYDPEGNEIVQHKNWSENNKSKLAHFTSSIYLPGNARNINVYAKECTGLAWEWWRTVIDDRNLPLVKNRNISIWGTTLYPKYSNKVDNPIE","dataset":["Unicellular toxins and antitoxins","Bacterial virulence-related proteins"],"regions":[{"region_id":"DP03028r001","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T19:04:39.061Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":38,"term_id":"IDPO:0000002","start":25,"version":2,"statement":[{"text":"While the PEST-like sequence (aa 39–51) is well resolved (Fig. 2), the preceding residues 25–38 are, due to their flexibility, not visible in the structure.","type":"Results"}],"term_name":"disorder","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24751541","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0006224","curator_id":"fquaglia","reference_html":"Crystal structure of listeriolysin O reveals molecular details of oligomerization and pore formation. <i> Köster S, van Pee K, Hudel M, Leustik M, Rhinow D, Kühlbrandt W, Chakraborty T, Yildiz Ö. </i> Nat Commun, 2014","ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2020_12","length":529,"ncbi_taxon_id":393133,"organism":"Listeria monocytogenes serotype 1/2a (strain 10403S)","disprot_id":"DP03028","date":"2020-12-07T09:54:59.187Z","regions_counter":1,"UniParc":"UPI0000054E10","uniref100":"UniRef100_D2NZ73","uniref90":"UniRef90_Q724L1","uniref50":"UniRef50_P31830","genes":[{"olnNames":[{"value":"LMRG_02624","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AEO05213.1","url":"https://www.ebi.ac.uk/ena/browser/view/AEO05213.1"}}]}]}],"alphafold_very_low_content":0.07183364839319471,"disorder_content":0.026465028355387523,"disprot_consensus":{"full":[{"start":25,"end":38,"type":"D"}],"Structural state":[{"start":25,"end":38,"type":"D"}]}},{"acc":"Q9ZKK2","features":{"pfam":[{"id":"PF08843","name":"Nucleotidyl transferase AbiEii toxin, Type IV TA system","start":22,"end":191}],"gene3D":[]},"name":"Putative","creator":"fquaglia","taxonomy":["Bacteria","Proteobacteria","Epsilonproteobacteria","Campylobacterales","Helicobacteraceae","Helicobacter"],"sequence":"MDSKKPHYRVSLSEQALNHEKLMRAIVKNLADTPMVLKGETALYLGYGLNRFSEDLDFDCHKKINLLGRVKSAIPNGIILNDIHIKKDTDSVGRYMVRYATKDNKEEQTLKLEISYRDAPKESEVNVIEGMRIAKIERIIDNKLCACFDGEHTRTKARDLFDLHFLAKHYEEHFNLDLASRLKDFSKDPDKLVSDYLVDVKLDALLNQIMDLEETALELGVMAQLIHKKLEKQSHSLNALQEQQGYSNNDNSLDNSNENTYTPKRRR","dataset":["Unicellular toxins and antitoxins"],"regions":[{"region_id":"DP03029r001","validated":{"curator_id":"bmesza","timestamp":"2020-12-11T10:30:51.490Z","curator_name":"Bálint Mészáros"},"ec_ontology":"ECO","end":11,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"We have determined the crystal structure of JHP933 at 2.17 A ̊resolution. The refined model contains 452 residues from two monomers of the recombinant JHP933 and 257 water molecules in the crystallographic asymmetric unit. It encompasses the residues 12–232 ofJHP933 and four (or six) residues of the C-terminal tag in chain A (or B). ","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-0341-4888","released":"2022_03","term_ontology":"IDPO","curator_name":"Federica Quaglia","reference_id":"24677396","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4OK0"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"fquaglia","reference_html":"Crystal structure of JHP933 from Helicobacter pylori J99 shows two-domain architecture with a DUF1814 family nucleotidyltransferase domain and a helical bundle domain. <i> Yoon JY, Lee SJ, Kim DJ, Lee BJ, Yang JK, Suh SW. </i> Proteins, 2014","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":267,"ncbi_taxon_id":85963,"organism":"Helicobacter pylori (strain J99 / ATCC 700824)","disprot_id":"DP03029","date":"2020-12-07T10:04:28.603Z","regions_counter":1,"UniParc":"UPI00000D7292","uniref100":"UniRef100_A0A1W0VLK6","uniref90":"UniRef90_A0A438UZA0","uniref50":"UniRef50_A0A438UZA0","genes":[{"olnNames":[{"value":"jhp_0933","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAD06511.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD06511.1"}}]}]}],"alphafold_very_low_content":0.09737827715355805,"disorder_content":0.04119850187265917,"disprot_consensus":{"full":[{"start":1,"end":11,"type":"D"}],"Structural state":[{"start":1,"end":11,"type":"D"}]}},{"acc":"P76063","features":{"pfam":[{"id":"PF15943","name":"Bacterial toxin YdaS","start":9,"end":71}],"gene3D":[]},"name":"Uncharacterized protein YdaS","creator":"rpancsa","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"sequence":"MKKENYSFKQACAVVGGQSAMARLLGVSPPSVNQWIKGVRQLPAERCPAIERATRGEVLCEELRPDIDWSYLRRSACCSQNMSVKQLNDSNKSSFDHT","dataset":["Unicellular toxins and antitoxins"],"regions":[{"region_id":"DP03032r001","validated":{"curator_id":"fquaglia","timestamp":"2020-12-10T18:01:43.132Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":98,"term_id":"IDPO:0000002","start":80,"version":2,"statement":[{"text":"We show that, contrary to expectation, YdaS behaves as a monomer and contains an intrinsically disordered region at its C-terminus. This makes it the representative of a fourth yet uncharacterized class of HigA proteins.","type":"Article"},{"text":"Predicted from the backbone chemical shifts using the chemical  shift  index  (CSI)  function  and  the  DANGLE  module (Cheung et al. 2010) in CCPNMR, the secondary structure of YdaS consists of five short α-helices, followed by a tail that contains several isolated residues with a high propensity for β-strand. There is, however, only a single such stretch (residues 80–90) that contains three residues, which indicates that likely no real β-sheet is formed and that the C-terminal tail lacks regular secondary structure (Fig. 3).","type":"Article"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"31625047","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"BMRB","id":"27917"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"rpancsa","reference_html":"<sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N backbone and side chain chemical shift assignment of YdaS, a monomeric member of the HigA family. <i> Prolič-Kalinšek M, De Bruyn P, Jurėnas D, Van Melderen L, Loris R, Volkov AN. </i> Biomol NMR Assign, 2020","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":98,"ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","disprot_id":"DP03032","date":"2020-12-07T11:59:53.318Z","regions_counter":1,"UniParc":"UPI000013A8F7","uniref100":"UniRef100_P76063","uniref90":"UniRef90_P76063","uniref50":"UniRef50_P76063","genes":[{"name":{"value":"ydaS"},"olnNames":[{"value":"b1357"},{"value":"JW1352"}]}],"alphafold_very_low_content":0.030612244897959183,"disorder_content":0.19387755102040816,"disprot_consensus":{"full":[{"start":80,"end":98,"type":"D"}],"Structural state":[{"start":80,"end":98,"type":"D"}]}},{"acc":"Q48245","features":{"pfam":[{"id":"PF02691","name":"Vacuolating cyotoxin beta-helical domain","start":87,"end":758},{"id":"PF29188","name":"Vacuolating cytotoxin autotransporter VacA, C-terminal domain","start":971,"end":1287}],"gene3D":[]},"name":"Vacuolating cytotoxin autotransporter","creator":"rpancsa","taxonomy":["Bacteria","Proteobacteria","Epsilonproteobacteria","Campylobacterales","Helicobacteraceae","Helicobacter"],"sequence":"MEIQQTHRKINRPLVSLALVGALVSITPQQSHAAFFTTVIIPAIVGGIATGTAVGTVSGLLGWGLKQAEEANKTPDKPDKVWRIQAGKGFNEFPNKEYDLYKSLLSSKIDGGWDWGNAATHYWIKGGQWNKLEVDMKDAVGTYKLSGLRNFTGGDLDVNMQKATLRLGQFNGNSFTSYKDSADRTTRVDFNAKNILIDNFLEINNRVGSGAGRKASSTVLTLQASEGITSSKNAEISLYDGATLNLASNSVKLNGNVWMGRLQYVGAYLAPSYSTINTSKVTGEVNFNHLTVGDHNAAQAGIIASNKTHIGTLDLWQSAGLNIIAPPEGGYKDKPNNTPSQSGAKNDKQESSQNNSNTQVINPPNSTQKTEVQPTQVIDGPFAGGKDTVVNIDRINTKADGTIKVGGFKASLTTNAAHLNIGKGGVNLSNQASGRTLLVENLTGNITVDGPLRVNNQVGGYALAGSSANFEFKAGVDTKNGTATFNNDISLGRFVNLKVDAHTANFKGIDTGNGGFNTLDFSGVTNKVNINKLITASTNVAVKNFNINELIVKTNGVSVGEYTHFSEDIGSQSRINTVRLETGTRSIFSGGVKFKSGEKLVIDEFYYSPWNYFDARNIKNVEITRKFASSTPENPWGTSKLMFNNLTLGQNAVMDYSQFSNLTIQGDFINNQGTINYLVRGGKVATLNVGNAAAMMFNNDIDSATGFYKPLIKINSAQDLIKNTEHVLLKAKIIGYGNVSTGTNGISNVNLEEQFKERLALYNNNNRMDTCVVRNTDDIKACGMAIGNQSMVNNPDNYKYLIGKAWKNIGISKTANGSKISVYYLGNSTPTENGGNTTNLPTNTTNNARFASYALIKNAPFAHSATPNLVAINQHDFGTIESVFELANRSKDIDTLYANSGAQGRDLLQTLLIDSHDAGYARTMIDATSANEITKQLNTATTTLNNIASLEHKTSSLQTLSLSNAMILNSRLVNLSRRHTNNIDSFAKRLQALKDQRFASLESAAEVLYQFAPKYEKPTNVWANAIGGASLNNGGNASLYGTSAGVDAYLNGQVEAIVGGFGSYGYSSFNNQANSLNSGANNTNFGVYSRIFANQHEFDFEAQGALGSDQSSLNFKSALLRDLNQSYNYLAYSAATRASYGYDFAFFRNALVLKPSVGVSYNHLGSTNFKSNSTNKVALSNGSSSQHLFNASANVEARYYYGDTSYFYMNAGVLQEFANFGSSNAVSLNTFKVNATRNPLNTHARVMMGGELKLAKEVFLNLGVVYLHNLISNIGHFASNLGMRYSF","dataset":["Unicellular toxins and antitoxins","Bacterial virulence-related proteins"],"regions":[{"region_id":"DP03034r001","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T18:10:45.672Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":367,"term_id":"IDPO:0000002","start":333,"version":2,"statement":[{"text":"It is likely that the two missing regions, residues 1–26 in p33 domain and 300–334 between p33 and p55 domains, in our current map are highly flexible.","type":"Results"},{"text":"Authors mention region 300-334. Although these boundaries are true for the protein chain without signal peptide, they correspond to region 333-367 in the UniProt sequence. The 1-26 short hydrophobic region was told to be inserted into the membrane in the native protein, so it cannot be considered as disordered, this is why it was not annotated separately.","type":"Curator statement"}],"term_name":"disorder","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"30894496","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"6NYJ"},{"db":"PDB","id":"6NYF"},{"db":"PDB","id":"6NYN"},{"db":"PDB","id":"6NYM"},{"db":"PDB","id":"6NYL"},{"db":"PDB","id":"6NYG"}],"term_namespace":"Structural state","ec_id":"ECO:0006224","curator_id":"rpancsa","reference_html":"Cryo-EM structures of <i>Helicobacter pylori</i> vacuolating cytotoxin A oligomeric assemblies at near-atomic resolution. <i> Zhang K, Zhang H, Li S, Pintilie GD, Mou TC, Gao Y, Zhang Q, van den Bedem H, Schmid MF, Au SWN, Chiu W. </i> Proc Natl Acad Sci U S A, 2019","ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP03034r002","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T09:53:23.214Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":350,"term_id":"IDPO:0000002","start":339,"version":2,"statement":[{"text":"Partial proteolytic digestion of the mature secreted 88-kDa VacA toxin yields two fragments that are ∼33 and 55 kDa in mass (p33 and p55, respectively) (see Fig. 1A). This proteolytic cleavage occurs primarily between amino acids 311 and 312 of the mature secreted toxin from H. pylori strain 60190 (and possibly several adjacent sites) (27), which are predicted to comprise a hydrophilic surface-exposed loop of VacA.","type":"Article"},{"text":"The authors do not define the precise length of the digested region but mention that several neighboring residues might also be affected, therefore I have added 5 residues on each side of the two residues named as the primary cleavage site. Authors mention residues 311-312, but those correspond to residues 344-345 in the UniProt sequence due to the presence of a 33 residues long signal peptide in the latter.","type":"Curator statement"}],"term_name":"disorder","ec_name":"cleavage assay evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"15817461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Structural state","ec_id":"ECO:0007691","curator_id":"rpancsa","reference_html":"Functional properties of the p33 and p55 domains of the Helicobacter pylori vacuolating cytotoxin. <i> Torres VJ, Ivie SE, McClain MS, Cover TL. </i> J Biol Chem, 2005","ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP03034r003","validated":{"curator_id":"fquaglia","timestamp":"2020-12-11T09:53:22.343Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":350,"term_id":"IDPO:0000033","start":339,"version":3,"statement":[{"text":"Partial proteolytic digestion of the mature secreted 88-kDa VacA toxin yields two fragments that are ∼33 and 55 kDa in mass (p33 and p55, respectively) (see Fig. 1A). This proteolytic cleavage occurs primarily between amino acids 311 and 312 of the mature secreted toxin from H. pylori strain 60190 (and possibly several adjacent sites) (27), which are predicted to comprise a hydrophilic surface-exposed loop of VacA. It has been suggested that the p33 and p55 fragments represent two domains or subunits of VacA.","type":"Article"},{"text":"The authors do not define the precise length of the digested region but mention that several neighboring residues might also be affected, therefore I have added 5 residues on each side of the two residues named as the primary cleavage site. Authors mention residues 311-312, but those correspond to residues 344-345 in the UniProt sequence due to the presence of a 33 residues long signal peptide in the latter.","type":"Curator statement"}],"term_name":"flexible linker","ec_name":"cleavage assay evidence used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"15817461","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Disorder function","ec_id":"ECO:0007691","curator_id":"rpancsa","reference_html":"Functional properties of the p33 and p55 domains of the Helicobacter pylori vacuolating cytotoxin. <i> Torres VJ, Ivie SE, McClain MS, Cover TL. </i> J Biol Chem, 2005","ec_go":"IDA","disprot_namespace":"Disorder function"}],"released":"2020_12","length":1287,"ncbi_taxon_id":210,"organism":"Helicobacter pylori","disprot_id":"DP03034","date":"2020-12-07T12:20:10.653Z","regions_counter":4,"UniParc":"UPI00001380B4","uniref100":"UniRef100_Q48245","uniref90":"UniRef90_Q48245","uniref50":"UniRef50_Q48245","genes":[{"name":{"value":"vacA"}}],"alphafold_very_low_content":0.1250971250971251,"disorder_content":0.027195027195027196,"disprot_consensus":{"full":[{"start":333,"end":367,"type":"D"}],"Structural state":[{"start":333,"end":367,"type":"D"}],"Disorder function":[{"start":339,"end":350,"type":"F"}]}},{"acc":"P35269","features":{"pfam":[{"id":"PF05793","name":"Transcription initiation factor IIF, alpha subunit (TFIIF-alpha)","start":3,"end":517}],"gene3D":[]},"creator":"achasapi","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MAALGPSSQNVTEYVVRVPKNTTKKYNIMAFNAADKVNFATWNQARLERDLSNKKIYQEEEMPESGAGSEFNRKLREEARRKKYGIVLKEFRPEDQPWLLRVNGKSGRKFKGIKKGGVTENTSYYIFTQCPDGAFEAFPVHNWYNFTPLARHRTLTAEEAEEEWERRNKVLNHFSIMQQRRLKDQDQDEDEEEKEKRGRRKASELRIHDLEDDLEMSSDASDASGEEGGRVPKAKKKAPLAKGGRKKKKKKGSDDEAFEDSDDGDFEGQEVDYMSDGSSSSQEEPESKAKAPQQEEGPKGVDEQSDSSEESEEEKPPEEDKEEEEEKKAPTPQEKKRRKDSSEESDSSEESDIDSEASSALFMAKKKTPPKRERKPSGGSSRGNSRPGTPSAEGGSTSSTLRAAASKLEQGKRVSEMPAAKRLRLDTGPQSLSGKSTPQPPSGKTTPNSGDVQVTEDAVRRYLTRKPMTTKDLLKKFQTKKTGLSSEQTVNVLAQILKRLNPERKMINDKMHFSLKE","name":"General transcription factor IIF subunit 1","regions":[{"start":55,"end":92,"reference_id":"27193682","reference_source":"pmid","reference_html":"Near-atomic resolution visualization of human transcription promoter opening. <i> He Y, Yan C, Fang J, Inouye C, Tjian R, Ivanov I, Nogales E. </i> Nature, 2016","date":"2022-12-27T14:09:53.346Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5IYB"},{"db":"PDB","id":"5IY8"}],"region_id":"DP03035r004","statement":[{"text":"The cryo-EM structure of the transcription pre-initiation complex (PIC) shows this region of the General transcription factor IIF subunit 1 lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"released":"2021_12","length":517,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP03035","date":"2020-12-07T12:23:48.916Z","regions_counter":4,"dataset":[],"UniParc":"UPI00001367FB","uniref100":"UniRef100_P35269","uniref90":"UniRef90_P35269","uniref50":"UniRef50_P35269","genes":[{"name":{"value":"GTF2F1"},"synonyms":[{"value":"RAP74"}]}],"alphafold_very_low_content":0.4332688588007737,"disorder_content":0.0735009671179884,"disprot_consensus":{"full":[{"start":55,"end":92,"type":"D"}],"Structural state":[{"start":55,"end":92,"type":"D"}]}},{"acc":"Q96GX5","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":36,"end":195},{"id":"PF00069","name":"Protein kinase domain","start":738,"end":835}],"gene3D":[]},"creator":"zskalman","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MDPTAGSKKEPGGGAATEEGVNRIAVPKPPSIEEFSIVKPISRGAFGKVYLGQKGGKLYAVKVVKKADMINKNMTHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLNRDINMMDILTTPSMAKPRQDYSRTPGQVLSLISSLGFNTPIAEKNQDPANILSACLSETSQLSQGLVCPMSVDQKDTTPYSSKLLKSCLETVASNPGMPVKCLTSNLLQSRKRLATSSASSQSHTFISSVESECHSSPKWEKDCQESDEALGPTMMSWNAVEKLCAKSANAIETKGFNKKDLELALSPIHNSSALPTTGRSCVNLAKKCFSGEVSWEAVELDVNNINMDTDTSQLGFHQSNQWAVDSGGISEEHLGKRSLKRNFELVDSSPCKKIIQNKKTCVEYKHNEMTNCYTNQNTGLTVEVQDLKLSVHKSQQNDCANKENIVNSFTDKQQTPEKLPIPMIAKNLMCELDEDCEKNSKRDYLSSSFLCSDDDRASKNISMNSDSSFPGISIMESPLESQPLDSDRSIKESSFEESNIEDPLIVTPDCQEKTSPKGVENPAVQESNQKMLGPPLEVLKTLASKRNAVAFRSFNSHINASNNSEPSRMNMTSLDAMDISCAYSGSYPMAITPTQKRRSCMPHQQTPNQIKSGTPYRTPKSVRRGVAPVDDGRILGTPDYLAPELLLGRAHGPAVDWWALGVCLFEFLTGIPPFNDETPQQVFQNILKRDIPWPEGEEKLSDNAQSAVEILLTIDDTKRAGMKELKRHPLFSDVDWENLQHQTMPFIPQPDDETDTSYFEARNTAQHLTVSGFSL","name":"Serine/threonine-protein kinase greatwall","regions":[{"region_id":"DP03037r001","unpublished":true,"ec_ontology":"ECO","end":879,"term_id":"IDPO:0000002","start":855,"version":2,"statement":[{"text":"However, the active-site tether (AST) region at the extreme C-terminus of hGWL-KinDom is not visible (aa 855-879) despite being encoded in the expression construct.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-4634-0433","released":"2023_12","term_ontology":"IDPO","curator_name":"Zsófia Kálmán","reference_id":"27563826","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5LOH"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"zskalman","reference_html":"A first generation inhibitor of human Greatwall kinase, enabled by structural and functional characterisation of a minimal kinase domain construct. <i> Ocasio CA, Rajasekaran MB, Walker S, Le Grand D, Spencer J, Pearl FM, Ward SE, Savic V, Pearl LH, Hochegger H, Oliver AW. </i> Oncotarget, 2016","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-15T15:48:39.070Z"}}],"released":"2023_12","length":879,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP03037","date":"2020-12-07T14:28:41.511Z","regions_counter":1,"dataset":[],"UniParc":"UPI000004060D","uniref100":"UniRef100_Q96GX5","uniref90":"UniRef90_Q96GX5","uniref50":"UniRef50_Q96GX5","genes":[{"name":{"value":"MASTL"},"synonyms":[{"value":"GW"},{"value":"GWL"},{"value":"THC2"}]}],"alphafold_very_low_content":0.5870307167235495,"disorder_content":0.02844141069397042,"disprot_consensus":{"full":[{"start":855,"end":879,"type":"D"}],"Structural state":[{"start":855,"end":879,"type":"D"}]}},{"acc":"Q00653","features":{"pfam":[{"id":"PF00023","name":"Ankyrin repeat","start":487,"end":508},{"id":"PF00531","name":"Death domain","start":776,"end":848},{"id":"PF00554","name":"Rel homology DNA-binding domain","start":40,"end":220},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":520,"end":586},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":605,"end":697},{"id":"PF16179","name":"Rel homology dimerisation domain","start":229,"end":327}],"gene3D":[]},"creator":"zskalman","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MESCYNPGLDGIIEYDDFKLNSSIVEPKEPAPETADGPYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSELGICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQRQRLRSRPQGLTEAEQRELEQEAKELKKVMDLSIVRLRFSAFLRASDGSFSLPLKPVISQPIHDSKSPGASNLKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDENGWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTVFLQLKRKRGGDVSDSKQFTYYPLVEDKEEVQRKRRKALPTFSQPFGGGSHMGGGSGGAAGGYGGAGGGGSLGFFPSSLAYSPYQSGAGPMGCYPGGGGGAQMAATVPSRDSGEEAAEPSAPSRTPQCEPQAPEMLQRAREYNARLFGLAQRSARALLDYGVTADARALLAGQRHLLTAQDENGDTPLHLAIIHGQTSVIEQIVYVIHHAQDLGVVNLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLALRAGAGAPELLRALLQSGAPAVPQLLHMPDFEGLYPVHLAVRARSPECLDLLVDSGAEVEATERQGGRTALHLATEMEELGLVTHLVTKLRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEEPLCPLPSPPTSDSDSDSEGPEKDTRSSFRGHTPLDLTCSTKVKTLLLNAAQNTMEPPLTPPSPAGPGLSLGDTALQNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRQTTSPSGSLLRSYELAGGDLAGLLEALSDMGLEEGVRLLRGPETRDKLPSTAEVKEDSAYGSQSVEQEAEKLGPPPEPPGGLCHGHPQPQVH","name":"Nuclear factor NF-kappa-B p100 subunit","regions":[{"region_id":"DP03039r001","unpublished":true,"ec_ontology":"ECO","end":725,"term_id":"IDPO:0000002","start":702,"version":2,"statement":[{"text":"A long acidic insert (residues 702–725) between AR6 and AR7 is disordered.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-4634-0433","released":"2022_03","term_ontology":"IDPO","curator_name":"Zsófia Kálmán","reference_id":"25349408","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4OT9"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"zskalman","reference_html":"p100/IκBδ sequesters and inhibits NF-κB through kappaBsome formation. <i> Tao Z, Fusco A, Huang DB, Gupta K, Young Kim D, Ware CF, Van Duyne GD, Ghosh G. </i> Proc Natl Acad Sci U S A, 2014","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-24T17:40:09.973Z"}}],"released":"2021_12","length":900,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP03039","date":"2020-12-07T15:06:21.650Z","regions_counter":3,"dataset":["Cancer-related proteins"],"UniParc":"UPI0000160EAA","uniref100":"UniRef100_Q00653","uniref90":"UniRef90_Q00653","uniref50":"UniRef50_Q00653","genes":[{"name":{"value":"NFKB2"},"synonyms":[{"value":"LYT10"}]}],"alphafold_very_low_content":0.24,"disorder_content":0.02666666666666667,"disprot_consensus":{"full":[{"start":702,"end":725,"type":"D"}],"Structural state":[{"start":702,"end":725,"type":"D"}]}},{"acc":"A8ULG6","features":{"pfam":[{"id":"PF07968","name":"Leukocidin/Hemolysin toxin family","start":77,"end":314}],"gene3D":[]},"name":"Alpha hemolysin","creator":"rpancsa","taxonomy":["Bacteria","Firmicutes","Clostridia","Eubacteriales","Clostridiaceae","Clostridium"],"sequence":"MKRLKIISITLVLTSVISTSLFSTQTQVFASELNDINKIELKNLSGEIIKENGKEAIKYTSSDTASHKGWKATLSGTFIEDPHSDKKTALLNLEGFIPSDKQIFGSKYYGKMKWPETYRINVKSADVNNNIKIANSIPKNTIDKKDVSNSIGYSIGGNISVEGKTAGAGINASYNVQNTISYEQPDFRTIQRKDDANLASWDIKFVETKDGYNIDSYHAIYGNQLFMKSRLYNNGDKNFTDDRDLSTLISGGFSPNMALALTAPKNAKESVIIVEYQRFDNDYILNWETTQWRGTNKLSSTSEYNEFMFKINWQDHKIEYYL","dataset":["Unicellular toxins and antitoxins"],"regions":[{"region_id":"DP03040r001","validated":{"curator_id":"fquaglia","timestamp":"2020-12-10T12:26:09.281Z","curator_name":"Federica Quaglia"},"ec_ontology":"ECO","end":175,"term_id":"IDPO:0000002","start":162,"version":2,"statement":[{"text":"Residues 162 to 175 were disordered and therefore not included in the final model.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-0849-9312","released":"2022_03","term_ontology":"IDPO","curator_name":"Rita Pancsa","reference_id":"23386432","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4I0N"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"rpancsa","reference_html":"Structural and functional analysis of the pore-forming toxin NetB from Clostridium perfringens. <i> Yan XX, Porter CJ, Hardy SP, Steer D, Smith AI, Quinsey NS, Hughes V, Cheung JK, Keyburn AL, Kaldhusdal M, Moore RJ, Bannam TL, Whisstock JC, Rood JI. </i> mBio, 2013","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2020_12","length":322,"ncbi_taxon_id":1502,"organism":"Clostridium perfringens","disprot_id":"DP03040","date":"2020-12-08T00:08:55.061Z","regions_counter":1,"UniParc":"UPI00015EEE8D","uniref100":"UniRef100_A8ULG6","uniref90":"UniRef90_A8ULG6","uniref50":"UniRef50_A8ULG6","genes":[{"name":{"value":"netB","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ABW71134.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABW71134.1"}}]},"orfNames":[{"value":"CYK96_16075","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AWS27142.1","url":"https://www.ebi.ac.uk/ena/browser/view/AWS27142.1"}}]}]}],"alphafold_very_low_content":0.15838509316770186,"disorder_content":0.043478260869565216,"disprot_consensus":{"full":[{"start":162,"end":175,"type":"D"}],"Structural state":[{"start":162,"end":175,"type":"D"}]}},{"acc":"Q9UBU7","features":{"pfam":[{"id":"PF07535","name":"DBF zinc finger","start":291,"end":334}],"gene3D":[]},"creator":"zskalman","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MNSGAMRIHSKGHFQGGIQVKNEKNRPSLKSLKTDNRPEKSKCKPLWGKVFYLDLPSVTISEKLQKDIKDLGGRVEEFLSKDISYLISNKKEAKFAQTLGRISPVPSPESAYTAETTSPHPSHDGSSFKSPDTVCLSRGKLLVEKAIKDHDFIPSNSILSNALSWGVKILHIDDIRYYIEQKKKELYLLKKSSTSVRDGGKRVGSGAQKTRTGRLKKPFVKVEDMSQLYRPFYLQLTNMPFINYSIQKPCSPFDVDKPSSMQKQTQVKLRIQTDGDKYGGTSIQLQLKEKKKKGYCECCLQKYEDLETHLLSEQHRNFAQSNQYQVVDDIVSKLVFDFVEYEKDTPKKKRIKYSVGSLSPVSASVLKKTEQKEKVELQHISQKDCQEDDTTVKEQNFLYKETQETEKKLLFISEPIPHPSNELRGLNEKMSNKCSMLSTAEDDIRQNFTQLPLHKNKQECILDISEHTLSENDLEELRVDHYKCNIQASVHVSDFSTDNSGSQPKQKSDTVLFPAKDLKEKDLHSIFTHDSGLITINSSQEHLTVQAKAPFHTPPEEPNECDFKNMDSLPSGKIHRKVKIILGRNRKENLEPNAEFDKRTEFITQEENRICSSPVQSLLDLFQTSEEKSEFLGFTSYTEKSGICNVLDIWEEENSDNLLTAFFSSPSTSTFTGF","name":"Protein DBF4 homolog A","regions":[{"region_id":"DP03042r001","unpublished":true,"ec_ontology":"ECO","end":293,"term_id":"IDPO:0000002","start":255,"version":2,"statement":[{"text":"Thirty-seven residues belonging to the linker that connects the coil region of DBF4 motif M to β3 of the Zn2+ binding domain of motif C are disordered in the crystals.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-4634-0433","released":"2023_12","term_ontology":"IDPO","curator_name":"Zsófia Kálmán","reference_id":"23064647","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4F9A"},{"db":"PDB","id":"4F9C"},{"db":"PDB","id":"4F99"},{"db":"PDB","id":"4F9B"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"zskalman","reference_html":"Crystal structure of human CDC7 kinase in complex with its activator DBF4. <i> Hughes S, Elustondo F, Di Fonzo A, Leroux FG, Wong AC, Snijders AP, Matthews SJ, Cherepanov P. </i> Nat Struct Mol Biol, 2012","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-08T19:14:17.242Z"}}],"released":"2023_12","length":674,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP03042","date":"2020-12-08T11:43:19.778Z","regions_counter":2,"dataset":[],"UniParc":"UPI000000DC33","uniref100":"UniRef100_Q9UBU7","uniref90":"UniRef90_Q9UBU7","uniref50":"UniRef50_Q9UBU7","genes":[{"name":{"value":"DBF4"},"synonyms":[{"value":"ASK"},{"value":"DBF4A"},{"value":"ZDBF1"}]}],"alphafold_very_low_content":0.6275964391691394,"disorder_content":0.057863501483679525,"disprot_consensus":{"full":[{"start":255,"end":293,"type":"D"}],"Structural state":[{"start":255,"end":293,"type":"D"}]}},{"acc":"Q9JJW6","features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":77,"end":145},{"id":"PF13865","name":"C-terminal duplication domain of Friend of PRMT1","start":158,"end":214}],"gene3D":[]},"creator":"eschad","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MADKMDMSLDDIIKLNRNQRRVNRGGGPRRNRPAIARGGRNRPAPYSRPKPLPDKWQHDLFDSGCGGGEGVETGAKLLVSNLDFGVSDADIQELFAEFGTLKKAAVDYDRSGRSLGTADVHFERRADALKAMKQYKGVPLDGRPMDIQLVASQIDPQRRPAQSGNRGGMTRSRGSGGFGGRGSQGRGRGTGRNSKQQQLSAEELDAQLDAYNARMDTS","name":"Aly/REF export factor 2","regions":[{"region_id":"DP03043r001","unpublished":true,"ec_ontology":"ECO","end":74,"term_id":"IDPO:0000002","start":19,"version":2,"statement":[{"text":"The results of structural calculation revealed that the\nN-terminal residues 9–18 form an a-helix (N-helix), as\npredicted previously (Stutz et al. 2000). The helical structure is supported by the chemical shift index (Wishart and\nSykes 1994), strong sequential HN-HN NOE contacts, and\nseveral weak NOEs between residue side chains (Fig. 3A,B). One side of the N-helix is formed by hydrophobic residues,\nand the opposite side is polar. The N-helix is likely to be\ntransient, as the values of heteronuclear 15N[1\nH] NOEs for\nthis region were significantly reduced compared with those\nfor the RRM (Fig. 6B, see below), and the intensities of Ha/\nHb(i) to HN(i+3/i+4) NOE cross-peaks were smaller than\nexpected for stable a-helices. The remainder of the N domain appears largely unstructured, although some regions\nhave restricted mobility (see below).","type":"Results"},{"text":"The absence of long-range proton–proton NOEs and\nreduced 15N[1\nH] NOEs indicates that the N domain is\nflexible (Fig. 6B, see below) yet has restricted mobility in\nthe following regions: amino acids 6–23, 30–34, and 46–62,\nmapping to the N-helix, and Arg- and aromatic-rich\nregions, respectively (Fig. 1). This suggests that regions of\nthe N domain may have the propensity to form local structure and/or interact with other parts of REF2-I.","type":"Results"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0002-3006-2910","released":"2022_03","term_ontology":"IDPO","curator_name":"Eva Schad","reference_id":"17000901","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2F3J"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"eschad","reference_html":"The solution structure of REF2-I reveals interdomain interactions and regions involved in binding mRNA export factors and RNA. <i> Golovanov AP, Hautbergue GM, Tintaru AM, Lian LY, Wilson SA. </i> RNA, 2006","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-20T08:22:43.598Z"}},{"start":19,"end":58,"reference_id":"17000901","reference_source":"pmid","reference_html":"The solution structure of REF2-I reveals interdomain interactions and regions involved in binding mRNA export factors and RNA. <i> Golovanov AP, Hautbergue GM, Tintaru AM, Lian LY, Wilson SA. </i> RNA, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03043r002","statement":[{"text":"The RNA binding activity of NM was investigated here\nusing NMR chemical shift and dynamic mapping. In 50 mM\nL-Arg, L-Glu a number of residues from the N domain of\nNM displayed signal shifts on addition of a 15-mer RNA\noligonucleotide (Fig. 6A, left panel, B) with changes for\namino acids 7–24 and 29–47 being most pronounced, consistent with EMSA data (Rodrigues et al. 2001; Zenklusen et al. 2001.)","type":"Results"},{"text":"To investigate further which residues participate in RNA\nbinding we measured the changes in heteronuclear 15N[1\nH]\nNOEs that provide a quantitative parameter for mobility of\npolypeptide chain. Residues 15–58 show significantly increased heteronuclear 15N[1\nH] NOEs upon addition of\nRNA, indicating reduced mobility and direct involvement\nin RNA binding (Fig. 6B), even in high-salt buffer, yet the\nheteronuclear 15N[1\nH] NOEs for amino acids 7–14 were\nvirtually unchanged, implying these residues are not directly involved in RNA binding, despite the changes in their\namide signal positions.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-20T08:19:49.933Z"}},{"start":29,"end":41,"reference_id":"17000901","reference_source":"pmid","reference_html":"The solution structure of REF2-I reveals interdomain interactions and regions involved in binding mRNA export factors and RNA. <i> Golovanov AP, Hautbergue GM, Tintaru AM, Lian LY, Wilson SA. </i> RNA, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"O00148","partner_start":null,"partner_end":null}],"region_id":"DP03043r003","statement":[{"text":"We investigated\nthe changes in the HSQC spectra on\naddition of nonlabeled DDX39 to\n15N,2\nH-labeled NM. A significant number of NM signals in the NM:DDX39\ndisappear from the spectra due to line\nbroadening, suggesting that both the\nN and RRM domains are involved in\ncomplex formation (Fig. 8A,C).","type":"Results"},{"text":"In the N\ndomain, signals disappear within amino acids 5–16, which\nincludes a major part of the N-helix, and additionally within\namino acids 29–41 from the Arg-rich region. Together the\nbiochemical and NMR data indicate that NM presents an\nextended binding interface for DDX39 involving both the N\nand RRM domains.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-20T08:19:55.067Z"}},{"start":23,"end":48,"reference_id":"17000901","reference_source":"pmid","reference_html":"The solution structure of REF2-I reveals interdomain interactions and regions involved in binding mRNA export factors and RNA. <i> Golovanov AP, Hautbergue GM, Tintaru AM, Lian LY, Wilson SA. </i> RNA, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"Q9UBU9","partner_start":null,"partner_end":null}],"region_id":"DP03043r004","statement":[{"text":"Analysis of HSQC spectra of 15N,2\nH-NM upon addition\nof TAP-p15 revealed that signals from amino acids 8, 9, 17\n(N-helix), and 23–48 (Arg-rich) of the N domain are broadened and disappear from the spectra (Fig. 8B,C). In\ncontrast to the complex of NM with DDX39, no signals\nbelonging to the RRM disappear completely nor are shifted\nsignificantly in the NM:TAP-p15 spectra.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-20T08:21:20.400Z"}},{"start":19,"end":53,"reference_id":"17000901","reference_source":"pmid","reference_html":"The solution structure of REF2-I reveals interdomain interactions and regions involved in binding mRNA export factors and RNA. <i> Golovanov AP, Hautbergue GM, Tintaru AM, Lian LY, Wilson SA. </i> RNA, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"O00148","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9UBU9","partner_start":null,"partner_end":null}],"region_id":"DP03043r005","statement":[{"text":"We assessed the contribution of the N and RRM domains to the DDX39 interaction using GST pull-down assays (Fig. 8D). The\nD53 construct was used in these assays, since further\ntruncation of the protein leads to extensive perturbation of the HSQC spectrum for the RRM (Fig. 4C).\nWhereas NM showed a strong interaction with DDX39, the D53 construct encompassing the RRM showed a weak\ninteraction.","type":"Results"},{"text":"This is consistent with the GST pull-down data,\nwhich show that TAP interacts weakly with the RRM and\nmore strongly with NM (Fig. 8D).","type":"Results"}],"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-20T08:19:32.728Z"}},{"start":24,"end":48,"reference_id":"24550725","reference_source":"pmid","reference_html":"Competitive and cooperative interactions mediate RNA transfer from herpesvirus saimiri ORF57 to the mammalian export adaptor ALYREF. <i> Tunnicliffe RB, Hautbergue GM, Wilson SA, Kalra P, Golovanov AP. </i> PLoS Pathog, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03043r006","statement":[{"text":"The NMR experiments therefore all indicate that ALYREF\npartially displaces the viral RNA initially bound specifically to\nORF57, but retains it within the complex. In the ternary complex\nORF57 aa106–120 directly interacts with the ALYREF RRM,\nwhereas flexible flanking regions of ALYREF (aa24–48) and\nORF57 (aa81–92), and to lesser extent, parts of helix 2 of the\nALYREF RRM, jointly keep hold of the viral RNA molecule.\nInterestingly, amide signals from flexible protein regions which\nbecome involved in direct contacts with RNA (as evidenced by\nRNA-protein saturation transfer), are only partially broadened in\nthe complex. They had intensities higher than signals from the\nfolded regions, but lower than signals from the unfolded noninteracting regions (examples of this behavior can be seen in Fig. 5\nand Fig. S5). This suggests that the interaction with RNA in these\nconditions was somewhat transient and did not lead to the\nformation of a rigid 3D structure.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-20T08:19:06.708Z"}}],"released":"2021_12","length":218,"ncbi_taxon_id":10090,"organism":"Mus musculus","disprot_id":"DP03043","date":"2020-12-10T13:09:12.646Z","regions_counter":6,"dataset":["RNA-binding proteins"],"UniParc":"UPI0000028971","uniref100":"UniRef100_Q9JJW6","uniref90":"UniRef90_Q9JJW6","uniref50":"UniRef50_Q9JJW6","genes":[{"name":{"value":"Alyref2"},"synonyms":[{"value":"Ref2"},{"value":"Refbp2"}]}],"alphafold_very_low_content":0.25688073394495414,"disorder_content":0.25688073394495414,"disprot_consensus":{"full":[{"start":19,"end":74,"type":"D"}],"Structural state":[{"start":19,"end":74,"type":"D"}],"Molecular function":[{"start":19,"end":58,"type":"F"}]}},{"acc":"Q9UIF9","features":{"pfam":[{"id":"PF00439","name":"Bromodomain","start":1802,"end":1883},{"id":"PF00628","name":"PHD-finger","start":1679,"end":1723},{"id":"PF01429","name":"Methyl-CpG binding domain","start":547,"end":619},{"id":"PF02791","name":"DDT domain","start":850,"end":910},{"id":"PF15612","name":"WSTF, HB1, Itc1p, MBD9 motif 1","start":952,"end":993},{"id":"PF15613","name":"Williams-Beuren syndrome DDT (WSD), D-TOX E motif","start":1112,"end":1472}],"gene3D":[]},"creator":"eschad","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MEMEANDHFNFTGLPPAPAASGLKPSPSSGEGLYTNGSPMNFPQQGKSLNGDVNVNGLSTVSHTTTSGILNSAPHSSSTSHLHHPSVAYDCLWNYSQYPSANPGSNLKDPPLLSQFSGGQYPLNGILGGSRQPSSPSHNTNLRAGSQEFWANGTQSPMGLNFDSQELYDSFPDQNFEVMPNGPPSFFTSPQTSPMLGSSIQTFAPSQEVGSGIHPDEAAEKEMTSVVAENGTGLVGSLELEEEQPELKMCGYNGSVPSVESLHQEVSVLVPDPTVSCLDDPSHLPDQLEDTPILSEDSLEPFNSLAPEPVSGGLYGIDDTELMGAEDKLPLEDSPVISALDCPSLNNATAFSLLADDSQTSTSIFASPTSPPVLGESVLQDNSFDLNNGSDAEQEEMETQSSDFPPSLTQPAPDQSSTIQLHPATSPAVSPTTSPAVSLVVSPAASPEISPEVCPAASTVVSPAVFSVVSPASSAVLPAVSLEVPLTASVTSPKASPVTSPAAAFPTASPANKDVSSFLETTADVEEITGEGLTASGSGDVMRRRIATPEEVRLPLQHGWRREVRIKKGSHRWQGETWYYGPCGKRMKQFPEVIKYLSRNVVHSVRREHFSFSPRMPVGDFFEERDTPEGLQWVQLSAEEIPSRIQAITGKRGRPRNTEKAKTKEVPKVKRGRGRPPKVKITELLNKTDNRPLKKLEAQETLNEEDKAKIAKSKKKMRQKVQRGECQTTIQGQARNKRKQETKSLKQKEAKKKSKAEKEKGKTKQEKLKEKVKREKKEKVKMKEKEEVTKAKPACKADKTLATQRRLEERQRQQMILEEMKKPTEDMCLTDHQPLPDFSRVPGLTLPSGAFSDCLTIVEFLHSFGKVLGFDPAKDVPSLGVLQEGLLCQGDSLGEVQDLLVRLLKAALHDPGFPSYCQSLKILGEKVSEIPLTRDNVSEILRCFLMAYGVEPALCDRLRTQPFQAQPPQQKAAVLAFLVHELNGSTLIINEIDKTLESMSSYRKNKWIVEGRLRRLKTVLAKRTGRSEVEMEGPEECLGRRRSSRIMEETSGMEEEEEEESIAAVPGRRGRRDGEVDATASSIPELERQIEKLSKRQLFFRKKLLHSSQMLRAVSLGQDRYRRRYWVLPYLAGIFVEGTEGNLVPEEVIKKETDSLKVAAHASLNPALFSMKMELAGSNTTASSPARARGRPRKTKPGSMQPRHLKSPVRGQDSEQPQAQLQPEAQLHAPAQPQPQLQLQLQSHKGFLEQEGSPLSLGQSQHDLSQSAFLSWLSQTQSHSSLLSSSVLTPDSSPGKLDPAPSQPPEEPEPDEAESSPDPQALWFNISAQMPCNAAPTPPPAVSEDQPTPSPQQLASSKPMNRPSAANPCSPVQFSSTPLAGLAPKRRAGDPGEMPQSPTGLGQPKRRGRPPSKFFKQMEQRYLTQLTAQPVPPEMCSGWWWIRDPEMLDAMLKALHPRGIREKALHKHLNKHRDFLQEVCLRPSADPIFEPRQLPAFQEGIMSWSPKEKTYETDLAVLQWVEELEQRVIMSDLQIRGWTCPSPDSTREDLAYCEHLSDSQEDITWRGRGREGLAPQRKTTNPLDLAVMRLAALEQNVERRYLREPLWPTHEVVLEKALLSTPNGAPEGTTTEISYEITPRIRVWRQTLERCRSAAQVCLCLGQLERSIAWEKSVNKVTCLVCRKGDNDEFLLLCDGCDRGCHIYCHRPKMEAVPEGDWFCTVCLAQQVEGEFTQKPGFPKRGQKRKSGYSLNFSEGDGRRRRVLLRGRESPAAGPRYSEEGLSPSKRRRLSMRNHHSDLTFCEIILMEMESHDAAWPFLEPVNPRLVSGYRRIIKNPMDFSTMRERLLRGGYTSSEEFAADALLVFDNCQTFNEDDSEVGKAGHIMRRFFESRWEEFYQGKQANL","name":"Bromodomain adjacent to zinc finger domain protein 2A","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":519,"term_name":"disorder","start":496,"region_id":"DP03044r001","term_id":"IDPO:0000002","unpublished":true,"reference_html":"A novel RNA binding surface of the TAM domain of TIP5/BAZ2A mediates epigenetic regulation of rRNA genes. <i> Anosova I, Melnik S, Tripsianes K, Kateb F, Grummt I, Sattler M. </i> Nucleic Acids Res, 2015","curator_id":"eschad","released":"2023_12","term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","reference_id":"25916849","statement":[{"text":" The\n13C secondary chemical shifts, 15N relaxation rates and\nlow {1H}-\n15N heteronuclear NOE values for the amides of\nresidues 496–519 and 622–664 (comprising the AT-hooks)\nindicate that these regions are flexible and intrinsically disordered, while residues 520–621 are structured and define\nthe globular fold of the TAM domain.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-31T19:04:05.008Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":664,"term_name":"disorder","start":622,"region_id":"DP03044r002","term_id":"IDPO:0000002","unpublished":true,"reference_html":"A novel RNA binding surface of the TAM domain of TIP5/BAZ2A mediates epigenetic regulation of rRNA genes. <i> Anosova I, Melnik S, Tripsianes K, Kateb F, Grummt I, Sattler M. </i> Nucleic Acids Res, 2015","curator_id":"eschad","released":"2023_12","term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","reference_id":"25916849","statement":[{"text":" The\n13C secondary chemical shifts, 15N relaxation rates and\nlow {1H}-\n15N heteronuclear NOE values for the amides of\nresidues 496–519 and 622–664 (comprising the AT-hooks)\nindicate that these regions are flexible and intrinsically disordered, while residues 520–621 are structured and define\nthe globular fold of the TAM domain.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-31T19:04:06.269Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1731,"end":1797,"reference_id":"25533489","reference_source":"pmid","reference_html":"Molecular basis of histone tail recognition by human TIP5 PHD finger and bromodomain of the chromatin remodeling complex NoRC. <i> Tallant C, Valentini E, Fedorov O, Overvoorde L, Ferguson FM, Filippakopoulos P, Svergun DI, Knapp S, Ciulli A. </i> Structure, 2015","date":"2022-11-15T19:18:46.840Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03044r004","statement":[{"text":"Our attempts at crystallizing constructs harboring both reader domains have failed to date. Likely the unstructured nature of the linker amino acid sequence between the PHD finger and the BRD prevented our efforts in crystallizing the full-length tandem proteins.","type":"Results"},{"text":"The supplementary figure S1 shows this region is disordered.","type":"Curator statement"}]}],"released":"2023_12","length":1905,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP03044","date":"2020-12-10T14:17:32.612Z","regions_counter":4,"dataset":["RNA-binding proteins"],"UniParc":"UPI0000163B83","uniref100":"UniRef100_Q9UIF9","uniref90":"UniRef90_Q9UIF9","uniref50":"UniRef50_Q91YE5","genes":[{"name":{"value":"BAZ2A"},"synonyms":[{"value":"KIAA0314"},{"value":"TIP5"}]}],"alphafold_very_low_content":0.573228346456693,"disorder_content":0.07034120734908136,"disprot_consensus":{"full":[{"start":496,"end":519,"type":"D"},{"start":622,"end":664,"type":"D"},{"start":1731,"end":1797,"type":"D"}],"Structural state":[{"start":496,"end":519,"type":"D"},{"start":622,"end":664,"type":"D"},{"start":1731,"end":1797,"type":"D"}]}},{"acc":"P30429-2","features":{"pfam":[],"gene3D":[]},"creator":"lrodriguez","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"sequence":"MLCEIECRALSTAHTRLIHDFEPRDALTYLEGKNIFTEDHSELISKMSTRLERIANFLRIYRRQASELGPLIDFFNYNNQSHLADFLEDYIDFAINEPDLLRPVVIAPQFSRQMLDRKLLLGNVPKQMTCYIREYHVDRVIKKLDEMCDLDSFFLFLHGRAGSGKSVIASQALSKSDQLIGINYDSIVWLKDSGTAPKSTFDLFTDILLMLKSEDDLLNFPSVEHVTSVVLKRMICNALIDRPNTLFVFDDVVQEETIRWAQELRLRCLVTTRDVEISNAASQTCEFIEVTSLEIDECYDFLEAYGMPMPVGEKEEDVLNKTIELSSGNPATLMMFFKSCEPKTFEKMAQLNNKLESRGLVGVECITPYSYKSLAMALQRCVEVLSDEDRSALAFAVVMPPGVDIPVKLWSCVIPVDICSNEEEQLDDEVADRLKRLSKRGALLSGKRMPVLTFKIDHIIHMFLKHVVDAQTIANGISILEQRLLEIGNNNVSVPERHIPSHFQKFRRSSASEMYPKTTEETVIRPEDFPKFMQLHQKFYDSLKNFACC","name":"Isoform a of Cell death protein 4","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":105,"term_name":"disorder","reference_html":"Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans. <i> Yan N, Chai J, Lee ES, Gu L, Liu Q, He J, Wu JW, Kokel D, Li H, Hao Q, Xue D, Shi Y. </i> Nature, 2005","start":1,"region_id":"DP03045r001","term_id":"IDPO:0000002","unpublished":true,"version":2,"curator_id":"lrodriguez","released":"2022_03","term_ontology":"IDPO","curator_name":"Luciana Rodriguez Sawicki","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","statement":[{"text":"CED-4b exhibits a similar structure, except that its CARD domain is flexible and disordered in the crystals.","type":"Results"},{"text":"However, the CARD domain of CED-4a adopts a rigid conformation through interactions with thea/b-fold of CED-4b and CED-9, whereas the CARD domain of CED-4b is disordered in the crystals.","type":"Results"}],"curator_orcid":"0000-0001-5782-6573","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","reference_id":"16208361","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_12","length":549,"ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","disprot_id":"DP03045","date":"2020-12-10T14:48:10.590Z","regions_counter":1,"dataset":[],"UniParc":"UPI00001274C8","uniref100":"","uniref90":"","uniref50":"","genes":[{"name":{"value":"ced-4"},"orfNames":[{"value":"C35D10.9"}]}],"disorder_content":0.1912568306010929,"disprot_consensus":{"full":[{"start":1,"end":105,"type":"D"}],"Structural state":[{"start":1,"end":105,"type":"D"}]}},{"acc":"Q9J0X9","features":{"pfam":[{"id":"PF05459","name":"Herpesvirus transcriptional regulator family","start":306,"end":508},{"id":"PF16852","name":"Herpes viral adaptor-to-host cellular mRNA binding domain","start":99,"end":138}],"gene3D":[]},"creator":"eschad","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Peploviricota","Herviviricetes","Herpesvirales","Herpesviridae","Alphaherpesvirinae","Simplexvirus"],"sequence":"MATDIDMLIDLGLDLSDSDLDEDPPEPAESRRDDLESDSNGECSSSDEDMEDPHGEDGPEPILDAARPAVRPSRPEDPGVPSTQTPRPTERQGPNDPQPAPHSVWSRLGARRPSCSPERHGGKVARLQPPPTKAQPARGGRRGRRRGRGRGGPGAADGLSDPRRRAPRTNRNPGGPRPGAGWTDGPGAPHGEAWRGSEQPDPPGGPRTRSVRQAPPPLMTLAIAPPPADPRAPAPERKAPAADTIDATTRLVLRSISERAAVDRISESFGRSAQVMHDPFGGQPFPAANSPWAPVLAGQGGPFDAETRRVSWETLVAHGPSLYRTFAGNPRAASTAKAMRDCVLRQENFIEALASADETLAWCKMCIHHNLPLRPQDPIIGTAAAVLDNLATRLRPFLQCYLKARGLCGLDELCSRRRLADIKDIASFVFVILARLANRVERGVAEIDYATLGVGVGEKMHFYLPGACMAGLIEILDTHRQECSSRVCELTASHIVAPPYVHGKYFYCNSLF","name":"ICP27","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":160,"term_name":"disorder","start":1,"region_id":"DP03046r001","term_id":"IDPO:0000002","unpublished":true,"reference_html":"Three arginine residues within the RGG box are crucial for ICP27 binding to herpes simplex virus 1 GC-rich sequences and for efficient viral RNA export. <i> Corbin-Lickfett KA, Souki SK, Cocco MJ, Sandri-Goldin RM. </i> J Virol, 2010","curator_id":"eschad","released":"2022_03","term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"circular dichroism evidence used in manual assertion","version":2,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006200","reference_id":"20410270","statement":[{"text":"The CD spectra of\nthe ICP27 N-terminal 160 amino acids (Fig. 5A) were consistent with a protein in a random-coil conformation due to the\nshape of the CD curve (31).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-01T12:52:56.409Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":160,"reference_id":"20410270","reference_source":"pmid","reference_html":"Three arginine residues within the RGG box are crucial for ICP27 binding to herpes simplex virus 1 GC-rich sequences and for efficient viral RNA export. <i> Corbin-Lickfett KA, Souki SK, Cocco MJ, Sandri-Goldin RM. </i> J Virol, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03046r002","statement":[{"text":"1\nH-15N HSQC spectra\nfor the ICP27 N-terminal protein alone showed peaks that\nwere not well dispersed in the proton dimension and that\nresonated between 7.5 and 9.0 ppm (Fig. 5B). Proton HSQC\nchemical shifts in this range are typical of shifts found in\nproteins with a random-coil conformation (42). Each HSQC\nsignal represents one N-H group in the protein, and there\nshould be at least 1 peak per amino acid of the protein. Approximately 70 clearly defined HSQC peaks were observed in\nthe ICP27 N-terminal HSQC spectra, which is less than half of\nthe expected 160 HSQC peaks. There was also a high degree of\nsignal overlap in the region between 8.0 and 9.0 ppm in the\nproton dimension and in the region between 120 and 124 ppm\nin the nitrogen dimension, which prevents the resolution of all\n160 HSQC peaks. The lack of peak dispersion and the high\ndegree of peak overlap in the ICP27 N-terminal HSQC spectrum suggests that the protein is not in a single conformation,\nnor is it rigidly folded.","type":"Results"},{"text":"HET-NOE spectrum of the ICP27 N-terminal 160 amino\nacids reveals a flexible yet compact conformation.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-01T12:52:55.535Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":138,"end":150,"reference_id":"20410270","reference_source":"pmid","reference_html":"Three arginine residues within the RGG box are crucial for ICP27 binding to herpes simplex virus 1 GC-rich sequences and for efficient viral RNA export. <i> Corbin-Lickfett KA, Souki SK, Cocco MJ, Sandri-Goldin RM. </i> J Virol, 2010","date":"2022-03-08T14:06:56.183Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0003676","term_name":"nucleic acid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":4,"region_id":"DP03046r003","statement":[{"text":"The gC oligonucleotide\ngC 1-30 was shifted well by the wild-type ICP27 N-terminal\nprotein (Fig. 1B). The substitution of lysine for arginine at\nresidue 148 (R148K) or at residues 138 and 150 (R138,150K)\ndid not affect the ability of the ICP27 N terminus to shift the\ngC 1-30 sequence. An arginine-to-lysine substitution at residue\n138 or 150 also did not affect the ability of the ICP27 N\nterminus to shift gC 1-30 (data not shown). However, triple\narginine-to-lysine substitutions at residues 138, 148, and 150\nshowed reduced binding because the mutant protein did not\nefficiently shift gC 1-30. ","type":"Results"},{"text":"The R138,148,150K mutant binds poorly to GC-rich sequences bound by wild-type (WT) ICP27.","type":"Figure"},{"text":"These results suggest that three arginines at\npositions 138, 148, and 150 within the RGG box motif are all\nrequired to efficiently shift gC sequences.","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"RNAcentral","id":"URS0000EC1A22_9606","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-12T19:13:56.820Z"}},{"start":138,"end":150,"reference_id":"20410270","reference_source":"pmid","reference_html":"Three arginine residues within the RGG box are crucial for ICP27 binding to herpes simplex virus 1 GC-rich sequences and for efficient viral RNA export. <i> Corbin-Lickfett KA, Souki SK, Cocco MJ, Sandri-Goldin RM. </i> J Virol, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"GO:0003676","term_name":"nucleic acid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001163","ec_ontology":"ECO","ec_name":"co-localization evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03046r004","statement":[{"text":"To determine if arginine residues 138, 148,\nand 150 within the RGG box were also required for efficient\nRNA export by ICP27 during infection, we looked at the localization of poly(A)\b RNA at 8 h after infection, when viral\ntranscription is much more active than cellular transcription\n(40). Cells were infected with wild-type HSV-1 KOS and the\nRGG, R138,150K, and R138,148,150K mutants (Fig. 2).\nPoly(A)\b was visualized by hybridization with an oligo(dT)\nprobe. ICP27 is actively shuttling at 8 h after infection and was\nseen to be predominantly cytoplasmic in both wild-type and\nmutant infections (Fig. 2). Poly(A)\b was seen to be distributed\nin the cytoplasm of KOS-infected cells, as expected, whereas\npoly(A)\b RNA was confined to the nucleus in RGG-infected\ncells, as seen previously. Poly(A)\b RNA was seen to be present\nin the cytoplasm of cells infected with the R138,150K mutant,\nbut in contrast, poly(A)\b RNA was nuclear in cells infected\nwith the R138,148,150K mutant (Fig. 2).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-01T12:52:57.941Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a nucleic acid.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":138,"end":150,"reference_id":"20410270","reference_source":"pmid","reference_html":"Three arginine residues within the RGG box are crucial for ICP27 binding to herpes simplex virus 1 GC-rich sequences and for efficient viral RNA export. <i> Corbin-Lickfett KA, Souki SK, Cocco MJ, Sandri-Goldin RM. </i> J Virol, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"GO:0006611","term_name":"protein export from nucleus","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0001163","ec_ontology":"ECO","ec_name":"co-localization evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03046r005","statement":[{"text":"To determine if arginine residues 138, 148,\nand 150 within the RGG box were also required for efficient\nRNA export by ICP27 during infection, we looked at the localization of poly(A)\b RNA at 8 h after infection, when viral\ntranscription is much more active than cellular transcription\n(40). Cells were infected with wild-type HSV-1 KOS and the\nRGG, R138,150K, and R138,148,150K mutants (Fig. 2).\nPoly(A)\b was visualized by hybridization with an oligo(dT)\nprobe. ICP27 is actively shuttling at 8 h after infection and was\nseen to be predominantly cytoplasmic in both wild-type and\nmutant infections (Fig. 2). Poly(A)\b was seen to be distributed\nin the cytoplasm of KOS-infected cells, as expected, whereas\npoly(A)\b RNA was confined to the nucleus in RGG-infected\ncells, as seen previously. Poly(A)\b RNA was seen to be present\nin the cytoplasm of cells infected with the R138,150K mutant,\nbut in contrast, poly(A)\b RNA was nuclear in cells infected\nwith the R138,148,150K mutant (Fig. 2).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-01T12:52:59.852Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The directed movement of a protein from the nucleus into the cytoplasm.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":136,"end":140,"reference_id":"19321610","reference_source":"pmid","reference_html":"Arginine methylation of the ICP27 RGG box regulates ICP27 export and is required for efficient herpes simplex virus 1 replication. <i> Souki SK, Gershon PD, Sandri-Goldin RM. </i> J Virol, 2009","date":"2024-08-08T09:45:08.446Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000042","term_name":"methylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001215","ec_ontology":"ECO","ec_name":"in vivo methylation assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IDA","region_id":"DP03046r006","statement":[{"text":"This annotation refers to the mathylation of the Arg 138 residue of ICP27 protein.","type":"Curator statement"},{"text":"The arginines at positions 138, 148, and 150 were consistently found to be methylated in these experiments.","type":"Results"},{"text":"The arginine at position 138 was found to be dimethylated in the cytoplasmic fraction.","type":"Results"}],"term_comment":"","term_def":"\"The addition of a methyl group to an arginine residue in a protein.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-03T14:07:07.957Z"}},{"start":147,"end":151,"reference_id":"19321610","reference_source":"pmid","reference_html":"Arginine methylation of the ICP27 RGG box regulates ICP27 export and is required for efficient herpes simplex virus 1 replication. <i> Souki SK, Gershon PD, Sandri-Goldin RM. </i> J Virol, 2009","date":"2024-08-09T12:29:35.312Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000042","term_name":"methylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001215","ec_ontology":"ECO","ec_name":"in vivo methylation assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IDA","region_id":"DP03046r007","statement":[{"text":"This annotation refers to the mathylation of Arg 148  and Arg 150 residues of ICP27 protein.","type":"Curator statement"},{"text":"The arginines at positions 138, 148, and 150 were consistently found to be methylated in these experiments.","type":"Results"},{"text":"In the data analysis shown in Fig.2B, the arginine at position 148 was found to be monomethylated and the arginine at position 150 was found to be dimethylated in the nuclear sample in this experiment. ","type":"Results"}],"term_comment":"","term_def":"\"The addition of a methyl group to an arginine residue in a protein.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-03T14:07:07.705Z"}},{"start":138,"end":151,"reference_id":"19321610","reference_source":"pmid","reference_html":"Arginine methylation of the ICP27 RGG box regulates ICP27 export and is required for efficient herpes simplex virus 1 replication. <i> Souki SK, Gershon PD, Sandri-Goldin RM. </i> J Virol, 2009","date":"2024-08-09T11:59:16.351Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"GO:0045071","term_name":"negative regulation of viral genome replication","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":2,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg148Lys","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg138Lys","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg150Lys","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP03046r008","statement":[{"text":"DNA replication was also reduced relative to that for wild-type KOS, in that viral DNA copies per cell were found to be about 2.5 to 5 times lower for the mutants, as measured by quantitative real-time PCR of the glycoprotein C (gC) locus (Fig. 6B).","type":"Results"},{"text":"DNA copy number was reduced in the presence of this drug, but not to the extent seen with the arginine substitution mutants. This does suggest, however, that the arginine substitution mutants are impaired because of hypomethylation.","type":"Results"}],"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of viral genome replication.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-03T14:04:55.127Z"}},{"start":138,"end":151,"reference_id":"19321610","reference_source":"pmid","reference_html":"Arginine methylation of the ICP27 RGG box regulates ICP27 export and is required for efficient herpes simplex virus 1 replication. <i> Souki SK, Gershon PD, Sandri-Goldin RM. </i> J Virol, 2009","date":"2024-08-09T12:23:32.176Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"GO:0031647","term_name":"regulation of protein stability","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IMP","region_id":"DP03046r010","statement":[{"text":"ICP27 arginine-to-lysine mutant proteins are less stable than wild-type (WT) HSV-1 ICP27. HeLa cells were infected with WT HSV-1 KOS, ΔRGG, or the indicated ICP27 arginine-to-lysine viral mutants.","type":"Figure"},{"text":"Hypomethylation of ICP27 had two major effects, decreased protein stability ​(Fig.7) and an earlier and more rapid export of ICP27 from the nucleus to the cytoplasm (Fig.11). The same effects were observed with the methylase inhibitor AdOx. These results strongly suggest that it is the hypomethylation of ICP27, rather than structural changes that may have occurred in the RGG box associated with mutating arginines to lysines, that is responsible for the reduced stability and more-rapid nuclear export of ICP27.","type":"Discussion"},{"text":"The amminoacids sequence reported (138-151) contains three substitutions arginine to lysine at position 138, 148 and 150.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.\" [GOC:dph, GOC:mah, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg138Lys","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg148Lys","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg150Lys","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-03T14:05:54.184Z"}},{"start":138,"end":151,"reference_id":"19321610","reference_source":"pmid","reference_html":"Arginine methylation of the ICP27 RGG box regulates ICP27 export and is required for efficient herpes simplex virus 1 replication. <i> Souki SK, Gershon PD, Sandri-Goldin RM. </i> J Virol, 2009","date":"2024-08-09T11:21:51.985Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"GO:0032897","term_name":"negative regulation of viral transcription","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IMP","region_id":"DP03046r011","statement":[{"text":"Global transcription of the ICP27 arginine-to-lysine viral mutants is decreased.","type":"Figure"},{"text":"Moderate decreases in the levels of all classes of viral transcripts were seen for the three single mutants (Fig. 5, left panels), and more notable decreases in some early and late transcript levels were seen for the double and triple mutants (Fig. 5, right panels).","type":"Results"},{"text":"The amminoacids sequence reported (138-151) contains three substitutions arginine to lysine at position 138, 148 and 150.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of viral transcription.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg148Lys","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg150Lys","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg138Lys","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-03T14:02:19.819Z"}},{"start":136,"end":140,"reference_id":"19321610","reference_source":"pmid","reference_html":"Arginine methylation of the ICP27 RGG box regulates ICP27 export and is required for efficient herpes simplex virus 1 replication. <i> Souki SK, Gershon PD, Sandri-Goldin RM. </i> J Virol, 2009","date":"2024-09-11T15:41:43.292Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000042","term_name":"methylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":2,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg138Lys","start":null,"end":null,"position":null}],"ec_go":"IDA","region_id":"DP03046r012","statement":[{"text":"This annotation refers to the methylation of the Arg 138 residue of the ICP27 protein.","type":"Curator statement"},{"text":"The single substitutions R138K and R148K had relatively little effect on ICP27 methylation, while R150K produced about a twofold reduction (Fig. 3). However, the R138,150K double mutant and the R138,148,150K triple mutant showed a substantial reduction in methylation. Methylation of the d4-5 mutant (ΔRGG) was not detectable, as we saw previously.","type":"Results"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of the directed movement of proteins from the nucleus to the cytoplasm.\" [GOC:bf]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-18T10:59:04.587Z"}},{"start":147,"end":151,"reference_id":"19321610","reference_source":"pmid","reference_html":"Arginine methylation of the ICP27 RGG box regulates ICP27 export and is required for efficient herpes simplex virus 1 replication. <i> Souki SK, Gershon PD, Sandri-Goldin RM. </i> J Virol, 2009","date":"2024-09-11T15:41:30.023Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000042","term_name":"methylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg148Lys","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg150Lys","start":null,"end":null,"position":null}],"region_id":"DP03046r015","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"statement":[{"text":"This annotation refers to the methylation of the Arg 148 and Arg 150 residues of the ICP27 protein.","type":"Curator statement"},{"text":"The single substitutions R138K and R148K had relatively little effect on ICP27 methylation, while R150K produced about a twofold reduction (Fig. 3). However, the R138,150K double mutant and the R138,148,150K triple mutant showed a substantial reduction in methylation. Methylation of the d4-5 mutant (ΔRGG) was not detectable, as we saw previously.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-18T10:58:38.269Z"}},{"start":72,"end":76,"reference_id":"19321610","reference_source":"pmid","reference_html":"Arginine methylation of the ICP27 RGG box regulates ICP27 export and is required for efficient herpes simplex virus 1 replication. <i> Souki SK, Gershon PD, Sandri-Goldin RM. </i> J Virol, 2009","date":"2024-09-03T17:10:42.407Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000042","term_name":"methylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005527","ec_ontology":"ECO","ec_name":"matrix-assisted laser desorption/ionization time-of-flight mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP03046r016","statement":[{"text":"Other arginines scattered throughout the protein were also found to be methylated, but these residues were not located at the major site of methylation, the RGG box (Fig. 1B and C).","type":"Results"},{"text":"Supplementary data shows residues R74, R111 and R119, within the IDR were found to be methylated.","type":"Curator statement"}]},{"start":109,"end":113,"reference_id":"19321610","reference_source":"pmid","reference_html":"Arginine methylation of the ICP27 RGG box regulates ICP27 export and is required for efficient herpes simplex virus 1 replication. <i> Souki SK, Gershon PD, Sandri-Goldin RM. </i> J Virol, 2009","date":"2024-09-03T17:10:53.013Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000042","term_name":"methylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005527","ec_ontology":"ECO","ec_name":"matrix-assisted laser desorption/ionization time-of-flight mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP03046r017","statement":[{"text":"Other arginines scattered throughout the protein were also found to be methylated, but these residues were not located at the major site of methylation, the RGG box (Fig. 1B and C).","type":"Results"},{"text":"Supplementary data shows residues R74, R111 and R119, within the IDR were found to be methylated.","type":"Curator statement"}]},{"start":117,"end":121,"reference_id":"19321610","reference_source":"pmid","reference_html":"Arginine methylation of the ICP27 RGG box regulates ICP27 export and is required for efficient herpes simplex virus 1 replication. <i> Souki SK, Gershon PD, Sandri-Goldin RM. </i> J Virol, 2009","date":"2024-09-03T17:11:02.746Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000042","term_name":"methylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005527","ec_ontology":"ECO","ec_name":"matrix-assisted laser desorption/ionization time-of-flight mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP03046r018","statement":[{"text":"Other arginines scattered throughout the protein were also found to be methylated, but these residues were not located at the major site of methylation, the RGG box (Fig. 1B and C).","type":"Results"},{"text":"Supplementary data shows residues R74, R111 and R119, within the IDR were found to be methylated.","type":"Curator statement"}]}],"released":"2021_12","length":512,"ncbi_taxon_id":10298,"organism":"Human herpesvirus 1","disprot_id":"DP03046","date":"2020-12-10T15:37:44.452Z","regions_counter":18,"dataset":["Viral proteins","RNA-binding proteins"],"UniParc":"UPI00000F8845","uniref100":"UniRef100_Q9J0X9","uniref90":"UniRef90_P10238","uniref50":"UniRef50_P10238","genes":[{"name":{"value":"UL54","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AFE62883.1","url":"https://www.ebi.ac.uk/ena/browser/view/AFE62883.1"}}]},"orfNames":[{"value":"HHV1gp079","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AFE62883.1","url":"https://www.ebi.ac.uk/ena/browser/view/AFE62883.1"}}]}]}],"disorder_content":0.3125,"disprot_consensus":{"full":[{"start":1,"end":160,"type":"D"}],"Structural state":[{"start":1,"end":160,"type":"D"}],"Molecular function":[{"start":138,"end":150,"type":"F"}],"Biological process":[{"start":138,"end":151,"type":"F"}],"Disorder function":[{"start":72,"end":76,"type":"F"},{"start":109,"end":113,"type":"F"},{"start":117,"end":121,"type":"F"},{"start":136,"end":140,"type":"F"},{"start":147,"end":151,"type":"F"}]}},{"acc":"O62301","features":{"pfam":[{"id":"PF10220","name":"Smg8_Smg9","start":17,"end":859}],"gene3D":[]},"creator":"lrodriguez","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"sequence":"MDIAKWVEHARTCYSTQLDTKIKVIGVIGKDYPDHGKGDNINCYLRENVFPVAATEDETCTIRGHFSEDDQILFLVMNGVDDVANIRKCLKSNPKSNYFDAMAESECQQIRMLHFLFISCHFIIIFEQTSRIDLELMRFLKKVNSARIQLRKKINQRLVASDLRDVSFNNRILSSAESEGRMVVPRLLIAFQRNNIRPDVNPGKKLQRELYEKLEKNLDNQFSDILKLYDLIDCGASSLCQLNETIPVVHLLNPKIVKRDIIGEMFEILMADAENTKISGNAGTLPSNNSFVKFLEDNFRSEKNEISLENVIELMNCLQCVLDGDLEEKHEKTAIQTFIKRIQNDHMEEARRLYTNAQRPGERRGADRFKDSEKPVKIRSKEEHLMRFNEATHYIDSVVGVNSREALSQLQAQCNEMWQSDMRACESVSMMGRSCVRKIHPTFGDQTAPEHRWTAHDASNTMISTCVCGRKQLIRPEPFSVKEANSDFYDHPDFKCCRRLWRYQFQLYQEDSEEKDDIMWADRESNSLRAAKKMAQREDELAEEDTDLDIPESLLDPDSTSPSDEDDVRVRTMSSSESSSQESDAYLRPTSRRDESMASKTERELTIDHVKRMQKLELAGKSEDFLITVPNSMTTGKLPIFPSWHLTSLGDSSIYSHGAGLKNQPNFKIGGDYLSPVVVLLDVNFDVWNRDLNKIRSEDFSRKCGKDNKDDSARVKLFVGFEYECSRGHRFFVDYNGEPLIYSKGSNVIRESAHRSSLGNVLQADLPIRRPCTCRKLPLQSAQLQKVHVVTPKAPVHITIDPKVLIPTHEGVYGTGQEPLELHHSKYYILHLPTVYSGPSGAWMPGEFNPEKQGVWMGGALKVAYKPVMSFKW","name":"Protein smg-8","regions":[{"region_id":"DP03047r001","unpublished":true,"ec_ontology":"ECO","end":210,"term_id":"IDPO:0000002","start":194,"version":2,"statement":[{"text":"Disordered loops are highlighted with dotted lines.","type":"Figure"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-5782-6573","released":"2022_03","term_ontology":"IDPO","curator_name":"Luciana Rodriguez Sawicki","reference_id":"28389433","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5NKK"},{"db":"PDB","id":"5NKM"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lrodriguez","reference_html":"Structure of a SMG8-SMG9 complex identifies a G-domain heterodimer in the NMD effector proteins. <i> Li L, Lingaraju M, Basquin C, Basquin J, Conti E. </i> RNA, 2017","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":255,"end":288,"reference_id":"28389433","reference_source":"pmid","reference_html":"Structure of a SMG8-SMG9 complex identifies a G-domain heterodimer in the NMD effector proteins. <i> Li L, Lingaraju M, Basquin C, Basquin J, Conti E. </i> RNA, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5NKM"},{"db":"PDB","id":"5NKK"}],"region_id":"DP03047r002","statement":[{"text":"Disordered loops are highlighted with dotted lines.","type":"Figure"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_12","length":873,"ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","disprot_id":"DP03047","date":"2020-12-10T21:23:18.354Z","regions_counter":2,"dataset":[],"UniParc":"UPI000007A7E8","uniref100":"UniRef100_O62301","uniref90":"UniRef90_O62301","uniref50":"UniRef50_O62301","genes":[{"name":{"value":"smg-8"},"orfNames":[{"value":"K04B12.3"}]}],"alphafold_very_low_content":0.10652920962199312,"disorder_content":0.058419243986254296,"disprot_consensus":{"full":[{"start":194,"end":210,"type":"D"},{"start":255,"end":288,"type":"D"}],"Structural state":[{"start":194,"end":210,"type":"D"},{"start":255,"end":288,"type":"D"}]}},{"acc":"Q9XWJ1","features":{"pfam":[],"gene3D":[]},"creator":"lrodriguez","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"sequence":"MKKVEILKTSRPSSAGGAARPSTASPTHGAPKIAIKTRPVADDVAPTAATVIEPSQKAMKESVRFLTDFGEISDAISDLLTSSPNFNVISAIGPQGAGKSTLLSMLAGNNSRQMYREYVFRPVSREANEQSRHQTIQIDIYIVNHQIFLDCQPMYSFSIMEGLPKVRGGRFDDSTAMSDTLRLTAFLLYVSHTVLVVSETHYDKVIIDTLRVAEQIRPYLAIFRPKLAIDRKTNLVFIKTKASSIDLAPTVIREREELLRLSFQDSRWLKVSQEPFKTLIVLEEIRVRREHLFEEGDEPDEAASLNEFDEQIAELREELQKNREDFTVETAAMDEKKWLDMCREVIRDKTLHKTLKEYQRAMTDGVRTHFDNGFHAERDANKFFS","name":"Protein smg-9","regions":[{"region_id":"DP03048r001","unpublished":true,"ec_ontology":"ECO","end":133,"term_id":"IDPO:0000002","start":124,"version":2,"statement":[{"text":"The GDP moiety bound to the SMG9 G domain is shown in stick representation. Disordered loops are highlighted with dotted lines.","type":"Figure"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-5782-6573","released":"2022_03","term_ontology":"IDPO","curator_name":"Luciana Rodriguez Sawicki","reference_id":"28389433","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5NKM"},{"db":"PDB","id":"5NKK"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lrodriguez","reference_html":"Structure of a SMG8-SMG9 complex identifies a G-domain heterodimer in the NMD effector proteins. <i> Li L, Lingaraju M, Basquin C, Basquin J, Conti E. </i> RNA, 2017","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP03048r002","unpublished":true,"ec_ontology":"ECO","end":171,"term_id":"IDPO:0000002","start":153,"version":2,"statement":[{"text":"First, there is a conserved proline residue (Pro153SMG9, disordered in the present structure) at the position of switch 2 typically occupied by a glycine (Fig. 2B,C).","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-5782-6573","released":"2022_03","term_ontology":"IDPO","curator_name":"Luciana Rodriguez Sawicki","reference_id":"28389433","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5NKM"},{"db":"PDB","id":"5NKK"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lrodriguez","reference_html":"Structure of a SMG8-SMG9 complex identifies a G-domain heterodimer in the NMD effector proteins. <i> Li L, Lingaraju M, Basquin C, Basquin J, Conti E. </i> RNA, 2017","ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP03048r003","unpublished":true,"ec_ontology":"ECO","end":307,"term_id":"IDPO:0000002","start":285,"version":2,"statement":[{"text":"At the corresponding position of Asp218Atlastin, SMG9 features a conserved lysine residue (Lys241SMG9) that stacks with its aliphatic portion on top of the guanine base. With the caveat that motif  G5 is largely  disordered, none of the interactions in the current structure engage guanine-specific moieties. ","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-5782-6573","released":"2022_03","term_ontology":"IDPO","curator_name":"Luciana Rodriguez Sawicki","reference_id":"28389433","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5NKM"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lrodriguez","reference_html":"Structure of a SMG8-SMG9 complex identifies a G-domain heterodimer in the NMD effector proteins. <i> Li L, Lingaraju M, Basquin C, Basquin J, Conti E. </i> RNA, 2017","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":124,"end":133,"reference_id":"28389433","reference_source":"pmid","reference_html":"Structure of a SMG8-SMG9 complex identifies a G-domain heterodimer in the NMD effector proteins. <i> Li L, Lingaraju M, Basquin C, Basquin J, Conti E. </i> RNA, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"5NKM"},{"db":"PDB","id":"5NKK"}],"interaction_partner":[{"db":"UniProt","id":"O62301","partner_start":null,"partner_end":null}],"region_id":"DP03048r004","statement":[{"text":"The G domains of SMG8c and SMG9c face each other and interact with part of their convex surfaces (Fig. 1B).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":107,"end":139,"reference_id":"28389433","reference_source":"pmid","reference_html":"Structure of a SMG8-SMG9 complex identifies a G-domain heterodimer in the NMD effector proteins. <i> Li L, Lingaraju M, Basquin C, Basquin J, Conti E. </i> RNA, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"GO:0140313","term_name":"molecular sequestering activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"5NKK"}],"region_id":"DP03048r005","statement":[{"text":"GDP binds SMG9c at a similar position as in Atlastin and GBP1, in particular with similarities at the phosphatebinding loops, e.g., at the motifs G1 (P loop), G2 (switch 1), and G3 (switch 2) (Fig. 2B,C). In SMG9c, the P loop residues Lys99SMG9 and Ser100SMG9 coordinate the phosphates of GDP. Although parts of the switch regions are disordered in our GDP-bound structure, the switch 2 residue Asp150SMG9 is at the position expected for coordinating the magnesium ion, while the switch 1 residue Thr135SMG9 is 10 Å away from the position expected upon γ -phosphate binding.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":150,"end":176,"reference_id":"28389433","reference_source":"pmid","reference_html":"Structure of a SMG8-SMG9 complex identifies a G-domain heterodimer in the NMD effector proteins. <i> Li L, Lingaraju M, Basquin C, Basquin J, Conti E. </i> RNA, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"GO:0140313","term_name":"molecular sequestering activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"5NKK"}],"region_id":"DP03048r006","statement":[{"text":"GDP binds SMG9c at a similar position as in Atlastin and GBP1, in particular with similarities at the phosphatebinding loops, e.g., at the motifs G1 (P loop), G2 (switch 1), and G3 (switch 2) (Fig. 2B,C). In SMG9c, the P loop residues Lys99SMG9 and Ser100SMG9 coordinate the phosphates of GDP. Although parts of the switch regions are disordered in our GDP-bound structure, the switch 2 residue Asp150SMG9 is at the position expected for coordinating the magnesium ion, while the switch 1 residue Thr135SMG9 is 10 Å away from the position expected upon γ -phosphate binding.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":150,"end":176,"reference_id":"28389433","reference_source":"pmid","reference_html":"Structure of a SMG8-SMG9 complex identifies a G-domain heterodimer in the NMD effector proteins. <i> Li L, Lingaraju M, Basquin C, Basquin J, Conti E. </i> RNA, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5NKK"}],"region_id":"DP03048r007","statement":[{"text":"GDP binds SMG9c at a similar position as in Atlastin and GBP1, in particular with similarities at the phosphatebinding loops, e.g., at the motifs G1 (P loop), G2 (switch 1), and G3 (switch 2) (Fig. 2B,C). In SMG9c, the P loop residues Lys99SMG9 and Ser100SMG9 coordinate the phosphates of GDP. Although parts of the switch regions are disordered in our GDP-bound structure, the switch 2 residue Asp150SMG9 is at the position expected for coordinating the magnesium ion, while the switch 1 residue Thr135SMG9 is 10 Å away from the position expected upon γ -phosphate binding.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":107,"end":139,"reference_id":"28389433","reference_source":"pmid","reference_html":"Structure of a SMG8-SMG9 complex identifies a G-domain heterodimer in the NMD effector proteins. <i> Li L, Lingaraju M, Basquin C, Basquin J, Conti E. </i> RNA, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5NKK"}],"region_id":"DP03048r008","statement":[{"text":"GDP binds SMG9c at a similar position as in Atlastin and GBP1, in particular with similarities at the phosphatebinding loops, e.g., at the motifs G1 (P loop), G2 (switch 1), and G3 (switch 2) (Fig. 2B,C). In SMG9c, the P loop residues Lys99SMG9 and Ser100SMG9 coordinate the phosphates of GDP. Although parts of the switch regions are disordered in our GDP-bound structure, the switch 2 residue Asp150SMG9 is at the position expected for coordinating the magnesium ion, while the switch 1 residue Thr135SMG9 is 10 Å away from the position expected upon γ -phosphate binding.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_12","length":385,"ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","disprot_id":"DP03048","date":"2020-12-10T21:30:31.878Z","regions_counter":8,"dataset":[],"UniParc":"UPI0000075C7C","uniref100":"UniRef100_Q9XWJ1","uniref90":"UniRef90_Q9XWJ1","uniref50":"UniRef50_Q9XWJ1","genes":[{"name":{"value":"smg-9"},"orfNames":[{"value":"Y54E2A.2"}]}],"alphafold_very_low_content":0.21298701298701297,"disorder_content":0.21558441558441557,"disprot_consensus":{"full":[{"start":107,"end":139,"type":"D"},{"start":150,"end":176,"type":"D"},{"start":285,"end":307,"type":"D"}],"Structural state":[{"start":107,"end":139,"type":"D"},{"start":150,"end":176,"type":"D"},{"start":285,"end":307,"type":"D"}],"Molecular function":[{"start":107,"end":139,"type":"F"},{"start":150,"end":176,"type":"F"}]}},{"acc":"Q18235","features":{"pfam":[],"gene3D":[]},"creator":"lrodriguez","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"sequence":"MEDLNFEERGSTQIPASLQQHFSAKLGRQNELEKTPSRGGLGLVVNSSKTPGGKSLQSLASACKVPPSTKKNTIPIAFECYEDETDDQIADVATIKKTEKHPCSPIDTANRCETFDSLAADIEDDMLNLEDQDVVLSEDRPYGDVIDPAESEAEALAELGVEEWDSYPPIDPASRIGDDFNYVLRTEDFAEEGDVKLEETRHRTVIADIDEVKMSKAERNELFSMLADDLDSYDLLAEEANLPL","name":"Securin-like protein","regions":[{"region_id":"DP03049r003","unpublished":true,"ec_ontology":"ECO","end":244,"term_id":"IDPO:0000002","start":193,"version":2,"statement":[{"text":"Securin, which forms an extended structure that interacts mainly with the  periphery of separase, was well resolved around the substrate-binding site but less well defined elsewhere (Supplementary Fig. 2 and Table 1).","type":"Results"},{"text":"Table 1. Disordered regions. Securin 1-117, 193-244","type":"Table"}],"term_name":"disorder","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-5782-6573","released":"2022_03","term_ontology":"IDPO","curator_name":"Luciana Rodriguez Sawicki","reference_id":"28263324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5MZ6"}],"term_namespace":"Structural state","ec_id":"ECO:0006224","curator_id":"lrodriguez","reference_html":"Cryo-EM structure of a metazoan separase-securin complex at near-atomic resolution. <i> Boland A, Martin TG, Zhang Z, Yang J, Bai XC, Chang L, Scheres SH, Barford D. </i> Nat Struct Mol Biol, 2017","ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP03049r004","unpublished":true,"ec_ontology":"ECO","end":117,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"Securin, which forms an extended structure that interacts mainly with the  periphery of separase, was well resolved around the substrate-binding site but less well defined elsewhere (Supplementary Fig. 2 and Table 1).","type":"Results"},{"text":"The N-terminal 116 residues, including the APC/C degron  recognition and ubiquitination sites are unstructured (Fig. 1a).","type":"Results"},{"text":"Table 1. Disordered regions. Securin 1-117, 193-244","type":"Table"}],"term_name":"disorder","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-5782-6573","released":"2022_03","term_ontology":"IDPO","curator_name":"Luciana Rodriguez Sawicki","reference_id":"28263324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5MZ6"}],"term_namespace":"Structural state","ec_id":"ECO:0006224","curator_id":"lrodriguez","reference_html":"Cryo-EM structure of a metazoan separase-securin complex at near-atomic resolution. <i> Boland A, Martin TG, Zhang Z, Yang J, Bai XC, Chang L, Scheres SH, Barford D. </i> Nat Struct Mol Biol, 2017","ec_go":"IDA","disprot_namespace":"Structural state"},{"region_id":"DP03049r005","unpublished":true,"ec_ontology":"ECO","end":192,"term_id":"GO:0005515","start":118,"version":3,"statement":[{"text":"Securin, which forms an extended structure that interacts mainly with the  periphery of separase, was well resolved around the substrate-binding site but less well defined elsewhere (Supplementary Fig. 2 and Table 1).","type":"Results"},{"text":"Our structure shows that bound to separase, securin forms an  extended conformation interacting along the entire length of separase in an anti-parallel  orientation (Fig. 1b, c). ","type":"Results"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"G5ED39","partner_end":null}],"term_name":"protein binding","ec_name":"cryogenic electron microscopy evidence used in manual assertion","curator_orcid":"0000-0001-5782-6573","released":"2022_03","term_ontology":"GO","curator_name":"Luciana Rodriguez Sawicki","reference_id":"28263324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5MZ6"}],"term_namespace":"Molecular function","ec_id":"ECO:0006208","curator_id":"lrodriguez","reference_html":"Cryo-EM structure of a metazoan separase-securin complex at near-atomic resolution. <i> Boland A, Martin TG, Zhang Z, Yang J, Bai XC, Chang L, Scheres SH, Barford D. </i> Nat Struct Mol Biol, 2017","ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"region_id":"DP03049r006","unpublished":true,"ec_ontology":"ECO","end":192,"term_id":"IDPO:0000011","start":118,"version":2,"statement":[{"text":"Securin, which forms an extended structure that interacts mainly with the  periphery of separase, was well resolved around the substrate-binding site but less well defined elsewhere (Supplementary Fig. 2 and Table 1).","type":"Results"},{"text":"Our structure shows that bound to separase, securin forms an  extended conformation interacting along the entire length of separase in an anti-parallel  orientation (Fig. 1b, c). ","type":"Results"}],"term_name":"disorder to order","ec_name":"cryogenic electron microscopy evidence used in manual assertion","curator_orcid":"0000-0001-5782-6573","released":"2022_03","term_ontology":"IDPO","curator_name":"Luciana Rodriguez Sawicki","reference_id":"28263324","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5MZ6"}],"term_namespace":"Structural transition","ec_id":"ECO:0006208","curator_id":"lrodriguez","reference_html":"Cryo-EM structure of a metazoan separase-securin complex at near-atomic resolution. <i> Boland A, Martin TG, Zhang Z, Yang J, Bai XC, Chang L, Scheres SH, Barford D. </i> Nat Struct Mol Biol, 2017","ec_go":"IDA","disprot_namespace":"Structural transition"}],"released":"2021_12","length":244,"ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","disprot_id":"DP03049","date":"2020-12-11T14:03:24.077Z","regions_counter":6,"dataset":[],"UniParc":"UPI000007E1A1","uniref100":"UniRef100_Q18235","uniref90":"UniRef90_Q18235","uniref50":"UniRef50_Q18235","genes":[{"name":{"value":"ify-1","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"C27A2.3","url":"https://www.wormbase.org/db/seq/sequence?name=C27A2.3;class=Transcript"}}]},"orfNames":[{"value":"C27A2.3","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"C27A2.3","url":"https://www.wormbase.org/db/seq/sequence?name=C27A2.3;class=Transcript"}}]}]}],"alphafold_very_low_content":0.3442622950819672,"disorder_content":0.6926229508196722,"disprot_consensus":{"full":[{"start":1,"end":117,"type":"D"},{"start":118,"end":192,"type":"T"},{"start":193,"end":244,"type":"D"}],"Structural state":[{"start":1,"end":117,"type":"D"},{"start":193,"end":244,"type":"D"}],"Molecular function":[{"start":118,"end":192,"type":"F"}],"Structural transition":[{"start":118,"end":192,"type":"T"}]}},{"acc":"G5ED39","features":{"pfam":[{"id":"PF03568","name":"Separin, protease domain","start":728,"end":1081}],"gene3D":[]},"creator":"lrodriguez","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"sequence":"MKITNKSVDKQHIEKLDELRKNVSCTVIGFAEQTAELQQEISELFIAEFGVNGPIDMNSLSKLARITSYYASSEYFQGLAKYQRTACKMFITWQTLRKEAMECRSKDREIFASIPAKLCFFYFYNGELCRAVVCLLDYIDLSDDTLAKEAALRWLMFLGETELIEKKLKTWKMDKSSKDMFSATEFAMNYLKKSEYRVEMLEKLMKLRDKVKSDPTRSFSRYELASYVSWLCSTLSNVPVGSALRECEFPDRVSHIQEAALKSDSLVRNRIPGLASSQFDNSVNASIWPFLDGHQEDSNYYVHIGSTIAWHFEMRRECALVNVTTAQTRDSMSAMILNLRVALKSASFFRVLQTTNTLAYYSSIIEEAGSEKNAKLMRVSCVNLLSSNPIIVRCSTPKETGATSRAHTPMAGSSVSEKQNTMRPDLADLLGDLELLDEQSFHPITRSCVCNVCTIYPLHSSFAAEYMMSYAIHSDFSQLSIKHFNDEFARIRERGMSSQVLMHRDSSVRPRPNIIQNEIFGMCVIRWLTKKLDSKESADEDTMEIFNNALKIVRYLQQRTTDMILAVTQLGRQLEFPMECNYSWMRPTIRKPRVKATIDCAVDILRAVSPFGRRPKVEKLEKNLQPFDKERFEKVRLAMRNEMNHYGHILYREWRCRLFAYVGRTSRDPWEAAYAWAESTQIGARNAVQSRLEKCKRGLVTMSGHDRFKTCVQSMPDEMTLVQIAMADDKTIYLVKLHADRDPIIMPLAHYSQAVELMDKFTFLLDEDEMIAKYPGDITPEEFWKRRKIVDGRMMTFVDEVQKHFLGVAASLLMPSGQLGPKAAELAIKIHKLSKGGLLLGEAKEMVYQSKLMDAKSWEALILRFCEMRTTDEKFKSFLPLMHRNSVEVMNQDDSIVTEKKYTYLVICPHLSQFCWERLPIFDEYPYVGRQVSIHSTFSQLEAMKSQEKQIPLQIDVQNAYYILDPDNNLGETQKRMVEYINKFNWEGTVGSAPKSNEISAALSQRDAFFFIGHGSGSSVMPRSVLKQSTCNAISLLMGCGSVRTIPQALGFDGKTAILDYAMAKCPLIVGCLWTVTDGEIDRFLIRMIDDCFEDSKSLTGIDKLRQLSEAMHEARSKARLKYLTGAAVVMYGLPVVAKQTTPFVEKDQRNLPQTPKTSARTSMRMETVPKTPKQEFVTSKSVPMTPIFSNNENKSPSRARMPSRVLKTPRQVKTFQEEDDEAPKRSTTRQLKPLVAPPIPATPTTRTTRSSARTPSRSRNL","name":"Separin homolog sep-1","regions":[{"region_id":"DP03050r001","unpublished":true,"ec_ontology":"ECO","end":446,"term_id":"IDPO:0000002","start":391,"version":3,"statement":[{"text":"Table 1 shows that the region 391-446 based on the Cryo-EM experiments","type":"Curator statement"},{"text":"The αsolenoid domain accommodates two disordered insertions. Insert-1 includes the site of\nregulatory CDK-phosphorylation of human separase 17,28, whereas insert-2 incorporates\nthe auto-cleavage sites 2,29,30 and cyclin B1 (refs 15,18) and PP2A 31 binding sites of\nvertebrate separase (Fig. 1 and Supplementary Fig. 4).","type":"Results"}],"term_name":"disorder","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-5782-6573","released":"2024_06","term_ontology":"IDPO","curator_name":"Luciana Rodriguez Sawicki","reference_id":"28263324","date":"2024-01-29T15:36:46.002Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5MZ6"}],"term_namespace":"Structural state","ec_id":"ECO:0006224","curator_id":"lrodriguez","reference_html":"Cryo-EM structure of a metazoan separase-securin complex at near-atomic resolution. <i> Boland A, Martin TG, Zhang Z, Yang J, Bai XC, Chang L, Scheres SH, Barford D. </i> Nat Struct Mol Biol, 2017","ec_go":"IDA","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q18235"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:57:19.055Z"}},{"region_id":"DP03050r002","unpublished":true,"ec_ontology":"ECO","end":628,"term_id":"IDPO:0000002","start":590,"version":3,"statement":[{"text":"Table 1 shows that the region 590-628 based on the Cryo-EM experiments.","type":"Curator statement"},{"text":"The αsolenoid domain accommodates two disordered insertions. Insert-1 includes the site of\nregulatory CDK-phosphorylation of human separase 17,28, whereas insert-2 incorporates\nthe auto-cleavage sites 2,29,30 and cyclin B1 (refs 15,18) and PP2A 31 binding sites of\nvertebrate separase (Fig. 1 and Supplementary Fig. 4).","type":"Results"}],"term_name":"disorder","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-5782-6573","released":"2024_06","term_ontology":"IDPO","curator_name":"Luciana Rodriguez Sawicki","reference_id":"28263324","date":"2024-01-29T15:20:39.967Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5MZ6"}],"term_namespace":"Structural state","ec_id":"ECO:0006224","curator_id":"lrodriguez","reference_html":"Cryo-EM structure of a metazoan separase-securin complex at near-atomic resolution. <i> Boland A, Martin TG, Zhang Z, Yang J, Bai XC, Chang L, Scheres SH, Barford D. </i> Nat Struct Mol Biol, 2017","ec_go":"IDA","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q18235"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-01-29T15:29:35.747Z"}},{"region_id":"DP03050r003","unpublished":true,"ec_ontology":"ECO","end":10,"term_id":"IDPO:0000002","start":1,"version":3,"statement":[{"text":"Table 1 shows that the region 1-10 based on the Cryo-EM experiments","type":"Curator statement"}],"term_name":"disorder","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-5782-6573","released":"2024_06","term_ontology":"IDPO","curator_name":"Luciana Rodriguez Sawicki","reference_id":"28263324","date":"2024-01-29T14:45:49.046Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5MZ6"}],"term_namespace":"Structural state","ec_id":"ECO:0006224","curator_id":"lrodriguez","reference_html":"Cryo-EM structure of a metazoan separase-securin complex at near-atomic resolution. <i> Boland A, Martin TG, Zhang Z, Yang J, Bai XC, Chang L, Scheres SH, Barford D. </i> Nat Struct Mol Biol, 2017","ec_go":"IDA","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":" Q18235"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-01-29T15:29:36.575Z"}},{"region_id":"DP03050r004","unpublished":true,"ec_ontology":"ECO","end":1262,"term_id":"IDPO:0000002","start":1141,"version":3,"statement":[{"text":"Table 1 shows that the region  1141-1262 based on the Cryo-EM experiments. ","type":"Curator statement"},{"text":"Figure 1 A shows a scheme indicating region 1141-1262 as an IDR.","type":"Curator statement"}],"term_name":"disorder","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-5782-6573","released":"2024_06","term_ontology":"IDPO","curator_name":"Luciana Rodriguez Sawicki","reference_id":"28263324","date":"2024-01-29T14:39:48.272Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5MZ6"}],"term_namespace":"Structural state","ec_id":"ECO:0006224","curator_id":"lrodriguez","reference_html":"Cryo-EM structure of a metazoan separase-securin complex at near-atomic resolution. <i> Boland A, Martin TG, Zhang Z, Yang J, Bai XC, Chang L, Scheres SH, Barford D. </i> Nat Struct Mol Biol, 2017","ec_go":"IDA","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q18235"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-01-29T15:29:41.372Z"}}],"released":"2021_12","length":1262,"ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","disprot_id":"DP03050","date":"2020-12-11T14:37:02.555Z","regions_counter":4,"dataset":[],"UniParc":"UPI0000055FF8","uniref100":"UniRef100_G5ED39","uniref90":"UniRef90_G5ED39","uniref50":"UniRef50_G5ED39","genes":[{"name":{"value":"sep-1","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"Y47G6A.12","url":"https://www.wormbase.org/db/seq/sequence?name=Y47G6A.12;class=Transcript"}}]},"orfNames":[{"value":"Y47G6A.12","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"Y47G6A.12","url":"https://www.wormbase.org/db/seq/sequence?name=Y47G6A.12;class=Transcript"}}]}]}],"alphafold_very_low_content":0.16957210776545167,"disorder_content":0.17987321711568938,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"},{"start":391,"end":446,"type":"D"},{"start":590,"end":628,"type":"D"},{"start":1141,"end":1262,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":391,"end":446,"type":"D"},{"start":590,"end":628,"type":"D"},{"start":1141,"end":1262,"type":"D"}]}},{"acc":"O54952","features":{"pfam":[{"id":"PF00097","name":"Zinc finger, C3HC4 type (RING finger)","start":24,"end":64},{"id":"PF00533","name":"BRCA1 C Terminus (BRCT) domain","start":1592,"end":1669},{"id":"PF00533","name":"BRCA1 C Terminus (BRCT) domain","start":1702,"end":1787},{"id":"PF12820","name":"Serine-rich domain associated with BRCT","start":343,"end":504}],"gene3D":[]},"creator":"ashenoy","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"sequence":"MDLSAVRIQEVQNVLHAMQKILECPICLELIKEPVSTQCDHIFCKFCMLKLLNQKKGPSQCPLCKNEITKRSLQGSARFSQLVEELLKIIDAFELDTGMQCANGFSFSKKKNSSSELLNEDASIIQSVGYRNRVKKLQQIESGSATLKDSLSVQLSNLGIVRSMKKNRQTQPQNKSVYIALESDSSEERVNAPDGCSVRDQELFQIAPGGAGDEGKLNSAKKAACDFSEGIRNIEHHQCSDKDLNPTENHATERHPEKCPRISVANVHVEPCGTDARASSLQRGTRSLLFTEDRLDAEKAEFCDRSKQSGAAVSQQSRWADSKETCNGRPVPRTEGKADPNVDSLCGRKQWNHPKSLCPENSGATTDVPWITLNSSIQKVNEWFSRTGEMLTSDNASDRRPASNAEAAVVLEVSNEVDGCFSSSKKIDLVAPDPDNAVMCTSGRDFSKPVENIINDKIFGKTYQRKGSRPHLNHVTEIIGTFTTEPQIIQEQPFTNKLKRKRSTCLHPEDFIKKADLTVVQRISENLNQGTDQMEPNDQAMSITSNGQENRATGNDLQRGRNAHPIESLRKEPAFTAKAKSISNSISDLEVELNVHSSKAPKKNRLRRKSTRCVLPLEPISRNPSPPTCAELQIESCGSSEETKKNNSNQTPAGHIREPQLIEDTEPAADAKKNEPNEHIRKRSASDAFPEEKLMNKAGLLTSCSSPRKPQGPVNPSPERKGIEQLEMCQMPDNNKELGDLVLGGEPSGKPTEPSEESTSVSLVPDTDYDTQNSVSILEANTVRYARTGSVQCMTQFVASENPKELVHGSNNAGSGSECFKHPLRHELNHNQETIEMEDSELDTQYLQNTFQVSKRQSFALFSKLRSPQKDCTLVGARSVPSREPSPKVTSRGEQKERQGQEESEISHVQAVTVTVGLPVPCQEGKPGAVTMCADVSRLCPSSHYRSCENGLNTTDKSGISQNSHFRQSVSPLRSSIKTDNRKTLTEGRFEKHTERGMGNETAVQSTIHTISLNNRGDACLEASSGSVIEVHSTGENVQGQLDRNRGPKVNTVSLLDSTQPGVSKQSAPVSDKYLEIKQESKAVSADFSPCLFSDHLEKPMRSDKTFQVCSETPDDLLDDVEIQENASFGEGGITEKSAIFNGSVLRRESSRSPSPVTHASKSRSLHRGSRKLEFSEESDSTEDEDLPCFQHLLSRVSSTPELTRCSSVVTQRVPEKAKGTQAPRKSSISDCNNEVILGEASQEYQFSEDAKCSGSMFSSQHSAALGSPANALSQDPDFNPPSKQRRHQAENEEAFLSDKELISDHEDMAACLEEASDQEEDSIIPDSVASGYESEANLSEDCSQSDILTTQQRATMKDNLIKLQQEMAQLEAVLEQHGSQPSGHPPCLPADPCALEDLPDPEQNRSGTAILTSKNINENPVSQNPKRACDDKSQPQPPDGLPSGDKESGMRRPSPFKSPLTSSRCSARGHSRSLQNRNSTSQEELLQPAXLEKSCEPHNLTGRSCLPRQDLEGTPYPESGIRLVSSRDPDSESPKVSALVCTAPASTSALKISQGQVAGSCRSPAAGGADTAVVEIVSKIKPEVTSPKERAERDISMVVSGLTPKEVMIVQKFAEKYRLALTDVITEETTHVIIKTDAEFVCERTLKYFLGIAGGKWIVSYSWVIKSIQERKLLSVHEFEVKGDVVTGSNHQGPRRSRESQEKLFEGLQIYCCEPFTNMPKDELERMLQLCGASVVKELPLLTRDTGAHPIVLVQPSAWTEDNDCPDIGQLCKGRLVMWDWVLDSISVYRCRDLDAYLVQNITCGRDGSEPQDSND","name":"Breast cancer type 1 susceptibility protein homolog","regions":[{"region_id":"DP03051r002","unpublished":true,"ec_ontology":"ECO","end":1817,"term_id":"IDPO:0000002","start":1801,"version":2,"statement":[{"text":"Five N-terminal residues (residues 1589–1593), a three-residue portion of the inter-repeat linker region (residues 1702–1704), and the C terminus (residues 1800–1817) do not have interpretable electron density, and we presume are disordered. ","type":"Methods"},{"text":"On matching missing residues in PDB structure 1L0B with Uniprot sequence, the disordered region starts at 1801 and not 1800. ","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-7748-2501","released":"2023_12","term_ontology":"IDPO","curator_name":"Aditi Shenoy","reference_id":"11877378","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1L0B"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"ashenoy","reference_html":"Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure. <i> Joo WS, Jeffrey PD, Cantor SB, Finnin MS, Livingston DM, Pavletich NP. </i> Genes Dev, 2002","validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-15T17:34:44.970Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2024_06","length":1817,"ncbi_taxon_id":10116,"organism":"Rattus norvegicus","disprot_id":"DP03051","date":"2020-12-11T16:42:05.541Z","regions_counter":2,"dataset":[],"UniParc":"UPI00000E8761","uniref100":"UniRef100_O54952","uniref90":"UniRef90_O54952","uniref50":"UniRef50_P48754","genes":[{"name":{"value":"Brca1"}}],"disorder_content":0.009356081452944413,"disprot_consensus":{"full":[{"start":1801,"end":1817,"type":"D"}],"Structural state":[{"start":1801,"end":1817,"type":"D"}]}},{"acc":"Q06486","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":9,"end":226}],"gene3D":[]},"creator":"ashenoy","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"sequence":"MELRVGNRYRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKHPQLHIESKIYKMMQGGVGIPTIRWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFATYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGASRAADDAERERRDREERLRHSRNPATRGLPSTASGRLRGTQEVAPPTPLTPTSHTANTSPRPVSGMERERKVSMRLHRGAPVNVSSSDLTGRQDTSRMSTSQIPGRVASSGLQSVVHR","name":"Casein kinase I isoform delta","regions":[{"region_id":"DP03052r001","unpublished":true,"ec_ontology":"ECO","end":314,"term_id":"IDPO:0000002","start":297,"version":2,"statement":[{"text":"The last 18 residues at the C terminus were disorderedin  both  molecules.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-7748-2501","released":"2022_03","term_ontology":"IDPO","curator_name":"Aditi Shenoy","reference_id":"8648628","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1CKJ"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"ashenoy","reference_html":"Three-dimensional structure of mammalian casein kinase I: molecular basis for phosphate recognition. <i> Longenecker KL, Roach PJ, Hurley TD. </i> J Mol Biol, 1996","ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_12","length":415,"ncbi_taxon_id":10116,"organism":"Rattus norvegicus","disprot_id":"DP03052","date":"2020-12-11T17:30:58.864Z","regions_counter":1,"dataset":[],"UniParc":"UPI000012DC66","uniref100":"UniRef100_Q9DC28","uniref90":"UniRef90_P48730","uniref50":"UniRef50_P48730","genes":[{"name":{"value":"Csnk1d"},"synonyms":[{"value":"Hckid"}]}],"alphafold_very_low_content":0.22650602409638554,"disorder_content":0.043373493975903614,"disprot_consensus":{"full":[{"start":297,"end":314,"type":"D"}],"Structural state":[{"start":297,"end":314,"type":"D"}]}},{"acc":"P91870","features":{"pfam":[{"id":"PF22073","name":"Cep192 domain 4","start":475,"end":576}],"gene3D":[]},"creator":"lrodriguez","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"sequence":"MEDDAPMNLCNEQFEEIEDSPIDDNDNESFYNADGDVELEEEEVHETPKNFKNGGRFKTNMTNPKVNDLTTIEEKNEDLRSAASSRSASRPASVMSDKSFSSQFEFQSGGENAIEEYTNQVFADENKADLLFPETSKFMNGASPPKDKHHSWEPSIHHYDKQPPPDIQTNSPVFGNLNHRKNKLIPQARAKPGANDNEIVERDNDENVPTTSDKSAFITSPMNSTNHDEKTSTPKRPTNRKIGQYQGPNFDLSSIYVGSPQHQNTSISTGQQMPTSSYSHAHSETMMTNQTINESMVRRVLNGNNKNQDLFAALEEARKRRAAQPSKPDFRINTTRTRVPIKPTSARHSGNVVSSTSNDNTTAASSKDLTTSRKAMETFRQNASMADATNSNTASMTSILSTISTARTDISRSSRNHGGGFSNTSVSTVIPANNGNVSLSHGRDGRDSVSSVRTMSRASSTSTVYAGSTFSGVSKPLRIHAKRVAFGCVAVGETLRVEVEVENISDRQCLVRASTDSTTPVYQILDNKLTMVDPKKSIKFQVSFSPSSVGRYQVIMSIEVPAQNFIHKIPMWGNGGIAKFVPTSPDLQQTINQSEYAMCTSCAKRISFKISNSAGTRDGFAMIKVFDSAMRQLPDGCVAFFPAPGFIVKKKSDKRVDIRIDSSYIDLHDENNFRTSSSLSTASTTSSFQRRILPGAKFFVHVVWGEETMRTRLRLLEVRTGQHQLIDGHDFTSFQFSDEEVLRAVPVGFPAIKPEDRDLFAASYRSFFINFFTSTTEFRAATSRKKKEICSNDDSTLLETTAFRNQTFVNDVTIVPNTRFSNRK","name":"Spindle-defective protein 2","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":44,"term_name":"disorder","reference_html":"Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. <i> Shimanovskaya E, Viscardi V, Lesigang J, Lettman MM, Qiao R, Svergun DI, Round A, Oegema K, Dong G. </i> Structure, 2014","start":11,"region_id":"DP03054r001","term_id":"IDPO:0000002","unpublished":true,"version":2,"curator_id":"lrodriguez","released":"2023_12","term_ontology":"IDPO","curator_name":"Luciana Rodriguez Sawicki","ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"Far-UV circular dichroism and nuclear magnetic resonance confirmed that the CeSPD-2 AR is intrinsically disordered with a classical random-coil structure (Figure S2CE).","type":"Results"},{"text":"Far-UV circular dichroism (CD) spectra of recombinant acidic regions: CeSPD-2 (aa 11-44), DmAsl (aa 21-60), MmAsl (aa 1-47), and MmSPD-2 (aa 168-256). All acidic regions demonstrated a classical random coil structure with maximum below 0 and minimum at ~200 nm.","type":"Supplementary material"}],"curator_orcid":"0000-0001-5782-6573","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","reference_id":"24980795","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-30T10:31:03.789Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":46,"term_name":"disorder","reference_html":"Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. <i> Shimanovskaya E, Viscardi V, Lesigang J, Lettman MM, Qiao R, Svergun DI, Round A, Oegema K, Dong G. </i> Structure, 2014","start":1,"region_id":"DP03054r002","term_id":"IDPO:0000002","unpublished":true,"version":2,"curator_id":"lrodriguez","released":"2023_12","term_ontology":"IDPO","curator_name":"Luciana Rodriguez Sawicki","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Far-UV circular dichroism and nuclear magnetic resonance confirmed that the CeSPD-2 AR is intrinsically disordered with a classical random-coil structure (Figure S2CE).","type":"Results"},{"text":"2D 1H-15N HSQC spectrum of the CeSPD-2 AR (aa 1-46) shows a very narrow chemical shift range of amide proton resonances (8.0 - 8.6 ppm), suggesting that the protein is either intrinsically disordered or composed of helical secondary structures.","type":"Supplementary material"},{"text":"Amide region of the 2D NOESY spectrum of the CeSPD-2 AR (aa 1-46) shows no helical HN-HN cross peaks (dashed-line encircled regions), suggesting that the protein does not have any helical content.","type":"Supplementary material"}],"curator_orcid":"0000-0001-5782-6573","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","reference_id":"24980795","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-30T10:31:03.191Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP03054r003","unpublished":true,"ec_ontology":"ECO","end":46,"term_id":"GO:0005515","start":1,"version":3,"statement":[{"text":"To find out whether the ZYG-1 CPB interacts with all or part of the CeSPD-2 acidic region (CeSPD-2 AR), we generated maltose binding protein (MBP)-tagged WT CeSPD-2 (aa 1-46) and three mutant versions (LEFT, CENTER and RIGHT; Figure 2C) that charge reversed negatively charged residues in the center or in the left or right flanking sides of the CeSPD-2 AR. All three mutants pulled down significantly less ZYG-1 CPB than the WT AR, suggesting that negatively charged residues across the entire CeSPD-2 AR interact with the ZYG-1 CPB (Figures 2D, S3A).","type":"Results"},{"text":"Interestingly, the CeSPD-2 AR has distal acidic patches on both sides (Figure 7E, F) that are functionally important in vitro and in vivo (Figures 2C, 2D, 3) and basic residues on the sides of the ZYG-1 CPB dimer are also important for SPD-2 AR binding, ZYG-1 targeting, and daughter centriole assembly (Figures 2E, 2F, 4).","type":"Discussion"}],"interaction_partner":[{"partner_start":null,"db":"UniProt","id":"Q9GT24","partner_end":null}],"term_name":"protein binding","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","curator_orcid":"0000-0001-5782-6573","released":"2023_12","term_ontology":"GO","curator_name":"Luciana Rodriguez Sawicki","reference_id":"24980795","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_namespace":"Molecular function","ec_id":"ECO:0006077","curator_id":"lrodriguez","reference_html":"Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. <i> Shimanovskaya E, Viscardi V, Lesigang J, Lettman MM, Qiao R, Svergun DI, Round A, Oegema K, Dong G. </i> Structure, 2014","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-30T10:31:01.842Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":11,"end":44,"reference_id":"24980795","reference_source":"pmid","reference_html":"Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. <i> Shimanovskaya E, Viscardi V, Lesigang J, Lettman MM, Qiao R, Svergun DI, Round A, Oegema K, Dong G. </i> Structure, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006303","ec_ontology":"ECO","ec_name":"microscale thermophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"interaction_partner":[{"db":"UniProt","id":"Q9GT24","partner_start":null,"partner_end":null}],"region_id":"DP03054r004","statement":[{"text":"Microscale thermophoresis (MST; Seidel et al., 2013) using fluorescently labeled ZYG-1 CPB as reporter revealed that thioredoxin fusions with three CeSPD-2 N-terminal fragments (aa 1-147, 1-46 and 11-44) bound with nearly identical affinities (Kd ~ 0.5 μM; Figure 2B), indicating that residues 11-44 of CeSPD-2 are sufficient for interaction.","type":"Results"},{"text":"Interestingly, the CeSPD-2 AR has distal acidic patches on both sides (Figure 7E, F) that are functionally important in vitro and in vivo (Figures 2C, 2D, 3) and basic residues on the sides of the ZYG-1 CPB dimer are also important for SPD-2 AR binding, ZYG-1 targeting, and daughter centriole assembly (Figures 2E, 2F, 4).","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-30T10:30:58.109Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":46,"reference_id":"24980795","reference_source":"pmid","reference_html":"Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. <i> Shimanovskaya E, Viscardi V, Lesigang J, Lettman MM, Qiao R, Svergun DI, Round A, Oegema K, Dong G. </i> Structure, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0005589","ec_ontology":"ECO","ec_name":"confocal microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03054r005","statement":[{"text":"A distributed array of negatively charged residues in the CeSPD-2 N-terminus recruits ZYG-1 to mother centrioles to initiate centriole duplication in vivo.","type":"Results"},{"text":"Interestingly, the CeSPD-2 AR has distal acidic patches on both sides (Figure 7E, F) that are functionally important in vitro and in vivo (Figures 2C, 2D, 3) and basic residues on the sides of the ZYG-1 CPB dimer are also important for SPD-2 AR binding, ZYG-1 targeting, and daughter centriole assembly (Figures 2E, 2F, 4).","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-30T10:30:58.861Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":46,"reference_id":"24980795","reference_source":"pmid","reference_html":"Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. <i> Shimanovskaya E, Viscardi V, Lesigang J, Lettman MM, Qiao R, Svergun DI, Round A, Oegema K, Dong G. </i> Structure, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03054r006","statement":[{"text":"We conclude that an array of negatively charged residues in the CeSPD-2 N-terminus recruits ZYG-1 to mother centrioles; selective alteration of charges in the beginning, middle or end of this region disrupts ZYG-1 docking and centriole duplication.","type":"Results"},{"text":"Graph plotting mean centrosomal ZYG-1 fluorescence. Values are percentage of the mean control value. n = number of centrosomes.","type":"Figure"},{"text":"Interestingly, the CeSPD-2 AR has distal acidic patches on both sides (Figure 7E, F) that are functionally important in vitro and in vivo (Figures 2C, 2D, 3) and basic residues on the sides of the ZYG-1 CPB dimer are also important for SPD-2 AR binding, ZYG-1 targeting, and daughter centriole assembly (Figures 2E, 2F, 4).","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-30T10:31:00.392Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2023_12","length":824,"ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","disprot_id":"DP03054","date":"2020-12-11T19:54:34.155Z","regions_counter":6,"dataset":[],"UniParc":"UPI0000080414","uniref100":"UniRef100_P91870","uniref90":"UniRef90_P91870","uniref50":"UniRef50_P91870","genes":[{"name":{"value":"spd-2","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"F32H2.3","url":"https://www.wormbase.org/db/seq/sequence?name=F32H2.3;class=Transcript"}}]},"orfNames":[{"value":"F32H2.3","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"F32H2.3","url":"https://www.wormbase.org/db/seq/sequence?name=F32H2.3;class=Transcript"}}]}]}],"alphafold_very_low_content":0.5461165048543689,"disorder_content":0.055825242718446605,"disprot_consensus":{"full":[{"start":1,"end":46,"type":"D"}],"Structural state":[{"start":1,"end":46,"type":"D"}],"Molecular function":[{"start":1,"end":46,"type":"F"}],"Biological process":[{"start":1,"end":46,"type":"F"}]}},{"acc":"P13199","features":{"pfam":[{"id":"PF05459","name":"Herpesvirus transcriptional regulator family","start":198,"end":415}],"gene3D":[]},"creator":"eschad","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Peploviricota","Herviviricetes","Herpesvirales","Herpesviridae","Gammaherpesvirinae","Rhadinovirus"],"sequence":"MEDIIEGGISSDDDFDSSDSSSDEEESDTSPQIMKSDVTMASPPSTPEPSPDVSASTSNLKRERQRSPITWEHQSPLSRVYRSPSPMRFGKRPRISSNSTSRSCKTSWADRVREAAAQRRPSRPFRKPYSHPRNGPLRNGPPRAPPLLKLFDISILPKSGEPKLFLPVPSLPCQEAEKTNDKYVLAMAQRAMHDVPISSKQLTANLLPVKFKPLLSIVRYTPNYYYWVSMRKETIASANLCTVAAFLDESLCWGQQYLKNDFIFSENGKDIILDTSSALLSQLVHKIKMLPFCHCLMQTTPQDHIVKQVCYLIASNNRILDAVRYLQTSVIKSPIVLLLAYAVCLPAAIICTKNETQLYSHCMRILKEYRPGDVMNILHESLTQHLNKCPSSTCAYTTRAIVGTKANTTGLFFLPTQ","name":"mRNA export factor ICP27 homolog","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":107,"term_name":"disorder","reference_html":"Competitive and cooperative interactions mediate RNA transfer from herpesvirus saimiri ORF57 to the mammalian export adaptor ALYREF. <i> Tunnicliffe RB, Hautbergue GM, Wilson SA, Kalra P, Golovanov AP. </i> PLoS Pathog, 2014","start":8,"region_id":"DP03056r001","term_id":"IDPO:0000002","unpublished":true,"version":2,"curator_id":"eschad","released":"2022_03","term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"In its free form the Nterminal region aa8–120 of ORF57 is flexible and mainly\nunstructured, apart from the short a-helix aa108–118 which we\nnamed R-b helix.","type":"Results"},{"text":"Our experimental NMR data,\nnamely dihedral angles derived from TALOS+ [42], 15N[1\nH] NOE\nexperiments, and presence of characteristic i to i+3 NOEs for a\nshorter peptide ORF57103–120 (see Fig. S2), also all demonstrate that\nthe ORF578–120 site aa107–118 exists in a-helical conformation;\ntherefore this region was named ‘‘R-b helix’’.","type":"Results"}],"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","reference_id":"24550725","ec_go":"EXP","disprot_namespace":"Structural state"},{"start":64,"end":107,"reference_id":"24550725","reference_source":"pmid","reference_html":"Competitive and cooperative interactions mediate RNA transfer from herpesvirus saimiri ORF57 to the mammalian export adaptor ALYREF. <i> Tunnicliffe RB, Hautbergue GM, Wilson SA, Kalra P, Golovanov AP. </i> PLoS Pathog, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03056r002","statement":[{"text":"In contrast, the ORF57-specific oligos caused substantial signal broadening in\nall signals corresponding to the region aa64–120 (Fig. 1A).","type":"Results"},{"text":"Signal perturbation mapping therefore suggested a specific\nRNA binding site encompassing aa64–120 within ORF578–120,\nwhilst also showing the ALYREF-binding region aa103–120\nlocated within this site is not sufficient for the recognition of\nspecific viral RNA.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":64,"end":79,"reference_id":"24550725","reference_source":"pmid","reference_html":"Competitive and cooperative interactions mediate RNA transfer from herpesvirus saimiri ORF57 to the mammalian export adaptor ALYREF. <i> Tunnicliffe RB, Hautbergue GM, Wilson SA, Kalra P, Golovanov AP. </i> PLoS Pathog, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03056r003","statement":[{"text":"Based on the results of saturation transfer\nmapping, which are also in line with signal perturbation mapping,\nwe conclude that ORF578–120 contacts the specific RNA motifs\ndirectly using primarily its regions aa107–120 and aa81–92, with\nadditional contribution from residues within aa94–105 and aa64–\n79.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":81,"end":92,"reference_id":"24550725","reference_source":"pmid","reference_html":"Competitive and cooperative interactions mediate RNA transfer from herpesvirus saimiri ORF57 to the mammalian export adaptor ALYREF. <i> Tunnicliffe RB, Hautbergue GM, Wilson SA, Kalra P, Golovanov AP. </i> PLoS Pathog, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03056r004","statement":[{"text":"Based on the results of saturation transfer\nmapping, which are also in line with signal perturbation mapping,\nwe conclude that ORF578–120 contacts the specific RNA motifs\ndirectly using primarily its regions aa107–120 and aa81–92, with\nadditional contribution from residues within aa94–105 and aa64–\n79.","type":"Results"},{"text":"In the ternary complex\nORF57 aa106–120 directly interacts with the ALYREF RRM,\nwhereas flexible flanking regions of ALYREF (aa24–48) and\nORF57 (aa81–92), and to lesser extent, parts of helix 2 of the\nALYREF RRM, jointly keep hold of the viral RNA molecule.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":94,"end":105,"reference_id":"24550725","reference_source":"pmid","reference_html":"Competitive and cooperative interactions mediate RNA transfer from herpesvirus saimiri ORF57 to the mammalian export adaptor ALYREF. <i> Tunnicliffe RB, Hautbergue GM, Wilson SA, Kalra P, Golovanov AP. </i> PLoS Pathog, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03056r005","statement":[{"text":"Based on the results of saturation transfer\nmapping, which are also in line with signal perturbation mapping,\nwe conclude that ORF578–120 contacts the specific RNA motifs\ndirectly using primarily its regions aa107–120 and aa81–92, with\nadditional contribution from residues within aa94–105 and aa64–\n79.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":81,"end":89,"reference_id":"24550725","reference_source":"pmid","reference_html":"Competitive and cooperative interactions mediate RNA transfer from herpesvirus saimiri ORF57 to the mammalian export adaptor ALYREF. <i> Tunnicliffe RB, Hautbergue GM, Wilson SA, Kalra P, Golovanov AP. </i> PLoS Pathog, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03056r006","statement":[{"text":"The results of NMR mapping of RNA binding regions of\nORF578–120 were confirmed by UV cross-linking using purified\nprotein and radio-labeled RNA oligonucleotide, performed as\npreviously described [10]. The ORF57 mutants Y81A+R82A,\nR88A+F89A and W108A+R111A+V112A all significantly reduced the efficiency of cross-linking with RNA 14merS (Fig. 7A).","type":"Results"}],"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":8,"end":107,"reference_id":"24550725","reference_source":"pmid","reference_html":"Competitive and cooperative interactions mediate RNA transfer from herpesvirus saimiri ORF57 to the mammalian export adaptor ALYREF. <i> Tunnicliffe RB, Hautbergue GM, Wilson SA, Kalra P, Golovanov AP. </i> PLoS Pathog, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001170","ec_ontology":"ECO","ec_name":"cross-linking evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03056r007","statement":[{"text":"To independently confirm the NMR observations in regard to\nRNA oligonucleotide binding with ORF578–120, ALYREF1–155\nand their complex, we performed in vitro reconstitution assays\nfollowed by UV cross-linking experiments. ORF578–120 showed a\nstrong RNA-binding activity for 7merS and 14merS in sharp\ncontrast to GST-ALYREF which bound weakly with both RNAs\n(Fig. 7B,C). When ORF578–120 was incubated with RNA prior to\nmixing with GST-ALYREF, followed by GST affinity purification\nof the resulting complexes and UV cross-linking, there was a\ndrastic reduction of the RNA cross-linked to ORF578–120 and a\nconcomitant increase in the RNA cross-linked onto GSTALYREF. Therefore the RNA-binding activity of ORF578–120 is\nseverely reduced upon interaction with ALYREF, whereas the\namount of RNA in contact with ALYREF increases in the ternary\ncomplex. This independent data obtained at a molecular (i.e,\nmacroscopic) level concurs fully with the NMR data obtained at a\nresidue-specific level of detail. ","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":81,"end":92,"reference_id":"24550725","reference_source":"pmid","reference_html":"Competitive and cooperative interactions mediate RNA transfer from herpesvirus saimiri ORF57 to the mammalian export adaptor ALYREF. <i> Tunnicliffe RB, Hautbergue GM, Wilson SA, Kalra P, Golovanov AP. </i> PLoS Pathog, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03056r008","statement":[{"text":"In this study we used solution state NMR to reveal molecular\ndetails of the ternary complex assembly of functional fragments of\nHVS ORF57, HVS RNA and ALYREF, and suggest a model for\nthe mechanism of RNA transfer between protein molecules in this\nsystem.","type":"Introduction"},{"text":"The NMR experiments therefore all indicate that ALYREF\npartially displaces the viral RNA initially bound specifically to\nORF57, but retains it within the complex. In the ternary complex\nORF57 aa106–120 directly interacts with the ALYREF RRM,\nwhereas flexible flanking regions of ALYREF (aa24–48) and\nORF57 (aa81–92), and to lesser extent, parts of helix 2 of the\nALYREF RRM, jointly keep hold of the viral RNA molecule.\nInterestingly, amide signals from flexible protein regions which\nbecome involved in direct contacts with RNA (as evidenced by\nRNA-protein saturation transfer), are only partially broadened in\nthe complex. They had intensities higher than signals from the\nfolded regions, but lower than signals from the unfolded noninteracting regions (examples of this behavior can be seen in Fig. 5\nand Fig. S5). This suggests that the interaction with RNA in these\nconditions was somewhat transient and did not lead to the\nformation of a rigid 3D structure.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":8,"end":107,"reference_id":"24550725","reference_source":"pmid","reference_html":"Competitive and cooperative interactions mediate RNA transfer from herpesvirus saimiri ORF57 to the mammalian export adaptor ALYREF. <i> Tunnicliffe RB, Hautbergue GM, Wilson SA, Kalra P, Golovanov AP. </i> PLoS Pathog, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03056r009","statement":[{"text":"The experimental fluorescence equilibrium binding data thus\nreveal the overall cooperativity in the ternary complex formation\nwhen the components are present at or near stoichiometric\namounts, and support a role of ORF57 as an adaptor introducing\nRNA to ALYREF.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":8,"end":107,"reference_id":"24550725","reference_source":"pmid","reference_html":"Competitive and cooperative interactions mediate RNA transfer from herpesvirus saimiri ORF57 to the mammalian export adaptor ALYREF. <i> Tunnicliffe RB, Hautbergue GM, Wilson SA, Kalra P, Golovanov AP. </i> PLoS Pathog, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001170","ec_ontology":"ECO","ec_name":"cross-linking evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03056r010","statement":[{"text":"To independently confirm the NMR observations in regard to\nRNA oligonucleotide binding with ORF578–120, ALYREF1–155\nand their complex, we performed in vitro reconstitution assays\nfollowed by UV cross-linking experiments. ORF578–120 showed a\nstrong RNA-binding activity for 7merS and 14merS in sharp\ncontrast to GST-ALYREF which bound weakly with both RNAs\n(Fig. 7B,C). When ORF578–120 was incubated with RNA prior to\nmixing with GST-ALYREF, followed by GST affinity purification\nof the resulting complexes and UV cross-linking, there was a\ndrastic reduction of the RNA cross-linked to ORF578–120 and a\nconcomitant increase in the RNA cross-linked onto GSTALYREF. Therefore the RNA-binding activity of ORF578–120 is\nseverely reduced upon interaction with ALYREF, whereas the\namount of RNA in contact with ALYREF increases in the ternary\ncomplex.","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":8,"end":107,"reference_id":"24550725","reference_source":"pmid","reference_html":"Competitive and cooperative interactions mediate RNA transfer from herpesvirus saimiri ORF57 to the mammalian export adaptor ALYREF. <i> Tunnicliffe RB, Hautbergue GM, Wilson SA, Kalra P, Golovanov AP. </i> PLoS Pathog, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03056r011","statement":[{"text":"As the measured Kd values\nfor the formation of binary complexes are significantly higher than\nfor the ternary complexes (e.g., Kd\nO+R= 7.57 mM.\nKd\nOA+R= 1.55 mM), the assembly shows clear-cut cooperative behavior [44].","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2021_12","length":417,"ncbi_taxon_id":10383,"organism":"Saimiriine herpesvirus 2 (strain 11)","disprot_id":"DP03056","date":"2020-12-14T16:15:36.333Z","regions_counter":11,"dataset":["Viral proteins"],"UniParc":"UPI000012D21D","uniref100":"UniRef100_P13199","uniref90":"UniRef90_P13199","uniref50":"UniRef50_P13199","genes":[{"name":{"value":"EJRF1"},"orfNames":[{"value":"ORF57"}]}],"disorder_content":0.23980815347721823,"disprot_consensus":{"full":[{"start":8,"end":107,"type":"D"}],"Structural state":[{"start":8,"end":107,"type":"D"}],"Molecular function":[{"start":8,"end":107,"type":"F"}]}},{"acc":"Q20728","features":{"pfam":[{"id":"PF01302","name":"CAP-Gly domain","start":148,"end":215},{"id":"PF14560","name":"Ubiquitin-like domain","start":6,"end":85}],"gene3D":[]},"creator":"lrodriguez","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"sequence":"MTEVYDLEITTNATDFPMEKKYPAGMSLNDLKKKLELVVGTTVDSMRIQLFDGDDQLKGELTDGAKSLKDLGVRDGYRIHAVDVTGGNEDFKDESMVEKYEMSDDTYGKRTDSVRAWKKKMQEEQGSAAPMENESDKLNEEAAKNIMVGNRCEVTVGAQMARRGEVAYVGATKFKEGVWVGVKYDEPVGKNDGSVAGVRYFDCDPKYGGFVRPVDVKVGDFPELSIDEI","name":"Tubulin-specific chaperone B","regions":[{"region_id":"DP03057r001","unpublished":true,"ec_ontology":"ECO","end":120,"term_id":"IDPO:0000002","start":91,"version":2,"statement":[{"text":"Because no long range NOEs were observed for residues 91–120, and 15N-1H heteronuclear NOEvalues (Fig. 2A) confirmed that those C-terminal residues are dynamically disordered on the picosecond to nanosecond timescale (23), the final structure calculations included only CoB residues 1–90. ","type":"Results"},{"text":"Values for residues 91–120 (not shown) ranged from -0.4 to +0.2 consistent with an absence of defined tertiary structure beyond the extent of the β-grasp domain.","type":"Figure"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0001-5782-6573","released":"2022_03","term_ontology":"IDPO","curator_name":"Luciana Rodriguez Sawicki","reference_id":"15364906","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1T0Y"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"lrodriguez","reference_html":"Solution structure of a ubiquitin-like domain from tubulin-binding cofactor B. <i> Lytle BL, Peterson FC, Qiu SH, Luo M, Zhao Q, Markley JL, Volkman BF. </i> J Biol Chem, 2004","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-31T16:26:49.978Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP03057r002","unpublished":true,"ec_ontology":"ECO","end":120,"term_id":"IDPO:0000033","start":91,"version":3,"statement":[{"text":"Disordered C-terminal residues of the construct used in this analysis may serve as a flexible linker between the N-terminal Ubl domain and the C-terminal CAP-Gly domain (12) of CoB.","type":"Results"}],"term_name":"flexible linker","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0001-5782-6573","released":"2022_03","term_ontology":"IDPO","curator_name":"Luciana Rodriguez Sawicki","reference_id":"15364906","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1T0Y"}],"term_namespace":"Disorder function","ec_id":"ECO:0006165","curator_id":"lrodriguez","reference_html":"Solution structure of a ubiquitin-like domain from tubulin-binding cofactor B. <i> Lytle BL, Peterson FC, Qiu SH, Luo M, Zhao Q, Markley JL, Volkman BF. </i> J Biol Chem, 2004","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-30T12:49:12.655Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_12","length":229,"ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","disprot_id":"DP03057","date":"2020-12-14T22:30:44.439Z","regions_counter":3,"dataset":[],"UniParc":"UPI000013C244","uniref100":"UniRef100_Q20728","uniref90":"UniRef90_Q20728","uniref50":"UniRef50_Q20728","genes":[{"name":{"value":"tbcb-1","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"F53F4.3","url":"https://www.wormbase.org/db/seq/sequence?name=F53F4.3;class=Transcript"}}]},"orfNames":[{"value":"F53F4.3","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"F53F4.3","url":"https://www.wormbase.org/db/seq/sequence?name=F53F4.3;class=Transcript"}}]}]}],"alphafold_very_low_content":0.026200873362445413,"disorder_content":0.13100436681222707,"disprot_consensus":{"full":[{"start":91,"end":120,"type":"D"}],"Structural state":[{"start":91,"end":120,"type":"D"}],"Disorder function":[{"start":91,"end":120,"type":"F"}]}},{"acc":"Q58F21","features":{"pfam":[{"id":"PF00439","name":"Bromodomain","start":39,"end":120},{"id":"PF00439","name":"Bromodomain","start":276,"end":362},{"id":"PF17035","name":"Bromodomain extra-terminal - transcription regulation","start":509,"end":572},{"id":"PF17105","name":"C-terminal domain of bromodomain protein 4","start":905,"end":947}],"gene3D":[]},"creator":"eschad","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MSLPSRQTAIIVNPPPPEYINTKKNGRLTNQLQYLQKVVLKDLWKHSFSWPFQRPVDAVKLQLPDYYTIIKNPMDLNTIKKRLENKYYAKASECIEDFNTMFSNCYLYNKPGDDIVLMAQALEKLFMQKLSQMPQEEQVVGVKERIKKGTQQNIAVSSAKEKSSPSATEKVFKQQEIPSVFPKTSISPLNVVQGASVNSSSQTAAQVTKGVKRKADTTTPATSAVKASSEFSPTFTEKSVALPPIKENMPKNVLPDSQQQYNVVKTVKVTEQLRHCSEILKEMLAKKHFSYAWPFYNPVDVNALGLHNYYDVVKNPMDLGTIKEKMDNQEYKDAYKFAADVRLMFMNCYKYNPPDHEVVTMARMLQDVFETHFSKIPIEPVESMPLCYIKTDITETTGRENTNEASSEGNSSDDSEDERVKRLAKLQEQLKAVHQQLQVLSQVPFRKLNKKKEKSKKEKKKEKVNNSNENPRKMCEQMRLKEKSKRNQPKKRKQQFIGLKSEDEDNAKPMNYDEKRQLSLNINKLPGDKLGRVVHIIQSREPSLSNSNPDEIEIDFETLKASTLRELEKYVSACLRKRPLKPPAKKIMMSKEELHSQKKQELEKRLLDVNNQLNSRKRQTKSDKTQPSKAVENVSRLSESSSSSSSSSESESSSSDLSSSDSSDSESEMFPKFTEVKPNDSPSKENVKKMKNECIPPEGRTGVTQIGYCVQDTTSANTTLVHQTTPSHVMPPNHHQLAFNYQELEHLQTVKNISPLQILPPSGDSEQLSNGITVMHPSGDSDTTMLESECQAPVQKDIKIKNADSWKSLGKPVKPSGVMKSSDELFNQFRKAAIEKEVKARTQELIRKHLEQNTKELKASQENQRDLGNGLTVESFSNKIQNKCSGEEQKEHQQSSEAQDKSKLWLLKDRDLARQKEQERRRREAMVGTIDMTLQSDIMTMFENNFD","name":"Bromodomain testis-specific protein","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":257,"term_name":"disorder","reference_html":"A bromodomain-DNA interaction facilitates acetylation-dependent bivalent nucleosome recognition by the BET protein BRDT. <i> Miller TC, Simon B, Rybin V, Grötsch H, Curtet S, Khochbin S, Carlomagno T, Müller CW. </i> Nat Commun, 2016","start":144,"region_id":"DP03058r001","term_id":"IDPO:0000002","unpublished":true,"version":2,"curator_id":"eschad","released":"2023_12","term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":" New resonances, which appeared in the BRDT\n(1–2) 1H, 15N HSQC spectrum (Supplementary Fig. 3c), were\nattributed to the linker; these resonances were predominantly\ngrouped in the middle of the spectrum and have significantly higher intensities, suggesting that the linker is unstructured.","type":"Results"}],"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","reference_id":"27991587","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:40:07.445Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":257,"term_name":"disorder","reference_html":"A bromodomain-DNA interaction facilitates acetylation-dependent bivalent nucleosome recognition by the BET protein BRDT. <i> Miller TC, Simon B, Rybin V, Grötsch H, Curtet S, Khochbin S, Carlomagno T, Müller CW. </i> Nat Commun, 2016","start":144,"region_id":"DP03058r002","term_id":"IDPO:0000002","unpublished":true,"version":2,"curator_id":"eschad","released":"2023_12","term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"small-angle X-ray scattering evidence used in manual assertion","statement":[{"text":"The radius of gyration (Rg) = 49 +/- 9 Å and Dmax of > 160 Å derived from the\nSAXS data of BRDT(1-2) indicate a large average distance between the two bromodomains. In\nstructures with random linker conformations and a corresponding Rg, the distance between the\ncenter of mass of the two bromodomains is > 80 Å. The Kratky plot shows a clear bell-shaped\ncurve indicative of structured proteins; however, the curve increases asymptotically as expected\nfor a non-structured protein. Thus the data confirm the existence of an unstructured linker\nconnecting the two bromodomains.","type":"Supplementary material"}],"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","reference_id":"27991587","validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:40:06.645Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":209,"end":220,"reference_id":"22971749","reference_source":"pmid","reference_html":"The conserved 12-amino acid stretch in the inter-bromodomain region of BET family proteins functions as a nuclear localization signal. <i> Fukazawa H, Masumi A. </i> Biol Pharm Bull, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03058r005","statement":[{"text":"We identified a 12-amino acid stretch (KGVKRKADTTTP) in the inter-bromodomain region that is perfectly conserved among the BET family of proteins (Fig. 1). To investigate the function of this motif, we deleted the 12 residues and expressed the mutant proteins tagged with GFP in HEK293T cells.","type":"Article"},{"text":"In humans, the BET family consists of four members, BRD2, BRD3, BRD4 and BRDT, that all normally localize to the nucleus. We identified a 12-amino acid stretch in the inter-bromodomain region that is perfectly conserved among the BET family members. We deleted these residues and expressed the mutant proteins in HEK293T cells to investigate the function of this motif. We found that the deletion of this motif alters the localization of BET proteins.","type":"Abstract"},{"text":"Nevertheless, BET mutants lacking the reported nuclear localization signal motif but re-taining the 12-amino acid stretch resided in the nucleus. Furthermore, these mutants were diffused throughout the cytoplasm when the 12 residues were removed. These results indicate that the conserved amino acid stretch in the inter-bromodomain region of the BET family functions as a nuclear localization signal","type":"Abstract"},{"text":"In summary, we conclude that the conserved 12-amino acid sequence in the inter-bromodomain is at least part of the nuclear localization signal and plays important roles in the cytoplasmic/nuclear partitioning of the BET proteins.","type":"Discussion"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:40:10.917Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":209,"end":220,"reference_id":"22971749","reference_source":"pmid","reference_html":"The conserved 12-amino acid stretch in the inter-bromodomain region of BET family proteins functions as a nuclear localization signal. <i> Fukazawa H, Masumi A. </i> Biol Pharm Bull, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03058r006","statement":[{"text":"We identified a 12-amino acid stretch (KGVKRKADTTTP) in the inter-bromodomain region that is perfectly conserved among the BET family of proteins (Fig. 1). To investigate the function of this motif, we deleted the 12 residues and expressed the mutant proteins tagged with GFP in HEK293T cells.","type":"Article"},{"text":"In humans, the BET family consists of four members, BRD2, BRD3, BRD4 and BRDT, that all normally localize to the nucleus. We identified a 12-amino acid stretch in the inter-bromodomain region that is perfectly conserved among the BET family members. We deleted these residues and expressed the mutant proteins in HEK293T cells to investigate the function of this motif. We found that the deletion of this motif alters the localization of BET proteins.","type":"Abstract"},{"text":"Nevertheless, BET mutants lacking the reported nuclear localization signal motif but re-taining the 12-amino acid stretch resided in the nucleus. Furthermore, these mutants were diffused throughout the cytoplasm when the 12 residues were removed. These results indicate that the conserved amino acid stretch in the inter-bromodomain region of the BET family functions as a nuclear localization signal","type":"Abstract"},{"text":"In summary, we conclude that the conserved 12-amino acid sequence in the inter-bromodomain is at least part of the nuclear localization signal and plays important roles in the cytoplasmic/nuclear partitioning of the BET proteins.","type":"Discussion"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:40:10.168Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":583,"end":947,"reference_id":"17049203","reference_source":"pmid","reference_html":"Bromodomain testis-specific protein is expressed in mouse oocyte and evolves faster than its ubiquitously expressed paralogs BRD2, -3, and -4. <i> Paillisson A, Levasseur A, Gouret P, Callebaut I, Bontoux M, Pontarotti P, Monget P. </i> Genomics, 2007","date":"2022-11-17T16:59:05.896Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03058r007","statement":[{"text":"BRDT has a long C-terminal, largely unstructured extension of more than 300 residues after the ET domain, which might play a specific role in the function of this paralog.","type":"Introduction"}]}],"released":"2023_12","length":947,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP03058","date":"2020-12-15T13:56:18.232Z","regions_counter":7,"dataset":[],"UniParc":"UPI00004F6EC3","uniref100":"UniRef100_Q58F21","uniref90":"UniRef90_Q58F21","uniref50":"UniRef50_Q58F21","genes":[{"name":{"value":"BRDT"}}],"alphafold_very_low_content":0.48785638859556496,"disorder_content":0.5058078141499472,"disprot_consensus":{"full":[{"start":144,"end":257,"type":"D"},{"start":583,"end":947,"type":"D"}],"Structural state":[{"start":144,"end":257,"type":"D"},{"start":583,"end":947,"type":"D"}],"Biological process":[{"start":209,"end":220,"type":"F"}]}},{"acc":"Q15059","features":{"pfam":[{"id":"PF00439","name":"Bromodomain","start":46,"end":127},{"id":"PF00439","name":"Bromodomain","start":315,"end":402},{"id":"PF17035","name":"Bromodomain extra-terminal - transcription regulation","start":571,"end":635}],"gene3D":[]},"creator":"eschad","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MSTATTVAPAGIPATPGPVNPPPPEVSNPSKPGRKTNQLQYMQNVVVKTLWKHQFAWPFYQPVDAIKLNLPDYHKIIKNPMDMGTIKKRLENNYYWSASECMQDFNTMFTNCYIYNKPTDDIVLMAQALEKIFLQKVAQMPQEEVELLPPAPKGKGRKPAAGAQSAGTQQVAAVSSVSPATPFQSVPPTVSQTPVIAATPVPTITANVTSVPVPPAAAPPPPATPIVPVVPPTPPVVKKKGVKRKADTTTPTTSAITASRSESPPPLSDPKQAKVVARRESGGRPIKPPKKDLEDGEVPQHAGKKGKLSEHLRYCDSILREMLSKKHAAYAWPFYKPVDAEALELHDYHDIIKHPMDLSTVKRKMDGREYPDAQGFAADVRLMFSNCYKYNPPDHEVVAMARKLQDVFEMRFAKMPDEPVEAPALPAPAAPMVSKGAESSRSSEESSSDSGSSDSEEERATRLAELQEQLKAVHEQLAALSQAPVNKPKKKKEKKEKEKKKKDKEKEKEKHKVKAEEEKKAKVAPPAKQAQQKKAPAKKANSTTTAGRQLKKGGKQASASYDSEEEEEGLPMSYDEKRQLSLDINRLPGEKLGRVVHIIQSREPSLRDSNPDEIEIDFETLKPTTLRELERYVKSCLQKKQRKPFSASGKKQAAKSKEELAQEKKKELEKRLQDVSGQLSSSKKPARKEKPGSAPSGGPSRLSSSSSSESGSSSSSGSSSDSSDSE","name":"Bromodomain-containing protein 3","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":556,"term_name":"disorder","reference_html":"The BRD3 ET domain recognizes a short peptide motif through a mechanism that is conserved across chromatin remodelers and transcriptional regulators. <i> Wai DCC, Szyszka TN, Campbell AE, Kwong C, Wilkinson-White LE, Silva APG, Low JKK, Kwan AH, Gamsjaeger R, Chalmers JD, Patrick WM, Lu B, Vakoc CR, Blobel GA, Mackay JP. </i> J Biol Chem, 2018","start":429,"region_id":"DP03059r001","term_id":"IDPO:0000002","unpublished":true,"version":2,"curator_id":"eschad","released":"2022_03","term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Most of BRD3-L outside of the core ET domain appears to be disordered.","type":"Figure"},{"text":"15N HSQC spectra of BRD3-L and\nBRD3-ET are shown in Fig. 3A. The majority of peaks in the\nspectrum of BRD3-L (Fig. 3A, black) appear as intense, overlapping signals with amide proton shifts in the 8.0– 8.6 ppm region\nof the spectrum, a pattern characteristic of the disordered polypeptide. A number of weaker and more dispersed signals are\nalso observed. In contrast, peaks in the 15N HSQC of BRD3-ET\n(Fig. 3A, red) are well-dispersed, as expected of a small, folded\nprotein domain. An overlay of the two 15N HSQC spectra\nreveals that almost all signals in the BRD3-ET spectrum are\nessentially unchanged in the BRD3-L spectrum, indicating that\nthe folded ET domain takes up the same conformation in the\ncontext of the longer polypeptide.","type":"Results"}],"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","reference_id":"29567837","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-12-13T21:03:22.125Z"}},{"term_namespace":"Structural state","ec_ontology":"ECO","end":726,"term_name":"disorder","reference_html":"The BRD3 ET domain recognizes a short peptide motif through a mechanism that is conserved across chromatin remodelers and transcriptional regulators. <i> Wai DCC, Szyszka TN, Campbell AE, Kwong C, Wilkinson-White LE, Silva APG, Low JKK, Kwan AH, Gamsjaeger R, Chalmers JD, Patrick WM, Lu B, Vakoc CR, Blobel GA, Mackay JP. </i> J Biol Chem, 2018","start":645,"region_id":"DP03059r002","term_id":"IDPO:0000002","unpublished":true,"version":2,"curator_id":"eschad","released":"2022_03","term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"Most of BRD3-L outside of the core ET domain appears to be disordered.","type":"Figure"},{"text":"15N HSQC spectra of BRD3-L and\nBRD3-ET are shown in Fig. 3A. The majority of peaks in the\nspectrum of BRD3-L (Fig. 3A, black) appear as intense, overlapping signals with amide proton shifts in the 8.0– 8.6 ppm region\nof the spectrum, a pattern characteristic of the disordered polypeptide. A number of weaker and more dispersed signals are\nalso observed. In contrast, peaks in the 15N HSQC of BRD3-ET\n(Fig. 3A, red) are well-dispersed, as expected of a small, folded\nprotein domain. An overlay of the two 15N HSQC spectra\nreveals that almost all signals in the BRD3-ET spectrum are\nessentially unchanged in the BRD3-L spectrum, indicating that\nthe folded ET domain takes up the same conformation in the\ncontext of the longer polypeptide.","type":"Results"}],"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","reference_id":"29567837","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-24T17:11:24.739Z"}}],"released":"2021_12","length":726,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP03059","date":"2020-12-15T15:19:57.945Z","regions_counter":2,"dataset":["Cancer-related proteins","Condensates-related proteins","NDDs-related proteins"],"UniParc":"UPI0000126ACD","uniref100":"UniRef100_Q15059","uniref90":"UniRef90_Q15059","uniref50":"UniRef50_Q15059","genes":[{"name":{"value":"BRD3"},"synonyms":[{"value":"KIAA0043"},{"value":"RING3L"}]}],"alphafold_very_low_content":0.41735537190082644,"disorder_content":0.2892561983471074,"disprot_consensus":{"full":[{"start":429,"end":556,"type":"D"},{"start":645,"end":726,"type":"D"}],"Structural state":[{"start":429,"end":556,"type":"D"},{"start":645,"end":726,"type":"D"}]}},{"acc":"P60340","features":{"pfam":[{"id":"PF01509","name":"TruB family pseudouridylate synthase (N terminal domain)","start":33,"end":180},{"id":"PF09157","name":"Pseudouridine synthase II TruB, C-terminal","start":252,"end":309},{"id":"PF16198","name":"tRNA pseudouridylate synthase B C-terminal domain","start":181,"end":246}],"gene3D":[]},"creator":"eschad","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"sequence":"MSRPRRRGRDINGVLLLDKPQGMSSNDALQKVKRIYNANRAGHTGALDPLATGMLPICLGEATKFSQYLLDSDKRYRVIARLGQRTDTSDADGQIVEERPVTFSAEQLAAALDTFRGDIEQIPSMYSALKYQGKKLYEYARQGIEVPREARPITVYELLFIRHEGNELELEIHCSKGTYIRTIIDDLGEKLGCGAHVIYLRRLAVSKYPVERMVTLEHLRELVEQAEQQDIPAAELLDPLLMPMDSPASDYPVVNLPLTSSVYFKNGNPVRTSGAPLEGLVRVTEGENGKFIGMGEIDDEGRVAPRRLVVEYPA","name":"tRNA pseudouridine synthase B","regions":[{"region_id":"DP03060r001","unpublished":true,"ec_ontology":"ECO","end":152,"term_id":"IDPO:0000002","start":124,"version":2,"statement":[{"text":"  The overall fold of the apo\nstructure is similar to that of the E. coli TruB–RNA complex (14)\nbut with one striking difference: a 29-aa segment (residues 124–152) of the apoprotein corresponding to the thumb-loop\nregion is disordered in the crystals and was not observed in the\nelectron density map.","type":"Results"},{"text":"A 29-amino acid segment containing residues\n124–152 was not observed in the electron density.","type":"Methods"},{"text":" The most prominent\nchange is that a 29-aa segment (residues 124–152) of the protein\ncorresponding to the thumb-loop region, which is totally disordered in the apoprotein, becomes ordered on RNA binding. It\nis possible that the thumb loop is unstructured in the RNA-free\nstate, or it oscillates between free and bound forms, and the\nRNA binding shifts the equilibrium to the bound form.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0002-3006-2910","released":"2022_03","term_ontology":"IDPO","curator_name":"Eva Schad","reference_id":"14566049","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"1R3F"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"eschad","reference_html":"Structure of tRNA pseudouridine synthase TruB and its RNA complex: RNA recognition through a combination of rigid docking and induced fit. <i> Pan H, Agarwalla S, Moustakas DT, Finer-Moore J, Stroud RM. </i> Proc Natl Acad Sci U S A, 2003","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-31T17:45:18.551Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2021_12","length":314,"ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","disprot_id":"DP03060","date":"2020-12-16T13:58:50.755Z","regions_counter":2,"dataset":[],"UniParc":"UPI000013769B","uniref100":"UniRef100_P60342","uniref90":"UniRef90_P60342","uniref50":"UniRef50_P60342","genes":[{"name":{"value":"truB"},"synonyms":[{"value":"yhbA"}],"olnNames":[{"value":"b3166"},{"value":"JW3135"}]}],"alphafold_very_low_content":0.009554140127388535,"disorder_content":0.09235668789808917,"disprot_consensus":{"full":[{"start":124,"end":152,"type":"D"}],"Structural state":[{"start":124,"end":152,"type":"D"}]}},{"acc":"P54132","features":{"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":670,"end":839},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":882,"end":984},{"id":"PF00570","name":"HRDC domain","start":1217,"end":1281},{"id":"PF08072","name":"BDHCT (NUC031) domain","start":372,"end":412},{"id":"PF09382","name":"RQC domain","start":1072,"end":1195},{"id":"PF16124","name":"RecQ zinc-binding","start":995,"end":1067},{"id":"PF16202","name":"N-terminal region of Bloom syndrome protein","start":1,"end":368},{"id":"PF16204","name":"BDHCT-box associated domain on Bloom syndrome protein","start":425,"end":647}],"gene3D":[]},"creator":"ldobson","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MAAVPQNNLQEQLERHSARTLNNKLSLSKPKFSGFTFKKKTSSDNNVSVTNVSVAKTPVLRNKDVNVTEDFSFSEPLPNTTNQQRVKDFFKNAPAGQETQRGGSKSLLPDFLQTPKEVVCTTQNTPTVKKSRDTALKKLEFSSSPDSLSTINDWDDMDDFDTSETSKSFVTPPQSHFVRVSTAQKSKKGKRNFFKAQLYTTNTVKTDLPPPSSESEQIDLTEEQKDDSEWLSSDVICIDDGPIAEVHINEDAQESDSLKTHLEDERDNSEKKKNLEEAELHSTEKVPCIEFDDDDYDTDFVPPSPEEIISASSSSSKCLSTLKDLDTSDRKEDVLSTSKDLLSKPEKMSMQELNPETSTDCDARQISLQQQLIHVMEHICKLIDTIPDDKLKLLDCGNELLQQRNIRRKLLTEVDFNKSDASLLGSLWRYRPDSLDGPMEGDSCPTGNSMKELNFSHLPSNSVSPGDCLLTTTLGKTGFSATRKNLFERPLFNTHLQKSFVSSNWAETPRLGKKNESSYFPGNVLTSTAVKDQNKHTASINDLERETQPSYDIDNFDIDDFDDDDDWEDIMHNLAASKSSTAAYQPIKEGRPIKSVSERLSSAKTDCLPVSSTAQNINFSESIQNYTDKSAQNLASRNLKHERFQSLSFPHTKEMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATYLTGDKTDSEATNIYLQLSKKDPIIKLLYVTPEKICASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQDYKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPKKVAFDCLEWIRKHHPYDSGIIYCLSRRECDTMADTLQRDGLAALAYHAGLSDSARDEVQQKWINQDGCQVICATIAFGMGIDKPDVRFVIHASLPKSVEGYYQESGRAGRDGEISHCLLFYTYHDVTRLKRLIMMEKDGNHHTRETHFNNLYSMVHYCENITECRRIQLLAYFGENGFNPDFCKKHPDVSCDNCCKTKDYKTRDVTDDVKSIVRFVQEHSSSQGMRNIKHVGPSGRFTMNMLVDIFLGSKSAKIQSGIFGKGSAYSRHNAERLFKKLILDKILDEDLYINANDQAIAYVMLGNKAQTVLNGNLKVDFMETENSSSVKKQKALVAKVSQREEMVKKCLGELTEVCKSLGKVFGVHYFNIFNTVTLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVISVLQKYSEWTSPAEDSSPGISLSSSRGPGRSAAEELDEEIPVSSHYFASKTRNERKRKKMPASQRSKRRKTASSGSKAKGGSATCRKISSKTKSSSIIGSSSASHTSQATSGANSKLGIMAPPKPINRPFLKPSYAFS","name":"Bloom syndrome protein","regions":[{"region_id":"DP03061r001","unpublished":true,"ec_ontology":"ECO","end":1106,"term_id":"IDPO:0000002","start":1093,"version":2,"statement":[{"text":"The structure of the second molecule (Mol-B), which is illustrated in Figure 3b, is essentially the same except that the looping-out region (referred to as the BLM-insertion) is disordered.","type":"Results"},{"text":"Structure of Mol-A. Secondary-structure elements (five α-helices and two β-strands) are labeled. The BLM-insertion (a.a. 1093–1106) and C-term extended loop (a.a. 1183–1194) are colored red","type":"Figure"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-2765-3872","released":"2022_06","term_ontology":"IDPO","curator_name":"László Dobson","reference_id":"24257077","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"3WE2"},{"db":"PDB","id":"3WE3"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"ldobson","reference_html":"Structure of the RecQ C-terminal domain of human Bloom syndrome protein. <i> Kim SY, Hakoshima T, Kitano K. </i> Sci Rep, 2013","validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-18T12:13:09.437Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP03061r002","unpublished":true,"ec_ontology":"ECO","end":1110,"term_id":"IDPO:0000002","start":1091,"version":2,"statement":[{"text":"The long and flexible loop between α1 and α2 (α1–α2 loop, from H1091 to T1100), which has several missed N–H peaks in the 1H–15N HSQC (R1098, N1099, S1106 and G1107), is not well converged.","type":"Results"},{"text":"According to Fig2, PDB and UniProt sequence data, T1100 referred in the text has wrong numbering. The correct end boundary is the disordered regions is T1110.","type":"Curator statement"}],"term_name":"disorder","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","curator_orcid":"0000-0003-2765-3872","released":"2022_06","term_ontology":"IDPO","curator_name":"László Dobson","reference_id":"24435566","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"2MH9"}],"term_namespace":"Structural state","ec_id":"ECO:0006165","curator_id":"ldobson","reference_html":"Solution structure of the RecQ C-terminal domain of human Bloom syndrome protein. <i> Park CJ, Ko J, Ryu KS, Choi BS. </i> J Biomol NMR, 2014","validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-18T12:23:45.636Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP03061r003","unpublished":true,"ec_ontology":"ECO","end":1014,"term_id":"IDPO:0000002","start":1004,"version":2,"statement":[{"text":"All of the residues of BLM are present in the final model with the exception of the first three residues at the N-terminus and eight at the C-terminus, and two loops spanning residues 1004–1016 and 1093–1106 which are disordered.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-2765-3872","released":"2022_06","term_ontology":"IDPO","curator_name":"László Dobson","reference_id":"25901030","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4CDG"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"ldobson","reference_html":"Crystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changes. <i> Newman JA, Savitsky P, Allerston CK, Bizard AH, Özer Ö, Sarlós K, Liu Y, Pardon E, Steyaert J, Hickson ID, Gileadi O. </i> Nucleic Acids Res, 2015","validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-18T12:35:32.345Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"region_id":"DP03061r004","unpublished":true,"ec_ontology":"ECO","end":1107,"term_id":"IDPO:0000002","start":1092,"version":2,"statement":[{"text":"All of the residues of BLM are present in the final model with the exception of the first three residues at the N-terminus and eight at the C-terminus, and two loops spanning residues 1004–1016 and 1093–1106 which are disordered.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-2765-3872","released":"2022_06","term_ontology":"IDPO","curator_name":"László Dobson","reference_id":"25901030","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4CDG"},{"db":"PDB","id":"4CGZ"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"ldobson","reference_html":"Crystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changes. <i> Newman JA, Savitsky P, Allerston CK, Bizard AH, Özer Ö, Sarlós K, Liu Y, Pardon E, Steyaert J, Hickson ID, Gileadi O. </i> Nucleic Acids Res, 2015","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:09:42.019Z"}},{"start":1195,"end":1207,"reference_id":"24257077","reference_source":"pmid","reference_html":"Structure of the RecQ C-terminal domain of human Bloom syndrome protein. <i> Kim SY, Hakoshima T, Kitano K. </i> Sci Rep, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":2,"cross_refs":[{"db":"PDB","id":"3WE2"},{"db":"PDB","id":"3WE3"}],"region_id":"DP03061r007","statement":[{"text":"In the full-length protein, the C-term extended loop is followed by the 13 amino acids 1195SSSVKKQKALVAK1207, which tether the C-terminal HRDC domain (Figure 5d). Interestingly, this linker is considerably shorter than that of WRN (77 residues)","type":"Results"},{"text":"Missing atomic coordinates in the corresponding PDB files","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:08:18.008Z"}},{"start":1195,"end":1207,"reference_id":"24257077","reference_source":"pmid","reference_html":"Structure of the RecQ C-terminal domain of human Bloom syndrome protein. <i> Kim SY, Hakoshima T, Kitano K. </i> Sci Rep, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_06","version":3,"cross_refs":[{"db":"PDB","id":"3WE2"},{"db":"PDB","id":"3WE3"}],"region_id":"DP03061r008","statement":[{"text":"In the full-length protein, the C-term extended loop is followed by the 13 amino acids 1195SSSVKKQKALVAK1207, which tether the C-terminal HRDC domain (Figure 5d). Interestingly, this linker is considerably shorter than that of WRN (77 residues)","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T15:07:49.656Z"}}],"released":"2022_06","length":1417,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP03061","date":"2020-12-16T14:46:48.857Z","regions_counter":8,"dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI00001269FA","uniref100":"UniRef100_P54132","uniref90":"UniRef90_P54132","uniref50":"UniRef50_P54132","genes":[{"name":{"value":"BLM"},"synonyms":[{"value":"RECQ2"},{"value":"RECQL3"}]}],"alphafold_very_low_content":0.5137614678899083,"disorder_content":0.031051517290049402,"disprot_consensus":{"full":[{"start":1004,"end":1014,"type":"D"},{"start":1091,"end":1110,"type":"D"},{"start":1195,"end":1207,"type":"D"}],"Structural state":[{"start":1004,"end":1014,"type":"D"},{"start":1091,"end":1110,"type":"D"},{"start":1195,"end":1207,"type":"D"}],"Disorder function":[{"start":1195,"end":1207,"type":"F"}]}},{"acc":"P40692","features":{"pfam":[{"id":"PF01119","name":"DNA mismatch repair protein, C-terminal domain","start":216,"end":334},{"id":"PF13589","name":"Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase","start":29,"end":131},{"id":"PF16413","name":"DNA mismatch repair protein Mlh1 C-terminus","start":502,"end":756}],"gene3D":[]},"creator":"ldobson","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MSFVAGVIRRLDETVVNRIAAGEVIQRPANAIKEMIENCLDAKSTSIQVIVKEGGLKLIQIQDNGTGIRKEDLDIVCERFTTSKLQSFEDLASISTYGFRGEALASISHVAHVTITTKTADGKCAYRASYSDGKLKAPPKPCAGNQGTQITVEDLFYNIATRRKALKNPSEEYGKILEVVGRYSVHNAGISFSVKKQGETVADVRTLPNASTVDNIRSIFGNAVSRELIEIGCEDKTLAFKMNGYISNANYSVKKCIFLLFINHRLVESTSLRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQHIESKLLGSNSSRMYFTQTLLPGLAGPSGEMVKSTTSLTSSSTSGSSDKVYAHQMVRTDSREQKLDAFLQPLSKPLSSQPQAIVTEDKTDISSGRARQQDEEMLELPAPAEVAAKNQSLEGDTTKGTSEMSEKRGPTSSNPRKRHREDSDVEMVEDDSRKEMTAACTPRRRIINLTSVLSLQEEINEQGHEVLREMLHNHSFVGCVNPQWALAQHQTKLYLLNTTKLSEELFYQILIYDFANFGVLRLSEPAPLFDLAMLALDSPESGWTEEDGPKEGLAEYIVEFLKKKAEMLADYFSLEIDEEGNLIGLPLLIDNYVPPLEGLPIFILRLATEVNWDEEKECFESLSKECAMFYSIRKQYISEESTLSGQQSEVPGSIPNSWKWTVEHIVYKALRSHILPPKHFTEDGNILQLANLPDLYKVFERC","name":"DNA mismatch repair protein Mlh1","regions":[{"region_id":"DP03062r001","unpublished":true,"ec_ontology":"ECO","end":97,"term_id":"IDPO:0000002","start":86,"version":2,"statement":[{"text":"Accordingly, residues 86–97 have been omitted from our model owing to a lack of interpretable electron density.","type":"Results"},{"text":"The crystallographic model included amino-acid residues 3–85, 98–299 and 320–336. Atoms with little or no electron density were deemed to be disordered and were omitted from the final model.","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-2765-3872","released":"2022_03","term_ontology":"IDPO","curator_name":"László Dobson","reference_id":"26249686","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4P7A"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"ldobson","reference_html":"Structure of the human MLH1 N-terminus: implications for predisposition to Lynch syndrome. <i> Wu H, Zeng H, Lam R, Tempel W, Kerr ID, Min J. </i> Acta Crystallogr F Struct Biol Commun, 2015","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-24T16:54:56.030Z"}},{"region_id":"DP03062r002","unpublished":true,"ec_ontology":"ECO","end":319,"term_id":"IDPO:0000002","start":301,"version":2,"statement":[{"text":"Residues 301–320 in the hLN40 QTK loop are disordered; however, we can infer from MutL structures (Ban et al., 1999 ▸) that Lys311 within the PTK motif should act as the conserved basic, γ-phosphate-sensing residue","type":"Results"},{"text":"The crystallographic model included amino-acid residues 3–85, 98–299 and 320–336. Atoms with little or no electron density were deemed to be disordered and were omitted from the final model.","type":"Curator statement"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-2765-3872","released":"2022_03","term_ontology":"IDPO","curator_name":"László Dobson","reference_id":"26249686","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"4P7A"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"ldobson","reference_html":"Structure of the human MLH1 N-terminus: implications for predisposition to Lynch syndrome. <i> Wu H, Zeng H, Lam R, Tempel W, Kerr ID, Min J. </i> Acta Crystallogr F Struct Biol Commun, 2015","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-24T16:56:30.127Z"}}],"released":"2021_12","length":756,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP03062","date":"2020-12-16T15:20:31.100Z","regions_counter":2,"dataset":["Cancer-related proteins"],"UniParc":"UPI0000000C7E","uniref100":"UniRef100_P40692","uniref90":"UniRef90_P40692","uniref50":"UniRef50_P40692","genes":[{"name":{"value":"MLH1"},"synonyms":[{"value":"COCA2"}]}],"alphafold_very_low_content":0.19576719576719576,"disorder_content":0.041005291005291,"disprot_consensus":{"full":[{"start":86,"end":97,"type":"D"},{"start":301,"end":319,"type":"D"}],"Structural state":[{"start":86,"end":97,"type":"D"},{"start":301,"end":319,"type":"D"}]}},{"acc":"Q9BRZ2","features":{"pfam":[{"id":"PF00643","name":"B-box zinc finger","start":166,"end":205},{"id":"PF13445","name":"RING-type zinc-finger","start":21,"end":57}],"gene3D":[]},"creator":"ldobson","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MVSHGSSPSLLEALSSDFLACKICLEQLRAPKTLPCLHTYCQDCLAQLADGGRVRCPECRETVPVPPEGVASFKTNFFVNGLLDLVKARACGDLRAGKPACALCPLVGGTSTGGPATARCLDCADDLCQACADGHRCTRQTHTHRVVDLVGYRAGWYDEEARERQAAQCPQHPGEALRFLCQPCSQLLCRECRLDPHLDHPCLPLAEAVRARRPGLEGLLAGVDNNLVELEAARRVEKEALARLREQAARVGTQVEEAAEGVLRALLAQKQEVLGQLRAHVEAAEEAARERLAELEGREQVARAAAAFARRVLSLGREAEILSLEGAIAQRLRQLQGCPWAPGPAPCLLPQLELHPGLLDKNCHLLRLSFEEQQPQKDGGKDGAGTQGGEESQSRREDEPKTERQGGVQPQAGDGAQTPKEEKAQTTREEGAQTLEEDRAQTPHEDGGPQPHRGGRPNKKKKFKGRLKSISREPSPALGPNLDGSGLLPRPIFYCSFPTRMPGDKRSPRITGLCPFGPREILVADEQNRALKRFSLNGDYKGTVPVPEGCSPCSVAALQSAVAFSASARLYLINPNGEVQWRRALSLSQASHAVAALPSGDRVAVSVAGHVEVYNMEGSLATRFIPGGKASRGLRALVFLTTSPQGHFVGSDWQQNSVVICDGLGQVVGEYKGPGLHGCQPGSVSVDKKGYIFLTLREVNKVVILDPKGSLLGDFLTAYHGLEKPRVTTMVDGRYLVVSLSNGTIHIFRVRSPDS","name":"E3 ubiquitin-protein ligase TRIM56","regions":[{"region_id":"DP03063r001","unpublished":true,"ec_ontology":"ECO","end":17,"term_id":"IDPO:0000002","start":1,"version":2,"statement":[{"text":"Both the linker residues between TRIM56 and SopA, as well as the 17 N-terminal residues of TRIM56 were disordered and could not be observed in the electron density.","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0003-2765-3872","released":"2023_12","term_ontology":"IDPO","curator_name":"László Dobson","reference_id":"28084320","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5JW7"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"ldobson","reference_html":"Structural basis for the recognition and degradation of host TRIM proteins by Salmonella effector SopA. <i> Fiskin E, Bhogaraju S, Herhaus L, Kalayil S, Hahn M, Dikic I. </i> Nat Commun, 2017","validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-18T13:35:28.966Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2023_12","length":755,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP03063","date":"2020-12-16T15:37:31.368Z","regions_counter":1,"dataset":[],"UniParc":"UPI000013EAE8","uniref100":"UniRef100_Q9BRZ2","uniref90":"UniRef90_Q9BRZ2","uniref50":"UniRef50_Q9BRZ2","genes":[{"name":{"value":"TRIM56","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"21289118","url":"http://www.ncbi.nlm.nih.gov/pubmed/21289118","alternativeUrl":"https://europepmc.org/abstract/MED/21289118"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:19028","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:19028"}}]},"synonyms":[{"value":"RNF109"}]}],"alphafold_very_low_content":0.16556291390728478,"disorder_content":0.022516556291390728,"disprot_consensus":{"full":[{"start":1,"end":17,"type":"D"}],"Structural state":[{"start":1,"end":17,"type":"D"}]}},{"acc":"P51400","features":{"pfam":[{"id":"PF00035","name":"Double-stranded RNA binding motif","start":79,"end":140},{"id":"PF00035","name":"Double-stranded RNA binding motif","start":244,"end":294},{"id":"PF02137","name":"Adenosine-deaminase (editase) domain","start":370,"end":701}],"gene3D":[]},"creator":"eschad","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"sequence":"MDIEDEENMSSSSIDVKENRNLDNMPPKDSSTPGPGEGIPLSNGGGGSTSRKRPLEEGSNGHSKYRLKKRRKTPGPVLPKNALMQLNEIKPGLQYMLLSQTGPVHAPLFVMSVEVNGQVFEGSGPTKKKAKLHAAEKALRSFVQFPNASEAHLAMGRTLSVNTDFTSDQADFPDTLFNGFETPDKSEPPFYVGSNGDDSFSSSGDVSLSASPVPASLTQPPLPIPPPFPPPSGKNPVMILNELRPGLKYDFLSESGESHAKSFVMSVVVDGQFFEGSGRNKKLAKARAAQSALATVFNLHLDQTPSRQPVLSEGLQLHLPQVLADAVSRLVLGKFSDLTDNFSSPHARRKVLSGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSLLRFLYAQLELYLNNKEDQKKSIFQKSERGGFRLKDTVQFHLYISTSPCGDARIFSPHEPVLEGMAPDSHQLTEPADRHPNRKARGQLRTKIESGEGTIPVRSNASIQTWDGVLQGERLLTMSCSDKIARWNVVGIQGALLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAPNFSVNWTVGDTAIEVINATTGKDELGRPSRLCKHALYCRWMRVHGKVPPHLLRTKITKPTTYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEKPTEQDQFSFTP","name":"Double-stranded RNA-specific editase 1","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":230,"term_name":"disorder","reference_html":"Structure and specific RNA binding of ADAR2 double-stranded RNA binding motifs. <i> Stefl R, Xu M, Skrisovska L, Emeson RB, Allain FH. </i> Structure, 2006","start":148,"region_id":"DP03065r001","term_id":"IDPO:0000002","unpublished":true,"version":2,"curator_id":"eschad","released":"2022_03","term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"The comparison between the [1\nH,15N]-TROSY spectrum of a deuterated GB1-dsRBM12 and the [1\nH,15N]-HSQC spectra\nof both isolated dsRBM1 and dsRBM2 (Figure S1; see\nthe Supplemental Data available with this article online)\nshows that the dsRBM resonances are identical in both\ncontexts, except for a few N- and C-terminal residues.\nIn addition, this comparison indicates that the interdomain linker is flexible, as the chemical shifts of the\nlinker residues have random coil values (Stefl et al.,\n2005b).","type":"Results"}],"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","reference_id":"16472753","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-31T18:47:08.037Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Disorder function","ec_ontology":"ECO","end":230,"term_name":"flexible linker","start":148,"region_id":"DP03065r002","term_id":"IDPO:0000033","unpublished":true,"reference_html":"Structure and specific RNA binding of ADAR2 double-stranded RNA binding motifs. <i> Stefl R, Xu M, Skrisovska L, Emeson RB, Allain FH. </i> Structure, 2006","curator_id":"eschad","released":"2022_03","term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","reference_id":"16472753","statement":[{"text":"These results indicate that the ADAR2\ndsRBMs are independent domains separated by a flexible linker,similar to the two dsRBMs of PKR(Nanduriet al.,\n1998).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-31T18:47:09.867Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":152,"end":232,"reference_id":"20946981","reference_source":"pmid","reference_html":"The solution structure of the ADAR2 dsRBM-RNA complex reveals a sequence-specific readout of the minor groove. <i> Stefl R, Oberstrass FC, Hood JL, Jourdan M, Zimmermann M, Skrisovska L, Maris C, Peng L, Hofr C, Emeson RB, Allain FH. </i> Cell, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2L3J"},{"db":"PDB","id":"2L3C"}],"region_id":"DP03065r003","statement":[{"text":"This strategy could be used considering (1) the distinct RNA binding location for each dsRBMs, with no mutual interactions (Stefl et al., 2006), (2) the flexible unstructured linker connecting dsRBM1 and dsRBM2 in the complex (Stefl et al., 2006) and (3) an overlap in the RNA sequence of the joint region of the subcomplexes (Figure 1).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-04T15:35:26.161Z"}},{"start":152,"end":232,"reference_id":"20946981","reference_source":"pmid","reference_html":"The solution structure of the ADAR2 dsRBM-RNA complex reveals a sequence-specific readout of the minor groove. <i> Stefl R, Oberstrass FC, Hood JL, Jourdan M, Zimmermann M, Skrisovska L, Maris C, Peng L, Hofr C, Emeson RB, Allain FH. </i> Cell, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2L3J"},{"db":"PDB","id":"2L3C"}],"region_id":"DP03065r004","statement":[{"text":"This strategy could be used considering (1) the distinct RNA binding location for each dsRBMs, with no mutual interactions (Stefl et al., 2006), (2) the flexible unstructured linker connecting dsRBM1 and dsRBM2 in the complex (Stefl et al., 2006) and (3) an overlap in the RNA sequence of the joint region of the subcomplexes (Figure 1).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-04T15:35:24.865Z"}}],"released":"2021_12","length":711,"ncbi_taxon_id":10116,"organism":"Rattus norvegicus","disprot_id":"DP03065","date":"2020-12-16T15:57:14.570Z","regions_counter":4,"dataset":["RNA-binding proteins"],"UniParc":"UPI0000133623","uniref100":"UniRef100_P51400","uniref90":"UniRef90_P51400","uniref50":"UniRef50_P78563","genes":[{"name":{"value":"Adarb1"},"synonyms":[{"value":"Red1"}]}],"alphafold_very_low_content":0.2348804500703235,"disorder_content":0.11954992967651196,"disprot_consensus":{"full":[{"start":148,"end":232,"type":"D"}],"Structural state":[{"start":148,"end":232,"type":"D"}],"Disorder function":[{"start":148,"end":232,"type":"F"}]}},{"acc":"O16043","features":{"pfam":[],"gene3D":[]},"creator":"eschad","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"sequence":"MADVAEQKNETPVVEKVAAEEVDAVKKDAVAAEEVAAEKASITENGGAEEESVAKENGAADSSATEPTDAVDGEKASEPTVSFAADKDEKKDEDKKEDSAADGEDTKKESSEAVLPAVENGSEEVTNGDSTDAPAIEAVKRKVDEAAAKADEAVATPEKKAKLDEASTKDEVQNGAEASEVAA","name":"Anon1A4","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":183,"term_name":"disorder","reference_html":"Intrinsic structural disorder of DF31, a Drosophila protein of chromatin decondensation and remodeling activities. <i> Szollosi E, Bokor M, Bodor A, Perczel A, Klement E, Medzihradszky KF, Tompa K, Tompa P. </i> J Proteome Res, 2008","start":1,"region_id":"DP03066r001","term_id":"IDPO:0000002","unpublished":true,"version":2,"curator_id":"eschad","released":"2023_12","term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"far-UV circular dichroism evidence used in manual assertion","statement":[{"text":"Distinctive feature of the spectrum is a large negative peak at\n200 nm, typical of IDPs. Further, the lack of a shoulder in the\nrange 210-230 nm indicates that the protein has practically no\nsecondary structural elements.","type":"Figure"}],"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006204","reference_id":"18484763","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-31T19:01:21.549Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":183,"term_name":"disorder","reference_html":"Intrinsic structural disorder of DF31, a Drosophila protein of chromatin decondensation and remodeling activities. <i> Szollosi E, Bokor M, Bodor A, Perczel A, Klement E, Medzihradszky KF, Tompa K, Tompa P. </i> J Proteome Res, 2008","start":1,"region_id":"DP03066r002","term_id":"IDPO:0000002","unpublished":true,"version":2,"curator_id":"eschad","released":"2023_12","term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","statement":[{"text":"Considering the molecular mass of Df31, the onedimensional 1\nH NMR spectrum has unexpectedly sharp resonance lines. In addition, the lack of signal dispersion typical\nof folded proteins suggests that Df31 is either unfolded or may\nhave very little stable 3D structure.","type":"Results"}],"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006198","reference_id":"18484763","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-31T19:01:22.874Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":183,"term_name":"disorder","reference_html":"Intrinsic structural disorder of DF31, a Drosophila protein of chromatin decondensation and remodeling activities. <i> Szollosi E, Bokor M, Bodor A, Perczel A, Klement E, Medzihradszky KF, Tompa K, Tompa P. </i> J Proteome Res, 2008","start":1,"region_id":"DP03066r003","term_id":"IDPO:0000002","unpublished":true,"version":2,"curator_id":"eschad","released":"2023_12","term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","statement":[{"text":"As seen, Df31 resists\nboiling, whereas BSA precipitates, underscoring the mostly\ndisordered character of Df31.","type":"Results"}],"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006317","reference_id":"18484763","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-31T19:01:24.492Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":183,"term_name":"disorder","reference_html":"Intrinsic structural disorder of DF31, a Drosophila protein of chromatin decondensation and remodeling activities. <i> Szollosi E, Bokor M, Bodor A, Perczel A, Klement E, Medzihradszky KF, Tompa K, Tompa P. </i> J Proteome Res, 2008","start":1,"region_id":"DP03066r004","term_id":"IDPO:0000002","unpublished":true,"version":2,"curator_id":"eschad","released":"2023_12","term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"cleavage assay evidence used in manual assertion","statement":[{"text":"Another indirect indication of disorder is proteolytic sensitivity, signaling accessibility of the polypeptide chain. To explore\nthis opportunity, we have tested the effect of wide-specificity proteases (subtilisin and proteinase NOVO) and also a narrowspecificity protease (trypsin) on Df31. As seen (Figure 3B), each\nenzyme digested Df31 within 5 min, even though the enzymes\nwere used at very low enzyme/substrate ratios, typically in the\norder of 1:1000 to 1:2000 (w/w). ","type":"Results"}],"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007691","reference_id":"18484763","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-31T19:01:29.169Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":183,"term_name":"disorder","reference_html":"Intrinsic structural disorder of DF31, a Drosophila protein of chromatin decondensation and remodeling activities. <i> Szollosi E, Bokor M, Bodor A, Perczel A, Klement E, Medzihradszky KF, Tompa K, Tompa P. </i> J Proteome Res, 2008","start":1,"region_id":"DP03066r005","term_id":"IDPO:0000002","unpublished":true,"version":2,"curator_id":"eschad","released":"2023_12","term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"chromatography evidence used in manual assertion","statement":[{"text":"In our case, on a Superdex 200 gel-filtration column, Df31\nelutes at an apparent MW of about 67 kDa (Figure 7). This value\nreflects the behavior of full-length native Df31, as confirmed by SDS-PAGE analysis of the protein eluting from the column.\nOn the SDS gel, the protein migrates as a single band with an\napparent MW of 31 kDa (data not shown), in accord with its\napparent MW reported originally.","type":"Results"}],"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0007680","reference_id":"18484763","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-31T19:01:30.262Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":183,"term_name":"disorder","reference_html":"Intrinsic structural disorder of DF31, a Drosophila protein of chromatin decondensation and remodeling activities. <i> Szollosi E, Bokor M, Bodor A, Perczel A, Klement E, Medzihradszky KF, Tompa K, Tompa P. </i> J Proteome Res, 2008","start":1,"region_id":"DP03066r006","term_id":"IDPO:0000002","unpublished":true,"version":2,"curator_id":"eschad","released":"2023_12","term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"differential scanning calorimetry evidence used in manual assertion","statement":[{"text":"As opposed\nto this behavior, the calorimetric curve of Df31 is entirely flat,\nshowing no signs of a major cooperative structural transition.\nThus, Df31 lacks a folded structure; that is, it is disordered by\nthis criterion.","type":"Results"}],"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006232","reference_id":"18484763","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-31T19:01:31.812Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"released":"2023_12","length":183,"ncbi_taxon_id":7227,"organism":"Drosophila melanogaster","disprot_id":"DP03066","date":"2020-12-16T17:13:27.286Z","regions_counter":6,"dataset":[],"UniParc":"UPI00000770EC","uniref100":"UniRef100_O16043","uniref90":"UniRef90_O16043","uniref50":"UniRef50_O16043","genes":[{"name":{"value":"Df31","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF57222.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF57222.1"}},{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0022893","url":"http://flybase.org/reports/FBgn0022893.html"}}]},"synonyms":[{"value":"anon-EST:fe1A4","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF57222.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF57222.1"}}]},{"value":"anon-EST:Liang-1.46","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF57222.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF57222.1"}}]},{"value":"anon-EST:Posey126","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF57222.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF57222.1"}}]},{"value":"anon-WO0153538.53","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF57222.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF57222.1"}}]},{"value":"anon1A4","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF57222.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF57222.1"}}]},{"value":"BEST:LD04967","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF57222.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF57222.1"}}]},{"value":"clone 1.46","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF57222.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF57222.1"}}]},{"value":"DF 31","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF57222.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF57222.1"}}]},{"value":"DF31","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF57222.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF57222.1"}}]},{"value":"Dmel\\CG2207","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF57222.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF57222.1"}}]},{"value":"l(2)k05815","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF57222.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF57222.1"}}]},{"value":"LD04967","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF57222.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF57222.1"}}]}],"orfNames":[{"value":"CG2207","evidences":[{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0022893","url":"http://flybase.org/reports/FBgn0022893.html"}}]},{"value":"Dmel_CG2207","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF57222.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF57222.1"}}]}]}],"alphafold_very_low_content":0.3551912568306011,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":183,"type":"D"}],"Structural state":[{"start":1,"end":183,"type":"D"}]}},{"acc":"Q07475","features":{"pfam":[{"id":"PF11092","name":"Neuronal protein 3.1 (p311)","start":2,"end":68}],"gene3D":[]},"creator":"eschad","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"sequence":"MVYYPELLVWVSQEPFAYKEMEGGLIKGRLPVPKEVNRKKMEETGAASLTPPGSREFTSPATSYLHPF","name":"Neuronal regeneration-related protein","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":68,"term_name":"disorder","reference_html":"Novel RNA-binding protein P311 binds eukaryotic translation initiation factor 3 subunit b (eIF3b) to promote translation of transforming growth factor β1-3 (TGF-β1-3). <i> Yue MM, Lv K, Meredith SC, Martindale JL, Gorospe M, Schuger L. </i> J Biol Chem, 2014","start":1,"region_id":"DP03067r001","term_id":"IDPO:0000002","unpublished":true,"version":2,"curator_id":"eschad","released":"2023_12","term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"circular dichroism evidence used in manual assertion","statement":[{"text":"CD spectroscopy confirmed the lack of structure in the\nisolated protein in solution (Fig. 1).","type":"Results"}],"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006200","reference_id":"25336651","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-08T17:03:36.552Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2023_12","length":68,"ncbi_taxon_id":10090,"organism":"Mus musculus","disprot_id":"DP03067","date":"2020-12-16T18:03:23.621Z","regions_counter":8,"dataset":[],"UniParc":"UPI0000004151","uniref100":"UniRef100_Q07475","uniref90":"UniRef90_Q07475","uniref50":"UniRef50_Q07475","genes":[{"name":{"value":"Nrep"},"synonyms":[{"value":"D0H4S114"},{"value":"P311"}]}],"alphafold_very_low_content":0.014705882352941176,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":68,"type":"D"}],"Structural state":[{"start":1,"end":68,"type":"D"}]}},{"acc":"P24348","features":{"pfam":[{"id":"PF00757","name":"Furin-like cysteine rich region","start":213,"end":369},{"id":"PF01030","name":"Receptor L domain","start":65,"end":192},{"id":"PF01030","name":"Receptor L domain","start":384,"end":490},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":886,"end":1140},{"id":"PF14843","name":"Growth factor receptor domain IV","start":519,"end":638}],"gene3D":[]},"creator":"lrodriguez","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"sequence":"MRYPPSIGSILLIIPIFLTFFGNSNAQLWKRCVSPQDCLCSGTTNGISRYGTGNILEDLETMYRGCRRVYGNLEITWIEANEIKKWRESTNSTVDPKNEDSPLKSINFFDNLEEIRGSLIIYRANIQKISFPRLRVIYGDEVFHDNALYIHKNDKVHEVVMRELRVIRNGSVTIQDNPKMCYIGDKIDWKELLYDPDVQKVETTNSHQHCYQNGKSMAKCHESCNDKCWGSGDNDCQRVYRSVCPKSCSQCFYSNSTSSYECCDSACLGGCTGHGPKNCIACSKYELDGICIETCPSRKIFNHKTGRLVFNPDGRYQNGNHCVKECPPELLIENDVCVRHCSDGHHYDATKDVRECEKCRSSSCPKICTVDGHLTNETLKNLEGCEQIDGHLIIEHAFTYEQLKVLETVKIVSEYITIVQQNFYDLKFLKNLQIIEGRKLHNVRWALAIYQCDDLEELSLNSLKLIKTGAVLIMKNHRLCYVSKIDWSSIITSKGKDNKPSLAIAENRDSKLCETEQRVCDKNCNKRGCWGKEPEDCLECKTWKSVGTCVEKCDTKGFLRNQTSMKCERCSPECETCNGLGELDCLTCRHKTLYNSDFGNRMECVHDCPVSHFPTQKNVCEKCHPTCYDNGCTGPDSNLGYGGCKQCKYAVKYENDTIFCLQSSGMNNVCVENDLPNYYISTYDTEGVIETHCEKCSISCKTCSSAGRNVVQNKCVCKHVEYQPNPSERICMDQCPVNSFMVPDTNNTVCKKCHHECDQNYHCANGQSTGCQKCKNFTVFKGDIAQCVSECPKNLPFSNPANGECLDYDIASRQRKTRMVIIGSVLFGFAVMFLFILLVYWRCQRIGKKLKIAEMVDMPELTPIDASVRPNMSRICLIPSSELQTKLDKKLGAGAFGTVFAGIYYPKRAKNVKIPVAIKVFQTDQSQTDEMLEEATNMFRLRHDNLLKIIGFCMHDDGLKIVTIYRPLGNLQNFLKLHKENLGAREQVLYCYQIASGMQYLEKQRVVHRDLATRNVLVKKFNHVEITDFGLSKILKHDADSITIKSGKVAIKWLAIEIFSKHCYTHASDVWAFGVTCWEIITFGQSPYQGMSTDSIHNFLKDGNRLSQPPNCSQDLYQELLRCWMADPKSRPGFEILYERFKEFCKVPQLFLENSNKISESDLSAEERFQTERIREMFDGNIDPQMYFDQGSLPSMPSSPTSMATFTIPHGDLMNRMQSVNSSRYKTEPFDYGSTAQEDNSYLIPKTKEVQQSAVLYTAVTNEDGQTELSPSNGDYYNQPNTPSSSSGYYNEPHLKTKKPETSEEAEAVQYENEEVSQKETCL","name":"Receptor tyrosine-protein kinase let-23","regions":[{"region_id":"DP03068r001","unpublished":true,"ec_ontology":"ECO","end":1047,"term_id":"IDPO:0000002","start":1036,"version":2,"statement":[{"text":"The activation loop (residues 1028 – 1048) in LET-23 is largely disordered with the  exception of the N-terminal fragment encompassing the DFG motif (residues 1028 – 1035).","type":"Results"}],"term_name":"disorder","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","curator_orcid":"0000-0001-5782-6573","released":"2023_12","term_ontology":"IDPO","curator_name":"Luciana Rodriguez Sawicki","reference_id":"29358026","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","cross_refs":[{"db":"PDB","id":"5WNO"}],"term_namespace":"Structural state","ec_id":"ECO:0006220","curator_id":"lrodriguez","reference_html":"Regulation of Kinase Activity in the Caenorhabditis elegans EGF Receptor, LET-23. <i> Liu L, Thaker TM, Freed DM, Frazier N, Malhotra K, Lemmon MA, Jura N. </i> Structure, 2018","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-30T10:09:43.459Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1036,"end":1047,"reference_id":"29358026","reference_source":"pmid","reference_html":"Regulation of Kinase Activity in the Caenorhabditis elegans EGF Receptor, LET-23. <i> Liu L, Thaker TM, Freed DM, Frazier N, Malhotra K, Lemmon MA, Jura N. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"GO:0140677","term_name":"molecular function activator activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007687","ec_ontology":"ECO","ec_name":"protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03068r002","statement":[{"text":"LET-23 has no such tyrosine phosphorylation site in its activation loop (Figure 3C), suggesting that the observed concentration-dependent increase in kinase activity likely arises  through the allosteric effects of intermolecular interactions within kinase oligomers  stabilized on the vesicle surfaces. ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-31T16:28:45.420Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1036,"end":1047,"reference_id":"29358026","reference_source":"pmid","reference_html":"Regulation of Kinase Activity in the Caenorhabditis elegans EGF Receptor, LET-23. <i> Liu L, Thaker TM, Freed DM, Frazier N, Malhotra K, Lemmon MA, Jura N. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007687","ec_ontology":"ECO","ec_name":"protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03068r003","statement":[{"text":"Like human EGFR, LET-23 is also inactive in solution, but its activity is significantly increased by concentrating it on the surface of lipid vesicles - implicating the involvement of intermolecular interactions in kinase activation.","type":"Introduction"},{"text":"Figure 3. Catalytic activity of the LET-23 kinase domain in solution and associated with lipid  vesicles . ","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-31T16:28:32.786Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"released":"2023_12","length":1323,"ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","disprot_id":"DP03068","date":"2020-12-17T14:39:24.120Z","regions_counter":3,"dataset":[],"UniParc":"UPI0000164043","uniref100":"UniRef100_P24348","uniref90":"UniRef90_P24348","uniref50":"UniRef50_P24348","genes":[{"name":{"value":"let-23","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"ZK1067.1a","url":"https://www.wormbase.org/db/seq/sequence?name=ZK1067.1a;class=Transcript"}}]},"synonyms":[{"value":"kin-7","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"ZK1067.1a","url":"https://www.wormbase.org/db/seq/sequence?name=ZK1067.1a;class=Transcript"}}]}],"orfNames":[{"value":"ZK1067.1","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"ZK1067.1a","url":"https://www.wormbase.org/db/seq/sequence?name=ZK1067.1a;class=Transcript"}}]}]}],"alphafold_very_low_content":0.14285714285714285,"disorder_content":0.009070294784580499,"disprot_consensus":{"full":[{"start":1036,"end":1047,"type":"D"}],"Structural state":[{"start":1036,"end":1047,"type":"D"}],"Molecular function":[{"start":1036,"end":1047,"type":"F"}]}},{"acc":"P34712","features":{"pfam":[{"id":"PF00005","name":"ABC transporter","start":434,"end":583},{"id":"PF00005","name":"ABC transporter","start":1095,"end":1246},{"id":"PF00664","name":"ABC transporter transmembrane region","start":77,"end":367},{"id":"PF00664","name":"ABC transporter transmembrane region","start":754,"end":1026}],"gene3D":[]},"creator":"lrodriguez","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"sequence":"MLRNGSLRQSLRTLDSFSLAPEDVLKTAIKTVEDYEGDNIDSNGEIKITRDAKEEVVNKVSIPQLYRYTTTLEKLLLFIGTLVAVITGAGLPLMSILQGKVSQAFINEQIVINNNGSTFLPTGQNYTKTDFEHDVMNVVWSYAAMTVGMWAAGQITVTCYLYVAEQMNNRLRREFVKSILRQEISWFDTNHSGTLATKLFDNLERVKEGTGDKIGMAFQYLSQFITGFIVAFTHSWQLTLVMLAVTPIQALCGFAIAKSMSTFAIRETLRYAKAGKVVEETISSIRTVVSLNGLRYELERYSTAVEEAKKAGVLKGLFLGISFGAMQASNFISFALAFYIGVGWVHDGSLNFGDMLTTFSSVMMGSMALGLAGPQLAVLGTAQGAASGIYEVLDRKPVIDSSSKAGRKDMKIKGDITVENVHFTYPSRPDVPILRGMNLRVNAGQTVALVGSSGCGKSTIISLLLRYYDVLKGKITIDGVDVRDINLEFLRKNVAVVSQEPALFNCTIEENISLGKEGITREEMVAACKMANAEKFIKTLPNGYNTLVGDRGTQLSGGQKQRIAIARALVRNPKILLLDEATSALDAESEGIVQQALDKAAKGRTTIIIAHRLSTIRNADLIISCKNGQVVEVGDHRALMAQQGLYYDLVTAQTFTDAVDSAAEGKFSRENSVARQTSEHEGLSRQASEMDDIMNRVRSSTIGSITNGPVIDEKEERIGKDALSRLKQELEENNAQKTNLFEILYHARPHALSLFIGMSTATIGGFIYPTYSVFFTSFMNVFAGNPADFLSQGHFWALMFLVLAAAQGICSFLMTFFMGIASESLTRDLRNKLFRNVLSQHIGFFDSPQNASGKISTRLATDVPNLRTAIDFRFSTVITTLVSMVAGIGLAFFYGWQMALLIIAILPIVAFGQYLRGRRFTGKNVKSASEFADSGKIAIEAIENVRTVQALAREDTFYENFCEKLDIPHKEAIKEAFIQGLSYGCASSVLYLLNTCAYRMGLALIITDPPTMQPMRVLRVMYAITISTSTLGFATSYFPEYAKATFAGGIIFGMLRKISKIDSLSLAGEKKKLYGKVIFKNVRFAYPERPEIEILKGLSFSVEPGQTLALVGPSGCGKSTVVALLERFYDTLGGEIFIDGSEIKTLNPEHTRSQIAIVSQEPTLFDCSIAENIIYGLDPSSVTMAQVEEAARLANIHNFIAELPEGFETRVGDRGTQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEKVVQEALDRAREGRTCIVIAHRLNTVMNADCIAVVSNGTIIEKGTHTQLMSEKGAYYKLTQKQMTEKK","name":"Multidrug resistance protein pgp-1","regions":[{"start":666,"end":715,"reference_id":"23000902","reference_source":"pmid","reference_html":"Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegans. <i> Jin MS, Oldham ML, Zhang Q, Chen J. </i> Nature, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4F4C"}],"region_id":"DP03069r002","statement":[{"text":"Residues of the N-terminus (1–3, 52–54), the linker region (666– 715) and the C-terminus (1307–1321) were not visible in the electron density map and were  not included in the final structure. ","type":"Methods"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-31T16:49:08.794Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1307,"end":1321,"reference_id":"23000902","reference_source":"pmid","reference_html":"Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegans. <i> Jin MS, Oldham ML, Zhang Q, Chen J. </i> Nature, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4F4C"}],"region_id":"DP03069r003","statement":[{"text":"Residues of the N-terminus (1–3, 52–54), the linker region (666– 715) and the C-terminus (1307–1321) were not visible in the electron density map and were  not included in the final structure. ","type":"Methods"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-31T16:49:10.108Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":666,"end":715,"reference_id":"23000902","reference_source":"pmid","reference_html":"Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegans. <i> Jin MS, Oldham ML, Zhang Q, Chen J. </i> Nature, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"4F4C"}],"region_id":"DP03069r004","statement":[{"text":"Residues of the N-terminus (1–3, 52–54), the linker region (666– 715) and the C-terminus (1307–1321) were not visible in the electron density map and were  not included in the final structure. ","type":"Methods"},{"text":"This flexible linker connects nucleotide binding domain 1 (NBD1)  and transmembrane domain 2 (TMD) of protein P-gp.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Disorder function"}],"released":"2021_12","length":1321,"ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","disprot_id":"DP03069","date":"2020-12-17T22:34:26.464Z","regions_counter":4,"dataset":[],"UniParc":"UPI000012EE81","uniref100":"UniRef100_P34712","uniref90":"UniRef90_P34712","uniref50":"UniRef50_P34712","genes":[{"name":{"value":"pgp-1"},"orfNames":[{"value":"K08E7.9"}]}],"alphafold_very_low_content":0.07418622255866768,"disorder_content":0.04920514761544285,"disprot_consensus":{"full":[{"start":666,"end":715,"type":"D"},{"start":1307,"end":1321,"type":"D"}],"Structural state":[{"start":666,"end":715,"type":"D"},{"start":1307,"end":1321,"type":"D"}],"Disorder function":[{"start":666,"end":715,"type":"F"}]}},{"acc":"Q8TEQ6","features":{"pfam":[{"id":"PF00400","name":"WD domain, G-beta repeat","start":238,"end":255},{"id":"PF23770","name":"RIG first beta-propeller","start":80,"end":237},{"id":"PF23774","name":"GEMI5 TPR domain","start":893,"end":1101},{"id":"PF23775","name":"RIG second beta-propeller","start":391,"end":701},{"id":"PF23777","name":"GEMI5 RBS C-terminal domain","start":1156,"end":1494}],"gene3D":[]},"creator":"ldobson","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MGQEPRTLPPSPNWYCARCSDAVPGGLFGFAARTSVFLVRVGPGAGESPGTPPFRVIGELVGHTERVSGFTFSHHPGQYNLCATSSDDGTVKIWDVETKTVVTEHALHQHTISTLHWSPRVKDLIVSGDEKGVVFCYWFNRNDSQHLFIEPRTIFCLTCSPHHEDLVAIGYKDGIVVIIDISKKGEVIHRLRGHDDEIHSIAWCPLPGEDCLSINQEETSEEAEITNGNAVAQAPVTKGCYLATGSKDQTIRIWSCSRGRGVMILKLPFLKRRGGGIDPTVKERLWLTLHWPSNQPTQLVSSCFGGELLQWDLTQSWRRKYTLFSASSEGQNHSRIVFNLCPLQTEDDKQLLLSTSMDRDVKCWDIATLECSWTLPSLGGFAYSLAFSSVDIGSLAIGVGDGMIRVWNTLSIKNNYDVKNFWQGVKSKVTALCWHPTKEGCLAFGTDDGKVGLYDTYSNKPPQISSTYHKKTVYTLAWGPPVPPMSLGGEGDRPSLALYSCGGEGIVLQHNPWKLSGEAFDINKLIRDTNSIKYKLPVHTEISWKADGKIMALGNEDGSIEIFQIPNLKLICTIQQHHKLVNTISWHHEHGSQPELSYLMASGSNNAVIYVHNLKTVIESSPESPVTITEPYRTLSGHTAKITSVAWSPHHDGRLVSASYDGTAQVWDALREEPLCNFRGHRGRLLCVAWSPLDPDCIYSGADDFCVHKWLTSMQDHSRPPQGKKSIELEKKRLSQPKAKPKKKKKPTLRTPVKLESIDGNEEESMKENSGPVENGVSDQEGEEQAREPELPCGLAPAVSREPVICTPVSSGFEKSKVTINNKVILLKKEPPKEKPETLIKKRKARSLLPLSTSLDHRSKEELHQDCLVLATAKHSRELNEDVSADVEERFHLGLFTDRATLYRMIDIEGKGHLENGHPELFHQLMLWKGDLKGVLQTAAERGELTDNLVAMAPAAGYHVWLWAVEAFAKQLCFQDQYVKAASHLLSIHKVYEAVELLKSNHFYREAIAIAKARLRPEDPVLKDLYLSWGTVLERDGHYAVAAKCYLGATCAYDAAKVLAKKGDAASLRTAAELAAIVGEDELSASLALRCAQELLLANNWVGAQEALQLHESLQGQRLVFCLLELLSRHLEEKQLSEGKSSSSYHTWNTGTEGPFVERVTAVWKSIFSLDTPEQYQEAFQKLQNIKYPSATNNTPAKQLLLHICHDLTLAVLSQQMASWDEAVQALLRAVVRSYDSGSFTIMQEVYSAFLPDGCDHLRDKLGDHQSPATPAFKSLEAFFLYGRLYEFWWSLSRPCPNSSVWVRAGHRTLSVEPSQQLDTASTEETDPETSQPEPNRPSELDLRLTEEGERMLSTFKELFSEKHASLQNSQRTVAEVQETLAEMIRQHQKSQLCKSTANGPDKNEPEVEAEQPLCSSQSQCKEEKNEPLSLPELTKRLTEANQRMAKFPESIKAWPFPDVLECCLVLLLIRSHFPGCLAQEMQQQAQELLQKYGNTKTYRRHCQTFCM","name":"Gem-associated protein 5","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":1412,"term_name":"disorder","reference_html":"Identification of novel non-canonical RNA-binding sites in Gemin5 involved in internal initiation of translation. <i> Fernandez-Chamorro J, Piñeiro D, Gordon JM, Ramajo J, Francisco-Velilla R, Macias MJ, Martinez-Salas E. </i> Nucleic Acids Res, 2014","start":1297,"region_id":"DP03070r001","term_id":"IDPO:0000002","unpublished":true,"version":2,"curator_id":"eschad","released":"2022_03","term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","statement":[{"text":"All experimental conditions we assayed\nyielded samples that provide NMR data in agreement with\nthe absence of tertiary structure (Supplementary Figure\nS1). Only ∼80% of the signals corresponding to the RBS1 domain were defined in the spectrum, precluding the unambiguous assignment of all resonances. Still, we have assigned\nsome fragments of the sequence using standard backbone\ntriple resonance experiments. Based on these assignments\nand on the dispersion of the NMR signals shown in the\nspectrum, we conclude that the RBS1 construct has a short\nhelical conformation surrounded by unstructured regions,\nyielding the ensemble of flexible conformations observed\nin 2D and 3D NOESY (Nuclear Overhauser effect spectroscopy) experiments.","type":"Results"}],"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","reference_id":"24598255","ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T17:07:46.766Z"}},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":1412,"term_name":"RNA binding","reference_html":"Identification of novel non-canonical RNA-binding sites in Gemin5 involved in internal initiation of translation. <i> Fernandez-Chamorro J, Piñeiro D, Gordon JM, Ramajo J, Francisco-Velilla R, Macias MJ, Martinez-Salas E. </i> Nucleic Acids Res, 2014","start":1297,"region_id":"DP03070r002","term_id":"GO:0003723","unpublished":true,"version":4,"curator_id":"esalladini","released":"2022_03","term_ontology":"GO","curator_name":"Edoardo Salladini","ec_name":"cross-linking evidence used in manual assertion","statement":[{"text":"Therefore,\nwe conclude that a bipartite RNA-binding site, comprising\nresidues 1297–1412 (RBS1) and 1383–1508 (RBS2), within\nthe C-terminal region of Gemin5 enables a direct interaction with the IRES element with RBS1 being more intense\nthan RBS2 in UV-crosslinking experiments.","type":"Results"}],"curator_orcid":"0000-0002-5152-5953","date":"2022-03-08T14:04:05.827Z","reference_source":"pmid","ec_id":"ECO:0001170","reference_id":"24598255","ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"RNAcentral","id":"URS0001BC0BF1_9606","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T17:07:59.490Z"}},{"start":1294,"end":1361,"reference_id":"34424823","reference_source":"pmid","reference_html":"The RBS1 domain of Gemin5 is intrinsically unstructured and interacts with RNA through conserved Arg and aromatic residues. <i> Embarc-Buh A, Francisco-Velilla R, Camero S, Pérez-Cañadillas JM, Martínez-Salas E. </i> RNA Biol, 2021","date":"2025-03-24T15:35:34.287Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"ec_go":"IPI","region_id":"DP03070r005","statement":[{"text":"Interestingly, the protein RBS11361-HIS encompassing mostly the predicted unstructured region of RBS1 retained RNA-binding activity (Fig. 2C), although with moderate affinity relative to HIS-RBS11412 (Table 1). Similar results were observed with HIS-RBS11361 (Fig. 2D).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"RNAcentral","id":"URS0002318D25_12116","operator":null,"partner_start":null,"partner_end":null}]}],"released":"2021_12","length":1508,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP03070","date":"2020-12-18T15:49:48.463Z","regions_counter":5,"dataset":["NDDs-related proteins","RNA-binding proteins"],"UniParc":"UPI000020D072","uniref100":"UniRef100_Q8TEQ6","uniref90":"UniRef90_Q8TEQ6","uniref50":"UniRef50_Q8TEQ6","genes":[{"name":{"value":"GEMIN5"}}],"alphafold_very_low_content":0.15915119363395225,"disorder_content":0.07692307692307693,"disprot_consensus":{"full":[{"start":1294,"end":1296,"type":"F"},{"start":1297,"end":1412,"type":"D"}],"Structural state":[{"start":1297,"end":1412,"type":"D"}],"Molecular function":[{"start":1294,"end":1412,"type":"F"}]}},{"acc":"Q92499","features":{"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":26,"end":70},{"id":"PF00270","name":"DEAD/DEAH box helicase","start":283,"end":413},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":496,"end":609},{"id":"PF00622","name":"SPRY domain","start":132,"end":244}],"gene3D":[]},"creator":"eschad","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"sequence":"MAAFSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVYETLKDQQEGKKGKTTIKTGASVLNKWQMNPYDRGSAFAIGSDGLCCQSREVKEWHGCRATKGLMKGKHYYEVSCHDQGLCRVGWSTMQASLDLGTDKFGFGFGGTGKKSHNKQFDNYGEEFTMHDTIGCYLDIDKGHVKFSKNGKDLGLAFEIPPHMKNQALFPACVLKNAELKFNFGEEEFKFPPKDGFVALSKAPDGYIVKSQHSGNAQVTQTKFLPNAPKALIVEPSRELAEQTLNNIKQFKKYIDNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVRFLVLDEADGLLSQGYSDFINRMHNQIPQVTSDGKRLQVIVCSATLHSFDVKKLSEKIMHFPTWVDLKGEDSVPDTVHHVVVPVNPKTDRLWERLGKSHIRTDDVHAKDNTRPGANSPEMWSEAIKILKGEYAVRAIKEHKMDQAIIFCRTKIDCDNLEQYFIQQGGGPDKKGHQFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRIGRVGRAERMGLAISLVATEKEKVWYHVCSSRGKGCYNTRLKEDGGCTIWYNEMQLLSEIEEHLNCTISQVEPDIKVPVDEFDGKVTYGQKRAAGGGSYKGHVDILAPTVQELAALEKEAQTSFLHLGYLPNQLFRTF","name":"ATP-dependent RNA helicase DDX1","regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":85,"term_name":"disorder","reference_html":"Structure of the SPRY domain of the human RNA helicase DDX1, a putative interaction platform within a DEAD-box protein. <i> Kellner JN, Meinhart A. </i> Acta Crystallogr F Struct Biol Commun, 2015","start":72,"region_id":"DP03071r001","term_id":"IDPO:0000002","unpublished":true,"version":2,"curator_id":"eschad","released":"2023_12","term_ontology":"IDPO","curator_name":"Eva Schad","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","statement":[{"text":"The protein construct used in the final crystallization setup\nconsisted of residues 72–283 of human DDX1; however, clear\nelectron density was only observed for residues 86–275 of\nchain A and residues 86–279 of chain B. The residues at the Nand C-terminus that could not be modelled are likely to be\ndisordered in the crystal since we observed some ambiguous\ndensity that could not be interpreted.","type":"Results"}],"curator_orcid":"0000-0002-3006-2910","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006220","reference_id":"26323305","cross_refs":[{"db":"PDB","id":"4XW3"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-05T16:31:31.933Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"released":"2023_12","length":740,"ncbi_taxon_id":9606,"organism":"Homo sapiens","disprot_id":"DP03071","date":"2020-12-18T18:35:11.654Z","regions_counter":1,"dataset":[],"UniParc":"UPI0000527EC5","uniref100":"UniRef100_Q92499","uniref90":"UniRef90_Q92499","uniref50":"UniRef50_Q92499","genes":[{"name":{"value":"DDX1"}}],"alphafold_very_low_content":0.052702702702702706,"disorder_content":0.01891891891891892,"disprot_consensus":{"full":[{"start":72,"end":85,"type":"D"}],"Structural state":[{"start":72,"end":85,"type":"D"}]}},{"disprot_id":"DP03072","acc":"P53420","creator":"gpozzati","date":"2020-12-23T17:56:01.336Z","features":{"pfam":[{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":62,"end":119},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":183,"end":235},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":296,"end":354},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":367,"end":427},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":500,"end":557},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":906,"end":964},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":1015,"end":1073},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":1082,"end":1139},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":1198,"end":1249},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":1313,"end":1370},{"id":"PF01413","name":"C-terminal tandem repeated domain in type 4 procollagen","start":1467,"end":1570},{"id":"PF01413","name":"C-terminal tandem repeated domain in type 4 procollagen","start":1575,"end":1687}],"gene3D":[]},"length":1690,"name":"Collagen alpha-4(IV) chain","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1656,"end":1671,"reference_id":"30443360","reference_source":"pmid","reference_html":"Structures of collagen IV globular domains: insight into associated pathologies, folding and network assembly. <i> Casino P, Gozalbo-Rovira R, Rodríguez-Díaz J, Banerjee S, Boutaud A, Rubio V, Hudson BG, Saus J, Cervera J, Marina A. </i> IUCrJ, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"gpozzati","curator_name":"Gabriele Pozzati","curator_orcid":"0000-0002-4303-9939","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5NB1"}],"region_id":"DP03072r001","statement":[{"text":"SM3' was disordered and was not visible in either a2NC1 homo or a4NC1 homo (Fig. 3)","type":"Results"}],"validated":{"curator_name":"Lucia Chemes","curator_id":"lchemes","timestamp":"2021-06-15T21:03:09.255Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1656,"end":1671,"reference_id":"30443360","reference_source":"pmid","reference_html":"Structures of collagen IV globular domains: insight into associated pathologies, folding and network assembly. <i> Casino P, Gozalbo-Rovira R, Rodríguez-Díaz J, Banerjee S, Boutaud A, Rubio V, Hudson BG, Saus J, Cervera J, Marina A. </i> IUCrJ, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"gpozzati","curator_name":"Gabriele Pozzati","curator_orcid":"0000-0002-4303-9939","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"5NB1"}],"region_id":"DP03072r002","statement":[{"text":"Overall, a comparison of noncanonical and canonical oligomers (Figs. 3a and 3b) revealed that the SM1, SM1’ and SM2 flexible regions are key determinants in protomer formation, while the loops connecting these motifs, Lb7b8 (motif ClA), Lb70b80 and SM3’, are needed to establish the protomer–protomer interactions that generate the hexamer.","type":"Results"},{"text":"Proposed model for canonical hexamer assembly. Individual monomers (a) start to nucleate a protomer via\n\nb-sheets I/I0 (b). Next, the SM1/1’ and SM2/SM2’ flexible regions from b-sheets II/II0 are stabilized in the nascent protomer, resulting in favoured additional intersubunit interactions within the protomer (c). Final stabilization is attained with the proper folding of SM3’ and of the ClA and ClB motifs that allow the binding of chloride ions (green spheres) (d). The two protomers in the hexamer are now ready to be joined by sulfilimine bonds (red lines).","type":"Figure"},{"text":"Our findings of noncanonical assemblies for a2NC1 and a4NC1 homo-oligomers and the structural changes observed in the chains forming these noncanonical protomers in comparison to a2NC1_121 and to the chains in a1NC1homo, a3NC1homo and a5NC1homo could imply that chain folding is closely related to protomer assembly. It is unlikely that a2NC1homo and a4NC1homo could represent stable physiological assemblies, but the structures of the individual chains in these noncanonical oligomers might provide a frozen glimpse of transient conformational states in the process of NC1 folding and hexamer building.","type":"Discussion"}],"validated":{"curator_name":"Lucia Chemes","curator_id":"lchemes","timestamp":"2021-06-15T21:03:49.104Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":2,"released":"2021_12","sequence":"MWSLHIVLMRCSFRLTKSLATGPWSLILILFSVQYVYGSGKKYIGPCGGRDCSVCHCVPEKGSRGPPGPPGPQGPIGPLGAPGPIGLSGEKGMRGDRGPPGAAGDKGDKGPTGVPGFPGLDGIPGHPGPPGPRGKPGMSGHNGSRGDPGFPGGRGALGPGGPLGHPGEKGEKGNSVFILGAVKGIQGDRGDPGLPGLPGSWGAGGPAGPTGYPGEPGLVGPPGQPGRPGLKGNPGVGVKGQMGDPGEVGQQGSPGPTLLVEPPDFCLYKGEKGIKGIPGMVGLPGPPGRKGESGIGAKGEKGIPGFPGPRGDPGSYGSPGFPGLKGELGLVGDPGLFGLIGPKGDPGNRGHPGPPGVLVTPPLPLKGPPGDPGFPGRYGETGDVGPPGPPGLLGRPGEACAGMIGPPGPQGFPGLPGLPGEAGIPGRPDSAPGKPGKPGSPGLPGAPGLQGLPGSSVIYCSVGNPGPQGIKGKVGPPGGRGPKGEKGNEGLCACEPGPMGPPGPPGLPGRQGSKGDLGLPGWLGTKGDPGPPGAEGPPGLPGKHGASGPPGNKGAKGDMVVSRVKGHKGERGPDGPPGFPGQPGSHGRDGHAGEKGDPGPPGDHEDATPGGKGFPGPLGPPGKAGPVGPPGLGFPGPPGERGHPGVPGHPGVRGPDGLKGQKGDTISCNVTYPGRHGPPGFDGPPGPKGFPGPQGAPGLSGSDGHKGRPGTPGTAEIPGPPGFRGDMGDPGFGGEKGSSPVGPPGPPGSPGVNGQKGIPGDPAFGHLGPPGKRGLSGVPGIKGPRGDPGCPGAEGPAGIPGFLGLKGPKGREGHAGFPGVPGPPGHSCERGAPGIPGQPGLPGYPGSPGAPGGKGQPGDVGPPGPAGMKGLPGLPGRPGAHGPPGLPGIPGPFGDDGLPGPPGPKGPRGLPGFPGFPGERGKPGAEGCPGAKGEPGEKGMSGLPGDRGLRGAKGAIGPPGDEGEMAIISQKGTPGEPGPPGDDGFPGERGDKGTPGMQGRRGEPGRYGPPGFHRGEPGEKGQPGPPGPPGPPGSTGLRGFIGFPGLPGDQGEPGSPGPPGFSGIDGARGPKGNKGDPASHFGPPGPKGEPGSPGCPGHFGASGEQGLPGIQGPRGSPGRPGPPGSSGPPGCPGDHGMPGLRGQPGEMGDPGPRGLQGDPGIPGPPGIKGPSGSPGLNGLHGLKGQKGTKGASGLHDVGPPGPVGIPGLKGERGDPGSPGISPPGPRGKKGPPGPPGSSGPPGPAGATGRAPKDIPDPGPPGDQGPPGPDGPRGAPGPPGLPGSVDLLRGEPGDCGLPGPPGPPGPPGPPGYKGFPGCDGKDGQKGPVGFPGPQGPHGFPGPPGEKGLPGPPGRKGPTGLPGPRGEPGPPADVDDCPRIPGLPGAPGMRGPEGAMGLPGMRGPSGPGCKGEPGLDGRRGVDGVPGSPGPPGRKGDTGEDGYPGGPGPPGPIGDPGPKGFGPGYLGGFLLVLHSQTDQEPTCPLGMPRLWTGYSLLYLEGQEKAHNQDLGLAGSCLPVFSTLPFAYCNIHQVCHYAQRNDRSYWLASAAPLPMMPLSEEAIRPYVSRCAVCEAPAQAVAVHSQDQSIPPCPQTWRSLWIGYSFLMHTGAGDQGGGQALMSPGSCLEDFRAAPFLECQGRQGTCHFFANKYSFWLTTVKADLQFSSAPAPDTLKESQAQRQKISRCQVCVKYS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000000769","uniref100":"UniRef100_P53420","uniref90":"UniRef90_P53420","uniref50":"UniRef50_P53420","genes":[{"name":{"value":"COL4A4"}}],"alphafold_very_low_content":0.7520710059171598,"disorder_content":0.009467455621301775,"disprot_consensus":{"full":[{"start":1656,"end":1671,"type":"D"}],"Structural state":[{"start":1656,"end":1671,"type":"D"}],"Molecular function":[{"start":1656,"end":1671,"type":"F"}]}},{"disprot_id":"DP03073","acc":"P26285","creator":"gpozzati","date":"2020-12-23T21:10:08.940Z","features":{"pfam":[{"id":"PF00300","name":"Histidine phosphatase superfamily (branch 1)","start":253,"end":436},{"id":"PF01591","name":"6-phosphofructo-2-kinase","start":28,"end":250}],"gene3D":[]},"length":531,"name":"6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2","ncbi_taxon_id":9913,"organism":"Bos taurus","regions":[{"start":1,"end":27,"reference_id":"27802586","reference_source":"pmid","reference_html":"Crystal structure of heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB2) and the inhibitory influence of citrate on substrate binding. <i> Crochet RB, Kim JD, Lee H, Yim YS, Kim SG, Neau D, Lee YH. </i> Proteins, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"gpozzati","curator_name":"Gabriele Pozzati","curator_orcid":"0000-0002-4303-9939","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"5HR5"}],"region_id":"DP03073r001","statement":[{"text":"The missing residues are all from both the N- and C-terminal regulatory domains and are considered disordered, based on the results from mass spectroscopy of melt crystals (data not shown).","type":"Methods"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-28T15:31:02.744Z"}},{"start":452,"end":531,"reference_id":"27802586","reference_source":"pmid","reference_html":"Crystal structure of heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB2) and the inhibitory influence of citrate on substrate binding. <i> Crochet RB, Kim JD, Lee H, Yim YS, Kim SG, Neau D, Lee YH. </i> Proteins, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"gpozzati","curator_name":"Gabriele Pozzati","curator_orcid":"0000-0002-4303-9939","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"5HR5"}],"region_id":"DP03073r002","statement":[{"text":"The missing residues are all from both the N- and C-terminal regulatory domains and are considered disordered, based on the results from mass spectroscopy of melt crystals (data not shown).","type":"Methods"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-28T15:31:19.298Z"}}],"regions_counter":2,"released":"2023_12","sequence":"MSGNPASSSEQNNNSYETKASLRISEKKCSWASYMTNSPTLIVMIGLPARGKTYVSKKLTRYLNWIGVPTKVFNLGVYRRQAVKSYKSYDFFRHDNEEAMKIRKQCALVALKDVKAYLTEESGQIAVFDATNTTRERRDLILNFAEENSFKVFFVESVCDDPDVIAANILEVKVSSPDYPERNRENVMDDFLKRIECYKVTYQPLDPDSHDKDLSFIKVINVGQRFLVNKVQDYIQSKIVYYLMNIHVHPRTIYLCRHGESEFNLLGKIGGDSGLSVRGKQFAQALRKFLEEQEIADLKVWTSQLKRTIQTAESLGVTYEQWKILNEIDAGVCEEMTYAEIQEQYPDEFALRDEEKYLYRYPGGESYQDLVQRLEPVIMELERQGNVLVISHQAVMRCLLAYFLDKGADELPYLRCPLHTIFKLTPVAYGCKVETIKLNVEAVNTHRDKPTNNFPKSQTPVRMRRNSFTPLSSSNTIRRPRNYSVGSRPLQPLSPLRALDTQEGADQPKTQAETSRAAHRLPSPAPPTSPS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"dataset":[],"UniParc":"UPI000012A3EF","uniref100":"UniRef100_P26285","uniref90":"UniRef90_O60825","uniref50":"UniRef50_O60825","genes":[{"name":{"value":"PFKFB2"}}],"alphafold_very_low_content":0.18455743879472694,"disorder_content":0.2015065913370998,"disprot_consensus":{"full":[{"start":1,"end":27,"type":"D"},{"start":452,"end":531,"type":"D"}],"Structural state":[{"start":1,"end":27,"type":"D"},{"start":452,"end":531,"type":"D"}]}},{"disprot_id":"DP03074","acc":"O60825","creator":"gpozzati","date":"2020-12-23T21:22:29.902Z","features":{"pfam":[{"id":"PF00300","name":"Histidine phosphatase superfamily (branch 1)","start":252,"end":435},{"id":"PF01591","name":"6-phosphofructo-2-kinase","start":27,"end":249}],"gene3D":[]},"length":505,"name":"6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":30,"reference_id":"27802586","reference_source":"pmid","reference_html":"Crystal structure of heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB2) and the inhibitory influence of citrate on substrate binding. <i> Crochet RB, Kim JD, Lee H, Yim YS, Kim SG, Neau D, Lee YH. </i> Proteins, 2017","date":"2022-12-28T15:36:40.700Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03074r001","statement":[{"text":"The final models revealed the residues 31–450 out of 505 of hPFKFB2 and those of 28–450 of bPFKFB2. The missing residues are all from both the N- and C-terminal regulatory domains and are considered disordered, based on the results from mass spectroscopy of melt crystals (data not shown).","type":"Methods"}],"ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"5HTK"}]},{"start":451,"end":505,"reference_id":"27802586","reference_source":"pmid","reference_html":"Crystal structure of heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB2) and the inhibitory influence of citrate on substrate binding. <i> Crochet RB, Kim JD, Lee H, Yim YS, Kim SG, Neau D, Lee YH. </i> Proteins, 2017","date":"2022-12-28T15:36:26.037Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03074r002","statement":[{"text":"The final models revealed the residues 31–450 out of 505 of hPFKFB2 and those of 28–450 of bPFKFB2. The missing residues are all from both the N- and C-terminal regulatory domains and are considered disordered, based on the results from mass spectroscopy of melt crystals (data not shown).","type":"Methods"}],"ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"5HTK"}]}],"regions_counter":2,"released":"2023_12","sequence":"MSGASSSEQNNNSYETKTPNLRMSEKKCSWASYMTNSPTLIVMIGLPARGKTYVSKKLTRYLNWIGVPTKVFNLGVYRREAVKSYKSYDFFRHDNEEAMKIRKQCALVALEDVKAYLTEENGQIAVFDATNTTRERRDMILNFAEQNSFKVFFVESVCDDPDVIAANILEVKVSSPDYPERNRENVMEDFLKRIECYKVTYRPLDPDNYDKDLSFIKVINVGQRFLVNRVQDYIQSKIVYYLMNIHVQPRTIYLCRHGESEFNLLGKIGGDSGLSVRGKQFAQALRKFLEEQEITDLKVWTSQLKRTIQTAESLGVPYEQWKILNEIDAGVCEEMTYAEIEKRYPEEFALRDQEKYLYRYPGGESYQDLVQRLEPVIMELERQGNVLVISHQAVMRCLLAYFLDKGADELPYLRCPLHTIFKLTPVAYGCKVETIKLNVEAVNTHRDKPTNNFPKNQTPVRMRRNSFTPLSSSNTIRRPRNYSVGSRPLKPLSPLRAQDMQEGAD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI0000163B6A","uniref100":"UniRef100_O60825","uniref90":"UniRef90_O60825","uniref50":"UniRef50_O60825","genes":[{"name":{"value":"PFKFB2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:8873","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8873"}}]}}],"alphafold_very_low_content":0.1485148514851485,"disorder_content":0.16831683168316833,"disprot_consensus":{"full":[{"start":1,"end":30,"type":"D"},{"start":451,"end":505,"type":"D"}],"Structural state":[{"start":1,"end":30,"type":"D"},{"start":451,"end":505,"type":"D"}]}},{"disprot_id":"DP03075","acc":"Q9H3M7","creator":"gpozzati","date":"2020-12-23T21:44:25.761Z","features":{"pfam":[{"id":"PF00339","name":"Arrestin (or S-antigen), N-terminal domain","start":10,"end":152},{"id":"PF02752","name":"Arrestin (or S-antigen), C-terminal domain","start":175,"end":298}],"gene3D":[]},"length":391,"name":"Thioredoxin-interacting protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":300,"end":317,"reference_id":"24389582","reference_source":"pmid","reference_html":"The structural basis for the negative regulation of thioredoxin by thioredoxin-interacting protein. <i> Hwang J, Suh HW, Jeon YH, Hwang E, Nguyen LT, Yeom J, Lee SG, Lee C, Kim KJ, Kang BS, Jeong JO, Oh TK, Choi I, Lee JO, Kim MH. </i> Nat Commun, 2014","date":"2022-12-28T15:44:53.666Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":3,"cross_refs":[{"db":"PDB","id":"4LL1"},{"db":"PDB","id":"4LL4"}],"region_id":"DP03075r001","statement":[{"text":"The electron density map of T–TXNIP presented here was not visible beyond residue 299, suggesting the presence of a flexible region.","type":"Discussion"}],"ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P10599"}]}],"regions_counter":1,"released":"2023_12","sequence":"MVMFKKIKSFEVVFNDPEKVYGSGEKVAGRVIVEVCEVTRVKAVRILACGVAKVLWMQGSQQCKQTSEYLRYEDTLLLEDQPTGENEMVIMRPGNKYEYKFGFELPQGPLGTSFKGKYGCVDYWVKAFLDRPSQPTQETKKNFEVVDLVDVNTPDLMAPVSAKKEKKVSCMFIPDGRVSVSARIDRKGFCEGDEISIHADFENTCSRIVVPKAAIVARHTYLANGQTKVLTQKLSSVRGNHIISGTCASWRGKSLRVQKIRPSILGCNILRVEYSLLIYVSVPGSKKVILDLPLVIGSRSGLSSRTSSMASRTSSEMSWVDLNIPDTPEAPPCYMDVIPEDHRLESPTTPLLDDMDGSQDSPIFMYAPEFKFMPPPTYTEVDPCILNNNVQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI0000072AFB","uniref100":"UniRef100_Q9H3M7","uniref90":"UniRef90_Q9H3M7","uniref50":"UniRef50_Q9H3M7","genes":[{"name":{"value":"TXNIP"},"synonyms":[{"value":"VDUP1"}]}],"alphafold_very_low_content":0.20460358056265984,"disorder_content":0.04603580562659847,"disprot_consensus":{"full":[{"start":300,"end":317,"type":"D"}],"Structural state":[{"start":300,"end":317,"type":"D"}]}},{"disprot_id":"DP03076","acc":"P0A910","creator":"vpromp","date":"2020-12-26T09:55:59.876Z","features":{"pfam":[{"id":"PF00691","name":"OmpA family","start":222,"end":317},{"id":"PF01389","name":"OmpA-like transmembrane domain","start":23,"end":195}],"gene3D":[]},"length":346,"name":"Outer membrane protein A","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":39,"end":51,"reference_id":"10764596","reference_source":"pmid","reference_html":"High-resolution structure of the OmpA membrane domain. <i> Pautsch A, Schulz GE. </i> J Mol Biol, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"vpromp","curator_name":"Vasilis J Promponas","curator_orcid":"0000-0003-3352-4831","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1QJP"}],"region_id":"DP03076r001","statement":[{"text":"The rms deviation between the common Ca atoms of both models (1-17, 31-63, 71-145 and 160-171) is 0.42 AÊ, and thus only slightly higher than expected from the coordinate errors. The largest deviations occur in the loop regions and smaller ones in turns T1 through to T3, and they correlate with the chain mobilities (Figure 2).","type":"Results"},{"text":"Loops L1, L2 and L4 have no density, indicating that they are extremely mobile.","type":"Figure"},{"text":"Please, notice that residue numbering in the author statements refer to a construct lacking the N-terminal signal peptide. This entry refers to extracellular loop L1. Extracellular loop L2 is not listed due to its short length (<10 AAs).","type":"Curator statement"},{"text":"The membrane domain of OmpA consists of an eight-stranded all-next-neighbor antiparallel beta-barrel with short turns at the periplasmic barrel end and long flexible loops at the external end. The structure analysis has been extended from medium resolution to 1.65 A (1 A=0.1 nm), and the molecular model has been refined anisotropically to show oriented mobilities of the structural elements.","type":"Abstract"},{"text":"The analysis indicates that the beta-barrel constitutes a solid scaffold such that the long external loops need not contribute to stability. These loops are highly mobile and thus cause a major problem during the crystallization process.","type":"Abstract"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-29T21:16:45.547Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":167,"end":180,"reference_id":"10764596","reference_source":"pmid","reference_html":"High-resolution structure of the OmpA membrane domain. <i> Pautsch A, Schulz GE. </i> J Mol Biol, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"vpromp","curator_name":"Vasilis J Promponas","curator_orcid":"0000-0003-3352-4831","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1QJP"}],"region_id":"DP03076r002","statement":[{"text":"The rms deviation between the common Ca atoms of both models (1-17, 31-63, 71-145 and 160-171) is 0.42 AÊ, and thus only slightly higher than expected from the coordinate errors. The largest deviations occur in the loop regions and smaller ones in turns T1 through to T3, and they correlate with the chain mobilities (Figure 2).","type":"Results"},{"text":"Loops L1, L2 and L4 have no density, indicating that they are extremely mobile.","type":"Figure"},{"text":"Please, notice that residue numbering in the author statements refer to a construct lacking the N-terminal signal peptide. This entry refers to extracellular loop L3. Extracellular loop L2 is not listed due to its short length (<10 AAs).","type":"Curator statement"},{"text":"he membrane domain of OmpA consists of an eight-stranded all-next-neighbor antiparallel beta-barrel with short turns at the periplasmic barrel end and long flexible loops at the external end. The structure analysis has been extended from medium resolution to 1.65 A (1 A=0.1 nm), and the molecular model has been refined anisotropically to show oriented mobilities of the structural elements.","type":"Abstract"},{"text":"The analysis indicates that the beta-barrel constitutes a solid scaffold such that the long external loops need not contribute to stability. These loops are highly mobile and thus cause a major problem during the crystallization process.","type":"Abstract"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-29T21:16:46.927Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MKKTAIAIAVALAGFATVAQAAPKDNTWYTGAKLGWSQYHDTGFINNNGPTHENQLGAGAFGGYQVNPYVGFEMGYDWLGRMPYKGSVENGAYKAQGVQLTAKLGYPITDDLDIYTRLGGMVWRADTKSNVYGKNHDTGVSPVFAGGVEYAITPEIATRLEYQWTNNIGDAHTIGTRPDNGMLSLGVSYRFGQGEAAPVVAPAPAPAPEVQTKHFTLKSDVLFNFNKATLKPEGQAALDQLYSQLSNLDPKDGSVVVLGYTDRIGSDAYNQGLSERRAQSVVDYLISKGIPADKISARGMGESNPVTGNTCDNVKQRAALIDCLAPDRRVEIEVKGIKDVVTQPQA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":[],"UniParc":"UPI0000130CF0","uniref100":"UniRef100_P0A911","uniref90":"UniRef90_B7LNW7","uniref50":"UniRef50_A0A2S4N3N0","genes":[{"name":{"value":"ompA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00842","url":"https://hamap.expasy.org/unirule/MF_00842"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"791936","url":"http://www.ncbi.nlm.nih.gov/pubmed/791936","alternativeUrl":"https://europepmc.org/abstract/MED/791936"}}]},"synonyms":[{"value":"con","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"4604263","url":"http://www.ncbi.nlm.nih.gov/pubmed/4604263","alternativeUrl":"https://europepmc.org/abstract/MED/4604263"}}]},{"value":"tolG","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"4591955","url":"http://www.ncbi.nlm.nih.gov/pubmed/4591955","alternativeUrl":"https://europepmc.org/abstract/MED/4591955"}}]},{"value":"tut","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"1107069","url":"http://www.ncbi.nlm.nih.gov/pubmed/1107069","alternativeUrl":"https://europepmc.org/abstract/MED/1107069"}}]}],"olnNames":[{"value":"b0957"},{"value":"JW0940"}]}],"alphafold_very_low_content":0.08959537572254335,"disorder_content":0.07803468208092486,"disprot_consensus":{"full":[{"start":39,"end":51,"type":"D"},{"start":167,"end":180,"type":"D"}],"Structural state":[{"start":39,"end":51,"type":"D"},{"start":167,"end":180,"type":"D"}]}},{"disprot_id":"DP03078","acc":"P76045","creator":"vpromp","date":"2020-12-28T20:38:50.574Z","features":{"pfam":[{"id":"PF09381","name":"Outer membrane protein G (OmpG)","start":25,"end":299}],"gene3D":[]},"length":301,"name":"Outer membrane porin G","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":241,"end":252,"reference_id":"16797588","reference_source":"pmid","reference_html":"Crystal structure of the monomeric porin OmpG. <i> Subbarao GV, van den Berg B. </i> J Mol Biol, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"vpromp","curator_name":"Vasilis J Promponas","curator_orcid":"0000-0003-3352-4831","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2F1C"}],"region_id":"DP03078r001","statement":[{"text":"The final OmpG model includes ∼90% of the residues of the mature protein; the residues 20–27 in loop L1, 59-60 in L2, 220–231 in L6 and 261–266 in L7 are not visible in the electron density maps, presumably because they are disordered.","type":"Results"},{"text":"Please, notice that residue numbering in the author statements refer to the mature protein form lacking the N-terminal signal peptide. This entry refers to part of the extracellular loop L6. Other regions not visible in the electron density maps are not reported here due to their short length (<10 AAs).\"","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-29T16:45:37.260Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MKKLLPCTALVMCAGMACAQAEERNDWHFNIGAMYEIENVEGYGEDMDGLAEPSVYFNAANGPWRIALAYYQEGPVDYSAGKRGTWFDRPELEVHYQFLENDDFSFGLTGGFRNYGYHYVDEPGKDTANMQRWKIAPDWDVKLTDDLRFNGWLSMYKFANDLNTTGYADTRVETETGLQYTFNETVALRVNYYLERGFNMDDSRNNGEFSTQEIRAYLPLTLGNHSVTPYTRIGLDRWSNWDWQDDIEREGHDFNRVGLFYGYDFQNGLSVSLEYAFEWQDHDEGDSDKFHYAGVGVNYSF","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":[],"UniParc":"UPI0000130D0A","uniref100":"UniRef100_P76045","uniref90":"UniRef90_P76045","uniref50":"UniRef50_P76045","genes":[{"name":{"value":"ompG"},"olnNames":[{"value":"b1319"},{"value":"JW1312"}]}],"alphafold_very_low_content":0.07973421926910298,"disorder_content":0.03986710963455149,"disprot_consensus":{"full":[{"start":241,"end":252,"type":"D"}],"Structural state":[{"start":241,"end":252,"type":"D"}]}},{"disprot_id":"DP03080","acc":"Q9Z214","creator":"ashenoy","date":"2020-12-29T17:25:01.007Z","features":{"pfam":[{"id":"PF00568","name":"WH1 domain","start":4,"end":106}],"gene3D":[]},"length":366,"name":"Homer protein homolog 1","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions":[{"start":144,"end":163,"reference_id":"12054806","reference_source":"pmid","reference_html":"Crystal structure of the Homer 1 family conserved region reveals the interaction between the EVH1 domain and own proline-rich motif. <i> Irie K, Nakatsu T, Mitsuoka K, Miyazawa A, Sobue K, Hiroaki Y, Doi T, Fujiyoshi Y, Kato H. </i> J Mol Biol, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"ashenoy","curator_name":"Aditi Shenoy","curator_orcid":"0000-0001-7748-2501","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1I2H"}],"region_id":"DP03080r001","statement":[{"text":"Only residues 1 – 143 were clearly modelled into the experimental map (Figure 3) with a final R-factor of 19.5% and good stereochemistry (Table 1), while we could find a suitable space for about 20 residues from 144–163 in the electron density map. We concluded, therefore, that removal of the 12  residues from the original was essential for crystallization and that the 20 remaining C-terminal residues of the fragment in the crystal are disordered.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MGEQPIFSTRAHVFQIDPNTKKNWVPTSKHAVTVSYFYDSTRNVYRIISLDGSKAIINSTITPNMTFTKTSQKFGQWADSRANTVYGLGFSSEHHLSKFAEKFQEFKEAARLAKEKSQEKMELTSTPSQESAGGDLQSPLTPESINGTDDERTPDVTQNSEPRAEPAQNALPFSHSAGDRTQGLSHASSAISKHWEAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELECVSSQANAVHSHKTELSQTVQELEETLKVKEEEIERLKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSELEQRLEKSQSEQDAFRSNLKTLLEILDGKIFELTELRDNLAKLLECS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"dataset":[],"UniParc":"UPI00000E6998","uniref100":"UniRef100_Q9Z214","uniref90":"UniRef90_Q9Z214","uniref50":"UniRef50_Q9Z214","genes":[{"name":{"value":"Homer1","evidences":[{"code":"ECO:0000312","source":{"name":"RGD","id":"628725","url":"https://rgd.mcw.edu/tools/genes/genes_view.cgi?id=628725"}}]},"synonyms":[{"value":"Homer"},{"value":"Vesl"}]}],"alphafold_very_low_content":0.15300546448087432,"disorder_content":0.0546448087431694,"disprot_consensus":{"full":[{"start":144,"end":163,"type":"D"}],"Structural state":[{"start":144,"end":163,"type":"D"}]}},{"disprot_id":"DP03081","acc":"P0DJI8","creator":"msalas","date":"2020-12-29T23:08:14.931Z","features":{"pfam":[{"id":"PF00277","name":"Serum amyloid A protein","start":23,"end":122}],"gene3D":[]},"length":122,"name":"Serum amyloid A-1 protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":74,"end":85,"reference_id":"30846696","reference_source":"pmid","reference_html":"Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids. <i> Liberta F, Loerch S, Rennegarbe M, Schierhorn A, Westermark P, Westermark GT, Hazenberg BPC, Grigorieff N, Fändrich M, Schmidt M. </i> Nat Commun, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"msalas","curator_name":"Martin Salas","curator_orcid":"0000-0001-6352-1282","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6MST"}],"region_id":"DP03081r001","statement":[{"text":"The IDR characterized in the publication and spanning residues 56-67 in the experimental construct corresponds to region 74-85 of the amino acid sequence.","type":"Curator statement"},{"text":"Adjacent to the C-terminal ends of their ordered parts, both fibril reconstructions show diffuse density (Supplementary Figure 5), indicating that C-terminal tails of the fibril proteins, corresponding to residues 70–83 in the murine and 56–67 in the human fibril proteins, are structurally disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-30T10:04:22.451Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MKLLTGLVFCSLVLGVSSRSFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGAWAAEVITDARENIQRFFGHGAEDSLADQAANEWGRSGKDPNHFRPAGLPEKY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI00001354CB","uniref100":"UniRef100_P0DJI8","uniref90":"UniRef90_P0DJI8","uniref50":"UniRef50_P0DJI8","genes":[{"name":{"value":"SAA1"}}],"alphafold_very_low_content":0,"disorder_content":0.09836065573770492,"disprot_consensus":{"full":[{"start":74,"end":85,"type":"D"}],"Structural state":[{"start":74,"end":85,"type":"D"}]}},{"disprot_id":"DP03082","acc":"P05367","creator":"msalas","date":"2020-12-29T23:24:32.558Z","features":{"pfam":[{"id":"PF00277","name":"Serum amyloid A protein","start":23,"end":122}],"gene3D":[]},"length":122,"name":"Serum amyloid A-2 protein","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":89,"end":102,"reference_id":"30846696","reference_source":"pmid","reference_html":"Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids. <i> Liberta F, Loerch S, Rennegarbe M, Schierhorn A, Westermark P, Westermark GT, Hazenberg BPC, Grigorieff N, Fändrich M, Schmidt M. </i> Nat Commun, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"msalas","curator_name":"Martin Salas","curator_orcid":"0000-0001-6352-1282","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6DSO"}],"region_id":"DP03082r001","statement":[{"text":"The IDR characterized in the publication and spanning residues 70–83 in the experimental construct corresponds to region 89-102 of the amino acid sequence.","type":"Curator statement"},{"text":"Adjacent to the C-terminal ends of their ordered parts, both fibril reconstructions show diffuse density (Supplementary Figure 5), indicating that C-terminal tails of the fibril proteins, corresponding to residues 70–83 in the murine and 56–67 in the human fibril proteins, are structurally disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-30T10:05:13.007Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MKLLTSLVFCSLLLGVCHGGFFSFIGEAFQGAGDMWRAYTDMKEAGWKDGDKYFHARGNYDAAQRGPGGVWAAEKISDARESFQEFFGRGHEDTMADQEANRHGRSGKDPNYYRPPGLPAKY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"dataset":[],"UniParc":"UPI0000020FCE","uniref100":"UniRef100_P05367","uniref90":"UniRef90_P05367","uniref50":"UniRef50_P05367","genes":[{"name":{"value":"Saa2","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:98222","url":"http://www.informatics.jax.org/marker/MGI:98222"}}]}}],"alphafold_very_low_content":0,"disorder_content":0.11475409836065574,"disprot_consensus":{"full":[{"start":89,"end":102,"type":"D"}],"Structural state":[{"start":89,"end":102,"type":"D"}]}},{"disprot_id":"DP03083","acc":"Q9VNE4","creator":"lrodriguez","date":"2020-12-29T23:34:19.879Z","features":{"pfam":[],"gene3D":[]},"length":994,"name":"Asterless","ncbi_taxon_id":7227,"organism":"Drosophila melanogaster","regions":[{"start":21,"end":60,"reference_id":"24980795","reference_source":"pmid","reference_html":"Structure of the C. elegans ZYG-1 cryptic polo box suggests a conserved mechanism for centriolar docking of Plk4 kinases. <i> Shimanovskaya E, Viscardi V, Lesigang J, Lettman MM, Qiao R, Svergun DI, Round A, Oegema K, Dong G. </i> Structure, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03083r001","statement":[{"text":"Far-UV circular dichroism (CD) spectra of recombinant acidic regions: CeSPD-2 (aa 11-44), DmAsl (aa 21-60), MmAsl (aa 1-47), and MmSPD-2 (aa 168-256). All acidic regions demonstrated a classical random coil structure with maximum below 0 and minimum at ~200 nm.","type":"Supplementary material"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-30T10:21:30.671Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_12","sequence":"MNTPGISLFQGADALNINSTLDRQEEEEALQDQKRREEELGRIMVNAFDDLLDEENTIDSTTNYQSELEQPPVLPNYPSHPHHKPLQDDAQRANEIEMHRLQILLESKNNELQNVNQVANAAHKKLDDLQKHLSIMQAELDRAIREKQNTHELLVETKETCSNKDSDLDKLRSEKKQLEEDNTRLVGQLEAAKTLLTDVQSKYDMVQASKQKWEERNADLRLKQMEEAHRAQSDLLQQQLCQMKDQLDRKQNELDQINSRYNALQSGHETMLVDKAAKINELSQALDEAQMRCNQLSARPDLQAENRRQQQCIVDLKARIAYLEQTVASLHERLNETTTELDLIDSVIQQHQADESPTSRLSQMGGSRLVGSTPLNPLDRVGHIKQELYRALGNLKNKREEVRRLEKLLEERNQELRVLRDQENQSLVQLETLNEGKMRLENKVKAMQQELEEQKHRSQQESDVHSQLNSIVAERDALREKRQQIEEDLEQLKQQNESLQRNYDQLSQENRQLRTRETADNLRLELERHKILLRDSQSEVERLKKLYSDIATDKESLGYELRKLRESDTLKELQDQRQNLATVQRNLQLAEMKSEELKKLLETEKLSHERDLQALRQRSEREKREEAVAVAKESSENCSKCIESIAEITKAEIQLLKLQNVNSMQAKELKELEHALEQSKNLQAEMQEKIELSNKQDELISDLKERAKQFEAYIRQQEEHKQQNKCTPSPKSNSVSPSDPSPKELTQNRIRLIEQRVRDEMAKLFAAELKRFTNRLQKSEERSQCLQREYQTVCAELQQRQTEVDLLKQTILAERENIDEILAGREEKQKEMLQKCRQELQAKNQRIAELLREVEEQHASIDSERQSMKAVMAQWEKQRQSVDQVEHHWRQQLESLRSTHEEAMRSAQQRYQSAKRTAHNYKLYAEDKEAHMKREYERIKHEYELSLAKIEATMNQHLERRSREKHRDKENVPSNSSSDPITNSNRKPKGNGHS","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"dataset":[],"UniParc":"UPI0000077846","uniref100":"UniRef100_Q9VNE4","uniref90":"UniRef90_Q9VNE4","uniref50":"UniRef50_Q9VNE4","genes":[{"name":{"value":"asl","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF51993.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF51993.2"}},{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0261004","url":"http://flybase.org/reports/FBgn0261004.html"}}]},"synonyms":[{"value":"ASL","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF51993.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF51993.2"}}]},{"value":"Asl","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF51993.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF51993.2"}}]},{"value":"Cep152","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF51993.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF51993.2"}}]},{"value":"DmAsl","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF51993.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF51993.2"}}]},{"value":"Dmel\\CG2919","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF51993.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF51993.2"}}]},{"value":"MecD","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF51993.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF51993.2"}}]},{"value":"mecD","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF51993.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF51993.2"}}]},{"value":"sdu","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF51993.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF51993.2"}}]}],"orfNames":[{"value":"CG2919","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF51993.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF51993.2"}},{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0261004","url":"http://flybase.org/reports/FBgn0261004.html"}}]},{"value":"Dmel_CG2919","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF51993.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF51993.2"}}]}]}],"alphafold_very_low_content":0.14688128772635814,"disorder_content":0.04024144869215292,"disprot_consensus":{"full":[{"start":21,"end":60,"type":"D"}],"Structural state":[{"start":21,"end":60,"type":"D"}]}},{"disprot_id":"DP03085","acc":"Q0PF16","creator":"mpajkos","date":"2020-12-30T11:11:47.674Z","features":{"pfam":[{"id":"PF00622","name":"SPRY domain","start":362,"end":492},{"id":"PF00643","name":"B-box zinc finger","start":93,"end":130},{"id":"PF13445","name":"RING-type zinc-finger","start":15,"end":57}],"gene3D":[]},"length":497,"name":"Tripartite motif-containing protein 5","ncbi_taxon_id":9544,"organism":"Macaca mulatta","regions":[{"start":40,"end":54,"reference_id":"26212332","reference_source":"pmid","reference_html":"RING Dimerization Links Higher-Order Assembly of TRIM5α to Synthesis of K63-Linked Polyubiquitin. <i> Yudina Z, Roa A, Johnson R, Biris N, de Souza Aranha Vieira DA, Tsiperson V, Reszka N, Taylor AB, Hart PJ, Demeler B, Diaz-Griffero F, Ivanov DN. </i> Cell Rep, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"mpajkos","curator_name":"Mátyás Pajkos","curator_orcid":"0000-0001-5791-9825","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4TKP"}],"region_id":"DP03085r001","statement":[{"text":"A segment of the RING domain (amino acids 40–54) that includes most of the central helix is disordered in the crystal and is shown in the figure as a grey backbone trace modeled using the NMR structure of the human TRIM5α RING.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2020-12-30T11:45:40.135Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_06","sequence":"MASGILLNVKEEVTCPICLELLTEPLSLHCGHSFCQACITANHKKSMLYKEGERSCPVCRISYQPENIQPNRHVANIVEKLREVKLSPEEGQKVDHCARHGEKLLLFCQEDSKVICWLCERSQEHRGHHTFLMEEVAQEYHVKLQTALEMLRQKQQEAEKLEADIREEKASWKIQIDYDKTNVSADFEQLREILDWEESNELQNLEKEEEDILKSLTKSETEMVQQTQYMRELISELEHRLQGSMMDLLQGVDGIIKRIENMTLKKPKTFHKNQRRVFRAPDLKGMLDMFRELTDARRYWVDVTLAPNNISHAVIAEDKRQVSSRNPQIMYQAPGTLFTFPSLTNFNYCTGVLGSQSITSGKHYWEVDVSKKSAWILGVCAGFQSDAMYNIEQNENYQPKYGYWVIGLQEGVKYSVFQDGSSHTPFAPFIVPLSVIICPDRVGVFVDYEACTVSFFNITNHGFLIYKFSQCSFSKPVFPYLNPRKCTVPMTLCSPSS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Cercopithecidae","Cercopithecinae","Macaca"],"dataset":[],"UniParc":"UPI0000DB12B9","uniref100":"UniRef100_Q0PF16","uniref90":"UniRef90_Q0PF16","uniref50":"UniRef50_Q0PF16","genes":[{"name":{"value":"TRIM5"}}],"alphafold_very_low_content":0.0744466800804829,"disorder_content":0.030181086519114688,"disprot_consensus":{"full":[{"start":40,"end":54,"type":"D"}],"Structural state":[{"start":40,"end":54,"type":"D"}]}},{"disprot_id":"DP03088","acc":"Q9BV68","creator":"mpajkos","date":"2021-01-04T11:27:29.587Z","features":{"pfam":[{"id":"PF13639","name":"Ring finger domain","start":228,"end":270},{"id":"PF14369","name":"zinc-ribbon","start":10,"end":40}],"gene3D":[]},"length":311,"name":"E3 ubiquitin-protein ligase RNF126","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":41,"end":66,"reference_id":"27193484","reference_source":"pmid","reference_html":"Structural and functional insights into the E3 ligase, RNF126. <i> Krysztofinska EM, Martínez-Lumbreras S, Thapaliya A, Evans NJ, High S, Isaacson RL. </i> Sci Rep, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"mpajkos","curator_name":"Mátyás Pajkos","curator_orcid":"0000-0001-5791-9825","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"2N9O"}],"region_id":"DP03088r001","statement":[{"text":"Backbone assignment of residues 1–66 shows that residues 1–40 constitute the structured region while the remainder presents the chemical shift dispersion typical of disordered proteins.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-04T13:36:22.908Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_12","sequence":"MAEASPHPGRYFCHCCSVEIVPRLPDYICPRCESGFIEELPEETRSTENGSAPSTAPTDQSRPPLEHVDQHLFTLPQGYGQFAFGIFDDSFEIPTFPPGAQADDGRDPESRRERDHPSRHRYGARQPRARLTTRRATGRHEGVPTLEGIIQQLVNGIITPATIPSLGPWGVLHSNPMDYAWGANGLDAIITQLLNQFENTGPPPADKEKIQALPTVPVTEEHVGSGLECPVCKDDYALGERVRQLPCNHLFHDGCIVPWLEQHDSCPVCRKSLTGQNTATNPPGLTGVSFSSSSSSSSSSSPSNENATSNS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI0000073A73","uniref100":"UniRef100_Q9BV68","uniref90":"UniRef90_Q9BV68","uniref50":"UniRef50_Q9BV68","genes":[{"name":{"value":"RNF126","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:21151","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:21151"}}]}}],"alphafold_very_low_content":0.36012861736334406,"disorder_content":0.08360128617363344,"disprot_consensus":{"full":[{"start":41,"end":66,"type":"D"}],"Structural state":[{"start":41,"end":66,"type":"D"}]}},{"disprot_id":"DP03090","acc":"Q20363","creator":"ashenoy","date":"2021-01-04T13:00:10.645Z","features":{"pfam":[{"id":"PF00011","name":"Hsp20/alpha crystallin family","start":46,"end":138}],"gene3D":[]},"length":159,"name":"Stress-induced protein 1","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":1,"end":17,"reference_id":"26009280","reference_source":"pmid","reference_html":"The Chaperone Activity of the Developmental Small Heat Shock Protein Sip1 Is Regulated by pH-Dependent Conformational Changes. <i> Fleckenstein T, Kastenmüller A, Stein ML, Peters C, Daake M, Krause M, Weinfurtner D, Haslbeck M, Weinkauf S, Groll M, Buchner J. </i> Mol Cell, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"ashenoy","curator_name":"Aditi Shenoy","curator_orcid":"0000-0001-7748-2501","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4YDZ"}],"region_id":"DP03090r001","statement":[{"text":"Interestingly, the flexible N- and C-terminal regions of Sip1 are resolved to a large extent in the equatorial monomers with only 7 C- and 17 N-terminal residues missing, respectively (Figures 4C and 4D). ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-01T11:58:57.834Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MSSLCPYTGRPTGLFRDFEDMMPYWAQRHSMLNNFNNIVPQQLNEVENTAQKFCVKLDVAAFKPEELKVNLEGHVLTIEGHHEVKTEHGFSKRSFTRQFTLPKDVDLAHIHTVINKEGQMTIDAPKTGSNTTVRALPIHTSAGHAVTQKPSSTTTTGKH","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"dataset":[],"UniParc":"UPI0000082588","uniref100":"UniRef100_Q20363","uniref90":"UniRef90_Q20363","uniref50":"UniRef50_Q20363","genes":[{"name":{"value":"sip-1","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"CAA84703.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA84703.1"}}]},"orfNames":[{"value":"F43D9.4"}]}],"alphafold_very_low_content":0.09433962264150944,"disorder_content":0.1069182389937107,"disprot_consensus":{"full":[{"start":1,"end":17,"type":"D"}],"Structural state":[{"start":1,"end":17,"type":"D"}]}},{"disprot_id":"DP03091","acc":"P0AG86","creator":"vpromp","date":"2021-01-04T13:27:46.955Z","features":{"pfam":[{"id":"PF02556","name":"Preprotein translocase subunit SecB","start":5,"end":144}],"gene3D":[]},"length":155,"name":"Protein-export protein SecB","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":143,"end":155,"reference_id":"10544036","reference_source":"pmid","reference_html":"A highly mobile C-terminal tail of the Escherichia coli protein export chaperone SecB. <i> Volkert TL, Baleja JD, Kumamoto CA. </i> Biochem Biophys Res Commun, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"vpromp","curator_name":"Vasilis J Promponas","curator_orcid":"0000-0003-3352-4831","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03091r001","statement":[{"text":"In this study, the C-terminal thirteen amino acid residues of SecB were shown to be highly mobile.","type":"Introduction"},{"text":"The 1H NMR resonances of these thirteen C-terminal amino acid residues (Q143QAGEGTEEHQDA155) had narrow linewidths, and appeared at positions corresponding to random chemical shift values (Wuthrich, 1986). Therefore, these amino acid residues represent a mobile C-terminal tail of SecB.","type":"Results"},{"text":"In this study, it was demonstrated that SecB contains a highly mobile C-terminal region and that deletion of the C-terminal tail produced a stable truncated protein that was defective in its function under certain conditions. The 1H NMR spectrum of wild type SecB contained narrow resonances most of which could be assigned to the C-terminal thirteen amino acid residues of SecB.","type":"Discussion"},{"text":"In this study, we demonstrate that the C-terminal 13 residues of SecB were highly mobile using 1H NMR spectroscopy.","type":"Abstract"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-04T16:10:22.097Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":143,"end":155,"reference_id":"10544036","reference_source":"pmid","reference_html":"A highly mobile C-terminal tail of the Escherichia coli protein export chaperone SecB. <i> Volkert TL, Baleja JD, Kumamoto CA. </i> Biochem Biophys Res Commun, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"vpromp","curator_name":"Vasilis J Promponas","curator_orcid":"0000-0003-3352-4831","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03091r002","statement":[{"text":"A protein lacking the C-terminal 13 amino acids of wild-type SecB was found to retain the ability to bind unfolded maltose-binding protein (MBP) in vitro but to interfere with the normal kinetics of pre-MBP export when overexpressed in vivo.","type":"Abstract"},{"text":"Deletion of the C-terminal mobile region of SecB was found to alter the function of SecB when the mutant protein was overproduced and overproduction of SecA reversed this defect.","type":"Introduction"},{"text":"When SecB142 lacking the C-terminal mobile region was expressed at high levels, a kinetic defect in the export of pre-MBP was observed, demonstrating that removal of the mobile region altered the function of SecB. Despite the truncation, SecB142 was capable of binding pre-MBP as demonstrated by its ability to block the refolding of unfolded MBP.","type":"Discussion"},{"text":"In vitro experiments (intrinsic tryptophan fluorescence), monitoring MBP(Y283D) refolding in the presence of SecB (wt or SecB142). Results displayed in Figure 2.","type":"Curator statement"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":143,"end":155,"reference_id":"10544036","reference_source":"pmid","reference_html":"A highly mobile C-terminal tail of the Escherichia coli protein export chaperone SecB. <i> Volkert TL, Baleja JD, Kumamoto CA. </i> Biochem Biophys Res Commun, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"vpromp","curator_name":"Vasilis J Promponas","curator_orcid":"0000-0003-3352-4831","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03091r003","statement":[{"text":"Deletion of the C-terminal mobile region of SecB was found to alter the function of SecB when the mutant protein was overproduced and overproduction of SecA reversed this defect.","type":"Abstract"},{"text":"As shown in Fig. 3A, pre-MBP export was severely defective in secB- strains containing vector only. In contrast, export was rapid in the same strain transformed with wild type secB on the overproducing plasmid. When the strain was transformed with the plasmid containing the secB142op mutation, a moderate export defect was observed. Pre-MBP export in the psecB142op containing strain exhibited the kinetics typically seen for other secB missense mutations (36, 37).","type":"Results"},{"text":"In Fig. 3B, the same set of plasmids were transformed into a strain containing a chromosomal secB+ allele. As expected, export was rapid in the strains containing wild type secB and a mild defect was evident in the strain containing secB+ on the overproducing plasmid. When the plasmid containing the secB142op mutation was transformed into the secB+ strain, a dominant negative export defect was observed. ","type":"Results"},{"text":"As seen in Fig. 3C, when SecA was overexpressed in a secB1- strain both the mild export defect due to wild type SecB overproduction, and the moderate defect of the secB142op mutation were suppressed. This result suggests that SecA levels were limiting in the presence of excess SecB and that this effect was more pronounced with the secB142op mutation.","type":"Results"},{"text":"In vivo experiments to determine whether SecB142 was functional: \"pre- maltose binding protein (pre-MBP) export was analyzed by pulse-chase labeling of cells with Tran[35S]- label (ICN), extraction and immunoprecipitation with anti-MBP anti-serum. MBP species were analyzed by SDS polyacrylamide gel electrophoresis and fluorography.\"","type":"Curator statement"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":143,"end":153,"reference_id":"14643199","reference_source":"pmid","reference_html":"Crystal structure of SecB from Escherichia coli. <i> Dekker C, de Kruijff B, Gros P. </i> J Struct Biol, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"vpromp","curator_name":"Vasilis J Promponas","curator_orcid":"0000-0003-3352-4831","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1QYN"}],"region_id":"DP03091r004","statement":[{"text":"The model is not complete, as 8N-terminal residues and 11 C-terminal residues are not visible in the electron density maps. ","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":4,"released":"2021_12","sequence":"MSEQNNTEMTFQIQRIYTKDISFEAPNAPHVFQKDWQPEVKLDLDTASSQLADDVYEVVLRVTVTASLGEETAFLCEVQQGGIFSIAGIEGTQMAHCLGAYCPNILFPYARECITSMVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGTEEHQDA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":[],"UniParc":"UPI000013577D","uniref100":"UniRef100_A7ZTG3","uniref90":"UniRef90_A8ARJ6","uniref50":"UniRef50_Q8KRM2","genes":[{"name":{"value":"secB"},"olnNames":[{"value":"b3609"},{"value":"JW3584"}]}],"alphafold_very_low_content":0.07741935483870968,"disorder_content":0.08387096774193549,"disprot_consensus":{"full":[{"start":143,"end":155,"type":"D"}],"Structural state":[{"start":143,"end":155,"type":"D"}],"Biological process":[{"start":143,"end":155,"type":"F"}]}},{"disprot_id":"DP03092","acc":"O00308","creator":"mpajkos","date":"2021-01-04T14:46:50.734Z","features":{"pfam":[{"id":"PF00397","name":"WW domain","start":302,"end":331},{"id":"PF00397","name":"WW domain","start":332,"end":361},{"id":"PF00397","name":"WW domain","start":407,"end":435},{"id":"PF00397","name":"WW domain","start":446,"end":475},{"id":"PF00632","name":"HECT-domain (ubiquitin-transferase)","start":566,"end":868}],"gene3D":[]},"length":870,"name":"NEDD4-like E3 ubiquitin-protein ligase WWP2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":662,"end":702,"reference_id":"26457515","reference_source":"pmid","reference_html":"Structure of the HECT domain of human WWP2. <i> Gong W, Zhang X, Zhang W, Li J, Li Z. </i> Acta Crystallogr F Struct Biol Commun, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"mpajkos","curator_name":"Mátyás Pajkos","curator_orcid":"0000-0001-5791-9825","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4Y07"}],"region_id":"DP03092r001","statement":[{"text":"Notably, residues 661–702 of WWP2 were not built in the model owing to a lack of electron density, which might be the result of intrinsic flexibility","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-04T16:08:20.201Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_06","sequence":"MASASSSRAGVALPFEKSQLTLKVVSAKPKVHNRQPRINSYVEVAVDGLPSETKKTGKRIGSSELLWNEIIILNVTAQSHLDLKVWSCHTLRNELLGTASVNLSNVLKNNGGKMENMQLTLNLQTENKGSVVSGGELTIFLDGPTVDLGNVPNGSALTDGSQLPSRDSSGTAVAPENRHQPPSTNCFGGRSRTHRHSGASARTTPATGEQSPGARSRHRQPVKNSGHSGLANGTVNDEPTTATDPEEPSVVGVTSPPAAPLSVTPNPNTTSLPAPATPAEGEEPSTSGTQQLPAAAQAPDALPAGWEQRELPNGRVYYVDHNTKTTTWERPLPPGWEKRTDPRGRFYYVDHNTRTTTWQRPTAEYVRNYEQWQSQRNQLQGAMQHFSQRFLYQSSSASTDHDPLGPLPPGWEKRQDNGRVYYVNHNTRTTQWEDPRTQGMIQEPALPPGWEMKYTSEGVRYFVDHNTRTTTFKDPRPGFESGTKQGSPGAYDRSFRWKYHQFRFLCHSNALPSHVKISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKRPTLKDLESIDPEFYNSIVWIKENNLEECGLELYFIQDMEILGKVTTHELKEGGESIRVTEENKEEYIMLLTDWRFTRGVEEQTKAFLDGFNEVAPLEWLRYFDEKELELMLCGMQEIDMSDWQKSTIYRHYTKNSKQIQWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELIGSNGPQKFCIDKVGKETWLPRSHTCFNRLDLPPYKSYEQLREKLLYAIEETEGFGQE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000006E5A2","uniref100":"UniRef100_O00308","uniref90":"UniRef90_O00308","uniref50":"UniRef50_O00308","genes":[{"name":{"value":"WWP2"}}],"alphafold_very_low_content":0.21724137931034482,"disorder_content":0.047126436781609195,"disprot_consensus":{"full":[{"start":662,"end":702,"type":"D"}],"Structural state":[{"start":662,"end":702,"type":"D"}]}},{"disprot_id":"DP03093","acc":"Q9SSN3","creator":"viglesias","date":"2021-01-04T14:47:51.247Z","features":{"pfam":[{"id":"PF01582","name":"TIR domain","start":8,"end":172}],"gene3D":[]},"length":176,"name":"Toll/interleukin-1 receptor-like protein","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":45,"end":58,"reference_id":"19845004","reference_source":"pmid","reference_html":"The crystal structure of a TIR domain from Arabidopsis thaliana reveals a conserved helical region unique to plants. <i> Chan SL, Mukasa T, Santelli E, Low LY, Pascual J. </i> Protein Sci, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3JRN"}],"region_id":"DP03093r001","statement":[{"text":"The electron density for the region between residues 45 and 58 was not observed and therefore not modeled.","type":"Figure"},{"text":"Electron density between residues 45 and 58, comprising the BB‐loop and αB‐helix, was not observed and therefore not modeled. ","type":"Results"},{"text":" Incidentally, the electron density corresponding to the BB‐loop residues of AtTIR was not visible, probably because of the intrinsic flexibility of this particular sequence.","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-04T16:30:18.983Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MSSHTATKYDVFLSFRGHDTRHNFISFLYKELVRRSIRTFKDDKELENGQRFSPELKSPIEVSRFAVVVVSENYAASSWCLDELVTIMDFEKKGSITVMPIFYGVEPNHVRWQTGVLAEQFKKHASREDPEKVLKWRQALTNFAQLSGDCSGDDDSKLVDKIANEISNKKTIYATI","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"dataset":[],"UniParc":"UPI00000A1B32","uniref100":"UniRef100_Q9SSN3","uniref90":"UniRef90_Q9SSN3","uniref50":"UniRef50_Q9SSN3","genes":[{"name":{"value":"TIR"},"orfNames":[{"value":"F3N23.13"}],"olnNames":[{"value":"At1g72930"}]}],"alphafold_very_low_content":0.03409090909090909,"disorder_content":0.07954545454545454,"disprot_consensus":{"full":[{"start":45,"end":58,"type":"D"}],"Structural state":[{"start":45,"end":58,"type":"D"}]}},{"disprot_id":"DP03094","acc":"Q9SEL7","creator":"viglesias","date":"2021-01-04T15:14:21.286Z","features":{"pfam":[{"id":"PF13365","name":"Trypsin-like peptidase domain","start":131,"end":280}],"gene3D":[]},"length":323,"name":"Protease Do-like 5, chloroplastic","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":111,"end":127,"reference_id":"23633592","reference_source":"pmid","reference_html":"The structures of Arabidopsis Deg5 and Deg8 reveal new insights into HtrA proteases. <i> Sun W, Gao F, Fan H, Shan X, Sun R, Liu L, Gong W. </i> Acta Crystallogr D Biol Crystallogr, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4IC5"}],"region_id":"DP03094r001","statement":[{"text":"In Deg5 (S266A), residues 111–125 from loop LA, 155–159 from loop LB and 287–295 from loop L2 cannot be traced in the electron-density map. These loops, together with loop L3 (241–251), which has significantly high B-factor values, are flexible in the crystal.","type":"Results"},{"text":"A few additional residues are invisible in the electron density map","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":286,"end":295,"reference_id":"23633592","reference_source":"pmid","reference_html":"The structures of Arabidopsis Deg5 and Deg8 reveal new insights into HtrA proteases. <i> Sun W, Gao F, Fan H, Shan X, Sun R, Liu L, Gong W. </i> Acta Crystallogr D Biol Crystallogr, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03094r002","statement":[{"text":"In Deg5 (S266A), residues 111–125 from loop LA, 155–159 from loop LB and 287–295 from loop L2 cannot be traced in the electron-density map. These loops, together with loop L3 (241–251), which has significantly high B-factor values, are flexible in the crystal.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"4IC5"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MTMALASSKAFSSIFNTLSPINQSKFVLACSGSNHVDVIDRRRRIMIFGSSLALTSSLLGSNQQRLPMESAIALEQFKEKEEELEEEEERNVNLFQKTSPSVVYIEAIELPKTSSGDILTDEENGKIEGTGSGFVWDKLGHIVTNYHVIAKLATDQFGLQRCKVSLVDAKGTRFSKEGKIVGLDPDNDLAVLKIETEGRELNPVVLGTSNDLRVGQSCFAIGNPYGYENTLTIGVVSGLGREIPSPNGKSISEAIQTDADINSGNSGGPLLDSYGHTIGVNTATFTRKGSGMSSGVNFAIPIDTVVRTVPYLIVYGTAYRDRF","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"dataset":[],"UniParc":"UPI000016D987","uniref100":"UniRef100_Q9SEL7","uniref90":"UniRef90_Q9SEL7","uniref50":"UniRef50_Q9SEL7","genes":[{"name":{"value":"DEGP5"},"synonyms":[{"value":"HHOA"}],"orfNames":[{"value":"F28J12.30"}],"olnNames":[{"value":"At4g18370"}]}],"alphafold_very_low_content":0.20743034055727555,"disorder_content":0.08359133126934984,"disprot_consensus":{"full":[{"start":111,"end":127,"type":"D"},{"start":286,"end":295,"type":"D"}],"Structural state":[{"start":111,"end":127,"type":"D"},{"start":286,"end":295,"type":"D"}]}},{"disprot_id":"DP03096","acc":"O04147","creator":"viglesias","date":"2021-01-04T16:23:01.473Z","features":{"pfam":[{"id":"PF07823","name":"Cyclic phosphodiesterase-like protein","start":10,"end":150}],"gene3D":[]},"length":181,"name":"Cyclic phosphodiesterase","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":103,"end":113,"reference_id":"11080166","reference_source":"pmid","reference_html":"Structure and mechanism of activity of the cyclic phosphodiesterase of Appr>p, a product of the tRNA splicing reaction. <i> Hofmann A, Zdanov A, Genschik P, Ruvinov S, Filipowicz W, Wlodawer A. </i> EMBO J, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"1FSI"}],"region_id":"DP03096r001","statement":[{"text":"It is noteworthy that an exposed surface loop connecting α3 and β5 (residues 101–115) is positioned in the immediate vicinity of the active site. The loop is poorly defined in the present structure, most likely due to the inherent flexibility of this region. It is highly disordered and could not be traced at all in molecules 2 and 3. ","type":"Results"},{"text":"The averaged density allowed building of all three molecules in the asymmetric unit, with the exception of a surface loop constituted by residues 100–115.","type":"Results"},{"text":"A solvent-exposed surface loop (residues 100–115) is very likely to play a flap-like role, opening and closing the active site.","type":"Abstract"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-28T08:57:26.375Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_12","sequence":"MEEVKKDVYSVWALPDEESEPRFKKLMEALRSEFTGPRFVPHVTVAVSAYLTADEAKKMFESACDGLKAYTATVDRVSTGTFFFQCVFLLLQTTPEVMEAGEHCKNHFNCSTTTPYMPHLSLLYAELTEEEKKNAQEKAYTLDSSLDGLSFRLNRLALCKTDTEDKTLETWETVAVCNLNP","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"dataset":[],"UniParc":"UPI00000AD028","uniref100":"UniRef100_O04147","uniref90":"UniRef90_O04147","uniref50":"UniRef50_O04147","genes":[{"orfNames":[{"value":"F13C5.100"},{"value":"F13C5_100"}],"olnNames":[{"value":"At4g18930"}]}],"alphafold_very_low_content":0,"disorder_content":0.06077348066298342,"disprot_consensus":{"full":[{"start":103,"end":113,"type":"D"}],"Structural state":[{"start":103,"end":113,"type":"D"}]}},{"disprot_id":"DP03098","acc":"P02774","creator":"msalas","date":"2021-01-04T19:24:28.846Z","features":{"pfam":[{"id":"PF00273","name":"Serum albumin family","start":27,"end":199},{"id":"PF00273","name":"Serum albumin family","start":219,"end":385},{"id":"PF09164","name":"Vitamin D binding protein, domain III","start":405,"end":469}],"gene3D":[]},"length":474,"name":"Vitamin D-binding protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":107,"end":125,"reference_id":"12048248","reference_source":"pmid","reference_html":"Crystal structures of the vitamin D-binding protein and its complex with actin: structural basis of the actin-scavenger system. <i> Otterbein LR, Cosio C, Graceffa P, Dominguez R. </i> Proc Natl Acad Sci U S A, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"msalas","curator_name":"Martin Salas","curator_orcid":"0000-0001-6352-1282","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1KW2"},{"db":"PDB","id":"1KXP"}],"region_id":"DP03098r001","statement":[{"text":"The IDR characterized in the PDB and spanning residues 91-109 corresponds to region 107-125 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-16) that is missing in the mature protein.","type":"Curator statement"},{"text":"Not included in the final model are a few flexible regions that are poorly defined in the electron density maps, which include actin residues Asp-1–Asp-3, His-40–Asp-51, and Ala-365–Ala-375, DBP residues Gly-107–Ala-125, and the C-terminal Leu-474.","type":"Results"},{"text":"Limited Structural Changes After Formation of the Actin–DBP Complex. ","type":"Results"},{"text":"The structure of DBP shows only minor changes after formation of the actin–DBP complex.","type":"Results"},{"text":"Formation of the strong actin–DBP complex proceeds with limited conformational changes to both proteins, demonstrating how DBP has evolved to become an effective actin-scavenger protein.","type":"Abstract"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":107,"end":127,"reference_id":"12119014","reference_source":"pmid","reference_html":"Crystal structure of the complex between actin and human vitamin D-binding protein at 2.5 A resolution. <i> Head JF, Swamy N, Ray R. </i> Biochemistry, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"msalas","curator_name":"Martin Salas","curator_orcid":"0000-0001-6352-1282","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1LOT"}],"region_id":"DP03098r002","statement":[{"text":"The IDR characterized in the publication and spanning residues 91-111 corresponds to region 107-127 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-16) that is missing in the mature protein.","type":"Curator statement"},{"text":"DBP residues 91-111 and actin residues 1, 2, 40-50, 374, and 375 appear to be disordered in this structure and are absent from the model.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T12:14:14.829Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MKRVLVLLLAVAFGHALERGRDYEKNKVCKEFSHLGKEDFTSLSLVLYSRKFPSGTFEQVSQLVKEVVSLTEACCAEGADPDCYDTRTSALSAKSCESNSPFPVHPGTAECCTKEGLERKLCMAALKHQPQEFPTYVEPTNDEICEAFRKDPKEYANQFMWEYSTNYGQAPLSLLVSYTKSYLSMVGSCCTSASPTVCFLKERLQLKHLSLLTTLSNRVCSQYAAYGEKKSRLSNLIKLAQKVPTADLEDVLPLAEDITNILSKCCESASEDCMAKELPEHTVKLCDNLSTKNSKFEDCCQEKTAMDVFVCTYFMPAAQLPELPDVELPTNKDVCDPGNTKVMDKYTFELSRRTHLPEVFLSKVLEPTLKSLGECCDVEDSTTCFNAKGPLLKKELSSFIDKGQELCADYSENTFTEYKKKLAERLKAKLPDATPTELAKLVNKHSDFASNCCSINSPPLYCDSEIDAELKNIL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000013D9E0","uniref100":"UniRef100_P02774","uniref90":"UniRef90_P02774","uniref50":"UniRef50_P02774","genes":[{"name":{"value":"GC"}}],"alphafold_very_low_content":0.0379746835443038,"disorder_content":0.04430379746835443,"disprot_consensus":{"full":[{"start":107,"end":127,"type":"D"}],"Structural state":[{"start":107,"end":127,"type":"D"}]}},{"disprot_id":"DP03099","acc":"P68135","creator":"msalas","date":"2021-01-04T20:59:38.479Z","features":{"pfam":[{"id":"PF00022","name":"Actin","start":5,"end":377}],"gene3D":[]},"length":377,"name":"Actin, alpha skeletal muscle","ncbi_taxon_id":9986,"organism":"Oryctolagus cuniculus","regions":[{"start":41,"end":53,"reference_id":"12048248","reference_source":"pmid","reference_html":"Crystal structures of the vitamin D-binding protein and its complex with actin: structural basis of the actin-scavenger system. <i> Otterbein LR, Cosio C, Graceffa P, Dominguez R. </i> Proc Natl Acad Sci U S A, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"msalas","curator_name":"Martin Salas","curator_orcid":"0000-0001-6352-1282","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1KXP"}],"region_id":"DP03099r001","statement":[{"text":"The IDR characterized in the publication and spanning residues 40–51 corresponds to region 41-53 of the amino acid sequence, as it includes a few more residues invisible in the electron density map.","type":"Curator statement"},{"text":"Not included in the final model are a few flexible regions that are poorly defined in the electron density maps, which include actin residues Asp-1–Asp-3, His-40–Asp-51, and Ala-365–Ala-375, DBP residues Gly-107–Ala-125, and the C-terminal Leu-474.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-05T08:40:40.331Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":367,"end":377,"reference_id":"12048248","reference_source":"pmid","reference_html":"Crystal structures of the vitamin D-binding protein and its complex with actin: structural basis of the actin-scavenger system. <i> Otterbein LR, Cosio C, Graceffa P, Dominguez R. </i> Proc Natl Acad Sci U S A, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"msalas","curator_name":"Martin Salas","curator_orcid":"0000-0001-6352-1282","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1KXP"}],"region_id":"DP03099r002","statement":[{"text":"The IDR characterized in the publication and spanning residues 365-375 corresponds to region 367-377 of the amino acid sequence, as it includes a few more residues invisible in the electron density map.","type":"Curator statement"},{"text":"Not included in the final model are a few flexible regions that are poorly defined in the electron density maps, which include actin residues Asp-1–Asp-3, His-40–Asp-51, and Ala-365–Ala-375, DBP residues Gly-107–Ala-125, and the C-terminal Leu-474.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-05T08:40:41.165Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":42,"end":52,"reference_id":"12119014","reference_source":"pmid","reference_html":"Crystal structure of the complex between actin and human vitamin D-binding protein at 2.5 A resolution. <i> Head JF, Swamy N, Ray R. </i> Biochemistry, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"msalas","curator_name":"Martin Salas","curator_orcid":"0000-0001-6352-1282","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1LOT"}],"region_id":"DP03099r003","statement":[{"text":"The IDR characterized in the publication and spanning residues 40-50 corresponds to region 42-52 of the amino acid sequence, as it includes a few more residues invisible in the electron density map.","type":"Curator statement"},{"text":"DBP residues 91-111 and actin residues 1, 2, 40-50, 374, and 375 appear to be disordered in this structure and are absent from the model.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T12:15:37.387Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2021_12","sequence":"MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHRKCF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Lagomorpha","Leporidae","Oryctolagus"],"dataset":[],"UniParc":"UPI0000000860","uniref100":"UniRef100_P68133","uniref90":"UniRef90_P68133","uniref50":"UniRef50_P68133","genes":[{"name":{"value":"ACTA1"},"synonyms":[{"value":"ACTA"}]}],"alphafold_very_low_content":0.010610079575596816,"disorder_content":0.0636604774535809,"disprot_consensus":{"full":[{"start":41,"end":53,"type":"D"},{"start":367,"end":377,"type":"D"}],"Structural state":[{"start":41,"end":53,"type":"D"},{"start":367,"end":377,"type":"D"}]}},{"disprot_id":"DP03100","acc":"Q14258","creator":"mpajkos","date":"2021-01-05T14:30:57.558Z","features":{"pfam":[{"id":"PF00622","name":"SPRY domain","start":512,"end":623},{"id":"PF13445","name":"RING-type zinc-finger","start":13,"end":51},{"id":"PF13765","name":"SPRY-associated domain","start":459,"end":506},{"id":"PF25600","name":"TRIM protein coiled-coil region","start":217,"end":350}],"gene3D":[]},"length":630,"name":"E3 ubiquitin/ISG15 ligase TRIM25","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":361,"end":433,"reference_id":"29739942","reference_source":"pmid","reference_html":"Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition. <i> Koliopoulos MG, Lethier M, van der Veen AG, Haubrich K, Hennig J, Kowalinski E, Stevens RV, Martin SR, Reis e Sousa C, Cusack S, Rittinger K. </i> Nat Commun, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"mpajkos","curator_name":"Mátyás Pajkos","curator_orcid":"0000-0001-5791-9825","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6FLN"}],"region_id":"DP03100r001","statement":[{"text":"The 73-residue long linker (residues 361–433) connecting the CC and PRYSPRY domain is not visible in the electron density so the exact connectivity is uncertain","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-05T15:34:20.248Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":361,"end":433,"reference_id":"29739942","reference_source":"pmid","reference_html":"Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition. <i> Koliopoulos MG, Lethier M, van der Veen AG, Haubrich K, Hennig J, Kowalinski E, Stevens RV, Martin SR, Reis e Sousa C, Cusack S, Rittinger K. </i> Nat Commun, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"mpajkos","curator_name":"Mátyás Pajkos","curator_orcid":"0000-0001-5791-9825","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"6FLN"}],"region_id":"DP03100r002","statement":[{"text":"The 73-residue long linker (residues 361–433) connecting the CC and PRYSPRY domain is not visible in the electron density so the exact connectivity is uncertain","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-05T15:34:20.923Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":2,"released":"2021_06","sequence":"MAELCPLAEELSCSICLEPFKEPVTTPCGHNFCGSCLNETWAVQGSPYLCPQCRAVYQARPQLHKNTVLCNVVEQFLQADLAREPPADVWTPPARASAPSPNAQVACDHCLKEAAVKTCLVCMASFCQEHLQPHFDSPAFQDHPLQPPVRDLLRRKCSQHNRLREFFCPEHSECICHICLVEHKTCSPASLSQASADLEATLRHKLTVMYSQINGASRALDDVRNRQQDVRMTANRKVEQLQQEYTEMKALLDASETTSTRKIKEEEKRVNSKFDTIYQILLKKKSEIQTLKEEIEQSLTKRDEFEFLEKASKLRGISTKPVYIPEVELNHKLIKGIHQSTIDLKNELKQCIGRLQEPTPSSGDPGEHDPASTHKSTRPVKKVSKEEKKSKKPPPVPALPSKLPTFGAPEQLVDLKQAGLEAAAKATSSHPNSTSLKAKVLETFLAKSRPELLEYYIKVILDYNTAHNKVALSECYTVASVAEMPQNYRPHPQRFTYCSQVLGLHCYKKGIHYWEVELQKNNFCGVGICYGSMNRQGPESRLGRNSASWCVEWFNTKISAWHNNVEKTLPSTKATRVGVLLNCDHGFVIFFAVADKVHLMYKFRVDFTEALYPAFWVFSAGATLSICSPK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI00001AE6B8","uniref100":"UniRef100_Q14258","uniref90":"UniRef90_Q14258","uniref50":"UniRef50_Q14258","genes":[{"name":{"value":"TRIM25"},"synonyms":[{"value":"EFP","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8248217","url":"http://www.ncbi.nlm.nih.gov/pubmed/8248217","alternativeUrl":"https://europepmc.org/abstract/MED/8248217"}}]},{"value":"RNF147"},{"value":"ZNF147"}]}],"alphafold_very_low_content":0.14603174603174604,"disorder_content":0.11587301587301588,"disprot_consensus":{"full":[{"start":361,"end":433,"type":"D"}],"Structural state":[{"start":361,"end":433,"type":"D"}],"Disorder function":[{"start":361,"end":433,"type":"F"}]}},{"disprot_id":"DP03101","acc":"O15344","creator":"mpajkos","date":"2021-01-05T17:19:55.830Z","features":{"pfam":[{"id":"PF00041","name":"Fibronectin type III domain","start":393,"end":475},{"id":"PF00622","name":"SPRY domain","start":540,"end":654},{"id":"PF00643","name":"B-box zinc finger","start":174,"end":210},{"id":"PF13445","name":"RING-type zinc-finger","start":10,"end":57},{"id":"PF18568","name":"TRIM C-terminal subgroup One Signature domain","start":323,"end":374},{"id":"PF22586","name":"ANCHR-like B-box zinc-binding domain","start":118,"end":160}],"gene3D":[]},"length":667,"name":"E3 ubiquitin-protein ligase Midline-1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":87,"end":116,"reference_id":"16529770","reference_source":"pmid","reference_html":"Solution structure of the RBCC/TRIM B-box1 domain of human MID1: B-box with a RING. <i> Massiah MA, Simmons BN, Short KM, Cox TC. </i> J Mol Biol, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"mpajkos","curator_name":"Mátyás Pajkos","curator_orcid":"0000-0001-5791-9825","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"cross_refs":[{"db":"PDB","id":"2FFW"},{"db":"BMRB","id":"6920"}],"region_id":"DP03101r001","statement":[{"text":"The NH signals for the first 30 amino acid residues were less dispersed and located centrally within the spectrum with less than 1 ppm and 5 ppm signal dispersion in the 1H and 15N resonances, respectively. This indicated that these residues were most likely unstructured.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-07T21:00:59.855Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":87,"end":116,"reference_id":"16529770","reference_source":"pmid","reference_html":"Solution structure of the RBCC/TRIM B-box1 domain of human MID1: B-box with a RING. <i> Massiah MA, Simmons BN, Short KM, Cox TC. </i> J Mol Biol, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"mpajkos","curator_name":"Mátyás Pajkos","curator_orcid":"0000-0001-5791-9825","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":3,"region_id":"DP03101r002","statement":[{"text":"The 78 native amino acid residues comprised the 48 amino acid region defining the B-box1 motif and an additional 30 residues from the N-terminal linker that joined the RING and B-box1 sequences","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-07T21:01:02.909Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":2,"released":"2023_06","sequence":"METLESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATNESVESITAFQCPTCRHVITLSQRGLDGLKRNVTLQNIIDRFQKASVSGPNSPSETRRERAFDANTMTSAEKVLCQFCDQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEPIPDSHIRGLMCLEHEDEKVNMYCVTDDQLICALCKLVGRHRDHQVAALSERYDKLKQNLESNLTNLIKRNTELETLLAKLIQTCQHVEVNASRQEAKLTEECDLLIEIIQQRRQIIGTKIKEGKVMRLRKLAQQIANCKQCIERSASLISQAEHSLKENDHARFLQTAKNITERVSMATASSQVLIPEINLNDTFDTFALDFSREKKLLECLDYLTAPNPPTIREELCTASYDTITVHWTSDDEFSVVSYELQYTIFTGQANVVSLCNSADSWMIVPNIKQNHYTVHGLQSGTKYIFMVKAINQAGSRSSEPGKLKTNSQPFKLDPKSAHRKLKVSHDNLTVERDESSSKKSHTPERFTSQGSYGVAGNVFIDSGRHYWEVVISGSTWYAIGLAYKSAPKHEWIGKNSASWALCRCNNNWVVRHNSKEIPIEPAPHLRRVGILLDYDNGSIAFYDALNSIHLYTFDVAFAQPVCPTFTVWNKCLTIITGLPIPDHLDCTEQLP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"UniParc":"UPI000012F0E6","uniref100":"UniRef100_O15344","uniref90":"UniRef90_O15344","uniref50":"UniRef50_O15344","genes":[{"name":{"value":"MID1"},"synonyms":[{"value":"FXY"},{"value":"RNF59"},{"value":"TRIM18"},{"value":"XPRF"}]}],"alphafold_very_low_content":0.047976011994003,"disorder_content":0.044977511244377814,"disprot_consensus":{"full":[{"start":87,"end":116,"type":"D"}],"Structural state":[{"start":87,"end":116,"type":"D"}],"Disorder function":[{"start":87,"end":116,"type":"F"}]}},{"disprot_id":"DP03102","acc":"O44326","creator":"lrodriguez","date":"2021-01-05T21:55:08.249Z","features":{"pfam":[{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":280,"end":320},{"id":"PF00514","name":"Armadillo/beta-catenin-like repeat","start":361,"end":402}],"gene3D":[]},"length":678,"name":"Beta-catenin-like protein hmp-2","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":613,"end":678,"reference_id":"25850673","reference_source":"pmid","reference_html":"A conserved phosphorylation switch controls the interaction between cadherin and β-catenin in vitro and in vivo. <i> Choi HJ, Loveless T, Lynch AM, Bang I, Hardin J, Weis WI. </i> Dev Cell, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4R0Z"}],"region_id":"DP03102r001","statement":[{"text":"Although the C-terminal tail (residues 613–678) is part of the crystallized construct, it was  not visible in the structure; in particular, the extra  α helix (“helix C”) found just after the  arm repeats in crystals of full-length zebrafish  β-catenin (Xing et al., 2008) and in  plakoglobin (Choi et al., 2009) is absent.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-25T13:07:54.690Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":613,"end":678,"reference_id":"25850673","reference_source":"pmid","reference_html":"A conserved phosphorylation switch controls the interaction between cadherin and β-catenin in vitro and in vivo. <i> Choi HJ, Loveless T, Lynch AM, Bang I, Hardin J, Weis WI. </i> Dev Cell, 2015","date":"2022-03-08T14:03:40.689Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":4,"region_id":"DP03102r002","statement":[{"text":"To test whether the tails of HMP-2 affect the  affinity for pHMR-1  cyto80  , ITC experiments were performed using HMP-2  13end   and  HMP-2  54end  . The presence of the C-terminal tail of HMP-2 weakens the affinity  approximately 7-fold (23 nM vs. 3.1 nM), whereas the presence of the N-terminal tail did  not significantly affect binding to phosphorylated HMR-1 (Figs. 1A, S2, Table S2). ","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"Q967F4","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-26T13:48:40.537Z"}},{"start":613,"end":678,"reference_id":"25850673","reference_source":"pmid","reference_html":"A conserved phosphorylation switch controls the interaction between cadherin and β-catenin in vitro and in vivo. <i> Choi HJ, Loveless T, Lynch AM, Bang I, Hardin J, Weis WI. </i> Dev Cell, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":" Q967F4","partner_start":null,"partner_end":null}],"region_id":"DP03102r003","statement":[{"text":"To test whether the tails of HMP-2 affect the  affinity for pHMR-1  cyto80  , ITC experiments were performed using HMP-2  13end   and  HMP-2  54end. The presence of the C-terminal tail of HMP-2 weakens the affinity  approximately 7-fold (23 nM vs. 3.1 nM), whereas the presence of the N-terminal tail did  not significantly affect binding to phosphorylated HMR-1 (Figs. 1A, S2, Table S2). ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-25T13:07:55.783Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":3,"released":"2021_12","sequence":"MLLHSTNSYSIFTDHEVETRTSRIRSAMFPDWIPPTSAAEATNSTTSIVEMMQMPTQQLKQSVMDLLTYEGSNDMSGLSLPDLVKLMCDHDESVVARAVHRAYMLSREDPNFFNAPGFDHRSFVEALMAASKSSNVNVRRNAIGALSHMSEQRGGPLLIFRSGGLAEIIRMLYDSLESVVHYAVTTLRNLLMHVSDSRAQARALNAVEALTPHLHKTNPKLLAQVADGLYFLLIDDAPSKITFLSLLGPQILVSILREYSDHRKLIYTVVRCIRSLSVCPSNKPALISLGCLPALYVELCTAKDERSQTAILVAMRNLSDSATNEENLTQLIIKLLEIIRVANDGMTACACGTLSNLTCNNTRNKQTVCSHGGIDALVTAIRRLPEVEEVTEPALCALRHCTARHSLAEEAQSELRFCQAFPVILDQLETLRTPVIKAALGVIRNSALLQTNLIELTQEQTANGHTAVSLTMDILRRAITAIEENPDIAVDGVPMWGVIEGAVSALHQLANHPAVAAACCDDIGQVGNPECPPFLDLLHRLLAHPRLGSMDDEVLEREILGLLYQLSKRPDGARAVESTGVSALLMESRGSQYKSVVTYANGVLSNLKRGDSAAIMNMSNSYDYEMSGSAADWQRDGLERELFAEMYPTNDGGHSESINMALNNSQMRPNHNWYDTDL","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"dataset":[],"UniParc":"UPI0000082583","uniref100":"UniRef100_O44326","uniref90":"UniRef90_O44326","uniref50":"UniRef50_O44326","genes":[{"name":{"value":"hmp-2"},"orfNames":[{"value":"K05C4.6"}]}],"alphafold_very_low_content":0.11356932153392331,"disorder_content":0.09734513274336283,"disprot_consensus":{"full":[{"start":613,"end":678,"type":"D"}],"Structural state":[{"start":613,"end":678,"type":"D"}],"Molecular function":[{"start":613,"end":678,"type":"F"}]}},{"disprot_id":"DP03104","acc":"P29590","creator":"mpajkos","date":"2021-01-06T14:51:13.087Z","features":{"pfam":[{"id":"PF00097","name":"Zinc finger, C3HC4 type (RING finger)","start":57,"end":91},{"id":"PF12126","name":"PML-like, coiled-coil","start":240,"end":570},{"id":"PF22586","name":"ANCHR-like B-box zinc-binding domain","start":128,"end":161},{"id":"PF25244","name":"PML, C-terminal domain","start":777,"end":852}],"gene3D":[]},"length":882,"name":"Protein PML","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":94,"end":104,"reference_id":"25627356","reference_source":"pmid","reference_html":"The RING domain of human promyelocytic leukemia protein (PML). <i> Huang SY, Chang CF, Fang PJ, Naik MT, Güntert P, Shih HM, Huang TH. </i> J Biomol NMR, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"mpajkos","curator_name":"Mátyás Pajkos","curator_orcid":"0000-0001-5791-9825","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":2,"cross_refs":[{"db":"PDB","id":"2MWX"}],"region_id":"DP03104r001","statement":[{"text":"The N terminal segment from Glu49 to Phe54 and the C-terminal segment from Pro94 to Ile104 are disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-08T13:20:59.472Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2022_06","sequence":"MEPAPARSPRPQQDPARPQEPTMPPPETPSEGRQPSPSPSPTERAPASEEEFQFLRCQQCQAEAKCPKLLPCLHTLCSGCLEASGMQCPICQAPWPLGADTPALDNVFFESLQRRLSVYRQIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEARPLAELRNQSVREFLDGTRKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSELKCDISAEIQQRQEELDAMTQALQEQDSAFGAVHAQMHAAVGQLGRARAETEELIRERVRQVVAHVRAQERELLEAVDARYQRDYEEMASRLGRLDAVLQRIRTGSALVQRMKCYASDQEVLDMHGFLRQALCRLRQEEPQSLQAAVRTDGFDEFKVRLQDLSSCITQGKDAAVSKKASPEAASTPRDPIDVDLPEEAERVKAQVQALGLAEAQPMAVVQSVPGAHPVPVYAFSIKGPSYGEDVSNTTTAQKRKCSQTQCPRKVIKMESEEGKEARLARSSPEQPRPSTSKAVSPPHLDGPPSPRSPVIGSEVFLPNSNHVASGAGEAEERVVVISSSEDSDAENSSSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLVFFDLKIDNETQKISQLAAVNRESKFRVVIQPEAFFSIYSKAVSLEVGLQHFLSFLSSMRRPILACYKLWGPGLPNFFRALEDINRLWEFQEAISGFLAALPLIRERVPGASSFKLKNLAQTYLARNMSERSAMAAVLAMRDLCRLLEVSPGPQLAQHVYPFSSLQCFASLQPLVQAAVLPRAEARLLALHNVSFMELLSAHRRDRQGGLKKYSRYLSLQTTTLPPAQPAFNLQALGTYFEGLLEGPALARAEGVSTPLAGRGLAERASQQS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins"],"UniParc":"UPI000013D78F","uniref100":"UniRef100_P29590","uniref90":"UniRef90_P29590","uniref50":"UniRef50_P29590","genes":[{"name":{"value":"PML"},"synonyms":[{"value":"MYL"},{"value":"PP8675"},{"value":"RNF71"},{"value":"TRIM19"}]}],"alphafold_very_low_content":0.3321995464852608,"disorder_content":0.012471655328798186,"disprot_consensus":{"full":[{"start":94,"end":104,"type":"D"}],"Structural state":[{"start":94,"end":104,"type":"D"}]}},{"disprot_id":"DP03105","acc":"Q967F4","creator":"lrodriguez","date":"2021-01-06T15:21:45.373Z","features":{"pfam":[{"id":"PF00028","name":"Cadherin domain","start":647,"end":735},{"id":"PF00028","name":"Cadherin domain","start":886,"end":969},{"id":"PF00028","name":"Cadherin domain","start":1231,"end":1322},{"id":"PF00028","name":"Cadherin domain","start":1342,"end":1426},{"id":"PF00028","name":"Cadherin domain","start":1445,"end":1536},{"id":"PF00028","name":"Cadherin domain","start":1565,"end":1652},{"id":"PF00028","name":"Cadherin domain","start":1666,"end":1755},{"id":"PF00028","name":"Cadherin domain","start":1779,"end":1850},{"id":"PF02210","name":"Laminin G domain","start":2312,"end":2460},{"id":"PF22417","name":"Cadherin-related hmr-1 E-cadherin-like","start":2876,"end":2898},{"id":"PF24613","name":"Cadherin-related hmr-1, EGF domain","start":2721,"end":2765},{"id":"PF24811","name":"DE-cadherin, Ig-like domain","start":2082,"end":2235}],"gene3D":[]},"length":2920,"name":"Cadherin-related hmr-1","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":2850,"end":2875,"reference_id":"25850673","reference_source":"pmid","reference_html":"A conserved phosphorylation switch controls the interaction between cadherin and β-catenin in vitro and in vivo. <i> Choi HJ, Loveless T, Lynch AM, Bang I, Hardin J, Weis WI. </i> Dev Cell, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"4R10"},{"db":"PDB","id":"4R11"}],"region_id":"DP03105r001","statement":[{"text":"Region I interacts with side  chains from arm repeats 7, 8 and 9 (Fig. 3B). Residues 1153–1178, which connect regions I  and II, are disordered.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-15T06:42:34.026Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":2850,"end":2875,"reference_id":"25850673","reference_source":"pmid","reference_html":"A conserved phosphorylation switch controls the interaction between cadherin and β-catenin in vitro and in vivo. <i> Choi HJ, Loveless T, Lynch AM, Bang I, Hardin J, Weis WI. </i> Dev Cell, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"cross_refs":[{"db":"PDB","id":"4R10"},{"db":"PDB","id":"4R11"}],"interaction_partner":[{"db":"UniProt","id":"O44326","partner_start":null,"partner_end":null}],"region_id":"DP03105r002","statement":[{"text":"Region I interacts with side  chains from arm repeats 7, 8 and 9 (Fig. 3B). Residues 1153–1178, which connect regions I  and II, are disordered. Hydrophobic residues on the amphipathic helix in region II pack  against HMP-2 residues located on arm repeats 11 and 12, including Tyr599 (see below)  (Fig. 3C). ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-15T06:42:29.717Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":2910,"end":2920,"reference_id":"25850673","reference_source":"pmid","reference_html":"A conserved phosphorylation switch controls the interaction between cadherin and β-catenin in vitro and in vivo. <i> Choi HJ, Loveless T, Lynch AM, Bang I, Hardin J, Weis WI. </i> Dev Cell, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":5,"cross_refs":[{"db":"PDB","id":"4R10"},{"db":"PDB","id":"4R11"}],"region_id":"DP03105r003","statement":[{"text":"The mass spectrometry analysis of in vitro  phosphorylated HMR-1 suggested that four  residues in region IV are sequentially phosphorylated by CKI. In pHMR-1 conformation A,  only the first phosphorylated residue, Ser1212, is observed; all of the HMR-1 residues Cterminal to this position are disordered (Fig. 4A,B).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-15T06:42:43.526Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":2841,"end":2920,"reference_id":"25850673","reference_source":"pmid","reference_html":"A conserved phosphorylation switch controls the interaction between cadherin and β-catenin in vitro and in vivo. <i> Choi HJ, Loveless T, Lynch AM, Bang I, Hardin J, Weis WI. </i> Dev Cell, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03105r004","statement":[{"text":"The purified HMR-1 cytoplasmic tail runs about 3x larger than its predicted size on a gel filtration column, similar to the  behavior of the unstructured E-cadherin cytoplasmic domain (  Huber et al., 2001  ), consistent  with its being an intrinsically unstructured protein.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-15T06:42:44.486Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":2841,"end":2920,"reference_id":"25850673","reference_source":"pmid","reference_html":"A conserved phosphorylation switch controls the interaction between cadherin and β-catenin in vitro and in vivo. <i> Choi HJ, Loveless T, Lynch AM, Bang I, Hardin J, Weis WI. </i> Dev Cell, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03105r005","statement":[{"text":"The purified HMR-1 cytoplasmic tail runs about 3x larger than its predicted size on a gel filtration column, similar to the  behavior of the unstructured E-cadherin cytoplasmic domain (  Huber et al., 2001  ), consistent  with its being an intrinsically unstructured protein. Thus it is likely that the region around  HMR-1 S1212 is disordered unless it is phosphorylated and bound to HMP-2.","type":"Discussion"},{"text":"From the experimental information (SEC evidence of disorder state and crystallography evidence of order state) it can be concluded a structural transition.","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"4R10"},{"db":"PDB","id":"4R11"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-15T06:42:30.406Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"}],"regions_counter":5,"released":"2023_12","sequence":"MSWNILLILLISNLDEVLAKTLLKLPSNAPPGWLISDLQFQNLIGDSEIATLQPSIFSTNFEVEDGYRIITNTTVTQFHGELFELFLNVKEQNFQRLVTLHVYVDPRGTSQQPATFLSTVYHATVYTSQQPGSTVVFSKPITVRNRKNFVISPISKIDKISKYSSPFSVMTRGKSVDIVMMKQKLEEDDITRHVIFLGAFTEKTGEMIAQTKVIIDVIDSGDVHFLLKSKKSIAKFASAIPANSTVFDVEKRNLSEPLLFHLEEPSRFFKIDQFSGRVSTVLPVGYGTYHIHVVARNQKKQRSDAWLEISVKKEQKLEPMTSSRSRRHLDDIVFRIPENTTMEDIEKKDMKIPLFAGETIGEINVAKEWLKIDDDGKIHLLKPLNYEKTSSIIATVPINGLQSTRTQTIRIHVADIDEPPSFVNSPLPMLAVVPLNPTIGRIVYQFVARDEHGDGDSNVLYKTIDVIPAGSFIVDPKSGVVRTGWSKYERGDTYRISAQAMDLSPSDNTTSQLSEVAILEILADERPPQFAKQEYEVTVSEDNLVDYSVVDVKAQSFRSFEDGRSKGPITYSLEGDTPEDETKWFRIDPSTGIIHLTRLLDFDDPALPKLHKLKVTAREDNRESHVDLTIRIDDVNDNVPTFTRPLYTAQVREDIPLNQTILKVTAVDKDTGDNSRITYSVDNHNFSINSNGEISAKVRLDADQLNERHFVYRFNVTARDHGEPVSLSSSAMIHIRTENTNDESAVFLPTSQYTAFVAEDAQGGTPVIQIQARDADRDEVTYSFMDKNGRSTQKMNLFSIDEHTGLVKLRHGVSAADLAEAENPINLTVIVQDDGSCCVYPSKTHTSYATLLIGIEDVNNNKPEFPDCAKYSDIAKIMEGTYKTDPPTIVKVEATDDDSSANGDIVYSLYYTQSESRKAFVIDRQTGVLTPSPHVVFDRETRPREDVTVKATDRGDRPLIGFCQFSVEVVDINDNSPQFERPSYETSVSRFEAVGTSVITVFAFDNDAAHNAEITYSLEIDTTAGEEHQNDLDFFELVNRRSGEITLIKPIPMKTQKFIFNVIADDNGIPEALQSSAQVTLNVLDKQQKAPKWQTSPDCKPGITVDENVELNKVILRCRAVSSGDSRNSDVIYKLTASGGPGNKAESKFRQFNKFENGNEWVEVVIMEGLDYEQVNNYTLTLTATDMTSRVASTKTFVVEVRDVNDVVPQFTVDLFTGTIDEEMTPNEHLEKTNGKPIVTVKAIDTDSDGPQNEVHYRIVGEANGEETKHFRIDELTGEIFPNEKFDREKIDMYILTVEASDRSVSALPGANGPNKDNVKVQIVINDVNDNAPSFEEQKYIGRVKESEGEGHDVITIKAHDLDKHSNLRYHLIGAGGGRIPFGVRTDSGTIFVKEPLDFEASDQYHLVLIASDGRHNATTNVYIHIEDVNDNAPQFEQQKYATTVIEEDVDIPKVLFNVHATDADQDEKSSRIVYRLEGQGADEVFRIGKYSGTIELVKALDRDPPAGVPSWNFVVQAIDDDGNGLVGYADVQVNVRDINDNSPIFPERLFGYIEENREPIHSDGVYFMDVQARDFDDPTTENANIEYGIVRNKLINGESVFRIDQNTGKIFAMRSLDREISSEREFIIEVRANDRGVPSREGFANVTIKVTDMNDNAPFFEKTRYEGSVEETAPIGAAVMSFSAFDADEEAKDNVFTYQLSEESDYFYVTTDKDSKQSSVGVLRVKQPLDYEDVTQRDGFHLGIRVSDGRHDAEAAVHVALVDRNDHAPHIHGATEHRVREDVPRGTSIGRYTATDRDAGDTARFRINRQSDPKRQFTIDQDGTLRVAHTLDREDIAVYNLIIEAYDNSNNIGRQMVAVYLQDVNDNGPEPYTVPRPCIFRENTPVNQLGTCEIRATDRDTAEFGPPFTMEVSPSFKYSQYLNVIFNANGDGGNGSMTITPLQEFDREAPVPGKILEIPLILADRAGRRNEASVHVIIGDLNDNTMHDGRMTIHVNSYLGRLKETVIGRVYVDDADDWDLGDKTFSWKDSRPGFELSDKGSITMAGEMAAGTYTMSANVHDNARDEDAVGYVTVIVNAVPQIAFDNQGSVQLLIAEETPLQLPDDFIRADSNGQSLMDTFKQEMTAYMGGDVTVDVFSVQVGIATLQTRDVPVLNVRFNARGSTYRDTAQLNGLIAAHRADLQRKLNVEIVGVGIDMCKFTQCDAGCQTLNSADYDGIVVSANSTVIVGVNATSRDDCTCPVWRAPPACQHSLCHNDGVCHNTNPGFFCECRNDGLKGARCQGTTRSFGGNGFAWYKPMPACTSLNISFSFMTTQSDALLFYNGPLETLRNDTHIEYSDYIFIQLRGGRISLEVSMNGQSRSSLEVASTALNDGTWHDISVNQEGKRVELVVDNCRFLGAGADDSSCRAELYTPDDDERLNIVTPVQIGGLAPLSGQDYPQTIPRAGLNGCVRNLNVNGDQYDLATPAFEQNSEKGCRLWGATCDSNSVDSLNHCIHGDCFADVQGSGAMVAKCVCDPGWGGARCERRMEWIQFAQGAFIEYSPRIAFPEQVSDIELLFISGKVNGAPAELSFGTDSQQSYVSTNLESGQNGVTAAGKFDIGTGGRRARQELRVSEVLLKENASYWLQFTRNPTRASLSIDNAYTVSTQLDKGEPFSLQVNQITLGTQGQNKGFQGCIGTYRWSKQNLPLKRGGAMDENEESIVSISNMAGVQDGCDLRITCADLPAGYCGGSFVCVDFWKGPFCTCNDGANAILGDDGQVVGCGETLAVSKLGISSPAIILILVSLALLILLVMMMVVYTRRSPGAFENVRPEEMNRDNLRQYGVEGGGEADNDQYSMAGLRKPVMPLDTGMGPAIGGHPPHYPPRGMAPPKDDHELNSKIKDLETDQNAAPYDELRIYDDERDNISVVTLESIESAQ","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"dataset":[],"UniParc":"UPI000007DA26","uniref100":"UniRef100_Q967F4","uniref90":"UniRef90_Q967F4","uniref50":"UniRef50_Q967F4","genes":[{"name":{"value":"hmr-1"},"orfNames":[{"value":"W02B9.1"}]}],"disorder_content":0.0273972602739726,"disprot_consensus":{"full":[{"start":2841,"end":2920,"type":"T"}],"Structural state":[{"start":2841,"end":2920,"type":"D"}],"Molecular function":[{"start":2850,"end":2875,"type":"F"}],"Structural transition":[{"start":2841,"end":2920,"type":"T"}]}},{"disprot_id":"DP03106","acc":"P34369","creator":"lrodriguez","date":"2021-01-06T20:24:33.671Z","features":{"pfam":[{"id":"PF01398","name":"JAB1/Mov34/MPN/PAD-1 ubiquitin protease","start":2093,"end":2192},{"id":"PF08082","name":"PRO8NT (NUC069), PrP8 N-terminal domain","start":48,"end":199},{"id":"PF08083","name":"PROCN (NUC071) domain","start":388,"end":793},{"id":"PF08084","name":"PROCT (NUC072) domain","start":2205,"end":2326},{"id":"PF10596","name":"U6-snRNA interacting domain of PrP8","start":1435,"end":1593},{"id":"PF10597","name":"U5-snRNA binding site 2 of PrP8","start":1229,"end":1365},{"id":"PF10598","name":"RNA recognition motif of the spliceosomal PrP8","start":978,"end":1068},{"id":"PF12134","name":"PRP8 domain IV core","start":1753,"end":1981}],"gene3D":[]},"length":2329,"name":"Pre-mRNA-splicing factor 8 homolog","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":2308,"end":2329,"reference_id":"17473007","reference_source":"pmid","reference_html":"Crystal structure of the C-terminal domain of splicing factor Prp8 carrying retinitis pigmentosa mutants. <i> Zhang L, Shen J, Guarnieri MT, Heroux A, Yang K, Zhao R. </i> Protein Sci, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2P87"}],"region_id":"DP03106r001","statement":[{"text":"The  extreme  N-terminal  five  residues  and  Cterminal 22 residues of cC273 are disordered and cannot be seen in the crystal structure.","type":"Results"},{"text":"The  remaining  five  frameshift  and  one missense  RP13  mutations  are  downstream  from  c-F2307 (h-R2314)  and  fall  within  the  terminal  peptide  that  is disordered in the cC273 structure. ","type":"Results"},{"text":"Although the peptide downstream  from  c-F2307  (h-F2314)  is  disordered  in  our crystal structure, it may  take on a  defined conformation upon  interaction  with  its  partner. ","type":"Results"},{"text":"Figure 2. Multiple  sequence  alignment  among  cC273,  hC273,  y C273,  and  Af2198.  The  three  Prp8  sequences  are  aligned  using MultAlin (Corpet 1988). Af2198 is aligned with cC273 based on structural superimposition. Secondary structures as they are observed in  the crystal  structures of  cC273 and Af2198 are  labeled on top of  the cC273 sequence and the bottom of  the  Af2198 sequence, respectively.  3 10 helices  are  not  differentiated  from a helices  and  are  both  labeled  as  helices  with  prefixafor  simplicity. Gray represents residues that are disordered in the crystal structure.","type":"Figure"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MANYGGHPQTEPHAIPDSILEEKSRKWKQLQGKRYSEKKKFGMSDTQKEEMPPEHVRKVIRDHGDMTSRKYRHDKRVYLGALKYMPHAVLKLLENMPMPWEQIRDVKVLYHITGAITFVNDIPRVIEPVYMAQWGTMWIMMRREKRDRRHFKRMRFPPFDDEEPPLDYADNILDVEPLEPIQMELDPEEDGAVAEWFYDHKPLATTRFVNGPTYRKWAFSIPQMSTLYRLANQLLTDLVDDNYFYLFDMKSFFTAKALNVAIPGGPKFEPLVKDLHTDEDWNEFNDINKVIIRAPIRTEYRIAFPFMYNNLISSLPVQVSWYHTPSVVFIKTEDPDLPAFYYDPLINPIVLSNLKATEENLPEGEEEDEWELPEDVRPIFEDVPLYTDNTANGLALLWAPRPFNLRSGRTRRAVDVPLVKSWYREHCPAGMPVKVRVSYQKLLKVFVLNALKHRPPKPQKRRYLFRSFKATKFFQTTTLDWVEAGLQVLRQGYNMLNLLIHRKNLNYLHLDYNFNLKPVKTLTTKERKKSRFGNAFHLCREILRLTKLVVDAHVQYRLNNVDAYQLADGLQYIFAHVGQLTGMYRYKYKLMRQVRMCKDLKHLIYYRFNTGPVGKGPGCGFWAPGWRVWLFFLRGITPLLERWLGNLLSRQFEGRHSKGVAKTVTKQRVESHFDLELRAAVMHDILDMMPDGIKQNKARVILQHLSEAWRCWKANIPWKVPGLPTPVENMILRYVKAKADWWTNSAHYNRERVRRGATVDKTVCKKNLGRLTRLYLKSEQERQHNYLKDGPYISAEEAVAIYTTTVHWLESRRFSPIPFPPLSYKHDTKLLILALERLKESYSVKNRLNQSQREELALIEQAYDNPHEALSRIKRHMLTQRAFKEVGIEFMDLYTHLIPVYDIEPLEKVTDAYLDQYLWYEADKRRLFPAWVKPGDTEPPPLLTYKWCQGLNNLQDVWETSEGECNVIMETKLEKIAEKMDLTLLNRLLRLIVDHNIADYMTSKNNVLINYKDMNHTNSFGIIRGLQFASFIVQFYGLVLDLLVLGLRRASEIAGPPQCPNEFLQFQDVATEIGHPIRLYCRYIDRVWIMFRFSADEARDLIQRYLTEHPDPNNENIVGYNNKKCWPRDARMRLMKHDVNLGRAVFWDIKNRLPRSITTVEWENSFVSVYSKDNPNMLFDMSGFECRILPKCRTANEEFVHRDGVWNLQNEVTKERTAQCFLKVDEESLSKFHNRIRQILMSSGSTTFTKIVNKWNTALIGLMTYFREAVVNTQELLDLLVKCENKIQTRIKIGLNSKMPSRFPPVVFYTPKEIGGLGMLSMGHVLIPQSDLRWMQQTEAGGVTHFRSGMSHDEDQLIPNLYRYIQPWEAEFVDSVRVWAEYALKRQEANAQNRRLTLEDLDDSWDRGIPRINTLFQKDRHTLAYDKGWRVRTEFKAYQILKQNPFWWTHQRHDGKLWNLNNYRTDMIQALGGVEGILEHTLFRGTYFPTWEGLFWERASGFEESMKFKKLTNAQRSGLNQIPNRRFTLWWSPTINRANVYVGFQVQLDLTGIFMHGKIPTLKISLIQIFRAHLWQKIHESVVMDLCQVFDQELDALEIQTVQKETIHPRKSYKMNSSCADVLLFAQYKWNVSRPSLMADSKDVMDNTTTQKYWLDVQLRWGDYDSHDVERYARAKFLDYTTDNMSIYPSPTGVLIAIDLAYNLYSAYGNWFPGMKPLIRQAMAKIIKANPAFYVLRERIRKGLQLYSSEPTEPYLTSQNYGELFSNQIIWFVDDTNVYRVTIHKTFEGNLTTKPINGAIFIFNPRTGQLFLKIIHTSVWAGQKRLSQLAKWKTAEEVAALIRSLPVEEQPRQIIVTRKAMLDPLEVHLLDFPNIVIKGSELMLPFQAIMKVEKFGDLILKATEPQMVLFNLYDDWLKTISSYTAFSRVVLIMRGMHINPDKTKVILKPDKTTITEPHHIWPTLSDDDWIKVELALKDMILADYGKKNNVNVASLTQSEVRDIILGMEISAPSQQRQQIADIEKQTKEQSQVTATTTRTVNKHGDEIITATTSNYETASFASRTEWRVRAISSTNLHLRTQHIYVNSDDVKDTGYTYILPKNILKKFITISDLRTQIAGFMYGVSPPDNPQVKEIRCIVLVPQTGSHQQVNLPTQLPDHELLRDFEPLGWMHTQPNELPQLSPQDVTTHAKLLTDNISWDGEKTVMITCSFTPGSVSLTAYKLTPSGYEWGKANTDKGNNPKGYMPTHYEKVQMLLSDRFLGYFMVPSNGVWNYNFQGQRWSPAMKFDVCLSNPKEYYHEDHRPVHFHNFKAFDDPLGTGSADREDAFA","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"dataset":[],"UniParc":"UPI000013B834","uniref100":"UniRef100_P34369","uniref90":"UniRef90_P34369","uniref50":"UniRef50_P34369","genes":[{"name":{"value":"prp-8"},"orfNames":[{"value":"C50C3.6"}]}],"alphafold_very_low_content":0.03349076857020181,"disorder_content":0.009446114212108201,"disprot_consensus":{"full":[{"start":2308,"end":2329,"type":"D"}],"Structural state":[{"start":2308,"end":2329,"type":"D"}]}},{"disprot_id":"DP03107","acc":"Q23229","creator":"lrodriguez","date":"2021-01-06T22:13:03.263Z","features":{"pfam":[{"id":"PF09108","name":"Switch protein XOL-1, N-terminal","start":18,"end":177},{"id":"PF09109","name":"Switch protein XOL-1, GHMP-like","start":184,"end":372}],"gene3D":[]},"length":417,"name":"XO lethal protein 1","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":29,"end":38,"reference_id":"12672694","reference_source":"pmid","reference_html":"XOL-1, primary determinant of sexual fate in C. elegans, is a GHMP kinase family member and a structural prototype for a class of developmental regulators. <i> Luz JG, Hassig CA, Pickle C, Godzik A, Meyer BJ, Wilson IA. </i> Genes Dev, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1MG7"}],"region_id":"DP03107r001","statement":[{"text":"The following regions were omitted from the final model for lack of interpretable density: residues 1–7, 29–38, and 190–195 in monomer 1 and residues 1–7, 29–38, and 190–194 in monomer 2.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-07T10:45:57.151Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MQVEANSERRVKILGIDRSENSPVLTYMETEDDPNFRNSKLAAAPHTVHMMDSGFLAINRQCLVKGKAILAREPKSSNEHMIDDLPKHAHDQHTLSILRDFIDQLKLHNVYEINFYDPLDSSGKLAVIPMLIALWKCMLASETDICDQEVLKSIMNSVIAKFELQIPCKNAVIDATLSGSREEVHIIAEDGSLENSNGTTEHFNKKHDLVFVKTDLHPEDFTPQMFPSQAKAKLLRDAFNNEEDEDTFPDILVPAYMTAHSKNRVRQEDYTCLEVEFDSQVALEKLMNEHEQVEGFEVQQGGILVALKKDSFFDDELIEKIAIAIATESRQSVSSVSFDLLKLGPGASLVTLANSRRFEPECRVVLQIEVKPVSPGETSSEGISDEHHYEEYDEDDIMEEEEAPSARQDDTYDEDEE","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"dataset":[],"UniParc":"UPI000007901D","uniref100":"UniRef100_Q23229","uniref90":"UniRef90_Q23229","uniref50":"UniRef50_Q23229","genes":[{"name":{"value":"xol-1","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"C18A11.5b","url":"https://www.wormbase.org/db/seq/sequence?name=C18A11.5b;class=Transcript"}}]},"orfNames":[{"value":"C18A11.5","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"C18A11.5b","url":"https://www.wormbase.org/db/seq/sequence?name=C18A11.5b;class=Transcript"}}]}]}],"alphafold_very_low_content":0.11510791366906475,"disorder_content":0.023980815347721823,"disprot_consensus":{"full":[{"start":29,"end":38,"type":"D"}],"Structural state":[{"start":29,"end":38,"type":"D"}]}},{"disprot_id":"DP03108","acc":"P15374","creator":"viglesias","date":"2021-01-07T10:46:52.971Z","features":{"pfam":[{"id":"PF01088","name":"Ubiquitin carboxyl-terminal hydrolase, family 1","start":6,"end":214}],"gene3D":[]},"length":230,"name":"Ubiquitin carboxyl-terminal hydrolase isozyme L3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":147,"end":166,"reference_id":"9233788","reference_source":"pmid","reference_html":"Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution. <i> Johnston SC, Larsen CN, Cook WJ, Wilkinson KD, Hill CP. </i> EMBO J, 1997","date":"2022-02-14T09:00:00.000Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1UCH"}],"region_id":"DP03108r001","statement":[{"text":"The UCH‐L3 structure includes a disordered 20 residue loop (residues 147‐166) that is positioned over the active site and may function in the definition of substrate specificity.","type":"Abstract"},{"text":"Two regions of UCH‐L3 lack defined electron density and have been omitted from the model (residues 1‐4 and 147‐166).","type":"Results"},{"text":"Access to the active site appears to be restricted futher by a 20 residue disordered loop consisting of residues 147‐166 which spans the active site cleft. ","type":"Results"},{"text":"The 20 residue loop between Thr147 and Val166 that is disordered in our crystals.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-07T17:43:10.528Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":147,"end":166,"reference_id":"9233788","reference_source":"pmid","reference_html":"Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution. <i> Johnston SC, Larsen CN, Cook WJ, Wilkinson KD, Hill CP. </i> EMBO J, 1997","date":"2022-02-14T09:00:00.000Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"1UCH"}],"region_id":"DP03108r002","statement":[{"text":"Access to the active site appears to be restricted futher by a 20 residue disordered loop consisting of residues 147‐166 which spans the active site cleft.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-28T09:01:26.135Z"},"ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":2,"released":"2021_12","sequence":"MEGQRWLPLEANPEVTNQFLKQLGLHPNWQFVDVYGMDPELLSMVPRPVCAVLLLFPITEKYEVFRTEEEEKIKSQGQDVTSSVYFMKQTISNACGTIGLIHAIANNKDKMHFESGSTLKKFLEESVSMSPEERARYLENYDAIRVTHETSAHEGQTEAPSIDEKVDLHFIALVHVDGHLYELDGRKPFPINHGETSDETLLEDAIEVCKKFMERDPDELRFNAIALSAA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000004D00E","uniref100":"UniRef100_P15374","uniref90":"UniRef90_P15374","uniref50":"UniRef50_P15374","genes":[{"name":{"value":"UCHL3"}}],"alphafold_very_low_content":0.004347826086956522,"disorder_content":0.08695652173913043,"disprot_consensus":{"full":[{"start":147,"end":166,"type":"D"}],"Structural state":[{"start":147,"end":166,"type":"D"}],"Molecular function":[{"start":147,"end":166,"type":"F"}]}},{"disprot_id":"DP03109","acc":"Q9BYI3","creator":"tszani","date":"2021-01-07T12:47:12.770Z","features":{"pfam":[{"id":"PF09790","name":"Hyccin","start":23,"end":330}],"gene3D":[]},"length":521,"name":"Hyccin","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":149,"end":253,"reference_id":"26571211","reference_source":"pmid","reference_html":"The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P synthesis at the plasma membrane. <i> Baskin JM, Wu X, Christiano R, Oh MS, Schauder CM, Gazzerro E, Messa M, Baldassari S, Assereto S, Biancheri R, Zara F, Minetti C, Raimondi A, Simons M, Walther TC, Reinisch KM, De Camilli P. </i> Nat Cell Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5DSE"}],"region_id":"DP03109r001","statement":[{"text":"Ribbon diagrams for TTC7B and FAM126A-N colored from blue (N-terminus) to red (C-terminus). The “arm” in FAM126A is green. Disordered residues absent from the model are indicated by dotted lines.","type":"Figure"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MFTSEKGVVEEWLSEFKTLPETSLPNYATNLKDKSSLVSSLYKVIQEPQSELLEPVCHQLFEFYRSGEEQLLQFTLQFLPELIWCYLAVSASRNVHSSGCIEALLLGVYNLEIVDKQGHTKVLSFTIPSLSKPSVYHEPSSIGSMALTESALSQHGLSKVVYSGPHPQREMLTAQNRFEVLTFLLLCYNAALTYMPSVSLQSLCQICSRICVCGYPRQHVRKYKGISSRIPVSSGFMVQMLTGIYFAFYNGEWDLAQKALDDIIYRAQLELYPEPLLVANAIKASLPHGPMKSNKEGTRCIQVEITPTSSRISRNAVTSMSIRGHRWKRHGNTELTGQEELMEISEVDEGFYSRAASSTSQSGLSNSSHNCSNKPSIGKNHRRSGGSKTGGKEKETTGESCKDHFARKQTQRAQSENLELLSLKRLTLTTSQSLPKPSSHGLAKTAATVFSKSFEQVSGVTVPHNPSSAVGCGAGTDANRFSACSLQEEKLIYVSERTELPMKHQSGQQRPPSISITLSTD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI00000714E2","uniref100":"UniRef100_Q9BYI3","uniref90":"UniRef90_Q9BYI3","uniref50":"UniRef50_Q9BYI3","genes":[{"name":{"value":"FAM126A"},"synonyms":[{"value":"DRCTNNB1A","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10910037","url":"http://www.ncbi.nlm.nih.gov/pubmed/10910037","alternativeUrl":"https://europepmc.org/abstract/MED/10910037"}}]}]}],"alphafold_very_low_content":0.40115163147792704,"disorder_content":0.20153550863723607,"disprot_consensus":{"full":[{"start":149,"end":253,"type":"D"}],"Structural state":[{"start":149,"end":253,"type":"D"}]}},{"disprot_id":"DP03110","acc":"Q9FIX2","creator":"viglesias","date":"2021-01-07T15:55:15.360Z","features":{"pfam":[{"id":"PF06094","name":"Gamma-glutamyl cyclotransferase, AIG2-like","start":12,"end":123}],"gene3D":[]},"length":165,"name":"AIG2-like protein A","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":151,"end":165,"reference_id":"16754964","reference_source":"pmid","reference_html":"Solution structure of Arabidopsis thaliana protein At5g39720.1, a member of the AIG2-like protein family. <i> Lytle BL, Peterson FC, Tyler EM, Newman CL, Vinarov DA, Markley JL, Volkman BF. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2G0Q"}],"region_id":"DP03110r001","statement":[{"text":" Residues of the N-terminal tag (1–9) and the disordered C-terminus (159–173) are omitted for clarity and were not included in the coordinates deposited in the PDB. ","type":"Figure"},{"text":"Authors refered residues 159-173 correspond to annotated residues 151-165.","type":"Curator statement"},{"text":"A long flexible α-helix protrudes from the structure at the C-terminal end.","type":"Abstract"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MCSSDSLQLHNVFVYGSFQDPDVINVMLDRTPEIVSATLPGFQRFRLKGRLYPCIVPSEKGEVHGKVLMGVTSDELENLDAVEGNEYERVTVGIVREDNSEKMAVKTYMWINKADPDMFGEWNFEEWKRLHKKKFIETFKKIMECKKKPQGQGNDDISHVLREDQ","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"dataset":[],"UniParc":"UPI00000A6847","uniref100":"UniRef100_Q9FIX2","uniref90":"UniRef90_Q9FIX2","uniref50":"UniRef50_P54121","genes":[{"name":{"value":"AIG2LA","evidences":[{"code":"ECO:0000305"}]},"orfNames":[{"value":"MIJ24.180"},{"value":"MKM21.1"},{"value":"MKM21.3","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"BAB11378.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAB11378.1"}}]},{"value":"MKM21_10"}],"olnNames":[{"value":"At5g39720","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT5G39720","url":""}}]}]}],"alphafold_very_low_content":0.06060606060606061,"disorder_content":0.09090909090909091,"disprot_consensus":{"full":[{"start":151,"end":165,"type":"D"}],"Structural state":[{"start":151,"end":165,"type":"D"}]}},{"disprot_id":"DP03111","acc":"O23813","creator":"viglesias","date":"2021-01-07T16:19:09.581Z","features":{"pfam":[{"id":"PF01077","name":"Nitrite and sulphite reductase 4Fe-4S domain","start":217,"end":393},{"id":"PF01077","name":"Nitrite and sulphite reductase 4Fe-4S domain","start":535,"end":627},{"id":"PF03460","name":"Nitrite/Sulfite reductase ferredoxin-like half domain","start":115,"end":175},{"id":"PF03460","name":"Nitrite/Sulfite reductase ferredoxin-like half domain","start":412,"end":475}],"gene3D":[]},"length":635,"name":"Sulfite reductase [ferredoxin], chloroplastic","ncbi_taxon_id":4577,"organism":"Zea mays","regions":[{"start":53,"end":62,"reference_id":"26920048","reference_source":"pmid","reference_html":"Structural and mutational studies of an electron transfer complex of maize sulfite reductase and ferredoxin. <i> Kim JY, Nakayama M, Toyota H, Kurisu G, Hase T. </i> J Biochem, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5H8V"},{"db":"PDB","id":"5H92"},{"db":"PDB","id":"5H8Y"}],"region_id":"DP03111r001","statement":[{"text":"In the crystallographic asymmetric unit of Form-1 crystal, there were two SiRs, designated as molecules A and B, aligned face-to-face; the structures of the polypeptide chain and two prosthetic groups were clearly revealed except for those of a flexible loop (Ser240 and Ala241 for molecule A and Gly236 to Ala241 for molecule B) and the terminal regions (the N-terminal ten residues and the C-terminal nine residues).","type":"Results"},{"text":"The construct's C-terminal residues correspond to annotated 53-62 region. ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-07T17:27:53.402Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MSGAIGGAEVHGFRGAAAQLPRSRVLGRPIRVAPPAAARPGGASAGSIRAVSAPAKKDASEVKRSKVEIIKEKSNFLRYPLNEELVSEAPNINESAVQLIKFHGSYQQTDRDVRGQKNYSFMLRTKNPCGKVPNQLYLAMDTLADEFGIGTLRLTTRQTFQLHGVLKKNLKTVLSTVIKNMGSTLGACGDLNRNVLAPAAPYVKKDILFAQQTAENIAALLTPQSGAYYDLWVDGEKIMSAEEPPEVTKARNDNSHGTNFPDSPEPIYGTQYLPRKFKVAVTAAGDNSVDILTNDIGVVVVSDDAGEPIGFNIYVGGGMGRTHRVETTFPRLADPLGYVPKEDILYAIKAIVVTQRENGRRDDRKYSRMKYMIDRWGIDRFRAEVEKYYGKKFESFRPLPEWQFNSYLGWQEQGDGKLFYGVHVDNGRVGGQAKKTLREIIEKYNLDVSITPNQNLILCGIDQAWREPITTALAQAGLLEPKDVDPLNLTAMACPALPLCPLAQTEAERGILPILKRIRAVFNKVGIKDSESVVVRITGCPNGCARPYMAELGFVGDGPKSYQIWLGGTPNQSTLAESFMDKVKLDDIEKVLEPLFTYWNGTRQEGESFGSFTNRTGFDKLKEVVNKWAESPSAA","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","PACMAD clade","Panicoideae","Andropogonodae","Andropogoneae","Tripsacinae","Zea"],"dataset":[],"UniParc":"UPI00000A0A99","uniref100":"UniRef100_O23813","uniref90":"UniRef90_O23813","uniref50":"UniRef50_O23813","genes":[{"name":{"value":"SIR"}}],"alphafold_very_low_content":0.09448818897637795,"disorder_content":0.015748031496062992,"disprot_consensus":{"full":[{"start":53,"end":62,"type":"D"}],"Structural state":[{"start":53,"end":62,"type":"D"}]}},{"disprot_id":"DP03112","acc":"P49235","creator":"viglesias","date":"2021-01-07T16:42:46.195Z","features":{"pfam":[{"id":"PF00232","name":"Glycosyl hydrolase family 1","start":75,"end":557}],"gene3D":[]},"length":566,"name":"4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1, chloroplastic","ncbi_taxon_id":4577,"organism":"Zea mays","regions":[{"start":55,"end":65,"reference_id":"11171077","reference_source":"pmid","reference_html":"Crystal structure of a monocotyledon (maize ZMGlu1) beta-glucosidase and a model of its complex with p-nitrophenyl beta-D-thioglucoside. <i> Czjzek M, Cicek M, Zamboni V, Burmeister WP, Bevan DR, Henrissat B, Esen A. </i> Biochem J, 2001","date":"2024-03-21T17:07:14.129Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":3,"cross_refs":[{"db":"PDB","id":"1E1F"}],"region_id":"DP03112r001","statement":[{"text":"In both structures (ZMGlu1 and ZMGlu1–pNPTGlc complex), the extreme N-terminal 12 and C-terminal 11 residues were\nnot defined in the electron-density maps, suggesting that these\nregions are disordered.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:656902"}]},{"start":556,"end":566,"reference_id":"11171077","reference_source":"pmid","reference_html":"Crystal structure of a monocotyledon (maize ZMGlu1) beta-glucosidase and a model of its complex with p-nitrophenyl beta-D-thioglucoside. <i> Czjzek M, Cicek M, Zamboni V, Burmeister WP, Bevan DR, Henrissat B, Esen A. </i> Biochem J, 2001","date":"2024-03-21T17:07:51.940Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":3,"cross_refs":[{"db":"PDB","id":"1E1E"},{"db":"PDB","id":"1E1F"}],"region_id":"DP03112r002","statement":[{"text":"In both structures (ZMGlu1 and ZMGlu1–pNPTGlc complex), the extreme N-terminal 12 and C-terminal 11 residues were\nnot defined in the electron-density maps, suggesting that these\nregions are disordered.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MAPLLAAAMNHAAAHPGLRSHLVGPNNESFSRHHLPSSSPQSSKRRCNLSFTTRSARVGSQNGVQMLSPSEIPQRDWFPSDFTFGAATSAYQIEGAWNEDGKGESNWDHFCHNHPERILDGSNSDIGANSYHMYKTDVRLLKEMGMDAYRFSISWPRILPKGTKEGGINPDGIKYYRNLINLLLENGIEPYVTIFHWDVPQALEEKYGGFLDKSHKSIVEDYTYFAKVCFDNFGDKVKNWLTFNEPQTFTSFSYGTGVFAPGRCSPGLDCAYPTGNSLVEPYTAGHNILLAHAEAVDLYNKHYKRDDTRIGLAFDVMGRVPYGTSFLDKQAEERSWDINLGWFLEPVVRGDYPFSMRSLARERLPFFKDEQKEKLAGSYNMLGLNYYTSRFSKNIDISPNYSPVLNTDDAYASQEVNGPDGKPIGPPMGNPWIYMYPEGLKDLLMIMKNKYGNPPIYITENGIGDVDTKETPLPMEAALNDYKRLDYIQRHIATLKESIDLGSNVQGYFAWSLLDNFEWFAGFTERYGIVYVDRNNNCTRYMKESAKWLKEFNTAKKPSKKILTPA","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","PACMAD clade","Panicoideae","Andropogonodae","Andropogoneae","Tripsacinae","Zea"],"dataset":[],"UniParc":"UPI000000057C","uniref100":"UniRef100_P49235","uniref90":"UniRef90_P49235","uniref50":"UniRef50_P49235","genes":[{"name":{"value":"GLU1"}}],"alphafold_very_low_content":0.12367491166077739,"disorder_content":0.038869257950530034,"disprot_consensus":{"full":[{"start":55,"end":65,"type":"D"},{"start":556,"end":566,"type":"D"}],"Structural state":[{"start":55,"end":65,"type":"D"},{"start":556,"end":566,"type":"D"}]}},{"disprot_id":"DP03113","acc":"Q6ZNA4","creator":"mpajkos","date":"2021-01-07T17:05:56.182Z","features":{"pfam":[{"id":"PF13639","name":"Ring finger domain","start":941,"end":983},{"id":"PF15303","name":"E3 ubiquitin-protein ligase Arkadia N-terminus","start":18,"end":292}],"gene3D":[]},"length":994,"name":"E3 ubiquitin-protein ligase Arkadia","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":927,"end":937,"reference_id":"22411132","reference_source":"pmid","reference_html":"NMR-based insights into the conformational and interaction properties of Arkadia RING-H2 E3 Ub ligase. <i> Chasapis CT, Kandias NG, Episkopou V, Bentrop D, Spyroulias GA. </i> Proteins, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"mpajkos","curator_name":"Mátyás Pajkos","curator_orcid":"0000-0001-5791-9825","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"2KIZ"}],"region_id":"DP03113r001","statement":[{"text":"For the N- and C-terminal residues (Lys927–Asp937 and Gln989–Ser994, respectively) the average S2 order parameter is 0.29 +- 0.02, whereas S2 values are much higher for the RING core region (Thr938–Ala988; average S2 value of 0.85 +- 0.02) (Supporting Information Fig. S5). Thus, the core of the Arkadia RING domain exhibits a rather rigid structure, while the two termini are mobile on the sub-nanosecond time scale and show only few NOEs (Supporting Information Figs. S2 and S5). The 15N relaxation data and order parameters clearly show that the above-mentioned b1-strand Thr938-Glu940 separates the flexibly disordered N-terminus from the wellstructured rigid core of the RING-H2 domain.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-08T13:52:27.335Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":300,"end":386,"reference_id":"24844634","reference_source":"pmid","reference_html":"Structural analysis of poly-SUMO chain recognition by the RNF4-SIMs domain. <i> Kung CC, Naik MT, Wang SH, Shih HM, Chang CC, Lin LY, Chen CL, Ma C, Chang CF, Huang TH. </i> Biochem J, 2014","date":"2022-11-03T19:50:29.377Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03113r002","statement":[{"text":"The free RNF111/Arkadia SIMs domain is also likely to be disordered and a similar poly-SUMO binding mechanism is employed.","type":"Results"},{"text":"By using NMR, SAXS and X-ray crystallography, the authors demonstrated that the SIMs domain in another related member of the family of SUMO-targeted ubiquitin ligases (RNF4) is largely unstructured. The region 300-386 encompass the SUMO interaction motif (SIM) 1, 2 and 3 present in the protein.","type":"Conclusion"}]}],"regions_counter":2,"released":"2023_12","sequence":"MSQWTPEYNELYTLKVDMKSEIPSDAPKTQESLKGILLHPEPIGAAKSFPAGVEMINSKVGNEFSHLCDDSQKQEKEMNGNQQEQEKSLVVRKKRKSQQAGPSYVQNCVKENQGILGLRQHLGTPSDEDNDSSFSDCLSSPSSSLHFGDSDTVTSDEDKEVSVRHSQTILNAKSRSHSARSHKWPRTETESVSGLLMKRPCLHGSSLRRLPCRKRFVKNNSSQRTQKQKERILMQRKKREVLARRKYALLPSSSSSSENDLSSESSSSSSTEGEEDLFVSASENHQNNPAVPSGSIDEDVVVIEASSTPQVTANEEINVTSTDSEVEIVTVGESYRSRSTLGHSRSHWSQGSSSHASRPQEPRNRSRISTVIQPLRQNAAEVVDLTVDEDEPTVVPTTSARMESQATSASINNSNPSTSEQASDTASAVTSSQPSTVSETSATLTSNSTTGTSIGDDSRRTTSSAVTETGPPAMPRLPSCCPQHSPCGGSSQNHHALGHPHTSCFQQHGHHFQHHHHHHHTPHPAVPVSPSFSDPACPVERPPQVQAPCGANSSSGTSYHEQQALPVDLSNSGIRSHGSGSFHGASAFDPCCPVSSSRAAIFGHQAAAAAPSQPLSSIDGYGSSMVAQPQPQPPPQPSLSSCRHYMPPPYASLTRPLHHQASACPHSHGNPPPQTQPPPQVDYVIPHPVHAFHSQISSHATSHPVAPPPPTHLASTAAPIPQHLPPTHQPISHHIPATAPPAQRLHPHEVMQRMEVQRRRMMQHPTRAHERPPPHPHRMHPNYGHGHHIHVPQTMSSHPRQAPERSAWELGIEAGVTAATYTPGALHPHLAHYHAPPRLHHLQLGALPLMVPDMAGYPHIRYISSGLDGTSFRGPFRGNFEELIHLEERLGNVNRGASQGTIERCTYPHKYKKVTTDWFSQRKLHCKQDGEEGTEEDTEEKCTICLSILEEGEDVRRLPCMHLFHQVCVDQWLITNKKCPICRVDIEAQLPSES","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000035E767","uniref100":"UniRef100_Q6ZNA4","uniref90":"UniRef90_Q6ZNA4","uniref50":"UniRef50_Q6ZNA4","genes":[{"name":{"value":"RNF111","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:17384","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:17384"}}]}}],"alphafold_very_low_content":0.8219315895372233,"disorder_content":0.09859154929577464,"disprot_consensus":{"full":[{"start":300,"end":386,"type":"D"},{"start":927,"end":937,"type":"D"}],"Structural state":[{"start":300,"end":386,"type":"D"},{"start":927,"end":937,"type":"D"}]}},{"disprot_id":"DP03114","acc":"Q86TV6","creator":"tszani","date":"2021-01-08T09:23:13.113Z","features":{"pfam":[{"id":"PF12895","name":"Anaphase-promoting complex, cyclosome, subunit 3","start":498,"end":573},{"id":"PF13181","name":"Tetratricopeptide repeat","start":398,"end":430},{"id":"PF13181","name":"Tetratricopeptide repeat","start":799,"end":829},{"id":"PF13424","name":"Tetratricopeptide repeat","start":732,"end":792},{"id":"PF19440","name":"Tetratricopeptide repeat protein 7 N-terminal","start":1,"end":386}],"gene3D":[]},"length":843,"name":"Tetratricopeptide repeat protein 7B","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":343,"end":358,"reference_id":"26571211","reference_source":"pmid","reference_html":"The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P synthesis at the plasma membrane. <i> Baskin JM, Wu X, Christiano R, Oh MS, Schauder CM, Gazzerro E, Messa M, Baldassari S, Assereto S, Biancheri R, Zara F, Minetti C, Raimondi A, Simons M, Walther TC, Reinisch KM, De Camilli P. </i> Nat Cell Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"5DSE"}],"region_id":"DP03114r001","statement":[{"text":" Ribbon diagrams for TTC7B and FAM126A-N colored from blue (N-terminus) to red (C-terminus). The “arm” in FAM126A is green. Disordered residues absent from the model are indicated by dotted lines","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-02-17T17:58:56.186Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":619,"end":686,"reference_id":"26571211","reference_source":"pmid","reference_html":"The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P synthesis at the plasma membrane. <i> Baskin JM, Wu X, Christiano R, Oh MS, Schauder CM, Gazzerro E, Messa M, Baldassari S, Assereto S, Biancheri R, Zara F, Minetti C, Raimondi A, Simons M, Walther TC, Reinisch KM, De Camilli P. </i> Nat Cell Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"5DSE"}],"region_id":"DP03114r002","statement":[{"text":" Ribbon diagrams for TTC7B and FAM126A-N colored from blue (N-terminus) to red (C-terminus). The “arm” in FAM126A is green. Disordered residues absent from the model are indicated by dotted lines","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-02-17T17:59:29.318Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":197,"end":212,"reference_id":"26571211","reference_source":"pmid","reference_html":"The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P synthesis at the plasma membrane. <i> Baskin JM, Wu X, Christiano R, Oh MS, Schauder CM, Gazzerro E, Messa M, Baldassari S, Assereto S, Biancheri R, Zara F, Minetti C, Raimondi A, Simons M, Walther TC, Reinisch KM, De Camilli P. </i> Nat Cell Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"5DSE"}],"region_id":"DP03114r003","statement":[{"text":" Ribbon diagrams for TTC7B and FAM126A-N colored from blue (N-terminus) to red (C-terminus). The “arm” in FAM126A is green. Disordered residues absent from the model are indicated by dotted lines","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-02-17T17:57:39.338Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":157,"end":166,"reference_id":"26571211","reference_source":"pmid","reference_html":"The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P synthesis at the plasma membrane. <i> Baskin JM, Wu X, Christiano R, Oh MS, Schauder CM, Gazzerro E, Messa M, Baldassari S, Assereto S, Biancheri R, Zara F, Minetti C, Raimondi A, Simons M, Walther TC, Reinisch KM, De Camilli P. </i> Nat Cell Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"5DSE"}],"region_id":"DP03114r004","statement":[{"text":" Ribbon diagrams for TTC7B and FAM126A-N colored from blue (N-terminus) to red (C-terminus). The “arm” in FAM126A is green. Disordered residues absent from the model are indicated by dotted lines","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-02-17T17:57:21.172Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":4,"released":"2023_12","sequence":"MATKKAGSRLETEIERCRSECQWERIPELVKQLSAKLIANDDMAELLLGESKLEQYLKEHPLRQGASPRGPKPQLTEVRKHLTAALDRGNLKSEFLQESNLIMAKLNYVEGDYKEALNIYARVGLDDLPLTAVPPYRLRVIAEAYATKGLCLEKLPISSSTSNLHVDREQDVITCYEKAGDIALLYLQEIERVILSNIQNRSPKPGPAPHDQELGFFLETGLQRAHVLYFKNGNLTRGVGRFRELLRAVETRTTQNLRMTIARQLAEILLRGMCEQSYWNPLEDPPCQSPLDDPLRKGANTKTYTLTRRARVYSGENIFCPQENTEEALLLLLISESMANRDAVLSRIPEHKSDRLISLQSASVVYDLLTIALGRRGQYEMLSECLERAMKFAFEEFHLWYQFALSLMAAGKSARAVKVLKECIRLKPDDATIPLLAAKLCMGSLHWLEEAEKFAKTVVDVGEKTSEFKAKGYLALGLTYSLQATDASLRGMQEVLQRKALLAFQRAHSLSPTDHQAAFYLALQLAISRQIPEALGYVRQALQLQGDDANSLHLLALLLSAQKHYHDALNIIDMALSEYPENFILLFSKVKLQSLCRGPDEALLTCKHMLQIWKSCYNLTNPSDSGRGSSLLDRTIADRRQLNTITLPDFSDPETGSVHATSVAASRVEQALSEVASSLQSSAPKQGPLHPWMTLAQIWLHAAEVYIGIGKPAEATACTQEAANLFPMSHNVLYMRGQIAELRGSMDEARRWYEEALAISPTHVKSMQRLALILHQLGRYSLAEKILRDAVQVNSTAHEVWNGLGEVLQAQGNDAAATECFLTALELEASSPAVPFTIIPRVL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000000CC5D","uniref100":"UniRef100_Q86TV6","uniref90":"UniRef90_Q86TV6","uniref50":"UniRef50_Q86TV6","genes":[{"name":{"value":"TTC7B"},"synonyms":[{"value":"TTC7L1"}]}],"alphafold_very_low_content":0.099644128113879,"disorder_content":0.13048635824436536,"disprot_consensus":{"full":[{"start":157,"end":166,"type":"D"},{"start":197,"end":212,"type":"D"},{"start":343,"end":358,"type":"D"},{"start":619,"end":686,"type":"D"}],"Structural state":[{"start":157,"end":166,"type":"D"},{"start":197,"end":212,"type":"D"},{"start":343,"end":358,"type":"D"},{"start":619,"end":686,"type":"D"}]}},{"disprot_id":"DP03115","acc":"Q6P4R8","creator":"ldobson","date":"2021-01-08T10:56:22.690Z","features":{"pfam":[{"id":"PF14465","name":"NFRKB Winged Helix-like","start":379,"end":478},{"id":"PF25793","name":"NFRKB second winged helix domain","start":518,"end":657}],"gene3D":[]},"length":1299,"name":"Nuclear factor related to kappa-B-binding protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":483,"end":495,"reference_id":"22984442","reference_source":"pmid","reference_html":"Structure of a novel winged-helix like domain from human NFRKB protein. <i> Kumar A, Möcklinghoff S, Yumoto F, Jaroszewski L, Farr CL, Grzechnik A, Nguyen P, Weichenberger CX, Chiu HJ, Klock HE, Elsliger MA, Deacon AM, Godzik A, Lesley SA, Conklin BR, Fletterick RJ, Wilson IA. </i> PLoS One, 2012","date":"2023-06-14T13:17:24.277Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"3U21"}],"region_id":"DP03115r001","statement":[{"text":"The last 12 residues of the construct (residues 484–495) were disordered and were not modeled.","type":"Results"},{"text":"Region bundaries are updated according to PDB file","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:923"}],"construct_alterations":[{"term_id":"MOD:00084","term_name":"N6,N6-dimethyl-L-lysine","term_namespace":"Protein modification","start":452,"end":452,"position":"Specific residue"},{"term_id":"MOD:00083","term_name":"N6,N6,N6-trimethyl-L-lysine","term_namespace":"Protein modification","start":454,"end":454,"position":"Specific residue"},{"term_id":"MOD:00083","term_name":"N6,N6,N6-trimethyl-L-lysine","term_namespace":"Protein modification","start":459,"end":459,"position":"Specific residue"},{"term_id":"MOD:00083","term_name":"N6,N6,N6-trimethyl-L-lysine","term_namespace":"Protein modification","start":469,"end":469,"position":"Specific residue"},{"term_id":"MOD:00083","term_name":"N6,N6,N6-trimethyl-L-lysine","term_namespace":"Protein modification","start":482,"end":482,"position":"Specific residue"},{"term_id":"MOD:00083","term_name":"N6,N6,N6-trimethyl-L-lysine","term_namespace":"Protein modification","start":488,"end":488,"position":"Specific residue"}],"sequence_construct":"GLGINEISSSFFSLLLEILLLESQASLPMLEERVLDWQSSPASSLNSWFSAAPNWAELVLPALQYLAGESRAVPSSFSPFVEFKEKTQQWKLLGQSQDNEKELAALFQLWLETKDQAFCKQENEDSS","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-16T12:54:22.353Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MDSLDHMLTDPLELGPCGDGHGTRIMEDCLLGGTRVSLPEDLLEDPEIFFDVVSLSTWQEVLSDSQREHLQQFLPQFPEDSAEQQNELILALFSGENFRFGNPLHIAQKLFRDGHFNPEVVKYRQLCFKSQYKRYLNSQQQYFHRLLKQILASRSDLLEMARRSGPALPFRQKRPSPSRTPEEREWRTQQRYLKVLREVKEECGDTALSSDEEDLSSWLPSSPARSPSPAVPLRVVPTLSTTDMKTADKVELGDSDLKIMLKKHHEKRKHQPDHPDLLTGDLTLNDIMTRVNAGRKGSLAALYDLAVLKKKVKEKEEKKKKKIKTIKSEAEDLAEPLSSTEGVAPLSQAPSPLAIPAIKEEPLEDLKPCLGINEISSSFFSLLLEILLLESQASLPMLEERVLDWQSSPASSLNSWFSAAPNWAELVLPALQYLAGESRAVPSSFSPFVEFKEKTQQWKLLGQSQDNEKELAALFQLWLETKDQAFCKQENEDSSDATTPVPRVRTDYVVRPSTGEEKRVFQEQERYRYSQPHKAFTFRMHGFESVVGPVKGVFDKETSLNKAREHSLLRSDRPAYVTILSLVRDAAARLPNGEGTRAEICELLKDSQFLAPDVTSTQVNTVVSGALDRLHYEKDPCVKYDIGRKLWIYLHRDRSEEEFERIHQAQAAAAKARKALQQKPKPPSKVKSSSKESSIKVLSSGPSEQSQMSLSDSSMPPTPVTPVTPTTPALPAIPISPPPVSAVNKSGPSTVSEPAKSSSGVLLVSSPTMPHLGTMLSPASSQTAPSSQAAARVVSHSGSAGLSQVRVVAQPSLPAVPQQSGGPAQTLPQMPAGPQIRVPATATQTKVVPQTVMATVPVKAQTTAATVQRPGPGQTGLTVTSLPATASPVSKPATSSPGTSAPSASTAAVIQNVTGQNIIKQVAITGQLGVKPQTGNSIPLTATNFRIQGKDVLRLPPSSITTDAKGQTVLRITPDMMATLAKSQVTTVKLTQDLFGTGGNTTGKGISATLHVTSNPVHAADSPAKASSASAPSSTPTGTTVVKVTPDLKPTEASSSAFRLMPALGVSVADQKGKSTVASSEAKPAATIRIVQGLGVMPPKAGQTITVATHAKQGASVASGSGTVHTSAVSLPSMNAAVSKTVAVASGAASTPISISTGAPTVRQVPVSTTVVSTSQAGKLPTRITVPLSVISQPMKGKSVVTAPIIKGNLGANLSGLGRNIILTTMPAGTKLIAGNKPVSFLTAQQLQQLQQQGQATQVRIQTVPASHLQQGTASGSSKAVSTVVVTTAPSPKQAPEQQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI0000226313","uniref100":"UniRef100_Q6P4R8","uniref90":"UniRef90_Q6P4R8","uniref50":"UniRef50_Q6P4R8","genes":[{"name":{"value":"NFRKB"},"synonyms":[{"value":"INO80G"}]}],"alphafold_very_low_content":0.5742879137798307,"disorder_content":0.010007698229407237,"disprot_consensus":{"full":[{"start":483,"end":495,"type":"D"}],"Structural state":[{"start":483,"end":495,"type":"D"}]}},{"disprot_id":"DP03116","acc":"O95155","creator":"mpajkos","date":"2021-01-08T11:12:56.898Z","features":{"pfam":[{"id":"PF04564","name":"U-box domain","start":1228,"end":1299},{"id":"PF10408","name":"Ubiquitin elongating factor core","start":591,"end":1212}],"gene3D":[]},"length":1302,"name":"Ubiquitin conjugation factor E4 B","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1208,"end":1227,"reference_id":"20696396","reference_source":"pmid","reference_html":"Molecular basis for the association of human E4B U box ubiquitin ligase with E2-conjugating enzymes UbcH5c and Ubc4. <i> Benirschke RC, Thompson JR, Nominé Y, Wasielewski E, Juranić N, Macura S, Hatakeyama S, Nakayama KI, Botuyan MV, Mer G. </i> Structure, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"mpajkos","curator_name":"Mátyás Pajkos","curator_orcid":"0000-0001-5791-9825","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"2KRE"}],"region_id":"DP03116r001","statement":[{"text":"The first 20 N-terminal amino acids of the E4B construct used for structure determination (aa 1208-1302) lack a defined conformation and connect to a long loop (L1: Ala1228 - Asp1243) that extends to a first β-strand (B1: Pro1244 - Leu1247).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-08T14:31:10.288Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1208,"end":1225,"reference_id":"20696396","reference_source":"pmid","reference_html":"Molecular basis for the association of human E4B U box ubiquitin ligase with E2-conjugating enzymes UbcH5c and Ubc4. <i> Benirschke RC, Thompson JR, Nominé Y, Wasielewski E, Juranić N, Macura S, Hatakeyama S, Nakayama KI, Botuyan MV, Mer G. </i> Structure, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"mpajkos","curator_name":"Mátyás Pajkos","curator_orcid":"0000-0001-5791-9825","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"3L1X"}],"region_id":"DP03116r002","statement":[{"text":"The resulting electron density map has a good fit for most regions of E4B and UbcH5c, except for the first eighteen N-terminal residues (aa 1208-1225) and last two C-terminal residues (1301 and 1302) of E4B, which are not visible in the electron density.","type":"Results"},{"text":"The solved structure is the U-box Domain of Human E4B Ubiquitin Ligase","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-08T14:54:50.217Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1208,"end":1222,"reference_id":"20696396","reference_source":"pmid","reference_html":"Molecular basis for the association of human E4B U box ubiquitin ligase with E2-conjugating enzymes UbcH5c and Ubc4. <i> Benirschke RC, Thompson JR, Nominé Y, Wasielewski E, Juranić N, Macura S, Hatakeyama S, Nakayama KI, Botuyan MV, Mer G. </i> Structure, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"mpajkos","curator_name":"Mátyás Pajkos","curator_orcid":"0000-0001-5791-9825","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"3L1Z"}],"region_id":"DP03116r003","statement":[{"text":"The resulting electron density map has a good fit for most regions of E4B and UbcH5c, except for the first eighteen N-terminal residues (aa 1208-1225) and last two C-terminal residues (1301 and 1302) of E4B, which are not visible in the electron density.","type":"Results"},{"text":"the solved structure is the the U-BOX domain of human E4B ubiquitin ligase in complex with UBCH5C E2 ubiquitin conjugating enzyme","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-08T14:54:50.981Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2023_12","sequence":"MEELSADEIRRRRLARLAGGQTSQPTTPLTSPQRENPPGPPIAASAPGPSQSLGLNVHNMTPATSPIGASGVAHRSQSSEGVSSLSSSPSNSLETQSQSLSRSQSMDIDGVSCEKSMSQVDVDSGIENMEVDENDRREKRSLSDKEPSSGPEVSEEQALQLVCKIFRVSWKDRDRDVIFLSSLSAQFKQNPKEVFSDFKDLIGQILMEVLMMSTQTRDENPFASLTATSQPIAAAARSPDRNLLLNTGSNPGTSPMFCSVASFGASSLSSLYESSPAPTPSFWSSVPVMGPSLASPSRAASQLAVPSTPLSPHSAASGTAAGSQPSSPRYRPYTVTHPWASSGVSILSSSPSPPALASSPQAVPASSSRQRPSSTGPPLPPASPSATSRRPSSLRISPSLGASGGASNWDSYSDHFTIETCKETDMLNYLIECFDRVGIEEKKAPKMCSQPAVSQLLSNIRSQCISHTALVLQGSLTQPRSLQQPSFLVPYMLCRNLPYGFIQELVRTTHQDEEVFKQIFIPILQGLALAAKECSLDSDYFKYPLMALGELCETKFGKTHPVCNLVASLRLWLPKSLSPGCGRELQRLSYLGAFFSFSVFAEDDVKVVEKYFSGPAITLENTRVVSQSLQHYLELGRQELFKILHSILLNGETREAALSYMAAVVNANMKKAQMQTDDRLVSTDGFMLNFLWVLQQLSTKIKLETVDPTYIFHPRCRITLPNDETRVNATMEDVNDWLTELYGDQPPFSEPKFPTECFFLTLHAHHLSILPSCRRYIRRLRAIRELNRTVEDLKNNESQWKDSPLATRHREMLKRCKTQLKKLVRCKACADAGLLDESFLRRCLNFYGLLIQLLLRILDPAYPDITLPLNSDVPKVFAALPEFYVEDVAEFLFFIVQYSPQALYEPCTQDIVMFLVVMLCNQNYIRNPYLVAKLVEVMFMTNPAVQPRTQKFFEMIENHPLSTKLLVPSLMKFYTDVEHTGATSEFYDKFTIRYHISTIFKSLWQNIAHHGTFMEEFNSGKQFVRYINMLINDTTFLLDESLESLKRIHEVQEEMKNKEQWDQLPRDQQQARQSQLAQDERVSRSYLALATETVDMFHILTKQVQKPFLRPELGPRLAAMLNFNLQQLCGPKCRDLKVENPEKYGFEPKKLLDQLTDIYLQLDCARFAKAIADDQRSYSKELFEEVISKMRKAGIKSTIAIEKFKLLAEKVEEIVAKNARAEIDYSDAPDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQTLTESMLEPVPELKEQIQAWMREKQNSDH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI0000137944","uniref100":"UniRef100_O95155","uniref90":"UniRef90_O95155","uniref50":"UniRef50_Q9ES00","genes":[{"name":{"value":"UBE4B","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:12500","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:12500"}}]},"synonyms":[{"value":"HDNB1","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"BAB40446.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAB40446.1"}}]},{"value":"KIAA0684","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"BAA31659.3","url":"https://www.ebi.ac.uk/ena/browser/view/BAA31659.3"}}]},{"value":"UFD2","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAD02233.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD02233.1"}}]}]}],"alphafold_very_low_content":0.24961597542242703,"disorder_content":0.015360983102918587,"disprot_consensus":{"full":[{"start":1208,"end":1227,"type":"D"}],"Structural state":[{"start":1208,"end":1227,"type":"D"}]}},{"disprot_id":"DP03118","acc":"P30793","creator":"viglesias","date":"2021-01-08T11:42:08.015Z","features":{"pfam":[{"id":"PF01227","name":"GTP cyclohydrolase I","start":73,"end":249}],"gene3D":[]},"length":250,"name":"GTP cyclohydrolase 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":42,"end":57,"reference_id":"33387654","reference_source":"pmid","reference_html":"Biophysical and structural investigation of the regulation of human GTP cyclohydrolase I by its regulatory protein GFRP. <i> Ebenhoch R, Bauer M, Reinert D, Kersting A, Huber S, Schmid A, Hinz I, Feiler M, Müller K, Nar H. </i> J Struct Biol, 2021","date":"2023-05-10T09:55:19.213Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":3,"region_id":"DP03118r001","statement":[{"text":"The region 42-57 is missing in the electron density in the PDB structures, indicating disorder.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","cross_refs":[{"db":"PDB","id":"7ALQ"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-10T13:28:22.320Z"}},{"start":1,"end":42,"reference_id":"11087827","reference_source":"pmid","reference_html":"Zinc plays a key role in human and bacterial GTP cyclohydrolase I. <i> Auerbach G, Herrmann A, Bracher A, Bader G, Gutlich M, Fischer M, Neukamm M, Garrido-Franco M, Richardson J, Nar H, Huber R, Bacher A. </i> Proc Natl Acad Sci U S A, 2000","date":"2023-05-09T08:29:15.164Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":3,"region_id":"DP03118r002","statement":[{"text":"All attempts to purify this protein yielded mixtures of partially proteolyzed polypeptides as shown by SDS/PAGE. N-terminal sequencing showed that different subunits had been proteolyzed at any one of eight Arg residues in the N-terminal stretch of 41 residues, affording a variety of cleavage products.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-09T13:06:09.946Z"}}],"regions_counter":2,"released":"2021_12","sequence":"MEKGPVRAPAEKPRGARCSNGFPERDPPRPGPSRPAEKPPRPEAKSAQPADGWKGERPRSEEDNELNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIRS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Age-related disorders proteins"],"UniParc":"UPI0000001289","uniref100":"UniRef100_P30793","uniref90":"UniRef90_P30793","uniref50":"UniRef50_P30793","genes":[{"name":{"value":"GCH1"},"synonyms":[{"value":"DYT5"},{"value":"GCH"}]}],"alphafold_very_low_content":0.096,"disorder_content":0.228,"disprot_consensus":{"full":[{"start":1,"end":57,"type":"D"}],"Structural state":[{"start":1,"end":57,"type":"D"}]}},{"disprot_id":"DP03120","acc":"Q9HC77","creator":"tszani","date":"2021-01-08T13:35:45.323Z","features":{"pfam":[{"id":"PF07202","name":"T-complex protein 10 C-terminus","start":1151,"end":1181},{"id":"PF07202","name":"T-complex protein 10 C-terminus","start":1221,"end":1249},{"id":"PF07202","name":"T-complex protein 10 C-terminus","start":1257,"end":1291},{"id":"PF07202","name":"T-complex protein 10 C-terminus","start":1296,"end":1325},{"id":"PF25779","name":"CPAP, tubulin-binding region","start":321,"end":387}],"gene3D":[]},"length":1338,"name":"Centromere protein J","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":311,"end":348,"reference_id":"19131341","reference_source":"pmid","reference_html":"The PN2-3 domain of centrosomal P4.1-associated protein implements a novel mechanism for tubulin sequestration. <i> Cormier A, Clément MJ, Knossow M, Lachkar S, Savarin P, Toma F, Sobel A, Gigant B, Curmi PA. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03120r001","statement":[{"text":"NMR data show that PN2-3 does not fold into a well defined tertiary structure but that a 23-residue region (from residues 29 to 51) is predominantly α-helical in agreement with CD measurements. ","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-02-17T17:41:05.223Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":361,"end":422,"reference_id":"19131341","reference_source":"pmid","reference_html":"The PN2-3 domain of centrosomal P4.1-associated protein implements a novel mechanism for tubulin sequestration. <i> Cormier A, Clément MJ, Knossow M, Lachkar S, Savarin P, Toma F, Sobel A, Gigant B, Curmi PA. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03120r002","statement":[{"text":"NMR data show that PN2-3 does not fold into a well defined tertiary structure but that a 23-residue region (from residues 29 to 51) is predominantly α-helical in agreement with CD measurements. ","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-02-17T17:41:05.990Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2023_06","sequence":"MFLMPTSSELNSGQNFLTQWMTNPSRAGVILNRGFPILEADKEKRAAVDISTSFPIKGTHFSDSFSFINEEDSLLEEQKLESNNPYKPQSDKSETHTAFPCIKKGPQVAACHSAPGHQEENKNDFIPDLASEFKEGAYKDPLFKKLEQLKEVQQKKQEQLKRQQLEQLQRLMEEQEKLLTMVSGQCTLPGLSLLPDDQSQKHRSPGNTTTGERATCCFPSYVYPDPTQEETYPSNILSHEQSNFCRTAHGDFVLTSKRASPNLFSEAQYQEAPVEKNNLKEENRNHPTGESILCWEKVTEQIQEANDKNLQKHDDSSEVANIEERPIKAAIGERKQTFEDYLEEQIQLEEQELKQKQLKEAEGPLPIKAKPKQPFLKRGEGLARFTNAKSKFQKGKESKLVTNQSTSEDQPLFKMDRQQLQRKTALKNKELCADNPILKKDSKARTKSGSVTLSQKPKMLKCSNRKSLSPSGLKIQTGKKCDGQFRDQIKFENKVTSNNKENVTECPKPCDTGCTGWNKTQGKDRLPLSTGPASRLAAKSPIRETMKESESSLDVSLQKKLETWEREKEKENLELDEFLFLEQAADEISFSSNSSFVLKILERDQQICKGHRMSSTPVKAVPQKTNPADPISHCNRSEDLDHTAREKESECEVAPKQLHSLSSADELREQPCKIRKAVQKSTSENQTEWNARDDEGVPNSDSSTDSEEQLDVTIKPSTEDRERGISSREDSPQVCDDKGPFKDTRTQEDKRRDVDLDLSDKDYSSDESIMESIKHKVSEPSRSSSLSLSKMDFDDERTWTDLEENLCNHDVVLGNESTYGTPQTCYPNNEIGILDKTIKRKIAPVKRGEDLSKSRRSRSPPTSELMMKFFPSLKPKPKSDSHLGNELKLNISQDQPPGDNARSQVLREKIIELETEIEKFKAENASLAKLRIERESALEKLRKEIADFEQQKAKELARIEEFKKEEMRKLQKERKVFEKYTTAARTFPDKKEREEIQTLKQQIADLREDLKRKETKWSSTHSRLRSQIQMLVRENTDLREEIKVMERFRLDAWKRAEAIESSLEVEKKDKLANTSVRFQNSQISSGTQVEKYKKNYLPMQGNPPRRSKSAPPRDLGNLDKGQAASPREPLEPLNFPDPEYKEEEEDQDIQGEISHPDGKVEKVYKNGCRVILFPNGTRKEVSADGKTITVTFFNGDVKQVMPDQRVIYYYAAAQTTHTTYPEGLEVLHFSSGQIEKHYPDGRKEITFPDQTVKNLFPDGQEESIFPDGTIVRVQRDGNKLIEFNNGQRELHTAQFKRREYPDGTVKTVYANGHQETKYRSGRIRVKDKEGNVLMDTEL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Age-related disorders proteins"],"UniParc":"UPI000006F758","uniref100":"UniRef100_Q9HC77","uniref90":"UniRef90_Q9HC77","uniref50":"UniRef50_Q9HC77","genes":[{"name":{"value":"CENPJ"},"synonyms":[{"value":"CPAP"},{"value":"LAP"},{"value":"LIP1"}]}],"alphafold_very_low_content":0.6150971599402093,"disorder_content":0.07473841554559044,"disprot_consensus":{"full":[{"start":311,"end":348,"type":"D"},{"start":361,"end":422,"type":"D"}],"Structural state":[{"start":311,"end":348,"type":"D"},{"start":361,"end":422,"type":"D"}]}},{"disprot_id":"DP03121","acc":"P11686","creator":"ldobson","date":"2021-01-08T15:14:49.791Z","features":{"pfam":[{"id":"PF04089","name":"BRICHOS domain","start":98,"end":196},{"id":"PF08999","name":"Surfactant protein C, N terminal propeptide","start":1,"end":93}],"gene3D":[]},"length":197,"name":"Pulmonary surfactant-associated protein C","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":151,"end":182,"reference_id":"22308375","reference_source":"pmid","reference_html":"High-resolution structure of a BRICHOS domain and its implications for anti-amyloid chaperone activity on lung surfactant protein C. <i> Willander H, Askarieh G, Landreh M, Westermark P, Nordling K, Keränen H, Hermansson E, Hamvas A, Nogee LM, Bergman T, Saenz A, Casals C, Åqvistg J, Jörnvall H, Berglund H, Presto J, Knight SD, Johansson J. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2YAD"}],"region_id":"DP03121r001","statement":[{"text":"Residues 149–180 and 82–88, corresponding to the disordered regions defined by HDX-MS of intact CTC (Fig. 1A) and encompassing the proteolyzed 161–167 segment, have little visible electron density in our maps and were not modeled (Fig. 1B).","type":"Results"},{"text":"IDR region boundaries were modified according to alignment of the PDB and UniProt sequences","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-04T09:18:11.694Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":59,"end":89,"reference_id":"22308375","reference_source":"pmid","reference_html":"High-resolution structure of a BRICHOS domain and its implications for anti-amyloid chaperone activity on lung surfactant protein C. <i> Willander H, Askarieh G, Landreh M, Westermark P, Nordling K, Keränen H, Hermansson E, Hamvas A, Nogee LM, Bergman T, Saenz A, Casals C, Åqvistg J, Jörnvall H, Berglund H, Presto J, Knight SD, Johansson J. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2YAD"}],"region_id":"DP03121r002","statement":[{"text":"The paper does not state this region is IDR, however atomic coordinates are missing from the PDB file. 3 Met residues present in this region were not included in the PDB protein construct.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-04T09:18:10.476Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":59,"end":89,"reference_id":"22308375","reference_source":"pmid","reference_html":"High-resolution structure of a BRICHOS domain and its implications for anti-amyloid chaperone activity on lung surfactant protein C. <i> Willander H, Askarieh G, Landreh M, Westermark P, Nordling K, Keränen H, Hermansson E, Hamvas A, Nogee LM, Bergman T, Saenz A, Casals C, Åqvistg J, Jörnvall H, Berglund H, Presto J, Knight SD, Johansson J. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"2YAD"}],"region_id":"DP03121r003","statement":[{"text":" Surfactant protein C proprotein (proSP-C) contains four regions; a short N-terminal segment (residues 1–23) facing the cytosol and important for intracellular trafficking, a transmembrane (TM) region constituting the main part of mature SP-C (residues 24–58) eventually secreted with phospholipids into the alveoli, a linker region (residues 59–89), and a BRICHOS domain (residues 90–197), defined from the structure presented here and localized to the ER lumen (1) (Fig. 1A)","type":"Introduction"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-04T09:18:13.377Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":3,"released":"2021_06","sequence":"MDVGSKEVLMESPPDYSAAPRGRFGIPCCPVHLKRLLIVVVVVVLIVVVIVGALLMGLHMSQKHTEMVLEMSIGAPEAQQRLALSEHLVTTATFSIGSTGLVVYDYQQLLIAYKPAPGTCCYIMKIAPESIPSLEALTRKVHNFQMECSLQAKPAVPTSKLGQAEGRDAGSAPSGGDPAFLGMAVSTLCGEVPLYYI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000016AED0","uniref100":"UniRef100_P11686","uniref90":"UniRef90_P11686","uniref50":"UniRef50_P11686","genes":[{"name":{"value":"SFTPC"},"synonyms":[{"value":"SFTP2"}]}],"alphafold_very_low_content":0.2639593908629442,"disorder_content":0.3197969543147208,"disprot_consensus":{"full":[{"start":59,"end":89,"type":"D"},{"start":151,"end":182,"type":"D"}],"Structural state":[{"start":59,"end":89,"type":"D"},{"start":151,"end":182,"type":"D"}],"Disorder function":[{"start":59,"end":89,"type":"F"}]}},{"disprot_id":"DP03122","acc":"Q14691","creator":"ldobson","date":"2021-01-08T15:29:05.522Z","features":{"pfam":[{"id":"PF05916","name":"GINS complex protein helical bundle domain","start":42,"end":128},{"id":"PF24997","name":"PSF1 C-terminal domain","start":144,"end":195}],"gene3D":[]},"length":196,"name":"DNA replication complex GINS protein PSF1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":146,"end":196,"reference_id":"17652513","reference_source":"pmid","reference_html":"Crystal structure of the GINS complex and functional insights into its role in DNA replication. <i> Chang YP, Wang G, Bermudez V, Hurwitz J, Chen XS. </i> Proc Natl Acad Sci U S A, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2Q9Q"}],"region_id":"DP03122r001","statement":[{"text":"Psf1 has only an α-domain (residues 1–145), whereas all of its C-terminal 51 residues are disordered.","type":"Results"},{"text":"Possibly not IDR? \"Kamada et al. (13) reported that their GINS complex crystallized only when a Psf1 mutant lacking the C-terminal 47 residues (14) was used, suggesting that the presence of this β-domain inhibited crystal packing of the GINS complex. Kamada et al. (13) proposed that the deleted region of Psf1 folds into a β-domain structure and that the correct positioning of this domain on the surface of the GINS complex is critical for function.\"","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":146,"end":196,"reference_id":"17652513","reference_source":"pmid","reference_html":"Crystal structure of the GINS complex and functional insights into its role in DNA replication. <i> Chang YP, Wang G, Bermudez V, Hurwitz J, Chen XS. </i> Proc Natl Acad Sci U S A, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"2Q9Q"}],"region_id":"DP03122r002","statement":[{"text":"The last visible C-terminal residue of Psf1 (S145) before the disordered C-terminal domain is adjacent to the disordered fragment of Sld5 (residue 65–71) and to the disordered C-terminal residues of Psf3 (residues 194–216); these disordered regions are shown as spheres in Fig. 3d. The colocalization of these disordered parts of three different subunits on the GINS surface suggests that this site may bind partner proteins in the replication complex.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":2,"released":"2021_12","sequence":"MFCEKAMELIRELHRAPEGQLPAFNEDGLRQVLEEMKALYEQNQSDVNEAKSGGRSDLIPTIKFRHCSLLRNRRCTVAYLYDRLLRIRALRWEYGSVLPNALRFHMAAEEMEWFNNYKRSLATYMRSLGGDEGLDITQDMKPPKSLYIEVRCLKDYGEFEVDDGTSVLLKKNSQHFLPRWKCEQLIRQGVLEHILS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI00001393F9","uniref100":"UniRef100_Q14691","uniref90":"UniRef90_Q14691","uniref50":"UniRef50_Q14691","genes":[{"name":{"value":"GINS1"},"synonyms":[{"value":"KIAA0186"},{"value":"PSF1"}]}],"alphafold_very_low_content":0,"disorder_content":0.2602040816326531,"disprot_consensus":{"full":[{"start":146,"end":196,"type":"D"}],"Structural state":[{"start":146,"end":196,"type":"D"}],"Molecular function":[{"start":146,"end":196,"type":"F"}]}},{"disprot_id":"DP03123","acc":"Q9BRX5","creator":"ldobson","date":"2021-01-08T15:37:27.285Z","features":{"pfam":[{"id":"PF05916","name":"GINS complex protein helical bundle domain","start":96,"end":189},{"id":"PF22466","name":"PSF3 N-terminal domain","start":21,"end":77}],"gene3D":[]},"length":216,"name":"DNA replication complex GINS protein PSF3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":194,"end":216,"reference_id":"17652513","reference_source":"pmid","reference_html":"Crystal structure of the GINS complex and functional insights into its role in DNA replication. <i> Chang YP, Wang G, Bermudez V, Hurwitz J, Chen XS. </i> Proc Natl Acad Sci U S A, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2Q9Q"}],"region_id":"DP03123r001","statement":[{"text":"The last visible C-terminal residue of Psf1 (S145) before the disordered C-terminal domain is adjacent to the disordered fragment of Sld5 (residue 65–71) and to the disordered C-terminal residues of Psf3 (residues 194–216); these disordered regions are shown as spheres in Fig. 3d. ","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":194,"end":216,"reference_id":"17652513","reference_source":"pmid","reference_html":"Crystal structure of the GINS complex and functional insights into its role in DNA replication. <i> Chang YP, Wang G, Bermudez V, Hurwitz J, Chen XS. </i> Proc Natl Acad Sci U S A, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"2Q9Q"}],"region_id":"DP03123r002","statement":[{"text":"The last visible C-terminal residue of Psf1 (S145) before the disordered C-terminal domain is adjacent to the disordered fragment of Sld5 (residue 65–71) and to the disordered C-terminal residues of Psf3 (residues 194–216); these disordered regions are shown as spheres in Fig. 3d. The colocalization of these disordered parts of three different subunits on the GINS surface suggests that this site may bind partner proteins in the replication complex.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":2,"released":"2021_12","sequence":"MSEAYFRVESGALGPEENFLSLDDILMSHEKLPVRTETAMPRLGAFFLERSAGAETDNAVPQGSKLELPLWLAKGLFDNKRRILSVELPKIYQEGWRTVFSADPNVVDLHKMGPHFYGFGSQLLHFDSPENADISQSLLQTFIGRFRRIMDSSQNAYNEDTSALVARLDEMERGLFQTGQKGLNDFQCWEKGQASQITASNLVQNYKKRKFTDMED","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000006D678","uniref100":"UniRef100_Q9BRX5","uniref90":"UniRef90_Q9BRX5","uniref50":"UniRef50_Q9BRX5","genes":[{"name":{"value":"GINS3"},"synonyms":[{"value":"PSF3"}]}],"alphafold_very_low_content":0.004629629629629629,"disorder_content":0.10648148148148148,"disprot_consensus":{"full":[{"start":194,"end":216,"type":"D"}],"Structural state":[{"start":194,"end":216,"type":"D"}],"Molecular function":[{"start":194,"end":216,"type":"F"}]}},{"disprot_id":"DP03124","acc":"O95835","creator":"tszani","date":"2021-01-08T16:04:35.500Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":706,"end":854},{"id":"PF00069","name":"Protein kinase domain","start":904,"end":1010},{"id":"PF00433","name":"Protein kinase C terminal domain","start":1030,"end":1080},{"id":"PF00627","name":"UBA/TS-N domain","start":101,"end":138}],"gene3D":[]},"length":1130,"name":"Serine/threonine-protein kinase LATS1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":622,"end":635,"reference_id":"27335147","reference_source":"pmid","reference_html":"Structural basis for autoinhibition and its relief of MOB1 in the Hippo pathway. <i> Kim SY, Tachioka Y, Mori T, Hakoshima T. </i> Sci Rep, 2016","date":"2022-06-24T18:05:43.466Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":3,"cross_refs":[{"db":"PDB","id":"5B5W"}],"region_id":"DP03124r001","statement":[{"text":"The secondary structure elements of our structure are shown at the top with broken lines for residues undefined in the current electron density map. ","type":"Figure"},{"text":"The N-terminal 14 residues and a short C-terminal segment comprising 5 residues are unstructured (broken lines). ","type":"Figure"}],"ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8BPB0"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-26T17:12:12.460Z"}},{"start":361,"end":567,"reference_id":"29487715","reference_source":"pmid","reference_html":"Biophysical studies and NMR structure of YAP2 WW domain - LATS1 PPxY motif complexes reveal the basis of their interaction. <i> Verma A, Jing-Song F, Finch-Edmondson ML, Velazquez-Campoy A, Balasegaran S, Sudol M, Sivaraman J. </i> Oncotarget, 2018","date":"2022-06-27T14:38:30.901Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03124r002","statement":[{"text":"15N-labelled PY12 (containing both PPxY motifs; aa 361–567) was titrated against unlabeled WW12 (containing both WW domains; aa 163–266). The HSQCs of the free and bound PY12 were compared to observe changes in the peaks. The HSQC of free PY12 shows that the protein is unstructured, as most of the peaks are clustered together around the 1H chemical shift 8 ppm (Figure 6A green).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-27T14:52:29.310Z"}}],"regions_counter":2,"released":"2022_06","sequence":"MKRSEKPEGYRQMRPKTFPASNYTVSSRQMLQEIRESLRNLSKPSDAAKAEHNMSKMSTEDPRQVRNPPKFGTHHKALQEIRNSLLPFANETNSSRSTSEVNPQMLQDLQAAGFDEDMVIQALQKTNNRSIEAAIEFISKMSYQDPRREQMAAAAARPINASMKPGNVQQSVNRKQSWKGSKESLVPQRHGPPLGESVAYHSESPNSQTDVGRPLSGSGISAFVQAHPSNGQRVNPPPPPQVRSVTPPPPPRGQTPPPRGTTPPPPSWEPNSQTKRYSGNMEYVISRISPVPPGAWQEGYPPPPLNTSPMNPPNQGQRGISSVPVGRQPIIMQSSSKFNFPSGRPGMQNGTGQTDFMIHQNVVPAGTVNRQPPPPYPLTAANGQSPSALQTGGSAAPSSYTNGSIPQSMMVPNRNSHNMELYNISVPGLQTNWPQSSSAPAQSSPSSGHEIPTWQPNIPVRSNSFNNPLGNRASHSANSQPSATTVTAITPAPIQQPVKSMRVLKPELQTALAPTHPSWIPQPIQTVQPSPFPEGTASNVTVMPPVAEAPNYQGPPPPYPKHLLHQNPSVPPYESISKPSKEDQPSLPKEDESEKSYENVDSGDKEKKQITTSPITVRKNKKDEERRESRIQSYSPQAFKFFMEQHVENVLKSHQQRLHRKKQLENEMMRVGLSQDAQDQMRKMLCQKESNYIRLKRAKMDKSMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMGIFPESLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYYQSGDHPRQDSMDFSNEWGDPSSCRCGDRLKPLERRAARQHQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCRGPEDRLGKNGADEIKAHPFFKTIDFSSDLRQQSASYIPKITHPTDTSNFDPVDPDKLWSDDNEEENVNDTLNGWYKNGKHPEHAFYEFTFRRFFDDNGYPYNYPKPIEYEYINSQGSEQQSDEDDQNTGSEIKNRDLVYV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI0000073DC2","uniref100":"UniRef100_O95835","uniref90":"UniRef90_O95835","uniref50":"UniRef50_O95835","genes":[{"name":{"value":"LATS1","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAD16882.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD16882.1"}}]},"synonyms":[{"value":"WARTS","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAD50272.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD50272.1"}}]}]}],"alphafold_very_low_content":0.5796460176991151,"disorder_content":0.19557522123893806,"disprot_consensus":{"full":[{"start":361,"end":567,"type":"D"},{"start":622,"end":635,"type":"D"}],"Structural state":[{"start":361,"end":567,"type":"D"},{"start":622,"end":635,"type":"D"}]}},{"disprot_id":"DP03125","acc":"O14965","creator":"tszani","date":"2021-01-08T16:33:19.880Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":133,"end":383}],"gene3D":[]},"length":403,"name":"Aurora kinase A","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":279,"end":288,"reference_id":"12237287","reference_source":"pmid","reference_html":"Crystal structure of aurora-2, an oncogenic serine/threonine kinase. <i> Cheetham GM, Knegtel RM, Coll JT, Renwick SB, Swenson L, Weber P, Lippke JA, Austen DA. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1MUO"}],"region_id":"DP03125r001","statement":[{"text":"As observed in the structures of CSK kinase (c-SRC-specific tyrosine kinase) bound to staurosporine (27) and the SRC family kinase HCK (human Cyclin-dependent kinase) bound to AMP-PNP (25), a part of the Aurora-2 activation loop (defined as residues 273–292) is disordered. Only residues 273–278 and 289–292 were clearly visible and have been included in the final model. Residue Thr-288, which is phosphorylated during activation of Aurora-2, belongs to part of the disordered region and was not visible in electron density maps","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-12T17:11:12.624Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":107,"end":127,"reference_id":"12237287","reference_source":"pmid","reference_html":"Crystal structure of aurora-2, an oncogenic serine/threonine kinase. <i> Cheetham GM, Knegtel RM, Coll JT, Renwick SB, Swenson L, Weber P, Lippke JA, Austen DA. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1MUO"}],"region_id":"DP03125r002","statement":[{"text":"In the refined crystal structure, a number of residues located at the N and C termini of the kinase domain (residues 107–127 and 389–403, respectively) exhibited poor electron density, and these residues could not be placed in electron density","type":"Results"},{"text":"Accordingly, an expression construct comprising residues 107–403 was used for crystallographic studies. The disordered nature of residues 107–126 in the final crystal structure suggests that this spanning polypeptide linker is particularly long and flexible in Aurora-2","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-12T17:11:24.130Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":389,"end":403,"reference_id":"12237287","reference_source":"pmid","reference_html":"Crystal structure of aurora-2, an oncogenic serine/threonine kinase. <i> Cheetham GM, Knegtel RM, Coll JT, Renwick SB, Swenson L, Weber P, Lippke JA, Austen DA. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1MUO"}],"region_id":"DP03125r003","statement":[{"text":"In the refined crystal structure, a number of residues located at the N and C termini of the kinase domain (residues 107–127 and 389–403, respectively) exhibited poor electron density, and these residues could not be placed in electron density","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-12T17:11:25.656Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":273,"end":292,"reference_id":"12237287","reference_source":"pmid","reference_html":"Crystal structure of aurora-2, an oncogenic serine/threonine kinase. <i> Cheetham GM, Knegtel RM, Coll JT, Renwick SB, Swenson L, Weber P, Lippke JA, Austen DA. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"GO:0140677","term_name":"molecular function activator activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"1MUO"}],"region_id":"DP03125r004","statement":[{"text":"As observed in the structures of CSK kinase (c-SRC-specific tyrosine kinase) bound to staurosporine (27) and the SRC family kinase HCK (human Cyclin-dependent kinase) bound to AMP-PNP (25), a part of the Aurora-2 activation loop (defined as residues 273–292) is disordered. Only residues 273–278 and 289–292 were clearly visible and have been included in the final model. Residue Thr-288, which is phosphorylated during activation of Aurora-2, belongs to part of the disordered region and was not visible in electron density maps","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-12T17:11:43.094Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":107,"end":127,"reference_id":"12237287","reference_source":"pmid","reference_html":"Crystal structure of aurora-2, an oncogenic serine/threonine kinase. <i> Cheetham GM, Knegtel RM, Coll JT, Renwick SB, Swenson L, Weber P, Lippke JA, Austen DA. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"1MUO"}],"region_id":"DP03125r005","statement":[{"text":"The disordered nature of residues 107–126 in the final crystal structure suggests that this spanning polypeptide linker is particularly long and flexible in Aurora-2","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":279,"end":290,"reference_id":"16337122","reference_source":"pmid","reference_html":"SAR and inhibitor complex structure determination of a novel class of potent and specific Aurora kinase inhibitors. <i> Heron NM, Anderson M, Blowers DP, Breed J, Eden JM, Green S, Hill GB, Johnson T, Jung FH, McMiken HH, Mortlock AA, Pannifer AD, Pauptit RA, Pink J, Roberts NJ, Rowsell S. </i> Bioorg Med Chem Lett, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2C6D"},{"db":"PDB","id":"2C6E"}],"region_id":"DP03125r006","statement":[{"text":"The activation loop, residues 279–290 containing the T287D mutation, is disordered in both structures suggesting mobility, as is the case in many other kinase structures. ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-12T17:09:53.659Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":6,"released":"2021_12","sequence":"MDRSKENCISGPVKATAPVGGPKRVLVTQQFPCQNPLPVNSGQAQRVLCPSNSSQRIPLQAQKLVSSHKPVQNQKQKQLQATSVPHPVSRPLNNTQKSKQPLPSAPENNPEEELASKQKNEESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWITANSSKPSNCQNKESASKQS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000016A02C","uniref100":"UniRef100_O14965","uniref90":"UniRef90_O14965","uniref50":"UniRef50_O14965","genes":[{"name":{"value":"AURKA","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11393","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11393"}}]},"synonyms":[{"value":"AIK"},{"value":"AIRK1"},{"value":"ARK1"},{"value":"AURA"},{"value":"AYK1"},{"value":"BTAK"},{"value":"IAK1"},{"value":"STK15","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15867347","url":"http://www.ncbi.nlm.nih.gov/pubmed/15867347","alternativeUrl":"https://europepmc.org/abstract/MED/15867347"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"16011022","url":"http://www.ncbi.nlm.nih.gov/pubmed/16011022","alternativeUrl":"https://europepmc.org/abstract/MED/16011022"}}]},{"value":"STK6"}]}],"alphafold_very_low_content":0.31265508684863524,"disorder_content":0.11910669975186104,"disprot_consensus":{"full":[{"start":107,"end":127,"type":"D"},{"start":273,"end":278,"type":"F"},{"start":279,"end":290,"type":"D"},{"start":291,"end":292,"type":"F"},{"start":389,"end":403,"type":"D"}],"Structural state":[{"start":107,"end":127,"type":"D"},{"start":279,"end":290,"type":"D"},{"start":389,"end":403,"type":"D"}],"Molecular function":[{"start":273,"end":292,"type":"F"}],"Disorder function":[{"start":107,"end":127,"type":"F"}]}},{"disprot_id":"DP03126","acc":"Q9WTL8","creator":"jssuarez","date":"2021-01-09T17:28:29.587Z","features":{"pfam":[{"id":"PF00010","name":"Helix-loop-helix DNA-binding domain","start":81,"end":133},{"id":"PF00989","name":"PAS fold","start":156,"end":259},{"id":"PF14598","name":"PAS domain","start":345,"end":447}],"gene3D":[]},"length":632,"name":"Aryl hydrocarbon receptor nuclear translocator-like protein 1","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":497,"end":632,"reference_id":"21521686","reference_source":"pmid","reference_html":"Quantitative analyses of cryptochrome-mBMAL1 interactions: mechanistic insights into the transcriptional regulation of the mammalian circadian clock. <i> Czarna A, Breitkreuz H, Mahrenholz CC, Arens J, Strauss HM, Wolf E. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03126r001","statement":[{"text":"The hydrodynamic (Stokes) radii determined by AUC analyses (Table 1) suggest that the mCRY and mBMAL1 proteins have somewhat elongated shapes and might be at least partially unstructured. ","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":497,"end":632,"reference_id":"21521686","reference_source":"pmid","reference_html":"Quantitative analyses of cryptochrome-mBMAL1 interactions: mechanistic insights into the transcriptional regulation of the mammalian circadian clock. <i> Czarna A, Breitkreuz H, Mahrenholz CC, Arens J, Strauss HM, Wolf E. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03126r002","statement":[{"text":"The spectra suggest, that the mBMAL1 and mCRY\nproteins are partially disordered (Table 2). ","type":"Supplementary material"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":584,"end":632,"reference_id":"21521686","reference_source":"pmid","reference_html":"Quantitative analyses of cryptochrome-mBMAL1 interactions: mechanistic insights into the transcriptional regulation of the mammalian circadian clock. <i> Czarna A, Breitkreuz H, Mahrenholz CC, Arens J, Strauss HM, Wolf E. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03126r003","statement":[{"text":"The spectra suggest, that the mBMAL1 and mCRY\nproteins are partially disordered (Table 2). ","type":"Supplementary material"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":584,"end":632,"reference_id":"21521686","reference_source":"pmid","reference_html":"Quantitative analyses of cryptochrome-mBMAL1 interactions: mechanistic insights into the transcriptional regulation of the mammalian circadian clock. <i> Czarna A, Breitkreuz H, Mahrenholz CC, Arens J, Strauss HM, Wolf E. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000269","ec_ontology":"ECO","ec_name":"experimental evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P97784","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9R194","partner_start":null,"partner_end":null}],"region_id":"DP03126r004","statement":[{"text":"The shorter mBMAL1-(577–625) fragment bound to both mCRYCCtail fragments with a roughly 10 μm affinity (Fig. 2A).","type":"Results"},{"text":"Region 577–625 discussed in the article corresponds to 584-632 in UniProt entry.","type":"Curator statement"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":497,"end":632,"reference_id":"21521686","reference_source":"pmid","reference_html":"Quantitative analyses of cryptochrome-mBMAL1 interactions: mechanistic insights into the transcriptional regulation of the mammalian circadian clock. <i> Czarna A, Breitkreuz H, Mahrenholz CC, Arens J, Strauss HM, Wolf E. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000269","ec_ontology":"ECO","ec_name":"experimental evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P97784","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9R194","partner_start":null,"partner_end":null}],"region_id":"DP03126r005","statement":[{"text":"In contrast, the longer mBMAL1-(490–625) fragment bound to mCRY1 with an ∼40 μm affinity and to mCRY2 with an ∼10 μm affinity (Fig. 2B).","type":"Results"},{"text":"Region 490–625 discussed in the article corresponds to 497-632 in UniProt entry.","type":"Curator statement"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":584,"end":632,"reference_id":"21521686","reference_source":"pmid","reference_html":"Quantitative analyses of cryptochrome-mBMAL1 interactions: mechanistic insights into the transcriptional regulation of the mammalian circadian clock. <i> Czarna A, Breitkreuz H, Mahrenholz CC, Arens J, Strauss HM, Wolf E. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"Q9R194","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P97784","partner_start":null,"partner_end":null}],"region_id":"DP03126r006","statement":[{"text":"In good agreement with the fluorescence polarization data, mCRY1 and mCRY2 bind to the mBMAL1-(577–625) fragment with a roughly 10 μm affinity (Fig. 3A and Table 3).","type":"Results"},{"text":"Region 577–625 discussed in the article corresponds to 584-632 in UniProt entry.","type":"Curator statement"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":497,"end":632,"reference_id":"21521686","reference_source":"pmid","reference_html":"Quantitative analyses of cryptochrome-mBMAL1 interactions: mechanistic insights into the transcriptional regulation of the mammalian circadian clock. <i> Czarna A, Breitkreuz H, Mahrenholz CC, Arens J, Strauss HM, Wolf E. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P97784","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9R194","partner_start":null,"partner_end":null}],"region_id":"DP03126r007","statement":[{"text":"Whereas mCRY2 shows a similar (∼10 μm) affinity to both mBMAL1 fragments, mCRY1 binds to the longer mBMAL1-(490–625) fragment with a roughly 20 μm affinity (Fig. 3B and Table 3).","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":584,"end":632,"reference_id":"21521686","reference_source":"pmid","reference_html":"Quantitative analyses of cryptochrome-mBMAL1 interactions: mechanistic insights into the transcriptional regulation of the mammalian circadian clock. <i> Czarna A, Breitkreuz H, Mahrenholz CC, Arens J, Strauss HM, Wolf E. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03126r008","statement":[{"text":"The hydrodynamic (Stokes) radii determined by AUC analyses (Table 1) suggest that the mCRY and mBMAL1 proteins have somewhat elongated shapes and might be at least partially unstructured.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":8,"released":"2021_12","sequence":"MADQRMDISSTISDFMSPGPTDLLSGSLGTSGVDCNRKRKGSATDYQLDDFAFEESMDTDKDDPHGRLEYAEHQGRIKNAREAHSQIEKRRRDKMNSFIDELASLVPTCNAMSRKLDKLTVLRMAVQHMKTLRGATNPYTEANYKPTFLSDDELKHLILRAADGFLFVVGCDRGKILFVSESVFKILNYSQNDLIGQSLFDYLHPKDIAKVKEQLSSSDTAPRERLIDAKTGLPVKTDITPGPSRLCSGARRSFFCRMKCNRPSVKVEDKDFASTCSKKKDRKSFCTIHSTGYLKSWPPTKMGLDEDNEPDNEGCNLSCLVAIGRLHSHMVPQPANGEIRVKSMEYVSRHAIDGKFVFVDQRATAILAYLPQELLGTSCYEYFHQDDIGHLAECHRQVLQTREKITTNCYKFKIKDGSFITLRSRWFSFMNPWTKEVEYIVSTNTVVLANVLEGGDPTFPQLTAPPHSMDSMLPSGEGGPKRTHPTVPGIPGGTRAGAGKIGRMIAEEIMEIHRIRGSSPSSCGSSPLNITSTPPPDASSPGGKKILNGGTPDIPSTGLLPGQAQETPGYPYSDSSSILGENPHIGIDMIDNDQGSSSPSNDEAAMAVIMSLLEADAGLGGPVDFSDLPWPL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"dataset":[],"UniParc":"UPI0000028BE1","uniref100":"UniRef100_Q9WTL8","uniref90":"UniRef90_Q9WTL8","uniref50":"UniRef50_Q9WTL8","genes":[{"name":{"value":"Arntl"},"synonyms":[{"value":"Bmal1"}]}],"alphafold_very_low_content":0.41139240506329117,"disorder_content":0.21518987341772153,"disprot_consensus":{"full":[{"start":497,"end":632,"type":"D"}],"Structural state":[{"start":497,"end":632,"type":"D"}],"Molecular function":[{"start":497,"end":632,"type":"F"}]}},{"disprot_id":"DP03127","acc":"Q9R194","creator":"jssuarez","date":"2021-01-09T17:50:51.665Z","features":{"pfam":[{"id":"PF00875","name":"DNA photolyase","start":23,"end":175},{"id":"PF03441","name":"FAD binding domain of DNA photolyase","start":306,"end":504}],"gene3D":[]},"length":592,"name":"Cryptochrome-2","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":489,"end":592,"reference_id":"21521686","reference_source":"pmid","reference_html":"Quantitative analyses of cryptochrome-mBMAL1 interactions: mechanistic insights into the transcriptional regulation of the mammalian circadian clock. <i> Czarna A, Breitkreuz H, Mahrenholz CC, Arens J, Strauss HM, Wolf E. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006200","ec_ontology":"ECO","ec_name":"circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03127r001","statement":[{"text":"The spectra suggest, that the mBMAL1 and mCRY\nproteins are partially disordered (Table 2). ","type":"Supplementary material"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":489,"end":592,"reference_id":"21521686","reference_source":"pmid","reference_html":"Quantitative analyses of cryptochrome-mBMAL1 interactions: mechanistic insights into the transcriptional regulation of the mammalian circadian clock. <i> Czarna A, Breitkreuz H, Mahrenholz CC, Arens J, Strauss HM, Wolf E. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03127r002","statement":[{"text":"he hydrodynamic (Stokes) radii determined by AUC analyses (Table 1) suggest that the mCRY and mBMAL1 proteins have somewhat elongated shapes and might be at least partially unstructured.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":489,"end":592,"reference_id":"21521686","reference_source":"pmid","reference_html":"Quantitative analyses of cryptochrome-mBMAL1 interactions: mechanistic insights into the transcriptional regulation of the mammalian circadian clock. <i> Czarna A, Breitkreuz H, Mahrenholz CC, Arens J, Strauss HM, Wolf E. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000269","ec_ontology":"ECO","ec_name":"experimental evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"Q9WTL8","partner_start":null,"partner_end":null}],"region_id":"DP03127r003","statement":[{"text":"In contrast, the longer mBMAL1-(490–625) fragment bound to mCRY1 with an ∼40 μm affinity and to mCRY2 with an ∼10 μm affinity (Fig. 2B). ","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":489,"end":592,"reference_id":"21521686","reference_source":"pmid","reference_html":"Quantitative analyses of cryptochrome-mBMAL1 interactions: mechanistic insights into the transcriptional regulation of the mammalian circadian clock. <i> Czarna A, Breitkreuz H, Mahrenholz CC, Arens J, Strauss HM, Wolf E. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"Q9WTL8","partner_start":null,"partner_end":null}],"region_id":"DP03127r004","statement":[{"text":"In good agreement with the fluorescence polarization data, mCRY1 and mCRY2 bind to the mBMAL1-(577–625) fragment with a roughly 10 μm affinity (Fig. 3A and Table 3). Whereas mCRY2 shows a similar (∼10 μm) affinity to both mBMAL1 fragments, mCRY1 binds to the longer mBMAL1-(490–625) fragment with a roughly 20 μm affinity (Fig. 3B and Table 3). ","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":4,"released":"2021_12","sequence":"MAAAAVVAATVPAQSMGADGASSVHWFRKGLRLHDNPALLAAVRGARCVRCVYILDPWFAASSSVGINRWRFLLQSLEDLDTSLRKLNSRLFVVRGQPADVFPRLFKEWGVTRLTFEYDSEPFGKERDAAIMKMAKEAGVEVVTENSHTLYDLDRIIELNGQKPPLTYKRFQALISRMELPKKPAVAVSSQQMESCRAEIQENHDDTYGVPSLEELGFPTEGLGPAVWQGGETEALARLDKHLERKAWVANYERPRMNANSLLASPTGLSPYLRFGCLSCRLFYYRLWDLYKKVKRNSTPPLSLFGQLLWREFFYTAATNNPRFDRMEGNPICIQIPWDRNPEALAKWAEGKTGFPWIDAIMTQLRQEGWIHHLARHAVACFLTRGDLWVSWESGVRVFDELLLDADFSVNAGSWMWLSCSAFFQQFFHCYCPVGFGRRTDPSGDYIRRYLPKLKGFPSRYIYEPWNAPESVQKAAKCIIGVDYPRPIVNHAETSRLNIERMKQIYQQLSRYRGLCLLASVPSCVEDLSHPVAEPGSSQAGSISNTGPRALSSGPASPKRKLEAAEEPPGEELTKRARVTEMPTQEPASKDS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"dataset":[],"UniParc":"UPI00000293C8","uniref100":"UniRef100_Q9R194","uniref90":"UniRef90_Q9R194","uniref50":"UniRef50_Q9R194","genes":[{"name":{"value":"Cry2"},"synonyms":[{"value":"Kiaa0658"}]}],"alphafold_very_low_content":0.16385135135135134,"disorder_content":0.17567567567567569,"disprot_consensus":{"full":[{"start":489,"end":592,"type":"D"}],"Structural state":[{"start":489,"end":592,"type":"D"}],"Molecular function":[{"start":489,"end":592,"type":"F"}]}},{"disprot_id":"DP03129","acc":"O08679","creator":"mlambrughi","date":"2021-01-10T21:32:54.166Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":53,"end":304},{"id":"PF00627","name":"UBA/TS-N domain","start":325,"end":360},{"id":"PF02149","name":"Kinase associated domain 1","start":679,"end":722}],"gene3D":[]},"length":722,"name":"Serine/threonine-protein kinase MARK2","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions":[{"start":38,"end":48,"reference_id":"16472737","reference_source":"pmid","reference_html":"Structure of the catalytic and ubiquitin-associated domains of the protein kinase MARK/Par-1. <i> Panneerselvam S, Marx A, Mandelkow EM, Mandelkow E. </i> Structure, 2006","date":"2024-02-20T16:27:30.197Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":3,"cross_refs":[{"db":"PDB","id":"1ZMU"}],"region_id":"DP03129r001","statement":[{"text":"The 11 initial residues (G38–P48) are invisible due to disorder.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":193,"end":210,"reference_id":"16472737","reference_source":"pmid","reference_html":"Structure of the catalytic and ubiquitin-associated domains of the protein kinase MARK/Par-1. <i> Panneerselvam S, Marx A, Mandelkow EM, Mandelkow E. </i> Structure, 2006","date":"2024-02-20T16:27:38.714Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":3,"cross_refs":[{"db":"PDB","id":"1ZMU"}],"region_id":"DP03129r002","statement":[{"text":"Whereas most of the activation loop is disordered in the wild-type and K82R structures (D193–C210), the T208A/S212A mutant reveals five more residues at the end of the activation loop (L206–C210).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":4,"released":"2021_12","sequence":"MSSARTPLPTLNERDTEQPTLGHLDSKPSSKSNMLRGRNSATSADEQPHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWMNVGHEDDELKPYVEPLPDYKDPRRTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGYKSSELEGDTITLKPRPSADLTNSSAPSPSHKVQRSVSANPKQRRSSDQAVPAIPTSNSYSKKTQSNNAENKRPEEETGRKASSTAKVPASPLPGLDRKKTTPTPSTNSVLSTSTNRSRNSPLLDRASLGQASIQNGKDSTAPQRVPVASPSAHNISSSSGAPDRTNFPRGVSSRSTFHAGQLRQVRDQQNLPFGVTPASPSGHSQGRRGASGSIFSKFTSKFVRRNLNEPESKDRVETLRPHVVGGGGTDKEKEEFREAKPRSLRFTWSMKTTSSMEPNEMMREIRKVLDANSCQSELHERYMLLCVHGTPGHENFVQWEMEVCKLPRLSLNGVRFKRISGTSMAFKNIASKIANELKL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"dataset":[],"UniParc":"UPI00000E62CD","uniref100":"UniRef100_O08679","uniref90":"UniRef90_O08679","uniref50":"UniRef50_O08679","genes":[{"name":{"value":"Mark2","evidences":[{"code":"ECO:0000312","source":{"name":"RGD","id":"708483","url":"https://rgd.mcw.edu/tools/genes/genes_view.cgi?id=708483"}}]}}],"alphafold_very_low_content":0.40443213296398894,"disorder_content":0.04016620498614958,"disprot_consensus":{"full":[{"start":38,"end":48,"type":"D"},{"start":193,"end":210,"type":"D"}],"Structural state":[{"start":38,"end":48,"type":"D"},{"start":193,"end":210,"type":"D"}]}},{"disprot_id":"DP03130","acc":"Q7KZI7","creator":"mlambrughi","date":"2021-01-11T00:53:29.925Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":53,"end":304},{"id":"PF00627","name":"UBA/TS-N domain","start":325,"end":360},{"id":"PF02149","name":"Kinase associated domain 1","start":746,"end":788}],"gene3D":[]},"length":788,"name":"Serine/threonine-protein kinase MARK2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":197,"end":209,"reference_id":"27491711","reference_source":"pmid","reference_html":"Optimization of microtubule affinity regulating kinase (MARK) inhibitors with improved physical properties. <i> Sloman DL, Noucti N, Altman MD, Chen D, Mislak AC, Szewczak A, Hayashi M, Warren L, Dellovade T, Wu Z, Marcus J, Walker D, Su HP, Edavettal SC, Munshi S, Hutton M, Nuthall H, Stanton MG. </i> Bioorg Med Chem Lett, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"mlambrughi","curator_name":"Matteo Lambrughi","curator_orcid":"0000-0002-0894-8627","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5EAK"}],"region_id":"DP03130r001","statement":[{"text":"The overall protein structure is very similar to what has been previously reported (S. Panneerselvam, A. Marx, E.M. Mandelkow, E. Mandelkow\nStructure, 14 (2006), p. 173)","type":"Results"},{"text":"The crystallographic structure of the catalytic domain of human MARK2 is very similar to the crystallographic structure of the catalytic domain of rat MARK2 and they both present a disordered activation loop in the inactive state","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T08:59:18.170Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":196,"end":211,"reference_id":"27816515","reference_source":"pmid","reference_html":"Structure guided design of a series of selective pyrrolopyrimidinone MARK inhibitors. <i> Katz JD, Haidle A, Childers KK, Zabierek AA, Jewell JP, Hou Y, Altman MD, Szewczak A, Chen D, Harsch A, Hayashi M, Warren L, Hutton M, Nuthall H, Su HP, Munshi S, Stanton MG, Davies IW, Munoz B, Northrup A. </i> Bioorg Med Chem Lett, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"mlambrughi","curator_name":"Matteo Lambrughi","curator_orcid":"0000-0002-0894-8627","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5KZ8"},{"db":"PDB","id":"5KZ7"}],"region_id":"DP03130r002","statement":[{"text":"The crystallographic structure of the catalytic domain of human MARK2 is very similar to the crystallographic structure of the catalytic domain of rat MARK2 and they both present a disordered activation loop in their inactive state","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T08:59:17.162Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":196,"end":211,"reference_id":"19966800","reference_source":"pmid","reference_html":"Helicobacter pylori CagA inhibits PAR1-MARK family kinases by mimicking host substrates. <i> Nesić D, Miller MC, Quinkert ZT, Stein M, Chait BT, Stebbins CE. </i> Nat Struct Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"mlambrughi","curator_name":"Matteo Lambrughi","curator_orcid":"0000-0002-0894-8627","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3IEC"}],"region_id":"DP03130r003","statement":[{"text":"The second major difference is in the activation loop of the kinase, which adopts an ordered and activated structure in the presence of CagA","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T08:59:19.425Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":206,"end":210,"reference_id":"14976552","reference_source":"pmid","reference_html":"LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1. <i> Lizcano JM, Göransson O, Toth R, Deak M, Morrice NA, Boudeau J, Hawley SA, Udd L, Mäkelä TP, Hardie DG, Alessi DR. </i> EMBO J, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"mlambrughi","curator_name":"Matteo Lambrughi","curator_orcid":"0000-0002-0894-8627","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03130r004","statement":[{"text":"The LKB1 complex phosphorylates AMPK-related kinases at the activation loop","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T08:59:20.244Z"},"ec_go":"IEP","disprot_namespace":"Disorder function"}],"regions_counter":4,"released":"2021_12","sequence":"MSSARTPLPTLNERDTEQPTLGHLDSKPSSKSNMIRGRNSATSADEQPHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWMNVGHEDDELKPYVEPLPDYKDPRRTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGYKSSELEGDTITLKPRPSADLTNSSAPSPSHKVQRSVSANPKQRRFSDQAAGPAIPTSNSYSKKTQSNNAENKRPEEDRESGRKASSTAKVPASPLPGLERKKTTPTPSTNSVLSTSTNRSRNSPLLERASLGQASIQNGKDSLTMPGSRASTASASAAVSAARPRQHQKSMSASVHPNKASGLPPTESNCEVPRPSTAPQRVPVASPSAHNISSSGGAPDRTNFPRGVSSRSTFHAGQLRQVRDQQNLPYGVTPASPSGHSQGRRGASGSIFSKFTSKFVRRNLSFRFARRNLNEPESKDRVETLRPHVVGSGGNDKEKEEFREAKPRSLRFTWSMKTTSSMEPNEMMREIRKVLDANSCQSELHEKYMLLCMHGTPGHEDFVQWEMEVCKLPRLSLNGVRFKRISGTSMAFKNIASKIANELKL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"UniParc":"UPI00004F6F00","uniref100":"UniRef100_Q7KZI7","uniref90":"UniRef90_Q7KZI7","uniref50":"UniRef50_Q7KZI7","genes":[{"name":{"value":"MARK2","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAH08771.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAH08771.2"}}]},"synonyms":[{"value":"EMK1"}]}],"alphafold_very_low_content":0.4530456852791878,"disorder_content":0.02030456852791878,"disprot_consensus":{"full":[{"start":196,"end":211,"type":"T"}],"Structural state":[{"start":196,"end":211,"type":"D"}],"Structural transition":[{"start":196,"end":211,"type":"T"}],"Disorder function":[{"start":206,"end":210,"type":"F"}]}},{"disprot_id":"DP03131","acc":"Q96AE4","creator":"mlambrughi","date":"2021-01-11T01:51:19.884Z","features":{"pfam":[{"id":"PF00013","name":"KH domain","start":102,"end":165},{"id":"PF00013","name":"KH domain","start":188,"end":253},{"id":"PF00013","name":"KH domain","start":280,"end":340},{"id":"PF00013","name":"KH domain","start":380,"end":445},{"id":"PF09005","name":"Far upstream element-binding protein, C-terminal","start":576,"end":595},{"id":"PF09005","name":"Far upstream element-binding protein, C-terminal","start":604,"end":622}],"gene3D":[]},"length":644,"name":"Far upstream element-binding protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":347,"end":377,"reference_id":"11875576","reference_source":"pmid","reference_html":"Structure and dynamics of KH domains from FBP bound to single-stranded DNA. <i> Braddock DT, Louis JM, Baber JL, Levens D, Clore GM. </i> Nature, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"mlambrughi","curator_name":"Matteo Lambrughi","curator_orcid":"0000-0002-0894-8627","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":2,"cross_refs":[{"db":"PDB","id":"1J4W"}],"region_id":"DP03131r001","statement":[{"text":"The 30-residue protein linker between the KH3 and KH4 domains is highly disordered (Fig. 3a), such that in free FBP3/4 the two domains reorient essentially independently of each other (unpublished data), as in the case of other modular proteins connected by long linkers","type":"Results"},{"text":"In the paper the authors included residues 278–447 of human FBP and renumbered them as 5–174","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":347,"end":377,"reference_id":"11875576","reference_source":"pmid","reference_html":"Structure and dynamics of KH domains from FBP bound to single-stranded DNA. <i> Braddock DT, Louis JM, Baber JL, Levens D, Clore GM. </i> Nature, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"mlambrughi","curator_name":"Matteo Lambrughi","curator_orcid":"0000-0002-0894-8627","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":3,"cross_refs":[{"db":"PDB","id":"1J4W"}],"region_id":"DP03131r002","statement":[{"text":"Interdomain motion observed in the FBP3/4–M29 ssDNA complex in which the linkers, both protein and ssDNA, possess intrinsic flexibility, is likely to be an essential component of FBP function. This property can readily accommodate changes in the direction of the DNA.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":2,"released":"2022_06","sequence":"MADYSTVPPPSSGSAGGGGGGGGGGGVNDAFKDALQRARQIAAKIGGDAGTSLNSNDYGYGGQKRPLEDGDQPDAKKVAPQNDSFGTQLPPMHQQQSRSVMTEEYKVPDGMVGFIIGRGGEQISRIQQESGCKIQIAPDSGGLPERSCMLTGTPESVQSAKRLLDQIVEKGRPAPGFHHGDGPGNAVQEIMIPASKAGLVIGKGGETIKQLQERAGVKMVMIQDGPQNTGADKPLRITGDPYKVQQAKEMVLELIRDQGGFREVRNEYGSRIGGNEGIDVPIPRFAVGIVIGRNGEMIKKIQNDAGVRIQFKPDDGTTPERIAQITGPPDRCQHAAEIITDLLRSVQAGNPGGPGPGGRGRGRGQGNWNMGPPGGLQEFNFIVPTGKTGLIIGKGGETIKSISQQSGARIELQRNPPPNADPNMKLFTIRGTPQQIDYARQLIEEKIGGPVNPLGPPVPHGPHGVPGPHGPPGPPGPGTPMGPYNPAPYNPGPPGPAPHGPPAPYAPQGWGNAYPHWQQQAPPDPAKAGTDPNSAAWAAYYAHYYQQQAQPPPAAPAGAPTTTQTNGQGDQQNPAPAGQVDYTKAWEEYYKKMGQAVPAPTGAPPGGQPDYSAAWAEYYRQQAAYYAQTSPQGMPQHPPAPQGQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins"],"UniParc":"UPI00000715F3","uniref100":"UniRef100_Q96AE4","uniref90":"UniRef90_Q96AE4","uniref50":"UniRef50_Q96AE4","genes":[{"name":{"value":"FUBP1"}}],"alphafold_very_low_content":0.39906832298136646,"disorder_content":0.04813664596273292,"disprot_consensus":{"full":[{"start":347,"end":377,"type":"D"}],"Structural state":[{"start":347,"end":377,"type":"D"}],"Disorder function":[{"start":347,"end":377,"type":"F"}]}},{"disprot_id":"DP03134","acc":"Q9NPF0","creator":"zskalman","date":"2021-01-11T09:18:44.486Z","features":{"pfam":[{"id":"PF00057","name":"Low-density lipoprotein receptor domain class A","start":53,"end":89},{"id":"PF00057","name":"Low-density lipoprotein receptor domain class A","start":131,"end":167}],"gene3D":[]},"length":282,"name":"CD320 antigen","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":90,"end":128,"reference_id":"27411955","reference_source":"pmid","reference_html":"Structural basis of transcobalamin recognition by human CD320 receptor. <i> Alam A, Woo JS, Schmitz J, Prinz B, Root K, Chen F, Bloch JS, Zenobi R, Locher KP. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4ZRP"}],"region_id":"DP03134r001","statement":[{"text":"Whereas clear electron density was observed for LDLR-A1 residues 53–89 and LDLR-A2 residues 129-171, no density was observed for the EGF-like domain (residues 90–128).","type":"Introduction"},{"text":"The EGF-like domain of CD320 is not visible in our electron density maps despite chemically being present, suggesting positional disorder in the crystal. ","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":86,"end":128,"reference_id":"27411955","reference_source":"pmid","reference_html":"Structural basis of transcobalamin recognition by human CD320 receptor. <i> Alam A, Woo JS, Schmitz J, Prinz B, Root K, Chen F, Bloch JS, Zenobi R, Locher KP. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4ZRQ"}],"region_id":"DP03134r002","statement":[{"text":"From the statement „Moreover, electron density for the Ca2+ binding residue Glu86 as well as Glu87 and disulfide forming Cys88 (equivalent to Cys89 in wild type) was missing\". Besides this small region, the electron density map is missing also for the 90-128 region (as it was observed in the wild type as well (PDB: 4ZRP)).","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MSGGWMAQVGAWRTGALGLALLLLLGLGLGLEAAASPLSTPTSAQAAGPSSGSCPPTKFQCRTSGLCVPLTWRCDRDLDCSDGSDEEECRIEPCTQKGQCPPPPGLPCPCTGVSDCSGGTDKKLRNCSRLACLAGELRCTLSDDCIPLTWRCDGHPDCPDSSDELGCGTNEILPEGDATTMGPPVTLESVTSLRNATTMGPPVTLESVPSVGNATSSSAGDQSGSPTAYGVIAAAAVLSASLVTATLLLLSWLRAQERLRPLGLLVAMKESLLLSEQKTSLP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI0000037B71","uniref100":"UniRef100_Q9NPF0","uniref90":"UniRef90_Q9NPF0","uniref50":"UniRef50_Q9NPF0","genes":[{"name":{"value":"CD320"},"synonyms":[{"value":"8D6A"}],"orfNames":[{"value":"UNQ198/PRO224"}]}],"alphafold_very_low_content":0.3900709219858156,"disorder_content":0.1524822695035461,"disprot_consensus":{"full":[{"start":86,"end":128,"type":"D"}],"Structural state":[{"start":86,"end":128,"type":"D"}]}},{"disprot_id":"DP03135","acc":"P35680","creator":"zskalman","date":"2021-01-11T09:30:45.944Z","features":{"pfam":[{"id":"PF04812","name":"Hepatocyte nuclear factor 1 (HNF-1), beta isoform C terminus","start":314,"end":550},{"id":"PF04814","name":"Hepatocyte nuclear factor 1 (HNF-1), N terminus","start":8,"end":174}],"gene3D":[]},"length":557,"name":"Hepatocyte nuclear factor 1-beta","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":188,"end":230,"reference_id":"17924661","reference_source":"pmid","reference_html":"Structural basis of disease-causing mutations in hepatocyte nuclear factor 1beta. <i> Lu P, Rha GB, Chi YI. </i> Biochemistry, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2H8R"}],"region_id":"DP03135r001","statement":[{"text":"The linker between the POUS and POUH domains (amino acids 186−229) of HNF1β contains the nuclear localization signal (NLS; 229KKMRRNRFK237) and is even longer than that of HNF1α (by 26 residues) (Figure 1). The majority of the linker is disordered, as also seen in the HNF1α structure.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MVSKLTSLQQELLSALLSSGVTKEVLVQALEELLPSPNFGVKLETLPLSPGSGAEPDTKPVFHTLTNGHAKGRLSGDEGSEDGDDYDTPPILKELQALNTEEAAEQRAEVDRMLSEDPWRAAKMIKGYMQQHNIPQREVVDVTGLNQSHLSQHLNKGTPMKTQKRAALYTWYVRKQREILRQFNQTVQSSGNMTDKSSQDQLLFLFPEFSQQSHGPGQSDDACSEPTNKKMRRNRFKWGPASQQILYQAYDRQKNPSKEEREALVEECNRAECLQRGVSPSKAHGLGSNLVTEVRVYNWFANRRKEEAFRQKLAMDAYSSNQTHSLNPLLSHGSPHHQPSSSPPNKLSGVRYSQQGNNEITSSSTISHHGNSAMVTSQSVLQQVSPASLDPGHNLLSPDGKMISVSGGGLPPVSTLTNIHSLSHHNPQQSQNLIMTPLSGVMAIAQSLNTSQAQSVPVINSVAGSLAALQPVQFSQQLHSPHQQPLMQQSPGSHMAQQPFMAAVTQLQNSHMYAHKQEPPQYSHTSRFPSAMVVTDTSSISTLTNMSSSKQCPLQAW","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000012CA96","uniref100":"UniRef100_P35680","uniref90":"UniRef90_P35680","uniref50":"UniRef50_P35680","genes":[{"name":{"value":"HNF1B"},"synonyms":[{"value":"TCF2"}]}],"alphafold_very_low_content":0.5709156193895871,"disorder_content":0.07719928186714542,"disprot_consensus":{"full":[{"start":188,"end":230,"type":"D"}],"Structural state":[{"start":188,"end":230,"type":"D"}]}},{"disprot_id":"DP03136","acc":"F4IED2","creator":"eficho","date":"2021-01-11T11:51:44.747Z","features":{"pfam":[{"id":"PF02365","name":"No apical meristem (NAM) protein","start":12,"end":135}],"gene3D":[]},"length":528,"name":"NAC domain-containing protein 13","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":254,"end":274,"reference_id":"27881680","reference_source":"pmid","reference_html":"Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1. <i> O'Shea C, Staby L, Bendsen SK, Tidemand FG, Redsted A, Willemoës M, Kragelund BB, Skriver K. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03136r001","statement":[{"text":"Experimental analysis for secondary structure content by far-UV CD indicated low α-helical contents of 12, 18, 10, and 13% in the ANAC013(254–274), DREB2A(255–272), COL10(175–208), and bZIP23(15–36) peptides, respectively (Fig. 5, B–E).","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-13T15:57:07.651Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":254,"end":274,"reference_id":"27881680","reference_source":"pmid","reference_html":"Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1. <i> O'Shea C, Staby L, Bendsen SK, Tidemand FG, Redsted A, Willemoës M, Kragelund BB, Skriver K. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03136r002","statement":[{"text":"For ANAC013(254–274) in complex with RCD1-RST, the wavelength of the absolute minimum changed slightly compared with the theoretical spectra, and the α-helical content of 32% in the complex was minimally higher than in the theoretical complex (29%) (Fig. 6C).","type":"Results"},{"text":"Together, the results suggested that complex formation involving ANAC046(319–338) and ANAC013(254–274) resulted in structure induction, although to a lower degree than that of the DREB2A(255–272)·RCD1-RST(499–572) complex.","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-13T15:57:28.138Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":254,"end":274,"reference_id":"27881680","reference_source":"pmid","reference_html":"Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1. <i> O'Shea C, Staby L, Bendsen SK, Tidemand FG, Redsted A, Willemoës M, Kragelund BB, Skriver K. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03136r003","statement":[{"text":"Similar to DREB2A(255–272), free ANAC013(254–274) and ANAC046(319–338) had poorly dispersed HSQC spectra (Fig. 7, B and C, black spectra), and ΔδCα values close to zero (Fig. 7, E and F, top figures) again confirming a lack of preformed structure. ","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-13T15:57:22.601Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":254,"end":274,"reference_id":"27881680","reference_source":"pmid","reference_html":"Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1. <i> O'Shea C, Staby L, Bendsen SK, Tidemand FG, Redsted A, Willemoës M, Kragelund BB, Skriver K. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"interaction_partner":[{"db":"UniProt","id":"Q8RY59","partner_start":null,"partner_end":null}],"region_id":"DP03136r004","statement":[{"text":"Comparison of the HSQC spectra of free and bound ANAC013(254–274) and ANAC046(319–338) confirmed their interaction with RCD1-RST(499–572) (Fig. 7, B and C), but in contrast to those of DREB2A(255–272), the dispersion in the proton dimension appeared immediately unaffected.","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-13T15:57:29.632Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":254,"end":274,"reference_id":"27881680","reference_source":"pmid","reference_html":"Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1. <i> O'Shea C, Staby L, Bendsen SK, Tidemand FG, Redsted A, Willemoës M, Kragelund BB, Skriver K. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"interaction_partner":[{"db":"UniProt","id":"Q8RY59","partner_start":null,"partner_end":null}],"region_id":"DP03136r005","statement":[{"text":"For ANAC013(254–274) in complex with RCD1-RST, the wavelength of the absolute minimum changed slightly compared with the theoretical spectra, and the α-helical content of 32% in the complex was minimally higher than in the theoretical complex (29%) (Fig. 6C).","type":"Results"},{"text":"Together, the results suggested that complex formation involving ANAC046(319–338) and ANAC013(254–274) resulted in structure induction, although to a lower degree than that of the DREB2A(255–272)·RCD1-RST(499–572) complex.","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-13T15:57:39.301Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":254,"end":274,"reference_id":"27881680","reference_source":"pmid","reference_html":"Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1. <i> O'Shea C, Staby L, Bendsen SK, Tidemand FG, Redsted A, Willemoës M, Kragelund BB, Skriver K. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"interaction_partner":[{"db":"UniProt","id":"Q8RY59","partner_start":null,"partner_end":null}],"region_id":"DP03136r006","statement":[{"text":"The affinity increased further by additional truncation resulting in a Kd of 32 nm for ANAC013(254–299), and removal of most of the negatively charged fragment (Fig. 1) to generate ANAC013(254–274) resulted in a further decrease of Kd to 9.0 nm (Fig. 2A). This is a relatively low Kd value for an interaction involving a putative SLiM and a globular domain (10), and the results indicate that the ANAC013 context of the SLiM has negative allosteric effects on binding.","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-13T15:57:41.454Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":161,"end":498,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2022-11-09T18:44:49.915Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03136r007","statement":[{"text":"Although the relative migration pattern of the recombinant proteins by SDS/PAGE was in accordance with their relative molecular mass values [NAP (162–268): 15.0 kDa; ANAC019 (163–317): 17.2 kDa; ANAC046 (172–338): 18.2 kDa; histidine–NTL8 (156–335): 20.3 kDa; histidine–SOG (210–449): 29.0 kDa; ANAC013 (161–498): 37.5 kDa], they displayed slow migration during SDS/PAGE compared with standard globular proteins, which is in accordance with their ID nature and previous analysis of two NAC TRDs [39].","type":"Results"}]},{"start":161,"end":498,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2022-11-09T18:47:23.720Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03136r008","statement":[{"text":"The hydrodynamic radii (Stokes radii) of ANAC046 (172–338), NAP (162–268) and ANAC019 (163–317) corresponded to pre-molten globule states, whereas ANAC013 (161–498) had a more compact structure consistent with its disorder profile (Figures 1d and 3).","type":"Results"}]},{"start":161,"end":498,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2022-11-09T18:50:05.315Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03136r009","statement":[{"text":"Although the spectra of the six recombinant proteins showed different characteristics, they all had a minimum around 200 nm and only slightly negative ellipticities at 222 nm (Figure 4a). Both the [θ]222 and [θ]200 values suggested that histidine–NTL8 (156–335), ANAC013 (161–498), NAP (162–268) and ANAC019 (163–317) are similar, populating pre-molten globule like ensembles, whereas the values for histidine–SOG1 (210–449) and ANAC046 (172–338) suggest more random coil-like ensembles.","type":"Results"}]},{"start":205,"end":299,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2024-02-22T16:48:22.194Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140537","term_name":"transcription regulator activator activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006295","ec_ontology":"ECO","ec_name":"beta galactosidase functional complementation evidence used in manual assertion","unpublished":true,"released":"2024_06","version":1,"ec_go":"IPI","region_id":"DP03136r010","statement":[{"text":"Both full-length ANAC013, DBD–ANAC013(1–498) and the TRD, DBD–ANAC013 (161–498), both lacking the transmembrane region, activated transcription in yeast. ","type":"Results"},{"text":"Stepwise C-terminal truncation of both constructs revealed that removal of the region between residue 205 and 299, containing several MoRFs and α-helices (Figure 1d), abolished the ability to activate transcription (Figure 7b).","type":"Results"}],"term_comment":"Usage guidance: transcription regulator activators bind to a transcription regulator to allow it to reach the chromatin or to contact other transcriptional regulators. This activity does not occur at the promoter. For activities that do occur at the promoter, consider GO:0001216 ; DNA-binding transcription activator activity or GO:0003713; transcription coactivator activity; those activities respectively bind DNA themselves or positively regulate a transcription regulator when it is located at the chromatin.","term_def":"\"A molecular function regulator that increases the activity of a transcription regulator via direct binding and/or post-translational modification.\" [PMID:9597751]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0693","term_name":"Gal4 DNA-binding domain tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}]},{"start":205,"end":299,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2024-02-22T17:04:50.303Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005805","ec_ontology":"ECO","ec_name":"yeast 2-hybrid evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0693","term_name":"Gal4 DNA-binding domain tag","term_namespace":"Tag","start":null,"end":null,"position":null,"statements":[{"type":"Figure","text":"Fusions of GAL4 DBD and the RST domain of RCD1 (residues 498–573; DBD–RST) and of GAL4 AD and the NAP fragment shown were expressed in yeast and screened for interactions \n through the ability to activate the reporter genes HIS3 and ADE2."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q8RY59","operator":null,"partner_start":498,"partner_end":573}],"region_id":"DP03136r011","statement":[{"text":"As expected, the RST domain of RCD1 interacted with both full-length ANAC013 and ANAC046 and their TRDs (Figures 7b and 7c), whereas no interaction was detected with NAP (Figure 7a) [27].","type":"Results"},{"text":"C-terminal truncations were also analysed for their ability to interact with DBD–RCD1 (498-573). This suggested that residues 205–299 of ANAC013 and that the very C-terminal MoRF region of ANAC046 were responsible for the interactions (Figures 7b–7c).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":161,"end":498,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2024-02-22T17:11:16.300Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q8RY59","operator":null,"partner_start":487,"partner_end":589}],"region_id":"DP03136r012","statement":[{"text":"Likewise, the CD spectrum of interacting ANAC013 (161–498) and histidine–RCD1–RST (487–589) showed a shift of the minimum around 200 nm towards a lower wavelength and also a decrease in the negativity at 222 nm compared with the theoretical complex suggestive of induced unfolding (Figure 4c).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":161,"end":498,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2024-02-22T17:19:03.172Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q8RY59","operator":null,"partner_start":499,"partner_end":572}],"region_id":"DP03136r013","statement":[{"text":"The change in entropy for binding of ANAC013 (161–498) to RCD1–RST (499–572) is relatively small and negative, indicating that binding is enthalpically driven.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":184,"end":274,"reference_id":"39933695","reference_source":"pmid","reference_html":"Allovalent scavenging of activation domains in the transcription factor ANAC013 gears transcriptional regulation. <i> Delaforge E, Due AD, Theisen FF, Morffy N, O'Shea C, Blackledge M, Strader LC, Skriver K, Kragelund BB. </i> Nucleic Acids Res, 2025","date":"2025-04-22T11:20:58.871Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7.4,"statements":[{"type":"Methods","text":"All samples for NMR contained 20 mM sodium phosphate (pH 7.4), 150 mM NaCl, 2 mM DTT, 10% (v/v) D2O, and 2 mM DSS."}]}],"region_id":"DP03136r014","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":20,"db":"ChEBI","id":"37586","statements":[{"type":"Results","text":"All samples for NMR contained 20 mM sodium phosphate (pH 7.4), 150 mM NaCl, 2 mM DTT, 10% (v/v) D2O, and 2 mM DSS."}],"entry_name":"sodium phosphate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":150,"db":"ChEBI","id":"26710","statements":[{"type":"Methods","text":"All samples for NMR contained 20 mM sodium phosphate (pH 7.4), 150 mM NaCl, 2 mM DTT, 10% (v/v) D2O, and 2 mM DSS."}],"entry_name":"sodium chloride"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":2,"db":"ChEBI","id":"16130","statements":[{"type":"Methods","text":"All samples for NMR contained 20 mM sodium phosphate (pH 7.4), 150 mM NaCl, 2 mM DTT, 10% (v/v) D2O, and 2 mM DSS."}],"entry_name":"DDT"}],"statement":[{"text":"Using NMR spectroscopy, only ∼100 of the expected 321 NMR resonances were observed in the 1H, 15N HSQC NMR spectrum, located within a narrow 1H dispersion typical of IDRs (Fig. 1C). ","type":"Results"},{"text":"Using a set of BEST-type triple-resonance NMR experiments, we assigned the backbone resonances of ANAC013161–274 to 81% completeness (Fig. 1C and E; BMRB: 51969). The secondary 13Cα and 13Cβ chemical shifts (Fig. 1E and Supplementary Fig. S2) showed few consistent patterns from transient secondary structures, inferring that ANAC013161–274 is mostly disordered, except for a transient helix between D217 and G232. This helix is populated to ∼20% as deduced from consecutive positive SCSs [52] and overlaps AD1/AI2 (Fig. 1E). ","type":"Results"},{"text":"We therefore assessed\nwhether supramolecular interactions could explain the lack\nof NMR signals and recorded a 1H, 15N HSQC spectrum\nof ANAC013161–498 in 6 M urea (Supplementary Fig. S1D).\nAll resonances were recovered, indicating that a relatively\nlarge part (∼2/3) of the ANAC013 IDR contributes to these\nstructures.","type":"Results"}],"cross_refs":[{"db":"BMRB","id":"51969"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-02T14:31:32.908Z"}},{"start":161,"end":498,"reference_id":"39933695","reference_source":"pmid","reference_html":"Allovalent scavenging of activation domains in the transcription factor ANAC013 gears transcriptional regulation. <i> Delaforge E, Due AD, Theisen FF, Morffy N, O'Shea C, Blackledge M, Strader LC, Skriver K, Kragelund BB. </i> Nucleic Acids Res, 2025","date":"2025-02-26T12:24:05.029Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP03136r015","statement":[{"text":"A SEC analysis indicated higher order soluble structures (Supplementary Fig. S1B), and a far-UV CD spectrum revealed the presence of ∼15% helicity (Fig. 1D), in line with PSIPRED prediction of helicity in the regions 420–460 (Supplementary Fig. S1C). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-19T16:40:11.173Z"}},{"start":161,"end":274,"reference_id":"39933695","reference_source":"pmid","reference_html":"Allovalent scavenging of activation domains in the transcription factor ANAC013 gears transcriptional regulation. <i> Delaforge E, Due AD, Theisen FF, Morffy N, O'Shea C, Blackledge M, Strader LC, Skriver K, Kragelund BB. </i> Nucleic Acids Res, 2025","date":"2025-04-22T11:17:13.373Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP03136r016","statement":[{"text":"The average SAXS curve of these conformers did not reproduce the experimental data accurately (χ2 = 25) (Supplementary Fig. S6A), indicating that ANAC013161–274 does not behave as a statistical coil. The average Rg of this ensemble (31 Å) was smaller than the experimentally determined Rg (36 Å) (Supplementary Fig. S6B), showing ANAC013161–274 to be extended in solution, consistent with its net negative charge (Fig. 1A, middle panel), and correlating with the R2 values that were overall higher than expected for a random coil (Fig. 1D). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-02T14:28:07.876Z"}},{"start":200,"end":230,"reference_id":"39933695","reference_source":"pmid","reference_html":"Allovalent scavenging of activation domains in the transcription factor ANAC013 gears transcriptional regulation. <i> Delaforge E, Due AD, Theisen FF, Morffy N, O'Shea C, Blackledge M, Strader LC, Skriver K, Kragelund BB. </i> Nucleic Acids Res, 2025","date":"2025-03-19T17:09:47.778Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP03136r017","statement":[{"text":"The ANAC013 IDR interacts with the DBD through negatively charged islands—AIs","type":"Results"},{"text":"The two other regions with increased R2values were S200–Q230, AD1/AI2, comprising the transient helix, and V240–E270, AD2/AI3, comprising the RIM (Fig. ​(Fig.1A).1A).","type":"Results"},{"text":" We therefore hypothesized that the IDR interacts with the DBD through dynamic electrostatic interactions between negatively (IDR) and positively (DBD) charged areas. Indeed, R2 rates showed a gradual decrease across the IDR with increasing ionic strength (Fig. ​(Fig.1E, middle1E, middle panel), reflecting screening of the DBD–IDR interaction involving the AD1/AI2 and AD2/AI3 and confirming the observed interactions to be mainly electrostatic.","type":"Results"}]},{"start":240,"end":270,"reference_id":"39933695","reference_source":"pmid","reference_html":"Allovalent scavenging of activation domains in the transcription factor ANAC013 gears transcriptional regulation. <i> Delaforge E, Due AD, Theisen FF, Morffy N, O'Shea C, Blackledge M, Strader LC, Skriver K, Kragelund BB. </i> Nucleic Acids Res, 2025","date":"2025-03-19T17:09:59.317Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP03136r018","statement":[{"text":"The ANAC013 IDR interacts with the DBD through negatively charged islands—AIs","type":"Results"},{"text":"The two other regions with increased R2values were S200–Q230, AD1/AI2, comprising the transient helix, and V240–E270, AD2/AI3, comprising the RIM (Fig. ​(Fig.1A).1A).","type":"Results"},{"text":" We therefore hypothesized that the IDR interacts with the DBD through dynamic electrostatic interactions between negatively (IDR) and positively (DBD) charged areas. Indeed, R2 rates showed a gradual decrease across the IDR with increasing ionic strength (Fig. ​(Fig.1E, middle1E, middle panel), reflecting screening of the DBD–IDR interaction involving the AD1/AI2 and AD2/AI3 and confirming the observed interactions to be mainly electrostatic.","type":"Results"}]},{"start":254,"end":274,"reference_id":"39933695","reference_source":"pmid","reference_html":"Allovalent scavenging of activation domains in the transcription factor ANAC013 gears transcriptional regulation. <i> Delaforge E, Due AD, Theisen FF, Morffy N, O'Shea C, Blackledge M, Strader LC, Skriver K, Kragelund BB. </i> Nucleic Acids Res, 2025","date":"2025-03-19T17:18:41.653Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"M5BF30","operator":null,"partner_start":499,"partner_end":572}],"region_id":"DP03136r019","statement":[{"text":"To decompose a possible second RCD1-RST binding site in ANAC013, we first re-established the interaction between the ANAC013-RIM (N254–T274) and RCD1-RST using ITC at the current conditions, showing the formation of a 1:1 complex with a KD of 70 ± 30 nM (Table 2 and Fig. 3A, left panel) consistent with previous work (KD = 9 ± 4 nM; different buffers [21]).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":254,"end":274,"reference_id":"39933695","reference_source":"pmid","reference_html":"Allovalent scavenging of activation domains in the transcription factor ANAC013 gears transcriptional regulation. <i> Delaforge E, Due AD, Theisen FF, Morffy N, O'Shea C, Blackledge M, Strader LC, Skriver K, Kragelund BB. </i> Nucleic Acids Res, 2025","date":"2025-03-19T17:24:22.297Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"51970"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"M5BF30","operator":null,"partner_start":499,"partner_end":572}],"region_id":"DP03136r020","statement":[{"text":"ANAC013 resonances did not show measurable CSPs upon RCD1-RST addition but underwent extensive line broadening, suggesting slow exchange on the NMR timescale (Fig. 3B and Supplementary Fig. S10A). In both instances, residues corresponding to the RIM (N254–T274) located in AD2/AI3 were broadened beyond detection at a 1:1 ratio of RCD1-RST:ANAC013 (Fig. 3B and Supplementary Fig. S10B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":220,"end":230,"reference_id":"39933695","reference_source":"pmid","reference_html":"Allovalent scavenging of activation domains in the transcription factor ANAC013 gears transcriptional regulation. <i> Delaforge E, Due AD, Theisen FF, Morffy N, O'Shea C, Blackledge M, Strader LC, Skriver K, Kragelund BB. </i> Nucleic Acids Res, 2025","date":"2025-03-19T17:25:13.239Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"51970"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"M5BF30","operator":null,"partner_start":499,"partner_end":572}],"region_id":"DP03136r021","statement":[{"text":"However, a second interaction site was identified in ANAC013 between I220 and Q230, corresponding to the transient helix located in AD1/AI2 (Fig. 1E and Supplementary Fig. S2). For this second site, which bears sequence similarities to the known RIM (Supplementary Fig. S10C), resonances were broadened beyond detection at a ratio of RCD1-RST:ANAC013161–274 of 1.5:1, suggesting a weaker affinity compared to RIM1 (Fig. 4B). We term this second site RIM2 (residues I220–Q230), keeping the known site (N254–T274) as RIM1 (Fig. 1A).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":204,"end":234,"reference_id":"39933695","reference_source":"pmid","reference_html":"Allovalent scavenging of activation domains in the transcription factor ANAC013 gears transcriptional regulation. <i> Delaforge E, Due AD, Theisen FF, Morffy N, O'Shea C, Blackledge M, Strader LC, Skriver K, Kragelund BB. </i> Nucleic Acids Res, 2025","date":"2025-03-19T17:26:45.293Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"M5BF30","operator":null,"partner_start":499,"partner_end":572}],"region_id":"DP03136r022","statement":[{"text":"To investigate the RIM2 interaction with RCD1-RST separately, we produced ANAC013204–234 and studied the interaction by ITC. This revealed a KD of 11 ± 2 μM (Table 2 and Fig. 3A, middle panel). The large entropic penalty (–TΔS = 25 ± 5 kJ mol−1) as well as large enthalpy contribution (ΔH = −53 ± 5 kJ mol−1) suggested that the transient helix (D217–G232) would fold further upon binding.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":217,"end":232,"reference_id":"39933695","reference_source":"pmid","reference_html":"Allovalent scavenging of activation domains in the transcription factor ANAC013 gears transcriptional regulation. <i> Delaforge E, Due AD, Theisen FF, Morffy N, O'Shea C, Blackledge M, Strader LC, Skriver K, Kragelund BB. </i> Nucleic Acids Res, 2025","date":"2025-03-19T17:28:00.790Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006232","ec_ontology":"ECO","ec_name":"differential scanning calorimetry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP03136r023","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"51970"}],"statement":[{"text":"To investigate the RIM2 interaction with RCD1-RST separately, we produced ANAC013204–234 and studied the interaction by ITC. This revealed a KD of 11 ± 2 μM (Table 2 and Fig. 3A, middle panel). The large entropic penalty (–TΔS = 25 ± 5 kJ mol−1) as well as large enthalpy contribution (ΔH = −53 ± 5 kJ mol−1) suggested that the transient helix (D217–G232) would fold further upon binding.","type":"Results"}]}],"regions_counter":23,"released":"2023_12","sequence":"MDLSVENGGLAPGFRFHPTDEELVVYYLKRKIRRKKLRVEAIGETDVYKFDPEELPEKALYKTRDRQWFFFSLRDRKHGSRSSRATERGYWKATGKDRVIHCDSRPVGEKKTLVFHRGRAPNGERTNWVMHEYTLHKEELKRCGGEDVKDAYVLYKIYKKSGSGPKNGEQYGAPFIEEEWAEDDDDDVDEPANQLVVSASVDNSLWGKGLNQSELDDNDIEELMSQVRDQSGPTLQQNGVSGLNSHVDTYNLENLEEDMYLEINDLMEPEPEPTSVEVMENNWNEDGSGLLNDDDFVGADSYFLDLGVTNPQLDFVSGDLKNGFAQSLQVNTSLMTYQANNNQFQQQSGKNQASNWPLRNSYTRQINNGSSWVQELNNDGLTVTRFGEAPGTGDSSEFLNPVPSGISTTNEDDPSKDESSKFASSVWTFLESIPAKPAYASENPFVKLNLVRMSTSGGRFRFTSKSTGNNVVVMDSDSAVKRNKSGGNNDKKKKKNKGFFCLSIIGALCALFWVIIGTMGGSGRPLLW","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"dataset":["Stress response proteins"],"UniParc":"UPI0000162F5F","uniref100":"UniRef100_F4IED2","uniref90":"UniRef90_F4IED2","uniref50":"UniRef50_F4IED2","genes":[{"name":{"value":"NAC013","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AEE31534.1","url":"https://www.ebi.ac.uk/ena/browser/view/AEE31534.1"}}]},"synonyms":[{"value":"NTL1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"17158162","url":"http://www.ncbi.nlm.nih.gov/pubmed/17158162","alternativeUrl":"https://europepmc.org/abstract/MED/17158162"}}]}],"orfNames":[{"value":"F9L11.7","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAF31294.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF31294.1"}}]}],"olnNames":[{"value":"At1g32870","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT1G32870","url":""}}]}]}],"alphafold_very_low_content":0.5132575757575758,"disorder_content":0.6401515151515151,"disprot_consensus":{"full":[{"start":161,"end":216,"type":"D"},{"start":217,"end":232,"type":"T"},{"start":233,"end":253,"type":"D"},{"start":254,"end":274,"type":"T"},{"start":275,"end":498,"type":"D"}],"Structural state":[{"start":161,"end":498,"type":"D"}],"Structural transition":[{"start":217,"end":232,"type":"T"},{"start":254,"end":274,"type":"T"}],"Molecular function":[{"start":161,"end":498,"type":"F"}],"Disorder function":[{"start":200,"end":230,"type":"F"},{"start":240,"end":270,"type":"F"}]}},{"disprot_id":"DP03137","acc":"Q9LUA9","creator":"jssuarez","date":"2021-01-11T12:19:15.877Z","features":{"pfam":[{"id":"PF06203","name":"CCT motif","start":316,"end":358},{"id":"PF22586","name":"ANCHR-like B-box zinc-binding domain","start":47,"end":86}],"gene3D":[]},"length":373,"name":"Zinc finger protein CONSTANS-LIKE 10","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":175,"end":208,"reference_id":"27881680","reference_source":"pmid","reference_html":"Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1. <i> O'Shea C, Staby L, Bendsen SK, Tidemand FG, Redsted A, Willemoës M, Kragelund BB, Skriver K. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03137r001","statement":[{"text":"Experimental analysis for secondary structure content by far-UV CD indicated low α-helical contents of 12, 18, 10, and 13% in the ANAC013(254–274), DREB2A(255–272), COL10(175–208), and bZIP23(15–36) peptides, respectively (Fig. 5, B–E). ","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-13T16:05:53.803Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":175,"end":208,"reference_id":"27881680","reference_source":"pmid","reference_html":"Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1. <i> O'Shea C, Staby L, Bendsen SK, Tidemand FG, Redsted A, Willemoës M, Kragelund BB, Skriver K. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"interaction_partner":[{"db":"UniProt","id":"Q8RY59","partner_start":null,"partner_end":null}],"region_id":"DP03137r002","statement":[{"text":"Putative RCD1-binding motifs were also identified for the B-box transcription factors STO and COL10 (Fig. 3A), which bound RCD1 both in vivo and in vitro (14). Here, the Kd values for the interactions of RCD1 with the STO and COL10 peptides were determined to 90 and 418 nm, respectively. Interestingly, in both cases the change in binding enthalpy was low, −3.8 kJ/mol and −9.2 kJ/mol, respectively, which could be explained by entropy-driven interactions (Table 2).","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-13T16:05:58.225Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":2,"released":"2023_12","sequence":"MGYMCDFCGEQRSMVYCRSDAACLCLSCDRNVHSANALSKRHSRTLVCERCNAQPASVRCSDERVSLCQNCDWSGHDGKNSTTTSHHKRQTINCYSGCPSSAELSSIWSFCMDLNISSAEESACEQGMGLMTIDEDGTGEKSGVQKINVEQPETSSAAQGMDHSSVPENSSMAKELGVCEDDFNGNLISDEVDLALENYEELFGSAFNSSRYLFEHGGIGSLFEKDEAHEGSMQQPALSNNASADSFMTCRTEPIICYSSKPAHSNISFSGITGESNAGDFQDCGASSMKQLSREPQPWCHPTAQDIIASSHATTRNNAVMRYKEKKKARKFDKRVRYVSRKERADVRRRVKGRFVKSGEAYDYDPMSPTRSY","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"dataset":[],"UniParc":"UPI00000017FE","uniref100":"UniRef100_Q9LUA9","uniref90":"UniRef90_Q9LUA9","uniref50":"UniRef50_Q9SSE5","genes":[{"name":{"value":"COL10"},"orfNames":[{"value":"MIF21.14"}],"olnNames":[{"value":"At5g48250"}]}],"alphafold_very_low_content":0.4101876675603217,"disorder_content":0.09115281501340483,"disprot_consensus":{"full":[{"start":175,"end":208,"type":"D"}],"Structural state":[{"start":175,"end":208,"type":"D"}],"Molecular function":[{"start":175,"end":208,"type":"F"}]}},{"disprot_id":"DP03138","acc":"Q8GTS2","creator":"jssuarez","date":"2021-01-11T12:27:06.142Z","features":{"pfam":[{"id":"PF07716","name":"Basic region leucine zipper","start":73,"end":127}],"gene3D":[]},"length":249,"name":"Basic leucine zipper 23","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":15,"end":36,"reference_id":"27881680","reference_source":"pmid","reference_html":"Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1. <i> O'Shea C, Staby L, Bendsen SK, Tidemand FG, Redsted A, Willemoës M, Kragelund BB, Skriver K. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03138r001","statement":[{"text":"Experimental analysis for secondary structure content by far-UV CD indicated low α-helical contents of 12, 18, 10, and 13% in the ANAC013(254–274), DREB2A(255–272), COL10(175–208), and bZIP23(15–36) peptides, respectively (Fig. 5, B–E).","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-13T16:06:41.290Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":15,"end":36,"reference_id":"27881680","reference_source":"pmid","reference_html":"Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1. <i> O'Shea C, Staby L, Bendsen SK, Tidemand FG, Redsted A, Willemoës M, Kragelund BB, Skriver K. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"interaction_partner":[{"db":"UniProt","id":"Q8RY59","partner_start":null,"partner_end":null}],"region_id":"DP03138r002","statement":[{"text":"Peptide bZIP23(15–36), derived from bZIP23, a member of the basic ZIP transcription factor family, interacted with RCD1 with an affinity corresponding to a Kd of 128 nm, comparable with that of the DREB2A·RCD1 interaction (Table 2).","type":"Results"}],"validated":{"curator_name":"Bálint Mészáros","curator_id":"bmesza","timestamp":"2021-01-13T16:06:42.620Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":2,"released":"2023_12","sequence":"MDDGELEFSNSNMGGELPSCSMDSFFDELLRDSHACTHTHTCNPPGPENTHTHTCLHVHTKILPDKVSTDDTSESSGKKRPLGNREAVRKYREKKKAKAASLEDEVMRLKAVNNQLLKRLQGQAALEAEVTRLKCLLVDIRGRIDGEIGAFPYQKPAVTNVPYSYMMHPCNMQCDVDNLYCLQNGNNGEGASMNEQGLNGCEFDQLECLANQNLAGKEIPVCSNGIGTFTVNGSGVNKRKGEPRAAKAV","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"dataset":[],"UniParc":"UPI00000AE2F6","uniref100":"UniRef100_Q8GTS2","uniref90":"UniRef90_Q8GTS2","uniref50":"UniRef50_Q8GTS2","genes":[{"name":{"value":"BZIP23","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11906833","url":"http://www.ncbi.nlm.nih.gov/pubmed/11906833","alternativeUrl":"https://europepmc.org/abstract/MED/11906833"}}]},"olnNames":[{"value":"At2g16770","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT2G16770","url":""}}]}]}],"alphafold_very_low_content":0.3614457831325301,"disorder_content":0.08835341365461848,"disprot_consensus":{"full":[{"start":15,"end":36,"type":"D"}],"Structural state":[{"start":15,"end":36,"type":"D"}],"Molecular function":[{"start":15,"end":36,"type":"F"}]}},{"disprot_id":"DP03139","acc":"Q4VP08","creator":"viglesias","date":"2021-01-11T15:33:06.208Z","features":{"pfam":[{"id":"PF28001","name":"Protein LURE 1.1-1.6, defensin-like domain","start":53,"end":90}],"gene3D":[]},"length":90,"name":"Protein LURE 1.2","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":20,"end":52,"reference_id":"29109411","reference_source":"pmid","reference_html":"Structural basis for receptor recognition of pollen tube attraction peptides. <i> Zhang X, Liu W, Nagae TT, Takeuchi H, Zhang H, Han Z, Higashiyama T, Chai J. </i> Nat Commun, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5Y9W"},{"db":"PDB","id":"5YAH"}],"region_id":"DP03139r001","statement":[{"text":"The N-terminal segment (residues 20–52) of AtLURE1.2 is completely disordered, whereas its C-terminal portion (residues 53–89) adopts a typical structure of plant defensin peptides characterized by cysteine-stabilized αβ-motif (CSαβ)","type":"Results"},{"text":"Therefore, whether and how the N-terminal (residues 21–52) disordered in our structure contributes to AtLURE1.2-induced signaling remain unknown.","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-28T09:14:05.394Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MKLPIIFLTLLIFVSSCTSTLINGSSDEERTYSFSPTTSPFDPRSLNQELKIGRIGYCFDCARACMRRGKYIRTCSFERKLCRCSISDIK","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"dataset":[],"UniParc":"UPI000051DA2F","uniref100":"UniRef100_Q4VP08","uniref90":"UniRef90_Q4VP08","uniref50":"UniRef50_Q4VP08","genes":[{"name":{"value":"LURE1.2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"23271953","url":"http://www.ncbi.nlm.nih.gov/pubmed/23271953","alternativeUrl":"https://europepmc.org/abstract/MED/23271953"}}]},"synonyms":[{"value":"CRP810_1.2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"23271953","url":"http://www.ncbi.nlm.nih.gov/pubmed/23271953","alternativeUrl":"https://europepmc.org/abstract/MED/23271953"}}]}],"orfNames":[{"value":"MWF20.23","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"BAA97430.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAA97430.1"}}]}],"olnNames":[{"value":"At5g43510","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT5G43510","url":""}}]}]}],"alphafold_very_low_content":0.25555555555555554,"disorder_content":0.36666666666666664,"disprot_consensus":{"full":[{"start":20,"end":52,"type":"D"}],"Structural state":[{"start":20,"end":52,"type":"D"}]}},{"disprot_id":"DP03140","acc":"O50008","creator":"viglesias","date":"2021-01-11T15:51:33.045Z","features":{"pfam":[{"id":"PF01717","name":"Cobalamin-independent synthase, Catalytic domain","start":432,"end":755},{"id":"PF08267","name":"Cobalamin-independent synthase, N-terminal domain","start":3,"end":315}],"gene3D":[]},"length":765,"name":"5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 1","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":448,"end":460,"reference_id":"15326182","reference_source":"pmid","reference_html":"Crystal structures of cobalamin-independent methionine synthase complexed with zinc, homocysteine, and methyltetrahydrofolate. <i> Ferrer JL, Ravanel S, Robert M, Dumas R. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1U1J"},{"db":"PDB","id":"1U1H"},{"db":"PDB","id":"1U1U"},{"db":"PDB","id":"1U22"}],"region_id":"DP03140r002","statement":[{"text":"The model was extended to a total of 746 residues (residues 1 and 418–460 were not observed in the electronic density) by manual building using the O molecular modeling package.","type":"Results"},{"text":"Residues 448-460 are missing from the PDBs structures","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-28T09:08:08.984Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MASHIVGYPRMGPKRELKFALESFWDGKSTAEDLQKVSADLRSSIWKQMSAAGTKFIPSNTFAHYDQVLDTTAMLGAVPPRYGYTGGEIGLDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYLLLSKAAKGVDKSFELLSLLPKILPIYKEVITELKAAGATWIQLDEPVLVMDLEGQKLQAFTGAYAELESTLSGLNVLVETYFADIPAEAYKTLTSLKGVTAFGFDLVRGTKTLDLVKAGFPEGKYLFAGVVDGRNIWANDFAASLSTLQALEGIVGKDKLVVSTSCSLLHTAVDLINETKLDDEIKSWLAFAAQKVVEVNALAKALAGQKDEALFSANAAALASRRSSPRVTNEGVQKAAAALKGSDHRRATNVSARLDAQQKKLNLPILPTTTIGSFPQTVELRRVRREYKAKKVSEEDYVKAIKEEIKKVVDLQEELDIDVLVHGEPERNDMVEYFGEQLSGFAFTANGWVQSYGSRCVKPPVIYGDVSRPKAMTVFWSAMAQSMTSRPMKGMLTGPVTILNWSFVRNDQPRHETCYQIALAIKDEVEDLEKGGIGVIQIDEAALREGLPLRKSEHAFYLDWAVHSFRITNCGVQDSTQIHTHMCYSHFNDIIHSIIDMDADVITIENSRSDEKLLSVFREGVKYGAGIGPGVYDIHSPRIPSSEEIADRVNKMLAVLEQNILWVNPDCGLKTRKYTEVKPALKNMVDAAKLIRSQLASAK","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"dataset":[],"UniParc":"UPI0000000BAB","uniref100":"UniRef100_O50008","uniref90":"UniRef90_O50008","uniref50":"UniRef50_O50008","genes":[{"name":{"value":"MS1"},"synonyms":[{"value":"CIMS"}],"orfNames":[{"value":"MPI7.9"}],"olnNames":[{"value":"At5g17920"}]}],"alphafold_very_low_content":0,"disorder_content":0.01699346405228758,"disprot_consensus":{"full":[{"start":448,"end":460,"type":"D"}],"Structural state":[{"start":448,"end":460,"type":"D"}]}},{"disprot_id":"DP03141","acc":"Q9BYG3","creator":"gerdos","date":"2021-01-12T11:57:16.871Z","features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":47,"end":116},{"id":"PF12196","name":"FHA Ki67 binding domain of hNIFK","start":227,"end":266}],"gene3D":[]},"length":293,"name":"MKI67 FHA domain-interacting nucleolar phosphoprotein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":226,"end":269,"reference_id":"16244663","reference_source":"pmid","reference_html":"Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67. <i> Byeon IJ, Li H, Song H, Gronenborn AM, Tsai MD. </i> Nat Struct Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03141r001","statement":[{"text":"In the 1H-15N HSQC spectrum of the free 13C,15N-hNIFK226–2693P peptide (Fig. 1, black contours), the amide resonances of the phosphorylated residues, pSer230, pThr234 and pThr238, were all substantially downfield shifted, consistent with known shift effects of phosphorylation. However, the small spectral dispersion of all other backbone 1HN resonances (7.9–8.5 p.p.m.) clearly indicated that the peptide is essentially unstructured.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-13T17:39:46.145Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":226,"end":269,"reference_id":"16244663","reference_source":"pmid","reference_html":"Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67. <i> Byeon IJ, Li H, Song H, Gronenborn AM, Tsai MD. </i> Nat Struct Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"interaction_partner":[{"db":"UniProt","id":"P46013","partner_start":null,"partner_end":null}],"region_id":"DP03141r002","statement":[{"text":"Upon interaction with Ki67FHA (Fig. 1, red), all resonances showed substantially increased chemical shift dispersion (7.0–10.2 p.p.m.), indicating that the random-coiled peptide adopts a well-defined structure.","type":"Results"},{"text":"For hNIFK226–2693P, on the other hand, a substantial conformational change between the free and bound structures occurs: residues 239–251 become α-helical and residues 260–264 adopt a β-strand conformation. Most notably, this β-strand extends the β-sheet of Ki67FHA, running antiparallel to β4. Residues residing on the α-helix interact with the β4-β5 and β10-β11 loops of Ki67FHA. The peptide shows close packing against Ki67FHA and buries a large surface area of Ki67FHA (1,450 Å2 of a total 6,037 Å2).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-13T17:39:35.018Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":226,"end":269,"reference_id":"16244663","reference_source":"pmid","reference_html":"Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67. <i> Byeon IJ, Li H, Song H, Gronenborn AM, Tsai MD. </i> Nat Struct Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"2AFF"}],"region_id":"DP03141r003","statement":[{"text":"Upon interaction with Ki67FHA (Fig. 1, red), all resonances showed substantially increased chemical shift dispersion (7.0–10.2 p.p.m.), indicating that the random-coiled peptide adopts a well-defined structure.","type":"Results"},{"text":"For hNIFK226–2693P, on the other hand, a substantial conformational change between the free and bound structures occurs: residues 239–251 become α-helical and residues 260–264 adopt a β-strand conformation. Most notably, this β-strand extends the β-sheet of Ki67FHA, running antiparallel to β4. Residues residing on the α-helix interact with the β4-β5 and β10-β11 loops of Ki67FHA. The peptide shows close packing against Ki67FHA and buries a large surface area of Ki67FHA (1,450 Å2 of a total 6,037 Å2).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-13T17:39:38.541Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":226,"end":269,"reference_id":"16244663","reference_source":"pmid","reference_html":"Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67. <i> Byeon IJ, Li H, Song H, Gronenborn AM, Tsai MD. </i> Nat Struct Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"interaction_partner":[{"db":"UniProt","id":"P46013","partner_start":null,"partner_end":null}],"region_id":"DP03141r004","statement":[{"text":"Dissociation constants (Kd) for the Ki67FHA–hNIFK226–269 complexes were determined using surface plasmon resonance (SPR) (Table 1). hNIFK226–2693P bound tightly to Ki67FHA, with a Kd value of 0.077 μM, and the doubly phosphorylated S230A mutant showed only slightly weaker binding.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-13T17:39:32.067Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":228,"end":232,"reference_id":"16244663","reference_source":"pmid","reference_html":"Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67. <i> Byeon IJ, Li H, Song H, Gronenborn AM, Tsai MD. </i> Nat Struct Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03141r005","statement":[{"text":"The forkhead-associated (FHA) domain of human Ki67 interacts with the human nucleolar protein hNIFK, recognizing a 44-residue fragment, hNIFK226–269, phosphorylated at Thr234. Here we show that high-affinity binding requires sequential phosphorylation by two kinases, CDK1 and GSK3, yielding pThr238, pThr234 and pSer230.","type":"Abstract"},{"text":"We speculated that Ser230 might be the third residue and confirmed this proposal by mutagenesis. Phosphorylation of hNIFK226–269 S230A by both kinases resulted only in double phosphorylation (Supplementary Table 1 online).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-13T17:39:30.551Z"},"ec_go":"IMP","disprot_namespace":"Disorder function"},{"start":232,"end":236,"reference_id":"16244663","reference_source":"pmid","reference_html":"Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67. <i> Byeon IJ, Li H, Song H, Gronenborn AM, Tsai MD. </i> Nat Struct Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03141r006","statement":[{"text":"The forkhead-associated (FHA) domain of human Ki67 interacts with the human nucleolar protein hNIFK, recognizing a 44-residue fragment, hNIFK226–269, phosphorylated at Thr234. Here we show that high-affinity binding requires sequential phosphorylation by two kinases, CDK1 and GSK3, yielding pThr238, pThr234 and pSer230.","type":"Abstract"},{"text":"Given that GSK3 can uniquely recognize a priming phosphoryl group at +4 serine or threonine, we tested for the possibility that phosphorylation of Thr234 by GSK3 proceeds only after Thr238 is already phosphorylated by CDK1. Such double phosphorylation was indeed observed and confirmed by MS and mutagenesis. Only a single residue, Thr238, became phosphorylated in the T234A mutant of hNIFK226–269 when both kinases were used.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-13T17:39:29.570Z"},"ec_go":"IMP","disprot_namespace":"Disorder function"},{"start":232,"end":236,"reference_id":"16244663","reference_source":"pmid","reference_html":"Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67. <i> Byeon IJ, Li H, Song H, Gronenborn AM, Tsai MD. </i> Nat Struct Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03141r007","statement":[{"text":"The forkhead-associated (FHA) domain of human Ki67 interacts with the human nucleolar protein hNIFK, recognizing a 44-residue fragment, hNIFK226–269, phosphorylated at Thr234. Here we show that high-affinity binding requires sequential phosphorylation by two kinases, CDK1 and GSK3, yielding pThr238, pThr234 and pSer230.","type":"Abstract"},{"text":"Given that GSK3 can uniquely recognize a priming phosphoryl group at +4 serine or threonine, we tested for the possibility that phosphorylation of Thr234 by GSK3 proceeds only after Thr238 is already phosphorylated by CDK1. Such double phosphorylation was indeed observed and confirmed by MS and mutagenesis. Only a single residue, Thr238, became phosphorylated in the T234A mutant of hNIFK226–269 when both kinases were used.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-13T17:39:28.663Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":236,"end":240,"reference_id":"16244663","reference_source":"pmid","reference_html":"Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67. <i> Byeon IJ, Li H, Song H, Gronenborn AM, Tsai MD. </i> Nat Struct Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03141r008","statement":[{"text":"The forkhead-associated (FHA) domain of human Ki67 interacts with the human nucleolar protein hNIFK, recognizing a 44-residue fragment, hNIFK226–269, phosphorylated at Thr234. Here we show that high-affinity binding requires sequential phosphorylation by two kinases, CDK1 and GSK3, yielding pThr238, pThr234 and pSer230.","type":"Abstract"},{"text":"Mass spectrometry (MS) analyses indicated a single phosphorylation, and the amino acid target of phosphorylation was identified as Thr238 by mutagenesis.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-13T17:45:46.583Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":236,"end":240,"reference_id":"16244663","reference_source":"pmid","reference_html":"Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67. <i> Byeon IJ, Li H, Song H, Gronenborn AM, Tsai MD. </i> Nat Struct Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03141r009","statement":[{"text":"The forkhead-associated (FHA) domain of human Ki67 interacts with the human nucleolar protein hNIFK, recognizing a 44-residue fragment, hNIFK226–269, phosphorylated at Thr234. Here we show that high-affinity binding requires sequential phosphorylation by two kinases, CDK1 and GSK3, yielding pThr238, pThr234 and pSer230.","type":"Abstract"},{"text":"Mass spectrometry (MS) analyses indicated a single phosphorylation, and the amino acid target of phosphorylation was identified as Thr238 by mutagenesis.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-13T17:55:21.437Z"},"ec_go":"IMP","disprot_namespace":"Disorder function"}],"regions_counter":9,"released":"2023_12","sequence":"MATFSGPAGPILSLNPQEDVEFQKEVAQVRKRITQRKKQEQLTPGVVYVRHLPNLLDETQIFSYFSQFGTVTRFRLSRSKRTGNSKGYAFVEFESEDVAKIVAETMNNYLFGERLLECHFMPPEKVHKELFKDWNIPFKQPSYPSVKRYNRNRTLTQKLRMEERFKKKERLLRKKLAKKGIDYDFPSLILQKTESISKTNRQTSTKGQVLRKKKKKVSGTLDTPEKTVDSQGPTPVCTPTFLERRKSQVAELNDDDKDDEIVFKQPISCVKEEIQETQTPTHSRKKRRRSSNQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["RNA-binding proteins"],"UniParc":"UPI00000738EB","uniref100":"UniRef100_Q9BYG3","uniref90":"UniRef90_Q9BYG3","uniref50":"UniRef50_Q9BYG3","genes":[{"name":{"value":"NIFK"},"synonyms":[{"value":"MKI67IP"},{"value":"NOPP34"}]}],"alphafold_very_low_content":0.24914675767918087,"disorder_content":0.15017064846416384,"disprot_consensus":{"full":[{"start":226,"end":269,"type":"T"}],"Structural state":[{"start":226,"end":269,"type":"D"}],"Molecular function":[{"start":226,"end":269,"type":"F"}],"Structural transition":[{"start":226,"end":269,"type":"T"}],"Disorder function":[{"start":228,"end":240,"type":"F"}]}},{"disprot_id":"DP03142","acc":"Q16667","creator":"emaiani","date":"2021-01-12T14:03:30.875Z","features":{"pfam":[{"id":"PF05706","name":"Cyclin-dependent kinase inhibitor 3 (CDKN3)","start":1,"end":168}],"gene3D":[]},"length":212,"name":"Cyclin-dependent kinase inhibitor 3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":22,"reference_id":"11463386","reference_source":"pmid","reference_html":"Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2. <i> Song H, Hanlon N, Brown NR, Noble ME, Johnson LN, Barford D. </i> Mol Cell, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"emaiani","curator_name":"Emiliano Maiani","curator_orcid":"0000-0003-1432-5394","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1FQ1"},{"db":"PDB","id":"1FPZ"}],"region_id":"DP03142r001","statement":[{"text":"Residues 25–198 of KAP were visible in the electron density map; however, the N-terminal PEST sequence of ~23 residues was disordered.","type":"Results"},{"text":"Residues 23–200 were visible in the electron density maps, and the structure has been refined to final Rwork and Rfree of 20.2% and 25.4%, respectively (Table 2).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T10:47:06.981Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":201,"end":212,"reference_id":"11463386","reference_source":"pmid","reference_html":"Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2. <i> Song H, Hanlon N, Brown NR, Noble ME, Johnson LN, Barford D. </i> Mol Cell, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"emaiani","curator_name":"Emiliano Maiani","curator_orcid":"0000-0003-1432-5394","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1FQ1"},{"db":"PDB","id":"1FPZ"}],"region_id":"DP03142r002","statement":[{"text":"Residues 23–200 were visible in the electron density maps, and the structure has been refined to final Rwork and Rfree of 20.2% and 25.4%, respectively (Table 2).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T10:47:06.020Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MKPPSSIQTSEFDSSDEEPIEDEQTPIHISWLSLSRVNCSQFLGLCALPGCKFKDVRRNVQKDTEELKSCGIQDIFVFCTRGELSKYRVPNLLDLYQQCGIITHHHPIADGGTPDIASCCEIMEELTTCLKNYRKTLIHCYGGLGRSCLVAACLLLYLSDTISPEQAIDSLRDLRGSGAIQTIKQYNYLHEFRDKLAAHLSSRDSQSRSVSR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000000D8BB","uniref100":"UniRef100_Q16667","uniref90":"UniRef90_Q16667","uniref50":"UniRef50_Q16667","genes":[{"name":{"value":"CDKN3","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:1791","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:1791"}}]},"synonyms":[{"value":"CDI1"},{"value":"CIP2"},{"value":"KAP"}]}],"alphafold_very_low_content":0.08018867924528301,"disorder_content":0.16037735849056603,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"},{"start":201,"end":212,"type":"D"}],"Structural state":[{"start":1,"end":22,"type":"D"},{"start":201,"end":212,"type":"D"}]}},{"disprot_id":"DP03143","acc":"P49327","creator":"emaiani","date":"2021-01-12T15:16:30.117Z","features":{"pfam":[{"id":"PF00107","name":"Zinc-binding dehydrogenase","start":1679,"end":1815},{"id":"PF00109","name":"Beta-ketoacyl synthase, N-terminal domain","start":1,"end":237},{"id":"PF00550","name":"Phosphopantetheine attachment site","start":2126,"end":2187},{"id":"PF00698","name":"Acyl transferase domain","start":493,"end":809},{"id":"PF00975","name":"Thioesterase domain","start":2242,"end":2500},{"id":"PF02801","name":"Beta-ketoacyl synthase, C-terminal domain","start":243,"end":360},{"id":"PF08242","name":"Methyltransferase domain","start":1244,"end":1342},{"id":"PF08659","name":"KR domain","start":1886,"end":2064},{"id":"PF16197","name":"Ketoacyl-synthetase C-terminal extension","start":362,"end":472},{"id":"PF21089","name":"Polyketide synthase dehydratase domain","start":870,"end":947},{"id":"PF21149","name":"Fatty acid synthase, pseudo-KR domain","start":1421,"end":1519}],"gene3D":[]},"length":2511,"name":"Fatty acid synthase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":2344,"end":2360,"reference_id":"17618296","reference_source":"pmid","reference_html":"Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat. <i> Pemble CW, Johnson LC, Kridel SJ, Lowther WT. </i> Nat Struct Mol Biol, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"emaiani","curator_name":"Emiliano Maiani","curator_orcid":"0000-0003-1432-5394","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2PX6"}],"region_id":"DP03143r002","statement":[{"text":"As a result, a protein model could not be built for the following disordered regions: residues 2326–2328 (loop I, chain B only), 2344–2360 (loop II, both chains), 2450–2460 (loop III, both chains) and residues 2200–2220 and 2502–2510 on the N and C termini, respectively.","type":"Methods"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-13T10:34:27.760Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":2200,"end":2220,"reference_id":"17618296","reference_source":"pmid","reference_html":"Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat. <i> Pemble CW, Johnson LC, Kridel SJ, Lowther WT. </i> Nat Struct Mol Biol, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"emaiani","curator_name":"Emiliano Maiani","curator_orcid":"0000-0003-1432-5394","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2PX6"}],"region_id":"DP03143r004","statement":[{"text":"As a result, a protein model could not be built for the following disordered regions: residues 2326–2328 (loop I, chain B only), 2344–2360 (loop II, both chains), 2450–2460 (loop III, both chains) and residues 2200–2220 and 2502–2510 on the N and C termini, respectively.","type":"Methods"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-13T10:34:32.073Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":2344,"end":2356,"reference_id":"15507492","reference_source":"pmid","reference_html":"Human fatty acid synthase: structure and substrate selectivity of the thioesterase domain. <i> Chakravarty B, Gu Z, Chirala SS, Wakil SJ, Quiocho FA. </i> Proc Natl Acad Sci U S A, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"emaiani","curator_name":"Emiliano Maiani","curator_orcid":"0000-0003-1432-5394","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1XKT"}],"region_id":"DP03143r005","statement":[{"text":"Most of the entire TE domain structure could be fitted into the electron density, except for the three segments and a glycine residue shown in Figs. ​Figs.1,1, ​,2,2, ​,3,3, with missing or weak density, indicating their high mobility. All of the disordered segments are in solvent-exposed regions and nowhere close to being involved in crystal contacts.","type":"Methods"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-13T16:13:13.513Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":5,"released":"2021_12","sequence":"MEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDRRWKAGLYGLPRRSGKLKDLSRFDASFFGVHPKQAHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEALSRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLARRVYATILNAGTNTDGFKEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVGDPQELNGITRALCATRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFHSPNPEIPALLDGRLQVVDQPLPVRGGNVGINSFGFGGSNVHIILRPNTQPPPAPAPHATLPRLLRASGRTPEAVQKLLEQGLRHSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERGGPEVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDRFRDSILRSDEAVKPFGLKVSQLLLSTDESTFDDIVHSFVSLTAIQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAVLAAYWRGQCIKEAHLPPGAMAAVGLSWEECKQRCPPGVVPACHNSKDTVTISGPQAPVFEFVEQLRKEGVFAKEVRTGGMAFHSYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIPEAQWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVVLEIAPHALLQAVLKRGLKPSCTIIPLMKKDHRDNLEFFLAGIGRLHLSGIDANPNALFPPVEFPAPRGTPLISPLIKWDHSLAWDVPAAEDFPNGSGSPSAAIYNIDTSSESPDHYLVDHTLDGRVLFPATGYLSIVWKTLARALGLGVEQLPVVFEDVVLHQATILPKTGTVSLEVRLLEASRAFEVSENGNLVVSGKVYQWDDPDPRLFDHPESPTPNPTEPLFLAQAEVYKELRLRGYDYGPHFQGILEASLEGDSGRLLWKDNWVSFMDTMLQMSILGSAKHGLYLPTRVTAIHIDPATHRQKLYTLQDKAQVADVVVSRWLRVTVAGGVHISGLHTESAPRRQQEQQVPILEKFCFTPHTEEGCLSERAALQEELQLCKGLVQALQTKVTQQGLKMVVPGLDGAQIPRDPSQQELPRLLSAACRLQLNGNLQLELAQVLAQERPKLPEDPLLSGLLDSPALKACLDTAVENMPSLKMKVVEVLAGHGHLYSRIPGLLSPHPLLQLSYTATDRHPQALEAAQAELQQHDVAQGQWDPADPAPSALGSADLLVCNCAVAALGDPASALSNMVAALREGGFLLLHTLLRGHPLGDIVAFLTSTEPQYGQGILSQDAWESLFSRVSLRLVGLKKSFYGSTLFLCRRPTPQDSPIFLPVDDTSFRWVESLKGILADEDSSRPVWLKAINCATSGVVGLVNCLRREPGGNRLRCVLLSNLSSTSHVPEVDPGSAELQKVLQGDLVMNVYRDGAWGAFRHFLLEEDKPEEPTAHAFVSTLTRGDLSSIRWVCSSLRHAQPTCPGAQLCTVYYASLNFRDIMLATGKLSPDAIPGKWTSQDSLLGMEFSGRDASGKRVMGLVPAKGLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGVGQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPQLDSTSFANSRDTSFEQHVLWHTGGKGVDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFFNESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQVLAEEPEAVLKGAKPKLMSAISKTFCPAHKSYIIAGGLGGFGLELAQWLIQRGVQKLVLTSRSGIRTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLLENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNAGQSNYGFANSAMERICEKRRHEGLPGLAVQWGAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLNQPHMVLSSFVLAEKAAAYRDRDSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSVEVRQTLERELNLVLSVREVRQLTLRKLQELSSKADEASELACPTPKEDGLAQQQTQLNLRSLLVNPEGPTLMRLNSVQSSERPLFLVHPIEGSTTVFHSLASRLSIPTYGLQCTRAAPLDSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQQSPAPTHNSLFLFDGSPTYVLAYTQSYRAKLTPGCEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAAVDLIIKSHQGLDRQELSFAARSFYYKLRAAEQYTPKAKYHGNVMLLRAKTGGAYGEDLGADYNLSQVCDGKVSVHVIEGDHRTLLEGSGLESIISIIHSSLAEPRVSVREG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000013EB82","uniref100":"UniRef100_P49327","uniref90":"UniRef90_P49327","uniref50":"UniRef50_P49327","genes":[{"name":{"value":"FASN"},"synonyms":[{"value":"FAS"}]}],"alphafold_very_low_content":0.022700119474313024,"disorder_content":0.015133412982875348,"disprot_consensus":{"full":[{"start":2200,"end":2220,"type":"D"},{"start":2344,"end":2360,"type":"D"}],"Structural state":[{"start":2200,"end":2220,"type":"D"},{"start":2344,"end":2360,"type":"D"}]}},{"disprot_id":"DP03144","acc":"Q05397","creator":"tszani","date":"2021-01-12T15:28:36.816Z","features":{"pfam":[{"id":"PF00373","name":"FERM central domain","start":136,"end":248},{"id":"PF03623","name":"Focal adhesion targeting region","start":912,"end":1048},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":422,"end":676},{"id":"PF18038","name":"FERM N-terminal domain","start":35,"end":130},{"id":"PF21477","name":"FAK1/PYK2, FERM domain C-lobe","start":260,"end":357}],"gene3D":[]},"length":1052,"name":"Focal adhesion kinase 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":565,"end":583,"reference_id":"12467573","reference_source":"pmid","reference_html":"Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography. <i> Nowakowski J, Cronin CN, McRee DE, Knuth MW, Nelson CG, Pavletich NP, Rogers J, Sang BC, Scheibe DN, Swanson RV, Thompson DA. </i> Structure, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1MP8"}],"region_id":"DP03144r001","statement":[{"text":"The majority of the structure is well defined, with the exception of the disordered activation loop (residues 565–583) and a short loop connecting β2 and β3 (residues 445–446) in the N-terminal domain","type":"Methods"},{"text":"The αC helix is rotated away from the C-terminal lobe, and the activation loop is disordered, consistent with a lack of phosphorylation Figure 2, Figure 3, Figure 4.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-12T16:54:50.790Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":565,"end":583,"reference_id":"12467573","reference_source":"pmid","reference_html":"Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography. <i> Nowakowski J, Cronin CN, McRee DE, Knuth MW, Nelson CG, Pavletich NP, Rogers J, Sang BC, Scheibe DN, Swanson RV, Thompson DA. </i> Structure, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"GO:0140677","term_name":"molecular function activator activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"1MP8"}],"region_id":"DP03144r002","statement":[{"text":"The majority of the structure is well defined, with the exception of the disordered activation loop (residues 565–583) and a short loop connecting β2 and β3 (residues 445–446) in the N-terminal domain","type":"Methods"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-12T16:54:51.804Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":2,"released":"2021_12","sequence":"MAAAYLDPNLNHTPNSSTKTHLGTGMERSPGAMERVLKVFHYFESNSEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIADQVDQEIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFTQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGTSQSFIIRPQKEGERALPSIPKLANSEKQGMRTHAVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQTNHYQVSGYPGSHGITAMAGSIYPGQASLLDQTDSWNHRPQEIAMWQPNVEDSTVLDLRGIGQVLPTHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSLQGPIGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLGSLASLSSPADSYNEGVKLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPLLPASTHREIEMAQKLLNSDLGELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMLGQTRPH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000016A8D5","uniref100":"UniRef100_Q05397","uniref90":"UniRef90_Q05397","uniref50":"UniRef50_Q05397","genes":[{"name":{"value":"PTK2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9611","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9611"}}]},"synonyms":[{"value":"FAK"},{"value":"FAK1"}]}],"alphafold_very_low_content":0.26045627376425856,"disorder_content":0.01806083650190114,"disprot_consensus":{"full":[{"start":565,"end":583,"type":"D"}],"Structural state":[{"start":565,"end":583,"type":"D"}],"Molecular function":[{"start":565,"end":583,"type":"F"}]}},{"disprot_id":"DP03145","acc":"P29317","creator":"tszani","date":"2021-01-12T15:34:06.678Z","features":{"pfam":[{"id":"PF00041","name":"Fibronectin type III domain","start":331,"end":420},{"id":"PF00041","name":"Fibronectin type III domain","start":439,"end":524},{"id":"PF00536","name":"SAM domain (Sterile alpha motif)","start":904,"end":966},{"id":"PF01404","name":"Ephrin receptor ligand binding domain","start":30,"end":201},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":614,"end":871},{"id":"PF14575","name":"Ephrin type-A receptor 2 transmembrane domain","start":538,"end":610},{"id":"PF25599","name":"Ephrin cysteine rich domain","start":202,"end":262}],"gene3D":[]},"length":976,"name":"Ephrin type-A receptor 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":761,"end":777,"reference_id":"12467573","reference_source":"pmid","reference_html":"Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography. <i> Nowakowski J, Cronin CN, McRee DE, Knuth MW, Nelson CG, Pavletich NP, Rogers J, Sang BC, Scheibe DN, Swanson RV, Thompson DA. </i> Structure, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1MQB"}],"region_id":"DP03145r001","statement":[{"text":"Most of the structure is well defined, with the exception of residues 596–603 and 734–738 (the loop connecting β2 and β3) and the activation loop residues 760–883.","type":"Methods"},{"text":"The lobes of EphA2 are in the open conformation, and the activation loop is disordered (Figure 2C).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":760,"end":883,"reference_id":"12467573","reference_source":"pmid","reference_html":"Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography. <i> Nowakowski J, Cronin CN, McRee DE, Knuth MW, Nelson CG, Pavletich NP, Rogers J, Sang BC, Scheibe DN, Swanson RV, Thompson DA. </i> Structure, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"GO:0140677","term_name":"molecular function activator activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"1MQB"}],"region_id":"DP03145r002","statement":[{"text":"Most of the structure is well defined, with the exception of residues 596–603 and 734–738 (the loop connecting β2 and β3) and the activation loop residues 760–883.","type":"Methods"},{"text":"The lobes of EphA2 are in the open conformation, and the activation loop is disordered (Figure 2C).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-12T16:57:32.315Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":2,"released":"2021_12","sequence":"MELQAARACFALLWGCALAAAAAAQGKEVVLLDFAAAGGELGWLTHPYGKGWDLMQNIMNDMPIYMYSVCNVMSGDQDNWLRTNWVYRGEAERIFIELKFTVRDCNSFPGGASSCKETFNLYYAESDLDYGTNFQKRLFTKIDTIAPDEITVSSDFEARHVKLNVEERSVGPLTRKGFYLAFQDIGACVALLSVRVYYKKCPELLQGLAHFPETIAGSDAPSLATVAGTCVDHAVVPPGGEEPRMHCAVDGEWLVPIGQCLCQAGYEKVEDACQACSPGFFKFEASESPCLECPEHTLPSPEGATSCECEEGFFRAPQDPASMPCTRPPSAPHYLTAVGMGAKVELRWTPPQDSGGREDIVYSVTCEQCWPESGECGPCEASVRYSEPPHGLTRTSVTVSDLEPHMNYTFTVEARNGVSGLVTSRSFRTASVSINQTEPPKVRLEGRSTTSLSVSWSIPPPQQSRVWKYEVTYRKKGDSNSYNVRRTEGFSVTLDDLAPDTTYLVQVQALTQEGQGAGSKVHEFQTLSPEGSGNLAVIGGVAVGVVLLLVLAGVGFFIHRRRKNQRARQSPEDVYFSKSEQLKPLKTYVDPHTYEDPNQAVLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTSSGKKEVPVAIKTLKAGYTEKQRVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFLREKDGEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEATYTTSGGKIPIRWTAPEAISYRKFTSASDVWSFGIVMWEVMTYGERPYWELSNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQERARRPKFADIVSILDKLIRAPDSLKTLADFDPRVSIRLPSTSGSEGVPFRTVSEWLESIKMQQYTEHFMAAGYTAIEKVVQMTNDDIKRIGVRLPGHQKRIAYSLLGLKDQVNTVGIPI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000012A070","uniref100":"UniRef100_P29317","uniref90":"UniRef90_P29317","uniref50":"UniRef50_P29317","genes":[{"name":{"value":"EPHA2"},"synonyms":[{"value":"ECK"}]}],"alphafold_very_low_content":0.09938524590163934,"disorder_content":0.017418032786885244,"disprot_consensus":{"full":[{"start":760,"end":760,"type":"F"},{"start":761,"end":777,"type":"D"},{"start":778,"end":883,"type":"F"}],"Structural state":[{"start":761,"end":777,"type":"D"}],"Molecular function":[{"start":760,"end":883,"type":"F"}]}},{"disprot_id":"DP03147","acc":"Q86Y38","creator":"mlambrughi","date":"2021-01-12T16:37:39.635Z","features":{"pfam":[{"id":"PF02485","name":"Core-2/I-Branching enzyme","start":328,"end":581},{"id":"PF12529","name":"Xylosyltransferase C terminal","start":613,"end":793}],"gene3D":[]},"length":959,"name":"Xylosyltransferase 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":232,"end":251,"reference_id":"29681470","reference_source":"pmid","reference_html":"Structural Basis for the Initiation of Glycosaminoglycan Biosynthesis by Human Xylosyltransferase 1. <i> Briggs DC, Hohenester E. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"mlambrughi","curator_name":"Matteo Lambrughi","curator_orcid":"0000-0002-0894-8627","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":2,"cross_refs":[{"db":"PDB","id":"6FOA"},{"db":"PDB","id":"6EJ7"},{"db":"PDB","id":"6EJ8"},{"db":"PDB","id":"6EJA"},{"db":"PDB","id":"6EJC"},{"db":"PDB","id":"6EJE"}],"region_id":"DP03147r001","statement":[{"text":"The final model is complete except for the disordered N-terminus (purification tag and XT1 residues 232-251) and two surface loops (XT1 residues 310-313 and 730-735). ","type":"Methods"},{"text":"The N-terminus is disordered in the crystal structure of the apo form of XYLT1 (PDB:6FOA) but also in the structures where XYLT1 is complexed with peptides","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-19T11:45:04.569Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MVAAPCARRLARRSHSALLAALTVLLLQTLVVWNFSSLDSGAGERRGGAAVGGGEQPPPAPAPRRERRDLPAEPAAARGGGGGGGGGGGGRGPQARARGGGPGEPRGQQPASRGALPARALDPHPSPLITLETQDGYFSHRPKEKVRTDSNNENSVPKDFENVDNSNFAPRTQKQKHQPELAKKPPSRQKELLKRKLEQQEKGKGHTFPGKGPGEVLPPGDRAAANSSHGKDVSRPPHARKTGGSSPETKYDQPPKCDISGKEAISALSRAKSKHCRQEIGETYCRHKLGLLMPEKVTRFCPLEGKANKNVQWDEDSVEYMPANPVRIAFVLVVHGRASRQLQRMFKAIYHKDHFYYIHVDKRSNYLHRQVLQVSRQYSNVRVTPWRMATIWGGASLLSTYLQSMRDLLEMTDWPWDFFINLSAADYPIRTNDQLVAFLSRYRDMNFLKSHGRDNARFIRKQGLDRLFLECDAHMWRLGDRRIPEGIAVDGGSDWFLLNRRFVEYVTFSTDDLVTKMKQFYSYTLLPAESFFHTVLENSPHCDTMVDNNLRITNWNRKLGCKCQYKHIVDWCGCSPNDFKPQDFHRFQQTARPTFFARKFEAVVNQEIIGQLDYYLYGNYPAGTPGLRSYWENVYDEPDGIHSLSDVTLTLYHSFARLGLRRAETSLHTDGENSCRYYPMGHPASVHLYFLADRFQGFLIKHHATNLAVSKLETLETWVMPKKVFKIASPPSDFGRLQFSEVGTDWDAKERLFRNFGGLLGPMDEPVGMQKWGKGPNVTVTVIWVDPVNVIAATYDILIESTAEFTHYKPPLNLPLRPGVWTVKILHHWVPVAETKFLVAPLTFSNRQPIKPEEALKLHNGPLRNAYMEQSFQSLNPVLSLPINPAQVEQARRNAASTGTALEGWLDSLVGGMWTAMDICATGPTACPVMQTCSQTAWSSFSPDPKSELGAVKPDGRLR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"UniParc":"UPI000000DCCE","uniref100":"UniRef100_Q86Y38","uniref90":"UniRef90_Q86Y38","uniref50":"UniRef50_Q86Y38","genes":[{"name":{"value":"XYLT1"},"synonyms":[{"value":"XT1"}]}],"alphafold_very_low_content":0.22314911366006257,"disorder_content":0.020855057351407715,"disprot_consensus":{"full":[{"start":232,"end":251,"type":"D"}],"Structural state":[{"start":232,"end":251,"type":"D"}]}},{"disprot_id":"DP03148","acc":"P41227","creator":"mlambrughi","date":"2021-01-12T16:53:49.945Z","features":{"pfam":[{"id":"PF00583","name":"Acetyltransferase (GNAT) family","start":19,"end":124}],"gene3D":[]},"length":235,"name":"N-alpha-acetyltransferase 10","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":161,"end":235,"reference_id":"32042062","reference_source":"pmid","reference_html":"Molecular basis for N-terminal acetylation by human NatE and its modulation by HYPK. <i> Deng S, McTiernan N, Wei X, Arnesen T, Marmorstein R. </i> Nat Commun, 2020","date":"2023-05-05T13:34:39.355Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":3,"cross_refs":[{"db":"PDB","id":"6PPL"},{"db":"PDB","id":"6PW9"},{"db":"EMDB","id":"EMD-20442"},{"db":"EMDB","id":"EMD-20501"}],"region_id":"DP03148r001","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9GZZ1"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9BXJ9"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NX55"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:890"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:444493"}],"statement":[{"text":"The PDB structure of the human NatE complex (NatA/Naa50) and NatE/HYPK complex shows this region of NAA10 protein lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"regions_counter":1,"released":"2021_12","sequence":"MNIRNARPEDLMNMQHCNLLCLPENYQMKYYFYHGLSWPQLSYIAEDENGKIVGYVLAKMEEDPDDVPHGHITSLAVKRSHRRLGLAQKLMDQASRAMIENFNAKYVSLHVRKSNRAALHLYSNTLNFQISEVEPKYYADGEDAYAMKRDLTQMADELRRHLELKEKGRHVVLGAIENKVESKGNSPPSSGEACREEKGLAAEDSGGDSKDLSEVSETTESTDVKDSSEASDSAS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"UniParc":"UPI0000125DBA","uniref100":"UniRef100_P41227","uniref90":"UniRef90_P41227","uniref50":"UniRef50_P41227","genes":[{"name":{"value":"NAA10"},"synonyms":[{"value":"ARD1"},{"value":"ARD1A"},{"value":"TE2"}]}],"alphafold_very_low_content":0.2297872340425532,"disorder_content":0.3191489361702128,"disprot_consensus":{"full":[{"start":161,"end":235,"type":"D"}],"Structural state":[{"start":161,"end":235,"type":"D"}]}},{"disprot_id":"DP03149","acc":"Q9BXJ9","creator":"mlambrughi","date":"2021-01-12T17:39:58.902Z","features":{"pfam":[{"id":"PF12569","name":"N-terminal acetyltransferase A, auxiliary subunit","start":187,"end":698},{"id":"PF13181","name":"Tetratricopeptide repeat","start":83,"end":113}],"gene3D":[]},"length":866,"name":"N-alpha-acetyltransferase 15, NatA auxiliary subunit","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":573,"end":639,"reference_id":"29754825","reference_source":"pmid","reference_html":"Structure of Human NatA and Its Regulation by the Huntingtin Interacting Protein HYPK. <i> Gottlieb L, Marmorstein R. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"mlambrughi","curator_name":"Matteo Lambrughi","curator_orcid":"0000-0002-0894-8627","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6C9M"}],"region_id":"DP03149r001","statement":[{"text":"Using the helical numbering of the S. pombe structure, we did not observe electron density corresponding to the hNatA α33 and α34 helices, which are presumably disordered, and the loop-α40-loop segment of the hNaa15 C-terminus is only resolved in one of the protomer subunits due to stabilization by crystal packing.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T08:07:21.525Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":842,"end":866,"reference_id":"29754825","reference_source":"pmid","reference_html":"Structure of Human NatA and Its Regulation by the Huntingtin Interacting Protein HYPK. <i> Gottlieb L, Marmorstein R. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"mlambrughi","curator_name":"Matteo Lambrughi","curator_orcid":"0000-0002-0894-8627","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6C9M"}],"region_id":"DP03149r002","statement":[{"text":"Using the helical numbering of the S. pombe structure, we did not observe electron density corresponding to the hNatA α33 and α34 helices, which are presumably disordered, and the loop-α40-loop segment of the hNaa15 C-terminus is only resolved in one of the protomer subunits due to stabilization by crystal packing.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T08:07:20.238Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":574,"end":637,"reference_id":"32042062","reference_source":"pmid","reference_html":"Molecular basis for N-terminal acetylation by human NatE and its modulation by HYPK. <i> Deng S, McTiernan N, Wei X, Arnesen T, Marmorstein R. </i> Nat Commun, 2020","date":"2023-05-05T13:26:16.529Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":3,"cross_refs":[{"db":"PDB","id":"6PPL"},{"db":"EMDB","id":"EMD-20442"},{"db":"PDB","id":"6PW9"},{"db":"EMDB","id":"EMD-20501"}],"region_id":"DP03149r003","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9GZZ1 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P41227"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NX55"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:890"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:444493"}],"statement":[{"text":"The PDB structure of the human NatE complex (NatA/Naa50) and NatE/HYPK complex shows this region of  NAA15 protein lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":842,"end":866,"reference_id":"32042062","reference_source":"pmid","reference_html":"Molecular basis for N-terminal acetylation by human NatE and its modulation by HYPK. <i> Deng S, McTiernan N, Wei X, Arnesen T, Marmorstein R. </i> Nat Commun, 2020","date":"2023-05-05T13:28:09.874Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":3,"cross_refs":[{"db":"PDB","id":"6PPL"},{"db":"PDB","id":"6PW9"},{"db":"EMDB","id":"EMD-20442"},{"db":"EMDB","id":"EMD-20501"}],"region_id":"DP03149r004","ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9GZZ1"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P41227"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NX55"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:890"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:444493"}],"statement":[{"text":"The PDB structure of the human NatE complex (NatA/Naa50) and NatE/HYPK complex shows this region of NAA15 protein lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"regions_counter":4,"released":"2021_12","sequence":"MPAVSLPPKENALFKRILRCYEHKQYRNGLKFCKQILSNPKFAEHGETLAMKGLTLNCLGKKEEAYELVRRGLRNDLKSHVCWHVYGLLQRSDKKYDEAIKCYRNALKWDKDNLQILRDLSLLQIQMRDLEGYRETRYQLLQLRPAQRASWIGYAIAYHLLEDYEMAAKILEEFRKTQQTSPDKVDYEYSELLLYQNQVLREAGLYREALEHLCTYEKQICDKLAVEETKGELLLQLCRLEDAADVYRGLQERNPENWAYYKGLEKALKPANMLERLKIYEEAWTKYPRGLVPRRLPLNFLSGEKFKECLDKFLRMNFSKGCPPVFNTLRSLYKDKEKVAIIEELVVGYETSLKSCRLFNPNDDGKEEPPTTLLWVQYYLAQHYDKIGQPSIALEYINTAIESTPTLIELFLVKAKIYKHAGNIKEAARWMDEAQALDTADRFINSKCAKYMLKANLIKEAEEMCSKFTREGTSAVENLNEMQCMWFQTECAQAYKAMNKFGEALKKCHEIERHFIEITDDQFDFHTYCMRKITLRSYVDLLKLEDVLRQHPFYFKAARIAIEIYLKLHDNPLTDENKEHEADTANMSDKELKKLRNKQRRAQKKAQIEEEKKNAEKEKQQRNQKKKKDDDDEEIGGPKEELIPEKLAKVETPLEEAIKFLTPLKNLVKNKIETHLFAFEIYFRKEKFLLMLQSVKRAFAIDSSHPWLHECMIRLFNTAVCESKDLSDTVRTVLKQEMNRLFGATNPKNFNETFLKRNSDSLPHRLSAAKMVYYLDPSSQKRAIELATTLDESLTNRNLQTCMEVLEALYDGSLGDCKEAAEIYRANCHKLFPYALAFMPPGYEEDMKITVNGDSSAEAEELANEI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","RNA-binding proteins"],"UniParc":"UPI000004B631","uniref100":"UniRef100_Q9BXJ9","uniref90":"UniRef90_Q9BXJ9","uniref50":"UniRef50_Q9BXJ9","genes":[{"name":{"value":"NAA15"},"synonyms":[{"value":"GA19"},{"value":"NARG1"},{"value":"NATH"},{"value":"TBDN100"}]}],"alphafold_very_low_content":0.050808314087759814,"disorder_content":0.10623556581986143,"disprot_consensus":{"full":[{"start":573,"end":639,"type":"D"},{"start":842,"end":866,"type":"D"}],"Structural state":[{"start":573,"end":639,"type":"D"},{"start":842,"end":866,"type":"D"}]}},{"disprot_id":"DP03150","acc":"Q99598","creator":"mlambrughi","date":"2021-01-13T03:42:46.327Z","features":{"pfam":[{"id":"PF01997","name":"Translin family","start":51,"end":264}],"gene3D":[]},"length":290,"name":"Translin-associated protein X","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":30,"reference_id":"21552258","reference_source":"pmid","reference_html":"Structure of C3PO and mechanism of human RISC activation. <i> Ye X, Huang N, Liu Y, Paroo Z, Huerta C, Li P, Chen S, Liu Q, Zhang H. </i> Nat Struct Mol Biol, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"mlambrughi","curator_name":"Matteo Lambrughi","curator_orcid":"0000-0002-0894-8627","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3PJA"},{"db":"PDB","id":"3QB5"}],"region_id":"DP03150r001","statement":[{"text":"TRAX also contains several extra loop sequences, of which the N-terminal 30 amino acids and amino acids 157–176 are disordered in the structure.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":157,"end":176,"reference_id":"21552258","reference_source":"pmid","reference_html":"Structure of C3PO and mechanism of human RISC activation. <i> Ye X, Huang N, Liu Y, Paroo Z, Huerta C, Li P, Chen S, Liu Q, Zhang H. </i> Nat Struct Mol Biol, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"mlambrughi","curator_name":"Matteo Lambrughi","curator_orcid":"0000-0002-0894-8627","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3PJA"},{"db":"PDB","id":"3QB5"}],"region_id":"DP03150r002","statement":[{"text":"TRAX also contains several extra loop sequences, of which the N-terminal 30 amino acids and amino acids 157–176 are disordered in the structure.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":275,"end":290,"reference_id":"21552258","reference_source":"pmid","reference_html":"Structure of C3PO and mechanism of human RISC activation. <i> Ye X, Huang N, Liu Y, Paroo Z, Huerta C, Li P, Chen S, Liu Q, Zhang H. </i> Nat Struct Mol Biol, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"mlambrughi","curator_name":"Matteo Lambrughi","curator_orcid":"0000-0002-0894-8627","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3PJA"},{"db":"PDB","id":"3QB5"}],"region_id":"DP03150r003","statement":[{"text":"Upon visual inspection of the crystal structure we identified this region as intrinsically disordered, as described in 21552258","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2021_12","sequence":"MSNKEGSGGFRKRKHDNFPHNQRREGKDVNSSSPVMLAFKSFQQELDARHDKYERLVKLSRDITVESKRTIFLLHRITSAPDMEDILTESEIKLDGVRQKIFQVAQELSGEDMHQFHRAITTGLQEYVEAVSFQHFIKTRSLISMDEINKQLIFTTEDNGKENKTPSSDAQDKQFGTWRLRVTPVDYLLGVADLTGELMRMCINSVGNGDIDTPFEVSQFLRQVYDGFSFIGNTGPYEVSKKLYTLKQSLAKVENACYALKVRGSEIPKHMLADVFSVKTEMIDQEEGIS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI0000137768","uniref100":"UniRef100_Q99598","uniref90":"UniRef90_Q99598","uniref50":"UniRef50_Q99598","genes":[{"name":{"value":"TSNAX"},"synonyms":[{"value":"TRAX"}]}],"alphafold_very_low_content":0.16206896551724137,"disorder_content":0.22758620689655173,"disprot_consensus":{"full":[{"start":1,"end":30,"type":"D"},{"start":157,"end":176,"type":"D"},{"start":275,"end":290,"type":"D"}],"Structural state":[{"start":1,"end":30,"type":"D"},{"start":157,"end":176,"type":"D"},{"start":275,"end":290,"type":"D"}]}},{"disprot_id":"DP03151","acc":"Q13363","creator":"mlambrughi","date":"2021-01-13T04:12:41.940Z","features":{"pfam":[{"id":"PF00389","name":"D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain","start":38,"end":134},{"id":"PF00389","name":"D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain","start":318,"end":352},{"id":"PF02826","name":"D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain","start":135,"end":317}],"gene3D":[]},"length":440,"name":"C-terminal-binding protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":357,"end":378,"reference_id":"29700119","reference_source":"pmid","reference_html":"Assembly of human C-terminal binding protein (CtBP) into tetramers. <i> Bellesis AG, Jecrois AM, Hayes JA, Schiffer CA, Royer WE. </i> J Biol Chem, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"mlambrughi","curator_name":"Matteo Lambrughi","curator_orcid":"0000-0002-0894-8627","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6CDF"}],"region_id":"DP03151r001","statement":[{"text":"Despite an additional 25 residues in the WT and A123V CtBP1(28–378), only four additional residues are evident in the electron density maps and modeled in our final structures (Fig. 5). These results are consistent with findings on rat CtBP that the C terminus is largely disordered (31).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T16:44:15.513Z"}}],"regions_counter":1,"released":"2021_12","sequence":"MGSSHLLNKGLPLGVRPPIMNGPLHPRPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKNCVNKDHLTAATHWASMDPAVVHPELNGAAYRYPPGVVGVAPTGIPAAVEGIVPSAMSLSHGLPPVAHPPHAPSPGQTVKPEADRDHASDQL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"UniParc":"UPI00001487FE","uniref100":"UniRef100_Q13363","uniref90":"UniRef90_Q13363","uniref50":"UniRef50_P56545","genes":[{"name":{"value":"CTBP1"},"synonyms":[{"value":"CTBP"}]}],"alphafold_very_low_content":0.21136363636363636,"disorder_content":0.05,"disprot_consensus":{"full":[{"start":357,"end":378,"type":"D"}],"Structural state":[{"start":357,"end":378,"type":"D"}]}},{"disprot_id":"DP03152","acc":"P42574","creator":"emaiani","date":"2021-01-13T14:22:33.755Z","features":{"pfam":[{"id":"PF00656","name":"Caspase domain","start":45,"end":274}],"gene3D":[]},"length":277,"name":"Caspase-3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":57,"end":66,"reference_id":"23650375","reference_source":"pmid","reference_html":"Structural snapshots reveal distinct mechanisms of procaspase-3 and -7 activation. <i> Thomsen ND, Koerber JT, Wells JA. </i> Proc Natl Acad Sci U S A, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"emaiani","curator_name":"Emiliano Maiani","curator_orcid":"0000-0003-1432-5394","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4JQY"},{"db":"PDB","id":"4JQZ"}],"region_id":"DP03152r001","statement":[{"text":"The P3-1 structure contains a dimer in the asymmetric unit and resolves ∼80% of the amino acids due to a number of disordered loops.","type":"Results"},{"text":"First, loop-1 (L1), which to our knowledge is visible in every C3 and C7 structure solved to date, is disordered in the structure of P3. This includes disorder of Arg64, one of the primary residues responsible for binding the P1 aspartate in caspase substrates.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T09:01:58.316Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":201,"end":211,"reference_id":"23650375","reference_source":"pmid","reference_html":"Structural snapshots reveal distinct mechanisms of procaspase-3 and -7 activation. <i> Thomsen ND, Koerber JT, Wells JA. </i> Proc Natl Acad Sci U S A, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"emaiani","curator_name":"Emiliano Maiani","curator_orcid":"0000-0003-1432-5394","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4JQY"},{"db":"PDB","id":"4JQZ"}],"region_id":"DP03152r002","statement":[{"text":"The P3-1 structure contains a dimer in the asymmetric unit and resolves ∼80% of the amino acids due to a number of disordered loops.","type":"Results"},{"text":"Loop-3 (L3), or the “activation loop,” which forms the primary substrate binding groove in the active enzyme, is pulled out of the active site in both P3 monomers, although one is partially disordered whereas the other is fully resolved (Fig. 1 A and B). This could be caused in part by asymmetric crystal packing contacts that appear to stabilize the single L3 resolved in our structure, although the existing structures of P7 (PDB ID codes 1K88 and 1GQF) also reveal a variety of ordered and disordered L3s, suggesting that this loop samples a large number of conformations in P3 and P7 (8, 9).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T09:01:13.741Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":165,"end":185,"reference_id":"23650375","reference_source":"pmid","reference_html":"Structural snapshots reveal distinct mechanisms of procaspase-3 and -7 activation. <i> Thomsen ND, Koerber JT, Wells JA. </i> Proc Natl Acad Sci U S A, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"emaiani","curator_name":"Emiliano Maiani","curator_orcid":"0000-0003-1432-5394","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4JQY"},{"db":"PDB","id":"4JQZ"},{"db":"PDB","id":"4JR0"}],"region_id":"DP03152r003","statement":[{"text":"The P3-1 structure contains a dimer in the asymmetric unit and resolves ∼80% of the amino acids due to a number of disordered loops.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T08:58:16.707Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":174,"end":184,"reference_id":"18768468","reference_source":"pmid","reference_html":"Isoquinoline-1,3,4-trione derivatives inactivate caspase-3 by generation of reactive oxygen species. <i> Du JQ, Wu J, Zhang HJ, Zhang YH, Qiu BY, Wu F, Chen YH, Li JY, Nan FJ, Ding JP, Li J. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"emaiani","curator_name":"Emiliano Maiani","curator_orcid":"0000-0003-1432-5394","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3DEI"}],"region_id":"DP03152r004","statement":[{"text":"Residues belonging to loop 2 are not resolved.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T08:52:40.889Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":4,"released":"2021_12","sequence":"MENTENSVDSKSIKNLEPKIIHGSESMDSGISLDNSYKMDYPEMGLCIIINNKNFHKSTGMTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLSHGEEGIIFGTNGPVDLKKITNFFRGDRCRSLTGKPKLFIIQACRGTELDCGIETDSGVDDDMACHKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVNRKVATEFESFSFDATFHAKKQIPCIVSMLTKELYFYH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins","Cancer-related proteins"],"UniParc":"UPI000003AEF9","uniref100":"UniRef100_P42574","uniref90":"UniRef90_P42574","uniref50":"UniRef50_P42574","genes":[{"name":{"value":"CASP3"},"synonyms":[{"value":"CPP32"}]}],"alphafold_very_low_content":0.1552346570397112,"disorder_content":0.15162454873646208,"disprot_consensus":{"full":[{"start":57,"end":66,"type":"D"},{"start":165,"end":185,"type":"D"},{"start":201,"end":211,"type":"D"}],"Structural state":[{"start":57,"end":66,"type":"D"},{"start":165,"end":185,"type":"D"},{"start":201,"end":211,"type":"D"}]}},{"disprot_id":"DP03153","acc":"Q658P3","creator":"gerdos","date":"2021-01-13T15:18:50.370Z","features":{"pfam":[{"id":"PF01794","name":"Ferric reductase like transmembrane component","start":261,"end":404},{"id":"PF03807","name":"NADP oxidoreductase coenzyme F420-dependent","start":30,"end":117}],"gene3D":[]},"length":488,"name":"Metalloreductase STEAP3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":28,"reference_id":"18495927","reference_source":"pmid","reference_html":"Structure of the membrane proximal oxidoreductase domain of human Steap3, the dominant ferrireductase of the erythroid transferrin cycle. <i> Sendamarai AK, Ohgami RS, Fleming MD, Lawrence CM. </i> Proc Natl Acad Sci U S A, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2VNS"},{"db":"PDB","id":"2VQ3"}],"region_id":"DP03153r001","statement":[{"text":"The N-terminal His-tag and Steap3 residues 1–28 are not observed in the crystal structure. However, Western blot analyses of the crystallized\nmaterial, using anti-His6 antibodies, indicate that these N-terminal residues are indeed present and are therefore disordered in the crystal.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-13T16:26:21.564Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MPEEMDKPLISLHLVDSDSSLAKVPDEAPKVGILGSGDFARSLATRLVGSGFKVVVGSRNPKRTARLFPSAAQVTFQEEAVSSPEVIFVAVFREHYSSLCSLSDQLAGKILVDVSNPTEQEHLQHRESNAEYLASLFPTCTVVKAFNVISAWTLQAGPRDGNRQVPICGDQPEAKRAVSEMALAMGFMPVDMGSLASAWEVEAMPLRLLPAWKVPTLLALGLFVCFYAYNFVRDVLQPYVQESQNKFFKLPVSVVNTTLPCVAYVLLSLVYLPGVLAAALQLRRGTKYQRFPDWLDHWLQHRKQIGLLSFFCAALHALYSFCLPLRRAHRYDLVNLAVKQVLANKSHLWVEEEVWRMEIYLSLGVLALGTLSLLAVTSLPSIANSLNWREFSFVQSSLGFVALVLSTLHTLTYGWTRAFEESRYKFYLPPTFTLTLLVPCVVILAKALFLLPCISRRLARIRRGWERESTIKFTLPTDHALAEKTSHV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI0000207E04","uniref100":"UniRef100_Q658P3","uniref90":"UniRef90_Q658P3","uniref50":"UniRef50_Q658P3","genes":[{"name":{"value":"STEAP3"},"synonyms":[{"value":"TSAP6"}]}],"alphafold_very_low_content":0.07991803278688525,"disorder_content":0.05737704918032787,"disprot_consensus":{"full":[{"start":1,"end":28,"type":"D"}],"Structural state":[{"start":1,"end":28,"type":"D"}]}},{"disprot_id":"DP03154","acc":"P35207","creator":"gerdos","date":"2021-01-13T16:38:56.986Z","features":{"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":333,"end":482},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":653,"end":768},{"id":"PF08148","name":"DSHCT (NUC185) domain","start":1109,"end":1282},{"id":"PF17911","name":"Ski2 N-terminal region","start":83,"end":215},{"id":"PF21408","name":"Exosome RNA helicase MTR4-like, stalk","start":823,"end":888},{"id":"PF21409","name":"Ski2, beta-barrel domain","start":899,"end":985}],"gene3D":[]},"length":1287,"name":"Antiviral helicase SKI2","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":542,"end":606,"reference_id":"22114319","reference_source":"pmid","reference_html":"The crystal structure of S. cerevisiae Ski2, a DExH helicase associated with the cytoplasmic functions of the exosome. <i> Halbach F, Rode M, Conti E. </i> RNA, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4A4Z"},{"db":"PDB","id":"4A4K"}],"region_id":"DP03154r001","statement":[{"text":"The DExH helicase core of Ski2-ΔN could be built and refined almost in its entirety (with the exception of a disordered region between residues 542 and 606) and included electron density for an AMPPNP molecule.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-28T09:41:34.399Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MSEGFSSSSIQELYQSLKEITNNADVELFEDRITKLDFESTDEPKHANDIIKDRFLRPSNALPWSLLDMVQDVPHTSSPEDCSGKLDYKELLKVPDPINRTSYQFKRTGLEGKISGYKEEVDLKEVANANASNSLSITRSINHNQNSVRGSTAQLPFTPGGIPMKSVKTDSEQNGSSTMANATKLLHKDGQGLFDIPEGMNRGIKPMDSPAENEDQNGQFKELKQLNEIDNELDIRIEANEAKLKEEEKSAKSISEEIMEEATEETTADNADDAEIDELLPIGIDFGRTKPVSKSVPVKKEWAHVVDLNHKIENFDELIPNPARSWPFELDTFQKEAVYHLEQGDSVFVAAHTSAGKTVVAEYAIAMAHRNMTKTIYTSPIKALSNQKFRDFKETFDDVNIGLITGDVQINPDANCLIMTTEILRSMLYRGADLIRDVEFVIFDEVHYVNDQDRGVVWEEVIIMLPQHVKFILLSATVPNTYEFANWIGRTKQKNIYVISTPKRPVPLEINIWAKKELIPVINQNSEFLEANFRKHKEILNGESAKGAPSKTDNGRGGSTARGGRGGSNTRDGRGGRGNSTRGGANRGGSRGAGAIGSNKRKFFTQDGPSKKTWPEIVNYLRKRELLPMVVFVFSKKRCEEYADWLEGINFCNNKEKSQIHMFIEKSITRLKKEDRDLPQILKTRSLLERGIAVHHGGLLPIVKELIEILFSKGFIKVLFATETFAMGLNLPTRTVIFSSIRKHDGNGLRELTPGEFTQMAGRAGRRGLDSTGTVIVMAYNSPLSIATFKEVTMGVPTRLQSQFRLTYNMILNLLRIEALRVEEMIKYSFSENAKETLQPEHEKQIKVLQEELQTIEYKSCEICDNDIEKFLELMLAYKEATVNLMQEMVKSPSILHILKEGRLVAFRDPNDCLKLGFVFKVSLKDAVCVIMTFTKPYKLPNGEPNHLIYFPKADGYRRRNFPKFQKTDFYMEEVPVTAIEVITKRKFAAPLGKVIKKDVAALNEFNAETNNILDGKTLKEAINIEKQGLKIHQILLDRTNIRDEIFKLKSIKCPNLSQHIVPKFKAHVIKKKIEELYHLMSDQNLSLLPDYEKRLAVLKDTEFIDQNHNVLLKGRVACEINSGYELVLTELILDNFLGSFEPEEIVALLSVFVYEGKTREEEPPIVTPRLAKGKQRIEEIYKKMLCVFNTHQIPLTQDEAEFLDRKRFAMMNVVYEWARGLSFKEIMEMSPEAEGTVVRVITWLDEICREVKTASIIIGNSTLHMKMSRAQELIKRDIVFAASLYL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"dataset":["RNA-binding proteins"],"UniParc":"UPI0000168E36","uniref100":"UniRef100_P35207","uniref90":"UniRef90_P35207","uniref50":"UniRef50_P35207","genes":[{"name":{"value":"SKI2"},"orfNames":[{"value":"L8084.17"}],"olnNames":[{"value":"YLR398C"}]}],"alphafold_very_low_content":0.09634809634809635,"disorder_content":0.050505050505050504,"disprot_consensus":{"full":[{"start":542,"end":606,"type":"D"}],"Structural state":[{"start":542,"end":606,"type":"D"}]}},{"disprot_id":"DP03155","acc":"P01019","creator":"achasapi","date":"2021-01-13T17:07:01.366Z","features":{"pfam":[{"id":"PF00079","name":"Serpin (serine protease inhibitor)","start":102,"end":472}],"gene3D":[]},"length":476,"name":"Angiotensinogen","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":428,"end":439,"reference_id":"20927107","reference_source":"pmid","reference_html":"A redox switch in angiotensinogen modulates angiotensin release. <i> Zhou A, Carrell RW, Murphy MP, Wei Z, Yan Y, Stanley PL, Stein PE, Broughton Pipkin F, Read RJ. </i> Nature, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"achasapi","curator_name":"Anastasia Chasapi","curator_orcid":"0000-0003-1986-5007","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2WXW"},{"db":"PDB","id":"2X0B"}],"region_id":"DP03155r001","statement":[{"text":" With the exception of the exposed and hence mobile reactive centre loop (residues 408-425), the overall results show the complete fold of the human molecule including the full amino-terminal extension with the renin cleavage site (Fig 1a).","type":"Results"},{"text":"The disorder region boundaries differ from the ones mentioned in the article as there is a signal peptide of 33 amino acids not accounted for.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":43,"end":54,"reference_id":"20927107","reference_source":"pmid","reference_html":"A redox switch in angiotensinogen modulates angiotensin release. <i> Zhou A, Carrell RW, Murphy MP, Wei Z, Yan Y, Stanley PL, Stein PE, Broughton Pipkin F, Read RJ. </i> Nature, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"achasapi","curator_name":"Anastasia Chasapi","curator_orcid":"0000-0003-1986-5007","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2X0B"}],"region_id":"DP03155r002","statement":[{"text":"The mouse structures were determined at higher resolution (2.3, 2.1, 2.95Å) but the general features are preserved in the 3.15Å rat and 3.3Å human structures (as shown separately and with statistics in Figure 2 and Table 1 of the Supplementary information).","type":"Results"},{"text":"Although the disordered region in not explicitly mentioned, it is shown in the deposited PDB structure.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":43,"end":53,"reference_id":"30563843","reference_source":"pmid","reference_html":"Structural basis for the specificity of renin-mediated angiotensinogen cleavage. <i> Yan Y, Zhou A, Carrell RW, Read RJ. </i> J Biol Chem, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"achasapi","curator_name":"Anastasia Chasapi","curator_orcid":"0000-0003-1986-5007","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5M3Y"},{"db":"PDB","id":"5M3X"},{"db":"PDB","id":"6I3I"}],"region_id":"DP03155r003","statement":[{"text":"The segment from Glu20 to Pro29 (dashed, pale green) is disordered in the structure and modeled for illustration. ","type":"Figure"},{"text":"The correct disordered region boundaries also account for angiotensinogen's signal peptide.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":427,"end":440,"reference_id":"30563843","reference_source":"pmid","reference_html":"Structural basis for the specificity of renin-mediated angiotensinogen cleavage. <i> Yan Y, Zhou A, Carrell RW, Read RJ. </i> J Biol Chem, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"achasapi","curator_name":"Anastasia Chasapi","curator_orcid":"0000-0003-1986-5007","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5M3Y"}],"region_id":"DP03155r004","statement":[{"text":"The serpin template is in gray, and helix A (hA) is in marine with the A-sheet (sA) in light blue and the disordered RCL in red dashes. ","type":"Figure"},{"text":"The disordered region boundaries for the Reactive Center Loop (RCL) are not mentioned but were deposited in PDB.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":35,"end":55,"reference_id":"30563843","reference_source":"pmid","reference_html":"Structural basis for the specificity of renin-mediated angiotensinogen cleavage. <i> Yan Y, Zhou A, Carrell RW, Read RJ. </i> J Biol Chem, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"achasapi","curator_name":"Anastasia Chasapi","curator_orcid":"0000-0003-1986-5007","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5M3X"}],"region_id":"DP03155r005","statement":[{"text":"Subsequently, we prepared spent AGT, where the N-terminal 10-residue angiotensin I peptide was removed from the AGT-N14 expression construct and loop- cleaved AGT, where AGT-N14 was cleaved between Gln412 and Leu413 by thermolysin treatment.","type":"Results"},{"text":"Removal of the N-terminal decapeptide augments the disordered region (evidence in PDB entry)","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":427,"end":441,"reference_id":"30563843","reference_source":"pmid","reference_html":"Structural basis for the specificity of renin-mediated angiotensinogen cleavage. <i> Yan Y, Zhou A, Carrell RW, Read RJ. </i> J Biol Chem, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"achasapi","curator_name":"Anastasia Chasapi","curator_orcid":"0000-0003-1986-5007","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6I3F"}],"region_id":"DP03155r006","statement":[{"text":"The fragments without clear electron density are shown with dashed lines for illustration.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T10:11:33.966Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":40,"end":52,"reference_id":"30563843","reference_source":"pmid","reference_html":"Structural basis for the specificity of renin-mediated angiotensinogen cleavage. <i> Yan Y, Zhou A, Carrell RW, Read RJ. </i> J Biol Chem, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"achasapi","curator_name":"Anastasia Chasapi","curator_orcid":"0000-0003-1986-5007","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6I3F"}],"region_id":"DP03155r007","statement":[{"text":"The fragments without clear electron density are shown with dashed lines for illustration.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T10:12:15.041Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":7,"released":"2021_12","sequence":"MAPAGVSLRATILCLLAWAGLAAGDRVYIHPFHLVIHNESTCEQLAKANAGKPKDPTFIPAPIQAKTSPVDEKALQDQLVLVAAKLDTEDKLRAAMVGMLANFLGFRIYGMHSELWGVVHGATVLSPTAVFGTLASLYLGALDHTADRLQAILGVPWKDKNCTSRLDAHKVLSALQAVQGLLVAQGRADSQAQLLLSTVVGVFTAPGLHLKQPFVQGLALYTPVVLPRSLDFTELDVAAEKIDRFMQAVTGWKTGCSLMGASVDSTLAFNTYVHFQGKMKGFSLLAEPQEFWVDNSTSVSVPMLSGMGTFQHWSDIQDNFSVTQVPFTESACLLLIQPHYASDLDKVEGLTFQQNSLNWMKKLSPRTIHLTMPQLVLQGSYDLQDLLAQAELPAILHTELNLQKLSNDRIRVGEVLNSIFFELEADEREPTESTQQLNKPEVLEVTLNRPFLFAVYDQSATALHFLGRVANPLSTA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000125B13","uniref100":"UniRef100_P01019","uniref90":"UniRef90_P01019","uniref50":"UniRef50_P01019","genes":[{"name":{"value":"AGT"},"synonyms":[{"value":"SERPINA8"}]}],"alphafold_very_low_content":0.07216494845360824,"disorder_content":0.07563025210084033,"disprot_consensus":{"full":[{"start":35,"end":55,"type":"D"},{"start":427,"end":441,"type":"D"}],"Structural state":[{"start":35,"end":55,"type":"D"},{"start":427,"end":441,"type":"D"}]}},{"disprot_id":"DP03156","acc":"P11859","creator":"achasapi","date":"2021-01-13T18:14:15.820Z","features":{"pfam":[{"id":"PF00079","name":"Serpin (serine protease inhibitor)","start":102,"end":473}],"gene3D":[]},"length":477,"name":"Angiotensinogen","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":431,"end":440,"reference_id":"20927107","reference_source":"pmid","reference_html":"A redox switch in angiotensinogen modulates angiotensin release. <i> Zhou A, Carrell RW, Murphy MP, Wei Z, Yan Y, Stanley PL, Stein PE, Broughton Pipkin F, Read RJ. </i> Nature, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"achasapi","curator_name":"Anastasia Chasapi","curator_orcid":"0000-0003-1986-5007","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2WY0"},{"db":"PDB","id":"2WXY"}],"region_id":"DP03156r001","statement":[{"text":"The mouse structures were determined at higher resolution (2.3, 2.1, 2.95Å) but the general features are preserved in the 3.15Å rat and 3.3Å human structures (as shown separately and with statistics in Figure 2 and Table 1 of the Supplementary information).","type":"Results"},{"text":"With the exception of the exposed and hence mobile reactive centre loop (residues 408-425), the overall results show the complete fold of the human molecule including the full amino-terminal extension with the renin cleavage site (Fig 1a)","type":"Results"},{"text":"Exact boundary statements in the text concern only human angiotensinogen but the exact boundaries of the disordered regions in mouse can be found at the deposited structure in PDB","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":429,"end":440,"reference_id":"20927107","reference_source":"pmid","reference_html":"A redox switch in angiotensinogen modulates angiotensin release. <i> Zhou A, Carrell RW, Murphy MP, Wei Z, Yan Y, Stanley PL, Stein PE, Broughton Pipkin F, Read RJ. </i> Nature, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"achasapi","curator_name":"Anastasia Chasapi","curator_orcid":"0000-0003-1986-5007","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2WXX"}],"region_id":"DP03156r002","statement":[{"text":"The mouse structures were determined at higher resolution (2.3, 2.1, 2.95Å) but the general features are preserved in the 3.15Å rat and 3.3Å human structures (as shown separately and with statistics in Figure 2 and Table 1 of the Supplementary information).","type":"Results"},{"text":"With the exception of the exposed and hence mobile reactive centre loop (residues 408-425), the overall results show the complete fold of the human molecule including the full amino-terminal extension with the renin cleavage site (Fig 1a)","type":"Results"},{"text":"Exact boundary statements in the text concern only human angiotensinogen but the exact boundaries of the disordered regions in mouse can be found at the deposited structure in PDB","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":41,"end":51,"reference_id":"20927107","reference_source":"pmid","reference_html":"A redox switch in angiotensinogen modulates angiotensin release. <i> Zhou A, Carrell RW, Murphy MP, Wei Z, Yan Y, Stanley PL, Stein PE, Broughton Pipkin F, Read RJ. </i> Nature, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"achasapi","curator_name":"Anastasia Chasapi","curator_orcid":"0000-0003-1986-5007","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2WXY"}],"region_id":"DP03156r003","statement":[{"text":"The mouse structures were determined at higher resolution (2.3, 2.1, 2.95Å) but the general features are preserved in the 3.15Å rat and 3.3Å human structures (as shown separately and with statistics in Figure 2 and Table 1 of the Supplementary information).","type":"Results"},{"text":"Exact boundary statements in the text concern only human angiotensinogen but the exact boundaries of the disordered regions in mouse can be found at the deposited structure in PDB","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2021_12","sequence":"MTPTGAGLKATIFCILTWVSLTAGDRVYIHPFHLLYHNKSTCAQLENPSVETLPESTFEPVPIQAKTSPVNEKTLHDQLVLAAEKLEDEDRKRAAQVAMIANFVGFRMYKMLNEAGSGASGAILSPPALFGTLVSFYLGSLDPTASQLQTLLDVPVKEGDCTSRLDGHKVLAALRAVQGLLVTQGGSSSQTPLLQSIMVGLFTAPGFRLKHSFVQSLALFTPALFPRSLDLSTDPVLATEKINRFIKAVTGWKMNLPLEGVSTDSTLLFNTYVHFQGTMRGFSQLPGVHEFWVDNSISVSVPMISGTGNFQHWSDAQNNFSVTCVPLGERATLLLIQPHCTSDLDRVEALIFRNDLLTWIENPPPRAIRLTLPQLEIRGSYNLQDLLAEDKLPTLLGAEANLSNIGDTNPRVGEVLNSILLELKAGEEEQPTTSVQQPGSPEALDVTLSSPFLFAIYEQDSGTLHFLGRVNNPQSVV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"dataset":[],"UniParc":"UPI0000027DFE","uniref100":"UniRef100_P11859","uniref90":"UniRef90_P11859","uniref50":"UniRef50_P01019","genes":[{"name":{"value":"Agt"},"synonyms":[{"value":"Serpina8"}]}],"alphafold_very_low_content":0.08385744234800839,"disorder_content":0.04821802935010482,"disprot_consensus":{"full":[{"start":41,"end":51,"type":"D"},{"start":429,"end":440,"type":"D"}],"Structural state":[{"start":41,"end":51,"type":"D"},{"start":429,"end":440,"type":"D"}]}},{"disprot_id":"DP03158","acc":"P54578","creator":"gerdos","date":"2021-01-13T20:23:46.590Z","features":{"pfam":[{"id":"PF00443","name":"Ubiquitin carboxyl-terminal hydrolase","start":105,"end":480}],"gene3D":[]},"length":494,"name":"Ubiquitin carboxyl-terminal hydrolase 14","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":484,"end":494,"reference_id":"16211010","reference_source":"pmid","reference_html":"Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14. <i> Hu M, Li P, Song L, Jeffrey PD, Chenova TA, Wilkinson KD, Cohen RE, Shi Y. </i> EMBO J, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"2AYN"},{"db":"PDB","id":"2AYO"}],"region_id":"DP03158r003","statement":[{"text":"There is no significant electron density for residues 94–98, 217–234, 380–397, and 484–494; these residues are\nlikely flexible and disordered in the crystals.","type":"Methods"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-14T10:16:09.620Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":4,"released":"2023_12","sequence":"MPLYSVTVKWGKEKFEGVELNTDEPPMVFKAQLFALTGVQPARQKVMVKGGTLKDDDWGNIKIKNGMTLLMMGSADALPEEPSAKTVFVEDMTEEQLASAMELPCGLTNLGNTCYMNATVQCIRSVPELKDALKRYAGALRASGEMASAQYITAALRDLFDSMDKTSSSIPPIILLQFLHMAFPQFAEKGEQGQYLQQDANECWIQMMRVLQQKLEAIEDDSVKETDSSSASAATPSKKKSLIDQFFGVEFETTMKCTESEEEEVTKGKENQLQLSCFINQEVKYLFTGLKLRLQEEITKQSPTLQRNALYIKSSKISRLPAYLTIQMVRFFYKEKESVNAKVLKDVKFPLMLDMYELCTPELQEKMVSFRSKFKDLEDKKVNQQPNTSDKKSSPQKEVKYEPFSFADDIGSNNCGYYDLQAVLTHQGRSSSSGHYVSWVKRKQDEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLYGPRRVEIMEEESEQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI00001379F5","uniref100":"UniRef100_P54578","uniref90":"UniRef90_P54578","uniref50":"UniRef50_P54578","genes":[{"name":{"value":"USP14"},"synonyms":[{"value":"TGT"}]}],"alphafold_very_low_content":0.0708502024291498,"disorder_content":0.022267206477732792,"disprot_consensus":{"full":[{"start":484,"end":494,"type":"D"}],"Structural state":[{"start":484,"end":494,"type":"D"}]}},{"disprot_id":"DP03159","acc":"Q9UBR1","creator":"achasapi","date":"2021-01-13T20:30:25.515Z","features":{"pfam":[{"id":"PF00795","name":"Carbon-nitrogen hydrolase","start":74,"end":350}],"gene3D":[]},"length":384,"name":"Beta-ureidopropionase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":32,"reference_id":"29976570","reference_source":"pmid","reference_html":"Crystal structure and pH-dependent allosteric regulation of human β-ureidopropionase, an enzyme involved in anticancer drug metabolism. <i> Maurer D, Lohkamp B, Krumpel M, Widersten M, Dobritzsch D. </i> Biochem J, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"achasapi","curator_name":"Anastasia Chasapi","curator_orcid":"0000-0003-1986-5007","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6FTQ"}],"region_id":"DP03159r001","statement":[{"text":"The lack of electron density for the not modelled N-terminal 32 residues of the native sequence and two loop regions is very likely due to structural disorder.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":202,"end":211,"reference_id":"29976570","reference_source":"pmid","reference_html":"Crystal structure and pH-dependent allosteric regulation of human β-ureidopropionase, an enzyme involved in anticancer drug metabolism. <i> Maurer D, Lohkamp B, Krumpel M, Widersten M, Dobritzsch D. </i> Biochem J, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"achasapi","curator_name":"Anastasia Chasapi","curator_orcid":"0000-0003-1986-5007","term_id":"IDPO:0000030","term_name":"entropic chain","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"6FTQ"}],"region_id":"DP03159r002","statement":[{"text":"As intended, Cys299 does indeed form a disulfide bond in the crystal structure, however, not an intermolecular bond with Cys299 from another subunit, but an intramolecular bond with Cys128 (Figure 4, S8). Both cysteines are located in active- site entrance loops that were found disordered in the “corner subunits” flanking the DmβUP octamer.","type":"Results"},{"text":"Mutation of Thr299 to cysteine, a rather conservative exchange intended to promote formation of an intersubunit disulfide bridge, renders the enzyme incapable of forming higher oligomers.","type":"Discussion"},{"text":"Our results show that this is synonymous with enzyme inactivation, which is in agreement with our hypothesis that ordering of flexible loops at the active site entrance, triggered by substrate binding, inserts Glu207 into the active site and induces oligomerization, which in turn stabilizes the catalytically active conformation of the interacting subunits by burying these loops between them.","type":"Discussion"}],"ec_go":"IMP","disprot_namespace":"Disorder function"},{"start":301,"end":309,"reference_id":"29976570","reference_source":"pmid","reference_html":"Crystal structure and pH-dependent allosteric regulation of human β-ureidopropionase, an enzyme involved in anticancer drug metabolism. <i> Maurer D, Lohkamp B, Krumpel M, Widersten M, Dobritzsch D. </i> Biochem J, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"achasapi","curator_name":"Anastasia Chasapi","curator_orcid":"0000-0003-1986-5007","term_id":"IDPO:0000030","term_name":"entropic chain","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"6FTQ"}],"region_id":"DP03159r003","statement":[{"text":"As intended, Cys299 does indeed form a disulfide bond in the crystal structure, however, not an intermolecular bond with Cys299 from another subunit, but an intramolecular bond with Cys128 (Figure 4, S8). Both cysteines are located in active- site entrance loops that were found disordered in the “corner subunits” flanking the DmβUP octamer.","type":"Results"},{"text":"Mutation of Thr299 to cysteine, a rather conservative exchange intended to promote formation of an intersubunit disulfide bridge, renders the enzyme incapable of forming higher oligomers.","type":"Discussion"},{"text":"Our results show that this is synonymous with enzyme inactivation, which is in agreement with our hypothesis that ordering of flexible loops at the active site entrance, triggered by substrate binding, inserts Glu207 into the active site and induces oligomerization, which in turn stabilizes the catalytically active conformation of the interacting subunits by burying these loops between them.","type":"Discussion"}],"ec_go":"IMP","disprot_namespace":"Disorder function"}],"regions_counter":3,"released":"2021_12","sequence":"MAGAEWKSLEECLEKHLPLPDLQEVKRVLYGKELRKLDLPREAFEAASREDFELQGYAFEAAEEQLRRPRIVHVGLVQNRIPLPANAPVAEQVSALHRRIKAIVEVAAMCGVNIICFQEAWTMPFAFCTREKLPWTEFAESAEDGPTTRFCQKLAKNHDMVVVSPILERDSEHGDVLWNTAVVISNSGAVLGKTRKNHIPRVGDFNESTYYMEGNLGHPVFQTQFGRIAVNICYGRHHPLNWLMYSINGAEIIFNPSATIGALSESLWPIEARNAAIANHCFTCAINRVGTEHFPNEFTSGDGKKAHQDFGYFYGSSYVAAPDSSRTPGLSRSRDGLLVAKLDLNLCQQVNDVWNFKMTGRYEMYARELAEAVKSNYSPTIVKE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI0000126B4C","uniref100":"UniRef100_Q9UBR1","uniref90":"UniRef90_Q9UBR1","uniref50":"UniRef50_Q9UBR1","genes":[{"name":{"value":"UPB1"},"synonyms":[{"value":"BUP1"}]}],"alphafold_very_low_content":0.0026041666666666665,"disorder_content":0.08333333333333333,"disprot_consensus":{"full":[{"start":1,"end":32,"type":"D"},{"start":202,"end":211,"type":"F"},{"start":301,"end":309,"type":"F"}],"Structural state":[{"start":1,"end":32,"type":"D"}],"Disorder function":[{"start":202,"end":211,"type":"F"},{"start":301,"end":309,"type":"F"}]}},{"disprot_id":"DP03160","acc":"S7W634","creator":"gerdos","date":"2021-01-13T20:47:03.824Z","features":{"pfam":[{"id":"PF00063","name":"Myosin head (motor domain)","start":103,"end":761}],"gene3D":[]},"length":831,"name":"Myosin A","ncbi_taxon_id":507601,"organism":"Toxoplasma gondii (strain ATCC 50853 / GT1)","regions":[{"start":1,"end":32,"reference_id":"30348763","reference_source":"pmid","reference_html":"Structural and mechanistic insights into the function of the unconventional class XIV myosin MyoA from <i>Toxoplasma gondii</i>. <i> Powell CJ, Ramaswamy R, Kelsen A, Hamelin DJ, Warshaw DM, Bosch J, Burke JE, Ward GE, Boulanger MJ. </i> Proc Natl Acad Sci U S A, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6DUE"}],"region_id":"DP03160r001","statement":[{"text":"The sequence-divergent\nN terminus (M1–N111) comprises a disordered N-terminal extension (M1–V32) and a more domain-like region (Y33–L95).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-14T09:53:24.092Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MASKTTSEELKTATALKKRSSDVHAVDHSGNVYKGFQIWTDLAPSVKEEPDLMFAKCIVQAGTDKGNLTCVQIDPPGFDEPFEVPQANAWNVNSLIDPMTYGDIGMLPHTNIPCVLDFLKVRFMKNQIYTTADPLVVAINPFRDLGNTTLDWIVRYRDTFDLSKLAPHVFYTARRALDNLHAVNKSQTIIVSGESGAGKTEATKQIMRYFAAAKTGSMDLRIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVGREGGIKFGSVVAFLLEKSRVLTQDEQERSYHIFYQMCKGADAAMKERFHILPLSEYKYINPLCLDAPGIDDVAEFHEVCESFRSMNLTEDEVASVWSIVSGVLLLGNVEVTATKDGGIDDAAAIEGKNLEVFKKACGLLFLDAERIREELTVKVSYAGNQEIRGRWKQEDGDMLKSSLAKAMYDKLFMWIIAVLNRSIKPPGGFKIFMGMLDIFGFEVFKNNSLEQFFINITNEMLQKNFVDIVFDRESKLYRDEGVSSKELIFTSNAEVIKILTAKNNSVLAALEDQCLAPGGSDEKFLSTCKNALKGTTKFKPAKVSPNINFLISHTVGDIQYNAEGFLFKNKDVLRAEIMEIVQQSKNPVVAQLFAGIVMEKGKMAKGQLIGSQFLSQLQSLMELINSTEPHFIRCIKPNDTKKPLDWVPSKMLIQLHALSVLEALQLRQLGYSYRRPFKEFLFQFKFIDLSASENPNLDPKEAALRLLKSSKLPSEEYQLGKTMVFLKQTGAKELTQIQRECLSSWEPLVSVLEAYYAGRRHKKQLLKKTPFIIRAQAHIRRHLVDNNVSPATVQPAF","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Conoidasida","Coccidia","Eucoccidiorida","Eimeriorina","Sarcocystidae","Toxoplasma"],"dataset":[],"UniParc":"UPI0000083536","uniref100":"UniRef100_O00934","uniref90":"UniRef90_O00934","uniref50":"UniRef50_Q8IDR3","genes":[{"orfNames":[{"value":"TGGT1_235470","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EPR60343.1","url":"https://www.ebi.ac.uk/ena/browser/view/EPR60343.1"}}]}]}],"alphafold_very_low_content":0.010830324909747292,"disorder_content":0.03850782190132371,"disprot_consensus":{"full":[{"start":1,"end":32,"type":"D"}],"Structural state":[{"start":1,"end":32,"type":"D"}]}},{"disprot_id":"DP03161","acc":"Q8WVQ1","creator":"achasapi","date":"2021-01-13T21:22:20.780Z","features":{"pfam":[{"id":"PF06079","name":"Apyrase","start":113,"end":401}],"gene3D":[]},"length":401,"name":"Soluble calcium-activated nucleotidase 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":71,"end":84,"reference_id":"15006348","reference_source":"pmid","reference_html":"Structure and protein design of a human platelet function inhibitor. <i> Dai J, Liu J, Deng Y, Smith TM, Lu M. </i> Cell, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"achasapi","curator_name":"Anastasia Chasapi","curator_orcid":"0000-0003-1986-5007","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03161r001","statement":[{"text":"Iterative rounds of model building with O, refinement with Refmac (Murshudov et al., 1997), and addition of ordered solvent clarified the trace except the N-terminal region, which is not visible in the electron density maps and therefore must be disordered. ","type":"Methods"}],"cross_refs":[{"db":"PDB","id":"1S18"},{"db":"PDB","id":"1S1D"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-15T18:22:31.263Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLCSHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQEENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSVDDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDVVNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPRRASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVALKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins"],"UniParc":"UPI00000734F8","uniref100":"UniRef100_Q8WVQ1","uniref90":"UniRef90_Q8WVQ1","uniref50":"UniRef50_Q8WVQ1","genes":[{"name":{"value":"CANT1"},"synonyms":[{"value":"SHAPY"}]}],"alphafold_very_low_content":0.08977556109725686,"disorder_content":0.034912718204488775,"disprot_consensus":{"full":[{"start":71,"end":84,"type":"D"}],"Structural state":[{"start":71,"end":84,"type":"D"}]}},{"disprot_id":"DP03162","acc":"O00299","creator":"tszani","date":"2021-01-15T11:20:12.247Z","features":{"pfam":[{"id":"PF13410","name":"Glutathione S-transferase, C-terminal domain","start":126,"end":210},{"id":"PF22441","name":"CLIC-like N-terminal domain","start":6,"end":91}],"gene3D":[]},"length":241,"name":"Chloride intracellular channel protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":152,"end":162,"reference_id":"11551966","reference_source":"pmid","reference_html":"Crystal structure of a soluble form of the intracellular chloride ion channel CLIC1 (NCC27) at 1.4-A resolution. <i> Harrop SJ, DeMaere MZ, Fairlie WD, Reztsova T, Valenzuela SM, Mazzanti M, Tonini R, Qiu MR, Jankova L, Warton K, Bauskin AR, Wu WM, Pankhurst S, Campbell TJ, Breit SN, Curmi PM. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1K0O"}],"region_id":"DP03162r001","statement":[{"text":"In  the  1.4Å structure,  clear electron density was seen for all residues from Pro6to Lys241,while  in  the  second  form,  residues  Leu148–Arg165 are  disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-02-17T16:42:28.373Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":147,"end":164,"reference_id":"11551966","reference_source":"pmid","reference_html":"Crystal structure of a soluble form of the intracellular chloride ion channel CLIC1 (NCC27) at 1.4-A resolution. <i> Harrop SJ, DeMaere MZ, Fairlie WD, Reztsova T, Valenzuela SM, Mazzanti M, Tonini R, Qiu MR, Jankova L, Warton K, Bauskin AR, Wu WM, Pankhurst S, Campbell TJ, Breit SN, Curmi PM. </i> J Biol Chem, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"1K0O"}],"region_id":"DP03162r002","statement":[{"text":"The long loop between helices h5 and h6 at the foot of CLIC1(Pro147–Gln164) is a distinctive feature of the CLICs. It is highlynegatively charged with seven acidic residues between Pro149and  Glu160in  CLIC1  giving  a  net  charge  of\u00037(cf.a  netnegative  charge  of  6  in  CLIC4  and  p64,  5  in  CLIC2,  5  inparchorin, and 3 in CLIC3). This loop is spatially adjacent tothe loop linking the two domains, and it may be important inprotein-protein interactions.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":1,"end":21,"reference_id":"14613939","reference_source":"pmid","reference_html":"The intracellular chloride ion channel protein CLIC1 undergoes a redox-controlled structural transition. <i> Littler DR, Harrop SJ, Fairlie WD, Brown LJ, Pankhurst GJ, Pankhurst S, DeMaere MZ, Campbell TJ, Bauskin AR, Tonini R, Mazzanti M, Breit SN, Curmi PM. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1RK4"}],"region_id":"DP03162r003","statement":[{"text":"In the dimer there is no electron density for the first 22 residues (β-strand 1 in monomer), and helix 2 is extended by an extra 2turns   to   include   residues   starting   at   Thr-44   (originally β-strand 2; Fig. 2E).\n","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-02-17T16:34:05.159Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2021_12","sequence":"MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKIEEFLEAVLCPPRYPKLAALNPESNTAGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDEGVSQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVAKALK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI00001698DA","uniref100":"UniRef100_O00299","uniref90":"UniRef90_O00299","uniref50":"UniRef50_O00299","genes":[{"name":{"value":"CLIC1"},"synonyms":[{"value":"G6"},{"value":"NCC27"}]}],"alphafold_very_low_content":0.004149377593360996,"disorder_content":0.13278008298755187,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"},{"start":147,"end":151,"type":"F"},{"start":152,"end":162,"type":"D"},{"start":163,"end":164,"type":"F"}],"Structural state":[{"start":1,"end":21,"type":"D"},{"start":152,"end":162,"type":"D"}],"Disorder function":[{"start":147,"end":164,"type":"F"}]}},{"disprot_id":"DP03163","acc":"O15247","creator":"tszani","date":"2021-01-15T11:25:10.083Z","features":{"pfam":[{"id":"PF13410","name":"Glutathione S-transferase, C-terminal domain","start":169,"end":216},{"id":"PF22441","name":"CLIC-like N-terminal domain","start":12,"end":97}],"gene3D":[]},"length":247,"name":"Chloride intracellular channel protein 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":55,"end":68,"reference_id":"18186468","reference_source":"pmid","reference_html":"The crystal structure of human chloride intracellular channel protein 2: a disulfide bond with functional implications. <i> Mi W, Liang YH, Li L, Su XD. </i> Proteins, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2PER"}],"region_id":"DP03163r001","statement":[{"text":" The electron density of residues 55–69 could not be observed at the contour level of 1.0 sigma due to the flexibility of this region.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-02-16T16:56:52.213Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MSGLRPGTQVDPEIELFVKAGSDGESIGNCPFCQRLFMILWLKGVKFNVTTVDMTRKPEELKDLAPGTNPPFLVYNKELKTDFIKIEEFLEQTLAPPRYPHLSPKYKESFDVGCNLFAKFSAYIKNTQKEANKNFEKSLLKEFKRLDDYLNTPLLDEIDPDSAEEPPVSRRLFLDGDQLTLADCSLLPKLNIIKVAAKKYRDFDIPAEFSGVWRYLHNAYAREEFTHTCPEDKEIENTYANVAKQKS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000015C44D","uniref100":"UniRef100_O15247","uniref90":"UniRef90_O15247","uniref50":"UniRef50_O15247","genes":[{"name":{"value":"CLIC2"}}],"alphafold_very_low_content":0.02834008097165992,"disorder_content":0.05668016194331984,"disprot_consensus":{"full":[{"start":55,"end":68,"type":"D"}],"Structural state":[{"start":55,"end":68,"type":"D"}]}},{"disprot_id":"DP03164","acc":"Q9Y696","creator":"tszani","date":"2021-01-15T11:38:33.787Z","features":{"pfam":[{"id":"PF22441","name":"CLIC-like N-terminal domain","start":17,"end":102}],"gene3D":[]},"length":253,"name":"Chloride intracellular channel protein 4","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":159,"end":175,"reference_id":"16176272","reference_source":"pmid","reference_html":"Crystal structure of the soluble form of the redox-regulated chloride ion channel protein CLIC4. <i> Littler DR, Assaad NN, Harrop SJ, Brown LJ, Pankhurst GJ, Luciani P, Aguilar MI, Mazzanti M, Berryman MA, Breit SN, Curmi PM. </i> FEBS J, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"2AHE"}],"region_id":"DP03164r001","statement":[{"text":"The observed structure consists of residues 16–163 and 173–257 with the break in density corresponding to the flexible foot loop between helix 5 and helix 6 (Fig. 1A, bottom left), which is not ordered in the CLIC4(ext) structure. ","type":"Results"},{"text":"The backbone structures overlay well except for the region around helix 2 (including connecting loops, Leu59 to His74) and the flexible foot loop (Leu159 to Thr175).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":160,"end":173,"reference_id":"16176272","reference_source":"pmid","reference_html":"Crystal structure of the soluble form of the redox-regulated chloride ion channel protein CLIC4. <i> Littler DR, Assaad NN, Harrop SJ, Brown LJ, Pankhurst GJ, Luciani P, Aguilar MI, Mazzanti M, Berryman MA, Breit SN, Curmi PM. </i> FEBS J, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"tszani","curator_name":"Tamás Szaniszló","curator_orcid":"0000-0002-3130-9284","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2AHE"}],"region_id":"DP03164r002","statement":[{"text":"The observed structure consists of residues 16–163 and 173–257 with the break in density corresponding to the flexible foot loop between helix 5 and helix 6 (Fig. 1A, bottom left), which is not ordered in the CLIC4(ext) structure. ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-02-17T16:14:59.771Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MALSMPLNGLKEEDKEPLIELFVKAGSDGESIGNCPFSQRLFMILWLKGVVFSVTTVDLKRKPADLQNLAPGTHPPFITFNSEVKTDVNKIEEFLEEVLCPPKYLKLSPKHPESNTAGMDIFAKFSAYIKNSRPEANEALERGLLKTLQKLDEYLNSPLPDEIDENSMEDIKFSTRKFLDGNEMTLADCNLLPKLHIVKVVAKKYRNFDIPKEMTGIWRYLTNAYSRDEFTNTCPSDKEVEIAYSDVAKRLTK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI00006A7837","uniref100":"UniRef100_Q9Y696","uniref90":"UniRef90_Q9Y696","uniref50":"UniRef50_Q9Y696","genes":[{"name":{"value":"CLIC4"}}],"alphafold_very_low_content":0.039525691699604744,"disorder_content":0.05533596837944664,"disprot_consensus":{"full":[{"start":159,"end":159,"type":"F"},{"start":160,"end":173,"type":"D"},{"start":174,"end":175,"type":"F"}],"Structural state":[{"start":160,"end":173,"type":"D"}],"Disorder function":[{"start":159,"end":175,"type":"F"}]}},{"disprot_id":"DP03166","acc":"P00519","creator":"npalopoli","date":"2021-01-16T04:26:09.624Z","features":{"pfam":[{"id":"PF00017","name":"SH2 domain","start":127,"end":202},{"id":"PF00018","name":"SH3 domain","start":67,"end":113},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":242,"end":492},{"id":"PF08919","name":"F-actin binding","start":1026,"end":1130}],"gene3D":[]},"length":1130,"name":"Tyrosine-protein kinase ABL1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":385,"end":401,"reference_id":"17164530","reference_source":"pmid","reference_html":"Structural biology contributions to the discovery of drugs to treat chronic myelogenous leukaemia. <i> Cowan-Jacob SW, Fendrich G, Floersheimer A, Furet P, Liebetanz J, Rummel G, Rheinberger P, Centeleghe M, Fabbro D, Manley PW. </i> Acta Crystallogr D Biol Crystallogr, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"npalopoli","curator_name":"Nicolás Palopoli","curator_orcid":"0000-0001-7925-6436","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2HZ0"}],"region_id":"DP03166r001","statement":[{"text":"The main differences occur in loop regions where the temperature factors are high (e.g. the β3-αC loop and the A-loop)","type":"Results"},{"text":"There are two molecules in the asymmetric unit of the crystals and one of these shows a novel A-loop conformation, while the A-loop is not visible in the other owing to disorder.","type":"Results"},{"text":"Superposition of the various structures reported here and one recently reported structure (Levinson et al., 2006; PDB code 2g1t) shows that there are four main regions of conformational flexibility in the Abl kinase domain: the A-loop, the P-loop, the C-helix and the relative position of the N-terminal lobe with respect to the C-terminal lobe","type":"Results"},{"text":"A-loop comprises residues 381-401 but region is defined on the basis of missing residues 385-401 in 2HZ0_B.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:41:02.301Z"}},{"start":385,"end":401,"reference_id":"17164530","reference_source":"pmid","reference_html":"Structural biology contributions to the discovery of drugs to treat chronic myelogenous leukaemia. <i> Cowan-Jacob SW, Fendrich G, Floersheimer A, Furet P, Liebetanz J, Rummel G, Rheinberger P, Centeleghe M, Fabbro D, Manley PW. </i> Acta Crystallogr D Biol Crystallogr, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"npalopoli","curator_name":"Nicolás Palopoli","curator_orcid":"0000-0001-7925-6436","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2HZ0"}],"region_id":"DP03166r002","statement":[{"text":"There are two molecules in the asymmetric unit of the crystals and one of these shows a novel A-loop conformation, while the A-loop is not visible in the other owing to disorder. The novel\nA-loop conformation lies in an intermediate position between the active conformation and the imatinib-bound conformation. The path of this segment departs from the latter conformation at Leu383, superimposes again at Lys400, has Tyr393 exposed at the surface and shows some weak resemblance to the intermediate conformation observed in partially phosphorylated Igf1r kinase (Pautsch et al., 2001). However, this conformation is stabilized by crystal contacts in the Abl structure, so it is not clear if this is really a natural inactive state of the A-loop of Abl kinase.","type":"Results"},{"text":"A-loop comprises residues 381-401 but region is defined on the basis of missing residues 385-401 in 2HZ0_B","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-07T09:41:04.428Z"}}],"regions_counter":2,"released":"2021_12","sequence":"MLEICLKLVGCKSKKGLSSSSSCYLEEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESDPLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRDISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKDIMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKHSSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVLPATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins","Condensates-related proteins","NDDs-related proteins"],"UniParc":"UPI0000072191","uniref100":"UniRef100_P00519","uniref90":"UniRef90_P00519","uniref50":"UniRef50_P00519","genes":[{"name":{"value":"ABL1"},"synonyms":[{"value":"ABL"},{"value":"JTK7"}]}],"alphafold_very_low_content":0.4982300884955752,"disorder_content":0.01504424778761062,"disprot_consensus":{"full":[{"start":385,"end":401,"type":"T"}],"Structural state":[{"start":385,"end":401,"type":"D"}],"Structural transition":[{"start":385,"end":401,"type":"T"}]}},{"disprot_id":"DP03168","acc":"P00519-2","creator":"npalopoli","date":"2021-01-16T05:38:25.094Z","features":{"pfam":[],"gene3D":[]},"length":1149,"name":"Isoform IB of Tyrosine-protein kinase ABL1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1026,"end":1045,"reference_id":"16109371","reference_source":"pmid","reference_html":"Structural basis for the cytoskeletal association of Bcr-Abl/c-Abl. <i> Hantschel O, Wiesner S, Güttler T, Mackereth CD, Rix LL, Mikes Z, Dehne J, Görlich D, Sattler M, Superti-Furga G. </i> Mol Cell, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"npalopoli","curator_name":"Nicolás Palopoli","curator_orcid":"0000-0001-7925-6436","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":4,"region_id":"DP03168r001","statement":[{"text":"We determined the three-dimensional (3D) solution structure of the FABD (corresponding to residues 1026–1149 of human c-Abl spliceform 1b) by heteronuclear NMR spectroscopy (Figures 1B and 1C and Table 1). This domain also includes the previously proposed NES (residues 1109–1118) (Taagepera et al., 1998). The ordered region of the FABD, which encompasses residues 1047–1149, is a monomer in solution","type":"Results"},{"text":"15N relaxation data shows that the αIII-αIV loop displays high internal mobility and that the 20 N-terminal residues of the expression construct are unstructured","type":"Results"},{"text":"{1H}-15N heteronuclear NOE, longitudinal and transverse 15N relaxation data of the Bcr-Abl/c-Abl FABD demonstrate significant conformational flexibility for the N-terminal region and the loop between helices αIII and αIV","type":"Supplementary material"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":520,"end":531,"reference_id":"21338916","reference_source":"pmid","reference_html":"Discovery and characterization of a cell-permeable, small-molecule c-Abl kinase activator that binds to the myristoyl binding site. <i> Yang J, Campobasso N, Biju MP, Fisher K, Pan XQ, Cottom J, Galbraith S, Ho T, Zhang H, Hong X, Ward P, Hofmann G, Siegfried B, Zappacosta F, Washio Y, Cao P, Qu J, Bertrand S, Wang DY, Head MS, Li H, Moores S, Lai Z, Johanson K, Burton G, Erickson-Miller C, Simpson G, Tummino P, Copeland RA, Oliff A. </i> Chem Biol, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"npalopoli","curator_name":"Nicolás Palopoli","curator_orcid":"0000-0001-7925-6436","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03168r002","statement":[{"text":"R-DPH binds to c-Abl in the myristoyl binding site and straightens the αI’ helix to elongate the αI helix (Figure 5A). In chain A, the αI helix extends to residue 519 and in Chain B, the αI helix extends to residue 529. The remaining C-terminal residues of the respective molecules in the asymmetric unit are disordered. In contrast, the autoinhibited c-Abl has αI helix ending at residue 515, with a loop between residues 515–521 and with αI’ helix defined by residues 521–529 (Figure 1). The elongated αI helix of Chain B with R-DPH shows significant crystal packing and is an artifact of crystallization. However, the C terminus of Chain A with R-DPH shows no crystal packing and will be the focus of subsequent discussion.","type":"Results"},{"text":"Residues 520-531 in PDB 3PYY chain A correspond to region 501-512 in the UniProt amino acid sequence of canonical isoform 1A of P00519..","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":138,"end":249,"reference_id":"25779001","reference_source":"pmid","reference_html":"Crystal structure of an SH2-kinase construct of c-Abl and effect of the SH2 domain on kinase activity. <i> Lorenz S, Deng P, Hantschel O, Superti-Furga G, Kuriyan J. </i> Biochem J, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"npalopoli","curator_name":"Nicolás Palopoli","curator_orcid":"0000-0001-7925-6436","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03168r003","statement":[{"text":"The crystal form has two copies of the KD in the asymmetric unit, however only one SH2 domain could be localized in the electron density map, presumably due to a high degree of disorder in the second SH2 domain. Since the conformation of both KDs is very similar, we focus our interpretation on the molecule for which the SH2 domain could be built. The structure shows the SH2 and KD in an extended conformation (Figure 4A), as was observed previously for the SH3–SH2–KD construct bound to PD166326 (PDB ID: 1OPL) [2]. The previous crystal form, however contained two different conformational states of the SH3–SH2–KD construct, (i) the compact auto-inhibited conformation, in which the SH2 domain docks on to the C-lobe of the KD and (ii) the extended conformation, for which only the SH2 and KDs could be modelled and which was characterized by very high temperature factors.","type":"Results"},{"text":"Missing electron density correspond to crystallography experiment for PDB 4XEY chain B.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2021_12","sequence":"MGQQPGKVLGDQRRPSLPALHFIKGAGKKESSRHGGPHCNVFVEHEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYLLSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVHHHSTVADGLITTLHYPAPKRNKPTVYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKQGVRGAVSTLLQAPELPTKTRTSRRAAEHRDTTDVPEMPHSKGQGESDPLDHEPAVSPLLPRKERGPPEGGLNEDERLLPKDKKTNLFSALIKKKKKTAPTPPKRSSSFREMDGQPERRGAGEEEGRDISNGALAFTPLDTADPAKSPKPSNGAGVPNGALRESGGSGFRSPHLWKKSSTLTSSRLATGEEEGGGSSSKRFLRSCSASCVPHGAKDTEWRSVTLPRDLQSTGRQFDSSTFGGHKSEKPALPRKRAGENRSDQVTRGTVTPPPRLVKKNEEAADEVFKDIMESSPGSSPPNLTPKPLRRQVTVAPASGLPHKEEAGKGSALGTPAAAEPVTPTSKAGSGAPGGTSKGPAEESRVRRHKHSSESPGRDKGKLSRLKPAPPPPPAASAGKAGGKPSQSPSQEAAGEAVLGAKTKATSLVDAVNSDAAKPSQPGEGLKKPVLPATPKPQSAKPSGTPISPAPVPSTLPSASSALAGDQPSSTAFIPLISTRVSLRKTRQPPERIASGAITKGVVLDSTEALCLAISRNSEQMASHSAVLEAGKNLYTFCVSYVDSIQQMRNKFAFREAINKLENNLRELQICPATAGSGPAATQDFSKLLSSVKEISDIVQR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000013E4DE","uniref100":"","uniref90":"","uniref50":"","genes":[{"name":{"value":"ABL1"},"synonyms":[{"value":"ABL"},{"value":"JTK7"}]}],"disorder_content":0.12532637075718014,"disprot_consensus":{"full":[{"start":138,"end":249,"type":"D"},{"start":520,"end":531,"type":"D"},{"start":1026,"end":1045,"type":"D"}],"Structural state":[{"start":138,"end":249,"type":"D"},{"start":520,"end":531,"type":"D"},{"start":1026,"end":1045,"type":"D"}]}},{"disprot_id":"DP03169","acc":"Q9NQC7","creator":"emaiani","date":"2021-01-16T13:52:09.275Z","features":{"pfam":[{"id":"PF00443","name":"Ubiquitin carboxyl-terminal hydrolase","start":593,"end":889},{"id":"PF01302","name":"CAP-Gly domain","start":138,"end":201},{"id":"PF01302","name":"CAP-Gly domain","start":478,"end":538},{"id":"PF16607","name":"Phosphorylation region of CYLD, unstructured","start":308,"end":471},{"id":"PF28930","name":"CYLD SH3 domain","start":19,"end":122}],"gene3D":[]},"length":956,"name":"Ubiquitin carboxyl-terminal hydrolase CYLD","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":841,"end":857,"reference_id":"18313383","reference_source":"pmid","reference_html":"The structure of the CYLD USP domain explains its specificity for Lys63-linked polyubiquitin and reveals a B box module. <i> Komander D, Lord CJ, Scheel H, Swift S, Hofmann K, Ashworth A, Barford D. </i> Mol Cell, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"emaiani","curator_name":"Emiliano Maiani","curator_orcid":"0000-0003-1432-5394","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2VHF"}],"region_id":"DP03169r001","statement":[{"text":"In molecule A, the surface loops 671–678, 723–723, 841–857, and 893–899 are disordered, while, in molecule B, residues 672–679, 719–727, 759–766, 894–901, 929–934, and 956 lacked electron density.","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T12:24:56.560Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MSSGLWSQEKVTSPYWEERIFYLLLQECSVTDKQTQKLLKVPKGSIGQYIQDRSVGHSRIPSAKGKKNQIGLKILEQPHAVLFVDEKDVVEINEKFTELLLAITNCEERFSLFKNRNRLSKGLQIDVGCPVKVQLRSGEEKFPGVVRFRGPLLAERTVSGIFFGVELLEEGRGQGFTDGVYQGKQLFQCDEDCGVFVALDKLELIEDDDTALESDYAGPGDTMQVELPPLEINSRVSLKVGETIESGTVIFCDVLPGKESLGYFVGVDMDNPIGNWDGRFDGVQLCSFACVESTILLHINDIIPALSESVTQERRPPKLAFMSRGVGDKGSSSHNKPKATGSTSDPGNRNRSELFYTLNGSSVDSQPQSKSKNTWYIDEVAEDPAKSLTEISTDFDRSSPPLQPPPVNSLTTENRFHSLPFSLTKMPNTNGSIGHSPLSLSAQSVMEELNTAPVQESPPLAMPPGNSHGLEVGSLAEVKENPPFYGVIRWIGQPPGLNEVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNSLAFGGYLSEVVEENTPPKMEKEGLEIMIGKKKGIQGHYNSCYLDSTLFCLFAFSSVLDTVLLRPKEKNDVEYYSETQELLRTEIVNPLRIYGYVCATKIMKLRKILEKVEAASGFTSEEKDPEEFLNILFHHILRVEPLLKIRSAGQKVQDCYFYQIFMEKNEKVGVPTIQQLLEWSFINSNLKFAEAPSCLIIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYECRECYDDPDISAGKIKQFCKTCNTQVHLHPKRLNHKYNPVSLPKDLPDWDWRHGCIPCQNMELFAVLCIETSHYVAFVKYGKDDSAWLFFDSMADRDGGQNGFNIPQVTPCPEVGEYLKMSLEDLHSLDSRRIQGCARRLLCDAYMCMYQSPTMSLYK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins"],"UniParc":"UPI0000073A15","uniref100":"UniRef100_Q9NQC7","uniref90":"UniRef90_Q9NQC7","uniref50":"UniRef50_Q9NQC7","genes":[{"name":{"value":"CYLD","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12917689","url":"http://www.ncbi.nlm.nih.gov/pubmed/12917689","alternativeUrl":"https://europepmc.org/abstract/MED/12917689"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:2584","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:2584"}}]},"synonyms":[{"value":"CYLD1"},{"value":"KIAA0849","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10048485","url":"http://www.ncbi.nlm.nih.gov/pubmed/10048485","alternativeUrl":"https://europepmc.org/abstract/MED/10048485"}}]}],"orfNames":[{"value":"HSPC057"}]}],"alphafold_very_low_content":0.2395397489539749,"disorder_content":0.01778242677824268,"disprot_consensus":{"full":[{"start":841,"end":857,"type":"D"}],"Structural state":[{"start":841,"end":857,"type":"D"}]}},{"disprot_id":"DP03170","acc":"Q8NBZ7","creator":"emaiani","date":"2021-01-16T14:15:32.461Z","features":{"pfam":[{"id":"PF11803","name":"UDP-glucuronate decarboxylase N-terminal","start":5,"end":78},{"id":"PF16363","name":"GDP-mannose 4,6 dehydratase","start":92,"end":386}],"gene3D":[]},"length":420,"name":"UDP-glucuronic acid decarboxylase 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":395,"end":420,"reference_id":"23072385","reference_source":"pmid","reference_html":"Human UDP-α-D-xylose synthase and Escherichia coli ArnA conserve a conformational shunt that controls whether xylose or 4-keto-xylose is produced. <i> Polizzi SJ, Walsh RM, Peeples WB, Lim JM, Wells L, Wood ZA. </i> Biochemistry, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"emaiani","curator_name":"Emiliano Maiani","curator_orcid":"0000-0003-1432-5394","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4GLL"}],"region_id":"DP03170r001","statement":[{"text":"The extreme N-terminus of both chains is disordered (residues\n85–87), as is the C-terminus of chain A (395–420) and chain B (399–420).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T09:12:05.627Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MVSKALLRLVSAVNRRRMKLLLGIALLAYVASVWGNFVNMRSIQENGELKIESKIEEMVEPLREKIRDLEKSFTQKYPPVKFLSEKDRKRILITGGAGFVGSHLTDKLMMDGHEVTVVDNFFTGRKRNVEHWIGHENFELINHDVVEPLYIEVDQIYHLASPASPPNYMYNPIKTLKTNTIGTLNMLGLAKRVGARLLLASTSEVYGDPEVHPQSEDYWGHVNPIGPRACYDEGKRVAETMCYAYMKQEGVEVRVARIFNTFGPRMHMNDGRVVSNFILQALQGEPLTVYGSGSQTRAFQYVSDLVNGLVALMNSNVSSPVNLGNPEEHTILEFAQLIKNLVGSGSEIQFLSEAQDDPQKRKPDIKKAKLMLGWEPVVPLEEGLNKAIHYFRKELEYQANNQYIPKPKPARIKKGRTRHS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI0000047828","uniref100":"UniRef100_Q8NBZ7","uniref90":"UniRef90_Q8NBZ7","uniref50":"UniRef50_Q8NBZ7","genes":[{"name":{"value":"UXS1"},"orfNames":[{"value":"UNQ2538/PRO6079"}]}],"alphafold_very_low_content":0.04047619047619048,"disorder_content":0.06190476190476191,"disprot_consensus":{"full":[{"start":395,"end":420,"type":"D"}],"Structural state":[{"start":395,"end":420,"type":"D"}]}},{"disprot_id":"DP03171","acc":"Q16831","creator":"emaiani","date":"2021-01-16T14:50:57.873Z","features":{"pfam":[{"id":"PF01048","name":"Phosphorylase superfamily","start":54,"end":304}],"gene3D":[]},"length":310,"name":"Uridine phosphorylase 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":15,"reference_id":"19291308","reference_source":"pmid","reference_html":"Implications of the structure of human uridine phosphorylase 1 on the development of novel inhibitors for improving the therapeutic window of fluoropyrimidine chemotherapy. <i> Roosild TP, Castronovo S, Fabbiani M, Pizzorno G. </i> BMC Struct Biol, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"emaiani","curator_name":"Emiliano Maiani","curator_orcid":"0000-0003-1432-5394","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3EUE"},{"db":"PDB","id":"3EUF"}],"region_id":"DP03171r001","statement":[{"text":"Due to a lack of electron-density, the first 15 residues of hUPP1 and the N-terminal cloning artifact residues 'MRGSHHHHHHGSPGLQEF' were not built.","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T09:06:39.504Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MAATGANAEKAESHNDCPVRLLNPNIAKMKEDILYHFNLTTSRHNFPALFGDVKFVCVGGSPSRMKAFIRCVGAELGLDCPGRDYPNICAGTDRYAMYKVGPVLSVSHGMGIPSISIMLHELIKLLYYARCSNVTIIRIGTSGGIGLEPGTVVITEQAVDTCFKAEFEQIVLGKRVIRKTDLNKKLVQELLLCSAELSEFTTVVGNTMCTLDFYEGQGRLDGALCSYTEKDKQAYLEAAYAAGVRNIEMESSVFAAMCSACGLQAAVVCVTLLNRLEGDQISSPRNVLSEYQQRPQRLVSYFIKKKLSKA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI0000137AC5","uniref100":"UniRef100_Q16831","uniref90":"UniRef90_Q16831","uniref50":"UniRef50_P52624","genes":[{"name":{"value":"UPP1"},"synonyms":[{"value":"UP"}]}],"alphafold_very_low_content":0.041935483870967745,"disorder_content":0.04838709677419355,"disprot_consensus":{"full":[{"start":1,"end":15,"type":"D"}],"Structural state":[{"start":1,"end":15,"type":"D"}]}},{"disprot_id":"DP03172","acc":"Q9NRN7","creator":"emaiani","date":"2021-01-16T15:25:21.860Z","features":{"pfam":[{"id":"PF01648","name":"4'-phosphopantetheinyl transferase superfamily","start":125,"end":241},{"id":"PF22624","name":"4'-phosphopantetheinyl transferase, N-terminal","start":25,"end":122}],"gene3D":[]},"length":309,"name":"L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":248,"end":263,"reference_id":"18022563","reference_source":"pmid","reference_html":"Mechanism and substrate recognition of human holo ACP synthase. <i> Bunkoczi G, Pasta S, Joshi A, Wu X, Kavanagh KL, Smith S, Oppermann U. </i> Chem Biol, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"emaiani","curator_name":"Emiliano Maiani","curator_orcid":"0000-0003-1432-5394","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2BYD"},{"db":"PDB","id":"2C43"}],"region_id":"DP03172r001","statement":[{"text":"Another feature is the disordered loop between residues 248–263, which starts after the superposition of the PPT C-terminal domain and AcpS ends, suggesting that this may act as a flexible linker.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-28T10:58:11.834Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MVFPAKRFCLVPSMEGVRWAFSCGTWLPSRAEWLLAVRSIQPEEKERIGQFVFARDAKAAMAGRLMIRKLVAEKLNIPWNHIRLQRTAKGKPVLAKDSSNPYPNFNFNISHQGDYAVLAAEPELQVGIDIMKTSFPGRGSIPEFFHIMKRKFTNKEWETIRSFKDEWTQLDMFYRNWALKESFIKAIGVGLGFELQRLEFDLSPLNLDIGQVYKETRLFLDGEEEKEWAFEESKIDEHHFVAVALRKPDGSRHQDVPSQDDSKPTQRQFTILNFNDLMSSAVPMTPEDPSFWDCFCFTEEIPIRNGTKS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000006D980","uniref100":"UniRef100_Q9NRN7","uniref90":"UniRef90_Q9NRN7","uniref50":"UniRef50_Q9NRN7","genes":[{"name":{"value":"AASDHPPT"},"orfNames":[{"value":"CGI-80"},{"value":"HAH-P"},{"value":"HSPC223"},{"value":"x0005"}]}],"alphafold_very_low_content":0.0744336569579288,"disorder_content":0.05177993527508091,"disprot_consensus":{"full":[{"start":248,"end":263,"type":"D"}],"Structural state":[{"start":248,"end":263,"type":"D"}]}},{"disprot_id":"DP03173","acc":"O14727","creator":"emaiani","date":"2021-01-16T15:49:33.832Z","features":{"pfam":[{"id":"PF00400","name":"WD domain, G-beta repeat","start":875,"end":909},{"id":"PF00400","name":"WD domain, G-beta repeat","start":1001,"end":1031},{"id":"PF00400","name":"WD domain, G-beta repeat","start":1040,"end":1071},{"id":"PF00400","name":"WD domain, G-beta repeat","start":1079,"end":1113},{"id":"PF00400","name":"WD domain, G-beta repeat","start":1119,"end":1155},{"id":"PF00400","name":"WD domain, G-beta repeat","start":1176,"end":1203},{"id":"PF00619","name":"Caspase recruitment domain","start":6,"end":89},{"id":"PF00931","name":"NB-ARC domain","start":130,"end":304},{"id":"PF17908","name":"APAF-1 helical domain","start":453,"end":587},{"id":"PF21296","name":"Apoptotic protease-activating factor 1-like, winged-helix domain","start":378,"end":445},{"id":"PF23381","name":"IFT122 first beta-propeller","start":618,"end":781}],"gene3D":[]},"length":1248,"name":"Apoptotic protease-activating factor 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":100,"reference_id":"26543158","reference_source":"pmid","reference_html":"Atomic structure of the apoptosome: mechanism of cytochrome c- and dATP-mediated activation of Apaf-1. <i> Zhou M, Li Y, Hu Q, Bai XC, Huang W, Yan C, Scheres SH, Shi Y. </i> Genes Dev, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"emaiani","curator_name":"Emiliano Maiani","curator_orcid":"0000-0003-1432-5394","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3JBT"},{"db":"EMDB","id":"EMD-6480"}],"region_id":"DP03173r001","statement":[{"text":"The disordered N-terminus of APAF contains the caspase recruitment domain (CARD).","type":"Curator statement"},{"text":"The seven CARDs exhibit no EM density, likely reflecting their dynamic locations.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":104,"reference_id":"27697150","reference_source":"pmid","reference_html":"A near atomic structure of the active human apoptosome. <i> Cheng TC, Hong C, Akey IV, Yuan S, Akey CW. </i> Elife, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"emaiani","curator_name":"Emiliano Maiani","curator_orcid":"0000-0003-1432-5394","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5JUY"},{"db":"EMDB","id":"EMD-8178"}],"region_id":"DP03173r002","statement":[{"text":"The disordered N-terminus of APAF contains the caspase recruitment domain (CARD).","type":"Curator statement"},{"text":"We surmise that the three excluded Apaf-1 CARDs are disordered since they are not visible, but they may contribute to the propensity of the particles to aggregate.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":104,"reference_id":"28143931","reference_source":"pmid","reference_html":"Mechanistic insights into caspase-9 activation by the structure of the apoptosome holoenzyme. <i> Li Y, Zhou M, Hu Q, Bai XC, Huang W, Scheres SH, Shi Y. </i> Proc Natl Acad Sci U S A, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"emaiani","curator_name":"Emiliano Maiani","curator_orcid":"0000-0003-1432-5394","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5WVE"}],"region_id":"DP03173r003","ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2021_12","sequence":"MDAKARNCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGYKDLAALLHDGIPVVSSSSGKDSVSGITSYVRTVLCEGGVPQRPVVFVTRKKLVNAIQQKLSKLKGEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPGGVHWVSVGKQDKSGLLMKLQNLCTRLDQDESFSQRLPLNIEEAKDRLRILMLRKHPRSLLILDDVWDSWVLKAFDSQCQILLTTRDKSVTDSVMGPKYVVPVESSLGKEKGLEILSLFVNMKKADLPEQAHSIIKECKGSPLVVSLIGALLRDFPNRWEYYLKQLQNKQFKRIRKSSSYDYEALDEAMSISVEMLREDIKDYYTDLSILQKDVKVPTKVLCILWDMETEEVEDILQEFVNKSLLFCDRNGKSFRYYLHDLQVDFLTEKNCSQLQDLHKKIITQFQRYHQPHTLSPDQEDCMYWYNFLAYHMASAKMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEYRHILDEKDCAVSENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQAKQEVDNGMLYLEWINKKNITNLSRLVVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNCCHFTNSSHHLLLATGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWDATSANERKSINVKQFFLNLEDPQEDMEVIVKCCSWSADGARIMVAAKNKIFLFDIHTSGLLGEIHTGHHSTIQYCDFSPQNHLAVVALSQYCVELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQTIRLWETKKVCKNSAVMLKQEVDVVFQENEVMVLAVDHIRRLQLINGRTGQIDYLTEAQVSCCCLSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCIFLRGHQETVKDFRLLKNSRLLSWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHLCAPLSEEGAATHGGWVTDLCFSPDGKMLISAGGYIKWWNVVTGESSQTFYTNGTNLKKIHVSPDFKTYVTVDNLGILYILQTLE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000002A3D9","uniref100":"UniRef100_O14727","uniref90":"UniRef90_O14727","uniref50":"UniRef50_O14727","genes":[{"name":{"value":"APAF1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:576","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:576"}}]},"synonyms":[{"value":"KIAA0413"}]}],"alphafold_very_low_content":0.016025641025641024,"disorder_content":0.08333333333333333,"disprot_consensus":{"full":[{"start":1,"end":104,"type":"D"}],"Structural state":[{"start":1,"end":104,"type":"D"}]}},{"disprot_id":"DP03174","acc":"Q3UKX1","creator":"gerdos","date":"2021-01-17T07:51:22.187Z","features":{"pfam":[{"id":"PF00018","name":"SH3 domain","start":48,"end":93},{"id":"PF05175","name":"Methyltransferase small domain","start":142,"end":222},{"id":"PF22528","name":"Arginine methyltransferase oligomerization subdomain","start":256,"end":427}],"gene3D":[]},"length":445,"name":"Protein arginine N-methyltransferase 2","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":1,"end":106,"reference_id":"27879050","reference_source":"pmid","reference_html":"Structural studies of protein arginine methyltransferase 2 reveal its interactions with potential substrates and inhibitors. <i> Cura V, Marechal N, Troffer-Charlier N, Strub JM, van Haren MJ, Martin NI, Cianférani S, Bonnefond L, Cavarelli J. </i> FEBS J, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5FUL"},{"db":"PDB","id":"5FWD"},{"db":"PDB","id":"5FWA"}],"region_id":"DP03174r001","statement":[{"text":"The N-terminal module of mPRMT2 (residues 1-106)\npartially folded in a SH3 domain is missing in the electron density although present in the crystal.","type":"Discussion"},{"text":"We reveal that the N-terminal containing SH3 module is\ndisordered in the full-length crystal structures, and highlight idiosyncratic features of the PRMT2\nactive site.","type":"Abstract"},{"text":"Therefore, unlike zPRMT2, the absence of residues 1–106 in the electron density map was not the result of proteolysis before or during the crystallization process, but could be explained by a high flexibility of the N-terminal region within the crystals.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-28T09:23:31.904Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MEAPGEGPCSESQVIPVLEEDPVDYGCEMQLLQDGAQLQLQLQPEEFVAIADYTATDETQLSFLRGEKILILRQTTADWWWGERAGCCGYIPANHLGKQLEEYDPEDTWQDEEYFDSYGTLKLHLEMLADQPRTTKYHSVILQNKESLKDKVILDVGCGTGIISLFCAHHARPKAVYAVEASDMAQHTSQLVLQNGFADTITVFQQKVEDVVLPEKVDVLVSEWMGTCLLFEFMIESILYARDTWLKGDGIIWPTTAALHLVPCSAEKDYHSKVLFWDNAYEFNLSALKSLAIKEFFSRPKSNHILKPEDCLSEPCTILQLDMRTVQVPDLETMRGELRFDIQKAGTLHGFTAWFSVYFQSLEEGQPQQVLSTGPLHPTTHWKQTLFMMDDPVPVHTGDVVTGSVVLQRNPVWRRHMSVSLSWVVTSALDPTSQRVGEKVFPIWR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"dataset":[],"UniParc":"UPI00005AC2EF","uniref100":"UniRef100_Q3UKX1","uniref90":"UniRef90_Q6AYB9","uniref50":"UniRef50_P55345","genes":[{"name":{"value":"Prmt2","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAI22564.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAI22564.1"}},{"code":"ECO:0000313","source":{"name":"Ensembl","id":"ENSMUSP00000020452","url":"https://www.ensembl.org/id/ENSMUSP00000020452"}},{"code":"ECO:0000313","source":{"name":"MGI","id":"MGI:1316652","url":"http://www.informatics.jax.org/marker/MGI:1316652"}}]},"synonyms":[{"value":"Hrmt1l1","evidences":[{"code":"ECO:0000313","source":{"name":"MGI","id":"MGI:1316652","url":"http://www.informatics.jax.org/marker/MGI:1316652"}}]}]}],"alphafold_very_low_content":0.10112359550561797,"disorder_content":0.23820224719101124,"disprot_consensus":{"full":[{"start":1,"end":106,"type":"D"}],"Structural state":[{"start":1,"end":106,"type":"D"}]}},{"disprot_id":"DP03175","acc":"A1L1Q4","creator":"gerdos","date":"2021-01-17T07:59:43.412Z","features":{"pfam":[{"id":"PF00018","name":"SH3 domain","start":18,"end":61},{"id":"PF13649","name":"Methyltransferase domain","start":119,"end":216},{"id":"PF22528","name":"Arginine methyltransferase oligomerization subdomain","start":222,"end":393}],"gene3D":[]},"length":408,"name":"Protein arginine methyltransferase 2","ncbi_taxon_id":7955,"organism":"Danio rerio","regions":[{"start":1,"end":71,"reference_id":"27879050","reference_source":"pmid","reference_html":"Structural studies of protein arginine methyltransferase 2 reveal its interactions with potential substrates and inhibitors. <i> Cura V, Marechal N, Troffer-Charlier N, Strub JM, van Haren MJ, Martin NI, Cianférani S, Bonnefond L, Cavarelli J. </i> FEBS J, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03175r001","statement":[{"text":" The electron density map revealed the absence of residues 1-71 corresponding to\nthe N-terminus part containing the SH3 domain.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-28T09:26:05.759Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MIESESRDCNEGEEYVGLVDFVAEGDEQLSFSVGDRLLVHDRSSDVWWWAEMQGHFGYVPSSYLHQRTEDMEDAWQDDEYFGNYGTLRLHLEMLSDKPRTETYRQVILSNSAALREKVVLDLGCGTGVISLFCALLAKPAGVYAVEASSMAEHTEELVKQNGCDGVVTVFQERAENLTLPTKVDVLVSEWMGNCLLFEYMLESVLLARDRWLKKGGMMWPSSACLTIVPCQAFSDYRQKVEFWENPYGLNFSYLQSLAQKEFLSKPKFSHHLQPEDCLSTPADVITLDMVTIQVSDLERLKGEFTFTVEKSGMFHGFTVWFSAHFQCLEEDGPSIELNTGPYSEITHWKQTLFMLDAPVSVEEGDIIAGSIRLQRNPIWRRHLSITFLWNINSTEVSTVKTKCFPMWR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Actinopterygii","Neopterygii","Teleostei","Ostariophysi","Cypriniformes","Danionidae","Danioninae","Danio"],"dataset":[],"UniParc":"UPI0000ECF116","uniref100":"UniRef100_A1L1Q4","uniref90":"UniRef90_F1QDD1","uniref50":"UniRef50_F1QDD1","genes":[{"orfNames":[{"value":"SO:0001217","evidences":[{"code":"ECO:0000313","source":{"name":"ZFIN","id":"ZDB-GENE-041104-1","url":"http://zfin.org/cgi-bin/webdriver?MIval=aa-markerview.apg&OID=ZDB-GENE-041104-1"}}]}],"olnNames":[{"value":"prmt2","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAI29172.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAI29172.1"}},{"code":"ECO:0000313","source":{"name":"ZFIN","id":"ZDB-GENE-041104-1","url":"http://zfin.org/cgi-bin/webdriver?MIval=aa-markerview.apg&OID=ZDB-GENE-041104-1"}}]}]}],"alphafold_very_low_content":0.031862745098039214,"disorder_content":0.17401960784313725,"disprot_consensus":{"full":[{"start":1,"end":71,"type":"D"}],"Structural state":[{"start":1,"end":71,"type":"D"}]}},{"disprot_id":"DP03176","acc":"Q10344","creator":"gerdos","date":"2021-01-17T11:38:57.710Z","features":{"pfam":[{"id":"PF00838","name":"Translationally controlled tumour protein","start":1,"end":163}],"gene3D":[]},"length":168,"name":"Translationally-controlled tumor protein homolog","ncbi_taxon_id":284812,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","regions":[{"start":40,"end":61,"reference_id":"11473261","reference_source":"pmid","reference_html":"Structure of TCTP reveals unexpected relationship with guanine nucleotide-free chaperones. <i> Thaw P, Baxter NJ, Hounslow AM, Price C, Waltho JP, Craven CJ. </i> Nat Struct Biol, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1H7Y"},{"db":"PDB","id":"1H6Q"}],"region_id":"DP03176r001","statement":[{"text":"We have determined the three-dimensional structure of p23fyp, the TCTP from S. pombe, by heteronuclear NMR spectroscopy using a total of 2,254 experimentally determined restraints. Excluding the region Gly 40–Gly 61, which is highly mobile and disordered10, the structure is well defined (Fig. 2a; Table 1). ","type":"Introduction"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-28T09:17:26.700Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MLLYKDVISGDELVSDAYDLKEVDDIVYEADCQMVTVKQGGDVDIGANPSAEDAEENAEEGTETVNNLVYSFRLSPTSFDKKSYMSYIKGYMKAIKARLQESNPERVPVFEKNAIGFVKKILANFKDYDFYIGESMDPDAMVVLMNYREDGITPYMIFFKDGLVSEKF","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"dataset":[],"UniParc":"UPI00001130BC","uniref100":"UniRef100_Q10344","uniref90":"UniRef90_Q10344","uniref50":"UniRef50_P35691","genes":[{"name":{"value":"p23fy"},"orfNames":[{"value":"SPAC1F12.02c"}]}],"alphafold_very_low_content":0.047619047619047616,"disorder_content":0.13095238095238096,"disprot_consensus":{"full":[{"start":40,"end":61,"type":"D"}],"Structural state":[{"start":40,"end":61,"type":"D"}]}},{"disprot_id":"DP03177","acc":"Q8CJ26","creator":"gerdos","date":"2021-01-17T11:59:36.735Z","features":{"pfam":[{"id":"PF00531","name":"Death domain","start":143,"end":220},{"id":"PF18422","name":"Tumor necrosis factor receptor member 16 trans-membrane domain","start":48,"end":85}],"gene3D":[]},"length":228,"name":"Death domain-containing membrane protein NRADD","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":1,"end":54,"reference_id":"31033000","reference_source":"pmid","reference_html":"NMR structure of a full-length single-pass membrane protein NRADD. <i> Nadezhdin KD, Goncharuk SA, Arseniev AS, Mineev KS. </i> Proteins, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6HJ7"}],"region_id":"DP03177r001","statement":[{"text":"N-terminal ectodomain is 54 residues long (excl. N-terminal tag) and is disordered.","type":"Results"},{"text":"The unstructured nature of both N- and C-terminal juxta-membrane regions is supported by the lack of long-range NOEs and analysis of chemical shifts in TALOS-N software (see Figure 2B).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-28T09:35:51.703Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":78,"end":127,"reference_id":"31033000","reference_source":"pmid","reference_html":"NMR structure of a full-length single-pass membrane protein NRADD. <i> Nadezhdin KD, Goncharuk SA, Arseniev AS, Mineev KS. </i> Proteins, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6HJ7"}],"region_id":"DP03177r002","statement":[{"text":"The cytoplasmic domain consists of two parts: an intrinsically disordered juxta-membrane region and a globular C-terminal death domain. The unstructured nature of both N- and C-terminal juxta-membrane regions is supported by the lack of long-range NOEs and analysis of chemical shifts in TALOS-N software (see Figure 2B).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-28T09:36:28.308Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MLYNVSKGVVYSDTALQGQDGDREGMWVGAGGALAPNTSSLFPPEPPGASSNIIPVYCALLATVILGLLAYVAFKCWRSHKQRQQLAKARTVELGDPDRDQRRGDSNVFVDSPPSLEPCIPSQGPHPDLGCQLYLHIPQQQQEEVQRLLMMGEPAKGWQELAGHLGYQAEAVETMACDQMPAYTLLRNWAAQEGNRATLRVLEDALAAIGREDVVQVLSSPAESSSVV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"dataset":[],"UniParc":"UPI0000028111","uniref100":"UniRef100_Q8CJ26","uniref90":"UniRef90_Q8K5A9","uniref50":"UniRef50_Q8K5A9","genes":[{"name":{"value":"Nradd"}}],"alphafold_very_low_content":0.33771929824561403,"disorder_content":0.45614035087719296,"disprot_consensus":{"full":[{"start":1,"end":54,"type":"D"},{"start":78,"end":127,"type":"D"}],"Structural state":[{"start":1,"end":54,"type":"D"},{"start":78,"end":127,"type":"D"}]}},{"disprot_id":"DP03178","acc":"Q99250","creator":"maspromonte","date":"2021-01-17T15:13:54.139Z","features":{"pfam":[{"id":"PF00520","name":"Ion transport protein","start":128,"end":434},{"id":"PF00520","name":"Ion transport protein","start":759,"end":990},{"id":"PF00520","name":"Ion transport protein","start":1207,"end":1482},{"id":"PF00520","name":"Ion transport protein","start":1531,"end":1786},{"id":"PF06512","name":"Sodium ion transport-associated","start":997,"end":1203},{"id":"PF11933","name":"Cytoplasmic domain of voltage-gated Na+ ion channel","start":558,"end":709},{"id":"PF24609","name":"SCN5A-like, C-terminal IQ motif","start":1898,"end":1930}],"gene3D":[]},"length":2005,"name":"Sodium channel protein type 2 subunit alpha","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1777,"end":1789,"reference_id":"19129176","reference_source":"pmid","reference_html":"Solution structure of the NaV1.2 C-terminal EF-hand domain. <i> Miloushev VZ, Levine JA, Arbing MA, Hunt JF, Pitt GS, Palmer AG. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2KAV"}],"region_id":"DP03178r001","statement":[{"text":"The ordered structure extends from residues Leu-1790 to Glu-1868 and is composed of\nfour α-helices separated by two short anti-parallel -strands; a less well defined helical region extends from residue Ser-1869 to Arg-1882, and a disordered N-terminal region encompasses residues 1777–1789.","type":"Abstract"},{"text":"The cis conformation is evidenced by stronger X-Pro Hα-Hα than X-Pro Hα-Hδ NOE contacts and differences of Cβ-Cγ chemical shifts of 9.4 and 8.5 ppm, respectively (59, 60).\nMedium range 1 H-1 H NOEs, steady-state {1H}-15N NOE, and 13Cα secondary chemical shifts for NaV1.2 indicate that the CTD forms a well folded domain between residues Leu-1790\nand Glu-1868, with a less well ordered region between residues Ser-1869 and Arg-1882 and a disordered N-terminal region between residues Gly-1777 and Pro-1789 (Fig. 1 and supplemental Fig. S1).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-28T09:18:49.381Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":116,"reference_id":"30765605","reference_source":"pmid","reference_html":"Molecular basis for pore blockade of human Na<sup>+</sup> channel Na<sub>v</sub>1.2 by the μ-conotoxin KIIIA. <i> Pan X, Li Z, Huang X, Huang G, Gao S, Shen H, Liu L, Lei J, Yan N. </i> Science, 2019","date":"2022-09-28T10:07:08.293Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":3,"cross_refs":[{"db":"PDB","id":"6J8E"}],"region_id":"DP03178r002","statement":[{"text":"For Nav1.2, the N-terminal 116 residues, extracellular loop (residues 285-313), intracellular I-II linker (residues 442-739), II-III linker (residues 988-1190), and C-terminal sequences after Ser1786 were not modelled due to the lack of corresponding densities. ","type":"Supplementary material"}],"ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:134817783"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29101","entry_name":"sodium(1+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-28T13:56:54.350Z"}},{"start":285,"end":313,"reference_id":"30765605","reference_source":"pmid","reference_html":"Molecular basis for pore blockade of human Na<sup>+</sup> channel Na<sub>v</sub>1.2 by the μ-conotoxin KIIIA. <i> Pan X, Li Z, Huang X, Huang G, Gao S, Shen H, Liu L, Lei J, Yan N. </i> Science, 2019","date":"2022-09-26T15:15:00.541Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":3,"cross_refs":[{"db":"PDB","id":"6J8E"}],"region_id":"DP03178r003","statement":[{"text":"For Nav1.2, the N-terminal 116 residues, extracellular loop (residues 285-313), intracellular I-II linker (residues 442-739), II-III linker (residues 988-1190), and C-terminal sequences after Ser1786 were not modelled due to the lack of corresponding densities. ","type":"Supplementary material"}],"ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:134817783"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29101 ","entry_name":"sodium(1+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-27T14:10:56.805Z"}},{"start":442,"end":739,"reference_id":"30765605","reference_source":"pmid","reference_html":"Molecular basis for pore blockade of human Na<sup>+</sup> channel Na<sub>v</sub>1.2 by the μ-conotoxin KIIIA. <i> Pan X, Li Z, Huang X, Huang G, Gao S, Shen H, Liu L, Lei J, Yan N. </i> Science, 2019","date":"2022-09-26T15:15:49.597Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":3,"cross_refs":[{"db":"PDB","id":"6J8E"}],"region_id":"DP03178r004","statement":[{"text":"For Nav1.2, the N-terminal 116 residues, extracellular loop (residues 285-313), intracellular I-II linker (residues 442-739), II-III linker (residues 988-1190), and C-terminal sequences after Ser1786 were not modelled due to the lack of corresponding densities. ","type":"Supplementary material"}],"ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:134817783"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29101 ","entry_name":"sodium(1+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-27T14:10:56.935Z"}},{"start":988,"end":1190,"reference_id":"30765605","reference_source":"pmid","reference_html":"Molecular basis for pore blockade of human Na<sup>+</sup> channel Na<sub>v</sub>1.2 by the μ-conotoxin KIIIA. <i> Pan X, Li Z, Huang X, Huang G, Gao S, Shen H, Liu L, Lei J, Yan N. </i> Science, 2019","date":"2022-10-25T14:43:25.929Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":3,"cross_refs":[{"db":"PDB","id":"6J8E"}],"region_id":"DP03178r005","statement":[{"text":"For Nav1.2, the N-terminal 116 residues, extracellular loop (residues 285-313), intracellular I-II linker (residues 442-739), II-III linker (residues 988-1190), and C-terminal sequences after Ser1786 were not modelled due to the lack of corresponding densities. ","type":"Supplementary material"}],"ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:134817783"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29101 ","entry_name":"sodium(1+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-25T14:44:58.051Z"}},{"start":1786,"end":2005,"reference_id":"30765605","reference_source":"pmid","reference_html":"Molecular basis for pore blockade of human Na<sup>+</sup> channel Na<sub>v</sub>1.2 by the μ-conotoxin KIIIA. <i> Pan X, Li Z, Huang X, Huang G, Gao S, Shen H, Liu L, Lei J, Yan N. </i> Science, 2019","date":"2022-09-28T10:19:15.510Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":3,"cross_refs":[{"db":"PDB","id":"6J8E"}],"region_id":"DP03178r006","statement":[{"text":"For Nav1.2, the N-terminal 116 residues, extracellular loop (residues 285-313), intracellular I-II linker (residues 442-739), II-III linker (residues 988-1190), and C-terminal sequences after Ser1786 were not modelled due to the lack of corresponding densities. ","type":"Supplementary material"}],"ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:134817783"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29101 ","entry_name":"sodium(1+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-28T13:56:56.923Z"}},{"start":442,"end":739,"reference_id":"30765605","reference_source":"pmid","reference_html":"Molecular basis for pore blockade of human Na<sup>+</sup> channel Na<sub>v</sub>1.2 by the μ-conotoxin KIIIA. <i> Pan X, Li Z, Huang X, Huang G, Gao S, Shen H, Liu L, Lei J, Yan N. </i> Science, 2019","date":"2022-10-11T07:59:33.225Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6J8E"}],"region_id":"DP03178r007","statement":[{"text":"For Nav1.2, the N-terminal 116 residues, extracellular loop (residues 285-313), intracellular I-II linker (residues 442-739), II-III linker (residues 988-1190), and C-terminal sequences after Ser1786 were not modelled due to the lack of corresponding densities.","type":"Supplementary material"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:134817783"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29101","entry_name":"sodium(1+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-17T14:49:38.338Z"}},{"start":988,"end":1190,"reference_id":"30765605","reference_source":"pmid","reference_html":"Molecular basis for pore blockade of human Na<sup>+</sup> channel Na<sub>v</sub>1.2 by the μ-conotoxin KIIIA. <i> Pan X, Li Z, Huang X, Huang G, Gao S, Shen H, Liu L, Lei J, Yan N. </i> Science, 2019","date":"2022-10-11T08:00:31.479Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6J8E"}],"region_id":"DP03178r008","statement":[{"text":"For Nav1.2, the N-terminal 116 residues, extracellular loop (residues 285-313), intracellular I-II linker (residues 442-739), II-III linker (residues 988-1190), and C-terminal sequences after Ser1786 were not modelled due to the lack of corresponding densities.","type":"Supplementary material"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:134817783"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29101","entry_name":"sodium(1+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-17T14:49:38.778Z"}},{"start":1777,"end":1787,"reference_id":"25232683","reference_source":"pmid","reference_html":"Structural analyses of Ca²⁺/CaM interaction with NaV channel C-termini reveal mechanisms of calcium-dependent regulation. <i> Wang C, Chung BC, Yan H, Wang HG, Lee SY, Pitt GS. </i> Nat Commun, 2014","date":"2022-10-27T10:01:24.509Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"4JPZ"}],"region_id":"DP03178r009","statement":[{"text":"The final model contains the NaV1.2 amino acids 1788-1929, FGF13U amino acids 11-158, and the CaM amino acids 7-149. The model was refined to Rwork/Rfree of 21.5/24.6 % (Table 1). ","type":"Results"},{"text":"The PDB evidence shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92913"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0DP23"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-28T18:47:07.340Z"}},{"start":1900,"end":1905,"reference_id":"25232683","reference_source":"pmid","reference_html":"Structural analyses of Ca²⁺/CaM interaction with NaV channel C-termini reveal mechanisms of calcium-dependent regulation. <i> Wang C, Chung BC, Yan H, Wang HG, Lee SY, Pitt GS. </i> Nat Commun, 2014","date":"2022-10-27T10:17:00.940Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"GO:0005516","term_name":"calmodulin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":" Arg1902Cys","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP03178r011","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"Second, to test the proposed role of Arg1902 in the relayed interactions in NaV1.2 CTD/apoCaM, we measured the affinity of apoCaM for the wild type and Arg1902Cys mutant NaV1.2 CTDs by ITC. Consistent with our hypothesis, the Arg1902Cys mutation reduced affinity of apoCaM for the NaV1.2 CTD significantly (Table 3 and Supplementary Fig. 4C).","type":"Results"},{"text":"The ITC experiment with the CaM34 mutant showed a reduced affinity for the Arg1902Cys mutant compared to the wild CTD in the presence of Ca2+ (Table 3 and Supplementary Fig. 4E).","type":"Results"}],"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"P0DP23","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-28T18:53:19.861Z"}}],"regions_counter":14,"released":"2021_12","sequence":"MAQSVLVPPGPDSFRFFTRESLAAIEQRIAEEKAKRPKQERKDEDDENGPKPNSDLEAGKSLPFIYGDIPPEMVSVPLEDLDPYYINKKTFIVLNKGKAISRFSATPALYILTPFNPIRKLAIKILVHSLFNMLIMCTILTNCVFMTMSNPPDWTKNVEYTFTGIYTFESLIKILARGFCLEDFTFLRDPWNWLDFTVITFAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCLQWPPDNSSFEINITSFFNNSLDGNGTTFNRTVSIFNWDEYIEDKSHFYFLEGQNDALLCGNSSDAGQCPEGYICVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDFWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLINLILAVVAMAYEEQNQATLEEAEQKEAEFQQMLEQLKKQQEEAQAAAAAASAESRDFSGAGGIGVFSESSSVASKLSSKSEKELKNRRKKKKQKEQSGEEEKNDRVRKSESEDSIRRKGFRFSLEGSRLTYEKRFSSPHQSLLSIRGSLFSPRRNSRASLFSFRGRAKDIGSENDFADDEHSTFEDNDSRRDSLFVPHRHGERRHSNVSQASRASRVLPILPMNGKMHSAVDCNGVVSLVGGPSTLTSAGQLLPEGTTTETEIRKRRSSSYHVSMDLLEDPTSRQRAMSIASILTNTMEELEESRQKCPPCWYKFANMCLIWDCCKPWLKVKHLVNLVVMDPFVDLAITICIVLNTLFMAMEHYPMTEQFSSVLSVGNLVFTGIFTAEMFLKIIAMDPYYYFQEGWNIFDGFIVSLSLMELGLANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKISNDCELPRWHMHDFFHSFLIVFRVLCGEWIETMWDCMEVAGQTMCLTVFMMVMVIGNLVVLNLFLALLLSSFSSDNLAATDDDNEMNNLQIAVGRMQKGIDFVKRKIREFIQKAFVRKQKALDEIKPLEDLNNKKDSCISNHTTIEIGKDLNYLKDGNGTTSGIGSSVEKYVVDESDYMSFINNPSLTVTVPIAVGESDFENLNTEEFSSESDMEESKEKLNATSSSEGSTVDIGAPAEGEQPEVEPEESLEPEACFTEDCVRKFKCCQISIEEGKGKLWWNLRKTCYKIVEHNWFETFIVFMILLSSGALAFEDIYIEQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGFQVYFTNAWCWLDFLIVDVSLVSLTANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALLGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCINYTTGEMFDVSVVNNYSECKALIESNQTARWKNVKVNFDNVGLGYLSLLQVATFKGWMDIMYAAVDSRNVELQPKYEDNLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPANKFQGMVFDFVTKQVFDISIMILICLNMVTMMVETDDQSQEMTNILYWINLVFIVLFTGECVLKLISLRYYYFTIGWNIFDFVVVILSIVGMFLAELIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKREVGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSGPPDCDPDKDHPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFIEFAKLSDFADALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEERFMASNPSKVSYEPITTTLKRKQEEVSAIIIQRAYRRYLLKQKVKKVSSIYKKDKGKECDGTPIKEDTLIDKLNENSTPEKTDMTPSTTSPPSYDSVTKPEKEKFEKDKSEKEDKGKDIRESKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"UniParc":"UPI00001684BB","uniref100":"UniRef100_Q99250","uniref90":"UniRef90_Q99250","uniref50":"UniRef50_Q99250","genes":[{"name":{"value":"SCN2A"},"synonyms":[{"value":"NAC2"},{"value":"SCN2A1"},{"value":"SCN2A2"}]}],"alphafold_very_low_content":0.25885286783042394,"disorder_content":0.43640897755610975,"disprot_consensus":{"full":[{"start":1,"end":116,"type":"D"},{"start":285,"end":313,"type":"D"},{"start":442,"end":739,"type":"D"},{"start":988,"end":1190,"type":"D"},{"start":1777,"end":2005,"type":"D"}],"Structural state":[{"start":1,"end":116,"type":"D"},{"start":285,"end":313,"type":"D"},{"start":442,"end":739,"type":"D"},{"start":988,"end":1190,"type":"D"},{"start":1777,"end":2005,"type":"D"}],"Disorder function":[{"start":442,"end":739,"type":"F"},{"start":988,"end":1190,"type":"F"}],"Molecular function":[{"start":1900,"end":1905,"type":"F"}]}},{"disprot_id":"DP03179","acc":"O95391","creator":"rdavidovic","date":"2021-01-17T16:32:43.269Z","features":{"pfam":[{"id":"PF11708","name":"Pre-mRNA splicing Prp18-interacting factor","start":162,"end":434},{"id":"PF30379","name":"SLU7_N","start":115,"end":140}],"gene3D":[]},"length":586,"name":"Pre-mRNA-splicing factor SLU7","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":61,"reference_id":"28502770","reference_source":"pmid","reference_html":"An Atomic Structure of the Human Spliceosome. <i> Zhang X, Yan C, Hang J, Finci LI, Lei J, Shi Y. </i> Cell, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"rdavidovic","curator_name":"Radoslav Davidović","curator_orcid":"0000-0002-6097-6203","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5XJC"},{"db":"EMDB","id":"EMD-6721"}],"region_id":"DP03179r007","statement":[{"text":"Importantly, the disordered portions of Slu7 (residues 1–61, 197–264, and 372–586) are highly enriched by positively charged amino acids: 62 Arg and Lys residues in total. ","type":"Discussion"},{"text":"The fine quality of the EM density map allows identification of two large segments of Slu7: residues 62–196 and 265–371 (Table S2).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-07T08:41:34.122Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":197,"end":264,"reference_id":"28502770","reference_source":"pmid","reference_html":"An Atomic Structure of the Human Spliceosome. <i> Zhang X, Yan C, Hang J, Finci LI, Lei J, Shi Y. </i> Cell, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"rdavidovic","curator_name":"Radoslav Davidović","curator_orcid":"0000-0002-6097-6203","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5XJC"},{"db":"EMDB","id":"EMD-6721"}],"region_id":"DP03179r008","statement":[{"text":"Importantly, the disordered portions of Slu7 (residues 1–61, 197–264, and 372–586) are highly enriched by positively charged amino acids: 62 Arg and Lys residues in total. ","type":"Discussion"},{"text":"The fine quality of the EM density map allows identification of two large segments of Slu7: residues 62–196 and 265–371 (Table S2).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-07T08:41:35.406Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":372,"end":586,"reference_id":"28502770","reference_source":"pmid","reference_html":"An Atomic Structure of the Human Spliceosome. <i> Zhang X, Yan C, Hang J, Finci LI, Lei J, Shi Y. </i> Cell, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"rdavidovic","curator_name":"Radoslav Davidović","curator_orcid":"0000-0002-6097-6203","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5XJC"},{"db":"EMDB","id":"EMD-6721"}],"region_id":"DP03179r009","statement":[{"text":"Importantly, the disordered portions of Slu7 (residues 1–61, 197–264, and 372–586) are highly enriched by positively charged amino acids: 62 Arg and Lys residues in total. ","type":"Discussion"},{"text":"The fine quality of the EM density map allows identification of two large segments of Slu7: residues 62–196 and 265–371 (Table S2).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-07T08:41:36.271Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":9,"released":"2021_12","sequence":"MSATVVDAVNAAPLSGSKEMSLEEPKKMTREDWRKKKELEEQRKLGNAPAEVDEEGKDINPHIPQYISSVPWYIDPSKRPTLKHQRPQPEKQKQFSSSGEWYKRGVKENSIITKYRKGACENCGAMTHKKKDCFERPRRVGAKFTGTNIAPDEHVQPQLMFDYDGKRDRWNGYNPEEHMKIVEEYAKVDLAKRTLKAQKLQEELASGKLVEQANSPKHQWGEEEPNSQMEKDHNSEDEDEDKYADDIDMPGQNFDSKRRITVRNLRIREDIAKYLRNLDPNSAYYDPKTRAMRENPYANAGKNPDEVSYAGDNFVRYTGDTISMAQTQLFAWEAYDKGSEVHLQADPTKLELLYKSFKVKKEDFKEQQKESILEKYGGQEHLDAPPAELLLAQTEDYVEYSRHGTVIKGQERAVACSKYEEDVKIHNHTHIWGSYWKEGRWGYKCCHSFFKYSYCTGEAGKEIVNSEECIINEITGEESVKKPQTLMELHQEKLKEEKKKKKKKKKKHRKSSSDSDDEEKKHEKLKKALNAEEARLLHVKETMQIDERKRPYNSMYETREPTEEEMEAYRMKRQRPDDPMASFLGQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["RNA-binding proteins"],"UniParc":"UPI000013E3CE","uniref100":"UniRef100_O95391","uniref90":"UniRef90_O95391","uniref50":"UniRef50_O95391","genes":[{"name":{"value":"SLU7"}}],"alphafold_very_low_content":0.14334470989761092,"disorder_content":0.5870307167235495,"disprot_consensus":{"full":[{"start":1,"end":61,"type":"D"},{"start":197,"end":264,"type":"D"},{"start":372,"end":586,"type":"D"}],"Structural state":[{"start":1,"end":61,"type":"D"},{"start":197,"end":264,"type":"D"},{"start":372,"end":586,"type":"D"}]}},{"disprot_id":"DP03180","acc":"Q03692","creator":"rdavidovic","date":"2021-01-17T17:40:00.866Z","features":{"pfam":[{"id":"PF00386","name":"C1q domain","start":553,"end":677},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":106,"end":151},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":464,"end":518}],"gene3D":[]},"length":680,"name":"Collagen alpha-1(X) chain","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":521,"end":548,"reference_id":"11839302","reference_source":"pmid","reference_html":"Insight into Schmid metaphyseal chondrodysplasia from the crystal structure of the collagen X NC1 domain trimer. <i> Bogin O, Kvansakul M, Rom E, Singer J, Yayon A, Hohenester E. </i> Structure, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"rdavidovic","curator_name":"Radoslav Davidović","curator_orcid":"0000-0002-6097-6203","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1GR3"}],"region_id":"DP03180r001","statement":[{"text":"Untagged collagen X NC1 domain produced in an in vitro expression system is stabilized significantly by the N-terminal segment. The most obvious interpretation of this observation is that a defined structure of the N-terminal segment contributes to NC1 trimer formation, yet this is not observed in our crystals.","type":"Discussion"},{"text":"Residues 549–680 have clear and continuous electron density; the N-terminal 28 residues and the His6 tag are not visible and are presumed to be disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-02-12T15:35:59.571Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MLPQIPFLLLVSLNLVHGVFYAERYQMPTGIKGPLPNTKTQFFIPYTIKSKGIAVRGEQGTPGPPGPAGPRGHPGPSGPPGKPGYGSPGLQGEPGLPGPPGPSAVGKPGVPGLPGKPGERGPYGPKGDVGPAGLPGPRGPPGPPGIPGPAGISVPGKPGQQGPTGAPGPRGFPGEKGAPGVPGMNGQKGEMGYGAPGRPGERGLPGPQGPTGPSGPPGVGKRGENGVPGQPGIKGDRGFPGEMGPIGPPGPQGPPGERGPEGIGKPGAAGAPGQPGIPGTKGLPGAPGIAGPPGPPGFGKPGLPGLKGERGPAGLPGGPGAKGEQGPAGLPGKPGLTGPPGNMGPQGPKGIPGSHGLPGPKGETGPAGPAGYPGAKGERGSPGSDGKPGYPGKPGLDGPKGNPGLPGPKGDPGVGGPPGLPGPVGPAGAKGMPGHNGEAGPRGAPGIPGTRGPIGPPGIPGFPGSKGDPGSPGPPGPAGIATKGLNGPTGPPGPPGPRGHSGEPGLPGPPGPPGPPGQAVMPEGFIKAGQRPSLSGTPLVSANQGVTGMPVSAFTVILSKAYPAIGTPIPFDKILYNRQQHYDPRTGIFTCQIPGIYYFSYHVHVKGTHVWVGLYKNGTPVMYTYDEYTKGYLDQASGSAIIDLTENDQVWLQLPNAESNGLYSSEYVHSSFSGFLVAPM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000016A719","uniref100":"UniRef100_Q03692","uniref90":"UniRef90_Q03692","uniref50":"UniRef50_Q03692","genes":[{"name":{"value":"COL10A1"}}],"alphafold_very_low_content":0.35,"disorder_content":0.041176470588235294,"disprot_consensus":{"full":[{"start":521,"end":548,"type":"D"}],"Structural state":[{"start":521,"end":548,"type":"D"}]}},{"disprot_id":"DP03182","acc":"Q17RS7","creator":"rdavidovic","date":"2021-01-17T18:29:53.497Z","features":{"pfam":[{"id":"PF00752","name":"XPG N-terminal domain","start":1,"end":93},{"id":"PF00867","name":"XPG I-region","start":125,"end":208},{"id":"PF18704","name":"Chromatin organization modifier domain 2","start":398,"end":458}],"gene3D":[]},"length":908,"name":"Flap endonuclease GEN homolog 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":243,"end":307,"reference_id":"26682650","reference_source":"pmid","reference_html":"Human Holliday junction resolvase GEN1 uses a chromodomain for efficient DNA recognition and cleavage. <i> Lee SH, Princz LN, Klügel MF, Habermann B, Pfander B, Biertümpfel C. </i> Elife, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"rdavidovic","curator_name":"Radoslav Davidović","curator_orcid":"0000-0002-6097-6203","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5T9J"}],"region_id":"DP03182r003","statement":[{"text":"The EXO domain in GEN1 has a 78 amino acid insertion (residues 245–322), of which only helix α12b (residues 308–322) is ordered in the structure (Figure 1A, gray and Figure 2).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-23T09:17:35.614Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2021_12","sequence":"MGVNDLWQILEPVKQHIPLRNLGGKTIAVDLSLWVCEAQTVKKMMGSVMKPHLRNLFFRISYLTQMDVKLVFVMEGEPPKLKADVISKRNQSRYGSSGKSWSQKTGRSHFKSVLRECLHMLECLGIPWVQAAGEAEAMCAYLNAGGHVDGCLTNDGDTFLYGAQTVYRNFTMNTKDPHVDCYTMSSIKSKLGLDRDALVGLAILLGCDYLPKGVPGVGKEQALKLIQILKGQSLLQRFNRWNETSCNSSPQLLVTKKLAHCSVCSHPGSPKDHERNGCRLCKSDKYCEPHDYEYCCPCEWHRTEHDRQLSEVENNIKKKACCCEGFPFHEVIQEFLLNKDKLVKVIRYQRPDLLLFQRFTLEKMEWPNHYACEKLLVLLTHYDMIERKLGSRNSNQLQPIRIVKTRIRNGVHCFEIEWEKPEHYAMEDKQHGEFALLTIEEESLFEAAYPEIVAVYQKQKLEIKGKKQKRIKPKENNLPEPDEVMSFQSHMTLKPTCEIFHKQNSKLNSGISPDPTLPQESISASLNSLLLPKNTPCLNAQEQFMSSLRPLAIQQIKAVSKSLISESSQPNTSSHNISVIADLHLSTIDWEGTSFSNSPAIQRNTFSHDLKSEVESELSAIPDGFENIPEQLSCESERYTANIKKVLDEDSDGISPEEHLLSGITDLCLQDLPLKERIFTKLSYPQDNLQPDVNLKTLSILSVKESCIANSGSDCTSHLSKDLPGIPLQNESRDSKILKGDQLLQEDYKVNTSVPYSVSNTVVKTCNVRPPNTALDHSRKVDMQTTRKILMKKSVCLDRHSSDEQSAPVFGKAKYTTQRMKHSSQKHNSSHFKESGHNKLSSPKIHIKETEQCVRSYETAENEESCFPDSTKSSLSSLQCHKKENNSGTCLDSPLPLRQRLKLRFQST","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI00004113DA","uniref100":"UniRef100_Q17RS7","uniref90":"UniRef90_Q17RS7","uniref50":"UniRef50_Q17RS7","genes":[{"name":{"value":"GEN1"}}],"alphafold_very_low_content":0.46806167400881055,"disorder_content":0.07158590308370044,"disprot_consensus":{"full":[{"start":243,"end":307,"type":"D"}],"Structural state":[{"start":243,"end":307,"type":"D"}]}},{"disprot_id":"DP03184","acc":"P09919","creator":"achasapi","date":"2021-01-17T18:51:28.722Z","features":{"pfam":[{"id":"PF16647","name":"Granulocyte colony-stimulating factor","start":51,"end":202}],"gene3D":[]},"length":207,"name":"Granulocyte colony-stimulating factor","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":157,"end":166,"reference_id":"7685117","reference_source":"pmid","reference_html":"The structure of granulocyte-colony-stimulating factor and its relationship to other growth factors. <i> Hill CP, Osslund TD, Eisenberg D. </i> Proc Natl Acad Sci U S A, 1993","date":"2022-02-14T09:00:00.000Z","curator_id":"achasapi","curator_name":"Anastasia Chasapi","curator_orcid":"0000-0003-1986-5007","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1RHG"}],"region_id":"DP03184r001","statement":[{"text":"Other sections were less precisely determined; in particular, residues -1 to 9, 65 to 70, 127 to 136, and 173 to 174 did not have convincing density.","type":"Methods"},{"text":"This gave a noticeable improvement in the map quality; however, it was still not possible to locate the missing residues, which remain undefined even after refinement.","type":"Methods"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MAGPATQSPMKLMALQLLLWHSALWTVQEATPLGPASSLPQSFLLKCLEQVRKIQGDGAALQEKLVSECATYKLCHPEELVLLGHSLGIPWAPLSSCPSQALQLAGCLSQLHSGLFLYQGLLQALEGISPELGPTLDTLQLDVADFATTIWQQMEELGMAPALQPTQGAMPAFASAFQRRAGGVLVASHLQSFLEVSYRVLRHLAQP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI0000128525","uniref100":"UniRef100_P09919","uniref90":"UniRef90_P09919","uniref50":"UniRef50_P09919","genes":[{"name":{"value":"CSF3"},"synonyms":[{"value":"C17orf33"},{"value":"GCSF"}]}],"alphafold_very_low_content":0.03864734299516908,"disorder_content":0.04830917874396135,"disprot_consensus":{"full":[{"start":157,"end":166,"type":"D"}],"Structural state":[{"start":157,"end":166,"type":"D"}]}},{"disprot_id":"DP03185","acc":"O75223","creator":"rdavidovic","date":"2021-01-17T18:51:47.052Z","features":{"pfam":[{"id":"PF13772","name":"AIG2-like family","start":78,"end":160}],"gene3D":[]},"length":188,"name":"Gamma-glutamylcyclotransferase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":2,"end":13,"reference_id":"17932939","reference_source":"pmid","reference_html":"Crystal structure of Homo sapiens protein LOC79017. <i> Bae E, Bingman CA, Aceti DJ, Phillips GN. </i> Proteins, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"rdavidovic","curator_name":"Radoslav Davidović","curator_orcid":"0000-0002-6097-6203","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":4,"region_id":"DP03185r002","statement":[{"text":"The asymmetric unit of the structure contains two LOC79017 monomers and 141 water molecules. Several N‐ and C‐terminal residues (residues 1–13 and 183–188 for chain A; residues 1–14 and 184–188 for chain B) were not included in the model due to insufficient electron density. ","type":"Results"},{"text":"The starting Met is missing and the first residue  in the PDB is just a cloning artifact.","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"2Q53"},{"db":"PDB","id":"2I5T"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-07T09:00:35.067Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":13,"reference_id":"18515354","reference_source":"pmid","reference_html":"The identification and structural characterization of C7orf24 as gamma-glutamyl cyclotransferase. An essential enzyme in the gamma-glutamyl cycle. <i> Oakley AJ, Yamada T, Liu D, Coggan M, Clark AG, Board PG. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"rdavidovic","curator_name":"Radoslav Davidović","curator_orcid":"0000-0002-6097-6203","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3CRY"},{"db":"PDB","id":"2RBH"}],"region_id":"DP03185r004","statement":[{"text":"The structure comprises a dimer with continuous electron density observable for residues 14–182 in monomer A and residues 15–183 in monomer B as well as 34 water molecules. No electron density is apparent for the NH2-terminal 13 (monomer A) or 14 (monomer B) residues.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-02-12T17:03:30.262Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":4,"released":"2021_12","sequence":"MANSGCKDVTGPDEESFLYFAYGSNLLTERIHLRNPSAAFFCVARLQDFKLDFGNSQGKTSQTWHGGIATIFQSPGDEVWGVVWKMNKSNLNSLDEQEGVKSGMYVVIEVKVATQEGKEITCRSYLMTNYESAPPSPQYKKIICMGAKENGLPLEYQEKLKAIEPNDYTGKVSEEIEDIIKKGETQTL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI00000473DC","uniref100":"UniRef100_O75223","uniref90":"UniRef90_O75223","uniref50":"UniRef50_O75223","genes":[{"name":{"value":"GGCT","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:21705","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:21705"}}]},"synonyms":[{"value":"C7orf24"},{"value":"CRF21"}]}],"alphafold_very_low_content":0.026595744680851064,"disorder_content":0.06914893617021277,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"D"}],"Structural state":[{"start":1,"end":13,"type":"D"}]}},{"disprot_id":"DP03186","acc":"P28325","creator":"achasapi","date":"2021-01-17T19:16:26.554Z","features":{"pfam":[{"id":"PF00031","name":"Cystatin domain","start":32,"end":128}],"gene3D":[]},"length":142,"name":"Cystatin-D","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":21,"end":31,"reference_id":"15728581","reference_source":"pmid","reference_html":"Crystal structure of human cystatin D, a cysteine peptidase inhibitor with restricted inhibition profile. <i> Alvarez-Fernandez M, Liang YH, Abrahamson M, Su XD. </i> J Biol Chem, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"achasapi","curator_name":"Anastasia Chasapi","curator_orcid":"0000-0003-1986-5007","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1ROA"}],"region_id":"DP03186r001","statement":[{"text":"No electron density was detected for the residues in the N-terminal segment before Ala10 (Fig. 1A). This region must thus be disordered in structure. ","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":21,"end":30,"reference_id":"15728581","reference_source":"pmid","reference_html":"Crystal structure of human cystatin D, a cysteine peptidase inhibitor with restricted inhibition profile. <i> Alvarez-Fernandez M, Liang YH, Abrahamson M, Su XD. </i> J Biol Chem, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"achasapi","curator_name":"Anastasia Chasapi","curator_orcid":"0000-0003-1986-5007","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1RN7"}],"region_id":"DP03186r002","statement":[{"text":"No electron density was detected for the residues in the N-terminal segment before Ala10 (Fig. 1A). This region must thus be disordered in structure. ","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MMWPMHTPLLLLTALMVAVAGSASAQSRTLAGGIHATDLNDKSVQCALDFAISEYNKVINKDEYYSRPLQVMAAYQQIVGGVNYYFNVKFGRTTCTKSQPNLDNCPFNDQPKLKEEEFCSFQINEVPWEDKISILNYKCRKV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI0000128D6F","uniref100":"UniRef100_P28325","uniref90":"UniRef90_P28325","uniref50":"UniRef50_P28325","genes":[{"name":{"value":"CST5"}}],"alphafold_very_low_content":0.007042253521126761,"disorder_content":0.07746478873239436,"disprot_consensus":{"full":[{"start":21,"end":31,"type":"D"}],"Structural state":[{"start":21,"end":31,"type":"D"}]}},{"acc":"P43250","sequence":"MELENIVANTVLLKAREGGGGNRKGKSKKWRQMLQFPHISQCEELRLSLERDYHSLCERQPIGRLLFREFCATRPELSRCVAFLDGVAEYEVTPDDKRKACGRQLTQNFLSHTGPDLIPEVPRQLVTNCTQRLEQGPCKDLFQELTRLTHEYLSVAPFADYLDSIYFNRFLQWKWLERQPVTKNTFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGDLKFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSERFSPQARSLCSQLLCKDPAERLGCRGGSAREVKEHPLFKKLNFKRLGAGMLEPPFKPDPQAIYCKDVLDIEQFSTVKGVELEPTDQDFYQKFATGSVPIPWQNEMVETECFQELNVFGLDGSVPPDLDWKGQPPAPPKKGLLQRLFSRQDCCGNCSDSEEELPTRL","alphafold_very_low_content":"0.05555555555555555","creator":"rdavidovic","dataset":[],"date":"2021-01-17T19:17:49.980Z","disprot_id":"DP03187","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":187,"end":448},{"id":"PF00615","name":"Regulator of G protein signaling domain","start":53,"end":170}],"gene3D":[]},"genes":[{"name":{"value":"GRK6","evidences":[],"_id":"685af523b4ac24d5329d970f"},"synonyms":[{"value":"GPRK6","evidences":[],"_id":"685af523b4ac24d5329d9710"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d970e"}],"length":576,"name":"G protein-coupled receptor kinase 6","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":5,"released":"2021_12","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000161B2C","uniref100":"UniRef100_P43250","uniref50":"UniRef50_P43250","uniref90":"UniRef90_P43250","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2ACX","_id":"685af523b4ac24d5329d96fe"}],"curator_id":"rdavidovic","curator_name":"Radoslav Davidović","curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":13,"interaction_partner":[],"reference_html":"The structure of G protein-coupled receptor kinase (GRK)-6 defines a second lineage of GRKs. <i> Lodowski DT, Tesmer VM, Benovic JL, Tesmer JJ. </i> J Biol Chem, 2006","reference_id":"16613860","region_id":"DP03187r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The final model contains residues 24–474 and 492–532 in chain A and residues 24–387, 391–473, and 492–535 in chain B (sup-plemental Fig. S1). Mass spectroscopic analysis of the protein used for crystallization suggests that the missing regions are disordered and not proteolyzed. The missing residues from positions 474/475 to 491 in each chain correspond to the so-called “nucleotide gate” region of the kinase domain (45), which was similarly disordered in structures of GRK2\n\n","_id":"685af523b4ac24d5329d96ff"},{"type":"Curator statement","text":"Despite the statement in the publication that residues 1- 23 are disordered, reviewing of the PDB structure (https://ftp.wwpdb.org/pub/pdb/validation_reports/ac/2acx/2acx_full_validation.pdf.gz) shows three visible residues (14 - 16) in the aforementioned region.","_id":"685af523b4ac24d5329d9700"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-06-07T08:42:23.838Z","_id":"685af523b4ac24d5329d9701"},"version":2,"_id":"685af523b4ac24d5329d96fd","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2ACX","_id":"685af523b4ac24d5329d9703"}],"curator_id":"rdavidovic","curator_name":"Radoslav Davidović","curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":475,"end":491,"interaction_partner":[],"reference_html":"The structure of G protein-coupled receptor kinase (GRK)-6 defines a second lineage of GRKs. <i> Lodowski DT, Tesmer VM, Benovic JL, Tesmer JJ. </i> J Biol Chem, 2006","reference_id":"16613860","region_id":"DP03187r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The final model contains residues 24–474 and 492–532 in chain A and residues 24–387, 391–473, and 492–535 in chain B (sup-plemental Fig. S1). Mass spectroscopic analysis of the protein used for crystallization suggests that the missing regions are disordered and not proteolyzed. The missing residues from positions 474/475 to 491 in each chain correspond to the so-called “nucleotide gate” region of the kinase domain (45), which was similarly disordered in structures of GRK2","_id":"685af523b4ac24d5329d9704"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-06-07T08:44:49.246Z","_id":"685af523b4ac24d5329d9705"},"version":2,"_id":"685af523b4ac24d5329d9702","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2ACX","_id":"685af523b4ac24d5329d970b"}],"curator_id":"rdavidovic","curator_name":"Radoslav Davidović","curator_orcid":"0000-0002-6097-6203","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":536,"end":576,"interaction_partner":[],"reference_html":"The structure of G protein-coupled receptor kinase (GRK)-6 defines a second lineage of GRKs. <i> Lodowski DT, Tesmer VM, Benovic JL, Tesmer JJ. </i> J Biol Chem, 2006","reference_id":"16613860","region_id":"DP03187r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The final model contains residues 24–474 and 492–532 in chain A and residues 24–387, 391–473, and 492–535 in chain B (sup-plemental Fig. S1). Mass spectroscopic analysis of the protein used for crystallization suggests that the missing regions are disordered and not proteolyzed. The missing residues from positions 474/475 to 491 in each chain correspond to the so-called “nucleotide gate” region of the kinase domain (45), which was similarly disordered in structures of GRK2","_id":"685af523b4ac24d5329d970c"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-06-07T08:44:50.334Z","_id":"685af523b4ac24d5329d970d"},"version":2,"_id":"685af523b4ac24d5329d970a","reference_source":"pmid"}],"__v":0,"disorder_content":0.1232638888888889,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"D"},{"start":475,"end":491,"type":"D"},{"start":536,"end":576,"type":"D"}],"Structural state":[{"start":1,"end":13,"type":"D"},{"start":475,"end":491,"type":"D"},{"start":536,"end":576,"type":"D"}]}},{"disprot_id":"DP03190","acc":"P49257","creator":"rdavidovic","date":"2021-01-17T21:05:07.211Z","features":{"pfam":[{"id":"PF03388","name":"Legume-like lectin family","start":43,"end":273}],"gene3D":[]},"length":510,"name":"Protein ERGIC-53","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":176,"end":185,"reference_id":"24498414","reference_source":"pmid","reference_html":"Structural basis for disparate sugar-binding specificities in the homologous cargo receptors ERGIC-53 and VIP36. <i> Satoh T, Suzuki K, Yamaguchi T, Kato K. </i> PLoS One, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"rdavidovic","curator_name":"Radoslav Davidović","curator_orcid":"0000-0002-6097-6203","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3WNX"},{"db":"PDB","id":"3WHU"}],"region_id":"DP03190r001","statement":[{"text":" In the both structures, two loops comprised of residues 155–161 and 176–185 (termed Loops 1 and 2, respectively) of ERGIC-53, which were disordered in the Ca2+-free form.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-07T08:57:18.989Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":176,"end":185,"reference_id":"24498414","reference_source":"pmid","reference_html":"Structural basis for disparate sugar-binding specificities in the homologous cargo receptors ERGIC-53 and VIP36. <i> Satoh T, Suzuki K, Yamaguchi T, Kato K. </i> PLoS One, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"rdavidovic","curator_name":"Radoslav Davidović","curator_orcid":"0000-0002-6097-6203","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03190r002","statement":[{"text":" In the both structures, two loops comprised of residues 155–161 and 176–185 (termed Loops 1 and 2, respectively) of ERGIC-53, which were disordered in the Ca2+-free form.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-07T08:57:19.656Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":176,"end":185,"reference_id":"24498414","reference_source":"pmid","reference_html":"Structural basis for disparate sugar-binding specificities in the homologous cargo receptors ERGIC-53 and VIP36. <i> Satoh T, Suzuki K, Yamaguchi T, Kato K. </i> PLoS One, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"rdavidovic","curator_name":"Radoslav Davidović","curator_orcid":"0000-0002-6097-6203","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03190r003","statement":[{"text":"In the both structures, two loops comprised of residues 155–161 and 176–185 (termed Loops 1 and 2, respectively) of ERGIC-53, which were disordered in the Ca2+-free form.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"3WHT"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-07T08:57:18.117Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":4,"released":"2021_12","sequence":"MAGSRQRGLRARVRPLFCALLLSLGRFVRGDGVGGDPAVALPHRRFEYKYSFKGPHLVQSDGTVPFWAHAGNAIPSSDQIRVAPSLKSQRGSVWTKTKAAFENWEVEVTFRVTGRGRIGADGLAIWYAENQGLEGPVFGSADLWNGVGIFFDSFDNDGKKNNPAIVIIGNNGQIHYDHQNDGASQALASCQRDFRNKPYPVRAKITYYQNTLTVMINNGFTPDKNDYEFCAKVENMIIPAQGHFGISAATGGLADDHDVLSFLTFQLTEPGKEPPTPDKEISEKEKEKYQEEFEHFQQELDKKKEEFQKGHPDLQGQPAEEIFESVGDRELRQVFEGQNRIHLEIKQLNRQLDMILDEQRRYVSSLTEEISKRGAGMPGQHGQITQQELDTVVKTQHEILRQVNEMKNSMSETVRLVSGMQHPGSAGGVYETTQHFIDIKEHLHIVKRDIDNLVQRNMPSNEKPKCPELPPFPSCLSTVHFIIFVVVQTVLFIGYIMYRSQQEAAAKKFF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000016A8AE","uniref100":"UniRef100_P49257","uniref90":"UniRef90_P49257","uniref50":"UniRef50_P49257","genes":[{"name":{"value":"LMAN1"},"synonyms":[{"value":"ERGIC53"},{"value":"F5F8D"}]}],"alphafold_very_low_content":0.13725490196078433,"disorder_content":0.0196078431372549,"disprot_consensus":{"full":[{"start":176,"end":185,"type":"T"}],"Structural state":[{"start":176,"end":185,"type":"D"}],"Structural transition":[{"start":176,"end":185,"type":"T"}],"Molecular function":[{"start":176,"end":185,"type":"F"}]}},{"disprot_id":"DP03191","acc":"P55145","creator":"rdavidovic","date":"2021-01-17T21:49:07.474Z","features":{"pfam":[{"id":"PF10208","name":"ARMET, C-terminal","start":129,"end":171},{"id":"PF20145","name":"ARMET, N-terminal","start":29,"end":125}],"gene3D":[]},"length":182,"name":"Mesencephalic astrocyte-derived neurotrophic factor","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":162,"end":182,"reference_id":"19258449","reference_source":"pmid","reference_html":"The structure of the conserved neurotrophic factors MANF and CDNF explains why they are bifunctional. <i> Parkash V, Lindholm P, Peränen J, Kalkkinen N, Oksanen E, Saarma M, Leppänen VM, Goldman A. </i> Protein Eng Des Sel, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"rdavidovic","curator_name":"Radoslav Davidović","curator_orcid":"0000-0002-6097-6203","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2W51"}],"region_id":"DP03191r003","statement":[{"text":"Due to the poor quality of the MANF electron density maps in the C-terminus region, residues 99–137 were modelled as polyalanine, except for the disulphide bridge between C127 and C130, which was modelled based on density in a sulphur-anomalous map (Fig. 1B). Residues 138–158 are not visible at all.","type":"Results"},{"text":"The region 138-158 in the publication corresponds to region 162-182 because residues 1-24 are not in the crystal.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-07T08:58:05.922Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":4,"released":"2021_12","sequence":"MRRMWATQGLAVALALSVLPGSRALRPGDCEVCISYLGRFYQDLKDRDVTFSPATIENELIKFCREARGKENRLCYYIGATDDAATKIINEVSKPLAHHIPVEKICEKLKKKDSQICELKYDKQIDLSTVDLKKLRVKELKKILDDWGETCKGCAEKSDYIRKINELMPKYAPKAASARTDL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Stress response proteins"],"UniParc":"UPI000015C44A","uniref100":"UniRef100_P55145","uniref90":"UniRef90_P55145","uniref50":"UniRef50_P55145","genes":[{"name":{"value":"MANF"},"synonyms":[{"value":"ARMET"},{"value":"ARP"}]}],"alphafold_very_low_content":0.02197802197802198,"disorder_content":0.11538461538461539,"disprot_consensus":{"full":[{"start":162,"end":182,"type":"D"}],"Structural state":[{"start":162,"end":182,"type":"D"}]}},{"disprot_id":"DP03192","acc":"Q15013","creator":"rdavidovic","date":"2021-01-17T22:04:23.460Z","features":{"pfam":[{"id":"PF06581","name":"Mad1 and Cdc20-bound-Mad2 binding","start":10,"end":274}],"gene3D":[]},"length":274,"name":"MAD2L1-binding protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":36,"end":53,"reference_id":"18022368","reference_source":"pmid","reference_html":"p31comet blocks Mad2 activation through structural mimicry. <i> Yang M, Li B, Tomchick DR, Machius M, Rizo J, Yu H, Luo X. </i> Cell, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"rdavidovic","curator_name":"Radoslav Davidović","curator_orcid":"0000-0002-6097-6203","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2QYF"}],"region_id":"DP03192r001","statement":[{"text":"The N-terminal region (residues 36-53) and the loop connecting helices αAB and αB (residues 97-118) in p31comet could not be located in the final electron density map and are likely disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-02-12T16:53:50.482Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":97,"end":118,"reference_id":"18022368","reference_source":"pmid","reference_html":"p31comet blocks Mad2 activation through structural mimicry. <i> Yang M, Li B, Tomchick DR, Machius M, Rizo J, Yu H, Luo X. </i> Cell, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"rdavidovic","curator_name":"Radoslav Davidović","curator_orcid":"0000-0002-6097-6203","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2QYF"}],"region_id":"DP03192r002","statement":[{"text":"The N-terminal region (residues 36-53) and the loop connecting helices αAB and αB (residues 97-118) in p31comet could not be located in the final electron density map and are likely disordered.","type":"Results"},{"text":"The construct differs from the canonical sequence as Met108 is a modified residue, i.e. a selenomethionine.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-07T08:59:48.444Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MAAPEAEVLSSAAVPDLEWYEKSEETHASQIELLETSSTQEPLNASEAFCPRDCMVPVVFPGPVSQEGCCQFTCELLKHIMYQRQQLPLPYEQLKHFYRKPSPQAEEMLKKKPRATTEVSSRKCQQALAELESVLSHLEDFFARTLVPRVLILLGGNALSPKEFYELDLSLLAPYSVDQSLSTAACLRRLFRAIFMADAFSELQAPPLMGTVVMAQGHRNCGEDWFRPKLNYRVPSRGHKLTVTLSCGRPSIRTTAWEDYIWFQAPVTFKGFRE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI0000000C4A","uniref100":"UniRef100_Q15013","uniref90":"UniRef90_Q15013","uniref50":"UniRef50_Q15013","genes":[{"name":{"value":"MAD2L1BP"},"synonyms":[{"value":"CMT2"},{"value":"KIAA0110"}]}],"alphafold_very_low_content":0.17883211678832117,"disorder_content":0.145985401459854,"disprot_consensus":{"full":[{"start":36,"end":53,"type":"D"},{"start":97,"end":118,"type":"D"}],"Structural state":[{"start":36,"end":53,"type":"D"},{"start":97,"end":118,"type":"D"}]}},{"disprot_id":"DP03193","acc":"P16869","creator":"vpromp","date":"2021-01-18T02:48:43.335Z","features":{"pfam":[{"id":"PF00593","name":"TonB dependent receptor-like, beta-barrel","start":256,"end":700},{"id":"PF07715","name":"TonB-dependent Receptor Plug Domain","start":75,"end":175}],"gene3D":[]},"length":729,"name":"FhuE receptor","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":37,"end":57,"reference_id":"31098021","reference_source":"pmid","reference_html":"Determination of the molecular basis for coprogen import by Gram-negative bacteria. <i> Grinter R, Lithgow T. </i> IUCrJ, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"vpromp","curator_name":"Vasilis J Promponas","curator_orcid":"0000-0003-3352-4831","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6E4V"}],"region_id":"DP03193r001","statement":[{"text":"No direct statement on Intrinsic Disorder is given either in the paper or the supplementary information. However, (i) there exists such information within the PDB file (REMARK 465 MISSING RESIDUES) and (ii) the authors clearly state within the manuscript that the N-terminal signal peptide (AAs 1-36) was removed for protein production.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MLSTQFNRDNQYQAITKPSLLAGCIALALLPSAAFAAPATEETVIVEGSATAPDDGENDYSVTSTSAGTKMQMTQRDIPQSVTIVSQQRMEDQQLQTLGEVMENTLGISKSQADSDRALYYSRGFQIDNYMVDGIPTYFESRWNLGDALSDMALFERVEVVRGATGLMTGTGNPSAAINMVRKHATSREFKGDVSAEYGSWNKERYVADLQSPLTEDGKIRARIVGGYQNNDSWLDRYNSEKTFFSGIVDADLGDLTTLSAGYEYQRIDVNSPTWGGLPRWNTDGSSNSYDRARSTAPDWAYNDKEINKVFMTLKQQFADTWQATLNATHSEVEFDSKMMYVDAYVNKADGMLVGPYSNYGPGFDYVGGTGWNSGKRKVDALDLFADGSYELFGRQHNLMFGGSYSKQNNRYFSSWANIFPDEIGSFYNFNGNFPQTDWSPQSLAQDDTTHMKSLYAATRVTLADPLHLILGARYTNWRVDTLTYSMEKNHTTPYAGLVFDINDNWSTYASYTSIFQPQNDRDSSGKYLAPITGNNYELGLKSDWMNSRLTTTLAIFRIEQDNVAQSTGTPIPGSNGETAYKAVDGTVSKGVEFELNGAITDNWQLTFGATRYIAEDNEGNAVNPNLPRTTVKMFTSYRLPVMPELTVGGGVNWQNRVYTDTVTPYGTFRAEQGSYALVDLFTRYQVTKNFSLQGNVNNLFDKTYDTNVEGSIVYGTPRNFSITGTYQF","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":[],"UniParc":"UPI000016F146","uniref100":"UniRef100_P16869","uniref90":"UniRef90_P16869","uniref50":"UniRef50_P16869","genes":[{"name":{"value":"fhuE"},"olnNames":[{"value":"b1102"},{"value":"JW1088"}]}],"alphafold_very_low_content":0.06035665294924554,"disorder_content":0.02880658436213992,"disprot_consensus":{"full":[{"start":37,"end":57,"type":"D"}],"Structural state":[{"start":37,"end":57,"type":"D"}]}},{"disprot_id":"DP03195","acc":"Q9HAV4","creator":"vpromp","date":"2021-01-18T04:22:37.128Z","features":{"pfam":[{"id":"PF03810","name":"Importin-beta N-terminal domain","start":35,"end":98},{"id":"PF08389","name":"Exportin 1-like protein","start":110,"end":271},{"id":"PF19273","name":"Exportin-5 family","start":313,"end":1164}],"gene3D":[]},"length":1204,"name":"Exportin-5","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":474,"end":490,"reference_id":"19965479","reference_source":"pmid","reference_html":"A high-resolution structure of the pre-microRNA nuclear export machinery. <i> Okada C, Yamashita E, Lee SJ, Shibata S, Katahira J, Nakagawa A, Yoneda Y, Tsukihara T. </i> Science, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"vpromp","curator_name":"Vasilis J Promponas","curator_orcid":"0000-0003-3352-4831","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3A6P"}],"region_id":"DP03195r001","statement":[{"text":"We modeled 1082 of 1204 residues of Exp-5. Several loop regions in the 20 HEAT repeats and 55 residues at the C terminus could not be modeled (details in fig. S1), and 13 residues at the C terminus were modeled as a polyalanine a helix.","type":"Results"},{"text":"The N-terminal residue 1, residues 474-490 in the loop of HEAT12, residues 705-706 in the loop of HEAT14, residues 938-951 in the loop of HEAT17 and residues 980-1069 in the loop between HEAT17 and HEAT18 are disordered in the crystal. Out of 68 C-terminal residues, 55 residues were not modeled because of disordered structure, and 13 residues were built as a poly-alanine α-helix because of high temperature factor.","type":"Supplementary material"},{"text":"This feature corresponds to the IDR in the loop of HEAT10 as shown in Supplementary Fig. S1. The respective author statement, taken from the legend of Fig. S1, erroneously refers to the loop for HEAT12. See Supplementary Fig. S1 for more details.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":938,"end":951,"reference_id":"19965479","reference_source":"pmid","reference_html":"A high-resolution structure of the pre-microRNA nuclear export machinery. <i> Okada C, Yamashita E, Lee SJ, Shibata S, Katahira J, Nakagawa A, Yoneda Y, Tsukihara T. </i> Science, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"vpromp","curator_name":"Vasilis J Promponas","curator_orcid":"0000-0003-3352-4831","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3A6P"}],"region_id":"DP03195r002","statement":[{"text":"We modeled 1082 of 1204 residues of Exp-5. Several loop regions in the 20 HEAT repeats and 55 residues at the C terminus could not be modeled (details in fig. S1), and 13 residues at the C terminus were modeled as a polyalanine a helix.","type":"Results"},{"text":"The N-terminal residue 1, residues 474-490 in the loop of HEAT12, residues 705-706 in the loop of HEAT14, residues 938-951 in the loop of HEAT17 and residues 980-1069 in the loop between HEAT17 and HEAT18 are disordered in the crystal. Out of 68 C-terminal residues, 55 residues were not modeled because of disordered structure, and 13 residues were built as a poly-alanine α-helix because of high temperature factor.","type":"Supplementary material"},{"text":"This feature corresponds to the IDR in the loop of HEAT17.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":980,"end":1009,"reference_id":"19965479","reference_source":"pmid","reference_html":"A high-resolution structure of the pre-microRNA nuclear export machinery. <i> Okada C, Yamashita E, Lee SJ, Shibata S, Katahira J, Nakagawa A, Yoneda Y, Tsukihara T. </i> Science, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"vpromp","curator_name":"Vasilis J Promponas","curator_orcid":"0000-0003-3352-4831","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3A6P"}],"region_id":"DP03195r003","statement":[{"text":"We modeled 1082 of 1204 residues of Exp-5. Several loop regions in the 20 HEAT repeats and 55 residues at the C terminus could not be modeled (details in fig. S1), and 13 residues at the C terminus were modeled as a polyalanine a helix.","type":"Results"},{"text":"he N-terminal residue 1, residues 474-490 in the loop of HEAT12, residues 705-706 in the loop of HEAT14, residues 938-951 in the loop of HEAT17 and residues 980-1069 in the loop between HEAT17 and HEAT18 are disordered in the crystal. Out of 68 C-terminal residues, 55 residues were not modeled because of disordered structure, and 13 residues were built as a poly-alanine α-helix because of high temperature factor.","type":"Supplementary material"},{"text":"This feature corresponds to the IDR in the loop between HEAT17 and HEAT18  as shown in Supplementary Fig. S1. The respective author statement, taken from the legend of Fig. S1, erroneously refers to the range of this IDR as 980-1069. See Supplementary Fig. S1 and the respective PDB entry (PDB:3A6P) for more details.\n","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1137,"end":1191,"reference_id":"19965479","reference_source":"pmid","reference_html":"A high-resolution structure of the pre-microRNA nuclear export machinery. <i> Okada C, Yamashita E, Lee SJ, Shibata S, Katahira J, Nakagawa A, Yoneda Y, Tsukihara T. </i> Science, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"vpromp","curator_name":"Vasilis J Promponas","curator_orcid":"0000-0003-3352-4831","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3A6P"}],"region_id":"DP03195r004","statement":[{"text":"We modeled 1082 of 1204 residues of Exp-5. Several loop regions in the 20 HEAT repeats and 55 residues at the C terminus could not be modeled (details in fig. S1), and 13 residues at the C terminus were modeled as a polyalanine a helix.","type":"Results"},{"text":"The N-terminal residue 1, residues 474-490 in the loop of HEAT12, residues 705-706 in the loop of HEAT14, residues 938-951 in the loop of HEAT17 and residues 980-1069 in the loop between HEAT17 and HEAT18 are disordered in the crystal. Out of 68 C-terminal residues, 55 residues were not modeled because of disordered structure, and 13 residues were built as a poly-alanine α-helix because of high temperature factor.","type":"Supplementary material"},{"text":"This feature corresponds to the 55 disordered residues within the 68 residue long C-terminal segment mentioned in Supplementary Fig. S1.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1180,"end":1204,"reference_id":"30100359","reference_source":"pmid","reference_html":"Structural Basis for Selective Binding of Export Cargoes by Exportin-5. <i> Yamazawa R, Jiko C, Choi S, Park IY, Nakagawa A, Yamashita E, Lee SJ. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"vpromp","curator_name":"Vasilis J Promponas","curator_orcid":"0000-0003-3352-4831","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5YU7"}],"region_id":"DP03195r005","statement":[{"text":"The last 25 C-terminal residues (residues 1,180–1,204) could not be traced in all three Exp-5 structures (Figure 1E).","type":"Results"},{"text":"Figure 1E. The secondary structure of the C-terminal area of Exp-5 alone and Exp-5 complexes. C-terminal 1,180–1,204 residues (light gray) are not shown in all Exp-5 structures.","type":"Figure"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1180,"end":1204,"reference_id":"30100359","reference_source":"pmid","reference_html":"Structural Basis for Selective Binding of Export Cargoes by Exportin-5. <i> Yamazawa R, Jiko C, Choi S, Park IY, Nakagawa A, Yamashita E, Lee SJ. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"vpromp","curator_name":"Vasilis J Promponas","curator_orcid":"0000-0003-3352-4831","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03195r006","statement":[{"text":"On the other hand, the last 25 ‘‘C-terminal end’’ (residues 1,180–1,204) might not be keenly involved in the stabilization of the protein based on X-ray structures because C-terminal end residues showed no electron density for Exp-5 structures at three states: Exp-5 alone, the binary complex, and the ternary complex. Interestingly, the C-terminal end has shown important biological functions involved in the binding and/or recognition of pre-miRNAs as cargo substrate (Melo et al., 2010).","type":"Results"}],"cross_refs":[{"db":"PDB","id":"5YU6"},{"db":"PDB","id":"5YU7"}],"term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":478,"end":490,"reference_id":"30100359","reference_source":"pmid","reference_html":"Structural Basis for Selective Binding of Export Cargoes by Exportin-5. <i> Yamazawa R, Jiko C, Choi S, Park IY, Nakagawa A, Yamashita E, Lee SJ. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"vpromp","curator_name":"Vasilis J Promponas","curator_orcid":"0000-0003-3352-4831","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5YU7"}],"region_id":"DP03195r007","statement":[{"text":"Not explicitly mentioned in the manuscript, but reported within the PDB file (under REMARK 465 MISSING RESIDUES).","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":474,"end":490,"reference_id":"30100359","reference_source":"pmid","reference_html":"Structural Basis for Selective Binding of Export Cargoes by Exportin-5. <i> Yamazawa R, Jiko C, Choi S, Park IY, Nakagawa A, Yamashita E, Lee SJ. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"vpromp","curator_name":"Vasilis J Promponas","curator_orcid":"0000-0003-3352-4831","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5YU6"}],"region_id":"DP03195r008","statement":[{"text":"Not explicitly mentioned in the manuscript, but reported within the PDB file (under REMARK 465 MISSING RESIDUES).","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1167,"end":1179,"reference_id":"30100359","reference_source":"pmid","reference_html":"Structural Basis for Selective Binding of Export Cargoes by Exportin-5. <i> Yamazawa R, Jiko C, Choi S, Park IY, Nakagawa A, Yamashita E, Lee SJ. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"vpromp","curator_name":"Vasilis J Promponas","curator_orcid":"0000-0003-3352-4831","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5YU7"},{"db":"PDB","id":"5YU6"}],"region_id":"DP03195r009","statement":[{"text":"The interaction site of the C-terminal anchor with HEATs 4–9 in Exp-5 alone overlaps with the RanGTP binding site at the N-terminal HEATs of Exp-5 of the binary complex. The interaction between the C-terminal anchor and the N-terminal HEATs of Exp-5 is likely to be important in stabilizing the closed conformation of Exp-5 alone.","type":"Results"},{"text":"The 'C-terminal anchor' segment is ordered in the monomeric form of Exp-5 (5YU7), while it is disordered in the oligomeric forms Exp-5:RanGTP (5YU7), Exp-5:RanGTP:pre-miRNA (PDB:3A6P, PMID:19965479).","type":"Curator statement"},{"text":"\nTo accommodate RanGTP, intramolecular interaction between the C-terminal anchor and HEATs 4–9 of Exp-5 should be removed (Figure 3). For this motion, a notable key region is in the last 24 amino acids at the C-terminal end of Exp-5.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":938,"end":951,"reference_id":"30100359","reference_source":"pmid","reference_html":"Structural Basis for Selective Binding of Export Cargoes by Exportin-5. <i> Yamazawa R, Jiko C, Choi S, Park IY, Nakagawa A, Yamashita E, Lee SJ. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"vpromp","curator_name":"Vasilis J Promponas","curator_orcid":"0000-0003-3352-4831","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5YU6"}],"region_id":"DP03195r010","statement":[{"text":"Not explicitly mentioned in the manuscript, but reported within the PDB file (under REMARK 465 MISSING RESIDUES).","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":10,"released":"2021_12","sequence":"MAMDQVNALCEQLVKAVTVMMDPNSTQRYRLEALKFCEEFKEKCPICVPCGLRLAEKTQVAIVRHFGLQILEHVVKFRWNGMSRLEKVYLKNSVMELIANGTLNILEEENHIKDALSRIVVEMIKREWPQHWPDMLIELDTLSKQGETQTELVMFILLRLAEDVVTFQTLPPQRRRDIQQTLTQNMERIFSFLLNTLQENVNKYQQVKTDTSQESKAQANCRVGVAALNTLAGYIDWVSMSHITAENCKLLEILCLLLNEQELQLGAAECLLIAVSRKGKLEDRKPLMVLFGDVAMHYILSAAQTADGGGLVEKHYVFLKRLCQVLCALGNQLCALLGADSDVETPSNFGKYLESFLAFTTHPSQFLRSSTQMTWGALFRHEILSRDPLLLAIIPKYLRASMTNLVKMGFPSKTDSPSCEYSRFDFDSDEDFNAFFNSSRAQQGEVMRLACRLDPKTSFQMAGEWLKYQLSTFLDAGSVNSCSAVGTGEGSLCSVFSPSFVQWEAMTLFLESVITQMFRTLNREEIPVNDGIELLQMVLNFDTKDPLILSCVLTNVSALFPFVTYRPEFLPQVFSKLFSSVTFETVEESKAPRTRAVRNVRRHACSSIIKMCRDYPQLVLPNFDMLYNHVKQLLSNELLLTQMEKCALMEALVLISNQFKNYERQKVFLEELMAPVASIWLSQDMHRVLSDVDAFIAYVGTDQKSCDPGLEDPCGLNRARMSFCVYSILGVVKRTCWPTDLEEAKAGGFVVGYTSSGNPIFRNPCTEQILKLLDNLLALIRTHNTLYAPEMLAKMAEPFTKALDMLDAEKSAILGLPQPLLELNDSPVFKTVLERMQRFFSTLYENCFHILGKAGPSMQQDFYTVEDLATQLLSSAFVNLNNIPDYRLRPMLRVFVKPLVLFCPPEHYEALVSPILGPLFTYLHMRLSQKWQVINQRSLLCGEDEAADENPESQEMLEEQLVRMLTREVMDLITVCCVSKKGADHSSAPPADGDDEEMMATEVTPSAMAELTDLGKCLMKHEDVCTALLITAFNSLAWKDTLSCQRTTSQLCWPLLKQVLSGTLLADAVTWLFTSVLKGLQMHGQHDGCMASLVHLAFQIYEALRPRYLEIRAVMEQIPEIQKDSLDQFDCKLLNPSLQKVADKRRKDQFKRLIAGCIGKPLGEQFRKEVHIKNLPSLFKKTKPMLETEVLDNDGGGLATIFEP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000006CC97","uniref100":"UniRef100_Q9HAV4","uniref90":"UniRef90_Q9HAV4","uniref50":"UniRef50_Q9HAV4","genes":[{"name":{"value":"XPO5"},"synonyms":[{"value":"KIAA1291"},{"value":"RANBP21"}]}],"alphafold_very_low_content":0.058970099667774084,"disorder_content":0.10714285714285714,"disprot_consensus":{"full":[{"start":474,"end":490,"type":"D"},{"start":938,"end":951,"type":"D"},{"start":980,"end":1009,"type":"D"},{"start":1137,"end":1166,"type":"D"},{"start":1167,"end":1179,"type":"T"},{"start":1180,"end":1204,"type":"D"}],"Structural state":[{"start":474,"end":490,"type":"D"},{"start":938,"end":951,"type":"D"},{"start":980,"end":1009,"type":"D"},{"start":1137,"end":1204,"type":"D"}],"Molecular function":[{"start":1180,"end":1204,"type":"F"}],"Structural transition":[{"start":1167,"end":1179,"type":"T"}]}},{"disprot_id":"DP03196","acc":"Q8N1Q8","creator":"rdavidovic","date":"2021-01-18T15:22:25.656Z","features":{"pfam":[{"id":"PF03061","name":"Thioesterase superfamily","start":155,"end":228}],"gene3D":[]},"length":247,"name":"Acyl-coenzyme A thioesterase THEM5","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":102,"end":111,"reference_id":"22586271","reference_source":"pmid","reference_html":"Acyl coenzyme A thioesterase Them5/Acot15 is involved in cardiolipin remodeling and fatty liver development. <i> Zhuravleva E, Gut H, Hynx D, Marcellin D, Bleck CK, Genoud C, Cron P, Keusch JJ, Dummler B, Esposti MD, Hemmings BA. </i> Mol Cell Biol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"rdavidovic","curator_name":"Radoslav Davidović","curator_orcid":"0000-0002-6097-6203","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4AE7"}],"region_id":"DP03196r001","statement":[{"text":"Them4 and Them5 proteins contain a highly variable sequence stretch (ca. residues 83 to 109 and ca. residues 91 to 114 for Them4 and Them5, respectively) that is partially disordered in both crystal structures.","type":"Results"},{"text":"PDB structure (https://files.rcsb.org/pub/pdb/validation_reports/ae/4ae7/4ae7_full_validation.pdf) shows that region 102-111 is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-07T08:54:27.698Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MIRRCFQVAARLGHHRGLLEAPRILPRLNPASAFGSSTDSMFSRFLPEKTDLKDYALPNASWCSDMLSLYQEFLEKTKSSGWIKLPSFKSNRDHIRGLKLPSGLAVSSDKGDCRIFTRCIQVEGQGFEYVIFFQPTQKKSVCLFQPGSYLEGPPGFAHGGSLAAMMDETFSKTAFLAGEGLFTLSLNIRFKNLIPVDSLVVMDVELDKIEDQKLYMSCIAHSRDQQTVYAKSSGVFLQLQLEEESPQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI0000071FE4","uniref100":"UniRef100_Q8N1Q8","uniref90":"UniRef90_Q8N1Q8","uniref50":"UniRef50_Q8N1Q8","genes":[{"name":{"value":"THEM5"},"synonyms":[{"value":"ACOT15"}]}],"alphafold_very_low_content":0.13765182186234817,"disorder_content":0.04048582995951417,"disprot_consensus":{"full":[{"start":102,"end":111,"type":"D"}],"Structural state":[{"start":102,"end":111,"type":"D"}]}},{"disprot_id":"DP03197","acc":"P41209","creator":"achasapi","date":"2021-01-18T19:58:33.163Z","features":{"pfam":[{"id":"PF13499","name":"EF-hand domain pair","start":31,"end":94},{"id":"PF13499","name":"EF-hand domain pair","start":103,"end":167}],"gene3D":[]},"length":172,"name":"Centrin-1","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":1,"end":24,"reference_id":"29037133","reference_source":"pmid","reference_html":"Crystal Structure of Wild-Type Centrin 1 from Mus musculus Occupied by Ca2. <i> Kim SY, Kim DS, Hong JE, Park JH. </i> Biochemistry (Mosc), 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"achasapi","curator_name":"Anastasia Chasapi","curator_orcid":"0000-0003-1986-5007","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5D43"}],"region_id":"DP03197r001","statement":[{"text":"Twenty-five amino acids from the N-terminus in the crystal structure, which was interpretable and used to build a structural model of residues L26 to Y172, were not modeled because of high flexibility. ","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MASTFRKSNVASTSYKRKVGPKPELTEDQKQEVREAFDLFDSDGSGTIDVKELKVAMRALGFEPRKEEMKKMISEVDKEATGKISFNDFLAVMTQKMAEKDTKEEILKAFRLFDDDETGKISFKNLKRVANELGESLTDEELQEMIDEADRDGDGEVNEEEFLKIMKKTNLY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"dataset":[],"UniParc":"UPI000000410E","uniref100":"UniRef100_P41209","uniref90":"UniRef90_P41209","uniref50":"UniRef50_P41209","genes":[{"name":{"value":"Cetn1","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:1347086","url":"http://www.informatics.jax.org/marker/MGI:1347086"}}]},"synonyms":[{"value":"Calt"}]}],"alphafold_very_low_content":0.09883720930232558,"disorder_content":0.13953488372093023,"disprot_consensus":{"full":[{"start":1,"end":24,"type":"D"}],"Structural state":[{"start":1,"end":24,"type":"D"}]}},{"disprot_id":"DP03198","acc":"P62696","creator":"achasapi","date":"2021-01-18T20:35:19.019Z","features":{"pfam":[{"id":"PF00030","name":"Beta/Gamma crystallin","start":18,"end":100},{"id":"PF00030","name":"Beta/Gamma crystallin","start":108,"end":190}],"gene3D":[]},"length":205,"name":"Beta-crystallin B2","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":1,"end":14,"reference_id":"11090271","reference_source":"pmid","reference_html":"The N-terminal domain of betaB2-crystallin resembles the putative ancestral homodimer. <i> Clout NJ, Basak A, Wieligmann K, Bateman OA, Jaenicke R, Slingsby C. </i> J Mol Biol, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"achasapi","curator_name":"Anastasia Chasapi","curator_orcid":"0000-0003-1986-5007","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1E7N"}],"region_id":"DP03198r001","statement":[{"text":"However, it was not possible to model the first 13 residues of the N-terminal extension of βB2-N, nor linker residues 85 to 88, in either molecule of βB2-N, suggesting a disordered conformation for the N-terminal extension and residues 85 to 88.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MASDHQTQAGKPQPLNPKIIIFEQENFQGHSHELSGPCPNLKETGMEKAGSVLVQAGPWVGYEQANCKGEQFVFEKGEYPRWDSWTSSRRTDSLSSLRPIKVDSQEHKIILYENPNFTGKKMEIVDDDVPSFHAHGYQEKVSSVRVQSGTWVGYQYPGYRGLQYLLEKGDYKDNSDFGAPHPQVQSVRRIRDMQWHQRGAFHPSS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"dataset":[],"UniParc":"UPI0000003F4B","uniref100":"UniRef100_P62696","uniref90":"UniRef90_P62696","uniref50":"UniRef50_P02522","genes":[{"name":{"value":"Crybb2"}}],"alphafold_very_low_content":0.11219512195121951,"disorder_content":0.06829268292682927,"disprot_consensus":{"full":[{"start":1,"end":14,"type":"D"}],"Structural state":[{"start":1,"end":14,"type":"D"}]}},{"disprot_id":"DP03199","acc":"P00749","creator":"npalopoli","date":"2021-01-18T22:27:59.180Z","features":{"pfam":[{"id":"PF00051","name":"Kringle domain","start":70,"end":151},{"id":"PF00089","name":"Trypsin","start":179,"end":419}],"gene3D":[]},"length":431,"name":"Urokinase-type plasminogen activator","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":21,"end":30,"reference_id":"16979660","reference_source":"pmid","reference_html":"Structural basis of interaction between urokinase-type plasminogen activator and its receptor. <i> Barinka C, Parry G, Callahan J, Shaw DE, Kuo A, Bdeir K, Cines DB, Mazar A, Lubkowski J. </i> J Mol Biol, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"npalopoli","curator_name":"Nicolás Palopoli","curator_orcid":"0000-0001-7925-6436","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2I9A"},{"db":"PDB","id":"2I9B"}],"region_id":"DP03199r001","statement":[{"text":"Due to a disorder, residues 1–10 and 133–143 are not modeled in the final structure.","type":"Methods"},{"text":"Additionally, due to a lack of the interpretable electron density peaks, residues 1–10 and 133–143 of ATF and 108–111, 134–138, and 248–251 of suPAR 2345 are not included in the final model.","type":"Methods"},{"text":"The disordered region described in the publication comprises residues 1-10 which maps to region 21-30 of the UniProt amino acid sequence, since the latter includes a natural signal peptide (1-20) that is cleaved in the mature protein.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-25T13:46:29.195Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":153,"end":163,"reference_id":"16979660","reference_source":"pmid","reference_html":"Structural basis of interaction between urokinase-type plasminogen activator and its receptor. <i> Barinka C, Parry G, Callahan J, Shaw DE, Kuo A, Bdeir K, Cines DB, Mazar A, Lubkowski J. </i> J Mol Biol, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"npalopoli","curator_name":"Nicolás Palopoli","curator_orcid":"0000-0001-7925-6436","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2I9A"},{"db":"PDB","id":"2I9B"}],"region_id":"DP03199r002","statement":[{"text":"Due to a disorder, residues 1–10 and 133–143 are not modeled in the final structure.","type":"Methods"},{"text":"Additionally, due to a lack of the interpretable electron density peaks, residues 1–10 and 133–143 of ATF and 108–111, 134–138, and 248–251 of suPAR 2345 are not included in the final model.","type":"Methods"},{"text":"The disordered region described in the publication comprises residues 133-143 which maps to region 153-163 of the UniProt amino acid sequence, since the latter includes a natural signal peptide (1-20) that is cleaved in the mature protein.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-25T13:46:28.434Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MRALLARLLLCVLVVSDSKGSNELHQVPSNCDCLNGGTCVSNKYFSNIHWCNCPKKFGGQHCEIDKSKTCYEGNGHFYRGKASTDTMGRPCLPWNSATVLQQTYHAHRSDALQLGLGKHNYCRNPDNRRRPWCYVQVGLKLLVQECMVHDCADGKKPSSPPEELKFQCGQKTLRPRFKIIGGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVISATHCFIDYPKKEDYIVYLGRSRLNSNTQGEMKFEVENLILHKDYSADTLAHHNDIALLKIRSKEGRCAQPSRTIQTICLPSMYNDPQFGTSCEITGFGKENSTDYLYPEQLKMTVVKLISHRECQQPHYYGSEVTTKMLCAADPQWKTDSCQGDSGGPLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLPWIRSHTKEENGLAL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000137E15","uniref100":"UniRef100_P00749","uniref90":"UniRef90_P00749","uniref50":"UniRef50_P00749","genes":[{"name":{"value":"PLAU","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9052","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9052"}}]}}],"alphafold_very_low_content":0.11136890951276102,"disorder_content":0.048723897911832945,"disprot_consensus":{"full":[{"start":21,"end":30,"type":"D"},{"start":153,"end":163,"type":"D"}],"Structural state":[{"start":21,"end":30,"type":"D"},{"start":153,"end":163,"type":"D"}]}},{"disprot_id":"DP03200","acc":"P04711","creator":"npalopoli","date":"2021-01-18T23:32:14.412Z","features":{"pfam":[{"id":"PF00311","name":"Phosphoenolpyruvate carboxylase","start":39,"end":970}],"gene3D":[]},"length":970,"name":"Phosphoenolpyruvate carboxylase 1","ncbi_taxon_id":4577,"organism":"Zea mays","regions":[{"start":124,"end":140,"reference_id":"12467579","reference_source":"pmid","reference_html":"Crystal structures of C4 form maize and quaternary complex of E. coli phosphoenolpyruvate carboxylases. <i> Matsumura H, Xie Y, Shirakata S, Inoue T, Yoshinaga T, Ueno Y, Izui K, Kai Y. </i> Structure, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"npalopoli","curator_name":"Nicolás Palopoli","curator_orcid":"0000-0001-7925-6436","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1JQO"}],"region_id":"DP03200r001","statement":[{"text":"The N-terminal region (residues 1–34) and three loops comprising residues 124–140, 761–768, and 928–935 in the structure of ZmPEPC show little or no electron density (Figure 1E). Since there was no significant cleavage, as judged by SDS-PAGE [17], it is apparent that the three loops exist in multiple conformations, whereas only the N-terminal region is partially truncated.","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-25T13:26:32.995Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MASTKAPGPGEKHHSIDAQLRQLVPGKVSEDDKLIEYDALLVDRFLNILQDLHGPSLREFVQECYEVSADYEGKGDTTKLGELGAKLTGLAPADAILVASSILHMLNLANLAEEVQIAHRRRNSKLKKGGFADEGSATTESDIEETLKRLVSEVGKSPEEVFEALKNQTVDLVFTAHPTQSARRSLLQKNARIRNCLTQLNAKDITDDDKQELDEALQREIQAAFRTDEIRRAQPTPQAEMRYGMSYIHETVWKGVPKFLRRVDTALKNIGINERLPYNVSLIRFSSWMGGDRDGNPRVTPEVTRDVCLLARMMAANLYIDQIEELMFELSMWRCNDELRVRAEELHSSSGSKVTKYYIEFWKQIPPNEPYRVILGHVRDKLYNTRERARHLLASGVSEISAESSFTSIEEFLEPLELCYKSLCDCGDKAIADGSLLDLLRQVFTFGLSLVKLDIRQESERHTDVIDAITTHLGIGSYREWPEDKRQEWLLSELRGKRPLLPPDLPQTDEIADVIGAFHVLAELPPDSFGPYIISMATAPSDVLAVELLQRECGVRQPLPVVPLFERLADLQSAPASVERLFSVDWYMDRIKGKQQVMVGYSDSGKDAGRLSAAWQLYRAQEEMAQVAKRYGVKLTLFHGRGGTVGRGGGPTHLAILSQPPDTINGSIRVTVQGEVIEFCFGEEHLCFQTLQRFTAATLEHGMHPPVSPKPEWRKLMDEMAVVATEEYRSVVVKEARFVEYFRSATPETEYGRMNIGSRPAKRRPGGGITTLRAIPWIFSWTQTRFHLPVWLGVGAAFKFAIDKDVRNFQVLKEMYNEWPFFRVTLDLLEMVFAKGDPGIAGLYDELLVAEELKPFGKQLRDKYVETQQLLLQIAGHKDILEGDPFLKQGLVLRNPYITTLNVFQAYTLKRIRDPNFKVTPQPPLSKEFADENKPAGLVKLNPASEYPPGLEDTLILTMKGIAAGMQNTG","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","PACMAD clade","Panicoideae","Andropogonodae","Andropogoneae","Tripsacinae","Zea"],"dataset":[],"UniParc":"UPI0000113214","uniref100":"UniRef100_P04711","uniref90":"UniRef90_P04711","uniref50":"UniRef50_Q9MAH0","genes":[{"name":{"value":"PEP1"},"synonyms":[{"value":"PPC"}]}],"alphafold_very_low_content":0.015463917525773196,"disorder_content":0.01752577319587629,"disprot_consensus":{"full":[{"start":124,"end":140,"type":"D"}],"Structural state":[{"start":124,"end":140,"type":"D"}]}},{"disprot_id":"DP03201","acc":"Q96CV9","creator":"vpromp","date":"2021-01-19T00:19:10.996Z","features":{"pfam":[{"id":"PF11577","name":"NF-kappa-B essential modulator NEMO","start":37,"end":104},{"id":"PF16516","name":"Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator","start":408,"end":506},{"id":"PF18414","name":"C2H2 type zinc-finger","start":551,"end":576}],"gene3D":[]},"length":577,"name":"Optineurin","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":416,"end":442,"reference_id":"27552911","reference_source":"pmid","reference_html":"Linear ubiquitination is involved in the pathogenesis of optineurin-associated amyotrophic lateral sclerosis. <i> Nakazawa S, Oikawa D, Ishii R, Ayaki T, Takahashi H, Takeda H, Ishitani R, Kamei K, Takeyoshi I, Kawakami H, Iwai K, Hatada I, Sawasaki T, Ito H, Nureki O, Tokunaga F. </i> Nat Commun, 2016","date":"2022-05-30T14:30:46.499Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":3,"cross_refs":[{"db":"PDB","id":"5B83"}],"region_id":"DP03201r001","statement":[{"text":"Although we used the OPTN CC2-UBAN region for crystallization experiments, the electron density for the majority of the CC2 region in all OPTN molecules was very weak and thus we modelled only the UBAN motif with some extensions on both sides (residues 445–505 for the longest chain).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","sequence_construct":"GPLGSHMEKVDRAVLKELSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETMTILRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAVLLKENDAFEDGG"}],"regions_counter":4,"released":"2022_06","sequence":"MSHQPLSCLTEKEDSPSESTGNGPPHLAHPNLDTFTPEELLQQMKELLTENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERQFFEIQSKEAKERLMALSHENEKLKEELGKLKGKSERSSEDPTDDSRLPRAEAEQEKDQLRTQVVRLQAEKADLLGIVSELQLKLNSSGSSEDSFVEIRMAEGEAEGSVKEIKHSPGPTRTVSTGTALSKYRSRSADGAKNYFEHEELTVSQLLLCLREGNQKVERLEVALKEAKERVSDFEKKTSNRSEIETQTEGSTEKENDEEKGPETVGSEVEALNLQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSAIPSELNEKQELVYTNKKLELQVESMLSEIKMEQAKTEDEKSKLTVLQMTHNKLLQEHNNALKTIEELTRKESEKVDRAVLKELSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETMTILRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAVLLKENDAFEDGGRQSLMEMQSRHGARTSDSDQQAYLVQRGAEDRDWRQQRNIPIHSCPKCGEVLPDIDTLQIHVMDCII","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins","Age-related disorders proteins"],"UniParc":"UPI0000073FF7","uniref100":"UniRef100_Q96CV9","uniref90":"UniRef90_Q96CV9","uniref50":"UniRef50_Q96CV9","genes":[{"name":{"value":"OPTN"},"synonyms":[{"value":"FIP2"},{"value":"GLC1E"},{"value":"HIP7"},{"value":"HYPL"},{"value":"NRP"}]}],"alphafold_very_low_content":0.22876949740034663,"disorder_content":0.04679376083188908,"disprot_consensus":{"full":[{"start":416,"end":442,"type":"D"}],"Structural state":[{"start":416,"end":442,"type":"D"}]}},{"disprot_id":"DP03203","acc":"P55210","creator":"npalopoli","date":"2021-01-19T01:42:25.331Z","features":{"pfam":[{"id":"PF00656","name":"Caspase domain","start":68,"end":300}],"gene3D":[]},"length":303,"name":"Caspase-7","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":197,"end":210,"reference_id":"19530232","reference_source":"pmid","reference_html":"L2' loop is critical for caspase-7 active site formation. <i> Witkowski WA, Hardy JA. </i> Protein Sci, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"npalopoli","curator_name":"Nicolás Palopoli","curator_orcid":"0000-0001-7925-6436","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3H1P"}],"region_id":"DP03203r001","statement":[{"text":"The final refined model contains residues 58–196, 211–303 for chain A and 57–196, 211–304 for chain B.","type":"Methods"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-02-18T16:59:00.307Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":197,"end":211,"reference_id":"10873833","reference_source":"pmid","reference_html":"The structures of caspases-1, -3, -7 and -8 reveal the basis for substrate and inhibitor selectivity. <i> Wei Y, Fox T, Chambers SP, Sintchak J, Coll JT, Golec JM, Swenson L, Wilson KP, Charifson PS. </i> Chem Biol, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"npalopoli","curator_name":"Nicolás Palopoli","curator_orcid":"0000-0001-7925-6436","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1F1J"}],"region_id":"DP03203r002","statement":[{"text":"The refined model of Csp7 contains a complete catalytic unit comprising two p20–p10 heterodimers. The p20 and p10 polypeptide chains are composed of residues 57–196 and 212–302, respectively. ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-02-18T17:03:49.778Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":197,"end":210,"reference_id":"11257231","reference_source":"pmid","reference_html":"Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain. <i> Huang Y, Park YC, Rich RL, Segal D, Myszka DG, Wu H. </i> Cell, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"npalopoli","curator_name":"Nicolás Palopoli","curator_orcid":"0000-0001-7925-6436","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1I4O"}],"region_id":"DP03203r003","statement":[{"text":"The final atomic model contains residues 55–196 and 211–303 from the first caspase-7 protomer, residues 58–196 and 211–303 from the second caspase-7 protomer, and residues 134–150 for both bound XIAP linkers.","type":"Methods"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-02-18T17:08:10.775Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2021_12","sequence":"MADDQGCIEEQGVEDSANEDSVDAKPDRSSFVPSLFSKKKKNVTMRSIKTTRDRVPTYQYNMNFEKLGKCIIINNKNFDKVTGMGVRNGTDKDAEALFKCFRSLGFDVIVYNDCSCAKMQDLLKKASEEDHTNAACFACILLSHGEENVIYGKDGVTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQADSGPINDTDANPRYKIPVEADFLFAYSTVPGYYSWRSPGRGSWFVQALCSILEEHGKDLEIMQILTRVNDRVARHFESQSDDPHFHEKKQIPCVVSMLTKELYFSQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000003AEFD","uniref100":"UniRef100_P55210","uniref90":"UniRef90_P55210","uniref50":"UniRef50_P55210","genes":[{"name":{"value":"CASP7"},"synonyms":[{"value":"MCH3","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8521391","url":"http://www.ncbi.nlm.nih.gov/pubmed/8521391","alternativeUrl":"https://europepmc.org/abstract/MED/8521391"}}]}]}],"alphafold_very_low_content":0.20132013201320131,"disorder_content":0.04950495049504951,"disprot_consensus":{"full":[{"start":197,"end":211,"type":"D"}],"Structural state":[{"start":197,"end":211,"type":"D"}]}},{"disprot_id":"DP03204","acc":"Q16629","creator":"eschad","date":"2021-01-20T11:05:12.407Z","features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":13,"end":77}],"gene3D":[]},"length":238,"name":"Serine/arginine-rich splicing factor 7","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":81,"end":98,"reference_id":"17036044","reference_source":"pmid","reference_html":"Molecular basis of RNA recognition and TAP binding by the SR proteins SRp20 and 9G8. <i> Hargous Y, Hautbergue GM, Tintaru AM, Skrisovska L, Golovanov AP, Stevenin J, Lian LY, Wilson SA, Allain FH. </i> EMBO J, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2HVZ"}],"region_id":"DP03204r001","statement":[{"text":"The narrow signal linewidth and small\nchemical shift dispersion observed in the 1\nH-15N-correlated\n(HSQC) NMR spectrum reveal that the C-terminal argininerich region, required for TAP binding (Figure 1A and below),\nis unstructured and highly flexible.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":81,"end":98,"reference_id":"17036044","reference_source":"pmid","reference_html":"Molecular basis of RNA recognition and TAP binding by the SR proteins SRp20 and 9G8. <i> Hargous Y, Hautbergue GM, Tintaru AM, Skrisovska L, Golovanov AP, Stevenin J, Lian LY, Wilson SA, Allain FH. </i> EMBO J, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006077","ec_ontology":"ECO","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"Q9UBU9","partner_start":null,"partner_end":null}],"region_id":"DP03204r002","statement":[{"text":"A similar analysis was undertaken with 9G8 and it was\nshown that a short arginine-rich peptide (aa 81–98), which\nlies between the RRM and the zinc-knuckle, was sufficient\nfor interaction with TAP-p15 (Figure 4D–F). Within this\nsequence, the arginine dipeptides at positions 87, 88 and\n97, 98 were required for the interaction, whereas Arg 90, 93\nwere not. These data indicate that 9G8 and SRp20 harbor\na TAP-binding motif, which consists of an arginine-rich\npeptide, which from the NMR analysis, appears flexible and\nis tightly juxtaposed with their RRMs.","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":123,"end":176,"reference_id":"https://mobidb.org/Q16629","reference_source":"mobidb","reference_html":"An Entry Referenced from MobiDB","date":"2022-02-14T09:00:00.000Z","curator_id":"amonzon","curator_name":"Alex Monzon","curator_orcid":"0000-0003-0362-8218","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007759","ec_ontology":"ECO","ec_name":"curator inference from database used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03204r003","statement":[{"text":"This poly-E region is inferred by the curator to be disordered, based on MobiDB-Lite and according to experimental evidence demonstrating that poly-E repeats display random-coil-like conformation (PMID:16949547)","type":"Curator statement"}],"ec_go":"IC","disprot_namespace":"Structural state"},{"start":200,"end":217,"reference_id":"https://mobidb.org/Q16629","reference_source":"mobidb","reference_html":"An Entry Referenced from MobiDB","date":"2022-02-14T09:00:00.000Z","curator_id":"amonzon","curator_name":"Alex Monzon","curator_orcid":"0000-0003-0362-8218","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007759","ec_ontology":"ECO","ec_name":"curator inference from database used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03204r004","statement":[{"text":"This poly-E region is inferred by the curator to be disordered, based on MobiDB-Lite and according to experimental evidence demonstrating that poly-E repeats display random-coil-like conformation (PMID:16949547)","type":"Curator statement"}],"ec_go":"IC","disprot_namespace":"Structural state"}],"regions_counter":4,"released":"2021_12","sequence":"MSRYGRYGGETKVYVGNLGTGAGKGELERAFSYYGPLRTVWIARNPPGFAFVEFEDPRDAEDAVRGLDGKVICGSRVRVELSTGMPRRSRFDRPPARRPFDPNDRCYECGEKGHYAYDCHRYSRRRRSRSRSRSHSRSRGRRYSRSRSRSRGRRSRSASPRRSRSISLRRSRSASLRRSRSGSIKGSRYFQSPSRSRSRSRSISRPRSSRSKSRSPSPKRSRSPSGSPRRSASPERMD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000000D853","uniref100":"UniRef100_Q16629","uniref90":"UniRef90_Q16629","uniref50":"UniRef50_Q16629","genes":[{"name":{"value":"SRSF7"},"synonyms":[{"value":"SFRS7"}]}],"alphafold_very_low_content":0.3949579831932773,"disorder_content":0.37815126050420167,"disprot_consensus":{"full":[{"start":81,"end":98,"type":"D"},{"start":123,"end":176,"type":"D"},{"start":200,"end":217,"type":"D"}],"Structural state":[{"start":81,"end":98,"type":"D"},{"start":123,"end":176,"type":"D"},{"start":200,"end":217,"type":"D"}],"Molecular function":[{"start":81,"end":98,"type":"F"}]}},{"disprot_id":"DP03205","acc":"O95696","creator":"eschad","date":"2021-01-20T15:13:20.008Z","features":{"pfam":[{"id":"PF00439","name":"Bromodomain","start":572,"end":653},{"id":"PF00855","name":"PWWP domain","start":931,"end":1037},{"id":"PF10513","name":"Enhancer of polycomb-like","start":47,"end":196},{"id":"PF13831","name":"PHD-finger","start":229,"end":261},{"id":"PF13832","name":"PHD-zinc-finger like domain","start":270,"end":388}],"gene3D":[]},"length":1058,"name":"Bromodomain-containing protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":63,"end":80,"reference_id":"28334966","reference_source":"pmid","reference_html":"Structural and mechanistic insights into regulation of HBO1 histone acetyltransferase activity by BRPF2. <i> Tao Y, Zhong C, Zhu J, Xu S, Ding J. </i> Nucleic Acids Res, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03205r001","statement":[{"text":"However, only the central portion of the\nBRPF2 fragment (residues 39–62) is visible; both the Nterminal and C-terminal regions are disordered.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"5GK9"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-01-22T11:07:40.250Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_12","sequence":"MRRKGRCHRGSAARHPSSPCSVKHSPTRETLTYAQAQRMVEIEIEGRLHRISIFDPLEIILEDDLTAQEMSECNSNKENSERPPVCLRTKRHKNNRVKKKNEALPSAHGTPASASALPEPKVRIVEYSPPSAPRRPPVYYKFIEKSAEELDNEVEYDMDEEDYAWLEIVNEKRKGDCVPAVSQSMFEFLMDRFEKESHCENQKQGEQQSLIDEDAVCCICMDGECQNSNVILFCDMCNLAVHQECYGVPYIPEGQWLCRHCLQSRARPADCVLCPNKGGAFKKTDDDRWGHVVCALWIPEVGFANTVFIEPIDGVRNIPPARWKLTCYLCKQKGVGACIQCHKANCYTAFHVTCAQKAGLYMKMEPVKELTGGGTTFSVRKTAYCDVHTPPGCTRRPLNIYGDVEMKNGVCRKESSVKTVRSTSKVRKKAKKAKKALAEPCAVLPTVCAPYIPPQRLNRIANQVAIQRKKQFVERAHSYWLLKRLSRNGAPLLRRLQSSLQSQRSSQQRENDEEMKAAKEKLKYWQRLRHDLERARLLIELLRKREKLKREQVKVEQVAMELRLTPLTVLLRSVLDQLQDKDPARIFAQPVSLKEVPDYLDHIKHPMDFATMRKRLEAQGYKNLHEFEEDFDLIIDNCMKYNARDTVFYRAAVRLRDQGGVVLRQARREVDSIGLEEASGMHLPERPAAAPRRPFSWEDVDRLLDPANRAHLGLEEQLRELLDMLDLTCAMKSSGSRSKRAKLLKKEIALLRNKLSQQHSQPLPTGPGLEGFEEDGAALGPEAGEEVLPRLETLLQPRKRSRSTCGDSEVEEESPGKRLDAGLTNGFGGARSEQEPGGGLGRKATPRRRCASESSISSSNSPLCDSSFNAPKCGRGKPALVRRHTLEDRSELISCIENGNYAKAARIAAEVGQSSMWISTDAAASVLEPLKVVWAKCSGYPSYPALIIDPKMPRVPGHHNGVTIPAPPLDVLKIGEHMQTKSDEKLFLVLFFDNKRSWQWLPKSKMVPLGIDETIDKLKMMEGRNSSIRKAVRIAFDRAMNHLSRVHGEPTSDLSDID","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI0000126ACA","uniref100":"UniRef100_O95696","uniref90":"UniRef90_O95696","uniref50":"UniRef50_O95696","genes":[{"name":{"value":"BRD1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16387653","url":"http://www.ncbi.nlm.nih.gov/pubmed/16387653","alternativeUrl":"https://europepmc.org/abstract/MED/16387653"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:1102","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:1102"}}]},"synonyms":[{"value":"BRL","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10602503","url":"http://www.ncbi.nlm.nih.gov/pubmed/10602503","alternativeUrl":"https://europepmc.org/abstract/MED/10602503"}}]},{"value":"BRPF2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16387653","url":"http://www.ncbi.nlm.nih.gov/pubmed/16387653","alternativeUrl":"https://europepmc.org/abstract/MED/16387653"}}]}]}],"alphafold_very_low_content":0.2523629489603025,"disorder_content":0.017013232514177693,"disprot_consensus":{"full":[{"start":63,"end":80,"type":"D"}],"Structural state":[{"start":63,"end":80,"type":"D"}]}},{"disprot_id":"DP03206","acc":"Q8IYB8","creator":"eschad","date":"2021-01-22T14:16:14.762Z","features":{"pfam":[{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":364,"end":474},{"id":"PF12513","name":"ATP-dependent RNA helicase SUV3 C-terminal domain","start":625,"end":671},{"id":"PF18114","name":"Suv3 helical N-terminal domain","start":62,"end":179},{"id":"PF18147","name":"Suv3 C-terminal domain 1","start":558,"end":598},{"id":"PF22527","name":"DEXQ-box helicase domain of Suv3","start":188,"end":345}],"gene3D":[]},"length":786,"name":"ATP-dependent RNA helicase SUPV3L1, mitochondrial","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":47,"end":57,"reference_id":"22101826","reference_source":"pmid","reference_html":"Human Suv3 protein reveals unique features among SF2 helicases. <i> Jedrzejczak R, Wang J, Dauter M, Szczesny RJ, Stepien PP, Dauter Z. </i> Acta Crystallogr D Biol Crystallogr, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3RC8"},{"db":"PDB","id":"3RC3"}],"region_id":"DP03206r001","statement":[{"text":"The construct of hSuv3 used for crystallization contained\nresidues 47–722 of the complete genome sequence plus an\nadditional Gly at the N-terminus. In both crystal structures\nfragments of the N- and C-termini (residues 46–57 and 690–\n722), as well as two other fragments of the chain (73–86 and\n446–456), are disordered and are not visible in the electrondensity map.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-01T12:18:04.311Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":73,"end":86,"reference_id":"22101826","reference_source":"pmid","reference_html":"Human Suv3 protein reveals unique features among SF2 helicases. <i> Jedrzejczak R, Wang J, Dauter M, Szczesny RJ, Stepien PP, Dauter Z. </i> Acta Crystallogr D Biol Crystallogr, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3RC8"},{"db":"PDB","id":"3RC3"}],"region_id":"DP03206r002","statement":[{"text":"The construct of hSuv3 used for crystallization contained\nresidues 47–722 of the complete genome sequence plus an\nadditional Gly at the N-terminus. In both crystal structures\nfragments of the N- and C-termini (residues 46–57 and 690–\n722), as well as two other fragments of the chain (73–86 and\n446–456), are disordered and are not visible in the electrondensity map.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-01T12:18:03.315Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":446,"end":456,"reference_id":"22101826","reference_source":"pmid","reference_html":"Human Suv3 protein reveals unique features among SF2 helicases. <i> Jedrzejczak R, Wang J, Dauter M, Szczesny RJ, Stepien PP, Dauter Z. </i> Acta Crystallogr D Biol Crystallogr, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3RC8"},{"db":"PDB","id":"3RC3"}],"region_id":"DP03206r003","statement":[{"text":"The construct of hSuv3 used for crystallization contained\nresidues 47–722 of the complete genome sequence plus an\nadditional Gly at the N-terminus. In both crystal structures\nfragments of the N- and C-termini (residues 46–57 and 690–\n722), as well as two other fragments of the chain (73–86 and\n446–456), are disordered and are not visible in the electrondensity map.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-01T12:18:02.449Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":690,"end":722,"reference_id":"22101826","reference_source":"pmid","reference_html":"Human Suv3 protein reveals unique features among SF2 helicases. <i> Jedrzejczak R, Wang J, Dauter M, Szczesny RJ, Stepien PP, Dauter Z. </i> Acta Crystallogr D Biol Crystallogr, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"eschad","curator_name":"Eva Schad","curator_orcid":"0000-0002-3006-2910","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3RC8"},{"db":"PDB","id":"3RC3"}],"region_id":"DP03206r004","statement":[{"text":"The construct of hSuv3 used for crystallization contained\nresidues 47–722 of the complete genome sequence plus an\nadditional Gly at the N-terminus. In both crystal structures\nfragments of the N- and C-termini (residues 46–57 and 690–\n722), as well as two other fragments of the chain (73–86 and\n446–456), are disordered and are not visible in the electrondensity map.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-01T12:17:32.064Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":4,"released":"2021_12","sequence":"MSFSRALLWARLPAGRQAGHRAAICSALRPHFGPFPGVLGQVSVLATASSSASGGSKIPNTSLFVPLTVKPQGPSADGDVGAELTRPLDKNEVKKVLDKFYKRKEIQKLGADYGLDARLFHQAFISFRNYIMQSHSLDVDIHIVLNDICFGAAHADDLFPFFLRHAKQIFPVLDCKDDLRKISDLRIPPNWYPDARAMQRKIIFHSGPTNSGKTYHAIQKYFSAKSGVYCGPLKLLAHEIFEKSNAAGVPCDLVTGEERVTVQPNGKQASHVSCTVEMCSVTTPYEVAVIDEIQMIRDPARGWAWTRALLGLCAEEVHLCGEPAAIDLVMELMYTTGEEVEVRDYKRLTPISVLDHALESLDNLRPGDCIVCFSKNDIYSVSRQIEIRGLESAVIYGSLPPGTKLAQAKKFNDPNDPCKILVATDAIGMGLNLSIRRIIFYSLIKPSINEKGERELEPITTSQALQIAGRAGRFSSRFKEGEVTTMNHEDLSLLKEILKRPVDPIRAAGLHPTAEQIEMFAYHLPDATLSNLIDIFVDFSQVDGQYFVCNMDDFKFSAELIQHIPLSLRVRYVFCTAPINKKQPFVCSSLLQFARQYSRNEPLTFAWLRRYIKWPLLPPKNIKDLMDLEAVHDVLDLYLWLSYRFMDMFPDASLIRDLQKELDGIIQDGVHNITKLIKMSETHKLLNLEGFPSGSQSRLSGTLKSQARRTRGTKALGSKATEPPSPDAGELSLASRLVQQGLLTPDMLKQLEKEWMTQQTEHNKEKTESGTHPKGTRRKKKEPDSD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["RNA-binding proteins"],"UniParc":"UPI000007428D","uniref100":"UniRef100_Q8IYB8","uniref90":"UniRef90_Q8IYB8","uniref50":"UniRef50_Q8IYB8","genes":[{"name":{"value":"SUPV3L1"},"synonyms":[{"value":"SUV3"}]}],"alphafold_very_low_content":0.15394402035623408,"disorder_content":0.08778625954198473,"disprot_consensus":{"full":[{"start":47,"end":57,"type":"D"},{"start":73,"end":86,"type":"D"},{"start":446,"end":456,"type":"D"},{"start":690,"end":722,"type":"D"}],"Structural state":[{"start":47,"end":57,"type":"D"},{"start":73,"end":86,"type":"D"},{"start":446,"end":456,"type":"D"},{"start":690,"end":722,"type":"D"}]}},{"disprot_id":"DP03207","acc":"Q8IYV9","creator":"gparra","date":"2021-01-25T20:19:13.820Z","features":{"pfam":[{"id":"PF15005","name":"Izumo sperm-egg fusion, N-terminal domain","start":21,"end":165},{"id":"PF16706","name":"Izumo-like Immunoglobulin domain","start":168,"end":255}],"gene3D":[]},"length":350,"name":"Izumo sperm-egg fusion protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":257,"end":268,"reference_id":"27309818","reference_source":"pmid","reference_html":"Molecular architecture of the human sperm IZUMO1 and egg JUNO fertilization complex. <i> Aydin H, Sultana A, Li S, Thavalingam A, Lee JE. </i> Nature, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"gparra","curator_name":"Gonzalo Parra","curator_orcid":"0000-0003-2446-016X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5F4T"}],"region_id":"DP03207r001","statement":[{"text":" Residues 257-268 in Izumo122-268 are disordered suggesting that the linker region between the Ig-like domain and the transmembrane domain is highly flexible.","type":"Supplementary material"},{"text":"The Izumo122-268 structure superimposes well with Izumo122-254 (rmsd 1.0-Å over all atoms) (Supplementary Fig. 4). However, no electron density was observed after residue 256, suggesting that the linker region following the Ig-like domain is flexible.","type":"Abstract"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":127,"end":140,"reference_id":"27309818","reference_source":"pmid","reference_html":"Molecular architecture of the human sperm IZUMO1 and egg JUNO fertilization complex. <i> Aydin H, Sultana A, Li S, Thavalingam A, Lee JE. </i> Nature, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"gparra","curator_name":"Gonzalo Parra","curator_orcid":"0000-0003-2446-016X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03207r002","statement":[{"text":"Moreover, DXMS experiments performed\non Izumo1 alone indicated a high level of exchange in the hinge region, thus suggesting\ndynamic flexible motion within this region. Upon Juno binding, deuterium exchange of\nresidues 127-140 in the hinge region was reduced by >50%, which is more than the\nreduction seen by residues at the Izumo1-Juno interface (Fig. 4). The strong level of H/D\nprotection is due to the formation of 10 additional main chain hydrogen bonds within\nresidues 127-140 of the hinge region. This suggests that the Izumo1 hinge region is\nstabilized in a “locked” upright position in the presence of Juno","type":"Abstract"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MGPHFTLLCAALAGCLLPAEGCVICDPSVVLALKSLEKDYLPGHLDAKHHKAMMERVENAVKDFQELSLNEDAYMGVVDEATLQKGSWSLLKDLKRITDSDVKGDLFVKELFWMLHLQKETFATYVARFQKEAYCPNKCGVMLQTLIWCKNCKKEVHACRKSYDCGERNVEVPQMEDMILDCELNWHQASEGLTDYSFYRVWGNNTETLVSKGKEATLTKPMVGPEDAGSYRCELGSVNSSPATIINFHVTVLPKMIKEEKPSPNIVTPGEATTESSISLQPLQPEKMLASRLLGLLICGSLALITGLTFAIFRRRKVIDFIKSSLFGLGSGAAEQTQVPKEKATDSRQQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI00000741D7","uniref100":"UniRef100_Q8IYV9","uniref90":"UniRef90_Q8IYV9","uniref50":"UniRef50_Q8IYV9","genes":[{"name":{"value":"IZUMO1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15759005","url":"http://www.ncbi.nlm.nih.gov/pubmed/15759005","alternativeUrl":"https://europepmc.org/abstract/MED/15759005"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:28539","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:28539"}}]}}],"alphafold_very_low_content":0.18,"disorder_content":0.07428571428571429,"disprot_consensus":{"full":[{"start":127,"end":140,"type":"D"},{"start":257,"end":268,"type":"D"}],"Structural state":[{"start":127,"end":140,"type":"D"},{"start":257,"end":268,"type":"D"}]}},{"disprot_id":"DP03208","acc":"Q9KPH3","creator":"ngarrone","date":"2021-01-25T21:25:29.085Z","features":{"pfam":[{"id":"PF05258","name":"Dna[CI] antecedent, DciA","start":12,"end":91}],"gene3D":[]},"length":157,"name":"Uncharacterized protein","ncbi_taxon_id":243277,"organism":"Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)","regions":[{"start":112,"end":157,"reference_id":"32679070","reference_source":"pmid","reference_html":"Structural ensemble and biological activity of DciA intrinsically disordered region. <i> Chan-Yao-Chong M, Marsin S, Quevillon-Cheruel S, Durand D, Ha-Duong T. </i> J Struct Biol, 2020","date":"2026-03-27T15:44:40.819Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008035","ec_ontology":"ECO","ec_name":"author inference based on intrinsic disorder prediction used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP03208r001","statement":[{"text":"Beside their folded domain, all four previous helicase binding proteins (DciA, DnaC, DnaI, and DnaA) have an intrinsically disordered region predicted by PONDR (Romero et al., 1997). ","type":"Introduction"},{"text":"From a structural point of view, nuclear magnetic resonance (NMR) and SAXS experiments showed that V. cholerae DciA has a N-terminal domain which is well folded (residues 1–111) and a C-terminal tail which is presumably intrinsically disordered (segment 112–157 residues) (Marsin et al., 2020).","type":"Introduction"}]},{"start":112,"end":157,"reference_id":"32679070","reference_source":"pmid","reference_html":"Structural ensemble and biological activity of DciA intrinsically disordered region. <i> Chan-Yao-Chong M, Marsin S, Quevillon-Cheruel S, Durand D, Ha-Duong T. </i> J Struct Biol, 2020","date":"2026-03-27T15:47:14.925Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP03208r002","statement":[{"text":"The dimensionless Kratky plot of SAXS data has a bell shape at low scattering angles followed by a continuously increasing curve for larger angles, demonstrating that DciA has a folded domain and a disordered tail (Receveur-Brechot and Durand, 2012).","type":"Results"},{"text":"Regarding full-length DciA, the first minimum is slightly shifted toward low wavelengths and deeper than the second one, consistently with an increase in random coil residues relative to truncated protein 6xHis-DciA[1−111].","type":"Results"},{"text":"On the other hand, SAXS experiments reported here clearly demonstrated that DciA C-terminal tail is intrinsically disordered in the unbound state (Fig. 5), consistently with disorder predictions of PONDER and IUPRed2A (Fig. 2).","type":"Discussion"}]},{"start":112,"end":157,"reference_id":"32679070","reference_source":"pmid","reference_html":"Structural ensemble and biological activity of DciA intrinsically disordered region. <i> Chan-Yao-Chong M, Marsin S, Quevillon-Cheruel S, Durand D, Ha-Duong T. </i> J Struct Biol, 2020","date":"2026-03-27T16:44:49.736Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051096","term_name":"positive regulation of helicase activity","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Arg112_Asp157del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP03208r003","statement":[{"text":"SPR results first show that binding of DnaB onto ssDNA without any DciA (pink curve of Fig. 3) or in the presence of DciA[1−111] (cyan curve) are quite similar, indicating that truncated DciA[1−111] does not particularly contribute to the loading of additional DnaB on ssDNA. In contrast, as shown by the significant increase from 100–200 to 500–600 RU of the grey, blue, and red curves of Fig. 3, full-length DciA clearly stimulates and increases the binding to ssDNA of proteins which are probably complexes of DciA-DnaB. After these increases, a biphasic dissociation can be observed. First, there is a rapid signal decrease by about 100 RU in less than 100 s which would originate from the release of DciA while DnaB still hangs on DNA. Then, a slow decrease of SPR signals can be observed, which would be associated to the slow dissociation of DnaB from attached DNA (Fig. 3).","type":"Results"}],"term_comment":"","term_def":"\"Any process that activates or increases the activity of a helicase.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":112,"end":157,"reference_id":"32679070","reference_source":"pmid","reference_html":"Structural ensemble and biological activity of DciA intrinsically disordered region. <i> Chan-Yao-Chong M, Marsin S, Quevillon-Cheruel S, Durand D, Ha-Duong T. </i> J Struct Biol, 2020","date":"2026-03-27T16:50:29.996Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990099","term_name":"pre-primosome complex","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Arg112_Asp157del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP03208r004","statement":[{"text":"SPR results first show that binding of DnaB onto ssDNA without any DciA (pink curve of Fig. 3) or in the presence of DciA[1−111] (cyan curve) are quite similar, indicating that truncated DciA[1−111] does not particularly contribute to the loading of additional DnaB on ssDNA. In contrast, as shown by the significant increase from 100–200 to 500–600 RU of the grey, blue, and red curves of Fig. 3, full-length DciA clearly stimulates and increases the binding to ssDNA of proteins which are probably complexes of DciA-DnaB.","type":"Results"},{"text":"It is observed that DciA, but not DciA[1−111], can induces an increase in the SPR signal (red curve of Fig. 3), indicating that full-length DciA can rebind and reform a ternary complex DciA-DnaB-ssDNA.","type":"Results"},{"text":"Altogether, these SPR experiments showed the importance of DciA disordered region in the loading of DnaB helicase on DNA. They suggest that DciA C-terminal tail is involved in forming the ternary complex DciA-DnaB-ssDNA.","type":"Results"}],"term_comment":"","term_def":"\"Any of the protein-DNA complexes that contain a DNA helicase and associated protein(s) at the origin of replication, and build up to assembling the core primosome. The associated protein(s) chaperone the helicase to the DNA, and assembly of the pre-primosome is essential for the initiation or restart of replication. Pre-primosome complexes lack a primase component.\" [GOC:bhm, PMID:18179598, PMID:20129058, PMID:8663105]","term_is_obsolete":false,"term_not_annotate":false},{"start":112,"end":157,"reference_id":"32679070","reference_source":"pmid","reference_html":"Structural ensemble and biological activity of DciA intrinsically disordered region. <i> Chan-Yao-Chong M, Marsin S, Quevillon-Cheruel S, Durand D, Ha-Duong T. </i> J Struct Biol, 2020","date":"2026-03-27T16:53:39.701Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Arg112_Asp157del","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q9KUY7","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03208r005","statement":[{"text":"Altogether, these SPR experiments showed the importance of DciA disordered region in the loading of DnaB helicase on DNA. They suggest that DciA C-terminal tail is involved in forming the ternary complex DciA-DnaB-ssDNA.","type":"Results"},{"text":"These results were complemented by ITC experiments which evidenced an absence of interaction between DnaB and DciA[1−111] but a direct binding of full-length DciA to the helicase with an estimated \n μM (Fig. 4). Altogether, these experimental data demonstrated that the C-terminal disordered region of DciA make direct interactions with DnaB.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":5,"released":"2026_06","sequence":"MRDHRPTATDELIQASKLKQIQEHAKAILLINRQLQDILPKGLKTQVRAANVRGGNLVLEAASAALKMKVDYERLHILTQLRQNGFGHLISIEVRVNPELYRQSKITSEDARAANPRPPLSEHAAHVLLAIADQASDKVKKRLQSLARLAKANQKDD","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Vibrionales","Vibrionaceae","Vibrio"],"dataset":[],"UniParc":"UPI00000C32B2","uniref100":"UniRef100_A0A7U8WMZ5","uniref90":"UniRef90_A0A0Q0VVK9","uniref50":"UniRef50_D0IM16","genes":[{"olnNames":[{"value":"VC_2395","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF95538.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF95538.1"}}]}]}],"alphafold_very_low_content":0.03184713375796178,"disorder_content":0.2929936305732484,"disprot_consensus":{"full":[{"start":112,"end":157,"type":"D"}],"Structural state":[{"start":112,"end":157,"type":"D"}],"Biological process":[{"start":112,"end":157,"type":"F"}],"Cellular component":[{"start":112,"end":157,"type":"F"}],"Molecular function":[{"start":112,"end":157,"type":"F"}]}},{"disprot_id":"DP03209","acc":"A6ND01","creator":"gparra","date":"2021-01-25T22:14:11.067Z","features":{"pfam":[{"id":"PF03024","name":"Folate receptor family","start":26,"end":208}],"gene3D":[]},"length":250,"name":"Sperm-egg fusion protein Juno","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":111,"end":122,"reference_id":"27309818","reference_source":"pmid","reference_html":"Molecular architecture of the human sperm IZUMO1 and egg JUNO fertilization complex. <i> Aydin H, Sultana A, Li S, Thavalingam A, Lee JE. </i> Nature, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"gparra","curator_name":"Gonzalo Parra","curator_orcid":"0000-0003-2446-016X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5F4Q"}],"region_id":"DP03209r001","statement":[{"text":"A disordered loop between the β1 and β2 strands of the Juno20-228 is shown with a black dashed line. ","type":"Figure"},{"text":"The region corresponding to residues 111-122 corresponds to a missing residues region in the 5F4Q PDB structure","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":111,"end":122,"reference_id":"27309808","reference_source":"pmid","reference_html":"Structure of IZUMO1-JUNO reveals sperm-oocyte recognition during mammalian fertilization. <i> Ohto U, Ishida H, Krayukhina E, Uchiyama S, Inoue N, Shimizu T. </i> Nature, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"gparra","curator_name":"Gonzalo Parra","curator_orcid":"0000-0003-2446-016X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5JKA"}],"region_id":"DP03209r002","statement":[{"text":"The human JUNO L2 region, which corresponds to the inhibitory loop in FRs11, is disordered (Fig. 2b), possibly due to a 6–7 amino acid insertion not present in other species (Extended Data Figs 1 and 2)","type":"Abstract"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MACWWPLLLELWTVMPTWAGDELLNICMNAKHHKRVPSPEDKLYEECIPWKDNACCTLTTSWEAHLDVSPLYNFSLFHCGLLMPGCRKHFIQAICFYECSPNLGPWIQPVGSLGWEVAPSGQGERVVNVPLCQEDCEEWWEDCRMSYTCKSNWRGGWDWSQGKNRCPKGAQCLPFSHYFPTPADLCEKTWSNSFKASPERRNSGRCLQKWFEPAQGNPNVAVARLFASSAPSWELSYTIMVCSLFLPFLS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI00003D6FE9","uniref100":"UniRef100_A6ND01","uniref90":"UniRef90_A6ND01","uniref50":"UniRef50_Q9EQF4","genes":[{"name":{"value":"IZUMO1R","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:32565","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:32565"}}]},"synonyms":[{"value":"FOLR4"},{"value":"JUNO","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"24739963","url":"http://www.ncbi.nlm.nih.gov/pubmed/24739963","alternativeUrl":"https://europepmc.org/abstract/MED/24739963"}}]}]}],"alphafold_very_low_content":0.068,"disorder_content":0.048,"disprot_consensus":{"full":[{"start":111,"end":122,"type":"D"}],"Structural state":[{"start":111,"end":122,"type":"D"}]}},{"disprot_id":"DP03211","acc":"Q9BRT9","creator":"ldobson","date":"2021-01-30T12:45:58.225Z","features":{"pfam":[{"id":"PF05916","name":"GINS complex protein helical bundle domain","start":70,"end":144},{"id":"PF16922","name":"DNA replication complex GINS protein SLD5 C-terminus","start":165,"end":223}],"gene3D":[]},"length":223,"name":"DNA replication complex GINS protein SLD5","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":20,"reference_id":"17652513","reference_source":"pmid","reference_html":"Crystal structure of the GINS complex and functional insights into its role in DNA replication. <i> Chang YP, Wang G, Bermudez V, Hurwitz J, Chen XS. </i> Proc Natl Acad Sci U S A, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2Q9Q"}],"region_id":"DP03211r001","statement":[{"text":"No clear indication in the paper, atomic coordinates are missing from PDB file","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MTEEVDFLGQDSDGGSEEVVLTPAELIERLEQAWMNEKFAPELLESKPEIVECVMEQLEHMEENLRRAKREDLKVSIHQMEMERIRYVLSSYLRCRLMKIEKFFPHVLEKEKTRPEGEPSSLSPEELAFAREFMANTESYLKNVALKHMPPNLQKVDLFRAVPKPDLDSYVFLRVRERQENILVEPDTDEQRDYVIDLEKGSQHLIRYKTIAPLVASGAVQLI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000007007B","uniref100":"UniRef100_Q9BRT9","uniref90":"UniRef90_Q9BRT9","uniref50":"UniRef50_Q9BRT9","genes":[{"name":{"value":"GINS4"},"synonyms":[{"value":"SLD5"}]}],"alphafold_very_low_content":0.07623318385650224,"disorder_content":0.08968609865470852,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"D"}],"Structural state":[{"start":1,"end":20,"type":"D"}]}},{"disprot_id":"DP03212","acc":"P0DTC9","creator":"eficho","date":"2021-02-09T15:11:24.277Z","features":{"pfam":[{"id":"PF00937","name":"Coronavirus nucleocapsid","start":45,"end":381}],"gene3D":[]},"length":419,"name":"Nucleoprotein","ncbi_taxon_id":2697049,"organism":"Severe acute respiratory syndrome coronavirus 2","regions":[{"start":182,"end":197,"reference_id":"33247108","reference_source":"pmid","reference_html":"Nucleocapsid protein of SARS-CoV-2 phase separates into RNA-rich polymerase-containing condensates. <i> Savastano A, Ibáñez de Opakua A, Rankovic M, Zweckstetter M. </i> Nat Commun, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03212r001","statement":[{"text":"Chemical shift analysis\nshowed that residues A182-S197 are very dynamic with a small propensity of α-helical structure next to R189","type":"Results"},{"text":"Fig 3b. clearly indicates that the region is intrinsically disordered","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-29T10:10:16.382Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":182,"end":197,"reference_id":"33247108","reference_source":"pmid","reference_html":"Nucleocapsid protein of SARS-CoV-2 phase separates into RNA-rich polymerase-containing condensates. <i> Savastano A, Ibáñez de Opakua A, Rankovic M, Zweckstetter M. </i> Nat Commun, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03212r002","statement":[{"text":"NMR titrations showed that the unmodified SR-peptide strongly interacts with polyU","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-29T10:17:54.041Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":186,"end":190,"reference_id":"33247108","reference_source":"pmid","reference_html":"Nucleocapsid protein of SARS-CoV-2 phase separates into RNA-rich polymerase-containing condensates. <i> Savastano A, Ibáñez de Opakua A, Rankovic M, Zweckstetter M. </i> Nat Commun, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000037","term_name":"molecular recognition display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03212r003","statement":[{"text":"SRPK1-phosphorylation resulted in two species, a single phosphorylation at S188 (Fig. 4b, middle) and a di-phosphorylated state, which is heterogeneously phosphorylated at four different serines (Fig. 4b, bottom; Supplementary Fig. 7). NMR titrations showed that the unmodified SR-peptide strongly interacts with polyU, but not when it is phosphorylated at S188 (Fig. 4b and Supplementary Fig. 4b). LLPS experiments further demonstrated that phosphorylation of full-length NSARS-CoV-2 by SRPK1 changes its RNA-induced phase separation behavior (Fig. 4c and Supplementary Fig. 8). The maximum of RNA- induced turbidity was shifted to lower polyU-concentrations for SRPK1-phosphorylated NSARS-CoV-2 (Fig. 4c). In addition, fluorescently labeled RNA was less recruited to droplets formed by SRPK1-phosphorylated NSARS-CoV-2 (Fig. 4d). In agreement with an attenuated interaction of NSARS-CoV-2 with RNA upon SRPK1-phosphorylation, we also observed a more rapid diffusion of SRPK1-phosphorylated NSARS-CoV-2 inside of polyU-induced droplets when compared to the unmodified protein (Fig. 4e). On the other hand, SRPK1-phosphorylated NSARS-CoV-2 still co-localized with stress granules (Fig. 4d).","type":"Results"},{"text":"The evidence refers to phosphorylated serine pS188.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-29T14:12:35.826Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":182,"end":197,"reference_id":"33247108","reference_source":"pmid","reference_html":"Nucleocapsid protein of SARS-CoV-2 phase separates into RNA-rich polymerase-containing condensates. <i> Savastano A, Ibáñez de Opakua A, Rankovic M, Zweckstetter M. </i> Nat Commun, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006307","ec_ontology":"ECO","ec_name":"turbidity measurement evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03212r004","statement":[{"text":"SRPK1-phosphorylation resulted in two species, a single phosphorylation at S188 (Fig. 4b, middle) and a di-phosphorylated state, which is heterogeneously phosphorylated at four different serines (Fig. 4b, bottom; Supplementary Fig. 7). NMR titrations showed that the unmodified SR-peptide strongly interacts with polyU, but not when it is phosphorylated at S188 (Fig. 4b and Supplementary Fig. 4b). LLPS experiments further demonstrated that phosphorylation of full-length NSARS-CoV-2 by SRPK1 changes its RNA-induced phase separation behavior (Fig. 4c and Supplementary Fig. 8). The maximum of RNA-induced turbidity was shifted to lower polyU-concentrations for SRPK1-phosphorylated NSARS-CoV-2 (Fig. 4c). In addition, fluorescently labeled RNA was less recruited to droplets formed by SRPK1-phosphorylated NSARS-CoV-2 (Fig. 4d). In agreement with an attenuated interaction of NSARS-CoV-2 with RNA upon SRPK1-phosphorylation, we also observed a more rapid diffusion of SRPK1-phosphorylated NSARS-CoV-2 inside of polyU-induced droplets when compared to the unmodified protein (Fig. 4e).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-29T14:12:26.449Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":182,"end":197,"reference_id":"33247108","reference_source":"pmid","reference_html":"Nucleocapsid protein of SARS-CoV-2 phase separates into RNA-rich polymerase-containing condensates. <i> Savastano A, Ibáñez de Opakua A, Rankovic M, Zweckstetter M. </i> Nat Commun, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0043232","term_name":"intracellular non-membrane-bounded organelle","term_namespace":"Cellular component","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03212r005","statement":[{"text":"SRPK1-phosphorylated NSARS-CoV-2 still co-localized with stress granules.","type":"Results"},{"text":"Association of unmodified (NSARS-CoV-2, left panels) and phosphorylated (phosphoNSARS-CoV-2, right panels) nucleocapsid protein of SARS-CoV-2 with stress granules in HeLa cells","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-29T14:12:47.203Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Organized structure of distinctive morphology and function, not bounded by a lipid bilayer membrane and occurring within the cell. Includes ribosomes, the cytoskeleton and chromosomes.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":40,"reference_id":"33660218","reference_source":"pmid","reference_html":"The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1-248 residue construct: sequence-specific resonance assignments through NMR. <i> Schiavina M, Pontoriero L, Uversky VN, Felli IC, Pierattelli R. </i> Biomol NMR Assign, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03212r006","statement":[{"text":"The two globular domains of the protein (NTD and CTD) have been investigated while no high-resolution information is available yet for the flexible regions of the protein. We focus here on the 1-248 construct which comprises two disordered fragments (IDR1 and IDR2) in addition to the N-terminal globular domain (NTD) and report the sequence-specific assignment of the two disordered regions, a step forward towards the complete characterization of the whole protein.","type":"Abstract"},{"text":"In this frame, we provide here the backbone assignment of the two disordered regions flanking the NTD, the N-terminal IDR1 and the serine-rich disordered region IDR2, in the 1–248 residue construct (IDR1-NTD-IDR2).","type":"Article"},{"text":"The 2D HN spectrum recorded on the IDR1-NTD-IDR2 (1–248) construct of the SARS-CoV-2 nucleocapsid protein N is shown in Fig. 2. The 2D HN spectrum clearly shows a set of well-resolved NMR signals deriving from the globular NTD domain, as one can verify by superimposing the available sequence-specific assignment (BMRB 34511, Dinesh et al. 2020). In addition, a set of signals, with smaller dispersion and higher intensity, are observed. These are expected to originate from the flexible and disordered fragments of the protein (black contours in Fig. 2).","type":"Results"},{"text":"This region corresponds to IDR1.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-29T13:43:42.618Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":181,"end":248,"reference_id":"33660218","reference_source":"pmid","reference_html":"The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1-248 residue construct: sequence-specific resonance assignments through NMR. <i> Schiavina M, Pontoriero L, Uversky VN, Felli IC, Pierattelli R. </i> Biomol NMR Assign, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03212r007","statement":[{"text":"The two globular domains of the protein (NTD and CTD) have been investigated while no high-resolution information is available yet for the flexible regions of the protein. We focus here on the 1-248 construct which comprises two disordered fragments (IDR1 and IDR2) in addition to the N-terminal globular domain (NTD) and report the sequence-specific assignment of the two disordered regions, a step forward towards the complete characterization of the whole protein.","type":"Abstract"},{"text":"In this frame, we provide here the backbone assignment of the two disordered regions flanking the NTD, the N-terminal IDR1 and the serine-rich disordered region IDR2, in the 1–248 residue construct (IDR1-NTD-IDR2).","type":"Article"},{"text":"The 2D HN spectrum recorded on the IDR1-NTD-IDR2 (1–248) construct of the SARS-CoV-2 nucleocapsid protein N is shown in Fig. 2. The 2D HN spectrum clearly shows a set of well-resolved NMR signals deriving from the globular NTD domain, as one can verify by superimposing the available sequence-specific assignment (BMRB 34511, Dinesh et al. 2020). In addition, a set of signals, with smaller dispersion and higher intensity, are observed. These are expected to originate from the flexible and disordered fragments of the protein (black contours in Fig. 2).","type":"Results"},{"text":"This region corresponds to IDR2 and links the NTD and CTD domains.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-29T10:51:03.163Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":181,"end":248,"reference_id":"33660218","reference_source":"pmid","reference_html":"The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1-248 residue construct: sequence-specific resonance assignments through NMR. <i> Schiavina M, Pontoriero L, Uversky VN, Felli IC, Pierattelli R. </i> Biomol NMR Assign, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03212r008","statement":[{"text":"The two globular domains of the protein (NTD and CTD) have been investigated while no high-resolution information is available yet for the flexible regions of the protein. We focus here on the 1-248 construct which comprises two disordered fragments (IDR1 and IDR2) in addition to the N-terminal globular domain (NTD) and report the sequence-specific assignment of the two disordered regions, a step forward towards the complete characterization of the whole protein.","type":"Abstract"},{"text":"In this frame, we provide here the backbone assignment of the two disordered regions flanking the NTD, the N-terminal IDR1 and the serine-rich disordered region IDR2, in the 1–248 residue construct (IDR1-NTD-IDR2).","type":"Article"},{"text":"The 2D HN spectrum recorded on the IDR1-NTD-IDR2 (1–248) construct of the SARS-CoV-2 nucleocapsid protein N is shown in Fig. 2. The 2D HN spectrum clearly shows a set of well-resolved NMR signals deriving from the globular NTD domain, as one can verify by superimposing the available sequence-specific assignment (BMRB 34511, Dinesh et al. 2020). In addition, a set of signals, with smaller dispersion and higher intensity, are observed. These are expected to originate from the flexible and disordered fragments of the protein (black contours in Fig. 2).","type":"Results"},{"text":"This region corresponds to IDR2 and links the NTD and CTD domains.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-29T13:43:47.086Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":1,"end":68,"reference_id":"33782395","reference_source":"pmid","reference_html":"The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA. <i> Cubuk J, Alston JJ, Incicco JJ, Singh S, Stuchell-Brereton MD, Ward MD, Zimmerman MI, Vithani N, Griffith D, Wagoner JA, Bowman GR, Hall KB, Soranno A, Holehouse AS. </i> Nat Commun, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03212r009","statement":[{"text":"This corresponds to values of persistence length (see SI) equal to 4.5 ± 0.4 and 4.3 ± 0.4 Å for the Gaussian and SAW distribution, respectively, which are similar to values reported for another unfolded protein under native conditions44–46,50. Overall, these results confirm the NTD is disordered, as predicted by sequence analysis.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-29T14:35:53.571Z"},"ec_go":"IPI","disprot_namespace":"Structural state"},{"start":172,"end":245,"reference_id":"33782395","reference_source":"pmid","reference_html":"The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA. <i> Cubuk J, Alston JJ, Incicco JJ, Singh S, Stuchell-Brereton MD, Ward MD, Zimmerman MI, Vithani N, Griffith D, Wagoner JA, Bowman GR, Hall KB, Soranno A, Holehouse AS. </i> Nat Commun, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03212r010","statement":[{"text":"We next turned to the linker (LINK FL) construct to investigate how the disordered region modulates the interaction and dynamics between the two folded domains.","type":"Results"},{"text":"This reconfiguration time is compatible with high internal friction effects, as observed for other unstructured proteins44,45, but may also account for the drag of the surrounding domains.","type":"Results"},{"text":"The RNA-binding domain (RBD) and dimerization domains are interconnected by a flexible disordered linker (LINK).","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-29T14:37:05.905Z"},"ec_go":"IPI","disprot_namespace":"Structural state"},{"start":363,"end":419,"reference_id":"33782395","reference_source":"pmid","reference_html":"The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA. <i> Cubuk J, Alston JJ, Incicco JJ, Singh S, Stuchell-Brereton MD, Ward MD, Zimmerman MI, Vithani N, Griffith D, Wagoner JA, Bowman GR, Hall KB, Soranno A, Holehouse AS. </i> Nat Commun, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03212r011","statement":[{"text":"Finally, we again applied single-molecule FRET (Fig. 4A) and ns-FCS (Fig. 4B) to understand the conformational behavior of the CTD FL construct. Single-molecule FRET experiments again reveal a single population with a mean transfer efficiency of 0.59 ± 0.03 (Fig. 4A) and the denaturant dependence follows the expected trend for a disordered region, with a shift of the transfer efficiency toward lower values (Figs. 4C, S6 and S8), from 0.59 to 0.35.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-29T14:39:17.442Z"},"ec_go":"IPI","disprot_namespace":"Structural state"},{"start":174,"end":247,"reference_id":"33200826","reference_source":"pmid","reference_html":"SARS-CoV-2 nucleocapsid protein phase-separates with RNA and with human hnRNPs. <i> Perdikari TM, Murthy AC, Ryan VH, Watters S, Naik MT, Fawzi NL. </i> EMBO J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03212r012","statement":[{"text":"Similar to deletion of the folded CTD, deletion of the linkerIDR dramatically reduces formation of droplets and turbidity associated with LLPS in both conditions (Fig 5A–C).","type":"Results"},{"text":"In summary, these data suggest that in the presence of RNA, the NIDR, the linkerIDR, and the folded CTD form protein–protein and/or protein–RNA contacts important for the multivalent interactions stabilizing in vitro LLPS of N.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-29T14:39:28.128Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":174,"end":247,"reference_id":"33200826","reference_source":"pmid","reference_html":"SARS-CoV-2 nucleocapsid protein phase-separates with RNA and with human hnRNPs. <i> Perdikari TM, Murthy AC, Ryan VH, Watters S, Naik MT, Fawzi NL. </i> EMBO J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000269","ec_ontology":"ECO","ec_name":"experimental evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03212r013","statement":[{"text":"Similar to deletion of the folded CTD, deletion of the linkerIDR dramatically reduces formation of droplets and turbidity associated with LLPS in both conditions (Fig 5A–C).","type":"Results"},{"text":"In summary, these data suggest that in the presence of RNA, the NIDR, the linkerIDR, and the folded CTD form protein–protein and/or protein–RNA contacts important for the multivalent interactions stabilizing in vitro LLPS of N.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-29T14:39:30.642Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":43,"reference_id":"33200826","reference_source":"pmid","reference_html":"SARS-CoV-2 nucleocapsid protein phase-separates with RNA and with human hnRNPs. <i> Perdikari TM, Murthy AC, Ryan VH, Watters S, Naik MT, Fawzi NL. </i> EMBO J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000269","ec_ontology":"ECO","ec_name":"experimental evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03212r014","statement":[{"text":"In summary, these data suggest that in the presence of RNA, the NIDR, the linkerIDR, and the folded CTD form protein–protein and/or protein–RNA contacts important for the multivalent interactions stabilizing in vitro LLPS of N.","type":"Results"},{"text":"Regarding the disordered regions, we found that deletion of the NIDR modestly enhanced droplet formation and turbidity in the absence of RNA (Fig 5A and B), while, in the presence of RNA, phase separation is strongly decreased (Fig 5A and C).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-29T14:39:31.727Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":43,"reference_id":"33200826","reference_source":"pmid","reference_html":"SARS-CoV-2 nucleocapsid protein phase-separates with RNA and with human hnRNPs. <i> Perdikari TM, Murthy AC, Ryan VH, Watters S, Naik MT, Fawzi NL. </i> EMBO J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03212r015","statement":[{"text":"In summary, these data suggest that in the presence of RNA, the NIDR, the linkerIDR, and the folded CTD form protein–protein and/or protein–RNA contacts important for the multivalent interactions stabilizing in vitro LLPS of N.","type":"Results"},{"text":"Regarding the disordered regions, we found that deletion of the NIDR modestly enhanced droplet formation and turbidity in the absence of RNA (Fig 5A and B), while, in the presence of RNA, phase separation is strongly decreased (Fig 5A and C).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-29T14:39:33.192Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":182,"end":197,"reference_id":"33247108","reference_source":"pmid","reference_html":"Nucleocapsid protein of SARS-CoV-2 phase separates into RNA-rich polymerase-containing condensates. <i> Savastano A, Ibáñez de Opakua A, Rankovic M, Zweckstetter M. </i> Nat Commun, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0043232","term_name":"intracellular non-membrane-bounded organelle","term_namespace":"Cellular component","term_ontology":"GO","ec_id":"ECO:0006067","ec_ontology":"ECO","ec_name":"fluorescence recovery after photobleaching evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03212r016","statement":[{"text":"Nucleocapsid protein of SARS-CoV-2 associates with stress granules.\na. Alexa Fluor 488 labeled N(SARS-CoV-2) (green) colocalizes with the stress granule marker G3BP1 (red) in arsenite-treated digitonin-permeabilized HeLa cells.","type":"Figure"},{"text":"FRAP of SG-associated N(SARS-CoV-2) suggested the presence of three N(SARS-CoV-2) populations (Fig. 2b): a very mobile with rapid fluorescence recovery, a slower diffusing component, and an immobile fraction, which does not recover its fluorescence after photobleaching (Fig. 2c). Because SGs consists of a rigid core and a dynamic shell, we attribute the different N(SARS-CoV-2) diffusion properties to the localization of N(SARS-CoV-2) to different sub-structures of SGs.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-29T14:26:08.146Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Organized structure of distinctive morphology and function, not bounded by a lipid bilayer membrane and occurring within the cell. Includes ribosomes, the cytoskeleton and chromosomes.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":172,"end":245,"reference_id":"33782395","reference_source":"pmid","reference_html":"The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA. <i> Cubuk J, Alston JJ, Incicco JJ, Singh S, Stuchell-Brereton MD, Ward MD, Zimmerman MI, Vithani N, Griffith D, Wagoner JA, Bowman GR, Hall KB, Soranno A, Holehouse AS. </i> Nat Commun, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03212r017","statement":[{"text":"The RNA-binding domain (RBD) and dimerization domains are interconnected by a flexible disordered linker (LINK).","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-08-04T08:08:00.956Z"},"ec_go":"IPI","disprot_namespace":"Disorder function"},{"start":1,"end":44,"reference_id":"33730325","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N Backbone chemical shift assignments of the n-terminal and central intrinsically disordered domains of SARS-CoV-2 nucleoprotein. <i> Guseva S, Perez LM, Camacho-Zarco A, Bessa LM, Salvi N, Malki A, Maurin D, Blackledge M. </i> Biomol NMR Assign, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03212r018","statement":[{"text":"N is a 419 amino acid multidomain protein, comprising two folded, RNA-binding and dimerization domains spanning residues 45-175 and 264-365 respectively. The remaining 164 amino acids are predicted to be intrinsically disordered, but there is currently no atomic resolution information describing their behaviour. Here we assign the backbone resonances of the first two intrinsically disordered domains (N1, spanning residues 1-44 and N3, spanning residues 176-263).","type":"Abstract"}],"cross_refs":[{"db":"BMRB","id":"50558"},{"db":"BMRB","id":"50557"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-06T08:46:54.791Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":176,"end":263,"reference_id":"33730325","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N Backbone chemical shift assignments of the n-terminal and central intrinsically disordered domains of SARS-CoV-2 nucleoprotein. <i> Guseva S, Perez LM, Camacho-Zarco A, Bessa LM, Salvi N, Malki A, Maurin D, Blackledge M. </i> Biomol NMR Assign, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03212r019","statement":[{"text":"N is a 419 amino acid multidomain protein, comprising two folded, RNA-binding and dimerization domains spanning residues 45-175 and 264-365 respectively. The remaining 164 amino acids are predicted to be intrinsically disordered, but there is currently no atomic resolution information describing their behaviour. Here we assign the backbone resonances of the first two intrinsically disordered domains (N1, spanning residues 1-44 and N3, spanning residues 176-263).","type":"Abstract"}],"cross_refs":[{"db":"BMRB","id":"50557"},{"db":"BMRB","id":"50558"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-06T08:46:53.537Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":222,"end":230,"reference_id":"33521593","reference_source":"pmid","reference_html":"The presentation of SARS-CoV-2 peptides by the common HLA-A<sup>∗</sup>02:01 molecule. <i> Szeto C, Chatzileontiadou DSM, Nguyen AT, Sloane H, Lobos CA, Jayasinghe D, Halim H, Smith C, Riboldi-Tunnicliffe A, Grant EJ, Gras S. </i> iScience, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0042288","term_name":"MHC class I protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"7KGQ"}],"interaction_partner":[{"db":"UniProt","id":"P61769","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q861F7","partner_start":null,"partner_end":null}],"region_id":"DP03212r020","statement":[{"text":"We then determined the crystal structure of six HLA-A*02:01-SARS-CoV-2 complexes, providing the first description of CD8+ T cell SARS-CoV-2 epitopes at an atomic level. Interestingly, three of our selected peptides have since been shown to be immunogenic (N219-227 (Isabel Schulien et al., 2021), N222-230 (Ferretti et al., 2020; Isabel Schulien et al., 2021), and N316-324 (Habel et al., 2020; Isabel Schulien et al., 2021)) in COVID-19 recovered individuals. As expected, these immunogenic peptides were able to form a stable complex with the HLA-A*02:01 molecule.","type":"Introduction"},{"text":"Overall, we demonstrate that not all selected peptides were able to form stable complexes with HLA-A*02:01, which was a consequence of unfavourable P2 and/or PΩ residues and an important factor for immunogenicity. In addition, we saw limited pre-existing CD8+ T cell response for these peptides in unexposed donors, whereas peptides that have subsequently been shown to be immunogenic in COVID-19 recovered patients were stable and adopted a canonical conformation in the cleft of HLA-A*02:01. Altogether, our data provide molecular insight into CD8+ T cell epitopes from SARS-CoV-2.","type":"Introduction"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-29T10:46:15.200Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Note that this term does not include binding to the antigen peptide bound to the MHC protein. Consider also annotating to the molecular function term 'peptide antigen binding ; GO:0042605' or one of its children.","term_def":"\"Binding to a major histocompatibility complex class I molecule; a set of molecules displayed on cell surfaces that are responsible for lymphocyte recognition and antigen presentation.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":222,"end":230,"reference_id":"33521593","reference_source":"pmid","reference_html":"The presentation of SARS-CoV-2 peptides by the common HLA-A<sup>∗</sup>02:01 molecule. <i> Szeto C, Chatzileontiadou DSM, Nguyen AT, Sloane H, Lobos CA, Jayasinghe D, Halim H, Smith C, Riboldi-Tunnicliffe A, Grant EJ, Gras S. </i> iScience, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0042612","term_name":"MHC class I protein complex","term_namespace":"Cellular component","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"7KGQ"}],"region_id":"DP03212r021","statement":[{"text":"We then determined the crystal structure of six HLA-A*02:01-SARS-CoV-2 complexes, providing the first description of CD8+ T cell SARS-CoV-2 epitopes at an atomic level. Interestingly, three of our selected peptides have since been shown to be immunogenic (N219-227 (Isabel Schulien et al., 2021), N222-230 (Ferretti et al., 2020; Isabel Schulien et al., 2021), and N316-324 (Habel et al., 2020; Isabel Schulien et al., 2021)) in COVID-19 recovered individuals. As expected, these immunogenic peptides were able to form a stable complex with the HLA-A*02:01 molecule.","type":"Introduction"},{"text":"Overall, we demonstrate that not all selected peptides were able to form stable complexes with HLA-A*02:01, which was a consequence of unfavourable P2 and/or PΩ residues and an important factor for immunogenicity. In addition, we saw limited pre-existing CD8+ T cell response for these peptides in unexposed donors, whereas peptides that have subsequently been shown to be immunogenic in COVID-19 recovered patients were stable and adopted a canonical conformation in the cleft of HLA-A*02:01. Altogether, our data provide molecular insight into CD8+ T cell epitopes from SARS-CoV-2.","type":"Introduction"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-29T11:01:37.839Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"See also the cellular component term 'MHC class I peptide loading complex ; GO:0042824'.","term_def":"\"A transmembrane protein complex composed of a MHC class I alpha chain and an invariant beta2-microglobin chain, and with or without a bound peptide antigen. Class I here refers to classical class I molecules.\" [GOC:add, GOC:jl, ISBN:0120781859, ISBN:0781735149]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":222,"end":230,"reference_id":"33521593","reference_source":"pmid","reference_html":"The presentation of SARS-CoV-2 peptides by the common HLA-A<sup>∗</sup>02:01 molecule. <i> Szeto C, Chatzileontiadou DSM, Nguyen AT, Sloane H, Lobos CA, Jayasinghe D, Halim H, Smith C, Riboldi-Tunnicliffe A, Grant EJ, Gras S. </i> iScience, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0042612","term_name":"MHC class I protein complex","term_namespace":"Cellular component","term_ontology":"GO","ec_id":"ECO:0006317","ec_ontology":"ECO","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03212r022","statement":[{"text":"Two peptides, N138-146 and N159-167, were not immunogenic in COVID-19-recovered individuals (Isabel Schulien et al., 2021), whereas three peptides, namely N219-227 (Isabel Schulien et al., 2021), N222-230 (Isabel Schulien et al., 2021), and N316-324 (Isabel Schulien et al., 2021; Habel et al., 2020), were immunogenic in COVID-19 recovered individuals, further highlighting the importance of further investigation into these epitopes.","type":"Results"},{"text":"The most stable pHLA complexes were the one with the N222-230 (Tm of 55°C) and N316-324 (Tm of 49°C) peptides, followed by the one with N219-227, N226-234, and N351-359 peptides with a Tm of ~40°C (Table 1, Figure S1). Surprisingly, the Tm was ~35°C for complexes with the NTD-derived peptides N138-146 and N159-167, an extremely low Tm value for pHLA-A*02:01 complexes (Valkenburg et al., 2016; Blaha et al., 2019; Khan et al., 2000).","type":"Results"},{"text":"The three peptides that resulted in a pHLA complex with a Tm above 40°C were recently described as immunogenic in COVID-19-recovered patients (N219-227 (Isabel Schulien et al., 2021), N222-230 (Ferretti et al., 2020; Isabel Schulien et al., 2021), and N316-324 (Habel et al., 2020; Isabel Schulien et al., 2021)), whereas the two peptides leading to a pHLA with a Tm below 40°C were described as non-immunogenic (N138-146 and N159-167 (Isabel Schulien et al., 2021)) (Table 1). This suggests that indeed pHLA complex stability may play a role in peptide immunogenicity.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-29T10:49:48.184Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"See also the cellular component term 'MHC class I peptide loading complex ; GO:0042824'.","term_def":"\"A transmembrane protein complex composed of a MHC class I alpha chain and an invariant beta2-microglobin chain, and with or without a bound peptide antigen. Class I here refers to classical class I molecules.\" [GOC:add, GOC:jl, ISBN:0120781859, ISBN:0781735149]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":219,"end":227,"reference_id":"33521593","reference_source":"pmid","reference_html":"The presentation of SARS-CoV-2 peptides by the common HLA-A<sup>∗</sup>02:01 molecule. <i> Szeto C, Chatzileontiadou DSM, Nguyen AT, Sloane H, Lobos CA, Jayasinghe D, Halim H, Smith C, Riboldi-Tunnicliffe A, Grant EJ, Gras S. </i> iScience, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0042612","term_name":"MHC class I protein complex","term_namespace":"Cellular component","term_ontology":"GO","ec_id":"ECO:0006317","ec_ontology":"ECO","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03212r023","statement":[{"text":"Two peptides, N138-146 and N159-167, were not immunogenic in COVID-19-recovered individuals (Isabel Schulien et al., 2021), whereas three peptides, namely N219-227 (Isabel Schulien et al., 2021), N222-230 (Isabel Schulien et al., 2021), and N316-324 (Isabel Schulien et al., 2021; Habel et al., 2020), were immunogenic in COVID-19 recovered individuals, further highlighting the importance of further investigation into these epitopes.","type":"Results"},{"text":"The most stable pHLA complexes were the one with the N222-230 (Tm of 55°C) and N316-324 (Tm of 49°C) peptides, followed by the one with N219-227, N226-234, and N351-359 peptides with a Tm of ~40°C (Table 1, Figure S1). Surprisingly, the Tm was ~35°C for complexes with the NTD-derived peptides N138-146 and N159-167, an extremely low Tm value for pHLA-A*02:01 complexes (Valkenburg et al., 2016; Blaha et al., 2019; Khan et al., 2000).","type":"Results"},{"text":"The three peptides that resulted in a pHLA complex with a Tm above 40°C were recently described as immunogenic in COVID-19-recovered patients (N219-227 (Isabel Schulien et al., 2021), N222-230 (Ferretti et al., 2020; Isabel Schulien et al., 2021), and N316-324 (Habel et al., 2020; Isabel Schulien et al., 2021)), whereas the two peptides leading to a pHLA with a Tm below 40°C were described as non-immunogenic (N138-146 and N159-167 (Isabel Schulien et al., 2021)) (Table 1). This suggests that indeed pHLA complex stability may play a role in peptide immunogenicity.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-29T10:49:40.498Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"See also the cellular component term 'MHC class I peptide loading complex ; GO:0042824'.","term_def":"\"A transmembrane protein complex composed of a MHC class I alpha chain and an invariant beta2-microglobin chain, and with or without a bound peptide antigen. Class I here refers to classical class I molecules.\" [GOC:add, GOC:jl, ISBN:0120781859, ISBN:0781735149]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":219,"end":227,"reference_id":"33521593","reference_source":"pmid","reference_html":"The presentation of SARS-CoV-2 peptides by the common HLA-A<sup>∗</sup>02:01 molecule. <i> Szeto C, Chatzileontiadou DSM, Nguyen AT, Sloane H, Lobos CA, Jayasinghe D, Halim H, Smith C, Riboldi-Tunnicliffe A, Grant EJ, Gras S. </i> iScience, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0042288","term_name":"MHC class I protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006317","ec_ontology":"ECO","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"Q861F7","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P61769","partner_start":null,"partner_end":null}],"region_id":"DP03212r024","statement":[{"text":"Two peptides, N138-146 and N159-167, were not immunogenic in COVID-19-recovered individuals (Isabel Schulien et al., 2021), whereas three peptides, namely N219-227 (Isabel Schulien et al., 2021), N222-230 (Isabel Schulien et al., 2021), and N316-324 (Isabel Schulien et al., 2021; Habel et al., 2020), were immunogenic in COVID-19 recovered individuals, further highlighting the importance of further investigation into these epitopes.","type":"Results"},{"text":"The most stable pHLA complexes were the one with the N222-230 (Tm of 55°C) and N316-324 (Tm of 49°C) peptides, followed by the one with N219-227, N226-234, and N351-359 peptides with a Tm of ~40°C (Table 1, Figure S1). Surprisingly, the Tm was ~35°C for complexes with the NTD-derived peptides N138-146 and N159-167, an extremely low Tm value for pHLA-A*02:01 complexes (Valkenburg et al., 2016; Blaha et al., 2019; Khan et al., 2000).","type":"Results"},{"text":"The three peptides that resulted in a pHLA complex with a Tm above 40°C were recently described as immunogenic in COVID-19-recovered patients (N219-227 (Isabel Schulien et al., 2021), N222-230 (Ferretti et al., 2020; Isabel Schulien et al., 2021), and N316-324 (Habel et al., 2020; Isabel Schulien et al., 2021)), whereas the two peptides leading to a pHLA with a Tm below 40°C were described as non-immunogenic (N138-146 and N159-167 (Isabel Schulien et al., 2021)) (Table 1). This suggests that indeed pHLA complex stability may play a role in peptide immunogenicity.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-29T10:44:39.214Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Note that this term does not include binding to the antigen peptide bound to the MHC protein. Consider also annotating to the molecular function term 'peptide antigen binding ; GO:0042605' or one of its children.","term_def":"\"Binding to a major histocompatibility complex class I molecule; a set of molecules displayed on cell surfaces that are responsible for lymphocyte recognition and antigen presentation.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":222,"end":230,"reference_id":"33521593","reference_source":"pmid","reference_html":"The presentation of SARS-CoV-2 peptides by the common HLA-A<sup>∗</sup>02:01 molecule. <i> Szeto C, Chatzileontiadou DSM, Nguyen AT, Sloane H, Lobos CA, Jayasinghe D, Halim H, Smith C, Riboldi-Tunnicliffe A, Grant EJ, Gras S. </i> iScience, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0042288","term_name":"MHC class I protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006317","ec_ontology":"ECO","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"Q861F7","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P61769","partner_start":null,"partner_end":null}],"region_id":"DP03212r025","statement":[{"text":"Two peptides, N138-146 and N159-167, were not immunogenic in COVID-19-recovered individuals (Isabel Schulien et al., 2021), whereas three peptides, namely N219-227 (Isabel Schulien et al., 2021), N222-230 (Isabel Schulien et al., 2021), and N316-324 (Isabel Schulien et al., 2021; Habel et al., 2020), were immunogenic in COVID-19 recovered individuals, further highlighting the importance of further investigation into these epitopes.","type":"Results"},{"text":"The most stable pHLA complexes were the one with the N222-230 (Tm of 55°C) and N316-324 (Tm of 49°C) peptides, followed by the one with N219-227, N226-234, and N351-359 peptides with a Tm of ~40°C (Table 1, Figure S1). Surprisingly, the Tm was ~35°C for complexes with the NTD-derived peptides N138-146 and N159-167, an extremely low Tm value for pHLA-A*02:01 complexes (Valkenburg et al., 2016; Blaha et al., 2019; Khan et al., 2000).","type":"Results"},{"text":"The three peptides that resulted in a pHLA complex with a Tm above 40°C were recently described as immunogenic in COVID-19-recovered patients (N219-227 (Isabel Schulien et al., 2021), N222-230 (Ferretti et al., 2020; Isabel Schulien et al., 2021), and N316-324 (Habel et al., 2020; Isabel Schulien et al., 2021)), whereas the two peptides leading to a pHLA with a Tm below 40°C were described as non-immunogenic (N138-146 and N159-167 (Isabel Schulien et al., 2021)) (Table 1). This suggests that indeed pHLA complex stability may play a role in peptide immunogenicity.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-29T10:44:21.619Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Note that this term does not include binding to the antigen peptide bound to the MHC protein. Consider also annotating to the molecular function term 'peptide antigen binding ; GO:0042605' or one of its children.","term_def":"\"Binding to a major histocompatibility complex class I molecule; a set of molecules displayed on cell surfaces that are responsible for lymphocyte recognition and antigen presentation.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":222,"end":230,"reference_id":"33184509","reference_source":"pmid","reference_html":"Characterization of pre-existing and induced SARS-CoV-2-specific CD8<sup>+</sup> T cells. <i> Schulien I, Kemming J, Oberhardt V, Wild K, Seidel LM, Killmer S, Sagar, Daul F, Salvat Lago M, Decker A, Luxenburger H, Binder B, Bettinger D, Sogukpinar O, Rieg S, Panning M, Huzly D, Schwemmle M, Kochs G, Waller CF, Nieters A, Duerschmied D, Emmerich F, Mei HE, Schulz AR, Llewellyn-Lacey S, Price DA, Boettler T, Bengsch B, Thimme R, Hofmann M, Neumann-Haefelin C. </i> Nat Med, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0052572","term_name":"response to host immune response","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0005580","ec_ontology":"ECO","ec_name":"flow cytometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03212r026","statement":[{"text":"SARS-CoV-2-specific memory CD8+ T cells exhibited functional characteristics comparable to influenza-specific CD8+ T cells and were detectable in SARS-CoV-2 convalescent individuals who were seronegative for anti-SARS-CoV-2 antibodies targeting spike (S) and nucleoprotein (N). These results define cross-reactive and induced SARS-CoV-2-specific CD8+ T cell responses as potentially important determinants of immune protection in mild SARS-CoV-2 infection.","type":"Abstract"},{"text":"Percentage of convalescent SARS-CoV-2 individuals with a positive response toward HLA-A- and HLA-B-restricted SARS-CoV-2 peptides and the strength of individual responses as percent IFN-γ+ of CD8+ T cells.","type":"Figure"},{"text":"Based on Figure 1d, region 222-230 is an immunogenic peptide toward HLA-A-.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-29T10:47:04.048Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detecting the immune response of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.\" [GOC:mtg_pamgo_17jul06]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":44,"reference_id":"34665939","reference_source":"pmid","reference_html":"Crystal structures of the SARS-CoV-2 nucleocapsid protein C-terminal domain and development of nucleocapsid-targeting nanobodies. <i> Jia Z, Liu C, Chen Y, Jiang H, Wang Z, Yao J, Yang J, Zhu J, Zhang B, Yuchi Z. </i> FEBS J, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0019865","term_name":"immunoglobulin binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03212r027","statement":[{"text":"We characterized the interactions between sdAbs and N‐protein using isothermal titration calorimetry (ITC). We first tested their binding to the FLN. Four out of six sdAbs showed clear binding. The Kd values of positive sdAb‐N2, sdAb‐N3, sdAb‐N5, and sdAb‐N6 are 1.75 µm, 4.37 µm, 3.97 µm, and 3.53 µm, respectively (Fig. 2). Next, we tested the binding of these four sdAbs with NLC protein. Only sdAb‐N2 and sdAb‐N3 showed positive results with Kd values of 2.24 µm and 1.09 µm, respectively (Fig. 3), indicating that the binding of sdAbs‐N5 and sdAb‐N6 requires the presence of the N‐arm or C‐tail of N‐protein.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-01-18T11:32:43.834Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an immunoglobulin.\" [GOC:ma]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":362,"end":419,"reference_id":"34665939","reference_source":"pmid","reference_html":"Crystal structures of the SARS-CoV-2 nucleocapsid protein C-terminal domain and development of nucleocapsid-targeting nanobodies. <i> Jia Z, Liu C, Chen Y, Jiang H, Wang Z, Yao J, Yang J, Zhu J, Zhang B, Yuchi Z. </i> FEBS J, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0019865","term_name":"immunoglobulin binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03212r028","statement":[{"text":"We characterized the interactions between sdAbs and N‐protein using isothermal titration calorimetry (ITC). We first tested their binding to the FLN. Four out of six sdAbs showed clear binding. The Kd values of positive sdAb‐N2, sdAb‐N3, sdAb‐N5, and sdAb‐N6 are 1.75 µm, 4.37 µm, 3.97 µm, and 3.53 µm, respectively (Fig. 2). Next, we tested the binding of these four sdAbs with NLC protein. Only sdAb‐N2 and sdAb‐N3 showed positive results with Kd values of 2.24 µm and 1.09 µm, respectively (Fig. 3), indicating that the binding of sdAbs‐N5 and sdAb‐N6 requires the presence of the N‐arm or C‐tail of N‐protein.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-01-18T11:32:45.147Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an immunoglobulin.\" [GOC:ma]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":43,"reference_id":"34095780","reference_source":"pmid","reference_html":"Characterization of SARS-CoV-2 nucleocapsid protein reveals multiple functional consequences of the C-terminal domain. <i> Wu C, Qavi AJ, Hachim A, Kavian N, Cole AR, Moyle AB, Wagner ND, Sweeney-Gibbons J, Rohrs HW, Gross ML, Peiris JSM, Basler CF, Farnsworth CW, Valkenburg SA, Amarasinghe GK, Leung DW. </i> iScience, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":null,"ec_id":"ECO:0001253","ec_ontology":"ECO","ec_name":"quantitative mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03212r029","statement":[{"text":"Removal of the Narm and Carm (NNTD-LKR-CTD) results in two major species that are similar to NWT. However, both NNTD-LKR-CTD populations display reduced polydispersity (narrower peak width, Figure S2A), suggesting that both Narm and Carm contribute to N oligomerization.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-01-18T11:41:20.970Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":370,"end":419,"reference_id":"34095780","reference_source":"pmid","reference_html":"Characterization of SARS-CoV-2 nucleocapsid protein reveals multiple functional consequences of the C-terminal domain. <i> Wu C, Qavi AJ, Hachim A, Kavian N, Cole AR, Moyle AB, Wagner ND, Sweeney-Gibbons J, Rohrs HW, Gross ML, Peiris JSM, Basler CF, Farnsworth CW, Valkenburg SA, Amarasinghe GK, Leung DW. </i> iScience, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":null,"ec_id":"ECO:0001253","ec_ontology":"ECO","ec_name":"quantitative mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03212r030","statement":[{"text":"Removal of the Narm and Carm (NNTD-LKR-CTD) results in two major species that are similar to NWT. However, both NNTD-LKR-CTD populations display reduced polydispersity (narrower peak width, Figure S2A), suggesting that both Narm and Carm contribute to N oligomerization.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-01-18T11:41:19.269Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":370,"end":419,"reference_id":"34095780","reference_source":"pmid","reference_html":"Characterization of SARS-CoV-2 nucleocapsid protein reveals multiple functional consequences of the C-terminal domain. <i> Wu C, Qavi AJ, Hachim A, Kavian N, Cole AR, Moyle AB, Wagner ND, Sweeney-Gibbons J, Rohrs HW, Gross ML, Peiris JSM, Basler CF, Farnsworth CW, Valkenburg SA, Amarasinghe GK, Leung DW. </i> iScience, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0035613","term_name":"RNA stem-loop binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005632","ec_ontology":"ECO","ec_name":"fluorescence anisotropy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03212r031","statement":[{"text":"Furthermore, the Narm and Carm may contribute more to slRNA binding than ssRNA because the impact on N binding is more pronounced after removal of the Narm or Carm (Figure S3C).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-01-18T11:29:32.024Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a stem-loop in an RNA molecule. An RNA stem-loop is a secondary RNA structure consisting of a double-stranded RNA (dsRNA) stem and a terminal loop.\" [GOC:sart, PMID:16568238, PMID:20455544]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":43,"reference_id":"34095780","reference_source":"pmid","reference_html":"Characterization of SARS-CoV-2 nucleocapsid protein reveals multiple functional consequences of the C-terminal domain. <i> Wu C, Qavi AJ, Hachim A, Kavian N, Cole AR, Moyle AB, Wagner ND, Sweeney-Gibbons J, Rohrs HW, Gross ML, Peiris JSM, Basler CF, Farnsworth CW, Valkenburg SA, Amarasinghe GK, Leung DW. </i> iScience, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0035613","term_name":"RNA stem-loop binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005632","ec_ontology":"ECO","ec_name":"fluorescence anisotropy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03212r032","statement":[{"text":"Furthermore, the Narm and Carm may contribute more to slRNA binding than ssRNA because the impact on N binding is more pronounced after removal of the Narm or Carm (Figure S3C).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-01-18T11:29:31.115Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a stem-loop in an RNA molecule. An RNA stem-loop is a secondary RNA structure consisting of a double-stranded RNA (dsRNA) stem and a terminal loop.\" [GOC:sart, PMID:16568238, PMID:20455544]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":43,"reference_id":"34095780","reference_source":"pmid","reference_html":"Characterization of SARS-CoV-2 nucleocapsid protein reveals multiple functional consequences of the C-terminal domain. <i> Wu C, Qavi AJ, Hachim A, Kavian N, Cole AR, Moyle AB, Wagner ND, Sweeney-Gibbons J, Rohrs HW, Gross ML, Peiris JSM, Basler CF, Farnsworth CW, Valkenburg SA, Amarasinghe GK, Leung DW. </i> iScience, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0035613","term_name":"RNA stem-loop binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03212r033","statement":[{"text":"Truncation of the Narm results in an increase of the RNA-free peak (p3), suggesting that N truncations can alter the structure of N and correspondingly impact RNA binding and oligomerization. When both Narm and Carm were removed, we observed an even greater shift to p3, suggesting that both arms contribute to RNA-binding interactions.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-01-18T11:28:12.456Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a stem-loop in an RNA molecule. An RNA stem-loop is a secondary RNA structure consisting of a double-stranded RNA (dsRNA) stem and a terminal loop.\" [GOC:sart, PMID:16568238, PMID:20455544]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":370,"end":419,"reference_id":"34095780","reference_source":"pmid","reference_html":"Characterization of SARS-CoV-2 nucleocapsid protein reveals multiple functional consequences of the C-terminal domain. <i> Wu C, Qavi AJ, Hachim A, Kavian N, Cole AR, Moyle AB, Wagner ND, Sweeney-Gibbons J, Rohrs HW, Gross ML, Peiris JSM, Basler CF, Farnsworth CW, Valkenburg SA, Amarasinghe GK, Leung DW. </i> iScience, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0035613","term_name":"RNA stem-loop binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03212r034","statement":[{"text":"Truncation of the Narm results in an increase of the RNA-free peak (p3), suggesting that N truncations can alter the structure of N and correspondingly impact RNA binding and oligomerization. When both Narm and Carm were removed, we observed an even greater shift to p3, suggesting that both arms contribute to RNA-binding interactions.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-01-18T11:28:10.655Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a stem-loop in an RNA molecule. An RNA stem-loop is a secondary RNA structure consisting of a double-stranded RNA (dsRNA) stem and a terminal loop.\" [GOC:sart, PMID:16568238, PMID:20455544]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":370,"end":419,"reference_id":"34095780","reference_source":"pmid","reference_html":"Characterization of SARS-CoV-2 nucleocapsid protein reveals multiple functional consequences of the C-terminal domain. <i> Wu C, Qavi AJ, Hachim A, Kavian N, Cole AR, Moyle AB, Wagner ND, Sweeney-Gibbons J, Rohrs HW, Gross ML, Peiris JSM, Basler CF, Farnsworth CW, Valkenburg SA, Amarasinghe GK, Leung DW. </i> iScience, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03212r035","statement":[{"text":"To determine if N regions that impact RNA binding also impact liquid droplet formation, we next examined the role of Narm and Carm. NNTD-LKR-CTD-Carm behaves similarly to NWT, having loose coils in p1 (Figure 4B, middle left) and forming spherical liquid droplets in p2 (Figure 4B, middle right). However, examination of p2 from NNTD-LKR-CTD (Figure 4B, bottom right) revealed a much smaller population of liquid droplets (red arrow) and mostly crystal-like needle aggregates, suggesting that the Carm is important for droplet formation. A transition from spherical liquids to needle-like solids is consistent with the liquid-to-solid transitions observed for other proteins that undergo phase separation (Patel et al., 2015).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-01-18T11:40:58.478Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":68,"reference_id":"38153183","reference_source":"pmid","reference_html":"The disordered N-terminal tail of SARS-CoV-2 Nucleocapsid protein forms a dynamic complex with RNA. <i> Cubuk J, Alston JJ, Incicco JJ, Holehouse AS, Hall KB, Stuchell-Brereton MD, Soranno A. </i> Nucleic Acids Res, 2024","date":"2024-03-26T10:40:28.651Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0008266","term_name":"poly(U) RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","region_id":"DP03212r036","statement":[{"text":"With increasing concentration of poly(rU), we observe a modulation of the transfer efficiency distribution with a shift toward lower transfer efficiencies, from a mean transfer efficiency E = 0.709 ± 0.009 in absence of RNA to E = 0.542 ± 0.003 in presence of 10 μM of poly(rU) (Figure 2). This observation clearly supports that the disordered tail is directly affected by the binding of RNA.","type":"Results"},{"text":"Based on these observations, the affinity of the NTD-RBD constructs appears to be ∼40–80 times tighter than that of the RBD alone, pointing to a direct contribution of the disordered region in favoring RNA binding.","type":"Results"},{"text":"Taken together with the tighter Kint observed for NTD-RBD, these observations indicate that the complex between RNA and NTD-RBD is not solely initiated by contacts with the RBD domain but instead relies on dynamic interactions between the RNA and both RBD and NTD.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a sequence of uracil residues in an RNA molecule.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":68,"end":68,"position":"Specific residue","statements":[{"type":"Results","text":"All constructs have been expressed in E.coli, purified, and labeled with Alexa Fluor 488 and Alexa Fluor 594."}]},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":1,"end":1,"position":"Specific residue","statements":[{"type":"Results","text":"All constructs have been expressed in E.coli, purified, and labeled with Alexa Fluor 488 and Alexa Fluor 594."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met1Cys","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Cysteine mutations were introduced in the wild-type sequence to enable fluorophore addition to the constructs via maleimide-thiol chemistry."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg68Cys","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Cysteine mutations were introduced in the wild-type sequence to enable fluorophore addition to the constructs via maleimide-thiol chemistry."}]}],"interaction_partner":[{"db":"ChEBI","id":"8758","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-26T13:31:44.481Z"}},{"start":1,"end":68,"reference_id":"38153183","reference_source":"pmid","reference_html":"The disordered N-terminal tail of SARS-CoV-2 Nucleocapsid protein forms a dynamic complex with RNA. <i> Cubuk J, Alston JJ, Incicco JJ, Holehouse AS, Hall KB, Stuchell-Brereton MD, Soranno A. </i> Nucleic Acids Res, 2024","date":"2024-03-26T15:24:21.289Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":1,"end":1,"position":"Specific residue","statements":[{"type":"Results","text":"All constructs have been expressed in E.coli, purified, and labeled with Alexa Fluor 488 and Alexa Fluor 594."}]},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":68,"end":68,"position":"Specific residue","statements":[{"type":"Results","text":"All constructs have been expressed in E.coli, purified, and labeled with Alexa Fluor 488 and Alexa Fluor 594."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met1Cys","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Cysteine mutations were introduced in the wild-type sequence to enable fluorophore addition to the constructs via maleimide-thiol chemistry."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg68Cys","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Cysteine mutations were introduced in the wild-type sequence to enable fluorophore addition to the constructs via maleimide-thiol chemistry."}]}],"region_id":"DP03212r037","statement":[{"text":"ns-FCS measurements of the NTDL-RBD in the absence of RNA reveals a reconfiguration time of approximately 110 ± 20 ns, which is marginally affected upon binding RNA, with a reconfiguration time of the NTD spanning a range between 94 and 108 ns across the different lengths tested from (rU)10 to (rU)40 (Supplementary Figure S3). This indicates that the NTD remains largely dynamic and contacts must occur only across a small set of nucleotides.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-26T16:32:26.609Z"}},{"start":1,"end":68,"reference_id":"38153183","reference_source":"pmid","reference_html":"The disordered N-terminal tail of SARS-CoV-2 Nucleocapsid protein forms a dynamic complex with RNA. <i> Cubuk J, Alston JJ, Incicco JJ, Holehouse AS, Hall KB, Stuchell-Brereton MD, Soranno A. </i> Nucleic Acids Res, 2024","date":"2024-03-26T15:27:45.218Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:0008266","term_name":"poly(U) RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro13Leu","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Glu31Ser33del","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met1Cys","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Cysteine mutations were introduced in the wild-type sequence to enable fluorophore addition to the constructs via maleimide-thiol chemistry."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg68Cys","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Cysteine mutations were introduced in the wild-type sequence to enable fluorophore addition to the constructs via maleimide-thiol chemistry."}]},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":1,"end":1,"position":"Specific residue","statements":[{"type":"Results","text":"All constructs have been expressed in E.coli, purified, and labeled with Alexa Fluor 488 and Alexa Fluor 594."}]},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":68,"end":68,"position":"Specific residue","statements":[{"type":"Results","text":"All constructs have been expressed in E.coli, purified, and labeled with Alexa Fluor 488 and Alexa Fluor 594."}]}],"ec_go":"IMP","region_id":"DP03212r043","statement":[{"text":"These observations overall support that the mode of binding of RNA is similar between NTDL RBD (Wuhan-Hu-1) and OmNTDL-RBD (as supported by the same transfer efficiency in the bound state), but with different affinities (as indicated by the concentration dependence).","type":"Results"},{"text":"(C) Comparison of binding affinity for Wuhan-Hu-1 (red) and Omicron variant (cyan) reveals different affinities for poly(rU). Solid lines are fit to Equation (2).","type":"Figure"},{"text":"Overall, our observations indicate that small changes in the sequence composition of NTD may not alter the overall conformational behavior of the chain, but can significantly impact the binding affinity.","type":"Results"},{"text":"Our results on the impact of the Omicron NTD mutations clearly show that alterations of three amino acids in this IDR are sufficient to decrease the interaction affinity between the construct and the nucleic acid. ","type":"Discussion"},{"text":"The authors assessed the poly(U) RNA binding capability of the NTD Omicron variant (that carries a proline to leucine substitution in position 13 and deletion of three residues between positions 31 and 33) and found it to be of lesser affinity that the wildtype/ Wuhan-Hu-1 type.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a sequence of uracil residues in an RNA molecule.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"ChEBI","id":"8758","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-26T16:32:39.145Z"}},{"start":1,"end":43,"reference_id":"38153183","reference_source":"pmid","reference_html":"The disordered N-terminal tail of SARS-CoV-2 Nucleocapsid protein forms a dynamic complex with RNA. <i> Cubuk J, Alston JJ, Incicco JJ, Holehouse AS, Hall KB, Stuchell-Brereton MD, Soranno A. </i> Nucleic Acids Res, 2024","date":"2024-08-26T15:06:44.403Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP03212r044","statement":[{"text":"Figure 1. - Panels A and B report the spectra obtained through the mr_CON//HN experiment. The 2D HN spectrum (A) shows a set of well-isolated signals deriving from the globular NTD domain as well as a number of signals, clustered in a narrow central region of the spectrum, deriving from the IDRs. The 2D CON spectrum (B) allows achieving the necessary resolution to investigate resonances from IDRs, including signals of proline residues. While IDR peaks fall in a very crowded region of the HN spectrum (1.1 ppm on 1H dimension), they are well dispersed in the CON spectrum (7.2 ppm on 13C dimension), as indicated by the two boxes. A zoom of a region of the two spectra centered at 120 ppm for 15N is reported in panels (C,D) to stress this concept.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:38:41.331Z"}},{"start":181,"end":248,"reference_id":"35883485","reference_source":"pmid","reference_html":"NMR Reveals Specific Tracts within the Intrinsically Disordered Regions of the SARS-CoV-2 Nucleocapsid Protein Involved in RNA Encountering. <i> Pontoriero L, Schiavina M, Korn SM, Schlundt A, Pierattelli R, Felli IC. </i> Biomolecules, 2022","date":"2024-08-26T15:06:13.666Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP03212r045","statement":[{"text":"Figure 1. - Panels A and B report the spectra obtained through the mr_CON//HN experiment. The 2D HN spectrum (A) shows a set of well-isolated signals deriving from the globular NTD domain as well as a number of signals, clustered in a narrow central region of the spectrum, deriving from the IDRs. The 2D CON spectrum (B) allows achieving the necessary resolution to investigate resonances from IDRs, including signals of proline residues. While IDR peaks fall in a very crowded region of the HN spectrum (1.1 ppm on 1H dimension), they are well dispersed in the CON spectrum (7.2 ppm on 13C dimension), as indicated by the two boxes. A zoom of a region of the two spectra centered at 120 ppm for 15N is reported in panels (C,D) to stress this concept.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:38:42.012Z"}},{"start":181,"end":248,"reference_id":"35883485","reference_source":"pmid","reference_html":"NMR Reveals Specific Tracts within the Intrinsically Disordered Regions of the SARS-CoV-2 Nucleocapsid Protein Involved in RNA Encountering. <i> Pontoriero L, Schiavina M, Korn SM, Schlundt A, Pierattelli R, Felli IC. </i> Biomolecules, 2022","date":"2024-08-26T14:58:14.409Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"EXP","region_id":"DP03212r046","statement":[{"text":"NMR spectroscopy reveals at the residue level the importance of the two disordered regions for the interaction with RNA.","type":"Results"},{"text":"As an example, Figure 3 shows the enlargement of selected portions of the 2D CON in diagnostic spectral regions such as that of glycine (top) and proline residues (bottom). Addition of 0.1 equivalents of RNA shows intensity changes for specific cross-peaks, suggesting the presence of preferred IDR sites for the interaction with RNA.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"RNAcentral","id":"URS00026814A2_2697049","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:36:03.902Z"}},{"start":181,"end":248,"reference_id":"35883485","reference_source":"pmid","reference_html":"NMR Reveals Specific Tracts within the Intrinsically Disordered Regions of the SARS-CoV-2 Nucleocapsid Protein Involved in RNA Encountering. <i> Pontoriero L, Schiavina M, Korn SM, Schlundt A, Pierattelli R, Felli IC. </i> Biomolecules, 2022","date":"2024-08-26T15:04:01.562Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP03212r047","statement":[{"text":"The results indicate that the NTR construct has a higher affinity towards RNA compared to the NTD alone as indicated by gel shifts observed at lower concentrations. While both NTD-containing proteins show binding to RNA, the two IDRs flanking the NTD visibly increase affinity to RNA.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:37:45.280Z"}},{"start":1,"end":43,"reference_id":"35883485","reference_source":"pmid","reference_html":"NMR Reveals Specific Tracts within the Intrinsically Disordered Regions of the SARS-CoV-2 Nucleocapsid Protein Involved in RNA Encountering. <i> Pontoriero L, Schiavina M, Korn SM, Schlundt A, Pierattelli R, Felli IC. </i> Biomolecules, 2022","date":"2024-08-26T15:05:36.039Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP03212r048","statement":[{"text":"The results indicate that the NTR construct has a higher affinity towards RNA compared to the NTD alone as indicated by gel shifts observed at lower concentrations. While both NTD-containing proteins show binding to RNA, the two IDRs flanking the NTD visibly increase affinity to RNA.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:36:54.522Z"}},{"start":1,"end":43,"reference_id":"35883485","reference_source":"pmid","reference_html":"NMR Reveals Specific Tracts within the Intrinsically Disordered Regions of the SARS-CoV-2 Nucleocapsid Protein Involved in RNA Encountering. <i> Pontoriero L, Schiavina M, Korn SM, Schlundt A, Pierattelli R, Felli IC. </i> Biomolecules, 2022","date":"2024-08-26T14:58:45.964Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"EXP","region_id":"DP03212r049","statement":[{"text":"NMR spectroscopy reveals at the residue level the importance of the two disordered regions for the interaction with RNA.","type":"Results"},{"text":"As an example, Figure 3 shows the enlargement of selected portions of the 2D CON in diagnostic spectral regions such as that of glycine (top) and proline residues (bottom). Addition of 0.1 equivalents of RNA shows intensity changes for specific cross-peaks, suggesting the presence of preferred IDR sites for the interaction with RNA.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"RNAcentral","id":"URS00026814A2_2697049","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:36:07.901Z"}},{"start":1,"end":43,"reference_id":"35883485","reference_source":"pmid","reference_html":"NMR Reveals Specific Tracts within the Intrinsically Disordered Regions of the SARS-CoV-2 Nucleocapsid Protein Involved in RNA Encountering. <i> Pontoriero L, Schiavina M, Korn SM, Schlundt A, Pierattelli R, Felli IC. </i> Biomolecules, 2022","date":"2024-08-26T15:03:06.172Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"RNAcentral","id":"URS00026814A2_2697049","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03212r050","statement":[{"text":"The results indicate that the NTR construct has a higher affinity towards RNA compared to the NTD alone as indicated by gel shifts observed at lower concentrations. While both NTD-containing proteins show binding to RNA, the two IDRs flanking the NTD visibly increase affinity to RNA.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:36:35.466Z"}},{"start":181,"end":248,"reference_id":"35883485","reference_source":"pmid","reference_html":"NMR Reveals Specific Tracts within the Intrinsically Disordered Regions of the SARS-CoV-2 Nucleocapsid Protein Involved in RNA Encountering. <i> Pontoriero L, Schiavina M, Korn SM, Schlundt A, Pierattelli R, Felli IC. </i> Biomolecules, 2022","date":"2024-08-26T15:03:34.599Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"RNAcentral","id":"URS00026814A2_2697049","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03212r051","statement":[{"text":"The results indicate that the NTR construct has a higher affinity towards RNA compared to the NTD alone as indicated by gel shifts observed at lower concentrations. While both NTD-containing proteins show binding to RNA, the two IDRs flanking the NTD visibly increase affinity to RNA.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:36:33.083Z"}}],"regions_counter":51,"released":"2021_12","sequence":"MSDNGPQNQRNAPRITFGGPSDSTGSNQNGERSGARSKQRRPQGLPNNTASWFTALTQHGKEDLKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGANKDGIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYAEGSRGGSQASSRSSSRSRNSSRNSTPGSSRGTSPARMAGNGGDAALALLLLDRLNQLESKMSGKGQQQQGQTVTKKSAAEASKKPRQKRTATKAYNVTQAFGRRGPEQTQGNFGDQELIRQGTDYKHWPQIAQFAPSASAFFGMSRIGMEVTPSGTWLTYTGAIKLDDKDPNFKDQVILLNKHIDAYKTFPPTEPKKDKKKKADETQALPQRQKKQQTVTLLPAADLDDFSKQLQQSMSSADSTQA","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Nidovirales","Cornidovirineae","Coronaviridae","Orthocoronavirinae","Betacoronavirus","Sarbecovirus"],"dataset":["Viral proteins","Condensates-related proteins","RNA-binding proteins"],"UniParc":"UPI0013520DDB","uniref100":"UniRef100_P0DTC9","uniref90":"UniRef90_P0DTC9","uniref50":"UniRef50_P0DTC9","genes":[{"name":{"value":"N","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04096","url":"https://hamap.expasy.org/unirule/MF_04096"}}]}}],"disorder_content":0.5178997613365155,"disprot_consensus":{"full":[{"start":1,"end":68,"type":"D"},{"start":172,"end":263,"type":"D"},{"start":362,"end":362,"type":"F"},{"start":363,"end":419,"type":"D"}],"Structural state":[{"start":1,"end":68,"type":"D"},{"start":172,"end":263,"type":"D"},{"start":363,"end":419,"type":"D"}],"Molecular function":[{"start":1,"end":68,"type":"F"},{"start":174,"end":248,"type":"F"},{"start":362,"end":419,"type":"F"}],"Disorder function":[{"start":1,"end":43,"type":"F"},{"start":172,"end":248,"type":"F"}],"Cellular component":[{"start":182,"end":197,"type":"F"},{"start":219,"end":230,"type":"F"}],"Biological process":[{"start":222,"end":230,"type":"F"}]}},{"disprot_id":"DP03213","acc":"P69411","creator":"jnilsson","date":"2021-02-10T10:08:43.426Z","features":{"pfam":[{"id":"PF16358","name":"RcsF lipoprotein","start":26,"end":132}],"gene3D":[]},"length":134,"name":"Outer membrane lipoprotein RcsF","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":17,"end":46,"reference_id":"21454485","reference_source":"pmid","reference_html":"Crystal structure of the outer membrane protein RcsF, a new substrate for the periplasmic protein-disulfide isomerase DsbC. <i> Leverrier P, Declercq JP, Denoncin K, Vertommen D, Hiniker A, Cho SH, Collet JF. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2Y1B"}],"region_id":"DP03213r001","statement":[{"text":"N-terminal Segment of RcsF Is Disordered","type":"Results"},{"text":"The protein that was used for crystallization was expressed as a soluble protein containing a C-terminal His tag and lacking the first 16 residues corresponding to the signal peptide and the lipobox (remember that RcsF is a lipoprotein whose lipid moiety is anchored in the outer membrane). However, the observed electron density begins at residue Pro48, suggesting that about 30 residues in the N-terminal part of the protein are completely disordered. The integrity of the sequence of the purified protein was confirmed using mass spectrometry to rule out any nonspecific proteolytic cleavage of the protein during expression and purification. The measured average mass was 13,609 \u0006 2 Da, which is in good agreement with a theoretical average mass of 13,612 Da taking into account the complete processing of the N-terminal methionine.","type":"Results"},{"text":"Therefore, we decided to study the ability of a truncated version of the protein (RcsFtrunc), corresponding to residues Pro48 to Lys134, to induce the Rcs phosphorelay when expressed in the periplasm, using strain mucoidity as a read-out. As explained in the Introduction, induction of the Rcs system leads to colanic acid production, which results in a distinctive mucoid phenotype. As indicated in Table 2, we observed that expression of RcsFtrunc leads to a mucoid phenotype comparable with that observed when wild-type RcsF is expressed unanchored in the periplasm (supplemental Fig. S1). Thus, we can conclude from this experiment that the fraction of the polypeptide chain that is disordered in the crystal is not required for signaling, at least when RcsF is expressed as a soluble protein in the periplasm.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-02-12T15:15:16.689Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MRALPICLVALMLSGCSMLSRSPVEPVQSTAPQPKAEPAKPKAPRATPVRIYTNAEELVGKPFRDLGEVSGDSCQASNQDSPPSIPTARKRMQINASKMKANAVLLHSCEVTSGTPGCYRQAVCIGSALNITAK","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":[],"UniParc":"UPI0000133484","uniref100":"UniRef100_P69412","uniref90":"UniRef90_P69412","uniref50":"UniRef50_P69412","genes":[{"name":{"value":"rcsF","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00976","url":"https://hamap.expasy.org/unirule/MF_00976"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"1459951","url":"http://www.ncbi.nlm.nih.gov/pubmed/1459951","alternativeUrl":"https://europepmc.org/abstract/MED/1459951"}}]},"olnNames":[{"value":"b0196"},{"value":"JW0192"}]}],"alphafold_very_low_content":0.007462686567164179,"disorder_content":0.22388059701492538,"disprot_consensus":{"full":[{"start":17,"end":46,"type":"D"}],"Structural state":[{"start":17,"end":46,"type":"D"}]}},{"disprot_id":"DP03214","acc":"O60508","creator":"fquaglia","date":"2021-02-16T10:56:06.103Z","features":{"pfam":[{"id":"PF00400","name":"WD domain, G-beta repeat","start":279,"end":316},{"id":"PF00400","name":"WD domain, G-beta repeat","start":323,"end":360},{"id":"PF00400","name":"WD domain, G-beta repeat","start":365,"end":404},{"id":"PF00400","name":"WD domain, G-beta repeat","start":409,"end":445},{"id":"PF00400","name":"WD domain, G-beta repeat","start":499,"end":536},{"id":"PF00400","name":"WD domain, G-beta repeat","start":542,"end":579}],"gene3D":[]},"length":579,"name":"Pre-mRNA-processing factor 17","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":82,"reference_id":"28502770","reference_source":"pmid","reference_html":"An Atomic Structure of the Human Spliceosome. <i> Zhang X, Yan C, Hang J, Finci LI, Lei J, Shi Y. </i> Cell, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5XJC"}],"region_id":"DP03214r001","statement":[{"text":"The N-terminal region of CDC40 is disordered, as referenced in Table S2 and confirmed upon visual inspection of the structure.","type":"Curator statement"}],"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MSAAIAALAASYGSGSGSESDSDSESSRCPLPAADSLMHLTKSPSSKPSLAVAVDSAPEVAVKEDLETGVHLDPAVKEVQYNPTYETMFAPEFGPENPFRTQQMAAPRNMLSGYAEPAHINDFMFEQQRRTFATYGYALDPSLDNHQVSAKYIGSVEEAEKNQGLTVFETGQKKTEKRKKFKENDASNIDGFLGPWAKYVDEKDVAKPSEEEQKELDEITAKRQKKGKQEEEKPGEEKTILHVKEMYDYQGRSYLHIPQDVGVNLRSTMPPEKCYLPKKQIHVWSGHTKGVSAVRLFPLSGHLLLSCSMDCKIKLWEVYGERRCLRTFIGHSKAVRDICFNTAGTQFLSAAYDRYLKLWDTETGQCISRFTNRKVPYCVKFNPDEDKQNLFVAGMSDKKIVQWDIRSGEIVQEYDRHLGAVNTIVFVDENRRFVSTSDDKSLRVWEWDIPVDFKYIAEPSMHSMPAVTLSPNGKWLACQSMDNQILIFGAQNRFRLNKKKIFKGHMVAGYACQVDFSPDMSYVISGDGNGKLNIWDWKTTKLYSRFKAHDKVCIGAVWHPHETSKVITCGWDGLIKLWD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI0000132145","uniref100":"UniRef100_O60508","uniref90":"UniRef90_O60508","uniref50":"UniRef50_O60508","genes":[{"name":{"value":"CDC40"},"synonyms":[{"value":"EHB3"},{"value":"PRP17"},{"value":"PRPF17"}]}],"alphafold_very_low_content":0.11226252158894647,"disorder_content":0.14162348877374784,"disprot_consensus":{"full":[{"start":1,"end":82,"type":"D"}],"Structural state":[{"start":1,"end":82,"type":"D"}]}},{"disprot_id":"DP03215","acc":"Q9H875","creator":"fquaglia","date":"2021-02-16T11:23:45.086Z","features":{"pfam":[{"id":"PF06658","name":"Protein of unknown function (DUF1168)","start":42,"end":174}],"gene3D":[]},"length":184,"name":"PRKR-interacting protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":50,"reference_id":"28502770","reference_source":"pmid","reference_html":"An Atomic Structure of the Human Spliceosome. <i> Zhang X, Yan C, Hang J, Finci LI, Lei J, Shi Y. </i> Cell, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5XJC"}],"region_id":"DP03215r001","statement":[{"text":"The N-terminal region of PRKRIP1 is disordered, as referenced in Table S2 and confirmed upon visual inspection of the structure.","type":"Curator statement"}],"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":143,"end":184,"reference_id":"28502770","reference_source":"pmid","reference_html":"An Atomic Structure of the Human Spliceosome. <i> Zhang X, Yan C, Hang J, Finci LI, Lei J, Shi Y. </i> Cell, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5XJC"}],"region_id":"DP03215r002","statement":[{"text":"The C-terminal region of PRKRIP1 is disordered, as referenced in Table S2 and confirmed upon visual inspection of the structure.","type":"Curator statement"}],"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MASPAASSVRPPRPKKEPQTLVIPKNAAEEQKLKLERLMKNPDKAVPIPEKMSEWAPRPPPEFVRDVMGSSAGAGSGEFHVYRHLRRREYQRQDYMDAMAEKQKLDAEFQKRLEKNKIAAEEQTAKRRKKRQKLKEKKLLAKKMKLEQKKQEGPGQPKEQGSSSSAEASGTEEEEEVPSFTMGR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000003587A","uniref100":"UniRef100_Q9H875","uniref90":"UniRef90_Q9H875","uniref50":"UniRef50_Q9CWV6","genes":[{"name":{"value":"PRKRIP1"}}],"alphafold_very_low_content":0.14673913043478262,"disorder_content":0.5,"disprot_consensus":{"full":[{"start":1,"end":50,"type":"D"},{"start":143,"end":184,"type":"D"}],"Structural state":[{"start":1,"end":50,"type":"D"},{"start":143,"end":184,"type":"D"}]}},{"disprot_id":"DP03216","acc":"Q96EQ8","creator":"ldobson","date":"2021-03-01T08:17:48.186Z","features":{"pfam":[{"id":"PF05605","name":"Drought induced 19 protein (Di19), zinc-binding","start":140,"end":196},{"id":"PF13923","name":"Zinc finger, C3HC4 type (RING finger)","start":37,"end":75},{"id":"PF18574","name":"C2HC Zing finger domain","start":94,"end":126}],"gene3D":[]},"length":232,"name":"E3 ubiquitin-protein ligase RNF125","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":32,"reference_id":"27411375","reference_source":"pmid","reference_html":"A C2HC zinc finger is essential for the RING-E2 interaction of the ubiquitin ligase RNF125. <i> Bijlmakers MJ, Teixeira JM, Boer R, Mayzel M, Puig-Sàrries P, Karlsson G, Coll M, Pons M, Crosas B. </i> Sci Rep, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5DKA"}],"region_id":"DP03216r001","statement":[{"text":"The predicted unstructured N-terminal 30 amino acids were not observed in the electron density","type":"Results"},{"text":"Regions (1-32) updated based on missing residues in PDB files ","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-03T20:35:47.195Z"}}],"regions_counter":1,"released":"2021_12","sequence":"MGSVLSTDSGKSAPASATARALERRRDPELPVTSFDCAVCLEVLHQPVRTRCGHVFCRSCIATSLKNNKWTCPYCRAYLPSEGVPATDVAKRMKSEYKNCAECDTLVCLSEMRAHIRTCQKYIDKYGPLQELEETAARCVCPFCQRELYEDSLLDHCITHHRSERRPVFCPLCRLIPDENPSSFSGSLIRHLQVSHTLFYDDFIDFNIIEEALIRRVLDRSLLEYVNHSNTT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"UniParc":"UPI0000073E70","uniref100":"UniRef100_Q96EQ8","uniref90":"UniRef90_Q96EQ8","uniref50":"UniRef50_Q96EQ8","genes":[{"name":{"value":"RNF125","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:21150","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:21150"}}]}}],"alphafold_very_low_content":0.1336206896551724,"disorder_content":0.13793103448275862,"disprot_consensus":{"full":[{"start":1,"end":32,"type":"D"}],"Structural state":[{"start":1,"end":32,"type":"D"}]}},{"disprot_id":"DP03217","acc":"Q9XWG3","creator":"spenadias","date":"2021-03-11T11:53:18.727Z","features":{"pfam":[{"id":"PF03372","name":"Endonuclease/Exonuclease/phosphatase family","start":123,"end":353},{"id":"PF22566","name":"UBA-like domain","start":43,"end":86}],"gene3D":[]},"length":362,"name":"5'-tyrosyl-DNA phosphodiesterase","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":1,"end":20,"reference_id":"23104058","reference_source":"pmid","reference_html":"Structural basis for recognition of 5'-phosphotyrosine adducts by Tdp2. <i> Shi K, Kurahashi K, Gao R, Tsutakawa SE, Tainer JA, Pommier Y, Aihara H. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4FVA"},{"db":"PDB","id":"4GEW"},{"db":"PDB","id":"4F1I"}],"region_id":"DP03217r001","statement":[{"text":"Figure 3 The full-length Tdp2 has a modular architecture. (a) Fulllength\ncTdp2 molecule in the crystal, with residue numbers indicated.\nThe N-terminal 20 residues as well as the linker between the α-helical\nbundle and the catalytic domain are disordered (dotted lines).","type":"Figure"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":98,"end":111,"reference_id":"23104058","reference_source":"pmid","reference_html":"Structural basis for recognition of 5'-phosphotyrosine adducts by Tdp2. <i> Shi K, Kurahashi K, Gao R, Tsutakawa SE, Tainer JA, Pommier Y, Aihara H. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4FVA"},{"db":"PDB","id":"4GEW"},{"db":"PDB","id":"4F1I"}],"region_id":"DP03217r002","statement":[{"text":"Despite a disordered linker between the a-helical bundle and the\ncatalytic domain (residues 98–111)","type":"Results"},{"text":"Figure 3 The full-length Tdp2 has a modular architecture. (a) Fulllength\ncTdp2 molecule in the crystal, with residue numbers indicated.\nThe N-terminal 20 residues as well as the linker between the α-helical\nbundle and the catalytic domain are disordered (dotted lines).","type":"Figure"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":98,"end":111,"reference_id":"23104058","reference_source":"pmid","reference_html":"Structural basis for recognition of 5'-phosphotyrosine adducts by Tdp2. <i> Shi K, Kurahashi K, Gao R, Tsutakawa SE, Tainer JA, Pommier Y, Aihara H. </i> Nat Struct Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"4FVA"},{"db":"PDB","id":"4GEW"},{"db":"PDB","id":"4F1I"}],"region_id":"DP03217r003","statement":[{"text":"Despite a disordered linker between the a-helical bundle and the\ncatalytic domain (residues 98–111)","type":"Results"},{"text":"Figure 3 The full-length Tdp2 has a modular architecture. (a) Fulllength\ncTdp2 molecule in the crystal, with residue numbers indicated.\nThe N-terminal 20 residues as well as the linker between the α-helical\nbundle and the catalytic domain are disordered (dotted lines).","type":"Figure"}],"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":3,"released":"2021_12","sequence":"MSNSDDEIQEIEAKRQKMSQEDSEVEIEILDEPEQGKLKNSSMSDEQKLHEFAIITATDEAFAQSILQDVDWDLKKALDVFYGSEAFAEARSAAVMGASSSMASSGAAVMTAEDLKGFEVSVMSWNIDGLDGRSLLTRMKAVAHIVKNVNPDILFLQEVVDRDLAPIDKLQSLYKIYYSNKGCQYYTAILVSKMFDVEKHDVIHFQNSGMYRTLQILEGSIGGLKVFLLNTHLESTREHRPQRCAQFGFCMDKVREIIAQNPGALVFFGGDLNLRDEEVSRVPDGVKDAWEAAGSDNKTKFTWDTFKNDNKQGFHGAKMRFDRLYWSGPLDKVKFTLEGRQRIRSCLCFPSDHWAINATFFA","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"dataset":[],"UniParc":"UPI000008191F","uniref100":"UniRef100_Q9XWG3","uniref90":"UniRef90_Q9XWG3","uniref50":"UniRef50_Q9XWG3","genes":[{"orfNames":[{"value":"Y63D3A.4"}]}],"alphafold_very_low_content":0.09392265193370165,"disorder_content":0.09392265193370165,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"D"},{"start":98,"end":111,"type":"D"}],"Structural state":[{"start":1,"end":20,"type":"D"},{"start":98,"end":111,"type":"D"}],"Disorder function":[{"start":98,"end":111,"type":"F"}]}},{"disprot_id":"DP03218","acc":"O76463","creator":"spenadias","date":"2021-03-12T11:30:38.253Z","features":{"pfam":[{"id":"PF00795","name":"Carbon-nitrogen hydrolase","start":17,"end":271},{"id":"PF01230","name":"HIT domain","start":309,"end":400}],"gene3D":[]},"length":440,"name":"Nitrilase and fragile histidine triad fusion protein NitFhit","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":404,"end":422,"reference_id":"10959838","reference_source":"pmid","reference_html":"Crystal structure of the worm NitFhit Rosetta Stone protein reveals a Nit tetramer binding two Fhit dimers. <i> Pace HC, Hodawadekar SC, Draganescu A, Huang J, Bieganowski P, Pekarsky Y, Croce CM, Brenner C. </i> Curr Biol, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1EMS"}],"region_id":"DP03218r001","statement":[{"text":"Theexperimental map was of sufficient quality to build from residues 13 tothe carboxyl terminus of each non-identical, 440 amino acid polypeptidewith 23 residues missing from the Fhit domain of one molecule and 30residues  missing  from  the  other.","type":"Methods"},{"text":"These 23 amino acids corresponds to the protein region comprised between residues 404 and 422, approximately, as indicated in PDB:1EMS and disorder predictors as MobiDB","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MLSTVFRRTMATGRHFIAVCQMTSDNDLEKNFQAAKNMIERAGEKKCEMVFLPECFDFIGLNKNEQIDLAMATDCEYMEKYRELARKHNIWLSLGGLHHKDPSDAAHPWNTHLIIDSDGVTRAEYNKLHLFDLEIPGKVRLMESEFSKAGTEMIPPVDTPIGRLGLSICYDVRFPELSLWNRKRGAQLLSFPSAFTLNTGLAHWETLLRARAIENQCYVVAAAQTGAHNPKRQSYGHSMVVDPWGAVVAQCSERVDMCFAEIDLSYVDTLREMQPVFSHRRSDLYTLHINEKSSETGGLKFARFNIPADHIFYSTPHSFVFVNLKPVTDGHVLVSPKRVVPRLTDLTDAETADLFIVAKKVQAMLEKHHNVTSTTICVQDGKDAGQTVPHVHIHILPRRAGDFGDNEIYQKLASHDKEPERKPRSNEQMAEEAVVYRNLM","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"dataset":[],"UniParc":"UPI00000612CD","uniref100":"UniRef100_O76463","uniref90":"UniRef90_O76463","uniref50":"UniRef50_O76463","genes":[{"name":{"value":"nft-1","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"Y56A3A.13","url":"https://www.wormbase.org/db/seq/sequence?name=Y56A3A.13;class=Transcript"}}]},"orfNames":[{"value":"Y56A3A.13"}]}],"alphafold_very_low_content":0.025,"disorder_content":0.04318181818181818,"disprot_consensus":{"full":[{"start":404,"end":422,"type":"D"}],"Structural state":[{"start":404,"end":422,"type":"D"}]}},{"disprot_id":"DP03219","acc":"Q9U3N4","creator":"spenadias","date":"2021-03-12T11:46:53.958Z","features":{"pfam":[{"id":"PF00876","name":"Innexin","start":25,"end":361}],"gene3D":[]},"length":389,"name":"Innexin-6","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":370,"end":389,"reference_id":"27905396","reference_source":"pmid","reference_html":"Atomic structure of the innexin-6 gap junction channel determined by cryo-EM. <i> Oshima A, Tani K, Fujiyoshi Y. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5H1Q"},{"db":"PDB","id":"5H1R"}],"region_id":"DP03219r001","statement":[{"text":"The Met1 to Gly6 residues at the\nN-terminal end, Ile52 and Gly53 following TM1, and Glu370 to\nthe C-terminal end were not assigned due to the disorder of\nthe structure.","type":"Results"},{"text":"Approximately 20 residues at the C-terminal end are missing and\nmay possibly account for the cytoplasmic bobble found in\nINX-6dN.","type":"Results"},{"text":"Dashed lines indicate unassigned residues due to disorder.","type":"Figure"},{"text":"Dashed lines in figure 2 are located at the end of TM1, and at the C- and N-terminus end region.","type":"Curator statement"}],"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":252,"end":261,"reference_id":"32095518","reference_source":"pmid","reference_html":"Cryo-EM structures of undocked innexin-6 hemichannels in phospholipids. <i> Burendei B, Shinozaki R, Watanabe M, Terada T, Tani K, Fujiyoshi Y, Oshima A. </i> Sci Adv, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03219r002","statement":[{"text":"The antiparallel E2 beta sheets mostly disappeared, and the hairpin loop was disordered from R252 to D261","type":"Results"}],"cross_refs":[{"db":"PDB","id":"6KFG"},{"db":"PDB","id":"6KFF"},{"db":"PDB","id":"6KFH"}],"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":87,"end":100,"reference_id":"32095518","reference_source":"pmid","reference_html":"Cryo-EM structures of undocked innexin-6 hemichannels in phospholipids. <i> Burendei B, Shinozaki R, Watanabe M, Terada T, Tani K, Fujiyoshi Y, Oshima A. </i> Sci Adv, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6KFG"},{"db":"PDB","id":"6KFF"},{"db":"PDB","id":"6KFH"}],"region_id":"DP03219r003","statement":[{"text":"The E1 outer lobe contained relaxed and disordered residues from D87 to V100, which\nprevent the E1 outer lobe from interfacing with the opposed hemichannel","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2021_12","sequence":"MASQVGAINSVNALISRVFVQPKGDLADRLNSRVTVVILAVSSALLLSSHFIGDPITCWTPAQFNAQWVNFVNQYCFVHGTYFVPLDQQLAFEEEERTKVSIQYYQWVPYVFALQAFLFYIPRFIWKAMIAYSGYDLAAAVKYVDRFWSENRDKDDKFKTRLAAFEGRPSVYIWDGIRLARKKRSRNMALFYTLSTVWQAVNAWIQFYILTQLLDSSIYTLWGPSILGDLLQGNDWQTTGHFPRIVHCDFNRRRPASVQLDTVLCVLTLNIYYEKLFIFLWFWLVFVAVVSTVNCFKWIYYLCNKTKAQKTIKNYLSTAPIKSTISDDQFFSALGEDGLFIMDQMALNLGDIPASYLTISMRNICQDFIESEDYIDEERTPFVKSIKHT","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"dataset":[],"UniParc":"UPI000012D736","uniref100":"UniRef100_Q9U3N4","uniref90":"UniRef90_Q9U3N4","uniref50":"UniRef50_Q9U3N4","genes":[{"name":{"value":"inx-6"},"synonyms":[{"value":"opu-6"}],"orfNames":[{"value":"C36H8.2"}]}],"alphafold_very_low_content":0.015424164524421594,"disorder_content":0.11311053984575835,"disprot_consensus":{"full":[{"start":87,"end":100,"type":"D"},{"start":252,"end":261,"type":"D"},{"start":370,"end":389,"type":"D"}],"Structural state":[{"start":87,"end":100,"type":"D"},{"start":252,"end":261,"type":"D"},{"start":370,"end":389,"type":"D"}]}},{"disprot_id":"DP03221","acc":"P55265","creator":"fquaglia","date":"2021-03-24T10:10:08.020Z","features":{"pfam":[{"id":"PF00035","name":"Double-stranded RNA binding motif","start":504,"end":567},{"id":"PF00035","name":"Double-stranded RNA binding motif","start":615,"end":679},{"id":"PF00035","name":"Double-stranded RNA binding motif","start":727,"end":792},{"id":"PF02137","name":"Adenosine-deaminase (editase) domain","start":886,"end":1215},{"id":"PF02295","name":"Adenosine deaminase z-alpha domain","start":135,"end":200},{"id":"PF02295","name":"Adenosine deaminase z-alpha domain","start":295,"end":358}],"gene3D":[]},"length":1226,"name":"Double-stranded RNA-specific adenosine deaminase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":202,"end":296,"reference_id":"33742389","reference_source":"pmid","reference_html":"Solution NMR backbone assignments of the N-terminal Zα-linker-Zβ segment from Homo sapiens ADAR1p150. <i> Nichols PJ, Henen MA, Vicens Q, Vögeli B. </i> Biomol NMR Assign, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03221r001","statement":[{"text":"Here we present the solution NMR backbone assignment of Zα-Zβ from H. Sapiens ADAR1. The predicted secondary structure of Zα-Zβ based on chemical shifts is in agreement with previously determined structures of Zα and Zβ in isolation, and indicates that the linker is intrinsically disordered. Comparison of the chemical shifts between the individual Zα and Zβ domains to the full Zα-Zβ construct suggests that Zβ may interact with the linker, the function of which is currently unknown.","type":"Abstract"},{"text":"First, the linker between the Zα and Zβ domains is intrinsically disordered, as determined by its low chemical shift dispersion and favorable relaxation properties (Fig. 2).","type":"Methods"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:39:53.448Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":202,"end":296,"reference_id":"33742389","reference_source":"pmid","reference_html":"Solution NMR backbone assignments of the N-terminal Zα-linker-Zβ segment from Homo sapiens ADAR1p150. <i> Nichols PJ, Henen MA, Vicens Q, Vögeli B. </i> Biomol NMR Assign, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":3,"region_id":"DP03221r002","statement":[{"text":"Here we present the solution NMR backbone assignment of Zα-Zβ from H. Sapiens ADAR1. The predicted secondary structure of Zα-Zβ based on chemical shifts is in agreement with previously determined structures of Zα and Zβ in isolation, and indicates that the linker is intrinsically disordered. Comparison of the chemical shifts between the individual Zα and Zβ domains to the full Zα-Zβ construct suggests that Zβ may interact with the linker, the function of which is currently unknown.","type":"Abstract"},{"text":"First, the linker between the Zα and Zβ domains is intrinsically disordered, as determined by its low chemical shift dispersion and favorable relaxation properties (Fig. 2).","type":"Methods"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:39:54.233Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":2,"released":"2023_06","sequence":"MNPRQGYSLSGYYTHPFQGYEHRQLRYQQPGPGSSPSSFLLKQIEFLKGQLPEAPVIGKQTPSLPPSLPGLRPRFPVLLASSTRGRQVDIRGVPRGVHLRSQGLQRGFQHPSPRGRSLPQRGVDCLSSHFQELSIYQDQEQRILKFLEELGEGKATTAHDLSGKLGTPKKEINRVLYSLAKKGKLQKEAGTPPLWKIAVSTQAWNQHSGVVRPDGHSQGAPNSDPSLEPEDRNSTSVSEDLLEPFIAVSAQAWNQHSGVVRPDSHSQGSPNSDPGLEPEDSNSTSALEDPLEFLDMAEIKEKICDYLFNVSDSSALNLAKNIGLTKARDINAVLIDMERQGDVYRQGTTPPIWHLTDKKRERMQIKRNTNSVPETAPAAIPETKRNAEFLTCNIPTSNASNNMVTTEKVENGQEPVIKLENRQEARPEPARLKPPVHYNGPSKAGYVDFENGQWATDDIPDDLNSIRAAPGEFRAIMEMPSFYSHGLPRCSPYKKLTECQLKNPISGLLEYAQFASQTCEFNMIEQSGPPHEPRFKFQVVINGREFPPAEAGSKKVAKQDAAMKAMTILLEEAKAKDSGKSEESSHYSTEKESEKTAESQTPTPSATSFFSGKSPVTTLLECMHKLGNSCEFRLLSKEGPAHEPKFQYCVAVGAQTFPSVSAPSKKVAKQMAAEEAMKALHGEATNSMASDNQPEGMISESLDNLESMMPNKVRKIGELVRYLNTNPVGGLLEYARSHGFAAEFKLVDQSGPPHEPKFVYQAKVGGRWFPAVCAHSKKQGKQEAADAALRVLIGENEKAERMGFTEVTPVTGASLRRTMLLLSRSPEAQPKTLPLTGSTFHDQIAMLSHRCFNTLTNSFQPSLLGRKILAAIIMKKDSEDMGVVVSLGTGNRCVKGDSLSLKGETVNDCHAEIISRRGFIRFLYSELMKYNSQTAKDSIFEPAKGGEKLQIKKTVSFHLYISTAPCGDGALFDKSCSDRAMESTESRHYPVFENPKQGKLRTKVENGEGTIPVESSDIVPTWDGIRLGERLRTMSCSDKILRWNVLGLQGALLTHFLQPIYLKSVTLGYLFSQGHLTRAICCRVTRDGSAFEDGLRHPFIVNHPKVGRVSIYDSKRQSGKTKETSVNWCLADGYDLEILDGTRGTVDGPRNELSRVSKKNIFLLFKKLCSFRYRRDLLRLSYGEAKKAARDYETAKNYFKKGLKDMGYGNWISKPQEEKNFYLCPV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","RNA-binding proteins"],"UniParc":"UPI0000001C6A","uniref100":"UniRef100_P55265","uniref90":"UniRef90_P55265","uniref50":"UniRef50_P55265","genes":[{"name":{"value":"ADAR"},"synonyms":[{"value":"ADAR1"},{"value":"DSRAD"},{"value":"G1P1"},{"value":"IFI4"}]}],"alphafold_very_low_content":0.34991843393148453,"disorder_content":0.07748776508972267,"disprot_consensus":{"full":[{"start":202,"end":296,"type":"D"}],"Structural state":[{"start":202,"end":296,"type":"D"}],"Disorder function":[{"start":202,"end":296,"type":"F"}]}},{"disprot_id":"DP03222","acc":"Q92783","creator":"fquaglia","date":"2021-03-24T14:25:14.298Z","features":{"pfam":[{"id":"PF00018","name":"SH3 domain","start":216,"end":261},{"id":"PF00790","name":"VHS domain","start":7,"end":139},{"id":"PF02809","name":"Ubiquitin interaction motif","start":172,"end":187}],"gene3D":[]},"length":540,"name":"Signal transducing adapter molecule 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":140,"end":170,"reference_id":"20927613","reference_source":"pmid","reference_html":"Backbone 1H, 13C, and 15N assignments for the tandem ubiquitin binding domains of signal transducing adapter molecule 1. <i> Lim J, Hong YH, Lee BJ, Ahn HC. </i> Biomol NMR Assign, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03222r001","statement":[{"text":"The {(1)H}-(15)N heteronuclear NOE experiments revealed that an unstructured and flexible loop region connects the VHS domain and UIM.","type":"Abstract"},{"text":"The amino acid sequences of STAM1N191 are shown in Fig. 1b. STAM1N191 consists of the VHS domain (M1-G139), the connecting region (V140-K170), and UIM (K171-S191). 1H-15N HSQC spectrum of STAM1N191 and the assigned residues are shown in Fig. 1b. Most of the resonances from the VHS domain were well dispersed, however, those from the connecting region and UIM showed narrow chemical shift dispersion and intense signals.","type":"Article"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:39:40.772Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":140,"end":170,"reference_id":"20927613","reference_source":"pmid","reference_html":"Backbone 1H, 13C, and 15N assignments for the tandem ubiquitin binding domains of signal transducing adapter molecule 1. <i> Lim J, Hong YH, Lee BJ, Ahn HC. </i> Biomol NMR Assign, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03222r002","statement":[{"text":"The {(1)H}-(15)N heteronuclear NOE experiments revealed that an unstructured and flexible loop region connects the VHS domain and UIM.","type":"Abstract"},{"text":"The amino acid sequences of STAM1N191 are shown in Fig. 1b. STAM1N191 consists of the VHS domain (M1-G139), the connecting region (V140-K170), and UIM (K171-S191). 1H-15N HSQC spectrum of STAM1N191 and the assigned residues are shown in Fig. 1b. Most of the resonances from the VHS domain were well dispersed, however, those from the connecting region and UIM showed narrow chemical shift dispersion and intense signals.","type":"Article"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:39:41.719Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":2,"released":"2023_12","sequence":"MPLFATNPFDQDVEKATSEMNTAEDWGLILDICDKVGQSRTGPKDCLRSIMRRVNHKDPHVAMQALTLLGACVSNCGKIFHLEVCSRDFASEVSNVLNKGHPKVCEKLKALMVEWTDEFKNDPQLSLISAMIKNLKEQGVTFPAIGSQAAEQAKASPALVAKDPGTVANKKEEEDLAKAIELSLKEQRQQSTTLSTLYPSTSSLLTNHQHEGRKVRAIYDFEAAEDNELTFKAGEIITVLDDSDPNWWKGETHQGIGLFPSNFVTADLTAEPEMIKTEKKTVQFSDDVQVETIEPEPEPAFIDEDKMDQLLQMLQSTDPSDDQPDLPELLHLEAMCHQMGPLIDEKLEDIDRKHSELSELNVKVMEALSLYTKLMNEDPMYSMYAKLQNQPYYMQSSGVSGSQVYAGPPPSGAYLVAGNAQMSHLQSYSLPPEQLSSLSQAVVPPSANPALPSQQTQAAYPNTMVSSVQGNTYPSQAPVYSPPPAATAAAATADVTLYQNAGPNMPQVPNYNLTSSTLPQPGGSQQPPQPQQPYSQKALL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000006E278","uniref100":"UniRef100_Q92783","uniref90":"UniRef90_Q92783","uniref50":"UniRef50_Q92783","genes":[{"name":{"value":"STAM"},"synonyms":[{"value":"STAM1"}]}],"alphafold_very_low_content":0.37777777777777777,"disorder_content":0.05740740740740741,"disprot_consensus":{"full":[{"start":140,"end":170,"type":"D"}],"Structural state":[{"start":140,"end":170,"type":"D"}],"Disorder function":[{"start":140,"end":170,"type":"F"}]}},{"disprot_id":"DP03223","acc":"P33316-2","creator":"fquaglia","date":"2021-03-25T09:45:26.869Z","features":{"pfam":[],"gene3D":[]},"length":164,"name":"Isoform 2 of Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":23,"reference_id":"17880943","reference_source":"pmid","reference_html":"Active site closure facilitates juxtaposition of reactant atoms for initiation of catalysis by human dUTPase. <i> Varga B, Barabás O, Kovári J, Tóth J, Hunyadi-Gulyás E, Klement E, Medzihradszky KF, Tölgyesi F, Fidy J, Vértessy BG. </i> FEBS Lett, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2HQU"}],"region_id":"DP03223r001","statement":[{"text":"Lower thermostability may be partially due to increased flexibility of N- and C-terminal segments. In fact, the N-terminus could not be localized in the 3D structure, and for one monomer, the C-terminus was also missing from the density maps.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MPCSEETPAISPSKRARPAEVGGMQLRFARLSEHATAPTRGSARAAGYDLYSAYDYTIPPMEKAVVKTDIQIALPSGCYGRVAPRSGLAAKHFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEVKKGDRIAQLICERIFYPEIEEVQALDDTERGSGGFGSTGKN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI0000001639","uniref100":"","uniref90":"","uniref50":"","genes":[{"name":{"value":"DUT"}}],"disorder_content":0.1402439024390244,"disprot_consensus":{"full":[{"start":1,"end":23,"type":"D"}],"Structural state":[{"start":1,"end":23,"type":"D"}]}},{"disprot_id":"DP03224","acc":"Q97W73","creator":"fquaglia","date":"2021-03-25T10:10:15.200Z","features":{"pfam":[{"id":"PF21473","name":"Single-stranded DNA binding protein Ssb-like, OB fold","start":8,"end":89}],"gene3D":[]},"length":148,"name":"Single-stranded DNA binding protein Ssb","ncbi_taxon_id":273057,"organism":"Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)","regions":[{"start":119,"end":148,"reference_id":"11160923","reference_source":"pmid","reference_html":"Identification and properties of the crenarchaeal single-stranded DNA binding protein from Sulfolobus solfataricus. <i> Wadsworth RI, White MF. </i> Nucleic Acids Res, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03224r001","statement":[{"text":"Sulfolobus SSB lacks the zinc finger motif found in the eucaryal and euryarchaeal proteins, possessing instead a flexible C-terminal tail, sensitive to trypsin digestion, that is not required for DNA binding.","type":"Abstract"},{"text":"This allowed the unambiguous identification of the site of cleavage by trypsin as Arg-119, the first arginine present in the Gly/Pro-rich C-terminal region, suggesting that the C-terminal 30 amino acids of Sulfolobus SSB exist in a flexible conformation.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MEEKVGNLKPNMESVNVTVRVLEASEARQIQTKNGVRTISEAIVGDETGRVKLTLWGKHAGSIKEGQVVKIENAWTTAFKGQVQLNAGSKTKIAEASEDGFPESSQIPENTPTAPQQMRGGGRGFRGGGRRYGRRGGRRQENEEGEEE","taxonomy":["Archaea","Crenarchaeota","Thermoprotei","Sulfolobales","Sulfolobaceae","Saccharolobus"],"dataset":[],"UniParc":"UPI0000064711","uniref100":"UniRef100_Q97W73","uniref90":"UniRef90_Q97W73","uniref50":"UniRef50_Q97W73","genes":[{"name":{"value":"ssb"},"olnNames":[{"value":"SSO2364"}]}],"alphafold_very_low_content":0.16216216216216217,"disorder_content":0.20270270270270271,"disprot_consensus":{"full":[{"start":119,"end":148,"type":"D"}],"Structural state":[{"start":119,"end":148,"type":"D"}]}},{"disprot_id":"DP03225","acc":"P19957","creator":"fquaglia","date":"2021-03-25T11:22:17.891Z","features":{"pfam":[{"id":"PF00095","name":"WAP-type (Whey Acidic Protein) 'four-disulfide core'","start":72,"end":116},{"id":"PF10511","name":"Trappin protein transglutaminase binding domain","start":27,"end":50}],"gene3D":[]},"length":117,"name":"Elafin","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":23,"end":60,"reference_id":"26878852","reference_source":"pmid","reference_html":"Complete 1H, 15N and 13C assignment of trappin-2 and 1H assignment of its two domains, elafin and cementoin. <i> Loth K, Alami SA, Habès C, Garrido S, Aucagne V, Delmas AF, Moreau T, Zani ML, Landon C. </i> Biomol NMR Assign, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03225r001","statement":[{"text":"Figure 1b shows the assigned 1H-15N HSQC spectra of the 15N, 13C labelled trappin-2. As expected, the dispersion of the resonances shows that the elafin domain (A39-Q95) is well folded whereas the cementoin domain (A1-K38) shows a narrow profile with chemical shift values close to random coil values which is typical for an intrinsically disordered domain.","type":"Article"},{"text":"Our results strongly suggest that the cementoin domain is disordered in the context of the full length protein (not just as the isolated form) under our experimental conditions.","type":"Article"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MRASSFLIVVVFLIAGTLVLEAAVTGVPVKGQDTVKGRVPFNGQDPVKGQVSVKGQDKVKAQEPVKGPVSTKPGSCPIILIRCAMLNPPNRCLKDTDCPGIKKCCEGSCGMACFVPQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000059C625","uniref100":"UniRef100_P19957","uniref90":"UniRef90_P19957","uniref50":"UniRef50_P19957","genes":[{"name":{"value":"PI3"},"synonyms":[{"value":"WAP3"},{"value":"WFDC14"}]}],"alphafold_very_low_content":0.24786324786324787,"disorder_content":0.3247863247863248,"disprot_consensus":{"full":[{"start":23,"end":60,"type":"D"}],"Structural state":[{"start":23,"end":60,"type":"D"}]}},{"disprot_id":"DP03226","acc":"P30771","creator":"vacs","date":"2021-03-26T10:28:20.352Z","features":{"pfam":[{"id":"PF09416","name":"RNA helicase (UPF2 interacting domain)","start":61,"end":208},{"id":"PF13086","name":"AAA domain","start":408,"end":508},{"id":"PF13086","name":"AAA domain","start":523,"end":607},{"id":"PF13087","name":"AAA domain","start":616,"end":812},{"id":"PF18141","name":"RNA helicase UPF1, 1B domain","start":260,"end":352}],"gene3D":[]},"length":971,"name":"ATP-dependent helicase NAM7","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":213,"end":224,"reference_id":"21419344","reference_source":"pmid","reference_html":"Molecular mechanisms for the RNA-dependent ATPase activity of Upf1 and its regulation by Upf2. <i> Chakrabarti S, Jayachandran U, Bonneau F, Fiorini F, Basquin C, Domcke S, Le Hir H, Conti E. </i> Mol Cell, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2XZL"}],"region_id":"DP03226r001","statement":[{"text":"In the Upf1-RNA-ADP:AlF4 complex, there is no ordered electron density for the 13-residue linker that would connect the last residue of the CH domain (Thr212y) to the first residue of the stalk (Ile225y). The two ordered ends of the CH and helicase regions are located on the same side of the molecule at a distance of 30 A˚ from each other, which can be spanned by the disordered and flexible linker.","type":"Results"},{"text":"The linker with no ordered electron density consists of 12 residues.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-04-20T16:12:36.176Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":213,"end":224,"reference_id":"21419344","reference_source":"pmid","reference_html":"Molecular mechanisms for the RNA-dependent ATPase activity of Upf1 and its regulation by Upf2. <i> Chakrabarti S, Jayachandran U, Bonneau F, Fiorini F, Basquin C, Domcke S, Le Hir H, Conti E. </i> Mol Cell, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"2XZL"}],"region_id":"DP03226r002","statement":[{"text":"In the Upf1-RNA-ADP:AlF4 complex, there is no ordered electron density for the 13-residue linker that would connect the last residue of the CH domain (Thr212y) to the first residue of the stalk (Ile225y). The two ordered ends of the CH and helicase regions are located on the same side of the molecule at a distance of 30 A˚ from each other, which can be spanned by the disordered and flexible linker.","type":"Results"},{"text":"The linker with no ordered electron density consists of 12 residues.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-04-20T16:12:37.244Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":2,"released":"2021_06","sequence":"MVGSGSHTPYDISNSPSDVNVQPATQLNSTLVEDDDVDNQLFEEAQVTETGFRSPSASDNSCAYCGIDSAKCVIKCNSCKKWFCNTKNGTSSSHIVNHLVLSHHNVVSLHPDSDLGDTVLECYNCGRKNVFLLGFVSAKSEAVVVLLCRIPCAQTKNANWDTDQWQPLIEDRQLLSWVAEQPTEEEKLKARLITPSQISKLEAKWRSNKDATINDIDAPEEQEAIPPLLLRYQDAYEYQRSYGPLIKLEADYDKQLKESQALEHISVSWSLALNNRHLASFTLSTFESNELKVAIGDEMILWYSGMQHPDWEGRGYIVRLPNSFQDTFTLELKPSKTPPPTHLTTGFTAEFIWKGTSYDRMQDALKKFAIDKKSISGYLYYKILGHQVVDISFDVPLPKEFSIPNFAQLNSSQSNAVSHVLQRPLSLIQGPPGTGKTVTSATIVYHLSKIHKDRILVCAPSNVAVDHLAAKLRDLGLKVVRLTAKSREDVESSVSNLALHNLVGRGAKGELKNLLKLKDEVGELSASDTKRFVKLVRKTEAEILNKADVVCCTCVGAGDKRLDTKFRTVLIDESTQASEPECLIPIVKGAKQVILVGDHQQLGPVILERKAADAGLKQSLFERLISLGHVPIRLEVQYRMNPYLSEFPSNMFYEGSLQNGVTIEQRTVPNSKFPWPIRGIPMMFWANYGREEISANGTSFLNRIEAMNCERIITKLFRDGVKPEQIGVITPYEGQRAYILQYMQMNGSLDKDLYIKVEVASVDAFQGREKDYIILSCVRANEQQAIGFLRDPRRLNVGLTRAKYGLVILGNPRSLARNTLWNHLLIHFREKGCLVEGTLDNLQLCTVQLVRPQPRKTERPMNAQFNVESEMGDFPKFQDFDAQSMVSFSGQIGDFGNAFVDNTELSSYINNEYWNFENFKSAFSQKQNRNEIDDRNLYQEEASHLNSNFARELQREEQKHELSKDFSNLGI","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"dataset":[],"UniParc":"UPI000004EEDA","uniref100":"UniRef100_P30771","uniref90":"UniRef90_P30771","uniref50":"UniRef50_P30771","genes":[{"name":{"value":"NAM7"},"synonyms":[{"value":"IFS2"},{"value":"MOF4","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8896465","url":"http://www.ncbi.nlm.nih.gov/pubmed/8896465","alternativeUrl":"https://europepmc.org/abstract/MED/8896465"}}]},{"value":"UPF1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8896465","url":"http://www.ncbi.nlm.nih.gov/pubmed/8896465","alternativeUrl":"https://europepmc.org/abstract/MED/8896465"}}]}],"orfNames":[{"value":"YM9582.05C"}],"olnNames":[{"value":"YMR080C"}]}],"alphafold_very_low_content":0.18640576725025745,"disorder_content":0.012358393408856848,"disprot_consensus":{"full":[{"start":213,"end":224,"type":"D"}],"Structural state":[{"start":213,"end":224,"type":"D"}],"Disorder function":[{"start":213,"end":224,"type":"F"}]}},{"disprot_id":"DP03227","acc":"P15205","creator":"fquaglia","date":"2021-03-26T14:53:24.992Z","features":{"pfam":[{"id":"PF00414","name":"Neuraxin and MAP1B repeat","start":1888,"end":1904},{"id":"PF00414","name":"Neuraxin and MAP1B repeat","start":1939,"end":1955},{"id":"PF00414","name":"Neuraxin and MAP1B repeat","start":1956,"end":1972},{"id":"PF00414","name":"Neuraxin and MAP1B repeat","start":2024,"end":2040},{"id":"PF00414","name":"Neuraxin and MAP1B repeat","start":2041,"end":2057},{"id":"PF23415","name":"Microtubule-associated protein 1B N-terminal","start":39,"end":235},{"id":"PF25281","name":"MAP1B MBL-like domain","start":240,"end":523}],"gene3D":[]},"length":2461,"name":"Microtubule-associated protein 1B","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions":[{"start":2212,"end":2338,"reference_id":"23339032","reference_source":"pmid","reference_html":"Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain. <i> Orbán-Németh Z, Henen MA, Geist L, Żerko S, Saxena S, Stanek J, Koźmiński W, Propst F, Konrat R. </i> Biomol NMR Assign, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03227r001","statement":[{"text":"Here we focus on the intrinsically disordered microtubule binding domain of the light chain of MAP1B.","type":"Abstract"},{"text":"The 1H–15N HSQC spectrum of the NH2 terminus of the light chain of MAP1B shows the for intrinsically disordered proteins typical narrow peak dispersion in the 1H dimension (Fig. 1).","type":"Article"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-15T14:26:42.605Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MATVVVEATEPEPSGSIGNPAATTSPSLSHRFLDSKFYLLVVVGETVTEEHLRRAIGNIELGIRSWDTNLIECNLDQELKLFVSRHSARFSPEVPGQKILHHRSDVLETVVLINPSDEAVSTEVRLMITDAARHKLLVLTGQCFENTGELILQSGSFSFQNFIEIFTDQEIGELLSTTHPANKASLTLFCPEEGDWKNSNLDRHNLQDFINIKLNSASILPEMEGLSEFTEYLSESVEVPSPFDILEPPTSGGFLKLSKPCCYIFPGGRGDSALFAVNGFNMLINGGSERKSCFWKLIRHLDRVDSILLTHIGDDNLPGINSMLQRKIAELEEERSQGSTSNSDWMKNLISPDLGVVFLNVPENLKNPEPNIKMKRSTEEACFTLQYLNKLSMKPEPLFRSVGNAIEPVILFQKMGVGKLEMYVLNPVKSSKEMQYFMQQWTGTNKDKAELILPNGQEVDIPISYLTSVSSLIVWHPANPAEKIIRVLFPGNSTQYNILEGLEKLKHLDFLKQPLATQKDLTGQVSTPPVKQVKLKQRADSRESLKPATKPLSSKSVRKESKEEAPEATKASQVEKTPKVESKEKVIVKKDKPGKVESKPSVTEKEVPSKEEQSPVKAEVAEKAATESKPKVTKDKVVKKEIKTKPEEKKEEKPKKEVAKKEDKTPLKKDEKPKKEEAKKEIKKEIKKEEKKELKKEVKKETPLKDAKKEVKKDEKKEVKKEEKEPKKEIKKISKDIKKSTPLSDTKKPAALKPKVAKKEEPTKKEPIAAGKLKDKGKVKVIKKEGKTTEAAATAVGTAAVAAAAGVAASGPAKELEAERSLMSSPEDLTKDFEELKAEEIDVAKDIKPQLELIEDEEKLKETEPGEAYVIQKETEVSKGSAESPDEGITTTEGEGECEQTPEELEPVEKQGVDDIEKFEDEGAGFEESSEAGDYEEKAETEEAEEPEEDGEDNVSGSASKHSPTEDEEIAKAEADVHIKEKRESVASGDDRAEEDMDEALEKGEAEQSEEEGEEEEDKAEDAREEDHEPDKTEAEDYVMAVVDKAAEAGVTEDQYGFLGTPAKQPGVQSPSREPASSIHDETLPGGSESEATASDEENREDQPEEFTATSGYTQSTIEISSEPTPMDEMSTPRDVMSDETNNEETESPSQEFVNITKYESSLYSQEYSKPVVASFNGLSDGSKTDATDGRDYNASASTISPPSSMEEDKFSKSALRDAYRPEETDVKTGAELDIKDVSDERLSPAKSPSLSPSPPSPIEKTPLGERSVNFSLTPNEIKASAEGEATAVVSPGVTQAVVEEHCASPEEKTLEVVSPSQSVTGSAGHTPYYQSPTDEKSSHLPTEVTEKPQAVPVSFEFTEAKDENERSSISPMDEPVPDSESPIEKVLSPLRSPPLIGSESAYEDFLSADDKALGRRSESPFEGKNGKQGFSDKESPVSDLTSDLYQDKQEEKSAGFIPIKEDFSPEKKASDAEIMSSQSALALDERKLGGDGSPTQVDVSQFGSFKEDTKMSISEGTVSDKSATPVDEGVAEDTYSHMEGVASVSTASVATSSFPEPTTDDVSPSLHAEVGSPHSTEVDDSLSVSVVQTPTTFQETEMSPSKEECPRPMSISPPDFSPKTAKSRTPVQDHRSEQSSMSIEFGQESPEHSLAMDFSRQSPDHPTVGAGMLHITENGPTEVDYSPSDIQDSSLSHKIPPTEEPSYTQDNDLSELISVSQVEASPSTSSAHTPSQIASPLQEDTLSDVVPPRDMSLYASLASEKVQSLEGEKLSPKSDISPLTPRESSPTYSPGFSDSTSGAKESTAAYQTSSSPPIDAAAAEPYGFRSSMLFDTMQHHLALSRDLTTSSVEKDNGGKTPGDFNYAYQKPESTTESPDEEDYDYESHEKTIQAHDVGGYYYEKTERTIKSPCDSGYSYETIEKTTKTPEDGGYSCEITEKTTRTPEEGGYSYEISEKTTRTPEVSGYTYEKTERSRRLLDDISNGYDDTEDGGHTLGDCSYSYETTEKITSFPESESYSYETTTKTTRSPDTSAYCYETMEKITKTPQASTYSYETSDRCYTPERKSPSEARQDVDLCLVSSCEFKHPKTELSPSFINPNPLEWFAGEEPTEESEKPLTQSGGAPPPSGGKQQGRQCDETPPTSVSESAPSQTDSDVPPETEECPSITADANIDSEDESETIPTDKTVTYKHMDPPPAPMQDRSPSPRHPDVSMVDPEALAIEQNLGKALKKDLKEKAKTKKPGTKTKSSSPVKKGDGKSKPSAASPKPGALKESSDKVSRVASPKKKESVEKAMKTTTTPEVKATRGEEKDKETKNAANASASKSVKTATAGPGTTKTAKSSTVPPGLPVYLDLCYIPNHSNSKNVDVEFFKRVRSSYYVVSGNDPAAEEPSRAVLDALLEGKAQWGSNMQVTLIPTHDSEVMREWYQETHEKQQDLNIMVLASSSTVVMQDESFPACKIEL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"dataset":[],"UniParc":"UPI0000170C18","uniref100":"UniRef100_P15205","uniref90":"UniRef90_P15205","uniref50":"UniRef50_P15205","genes":[{"name":{"value":"Map1b"}}],"alphafold_very_low_content":0.7553839902478667,"disorder_content":0.05160503860219423,"disprot_consensus":{"full":[{"start":2212,"end":2338,"type":"D"}],"Structural state":[{"start":2212,"end":2338,"type":"D"}]}},{"disprot_id":"DP03228","acc":"P26447","creator":"vacs","date":"2021-03-30T13:54:47.921Z","features":{"pfam":[{"id":"PF01023","name":"S-100/ICaBP type calcium binding domain","start":5,"end":48}],"gene3D":[]},"length":101,"name":"Protein S100-A4","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":91,"end":101,"reference_id":"18783790","reference_source":"pmid","reference_html":"Crystal structure of metastasis-associated protein S100A4 in the active calcium-bound form. <i> Pathuri P, Vogeley L, Luecke H. </i> J Mol Biol, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3CGA"}],"region_id":"DP03228r001","statement":[{"text":"The final model of Ca2+-bound S100A4 exhibits good stereochemistry and consists of 176 amino acids (dimer in the asymmetric unit), 51 water molecules and four calcium ions.","type":"Results"},{"text":"In S100A4, the C-terminal loop is long and very basic and makes it unique in comparison to other S100 proteins; however, in the Ca2+-bound S100A4 crystal structure the C-terminal loop (Phe89-Lys101) was disordered in the electron density maps.","type":"Results"},{"text":"Region 91-101 is disordered in the structure.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-04-21T07:49:35.320Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_06","sequence":"MACPLEKALDVMVSTFHKYSGKEGDKFKLNKSELKELLTRELPSFLGKRTDEAAFQKLMSNLDSNRDNEVDFQEYCVFLSCIAMMCNEFFEGFPDKQPRKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000003417D","uniref100":"UniRef100_P26447","uniref90":"UniRef90_P26447","uniref50":"UniRef50_P26447","genes":[{"name":{"value":"S100A4"},"synonyms":[{"value":"CAPL"},{"value":"MTS1"}]}],"alphafold_very_low_content":0.039603960396039604,"disorder_content":0.10891089108910891,"disprot_consensus":{"full":[{"start":91,"end":101,"type":"D"}],"Structural state":[{"start":91,"end":101,"type":"D"}]}},{"disprot_id":"DP03229","acc":"P05451","creator":"vacs","date":"2021-04-01T14:58:01.665Z","features":{"pfam":[{"id":"PF00059","name":"Lectin C-type domain","start":54,"end":164}],"gene3D":[]},"length":166,"name":"Lithostathine-1-alpha","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":23,"end":35,"reference_id":"8654365","reference_source":"pmid","reference_html":"Crystal structure of human lithostathine, the pancreatic inhibitor of stone formation. <i> Bertrand JA, Pignol D, Bernard JP, Verdier JM, Dagorn JC, Fontecilla-Camps JC. </i> EMBO J, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1LIT"}],"region_id":"DP03229r001","statement":[{"text":"The first 13 residues, including the O-glycosylation site, Thr5, are disordered in the crystal. Although the first N-terminal residue of our model (Cysl4) is well defined in electron density (Figure 1), no electron density is present for the adjacent N terminal residues.","type":"Results"},{"text":"Although at this temperature thermal disorder should be minimal, no density corresponding to the missing amino acids was observed. This indicates that residues 1-13 are statically disordered in the crystal.","type":"Results"},{"text":"HLIT and the C-type lectins differ at two levels: the extreme conformational flexibility of the N-terminal segment of HLIT (residues 1-13) and the lack of both calcium- and carbohydrate-binding sites.","type":"Results"},{"text":"The IDR characterized in the publication and spanning residues 1-13 corresponds to region 23-35 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-22).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-21T14:39:44.133Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":23,"end":35,"reference_id":"10625646","reference_source":"pmid","reference_html":"Mechanism of calcite crystal growth inhibition by the N-terminal undecapeptide of lithostathine. <i> Gerbaud V, Pignol D, Loret E, Bertrand JA, Berland Y, Fontecilla-Camps JC, Canselier JP, Gabas N, Verdier JM. </i> J Biol Chem, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1QDD"}],"region_id":"DP03229r002","statement":[{"text":"The N-terminal domain is a 13-residue peptide chain that stretches out of the heart shape of the C-type lectin domain. Three residues (positions 9–11) are involved in a helix turn motif that represented the only secondary element of this domain. As a result, the N-terminal domain was much more agitated in the crystal (averaged B-factor of 36 Å2) than the rest of the protein (averaged B-factor of 22 Å2).","type":"Results"},{"text":"The IDR characterized in the publication and spanning residues 1-13 corresponds to region 23-35 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-22).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-21T14:22:35.815Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":25,"end":29,"reference_id":"10625646","reference_source":"pmid","reference_html":"Mechanism of calcite crystal growth inhibition by the N-terminal undecapeptide of lithostathine. <i> Gerbaud V, Pignol D, Loret E, Bertrand JA, Berland Y, Fontecilla-Camps JC, Canselier JP, Gabas N, Verdier JM. </i> J Biol Chem, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000041","term_name":"glycosylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1QDD"}],"region_id":"DP03229r003","statement":[{"text":"During structure refinement, we observed a large electron density around Thr5, clearly indicating the presence of O-linked sugars to the Thr5 side chain.","type":"Results"},{"text":"The O-glycosylation site (Thr5) characterized in the publication corresponds to Thr27 in the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-22).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-21T14:38:51.883Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":24,"end":33,"reference_id":"10625646","reference_source":"pmid","reference_html":"Mechanism of calcite crystal growth inhibition by the N-terminal undecapeptide of lithostathine. <i> Gerbaud V, Pignol D, Loret E, Bertrand JA, Berland Y, Fontecilla-Camps JC, Canselier JP, Gabas N, Verdier JM. </i> J Biol Chem, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP03229r004","statement":[{"text":"The CD spectrum (Fig. 2) was typical of a random coil structure (28) and strengthened our x-ray data. The negative band near 200 nm had an intensity in the range of those observed with model peptides with no steric constraints or internal hydrogen bonds. Random coil CD spectra were characterized by an intense negative band at 200 nm due to π-π* transition and low intensity bands near 210 nm due to n- π* transitions (28). No typical secondary structures could be deduced from this spectrum. Similar results were obtained in trifluoroethanol or SDS (data not shown). Both x-ray and CD experiments therefore suggest that pE1R11 is a highly flexible molecule that can display many configurations depending on the environment.","type":"Results"},{"text":"The authors also used a synthetic peptide which is almost identical to the first 11 residues (the 1. residue is different). The peptide sequence corresponds to region 23-33 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-22).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-21T14:22:21.921Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":24,"end":33,"reference_id":"1397886","reference_source":"pmid","reference_html":"Inhibition of nucleation and crystal growth of calcium carbonate by human lithostathine. <i> Bernard JP, Adrich Z, Montalto G, De Caro A, De Reggi M, Sarles H, Dagorn JC. </i> Gastroenterology, 1992","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007707","ec_ontology":"ECO","ec_name":"protein inhibition evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03229r005","statement":[{"text":"The glycosylated aminoterminal undecapeptide generated by limited trypsin hydrolysis inhibited CaCO, crystal growth with a Kd = 3.0x10e6 mol/L, similar to that of lithostathine. On the contrary, the carboxy-terminal polypeptide was inactive. A synthetic undecapeptide identical to the N-terminal end but not glycosylated was equally active. The activity disappeared upon digestion of the undecapeptide with V8 protease. The N-terminal undecapeptide of lithostathine is therefore essential to the inhibitory activity of the protein on CaCO, crystal growth.","type":"Abstract"},{"text":"As shown on Figure 2A, the rate of disappearance of calcium from the solution containing seed crystals was decreased in the presence of lithostathine. The N-terminal undecapeptide of lithostathine and its synthetic analogue showed similar activity (Figures 2B and 3).","type":"Results"},{"text":"We studied in vitro the inhibitory properties of human lithostathine on CaCO, precipitation. The inhibitory activity was localized to the amino-terminal undecapeptide of the molecule.","type":"Discussion"},{"text":"On the contrary, the undecapeptide had retained the inhibitory properties of lithostathine, with a similar Kd for CaCO, crystals (3.0 x 10-6 mol/L). Abolition of inhibition after treating the peptide with protease V8, which generates three fragments, suggested that the glycan chain was not responsible by itself for the inhibition. Actually, it might not be involved at all, because a synthetic peptide with the sequence of the undecapeptide but without glycan was equally active, with a Kd of 4.1 X 10-6 mol/L (Figure 3B).","type":"Discussion"},{"text":"The authors used two undecapeptides (one of them was glycosylated), which are almost identical to the first 11 residues (the 1. residue is different) of the mature protein. The peptide sequence corresponds to region 23-33 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-22).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-21T15:20:12.280Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":5,"released":"2021_06","sequence":"MAQTSSYFMLISCLMFLSQSQGQEAQTELPQARISCPEGTNAYRSYCYYFNEDRETWVDADLYCQNMNSGNLVSVLTQAEGAFVASLIKESGTDDFNVWIGLHDPKKNRRWHWSSGSLVSYKSWGIGAPSSVNPGYCVSLTSSTGFQKWKDVPCEDKFSFVCKFKN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000017415C","uniref100":"UniRef100_P05451","uniref90":"UniRef90_P05451","uniref50":"UniRef50_P05451","genes":[{"name":{"value":"REG1A"},"synonyms":[{"value":"PSPS"},{"value":"PSPS1"},{"value":"REG"}]}],"alphafold_very_low_content":0,"disorder_content":0.0783132530120482,"disprot_consensus":{"full":[{"start":23,"end":35,"type":"D"}],"Structural state":[{"start":23,"end":35,"type":"D"}],"Disorder function":[{"start":25,"end":29,"type":"F"}],"Molecular function":[{"start":24,"end":33,"type":"F"}]}},{"disprot_id":"DP03230","acc":"P11940","creator":"vacs","date":"2021-04-07T16:08:07.123Z","features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":13,"end":82},{"id":"PF00076","name":"RNA recognition motif","start":101,"end":167},{"id":"PF00076","name":"RNA recognition motif","start":193,"end":261},{"id":"PF00076","name":"RNA recognition motif","start":296,"end":363},{"id":"PF00658","name":"MLLE domain","start":549,"end":614}],"gene3D":[]},"length":636,"name":"Polyadenylate-binding protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":179,"end":199,"reference_id":"23041282","reference_source":"pmid","reference_html":"Interdomain allostery promotes assembly of the poly(A) mRNA complex with PABP and eIF4G. <i> Safaee N, Kozlov G, Noronha AM, Xie J, Wilds CJ, Gehring K. </i> Mol Cell, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4F25"},{"db":"PDB","id":"4F26"}],"region_id":"DP03230r001","statement":[{"text":"The structures were solved by molecular replacement using the RRM1-2·poly(A)11 crystal structure (PDB code 1cvj). The C-termini of both structures are disordered. The final model of the orthorhombic crystal form includes residues G99-S175. The final model of the trigonal crystal form includes residues G99-E178.","type":"Supplementary material"},{"text":"Overlay of the ternary complex with the free RRM2 domain shows the absence of the C-terminal helix α3 in the unliganded forms (Figure S3B). Residues 179 to 199 are disordered in both crystal forms in the absence of RNA but form an α-helix in the ternary complex.","type":"Supplementary material"},{"text":"Our NMR and crystallography studies (Figure S3) have suggested that the linkers connecting the RRM domains are flexible in the absence of RNA. As the result of this flexibility, the RRM domains are free to adopt different orientations.","type":"Discussion"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T16:34:04.057Z"}},{"start":180,"end":190,"reference_id":"10499800","reference_source":"pmid","reference_html":"Recognition of polyadenylate RNA by the poly(A)-binding protein. <i> Deo RC, Bonanno JB, Sonenberg N, Burley SK. </i> Cell, 1999","date":"2023-05-09T06:49:06.350Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":3,"cross_refs":[{"db":"PDB","id":"1CVJ"}],"region_id":"DP03230r002","statement":[{"text":"The final PABP RRM1/2–RNA model consists of 53 water molecules and 8 protein–nucleic acid complexes: complex A, PABP residues 11–179 plus nucleotides Ade-1 to Ade-8; complex B, PABP 11–132, 137–159, 170–175 plus Ade-3 to Ade-8; complex C, PABP 11–179 plus Ade-3 to Ade-8; complex D, PABP 11–132, 137–175 plus Ade-3 to Ade-8; complex E, PABP 11–179 plus Ade-2 to Ade-8; complex F, PABP 11–101, 112–132, 137–149, 168–173 plus Ade-3 to Ade-8; complex G, PABP 11–175 plus Ade-3 to Ade-8; complex H, PABP 11–103, 113–132, 137–152, 173–175 plus Ade-3 to Ade-8.","type":"Methods"},{"text":"As suggested for the domain linker between RRM1 and RRM2, we believe that the RRM2/3 and RRM3/4 domain linkers are disordered in the absence of RNA.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-09T12:59:54.112Z"}},{"start":179,"end":190,"reference_id":"23041282","reference_source":"pmid","reference_html":"Interdomain allostery promotes assembly of the poly(A) mRNA complex with PABP and eIF4G. <i> Safaee N, Kozlov G, Noronha AM, Xie J, Wilds CJ, Gehring K. </i> Mol Cell, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03230r003","statement":[{"text":"Our NMR and crystallography studies (Figure S3) have suggested that the linkers connecting the RRM domains are flexible in the absence of RNA. As the result of this flexibility, the RRM domains are free to adopt different orientations.","type":"Discussion"},{"text":"According to Figure 1, the RRM2/3 linker includes residues 176-190. Linker residues 179-190 are disordered in the structures (PDB: 4F25 and 4F26).","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"4F25"},{"db":"PDB","id":"4F26"}],"ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T16:40:46.309Z"}},{"start":179,"end":183,"reference_id":"23041282","reference_source":"pmid","reference_html":"Interdomain allostery promotes assembly of the poly(A) mRNA complex with PABP and eIF4G. <i> Safaee N, Kozlov G, Noronha AM, Xie J, Wilds CJ, Gehring K. </i> Mol Cell, 2012","date":"2023-05-09T07:03:29.881Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"GO:0003729","term_name":"mRNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":4,"region_id":"DP03230r004","statement":[{"text":"Helices following RRM1 (residues 92–96) and RRM2 (residues 176–183) contribute to RNA binding. R94 makes hydrogen bonds with the hydroxyl oxygen (O20) of the ribose moieties rA5 and rA6 while R179 forms hydrogen bonds with the phosphate oxygens of rA2.","type":"Figure"},{"text":"In the α helices, key arginine residues, Arg94 in the first helix and Arg179 in the second, contribute to poly(A) binding by forming hydrogen bonds with the hydroxyl oxygen (O2) of the ribose moieties of rA5 and rA6 and the backbone phosphate oxygen of rA2 (Figures 3D and 3E). ","type":"Results"},{"text":"Linker residues 179-190 are disordered in the structures (PDB: 4F25 and 4F26) and residues 179-183 contribute to RNA binding (PDB: 4F02).","type":"Curator statement"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns.\" [GOC:kmv, GOC:pr, SO:0000234]","disprot_namespace":"Disorder function","term_is_binding":true,"cross_refs":[{"db":"PDB","id":"4F02"}],"interaction_partner":[{"db":"RNAcentral","id":"URS000080E35F_32630","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-09T13:00:13.561Z"}},{"start":179,"end":190,"reference_id":"23041282","reference_source":"pmid","reference_html":"Interdomain allostery promotes assembly of the poly(A) mRNA complex with PABP and eIF4G. <i> Safaee N, Kozlov G, Noronha AM, Xie J, Wilds CJ, Gehring K. </i> Mol Cell, 2012","date":"2022-03-08T14:02:45.126Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":4,"region_id":"DP03230r005","statement":[{"text":"The importance of this second helix, which was not observed in the binary complex, was quantified by measuring the RNA binding affinity of a fragment (RRM1-2ΔR) that lacks the 13 C-terminal residues. ITC measurements revealed a 2.7-fold loss of affinity of RRM1-2ΔR (1.6 mM) relative to the larger crystallized fragment (Kd 0.6 mM; Figure S1B).","type":"Results"},{"text":"Linker residues 179-190 are disordered in the structures (PDB: 4F25 and 4F26).","type":"Curator statement"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"RNAcentral","id":"URS000080E35F_32630","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T16:38:35.257Z"}},{"start":179,"end":190,"reference_id":"23041282","reference_source":"pmid","reference_html":"Interdomain allostery promotes assembly of the poly(A) mRNA complex with PABP and eIF4G. <i> Safaee N, Kozlov G, Noronha AM, Xie J, Wilds CJ, Gehring K. </i> Mol Cell, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03230r006","statement":[{"text":"Analysis of the scattering profiles using the program GNOM (Svergun, 1992) shows that the radius of gyration (Rg) of RRM1-2-3 is significantly larger for the poly(A)- bound form than without RNA (Table S2). The ab initio models of RRM1 2-3 generated by the software DAMMIF (Volkov and Svergun, 2003) show that the poly(A)-bound form of RRM1-2-3 in solution is more extended with a longer maximum dimension (Dmax) than the unbound RRM1-2-3 (Figures 5A and 5B and Table S2). Our NMR and crystallography studies (Figure S3) have suggested that the linkers connecting the RRM domains are flexible in the absence of RNA. As the result of this flexibility, the RRM domains are free to adopt different orientations. Our SAXS data show that this leads to a more compact conformation. In contrast, upon binding to poly(A), the linkers between the RRMs fold into a helices (Figure S3), leading to a more extended conformation (Figures 5A and 5B).","type":"Results"},{"text":"According to Figure 1, the RRM2/3 linker includes residues 176-190. Linker residues 179-190 are disordered in the structures (PDB: 4F25 and 4F26).","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T16:36:25.764Z"}},{"start":1,"end":10,"reference_id":"10499800","reference_source":"pmid","reference_html":"Recognition of polyadenylate RNA by the poly(A)-binding protein. <i> Deo RC, Bonanno JB, Sonenberg N, Burley SK. </i> Cell, 1999","date":"2023-05-09T06:50:04.780Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":3,"cross_refs":[{"db":"PDB","id":"1CVJ"}],"region_id":"DP03230r008","statement":[{"text":"The final PABP RRM1/2–RNA model consists of 53 water molecules and 8 protein–nucleic acid complexes: complex A, PABP residues 11–179 plus nucleotides Ade-1 to Ade-8; complex B, PABP 11–132, 137–159, 170–175 plus Ade-3 to Ade-8; complex C, PABP 11–179 plus Ade-3 to Ade-8; complex D, PABP 11–132, 137–175 plus Ade-3 to Ade-8; complex E, PABP 11–179 plus Ade-2 to Ade-8; complex F, PABP 11–101, 112–132, 137–149, 168–173 plus Ade-3 to Ade-8; complex G, PABP 11–175 plus Ade-3 to Ade-8; complex H, PABP 11–103, 113–132, 137–152, 173–175 plus Ade-3 to Ade-8.","type":"Methods"},{"text":"Residues 1-10 are completely missing in all chains and are presumably disordered.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-09T12:59:54.711Z"}}],"regions_counter":8,"released":"2021_12","sequence":"MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFIKNLDKSIDNKALYDTFSAFGNILSCKVVCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAELGARAKEFTNVYIKNFGEDMDDERLKDLFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQIYVGRAQKKVERQTELKRKFEQMKQDRITRYQGVNLYVKNLDDGIDDERLRKEFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQRKEERQAHLTNQYMQRMASVRAVPNPVINPYQPAPPSGYFMAAIPQTQNRAAYYPPSQIAQLRPSPRWTAQGARPHPFQNMPGAIRPAAPRPPFSTMRPASSQVPRVMSTQRVANTSTQTMGPRPAAAAAAATPAVRTVPQYKYAAGVRNPQQHLNAQPQVTMQQPAVHVQGQEPLTASMLASAPPQEQKQMLGERLFPLIQAMHPTLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHQAKEAAQKAVNSATGVPTV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Cancer-related proteins","Condensates-related proteins","RNA-binding proteins"],"UniParc":"UPI0000161C54","uniref100":"UniRef100_P11940","uniref90":"UniRef90_P11940","uniref50":"UniRef50_P11940","genes":[{"name":{"value":"PABPC1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:8554","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8554"}}]},"synonyms":[{"value":"PAB1"},{"value":"PABP","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"20102337","url":"http://www.ncbi.nlm.nih.gov/pubmed/20102337","alternativeUrl":"https://europepmc.org/abstract/MED/20102337"}}]},{"value":"PABP1"},{"value":"PABPC2"}]}],"alphafold_very_low_content":0.25,"disorder_content":0.04874213836477988,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"},{"start":179,"end":190,"type":"T"},{"start":191,"end":199,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":179,"end":199,"type":"D"}],"Disorder function":[{"start":179,"end":190,"type":"F"}],"Molecular function":[{"start":179,"end":190,"type":"F"}],"Structural transition":[{"start":179,"end":190,"type":"T"}]}},{"disprot_id":"DP03231","acc":"P15498","creator":"fquaglia","date":"2021-04-08T08:55:04.055Z","features":{"pfam":[{"id":"PF00017","name":"SH2 domain","start":671,"end":745},{"id":"PF00018","name":"SH3 domain","start":617,"end":652},{"id":"PF00018","name":"SH3 domain","start":788,"end":834},{"id":"PF00130","name":"Phorbol esters/diacylglycerol binding domain (C1 domain)","start":516,"end":566},{"id":"PF00169","name":"PH domain","start":404,"end":503},{"id":"PF00621","name":"RhoGEF domain","start":199,"end":371},{"id":"PF11971","name":"CAMSAP CH domain","start":19,"end":102}],"gene3D":[]},"length":845,"name":"Proto-oncogene vav","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":130,"end":141,"reference_id":"20141838","reference_source":"pmid","reference_html":"Structural and energetic mechanisms of cooperative autoinhibition and activation of Vav1. <i> Yu B, Martins IR, Li P, Amarasinghe GK, Umetani J, Fernandez-Zapico ME, Billadeau DD, Machius M, Tomchick DR, Rosen MK. </i> Cell, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3KY9"}],"region_id":"DP03231r001","statement":[{"text":"Dashed lines indicate regions not observed in the electron density map.","type":"Figure"},{"text":"The current model contains two Vav1 CADPZ monomers (labeled A and B,respectively) in the asymmetric unit with backbone root-mean-square deviation (rmsd) of 0.13 A ̊for residues 2–129, 142–150, 156–180, 189–417,419–456, 463–478, 482–564.","type":"Supplementary material"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":565,"end":584,"reference_id":"20141838","reference_source":"pmid","reference_html":"Structural and energetic mechanisms of cooperative autoinhibition and activation of Vav1. <i> Yu B, Martins IR, Li P, Amarasinghe GK, Umetani J, Fernandez-Zapico ME, Billadeau DD, Machius M, Tomchick DR, Rosen MK. </i> Cell, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3KY9"}],"region_id":"DP03231r002","statement":[{"text":"Dashed lines indicate regions not observed in the electron density map.","type":"Figure"},{"text":"The current model contains two Vav1 CADPZ monomers (labeled A and B,respectively) in the asymmetric unit with backbone root-mean-square deviation (rmsd) of 0.13 A ̊for residues 2–129, 142–150, 156–180, 189–417,419–456, 463–478, 482–564.","type":"Supplementary material"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MELWRQCTHWLIQCRVLPPSHRVTWDGAQVCELAQALRDGVLLCQLLNNLLPHAINLREVNLRPQMSQFLCLKNIRTFLSTCCEKFGLKRSELFEAFDLFDVQDFGKVIYTLSALSWTPIAQNRGIMPFPTEEESVGDEDIYSGLSDQIDDTVEEDEDLYDCVENEEAEGDEIYEDLMRSEPVSMPPKMTEYDKRCCCLREIQQTEEKYTDTLGSIQQHFLKPLQRFLKPQDIEIIFINIEDLLRVHTHFLKEMKEALGTPGAANLYQVFIKYKERFLVYGRYCSQVESASKHLDRVAAAREDVQMKLEECSQRANNGRFTLRDLLMVPMQRVLKYHLLLQELVKHTQEAMEKENLRLALDAMRDLAQCVNEVKRDNETLRQITNFQLSIENLDQSLAHYGRPKIDGELKITSVERRSKMDRYAFLLDKALLICKRRGDSYDLKDFVNLHSFQVRDDSSGDRDNKKWSHMFLLIEDQGAQGYELFFKTRELKKKWMEQFEMAISNIYPENATANGHDFQMFSFEETTSCKACQMLLRGTFYQGYRCHRCRASAHKECLGRVPPCGRHGQDFPGTMKKDKLHRRAQDKKRNELGLPKMEVFQEYYGLPPPPGAIGPFLRLNPGDIVELTKAEAEQNWWEGRNTSTNEIGWFPCNRVKPYVHGPPQDLSVHLWYAGPMERAGAESILANRSDGTFLVRQRVKDAAEFAISIKYNVEVKHIKIMTAEGLYRITEKKAFRGLTELVEFYQQNSLKDCFKSLDTTLQFPFKEPEKRTISRPAVGSTKYFGTAKARYDFCARDRSELSLKEGDIIKILNKKGQQGWWRGEIYGRVGWFPANYVEEDYSEYC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins"],"UniParc":"UPI000016B2E9","uniref100":"UniRef100_P15498","uniref90":"UniRef90_P15498","uniref50":"UniRef50_P15498","genes":[{"name":{"value":"VAV1"},"synonyms":[{"value":"VAV"}]}],"alphafold_very_low_content":0.0485207100591716,"disorder_content":0.0378698224852071,"disprot_consensus":{"full":[{"start":130,"end":141,"type":"D"},{"start":565,"end":584,"type":"D"}],"Structural state":[{"start":130,"end":141,"type":"D"},{"start":565,"end":584,"type":"D"}]}},{"disprot_id":"DP03232","acc":"Q7KZF4","creator":"fquaglia","date":"2021-04-08T08:57:14.807Z","features":{"pfam":[{"id":"PF00565","name":"Staphylococcal nuclease homologue","start":51,"end":166},{"id":"PF00565","name":"Staphylococcal nuclease homologue","start":220,"end":327},{"id":"PF00565","name":"Staphylococcal nuclease homologue","start":368,"end":495},{"id":"PF00565","name":"Staphylococcal nuclease homologue","start":553,"end":659},{"id":"PF00565","name":"Staphylococcal nuclease homologue","start":847,"end":894},{"id":"PF00567","name":"Tudor domain","start":680,"end":797}],"gene3D":[]},"length":910,"name":"Staphylococcal nuclease domain-containing protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":660,"end":669,"reference_id":"18453631","reference_source":"pmid","reference_html":"Structural and functional insights into human Tudor-SN, a key component linking RNA interference and editing. <i> Li CL, Yang WZ, Chen YP, Yuan HS. </i> Nucleic Acids Res, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":2,"cross_refs":[{"db":"PDB","id":"3BDL"}],"region_id":"DP03232r001","statement":[{"text":"A long loop between SN4 and SN5 domains (residues 635–644) was disordered without visible electron density.","type":"Results"},{"text":"A loop between SN4 and SN5 (residues 635–644) is disordered and is displayed as a dotted line.","type":"Figure"},{"text":"The aforementioned IDR corresponds to region 660-669 of the UniProt sequence.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:39:27.800Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":660,"end":669,"reference_id":"18453631","reference_source":"pmid","reference_html":"Structural and functional insights into human Tudor-SN, a key component linking RNA interference and editing. <i> Li CL, Yang WZ, Chen YP, Yuan HS. </i> Nucleic Acids Res, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":3,"cross_refs":[{"db":"PDB","id":"3BDL"}],"region_id":"DP03232r002","statement":[{"text":"Tudor-SN contains four tandem repeats of staphylococcal nuclease-like domains (SN1-SN4) followed by a tudor and C-terminal SN domain (SN5).","type":"Abstract"},{"text":"A loop between SN4 and SN5 (residues 635–644) is disordered and is displayed as a dotted line.","type":"Figure"},{"text":"A long loop between SN4 and SN5 domains (residues 635–644) was disordered without visible electron density.","type":"Results"},{"text":"The aforementioned IDR corresponds to region 660-669 of the UniProt sequence.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:39:28.692Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":2,"released":"2022_06","sequence":"MASSAQSGGSSGGPAVPTVQRGIIKMVLSGCAIIVRGQPRGGPPPERQINLSNIRAGNLARRAAATQPDAKDTPDEPWAFPAREFLRKKLIGKEVCFTIENKTPQGREYGMIYLGKDTNGENIAESLVAEGLATRREGMRANNPEQNRLSECEEQAKAAKKGMWSEGNGSHTIRDLKYTIENPRHFVDSHHQKPVNAIIEHVRDGSVVRALLLPDYYLVTVMLSGIKCPTFRREADGSETPEPFAAEAKFFTESRLLQRDVQIILESCHNQNILGTILHPNGNITELLLKEGFARCVDWSIAVYTRGAEKLRAAERFAKERRLRIWRDYVAPTANLDQKDKQFVAKVMQVLNADAIVVKLNSGDYKTIHLSSIRPPRLEGENTQDKNKKLRPLYDIPYMFEAREFLRKKLIGKKVNVTVDYIRPASPATETVPAFSERTCATVTIGGINIAEALVSKGLATVIRYRQDDDQRSSHYDELLAAEARAIKNGKGLHSKKEVPIHRVADISGDTQKAKQFLPFLQRAGRSEAVVEYVFSGSRLKLYLPKETCLITFLLAGIECPRGARNLPGLVQEGEPFSEEATLFTKELVLQREVEVEVESMDKAGNFIGWLHIDGANLSVLLVEHALSKVHFTAERSSYYKSLLSAEEAAKQKKEKVWAHYEEQPVEEVMPVLEEKERSASYKPVFVTEITDDLHFYVQDVETGTQLEKLMENMRNDIASHPPVEGSYAPRRGEFCIAKFVDGEWYRARVEKVESPAKIHVFYIDYGNREVLPSTRLGTLSPAFSTRVLPAQATEYAFAFIQVPQDDDARTDAVDSVVRDIQNTQCLLNVEHLSAGCPHVTLQFADSKGDVGLGLVKEGLVMVEVRKEKQFQKVITEYLNAQESAKSARLNLWRYGDFRADDADEFGYSR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins","NDDs-related proteins","RNA-binding proteins"],"UniParc":"UPI00000727E5","uniref100":"UniRef100_Q7KZF4","uniref90":"UniRef90_Q7KZF4","uniref50":"UniRef50_Q7KZF4","genes":[{"name":{"value":"SND1"},"synonyms":[{"value":"TDRD11"}]}],"alphafold_very_low_content":0.03626373626373627,"disorder_content":0.01098901098901099,"disprot_consensus":{"full":[{"start":660,"end":669,"type":"D"}],"Structural state":[{"start":660,"end":669,"type":"D"}],"Disorder function":[{"start":660,"end":669,"type":"F"}]}},{"disprot_id":"DP03233","acc":"Q92900-2","creator":"vacs","date":"2021-04-12T16:31:20.760Z","features":{"pfam":[],"gene3D":[]},"length":1118,"name":"Isoform 2 of Regulator of nonsense transcripts 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":219,"end":228,"reference_id":"19556969","reference_source":"pmid","reference_html":"Unusual bipartite mode of interaction between the nonsense-mediated decay factors, UPF1 and UPF2. <i> Clerici M, Mourão A, Gutsche I, Gehring NH, Hentze MW, Kulozik A, Kadlec J, Sattler M, Cusack S. </i> EMBO J, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2WJV"},{"db":"PDB","id":"2WJY"}],"region_id":"DP03233r001","statement":[{"text":"The conserved loop L9 (residues 219–224) is poorly ordered in all structures, although it is in the vicinity of the long linker connecting the two interacting regions of UPF2.","type":"Results"},{"text":"However, the first part of this linker (1130–1145) has certain conserved features and is partially visible in the electron density in the vicinity of residues 219–224 of UPF1 loop L9, suggesting that both these regions may be involved in additional interactions at some stage during complex assembly.","type":"Discussion"},{"text":"Residues 219–228 are disordered in the unbound structure and become partially ordered in the UPF2-bound form (PDB 2WJV). The sequence in the PDB corresponds to isoform 2 of protein UPF1.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":219,"end":228,"reference_id":"19556969","reference_source":"pmid","reference_html":"Unusual bipartite mode of interaction between the nonsense-mediated decay factors, UPF1 and UPF2. <i> Clerici M, Mourão A, Gutsche I, Gehring NH, Hentze MW, Kulozik A, Kadlec J, Sattler M, Cusack S. </i> EMBO J, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03233r002","statement":[{"text":"The conserved loop L9 (residues 219–224) is poorly ordered in all structures, although it is in the vicinity of the long linker connecting the two interacting regions of UPF2.","type":"Results"},{"text":"Residues 219–228 are not visible in the electron density map. The sequence in the PDB corresponds to isoform 2 of protein UPF1.","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"2WJY"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MSVEAYGPSSQTLTFLDTEEAELLGADTQGSEFEFTDFTLPSQTQTPPGGPGGPGGGGAGGPGGAGAGAAAGQLDAQVGPEGILQNGAVDDSVAKTSQLLAELNFEEDEEDTYYTKDLPIHACSYCGIHDPACVVYCNTSKKWFCNGRGNTSGSHIVNHLVRAKCKEVTLHKDGPLGETVLECYNCGCRNVFLLGFIPAKADSVVVLLCRQPCASQSSLKDINWDSSQWQPLIQDRCFLSWLVKIPSEQEQLRARQITAQQINKLEELWKENPSATLEDLEKPGVDEEPQHVLLRYEDAYQYQNIFGPLVKLEADYDKKLKESQTQDNITVRWDLGLNKKRIAYFTLPKTDSDMRLMQGDEICLRYKGDLAPLWKGIGHVIKVPDNYGDEIAIELRSSVGAPVEVTHNFQVDFVWKSTSFDRMQSALKTFAVDETSVSGYIYHKLLGHEVEDVIIKCQLPKRFTAQGLPDLNHSQVYAVKTVLQRPLSLIQGPPGTGKTVTSATIVYHLARQGNGPVLVCAPSNIAVDQLTEKIHQTGLKVVRLCAKSREAIDSPVSFLALHNQIRNMDSMPELQKLQQLKDETGELSSADEKRYRALKRTAERELLMNADVICCTCVGAGDPRLAKMQFRSILIDESTQATEPECMVPVVLGAKQLILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVVLGIRPIRLQVQYRMHPALSAFPSNIFYEGSLQNGVTAADRVKKGFDFQWPQPDKPMFFYVTQGQEEIASSGTSYLNRTEAANVEKITTKLLKAGAKPDQIGIITPYEGQRSYLVQYMQFSGSLHTKLYQEVEIASVDAFQGREKDFIILSCVRANEHQGIGFLNDPRRLNVALTRARYGVIIVGNPKALSKQPLWNHLLNYYKEQKVLVEGPLNNLRESLMQFSKPRKLVNTINPGARFMTTAMYDAREAIIPGSVYDRSSQGRPSSMYFQTHDQIGMISAGPSHVAAMNIPIPFNLVMPPMPPPGYFGQANGPAAGRGTPKGKTGRGGRQKNRFGLPGPSQTNLPNSQASQDVASQPFSQGALTQGYISMSQPSQMSQPGLSQPELSQDSYLGDEFKSQIDVALSQDSTYQGERAYQHGGVTGLSQY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI0000001C89","uniref100":"","uniref90":"","uniref50":"","genes":[{"name":{"value":"UPF1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9962","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9962"}}]},"synonyms":[{"value":"KIAA0221"},{"value":"RENT1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9962","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9962"}}]}]}],"disorder_content":0.008944543828264758,"disprot_consensus":{"full":[{"start":219,"end":228,"type":"T"}],"Structural state":[{"start":219,"end":228,"type":"D"}],"Structural transition":[{"start":219,"end":228,"type":"T"}]}},{"disprot_id":"DP03234","acc":"P49915","creator":"fquaglia","date":"2021-04-13T08:37:17.693Z","features":{"pfam":[{"id":"PF00117","name":"Glutamine amidotransferase class-I","start":29,"end":209},{"id":"PF00958","name":"GMP synthase C terminal domain","start":599,"end":692},{"id":"PF02540","name":"NAD synthase","start":225,"end":300}],"gene3D":[]},"length":693,"name":"GMP synthase [glutamine-hydrolyzing]","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":312,"end":321,"reference_id":"23816837","reference_source":"pmid","reference_html":"Substrate specificity and oligomerization of human GMP synthetase. <i> Welin M, Lehtiö L, Johansson A, Flodin S, Nyman T, Trésaugues L, Hammarström M, Gräslund S, Nordlund P. </i> J Mol Biol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2VXO"}],"region_id":"DP03234r001","statement":[{"text":"Residues 25–693 and 23–693 have been modeled for subunits A and B, respectively (Fig. 1a), with the exception of some flexible regions with no electron density in chain A (35–36, 79–85, 121–127, 312–321) and in chain B (123–125, 312–321).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MALCNGDSKLENAGGDLKDGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETPAFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHKKSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANESKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVLVLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAAHSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPEEVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVRILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPHTLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDWESLIFLARLIPRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILRESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIPATPGNEIPVEVVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins"],"UniParc":"UPI0000000CC6","uniref100":"UniRef100_P49915","uniref90":"UniRef90_P49915","uniref50":"UniRef50_P49915","genes":[{"name":{"value":"GMPS"}}],"alphafold_very_low_content":0.05194805194805195,"disorder_content":0.01443001443001443,"disprot_consensus":{"full":[{"start":312,"end":321,"type":"D"}],"Structural state":[{"start":312,"end":321,"type":"D"}]}},{"disprot_id":"DP03235","acc":"P50148","creator":"fquaglia","date":"2021-04-13T08:51:26.664Z","features":{"pfam":[{"id":"PF00503","name":"G-protein alpha subunit","start":20,"end":348}],"gene3D":[]},"length":359,"name":"Guanine nucleotide-binding protein G(q) subunit alpha","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":216,"reference_id":"32126208","reference_source":"pmid","reference_html":"Structures of Gα Proteins in Complex with Their Chaperone Reveal Quality Control Mechanisms. <i> Seven AB, Hilger D, Papasergi-Scott MM, Zhang L, Qu Q, Kobilka BK, Tall GG, Skiniotis G. </i> Cell Rep, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6VU5"}],"region_id":"DP03235r001","statement":[{"text":"For Gαq, we were only able to build a model for residues 217–359 due to the weaker cryoEM map density in the N-terminal region compared to Gαi1.","type":"Methods"},{"text":"The majority of the Ras-like domain residues of both Gαi1 (residues 32–54 and 193–354) and Gαq (residues 217–359) were also unambiguously modeled in these maps.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPAYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI000016A979","uniref100":"UniRef100_P50148","uniref90":"UniRef90_P50148","uniref50":"UniRef50_P50148","genes":[{"name":{"value":"GNAQ"},"synonyms":[{"value":"GAQ"}]}],"alphafold_very_low_content":0.011142061281337047,"disorder_content":0.6016713091922006,"disprot_consensus":{"full":[{"start":1,"end":216,"type":"D"}],"Structural state":[{"start":1,"end":216,"type":"D"}]}},{"disprot_id":"DP03236","acc":"Q9UDY8","creator":"fquaglia","date":"2021-04-13T09:10:38.792Z","features":{"pfam":[{"id":"PF00656","name":"Caspase domain","start":343,"end":556},{"id":"PF13895","name":"Immunoglobulin domain","start":230,"end":307},{"id":"PF13927","name":"Immunoglobulin domain","start":128,"end":194},{"id":"PF18703","name":"MALT1 Ig-like domain","start":583,"end":719}],"gene3D":[]},"length":824,"name":"Mucosa-associated lymphoid tissue lymphoma translocation protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":469,"end":480,"reference_id":"22366302","reference_source":"pmid","reference_html":"Structural determinants of MALT1 protease activity. <i> Wiesmann C, Leder L, Blank J, Bernardi A, Melkko S, Decock A, D'Arcy A, Villard F, Erbel P, Hughes N, Freuler F, Nikolay R, Alves J, Bornancin F, Renatus M. </i> J Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3V55"}],"region_id":"DP03236r001","statement":[{"text":"As expected, the secondary structure elements are highly conserved between the two structures, and most of the changes occur in flexible loops connecting them (Fig. 2a, b, and d). Closer inspection of MALT1 and comparison with caspases reveal that the enzyme, albeit in its dimeric form and without the requirement of further processing to be active, has crystallized in an inactive state: loop L2 (residues 463–485), which carries the active-site cysteine C464 and forms the linker between the large and small subunits in caspases, appears flexible in MALT1 with residues 467–480 completely disordered in the electron density.","type":"Results"},{"text":"Binding of the covalent peptidic inhibitor induces the active conformation of MALT1. This transition involves structural changes especially in the loops L2, L3, and, to a lesser extent, L4, which delineate the active site but propagate throughout the molecule (Fig. 2a and d). Most prominently, loop L2, which is disordered in the inactive state of ligand-free MALT1, can be fully traced in the electron density of the inhibitor-bound structures.","type":"Results"},{"text":"PDB:3V55 and PDB:3V4O corresponds to the crystal structures of human MALT1(334-719) in its ligand free form and of of human MALT1 (caspase domain) in complex with an irreversible peptidic inhibitor, respectively.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:39:11.390Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":469,"end":480,"reference_id":"22366302","reference_source":"pmid","reference_html":"Structural determinants of MALT1 protease activity. <i> Wiesmann C, Leder L, Blank J, Bernardi A, Melkko S, Decock A, D'Arcy A, Villard F, Erbel P, Hughes N, Freuler F, Nikolay R, Alves J, Bornancin F, Renatus M. </i> J Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0036094","term_name":"small molecule binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"3V4O"}],"region_id":"DP03236r002","statement":[{"text":"Binding of the covalent peptidic inhibitor induces the active conformation of MALT1. This transition involves structural changes especially in the loops L2, L3, and, to a lesser extent, L4, which delineate the active site but propagate throughout the molecule (Fig. 2a and d). Most prominently, loop L2, which is disordered in the inactive state of ligand-free MALT1, can be fully traced in the electron density of the inhibitor-bound structures.","type":"Results"},{"text":"PDB:3V55 and PDB:3V4O corresponds to the crystal structures of human MALT1(334-719) in its ligand free form and of of human MALT1 (caspase domain) in complex with an irreversible peptidic inhibitor, respectively.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:39:13.789Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":469,"end":480,"reference_id":"22366302","reference_source":"pmid","reference_html":"Structural determinants of MALT1 protease activity. <i> Wiesmann C, Leder L, Blank J, Bernardi A, Melkko S, Decock A, D'Arcy A, Villard F, Erbel P, Hughes N, Freuler F, Nikolay R, Alves J, Bornancin F, Renatus M. </i> J Mol Biol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3V4O"}],"region_id":"DP03236r003","statement":[{"text":"Binding of the covalent peptidic inhibitor induces the active conformation of MALT1. This transition involves structural changes especially in the loops L2, L3, and, to a lesser extent, L4, which delineate the active site but propagate throughout the molecule (Fig. 2a and d). Most prominently, loop L2, which is disordered in the inactive state of ligand-free MALT1, can be fully traced in the electron density of the inhibitor-bound structures.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:39:12.235Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":566,"end":579,"reference_id":"22158899","reference_source":"pmid","reference_html":"Crystal structure of the mucosa-associated lymphoid tissue lymphoma translocation 1 (MALT1) paracaspase region. <i> Yu JW, Jeffrey PD, Ha JY, Yang X, Shi Y. </i> Proc Natl Acad Sci U S A, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3UOA"},{"db":"PDB","id":"3UO8"}],"region_id":"DP03236r004","statement":[{"text":"The intervening loop between the paracaspase domain and Ig domain, which extends from strand β6 of the caspase-like fold to helix α1 of the Ig fold, is likely flexible in solution as it is partially disordered in the crystal structure (Fig. 1B).","type":"Results"},{"text":"The intervening peptide sequences between the paracaspase domain and the Ig fold are disordered and are represented here as gray dotted lines.","type":"Figure"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:39:09.763Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":566,"end":579,"reference_id":"22158899","reference_source":"pmid","reference_html":"Crystal structure of the mucosa-associated lymphoid tissue lymphoma translocation 1 (MALT1) paracaspase region. <i> Yu JW, Jeffrey PD, Ha JY, Yang X, Shi Y. </i> Proc Natl Acad Sci U S A, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"3UOA"},{"db":"PDB","id":"3UO8"}],"region_id":"DP03236r005","statement":[{"text":"The intervening loop between the paracaspase domain and Ig domain, which extends from strand β6 of the caspase-like fold to helix α1 of the Ig fold, is likely flexible in solution as it is partially disordered in the crystal structure (Fig. 1B).","type":"Results"},{"text":"The intervening peptide sequences between the paracaspase domain and the Ig fold are disordered and are represented here as gray dotted lines.","type":"Figure"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:39:14.656Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":466,"end":481,"reference_id":"30692685","reference_source":"pmid","reference_html":"An allosteric MALT1 inhibitor is a molecular corrector rescuing function in an immunodeficient patient. <i> Quancard J, Klein T, Fung SY, Renatus M, Hughes N, Israël L, Priatel JJ, Kang S, Blank MA, Viner RI, Blank J, Schlapbach A, Erbel P, Kizhakkedathu J, Villard F, Hersperger R, Turvey SE, Eder J, Bornancin F, Overall CM. </i> Nat Chem Biol, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6H4A"},{"db":"PDB","id":"6F7I"}],"region_id":"DP03236r006","statement":[{"text":"While the ligand and the surrounding parts of the protein are well defined by electron density, other parts of the structure, mainly distal loops in the Ig3 domain and loops in the proximity of the active site, were disordered.","type":"Methods"},{"text":"PDB:6H4A and PDB:6F7I corresponds to the crystal structures of human MALT1(329-728) in complex with MLT-748 and with MLT-747, respectively.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:39:08.781Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":6,"released":"2021_12","sequence":"MSLLGDPLQALPPSAAPTGPLLAPPAGATLNRLREPLLRRLSELLDQAPEGRGWRRLAELAGSRGRLRLSCLDLEQCSLKVLEPEGSPSLCLLKLMGEKGCTVTELSDFLQAMEHTEVLQLLSPPGIKITVNPESKAVLAGQFVKLCCRATGHPFVQYQWFKMNKEIPNGNTSELIFNAVHVKDAGFYVCRVNNNFTFEFSQWSQLDVCDIPESFQRSVDGVSESKLQICVEPTSQKLMPGSTLVLQCVAVGSPIPHYQWFKNELPLTHETKKLYMVPYVDLEHQGTYWCHVYNDRDSQDSKKVEIIIGRTDEAVECTEDELNNLGHPDNKEQTTDQPLAKDKVALLIGNMNYREHPKLKAPLVDVYELTNLLRQLDFKVVSLLDLTEYEMRNAVDEFLLLLDKGVYGLLYYAGHGYENFGNSFMVPVDAPNPYRSENCLCVQNILKLMQEKETGLNVFLLDMCRKRNDYDDTIPILDALKVTANIVFGYATCQGAEAFEIQHSGLANGIFMKFLKDRLLEDKKITVLLDEVAEDMGKCHLTKGKQALEIRSSLSEKRALTDPIQGTEYSAESLVRNLQWAKAHELPESMCLKFDCGVQIQLGFAAEFSNVMIIYTSIVYKPPEIIMCDAYVTDFPLDLDIDPKDANKGTPEETGSYLVSKDLPKHCLYTRLSSLQKLKEHLVFTVCLSYQYSGLEDTVEDKQEVNVGKPLIAKLDMHRGLGRKTCFQTCLMSNGPYQSSAATSGGAGHYHSLQDPFHGVYHSHPGNPSNVTPADSCHCSRTPDAFISSFAHHASCHFSRSNVPVETTDEIPFSFSDRLRISEK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins"],"UniParc":"UPI000004D05E","uniref100":"UniRef100_Q9UDY8","uniref90":"UniRef90_Q9UDY8","uniref50":"UniRef50_Q9UDY8","genes":[{"name":{"value":"MALT1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10523859","url":"http://www.ncbi.nlm.nih.gov/pubmed/10523859","alternativeUrl":"https://europepmc.org/abstract/MED/10523859"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6819","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6819"}}]},"synonyms":[{"value":"MLT","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10339464","url":"http://www.ncbi.nlm.nih.gov/pubmed/10339464","alternativeUrl":"https://europepmc.org/abstract/MED/10339464"}}]}]}],"alphafold_very_low_content":0.19053398058252427,"disorder_content":0.03640776699029126,"disprot_consensus":{"full":[{"start":466,"end":468,"type":"D"},{"start":469,"end":480,"type":"T"},{"start":481,"end":481,"type":"D"},{"start":566,"end":579,"type":"D"}],"Structural state":[{"start":466,"end":481,"type":"D"},{"start":566,"end":579,"type":"D"}],"Molecular function":[{"start":469,"end":480,"type":"F"}],"Structural transition":[{"start":469,"end":480,"type":"T"}],"Disorder function":[{"start":566,"end":579,"type":"F"}]}},{"disprot_id":"DP03237","acc":"Q9BZE9","creator":"fquaglia","date":"2021-04-13T12:47:00.861Z","features":{"pfam":[{"id":"PF00789","name":"UBX domain","start":387,"end":459},{"id":"PF11470","name":"TUG ubiquitin-like domain","start":16,"end":78}],"gene3D":[]},"length":553,"name":"Tether containing UBX domain for GLUT4","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":498,"end":553,"reference_id":"27762274","reference_source":"pmid","reference_html":"Quantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers. <i> Arumughan A, Roske Y, Barth C, Forero LL, Bravo-Rodriguez K, Redel A, Kostova S, McShane E, Opitz R, Faelber K, Rau K, Mielke T, Daumke O, Selbach M, Sanchez-Garcia E, Rocks O, Panáková D, Heinemann U, Wanker EE. </i> Nat Commun, 2016","date":"2022-06-25T21:00:11.063Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":2,"cross_refs":[{"db":"PDB","id":"5IFS"}],"region_id":"DP03237r001","statement":[{"text":"Residues 313–316, 468–470 and 498–553 for ASPL-C and residues 1–20, 428–432 and 462–472 for p97-ND1 were disordered and therefore not visible in the electron density.","type":"Methods"}],"ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P55072"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":"glycerol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":"ethylene glycol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T12:45:23.147Z"}}],"regions_counter":1,"released":"2022_06","sequence":"MAAPAGGGGSAVSVLAPNGRRHTVKVTPSTVLLQVLEDTCRRQDFNPCEYDLKFQRSVLDLSLQWRFANLPNNAKLEMVPASRSREGPENMVRIALQLDDGSRLQDSFCSGQTLWELLSHFPQIRECLQHPGGATPVCVYTRDEVTGEAALRGTTLQSLGLTGGSATIRFVMKCYDPVGKTPGSLGSSASAGQAAASAPLPLESGELSRGDLSRPEDADTSGPCCEHTQEKQSTRAPAAAPFVPFSGGGQRLGGPPGPTRPLTSSSAKLPKSLSSPGGPSKPKKSKSGQDPQQEQEQERERDPQQEQERERPVDREPVDREPVVCHPDLEERLQAWPAELPDEFFELTVDDVRRRLAQLKSERKRLEEAPLVTKAFREAQIKEKLERYPKVALRVLFPDRYVLQGFFRPSETVGDLRDFVRSHLGNPELSFYLFITPPKTVLDDHTQTLFQANLFPAALVHLGAEEPAGVYLEPGLLEHAISPSAADVLVARYMSRAAGSPSPLPAPDPAPKSEPAAEEGALVPPEPIPGTAQPVKRSLGKVPKWLKLPASKR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins"],"UniParc":"UPI000004EF25","uniref100":"UniRef100_Q9BZE9","uniref90":"UniRef90_Q9BZE9","uniref50":"UniRef50_Q9BZE9","genes":[{"name":{"value":"ASPSCR1"},"synonyms":[{"value":"ASPL"},{"value":"RCC17"},{"value":"TUG"},{"value":"UBXD9"},{"value":"UBXN9"}]}],"alphafold_very_low_content":0.3309222423146474,"disorder_content":0.10126582278481013,"disprot_consensus":{"full":[{"start":498,"end":553,"type":"D"}],"Structural state":[{"start":498,"end":553,"type":"D"}]}},{"disprot_id":"DP03238","acc":"P55072","creator":"fquaglia","date":"2021-04-13T12:48:15.379Z","features":{"pfam":[{"id":"PF00004","name":"ATPase family associated with various cellular activities (AAA)","start":241,"end":370},{"id":"PF00004","name":"ATPase family associated with various cellular activities (AAA)","start":514,"end":647},{"id":"PF02359","name":"Cell division protein 48 (CDC48), N-terminal domain","start":25,"end":106},{"id":"PF02933","name":"Cell division protein 48 (CDC48), domain 2","start":126,"end":190},{"id":"PF17862","name":"AAA+ lid domain","start":393,"end":434},{"id":"PF17862","name":"AAA+ lid domain","start":669,"end":708}],"gene3D":[]},"length":806,"name":"Transitional endoplasmic reticulum ATPase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":20,"reference_id":"27762274","reference_source":"pmid","reference_html":"Quantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers. <i> Arumughan A, Roske Y, Barth C, Forero LL, Bravo-Rodriguez K, Redel A, Kostova S, McShane E, Opitz R, Faelber K, Rau K, Mielke T, Daumke O, Selbach M, Sanchez-Garcia E, Rocks O, Panáková D, Heinemann U, Wanker EE. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5IFS"}],"region_id":"DP03238r001","statement":[{"text":"Residues 313–316, 468–470 and 498–553 for ASPL-C and residues 1–20, 428–432 and 462–472 for p97-ND1 were disordered and therefore not visible in the electron density.","type":"Methods"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-10-31T19:20:48.775Z"}},{"start":462,"end":472,"reference_id":"27762274","reference_source":"pmid","reference_html":"Quantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers. <i> Arumughan A, Roske Y, Barth C, Forero LL, Bravo-Rodriguez K, Redel A, Kostova S, McShane E, Opitz R, Faelber K, Rau K, Mielke T, Daumke O, Selbach M, Sanchez-Garcia E, Rocks O, Panáková D, Heinemann U, Wanker EE. </i> Nat Commun, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5IFS"}],"region_id":"DP03238r002","statement":[{"text":"Residues 313–316, 468–470 and 498–553 for ASPL-C and residues 1–20, 428–432 and 462–472 for p97-ND1 were disordered and therefore not visible in the electron density.","type":"Methods"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-10-31T19:20:48.066Z"}},{"start":776,"end":806,"reference_id":"34765927","reference_source":"pmid","reference_html":"Cryo-electron microscopy structures of VCP/p97 reveal a new mechanism of oligomerization regulation. <i> Yu G, Bai Y, Li K, Amarasinghe O, Jiang W, Zhang ZY. </i> iScience, 2021","date":"2024-08-19T14:10:18.380Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"EMDB","id":"22675"},{"db":"PDB","id":"7K56"}],"region_id":"DP03238r003","statement":[{"text":"Unlike others in the NSF/Cdc48/Pex AAA+ ATPase family, members of the VCP/Cdc48 subgroup contain a unique CTE that provides the binding interface for a subset of VCP cofactors (Hänzelmann and Schindelin, 2017) but has been found disordered and missing in most resolved structures (X. Zhang et al., 2000; DeLaBarre and Brunger, 2003; Davies et al., 2008; Banerjee et al., 2016; Hänzelmann and Schindelin, 2016).","type":"Introduction"},{"text":"This region lacks electron density in the PDB structure, indicating it is disordered.","type":"Curator statement"}]},{"start":776,"end":806,"reference_id":"34765927","reference_source":"pmid","reference_html":"Cryo-electron microscopy structures of VCP/p97 reveal a new mechanism of oligomerization regulation. <i> Yu G, Bai Y, Li K, Amarasinghe O, Jiang W, Zhang ZY. </i> iScience, 2021","date":"2024-08-19T14:12:07.333Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"EMDB","id":"22675"},{"db":"PDB","id":"7K56"}],"region_id":"DP03238r004","statement":[{"text":"Unlike others in the NSF/Cdc48/Pex AAA+ ATPase family, members of the VCP/Cdc48 subgroup contain a unique CTE that provides the binding interface for a subset of VCP cofactors (Hänzelmann and Schindelin, 2017) but has been found disordered and missing in most resolved structures (X. Zhang et al., 2000; DeLaBarre and Brunger, 2003; Davies et al., 2008; Banerjee et al., 2016; Hänzelmann and Schindelin, 2016).","type":"Introduction"},{"text":"This region lacks electron density in the PDB structure, indicating it is disordered.","type":"Curator statement"},{"text":"(C) The domain organization and key structural elements of VCP. Each VCP monomer comprises a regulatory N-terminal domain (NTD, residues 1-187), two AAA+ ATPase domains (D1: residues 209–462 and D2: residues 481–762) and a C-terminal extension (CTE, residues 763–806).","type":"Figure"}]},{"start":586,"end":598,"reference_id":"34765927","reference_source":"pmid","reference_html":"Cryo-electron microscopy structures of VCP/p97 reveal a new mechanism of oligomerization regulation. <i> Yu G, Bai Y, Li K, Amarasinghe O, Jiang W, Zhang ZY. </i> iScience, 2021","date":"2024-08-19T14:15:48.609Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"EMDB","id":"22675"},{"db":"PDB","id":"7K56"}],"region_id":"DP03238r005","statement":[{"text":"Residues 586–598 in D2 were disordered.","type":"Figure"},{"text":"Residues 1–21 and 586–598 were removed from the model due to weak electron densities (Figures S3A and S3B).","type":"Results"},{"text":"This region lacks electron density in the PDB structure, indicating it is disordered.","type":"Curator statement"}]},{"start":1,"end":21,"reference_id":"34765927","reference_source":"pmid","reference_html":"Cryo-electron microscopy structures of VCP/p97 reveal a new mechanism of oligomerization regulation. <i> Yu G, Bai Y, Li K, Amarasinghe O, Jiang W, Zhang ZY. </i> iScience, 2021","date":"2024-08-19T14:16:17.888Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"EMDB","id":"22675"},{"db":"PDB","id":"7K56"}],"region_id":"DP03238r006","statement":[{"text":"Residues 1–21 and 586–598 were removed from the model due to weak electron densities (Figures S3A and S3B).","type":"Introduction"},{"text":"This region lacks electron density in the PDB structure, indicating it is disordered.","type":"Curator statement"}]},{"start":1,"end":21,"reference_id":"34765927","reference_source":"pmid","reference_html":"Cryo-electron microscopy structures of VCP/p97 reveal a new mechanism of oligomerization regulation. <i> Yu G, Bai Y, Li K, Amarasinghe O, Jiang W, Zhang ZY. </i> iScience, 2021","date":"2024-08-19T14:16:28.764Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"EMDB","id":"22675"},{"db":"PDB","id":"7K56"}],"region_id":"DP03238r007","statement":[{"text":"Residues 1–21 and 586–598 were removed from the model due to weak electron densities (Figures S3A and S3B).","type":"Introduction"},{"text":"This region lacks electron density in the PDB structure, indicating it is disordered.","type":"Curator statement"}]},{"start":794,"end":806,"reference_id":"31847414","reference_source":"pmid","reference_html":"Structure of the PUB Domain from Ubiquitin Regulatory X Domain Protein 1 (UBXD1) and Its Interaction with the p97 AAA+ ATPase. <i> Blueggel M, van den Boom J, Meyer H, Bayer P, Beuck C. </i> Biomolecules, 2019","date":"2024-08-19T14:28:34.554Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9BZV1","operator":null,"partner_start":175,"partner_end":261}],"region_id":"DP03238r008","statement":[{"text":"Titration of 15N-UBXD1-PUB with the p97-C10 and p97-C13 peptide showed large (>0.2 ppm) chemical shift perturbations (CSPs) of resonances assigned to amide groups residing in the region between the second and fourth α-helix (Figure 3 and Figure S1). The interacting residues V175, A179, K180, Y181, L182, I185, L187, E191, K193, Y194, K198, L199, Q200, N201, V203, E206, R207, N209, A230, F239, E258, and L261 are mapped onto the PUB structure in Figure 3.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":797,"end":806,"reference_id":"31847414","reference_source":"pmid","reference_html":"Structure of the PUB Domain from Ubiquitin Regulatory X Domain Protein 1 (UBXD1) and Its Interaction with the p97 AAA+ ATPase. <i> Blueggel M, van den Boom J, Meyer H, Bayer P, Beuck C. </i> Biomolecules, 2019","date":"2024-08-19T14:31:01.661Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9BZV1","operator":null,"partner_start":150,"partner_end":264}],"region_id":"DP03238r009","statement":[{"text":"In our hands, isothermal titration calorimetry (ITC) experiments showed that the peptide comprising the last 10 residues of p97 (p97–C10) interacts with UBXD1-PUB with a 1:1 stoichiometry (n = 1.1 ± 0.2) and a KD of 15 ± 5 µM, ΔH = -3255 ± 483 cal/mol, and ΔS = 10 cal/mol/K.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":802,"end":806,"reference_id":"31847414","reference_source":"pmid","reference_html":"Structure of the PUB Domain from Ubiquitin Regulatory X Domain Protein 1 (UBXD1) and Its Interaction with the p97 AAA+ ATPase. <i> Blueggel M, van den Boom J, Meyer H, Bayer P, Beuck C. </i> Biomolecules, 2019","date":"2024-08-19T14:35:17.761Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0032091","term_name":"negative regulation of protein binding","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":805,"end":805,"position":"Specific residue","statements":[{"type":"Methods","text":"Unlabeled p97-C10 (TEDNDDDLYG), p97-C13 (SVYTEDNDDDLYG), and phosphorylated p97-C13 (SVYTEDNDDDLpYG) peptides for NMR and ITC as well as 5,6-FAM-labeled peptides for fluorescence studies were purchased from Caslo ApS (Denmark)."}]}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9BZV1","operator":null,"partner_start":150,"partner_end":264}],"region_id":"DP03238r010","statement":[{"text":"In contrast to the unmodified p97-PIM, the p97-C13 peptide carrying a phosphorylated pY805 did not show any binding in a 15N-HSQC NMR titration up to a concentration of 1.25 mM (Figure S1B), which is consistent with phosphorylation of p97-Y805 also completely abolishing binding of the PNGase and HOIP PUB domains [25,34].","type":"Results"}],"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of protein binding.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":10,"released":"2021_12","sequence":"MASGADSKGDDLSTAILKQKNRPNRLIVDEAINEDNSVVSLSQPKMDELQLFRGDTVLLKGKKRREAVCIVLSDDTCSDEKIRMNRVVRNNLRVRLGDVISIQPCPDVKYGKRIHVLPIDDTVEGITGNLFEVYLKPYFLEAYRPIRKGDIFLVRGGMRAVEFKVVETDPSPYCIVAPDTVIHCEGEPIKREDEEESLNEVGYDDIGGCRKQLAQIKEMVELPLRHPALFKAIGVKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAIIFIDELDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFDREVDIGIPDATGRLEILQIHTKNMKLADDVDLEQVANETHGHVGADLAALCSEAALQAIRKKMDLIDLEDETIDAEVMNSLAVTMDDFRWALSQSNPSALRETVVEVPQVTWEDIGGLEDVKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVREIFDKARQAAPCVLFFDELDSIAKARGGNIGDGGGAADRVINQILTEMDGMSTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIPLPDEKSRVAILKANLRKSPVAKDVDLEFLAKMTNGFSGADLTEICQRACKLAIRESIESEIRRERERQTNPSAMEVEEDDPVPEIRRDHFEEAMRFARRSVSDNDIRKYEMFAQTLQQSRGFGSFRFPSGNQGGAGPSQGSGGGTGGSVYTEDNDDDLYG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Condensates-related proteins","Age-related disorders proteins"],"UniParc":"UPI00003BF806","uniref100":"UniRef100_P55072","uniref90":"UniRef90_P55072","uniref50":"UniRef50_P55072","genes":[{"name":{"value":"VCP"}}],"alphafold_very_low_content":0.06699751861042183,"disorder_content":0.09429280397022333,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"},{"start":462,"end":472,"type":"D"},{"start":586,"end":598,"type":"D"},{"start":776,"end":806,"type":"D"}],"Structural state":[{"start":1,"end":21,"type":"D"},{"start":462,"end":472,"type":"D"},{"start":586,"end":598,"type":"D"},{"start":776,"end":806,"type":"D"}],"Disorder function":[{"start":1,"end":21,"type":"F"},{"start":776,"end":806,"type":"F"}],"Molecular function":[{"start":794,"end":806,"type":"F"}],"Biological process":[{"start":802,"end":806,"type":"F"}]}},{"disprot_id":"DP03239","acc":"P52874","creator":"lrodriguez","date":"2021-04-15T12:43:53.370Z","features":{"pfam":[{"id":"PF06807","name":"Pre-mRNA cleavage complex II protein Clp1","start":313,"end":423},{"id":"PF16573","name":"N-terminal beta-sandwich domain of polyadenylation factor","start":11,"end":100},{"id":"PF16575","name":"mRNA cleavage and polyadenylation factor CLP1 P-loop","start":121,"end":307}],"gene3D":[]},"length":428,"name":"Protein clpf-1","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":332,"end":348,"reference_id":"24813946","reference_source":"pmid","reference_html":"RNA specificity and regulation of catalysis in the eukaryotic polynucleotide kinase Clp1. <i> Dikfidan A, Loll B, Zeymer C, Magler I, Clausen T, Meinhart A. </i> Mol Cell, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"lrodriguez","curator_name":"Luciana Rodriguez Sawicki","curator_orcid":"0000-0001-5782-6573","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4OI2"},{"db":"PDB","id":"4OHW"},{"db":"PDB","id":"4OHX"},{"db":"PDB","id":"4OHY"},{"db":"PDB","id":"4OI0"},{"db":"PDB","id":"4OI1"}],"region_id":"DP03239r001","statement":[{"text":"\"Gray lines, framed by slanted lines, indicated sections of ceClp1 that are not included in  the crystal structure.\"","type":"Supplementary material"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-05T14:32:56.862Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MSEENVQEFVLKEDCELRFAAGDDSDVCLELVKGYAEIFGTELLLNKKYTFPAKSRVAAFTWKGATIELVGTTESAYVAESTPMVIYLNIHAAMEEVRKKREEQAAGNSNKAKGPRLLLVGPTDVGKTTVSRILCNYSVRQGRTPIFVELDVGQNSVSVPGTVAAVLVQKTADVIDGFERNQPIVFNFGHTSPSANLSLYEALFKEMATTLNAQIQENDEAKIGGMIINTCGWVDGEGYKCIVKAASAFEVDVVIVLDHERLYSDLSKELPEFVRLTHVPKSGGVEQRTGQIRSKMRGENVHRYFYGTRANNLYPFTFDVSFDDVTLCKIGAEQLPDSCLPFGMEVENHETKLVIMEPSADIKHHLFAFSRSTKADENVLKSPVFGFCLVTEVDLEKRTMSILCPQRTIPSKVLVFSDITHLDDQIKR","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"dataset":[],"UniParc":"UPI000006109C","uniref100":"UniRef100_P52874","uniref90":"UniRef90_P52874","uniref50":"UniRef50_P52874","genes":[{"name":{"value":"clpf-1","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03035","url":"https://hamap.expasy.org/unirule/MF_03035"}}]},"orfNames":[{"value":"F59A2.4"}]}],"alphafold_very_low_content":0.007009345794392523,"disorder_content":0.0397196261682243,"disprot_consensus":{"full":[{"start":332,"end":348,"type":"D"}],"Structural state":[{"start":332,"end":348,"type":"D"}]}},{"disprot_id":"DP03240","acc":"P0A8Q6","creator":"vacs","date":"2021-04-16T11:55:42.151Z","features":{"pfam":[{"id":"PF02617","name":"ATP-dependent Clp protease adaptor protein ClpS","start":23,"end":102}],"gene3D":[]},"length":106,"name":"ATP-dependent Clp protease adapter protein ClpS","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":1,"end":20,"reference_id":"12235156","reference_source":"pmid","reference_html":"Crystal structure of the heterodimeric complex of the adaptor, ClpS, with the N-domain of the AAA+ chaperone, ClpA. <i> Guo F, Esser L, Singh SK, Maurizi MR, Xia D. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1MBU"},{"db":"PDB","id":"1MBV"},{"db":"PDB","id":"1MBX"}],"region_id":"DP03240r001","statement":[{"text":"The N-terminal 20 residues of ClpS are not visible in the crystal structures; the removal of the first 17 residues produces ClpSΔN, which binds to the ClpA N-domain but no longer inhibits ClpA activity.","type":"Abstract"},{"text":"In the trigonal crystal, 87 out of 106 residues in ClpS can be seen in the two NCS-related heterodimers; the missing residues are from the N terminus.","type":"Results"},{"text":"The N-terminal residues from 21 to 26 extend out of the top of the cone, but residues 1–20 were not all visible.","type":"Results"},{"text":"The N-terminal chain of ClpS extends along the N-domain parallel to helix H3 until the density disappears; this configuration would probably place the missing residues near the C terminus of the N-domain and away from the acidic loop connecting the two halves (Fig. 2A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-04-20T16:01:49.870Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":17,"reference_id":"12235156","reference_source":"pmid","reference_html":"Crystal structure of the heterodimeric complex of the adaptor, ClpS, with the N-domain of the AAA+ chaperone, ClpA. <i> Guo F, Esser L, Singh SK, Maurizi MR, Xia D. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03240r002","statement":[{"text":"The N-terminal 20 residues of ClpS are not visible in the crystal structures; the removal of the first 17 residues produces ClpSΔN, which binds to the ClpA N-domain but no longer inhibits ClpA activity.","type":"Abstract"},{"text":"When the N-terminal 17 amino acids of ClpS were removed by lysylendopeptidase C treatment, the resulting ClpSΔN could still bind to ClpA and the isolated N-domain of ClpA (Fig. 1, A and B); however, ClpSΔN was no longer able to inhibit proteolytic activity of ClpAP. Table III shows that both casein and green fluorescent protein-SsrA degradation were unaffected by ClpSΔN.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-04-21T07:48:33.791Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":22,"reference_id":"12426582","reference_source":"pmid","reference_html":"Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA. <i> Zeth K, Ravelli RB, Paal K, Cusack S, Bukau B, Dougan DA. </i> Nat Struct Biol, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1MG9"}],"region_id":"DP03240r003","statement":[{"text":"The structure of the complex crystallized in tetragonal space group was solved by molecular replacement using the refined model of the orthorhombic space group. Although this structure could be refined at 2.3 Å resolution to a crystallographic R-factor of 25.2 (Rfree = 29.4%), several residues were not visible, namely the N-terminal residues of ClpS (1–22) and three residues in the N-domain of ClpA (73–75).","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-04-20T16:01:27.685Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":20,"reference_id":"12426582","reference_source":"pmid","reference_html":"Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA. <i> Zeth K, Ravelli RB, Paal K, Cusack S, Bukau B, Dougan DA. </i> Nat Struct Biol, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1LZW"}],"region_id":"DP03240r004","statement":[{"text":"In the final structure, five residues of ClpS (16–20) and three residues in ClpA161 (73–75) were replaced with Ala because they showed only main chain density. The final structure consists of 146 of the 161 residues from ClpA161, 91 of 106 residues from ClpS and 49 ordered solvent molecules.","type":"Article"},{"text":"The N-terminal region of ClpS is poorly defined; the first 15 residues are not visible in the electron density maps, and the next 13 residues (16–28), although present, form an extended coiled protein chain.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-04-20T16:01:21.701Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":4,"released":"2021_06","sequence":"MGKTNDWLDFDQLAEEKVRDALKPPSMYKVILVNDDYTPMEFVIDVLQKFFSYDVERATQLMLAVHYQGKAICGVFTAEVAETKVAMVNKYARENEHPLLCTLEKA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":[],"UniParc":"UPI00000350BA","uniref100":"UniRef100_A7ZJU9","uniref90":"UniRef90_A9MI06","uniref50":"UniRef50_Q6D3T7","genes":[{"name":{"value":"clpS","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00302","url":"https://hamap.expasy.org/unirule/MF_00302"}}]},"synonyms":[{"value":"yljA"}],"olnNames":[{"value":"b0881"},{"value":"JW0865"}]}],"alphafold_very_low_content":0.018867924528301886,"disorder_content":0.20754716981132076,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"}],"Structural state":[{"start":1,"end":22,"type":"D"}],"Molecular function":[{"start":1,"end":17,"type":"F"}]}},{"disprot_id":"DP03241","acc":"P0ABH9","creator":"vacs","date":"2021-04-16T15:06:14.660Z","features":{"pfam":[{"id":"PF00004","name":"ATPase family associated with various cellular activities (AAA)","start":211,"end":343},{"id":"PF02861","name":"Clp repeat (R) N-terminal domain","start":2,"end":126},{"id":"PF07724","name":"AAA domain (Cdc48 subfamily)","start":486,"end":647},{"id":"PF10431","name":"C-terminal, D2-small domain, of ClpB protein","start":653,"end":733},{"id":"PF17871","name":"AAA lid domain","start":350,"end":452}],"gene3D":[]},"length":758,"name":"ATP-dependent Clp protease ATP-binding subunit ClpA","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":143,"end":167,"reference_id":"12205096","reference_source":"pmid","reference_html":"Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease. <i> Guo F, Maurizi MR, Esser L, Xia D. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1KSF"}],"region_id":"DP03241r001","statement":[{"text":"There are several disordered regions in the ClpA structure; all of them are loops connecting secondary structure elements or between domains (Fig. 1b).","type":"Results"},{"text":"The electron density for the 25 residues connecting the N-domain and D1 was not visible, but we were able to identify the cognate N-domain based on three criteria: the distance between the C-terminal residues of the N-domains and the first determined residue of D1, the surface area buried by each N-domain-D1D2 contact, and the location of contact interface.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-04-20T16:24:14.737Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":611,"end":623,"reference_id":"12205096","reference_source":"pmid","reference_html":"Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease. <i> Guo F, Maurizi MR, Esser L, Xia D. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1KSF"}],"region_id":"DP03241r002","statement":[{"text":"There are several disordered regions in the ClpA structure; all of them are loops connecting secondary structure elements or between domains (Fig. 1b).","type":"Results"},{"text":"Other regions for which density was not well defined included residues 252–255, residues 295–300, and notably residues 611–625 (Fig. 1b).","type":"Results"},{"text":"The “ClpP loop,” containing the sequence IGL, which has been implicated in activation of ClpP activity by ClpA (25, 26), was not visible in the crystal. However, residues 611 and 624, which flank the loop, are located on the distal surface of D2 at about 30–35 Å from the center (Fig. 5, b and d).","type":"Results"},{"text":"Residues 611-623 are not visible in the electron density map.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":142,"end":168,"reference_id":"15037248","reference_source":"pmid","reference_html":"Crystallographic investigation of peptide binding sites in the N-domain of the ClpA chaperone. <i> Xia D, Esser L, Singh SK, Guo F, Maurizi MR. </i> J Struct Biol, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1R6B"}],"region_id":"DP03241r003","statement":[{"text":"ClpA consists of three functional domains: an N-terminal domain and two ATPase domains, D1 and D2. The N-domain is attached to D1 by a mobile linker and is made up of two tightly bound, identically folded a-helical bundles related by a pseudo 2-fold symmetry.","type":"Abstract"},{"text":"Residues 142-168 are not visible in the electron density map.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-04-20T16:26:28.867Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":143,"end":167,"reference_id":"12205096","reference_source":"pmid","reference_html":"Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease. <i> Guo F, Maurizi MR, Esser L, Xia D. </i> J Biol Chem, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":4,"region_id":"DP03241r004","statement":[{"text":"There are several disordered regions in the ClpA structure; all of them are loops connecting secondary structure elements or between domains (Fig. 1b).","type":"Results"},{"text":"The full length ClpA subunit consists of five tandemly linked structural domains (Fig. 1a) corresponding to three functional groups: an N-domain and two AAA ATPase modules. The N-domain has 142 residues; the first AAA ATPase module (D1) has 270 residues and the second ATPase module (D2) contains 319 residues, each consisting of a large and a small sub-domain (Fig. 1b).","type":"Results"},{"text":"The electron density for the 25 residues connecting the N-domain and D1 was not visible, but we were able to identify the cognate N-domain based on three criteria: the distance between the C-terminal residues of the N-domains and the first determined residue of D1, the surface area buried by each N-domain-D1D2 contact, and the location of contact interface.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":4,"released":"2021_12","sequence":"MLNQELELSLNMAFARAREHRHEFMTVEHLLLALLSNPSAREALEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQPTLSFQRVLQRAVFHVQSSGRNEVTGANVLVAIFSEQESQAAYLLRKHEVSRLDVVNFISHGTRKDEPTQSSDPGSQPNSEEQAGGEERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYSLDIGSLLAGTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTIIGAGAASGGQVDAANLIKPLLSSGKIRVIGSTTYQEFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGARARLMPVSKRKKTVNVADIESVVARIARIPEKSVSQSDRDTLKNLGDRLKMLVFGQDKAIEALTEAIKMARAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKALGIELLRFDMSEYMERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNILLQVMDNGTLTDNNGRKADFRNVVLVMTTNAGVRETERKSIGLIHQDNSTDAMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQVQLDQKGVSLEVSQEARNWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKEKNELTYGFQSAQKHKAEAAH","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":[],"UniParc":"UPI0000127B09","uniref100":"UniRef100_P0ABI1","uniref90":"UniRef90_P0ABI1","uniref50":"UniRef50_P0ABI1","genes":[{"name":{"value":"clpA"},"synonyms":[{"value":"lopD"}],"olnNames":[{"value":"b0882"},{"value":"JW0866"}]}],"alphafold_very_low_content":0.047493403693931395,"disorder_content":0.052770448548812667,"disprot_consensus":{"full":[{"start":142,"end":168,"type":"D"},{"start":611,"end":623,"type":"D"}],"Structural state":[{"start":142,"end":168,"type":"D"},{"start":611,"end":623,"type":"D"}],"Disorder function":[{"start":143,"end":167,"type":"F"}]}},{"disprot_id":"DP03242","acc":"P23588","creator":"rpancsa","date":"2021-04-19T14:27:32.762Z","features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":99,"end":167}],"gene3D":[]},"length":611,"name":"Eukaryotic translation initiation factor 4B","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":96,"reference_id":"29401259","reference_source":"pmid","reference_html":"Structure of a human cap-dependent 48S translation pre-initiation complex. <i> Eliseev B, Yeramala L, Leitner A, Karuppasamy M, Raimondeau E, Huard K, Alkalaeva E, Aebersold R, Schaffitzel C. </i> Nucleic Acids Res, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"cbassot","curator_name":"Claudio Bassot","curator_orcid":"0000-0001-7161-9028","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6FEC"}],"region_id":"DP03242r001","statement":[{"text":"In the structure, no additional unfilled density is observed next to eS28 and eIF3d (Supplementary Figure S7B), indicating that the eIF4B BD is rather flexible.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":172,"end":611,"reference_id":"29401259","reference_source":"pmid","reference_html":"Structure of a human cap-dependent 48S translation pre-initiation complex. <i> Eliseev B, Yeramala L, Leitner A, Karuppasamy M, Raimondeau E, Huard K, Alkalaeva E, Aebersold R, Schaffitzel C. </i> Nucleic Acids Res, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"cbassot","curator_name":"Claudio Bassot","curator_orcid":"0000-0001-7161-9028","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6FEC"}],"region_id":"DP03242r002","statement":[{"text":" \"In the structure, no additional unfilled density is observed next to eS28 and eIF3d (Supplementary Figure S7B), indicating that the eIF4B BD is rather flexible.\" ","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":333,"end":611,"reference_id":"37368134","reference_source":"pmid","reference_html":"Backbone resonance assignments of the C-terminal region of human translation initiation factor eIF4B. <i> Mondal S, Rousseau S, Talenton V, Thiam CAB, Aznauryan M, Mackereth CD. </i> Biomol NMR Assign, 2023","date":"2024-02-29T08:24:47.690Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":null,"value":293,"statements":[{"type":"Article","text":"The final samples of uniformly 13C, 15N-labeled eIF4B constructs were prepared in a buffer of 20 mM sodium phosphate (pH 7.0), 150 mM NaCl, 2 mM dithithreitol (DTT), with 10% (v/v) D2O added for the lock. NMR samples contained 170 µL in a 3 mm NMR tube, and assignment spectra were collected at 293 K on a Bruker Avance 700 MHz spectrometer with a triple-resonance gradient room-temperature probe."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7,"statements":[{"type":"Article","text":"The final samples of uniformly 13C, 15N-labeled eIF4B constructs were prepared in a buffer of 20 mM sodium phosphate (pH 7.0), 150 mM NaCl, 2 mM dithithreitol (DTT), with 10% (v/v) D2O added for the lock. NMR samples contained 170 µL in a 3 mm NMR tube, and assignment spectra were collected at 293 K on a Bruker Avance 700 MHz spectrometer with a triple-resonance gradient room-temperature probe."}]}],"cross_refs":[{"db":"BMRB","id":"51957"},{"db":"BMRB","id":"51952"},{"db":"BMRB","id":"51953"}],"region_id":"DP03242r003","statement":[{"text":"Based on an initial 1H,15N-HSQC spectrum acquired for the complete C-terminal region of human eIF4B (eIF4B-CTR, residues 333–611), it was evident that the backbone amide 1HN chemical shift values were restricted to 8.0-8.5 ppm (Fig. 1A), and thus the construct was predominantly disordered.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T10:24:55.222Z"}}],"regions_counter":3,"released":"2021_12","sequence":"MAASAKKKNKKGKTISLTDFLAEDGGTGGGSTYVSKPVSWADETDDLEGDVSTTWHSNDDDVYRAPPIDRSILPTAPRAAREPNIDRSRLPKSPPYTAFLGNLPYDVTEESIKEFFRGLNISAVRLPREPSNPERLKGFGYAEFEDLDSLLSALSLNEESLGNRRIRVDVADQAQDKDRDDRSFGRDRNRDSDKTDTDWRARPATDSFDDYPPRRGDDSFGDKYRDRYDSDRYRDGYRDGYRDGPRRDMDRYGGRDRYDDRGSRDYDRGYDSRIGSGRRAFGSGYRRDDDYRGGGDRYEDRYDRRDDRSWSSRDDYSRDDYRRDDRGPPQRPKLNLKPRSTPKEDDSSASTSQSTRAASIFGGAKPVDTAAREREVEERLQKEQEKLQRQLDEPKLERRPRERHPSWRSEETQERERSRTGSESSQTGTSTTSSRNARRRESEKSLENETLNKEEDCHSPTSKPPKPDQPLKVMPAPPPKENAWVKRSSNPPARSQSSDTEQQSPTSGGGKVAPAQPSEEGPGRKDENKVDGMNAPKGQTGNSSRGPGDGGNRDHWKESDRKDGKKDQDSRSAPEPKKPEENPASKFSSASKYAALSVDGEDENEGEDYAE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000004BA76","uniref100":"UniRef100_P23588","uniref90":"UniRef90_P23588","uniref50":"UniRef50_P23588","genes":[{"name":{"value":"EIF4B"}}],"alphafold_very_low_content":0.602291325695581,"disorder_content":0.8772504091653028,"disprot_consensus":{"full":[{"start":1,"end":96,"type":"D"},{"start":172,"end":611,"type":"D"}],"Structural state":[{"start":1,"end":96,"type":"D"},{"start":172,"end":611,"type":"D"}]}},{"disprot_id":"DP03243","acc":"Q68D10","creator":"cbassot","date":"2021-04-19T15:39:52.928Z","features":{"pfam":[{"id":"PF08243","name":"SPT2 chromatin protein","start":582,"end":681},{"id":"PF22878","name":"SPT2 N-terminal domain","start":1,"end":90}],"gene3D":[]},"length":685,"name":"Protein SPT2 homolog","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":571,"end":604,"reference_id":"26109053","reference_source":"pmid","reference_html":"Structure-function studies of histone H3/H4 tetramer maintenance during transcription by chaperone Spt2. <i> Chen S, Rufiange A, Huang H, Rajashankar KR, Nourani A, Patel DJ. </i> Genes Dev, 2015","date":"2022-08-03T14:19:50.765Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":3,"cross_refs":[{"db":"PDB","id":"5BS7"}],"region_id":"DP03243r001","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":8,"released":"2023_12","sequence":"MDFREILMIASKGQGVNNVPKRYSLAVGPPKKDPKVKGVQSAAVQAFLKRKEEELRRKALEEKRRKEELVKKRIELKHDKKARAMAKRTKDNFHGYNGIPIEEKSKKRQATESHTSQGTDREYEMEEENEFLEYNHAESEQEYEEEQEPPKVESKPKVPLKSAPPPMNFTDLLRLAEKKQFEPVEIKVVKKSEERPMTAEELREREFLERKHRRKKLETDGKLPPTVSKKAPSQKESVGTKLSKGSGDRHPSSKGMPLPHAEKKSRPSMANEKHLALSSSKSMPGERIKAGSGNSSQPSLREGHDKPVFNGAGKPHSSTSSPSVPKTSASRTQKSAVEHKAKKSLSHPSHSRPGPMVTPHNKAKSPGVRQPGSSSSSAPGQPSTGVARPTVSSGPVPRRQNGSSSSGPERSISGSKKPTNDSNPSRRTVSGTCGPGQPASSSGGPGRPISGSVSSARPLGSSRGPGRPVSSPHELRRPVSGLGPPGRSVSGPGRSISGSIPAGRTVSNSVPGRPVSSLGPGQTVSSSGPTIKPKCTVVSETISSKNIISRSSNGQMNGMKPPLSGYRAAQGPQRLPFPTGYKRQREYEEEDDDDDEYDSEMEDFIEDEGEPQEEISKHIREIFGYDRKKYKDESDYALRYMESSWKEQQKEEAKSLRLGMQEDLEEMRREEEEMQRRRAKKLKRR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000041A189","uniref100":"UniRef100_Q68D10","uniref90":"UniRef90_Q68D10","uniref50":"UniRef50_Q68D10","genes":[{"name":{"value":"SPTY2D1"}}],"alphafold_very_low_content":0.5255474452554745,"disorder_content":0.049635036496350364,"disprot_consensus":{"full":[{"start":571,"end":604,"type":"D"}],"Structural state":[{"start":571,"end":604,"type":"D"}]}},{"disprot_id":"DP03245","acc":"Q9UQ35","creator":"smribeiro","date":"2021-04-19T20:24:48.251Z","features":{"pfam":[{"id":"PF08312","name":"cwf21 domain","start":58,"end":101}],"gene3D":[]},"length":2752,"name":"Serine/arginine repetitive matrix protein 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":31,"end":2752,"reference_id":"28076346","reference_source":"pmid","reference_html":"Cryo-EM structure of a human spliceosome activated for step 2 of splicing. <i> Bertram K, Agafonov DE, Liu WT, Dybkov O, Will CL, Hartmuth K, Urlaub H, Kastner B, Stark H, Lührmann R. </i> Nature, 2017","date":"2023-11-28T17:16:42.749Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":4,"cross_refs":[{"db":"PDB","id":"5MQF"}],"region_id":"DP03245r001","statement":[{"text":"The authors do not specify in the paper that the 31 - 2752 region is disordered, but the specified residues are missing in the PDB.","type":"Curator statement"},{"text":"The SRM300 protein is part of human spliceosomal C complex, composed of 34 other macromolecules.","type":"Curator statement"}],"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-11-28T17:25:40.013Z"}},{"start":27,"end":2752,"reference_id":"28502770","reference_source":"pmid","reference_html":"An Atomic Structure of the Human Spliceosome. <i> Zhang X, Yan C, Hang J, Finci LI, Lei J, Shi Y. </i> Cell, 2017","date":"2023-08-23T14:04:26.159Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":3,"cross_refs":[{"db":"PDB","id":"5XJC"}],"region_id":"DP03245r004","statement":[{"text":"PDB - unmodeled residue 27-2752","type":"Curator statement"}],"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":27,"end":2752,"reference_id":"29301961","reference_source":"pmid","reference_html":"Structure of a human catalytic step I spliceosome. <i> Zhan X, Yan C, Zhang X, Zhang X, Lei J, Shi Y. </i> Science, 2018","date":"2023-08-23T14:04:36.115Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":3,"cross_refs":[{"db":"PDB","id":"5YZG"}],"region_id":"DP03245r005","statement":[{"text":"PDB - Unmodeled residue 27-2752","type":"Curator statement"}],"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":27,"end":2752,"reference_id":"29360106","reference_source":"pmid","reference_html":"Structure of the human activated spliceosome in three conformational states. <i> Zhang X, Yan C, Zhan X, Li L, Lei J, Shi Y. </i> Cell Res, 2018","date":"2023-08-23T14:04:06.196Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":3,"cross_refs":[{"db":"PDB","id":"5Z56"}],"region_id":"DP03245r006","statement":[{"text":"PDB - unmodeled residues 27 - 2752","type":"Curator statement"}],"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":35,"end":2752,"reference_id":"29361316","reference_source":"pmid","reference_html":"Structure and Conformational Dynamics of the Human Spliceosomal Bact Complex. <i> Haselbach D, Komarov I, Agafonov DE, Hartmuth K, Graf B, Dybkov O, Urlaub H, Kastner B, Lührmann R, Stark H. </i> Cell, 2018","date":"2023-08-23T14:03:56.774Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":3,"cross_refs":[{"db":"PDB","id":"6FF4"}],"region_id":"DP03245r007","statement":[{"text":"PDB - unmodeled residues 35 - 2752","type":"Curator statement"}],"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":27,"end":2752,"reference_id":"30728453","reference_source":"pmid","reference_html":"Structures of the human spliceosomes before and after release of the ligated exon. <i> Zhang X, Zhan X, Yan C, Zhang W, Liu D, Lei J, Shi Y. </i> Cell Res, 2019","date":"2023-08-23T14:02:21.815Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":3,"cross_refs":[{"db":"PDB","id":"6ICZ"}],"region_id":"DP03245r009","statement":[{"text":"PDB - unmodeled residues 27- 2752","type":"Curator statement"}],"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":9,"released":"2023_12","sequence":"MYNGIGLPTPRGSGTNGYVQRNLSLVRGRRGERPDYKGEEELRRLEAALVKRPNPDILDHERKRRVELRCLELEEMMEEQGYEEQQIQEKVATFRLMLLEKDVNPGGKEETPGQRPAVTETHQLAELNEKKNERLRAAFGISDSYVDGSSFDPQRRAREAKQPAPEPPKPYSLVRESSSSRSPTPKQKKKKKKKDRGRRSESSSPRRERKKSSKKKKHRSESESKKRKHRSPTPKSKRKSKDKKRKRSRSTTPAPKSRRAHRSTSADSASSSDTSRSRSRSAAAKTHTTALAGRSPSPASGRRGEGDAPFSEPGTTSTQRPSSPETATKQPSSPYEDKDKDKKEKSATRPSPSPERSSTGPEPPAPTPLLAERHGGSPQPLATTPLSQEPVNPPSEASPTRDRSPPKSPEKLPQSSSSESSPPSPQPTKVSRHASSSPESPKPAPAPGSHREISSSPTSKNRSHGRAKRDKSHSHTPSRRMGRSRSPATAKRGRSRSRTPTKRGHSRSRSPQWRRSRSAQRWGRSRSPQRRGRSRSPQRPGWSRSRNTQRRGRSRSARRGRSHSRSPATRGRSRSRTPARRGRSRSRTPARRRSRSRTPTRRRSRSRTPARRGRSRSRTPARRRSRTRSPVRRRSRSRSPARRSGRSRSRTPARRGRSRSRTPARRGRSRSRTPARRSGRSRSRTPARRGRSRSRTPRRGRSRSRSLVRRGRSHSRTPQRRGRSGSSSERKNKSRTSQRRSRSNSSPEMKKSRISSRRSRSLSSPRSKAKSRLSLRRSLSGSSPCPKQKSQTPPRRSRSGSSQPKAKSRTPPRRSRSSSSPPPKQKSKTPSRQSHSSSSPHPKVKSGTPPRQGSITSPQANEQSVTPQRRSCFESSPDPELKSRTPSRHSCSGSSPPRVKSSTPPRQSPSRSSSPQPKVKAIISPRQRSHSGSSSPSPSRVTSRTTPRRSRSVSPCSNVESRLLPRYSHSGSSSPDTKVKPETPPRQSHSGSISPYPKVKAQTPPGPSLSGSKSPCPQEKSKDSLVQSCPGSLSLCAGVKSSTPPGESYFGVSSLQLKGQSQTSPDHRSDTSSPEVRQSHSESPSLQSKSQTSPKGGRSRSSSPVTELASRSPIRQDRGEFSASPMLKSGMSPEQSRFQSDSSSYPTVDSNSLLGQSRLETAESKEKMALPPQEDATASPPRQKDKFSPFPVQDRPESSLVFKDTLRTPPRERSGAGSSPETKEQNSALPTSSQDEELMEVVEKSEEPAGQILSHLSSELKEMSTSNFESSPEVEERPAVSLTLDQSQSQASLEAVEVPSMASSWGGPHFSPEHKELSNSPLRENSFGSPLEFRNSGPLGTEMNTGFSSEVKEDLNGPFLNQLETDPSLDMKEQSTRSSGHSSSELSPDAVEKAGMSSNQSISSPVLDAVPRTPSRERSSSASSPEMKDGLPRTPSRRSRSGSSPGLRDGSGTPSRHSLSGSSPGMKDIPRTPSRGRSECDSSPEPKALPQTPRPRSRSPSSPELNNKCLTPQRERSGSESSVDQKTVARTPLGQRSRSGSSQELDVKPSASPQERSESDSSPDSKAKTRTPLRQRSRSGSSPEVDSKSRLSPRRSRSGSSPEVKDKPRAAPRAQSGSDSSPEPKAPAPRALPRRSRSGSSSKGRGPSPEGSSSTESSPEHPPKSRTARRGSRSSPEPKTKSRTPPRRRSSRSSPELTRKARLSRRSRSASSSPETRSRTPPRHRRSPSVSSPEPAEKSRSSRRRRSASSPRTKTTSRRGRSPSPKPRGLQRSRSRSRREKTRTTRRRDRSGSSQSTSRRRQRSRSRSRVTRRRRGGSGYHSRSPARQESSRTSSRRRRGRSRTPPTSRKRSRSRTSPAPWKRSRSRASPATHRRSRSRTPLISRRRSRSRTSPVSRRRSRSRTSVTRRRSRSRASPVSRRRSRSRTPPVTRRRSRSRTPTTRRRSRSRTPPVTRRRSRSRTPPVTRRRSRSRTSPITRRRSRSRTSPVTRRRSRSRTSPVTRRRSRSRTSPVTRRRSRSRTPPAIRRRSRSRTPLLPRKRSRSRSPLAIRRRSRSRTPRTARGKRSLTRSPPAIRRRSASGSSSDRSRSATPPATRNHSGSRTPPVALNSSRMSCFSRPSMSPTPLDRCRSPGMLEPLGSSRTPMSVLQQAGGSMMDGPGPRIPDHQRTSVPENHAQSRIALALTAISLGTARPPPSMSAAGLAARMSQVPAPVPLMSLRTAPAANLASRIPAASAAAMNLASARTPAIPTAVNLADSRTPAAAAAMNLASPRTAVAPSAVNLADPRTPTAPAVNLAGARTPAALAALSLTGSGTPPTAANYPSSSRTPQAPASANLVGPRSAHATAPVNIAGSRTAAALAPASLTSARMAPALSGANLTSPRVPLSAYERVSGRTSPPLLDRARSRTPPSAPSQSRMTSERAPSPSSRMGQAPSQSLLPPAQDQPRSPVPSAFSDQSRCLIAQTTPVAGSQSLSSGAVATTTSSAGDHNGMLSVPAPGVPHSDVGEPPASTGAQQPSALAALQPAKERRSSSSSSSSSSSSSSSSSSSSSSSSSGSSSSDSEGSSLPVQPEVALKRVPSPTPAPKEAVREGRPPEPTPAKRKRRSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSPSPAKPGPQALPKPASPKKPPPGERRSRSPRKPIDSLRDSRSLSYSPVERRRPSPQPSPRDQQSSSSERGSRRGQRGDSRSPSHKRRRETPSPRPMRHRSSRSP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Condensates-related proteins"],"UniParc":"UPI000006E353","uniref100":"UniRef100_Q9UQ35","uniref90":"UniRef90_Q9UQ35","uniref50":"UniRef50_Q9UQ35","genes":[{"name":{"value":"SRRM2"},"synonyms":[{"value":"KIAA0324"},{"value":"SRL300"},{"value":"SRM300"}],"orfNames":[{"value":"HSPC075"}]}],"disorder_content":0.9905523255813954,"disprot_consensus":{"full":[{"start":27,"end":2752,"type":"D"}],"Structural state":[{"start":27,"end":2752,"type":"D"}]}},{"disprot_id":"DP03246","acc":"O75475","creator":"cbassot","date":"2021-04-20T09:13:56.361Z","features":{"pfam":[{"id":"PF00855","name":"PWWP domain","start":8,"end":87},{"id":"PF11467","name":"Lens epithelium-derived growth factor (LEDGF)","start":349,"end":449}],"gene3D":[]},"length":530,"name":"PC4 and SFRS1-interacting protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":430,"end":471,"reference_id":"15895093","reference_source":"pmid","reference_html":"Solution structure of the HIV-1 integrase-binding domain in LEDGF/p75. <i> Cherepanov P, Sun ZY, Rahman S, Maertens G, Wagner G, Engelman A. </i> Nat Struct Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"cbassot","curator_name":"Claudio Bassot","curator_orcid":"0000-0001-7161-9028","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006196","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1Z9E"}],"region_id":"DP03246r001","statement":[{"text":"Scarcity of NOEs observed for residues C-terminal to Gly430, poor chemical shift dispersion on the 2D 1H-15N HSQC spectrum, and fast hydrogen-deuterium exchange of the main chain amide protons collectively suggested that residues 430–471 were not involved in a stable fold","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-09T15:11:00.161Z"}},{"start":92,"end":135,"reference_id":"25277115","reference_source":"pmid","reference_html":"Structure and function of the nucleosome-binding PWWP domain. <i> Qin S, Min J. </i> Trends Biochem Sci, 2014","date":"2023-08-09T15:16:07.594Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4FU6"}],"region_id":"DP03246r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"}],"statement":[{"text":"The PDB structure shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"regions_counter":2,"released":"2021_12","sequence":"MTRDFKPGDLIFAKMKGYPHWPARVDEVPDGAVKPPTNKLPIFFFGTHETAFLGPKDIFPYSENKEKYGKPNKRKGFNEGLWEIDNNPKVKFSSQQAATKQSNASSDVEVEEKETSVSKEDTDHEEKASNEDVTKAVDITTPKAARRGRKRKAEKQVETEEAGVVTTATASVNLKVSPKRGRPAATEVKIPKPRGRPKMVKQPCPSESDIITEEDKSKKKGQEEKQPKKQPKKDEEGQKEEDKPRKEPDKKEGKKEVESKRKNLAKTGVTSTSDSEEEGDDQEGEKKRKGGRNFQTAHRRNMLKGQHEKEAADRKRKQEEQMETEQQNKDEGKKPEVKKVEKKRETSMDSRLQRIHAEIKNSLKIDNLDVNRCIEALDELASLQVTMQQAQKHTEMITTLKKIRRFKVSQVIMEKSTMLYNKFKNMFLVGEGDSVITQVLNKSLAEQRQHEEANKTKDQGKKGPNKKLEKEQTGSKTLNGGSDAQDGNQPQHNGESNEDSKDNHEASTKKKPSSEERETEISLKDSTLDN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins"],"UniParc":"UPI0000073FC4","uniref100":"UniRef100_O75475","uniref90":"UniRef90_O75475","uniref50":"UniRef50_O75475","genes":[{"name":{"value":"PSIP1"},"synonyms":[{"value":"DFS70"},{"value":"LEDGF"},{"value":"PSIP2"}]}],"alphafold_very_low_content":0.46226415094339623,"disorder_content":0.16226415094339622,"disprot_consensus":{"full":[{"start":92,"end":135,"type":"D"},{"start":430,"end":471,"type":"D"}],"Structural state":[{"start":92,"end":135,"type":"D"},{"start":430,"end":471,"type":"D"}]}},{"disprot_id":"DP03248","acc":"Q9NYV4","creator":"cbassot","date":"2021-04-21T10:42:14.809Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":729,"end":1020}],"gene3D":[]},"length":1490,"name":"Cyclin-dependent kinase 12","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1023,"end":1063,"reference_id":"30067358","reference_source":"pmid","reference_html":"Discovery of 3-Benzyl-1-( trans-4-((5-cyanopyridin-2-yl)amino)cyclohexyl)-1-arylurea Derivatives as Novel and Selective Cyclin-Dependent Kinase 12 (CDK12) Inhibitors. <i> Ito M, Tanaka T, Toita A, Uchiyama N, Kokubo H, Morishita N, Klein MG, Zou H, Murakami M, Kondo M, Sameshima T, Araki S, Endo S, Kawamoto T, Morin GB, Aparicio SA, Nakanishi A, Maezaki H, Imaeda Y. </i> J Med Chem, 2018","date":"2022-08-03T14:38:17.001Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":3,"cross_refs":[{"db":"PDB","id":"6CKX"}],"region_id":"DP03248r001","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75909"}]}],"regions_counter":1,"released":"2023_12","sequence":"MPNSERHGGKKDGSGGASGTLQPSSGGGSSNSRERHRLVSKHKRHKSKHSKDMGLVTPEAASLGTVIKPLVEYDDISSDSDTFSDDMAFKLDRRENDERRGSDRSDRLHKHRHHQHRRSRDLLKAKQTEKEKSQEVSSKSGSMKDRISGSSKRSNEETDDYGKAQVAKSSSKESRSSKLHKEKTRKERELKSGHKDRSKSHRKRETPKSYKTVDSPKRRSRSPHRKWSDSSKQDDSPSGASYGQDYDLSPSRSHTSSNYDSYKKSPGSTSRRQSVSPPYKEPSAYQSSTRSPSPYSRRQRSVSPYSRRRSSSYERSGSYSGRSPSPYGRRRSSSPFLSKRSLSRSPLPSRKSMKSRSRSPAYSRHSSSHSKKKRSSSRSRHSSISPVRLPLNSSLGAELSRKKKERAAAAAAAKMDGKESKGSPVFLPRKENSSVEAKDSGLESKKLPRSVKLEKSAPDTELVNVTHLNTEVKNSSDTGKVKLDENSEKHLVKDLKAQGTRDSKPIALKEEIVTPKETETSEKETPPPLPTIASPPPPLPTTTPPPQTPPLPPLPPIPALPQQPPLPPSQPAFSQVPASSTSTLPPSTHSKTSAVSSQANSQPPVQVSVKTQVSVTAAIPHLKTSTLPPLPLPPLLPGDDDMDSPKETLPSKPVKKEKEQRTRHLLTDLPLPPELPGGDLSPPDSPEPKAITPPQQPYKKRPKICCPRYGERRQTESDWGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLIHRSVVNMKEIVTDKQDALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLEYCHKKNFLHRDIKCSNILLNNSGQIKLADFGLARLYNSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIKLPYFNTMKPKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKDVELSKMAPPDLPHWQDCHELWSKKRRRQRQSGVVVEEPPPSKTSRKETTSGTSTEPVKNSSPAPPQPAPGKVESGAGDAIGLADITQQLNQSELAVLLNLLQSQTDLSIPQMAQLLNIHSNPEMQQQLEALNQSISALTEATSQQQDSETMAPEESLKEAPSAPVILPSAEQTTLEASSTPADMQNILAVLLSQLMKTQEPAGSLEENNSDKNSGPQGPRRTPTMPQEEAAACPPHILPPEKRPPEPPGPPPPPPPPPLVEGDLSSAPQELNPAVTAALLQLLSQPEAEPPGHLPHEHQALRPMEYSTRPRPNRTYGNTDGPETGFSAIDTDERNSGPALTESLVQTLVKNRTFSGSLSHLGESSSYQGTGSVQFPGDQDLRFARVPLALHPVVGQPFLKAEGSSNSVVHAETKLQNYGELGPGTTGASSSGAGLHWGGPTQSSAYGKLYRGPTRVPPRGGRGRGVPY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins"],"UniParc":"UPI0000035B71","uniref100":"UniRef100_Q9NYV4","uniref90":"UniRef90_Q9NYV4","uniref50":"UniRef50_Q9NYV4","genes":[{"name":{"value":"CDK12"},"synonyms":[{"value":"CRK7"},{"value":"CRKRS"},{"value":"KIAA0904"}]}],"alphafold_very_low_content":0.6859060402684564,"disorder_content":0.027516778523489934,"disprot_consensus":{"full":[{"start":1023,"end":1063,"type":"D"}],"Structural state":[{"start":1023,"end":1063,"type":"D"}]}},{"disprot_id":"DP03249","acc":"Q96RJ3","creator":"cbassot","date":"2021-04-21T11:03:16.391Z","features":{"pfam":[{"id":"PF09256","name":"BAFF-R, TALL-1 binding","start":16,"end":45}],"gene3D":[]},"length":184,"name":"Tumor necrosis factor receptor superfamily member 13C","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":19,"reference_id":"12755599","reference_source":"pmid","reference_html":"BAFF/BLyS receptor 3 comprises a minimal TNF receptor-like module that encodes a highly focused ligand-binding site. <i> Gordon NC, Pan B, Hymowitz SG, Yin J, Kelley RF, Cochran AG, Yan M, Dixit VM, Fairbrother WJ, Starovasnik MA. </i> Biochemistry, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"cbassot","curator_name":"Claudio Bassot","curator_orcid":"0000-0001-7161-9028","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1OSX"}],"region_id":"DP03249r001","statement":[{"text":"Nineteen residues, including Cys19 through Leu37, define the structured core of the BR3 ECD, while the rest of the N- and C-terminal residues are highly flexible (Figure 1)","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":37,"end":184,"reference_id":"12755599","reference_source":"pmid","reference_html":"BAFF/BLyS receptor 3 comprises a minimal TNF receptor-like module that encodes a highly focused ligand-binding site. <i> Gordon NC, Pan B, Hymowitz SG, Yin J, Kelley RF, Cochran AG, Yan M, Dixit VM, Fairbrother WJ, Starovasnik MA. </i> Biochemistry, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"cbassot","curator_name":"Claudio Bassot","curator_orcid":"0000-0001-7161-9028","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1OSX"}],"region_id":"DP03249r002","statement":[{"text":"Nineteen residues, including Cys19 through Leu37, define the structured core of the BR3 ECD, while the rest of the N- and C-terminal residues are highly flexible (Figure 1)","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MRRGPRSLRGRDAPAPTPCVPAECFDLLVRHCVACGLLRTPRPKPAGASSPAPRTALQPQESVGAGAGEAALPLPGLLFGAPALLGLALVLALVLVGLVSWRRRQRRLRGASSAEAPDGDKDAPEPLDKVIILSPGISDATAPAWPPPGEDPGTTPPGHSVPVPATELGSTELVTTKTAGPEQQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI0000049F80","uniref100":"UniRef100_Q96RJ3","uniref90":"UniRef90_Q96RJ3","uniref50":"UniRef50_Q96RJ3","genes":[{"name":{"value":"TNFRSF13C"},"synonyms":[{"value":"BAFFR"},{"value":"BR3"}]}],"alphafold_very_low_content":0.27717391304347827,"disorder_content":0.907608695652174,"disprot_consensus":{"full":[{"start":1,"end":19,"type":"D"},{"start":37,"end":184,"type":"D"}],"Structural state":[{"start":1,"end":19,"type":"D"},{"start":37,"end":184,"type":"D"}]}},{"disprot_id":"DP03250","acc":"Q9UBW5","creator":"cbassot","date":"2021-04-21T11:25:24.387Z","features":{"pfam":[{"id":"PF03114","name":"BAR domain","start":18,"end":236},{"id":"PF21532","name":"Bridging integrator 2, C-terminal tail","start":239,"end":505}],"gene3D":[]},"length":565,"name":"Bridging integrator 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":37,"reference_id":"23285027","reference_source":"pmid","reference_html":"Bin2 is a membrane sculpting N-BAR protein that influences leucocyte podosomes, motility and phagocytosis. <i> Sánchez-Barrena MJ, Vallis Y, Clatworthy MR, Doherty GJ, Veprintsev DB, Evans PR, McMahon HT. </i> PLoS One, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"cbassot","curator_name":"Claudio Bassot","curator_orcid":"0000-0001-7161-9028","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4I1Q"}],"region_id":"DP03250r001","statement":[{"text":"The final model included residues 37 to 238, that is, the N-terminal amphipathic helix was disordered in both subunits","type":"Methods"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MAEGKAGGAAGLFAKQVQKKFSRAQEKVLQKLGKAVETKDERFEQSASNFYQQQAEGHKLYKDLKNFLSAVKVMHESSKRVSETLQEIYSSEWDGHEELKAIVWNNDLLWEDYEEKLADQAVRTMEIYVAQFSEIKERIAKRGRKLVDYDSARHHLEAVQNAKKKDEAKTAKAEEEFNKAQTVFEDLNQELLEELPILYNSRIGCYVTIFQNISNLRDVFYREMSKLNHNLYEVMSKLEKQHSNKVFVVKGLSSSSRRSLVISPPVRTATVSSPLTSPTSPSTLSLKSESESVSATEDLAPDAAQGEDNSEIKELLEEEEIEKEGSEASSSEEDEPLPACNGPAQAQPSPTTERAKSQEEVLPSSTTPSPGGALSPSGQPSSSATEVVLRTRTASEGSEQPKKRASIQRTSAPPSRPPPPRATASPRPSSGNIPSSPTASGGGSPTSPRASLGTGTASPRTSLEVSPNPEPPEKPVRTPEAKENENIHNQNPEELCTSPTLMTSQVASEPGEAKKMEDKEKDNKLISANSSEGQDQLQVSMVPENNNLTAPEPQEEVSTSENPQL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000006FE75","uniref100":"UniRef100_Q9UBW5","uniref90":"UniRef90_Q9UBW5","uniref50":"UniRef50_Q9UBW5","genes":[{"name":{"value":"BIN2"},"synonyms":[{"value":"BRAP1"}]}],"alphafold_very_low_content":0.49380530973451325,"disorder_content":0.06548672566371681,"disprot_consensus":{"full":[{"start":1,"end":37,"type":"D"}],"Structural state":[{"start":1,"end":37,"type":"D"}]}},{"disprot_id":"DP03251","acc":"Q8N300","creator":"cbassot","date":"2021-04-21T12:44:37.736Z","features":{"pfam":[{"id":"PF15674","name":"Coiled-coil domain-containing protein 23","start":4,"end":64}],"gene3D":[]},"length":66,"name":"Small vasohibin-binding protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":23,"reference_id":"31235911","reference_source":"pmid","reference_html":"Structural basis of tubulin detyrosination by the vasohibin-SVBP enzyme complex. <i> Wang N, Bosc C, Ryul Choi S, Boulan B, Peris L, Olieric N, Bao H, Krichen F, Chen L, Andrieux A, Olieric V, Moutin MJ, Steinmetz MO, Huang H. </i> Nat Struct Mol Biol, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"cbassot","curator_name":"Claudio Bassot","curator_orcid":"0000-0001-7161-9028","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6J4S"},{"db":"PDB","id":"6QBY"},{"db":"PDB","id":"6J4O"},{"db":"PDB","id":"6J4P"},{"db":"PDB","id":"6J4U"}],"region_id":"DP03251r004","statement":[{"text":" Superimposition of the structures of V2c–SVBP (colored as in Fig. 1a) and V2–SVBP (colored in wheat) in cartoon representation. The rmsd of the two superimposed structures is 0.29 Å. The comparison reveals that the structures of V2c and full-length V2 are almost the same, and that the N- and C-terminal flanking regions of V2 are disordered. ","type":"Supplementary material"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T16:19:27.305Z"}}],"regions_counter":5,"released":"2021_12","sequence":"MDPPARKEKTKVKESVSRVEKAKQKSAQQELKQRQRAEIYALNRVMTELEQQQFDEFCKQMQPPGE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"UniParc":"UPI000006CFBA","uniref100":"UniRef100_Q8N300","uniref90":"UniRef90_Q8N300","uniref50":"UniRef50_Q8N300","genes":[{"name":{"value":"SVBP","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"20736312","url":"http://www.ncbi.nlm.nih.gov/pubmed/20736312","alternativeUrl":"https://europepmc.org/abstract/MED/20736312"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:29204","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:29204"}}]},"synonyms":[{"value":"CCDC23","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:29204","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:29204"}}]}]}],"alphafold_very_low_content":0.030303030303030304,"disorder_content":0.3484848484848485,"disprot_consensus":{"full":[{"start":1,"end":23,"type":"D"}],"Structural state":[{"start":1,"end":23,"type":"D"}]}},{"disprot_id":"DP03253","acc":"P08799","creator":"smribeiro","date":"2021-04-22T11:19:44.358Z","features":{"pfam":[{"id":"PF00063","name":"Myosin head (motor domain)","start":88,"end":747},{"id":"PF01576","name":"Myosin tail","start":1403,"end":2082},{"id":"PF02736","name":"Myosin N-terminal SH3-like domain","start":29,"end":81}],"gene3D":[]},"length":2116,"name":"Myosin-2 heavy chain","ncbi_taxon_id":44689,"organism":"Dictyostelium discoideum","regions":[{"start":703,"end":735,"reference_id":"15750603","reference_source":"pmid","reference_html":"The structural basis of blebbistatin inhibition and specificity for myosin II. <i> Allingham JS, Smith R, Rayment I. </i> Nat Struct Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1YV3"}],"region_id":"DP03253r001","statement":[{"text":"PDB - unmodeled residue 703 -735","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":748,"end":762,"reference_id":"15750603","reference_source":"pmid","reference_html":"The structural basis of blebbistatin inhibition and specificity for myosin II. <i> Allingham JS, Smith R, Rayment I. </i> Nat Struct Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1YV3"}],"region_id":"DP03253r002","statement":[{"text":"PDB - unmodeled residue 748 -762","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":701,"end":732,"reference_id":"20459085","reference_source":"pmid","reference_html":"Insights into the importance of hydrogen bonding in the gamma-phosphate binding pocket of myosin: structural and functional studies of serine 236. <i> Frye JJ, Klenchin VA, Bagshaw CR, Rayment I. </i> Biochemistry, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3MYH"}],"region_id":"DP03253r003","statement":[{"text":"PDB - unmodeled residue 701-732","type":"Curator statement"},{"text":"S236A mutant","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":748,"end":762,"reference_id":"20459085","reference_source":"pmid","reference_html":"Insights into the importance of hydrogen bonding in the gamma-phosphate binding pocket of myosin: structural and functional studies of serine 236. <i> Frye JJ, Klenchin VA, Bagshaw CR, Rayment I. </i> Biochemistry, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3MYH"}],"region_id":"DP03253r004","statement":[{"text":"PDB - unmodeled residue 748-762","type":"Curator statement"},{"text":"S236A mutant","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":701,"end":732,"reference_id":"20459085","reference_source":"pmid","reference_html":"Insights into the importance of hydrogen bonding in the gamma-phosphate binding pocket of myosin: structural and functional studies of serine 236. <i> Frye JJ, Klenchin VA, Bagshaw CR, Rayment I. </i> Biochemistry, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3MYL"}],"region_id":"DP03253r005","statement":[{"text":"PDB - residues 701-732 ordered by crystal contact in space group P21212","type":"Curator statement"},{"text":"S236A mutant","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":748,"end":759,"reference_id":"20459085","reference_source":"pmid","reference_html":"Insights into the importance of hydrogen bonding in the gamma-phosphate binding pocket of myosin: structural and functional studies of serine 236. <i> Frye JJ, Klenchin VA, Bagshaw CR, Rayment I. </i> Biochemistry, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3MYL"}],"region_id":"DP03253r006","statement":[{"text":"PDB - residues 748-759 ordered by crystal contact in space group P21212","type":"Curator statement"},{"text":"S236A mutant","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":698,"end":735,"reference_id":"20459085","reference_source":"pmid","reference_html":"Insights into the importance of hydrogen bonding in the gamma-phosphate binding pocket of myosin: structural and functional studies of serine 236. <i> Frye JJ, Klenchin VA, Bagshaw CR, Rayment I. </i> Biochemistry, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3MYK"}],"region_id":"DP03253r007","statement":[{"text":"PDB - unmodeled residues 698-735 ","type":"Curator statement"},{"text":"S236A mutant","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":750,"end":762,"reference_id":"20459085","reference_source":"pmid","reference_html":"Insights into the importance of hydrogen bonding in the gamma-phosphate binding pocket of myosin: structural and functional studies of serine 236. <i> Frye JJ, Klenchin VA, Bagshaw CR, Rayment I. </i> Biochemistry, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3MYK"}],"region_id":"DP03253r008","statement":[{"text":"PDB - unmodeled residues 750-762","type":"Curator statement"},{"text":"S236A mutant","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":702,"end":721,"reference_id":"25936506","reference_source":"pmid","reference_html":"How actin initiates the motor activity of Myosin. <i> Llinas P, Isabet T, Song L, Ropars V, Zong B, Benisty H, Sirigu S, Morris C, Kikuti C, Safer D, Sweeney HL, Houdusse A. </i> Dev Cell, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4PJK"}],"region_id":"DP03253r009","statement":[{"text":"PDB - unmodeled residues 702-721","type":"Curator statement"},{"text":"R238E.E459R mutant","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":748,"end":761,"reference_id":"25936506","reference_source":"pmid","reference_html":"How actin initiates the motor activity of Myosin. <i> Llinas P, Isabet T, Song L, Ropars V, Zong B, Benisty H, Sirigu S, Morris C, Kikuti C, Safer D, Sweeney HL, Houdusse A. </i> Dev Cell, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4PJK"}],"region_id":"DP03253r010","statement":[{"text":"PDB - unmodeled residues 748-761","type":"Curator statement"},{"text":"R238E.E459R mutant","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":487,"end":508,"reference_id":"7619795","reference_source":"pmid","reference_html":"X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-. <i> Fisher AJ, Smith CA, Thoden JB, Smith R, Sutoh K, Holden HM, Rayment I. </i> Biochemistry, 1995","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1MND"}],"region_id":"DP03253r011","statement":[{"text":"There are breaks in the polypeptide chain  between  Gln  19 and  Leu  27,  Ala  205  and  Gly  209, Phe 487 and Leu 508, Arg 620 and Asn 626, and Glu  681 and Gly 683, where the density is poorly defined.","type":"Methods"},{"text":"PDB - unmodeled residues 487 - 508","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":691,"end":762,"reference_id":"7619795","reference_source":"pmid","reference_html":"X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-. <i> Fisher AJ, Smith CA, Thoden JB, Smith R, Sutoh K, Holden HM, Rayment I. </i> Biochemistry, 1995","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1MND"}],"region_id":"DP03253r012","statement":[{"text":"There are breaks in the polypeptide chain  between  Gln  19 and  Leu  27,  Ala  205  and  Gly  209, Phe 487 and Leu 508, Arg 620 and Asn 626, and Glu  681 and Gly 683, where the density is poorly defined.","type":"Methods"},{"text":"PDB - unmodeled residues 691 - 762","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":487,"end":500,"reference_id":"7619795","reference_source":"pmid","reference_html":"X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-. <i> Fisher AJ, Smith CA, Thoden JB, Smith R, Sutoh K, Holden HM, Rayment I. </i> Biochemistry, 1995","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1MMD"}],"region_id":"DP03253r013","statement":[{"text":" After  refinement  the final model included 743 residues","type":"Methods"},{"text":"PDB - residues 487-500 ordered","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":691,"end":759,"reference_id":"7619795","reference_source":"pmid","reference_html":"X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-. <i> Fisher AJ, Smith CA, Thoden JB, Smith R, Sutoh K, Holden HM, Rayment I. </i> Biochemistry, 1995","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1MMD"}],"region_id":"DP03253r014","statement":[{"text":" After  refinement  the final model included 743 residues","type":"Methods"},{"text":"PDB - residues 691-759 ordered","type":"Curator statement"},{"text":"Movement of the  lower domain  relative to the  upper domain of the central  segment of the heavy chain in the MgADPAIF4S1Dc complex is coupled to a structural change in the COOH-terminal domains.","type":"Results"},{"text":"The structures of the beryllium and aluminum fluoride complexes suggest that movements in the myosin heavy chain associated with the lower domain of the central 50 kDa segment coupled to movements  in  the  COOH-terminal  segment are the primary source of this conformational change. ","type":"Discussion"}],"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":702,"end":719,"reference_id":"9305951","reference_source":"pmid","reference_html":"X-ray structures of the MgADP, MgATPgammaS, and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain. <i> Gulick AM, Bauer CB, Thoden JB, Rayment I. </i> Biochemistry, 1997","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1MMA"}],"region_id":"DP03253r015","statement":[{"text":"PDB - unmodeled residues 702-719","type":"Curator statement"},{"text":"It has been observed that when the c-axis shrinks below 180 Å disorder is induced into the NH2- and COOH-terminal regions of the protein.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":748,"end":762,"reference_id":"8611530","reference_source":"pmid","reference_html":"X-ray structure of the magnesium(II).ADP.vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 A resolution. <i> Smith CA, Rayment I. </i> Biochemistry, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1VOM"}],"region_id":"DP03253r016","statement":[{"text":"PDB - unmodeled residues 748-752","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":16,"released":"2021_12","sequence":"MNPIHDRTSDYHKYLKVKQGDSDLFKLTVSDKRYIWYNPDPKERDSYECGEIVSETSDSFTFKTVDGQDRQVKKDDANQRNPIKFDGVEDMSELSYLNEPAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGESGAGKTENTKKVIQYLASVAGRNQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSDSEEFKITRQAMDIVGFSQEEQMSIFKIIAGILHLGNIKFEKGAGEGAVLKDKTALNAASTVFGVNPSVLEKALMEPRILAGRDLVAQHLNVEKSSSSRDALVKALYGRLFLWLVKKINNVLCQERKAYFIGVLDISGFEIFKVNSFEQLCINYTNEKLQQFFNHHMFKLEQEEYLKEKINWTFIDFGLDSQATIDLIDGRQPPGILALLDEQSVFPNATDNTLITKLHSHFSKKNAKYEEPRFSKTEFGVTHYAGQVMYEIQDWLEKNKDPLQQDLELCFKDSSDNVVTKLFNDPNIASRAKKGANFITVAAQYKEQLASLMATLETTNPHFVRCIIPNNKQLPAKLEDKVVLDQLRCNGVLEGIRITRKGFPNRIIYADFVKRYYLLAPNVPRDAEDSQKATDAVLKHLNIDPEQYRFGITKIFFRAGQLARIEEAREQRISEIIKAIQAATRGWIARKVYKQAREHTVAARIIQQNLRAYIDFKSWPWWKLFSKARPLLKRRNFEKEIKEKEREILELKSNLTDSTTQKDKLEKSLKDTESNVLDLQRQLKAEKETLKAMYDSKDALEAQKRELEIRVEDMESELDEKKLALENLQNQKRSVEEKVRDLEEELQEEQKLRNTLEKLKKKYEEELEEMKRVNDGQSDTISRLEKIKDELQKEVEELTESFSEESKDKGVLEKTRVRLQSELDDLTVRLDSETKDKSELLRQKKKLEEELKQVQEALAAETAAKLAQEAANKKLQGEYTELNEKFNSEVTARSNVEKSKKTLESQLVAVNNELDEEKKNRDALEKKKKALDAMLEEMKDQLESTGGEKKSLYDLKVKQESDMEALRNQISELQSTIAKLEKIKSTLEGEVARLQGELEAEQLAKSNVEKQKKKVELDLEDKSAQLAEETAAKQALDKLKKKLEQELSEVQTQLSEANNKNVNSDSTNKHLETSFNNLKLELEAEQKAKQALEKKRLGLESELKHVNEQLEEEKKQKESNEKRKVDLEKEVSELKDQIEEEVASKKAVTEAKNKKESELDEIKRQYADVVSSRDKSVEQLKTLQAKNEELRNTAEEAEGQLDRAERSKKKAEFDLEEAVKNLEEETAKKVKAEKAMKKAETDYRSTKSELDDAKNVSSEQYVQIKRLNEELSELRSVLEEADERCNSAIKAKKTAESALESLKDEIDAANNAKAKAERKSKELEVRVAELEESLEDKSGTVNVEFIRKKDAEIDDLRARLDRETESRIKSDEDKKNTRKQFADLEAKVEEAQREVVTIDRLKKKLESDIIDLSTQLDTETKSRIKIEKSKKKLEQTLAERRAAEEGSSKAADEEIRKQVWQEVDELRAQLDSERAALNASEKKIKSLVAEVDEVKEQLEDEILAKDKLVKAKRALEVELEEVRDQLEEEEDSRSELEDSKRRLTTEVEDIKKKYDAEVEQNTKLDEAKKKLTDDVDTLKKQLEDEKKKLNESERAKKRLESENEDFLAKLDAEVKNRSRAEKDRKKYEKDLKDTKYKLNDEAATKTQTEIGAAKLEDQIDELRSKLEQEQAKATQADKSKKTLEGEIDNLRAQIEDEGKIKMRLEKEKRALEGELEELRETVEEAEDSKSEAEQSKRLVELELEDARRNLQKEIDAKEIAEDAKSNLQREIVEAKGRLEEESIARTNSDRSRKRLEAEIDALTAQVDAEQKAKNQQIKENKKIETELKEYRKKFGESEKTKTKEFLVVEKLETDYKRAKKEAADEQQQRLTVENDLRKHLSEISLLKDAIDKLQRDHDKTKRELETETASKIEMQRKMADFFGGFKA","taxonomy":["Eukaryota","Amoebozoa","Evosea","Eumycetozoa","Dictyostelia","Dictyosteliales","Dictyosteliaceae","Dictyostelium"],"dataset":[],"UniParc":"UPI000012FBD3","uniref100":"UniRef100_P08799","uniref90":"UniRef90_P08799","uniref50":"UniRef50_P08799","genes":[{"name":{"value":"mhcA"},"orfNames":[{"value":"DDB_G0286355"}]}],"alphafold_very_low_content":0.0671077504725898,"disorder_content":0.0444234404536862,"disprot_consensus":{"full":[{"start":487,"end":508,"type":"D"},{"start":691,"end":759,"type":"T"},{"start":760,"end":762,"type":"D"}],"Structural state":[{"start":487,"end":508,"type":"D"},{"start":691,"end":762,"type":"D"}],"Structural transition":[{"start":691,"end":759,"type":"T"}]}},{"disprot_id":"DP03254","acc":"P52848","creator":"fquaglia","date":"2021-04-26T10:38:11.328Z","features":{"pfam":[{"id":"PF00685","name":"Sulfotransferase domain","start":605,"end":858},{"id":"PF12062","name":"Heparan sulfate-N-deacetylase, deacetylase domain","start":311,"end":515},{"id":"PF25119","name":"Heparan sulfate-N-deacetylase, N-terminal domain","start":81,"end":301}],"gene3D":[]},"length":882,"name":"Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":558,"end":578,"reference_id":"10196134","reference_source":"pmid","reference_html":"Crystal structure of the sulfotransferase domain of human heparan sulfate N-deacetylase/ N-sulfotransferase 1. <i> Kakuta Y, Sueyoshi T, Negishi M, Pedersen LC. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1NST"}],"region_id":"DP03254r001","statement":[{"text":"Interdomain region not visible in the crystal structure.","type":"Curator statement"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-21T15:34:48.965Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":587,"end":600,"reference_id":"10196134","reference_source":"pmid","reference_html":"Crystal structure of the sulfotransferase domain of human heparan sulfate N-deacetylase/ N-sulfotransferase 1. <i> Kakuta Y, Sueyoshi T, Negishi M, Pedersen LC. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1NST"}],"region_id":"DP03254r002","statement":[{"text":"The N-terminal 18 residues (587–600) and 4 residues from 665 to 669 are disordered in the NST1 crystal.","type":"Figure"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-04-30T13:03:56.543Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_06","sequence":"MPALACLRRLCRHVSPQAVLFLLFIFCLFSVFISAYYLYGWKRGLEPSADAPEPDCGDPPPVAPSRLLPLKPVQAATPSRTDPLVLVFVESLYSQLGQEVVAILESSRFKYRTEIAPGKGDMPTLTDKGRGRFALIIYENILKYVNLDAWNRELLDKYCVAYGVGIIGFFKANENSLLSAQLKGFPLFLHSNLGLKDCSINPKSPLLYVTRPSEVEKGVLPGEDWTVFQSNHSTYEPVLLAKTRSSESIPHLGADAGLHAALHATVVQDLGLHDGIQRVLFGNNLNFWLHKLVFVDAVAFLTGKRLSLPLDRYILVDIDDIFVGKEGTRMKVEDVKALFDTQNELRAHIPNFTFNLGYSGKFFHTGTNAEDAGDDLLLSYVKEFWWFPHMWSHMQPHLFHNQSVLAEQMALNKKFAVEHGIPTDMGYAVAPHHSGVYPVHVQLYEAWKQVWSIRVTSTEEYPHLKPARYRRGFIHNGIMVLPRQTCGLFTHTIFYNEYPGGSSELDKIINGGELFLTVLLNPISIFMTHLSNYGNDRLGLYTFKHLVRFLHSWTNLRLQTLPPVQLAQKYFQIFSEEKDPLWQDPCEDKRHKDIWSKEKTCDRFPKLLIIGPQKTGTTALYLFLGMHPDLSSNYPSSETFEEIQFFNGHNYHKGIDWYMEFFPIPSNTTSDFYFEKSANYFDSEVAPRRAAALLPKAKVLTILINPADRAYSWYQHQRAHDDPVALKYTFHEVITAGSDASSKLRALQNRCLVPGWYATHIERWLSAYHANQILVLDGKLLRTEPAKVMDMVQKFLGVTNTIDYHKTLAFDPKKGFWCQLLEGGKTKCLGKSKGRKYPEMDLDSRAFLKDYYRDHNIELSKLLYKMGQTLPTWLREDLQNTR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins","NDDs-related proteins"],"UniParc":"UPI000012CDA5","uniref100":"UniRef100_P52848","uniref90":"UniRef90_P52848","uniref50":"UniRef50_Q3UHN9","genes":[{"name":{"value":"NDST1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:7680","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:7680"}}]},"synonyms":[{"value":"HSST"},{"value":"HSST1"}]}],"alphafold_very_low_content":0.06575963718820861,"disorder_content":0.03968253968253968,"disprot_consensus":{"full":[{"start":558,"end":578,"type":"D"},{"start":587,"end":600,"type":"D"}],"Structural state":[{"start":558,"end":578,"type":"D"},{"start":587,"end":600,"type":"D"}]}},{"disprot_id":"DP03255","acc":"P16035","creator":"fquaglia","date":"2021-04-26T13:18:09.685Z","features":{"pfam":[{"id":"PF00965","name":"Tissue inhibitor of metalloproteinase","start":25,"end":203}],"gene3D":[]},"length":220,"name":"Metalloproteinase inhibitor 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":209,"end":220,"reference_id":"9837731","reference_source":"pmid","reference_html":"Three-dimensional structure of human tissue inhibitor of metalloproteinases-2 at 2.1 A resolution. <i> Tuuttila A, Morgunova E, Bergmann U, Lindqvist Y, Maskos K, Fernandez-Catalan C, Bode W, Tryggvason K, Schneider G. </i> J Mol Biol, 1998","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1BR9"}],"region_id":"DP03255r001","statement":[{"text":"No electron density was found for the C-terminal 12 residues, indicating disorder for this part of the chain.","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-05-03T12:47:56.083Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":212,"end":220,"reference_id":"8476862","reference_source":"pmid","reference_html":"The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: a kinetic analysis of the inhibition of gelatinase A. <i> Willenbrock F, Crabbe T, Slocombe PM, Sutton CW, Docherty AJ, Cockett MI, O'Shea M, Brocklehurst K, Phillips IR, Murphy G. </i> Biochemistry, 1993","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P08253","partner_start":null,"partner_end":null}],"region_id":"DP03255r002","statement":[{"text":"The C-terminal peptide of TIMP-2 is proposed to exist as an exposed \"tail\" responsible for binding to progelatinase A and for increasing the rate of inhibition of active gelatinase A through electrostatic interactions with the C-terminal domain of the enzyme. The C-terminal domains of both TIMP-1 and TIMP-2 participate in low-affinity interactions with the C-terminal domain of gelatinase A which increase the rate of association by a factor of about 100 in both cases.","type":"Abstract"},{"text":"The work concentrates on a kinetic analysis of factors affecting the rate of association of the inhibitors with gelatinase A and demonstrates that the C-terminal domains of both proteins play an important role in controlling the rate of reaction with active enzyme. C-Terminal domain interactions are also responsible for the binding of TIMP-2 to progelatinase A.","type":"Introduction"},{"text":"The C-terminal nine amino acid peptide of TIMP-2 appears to make an important contribution to the rate of reaction because when this is removed the rate constant decreases approximately 4-fold to resemble that of TIMP-1. The marked decrease in the rate of inhibition by TIMP-2 with increasing ionic strength confirms the importance of ionic interactions to its mechanism. The effect is considerably decreased with the forms of TIMP-2 that lack the C-terminal peptide and is insignificant in the case of TIMP-1. Thus, the C-terminus of TIMP-2 is primarily, although not completely, responsible for the ionic interactions with gelatinase A.","type":"Discussion"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-18T13:05:32.530Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":212,"end":220,"reference_id":"8476862","reference_source":"pmid","reference_html":"The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: a kinetic analysis of the inhibition of gelatinase A. <i> Willenbrock F, Crabbe T, Slocombe PM, Sutton CW, Docherty AJ, Cockett MI, O'Shea M, Brocklehurst K, Phillips IR, Murphy G. </i> Biochemistry, 1993","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03255r003","statement":[{"text":"The C-terminal peptide of TIMP-2 is proposed to exist as an exposed \"tail\" responsible for binding to progelatinase A and for increasing the rate of inhibition of active gelatinase A through electrostatic interactions with the C-terminal domain of the enzyme. The C-terminal domains of both TIMP-1 and TIMP-2 participate in low-affinity interactions with the C-terminal domain of gelatinase A which increase the rate of association by a factor of about 100 in both cases.","type":"Abstract"},{"text":"The work concentrates on a kinetic analysis of factors affecting the rate of association of the inhibitors with gelatinase A and demonstrates that the C-terminal domains of both proteins play an important role in controlling the rate of reaction with active enzyme. C-Terminal domain interactions are also responsible for the binding of TIMP-2 to progelatinase A.","type":"Introduction"},{"text":"The C-terminal nine amino acid peptide of TIMP-2 appears to make an important contribution to the rate of reaction because when this is removed the rate constant decreases approximately 4-fold to resemble that of TIMP-1. The marked decrease in the rate of inhibition by TIMP-2 with increasing ionic strength confirms the importance of ionic interactions to its mechanism. The effect is considerably decreased with the forms of TIMP-2 that lack the C-terminal peptide and is insignificant in the case of TIMP-1. Thus, the C-terminus of TIMP-2 is primarily, although not completely, responsible for the ionic interactions with gelatinase A.","type":"Discussion"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-18T13:05:34.270Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":3,"released":"2021_06","sequence":"MGAAARTLRLALGLLLLATLLRPADACSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPEKDIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEGDGKMHITLCDFIVPWDTLSTTQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKNINGHQAKFFACIKRSDGSCAWYRGAAPPKQEFLDIEDP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000052A5A4","uniref100":"UniRef100_P16035","uniref90":"UniRef90_P16035","uniref50":"UniRef50_P16035","genes":[{"name":{"value":"TIMP2"}}],"alphafold_very_low_content":0,"disorder_content":0.05454545454545454,"disprot_consensus":{"full":[{"start":209,"end":220,"type":"D"}],"Structural state":[{"start":209,"end":220,"type":"D"}],"Molecular function":[{"start":212,"end":220,"type":"F"}]}},{"disprot_id":"DP03256","acc":"P08253","creator":"fquaglia","date":"2021-04-26T14:10:12.643Z","features":{"pfam":[{"id":"PF00040","name":"Fibronectin type II domain","start":233,"end":274},{"id":"PF00040","name":"Fibronectin type II domain","start":291,"end":332},{"id":"PF00045","name":"Hemopexin","start":475,"end":517},{"id":"PF00045","name":"Hemopexin","start":520,"end":563},{"id":"PF00045","name":"Hemopexin","start":568,"end":614},{"id":"PF00045","name":"Hemopexin","start":618,"end":660},{"id":"PF00413","name":"Matrixin","start":118,"end":219},{"id":"PF00413","name":"Matrixin","start":378,"end":446}],"gene3D":[]},"length":660,"name":"72 kDa type IV collagenase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":450,"end":460,"reference_id":"10356396","reference_source":"pmid","reference_html":"Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed. <i> Morgunova E, Tuuttila A, Bergmann U, Isupov M, Lindqvist Y, Schneider G, Tryggvason K. </i> Science, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1CK7"}],"region_id":"DP03256r001","statement":[{"text":"No electron density was observed for the NH2-terminal residue Ala30 and for residues Ser448 to Leu461 of the hinge region.","type":"Table"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-21T15:06:17.286Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":450,"end":460,"reference_id":"10356396","reference_source":"pmid","reference_html":"Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed. <i> Morgunova E, Tuuttila A, Bergmann U, Isupov M, Lindqvist Y, Schneider G, Tryggvason K. </i> Science, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"1CK7"}],"region_id":"DP03256r002","statement":[{"text":"No electron density was observed for the NH2-terminal residue Ala30 and for residues Ser448 to Leu461 of the hinge region.","type":"Table"},{"text":"The COOH-terminal hemopexin-like domain of MMPs is linked to the catalytic domain by a hinge peptide, and it may determine the substrate specificity of MMPs.","type":"Article"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-21T15:06:18.559Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":2,"released":"2021_06","sequence":"MEALMARGALTGPLRALCLLGCLLSHAAAAPSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000172CE7","uniref100":"UniRef100_P08253","uniref90":"UniRef90_P08253","uniref50":"UniRef50_P08253","genes":[{"name":{"value":"MMP2"},"synonyms":[{"value":"CLG4A"}]}],"alphafold_very_low_content":0.05909090909090909,"disorder_content":0.016666666666666666,"disprot_consensus":{"full":[{"start":450,"end":460,"type":"D"}],"Structural state":[{"start":450,"end":460,"type":"D"}],"Disorder function":[{"start":450,"end":460,"type":"F"}]}},{"disprot_id":"DP03257","acc":"P03956","creator":"fquaglia","date":"2021-04-26T14:30:08.691Z","features":{"pfam":[{"id":"PF00045","name":"Hemopexin","start":284,"end":326},{"id":"PF00045","name":"Hemopexin","start":329,"end":371},{"id":"PF00045","name":"Hemopexin","start":377,"end":424},{"id":"PF00045","name":"Hemopexin","start":426,"end":466},{"id":"PF00413","name":"Matrixin","start":108,"end":261},{"id":"PF01471","name":"Putative peptidoglycan binding domain","start":28,"end":87}],"gene3D":[]},"length":469,"name":"Interstitial collagenase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":20,"end":31,"reference_id":"15611040","reference_source":"pmid","reference_html":"X-ray structure of human proMMP-1: new insights into procollagenase activation and collagen binding. <i> Jozic D, Bourenkov G, Lim NH, Visse R, Nagase H, Bode W, Maskos K. </i> J Biol Chem, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1SU3"}],"region_id":"DP03257r001","statement":[{"text":"In the structure described here, the first 12 residues of the prodomain (Phe1-Val12) are not visible in the electron density and are probably flexible.","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-04-30T13:07:04.682Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":46,"end":57,"reference_id":"15611040","reference_source":"pmid","reference_html":"X-ray structure of human proMMP-1: new insights into procollagenase activation and collagen binding. <i> Jozic D, Bourenkov G, Lim NH, Visse R, Nagase H, Bode W, Maskos K. </i> J Biol Chem, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1SU3"}],"region_id":"DP03257r002","statement":[{"text":"Except for the prodomain residues 27–38 and 80–87 the main chains can be traced in continuous electron density.","type":"Methods"},{"text":"Twelve residues (Asn27-Ser38) of loop 1 are not visible in the electron density, suggesting that this region is flexible in solution. The flexible part of loop 1 contains the EKRRN sequence of the “bait” region. This EKRRN peptide would be positioned distal to the catalytic domain and is expected to be fully exposed to the solvent, which would provide maximum accessibility for activating proteases such as plasmin, plasma kallikrein, and trypsin (29).","type":"Results"},{"text":"The residues of loop 1 that contain the proteinase susceptible “bait” region are missing and therefore presumed flexible.","type":"Discussion"},{"text":"The IDR described here and not visible in DPB:1SU3 corresponds to residues 46-57 of the corresponding UniProt sequence.","type":"Curator statement"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-04-30T13:09:18.641Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":52,"end":56,"reference_id":"2176865","reference_source":"pmid","reference_html":"Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin). <i> Suzuki K, Enghild JJ, Morodomi T, Salvesen G, Nagase H. </i> Biochemistry, 1990","date":"2022-02-14T09:00:00.000Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000048","term_name":"limited proteolysis display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP03257r003","statement":[{"text":"Since the Thr64-Leu65 bond is unlikely to be cleaved by these serine proteinases, we postulated that these enzymes initially cleave peptide bonds closer to the NH2 terminus in the propeptide to produce initial intermediates which, in turn, cleave the Thr64-Leu65 bond. To confirm this, procollagenase was incubated with plasma kallikrein (2 ug/mL) or plasmin (10 ug/mL) at 0C for 16 h to minimize the proteolytic action of collagenase intermediates. SDS/PAGE analyses of these products showed intermediates with Mr = 46000 (Figure 8). Sequence analysis of the intermediate generated by plasma kallikrein demonstrated that the Arg35-Arg36 and Arg36-Asn37 bonds were initially attacked by this enzyme. The results agree with the specificity of plasma kallikrein. It is therefore concluded that the formation of the 43 000-Mr species by serine proteinases is a two-step process (Figure 9B).","type":"Results"},{"text":"Asn37 corresponds to Asn56 of the EKRRN sequence in UniProt numbering","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T16:48:16.719Z"},"ec_go":"IDA","disprot_namespace":"Disorder function"}],"regions_counter":3,"released":"2021_06","sequence":"MHSFPPLLLLLFWGVVSHSFPATLETQEQDVDLVQKYLEKYYNLKNDGRQVEKRRNSGPVVEKLKQMQEFFGLKVTGKPDAETLKVMKQPRCGVPDVAQFVLTEGNPRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQAIYGRSQNPVQPIGPQTPKACDSKLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQNVLHGYPKDIYSSFGFPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQKANSWFNCRKN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000014E06D","uniref100":"UniRef100_P03956","uniref90":"UniRef90_P03956","uniref50":"UniRef50_P03956","genes":[{"name":{"value":"MMP1"},"synonyms":[{"value":"CLG"}]}],"alphafold_very_low_content":0.0511727078891258,"disorder_content":0.0511727078891258,"disprot_consensus":{"full":[{"start":20,"end":31,"type":"D"},{"start":46,"end":57,"type":"D"}],"Structural state":[{"start":20,"end":31,"type":"D"},{"start":46,"end":57,"type":"D"}],"Disorder function":[{"start":52,"end":56,"type":"F"}]}},{"disprot_id":"DP03258","acc":"Q60841","creator":"fquaglia","date":"2021-04-26T15:23:21.483Z","features":{"pfam":[{"id":"PF02014","name":"Reeler domain","start":61,"end":171},{"id":"PF21471","name":"Reelin subrepeat B","start":227,"end":351},{"id":"PF21471","name":"Reelin subrepeat B","start":436,"end":557},{"id":"PF21471","name":"Reelin subrepeat B","start":568,"end":672},{"id":"PF21471","name":"Reelin subrepeat B","start":732,"end":862},{"id":"PF21471","name":"Reelin subrepeat B","start":889,"end":1031},{"id":"PF21471","name":"Reelin subrepeat B","start":1095,"end":1220},{"id":"PF21471","name":"Reelin subrepeat B","start":1267,"end":1410},{"id":"PF21471","name":"Reelin subrepeat B","start":1468,"end":1598},{"id":"PF21471","name":"Reelin subrepeat B","start":1626,"end":1765},{"id":"PF21471","name":"Reelin subrepeat B","start":1832,"end":1947},{"id":"PF21471","name":"Reelin subrepeat B","start":1976,"end":2130},{"id":"PF21471","name":"Reelin subrepeat B","start":2188,"end":2315},{"id":"PF21471","name":"Reelin subrepeat B","start":2341,"end":2479},{"id":"PF21471","name":"Reelin subrepeat B","start":2537,"end":2662},{"id":"PF21471","name":"Reelin subrepeat B","start":2720,"end":2854},{"id":"PF21471","name":"Reelin subrepeat B","start":2912,"end":3050},{"id":"PF21471","name":"Reelin subrepeat B","start":3104,"end":3229},{"id":"PF21471","name":"Reelin subrepeat B","start":3289,"end":3426},{"id":"PF23106","name":"Teneurin-like EGF domain","start":1034,"end":1061},{"id":"PF23106","name":"Teneurin-like EGF domain","start":3232,"end":3261}],"gene3D":[]},"length":3461,"name":"Reelin","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":1222,"end":1293,"reference_id":"16858396","reference_source":"pmid","reference_html":"Structure of a signaling-competent reelin fragment revealed by X-ray crystallography and electron tomography. <i> Nogi T, Yasui N, Hattori M, Iwasaki K, Takagi J. </i> EMBO J, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"2DDU"}],"region_id":"DP03258r001","statement":[{"text":"The crystals have one R3 molecule per asymmetric unit, and 301 out of 387 residues of the R3 construct are visible in the electron density (Figure 2).","type":"Results"},{"text":"As the quality of the electron density corresponding to the N-terminal (1222–1293) and a loop (1393–1398) segment was poor, we omitted these segments from the final model.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_12","sequence":"MERGCWAPRALVLAVLLLLATLRARAATGYYPRFSPFFFLCTHHGELEGDGEQGEVLISLHIAGNPTYYVPGQEYHVTISTSTFFDGLLVTGLYTSTSIQSSQSIGGSSAFGFGIMSDHQFGNQFMCSVVASHVSHLPTTNLSFVWIAPPAGTGCVNFMATATHRGQVIFKDALAQQLCEQGAPTEATAYSHLAEIHSDSVILRDDFDSYQQLELNPNIWVECSNCEMGEQCGTIMHGNAVTFCEPYGPRELTTTCLNTTTASVLQFSIGSGSCRFSYSDPSITVSYAKNNTADWIQLEKIRAPSNVSTVIHILYLPEEAKGESVQFQWKQDSLRVGEVYEACWALDNILVINSAHREVVLEDNLDPVDTGNWLFFPGATVKHSCQSDGNSIYFHGNEGSEFNFATTRDVDLSTEDIQEQWSEEFESQPTGWDILGAVVGADCGTVESGLSLVFLKDGERKLCTPYMDTTGYGNLRFYFVMGGICDPGVSHENDIILYAKIEGRKEHIALDTLTYSSYKVPSLVSVVINPELQTPATKFCLRQKSHQGYNRNVWAVDFFHVLPVLPSTMSHMIQFSINLGCGTHQPGNSVSLEFSTNHGRSWSLLHTECLPEICAGPHLPHSTVYSSENYSGWNRITIPLPNAALTRDTRIRWRQTGPILGNMWAIDNVYIGPSCLKFCSGRGQCTRHGCKCDPGFSGPACEMASQTFPMFISESFGSARLSSYHNFYSIRGAEVSFGCGVLASGKALVFNKDGRRQLITSFLDSSQSRFLQFTLRLGSKSVLSTCRAPDQPGEGVLLHYSYDNGITWKLLEHYSYVNYHEPRIISVELPDDARQFGIQFRWWQPYHSSQGEDVWAIDEIVMTSVLFNSISLDFTNLVEVTQSLGFYLGNVQPYCGHDWTLCFTGDSKLASSMRYVETQSMQIGASYMIQFSLVMGCGQKYTPHMDNQVKLEYSANHGLTWHLVQEECLPSMPSCQEFTSASIYHASEFTQWRRVTVVLPQKTWSGATRFRWSQSYYTAQDEWALDNIYIGQQCPNMCSGHGSCDHGVCRCDQGYQGTECHPEAALPSTIMSDFENPSSWESDWQEVIGGEVVKPEQGCGVVSSGSSLYFSKAGKRQLVSWDLDTSWVDFVQFYIQIGGESAACNKPDSREEGILLQYSNNGGIQWHLLAEMYFSDFSKPRFVYLELPAAAKTPCTRFRWWQPVFSGEDYDQWAVDDIIILSEKQKQVIPVVNPTLPQNFYEKPAFDYPMNQMSVWLMLANEGMAKNDSFCATTPSAMVFGKSDGDRFAVTRDLTLKPGYVLQFKLNIGCTSQFSSTAPVLLQYSHDAGMSWFLVKEGCFPASAGKGCEGNSRELSEPTVYYTGDFEEWTRITIAIPRSLASSKTRFRWIQESSSQKNVPPFGLDGVYISEPCPSYCSGHGDCISGVCFCDLGYTAAQGTCVSNTPNHSEMFDRFEGKLSPLWYKITGGQVGTGCGTLNDGRSLYFNGLGKREARTVPLDTRNIRLVQFYIQIGSKTSGITCIKPRARNEGLVVQYSNDNGILWHLLRELDFMSFLEPQIISIDLPREAKTPATAFRWWQPQHGKHSAQWALDDVLIGVNDSSQTGFQDKFDGSIDLQANWYRIQGGQVDIDCLSMDTALIFTENIGKPRYAETWDFHVSASSFLQFEMNMGCSKPFSGAHGIQLQYSLNNGKDWQLVTEECVPPTIGCVHYTESSTYTSERFQNWRRVTVYLPLATNSPRTRFRWIQTNYTVGADSWAIDNVILASGCPWMCSGRGICDSGRCVCDRGFGGPFCVPVVPLPSILKDDFNGNLHPDLWPEVYGAERGNLNGETIKSGTCLIFKGEGLRMLISRDLDCTNTMYVQFSLRFIAKGTPERSHSILLQFSVSGGVTWHLMDEFYFPQTTSILFINVPLPYGAQTNATRFRLWQPYNNGKKEEIWIIDDFIIDGNNLNNPVLLLDTFDFGPREDNWFFYPGGNIGLYCPYSSKGAPEEDSAMVFVSNEVGEHSITTRDLSVNENTIIQFEINVGCSTDSSSADPVRLEFSRDFGATWHLLLPLCYHSSSLVSSLCSTEHHPSSTYYAGTTQGWRREVVHFGKLHLCGSVRFRWYQGFYPAGSQPVTWAIDNVYIGPQCEEMCYGHGSCINGTKCICDPGYSGPTCKISTKNPDFLKDDFEGQLESDRFLLMSGGKPSRKCGILSSGNNLFFNEDGLRMLVTRDLDLSHARFVQFFMRLGCGKGVPDPRSQPVLLQYSLNGGLSWSLLQEFLFSNSSNVGRYIALEMPLKARSGSTRLRWWQPSENGHFYSPWVIDQILIGGNISGNTVLEDDFSTLDSRKWLLHPGGTKMPVCGSTGDALVFIEKASTRYVVTTDIAVNEDSFLQIDFAASCSVTDSCYAIELEYSVDLGLSWHPLVRDCLPTNVECSRYHLQRILVSDTFNKWTRITLPLPSYTRSQATRFRWHQPAPFDKQQTWAIDNVYIGDGCLDMCSGHGRCVQGSCVCDEQWGGLYCDEPETSLPTQLKDNFNRAPSNQNWLTVSGGKLSTVCGAVASGLALHFSGGCSRLLVTVDLNLTNAEFIQFYFMYGCLITPSNRNQGVLLEYSVNGGITWNLLMEIFYDQYSKPGFVNILLPPDAKEIATRFRWWQPRHDGLDQNDWAIDNVLISGSADQRTVMLDTFSSAPVPQHERSPADAGPVGRIAFEMFLEDKTSVNENWLFHDDCTVERFCDSPDGVMLCGSHDGREVYAVTHDLTPTENWIMQFKISVGCKVPEKIAQNQIHVQFSTDFGVSWSYLVPQCLPADPKCSGSVSQPSVFFPTEGWKRITYPLPESLTGNPVRFRFYQKYSDVQWAIDNFYLGPGCLDNCGGHGDCLKEQCICDPGYSGPNCYLTHSLKTFLKERFDSEEIKPDLWMSLEGGSTCTECGVLAENTALYFGGSTVRQAITQDLDLRGAKFLQYWGRIGSENNMTSCHRPVCRKEGVLLDFSTDGGITWTLLHEMDFQKYISVRHDYILLPEGALTNTTRLRWWQPFVISNGLVVSGVERAQWALDNILIGGAEINPSQLVDTFDDEGSSHEENWSFYPNAVRTAGFCGNPSFHLYWPNKKKDKTHNALSSRELIIQPGYMMQFKIVVGCEATSCGDLHSVMLEYTKDARSDSWQLVQTQCLPSSSNSIGCSPFQFHEATIYNAVNSSSWKRITIQLPDHVSSSATQFRWIQKGEETEKQSWAIDHVYIGEACPKLCSGHGYCTTGAVCICDESFQGDDCSVFSHELPSYIKDNFESARVTEANWETIQGGVIGSGCGQLAPYAHGDSLYFNGCQIRQAATKPLDLTRASKIMFVLQIGSPAQTDSCNSDLSGPHTVDKAVLLQYSVNNGITWHVIAQHQPKDFTQAQRVSYNVPLEARMKGVLLRWWQPRHNGTGHDQWALDHVEVVLVSTRKQNYMMNFSRQHGLRHFYNRRRRSLRRYP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"dataset":[],"UniParc":"UPI0000028747","uniref100":"UniRef100_Q60841","uniref90":"UniRef90_Q60841","uniref50":"UniRef50_Q60841","genes":[{"name":{"value":"Reln"},"synonyms":[{"value":"Rl"}]}],"disorder_content":0.020803236058942503,"disprot_consensus":{"full":[{"start":1222,"end":1293,"type":"D"}],"Structural state":[{"start":1222,"end":1293,"type":"D"}]}},{"disprot_id":"DP03259","acc":"P13674","creator":"fquaglia","date":"2021-04-28T10:23:50.745Z","features":{"pfam":[{"id":"PF08336","name":"Prolyl 4-Hydroxylase alpha-subunit, N-terminal region","start":24,"end":155},{"id":"PF13640","name":"2OG-Fe(II) oxygenase superfamily","start":415,"end":518},{"id":"PF23558","name":"Prolyl 4-hydroxylase peptide-substrate-binding domain","start":164,"end":254}],"gene3D":[]},"length":534,"name":"Prolyl 4-hydroxylase subunit alpha-1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":151,"end":160,"reference_id":"24207127","reference_source":"pmid","reference_html":"The structural motifs for substrate binding and dimerization of the α subunit of collagen prolyl 4-hydroxylase. <i> Anantharajan J, Koski MK, Kursula P, Hieta R, Bergmann U, Myllyharju J, Wierenga RK. </i> Structure, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":2,"cross_refs":[{"db":"PDB","id":"4BT8"}],"region_id":"DP03259r001","statement":[{"text":"The return helix α4 is further connected to the PSB domain via a linker region (residues 104–143), forming two helices (α5 and α6) and an extended loop region (Figure 3).","type":"Results"},{"text":"The dimerization interactions within the four-helix bundle (between helices α1, α3, and α4), are complemented by interactions of the linker region. This region consists of two α helices, α5 and α6, and a loop following α6 (Figure 4B). This loop (residues 135–144) is either disordered, or modeled with high B factors (average B factor ranging from 35 to 122 Å2), indicating high flexibility (see Figure S2).","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-04-30T13:18:09.361Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":151,"end":160,"reference_id":"24207127","reference_source":"pmid","reference_html":"The structural motifs for substrate binding and dimerization of the α subunit of collagen prolyl 4-hydroxylase. <i> Anantharajan J, Koski MK, Kursula P, Hieta R, Bergmann U, Myllyharju J, Wierenga RK. </i> Structure, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03259r003","statement":[{"text":"The return helix α4 is further connected to the PSB domain via a linker region (residues 104–143), forming two helices (α5 and α6) and an extended loop region (Figure 3).","type":"Results"},{"text":"The dimerization interactions within the four-helix bundle (between helices α1, α3, and α4), are complemented by interactions of the linker region. This region consists of two α helices, α5 and α6, and a loop following α6 (Figure 4B). This loop (residues 135–144) is either disordered, or modeled with high B factors (average B factor ranging from 35 to 122 Å2), indicating high flexibility (see Figure S2).","type":"Results"}],"cross_refs":[{"db":"PDB","id":"4BT8"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-21T14:52:58.293Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2023_06","sequence":"MIWYILIIGILLPQSLAHPGFFTSIGQMTDLIHTEKDLVTSLKDYIKAEEDKLEQIKKWAEKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLVLKDMSDGFISNLTIQRQYFPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPGVKHKSFLTAEDCFELGKVAYTEADYYHTELWMEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQRANGNLKYFEYIMAKEKDVNKSASDDQSDQKTTPKKKGVAVDYLPERQKYEMLCRGEGIKMTPRRQKKLFCRYHDGNRNPKFILAPAKQEDEWDKPRIIRFHDIISDAEIEIVKDLAKPRLRRATISNPITGDLETVHYRISKSAWLSGYENPVVSRINMRIQDLTGLDVSTAEELQVANYGVGGQYEPHFDFARKDEPDAFKELGTGNRIATWLFYMSDVSAGGATVFPEVGASVWPKKGTAVFWYNLFASGEGDYSTRHAACPVLVGNKWVSNKWLHERGQEFRRPCTLSELE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000016AF4E","uniref100":"UniRef100_P13674","uniref90":"UniRef90_P13674","uniref50":"UniRef50_P13674","genes":[{"name":{"value":"P4HA1"},"synonyms":[{"value":"P4HA"}]}],"alphafold_very_low_content":0.056179775280898875,"disorder_content":0.018726591760299626,"disprot_consensus":{"full":[{"start":151,"end":160,"type":"D"}],"Structural state":[{"start":151,"end":160,"type":"D"}]}},{"disprot_id":"DP03260","acc":"O60568","creator":"fquaglia","date":"2021-04-28T10:56:32.811Z","features":{"pfam":[{"id":"PF03171","name":"2OG-Fe(II) oxygenase superfamily","start":651,"end":738},{"id":"PF13704","name":"Glycosyltransferase family 25, N-terminal domain","start":384,"end":518},{"id":"PF25342","name":"PLOD GT domain","start":37,"end":279}],"gene3D":[]},"length":738,"name":"Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":72,"end":86,"reference_id":"30089812","reference_source":"pmid","reference_html":"Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3. <i> Scietti L, Chiapparino A, De Giorgi F, Fumagalli M, Khoriauli L, Nergadze S, Basu S, Olieric V, Cucca L, Banushi B, Profumo A, Giulotto E, Gissen P, Forneris F. </i> Nat Commun, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6FXK"}],"region_id":"DP03260r001","statement":[{"text":"Among these, a very flexible surface loop comprising residues Gly72 to Gly87 is not visible in the electron density of ligand-free LH3 structures. This loop contains several residues highly conserved among LH isoforms (Supplementary Fig. 9), which are not found in other glycosyltransferases.","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-21T15:40:31.444Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":592,"end":605,"reference_id":"30089812","reference_source":"pmid","reference_html":"Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3. <i> Scietti L, Chiapparino A, De Giorgi F, Fumagalli M, Khoriauli L, Nergadze S, Basu S, Olieric V, Cucca L, Banushi B, Profumo A, Giulotto E, Gissen P, Forneris F. </i> Nat Commun, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6FXK"}],"region_id":"DP03260r002","statement":[{"text":"Residues 590–610 constitute a flexible loop capping the LH catalytic site.","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-21T15:40:56.116Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":73,"end":77,"reference_id":"30089812","reference_source":"pmid","reference_html":"Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3. <i> Scietti L, Chiapparino A, De Giorgi F, Fumagalli M, Khoriauli L, Nergadze S, Basu S, Olieric V, Cucca L, Banushi B, Profumo A, Giulotto E, Gissen P, Forneris F. </i> Nat Commun, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03260r003","statement":[{"text":"Structurally related glycosyltransferases also often bear tyrosine residues stacking with the UDP moiety, but these residues are located far in sequence from the canonical DxD motif40,41 responsible for metal ion coordination. Site-directed mutagenesis on Trp75 or Tyr114 into alanine residues yielded folded, but almost completely inactive LH3 variants (Fig. 2c, Supplementary fig. 11). Binding data using SPR on synthetic collagen peptides showed very limited differences between wild-type and mutant LH3 (Supplementary Fig. 11D). Together, these results highlight the distinguishing roles of Trp75 and Tyr114 in donor substrate binding and stabilization.","type":"Results"},{"text":"Trp75 stabilizes the UDP binding","type":"Curator statement"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-21T15:42:30.159Z"},"ec_go":"IMP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":72,"end":86,"reference_id":"30089812","reference_source":"pmid","reference_html":"Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3. <i> Scietti L, Chiapparino A, De Giorgi F, Fumagalli M, Khoriauli L, Nergadze S, Basu S, Olieric V, Cucca L, Banushi B, Profumo A, Giulotto E, Gissen P, Forneris F. </i> Nat Commun, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6FXT"},{"db":"PDB","id":"6FXR"},{"db":"PDB","id":"6FXY"},{"db":"PDB","id":"6FXX"}],"region_id":"DP03260r004","statement":[{"text":"Nonetheless, binding of these donor substrates induced dramatic conformational changes in the enzyme’s catalytic site, with full stabilization of the flexible Gly72-Gly87 loop in a “closed” conformation (Fig. 2b). The UDP pyrophosphate group is stabilized by interactions with Mn2+ and hydrogen bonding with Lys259 and backbone nitrogen of Gly256; both residues are positioned in a uniquely shaped α-helix located at the C-terminus of the domain.","type":"Results"},{"text":"Flexible loop 72–87 becomes well defined only in donor substrate-bound structures","type":"Figure"},{"text":"The uracil moiety is sandwiched through π-π stacking interactions between Trp75 and Tyr114, and is stabilized by hydrogen bonding with Thr46 (Fig. 2a, b, Supplementary Fig. 10). Of note, these two residues highlight an unprecedented arrangement of UDP binding residues in glycosyltransferases: Trp75 belongs to the distinctive LH3 flexible loop covering residues Gly72-Gly87, that becomes fully stabilized upon substrate binding (Fig. 2b); Tyr114 is part of a non-canonical DxxD motif (Supplementary fig. 9), where Asp112, and Asp115 are responsible for Mn2+ coordination.","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-21T15:59:32.285Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":73,"end":77,"reference_id":"30089812","reference_source":"pmid","reference_html":"Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3. <i> Scietti L, Chiapparino A, De Giorgi F, Fumagalli M, Khoriauli L, Nergadze S, Basu S, Olieric V, Cucca L, Banushi B, Profumo A, Giulotto E, Gissen P, Forneris F. </i> Nat Commun, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0036094","term_name":"small molecule binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"6FXT"},{"db":"PDB","id":"6FXR"},{"db":"PDB","id":"6FXY"},{"db":"PDB","id":"6FXX"}],"interaction_partner":[{"db":"ChEBI","id":"17659","partner_start":null,"partner_end":null}],"region_id":"DP03260r005","statement":[{"text":"Nonetheless, binding of these donor substrates induced dramatic conformational changes in the enzyme’s catalytic site, with full stabilization of the flexible Gly72-Gly87 loop in a “closed” conformation (Fig. 2b). The UDP pyrophosphate group is stabilized by interactions with Mn2+ and hydrogen bonding with Lys259 and backbone nitrogen of Gly256; both residues are positioned in a uniquely shaped α-helix located at the C-terminus of the domain.","type":"Results"},{"text":"Flexible loop 72–87 becomes well defined only in donor substrate-bound structures","type":"Figure"},{"text":"The uracil moiety is sandwiched through π-π stacking interactions between Trp75 and Tyr114, and is stabilized by hydrogen bonding with Thr46 (Fig. 2a, b, Supplementary Fig. 10). Of note, these two residues highlight an unprecedented arrangement of UDP binding residues in glycosyltransferases: Trp75 belongs to the distinctive LH3 flexible loop covering residues Gly72-Gly87, that becomes fully stabilized upon substrate binding (Fig. 2b); Tyr114 is part of a non-canonical DxxD motif (Supplementary fig. 9), where Asp112, and Asp115 are responsible for Mn2+ coordination.","type":"Results"},{"text":"Residues involved in coordination of the metal ion are shown with orange sticks, while residues interacting and stabilizing UDP binding are shown in blue.","type":"Figure"},{"text":"Nearly all residues surrounding the UDP moiety and shaping the LH3 glycosyltransferase catalytic site are conserved, including those involved in the unprecedented mode of UDP-substrate stabilization characterized by dual π-π stacking with Trp75 and Tyr114.","type":"Discussion"},{"text":"Trp75 stabilizes the UDP binding.","type":"Curator statement"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-05-10T15:12:05.722Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":73,"end":77,"reference_id":"30089812","reference_source":"pmid","reference_html":"Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3. <i> Scietti L, Chiapparino A, De Giorgi F, Fumagalli M, Khoriauli L, Nergadze S, Basu S, Olieric V, Cucca L, Banushi B, Profumo A, Giulotto E, Gissen P, Forneris F. </i> Nat Commun, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03260r006","statement":[{"text":"Nonetheless, binding of these donor substrates induced dramatic conformational changes in the enzyme’s catalytic site, with full stabilization of the flexible Gly72-Gly87 loop in a “closed” conformation (Fig. 2b). The UDP pyrophosphate group is stabilized by interactions with Mn2+ and hydrogen bonding with Lys259 and backbone nitrogen of Gly256; both residues are positioned in a uniquely shaped α-helix located at the C-terminus of the domain.","type":"Results"},{"text":"Flexible loop 72–87 becomes well defined only in donor substrate-bound structures","type":"Figure"},{"text":"The uracil moiety is sandwiched through π-π stacking interactions between Trp75 and Tyr114, and is stabilized by hydrogen bonding with Thr46 (Fig. 2a, b, Supplementary Fig. 10). Of note, these two residues highlight an unprecedented arrangement of UDP binding residues in glycosyltransferases: Trp75 belongs to the distinctive LH3 flexible loop covering residues Gly72-Gly87, that becomes fully stabilized upon substrate binding (Fig. 2b); Tyr114 is part of a non-canonical DxxD motif (Supplementary fig. 9), where Asp112, and Asp115 are responsible for Mn2+ coordination.","type":"Results"},{"text":"Residues involved in coordination of the metal ion are shown with orange sticks, while residues interacting and stabilizing UDP binding are shown in blue.","type":"Figure"},{"text":"Nearly all residues surrounding the UDP moiety and shaping the LH3 glycosyltransferase catalytic site are conserved, including those involved in the unprecedented mode of UDP-substrate stabilization characterized by dual π-π stacking with Trp75 and Tyr114.","type":"Discussion"},{"text":"Trp75 stabilizes the UDP binding.","type":"Curator statement"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-05-10T15:13:37.518Z"},"ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":593,"end":597,"reference_id":"30089812","reference_source":"pmid","reference_html":"Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3. <i> Scietti L, Chiapparino A, De Giorgi F, Fumagalli M, Khoriauli L, Nergadze S, Basu S, Olieric V, Cucca L, Banushi B, Profumo A, Giulotto E, Gissen P, Forneris F. </i> Nat Commun, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"ChEBI","id":"29033","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"29035","partner_start":null,"partner_end":null}],"region_id":"DP03260r007","statement":[{"text":"Analysis of electron density maps allowed the identification of a second Fe2+ in the LH domain, coordinated by residues His595, Asp597, Asp611 and His613 (Fig. 3b). Metal ion coordination stabilizes the flexible capping loop 590–610 into a conformation that completely plugs the LH catalytic site, in proximity to the dimer interface (Supplementary Fig. 16A). We could observe a very similar arrangement, although slightly more flexible, by replacing Fe2+ with Mn2+ in crystallization experiments (Supplementary Fig. 16B).","type":"Results"},{"text":"Co-crystallizations with Fe2+ allow identification of a second metal ion bound near the LH catalytic site that stabilizes the flexible capping loop 590–610 (shown in pink)","type":"Figure"},{"text":"Four residues coordinate the binding of the second Fe2+ in metal ion-inhibited structures: His595, Asp597, Asp611 and His613. Two of them, His595 and His597, are localized in the flexible capping loop of the protein. This annotation describes His595.","type":"Curator statement"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-21T15:59:47.010Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":593,"end":597,"reference_id":"30089812","reference_source":"pmid","reference_html":"Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3. <i> Scietti L, Chiapparino A, De Giorgi F, Fumagalli M, Khoriauli L, Nergadze S, Basu S, Olieric V, Cucca L, Banushi B, Profumo A, Giulotto E, Gissen P, Forneris F. </i> Nat Commun, 2018","date":"2022-12-06T11:00:08.532Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005506","term_name":"iron ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_12","version":4,"region_id":"DP03260r008","statement":[{"text":"Co-crystallizations with Fe2+ allow identification of a second metal ion bound near the LH catalytic site that stabilizes the flexible capping loop 590–610 (shown in pink).","type":"Figure"},{"text":"Analysis of electron density maps allowed the identification of a second Fe2+ in the LH domain, coordinated by residues His595, Asp597, Asp611 and His613 (Fig. 3b). Metal ion coordination stabilizes the flexible capping loop 590–610 into a conformation that completely plugs the LH catalytic site, in proximity to the dimer interface (Supplementary Fig. 16A). We could observe a very similar arrangement, although slightly more flexible, by replacing Fe2+ with Mn2+ in crystallization experiments (Supplementary Fig. 16B).","type":"Results"},{"text":"Four residues coordinate the Fe2+ binding: His595, Asp597, Asp611 and His613. Two of them, His595 and His597, are localized in the flexible capping loop of the protein. This annotation describes His595.","type":"Curator statement"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an iron (Fe) ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-20T17:39:35.822Z"}},{"start":595,"end":599,"reference_id":"30089812","reference_source":"pmid","reference_html":"Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3. <i> Scietti L, Chiapparino A, De Giorgi F, Fumagalli M, Khoriauli L, Nergadze S, Basu S, Olieric V, Cucca L, Banushi B, Profumo A, Giulotto E, Gissen P, Forneris F. </i> Nat Commun, 2018","date":"2022-12-06T11:00:28.401Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005506","term_name":"iron ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_12","version":4,"region_id":"DP03260r009","statement":[{"text":"Co-crystallizations with Fe2+ allow identification of a second metal ion bound near the LH catalytic site that stabilizes the flexible capping loop 590–610 (shown in pink).","type":"Figure"},{"text":"Analysis of electron density maps allowed the identification of a second Fe2+ in the LH domain, coordinated by residues His595, Asp597, Asp611 and His613 (Fig. 3b). Metal ion coordination stabilizes the flexible capping loop 590–610 into a conformation that completely plugs the LH catalytic site, in proximity to the dimer interface (Supplementary Fig. 16A). We could observe a very similar arrangement, although slightly more flexible, by replacing Fe2+ with Mn2+ in crystallization experiments (Supplementary Fig. 16B).","type":"Results"},{"text":"Four residues coordinate the Fe2+ binding: His595, Asp597, Asp611 and His613. Two of them, His595 and Asp597, are localized in the flexible capping loop of the protein. This annotation describes Asp597.","type":"Curator statement"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an iron (Fe) ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-20T17:39:34.886Z"}},{"start":595,"end":599,"reference_id":"30089812","reference_source":"pmid","reference_html":"Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3. <i> Scietti L, Chiapparino A, De Giorgi F, Fumagalli M, Khoriauli L, Nergadze S, Basu S, Olieric V, Cucca L, Banushi B, Profumo A, Giulotto E, Gissen P, Forneris F. </i> Nat Commun, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"ChEBI","id":"29033","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"29035","partner_start":null,"partner_end":null}],"region_id":"DP03260r010","statement":[{"text":"Co-crystallizations with Fe2+ allow identification of a second metal ion bound near the LH catalytic site that stabilizes the flexible capping loop 590–610 (shown in pink).","type":"Figure"},{"text":"Analysis of electron density maps allowed the identification of a second Fe2+ in the LH domain, coordinated by residues His595, Asp597, Asp611 and His613 (Fig. 3b). Metal ion coordination stabilizes the flexible capping loop 590–610 into a conformation that completely plugs the LH catalytic site, in proximity to the dimer interface (Supplementary Fig. 16A). We could observe a very similar arrangement, although slightly more flexible, by replacing Fe2+ with Mn2+ in crystallization experiments (Supplementary Fig. 16B).","type":"Results"},{"text":"Four residues coordinate the binding of the second Fe2+ in metal ion-inhibited structures: His595, Asp597, Asp611 and His613. Two of them, His595 and His597, are localized in the flexible capping loop of the protein. This annotation describes Asp597.","type":"Curator statement"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-21T15:59:52.494Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":10,"released":"2021_06","sequence":"MTSSGPGPRFLLLLPLLLPPAASASDRPRGRDPVNPEKLLVITVATAETEGYLRFLRSAEFFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDVILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIVRQWKYKDDDDDQLFYTRLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLGNYVPNGWTPEGGCGFCNQDRRTLPGGQPPPRVFLAVFVEQPTPFLPRFLQRLLLLDYPPDRVTLFLHNNEVFHEPHIADSWPQLQDHFSAVKLVGPEEALSPGEARDMAMDLCRQDPECEFYFSLDADAVLTNLQTLRILIEENRKVIAPMLSRHGKLWSNFWGALSPDEYYARSEDYVELVQRKRVGVWNVPYISQAYVIRGDTLRMELPQRDVFSGSDTDPDMAFCKSFRDKGIFLHLSNQHEFGRLLATSRYDTEHLHPDLWQIFDNPVDWKEQYIHENYSRALEGEGIVEQPCPDVYWFPLLSEQMCDELVAEMEHYGQWSGGRHEDSRLAGGYENVPTVDIHMKQVGYEDQWLQLLRTYVGPMTESLFPGYHTKARAVMNFVVRYRPDEQPSLRPHHDSSTFTLNVALNHKGLDYEGGGCRFLRYDCVISSPRKGWALLHPGRLTHYHEGLPTTWGTRYIMVSFVDP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000046664","uniref100":"UniRef100_O60568","uniref90":"UniRef90_O60568","uniref50":"UniRef50_O60568","genes":[{"name":{"value":"PLOD3"}}],"alphafold_very_low_content":0.04200542005420054,"disorder_content":0.03929539295392954,"disprot_consensus":{"full":[{"start":72,"end":86,"type":"T"},{"start":592,"end":605,"type":"D"}],"Structural state":[{"start":72,"end":86,"type":"D"},{"start":592,"end":605,"type":"D"}],"Molecular function":[{"start":73,"end":77,"type":"F"},{"start":593,"end":599,"type":"F"}],"Structural transition":[{"start":72,"end":86,"type":"T"}]}},{"disprot_id":"DP03261","acc":"P75966","creator":"jnilsson","date":"2021-04-30T10:24:24.062Z","features":{"pfam":[{"id":"PF00849","name":"RNA pseudouridylate synthase","start":41,"end":186}],"gene3D":[]},"length":217,"name":"Ribosomal large subunit pseudouridine synthase E","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":1,"end":36,"reference_id":"17320904","reference_source":"pmid","reference_html":"The crystal structure of E. coli rRNA pseudouridine synthase RluE. <i> Pan H, Ho JD, Stroud RM, Finer-Moore J. </i> J Mol Biol, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2OLW"}],"region_id":"DP03261r001","statement":[{"text":"The crystals of the full-length enzyme contain two molecules in the asymmetric unit and in both molecules the N-terminal domain is disordered.","type":"Abstract"},{"text":"Density for the N-terminal 35 amino acids of RluE was not visible in electron density maps calculated for either truncated or full-length RluE. A large single crystal of fulllength RluE was carefully washed in protein-free mother liquor, dissolved in water and run on an SDS-PAGE gel in order to find out if full-length RluE had undergone proteolysis during crystallization. The gel showed a single protein band with the molecular mass of full-length RluE. Therefore, the N-terminal 35 residues of RluE must be disordered in the crystal.","type":"Methods"},{"text":"The disordered N-terminal residues may comprise a separate protein domain that vibrates as a rigid body. Other Ψ synthases in the RsuA family contain an S4-like domain at their N-termini that is postulated to bind nonspecifically to RNA substrate29; 30.","type":"Results"},{"text":"The RNA-binding domains of Ψ synthases are usually attached to the rest of the protein by a flexible tether, and so are frequently disordered in crystal structures of the apo enzymes. The N-terminal 35 residues of E. coli RluE contain six arginines and three lysines. The basic nature of the N-terminal region is consistent with its putative role in RNA binding.","type":"Results"},{"text":"For the truncated protein structure, rounds of rebuilding and addition of solvent molecules using Quanta (Accelrys, San Diego, CA), alternated with restrained refinement of atomic positions and isotropic temperature factors in CNS42 were carried out until the R-factor reached 20.1% (Rfree=21.3%). There was no electron density for residues before Asn-36 or for residue Glu-159 in loop L7–8 (Fig. 1); these residues are either not present in the truncated protein or are disordered in the crystals. An analysis of the geometry45 shows that all refinement statistics are well within the expected values at this resolution (Table 2).","type":"Methods"},{"text":"Full-length RluE was refined in a similar manner, except that anisotropic B-factors were not refined, and only CNS and REFMAC5 were used for refinement. The two protein molecules in the asymmetric unit had slightly different conformations, so non-crystallographic symmetry restraints were not used. No density for residues 1–37 in one molecule or 1–38 in the other was present in electron density maps, and Glu-159 was also disordered in both molecules.","type":"Methods"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-06T08:42:00.816Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MRQFIISENTMQKTSFRNHQVKRFSSQRSTRRKPENQPTRVILFNKPYDVLPQFTDEAGRKTLKEFIPVQGVYAAGRLDRDSEGLLVLTNNGALQARLTQPGKRTGKIYYVQVEGIPTQDALEALRNGVTLNDGPTLPAGAELVDEPAWLWPRNPPIRERKSIPTSWLKITLYEGRNRQVRRMTAHVGFPTLRLIRYAMGDYSLDNLANGEWREVTD","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":[],"UniParc":"UPI000016807E","uniref100":"UniRef100_P75966","uniref90":"UniRef90_P75966","uniref50":"UniRef50_P75966","genes":[{"name":{"value":"rluE"},"synonyms":[{"value":"ymfC"}],"olnNames":[{"value":"b1135"},{"value":"JW1121"}]}],"alphafold_very_low_content":0.07834101382488479,"disorder_content":0.16589861751152074,"disprot_consensus":{"full":[{"start":1,"end":36,"type":"D"}],"Structural state":[{"start":1,"end":36,"type":"D"}]}},{"disprot_id":"DP03262","acc":"P01009","creator":"spenadias","date":"2021-05-04T16:44:16.053Z","features":{"pfam":[{"id":"PF00079","name":"Serpin (serine protease inhibitor)","start":54,"end":415}],"gene3D":[]},"length":418,"name":"Alpha-1-antitrypsin","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":26,"end":47,"reference_id":"12860985","reference_source":"pmid","reference_html":"Canonical inhibitor-like interactions explain reactivity of alpha1-proteinase inhibitor Pittsburgh and antithrombin with proteinases. <i> Dementiev A, Simonovic M, Volz K, Gettins PG. </i> J Biol Chem, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1OO8"}],"region_id":"DP03262r001","statement":[{"text":"22 N-terminal amino acids and the histidine tag were not visible in the final electron density maps","type":"Methods"},{"text":"The structure defined in this paper comprises residues 26-418","type":"Curator statement"},{"text":"The IDR characterized in the publication and spanning the N-terminal residues of the crystal structure corresponds to region 26-47 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-24) that is cleaved in the mature secreted protein.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-06T16:04:52.896Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":25,"end":42,"reference_id":"11178897","reference_source":"pmid","reference_html":"A 2.1 A resolution structure of an uncleaved alpha(1)-antitrypsin shows variability of the reactive center and other loops. <i> Kim S, Woo J, Seo EJ, Yu M, Ryu S. </i> J Mol Biol, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1HP7"}],"region_id":"DP03262r002","statement":[{"text":"The  first 18 residues were not visible in the electron density map.","type":"Results"},{"text":"The structure defined in this paper comprises residues 25-418","type":"Curator statement"},{"text":"he IDR characterized in the publication and spanning the N-terminal residues of the crystal structure corresponds to region 25-42 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-24) that is cleaved in the mature secreted protein.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-06T16:05:08.885Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":25,"end":43,"reference_id":"8543039","reference_source":"pmid","reference_html":"Crystal structure of an uncleaved alpha 1-antitrypsin reveals the conformation of its inhibitory reactive loop. <i> Song HK, Lee KN, Kwon KS, Yu MH, Suh SW. </i> FEBS Lett, 1995","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1KCT"}],"region_id":"DP03262r003","statement":[{"text":"The missing residues  are the N-terminal 19 residues, which are also missing in the starting model","type":"Results"},{"text":"The structure defined in this paper comprises residue 25-418","type":"Curator statement"},{"text":"The IDR characterized in the publication and spanning the N-terminal residues of the crystal structure corresponds to region 25-43 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-24) that is cleaved in the mature secreted protein.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-06T16:05:10.542Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2021_06","sequence":"MPSSVSWGILLLAGLCCLVPVSLAEDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins","Autophagy-related proteins"],"UniParc":"UPI000000CBEC","uniref100":"UniRef100_P01009","uniref90":"UniRef90_P01009","uniref50":"UniRef50_P01009","genes":[{"name":{"value":"SERPINA1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:8941","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8941"}}]},"synonyms":[{"value":"AAT"},{"value":"PI"}],"orfNames":[{"value":"PRO0684"},{"value":"PRO2209"}]}],"alphafold_very_low_content":0.10526315789473684,"disorder_content":0.05502392344497608,"disprot_consensus":{"full":[{"start":25,"end":47,"type":"D"}],"Structural state":[{"start":25,"end":47,"type":"D"}]}},{"disprot_id":"DP03263","acc":"O80358","creator":"jiserte","date":"2021-05-04T20:37:55.270Z","features":{"pfam":[{"id":"PF01149","name":"Formamidopyrimidine-DNA glycosylase N-terminal domain","start":1,"end":131},{"id":"PF06831","name":"Formamidopyrimidine-DNA glycosylase H2TH domain","start":146,"end":236},{"id":"PF21218","name":"Formamidopyrimidine-DNA glycosylase-like, C-terminal domain","start":240,"end":273}],"gene3D":[]},"length":390,"name":"Formamidopyrimidine-DNA glycosylase","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":86,"end":102,"reference_id":"22789755","reference_source":"pmid","reference_html":"Structural and biochemical studies of a plant formamidopyrimidine-DNA glycosylase reveal why eukaryotic Fpg glycosylases do not excise 8-oxoguanine. <i> Duclos S, Aller P, Jaruga P, Dizdaroglu M, Wallace SS, Doublié S. </i> DNA Repair (Amst), 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"jiserte","curator_name":"Javier Iserte","curator_orcid":"0000-0003-0056-1177","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3TWL"},{"db":"PDB","id":"3TWM"},{"db":"PDB","id":"3TWK"}],"region_id":"DP03263r006","statement":[{"text":"The final model, comprising residues 2 to 86, 101 to 261 and 268 to 286, was refined to an Rfree of 0.219 and RWork of 0.210 at 1.7 Å resolution.","type":"Results"},{"text":"From the description of the final model, it can be inferred that there is a disorder region from positions 87 to 100, however the region of missing residues in the pdb is from 86 to 102.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-04T07:49:40.044Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":6,"released":"2021_12","sequence":"MPELPEVEAARRAIEENCLGKKIKRVIIADDNKVIHGISPSDFQTSILGKTIISARRKGKNLWLELDSPPFPSFQFGMAGAIYIKGVAVTKYKRSAVKDSEEWPSKYSKFFVELDDGLELSFTDKRRFAKVRLLANPTSVSPISELGPDALLEPMTVDEFAESLAKKKITIKPLLLDQGYISGIGNWIADEVLYQARIHPLQTASSLSKEQCEALHTSIKEVIEKAVEVDADSSQFPSYWIFHNREKKPGKAFVDGKKIDFITAGGRTTAYVPELQKLYGKDAEKAAKVRPAKRGVKPKEDDGDGEEDEQETEKEDESAKSKKGQKPRGGRGKKPASKTKTEESDDDGDDSEAEEEVVKPKGRGTKPAIKRKSEEKATSQAGKKPKGRKS","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"dataset":[],"UniParc":"UPI000009E644","uniref100":"UniRef100_O80358","uniref90":"UniRef90_O80358","uniref50":"UniRef50_O80358","genes":[{"name":{"value":"FPG1"},"synonyms":[{"value":"FPG2"}],"orfNames":[{"value":"F6D8.28"}],"olnNames":[{"value":"At1g52500"}]}],"alphafold_very_low_content":0.24871794871794872,"disorder_content":0.04358974358974359,"disprot_consensus":{"full":[{"start":86,"end":102,"type":"D"}],"Structural state":[{"start":86,"end":102,"type":"D"}]}},{"disprot_id":"DP03265","acc":"O48963","creator":"jiserte","date":"2021-05-05T13:19:27.195Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":665,"end":952},{"id":"PF13426","name":"PAS domain","start":205,"end":301},{"id":"PF13426","name":"PAS domain","start":485,"end":577}],"gene3D":[]},"length":996,"name":"Phototropin-1","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":581,"end":592,"reference_id":"24316821","reference_source":"pmid","reference_html":"Coiled-coil dimerization of the LOV2 domain of the blue-light photoreceptor phototropin 1 from Arabidopsis thaliana. <i> Halavaty AS, Moffat K. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"jiserte","curator_name":"Javier Iserte","curator_orcid":"0000-0003-0056-1177","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"4HHD"}],"region_id":"DP03265r001","statement":[{"text":"In the AtLOV2 structure the disordered residues 581–592 of the junction\nin chain A and the partially ordered residues 580–586 in chain B\npresumably adopt a loop conformation","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-05T16:01:35.559Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_12","sequence":"MEPTEKPSTKPSSRTLPRDTRGSLEVFNPSTQLTRPDNPVFRPEPPAWQNLSDPRGTSPQPRPQQEPAPSNPVRSDQEIAVTTSWMALKDPSPETISKKTITAEKPQKSAVAAEQRAAEWGLVLKTDTKTGKPQGVGVRNSGGTENDPNGKKTTSQRNSQNSCRSSGEMSDGDVPGGRSGIPRVSEDLKDALSTFQQTFVVSDATKPDYPIMYASAGFFNMTGYTSKEVVGRNCRFLQGSGTDADELAKIRETLAAGNNYCGRILNYKKDGTSFWNLLTIAPIKDESGKVLKFIGMQVEVSKHTEGAKEKALRPNGLPESLIRYDARQKDMATNSVTELVEAVKRPRALSESTNLHPFMTKSESDELPKKPARRMSENVVPSGRRNSGGGRRNSMQRINEIPEKKSRKSSLSFMGIKKKSESLDESIDDGFIEYGEEDDEISDRDERPESVDDKVRQKEMRKGIDLATTLERIEKNFVITDPRLPDNPIIFASDSFLELTEYSREEILGRNCRFLQGPETDLTTVKKIRNAIDNQTEVTVQLINYTKSGKKFWNIFHLQPMRDQKGEVQYFIGVQLDGSKHVEPVRNVIEETAVKEGEDLVKKTAVNIDEAVRELPDANMTPEDLWANHSKVVHCKPHRKDSPPWIAIQKVLESGEPIGLKHFKPVKPLGSGDTGSVHLVELVGTDQLFAMKAMDKAVMLNRNKVHRARAEREILDLLDHPFLPALYASFQTKTHICLITDYYPGGELFMLLDRQPRKVLKEDAVRFYAAQVVVALEYLHCQGIIYRDLKPENVLIQGNGDISLSDFDLSCLTSCKPQLLIPSIDEKKKKKQQKSQQTPIFMAEPMRASNSFVGTEEYIAPEIISGAGHTSAVDWWALGILMYEMLYGYTPFRGKTRQKTFTNVLQKDLKFPASIPASLQVKQLIFRLLQRDPKKRLGCFEGANEVKQHSFFKGINWALIRCTNPPELETPIFSGEAENGEKVVDPELEDLQTNVF","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"dataset":[],"UniParc":"UPI00001303E1","uniref100":"UniRef100_O48963","uniref90":"UniRef90_O48963","uniref50":"UniRef50_O48963","genes":[{"name":{"value":"PHOT1"},"synonyms":[{"value":"JK224"},{"value":"NPH1"},{"value":"RPT1"}],"orfNames":[{"value":"T6D9_110"}],"olnNames":[{"value":"At3g45780"}]}],"alphafold_very_low_content":0.28815261044176704,"disorder_content":0.012048192771084338,"disprot_consensus":{"full":[{"start":581,"end":592,"type":"D"}],"Structural state":[{"start":581,"end":592,"type":"D"}]}},{"disprot_id":"DP03266","acc":"Q9M658","creator":"jiserte","date":"2021-05-05T13:42:13.896Z","features":{"pfam":[{"id":"PF25029","name":"MOM1-like domain","start":948,"end":1064}],"gene3D":[]},"length":2001,"name":"Helicase protein MOM1","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":1700,"end":1728,"reference_id":"22346760","reference_source":"pmid","reference_html":"Structural basis of transcriptional gene silencing mediated by Arabidopsis MOM1. <i> Nishimura T, Molinard G, Petty TJ, Broger L, Gabus C, Halazonetis TD, Thore S, Paszkowski J. </i> PLoS Genet, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"jiserte","curator_name":"Javier Iserte","curator_orcid":"0000-0003-0056-1177","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"3VEM"}],"region_id":"DP03266r001","statement":[{"text":"Residues 1700 to 1728 and 1811 to 1814 are\ndisordered or very poorly ordered in every CMM2 molecules. ","type":"Methods"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-05T15:41:45.211Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_12","sequence":"MKKDEKIGLTGRTIYTRSLAASIPASVEQETPGLRRSSRGTPSTKVITPASATRKSERLAPSPASVSKKSGGIVKNSTPSSLRRSNRGKTEVSLQSSKGSDNSIRKGDTSPDIEQRKDSVEESTDKIKPIMSARSYRALFRGKLKESEALVDASPNEEELVVVGCSRRIPAGNDDVQGKTDCPPPADAGSKRLPVDETSLDKGTDFPLKSVTETEKIVLDASPIVETGDDSVIGSPSENLETQKLQDGKTDCSPPANAESKTLPVGETSLEKEYPQKFQDDNTDCLPPANAESKRLPVGETSLEKDTDFPLKSTTETGKMVLYASPIVETRDDSVICSPSTNLETQKLLVSKTGLETDIVLPLKRKRDTAEIELDACATVANGDDHVMSSDGVIPSPSGCKNDNRPEMCNTCKKRQKVNGDCQNRSVCSCIVQPVEESDNVTQDMKETGPVTSREYEENGQIQHGKSSDPKFYSSVYPEYWVPVQLSDVQLEQYCQTLFSKSLSLSSLSKIDLGALEETLNSVRKTCDHPYVMDASLKQLLTKNLELHEILDVEIKASGKLHLLDKMLTHIKKNGLKAVVFYQATQTPEGLLLGNILEDFVGQRFGPKSYEHGIYSSKKNSAINNFNKESQCCVLLLETRACSQTIKLLRADAFILFGSSLNPSHDVKHVEKIKIESCSERTKIFRLYSVCTVEEKALILARQNKRQNKAVENLNRSLTHALLMWGASYLFDKLDHFHSSETPDSGVSFEQSIMDGVIHEFSSILSSKGGEENEVKLCLLLEAKHAQGTYSSDSTLFGEDHIKLSDEESPNIFWSKLLGGKNPMWKYPSDTPQRNRKRVQYFEGSEASPKTGDGGNAKKRKKASDDVTDPRVTDPPVDDDERKASGKDHMGALESPKVITLQSSCKSSGTDGTLDGNDAFGLYSMGSHISGIPEDMLASQDWGKIPDESQRRLHTVLKPKMAKLCQVLHLSDACTSMVGNFLEYVIENHRIYEEPATTFQAFQIALSWIAALLVKQILSHKESLVRANSELAFKCSRVEVDYIYSILSCMKSLFLEHTQGLQFDCFGTNSKQSVVSTKLVNESLSGATVRDEKINTKSMRNSSEDEECMTEKRCSHYSTATRDIEKTISGIKKKYKKQVQKLVQEHEEKKMELLNMYADKKQKLETSKSVEAAVIRITCSRTSTQVGDLKLLDHNYERKFDEIKSEKNECLKSLEQMHDVAKKKLAEDEACWINRIKSWAAKLKVCVPIQSGNNKHFSGSSNISQNAPDVQICNNANVEATYADTNCMASKVNQVPEAENTLGTMSGGSTQQVHEMVDVRNDETMDVSALSREQLTKSQSNEHASITVPEILIPADCQEEFAALNVHLSEDQNCDRITSAASDEDVSSRVPEVSQSLENLSASPEFSLNREEALVTTENRRTSHVGFDTDNILDQQNREDCSLDQEIPDELAMPVQHLASVVETRGAAESDQYGQDICPMPSSLAGKQPDPAANTESENLEEAIEPQSAGSETVETTDFAASHQGDQVTCPLLSSPTGNQPAPEANIEGQNINTSAEPHVAGPDAVESGDYAVIDQETMGAQDACSLPSGSVGTQSDLGANIEGQNVTTVAQLPTDGSDAVVTGGSPVSDQCAQDASPMPLSSPGNHPDTAVNIEGLDNTSVAEPHISGSDACEMEISEPGPQVERSTFANLFHEGGVEHSAGVTALVPSLLNNGTEQIAVQPVPQIPFPVFNDPFLHELEKLRRESENSKKTFEEKKSILKAELERKMAEVQAEFRRKFHEVEAEHNTRTTKIEKDKNLVIMNKLLANAFLSKCTDKKVSPSGAPRGKIQQLAQRAAQVSALRNYIAPQQLQASSFPAPALVSAPLQLQQSSFPAPGPAPLQPQASSFPSSVSRPSALLLNFAVCPMPQPRQPLISNIAPTPSVTPATNPGLRSPAPHLNSYRPSSSTPVATATPTSSVPPQALTYSAVSIQQQQEQQPQQSLSSGLQSNNEVVCLSDDE","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"dataset":[],"UniParc":"UPI000009DE23","uniref100":"UniRef100_Q9M658","uniref90":"UniRef90_Q9M658","uniref50":"UniRef50_Q9M658","genes":[{"name":{"value":"MOM1"},"synonyms":[{"value":"MOM"}],"orfNames":[{"value":"T6D22.14"}],"olnNames":[{"value":"At1g08060"}]}],"alphafold_very_low_content":0.6671664167916042,"disorder_content":0.014492753623188406,"disprot_consensus":{"full":[{"start":1700,"end":1728,"type":"D"}],"Structural state":[{"start":1700,"end":1728,"type":"D"}]}},{"disprot_id":"DP03267","acc":"Q9FIC3","creator":"jiserte","date":"2021-05-05T14:01:27.030Z","features":{"pfam":[{"id":"PF01722","name":"BolA-like protein","start":11,"end":77}],"gene3D":[]},"length":93,"name":"Protein BOLA2","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":75,"end":84,"reference_id":"25012657","reference_source":"pmid","reference_html":"Structural and spectroscopic insights into BolA-glutaredoxin complexes. <i> Roret T, Tsan P, Couturier J, Zhang B, Johnson MK, Rouhier N, Didierjean C. </i> J Biol Chem, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"jiserte","curator_name":"Javier Iserte","curator_orcid":"0000-0003-0056-1177","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03267r001","statement":[{"text":"The disordered region was not stated in the paper, but observed in the PDB structure (2MM9). It spans from the end of the sheet beta-3' to the beginning of helix alpha-4.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MVTKEQVEASLTSKLKPIHLEVIDISGGCGSSFEVEVVSEQFEGKRLLERHRMVNAALEEEMKEIHALSIKKAQTPQQWKPPSQDSATLTKDA","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"dataset":[],"UniParc":"UPI000000BF14","uniref100":"UniRef100_Q9FIC3","uniref90":"UniRef90_Q9FIC3","uniref50":"UniRef50_Q9FIC3","genes":[{"name":{"value":"BOLA2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"24203231","url":"http://www.ncbi.nlm.nih.gov/pubmed/24203231","alternativeUrl":"https://europepmc.org/abstract/MED/24203231"}}]},"orfNames":[{"value":"MYH9.4","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"BAB09404.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAB09404.1"}}]}],"olnNames":[{"value":"At5g09830","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT5G09830","url":""}}]}]}],"alphafold_very_low_content":0.06451612903225806,"disorder_content":0.10752688172043011,"disprot_consensus":{"full":[{"start":75,"end":84,"type":"D"}],"Structural state":[{"start":75,"end":84,"type":"D"}]}},{"disprot_id":"DP03268","acc":"Q682I1","creator":"jiserte","date":"2021-05-05T18:55:59.452Z","features":{"pfam":[{"id":"PF01722","name":"BolA-like protein","start":76,"end":155}],"gene3D":[]},"length":160,"name":"Protein BOLA1, chloroplastic","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":96,"end":108,"reference_id":"25012657","reference_source":"pmid","reference_html":"Structural and spectroscopic insights into BolA-glutaredoxin complexes. <i> Roret T, Tsan P, Couturier J, Zhang B, Johnson MK, Rouhier N, Didierjean C. </i> J Biol Chem, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"jiserte","curator_name":"Javier Iserte","curator_orcid":"0000-0003-0056-1177","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4PUG"}],"region_id":"DP03268r001","statement":[{"text":"All secondary structures are connected by short loops (1–4\nresidues) except the one situated between beta-1 and beta-2. This\nbeta1-beta2 loop that we refer to as [H/C] loop contains the histidine\nand cysteine residues from BolA_H and BolA_C groups,\nrespectively. In accordance with the existence of two groups,\nthe [H/C] loop can be formed by 11+/-6 (up to 20) residues in\nBolA_H members","type":"Results"},{"text":"Start and end position of the H/C were taken from PDB 4PUG.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MFSSSIRLIVSGFHRTQPLKSPVNSPSVFISVPKFFNSESKSTGTGSRSVAMSSVEKTGSDSGAIENRASRMREKLQKELEPVELVIEDVSYQHAGHAGMKGRTDDETHFNVKIVSKGFEGMNLVKRHRLVYHLLREELDTGLHALSIVSKTPSESPSKD","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"dataset":[],"UniParc":"UPI000034F4AC","uniref100":"UniRef100_Q682I1","uniref90":"UniRef90_Q682I1","uniref50":"UniRef50_Q682I1","genes":[{"name":{"value":"BOLA1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"24203231","url":"http://www.ncbi.nlm.nih.gov/pubmed/24203231","alternativeUrl":"https://europepmc.org/abstract/MED/24203231"}}]},"orfNames":[{"value":"F14J16","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AC002304","url":"https://www.ebi.ac.uk/ena/browser/view/AC002304"}}]}],"olnNames":[{"value":"At1g55805","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT1G55805","url":""}}]}]}],"alphafold_very_low_content":0.15,"disorder_content":0.08125,"disprot_consensus":{"full":[{"start":96,"end":108,"type":"D"}],"Structural state":[{"start":96,"end":108,"type":"D"}]}},{"disprot_id":"DP03269","acc":"Q9C552","creator":"jiserte","date":"2021-05-05T20:41:30.677Z","features":{"pfam":[{"id":"PF22493","name":"NOP9-like PUF repeat domain","start":126,"end":614}],"gene3D":[]},"length":753,"name":"Pumilio homolog 23","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":258,"end":270,"reference_id":"29036323","reference_source":"pmid","reference_html":"Structural basis for the specific recognition of 18S rRNA by APUM23. <i> Bao H, Wang N, Wang C, Jiang Y, Liu J, Xu L, Wu J, Shi Y. </i> Nucleic Acids Res, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jiserte","curator_name":"Javier Iserte","curator_orcid":"0000-0003-0056-1177","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5WZI"},{"db":"PDB","id":"5WZH"},{"db":"PDB","id":"5WZG"},{"db":"PDB","id":"5WZK"},{"db":"PDB","id":"5WZJ"}],"region_id":"DP03269r001","statement":[{"text":"A remarkable feature of the structure of APUM2385-655 is the unique characteristics of R3.\nThis PUF repeat contains 74 amino acid residues (residues\n213–286) and includes an insertion (residues 235–270; the\nelectron density of residues 258–270 was missing) located\nbetween the second and third helix. The insertion comprises\na disordered region and two short -helices (i1 and i2),\nlocated at the inner concave surface, that participate in the\nrecognition of RNA bases","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":258,"end":270,"reference_id":"29036323","reference_source":"pmid","reference_html":"Structural basis for the specific recognition of 18S rRNA by APUM23. <i> Bao H, Wang N, Wang C, Jiang Y, Liu J, Xu L, Wu J, Shi Y. </i> Nucleic Acids Res, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jiserte","curator_name":"Javier Iserte","curator_orcid":"0000-0003-0056-1177","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"5WZI"},{"db":"PDB","id":"5WZH"},{"db":"PDB","id":"5WZG"},{"db":"PDB","id":"5WZK"},{"db":"PDB","id":"5WZJ"}],"region_id":"DP03269r002","statement":[{"text":"A remarkable feature of the structure of APUM2385-655 is the unique characteristics of R3.\nThis PUF repeat contains 74 amino acid residues (residues\n213–286) and includes an insertion (residues 235–270; the\nelectron density of residues 258–270 was missing) located\nbetween the second and third helix. The insertion comprises\na disordered region and two short -helices (i1 and i2),\nlocated at the inner concave surface, that participate in the\nrecognition of RNA bases","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":2,"released":"2021_12","sequence":"MVSVGSKSLPSRRHRTIEEDSLMGERGKSSNNHSERNKGMRRKDHKGNRGFDVDSSKKNQSGGAPNVKPASKKHSEFEHQNQFVRKEIDPETSKYFSEIANLFDSNEVELEERSVICGNALEETRGREYEIATDYIISHVLQTLLEGCELDQLCSFIRNSASVFPAIAMDRSGSHVAESALKSLATHLENPDAYSVIEEALHSICKVIVDNPLDMMCNCYGSHVLRRLLCLCKGVSLDSPELYGAKSSKALAKRLNLKMSQLDDNNLEIPHQGFPGMLTYLLSGLLSCSREDMKYLQVDQYSSLVLQTALRLMLKQDEQLLEIIPLILRCNSTNKKVEGFHIETNVAKEILESMKDNSFSHLVEVILEVAPESLYNEMFNKVFKNSLFELSVDRCANFVIQALISHARDQEQMGIMWEELAPRFKDLLEQGKSGVVASLIAVSQRLQSHENKCCEALVGAVCSTNESRISILPRLLFLDYYFGCRDKSTWEWAPGAKMHVMGCLILQGIFKFSSDHIQPYITSLTSMKAEYITETAKDSSGARVIEAFLASDAATKQKRRLIIKLRGHFGELSLHTSGSFTVEKCFDACNLTLREAIASELLDVKVDLSKTKQGPYLLRKLDIDGYASRPDQWKSRQEAKQSTYNEFCSAFGSNKSNFPKNTFVSDASEDAAQEIEVKNTRKEIDHHPTSGFKRHREKHAKDKDEPFAGEKRSKQKKNKTSEATDKPKLAGSKRPFLSGEMTGKNRHSNKMRI","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"dataset":[],"UniParc":"UPI00000A5ECD","uniref100":"UniRef100_Q9C552","uniref90":"UniRef90_Q9C552","uniref50":"UniRef50_Q9C552","genes":[{"name":{"value":"APUM23"},"orfNames":[{"value":"T10D10.21"},{"value":"T9N14.7"}],"olnNames":[{"value":"At1g72320"}]}],"alphafold_very_low_content":0.25630810092961487,"disorder_content":0.017264276228419653,"disprot_consensus":{"full":[{"start":258,"end":270,"type":"D"}],"Structural state":[{"start":258,"end":270,"type":"D"}],"Molecular function":[{"start":258,"end":270,"type":"F"}]}},{"disprot_id":"DP03270","acc":"Q00958","creator":"jiserte","date":"2021-05-05T21:00:19.343Z","features":{"pfam":[{"id":"PF01698","name":"Floricaula / Leafy protein SAM domain","start":45,"end":123},{"id":"PF17538","name":"DNA Binding Domain (C-terminal) Leafy/Floricaula","start":225,"end":389}],"gene3D":[]},"length":420,"name":"Protein LEAFY","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":396,"end":420,"reference_id":"18784751","reference_source":"pmid","reference_html":"Structural basis for LEAFY floral switch function and similarity with helix-turn-helix proteins. <i> Hamès C, Ptchelkine D, Grimm C, Thevenon E, Moyroud E, Gérard F, Martiel JL, Benlloch R, Parcy F, Müller CW. </i> EMBO J, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"jiserte","curator_name":"Javier Iserte","curator_orcid":"0000-0003-0056-1177","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2VY2"},{"db":"PDB","id":"2VY1"}],"region_id":"DP03270r001","statement":[{"text":"Figure 2 Sequence alignments. (A) Aligned C-terminal amino-acid sequences of LFY (Arabidopsis thaliana, AAA32826), BgLFY (Brownea\ngrandiceps, AAS79888), FLO (Antirrhinum majus, P23915), NymodLFY (Nymphea odorata, AAF77609), WelLFY (Welwitschia mirabilis,\nAAF23870), MatstLFY (Matteuccia struthiopteris, AAF77608) and PpLFY1 (Physcomitrella patens, BAD91043). Identical and conservatively substituted residues are depicted on a grey ackground. Secondary structure elements are indicated. Residues involved in interactions with DNA bases and backbone are labelled with red and blue circles, respectively. Dashed bars indicate isordered regions in the crystal, blue rectangles indicate the residues involved in dimerization. Green triangles indicate the position of Arabidopsis mutations and residues divergent in PpLFY1 are highlighted in pink. (B) Two DNA duplexes containing the LEAFY-binding sites from AP1 and AG promoters present in the LEAFY–DNA complex crystals are depicted. Base pairs related by a dyad (indicated by a black dot) are highlighted in yellow.","type":"Figure"},{"text":"Figure 2 shows an alignment of LFY homologos. Positions 400 to 424 of LFY_ARATH are indicated as disoreded in the crystal, but positions numbers in the paper and the PDB do not correspond with Uniprot sequence. The corrected position numbers of the disordered region are 396 to 420.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-01T10:47:54.429Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MDPEGFTSGLFRWNPTRALVQAPPPVPPPLQQQPVTPQTAAFGMRLGGLEGLFGPYGIRFYTAAKIAELGFTASTLVGMKDEELEEMMNSLSHIFRWELLVGERYGIKAAVRAERRRLQEEEEEESSRRRHLLLSAAGDSGTHHALDALSQEGLSEEPVQQQDQTDAAGNNGGGGSGYWDAGQGKMKKQQQQRRRKKPMLTSVETDEDVNEGEDDDGMDNGNGGSGLGTERQREHPFIVTEPGEVARGKKNGLDYLFHLYEQCREFLLQVQTIAKDRGEKCPTKVTNQVFRYAKKSGASYINKPKMRHYVHCYALHCLDEEASNALRRAFKERGENVGSWRQACYKPLVNIACRHGWDIDAVFNAHPRLSIWYVPTKLRQLCHLERNNAVAAAAALVGGISCTGSSTSGRGGCGGDDLRF","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"dataset":[],"UniParc":"UPI00000010FA","uniref100":"UniRef100_Q00958","uniref90":"UniRef90_Q00958","uniref50":"UniRef50_Q00958","genes":[{"name":{"value":"LFY"},"orfNames":[{"value":"MAC9.18"}],"olnNames":[{"value":"At5g61850"}]}],"alphafold_very_low_content":0.32857142857142857,"disorder_content":0.05952380952380952,"disprot_consensus":{"full":[{"start":396,"end":420,"type":"D"}],"Structural state":[{"start":396,"end":420,"type":"D"}]}},{"disprot_id":"DP03271","acc":"P21580","creator":"fquaglia","date":"2021-05-06T08:42:59.420Z","features":{"pfam":[{"id":"PF01754","name":"A20-like zinc finger","start":386,"end":414},{"id":"PF01754","name":"A20-like zinc finger","start":476,"end":504},{"id":"PF01754","name":"A20-like zinc finger","start":605,"end":633},{"id":"PF01754","name":"A20-like zinc finger","start":655,"end":683},{"id":"PF01754","name":"A20-like zinc finger","start":760,"end":788},{"id":"PF02338","name":"OTU-like cysteine protease","start":98,"end":257}],"gene3D":[]},"length":790,"name":"Tumor necrosis factor alpha-induced protein 3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":150,"end":160,"reference_id":"31534238","reference_source":"pmid","reference_html":"Denisovan, modern human and mouse TNFAIP3 alleles tune A20 phosphorylation and immunity. <i> Zammit NW, Siggs OM, Gray PE, Horikawa K, Langley DB, Walters SN, Daley SR, Loetsch C, Warren J, Yap JY, Cultrone D, Russell A, Malle EK, Villanueva JE, Cowley MJ, Gayevskiy V, Dinger ME, Brink R, Zahra D, Chaudhri G, Karupiah G, Whittle B, Roots C, Bertram E, Yamada M, Jeelall Y, Enders A, Clifton BE, Mabbitt PD, Jackson CJ, Watson SR, Jenne CN, Lanier LL, Wiltshire T, Spitzer MH, Nolan GP, Schmitz F, Aderem A, Porebski BT, Buckle AM, Abbott DW, Ziegler JB, Craig ME, Benitez-Aguirre P, Teo J, Tangye SG, King C, Wong M, Cox MP, Phung W, Tang J, Sandoval W, Wertz IE, Christ D, Goodnow CC, Grey ST. </i> Nat Immunol, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5V3B"},{"db":"PDB","id":"5V3P"}],"region_id":"DP03271r001","statement":[{"text":"The β7–β8 loop itself is disordered in all available OTU structures but, like the disordered loops in the unliganded S1 ubiquitin-binding site, it may undergo conformational changes upon binding a cognate partner that are hindered by the I325N substitution.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T12:41:47.728Z"}},{"start":213,"end":228,"reference_id":"31534238","reference_source":"pmid","reference_html":"Denisovan, modern human and mouse TNFAIP3 alleles tune A20 phosphorylation and immunity. <i> Zammit NW, Siggs OM, Gray PE, Horikawa K, Langley DB, Walters SN, Daley SR, Loetsch C, Warren J, Yap JY, Cultrone D, Russell A, Malle EK, Villanueva JE, Cowley MJ, Gayevskiy V, Dinger ME, Brink R, Zahra D, Chaudhri G, Karupiah G, Whittle B, Roots C, Bertram E, Yamada M, Jeelall Y, Enders A, Clifton BE, Mabbitt PD, Jackson CJ, Watson SR, Jenne CN, Lanier LL, Wiltshire T, Spitzer MH, Nolan GP, Schmitz F, Aderem A, Porebski BT, Buckle AM, Abbott DW, Ziegler JB, Craig ME, Benitez-Aguirre P, Teo J, Tangye SG, King C, Wong M, Cox MP, Phung W, Tang J, Sandoval W, Wertz IE, Christ D, Goodnow CC, Grey ST. </i> Nat Immunol, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5V3B"},{"db":"PDB","id":"5V3P"}],"region_id":"DP03271r002","statement":[{"text":"The β7–β8 loop itself is disordered in all available OTU structures but, like the disordered loops in the unliganded S1 ubiquitin-binding site, it may undergo conformational changes upon binding a cognate partner that are hindered by the I325N substitution.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T12:41:45.631Z"}},{"start":152,"end":161,"reference_id":"17961127","reference_source":"pmid","reference_html":"Structure of the A20 OTU domain and mechanistic insights into deubiquitination. <i> Komander D, Barford D. </i> Biochem J, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2VFJ"}],"region_id":"DP03271r003","statement":[{"text":"In A20, two loops (residues 152-160 and 212-228) in this distal binding site are disordered despite high sequence conservation, and hence surface analysis in this region is not meaningful.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-24T14:24:48.203Z"}},{"start":213,"end":227,"reference_id":"17961127","reference_source":"pmid","reference_html":"Structure of the A20 OTU domain and mechanistic insights into deubiquitination. <i> Komander D, Barford D. </i> Biochem J, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2VFJ"}],"region_id":"DP03271r004","statement":[{"text":"In A20, two loops (residues 152-160 and 212-228) in this distal binding site are disordered despite high sequence conservation, and hence surface analysis in this region is not meaningful.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-24T14:23:24.520Z"}},{"start":213,"end":228,"reference_id":"27732584","reference_source":"pmid","reference_html":"Molecular basis of Lys11-polyubiquitin specificity in the deubiquitinase Cezanne. <i> Mevissen TET, Kulathu Y, Mulder MPC, Geurink PP, Maslen SL, Gersch M, Elliott PR, Burke JE, van Tol BDM, Akutsu M, Oualid FE, Kawasaki M, Freund SMV, Ovaa H, Komander D. </i> Nature, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5LRX"}],"region_id":"DP03271r005","statement":[{"text":"No large conformational changes occur upon Ub binding. However, two unstructured loops in A20 apo are stabilised by Ub, forming helix α6’ and the β2’-β2” sheet (compare Extended Data Fig. 2j).","type":"Supplementary material"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T12:44:43.290Z"}}],"regions_counter":5,"released":"2021_12","sequence":"MAEQVLPQALYLSNMRKAVKIRERTPEDIFKPTNGIIHHFKTMHRYTLEMFRTCQFCPQFREIIHKALIDRNIQATLESQKKLNWCREVRKLVALKTNGDGNCLMHATSQYMWGVQDTDLVLRKALFSTLKETDTRNFKFRWQLESLKSQEFVETGLCYDTRNWNDEWDNLIKMASTDTPMARSGLQYNSLEEIHIFVLCNILRRPIIVISDKMLRSLESGSNFAPLKVGGIYLPLHWPAQECYRYPIVLGYDSHHFVPLVTLKDSGPEIRAVPLVNRDRGRFEDLKVHFLTDPENEMKEKLLKEYLMVIEIPVQGWDHGTTHLINAAKLDEANLPKEINLVDDYFELVQHEYKKWQENSEQGRREGHAQNPMEPSVPQLSLMDVKCETPNCPFFMSVNTQPLCHECSERRQKNQNKLPKLNSKPGPEGLPGMALGASRGEAYEPLAWNPEESTGGPHSAPPTAPSPFLFSETTAMKCRSPGCPFTLNVQHNGFCERCHNARQLHASHAPDHTRHLDPGKCQACLQDVTRTFNGICSTCFKRTTAEASSSLSTSLPPSCHQRSKSDPSRLVRSPSPHSCHRAGNDAPAGCLSQAARTPGDRTGTSKCRKAGCVYFGTPENKGFCTLCFIEYRENKHFAAASGKVSPTASRFQNTIPCLGRECGTLGSTMFEGYCQKCFIEAQNQRFHEAKRTEEQLRSSQRRDVPRTTQSTSRPKCARASCKNILACRSEELCMECQHPNQRMGPGAHRGEPAPEDPPKQRCRAPACDHFGNAKCNGYCNECFQFKQMYG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins"],"UniParc":"UPI000000D92D","uniref100":"UniRef100_P21580","uniref90":"UniRef90_P21580","uniref50":"UniRef50_P21580","genes":[{"name":{"value":"TNFAIP3"},"synonyms":[{"value":"OTUD7C"}]}],"alphafold_very_low_content":0.24050632911392406,"disorder_content":0.035443037974683546,"disprot_consensus":{"full":[{"start":150,"end":161,"type":"D"},{"start":213,"end":228,"type":"T"}],"Structural state":[{"start":150,"end":161,"type":"D"},{"start":213,"end":228,"type":"D"}],"Structural transition":[{"start":213,"end":228,"type":"T"}]}},{"disprot_id":"DP03272","acc":"Q6GQQ9","creator":"fquaglia","date":"2021-05-06T08:55:09.940Z","features":{"pfam":[{"id":"PF01754","name":"A20-like zinc finger","start":801,"end":828},{"id":"PF02338","name":"OTU-like cysteine protease","start":190,"end":359},{"id":"PF28552","name":"OTUD7A/B, UBA domain","start":4,"end":53}],"gene3D":[]},"length":843,"name":"OTU domain-containing protein 7B","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":88,"end":129,"reference_id":"27732584","reference_source":"pmid","reference_html":"Molecular basis of Lys11-polyubiquitin specificity in the deubiquitinase Cezanne. <i> Mevissen TET, Kulathu Y, Mulder MPC, Geurink PP, Maslen SL, Gersch M, Elliott PR, Burke JE, van Tol BDM, Akutsu M, Oualid FE, Kawasaki M, Freund SMV, Ovaa H, Komander D. </i> Nature, 2016","date":"2022-08-04T08:34:14.421Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03272r001","statement":[{"text":"The first crystallised Cez apo construct (residues 88-438) contained an N-terminal flexible extension of 41 residues that was removed in subsequent crystallisation attempts for Cez apo and complexes.","type":"Methods"},{"text":"Electron density was not visible for the first 41 residues, which were removed from the construct for subsequent crystallisation attempts.","type":"Methods"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-04T14:45:46.011Z"}},{"start":267,"end":291,"reference_id":"27732584","reference_source":"pmid","reference_html":"Molecular basis of Lys11-polyubiquitin specificity in the deubiquitinase Cezanne. <i> Mevissen TET, Kulathu Y, Mulder MPC, Geurink PP, Maslen SL, Gersch M, Elliott PR, Burke JE, van Tol BDM, Akutsu M, Oualid FE, Kawasaki M, Freund SMV, Ovaa H, Komander D. </i> Nature, 2016","date":"2022-11-17T16:36:12.123Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03272r002","statement":[{"text":"To obtain crystals of Cez~Ub, the long, unstructured V-loop (residues 267-291) was replaced by the corresponding sequence in TRABID (Gln-Pro-Gly; QPG).","type":"Methods"}]}],"regions_counter":2,"released":"2023_12","sequence":"MTLDMDAVLSDFVRSTGAEPGLARDLLEGKNWDVNAALSDFEQLRQVHAGNLPPSFSEGSGGSRTPEKGFSDREPTRPPRPILQRQDDIVQEKRLSRGISHASSSIVSLARSHVSSNGGGGGSNEHPLEMPICAFQLPDLTVYNEDFRSFIERDLIEQSMLVALEQAGRLNWWVSVDPTSQRLLPLATTGDGNCLLHAASLGMWGFHDRDLMLRKALYALMEKGVEKEALKRRWRWQQTQQNKESGLVYTEDEWQKEWNELIKLASSEPRMHLGTNGANCGGVESSEEPVYESLEEFHVFVLAHVLRRPIVVVADTMLRDSGGEAFAPIPFGGIYLPLEVPASQCHRSPLVLAYDQAHFSALVSMEQKENTKEQAVIPLTDSEYKLLPLHFAVDPGKGWEWGKDDSDNVRLASVILSLEVKLHLLHSYMNVKWIPLSSDAQAPLAQPESPTASAGDEPRSTPESGDSDKESVGSSSTSNEGGRRKEKSKRDREKDKKRADSVANKLGSFGKTLGSKLKKNMGGLMHSKGSKPGGVGTGLGGSSGTETLEKKKKNSLKSWKGGKEEAAGDGPVSEKPPAESVGNGGSKYSQEVMQSLSILRTAMQGEGKFIFVGTLKMGHRHQYQEEMIQRYLSDAEERFLAEQKQKEAERKIMNGGIGGGPPPAKKPEPDAREEQPTGPPAESRAMAFSTGYPGDFTIPRPSGGGVHCQEPRRQLAGGPCVGGLPPYATFPRQCPPGRPYPHQDSIPSLEPGSHSKDGLHRGALLPPPYRVADSYSNGYREPPEPDGWAGGLRGLPPTQTKCKQPNCSFYGHPETNNFCSCCYREELRRREREPDGELLVHRF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000020415D","uniref100":"UniRef100_Q6GQQ9","uniref90":"UniRef90_Q6GQQ9","uniref50":"UniRef50_Q6GQQ9","genes":[{"name":{"value":"OTUD7B"},"synonyms":[{"value":"ZA20D1"}]}],"alphafold_very_low_content":0.4246737841043891,"disorder_content":0.07947805456702253,"disprot_consensus":{"full":[{"start":88,"end":129,"type":"D"},{"start":267,"end":291,"type":"D"}],"Structural state":[{"start":88,"end":129,"type":"D"},{"start":267,"end":291,"type":"D"}]}},{"disprot_id":"DP03273","acc":"Q99835","creator":"fquaglia","date":"2021-05-06T10:09:04.270Z","features":{"pfam":[{"id":"PF01392","name":"Fz domain","start":70,"end":170},{"id":"PF01534","name":"Frizzled/Smoothened family membrane region","start":221,"end":551}],"gene3D":[]},"length":787,"name":"Smoothened homolog","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":539,"end":640,"reference_id":"32929279","reference_source":"pmid","reference_html":"Sterols in an intramolecular channel of Smoothened mediate Hedgehog signaling. <i> Qi X, Friedberg L, De Bose-Boyd R, Long T, Li X. </i> Nat Chem Biol, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6XBJ"},{"db":"PDB","id":"6XBL"}],"region_id":"DP03273r001","statement":[{"text":"The residues 539–644 were not observed in the cryo-EM map, suggesting high flexibility of this region.","type":"Introduction"}],"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-24T17:59:10.405Z"}}],"regions_counter":1,"released":"2021_12","sequence":"MAAARPARGPELPLLGLLLLLLLGDPGRGAASSGNATGPGPRSAGGSARRSAAVTGPPPPLSHCGRAAPCEPLRYNVCLGSVLPYGATSTLLAGDSDSQEEAHGKLVLWSGLRNAPRCWAVIQPLLCAVYMPKCENDRVELPSRTLCQATRGPCAIVERERGWPDFLRCTPDRFPEGCTNEVQNIKFNSSGQCEVPLVRTDNPKSWYEDVEGCGIQCQNPLFTEAEHQDMHSYIAAFGAVTGLCTLFTLATFVADWRNSNRYPAVILFYVNACFFVGSIGWLAQFMDGARREIVCRADGTMRLGEPTSNETLSCVIIFVIVYYALMAGVVWFVVLTYAWHTSFKALGTTYQPLSGKTSYFHLLTWSLPFVLTVAILAVAQVDGDSVSGICFVGYKNYRYRAGFVLAPIGLVLIVGGYFLIRGVMTLFSIKSNHPGLLSEKAASKINETMLRLGIFGFLAFGFVLITFSCHFYDFFNQAEWERSFRDYVLCQANVTIGLPTKQPIPDCEIKNRPSLLVEKINLFAMFGTGIAMSTWVWTKATLLIWRRTWCRLTGQSDDEPKRIKKSKMIAKAFSKRHELLQNPGQELSFSMHTVSHDGPVAGLAFDLNEPSADVSSAWAQHVTKMVARRGAILPQDISVTPVATPVPPEEQANLWLVEAEISPELQKRLGRKKKRRKRKKEVCPLAPPPELHPPAPAPSTIPRLPQLPRQKCLVAAGAWGAGDSCRQGAWTLVSNPFCPEPSPPQDPFLPSAPAPVAWAHGRRQGLGPIHSRTNLMDTELMDADSDF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins","NDDs-related proteins"],"UniParc":"UPI0000050447","uniref100":"UniRef100_Q99835","uniref90":"UniRef90_Q99835","uniref50":"UniRef50_Q99835","genes":[{"name":{"value":"SMO"},"synonyms":[{"value":"SMOH"}]}],"alphafold_very_low_content":0.2795425667090216,"disorder_content":0.12960609911054638,"disprot_consensus":{"full":[{"start":539,"end":640,"type":"D"}],"Structural state":[{"start":539,"end":640,"type":"D"}]}},{"disprot_id":"DP03274","acc":"Q9Y4K0","creator":"rpancsa","date":"2021-05-06T13:34:15.116Z","features":{"pfam":[{"id":"PF00530","name":"Scavenger receptor cysteine-rich domain","start":65,"end":159},{"id":"PF00530","name":"Scavenger receptor cysteine-rich domain","start":202,"end":301},{"id":"PF00530","name":"Scavenger receptor cysteine-rich domain","start":330,"end":425},{"id":"PF00530","name":"Scavenger receptor cysteine-rich domain","start":439,"end":544},{"id":"PF01186","name":"Lysyl oxidase","start":548,"end":746}],"gene3D":[]},"length":774,"name":"Lysyl oxidase homolog 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":763,"end":774,"reference_id":"29581294","reference_source":"pmid","reference_html":"Crystal structure of human lysyl oxidase-like 2 (hLOXL2) in a precursor state. <i> Zhang X, Wang Q, Wu J, Wang J, Shi Y, Liu M. </i> Proc Natl Acad Sci U S A, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":2,"cross_refs":[{"db":"PDB","id":"5ZE3"}],"region_id":"DP03274r001","statement":[{"text":"Crystals of hLOXL2 (residues 318–774 with N455Q) were grown at 18 °C using the hanging-drop vapor-diffusion method.","type":"Methods"},{"text":"The atomic model comprising residues 322–762 was built and refined to 2.4-Å resolution.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-10T13:04:39.344Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_06","sequence":"MERPLCSHLCSCLAMLALLSPLSLAQYDSWPHYPEYFQQPAPEYHQPQAPANVAKIQLRLAGQKRKHSEGRVEVYYDGQWGTVCDDDFSIHAAHVVCRELGYVEAKSWTASSSYGKGEGPIWLDNLHCTGNEATLAACTSNGWGVTDCKHTEDVGVVCSDKRIPGFKFDNSLINQIENLNIQVEDIRIRAILSTYRKRTPVMEGYVEVKEGKTWKQICDKHWTAKNSRVVCGMFGFPGERTYNTKVYKMFASRRKQRYWPFSMDCTGTEAHISSCKLGPQVSLDPMKNVTCENGLPAVVSCVPGQVFSPDGPSRFRKAYKPEQPLVRLRGGAYIGEGRVEVLKNGEWGTVCDDKWDLVSASVVCRELGFGSAKEAVTGSRLGQGIGPIHLNEIQCTGNEKSIIDCKFNAESQGCNHEEDAGVRCNTPAMGLQKKLRLNGGRNPYEGRVEVLVERNGSLVWGMVCGQNWGIVEAMVVCRQLGLGFASNAFQETWYWHGDVNSNKVVMSGVKCSGTELSLAHCRHDGEDVACPQGGVQYGAGVACSETAPDLVLNAEMVQQTTYLEDRPMFMLQCAMEENCLSASAAQTDPTTGYRRLLRFSSQIHNNGQSDFRPKNGRHAWIWHDCHRHYHSMEVFTHYDLLNLNGTKVAEGHKASFCLEDTECEGDIQKNYECANFGDQGITMGCWDMYRHDIDCQWVDITDVPPGDYLFQVVINPNFEVAESDYSNNIMKCRSRYDGHRIWMYNCHIGGSFSEETEKKFEHFSGLLNNQLSPQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000012E7AB","uniref100":"UniRef100_Q9Y4K0","uniref90":"UniRef90_Q9Y4K0","uniref50":"UniRef50_Q9Y4K0","genes":[{"name":{"value":"LOXL2"}}],"alphafold_very_low_content":0.07235142118863049,"disorder_content":0.015503875968992248,"disprot_consensus":{"full":[{"start":763,"end":774,"type":"D"}],"Structural state":[{"start":763,"end":774,"type":"D"}]}},{"disprot_id":"DP03275","acc":"Q15276","creator":"fquaglia","date":"2021-05-06T13:57:29.544Z","features":{"pfam":[{"id":"PF03528","name":"Rabaptin","start":9,"end":495},{"id":"PF09311","name":"Rabaptin-like protein","start":533,"end":839}],"gene3D":[]},"length":862,"name":"Rab GTPase-binding effector protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":642,"end":661,"reference_id":"15457209","reference_source":"pmid","reference_html":"Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5. <i> Zhu G, Zhai P, He X, Wakeham N, Rodgers K, Li G, Tang J, Zhang XC. </i> EMBO J, 2004","date":"2022-06-25T21:05:18.122Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":2,"cross_refs":[{"db":"PDB","id":"1X79"}],"region_id":"DP03275r001","statement":[{"text":"The region of residues visible in the GAT–Rabaptin5 complex crystal is represented with capital letters, and mobile residues are in lowercase letters.","type":"Figure"}],"ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UJY5"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"42106","entry_name":"L-1,4-dithiothreitol"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T12:40:53.915Z"}}],"regions_counter":1,"released":"2022_06","sequence":"MAQPGPASQPDVSLQQRVAELEKINAEFLRAQQQLEQEFNQKRAKFKELYLAKEEDLKRQNAVLQAAQDDLGHLRTQLWEAQAEMENIKAIATVSENTKQEAIDEVKRQWREEVASLQAVMKETVRDYEHQFHLRLEQERTQWAQYRESAEREIADLRRRLSEGQEEENLENEMKKAQEDAEKLRSVVMPMEKEIAALKDKLTEAEDKIKELEASKVKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMEIVLTSEQLRQVEELKKKDQEDDEQQRLNKRKDHKKADVEEEIKIPVVCALTQEESSAQLSNEEEHLDSTRGSVHSLDAGLLLPSGDPFSKSDNDMFKDGLRRAQSTDSLGTSGSLQSKALGYNYKAKSAGNLDESDFGPLVGADSVSENFDTASLGSLQMPSGFMLTKDQERAIKAMTPEQEETASLLSSVTQGMESAYVSPSGYRLVSETEWNLLQKEVHNAGNKLGRRCDMCSNYEKQLQGIQIQEAETRDQVKKLQLMLRQANDQLEKTMKDKQELEDFIKQSSEDSSHQISALVLRAQASEILLEELQQGLSQAKRDVQEQMAVLMQSREQVSEELVRLQKDNDSLQGKHSLHVSLQQAEDFILPDTTEALRELVLKYREDIINVRTAADHVEEKLKAEILFLKEQIQAEQCLKENLEETLQLEIENCKEEIASISSLKAELERIKVEKGQLESTLREKSQQLESLQEIKISLEEQLKKETAAKATVEQLMFEEKNKAQRLQTELDVSEQVQRDFVKLSQTLQVQLERIRQADSLERIRAILNDTKLTDINQLPET","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins"],"UniParc":"UPI0000038DA4","uniref100":"UniRef100_Q15276","uniref90":"UniRef90_Q15276","uniref50":"UniRef50_Q15276","genes":[{"name":{"value":"RABEP1"},"synonyms":[{"value":"RAB5EP"},{"value":"RABPT5"},{"value":"RABPT5A"}]}],"alphafold_very_low_content":0.18677494199535963,"disorder_content":0.02320185614849188,"disprot_consensus":{"full":[{"start":642,"end":661,"type":"D"}],"Structural state":[{"start":642,"end":661,"type":"D"}]}},{"disprot_id":"DP03276","acc":"Q96PU8","creator":"fquaglia","date":"2021-05-06T14:24:23.674Z","features":{"pfam":[{"id":"PF16544","name":"Homodimerisation region of STAR domain protein","start":10,"end":62},{"id":"PF16551","name":"Putative nuclear localisation signal of quaking","start":312,"end":341},{"id":"PF22675","name":"KHDC4/BBP-like, KH-domain type I","start":92,"end":179}],"gene3D":[]},"length":341,"name":"Protein quaking","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":205,"end":214,"reference_id":"23630077","reference_source":"pmid","reference_html":"Structure-function studies of STAR family Quaking proteins bound to their in vivo RNA target sites. <i> Teplova M, Hafner M, Teplov D, Essig K, Tuschl T, Patel DJ. </i> Genes Dev, 2013","date":"2022-06-27T14:14:15.853Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":4,"cross_refs":[{"db":"PDB","id":"4JVH"}],"region_id":"DP03276r001","statement":[{"text":"The five N-terminal and 10 C-terminal residues and segments 32–39 and 61–68 were disordered in the crystal.","type":"Methods"}],"ec_go":"EXP","disprot_namespace":"Structural state","construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":21,"end":21,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":24,"end":24,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":30,"end":30,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":58,"end":58,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":124,"end":124,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":131,"end":131,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":194,"end":194,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":197,"end":197,"position":"Specific residue"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interactin RNA with sequence UUCACUAACAA"}]}]}],"regions_counter":1,"released":"2021_12","sequence":"MVGEMETKEKPKPTPDYLMQLMNDKKLMSSLPNFCGIFNHLERLLDEEISRVRKDMYNDTLNGSTEKRSAELPDAVGPIVQLQEKLYVPVKEYPDFNFVGRILGPRGLTAKQLEAETGCKIMVRGKGSMRDKKKEEQNRGKPNWEHLNEDLHVLITVEDAQNRAEIKLKRAVEEVKKLLVPAAEGEDSLKKMQLMELAILNGTYRDANIKSPALAFSLAATAQAAPRIITGPAPVLPPAALRTPTPAGPTIMPLIRQIQTAVMPNGTPHPTAAIVPPGPEAGLIYTPYEYPYTLAPATSILEYPIEPSGVLGAVATKVRRHDMRVHPYQRIVTADRAATGN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins"],"UniParc":"UPI0000029EBD","uniref100":"UniRef100_Q96PU8","uniref90":"UniRef90_Q96PU8","uniref50":"UniRef50_Q96PU8","genes":[{"name":{"value":"QKI"},"synonyms":[{"value":"HKQ"}]}],"alphafold_very_low_content":0.3460410557184751,"disorder_content":0.02932551319648094,"disprot_consensus":{"full":[{"start":205,"end":214,"type":"D"}],"Structural state":[{"start":205,"end":214,"type":"D"}]}},{"disprot_id":"DP03277","acc":"Q61001","creator":"rpancsa","date":"2021-05-06T20:36:47.946Z","features":{"pfam":[{"id":"PF00052","name":"Laminin B (Domain IV)","start":1694,"end":1830},{"id":"PF00053","name":"Laminin EGF domain","start":305,"end":352},{"id":"PF00053","name":"Laminin EGF domain","start":364,"end":427},{"id":"PF00053","name":"Laminin EGF domain","start":434,"end":475},{"id":"PF00053","name":"Laminin EGF domain","start":500,"end":541},{"id":"PF00053","name":"Laminin EGF domain","start":547,"end":588},{"id":"PF00053","name":"Laminin EGF domain","start":593,"end":634},{"id":"PF00053","name":"Laminin EGF domain","start":638,"end":679},{"id":"PF00053","name":"Laminin EGF domain","start":683,"end":731},{"id":"PF00053","name":"Laminin EGF domain","start":782,"end":827},{"id":"PF00053","name":"Laminin EGF domain","start":834,"end":872},{"id":"PF00053","name":"Laminin EGF domain","start":1443,"end":1491},{"id":"PF00053","name":"Laminin EGF domain","start":1533,"end":1578},{"id":"PF00053","name":"Laminin EGF domain","start":1582,"end":1630},{"id":"PF00053","name":"Laminin EGF domain","start":1831,"end":1855},{"id":"PF00053","name":"Laminin EGF domain","start":1915,"end":1968},{"id":"PF00053","name":"Laminin EGF domain","start":1971,"end":2022},{"id":"PF00053","name":"Laminin EGF domain","start":2025,"end":2069},{"id":"PF00053","name":"Laminin EGF domain","start":2072,"end":2119},{"id":"PF00055","name":"Laminin N-terminal (Domain VI)","start":51,"end":303},{"id":"PF02210","name":"Laminin G domain","start":2786,"end":2909},{"id":"PF02210","name":"Laminin G domain","start":2975,"end":3100},{"id":"PF02210","name":"Laminin G domain","start":3157,"end":3272},{"id":"PF02210","name":"Laminin G domain","start":3372,"end":3496},{"id":"PF02210","name":"Laminin G domain","start":3547,"end":3669},{"id":"PF06008","name":"Laminin Domain I","start":2194,"end":2452},{"id":"PF24973","name":"Laminin/attractin EGF domain","start":1865,"end":1907}],"gene3D":[]},"length":3718,"name":"Laminin subunit alpha-5","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":70,"end":119,"reference_id":"21311558","reference_source":"pmid","reference_html":"Determinants of laminin polymerization revealed by the structure of the α5 chain amino-terminal region. <i> Hussain SA, Carafoli F, Hohenester E. </i> EMBO Rep, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":2,"cross_refs":[{"db":"PDB","id":"2Y38"}],"region_id":"DP03277r001","statement":[{"text":"Residues 70–119—another insertion into the jelly-roll motif—are disordered in the a5LN–LEa1–2 structure. The disordered region contains four conserved cysteines, but otherwise its sequence is highly variable in the LN domain superfamily","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-10T14:05:22.825Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_06","sequence":"MAKRGGQLCAGSAPGALGPRSPAPRPLLLLLAGLALVGEARTPGGDGFSLHPPYFNLAEGARITASATCGEEAPTRSVSRPTEDLYCKLVGGPVAGGDPNQTIQGQYCDICTAANSNKAHPVSNAIDGTERWWQSPPLSRGLEYNEVNVTLDLGQVFHVAYVLIKFANSPRPDLWVLERSTDFGHTYQPWQFFASSKRDCLERFGPRTLERITQDDDVICTTEYSRIVPLENGEIVVSLVNGRPGALNFSYSPLLRDFTKATNIRLRFLRTNTLLGHLMGKALRDPTVTRRYYYSIKDISIGGRCVCHGHADVCDAKDPLDPFRLQCACQHNTCGGSCDRCCPGFNQQPWKPATTDSANECQSCNCHGHAYDCYYDPEVDRRNASQNQDNVYQGGGVCLDCQHHTTGINCERCLPGFFRAPDQPLDSPHVCRPCDCESDFTDGTCEDLTGRCYCRPNFTGELCAACAEGYTDFPHCYPLPSFPHNDTREQVLPAGQIVNCDCNAAGTQGNACRKDPRLGRCVCKPNFRGAHCELCAPGFHGPSCHPCQCSSPGVANSLCDPESGQCMCRTGFEGDRCDHCALGYFHFPLCQLCGCSPAGTLPEGCDEAGRCQCRPGFDGPHCDRCLPGYHGYPDCHACACDPRGALDQQCGVGGLCHCRPGYTGATCQECSPGFYGFPSCIPCHCSADGSLHTTCDPTTGQCRCRPRVTGLHCDMCVPGAYNFPYCEAGSCHPAGLAPANPALPETQAPCMCRAHVEGPSCDRCKPGYWGLSASNPEGCTRCSCDPRGTLGGVTECQGNGQCFCKAHVCGKTCAACKDGFFGLDYADYFGCRSCRCDVGGALGQGCEPKTGACRCRPNTQGPTCSEPAKDHYLPDLHHMRLELEEAATPEGHAVRFGFNPLEFENFSWRGYAHMMAIQPRIVARLNVTSPDLFRLVFRYVNRGSTSVNGQISVREEGKLSSCTNCTEQSQPVAFPPSTEPAFVTVPQRGFGEPFVLNPGIWALLVEAEGVLLDYVVLLPSTYYEAALLQHRVTEACTYRPSALHSTENCLVYAHLPLDGFPSAAGTEALCRHDNSLPRPCPTEQLSPSHPPLATCFGSDVDIQLEMAVPQPGQYVLVVEYVGEDSHQEMGVAVHTPQRAPQQGVLNLHPCPYSSLCRSPARDTQHHLAIFYLDSEASIRLTAEQAHFFLHSVTLVPVEEFSTEFVEPRVFCVSSHGTFNPSSAACLASRFPKPPQPIILKDCQVLPLPPDLPLTQSQELSPGAPPEGPQPRPPTAVDPNAEPTLLRHPQGTVVFTTQVPTLGRYAFLLHGYQPVHPSFPVEVLINGGRIWQGHANASFCPHGYGCRTLVLCEGQTMLDVTDNELTVTVRVPEGRWLWLDYVLIVPEDAYSSSYLQEEPLDKSYDFISHCATQGYHISPSSSSPFCRNAATSLSLFYNNGALPCGCHEVGAVSPTCEPFGGQCPCRGHVIGRDCSRCATGYWGFPNCRPCDCGARLCDELTGQCICPPRTVPPDCLVCQPQSFGCHPLVGCEECNCSGPGVQELTDPTCDMDSGQCRCRPNVAGRRCDTCAPGFYGYPSCRPCDCHEAGTMASVCDPLTGQCHCKENVQGSRCDQCRVGTFSLDAANPKGCTRCFCFGATERCGNSNLARHEFVDMEGWVLLSSDRQVVPHEHRPEIELLHADLRSVADTFSELYWQAPPSYLGDRVSSYGGTLHYELHSETQRGDIFIPYESRPDVVLQGNQMSIAFLELAYPPPGQVHRGQLQLVEGNFRHLETHNPVSREELMMVLAGLEQLQIRALFSQTSSSVSLRRVVLEVASEAGRGPPASNVELCMCPANYRGDSCQECAPGYYRDTKGLFLGRCVPCQCHGHSDRCLPGSGICVGCQHNTEGDQCERCRPGFVSSDPSNPASPCVSCPCPLAVPSNNFADGCVLRNGRTQCLCRPGYAGASCERCAPGFFGNPLVLGSSCQPCDCSGNGDPNMIFSDCDPLTGACRGCLRHTTGPHCERCAPGFYGNALLPGNCTRCDCSPCGTETCDPQSGRCLCKAGVTGQRCDRCLEGYFGFEQCQGCRPCACGPAAKGSECHPQSGQCHCQPGTTGPQCLECAPGYWGLPEKGCRRCQCPRGHCDPHTGHCTCPPGLSGERCDTCSQQHQVPVPGKPGGHGIHCEVCDHCVVLLLDDLERAGALLPAIREQLQGINASSAAWARLHRLNASIADLQSKLRSPPGPRYQAAQQLQTLEQQSISLQQDTERLGSQATGVQGQAGQLLDTTESTLGRAQKLLESVRAVGRALNELASRMGQGSPGDALVPSGEQLRWALAEVERLLWDMRTRDLGAQGAVAEAELAEAQRLMARVQEQLTSFWEENQSLATHIRDQLAQYESGLMDLREALNQAVNTTREAEELNSRNQERLKEALQWKQELSQDNATLKATLQAASLILGHVSELLQGIDQAKEDLEHLAASLDGAWTPLLKRMQAFSPASSKVDLVEAAEAHAQKLNQLAINLSGIILGINQDRFIQRAVEASNAYSSILQAVQAAEDAAGQALRQASRTWEMVVQRGLAAGARQLLANSSALEETILGHQGRLGLAQGRLQAAGIQLHNVWARKNQLAAQIQEAQAMLAMDTSETSEKIAHAKAVAAEALSTATHVQSQLQGMQKNVERWQSQLGGLQGQDLSQVERDASSSVSTLEKTLPQLLAKLSRLENRGVHNASLALSANIGRVRKLIAQARSAASKVKVSMKFNGRSGVRLRTPRDLADLAAYTALKFHIQSPVPAPEPGKNTGDHFVLYMGSRQATGDYMGVSLRNQKVHWVYRLGKAGPTTLSIDENIGEQFAAVSIDRTLQFGHMSVTVEKQMVHEIKGDTVAPGSEGLLNLHPDDFVFYVGGYPSNFTPPEPLRFPGYLGCIEMETLNEEVVSLYNFEQTFMLDTAVDKPCARSKATGDPWLTDGSYLDGSGFARISFEKQFSNTKRFDQELRLVSYNGIIFFLKQESQFLCLAVQEGTLVLFYDFGSGLKKADPLQPPQALTAASKAIQVFLLAGNRKRVLVRVERATVFSVDQDNMLEMADAYYLGGVPPEQLPLSLRQLFPSGGSVRGCIKGIKALGKYVDLKRLNTTGISFGCTADLLVGRTMTFHGHGFLPLALPDVAPITEVVYSGFGFRGTQDNNLLYYRTSPDGPYQVSLREGHVTLRFMNQEVETQRVFADGAPHYVAFYSNVTGVWLYVDDQLQLVKSHERTTPMLQLQPEEPSRLLLGGLPVSGTFHNFSGCISNVFVQRLRGPQRVFDLHQNMGSVNVSVGCTPAQLIETSRATAQKVSRRSRQPSQDLACTTPWLPGTIQDAYQFGGPLPSYLQFVGISPSHRNRLHLSMLVRPHAASQGLLLSTAPMSGRSPSLVLFLNHGHFVAQTEGPGPRLQVQSRQHSRAGQWHRVSVRWGMQQIQLVVDGSQTWSQKALHHRVPRAERPQPYTLSVGGLPASSYSSKLPVSVGFSGCLKKLQLDKRPLRTPTQMVGVTPCVSGPLEDGLFFPGSEGVVTLELPKAKMPYVSLELEMRPLAAAGLIFHLGQALATPYMQLKVLTEQVLLQANDGAGEFSTWVTYPKLCDGRWHRVAVIMGRDTLRLEVDTQSNHTTGRLPESLAGSPALLHLGSLPKSSTARPELPAYRGCLRKLLINGAPVNVTASVQIQGAVGMRGCPSGTLALSKQGKALTQRQAKPSVSPLLWH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000528BA8","uniref100":"UniRef100_Q61001","uniref90":"UniRef90_Q61001","uniref50":"UniRef50_Q61001","genes":[{"name":{"value":"Lama5"}}],"disorder_content":0.013448090371167294,"disprot_consensus":{"full":[{"start":70,"end":119,"type":"D"}],"Structural state":[{"start":70,"end":119,"type":"D"}]}},{"disprot_id":"DP03278","acc":"P18065","creator":"grivas","date":"2021-05-07T08:20:42.229Z","features":{"pfam":[{"id":"PF00086","name":"Thyroglobulin type-1 repeat","start":227,"end":306},{"id":"PF00219","name":"Insulin-like growth factor binding protein","start":42,"end":111}],"gene3D":[]},"length":325,"name":"Insulin-like growth factor-binding protein 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":312,"end":325,"reference_id":"17020769","reference_source":"pmid","reference_html":"Structure, dynamics and heparin binding of the C-terminal domain of insulin-like growth factor-binding protein-2 (IGFBP-2). <i> Kuang Z, Yao S, Keizer DW, Wang CC, Bach LA, Forbes BE, Wallace JC, Norton RS. </i> J Mol Biol, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2H7T"}],"region_id":"DP03278r001","statement":[{"text":"C-BP-2 has a longer disordered loop I, and an extended C-terminal tail, which is unstructured and very mobile.","type":"Abstract"},{"text":"The last 14 residues, 276–289, are unstructured.","type":"Results"},{"text":"Another noticeable feature of the C-BP-2 sequence relative to other IGFBP C- domains is its 11–13 residue extended C-terminal tail (Figure 2(e)). The solution structure of C-BP-2 shows clearly that this extended C-terminal tail is unstructured (Figure 1(a)).","type":"Results"},{"text":"Residues in the C-terminal tail beyond Gln277 exhibit J(0.87ωH) >15 ps rad- 1 and thus have even greater flexibility.","type":"Results"},{"text":"A possible explanation for the anomalously higher R2 values and the failure in fitting the relaxation parameters is that the motions of the core of C-BP-2 cannot be described by a simple anisotropic tumbling model with a unique diffusion tensor. This is probably a consequence of the presence of a longer and very flexible C-terminal tail, together with a longer disordered loop compared to C-BP-6.","type":"Discussion"},{"text":"The IDR characterized in the publication and spanning residues 276-289 corresponds to region 312-325 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-35).","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-10T14:20:50.492Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":5,"released":"2021_06","sequence":"MLPRVGCPALPLPPPPLLPLLLLLLGASGGGGGARAEVLFRCPPCTPERLAACGPPPVAPPAAVAAVAGGARMPCAELVREPGCGCCSVCARLEGEACGVYTPRCGQGLRCYPHPGSELPLQALVMGEGTCEKRRDAEYGASPEQVADNGDDHSEGGLVENHVDSTMNMLGGGGSAGRKPLKSGMKELAVFREKVTEQHRQMGKGGKHHLGLEEPKKLRPPPARTPCQQELDQVLERISTMRLPDERGPLEHLYSLHIPNCDKHGLYNLKQCKMSLNGQRGECWCVNPNTGKLIQGAPTIRGDPECHLFYNEQQEARGVHTQRMQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000012D112","uniref100":"UniRef100_P18065","uniref90":"UniRef90_P18065","uniref50":"UniRef50_P18065","genes":[{"name":{"value":"IGFBP2"},"synonyms":[{"value":"BP2"},{"value":"IBP2"}]}],"alphafold_very_low_content":0.28615384615384615,"disorder_content":0.043076923076923075,"disprot_consensus":{"full":[{"start":312,"end":325,"type":"D"}],"Structural state":[{"start":312,"end":325,"type":"D"}]}},{"disprot_id":"DP03279","acc":"Q08188","creator":"rpancsa","date":"2021-05-07T11:32:14.006Z","features":{"pfam":[{"id":"PF00868","name":"Transglutaminase family","start":7,"end":117},{"id":"PF00927","name":"Transglutaminase family, C-terminal ig like domain","start":485,"end":587},{"id":"PF00927","name":"Transglutaminase family, C-terminal ig like domain","start":595,"end":692},{"id":"PF01841","name":"Transglutaminase-like superfamily","start":269,"end":355}],"gene3D":[]},"length":693,"name":"Protein-glutamine gamma-glutamyltransferase E","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":463,"end":472,"reference_id":"11980702","reference_source":"pmid","reference_html":"Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions changes structure for activation. <i> Ahvazi B, Kim HC, Kee SH, Nemes Z, Steinert PM. </i> EMBO J, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1L9N"},{"db":"PDB","id":"1L9M"}],"region_id":"DP03279r001","statement":[{"text":"In the zymogen, one monomer has missing density for a flexible loop between residues 461 and 479, and the second monomer has missing density for residues 460–472. In the active enzyme, residues 460–480 are missing in both monomers.","type":"Results"},{"text":"Residues 462–471 form a flexible solvent-exposed loop that links the last α-helical segment of the catalytic core domain to the first β-strand of the barrel 1 domain.","type":"Results"},{"text":"Residues 462-471 represent the minimal region where densities are missing in all monomers of  all X-ray structures of the protein. There is one residue shift between the paper and UniProt, due to cleavage of the initiator methionine.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-10T13:27:14.901Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":463,"end":472,"reference_id":"12679341","reference_source":"pmid","reference_html":"Roles of calcium ions in the activation and activity of the transglutaminase 3 enzyme. <i> Ahvazi B, Boeshans KM, Idler W, Baxa U, Steinert PM. </i> J Biol Chem, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1NUD"},{"db":"PDB","id":"1NUF"},{"db":"PDB","id":"1NUG"},{"db":"PDB","id":"1L9M"}],"region_id":"DP03279r002","statement":[{"text":"Residues 462 to 471 form a highly flexible solventexposed loop that links the last alpha-helical segment of the catalytic core domain to the first beta-strand of the barrel 1 domain.","type":"Results"},{"text":"Both monomers have missing density for a flexible loop between residues 461–479.","type":"Results"},{"text":"Both monomers have missing density for a flexible loop between residues 462 and 478","type":"Results"},{"text":"Residues 462-471 represent the minimal region where densities are missing in all monomers of  all X-ray structures of the protein. Due to removal of the initiator methionine, there is one resiue shift between UniProt and the paper, Ser469 corresponds to UniProt residue 470.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-10T13:27:13.692Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":468,"end":472,"reference_id":"11980702","reference_source":"pmid","reference_html":"Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions changes structure for activation. <i> Ahvazi B, Kim HC, Kee SH, Nemes Z, Steinert PM. </i> EMBO J, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000048","term_name":"limited proteolysis display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","released":"2022_03","version":2,"region_id":"DP03279r003","statement":[{"text":"Residues 462-471 form a flexible solvent-exposed loop that link the last α-helical segment of the catalytic core domain to the first β-strand of the barrel 1 domain. This hinge region harbors Ser469, the cleavage site for proteolytic activation of the zymogen. This residue is flanked by polar residues, predicted to lie near the surface of the protein, which may be involved in recognition by an activating protease.","type":"Results"},{"text":"Due to removal of the initiator methionine, there is one resiue shift between UniProt and the paper, Ser469 corresponds to UniProt residue 470.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-10T13:27:17.202Z"},"disprot_namespace":"Disorder function"},{"start":468,"end":472,"reference_id":"12679341","reference_source":"pmid","reference_html":"Roles of calcium ions in the activation and activity of the transglutaminase 3 enzyme. <i> Ahvazi B, Boeshans KM, Idler W, Baxa U, Steinert PM. </i> J Biol Chem, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000048","term_name":"limited proteolysis display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","released":"2022_03","version":2,"region_id":"DP03279r004","statement":[{"text":"Proteolysis of the TGase 3 zymogen with dispase cleaves at Ser469 the flexible\nhinge of sequences that joins the active site domain to beta-barrel 1 domains.","type":"Results"},{"text":"Due to removal of the initiator methionine, there is one resiue shift between UniProt and the paper, Ser469 corresponds to UniProt residue 470.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-10T13:27:16.163Z"},"disprot_namespace":"Disorder function"}],"regions_counter":4,"released":"2021_06","sequence":"MAALGVQSINWQTAFNRQAHHTDKFSSQELILRRGQNFQVLMIMNKGLGSNERLEFIVSTGPYPSESAMTKAVFPLSNGSSGGWSAVLQASNGNTLTISISSPASAPIGRYTMALQIFSQGGISSVKLGTFILLFNPWLNVDSVFMGNHAEREEYVQEDAGIIFVGSTNRIGMIGWNFGQFEEDILSICLSILDRSLNFRRDAATDVASRNDPKYVGRVLSAMINSNDDNGVLAGNWSGTYTGGRDPRSWNGSVEILKNWKKSGFSPVRYGQCWVFAGTLNTALRSLGIPSRVITNFNSAHDTDRNLSVDVYYDPMGNPLDKGSDSVWNFHVWNEGWFVRSDLGPSYGGWQVLDATPQERSQGVFQCGPASVIGVREGDVQLNFDMPFIFAEVNADRITWLYDNTTGKQWKNSVNSHTIGRYISTKAVGSNARMDVTDKYKYPEGSDQERQVFQKALGKLKPNTPFAATSSMGLETEEQEPSIIGKLKVAGMLAVGKEVNLVLLLKNLSRDTKTVTVNMTAWTIIYNGTLVHEVWKDSATMSLDPEEEAEHPIKISYAQYEKYLKSDNMIRITAVCKVPDESEVVVERDIILDNPTLTLEVLNEARVRKPVNVQMLFSNPLDEPVRDCVLMVEGSGLLLGNLKIDVPTLGPKEGSRVRFDILPSRSGTKQLLADFSCNKFPAIKAMLSIDVAE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins","Age-related disorders proteins"],"UniParc":"UPI00001452F1","uniref100":"UniRef100_Q08188","uniref90":"UniRef90_Q08188","uniref50":"UniRef50_Q08188","genes":[{"name":{"value":"TGM3"}}],"alphafold_very_low_content":0.01875901875901876,"disorder_content":0.01443001443001443,"disprot_consensus":{"full":[{"start":463,"end":472,"type":"D"}],"Structural state":[{"start":463,"end":472,"type":"D"}],"Disorder function":[{"start":468,"end":472,"type":"F"}]}},{"disprot_id":"DP03280","acc":"P19827","creator":"vacs","date":"2021-05-07T15:22:08.176Z","features":{"pfam":[{"id":"PF00092","name":"von Willebrand factor type A domain","start":292,"end":472},{"id":"PF06668","name":"Inter-alpha-trypsin inhibitor heavy chain C-terminus","start":705,"end":892},{"id":"PF08487","name":"Vault protein inter-alpha-trypsin domain","start":53,"end":164}],"gene3D":[]},"length":911,"name":"Inter-alpha-trypsin inhibitor heavy chain H1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":653,"end":672,"reference_id":"32144206","reference_source":"pmid","reference_html":"Inter-α-inhibitor heavy chain-1 has an integrin-like 3D structure mediating immune regulatory activities and matrix stabilization during ovulation. <i> Briggs DC, Langford-Smith AWW, Birchenough HL, Jowitt TA, Kielty CM, Enghild JJ, Baldock C, Milner CM, Day AJ. </i> J Biol Chem, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6FPY"},{"db":"PDB","id":"6FPZ"}],"region_id":"DP03280r001","statement":[{"text":"The construct-derived His6 tag and residues 35–44, 631–638, and 653–672 of HC1, which were clearly present in the protein preparation as determined by MS, were not visible in the electron density and are therefore assumed to be unstructured or highly conformationally labile.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-10T14:16:00.317Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":35,"end":44,"reference_id":"32144206","reference_source":"pmid","reference_html":"Inter-α-inhibitor heavy chain-1 has an integrin-like 3D structure mediating immune regulatory activities and matrix stabilization during ovulation. <i> Briggs DC, Langford-Smith AWW, Birchenough HL, Jowitt TA, Kielty CM, Enghild JJ, Baldock C, Milner CM, Day AJ. </i> J Biol Chem, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6FPY"},{"db":"PDB","id":"6FPZ"}],"region_id":"DP03280r002","statement":[{"text":"The construct-derived His6 tag and residues 35–44, 631–638, and 653–672 of HC1, which were clearly present in the protein preparation as determined by MS, were not visible in the electron density and are therefore assumed to be unstructured or highly conformationally labile.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-10T14:16:01.388Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":653,"end":657,"reference_id":"9425062","reference_source":"pmid","reference_html":"Posttranslational modifications of human inter-alpha-inhibitor: identification of glycans and disulfide bridges in heavy chains 1 and 2. <i> Olsen EH, Rahbek-Nielsen H, Thogersen IB, Roepstorff P, Enghild JJ. </i> Biochemistry, 1998","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000041","term_name":"glycosylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP03280r003","statement":[{"text":"In addition, the IRI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.","type":"Abstract"},{"text":"Edman degradation of the C-terminal HC1 peptide, Thr608-Arg627, identified Thr619 as the site of O-glycosylation.","type":"Results"},{"text":"Thus the carbohydrate attached to HC1 Thr619 is a trisaccharide composed of (Thr)-GalNAc-Gal-SA (Figure 2B).","type":"Results"},{"text":"In addition to the N-glycans, the IRI heavy chains also carry 5 O-linked trisaccharides: one attached to HC1 Thr619 and a cluster of four near the C-terminus of HC2 (Figure 3).","type":"Discussion"},{"text":"Thr619 corresponds to Thr653, since the natural precursor form of the protein contains a signal peptide (1-27) and a propeptide (28-34).","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-20T16:04:02.668Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":668,"end":672,"reference_id":"7513643","reference_source":"pmid","reference_html":"Chondroitin sulphate covalently cross-links the three polypeptide chains of inter-alpha-trypsin inhibitor. <i> Morelle W, Capon C, Balduyck M, Sautiere P, Kouach M, Michalski C, Fournet B, Mizon J. </i> Eur J Biochem, 1994","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"GO:0030246","term_name":"carbohydrate binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03280r004","statement":[{"text":"As already pointed out by Enghild et al. [l], the C-terminal Asp residue, characterized by amino acid analysis of these peptides, was only identified with a low yield by Edman degradation. This is consistent with the fact that this residue is glycosylated.","type":"Results"},{"text":"Effectively fragment ions at mlz 679 for fraction 1 and mlz 652 for fraction 3 indicated that N-acetyl hexosamine is linked to the C-terminal Asp of each heavy chain.","type":"Results"},{"text":"A fragment ion at mlz 491 for fraction 3 (Fig. 6B) demonstrated that the linkage involves the C6 of the terminus (reducing) N-acetylhexosamine and the C-terminal Asp of H1.","type":"Results"},{"text":"The linkage to the H1 subunit involves an ester linkage between C6 of an internal N-acetylhexosamine and the C-terminal Asp638.","type":"Results"},{"text":"On the IT1 fragment obtained, two different tetrapeptides covalently linked to the chondroitin sulphate chain should be present: Val-Asp-ThrAsp proceeding from H1 and Val-Glu-Asn-Asp corresponding to the C-terminal sequence of H2.","type":"Discussion"},{"text":"Asp638 corresponds to Asp672, which is the C-terminal residue of the mature form of the protein, since the natural precursor form contains a signal peptide (1-27) and two propeptides (28-34 and 673-911).","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-20T16:04:01.853Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.\" [GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":4,"released":"2021_06","sequence":"MDGAMGPRGLLLCMYLVSLLILQAMPALGSATGRSKSSEKRQAVDTAVDGVFIRSLKVNCKVTSRFAHYVVTSQVVNTANEAREVAFDLEIPKTAFISDFAVTADGNAFIGDIKDKVTAWKQYRKAAISGENAGLVRASGRTMEQFTIHLTVNPQSKVTFQLTYEEVLKRNHMQYEIVIKVKPKQLVHHFEIDVDIFEPQGISKLDAQASFLPKELAAQTIKKSFSGKKGHVLFRPTVSQQQSCPTCSTSLLNGHFKVTYDVSRDKICDLLVANNHFAHFFAPQNLTNMNKNVVFVIDISGSMRGQKVKQTKEALLKILGDMQPGDYFDLVLFGTRVQSWKGSLVQASEANLQAAQDFVRGFSLDEATNLNGGLLRGIEILNQVQESLPELSNHASILIMLTDGDPTEGVTDRSQILKNVRNAIRGRFPLYNLGFGHNVDFNFLEVMSMENNGRAQRIYEDHDATQQLQGFYSQVAKPLLVDVDLQYPQDAVLALTQNHHKQYYEGSEIVVAGRIADNKQSSFKADVQAHGEGQEFSITCLVDEEEMKKLLRERGHMLENHVERLWAYLTIQELLAKRMKVDREERANLSSQALQMSLDYGFVTPLTSMSIRGMADQDGLKPTIDKPSEDSPPLEMLGPRRTFVLSALQPSPTHSSSNTQRLPDRVTGVDTDPHFIIHVPQKEDTLCFNINEEPGVILSLVQDPNTGFSVNGQLIGNKARSPGQHDGTYFGRLGIANPATDFQLEVTPQNITLNPGFGGPVFSWRDQAVLRQDGVVVTINKKRNLVVSVDDGGTFEVVLHRVWKGSSVHQDFLGFYVLDSHRMSARTHGLLGQFFHPIGFEVSDIHPGSDPTKPDATMVVRNRRLTVTRGLQKDYSKDPWHGAEVSCWFIHNNGAGLIDGAYTDYIVPDIF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000016AAD9","uniref100":"UniRef100_P19827","uniref90":"UniRef90_P19827","uniref50":"UniRef50_P19827","genes":[{"name":{"value":"ITIH1"},"synonyms":[{"value":"IGHEP1"}]}],"alphafold_very_low_content":0.0845225027442371,"disorder_content":0.03293084522502744,"disprot_consensus":{"full":[{"start":35,"end":44,"type":"D"},{"start":653,"end":672,"type":"D"}],"Structural state":[{"start":35,"end":44,"type":"D"},{"start":653,"end":672,"type":"D"}],"Disorder function":[{"start":653,"end":657,"type":"F"}],"Molecular function":[{"start":668,"end":672,"type":"F"}]}},{"disprot_id":"DP03281","acc":"Q2MKA7","creator":"rpancsa","date":"2021-05-07T16:14:45.967Z","features":{"pfam":[{"id":"PF15913","name":"Furin-like repeat, cysteine-rich","start":42,"end":142}],"gene3D":[]},"length":263,"name":"R-spondin-1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":131,"end":146,"reference_id":"23809763","reference_source":"pmid","reference_html":"Structure of stem cell growth factor R-spondin 1 in complex with the ectodomain of its receptor LGR5. <i> Peng WC, de Lau W, Forneris F, Granneman JC, Huch M, Clevers H, Gros P. </i> Cell Rep, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4BSO"}],"region_id":"DP03281r001","statement":[{"text":"Structure of (unbound) Rspo1-Fu1Fu2 (residues 31–145) at 2 Å resolution. Indicated are disulphide bonds (ball and stick) and disordered residues (dashed line).","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-20T14:17:46.554Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":131,"end":146,"reference_id":"23809763","reference_source":"pmid","reference_html":"Structure of stem cell growth factor R-spondin 1 in complex with the ectodomain of its receptor LGR5. <i> Peng WC, de Lau W, Forneris F, Granneman JC, Huch M, Clevers H, Gros P. </i> Cell Rep, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4BSO"},{"db":"PDB","id":"4BSU"},{"db":"PDB","id":"4BSR"},{"db":"PDB","id":"4BSS"},{"db":"PDB","id":"4BST"}],"region_id":"DP03281r002","statement":[{"text":"Structure of (unbound) Rspo1-Fu1Fu2 (residues 31–145) at 2 Å resolution. Indicated are disulphide bonds (ball and stick) and disordered residues (dashed line).","type":"Figure"},{"text":"Overlay of bound and unbound Rspo1. The arrow indicates a hinge around which the orientation between the Fu1 and Fu2 domains differs by ∼90° between the LGR5-bound and unbound structure of Rspo1.","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-20T14:17:47.395Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":131,"end":146,"reference_id":"24349440","reference_source":"pmid","reference_html":"Structures of Wnt-antagonist ZNRF3 and its complex with R-spondin 1 and implications for signaling. <i> Peng WC, de Lau W, Madoori PK, Forneris F, Granneman JC, Clevers H, Gros P. </i> PLoS One, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4BSO"},{"db":"PDB","id":"4CDK"}],"region_id":"DP03281r003","statement":[{"text":"Overlay of four representative RSPO1 structures in two orientations with free RSPO1 (grey; PDB code 4BSO), RSPO1 in LGR5-RSPO1-RNF43 complex (blue, PDB code 4KNG) and RSPO1 in complex with ZNRF3 (orange and red).","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-20T14:17:48.335Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"}],"regions_counter":3,"released":"2021_06","sequence":"MRLGLCVVALVLSWTHLTISSRGIKGKRQRRISAEGSQACAKGCELCSEVNGCLKCSPKLFILLERNDIRQVGVCLPSCPPGYFDARNPDMNKCIKCKIEHCEACFSHNFCTKCKEGLYLHKGRCYPACPEGSSAANGTMECSSPAQCEMSEWSPWGPCSKKQQLCGFRRGSEERTRRVLHAPVGDHAACSDTKETRRCTVRRVPCPEGQKRRKGGQGRRENANRNLARKESKEAGAGSRRRKGQQQQQQQGTVGPLTSAGPA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000674A16","uniref100":"UniRef100_Q2MKA7","uniref90":"UniRef90_Q2MKA7","uniref50":"UniRef50_Q2MKA7","genes":[{"name":{"value":"RSPO1"}}],"alphafold_very_low_content":0.22433460076045628,"disorder_content":0.060836501901140684,"disprot_consensus":{"full":[{"start":131,"end":146,"type":"T"}],"Structural state":[{"start":131,"end":146,"type":"D"}],"Structural transition":[{"start":131,"end":146,"type":"T"}]}},{"disprot_id":"DP03282","acc":"Q8L3W1","creator":"jiserte","date":"2021-05-09T15:01:24.168Z","features":{"pfam":[{"id":"PF02362","name":"B3 DNA binding domain","start":5,"end":96},{"id":"PF02362","name":"B3 DNA binding domain","start":244,"end":337}],"gene3D":[]},"length":341,"name":"B3 domain-containing transcription factor VRN1","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":208,"end":220,"reference_id":"23255593","reference_source":"pmid","reference_html":"The Arabidopsis B3 domain protein VERNALIZATION1 (VRN1) is involved in processes essential for development, with structural and mutational studies revealing its DNA-binding surface. <i> King GJ, Chanson AH, McCallum EJ, Ohme-Takagi M, Byriel K, Hill JM, Martin JL, Mylne JS. </i> J Biol Chem, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"jiserte","curator_name":"Javier Iserte","curator_orcid":"0000-0003-0056-1177","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4I1K"}],"region_id":"DP03282r001","statement":[{"text":"Of the 133 residues in the designed construct, 117 residues were modeled in each of the two molecules in the asymmetric unit. In both molecules, residues 208–220 and 339–341 of VRN1(208–341) were not modeled due to poor electron density at the N and C termini, indicating disorder.","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-01T10:54:08.102Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MPRPFFHKLIFSSTIQEKRLRVPDKFVSKFKDELSVAVALTVPDGHVWRVGLRKADNKIWFQDGWQEFVDRYSIRIGYLLIFRYEGNSAFSVYIFNLSHSEINYHSTGLMDSAHNHFKRARLFEDLEDEDAEVIFPSSVYPSPLPESTVPANKGYASSAIQTLFTGPVKAEEPTPTPKIPKKRGRKKKNADPEEINSSAPRDDDPENRSKFYESASARKRTVTAEERERAINAAKTFEPTNPFFRVVLRPSYLYRGCIMYLPSGFAEKYLSGISGFIKVQLAEKQWPVRCLYKAGRAKFSQGWYEFTLENNLGEGDVCVFELLRTRDFVLKVTAFRVNEYV","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"dataset":["Condensates-related proteins"],"UniParc":"UPI0000038E3E","uniref100":"UniRef100_Q8L3W1","uniref90":"UniRef90_Q8L3W1","uniref50":"UniRef50_Q8L3W1","genes":[{"name":{"value":"VRN1"},"orfNames":[{"value":"K13E13.10"}],"olnNames":[{"value":"At3g18990"}]}],"alphafold_very_low_content":0.2756598240469208,"disorder_content":0.03812316715542522,"disprot_consensus":{"full":[{"start":208,"end":220,"type":"D"}],"Structural state":[{"start":208,"end":220,"type":"D"}]}},{"disprot_id":"DP03283","acc":"O80452","creator":"jiserte","date":"2021-05-09T15:14:59.824Z","features":{"pfam":[{"id":"PF19326","name":"AMP deaminase","start":227,"end":831}],"gene3D":[]},"length":839,"name":"AMP deaminase","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":140,"end":211,"reference_id":"16543243","reference_source":"pmid","reference_html":"Membrane association, mechanism of action, and structure of Arabidopsis embryonic factor 1 (FAC1). <i> Han BW, Bingman CA, Mahnke DK, Bannen RM, Bednarek SY, Sabina RL, Phillips GN. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"jiserte","curator_name":"Javier Iserte","curator_orcid":"0000-0003-0056-1177","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"2A3L"}],"region_id":"DP03283r001","statement":[{"text":"The final crystallographic model of the I139M FAC1 enzyme comprises only 616 of the 701 amino acids in this polypeptide (residues\n212–273 and 286–839). Whereas 13 of the 85 unstructured amino acids\nare part of a loop that forms the Walker A motif, the remainder are\nlocated in the N terminus of this truncated enzyme. Regarding these\nlatter residues, several computer-based prediction servers (ROBETTA,\nGLOBPLOT, FoldIndex, and DRIPPRED) indicate that the entire\nstretch of sequence (residues 32–211) between the N-terminal helical\ntransmembrane domain and the globular catalytic domain is largely\nunstructured. ","type":"Discussion"},{"text":"The proposed configuration between FAC1 and a lipid bilayer is reminiscent\nof a “paddleball,” with the globular catalytic domain representing the\n“ball” and the transmembrane domains (residues 6–31) and disordered\nlinker regions (residues 32–211) comprising the anchors and flexible\nconnectors, respectively. ","type":"Discussion"},{"text":"The authors state that region from positions 32 to 211 is disordered from computer based predictions. However only the region from 140 to 211 is disordered in the PDB structure (N-terminal region). ","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-01T10:45:27.050Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":274,"end":285,"reference_id":"16543243","reference_source":"pmid","reference_html":"Membrane association, mechanism of action, and structure of Arabidopsis embryonic factor 1 (FAC1). <i> Han BW, Bingman CA, Mahnke DK, Bannen RM, Bednarek SY, Sabina RL, Phillips GN. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"jiserte","curator_name":"Javier Iserte","curator_orcid":"0000-0003-0056-1177","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"2A3L"}],"region_id":"DP03283r002","statement":[{"text":"The final crystallographic model of the I139M FAC1 enzyme comprises only 616 of the 701 amino acids in this polypeptide (residues\n212–273 and 286–839). Whereas 13 of the 85 unstructured amino acids\nare part of a loop that forms the Walker A motif, the remainder are\nlocated in the N terminus of this truncated enzyme. Regarding these\nlatter residues, several computer-based prediction servers (ROBETTA,\nGLOBPLOT, FoldIndex, and DRIPPRED) indicate that the entire\nstretch of sequence (residues 32–211) between the N-terminal helical\ntransmembrane domain and the globular catalytic domain is largely\nunstructured. ","type":"Discussion"},{"text":"The region of 13 disordered aminoacids correspond to positions 274 to 285 according to the PDB structure (2A3L).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-01T10:45:26.090Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":274,"end":285,"reference_id":"16543243","reference_source":"pmid","reference_html":"Membrane association, mechanism of action, and structure of Arabidopsis embryonic factor 1 (FAC1). <i> Han BW, Bingman CA, Mahnke DK, Bannen RM, Bednarek SY, Sabina RL, Phillips GN. </i> J Biol Chem, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"jiserte","curator_name":"Javier Iserte","curator_orcid":"0000-0003-0056-1177","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"cross_refs":[{"db":"PDB","id":"2A3L"}],"region_id":"DP03283r003","statement":[{"text":"The final crystallographic model of the I139M FAC1 enzyme comprises only 616 of the 701 amino acids in this polypeptide (residues\n212–273 and 286–839). Whereas 13 of the 85 unstructured amino acids\nare part of a loop that forms the Walker A motif, the remainder are\nlocated in the N terminus of this truncated enzyme. Regarding these\nlatter residues, several computer-based prediction servers (ROBETTA,\nGLOBPLOT, FoldIndex, and DRIPPRED) indicate that the entire\nstretch of sequence (residues 32–211) between the N-terminal helical\ntransmembrane domain and the globular catalytic domain is largely\nunstructured. ","type":"Discussion"},{"text":"The proposed configuration between FAC1 and a lipid bilayer is reminiscent of a “paddleball,” with the globular catalytic domain representing the “ball” and the transmembrane domains (residues 6–31) and disordered linker regions (residues 32–211) comprising the anchors and flexible connectors, respectively","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-01T10:45:28.687Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":3,"released":"2023_12","sequence":"MEPNIYQLALAALFGASFVAVSGFFMHFKALNLVLERGKERKENPDGDEPQNPTLVRRRSQVRRKVNDQYGRSPASLPDATPFTDGGGGGGGDTGRSNGHVYVDEIPPGLPRLHTPSEGRASVHGASSIRKTGSFVRPISPKSPVASASAFESVEESDDDDNLTNSEGLDASYLQANGDNEMPADANEEQISMAASSMIRSHSVSGDLHGVQPDPIAADILRKEPEQETFVRLNVPLEVPTSDEVEAYKCLQECLELRKRYVFQETVAPWEKEVISDPSTPKPNTEPFAHYPQGKSDHCFEMQDGVVHVFANKDAKEDLFPVADATAFFTDLHHVLKVIAAGNIRTLCHRRLVLLEQKFNLHLMLNADKEFLAQKSAPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGTYLTLREVFESLDLTGYDLNVDLLDVHADKSTFHRFDKFNLKYNPCGQSRLREIFLKQDNLIQGRFLGEITKQVFSDLEASKYQMAEYRISIYGRKMSEWDQLASWIVNNDLYSENVVWLIQLPRLYNIYKDMGIVTSFQNILDNIFIPLFEATVDPDSHPQLHVFLKQVVGFDLVDDESKPERRPTKHMPTPAQWTNAFNPAFSYYVYYCYANLYVLNKLRESKGMTTITLRPHSGEAGDIDHLAATFLTCHSIAHGINLRKSPVLQYLYYLAQIGLAMSPLSNNSLFLDYHRNPFPVFFLRGLNVSLSTDDPLQIHLTKEPLVEEYSIAASVWKLSACDLCEIARNSVYQSGFSHALKSHWIGKDYYKRGPDGNDIHKTNVPHIRVEFRDTIWKEEMQQVYLGKAVISDEVVP","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"dataset":[],"UniParc":"UPI0000037582","uniref100":"UniRef100_O80452","uniref90":"UniRef90_O80452","uniref50":"UniRef50_O80452","genes":[{"name":{"value":"AMPD","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15918887","url":"http://www.ncbi.nlm.nih.gov/pubmed/15918887","alternativeUrl":"https://europepmc.org/abstract/MED/15918887"}}]},"synonyms":[{"value":"FAC1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15918887","url":"http://www.ncbi.nlm.nih.gov/pubmed/15918887","alternativeUrl":"https://europepmc.org/abstract/MED/15918887"}}]}],"orfNames":[{"value":"F16M14.21","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAC27176.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAC27176.2"}}]}],"olnNames":[{"value":"At2g38280","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT2G38280","url":""}}]}]}],"alphafold_very_low_content":0.22169249106078665,"disorder_content":0.10011918951132301,"disprot_consensus":{"full":[{"start":140,"end":211,"type":"D"},{"start":274,"end":285,"type":"D"}],"Structural state":[{"start":140,"end":211,"type":"D"},{"start":274,"end":285,"type":"D"}],"Disorder function":[{"start":274,"end":285,"type":"F"}]}},{"disprot_id":"DP03284","acc":"Q8GUI6","creator":"jiserte","date":"2021-05-09T18:31:30.130Z","features":{"pfam":[{"id":"PF02373","name":"JmjC domain, hydroxylase","start":296,"end":412},{"id":"PF02375","name":"jmjN domain","start":57,"end":90},{"id":"PF02928","name":"C5HC2 zinc finger","start":519,"end":570},{"id":"PF05964","name":"F/Y-rich N-terminus","start":733,"end":783},{"id":"PF05965","name":"F/Y rich C-terminus","start":788,"end":875}],"gene3D":[]},"length":954,"name":"Probable lysine-specific demethylase JMJ14","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":125,"end":168,"reference_id":"29233856","reference_source":"pmid","reference_html":"Structure of the Arabidopsis JMJ14-H3K4me3 Complex Provides Insight into the Substrate Specificity of KDM5 Subfamily Histone Demethylases. <i> Yang Z, Qiu Q, Chen W, Jia B, Chen X, Hu H, He K, Deng X, Li S, Tao WA, Cao X, Du J. </i> Plant Cell, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"jiserte","curator_name":"Javier Iserte","curator_orcid":"0000-0003-0056-1177","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5YKN"},{"db":"PDB","id":"5YKO"}],"region_id":"DP03284r001","statement":[{"text":"In our JMJ14CD structure, the region corresponding to human KDM5\nARID-PHD cassette (residues 125–168) has no annotated domain\nand is disordered in the structure.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-13T12:36:30.431Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":196,"end":211,"reference_id":"29233856","reference_source":"pmid","reference_html":"Structure of the Arabidopsis JMJ14-H3K4me3 Complex Provides Insight into the Substrate Specificity of KDM5 Subfamily Histone Demethylases. <i> Yang Z, Qiu Q, Chen W, Jia B, Chen X, Hu H, He K, Deng X, Li S, Tao WA, Cao X, Du J. </i> Plant Cell, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"jiserte","curator_name":"Javier Iserte","curator_orcid":"0000-0003-0056-1177","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5YKN"},{"db":"PDB","id":"5YKO"}],"region_id":"DP03284r002","statement":[{"text":"PDB structures of both, free and ligand bound, forms have a range of missing residues from positions 196 to 212.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-13T12:36:29.668Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MDQLASLAESVAMEEDSEKQSIKGESSLEPDSTPSSPKITARWNPSEACRPLVDDAPIFYPTNEDFDDPLGYIEKLRSKAESYGICRIVPPVAWRPPCPLKEKKIWENSKFPTRIQFIDLLQNREPIKKSTKTKKRKRRRISKIGYTRRKRDSGCDTASSGSSDSEGKFGFQTGPDFTLEEFQKYDEYFKECYFQSEDHPGSKASENKKFKPKVKDLEGEYWRIVEQATDEVEVYYGADLETKKFGSGFPKYKPGYPISEADQYSQCGWNLNNLSRLPGSVLAFESCDISGVIVPWLYVGMCFSTFCWHVEDHHLYSMNYLHTGDPKVWYGIPGNHAESFENVMKKRLPDLFEEQPDLLHQLVTQLSPRILKEEGVPVYRAVQRSGEFILTFPKAYHSGFNCGFNCAEAVNVAPVDWLVHGQNAVEGYSKQRRKSSLSHDKLLLGAAMEATYCLWELSLSKKKTPVIARWKRVCSEDGLLTKAVKKRVQMEEERLNHLQDGFSLRKMEGDFDNKRERECFLCFYDLHMSASSCKCSPNRFACLIHAKDLCSCESKDRYILIRHTLDELWALVRALEGDLDAIDLWASKCRDQYPSQHPRAREYAYLKSAPCIKSRGSSKVQQREQNNLQLVSERLQSDLTSNKEVQLKQDGDSDVNRHGHESERNHVHGITDKSAVTDVKLGVGGKFDEKKISVESQNPHSVSDVGCSELAKKVDGCLGGKDQNAATNRLSLSVELLSSGSLVVKKLWCSKQAIYPKGFKSRVKFLSVLDPTNLTNYISEVLDAGLLGPLFRVSVEDYPTENFSNVSAEKCWQMVTQRLKLEIIKKCDQPVSSLTSLQPLESINGLEMFGFLSPHVIKVVEALDPKHQLEEYWNQKAVKLFGAEPIKEGEKDDTEKGGASDPSLDRDTRLLRGLLKKATPEELVMMHGLLCGETRNTELKEELSTLVDKMEISP","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"dataset":[],"UniParc":"UPI00000AE214","uniref100":"UniRef100_Q8GUI6","uniref90":"UniRef90_Q8GUI6","uniref50":"UniRef50_Q8GUI6","genes":[{"name":{"value":"JMJ14","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"18713399","url":"http://www.ncbi.nlm.nih.gov/pubmed/18713399","alternativeUrl":"https://europepmc.org/abstract/MED/18713399"}}]},"synonyms":[{"value":"JMJ4","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"19946624","url":"http://www.ncbi.nlm.nih.gov/pubmed/19946624","alternativeUrl":"https://europepmc.org/abstract/MED/19946624"}}]},{"value":"PKDM7B","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"18950507","url":"http://www.ncbi.nlm.nih.gov/pubmed/18950507","alternativeUrl":"https://europepmc.org/abstract/MED/18950507"}}]}],"orfNames":[{"value":"F9F13.50","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"CAB45806.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAB45806.1"}}]}],"olnNames":[{"value":"At4g20400","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT4G20400","url":""}}]}]}],"alphafold_very_low_content":0.26834381551362685,"disorder_content":0.06289308176100629,"disprot_consensus":{"full":[{"start":125,"end":168,"type":"D"},{"start":196,"end":211,"type":"D"}],"Structural state":[{"start":125,"end":168,"type":"D"},{"start":196,"end":211,"type":"D"}]}},{"disprot_id":"DP03285","acc":"Q8H1D4","creator":"jiserte","date":"2021-05-09T18:52:34.091Z","features":{"pfam":[{"id":"PF00035","name":"Double-stranded RNA binding motif","start":5,"end":71},{"id":"PF00035","name":"Double-stranded RNA binding motif","start":83,"end":144}],"gene3D":[]},"length":355,"name":"Double-stranded RNA-binding protein 4","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":154,"end":293,"reference_id":"28575480","reference_source":"pmid","reference_html":"DRB4 dsRBD1 drives dsRNA recognition in Arabidopsis thaliana tasi/siRNA pathway. <i> Chiliveri SC, Aute R, Rai U, Deshmukh MV. </i> Nucleic Acids Res, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jiserte","curator_name":"Javier Iserte","curator_orcid":"0000-0003-0056-1177","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03285r001","statement":[{"text":"The 1H–15N HSQC confirmed that most of the DRB4C is disordered in solution as we observed narrow spectral dispersion in the proton dimension (Supplementary Figure S1E). The random\ncoil nature of DRB4C was also evident from the chemical\nshifts of C-alpha and C-beta. Moreover, the majority of DRB4C resonances assume a negative value in 15N–{1H} hetronuclear NOE corroborating its unstructured nature (Figure 1B). Interestingly, resonances belonging to residues 294–355 (i.e.\nDRB4Cc) were absent in the 1H–15N HSQC of DRB4C.\nProtein disorder algorithms predicted that DRB4Cc may assume an ordered conformation. Subsequently, a welldispersed 1H–15N HSQC for DRB4Cc implied the presence of a tertiary structure.","type":"Results"},{"text":"The truncated fragments of DRB4; DRB4 (1-153) (hereafter DRB4D1D2), DRB4 (1-75) (hereafter: DRB4D1), DRB4 (80-153) (hereafter: DRB4D2), DRB4 (154-355) (hereafter: DRB4C), DRB4 (294-355) (hereafter: DRB4Cc), DRB4 (72-81 connected to 4-71) (hereafter: DRB4LD1) and DRB4 (72-153) (hereafter: DRB4LD2) were also cloned into pET-30a in a similar way.","type":"Supplementary material"},{"text":"The unstructured region of DRB4 is a flexible linker connecting DRB4D1D2 (1-153) and DRB4Cc (294-355).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-25T14:24:51.481Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":154,"end":293,"reference_id":"28575480","reference_source":"pmid","reference_html":"DRB4 dsRBD1 drives dsRNA recognition in Arabidopsis thaliana tasi/siRNA pathway. <i> Chiliveri SC, Aute R, Rai U, Deshmukh MV. </i> Nucleic Acids Res, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jiserte","curator_name":"Javier Iserte","curator_orcid":"0000-0003-0056-1177","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03285r002","statement":[{"text":"The 1H–15N HSQC confirmed that most of the DRB4C is disordered in solution as we observed narrow spectral dispersion in the proton dimension (Supplementary Figure S1E). The random coil nature of DRB4C was also evident from the chemical shifts of C-alpha and C-beta. Moreover, the majority of DRB4C resonances assume a negative value in 15N–{1H} hetronuclear NOE corroborating its unstructured nature (Figure 1B). Interestingly, resonances belonging to residues 294–355 (i.e. DRB4Cc) were absent in the 1H–15N HSQC of DRB4C. Protein disorder algorithms predicted that DRB4Cc may assume an ordered conformation. Subsequently, a welldispersed 1H–15N HSQC for DRB4Cc implied the presence of a tertiary structure.","type":"Results"},{"text":"The truncated fragments of DRB4; DRB4 (1-153) (hereafter DRB4D1D2), DRB4 (1-75) (hereafter: DRB4D1), DRB4 (80-153) (hereafter: DRB4D2), DRB4 (154-355) (hereafter: DRB4C), DRB4 (294-355) (hereafter: DRB4Cc), DRB4 (72-81 connected to 4-71) (hereafter: DRB4LD1) and DRB4 (72-153) (hereafter: DRB4LD2) were also cloned into pET-30a in a similar way.","type":"Supplementary material"},{"text":"The unstructured region of DRB4 is a flexible linker connecting DRB4D1D2 (1-153) and DRB4Cc (294-355).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-25T14:24:52.279Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":2,"released":"2021_12","sequence":"MDHVYKGQLQAYALQHNLELPVYANEREGPPHAPRFRCNVTFCGQTFQSSEFFPTLKSAEHAAAKIAVASLTPQSPEGIDVAYKNLLQEIAQKESSLLPFYATATSGPSHAPTFTSTVEFAGKVFSGEEAKTKKLAEMSAAKVAFMSIKNGNSNQTGSPTLPSERQEDVNSNVKSSPQEIHSQPSSKVVMTPDTPSKGIKVNEDEFPDLHDAPASNAKEINVALNEPENPTNDGTLSALTTDGMKMNIASSSLPIPHNPTNVITLNAPAANGIKRNIAACSSWMPQNPTNDGSETSSCVVDESEKKKLIMGTGHLSIPTGQHVVCRPWNPEITLPQDAEMLFRDDKFIAYRLVKP","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"dataset":["RNA-binding proteins"],"UniParc":"UPI00000ADA9F","uniref100":"UniRef100_Q8H1D4","uniref90":"UniRef90_Q8H1D4","uniref50":"UniRef50_Q8H1D4","genes":[{"name":{"value":"DBR4"},"orfNames":[{"value":"F26K9.230"}],"olnNames":[{"value":"At3g62800"}]}],"alphafold_very_low_content":0.43380281690140843,"disorder_content":0.39436619718309857,"disprot_consensus":{"full":[{"start":154,"end":293,"type":"D"}],"Structural state":[{"start":154,"end":293,"type":"D"}],"Disorder function":[{"start":154,"end":293,"type":"F"}]}},{"disprot_id":"DP03286","acc":"Q03479","creator":"smribeiro","date":"2021-05-10T08:24:18.711Z","features":{"pfam":[{"id":"PF00063","name":"Myosin head (motor domain)","start":11,"end":680},{"id":"PF00612","name":"IQ calmodulin-binding motif","start":698,"end":715},{"id":"PF00612","name":"IQ calmodulin-binding motif","start":719,"end":739},{"id":"PF06017","name":"Unconventional myosin tail, actin- and lipid-binding","start":811,"end":982}],"gene3D":[]},"length":1005,"name":"Myosin IE heavy chain","ncbi_taxon_id":44689,"organism":"Dictyostelium discoideum","regions":[{"start":549,"end":559,"reference_id":"12032065","reference_source":"pmid","reference_html":"Crystal structure of the motor domain of a class-I myosin. <i> Kollmar M, Dürrwang U, Kliche W, Manstein DJ, Kull FJ. </i> EMBO J, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1LKX"}],"region_id":"DP03286r001","statement":[{"text":"PDB - unmodeled residues 549-559","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MIPKTKAEGVPDFVLLNQITENAFIENLTMRHKSDNIYTYIGDVVISTNPFKNLNIYKESDIKAYNGRYKYEMPPHIYALANDAYRSMRQSQENQCVIISGESGAGKTEASKKIMQFLTFVSSNQSPNGERISKMLLDSNPLLEAFGNAKTLRNDNSSRFGKYMEMQFNAVGSPIGGKITNYLLEKSRVVGRTQGERSFHIFYQMLKGLSQSKLNELGLTPNAPAYEYLKKSGCFDVSTIDDSGEFKIIVKAMETLGLKESDQNSIWRILAAILHIGNITFAEAAEQRTGTTTVKVSDTKSLAAAASCLKTDQQSLSIALCYRSISTGVGKRCSVISVPMDCNQAAYSRDALAKALYERLFNWLVSKINTIINCTTEKGPVIGILDIYGFEVFQNNSFEQLNINFCNEKLQQLFIELTLKSEQEEYVREGIEWKNIEYFNNKPICELIEKKPIGLISLLDEACLIAKSTDQTFLDSICKQFEKNPHLQSYVVSKDRSIGDTCFRLKHYAGDVTYDVRGFLDKNKDTLFGDLISSMQSSSDPLVQGLFPPTRPEDSKKRPETAGSQFRNAMNALITTLLACSPHYVRCIKSNDNKQAGVIDEDRVRHQVRYLGLLENVRVRRAGFAGRIEYTRFYNRYKMLCKKTWPSFNGTAKQATELILQQHNIDKEEIRMGKTKVFIRNPTTLFYFEEKRELEMPRIVTLIQKTWRGYRARSKWNQRKAAIKIQLFYRSYRYKKWFRELHRAFKDVARDPQWGKQVFWPKHPSILDRAVQLTHKIHNCWRAEKMILSLGAGQNHMRQKVMAYDIFHGKKKWDFRRHFDADYLEKPSNPNQQKYVLAMQNLFSTYGDTEVLFADYVIKVNPKGVPQRRGIVVTGTNIYKHDPKNYKVKKWGTPLVDVTSISISPMADTFLVLHCKAPQRDFVLDLGCNGYEAVSEITTVIVQQVLKLTGVKLSVQFTSSITYNNARPKGSDTILTFAPINNDPKLIGSQFKKGKGNQATIQFKD","taxonomy":["Eukaryota","Amoebozoa","Evosea","Eumycetozoa","Dictyostelia","Dictyosteliales","Dictyosteliaceae","Dictyostelium"],"dataset":[],"UniParc":"UPI000012FBE4","uniref100":"UniRef100_Q03479","uniref90":"UniRef90_Q03479","uniref50":"UniRef50_Q03479","genes":[{"name":{"value":"myoE"},"synonyms":[{"value":"dmiE"}],"orfNames":[{"value":"DDB_G0288679"}]}],"alphafold_very_low_content":0.007960199004975124,"disorder_content":0.010945273631840797,"disprot_consensus":{"full":[{"start":549,"end":559,"type":"D"}],"Structural state":[{"start":549,"end":559,"type":"D"}]}},{"disprot_id":"DP03287","acc":"P13022","creator":"smribeiro","date":"2021-05-10T09:35:25.600Z","features":{"pfam":[{"id":"PF01267","name":"F-actin capping protein alpha subunit","start":11,"end":277}],"gene3D":[]},"length":281,"name":"F-actin-capping protein subunit alpha","ncbi_taxon_id":44689,"organism":"Dictyostelium discoideum","regions":[{"start":271,"end":281,"reference_id":"22657106","reference_source":"pmid","reference_html":"Conservation and divergence between cytoplasmic and muscle-specific actin capping proteins: insights from the crystal structure of cytoplasmic Cap32/34 from Dictyostelium discoideum. <i> Eckert C, Goretzki A, Faberova M, Kollmar M. </i> BMC Struct Biol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4AKR"}],"region_id":"DP03287r001","statement":[{"text":"The final model contains residues 2–272 (and 2–270 for the second molecule within the asymmetric unit, respectively) of the 281 residues of the α-subunit.","type":"Methods"},{"text":"PDB - unmodeled residues 271-281 (Chain A)","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MASNQELVQIATNFLLNAPPCEFMEVVSDVRALLPSESLLNASAGSTFREYNTSQMVSVQTSKGSALITKEGEISNNEYLDPKNKQVITYDHIKQEVTGERSASGEIEQDIEQYRAAFDEEATKYCNEYYPNGVSAVYGTKVSEGIKITVCISTCIYKPNAFYSGRWRSVWTCTFKPGSGNVTSNGKVQVNVHYFEDGNVQLNTVTQKQTTSPSADAQSTAVNAFKAIGKAELNLHTALDNNYSTMGDTTFKALRRALPINRTKINWQKVKNFKIANELNK","taxonomy":["Eukaryota","Amoebozoa","Evosea","Eumycetozoa","Dictyostelia","Dictyosteliales","Dictyosteliaceae","Dictyostelium"],"dataset":[],"UniParc":"UPI0000126ED0","uniref100":"UniRef100_P13022","uniref90":"UniRef90_P13022","uniref50":"UniRef50_P13022","genes":[{"name":{"value":"acpB"},"synonyms":[{"value":"abpD"}],"orfNames":[{"value":"DDB_G0272104"}]}],"alphafold_very_low_content":0.0035587188612099642,"disorder_content":0.03914590747330961,"disprot_consensus":{"full":[{"start":271,"end":281,"type":"D"}],"Structural state":[{"start":271,"end":281,"type":"D"}]}},{"disprot_id":"DP03288","acc":"P13021","creator":"smribeiro","date":"2021-05-10T10:38:06.447Z","features":{"pfam":[{"id":"PF01115","name":"F-actin capping protein, beta subunit","start":7,"end":242}],"gene3D":[]},"length":272,"name":"F-actin-capping protein subunit beta","ncbi_taxon_id":44689,"organism":"Dictyostelium discoideum","regions":[{"start":253,"end":272,"reference_id":"22657106","reference_source":"pmid","reference_html":"Conservation and divergence between cytoplasmic and muscle-specific actin capping proteins: insights from the crystal structure of cytoplasmic Cap32/34 from Dictyostelium discoideum. <i> Eckert C, Goretzki A, Faberova M, Kollmar M. </i> BMC Struct Biol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4AKR"}],"region_id":"DP03288r001","statement":[{"text":"The final model contains residues 2–272 (and 2–270 for the second molecule within the asymmetric unit, respectively) of the 281 residues of the α-subunit and all residues of the β-subunit except for residues 1, 140–145 and 251–272 (253–272 for the second molecule within the asymmetric unit).","type":"Methods"},{"text":"PDB - unmodeled residues 253-272 (chain D)","type":"Curator statement"},{"text":"In contrast to the α-tentacle, neither Cap32/34 nor CapZ crystals grown at physiological pH provided an interpretable electron density for the C-terminal segment of the β-subunit (β-tentacle), indicating that this part of the CP molecule is highly mobile.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":253,"end":272,"reference_id":"22657106","reference_source":"pmid","reference_html":"Conservation and divergence between cytoplasmic and muscle-specific actin capping proteins: insights from the crystal structure of cytoplasmic Cap32/34 from Dictyostelium discoideum. <i> Eckert C, Goretzki A, Faberova M, Kollmar M. </i> BMC Struct Biol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"4AKR"}],"region_id":"DP03288r002","statement":[{"text":"Although the β-tentacle sequence is not conserved in general, the three hydrophobic positions (residues L258, L262, and L266 in GgCapZ) at intervals of four residues are conserved (Figure  5) and exchanging them by polar residues abolishes actin-binding ","type":"Results"},{"text":"Mutational analysis done with His-tagged mouse CP alpha1/beta2 (PMID 20969875) ","type":"Curator statement"}],"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":251,"end":272,"reference_id":"22657106","reference_source":"pmid","reference_html":"Conservation and divergence between cytoplasmic and muscle-specific actin capping proteins: insights from the crystal structure of cytoplasmic Cap32/34 from Dictyostelium discoideum. <i> Eckert C, Goretzki A, Faberova M, Kollmar M. </i> BMC Struct Biol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4AKR"}],"region_id":"DP03288r003","statement":[{"text":"The final model contains residues 2–272 (and 2–270 for the second molecule within the asymmetric unit, respectively) of the 281 residues of the α-subunit and all residues of the β-subunit except for residues 1, 140–145 and 251–272 (253–272 for the second molecule within the asymmetric unit)","type":"Methods"},{"text":"PDB - unmodeled residues 253-272 (Chain B)","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":251,"end":272,"reference_id":"22657106","reference_source":"pmid","reference_html":"Conservation and divergence between cytoplasmic and muscle-specific actin capping proteins: insights from the crystal structure of cytoplasmic Cap32/34 from Dictyostelium discoideum. <i> Eckert C, Goretzki A, Faberova M, Kollmar M. </i> BMC Struct Biol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03288r004","statement":[{"text":"the region around the “basic triad” that harbours many solvent exposed lysines and arginines has been proposed to be the PIP2 binding site of CP. A triple mutation of two of the basic residues of the “basic triad” (K256 and R260) together with a closely located arginine of the β-subunit (R225) has been most effective in abolishing PIP2-binding ","type":"Results"},{"text":"Mutational analysis done with chicken CP α1/β1 (PMID 17182619)","type":"Curator statement"}],"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":253,"end":272,"reference_id":"22657106","reference_source":"pmid","reference_html":"Conservation and divergence between cytoplasmic and muscle-specific actin capping proteins: insights from the crystal structure of cytoplasmic Cap32/34 from Dictyostelium discoideum. <i> Eckert C, Goretzki A, Faberova M, Kollmar M. </i> BMC Struct Biol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03288r005","statement":[{"text":"the region around the “basic triad” that harbours many solvent exposed lysines and arginines has been proposed to be the PIP2 binding site of CP. A triple mutation of two of the basic residues of the “basic triad” (K256 and R260) together with a closely located arginine of the β-subunit (R225) has been most effective in abolishing PIP2-binding ","type":"Results"},{"text":"Mutational analysis done with chicken CP α1/β1 (PMID 17182619)","type":"Curator statement"}],"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":5,"released":"2021_12","sequence":"MTEKQLSCCLDLMRRLPPSQIEDNLAGLLDLVPDLTEDLLSSIDQPLKVAYDAVSKKDYLLCDYNRDADSYRSPWSNKYDPPLSGACYPSSKLRDIEVQANEIFEIYLNLYFEGGVSSVYCWDLDDNFAAVVLMKKTQDQSKKGQPMRGTWDSIHVVEVKLGKKDKAVYKLTSTVMLSIETDNDNTGKVNLAGSLTRQDEKEYTFNEVDTHCVNIGKMVEDMESKLRQTLETIYFGKTKEVVNTLRNATGNSELEKRKNLSNQIGSAIGNRG","taxonomy":["Eukaryota","Amoebozoa","Evosea","Eumycetozoa","Dictyostelia","Dictyosteliales","Dictyosteliaceae","Dictyostelium"],"dataset":[],"UniParc":"UPI0000126EDA","uniref100":"UniRef100_P13021","uniref90":"UniRef90_P13021","uniref50":"UniRef50_P13021","genes":[{"name":{"value":"acpA"},"synonyms":[{"value":"abpE"}],"orfNames":[{"value":"DDB_G0267374"}]}],"alphafold_very_low_content":0.003676470588235294,"disorder_content":0.08088235294117647,"disprot_consensus":{"full":[{"start":251,"end":272,"type":"D"}],"Structural state":[{"start":251,"end":272,"type":"D"}],"Molecular function":[{"start":251,"end":272,"type":"F"}]}},{"disprot_id":"DP03289","acc":"P0ACG8","creator":"csanchezrocha","date":"2021-05-10T10:51:44.560Z","features":{"pfam":[{"id":"PF01479","name":"S4 domain","start":9,"end":53},{"id":"PF28601","name":"Heat shock protein 15, C-terminal region","start":89,"end":133}],"gene3D":[]},"length":133,"name":"Heat shock protein 15","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":111,"end":133,"reference_id":"10675344","reference_source":"pmid","reference_html":"Structure of Hsp15 reveals a novel RNA-binding motif. <i> Staker BL, Korber P, Bardwell JC, Saper MA. </i> EMBO J, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1DM9"}],"region_id":"DP03289r001","statement":[{"text":"The electron density ends at approximately residue 110, leaving 23 residues unaccounted for in the electron density. Mass spectrometry of the crystals reveals completely intact protein of ~133 amino acids, suggesting that the unobserved residues are present in the crystal lattice but not visible in the electron density.","type":"Results"},{"text":"The C-terminal 23 residues were never visible in electron density maps despite map improvement and refinement, and are presumably disordered, which may contribute to the observed R-factors.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-11-19T18:24:12.249Z"}}],"regions_counter":1,"released":"2021_12","sequence":"MKEKPAVEVRLDKWLWAARFYKTRALAREMIEGGKVHYNGQRSKPSKIVELNATLTLRQGNDERTVIVKAITEQRRPASEAALLYEETAESVEKREKMALARKLNALTMPHPDRRPDKKERRDLLRFKHGDSE","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":["Stress response proteins"],"UniParc":"UPI000011103C","uniref100":"UniRef100_P0ACH0","uniref90":"UniRef90_P0ACH0","uniref50":"UniRef50_P0ACH0","genes":[{"name":{"value":"hslR"},"synonyms":[{"value":"yrfH"}],"olnNames":[{"value":"b3400"},{"value":"JW3363"}]}],"alphafold_very_low_content":0.03007518796992481,"disorder_content":0.17293233082706766,"disprot_consensus":{"full":[{"start":111,"end":133,"type":"D"}],"Structural state":[{"start":111,"end":133,"type":"D"}]}},{"disprot_id":"DP03290","acc":"Q8RNT4","creator":"smribeiro","date":"2021-05-10T11:27:51.254Z","features":{"pfam":[{"id":"PF00305","name":"Lipoxygenase","start":227,"end":667}],"gene3D":[]},"length":685,"name":"Linoleate 9/13-lipoxygenase","ncbi_taxon_id":287,"organism":"Pseudomonas aeruginosa","regions":[{"start":19,"end":49,"reference_id":"23985801","reference_source":"pmid","reference_html":"Structure and interaction with phospholipids of a prokaryotic lipoxygenase from Pseudomonas aeruginosa. <i> Garreta A, Val-Moraes SP, García-Fernández Q, Busquets M, Juan C, Oliver A, Ortiz A, Gaffney BJ, Fita I, Manresa À, Carpena X. </i> FASEB J, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4G32"}],"region_id":"DP03290r001","statement":[{"text":"PDB - unmodeled residues 19-49","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":19,"end":49,"reference_id":"23985801","reference_source":"pmid","reference_html":"Structure and interaction with phospholipids of a prokaryotic lipoxygenase from Pseudomonas aeruginosa. <i> Garreta A, Val-Moraes SP, García-Fernández Q, Busquets M, Juan C, Oliver A, Ortiz A, Gaffney BJ, Fita I, Manresa À, Carpena X. </i> FASEB J, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4G33"}],"region_id":"DP03290r002","statement":[{"text":"the 2 Pa_LOX structures available differ mainly in the N-terminal region, with models starting at residues Ile50 (Fig. 1A) and Ala19 (Fig. 1B).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":19,"end":49,"reference_id":"23985801","reference_source":"pmid","reference_html":"Structure and interaction with phospholipids of a prokaryotic lipoxygenase from Pseudomonas aeruginosa. <i> Garreta A, Val-Moraes SP, García-Fernández Q, Busquets M, Juan C, Oliver A, Ortiz A, Gaffney BJ, Fita I, Manresa À, Carpena X. </i> FASEB J, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"4G33"}],"region_id":"DP03290r003","statement":[{"text":"The longer N-terminal tail of the structure starting at Ala19 protrudes toward a neighboring molecule, where it is stabilized by a large number of interactions, in particular with the polar head of the phospholipid","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":3,"released":"2021_12","sequence":"MKRRSVLLSGVALSGTALANDSIFFSPLKYLGAEQQRSIDASRSLLDNLIPPSLPQYDNLAGKLARRAVLTSKKLVYVWTENFANVKGVPMARSVPLGELPNVDWLLKTAGVIVELIVNFVASLPASAAAQFERIAAGLSGDLEAARQVHEALLEEAKNDPAAAGSLLLRFTELQTRVIALLTRVGLLVDDILKSASNLVTQGGQGDGLNRFRAVFGTLRLPEVADSFRDDEAFAYWRVAGPNPLLIRRVDALPANFPLGEEQFRRVMGADDSLLEAAASRRLYLLDYAELGKLAPSGAVDKLLTGTGFAYAPIALFALGKDRAGLLPVAIQCGQDPATHPMFVRPAESESDLYWGWQMAKTVVQVAEENYHEMFVHLAQTHLVSEAFCLATQRTLAPSHPLHVLLAPHFEGTLFINEGAARILLPSAGFIDVMFAAPIQDTQATAGGNRLGFDFYRGMLPESLKARNVDDPAALPDYPYRDDGLLVWNAIRQWAADYVAVYYASDGDVTADVELAAWVGEVIGSGKVAGFRPITGRSQLVEVLTMVIFTASAQHAAVNFPQPSMMTYAPAICAMSAAPAPDSPSGKSEADWLKMMPPTLVALEKVNIYHLLGSVYHGRLGDYRQTGFPYAPVFSDRRVTASGGPLERFQARLKEVEATIRTRNQARRKPYEYLLPSRIPASTNI","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Pseudomonadales","Pseudomonadaceae","Pseudomonas"],"dataset":[],"UniParc":"UPI0001C239BE","uniref100":"UniRef100_Q8RNT4","uniref90":"UniRef90_Q8RNT4","uniref50":"UniRef50_Q8RNT4","genes":[{"name":{"value":"lox"}}],"alphafold_very_low_content":0.029197080291970802,"disorder_content":0.04525547445255475,"disprot_consensus":{"full":[{"start":19,"end":49,"type":"T"}],"Structural state":[{"start":19,"end":49,"type":"D"}],"Structural transition":[{"start":19,"end":49,"type":"T"}],"Molecular function":[{"start":19,"end":49,"type":"F"}]}},{"disprot_id":"DP03291","acc":"Q9UK55","creator":"spenadias","date":"2021-05-10T14:19:56.960Z","features":{"pfam":[{"id":"PF00079","name":"Serpin (serine protease inhibitor)","start":79,"end":441}],"gene3D":[]},"length":444,"name":"Protein Z-dependent protease inhibitor","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":22,"end":59,"reference_id":"19528533","reference_source":"pmid","reference_html":"Crystal structure of protein Z-dependent inhibitor complex shows how protein Z functions as a cofactor in the membrane inhibition of factor X. <i> Wei Z, Yan Y, Carrell RW, Zhou A. </i> Blood, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3F1S"}],"region_id":"DP03291r001","statement":[{"text":"The first 38 residues of ZPI, which include many acidic amino acids, are disordered and were not built in the structure","type":"Results"},{"text":"According to PDB available sequence, the 38 firsts residues correspond to the annotated region (22-59) as the protein structure is built from A60, considered in the structure as residue 39. Residues 1-21 correspond to the signal peptide","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T07:40:40.604Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":22,"end":60,"reference_id":"20427285","reference_source":"pmid","reference_html":"Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa. <i> Huang X, Dementiev A, Olson ST, Gettins PG. </i> J Biol Chem, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3H5C"}],"region_id":"DP03291r002","statement":[{"text":"For the ZPI moiety, the whole of the backbone is visible (Fig.1A), with the exception of the first 39 residues, all of which are part of the N-terminal tail, which is an extension that is not present in other serpins. ","type":"Results"},{"text":"According to PDB available sequence, the 39 firsts residues correspond to the annotated region (22-60). Residues 1-21 correspond to the signal peptide","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-31T09:03:41.050Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_06","sequence":"MKVVPSLLLSVLLAQVWLVPGLAPSPQSPETPAPQNQTSRVVQAPKEEEEDEQEASEEKASEEEKAWLMASRQQLAKETSNFGFSLLRKISMRHDGNMVFSPFGMSLAMTGLMLGATGPTETQIKRGLHLQALKPTKPGLLPSLFKGLRETLSRNLELGLTQGSFAFIHKDFDVKETFFNLSKRYFDTECVPMNFRNASQAKRLMNHYINKETRGKIPKLFDEINPETKLILVDYILFKGKWLTPFDPVFTEVDTFHLDKYKTIKVPMMYGAGKFASTFDKNFRCHVLKLPYQGNATMLVVLMEKMGDHLALEDYLTTDLVETWLRNMKTRNMEVFFPKFKLDQKYEMHELLRQMGIRRIFSPFADLSELSATGRNLQVSRVLQRTVIEVDERGTEAVAGILSEITAYSMPPVIKVDRPFHFMIYEETSGMLLFLGRVVNPTLL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000013C46E","uniref100":"UniRef100_Q9UK55","uniref90":"UniRef90_Q9UK55","uniref50":"UniRef50_Q9UK55","genes":[{"name":{"value":"SERPINA10"},"synonyms":[{"value":"ZPI"}],"orfNames":[{"value":"UNQ707/PRO1358"}]}],"alphafold_very_low_content":0.1373873873873874,"disorder_content":0.08783783783783784,"disprot_consensus":{"full":[{"start":22,"end":60,"type":"D"}],"Structural state":[{"start":22,"end":60,"type":"D"}]}},{"disprot_id":"DP03292","acc":"P00742","creator":"spenadias","date":"2021-05-10T15:04:03.404Z","features":{"pfam":[{"id":"PF00008","name":"EGF-like domain","start":90,"end":120},{"id":"PF00089","name":"Trypsin","start":235,"end":462},{"id":"PF00594","name":"Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain","start":45,"end":85},{"id":"PF14670","name":"Coagulation Factor Xa inhibitory site","start":129,"end":164}],"gene3D":[]},"length":488,"name":"Coagulation factor X","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":90,"end":120,"reference_id":"10966741","reference_source":"pmid","reference_html":"Crystal structures of human factor Xa complexed with potent inhibitors. <i> Maignan S, Guilloteau JP, Pouzieux S, Choi-Sledeski YM, Becker MR, Klein SI, Ewing WR, Pauls HW, Spada AP, Mikol V. </i> J Med Chem, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1EZQ"},{"db":"PDB","id":"1F0S"},{"db":"PDB","id":"1F0R"}],"region_id":"DP03292r001","statement":[{"text":"All atoms of the inhibitors and of FXa lie in well-defined electron density except the EGF1 domain which was not visible","type":"Methods"},{"text":"EGF1 domain is comprised on residues 90-120","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":90,"end":120,"reference_id":"8939944","reference_source":"pmid","reference_html":"X-ray structure of active site-inhibited clotting factor Xa. Implications for drug design and substrate recognition. <i> Brandstetter H, Kühne A, Bode W, Huber R, von der Saal W, Wirthensohn K, Engh RA. </i> J Biol Chem, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1FAX"}],"region_id":"DP03292r002","statement":[{"text":"The EGF1 domain, disordered in the tetragonal, arginine-bound crystal form, was suggested to become ordered in the presence of calcium (24). However, the orthorhombic crystals of fXazDX-9065a grown at 10 mM calcium also show apparent disorder of the EGF1 domain. Furthermore, the crystal packing of the two crystal forms is not compatible with a unique EGF1 orientation (relative to EGF2)","type":"Results"},{"text":"EGF1 domain is comprised on residues 90-120","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":90,"end":126,"reference_id":"11027132","reference_source":"pmid","reference_html":"Preparation, characterization, and the crystal structure of the inhibitor ZK-807834 (CI-1031) complexed with factor Xa. <i> Adler M, Davey DD, Phillips GB, Kim SH, Jancarik J, Rumennik G, Light DR, Whitlow M. </i> Biochemistry, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1FJS"}],"region_id":"DP03292r003","statement":[{"text":"The electron density for the factor Xa/ZK-807834 complex indicates that the first residue in the light chain is Lys-L87 and no electron density was observed for the EGF1 domain. ","type":"Results"},{"text":"EGF1 domain is comprised on residues 90-120","type":"Curator statement"},{"text":"Lys-L87 corresponds to Lys 127 in protein original sequence","type":"Curator statement"},{"text":"However, the protein used by Kamata et al. (9) included the first EGF domain of factor Xa, which was apparently missing from our own construct","type":"Methods"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":90,"end":120,"reference_id":"12061878","reference_source":"pmid","reference_html":"Design and quantitative structure-activity relationship of 3-amidinobenzyl-1H-indole-2-carboxamides as potent, nonchiral, and selective inhibitors of blood coagulation factor Xa. <i> Matter H, Defossa E, Heinelt U, Blohm PM, Schneider D, Müller A, Herok S, Schreuder H, Liesum A, Brachvogel V, Lönze P, Walser A, Al-Obeidi F, Wildgoose P. </i> J Med Chem, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1LPG"},{"db":"PDB","id":"1LPK"},{"db":"PDB","id":"1LPZ"},{"db":"PDB","id":"1LQD"}],"region_id":"DP03292r004","statement":[{"text":"The EGF-1 domain is not visible in the electron density maps probably because of disorder, and the rather high free R factors might relate to this disordered EGF-1 domain. ","type":"Results"},{"text":"EGF1 domain is comprised on residues 90-120","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":90,"end":120,"reference_id":"12593649","reference_source":"pmid","reference_html":"Molecular structures of human factor Xa complexed with ketopiperazine inhibitors: preference for a neutral group in the S1 pocket. <i> Maignan S, Guilloteau JP, Choi-Sledeski YM, Becker MR, Ewing WR, Pauls HW, Spada AP, Mikol V. </i> J Med Chem, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1NFU"},{"db":"PDB","id":"1NFY"},{"db":"PDB","id":"1NFW"},{"db":"PDB","id":"1NFX"}],"region_id":"DP03292r005","statement":[{"text":"All atoms of the inhibitors and of fXa lie in well-defined electron density except the EGF1 domain that was not visible.","type":"Methods"},{"text":"EGF1 domain is comprised on residues 90-120","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":90,"end":120,"reference_id":"8355279","reference_source":"pmid","reference_html":"Structure of human des(1-45) factor Xa at 2.2 A resolution. <i> Padmanabhan K, Padmanabhan KP, Tulinsky A, Park CH, Bode W, Huber R, Blankenship DT, Cardin AD, Kisiel W. </i> J Mol Biol, 1993","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1HCG"}],"region_id":"DP03292r006","statement":[{"text":"X-ray structure analysis confirmed the biochemical characterisation and also revealed that the N-terminal epidermal growth factor (EGF)-like domain is flexibly disordered in crystals","type":"Abstract"},{"text":"We report here the molecular consituents of these chemically characterized FXa crystals and the refined strcuture of the truncated FXa molecule (Fig. 1), which consists of the second EGF module, the catalytic domain of activated factor X and a flexibly disordered N-terminal EGF. ","type":"Introduction"},{"text":"EGF1 domain is comprised on residues 90-120","type":"Curator statement"},{"text":"This led us to conclude that the first EGF domain might be flexibly disordered so that subsequent refinement was based upon this premise","type":"Methods"},{"text":"However, there was no indication of a Gla domain and the N-terminal EGF module still remained disordered","type":"Methods"},{"text":"The final electron and difference density maps showed no evidence of a Gla domain or the N-terminal EGF module","type":"Methods"},{"text":"Due to the disorder of the first EGF module, however, the FXa structure described here begins with Cys389 (Fig. 1)","type":"Results"},{"text":"In contrast to the foregoing, the final electron density did not show any region assignable to the N-terminal EGF domain of FXa. Since biochemical analysis indicated presence of the module, it must be concluded that it is flexibly disordered in the crystal about its heptapeptide interdomain bridge (Fig. 1).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":90,"end":120,"reference_id":"15857135","reference_source":"pmid","reference_html":"Structural requirements for factor Xa inhibition by 3-oxybenzamides with neutral P1 substituents: combining X-ray crystallography, 3D-QSAR, and tailored scoring functions. <i> Matter H, Will DW, Nazaré M, Schreuder H, Laux V, Wehner V. </i> J Med Chem, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2BMG"}],"region_id":"DP03292r007","statement":[{"text":"The EGF-1 domain is not visible in the electron density maps probably because of disorder, and the rather high free R factors might relate to this disordered EGF-1 domain.","type":"Abstract"},{"text":"EGF1 domain is comprised on residues 90-120","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":90,"end":120,"reference_id":"15999990","reference_source":"pmid","reference_html":"Probing the subpockets of factor Xa reveals two binding modes for inhibitors based on a 2-carboxyindole scaffold: a study combining structure-activity relationship and X-ray crystallography. <i> Nazaré M, Will DW, Matter H, Schreuder H, Ritter K, Urmann M, Essrich M, Bauer A, Wagner M, Czech J, Lorenz M, Laux V, Wehner V. </i> J Med Chem, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2BQ7"},{"db":"PDB","id":"2BOH"},{"db":"PDB","id":"2BQW"},{"db":"PDB","id":"2BQ6"}],"region_id":"DP03292r008","statement":[{"text":"The EGF-1 domain is not visible in the electron density maps probably because of disorder, and the rather high free R-factors might relate to this disordered EGF-1 domain.","type":"Abstract"},{"text":"EGF1 domain is comprised on residues 90-120","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":90,"end":120,"reference_id":"12834348","reference_source":"pmid","reference_html":"The extended interactions and Gla domain of blood coagulation factor Xa. <i> Wang SX, Hur E, Sousa CA, Brinen L, Slivka EJ, Fletterick RJ. </i> Biochemistry, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1P0S"}],"region_id":"DP03292r009","statement":[{"text":" Surprisingly, the N-terminal EGF domain (EGF1) was found to be disordered. Numerous sparse density peaks in this region were observed in electron density maps, but efforts to trace a backbone through these\npeaks did not improve refinement statistics or result in improved density. The EGF1 domain was therefore omitted from the model","type":"Results"},{"text":"EGF1 domain is comprised on residues 90-120","type":"Curator statement"},{"text":"The EGF1 domain (transparent white) was disordered and modeled using the EGF1 domain from PDB 1XKA.","type":"Figure"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":90,"end":120,"reference_id":"17173931","reference_source":"pmid","reference_html":"Intermolecular interactions and characterization of the novel factor Xa exosite involved in macromolecular recognition and inhibition: crystal structure of human Gla-domainless factor Xa complexed with the anticoagulant protein NAPc2 from the hematophagous nematode Ancylostoma caninum. <i> Murakami MT, Rios-Steiner J, Weaver SE, Tulinsky A, Geiger JH, Arni RK. </i> J Mol Biol, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2H9E"}],"region_id":"DP03292r010","statement":[{"text":"The entire N-terminal EGF1 domain, and its leading pentapeptide, which is flexibly disordered in other des-fXastructures was not located in the electron density maps. ","type":"Results"},{"text":"EGF1 domain is comprised on residues 90-120","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":90,"end":120,"reference_id":"17338508","reference_source":"pmid","reference_html":"Factor Xa inhibitors: S1 binding interactions of a series of N-{(3S)-1-[(1S)-1-methyl-2-morpholin-4-yl-2-oxoethyl]-2-oxopyrrolidin-3-yl}sulfonamides. <i> Chan C, Borthwick AD, Brown D, Burns-Kurtis CL, Campbell M, Chaudry L, Chung CW, Convery MA, Hamblin JN, Johnstone L, Kelly HA, Kleanthous S, Patikis A, Patel C, Pateman AJ, Senger S, Shah GP, Toomey JR, Watson NS, Weston HE, Whitworth C, Young RJ, Zhou P. </i> J Med Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4Y76"},{"db":"PDB","id":"4Y79"},{"db":"PDB","id":"2J94"},{"db":"PDB","id":"2J95"}],"region_id":"DP03292r011","statement":[{"text":"The majority of the rest of the protein is in well-determined electron density, except for the EGF1 domain, which was not visible.","type":"Methods"},{"text":"EGF1 domain is comprised on residues 90-120","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":90,"end":120,"reference_id":"17588602","reference_source":"pmid","reference_html":"Active and exo-site inhibition of human factor Xa: structure of des-Gla factor Xa inhibited by NAP5, a potent nematode anticoagulant protein from Ancylostoma caninum. <i> Rios-Steiner JL, Murakami MT, Tulinsky A, Arni RK. </i> J Mol Biol, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2P3F"}],"region_id":"DP03292r012","statement":[{"text":"In addition, the whole N-terminal EGF1 module, and its leading pentapeptide, is flexibly disordered as in other des-fXa structures","type":"Results"},{"text":"EGF1 domain is comprised on residues 90-120","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":90,"end":120,"reference_id":"16529937","reference_source":"pmid","reference_html":"The discovery of glycine and related amino acid-based factor Xa inhibitors. <i> Kohrt JT, Filipski KJ, Cody WL, Bigge CF, La F, Welch K, Dahring T, Bryant JW, Leonard D, Bolton G, Narasimhan L, Zhang E, Peterson JT, Haarer S, Sahasrabudhe V, Janiczek N, Desiraju S, Hena M, Fiakpui C, Saraswat N, Sharma R, Sun S, Maiti SN, Leadley R, Edmunds JJ. </i> Bioorg Med Chem, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2Q1J"}],"region_id":"DP03292r013","statement":[{"text":"There is no electron density observed for the first EGF domain, thus models for the EGF1 domain were not included in subsequent refinement steps.","type":"Results"},{"text":"EGF1 domain is comprised on residues 90-120","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":99,"end":116,"reference_id":"31659163","reference_source":"pmid","reference_html":"Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern. <i> Pfeffer I, Brewitz L, Krojer T, Jensen SA, Kochan GT, Kershaw NJ, Hewitson KS, McNeill LA, Kramer H, Münzel M, Hopkinson RJ, Oppermann U, Handford PA, McDonough MA, Schofield CJ. </i> Nat Commun, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5JZU"},{"db":"PDB","id":"5JQY"},{"db":"PDB","id":"5JZ8"},{"db":"PDB","id":"6RK9"}],"region_id":"DP03292r014","statement":[{"text":"AspH-TPR-Ox was successfully co-crystallized with a 39- residue fragment of hFX EGF1 (AspH-TPR-Ox:hFX, Fig. 3 and Supplementary Fig. 9). The AspH-TPR-Ox structure reveals electron density at the active site corresponding to 18 of the 39 hFX EGF1 substrate residues (aa 99–116: -GKC3KDGLGEYTC4TC5LEGF-) and for a disulfide linkage between Cys101hFX and Cys110hFX (Fig. 3e). Highly specific interactions, including multiple protein–protein/peptide interactions with both AspH-Ox and TPR domains are apparent (Fig. 3b–d). The N-terminal region of hFX (aa 100–105) interacts with the AspH-Ox domain and the C-terminal region of hFX (aa 106–116) interacts with the TPR domain","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":106,"end":116,"reference_id":"31659163","reference_source":"pmid","reference_html":"Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern. <i> Pfeffer I, Brewitz L, Krojer T, Jensen SA, Kochan GT, Kershaw NJ, Hewitson KS, McNeill LA, Kramer H, Münzel M, Hopkinson RJ, Oppermann U, Handford PA, McDonough MA, Schofield CJ. </i> Nat Commun, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"5JZU"},{"db":"PDB","id":"5JQY"},{"db":"PDB","id":"5JZ8"},{"db":"PDB","id":"6RK9"}],"region_id":"DP03292r015","statement":[{"text":"Highly specific interactions, including multiple protein–protein/peptide interactions with both AspH-Ox and TPR domains are apparent (Fig. 3b–d). The N-terminal region of hFX (aa 100–105) interacts with the AspH-Ox domain and the C-terminal region of hFX (aa 106–116) interacts with the TPR domain","type":"Results"}],"interaction_partner":[{"db":"UniProt","id":"Q12797","partner_start":null,"partner_end":null}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":100,"end":105,"reference_id":"31659163","reference_source":"pmid","reference_html":"Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern. <i> Pfeffer I, Brewitz L, Krojer T, Jensen SA, Kochan GT, Kershaw NJ, Hewitson KS, McNeill LA, Kramer H, Münzel M, Hopkinson RJ, Oppermann U, Handford PA, McDonough MA, Schofield CJ. </i> Nat Commun, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"5JZU"},{"db":"PDB","id":"5JQY"},{"db":"PDB","id":"5JZ8"},{"db":"PDB","id":"6RK9"}],"region_id":"DP03292r016","statement":[{"text":"Highly specific interactions, including multiple protein–protein/peptide interactions with both AspH-Ox and TPR domains are apparent (Fig. 3b–d). The N-terminal region of hFX (aa 100–105) interacts with the AspH-Ox domain and the C-terminal region of hFX (aa 106–116) interacts with the TPR domain","type":"Results"}],"interaction_partner":[{"db":"UniProt","id":"Q12797","partner_start":null,"partner_end":null}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":16,"released":"2021_12","sequence":"MGRPLHLVLLSASLAGLLLLGESLFIRREQANNILARVTRANSFLEEMKKGHLERECMEETCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNNLTRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000016A93C","uniref100":"UniRef100_P00742","uniref90":"UniRef90_P00742","uniref50":"UniRef50_P00742","genes":[{"name":{"value":"F10"}}],"alphafold_very_low_content":0.13729508196721313,"disorder_content":0.07581967213114754,"disprot_consensus":{"full":[{"start":90,"end":98,"type":"D"},{"start":99,"end":116,"type":"T"},{"start":117,"end":126,"type":"D"}],"Structural state":[{"start":90,"end":126,"type":"D"}],"Structural transition":[{"start":99,"end":116,"type":"T"}],"Molecular function":[{"start":100,"end":116,"type":"F"}]}},{"disprot_id":"DP03293","acc":"O43791","creator":"fquaglia","date":"2021-05-11T10:29:53.020Z","features":{"pfam":[{"id":"PF00651","name":"BTB/POZ domain","start":192,"end":296},{"id":"PF22486","name":"MATH domain","start":33,"end":161},{"id":"PF24570","name":"BPM/SPOP, BACK domain","start":301,"end":351}],"gene3D":[]},"length":374,"name":"Speckle-type POZ protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":357,"end":374,"reference_id":"23999291","reference_source":"pmid","reference_html":"Structural basis of high-order oligomerization of the cullin-3 adaptor SPOP. <i> van Geersdaele LK, Stead MA, Harrison CM, Carr SB, Close HJ, Rosbrook GO, Connell SD, Wright SC. </i> Acta Crystallogr D Biol Crystallogr, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4J8Z"}],"region_id":"DP03293r001","statement":[{"text":"No electron density was observed for the residues comprising the predicted nuclear localization signal (residues 360–374) and BTB5–6 (residues 270–295), and they were not built in the model;","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:38:32.835Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":169,"end":178,"reference_id":"23999291","reference_source":"pmid","reference_html":"Structural basis of high-order oligomerization of the cullin-3 adaptor SPOP. <i> van Geersdaele LK, Stead MA, Harrison CM, Carr SB, Close HJ, Rosbrook GO, Connell SD, Wright SC. </i> Acta Crystallogr D Biol Crystallogr, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"4J8Z"}],"region_id":"DP03293r002","statement":[{"text":"No electron density was observed for residues 169–176 and 357–374 of SPOP169–374 Y353E, and residues comprising the 3–4loop were associated with higher crystallographic B factors, as reported previously (Zhuanget  al., 2009; Erringtonet  al.,2012).","type":"Results"},{"text":"Human SPOP is a 374-residue protein that contains an N-terminal MATH domain (residues 28–166) that recruits substrates and a central BTB domain (residues 177–296) that mediates dimerization and interactions with Cul3 (Fig. 1a).","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:38:39.821Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":169,"end":178,"reference_id":"23999291","reference_source":"pmid","reference_html":"Structural basis of high-order oligomerization of the cullin-3 adaptor SPOP. <i> van Geersdaele LK, Stead MA, Harrison CM, Carr SB, Close HJ, Rosbrook GO, Connell SD, Wright SC. </i> Acta Crystallogr D Biol Crystallogr, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4J8Z"}],"region_id":"DP03293r003","statement":[{"text":"No electron density was observed for residues 169–176 and 357–374 of SPOP169–374 Y353E, and residues comprising the 3–4loop were associated with higher crystallographic B factors, as reported previously (Zhuanget  al., 2009; Erringtonet  al.,2012).","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:38:31.839Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":361,"end":374,"reference_id":"31624231","reference_source":"pmid","reference_html":"SPOP suppresses pancreatic cancer progression by promoting the degradation of NANOG. <i> Tan P, Xu Y, Du Y, Wu L, Guo B, Huang S, Zhu J, Li B, Lin F, Yao L. </i> Cell Death Dis, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03293r004","statement":[{"text":"Co-immunoprecipitation experiments in SW1990 cells showed that SPOP interacted with the stem-cell marker NANOG, and this interaction has recently been shown to play a critical role in regulating progression of prostate cancer. We showed that, in one patient with pancreatic cancer, the expression of a truncated form of SPOP (p.Q360*) lacking the nuclear localization signal led to nuclear accumulation of NANOG, which promoted growth and metastasis of pancreatic cancer cells. Our results suggest that SPOP suppresses progression of pancreatic cancer by promoting the ubiquitination and subsequent degradation of NANOG. These results identify the SPOP-NANOG interaction as a potential therapeutic target against pancreatic cancer.","type":"Abstract"},{"text":"Since the Q360* mutation is located in the linker between the BTB domain and the nuclear localization sequence, we speculated that the mutated SPOP sequence containing the C1078T mutation encodes a truncated protein without the nuclear localization sequence (Supplementary Fig. 1a-c). Indeed, fluorescence microscopy and nuclear/cytoplasmic separation showed that SPOP-WT mainly located in cell nucleus, SPOP-Q360* mainly located in cell cytoplasm, NANOG localized predominantly in the nucleus (Fig. 7b, c).","type":"Results"},{"text":"The inability of SPOP-Q360* to accumulate in the nucleus was associated with an inability to bind importin subunit alpha-6 and 7 (IPOA6 and IPOA7), a shuttle carrier between nucleus and cytoplasm (Supplementary Fig. 2).","type":"Results"},{"text":"The patient-derived Q360* mutation disrupts nuclear localization of SPOP and impairs the SPOP-mediated poly-ubiquitination and degradation of NANOG.","type":"Figure"},{"text":"These results suggest that the Q360* mutation alters SPOP localization and allows hyperaccumulation of NANOG in the nucleus, where it can promote cell proliferation.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:38:37.666Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":361,"end":374,"reference_id":"31624231","reference_source":"pmid","reference_html":"SPOP suppresses pancreatic cancer progression by promoting the degradation of NANOG. <i> Tan P, Xu Y, Du Y, Wu L, Guo B, Huang S, Zhu J, Li B, Lin F, Yao L. </i> Cell Death Dis, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03293r005","statement":[{"text":"Co-immunoprecipitation experiments in SW1990 cells showed that SPOP interacted with the stem-cell marker NANOG, and this interaction has recently been shown to play a critical role in regulating progression of prostate cancer. We showed that, in one patient with pancreatic cancer, the expression of a truncated form of SPOP (p.Q360*) lacking the nuclear localization signal led to nuclear accumulation of NANOG, which promoted growth and metastasis of pancreatic cancer cells. Our results suggest that SPOP suppresses progression of pancreatic cancer by promoting the ubiquitination and subsequent degradation of NANOG. These results identify the SPOP-NANOG interaction as a potential therapeutic target against pancreatic cancer.","type":"Abstract"},{"text":"SPOP-Q360* repressed levels of NANOG and other downstream proteins to a much weaker extent than SPOP-WT (Fig. 7d), and these results were associated with impaired interaction between SPOP and NANOG, as well as impaired ubiquitination of NANOG (Fig. 7e, f).","type":"Results"},{"text":"The patient-derived Q360* mutation disrupts nuclear localization of SPOP and impairs the SPOP-mediated poly-ubiquitination and degradation of NANOG.","type":"Figure"},{"text":"These results suggest that the Q360* mutation alters SPOP localization and allows hyperaccumulation of NANOG in the nucleus, where it can promote cell proliferation.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:38:34.851Z"},"ec_go":"IEP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":361,"end":374,"reference_id":"31624231","reference_source":"pmid","reference_html":"SPOP suppresses pancreatic cancer progression by promoting the degradation of NANOG. <i> Tan P, Xu Y, Du Y, Wu L, Guo B, Huang S, Zhu J, Li B, Lin F, Yao L. </i> Cell Death Dis, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007634","ec_ontology":"ECO","ec_name":"experimental phenotypic evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03293r006","statement":[{"text":"Co-immunoprecipitation experiments in SW1990 cells showed that SPOP interacted with the stem-cell marker NANOG, and this interaction has recently been shown to play a critical role in regulating progression of prostate cancer. We showed that, in one patient with pancreatic cancer, the expression of a truncated form of SPOP (p.Q360*) lacking the nuclear localization signal led to nuclear accumulation of NANOG, which promoted growth and metastasis of pancreatic cancer cells. Our results suggest that SPOP suppresses progression of pancreatic cancer by promoting the ubiquitination and subsequent degradation of NANOG. These results identify the SPOP-NANOG interaction as a potential therapeutic target against pancreatic cancer.","type":"Abstract"},{"text":"To examine how the patient-derived Q360* mutation may disrupt the tumor-suppressive role of SPOP in pancreatic cancer, we transiently upregulated expression of SPOP-WT or SPOP-Q360* in cells overexpressing NANOG. We found that the Q360* mutation weakened the antiproliferative effect of SPOP under these conditions (Fig. 7a).","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:38:34.009Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":6,"released":"2021_12","sequence":"MSRVPSPPPPAEMSSGPVAESWCYTQIKVVKFSYMWTINNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEESKDYLSLYLLLVSCPKSEVRAKFKFSILNAKGEETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQDSVNISGQNTMNMVKVPECRLADELGGLWENSRFTDCCLCVAGQEFQAHKAILAARSPVFSAMFEHEMEESKKNRVEINDVEPEVFKEMMCFIYTGKAPNLDKMADDLLAAADKYALERLKVMCEDALCSNLSVENAAEILILADLHSADQLKTQAVDFINYHASDVLETSGWKSMVVSHPHLVAEAYRSLASAQCPFLGPPRKRLKQS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins","NDDs-related proteins","Condensates-related proteins"],"UniParc":"UPI0000003F5C","uniref100":"UniRef100_O43791","uniref90":"UniRef90_O43791","uniref50":"UniRef50_O43791","genes":[{"name":{"value":"SPOP","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11254","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11254"}}]}}],"alphafold_very_low_content":0.053475935828877004,"disorder_content":0.0748663101604278,"disprot_consensus":{"full":[{"start":169,"end":178,"type":"D"},{"start":357,"end":374,"type":"D"}],"Structural state":[{"start":169,"end":178,"type":"D"},{"start":357,"end":374,"type":"D"}],"Disorder function":[{"start":169,"end":178,"type":"F"}],"Biological process":[{"start":361,"end":374,"type":"F"}],"Molecular function":[{"start":361,"end":374,"type":"F"}]}},{"disprot_id":"DP03294","acc":"P02760","creator":"vacs","date":"2021-05-11T11:37:46.659Z","features":{"pfam":[{"id":"PF00014","name":"Kunitz/Bovine pancreatic trypsin inhibitor domain","start":231,"end":282},{"id":"PF00014","name":"Kunitz/Bovine pancreatic trypsin inhibitor domain","start":286,"end":337},{"id":"PF00061","name":"Lipocalin / cytosolic fatty-acid binding protein family","start":42,"end":184}],"gene3D":[]},"length":352,"name":"Protein AMBP","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":340,"end":352,"reference_id":"9566199","reference_source":"pmid","reference_html":"The crystal structure of bikunin from the inter-alpha-inhibitor complex: a serine protease inhibitor with two Kunitz domains. <i> Xu Y, Carr PD, Guss JM, Ollis DL. </i> J Mol Biol, 1998","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1BIK"}],"region_id":"DP03294r001","statement":[{"text":"There was no electron density for residues 1 to 24 or 135 to 145. The C-terminal residues are probably disordered.","type":"Results"},{"text":"Region 135-147 is not visible in the structure, which corresponds to region 340-352 of the amino acid sequence. Protein AMBP is proteolitically cleaved into separately functioning proteins. This region is part of protein bikunin.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-20T16:05:29.331Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":206,"end":229,"reference_id":"9566199","reference_source":"pmid","reference_html":"The crystal structure of bikunin from the inter-alpha-inhibitor complex: a serine protease inhibitor with two Kunitz domains. <i> Xu Y, Carr PD, Guss JM, Ollis DL. </i> J Mol Biol, 1998","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1BIK"}],"region_id":"DP03294r002","statement":[{"text":"There was no electron density for residues 1 to 24 or 135 to 145.","type":"Results"},{"text":"Bikunin has two glycosylation sites, residues Ser10 and Asn45. Ser10 is the more heavily glycosylated (Hochstrasser et al., 1981) but it is in a section of peptide that is not visible in our maps.","type":"Results"},{"text":"The IDR characterized in the publication and spanning residues 1-24 corresponds to region 206-229 of the amino acid sequence. Protein AMBP is proteolitically cleaved into separately functioning proteins. This region is part of protein bikunin.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-20T16:05:29.987Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":191,"end":202,"reference_id":"22512701","reference_source":"pmid","reference_html":"The crystal structure of human α(1)-microglobulin reveals a potential haem-binding site. <i> Meining W, Skerra A. </i> Biochem J, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3QKG"}],"region_id":"DP03294r003","statement":[{"text":"The first seven N-terminal residues, Gly1–Pro7, and the C-terminal residues Gly172–Lys193, as well as the Strep-tag II were not visible in the electron density map and hence were omitted from the final model.","type":"Results"},{"text":"Region 172-183 of the protein is not visible in the structure, which corresponds to region 191-202 of the associated UniProt sequence. Protein AMBP is proteolitically cleaved into separately functioning proteins. This region is part of protein α1-microglobulin.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-20T16:05:30.842Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":213,"end":217,"reference_id":"7513643","reference_source":"pmid","reference_html":"Chondroitin sulphate covalently cross-links the three polypeptide chains of inter-alpha-trypsin inhibitor. <i> Morelle W, Capon C, Balduyck M, Sautiere P, Kouach M, Michalski C, Fournet B, Mizon J. </i> Eur J Biochem, 1994","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"GO:0030246","term_name":"carbohydrate binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03294r004","statement":[{"text":"The chondroitin sulphate chain is bound at its reducing end by the typical linkage structure Gal-Gal-Xyl to the Ser10 of bikunin whereas the C-terminal Asp of the heavy chain H3 esterifies C6 of an internal N-acetylgalactosamine inside the GAG chain.","type":"Introduction"},{"text":"Fractions 4 and 5 correspond to the peptides Va12-Gln14 and Alal-Gln14 of bikunin, respectively (Table 2). As expected [l, 141], Ser10 was recovered with a low yield during Edman degradation: it constitutes the attachment point of the chondroitin sulphate chain as shown by the monosaccharide analysis of fraction 4 (Xyl/Gal = 1:2.1).","type":"Results"},{"text":"A molecular ion at mlz 1900 was identified in fraction 4 (data not shown). The expected mlz for the bikunin-derived peptide is 1286. The difference (614Da) was explained by the presence of the tetrasaccharide Xyl-Gal-Gal-dehydrohexuronic acid, typical of a chondroitin AC lyase digest of Ser-linked GAG [16].","type":"Results"},{"text":"Ser10 corresponds to Ser215, since protein AMBP is proteolitically cleaved into separately functioning proteins and this region is part of protein bikunin (206-352).","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-16T12:32:54.500Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.\" [GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":4,"released":"2021_06","sequence":"MRSLGALLLLLSACLAVSAGPVPTPPDNIQVQENFNISRIYGKWYNLAIGSTCPWLKKIMDRMTVSTLVLGEGATEAEISMTSTRWRKGVCEETSGAYEKTDTDGKFLYHKSKWNITMESYVVHTNYDEYAIFLTKKFSRHHGPTITAKLYGRAPQLRETLLQDFRVVAQGVGIPEDSIFTMADRGECVPGEQEPEPILIPRVRRAVLPQEEEGSGGGQLVTEVTKKEDSCQLGYSAGPCMGMTSRYFYNGTSMACETFQYGGCMGNGNNFVTEKECLQTCRTVAACNLPIVRGPCRAFIQLWAFDAVKGKCVLFPYGGCQGNGNKFYSEKECREYCGVPGDGDEELLRFSN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000000D9AF","uniref100":"UniRef100_P02760","uniref90":"UniRef90_P02760","uniref50":"UniRef50_P02760","genes":[{"name":{"value":"AMBP"},"synonyms":[{"value":"HCP"},{"value":"ITIL"}]}],"alphafold_very_low_content":0.16477272727272727,"disorder_content":0.13920454545454544,"disprot_consensus":{"full":[{"start":191,"end":202,"type":"D"},{"start":206,"end":229,"type":"D"},{"start":340,"end":352,"type":"D"}],"Structural state":[{"start":191,"end":202,"type":"D"},{"start":206,"end":229,"type":"D"},{"start":340,"end":352,"type":"D"}],"Molecular function":[{"start":213,"end":217,"type":"F"}]}},{"disprot_id":"DP03295","acc":"Q92854","creator":"spenadias","date":"2021-05-11T15:00:26.096Z","features":{"pfam":[{"id":"PF00047","name":"Immunoglobulin domain","start":563,"end":635},{"id":"PF01403","name":"Sema domain","start":293,"end":480},{"id":"PF01437","name":"Plexin repeat","start":503,"end":554}],"gene3D":[]},"length":862,"name":"Semaphorin-4D","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":649,"end":677,"reference_id":"12958590","reference_source":"pmid","reference_html":"The ligand-binding face of the semaphorins revealed by the high-resolution crystal structure of SEMA4D. <i> Love CA, Harlos K, Mavaddat N, Davis SJ, Stuart DI, Jones EY, Esnouf RM. </i> Nat Struct Biol, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1OLZ"}],"region_id":"DP03295r001","statement":[{"text":"Residues 1-2, 201-204 and 628-657 plus the His-tag are disordered in both subunits of the homodimer.","type":"Methods"},{"text":"Residues 628-657 correspond to residues 649 and 677 of the original protein sequence as the first 21 residues are omitted (signal peptide)","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MRMCTPIRGLLMALAVMFGTAMAFAPIPRITWEHREVHLVQFHEPDIYNYSALLLSEDKDTLYIGAREAVFAVNALNISEKQHEVYWKVSEDKKAKCAEKGKSKQTECLNYIRVLQPLSATSLYVCGTNAFQPACDHLNLTSFKFLGKNEDGKGRCPFDPAHSYTSVMVDGELYSGTSYNFLGSEPIISRNSSHSPLRTEYAIPWLNEPSFVFADVIRKSPDSPDGEDDRVYFFFTEVSVEYEFVFRVLIPRIARVCKGDQGGLRTLQKKWTSFLKARLICSRPDSGLVFNVLRDVFVLRSPGLKVPVFYALFTPQLNNVGLSAVCAYNLSTAEEVFSHGKYMQSTTVEQSHTKWVRYNGPVPKPRPGACIDSEARAANYTSSLNLPDKTLQFVKDHPLMDDSVTPIDNRPRLIKKDVNYTQIVVDRTQALDGTVYDVMFVSTDRGALHKAISLEHAVHIIEETQLFQDFEPVQTLLLSSKKGNRFVYAGSNSGVVQAPLAFCGKHGTCEDCVLARDPYCAWSPPTATCVALHQTESPSRGLIQEMSGDASVCPDKSKGSYRQHFFKHGGTAELKCSQKSNLARVFWKFQNGVLKAESPKYGLMGRKNLLIFNLSEGDSGVYQCLSEERVKNKTVFQVVAKHVLEVKVVPKPVVAPTLSVVQTEGSRIATKVLVASTQGSSPPTPAVQATSSGAITLPPKPAPTGTSCEPKIVINTVPQLHSEKTMYLKSSDNRLLMSLFLFFFVLFLCLFFYNCYKGYLPRQCLKFRSALLIGKKKPKSDFCDREQSLKETLVEPGSFSQQNGEHPKPALDTGYETEQDTITSKVPTDREDSQRIDDLSARDKPFDVKCELKFADSDADGD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000135A6C","uniref100":"UniRef100_Q92854","uniref90":"UniRef90_Q92854","uniref50":"UniRef50_Q92854","genes":[{"name":{"value":"SEMA4D"},"synonyms":[{"value":"C9orf164"},{"value":"CD100"},{"value":"SEMAJ"}]}],"alphafold_very_low_content":0.21809744779582366,"disorder_content":0.033642691415313224,"disprot_consensus":{"full":[{"start":649,"end":677,"type":"D"}],"Structural state":[{"start":649,"end":677,"type":"D"}]}},{"disprot_id":"DP03296","acc":"P60484","creator":"fquaglia","date":"2021-05-11T15:32:43.750Z","features":{"pfam":[{"id":"PF10409","name":"C2 domain of PTEN tumour-suppressor protein","start":189,"end":348},{"id":"PF22785","name":"Polymorphic toxin system, DSP-PTPase phosphatase","start":67,"end":143}],"gene3D":[]},"length":403,"name":"Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":354,"end":403,"reference_id":"10555148","reference_source":"pmid","reference_html":"Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association. <i> Lee JO, Yang H, Georgescu MM, Di Cristofano A, Maehama T, Shi Y, Dixon JE, Pandolfi P, Pavletich NP. </i> Cell, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03296r001","statement":[{"text":"Proteolytic digestion indicated that PTEN has unstructured or loosely folded regions of 7 and 49 residues at the N and C termini, respectively, and of 24 residues in an internal loop (residues 286–309; Figure 1B; data not shown).","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-30T09:28:54.554Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":353,"end":403,"reference_id":"10866658","reference_source":"pmid","reference_html":"Phosphorylation of the PTEN tail regulates protein stability and function. <i> Vazquez F, Ramaswamy S, Nakamura N, Sellers WR. </i> Mol Cell Biol, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03296r002","statement":[{"text":"Secondary structure prediction and the results of proteolytic digestion experiments suggest that the tail is a relatively unstructured and presumably flexible region.","type":"Discussion"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-30T09:30:58.358Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":353,"end":403,"reference_id":"10866658","reference_source":"pmid","reference_html":"Phosphorylation of the PTEN tail regulates protein stability and function. <i> Vazquez F, Ramaswamy S, Nakamura N, Sellers WR. </i> Mol Cell Biol, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03296r003","statement":[{"text":"Here, we show that the PTEN tail is necessary for maintaining protein stability and that it also acts to inhibit PTEN function. Thus, removing the tail results in a loss of stability but does not result in a loss of function because the resultant protein is more active. Furthermore, tail-dependent regulation of stability and activity is linked to the phosphorylation of three residues (S380, T382, and T383) within the tail. Therefore, the tail is likely to mediate the regulation of PTEN function through phosphorylation.","type":"Abstract"},{"text":"The PTEN tail modulates PTEN stability.","type":"Results"},{"text":"In keeping with these results, it was recently reported that the steady-state level of PTEN;1-351 is reduced compared to that of PTEN;WT when the protein is produced by transfection in COS-7 cells (14). Together these data suggest that the PTEN tail, while not required for the functional activity of the protein, is required for maintaining stability.","type":"Results"},{"text":"The tail domain modulates PTEN biological activity.","type":"Results"},{"text":"Surprisingly, at equivalent input plasmid concentrations PTEN;1-353 reproducibly induced a greater increase in G1 than PTEN;WT (data not shown). Next, the activities of PTEN;WT and PTEN;1-353 were compared when the proteins were produced at similar steady-state levels. Plasmid titration indicated that equivalent protein levels were obtained at 2 μg of PTEN;1-353 and 0.5 μg of PTEN;WT (Fig. ​(Fig.2A2A and B). At these levels PTEN;1-353 induced a significantly more robust G1 arrest (Fig. ​(Fig.2C).2C).","type":"Results"},{"text":"We next compared PTEN;WT and PTEN;1-353 in a FKHR transcriptional activation assay.","type":"Results"},{"text":"We next compared PTEN;WT and PTEN;1-353 in a FKHR transcriptional activation assay. Consistent with the results obtained in the cell cycle assay (Fig. ​(Fig.2C),2C), the ability of PTEN;1-353 to induce FKHR transcriptional activity was enhanced compared to that of PTEN;WT. Furthermore, at every DNA plasmid concentration tested, PTEN;1-353 induced FKHR activation more efficiently than PTEN;WT, although protein levels were reduced by more than fourfold. These results suggest that the PTEN tail not only plays a role in maintaining its protein stability but also in regulating its biological activity. Specifically, these data suggest that the tail acts to restrict or inhibit PTEN function.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-30T09:31:04.362Z"},"ec_go":"IMP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":378,"end":382,"reference_id":"10866658","reference_source":"pmid","reference_html":"Phosphorylation of the PTEN tail regulates protein stability and function. <i> Vazquez F, Ramaswamy S, Nakamura N, Sellers WR. </i> Mol Cell Biol, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03296r004","statement":[{"text":"Furthermore, tail-dependent regulation of stability and activity is linked to the phosphorylation of three residues (S380, T382, and T383) within the tail. Therefore, the tail is likely to mediate the regulation of PTEN function through phosphorylation.","type":"Abstract"},{"text":"PTEN is phosphorylated within the tail domain.","type":"Results"},{"text":"Next, every serine and threonine in the tail was mutated either singly or in clusters to alanine. These PTEN mutants were transfected into U2-OS cells and labeled with orthophosphate. No single-amino-acid substitution abrogated or significantly reduced the total phosphorylation of PTEN (data not shown). However, the substitution of a serine/threonine cluster, S380, T382, T383, and S385 (the A4 mutant), did significantly alter total PTEN phosphorylation.","type":"Results"},{"text":"These results indicate that most, if not all, of the PTEN tail phosphorylation occurs on serine 370 and one or more sites of the A4 cluster (S380, T382, T383, and S385).","type":"Results"},{"text":"Mutation of the phosphorylation sites in the tail alter PTEN stability and biological activity.","type":"Results"},{"text":"Taken together, these data show that the increased activity associated with deletion of the tail is entirely mimicked by mutations within the A4 cluster, specifically S380, T382, or T383.","type":"Results"},{"text":"The above data raised the possibility that phosphorylation of these three specific residues (S380, T382, and T383) might be required to maintain PTEN in a stable yet relatively inactive state.","type":"Results"},{"text":"In keeping with the data for PTEN;A4 and for the individual phosphorylation site mutants (with mutations S380A, T382A, and T383A), PTEN;A3 was found to have a reduced protein half-life, to be expressed at lower steady-state levels, and to be more active than wild-type PTEN in biological assays (Fig. ​(Fig.6C to F).","type":"Results"},{"text":"This region is associated to S380.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-30T09:31:03.138Z"},"ec_go":"IMP","disprot_namespace":"Disorder function"},{"start":380,"end":384,"reference_id":"10866658","reference_source":"pmid","reference_html":"Phosphorylation of the PTEN tail regulates protein stability and function. <i> Vazquez F, Ramaswamy S, Nakamura N, Sellers WR. </i> Mol Cell Biol, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03296r005","statement":[{"text":"Furthermore, tail-dependent regulation of stability and activity is linked to the phosphorylation of three residues (S380, T382, and T383) within the tail. Therefore, the tail is likely to mediate the regulation of PTEN function through phosphorylation.","type":"Abstract"},{"text":"PTEN is phosphorylated within the tail domain.","type":"Results"},{"text":"Next, every serine and threonine in the tail was mutated either singly or in clusters to alanine. These PTEN mutants were transfected into U2-OS cells and labeled with orthophosphate. No single-amino-acid substitution abrogated or significantly reduced the total phosphorylation of PTEN (data not shown). However, the substitution of a serine/threonine cluster, S380, T382, T383, and S385 (the A4 mutant), did significantly alter total PTEN phosphorylation.","type":"Results"},{"text":"These results indicate that most, if not all, of the PTEN tail phosphorylation occurs on serine 370 and one or more sites of the A4 cluster (S380, T382, T383, and S385).","type":"Results"},{"text":"Mutation of the phosphorylation sites in the tail alter PTEN stability and biological activity.","type":"Results"},{"text":"Taken together, these data show that the increased activity associated with deletion of the tail is entirely mimicked by mutations within the A4 cluster, specifically S380, T382, or T383.","type":"Results"},{"text":"The above data raised the possibility that phosphorylation of these three specific residues (S380, T382, and T383) might be required to maintain PTEN in a stable yet relatively inactive state.","type":"Results"},{"text":"In keeping with the data for PTEN;A4 and for the individual phosphorylation site mutants (with mutations S380A, T382A, and T383A), PTEN;A3 was found to have a reduced protein half-life, to be expressed at lower steady-state levels, and to be more active than wild-type PTEN in biological assays (Fig. ​(Fig.6C to F).","type":"Results"},{"text":"This region is associated to T382.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-30T09:31:01.568Z"},"ec_go":"IMP","disprot_namespace":"Disorder function"},{"start":381,"end":385,"reference_id":"10866658","reference_source":"pmid","reference_html":"Phosphorylation of the PTEN tail regulates protein stability and function. <i> Vazquez F, Ramaswamy S, Nakamura N, Sellers WR. </i> Mol Cell Biol, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03296r006","statement":[{"text":"Furthermore, tail-dependent regulation of stability and activity is linked to the phosphorylation of three residues (S380, T382, and T383) within the tail. Therefore, the tail is likely to mediate the regulation of PTEN function through phosphorylation.","type":"Abstract"},{"text":"PTEN is phosphorylated within the tail domain.","type":"Results"},{"text":"Next, every serine and threonine in the tail was mutated either singly or in clusters to alanine. These PTEN mutants were transfected into U2-OS cells and labeled with orthophosphate. No single-amino-acid substitution abrogated or significantly reduced the total phosphorylation of PTEN (data not shown). However, the substitution of a serine/threonine cluster, S380, T382, T383, and S385 (the A4 mutant), did significantly alter total PTEN phosphorylation.","type":"Results"},{"text":"These results indicate that most, if not all, of the PTEN tail phosphorylation occurs on serine 370 and one or more sites of the A4 cluster (S380, T382, T383, and S385).","type":"Results"},{"text":"Mutation of the phosphorylation sites in the tail alter PTEN stability and biological activity.","type":"Results"},{"text":"Taken together, these data show that the increased activity associated with deletion of the tail is entirely mimicked by mutations within the A4 cluster, specifically S380, T382, or T383.","type":"Results"},{"text":"The above data raised the possibility that phosphorylation of these three specific residues (S380, T382, and T383) might be required to maintain PTEN in a stable yet relatively inactive state.","type":"Results"},{"text":"In keeping with the data for PTEN;A4 and for the individual phosphorylation site mutants (with mutations S380A, T382A, and T383A), PTEN;A3 was found to have a reduced protein half-life, to be expressed at lower steady-state levels, and to be more active than wild-type PTEN in biological assays (Fig. ​(Fig.6C to F).","type":"Results"},{"text":"This region is associated to T383.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-30T09:31:00.232Z"},"ec_go":"IMP","disprot_namespace":"Disorder function"},{"start":286,"end":309,"reference_id":"10555148","reference_source":"pmid","reference_html":"Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association. <i> Lee JO, Yang H, Georgescu MM, Di Cristofano A, Maehama T, Shi Y, Dixon JE, Pandolfi P, Pavletich NP. </i> Cell, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03296r007","statement":[{"text":"Proteolytic digestion indicated that PTEN has unstructured or loosely folded regions of 7 and 49 residues at the N and C termini, respectively, and of 24 residues in an internal loop (residues 286–309; Figure 1B; data not shown).","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-30T09:28:53.519Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":366,"end":385,"reference_id":"26527737","reference_source":"pmid","reference_html":"The intrinsically disordered tails of PTEN and PTEN-L have distinct roles in regulating substrate specificity and membrane activity. <i> Masson GR, Perisic O, Burke JE, Williams RL. </i> Biochem J, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000059","term_name":"self-inhibition","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0007694","ec_ontology":"ECO","ec_name":"phosphatase assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03296r008","statement":[{"text":"Phosphorylation of six residues in the C-terminal tail of PTEN results in auto-inhibitory interactions with the phosphatase and C2 domains, effectively blocking both the active site and the membrane-binding interface of PTEN.","type":"Abstract"},{"text":"Phosphorylation of the C-terminal tail differentially inhibits PTEN towards distinct substrates","type":"Results"},{"text":"To compare the activities and specificities of differentially phosphorylated PTEN constructs, phosphatase assays were conducted against four substrates: a phosphotyrosine-containing acidic polypeptide, the soluble lipid diC8-PIP3, inositol tetrakis phosphate (IP4) and liposome-incorporated PIP3 (Figures 1B–1E).","type":"Results"},{"text":"We found that phosphorylation of PTEN caused a dramatic reduction in activity against all substrates. Intriguingly, when PTEN was phosphorylated on only four sites (pSer380/pThr382/pThr383/pSer385) by using the phosphorylated PTEN-2A mutant (Phos-PTEN-2A), activity against the phosphopeptide and soluble diC8-PIP3/IP4 substrates was restored (Figures 1B–1D), but PTEN remained inhibited against liposome-incorporated PIP3 substrate (Figure 1E; Supplementary Figure S3). This suggests that pThr366 and pSer370 may have a role in occluding the active site of PTEN, whereas pSer380, pThr382, pThr383 and pSer385 have a role in occluding the membrane-binding surface. Phos-PTEN-4A, phosphorylated on only two sites, pThr366 and pSer370, showed similar activities with all substrates to that of dephosphorylated PTEN-4A, with only a slight reduction in activity against liposome-incorporated PIP3","type":"Results"},{"text":"Region inside the disordered C-terminal tail that include multiple phosphorylation sites: T366, S370, S380, T382, T383, S385","type":"Curator statement"}],"ec_go":"IDA","disprot_namespace":"Disorder function"},{"start":366,"end":385,"reference_id":"26527737","reference_source":"pmid","reference_html":"The intrinsically disordered tails of PTEN and PTEN-L have distinct roles in regulating substrate specificity and membrane activity. <i> Masson GR, Perisic O, Burke JE, Williams RL. </i> Biochem J, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"construct_alterations":[{"term_namespace":"Protein modification","term_name":"phosphorylated residue","term_id":"MOD:00696","position":"Specific residue","start":366,"end":366,"statements":[]},{"term_namespace":"Protein modification","term_name":"phosphorylated residue","term_id":"MOD:00696","position":"Specific residue","start":370,"end":370,"statements":[]},{"term_namespace":"Protein modification","term_name":"phosphorylated residue","term_id":"MOD:00696","position":"Specific residue","start":380,"end":380,"statements":[]},{"term_namespace":"Protein modification","term_name":"phosphorylated residue","term_id":"MOD:00696","position":"Specific residue","start":382,"end":382,"statements":[]},{"term_namespace":"Protein modification","term_name":"phosphorylated residue","term_id":"MOD:00696","position":"Specific residue","start":383,"end":383,"statements":[]},{"term_namespace":"Protein modification","term_name":"phosphorylated residue","term_id":"MOD:00696","position":"Specific residue","start":385,"end":385,"statements":[]}],"interaction_partner":[{"db":"UniProt","id":"P60484","partner_start":null,"partner_end":null}],"region_id":"DP03296r009","statement":[{"text":"HDX–MS shows that the phosphorylated C-terminal tail forms intramolecular interactions with both the C2 and the phosphatase domains","type":"Results"},{"text":"Overall, these decreases in HDX suggest that the fully phosphorylated C-terminal tail makes contact at the C2/phosphatase interface and more extensive contacts within the phosphatase domain, interacting extensively with all three loops of the active site and the PBM.","type":"Results"},{"text":"Region inside the disordered C-terminal tail that include multiple phosphorylation sites: T366, S370, S380, T382, T383, S385","type":"Curator statement"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":366,"end":385,"reference_id":"26527737","reference_source":"pmid","reference_html":"The intrinsically disordered tails of PTEN and PTEN-L have distinct roles in regulating substrate specificity and membrane activity. <i> Masson GR, Perisic O, Burke JE, Williams RL. </i> Biochem J, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"construct_alterations":[{"term_namespace":"Protein modification","term_name":"phosphorylated residue","term_id":"MOD:00696","position":"Specific residue","start":366,"end":366,"statements":[]},{"term_namespace":"Protein modification","term_name":"phosphorylated residue","term_id":"MOD:00696","position":"Specific residue","start":370,"end":370,"statements":[]},{"term_namespace":"Protein modification","term_name":"phosphorylated residue","term_id":"MOD:00696","position":"Specific residue","start":380,"end":380,"statements":[]},{"term_namespace":"Protein modification","term_name":"phosphorylated residue","term_id":"MOD:00696","position":"Specific residue","start":382,"end":382,"statements":[]},{"term_namespace":"Protein modification","term_name":"phosphorylated residue","term_id":"MOD:00696","position":"Specific residue","start":383,"end":383,"statements":[]},{"term_namespace":"Protein modification","term_name":"phosphorylated residue","term_id":"MOD:00696","position":"Specific residue","start":385,"end":385,"statements":[]}],"region_id":"DP03296r010","statement":[{"text":"HDX–MS shows that the phosphorylated C-terminal tail forms intramolecular interactions with both the C2 and the phosphatase domains","type":"Results"},{"text":"Overall, these decreases in HDX suggest that the fully phosphorylated C-terminal tail makes contact at the C2/phosphatase interface and more extensive contacts within the phosphatase domain, interacting extensively with all three loops of the active site and the PBM.","type":"Results"},{"text":"Region inside the disordered C-terminal tail that include multiple phosphorylation sites: T366, S370, S380, T382, T383, S385","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":10,"released":"2021_12","sequence":"MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEIDSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHTQITKV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins","Autophagy-related proteins","NDDs-related proteins"],"UniParc":"UPI00001328C5","uniref100":"UniRef100_P60484","uniref90":"UniRef90_P60484","uniref50":"UniRef50_P60484","genes":[{"name":{"value":"PTEN"},"synonyms":[{"value":"MMAC1"},{"value":"TEP1"}]}],"alphafold_very_low_content":0.1687344913151365,"disorder_content":0.18610421836228289,"disprot_consensus":{"full":[{"start":286,"end":309,"type":"D"},{"start":353,"end":403,"type":"D"}],"Structural state":[{"start":286,"end":309,"type":"D"},{"start":353,"end":403,"type":"D"}],"Molecular function":[{"start":353,"end":403,"type":"F"}],"Disorder function":[{"start":366,"end":385,"type":"F"}]}},{"disprot_id":"DP03297","acc":"P01034","creator":"rpancsa","date":"2021-05-12T08:17:48.583Z","features":{"pfam":[{"id":"PF00031","name":"Cystatin domain","start":37,"end":132}],"gene3D":[]},"length":146,"name":"Cystatin-C","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":27,"end":37,"reference_id":"31330077","reference_source":"pmid","reference_html":"NMR and crystallographic structural studies of the extremely stable monomeric variant of human cystatin C with single amino acid substitution. <i> Maszota-Zieleniak M, Jurczak P, Orlikowska M, Zhukov I, Borek D, Otwinowski Z, Skowron P, Pietralik Z, Kozak M, Szymańska A, Rodziewicz-Motowidło S. </i> FEBS J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6RPV"},{"db":"BMRB","id":"34399"}],"region_id":"DP03297r001","statement":[{"text":"N and C termini of the protein are disordered. This is particularly evident in the case of the N terminus (see Fig. 3) which is very flexible and tends to form a bent structure at the top of the Gly11‐Gly12 residues and the neighboring Pro13.","type":"Results"},{"text":"The relaxation data for 21 residues (first eight residues form N terminus included) were not collected due to signals overlap, intensive exchange with water, or low signal‐to‐noise ratio","type":"Results"},{"text":"There is a signal peptide of 26 residues, so there is a shift between UniProt numbering and the numbering in the article. Gly11 mentioned in the article corresponds to UniProt residue 37.","type":"Curator statement"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-14T14:43:18.731Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":27,"end":37,"reference_id":"31330077","reference_source":"pmid","reference_html":"NMR and crystallographic structural studies of the extremely stable monomeric variant of human cystatin C with single amino acid substitution. <i> Maszota-Zieleniak M, Jurczak P, Orlikowska M, Zhukov I, Borek D, Otwinowski Z, Skowron P, Pietralik Z, Kozak M, Szymańska A, Rodziewicz-Motowidło S. </i> FEBS J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6ROA"}],"region_id":"DP03297r002","statement":[{"text":"N and C termini of the protein are disordered. This is particularly evident in the case of the N terminus (see Fig. 3)","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-17T15:19:51.639Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":35,"end":39,"reference_id":"31330077","reference_source":"pmid","reference_html":"NMR and crystallographic structural studies of the extremely stable monomeric variant of human cystatin C with single amino acid substitution. <i> Maszota-Zieleniak M, Jurczak P, Orlikowska M, Zhukov I, Borek D, Otwinowski Z, Skowron P, Pietralik Z, Kozak M, Szymańska A, Rodziewicz-Motowidło S. </i> FEBS J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000048","term_name":"limited proteolysis display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","released":"2022_03","version":2,"region_id":"DP03297r003","statement":[{"text":"It is worth mentioning that the N-terminal segment of hCC is cleaved by cysteine proteases. In the case of hCC, cleavage takes place after Gly11 residue.","type":"Discussion"},{"text":"There is a signal peptide of 26 residues, so there is a shift between UniProt numbering and the numbering in the article. Gly11 mentioned in the article corresponds to UniProt residue 37.","type":"Curator statement"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-14T14:45:23.549Z"},"disprot_namespace":"Disorder function"},{"start":27,"end":37,"reference_id":"31330077","reference_source":"pmid","reference_html":"NMR and crystallographic structural studies of the extremely stable monomeric variant of human cystatin C with single amino acid substitution. <i> Maszota-Zieleniak M, Jurczak P, Orlikowska M, Zhukov I, Borek D, Otwinowski Z, Skowron P, Pietralik Z, Kozak M, Szymańska A, Rodziewicz-Motowidło S. </i> FEBS J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","released":"2022_03","version":3,"region_id":"DP03297r004","statement":[{"text":"It is worth mentioning that the N-terminal segment of hCC is cleaved by cysteine proteases. In the case of hCC, cleavage takes place after Gly11 residue. The N-terminally truncated cystatin shows significantly decreased affinity toward cysteine proteases, which indicates that the N-terminal segment is necessary for the inhibitory activity.","type":"Discussion"},{"text":"There is a signal peptide of 26 residues, so there is a shift between UniProt numbering and the numbering in the article. Gly11 mentioned in the article corresponds to UniProt residue 37.","type":"Curator statement"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-14T14:49:09.684Z"},"term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":4,"released":"2021_06","sequence":"MAGPLRAPLLLLAILAVALAVSPAAGSSPGKPPRLVGGPMDASVEEEGVRRALDFAVGEYNKASNDMYHSRALQVVRARKQIVAGVNYFLDVELGRTTCTKTQPNLDNCPFHDQPHLKRKAFCSFQIYAVPWQGTMTLSKSTCQDA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins","Age-related disorders proteins"],"UniParc":"UPI000002B9AD","uniref100":"UniRef100_P01034","uniref90":"UniRef90_P01034","uniref50":"UniRef50_P01034","genes":[{"name":{"value":"CST3"}}],"alphafold_very_low_content":0.00684931506849315,"disorder_content":0.07534246575342465,"disprot_consensus":{"full":[{"start":27,"end":37,"type":"D"},{"start":38,"end":39,"type":"F"}],"Structural state":[{"start":27,"end":37,"type":"D"}],"Disorder function":[{"start":35,"end":39,"type":"F"}],"Molecular function":[{"start":27,"end":37,"type":"F"}]}},{"disprot_id":"DP03298","acc":"P63000","creator":"fquaglia","date":"2021-05-12T10:30:27.846Z","features":{"pfam":[{"id":"PF00071","name":"Ras family","start":5,"end":176}],"gene3D":[]},"length":192,"name":"Ras-related C3 botulinum toxin substrate 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":182,"end":192,"reference_id":"27150042","reference_source":"pmid","reference_html":"Structural and Biochemical Characterization of the Catalytic Core of the Metastatic Factor P-Rex1 and Its Regulation by PtdIns(3,4,5)P3. <i> Cash JN, Davis EM, Tesmer JJG. </i> Structure, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5FI0"}],"region_id":"DP03298r001","statement":[{"text":"Intrinsically disordered C-terminal tail of Rac1.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-07-09T05:27:14.448Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":179,"end":192,"reference_id":"11090627","reference_source":"pmid","reference_html":"Structure of the TPR domain of p67phox in complex with Rac.GTP. <i> Lapouge K, Smith SJ, Walker PA, Gamblin SJ, Smerdon SJ, Rittinger K. </i> Mol Cell, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1E96"}],"region_id":"DP03298r002","statement":[{"text":"Intrinsically disordered C-terminal tail of Rac1.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-07-09T05:27:13.447Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":179,"end":192,"reference_id":"11346801","reference_source":"pmid","reference_html":"The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways. <i> Tarricone C, Xiao B, Justin N, Walker PA, Rittinger K, Gamblin SJ, Smerdon SJ. </i> Nature, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1I4D"},{"db":"PDB","id":"1I4L"},{"db":"PDB","id":"1I4T"}],"region_id":"DP03298r003","statement":[{"text":"Intrinsically disordered C-terminal tail of Rac1.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-07-09T05:27:12.710Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":178,"end":188,"reference_id":"12874273","reference_source":"pmid","reference_html":"The C-terminal domain of Rac1 contains two motifs that control targeting and signaling specificity. <i> van Hennik PB, ten Klooster JP, Halstead JR, Voermans C, Anthony EC, Divecha N, Hordijk PL. </i> J Biol Chem, 2003","date":"2022-03-08T14:01:48.665Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006077","ec_ontology":"ECO","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","unpublished":true,"released":"2022_03","version":4,"region_id":"DP03298r004","statement":[{"text":"The Rac1 C-terminal Domain Associates with Effector and Adapter Proteins","type":"Results"},{"text":"Using pull-down experiments followed by lipid kinase activity assays (23), we found that indeed the TAT-Rac1 C terminus (amino acids 178-188) bound PIP5K activity when used as a bait to fish in HL60 cell lysates (Fig. 4).","type":"Results"},{"text":"TAT-Rac1 also bound PIP5K in KG1a, MDCKII, and COS7 cells (data not shown). Apparently, the Rac1 178-188 region, encoded by the peptide used in this study, is already sufficient to mediate association of Rac1 with PIP5K.","type":"Results"},{"text":"We next examined the binding of the Rac1 peptide to other signaling proteins, implicated in cell migration and cell-cell adhesion. We found that the adapter proteins NCK and Crk bound specifically to the Rac1 C-terminal peptide.","type":"Results"},{"text":"Subsequently, using transient transfection of v-Crk mutants that were mutated in the SH2 or the N-terminal SH3 domain (27), we could show that the association of Crk with the Rac1 C terminus is mediated by the N-terminal SH3 domain of Crk and is not dependent on an intact SH2 domain (Fig. 5C).","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"O60331","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-08T18:08:13.853Z"}},{"start":178,"end":188,"reference_id":"12874273","reference_source":"pmid","reference_html":"The C-terminal domain of Rac1 contains two motifs that control targeting and signaling specificity. <i> van Hennik PB, ten Klooster JP, Halstead JR, Voermans C, Anthony EC, Divecha N, Hordijk PL. </i> J Biol Chem, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007634","ec_ontology":"ECO","ec_name":"experimental phenotypic evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03298r006","statement":[{"text":"Apparently, both the effector loop and as the C terminus of Rac1 are required, in a non-redundant fashion, for growth factor-induced membrane ruffling and proper Rac1 localization.","type":"Results"},{"text":"The Rac1 C-terminal Domain Inhibits Actin Polymerization and Cell Migration","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-07-09T05:28:44.680Z"},"ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":184,"end":188,"reference_id":"12874273","reference_source":"pmid","reference_html":"The C-terminal domain of Rac1 contains two motifs that control targeting and signaling specificity. <i> van Hennik PB, ten Klooster JP, Halstead JR, Voermans C, Anthony EC, Divecha N, Hordijk PL. </i> J Biol Chem, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03298r007","statement":[{"text":"Having established at least two signaling proteins that associate directly with the Rac1 C terminus, we tested whether these interactions would involve identical residues within the Rac1 C-terminal sequence. To this end, two mutants of the TAT-Rac1 C-terminal peptide were synthesized. In the first one, the three prolines (amino acids 179-181) were replaced by alanine residues (Rac1 PPP-AAA). In the second, the RKR sequence (amino acids 185-187) was replaced by alanine residues (Rac1 RKR-AAA) (Fig. 6A). The interaction of the Rac1 C terminus with PIP5K was shown previously (28) to be mediated by basic amino acids, in particular Lys-186. In line with these data, the TAT-Rac1 RKR-AAA peptide no longer associated with PIP5K activity in the pull-down assay (Fig. 6B).","type":"Results"},{"text":"These data establish the presence of two binding motifs for signaling proteins within the Rac1 C terminus.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-07-09T05:28:16.177Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":178,"end":182,"reference_id":"12874273","reference_source":"pmid","reference_html":"The C-terminal domain of Rac1 contains two motifs that control targeting and signaling specificity. <i> van Hennik PB, ten Klooster JP, Halstead JR, Voermans C, Anthony EC, Divecha N, Hordijk PL. </i> J Biol Chem, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03298r008","statement":[{"text":"Having established at least two signaling proteins that associate directly with the Rac1 C terminus, we tested whether these interactions would involve identical residues within the Rac1 C-terminal sequence. To this end, two mutants of the TAT-Rac1 C-terminal peptide were synthesized. In the first one, the three prolines (amino acids 179-181) were replaced by alanine residues (Rac1 PPP-AAA). In the second, the RKR sequence (amino acids 185-187) was replaced by alanine residues (Rac1 RKR-AAA) (Fig. 6A).","type":"Results"},{"text":"Because the interaction with the Crk adapter protein involved the Crk SH3 domain, we tested whether the three consecutive prolines in the Rac1 C terminus mediated Crk binding. When using the Rac1 PPP-AAA peptide, the binding to Crk was abolished, confirming that these prolines were required for the interaction (Fig. 6C).","type":"Results"},{"text":"These data establish the presence of two binding motifs for signaling proteins within the Rac1 C terminus.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-07-09T05:28:14.622Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":184,"end":188,"reference_id":"12874273","reference_source":"pmid","reference_html":"The C-terminal domain of Rac1 contains two motifs that control targeting and signaling specificity. <i> van Hennik PB, ten Klooster JP, Halstead JR, Voermans C, Anthony EC, Divecha N, Hordijk PL. </i> J Biol Chem, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03298r009","statement":[{"text":"Next, the wild type and the two mutant peptides were used to determine the relation between the presence of either binding site and localization and effects of the peptides. Phosphatidylinositol 4,5-biphosphate, a product of PIP5K, is present in lipid rafts from where actin polymerization is mediated (29, 30). In line with this, the wild type Rac1 C terminus co-localized with lipid rafts in HL60 cells (Fig. 7A), suggesting that the inhibitory effect of this peptide on in vitro migration is because of interference with localized PIP5K/phosphatidylinositol 4,5-biphosphate-dependent, Rac-mediated signaling.","type":"Results"},{"text":"The Rac1 PPP-AAA peptide also localized to lipid rafts; the Rac1 RKR-AAA peptide showed less prominent co-localization with lipid rafts, suggesting that the basic motif in the C terminus is involved, perhaps via PIP5K, in mediating associations with raft-resident proteins.","type":"Results"},{"text":"In MDCKII cells, the Rac1 C terminus showed a clear localization to both cell-cell junctions and peripheral membranes (Fig. 7B). The peptide did not associate to endomembranes or to the nuclear membrane. This localization was mimicked by the Rac1 PPP-AAA peptide, but the Rac1 RKR-AAA peptide showed a marked loss of accumulation at peripheral membranes.","type":"Results"},{"text":"The Rac1 RKR-AAA peptide no longer inhibited HGF-induced membrane ruffling, whereas the Rac1 PPP-AAA peptide did (Fig. 7C). This suggests that the RKR sequence in the Rac1 C terminus controls membrane ruffling and Rac1-localization to these ruffles, possibly through the association with PIP5K.","type":"Results"},{"text":"These data further underscore the relationship between the amino acid sequence of the C-terminal domain of Rho-like GTPases and their intracellular targeting and suggests that binding partners for Rac1 are also differentially distributed over distinct regions of the plasma membrane (i.e. cell-cell junctions versus peripheral plasma membrane).","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-07-09T05:28:42.982Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":184,"end":188,"reference_id":"12874273","reference_source":"pmid","reference_html":"The C-terminal domain of Rac1 contains two motifs that control targeting and signaling specificity. <i> van Hennik PB, ten Klooster JP, Halstead JR, Voermans C, Anthony EC, Divecha N, Hordijk PL. </i> J Biol Chem, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007634","ec_ontology":"ECO","ec_name":"experimental phenotypic evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03298r010","statement":[{"text":"Finally, the different Rac1 peptides were characterized for their effects on SDF-1-induced actin polymerization and chemotaxis. The Rac1 PPP-AAA peptide efficiently blocked SDF-1-induced actin polymerization, whereas the Rac1 RKR-AAA peptide did not (Fig. 7E). Similarly, the Rac1 RKR-AAA peptide no longer interfered significantly with SDF-1-induced chemotaxis of HL60 cells. In contrast, the PPP-AAA mutant peptide inhibited migration as efficiently as the wild type peptide (Fig. 7F). This indicates that, in addition to the Crk binding proline-rich motif, it is primarily the basic, PIP5K binding motif that contributes to the control of actin polymerization and cell migration by Rac1.","type":"Results"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-07-09T05:28:20.465Z"},"ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":10,"released":"2021_12","sequence":"MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVLCPPPVKKRKRKCLLL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins","Autophagy-related proteins","NDDs-related proteins"],"UniParc":"UPI000000060F","uniref100":"UniRef100_P63000","uniref90":"UniRef90_P63000","uniref50":"UniRef50_P63000","genes":[{"name":{"value":"RAC1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9801","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9801"}}]},"synonyms":[{"value":"TC25"}],"orfNames":[{"value":"MIG5"}]}],"alphafold_very_low_content":0.005208333333333333,"disorder_content":0.07291666666666667,"disprot_consensus":{"full":[{"start":178,"end":178,"type":"F"},{"start":179,"end":192,"type":"D"}],"Structural state":[{"start":179,"end":192,"type":"D"}],"Molecular function":[{"start":178,"end":188,"type":"F"}],"Biological process":[{"start":184,"end":188,"type":"F"}]}},{"disprot_id":"DP03299","acc":"P00734","creator":"rpancsa","date":"2021-05-12T11:29:05.053Z","features":{"pfam":[{"id":"PF00051","name":"Kringle domain","start":108,"end":186},{"id":"PF00051","name":"Kringle domain","start":213,"end":291},{"id":"PF00089","name":"Trypsin","start":364,"end":613},{"id":"PF00594","name":"Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain","start":48,"end":88},{"id":"PF09396","name":"Thrombin light chain","start":317,"end":363}],"gene3D":[]},"length":622,"name":"Prothrombin","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":187,"end":211,"reference_id":"23775088","reference_source":"pmid","reference_html":"Crystal structure of prothrombin reveals conformational flexibility and mechanism of activation. <i> Pozzi N, Chen Z, Gohara DW, Niu W, Heyduk T, Di Cera E. </i> J Biol Chem, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4HZH"}],"region_id":"DP03299r001","statement":[{"text":"The construct (residues 45–579) can be traced in the electron density map almost in its entirety (Fig. 1), except for two disordered regions connecting the two kringles (residues 144–168) and kringle-2 to the A chain (residues 255–273).","type":"Results"},{"text":"The linker connecting the two kringles is 26 residues long, from Gly-144 to Gln-169, and completely disordered.","type":"Results"},{"text":"The residue numbering of the article refers to the residues of the prothrombin chain that lacks the first 43 residues (signal peptide + propeptide) of the respective UniProt entry.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-10T16:44:44.528Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":298,"end":316,"reference_id":"23775088","reference_source":"pmid","reference_html":"Crystal structure of prothrombin reveals conformational flexibility and mechanism of activation. <i> Pozzi N, Chen Z, Gohara DW, Niu W, Heyduk T, Di Cera E. </i> J Biol Chem, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4HZH"}],"region_id":"DP03299r002","statement":[{"text":"The construct (residues 45–579) can be traced in the electron density map almost in its entirety (Fig. 1), except for two disordered regions connecting the two kringles (residues 144–168) and kringle-2 to the A chain (residues 255–273).","type":"Results"},{"text":"There are no direct interactions between fragment 2 and the A chain, and 20 residues are missing from the highly acidic linker connecting these domains.","type":"Results"},{"text":"The residue numbering of the article refers to the residues of the prothrombin chain that lacks the first 43 residues (signal peptide + propeptide) of the respective UniProt entry.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-10T16:44:42.757Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":298,"end":316,"reference_id":"23775088","reference_source":"pmid","reference_html":"Crystal structure of prothrombin reveals conformational flexibility and mechanism of activation. <i> Pozzi N, Chen Z, Gohara DW, Niu W, Heyduk T, Di Cera E. </i> J Biol Chem, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"4HZH"}],"region_id":"DP03299r003","statement":[{"text":"The construct (residues 45–579) can be traced in the electron density map almost in its entirety (Fig. 1), except for two disordered regions connecting the two kringles (residues 144–168) and kringle-2 to the A chain (residues 255–273).","type":"Results"},{"text":"The residue numbering of the article refers to the residues of the prothrombin chain that lacks the first 43 residues (signal peptide + propeptide) of the respective UniProt entry.","type":"Curator statement"},{"text":"The linker connecting the two kringles is 26 residues long, from Gly-144 to Gln-169, and completely disordered.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-10T16:44:50.069Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":187,"end":211,"reference_id":"23775088","reference_source":"pmid","reference_html":"Crystal structure of prothrombin reveals conformational flexibility and mechanism of activation. <i> Pozzi N, Chen Z, Gohara DW, Niu W, Heyduk T, Di Cera E. </i> J Biol Chem, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"4HZH"}],"region_id":"DP03299r004","statement":[{"text":"The construct (residues 45–579) can be traced in the electron density map almost in its entirety (Fig. 1), except for two disordered regions connecting the two kringles (residues 144–168) and kringle-2 to the A chain (residues 255–273).","type":"Results"},{"text":"The residue numbering of the article refers to the residues of the prothrombin chain that lacks the first 43 residues (signal peptide + propeptide) of the respective UniProt entry.","type":"Curator statement"},{"text":"There are no direct interactions between fragment 2 and the A chain, and 20 residues are missing from the highly acidic linker connecting these domains.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-10T16:44:48.650Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":90,"end":110,"reference_id":"23775088","reference_source":"pmid","reference_html":"Crystal structure of prothrombin reveals conformational flexibility and mechanism of activation. <i> Pozzi N, Chen Z, Gohara DW, Niu W, Heyduk T, Di Cera E. </i> J Biol Chem, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4HZH"}],"region_id":"DP03299r005","statement":[{"text":"After molecular replacement of the Gla-domainless prothrombin structure using the coordinates 3NXP of prethrombin-1, extra electron density was clearly detected to assign fragment 1 with confidence from Gly-68 to Cys-143, covering kringle-1 (Cys-65 to Cys-143) almost entirely.","type":"Results"},{"text":"The residue numbering of the article refers to the residues of the prothrombin chain that lacks the first 43 residues (signal peptide + propeptide) of the respective UniProt entry.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-10T16:44:41.256Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":187,"end":211,"reference_id":"23775088","reference_source":"pmid","reference_html":"Crystal structure of prothrombin reveals conformational flexibility and mechanism of activation. <i> Pozzi N, Chen Z, Gohara DW, Niu W, Heyduk T, Di Cera E. </i> J Biol Chem, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"4HZH"}],"region_id":"DP03299r006","statement":[{"text":"The significant variation in the distance between residues 101 in kringle-1 and residue 210 in kringle-2 detected by LRET measurements is caused by the intrinsic flexibility of the connecting linker between the two kringles that appears as disordered in the crystal structure.","type":"Results"},{"text":"The residue numbering of the article refers to the residues of the prothrombin chain that lacks the first 43 residues (signal peptide + propeptide) of the respective UniProt entry.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-10T16:44:47.336Z"},"ec_go":"IPI","disprot_namespace":"Disorder function"},{"start":187,"end":211,"reference_id":"23775088","reference_source":"pmid","reference_html":"Crystal structure of prothrombin reveals conformational flexibility and mechanism of activation. <i> Pozzi N, Chen Z, Gohara DW, Niu W, Heyduk T, Di Cera E. </i> J Biol Chem, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4HZH"}],"region_id":"DP03299r007","statement":[{"text":"The significant variation in the distance between residues 101 in kringle-1 and residue 210 in kringle-2 detected by LRET measurements is caused by the intrinsic flexibility of the connecting linker between the two kringles that appears as disordered in the crystal structure.","type":"Results"},{"text":"The residue numbering of the article refers to the residues of the prothrombin chain that lacks the first 43 residues (signal peptide + propeptide) of the respective UniProt entry.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-10T16:44:39.876Z"},"ec_go":"IPI","disprot_namespace":"Structural state"},{"start":301,"end":316,"reference_id":"24821807","reference_source":"pmid","reference_html":"The linker connecting the two kringles plays a key role in prothrombin activation. <i> Pozzi N, Chen Z, Pelc LA, Shropshire DB, Di Cera E. </i> Proc Natl Acad Sci U S A, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4O03"},{"db":"PDB","id":"4NZQ"}],"region_id":"DP03299r008","statement":[{"text":"All domains of ProTΔ146–167 are clearly resolved in the electron density map, except for several residues of Lnk3. The important cleavage site at R271 is contained in this segment and has so far eluded X-ray detection in all published structures of human GD-ProT (15), prethrombin-1 (17) or meizothrombin desF1 (16). Disorder in this region supports the conclusion that R271 is constitutively exposed to solvent for proteolytic attack, regardless of the conformation of Lnk2.","type":"Results"},{"text":"The residue numbering of the article refers to the residues of the prothrombin chain that lacks the first 43 residues (signal peptide + propeptide) of the respective UniProt entry.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-10T16:44:38.109Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":312,"end":316,"reference_id":"24821807","reference_source":"pmid","reference_html":"The linker connecting the two kringles plays a key role in prothrombin activation. <i> Pozzi N, Chen Z, Pelc LA, Shropshire DB, Di Cera E. </i> Proc Natl Acad Sci U S A, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000048","term_name":"limited proteolysis display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4O03"},{"db":"PDB","id":"4NZQ"}],"region_id":"DP03299r009","statement":[{"text":"All domains of ProTΔ146–167 are clearly resolved in the electron density map, except for several residues of Lnk3. The important cleavage site at R271 is contained in this segment and has so far eluded X-ray detection in all published structures of human GD-ProT (15), prethrombin-1 (17) or meizothrombin desF1 (16). Disorder in this region supports the conclusion that R271 is constitutively exposed to solvent for proteolytic attack, regardless of the conformation of Lnk2","type":"Results"},{"text":"The residue numbering of the article refers to the residues of the prothrombin chain that lacks the first 43 residues (signal peptide + propeptide) of the respective UniProt entry. Therefore the known cleavage site mentioned by the authors (R271) corresponds to R314 in the UniProt sequence.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-10T16:44:46.018Z"},"disprot_namespace":"Disorder function"}],"regions_counter":9,"released":"2021_06","sequence":"MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000143316","uniref100":"UniRef100_P00734","uniref90":"UniRef90_P00734","uniref50":"UniRef50_P00734","genes":[{"name":{"value":"F2"}}],"alphafold_very_low_content":0.08681672025723473,"disorder_content":0.1045016077170418,"disprot_consensus":{"full":[{"start":90,"end":110,"type":"D"},{"start":187,"end":211,"type":"D"},{"start":298,"end":316,"type":"D"}],"Structural state":[{"start":90,"end":110,"type":"D"},{"start":187,"end":211,"type":"D"},{"start":298,"end":316,"type":"D"}],"Disorder function":[{"start":187,"end":211,"type":"F"},{"start":298,"end":316,"type":"F"}]}},{"disprot_id":"DP03300","acc":"P31749","creator":"fquaglia","date":"2021-05-12T15:50:10.121Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":150,"end":408},{"id":"PF00169","name":"PH domain","start":7,"end":106},{"id":"PF00433","name":"Protein kinase C terminal domain","start":429,"end":474}],"gene3D":[]},"length":480,"name":"RAC-alpha serine/threonine-protein kinase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":114,"end":144,"reference_id":"20886116","reference_source":"pmid","reference_html":"Crystal structure of human AKT1 with an allosteric inhibitor reveals a new mode of kinase inhibition. <i> Wu WI, Voegtli WC, Sturgis HL, Dizon FP, Vigers GP, Brandhuber BJ. </i> PLoS One, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3O96"}],"region_id":"DP03300r001","statement":[{"text":"Missing electron density region of AKT1 corresponding to the interdomain linker connecting the PH and Kinase domains.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:38:16.152Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":114,"end":144,"reference_id":"20886116","reference_source":"pmid","reference_html":"Crystal structure of human AKT1 with an allosteric inhibitor reveals a new mode of kinase inhibition. <i> Wu WI, Voegtli WC, Sturgis HL, Dizon FP, Vigers GP, Brandhuber BJ. </i> PLoS One, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"3O96"}],"region_id":"DP03300r002","statement":[{"text":"Missing electron density region of AKT1 corresponding to the interdomain linker connecting the PH and Kinase domains.","type":"Curator statement"}],"validated":{"curator_name":"Mátyás Pajkos","curator_id":"mpajkos","timestamp":"2021-06-16T14:38:17.129Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":2,"released":"2021_12","sequence":"MSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQEEEEMDFRSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins"],"UniParc":"UPI000002E75B","uniref100":"UniRef100_P31749","uniref90":"UniRef90_P31749","uniref50":"UniRef50_P31749","genes":[{"name":{"value":"AKT1"},"synonyms":[{"value":"PKB"},{"value":"RAC"}]}],"alphafold_very_low_content":0.1,"disorder_content":0.06458333333333334,"disprot_consensus":{"full":[{"start":114,"end":144,"type":"D"}],"Structural state":[{"start":114,"end":144,"type":"D"}],"Disorder function":[{"start":114,"end":144,"type":"F"}]}},{"disprot_id":"DP03301","acc":"P09237","creator":"spenadias","date":"2021-05-13T06:47:34.807Z","features":{"pfam":[{"id":"PF00413","name":"Matrixin","start":103,"end":259},{"id":"PF01471","name":"Putative peptidoglycan binding domain","start":31,"end":82}],"gene3D":[]},"length":267,"name":"Matrilysin","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":18,"end":28,"reference_id":"26439767","reference_source":"pmid","reference_html":"Charge-Triggered Membrane Insertion of Matrix Metalloproteinase-7, Supporter of Innate Immunity and Tumors. <i> Prior SH, Fulcher YG, Koppisetti RK, Jurkevich A, Van Doren SR. </i> Structure, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2MZH"},{"db":"PDB","id":"2MZI"},{"db":"PDB","id":"2MZE"}],"region_id":"DP03301r001","statement":[{"text":"These coordi-nates differ from the free form with a backbone RMSD of 1.6 A ̊across the catalytic domain and 2.1 A ̊across the pro-domain (omitting the disordered segments listed inTable 1)","type":"Results"},{"text":"Residue ranges used: 12–27, 31–72, 83–216, and 224–238. Uncertainties are SDs","type":"Table"},{"text":"The segments between the residues here indicated are the disordered regions (1-11, 28-30, 73-82, 217-223 and 239-250), corresponding to regions  18-28, 45-47, 90-99, 234-240 and 256-267 on the original protein sequence","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":90,"end":99,"reference_id":"26439767","reference_source":"pmid","reference_html":"Charge-Triggered Membrane Insertion of Matrix Metalloproteinase-7, Supporter of Innate Immunity and Tumors. <i> Prior SH, Fulcher YG, Koppisetti RK, Jurkevich A, Van Doren SR. </i> Structure, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2MZH"},{"db":"PDB","id":"2MZI"},{"db":"PDB","id":"2MZE"}],"region_id":"DP03301r002","statement":[{"text":"These coordi-nates differ from the free form with a backbone RMSD of 1.6 A ̊across the catalytic domain and 2.1 A ̊across the pro-domain (omitting the disordered segments listed inTable 1)","type":"Results"},{"text":"Residue ranges used: 12–27, 31–72, 83–216, and 224–238. Uncertainties are SDs","type":"Table"},{"text":"The segments between the residues here indicated are the disordered regions (1-11, 28-30, 73-82, 217-223 and 239-250), corresponding to regions  18-28, 45-47, 90-99, 234-240 and 256-267 on the original protein sequence","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":256,"end":267,"reference_id":"26439767","reference_source":"pmid","reference_html":"Charge-Triggered Membrane Insertion of Matrix Metalloproteinase-7, Supporter of Innate Immunity and Tumors. <i> Prior SH, Fulcher YG, Koppisetti RK, Jurkevich A, Van Doren SR. </i> Structure, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2MZH"},{"db":"PDB","id":"2MZI"},{"db":"PDB","id":"2MZE"}],"region_id":"DP03301r003","statement":[{"text":"These coordi-nates differ from the free form with a backbone RMSD of 1.6 A ̊across the catalytic domain and 2.1 A ̊across the pro-domain (omitting the disordered segments listed inTable 1)","type":"Results"},{"text":"Residue ranges used: 12–27, 31–72, 83–216, and 224–238. Uncertainties are SDs","type":"Table"},{"text":"The segments between the residues here indicated are the disordered regions (1-11, 28-30, 73-82, 217-223 and 239-250), corresponding to regions  18-28, 45-47, 90-99, 234-240 and 256-267 on the original protein sequence","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":90,"end":99,"reference_id":"26439767","reference_source":"pmid","reference_html":"Charge-Triggered Membrane Insertion of Matrix Metalloproteinase-7, Supporter of Innate Immunity and Tumors. <i> Prior SH, Fulcher YG, Koppisetti RK, Jurkevich A, Van Doren SR. </i> Structure, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2MZH"},{"db":"PDB","id":"2MZI"},{"db":"PDB","id":"2MZE"}],"region_id":"DP03301r004","statement":[{"text":"In concert with removal of auto-inhibition, bicelles introduce large peaks shifts (Figure S1A) and NOEs to theGlu74-Asn80 region that imply its change from disorder in the free state to formation of an ordered hairpin (Figure S6). ","type":"Results"},{"text":"The segments between the residues here indicated are the disordered regions (1-11, 28-30, 73-82, 217-223 and 239-250), corresponding to regions  18-28, 45-47, 90-99, 234-240 and 256-267 on the original protein sequence","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":21,"end":40,"reference_id":"28648610","reference_source":"pmid","reference_html":"Glycan Activation of a Sheddase: Electrostatic Recognition between Heparin and proMMP-7. <i> Fulcher YG, Prior SH, Masuko S, Li L, Pu D, Zhang F, Linhardt RJ, Van Doren SR. </i> Structure, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03301r005","statement":[{"text":"Also consistent with the hypothesis of distortion, the N-terminal 20 residues appear more disordered with heparin dp8 bound (Figures 6A and 6B)","type":"Discussion"},{"text":"Heparin dp8 may enhance disorder near the N terminus (Figure 6A) and appears to recruit the basic and dynamic C terminus a significant distance to the binding site on the back of the catalytic domain (Figure 6D), perhaps facilitating maturation (Figure 3)","type":"Discussion"},{"text":"The protein sequence here described starts on residue 21","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":5,"released":"2021_12","sequence":"MRLTVLCAVCLLPGSLALPLPQEAGGMSELQWEQAQDYLKRFYLYDSETKNANSLEAKLKEMQKFFGLPITGMLNSRVIEIMQKPRCGVPDVAEYSLFPNSPKWTSKVVTYRIVSYTRDLPHITVDRLVSKALNMWGKEIPLHFRKVVWGTADIMIGFARGAHGDSYPFDGPGNTLAHAFAPGTGLGGDAHFDEDERWTDGSSLGINFLYAATHELGHSLGMGHSSDPNAVMYPTYGNGDPQNFKLSQDDIKGIQKLYGKRSNSRKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI00000422BD","uniref100":"UniRef100_P09237","uniref90":"UniRef90_P09237","uniref50":"UniRef50_P09237","genes":[{"name":{"value":"MMP7"},"synonyms":[{"value":"MPSL1"},{"value":"PUMP1"}]}],"alphafold_very_low_content":0.052434456928838954,"disorder_content":0.16853932584269662,"disprot_consensus":{"full":[{"start":18,"end":40,"type":"D"},{"start":90,"end":99,"type":"T"},{"start":256,"end":267,"type":"D"}],"Structural state":[{"start":18,"end":40,"type":"D"},{"start":90,"end":99,"type":"D"},{"start":256,"end":267,"type":"D"}],"Structural transition":[{"start":90,"end":99,"type":"T"}]}},{"disprot_id":"DP03302","acc":"G5EFZ1","creator":"spenadias","date":"2021-05-13T08:01:52.957Z","features":{"pfam":[{"id":"PF01676","name":"Metalloenzyme superfamily","start":30,"end":105},{"id":"PF01676","name":"Metalloenzyme superfamily","start":323,"end":525},{"id":"PF06415","name":"BPG-independent PGAM N-terminus (iPGM_N)","start":106,"end":322}],"gene3D":[]},"length":539,"name":"2,3-bisphosphoglycerate-independent phosphoglycerate mutase","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":1,"end":19,"reference_id":"28368002","reference_source":"pmid","reference_html":"Macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases. <i> Yu H, Dranchak P, Li Z, MacArthur R, Munson MS, Mehzabeen N, Baird NJ, Battalie KP, Ross D, Lovell S, Carlow CK, Suga H, Inglese J. </i> Nat Commun, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5KGM"},{"db":"PDB","id":"5KGN"},{"db":"PDB","id":"5KGL"}],"region_id":"DP03302r001","statement":[{"text":"The final model of iPGM-m consisted of two subunits with two Mn2 þ and Zn2 þ ions modelled within domain A of each subunit (Supplementary Fig. 9a) and the first 20 residues of the N terminus and last 13 residues of the C terminus were disordered and could not be modelled. The\ntwo subunits are nearly identical with an RMSD deviation of 0.58 Å between Ca atoms for 517 residues aligned using GESAMT62 (Supplementary Fig. 9b). Crystals of the orthorhombic form (C. elegans iPGM-o) were obtained after approximately 6 months and diffracted to higher resolution than iPGM-m. Similarly, the N- and C-terminal residues were disordered in the iPGM-o as well.","type":"Methods"},{"text":"From the apo iPGM structure we observed that the N-terminal\n18 amino acids, unique to C. elegans iPGM, were disordered.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":520,"end":539,"reference_id":"28368002","reference_source":"pmid","reference_html":"Macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases. <i> Yu H, Dranchak P, Li Z, MacArthur R, Munson MS, Mehzabeen N, Baird NJ, Battalie KP, Ross D, Lovell S, Carlow CK, Suga H, Inglese J. </i> Nat Commun, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5KGM"},{"db":"PDB","id":"5KGN"},{"db":"PDB","id":"5KGL"}],"region_id":"DP03302r002","statement":[{"text":"The final model of iPGM-m consisted of two subunits with two Mn2 þ and Zn2 þ ions modelled within domain A of each subunit (Supplementary Fig. 9a) and the first 20 residues of the N terminus and last 13 residues of the C terminus were disordered and could not be modelled. The\ntwo subunits are nearly identical with an RMSD deviation of 0.58 Å between Ca atoms for 517 residues aligned using GESAMT62 (Supplementary Fig. 9b). Crystals of the orthorhombic form (C. elegans iPGM-o) were obtained after approximately 6 months and diffracted to higher resolution than iPGM-m. Similarly, the N- and C-terminal residues were disordered in the iPGM-o as well.","type":"Methods"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MFVALGAQIYRQYFGRRGMAMANNSSVANKVCLIVIDGWGVSEDPYGNAILNAQTPVMDKLCSGNWAQIEAHGLHVGLPEGLMGNSEVGHLNIGAGRVIYQDIVRINLAVKNNKFVTNESLVDACDRAKNGNGRLHLAGLVSDGGVHSHIDHMFALVKAIKELGVPELYLHFYGDGRDTSPNSGVGFLEQTLEFLEKTTGYGKLATVVGRYYAMDRDNRWERINVAYEAMIGGVGETSDEAGVVEVVRKRYAADETDEFLKPIILQGEKGRVQNDDTIIFFDYRADRMREISAAMGMDRYKDCNSKLAHPSNLQVYGMTQYKAEFPFKSLFPPASNKNVLAEWLAEQKVSQFHCAETEKYAHVTFFFNGGLEKQFEGEERCLVPSPKVATYDLQPEMSAAGVADKMIEQLEAGTHPFIMCNFAPPDMVGHTGVYEAAVKACEATDIAIGRIYEATQKHGYSLMVTADHGNAEKMKAPDGGKHTAHTCYRVPLTLSHPGFKFVDPADRHPALCDVAPTVLAIMGLPQPAEMTGVSIVQKI","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"dataset":[],"UniParc":"UPI000008014B","uniref100":"UniRef100_G5EFZ1","uniref90":"UniRef90_G5EFZ1","uniref50":"UniRef50_G5EFZ1","genes":[{"name":{"value":"ipgm-1","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"F57B10.3a","url":"https://www.wormbase.org/db/seq/sequence?name=F57B10.3a;class=Transcript"}}]},"orfNames":[{"value":"F57B10.3","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"F57B10.3a","url":"https://www.wormbase.org/db/seq/sequence?name=F57B10.3a;class=Transcript"}}]}]}],"alphafold_very_low_content":0.03710575139146568,"disorder_content":0.07235621521335807,"disprot_consensus":{"full":[{"start":1,"end":19,"type":"D"},{"start":520,"end":539,"type":"D"}],"Structural state":[{"start":1,"end":19,"type":"D"},{"start":520,"end":539,"type":"D"}]}},{"disprot_id":"DP03303","acc":"Q8IW75","creator":"rpancsa","date":"2021-05-13T08:31:38.042Z","features":{"pfam":[{"id":"PF00079","name":"Serpin (serine protease inhibitor)","start":51,"end":411}],"gene3D":[]},"length":414,"name":"Serpin A12","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":367,"end":377,"reference_id":"23370777","reference_source":"pmid","reference_html":"Vaspin inhibits kallikrein 7 by serpin mechanism. <i> Heiker JT, Klöting N, Kovacs P, Kuettner EB, Sträter N, Schultz S, Kern M, Stumvoll M, Blüher M, Beck-Sickinger AG. </i> Cell Mol Life Sci, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4IF8"}],"region_id":"DP03303r001","statement":[{"text":"The reactive center loop (RCL) (extending from G364 to P381) is flexible in the vaspin structure.","type":"Results"},{"text":"In one of the chains (A) of the 4IF8 structure the electron density is only missing for residues 367-377, not for the whole RCL.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-17T15:07:30.124Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":376,"end":380,"reference_id":"23370777","reference_source":"pmid","reference_html":"Vaspin inhibits kallikrein 7 by serpin mechanism. <i> Heiker JT, Klöting N, Kovacs P, Kuettner EB, Sträter N, Schultz S, Kern M, Stumvoll M, Blüher M, Beck-Sickinger AG. </i> Cell Mol Life Sci, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000048","term_name":"limited proteolysis display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4IF8"}],"region_id":"DP03303r002","statement":[{"text":"X-ray structures of SECs demonstrate that after initial cleavage of the RCL remaining residues beginning at the P15 glycine, following the standard nomenclature [28], are inserted into the β-sheet A as a new β-strand [27, 29].","type":"Results"},{"text":"SEC stands for serpin–enzyme complex (members of the serpin family typically form SDS-stable complexes with target proteases). ","type":"Curator statement"},{"text":"UniProt explanation for this protease cleavage reaction: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-20T14:15:54.400Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":367,"end":377,"reference_id":"23370777","reference_source":"pmid","reference_html":"Vaspin inhibits kallikrein 7 by serpin mechanism. <i> Heiker JT, Klöting N, Kovacs P, Kuettner EB, Sträter N, Schultz S, Kern M, Stumvoll M, Blüher M, Beck-Sickinger AG. </i> Cell Mol Life Sci, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03303r003","statement":[{"text":"It has been shown that the serpin inhibitory mechanism is critically dependent on the length of the RCL [31] and is furthermore structurally based on conserved small side-chain amino acids within the hinge region of inhibitory serpins. This also applies to vaspin, as the mutation of alanine 369 to proline (vaspinA369P) within the vaspin hinge region converts vaspin from inhibitor of hK7 to substrate.","type":"Results"},{"text":"The role of the Reactive Center Loop (RCL) in serpins is inhibition of proteases. I added the region 367-377 because that is the disordered fraction of the RCL.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T19:43:17.574Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":3,"released":"2021_06","sequence":"MNPTLGLAIFLAVLLTVKGLLKPSFSPRNYKALSEVQGWKQRMAAKELARQNMDLGFKLLKKLAFYNPGRNIFLSPLSISTAFSMLCLGAQDSTLDEIKQGFNFRKMPEKDLHEGFHYIIHELTQKTQDLKLSIGNTLFIDQRLQPQRKFLEDAKNFYSAETILTNFQNLEMAQKQINDFISQKTHGKINNLIENIDPGTVMLLANYIFFRARWKHEFDPNVTKEEDFFLEKNSSVKVPMMFRSGIYQVGYDDKLSCTILEIPYQKNITAIFILPDEGKLKHLEKGLQVDTFSRWKTLLSRRVVDVSVPRLHMTGTFDLKKTLSYIGVSKIFEEHGDLTKIAPHRSLKVGEAVHKAELKMDERGTEGAAGTGAQTLPMETPLVVKIDKPYLLLIYSEKIPSVLFLGKIVNPIGK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000000D86C","uniref100":"UniRef100_Q8IW75","uniref90":"UniRef90_Q8IW75","uniref50":"UniRef50_Q8IW75","genes":[{"name":{"value":"SERPINA12"}}],"alphafold_very_low_content":0.07246376811594203,"disorder_content":0.026570048309178744,"disprot_consensus":{"full":[{"start":367,"end":377,"type":"D"},{"start":378,"end":380,"type":"F"}],"Structural state":[{"start":367,"end":377,"type":"D"}],"Disorder function":[{"start":376,"end":380,"type":"F"}],"Molecular function":[{"start":367,"end":377,"type":"F"}]}},{"disprot_id":"DP03304","acc":"P36952","creator":"rpancsa","date":"2021-05-13T08:49:11.686Z","features":{"pfam":[{"id":"PF00079","name":"Serpin (serine protease inhibitor)","start":7,"end":375}],"gene3D":[]},"length":375,"name":"Serpin B5","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":332,"end":343,"reference_id":"15760906","reference_source":"pmid","reference_html":"The high resolution crystal structure of the human tumor suppressor maspin reveals a novel conformational switch in the G-helix. <i> Law RH, Irving JA, Buckle AM, Ruzyla K, Buzza M, Bashtannyk-Puhalovich TA, Beddoe TC, Nguyen K, Worrall DM, Bottomley SP, Bird PI, Rossjohn J, Whisstock JC. </i> J Biol Chem, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1XU8"},{"db":"PDB","id":"1WZ9"}],"region_id":"DP03304r001","statement":[{"text":"The RCL loop in both monomers was observed to be mobile and relatively disordered and was not modeled fully in either monomer.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-17T15:06:46.301Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":334,"end":338,"reference_id":"15760906","reference_source":"pmid","reference_html":"The high resolution crystal structure of the human tumor suppressor maspin reveals a novel conformational switch in the G-helix. <i> Law RH, Irving JA, Buckle AM, Ruzyla K, Buzza M, Bashtannyk-Puhalovich TA, Beddoe TC, Nguyen K, Worrall DM, Bottomley SP, Bird PI, Rossjohn J, Whisstock JC. </i> J Biol Chem, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000048","term_name":"limited proteolysis display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03304r002","statement":[{"text":"Recombinant maspin (18 μm) was treated with 0.25 μm recombinant human cathepsin L (24) at 37 °C for 30 min in 0.1 m NaAc, pH 5.5, 1 mm EDTA, 0.1% Brij-35, 10 mm cysteine. Complete cleavage within the RCL was confirmed by SDS-PAGE, and the molecular masses of the cleaved products were found to be 38.24 and 4.707 kDa by mass spectrometry. Based on these data (and the observation that the only cysteine residue in the C-terminal peptide is buried and unmodified in all crystal structures) the position of the cleavage site was mapped to P5/P6 (SIE↓VPG).","type":"Methods"},{"text":"The protease cleavage happens between residues 335 and 336 of the reactive center loop (RCL), which was annotated as regulation of limited proteolysis.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-20T14:07:16.440Z"},"ec_go":"IDA","disprot_namespace":"Disorder function"}],"regions_counter":2,"released":"2021_12","sequence":"MDALQLANSAFAVDLFKQLCEKEPLGNVLFSPICLSTSLSLAQVGAKGDTANEIGQVLHFENVKDVPFGFQTVTSDVNKLSSFYSLKLIKRLYVDKSLNLSTEFISSTKRPYAKELETVDFKDKLEETKGQINNSIKDLTDGHFENILADNSVNDQTKILVVNAAYFVGKWMKKFSESETKECPFRVNKTDTKPVQMMNMEATFCMGNIDSINCKIIELPFQNKHLSMFILLPKDVEDESTGLEKIEKQLNSESLSQWTNPSTMANAKVKLSIPKFKVEKMIDPKACLENLGLKHIFSEDTSDFSGMSETKGVALSNVIHKVCLEITEDGGDSIEVPGARILQHKDELNADHPFIYIIRHNKTRNIIFFGKFCSP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000004750D","uniref100":"UniRef100_P36952","uniref90":"UniRef90_P36952","uniref50":"UniRef50_P36952","genes":[{"name":{"value":"SERPINB5"},"synonyms":[{"value":"PI5"}]}],"alphafold_very_low_content":0.005333333333333333,"disorder_content":0.032,"disprot_consensus":{"full":[{"start":332,"end":343,"type":"D"}],"Structural state":[{"start":332,"end":343,"type":"D"}],"Disorder function":[{"start":334,"end":338,"type":"F"}]}},{"disprot_id":"DP03305","acc":"Q60675","creator":"rpancsa","date":"2021-05-14T07:55:57.137Z","features":{"pfam":[{"id":"PF00052","name":"Laminin B (Domain IV)","start":579,"end":718},{"id":"PF00052","name":"Laminin B (Domain IV)","start":1230,"end":1374},{"id":"PF00053","name":"Laminin EGF domain","start":340,"end":397},{"id":"PF00053","name":"Laminin EGF domain","start":410,"end":462},{"id":"PF00053","name":"Laminin EGF domain","start":465,"end":511},{"id":"PF00053","name":"Laminin EGF domain","start":719,"end":740},{"id":"PF00053","name":"Laminin EGF domain","start":803,"end":858},{"id":"PF00053","name":"Laminin EGF domain","start":861,"end":911},{"id":"PF00053","name":"Laminin EGF domain","start":914,"end":960},{"id":"PF00053","name":"Laminin EGF domain","start":963,"end":1007},{"id":"PF00053","name":"Laminin EGF domain","start":1010,"end":1048},{"id":"PF00053","name":"Laminin EGF domain","start":1056,"end":1104},{"id":"PF00053","name":"Laminin EGF domain","start":1375,"end":1401},{"id":"PF00053","name":"Laminin EGF domain","start":1465,"end":1520},{"id":"PF00053","name":"Laminin EGF domain","start":1523,"end":1563},{"id":"PF00054","name":"Laminin G domain","start":2170,"end":2309},{"id":"PF00054","name":"Laminin G domain","start":2364,"end":2503},{"id":"PF00054","name":"Laminin G domain","start":2550,"end":2690},{"id":"PF00054","name":"Laminin G domain","start":2789,"end":2916},{"id":"PF00055","name":"Laminin N-terminal (Domain VI)","start":36,"end":281},{"id":"PF02210","name":"Laminin G domain","start":2964,"end":3089},{"id":"PF06008","name":"Laminin Domain I","start":1590,"end":1849},{"id":"PF24973","name":"Laminin/attractin EGF domain","start":753,"end":796},{"id":"PF24973","name":"Laminin/attractin EGF domain","start":1416,"end":1453}],"gene3D":[]},"length":3118,"name":"Laminin subunit alpha-2","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":2730,"end":2743,"reference_id":"10747011","reference_source":"pmid","reference_html":"Structure of the C-terminal laminin G-like domain pair of the laminin alpha2 chain harbouring binding sites for alpha-dystroglycan and heparin. <i> Tisi D, Talts JF, Timpl R, Hohenester E. </i> EMBO J, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":2,"cross_refs":[{"db":"PDB","id":"1DYK"}],"region_id":"DP03305r001","statement":[{"text":"The first 19 residues including the APLA sequence are disordered in the crystal.","type":"Results"},{"text":"The disordered portion of the N–terminus, which is unusual in that it contains many prolines and hydrophobic residues, is likely to interact with some part of LG1–LG3 in the complete laminin LG1–LG5 tandem.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-10T14:05:25.761Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_06","sequence":"MPAATAGILLLLLLGTLEGSQTQRRQSQAHQQRGLFPAVLNLASNALITTNATCGEKGPEMYCKLVEHVPGQPVRNPQCRICNQNSSNPYQRHPITNAIDGKNTWWQSPSIKNGVEYHYVTITLDLQQVFQIAYVIVKAANSPRPGNWILERSLDDVEYKPWQYHAVTDTECLTLYNIYPRTGPPSYAKDDEVICTSFYSKIHPLENGEIHISLINGRPSADDPSPELLEFTSARYIRLRFQRIRTLNADLMMFAHKDPREIDPIVTRRYYYSVKDISVGGMCICYGHARACPLDPATNKSRCECEHNTCGESCDRCCPGFHQKPWRAGTFLTKSECEACNCHGKAEECYYDETVASRNLSLNIHGKYIGGGVCINCTHNTAGINCETCVDGFFRPKGVSPNYPRPCQPCHCDPTGSLSEVCVKDEKYAQRGLKPGSCHCKTGFGGVNCDRCVRGYHGYPDCQPCNCSGLGSTNEDPCVGPCSCKENVEGEDCSRCKSGFFNLQEDNQKGCEECFCSGVSNRCQSSYWTYGNIQDMRGWYLTDLSGRIRMAPQLDNPDSPQQISISNSEARKSLLDGYYWSAPPPYLGNRLPAVGGQLSFTISYDLEEEEDDTEKILQLMIIFEGNDLRISTAYKEVYLEPSEEHIEEVSLKEEAFTIHGTNLPVTRKDFMIVLTNLERVLMQITYNLGMDAIFRLSSVNLESAVPYPTDRRIATDVEVCQCPPGYSGSSCETCWPRHRRVNGTIFGGICEPCQCFAHAEACDDITGECLNCKDHTGGPYCNECLPGFYGDPTRGSPEDCQPCACPLNIPSNNFSPTCHLDRSLGLICDECPIGYTGPRCERCAEGYFGQPSIPGGSCQPCQCNDNLDYSIPGSCDSLSGSCLICKPGTTGRYCELCADGYFGDAVNAKNCQPCRCNINGSFSEICHTRTGQCECRPNVQGRHCDECKPETFGLQLGRGCLPCNCNSFGSKSFDCEASGQCWCQPGVAGKKCDRCAHGYFNFQEGGCIACDCSHLGNNCDPKTGQCICPPNTTGEKCSECLPNTWGHSIVTGCKVCNCSTVGSLASQCNVNTGQCSCHPKFSGMKCSECSRGHWNYPLCTLCDCFLPGTDATTCDLETRKCSCSDQTGQCSCKVNVEGVHCDRCRPGKFGLDAKNPLGCSSCYCFGVTSQCSEAKGLIRTWVTLSDEQTILPLVDEALQHTTTKGIAFQKPEIVAKMDEVRQELHLEPFYWKLPQQFEGKKLMAYGGKLKYAIYFEARDETGFATYKPQVIIRGGTPTHARIITRHMAAPLIGQLTRHEIEMTEKEWKYYGDDPRISRTVTREDFLDILYDIHYILIKATYGNVVRQSRISEISMEVAEPGHVLAGSPPAHLIERCDCPPGYSGLSCETCAPGFYRLRSEPGGRTPGPTLGTCVPCQCNGHSSQCDPETSVCQNCQHHTAGDFCERCALGYYGIVRGLPNDCQPCACPLISPSNNFSPSCVLEGLEDYRCTACPRGYEGQYCERCAPGYTGSPSSPGGSCQECECDPYGSLPVPCDRVTGLCTCRPGATGRKCDGCEHWHAREGAECVFCGDECTGLLLGDLARLEQMTMNINLTGPLPAPYKILYGLENTTQELKHLLSPQRAPERLIQLAEGNVNTLVMETNELLTRATKVTADGEQTGQDAERTNSRAESLEEFIKGLVQDAEAINEKAVQLNETLGNQDKTAERNLEELQKEIDRMLKELRSKDLQTQKEVAEDELVAAEGLLKRVNKLFGEPRAQNEDMEKDLQQKLAEYKNKLDDAWDLLREATDKTRDANRLSAANQKNMTILETKKEAIEGSKRQIENTLKEGNDILDEANRLLGEINSVIDYVDDIKTKLPPMSEELSDKIDDLAQEIKDRRLAEKVFQAESHAAQLNDSSAVLDGILDEAKNISFNATAAFRAYSNIKDYIDEAEKVAREAKELAQGATKLATSPQGLLKEDAKGSLQKSFRILNEAKKLANDVKGNHNDLNDLKTRLETADLRNSGLLGALNDTMDKLSAITNDTAAKLQAVKEKAREANDTAKAVLAQVKDLHQNLDGLKQNYNKLADSVAKTNAVVKDPSKNKIIADAGTSVRNLEQEADRLIDKLKPIKELEDNLKKNISEIKELINQARKQANSIKVSVSSGGDCVRTYRPEIKKGSYNNIVVHVKTAVADNLLFYLGSAKFIDFLAIEMRKGKVSFLWDVGSGVGRVEYPDLTIDDSYWYRIEASRTGRNGSISVRALDGPKASMVPSTYHSVSPPGYTILDVDANAMLFVGGLTGKIKKADAVRVITFTGCMGETYFDNKPIGLWNFREKEGDCKGCTVSPQVEDSEGTIQFDGEGYALVSRPIRWYPNISTVMFKFRTFSSSALLMYLATRDLKDFMSVELSDGHVKVSYDLGSGMTSVVSNQNHNDGKWKAFTLSRIQKQANISIVDIDSNQEENVATSSSGNNFGLDLKADDKIYFGGLPTLRNLSMKARPEVNVKKYSGCLKDIEISRTPYNILSSPDYVGVTKGCSLENVYTVSFPKPGFVELAAVSIDVGTEINLSFSTRNESGIILLGSGGTLTPPRRKRRQTTQAYYAIFLNKGRLEVHLSSGTRTMRKIVIKPEPNLFHDGREHSVHVERTRGIFTVQIDEDRRHMQNLTEEQPIEVKKLFVGGAPPEFQPSPLRNIPAFQGCVWNLVINSIPMDFAQPIAFKNADIGRCTYQKPREDESEAVPAEVIVQPQPVPTPAFPFPAPTMVHGPCVAESEPALLTGSKQFGLSRNSHIAIAFDDTKVKNRLTIELEVRTEAESGLLFYMARINHADFATVQLRNGFPYFSYDLGSGDTSTMIPTKINDGQWHKIKIVRVKQEGILYVDDASSQTISPKKADILDVVGILYVGGLPINYTTRRIGPVTYSLDGCVRNLHMEQAPVDLDQPTSSFHVGTCFANAESGTYFDGTGFAKAVGGFKVGLDLLVEFEFRTTRPTGVLLGVSSQKMDGMGIEMIDEKLMFHVDNGAGRFTAIYDAGIPGHMCNGQWHKVTAKKIKNRLELVVDGNQVDAQSPNSASTSADTNDPVFVGGFPGGLNQFGLTTNIRFRGCIRSLKLTKGTGKPLEVNFAKALELRGVQPVSCPTT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000002820F","uniref100":"UniRef100_Q60675","uniref90":"UniRef90_Q60675","uniref50":"UniRef50_P24043","genes":[{"name":{"value":"Lama2"}}],"disorder_content":0.004490057729313663,"disprot_consensus":{"full":[{"start":2730,"end":2743,"type":"D"}],"Structural state":[{"start":2730,"end":2743,"type":"D"}]}},{"disprot_id":"DP03306","acc":"Q02297","creator":"spenadias","date":"2021-05-17T11:57:28.057Z","features":{"pfam":[{"id":"PF00008","name":"EGF-like domain","start":187,"end":220},{"id":"PF02158","name":"Neuregulin intracellular region","start":267,"end":622},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":40,"end":129}],"gene3D":[]},"length":640,"name":"Pro-neuregulin-1, membrane-bound isoform","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":226,"end":239,"reference_id":"8639490","reference_source":"pmid","reference_html":"High-resolution solution structure of the EGF-like domain of heregulin-alpha. <i> Jacobsen NE, Abadi N, Sliwkowski MX, Reilly D, Skelton NJ, Fairbrother WJ. </i> Biochemistry, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":2,"cross_refs":[{"db":"PDB","id":"1HAF"},{"db":"PDB","id":"1HAE"}],"region_id":"DP03306r001","statement":[{"text":"The N- and C-terminal residues (1-2 and 50-63) and the Ω-loop comprising residues 24-30\nare disordered. ","type":"Abstract"},{"text":"Comparison of the HRG-R EGF-like domain structure with the previously determined\nstructure of human EGF [Hommel et al. (1992) J. Mol. Biol. 227, 271-282] reveals a high degree of structural similarity; excluding the N-terminal region (residues 1-13), the disordered Ω-loop region (residues 24-30) that contains a three-residue insertion in HRG-R relative to hEGF, and the disordered C-terminal region (residues 50-63), the CR alignment between the HRG-R and hEGF minimized mean structures has a rms difference of ∼1 Å.","type":"Abstract"},{"text":"The C-terminal residues, Met51-Tyr63, are clearly disordered (Figures 4 and 5) and flexible (as judged from 15N relaxation measurements; W. J. Fairbrother, unpublished results) in solution.","type":"Results"},{"text":"Excluding the N-terminal region (Ser1-Phe13), the disordered Ω-loop (Lys24-Ser30), and the disordered Cterminal region (Pro50-Tyr63), the CR alignment between the HRG-R EGF-like domain and hEGF minimized mean structures is very good, with an rms difference of 0.98 Å\n[this is likely within the accuracy limits of both structures (Zhao & Jardetzky, 1994)].","type":"Results"},{"text":"Pro20 and Tyr63 correspond to Pro226 and Tyr239","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-20T16:03:12.240Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":229,"end":241,"reference_id":"8062828","reference_source":"pmid","reference_html":"Solution structure of the epidermal growth factor-like domain of heregulin-alpha, a ligand for p180erbB-4. <i> Nagata K, Kohda D, Hatanaka H, Ichikawa S, Matsuda S, Yamamoto T, Suzuki A, Inagaki F. </i> EMBO J, 1994","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":2,"cross_refs":[{"db":"PDB","id":"1HRE"},{"db":"PDB","id":"1HRF"}],"region_id":"DP03306r002","statement":[{"text":"The C-terminal flanking region outside the EGF-like domain (Val229-Lys241) is highly disordered and is not shown.","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-20T16:03:18.117Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2022_06","sequence":"MSERKEGRGKGKGKKKERGSGKKPESAAGSQSPALPPRLKEMKSQESAAGSKLVLRCETSSEYSSLRFKWFKNGNELNRKNKPQNIKIQKKPGKSELRINKASLADSGEYMCKVISKLGNDSASANITIVESNEIITGMPASTEGAYVSSESPIRISVSTEGANTSSSTSTSTTGTSHLVKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCQPGFTGARCTENVPMKVQNQEKAEELYQKRVLTITGICIALLVVGIMCVVAYCKTKKQRKKLHDRLRQSLRSERNNMMNIANGPHHPNPPPENVQLVNQYVSKNVISSEHIVEREAETSFSTSHYTSTAHHSTTVTQTPSHSWSNGHTESILSESHSVIVMSSVENSRHSSPTGGPRGRLNGTGGPRECNSFLRHARETPDSYRDSPHSERYVSAMTTPARMSPVDFHTPSSPKSPPSEMSPPVSSMTVSMPSMAVSPFMEEERPLLLVTPPRLREKKFDHHPQQFSSFHHNPAHDSNSLPASPLRIVEDEEYETTQEYEPAQEPVKKLANSRRAKRTKPNGHIANRLEVDSNTSSQSSNSESETEDERVGEDTPFLGIQNPLAASLEATPAFRLADSRTNPAGRFSTQEEIQARLSSVIANQDPIAV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins","Cancer-related proteins","Extracellular matrix proteins"],"UniParc":"UPI000013DED6","uniref100":"UniRef100_Q02297","uniref90":"UniRef90_Q02297","uniref50":"UniRef50_Q02297","genes":[{"name":{"value":"NRG1"},"synonyms":[{"value":"GGF"},{"value":"HGL"},{"value":"HRGA"},{"value":"NDF"},{"value":"SMDF"}]}],"alphafold_very_low_content":0.60625,"disorder_content":0.025,"disprot_consensus":{"full":[{"start":226,"end":241,"type":"D"}],"Structural state":[{"start":226,"end":241,"type":"D"}]}},{"disprot_id":"DP03307","acc":"Q9UMD9","creator":"jssuarez","date":"2021-05-18T15:39:54.939Z","features":{"pfam":[{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":567,"end":621},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":749,"end":807},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":1438,"end":1482}],"gene3D":[]},"length":1497,"name":"Collagen alpha-1(XVII) chain","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":2,"end":455,"reference_id":"32219587","reference_source":"pmid","reference_html":"The intracellular domain of BP180/collagen XVII is intrinsically disordered and partially folds in an anionic membrane lipid-mimicking environment. <i> Tuusa J, Koski MK, Ruskamo S, Tasanen K. </i> Amino Acids, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03307r001","statement":[{"text":"The intracellular domain of BP180/collagen XVII is intrinsically disordered and partially folds in an anionic membrane lipid-mimicking environment.","type":"Title"},{"text":"The CD spectrum of BP180 ICD resembles one typical of a random coil structure (Fig. 3a), suggesting that bacterially expressed BP180 ICD is a disordered protein.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-20T14:36:28.863Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":2,"end":455,"reference_id":"32219587","reference_source":"pmid","reference_html":"The intracellular domain of BP180/collagen XVII is intrinsically disordered and partially folds in an anionic membrane lipid-mimicking environment. <i> Tuusa J, Koski MK, Ruskamo S, Tasanen K. </i> Amino Acids, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03307r002","statement":[{"text":"Next, we measured the CD spectrum for BP180 ICD in the presence of negatively charged unilamellar DMPC:DMPG lipid vesicles with a 1:100 protein:lipid molar ratio. A clear change in the CD spectrum was seen (Fig. 3b), with a more pronounced negative CD signal at the 222 nm wavelength as well as a decrease in the negative peak at 198 nm. This indicates a partially α-helical conformation with some regions remaining disordered. ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-20T14:36:32.696Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":2,"end":455,"reference_id":"32219587","reference_source":"pmid","reference_html":"The intracellular domain of BP180/collagen XVII is intrinsically disordered and partially folds in an anionic membrane lipid-mimicking environment. <i> Tuusa J, Koski MK, Ruskamo S, Tasanen K. </i> Amino Acids, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001164","ec_ontology":"ECO","ec_name":"co-sedimentation assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":3,"region_id":"DP03307r003","statement":[{"text":"Therefore, we incubated His-BP180 ICD with and without DMPC-DMPG vesicles (1:100 protein:lipid molar ratio) and centrifuged sedimentable material. The majority of BP180 ICD was co-sedimented with DMPC-DMPG vesicles, while a small amount of protein stayed in the supernatant (Fig. 3c). Little aggregation and sedimentation of BP180 ICD was visible in the absence of lipid vesicles. These results confirm the binding of the BP180 ICD to negatively charged lipid vesicles.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-20T14:36:37.086Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":3,"released":"2023_06","sequence":"MDVTKKNKRDGTEVTERIVTETVTTRLTSLPPKGGTSNGYAKTASLGGGSRLEKQSLTHGSSGYINSTGSTRGHASTSSYRRAHSPASTLPNSPGSTFERKTHVTRHAYEGSSSGNSSPEYPRKEFASSSTRGRSQTRESEIRVRLQSASPSTRWTELDDVKRLLKGSRSASVSPTRNSSNTLPIPKKGTVETKIVTASSQSVSGTYDATILDANLPSHVWSSTLPAGSSMGTYHNNMTTQSSSLLNTNAYSAGSVFGVPNNMASCSPTLHPGLSTSSSVFGMQNNLAPSLTTLSHGTTTTSTAYGVKKNMPQSPAAVNTGVSTSAACTTSVQSDDLLHKDCKFLILEKDNTPAKKEMELLIMTKDSGKVFTASPASIAATSFSEDTLKKEKQAAYNADSGLKAEANGDLKTVSTKGKTTTADIHSYGSSGGGGSGGGGGVGGAGGGPWGPAPAWCPCGSCCSWWKWLLGLLLTWLLLLGLLFGLIALAEEVRKLKARVDELERIRRSILPYGDSMDRIEKDRLQGMAPAAGADLDKIGLHSDSQEELWMFVRKKLMMEQENGNLRGSPGPKGDMGSPGPKGDRGFPGTPGIPGPLGHPGPQGPKGQKGSVGDPGMEGPMGQRGREGPMGPRGEAGPPGSGEKGERGAAGEPGPHGPPGVPGSVGPKGSSGSPGPQGPPGPVGLQGLRGEVGLPGVKGDKGPMGPPGPKGDQGEKGPRGLTGEPGMRGLPGAVGEPGAKGAMGPAGPDGHQGPRGEQGLTGMPGIRGPPGPSGDPGKPGLTGPQGPQGLPGTPGRPGIKGEPGAPGKIVTSEGSSMLTVPGPPGPPGAMGPPGPPGAPGPAGPAGLPGHQEVLNLQGPPGPPGPRGPPGPSIPGPPGPRGPPGEGLPGPPGPPGSFLSNSETFLSGPPGPPGPPGPKGDQGPPGPRGHQGEQGLPGFSTSGSSSFGLNLQGPPGPPGPQGPKGDKGDPGVPGALGIPSGPSEGGSSSTMYVSGPPGPPGPPGPPGSISSSGQEIQQYISEYMQSDSIRSYLSGVQGPPGPPGPPGPVTTITGETFDYSELASHVVSYLRTSGYGVSLFSSSISSEDILAVLQRDDVRQYLRQYLMGPRGPPGPPGASGDGSLLSLDYAELSSRILSYMSSSGISIGLPGPPGPPGLPGTSYEELLSLLRGSEFRGIVGPPGPPGPPGIPGNVWSSISVEDLSSYLHTAGLSFIPGPPGPPGPPGPRGPPGVSGALATYAAENSDSFRSELISYLTSPDVRSFIVGPPGPPGPQGPPGDSRLLSTDASHSRGSSSSSHSSSVRRGSSYSSSMSTGGGGAGSLGAGGAFGEAAGDRGPYGTDIGPGGGYGAAAEGGMYAGNGGLLGADFAGDLDYNELAVRVSESMQRQGLLQGMAYTVQGPPGQPGPQGPPGISKVFSAYSNVTADLMDFFQTYGAIQGPPGQKGEMGTPGPKGDRGPAGPPGHPGPPGPRGHKGEKGDKGDQVYAGRRRRRSIAVKP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000006F1D3","uniref100":"UniRef100_Q9UMD9","uniref90":"UniRef90_Q9UMD9","uniref50":"UniRef50_Q9UMD9","genes":[{"name":{"value":"COL17A1"},"synonyms":[{"value":"BP180"},{"value":"BPAG2"}]}],"alphafold_very_low_content":0.7107548430193721,"disorder_content":0.3032732130928524,"disprot_consensus":{"full":[{"start":2,"end":455,"type":"T"}],"Structural state":[{"start":2,"end":455,"type":"D"}],"Structural transition":[{"start":2,"end":455,"type":"T"}],"Molecular function":[{"start":2,"end":455,"type":"F"}]}},{"disprot_id":"DP03308","acc":"Q96MS0","creator":"jssuarez","date":"2021-05-18T17:00:25.343Z","features":{"pfam":[{"id":"PF00041","name":"Fibronectin type III domain","start":558,"end":645},{"id":"PF00041","name":"Fibronectin type III domain","start":682,"end":760},{"id":"PF00041","name":"Fibronectin type III domain","start":771,"end":860},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":168,"end":249},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":258,"end":343},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":451,"end":532},{"id":"PF13927","name":"Immunoglobulin domain","start":64,"end":147},{"id":"PF13927","name":"Immunoglobulin domain","start":346,"end":426}],"gene3D":[]},"length":1386,"name":"Roundabout homolog 3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":654,"end":667,"reference_id":"32198364","reference_source":"pmid","reference_html":"NELL2-Robo3 complex structure reveals mechanisms of receptor activation for axon guidance. <i> Pak JS, DeLoughery ZJ, Wang J, Acharya N, Park Y, Jaworski A, Özkan E. </i> Nat Commun, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP03308r001","statement":[{"text":"We crystallized a complex of NELL2 EGF1–6 with Robo3 FN1, and Robo3 FN2–3 alone, following proteolysis within the 15-residue-long flexible linker between FN1 and FN2 in crystallization drops (Supplementary Fig. 2a)","type":"Results"},{"text":"Silver staining of the gels revealed that the first crystal form was likely NELL2 EGF1–6 complexed to Robo3 FN1 following proteolysis in the linker joining FN1 and FN2 domains (Supplementary Fig. 2a), and the second crystal form likely contained the remaining FN2 and FN3 domains of Robo3.","type":"Methods"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-20T14:33:44.722Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":654,"end":667,"reference_id":"32198364","reference_source":"pmid","reference_html":"NELL2-Robo3 complex structure reveals mechanisms of receptor activation for axon guidance. <i> Pak JS, DeLoughery ZJ, Wang J, Acharya N, Park Y, Jaworski A, Özkan E. </i> Nat Commun, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03308r002","statement":[{"text":"We crystallized a complex of NELL2 EGF1–6 with Robo3 FN1, and Robo3 FN2–3 alone, following proteolysis within the 15-residue-long flexible linker between FN1 and FN2 in crystallization drops (Supplementary Fig. 2a)","type":"Results"},{"text":"Silver staining of the gels revealed that the first crystal form was likely NELL2 EGF1–6 complexed to Robo3 FN1 following proteolysis in the linker joining FN1 and FN2 domains (Supplementary Fig. 2a), and the second crystal form likely contained the remaining FN2 and FN3 domains of Robo3.","type":"Methods"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-20T14:33:45.579Z"},"ec_go":"IDA","disprot_namespace":"Disorder function"}],"regions_counter":2,"released":"2021_06","sequence":"MLRYLLKTLLQMNLFADSLAGDISNSSELLLGFNSSLAALNHTLLPPGDPSLNGSRVGPEDAMPRIVEQPPDLLVSRGEPATLPCRAEGRPRPNIEWYKNGARVATVREDPRAHRLLLPSGALFFPRIVHGRRARPDEGVYTCVARNYLGAAASRNASLEVAVLRDDFRQSPGNVVVAVGEPAVLECVPPRGHPEPSVSWRKDGARLKEEEGRITIRGGKLMMSHTLKSDAGMYVCVASNMAGERESAAAEVMVLERPSFLRRPVNQVVLADAPVTFLCEVKGDPPPRLRWRKEDGELPTGRYEIRSDHSLWIGHVSAEDEGTYTCVAENSVGRAEASGSLSVHVPPQLVTQPQDQMAAPGESVAFQCETKGNPPPAIFWQKEGSQVLLFPSQSLQPTGRFSVSPRGQLNITAVQRGDAGYYVCQAVSVAGSILAKALLEIKGASLDGLPPVILQGPANQTLVLGSSVWLPCRVTGNPQPSVRWKKDGQWLQGDDLQFKTMANGTLYIANVQEMDMGFYSCVAKSSTGEATWSGWLKMREDWGVSPDPPTEPSSPPGAPSQPVVTEITKNSITLTWKPNPQTGAAVTSYVIEAFSPAAGNTWRTVADGVQLETHTVSGLQPNTIYLFLVRAVGAWGLSEPSPVSEPVRTQDSSPSRPVEDPWRGQQGLAEVAVRLQEPIVLGPRTLQVSWTVDGPVQLVQGFRVSWRVAGPEGGSWTMLDLQSPSQQSTVLRGLPPGTQIQIKVQAQGQEGLGAESLSVTRSIPEEAPSGPPQGVAVALGGDGNSSITVSWEPPLPSQQNGVITEYQIWCLGNESRFHLNRSAAGWARSAMLRGLVPGLLYRTLVAAATSAGVGVPSAPVLVQLPSPPDLEPGLEVGAGLAVRLARVLREPAFLAGSGAACGALLLGLCAALYWRRKQRKELSHYTASFAYTPAVSFPHSEGLSGASSRPPMGLGPAPYSWLADSWPHPSRSPSAQEPRGSCCPSNPDPDDRYYNEAGISLYLAQTARGTAAPGEGPVYSTIDPAGEELQTFHGGFPQHPSGDLGPWSQYAPPEWSQGDSGAKGGKVKLLGKPVQMPSLNWPEALPPPPPSCELSCLEGPEEELEGSSEPEEWCPPMPERSHLTEPSSSGGCLVTPSRRETPSPTPSYGQQSTATLTPSPPDPPQPPTDMPHLHQMPRRVPLGPSSPLSVSQPMLGIREARPAGLGAGPAASPHLSPSPAPSTASSAPGRTWQGNGEMTPPLQGPRARFRKKPKALPYRRENSPGDLPPPPLPPPEEEASWALELRAAGSMSSLERERSGERKAVQAVPLAAQRVLHPDEEAWLPYSRPSFLSRGQGTSTCSTAGSNSSRGSSSSRGSRGPGRSRSRSQSRSQSQRPGQKRREEPR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000006DEA8","uniref100":"UniRef100_Q96MS0","uniref90":"UniRef90_Q96MS0","uniref50":"UniRef50_Q96MS0","genes":[{"name":{"value":"ROBO3"}}],"alphafold_very_low_content":0.42207792207792205,"disorder_content":0.010101010101010102,"disprot_consensus":{"full":[{"start":654,"end":667,"type":"D"}],"Structural state":[{"start":654,"end":667,"type":"D"}],"Disorder function":[{"start":654,"end":667,"type":"F"}]}},{"disprot_id":"DP03309","acc":"O60486","creator":"jssuarez","date":"2021-05-18T18:17:29.890Z","features":{"pfam":[{"id":"PF01437","name":"Plexin repeat","start":454,"end":507},{"id":"PF01833","name":"IPT/TIG domain","start":664,"end":747},{"id":"PF01833","name":"IPT/TIG domain","start":754,"end":840},{"id":"PF08337","name":"Plexin cytoplasmic RasGAP domain","start":1013,"end":1183},{"id":"PF08337","name":"Plexin cytoplasmic RasGAP domain","start":1302,"end":1535},{"id":"PF20170","name":"Plexin cytoplasmic RhoGTPase-binding domain","start":1184,"end":1301}],"gene3D":[]},"length":1568,"name":"Plexin-C1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":642,"end":659,"reference_id":"32327662","reference_source":"pmid","reference_html":"Cryo-EM structure of the PlexinC1/A39R complex reveals inter-domain interactions critical for ligand-induced activation. <i> Kuo YC, Chen H, Shang G, Uchikawa E, Tian H, Bai XC, Zhang X. </i> Nat Commun, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6VXK"}],"region_id":"DP03309r001","statement":[{"text":"There is a large gap of ~30 Å between the end of the first rod and the beginning of the second (Fig. 2a). This gap is actually connected by the ~15-residue linker between the PSI2 and IPT2 domains (Supplementary Fig. 6), which is invisible in the cryo-EM map and therefore not included in the atomic model. ","type":"Results"},{"text":"Disorder is inferred from missing residues in the cryo-EM map. ","type":"Curator statement"},{"text":"In contrast to class A plexins, the PSI2 and IPT2 domains in PlexinC1 are not rigidly connected to each other due to the flexible linker between them.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-20T14:38:11.680Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":642,"end":659,"reference_id":"32327662","reference_source":"pmid","reference_html":"Cryo-EM structure of the PlexinC1/A39R complex reveals inter-domain interactions critical for ligand-induced activation. <i> Kuo YC, Chen H, Shang G, Uchikawa E, Tian H, Bai XC, Zhang X. </i> Nat Commun, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"6VXK"}],"region_id":"DP03309r002","statement":[{"text":"There is a large gap of ~30 Å between the end of the first rod and the beginning of the second (Fig. 2a). This gap is actually connected by the ~15-residue linker between the PSI2 and IPT2 domains (Supplementary Fig. 6), which is invisible in the cryo-EM map and therefore not included in the atomic model. ","type":"Results"},{"text":"Disorder is inferred from missing residues in the cryo-EM map. ","type":"Curator statement"},{"text":"In contrast to class A plexins, the PSI2 and IPT2 domains in PlexinC1 are not rigidly connected to each other due to the flexible linker between them.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-20T14:38:13.545Z"},"ec_go":"IDA","disprot_namespace":"Disorder function"}],"regions_counter":2,"released":"2021_06","sequence":"MEVSRRKAPPRPPRPAAPLPLLAYLLALAAPGRGADEPVWRSEQAIGAIAASQEDGVFVASGSCLDQLDYSLEHSLSRLYRDQAGNCTEPVSLAPPARPRPGSSFSKLLLPYREGAAGLGGLLLTGWTFDRGACEVRPLGNLSRNSLRNGTEVVSCHPQGSTAGVVYRAGRNNRWYLAVAATYVLPEPETASRCNPAASDHDTAIALKDTEGRSLATQELGRLKLCEGAGSLHFVDAFLWNGSIYFPYYPYNYTSGAATGWPSMARIAQSTEVLFQGQASLDCGHGHPDGRRLLLSSSLVEALDVWAGVFSAAAGEGQERRSPTTTALCLFRMSEIQARAKRVSWDFKTAESHCKEGDQPERVQPIASSTLIHSDLTSVYGTVVMNRTVLFLGTGDGQLLKVILGENLTSNCPEVIYEIKEETPVFYKLVPDPVKNIYIYLTAGKEVRRIRVANCNKHKSCSECLTATDPHCGWCHSLQRCTFQGDCVHSENLENWLDISSGAKKCPKIQIIRSSKEKTTVTMVGSFSPRHSKCMVKNVDSSRELCQNKSQPNRTCTCSIPTRATYKDVSVVNVMFSFGSWNLSDRFNFTNCSSLKECPACVETGCAWCKSARRCIHPFTACDPSDYERNQEQCPVAVEKTSGGGRPKENKGNRTNQALQVFYIKSIEPQKVSTLGKSNVIVTGANFTRASNITMILKGTSTCDKDVIQVSHVLNDTHMKFSLPSSRKEMKDVCIQFDGGNCSSVGSLSYIALPHCSLIFPATTWISGGQNITMMGRNFDVIDNLIISHELKGNINVSEYCVATYCGFLAPSLKSSKVRTNVTVKLRVQDTYLDCGTLQYREDPRFTGYRVESEVDTELEVKIQKENDNFNISKKDIEITLFHGENGQLNCSFENITRNQDLTTILCKIKGIKTASTIANSSKKVRVKLGNLELYVEQESVPSTWYFLIVLPVLLVIVIFAAVGVTRHKSKELSRKQSQQLELLESELRKEIRDGFAELQMDKLDVVDSFGTVPFLDYKHFALRTFFPESGGFTHIFTEDMHNRDANDKNESLTALDALICNKSFLVTVIHTLEKQKNFSVKDRCLFASFLTIALQTKLVYLTSILEVLTRDLMEQCSNMQPKLMLRRTESVVEKLLTNWMSVCLSGFLRETVGEPFYLLVTTLNQKINKGPVDVITCKALYTLNEDWLLWQVPEFSTVALNVVFEKIPENESADVCRNISVNVLDCDTIGQAKEKIFQAFLSKNGSPYGLQLNEIGLELQMGTRQKELLDIDSSSVILEDGITKLNTIGHYEISNGSTIKVFKKIANFTSDVEYSDDHCHLILPDSEAFQDVQGKRHRGKHKFKVKEMYLTKLLSTKVAIHSVLEKLFRSIWSLPNSRAPFAIKYFFDFLDAQAENKKITDPDVVHIWKTNSLPLRFWVNILKNPQFVFDIKKTPHIDGCLSVIAQAFMDAFSLTEQQLGKEAPTNKLLYAKDIPTYKEEVKSYYKAIRDLPPLSSSEMEEFLTQESKKHENEFNEEVALTEIYKYIVKYFDEILNKLERERGLEEAQKQLLHVKVLFDEKKKCKWM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000038AF4","uniref100":"UniRef100_O60486","uniref90":"UniRef90_O60486","uniref50":"UniRef50_O60486","genes":[{"name":{"value":"PLXNC1"},"synonyms":[{"value":"VESPR"}]}],"alphafold_very_low_content":0.08482142857142858,"disorder_content":0.011479591836734694,"disprot_consensus":{"full":[{"start":642,"end":659,"type":"D"}],"Structural state":[{"start":642,"end":659,"type":"D"}],"Disorder function":[{"start":642,"end":659,"type":"F"}]}},{"disprot_id":"DP03310","acc":"Q3U4G3","creator":"jssuarez","date":"2021-05-19T10:04:17.915Z","features":{"pfam":[{"id":"PF01501","name":"Glycosyl transferase family 8","start":181,"end":354}],"gene3D":[]},"length":392,"name":"Xyloside xylosyltransferase 1","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":43,"end":87,"reference_id":"26414444","reference_source":"pmid","reference_html":"Notch-modifying xylosyltransferase structures support an SNi-like retaining mechanism. <i> Yu H, Takeuchi M, LeBarron J, Kantharia J, London E, Bakker H, Haltiwanger RS, Li H, Takeuchi H. </i> Nat Chem Biol, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP03310r001","statement":[{"text":"Computational secondary structure analysis using PSIPRED (http://bioinf.cs.ucl.ac.uk/psipred/) predicted a largely unstructured loop at the N-terminus spanning ~S43–P95. We therefore subjected the purified protein to limited proteolysis by a panel of ten proteases (Proti-Ace &Proti-Ace 2 kit, Hampton Research). Based on the favorable cleavage pattern, we chose trypsin for preparative treatment with protein to trypsin ratio of 500:1 (w/w) and 4°C overnight incubation. The trypsinized sample was further purified by size-exclusion chromatography (Superdex 200, GE Healthcare) in 20 mM HEPES, pH 7.5, 150 mM NaCl. Mass spectrometry detected peptides from S87 to R373 in the purified sample, indicating a stable domain, which was subsequently shown to retain the enzyme activity.","type":"Methods"},{"text":"The overall structure consists of ~300 residues (V93–E391), lacking the N-terminal unstructured loop (~S43–V92) that was removed by limited proteolysis (See Online Methods). ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-20T14:32:40.490Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_06","sequence":"MGLLRGGAACARAMARLGALRSHYCALLLAAALAVCAFYYLGSGRETFSSATKRLKEARAGAAAPTPPAPELARGSAAPASGAKAKSLEGGVVVPVDYHLLMMFTKAEHNAPLQAKARVALSSLLRLAKFEAHEVLNLHFVSEEASREVAKALLRELLPPAAGFKCKVIFHDVAVLTDKLFPVVEAMQKYFSAGSGTYYSDSIFFLSVAMHQIMPKEIPRIIQLDLDLKYKTNIRELFEEFDNFLPGAVIGIAREMQPVYRHTFWQFRHENPKTRVGDPPPEGLPGFNSGVMLLNLEAMRQSPLYSHLLEPSWVQQLADKYHFRGHLGDQDFFTMIGMEHPELFHVLDCTWNRQLCTWWRDHGYSDVFQAYFRCEGHVKIYHGNCNTPIPED","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"dataset":[],"UniParc":"UPI00005ACD93","uniref100":"UniRef100_Q3U4G3","uniref90":"UniRef90_Q3U4G3","uniref50":"UniRef50_Q3U4G3","genes":[{"name":{"value":"Xxylt1"}}],"alphafold_very_low_content":0.12244897959183673,"disorder_content":0.11479591836734694,"disprot_consensus":{"full":[{"start":43,"end":87,"type":"D"}],"Structural state":[{"start":43,"end":87,"type":"D"}]}},{"disprot_id":"DP03311","acc":"P00740","creator":"jssuarez","date":"2021-05-19T10:36:28.961Z","features":{"pfam":[{"id":"PF00008","name":"EGF-like domain","start":97,"end":127},{"id":"PF00089","name":"Trypsin","start":227,"end":454},{"id":"PF00594","name":"Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain","start":52,"end":92},{"id":"PF14670","name":"Coagulation Factor Xa inhibitory site","start":134,"end":170}],"gene3D":[]},"length":461,"name":"Coagulation factor IX","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":47,"end":93,"reference_id":"7713897","reference_source":"pmid","reference_html":"Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy. <i> Freedman SJ, Furie BC, Furie B, Baleja JD. </i> J Biol Chem, 1995","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1CFH"}],"region_id":"DP03311r001","statement":[{"text":"In the amide-amide proton region of the NOESY spectrum (Fig. 3), we observed sequential NH-NH contacts, which indicated α helical structure in the carboxyl terminus of the peptide(14). Following the assignment of all proton resonances, short range and medium range interactions were defined from the NOESY spectrum. The absence of any long range interactions indicated the lack of a compact tertiary structure or the presence of different conformers rapidly interconverting on an NMR time scale.","type":"Results"},{"text":"Of note, authors describe 3 structured regions, residues 6–9, 18–23, and 37–46. \n\"These three structured segments exist autonomously in that they appear to have no interactions with each other or with other portions of the molecule (Fig. 6).\"","type":"Curator statement"},{"text":"The absence of any long range interactions indicated the lack of a compact tertiary structure or the presence of different conformers rapidly interconverting on an NMR time scale. ","type":"Results"},{"text":"The domain described by the authors corresponds to residues 47-93 of the UniProt sequence.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-26T09:42:51.818Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":47,"end":93,"reference_id":"7713897","reference_source":"pmid","reference_html":"Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy. <i> Freedman SJ, Furie BC, Furie B, Baleja JD. </i> J Biol Chem, 1995","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000013","term_name":"pre-molten globule to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP03311r002","statement":[{"text":"The domain described by the authors corresponds to residues 47-93 of the UniProt sequence.","type":"Curator statement"},{"text":"Upon the addition of Ca(II), the proton spectrum revealed increased dispersion of resonances in all regions of the spectrum (>0.4 ppm from the random coil values) (Fig. 1B). Specifically, there were downfield-shifted amide proton resonances and upfield-shifted methyl proton resonances. In addition, the metal-free and Ca(II)-bound forms of the peptide were in slow exchange on an NMR time scale. For example, the tryptophan indole amide protons from apoFactor IX (1-47) and the Factor IX (1-47):Ca(II) binary complex could be observed simultaneously at 10.25 and 10.19 ppm, respectively. These results suggest that a new structure is adopted following the addition of calcium ions that is different from and likely more structured than the metal-free form.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-26T09:42:52.539Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":70,"end":74,"reference_id":"14722079","reference_source":"pmid","reference_html":"Crystal structure of the calcium-stabilized human factor IX Gla domain bound to a conformation-specific anti-factor IX antibody. <i> Huang M, Furie BC, Furie B. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03311r003","statement":[{"text":"Residues 72 and 73 bind Ca+2 ions according to the crystal structure (PDB: 1NLO).","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-26T09:43:22.695Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":47,"end":93,"reference_id":"7547952","reference_source":"pmid","reference_html":"Structure of the calcium ion-bound gamma-carboxyglutamic acid-rich domain of factor IX. <i> Freedman SJ, Furie BC, Furie B, Baleja JD. </i> Biochemistry, 1995","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000013","term_name":"pre-molten globule to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1CFI"}],"region_id":"DP03311r004","statement":[{"text":"The domain described by the authors corresponds to residues 47-93 of the UniProt sequence.","type":"Curator statement"},{"text":"We now report the three-dimensional structure of\nthe Ca(II)-bound peptide in solution as determined by NMR\nmethods. A comparison of this structure with apo-factor IX\n(1—47) reveals the nature of the Ca(ID-induced conformational transition in factor IX.","type":"Introduction"},{"text":"The tertiary structure consists of a large carboxyl-terminal\nglobular core (residues 13—47) adjacent to a large aminoterminal loop (residues 1-12) (Figure 6)","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-26T09:42:16.506Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":47,"end":57,"reference_id":"8663165","reference_source":"pmid","reference_html":"Identification of the phospholipid binding site in the vitamin K-dependent blood coagulation protein factor IX. <i> Freedman SJ, Blostein MD, Baleja JD, Jacobs M, Furie BC, Furie B. </i> J Biol Chem, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1MGX"}],"region_id":"DP03311r005","statement":[{"text":"The domain described by the authors corresponds to residues 47-93 of the UniProt sequence.","type":"Curator statement"},{"text":"Upon occupancy of specific metal bindings sites that interact with many divalent cations, including Mg2+, the Gla domain assumes formal structure except that residues 1–11 remain flexible and motile. ","type":"Results"},{"text":"In contrast, the amino-terminal 11 residues lacked defined structure in Factor IX (1–47)-Mg2+, with the exception of a short loop from residue 6 to 9.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-26T09:41:50.458Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":47,"end":57,"reference_id":"8663165","reference_source":"pmid","reference_html":"Identification of the phospholipid binding site in the vitamin K-dependent blood coagulation protein factor IX. <i> Freedman SJ, Blostein MD, Baleja JD, Jacobs M, Furie BC, Furie B. </i> J Biol Chem, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP03311r006","statement":[{"text":"The domain described by the authors corresponds to residues 47-93 of the UniProt sequence.","type":"Curator statement"},{"text":"With occupancy of another set of metal bindings, sites that can be occupied only by Ca2+, the entire polypeptide backbone of the Gla domain is defined, including the NH2-terminal loop (Fig. 5).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-26T09:41:45.513Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":70,"end":74,"reference_id":"14722079","reference_source":"pmid","reference_html":"Crystal structure of the calcium-stabilized human factor IX Gla domain bound to a conformation-specific anti-factor IX antibody. <i> Huang M, Furie BC, Furie B. </i> J Biol Chem, 2004","date":"2022-12-06T11:01:26.265Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_12","version":4,"cross_refs":[{"db":"PDB","id":"1NL0"}],"region_id":"DP03311r007","statement":[{"text":"Residues 72 and 73 bind Ca+2 ions according to the crystal structure (PDB: 1NLO).","type":"Curator statement"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a calcium ion (Ca2+).\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-20T17:15:52.781Z"}},{"start":74,"end":78,"reference_id":"14722079","reference_source":"pmid","reference_html":"Crystal structure of the calcium-stabilized human factor IX Gla domain bound to a conformation-specific anti-factor IX antibody. <i> Huang M, Furie BC, Furie B. </i> J Biol Chem, 2004","date":"2022-12-06T11:01:39.643Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_12","version":4,"cross_refs":[{"db":"PDB","id":"1NL0"}],"region_id":"DP03311r008","statement":[{"text":"Residue 76 binds Ca+2 ions according to the crystal structure (PDB: 1NLO).","type":"Curator statement"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a calcium ion (Ca2+).\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":74,"end":78,"reference_id":"14722079","reference_source":"pmid","reference_html":"Crystal structure of the calcium-stabilized human factor IX Gla domain bound to a conformation-specific anti-factor IX antibody. <i> Huang M, Furie BC, Furie B. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03311r009","statement":[{"text":"Residue 76 binds Ca+2 ions according to the crystal structure (PDB: 1NLO).","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-26T09:43:23.272Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":52,"end":56,"reference_id":"14722079","reference_source":"pmid","reference_html":"Crystal structure of the calcium-stabilized human factor IX Gla domain bound to a conformation-specific anti-factor IX antibody. <i> Huang M, Furie BC, Furie B. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03311r010","statement":[{"text":"Residues 53 and 54 bind Ca+2 ions according to the crystal structure (PDB: 1NLO).","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-26T09:43:23.973Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":52,"end":56,"reference_id":"14722079","reference_source":"pmid","reference_html":"Crystal structure of the calcium-stabilized human factor IX Gla domain bound to a conformation-specific anti-factor IX antibody. <i> Huang M, Furie BC, Furie B. </i> J Biol Chem, 2004","date":"2022-12-06T11:01:49.565Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_12","version":4,"cross_refs":[{"db":"PDB","id":"1NL0"}],"region_id":"DP03311r011","statement":[{"text":"Residues 53 and 54 bind Ca+2 ions according to the crystal structure (PDB: 1NLO).","type":"Curator statement"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a calcium ion (Ca2+).\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":47,"end":51,"reference_id":"14722079","reference_source":"pmid","reference_html":"Crystal structure of the calcium-stabilized human factor IX Gla domain bound to a conformation-specific anti-factor IX antibody. <i> Huang M, Furie BC, Furie B. </i> J Biol Chem, 2004","date":"2022-12-06T11:02:00.627Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_12","version":4,"cross_refs":[{"db":"PDB","id":"1NL0"}],"region_id":"DP03311r012","statement":[{"text":"Residues 47 and 48 bind Ca+2 ions according to the crystal structure (PDB: 1NLO).","type":"Curator statement"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a calcium ion (Ca2+).\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":47,"end":51,"reference_id":"14722079","reference_source":"pmid","reference_html":"Crystal structure of the calcium-stabilized human factor IX Gla domain bound to a conformation-specific anti-factor IX antibody. <i> Huang M, Furie BC, Furie B. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03311r013","statement":[{"text":"Residues 47 and 48 bind Ca+2 ions according to the crystal structure (PDB: 1NLO).","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-26T09:43:25.475Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":60,"end":64,"reference_id":"14722079","reference_source":"pmid","reference_html":"Crystal structure of the calcium-stabilized human factor IX Gla domain bound to a conformation-specific anti-factor IX antibody. <i> Huang M, Furie BC, Furie B. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03311r014","statement":[{"text":"Residues 61 and 63 bind Ca+2 ions according to the crystal structure (PDB: 1NLO).","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-26T09:43:26.078Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":60,"end":64,"reference_id":"14722079","reference_source":"pmid","reference_html":"Crystal structure of the calcium-stabilized human factor IX Gla domain bound to a conformation-specific anti-factor IX antibody. <i> Huang M, Furie BC, Furie B. </i> J Biol Chem, 2004","date":"2022-12-06T11:02:10.812Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_12","version":4,"cross_refs":[{"db":"PDB","id":"1NL0"}],"region_id":"DP03311r015","statement":[{"text":"Residues 61 and 63 bind Ca+2 ions according to the crystal structure (PDB: 1NLO).","type":"Curator statement"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a calcium ion (Ca2+).\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":64,"end":68,"reference_id":"14722079","reference_source":"pmid","reference_html":"Crystal structure of the calcium-stabilized human factor IX Gla domain bound to a conformation-specific anti-factor IX antibody. <i> Huang M, Furie BC, Furie B. </i> J Biol Chem, 2004","date":"2022-12-06T11:02:21.185Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_12","version":4,"cross_refs":[{"db":"PDB","id":"1NL0"}],"region_id":"DP03311r016","statement":[{"text":"Residues 66 and 67 bind Ca+2 ions according to the crystal structure (PDB: 1NLO).","type":"Curator statement"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a calcium ion (Ca2+).\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":64,"end":68,"reference_id":"14722079","reference_source":"pmid","reference_html":"Crystal structure of the calcium-stabilized human factor IX Gla domain bound to a conformation-specific anti-factor IX antibody. <i> Huang M, Furie BC, Furie B. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03311r017","statement":[{"text":"Residues 66 and 67 bind Ca+2 ions according to the crystal structure (PDB: 1NLO).","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-26T09:43:27.561Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":17,"released":"2021_06","sequence":"MQRVNMIMAESPGLITICLLGYLLSAECTVFLDHENANKILNRPKRYNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCPFGFEGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGRVSVSQTSKLTRAETVFPDVDYVNSTEAETILDNITQSTQSFNDFTRVVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRIIPHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFLKFGSGYVSGWGRVFHKGRSALVLQYLRVPLVDRATCLRSTKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000042504","uniref100":"UniRef100_P00740","uniref90":"UniRef90_P00740","uniref50":"UniRef50_P00740","genes":[{"name":{"value":"F9"}}],"alphafold_very_low_content":0.11279826464208242,"disorder_content":0.1019522776572668,"disprot_consensus":{"full":[{"start":47,"end":93,"type":"T"}],"Structural state":[{"start":47,"end":93,"type":"D"}],"Structural transition":[{"start":47,"end":93,"type":"T"}],"Molecular function":[{"start":47,"end":56,"type":"F"},{"start":60,"end":68,"type":"F"},{"start":70,"end":78,"type":"F"}]}},{"disprot_id":"DP03312","acc":"P10619","creator":"jssuarez","date":"2021-05-19T12:24:57.528Z","features":{"pfam":[{"id":"PF00450","name":"Serine carboxypeptidase","start":39,"end":476}],"gene3D":[]},"length":480,"name":"Lysosomal protective protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":288,"end":327,"reference_id":"24530914","reference_source":"pmid","reference_html":"Crystal structure of cathepsin A, a novel target for the treatment of cardiovascular diseases. <i> Schreuder HA, Liesum A, Kroll K, Böhnisch B, Buning C, Ruf S, Sadowski T. </i> Biochem Biophys Res Commun, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4CI9"}],"region_id":"DP03312r001","statement":[{"text":"Coming from the N-terminus, the electron density around Pro258–Ser259 becomes progressively more disordered, and from around Met299–Asp300 towards the C-terminus, the electron density gets clear again. Blobs of density in between suggest that more residues of the activation loop are still present but not clearly visible due to disorder. ","type":"Results"},{"text":"Residues 260 to 299 (unmodelled in the PDB structure) correspond to residues 288-327 of the Uniprot sequence.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-20T14:22:37.395Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_06","sequence":"MIRAAPPPLFLLLLLLLLLVSWASRGEAAPDQDEIQRLPGLAKQPSFRQYSGYLKGSGSKHLHYWFVESQKDPENSPVVLWLNGGPGCSSLDGLLTEHGPFLVQPDGVTLEYNPYSWNLIANVLYLESPAGVGFSYSDDKFYATNDTEVAQSNFEALQDFFRLFPEYKNNKLFLTGESYAGIYIPTLAVLVMQDPSMNLQGLAVGNGLSSYEQNDNSLVYFAYYHGLLGNRLWSSLQTHCCSQNKCNFYDNKDLECVTNLQEVARIVGNSGLNIYNLYAPCAGGVPSHFRYEKDTVVVQDLGNIFTRLPLKRMWHQALLRSGDKVRMDPPCTNTTAASTYLNNPYVRKALNIPEQLPQWDMCNFLVNLQYRRLYRSMNSQYLKLLSSQKYQILLYNGDVDMACNFMGDEWFVDSLNQKMEVQRRPWLVKYGDSGEQIAGFVKEFSHIAFLTIKGAGHMVPTDKPLAAFTMFSRFLNKQPY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI00000362E6","uniref100":"UniRef100_P10619","uniref90":"UniRef90_P10619","uniref50":"UniRef50_P10619","genes":[{"name":{"value":"CTSA"},"synonyms":[{"value":"PPGB"}]}],"alphafold_very_low_content":0.0125,"disorder_content":0.08333333333333333,"disprot_consensus":{"full":[{"start":288,"end":327,"type":"D"}],"Structural state":[{"start":288,"end":327,"type":"D"}]}},{"disprot_id":"DP03313","acc":"P00488","creator":"jssuarez","date":"2021-05-20T08:41:21.569Z","features":{"pfam":[{"id":"PF00868","name":"Transglutaminase family","start":58,"end":164},{"id":"PF00927","name":"Transglutaminase family, C-terminal ig like domain","start":519,"end":623},{"id":"PF00927","name":"Transglutaminase family, C-terminal ig like domain","start":631,"end":727},{"id":"PF01841","name":"Transglutaminase-like superfamily","start":311,"end":397}],"gene3D":[]},"length":732,"name":"Coagulation factor XIII A chain","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":2,"end":38,"reference_id":"20375315","reference_source":"pmid","reference_html":"Sensitive and selective detection of free FXIII activation peptide: a potential marker of acute thrombotic events. <i> Ortner E, Schroeder V, Walser R, Zerbe O, Kohler HP. </i> Blood, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03313r001","statement":[{"text":"The [15N,1H]-HSQC spectra of the AP-FXIII in water revealed the presence of too many peaks, and the extra peaks were attributed to the presence of cis conformers about the Pro-peptide bonds. The presence of these additional peaks already indicated that AP-FXIII in water was mainly unstructured.","type":"Results"},{"text":"To assess whether segments of the polypeptide chain are folded, a 15N{1H}-NOE experiment was recorded. Typically, amide nitrogen atoms of well-structured regions adopt values larger than 0.5, whereas for fully flexible regions the values are negative. In our experience secondary structure can only be reliably determined by NMR if the H-NOE in the corresponding segment is larger than 0.4. Values of the 15N{1H}-NOE of AP-FXIII are depicted in Figure 5 for both environments. Clearly, no values larger than 0.4 are encountered, and for many residues the heteronuclear NOE is close to 0.2, indicating that they are not fully flexible but that structure determination using NMR is not possible.","type":"Results"},{"text":"These experiments indicated a high conformational flexibility of the peptide in both water and plasma environments, precluding a more detailed structural characterization by NMR.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T08:06:06.196Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":2,"end":38,"reference_id":"20375315","reference_source":"pmid","reference_html":"Sensitive and selective detection of free FXIII activation peptide: a potential marker of acute thrombotic events. <i> Ortner E, Schroeder V, Walser R, Zerbe O, Kohler HP. </i> Blood, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1EVU"}],"region_id":"DP03313r002","statement":[{"text":"Recombinant AP-FXIII was largely flexible both in plasma and water, differing significantly from the rigid structure in the bound state. ","type":"Abstract"},{"text":"Finally, NMR analysis of 15N-labeled recombinant AP-FXIII in water and in plasma proved the peptide to be largely unstructured. ","type":"Introduction"},{"text":"The [15N,1H]-HSQC spectra of the AP-FXIII in water revealed the presence of too many peaks, and the extra peaks were attributed to the presence of cis conformers about the Pro-peptide bonds. The presence of these additional peaks already indicated that AP-FXIII in water was mainly unstructured.","type":"Results"},{"text":"To assess whether segments of the polypeptide chain are folded, a 15N{1H}-NOE experiment was recorded. Typically, amide nitrogen atoms of well-structured regions adopt values larger than 0.5, whereas for fully flexible regions the values are negative. In our experience secondary structure can only be reliably determined by NMR if the H-NOE in the corresponding segment is larger than 0.4. Values of the 15N{1H}-NOE of AP-FXIII are depicted in Figure 5 for both environments. Clearly, no values larger than 0.4 are encountered, and for many residues the heteronuclear NOE is close to 0.2, indicating that they are not fully flexible but that structure determination using NMR is not possible.","type":"Results"},{"text":"Coagulation factor XIII A chain activation peptide suffers a order to disorder transition upon cleavage. In the bound state, this activation peptide is structured as can be observed in PDB:1EVU","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T08:06:39.294Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":2,"end":38,"reference_id":"20375315","reference_source":"pmid","reference_html":"Sensitive and selective detection of free FXIII activation peptide: a potential marker of acute thrombotic events. <i> Ortner E, Schroeder V, Walser R, Zerbe O, Kohler HP. </i> Blood, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03313r003","statement":[{"text":"In addition circular dichroism spectra were recorded at physiologic pH 7.0 and the lower pH 5.5. The data indicate that neither α-helical nor β-strand type secondary structural elements become populated at the greater pH value, although slightly more polyproline-type absorption at 208 nm occurs at the greater pH value (data not shown).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T08:05:51.031Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2021_12","sequence":"MSETSRTAFGGRRAVPPNNSNAAEDDLPTVELQGVVPRGVNLQEFLNVTSVHLFKERWDTNKVDHHTDKYENNKLIVRRGQSFYVQIDFSRPYDPRRDLFRVEYVIGRYPQENKGTYIPVPIVSELQSGKWGAKIVMREDRSVRLSIQSSPKCIVGKFRMYVAVWTPYGVLRTSRNPETDTYILFNPWCEDDAVYLDNEKEREEYVLNDIGVIFYGEVNDIKTRSWSYGQFEDGILDTCLYVMDRAQMDLSGRGNPIKVSRVGSAMVNAKDDEGVLVGSWDNIYAYGVPPSAWTGSVDILLEYRSSENPVRYGQCWVFAGVFNTFLRCLGIPARIVTNYFSAHDNDANLQMDIFLEEDGNVNSKLTKDSVWNYHCWNEAWMTRPDLPVGFGGWQAVDSTPQENSDGMYRCGPASVQAIKHGHVCFQFDAPFVFAEVNSDLIYITAKKDGTHVVENVDATHIGKLIVTKQIGGDGMMDITDTYKFQEGQEEERLALETALMYGAKKPLNTEGVMKSRSNVDMDFEVENAVLGKDFKLSITFRNNSHNRYTITAYLSANITFYTGVPKAEFKKETFDVTLEPLSFKKEAVLIQAGEYMGQLLEQASLHFFVTARINETRDVLAKQKSTVLTIPEIIIKVRGTQVVGSDMTVTVEFTNPLKETLRNVWVHLDGPGVTRPMKKMFREIRPNSTVQWEEVCRPWVSGHRKLIASMSSDSLRHVYGELDVQIQRRPSM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000142757","uniref100":"UniRef100_P00488","uniref90":"UniRef90_P00488","uniref50":"UniRef50_P00488","genes":[{"name":{"value":"F13A1"},"synonyms":[{"value":"F13A"}]}],"alphafold_very_low_content":0.00819672131147541,"disorder_content":0.050546448087431695,"disprot_consensus":{"full":[{"start":2,"end":38,"type":"T"}],"Structural state":[{"start":2,"end":38,"type":"D"}],"Structural transition":[{"start":2,"end":38,"type":"T"}]}},{"disprot_id":"DP03314","acc":"Q06141","creator":"jmarchetti","date":"2021-05-20T12:27:40.242Z","features":{"pfam":[{"id":"PF00059","name":"Lectin C-type domain","start":58,"end":173}],"gene3D":[]},"length":175,"name":"Regenerating islet-derived protein 3-alpha","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":27,"end":36,"reference_id":"10417404","reference_source":"pmid","reference_html":"Crystallization and preliminary crystallographic study of HIP/PAP, a human C-lectin overexpressed in primary liver cancers. <i> Abergel C, Chenivesse S, Stinnakre MG, Guasco S, Bréchot C, Claverie JM, Devinoy E, Christa L. </i> Acta Crystallogr D Biol Crystallogr, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1UV0"}],"region_id":"DP03314r001","statement":[{"text":"The reference is to the structure obtained by X-ray crystallography. In the paper there is no mention to missing electron density but It can be found in the structure","type":"Curator statement"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-14T14:55:13.353Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":27,"end":36,"reference_id":"19095652","reference_source":"pmid","reference_html":"Regulation of C-type lectin antimicrobial activity by a flexible N-terminal prosegment. <i> Mukherjee S, Partch CL, Lehotzky RE, Whitham CV, Chu H, Bevins CL, Gardner KH, Hooper LV. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":4,"region_id":"DP03314r002","statement":[{"text":"The disordered N-terminal 10 amino acids are indicated by a dotted line , and the locations of the N-terminal disulfide bond( red )and the trypsin cleavage site are indicated.","type":"Figure"},{"text":"The position number 10 from the structure (cited in the paper 1UV0) corresponds to position number 36 from UniProt sequence. The statement from the paper claims that the first 10 residues are disordered and actually are 9 residues. ","type":"Curator statement"},{"text":"In particular, N-terminal residues 27–35 are disordered and thus absent from the structure (Fig. 5 A ) and residues 36–41 appear to be involved in crystal packing interactions, raising questions about the observed structure of this essential region of the protein.","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-16T07:46:10.134Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":27,"end":37,"reference_id":"19095652","reference_source":"pmid","reference_html":"Regulation of C-type lectin antimicrobial activity by a flexible N-terminal prosegment. <i> Mukherjee S, Partch CL, Lehotzky RE, Whitham CV, Chu H, Bevins CL, Gardner KH, Hooper LV. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000059","term_name":"self-inhibition","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03314r003","statement":[{"text":"These data demonstrate that removal of the N-terminal prosegment by trypsin enhances RegIII\u0001and HIP/PAP antibacterial activity. ","type":"Results"},{"text":"Collectively, these data establish that the RegIII lectin N-terminal prosegment inhibits antibacterial activity in cis, but does not affect peptidoglycan binding.","type":"Results"},{"text":"Overall, these results suggested a model in which the prosegment maintains HIP/PAP in an inactive state through transient interactions between acidic N-terminal residues and basic residues positioned C-terminal to the trypsin site. ","type":"Results"},{"text":" The inhibitory activity of the N-terminal segment depends on charge-charge interactions with the main body of the protein. Derepression of antibacterial activity occurs when these interactions are perturbed, either through proteolytic removal of the prosegment or by mutation of the charged residues ","type":"Discussion"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-01T15:33:15.531Z"},"ec_go":"IDA","disprot_namespace":"Disorder function"},{"start":27,"end":37,"reference_id":"19095652","reference_source":"pmid","reference_html":"Regulation of C-type lectin antimicrobial activity by a flexible N-terminal prosegment. <i> Mukherjee S, Partch CL, Lehotzky RE, Whitham CV, Chu H, Bevins CL, Gardner KH, Hooper LV. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP03314r005","statement":[{"text":"This indicates a high degree of backbone conformational mobility at the N terminus. Furthermore, TALOS analyses of backbone chemical shifts (17) and 1H-1H NOEs indicated that the prosegment adopts an extended structure.","type":"Results"},{"text":"The results corresponds to the prosegment specifically for the region comprising residue 27 to residue 37","type":"Curator statement"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-15T08:13:32.041Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":27,"end":37,"reference_id":"19095652","reference_source":"pmid","reference_html":"Regulation of C-type lectin antimicrobial activity by a flexible N-terminal prosegment. <i> Mukherjee S, Partch CL, Lehotzky RE, Whitham CV, Chu H, Bevins CL, Gardner KH, Hooper LV. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000059","term_name":"self-inhibition","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03314r006","statement":[{"text":"Together, these data suggest that the prosegment is flexible and transiently interacts with the rest of the protein.","type":"Results"},{"text":"The results corresponds to the prosegment specifically for the region comprising residue 27 to residue 37.","type":"Curator statement"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-15T08:13:37.404Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":6,"released":"2021_06","sequence":"MLPPMALPSVSWMLLSCLMLLSQVQGEEPQRELPSARIRCPKGSKAYGSHCYALFLSPKSWTDADLACQKRPSGNLVSVLSGAEGSFVSSLVKSIGNSYSYVWIGLHDPTQGTEPNGEGWEWSSSDVMNYFAWERNPSTISSPGHCASLSRSTAFLRWKDYNCNVRLPYVCKFTD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000001C5B","uniref100":"UniRef100_Q06141","uniref90":"UniRef90_Q06141","uniref50":"UniRef50_P25031","genes":[{"name":{"value":"REG3A"},"synonyms":[{"value":"HIP"},{"value":"PAP"},{"value":"PAP1"}]}],"alphafold_very_low_content":0.022857142857142857,"disorder_content":0.06285714285714286,"disprot_consensus":{"full":[{"start":27,"end":37,"type":"D"}],"Structural state":[{"start":27,"end":37,"type":"D"}],"Disorder function":[{"start":27,"end":37,"type":"F"}]}},{"disprot_id":"DP03315","acc":"P0ADC1","creator":"jnilsson","date":"2021-05-20T12:31:53.781Z","features":{"pfam":[{"id":"PF04390","name":"Lipopolysaccharide-assembly","start":40,"end":159}],"gene3D":[]},"length":193,"name":"LPS-assembly lipoprotein LptE","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":20,"end":32,"reference_id":"24938785","reference_source":"pmid","reference_html":"LptE binds to and alters the physical state of LPS to catalyze its assembly at the cell surface. <i> Malojčić G, Andres D, Grabowicz M, George AH, Ruiz N, Silhavy TJ, Kahne D. </i> Proc Natl Acad Sci U S A, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4NHR"}],"region_id":"DP03315r001","statement":[{"text":"The electron density for the first 15 N-terminal residues and the final 18 C-terminal residues of mature LptE are missing. It is possible that the N terminus of LptE is flexible to allow it to be connected to its membrane anchor at the N terminus, while forming a plug within the lumen of the β-barrel of LptD (11, 15).","type":"Results"},{"text":"The IDR characterized in the publication and spanning residues the N-terminal corresponds to region 20-32 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-18) that is cleaved in the mature secreted protein. ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-25T08:13:15.639Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":170,"end":182,"reference_id":"24938785","reference_source":"pmid","reference_html":"LptE binds to and alters the physical state of LPS to catalyze its assembly at the cell surface. <i> Malojčić G, Andres D, Grabowicz M, George AH, Ruiz N, Silhavy TJ, Kahne D. </i> Proc Natl Acad Sci U S A, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4NHR"}],"region_id":"DP03315r002","statement":[{"text":"The electron density for the first 15 N-terminal residues and the final 18 C-terminal residues of mature LptE are missing. It is possible that the N terminus of LptE is flexible to allow it to be connected to its membrane anchor at the N terminus, while forming a plug within the lumen of the β-barrel of LptD (11, 15). The disordered C-terminal portion of LptE is consistent with the observation that it is readily cleaved by limited proteolysis of the LptDE complex (11). In any event, genetic studies have established\nthat this construct is functional (20).","type":"Results"},{"text":"The IDR characterized in the publication and spanning residues the C-terminal corresponds to region 170-182 of the amino acid sequence, since the natural precursor form of the protein contains a signal peptide (1-18) that is cleaved in the mature secreted protein. ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-25T08:13:22.159Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MRYLATLLLSLAVLITAGCGWHLRDTTQVPSTMKVMILDSGDPNGPLSRAVRNQLRLNGVELLDKETTRKDVPSLRLGKVSIAKDTASVFRNGQTAEYQMIMTVNATVLIPGRDIYPISAKVFRSFFDNPQMALAKDNEQDMIVKEMYDRAAEQLIRKLPSIRAADIRSDEEQTSTTTDTPATPARVSTTLGN","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":[],"UniParc":"UPI0000134285","uniref100":"UniRef100_A7ZJ30","uniref90":"UniRef90_Q8XBN9","uniref50":"UniRef50_Q8ZQZ7","genes":[{"name":{"value":"lptE","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01186","url":"https://hamap.expasy.org/unirule/MF_01186"}}]},"synonyms":[{"value":"rlpB"}],"olnNames":[{"value":"b0641"},{"value":"JW0636"}]}],"alphafold_very_low_content":0.05181347150259067,"disorder_content":0.13471502590673576,"disprot_consensus":{"full":[{"start":20,"end":32,"type":"D"},{"start":170,"end":182,"type":"D"}],"Structural state":[{"start":20,"end":32,"type":"D"},{"start":170,"end":182,"type":"D"}]}},{"disprot_id":"DP03316","acc":"P06149","creator":"jnilsson","date":"2021-05-20T14:33:41.615Z","features":{"pfam":[{"id":"PF01565","name":"FAD binding domain","start":47,"end":166},{"id":"PF09330","name":"D-lactate dehydrogenase, membrane binding","start":278,"end":567}],"gene3D":[]},"length":571,"name":"Quinone-dependent D-lactate dehydrogenase","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":320,"end":376,"reference_id":"10944213","reference_source":"pmid","reference_html":"The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme. <i> Dym O, Pratt EA, Ho C, Eisenberg D. </i> Proc Natl Acad Sci U S A, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1F0X"}],"region_id":"DP03316r001","statement":[{"text":"During model building, it became clear that a '50 residue portion of the D-LDH structure is disordered. The disordered region exhibits electron density that is discontinuous and untraceable in both the original multiple-wavelength anomalous diffraction electron density map and the final refined maps. ","type":"Methods"},{"text":"Overall Structure. The D-LDH structure is composed of three discontinuous domains: the FAD-binding domain (residues 1–268 and 520–571), the cap domain (residues 269–310, 388–425, and 450–519), and the membrane-binding domain (residues 311–387 and 426–449, of which residues 329–376 are in the disordered region) (Fig. 1).","type":"Results"},{"text":"We propose a model for the association of D-LDH to the membrane. We note that there are nine other positive residues (Lys-331, Lys-336, Lys-344, Arg-346, Lys-353, Lys-355, Arg-358, Arg-364, and Lys-368) in the membrane-binding domain but not modeled in the discontinuous density map. These are shown as yellow balls in Fig. 4. A possible explanation for this disordered segment may be the absence of detergent or lipid in the\ncrystallization solution. That is, this region may not have a defined structure until it binds the membrane, or it may have a defined structure but with several orientations with respect to the rest of the molecule. Therefore, we propose that positive residues, both from the observed structure and possibly from the missing segment, facilitate the interaction of D-LDH with the negatively charged phosphate groups of the phospholipid membrane.","type":"Discussion"},{"text":"Another mechanism proposed for association of peripheral membrane proteins with the membrane is through a mixture of hydrophobic and electrostatic interactions (4, 5). The membrane-binding domain of D-LDH contains 16 apolar residues, nine in the observed structure and seven in the disordered region. Notably, all of the nine residues in the observed structure are distributed on a surface close to the cap domain and away\nfrom the membrane-binding surface.","type":"Discussion"},{"text":"Fig. 1. Ribbon representation of the D-LDH molecule complexed with FAD. The three domains are: in cyan, the FAD-binding domain; in purple, the cap\ndomain; and in blue, the membrane-binding domain. The 50 missing residues\nfrom the membrane-binding domain lie between Met-328 and Ser-375.","type":"Figure"},{"text":"A putative model of the 50 missing residues (329–374) (yellow segment in Fig. 4), was built to attach both ends to the structure (residues 328 to 329 and 374 to 375) (blue segment in Fig. 4). This model seems reasonable, given that the solvent content of the crystal is small (30%), which results in tight crystal packing of symmetry-related molecules, especially in the vicinity of the missing residues, constraining the model of this segment.","type":"Discussion"},{"text":"Fig. 4. Cartoon of D-LDH associating with the membrane. D-LDH is anchored to the membrane by electrostatic interactions between basic residues (blue balls) from the observed membrane-binding domain\n(blue) and possibly from the modeled missing segment (dashed yellow) comprising nine basic residues (yellow balls) and the negatively charged phospholipid head groups (red balls) of the membrane. ","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-20T16:26:53.065Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MSSMTTTDNKAFLNELARLVGSSHLLTDPAKTARYRKGFRSGQGDALAVVFPGSLLELWRVLKACVTADKIILMQAANTGLTEGSTPNGNDYDRDVVIISTLRLDKLHVLGKGEQVLAYPGTTLYSLEKALKPLGREPHSVIGSSCIGASVIGGICNNSGGSLVQRGPAYTEMSLFARINEDGKLTLVNHLGIDLGETPEQILSKLDDDRIKDDDVRHDGRHAHDYDYVHRVRDIEADTPARYNADPDRLFESSGCAGKLAVFAVRLDTFEAEKNQQVFYIGTNQPEVLTEIRRHILANFENLPVAGEYMHRDIYDIAEKYGKDTFLMIDKLGTDKMPFFFNLKGRTDAMLEKVKFFRPHFTDRAMQKFGHLFPSHLPPRMKNWRDKYEHHLLLKMAGDGVGEAKSWLVDYFKQAEGDFFVCTPEEGSKAFLHRFAAAGAAIRYQAVHSDEVEDILALDIALRRNDTEWYEHLPPEIDSQLVHKLYYGHFMCYVFHQDYIVKKGVDVHALKEQMLELLQQRGAQYPAEHNVGHLYKAPETLQKFYRENDPTNSMNPGIGKTSKRKNWQEVE","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":[],"UniParc":"UPI00001114B6","uniref100":"UniRef100_P06149","uniref90":"UniRef90_P06149","uniref50":"UniRef50_P06149","genes":[{"name":{"value":"dld","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_02092","url":"https://hamap.expasy.org/unirule/MF_02092"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"6386470","url":"http://www.ncbi.nlm.nih.gov/pubmed/6386470","alternativeUrl":"https://europepmc.org/abstract/MED/6386470"}}]},"olnNames":[{"value":"b2133"},{"value":"JW2121"}]}],"alphafold_very_low_content":0.0070052539404553416,"disorder_content":0.09982486865148861,"disprot_consensus":{"full":[{"start":320,"end":376,"type":"D"}],"Structural state":[{"start":320,"end":376,"type":"D"}]}},{"disprot_id":"DP03317","acc":"O16299","creator":"spenadias","date":"2021-05-20T15:11:31.991Z","features":{"pfam":[{"id":"PF00004","name":"ATPase family associated with various cellular activities (AAA)","start":352,"end":481},{"id":"PF09336","name":"Vps4 C terminal oligomerisation domain","start":552,"end":585},{"id":"PF17862","name":"AAA+ lid domain","start":507,"end":549}],"gene3D":[]},"length":594,"name":"Fidgetin-like protein 1","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":261,"end":285,"reference_id":"23979136","reference_source":"pmid","reference_html":"Structural insights into the unusually strong ATPase activity of the AAA domain of the Caenorhabditis elegans fidgetin-like 1 (FIGL-1) protein. <i> Peng W, Lin Z, Li W, Lu J, Shen Y, Wang C. </i> J Biol Chem, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4L16"},{"db":"PDB","id":"4L15"}],"region_id":"DP03317r001","statement":[{"text":"Residues that are not visible in the crystal structure are indicated with dashed lines","type":"Figure"},{"text":"Dashed line corresponds to the region comprised from residue 261 to residue 285","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-01T11:32:28.600Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_06","sequence":"MYSPKRVKLNVTSGMRKRPETGENNDDLYPPTALARNGISPYFIGKPRRKIVVETPSDSAQQQPPFKSRSQQNGLDDELDGIIIDEDEDRTVDVSFSQKQDTRKLKSRPFLGEKSSFKLGEIPKPKEEKRREEPFTMRGFDFGSDDKVTKIRDKICDIVDPTNARRTDPNFIRQMHENTLKGIEVASNPHFKKTRAPTKNRAAIQNTLGTLYPSFTTAAGQDPQNSKFQVPLDRQSSSQSIGSLAGIPPARRAPDIPKRCSNPLIRKAMGMDTEGGGKDEKMSGLRAEPTLKHFDENIISLIESEIMSVNNEIGWADVAGLEGAKKALREIVVLPFKRPDVFTGIRAPPKGVLLFGPPGTGKTMIGRCVASQCKATFFNISASSLTSKWVGEGEKLVRALFSVARLKLPSVIFIDEIDSLLSSRSESEHESSRRIKTEFLVQLDGVNTAPDERLLVLGATNRPQELDEAARRRFQKRLYIALPEPESRTQIVQNLLVGTRHDITNHNLERIRELTDGYSGADMRQLCTEAAMGPIRDIGDDIETIDKDDIRAVTVMDFAEAARVVRPTVDDSQLDAYAAWDKKFGCLPPPSISR","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"dataset":[],"UniParc":"UPI0000074E0E","uniref100":"UniRef100_O16299","uniref90":"UniRef90_O16299","uniref50":"UniRef50_O16299","genes":[{"name":{"value":"figl-1"},"orfNames":[{"value":"F32D1.1"}]}],"alphafold_very_low_content":0.3787878787878788,"disorder_content":0.04208754208754209,"disprot_consensus":{"full":[{"start":261,"end":285,"type":"D"}],"Structural state":[{"start":261,"end":285,"type":"D"}]}},{"disprot_id":"DP03318","acc":"Q95ZK7","creator":"spenadias","date":"2021-05-21T11:55:43.159Z","features":{"pfam":[{"id":"PF17905","name":"GLD-3 4th KH domain (aka KH5)","start":342,"end":421},{"id":"PF21482","name":"GLD-3 2nd KH domain (aka KH3)","start":188,"end":253},{"id":"PF22467","name":"GLD-3 3rd KH domain (aka KH4)","start":270,"end":341},{"id":"PF22801","name":"GLD-3 1st KH domain (aka KH2)","start":111,"end":185}],"gene3D":[]},"length":969,"name":"Defective in germ line development protein 3","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":260,"end":269,"reference_id":"20823118","reference_source":"pmid","reference_html":"Four KH domains of the C. elegans Bicaudal-C ortholog GLD-3 form a globular structural platform. <i> Nakel K, Hartung SA, Bonneau F, Eckmann CR, Conti E. </i> RNA, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3N89"}],"region_id":"DP03318r001","statement":[{"text":"The linkers connecting the head-to-toe dimers consist of a single amino-acid residue (Cys 188 for KH2–KH3 and Leu 343 for KH4–KH5, while the side-by-side positioning of the consecutive KH3–KH4 domains is mediated by a 10-residue-long linker (residues 260–269) that is disordered in the structure.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":260,"end":269,"reference_id":"20823118","reference_source":"pmid","reference_html":"Four KH domains of the C. elegans Bicaudal-C ortholog GLD-3 form a globular structural platform. <i> Nakel K, Hartung SA, Bonneau F, Eckmann CR, Conti E. </i> RNA, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"3N89"}],"region_id":"DP03318r002","statement":[{"text":"Results: The linkers connecting the head-to-toe dimers consist of a single amino-acid residue (Cys 188 for KH2–KH3 and Leu 343 for KH4–KH5, while the side-by-side positioning of the consecutive KH3–KH4 domains is mediated by a 10-residue-long linker (residues 260–269) that is disordered in the structure.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":2,"released":"2021_12","sequence":"MGEQSHEKDHDEAHSYNPFVRSAVEYDADTRLQMAENAASARKLFVSSALKDIIVNPENFYHDFQQSAQMAEDANQRRQVSYNTKREAHIHQLKAQGLPLPSNIPMIEINPTRVTLNMEFESQYYSLMTSDNGDHENVASIMAETNTLIQLPDRSVGGTTPDPFAQQVTITGYFGDVDRARMLMRRNCHFTVFMALSKMKMPLHELQAHVRQNPIQNVEMSFVDAPEKNGIVTTYLRITAREKNQHELIEAAKRLNEILFRESPAPENNFTLHFTLSTYYVDQVLGSSSTAQLMPVIERETTTIISYPCYNNRNETRGNIYEIKVVGNIDNVLKARRYIMDLLPISMCFNIKNTDMAEPSRVSDRNIHMIIDESGIILKMTPSVYEPADLLSGEVPLNCASLRSKEFNIKKLYTAYQKVLSKKFDFIAPQPNDYDNSIWHHSLPANFLKNFNMPCRGELSDGSNGRRHRSSSIASSRSKHSYMSKGKQFSESSGGPSRSHTRVSSFSENSSTVPIMQFPTPHFAPPMLTPHHHMLKYVYLQQHQQAQTFLKGAAGLHPGTHIMFPPPIIVDGSFVSALPFADPVVFDGFPYVHGLFPVNEAEQHRNHRESSPSLRSTQEIRKPSRNMGNRPSSSTGSYYPSTTPRQRVYEQVREDDLRSHIGSRRTSVNGDDQNVESMHDQGYERQYPRQHQRLQKDDQQRWKTGSRGDIHSSRTINVHRDVRNSNEYDFHVGNSGPAKRSPSLEQVQLQMTHHLKLKSNDVDLDHEKLYMHESPHNDSDTTVSASGFGNDLMDGDFVQRFLSNANINESGRRPRTVSCFTEKDGQSARYIDSDGAYSVVDHASTHQSRSYDSFRKVGDNGVTKTILEPRARVEKDYGKISLEHKTKYSNEYGDEEKSAENDTSSLGSRQYRIDPMKLIASVRESSEQLPRIHERQFSDVLNEKEKEIADKSIESTVTQDLSLDETSTY","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"dataset":[],"UniParc":"UPI000007C575","uniref100":"UniRef100_Q95ZK7","uniref90":"UniRef90_Q95ZK7","uniref50":"UniRef50_Q95ZK7","genes":[{"name":{"value":"gld-3","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"T07F8.3a","url":"https://www.wormbase.org/db/seq/sequence?name=T07F8.3a;class=Transcript"}}]},"orfNames":[{"value":"T07F8.3"}]}],"alphafold_very_low_content":0.5118679050567595,"disorder_content":0.010319917440660475,"disprot_consensus":{"full":[{"start":260,"end":269,"type":"D"}],"Structural state":[{"start":260,"end":269,"type":"D"}],"Disorder function":[{"start":260,"end":269,"type":"F"}]}},{"disprot_id":"DP03319","acc":"O17087","creator":"spenadias","date":"2021-05-21T12:01:06.398Z","features":{"pfam":[{"id":"PF03828","name":"Cid1 family poly A polymerase","start":780,"end":815},{"id":"PF22600","name":"Poly(A) RNA polymerase, mitochondrial-like, central palm domain","start":549,"end":687}],"gene3D":[]},"length":1113,"name":"Poly(A) RNA polymerase gld-2","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":815,"end":860,"reference_id":"27288313","reference_source":"pmid","reference_html":"Structural basis for the antagonistic roles of RNP-8 and GLD-3 in GLD-2 poly(A)-polymerase activity. <i> Nakel K, Bonneau F, Basquin C, Habermann B, Eckmann CR, Conti E. </i> RNA, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5JNB"}],"region_id":"DP03319r001","statement":[{"text":"The final model includes residues 544–922 of GLD-2 (with the exception of missing or disordered residues between 815–860 and 879–882) and residues 177–222 of RNP-8.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":813,"end":846,"reference_id":"26124149","reference_source":"pmid","reference_html":"Structural basis for the activation of the C. elegans noncanonical cytoplasmic poly(A)-polymerase GLD-2 by GLD-3. <i> Nakel K, Bonneau F, Eckmann CR, Conti E. </i> Proc Natl Acad Sci U S A, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4ZRL"}],"region_id":"DP03319r002","statement":[{"text":"The final model includes residues 546–923 of GLD-2ΔI (with the exception of disordered loops between residues 766 and 773, 804 and 812, 847 and 854, and 876 and 881), residues 25–88 of GLD-3NT, and a chloride ion","type":"Results"},{"text":"Disordered regions are shown with dotted lines. The region deleted for crystallization (residues 813–846) resides in the disordered loop region between α-helices 7 and 8. ","type":"Figure"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MVMAQQQKNAERNDEHTRRNRSPSVDSVSRVQQQSGGFAFYNQQSNHQYQQSHPRRTSFSRDGNTGYYNNHSGNKRQTYNNQRGGRSYNHRGNSNYQQNGEYSGNQGCVPKYHQRNQNYPQLQPKYSYFQPHQRPIFNSTQGYGTYSVRRSSPPSPSALSSSTANSTSNRAPTQPPILLRHAEPASDKNHQGSDHEQNHDPKIHLYRSAGTAPGGYTQCPSPYKQPPPQPPSTPSSSDKRIEQQQAEDWPTRFQHPPPQFRRGQDPMPASIELQHKTANQTMPVDIVQTNQQKTVSSYERAAQFRASASELPTDSVDAKHPCFANERMQSALIGISPQLKTQQQSPGIPIQNEAEASAVMKAMRSFQFHNWPQMSHGSYYPMPYHLENQMRPMKSGDQLPLNQQNHNLSGFPAFVGKSSLVGSSLNTRNSSEADPEEMPRIMEKLDDEVTGADHDKTIDENRRRIHKSQEPRIGTEEKALNELPRKANRRNSSCSSISSVSESSSPSALDESTLTKILPTDNFRGGRGFASPSPPTSLLSEPLSRMDVLSEKIWDYHNKVSQTDEMLQRKLHLRDMLYTAISPVFPLSGLYVVGSSLNGFGNNSSDMDLCLMITNKDLDQKNDAVVVLNLILSTLQYEKFVESQKLILAKVPILRINFAAPFDDITVDLNANNSVAIRNTHLLCYYSSYDWRVRPLVSVVKEWAKRKGINDANKSSFTSYSLVLMVIHFLQCGPTKVLPNLQQSYPNRFSNKVDVRTLNVTMALEEVADDIDQSLSEKTTLGELLIGFLDYYANEFNYDRDAISIRQGRRVERAALAVRPKIHSNSEGDKETPPPSSSASTSSIHNGGTPGIPMHHSISNPHFWRSQWRCVCIEEPFTNSNTAHSIYDEMVFEAIKKAFREAHGELQHNHDLDKLMECEPIKASTTNTGAAVFAATYEGERPLAQQPNTIACASLRVLNSIPVSSGPGHYHYQQQSNQNLSRPQRPGSNQGYQMNNNRGFNGNNQQQHQNRRSFNNQSSSNPGNGSTGPRSSRSNENVRDSSRQQNSQKGSSGVSVSKENVASTTGVPVDKKQQNSNRKDDGNRTKRSPMVQSPEPAKTKSEKTPMASSNVSQ","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"dataset":[],"UniParc":"UPI0000083E0B","uniref100":"UniRef100_O17087","uniref90":"UniRef90_O17087","uniref50":"UniRef50_O17087","genes":[{"name":{"value":"gld-2"},"orfNames":[{"value":"ZC308.1"}]}],"alphafold_very_low_content":0.6594788858939802,"disorder_content":0.0431266846361186,"disprot_consensus":{"full":[{"start":813,"end":860,"type":"D"}],"Structural state":[{"start":813,"end":860,"type":"D"}]}},{"disprot_id":"DP03320","acc":"P46580","creator":"spenadias","date":"2021-05-21T12:14:18.557Z","features":{"pfam":[{"id":"PF05185","name":"PRMT5 arginine-N-methyltransferase","start":354,"end":528},{"id":"PF17285","name":"PRMT5 TIM barrel domain","start":78,"end":334},{"id":"PF17286","name":"PRMT5 oligomerisation domain","start":531,"end":732}],"gene3D":[]},"length":734,"name":"Protein arginine N-methyltransferase 5","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":359,"end":380,"reference_id":"22143770","reference_source":"pmid","reference_html":"Structural insights into protein arginine symmetric dimethylation by PRMT5. <i> Sun L, Wang M, Lv Z, Yang N, Liu Y, Bao S, Gong W, Xu RM. </i> Proc Natl Acad Sci U S A, 2011","date":"2026-03-13T15:37:43.886Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"cross_refs":[{"db":"PDB","id":"3UA4"},{"db":"PDB","id":"3UA3"}],"region_id":"DP03320r001","statement":[{"text":"In particular, a segment including a N-terminal loop (L0) and a following helix (αA) (a.a. 359–380) became ordered upon SAH binding. Helix αA is positioned similar to that found in type-I enzymes, sheltering SAH from exposing to the solvent and creating a secluded catalytic active site. However, key residues responsible for the disordered-to-ordered conformational transition upon SAH/SAM binding are separately conserved among PRMT5 family members (Fig. 1B).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16680","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":"17754"}]},{"start":331,"end":380,"reference_id":"22143770","reference_source":"pmid","reference_html":"Structural insights into protein arginine symmetric dimethylation by PRMT5. <i> Sun L, Wang M, Lv Z, Yang N, Liu Y, Bao S, Gong W, Xu RM. </i> Proc Natl Acad Sci U S A, 2011","date":"2026-03-13T14:57:35.345Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"3UA4"}],"region_id":"DP03320r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":null}],"statement":[{"text":"The structure of the SAH-bound PRMT5 differs from that of free protein in that a N-terminal loop (L0) and helix (αA) are ordered in the SAH-bound structure.","type":"Results"},{"text":"The free PRMT5 structure shows this region, corresponding to the L0 and αA, is missing electron density.","type":"Curator statement"}]},{"start":1,"end":44,"reference_id":"22143770","reference_source":"pmid","reference_html":"Structural insights into protein arginine symmetric dimethylation by PRMT5. <i> Sun L, Wang M, Lv Z, Yang N, Liu Y, Bao S, Gong W, Xu RM. </i> Proc Natl Acad Sci U S A, 2011","date":"2026-03-13T15:08:36.745Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"3UA4"},{"db":"PDB","id":"3UA3"}],"region_id":"DP03320r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":null}],"statement":[{"text":"This region lacks electron density in both the SAH-bound and free form of PRMT5, indicating it is disordered.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":1,"end":44,"reference_id":"22143770","reference_source":"pmid","reference_html":"Structural insights into protein arginine symmetric dimethylation by PRMT5. <i> Sun L, Wang M, Lv Z, Yang N, Liu Y, Bao S, Gong W, Xu RM. </i> Proc Natl Acad Sci U S A, 2011","date":"2026-03-13T15:01:07.322Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"3UA4"}],"region_id":"DP03320r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":null}],"statement":[{"text":"This region lacks electron density, indicating it is disordered.","type":"Results"}]},{"start":331,"end":358,"reference_id":"22143770","reference_source":"pmid","reference_html":"Structural insights into protein arginine symmetric dimethylation by PRMT5. <i> Sun L, Wang M, Lv Z, Yang N, Liu Y, Bao S, Gong W, Xu RM. </i> Proc Natl Acad Sci U S A, 2011","date":"2026-03-13T15:08:08.478Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"3UA4"},{"db":"PDB","id":"3UA3"}],"region_id":"DP03320r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":null}],"statement":[{"text":"This region, between the Tim barrel and the methyltransferase domain,  lacks electron density in both the SAH-bound and free form of PRMT5, indicating it is disordered linker.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":366,"end":371,"reference_id":"22143770","reference_source":"pmid","reference_html":"Structural insights into protein arginine symmetric dimethylation by PRMT5. <i> Sun L, Wang M, Lv Z, Yang N, Liu Y, Bao S, Gong W, Xu RM. </i> Proc Natl Acad Sci U S A, 2011","date":"2026-03-13T15:25:16.725Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1904047","term_name":"S-adenosyl-L-methionine binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"3UA3"}],"ec_go":"EXP","region_id":"DP03320r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16680","entry_name":null}],"statement":[{"text":"This PRMT5 loop has two apparent functions, (i) contact the SAH/SAM molecule via residues conserved in PRMT5 proteins (Pro366, Leu367, and Leu371) and forms a solvent inaccessible area for catalysis; (ii) the N-terminal end of L0 makes a U-turn and contacts the dimerization domain, which stabilizes the loop in a conformation endowed with the ability to influence substrate binding (Figs. 3 A and B). Hence, the highly conserved PRMT5 loop is important for SAH/SAM binding, as well as in a position to regulate substrate binding.","type":"Results"}],"term_comment":"","term_def":"\"Binding to S-adenosyl-L-methionine.\" [GO_REF:0000067, GOC:BHF, GOC:hal, GOC:TermGenie, PMID:22985361]","term_is_obsolete":false,"term_not_annotate":false},{"start":375,"end":380,"reference_id":"22143770","reference_source":"pmid","reference_html":"Structural insights into protein arginine symmetric dimethylation by PRMT5. <i> Sun L, Wang M, Lv Z, Yang N, Liu Y, Bao S, Gong W, Xu RM. </i> Proc Natl Acad Sci U S A, 2011","date":"2026-03-13T16:01:18.092Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0016274","term_name":"protein-arginine N-methyltransferase activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001247","ec_ontology":"ECO","ec_name":"point mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe379Met","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe379Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe379Gly","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP03320r008","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62784"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"194378","entry_name":null}],"statement":[{"text":"Interestingly, changing Phe379 to a methionine (F379M) resulted in a more active enzyme, while an F279Y mutant is inactive, and mutations to an alanine or a glycine pronouncedly reduced the enzymatic activity (Fig. 3C).","type":"Results"},{"text":"These observation imply that: (i) symmetric and asymmetric dimethylation of arginine shares a common catalytic mechanism, as the same active site is involved; (ii) Phe379 occupies a key position for PRMT5’s sDMA product specificity.","type":"Results"},{"text":"Phe379 is important for protein-arginine N-methyltransferase activity, as substitutions at this position alter both the level and specificity of enzymatic activity.","type":"Curator statement"}],"term_comment":"","term_def":"\"Catalysis of the reaction: S-adenosyl-L-methionine + (protein)-arginine = S-adenosyl-L-homocysteine + (protein)-N-methyl-arginine.\" [GOC:mah, PMID:12351636, PMID:31284549]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"}],"regions_counter":8,"released":"2023_12","sequence":"MSNRTYADNLFPQQVAEQHEEQMSSGSSPKSNSPSRSISSVEAANSRIHIGWMATTLDVAENLDRHVATFCTRLGEFKYNFVVYPIGGVVRAFWTPNGSAENHPPVIDLPDVQLRNDLWESYVVGKISPWIDCDSSDPAFASLSEEHLLKELSYICYLGLQTMAIELTRISSPRTAAILKKWIWTRNSRFTVWVQLPSAIEKCKDYDAFTIEHVDLWTIWADFRKNCGNFSGVYFQVALTISSELPDELTELKLVDRWKAEPLAAFVIESGLFISGRNGEASIPSAHINLLKHLWTTDALRIVLRATTDTFKYNTSIKSEYSQALRHAVRNVNYRSRPDVGEGSNDSTHYLNVIEYKDVLQAPLQPLSENLDSGVYNTFEQDQIKYDVYGEAVVGALKDLGADGRKTVVIYLLGGGRGPIGTKILKSEREYNNTFRQGQESLKVKLYIVEKNPNAIVTLKYMNVRTWKRRVTIIESDMRSLPGIAKDRGFEQPDIIVSELLGSFGDNELSPECLDGVTGFLKPTTISIPQKYTSYVKPIMSTHIHQTIKAQSIPYLSRAIPSHGRGEPELDEDEMWIQKYPQGHVRNNMDQIYVVYLSKYIPLAETTKPVFTFEHPNFMNSSNERSDSIEFVMDRNADLMGFAGYFDLQLYKTVMLSIEPSTHTPGMVSWFPAVIPLRDQLRVGEGDRISLKIDRKVDNTGVWYEWHVEKKKTNGESVSTPIQNPNGESYYMRM","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"dataset":[],"UniParc":"UPI000007854E","uniref100":"UniRef100_P46580","uniref90":"UniRef90_P46580","uniref50":"UniRef50_P46580","genes":[{"name":{"value":"prmt-5","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"C34E10.5","url":"https://www.wormbase.org/db/seq/sequence?name=C34E10.5;class=Transcript"}}]},"synonyms":[{"value":"tag-251","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"C34E10.5","url":"https://www.wormbase.org/db/seq/sequence?name=C34E10.5;class=Transcript"}}]}],"orfNames":[{"value":"C34E10.5","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"C34E10.5","url":"https://www.wormbase.org/db/seq/sequence?name=C34E10.5;class=Transcript"}}]}]}],"alphafold_very_low_content":0.07356948228882834,"disorder_content":0.12806539509536785,"disprot_consensus":{"full":[{"start":1,"end":44,"type":"D"},{"start":331,"end":358,"type":"D"},{"start":359,"end":380,"type":"T"}],"Structural state":[{"start":1,"end":44,"type":"D"},{"start":331,"end":380,"type":"D"}],"Structural transition":[{"start":359,"end":380,"type":"T"}],"Disorder function":[{"start":1,"end":44,"type":"F"},{"start":331,"end":358,"type":"F"}],"Molecular function":[{"start":366,"end":371,"type":"F"},{"start":375,"end":380,"type":"F"}]}},{"disprot_id":"DP03322","acc":"Q94218-2","creator":"spenadias","date":"2021-05-21T14:06:15.836Z","features":{"pfam":[],"gene3D":[]},"length":575,"name":"Isoform b of Ufm1-specific protease","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":222,"end":243,"reference_id":"29251776","reference_source":"pmid","reference_html":"Structural basis for Ufm1 recognition by UfSP. <i> Kim KH, Ha BH, Kim EE. </i> FEBS Lett, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03322r001","statement":[{"text":"In cUfSP, the ten residues at the N-terminus of all chains, the loops between the a1 helix and b2 strand (residues 34–41) of four chains (chains C, D, E, F), and the regions between b10 and b11 (residues 222–243) of all chains are disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-01T12:57:25.033Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":10,"reference_id":"29251776","reference_source":"pmid","reference_html":"Structural basis for Ufm1 recognition by UfSP. <i> Kim KH, Ha BH, Kim EE. </i> FEBS Lett, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03322r002","statement":[{"text":"In cUfSP, the ten residues at the N-terminus of all chains, the loops between the a1 helix and b2 strand (residues 34–41) of four chains (chains C, D, E, F), and the regions between b10 and b11 (residues 222–243) of all chains are disordered.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MAPQSTPPPPVNELWFIDAQAMFQNYANLRSFSKSNANEINTTIGGFVFGRKARKQVIHVLFAYAEDLTESNRQFLESSLSADIELVGNLNIDGQSQILPGGQFTLQLTSRMLENRSISEFLDMNVMFNNEHVLMEGASCVSRVGYEWSLRAGREQEDVKSAAERLSMASFRFTYLNAEHGLVIREQKPEAAQQKYLDKFSKGAVPYKDVIEFTAMQSLTRDTSNDTEDQKLVPTVKVTKDNKHFTRLVTIGEVVFPAFFGDSSLDLYKRSREAFNRRANNTMMVTVNGIRAGRGVTTTTSATYLPPGWVSLLHLQLPTKWTDNEQRNYRIRLHKLFNLPSSKPVLRLSQALALHSESARLTNKKLIREPHLSITNYQPVGEITTVNGPYNYHHYMQDGIDDSGWGCAYRSFQTIWSWFILNGYTDKPVPSHREIQQALVDIQDKQAKFVGSRQWIGSTEISFVLNELLKLECRFIATNSGAEVVERVRELARHFETSGTPVMIGGNMLAHTILGVDFNDTTGETKFLVLDPHYTGSEDIKTITSKGWCAWKPASFWSKDHFYNMVLPQPPSDAI","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"dataset":[],"UniParc":"UPI0000185C15","uniref100":"","uniref90":"","uniref50":"","genes":[{"name":{"value":"odr-8","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9590179","url":"http://www.ncbi.nlm.nih.gov/pubmed/9590179","alternativeUrl":"https://europepmc.org/abstract/MED/9590179"}},{"code":"ECO:0000312","source":{"name":"WormBase","id":"F38A5.1a","url":"https://www.wormbase.org/db/seq/sequence?name=F38A5.1a;class=Transcript"}}]},"synonyms":[{"value":"ufsp-2","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"F38A5.1a","url":"https://www.wormbase.org/db/seq/sequence?name=F38A5.1a;class=Transcript"}}]}],"orfNames":[{"value":"F38A5.1","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"F38A5.1a","url":"https://www.wormbase.org/db/seq/sequence?name=F38A5.1a;class=Transcript"}}]}]}],"disorder_content":0.05565217391304348,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"},{"start":222,"end":243,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":222,"end":243,"type":"D"}]}},{"disprot_id":"DP03323","acc":"Q13316","creator":"jmarchetti","date":"2021-05-21T16:33:59.896Z","features":{"pfam":[{"id":"PF07263","name":"Dentin matrix protein 1 (DMP1)","start":1,"end":513}],"gene3D":[]},"length":513,"name":"Dentin matrix acidic phosphoprotein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":17,"end":217,"reference_id":"32190922","reference_source":"pmid","reference_html":"Functional derivatives of human dentin matrix protein 1 modulate morphology of calcium carbonate crystals. <i> Porębska A, Różycka M, Hołubowicz R, Szewczuk Z, Ożyhar A, Dobryszycki P. </i> FASEB J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03323r001","statement":[{"text":"The elution volumes (Ve) of standard proteins obtained by the gel filtration were used to calculate the partition coefficients  (Kav) and Stokes radii (RS).65 About 44K was eluted from the Superdex 75 10/300 GL column with a Ve corresponding to 41.4 Å for the 0.5 mg/mL and 40.9 Å for the 2.5 mg/ mL sample. \n RS values were significantly higher than the theoretical values calculated  under the assumption that the proteins are globular (20.4  Å  for 44K).","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-01T15:45:22.746Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":218,"end":513,"reference_id":"32190922","reference_source":"pmid","reference_html":"Functional derivatives of human dentin matrix protein 1 modulate morphology of calcium carbonate crystals. <i> Porębska A, Różycka M, Hołubowicz R, Szewczuk Z, Ożyhar A, Dobryszycki P. </i> FASEB J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03323r002","statement":[{"text":"The elution volumes (Ve) of standard proteins obtained by the gel filtration were used to calculate the partition coefficients  (Kav) and Stokes radii (RS). The calculated RS value for 56K was 47.8 Å for the 0.1 mg/mL and 48.1 Å for both (0.5 mg/mL and 2.5 mg/ mL) sample concentrations. RS values were significantly higher than the theoretical values calculated under the assumption that the proteins are globular (25.1  Å for 56K).","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-01T15:47:13.943Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":17,"end":217,"reference_id":"32190922","reference_source":"pmid","reference_html":"Functional derivatives of human dentin matrix protein 1 modulate morphology of calcium carbonate crystals. <i> Porębska A, Różycka M, Hołubowicz R, Szewczuk Z, Ożyhar A, Dobryszycki P. </i> FASEB J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03323r003","statement":[{"text":"The disordered nature of 44K and 56K fragments was confirmed by AUC. For globular compact proteins most common f/f0 values are within the range of 1.2-1.3, depending on the molecular weight. For IDPs, the f/f0 is higher due to the asymmetry and conformational flexibility that results in  higher friction and slows down sedimentation.80 The average f/f0 values calculated for 44K (2.26) and 56K (2.33) are high. These results indicate that both proteins have an elongated  shape and a high degree of conformational freedom.\n","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-01T15:48:03.151Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":218,"end":513,"reference_id":"32190922","reference_source":"pmid","reference_html":"Functional derivatives of human dentin matrix protein 1 modulate morphology of calcium carbonate crystals. <i> Porębska A, Różycka M, Hołubowicz R, Szewczuk Z, Ożyhar A, Dobryszycki P. </i> FASEB J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03323r004","statement":[{"text":"The disordered nature of 44K and 56K fragments was confirmed by AUC. For globular compact proteins most common f/f0 values are within the range of 1.2-1.3, depending on the molecular weight. For IDPs, the f/f0 is higher due to the asymmetry and conformational flexibility that results in  higher friction and slows down sedimentation.80 The average f/f0 values calculated for 44K (2.26) and 56K (2.33) are high. These results indicate that both proteins have an elongated  shape and a high degree of conformational freedom.\n","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-01T15:48:04.222Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":17,"end":217,"reference_id":"32190922","reference_source":"pmid","reference_html":"Functional derivatives of human dentin matrix protein 1 modulate morphology of calcium carbonate crystals. <i> Porębska A, Różycka M, Hołubowicz R, Szewczuk Z, Ożyhar A, Dobryszycki P. </i> FASEB J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03323r005","statement":[{"text":"The CD spectra of 44K (Figure 6A) and 56K (Figure 6B) exhibit such properties.  The analysis conducted using CDPro revealed that 44K is mostly disordered (70.7%±6.3%). The dominant type of ordered structures are β-strands (15.1%±5.9%) and turns  (9.7%±3.8%). Only 2.9%±2.5% are predicted to be α-helices (Table 3).\n","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-01T15:49:13.017Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":218,"end":513,"reference_id":"32190922","reference_source":"pmid","reference_html":"Functional derivatives of human dentin matrix protein 1 modulate morphology of calcium carbonate crystals. <i> Porębska A, Różycka M, Hołubowicz R, Szewczuk Z, Ożyhar A, Dobryszycki P. </i> FASEB J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03323r006","statement":[{"text":"The same calculations were conducted for the 56K protein. The results suggest that 56K may be more disordered than 44K, but the differences do not seem to be significant (Table 3).","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-01T15:49:14.199Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":17,"end":217,"reference_id":"32190922","reference_source":"pmid","reference_html":"Functional derivatives of human dentin matrix protein 1 modulate morphology of calcium carbonate crystals. <i> Porębska A, Różycka M, Hołubowicz R, Szewczuk Z, Ożyhar A, Dobryszycki P. </i> FASEB J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000018","term_name":"disorder to molten globule","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03323r007","statement":[{"text":"For 44K and 56K we observed an increase in the ellipticity minimum at 200 nm and the simultaneous appearance of two minima at 208 nm and 222 nm with increasing concentrations of TFE (Supporting Figure S1). We conclude  that fragments of both 44K and 56K may become ordered  in a hydrophobic and/or crowded environment,87,88 for example, in contact with interaction partners or in the biomineralizing extracellular matrix","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-14T15:05:40.125Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":218,"end":513,"reference_id":"32190922","reference_source":"pmid","reference_html":"Functional derivatives of human dentin matrix protein 1 modulate morphology of calcium carbonate crystals. <i> Porębska A, Różycka M, Hołubowicz R, Szewczuk Z, Ożyhar A, Dobryszycki P. </i> FASEB J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000018","term_name":"disorder to molten globule","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03323r008","statement":[{"text":"For 44K and 56K we observed an increase in the ellipticity minimum at 200 nm and the simultaneous appearance of two minima at 208 nm and 222 nm with increasing concentrations of TFE (Supporting Figure S1). We conclude  that fragments of both 44K and 56K may become ordered  in a hydrophobic and/or crowded environment,87,88 for example, in contact with interaction partners or in the biomineralizing extracellular matrix","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-15T08:06:49.558Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":17,"end":217,"reference_id":"32190922","reference_source":"pmid","reference_html":"Functional derivatives of human dentin matrix protein 1 modulate morphology of calcium carbonate crystals. <i> Porębska A, Różycka M, Hołubowicz R, Szewczuk Z, Ożyhar A, Dobryszycki P. </i> FASEB J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03323r009","statement":[{"text":"For 44K, the experiment has revealed two values (22 788 ± 6 Da and 22 773 ± 6 Da) which were in agreement with theoretical value calculated by the ProtParam tool50 (22 774.7 Da)","type":"Results"},{"text":"The observed discrepancy between the theoretical and SDS-PAGE-based molecular mass values is typical for members of the family of IDPs,  which fail to form the rigid 3D structures under physiological  conditions. ","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-15T08:06:32.451Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":218,"end":513,"reference_id":"32190922","reference_source":"pmid","reference_html":"Functional derivatives of human dentin matrix protein 1 modulate morphology of calcium carbonate crystals. <i> Porębska A, Różycka M, Hołubowicz R, Szewczuk Z, Ożyhar A, Dobryszycki P. </i> FASEB J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03323r010","statement":[{"text":"The experimental MW for 56K (34 025 ± 6 Da) was higher by 10.7 Da than the theoretical value (34 014.3 Da). The small mass differences observed may come from the methylation of the amino groups, probably from the N-terminal methionine. ","type":"Results"},{"text":"The observed discrepancy between the theoretical and SDS-PAGE-based molecular mass values is typical for members of the family of IDPs,  which fail to form the rigid 3D structures under physiological  conditions. ","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-15T08:06:33.498Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":17,"end":217,"reference_id":"32190922","reference_source":"pmid","reference_html":"Functional derivatives of human dentin matrix protein 1 modulate morphology of calcium carbonate crystals. <i> Porębska A, Różycka M, Hołubowicz R, Szewczuk Z, Ożyhar A, Dobryszycki P. </i> FASEB J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000018","term_name":"disorder to molten globule","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03323r011","statement":[{"text":"In contrast, a series of SEC experiments  revealed that calcium ions influenced the conformations of  both fragments. Concomitantly to the increase of concentration of calcium ions, the RS of 44K and 56K fragments decreased from 47.8 to 39.6 Å and from 62.0 to 53.3 Å, respectively (Figure 7D)","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-15T08:05:22.881Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":218,"end":513,"reference_id":"32190922","reference_source":"pmid","reference_html":"Functional derivatives of human dentin matrix protein 1 modulate morphology of calcium carbonate crystals. <i> Porębska A, Różycka M, Hołubowicz R, Szewczuk Z, Ożyhar A, Dobryszycki P. </i> FASEB J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000018","term_name":"disorder to molten globule","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03323r012","statement":[{"text":"In contrast, a series of SEC experiments  revealed that calcium ions influenced the conformations of  both fragments. Concomitantly to the increase of concentration of calcium ions, the RS of 44K and 56K fragments decreased from 47.8 to 39.6 Å and from 62.0 to 53.3 Å, respectively (Figure 7D)","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-15T08:05:21.449Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":17,"end":217,"reference_id":"32190922","reference_source":"pmid","reference_html":"Functional derivatives of human dentin matrix protein 1 modulate morphology of calcium carbonate crystals. <i> Porębska A, Różycka M, Hołubowicz R, Szewczuk Z, Ożyhar A, Dobryszycki P. </i> FASEB J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000018","term_name":"disorder to molten globule","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03323r013","statement":[{"text":" The RS values calculated for 44K (42.3-41.6  Å) (Table  4) are in good  agreement with the values derived from SEC (47.7-39.6 Å).  10 mM of calcium ions was enough to decrease the RS of 44K from 46.7 to 42.3 Å. The frictional coefficient f/f0 decreased from 2.331 to 2.192, while the sedimentation coefficient  s20,w increased from 1.686 to 1.794 S. There was no signif-icant change in the MW. These results clearly indicate that  44K becomes more compact in the presence of calcium ions.  Increasing the concentration of calcium ions above 10  mM  did not result in significant changes.","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-15T08:05:19.921Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":218,"end":513,"reference_id":"32190922","reference_source":"pmid","reference_html":"Functional derivatives of human dentin matrix protein 1 modulate morphology of calcium carbonate crystals. <i> Porębska A, Różycka M, Hołubowicz R, Szewczuk Z, Ożyhar A, Dobryszycki P. </i> FASEB J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000018","term_name":"disorder to molten globule","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03323r014","statement":[{"text":"In the case of 56K, adding 10 mM of calcium ions induced a decrease in the RS from 49.3 to 44.3  Å. The f/f0 decreased from 2.336 to 2.135, the s20,w increased from 2.008 to 2.125, and the apparent MW decreased slightly from 34.9 to 33.2 kDa. At higher concentrations of calcium ions, small amounts of heavier species were detected.","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-15T08:05:19.001Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":17,"end":217,"reference_id":"32190922","reference_source":"pmid","reference_html":"Functional derivatives of human dentin matrix protein 1 modulate morphology of calcium carbonate crystals. <i> Porębska A, Różycka M, Hołubowicz R, Szewczuk Z, Ożyhar A, Dobryszycki P. </i> FASEB J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2023_06","version":3,"region_id":"DP03323r015","statement":[{"text":"The RS values calculated for 44K (42.3-41.6 Å) (Table 4) are in good agreement with the values derived from SEC (47.7-39.6 Å). 10 mM of calcium ions was enough to decrease the RS of 44K from 46.7 to 42.3 Å. The frictional coefficient f/f0 decreased from 2.331 to 2.192, while the sedimentation coefficient s20,w increased from 1.686 to 1.794 S. There was no signif-icant change in the MW. These results clearly indicate that 44K becomes more compact in the presence of calcium ions. Increasing the concentration of calcium ions above 10 mM did not result in significant changes.","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-15T08:05:07.819Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":218,"end":513,"reference_id":"32190922","reference_source":"pmid","reference_html":"Functional derivatives of human dentin matrix protein 1 modulate morphology of calcium carbonate crystals. <i> Porębska A, Różycka M, Hołubowicz R, Szewczuk Z, Ożyhar A, Dobryszycki P. </i> FASEB J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":3,"region_id":"DP03323r016","statement":[{"text":"In contrast, a series of SEC experiments  revealed that calcium ions influenced the conformations of  both fragments. Concomitantly to the increase of concentration of calcium ions, the RS of 44K and 56K fragments decreased from 47.8 to 39.6 Å and from 62.0 to 53.3 Å, respectively (Figure 7D).","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-14T15:05:53.342Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":17,"end":217,"reference_id":"32190922","reference_source":"pmid","reference_html":"Functional derivatives of human dentin matrix protein 1 modulate morphology of calcium carbonate crystals. <i> Porębska A, Różycka M, Hołubowicz R, Szewczuk Z, Ożyhar A, Dobryszycki P. </i> FASEB J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":3,"region_id":"DP03323r017","statement":[{"text":"Concomitantly to the increase of concentration of calcium ions, the RS of 44K and 56K fragments decreased from 47.8 to 39.6 Å and from 62.0 to 53.3 Å, respectively (Figure 7D).","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-14T15:05:54.315Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":218,"end":513,"reference_id":"32190922","reference_source":"pmid","reference_html":"Functional derivatives of human dentin matrix protein 1 modulate morphology of calcium carbonate crystals. <i> Porębska A, Różycka M, Hołubowicz R, Szewczuk Z, Ożyhar A, Dobryszycki P. </i> FASEB J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2023_06","version":3,"region_id":"DP03323r018","statement":[{"text":"The RS values calculated for 44K (42.3-41.6 Å) (Table 4) are in good agreement with the values derived from SEC (47.7-39.6 Å). 10 mM of calcium ions was enough to decrease the RS of 44K from 46.7 to 42.3 Å. The frictional coefficient f/f0 decreased from 2.331 to 2.192, while the sedimentation coefficient s20,w increased from 1.686 to 1.794 S. There was no signif-icant change in the MW. These results clearly indicate that 44K becomes more compact in the presence of calcium ions. Increasing the concentration of calcium ions above 10 mM did not result in significant changes.","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-14T15:05:58.846Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":18,"released":"2023_06","sequence":"MKISILLMFLWGLSCALPVTRYQNNESEDSEEWKGHLAQAPTPPLESSESSEGSKVSSEEQANEDPSDSTQSEEGLGSDDHQYIYRLAGGFSRSTGKGGDDKDDDEDDSGDDTFGDDDSGPGPKDRQEGGNSRLGSDEDSDDTIQASEESAPQGQDSAQDTTSESRELDNEDRVDSKPEGGDSTQESESEEHWVGGGSDGESSHGDGSELDDEGMQSDDPESIRSERGNSRMNSAGMKSKESGENSEQANTQDSGGSQLLEHPSRKIFRKSRISEEDDRSELDDNNTMEEVKSDSTENSNSRDTGLSQPRRDSKGDSQEDSKENLSQEESQNVDGPSSESSQEANLSSQENSSESQEEVVSESRGDNPDPTTSYVEDQEDSDSSEEDSSHTLSHSKSESREEQADSESSESLNFSEESPESPEDENSSSQEGLQSHSSSAESQSEESHSEEDDSDSQDSSRSKEDSNSTESKSSSEEDGQLKNIEIESRKLTVDAYHNKPIGDQDDNDCQDGY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000016A23C","uniref100":"UniRef100_Q13316","uniref90":"UniRef90_Q13316","uniref50":"UniRef50_Q13316","genes":[{"name":{"value":"DMP1"}}],"alphafold_very_low_content":0.7251461988304093,"disorder_content":0.9688109161793372,"disprot_consensus":{"full":[{"start":17,"end":513,"type":"T"}],"Structural state":[{"start":17,"end":513,"type":"D"}],"Structural transition":[{"start":17,"end":513,"type":"T"}],"Molecular function":[{"start":17,"end":513,"type":"F"}]}},{"disprot_id":"DP03324","acc":"P35052","creator":"jmarchetti","date":"2021-05-21T22:34:30.925Z","features":{"pfam":[{"id":"PF01153","name":"Glypican","start":19,"end":550}],"gene3D":[]},"length":558,"name":"Glypican-1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":350,"end":361,"reference_id":"24311593","reference_source":"pmid","reference_html":"Improvements in the order, isotropy and electron density of glypican-1 crystals by controlled dehydration. <i> Awad W, Svensson Birkedal G, Thunnissen MM, Mani K, Logan DT. </i> Acta Crystallogr D Biol Crystallogr, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4ACR"}],"region_id":"DP03324r002","statement":[{"text":"As noted, some parts of the structure (PDB entry 4acr) were partially disordered and were not visible in the initial electron-density map.","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-15T08:32:20.312Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2021_06","sequence":"MELRARGWWLLCAAAALVACARGDPASKSRSCGEVRQIYGAKGFSLSDVPQAEISGEHLRICPQGYTCCTSEMEENLANRSHAELETALRDSSRVLQAMLATQLRSFDDHFQHLLNDSERTLQATFPGAFGELYTQNARAFRDLYSELRLYYRGANLHLEETLAEFWARLLERLFKQLHPQLLLPDDYLDCLGKQAEALRPFGEAPRELRLRATRAFVAARSFVQGLGVASDVVRKVAQVPLGPECSRAVMKLVYCAHCLGVPGARPCPDYCRNVLKGCLANQADLDAEWRNLLDSMVLITDKFWGTSGVESVIGSVHTWLAEAINALQDNRDTLTAKVIQGCGNPKVNPQGPGPEEKRRRGKLAPRERPPSGTLEKLVSEAKAQLRDVQDFWISLPGTLCSEKMALSTASDDRCWNGMARGRYLPEVMGDGLANQINNPEVEVDITKPDMTIRQQIMQLKIMTNRLRSAYNGNDVDFQDASDDGSGSGSGDGCLDDLCSRKVSRKSSSSRTPLTHALPGLSEQEGQKTSAASCPQPPTFLLPLLLFLALTVARPRWR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000032F5D","uniref100":"UniRef100_P35052","uniref90":"UniRef90_P35052","uniref50":"UniRef50_P35052","genes":[{"name":{"value":"GPC1"}}],"alphafold_very_low_content":0.15591397849462366,"disorder_content":0.021505376344086023,"disprot_consensus":{"full":[{"start":350,"end":361,"type":"D"}],"Structural state":[{"start":350,"end":361,"type":"D"}]}},{"disprot_id":"DP03325","acc":"Q9SZF7","creator":"gerdos","date":"2021-05-24T13:03:54.170Z","features":{"pfam":[{"id":"PF03514","name":"GRAS domain family","start":145,"end":529}],"gene3D":[]},"length":531,"name":"Protein SHORT-ROOT","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":59,"end":120,"reference_id":"28211915","reference_source":"pmid","reference_html":"Structure of the SHR-SCR heterodimer bound to the BIRD/IDD transcriptional factor JKD. <i> Hirano Y, Nakagawa M, Suyama T, Murase K, Shirakawa M, Takayama S, Sun TP, Hakoshima T. </i> Nat Plants, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jiserte","curator_name":"Javier Iserte","curator_orcid":"0000-0003-0056-1177","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5B3G"}],"region_id":"DP03325r001","statement":[{"text":"Most of the N-terminal extensions were not observed in the current electron density map, whereas the short N-terminal segment of SHR, the N-terminal strap, was observed to extend towards SCR.","type":"Results"},{"text":"The N-terminal 6 residues of SCR (residues 275-280) and 61 residues of SHR (residues 59-119) were not observed in the current map.","type":"Figure"},{"text":"The boundaries of the N-terminal region are 59 to 120 according the PDB 5B3G.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-13T12:36:43.963Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MDTLFRLVSLQQQQQSDSIITNQSSLSRTSTTTTGSPQTAYHYNFPQNDVVEECFNFFMDEEDLSSSSSHHNHHNHNNPNTYYSPFTTPTQYHPATSSTPSSTAAAAALASPYSSSGHHNDPSAFSIPQTPPSFDFSANAKWADSVLLEAARAFSDKDTARAQQILWTLNELSSPYGDTEQKLASYFLQALFNRMTGSGERCYRTMVTAAATEKTCSFESTRKTVLKFQEVSPWATFGHVAANGAILEAVDGEAKIHIVDISSTFCTQWPTLLEALATRSDDTPHLRLTTVVVANKFVNDQTASHRMMKEIGNRMEKFARLMGVPFKFNIIHHVGDLSEFDLNELDVKPDEVLAINCVGAMHGIASRGSPRDAVISSFRRLRPRIVTVVEEEADLVGEEEGGFDDEFLRGFGECLRWFRVCFESWEESFPRTSNERLMLERAAGRAIVDLVACEPSDSTERRETARKWSRRMRNSGFGAVGYSDEVADDVRALLRRYKEGVWSMVQCPDAAGIFLCWRDQPVVWASAWRPT","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"dataset":[],"UniParc":"UPI00000AB228","uniref100":"UniRef100_Q9SZF7","uniref90":"UniRef90_Q9SZF7","uniref50":"UniRef50_Q9SZF7","genes":[{"name":{"value":"SHR","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10850497","url":"http://www.ncbi.nlm.nih.gov/pubmed/10850497","alternativeUrl":"https://europepmc.org/abstract/MED/10850497"}}]},"synonyms":[{"value":"SGR7","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9670559","url":"http://www.ncbi.nlm.nih.gov/pubmed/9670559","alternativeUrl":"https://europepmc.org/abstract/MED/9670559"}}]}],"orfNames":[{"value":"F19F18.140","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"CAB38304.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAB38304.1"}}]}],"olnNames":[{"value":"At4g37650","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT4G37650","url":""}}]}]}],"alphafold_very_low_content":0.21657250470809794,"disorder_content":0.1167608286252354,"disprot_consensus":{"full":[{"start":59,"end":120,"type":"D"}],"Structural state":[{"start":59,"end":120,"type":"D"}]}},{"disprot_id":"DP03326","acc":"P39286","creator":"csanchezrocha","date":"2021-05-25T13:59:01.371Z","features":{"pfam":[{"id":"PF03193","name":"RsgA GTPase","start":100,"end":276}],"gene3D":[]},"length":350,"name":"Small ribosomal subunit biogenesis GTPase RsgA","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":1,"end":34,"reference_id":"21788480","reference_source":"pmid","reference_html":"Structural basis for the function of a small GTPase RsgA on the 30S ribosomal subunit maturation revealed by cryoelectron microscopy. <i> Guo Q, Yuan Y, Xu Y, Feng B, Liu L, Chen K, Sun M, Yang Z, Lei J, Gao N. </i> Proc Natl Acad Sci U S A, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2YKR"},{"db":"EMDB","id":"1884"}],"region_id":"DP03326r001","statement":[{"text":"A major species-specific feature of RsgA from E. coli is that it possesses an additional N-terminal extension, which is disordered in the crystal structure of RsgA (19) and therefore absent in our atomic model as well (missing residues 1–34). Because of its flexible nature, we were only able to locate partial densities for this N-terminal extension.","type":"Results"},{"text":" The first 34 residues were cut from the model because of the disorderness in the template.","type":"Supplementary material"},{"text":"The RsgA N-terminal extension is disordered in the crystal structure, and thus absent in the atomic model. Partially resolved densities for the N extension show that it interacts with h18, h34, and S3.","type":"Supplementary material"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-01T12:00:14.367Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":1,"end":34,"reference_id":"21788480","reference_source":"pmid","reference_html":"Structural basis for the function of a small GTPase RsgA on the 30S ribosomal subunit maturation revealed by cryoelectron microscopy. <i> Guo Q, Yuan Y, Xu Y, Feng B, Liu L, Chen K, Sun M, Yang Z, Lei J, Gao N. </i> Proc Natl Acad Sci U S A, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"GO:0019843","term_name":"rRNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"2YKR"},{"db":"EMDB","id":"1884"}],"region_id":"DP03326r002","statement":[{"text":"A major species-specific feature of RsgA from E. coli is that it possesses an additional N-terminal extension, which is disordered in the crystal structure of RsgA (19) and therefore absent in our atomic model as well (missing residues 1–34). Because of its flexible nature, we were only able to locate partial densities for this N-terminal extension. Nevertheless, the map clearly indicates that this extension interacts at least with helix 18 (loop 530) of the body, and helix 34 and S3 of the head (Fig. S2), consistent with the fact that the first 20 N-terminal residues are required for the 30S subunit binding.","type":"Results"},{"text":"The RsgA N-terminal extension is disordered in the crystal structure, and thus absent in the atomic model. Partially resolved densities for the N extension show that it interacts with h18, h34, and S3.","type":"Supplementary material"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-04T12:35:39.716Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a ribosomal RNA.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":2,"released":"2021_12","sequence":"MSKNKLSKGQQRRVNANHQRRLKTSKEKPDYDDNLFGEPDEGIVISRFGMHADVESADGDVHRCNIRRTIRSLVTGDRVVWRPGKPAAEGVNVKGIVEAVHERTSVLTRPDFYDGVKPIAANIDQIVIVSAILPELSLNIIDRYLVACETLQIEPIIVLNKIDLLDDEGMAFVNEQMDIYRNIGYRVLMVSSHTQDGLKPLEEALTGRISIFAGQSGVGKSSLLNALLGLQKEILTNDISDNSGLGQHTTTAARLYHFPHGGDVIDSPGVREFGLWHLEPEQITQGFVEFHDYLGLCKYRDCKHDTDPGCAIREAVEEGKIAETRFENYHRILESMAQVKTRKNFSDTDD","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":["RNA-binding proteins"],"UniParc":"UPI00000322AA","uniref100":"UniRef100_C5A1F5","uniref90":"UniRef90_Q83IK0","uniref50":"UniRef50_Q8EJ79","genes":[{"name":{"value":"rsgA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01820","url":"https://hamap.expasy.org/unirule/MF_01820"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"15466596","url":"http://www.ncbi.nlm.nih.gov/pubmed/15466596","alternativeUrl":"https://europepmc.org/abstract/MED/15466596"}}]},"synonyms":[{"value":"engC"},{"value":"yjeQ"}],"olnNames":[{"value":"b4161"},{"value":"JW4122"}]}],"alphafold_very_low_content":0.10571428571428572,"disorder_content":0.09714285714285714,"disprot_consensus":{"full":[{"start":1,"end":34,"type":"D"}],"Structural state":[{"start":1,"end":34,"type":"D"}],"Molecular function":[{"start":1,"end":34,"type":"F"}]}},{"disprot_id":"DP03327","acc":"P05055","creator":"csanchezrocha","date":"2021-05-25T14:23:13.440Z","features":{"pfam":[{"id":"PF00013","name":"KH domain","start":556,"end":614},{"id":"PF00575","name":"S1 RNA binding domain","start":619,"end":690},{"id":"PF01138","name":"3' exoribonuclease family, domain 1","start":15,"end":144},{"id":"PF01138","name":"3' exoribonuclease family, domain 1","start":324,"end":456},{"id":"PF03725","name":"3' exoribonuclease family, domain 2","start":147,"end":210},{"id":"PF03726","name":"Polyribonucleotide nucleotidyltransferase, RNA binding domain","start":242,"end":320}],"gene3D":[]},"length":711,"name":"Polyribonucleotide nucleotidyltransferase","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":553,"end":612,"reference_id":"18812438","reference_source":"pmid","reference_html":"Crystal structure of Escherichia coli PNPase: central channel residues are involved in processive RNA degradation. <i> Shi Z, Yang WZ, Lin-Chao S, Chak KF, Yuan HS. </i> RNA, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3CDI"}],"region_id":"DP03327r001","statement":[{"text":"The C-terminal KH and S1 domains (Fig. 1A, residues 566–734) were not visible, containing only broken densities in the electron density maps. These KH and S1 domains were likely disordered as a whole in the crystal structure since they were connected to the second RNase PH domain by a long flexible loop.","type":"Results"},{"text":"The C-terminal KH/S1 domain (marked by dashed circle) was disordered and thus not visible in the crystal structure.","type":"Figure"},{"text":"The IDR was separated according to the protein domain composition. This corresponds to the domain \"KH\".","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-25T13:09:50.265Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":238,"end":298,"reference_id":"18812438","reference_source":"pmid","reference_html":"Crystal structure of Escherichia coli PNPase: central channel residues are involved in processive RNA degradation. <i> Shi Z, Yang WZ, Lin-Chao S, Chak KF, Yuan HS. </i> RNA, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3CDJ"}],"region_id":"DP03327r002","statement":[{"text":"These results suggest that the structure of DKH/S1 was less compact than full-length PNPase.\nTo further confirm this observation, the sizes of central channel of full-length PNPase and DKH/S1 mutant were calculated by Hole (Smart et al. 1993). To ensure a fair comparison, disordered side chains or side chains with different conformations in the two structures were removed for the calculation, including the side chains of 105–107, 261–321, 394, and 409–418.","type":"Results"},{"text":" The IDR characterized in the publication and spanning residues 261–321 corresponds to region 238-298 of the amino acid sequence.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-25T13:09:51.452Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":386,"end":395,"reference_id":"18812438","reference_source":"pmid","reference_html":"Crystal structure of Escherichia coli PNPase: central channel residues are involved in processive RNA degradation. <i> Shi Z, Yang WZ, Lin-Chao S, Chak KF, Yuan HS. </i> RNA, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3CDJ"}],"region_id":"DP03327r003","statement":[{"text":"These results suggest that the structure of DKH/S1 was less compact than full-length PNPase.\nTo further confirm this observation, the sizes of central channel of full-length PNPase and DKH/S1 mutant were calculated by Hole (Smart et al. 1993). To ensure a fair comparison, disordered side chains or side chains with different conformations in the two structures were removed for the calculation, including the side chains of 105–107, 261–321, 394, and 409–418.","type":"Results"},{"text":" The IDR characterized in the publication and spanning residues 409-418 corresponds to region 386-395 of the amino acid sequence.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-25T13:09:52.317Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":543,"end":711,"reference_id":"18812438","reference_source":"pmid","reference_html":"Crystal structure of Escherichia coli PNPase: central channel residues are involved in processive RNA degradation. <i> Shi Z, Yang WZ, Lin-Chao S, Chak KF, Yuan HS. </i> RNA, 2008","date":"2022-03-08T14:00:59.388Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":4,"region_id":"DP03327r004","statement":[{"text":"We purified full-length PNPase (Fig. 1A, residues 17–734) and the KH/S1 domain-truncated mutant (Fig. 1A, DKH/S1, residues 17–570), and compared their RNA binding activities by electrophoresis mobility shift assays, using a 20-mer and an 8-mer single-stranded RNA as substrates. The EMSA (Fig. 1B) showed that the full-length PNPase bound 20-mer and 8-mer RNA at concentrations >4 nM, whereas the truncated mutant DKH/S1 bound 20-mer and 8-mer RNA at concentrations >z20 nM.","type":"Results"},{"text":"The KH/S1 domain pair is responsible for direct interaction with RNA.","type":"Discussion"},{"text":"Our biochemical, circular dichroism, dynamic light scat- tering, and structural results consistently suggest that the KH/S1 domains are involved not only in RNA binding but also in the formation of a compact trimer with a more constricted central channel","type":"Discussion"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"RNAcentral","id":"URS0000B2BA01_10116","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-14T16:49:00.875Z"}},{"start":543,"end":711,"reference_id":"18812438","reference_source":"pmid","reference_html":"Crystal structure of Escherichia coli PNPase: central channel residues are involved in processive RNA degradation. <i> Shi Z, Yang WZ, Lin-Chao S, Chak KF, Yuan HS. </i> RNA, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"3CDI"}],"region_id":"DP03327r005","statement":[{"text":"We then tested the exoribonucleolytic activity of full- length PNPase and DKH/S1 mutant in time course activity assays. The full-length PNPase digested both 20-mer and 8- mer RNA into small oligonucleotides, as shown in Figure 1C.","type":"Results"},{"text":"These results imply that the KH/S1 domain is involved not only in RNA binding, but also in modulation of enzyme activity in an unknown way.","type":"Results"},{"text":"RNase activities of full-length PNPase and DKH/S1 mutant were assayed by incubation of enzymes, respectively, with 8-mer and 20-mer single-stranded RNAs in time course experiments under the conditions described in Materials and Methods. The left panel shows that DKH/S1 had lower activities in cleaving 20-mer ssRNAs compared to the full-length PNPase. The right panel shows that DKH/S1 cannot degrade shorter 8-mer ssRNAs.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-25T13:09:45.590Z"},"ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":543,"end":711,"reference_id":"18812438","reference_source":"pmid","reference_html":"Crystal structure of Escherichia coli PNPase: central channel residues are involved in processive RNA degradation. <i> Shi Z, Yang WZ, Lin-Chao S, Chak KF, Yuan HS. </i> RNA, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006200","ec_ontology":"ECO","ec_name":"circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"3CDI"}],"region_id":"DP03327r006","statement":[{"text":"This result showed that the truncated PNPase, without the KH/S1 domain, was melted at lower temperatures and dissociated into monomers in less acidic solutions. Therefore, we conclude that the KH and S1 domains contribute to the formation of a more stable trimeric PNPase.","type":"Results"},{"text":"The KH/S1 domain helps PNPase to form a more stable compact trimer. Our biochemical, circular dichroism, dynamic light scattering, and structural results consistently suggest that the KH/S1 domains are involved not only in RNA binding but also in the formation of a compact trimer with a more constricted central channel.","type":"Discussion"},{"text":"We conclude that the KH/S1 domains and the upper neck in the channel recruit RNA into the channel, and the lower neck keeps hold of the RNA as it guides it into the PNPase active site for processive degradation. Constrictions of the appropriate size at the necks in the central channel of exosomes and PNPases play a crucial role in RNA binding and processive degradation.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-25T13:09:48.055Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":543,"end":711,"reference_id":"18812438","reference_source":"pmid","reference_html":"Crystal structure of Escherichia coli PNPase: central channel residues are involved in processive RNA degradation. <i> Shi Z, Yang WZ, Lin-Chao S, Chak KF, Yuan HS. </i> RNA, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"3CDI"}],"region_id":"DP03327r007","statement":[{"text":"This result showed that the truncated PNPase, without the KH/S1 domain, was melted at lower temperatures and dissociated into monomers in less acidic solutions. Therefore, we conclude that the KH and S1 domains contribute to the formation of a more stable trimeric PNPase.","type":"Results"},{"text":"The KH/S1 domain helps PNPase to form a more stable compact trimer. Our biochemical, circular dichroism, dynamic light scattering, and structural results consistently suggest that the KH/S1 domains are involved not only in RNA binding but also in the formation of a compact trimer with a more constricted central channel.","type":"Discussion"},{"text":"We conclude that the KH/S1 domains and the upper neck in the channel recruit RNA into the channel, and the lower neck keeps hold of the RNA as it guides it into the PNPase active site for processive degradation. Constrictions of the appropriate size at the necks in the central channel of exosomes and PNPases play a crucial role in RNA binding and processive degradation.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-25T13:09:48.816Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":75,"end":84,"reference_id":"18812438","reference_source":"pmid","reference_html":"Crystal structure of Escherichia coli PNPase: central channel residues are involved in processive RNA degradation. <i> Shi Z, Yang WZ, Lin-Chao S, Chak KF, Yuan HS. </i> RNA, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3CDJ"}],"region_id":"DP03327r008","statement":[{"text":"This region is not described in the publication, although it corresponds to a region with missing electron density in the PDB structure. ","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-25T13:09:53.182Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":359,"end":370,"reference_id":"18812438","reference_source":"pmid","reference_html":"Crystal structure of Escherichia coli PNPase: central channel residues are involved in processive RNA degradation. <i> Shi Z, Yang WZ, Lin-Chao S, Chak KF, Yuan HS. </i> RNA, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3CDJ"}],"region_id":"DP03327r009","statement":[{"text":"This region is not described in the publication, although it corresponds to a region with missing electron density in the PDB structure. ","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-25T13:09:54.145Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":622,"end":690,"reference_id":"18812438","reference_source":"pmid","reference_html":"Crystal structure of Escherichia coli PNPase: central channel residues are involved in processive RNA degradation. <i> Shi Z, Yang WZ, Lin-Chao S, Chak KF, Yuan HS. </i> RNA, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3CDI"}],"region_id":"DP03327r010","statement":[{"text":"The C-terminal KH and S1 domains (Fig. 1A, residues 566–734) were not visible, containing only broken densities in the electron density maps. These KH and S1 domains were likely disordered as a whole in the crystal structure since they were connected to the second RNase PH domain by a long flexible loop.","type":"Results"},{"text":"The C-terminal KH/S1 domain (marked by dashed circle) was disordered and thus not visible in the crystal structure.","type":"Figure"},{"text":"The IDR was separated according to the protein domain composition. This corresponds to the domain \"S1\".","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-25T13:09:55.131Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":10,"released":"2021_12","sequence":"MLNPIVRKFQYGQHTVTLETGMMARQATAAVMVSMDDTAVFVTVVGQKKAKPGQDFFPLTVNYQERTYAAGRIPGSFFRREGRPSEGETLIARLIDRPIRPLFPEGFVNEVQVIATVVSVNPQVNPDIVAMIGASAALSLSGIPFNGPIGAARVGYINDQYVLNPTQDELKESKLDLVVAGTEAAVLMVESEAQLLSEDQMLGAVVFGHEQQQVVIQNINELVKEAGKPRWDWQPEPVNEALNARVAALAEARLSDAYRITDKQERYAQVDVIKSETIATLLAEDETLDENELGEILHAIEKNVVRSRVLAGEPRIDGREKDMIRGLDVRTGVLPRTHGSALFTRGETQALVTATLGTARDAQVLDELMGERTDTFLFHYNFPPYSVGETGMVGSPKRREIGHGRLAKRGVLAVMPDMDKFPYTVRVVSEITESNGSSSMASVCGASLALMDAGVPIKAAVAGIAMGLVKEGDNYVVLSDILGDEDHLGDMDFKVAGSRDGISALQMDIKIEGITKEIMQVALNQAKGARLHILGVMEQAINAPRGDISEFAPRIHTIKINPDKIKDVIGKGGSVIRALTEETGTTIEIEDDGTVKIAATDGEKAKHAIRRIEEITAEIEVGRVYTGKVTRIVDFGAFVAIGGGKEGLVHISQIADKRVEKVTDYLQMGQEVPVKVLEVDRQGRIRLSIKEATEQSQPAAAPEAPAAEQGE","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":["RNA-binding proteins","Stress response proteins"],"UniParc":"UPI000016F4B7","uniref100":"UniRef100_C4ZSQ5","uniref90":"UniRef90_A8AQ53","uniref50":"UniRef50_P41121","genes":[{"name":{"value":"pnp","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01595","url":"https://hamap.expasy.org/unirule/MF_01595"}}]},"olnNames":[{"value":"b3164"},{"value":"JW5851"}]}],"alphafold_very_low_content":0.02250351617440225,"disorder_content":0.31223628691983124,"disprot_consensus":{"full":[{"start":75,"end":84,"type":"D"},{"start":238,"end":298,"type":"D"},{"start":359,"end":370,"type":"D"},{"start":386,"end":395,"type":"D"},{"start":543,"end":552,"type":"F"},{"start":553,"end":612,"type":"D"},{"start":613,"end":621,"type":"F"},{"start":622,"end":690,"type":"D"},{"start":691,"end":711,"type":"F"}],"Structural state":[{"start":75,"end":84,"type":"D"},{"start":238,"end":298,"type":"D"},{"start":359,"end":370,"type":"D"},{"start":386,"end":395,"type":"D"},{"start":553,"end":612,"type":"D"},{"start":622,"end":690,"type":"D"}],"Molecular function":[{"start":543,"end":711,"type":"F"}]}},{"disprot_id":"DP03329","acc":"P0AG67","creator":"csanchezrocha","date":"2021-05-25T15:23:12.650Z","features":{"pfam":[{"id":"PF00575","name":"S1 RNA binding domain","start":19,"end":78},{"id":"PF00575","name":"S1 RNA binding domain","start":104,"end":171},{"id":"PF00575","name":"S1 RNA binding domain","start":190,"end":260},{"id":"PF00575","name":"S1 RNA binding domain","start":275,"end":347},{"id":"PF00575","name":"S1 RNA binding domain","start":361,"end":434},{"id":"PF00575","name":"S1 RNA binding domain","start":449,"end":520}],"gene3D":[]},"length":557,"name":"30S ribosomal protein S1","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":73,"end":86,"reference_id":"29247757","reference_source":"pmid","reference_html":"Structural dynamics of protein S1 on the 70S ribosome visualized by ensemble cryo-EM. <i> Loveland AB, Korostelev AA. </i> Methods, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6BU8"},{"db":"EMDB","id":"EMD-7289"}],"region_id":"DP03329r001","statement":[{"text":"Deep classification of cryo-EM data reveals that the N-terminal helix of S1 acts as an anchor (Fig. 2C), whereas the rest of S1 is extremely dynamic (Movie 1).","type":"Results"},{"text":"However, continuous density was visible only in one or two classes and was not of sufficient quality to dock S1 domains. Overall, this unbiased global classification was useful in that it revealed S1 binding site, however the separation of classes occurred on too many different features of the 70S ribosome and the classes did not reveal domain distribution for S1.","type":"Results"},{"text":"We compared four approaches for deep classification of a ribosome dataset to identify conformational states of a highly dynamic protein S1.","type":"Conclusion"},{"text":"In the next step, a spherical mask around the region of interest, while masking out the large macromolecule using a 3D mask (negative masking), identifies different classes of the mobile protein in the region of interest.","type":"Conclusion"},{"text":"This work highlights that while critical mechanistic insights can be gleaned at the ribosome core of an ensemble of high-resolution structures (Loveland et al., 2017), the same data set does not provide high resolution for a flexible peripheral protein even after exhaustive classification into up to 48 classes.","type":"Conclusion"},{"text":"By contrast, domain 1 (D1), which is connected with the N-terminal helix via a 10-aa linker, is highly dynamic and adopts multiple positions, which differ by up to 50 Å.","type":"Results"},{"text":"While the N-terminal helix is relatively static, the rest of domain 1 is highly dynamic and interacts with S2 in many, but not all, classes.","type":"Conclusion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-11T07:38:36.894Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":180,"end":557,"reference_id":"29247757","reference_source":"pmid","reference_html":"Structural dynamics of protein S1 on the 70S ribosome visualized by ensemble cryo-EM. <i> Loveland AB, Korostelev AA. </i> Methods, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6BU8"},{"db":"EMDB","id":"EMD-7289"}],"region_id":"DP03329r002","statement":[{"text":"Deep classification of cryo-EM data reveals that the N-terminal helix of S1 acts as an anchor (Fig. 2C), whereas the rest of S1 is extremely dynamic (Movie 1).","type":"Results"},{"text":"However, continuous density was visible only in one or two classes and was not of sufficient quality to dock S1 domains. Overall, this unbiased global classification was useful in that it revealed S1 binding site, however the separation of classes occurred on too many different features of the 70S ribosome and the classes did not reveal domain distribution for S1.","type":"Results"},{"text":"We compared four approaches for deep classification of a ribosome dataset to identify conformational states of a highly dynamic protein S1.","type":"Conclusion"},{"text":"In the next step, a spherical mask around the region of interest, while masking out the large macromolecule using a 3D mask (negative masking), identifies different classes of the mobile protein in the region of interest.","type":"Conclusion"},{"text":"This work highlights that while critical mechanistic insights can be gleaned at the ribosome core of an ensemble of high-resolution structures (Loveland et al., 2017), the same data set does not provide high resolution for a flexible peripheral protein even after exhaustive classification into up to 48 classes.","type":"Conclusion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-11T07:38:40.140Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":73,"end":86,"reference_id":"29247757","reference_source":"pmid","reference_html":"Structural dynamics of protein S1 on the 70S ribosome visualized by ensemble cryo-EM. <i> Loveland AB, Korostelev AA. </i> Methods, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"6BU8"},{"db":"EMDB","id":"EMD-7289"}],"region_id":"DP03329r003","statement":[{"text":"While the N-terminal helix is relatively static, the rest of domain 1 is highly dynamic and interacts with S2 in many, but not all, classes.","type":"Conclusion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-25T13:11:22.151Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":194,"end":262,"reference_id":"29247757","reference_source":"pmid","reference_html":"Structural dynamics of protein S1 on the 70S ribosome visualized by ensemble cryo-EM. <i> Loveland AB, Korostelev AA. </i> Methods, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"GO:0003729","term_name":"mRNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"6BU8"},{"db":"EMDB","id":"EMD-7289"}],"region_id":"DP03329r004","statement":[{"text":"To visualize the region that the dynamic domains of S1 sample, we superimposed all the modeled domains from 15 classes (Fig. 5E). This superposition revealed that S1 excursions completely cover the 5′ tail of the mRNA upstream of the Shine-Dalgarno helix, rather than adopting preferred conformations that would leave a well-defined path for mRNA exit. Thus, S1 dynamics likely increases the probability of interactions with various mRNA structures near the mRNA exit, allowing S1 to facilitate mRNA association with the 30S subunit during initiation.","type":"Results"},{"text":" It is possible that the density corresponds to the multiple, interchangeable domains, yielding poor resolution. We have placed D3 in the density on the basis of connectivity with D2, crosslinking of S1 with the 30S subunit (Lauber et al., 2012) and NMR studies that identified the face of S1 domains that interacts with RNA (Aliprandi et al., 2008). One prominent position is near the mRNA tail (Fig. 4A–C). Our finding of one rather than multiple S1 domain bound to the four 5′ mRNA residues is consistent with the observation that S1 domains bind on average 2.5 nucleotides of RNA.","type":"Results"},{"text":"Our cryo-EM maps are also consistent with binding of the C-terminal domains of S1 to the 5′ end of the mRNA and the 3′ end of 16S rRNA at the mRNA exit channel.","type":"Conclusion"},{"text":"The region boundaries are defined by those corresponding to the C-terminal domains of S1.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-11T07:38:30.529Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns.\" [GOC:kmv, GOC:pr, SO:0000234]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":441,"end":557,"reference_id":"30177741","reference_source":"pmid","reference_html":"Structure of a hibernating 100S ribosome reveals an inactive conformation of the ribosomal protein S1. <i> Beckert B, Turk M, Czech A, Berninghausen O, Beckmann R, Ignatova Z, Plitzko JM, Wilson DN. </i> Nat Microbiol, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6H4N"},{"db":"EMDB","id":"EMD-0137"}],"region_id":"DP03329r005","statement":[{"text":"The bS1 protein comprises six structurally related oligosaccharide-oligonucleotide binding (OB-fold) domains (D1–D6), of which we observe cryo-EM density for D1 to D5 in the hibernating 70S (Fig. 3c,d and Supplementary Fig. 5a,b).","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-11T07:38:42.520Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":177,"end":263,"reference_id":"30177741","reference_source":"pmid","reference_html":"Structure of a hibernating 100S ribosome reveals an inactive conformation of the ribosomal protein S1. <i> Beckert B, Turk M, Czech A, Berninghausen O, Beckmann R, Ignatova Z, Plitzko JM, Wilson DN. </i> Nat Microbiol, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6H4N"},{"db":"EMDB","id":"EMD-0137"}],"region_id":"DP03329r006","statement":[{"text":"With the exception of bS1-D3, which was highly flexible and poorly ordered (Supplementary Fig. 5b), molecular models could be unambiguously fitted for D2, D4 and D5 of bS1 (Fig. 3e and Supplementary Fig. 5e–j).","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-25T13:11:15.456Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":6,"released":"2021_12","sequence":"MTESFAQLFEESLKEIETRPGSIVRGVVVAIDKDVVLVDAGLKSESAIPAEQFKNAQGELEIQVGDEVDVALDAVEDGFGETLLSREKAKRHEAWITLEKAYEDAETVTGVINGKVKGGFTVELNGIRAFLPGSLVDVRPVRDTLHLEGKELEFKVIKLDQKRNNVVVSRRAVIESENSAERDQLLENLQEGMEVKGIVKNLTDYGAFVDLGGVDGLLHITDMAWKRVKHPSEIVNVGDEITVKVLKFDRERTRVSLGLKQLGEDPWVAIAKRYPEGTKLTGRVTNLTDYGCFVEIEEGVEGLVHVSEMDWTNKNIHPSKVVNVGDVVEVMVLDIDEERRRISLGLKQCKANPWQQFAETHNKGDRVEGKIKSITDFGIFIGLDGGIDGLVHLSDISWNVAGEEAVREYKKGDEIAAVVLQVDAERERISLGVKQLAEDPFNNWVALNKKGAIVTGKVTAVDAKGATVELADGVEGYLRASEASRDRVEDATLVLSVGDEVEAKFTGVDRKNRAISLSVRAKDEADEKDAIATVNKQEDANFSNNAMAEAFKAAKGE","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":["RNA-binding proteins"],"UniParc":"UPI0000134E23","uniref100":"UniRef100_P0AG69","uniref90":"UniRef90_P0AG69","uniref50":"UniRef50_P0AG69","genes":[{"name":{"value":"rpsA"},"synonyms":[{"value":"ssyF"}],"olnNames":[{"value":"b0911"},{"value":"JW0894"}]}],"alphafold_very_low_content":0.02333931777378815,"disorder_content":0.7091561938958707,"disprot_consensus":{"full":[{"start":73,"end":86,"type":"D"},{"start":177,"end":557,"type":"D"}],"Structural state":[{"start":73,"end":86,"type":"D"},{"start":177,"end":557,"type":"D"}],"Molecular function":[{"start":73,"end":86,"type":"F"},{"start":194,"end":262,"type":"F"}]}},{"disprot_id":"DP03330","acc":"P0A705","creator":"eficho","date":"2021-05-25T16:20:39.548Z","features":{"pfam":[{"id":"PF00009","name":"Elongation factor Tu GTP binding domain","start":393,"end":549},{"id":"PF03144","name":"Elongation factor Tu domain 2","start":810,"end":877},{"id":"PF04760","name":"Translation initiation factor IF-2, N-terminal region","start":1,"end":50},{"id":"PF04760","name":"Translation initiation factor IF-2, N-terminal region","start":314,"end":364},{"id":"PF08364","name":"Bacterial translation initiation factor IF-2 associated region","start":56,"end":94},{"id":"PF11987","name":"Translation-initiation factor 2","start":665,"end":779},{"id":"PF22042","name":"Elongation factor G domain 2","start":565,"end":644}],"gene3D":[]},"length":890,"name":"Translation initiation factor IF-2","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":1,"end":381,"reference_id":"26973877","reference_source":"pmid","reference_html":"Structures of ribosome-bound initiation factor 2 reveal the mechanism of subunit association. <i> Sprink T, Ramrath DJ, Yamamoto H, Yamamoto K, Loerke J, Ismer J, Hildebrand PW, Scheerer P, Bürger J, Mielke T, Spahn CM. </i> Sci Adv, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3JCN"},{"db":"PDB","id":"3JCJ"}],"region_id":"DP03330r001","statement":[{"text":"The IF2 domain IV/ A76-fMet module is linked by flexible regions to the core of IF2 and the body of the tRNA, respectively, to uncouple the motion and to buffer the rotational movement of the 30S subunit. On the IF2 side, a flexible loop connects domain IV that extends from helix 12 of domain III.","type":"Results"},{"text":"The structure of poorly resolved, flexible loops in IF2 was predicted by FragFit, a fragment-based tool for modeling of missing protein segments into cryo-EM density maps (see section below).","type":"Methods"},{"text":"Helix 12 of IF2 fades out into a flexible loop that connects domain III and IV while in eIF5b both domains are connected by a more rigid α-helix explaining the different modes of motion employed for repositioning of the initiator tRNA.","type":"Supplementary material"},{"text":"The same region is also present in the structure with PDB code \"3JCJ\".","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-11T07:36:46.182Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":1,"end":381,"reference_id":"27986852","reference_source":"pmid","reference_html":"Structure of a 30S pre-initiation complex stalled by GE81112 reveals structural parallels in bacterial and eukaryotic protein synthesis initiation pathways. <i> López-Alonso JP, Fabbretti A, Kaminishi T, Iturrioz I, Brandi L, Gil-Carton D, Gualerzi CO, Fucini P, Connell SR. </i> Nucleic Acids Res, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5ME0"},{"db":"PDB","id":"5ME1"},{"db":"EMDB","id":"EMD-3494"}],"region_id":"DP03330r002","statement":[{"text":"In both 30S IC-1 and IC-2 maps, a second larger density (purple density in Figure 1B and E) is located at the entrance to the mRNA channel suitable to account for parts of the N1 and N2 domains which were shown by NMR to consist of a small ordered fold and a larger unstructured region (37).","type":"Results"},{"text":"In panels B–C and E–F the star indicates density that we attribute to the G1 domain of IF2 while the dark purple density located on the back of the subunit near the mRNA entrance channel is attributed to the N1/N2 domain of IF2.","type":"Figure"},{"text":"The same region is also present in the structure with PDB code \"5ME1\".","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-04T12:48:05.188Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":1,"end":294,"reference_id":"39975289","reference_source":"pmid","reference_html":"Bacterial IF2's N-terminal IDR drives cold-induced phase separation and promotes fitness during cold stress. <i> Ghosh A, Mallikaarachchi KS, Dzurik KG, Nandana V, Nunez NR, Childers WS, Schrader JM. </i> bioRxiv, 2025","date":"2025-03-19T17:49:19.683Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1_Ser194del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test the role of the N-terminal IDR on IF2’s observed phase separation, we purified a short form of the E. coli IF2 protein lacking the first 294 amino acids, called IF2ΔNTD."}]}],"ec_go":"IMP","region_id":"DP03330r009","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"Proteins were incubated at a final concentration of 5 μM with E. coli total RNA (5 ng/μL) in a buffer containing 20 mM Tris (pH 7.4), 75 mM KCl, 10 mM MgCl2, and 1 mM DTT."}]}],"statement":[{"text":"We observed IF2ΔNTD showed a notable reduction in IF2 droplets compared to the full length IF2 protein, suggesting the N-terminal IDR promotes IF2 phase separation. We also tested the β-isoform lacking the first 158 amino acids and found that the loss of this region leads to a robust loss in phase separation (Fig S5).","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":9,"released":"2021_12","sequence":"MTDVTIKTLAAERQTSVERLVQQFADAGIRKSADDSVSAQEKQTLIDHLNQKNSGPDKLTLQRKTRSTLNIPGTGGKSKSVQIEVRKKRTFVKRDPQEAERLAAEEQAQREAEEQARREAEESAKREAQQKAEREAAEQAKREAAEQAKREAAEKDKVSNQQDDMTKNAQAEKARREQEAAELKRKAEEEARRKLEEEARRVAEEARRMAEENKWTDNAEPTEDSSDYHVTTSQHARQAEDESDREVEGGRGRGRNAKAARPKKGNKHAESKADREEARAAVRGGKGGKRKGSSLQQGFQKPAQAVNRDVVIGETITVGELANKMAVKGSQVIKAMMKLGAMATINQVIDQETAQLVAEEMGHKVILRRENELEEAVMSDRDTGAAAEPRAPVVTIMGHVDHGKTSLLDYIRSTKVASGEAGGITQHIGAYHVETENGMITFLDTPGHAAFTSMRARGAQATDIVVLVVAADDGVMPQTIEAIQHAKAAQVPVVVAVNKIDKPEADPDRVKNELSQYGILPEEWGGESQFVHVSAKAGTGIDELLDAILLQAEVLELKAVRKGMASGAVIESFLDKGRGPVATVLVREGTLHKGDIVLCGFEYGRVRAMRNELGQEVLEAGPSIPVEILGLSGVPAAGDEVTVVRDEKKAREVALYRQGKFREVKLARQQKSKLENMFANMTEGEVHEVNIVLKADVQGSVEAISDSLLKLSTDEVKVKIIGSGVGGITETDATLAAASNAILVGFNVRADASARKVIEAESLDLRYYSVIYNLIDEVKAAMSGMLSPELKQQIIGLAEVRDVFKSPKFGAIAGCMVTEGVVKRHNPIRVLRDNVVIYEGELESLRRFKDDVNEVRNGMECGIGVKNYNDVRTGDVIEVFEIIEIQRTIA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":[],"UniParc":"UPI000012D2D5","uniref100":"UniRef100_A7ZS65","uniref90":"UniRef90_A7ZS65","uniref50":"UniRef50_Q9ZF31-3","genes":[{"name":{"value":"infB"},"synonyms":[{"value":"gicD"},{"value":"ssyG"}],"olnNames":[{"value":"b3168"},{"value":"JW3137"}]}],"alphafold_very_low_content":0.11910112359550562,"disorder_content":0.4280898876404494,"disprot_consensus":{"full":[{"start":1,"end":381,"type":"D"}],"Structural state":[{"start":1,"end":381,"type":"D"}],"Molecular function":[{"start":1,"end":294,"type":"F"}]}},{"disprot_id":"DP03331","acc":"P0A8N3","creator":"csanchezrocha","date":"2021-05-25T16:35:55.982Z","features":{"pfam":[{"id":"PF00152","name":"tRNA synthetases class II (D, K and N)","start":162,"end":501},{"id":"PF01336","name":"OB-fold nucleic acid binding domain","start":68,"end":146}],"gene3D":[]},"length":505,"name":"Lysine--tRNA ligase","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":445,"end":456,"reference_id":"11041850","reference_source":"pmid","reference_html":"Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding. <i> Onesti S, Desogus G, Brevet A, Chen J, Plateau P, Blanquet S, Brick P. </i> Biochemistry, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1BBW"}],"region_id":"DP03331r001","statement":[{"text":"No electron density is present for the 10 N-terminal amino acids, the 2 C-terminal amino acids, for residue 269 and the regions enclosed between residues 154-160, 215-217, and 444-455.","type":"Methods"},{"text":"The two loops (215-217 and 444-455) which are disordered in the uncomplexed LysS structure are indicated in magenta.","type":"Figure"},{"text":"Whereas in the unliganded enzyme the regions between residues 215-217 and 444-455 are completely disordered, in the lysine-bound structure both segments of polypeptide chain show well-defined electron density.","type":"Results"},{"text":"The two loops that are disordered in the unliganded structure are colored in red. A space filling model of the lysine is shown in yellow. (C) A close up of the active site showing a stereo superposition of the lysine-bound (green) and unliganded (blue) LysS. In the unliganded structure the loops that are disordered (residues 215-218 and 444-455) have been modeled for the sake of clarity and are shown in red.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-04T12:32:23.312Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":445,"end":456,"reference_id":"11041850","reference_source":"pmid","reference_html":"Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding. <i> Onesti S, Desogus G, Brevet A, Chen J, Plateau P, Blanquet S, Brick P. </i> Biochemistry, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1BBU"}],"region_id":"DP03331r002","statement":[{"text":"The two loops (215-217 and 444-455) which are disordered in the uncomplexed LysS structure are indicated in magenta.","type":"Figure"},{"text":"Whereas in the unliganded enzyme the regions between residues 215-217 and 444-455 are completely disordered, in the lysine-bound structure both segments of polypeptide chain show well-defined electron density.","type":"Results"},{"text":"The two loops that are disordered in the unliganded structure are colored in red. A space filling model of the lysine is shown in yellow. (C) A close up of the active site showing a stereo superposition of the lysine-bound (green) and unliganded (blue) LysS. In the unliganded structure the loops that are disordered (residues 215-218 and 444-455) have been modeled for the sake of clarity and are shown in red.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-04T12:32:26.296Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"}],"regions_counter":2,"released":"2021_12","sequence":"MSEQHAQGADAVVDLNNELKTRREKLANLREQGIAFPNDFRRDHTSDQLHAEFDGKENEELEALNIEVAVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDDLPEGVYNEQFKKWDLGDILGAKGKLFKTKTGELSIHCTELRLLTKALRPLPDKFHGLQDQEARYRQRYLDLISNDESRNTFKVRSQILSGIRQFMVNRGFMEVETPMMQVIPGGAAARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYKDLIELTESLFRTLAQDILGKTEVTYGDVTLDFGKPFEKLTMREAIKKYRPETDMADLDNFDSAKAIAESIGIHVEKSWGLGRIVTEIFEEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIGGREIGNGFSELNDAEDQAQRFLDQVAAKDAGDDEAMFYDEDYVTALEHGLPPTAGLGIGIDRMVMLFTNSHTIRDVILFPAMRPVK","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":[],"UniParc":"UPI000011083E","uniref100":"UniRef100_P0A8N4","uniref90":"UniRef90_P28354","uniref50":"UniRef50_P28354","genes":[{"name":{"value":"lysS"},"synonyms":[{"value":"asuD"},{"value":"herC"}],"olnNames":[{"value":"b2890"},{"value":"JW2858"}]}],"alphafold_very_low_content":0.011881188118811881,"disorder_content":0.023762376237623763,"disprot_consensus":{"full":[{"start":445,"end":456,"type":"T"}],"Structural state":[{"start":445,"end":456,"type":"D"}],"Structural transition":[{"start":445,"end":456,"type":"T"}]}},{"disprot_id":"DP03332","acc":"P0A3B2","creator":"csanchezrocha","date":"2021-05-25T16:44:13.160Z","features":{"pfam":[{"id":"PF00009","name":"Elongation factor Tu GTP binding domain","start":4,"end":195},{"id":"PF00679","name":"Elongation factor G C-terminus","start":397,"end":477},{"id":"PF03144","name":"Elongation factor Tu domain 2","start":219,"end":289},{"id":"PF21018","name":"TypA/BipA C-terminal domain","start":485,"end":593}],"gene3D":[]},"length":607,"name":"50S ribosomal subunit assembly factor BipA","ncbi_taxon_id":574521,"organism":"Escherichia coli O127:H6 (strain E2348/69 / EPEC)","regions":[{"start":32,"end":55,"reference_id":"26163516","reference_source":"pmid","reference_html":"Structural and Functional Analysis of BipA, a Regulator of Virulence in Enteropathogenic Escherichia coli. <i> Fan H, Hahm J, Diggs S, Perry JJP, Blaha G. </i> J Biol Chem, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4ZCI"}],"region_id":"DP03332r001","statement":[{"text":"Disordered regions are indicated with dashed lines. B, sequence alignment of EF-G, LepA, BipA, and C-terminal fragment of BipA with domains color-coded as in A. Residue number below the sequence indicates residue N-terminal to the boundary between domains. The beginning and end of disordered regions are indicated with the residue number of the last ordered residue on the top of the sequence. Disordered regions are displayed as an array of thin boxes.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-07T07:37:15.005Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":540,"end":555,"reference_id":"26163516","reference_source":"pmid","reference_html":"Structural and Functional Analysis of BipA, a Regulator of Virulence in Enteropathogenic Escherichia coli. <i> Fan H, Hahm J, Diggs S, Perry JJP, Blaha G. </i> J Biol Chem, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4ZCI"}],"region_id":"DP03332r002","statement":[{"text":"Disordered regions are indicated with dashed lines. B, sequence alignment of EF-G, LepA, BipA, and C-terminal fragment of BipA with domains color-coded as in A. Residue number below the sequence indicates residue N-terminal to the boundary between domains. The beginning and end of disordered regions are indicated with the residue number of the last ordered residue on the top of the sequence. Disordered regions are displayed as an array of thin boxes.","type":"Figure"},{"text":" A long, polar region (residues 540 –555) that extends from the distal end of the C-terminal domain is disordered in the crystal structure.","type":"Results"},{"text":"To evaluate the significance of the bound cations and to resolve the long, disordered, polar region, we set out to crystallize a C-terminal fragment of BipA consisting of domains III and V and the C-terminal domain in the presence of magnesium ions (Fig. 2A).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-04T12:37:00.579Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":32,"end":55,"reference_id":"26163516","reference_source":"pmid","reference_html":"Structural and Functional Analysis of BipA, a Regulator of Virulence in Enteropathogenic Escherichia coli. <i> Fan H, Hahm J, Diggs S, Perry JJP, Blaha G. </i> J Biol Chem, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4ZCL"}],"region_id":"DP03332r003","statement":[{"text":"The “switch 1” region of BipA (residues 42–65), whose position is affected by the γ-phosphate of GTP in other GTPases, is disordered.","type":"Results"},{"text":"The IDR characterized in the publication with residues 42-65, corresponds to region 32-55 of the amino acid sequence.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-04T15:27:56.724Z"}},{"start":540,"end":555,"reference_id":"26163516","reference_source":"pmid","reference_html":"Structural and Functional Analysis of BipA, a Regulator of Virulence in Enteropathogenic Escherichia coli. <i> Fan H, Hahm J, Diggs S, Perry JJP, Blaha G. </i> J Biol Chem, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4ZCK"}],"region_id":"DP03332r004","statement":[{"text":"In addition, nearly all of the long, basic, disordered region is now structured, and the position of the [Co(NH3 )6 ]3+ ion in the full-length protein structure has been replaced by two proximal magnesium ions.","type":"Results"},{"text":"This evidence comes from a protein fragment.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-04T12:38:44.813Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":32,"end":47,"reference_id":"26283392","reference_source":"pmid","reference_html":"Structure of BipA in GTP form bound to the ratcheted ribosome. <i> Kumar V, Chen Y, Ero R, Ahmed T, Tan J, Li Z, Wong AS, Bhushan S, Gao YG. </i> Proc Natl Acad Sci U S A, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5A9W"}],"region_id":"DP03332r005","statement":[{"text":"The switch I region of BipA, which was disordered in all of the isolated structures as mentioned above, can be visualized in the presence of the ribosome (Fig. S3D), allowing us to explore the structural basis of GTPase activation by BipA.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-04T12:36:39.882Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":32,"end":47,"reference_id":"26283392","reference_source":"pmid","reference_html":"Structure of BipA in GTP form bound to the ratcheted ribosome. <i> Kumar V, Chen Y, Ero R, Ahmed T, Tan J, Li Z, Wong AS, Bhushan S, Gao YG. </i> Proc Natl Acad Sci U S A, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5A9Z"}],"region_id":"DP03332r006","statement":[{"text":"The switch I region of BipA, which was disordered in all of the isolated structures as mentioned above, can be visualized in the presence of the ribosome (Fig. S3D), allowing us to explore the structural basis of GTPase activation by BipA.","type":"Results"},{"text":"The switch I region of BipA is ordered upon binding to ribosome. In addition to interacting with the GTP analog (GDPCP), the switch I region (Phe32 and Asp33) is stabilized by bilateral contacts with the SRL of the 50S subunit and h8 of the 30S subunit (Fig. 3B), resulting in an ordered structure.","type":"Supplementary material"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-04T12:38:24.164Z"},"ec_go":"IDA","disprot_namespace":"Structural transition"}],"regions_counter":6,"released":"2021_12","sequence":"MIEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSEGKTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPTVSMFFCVNTSPFCGKEGKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIFREIDGRKQEPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVRPGEVGQRQNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEAVVLVPPIRMTLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRRRANRAPKDD","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":["RNA-binding proteins","Bacterial virulence-related proteins"],"UniParc":"UPI000013788D","uniref100":"UniRef100_P0A3B2","uniref90":"UniRef90_H9L427","uniref50":"UniRef50_H9L427","genes":[{"name":{"value":"bipA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00849","url":"https://hamap.expasy.org/unirule/MF_00849"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"9622352","url":"http://www.ncbi.nlm.nih.gov/pubmed/9622352","alternativeUrl":"https://europepmc.org/abstract/MED/9622352"}}]},"synonyms":[{"value":"o591","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9642082","url":"http://www.ncbi.nlm.nih.gov/pubmed/9642082","alternativeUrl":"https://europepmc.org/abstract/MED/9642082"}}]},{"value":"typA","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9642082","url":"http://www.ncbi.nlm.nih.gov/pubmed/9642082","alternativeUrl":"https://europepmc.org/abstract/MED/9642082"}}]}],"olnNames":[{"value":"E2348C_4177"}]}],"alphafold_very_low_content":0.042833607907743,"disorder_content":0.06589785831960461,"disprot_consensus":{"full":[{"start":32,"end":47,"type":"T"},{"start":48,"end":55,"type":"D"},{"start":540,"end":555,"type":"T"}],"Structural state":[{"start":32,"end":55,"type":"D"},{"start":540,"end":555,"type":"D"}],"Structural transition":[{"start":32,"end":47,"type":"T"},{"start":540,"end":555,"type":"T"}]}},{"disprot_id":"DP03333","acc":"P0AFF6","creator":"csanchezrocha","date":"2021-05-25T19:08:48.970Z","features":{"pfam":[{"id":"PF00575","name":"S1 RNA binding domain","start":134,"end":195},{"id":"PF08529","name":"NusA N-terminal domain","start":4,"end":123},{"id":"PF13184","name":"NusA-like first KH domain","start":199,"end":276},{"id":"PF14520","name":"SAM-like Helix-hairpin-helix tandem","start":432,"end":486},{"id":"PF26594","name":"NusA-like second KH domain","start":280,"end":343}],"gene3D":[]},"length":495,"name":"Transcription termination/antitermination protein NusA","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":201,"end":495,"reference_id":"33296676","reference_source":"pmid","reference_html":"Pre-termination Transcription Complex: Structure and Function. <i> Hao Z, Epshtein V, Kim KH, Proshkin S, Svetlov V, Kamarthapu V, Bharati B, Mironov A, Walz T, Nudler E. </i> Mol Cell, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6XAS"},{"db":"EMDB","id":"EMD-22114"}],"region_id":"DP03333r001","statement":[{"text":"We observed clear density for the first 200 residues of NusA in the PTC60 map (Figures 2A and S4B); the more flexible NusA-CTD was not resolved.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-04T12:49:11.921Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":201,"end":495,"reference_id":"32871103","reference_source":"pmid","reference_html":"Structure-Based Mechanisms of a Molecular RNA Polymerase/Chaperone Machine Required for Ribosome Biosynthesis. <i> Huang YH, Hilal T, Loll B, Bürger J, Mielke T, Böttcher C, Said N, Wahl MC. </i> Mol Cell, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6TQO"},{"db":"EMDB","id":"EMD-10548"}],"region_id":"DP03333r002","statement":[{"text":"The region characterized as unfolded was folded upon interaction.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-22T12:40:36.254Z"},"ec_go":"IDA","disprot_namespace":"Structural transition"},{"start":201,"end":425,"reference_id":"28452979","reference_source":"pmid","reference_html":"Structural basis for λN-dependent processive transcription antitermination. <i> Said N, Krupp F, Anedchenko E, Santos KF, Dybkov O, Huang YH, Lee CT, Loll B, Behrmann E, Bürger J, Mielke T, Loerke J, Urlaub H, Spahn CMT, Weber G, Wahl MC. </i> Nat Microbiol, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"csanchezrocha","curator_name":"Alma Carolina Sanchez Rocha","curator_orcid":"0000-0001-7395-9173","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5MS0"},{"db":"EMDB","id":"EMD-3561"}],"region_id":"DP03333r003","statement":[{"text":"The region characterized as unfolded was folded upon interaction.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-22T12:40:35.364Z"},"ec_go":"IDA","disprot_namespace":"Structural transition"}],"regions_counter":3,"released":"2021_12","sequence":"MNKEILAVVEAVSNEKALPREKIFEALESALATATKKKYEQEIDVRVQIDRKSGDFDTFRRWLVVDEVTQPTKEITLEAARYEDESLNLGDYVEDQIESVTFDRITTQTAKQVIVQKVREAERAMVVDQFREHEGEIITGVVKKVNRDNISLDLGNNAEAVILREDMLPRENFRPGDRVRGVLYSVRPEARGAQLFVTRSKPEMLIELFRIEVPEIGEEVIEIKAAARDPGSRAKIAVKTNDKRIDPVGACVGMRGARVQAVSTELGGERIDIVLWDDNPAQFVINAMAPADVASIVVDEDKHTMDIAVEAGNLAQAIGRNGQNVRLASQLSGWELNVMTVDDLQAKHQAEAHAAIDTFTKYLDIDEDFATVLVEEGFSTLEELAYVPMKELLEIEGLDEPTVEALRERAKNALATIAQAQEESLGDNKPADDLLNLEGVDRDLAFKLAARGVCTLEDLAEQGIDDLADIEGLTDEKAGALIMAARNICWFGDEA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":["Condensates-related proteins","RNA-binding proteins","Stress response proteins"],"UniParc":"UPI0000130A38","uniref100":"UniRef100_P0AFF8","uniref90":"UniRef90_P0AFF8","uniref50":"UniRef50_P37430","genes":[{"name":{"value":"nusA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00945","url":"https://hamap.expasy.org/unirule/MF_00945"}}]},"olnNames":[{"value":"b3169"},{"value":"JW3138"}]}],"alphafold_very_low_content":0.006060606060606061,"disorder_content":0.5959595959595959,"disprot_consensus":{"full":[{"start":201,"end":495,"type":"T"}],"Structural state":[{"start":201,"end":495,"type":"D"}],"Structural transition":[{"start":201,"end":495,"type":"T"}]}},{"disprot_id":"DP03334","acc":"P90947","creator":"spenadias","date":"2021-05-26T09:00:30.866Z","features":{"pfam":[{"id":"PF01044","name":"Vinculin family","start":15,"end":869}],"gene3D":[]},"length":927,"name":"Alpha-catenin-like protein hmp-1","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":527,"end":537,"reference_id":"28298447","reference_source":"pmid","reference_html":"Structural and functional characterization of <i>Caenorhabditis elegans</i> α-catenin reveals constitutive binding to β-catenin and F-actin. <i> Kang H, Bang I, Jin KS, Lee B, Lee J, Shao X, Heier JA, Kwiatkowski AV, Nelson WJ, Hardin J, Weis WI, Choi HJ. </i> J Biol Chem, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"5H5M"}],"region_id":"DP03334r001","statement":[{"text":"The italicized residues are not visible in the structure","type":"Figure"},{"text":"Several cycles of refinement with PHENIX (32) and manual rebuilding with COOT (33) were run to generate the final model, which consists of one copy with residues 270–352,356–526, and 538–641 and the other with residues 270–347,355–526, 540–606, and 609–640","type":"Methods"},{"text":"Italicized residues on hrmp-1 sequence corresponds to residues 527-537 of Uniprot sequence","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-26T12:22:07.129Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_12","sequence":"MPANGNSHAYFNIDEVRSKNVLKQITQLINEVTNITETFPLKPGQTTEGLVATLDAAVANFLQTGSFAISKCPIANSDPRAIDLLHEALGAVQDTGQVMIQTGRDFVRDSTSTNKRAIATNSGRNLLTAVAKFLILADSIDVKVIVDKVDEVRETAHQMIEADTKIKVDDLYNLLISQIEELDITVRRRAIDLVKPNQRDDLLAARSALRQTAPLLYTSTRTFVRHPEHEEARRNRDYTADEMHSALNALESVLNGQQPKVTFSEYGRIGDLINEIDTFQNRIEIDPAHYRRGTDRPDLEGHCERIVSGSASIADAESTRENRKQKIVAECNNLRQALQELLTEYEKSTGRRDDNDDIPLGIAEVHKRTKDLRRHLRRAIVDHISDAFLDTRTPLILLIEAAKEGHEENTRYRSKMFQEHANEIVSVARLSCQLSSDVESVSVIQHTAAQLEKLAPQVAQAAILLCHQPTSKTAQENMETYKNAWFDKVRLLTTALDNITTLDDFLAVSEAHIVEDCERGIKGITANASTPDENAANCETVDCAAGSIRGRALRVCDVVDAEMDFLQNSEYTETVKQAVRILKTQRVDQFAERASALANRQEAHGLTWDPKTKEEEMNEFINACTLVHDAVKDIRHALLMNRSMNDVDSDVEYEADGVGAANADANRTISEQENQQNLMRRLPEEEKKKIQAQIDIFKVTQTRFEREVAKWDETGNDIISLANNMCKIMMSMTEFTRGCGPLKTTMDVIRAAQEISLNGSKLNALARQIGEESADSQTKKDLLAYLSQITLYCQQLNICSKVKADVTQVGNELVVSALDSAMSLIQTARNLLTAVVQTVKAAYIASTKFRRPNANSVRVEWRMAPPKKQPLIRPQKNNAIIRRASERRPLQPAKVLAEFTRNEIETGRDSDDEELDRRHQQRINGRL","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"dataset":[],"UniParc":"UPI0000077DB1","uniref100":"UniRef100_P90947","uniref90":"UniRef90_P90947","uniref50":"UniRef50_P90947","genes":[{"name":{"value":"hmp-1"},"orfNames":[{"value":"R13H4.4"}]}],"alphafold_very_low_content":0.09600862998921252,"disorder_content":0.011866235167206042,"disprot_consensus":{"full":[{"start":527,"end":537,"type":"D"}],"Structural state":[{"start":527,"end":537,"type":"D"}]}},{"disprot_id":"DP03335","acc":"P42573","creator":"spenadias","date":"2021-05-26T09:03:33.191Z","features":{"pfam":[{"id":"PF00619","name":"Caspase recruitment domain","start":8,"end":89},{"id":"PF00656","name":"Caspase domain","start":242,"end":493}],"gene3D":[]},"length":503,"name":"Cell death protein 3","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":370,"end":406,"reference_id":"24065769","reference_source":"pmid","reference_html":"Mechanistic insights into CED-4-mediated activation of CED-3. <i> Huang W, Jiang T, Choi W, Qi S, Pang Y, Hu Q, Xu Y, Gong X, Jeffrey PD, Wang J, Shi Y. </i> Genes Dev, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"spenadias","curator_name":"Samuel Peña Díaz","curator_orcid":"0000-0002-2902-823X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4M9R"}],"region_id":"DP03335r001","statement":[{"text":"In contrast, the active site in the adjacent CED-3 molecule does not have a well-defined conformation, with the L2 loop largely disordered in the crystals'","type":"Results"},{"text":"L2 loop is located in 370-406 region","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-26T12:22:49.751Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_06","sequence":"MMRQDRRSLLERNIMMFSSHLKVDEILEVLIAKQVLNSDNGDMINSCGTVREKRREIVKAVQRRGDVAFDAFYDALRSTGHEGLAEVLEPLARSVDSNAVEFECPMSPASHRRSRALSPAGYTSPTRVHRDSVSSVSSFTSYQDIYSRARSRSRSRALHSSDRHNYSSPPVNAFPSQPSSANSSFTGCSSLGYSSSRNRSFSKASGPTQYIFHEEDMNFVDAPTISRVFDEKTMYRNFSSPRGMCLIINNEHFEQMPTRNGTKADKDNLTNLFRCMGYTVICKDNLTGRGMLLTIRDFAKHESHGDSAILVILSHGEENVIIGVDDIPISTHEIYDLLNAANAPRLANKPKIVFVQACRGERRDNGFPVLDSVDGVPAFLRRGWDNRDGPLFNFLGCVRPQVQQVWRKKPSQADILIAYATTAQYVSWRNSARGSWFIQAVCEVFSTHAKDMDVVELLTEVNKKVACGFQTSQGSNILKQMPEMTSRLLKKFYFWPEARNSAV","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"dataset":[],"UniParc":"UPI000014D795","uniref100":"UniRef100_P42573","uniref90":"UniRef90_P42573","uniref50":"UniRef50_P42573","genes":[{"name":{"value":"ced-3","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"C48D1.2a","url":"https://www.wormbase.org/db/seq/sequence?name=C48D1.2a;class=Transcript"}}]},"orfNames":[{"value":"C48D1.2","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"C48D1.2a","url":"https://www.wormbase.org/db/seq/sequence?name=C48D1.2a;class=Transcript"}}]}]}],"alphafold_very_low_content":0.2982107355864811,"disorder_content":0.073558648111332,"disprot_consensus":{"full":[{"start":370,"end":406,"type":"D"}],"Structural state":[{"start":370,"end":406,"type":"D"}]}},{"disprot_id":"DP03336","acc":"P12996","creator":"jnilsson","date":"2021-05-27T08:46:25.414Z","features":{"pfam":[{"id":"PF04055","name":"Radical SAM superfamily","start":49,"end":205},{"id":"PF06968","name":"Biotin and Thiamin Synthesis associated domain","start":220,"end":311}],"gene3D":[]},"length":346,"name":"Biotin synthase","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":316,"end":346,"reference_id":"14704425","reference_source":"pmid","reference_html":"Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme. <i> Berkovitch F, Nicolet Y, Wan JT, Jarrett JT, Drennan CL. </i> Science, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1R30"}],"region_id":"DP03336r001","statement":[{"text":"The structure of BioB has been determined to 3.4 Å resolution by iron multi-wavelength anomalous dispersion (MAD) techniques (21). The fold of each subunit of the BioB dimer is a triosephosphate isomerase (TIM) type (α/β)8 barrel, with two additional helices at the N terminus and a disordered region at the C terminus (Fig. 1).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-28T08:13:25.047Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MAHRPRWTLSQVTELFEKPLLDLLFEAQQVHRQHFDPRQVQVSTLLSIKTGACPEDCKYCPQSSRYKTGLEAERLMEVEQVLESARKAKAAGSTRFCMGAAWKNPHERDMPYLEQMVQGVKAMGLEACMTLGTLSESQAQRLANAGLDYYNHNLDTSPEFYGNIITTRTYQERLDTLEKVRDAGIKVCSGGIVGLGETVKDRAGLLLQLANLPTPPESVPINMLVKVKGTPLADNDDVDAFDFIRTIAVARIMMPTSYVRLSAGREQMNEQTQAMCFMAGANSIFYGCKLLTTPNPEEDKDLQLFRKLGLNPQQTAVLAGDNEQQQRLEQALMTPDTDEYYNAAAL","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":[],"UniParc":"UPI0000149190","uniref100":"UniRef100_A7ZJI4","uniref90":"UniRef90_Q8X825","uniref50":"UniRef50_A9C2R2","genes":[{"name":{"value":"bioB"},"olnNames":[{"value":"b0775"},{"value":"JW0758"}]}],"alphafold_very_low_content":0.031791907514450865,"disorder_content":0.08959537572254335,"disprot_consensus":{"full":[{"start":316,"end":346,"type":"D"}],"Structural state":[{"start":316,"end":346,"type":"D"}]}},{"disprot_id":"DP03337","acc":"P0A9H7","creator":"jnilsson","date":"2021-05-27T09:57:00.971Z","features":{"pfam":[{"id":"PF02353","name":"Mycolic acid cyclopropane synthetase","start":108,"end":368}],"gene3D":[]},"length":382,"name":"Cyclopropane-fatty-acyl-phospholipid synthase","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":2,"end":13,"reference_id":"30057024","reference_source":"pmid","reference_html":"Structural and Functional Analysis of E. coli Cyclopropane Fatty Acid Synthase. <i> Hari SB, Grant RA, Sauer RT. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6BQC"}],"region_id":"DP03337r001","statement":[{"text":"The first 13 residues of the N-domain were disordered, as were residues from 100 to 120, which comprise a linker to the C-domain.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-28T08:16:45.907Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":100,"end":120,"reference_id":"30057024","reference_source":"pmid","reference_html":"Structural and Functional Analysis of E. coli Cyclopropane Fatty Acid Synthase. <i> Hari SB, Grant RA, Sauer RT. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6BQC"}],"region_id":"DP03337r002","statement":[{"text":"The first 13 residues of the N-domain were disordered, as were residues from 100 to 120, which comprise a linker to the C-domain.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-28T08:17:29.706Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":100,"end":120,"reference_id":"30057024","reference_source":"pmid","reference_html":"Structural and Functional Analysis of E. coli Cyclopropane Fatty Acid Synthase. <i> Hari SB, Grant RA, Sauer RT. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03337r003","statement":[{"text":"The linker (100-120 aa) connects N- and C-domains.","type":"Curator statement"},{"text":"Digestion of CFA synthase with a low concentration of trypsin\nresulted in two major polypeptide fragments (Figure 3B, inset).\nAnalysis by sequential Edman degradation showed that cleavage\noccurs between Arg111 and Ala112, in the linker between\nthe N- and C-domains. Following tryptic cleavage, the N- and\nC-terminal fragments remained associated during gel-filtration\nchromatography (Figure 3B).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-26T14:35:32.147Z"},"ec_go":"IDA","disprot_namespace":"Disorder function"},{"start":100,"end":120,"reference_id":"30057024","reference_source":"pmid","reference_html":"Structural and Functional Analysis of E. coli Cyclopropane Fatty Acid Synthase. <i> Hari SB, Grant RA, Sauer RT. </i> Structure, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"6BQC"}],"region_id":"DP03337r004","statement":[{"text":"The first 13 residues of the N-domain were disordered, as were residues from 100 to 120, which comprise a linker to the C-domain.","type":"Results"},{"text":"The interface between the N- and C-domains is formed by an\nextensive network of contacts between the a3 and a4 helices of\nthe N-domain and the a14 and a18 helices of the C-domain\n(Figure 2C). The surface buried in this interface was calculated\nto be 1,800 A°2 (Fraczkiewicz and Braun, 1998), representing\n34% of the total surface area of the N-domain. A linker must\nconnect residue 99 in the N-domain with residue 121 in the\nC-domain, a distance of \u000130 A°. However, electron density was\neither poor or absent for these linker residues, suggesting that\nthey adopt multiple conformations.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-26T14:35:30.812Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":4,"released":"2021_12","sequence":"MSSSCIEEVSVPDDNWYRIANELLSRAGIAINGSAPADIRVKNPDFFKRVLQEGSLGLGESYMDGWWECDRLDMFFSKVLRAGLENQLPHHFKDTLRIAGARLFNLQSKKRAWIVGKEHYDLGNDLFSRMLDPFMQYSCAYWKDADNLESAQQAKLKMICEKLQLKPGMRVLDIGCGWGGLAHYMASNYDVSVVGVTISAEQQKMAQERCEGLDVTILLQDYRDLNDQFDRIVSVGMFEHVGPKNYDTYFAVVDRNLKPEGIFLLHTIGSKKTDLNVDPWINKYIFPNGCLPSVRQIAQSSEPHFVMEDWHNFGADYDTTLMAWYERFLAAWPEIADNYSERFKRMFTYYLNACAGAFRARDIQLWQVVFSRGVENGLRVAR","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":[],"UniParc":"UPI0000167DB0","uniref100":"UniRef100_P0A9H8","uniref90":"UniRef90_P0A9H8","uniref50":"UniRef50_P0A9H8","genes":[{"name":{"value":"cfa"},"synonyms":[{"value":"cdfA"}],"olnNames":[{"value":"b1661"},{"value":"JW1653"}]}],"alphafold_very_low_content":0.01832460732984293,"disorder_content":0.08638743455497382,"disprot_consensus":{"full":[{"start":2,"end":13,"type":"D"},{"start":100,"end":120,"type":"D"}],"Structural state":[{"start":2,"end":13,"type":"D"},{"start":100,"end":120,"type":"D"}],"Disorder function":[{"start":100,"end":120,"type":"F"}]}},{"disprot_id":"DP03338","acc":"Q9A8N4","creator":"jssuarez","date":"2021-05-27T10:19:14.220Z","features":{"pfam":[{"id":"PF10691","name":"Protein of unknown function (DUF2497)","start":105,"end":173}],"gene3D":[]},"length":177,"name":"PopZ","ncbi_taxon_id":190650,"organism":"Caulobacter vibrioides (strain ATCC 19089 / CB15)","regions":[{"start":1,"end":133,"reference_id":"33058876","reference_source":"pmid","reference_html":"Intrinsically Disordered Bacterial Polar Organizing Protein Z, PopZ, Interacts with Protein Binding Partners Through an N-terminal Molecular Recognition Feature. <i> Nordyke CT, Ahmed YM, Puterbaugh RZ, Bowman GR, Varga K. </i> J Mol Biol, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6XRY"}],"region_id":"DP03338r001","statement":[{"text":"The intrinsic disorder of PopZΔ134–177 is shown by the 2D 1H-15N HSQC spectrum with the characteristic narrow 1H chemical shift dispersion typically seen for IDPs (Figure S1), with the exception of sidechain amine and amide resonances from arginine and glutamine residues, respectively. Comparatively, ordered proteins tend to have a wider dispersion of 1H resonances than proteins without a well-defined fold.49 The disordered nature of PopZΔ134–177 is further supported by the distinct lack of abundance of long-range interactions in 1H-15N NOESY data. ","type":"Results"},{"text":"The 20 predicted structures show no other well folded secondary structure elements besides an N-terminal α-helix (M10-I17) (Figure 2).","type":"Results"},{"text":"PopZ (1-133) is globally unstructured but retains a short helical motif between residues (M10-I17) according to NMR data.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-28T09:51:54.249Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":133,"reference_id":"27791060","reference_source":"pmid","reference_html":"Caulobacter PopZ forms an intrinsically disordered hub in organizing bacterial cell poles. <i> Holmes JA, Follett SE, Wang H, Meadows CP, Varga K, Bowman GR. </i> Proc Natl Acad Sci U S A, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP03338r002","statement":[{"text":"To determine the extent of structural disorder in this region of PopZ experimentally, we purified the PopZΔ134–177 fragment and analyzed it using solution NMR spectroscopy and circular dichroism. The 2D 1H-15N heteronuclear single quantum correlation (HSQC) spectrum (Fig. 5C, red signal, and SI Appendix, Fig. S7) shows well-defined peaks with roughly uniform intensities and line shapes for the majority of resonances. Notably, all the backbone proton peaks were clustered in the 7.80–8.85-ppm region. This narrow dispersion of proton chemical shifts is a strong indicator of an intrinsically disordered protein, compared with well-ordered proteins, which exhibit more broadly distributed peaks in the proton dimension (21).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-28T09:55:59.970Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":133,"reference_id":"27791060","reference_source":"pmid","reference_html":"Caulobacter PopZ forms an intrinsically disordered hub in organizing bacterial cell poles. <i> Holmes JA, Follett SE, Wang H, Meadows CP, Varga K, Bowman GR. </i> Proc Natl Acad Sci U S A, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP03338r003","statement":[{"text":"Circular dichroism analysis suggests that PopZ∆134–177 is mostly composed of random coil (Fig. 5B), providing further evidence of structural disorder.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-28T09:56:05.859Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":9,"end":23,"reference_id":"33058876","reference_source":"pmid","reference_html":"Intrinsically Disordered Bacterial Polar Organizing Protein Z, PopZ, Interacts with Protein Binding Partners Through an N-terminal Molecular Recognition Feature. <i> Nordyke CT, Ahmed YM, Puterbaugh RZ, Bowman GR, Varga K. </i> J Mol Biol, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03338r004","statement":[{"text":"Binding residues were determined by comparing combined ΔHN chemical shifts for each\nresidue, where peaks undergoing a shift greater than the standard deviation were considered\nbinding [63]. Combined ΔHN chemical shift perturbations (Figure 3(C)) and peak intensity perturbations (Figure S7) of PopZΔ134-177 upon binding to RcdA reveals that the binding motif of PopZΔ134-177 is between T9-E23 (Figures 4 and S8), as peaks corresponding to these residues undergo both significant chemical shift perturbations and line broadening most likely due to direct interaction with RcdA, although potential secondary structure changes cannot be excluded.","type":"Results"},{"text":"We therefore conclude that residues T9-E23, which include an α-helix that spans M10-I17, act as a MoRF region that is directly responsible for interacting with at least two of its 15 binding partners.","type":"Results"}],"ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":9,"end":23,"reference_id":"33058876","reference_source":"pmid","reference_html":"Intrinsically Disordered Bacterial Polar Organizing Protein Z, PopZ, Interacts with Protein Binding Partners Through an N-terminal Molecular Recognition Feature. <i> Nordyke CT, Ahmed YM, Puterbaugh RZ, Bowman GR, Varga K. </i> J Mol Biol, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"Q9A3A9","partner_start":null,"partner_end":null}],"region_id":"DP03338r005","statement":[{"text":"Combined ΔHN chemical shift perturbations (Figure 3(C)) and peak intensity perturbations (Figure S7) of PopZΔ134-177 upon binding to RcdA reveals that the binding motif of PopZΔ134-177 is between T9-E23 (Figures 4 and S8), as peaks corresponding to these residues undergo both significant chemical shift perturbations and line broadening most likely due to direct interaction with RcdA, although potential secondary structure changes cannot be excluded.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-28T09:52:30.973Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":133,"reference_id":"27791060","reference_source":"pmid","reference_html":"Caulobacter PopZ forms an intrinsically disordered hub in organizing bacterial cell poles. <i> Holmes JA, Follett SE, Wang H, Meadows CP, Varga K, Bowman GR. </i> Proc Natl Acad Sci U S A, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"Q9A3A9","partner_start":null,"partner_end":null},{"db":"UniProt","id":"A6H916","partner_start":null,"partner_end":null}],"region_id":"DP03338r006","statement":[{"text":"To ask whether the structure of PopZ is affected by interaction with another protein, we repeated our NMR analysis on isotopically labeled PopZΔ134–177, after mixing with RcdA, ChpT, or a noninteracting control protein (Fig. 5C). Whereas the addition of the control protein had little effect on the spectra, the addition of RcdA or ChpT induced significant changes in some of the peaks. Notably, mixing with RcdA or ChpT affected the same set of resonances, suggesting these proteins interact with the same amino acids in PopZΔ134–177. Future analyses will determine whether the affected amino acids are in the N-terminal MoRF-like region, and whether this sequence adopts helical structure on binding","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-28T09:57:00.904Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":133,"reference_id":"27791060","reference_source":"pmid","reference_html":"Caulobacter PopZ forms an intrinsically disordered hub in organizing bacterial cell poles. <i> Holmes JA, Follett SE, Wang H, Meadows CP, Varga K, Bowman GR. </i> Proc Natl Acad Sci U S A, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03338r007","statement":[{"text":"To ask whether the structure of PopZ is affected by interaction with another protein, we repeated our NMR analysis on isotopically labeled PopZΔ134–177, after mixing with RcdA, ChpT, or a noninteracting control protein (Fig. 5C). Whereas the addition of the control protein had little effect on the spectra, the addition of RcdA or ChpT induced significant changes in some of the peaks. Notably, mixing with RcdA or ChpT affected the same set of resonances, suggesting these proteins interact with the same amino acids in PopZΔ134–177. Future analyses will determine whether the affected amino acids are in the N-terminal MoRF-like region, and whether this sequence adopts helical structure on binding","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-28T09:57:41.752Z"},"ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":133,"reference_id":"33058876","reference_source":"pmid","reference_html":"Intrinsically Disordered Bacterial Polar Organizing Protein Z, PopZ, Interacts with Protein Binding Partners Through an N-terminal Molecular Recognition Feature. <i> Nordyke CT, Ahmed YM, Puterbaugh RZ, Bowman GR, Varga K. </i> J Mol Biol, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03338r008","statement":[{"text":"The polar organizing protein Z, PopZ, of Caulobacter functions as a hub protein.","type":"Article"},{"text":"The polar organizing protein Z (PopZ) is necessary for the formation of three-dimensional\nmicrodomains at the cell poles in Caulobacter crescentus, where it functions as a hub protein\nthat recruits multiple regulatory proteins from the cytoplasm.","type":"Abstract"},{"text":"Here, RcdA was produced as a fusion protein with\ngreen fluorescent protein (RcdA-GFP) and co-expressed with either full-length wildtype PopZ or\nthe full-length I17A mutant (each produced as fusions with mCherry for visualization by\nfluorescence microscopy). Due to the presence of the C-terminal self-assembly domain in fulllength PopZ, both of the PopZ variants accumulated at the cell poles of the bacteria [39].. RcdAGFP exhibited strong co-localization with wildtype PopZ, but much weaker co-localization with\nthe I17A mutant, confirming the interaction defect","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Disorder function"},{"start":1,"end":133,"reference_id":"27791060","reference_source":"pmid","reference_html":"Caulobacter PopZ forms an intrinsically disordered hub in organizing bacterial cell poles. <i> Holmes JA, Follett SE, Wang H, Meadows CP, Varga K, Bowman GR. </i> Proc Natl Acad Sci U S A, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03338r009","statement":[{"text":"Caulobacter PopZ forms an intrinsically disordered hub in organizing bacterial cell poles.","type":"Title"},{"text":"We used Escherichia coli cells to screen a pool of candidate proteins for the ability to interact with Caulobacter PopZ (Fig. 1 A–C). This was possible because PopZ self-assembles into macromolecular complexes that accumulate at E. coli cell poles (16), and these can be visualized as brightly fluorescent foci by expressing PopZ as a fusion with mCherry (mChy). When a PopZ binding protein such as ParA-GFP or GFP-ParB is coexpressed with mChy-PopZ, both proteins colocalize in polar foci (7, 16, 17).","type":"Results"},{"text":"Six other candidates exhibited the expected localization patterns for a PopZ binding protein: disperse when expressed without mChy-PopZ, and localized in polar foci with mChy-PopZ when the proteins were expressed simultaneously (Fig. 1C and SI Appendix, Figs. S1–S4).","type":"Results"},{"text":"Removing H3 and H4 (Δ134–177) from the DivIVA-mChy-PopZ fusion protein had no effect on the recruitment of binding partners (Fig. 4C), indicating that the homo-oligomerization and higher-order assembly determinants that enable polar localization of wild-type PopZ are not required for interactions with other proteins.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Disorder function"}],"regions_counter":9,"released":"2021_06","sequence":"MSDQSQEPTMEEILASIRRIISEDDAPAEPAAEAAPPPPPEPEPEPVSFDDEVLELTDPIAPEPELPPLETVGDIDVYSPPEPESEPAYTPPPAAPVFDRDEVAEQLVGVSAASAAASAFGSLSSALLMPKDGRTLEDVVRELLRPLLKEWLDQNLPRIVETKVEEEVQRISRGRGA","taxonomy":["Bacteria","Proteobacteria","Alphaproteobacteria","Caulobacterales","Caulobacteraceae","Caulobacter"],"dataset":[],"UniParc":"UPI00000C7348","uniref100":"UniRef100_Q9A8N4","uniref90":"UniRef90_Q9A8N4","uniref50":"UniRef50_Q9A8N4","genes":[{"name":{"value":"popZ","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ACG50671.1","url":"https://www.ebi.ac.uk/ena/browser/view/ACG50671.1"}}]},"olnNames":[{"value":"CC_1319","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAK23300.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAK23300.1"}}]}]}],"alphafold_very_low_content":0.05084745762711865,"disorder_content":0.751412429378531,"disprot_consensus":{"full":[{"start":1,"end":133,"type":"D"}],"Structural state":[{"start":1,"end":133,"type":"D"}],"Molecular function":[{"start":1,"end":133,"type":"F"}],"Disorder function":[{"start":1,"end":133,"type":"F"}]}},{"disprot_id":"DP03339","acc":"P07673","creator":"jssuarez","date":"2021-05-27T12:41:48.693Z","features":{"pfam":[{"id":"PF13614","name":"AAA domain","start":106,"end":282}],"gene3D":[]},"length":364,"name":"Protein IncC","ncbi_taxon_id":562,"organism":"Escherichia coli","regions":[{"start":1,"end":105,"reference_id":"33856628","reference_source":"pmid","reference_html":"Backbone assignments, and effect of Asn deamidation, of the N-terminal region of the partitioning protein IncC1 from the plasmid RK2. <i> Rehman MF, Jeeves M, Hyde EI. </i> Biomol NMR Assign, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03339r001","statement":[{"text":"In the 1\nH–15N HSQC of IncC NTD, the peaks are\ncrowded in a narrow ~ 1 ppm (7.7–8.7 ppm) region of the\n1\nH dimension and many peaks overlap (Fig. 1a). This shows\nthat the protein is likely to be intrinsically disordered, as\nexpected from its sequence. ","type":"Methods"},{"text":"The secondary chemical shifts of unmodifed IncC NTD\nwere examined using several programmes, namely CSI 3.0\n(Hafsa et al. 2015), DANGLE (Cheung et al. 2010), TALOSN (Shen and Bax 2013), and SSP (Marsh et al. 2006). In\neach case, the analysis suggests that the protein is nearly\nentirely random coil. ","type":"Methods"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-28T09:49:05.399Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_12","sequence":"MGVIHEETAYRKPVPGGDPGAGSGAADHRDSAGRLSRWEATGDVRNVAGTDQGRSVASGASRVGRVRGQELARGVRAGNGGSAGTSGVHRPEVGSGRQEKTGNQTMKTLVTANQKGGVGKTSTLVHLAFDFFERGLRVAVIDLDPQGNASYTLKDFATGLHASKLFGAVPAGGWTETAPAAGDGQAARLALIESNPVLANAERLSLDDARELFGANIKALANQGFDVCLIDTAPTLGVGLAAALFAADYVLSPIELEAYSIQGIKKMVTTIANVRQKNAKLQFLGMVPSKVDARNPRHARHQAELLAAYPKMMIPATVGLRSSIADALASGVPVWKIKKTAARKASKEVRALADYVFTKMEISQ","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":[],"UniParc":"UPI000005F1A4","uniref100":"UniRef100_P07673","uniref90":"UniRef90_P07673","uniref50":"UniRef50_P07673","genes":[{"name":{"value":"incC"}}],"alphafold_very_low_content":0.2802197802197802,"disorder_content":0.28846153846153844,"disprot_consensus":{"full":[{"start":1,"end":105,"type":"D"}],"Structural state":[{"start":1,"end":105,"type":"D"}]}},{"disprot_id":"DP03340","acc":"O62479","creator":"spenadias","date":"2021-05-27T12:41:56.043Z","features":{"pfam":[{"id":"PF16531","name":"Centriolar protein SAS N-terminal domain","start":31,"end":99},{"id":"PF21503","name":"Centriolar protein SAS, helical domain","start":169,"end":205}],"gene3D":[]},"length":492,"name":"Spindle assembly abnormal protein 6","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":106,"end":127,"reference_id":"21277013","reference_source":"pmid","reference_html":"Structural basis of the 9-fold symmetry of centrioles. <i> Kitagawa D, Vakonakis I, Olieric N, Hilbert M, Keller D, Olieric V, Bortfeld M, Erat MC, Flückiger I, Gönczy P, Steinmetz MO. </i> Cell, 2011","date":"2024-04-24T14:59:56.285Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser123Glu","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"3PYI"}],"region_id":"DP03340r002","statement":[{"text":"Loop α2-β5, which is unique to C. elegans, is not seen in the electron density presumably due to disorder and is indicated by a dashed line.","type":"Figure"}]}],"regions_counter":2,"released":"2021_12","sequence":"MTSKIALFDQTLIASLLQPLSLNQPDFKAYKTKVKLKISEQRNETSGEKELKFEISRSDDFEFLFSETLNNEKYQILARDHDLTVDFDAFPKVIIQHLLCKNIVKNLEEDGEVDARKKAGYHSIADPGKPTEINIILDAEKNFCSFELFSKTPISKGKIFSIKLHAVRGDHLISHLLKICSSQAVKLSTFYKSADELASLRQKCGDLEKQVEKLSGVKEEFEEMSEKFKELEDEVELVKEERENIRLLVEDKEDEVADLKQDTESLQKQLEENQEELEIVGNMLREEQGKVDQLQKRNVAHQKEIGKLRAELGTAQRNLEKADQLLKRNSQQQNQQSLDMRKLGELEADLKEKDSMVESLTETIGILRKELENEKLKAAENMDSFEKLSMENENLKEKIAHYRAQRFSPAPSGLPGLQTGLTNRLTPSFKPVLGPHTPYGANLNSRTPFRDNTTLNFQNSTIATPHAFRFNSQLIADETTGSSVTNTPPAQR","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"dataset":[],"UniParc":"UPI000007B7D7","uniref100":"UniRef100_O62479","uniref90":"UniRef90_O62479","uniref50":"UniRef50_O62479","genes":[{"name":{"value":"sas-6","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"Y45F10D.9","url":"https://www.wormbase.org/db/seq/sequence?name=Y45F10D.9;class=Transcript"}}]},"orfNames":[{"value":"Y45F10D.9","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"Y45F10D.9","url":"https://www.wormbase.org/db/seq/sequence?name=Y45F10D.9;class=Transcript"}}]}]}],"alphafold_very_low_content":0.22764227642276422,"disorder_content":0.044715447154471545,"disprot_consensus":{"full":[{"start":106,"end":127,"type":"D"}],"Structural state":[{"start":106,"end":127,"type":"D"}]}},{"disprot_id":"DP03341","acc":"P0A9D4","creator":"jnilsson","date":"2021-05-27T13:51:30.488Z","features":{"pfam":[{"id":"PF00132","name":"Bacterial transferase hexapeptide (six repeats)","start":193,"end":226},{"id":"PF06426","name":"Serine acetyltransferase, N-terminal","start":9,"end":113}],"gene3D":[]},"length":273,"name":"Serine acetyltransferase","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":263,"end":273,"reference_id":"15231846","reference_source":"pmid","reference_html":"The structure and mechanism of serine acetyltransferase from Escherichia coli. <i> Pye VE, Tingey AP, Robson RL, Moody PC. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1T3D"}],"region_id":"DP03341r001","statement":[{"text":"Eleven residues from each of the 273-residue monomers are not visible at the carboxyl termini and the polyhistidine tag is not visible at the amino termini in the electron density maps (maps calculated with σA-weighted Fourier coefficients).","type":"Methods"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-05-28T08:10:56.429Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MSCEELEIVWNNIKAEARTLADCEPMLASFYHATLLKHENLGSALSYMLANKLSSPIMPAIAIREVVEEAYAADPEMIASAACDIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIFLQNQVSVTFQVDIHPAAKIGRGIMLDHATGIVVGETAVIENDVSILQSVTLGGTGKSGGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVGKPDSDKPSMDMDQHFNGINHTFEYGDGI","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":[],"UniParc":"UPI000002DB2D","uniref100":"UniRef100_P0A9D6","uniref90":"UniRef90_P0A9D6","uniref50":"UniRef50_P29847","genes":[{"name":{"value":"cysE"},"olnNames":[{"value":"b3607"},{"value":"JW3582"}]}],"alphafold_very_low_content":0.02564102564102564,"disorder_content":0.040293040293040296,"disprot_consensus":{"full":[{"start":263,"end":273,"type":"D"}],"Structural state":[{"start":263,"end":273,"type":"D"}]}},{"disprot_id":"DP03343","acc":"Q9HCB6","creator":"vacs","date":"2021-05-31T07:06:16.125Z","features":{"pfam":[{"id":"PF00090","name":"Thrombospondin type 1 domain","start":446,"end":494},{"id":"PF00090","name":"Thrombospondin type 1 domain","start":505,"end":554},{"id":"PF00090","name":"Thrombospondin type 1 domain","start":563,"end":610},{"id":"PF00090","name":"Thrombospondin type 1 domain","start":618,"end":665},{"id":"PF00090","name":"Thrombospondin type 1 domain","start":759,"end":807},{"id":"PF02014","name":"Reeler domain","start":44,"end":184},{"id":"PF06468","name":"Spondin_N","start":205,"end":398},{"id":"PF19028","name":"Spondin-like TSP1 domain","start":669,"end":720}],"gene3D":[]},"length":807,"name":"Spondin-1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":29,"end":38,"reference_id":"18602404","reference_source":"pmid","reference_html":"The crystal structure of the heparin-binding reelin-N domain of f-spondin. <i> Tan K, Duquette M, Liu JH, Lawler J, Wang JH. </i> J Mol Biol, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3COO"}],"region_id":"DP03343r001","statement":[{"text":"The construct actually begins at Phe29 after the signal peptide. The first 15 amino acid residues are mostly disordered in the crystal.","type":"Results"},{"text":"The first 14 N-termnal residues (FSDETLDKVPKSEG) and the last 10 C-terminal residues (DSTFDGVTDK) in the expression construct of the human F-spondin reelin-N domain in this study were not used for the alignment. Most of these residues are disordered in the structure.","type":"Figure"},{"text":"The first 10 amino acid residues (29-38) are disordered in the crystal.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-01T08:41:00.740Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":185,"end":198,"reference_id":"19020352","reference_source":"pmid","reference_html":"Structure of the F-spondin reeler domain reveals a unique beta-sandwich fold with a deformable disulfide-bonded loop. <i> Nagae M, Nishikawa K, Yasui N, Yamasaki M, Nogi T, Takagi J. </i> Acta Crystallogr D Biol Crystallogr, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2ZOT"}],"region_id":"DP03343r002","statement":[{"text":"As the quality of the electron-density map corresponding to the N-terminal nine residues (29–37, assuming that the mature protein starts with Phe29) and C-terminal 14 residues (185–198) of both molecules was poor, we omitted these segments from the final model.","type":"Results"},{"text":"Thus, the largely disordered N-terminal and C-terminal segments were removed, leaving the core 145-residue portion (Gly42–Ser186, referred to as FSP145).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-01T08:41:01.787Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":29,"end":43,"reference_id":"19020352","reference_source":"pmid","reference_html":"Structure of the F-spondin reeler domain reveals a unique beta-sandwich fold with a deformable disulfide-bonded loop. <i> Nagae M, Nishikawa K, Yasui N, Yamasaki M, Nogi T, Takagi J. </i> Acta Crystallogr D Biol Crystallogr, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2ZOT"}],"region_id":"DP03343r003","statement":[{"text":"As the quality of the electron-density map corresponding to the N-terminal nine residues (29–37, assuming that the mature protein starts with Phe29) and C-terminal 14 residues (185–198) of both molecules was poor, we omitted these segments from the final model.","type":"Results"},{"text":"Thus, the largely disordered N-terminal and C-terminal segments were removed, leaving the core 145-residue portion (Gly42–Ser186, referred to as FSP145).","type":"Results"},{"text":"The N-terminal 15 residues (29-43) are completely missing in two chains and are presumably disordered. ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-03T14:22:21.542Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2021_06","sequence":"MRLSPAPLKLSRTPALLALALPLAAALAFSDETLDKVPKSEGYCSRILRAQGTRREGYTEFSLRVEGDPDFYKPGTSYRVTLSAAPPSYFRGFTLIALRENREGDKEEDHAGTFQIIDEEETQFMSNCPVAVTESTPRRRTRIQVFWIAPPAGTGCVILKASIVQKRIIYFQDEGSLTKKLCEQDSTFDGVTDKPILDCCACGTAKYRLTFYGNWSEKTHPKDYPRRANHWSAIIGGSHSKNYVLWEYGGYASEGVKQVAELGSPVKMEEEIRQQSDEVLTVIKAKAQWPAWQPLNVRAAPSAEFSVDRTRHLMSFLTMMGPSPDWNVGLSAEDLCTKECGWVQKVVQDLIPWDAGTDSGVTYESPNKPTIPQEKIRPLTSLDHPQSPFYDPEGGSITQVARVVIERIARKGEQCNIVPDNVDDIVADLAPEEKDEDDTPETCIYSNWSPWSACSSSTCDKGKRMRQRMLKAQLDLSVPCPDTQDFQPCMGPGCSDEDGSTCTMSEWITWSPCSISCGMGMRSRERYVKQFPEDGSVCTLPTEETEKCTVNEECSPSSCLMTEWGEWDECSATCGMGMKKRHRMIKMNPADGSMCKAETSQAEKCMMPECHTIPCLLSPWSEWSDCSVTCGKGMRTRQRMLKSLAELGDCNEDLEQVEKCMLPECPIDCELTEWSQWSECNKSCGKGHVIRTRMIQMEPQFGGAPCPETVQRKKCRIRKCLRNPSIQKLRWREARESRRSEQLKEESEGEQFPGCRMRPWTAWSECTKLCGGGIQERYMTVKKRFKSSQFTSCKDKKEIRACNVHPC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000038A5A","uniref100":"UniRef100_Q9HCB6","uniref90":"UniRef90_Q9HCB6","uniref50":"UniRef50_Q9HCB6","genes":[{"name":{"value":"SPON1"},"synonyms":[{"value":"KIAA0762"},{"value":"VSGP"}]}],"alphafold_very_low_content":0.12763320941759604,"disorder_content":0.03593556381660471,"disprot_consensus":{"full":[{"start":29,"end":43,"type":"D"},{"start":185,"end":198,"type":"D"}],"Structural state":[{"start":29,"end":43,"type":"D"},{"start":185,"end":198,"type":"D"}]}},{"disprot_id":"DP03344","acc":"P36955","creator":"vacs","date":"2021-05-31T15:45:08.066Z","features":{"pfam":[{"id":"PF00079","name":"Serpin (serine protease inhibitor)","start":57,"end":415}],"gene3D":[]},"length":418,"name":"Pigment epithelium-derived factor","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":21,"end":35,"reference_id":"11562499","reference_source":"pmid","reference_html":"Crystal structure of human PEDF, a potent anti-angiogenic and neurite growth-promoting factor. <i> Simonovic M, Gettins PG, Volz K. </i> Proc Natl Acad Sci U S A, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1IMV"}],"region_id":"DP03344r001","statement":[{"text":"However, 15 amino acids at the N terminus and 8 amino acids in the reactive center loop were not visible in the final electron density maps.","type":"Methods"},{"text":"With the exception of the extreme 15 residues at the N terminus (residues 1–15) and 8 residues in the reactive center loop (residues 353–360), all of the molecule backbone is well ordered in the final crystal structure (Rcryst 18.8% and Rfree 22.7%; Table 1).","type":"Results"},{"text":"Region 1-15 corresponds to region 21-35 of the amino acid sequence.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-01T08:22:13.503Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":22,"end":26,"reference_id":"15374885","reference_source":"pmid","reference_html":"Extracellular phosphorylation converts pigment epithelium-derived factor from a neurotrophic to an antiangiogenic factor. <i> Maik-Rachline G, Shaltiel S, Seger R. </i> Blood, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP03344r002","statement":[{"text":"CK2 phosphorylates PEDF on 2 main residues, Ser24 and Ser114, and PKA phosphorylates PEDF on one residue only, Ser227.","type":"Abstract"},{"text":"We report here that PEDF purified from human plasma is a phosphoprotein. It is phosphorylated in the serum mainly by CK2 on 2 main residues, Ser24 and Ser114, but also by PKA on Ser227.","type":"Introduction"},{"text":"Mutation of S24A significantly reduced CK2 phosphorylation (Figure 3), while the S24E mutation reduced phosphorylation only to a moderate extent. The S114A mutant significantly reduced CK2 phosphorylation, while the double mutant S24, 114A almost completely abolished this phosphorylation. We concluded that both Ser24 and Ser114 are the main sites for CK2 phosphorylation of PEDF.","type":"Results"},{"text":"Nonetheless, our results indicate that PEDF is phosphorylated by CK2 mainly on residues Ser24 and Ser114.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-07T09:04:12.343Z"},"ec_go":"IMP","disprot_namespace":"Disorder function"},{"start":22,"end":26,"reference_id":"15374885","reference_source":"pmid","reference_html":"Extracellular phosphorylation converts pigment epithelium-derived factor from a neurotrophic to an antiangiogenic factor. <i> Maik-Rachline G, Shaltiel S, Seger R. </i> Blood, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03344r003","statement":[{"text":"The fully CK2 phosphorylation site mutant S24, 114E abolished PEDF neurotrophic activity but enhanced its antiangiogenic activity, while the PKA phosphorylation site mutant S227E reduced PEDF antiangiogenic activity. This is a novel role of extracellular phosphorylation that is shown here to completely change the nature of PEDF from a neutrophic to an antiangiogenic factor.","type":"Abstract"},{"text":"We found that PEDF is functionally modulated by extracellular phosphorylation. The CK2 phosphorylated PEDF had a reduced neurotrophic activity, while its antiangiogenic activity was significantly increased.","type":"Introduction"},{"text":"Because of the differences in ERK activation between plPEDF and rPEDF, we used this system to examine whether the phosphorylation mutants indeed mimic the effect of phosphorylation on PEDF activity. When used to stimulate HUVECs, the CK2 phosphorylation site mutants S24A and S24E did not have a significant effect, while S114A and S114E mutants demonstrated slightly reduced ability to stimulate ERK phosphorylation (Figure 4C). However, significant effects were found with the double mutants, as S24, 114A had a reduced effect, while S24, 114E enhanced ERK phosphorylation. These effects were even stronger than the effects of rPEDF or plPEDF. The higher activity of S24, 114E suggests that the 2 Glu residues indeed mimic the activity of phosphorylated PEDF.","type":"Results"},{"text":"The CK2 phosphorylation site mutants S24E/S24A and S114E/S114A had only small effects, as they all induced neuronal differentiation of the Y-79 cells. However, much fewer neurite-like processes and cell aggregates were observed when cells were treated with the S24, 114E mutant. With this mutant, the cells formed small coronalike structures but were very compact without any sprouts projecting from the cells, and this inhibitory effect was stronger than that of plPEDF. On the other hand, cells treated with the S24, 114A mutant exhibit neurite outgrowth and big aggregates similar to rPEDF.","type":"Results"},{"text":"When incubated together with bFGF, the CK2 nonphosphorylated double mutant, S24, 114A, exhibited an antiangiogenic activity that was similar to or slightly less than that of rPEDF, where rearrangement toward vessels could be seen, but clear\nvessels did not form. On the other hand, the CK2 phosphorylated mutant, S24, 114E, appeared to be a very significant antiangiogenic factor, even stronger than plPEDF, as it did not allow any vessel formation.","type":"Results"},{"text":"We therefore conclude that phosphorylation of PEDF on its CK2 sites significantly enhanced the antiangiogenic activity of PEDF, while the phosphorylation on its PKA site may slightly reduce its antiangiogenic activity.","type":"Results"},{"text":"As shown in the aortic ring assay, the S24, 114E mutant had even stronger antiangiogenic activity relative to plPEDF, as plugs treated with this mutant had very little angiogenic response. In contrast, plugs treated with bFGF and S227E had much less antiangiogenic activity reflected in many infiltrating vessels. In addition plugs treated with bFGF and S24, 114A mutant or S227A mutant appeared similar to those treated with bFGF and rPEDF (not shown). These results further support that CK2-phosphorylated PEDF enhanced the antiangiogenic activity of PEDF, while the phosphorylation on its PKA site may reduce this activity.","type":"Results"},{"text":"Thus, we observed a CK2-dependent difference in the ability of PEDF to induce neuronal differentiation in retinoblastoma cells where both rPEDF and S24, 114A mutants induced neuronal differentiation, while the S24, 114E had almost no neurotrophic effect.","type":"Discussion"},{"text":"Thus, S24, 114E appeared to be a very significant antiangiogenic factor, and its inhibitory effect was more pronounced when compared with plPEDF antiangiogenic activity.","type":"Discussion"},{"text":"Additional support for a functional change of PEDF that is phosphorylation dependent was demonstrated by the degree of ERK activation. A significant effect was found with the double mutants, as S24, 114A reduced ERK activation, while S24, 114E enhanced ERK activation to a higher degree than the stimulation achieved by plPEDF.","type":"Discussion"},{"text":"We found that both CK2 and PKA phosphorylations of PEDF markedly affect its physiologic function. The fully CK2 phosphorylation site mutant S24, 114E abolished PEDF neurotrophic activity and enhanced its antiangiogenic activity, while the PKA phosphorylation site mutant S227E reduced PEDF antiangiogenic activity.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T09:14:54.444Z"},"ec_go":"IMP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":3,"released":"2021_06","sequence":"MQALVLLLCIGALLGHSSCQNPASPPEEGSPDPDSTGALVEEEDPFFKVPVNKLAAAVSNFGYDLYRVRSSTSPTTNVLLSPLSVATALSALSLGAEQRTESIIHRALYYDLISSPDIHGTYKELLDTVTAPQKNLKSASRIVFEKKLRIKSSFVAPLEKSYGTRPRVLTGNPRLDLQEINNWVQAQMKGKLARSTKEIPDEISILLLGVAHFKGQWVTKFDSRKTSLEDFYLDEERTVRVPMMSDPKAVLRYGLDSDLSCKIAQLPLTGSMSIIFFLPLKVTQNLTLIEESLTSEFIHDIDRELKTVQAVLTVPKLKLSYEGEVTKSLQEMKLQSLFDSPDFSKITGKPIKLTQVEHRAGFEWNEDGAGTTPSPGLQPAHLTFPLDYHLNQPFIFVLRDTDTGALLFIGKILDPRGP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000176321","uniref100":"UniRef100_P36955","uniref90":"UniRef90_P36955","uniref50":"UniRef50_P36955","genes":[{"name":{"value":"SERPINF1"},"synonyms":[{"value":"PEDF"}],"orfNames":[{"value":"PIG35"}]}],"alphafold_very_low_content":0.0861244019138756,"disorder_content":0.03588516746411483,"disprot_consensus":{"full":[{"start":21,"end":35,"type":"D"}],"Structural state":[{"start":21,"end":35,"type":"D"}],"Disorder function":[{"start":22,"end":26,"type":"F"}],"Molecular function":[{"start":22,"end":26,"type":"F"}]}},{"disprot_id":"DP03345","acc":"O00214","creator":"jmarchetti","date":"2021-05-31T18:48:07.186Z","features":{"pfam":[{"id":"PF00337","name":"Galactoside-binding lectin","start":18,"end":150},{"id":"PF00337","name":"Galactoside-binding lectin","start":186,"end":314}],"gene3D":[]},"length":317,"name":"Galectin-8","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":154,"end":175,"reference_id":"27973456","reference_source":"pmid","reference_html":"Crystallization of Galectin-8 Linker Reveals Intricate Relationship between the N-terminal Tail and the Linker. <i> Si Y, Wang Y, Gao J, Song C, Feng S, Zhou Y, Tai G, Su J. </i> Int J Mol Sci, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5GZF"},{"db":"PDB","id":"5GZG"}],"region_id":"DP03345r001","statement":[{"text":"In structures 4 and 5, the electron density of residues from Ser154 to the C-terminus was not visible, suggesting greater flexibility from this segment.","type":"Results"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-16T08:08:35.679Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":154,"end":175,"reference_id":"27973456","reference_source":"pmid","reference_html":"Crystallization of Galectin-8 Linker Reveals Intricate Relationship between the N-terminal Tail and the Linker. <i> Si Y, Wang Y, Gao J, Song C, Feng S, Zhou Y, Tai G, Su J. </i> Int J Mol Sci, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"5GZF"},{"db":"PDB","id":"5GZG"}],"region_id":"DP03345r002","statement":[{"text":"\"In structures 4 and 5, the electron density of residues from Ser154 to the C-terminus was not visible, suggesting greater flexibility from this segment.\"","type":"Results"},{"text":"However, the conformation of these linkers remains unknown due likely to their high flexibility. ","type":"Discussion"},{"text":"Tandem-repeat-type galectins, like Gal-8, contain two distinct CRDs that are covalently connected via a peptide linker","type":"Introduction"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-16T15:59:12.515Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":2,"released":"2021_06","sequence":"MMLSLNNLQNIIYNPVIPFVGTIPDQLDPGTLIVIRGHVPSDADRFQVDLQNGSSMKPRADVAFHFNPRFKRAGCIVCNTLINEKWGREEITYDTPFKREKSFEIVIMVLKDKFQVAVNGKHTLLYGHRIGPEKIDTLGIYGKVNIHSIGFSFSSDLQSTQASSLELTEISRENVPKSGTPQLRLPFAARLNTPMGPGRTVVVKGEVNANAKSFNVDLLAGKSKDIALHLNPRLNIKAFVRNSFLQESWGEEERNITSFPFSPGMYFEMIIYCDVREFKVAVNGVHSLEYKHRFKELSSIDTLEINGDIHLLEVRSW","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000014EA6F","uniref100":"UniRef100_O00214","uniref90":"UniRef90_O00214","uniref50":"UniRef50_O00214","genes":[{"name":{"value":"LGALS8","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6569","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6569"}}]}}],"alphafold_very_low_content":0.07255520504731862,"disorder_content":0.0694006309148265,"disprot_consensus":{"full":[{"start":154,"end":175,"type":"D"}],"Structural state":[{"start":154,"end":175,"type":"D"}],"Disorder function":[{"start":154,"end":175,"type":"F"}]}},{"disprot_id":"DP03346","acc":"P63090","creator":"lchemes","date":"2021-05-31T19:25:20.232Z","features":{"pfam":[{"id":"PF01091","name":"PTN/MK heparin-binding protein family, C-terminal domain","start":96,"end":158},{"id":"PF05196","name":"PTN/MK heparin-binding protein family, N-terminal domain","start":34,"end":95}],"gene3D":[]},"length":168,"name":"Pleiotrophin","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions":[{"start":33,"end":46,"reference_id":"10788472","reference_source":"pmid","reference_html":"Heparin-binding growth-associated molecule contains two heparin-binding beta -sheet domains that are homologous to the thrombospondin type I repeat. <i> Kilpelainen I, Kaksonen M, Kinnunen T, Avikainen H, Fath M, Linhardt RJ, Raulo E, Rauvala H. </i> J Biol Chem, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP03346r001","statement":[{"text":"These studies show that HB-GAM contains two b-sheet domains connected by a flexible linker. Both of these domains contain three antiparallel b-strands. In addition to this domain structure, HB-GAM contains the N and C-terminal lysine-rich sequences that lack a detectable structure and appear to form random coils.","type":"Abstract"},{"text":"The N-terminal (amino acids 1–14) and C-terminal (amino acids 111–136) areas of HB-GAM are highly flexible, as indicated by the long T2 15N relaxation rates and by the heteronuclear NOE intensities presented in Fig. 4. For some parts of the flexible N and C termini it was not possible to obtain individual assignments because of strong overlap in 1H, 15N, and 13C frequencies (Fig. 1). Also, the linker (amino acids 59–66) shows some flexibility, as indicated by slightly longer 15N T2 and smaller NOE values.","type":"Results"},{"text":"The numbering is shifted since the authors don’t consider the residues in the signal peptide (res 1-32). Therefore, residue 1 corresponds to residue 33 and residue 136 corresponds to residue 168. ","type":"Curator statement"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-15T21:52:44.838Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":133,"end":168,"reference_id":"10788472","reference_source":"pmid","reference_html":"Heparin-binding growth-associated molecule contains two heparin-binding beta -sheet domains that are homologous to the thrombospondin type I repeat. <i> Kilpelainen I, Kaksonen M, Kinnunen T, Avikainen H, Fath M, Linhardt RJ, Raulo E, Rauvala H. </i> J Biol Chem, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP03346r002","statement":[{"text":"These studies show that HB-GAM contains two b-sheet domains connected by a flexible linker. Both of these domains contain three antiparallel b-strands. In addition to this domain structure, HB-GAM contains the N and C-terminal lysine-rich sequences that lack a detectable structure and appear to form random coils.","type":"Abstract"},{"text":"The N-terminal (amino acids 1–14) and C-terminal (amino acids 111–136) areas of HB-GAM are highly flexible, as indicated by the long T2 15N relaxation rates and by the heteronuclear NOE intensities presented in Fig. 4. For some parts of the flexible N and C termini it was not possible to obtain individual assignments because of strong overlap in 1H, 15N, and 13C frequencies (Fig. 1). Also, the linker (amino acids 59–66) shows some flexibility, as indicated by slightly longer 15N T2 and smaller NOE values.","type":"Results"},{"text":"The numbering is shifted since the authors don’t consider the residues in the signal peptide (res 1-32). Therefore, residue 1 corresponds to residue 33 and residue 136 corresponds to residue 168. ","type":"Curator statement"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-15T21:52:46.298Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_06","sequence":"MSSQQYQQQRRKFAAAFLALIFILAAVDTAEAGKKEKPEKKVKKSDCGEWQWSVCVPTSGDCGLGTREGTRTGAECKQTMKTQRCKIPCNWKKQFGAECKYQFQAWGECDLNTALKTRTGSLKRALHNADCQKTVTISKPCGKLTKPKPQAESKKKKKEGKKQEKMLD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000001835","uniref100":"UniRef100_P63089","uniref90":"UniRef90_P63089","uniref50":"UniRef50_P21246","genes":[{"name":{"value":"Ptn","evidences":[{"code":"ECO:0000312","source":{"name":"RGD","id":"3444","url":"https://rgd.mcw.edu/tools/genes/genes_view.cgi?id=3444"}}]}}],"alphafold_very_low_content":0.15476190476190477,"disorder_content":0.2976190476190476,"disprot_consensus":{"full":[{"start":33,"end":46,"type":"D"},{"start":133,"end":168,"type":"D"}],"Structural state":[{"start":33,"end":46,"type":"D"},{"start":133,"end":168,"type":"D"}]}},{"disprot_id":"DP03347","acc":"P10824","creator":"fquaglia","date":"2021-06-03T15:48:52.024Z","features":{"pfam":[{"id":"PF00503","name":"G-protein alpha subunit","start":14,"end":343}],"gene3D":[]},"length":354,"name":"Guanine nucleotide-binding protein G(i) subunit alpha-1","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions":[{"start":2,"end":32,"reference_id":"8073283","reference_source":"pmid","reference_html":"Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis. <i> Coleman DE, Berghuis AM, Lee E, Linder ME, Gilman AG, Sprang SR. </i> Science, 1994","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1GIA"},{"db":"PDB","id":"1GIL"},{"db":"PDB","id":"1GFI"}],"region_id":"DP03347r001","statement":[{"text":"The amino-terminal 33 residues are disordered in GTP gamma S-Gi alpha 1, suggesting a mechanism that may promote release of the beta gamma subunit complex when the alpha subunit is activated by GTP. ","type":"Abstract"},{"text":"Although the Giα1 protein present in the crystals is intact, no electron density is observed for either the amino-terminal 32 residues or the carboxyl-terminal 11 residues.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-09T07:19:33.623Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":343,"end":354,"reference_id":"8073283","reference_source":"pmid","reference_html":"Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis. <i> Coleman DE, Berghuis AM, Lee E, Linder ME, Gilman AG, Sprang SR. </i> Science, 1994","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1GIA"},{"db":"PDB","id":"1GIL"},{"db":"PDB","id":"1GFI"}],"region_id":"DP03347r002","statement":[{"text":"Although the Giα1 protein present in the crystals is intact, no electron density is observed for either the amino-terminal 32 residues or the carboxyl-terminal 11 residues.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-09T07:19:32.271Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":11,"end":32,"reference_id":"9108480","reference_source":"pmid","reference_html":"Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis. <i> Tesmer JJ, Berman DM, Gilman AG, Sprang SR. </i> Cell, 1997","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1AGR"}],"region_id":"DP03347r003","statement":[{"text":"Structure of RGS4 bound to AlF4--activated Giα1: stabilization of the transition state for GTP hydrolysis.","type":"Title"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-09T07:33:32.807Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":343,"end":354,"reference_id":"9108480","reference_source":"pmid","reference_html":"Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis. <i> Tesmer JJ, Berman DM, Gilman AG, Sprang SR. </i> Cell, 1997","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1AGR"}],"region_id":"DP03347r004","statement":[{"text":"Structure of RGS4 bound to AlF4--activated Giα1: stabilization of the transition state for GTP hydrolysis.","type":"Title"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-09T07:33:31.927Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"}],"regions_counter":4,"released":"2021_06","sequence":"MGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDAARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"dataset":[],"UniParc":"UPI00001104ED","uniref100":"UniRef100_P10824","uniref90":"UniRef90_P08754","uniref50":"UniRef50_P08754","genes":[{"name":{"value":"Gnai1"},"synonyms":[{"value":"Gnai-1"}]}],"alphafold_very_low_content":0.005649717514124294,"disorder_content":0.12146892655367232,"disprot_consensus":{"full":[{"start":2,"end":10,"type":"D"},{"start":11,"end":32,"type":"T"},{"start":343,"end":354,"type":"T"}],"Structural state":[{"start":2,"end":32,"type":"D"},{"start":343,"end":354,"type":"D"}],"Structural transition":[{"start":11,"end":32,"type":"T"},{"start":343,"end":354,"type":"T"}]}},{"disprot_id":"DP03348","acc":"Q5T1C6","creator":"rdavidovic","date":"2021-06-06T14:05:27.519Z","features":{"pfam":[{"id":"PF03061","name":"Thioesterase superfamily","start":149,"end":221}],"gene3D":[]},"length":240,"name":"Acyl-coenzyme A thioesterase THEM4","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":81,"end":106,"reference_id":"22586271","reference_source":"pmid","reference_html":"Acyl coenzyme A thioesterase Them5/Acot15 is involved in cardiolipin remodeling and fatty liver development. <i> Zhuravleva E, Gut H, Hynx D, Marcellin D, Bleck CK, Genoud C, Cron P, Keusch JJ, Dummler B, Esposti MD, Hemmings BA. </i> Mol Cell Biol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"rdavidovic","curator_name":"Radoslav Davidović","curator_orcid":"0000-0002-6097-6203","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4AE8"}],"region_id":"DP03348r001","statement":[{"text":"Them4 and Them5 proteins contain a highly variable sequence stretch (ca. residues 83 to 109 and ca. residues 91 to 114 for Them4 and Them5, respectively) that is partially disordered in both crystal structures.","type":"Results"},{"text":"According to PDB 4AE8 region that spans residues from 81 to 106 is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-07T08:56:12.639Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MLRSCAARLRTLGALCLPPVGRRLPGSEPRPELRSFSSEEVILKDCSVPNPSWNKDLRLLFDQFMKKCEDGSWKRLPSYKRTPTEWIQDFKTHFLDPKLMKEEQMSQAQLFTRSFDDGLGFEYVMFYNDIEKRMVCLFQGGPYLEGPPGFIHGGAIATMIDATVGMCAMMAGGIVMTANLNINYKRPIPLCSVVMINSQLDKVEGRKFFVSCNVQSVDEKTLYSEATSLFIKLNPAKSLT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000045625A","uniref100":"UniRef100_Q5T1C6","uniref90":"UniRef90_Q5T1C6","uniref50":"UniRef50_Q5T1C6","genes":[{"name":{"value":"THEM4"},"synonyms":[{"value":"CTMP"}]}],"alphafold_very_low_content":0.16666666666666666,"disorder_content":0.10833333333333334,"disprot_consensus":{"full":[{"start":81,"end":106,"type":"D"}],"Structural state":[{"start":81,"end":106,"type":"D"}]}},{"disprot_id":"DP03349","acc":"P11795","creator":"fquaglia","date":"2021-06-07T09:34:29.362Z","features":{"pfam":[{"id":"PF00729","name":"Viral coat protein (S domain)","start":77,"end":269},{"id":"PF22402","name":"Coat protein, P (projecting) domain","start":276,"end":378}],"gene3D":[]},"length":388,"name":"Capsid protein","ncbi_taxon_id":12146,"organism":"Tomato bushy stunt virus (strain BS-3)","regions":[{"start":2,"end":101,"reference_id":"6481803","reference_source":"pmid","reference_html":"Structure of tomato bushy stunt virus. V. Coat protein sequence determination and its structural implications. <i> Hopper P, Harrison SC, Sauer RT. </i> J Mol Biol, 1984","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":2,"cross_refs":[{"db":"PDB","id":"2TBV"}],"region_id":"DP03349r001","statement":[{"text":"The N-terminal, inward projecting R domain is flexibly tethered to the rest of the subunit: it therefore cannot be seen in the electron density map.","type":"Introduction"},{"text":"Region 2-101 is disordered in PDB chains B and C although in chain A only residues 2-67 are missing.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-07T10:10:17.510Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_06","sequence":"MAMTTRNNNNVLAISKKQLGVLAASAAVGALRNHISESSPALLQSAVGLGKKALNKVRNRRKQGNQQIITHVGGVGGSIMAPVAVSRQLVGSKPKFTGRTSGSVTVTHREYLTQVNNSSGFVVNGGIVGNLLQLNPSNGTLFSWLPAIASNFDQYSFNSVVLHYVPLCGTTEVGRVALYFDKDSQDPEPADRVELANFGVLKETAPWAEAMLRIPTDKVKRYCNDSATVDQKLIDLGQLGIATYGGAGTNAVGDVFISYSVTLYFPQPTNTLLSTRRLDLTGSLADATGPGYLVLTRTPTVLTHTFRVTGTFNLSGGLRCLTSLTLGATGAVVINDILAIDNVGTASAYFLNCTVSSLPATVTFTTTGISSATVNVVRGTRANVVNLL","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Tolucaviricetes","Tolivirales","Tombusviridae","Procedovirinae","Tombusvirus"],"dataset":["Viral proteins","RNA-binding proteins"],"UniParc":"UPI00000F2225","uniref100":"UniRef100_P11795","uniref90":"UniRef90_P11795","uniref50":"UniRef50_P11795","genes":[{"orfNames":[{"value":"ORF2"}]}],"disorder_content":0.25773195876288657,"disprot_consensus":{"full":[{"start":2,"end":101,"type":"D"}],"Structural state":[{"start":2,"end":101,"type":"D"}]}},{"acc":"P03316","sequence":"MNRGFFNMLGRRPFPAPTAMWRPRRRRQAAPMPARNGLASQIQQLTTAVSALVIGQATRPQPPRPRPPPRQKKQAPKQPPKPKKPKTQEKKKKQPAKPKPGKRQRMALKLEADRLFDVKNEDGDVIGHALAMEGKVMKPLHVKGTIDHPVLSKLKFTKSSAYDMEFAQLPVNMRSEAFTYTSEHPEGFYNWHHGAVQYSGGRFTIPRGVGGRGDSGRPIMDNSGRVVAIVLGGADEGTRTALSVVTWNSKGKTIKTTPEGTEEWSAAPLVTAMCLLGNVSFPCDRPPTCYTREPSRALDILEENVNHEAYDTLLNAILRCGSSGRSKRSVIDDFTLTSPYLGTCSYCHHTVPCFSPVKIEQVWDEADDNTIRIQTSAQFGYDQSGAASANKYRYMSLKQDHTVKEGTMDDIKISTSGPCRRLSYKGYFLLAKCPPGDSVTVSIVSSNSATSCTLARKIKPKFVGREKYDLPPVHGKKIPCTVYDRLKETTAGYITMHRPRPHAYTSYLEESSGKVYAKPPSGKNITYECKCGDYKTGTVSTRTEITGCTAIKQCVAYKSDQTKWVFNSPDLIRHDDHTAQGKLHLPFKLIPSTCMVPVAHAPNVIHGFKHISLQLDTDHLTLLTTRRLGANPEPTTEWIVGKTVRNFTVDRDGLEYIWGNHEPVRVYAQESAPGDPHGWPHEIVQHYYHRHPVYTILAVASATVAMMIGVTVAVLCACKARRECLTPYALAPNAVIPTSLALLCCVRSANAETFTETMSYLWSNSQPFFWVQLCIPLAAFIVLMRCCSCCLPFLVVAGAYLAKVDAYEHATTVPNVPQIPYKALVERAGYAPLNLEITVMSSEVLPSTNQEYITCKFTTVVPSPKIKCCGSLECQPAAHADYTCKVFGGVYPFMWGGAQCFCDSENSQMSEAYVELSADCASDHAQAIKVHTAAMKVGLRIVYGNTTSFLDVYVNGVTPGTSKDLKVIAGPISASFTPFDHKVVIHRGLVYNYDFPEYGAMKPGAFGDIQATSLTSKDLIASTDIRLLKPSAKNVHVPYTQASSGFEMWKNNSGRPLQETAPFGCKIAVNPLRAVDCSYGNIPISIDIPNAAFIRTSDAPLVSTVKCEVSECTYSADFGGMATLQYVSDREGQCPVHSHSSTATLQESTVHVLEKGAVTVHFSTASPQANFIVSLCGKKTTCNAECKPPADHIVSTPHKNDQEFQAAISKTSWSWLFALFGGASSLLIIGLMIFACSMMLTSTRR","creator":"fquaglia","dataset":["Viral proteins","RNA-binding proteins"],"date":"2021-06-07T10:50:56.767Z","disprot_id":"DP03350","features":{"pfam":[{"id":"PF00943","name":"Alphavirus E2 glycoprotein","start":339,"end":745},{"id":"PF00944","name":"Alphavirus core protein","start":107,"end":265},{"id":"PF01563","name":"Alphavirus E3 glycoprotein","start":273,"end":328},{"id":"PF01589","name":"Alphavirus E1 glycoprotein","start":748,"end":1236}],"gene3D":[]},"genes":[],"length":1245,"name":"Structural polyprotein","ncbi_taxon_id":11034,"organism":"Sindbis virus","regions_counter":4,"released":"2021_06","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Alsuviricetes","Martellivirales","Togaviridae","Alphavirus"],"UniParc":"UPI0000131EC1","uniref100":"UniRef100_P03316","uniref50":"UniRef50_P03316","uniref90":"UniRef90_P03316","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":113,"interaction_partner":[],"reference_html":"Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion. <i> Choi HK, Tong L, Minor W, Dumas P, Boege U, Rossmann MG, Wengler G. </i> Nature, 1991","reference_id":"1944569","region_id":"DP03350r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The first 113 residues, as expected, are mostly disordered and account for much of the 'solvent' density. However, there is some electron density, corresponding to about 7  residues, whose assignment remains unknown.","_id":"685af523b4ac24d5329d9712"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-06-07T11:07:21.475Z","_id":"685af523b4ac24d5329d9713"},"version":2,"_id":"685af523b4ac24d5329d9711","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1LD4","_id":"685af523b4ac24d5329d9719"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006003","ec_name":"electron microscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":105,"interaction_partner":[],"reference_html":"Placement of the structural proteins in Sindbis virus. <i> Zhang W, Mukhopadhyay S, Pletnev SV, Baker TS, Kuhn RJ, Rossmann MG. </i> J Virol, 2002","reference_id":"12388725","region_id":"DP03350r003","released":"2022_03","sample":[],"statement":[{"type":"Figure","text":"Note that the amino-terminal residues 106 to 114 are out of density but that there is an obvious density region where these residues are positioned in the virus as opposed to the crystal structure.","_id":"685af523b4ac24d5329d971a"},{"type":"Curator statement","text":"Missing electron density from the PDB shows the region 1-105 as disordered.","_id":"685af523b4ac24d5329d971b"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-25T12:06:00.656Z","_id":"685af523b4ac24d5329d971c"},"version":1,"_id":"685af523b4ac24d5329d9718","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3J0F","_id":"685af523b4ac24d5329d971e"},{"db":"EMDB","id":"EMD-525","_id":"685af523b4ac24d5329d971f"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0006224","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":105,"interaction_partner":[],"reference_html":"Molecular links between the E2 envelope glycoprotein and nucleocapsid core in Sindbis virus. <i> Tang J, Jose J, Chipman P, Zhang W, Kuhn RJ, Baker TS. </i> J Mol Biol, 2011","reference_id":"22001018","region_id":"DP03350r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"These in turn surround a contiguous layer of density (yellow in Fig. 2b) that is mainly composed of the flexible CP N-terminal region (amino acids 1–113).","_id":"685af523b4ac24d5329d9720"},{"type":"Figure","text":"(b) Same as (a) but including the layer of unmodeled density that lies immediately below the ordered protease domain layer and is ascribed primarily to the disordered, 113-residue, N-terminal region of CP.","_id":"685af523b4ac24d5329d9721"},{"type":"Curator statement","text":"Missing electron density in the PDB shows that the 1-105 region is disordered.","_id":"685af523b4ac24d5329d9722"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-25T12:00:44.540Z","_id":"685af523b4ac24d5329d9723"},"version":1,"_id":"685af523b4ac24d5329d971d","reference_source":"pmid"}],"__v":0,"disorder_content":0.09076305220883533,"disprot_consensus":{"full":[{"start":1,"end":113,"type":"D"}],"Structural state":[{"start":1,"end":113,"type":"D"}]}},{"disprot_id":"DP03351","acc":"P23677","creator":"jvanlindt","date":"2021-06-07T14:30:51.544Z","features":{"pfam":[{"id":"PF03770","name":"Inositol polyphosphate kinase","start":245,"end":455}],"gene3D":[]},"length":461,"name":"Inositol-trisphosphate 3-kinase A","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":187,"end":196,"reference_id":"15350214","reference_source":"pmid","reference_html":"Structure of a human inositol 1,4,5-trisphosphate 3-kinase: substrate binding reveals why it is not a phosphoinositide 3-kinase. <i> González B, Schell MJ, Letcher AJ, Veprintsev DB, Irvine RF, Williams RL. </i> Mol Cell, 2004","date":"2023-03-13T13:42:33.456Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006222","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","unpublished":true,"released":"2023_06","version":3,"cross_refs":[{"db":"PDB","id":"1W2C"},{"db":"PDB","id":"1W2D"},{"db":"PDB","id":"1W2F"}],"region_id":"DP03351r001","statement":[{"text":"The most striking conformational change induced by substrates/products is that the N-terminal portion comprising residues 187 to 196 becomes disordered, whereas it is a defined α-helix (α0N) in the apo form (Figure 3D).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16783","entry_name":"1D-myo-inositol 1,3,4,5-tetrakisphosphate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29035","entry_name":"manganese(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"47785","entry_name":"AMP-PNP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16595","entry_name":"1D-myo-inositol 1,4,5-trisphosphate"}],"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":186,"end":186,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":223,"end":223,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":265,"end":265,"position":"Specific residue"},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala187Ser","start":null,"end":null,"position":null}],"sequence_construct":"MSWVQLAGHTGSFKAAGTSGLILKRCSEPERYCLARLMADALRGCVPAFHGVVERDGESYLQLQDLLDGFDGPCVLDCKMGVRTYLEEELTKARERPKLRKDMYKKMLAVDPEAPTEEEHAQRAVTKPRYMQWREGISSSTTLGFRIEGIKKADGSCSTDFKTTRSREQVLRVFEEFVQGDEEVLRRYLNRLQQIRDTLEVSEFFRRHEVIGSSLLFVHDHCHRAGVWLIDFGKTTPLPDGQILDHRRPWEEGNREDGYLLGLDNLIGILASLAER","states_connection":[{"source":"DP03351r003","target":"DP03351r002"}]},{"start":187,"end":196,"reference_id":"15350214","reference_source":"pmid","reference_html":"Structure of a human inositol 1,4,5-trisphosphate 3-kinase: substrate binding reveals why it is not a phosphoinositide 3-kinase. <i> González B, Schell MJ, Letcher AJ, Veprintsev DB, Irvine RF, Williams RL. </i> Mol Cell, 2004","date":"2023-03-13T13:36:39.154Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006222","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1W2D"},{"db":"PDB","id":"1W2C"}],"region_id":"DP03351r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16783","entry_name":"1D-myo-inositol 1,3,4,5-tetrakisphosphate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29035","entry_name":"manganese(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"47785","entry_name":"AMP-PNP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16595","entry_name":"1D-myo-inositol 1,4,5-trisphosphate"}],"statement":[{"text":"The N-terminal residues form a small α0N helix in the apo-form (residues 187-196) that is disordered when substrates or products are bound.","type":"Results"},{"text":"IP3-3K has these structural elements except that the N lobe has helix α0N instead of an N-terminal β strand (Figure 1B) and that this region is disordered in the presence of bound ATP or ADP.","type":"Results"}]},{"start":187,"end":196,"reference_id":"15350214","reference_source":"pmid","reference_html":"Structure of a human inositol 1,4,5-trisphosphate 3-kinase: substrate binding reveals why it is not a phosphoinositide 3-kinase. <i> González B, Schell MJ, Letcher AJ, Veprintsev DB, Irvine RF, Williams RL. </i> Mol Cell, 2004","date":"2023-03-13T13:42:10.044Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006222","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":186,"end":186,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":223,"end":223,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":265,"end":265,"position":"Specific residue"},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala187Ser","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"1W2F"}],"region_id":"DP03351r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"sequence_construct":"MSWVQLAGHTGSFKAAGTSGLILKRCSEPERYCLARLMADALRGCVPAFHGVVERDGESYLQLQDLLDGFDGPCVLDCKMGVRTYLEEELTKARERPKLRKDMYKKMLAVDPEAPTEEEHAQRAVTKPRYMQWREGISSSTTLGFRIEGIKKADGSCSTDFKTTRSREQVLRVFEEFVQGDEEVLRRYLNRLQQIRDTLEVSEFFRRHEVIGSSLLFVHDHCHRAGVWLIDFGKTTPLPDGQILDHRRPWEEGNREDGYLLGLDNLIGILASLAER","statement":[{"text":"The N-terminal residues form a small α0N helix in the apo-form (residues 187-196) that is disordered when substrates or products are bound.","type":"Results"},{"text":"The most striking conformational change induced by substrates/products is that the N-terminal portion comprising residues 187 to 196 becomes disordered, whereas it is a defined α-helix (α0N) in the apo form (Figure 3D).","type":"Results"}]}],"regions_counter":3,"released":"2021_12","sequence":"MTLPGGPTGMARPGGARPCSPGLERAPRRSVGELRLLFEARCAAVAAAAAAGEPRARGAKRRGGQVPNGLPRAPPAPVIPQLTVTAEEPDVPPTSPGPPERERDCLPAAGSSHLQQPRRLSTSSVSSTGSSSLLEDSEDDLLSDSESRSRGNVQLEAGEDVGQKNHWQKIRTMVNLPVISPFKKRYAWVQLAGHTGSFKAAGTSGLILKRCSEPERYCLARLMADALRGCVPAFHGVVERDGESYLQLQDLLDGFDGPCVLDCKMGVRTYLEEELTKARERPKLRKDMYKKMLAVDPEAPTEEEHAQRAVTKPRYMQWREGISSSTTLGFRIEGIKKADGSCSTDFKTTRSREQVLRVFEEFVQGDEEVLRRYLNRLQQIRDTLEVSEFFRRHEVIGSSLLFVHDHCHRAGVWLIDFGKTTPLPDGQILDHRRPWEEGNREDGYLLGLDNLIGILASLAER","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI0000049A1A","uniref100":"UniRef100_P23677","uniref90":"UniRef90_P23677","uniref50":"UniRef50_P23677","genes":[{"name":{"value":"ITPKA","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6178","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6178"}}]}}],"alphafold_very_low_content":0.3796095444685466,"disorder_content":0.021691973969631236,"disprot_consensus":{"full":[{"start":187,"end":196,"type":"T"}],"Structural state":[{"start":187,"end":196,"type":"D"}],"Structural transition":[{"start":187,"end":196,"type":"T"}]}},{"disprot_id":"DP03353","acc":"P05546","creator":"jmarchetti","date":"2021-06-07T19:56:27.403Z","features":{"pfam":[{"id":"PF00079","name":"Serpin (serine protease inhibitor)","start":130,"end":496}],"gene3D":[]},"length":499,"name":"Heparin cofactor 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":20,"end":79,"reference_id":"12169660","reference_source":"pmid","reference_html":"Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism. <i> Baglin TP, Carrell RW, Church FC, Esmon CT, Huntington JA. </i> Proc Natl Acad Sci U S A, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1JMJ"}],"region_id":"DP03353r001","statement":[{"text":" the position  for  the  majority  of  the  acidic  tail  is  undefined  in the  structure  of  native  HCII.  Of  the \u0003160  amino  acids  in  the N-terminal tails of the two molecules comprising the crystallographic asymmetric unit (Fig. 1 e ), only 11 can be unequivocally placed in density (Leu-61 – Asp-71).","type":"Results"},{"text":"Position 61 in the structure is residue 80 in the sequence and position 71 in the structure is residue 90 in the sequence.","type":"Curator statement"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-15T08:45:40.726Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":91,"end":113,"reference_id":"12169660","reference_source":"pmid","reference_html":"Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism. <i> Baglin TP, Carrell RW, Church FC, Esmon CT, Huntington JA. </i> Proc Natl Acad Sci U S A, 2002","date":"2022-02-14T09:00:00.000Z","curator_id":"jmarchetti","curator_name":"Julia Marchetti","curator_orcid":"0000-0002-2886-3647","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1JMJ"}],"region_id":"DP03353r002","statement":[{"text":" the position  for  the  majority  of  the  acidic  tail  is  undefined  in the  structure  of  native  HCII.  Of  the \u0003160  amino  acids  in  the N-terminal tails of the two molecules comprising the crystallographic asymmetric unit (Fig. 1 e ), only 11 can be unequivocally placed in density (Leu-61 – Asp-71).","type":"Results"},{"text":"Position 61 in the structure is residue 80 in the sequence and position 71 in the structure is residue 90 in the sequence.","type":"Curator statement"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-15T08:45:41.847Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_06","sequence":"MKHSLNALLIFLIITSAWGGSKGPLDQLEKGGETAQSADPQWEQLNNKNLSMPLLPADFHKENTVTNDWIPEGEEDDDYLDLEKIFSEDDDYIDIVDSLSVSPTDSDVSAGNILQLFHGKSRIQRLNILNAKFAFNLYRVLKDQVNTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNASSKYEITTIHNLFRKLTHRLFRRNFGYTLRSVNDLYIQKQFPILLDFKTKVREYYFAEAQIADFSDPAFISKTNNHIMKLTKGLIKDALENIDPATQMMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDILQLEYVGGISMLIVVPHKMSGMKTLEAQLTPRVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLKLMGIRMLFDKNGNMAGISDQRIAIDLFKHQGTITVNEEGTQATTVTTVGFMPLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRVANPSRS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000002C4DB","uniref100":"UniRef100_P05546","uniref90":"UniRef90_P05546","uniref50":"UniRef50_P05546","genes":[{"name":{"value":"SERPIND1"},"synonyms":[{"value":"HCF2"}]}],"alphafold_very_low_content":0.22645290581162325,"disorder_content":0.16633266533066132,"disprot_consensus":{"full":[{"start":20,"end":79,"type":"D"},{"start":91,"end":113,"type":"D"}],"Structural state":[{"start":20,"end":79,"type":"D"},{"start":91,"end":113,"type":"D"}]}},{"disprot_id":"DP03354","acc":"P63144","creator":"fquaglia","date":"2021-06-08T08:24:21.457Z","features":{"pfam":[{"id":"PF00248","name":"Aldo/keto reductase family","start":86,"end":389}],"gene3D":[]},"length":401,"name":"Voltage-gated potassium channel subunit beta-1","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions":[{"start":1,"end":62,"reference_id":"10585425","reference_source":"pmid","reference_html":"NMR structure and functional characteristics of the hydrophilic N terminus of the potassium channel beta-subunit Kvbeta1.1. <i> Wissmann R, Baukrowitz T, Kalbacher H, Kalbitzer HR, Ruppersberg JP, Pongs O, Antz C, Fakler B. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","released":"2022_03","version":2,"region_id":"DP03354r001","statement":[{"text":"βN-(1–62) Does Not Exhibit a Defined Structure in Solution","type":"Results"},{"text":"Furthermore, experiments performed to determine the rates of H/D exchange of amide protons showed that all these protons were exchanged in <3 min., indicating that none of these protons are protected by formation of hydrogen bonds within an “internal structure.” Rather all amide protons are easily accessible from the solvent, as is typical for not compactly folded peptides. In summary, these results indicated that βN-(1–62) does not exhibit a well defined structure in solution, but rather behaves like a flexible peptide showing only transient formation of local structures.","type":"Results"},{"text":"βN-(1–62) is a nonstructured peptide.","type":"Results"},{"text":"As determined from NMR experiments, the hydrophilic N terminus of Kvβ1.1 does not exhibit a well defined, unique three-dimensional structure. Rather it can be described by a fast conformational equilibrium of weakly structured substates.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-08T08:30:00.908Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":62,"reference_id":"10585425","reference_source":"pmid","reference_html":"NMR structure and functional characteristics of the hydrophilic N terminus of the potassium channel beta-subunit Kvbeta1.1. <i> Wissmann R, Baukrowitz T, Kalbacher H, Kalbitzer HR, Ruppersberg JP, Pongs O, Antz C, Fakler B. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000030","term_name":"entropic chain","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000353","ec_ontology":"ECO","ec_name":"physical interaction evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03354r002","statement":[{"text":"βN-(1–62) acts as an open channel blocker.","type":"Figure"},{"text":"Kinetics of βN-(1-62)-mediated inactivation. A, inactivation of non-inactivating Kv1.1 channels mediated by 50 μm βN-(1–62) applied to the cytoplasmic side of a giant inside-out patch by the fast application system.","type":"Figure"},{"text":"βN-(1–62) Interacts with the α-Subunit of Kv 1.1 Channels in a Ball-like Manner","type":"Results"},{"text":"The functional characteristics of βN-(1–62) were tested in inside-out patches from Xenopus oocytes expressing non-inactivating Kv1.1 channels. As shown in Fig. 1 B, βN-(1–62) induced rapid inactivation of these channels when present at 50 μm on the cytoplasmic side of the patch; the time-course of inactivation depended on the peptide concentration (not shown). βN-(1–62) blocked Kv1.1 channels only in the open state (Fig. 1 B), similar to IDs derived from Kvα subunits (6, 10).","type":"Results"},{"text":"The interaction between βN-(1–62) and the channel α-subunit was more closely investigated by the “fast application” technique. This technique (see “Materials and Methods”) allows solution exchange at giant inside-out patches in less than 2 ms and enables separate determination for on and off rates of channel-peptide interaction (8,24). Fig. 2, A andB, shows rapid application and wash-off of 50 μm βN-(1–62); these experiments were performed at a membrane potential of 0 mV under asymmetrical K+ conditions ([K+]ex 5 mm, [K+]in 120 mm). Inactivation occurred with a time constant of ≈10 ms (10.3 ± 1.6 ms,n = 3) and was the same whether determined by fast application (left panel, first activation) or in the continuous presence of βN-(1–62) (left, second activation).","type":"Results"},{"text":"The results presented here show that Kvβ1.1 mediates fast inactivation of Kv1α subunits via an N-type mechanism of inactivation. Accordingly, the unique N terminus of Kvβ1.1 comprises a ball-like domain that blocks the channel via interaction with a receptor site that becomes accessible upon channel opening.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-08T08:30:04.696Z"},"ec_go":"IPI","disprot_namespace":"Disorder function"},{"start":1,"end":62,"reference_id":"10585425","reference_source":"pmid","reference_html":"NMR structure and functional characteristics of the hydrophilic N terminus of the potassium channel beta-subunit Kvbeta1.1. <i> Wissmann R, Baukrowitz T, Kalbacher H, Kalbitzer HR, Ruppersberg JP, Pongs O, Antz C, Fakler B. </i> J Biol Chem, 1999","date":"2022-03-08T14:00:18.859Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000353","ec_ontology":"ECO","ec_name":"physical interaction evidence used in manual assertion","released":"2022_03","version":4,"region_id":"DP03354r003","statement":[{"text":"βN-(1–62) Interacts with the α-Subunit of Kv 1.1 Channels in a Ball-like Manner","type":"Results"},{"text":"The interaction between βN-(1–62) and the channel α-subunit was more closely investigated by the “fast application” technique. This technique (see “Materials and Methods”) allows solution exchange at giant inside-out patches in less than 2 ms and enables separate determination for on and off rates of channel-peptide interaction (8,24). Fig. 2, A andB, shows rapid application and wash-off of 50 μm βN-(1–62); these experiments were performed at a membrane potential of 0 mV under asymmetrical K+ conditions ([K+]ex 5 mm, [K+]in 120 mm). Inactivation occurred with a time constant of ≈10 ms (10.3 ± 1.6 ms,n = 3) and was the same whether determined by fast application (left panel, first activation) or in the continuous presence of βN-(1–62) (left, second activation).","type":"Results"},{"text":"The results presented here show that Kvβ1.1 mediates fast inactivation of Kv1α subunits via an N-type mechanism of inactivation. Accordingly, the unique N terminus of Kvβ1.1 comprises a ball-like domain that blocks the channel via interaction with a receptor site that becomes accessible upon channel opening.","type":"Discussion"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P10499","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-26T13:47:15.579Z"}}],"regions_counter":3,"released":"2021_06","sequence":"MQVSIACTEHNLKSRNGEDRLLSKQSSTAPNVVNAARAKFRTVAIIARSLGTFTPQHHISLKESTAKQTGMKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKPYSKKDYRS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"dataset":[],"UniParc":"UPI000000DA1F","uniref100":"UniRef100_Q4PJK1","uniref90":"UniRef90_P63143","uniref50":"UniRef50_P63143","genes":[{"name":{"value":"Kcnab1"},"synonyms":[{"value":"Kvb1"}]}],"alphafold_very_low_content":0.08977556109725686,"disorder_content":0.1546134663341646,"disprot_consensus":{"full":[{"start":1,"end":62,"type":"D"}],"Structural state":[{"start":1,"end":62,"type":"D"}],"Disorder function":[{"start":1,"end":62,"type":"F"}],"Molecular function":[{"start":1,"end":62,"type":"F"}]}},{"disprot_id":"DP03355","acc":"P0ABJ3","creator":"fquaglia","date":"2021-06-08T08:45:50.355Z","features":{"pfam":[{"id":"PF00510","name":"Cytochrome c oxidase subunit III","start":16,"end":202}],"gene3D":[]},"length":204,"name":"Cytochrome bo(3) ubiquinol oxidase subunit 3","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":1,"end":18,"reference_id":"11017202","reference_source":"pmid","reference_html":"The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site. <i> Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikström M. </i> Nat Struct Biol, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1FFT"}],"region_id":"DP03355r001","statement":[{"text":"Out of the 1,291 residues in cytochrome bo3 ubiquinol oxidase we could assign the sequence for 967 residues (subunit I, 52–81, 96–179, 186–488, 490–520 and 541–552; subunit II, 36–112 and 125–283; subunit III, 19–51, 66–124 and 134–203; subunit IV, 1–109).","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-08T09:02:28.329Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MATDTLTHATAHAHEHGHHDAGGTKIFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTWLFGAGFIGMEIYEFHHLIVNGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGAM","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":[],"UniParc":"UPI0000111626","uniref100":"UniRef100_P0ABJ4","uniref90":"UniRef90_P0ABJ4","uniref50":"UniRef50_P0ABJ4","genes":[{"name":{"value":"cyoC"},"olnNames":[{"value":"b0430"},{"value":"JW0420"}]}],"alphafold_very_low_content":0.1568627450980392,"disorder_content":0.08823529411764706,"disprot_consensus":{"full":[{"start":1,"end":18,"type":"D"}],"Structural state":[{"start":1,"end":18,"type":"D"}]}},{"disprot_id":"DP03357","acc":"Q5SHN5","creator":"fquaglia","date":"2021-06-08T14:19:56.302Z","features":{"pfam":[{"id":"PF00009","name":"Elongation factor Tu GTP binding domain","start":10,"end":282},{"id":"PF00679","name":"Elongation factor G C-terminus","start":601,"end":686},{"id":"PF03144","name":"Elongation factor Tu domain 2","start":323,"end":389},{"id":"PF03764","name":"Elongation factor G, domain IV","start":479,"end":597},{"id":"PF14492","name":"Elongation Factor G, domain III","start":404,"end":478}],"gene3D":[]},"length":691,"name":"Elongation factor G","ncbi_taxon_id":300852,"organism":"Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)","regions":[{"start":40,"end":67,"reference_id":"8070397","reference_source":"pmid","reference_html":"Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus. <i> AEvarsson A, Brazhnikov E, Garber M, Zheltonosova J, Chirgadze Y, al-Karadaghi S, Svensson LA, Liljas A. </i> EMBO J, 1994","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"region_id":"DP03357r001","statement":[{"text":"The so-called 'effector' region in the G domain is disordered and not visible in our maps (residues 38-68). This may reflect the functional flexibility of this region, which is possibly involved in interactions with the ribosome and under goes conformational changes upon GTP hydrolysis (Peter et al.,1990b).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-09T12:38:20.201Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":40,"end":67,"reference_id":"8070397","reference_source":"pmid","reference_html":"Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus. <i> AEvarsson A, Brazhnikov E, Garber M, Zheltonosova J, Chirgadze Y, al-Karadaghi S, Svensson LA, Liljas A. </i> EMBO J, 1994","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","released":"2022_03","version":3,"region_id":"DP03357r002","statement":[{"text":"The so-called 'effector' region in the G domain is disordered and not visible in our maps (residues 38-68). This may reflect the functional flexibility of this region, which is possibly involved in interactions with the ribosome and under goes conformational changes upon GTP hydrolysis (Peter et al.,1990b).","type":"Results"},{"text":"The active GTPase interacts with the effector which may be identical to the GAP or different. GEF may not dissociate until GTP is bound (Boguski and McCormick, 1993), and more complicated interactions between GTPase and GEF may exist (Kaziro et al., 1991).","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-09T12:38:33.587Z"},"term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":2,"released":"2021_06","sequence":"MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERERGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSETVWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDVLRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEEELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVEIHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHANHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKADQEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQVAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIPAVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPVILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLRSKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ","taxonomy":["Bacteria","Deinococcus-Thermus","Deinococci","Thermales","Thermaceae","Thermus"],"dataset":[],"UniParc":"UPI0000110F2D","uniref100":"UniRef100_Q5SHN5","uniref90":"UniRef90_Q5SHN5","uniref50":"UniRef50_Q5SHN5","genes":[{"name":{"value":"fusA"},"synonyms":[{"value":"fus"}],"olnNames":[{"value":"TTHA1695"}]}],"alphafold_very_low_content":0.008683068017366137,"disorder_content":0.04052098408104197,"disprot_consensus":{"full":[{"start":40,"end":67,"type":"D"}],"Structural state":[{"start":40,"end":67,"type":"D"}],"Molecular function":[{"start":40,"end":67,"type":"F"}]}},{"disprot_id":"DP03358","acc":"Q92743","creator":"vacs","date":"2021-06-08T15:40:11.163Z","features":{"pfam":[{"id":"PF00219","name":"Insulin-like growth factor binding protein","start":37,"end":89},{"id":"PF07648","name":"Kazal-type serine protease inhibitor domain","start":110,"end":155},{"id":"PF13365","name":"Trypsin-like peptidase domain","start":204,"end":342},{"id":"PF17820","name":"PDZ domain","start":414,"end":464}],"gene3D":[]},"length":480,"name":"Serine protease HTRA1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":94,"end":106,"reference_id":"22578544","reference_source":"pmid","reference_html":"Structural and functional analysis of HtrA1 and its subdomains. <i> Eigenbrot C, Ultsch M, Lipari MT, Moran P, Lin SJ, Ganesan R, Quan C, Tom J, Sandoval W, van Lookeren Campagne M, Kirchhofer D. </i> Structure, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3TJQ"}],"region_id":"DP03358r001","statement":[{"text":"The N-domain structure does not include residues Gly94-Gln106 due to disorder– the homologous IGFBP-4 residues form a short α-helix which contacts IGF-I.","type":"Supplementary material"},{"text":"N-domain molecules are tightly packed within the crystals – of the 118 amino acids in the final model (Gly36 to Ala154, not including Gly94-Gln106), 78 are within 4.5 Å of a neighboring molecule.","type":"Supplementary material"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-15T09:36:58.998Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":301,"end":313,"reference_id":"21297635","reference_source":"pmid","reference_html":"Substrate-induced remodeling of the active site regulates human HTRA1 activity. <i> Truebestein L, Tennstaedt A, Mönig T, Krojer T, Canellas F, Kaiser M, Clausen T, Ehrmann M. </i> Nat Struct Mol Biol, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3NUM"},{"db":"PDB","id":"3NWU"}],"region_id":"DP03358r002","statement":[{"text":"Similarly to those of other HtrAs in the inactive state, the active-site loops L1, L2, L3 and LD are severely disordered, impeding the proper function of the catalytic triad, oxyanion hole and S1 specificity pocket (Fig. 1b,c)3,11–13.","type":"Article"},{"text":"Upon activation, loops L1, L2, L3 and LD undergo a disorder-to-order transition yielding a stably folded activation domain.","type":"Article"},{"text":"Some protein segments including residues 158-160, 285-289 (loop LD), 301-314 (loop L3), and 371-480 (PDZ domain) were hardly visible or invisible in these maps and were therefore omitted from the model.","type":"Supplementary material"},{"text":"Residues 301-313 (loop L3) are disordered in all ligand-free structures (PDB 3NWU and 3NUM).","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-15T10:18:01.560Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":301,"end":313,"reference_id":"21297635","reference_source":"pmid","reference_html":"Substrate-induced remodeling of the active site regulates human HTRA1 activity. <i> Truebestein L, Tennstaedt A, Mönig T, Krojer T, Canellas F, Kaiser M, Clausen T, Ehrmann M. </i> Nat Struct Mol Biol, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3NUM"},{"db":"PDB","id":"3NWU"},{"db":"PDB","id":"3NZI"}],"region_id":"DP03358r003","statement":[{"text":"Peptide binding is the allosteric activation signal that is transmitted to the protease domain via the sensor loop L3 (nomenclature according to refs. 2,3). Rearrangement of L3 induces the remodeling of the activation domain (loops L1, L2, LD) from the resting into the active conformation, which includes a functional catalytic triad, the oxyanion hole, and substrate-specificity pockets3,4.","type":"Article"},{"text":"Upon activation, loops L1, L2, L3 and LD undergo a disorder-to-order transition yielding a stably folded activation domain.","type":"Article"},{"text":"Our data indicate that ligand binding to the protease domain is sufficient to rearrange the activation domain and loop L3 because, in contrast to what occurs with other serine proteases, substrates interact directly with L3 and complete the activation domain. Therefore, the activity of HTRA1 is controlled by induced-fit substrate binding and does not depend on allosteric ligands acting in trans such as are seen with DegP or DegS4,11,17,19.","type":"Article"},{"text":"Residues 301-313 (loop L3) are disordered in all ligand-free structures (PDB 3NWU and 3NUM) and become ordered in the ligand-bound form of HTRA1 (PDB 3NZI).","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-15T09:45:42.143Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":301,"end":313,"reference_id":"21297635","reference_source":"pmid","reference_html":"Substrate-induced remodeling of the active site regulates human HTRA1 activity. <i> Truebestein L, Tennstaedt A, Mönig T, Krojer T, Canellas F, Kaiser M, Clausen T, Ehrmann M. </i> Nat Struct Mol Biol, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"GO:0140677","term_name":"molecular function activator activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"3NUM"},{"db":"PDB","id":"3NWU"},{"db":"PDB","id":"3NZI"}],"region_id":"DP03358r004","statement":[{"text":"Peptide binding is the allosteric activation signal that is transmitted to the protease domain via the sensor loop L3 (nomenclature according to refs. 2,3). Rearrangement of L3 induces the remodeling of the activation domain (loops L1, L2, LD) from the resting into the active conformation, which includes a functional catalytic triad, the oxyanion hole, and substrate-specificity pockets3,4.","type":"Article"},{"text":"Similarly to those of other HtrAs in the inactive state, the active-site loops L1, L2, L3 and LD are severely disordered, impeding the proper function of the catalytic triad, oxyanion hole and S1 specificity pocket (Fig. 1b,c)3,11–13.","type":"Article"},{"text":"Upon activation, loops L1, L2, L3 and LD undergo a disorder-to-order transition yielding a stably folded activation domain.","type":"Article"},{"text":"Our data indicate that ligand binding to the protease domain is sufficient to rearrange the activation domain and loop L3 because, in contrast to what occurs with other serine proteases, substrates interact directly with L3 and complete the activation domain. Therefore, the activity of HTRA1 is controlled by induced-fit substrate binding and does not depend on allosteric ligands acting in trans such as are seen with DegP or DegS4,11,17,19.","type":"Article"},{"text":"Residues 301-313 (loop L3) are disordered in all ligand-free structures (PDB 3NWU and 3NUM) and become ordered in the ligand-bound form of HTRA1 (PDB 3NZI).","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-15T10:18:06.190Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":301,"end":313,"reference_id":"21297635","reference_source":"pmid","reference_html":"Substrate-induced remodeling of the active site regulates human HTRA1 activity. <i> Truebestein L, Tennstaedt A, Mönig T, Krojer T, Canellas F, Kaiser M, Clausen T, Ehrmann M. </i> Nat Struct Mol Biol, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","released":"2022_03","version":3,"region_id":"DP03358r005","statement":[{"text":"The bound ligand interacts closely with the sensor loop L3, contributing to the hydrophobic core of the activation domain involving residues Leu307, Leu309 and Tyr316 (loop L3), Leu345 and Thr344 along with P2-Leu and P4-Phe (Fig. 2b,c).","type":"Article"},{"text":"Residues in loop L3 forming hydrophobic interactions with the inhibitor molecule are shown in stick presentation (orange).","type":"Figure"},{"text":"Our data indicate that ligand binding to the protease domain is sufficient to rearrange the activation domain and loop L3 because, in contrast to what occurs with other serine proteases, substrates interact directly with L3 and complete the activation domain. Therefore, the activity of HTRA1 is controlled by induced-fit substrate binding and does not depend on allosteric ligands acting in trans such as are seen with DegP or DegS4,11,17,19.","type":"Article"},{"text":"Curator statement: Residues 301-313 (loop L3) are disordered in all ligand-free structures (PDB 3NWU and 3NUM) and become ordered in the ligand-bound form of HTRA1 (PDB 3NZI).","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-15T10:18:04.470Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":5,"released":"2021_06","sequence":"MQIPRAALLPLLLLLLAAPASAQLSRAGRSAPLAAGCPDRCEPARCPPQPEHCEGGRARDACGCCEVCGAPEGAACGLQEGPCGEGLQCVVPFGVPASATVRRRAQAGLCVCASSEPVCGSDANTYANLCQLRAASRRSERLHRPPVIVLQRGACGQGQEDPNSLRHKYNFIADVVEKIAPAVVHIELFRKLPFSKREVPVASGSGFIVSEDGLIVTNAHVVTNKHRVKVELKNGATYEAKIKDVDEKADIALIKIDHQGKLPVLLLGRSSELRPGEFVVAIGSPFSLQNTVTTGIVSTTQRGGKELGLRNSDMDYIQTDAIINYGNSGGPLVNLDGEVIGINTLKVTAGISFAIPSDKIKKFLTESHDRQAKGKAITKKKYIGIRMMSLTSSKAKELKDRHRDFPDVISGAYIIEVIPDTPAEAGGLKENDVIISINGQSVVSANDVSDVIKRESTLNMVVRRGNEDIMITVIPEEIDP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000114888","uniref100":"UniRef100_Q92743","uniref90":"UniRef90_Q92743","uniref50":"UniRef50_Q92743","genes":[{"name":{"value":"HTRA1"},"synonyms":[{"value":"HTRA"},{"value":"PRSS11"}]}],"alphafold_very_low_content":0.0875,"disorder_content":0.05416666666666667,"disprot_consensus":{"full":[{"start":94,"end":106,"type":"D"},{"start":301,"end":313,"type":"T"}],"Structural state":[{"start":94,"end":106,"type":"D"},{"start":301,"end":313,"type":"D"}],"Structural transition":[{"start":301,"end":313,"type":"T"}],"Molecular function":[{"start":301,"end":313,"type":"F"}]}},{"disprot_id":"DP03359","acc":"P9WJD9","creator":"ameszaros","date":"2021-06-09T15:42:58.589Z","features":{"pfam":[{"id":"PF18625","name":"ESX-1 secreted protein B PE domain","start":12,"end":88},{"id":"PF21856","name":"ESX-1 secretion-associated protein EspB, PPE domain","start":130,"end":281}],"gene3D":[]},"length":460,"name":"ESX-1 secretion-associated protein EspB","ncbi_taxon_id":83332,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","regions":[{"start":290,"end":460,"reference_id":"32875288","reference_source":"pmid","reference_html":"High resolution CryoEM structure of the ring-shaped virulence factor EspB from <i>Mycobacterium tuberculosis</i>. <i> Piton J, Pojer F, Wakatsuki S, Gati C, Cole ST. </i> J Struct Biol X, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6XZC"}],"region_id":"DP03359r001","statement":[{"text":"The final structure revealed the N-terminal domain of EspB to be organized as a cylindrical heptamer with dimensions of 90 Å x 90 Å and a central channel of 45 Å diameter whereas the C-terminal domain was unstructured.\n","type":"Abstract"},{"text":"The linker (86 to 126) and the C-terminal (291 to 460) domains were not visible in the final map and consequently, the atomic reconstruction was not possible for those domains.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-09T15:51:45.702Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":86,"end":126,"reference_id":"32875288","reference_source":"pmid","reference_html":"High resolution CryoEM structure of the ring-shaped virulence factor EspB from <i>Mycobacterium tuberculosis</i>. <i> Piton J, Pojer F, Wakatsuki S, Gati C, Cole ST. </i> J Struct Biol X, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6XZC"}],"region_id":"DP03359r002","statement":[{"text":"Indeed, for each monomer, the atomic model was accurately built from amino acids 8 to 85 corresponding to the PE domain, and from 127 to 290, corresponding to the PPE domain (Fig. 2B), thanks to a high quality density map at medium-resolution (Fig. S1). The linker (86 to 126) and the C-terminal (291 to 460) domains were not visible in the final map and consequently, the atomic reconstruction was not possible for those domains","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-09T15:51:46.932Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":86,"end":126,"reference_id":"32875288","reference_source":"pmid","reference_html":"High resolution CryoEM structure of the ring-shaped virulence factor EspB from <i>Mycobacterium tuberculosis</i>. <i> Piton J, Pojer F, Wakatsuki S, Gati C, Cole ST. </i> J Struct Biol X, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"6XZC"}],"region_id":"DP03359r003","statement":[{"text":"Indeed, for each monomer, the atomic model was accurately built from amino acids 8 to 85 corresponding to the PE domain, and from 127 to 290, corresponding to the PPE domain (Fig. 2B), thanks to a high quality density map at medium-resolution (Fig. S1). The linker (86 to 126) and the C-terminal (291 to 460) domains were not visible in the final map and consequently, the atomic reconstruction was not possible for those domains","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-09T15:51:47.811Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":3,"released":"2021_06","sequence":"MTQSQTVTVDQQEILNRANEVEAPMADPPTDVPITPCELTAAKNAAQQLVLSADNMREYLAAGAKERQRLATSLRNAAKAYGEVDEEAATALDNDGEGTVQAESAGAVGGDSSAELTDTPRVATAGEPNFMDLKEAARKLETGDQGASLAHFADGWNTFNLTLQGDVKRFRGFDNWEGDAATACEASLDQQRQWILHMAKLSAAMAKQAQYVAQLHVWARREHPTYEDIVGLERLYAENPSARDQILPVYAEYQQRSEKVLTEYNNKAALEPVNPPKPPPAIKIDPPPPPQEQGLIPGFLMPPSDGSGVTPGTGMPAAPMVPPTGSPGGGLPADTAAQLTSAGREAAALSGDVAVKAASLGGGGGGGVPSAPLGSAIGGAESVRPAGAGDIAGLGQGRAGGGAALGGGGMGMPMGAAHQGQGGAKSKGSQQEDEALYTEDRAWTEAVIGNRRRQDSKESK","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"dataset":["Bacterial virulence-related proteins"],"UniParc":"UPI000012ECFF","uniref100":"UniRef100_P9WJD8","uniref90":"UniRef90_P9WJD8","uniref50":"UniRef50_B2HNQ9","genes":[{"name":{"value":"espB","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"17676952","url":"http://www.ncbi.nlm.nih.gov/pubmed/17676952","alternativeUrl":"https://europepmc.org/abstract/MED/17676952"}}]},"synonyms":[{"value":"mtb48","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11427558","url":"http://www.ncbi.nlm.nih.gov/pubmed/11427558","alternativeUrl":"https://europepmc.org/abstract/MED/11427558"}}]}],"orfNames":[{"value":"MTV027.16c"}],"olnNames":[{"value":"Rv3881c"}]}],"alphafold_very_low_content":0.3760869565217391,"disorder_content":0.4608695652173913,"disprot_consensus":{"full":[{"start":86,"end":126,"type":"D"},{"start":290,"end":460,"type":"D"}],"Structural state":[{"start":86,"end":126,"type":"D"},{"start":290,"end":460,"type":"D"}],"Disorder function":[{"start":86,"end":126,"type":"F"}]}},{"disprot_id":"DP03360","acc":"Q56062","creator":"ameszaros","date":"2021-06-09T15:53:41.426Z","features":{"pfam":[{"id":"PF13714","name":"Phosphoenolpyruvate phosphomutase","start":10,"end":250}],"gene3D":[]},"length":295,"name":"2-methylisocitrate lyase","ncbi_taxon_id":99287,"organism":"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","regions":[{"start":119,"end":129,"reference_id":"14575713","reference_source":"pmid","reference_html":"Crystal structure of Salmonella typhimurium 2-methylisocitrate lyase (PrpB) and its complex with pyruvate and Mg(2+). <i> Simanshu DK, Satheshkumar PS, Savithri HS, Murthy MR. </i> Biochem Biophys Res Commun, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1O5Q"},{"db":"PDB","id":"1UJQ"}],"region_id":"DP03360r001","statement":[{"text":"In both the native enzyme and pyruvate/Mg(2+) bound forms, the active site loop is completely disordered.","type":"Abstract"},{"text":"However, significant and unambiguous density was not found in three different places: the N terminal 3–4 residues; the active site loop between fourth β-strand and sixth α-helix (residues 118–129), and the last 6–13 C-terminal residues in different subunits.","type":"Results"},{"text":"In the present case, the active site loop, which includes the critical cysteine residue that acts as the base during catalysis, is completely disordered in both native as well as pyruvate/Mg2+ bound PrpB.","type":"Conclusion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-09T16:00:27.626Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":119,"end":129,"reference_id":"14575713","reference_source":"pmid","reference_html":"Crystal structure of Salmonella typhimurium 2-methylisocitrate lyase (PrpB) and its complex with pyruvate and Mg(2+). <i> Simanshu DK, Satheshkumar PS, Savithri HS, Murthy MR. </i> Biochem Biophys Res Commun, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"GO:0140677","term_name":"molecular function activator activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"1O5Q"},{"db":"PDB","id":"1UJQ"}],"region_id":"DP03360r002","statement":[{"text":"In both the native enzyme and pyruvate/Mg(2+) bound forms, the active site loop is completely disordered.","type":"Abstract"},{"text":"However, significant and unambiguous density was not found in three different places: the N terminal 3–4 residues; the active site loop between fourth β-strand and sixth α-helix (residues 118–129), and the last 6–13 C-terminal residues in different subunits.","type":"Results"},{"text":"In the present case, the active site loop, which includes the critical cysteine residue that acts as the base during catalysis, is completely disordered in both native as well as pyruvate/Mg2+ bound PrpB.","type":"Conclusion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-09T16:00:28.473Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":2,"released":"2021_06","sequence":"MSLHSPGQAFRAALAKENPLQIVGAINANHALLAQRAGYQAIYLSGGGVAAGSLGLPDLGISTLDDVLTDIRRITDVCPLPLLVDADIGFGSSAFNVARTVKSIAKAGAAALHIEDQVGAKRCGHRPNKAIVSKEEMVDRIRAAVDARTDPNFVIMARTDALAVEGLEAALDRAQAYVDAGADMLFPEAITELSMYRRFADVAQVPILANITEFGATPLFTTDELRSAHVAMALYPLSAFRAMNRAAEKVYTVLRQEGTQKNVIDIMQTRNELYESINYYQFEEKLDALYRNKKS","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"],"dataset":[],"UniParc":"UPI0000162250","uniref100":"UniRef100_Q56062","uniref90":"UniRef90_Q56062","uniref50":"UniRef50_Q56062","genes":[{"name":{"value":"prpB","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10482501","url":"http://www.ncbi.nlm.nih.gov/pubmed/10482501","alternativeUrl":"https://europepmc.org/abstract/MED/10482501"}}]},"olnNames":[{"value":"STM0368"}]}],"alphafold_very_low_content":0.003389830508474576,"disorder_content":0.03728813559322034,"disprot_consensus":{"full":[{"start":119,"end":129,"type":"D"}],"Structural state":[{"start":119,"end":129,"type":"D"}],"Molecular function":[{"start":119,"end":129,"type":"F"}]}},{"disprot_id":"DP03361","acc":"Q8ZKB0","creator":"ameszaros","date":"2021-06-09T16:01:40.624Z","features":{"pfam":[{"id":"PF03193","name":"RsgA GTPase","start":100,"end":276}],"gene3D":[]},"length":350,"name":"Small ribosomal subunit biogenesis GTPase RsgA","ncbi_taxon_id":99287,"organism":"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","regions":[{"start":2,"end":34,"reference_id":"18007041","reference_source":"pmid","reference_html":"Structure of the ribosomal interacting GTPase YjeQ from the enterobacterial species Salmonella typhimurium. <i> Nichols CE, Johnson C, Lamb HK, Lockyer M, Charles IG, Hawkins AR, Stammers DK. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2RCN"}],"region_id":"DP03361r001","statement":[{"text":"The additional N-terminal domain is disordered in our StYjeQ structure, but is designated as a probable ribosome-interaction domain (RID; residues 1–20; Fig. 1) on the basis of sequence homology with the equivalent region of EcYjeQ, in which it has been shown experimentally to play a critical role in the tight binding of EcYjeQ to the 30S ribosome (Daigle & Brown, 2004).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-09T16:07:32.385Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":238,"end":250,"reference_id":"18007041","reference_source":"pmid","reference_html":"Structure of the ribosomal interacting GTPase YjeQ from the enterobacterial species Salmonella typhimurium. <i> Nichols CE, Johnson C, Lamb HK, Lockyer M, Charles IG, Hawkins AR, Stammers DK. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2RCN"}],"region_id":"DP03361r002","statement":[{"text":"missing electron density region of rsgA from Salmonella typhimurium.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-09T16:07:33.198Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":338,"end":350,"reference_id":"18007041","reference_source":"pmid","reference_html":"Structure of the ribosomal interacting GTPase YjeQ from the enterobacterial species Salmonella typhimurium. <i> Nichols CE, Johnson C, Lamb HK, Lockyer M, Charles IG, Hawkins AR, Stammers DK. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2RCN"}],"region_id":"DP03361r003","statement":[{"text":"IDR corresponding to the C-terminal domain of rsgA from Salmonella typhimurium.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-09T16:07:35.267Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2021_06","sequence":"MSKNKLSKGQQRRVNANHQRRLKTSAEKADYDDNLFGEPAEGIVISRFGMHADVESADGEVHRCNIRRTIRSLVTGDRVVWRPGKAAAEGVNVKGIVEAVHERTSVLTRPDFYDGVKPIAANIDQIVIVSAILPELSLNIIDRYLVGCETLQVEPLIVLNKIDLLDDEGMDFVNEQMDIYRNIGYRVLMVSSHTQDGLKPLEEALTGRISIFAGQSGVGKSSLLNALLGLQNEILTNDVSNVSGLGQHTTTAARLYHFPHGGDVIDSPGVREFGLWHLEPEQITQGFVEFHDYLGHCKYRDCKHDADPGCAIREAVENGAIAETRFENYHRILESMAQVKTRKNFSDTDD","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"],"dataset":["RNA-binding proteins"],"UniParc":"UPI00000CD5B6","uniref100":"UniRef100_B5F378","uniref90":"UniRef90_Q8Z193","uniref50":"UniRef50_Q8EJ79","genes":[{"name":{"value":"rsgA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01820","url":"https://hamap.expasy.org/unirule/MF_01820"}}]},"synonyms":[{"value":"engC"},{"value":"yjeQ"}],"olnNames":[{"value":"STM4349"}]}],"alphafold_very_low_content":0.10571428571428572,"disorder_content":0.16857142857142857,"disprot_consensus":{"full":[{"start":2,"end":34,"type":"D"},{"start":238,"end":250,"type":"D"},{"start":338,"end":350,"type":"D"}],"Structural state":[{"start":2,"end":34,"type":"D"},{"start":238,"end":250,"type":"D"},{"start":338,"end":350,"type":"D"}]}},{"disprot_id":"DP03362","acc":"B0Y813","creator":"ameszaros","date":"2021-06-09T16:13:12.625Z","features":{"pfam":[{"id":"PF00043","name":"Glutathione S-transferase, C-terminal domain","start":127,"end":216},{"id":"PF13409","name":"Glutathione S-transferase, N-terminal domain","start":29,"end":92}],"gene3D":[]},"length":240,"name":"Glutathione S-transferase GliG","ncbi_taxon_id":451804,"organism":"Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163)","regions":[{"start":119,"end":142,"reference_id":"33909314","reference_source":"pmid","reference_html":"Structural and Mechanistic Insights into C-S Bond Formation in Gliotoxin. <i> Scherlach K, Kuttenlochner W, Scharf DH, Brakhage AA, Hertweck C, Groll M, Huber EM. </i> Angew Chem Int Ed Engl, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"7NC1"}],"region_id":"DP03362r001","statement":[{"text":"The mutation K127G appears to increase the flexibility of helix a4, leading to a disordered active site pocket.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-09T16:17:45.976Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":119,"end":142,"reference_id":"33909314","reference_source":"pmid","reference_html":"Structural and Mechanistic Insights into C-S Bond Formation in Gliotoxin. <i> Scherlach K, Kuttenlochner W, Scharf DH, Brakhage AA, Hertweck C, Groll M, Huber EM. </i> Angew Chem Int Ed Engl, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"GO:0140677","term_name":"molecular function activator activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"7NC1"}],"region_id":"DP03362r002","statement":[{"text":"The mutation K127G appears to increase the flexibility of helix a4, leading to a disordered active site pocket.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-09T16:17:46.875Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that activates or increases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":2,"released":"2021_12","sequence":"MSERPSDLVVNRLVLFVVKGTATSTHNTVKPLILLEELGVPHDIYVVEKVSAPWFSEINPHKMVPAILDRSPDGRDTLRAWESTSTLMYIADAYDKDGTFGGRNVQERSEINNWLTLHTAALGPTAKYWLYFYKLHPEKLPKTIEKLRSNITVQYDILERRLNEPGQQYLALKDRPTIADIATLPFAMKSTAELFGLEFEKWPKLQEWSVRMGEREAVKRAWQRVAGFGHGEKEYGMLEA","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Eurotiomycetes","Eurotiomycetidae","Eurotiales","Aspergillaceae","Aspergillus","Aspergillus subgen. Fumigati"],"dataset":[],"UniParc":"UPI000170CA01","uniref100":"UniRef100_B0Y813","uniref90":"UniRef90_A4GYZ0","uniref50":"UniRef50_A4GYZ0","genes":[{"orfNames":[{"value":"AFUB_075740","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EDP49544.1","url":"https://www.ebi.ac.uk/ena/browser/view/EDP49544.1"}}]}]}],"alphafold_very_low_content":0.03333333333333333,"disorder_content":0.1,"disprot_consensus":{"full":[{"start":119,"end":142,"type":"D"}],"Structural state":[{"start":119,"end":142,"type":"D"}],"Molecular function":[{"start":119,"end":142,"type":"F"}]}},{"disprot_id":"DP03363","acc":"O05574","creator":"ameszaros","date":"2021-06-11T11:30:34.634Z","features":{"pfam":[{"id":"PF09723","name":"Zinc ribbon domain","start":1,"end":40}],"gene3D":[]},"length":110,"name":"Conserved serine rich protein","ncbi_taxon_id":83332,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","regions":[{"start":50,"end":110,"reference_id":"32843553","reference_source":"pmid","reference_html":"Mycobacterium tuberculosis Rv0991c Is a Redox-Regulated Molecular Chaperone. <i> Becker SH, Ulrich K, Dhabaria A, Ueberheide B, Beavers W, Skaar EP, Iyer LM, Aravind L, Jakob U, Darwin KH. </i> mBio, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03363r001","statement":[{"text":"To evaluate the degree of disorder in Ruc, we measured the secondary structures found in Rucred and Rucox using circular dichroism (CD) spectroscopy (reviewed in reference 37). In accordance with structural predictions, both Rucred and Rucox yielded a CD spectrum characteristic of disordered proteins (Fig. 3C) (38).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-25T13:38:18.087Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":50,"end":110,"reference_id":"32843553","reference_source":"pmid","reference_html":"Mycobacterium tuberculosis Rv0991c Is a Redox-Regulated Molecular Chaperone. <i> Becker SH, Ulrich K, Dhabaria A, Ueberheide B, Beavers W, Skaar EP, Iyer LM, Aravind L, Jakob U, Darwin KH. </i> mBio, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"GO:0044183","term_name":"protein folding chaperone","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007062","ec_ontology":"ECO","ec_name":"light scattering evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03363r002","statement":[{"text":"We therefore propose that Rv0991c, which we named “Ruc” (redox-regulated protein with unstructured C terminus), represents a founding member of a new chaperone family that protects M. tuberculosis and other species from proteotoxicity during oxidative stress. ","type":"Results"},{"text":"Oxidized Ruc prevents unfolded protein aggregation in vitro.","type":"Results"},{"text":"When we measured luciferase aggregation using a different method of detection, light scattering (40), we also observed the inhibition of aggregation by Rucox but not by Rucred (Fig. S1A). Furthermore, chaperone activity by Ruc was observed when Ruc was pretreated with the oxidizing agents hypochlorite or nitric oxide (Fig. S1B), further supporting a model whereby oxidized Ruc counteracts protein aggregation.","type":"Results"},{"text":"In this study, we identified Ruc as the founding member of a new family of bacterial redox-regulated chaperones.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-25T13:38:19.199Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":50,"end":110,"reference_id":"32843553","reference_source":"pmid","reference_html":"Mycobacterium tuberculosis Rv0991c Is a Redox-Regulated Molecular Chaperone. <i> Becker SH, Ulrich K, Dhabaria A, Ueberheide B, Beavers W, Skaar EP, Iyer LM, Aravind L, Jakob U, Darwin KH. </i> mBio, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"GO:0044183","term_name":"protein folding chaperone","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03363r003","statement":[{"text":"We therefore propose that Rv0991c, which we named “Ruc” (redox-regulated protein with unstructured C terminus), represents a founding member of a new chaperone family that protects M. tuberculosis and other species from proteotoxicity during oxidative stress. ","type":"Results"},{"text":"We therefore asked if the intrinsically disordered C-terminal domain of Ruc was required for its chaperone activity. We produced a truncated Ruc variant, RucNterm (amino acids 1 through 49), which harbors only the zinc-binding motif (Fig. 4B, lane 2). In contrast to the variety of multimers observed for Rucox, oxidized RucNterm (RucNterm-ox) formed a single high-molecular-weight species (Fig. 4B, compare lanes 3 and 4). When we tested the chaperone activity of oxidized RucNterm (RucNterm-ox), we found that it was unable to prevent luciferase aggregation (Fig. 4C). Thus, the disordered C terminus of Ruc is required for its chaperone activity, either by binding to client protein, by influencing the conformation or oligomerization state of Ruc, or through a combination of factors.","type":"Results"},{"text":"In this study, we identified Ruc as the founding member of a new family of bacterial redox-regulated chaperones.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-25T13:38:25.487Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":3,"released":"2021_12","sequence":"MPTYSYECTQCANRFDVVQAFTDDALTTCERCSGRLRKLFNAVGVVFKGTGFYRTDSRESGKKSKSQTNGSSTSESTKSSGSSGSSGSSESKASGSTEKSTSSTTAAAAV","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"dataset":[],"UniParc":"UPI00000CCAD7","uniref100":"UniRef100_A0A7U8TXK3","uniref90":"UniRef90_R4LTG9","uniref50":"UniRef50_A0A0H3MTR6","genes":[{"olnNames":[{"value":"Rv0991c","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CCP43741.1","url":"https://www.ebi.ac.uk/ena/browser/view/CCP43741.1"}}]}]}],"alphafold_very_low_content":0.2,"disorder_content":0.5545454545454546,"disprot_consensus":{"full":[{"start":50,"end":110,"type":"D"}],"Structural state":[{"start":50,"end":110,"type":"D"}],"Molecular function":[{"start":50,"end":110,"type":"F"}]}},{"disprot_id":"DP03364","acc":"Q15582","creator":"vacs","date":"2021-06-11T14:45:58.770Z","features":{"pfam":[{"id":"PF02469","name":"Fasciclin domain","start":124,"end":236},{"id":"PF02469","name":"Fasciclin domain","start":252,"end":373},{"id":"PF02469","name":"Fasciclin domain","start":387,"end":500},{"id":"PF02469","name":"Fasciclin domain","start":514,"end":634}],"gene3D":[]},"length":683,"name":"Transforming growth factor-beta-induced protein ig-h3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":24,"end":42,"reference_id":"28988748","reference_source":"pmid","reference_html":"Structural and Functional Implications of Human Transforming Growth Factor β-Induced Protein, TGFBIp, in Corneal Dystrophies. <i> García-Castellanos R, Nielsen NS, Runager K, Thøgersen IB, Lukassen MV, Poulsen ET, Goulas T, Enghild JJ, Gomis-Rüth FX. </i> Structure, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5NV6"}],"region_id":"DP03364r001","statement":[{"text":"The protein consists of a 23-residue signal peptide for secretion (M1-A23), a flexible linker (G24-R42), an N-terminal\ncysteine-rich domain (Q43-P102), four consecutive FAS1 domains (FAS1-1, L103-T238; FAS1-2, I239-K377; FAS1-3, T378-P500; andFAS1-4, P501-N637) with 20% sequence identity to Drosophila fasciclin-1, and a 46-residue C-terminal segment (CTS;\nR638-H683), which includes a ‘‘classic’’ integrin-recognition motif (RGD, residues R642-D644; Clout and Hohenester, 2003; Skonieret al., 1992).","type":"Results"},{"text":"In the crystal structure (seeTable 1), the protein was defined for residues Q43-N637, was monomeric, and had an elongated banana shape maximally spanning 120 A˚ (Figure 1A), which is in accordance with low-resolution small-angle X-ray scattering studies (Basaiawmoit et al., 2011).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-15T09:57:21.864Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":636,"end":657,"reference_id":"24129074","reference_source":"pmid","reference_html":"Mutation in transforming growth factor beta induced protein associated with granular corneal dystrophy type 1 reduces the proteolytic susceptibility through local structural stabilization. <i> Underhaug J, Koldsø H, Runager K, Nielsen JT, Sørensen CS, Kristensen T, Otzen DE, Karring H, Malmendal A, Schiøtt B, Enghild JJ, Nielsen NC. </i> Biochim Biophys Acta, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03364r002","statement":[{"text":"Finally, based on the relaxation experiment described below, we have determined the C-terminal part (residues A636-Ala657) of the full-length WT FAS1-4 domain (Met502–Ala657) to be unstructured (data not shown).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-15T09:52:46.446Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":638,"end":683,"reference_id":"28988748","reference_source":"pmid","reference_html":"Structural and Functional Implications of Human Transforming Growth Factor β-Induced Protein, TGFBIp, in Corneal Dystrophies. <i> García-Castellanos R, Nielsen NS, Runager K, Thøgersen IB, Lukassen MV, Poulsen ET, Goulas T, Enghild JJ, Gomis-Rüth FX. </i> Structure, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5NV6"}],"region_id":"DP03364r003","statement":[{"text":"The protein consists of a 23-residue signal peptide for secretion (M1-A23), a flexible linker (G24-R42), an N-terminal cysteine-rich domain (Q43-P102), four consecutive FAS1 domains (FAS1-1, L103-T238; FAS1-2, I239-K377; FAS1-3, T378-P500; andFAS1-4, P501-N637) with 20% sequence identity to Drosophila fasciclin-1, and a 46-residue C-terminal segment (CTS; R638-H683), which includes a ‘‘classic’’ integrin-recognition motif (RGD, residues R642-D644; Clout and Hohenester, 2003; Skonieret al., 1992).","type":"Results"},{"text":"In the crystal structure (seeTable 1), the protein was defined for residues Q43-N637, was monomeric, and had an elongated banana shape maximally spanning 120 A˚ (Figure 1A), which is in accordance with low-resolution small-angle X-ray scattering studies (Basaiawmoit et al., 2011).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-15T13:58:40.161Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":641,"end":645,"reference_id":"22640878","reference_source":"pmid","reference_html":"ß3 integrin modulates transforming growth factor beta induced (TGFBI) function and paclitaxel response in ovarian cancer cells. <i> Tumbarello DA, Temple J, Brenton JD. </i> Mol Cancer, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03364r004","statement":[{"text":"The RGD motif present in the carboxy-terminus of TGFBI is necessary, but not sufficient, for SKOV3 cell adhesion and is dispensable for adhesion of ovarian cancer cells lacking ß3 integrin expression.","type":"Abstract"},{"text":"Both TGFBI and periostin contain conserved motifs shown to mediate binding to the integrin receptor family. However, although TGFBI and periostin retain the four conserved fasciclin I domains, periostin contains a longer carboxy-terminus lacking an RGD motif, which is present in TGFBI (Figure 1A). Importantly, the RGD\nmotif has been implicated in integrin receptor binding and has been shown to be necessary for cell adhesion to various extracellular proteins, including fibronectin [36].","type":"Results"},{"text":"Both TGFBI and periostin contain conserved Fasciclin I and EMI domains, while only TGFBI contains an RGD motif.","type":"Figure"},{"text":"Unlike periostin, the carboxy-terminus of rTGFBI supports adhesion of ovarian cancer cells and is dependent on an intact RGD motif","type":"Results"},{"text":"The carboxyterminus of TGFBI (aa 498–683), which contains the fourth fasciclin I domain and the RGD motif, was capable of supporting SKOV3 cell adhesion similar to fulllength rTGFBI. However, the fourth fasciclin I domain alone (aa 498–637), previously shown to support HUVEC and human fibroblast cell adhesion [15,43], and the central domain (aa 24–506) were unable to support SKOV3 adhesion (Figure 5B, 5C). Furthermore, mutagenesis of the RGD motif to amino acid residues RAE in the carboxy-terminal truncated form of TGFBI (aa 498–683) abrogated adhesion of SKOV3 cells (Figure 5B, 5C).","type":"Results"},{"text":"To further understand how the fourth fasciclin I domain and the RGD motif cooperate with other TGFBI domains, we evaluated whether mutation of the RGD motif to amino acid residues RAE would affect the ability of full-length TGFBI to support SKOV3 adhesion. In these experiments we found that the RGD to RAE mutation in full-length TGFBI significantly reduced SKOV3 adhesion (Figure 6A).","type":"Results"},{"text":"Therefore, we tested whether the ERGDEL peptide derived from TGFBI was capable of competitively inhibiting adhesion of ovarian cancer cells to fibronectin and rTGFBI. Pretreatment of cells with the classical fibronectin\nGRGDSP peptide was capable of inhibiting adhesion to both fibronectin and rTGFBI (Figure 6B). By contrast, pretreatment with the TGFBI ERGDEL peptide did not alter adherence to fibronectin and rTGFBI (Figure 6B). Therefore, the RGD motif of TGFBI is necessary, but is not sufficient, to support adhesion of SKOV3 cells and\nbinding either requires a greater number of flanking amino acids or a complex with the fourth Fasciclin I domain.","type":"Results"},{"text":"Our results suggest that the RGD motif of full-length TGFBI is necessary, but not sufficient, for ovarian cancer cell adhesion, thus indicating it may cooperate with flanking residues or other motifs, potentially present within the fourth Fasciclin I domain to mediate this process. Importantly, we found that the TGFBI derived RGD peptide (ERGDEL) was unable to competitively inhibit SKOV3 adhesion to rTGFBI, suggesting its use as a therapeutic agent to inhibit TGFBI function may depend on the cellular context.","type":"Discussion"},{"text":"RGD motif (642-644) with flanking residues.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-15T13:58:41.261Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":641,"end":645,"reference_id":"25853243","reference_source":"pmid","reference_html":"Lysosomal trafficking of TGFBIp via caveolae-mediated endocytosis. <i> Choi SI, Maeng YS, Kim TI, Lee Y, Kim YS, Kim EK. </i> PLoS One, 2015","date":"2022-03-08T13:59:24.403Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_03","version":4,"region_id":"DP03364r005","statement":[{"text":"Co-immunoprecipitation revealed that TGFBIp interacted with integrin αVβ3.","type":"Abstract"},{"text":"Previous studies demonstrated that TGFBIp interacts directly with several integrins, including αVβ3, through mechanisms dependent and independent of the RGD binding motif [56,57]. These data suggest that the RGD motif mediates the internalization of TGFBIp through interaction with integrins.","type":"Results"},{"text":"TGFBIp interacts with integrin αVβ3 and αV.","type":"Figure"},{"text":"We also examined the potential association of TGFBIp with αVβ3 integrin by co-immunoprecipitation. Cell lysates from corneal fibroblasts were subjected to immunoprecipitation with specific antibodies against integrin αV or αVβ3, and the resulting immunoprecipitates were analyzed for the presence of TGFBIp by western blot. Our data demonstrate that TGFBIp was coimmunoprecipitated by both integrin αV and αVβ3 antibodies (Fig 6B), suggesting the association between integrin αVβ3 and TGFBIp.","type":"Results"},{"text":"Taken together, these data demonstrate that TGFBIp is internalized via the interaction of αVβ3 or/and αVβ5 integrins with an RGD-motif in TGFBIp.","type":"Results"},{"text":"TGFBIp is internalized via a caveolin-dependent endocytic pathway and transported to the lysosomes for degradation. This internalization is mediated by RGD motif-dependent binding of TGFBIp to integrin αVβ3 or αVβ5.","type":"Discussion"},{"text":"Moreover, we showed that TGFBIp interacted with αV integrin, and that RGD peptide inhibited TGFBIp internalization in a dose-dependent manner. These data suggest that the RGD motif could mediate interaction with integrins, even though TGFBIp is also able to interact with integrins in the absence of this motif [71].","type":"Discussion"},{"text":"RGD motif (642-644) with flanking residues.","type":"Curator statement"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P06756","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P05106","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-14T15:40:16.183Z"}},{"start":641,"end":645,"reference_id":"25853243","reference_source":"pmid","reference_html":"Lysosomal trafficking of TGFBIp via caveolae-mediated endocytosis. <i> Choi SI, Maeng YS, Kim TI, Lee Y, Kim YS, Kim EK. </i> PLoS One, 2015","date":"2022-03-08T13:59:50.576Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005589","ec_ontology":"ECO","ec_name":"confocal microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":4,"region_id":"DP03364r006","statement":[{"text":"Previous studies demonstrated that TGFBIp interacts directly with several integrins, including αVβ3, through mechanisms dependent and independent of the RGD binding motif [56,57]. These data suggest that the RGD motif mediates the internalization of TGFBIp through interaction with integrins.","type":"Results"},{"text":"Consistent with these results, confocal microscopy analysis showed the co-localization of internalized TGFBIp and integrin αV in corneal fibroblasts (Fig 6C). Taken together, these data demonstrate that TGFBIp is internalized via the interaction of αVβ3 or/and αVβ5 integrins with an RGD-motif in TGFBIp.","type":"Results"},{"text":"TGFBIp is internalized via a caveolin-dependent endocytic pathway and transported to the lysosomes for degradation. This internalization is mediated by RGD motif-dependent binding of TGFBIp to integrin αVβ3 or αVβ5.","type":"Discussion"},{"text":"Moreover, we showed that TGFBIp interacted with αV integrin, and that RGD peptide inhibited TGFBIp internalization in a dose-dependent manner. These data suggest that the RGD motif could mediate interaction with integrins, even though TGFBIp is also able to interact with integrins in the absence of this motif [71].","type":"Discussion"},{"text":"RGD motif (642-644) with flanking residues.","type":"Curator statement"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P06756","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P05106","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-14T15:40:18.000Z"}},{"start":641,"end":645,"reference_id":"25853243","reference_source":"pmid","reference_html":"Lysosomal trafficking of TGFBIp via caveolae-mediated endocytosis. <i> Choi SI, Maeng YS, Kim TI, Lee Y, Kim YS, Kim EK. </i> PLoS One, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03364r007","statement":[{"text":"Moreover, treatment with arginine-glycine-aspartic acid (RGD) tripeptide suppressed the internalization of TGFBIp.","type":"Abstract"},{"text":"These data suggest that the RGD motif mediates the internalization of TGFBIp through interaction with integrins. Therefore, we evaluated whether RGD-mediated interactions of TGFBIp with integrins are involved in its internalization. Exogenous human TGFBIp was incubated with corneal fibroblasts in the presence of either RGD peptide or control RAD peptide for 2 h. In the presence of the RGD peptide, the amount of internalized TGFBIp was reduced in a dose-dependent manner (Fig 6A, left panel). However, intracellular TGFBIp levels did not change in cells incubated with the control RAD peptide (Fig 6A, right panel). These results suggest that RGD peptides disrupt TGFBIp internalization by preventing its endocytosis from the ECM.","type":"Results"},{"text":"TGFBIp is internalized via a caveolin-dependent endocytic pathway and transported to the lysosomes for degradation. This internalization is mediated by RGD motif-dependent binding of TGFBIp to integrin αVβ3 or αVβ5.","type":"Discussion"},{"text":"Moreover, we showed that TGFBIp interacted with αV integrin, and that RGD peptide inhibited TGFBIp internalization in a dose-dependent manner. These data suggest that the RGD motif could mediate interaction with integrins, even though TGFBIp is also able to interact with integrins in the absence of this motif [71].","type":"Discussion"},{"text":"RGD motif (642-644) with flanking residues.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-16T12:09:13.768Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false}],"regions_counter":7,"released":"2021_12","sequence":"MALFVRLLALALALALGPAATLAGPAKSPYQLVLQHSRLRGRQHGPNVCAVQKVIGTNRKYFTNCKQWYQRKICGKSTVISYECCPGYEKVPGEKGCPAALPLSNLYETLGVVGSTTTQLYTDRTEKLRPEMEGPGSFTIFAPSNEAWASLPAEVLDSLVSNVNIELLNALRYHMVGRRVLTDELKHGMTLTSMYQNSNIQIHHYPNGIVTVNCARLLKADHHATNGVVHLIDKVISTITNNIQQIIEIEDTFETLRAAVAASGLNTMLEGNGQYTLLAPTNEAFEKIPSETLNRILGDPEALRDLLNNHILKSAMCAEAIVAGLSVETLEGTTLEVGCSGDMLTINGKAIISNKDILATNGVIHYIDELLIPDSAKTLFELAAESDVSTAIDLFRQAGLGNHLSGSERLTLLAPLNSVFKDGTPPIDAHTRNLLRNHIIKDQLASKYLYHGQTLETLGGKKLRVFVYRNSLCIENSCIAAHDKRGRYGTLFTMDRVLTPPMGTVMDVLKGDNRFSMLVAAIQSAGLTETLNREGVYTVFAPTNEAFRALPPRERSRLLGDAKELANILKYHIGDEILVSGGIGALVRLKSLQGDKLEVSLKNNVVSVNKEPVAEPDIMATNGVVHVITNVLQPPANRPQERGDELADSALEIFKQASAFSRASQRSVRLAPVYQKLLERMKH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000000C6A","uniref100":"UniRef100_Q15582","uniref90":"UniRef90_Q15582","uniref50":"UniRef50_Q15582","genes":[{"name":{"value":"TGFBI"},"synonyms":[{"value":"BIGH3"}]}],"alphafold_very_low_content":0.07759882869692533,"disorder_content":0.09809663250366032,"disprot_consensus":{"full":[{"start":24,"end":42,"type":"D"},{"start":636,"end":683,"type":"D"}],"Structural state":[{"start":24,"end":42,"type":"D"},{"start":636,"end":683,"type":"D"}],"Biological process":[{"start":641,"end":645,"type":"F"}],"Molecular function":[{"start":641,"end":645,"type":"F"}]}},{"disprot_id":"DP03365","acc":"P27469","creator":"ameszaros","date":"2021-06-11T15:17:34.885Z","features":{"pfam":[{"id":"PF15103","name":"G0/G1 switch protein 2","start":1,"end":103}],"gene3D":[]},"length":103,"name":"G0/G1 switch protein 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":103,"reference_id":"33073109","reference_source":"pmid","reference_html":"Bioinformatic Analysis and Biophysical Characterization Reveal Structural Disorder in G0S2 Protein. <i> Páez-Pérez ED, Llamas-García ML, Benítez-Cardoza CG, Montero-Morán GM, Lara-González S. </i> ACS Omega, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03365r001","statement":[{"text":"In analytical SEC experiments, human G0S2 eluted as a single peak (Figure ​Figure2A) with a retention volume corresponding to a Stokes radius (RS) of 18.8 Å. This value is 1.1 times larger than the theoretical value of 17.5 Å that can be calculated assuming that human G0S2 has a globular structure and a molecular weight of 11.3 kDa (Figure ​Figure2B).20 This difference resulted in being significant by means of a t-test of one sample (P = 0.0003). The experimental volume was 28.0 Å3, which was higher than the theoretical volume (22.4 Å3), while the experimental density of 0.4 kDa/Å3 was lower than the theoretical value (0.5 kDa/Å3, Table 1).\nThe extended conformation in human G0S2 could be explained in at least two possible ways. It may be due to a partially swelled tertiary structure, which would generate a globular conformation with larger dimensions, as in the case of a molten globule (MG). In this regard, the observed RS value (18.8 Å) is smaller compared to the expected RS value for an MG (19.9 Å).20 Alternatively, the extended conformation could also be attained by the presence of a disordered and extended region exposed to the solvent; in this case, the protein would have a globular domain with an extended segment that would generate an elongated conformation with the observed Rs.\nOur SEC and DLS results suggest that the human G0S2 protein has an elongated shape with a globular domain of approximately 8 kDa.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-16T16:06:39.144Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":103,"reference_id":"33073109","reference_source":"pmid","reference_html":"Bioinformatic Analysis and Biophysical Characterization Reveal Structural Disorder in G0S2 Protein. <i> Páez-Pérez ED, Llamas-García ML, Benítez-Cardoza CG, Montero-Morán GM, Lara-González S. </i> ACS Omega, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03365r002","statement":[{"text":"To gain further insights into the molecular shape of human and mouse G0S2 proteins, DLS measurements were subsequently carried out to calculate the hydrodynamic radius (Rh) for each protein. The size distribution of protein samples showed the presence of a single species with an apparent Rh of 1.4 ± 0.03 and 1.7 ± 0.02 nm, human and mouse G0S2, respectively (Figure3A).\nInterestingly, the Rh obtained for the human G0S2 protein was smaller than the calculated RS value of 1.9 nm determined by SEC, indicating that this protein diffuses like a smaller protein in solution with an apparent size of 8 kDa.\nThe elongated conformation of the human G0S2 could be explained by the presence of a disordered C-terminal region, as suggested by the bioinformatic analysis. Indeed, a theoretical molecular weight of 7.5 kDa can be calculated for human G0S2 by omitting the C-terminal region, which is in accordance with the observed Rh value.\nOur SEC and DLS results suggest that the human G0S2 protein has an elongated shape with a globular domain of approximately 8 kDa.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-16T16:06:40.194Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":103,"reference_id":"33073109","reference_source":"pmid","reference_html":"Bioinformatic Analysis and Biophysical Characterization Reveal Structural Disorder in G0S2 Protein. <i> Páez-Pérez ED, Llamas-García ML, Benítez-Cardoza CG, Montero-Morán GM, Lara-González S. </i> ACS Omega, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03365r003","statement":[{"text":"Secondary Structure Content Analysis Reveals That G0S2 Is Largely Unstructured.\nTo gain more insight into the structural content of G0S2, we used circular dichroism (CD) spectroscopy in the far UV region.31 The human and mouse G0S2 CD spectra exhibit properties previously observed for IDPs. They show a strong minimum signal close to 200 nm (−11.67 × 10–3 and −12.05 × 10–3 deg·cm2·dmol–1, human and mouse G0S2, respectively) and a small negative contribution close to 222 nm (−2.55 × 10–3 and −1.48 × 10–3 deg·cm2·dmol–1, human and mouse G0S2, respectively) (​Figure 5A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-16T16:06:40.890Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2021_12","sequence":"METVQELIPLAKEMMAQKRKGKMVKLYVLGSVLALFGVVLGLMETVCSPFTAARRLRDQEAAVAELQAALERQALQKQALQEKGKQQDTVLGGRALSNRQHAS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000012AE19","uniref100":"UniRef100_P27469","uniref90":"UniRef90_P27469","uniref50":"UniRef50_P27469","genes":[{"name":{"value":"G0S2"}}],"alphafold_very_low_content":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":103,"type":"D"}],"Structural state":[{"start":1,"end":103,"type":"D"}]}},{"disprot_id":"DP03366","acc":"P53778","creator":"msalas","date":"2021-06-11T15:17:58.995Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":27,"end":311}],"gene3D":[]},"length":367,"name":"Mitogen-activated protein kinase 12","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":354,"end":367,"reference_id":"10508788","reference_source":"pmid","reference_html":"The structure of phosphorylated p38gamma is monomeric and reveals a conserved activation-loop conformation. <i> Bellon S, Fitzgibbon MJ, Fox T, Hsiao HM, Wilson KP. </i> Structure, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"msalas","curator_name":"Martin Salas","curator_orcid":"0000-0001-6352-1282","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1CM8"}],"region_id":"DP03366r001","statement":[{"text":" No electron density was observed for amino acids 1–7, 34–39, 316–321, 330–334, and 354–end, therefore these residues were not included in the model.","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-15T08:15:01.451Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MSSPPPARSGFYRQEVTKTAWEVRAVYRDLQPVGSGAYGAVCSAVDGRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMRHENVIGLLDVFTPDETLDDFTDFYLVMPFMGTDLGKLMKHEKLGEDRIQFLVYQMLKGLRYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQADSEMTGYVVTRWYRAPEVILNWMRYTQTVDIWSVGCIMAEMITGKTLFKGSDHLDQLKEIMKVTGTPPAEFVQRLQSDEAKNYMKGLPELEKKDFASILTNASPLAVNLLEKMLVLDAEQRVTAGEALAHPYFESLHDTEDEPQVQKYDDSFDDVDRTLDEWKRVTYKEVLSFKPPRQLGARVSKETPL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Stress response proteins"],"UniParc":"UPI000059CD65","uniref100":"UniRef100_P53778","uniref90":"UniRef90_P53778","uniref50":"UniRef50_P53778","genes":[{"name":{"value":"MAPK12"},"synonyms":[{"value":"ERK6"},{"value":"SAPK3"}]}],"alphafold_very_low_content":0.05449591280653951,"disorder_content":0.03814713896457766,"disprot_consensus":{"full":[{"start":354,"end":367,"type":"D"}],"Structural state":[{"start":354,"end":367,"type":"D"}]}},{"disprot_id":"DP03367","acc":"Q61585","creator":"ameszaros","date":"2021-06-11T15:18:24.143Z","features":{"pfam":[{"id":"PF15103","name":"G0/G1 switch protein 2","start":1,"end":103}],"gene3D":[]},"length":103,"name":"G0/G1 switch protein 2","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":1,"end":103,"reference_id":"33073109","reference_source":"pmid","reference_html":"Bioinformatic Analysis and Biophysical Characterization Reveal Structural Disorder in G0S2 Protein. <i> Páez-Pérez ED, Llamas-García ML, Benítez-Cardoza CG, Montero-Morán GM, Lara-González S. </i> ACS Omega, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03367r001","statement":[{"text":"To gain more insight into the structural content of G0S2, we used circular dichroism (CD) spectroscopy in the far UV region.31 The human and mouse G0S2 CD spectra exhibit properties previously observed for IDPs. They show a strong minimum signal close to 200 nm (−11.67 × 10–3 and −12.05 × 10–3 deg·cm2·dmol–1, human and mouse G0S2, respectively) and a small negative contribution close to 222 nm (−2.55 × 10–3 and −1.48 × 10–3 deg·cm2·dmol–1, human and mouse G0S2, respectively) (​Figure5A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-16T16:08:29.693Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_12","sequence":"MESVQELIPLAKEMMAQKPRGKLVKLYVLGSVLALFGVVLGLVETVCSPFTAASRLRDQEAAVVELREACEQQSLHKQALLAGGKAQEATLCSRALSLRQHAS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"dataset":[],"UniParc":"UPI0000003E6D","uniref100":"UniRef100_Q61585","uniref90":"UniRef90_Q61585","uniref50":"UniRef50_P27469","genes":[{"name":{"value":"G0s2"}}],"alphafold_very_low_content":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":103,"type":"D"}],"Structural state":[{"start":1,"end":103,"type":"D"}]}},{"disprot_id":"DP03368","acc":"P38532-2","creator":"ameszaros","date":"2021-06-11T15:24:24.398Z","features":{"pfam":[],"gene3D":[]},"length":503,"name":"Isoform 1 of Heat shock factor protein 1","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":213,"end":503,"reference_id":"17323918","reference_source":"pmid","reference_html":"The carboxy-terminal domain of heat-shock factor 1 is largely unfolded but can be induced to collapse into a compact, partially structured state. <i> Pattaramanon N, Sangha N, Gafni A. </i> Biochemistry, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03368r001","statement":[{"text":"CD spectroscopy was performed to determine the secondary- and tertiary-structure components of CT. Similar to several papers showing that intrinsically unstructured proteins display a very low abundance of secondary and tertiary structure (19−21, 23, 25), the CD spectra revealed that CT possesses an extended structure with little secondary or tertiary structure. The far-UV CD spectrum at pH 7 (Figure 2a and Table 1) revealed that the random coil is the major component (45). In the near-UV CD spectra, the weak signal at pH 7 also indicated no tertiary structure in CT (Figure 2b).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-25T14:00:55.018Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":213,"end":503,"reference_id":"17323918","reference_source":"pmid","reference_html":"The carboxy-terminal domain of heat-shock factor 1 is largely unfolded but can be induced to collapse into a compact, partially structured state. <i> Pattaramanon N, Sangha N, Gafni A. </i> Biochemistry, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03368r002","statement":[{"text":"Determination of CT Hydrophobic Domain Formation. One characteristic of a natively unfolded protein is a lack of hydrophobic clusters. The hydrophobic probe TNS was used to monitor the hydrophobicity of CT. This probe has a low fluorescence quantum yield in a polar environment, such as water, and the quantum yield significantly increases when the probe is in a nonpolar environment. TNS fluorescence was nearly 0 when CT was incubated at neutral pH (pH 7.4), in the presence of 1 M TMAO, or in 30% TFE, indicating that CT lacks hydrophobic clusters under these conditions (Figure 4).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-25T14:00:56.110Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":213,"end":503,"reference_id":"17323918","reference_source":"pmid","reference_html":"The carboxy-terminal domain of heat-shock factor 1 is largely unfolded but can be induced to collapse into a compact, partially structured state. <i> Pattaramanon N, Sangha N, Gafni A. </i> Biochemistry, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006206","ec_ontology":"ECO","ec_name":"near-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03368r003","statement":[{"text":"CD spectroscopy was performed to determine the secondary- and tertiary-structure components of CT. Similar to several papers showing that intrinsically unstructured proteins display a very low abundance of secondary and tertiary structure (19−21, 23, 25), the CD spectra revealed that CT possesses an extended structure with little secondary or tertiary structure. The far-UV CD spectrum at pH 7 (Figure 2a and Table 1) revealed that the random coil is the major component (45). In the near-UV CD spectra, the weak signal at pH 7 also indicated no tertiary structure in CT (Figure 2b)","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-25T14:01:00.714Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":213,"end":503,"reference_id":"17323918","reference_source":"pmid","reference_html":"The carboxy-terminal domain of heat-shock factor 1 is largely unfolded but can be induced to collapse into a compact, partially structured state. <i> Pattaramanon N, Sangha N, Gafni A. </i> Biochemistry, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03368r004","statement":[{"text":"The degree of compactness of CT was used as an indicator of the collapse to a globular structure. When CT migrated in a size-exclusion column, it eluted fastest at pH 7.4 and slowest at pH 4 (Figure 5). When CT both at pH 7.4 and in the presence of 1 M TMAO was compared to the molecular-weight markers that were run under the same conditions, it eluted with a molecular weight of 165 kDa, about 5 times greater than its calculated molecular weight of 31 kDa. At pH 4 or in the presence of 1 mM DTA, on the other hand, CT eluted at the volume corresponding to a molecular weight of 12.5−30 kDa.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-25T14:01:01.947Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":4,"released":"2023_12","sequence":"MDLAVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVFDQGQFAKEVLPKYFKHNNMASFVRQLNMYGFRKVVHIEQGGLVKPERDDTEFQHPCFLRGQEQLLENIKRKVTSVSTLKSEDIKIRQDSVTRLLTDVQLMKGKQECMDSKLLAMKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLSDSNSAHSVPKYGRQYSLEHVHGPGPYSAPSPAYSSSSLYSSDAVTSSGPIISDITELAPTSPLASPGRSIDERPLSSSTLVRVKQEPPSPPHSPRVLEASPGRPSSMDTPLSPTAFIDSILRESEPTPAASNTAPMDTTGAQAPALPTPSTPEKCLSVACLDKNELSDHLDAMDSNLDNLQTMLTSHGFSVDTSALLDIQELLSPQEPPRPIEAENSNPDSGKQLVHYTAQPLFLLDPDAVDTGSSELPVLFELGESSYFSEGDDYTDDPTISLLTGTEPHKAKDPTVS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"dataset":[],"UniParc":"UPI0000021F45","uniref100":"","uniref90":"","uniref50":"","genes":[{"name":{"value":"Hsf1","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:96238","url":"http://www.informatics.jax.org/marker/MGI:96238"}}]}}],"disorder_content":0.5785288270377733,"disprot_consensus":{"full":[{"start":213,"end":503,"type":"D"}],"Structural state":[{"start":213,"end":503,"type":"D"}]}},{"disprot_id":"DP03369","acc":"O15391","creator":"ameszaros","date":"2021-06-11T15:27:48.990Z","features":{"pfam":[{"id":"PF00096","name":"Zinc finger, C2H2 type","start":283,"end":305},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":311,"end":335},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":341,"end":365}],"gene3D":[]},"length":372,"name":"Transcription factor YY2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":253,"reference_id":"31131888","reference_source":"pmid","reference_html":"The transcription factor YY2 has less momentous properties of an intrinsically disordered protein than its paralog YY1. <i> Figiel M, Łakomska J, Miłek P, Dziedzicka-Wasylewska M, Górecki A. </i> FEBS Lett, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03369r001","statement":[{"text":"The SDS/PAGE profile of the purified proteins (Fig. 2A) shows an anomalous migration of YY2 and NTF2, in agreement with the observations of Nguyen et al. [1] and similar to what we had found for YY1 and NTF1 [11]. The apparent masses calculated from SDS/PAGE are higher than the formula molecular masses for YY2 and NTF2 (Table 1). The discrepancy is typical for intrinsically disordered proteins, as they bind less SDS due to the decreased content of hydrophobic residues [23].","type":"Results"},{"text":"Here, we provide the first detailed structural analysis of YY2, which allows to classify it as an intrinsically disordered protein. The attribution is based on YY2's hydrodynamic properties that are characteristic for a premolten globule, its high proteolytic susceptibility, high content of irregular structures shown by both CD measurements and bioinformatic analyses, and its anomalous migration in SDS/PAGE that arises from atypical amino acid composition.","type":"Discussion"},{"text":"To conclude, YY2 can be classified as an intrinsically disordered protein (IDP) with a bipartite structure: the ordered DBD2, responsible for DNA binding, and the disordered, flexible NTF2.","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-25T14:21:36.069Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":1,"end":253,"reference_id":"31131888","reference_source":"pmid","reference_html":"The transcription factor YY2 has less momentous properties of an intrinsically disordered protein than its paralog YY1. <i> Figiel M, Łakomska J, Miłek P, Dziedzicka-Wasylewska M, Górecki A. </i> FEBS Lett, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03369r002","statement":[{"text":"Interestingly, the hydrodynamic radius of full-length YY2 was nearly the same as for its fragment NTF2 (42.2 Å vs 43.3 Å). The calculated Stokes radii can be compared to formula molecular masses to determine the compactness of the protein conformation (Fig. 4). The analysis of the Stokes radii vs the molecular masses predicts a premolten globule structure for YY2, a molten globule for DBD2 and a natively unfolded state for NTF2. Stokes radii of all three proteins increase in the presence of urea as compared to their respective values in native conditions (Table 3). Therefore, NTF2 also contains some residual stable structures in native conditions.","type":"Results"},{"text":"Here, we provide the first detailed structural analysis of YY2, which allows to classify it as an intrinsically disordered protein. The attribution is based on YY2's hydrodynamic properties that are characteristic for a premolten globule, its high proteolytic susceptibility, high content of irregular structures shown by both CD measurements and bioinformatic analyses, and its anomalous migration in SDS/PAGE that arises from atypical amino acid composition.","type":"Discussion"},{"text":"To conclude, YY2 can be classified as an intrinsically disordered protein (IDP) with a bipartite structure: the ordered DBD2, responsible for DNA binding, and the disordered, flexible NTF2.","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-25T14:21:42.205Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":253,"reference_id":"31131888","reference_source":"pmid","reference_html":"The transcription factor YY2 has less momentous properties of an intrinsically disordered protein than its paralog YY1. <i> Figiel M, Łakomska J, Miłek P, Dziedzicka-Wasylewska M, Górecki A. </i> FEBS Lett, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03369r003","statement":[{"text":"The spectrum registered for YY2 is typical for a protein with a considerable content of α-helices and β-sheets, with a double minimum at 200–230 nm and a maximum around 190 nm. The spectrum of NTF2 lacks the 190 nm maximum, which comes from α-helical structures. The 205 nm minimum is blue-shifted for NTF2 and red-shifted for DBD2, suggesting differing contributions from α- and β-structures. The spectra of YY1 and YY2 variants are generally similar in shape, especially the ones of DBD1 and DBD2. The spectrum of NTF2 has a more pronounced shoulder at 222 nm than the one of NTF1. The 222 nm shoulder also differentiates the spectra of full-length YY1 and YY2, together with the maximum at 190 nm, which is greater for YY2 than for YY1. The results of the bioinformatic analysis presented in Fig. 1 correspond with the CD spectra of YY1, YY2, and their fragments (Fig. 5)","type":"Results"},{"text":"Here, we provide the first detailed structural analysis of YY2, which allows to classify it as an intrinsically disordered protein. The attribution is based on YY2's hydrodynamic properties that are characteristic for a premolten globule, its high proteolytic susceptibility, high content of irregular structures shown by both CD measurements and bioinformatic analyses, and its anomalous migration in SDS/PAGE that arises from atypical amino acid composition.","type":"Discussion"},{"text":"To conclude, YY2 can be classified as an intrinsically disordered protein (IDP) with a bipartite structure: the ordered DBD2, responsible for DNA binding, and the disordered, flexible NTF2.","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-25T14:21:47.114Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":372,"reference_id":"31131888","reference_source":"pmid","reference_html":"The transcription factor YY2 has less momentous properties of an intrinsically disordered protein than its paralog YY1. <i> Figiel M, Łakomska J, Miłek P, Dziedzicka-Wasylewska M, Górecki A. </i> FEBS Lett, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"ameszaros","curator_name":"Attila Meszaros","curator_orcid":"0000-0002-4578-4879","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03369r004","statement":[{"text":"The spectrum registered for YY2 is typical for a protein with a considerable content of α-helices and β-sheets, with a double minimum at 200–230 nm and a maximum around 190 nm. The spectrum of NTF2 lacks the 190 nm maximum, which comes from α-helical structures. The 205 nm minimum is blue-shifted for NTF2 and red-shifted for DBD2, suggesting differing contributions from α- and β-structures. The spectra of YY1 and YY2 variants are generally similar in shape, especially the ones of DBD1 and DBD2. The spectrum of NTF2 has a more pronounced shoulder at 222 nm than the one of NTF1. The 222 nm shoulder also differentiates the spectra of full-length YY1 and YY2, together with the maximum at 190 nm, which is greater for YY2 than for YY1. The results of the bioinformatic analysis presented in Fig. 1 correspond with the CD spectra of YY1, YY2, and their fragments (Fig. 5)","type":"Results"},{"text":"Here, we provide the first detailed structural analysis of YY2, which allows to classify it as an intrinsically disordered protein. The attribution is based on YY2's hydrodynamic properties that are characteristic for a premolten globule, its high proteolytic susceptibility, high content of irregular structures shown by both CD measurements and bioinformatic analyses, and its anomalous migration in SDS/PAGE that arises from atypical amino acid composition.","type":"Discussion"},{"text":"To conclude, YY2 can be classified as an intrinsically disordered protein (IDP) with a bipartite structure: the ordered DBD2, responsible for DNA binding, and the disordered, flexible NTF2.","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-25T14:21:51.300Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":4,"released":"2023_12","sequence":"MASNEDFSITQDLEIPADIVELHDINVEPLPMEDIPTESVQYEDVDGNWIYGGHNHPPLMVLQPLFTNTGYGDHDQEMLMLQTQEEVVGYCDSDNQLGNDLEDQLALPDSIEDEHFQMTLASLSASAASTSTSTQSRSKKPSKKPSGKSATSTEANPAGSSSSLGTRKWEQKQMQVKTLEGEFSVTMWSPNDNNDQGAVGEGQAENPPDYSEYLKGKKLPPGGLPGIDLSDPKQLAEFTKVKPKRSKGEPPKTVPCSYSGCEKMFRDYAAMRKHLHIHGPRVHVCAECGKAFLESSKLRRHQLVHTGEKPFQCTFEGCGKRFSLDFNLRTHLRIHTGDKPFVCPFDVCNRKFAQSTNLKTHILTHVKTKNNP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI000006CE0D","uniref100":"UniRef100_O15391","uniref90":"UniRef90_O15391","uniref50":"UniRef50_O15391","genes":[{"name":{"value":"YY2"},"synonyms":[{"value":"ZNF631"}]}],"alphafold_very_low_content":0.6344086021505376,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":372,"type":"D"}],"Structural state":[{"start":1,"end":372,"type":"D"}]}},{"disprot_id":"DP03372","acc":"P04554","creator":"fquaglia","date":"2021-06-14T07:34:08.886Z","features":{"pfam":[{"id":"PF00841","name":"Sperm histone P2","start":1,"end":87}],"gene3D":[]},"length":102,"name":"Protamine-2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":46,"end":102,"reference_id":"2243113","reference_source":"pmid","reference_html":"Zinc-induced secondary structure transitions in human sperm protamines. <i> Gatewood JM, Schroth GP, Schmid CW, Bradbury EM. </i> J Biol Chem, 1990","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03372r001","statement":[{"text":"The CD spectra of protamine is characteristic of random coil proteins with a large minima at 197 nm.","type":"Abstract"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-14T10:37:22.401Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":46,"end":102,"reference_id":"2243113","reference_source":"pmid","reference_html":"Zinc-induced secondary structure transitions in human sperm protamines. <i> Gatewood JM, Schroth GP, Schmid CW, Bradbury EM. </i> J Biol Chem, 1990","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03372r002","statement":[{"text":"Using CD we show that human group II protamines undergo novel zinc-dependent secondary structure transitions.","type":"Abstract"},{"text":"We have demonstrated that human protamine II is a zinc binding protein based on the solution structure modulations induced by zinc and monitored by the CD spectra at 197 nm.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-14T10:41:05.518Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":46,"end":102,"reference_id":"2243113","reference_source":"pmid","reference_html":"Zinc-induced secondary structure transitions in human sperm protamines. <i> Gatewood JM, Schroth GP, Schmid CW, Bradbury EM. </i> J Biol Chem, 1990","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0008270","term_name":"zinc ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03372r003","statement":[{"text":"We have demonstrated that human protamine II is a zinc binding protein based on the solution structure modulations induced by zinc and monitored by the CD spectra at 197 nm.","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-14T10:37:24.549Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":4,"released":"2023_12","sequence":"MVRYRVRSLSERSHEVYRQQLHGQEQGHHGQEEQGLSPEHVEVYERTHGQSHYRRRHCSRRRLHRIHRRQHRSCRRRKRRSCRHRRRHRRGCRTRKRTCRRH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"UniParc":"UPI0000163B50","uniref100":"UniRef100_P04554","uniref90":"UniRef90_P04554","uniref50":"UniRef50_P04554","genes":[{"name":{"value":"PRM2"}}],"alphafold_very_low_content":0.3333333333333333,"disorder_content":0.5588235294117647,"disprot_consensus":{"full":[{"start":46,"end":102,"type":"T"}],"Structural state":[{"start":46,"end":102,"type":"D"}],"Structural transition":[{"start":46,"end":102,"type":"T"}],"Molecular function":[{"start":46,"end":102,"type":"F"}]}},{"disprot_id":"DP03374","acc":"P02400","creator":"esalladini","date":"2021-06-14T11:50:35.842Z","features":{"pfam":[{"id":"PF00428","name":"60s Acidic ribosomal protein","start":18,"end":109}],"gene3D":[]},"length":110,"name":"60S acidic ribosomal protein P2-beta","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":110,"reference_id":"9236009","reference_source":"pmid","reference_html":"The exchangeable yeast ribosomal acidic protein YP2beta shows characteristics of a partly folded state under physiological conditions. <i> Zurdo J, Sanz JM, González C, Rico M, Ballesta JP. </i> Biochemistry, 1997","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03374r001","statement":[{"text":"In fact, the experimental data indicate that the protein resembles a “molten globule” under physiological conditions.","type":"Abstract"},{"text":"bis-ANS binding experiments show that the hydrophobic core is accessible to the solvent at neutral pH, and more so at low pH.","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-14T13:21:02.132Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":1,"end":110,"reference_id":"9236009","reference_source":"pmid","reference_html":"The exchangeable yeast ribosomal acidic protein YP2beta shows characteristics of a partly folded state under physiological conditions. <i> Zurdo J, Sanz JM, González C, Rico M, Ballesta JP. </i> Biochemistry, 1997","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03374r002","statement":[{"text":"In fact, the experimental data indicate that the protein resembles a “molten globule” under physiological conditions.","type":"Abstract"},{"text":"The differences between the 1D NMR spectra of the native (Figure 8a) and the urea-denatured YP2β protein (Figure 8c) confirm the existence of a partly structured state at pH 7 clearly different from a fully unfolded one.","type":"Results"},{"text":"The fact that all the amide protons of the protein exchange so quickly with solvent suggests that no stable tight structured region exists in the protein.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-14T13:21:04.557Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":110,"reference_id":"10913306","reference_source":"pmid","reference_html":"Structural differences between Saccharomyces cerevisiae ribosomal stalk proteins P1 and P2 support their functional diversity. <i> Zurdo J, González C, Sanz JM, Rico M, Remacha M, Ballesta JP. </i> Biochemistry, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P05318","partner_start":null,"partner_end":null}],"region_id":"DP03374r003","statement":[{"text":"Incubation of both proteins was followed by far-UV CD and 1D-NMR measurements, and spectra were compared with those of the isolated proteins under the same conditions. The CD spectra of the protein mixture, when compared to the arithmetical addition of spectra from the individual proteins indicate that some secondary structural changes take place upon incubation of both proteins together (Figure 9A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-14T13:21:19.049Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":110,"reference_id":"10913306","reference_source":"pmid","reference_html":"Structural differences between Saccharomyces cerevisiae ribosomal stalk proteins P1 and P2 support their functional diversity. <i> Zurdo J, González C, Sanz JM, Rico M, Remacha M, Ballesta JP. </i> Biochemistry, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P05318","partner_start":null,"partner_end":null}],"region_id":"DP03374r004","statement":[{"text":"Incubation of both proteins was followed by far-UV CD and 1D-NMR measurements, and spectra were compared with those of the isolated proteins under the same conditions. The CD spectra of the protein mixture, when compared to the arithmetical addition of spectra from the individual proteins indicate that some secondary structural changes take place upon incubation of both proteins together (Figure 9A).","type":"Results"},{"text":"Protein interactions seems to increase the secondary structure of one or both proteins.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-14T13:21:23.022Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":110,"reference_id":"11080154","reference_source":"pmid","reference_html":"Phosphorylation and N-terminal region of yeast ribosomal protein P1 mediate its degradation, which is prevented by protein P2. <i> Nusspaumer G, Remacha M, Ballesta JP. </i> EMBO J, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005581","ec_ontology":"ECO","ec_name":"enzyme-linked immunoabsorbent assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03374r005","statement":[{"text":"Protein P2α protects protein P1β from degradation.","type":"Results"},{"text":" As shown above, transformation of S.cerevisiae W303-1b with the P1β-encoding multicopy plasmid alone causes an increase in expression of this protein. This increase was notably smaller than the increase detected when P2 protein was overexpressed, due to the higher sensitivity of P1 proteins to degradation.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-14T13:21:24.181Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":5,"released":"2021_12","sequence":"MKYLAAYLLLVQGGNAAPSAADIKAVVESVGAEVDEARINELLSSLEGKGSLEEIIAEGQKKFATVPTGGASSAAAGAAGAAAGGDAAEEEKEEEAKEESDDDMGFGLFD","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"dataset":[],"UniParc":"UPI0000173AB5","uniref100":"UniRef100_P02400","uniref90":"UniRef90_P02400","uniref50":"UniRef50_P02400","genes":[{"name":{"value":"RPP2B","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9559554","url":"http://www.ncbi.nlm.nih.gov/pubmed/9559554","alternativeUrl":"https://europepmc.org/abstract/MED/9559554"}}]},"synonyms":[{"value":"L12EIA"},{"value":"RPL45"},{"value":"RPLA4"}],"olnNames":[{"value":"YDR382W"}]}],"alphafold_very_low_content":0.23636363636363636,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":110,"type":"D"}],"Structural state":[{"start":1,"end":110,"type":"D"}],"Molecular function":[{"start":1,"end":110,"type":"F"}]}},{"disprot_id":"DP03377","acc":"Q7T2G3","creator":"smribeiro","date":"2021-06-15T15:30:28.696Z","features":{"pfam":[{"id":"PF00250","name":"Forkhead domain","start":181,"end":262}],"gene3D":[]},"length":623,"name":"Forkhead box M1","ncbi_taxon_id":7955,"organism":"Danio rerio","regions":[{"start":571,"end":623,"reference_id":"31134895","reference_source":"pmid","reference_html":"An order-to-disorder structural switch activates the FoxM1 transcription factor. <i> Marceau AH, Brison CM, Nerli S, Arsenault HE, McShan AC, Chen E, Lee HW, Benanti JA, Sgourakis NG, Rubin SM. </i> Elife, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03377r001","statement":[{"text":"The data support the conclusion that both the phosphorylated and unphosphorylated isolated TAD are primarily unstructured. ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-25T12:41:08.115Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":569,"end":593,"reference_id":"31134895","reference_source":"pmid","reference_html":"An order-to-disorder structural switch activates the FoxM1 transcription factor. <i> Marceau AH, Brison CM, Nerli S, Arsenault HE, McShan AC, Chen E, Lee HW, Benanti JA, Sgourakis NG, Rubin SM. </i> Elife, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03377r002","statement":[{"text":"These results in comparison with the NMR data for the NRD-TAD complex (Figure 2B–2D) suggest that the β-hairpin structure of the TAD is adopted upon binding to the NRD.","type":"Results"},{"text":"The observations that the NRD and TAD appear unstructured when alone suggest that the repressive NRD-TAD association drives the domains to fold into the inhibitory conformation, and conversely that activation of FoxM1 is marked by an order-to-disorder structural transition.","type":"Results"},{"text":"We find significant structural order within a set of residues including sequences from both the NRD and TAD. Importantly, within this ordered region, the backbone chemical shifts for 71 out of 75 non-proline residues were assigned. Notably, the SSI analysis suggests that a stretch of residues in the TAD adopts a β-hairpin conformation, which contrasts the helical TAD structures typically observed in complexes with co-activator domains","type":"Results"},{"text":"FoxM1 demonstrates a new example in which the order-to-disorder transition occurs coincident with modulation of an intramolecular association between domains. This plasticity of disordered domains and the ability to regulate the plasticity through posttranslational modifications explains why intrinsically disordered proteins are so well suited to regulate biological function.","type":"Discussion"}],"cross_refs":[{"db":"PDB","id":"6OSW"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-25T12:41:09.132Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":582,"end":592,"reference_id":"31134895","reference_source":"pmid","reference_html":"An order-to-disorder structural switch activates the FoxM1 transcription factor. <i> Marceau AH, Brison CM, Nerli S, Arsenault HE, McShan AC, Chen E, Lee HW, Benanti JA, Sgourakis NG, Rubin SM. </i> Elife, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03377r003","statement":[{"text":" The NRD-TAD structure consists of a five-stranded pleated β-sheet and a single α-helix. Three of the beta strands (β1-β3) are from sequences in the NRD, and two additional strands are from sequences in the TAD (β4-β5) ","type":"Results"},{"text":"The fact that both the NRD and TAD contribute essential residues to the hydrophobic core suggests the requirement of an association for forming the observed structure of both domains. ","type":"Results"},{"text":"The structured region of the TAD consists of a 12 amino acid sequence that adopts a β-hairpin conformation and binds the NRD by extending the β-sheet","type":"Results"}],"cross_refs":[{"db":"PDB","id":"60SW"}],"interaction_partner":[{"db":"UniProt","id":"Q7T2G3","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-25T12:41:09.930Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":582,"end":592,"reference_id":"31134895","reference_source":"pmid","reference_html":"An order-to-disorder structural switch activates the FoxM1 transcription factor. <i> Marceau AH, Brison CM, Nerli S, Arsenault HE, McShan AC, Chen E, Lee HW, Benanti JA, Sgourakis NG, Rubin SM. </i> Elife, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"smribeiro","curator_name":"Sandra Macedo-Ribeiro","curator_orcid":"0000-0002-7698-1170","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03377r004","statement":[{"text":"We conclude that Ser715 phosphorylation by Plk1 is necessary and sufficient for inhibiting the NRD-TAD association. ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-25T12:41:10.785Z"},"ec_go":"IPI","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":4,"released":"2023_12","sequence":"MRESPRRPIILKRRKLPFLKSESDLGCDEADGTRCKTTSTQSTARSFPDGIRVMDHPTMPDTQVVVIPKSADLQSVISVLTAKGKECGPQGRNKFILLSGDTSLEESKTLGCFSTELGSELGKVKKESECFPLDDSLTNIQWLGKMSSDGLGSEKCPNKDNPNDSQQQSKGPEKENDPHSERPPYSYMAMIQFAINSKNNRHMTLKEIYNWIEDHFPYFRDIAKPGWKNSIRHNLSLHDMFIRETSPDGKISYWTIRPEANRCLTLDQVYKPLGDPLTPTCPQIPQVAIHQQQKRGAPELKKAIPALGGTERKMKPLLPRTDSYLVPIQLPLGQSLFLPTSSPVSLSTPPQTQNSSTPSSSKRVRIAPKVSQSDLSSVLLCKPASQEIKEEPVFQPVTSSEAPPPKSRRTDNSSSRRKQRLVLPATEEPVLLYPDSTLFDSGVISDISTFQDTREADPKPELDSPNREYSFKTPIKSSHPSSSTPSKLPTVTLEPWRITPVGKGGVLDFSPIRTPTGPHVTPQRNQHTSLSFTSTPFKELPLFNSPRELLTCSRSSPKRSAPACSRELLQVGAANRSLTEGFVLDTMNDSLSKILVDISFSGLEDEDLGMGNISWSQFIPELK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Actinopterygii","Neopterygii","Teleostei","Ostariophysi","Cypriniformes","Danionidae","Danioninae","Danio"],"dataset":[],"UniParc":"UPI00001B06EC","uniref100":"UniRef100_Q7T2G3","uniref90":"UniRef90_Q7T2G3","uniref50":"UniRef50_A0A2K6M9P2","genes":[{"name":{"value":"foxm1l","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAH54560.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAH54560.1"}},{"code":"ECO:0000313","source":{"name":"RefSeq","id":"NP_957391.1","url":"https://www.ncbi.nlm.nih.gov/protein/NP_957391.1"}}]},"synonyms":[{"value":"zgc:63854","evidences":[{"code":"ECO:0000313","source":{"name":"RefSeq","id":"NP_957391.1","url":"https://www.ncbi.nlm.nih.gov/protein/NP_957391.1"}}]}],"orfNames":[{"value":"SO:0001217","evidences":[{"code":"ECO:0000313","source":{"name":"ZFIN","id":"ZDB-GENE-040426-1275","url":"http://zfin.org/cgi-bin/webdriver?MIval=aa-markerview.apg&OID=ZDB-GENE-040426-1275"}}]}],"olnNames":[{"value":"foxm1","evidences":[{"code":"ECO:0000313","source":{"name":"RefSeq","id":"NP_957391.1","url":"https://www.ncbi.nlm.nih.gov/protein/NP_957391.1"}},{"code":"ECO:0000313","source":{"name":"ZFIN","id":"ZDB-GENE-040426-1275","url":"http://zfin.org/cgi-bin/webdriver?MIval=aa-markerview.apg&OID=ZDB-GENE-040426-1275"}}]}]}],"alphafold_very_low_content":0.7046548956661316,"disorder_content":0.08507223113964688,"disprot_consensus":{"full":[{"start":569,"end":593,"type":"T"},{"start":594,"end":623,"type":"D"}],"Structural state":[{"start":571,"end":623,"type":"D"}],"Structural transition":[{"start":569,"end":593,"type":"T"}],"Molecular function":[{"start":582,"end":592,"type":"F"}]}},{"disprot_id":"DP03378","acc":"P20849","creator":"lchemes","date":"2021-06-15T22:51:40.617Z","features":{"pfam":[{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":268,"end":324},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":358,"end":403},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":416,"end":472},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":697,"end":755},{"id":"PF01391","name":"Collagen triple helix repeat (20 copies)","start":790,"end":847}],"gene3D":[]},"length":921,"name":"Collagen alpha-1(IX) chain","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":24,"end":41,"reference_id":"17553797","reference_source":"pmid","reference_html":"Crystal structure of the N-terminal NC4 domain of collagen IX, a zinc binding member of the laminin-neurexin-sex hormone binding globulin (LNS) domain family. <i> Leppänen VM, Tossavainen H, Permi P, Lehtiö L, Rönnholm G, Goldman A, Kilpelaïnen I, Pihlajamaa T. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2UUR"}],"region_id":"DP03378r001","statement":[{"text":"Except for residues 1–18, 25–29, and 234–245, the main chain is well defined by the electron density","type":"Results"},{"text":"The first ~30 residues, bearing the major heparin binding site (7), are unique for NC4. Unfortunately these N-terminal residues were largely unresolved both in the crystal structure and NMR chemical shift assignments","type":"Discussion"},{"text":"Residues 1-18 mentioned by the authors corresponds to residues 24-41 of the uniprot entry. The numbering used by the authors starts after the signal peptide.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-21T16:13:45.315Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":24,"end":40,"reference_id":"17553797","reference_source":"pmid","reference_html":"Crystal structure of the N-terminal NC4 domain of collagen IX, a zinc binding member of the laminin-neurexin-sex hormone binding globulin (LNS) domain family. <i> Leppänen VM, Tossavainen H, Permi P, Lehtiö L, Rönnholm G, Goldman A, Kilpelaïnen I, Pihlajamaa T. </i> J Biol Chem, 2007","date":"2022-03-08T13:57:25.747Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0030246","term_name":"carbohydrate binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006082","ec_ontology":"ECO","ec_name":"affinity chromatography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":4,"region_id":"DP03378r003","statement":[{"text":"NC4 Lacking the N Terminus Has Only Residual Heparin Affinity—To verify our initial mapping of the heparin binding site of NC4 to the N terminus of the domain (7), we created mutant NC4Ndel lacking the first 17 residues of the domain. Analytical heparin affinity chromatography showed that N-terminally truncated NC4 could not bind to the column at a physiological salt concentration. When bound to the column in a buffer containing no added NaCl, NC4Ndel eluted at 0.13 M salt compared with the 0.31 M salt required for elution of wild-type NC4 (Fig. 5).","type":"Results"},{"text":"In vitro mutagenesis (Stratagene) was used to create a mutant form of NC4, termed NC4Ndel, lacking the first 17 residues of the mature polypeptide","type":"Methods"},{"text":"The mutant used by the authors lacks residues 24-40 of the uniprot entry of this protein","type":"Curator statement"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.\" [GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"ChEBI","id":"28304","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-14T15:41:20.156Z"}},{"start":24,"end":42,"reference_id":"15047691","reference_source":"pmid","reference_html":"Characterization of recombinant amino-terminal NC4 domain of human collagen IX: interaction with glycosaminoglycans and cartilage oligomeric matrix protein. <i> Pihlajamaa T, Lankinen H, Ylöstalo J, Valmu L, Jäälinoja J, Zaucke F, Spitznagel L, Gösling S, Puustinen A, Mörgelin M, Peränen J, Maurer P, Ala-Kokko L, Kilpelaïnen I. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"GO:0030246","term_name":"carbohydrate binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03378r004","statement":[{"text":"In an attempt to characterize the NC4 domain in more detail, we set up a prokaryotic expression system to produce the domain. The purified 27.5-kDa product was analyzed for its glycosaminoglycan-binding potential by surface plasmon resonance and solid-state assays. The results show that the NC4 domain of collagen IX specifically binds heparin with a Kd of 0.6 µM, and the full-length recombinant collagen IX has an even stronger interaction with heparin, with an apparent Kd of 3.6 nM. The heparin-binding site of the NC4 domain was located in the extreme N terminus, containing a heparin-binding consensus sequence.","type":"Abstract"},{"text":"Identification of the Heparin-binding Region of the NC4 Domain—Alkylated rNC4 was digested with V8 protease and the resulting mixture of peptides subjected to heparin affinity chromatography. Analysis of the peptide mixture by MALDI-TOF mass spectrometry along with unbound and bound material from the affinity chromatography revealed that the extreme N-terminal peptide (amino acids 1–19, monoisotopic mass 2098.078) was able to bind to heparin, whereas other fragments were not. ","type":"Results"},{"text":"Our results show that the NC4 domain can now be added to the growing list of extracellular matrix proteins that interact with heparin or heparan sulfate","type":"Discussion"},{"text":"The peptide identified by the authors corresponds to residues 24-42 of the uniprot entry of this protein","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-21T16:13:50.957Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.\" [GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":24,"end":42,"reference_id":"15047691","reference_source":"pmid","reference_html":"Characterization of recombinant amino-terminal NC4 domain of human collagen IX: interaction with glycosaminoglycans and cartilage oligomeric matrix protein. <i> Pihlajamaa T, Lankinen H, Ylöstalo J, Valmu L, Jäälinoja J, Zaucke F, Spitznagel L, Gösling S, Puustinen A, Mörgelin M, Peränen J, Maurer P, Ala-Kokko L, Kilpelaïnen I. </i> J Biol Chem, 2004","date":"2022-03-08T13:57:04.259Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0030246","term_name":"carbohydrate binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006082","ec_ontology":"ECO","ec_name":"affinity chromatography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":4,"region_id":"DP03378r005","statement":[{"text":"In an attempt to characterize the NC4 domain in more detail, we set up a prokaryotic expression system to produce the domain. The purified 27.5-kDa product was analyzed for its glycosaminoglycan-binding potential by surface plasmon resonance and solid-state assays. The results show that the NC4 domain of collagen IX specifically binds heparin with a Kd of 0.6 µM, and the full-length recombinant collagen IX has an even stronger interaction with heparin, with an apparent Kd of 3.6 nM. The heparin-binding site of the NC4 domain was located in the extreme N terminus, containing a heparin-binding consensus sequence.","type":"Abstract"},{"text":"The N-terminal 19-amino acid fragment was subsequently prepared as a synthetic peptide (peptide 1–19), which was shown to bind to heparin-Sepharose and elute upon introduction of about a 0.15 M concentration of NaCl (i.e. a 40% smaller concentration than was required for the elution of native rNC4). CD analysis of peptide 1–19 indicated that it was largely devoid of secondary structure (data not shown).","type":"Results"},{"text":"Our results show that the NC4 domain can now be added to the growing list of extracellular matrix proteins that interact with heparin or heparan sulfate.","type":"Discussion"},{"text":"The peptide identified by the authors corresponds to residues 24-42 of the uniprot entry of this protein","type":"Curator statement"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.\" [GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"ChEBI","id":"28304","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-14T15:41:24.147Z"}},{"start":26,"end":31,"reference_id":"15047691","reference_source":"pmid","reference_html":"Characterization of recombinant amino-terminal NC4 domain of human collagen IX: interaction with glycosaminoglycans and cartilage oligomeric matrix protein. <i> Pihlajamaa T, Lankinen H, Ylöstalo J, Valmu L, Jäälinoja J, Zaucke F, Spitznagel L, Gösling S, Puustinen A, Mörgelin M, Peränen J, Maurer P, Ala-Kokko L, Kilpelaïnen I. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"GO:0030246","term_name":"carbohydrate binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03378r006","statement":[{"text":"The results show that the NC4 domain of collagen IX specifically binds heparin with a Kd of 0.6 µM, and the full-length recombinant collagen IX has an even stronger interaction with heparin, with an apparent Kd of 3.6 nM. The heparin-binding site of the NC4 domain was located in the extreme N terminus, containing a heparin-binding consensus sequence.","type":"Abstract"},{"text":"A mutant form of rNC4, carrying a sequence NGL in place of the basic amino acid sequence KRR of the suspected heparin binding site, was created. Using heparin affinity chromatography, it was demonstrated that this mutant rNC4 was unable to interact with heparin at physiological conditions. Comparison of the mutant rNC4 with wild-type rNC4 by far-UV CD analysis (data not shown) and by FTIR spectroscopy (Fig. 6) showed that the mutation did not affect the secondary structure of the NC4 domain","type":"Results"},{"text":"Collagen XI, for example, possesses several heparin-binding sequences, two of which comply with the heparin-binding consensus sequence XBBXBX, where B denotes a basic amino acid and X is any other amino acid (25). A sequence KRRPRF matching this consensus is present in the extreme N-terminal region of the NC4 domain of collagen IX and is indeed shown here to be the site of interaction of the domain with heparin. This sequence motif is also present in the N terminus of the mouse collagen a1(IX) chain (26). Comparison of this sequence of NC4 with a reported distribution of residues in known heparin-binding proteins (27) further implicates the sequence as a potential heparin-binding site.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-21T16:13:48.075Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.\" [GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":24,"end":42,"reference_id":"15047691","reference_source":"pmid","reference_html":"Characterization of recombinant amino-terminal NC4 domain of human collagen IX: interaction with glycosaminoglycans and cartilage oligomeric matrix protein. <i> Pihlajamaa T, Lankinen H, Ylöstalo J, Valmu L, Jäälinoja J, Zaucke F, Spitznagel L, Gösling S, Puustinen A, Mörgelin M, Peränen J, Maurer P, Ala-Kokko L, Kilpelaïnen I. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P35444","partner_start":null,"partner_end":null}],"region_id":"DP03378r007","statement":[{"text":"To analyze the interaction of COMP in a more reliable one-to-one situation, we used a biotinylated recombinant 57-kDa C-terminal fragment of the COMP monomer (COMP T3 TC) to coat a hydrophobic sensor chip. Soluble rNC4 was injected over the surface at various concentrations, and a Kd of 0.23 ± 0.11 M","type":"Results"},{"text":"The same sensor chip was also used to analyze the effect of excess heparin on the interaction of COMP T3+TC with rNC4 and rcIX. Heparin was found to inhibit both interactions at low micromolar concentrations. Preincubation of 20 nM rcIX with 4 M heparin (molecular mass 6 kDa) prior to injection over the coated surface resulted in more than 99% inhibition of the interaction with COMP T3+TC, and 50% inhibition was achieved with a heparin concentration lower than 0.1 M.","type":"Results"},{"text":"Somewhat surprisingly, our results show that COMP and heparin compete for the same binding site or overlapping ones in the NC4 domain. Similarly, we were able to block the interaction of full-length rcIX with the C-terminal domain of COMP using relatively low heparin levels.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-21T16:13:46.733Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":7,"released":"2021_12","sequence":"MKTCWKIPVFFFVCSFLEPWASAAVKRRPRFPVNSNSNGGNELCPKIRIGQDDLPGFDLISQFQVDKAASRRAIQRVVGSATLQVAYKLGNNVDFRIPTRNLYPSGLPEEYSFLTTFRMTGSTLKKNWNIWQIQDSSGKEQVGIKINGQTQSVVFSYKGLDGSLQTAAFSNLSSLFDSQWHKIMIGVERSSATLFVDCNRIESLPIKPRGPIDIDGFAVLGKLADNPQVSVPFELQWMLIHCDPLRPRRETCHELPARITPSQTTDERGPPGEQGPPGPPGPPGVPGIDGIDGDRGPKGPPGPPGPAGEPGKPGAPGKPGTPGADGLTGPDGSPGSIGSKGQKGEPGVPGSRGFPGRGIPGPPGPPGTAGLPGELGRVGPVGDPGRRGPPGPPGPPGPRGTIGFHDGDPLCPNACPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGAQGLRGITGIVGDKGEKGARGLDGEPGPQGLPGAPGDQGQRGPPGEAGPKGDRGAEGARGIPGLPGPKGDTGLPGVDGRDGIPGMPGTKGEPGKPGPPGDAGLQGLPGVPGIPGAKGVAGEKGSTGAPGKPGQMGNSGKPGQQGPPGEVGPRGPQGLPGSRGELGPVGSPGLPGKLGSLGSPGLPGLPGPPGLPGMKGDRGVVGEPGPKGEQGASGEEGEAGERGELGDIGLPGPKGSAGNPGEPGLRGPEGSRGLPGVEGPRGPPGPRGVQGEQGATGLPGVQGPPGRAPTDQHIKQVCMRVIQEHFAEMAASLKRPDSGATGLPGRPGPPGPPGPPGENGFPGQMGIRGLPGIKGPPGALGLRGPKGDLGEKGERGPPGRGPNGLPGAIGLPGDPGPASYGRNGRDGERGPPGVAGIPGVPGPPGPPGLPGFCEPASCTMQAGQRAFNKGPDP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000016A716","uniref100":"UniRef100_P20849","uniref90":"UniRef90_P20849","uniref50":"UniRef50_P20849","genes":[{"name":{"value":"COL9A1"}}],"alphafold_very_low_content":0.31813246471226925,"disorder_content":0.019543973941368076,"disprot_consensus":{"full":[{"start":24,"end":41,"type":"D"},{"start":42,"end":42,"type":"F"}],"Structural state":[{"start":24,"end":41,"type":"D"}],"Molecular function":[{"start":24,"end":42,"type":"F"}]}},{"disprot_id":"DP03379","acc":"Q14766","creator":"lchemes","date":"2021-06-16T05:20:18.923Z","features":{"pfam":[{"id":"PF00683","name":"TB domain","start":567,"end":609},{"id":"PF00683","name":"TB domain","start":688,"end":729},{"id":"PF00683","name":"TB domain","start":1359,"end":1401},{"id":"PF00683","name":"TB domain","start":1535,"end":1577},{"id":"PF07645","name":"Calcium-binding EGF domain","start":626,"end":665},{"id":"PF07645","name":"Calcium-binding EGF domain","start":874,"end":913},{"id":"PF07645","name":"Calcium-binding EGF domain","start":915,"end":955},{"id":"PF07645","name":"Calcium-binding EGF domain","start":957,"end":996},{"id":"PF07645","name":"Calcium-binding EGF domain","start":998,"end":1035},{"id":"PF07645","name":"Calcium-binding EGF domain","start":1120,"end":1159},{"id":"PF07645","name":"Calcium-binding EGF domain","start":1161,"end":1200},{"id":"PF07645","name":"Calcium-binding EGF domain","start":1424,"end":1465},{"id":"PF07645","name":"Calcium-binding EGF domain","start":1467,"end":1506},{"id":"PF07645","name":"Calcium-binding EGF domain","start":1662,"end":1705},{"id":"PF12662","name":"Complement Clr-like EGF-like","start":1059,"end":1082},{"id":"PF12662","name":"Complement Clr-like EGF-like","start":1224,"end":1247},{"id":"PF12662","name":"Complement Clr-like EGF-like","start":1266,"end":1289}],"gene3D":[]},"length":1721,"name":"Latent-transforming growth factor beta-binding protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1507,"end":1522,"reference_id":"24489852","reference_source":"pmid","reference_html":"NMR spectroscopic and bioinformatic analyses of the LTBP1 C-terminus reveal a highly dynamic domain organisation. <i> Robertson IB, Handford PA, Redfield C. </i> PLoS One, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"cross_refs":[{"db":"BMRB","id":"19322"}],"region_id":"DP03379r001","statement":[{"text":"15N relaxation studies further demonstrate that the three interdomain regions act as flexible linkers, allowing a wide range of motion between the well-structured domains. This work is consistent with the LTBP1 C-terminus adopting a flexible ‘‘knotted rope’’ structure, which may facilitate cell matrix interactions, and the accessibility to proteases or other factors that could contribute to TGFb activation.","type":"Abstract"},{"text":"LTBP sequences all contain linker regions of 17 or more amino acids between the cbEGF14 and TB3 domains, and 34 or many more residues between the TB3 and EGF3 domains. These long linker regions have no clear homology to previously identified domains and are not seen between homologous TB/EGF/cbEGF domains in fibrillin.These sequences are poorly conserved between LTBP variants, suggesting that these regions may be unstructured and potentially flexible.","type":"Results"},{"text":"For residues in the linkers connecting cbEGF14 to TB3 and TB3 to EGF3 and for the 13 C-terminal residues following cbEGF15, NOE ratios below 0.3 are observed, indicating significant amplitude backbone dynamics on a sub-nanosecond timescale. This high degree of flexibility and lack of well-defined structure is consistent with the poor sequence conservation of these regions (Figure 2).","type":"Results"},{"text":"The numerous flexible linkers identified would make many regions of the LTBP1 C-terminus unsuitable for crystallographic\nstudies, or other structural investigations that rely on rigid body modelling. The data presented here demonstrate that the Cterminus of LTBP1 behaves like a ‘‘knotted rope’’ in solution, where the linkers either side of the TB3 domain act as the highly\nflexible ‘‘rope’’ allowing the TB3 domain and EGF3-cbEGF15 domain pair, (the ‘‘knots’’ in this analogy), to move freely relative to each other and the rest of LTBP1. The presence of flexible linkers mean that long-range interdomain interactions, such as EGF3 interacting with cbEGF14 or other parts of the LTBP1 molecule, cannot be excluded by these studies.\n","type":"Discussion"},{"text":"Numbering needs to be shifted by one to correspond to the UNIPROT numbering, i.e. the C-terminal residue 1722 mentioned in the paper corresponds to residue 1721 in the uniprot sequence","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T08:47:04.308Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1582,"end":1623,"reference_id":"24489852","reference_source":"pmid","reference_html":"NMR spectroscopic and bioinformatic analyses of the LTBP1 C-terminus reveal a highly dynamic domain organisation. <i> Robertson IB, Handford PA, Redfield C. </i> PLoS One, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"cross_refs":[{"db":"BMRB","id":"19322"}],"region_id":"DP03379r002","statement":[{"text":"15N relaxation studies further demonstrate that the three interdomain regions act as flexible linkers, allowing a wide range of motion between the well-structured domains. This work is consistent with the LTBP1 C-terminus adopting a flexible ‘‘knotted rope’’ structure, which may facilitate cell matrix interactions, and the accessibility to proteases or other factors that could contribute to TGFb activation.","type":"Abstract"},{"text":"LTBP sequences all contain linker regions of 17 or more amino acids between the cbEGF14 and TB3 domains, and 34 or many more residues between the TB3 and EGF3 domains. These long linker regions have no clear homology to previously identified domains and are not seen between homologous TB/EGF/cbEGF domains in fibrillin.These sequences are poorly conserved between LTBP variants, suggesting that these regions may be unstructured and potentially flexible.","type":"Results"},{"text":"For residues in the linkers connecting cbEGF14 to TB3 and TB3 to EGF3 and for the 13 C-terminal residues following cbEGF15, NOE ratios below 0.3 are observed, indicating significant amplitude backbone dynamics on a sub-nanosecond timescale. This high degree of flexibility and lack of well-defined structure is consistent with the poor sequence conservation of these regions (Figure 2).","type":"Results"},{"text":"The numerous flexible linkers identified would make many regions of the LTBP1 C-terminus unsuitable for crystallographic\nstudies, or other structural investigations that rely on rigid body modelling. The data presented here demonstrate that the Cterminus of LTBP1 behaves like a ‘‘knotted rope’’ in solution, where the linkers either side of the TB3 domain act as the highly\nflexible ‘‘rope’’ allowing the TB3 domain and EGF3-cbEGF15 domain pair, (the ‘‘knots’’ in this analogy), to move freely relative to each other and the rest of LTBP1. The presence of flexible linkers mean that long-range interdomain interactions, such as EGF3 interacting with cbEGF14 or other parts of the LTBP1 molecule, cannot be excluded by these studies.\n","type":"Discussion"},{"text":"Numbering needs to be shifted by one to correspond to the UNIPROT numbering, i.e. the C-terminal residue 1722 mentioned in the paper corresponds to residue 1721 in the uniprot sequence","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T08:55:37.592Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1709,"end":1721,"reference_id":"24489852","reference_source":"pmid","reference_html":"NMR spectroscopic and bioinformatic analyses of the LTBP1 C-terminus reveal a highly dynamic domain organisation. <i> Robertson IB, Handford PA, Redfield C. </i> PLoS One, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"cross_refs":[{"db":"BMRB","id":"19322"}],"region_id":"DP03379r003","statement":[{"text":"15N relaxation studies further demonstrate that the three interdomain regions act as flexible linkers, allowing a wide range of motion between the well-structured domains. This work is consistent with the LTBP1 C-terminus adopting a flexible ‘‘knotted rope’’ structure, which may facilitate cell matrix interactions, and the accessibility to proteases or other factors that could contribute to TGFb activation.","type":"Abstract"},{"text":"LTBP sequences all contain linker regions of 17 or more amino acids between the cbEGF14 and TB3 domains, and 34 or many more residues between the TB3 and EGF3 domains. These long linker regions have no clear homology to previously identified domains and are not seen between homologous TB/EGF/cbEGF domains in fibrillin.These sequences are poorly conserved between LTBP variants, suggesting that these regions may be unstructured and potentially flexible.","type":"Results"},{"text":"For residues in the linkers connecting cbEGF14 to TB3 and TB3 to EGF3 and for the 13 C-terminal residues following cbEGF15, NOE ratios below 0.3 are observed, indicating significant amplitude backbone dynamics on a sub-nanosecond timescale. This high degree of flexibility and lack of well-defined structure is consistent with the poor sequence conservation of these regions (Figure 2).","type":"Results"},{"text":"The numerous flexible linkers identified would make many regions of the LTBP1 C-terminus unsuitable for crystallographic\nstudies, or other structural investigations that rely on rigid body modelling. The data presented here demonstrate that the Cterminus of LTBP1 behaves like a ‘‘knotted rope’’ in solution, where the linkers either side of the TB3 domain act as the highly\nflexible ‘‘rope’’ allowing the TB3 domain and EGF3-cbEGF15 domain pair, (the ‘‘knots’’ in this analogy), to move freely relative to each other and the rest of LTBP1. The presence of flexible linkers mean that long-range interdomain interactions, such as EGF3 interacting with cbEGF14 or other parts of the LTBP1 molecule, cannot be excluded by these studies.\n","type":"Discussion"},{"text":"Numbering needs to be shifted by one to correspond to the UNIPROT numbering, i.e. the C-terminal residue 1722 mentioned in the paper corresponds to residue 1721 in the uniprot sequence","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T08:55:40.026Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1507,"end":1521,"reference_id":"24489852","reference_source":"pmid","reference_html":"NMR spectroscopic and bioinformatic analyses of the LTBP1 C-terminus reveal a highly dynamic domain organisation. <i> Robertson IB, Handford PA, Redfield C. </i> PLoS One, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":3,"cross_refs":[{"db":"BMRB","id":"19322"}],"region_id":"DP03379r004","statement":[{"text":"15N relaxation studies further demonstrate that the three interdomain regions act as flexible linkers, allowing a wide range of motion between the well-structured domains. This work is consistent with the LTBP1 C-terminus adopting a flexible ‘‘knotted rope’’ structure, which may facilitate cell matrix interactions, and the accessibility to proteases or other factors that could contribute to TGFb activation.","type":"Abstract"},{"text":"LTBP sequences all contain linker regions of 17 or more amino acids between the cbEGF14 and TB3 domains, and 34 or many more residues between the TB3 and EGF3 domains. These long linker regions have no clear homology to previously identified domains and are not seen between homologous TB/EGF/cbEGF domains in fibrillin.These sequences are poorly conserved between LTBP variants, suggesting that these regions may be unstructured and potentially flexible.","type":"Results"},{"text":"For residues in the linkers connecting cbEGF14 to TB3 and TB3 to EGF3 and for the 13 C-terminal residues following cbEGF15, NOE ratios below 0.3 are observed, indicating significant amplitude backbone dynamics on a sub-nanosecond timescale. This high degree of flexibility and lack of well-defined structure is consistent with the poor sequence conservation of these regions (Figure 2).","type":"Results"},{"text":"The numerous flexible linkers identified would make many regions of the LTBP1 C-terminus unsuitable for crystallographic\nstudies, or other structural investigations that rely on rigid body modelling. The data presented here demonstrate that the Cterminus of LTBP1 behaves like a ‘‘knotted rope’’ in solution, where the linkers either side of the TB3 domain act as the highly\nflexible ‘‘rope’’ allowing the TB3 domain and EGF3-cbEGF15 domain pair, (the ‘‘knots’’ in this analogy), to move freely relative to each other and the rest of LTBP1. The presence of flexible linkers mean that long-range interdomain interactions, such as EGF3 interacting with cbEGF14 or other parts of the LTBP1 molecule, cannot be excluded by these studies.\n","type":"Discussion"},{"text":"Numbering needs to be shifted by one to correspond to the UNIPROT numbering, i.e. the C-terminal residue 1722 mentioned in the paper corresponds to residue 1721 in the uniprot sequence","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T08:49:04.707Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":1582,"end":1623,"reference_id":"24489852","reference_source":"pmid","reference_html":"NMR spectroscopic and bioinformatic analyses of the LTBP1 C-terminus reveal a highly dynamic domain organisation. <i> Robertson IB, Handford PA, Redfield C. </i> PLoS One, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":3,"cross_refs":[{"db":"BMRB","id":"19322"}],"region_id":"DP03379r005","statement":[{"text":"15N relaxation studies further demonstrate that the three interdomain regions act as flexible linkers, allowing a wide range of motion between the well-structured domains. This work is consistent with the LTBP1 C-terminus adopting a flexible ‘‘knotted rope’’ structure, which may facilitate cell matrix interactions, and the accessibility to proteases or other factors that could contribute to TGFb activation.","type":"Abstract"},{"text":"LTBP sequences all contain linker regions of 17 or more amino acids between the cbEGF14 and TB3 domains, and 34 or many more residues between the TB3 and EGF3 domains. These long linker regions have no clear homology to previously identified domains and are not seen between homologous TB/EGF/cbEGF domains in fibrillin.These sequences are poorly conserved between LTBP variants, suggesting that these regions may be unstructured and potentially flexible.","type":"Results"},{"text":"For residues in the linkers connecting cbEGF14 to TB3 and TB3 to EGF3 and for the 13 C-terminal residues following cbEGF15, NOE ratios below 0.3 are observed, indicating significant amplitude backbone dynamics on a sub-nanosecond timescale. This high degree of flexibility and lack of well-defined structure is consistent with the poor sequence conservation of these regions (Figure 2).","type":"Results"},{"text":"The numerous flexible linkers identified would make many regions of the LTBP1 C-terminus unsuitable for crystallographic\nstudies, or other structural investigations that rely on rigid body modelling. The data presented here demonstrate that the Cterminus of LTBP1 behaves like a ‘‘knotted rope’’ in solution, where the linkers either side of the TB3 domain act as the highly\nflexible ‘‘rope’’ allowing the TB3 domain and EGF3-cbEGF15 domain pair, (the ‘‘knots’’ in this analogy), to move freely relative to each other and the rest of LTBP1. The presence of flexible linkers mean that long-range interdomain interactions, such as EGF3 interacting with cbEGF14 or other parts of the LTBP1 molecule, cannot be excluded by these studies.\n","type":"Discussion"},{"text":"Numbering needs to be shifted by one to correspond to the UNIPROT numbering, i.e. the C-terminal residue 1722 mentioned in the paper corresponds to residue 1721 in the uniprot sequence","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T09:04:35.333Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":1618,"end":1624,"reference_id":"28669633","reference_source":"pmid","reference_html":"The N-Terminal Region of Fibrillin-1 Mediates a Bipartite Interaction with LTBP1. <i> Robertson IB, Dias HF, Osuch IH, Lowe ED, Jensen SA, Redfield C, Handford PA. </i> Structure, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2023_06","version":3,"interaction_partner":[{"db":"UniProt","id":"P35555","partner_start":null,"partner_end":null}],"region_id":"DP03379r006","statement":[{"text":"LTBP1 anchors itself to FBN1 using two independent epitopes. As part of this mechanism, a flexible pivot adjacent to the FBN1/LTBP1 binding site allows LTBP1 to make contacts with different ECM networks while presumably facilitating a force-induced/traction-based TGF-b activation mechanism.","type":"Abstract"},{"text":"We observed a specific interaction between a three-domain C-terminal LTBP1TB3cbEGF15 construct and a four-domain FBN1E2cbEGF1 construct using both surface plasmon resonance (SPR) and a plate-based binding assay (Figures 1B and 1C).","type":"Results"},{"text":"Dissociation constants (Kd) of _100 ± 20 and _300 ± 100 mM for the interaction of FBN1E2cbEGF1 with LTBP1E3cbEGF15, and LTBP1cbEGF14TB3, respectively, can be estimated from the SPR data (Figure S2). In contrast, the binding of LTBP1TB3E3 to FBN1E2cbEGF1 gives a non-linear Scatchard plot (Figure S2); this is not surprising as the multi-site mode of interaction for this LTBP1 construct may give rise to complicated binding kinetics. Nevertheless, a Kd of _0.5–1 mM can be estimated from the SPR data at the lowest analyte concentrations (which are similar to concentrations used in previous studies [Massam- Wu et al., 2010; Ono et al., 2009]). Thus, the pair of interaction sites between FBN1 and LTBP1 results in a substantial enhancement in overall binding affinity. A cartoon summarizing our proposed binding model based on our domain dissection data is shown in Figure 2C.","type":"Results"},{"text":"The necessity of the linker for the binding function is revealed by fragment-based dissection of the interacting regions. The presence of the linker allows affinity enhancement of this interaction, and the linker region is further shown to make contacts with FBN1 through NMR experiments.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T09:00:53.998Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1618,"end":1624,"reference_id":"28669633","reference_source":"pmid","reference_html":"The N-Terminal Region of Fibrillin-1 Mediates a Bipartite Interaction with LTBP1. <i> Robertson IB, Dias HF, Osuch IH, Lowe ED, Jensen SA, Redfield C, Handford PA. </i> Structure, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":3,"interaction_partner":[{"db":"UniProt","id":"P35555","partner_start":null,"partner_end":null}],"region_id":"DP03379r007","statement":[{"text":"LTBP1 anchors itself to FBN1 using two independent epitopes. As part of this mechanism, a flexible pivot adjacent to the FBN1/LTBP1 binding site allows LTBP1 to make contacts with different ECM networks while presumably facilitating a force-induced/traction-based TGF-b activation mechanism.","type":"Abstract"},{"text":"Titration of the four-domain FBN1E2cbEGF1 construct with the two-domain LTBP1 construct, LTBP1E3cbEGF15, shows specific broadening effects rather than chemical shift changes; this indicates intermediate/slow exchange behavior consistent with the stronger interaction between this pair of protein constructs seen by SPR (Figures 3C and 3D). These titrations show that residues located in the EGF3 domain of LTBP1, and some of the unstructured region that immediately precedes EGF3, interact with residues located in the Hyb1 and cbEGF1 domains of FBN1 (Figures 3C and 3D).","type":"Results"},{"text":"The boundaries of the linker region interacting with FBN1 was deduced from chemical shift and intensity changes shown in Figure 3 C and D.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T09:00:22.192Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1578,"end":1624,"reference_id":"28669633","reference_source":"pmid","reference_html":"The N-Terminal Region of Fibrillin-1 Mediates a Bipartite Interaction with LTBP1. <i> Robertson IB, Dias HF, Osuch IH, Lowe ED, Jensen SA, Redfield C, Handford PA. </i> Structure, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":3,"region_id":"DP03379r008","statement":[{"text":"LTBP1 anchors itself to FBN1 using two independent epitopes. As part of this mechanism, a flexible pivot adjacent to the FBN1/LTBP1 binding site allows LTBP1 to make contacts with different ECM networks while presumably facilitating a force-induced/traction-based TGF-b activation mechanism.","type":"Abstract"},{"text":"In the HADDOCK model of the FBN1/LTBP1 complex, the distance separating the last residue of LTBP1-TB3 and the first residue of LTBP1-EGF3 is small enough to be easily accommodated by the 36-residue flexible linker joining the two domains (Figure 8A). An LTBP1TB3E3 variant in which this linker was deleted showed lower binding to FBN1E2cbEGF1 in a plate-based assay (Figures 8B and 8C), consistent with only one of the two LTBP1 domains being able to interact at any given time in this construct. Replacement of the LTBP1 linker with the shorter 22-residue linker from LTBP3, which has a very different amino acid sequence, restored binding to levels comparable with the WT interaction indicating the linker plays a passive role as a connector (Figures 8B and 8C).","type":"Results"},{"text":"The boundaries of the linker region are taken from this paper and a previous publication (PMID:24489852). The structure-based prediction was performed based on experimental data from NMR chemical shifts and intensity changes.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T09:03:53.756Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":1578,"end":1624,"reference_id":"28669633","reference_source":"pmid","reference_html":"The N-Terminal Region of Fibrillin-1 Mediates a Bipartite Interaction with LTBP1. <i> Robertson IB, Dias HF, Osuch IH, Lowe ED, Jensen SA, Redfield C, Handford PA. </i> Structure, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"lchemes","curator_name":"Lucia Chemes","curator_orcid":"0000-0003-0192-9906","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":3,"region_id":"DP03379r009","statement":[{"text":"LTBP1 anchors itself to FBN1 using two independent epitopes. As part of this mechanism, a flexible pivot adjacent to the FBN1/LTBP1 binding site allows LTBP1 to make contacts with different ECM networks while presumably facilitating a force-induced/traction-based TGF-b activation mechanism.","type":"Abstract"},{"text":"In the HADDOCK model of the FBN1/LTBP1 complex, the distance separating the last residue of LTBP1-TB3 and the first residue of LTBP1-EGF3 is small enough to be easily accommodated by the 36-residue flexible linker joining the two domains (Figure 8A). An LTBP1TB3E3 variant in which this linker was deleted showed lower binding to FBN1E2cbEGF1 in a plate-based assay (Figures 8B and 8C), consistent with only one of the two LTBP1 domains being able to interact at any given time in this construct. Replacement of the LTBP1 linker with the shorter 22-residue linker from LTBP3, which has a very different amino acid sequence, restored binding to levels comparable with the WT interaction indicating the linker plays a passive role as a connector (Figures 8B and 8C).","type":"Results"},{"text":"The presence of a flexible linker between the two FBN1- interacting sites within LTBP1 suggests a mechanism by which proteases can regulate the affinity of this interaction. Protease cleavage of the TB3–EGF3 linker in LTBP1 may release the large latent complex from the 10–12 nm microfibril network, as the affinity of the TB3 binding site alone for FBN1 is very much weaker than the bipartite interaction.","type":"Discussion"},{"text":"We have further demonstrated an unusual bipartite interaction of LTBP1 with FBN1, adjacent to the LAP/TGF-b binding site, which facilitates complex formation in dynamic connective tissues. We propose that this contributes to integrin mediated activation of TGF-b in FBN1-rich tissues.","type":"Discussion"},{"text":"The boundaries of the linker region are taken from this paper and a previous publication (PMID:24489852). The structure-based prediction was performed based on experimental data from NMR chemical shifts and intensity changes.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-06-22T09:03:26.975Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":9,"released":"2023_06","sequence":"MAGAWLRWGLLLWAGLLASSAHGRLRRITYVVHPGPGLAAGALPLSGPPRSRTFNVALNARYSRSSAAAGAPSRASPGVPSERTRRTSKPGGAALQGLRPPPPPPPEPARPAVPGGQLHPNPGGHPAAAPFTKQGRQVVRSKVPQETQSGGGSRLQVHQKQQLQGVNVCGGRCCHGWSKAPGSQRCTKPSCVPPCQNGGMCLRPQLCVCKPGTKGKACETIAAQDTSSPVFGGQSPGAASSWGPPEQAAKHTSSKKADTLPRVSPVAQMTLTLKPKPSVGLPQQIHSQVTPLSSQSVVIHHGQTQEYVLKPKYFPAQKGISGEQSTEGSFPLRYVQDQVAAPFQLSNHTGRIKVVFTPSICKVTCTKGSCQNSCEKGNTTTLISENGHAADTLTATNFRVVICHLPCMNGGQCSSRDKCQCPPNFTGKLCQIPVHGASVPKLYQHSQQPGKALGTHVIHSTHTLPLTVTSQQGVKVKFPPNIVNIHVKHPPEASVQIHQVSRIDGPTGQKTKEAQPGQSQVSYQGLPVQKTQTIHSTYSHQQVIPHVYPVAAKTQLGRCFQETIGSQCGKALPGLSKQEDCCGTVGTSWGFNKCQKCPKKPSYHGYNQMMECLPGYKRVNNTFCQDINECQLQGVCPNGECLNTMGSYRCTCKIGFGPDPTFSSCVPDPPVISEEKGPCYRLVSSGRQCMHPLSVHLTKQLCCCSVGKAWGPHCEKCPLPGTAAFKEICPGGMGYTVSGVHRRRPIHHHVGKGPVFVKPKNTQPVAKSTHPPPLPAKEEPVEALTFSREHGPGVAEPEVATAPPEKEIPSLDQEKTKLEPGQPQLSPGISTIHLHPQFPVVIEKTSPPVPVEVAPEASTSSASQVIAPTQVTEINECTVNPDICGAGHCINLPVRYTCICYEGYRFSEQQRKCVDIDECTQVQHLCSQGRCENTEGSFLCICPAGFMASEEGTNCIDVDECLRPDVCGEGHCVNTVGAFRCEYCDSGYRMTQRGRCEDIDECLNPSTCPDEQCVNSPGSYQCVPCTEGFRGWNGQCLDVDECLEPNVCANGDCSNLEGSYMCSCHKGYTRTPDHKHCRDIDECQQGNLCVNGQCKNTEGSFRCTCGQGYQLSAAKDQCEDIDECQHRHLCAHGQCRNTEGSFQCVCDQGYRASGLGDHCEDINECLEDKSVCQRGDCINTAGSYDCTCPDGFQLDDNKTCQDINECEHPGLCGPQGECLNTEGSFHCVCQQGFSISADGRTCEDIDECVNNTVCDSHGFCDNTAGSFRCLCYQGFQAPQDGQGCVDVNECELLSGVCGEAFCENVEGSFLCVCADENQEYSPMTGQCRSRTSTDLDVDVDQPKEEKKECYYNLNDASLCDNVLAPNVTKQECCCTSGVGWGDNCEIFPCPVLGTAEFTEMCPKGKGFVPAGESSSEAGGENYKDADECLLFGQEICKNGFCLNTRPGYECYCKQGTYYDPVKLQCFDMDECQDPSSCIDGQCVNTEGSYNCFCTHPMVLDASEKRCIRPAESNEQIEETDVYQDLCWEHLSDEYVCSRPLVGKQTTYTECCCLYGEAWGMQCALCPLKDSDDYAQLCNIPVTGRRQPYGRDALVDFSEQYTPEADPYFIQDRFLNSFEELQAEECGILNGCENGRCVRVQEGYTCDCFDGYHLDTAKMTCVDVNECDELNNRMSLCKNAKCINTDGSYKCLCLPGYVPSDKPNYCTPLNTALNLEKDSDLE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins","NDDs-related proteins"],"UniParc":"UPI000016AC27","uniref100":"UniRef100_Q14766","uniref90":"UniRef90_Q14766","uniref50":"UniRef50_Q14766","genes":[{"name":{"value":"LTBP1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6714","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6714"}}]}}],"alphafold_very_low_content":0.37303893085415457,"disorder_content":0.04125508425334108,"disprot_consensus":{"full":[{"start":1507,"end":1522,"type":"D"},{"start":1578,"end":1581,"type":"F"},{"start":1582,"end":1623,"type":"D"},{"start":1624,"end":1624,"type":"F"},{"start":1709,"end":1721,"type":"D"}],"Structural state":[{"start":1507,"end":1522,"type":"D"},{"start":1582,"end":1623,"type":"D"},{"start":1709,"end":1721,"type":"D"}],"Disorder function":[{"start":1507,"end":1521,"type":"F"},{"start":1578,"end":1624,"type":"F"}],"Molecular function":[{"start":1578,"end":1624,"type":"F"}]}},{"disprot_id":"DP03380","acc":"P83110","creator":"vacs","date":"2021-06-18T08:16:00.428Z","features":{"pfam":[{"id":"PF00219","name":"Insulin-like growth factor binding protein","start":25,"end":76},{"id":"PF07648","name":"Kazal-type serine protease inhibitor domain","start":79,"end":126},{"id":"PF13180","name":"PDZ domain","start":357,"end":447},{"id":"PF13365","name":"Trypsin-like peptidase domain","start":175,"end":319}],"gene3D":[]},"length":453,"name":"Serine protease HTRA3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":279,"end":289,"reference_id":"26110759","reference_source":"pmid","reference_html":"Structural and Functional Analysis of Human HtrA3 Protease and Its Subdomains. <i> Glaza P, Osipiuk J, Wenta T, Zurawa-Janicka D, Jarzab M, Lesner A, Banecki B, Skorko-Glonek J, Joachimiak A, Lipinska B. </i> PLoS One, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4RI0"}],"region_id":"DP03380r001","statement":[{"text":"Chain A is the only molecule visible in full length in the ΔN-HtrA3 structure. It encompasses residues 135–459 with the exclusion of residues 163–168 and 277–289 of the loops LA and L3, respectively.","type":"Results"},{"text":"The fact that parts of the LA and L3 loops (Fig 3) were not visible in the ΔN-HtrA3 structure suggests their mobility and thus the possibility that they change conformation upon substrate binding. Similarly, the L3 loop is not visible in the HtrA1 and the E. coli HtrA(DegP) inactive structures, but is present in the active conformations [9] [56].","type":"Discussion"},{"text":"Residues 279-289 are missing in all chains and are presumably disordered.","type":"Curator statement"}],"validated":{"curator_name":"Tamas Lazar","curator_id":"tlazar","timestamp":"2021-06-21T17:11:26.518Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MQARALLLAALAALALAREPPAAPCPARCDVSRCPSPRCPGGYVPDLCNCCLVCAASEGEPCGGPLDSPCGESLECVRGLCRCRWSHAVCGTDGHTYANVCALQAASRRALQLSGTPVRQLQKGACPLGLHQLSSPRYKFNFIADVVEKIAPAVVHIELFLRHPLFGRNVPLSSGSGFIMSEAGLIITNAHVVSSNSAAPGRQQLKVQLQNGDSYEATIKDIDKKSDIATIKIHPKKKLPVLLLGHSADLRPGEFVVAIGSPFALQNTVTTGIVSTAQREGRELGLRDSDMDYIQTDAIINYGNSGGPLVNLDGEVIGINTLKVTAGISFAIPSDRITRFLTEFQDKQIKDWKKRFIGIRMRTITPSLVDELKASNPDFPEVSSGIYVQEVAPNSPSQRGGIQDGDIIVKVNGRPLVDSSELQEAVLTESPLLLEVRRGNDDLLFSIAPEVVM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000001647","uniref100":"UniRef100_P83110","uniref90":"UniRef90_P83110","uniref50":"UniRef50_P83110","genes":[{"name":{"value":"HTRA3"},"synonyms":[{"value":"PRSP"}]}],"alphafold_very_low_content":0.024282560706401765,"disorder_content":0.024282560706401765,"disprot_consensus":{"full":[{"start":279,"end":289,"type":"D"}],"Structural state":[{"start":279,"end":289,"type":"D"}]}},{"disprot_id":"DP03381","acc":"P63277-2","creator":"rpancsa","date":"2021-06-18T21:50:36.913Z","features":{"pfam":[],"gene3D":[]},"length":75,"name":"Isoform 2 of Amelogenin, X isoform","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":17,"end":75,"reference_id":"25449314","reference_source":"pmid","reference_html":"The leucine-rich amelogenin protein (LRAP) is primarily monomeric and unstructured in physiological solution. <i> Tarasevich BJ, Philo JS, Maluf NK, Krueger S, Buchko GW, Lin G, Shaw WJ. </i> J Struct Biol, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006214","ec_ontology":"ECO","ec_name":"small-angle neutron scattering evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03381r001","statement":[{"text":"The distribution of SASSIE structures indicates that LRAP(+P) can adopt a range of conformations dominated by extended structures with Rg of 1.5 – 2.5 nm.","type":"Results"},{"text":"(+P) means that a phosphorylated form was studied, where there is a single phosphorylation on residue S16 (equivalent to UniProt residue S32 due to the presence of a 16 residues long signal peptide in the UniProt sequence).","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:09:21.473Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":17,"end":75,"reference_id":"25449314","reference_source":"pmid","reference_html":"The leucine-rich amelogenin protein (LRAP) is primarily monomeric and unstructured in physiological solution. <i> Tarasevich BJ, Philo JS, Maluf NK, Krueger S, Buchko GW, Lin G, Shaw WJ. </i> J Struct Biol, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03381r002","statement":[{"text":"The solution NMR data for LRAP(−P), therefore, is consistent with random coil structures in the C-terminal and N-terminal regions.","type":"Results"},{"text":"The NMR data suggests a largely disordered structure for LRAP (−P), similar to the disordered, extended conformation reported for full-length porcine amelogenin at pH 3.8 in solution.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:09:23.097Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":17,"end":75,"reference_id":"25449314","reference_source":"pmid","reference_html":"The leucine-rich amelogenin protein (LRAP) is primarily monomeric and unstructured in physiological solution. <i> Tarasevich BJ, Philo JS, Maluf NK, Krueger S, Buchko GW, Lin G, Shaw WJ. </i> J Struct Biol, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2023_06","version":3,"region_id":"DP03381r003","statement":[{"text":"In vivo studies have shown that LRAP is localized within the extracellular matrix of growing enamel and in vitro studies have shown that LRAP can control HAP crystal formation suggesting that LRAP, like amelogenin, may have an extracellular matrix function in controlling enamel crystal growth.","type":"Introduction"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T15:32:01.745Z"},"term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":17,"end":75,"reference_id":"25449314","reference_source":"pmid","reference_html":"The leucine-rich amelogenin protein (LRAP) is primarily monomeric and unstructured in physiological solution. <i> Tarasevich BJ, Philo JS, Maluf NK, Krueger S, Buchko GW, Lin G, Shaw WJ. </i> J Struct Biol, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03381r004","statement":[{"text":"Circular dichroism (CD) spectra obtained for the phosphorylated LRAP (+P) in SCP at pH 7.4 and in solutions with 3 mM CaCl2 show that LRAP (+P) also has a largely disordered secondary structure.","type":"Results"},{"text":"CD studies show that LRAP(+P) is also predominantly unstructured.","type":"Discussion"},{"text":"(+P) means that a phosphorylated form was studied, where there is a single phosphorylation on residue S16 (equivalent to UniProt residue S32 due to the presence of a 16 residues long signal peptide in the UniProt sequence).","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:09:33.034Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":30,"end":34,"reference_id":"25449314","reference_source":"pmid","reference_html":"The leucine-rich amelogenin protein (LRAP) is primarily monomeric and unstructured in physiological solution. <i> Tarasevich BJ, Philo JS, Maluf NK, Krueger S, Buchko GW, Lin G, Shaw WJ. </i> J Struct Biol, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03381r005","statement":[{"text":"Both full-length amelogenin and LRAP are post-translationally modified by side chain phosphorylation of S16.","type":"Figure"},{"text":"Residue S16 is equivalent to UniProt residue S32 due to the presence of a 16 residues long signal peptide in the UniProt sequence.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-06-21T14:06:36.397Z"},"disprot_namespace":"Disorder function"}],"regions_counter":5,"released":"2023_06","sequence":"MGTWILFACLLGAAFAMPLPPHPGSPGYINLSYEVLTPLKWYQSMIRQPPLSPILPELPLEAWPATDKTKREEVD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI000002A3B1","uniref100":"","uniref90":"","uniref50":"","genes":[{"name":{"value":"Amelx"},"synonyms":[{"value":"Amel"}]}],"disorder_content":0.7866666666666666,"disprot_consensus":{"full":[{"start":17,"end":75,"type":"D"}],"Structural state":[{"start":17,"end":75,"type":"D"}],"Molecular function":[{"start":17,"end":75,"type":"F"}],"Disorder function":[{"start":30,"end":34,"type":"F"}]}},{"disprot_id":"DP03382","acc":"P98066","creator":"tlazar","date":"2021-06-22T09:25:50.537Z","features":{"pfam":[{"id":"PF00193","name":"Extracellular link domain","start":36,"end":128},{"id":"PF00431","name":"CUB domain","start":135,"end":244}],"gene3D":[]},"length":277,"name":"Tumor necrosis factor-inducible gene 6 protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":250,"end":277,"reference_id":"26468290","reference_source":"pmid","reference_html":"Metal Ion-dependent Heavy Chain Transfer Activity of TSG-6 Mediates Assembly of the Cumulus-Oocyte Matrix. <i> Briggs DC, Birchenough HL, Ali T, Rugg MS, Waltho JP, Ievoli E, Jowitt TA, Enghild JJ, Richter RP, Salustri A, Milner CM, Day AJ. </i> J Biol Chem, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2WNO"}],"region_id":"DP03382r001","statement":[{"text":"Only the CUB module (residues 128–249) was visible in the crystal structure with no electron density seen for the last 28 amino acid residues, although this region was verified as present in the crystals by SDS-PAGE (not shown). The last residue observed in the electron density is Pro-249, which protrudes into a large solvent channel; this might allow the C-terminal region to adopt a range of conformations, thus rendering it essentially invisible to crystallography.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-02T08:26:55.536Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":6,"released":"2021_12","sequence":"MIILIYLFLLLWEDTQGWGFKDGIFHNSIWLERAAGVYHREARSGKYKLTYAEAKAVCEFEGGHLATYKQLEAARKIGFHVCAAGWMAKGRVGYPIVKPGPNCGFGKTGIIDYGIRLNRSERWDAYCYNPHAKECGGVFTDPKQIFKSPGFPNEYEDNQICYWHIRLKYGQRIHLSFLDFDLEDDPGCLADYVEIYDSYDDVHGFVGRYCGDELPDDIISTGNVMTLKFLSDASVTAGGFQIKYVAMDPVSKSSQGKNTSTTSTGNKNFLAGRFSHL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"UniParc":"UPI0000137748","uniref100":"UniRef100_P98066","uniref90":"UniRef90_P98066","uniref50":"UniRef50_P98066","genes":[{"name":{"value":"TNFAIP6"},"synonyms":[{"value":"TSG6"}]}],"alphafold_very_low_content":0.1588447653429603,"disorder_content":0.10108303249097472,"disprot_consensus":{"full":[{"start":250,"end":277,"type":"D"}],"Structural state":[{"start":250,"end":277,"type":"D"}]}},{"disprot_id":"DP03383","acc":"Q8WVM7","creator":"fquaglia","date":"2021-06-28T14:28:54.476Z","features":{"pfam":[{"id":"PF08514","name":"STAG domain","start":161,"end":268},{"id":"PF21581","name":"Stromalin conservative domain","start":301,"end":375},{"id":"PF24571","name":"Cohesin subunit SCC3/SA, HEAT-repeats domain","start":483,"end":747},{"id":"PF31007","name":"STAG protein C-terminal domain","start":916,"end":1053}],"gene3D":[]},"length":1258,"name":"Cohesin subunit SA-1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":85,"reference_id":"32409525","reference_source":"pmid","reference_html":"Cryo-EM structure of the human cohesin-NIPBL-DNA complex. <i> Shi Z, Gao H, Bai XC, Yu H. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6WG3"}],"region_id":"DP03383r001","statement":[{"text":"Most of the SMC1 and SMC3 coiled coils (CCs), large segments of the flexible region of RAD21, and the N- and C-terminal unstructured parts of STAG1 and NIPBLC were completely unresolved.","type":"Article"}],"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-03T20:21:35.362Z"}},{"start":1053,"end":1258,"reference_id":"32409525","reference_source":"pmid","reference_html":"Cryo-EM structure of the human cohesin-NIPBL-DNA complex. <i> Shi Z, Gao H, Bai XC, Yu H. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6WG3"}],"region_id":"DP03383r002","statement":[{"text":"Most of the SMC1 and SMC3 coiled coils (CCs), large segments of the flexible region of RAD21, and the N- and C-terminal unstructured parts of STAG1 and NIPBLC were completely unresolved.","type":"Article"}],"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-03T20:21:45.863Z"}},{"start":442,"end":457,"reference_id":"32409525","reference_source":"pmid","reference_html":"Cryo-EM structure of the human cohesin-NIPBL-DNA complex. <i> Shi Z, Gao H, Bai XC, Yu H. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6WG3"}],"region_id":"DP03383r003","statement":[{"text":"unstructured region inside STAG1.","type":"Curator statement"}],"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-03T20:19:55.034Z"}},{"start":843,"end":853,"reference_id":"32409525","reference_source":"pmid","reference_html":"Cryo-EM structure of the human cohesin-NIPBL-DNA complex. <i> Shi Z, Gao H, Bai XC, Yu H. </i> Science, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6WG3"}],"region_id":"DP03383r004","statement":[{"text":"unstructured region inside STAG1.","type":"Curator statement"}],"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-03T20:19:41.596Z"}},{"start":34,"end":52,"reference_id":"22715410","reference_source":"pmid","reference_html":"Nuclear import and export signals of human cohesins SA1/STAG1 and SA2/STAG2 expressed in Saccharomyces cerevisiae. <i> Tarnowski LJ, Kowalec P, Milewski M, Jurek M, Plochocka D, Fronk J, Kurlandzka A. </i> PLoS One, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03383r005","statement":[{"text":"Since the SA1 protein was also nuclear in yeast, we asked whether the putative 19-amino acid-long bipartite NLS present in the N-terminal non-conserved part of this protein was responsible. The sequence 34KRKRGRPGRPPSTNKKPRK53 is specific to SA1 and is not homologous to the identified functional NLS32–47 of SA2L. Deleting K34–K53 resulted in the localization of SA1Δ34–53 in the whole cell, which confirmed that the signal is necessary for SA1 nuclear import. When we fused 71 N-terminal amino acids of SA1 containing this signal to GFP, the fusion protein SA11–71-GFP localized to the nucleus, confirming that it contained a functional NLS (Figure 5).","type":"Results"}],"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-03T20:22:46.678Z"}},{"start":34,"end":52,"reference_id":"22715410","reference_source":"pmid","reference_html":"Nuclear import and export signals of human cohesins SA1/STAG1 and SA2/STAG2 expressed in Saccharomyces cerevisiae. <i> Tarnowski LJ, Kowalec P, Milewski M, Jurek M, Plochocka D, Fronk J, Kurlandzka A. </i> PLoS One, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03383r006","statement":[{"text":"Since the SA1 protein was also nuclear in yeast, we asked whether the putative 19-amino acid-long bipartite NLS present in the N-terminal non-conserved part of this protein was responsible. The sequence 34KRKRGRPGRPPSTNKKPRK53 is specific to SA1 and is not homologous to the identified functional NLS32–47 of SA2L. Deleting K34–K53 resulted in the localization of SA1Δ34–53 in the whole cell, which confirmed that the signal is necessary for SA1 nuclear import. When we fused 71 N-terminal amino acids of SA1 containing this signal to GFP, the fusion protein SA11–71-GFP localized to the nucleus, confirming that it contained a functional NLS (Figure 5).","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-03T20:22:46.214Z"}}],"regions_counter":6,"released":"2021_12","sequence":"MITSELPVLQDSTNETTAHSDAGSELEETEVKGKRKRGRPGRPPSTNKKPRKSPGEKSRIEAGIRGAGRGRANGHPQQNGEGEPVTLFEVVKLGKSAMQSVVDDWIESYKQDRDIALLDLINFFIQCSGCRGTVRIEMFRNMQNAEIIRKMTEEFDEDSGDYPLTMPGPQWKKFRSNFCEFIGVLIRQCQYSIIYDEYMMDTVISLLTGLSDSQVRAFRHTSTLAAMKLMTALVNVALNLSIHQDNTQRQYEAERNKMIGKRANERLELLLQKRKELQENQDEIENMMNSIFKGIFVHRYRDAIAEIRAICIEEIGVWMKMYSDAFLNDSYLKYVGWTLHDRQGEVRLKCLKALQSLYTNRELFPKLELFTNRFKDRIVSMTLDKEYDVAVEAIRLVTLILHGSEEALSNEDCENVYHLVYSAHRPVAVAAGEFLHKKLFSRHDPQAEEALAKRRGRNSPNGNLIRMLVLFFLESELHEHAAYLVDSLWESSQELLKDWECMTELLLEEPVQGEEAMSDRQESALIELMVCTIRQAAEAHPPVGRGTGKRVLTAKERKTQIDDRNKLTEHFIITLPMLLSKYSADAEKVANLLQIPQYFDLEIYSTGRMEKHLDALLKQIKFVVEKHVESDVLEACSKTYSILCSEEYTIQNRVDIARSQLIDEFVDRFNHSVEDLLQEGEEADDDDIYNVLSTLKRLTSFHNAHDLTKWDLFGNCYRLLKTGIEHGAMPEQIVVQALQCSHYSILWQLVKITDGSPSKEDLLVLRKTVKSFLAVCQQCLSNVNTPVKEQAFMLLCDLLMIFSHQLMTGGREGLQPLVFNPDTGLQSELLSFVMDHVFIDQDEENQSMEGDEEDEANKIEALHKRRNLLAAFSKLIIYDIVDMHAAADIFKHYMKYYNDYGDIIKETLSKTRQIDKIQCAKTLILSLQQLFNELVQEQGPNLDRTSAHVSGIKELARRFALTFGLDQIKTREAVATLHKDGIEFAFKYQNQKGQEYPPPNLAFLEVLSEFSSKLLRQDKKTVHSYLEKFLTEQMMERREDVWLPLISYRNSLVTGGEDDRMSVNSGSSSSKTSSVRNKKGRPPLHKKRVEDESLDNTWLNRTDTMIQTPGPLPAPQLTSTVLRENSRPMGDQIQEPESEHGSEPDFLHNPQMQISWLGQPKLEDLNRKDRTGMNYMKVRTGVRHAVRGLMEEDAEPIFEDVMMSSRSQLEDMNEEFEDTMVIDLPPSRNRRERAELRPDFFDSAAIIEDDSGFGMPMF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000169F8F","uniref100":"UniRef100_Q8WVM7","uniref90":"UniRef90_Q8WVM7","uniref50":"UniRef50_Q8WVM7","dataset":["Cancer-related proteins","NDDs-related proteins"],"genes":[{"name":{"value":"STAG1"},"synonyms":[{"value":"SA1"},{"value":"SCC3","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"22628566","url":"http://www.ncbi.nlm.nih.gov/pubmed/22628566","alternativeUrl":"https://europepmc.org/abstract/MED/22628566"}}]}]}],"alphafold_very_low_content":0.23052464228934816,"disorder_content":0.2527821939586645,"disprot_consensus":{"full":[{"start":1,"end":85,"type":"D"},{"start":442,"end":457,"type":"D"},{"start":843,"end":853,"type":"D"},{"start":1053,"end":1258,"type":"D"}],"Structural state":[{"start":1,"end":85,"type":"D"},{"start":442,"end":457,"type":"D"},{"start":843,"end":853,"type":"D"},{"start":1053,"end":1258,"type":"D"}],"Biological process":[{"start":34,"end":52,"type":"F"}]}},{"disprot_id":"DP03385","acc":"P20592","creator":"msalas","date":"2021-06-30T17:20:28.764Z","features":{"pfam":[{"id":"PF00350","name":"Dynamin family","start":121,"end":295},{"id":"PF01031","name":"Dynamin central region","start":307,"end":593},{"id":"PF02212","name":"Dynamin GTPase effector domain","start":621,"end":709}],"gene3D":[]},"length":715,"name":"Interferon-induced GTP-binding protein Mx2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":599,"end":621,"reference_id":"28929138","reference_source":"pmid","reference_html":"CryoEM structure of MxB reveals a novel oligomerization interface critical for HIV restriction. <i> Alvarez FJD, He S, Perilla JR, Jang S, Schulten K, Engelman AN, Scheres SHW, Zhang P. </i> Sci Adv, 2017","date":"2023-07-12T20:22:12.983Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"8577"},{"db":"PDB","id":"5UOT"}],"region_id":"DP03385r002","statement":[{"text":"The Cryo-EM structure shows this region lacks electron density, indicating it is disordered. ","type":"Curator statement"}]},{"start":1,"end":92,"reference_id":"28929138","reference_source":"pmid","reference_html":"CryoEM structure of MxB reveals a novel oligomerization interface critical for HIV restriction. <i> Alvarez FJD, He S, Perilla JR, Jang S, Schulten K, Engelman AN, Scheres SHW, Zhang P. </i> Sci Adv, 2017","date":"2023-07-12T20:22:56.033Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"8577"},{"db":"PDB","id":"5UOT"}],"region_id":"DP03385r003","statement":[{"text":"The NTR, together with the MBP tag, is not resolved, probably because of their flexibility.","type":"Results"}]}],"regions_counter":3,"released":"2021_12","sequence":"MSKAHKPWPYRRRSQFSSRKYLKKEMNSFQQQPPPFGTVPPQMMFPPNWQGAEKDAAFLAKDFNFLTLNNQPPPGNRSQPRAMGPENNLYSQYEQKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLVLKLKKQPCEAWAGRISYRNTELELQDPGQVEKEIHKAQNVMAGNGRGISHELISLEITSPEVPDLTIIDLPGITRVAVDNQPRDIGLQIKALIKKYIQRQQTINLVVVPCNVDIATTEALSMAHEVDPEGDRTIGILTKPDLMDRGTEKSVMNVVRNLTYPLKKGYMIVKCRGQQEITNRLSLAEATKKEITFFQTHPYFRVLLEEGSATVPRLAERLTTELIMHIQKSLPLLEGQIRESHQKATEELRRCGADIPSQEADKMFFLIEKIKMFNQDIEKLVEGEEVVRENETRLYNKIREDFKNWVGILATNTQKVKNIIHEEVEKYEKQYRGKELLGFVNYKTFEIIVHQYIQQLVEPALSMLQKAMEIIQQAFINVAKKHFGEFFNLNQTVQSTIEDIKVKHTAKAENMIQLQFRMEQMVFCQDQIYSVVLKKVREEIFNPLGTPSQNMKLNSHFPSNESSVSSFTEIGIHLNAYFLETSKRLANQIPFIIQYFMLRENGDSLQKAMMQILQEKNRYSWLLQEQSETATKRRILKERIYRLTQARHALCQFSSKEIH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000001C2D","uniref100":"UniRef100_P20592","uniref90":"UniRef90_P20592","uniref50":"UniRef50_P20592","genes":[{"name":{"value":"MX2"}}],"alphafold_very_low_content":0.15524475524475526,"disorder_content":0.16083916083916083,"disprot_consensus":{"full":[{"start":1,"end":92,"type":"D"},{"start":599,"end":621,"type":"D"}],"Structural state":[{"start":1,"end":92,"type":"D"},{"start":599,"end":621,"type":"D"}]}},{"disprot_id":"DP03386","acc":"Q9Y237-2","creator":"eficho","date":"2021-07-01T09:34:53.495Z","features":{"pfam":[],"gene3D":[]},"length":156,"name":"Isoform 2 of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":59,"reference_id":"23179059","reference_source":"pmid","reference_html":"¹H, ¹³C and ¹⁵N resonance assignments of human parvulin 17. <i> Lin YJ, Schmidt A, Burgardt NI, Thiele A, Weiwad M, Lücke C. </i> Biomol NMR Assign, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"BMRB","id":"18615"}],"region_id":"DP03386r001","statement":[{"text":"The carbon-associated 1H resonances of the Par17 N-terminus up to residue Gly59, however, are missing due to a very high degree of resonance degeneracy within this apparently unstructured region.","type":"Article"},{"text":"Signals belonging to the first 60 N-terminal residues of Par17 show a low amide proton resonance dispersion (between 8.55 and 8.01 ppm), indicating that this region of the protein is largely unstructured.","type":"Figure"},{"text":"Subsequent chemical shift index analysis indicated that Par17 features a parvulin-type PPIase domain at the C-terminus, analogous to Par14, and an unstructured N-terminus encompassing the first 60 residues.","type":"Abstract"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-06T12:23:20.939Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":25,"reference_id":"17875217","reference_source":"pmid","reference_html":"The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae. <i> Kessler D, Papatheodorou P, Stratmann T, Dian EA, Hartmann-Fatu C, Rassow J, Bayer P, Mueller JW. </i> BMC Biol, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0001163","ec_ontology":"ECO","ec_name":"co-localization evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03386r003","statement":[{"text":"The Par17 protein differs from Par14 within the N-terminus by 25 additional amino acids.","type":"Results"},{"text":"Par17-RS- and -QR-EGFP co-localized with mitochondrial staining. Totals of 77 ± 5 and 63 ± 9% of EGFP fluorescence were measured to overlap with the MitoTracker signal for Par17-RS and -QR, respectively. Par14-EGFP fluorescence is equally distributed throughout the cytosol and partially enriched in the nucleus, as has been described previously. Co-localization values were far lower for Par14-EGFP (11 ± 6%) and EGFP alone (4 ± 1%). Therefore, the presequence seemed to be the determinant for mitochondrial targeting, and the question arose whether the Par17 N-terminus was necessary and/or sufficient for mitochondrial targeting.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-08T14:09:18.020Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false}],"regions_counter":3,"released":"2021_12","sequence":"MPMAGLLKGLVRQLERFSVQQQASKMPPKGKSGSGKAGKGGAASGSDSADKKAQGPKGGGNAVKVRHILCEKHGKIMEAMEKLKSGMRFNEVAAQYSEDKARQGGDLGWMTRGSMVGPFQEAAFALPVSGMDKPVFTDPPVKTKFGYHIIMVEGRK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI00002263A9","uniref100":"","uniref90":"","uniref50":"","genes":[{"name":{"value":"PIN4"}}],"disorder_content":0.3782051282051282,"disprot_consensus":{"full":[{"start":1,"end":59,"type":"D"}],"Structural state":[{"start":1,"end":59,"type":"D"}],"Biological process":[{"start":1,"end":25,"type":"F"}]}},{"disprot_id":"DP03387","acc":"Q9Y237-1","creator":"eficho","date":"2021-07-01T09:57:56.067Z","features":{"pfam":[],"gene3D":[]},"length":131,"name":"Isoform 1 of Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":35,"reference_id":"10966801","reference_source":"pmid","reference_html":"NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein. <i> Sekerina E, Rahfeld JU, Müller J, Fanghänel J, Rascher C, Fischer G, Bayer P. </i> J Mol Biol, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"BMRB","id":"4768"}],"region_id":"DP03387r001","statement":[{"text":"The hPar14 folds into aba3bab2 structure, and contains an unstructured 35-amino acid basic tail N-terminal to the catalytic core that replaces the WW domain of hPin1  homolog.","type":"Abstract"},{"text":"Poorly dispersed resonances of amino acid residues Lys4 to Gly35 within the amid region   of TOCSY and COSY-spectra point to the fact that these residues are localized in random  coil areas. Confirmation comes from the evaluation of NOESY spectra where only sequential NOEs of neighboring residues within this sequence were found. ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-05T09:17:13.216Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MPPKGKSGSGKAGKGGAASGSDSADKKAQGPKGGGNAVKVRHILCEKHGKIMEAMEKLKSGMRFNEVAAQYSEDKARQGGDLGWMTRGSMVGPFQEAAFALPVSGMDKPVFTDPPVKTKFGYHIIMVEGRK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000131AF2","uniref100":"","uniref90":"","uniref50":"","genes":[{"name":{"value":"PIN4"}}],"disorder_content":0.26717557251908397,"disprot_consensus":{"full":[{"start":1,"end":35,"type":"D"}],"Structural state":[{"start":1,"end":35,"type":"D"}]}},{"disprot_id":"DP03388","acc":"P0AB38","creator":"eficho","date":"2021-07-01T10:43:53.082Z","features":{"pfam":[{"id":"PF13036","name":"Peptidoglycan-synthase activator LpoB","start":72,"end":210}],"gene3D":[]},"length":213,"name":"Penicillin-binding protein activator LpoB","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":21,"end":80,"reference_id":"24691651","reference_source":"pmid","reference_html":"Solution NMR assignment of LpoB, an outer-membrane anchored Penicillin-Binding Protein activator from Escherichia coli. <i> Jean NL, Bougault CM, Egan AJ, Vollmer W, Simorre JP. </i> Biomol NMR Assign, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"BMRB","id":"19681"}],"region_id":"DP03388r001","statement":[{"text":"In agreement with the presence of 27 % Pro residues, the G1 to W64 segment is largely unstructured with Cα and CO chemical shifts close to random coil values and IUPred scores larger than 0.55.","type":"Article"},{"text":"We also provide evidence for a two-domain organization of LpoB and a largely disordered, 64 amino acid-long N-terminal domain.","type":"Abstract"},{"text":"The first four residues of the analyzed sequence construct belonged to a tag that replaced the signal peptide. Valine 21 was the first UniProt residue being part of the construct (equivalent to residue 5 in the construct).","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-05T09:19:50.935Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MTKMSRYALITALAMFLAGCVGQREPAPVEEVKPAPEQPAEPQQPVPTVPSVPTIPQQPGPIEHEDQTAPPAPHIRHYDWNGAMQPMVSKMLGADGVTAGSVLLVDSVNNRTNGSLNAAEATETLRNALANNGKFTLVSAQQLSMAKQQLGLSPQDSLGTRSKAIGIARNVGAHYVLYSSASGNVNAPTLQMQLMLVQTGEIIWSGKGAVSQQ","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"UniParc":"UPI000013A67F","uniref100":"UniRef100_P0AB39","uniref90":"UniRef90_P0AB39","uniref50":"UniRef50_P0AB39","genes":[{"name":{"value":"lpoB"},"synonyms":[{"value":"ycfM"}],"olnNames":[{"value":"b1105"},{"value":"JW5157"}]}],"alphafold_very_low_content":0.16901408450704225,"disorder_content":0.28169014084507044,"disprot_consensus":{"full":[{"start":21,"end":80,"type":"D"}],"Structural state":[{"start":21,"end":80,"type":"D"}]}},{"disprot_id":"DP03389","acc":"Q9UBT3","creator":"eficho","date":"2021-07-01T10:54:59.066Z","features":{"pfam":[{"id":"PF04706","name":"Dickkopf N-terminal cysteine-rich region","start":40,"end":91},{"id":"PF21479","name":"Dickkopf-related protein 1/2/4, C-terminal subdomain 2","start":173,"end":220},{"id":"PF21481","name":"Dickkopf-related protein 1/2/4, C-terminal subdomain 1","start":141,"end":170}],"gene3D":[]},"length":224,"name":"Dickkopf-related protein 4","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":19,"end":38,"reference_id":"24816897","reference_source":"pmid","reference_html":"Resonance assignment and secondary structure determination of full length human Dickkopf 4 (hDkk4), a secreted, disulphide-rich Wnt inhibitor protein. <i> Barkell AM, Holdsworth G, Waters LC, Veverka V, Slocombe PM, Muskett FW, Henry AJ, Robinson MK, Carr MD. </i> Biomol NMR Assign, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03389r001","statement":[{"text":"The N-terminal region of hDkk4 (M1–G21) and the relatively long linker between the two cysteine-rich regions (E77–Q123) appear to be unstructured and relatively mobile.","type":"Abstract"},{"text":"The N-terminus of the protein (M1–S21), the non-conserved linker (E77–Q123) between the two cysteine-rich regions and the C-terminal histidine-tag (E208–H222) are characterised by relatively intense and close to random coil chemical shifts for backbone amide signals, which together with predicted order parameters of 0.3–0.7 from TALOS+ for residues 2–22, 81–122 and 206–217 suggests that these regions are unstructured and relatively mobile compared to the cysteine-rich regions.","type":"Article"},{"text":"The mature form of the protein was studied UniProt (19-224), with an extra Met at the N-terminus and a tag at the C-terminus. Therefore there is a shift in the residue numbering and G21 in the construct is equivalent to G38 in the UniProt sequence.","type":"Curator statement"}],"cross_refs":[{"db":"BMRB","id":"19768"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-06T12:23:52.638Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":94,"end":140,"reference_id":"24816897","reference_source":"pmid","reference_html":"Resonance assignment and secondary structure determination of full length human Dickkopf 4 (hDkk4), a secreted, disulphide-rich Wnt inhibitor protein. <i> Barkell AM, Holdsworth G, Waters LC, Veverka V, Slocombe PM, Muskett FW, Henry AJ, Robinson MK, Carr MD. </i> Biomol NMR Assign, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03389r002","statement":[{"text":"The N-terminal region of hDkk4 (M1–G21) and the relatively long linker between the two cysteine-rich regions (E77–Q123) appear to be unstructured and relatively mobile.","type":"Abstract"},{"text":"The N-terminus of the protein (M1–S21), the non-conserved linker (E77–Q123) between the two cysteine-rich regions and the C-terminal histidine-tag (E208–H222) are characterised by relatively intense and close to random coil chemical shifts for backbone amide signals, which together with predicted order parameters of 0.3–0.7 from TALOS+ for residues 2–22, 81–122 and 206–217 suggests that these regions are unstructured and relatively mobile compared to the cysteine-rich regions.","type":"Article"},{"text":"The mature form of the protein was studied UniProt (19-224), with an extra Met at the N-terminus and a tag at the C-terminus. Therefore there is a shift in the residue numbering and E77-Q123 in the construct is equivalent to E94-Q140 in the UniProt sequence.","type":"Curator statement"}],"cross_refs":[{"db":"BMRB","id":"19768"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-06T12:23:53.696Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":94,"end":140,"reference_id":"24816897","reference_source":"pmid","reference_html":"Resonance assignment and secondary structure determination of full length human Dickkopf 4 (hDkk4), a secreted, disulphide-rich Wnt inhibitor protein. <i> Barkell AM, Holdsworth G, Waters LC, Veverka V, Slocombe PM, Muskett FW, Henry AJ, Robinson MK, Carr MD. </i> Biomol NMR Assign, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03389r003","statement":[{"text":"The N-terminal region of hDkk4 (M1–G21) and the relatively long linker between the two cysteine-rich regions (E77–Q123) appear to be unstructured and relatively mobile.","type":"Abstract"},{"text":"The N-terminus of the protein (M1–S21), the non-conserved linker (E77–Q123) between the two cysteine-rich regions and the C-terminal histidine-tag (E208–H222) are characterised by relatively intense and close to random coil chemical shifts for backbone amide signals, which together with predicted order parameters of 0.3–0.7 from TALOS+ for residues 2–22, 81–122 and 206–217 suggests that these regions are unstructured and relatively mobile compared to the cysteine-rich regions.","type":"Article"},{"text":"The mature form of the protein was studied UniProt (19-224), with an extra Met at the N-terminus and a tag at the C-terminus. Therefore there is a shift in the residue numbering and E77-Q123 in the construct is equivalent to E94-Q140 in the UniProt sequence.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-06T12:23:51.930Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":3,"released":"2021_12","sequence":"MVAAVLLGLSWLCSPLGALVLDFNNIRSSADLHGARKGSQCLSDTDCNTRKFCLQPRDEKPFCATCRGLRRRCQRDAMCCPGTLCVNDVCTTMEDATPILERQLDEQDGTHAEGTTGHPVQENQPKRKPSIKKSQGRKGQEGESCLRTFDCGPGLCCARHFWTKICKPVLLEGQVCSRRGHKDTAQAPEIFQRCDCGPGLLCRSQLTSNRQHARLRVCQKIEKL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000051057","uniref100":"UniRef100_Q9UBT3","uniref90":"UniRef90_Q9UBT3","uniref50":"UniRef50_Q9UBT3","genes":[{"name":{"value":"DKK4"}}],"alphafold_very_low_content":0.20535714285714285,"disorder_content":0.29910714285714285,"disprot_consensus":{"full":[{"start":19,"end":38,"type":"D"},{"start":94,"end":140,"type":"D"}],"Structural state":[{"start":19,"end":38,"type":"D"},{"start":94,"end":140,"type":"D"}],"Disorder function":[{"start":94,"end":140,"type":"F"}]}},{"disprot_id":"DP03390","acc":"Q2UZM9","creator":"eficho","date":"2021-07-01T12:13:55.585Z","features":{"pfam":[{"id":"PF00462","name":"Glutaredoxin","start":91,"end":155}],"gene3D":[]},"length":184,"name":"Mono-cysteine glutaredoxin","ncbi_taxon_id":5691,"organism":"Trypanosoma brucei","regions":[{"start":42,"end":76,"reference_id":"24830542","reference_source":"pmid","reference_html":"(1)H, (13)C and (15)N resonance assignment of the mature form of monothiol glutaredoxin 1 from the pathogen Trypanosoma brucei. <i> Sturlese M, Lelli M, Manta B, Mammi S, Comini MA, Bellanda M. </i> Biomol NMR Assign, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"BMRB","id":"19736"}],"region_id":"DP03390r001","statement":[{"text":"The mature form of mitochondrial Tb1-C-Grx1 (residues 42–184) was analyzed by NMR.","type":"Article"},{"text":"Although the good dispersion of peaks observed in the 15N-HSQC of Tb1-C-Grx1 WT clearly indicates that the protein is well folded in aqueous buffer, resonance assignment showed that the majority of the signals generated by the residues of the N-terminal tail resonate within a relative narrow region in the proton dimension. This feature suggests that the 35-mer N-terminal region is a largely unstructured element.","type":"Article"},{"text":"The first 35 residues of the mature protein are equivalent to UniProt residues 42-76.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-05T09:21:47.313Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MRRLSGSTCLLTGVTRAGRWLPTTAPCLSLCSFFLTASRRKQSTSGIGGDVRDIEETHPDFQPRLVSADLAEDEIAMVKKDIDDTIKSEDVVTFIKGLPEAPMCAYSKRMIDVLEALGLEYTSFDVLAHPVVRSYVKEVSEWPTIPQLFIKAEFVGGLDIVTKMLESGDLKKMLRDKGITCRDL","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Trypanosoma"],"UniParc":"UPI00006756E6","uniref100":"UniRef100_Q38FH2","uniref90":"UniRef90_Q38FH2","uniref50":"UniRef50_Q38FH2","dataset":["Neglected tropical diseases proteins"],"genes":[{"name":{"value":"mgrx","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAF02300.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAF02300.1"}}]}}],"alphafold_very_low_content":0.266304347826087,"disorder_content":0.19021739130434784,"disprot_consensus":{"full":[{"start":42,"end":76,"type":"D"}],"Structural state":[{"start":42,"end":76,"type":"D"}]}},{"disprot_id":"DP03391","acc":"C9ZXG5","creator":"eficho","date":"2021-07-01T12:28:45.035Z","features":{"pfam":[{"id":"PF00462","name":"Glutaredoxin","start":119,"end":183}],"gene3D":[]},"length":212,"name":"Glutaredoxin-like protein, putative","ncbi_taxon_id":679716,"organism":"Trypanosoma brucei gambiense (strain MHOM/CI/86/DAL972)","regions":[{"start":42,"end":76,"reference_id":"30209332","reference_source":"pmid","reference_html":"The lineage-specific, intrinsically disordered N-terminal extension of monothiol glutaredoxin 1 from trypanosomes contains a regulatory region. <i> Sturlese M, Manta B, Bertarello A, Bonilla M, Lelli M, Zambelli B, Grunberg K, Mammi S, Comini MA, Bellanda M. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2MXN"}],"region_id":"DP03391r001","statement":[{"text":"The residues belonging to the NTE show a poor dispersion of the proton chemical shifts\nin the 1H-15N HSQC spectrum. Most of these peaks cluster in the region between 8 and 8.5 ppm, with significantly higher intensities than average.","type":"Results"},{"text":"Cα secondary chemical shifts are highly sensitive probes for local conformation; most residues of the tail present absolute values below 0.5 ppm, which is typical of non-structured elements.","type":"Results"},{"text":"The model-free order parameters estimated with the RCI method show that most residues from the NTE present values consistently lower than the average value of 0.7 of the globular domain.","type":"Results"},{"text":"In contrast, hetNOE values below 0.4 were obtained for all residues upstream L70 providing additional evidence that the NTE is largely unstructured.","type":"Results"},{"text":"The plot of 1H-15N RDCs as a function of the residue number confirm that the NTE is largely disordered, presenting for most of the residues RDC absolute values below 3 Hz, hence significantly smaller than the average for the globular domain (7.2 Hz).","type":"Results"},{"text":"Assuming that the protein is monomeric, from the measured hydrodynamic radius it is possible to calculate for FL 1CGrx1 a compaction factor of 0.73, which is fully in agreement with the presence of a structured domain of around 100 residues, namely the Grx domain, and a disordered region of about 40 residues, the NTE.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-08T14:11:26.131Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":65,"end":76,"reference_id":"30209332","reference_source":"pmid","reference_html":"The lineage-specific, intrinsically disordered N-terminal extension of monothiol glutaredoxin 1 from trypanosomes contains a regulatory region. <i> Sturlese M, Manta B, Bertarello A, Bonilla M, Lelli M, Zambelli B, Grunberg K, Mammi S, Comini MA, Bellanda M. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"2MXN"}],"region_id":"DP03391r002","statement":[{"text":"Interestingly, the portion comprising residues 65–76 of the NTE modulates the conformational dynamics of the glutathione-binding pocket, which may play a role in iron-sulfur cluster assembly and delivery.","type":"Abstract"},{"text":"Comparison of the 1H-15N-HSQC spectra of Δ76 and FL 1CGrx1 revealed shifts in a significant number of peaks, which can be ascribed to structural rearrangements caused by the presence of the NTE.","type":"Results"},{"text":"Notably, the peak pattern of the 1H-15N-HSQC spectrum from Δ64 1CGrx1 is essentially identical to that observed for the full-length protein. This result clearly shows that the segment comprising amino acids L65 to M76, (i.e., the C-terminal part of the NTE), is responsible for modulating the conformational dynamics of FL 1CGrx1.","type":"Results"},{"text":"Altogether, our results support a pivotal role for residues 65-76 of the N-terminal tail of FL 1CGrx1 in modulating the structural dynamic properties of the binding pocket through a network of polar and hydrophobic interactions between residues from α1 and α3.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-08T14:11:28.970Z"},"ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":65,"end":76,"reference_id":"30209332","reference_source":"pmid","reference_html":"The lineage-specific, intrinsically disordered N-terminal extension of monothiol glutaredoxin 1 from trypanosomes contains a regulatory region. <i> Sturlese M, Manta B, Bertarello A, Bonilla M, Lelli M, Zambelli B, Grunberg K, Mammi S, Comini MA, Bellanda M. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"2MXN"}],"region_id":"DP03391r003","statement":[{"text":"The chemical shift perturbation (CSP) is evident not only for α1, to which the NTE is connected, but also for α3 and the downstream loop containing the conserved cis-proline. Mapping the CSP on the bundle of conformations for FL 1CGrx1 clearly shows that the regions of the protein most affected by the presence of the NTE correspond to those where the structure is less well defined because of internal mobility, as already described in the previous section.","type":"Results"},{"text":"Comparison of the 1H-15N-HSQC spectra of Δ76 and FL 1CGrx1 revealed shifts in a significant number of peaks, which can be ascribed to structural rearrangements caused by the presence of the NTE.","type":"Results"},{"text":"Notably, the peak pattern of the 1H-15N-HSQC spectrum from Δ64 1CGrx1 is essentially identical to that observed for the full-length protein. This result clearly shows that the segment comprising amino acids L65 to M76, (i.e., the C-terminal part of the NTE), is responsible for modulating the conformational dynamics of FL 1CGrx1.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-08T14:11:27.560Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":42,"end":75,"reference_id":"30209332","reference_source":"pmid","reference_html":"The lineage-specific, intrinsically disordered N-terminal extension of monothiol glutaredoxin 1 from trypanosomes contains a regulatory region. <i> Sturlese M, Manta B, Bertarello A, Bonilla M, Lelli M, Zambelli B, Grunberg K, Mammi S, Comini MA, Bellanda M. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03391r004","statement":[{"text":"Based on size exclusion chromatography (SEC), we have previously proposed that the NTE may promote the formation of non-covalent dimers in apo-1CGrx. Considering the IDR nature of the NTE and its potential contribution to an anomalous behaviour of 1CGrx1 in solution, we revisited this hypothesis by applying three complementary experimental approaches.","type":"Results"},{"text":"After filtering out residues from flexible regions or involved in chemical exchange processes, we estimated τc = 9.5 ± 0.5 ns for FL 1CGrx1, which is fully compatible with a monomeric and not a dimeric state, as previously assumed. Not surprisingly, this value is significantly larger than the previously measured τc for the Δ76 mutant (7.9 ± 0.6 ns) due to the expanded size of the protein containing the unstructured NTE.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-08T14:11:24.467Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":42,"end":75,"reference_id":"30209332","reference_source":"pmid","reference_html":"The lineage-specific, intrinsically disordered N-terminal extension of monothiol glutaredoxin 1 from trypanosomes contains a regulatory region. <i> Sturlese M, Manta B, Bertarello A, Bonilla M, Lelli M, Zambelli B, Grunberg K, Mammi S, Comini MA, Bellanda M. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03391r005","statement":[{"text":"After optimization of the cleavage conditions, trypsin treatment of FL 1CGrx1 yielded protein cleaved between K64 and L65, as confirmed by mass spectrometry, and therefore named Δ64 1CGrx1.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-08T14:10:42.935Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":5,"released":"2021_12","sequence":"MRHCHMSFAYCFCPFSAHRSASSQGYTRLMRRLSGSTCLLTGVTRAGRWLPTTAPCLSLCSFLTASRRKQSTSGIGGDVRDIEETHPDFQPRLVSADLAEDEIAMVKKDIDDTIKSEDVVTFIKGLPEAPMCAYSKRMIDVLEALGLEYTSFDVLAHPVVRSYVKEVSEWPTIPQLFIKAEFVGGLDIVTKMLESGDLKKMLRDKGITCRDL","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Trypanosoma"],"UniParc":"UPI0001B9DBDD","uniref100":"UniRef100_C9ZXG5","uniref90":"UniRef90_Q38FH2","uniref50":"UniRef50_Q38FH2","dataset":["Neglected tropical diseases proteins"],"genes":[{"orfNames":[{"value":"TbgDal_IX1840","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CBH14109.1","url":"https://www.ebi.ac.uk/ena/browser/view/CBH14109.1"}}]}]}],"alphafold_very_low_content":0.33962264150943394,"disorder_content":0.1650943396226415,"disprot_consensus":{"full":[{"start":42,"end":76,"type":"D"}],"Structural state":[{"start":42,"end":76,"type":"D"}],"Molecular function":[{"start":65,"end":76,"type":"F"}]}},{"disprot_id":"DP03392","acc":"A0A2U8QNT7","creator":"eficho","date":"2021-07-01T13:00:30.831Z","features":{"pfam":[{"id":"PF04927","name":"Seed maturation protein","start":15,"end":53},{"id":"PF04927","name":"Seed maturation protein","start":95,"end":136}],"gene3D":[]},"length":257,"name":"LEA6","ncbi_taxon_id":6661,"organism":"Artemia franciscana","regions":[{"start":1,"end":257,"reference_id":"31363993","reference_source":"pmid","reference_html":"Structural properties and cellular expression of AfrLEA6, a group 6 late embryogenesis abundant protein from embryos of Artemia franciscana. <i> LeBlanc BM, Le MT, Janis B, Menze MA, Hand SC. </i> Cell Stress Chaperones, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03392r001","statement":[{"text":"Assessment of secondary structure in aqueous and dried states with circular dichroism (CD) reveals 89% random coil in the aqueous state, thus supporting classification of AfrLEA6 as an IDP.","type":"Abstract"},{"text":"AfrLEA6 exists as an intrinsically disordered protein in solution with a minimum ellipticity of 200 nm that is characteristic of disordered, random coil proteins.","type":"Results"},{"text":"Our CD studies indicate that AfrLEA6 is clearly intrinsically disordered in solution based on an estimated 89% content of random coil.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-05T10:49:51.901Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":257,"reference_id":"31363993","reference_source":"pmid","reference_html":"Structural properties and cellular expression of AfrLEA6, a group 6 late embryogenesis abundant protein from embryos of Artemia franciscana. <i> LeBlanc BM, Le MT, Janis B, Menze MA, Hand SC. </i> Cell Stress Chaperones, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03392r002","statement":[{"text":"Removal of water from the protein by drying or exposure to trifluoroethanol (a chemical de-solvating agent) promotes a large gain in secondary structure of AfrLEA6, predominated by α-helix and exhibiting minimal β-sheet structure.","type":"Abstract"},{"text":"When interactions with water are decreased by drying or by the addition of 70% trifluoroethanol (TFE; a chemical de-solvating agent), AfrLEA6 gains significant secondary structure (α-helix, β-sheet, turns). A similar outcome was promoted by adding 2% SDS. A substantial increase in the proportion of α-helix was indicated in the CD spectra by double minima at 208 and 222 nm and a maximum at 191 nm.","type":"Results"},{"text":"Since AfrLEA6 is a LEA protein and many of those are dehydrins, the structural transition observed upon drying is likely to be physiologically relevant.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-05T10:49:51.900Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"}],"regions_counter":2,"released":"2023_12","sequence":"MSENIGHININANLQNVDRRDAAAIQSVERKLLGYNPPGGLASEAQSAAALNEGIGQPMNRGISTDIPAPADIDVDRGTASKDFGHVRFDVDLNQVRPEEAAALQAAESKIEGLAPSITVGGIGSAAQSMAAFNEREQSETGPFHPGIKATEPLPGPTYYQGVELSPSALPTYAPDVSVFPPSLSTNTSNVGAVPPSITTYSPDAGANDWERVYRKTTKTTQRIAIPGGIEDIVDEGKLGEAPRTNIRSTIGNVRMD","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Crustacea","Branchiopoda","Anostraca","Artemiidae","Artemia"],"UniParc":"UPI000D7E1C2A","uniref100":"UniRef100_A0A2U8QNT7","uniref90":"UniRef90_A0A2U8QNT7","uniref50":"UniRef50_A0A2U8QNT7","genes":[],"alphafold_very_low_content":0.5836575875486382,"dataset":["Condensates-related proteins"],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":257,"type":"T"}],"Structural state":[{"start":1,"end":257,"type":"D"}],"Structural transition":[{"start":1,"end":257,"type":"T"}]}},{"disprot_id":"DP03393","acc":"J2EKT7","creator":"eficho","date":"2021-07-01T13:40:17.362Z","features":{"pfam":[{"id":"PF02069","name":"Prokaryotic metallothionein","start":2,"end":50}],"gene3D":[]},"length":82,"name":"Uncharacterized protein","ncbi_taxon_id":1038922,"organism":"Pseudomonas fluorescens Q2-87","regions":[{"start":54,"end":82,"reference_id":"30191219","reference_source":"pmid","reference_html":"A histidine-rich Pseudomonas metallothionein with a disordered tail displays higher binding capacity for cadmium than zinc. <i> Habjanič J, Zerbe O, Freisinger E. </i> Metallomics, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"BMRB","id":"34282"},{"db":"PDB","id":"6GRV"}],"region_id":"DP03393r001","statement":[{"text":"Here we present the first NMR solution structure of a Pseudomonas MT, PflQ2 MT, using the strain P. fluorescens Q2-87. It consists of a metal binding domain and an intrinsically disordered C-terminal tail, that was not observed in other MTs so far.","type":"Abstract"},{"text":"To experimentally confirm this prediction but also to investigate the influence of the tail on the metal binding abilities and on the structure, the full-length protein PflQ2 MT and its shortened version, lacking the tail, (sh_PflQ2 MT) were compared using NMR and optical spectroscopy.","type":"Results"},{"text":"MT refers to Metallothionein. In the methods the authors state that \"The shortened version of the protein lacking the C-terminal tail, sh_PflQ2 MT (residues 1-52)\", these residues are equivalent to UniProt residues 2-53, therefore the C-terminal tail must span UniProt residues 54-82","type":"Curator statement"},{"text":"Backbone dynamics studies show a gradual decrease of 15N{1H}-NOE values from residue R51 on, which, however, only level off to -0.5 after residue 76. This indicates that there is still some, albeit rather loose, interaction of the tail with the folded part of the protein, and that it resembles a molten globule.","type":"Results"},{"text":"The disordered C-terminal tail has never been observed in other MTs so far. We\ncould demonstrate that this tail has no influence on the metal binding properties of the Pseudomonas MT and does not change the overall protein fold.","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-05T09:31:17.003Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MNELRCGCPDCHCKVDPERVFNHDGEAYCSQACAEQHPNGEPCPAPDCHCERSGKVGGRDITNNQLDEALEETFPASDPISP","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Pseudomonadales","Pseudomonadaceae","Pseudomonas"],"UniParc":"UPI00026E3114","uniref100":"UniRef100_J2EKT7","uniref90":"UniRef90_J2EKT7","uniref50":"UniRef50_W8PM51","genes":[{"orfNames":[{"value":"PflQ2_2045","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EJL04150.1","url":"https://www.ebi.ac.uk/ena/browser/view/EJL04150.1"}}]}]}],"alphafold_very_low_content":0.07317073170731707,"disorder_content":0.35365853658536583,"disprot_consensus":{"full":[{"start":54,"end":82,"type":"D"}],"Structural state":[{"start":54,"end":82,"type":"D"}]}},{"disprot_id":"DP03394","acc":"O60493","creator":"eficho","date":"2021-07-01T14:09:21.314Z","features":{"pfam":[{"id":"PF00787","name":"PX domain","start":58,"end":147}],"gene3D":[]},"length":162,"name":"Sorting nexin-3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":2,"end":28,"reference_id":"25893673","reference_source":"pmid","reference_html":"Secondary structure and (1)H, (13)C, (15)N resonance assignments of the endosomal sorting protein sorting nexin 3. <i> Overduin M, Rajesh S, Gruenberg J, Lenoir M. </i> Biomol NMR Assign, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03394r001","statement":[{"text":"The secondary structure of SNX3 was predicted from Hα, Cα, Cβ, C′ chemical shifts using Ccpnmr analysis suite and the corresponding chemical shift index. Three β-strands (29–39, 46–55, 64–69) followed by three α-helices (71–84, 112–130, 133–145) were predicted, consistent with the structural characteristics of PX domains and SNX12-PX in particular. The third helix may contain an irregularity midway based on an interrupted CSI pattern, while both termini exhibit random coil resonances and are intrinsically disordered.","type":"Results"}],"cross_refs":[{"db":"BMRB","id":"25402"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-05T09:22:12.680Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":146,"end":162,"reference_id":"25893673","reference_source":"pmid","reference_html":"Secondary structure and (1)H, (13)C, (15)N resonance assignments of the endosomal sorting protein sorting nexin 3. <i> Overduin M, Rajesh S, Gruenberg J, Lenoir M. </i> Biomol NMR Assign, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"BMRB","id":"25402"}],"region_id":"DP03394r002","statement":[{"text":"The secondary structure of SNX3 was predicted from Hα, Cα, Cβ, C′ chemical shifts using Ccpnmr analysis suite and the corresponding chemical shift index. Three β-strands (29–39, 46–55, 64–69) followed by three α-helices (71–84, 112–130, 133–145) were predicted, consistent with the structural characteristics of PX domains and SNX12-PX in particular. The third helix may contain an irregularity midway based on an interrupted CSI pattern, while both termini exhibit random coil resonances and are intrinsically disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-05T09:22:13.623Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MAETVADTRRLITKPQNLNDAYGPPSNFLEIDVSNPQTVGVGRGRFTTYEIRVKTNLPIFKLKESTVRRRYSDFEWLRSELERESKVVVPPLPGKAFLRQLPFRGDDGIFDDNFIEERKQGLEQFINKVAGHPLAQNERCLHMFLQDEIIDKSYTPSKIRHA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI00000013A7","uniref100":"UniRef100_O60493","uniref90":"UniRef90_O60493","uniref50":"UniRef50_O60493","genes":[{"name":{"value":"SNX3","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"30213940","url":"http://www.ncbi.nlm.nih.gov/pubmed/30213940","alternativeUrl":"https://europepmc.org/abstract/MED/30213940"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11174","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11174"}}]}}],"alphafold_very_low_content":0.006172839506172839,"disorder_content":0.2716049382716049,"disprot_consensus":{"full":[{"start":2,"end":28,"type":"D"},{"start":146,"end":162,"type":"D"}],"Structural state":[{"start":2,"end":28,"type":"D"},{"start":146,"end":162,"type":"D"}]}},{"disprot_id":"DP03396","acc":"Q716H0","creator":"eficho","date":"2021-07-02T11:46:08.484Z","features":{"pfam":[{"id":"PF11651","name":"P22 coat protein - gene protein 5","start":4,"end":421}],"gene3D":[]},"length":423,"name":"Gene 5 protein","ncbi_taxon_id":10761,"organism":"Shigella phage Sf6","regions":[{"start":320,"end":332,"reference_id":"27798771","reference_source":"pmid","reference_html":"NMR assignments for the insertion domain of bacteriophage Sf6 coat protein. <i> Tripler TN, Teschke CM, Alexandrescu AT. </i> Biomol NMR Assign, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"BMRB","id":"26844"}],"region_id":"DP03396r001","statement":[{"text":"In lieu of the D-loop, the Sf6 I-domain appears to have a new disordered loop between strands 5 and 6 of the β-barrel that is not observed in P22 or CUS-3.","type":"Article"},{"text":"For each protein the following are shown: amino acid sequence, residues protected from hydrogen exchange (indicated by filled circles), secondary structure prediction from sequence calculated with the JPred program, chemical-shift based secondary structure prediction calculated with TALOS-N (except for P22 where the schematic is based on the NMR structure) and prediction of backbone dynamics from TALOS-N where the green symbols “x” indicate flexible regions with small predicted S2 order parameters (except for P22 where the dynamics information is based on 15N-relaxation measurements).","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-06T12:24:27.838Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MPNNLDSNVSQIVLKKFLPGFMSDLVLAKTVDRQLLAGEINSSTGDSVSFKRPHQFSSLRTPTGDISGQNKNNLISGKATGRVGNYITVAVEYQQLEEAIKLNQLEEILAPVRQRIVTDLETELAHFMMNNGALSLGSPNTPITKWSDVAQTASFLKDLGVNEGENYAVMDPWSAQRLADAQTGLHASDQLVRTAWENAQIPTNFGGIRALMSNGLASRTQGAFGGTLTVKTQPTVTYNAVKDSYQFTVTLTGATASVTGFLKAGDQVKFTNTYWLQQQTKQALYNGATPISFTATVTADANSDSGGDVTVTLSGVPIYDTTNPQYNSVSRQVEAGDAVSVVGTASQTMKPNLFYNKFFCGLGSIPLPKLHSIDSAVATYEGFSIRVHKYADGDANVQKMRFDLLPAYVCFNPHMGGQFFGNP","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Uroviricota","Caudoviricetes","Caudovirales","Podoviridae","Lederbergvirus"],"UniParc":"UPI000022EFC1","uniref100":"UniRef100_A0A6D0IEA3","uniref90":"UniRef90_A0A137BYJ5","uniref50":"UniRef50_Q9T1S4","dataset":["Viral proteins"],"genes":[{"name":{"value":"5","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAQ12195.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAQ12195.1"}}]}}],"disorder_content":0.030732860520094562,"disprot_consensus":{"full":[{"start":320,"end":332,"type":"D"}],"Structural state":[{"start":320,"end":332,"type":"D"}]}},{"disprot_id":"DP03397","acc":"P13051-1","creator":"eficho","date":"2021-07-02T12:21:58.653Z","features":{"pfam":[],"gene3D":[]},"length":313,"name":"Isoform 2 of Uracil-DNA glycosylase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":92,"reference_id":"28879561","reference_source":"pmid","reference_html":"Backbone <sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N chemical shift assignment of full-length human uracil DNA glycosylase UNG2. <i> Buchinger E, Wiik SÅ, Kusnierczyk A, Rabe R, Aas PA, Kavli B, Slupphaug G, Aachmann FL. </i> Biomol NMR Assign, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"BMRB","id":"27133"}],"region_id":"DP03397r001","statement":[{"text":"Human uracil N-glycosylase isoform 2—UNG2 consists of an N-terminal intrinsically disordered regulatory domain (UNG2 residues 1–92, 9.3 kDa) and a C-terminal structured catalytic domain (UNG2 residues 93–313, 25.1 kDa).","type":"Abstract"},{"text":"In Figure 1 the N-HSQC spectrum of N-UNG2 (residues 1-92) shows very narrow peak dispersion that is typical for IDPs.","type":"Curator statement"},{"text":"Lack of any significant chemical shift changes indicates no interaction between the disorder N-UNG2 region and structured catalytic domain C-UNG2. ","type":"Article"},{"text":"The chemical shifts of HN, N, C′, Hα, Cα and Cβ were used to calculate secondary structure elements by TALOS+ (Shen et al. 2009) and SSP (Marsh et al. 2006). TALOS+ was developed to predict stable secondary structure elements while SSP was made for disordered proteins and therefore allows a more detailed view of the disordered regions. Both programs show similar predictions of N-UNG2 and C-UNG2. Both programs predict that the first 60 amino acids of N-UNG2 are intrinsically disordered followed by a long helical part from Ser67-Ala86.","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-06T12:24:48.281Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEESGDAAAIPAKKAPAGQEEPGTPPSSPLSAEQLDRIQRNKAAALLRLAARNVPVGFGESWKKHLSGEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWGSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGKKPIDWKEL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI000002E951","uniref100":"","uniref90":"","uniref50":"","genes":[{"name":{"value":"UNG","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03166","url":"https://hamap.expasy.org/unirule/MF_03166"}}]},"synonyms":[{"value":"DGU"},{"value":"UNG1","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03166","url":"https://hamap.expasy.org/unirule/MF_03166"}}]},{"value":"UNG15","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03166","url":"https://hamap.expasy.org/unirule/MF_03166"}}]}]}],"disorder_content":0.2939297124600639,"disprot_consensus":{"full":[{"start":1,"end":92,"type":"D"}],"Structural state":[{"start":1,"end":92,"type":"D"}]}},{"disprot_id":"DP03398","acc":"Q1HRL7","creator":"eficho","date":"2021-07-02T13:04:32.189Z","features":{"pfam":[{"id":"PF01395","name":"PBP/GOBP family","start":16,"end":126}],"gene3D":[]},"length":138,"name":"AAEL005772-PA","ncbi_taxon_id":7159,"organism":"Aedes aegypti","regions":[{"start":127,"end":138,"reference_id":"30684234","reference_source":"pmid","reference_html":"Complete NMR chemical shift assignments of odorant binding protein 22 from the yellow fever mosquito, Aedes aegypti, bound to arachidonic acid. <i> Jones DNM, Wang J, Murphy EJ. </i> Biomol NMR Assign, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"BMRB","id":"27724"}],"region_id":"DP03398r001","statement":[{"text":"These assignments reveal that the protein consists of seven α-helices, and that the arachidonic acid is bound tightly to the protein. Comparison with the chemical shift assignments of the apo-form of the protein reveals that binding of the fatty acid is accompanied by a large conformational change in the C-terminal helix, which appears disordered in the absence of lipid.","type":"Abstract"},{"text":"There are large chemical shift differences between the apo and bound states of AeOBP22 in multiple locations in the protein, with the largest differences localized to the C-terminal residues 104–123. A comparison of the calculated secondary structure propensities for the apo and bound states reveals that the overall secondary structure of the protein is maintained throughout most of the protein between the apo and bound states. In contrast, the C-terminal residues are significantly less ordered in the apo state.","type":"Article"},{"text":"The location of the predicted alpha-helical regions in the bound state is shown in the panel above as blue bars. For the apo-protein there is a clear break in the predicted secondary structure at residue 111.","type":"Figure"},{"text":"In the UniProt sequence there is a signal peptide of 16 residues that was not included in the experiment, so there is a shift of 16 residues in the numbering. Residue 111 is equivalent to UniProt residue 127.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-05T12:39:35.899Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":127,"end":138,"reference_id":"30684234","reference_source":"pmid","reference_html":"Complete NMR chemical shift assignments of odorant binding protein 22 from the yellow fever mosquito, Aedes aegypti, bound to arachidonic acid. <i> Jones DNM, Wang J, Murphy EJ. </i> Biomol NMR Assign, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"BMRB","id":"27724"}],"region_id":"DP03398r002","statement":[{"text":"These assignments reveal that the protein consists of seven α-helices, and that the arachidonic acid is bound tightly to the protein. Comparison with the chemical shift assignments of the apo-form of the protein reveals that binding of the fatty acid is accompanied by a large conformational change in the C-terminal helix, which appears disordered in the absence of lipid.","type":"Abstract"},{"text":"There are large chemical shift differences between the apo and bound states of AeOBP22 in multiple locations in the protein, with the largest differences localized to the C-terminal residues 104–123. A comparison of the calculated secondary structure propensities for the apo and bound states reveals that the overall secondary structure of the protein is maintained throughout most of the protein between the apo and bound states. In contrast, the C-terminal residues are significantly less ordered in the apo state.","type":"Article"},{"text":"The location of the predicted alpha-helical regions in the bound state is shown in the panel above as blue bars. For the apo-protein there is a clear break in the predicted secondary structure at residue 111.","type":"Figure"},{"text":"In the UniProt sequence there is a signal peptide of 16 residues that was not included in the experiment, so there is a shift of 16 residues in the numbering. Residue 111 is equivalent to UniProt residue 127.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-05T12:39:37.104Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":127,"end":138,"reference_id":"30684234","reference_source":"pmid","reference_html":"Complete NMR chemical shift assignments of odorant binding protein 22 from the yellow fever mosquito, Aedes aegypti, bound to arachidonic acid. <i> Jones DNM, Wang J, Murphy EJ. </i> Biomol NMR Assign, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"BMRB","id":"27724"}],"region_id":"DP03398r003","statement":[{"text":"These assignments reveal that the protein consists of seven α-helices, and that the arachidonic acid is bound tightly to the protein. Comparison with the chemical shift assignments of the apo-form of the protein reveals that binding of the fatty acid is accompanied by a large conformational change in the C-terminal helix, which appears disordered in the absence of lipid.","type":"Abstract"},{"text":"There are large chemical shift differences between the apo and bound states of AeOBP22 in multiple locations in the protein, with the largest differences localized to the C-terminal residues 104–123.","type":"Article"},{"text":"In the UniProt sequence there is a signal peptide of 16 residues that was not included in the experiment, so there is a shift of 16 residues in the numbering. Residue 111 is equivalent to UniProt residue 127.","type":"Curator statement"},{"text":"The location of the predicted alpha-helical regions in the bound state is shown in the panel above as blue bars. For the apo-protein there is a clear break in the predicted secondary structure at residue 111.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-05T12:39:40.102Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":3,"released":"2021_12","sequence":"MKVFIAVFALIAVAAAEFTVSTTEDLQRYRTECVSSLNIPADYVEKFKKWEFPEDDTTMCYIKCVFNKMQLFDDTEGPLVDNLVHQLAHGRDAEEVRTEVLKCVDKNTDNNACHWAFRGFKCFQKNNLSLIKASIKKD","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Nematocera","Culicoidea","Culicidae","Culicinae","Aedini","Aedes","Stegomyia"],"UniParc":"UPI0000D76DE8","uniref100":"UniRef100_Q1HRL7","uniref90":"UniRef90_Q1HRL7","uniref50":"UniRef50_Q1HRL7","genes":[{"name":{"value":"5567053","evidences":[{"code":"ECO:0000313","source":{"name":"EnsemblMetazoa","id":"AAEL005772-PA","url":"http://www.ensemblgenomes.org/id/AAEL005772-PA"}}]}}],"alphafold_very_low_content":0.021739130434782608,"disorder_content":0.08695652173913043,"disprot_consensus":{"full":[{"start":127,"end":138,"type":"T"}],"Structural state":[{"start":127,"end":138,"type":"D"}],"Structural transition":[{"start":127,"end":138,"type":"T"}],"Molecular function":[{"start":127,"end":138,"type":"F"}]}},{"disprot_id":"DP03399","acc":"P60484-2","creator":"fquaglia","date":"2021-07-02T13:39:30.818Z","features":{"pfam":[],"gene3D":[]},"length":576,"name":"Isoform alpha of Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":145,"reference_id":"26527737","reference_source":"pmid","reference_html":"The intrinsically disordered tails of PTEN and PTEN-L have distinct roles in regulating substrate specificity and membrane activity. <i> Masson GR, Perisic O, Burke JE, Williams RL. </i> Biochem J, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03399r001","statement":[{"text":"HDX–MS analysis of PTEN-L-6A (Supplementary Figure S9A) indicated that the first 145 residues of PTEN-L were intrinsically disordered as previously predicted [31], exhibiting very high levels of HDX–MS (>50% exchange at 3 s of exchange at 0°C). However, one region of the N-terminal extension of PTEN-L, residues 145–176, was below this threshold, suggesting that this region may be folded and forming an α-helix, as suggested by secondary structure prediction programs.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-02T13:48:49.440Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":47,"end":52,"reference_id":"23744781","reference_source":"pmid","reference_html":"A secreted PTEN phosphatase that enters cells to alter signaling and survival. <i> Hopkins BD, Fine B, Steinbach N, Dendy M, Rapp Z, Shaw J, Pappas K, Yu JS, Hodakoski C, Mense S, Klein J, Pegno S, Sulis ML, Goldstein H, Amendolara B, Lei L, Maurer M, Bruce J, Canoll P, Hibshoosh H, Parsons R. </i> Science, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03399r002","statement":[{"text":"To determine whether this sequence conferred similar properties to PTEN-Long, we constructed a PTEN-LongΔR6 construct in which these six arginines were deleted (Fig. S18). After treating cells with 100 nM purified Red Fluorescent Protein (RFP)-V5/His, PTEN-Long-RFP-V5/His, or PTEN-LongΔR6-RFP-V5/His, we detected PTEN-Long-RFP but not RFP nor PTEN-LongΔR6-RFP in the cells by fluorescence microscopy (Fig. 3A, Fig. S19).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-02T14:19:54.161Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":47,"end":52,"reference_id":"23744781","reference_source":"pmid","reference_html":"A secreted PTEN phosphatase that enters cells to alter signaling and survival. <i> Hopkins BD, Fine B, Steinbach N, Dendy M, Rapp Z, Shaw J, Pappas K, Yu JS, Hodakoski C, Mense S, Klein J, Pegno S, Sulis ML, Goldstein H, Amendolara B, Lei L, Maurer M, Bruce J, Canoll P, Hibshoosh H, Parsons R. </i> Science, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03399r003","statement":[{"text":"Inhibition of PI3K signaling appeared to be dependent upon the poly-arginine sequence of PTEN-Long because the PTEN-LongΔR6 mutant did not block Insulin or EGF-induced phosphorylation of AKT (Fig. S24).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-02T14:19:57.735Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":3,"released":"2021_12","sequence":"MERGGEAAAAAAAAAAAPGRGSESPVTISRAGNAGELVSPLLLPPTRRRRRRHIQGPGPVLNLPCAAAAPPVARAPEAAGGGSRSEDYSSSPHSAAAAARPLAAEEKQAQSLQPSSSRRSSHYPAAVQSQAAAERGASATAKSRAISILQKKPRHQQLLPSLSSFFFSHRLPDMTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEIDSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHTQITKV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0002578083","uniref100":"","uniref90":"","uniref50":"","genes":[{"name":{"value":"PTEN"},"synonyms":[{"value":"MMAC1"},{"value":"TEP1"}]}],"disorder_content":0.2517361111111111,"disprot_consensus":{"full":[{"start":1,"end":145,"type":"D"}],"Structural state":[{"start":1,"end":145,"type":"D"}],"Biological process":[{"start":47,"end":52,"type":"F"}],"Molecular function":[{"start":47,"end":52,"type":"F"}]}},{"disprot_id":"DP03400","acc":"Q9H4L7","creator":"eficho","date":"2021-07-02T13:40:11.798Z","features":{"pfam":[{"id":"PF00176","name":"SNF2-related domain","start":500,"end":785},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":855,"end":967}],"gene3D":[]},"length":1026,"name":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":109,"end":150,"reference_id":"30919308","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N resonance assignments for the tandem CUE domains from chromatin remodeler SMARCAD1. <i> Biasutto AJ, West PM, Mancini EJ, Redfield C. </i> Biomol NMR Assign, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"BMRB","id":"27780"}],"region_id":"DP03400r001","statement":[{"text":"The first, dCUE, corresponds to the tandem CUE domains spanning residues 144–295. The second, eCUE, corresponds to only the first CUE domain and the disordered region preceding it (residues 109–206).","type":"Article"},{"text":"The 13Cα, 13Cβ, 13Cʹ 1Hα, 1HN and 15N chemical shifts have been used to predict secondary structure propensities for dCUE and eCUE in solution using TALOS-N; these are plotted as a function of sequence. The predicted secondary structure shows the expected pattern of three α-helices in each CUE domain. Interestingly, a short β-strand is predicted in the otherwise disordered region preceding CUE1.","type":"Article"},{"text":"Annotation of region boundaries was done based on the information that the 1st CUE domain starts at residue 157 and based on Figure 2 a showing that the predicted helices of the domain only start after residue 150.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-05T09:40:39.672Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":200,"end":250,"reference_id":"30919308","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N resonance assignments for the tandem CUE domains from chromatin remodeler SMARCAD1. <i> Biasutto AJ, West PM, Mancini EJ, Redfield C. </i> Biomol NMR Assign, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"BMRB","id":"27785"}],"region_id":"DP03400r002","statement":[{"text":"Secondary structure prediction of the SMARCAD1 sequence suggests that the N-terminal tandem CUE domains, termed CUE1 (residues 157–199) and CUE2 (residues 251–294), are each composed of a three helix bundle and are connected by a disordered linker rich in serines and charged amino acids (residues 200–250).","type":"Article"},{"text":"Moreover, the statistics for dCUE are reported for the individual functional domains, from which it is evident that the relatively poor overall assignment coverage stems from the flexible linker connecting the two CUE domains. This is mostly due to high sequence degeneracy and the lack of structural propensity in this region of the protein.","type":"Article"},{"text":"Lack of secondary structure for the linker region is also evident from Figure 2 a.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-05T09:40:40.328Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":200,"end":250,"reference_id":"30919308","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N resonance assignments for the tandem CUE domains from chromatin remodeler SMARCAD1. <i> Biasutto AJ, West PM, Mancini EJ, Redfield C. </i> Biomol NMR Assign, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"cross_refs":[{"db":"BMRB","id":"27785"}],"region_id":"DP03400r003","statement":[{"text":"Secondary structure prediction of the SMARCAD1 sequence suggests that the N-terminal tandem CUE domains, termed CUE1 (residues 157–199) and CUE2 (residues 251–294), are each composed of a three helix bundle and are connected by a disordered linker rich in serines and charged amino acids (residues 200–250).","type":"Article"},{"text":"Moreover, the statistics for dCUE are reported for the individual functional domains, from which it is evident that the relatively poor overall assignment coverage stems from the flexible linker connecting the two CUE domains. This is mostly due to high sequence degeneracy and the lack of structural propensity in this region of the protein.","type":"Article"},{"text":"No significant changes in chemical shift are observed in the 1H–15N HSQC for the residues of the CUE1 domain in the dCUE and eCUE constructs. This suggests that the N-terminal region, the linker, and the CUE2 domain do not make specific contacts with the CUE1 domain.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-05T09:40:41.703Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":3,"released":"2023_12","sequence":"MNLFNLDRFRFEKRNKIEEAPEATPQPSQPGPSSPISLSAEEENAEGEVSRANTPDSDITEKTEDSSVPETPDNERKASISYFKNQRGIQYIDLSSDSEDVVSPNCSNTVQEKTFNKDTVIIVSEPSEDEESQGLPTMARRNDDISELEDLSELEDLKDAKLQTLKELFPQRSDNDLLKLIESTSTMDGAIAAALLMFGDAGGGPRKRKLSSSSEPYEEDEFNDDQSIKKTRLDHGEESNESAESSSNWEKQESIVLKLQKEFPNFDKQELREVLKEHEWMYTEALESLKVFAEDQDMQYVSQSEVPNGKEVSSRSQNYPKNATKTKLKQKFSMKAQNGFNKKRKKNVFNPKRVVEDSEYDSGSDVGSSLDEDYSSGEEVMEDGYKGKILHFLQDASIGELTLIPQCSQKKAQKITELRPFNSWEALFTKMSKTNGLSEDLIWHCKTLIQERDVVIRLMNKCEDISNKLTKQVTMLTGNGGGWNIEQPSILNQSLSLKPYQKVGLNWLALVHKHGLNGILADEMGLGKTIQAIAFLAYLYQEGNNGPHLIVVPASTIDNWLREVNLWCPTLKVLCYYGSQEERKQIRFNIHSRYEDYNVIVTTYNCAISSSDDRSLFRRLKLNYAIFDEGHMLKNMGSIRYQHLMTINANNRLLLTGTPVQNNLLELMSLLNFVMPHMFSSSTSEIRRMFSSKTKSADEQSIYEKERIAHAKQIIKPFILRRVKEEVLKQLPPKKDRIELCAMSEKQEQLYLGLFNRLKKSINNLEKNTEMCNVMMQLRKMANHPLLHRQYYTAEKLKEMSQLMLKEPTHCEANPDLIFEDMEVMTDFELHVLCKQYRHINNFQLDMDLILDSGKFRVLGCILSELKQKGDRVVLFSQFTMMLDILEVLLKHHQHRYLRLDGKTQISERIHLIDEFNTDMDIFVFLLSTKAGGLGINLTSANVVILHDIDCNPYNDKQAEDRCHRVGQTKEVLVIKLISQGTIEESMLKINQQKLKLEQDMTTVDEGDEGSMPADIATLLKTSMGL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI000013E22F","uniref100":"UniRef100_Q9H4L7","uniref90":"UniRef90_Q9H4L7","uniref50":"UniRef50_Q9H4L7","genes":[{"name":{"value":"SMARCAD1"},"synonyms":[{"value":"KIAA1122"}]}],"alphafold_very_low_content":0.29922027290448344,"disorder_content":0.09064327485380116,"disprot_consensus":{"full":[{"start":109,"end":150,"type":"D"},{"start":200,"end":250,"type":"D"}],"Structural state":[{"start":109,"end":150,"type":"D"},{"start":200,"end":250,"type":"D"}],"Disorder function":[{"start":200,"end":250,"type":"F"}]}},{"acc":"P18272","sequence":"MDSRPQKIWMAPSLTESDMDYHKILTAGLSVQQGIVRQRVIPVYQVNNLEEICQLIIQAFEAGVDFQESADSFLLMLCLHHAYQGDYKLFLESGAVKYLEGHGFRFEVKKRDGVKRLEELLPAVSSGKNIKRTLAAMPEEETTEANAGQFLSFASLFLPKLVVGEKACLEKVQRQIQVHAEQGLIQYPTAWQSVGHMMVIFRLMRTNFLIKFLLIHQGMHMVAGHDANDAVISNSVAQARFSGLLIVKTVLDHILQKTERGVRLHPLARTAKVKNEVNSFKAALSSLAKHGEYAPFARLLNLSGVNNLEHGLFPQLSAIALGVATAHGSTLAGVNVGEQYQQLREAATEAEKQLQQYAESRELDHLGLDDQEKKILMNFHQKKNEISFQQTNAMVTLRKERLAKLTEAITAASLPKTSGHYDDDDDIPFPGPINDDDNPGHQDDDPTDSQDTTIPDVVVDPDDGSYGEYQSYSENGMNAPDDLVLFDLDEDDEDTKPVPNRSTKGGQQKNSQKGQHIEGRQTQSRPIQNVPGPHRTIHHASAPLTDNDRRNEPSGSTSPRMLTPINEEADPLDDADDETSSLPPLESDDEEQDRDGTSNRTPTVAPPAPVYRDHSEKKELPQDEQQDQDHTQEARNQDSDNTQSEHSFEEMYRHILRSQGPFDAVLYYHMMKDEPVVFSTSDGKEYTYPDSLEEEYPPWLTEKEAMNEENRFVTLDGQQFYWPVMNHKNKFMAILQHHQ","creator":"eficho","dataset":["Viral proteins","RNA-binding proteins"],"date":"2021-07-02T14:06:21.148Z","disprot_id":"DP03401","features":{"pfam":[{"id":"PF05505","name":"Ebola nucleoprotein","start":19,"end":734}],"gene3D":[]},"genes":[{"name":{"value":"NP","evidences":[],"_id":"685af523b4ac24d5329d9739"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d9738"}],"length":739,"name":"Nucleoprotein","ncbi_taxon_id":128952,"organism":"Zaire ebolavirus (strain Mayinga-76)","regions_counter":4,"released":"2021_12","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Filoviridae","Ebolavirus"],"UniParc":"UPI0000170E39","uniref100":"UniRef100_P18272","uniref50":"UniRef50_P18272","uniref90":"UniRef90_P18272","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"27847","_id":"685af523b4ac24d5329d9725"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":600,"end":645,"interaction_partner":[],"reference_html":"Backbone resonance assignments and secondary structure of Ebola nucleoprotein 600-739 construct. <i> Lee W, Tonelli M, Wu C, Aceti DJ, Amarasinghe GK, Markley JL. </i> Biomol NMR Assign, 2019","reference_id":"31076990","region_id":"DP03401r001","released":"2022_03","sample":[],"statement":[{"type":"Article","text":" According to the RCI-S2 values provided by TALOS-N (Fig.2.c), the disordered (residues 600‒645) and ordered (residues 646‒739) regions are clearly differentiated.","_id":"685af523b4ac24d5329d9726"},{"type":"Curator statement","text":"A large fraction of the peaks of the presented HSQC spectrum show narrow peak dispersion and fall to the ppm range tipical for IDPs.","_id":"685af523b4ac24d5329d9727"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-21T14:08:10.619Z","_id":"685af523b4ac24d5329d9728"},"version":3,"_id":"685af523b4ac24d5329d9724","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"4YPI","_id":"685af523b4ac24d5329d972a"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":25,"end":62,"interaction_partner":[],"reference_html":"An Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral RNA Synthesis by Modulating Nucleoprotein-RNA Interactions. <i> Leung DW, Borek D, Luthra P, Binning JM, Anantpadma M, Liu G, Harvey IB, Su Z, Endlich-Frazier A, Pan J, Shabman RS, Chiu W, Davey RA, Otwinowski Z, Basler CF, Amarasinghe GK. </i> Cell Rep, 2015","reference_id":"25865894","region_id":"DP03401r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The first 37 residues at the N-terminus are unstructured.","_id":"685af523b4ac24d5329d972b"},{"type":"Curator statement","text":"In this publication the authors solved the crystal structure of the VP35 NPBP/ΔNPNTD complex. ΔNPNTD comprised the residues 25–457 of the Zaire ebolavirus (strain Mayinga-76) nucleoprotein.","_id":"685af523b4ac24d5329d972c"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-21T14:08:11.331Z","_id":"685af523b4ac24d5329d972d"},"version":1,"_id":"685af523b4ac24d5329d9729","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"4YPI","_id":"685af523b4ac24d5329d972f"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006222","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","ec_ontology":"ECO","start":38,"end":240,"interaction_partner":[],"reference_html":"An Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral RNA Synthesis by Modulating Nucleoprotein-RNA Interactions. <i> Leung DW, Borek D, Luthra P, Binning JM, Anantpadma M, Liu G, Harvey IB, Su Z, Endlich-Frazier A, Pan J, Shabman RS, Chiu W, Davey RA, Otwinowski Z, Basler CF, Amarasinghe GK. </i> Cell Rep, 2015","reference_id":"25865894","region_id":"DP03401r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"All four ΔNPNTD molecules are present in the structure. However, the head lobes of molecules B and D show a high degree of disorder with corresponding high average and individual B-factors (Table S1 and Figure S3D). The B-factors indicate that the conformations of head lobes in symmetrically-equivalent copies of these molecules across the crystal lattice differ in their orientation by 1–2 Å. ","_id":"685af523b4ac24d5329d9730"},{"type":"Curator statement","text":"In this publication the authors solved the crystal structure of the VP35 NPBP/ΔNPNTD complex. ΔNPNTD comprised the residues 25–457 of the Zaire ebolavirus (strain Mayinga-76) nucleoprotein. They identified a head lobe spanning NP residues 38 to 240.","_id":"685af523b4ac24d5329d9731"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-21T14:08:14.060Z","_id":"685af523b4ac24d5329d9732"},"version":1,"_id":"685af523b4ac24d5329d972e","reference_source":"pmid"}],"__v":0,"disorder_content":0.35453315290933696,"disprot_consensus":{"full":[{"start":25,"end":240,"type":"D"},{"start":600,"end":645,"type":"D"}],"Structural state":[{"start":25,"end":240,"type":"D"},{"start":600,"end":645,"type":"D"}]}},{"disprot_id":"DP03403","acc":"Q8WXS3-1","creator":"eficho","date":"2021-07-02T14:52:25.984Z","features":{"pfam":[],"gene3D":[]},"length":180,"name":"Isoform 2 of Brain and acute leukemia cytoplasmic protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":180,"reference_id":"32240523","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N Backbone assignments of the human brain and acute leukemia cytoplasmic (BAALC) protein. <i> Lang A, Kumar A, Jirschitzka J, Bordusa F, Ohlenschläger O, Wiedemann C. </i> Biomol NMR Assign, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"BMRB","id":"28084"}],"region_id":"DP03403r001","statement":[{"text":"Analysis of structural elements by the CSI web server (data not shown) resulted in an all-coil prediction. This supports the expectation based upon the appearance of the [1H, 15N]-HSQC spectrum which showed a reduced spectral dispersion of average chemical shifts implying flexibility typical for intrinsically disordered proteins.","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-05T11:12:37.996Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_12","sequence":"MGCGGSRADAIEPRYYESWTRETESTWLTYTDSDAPPSAAAPDSGPEAGGLHSVLEAEKSKIKAPTDSVSDEGLFSASKMAPLAVFSHGMLEDGLPSNGVPRSTAPGGIPNPEKKTNCETQCPNPQSLSSGPLTQKQNGLQTTEAKRDAKRMPAKEVTINVTDSIQQMDRSRRITKNCVN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000071FE0","uniref100":"","uniref90":"","uniref50":"","genes":[{"name":{"value":"BAALC","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11707601","url":"http://www.ncbi.nlm.nih.gov/pubmed/11707601","alternativeUrl":"https://europepmc.org/abstract/MED/11707601"}}]}}],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":180,"type":"D"}],"Structural state":[{"start":1,"end":180,"type":"D"}]}},{"disprot_id":"DP03404","acc":"P56211","creator":"eficho","date":"2021-07-02T15:01:04.312Z","features":{"pfam":[{"id":"PF04667","name":"cAMP-regulated phosphoprotein/endosulfine conserved region","start":26,"end":101}],"gene3D":[]},"length":112,"name":"cAMP-regulated phosphoprotein 19","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":112,"reference_id":"32468417","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP-19 and ARPP-16). <i> Thapa CJ, Haataja T, Pentikäinen U, Permi P. </i> Biomol NMR Assign, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"BMRB","id":"27912"}],"region_id":"DP03404r001","statement":[{"text":"The bioinformatical analyses were experimentally confirmed in 1H–15N 2D HSQC spectra of ARPPs, that is, the disordered nature of ARPPs manifests itself as low dispersion of chemical shift in the 1HN dimension, all amide proton resonances falling between 7.7 and 8.5 ppm.","type":"Article"},{"text":"In this paper, we have presented a nearly complete assignment of main-chain 1H, 13C, and 15N chemical shifts in two intrinsically disordered proteins, ARPP-16 and ARPP-19.","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-06T12:33:34.199Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":112,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-02T15:56:58.145Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"BMRB","id":"51881"}],"region_id":"DP03404r002","statement":[{"text":"The 2D 1H,15N heteronuclear single quantum coherence (HSQC) spectra of unbound ARPP1921,22 and FAM122ANterm confirmed that both are IDPs with multiple regions of amino acids with preferred α-helical propensities (using chemical shift index (CSI) analysis; Extended Data Fig. 3a–f).","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:22:51.604Z"}},{"start":60,"end":65,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-02T16:01:40.005Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"BMRB","id":"51882"}],"region_id":"DP03404r003","statement":[{"text":"The 2D 1H,15N HSQC spectrum of thiophosphorylated ARPP19 identified two phosphorylated residues, Ser62, the established MASTL phosphorylation substrate, and Ser104, a serine that was previously identified as a protein kinase A (PKA) substrate, and also shows recognition site homology to the MASTL specificity sequence23. ","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:23:08.851Z"}},{"start":102,"end":106,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-02T16:01:54.835Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"BMRB","id":"51882"}],"region_id":"DP03404r004","statement":[{"text":"The 2D 1H,15N HSQC spectrum of thiophosphorylated ARPP19 identified two phosphorylated residues, Ser62, the established MASTL phosphorylation substrate, and Ser104, a serine that was previously identified as a protein kinase A (PKA) substrate, and also shows recognition site homology to the MASTL specificity sequence23. ","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:23:11.329Z"}},{"start":20,"end":112,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T15:42:14.269Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051721","term_name":"protein phosphatase 2A binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P67775","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63151","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P30153","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP03404r005","statement":[{"text":"For ARPP19, around 90 N/HN cross-peaks (residues 20–112) showed reduced intensities.","type":"Article"}],"term_comment":"","term_def":"\"Binding to protein phosphatase 2A.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:23:13.286Z"}},{"start":20,"end":75,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T15:42:30.548Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051721","term_name":"protein phosphatase 2A binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P63151","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03404r006","statement":[{"text":"To identify which residues of ARPP19 and FAM122A bind B55, we repeated the NMR experiments using B55 loopless (B55LL), a variant that lacks the PP2Aa binding loop (amino acids 126–164 are replaced with NG; Extended Data Fig. 1a) and is thus unable to bind PP2Aa. Overlaying the 2D 1H,15N HSQC spectra of ARPP19 and tpS62tpS104ARPP19 with and without B55LL showed that the identity and number of N/HN cross-peaks with reduced intensities are similar, but not identical, to those observed with PP2A:B55 (Fig. 1f,g and Extended Data Fig. 5a,b). Specifically, the peaks corresponding to residues 20–75 and 105–112 show significant reductions in intensities, whereas ARPP19 residues 75–104 show little or no intensity loss with B55LL. This shows that two distinct ARPP19 domains—20–75 and 105–112—bind B55.","type":"Article"}],"term_comment":"","term_def":"\"Binding to protein phosphatase 2A.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:23:15.281Z"}},{"start":105,"end":112,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T15:42:50.696Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051721","term_name":"protein phosphatase 2A binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P63151","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03404r007","statement":[{"text":"To identify which residues of ARPP19 and FAM122A bind B55, we repeated the NMR experiments using B55 loopless (B55LL), a variant that lacks the PP2Aa binding loop (amino acids 126–164 are replaced with NG; Extended Data Fig. 1a) and is thus unable to bind PP2Aa. Overlaying the 2D 1H,15N HSQC spectra of ARPP19 and tpS62tpS104ARPP19 with and without B55LL showed that the identity and number of N/HN cross-peaks with reduced intensities are similar, but not identical, to those observed with PP2A:B55 (Fig. 1f,g and Extended Data Fig. 5a,b). Specifically, the peaks corresponding to residues 20–75 and 105–112 show significant reductions in intensities, whereas ARPP19 residues 75–104 show little or no intensity loss with B55LL. This shows that two distinct ARPP19 domains—20–75 and 105–112—bind B55.","type":"Article"}],"term_comment":"","term_def":"\"Binding to protein phosphatase 2A.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:23:18.235Z"}},{"start":42,"end":75,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T15:59:04.699Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051721","term_name":"protein phosphatase 2A binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":62,"end":62,"position":"Specific residue","statements":[{"type":"Article","text":"Because ARPP19 inhibition of PP2A:B55 strictly requires phosphorylation, we also thiophosphorylated ARPP19 using MASTL kinase."},{"type":"Curator statement","text":"The residue is thiophosphorylated, an hydrogen atom is replaced with a thiophosphono group (H2PO2S) http://purl.obolibrary.org/obo/MOD_00583."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser104Ala","start":null,"end":null,"position":null,"statements":[{"type":"Article","text":"Thus, we generated the Ser104 phosphorylation site mutant ARPP19S104A and repeated the thiophosphorylation step to obtain singly thiophosphorylated ARPP19 (tpS62ARPP19S104A; hereafter referred to as tpARPP19)."}]}],"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P67775","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P30151","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP03404r008","sequence_construct":"GHMSAEVPEAASAEEQKEMEDKVTSPEKAEEAKLKARYPHLGQKPGGSDFLRKRLQKGQKYFDSGDYNMAKAKMKNKQLPTAAPDKTEVTGDHIPTPQDLPQRKPALVASKLAG","statement":[{"text":"The remaining unaccounted density corresponds to tpARPP19 or FAM122A (tpARPP19 residues 42–75 and 86–112; FAM122A residues 81–111). tpARPP19 binds exclusively to B55 and PP2Ac using helices connected by extended yet ordered loops (helices are pre-populated in free ARPP19; Extended Data Fig. 3a,c,i).","type":"Article"}],"term_comment":"","term_def":"\"Binding to protein phosphatase 2A.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"cross_refs":[{"db":"PDB","id":"8TTB"},{"db":"EMDB","id":"41604"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:23:20.780Z"}},{"start":86,"end":112,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T16:04:02.102Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051721","term_name":"protein phosphatase 2A binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":62,"end":62,"position":"Specific residue","statements":[{"type":"Article","text":"Because ARPP19 inhibition of PP2A:B55 strictly requires phosphorylation, we also thiophosphorylated ARPP19 using MASTL kinase."},{"type":"Curator statement","text":"The residue is thiophosphorylated, an hydrogen atom is replaced with a thiophosphono group (H2PO2S) http://purl.obolibrary.org/obo/MOD_00583."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser104Ala","start":null,"end":null,"position":null,"statements":[{"type":"Article","text":"Thus, we generated the Ser104 phosphorylation site mutant ARPP19S104A and repeated the thiophosphorylation step to obtain singly thiophosphorylated ARPP19 (tpS62ARPP19S104A; hereafter referred to as tpARPP19)."}]}],"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P67775","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P30151","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP03404r009","sequence_construct":"GHMSAEVPEAASAEEQKEMEDKVTSPEKAEEAKLKARYPHLGQKPGGSDFLRKRLQKGQKYFDSGDYNMAKAKMKNKQLPTAAPDKTEVTGDHIPTPQDLPQRKPALVASKLAG","statement":[{"text":"The remaining unaccounted density corresponds to tpARPP19 or FAM122A (tpARPP19 residues 42–75 and 86–112; FAM122A residues 81–111). tpARPP19 binds exclusively to B55 and PP2Ac using helices connected by extended yet ordered loops (helices are pre-populated in free ARPP19; Extended Data Fig. 3a,c,i).","type":"Article"}],"term_comment":"","term_def":"\"Binding to protein phosphatase 2A.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"cross_refs":[{"db":"PDB","id":"8TTB"},{"db":"EMDB","id":"41604"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P30153"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:23:23.051Z"}},{"start":86,"end":112,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-02T17:09:34.207Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":62,"end":62,"position":"Specific residue","statements":[{"type":"Article","text":"Because ARPP19 inhibition of PP2A:B55 strictly requires phosphorylation, we also thiophosphorylated ARPP19 using MASTL kinase."},{"type":"Curator statement","text":"The residue is thiophosphorylated, an hydrogen atom is replaced with a thiophosphono group (H2PO2S) http://purl.obolibrary.org/obo/MOD_00583."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser104Ala","start":null,"end":null,"position":null,"statements":[{"type":"Article","text":"Thus, we generated the Ser104 phosphorylation site mutant ARPP19S104A and repeated the thiophosphorylation step to obtain singly thiophosphorylated ARPP19 (tpS62ARPP19S104A; hereafter referred to as tpARPP19)."}]}],"region_id":"DP03404r010","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63151"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63153"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P67775"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:29936"}],"sequence_construct":"GHMSAEVPEAASAEEQKEMEDKVTSPEKAEEAKLKARYPHLGQKPGGSDFLRKRLQKGQKYFDSGDYNMAKAKMKNKQLPTAAPDKTEVTGDHIPTPQDLPQRKPALVASKLAG","statement":[{"text":"tpARPP19 binds exclusively to B55 and PP2Ac using helices connected by extended yet ordered loops (helices are pre-populated in free ARPP19; Extended Data Fig. 3a,c,i).","type":"Article"}],"states_connection":[{"source":"DP03404r002","target":"DP03404r011"}],"cross_refs":[{"db":"PDB","id":"8TTB"},{"db":"EMDB","id":"41604"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:23:03.682Z"}},{"start":86,"end":112,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-02T17:09:02.959Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":62,"end":62,"position":"Specific residue","statements":[{"type":"Article","text":"Because ARPP19 inhibition of PP2A:B55 strictly requires phosphorylation, we also thiophosphorylated ARPP19 using MASTL kinase."},{"type":"Curator statement","text":"The residue is thiophosphorylated, an hydrogen atom is replaced with a thiophosphono group (H2PO2S) http://purl.obolibrary.org/obo/MOD_00583."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser104Ala","start":null,"end":null,"position":null,"statements":[{"type":"Article","text":"Thus, we generated the Ser104 phosphorylation site mutant ARPP19S104A and repeated the thiophosphorylation step to obtain singly thiophosphorylated ARPP19 (tpS62ARPP19S104A; hereafter referred to as tpARPP19)."}]}],"region_id":"DP03404r011","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63151"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63153"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P67775"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:29936"}],"sequence_construct":"GHMSAEVPEAASAEEQKEMEDKVTSPEKAEEAKLKARYPHLGQKPGGSDFLRKRLQKGQKYFDSGDYNMAKAKMKNKQLPTAAPDKTEVTGDHIPTPQDLPQRKPALVASKLAG","statement":[{"text":"tpARPP19 binds exclusively to B55 and PP2Ac using helices connected by extended yet ordered loops (helices are pre-populated in free ARPP19; Extended Data Fig. 3a,c,i).","type":"Article"}],"cross_refs":[{"db":"PDB","id":"8TTB"},{"db":"EMDB","id":"41604"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:22:54.023Z"}},{"start":42,"end":75,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-02T17:08:40.087Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":62,"end":62,"position":"Specific residue","statements":[{"type":"Article","text":"Because ARPP19 inhibition of PP2A:B55 strictly requires phosphorylation, we also thiophosphorylated ARPP19 using MASTL kinase."},{"type":"Curator statement","text":"The residue is thiophosphorylated, an hydrogen atom is replaced with a thiophosphono group (H2PO2S) http://purl.obolibrary.org/obo/MOD_00583."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser104Ala","start":null,"end":null,"position":null,"statements":[{"type":"Article","text":"Thus, we generated the Ser104 phosphorylation site mutant ARPP19S104A and repeated the thiophosphorylation step to obtain singly thiophosphorylated ARPP19 (tpS62ARPP19S104A; hereafter referred to as tpARPP19)."}]}],"region_id":"DP03404r012","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63151"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63153"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P67775"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:29936"}],"sequence_construct":"GHMSAEVPEAASAEEQKEMEDKVTSPEKAEEAKLKARYPHLGQKPGGSDFLRKRLQKGQKYFDSGDYNMAKAKMKNKQLPTAAPDKTEVTGDHIPTPQDLPQRKPALVASKLAG","statement":[{"text":"tpARPP19 binds exclusively to B55 and PP2Ac using helices connected by extended yet ordered loops (helices are pre-populated in free ARPP19; Extended Data Fig. 3a,c,i).","type":"Article"}],"cross_refs":[{"db":"PDB","id":"8TTB"},{"db":"EMDB","id":"41604"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:22:56.269Z"}},{"start":42,"end":75,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-02T17:09:21.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":62,"end":62,"position":"Specific residue","statements":[{"type":"Article","text":"Because ARPP19 inhibition of PP2A:B55 strictly requires phosphorylation, we also thiophosphorylated ARPP19 using MASTL kinase."},{"type":"Curator statement","text":"The residue is thiophosphorylated, an hydrogen atom is replaced with a thiophosphono group (H2PO2S) http://purl.obolibrary.org/obo/MOD_00583."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser104Ala","start":null,"end":null,"position":null,"statements":[{"type":"Article","text":"Thus, we generated the Ser104 phosphorylation site mutant ARPP19S104A and repeated the thiophosphorylation step to obtain singly thiophosphorylated ARPP19 (tpS62ARPP19S104A; hereafter referred to as tpARPP19)."}]}],"region_id":"DP03404r013","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63151"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63153"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P67775"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:29936"}],"sequence_construct":"GHMSAEVPEAASAEEQKEMEDKVTSPEKAEEAKLKARYPHLGQKPGGSDFLRKRLQKGQKYFDSGDYNMAKAKMKNKQLPTAAPDKTEVTGDHIPTPQDLPQRKPALVASKLAG","statement":[{"text":"tpARPP19 binds exclusively to B55 and PP2Ac using helices connected by extended yet ordered loops (helices are pre-populated in free ARPP19; Extended Data Fig. 3a,c,i).","type":"Article"}],"states_connection":[{"source":"DP03404r002","target":"DP03404r012"}],"cross_refs":[{"db":"PDB","id":"8TTB"},{"db":"EMDB","id":"41604"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:23:06.016Z"}},{"start":1,"end":41,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-02T17:21:32.411Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":62,"end":62,"position":"Specific residue","statements":[{"type":"Article","text":"Because ARPP19 inhibition of PP2A:B55 strictly requires phosphorylation, we also thiophosphorylated ARPP19 using MASTL kinase."},{"type":"Curator statement","text":"The residue is thiophosphorylated, an hydrogen atom is replaced with a thiophosphono group (H2PO2S) http://purl.obolibrary.org/obo/MOD_00583."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser104Ala","start":null,"end":null,"position":null,"statements":[{"type":"Article","text":"Thus, we generated the Ser104 phosphorylation site mutant ARPP19S104A and repeated the thiophosphorylation step to obtain singly thiophosphorylated ARPP19 (tpS62ARPP19S104A; hereafter referred to as tpARPP19)."}]}],"region_id":"DP03404r014","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63151"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63153"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P67775"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:29936"}],"sequence_construct":"GHMSAEVPEAASAEEQKEMEDKVTSPEKAEEAKLKARYPHLGQKPGGSDFLRKRLQKGQKYFDSGDYNMAKAKMKNKQLPTAAPDKTEVTGDHIPTPQDLPQRKPALVASKLAG","statement":[{"text":"The lack of electron density shows this region is disordered.","type":"Curator statement"},{"text":"The density for these residues is present but amorphous, suggesting that α2 remains somewhat mobile in the B55 bound state (a fuzzy interaction24,31,32).","type":"Article"}],"cross_refs":[{"db":"PDB","id":"8TTB"},{"db":"EMDB","id":"41604"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:22:58.497Z"}},{"start":76,"end":85,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-02T17:20:50.999Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":62,"end":62,"position":"Specific residue","statements":[{"type":"Article","text":"Because ARPP19 inhibition of PP2A:B55 strictly requires phosphorylation, we also thiophosphorylated ARPP19 using MASTL kinase."},{"type":"Curator statement","text":"The residue is thiophosphorylated, an hydrogen atom is replaced with a thiophosphono group (H2PO2S) http://purl.obolibrary.org/obo/MOD_00583."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser104Ala","start":null,"end":null,"position":null,"statements":[{"type":"Article","text":"Thus, we generated the Ser104 phosphorylation site mutant ARPP19S104A and repeated the thiophosphorylation step to obtain singly thiophosphorylated ARPP19 (tpS62ARPP19S104A; hereafter referred to as tpARPP19)."}]}],"region_id":"DP03404r015","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63151"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63153"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P67775"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:29936"}],"sequence_construct":"GHMSAEVPEAASAEEQKEMEDKVTSPEKAEEAKLKARYPHLGQKPGGSDFLRKRLQKGQKYFDSGDYNMAKAKMKNKQLPTAAPDKTEVTGDHIPTPQDLPQRKPALVASKLAG","statement":[{"text":"The lack of electron density shows this region is disordered.","type":"Curator statement"},{"text":"ARPP19 residues 76QLPTAAPD83 remain mobile when bound to PP2A:B55.","type":"Article"}],"cross_refs":[{"db":"PDB","id":"8TTB"},{"db":"EMDB","id":"41604"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:23:00.898Z"}},{"start":25,"end":41,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T15:58:54.125Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051721","term_name":"protein phosphatase 2A binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":62,"end":62,"position":"Specific residue","statements":[{"type":"Article","text":"Because ARPP19 inhibition of PP2A:B55 strictly requires phosphorylation, we also thiophosphorylated ARPP19 using MASTL kinase."},{"type":"Curator statement","text":"The residue is thiophosphorylated, an hydrogen atom is replaced with a thiophosphono group (H2PO2S) http://purl.obolibrary.org/obo/MOD_00583."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser104Ala","start":null,"end":null,"position":null,"statements":[{"type":"Article","text":"Thus, we generated the Ser104 phosphorylation site mutant ARPP19S104A and repeated the thiophosphorylation step to obtain singly thiophosphorylated ARPP19 (tpS62ARPP19S104A; hereafter referred to as tpARPP19)."}]}],"cross_refs":[{"db":"PDB","id":"8TTB"},{"db":"EMDB","id":"41604"}],"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P63151","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03404r016","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63151"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63153"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P67775"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:29936"}],"sequence_construct":"GHMSAEVPEAASAEEQKEMEDKVTSPEKAEEAKLKARYPHLGQKPGGSDFLRKRLQKGQKYFDSGDYNMAKAKMKNKQLPTAAPDKTEVTGDHIPTPQDLPQRKPALVASKLAG","statement":[{"text":"ARPP19 residues 25–41 include helix α2 (25–34) and bind the cleft between B55 loops L4/5 (L4/5 refers to the loop connecting β-propellers 4 and 5) and between L5/6 (B55 adopts a WD40 fold composed of 7 β-propellers connected by 7 loops). The density for these residues is present but amorphous, suggesting that α2 remains somewhat mobile in the B55 bound state (a fuzzy interaction24,31,32).","type":"Article"}],"term_comment":"","term_def":"\"Binding to protein phosphatase 2A.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:23:25.518Z"}},{"start":32,"end":41,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T16:00:50.312Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051721","term_name":"protein phosphatase 2A binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00484","term_name":"deletion-insertion","term_namespace":"Protein mutation","value":"p.Leu32_Tyr36delinsAlaAlaAlaAlaAla","start":null,"end":null,"position":null},{"term_id":"IDPO:00484","term_name":"deletion-insertion","term_namespace":"Protein mutation","value":"p.Phe37_Gln41delinsAlaAlaAlaAlaAla","start":null,"end":null,"position":null},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P63151","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03404r017","statement":[{"text":"To test α2 binding to PP2A:B55 in cells, we generated YFP–ARPP19 variants in which either five amino acids (5-Ala, 32AAAAA36 or 37AAAAA41) or one amino acid (32–41) were changed to alanine (or A34G) and then tested their ability to pull down PP2A:B55 from cells (Fig. 3b and Extended Data Fig. 9e,f). Although only a single point variant exhibited reduced B55 and PP2Ac binding (Y36A), both 5-Ala variants of YFP–ARPP19—32–36 and 37–41—were unable to pull down B55.","type":"Article"}],"term_comment":"","term_def":"\"Binding to protein phosphatase 2A.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:23:28.036Z"}},{"start":47,"end":56,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T16:01:45.369Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051721","term_name":"protein phosphatase 2A binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00484","term_name":"deletion-insertion","term_namespace":"Protein mutation","value":"p.Asp47_Lys51delinsAlaAlaAlaAlaAla","start":null,"end":null,"position":null},{"term_id":"IDPO:00484","term_name":"deletion-insertion","term_namespace":"Protein mutation","value":"p.Arg52_Gly56delinsAlaAlaAlaAlaAla","start":null,"end":null,"position":null},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P67775","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P30151","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP03404r018","statement":[{"text":"To test whether these ARPP19 residues contribute to B55 binding in cells, we generated 5-Ala and single point variants for the ARPP19 α2–α3 loop and helix α3 and tested their ability to pull down PP2A:B55 from cells. Although B55 binding to the 42AAAAA46 variant was unchanged, the 47AAAAA51 and 52AAAAA56 variants could not pull down B55 (Fig. 3b). Multiple single alanine mutations for ARPP19 residues 47–56 also exhibited reductions in B55 and PP2Ac binding, particularly L53A and R52A (less than 25% compared with wild type), R50A and F48A (around 50% compared with wild type) and L49A and K55A (approximately 75% compared with wild type) (Fig. 3e and Extended Data Fig. 9g).","type":"Article"}],"term_comment":"","term_def":"\"Binding to protein phosphatase 2A.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:23:30.783Z"}},{"start":57,"end":76,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T16:02:15.876Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051721","term_name":"protein phosphatase 2A binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00484","term_name":"deletion-insertion","term_namespace":"Protein mutation","value":"p.Gln57_Asp61delinsAlaAlaAlaAlaAla","start":null,"end":null,"position":null},{"term_id":"IDPO:00484","term_name":"deletion-insertion","term_namespace":"Protein mutation","value":"p.Pro62_Asn66delinsAlaAlaAlaAlaAla","start":null,"end":null,"position":null},{"term_id":"IDPO:00484","term_name":"deletion-insertion","term_namespace":"Protein mutation","value":"p.Met67_Lys71delinsAlaAlaAlaAlaAla","start":null,"end":null,"position":null},{"term_id":"IDPO:00484","term_name":"deletion-insertion","term_namespace":"Protein mutation","value":"p.Met72_Gln76delinsAlaAlaAlaAlaAla","start":null,"end":null,"position":null},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P63151","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03404r019","statement":[{"text":"Consistent with the structure, pull-down experiments using YFP–ARPP19 5-Ala variants, in which the kink and helix α4 residues are mutated to alanine (57AAAAA61, 62AAAAA66, 67AAAAA71 and 72AAAAA76), weaken B55 binding, albeit not to the same extent as 5-Ala variants of α2 or α3 (Fig. 3b).","type":"Article"}],"term_comment":"","term_def":"\"Binding to protein phosphatase 2A.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:23:32.676Z"}},{"start":76,"end":112,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T15:01:34.016Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0004864","term_name":"protein phosphatase inhibitor activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gln76Gly112del","start":null,"end":null,"position":null},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":62,"end":62,"position":"Specific residue","statements":[{"type":"Article","text":"Because ARPP19 inhibition of PP2A:B55 strictly requires phosphorylation, we also thiophosphorylated ARPP19 using MASTL kinase."},{"type":"Curator statement","text":"The residue is thiophosphorylated, an hydrogen atom is replaced with a thiophosphono group (H2PO2S) http://purl.obolibrary.org/obo/MOD_00583."}]}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P67775","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63151","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63153","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP03404r020","statement":[{"text":"Similarly, comparing the half-maximal inhibitory concentrations (IC50) of ARPP19 and a C-terminal deletion (ARPP19–75) with and without thiophosphorylation shows that the interaction of the C terminus with B55 is essential for the potent inhibition of PP2A:B55 (Fig. 3l and Extended Data Table 1), as the C-terminal deletion variants either do not inhibit (non-phosphorylated ARPP19 versus ARPP1919–75) or become a more than 50-fold weaker inhibitor (tpARPP19 versus tpARPP1919–75).","type":"Article"}],"term_comment":"","term_def":"\"Binds to and stops, prevents or reduces the activity of a protein phosphatase, an enzyme that hydrolyzes phosphate groups from phosphorylated proteins.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:23:34.786Z"}},{"start":1,"end":112,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T16:28:37.736Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0004864","term_name":"protein phosphatase inhibitor activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":62,"end":62,"position":"Specific residue","statements":[{"type":"Article","text":"The 2D 1H,15N HSQC spectrum of thiophosphorylated ARPP19 identified two phosphorylated residues, Ser62, the established MASTL phosphorylation substrate, and Ser104, a serine that was previously identified as a protein kinase A (PKA) substrate, and also shows recognition site homology to the MASTL specificity sequence23."},{"type":"Curator statement","text":"The residue is thiophosphorylated, an hydrogen atom is replaced with a thiophosphono group (H2PO2S) http://purl.obolibrary.org/obo/MOD_00583."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":104,"end":104,"position":"Specific residue","statements":[{"type":"Article","text":"The 2D 1H,15N HSQC spectrum of thiophosphorylated ARPP19 identified two phosphorylated residues, Ser62, the established MASTL phosphorylation substrate, and Ser104, a serine that was previously identified as a protein kinase A (PKA) substrate, and also shows recognition site homology to the MASTL specificity sequence23."},{"type":"Curator statement","text":"The residue is thiophosphorylated, an hydrogen atom is replaced with a thiophosphono group (H2PO2S) http://purl.obolibrary.org/obo/MOD_00583."}]}],"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P67775","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63151","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63153","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP03404r021","statement":[{"text":"We quantified PP2A:B55 inhibition by ARPP19, thiophosphorylated ARPP19 (full-length (amino acids 1–112) and phosphorylated with ATPγS using MASTL kinase) and FAM122A (N-terminal domain (amino acids 1–124) (FAM122ANterm)) (Fig. 1b). Whereas PP2A:B55 was only moderately inhibited by ARPP19, it was strongly inhibited by both thiophosphorylated ARPP19 and FAM122ANterm (Extended Data Table 1 and Extended Data Fig. 2a), with thiophosphorylated ARPP19 inhibiting PP2A:B55 around 250-fold more potently than FAM122A.","type":"Article"}],"term_comment":"","term_def":"\"Binds to and stops, prevents or reduces the activity of a protein phosphatase, an enzyme that hydrolyzes phosphate groups from phosphorylated proteins.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:23:37.315Z"}},{"start":20,"end":112,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-04T09:18:05.330Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP03404r022","statement":[{"text":"For ARPP19, around 90 N/HN cross-peaks (residues 20–112) showed reduced intensities.","type":"Article"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-24T14:55:34.161Z"}}],"regions_counter":22,"released":"2023_12","sequence":"MSAEVPEAASAEEQKEMEDKVTSPEKAEEAKLKARYPHLGQKPGGSDFLRKRLQKGQKYFDSGDYNMAKAKMKNKQLPTAAPDKTEVTGDHIPTPQDLPQRKPSLVASKLAG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI000000030A","uniref100":"UniRef100_P56211","uniref90":"UniRef90_P56211","uniref50":"UniRef50_P56211","genes":[{"name":{"value":"ARPP19"}}],"alphafold_very_low_content":0.07142857142857142,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":41,"type":"D"},{"start":42,"end":75,"type":"T"},{"start":76,"end":85,"type":"D"},{"start":86,"end":112,"type":"T"}],"Structural state":[{"start":1,"end":112,"type":"D"}],"Disorder function":[{"start":60,"end":65,"type":"F"},{"start":102,"end":106,"type":"F"}],"Molecular function":[{"start":1,"end":112,"type":"F"}],"Structural transition":[{"start":42,"end":75,"type":"T"},{"start":86,"end":112,"type":"T"}]}},{"disprot_id":"DP03405","acc":"P56211-2","creator":"eficho","date":"2021-07-02T15:04:46.553Z","features":{"pfam":[],"gene3D":[]},"length":96,"name":"Isoform ARPP-16 of cAMP-regulated phosphoprotein 19","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":96,"reference_id":"32468417","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP-19 and ARPP-16). <i> Thapa CJ, Haataja T, Pentikäinen U, Permi P. </i> Biomol NMR Assign, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"BMRB","id":"27911"}],"region_id":"DP03405r001","statement":[{"text":"The bioinformatical analyses were experimentally confirmed in 1H–15N 2D HSQC spectra of ARPPs, that is, the disordered nature of ARPPs manifests itself as low dispersion of chemical shift in the 1HN dimension, all amide proton resonances falling between 7.7 and 8.5 ppm.","type":"Article"},{"text":"In this paper, we have presented a nearly complete assignment of main-chain 1H, 13C, and 15N chemical shifts in two intrinsically disordered proteins, ARPP-16 and ARPP-19.","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-06T12:34:23.758Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_12","sequence":"MEDKVTSPEKAEEAKLKARYPHLGQKPGGSDFLRKRLQKGQKYFDSGDYNMAKAKMKNKQLPTAAPDKTEVTGDHIPTPQDLPQRKPSLVASKLAG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI00001FE4F6","uniref100":"","uniref90":"","uniref50":"","genes":[{"name":{"value":"ARPP19"}}],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":96,"type":"D"}],"Structural state":[{"start":1,"end":96,"type":"D"}]}},{"disprot_id":"DP03406","acc":"P0A7G2","creator":"eficho","date":"2021-07-02T20:31:15.327Z","features":{"pfam":[{"id":"PF02033","name":"Ribosome-binding factor A","start":7,"end":112}],"gene3D":[]},"length":133,"name":"30S ribosome-binding factor","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":101,"end":133,"reference_id":"32671633","reference_source":"pmid","reference_html":"Backbone and sidechain NMR assignments for the ribosome maturation factor RbfA from Escherichia coli. <i> Schedlbauer A, Iturrioz I, Ochoa-Lizarralde B, Çapuni R, Han X, de Astigarraga E, Diercks T, Fucini P, Connell SR. </i> Biomol NMR Assign, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"BMRB","id":"27857"}],"region_id":"DP03406r001","statement":[{"text":"Order parameters, S2, derived by comparing CSI versus RCI values, indicate an increased flexibility for the 33 C-terminal residues of RbfA.","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-08T14:30:49.114Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":109,"end":133,"reference_id":"12628255","reference_source":"pmid","reference_html":"Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock adaptation protein from Escherichia coli. <i> Huang YJ, Swapna GV, Rajan PK, Ke H, Xia B, Shukla K, Inouye M, Montelione GT. </i> J Mol Biol, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03406r002","statement":[{"text":"Limited  tryptic  proteolysis  of purified   full-length   RbfA   revealed   preferential cleavage   at   residue   Arg108,   indicating   that   the C-terminal  25  residue  sequence  is  susceptible  to digestion by protease and possibly flexible.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-08T14:30:48.039Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":109,"end":133,"reference_id":"12963368","reference_source":"pmid","reference_html":"The role of RbfA in 16S rRNA processing and cell growth at low temperature in Escherichia coli. <i> Xia B, Ke H, Shinde U, Inouye M. </i> J Mol Biol, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03406r003","statement":[{"text":"A  limited  trypsin  proteolysis  revealed  that  RbfA indeed  contained  an  easily  degradable  portion and   a   relatively   compact   region   resistant   to moderate  proteolysis .  The  molecular mass of the trypsin-resistant fragment was determined   to   be   12,143 Da   by   mass   spectroscopy, which  corresponds  to  an  RbfA  fragment  with  its C-terminal 25 residues truncated. ","type":"Results"},{"text":"The limited proteolysis data suggest that RbfA may have a C-terminal extension that is poorly  structured at least when the protein exists free from ribosomes.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-08T14:30:47.018Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":109,"end":133,"reference_id":"12963368","reference_source":"pmid","reference_html":"The role of RbfA in 16S rRNA processing and cell growth at low temperature in Escherichia coli. <i> Xia B, Ke H, Shinde U, Inouye M. </i> J Mol Biol, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03406r004","statement":[{"text":"In order to test whether the C-terminal regions of RbfA share a similar function, we studied the cellular localization of RbfAD25 by sucrose density-gradient centrifugation   followed by Western blotting. In cells expressing exogenous full-length RbfA, although the majority of the protein existed in soluble fractions, a significant amount co-fractionated with 30 S ribosomal subunits. In contrast, the truncated protein existed exclusively in the soluble fractions,  indicating that the C-terminal region of RbfA is required for its stable binding to 30 S subunits.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-08T14:30:50.278Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":4,"released":"2021_12","sequence":"MAKEFGRPQRVAQEMQKEIALILQREIKDPRLGMMTTVSGVEMSRDLAYAKVYVTFLNDKDEDAVKAGIKALQEASGFIRSLLGKAMRLRIVPELTFFYDNSLVEGMRMSNLVTSVVKHDEERRVNPDDSKED","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"UniParc":"UPI00001654F8","uniref100":"UniRef100_A7ZS64","uniref90":"UniRef90_A7ZS64","uniref50":"UniRef50_A0KNE2","genes":[{"name":{"value":"rbfA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00003","url":"https://hamap.expasy.org/unirule/MF_00003"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"7535280","url":"http://www.ncbi.nlm.nih.gov/pubmed/7535280","alternativeUrl":"https://europepmc.org/abstract/MED/7535280"}}]},"synonyms":[{"value":"P15B","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"2849753","url":"http://www.ncbi.nlm.nih.gov/pubmed/2849753","alternativeUrl":"https://europepmc.org/abstract/MED/2849753"}}]},{"value":"yhbB"}],"olnNames":[{"value":"b3167"},{"value":"JW3136"}]}],"alphafold_very_low_content":0.05263157894736842,"dataset":["Stress response proteins"],"disorder_content":0.24812030075187969,"disprot_consensus":{"full":[{"start":101,"end":133,"type":"D"}],"Structural state":[{"start":101,"end":133,"type":"D"}],"Molecular function":[{"start":109,"end":133,"type":"F"}]}},{"disprot_id":"DP03407","acc":"P51397","creator":"eficho","date":"2021-07-02T20:41:15.038Z","features":{"pfam":[{"id":"PF15228","name":"Death-associated protein","start":12,"end":101}],"gene3D":[]},"length":102,"name":"Death-associated protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":102,"reference_id":"33263927","reference_source":"pmid","reference_html":"Backbone and nearly complete side-chain chemical shift assignments of the human death-associated protein 1 (DAP1). <i> Wiedemann C, Voigt J, Jirschitzka J, Häfner S, Ohlenschläger O, Bordusa F. </i> Biomol NMR Assign, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"BMRB","id":"50465"}],"region_id":"DP03407r001","statement":[{"text":"The limited spectral dispersion, mainly in the 1HN region, and the lack of defined secondary structure elements, predicted based on chemical shifts, identifies human DAP1 as an intrinsically disordered protein (IDP).","type":"Abstract"},{"text":"The [1H, 15N]-HSQC spectrum shows a limited signal dispersion in the 1H dimension typically observed for highly flexible or intrinsically disordered proteins. ","type":"Article"},{"text":"The analysis of secondary structure content from the assigned chemical shifts by the CSI web server predicts an all coil formation for the entire human DAP1.","type":"Article"},{"text":"In addition, we analyzed the chemical shift data using the secondary structure propensity (SSP) method to reveal potential structural elements. Even when applying this method no relevant α-helical and β-sheet elements can be detected in the human DAP1 protein. The overall content of α-helical and β-sheet elements estimated by the SSP method amounts to 0% and 14%, respectively. From the experimental data and the structural predictions derived, it becomes clear that the human DAP1 is an intrinsically disordered protein under the chosen conditions.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-05T09:45:31.955Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_12","sequence":"MSSPPEGKLETKAGHPPAVKAGGMRIVQKHPHTGDTKEEKDKDDQEWESPSPPKPTVFISGVIARGDKDFPPAAAQVAHQKPHASMDKHPSPRTQHIQQPRK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000128E2E","uniref100":"UniRef100_P51397","uniref90":"UniRef90_P51397","uniref50":"UniRef50_P51397","genes":[{"name":{"value":"DAP"},"synonyms":[{"value":"DAP1"}]}],"alphafold_very_low_content":0.06862745098039216,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":102,"type":"D"}],"Structural state":[{"start":1,"end":102,"type":"D"}]}},{"disprot_id":"DP03409","acc":"Q61937","creator":"esalladini","date":"2021-07-07T11:02:00.378Z","features":{"pfam":[{"id":"PF03066","name":"Nucleoplasmin/nucleophosmin domain","start":16,"end":118},{"id":"PF16276","name":"Nucleophosmin C-terminal domain","start":243,"end":291}],"gene3D":[]},"length":292,"name":"Nucleophosmin","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":1,"end":12,"reference_id":"24616519","reference_source":"pmid","reference_html":"Structural polymorphism in the N-terminal oligomerization domain of NPM1. <i> Mitrea DM, Grace CR, Buljan M, Yun MK, Pytel NJ, Satumba J, Nourse A, Park CG, Madan Babu M, White SW, Kriwacki RW. </i> Proc Natl Acad Sci U S A, 2014","date":"2023-07-17T14:12:04.687Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":3,"cross_refs":[{"db":"PDB","id":"4N8M"}],"region_id":"DP03409r001","statement":[{"text":"The construct studied includes the previously characterized core domain, which incorporates acidic tract A1 (29), and additionally contains the complete N terminus and a disordered C-terminal segment (residues 123–130) containing a CK2 phosphorylation site (Ser125) (20) and acidic tract A2 associated with histone chaperone activity (30).","type":"Results"},{"text":"The N- and C-termini are highly flexible and are not observed in the structure.","type":"Figure"}],"ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":200,"db":"PubChem","id":"CID:5234","statements":[{"type":"Results","text":"We crystallized pentameric Npm-N in the presence of 0.2 M NaCl but were unable to crystallize monomeric Npm-N in the absence of salt."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:104729"}]},{"start":1,"end":130,"reference_id":"24616519","reference_source":"pmid","reference_html":"Structural polymorphism in the N-terminal oligomerization domain of NPM1. <i> Mitrea DM, Grace CR, Buljan M, Yun MK, Pytel NJ, Satumba J, Nourse A, Park CG, Madan Babu M, White SW, Kriwacki RW. </i> Proc Natl Acad Sci U S A, 2014","date":"2023-07-17T14:06:40.903Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03409r002","statement":[{"text":"CD spectra confirmed that, in solution, Npm-N exhibited β-sheet secondary structure in the presence of 0.15 M NaCl (termed the “high-salt” form; Fig. 2C, blue trace). However, in the absence of NaCl (termed the “low-salt” form; Fig. 2C, red trace), Npm-N was disordered.","type":"Results"},{"text":"(C) CD wavelength scans of disordered Npm-N in the absence of NaCl (red) and folded Npm-N in the presence of 0.2 M NaCl (blue).","type":"Figure"},{"text":"Npm-N converts from a folded pentamer to a disordered monomer as a function of Na+ concentration.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":150,"db":"PubChem","id":"CID:5234"}],"sequence_construct":"GSHMEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEDE","states_connection":[{"source":"DP03409r008","target":"DP03409r005"}]},{"start":1,"end":130,"reference_id":"24616519","reference_source":"pmid","reference_html":"Structural polymorphism in the N-terminal oligomerization domain of NPM1. <i> Mitrea DM, Grace CR, Buljan M, Yun MK, Pytel NJ, Satumba J, Nourse A, Park CG, Madan Babu M, White SW, Kriwacki RW. </i> Proc Natl Acad Sci U S A, 2014","date":"2023-07-17T14:05:31.929Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03409r003","statement":[{"text":"Velocity sedimentation AUC analysis shows the folded state to be pentameric and the disordered state to be monomeric.","type":"Figure"},{"text":"Analysis using sedimentation velocity analytical ultracentrifugation (AUC) confirmed that the high-salt form of Npm-N was pentameric (Fig. 2D, blue trace, and SI Appendix, Table S3) and that the disordered, low-salt form was an elongated monomer (Fig. 2D, red trace, and SI Appendix, Table S3).","type":"Results"},{"text":"Npm-N converts from a folded pentamer to a disordered monomer as a function of Na+ concentration.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":200,"db":"PubChem","id":"CID:5234"}],"sequence_construct":"GSHMEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEDE","states_connection":[{"source":"DP03409r007","target":"DP03409r006"}]},{"start":1,"end":130,"reference_id":"24616519","reference_source":"pmid","reference_html":"Structural polymorphism in the N-terminal oligomerization domain of NPM1. <i> Mitrea DM, Grace CR, Buljan M, Yun MK, Pytel NJ, Satumba J, Nourse A, Park CG, Madan Babu M, White SW, Kriwacki RW. </i> Proc Natl Acad Sci U S A, 2014","date":"2023-07-17T13:51:59.130Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03409r005","sequence_construct":"GSHMEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEDE","statement":[{"text":"However, in the absence of NaCl (termed the “low-salt” form; Fig. 2C, red trace), Npm-N was disordered.","type":"Results"},{"text":"(C) CD wavelength scans of disordered Npm-N in the absence of NaCl (red) and folded Npm-N in the presence of 0.2 M NaCl (blue).","type":"Figure"}]},{"start":1,"end":130,"reference_id":"24616519","reference_source":"pmid","reference_html":"Structural polymorphism in the N-terminal oligomerization domain of NPM1. <i> Mitrea DM, Grace CR, Buljan M, Yun MK, Pytel NJ, Satumba J, Nourse A, Park CG, Madan Babu M, White SW, Kriwacki RW. </i> Proc Natl Acad Sci U S A, 2014","date":"2023-07-17T14:02:45.538Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03409r006","sequence_construct":"GSHMEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEDE","statement":[{"text":"Analysis using sedimentation velocity analytical ultracentrifugation (AUC) confirmed that the high-salt form of Npm-N was pentameric (Fig. 2D, blue trace, and SI Appendix, Table S3) and that the disordered, low-salt form was an elongated monomer (Fig. 2D, red trace, and SI Appendix, Table S3).","type":"Results"}]},{"start":1,"end":130,"reference_id":"24616519","reference_source":"pmid","reference_html":"Structural polymorphism in the N-terminal oligomerization domain of NPM1. <i> Mitrea DM, Grace CR, Buljan M, Yun MK, Pytel NJ, Satumba J, Nourse A, Park CG, Madan Babu M, White SW, Kriwacki RW. </i> Proc Natl Acad Sci U S A, 2014","date":"2023-07-17T14:05:06.751Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03409r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":200,"db":"PubChem","id":"CID:5234"}],"sequence_construct":"GSHMEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEDE","statement":[{"text":"Analysis using sedimentation velocity analytical ultracentrifugation (AUC) confirmed that the high-salt form of Npm-N was pentameric (Fig. 2D, blue trace, and SI Appendix, Table S3) and that the disordered, low-salt form was an elongated monomer (Fig. 2D, red trace, and SI Appendix, Table S3).","type":"Results"},{"text":" (D) Velocity sedimentation AUC analysis shows the folded state to be pentameric and the disordered state to be monomeric.","type":"Figure"}]},{"start":1,"end":130,"reference_id":"24616519","reference_source":"pmid","reference_html":"Structural polymorphism in the N-terminal oligomerization domain of NPM1. <i> Mitrea DM, Grace CR, Buljan M, Yun MK, Pytel NJ, Satumba J, Nourse A, Park CG, Madan Babu M, White SW, Kriwacki RW. </i> Proc Natl Acad Sci U S A, 2014","date":"2023-07-17T14:06:22.367Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03409r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":200,"db":"PubChem","id":"CID:5234"}],"sequence_construct":"GSHMEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEDE","statement":[{"text":"CD spectra confirmed that, in solution, Npm-N exhibited β-sheet secondary structure in the presence of 0.15 M NaCl (termed the “high-salt” form; Fig. 2C, blue trace).","type":"Results"},{"text":"(C) CD wavelength scans of disordered Npm-N in the absence of NaCl (red) and folded Npm-N in the presence of 0.2 M NaCl (blue).","type":"Figure"}]},{"start":1,"end":130,"reference_id":"24616519","reference_source":"pmid","reference_html":"Structural polymorphism in the N-terminal oligomerization domain of NPM1. <i> Mitrea DM, Grace CR, Buljan M, Yun MK, Pytel NJ, Satumba J, Nourse A, Park CG, Madan Babu M, White SW, Kriwacki RW. </i> Proc Natl Acad Sci U S A, 2014","date":"2023-07-17T14:07:52.516Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03409r009","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":200,"db":"PubChem","id":"CID:5234"}],"sequence_construct":"GSHMEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEDE","statement":[{"text":"These findings were confirmed by using NMR spectroscopy; 2D [1H,15N] TROSY (33) spectra showed that the high-salt form of Npm-N was folded (Fig. 2E, blue spectrum) in a conformation consistent with that observed in the crystal structure (SI Appendix, Fig. S3A), and that the low-salt form was disordered (Fig. 2E, red spectrum, and SI Appendix, Fig. S3B).","type":"Results"},{"text":"(E) Two-dimensional transverse relaxation-optimized spectroscopy (TROSY) spectral overlay of the monomeric (red) and pentameric (blue) folds of 2H/15N-labeled Npm-N.","type":"Figure"}]},{"start":1,"end":130,"reference_id":"24616519","reference_source":"pmid","reference_html":"Structural polymorphism in the N-terminal oligomerization domain of NPM1. <i> Mitrea DM, Grace CR, Buljan M, Yun MK, Pytel NJ, Satumba J, Nourse A, Park CG, Madan Babu M, White SW, Kriwacki RW. </i> Proc Natl Acad Sci U S A, 2014","date":"2023-07-17T14:09:15.331Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03409r010","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":200,"db":"PubChem","id":"CID:5234"}],"sequence_construct":"GSHMEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEDE","statement":[{"text":"These findings were confirmed by using NMR spectroscopy; 2D [1H,15N] TROSY (33) spectra showed that the high-salt form of Npm-N was folded (Fig. 2E, blue spectrum) in a conformation consistent with that observed in the crystal structure (SI Appendix, Fig. S3A), and that the low-salt form was disordered (Fig. 2E, red spectrum, and SI Appendix, Fig. S3B).","type":"Results"},{"text":"(E) Two-dimensional transverse relaxation-optimized spectroscopy (TROSY) spectral overlay of the monomeric (red) and pentameric (blue) folds of 2H/15N-labeled Npm-N.","type":"Figure"}],"states_connection":[{"source":"DP03409r009","target":"DP03409r011"}]},{"start":1,"end":130,"reference_id":"24616519","reference_source":"pmid","reference_html":"Structural polymorphism in the N-terminal oligomerization domain of NPM1. <i> Mitrea DM, Grace CR, Buljan M, Yun MK, Pytel NJ, Satumba J, Nourse A, Park CG, Madan Babu M, White SW, Kriwacki RW. </i> Proc Natl Acad Sci U S A, 2014","date":"2023-07-17T14:08:53.031Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03409r011","sequence_construct":"GSHMEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEDE","statement":[{"text":"These findings were confirmed by using NMR spectroscopy; 2D [1H,15N] TROSY (33) spectra showed that the high-salt form of Npm-N was folded (Fig. 2E, blue spectrum) in a conformation consistent with that observed in the crystal structure (SI Appendix, Fig. S3A), and that the low-salt form was disordered (Fig. 2E, red spectrum, and SI Appendix, Fig. S3B).","type":"Results"},{"text":"(E) Two-dimensional transverse relaxation-optimized spectroscopy (TROSY) spectral overlay of the monomeric (red) and pentameric (blue) folds of 2H/15N-labeled Npm-N.","type":"Figure"}]},{"start":121,"end":130,"reference_id":"24616519","reference_source":"pmid","reference_html":"Structural polymorphism in the N-terminal oligomerization domain of NPM1. <i> Mitrea DM, Grace CR, Buljan M, Yun MK, Pytel NJ, Satumba J, Nourse A, Park CG, Madan Babu M, White SW, Kriwacki RW. </i> Proc Natl Acad Sci U S A, 2014","date":"2023-07-17T14:13:34.219Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03409r012","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":200,"db":"PubChem","id":"CID:5234","statements":[{"type":"Results","text":"We crystallized pentameric Npm-N in the presence of 0.2 M NaCl but were unable to crystallize monomeric Npm-N in the absence of salt."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:104729"}],"sequence_construct":"GSHMEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEDE","statement":[{"text":"The construct studied includes the previously characterized core domain, which incorporates acidic tract A1 (29), and additionally contains the complete N terminus and a disordered C-terminal segment (residues 123–130) containing a CK2 phosphorylation site (Ser125) (20) and acidic tract A2 associated with histone chaperone activity (30).","type":"Results"},{"text":"The N- and C-termini are highly flexible and are not observed in the structure.","type":"Figure"}]}],"regions_counter":12,"released":"2021_12","sequence":"MEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEDEEDVKLLGMSGKRSAPGGGNKVPQKKVKLDEDDEDDDEDDEDDEDDDDDDFDEEETEEKVPVKKSVRDTPAKNAQKSNQNGKDLKPSTPRSKGQESFKKQEKTPKTPKGPSSVEDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"UniParc":"UPI0000003F61","uniref100":"UniRef100_Q61937","uniref90":"UniRef90_Q61937","uniref50":"UniRef50_Q61937","genes":[{"name":{"value":"Npm1"}}],"alphafold_very_low_content":0.23972602739726026,"dataset":["RNA-binding proteins"],"disorder_content":0.4452054794520548,"disprot_consensus":{"full":[{"start":1,"end":130,"type":"T"}],"Structural state":[{"start":1,"end":130,"type":"D"}],"Structural transition":[{"start":1,"end":130,"type":"T"}]}},{"disprot_id":"DP03410","acc":"Q91MK1","creator":"eficho","date":"2021-07-09T06:51:26.420Z","features":{"pfam":[{"id":"PF03210","name":"Paramyxovirus P/V phosphoprotein C-terminal","start":230,"end":383},{"id":"PF14313","name":"N-terminal region of Paramyxovirinae phosphoprotein (P)","start":2,"end":56}],"gene3D":[]},"length":388,"name":"Phosphoprotein","ncbi_taxon_id":152219,"organism":"Menangle virus","regions":[{"start":267,"end":336,"reference_id":"30680534","reference_source":"pmid","reference_html":"NMR chemical shift assignment of the C-terminal region of the Menangle virus phosphoprotein. <i> Herr N, Webby MN, Bulloch EMM, Schmitz M, Kingston RL. </i> Biomol NMR Assign, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"BMRB","id":"27634"}],"region_id":"DP03410r001","statement":[{"text":"Conversely, residues from the flexible linker (amino acids 267–336) are poorly dispersed in the proton dimension, ranging from 8.06 ppm (A318) to 8.61 ppm (S334).","type":"Article"},{"text":"The disordered linker is not, however, a statistical random-coil over its entire length. The temperature-dependent attenuation of 1H–15N HSQC peak intensities is particularly pronounced for residues 279–287. This correlates with observed chemical shift deviations from random coil values, as well as the predicted helical propensity of the sequence (not shown).","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-09T11:45:30.879Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":267,"end":336,"reference_id":"30680534","reference_source":"pmid","reference_html":"NMR chemical shift assignment of the C-terminal region of the Menangle virus phosphoprotein. <i> Herr N, Webby MN, Bulloch EMM, Schmitz M, Kingston RL. </i> Biomol NMR Assign, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03410r002","statement":[{"text":"The phosphoprotein is the non-catalytic subunit of the polymerase, and its C-terminal region enables the polymerase to engage with the nucleocapsid. Here, we report the 1H, 15N, and 13C chemical shift assignments of the C-terminal region (amino acids 267-388) of the Menangle virus phosphoprotein. This region has a bipartite character, with a highly flexible and structurally disordered sequence preceding a structured nucleocapsid-binding domain.","type":"Abstract"},{"text":"Conversely, residues from the flexible linker (amino acids 267–336) are poorly dispersed in the proton dimension, ranging from 8.06 ppm (A318) to 8.61 ppm (S334).","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-12T07:13:12.363Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":267,"end":328,"reference_id":"34578318","reference_source":"pmid","reference_html":"Structural Analysis of the Menangle Virus P Protein Reveals a Soft Boundary between Ordered and Disordered Regions. <i> Webby MN, Herr N, Bulloch EMM, Schmitz M, Keown JR, Goldstone DC, Kingston RL. </i> Viruses, 2021","date":"2022-04-08T12:15:34.369Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"SASBDB","id":"SASDLJ9"}],"region_id":"DP03410r003","statement":[{"text":"the Kratky plot for the isolated linker (L) increases monotonically with the scattering angle, which is characteristic of unfolded proteins","type":"Results"},{"text":"Although the analytic expression describing the scattering of the worm-like chain (Equation 6) involves approximations which are strictly valid only for long chains (L/b > 10), and at low scattering angles (qb < 3) [53,54], the model fits the data very well over the q range 0.015–0.30 Å−1 (Figure 5). The SAXS analysis therefore confirms that the linker has an extended conformation with no significantly populated tertiary structure.","type":"Results"},{"text":"In Menangle virus, the ~62 residue linker is also globally disordered and lacks any tertiary structure. This is readily apparent from model-free analysis of the SAXS data (Figure 4).","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-12T20:09:52.786Z"}},{"start":267,"end":328,"reference_id":"34578318","reference_source":"pmid","reference_html":"Structural Analysis of the Menangle Virus P Protein Reveals a Soft Boundary between Ordered and Disordered Regions. <i> Webby MN, Herr N, Bulloch EMM, Schmitz M, Keown JR, Goldstone DC, Kingston RL. </i> Viruses, 2021","date":"2022-04-08T12:21:34.321Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"SASBDB","id":"SASDLJ9"}],"region_id":"DP03410r004","statement":[{"text":"We investigate the oligomerization state of the MenV P protein in solution, as well as the structural characteristics of the flexible linker that connects the coiled-coil and the C-terminal binding domain.","type":"Introduction"},{"text":"The Kratky plot (Figure 4) for the entire C-terminal region (CC-L-BD) has a bell-shaped appearance, consistent with the major scattering contribution coming from the two structured domains (CC and BD) positioned at either end of the chain. In contrast, the Kratky plot for the isolated linker (L) increases monotonically with the scattering angle, which is characteristic of unfolded proteins [76]. The Kratky plot for L-BD has a hybrid appearance, reflecting its nearly equal partition between structured and unstructured regions. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-12T20:09:51.260Z"}},{"start":267,"end":328,"reference_id":"34578318","reference_source":"pmid","reference_html":"Structural Analysis of the Menangle Virus P Protein Reveals a Soft Boundary between Ordered and Disordered Regions. <i> Webby MN, Herr N, Bulloch EMM, Schmitz M, Keown JR, Goldstone DC, Kingston RL. </i> Viruses, 2021","date":"2025-02-19T13:00:03.812Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"27634"}],"region_id":"DP03410r005","statement":[{"text":"As expected, backbone amide resonances associated with the linker (L) showed very limited chemical shift dispersion in the proton dimension, consistent with global disorder, while those associated with the binding domain (BD) were widely dispersed, consistent with overwhelming population of the folded state [61]. The propensity for structure formation in the linker was assessed using the ncSPC algorithm (Figure S4B), based on the weighted deviation of the chemical shifts of five backbone nuclei (1Hα, 13CO, 13Cα, 13Cβ, 15N) from reference values specific for intrinsically disordered proteins [83].","type":"Methods"}],"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-19T13:32:18.740Z"}}],"regions_counter":5,"released":"2021_12","sequence":"MDNPPSDAEISAWIDKGLDTVEHFLSVATDPARSLGKSTIKPGKTQELIRSAEKLAGAVVQGGEKGDRDNAKKEVTTAAPEPAVRGKVRPIDVEPSDNTYEEVIPSENSKLIPPVTPKKPPRHKDRIMSMMPLQSDKQLTESMESQVFKRGGKDLRHGPSDIGPGAIGGRSQLTGLAGGRESQSGATQYVTQSPSQPSEVAADVETAPASAPYVKEIIHYLQTLETRINNLDWKVDKILSQQSVITQIKHEQHAIKAGIATLEGLITTIKIMDPGVGDGATAAKSKRLFKEAPVVVSGPVIGDNPIVDADTIQLDELARPSLPKTKSQKSSAASPAALSGYKMTLLALIKECIPNQAKRQKFEMQVGGIRNEQDFKNLRREIIRSAAQ","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Paramyxoviridae","Rubulavirinae","Pararubulavirus","Menangle pararubulavirus"],"UniParc":"UPI00000F9E71","uniref100":"UniRef100_Q91MK1","uniref90":"UniRef90_K9MZ21","uniref50":"UniRef50_A0A2U8ZTU4","dataset":["Viral proteins"],"genes":[{"name":{"value":"V/P","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAK62280.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAK62280.1"}}]}}],"disorder_content":0.18041237113402062,"disprot_consensus":{"full":[{"start":267,"end":336,"type":"D"}],"Structural state":[{"start":267,"end":336,"type":"D"}],"Disorder function":[{"start":267,"end":336,"type":"F"}]}},{"disprot_id":"DP03411","acc":"Q61081","creator":"nfarahi","date":"2021-07-09T07:50:04.578Z","features":{"pfam":[{"id":"PF03234","name":"Cdc37 N terminal kinase binding","start":1,"end":109},{"id":"PF08564","name":"Cdc37 C terminal domain","start":293,"end":356},{"id":"PF08565","name":"Cdc37 Hsp90 binding domain","start":168,"end":270}],"gene3D":[]},"length":379,"name":"Hsp90 co-chaperone Cdc37","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":1,"end":144,"reference_id":"31226489","reference_source":"pmid","reference_html":"Structural characterization of the N-terminal kinase-interacting domain of an Hsp90-cochaperone Cdc37 by CD and solution NMR spectroscopy. <i> Ihama F, Yamamoto M, Kojima C, Fujiwara T, Matsuzaki K, Miyata Y, Hoshino M. </i> Biochim Biophys Acta Proteins Proteom, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03411r001","statement":[{"text":"We found that a cloud of peaks was present around the center of the spectrum (~ 8 ppm along the 1H axis). Although a small number of exceptional peaks appeared separately from the others, most overlapped with each other as the result of severe line broadening.","type":"Results"},{"text":"These observations suggest that the N-terminal fragment Cdc37(1–144) did not adopt a single rigid conformation under neutral conditions, but that it was in dynamic equilibrium between several different structures, probably between an α-helical and random coil-like structure.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-09T11:42:11.104Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":144,"reference_id":"31226489","reference_source":"pmid","reference_html":"Structural characterization of the N-terminal kinase-interacting domain of an Hsp90-cochaperone Cdc37 by CD and solution NMR spectroscopy. <i> Ihama F, Yamamoto M, Kojima C, Fujiwara T, Matsuzaki K, Miyata Y, Hoshino M. </i> Biochim Biophys Acta Proteins Proteom, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03411r002","statement":[{"text":"Because the ellipticity value of the CD spectrum is temporally and spatially averaged, its intensity directly depends on the stability or lifetime of α-helical conformations. That is, smaller CD signals could be recorded when the α-helical conformation adopted by each residue was not very stable, but transiently disappeared during measurement of the spectrum. In other words, the secondary and tertiary structures of the protein are not fixed to a single α-helical conformation, but change dynamically between two or more different conformational states.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-09T11:42:12.068Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":144,"reference_id":"31226489","reference_source":"pmid","reference_html":"Structural characterization of the N-terminal kinase-interacting domain of an Hsp90-cochaperone Cdc37 by CD and solution NMR spectroscopy. <i> Ihama F, Yamamoto M, Kojima C, Fujiwara T, Matsuzaki K, Miyata Y, Hoshino M. </i> Biochim Biophys Acta Proteins Proteom, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006206","ec_ontology":"ECO","ec_name":"near-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03411r003","statement":[{"text":"This is partly supported by the near-UV CD spectra. Although the spectra indicate that the protein has a certain degree of tertiary structure (well-ordered packing of sidechain of aromatic amino acids) under the neutral conditions, the signal is very weak.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-09T11:42:13.248Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":11,"end":15,"reference_id":"31226489","reference_source":"pmid","reference_html":"Structural characterization of the N-terminal kinase-interacting domain of an Hsp90-cochaperone Cdc37 by CD and solution NMR spectroscopy. <i> Ihama F, Yamamoto M, Kojima C, Fujiwara T, Matsuzaki K, Miyata Y, Hoshino M. </i> Biochim Biophys Acta Proteins Proteom, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007687","ec_ontology":"ECO","ec_name":"protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03411r004","statement":[{"text":"These physiological functions are considered to depend on phosphorylation at conserved Ser13 by protein kinase CK2α. To assess whether such chemical modification at the sidechain of aminoacids affects the conformational states of Cdc37, we attempted to prepare phosphorylated Cdc37(1–93) by incubating with CK2α. We first examined whether a phosphorylation reaction occurred in this small N-terminal fragment protein using Phos-tag SDS-PAGE, in which Phos-tag acrylamide gel specifically chelates phosphorylated residues in a protein and retards its migration during electrophoresis. The results clearly demonstrated that the smaller fragment Cdc37(1–93) was indeed phosphorylated by CK2α.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-09T11:42:08.976Z"},"ec_go":"IDA","disprot_namespace":"Disorder function"}],"regions_counter":4,"released":"2021_12","sequence":"MVDYSVWDHIEVSDDEDETHPNIDTASLFRWRHQARVERMEQFQKEKEELDRGCRECKRKVAECQRKLKELEVAESDGQVELERLRAEAQQLRKEERSWEQKLEDMRKKEKNMPWNVDTLSKDGFSKSMVNTKPEKAEEDSEEAREQKHKTFVEKYEKQIKHFGMLHRWDDSQKYLSDNVHLVCEETANYLVIWCIDLEVEEKCALMEQVAHQTMVMQFILELAKSLKVDPRACFRQFFTKIKTADHQYMEGFKYELEAFKERVRGRAKLRIEKAMKEYEEEERKKRLGPGGLDPVEVYESLPEELQKCFDVKDVQMLQDAISKMDPTDAKYHMQRCIDSGLWVPNSKSGEAKEGEEAGPGDPLLEAVPKAGNEKDVSA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"UniParc":"UPI0000027D08","uniref100":"UniRef100_Q61081","uniref90":"UniRef90_Q61081","uniref50":"UniRef50_Q61081","genes":[{"name":{"value":"Cdc37"}}],"alphafold_very_low_content":0.0870712401055409,"disorder_content":0.37994722955145116,"disprot_consensus":{"full":[{"start":1,"end":144,"type":"D"}],"Structural state":[{"start":1,"end":144,"type":"D"}],"Disorder function":[{"start":11,"end":15,"type":"F"}]}},{"disprot_id":"DP03412","acc":"P27395","creator":"nfarahi","date":"2021-07-09T11:11:36.059Z","features":{"pfam":[{"id":"PF00869","name":"Flavivirus glycoprotein, central and dimerisation domains","start":297,"end":592},{"id":"PF00948","name":"Flavivirus non-structural Protein NS1","start":797,"end":1146},{"id":"PF00949","name":"Peptidase S7, Flavivirus NS3 serine protease","start":1522,"end":1671},{"id":"PF00972","name":"Flavivirus RNA-directed RNA polymerase, fingers and palm domains","start":2780,"end":3232},{"id":"PF01002","name":"Flavivirus non-structural protein NS2B","start":1379,"end":1504},{"id":"PF01003","name":"Flavivirus capsid protein C","start":6,"end":123},{"id":"PF01004","name":"Flavivirus envelope glycoprotein M","start":221,"end":294},{"id":"PF01005","name":"Flavivirus non-structural protein NS2A","start":1158,"end":1289},{"id":"PF01349","name":"Flavivirus non-structural protein NS4B","start":2273,"end":2518},{"id":"PF01350","name":"Flavivirus non-structural protein NS4A","start":2129,"end":2269},{"id":"PF01570","name":"Flavivirus polyprotein propeptide","start":137,"end":218},{"id":"PF01728","name":"FtsJ-like methyltransferase","start":2582,"end":2750},{"id":"PF02832","name":"Flavivirus glycoprotein, immunoglobulin-like domain","start":595,"end":692},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1689,"end":1835},{"id":"PF20483","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","start":3236,"end":3398},{"id":"PF20907","name":"Flavivirus NS3 helicase, C-terminal helical domain","start":1979,"end":2121},{"id":"PF21659","name":"Flavivirus envelope glycoprotein E, stem/anchor domain","start":695,"end":788}],"gene3D":[]},"length":3432,"name":"Genome polyprotein","ncbi_taxon_id":11073,"organism":"Japanese encephalitis virus (strain SA-14)","regions":[{"start":1,"end":25,"reference_id":"34170495","reference_source":"pmid","reference_html":"NMR backbone resonance assignment of Japanese encephalitis virus capsid protein. <i> Guo Y, Yao C, Cheng K, Wu Q, Xu G, Jiang L, Li C. </i> Biomol NMR Assign, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"cross_refs":[{"db":"BMRB","id":"50839"}],"region_id":"DP03412r001","statement":[{"text":"Prediction of JEVC secondary structure derived on its backbone NMR chemical shifts by TALOS+. The predicted secondary structure elements obtained with TALOS+ are shown as red bars for α-helices.","type":"Figure"},{"text":"In Figure 2 the chemical shift-derived secondary structure elements only start at residue 30.","type":"Curator statement"},{"text":"The peaks belonging to residues 1-25 in the HSQC spectrum show a very narrow dispersion.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T10:02:58.470Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":25,"reference_id":"31284608","reference_source":"pmid","reference_html":"Crystal Structure of the Japanese Encephalitis Virus Capsid Protein. <i> Poonsiri T, Wright GSA, Solomon T, Antonyuk SV. </i> Viruses, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":2,"cross_refs":[{"db":"PDB","id":"5OW2"}],"region_id":"DP03412r003","statement":[{"text":"The first 25 residues at the N-terminus are not visible in the electron density map.","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:20:28.116Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":4,"released":"2023_06","sequence":"MTKKPGGPGKNRAINMLKRGLPRVFPLVGVKRVVMSLLDGRGPVRFVLALITFFKFTALAPTKALLGRWKAVEKSVAMKHLTSFKRELGTLIDAVNKRGRKQNKRGGNEGSIMWLASLAVVIACAGAMKLSNFQGKLLMTINNTDIADVIVIPTSKGENRCWVRAIDVGYMCEDTITYECPKLTMGNDPEDVDCWCDNQEVYVQYGRCTRTRHSKRSRRSVSVQTHGESSLVNKKEAWLDSTKATRYLMKTENWIIRNPGYAFLAAVLGWMLGSNNGQRVVFTILLLLVAPAYSFNCLGMGNRDFIEGASGATWVDLVLEGDSCLTIMANDKPTLDVRMINIEASQLAEVRSYCYHASVTDISTVARCPTTGEAHNEKRADSSYVCKQGFTDRGWGNGCGLFGKGSIDTCAKFSCTSKAIGRTIQPENIKYEVGIFVHGTTTSENHGNYSAQVGASQAAKFTVTPNAPSITLKLGDYGEVTLDCEPRSGLNTEAFYVMTVGSKSFLVHREWFHDLALPWTSPSSTAWRNRELLMEFEGAHATKQSVVALGSQEGGLHQALAGAIVVEYSSSVKLTSGHLKCRLKMDKLALKGTTYGMCTEKFSFAKNPVDTGHGTVVIELSYSGSDGPCKIPIVSVASLNDMTPVGRLVTVNPFVATSSANSKVLVEMEPPFGDSYIVVGRGDKQINHHWHKAGSTLGKAFSTTLKGAQRLAALGDTAWDFGSIGGVFNSIGRAVHQVFGGAFRTLFGGMSWITQGLMGALLLWMGVNARDRSIALAFLATGGVLVFLATNVHADTGCAIDITRKEMRCGSGIFVHNDVEAWVDRYKYLPETPRSLAKIVHKAHKEGVCGVRSVTRLEHQMWEAVRDELNVLLKENAVDLSVVVNKPVGRYRSAPKRLSMTQEKFEMGWKAWGKSILFAPELANSTFVVDGPETKECPDEHRAWNSMQIEDFGFGITSTRVWLKIREESTDECDGAIIGTAVKGHVAVHSDLSYWIESRYNDTWKLERAVFGEVKSCTWPETHTLWGDDVEESELIIPHTIAGPKSKHNRREGYKTQNQGPWDENGIVLDFDYCPGTKVTITEDCSKRGPSVRTTTDSGKLITDWCCRSCSLPPLRFRTENGCWYGMEIRPVMHDETTLVRSQVDAFKGEMVDPFQLGLLVMFLATQEVLRKRWTARLTIPAVLGVLLVLMLGGITYTDLARYVVLVAAAFAEANSGGDVLHLALIAVFKIQPAFLVMNMLSTRWTNQENVILVLGAAFFQLASVDLQIGVHGILNAAAIAWMIVRAITFPTTSSVTMPVLALLTPGMRALYLDTYRIILLVIGICSLLHERKKTMAKKKGAVLLGLALTSTGWFSPTTIAAGLMVCNPNKKRGWPATEFLSAVGLMFAIVGGLAELDIESMSIPFMLAGLMAVSYVVSGKATDMWLERAADISWEMDAAITGSSRRLDVKLDDDGDFHLIDDPGVPWKVWVLRMSCIGLAALTPWAIVPAAFGYWLTLKTTKRGGVFWDTPSPKPCSKGDTTTGVYRIMARGILGTYQAGVGVMYENVFHTLWHTTRGAAIMSGEGKLTPYWGSVREDRIAYGGPWRFDRKWNGTDDVQVIVVEPGKAAVNIQTKPGVFRTPFGEVGAVSLDYPRGTSGSPILDSNGDIIGLYGNGVELGDGSYVSAIVQGDRQEEPVPEAYTPNMLRKRQMTVLDLHPGSGKTRKILPQIIKDAIQQRLRTAVLAPTRVVAAEMAEALRGLPVRYQTSAVQREHQGNEIVDVMCHATLTHRLMSPNRVPNYNLFVMDEAHFTDPASIAARGYIATKVELGEAAAIFMTATPPGTTDPFPDSNAPIHDLQDEIPDRAWSSGYEWITEYAGKTVWFVASVKMGNEIAMCLQRAGKKVIQLNRKSYDTEYPKCKNGDWDFVITTDISEMGANFGASRVIDCRKSVKPTILEEGEGRVILGNPSPITSASAAQRRGRVGRNPNQVGDEYHYGGATSEDDSNLAHWTEAKIMLDNIHMPNGLVAQLYGPEREKAFTMDGEYRLRGEEKKNFLELLRTADLPVWLAYKVASNGIQYTDRKWCFDGPRTNAILEDNTEVEIVTRMGERKILKPRWLDARVYADHQALKWFKDFAAGKRSAVSFIEVLGRMPEHFMGKTREALDTMYLVATAEKGGKAHRMALEELPDALETITLIVAITVMTGGFFLLMMQRKGIGKMGLGALVLTLATFFLWAAEVPGTKIAGTLLIALLLMVVLIPEPEKQRSQTDNQLAVFLICVLTVVGVVAANEYGMLEKTKADLKSMFGGKTQASGLTGLPSMALDLRPATAWALYGGSTVVLTPLLKHLITSEYVTTSLASINSQAGSLFVLPRGVPFTDLDLTVGLVFLGCWGQITLTTFLTAMVLATLHYGYMLPGWQAEALRAAQRRTAAGIMKNAVVDGMVATDVPELERTTPLMQKKVGQVLLIGVSVAAFLVNPNVTTVREAGVLVTAATLTLWDNGASAVWNSTTATGLCHVMRGSYLAGGSIAWTLIKNADKPSLKRGRPGGRTLGEQWKEKLNAMSREEFFKYRREAIIEVDRTEARRARRENNIVGGHPVSRGSAKLRWLVEKGFVSPIGKVIDLGCGRGGWSYYAATLKKVQEVRGYTKGGAGHEEPMLMQSYGWNLVSLKSGVDVFYKPSEPSDTLFCDIGESSPSPEVEEQRTLRVLEMTSDWLHRGPREFCIKVLCPYMPKVIEKMEVLQRRFGGGLVRLPLSRNSNHEMYWVSGAAGNVVHAVNMTSQVLLGRMDRTVWRGPKYEEDVNLGSGTRAVGKGEVHSNQEKIKKRIQKLKEEFATTWHKDPEHPYRTWTYHGSYEVKATGSASSLVNGVVELMSKPWDAIANVTTMAMTDTTPFGQQRVFKEKVDTKAPEPPAGAKEVLNETTNWLWAHLSREKRPRLCTKEEFIKKVNSNAALGAVFAEQNQWSTAREAVDDPRFWEMVDEERENHLRGECHTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARYLEFEALGFLNEDHWLSRENSGGGVEGSGVQKLGYILRDIAGKQGGKMYADDTAGWDTRITRTDLENEAKVLELLDGEHRMLARAIIELTYRHKVVKVMRPAAEGKTVMDVISREDQRGSGQVVTYALNTFTNIAVQLVRLMEAEGVIGPQHLEQLPRKTKIAVRTWLFENGEERVTRMAISGDDCVVKPLDDRFATALHFLNAMSKVRKDIQEWKPSHGWHDWQQVPFCSNHFQEIVMKDGRSIVVPCRGQDELIGRARISPGAGWNVKDTACLAKAYAQMWLLLYFHRRDLRLMANAICSAVPVDWVPTGRTSWSIHSKGEWMTTEDMLQVWNRVWIEENEWMMDKTPITSWTDVPYVGKREDIWCGSLIGTRSRATWAENIYAAINQVRAVIGKENYVDYMTSLRRYEDVLIQEDRVI","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Flavivirus"],"UniParc":"UPI0000131E3F","uniref100":"UniRef100_P27395","uniref90":"UniRef90_P27395","uniref50":"UniRef50_P17763","dataset":["Viral proteins","RNA-binding proteins"],"genes":[],"disorder_content":0.007284382284382284,"disprot_consensus":{"full":[{"start":1,"end":25,"type":"D"}],"Structural state":[{"start":1,"end":25,"type":"D"}]}},{"disprot_id":"DP03413","acc":"P49880","creator":"nfarahi","date":"2021-07-09T12:19:49.542Z","features":{"pfam":[{"id":"PF00104","name":"Ligand-binding domain of nuclear hormone receptor","start":472,"end":656},{"id":"PF00105","name":"Double treble clef zinc finger, C4 type","start":290,"end":357}],"gene3D":[]},"length":776,"name":"Ecdysone receptor","ncbi_taxon_id":7159,"organism":"Aedes aegypti","regions":[{"start":564,"end":776,"reference_id":"30243841","reference_source":"pmid","reference_html":"The intrinsically disordered C-terminal F domain of the ecdysteroid receptor from Aedes aegypti exhibits metal ion-binding ability. <i> Więch A, Rowińska-Żyrek M, Wątły J, Czarnota A, Hołubowicz R, Szewczuk Z, Ożyhar A, Orłowski M. </i> J Steroid Biochem Mol Biol, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03413r001","statement":[{"text":"Our results showed that AaFEcR belongs to a family of intrinsically disordered proteins (IDPs) and possesses putative pre-molten globule (PMG) characteristics.","type":"Abstract"},{"text":"Far-UV circular dichorism (CD) spectroscopy was used to determine the secondary structure content in AaFEcR. Typical for IDPs features were observed for the native spectrum (Fig. 3A), such as: the presence of a minimum at ∼200 nm and the lack of a distinct minima at 208 nm and 222 nm [45]. ","type":"Results"},{"text":"The results obtained for AaFEcR, compared with data for coil-like and PMG-like IDPs, placed AaFEcR among PMG-like IDPs (Fig. 3D).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:09:25.263Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":564,"end":776,"reference_id":"30243841","reference_source":"pmid","reference_html":"The intrinsically disordered C-terminal F domain of the ecdysteroid receptor from Aedes aegypti exhibits metal ion-binding ability. <i> Więch A, Rowińska-Żyrek M, Wątły J, Czarnota A, Hołubowicz R, Szewczuk Z, Ożyhar A, Orłowski M. </i> J Steroid Biochem Mol Biol, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03413r002","statement":[{"text":"Our results showed that AaFEcR belongs to a family of intrinsically disordered proteins (IDPs) and possesses putative pre-molten globule (PMG) characteristics.","type":"Abstract"},{"text":"Sedimentation velocity analytical ultracentrifugation (SV-AUC) and a series of size exclusion chromatography (SEC) were conducted in order to determine hydrodynamic properties of AaFEcR. The value of the Stokes radius (RS) for the native AaFEcR is 2.67 nm ± 0.1 nm (Figs. 4A and 5 ). Using equations derived from [46], theoretical values of RS for AaFEcR considered as a native globular protein, a natively unfolded (NU) coil and a NU-PMG were calculated, plotted together with the value obtained experimentally and presented in Fig. 5. The most similar to determined by SEC RS value was the one calculated for NU-PMG, what confirms the results obtained from CD spectroscopy analysis (Fig. 3D).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:09:23.983Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":564,"end":776,"reference_id":"30243841","reference_source":"pmid","reference_html":"The intrinsically disordered C-terminal F domain of the ecdysteroid receptor from Aedes aegypti exhibits metal ion-binding ability. <i> Więch A, Rowińska-Żyrek M, Wątły J, Czarnota A, Hołubowicz R, Szewczuk Z, Ożyhar A, Orłowski M. </i> J Steroid Biochem Mol Biol, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03413r003","statement":[{"text":"Our results showed that AaFEcR belongs to a family of intrinsically disordered proteins (IDPs) and possesses putative pre-molten globule (PMG) characteristics.","type":"Abstract"},{"text":"Sedimentation velocity analytical ultracentrifugation (SV-AUC) and a series of size exclusion chromatography (SEC) were conducted in order to determine hydrodynamic properties of AaFEcR.","type":"Results"},{"text":"The sedimentation coefficient distributions (Fig. 4C) calculated from the SV-AUC data indicate that one major species with a sedimentation coefficient of approximately 1.2 S and a hydrodynamic radius (Rh) slightly greater than 2.9 nm is present in all samples of AaFEcR at different concentrations ranging from 0.15 mg/ml to 1.0 mg/ml range (Table 1).","type":"Results"},{"text":"The frictional ratio (f/f0) of 1.9–2.0, higher than the approximate value of 1.3 expected for a typical globular protein such as bovine serum albumin (BSA), indicates that the protein has an extended conformation. The relation between the frictional ratio and the molecular weight of a protein is an indicative of protein disorder [48].","type":"Results"},{"text":"Fitting the apparent molecular weight (MWapp) of AaFEcR calculated using the SV\ndata for all three tested concentrations indicated existence of AaFEcR as a monomer.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:09:22.809Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":564,"end":776,"reference_id":"30243841","reference_source":"pmid","reference_html":"The intrinsically disordered C-terminal F domain of the ecdysteroid receptor from Aedes aegypti exhibits metal ion-binding ability. <i> Więch A, Rowińska-Żyrek M, Wątły J, Czarnota A, Hołubowicz R, Szewczuk Z, Ożyhar A, Orłowski M. </i> J Steroid Biochem Mol Biol, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03413r004","statement":[{"text":"Using SEC, SV-AUC and ESI-TOF MS, we showed that the intrinsically disordered AaFEcR is able to bind metal ions and form complexes with these ions. ","type":"Abstract"},{"text":"Injected samples were prepared to determine the specific molar ratio between metal ions and AaFEcR (nM2+/nAaFEcR). For all samples with nM2+/nAaFEcR equal to 0.05, the AaFEcR RS slightly increased. A difference in the ion-AaFEcR interaction was observed for samples with higher metal ion/protein ratios. For the samples of AaFEcR containing Ca2+ (up to a 2.5-fold excess) the overall range of observed changes in the RS values was much smaller than in the presence of Zn2+ or Cu2+.","type":"Results"},{"text":"To investigate in detail whether AaFEcR is capable of binding Zn2+ and Cu2+, we conducted appropriate experiments using CD, SEC and MS techniques. The results clearly showed that recombinant AaFEcR is able to form complexes with Zn2+ and Cu2+, but the interactions result in the protein shrinking rather than structuring.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:09:28.297Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":564,"end":776,"reference_id":"30243841","reference_source":"pmid","reference_html":"The intrinsically disordered C-terminal F domain of the ecdysteroid receptor from Aedes aegypti exhibits metal ion-binding ability. <i> Więch A, Rowińska-Żyrek M, Wątły J, Czarnota A, Hołubowicz R, Szewczuk Z, Ożyhar A, Orłowski M. </i> J Steroid Biochem Mol Biol, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03413r005","statement":[{"text":"Using SEC, SV-AUC and ESI-TOF MS, we showed that the intrinsically disordered AaFEcR is able to bind metal ions and form complexes with these ions. ","type":"Abstract"},{"text":"The effect of the presence of metal ions on the possible secondary structure formation in AaFEcR was examined with CD spectroscopy. The obtained CD spectra for samples containing AaFEcR with the appropriate metal ion concentration (data not shown) did not indicate significant secondary structure formation. ","type":"Results"},{"text":"To investigate in detail whether AaFEcR is capable of binding Zn2+ and Cu2+, we conducted appropriate experiments using CD, SEC and MS techniques. The results clearly showed that recombinant AaFEcR is able to form complexes with Zn2+ and Cu2+, but the interactions result in the protein shrinking rather than structuring.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:09:27.334Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":564,"end":776,"reference_id":"30243841","reference_source":"pmid","reference_html":"The intrinsically disordered C-terminal F domain of the ecdysteroid receptor from Aedes aegypti exhibits metal ion-binding ability. <i> Więch A, Rowińska-Żyrek M, Wątły J, Czarnota A, Hołubowicz R, Szewczuk Z, Ożyhar A, Orłowski M. </i> J Steroid Biochem Mol Biol, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03413r006","statement":[{"text":"Using SEC, SV-AUC and ESI-TOF MS, we showed that the intrinsically disordered AaFEcR is able to bind metal ions and form complexes with these ions.","type":"Abstract"},{"text":"The mass spectrometric observations are in excellent agreement with the dependencies\nobserved in Fig. 4D, which shows that the RS of the protein decreased upon the addition of Zn2+ and Cu2+, while no pronounced changes were observed in the presence of Ca2+. MS shows that AaFEcR is able to bind two Zn2+ and Cu2+ ions and only one Ca2+ ion when the metal-to-ligand ratio = 2:1.","type":"Results"},{"text":"To investigate in detail whether AaFEcR is capable of binding Zn2+ and Cu2+, we conducted appropriate experiments using CD, SEC and MS techniques. The results clearly showed that recombinant AaFEcR is able to form complexes with Zn2+ and Cu2+, but the interactions result in the protein shrinking rather than structuring.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:09:25.974Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":9,"released":"2023_12","sequence":"MYRLNIVSTNPSGSVQQQQQAQGQQVISSVVRPQQQQPPPQLALVQTGGSGGTTTTIIGLTSLNALNATTITGLVAGAAGSSTSAIAAAGASNSGSGPSTATTKHILKAATTNNNISIVKIVDDIMLKAVKVEPLPMDTGGGGGGVSMIPSSATTSGGVTVTAIPASVAPMPPVAAGTNVSSNGSVTVYASGKRRLESNEEWISSPSPGSVPGSAPPLSPSPGSQSTTYTTTMSNGYSSPMSTGSYDPYSPNGKMGREDLSPSSSLNGYTDGSDAKKQKKGPTPRQQEELCLVCGDRESGYHYNALTCEGCKGFFRRSVTKNAVYCCKFGHACEMDMYMRRKCQECRLKKCLAVGMRPECVVPENQCAIKRKEKKAQKEKDKVQTNATVSTTNSTYRSEILPILMKCDPPPHQAIPLLPEKLLQENRLRNIPLLTANQMAVIYKLIWYQDGYEQPSEEDLKRIMIGSPNEEEDQHDVHFRHITEITILTVQLIVEFAKGLPAFTKIPQEDQITLLKACSSEVMMLRMARRYDAATDSILFANNRSYTRDSYRMAGMADTIEDLLHFCRQMFSLTVDNVEYALLTAIVIFSDRPGLEQAELVEHIQSYYIDTLRIYILNRHAGDPKCSVIFAKLLSILTELRTLGNQNSEMCFSLKLKNRKLPRFLEEIWDVQDIPPSMQAQMHSHGTQSSSSSSSSSSSSSNGSSNGNSSSNSNSSQHGPHPHPHGQQLTPNQQQHQQQHSQLQQVHANGSGSGGGSNNNSSSGGVVPGLGMLDQV","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Nematocera","Culicoidea","Culicidae","Culicinae","Aedini","Aedes","Stegomyia"],"UniParc":"UPI0000129BA0","uniref100":"UniRef100_P49880","uniref90":"UniRef90_P49880","uniref50":"UniRef50_P49880","genes":[{"name":{"value":"EcR"},"synonyms":[{"value":"NR1H1"}],"orfNames":[{"value":"AAEL009600"}]}],"alphafold_very_low_content":0.4884020618556701,"dataset":["Condensates-related proteins"],"disorder_content":0.27448453608247425,"disprot_consensus":{"full":[{"start":564,"end":776,"type":"D"}],"Structural state":[{"start":564,"end":776,"type":"D"}],"Molecular function":[{"start":564,"end":776,"type":"F"}]}},{"disprot_id":"DP03414","acc":"P40949","creator":"nfarahi","date":"2021-07-09T12:52:28.761Z","features":{"pfam":[{"id":"PF29750","name":"TasA anchoring/assembly domain","start":78,"end":185}],"gene3D":[]},"length":253,"name":"TasA anchoring/assembly protein","ncbi_taxon_id":224308,"organism":"Bacillus subtilis (strain 168)","regions":[{"start":33,"end":253,"reference_id":"30371005","reference_source":"pmid","reference_html":"The Bacterial Extracellular Matrix Protein TapA Is a Two-Domain Partially Disordered Protein. <i> Abbasi R, Mousa R, Dekel N, Amartely H, Danieli T, Lebendiker M, Levi-Kalisman Y, Shalev DE, Metanis N, Chai L. </i> Chembiochem, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03414r001","statement":[{"text":"We used circular dichroism and NMR spectroscopy to show that, unlike the structured TasA, TapA is disordered. In addition, TapA is composed of two weakly interacting domains: a disordered C-terminal domain and a more structured N-terminal domain.","type":"Abstract"},{"text":"The CD spectrum of a recombinant TapA (expressed in\nE. coli, see the Supporting Information for more details)\nshowed that TapA was partially disordered, according to the\nminimum at about 200 nm that was typical for disordered proteins (Figure 1 B).","type":"Article"},{"text":"The secondary structures of the polypeptides were then\ndetermined by means of CD spectroscopy. The CD spectra of\nFL TapA and the CTD and NTD fragments (Figure 2 B) show\nthat, similarly to the FL protein, the CTD and NTD were disordered, but to different extents.","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:29:40.482Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":33,"end":253,"reference_id":"30371005","reference_source":"pmid","reference_html":"The Bacterial Extracellular Matrix Protein TapA Is a Two-Domain Partially Disordered Protein. <i> Abbasi R, Mousa R, Dekel N, Amartely H, Danieli T, Lebendiker M, Levi-Kalisman Y, Shalev DE, Metanis N, Chai L. </i> Chembiochem, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03414r002","statement":[{"text":"The earlier elution of TapA in SEC, relative to a globular protein with the same mass, is expected for disordered proteins due to their extended hydrodynamic radius.","type":"Article"},{"text":"CD analysis, together with the analytical SEC and SEC-MALS results, indicated that TapA was a partially disordered monomer.","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:29:38.849Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":33,"end":253,"reference_id":"30371005","reference_source":"pmid","reference_html":"The Bacterial Extracellular Matrix Protein TapA Is a Two-Domain Partially Disordered Protein. <i> Abbasi R, Mousa R, Dekel N, Amartely H, Danieli T, Lebendiker M, Levi-Kalisman Y, Shalev DE, Metanis N, Chai L. </i> Chembiochem, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006317","ec_ontology":"ECO","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03414r003","statement":[{"text":"Thermal stability was determined for partially disordered FL\nTapA and its CTD and NTD. Figure 3 A–C shows the CD spectra\nof the FL, NTD, and CTD, respectively, upon gradual temperature increase. These plots surprisingly showed that TapA and its two domains were not melted with increasing temperature, but rather that they gained some a-helical structure (see Table S2 and Figure S5 for secondary-structure analysis). This thermodynamic signature is often an indication that folding under heating is entropically driven, and can be explained by the release of water molecules upon partial folding events.","type":"Article"},{"text":"In contrast to the semi-sigmoidal curve measured for the FL protein and the NTD fragment, the CTD melting curve decreased monotonically, which suggested that despite the clear existence of two states, the denatured-to-folded process was not cooperative.[27] Similar melting behavior has been previously observed for a variety of disordered proteins.","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:29:37.839Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":191,"end":253,"reference_id":"30371005","reference_source":"pmid","reference_html":"The Bacterial Extracellular Matrix Protein TapA Is a Two-Domain Partially Disordered Protein. <i> Abbasi R, Mousa R, Dekel N, Amartely H, Danieli T, Lebendiker M, Levi-Kalisman Y, Shalev DE, Metanis N, Chai L. </i> Chembiochem, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03414r004","statement":[{"text":"We used circular dichroism and NMR spectroscopy to show that, unlike the structured TasA, TapA is disordered. In addition, TapA is composed of two weakly interacting domains: a disordered C-terminal domain and a more structured N-terminal domain. ","type":"Abstract"},{"text":"The structure of TapA, studied herein by using circular dichroism (CD) and solution NMR spectroscopy, showed that it was partially disordered and composed of two domains: a 63- residue C-terminal domain (CTD) and a 158-residue N-terminal domain (NTD).","type":"Article"},{"text":"The 1H,15N HSQC NMR spectrum of the 15N-enriched CTD fragment (Figure 5, left-hand\nside, and the full spectrum in Figure S9) was typical for disordered proteins,[29] as indicated by the narrow chemical shift\ndispersion (Dd1H =0.56 ppm), and in agreement with the CD\nspectrum of the fragment (showing &70% disorder, excluding\nturns).\n","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:29:37.140Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":4,"released":"2021_12","sequence":"MFRLFHNQQKAKTKLKVLLIFQLSVIFSLTAAICLQFSDDTSAAFHDIETFDVSLQTCKDFQHTDKNCHYDKRWDQSDLHISDQTDTKGTVCSPFALFAVLENTGEKLKKSKWKWELHKLENARKPLKDGNVIEKGFVSNQIGDSLYKIETKKKMKPGIYAFKVYKPAGYPANGSTFEWSEPMRLAKCDEKPTVPKKETKSDVKKENETTQKDIPEKTMKEETSQEAVTKEKETQSDQKESGEEDEKSNEADQ","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Bacillus"],"UniParc":"UPI000016E7FC","uniref100":"UniRef100_P40949","uniref90":"UniRef90_P40949","uniref50":"UniRef50_P40949","genes":[{"name":{"value":"tapA","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"21477127","url":"http://www.ncbi.nlm.nih.gov/pubmed/21477127","alternativeUrl":"https://europepmc.org/abstract/MED/21477127"}}]},"synonyms":[{"value":"yqhD"},{"value":"yqxM"}],"olnNames":[{"value":"BSU24640"}]}],"alphafold_very_low_content":0.233201581027668,"disorder_content":0.8735177865612648,"disprot_consensus":{"full":[{"start":33,"end":253,"type":"D"}],"Structural state":[{"start":33,"end":253,"type":"D"}]}},{"disprot_id":"DP03415","acc":"A0A0M4HM24","creator":"nfarahi","date":"2021-07-09T14:21:00.903Z","features":{"pfam":[{"id":"PF27970","name":"LEA protein 1/2/D7/Stress-induced protein KIN2","start":125,"end":187}],"gene3D":[]},"length":212,"name":"LEA3","ncbi_taxon_id":4567,"organism":"Triticum turgidum subsp. durum","regions":[{"start":1,"end":212,"reference_id":"30842512","reference_source":"pmid","reference_html":"Structural properties and enzyme stabilization function of the intrinsically disordered LEA_4 protein TdLEA3 from wheat. <i> Koubaa S, Bremer A, Hincha DK, Brini F. </i> Sci Rep, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03415r001","statement":[{"text":"The purity of the protein was assessed by SDS-PAGE and western blotting (Fig. 1a). The protein migrated at a position in the gel corresponding to a higher molecular mass (35 kDa) than calculated from the amino acid sequence (21.9 kDa; Table 1), which has been frequently observed for LEA proteins34.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:29:56.096Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":1,"end":212,"reference_id":"30842512","reference_source":"pmid","reference_html":"Structural properties and enzyme stabilization function of the intrinsically disordered LEA_4 protein TdLEA3 from wheat. <i> Koubaa S, Bremer A, Hincha DK, Brini F. </i> Sci Rep, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03415r002","statement":[{"text":"The far UV-CD spectrum of TdLEA3 under fully hydrated conditions showed a negative ellipticity around 200 nm, indicating a largely unstructured conformation, typical for IDPs (Fig. 2a).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:29:54.617Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":212,"reference_id":"30842512","reference_source":"pmid","reference_html":"Structural properties and enzyme stabilization function of the intrinsically disordered LEA_4 protein TdLEA3 from wheat. <i> Koubaa S, Bremer A, Hincha DK, Brini F. </i> Sci Rep, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03415r003","statement":[{"text":"The Amide I peak of the hydrated protein was centered at 1648 cm−1, indicating a mainly unstructured protein.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:29:53.896Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":212,"reference_id":"30842512","reference_source":"pmid","reference_html":"Structural properties and enzyme stabilization function of the intrinsically disordered LEA_4 protein TdLEA3 from wheat. <i> Koubaa S, Bremer A, Hincha DK, Brini F. </i> Sci Rep, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03415r004","statement":[{"text":"The Amide I peak of the hydrated protein was centered at 1648 cm−1, indicating a mainly unstructured protein. Upon drying, this maximum was shifted to 1657 cm−1 (Fig. 3), indicating a gain in α-helix conformation during drying, in agreement with the CD spectra. ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:29:58.420Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":1,"end":212,"reference_id":"30842512","reference_source":"pmid","reference_html":"Structural properties and enzyme stabilization function of the intrinsically disordered LEA_4 protein TdLEA3 from wheat. <i> Koubaa S, Bremer A, Hincha DK, Brini F. </i> Sci Rep, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03415r005","statement":[{"text":"The far UV-CD spectrum of TdLEA3 under fully hydrated conditions showed a negative ellipticity around 200 nm, indicating a largely unstructured conformation, typical for IDPs (Fig. 2a). However, after drying, the spectrum changed drastically and showed two minima at 208 and 222 nm, typical of a mainly α-helical conformation. A similar spectrum was also obtained in the presence a chemical inducer of α-helicity, trifluoroethanol (TFE).","type":"Results"},{"text":"Many LEA proteins are dehydrins, so drying is physiologically relevant in their case, so the transition can be annotated.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:29:57.549Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":1,"end":212,"reference_id":"30842512","reference_source":"pmid","reference_html":"Structural properties and enzyme stabilization function of the intrinsically disordered LEA_4 protein TdLEA3 from wheat. <i> Koubaa S, Bremer A, Hincha DK, Brini F. </i> Sci Rep, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0044183","term_name":"protein folding chaperone","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03415r006","statement":[{"text":"Therefore, we tested the ability of TdLEA3 to prevent the loss of LDH activity after heating, dehydration and freezing. We compared the effects of TdLEA3 with the effects of BSA as an example of a non-specific protectant and with LDH treated in buffer without additional protein. Under all stress conditions and at all concentrations, TdLEA3 provided a higher degree of protection for LDH than BSA, indicating that the LEA protein had a protective activity that went beyond the unspecific effects of having a second protein present (Fig. 6). After heating at 48 °C for 10 min, LDH had lost about half of its activity in buffer and activity was further reduced with longer incubation times, to about 20% after 30 min. In contrast, the enzyme activity was completely preserved after 10 or 20 min of heat treatment in the presence of TdLEA3 at mass ratios (LDH: TdLEA3) of 1:20 and 1:40. At the highest mass ratio TdLEA3 preserved more than 90% of the enzyme activity after 30 min at 48 °C.","type":"Results"},{"text":" TdLEA3 did not only protect LDH from loss of catalytic activity, but also prevented enzyme aggregation. Such a reduction of enzyme aggregation, in particular during drying, has been observed for other LEA_4 proteins before and has been explained on the basis of the “molecular shield” hypothesis.","type":"Discussion"},{"text":"Quite strikingly, TdLEA3 protected LDH not only during drying and freezing, activities that have been reported frequently for LEA proteins in the literature, but also under heat stress. To the best of our knowledge, such a chaperone activity has previously only been reported for two dehydrins from Arabidopsis34, while a LEA_4 protein from an anhydrobiotic nematode was not able to stabilize enzymes during heating","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:30:02.318Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":212,"reference_id":"30842512","reference_source":"pmid","reference_html":"Structural properties and enzyme stabilization function of the intrinsically disordered LEA_4 protein TdLEA3 from wheat. <i> Koubaa S, Bremer A, Hincha DK, Brini F. </i> Sci Rep, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0044183","term_name":"protein folding chaperone","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006307","ec_ontology":"ECO","ec_name":"turbidity measurement evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03415r007","statement":[{"text":"We therefore investigated the ability of TdLEA3 to reduce LDH aggregation during stress treatments by measuring apparent light scattering of protein solutions as absorbance. We used two mass ratios of enzyme: protein (1:1 and 1:2). After heating for 20 min at 80 °C, LDH showed massive aggregation. The presence of TdLEA3 reduced the aggregation of LDH at both investigated mass ratios to a larger extent than BSA (Fig. 7a).","type":"Results"},{"text":"TdLEA3 did not only protect LDH from loss of catalytic activity, but also prevented enzyme aggregation. Such a reduction of enzyme aggregation, in particular during drying, has been observed for other LEA_4 proteins before and has been explained on the basis of the “molecular shield” hypothesis.","type":"Discussion"},{"text":"Quite strikingly, TdLEA3 protected LDH not only during drying and freezing, activities that have been reported frequently for LEA proteins in the literature, but also under heat stress. To the best of our knowledge, such a chaperone activity has previously only been reported for two dehydrins from Arabidopsis34, while a LEA_4 protein from an anhydrobiotic nematode was not able to stabilize enzymes during heating.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:30:00.912Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":7,"released":"2023_12","sequence":"MASNQNQASYHAGETKARTEEKTGQVMGATKDKAGQTTEATKQKAGQTTEATKQKAGETAEATKQKAGQATEATKQKAGETAEATKQKAAEAKDKTAQTAQAAKERAAETKDQTGSYLGEKTEMAKQKAAETTEAAKQKASETAQYTKESAVAGKDKTGSVLQQAGETVVNAVVGAKDAVANTLGMGGDNATKDTTTGATTKDTTTTTTRNH","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","BOP clade","Pooideae","Triticodae","Triticeae","Triticinae","Triticum"],"UniParc":"UPI00016EFB2B","uniref100":"UniRef100_A0A3B5Z3R9","uniref90":"UniRef90_Q8GV47","uniref50":"UniRef50_Q03968","genes":[],"alphafold_very_low_content":0.8962264150943396,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":212,"type":"T"}],"Structural state":[{"start":1,"end":212,"type":"D"}],"Structural transition":[{"start":1,"end":212,"type":"T"}],"Molecular function":[{"start":1,"end":212,"type":"F"}]}},{"disprot_id":"DP03416","acc":"Q87GF9","creator":"nfarahi","date":"2021-07-09T16:41:52.705Z","features":{"pfam":[],"gene3D":[]},"length":1622,"name":"Uncharacterized protein","ncbi_taxon_id":223926,"organism":"Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)","regions":[{"start":361,"end":428,"reference_id":"26039684","reference_source":"pmid","reference_html":"A repeat unit of Vibrio diarrheal T3S effector subverts cytoskeletal actin homeostasis via binding to interstrand region of actin filaments. <i> Nishimura M, Fujii T, Hiyoshi H, Makino F, Inoue H, Motooka D, Kodama T, Ohkubo T, Kobayashi Y, Nakamura S, Namba K, Iida T. </i> Sci Rep, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03416r001","statement":[{"text":"The circular dichroism spectrum of VopVrep1 was clearly indicative of a random coil pattern, demonstrating that the recombinant VopVrep1 did not form a stable fold in solution.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-12T11:58:03.575Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":361,"end":428,"reference_id":"26039684","reference_source":"pmid","reference_html":"A repeat unit of Vibrio diarrheal T3S effector subverts cytoskeletal actin homeostasis via binding to interstrand region of actin filaments. <i> Nishimura M, Fujii T, Hiyoshi H, Makino F, Inoue H, Motooka D, Kodama T, Ohkubo T, Kobayashi Y, Nakamura S, Namba K, Iida T. </i> Sci Rep, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03416r002","statement":[{"text":"To assess whether the recombinant protein bound to actin, the binding affinity of VopVrep1 to cytoskeletal actin was determined using isothermal titration calorimetry (ITC). Without a stable fold in solution, VopVrep1 bound to actin with high affinity (Kd = 54.4 nM) at a binding stoichiometry of N = 1.06, which is comparable to the well-known F-actin-binding toxin phalloidin17,18, which has a binding affinity of Kd = 36.5 nM and a binding stoichiometry of N = 1.16 in our experiment (Fig. 1(c,d) and Supplementary Table S1).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:28:40.448Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":361,"end":428,"reference_id":"26039684","reference_source":"pmid","reference_html":"A repeat unit of Vibrio diarrheal T3S effector subverts cytoskeletal actin homeostasis via binding to interstrand region of actin filaments. <i> Nishimura M, Fujii T, Hiyoshi H, Makino F, Inoue H, Motooka D, Kodama T, Ohkubo T, Kobayashi Y, Nakamura S, Namba K, Iida T. </i> Sci Rep, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03416r003","statement":[{"text":"Recent advances in the cryoEM method applied to F-actin25 have enabled the direct visualization of the human cytoskeletal actin/VopVrep1 complex at 9.6-Å resolution (Fig. 2(a)).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:28:34.429Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":361,"end":428,"reference_id":"26039684","reference_source":"pmid","reference_html":"A repeat unit of Vibrio diarrheal T3S effector subverts cytoskeletal actin homeostasis via binding to interstrand region of actin filaments. <i> Nishimura M, Fujii T, Hiyoshi H, Makino F, Inoue H, Motooka D, Kodama T, Ohkubo T, Kobayashi Y, Nakamura S, Namba K, Iida T. </i> Sci Rep, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03416r004","statement":[{"text":"In the density map, VopVrep1 occupied a key position surrounded by three actin monomers that reinforced both the lateral and longitudinal interactions within the filament, suggesting the ability of VopVrep1 to stabilize F-actin. In addition to the observed binding mode, the specific, high-affinity recognition of F-actin results in F-actin stabilization19.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:28:42.332Z"},"ec_go":"IDA","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":361,"end":428,"reference_id":"26039684","reference_source":"pmid","reference_html":"A repeat unit of Vibrio diarrheal T3S effector subverts cytoskeletal actin homeostasis via binding to interstrand region of actin filaments. <i> Nishimura M, Fujii T, Hiyoshi H, Makino F, Inoue H, Motooka D, Kodama T, Ohkubo T, Kobayashi Y, Nakamura S, Namba K, Iida T. </i> Sci Rep, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000353","ec_ontology":"ECO","ec_name":"physical interaction evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03416r005","statement":[{"text":"As expected, the F-actin-stabilizing activity of VopVrep1 was demonstrated by the observation that VopVrep1 strongly protected the actin filament from depolymerization in low-salt conditions (Fig. 3) to the same extent as phalloidin.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:28:41.564Z"},"ec_go":"IPI","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":5,"released":"2023_12","sequence":"MAYNISLNNITTTTAPVQQELSGISLQTSASALPRVDIQPNVNEHQLPQALSPSDSCLENEESSSQQPEVKKEQAEKKKKVHKKSNKYSNHTKAKGHLAAIAGATTLGAVLAPFTGGLSLLPTAFVVLFGNASALAMYGGSEFVLGQKGPNNQIDDKKDPEANKQPEENKQPEISVPVSPRPIRAQEFRGLDEVNGRREPEPEEKGSRGKGDTFNYSPVFNFNFGDLNFNQFNTQNNTQFNTQNNTDKTNQADTDSSPTLIEQTIEKFGGNPVINVEEITKDVLIRELREQEPLIGPESKVDEMIDALVSFHEQTNEAKLIQVSFESGHKAYIGGIPDTDEQKQTDPIKAEVCVEKAKKQWPEVKPAHRLITTSGNAKIDGNPGYRNARVDVDGQTVGYTRNERGGSQPQSSGVHTLQGSQQPSVEPSPVDPGHGASGAASAQPGGEAKGAQTPSLHTQGEPISTATQTGGAQGTQGGEDDGRPQVAQGHNPQGEPASLAKAGTPVDPGHGASDVASAQPGGEAKGTETPSLQTEGESISTSMPTGEEQGVQTGGVKKWPEVAAPQRVITSAGNAKIDGNPGYRNARVDVDGQTVGYTRNERGGSQPQSSGVHTLQGSQQPSVEPSPVDPGHGASGAASAQPGGEAKGAQTPSLHTQGEPISTSMPTGEEQGVQTGGVKKWPEVAAPQRVITSAGNAKIDGNPGYRNARVDVDGQTVGYTRNERSGSQPQSSGVHTLQGSQQPSVEPSPVDPGHGASGAASAQPGGEAKGAQTPGLHTQGEPISTATQTGGAQGTQGGEDDGRPQVAQGHNPQGEPASLAKAGTPVDPGHGASDVASAQPGGEAKGTQTPSLQTEGESISTSMPTGEEQGVQTGGVKKWPEVAAPQRVITSAGNAKIDGNPGYRNARVDVDGQTVGYTRNERGGSQPQSSGVHTSQGSQQPGVEPSPVDPGHGASGAASVQPGGEAKGAQTPSLHTQGEPISTATQTGEAQGTQGGEDDGRPQVAQGHNPQGEPASLAKAGTPVDPGHGASGAASAQPGGEAKGAQTPSLHTQGEPISTATQTGGAQGTQGGEDDGRPQVAQGHNPQGEPASLAKAGTPVDPGHGASDVASAQPGGEAKGAQTPSLHTQGEPISTATQTGGAQGTQGGEDDGRPQVAQGHNPQGEPASLAKAGTPVDPGHGASGAASAQPGGEAKGAQTPGLHTQGEPISTATQTGGAQGTQGGEDDGRPQVAQGHNPQGEPASLAKAGTPVDPGHGASDVASAQPGGEAKGTQTPSLQTEGESISTSMPTGEEQGVQTGGVKKWPEVAAPQRVITSAGNAKIDGNPGYRNARVDVDGQTVGYTRNERGGSQPQSSGVHTSQGSQQPGVEPSPVDPGHGASGAASVQPGGEAKGAQTPSLHTQGEPISTATQTGGAQNIQSVTLARADLQQTNVERGRITDVTKLVDVQALASTVAANKSEPERFVSKLHITLKGNSSADSKVGTNQPESLQAWSSNMLSHGPGVKLAQKSLVQNEIELMPQANNGETVKKIEVVSNISGKKWTVSMPAPVLTTQGMASGRGKNYTQGLFHNIRDINQTKRNIELNSTLMESTPKSDVSFVNMGDKVIPIKPAIISNLKLVS","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Vibrionales","Vibrionaceae","Vibrio"],"UniParc":"UPI000000A8D4","uniref100":"UniRef100_Q87GF9","uniref90":"UniRef90_Q87GF9","uniref50":"UniRef50_A0A481SI72","genes":[{"olnNames":[{"value":"VPA1357","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAC62700.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAC62700.1"}}]}]}],"disorder_content":0.04192355117139334,"disprot_consensus":{"full":[{"start":361,"end":428,"type":"D"}],"Structural state":[{"start":361,"end":428,"type":"D"}],"Molecular function":[{"start":361,"end":428,"type":"F"}]}},{"disprot_id":"DP03417","acc":"P10997","creator":"nfarahi","date":"2021-07-09T18:17:47.942Z","features":{"pfam":[{"id":"PF00214","name":"Calcitonin / CGRP / IAPP family","start":27,"end":73}],"gene3D":[]},"length":89,"name":"Islet amyloid polypeptide","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":23,"end":33,"reference_id":"32077246","reference_source":"pmid","reference_html":"Pro-islet amyloid polypeptide in micelles contains a helical prohormone segment. <i> DeLisle CF, Malooley AL, Banerjee I, Banerjee I, Lorieau JL. </i> FEBS J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03417r001","statement":[{"text":"We show that the solution NMR ensemble structure of the protein exchanges between multiple conformers, containing an unfolded Npro segment (residues 1–11) and a mostly helical IAPP region (residues 12–48).","type":"Introduction"},{"text":"There is a 22 residues long signal peptide in the UniProt sequence, therefore residue 1 of the propeptide corrsponds to residue 23 of the UniProt sequence.","type":"Curator statement"},{"text":"The N‐terminal propeptide segment (T1‐R11) is unfolded in DPC micelles, with average S2 values below 0.4.","type":"Results"}],"cross_refs":[{"db":"BMRB","id":"50007"},{"db":"PDB","id":"6UCK"},{"db":"PDB","id":"6UCJ"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T10:41:19.540Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":62,"end":71,"reference_id":"32077246","reference_source":"pmid","reference_html":"Pro-islet amyloid polypeptide in micelles contains a helical prohormone segment. <i> DeLisle CF, Malooley AL, Banerjee I, Banerjee I, Lorieau JL. </i> FEBS J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"BMRB","id":"50007"},{"db":"PDB","id":"6UCJ"},{"db":"PDB","id":"6UCK"}],"region_id":"DP03417r002","statement":[{"text":"There is a 22 residues long signal peptide in the UniProt sequence, therefore residue 1 of the propeptide corrsponds to residue 23 of the UniProt sequence.","type":"Curator statement"},{"text":"A disordered loop from S40‐G49 connects the C terminus of immature IAPP with the C‐terminal propeptide segment of N52‐L67, which appears fairly rigid.","type":"Results"},{"text":"The unstructured loop (S40‐K50) that tethers IAPP to Cpro is highly accessible to solvent.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T10:41:18.177Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":23,"end":89,"reference_id":"32077246","reference_source":"pmid","reference_html":"Pro-islet amyloid polypeptide in micelles contains a helical prohormone segment. <i> DeLisle CF, Malooley AL, Banerjee I, Banerjee I, Lorieau JL. </i> FEBS J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03417r003","statement":[{"text":"In the absence of lipid, unfolded features dominate the CD spectra for proIAPP, and the protein is intrinsically disordered.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T10:41:16.891Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":23,"end":89,"reference_id":"32077246","reference_source":"pmid","reference_html":"Pro-islet amyloid polypeptide in micelles contains a helical prohormone segment. <i> DeLisle CF, Malooley AL, Banerjee I, Banerjee I, Lorieau JL. </i> FEBS J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03417r004","statement":[{"text":"In the absence of lipid, unfolded features dominate the CD spectra for proIAPP, and the protein is intrinsically disordered. In the presence of detergent micelles and bicelles, the protein adopts a mostly α‐helical structure at both pH values. The helical structure is indicated by the mean residue ellipticity ([θ]) minima near 208 and 222 nm (Fig. 7A,B).","type":"Results"},{"text":"In the presence of membranes at pH 4.5, the proIAPP helicity is 47 ± 4%, 46 ± 5%, 50 ± 5%, and 31 ± 5% for DPC, SDS, 3 : 1 1,2‐dimyristoyl‐sn‐glycero‐3‐phosphocholine (DMPC)/1,2‐dimyristoyl‐sn‐glycero‐3‐phospho‐l‐serine (DMPS) bicelles, and DMPC bicelles, respectively. At pH 7.0, proIAPP helicity is 42 ± 4%, 50 ± 4%, 47 ± 5%, and 34 ± 5% for DPC, SDS, DMPC/DMPS bicelles, and DMPC bicelles respectively. The helical content of the protein in the absence of lipid is 14 ± 3% and 14 ± 3% at pH 4.5 at pH 7.0, respectively, which agrees with a previous report on the transiently helical α1 in IAPP and the presence of the C2‐C7 (C13‐C18 in proIAPP) disulfide bond [57].","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T10:41:21.499Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":23,"end":89,"reference_id":"32077246","reference_source":"pmid","reference_html":"Pro-islet amyloid polypeptide in micelles contains a helical prohormone segment. <i> DeLisle CF, Malooley AL, Banerjee I, Banerjee I, Lorieau JL. </i> FEBS J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03417r005","statement":[{"text":"In the absence of lipid, unfolded features dominate the CD spectra for proIAPP, and the protein is intrinsically disordered. In the presence of detergent micelles and bicelles, the protein adopts a mostly α‐helical structure at both pH values. The helical structure is indicated by the mean residue ellipticity ([θ]) minima near 208 and 222 nm (Fig. 7A,B).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T10:41:26.711Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":74,"end":89,"reference_id":"32077246","reference_source":"pmid","reference_html":"Pro-islet amyloid polypeptide in micelles contains a helical prohormone segment. <i> DeLisle CF, Malooley AL, Banerjee I, Banerjee I, Lorieau JL. </i> FEBS J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03417r006","statement":[{"text":"We used CD to conduct a secondary structure analysis of the Cpro peptide at pH 4.5 and 6.1, in the presence and absence of DPC micelles (Fig. 10A). In the absence of lipid, Cpro displays unfolded or coil characteristics at both pH values.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T10:41:15.829Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":74,"end":89,"reference_id":"32077246","reference_source":"pmid","reference_html":"Pro-islet amyloid polypeptide in micelles contains a helical prohormone segment. <i> DeLisle CF, Malooley AL, Banerjee I, Banerjee I, Lorieau JL. </i> FEBS J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03417r007","statement":[{"text":"We used CD to conduct a secondary structure analysis of the Cpro peptide at pH 4.5 and 6.1, in the presence and absence of DPC micelles (Fig. 10A). In the absence of lipid, Cpro displays unfolded or coil characteristics at both pH values. At pH 4.5 in DPC micelles, Cpro appears predominantly helical.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T10:41:20.709Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":74,"end":89,"reference_id":"32077246","reference_source":"pmid","reference_html":"Pro-islet amyloid polypeptide in micelles contains a helical prohormone segment. <i> DeLisle CF, Malooley AL, Banerjee I, Banerjee I, Lorieau JL. </i> FEBS J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03417r008","statement":[{"text":"We used CD to conduct a secondary structure analysis of the Cpro peptide at pH 4.5 and 6.1, in the presence and absence of DPC micelles (Fig. 10A). In the absence of lipid, Cpro displays unfolded or coil characteristics at both pH values. At pH 4.5 in DPC micelles, Cpro appears predominantly helical.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T10:41:25.715Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":23,"end":89,"reference_id":"32077246","reference_source":"pmid","reference_html":"Pro-islet amyloid polypeptide in micelles contains a helical prohormone segment. <i> DeLisle CF, Malooley AL, Banerjee I, Banerjee I, Lorieau JL. </i> FEBS J, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03417r009","statement":[{"text":"The entire proIAPP structure appears to wrap around the DPC micelle.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T10:41:23.706Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":9,"released":"2021_12","sequence":"MGILKLQVFLIVLSVALNHLKATPIESHQVEKRKCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTYGKRNAVEVLKREPLNYLPL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI000012D0C4","uniref100":"UniRef100_P10997","uniref90":"UniRef90_P10997","uniref50":"UniRef50_P10997","genes":[{"name":{"value":"IAPP"}}],"alphafold_very_low_content":0,"disorder_content":0.7528089887640449,"disprot_consensus":{"full":[{"start":23,"end":89,"type":"T"}],"Structural state":[{"start":23,"end":89,"type":"D"}],"Structural transition":[{"start":23,"end":89,"type":"T"}],"Molecular function":[{"start":23,"end":89,"type":"F"}]}},{"disprot_id":"DP03418","acc":"Q96PU8-9","creator":"nfarahi","date":"2021-07-09T19:01:26.289Z","features":{"pfam":[],"gene3D":[]},"length":319,"name":"Isoform 6 of Protein quaking","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":205,"end":319,"reference_id":"31547849","reference_source":"pmid","reference_html":"Stability and flexibility of full-length human oligodendrocytic QKI6. <i> Raasakka A, Kursula P. </i> BMC Res Notes, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006202","ec_ontology":"ECO","ec_name":"synchrotron radiation circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03418r001","statement":[{"text":"SRCD measurements of QKI6 produced a spectrum typical for a folded protein, but the minimum at 205 nm suggested the presence of disorder (Fig. 2a).","type":"Results"},{"text":"The SRCD measurement itself could not indicate the position of the disordered residues, however, for the folded part there is available structure, so it is most likely the C-terminal tail that was responsible for the presence of disoder.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:22:05.802Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":205,"end":319,"reference_id":"31547849","reference_source":"pmid","reference_html":"Stability and flexibility of full-length human oligodendrocytic QKI6. <i> Raasakka A, Kursula P. </i> BMC Res Notes, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03418r002","statement":[{"text":"The dimeric QKI6 was highly flexible, as evident from the Kratky plot (Fig. 2c), and elongated, based on its radius of gyration (Rg, 5.24 nm) and maximum dimension (Dmax, 21 nm). Ab initio models based on the SAXS data appear elongated with a compact core (Fig. 2e).","type":"Results"},{"text":"In all three modelling sets, the 115 C-terminal residues were extended, in agreement with secondary structure predictions. To conclude, in the absence of an mRNA binding partner, the subdomains of dimeric QKI6 present a great degree of flexibility with respect to each other and most likely collapse to a more ordered arrangement upon binding to a 3′-UTR. The STAR domain is followed by an intrinsically disordered C terminus of currently unknown function.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:22:00.271Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MVGEMETKEKPKPTPDYLMQLMNDKKLMSSLPNFCGIFNHLERLLDEEISRVRKDMYNDTLNGSTEKRSAELPDAVGPIVQLQEKLYVPVKEYPDFNFVGRILGPRGLTAKQLEAETGCKIMVRGKGSMRDKKKEEQNRGKPNWEHLNEDLHVLITVEDAQNRAEIKLKRAVEEVKKLLVPAAEGEDSLKKMQLMELAILNGTYRDANIKSPALAFSLAATAQAAPRIITGPAPVLPPAALRTPTPAGPTIMPLIRQIQTAVMPNGTPHPTAAIVPPGPEAGLIYTPYEYPYTLAPATSILEYPIEPSGVLGMAFPTKG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000071672","uniref100":"","uniref90":"","uniref50":"","genes":[{"name":{"value":"QKI"},"synonyms":[{"value":"HKQ"}]}],"disorder_content":0.3605015673981191,"disprot_consensus":{"full":[{"start":205,"end":319,"type":"D"}],"Structural state":[{"start":205,"end":319,"type":"D"}]}},{"disprot_id":"DP03419","acc":"A1B602","creator":"nfarahi","date":"2021-07-09T20:24:04.743Z","features":{"pfam":[{"id":"PF07345","name":"ATPase inhibitor subunit zeta","start":1,"end":99}],"gene3D":[]},"length":104,"name":"Uncharacterized protein","ncbi_taxon_id":318586,"organism":"Paracoccus denitrificans (strain Pd 1222)","regions":[{"start":1,"end":14,"reference_id":"24522203","reference_source":"pmid","reference_html":"The ζ subunit of the F1FO-ATP synthase of α-proteobacteria controls rotation of the nanomotor with a different structure. <i> Zarco-Zavala M, Morales-Ríos E, Mendoza-Hernández G, Ramírez-Silva L, Pérez-Hernández G, García-Trejo JJ. </i> FASEB J, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03419r001","statement":[{"text":"As a first approach to identify the inhibitory domain of the ζ subunit, the recombinant protein was subjected to limited proteolysis with trypsin, which removed 14 and 25 residues from the N- and C-terminal extremes, respectively, as found by tandem mass spectrometry analyses.","type":"Results"},{"text":"The proteolytic accessibility of the N and C termini indicates that both extremes of the protein are exposed and most likely highly mobile, whereas the central Pd-ζ15–79 domain seems resistant to the protease treatment, suggesting that it should have a rigid folded structure that competes with Pd-ζWT for binding to the PdF1-ATPase.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-12T11:00:43.764Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":80,"end":104,"reference_id":"24522203","reference_source":"pmid","reference_html":"The ζ subunit of the F1FO-ATP synthase of α-proteobacteria controls rotation of the nanomotor with a different structure. <i> Zarco-Zavala M, Morales-Ríos E, Mendoza-Hernández G, Ramírez-Silva L, Pérez-Hernández G, García-Trejo JJ. </i> FASEB J, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03419r002","statement":[{"text":"As a first approach to identify the inhibitory domain of the ζ subunit, the recombinant protein was subjected to limited proteolysis with trypsin, which removed 14 and 25 residues from the N- and C-terminal extremes, respectively, as found by tandem mass spectrometry analyses.","type":"Results"},{"text":"The proteolytic accessibility of the N and C termini indicates that both extremes of the protein are exposed and most likely highly mobile, whereas the central Pd-ζ15–79 domain seems resistant to the protease treatment, suggesting that it should have a rigid folded structure that competes with Pd-ζWT for binding to the PdF1-ATPase.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-12T11:00:44.731Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":1,"end":14,"reference_id":"24522203","reference_source":"pmid","reference_html":"The ζ subunit of the F1FO-ATP synthase of α-proteobacteria controls rotation of the nanomotor with a different structure. <i> Zarco-Zavala M, Morales-Ríos E, Mendoza-Hernández G, Ramírez-Silva L, Pérez-Hernández G, García-Trejo JJ. </i> FASEB J, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03419r003","statement":[{"text":"The recombinant Pd-ζΔNT construct was overexpressed in E. coli and purified as described for the Pd-ζWT to ~93% purity. The Pd-ζΔNT was reconstituted into the PdF1-ATPase, and the inhibitory activity was measured. As shown in Fig. 3, removal of the first 14 N-terminal residues of Pd-ζ in the Pd-ζΔNT construct completely abolished the inhibitory capacity of the protein at concentrations as high as 9 μM, i.e., concentrations that result in saturation of the Pd-ζWT and completely block PdF1-ATPase activity. These data indicate that the N-terminal side of the Pd-ζ subunit contains the inhibitory domain of the protein.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-12T11:00:37.701Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":19,"reference_id":"26460036","reference_source":"pmid","reference_html":"Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution. <i> Morales-Rios E, Montgomery MG, Leslie AG, Walker JE. </i> Proc Natl Acad Sci U S A, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03419r004","statement":[{"text":"The inhibitor is bound to the F1 domain via residues 1–19 of the N-terminal α-helix, which occupy a cleft in the lower region of the αDPβDP-catalytic interface, with the rest of the α-helix (residues 20–32) extending from the surface of the enzyme. ","type":"Results"},{"text":"In solution, residues 1–18 of the 107-aa chain of the ζ-inhibitor are unstructured, with the rest of the chain folded into a four-helix bundle (residues 19–42, 46–53, 66–77, and 81–103).","type":"Results"}],"cross_refs":[{"db":"PDB","id":"5DN6"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-12T11:17:08.252Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":1,"end":19,"reference_id":"26460036","reference_source":"pmid","reference_html":"Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution. <i> Morales-Rios E, Montgomery MG, Leslie AG, Walker JE. </i> Proc Natl Acad Sci U S A, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03419r005","statement":[{"text":"The inhibitor is bound to the F1 domain via residues 1–19 of the N-terminal α-helix, which occupy a cleft in the lower region of the αDPβDP-catalytic interface (Fig. 2 A and B), with the rest of the α-helix (residues 20–32) extending from the surface of the enzyme.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"5DN6"}],"interaction_partner":[{"db":"UniProt","id":"A1B8N8","partner_start":null,"partner_end":null},{"db":"UniProt","id":"A1B8P0","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:04:15.361Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":19,"reference_id":"24838125","reference_source":"pmid","reference_html":"NMR structures of α-proteobacterial ATPase-regulating ζ-subunits. <i> Serrano P, Geralt M, Mohanty B, Wüthrich K. </i> J Mol Biol, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03419r006","statement":[{"text":"The flexibly disordered N-terminal 19-residue segment of Pd-ζ is not shown.","type":"Figure"}],"cross_refs":[{"db":"BMRB","id":"18018"},{"db":"PDB","id":"2LL0"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-12T11:22:02.273Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":6,"released":"2021_12","sequence":"MTTFDDRERAHEAKFAHDAELNFKAEARRNRLLGEWAAGLLGKTGDDARAYALTVVTSDFDEPGDEDVFRKLAADLEGKADEETIRAKMVELRATAREQIISEI","taxonomy":["Bacteria","Proteobacteria","Alphaproteobacteria","Rhodobacterales","Rhodobacteraceae","Paracoccus"],"UniParc":"UPI0000555F09","uniref100":"UniRef100_A1B602","uniref90":"UniRef90_A1B602","uniref50":"UniRef50_A0A2D6T2L2","genes":[{"olnNames":[{"value":"Pden_2862","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ABL70946.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABL70946.1"}}]}]}],"alphafold_very_low_content":0,"disorder_content":0.4230769230769231,"disprot_consensus":{"full":[{"start":1,"end":19,"type":"T"},{"start":80,"end":104,"type":"D"}],"Structural state":[{"start":1,"end":19,"type":"D"},{"start":80,"end":104,"type":"D"}],"Molecular function":[{"start":1,"end":19,"type":"F"}],"Structural transition":[{"start":1,"end":19,"type":"T"}]}},{"disprot_id":"DP03420","acc":"Q7TMK9","creator":"nfarahi","date":"2021-07-09T20:50:58.345Z","features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":164,"end":229},{"id":"PF00076","name":"RNA recognition motif","start":245,"end":307},{"id":"PF00076","name":"RNA recognition motif","start":340,"end":401},{"id":"PF18360","name":"Heterogeneous nuclear ribonucleoprotein Q acidic domain","start":34,"end":103}],"gene3D":[]},"length":623,"name":"Heterogeneous nuclear ribonucleoprotein Q","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":108,"end":140,"reference_id":"27081926","reference_source":"pmid","reference_html":"The acidic domain is a unique structural feature of the splicing factor SYNCRIP. <i> Beuck C, Williamson JR, Wüthrich K, Serrano P. </i> Protein Sci, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03420r002","statement":[{"text":"Investigations with constructs expanding up to residue 140 revealed that AcD24–107 forms a globular domain and that the segment 108–140 is flexibly disordered in solution (Supporting Information, Fig. S1).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:07:11.871Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2023_12","sequence":"MATEHVNGNGTEEPMDTTSAVIHSENFQTLLDAGLPQKVAEKLDEIYVAGLVAHSDLDERAIEALKEFNEDGALAVLQQFKDSDLSHVQNKSAFLCGVMKTYRQREKQGTKVADSSKGPDEAKIKALLERTGYTLDVTTGQRKYGGPPPDSVYSGQQPSVGTEIFVGKIPRDLFEDELVPLFEKAGPIWDLRLMMDPLTGLNRGYAFVTFCTKEAAQEAVKLYNNHEIRSGKHIGVCISVANNRLFVGSIPKSKTKEQILEEFSKVTEGLTDVILYHQPDDKKKNRGFCFLEYEDHKTAAQARRRLMSGKVKVWGNVGTVEWADPIEDPDPEVMAKVKVLFVRNLANTVTEEILEKSFSQFGKLERVKKLKDYAFIHFDERDGAVKAMEEMNGKDLEGENIEIVFAKPPDQKRKERKAQRQAAKNQMYDDYYYYGPPHMPPPTRGRGRGGRGGYGYPPDYYGYEDYYDYYGYDYHNYRGGYEDPYYGYEDFQVGARGRGGRGARGAAPSRGRGAAPPRGRAGYSQRGGPGSARGVRGARGGAQQQRGRGVRGARGGRGGNVGGKRKADGYNQPDTKRRQTNNQNWGSQPIAQQPLQGGDHSGNYGYKSENQEFYQDTFGQQWK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"UniParc":"UPI00001B639C","uniref100":"UniRef100_Q7TMK9","uniref90":"UniRef90_Q7TMK9","uniref50":"UniRef50_O60506","genes":[{"name":{"value":"Syncrip"},"synonyms":[{"value":"Hnrpq"},{"value":"Nsap1"},{"value":"Nsap1l"}]}],"alphafold_very_low_content":0.3258426966292135,"dataset":["RNA-binding proteins"],"disorder_content":0.052969502407704656,"disprot_consensus":{"full":[{"start":108,"end":140,"type":"D"}],"Structural state":[{"start":108,"end":140,"type":"D"}]}},{"disprot_id":"DP03421","acc":"P12464","creator":"nfarahi","date":"2021-07-10T19:57:43.733Z","features":{"pfam":[{"id":"PF05066","name":"HB1, ASXL, restriction endonuclease HTH domain","start":14,"end":81}],"gene3D":[]},"length":173,"name":"DNA-directed RNA polymerase subunit delta","ncbi_taxon_id":224308,"organism":"Bacillus subtilis (strain 168)","regions":[{"start":84,"end":173,"reference_id":"31550880","reference_source":"pmid","reference_html":"Quantitative Conformational Analysis of Functionally Important Electrostatic Interactions in the Intrinsically Disordered Region of Delta Subunit of Bacterial RNA Polymerase. <i> Kubáň V, Srb P, Štégnerová H, Padrta P, Zachrdla M, Jaseňáková Z, Šanderová H, Vítovská D, Krásný L, Koval' T, Dohnálek J, Ziemska-Legiecka J, Grynberg M, Jarnot P, Gruca A, Jensen MR, Blackledge M, Žídek L. </i> J Am Chem Soc, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03421r001","statement":[{"text":"Here, we investigate the conformational behavior of the δ subunit of RNA polymerase from Bacillus subtilis whose unfolded domain is highly charged, with 7 positively charged amino acids followed by 51 acidic amino acids. Using a specifically designed analytical strategy, we identify transient contacts between the two regions using a combination of NMR paramagnetic relaxation enhancements, residual dipolar couplings (RDCs), chemical shifts, and small-angle scattering.","type":"Abstract"},{"text":"The unstructured C-terminal domain is 90 aa long and highly charged. The charge distribution of this domain is distinct, with a conserved stretch of 9 residues (96–104) containing 7 positive charges followed by the rest of the domain with 51 acidic residues (K-D/E motif).","type":"Introduction"},{"text":"Here, the ASTEROIDS approach(11−13) is used to describe the conformational behavior of the CTD of δ subunit in solution using a combination of NMR chemical shifts (CSs), paramagnetic relaxation enhancements (PREs), and residual dipolar couplings (RDCs) as well as small-angle scattering (SAXS).","type":"Introduction"},{"text":"All the RDC-s, PRE-s and all depicted values in Figure 1 clearly support that the C-terminal segment is and IDR.","type":"Curator statement"},{"text":"The most striking local feature was the deviation of Cα and C′ chemical shifts with respect to random coil values. Both shifts display negative average values as compared to secondary shifts, which translates into a tendency of the whole C-teminal domain toward an extended structure of the polyproline II type (PPII) and depletion of α helical conformations. This may be related to the high density of negative charges; indeed higher PPII conformation is detected in the acidic C-terminal part of the unfolded domain due to local electrostatic repulsion.","type":"Results"}],"cross_refs":[{"db":"BMRB","id":"27963"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-12T10:43:50.899Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":84,"end":173,"reference_id":"31550880","reference_source":"pmid","reference_html":"Quantitative Conformational Analysis of Functionally Important Electrostatic Interactions in the Intrinsically Disordered Region of Delta Subunit of Bacterial RNA Polymerase. <i> Kubáň V, Srb P, Štégnerová H, Padrta P, Zachrdla M, Jaseňáková Z, Šanderová H, Vítovská D, Krásný L, Koval' T, Dohnálek J, Ziemska-Legiecka J, Grynberg M, Jarnot P, Gruca A, Jensen MR, Blackledge M, Žídek L. </i> J Am Chem Soc, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03421r002","statement":[{"text":"Here, we investigate the conformational behavior of the δ subunit of RNA polymerase from Bacillus subtilis whose unfolded domain is highly charged, with 7 positively charged amino acids followed by 51 acidic amino acids. Using a specifically designed analytical strategy, we identify transient contacts between the two regions using a combination of NMR paramagnetic relaxation enhancements, residual dipolar couplings (RDCs), chemical shifts, and small-angle scattering.","type":"Abstract"},{"text":"The unstructured C-terminal domain is 90 aa long and highly charged. The charge distribution of this domain is distinct, with a conserved stretch of 9 residues (96–104) containing 7 positive charges followed by the rest of the domain with 51 acidic residues (K-D/E motif).","type":"Introduction"},{"text":"Here, the ASTEROIDS approach(11−13) is used to describe the conformational behavior of the CTD of δ subunit in solution using a combination of NMR chemical shifts (CSs), paramagnetic relaxation enhancements (PREs), and residual dipolar couplings (RDCs) as well as small-angle scattering (SAXS).","type":"Introduction"},{"text":"The Kratky plot depicted in Figure 1 as well as the normalized distribution of radius of gyrations of the selected ensembles compared to the statistical coil is typical for IDRs.","type":"Curator statement"}],"cross_refs":[{"db":"SASBDB","id":"SASDF58"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-12T10:43:52.142Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":96,"end":104,"reference_id":"31550880","reference_source":"pmid","reference_html":"Quantitative Conformational Analysis of Functionally Important Electrostatic Interactions in the Intrinsically Disordered Region of Delta Subunit of Bacterial RNA Polymerase. <i> Kubáň V, Srb P, Štégnerová H, Padrta P, Zachrdla M, Jaseňáková Z, Šanderová H, Vítovská D, Krásný L, Koval' T, Dohnálek J, Ziemska-Legiecka J, Grynberg M, Jarnot P, Gruca A, Jensen MR, Blackledge M, Žídek L. </i> J Am Chem Soc, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03421r003","statement":[{"text":"The most visible feature of the distance map are contacts observed between the lysine-rich stretch (K-tract, K96–K104) and the acidic region (F115–E170).","type":"Results"}],"cross_refs":[{"db":"BMRB","id":"27963"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-12T10:43:48.655Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":115,"end":170,"reference_id":"31550880","reference_source":"pmid","reference_html":"Quantitative Conformational Analysis of Functionally Important Electrostatic Interactions in the Intrinsically Disordered Region of Delta Subunit of Bacterial RNA Polymerase. <i> Kubáň V, Srb P, Štégnerová H, Padrta P, Zachrdla M, Jaseňáková Z, Šanderová H, Vítovská D, Krásný L, Koval' T, Dohnálek J, Ziemska-Legiecka J, Grynberg M, Jarnot P, Gruca A, Jensen MR, Blackledge M, Žídek L. </i> J Am Chem Soc, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03421r004","statement":[{"text":"The most visible feature of the distance map are contacts observed between the lysine-rich stretch (K-tract, K96–K104) and the acidic region (F115–E170).","type":"Results"}],"cross_refs":[{"db":"BMRB","id":"27963"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-12T10:43:50.012Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":93,"end":173,"reference_id":"20890634","reference_source":"pmid","reference_html":"Strategy for complete NMR assignment of disordered proteins with highly repetitive sequences based on resolution-enhanced 5D experiments. <i> Motáčková V, Nováček J, Zawadzka-Kazimierczuk A, Kazimierczuk K, Zídek L, Sanderová H, Krásný L, Koźmiński W, Sklenář V. </i> J Biomol NMR, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"BMRB","id":"16912"}],"region_id":"DP03421r005","statement":[{"text":"The 1HN chemical shift dispersion of the disordered C-terminal domain of the δ subunit is lower than that of the retroviral protease: 0.5 ppm versus 0.7 ppm. The 15N chemical shifts of the unstructured regions cover 6.4 and 11.1 ppm for the δ subunit and retroviral protease, respectively, with the most crowded regions spanning 3.4 ppm and 4.8 ppm, respectively.","type":"Results"},{"text":"The HSQC spectrum is typically that of a highly disordered protein. The authors provide the boundaries of the disordered C-terminus in Figure 1.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:01:20.660Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":96,"end":104,"reference_id":"31550880","reference_source":"pmid","reference_html":"Quantitative Conformational Analysis of Functionally Important Electrostatic Interactions in the Intrinsically Disordered Region of Delta Subunit of Bacterial RNA Polymerase. <i> Kubáň V, Srb P, Štégnerová H, Padrta P, Zachrdla M, Jaseňáková Z, Šanderová H, Vítovská D, Krásný L, Koval' T, Dohnálek J, Ziemska-Legiecka J, Grynberg M, Jarnot P, Gruca A, Jensen MR, Blackledge M, Žídek L. </i> J Am Chem Soc, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03421r006","statement":[{"text":"Experiments addressing the effect of the charge perturbation in δKE on the affinity of RNAP to DNA (Pilv promoter on a supercoiled plasmid) showed that δKE decreased the affinity of RNAP to DNA in comparison with RNAP with δ (Figure 5a). Experiments testing the effect of δ/δKE on the [iNTP] requirement (Pilv promoter on supercoiled plasmid) revealed that δ increased the requirement of RNAP for [GTP] in comparison to RNAP lacking δ, and this effect was more pronounced with δKE (Figure 5b).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:02:47.955Z"},"ec_go":"IMP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":6,"released":"2021_12","sequence":"MGIKQYSQEELKEMALVEIAHELFEEHKKPVPFQELLNEIASLLGVKKEELGDRIAQFYTDLNIDGRFLALSDQTWGLRSWYPYDQLDEETQPTVKAKKKKAKKAVEEDLDLDEFEEIDEDDLDLDEVEEELDLEADDFDEEDLDEDDDDLEIEEDIIDEDDEDYDDEEEEIK","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Bacillus"],"UniParc":"UPI0000060BC7","uniref100":"UniRef100_P12464","uniref90":"UniRef90_P12464","uniref50":"UniRef50_P12464","genes":[{"name":{"value":"rpoE","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"2843435","url":"http://www.ncbi.nlm.nih.gov/pubmed/2843435","alternativeUrl":"https://europepmc.org/abstract/MED/2843435"}}]},"olnNames":[{"value":"BSU37160"}]}],"alphafold_very_low_content":0.07514450867052024,"disorder_content":0.5202312138728323,"disprot_consensus":{"full":[{"start":84,"end":173,"type":"D"}],"Structural state":[{"start":84,"end":173,"type":"D"}],"Molecular function":[{"start":96,"end":104,"type":"F"},{"start":115,"end":170,"type":"F"}]}},{"disprot_id":"DP03422","acc":"A0A142G2L5","creator":"nfarahi","date":"2021-07-10T21:37:49.978Z","features":{"pfam":[],"gene3D":[]},"length":181,"name":"Uncharacterized protein","ncbi_taxon_id":714,"organism":"Aggregatibacter actinomycetemcomitans","regions":[{"start":21,"end":181,"reference_id":"31932991","reference_source":"pmid","reference_html":"Dispersion from Cα or NH: 4D experiments for backbone resonance assignment of intrinsically disordered proteins. <i> Tossavainen H, Salovaara S, Hellman M, Ihalin R, Permi P. </i> J Biomol NMR, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"BMRB","id":"27824"}],"region_id":"DP03422r001","statement":[{"text":"BilRI is an intrinsically disordered protein (IDP), as demonstrated by its 1H, 15N HSQC spectrum, which displays very limited signal dispersion (Ahlstrand et al. 2017). In the HN dimension their dispersion is only 0.63 ppm.","type":"Introduction"},{"text":"Peaks in the BilRI 2D 1H, 15N-HSQC spectrum display overwhelming overlap (Fig. 2a) and a very narrow distribution in the HN dimension.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:07:52.300Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":21,"end":181,"reference_id":"27459270","reference_source":"pmid","reference_html":"A novel intrinsically disordered outer membrane lipoprotein of Aggregatibacter actinomycetemcomitans binds various cytokines and plays a role in biofilm response to interleukin-1β and interleukin-8. <i> Ahlstrand T, Tuominen H, Beklen A, Torittu A, Oscarsson J, Sormunen R, Pöllänen MT, Permi P, Ihalin R. </i> Virulence, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03422r002","statement":[{"text":"The proton (1H) spectrum of BilRI measured at 600 MHz exhibits features typical of a disordered protein, including a collapsed chemical shift dispersion in the amide proton region (8.2 ± 0.3 1H ppm) and the lack of shielded methyl protons, i.e., clustering of methyl protons to so-called random coil shift, 0.7 ppm (Fig. 1A).","type":"Results"},{"text":"To slow down the chemical exchange of labile amide protons with solvent protons, we measured the 15N HSQC spectrum of BilRI under mildly acidic conditions (pH 5). This spectrum more clearly highlights the same features already visible in the corresponding 1H spectrum, i.e., poor dispersion of amide proton chemical shifts, indicating that BilRI remains disordered in solution and under slightly acidic conditions.","type":"Results"},{"text":"The results of the nuclear magnetic resonance (NMR) studies, which indicated the absence of a specific fold, were supported by the amino acid analysis showing high numbers of charged and polar residues and a low number of hydrophobic bulky amino acids, a composition that is typical for IDPs.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:08:01.503Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":21,"end":181,"reference_id":"33939577","reference_source":"pmid","reference_html":"Decreased temperature increases the expression of a disordered bacterial late embryogenesis abundant (LEA) protein that enhances natural transformation. <i> Maula T, Vahvelainen N, Tossavainen H, Koivunen T, T Pöllänen M, Johansson A, Permi P, Ihalin R. </i> Virulence, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03422r003","statement":[{"text":"We further characterized its structural features by analyzing the recently assigned chemical shifts of BilRI [37] and its {1H}-15N heteronuclear nuclear Overhauser effect (NOE), T1 and 1H, 15N nuclear Overhauser effect spectroscopy-heteronuclear single quantum coherence spectroscopy (NOESY-HSQC) spectra.","type":"Results"},{"text":"Chemical shift assignment for BilRI was extremely complicated due to the presence of repeating segments in the amino acid sequence leading to considerable overlap of NMR peaks [37]. This overlap also hampered the analyses of 15N relaxation and NOESY spectra because of the crowded 1H, 15N HSQC spectrum.","type":"Results"},{"text":"The deviations of the experimental BilRI chemical shifts from their random coil values were small (−0.13< SSP <0.23) throughout the sequence and were biased toward helical propensity (positive SSP scores). The score pattern was similar within the three repeating segments of the sequence (51–80, 91–120, and 131–160), suggesting that the minute residual structural propensity is not random: the N-terminal residues of these repeats show a helical tendency.","type":"Results"},{"text":"Overall, the BilRI backbone appears to be very flexible, as expected, and there is no evidence of specific long-range contacts in BilRI. The repeat regions, especially their N-terminal 2/3, appear to be slightly more rigid than the rest of the protein.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:08:03.562Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":21,"end":181,"reference_id":"27459270","reference_source":"pmid","reference_html":"A novel intrinsically disordered outer membrane lipoprotein of Aggregatibacter actinomycetemcomitans binds various cytokines and plays a role in biofilm response to interleukin-1β and interleukin-8. <i> Ahlstrand T, Tuominen H, Beklen A, Torittu A, Oscarsson J, Sormunen R, Pöllänen MT, Permi P, Ihalin R. </i> Virulence, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005581","ec_ontology":"ECO","ec_name":"enzyme-linked immunoabsorbent assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03422r004","statement":[{"text":"A microplate assay showed that recombinant BilRI bound to various cytokines, of which the binding to IL-8 was high compared with the binding of BilRI to the negative control protein bovine serum albumin (BSA; p = 0.008; paired-samples T-test; Fig. 2A).","type":"Results"},{"text":"Figure2. A) Recombinant BilRI containing an 8-histidine-long C-terminal tag bound to various recombinant human cytokines in a microplate assay. BSA served as a negative control and was used as a blocking agent in the assays. The bound BilRI was detected with HRP-labeled HisProbe™. The BilRI binding to IL-8 was high compared to the binding to the control protein BSA (**:p = 0.008, paired-samples T-test). ","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:07:51.541Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":4,"released":"2023_12","sequence":"MKKSVLAALVLGVTLSVTGCDDSKTSPQAEQAKTSVSEAKDAVVNAANDVKDATVEAAKDAQNMAADKMVEVKDAISEKMDAMTTQASEMKDAAVEAAKDAKDAAADKMAEVKDAISEKMDAMATQVNEMKDTAAEAVKDAKDAAADKMTEVKDAVSEKMGATATQTNEMKDAVKSETESK","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Pasteurellales","Pasteurellaceae","Aggregatibacter"],"UniParc":"UPI0001CA757B","uniref100":"UniRef100_A0A142G2L5","uniref90":"UniRef90_H0KF40","uniref50":"UniRef50_A0A1V3K9H2","genes":[{"orfNames":[{"value":"FXB68_04315","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TYA35270.1","url":"https://www.ebi.ac.uk/ena/browser/view/TYA35270.1"}}]}]}],"alphafold_very_low_content":0.9226519337016574,"disorder_content":0.8895027624309392,"disprot_consensus":{"full":[{"start":21,"end":181,"type":"D"}],"Structural state":[{"start":21,"end":181,"type":"D"}],"Molecular function":[{"start":21,"end":181,"type":"F"}]}},{"disprot_id":"DP03423","acc":"F1NGB1","creator":"nfarahi","date":"2021-07-10T22:05:20.625Z","features":{"pfam":[{"id":"PF13499","name":"EF-hand domain pair","start":247,"end":322},{"id":"PF25434","name":"NUCB1-like, N-terminal domain","start":22,"end":163}],"gene3D":[]},"length":455,"name":"Uncharacterized protein","ncbi_taxon_id":9031,"organism":"Gallus gallus","regions":[{"start":190,"end":455,"reference_id":"32184136","reference_source":"pmid","reference_html":"Calcium ions modulate the structure of the intrinsically disordered Nucleobindin-2 protein. <i> Skorupska A, Bystranowska D, Dąbrowska K, Ożyhar A. </i> Int J Biol Macromol, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03423r001","statement":[{"text":"Surprisingly, the hydrogen-deuterium exchange mass spectrometry results revealed\nthat Nucb2 is divided into two parts: an N-terminal half with a stable mosaic-like structure and a disordered C-terminal half.","type":"Abstract"},{"text":"The HDX pattern of this part of the proteins resembles a mosaic-like character, which contains regions with fast and slow HDX interlacing with each other. ","type":"Results"},{"text":"On the other hand, the carboxyl-terminal halves of both the Nucb2s (corresponding to nesfatin-3) were observed to exhibit a more uniform and fast exchange rate, even within the first 10 s, which indicates a very high level of solvent exposure and flexibility.","type":"Results"},{"text":"The authors do not mention exact residue boundaries, but the region corresponding to nesfatin-3 was shown for their construct in Figure 1 as starting from residue 166. There is a 24 residues long signal peptide in the UniProt sequence that was not present in the studied construct, so residue 166 corresponds to UniProt residue 190.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:25:23.794Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":265,"end":284,"reference_id":"32184136","reference_source":"pmid","reference_html":"Calcium ions modulate the structure of the intrinsically disordered Nucleobindin-2 protein. <i> Skorupska A, Bystranowska D, Dąbrowska K, Ożyhar A. </i> Int J Biol Macromol, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03423r002","statement":[{"text":"The presence of Ca2+ induces the structural changes within the C-terminal half, leading to the formation of the mosaic-like structure in these parts of Nucb2s. Additionally, in the presence of Ca2+, both proteins undergo significant disorder-to-order transition, which is a feature characteristic for Ca2+ sensors (i.e. calmodulin).","type":"Introduction"},{"text":"Upon Ca2+ binding, both the Nucb2s showed significant changes in deuterium incorporation, but only at their carboxyl-terminal half (Fig. 7C and D). The effects of Ca2+ binding were mainly detected for peptides 241–260 and 285–310 (ggNucb2), as well as for peptides 241–258 and 285–310 (hsNucb2).","type":"Results"},{"text":"There is a 24 residues long signal peptide in the UniProt sequence that was not present in the studied construct, so residue 241 corresponds to UniProt residue 265.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:25:14.988Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":309,"end":334,"reference_id":"32184136","reference_source":"pmid","reference_html":"Calcium ions modulate the structure of the intrinsically disordered Nucleobindin-2 protein. <i> Skorupska A, Bystranowska D, Dąbrowska K, Ożyhar A. </i> Int J Biol Macromol, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03423r003","statement":[{"text":"The presence of Ca2+ induces the structural changes within the C-terminal half, leading to the formation of the mosaic-like structure in these parts of Nucb2s. Additionally, in the presence of Ca2+, both proteins undergo significant disorder-to-order transition, which is a feature characteristic for Ca2+ sensors (i.e. calmodulin).","type":"Introduction"},{"text":"Upon Ca2+ binding, both the Nucb2s showed significant changes in deuterium incorporation, but only at their carboxyl-terminal half (Fig. 7C and D). The effects of Ca2+ binding were mainly detected for peptides 241–260 and 285–310 (ggNucb2), as well as for peptides 241–258 and 285–310 (hsNucb2).","type":"Results"},{"text":"There is a 24 residues long signal peptide in the UniProt sequence that was not present in the studied construct, so residue 241 corresponds to UniProt residue 265.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:25:16.123Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":309,"end":334,"reference_id":"32184136","reference_source":"pmid","reference_html":"Calcium ions modulate the structure of the intrinsically disordered Nucleobindin-2 protein. <i> Skorupska A, Bystranowska D, Dąbrowska K, Ożyhar A. </i> Int J Biol Macromol, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03423r004","statement":[{"text":"The presence of Ca2+ induces the structural changes within the C-terminal half, leading to the formation of the mosaic-like structure in these parts of Nucb2s. Additionally, in the presence of Ca2+, both proteins undergo significant disorder-to-order transition, which is a feature characteristic for Ca2+ sensors (i.e. calmodulin).","type":"Introduction"},{"text":"Upon Ca2+ binding, both the Nucb2s showed significant changes in deuterium incorporation, but only at their carboxyl-terminal half (Fig. 7C and D). The effects of Ca2+ binding were mainly detected for peptides 241–260 and 285–310 (ggNucb2), as well as for peptides 241–258 and 285–310 (hsNucb2).","type":"Results"},{"text":"There is a 24 residues long signal peptide in the UniProt sequence that was not present in the studied construct, so residue 241 corresponds to UniProt residue 265.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:25:20.451Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":265,"end":284,"reference_id":"32184136","reference_source":"pmid","reference_html":"Calcium ions modulate the structure of the intrinsically disordered Nucleobindin-2 protein. <i> Skorupska A, Bystranowska D, Dąbrowska K, Ożyhar A. </i> Int J Biol Macromol, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03423r005","statement":[{"text":"The presence of Ca2+ induces the structural changes within the C-terminal half, leading to the formation of the mosaic-like structure in these parts of Nucb2s. Additionally, in the presence of Ca2+, both proteins undergo significant disorder-to-order transition, which is a feature characteristic for Ca2+ sensors (i.e. calmodulin).","type":"Introduction"},{"text":"Upon Ca2+ binding, both the Nucb2s showed significant changes in deuterium incorporation, but only at their carboxyl-terminal half (Fig. 7C and D). The effects of Ca2+ binding were mainly detected for peptides 241–260 and 285–310 (ggNucb2), as well as for peptides 241–258 and 285–310 (hsNucb2).","type":"Results"},{"text":"There is a 24 residues long signal peptide in the UniProt sequence that was not present in the studied construct, so residue 241 corresponds to UniProt residue 265.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:25:21.626Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"}],"regions_counter":11,"released":"2023_12","sequence":"MKWQSLLPQQCILLIPCLLMALEAVPIDIDKTKVKGEGHVEGEKIENPDTGLYYDEYLRQVIDVLETDKHFREKLQTADIEEIKSGKLSRELDLVSHHVRTRLDELKRQEVARLRMLIKAKMDSVQDTGIDHQALLKQFEHLNHQNPDTFEPKDLDMLIKAATSDLENYDKTRHEEFKKYEMMKEHERREYLKTLDEEKRQREESKFEEMKKKHGDHPKVHHPGSKDQLKEVWEEADGLDPNEFDPKTFFKLHDVNNDRFLDEQELEALFTKELEKVYDPKNEEDDMVEMEEERLRMREHVMNEVDINKDRLVTLEEFLRATEKKEFLEPDSWETLDQQQLFTEDELKEFESHISQQEDELRKKAEELQKQKEELQRQHDQLQAQKQELQQVVKQMEQKKLQQANPPAGPAGELKFQPPGEHKIEEAPKHPAGGDQPLPPGHIQEPAARTDQVHP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Phasianinae","Gallus"],"UniParc":"UPI00003ADC2B","uniref100":"UniRef100_F1NGB1","uniref90":"UniRef90_A0A218UTL9","uniref50":"UniRef50_P80303","genes":[{"name":{"value":"NUCB2","evidences":[{"code":"ECO:0000313","source":{"name":"Ensembl","id":"ENSGALP00000038782","url":"https://www.ensembl.org/id/ENSGALP00000038782"}}]}}],"alphafold_very_low_content":0.20659340659340658,"disorder_content":0.5846153846153846,"disprot_consensus":{"full":[{"start":190,"end":264,"type":"D"},{"start":265,"end":284,"type":"T"},{"start":285,"end":308,"type":"D"},{"start":309,"end":334,"type":"T"},{"start":335,"end":455,"type":"D"}],"Structural state":[{"start":190,"end":455,"type":"D"}],"Molecular function":[{"start":265,"end":284,"type":"F"},{"start":309,"end":334,"type":"F"}],"Structural transition":[{"start":265,"end":284,"type":"T"},{"start":309,"end":334,"type":"T"}]}},{"disprot_id":"DP03424","acc":"P80303","creator":"nfarahi","date":"2021-07-11T19:50:03.561Z","features":{"pfam":[{"id":"PF13499","name":"EF-hand domain pair","start":247,"end":322},{"id":"PF25434","name":"NUCB1-like, N-terminal domain","start":22,"end":163}],"gene3D":[]},"length":420,"name":"Nucleobindin-2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":190,"end":420,"reference_id":"32184136","reference_source":"pmid","reference_html":"Calcium ions modulate the structure of the intrinsically disordered Nucleobindin-2 protein. <i> Skorupska A, Bystranowska D, Dąbrowska K, Ożyhar A. </i> Int J Biol Macromol, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03424r001","statement":[{"text":"Surprisingly, the hydrogen-deuterium exchange mass spectrometry results revealed that Nucb2 is divided into two parts: an N-terminal half with a stable mosaic-like structure and a disordered C-terminal half.","type":"Abstract"},{"text":"The HDX pattern of this part of the proteins resembles a mosaic-like character, which contains regions with fast and slow HDX interlacing with each other.","type":"Results"},{"text":"On the other hand, the carboxyl-terminal halves of both the Nucb2s (corresponding to nesfatin-3) were observed to exhibit a more uniform and fast exchange rate, even within the first 10 s, which indicates a very high level of solvent exposure and flexibility.","type":"Results"},{"text":"The authors do not mention exact residue boundaries, but the region corresponding to nesfatin-3 was shown for their construct in Figure 1 as starting from residue 166. There is a 24 residues long signal peptide in the UniProt sequence that was not present in the studied construct, so residue 166 corresponds to UniProt residue 190.\"","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:28:08.041Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":265,"end":282,"reference_id":"32184136","reference_source":"pmid","reference_html":"Calcium ions modulate the structure of the intrinsically disordered Nucleobindin-2 protein. <i> Skorupska A, Bystranowska D, Dąbrowska K, Ożyhar A. </i> Int J Biol Macromol, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03424r003","statement":[{"text":"The presence of Ca2+ induces the structural changes within the C-terminal half, leading to the formation of the mosaic-like structure in these parts of Nucb2s. Additionally, in the presence of Ca2+, both proteins undergo significant disorder-to-order transition, which is a feature characteristic for Ca2+ sensors (i.e. calmodulin).","type":"Introduction"},{"text":"Upon Ca2+ binding, both the Nucb2s showed significant changes in deuterium incorporation, but only at their carboxyl-terminal half (Fig. 7C and D). The effects of Ca2+ binding were mainly detected for peptides 241–260 and 285–310 (ggNucb2), as well as for peptides 241–258 and 285–310 (hsNucb2).","type":"Results"},{"text":"There is a 24 residues long signal peptide in the UniProt sequence that was not present in the studied construct, so residue 241 corresponds to UniProt residue 265.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:28:04.515Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":309,"end":334,"reference_id":"32184136","reference_source":"pmid","reference_html":"Calcium ions modulate the structure of the intrinsically disordered Nucleobindin-2 protein. <i> Skorupska A, Bystranowska D, Dąbrowska K, Ożyhar A. </i> Int J Biol Macromol, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03424r004","statement":[{"text":"The presence of Ca2+ induces the structural changes within the C-terminal half, leading to the formation of the mosaic-like structure in these parts of Nucb2s. Additionally, in the presence of Ca2+, both proteins undergo significant disorder-to-order transition, which is a feature characteristic for Ca2+ sensors (i.e. calmodulin).","type":"Introduction"},{"text":"Upon Ca2+ binding, both the Nucb2s showed significant changes in deuterium incorporation, but only at their carboxyl-terminal half (Fig. 7C and D). The effects of Ca2+ binding were mainly detected for peptides 241–260 and 285–310 (ggNucb2), as well as for peptides 241–258 and 285–310 (hsNucb2).","type":"Results"},{"text":"There is a 24 residues long signal peptide in the UniProt sequence that was not present in the studied construct, so residue 241 corresponds to UniProt residue 265.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:28:05.597Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":265,"end":282,"reference_id":"32184136","reference_source":"pmid","reference_html":"Calcium ions modulate the structure of the intrinsically disordered Nucleobindin-2 protein. <i> Skorupska A, Bystranowska D, Dąbrowska K, Ożyhar A. </i> Int J Biol Macromol, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03424r008","statement":[{"text":"The presence of Ca2+ induces the structural changes within the C-terminal half, leading to the formation of the mosaic-like structure in these parts of Nucb2s. Additionally, in the presence of Ca2+, both proteins undergo significant disorder-to-order transition, which is a feature characteristic for Ca2+ sensors (i.e. calmodulin).","type":"Introduction"},{"text":"Upon Ca2+ binding, both the Nucb2s showed significant changes in deuterium incorporation, but only at their carboxyl-terminal half (Fig. 7C and D). The effects of Ca2+ binding were mainly detected for peptides 241–260 and 285–310 (ggNucb2), as well as for peptides 241–258 and 285–310 (hsNucb2).","type":"Results"},{"text":"There is a 24 residues long signal peptide in the UniProt sequence that was not present in the studied construct, so residue 241 corresponds to UniProt residue 265.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:28:01.543Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":309,"end":334,"reference_id":"32184136","reference_source":"pmid","reference_html":"Calcium ions modulate the structure of the intrinsically disordered Nucleobindin-2 protein. <i> Skorupska A, Bystranowska D, Dąbrowska K, Ożyhar A. </i> Int J Biol Macromol, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0005509","term_name":"calcium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03424r009","statement":[{"text":"The presence of Ca2+ induces the structural changes within the C-terminal half, leading to the formation of the mosaic-like structure in these parts of Nucb2s. Additionally, in the presence of Ca2+, both proteins undergo significant disorder-to-order transition, which is a feature characteristic for Ca2+ sensors (i.e. calmodulin).","type":"Introduction"},{"text":"Upon Ca2+ binding, both the Nucb2s showed significant changes in deuterium incorporation, but only at their carboxyl-terminal half (Fig. 7C and D). The effects of Ca2+ binding were mainly detected for peptides 241–260 and 285–310 (ggNucb2), as well as for peptides 241–258 and 285–310 (hsNucb2).","type":"Results"},{"text":"There is a 24 residues long signal peptide in the UniProt sequence that was not present in the studied construct, so residue 241 corresponds to UniProt residue 265.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:28:02.837Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":12,"released":"2023_12","sequence":"MRWRTILLQYCFLLITCLLTALEAVPIDIDKTKVQNIHPVESAKIEPPDTGLYYDEYLKQVIDVLETDKHFREKLQKADIEEIKSGRLSKELDLVSHHVRTKLDELKRQEVGRLRMLIKAKLDSLQDIGMDHQALLKQFDHLNHLNPDKFESTDLDMLIKAATSDLEHYDKTRHEEFKKYEMMKEHERREYLKTLNEEKRKEEESKFEEMKKKHENHPKVNHPGSKDQLKEVWEETDGLDPNDFDPKTFFKLHDVNSDGFLDEQELEALFTKELEKVYDPKNEEDDMVEMEEERLRMREHVMNEVDTNKDRLVTLEEFLKATEKKEFLEPDSWETLDQQQFFTEEELKEYENIIALQENELKKKADELQKQKEELQRQHDQLEAQKLEYHQVIQQMEQKKLQQGIPPSGPAGELKFEPHI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI000013D6B1","uniref100":"UniRef100_P80303","uniref90":"UniRef90_P80303","uniref50":"UniRef50_P80303","genes":[{"name":{"value":"NUCB2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:8044","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8044"}}]},"synonyms":[{"value":"NEFA"}]}],"alphafold_very_low_content":0.09047619047619047,"disorder_content":0.55,"disprot_consensus":{"full":[{"start":190,"end":264,"type":"D"},{"start":265,"end":282,"type":"T"},{"start":283,"end":308,"type":"D"},{"start":309,"end":334,"type":"T"},{"start":335,"end":420,"type":"D"}],"Structural state":[{"start":190,"end":420,"type":"D"}],"Structural transition":[{"start":265,"end":282,"type":"T"},{"start":309,"end":334,"type":"T"}],"Molecular function":[{"start":265,"end":282,"type":"F"},{"start":309,"end":334,"type":"F"}]}},{"disprot_id":"DP03425","acc":"Q7G7J6","creator":"nfarahi","date":"2021-07-12T07:07:08.222Z","features":{"pfam":[{"id":"PF03514","name":"GRAS domain family","start":241,"end":621},{"id":"PF12041","name":"Transcriptional regulator DELLA protein N terminal","start":39,"end":113}],"gene3D":[]},"length":625,"name":"DELLA protein SLR1","ncbi_taxon_id":39947,"organism":"Oryza sativa subsp. japonica","regions":[{"start":28,"end":112,"reference_id":"30531945","reference_source":"pmid","reference_html":"Physical and thermodynamic characterization of the rice gibberellin receptor/gibberellin/DELLA protein complex. <i> Xiang H, Okamura H, Kezuka Y, Katoh E. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03425r001","statement":[{"text":"Furthermore, the results of SAXS, ITC, and gel filtration experiments indicate that when free in solution, SLR1(M28-A112) is a natively unfolded protein. The NMR experiments expand this observation to show that the unfolded mutant also contains a small amount of marginally stable secondary structure. ","type":"Abstract"},{"text":"The 1H-15N HSQC NMR spectrum of free SLR1(M28-A112) is very similar to that expected for a disordered protein (Fig. 5a)","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:22:52.869Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":28,"end":112,"reference_id":"30531945","reference_source":"pmid","reference_html":"Physical and thermodynamic characterization of the rice gibberellin receptor/gibberellin/DELLA protein complex. <i> Xiang H, Okamura H, Kezuka Y, Katoh E. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03425r002","statement":[{"text":"Furthermore, the results of SAXS, ITC, and gel filtration experiments indicate that when free in solution, SLR1(M28-A112) is a natively unfolded protein.","type":"Abstract"},{"text":"The molecular weight of SLR1(M28-A112) is estimated to be 12.9 kDa, which is approximately 1.5-fold larger than the theoretical value (8.9 kDa). Information about molecular shape can be obtained using the entire scattering profile in a Kratky plot. The presence of a peak in a Kratky plot indicates that a protein has a globular shape, while a plateau between 0.1 and 0.3 Å−1 indicates that an unfolded protein exists14. The plots of Fig. S3B clearly indicate that OsGID1/GA3 is globular and that SLR1(M28-A112) is unfolded. The larger than expected Rg value for SLR1(M28-A112), given its MW, is obviously a consequence of an unfolded structure.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:22:53.660Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":28,"end":112,"reference_id":"30531945","reference_source":"pmid","reference_html":"Physical and thermodynamic characterization of the rice gibberellin receptor/gibberellin/DELLA protein complex. <i> Xiang H, Okamura H, Kezuka Y, Katoh E. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03425r003","statement":[{"text":"Furthermore, the results of SAXS, ITC, and gel filtration experiments indicate that when free in solution, SLR1(M28-A112) is a natively unfolded protein.","type":"Abstract"},{"text":"As reported previously, all of the truncated SLR1 mutants elute as proteins of much larger size than would be predicted on the basis of their estimated molecular weights (MWs).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:22:55.325Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":28,"end":112,"reference_id":"30531945","reference_source":"pmid","reference_html":"Physical and thermodynamic characterization of the rice gibberellin receptor/gibberellin/DELLA protein complex. <i> Xiang H, Okamura H, Kezuka Y, Katoh E. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03425r004","statement":[{"text":"We have identified the shortest SLR1 sequence (M28-A112) that binds the rice GID/GA complex tightly. ","type":"Abstract"},{"text":"The ITC results also show that SLR1(M28-A112) is the shortest sequence that can bind OsGID1/GA3 with high affinity.","type":"Results"}],"interaction_partner":[{"db":"UniProt","id":"Q6L545","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:22:48.524Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":28,"end":112,"reference_id":"30531945","reference_source":"pmid","reference_html":"Physical and thermodynamic characterization of the rice gibberellin receptor/gibberellin/DELLA protein complex. <i> Xiang H, Okamura H, Kezuka Y, Katoh E. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03425r005","statement":[{"text":"The 1H-15N HSQC NMR spectrum of free SLR1(M28-A112) is very similar to that expected for a disordered protein (Fig. 5a). Conversely, the cross peaks of the 1H-15N HSQC NMR spectrum of SLR1(M28-A112) acquired when unlabelled OsGID1/GA3 is present are well dispersed (Fig. 5b).","type":"Results"},{"text":"Examination of the values of the SLR1 13Cα chemical shifts of GID1/GA3/SLR1(M28-A112) shows that the 13Cα resonances of the residues of the sequences E39-A44, R50-G69, D81-A88, and L99-E109 shift ca. 3.0–4.0 ppm downfield compared with those of free SLR1(M28-A112). This shift is consistent the formation of α-helices (Fig. 5c). Therefore, while the structure of free SLR1(M28-A112) is mostly disordered, the protein acquires a defined fold when bound to its physiological target, GID1.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:22:50.305Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":28,"end":112,"reference_id":"30531945","reference_source":"pmid","reference_html":"Physical and thermodynamic characterization of the rice gibberellin receptor/gibberellin/DELLA protein complex. <i> Xiang H, Okamura H, Kezuka Y, Katoh E. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03425r006","statement":[{"text":"Taken together, the Rg values, calculated molecular weights, and Kratky plots strongly suggest the following: OsGID1/GA3 and SLR1(M28-A112) form a 1:1 complex with a globular shape; as an isolated species, OsGID1/GA3 has a propensity to dimerize; and SLR1(M28-A112) is a natively unfolded protein.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:22:51.621Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":28,"end":112,"reference_id":"30531945","reference_source":"pmid","reference_html":"Physical and thermodynamic characterization of the rice gibberellin receptor/gibberellin/DELLA protein complex. <i> Xiang H, Okamura H, Kezuka Y, Katoh E. </i> Sci Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03425r007","statement":[{"text":"On the other hand, large positive deviations (ca. 3.0–4.0 ppm) in the 13Cα chemical shifts of the residues of E39-A44, R50-G69, D81-A88, and L99-E109 are observed when SLR1(M28-A112) and OsGID1/GA3 are both present, suggesting that these sequences form α-helices.","type":"Results"}],"interaction_partner":[{"db":"UniProt","id":"Q6L545","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-21T09:22:49.150Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":7,"released":"2023_12","sequence":"MKREYQEAGGSSGGGSSADMGSCKDKVMAGAAGEEEDVDELLAALGYKVRSSDMADVAQKLEQLEMAMGMGGVSAPGAADDGFVSHLATDTVHYNPSDLSSWVESMLSELNAPLPPIPPAPPAARHASTSSTVTGGGGSGFFELPAAADSSSSTYALRPISLPVVATADPSAADSARDTKRMRTGGGSTSSSSSSSSSLGGGASRGSVVEAAPPATQGAAAANAPAVPVVVVDTQEAGIRLVHALLACAEAVQQENFAAAEALVKQIPTLAASQGGAMRKVAAYFGEALARRVYRFRPADSTLLDAAFADLLHAHFYESCPYLKFAHFTANQAILEAFAGCHRVHVVDFGIKQGMQWPALLQALALRPGGPPSFRLTGVGPPQPDETDALQQVGWKLAQFAHTIRVDFQYRGLVAATLADLEPFMLQPEGEADANEEPEVIAVNSVFELHRLLAQPGALEKVLGTVHAVRPRIVTVVEQEANHNSGSFLDRFTESLHYYSTMFDSLEGGSSGQAELSPPAAGGGGGTDQVMSEVYLGRQICNVVACEGAERTERHETLGQWRNRLGRAGFEPVHLGSNAYKQASTLLALFAGGDGYRVEEKEGCLTLGWHTRPLIATSAWRVAAA","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","BOP clade","Oryzoideae","Oryzeae","Oryzinae","Oryza","Oryza sativa"],"UniParc":"UPI00000A5470","uniref100":"UniRef100_Q7G7J6","uniref90":"UniRef90_Q7G7J6","uniref50":"UniRef50_Q7G7J6","genes":[{"name":{"value":"SLR1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11340177","url":"http://www.ncbi.nlm.nih.gov/pubmed/11340177","alternativeUrl":"https://europepmc.org/abstract/MED/11340177"}}]},"synonyms":[{"value":"GAI","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10713441","url":"http://www.ncbi.nlm.nih.gov/pubmed/10713441","alternativeUrl":"https://europepmc.org/abstract/MED/10713441"}}]}],"orfNames":[{"value":"OsJ_12286","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"EEE59780.1","url":"https://www.ebi.ac.uk/ena/browser/view/EEE59780.1"}}]},{"value":"OSJNBb0022E02.5","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAK50137.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAK50137.1"}}]}],"olnNames":[{"value":"Os03g0707600","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"BAF12946.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAF12946.1"}}]},{"value":"LOC_Os03g49990","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"ABF98475.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABF98475.1"}}]}]}],"alphafold_very_low_content":0.3024,"disorder_content":0.136,"disprot_consensus":{"full":[{"start":28,"end":112,"type":"T"}],"Structural state":[{"start":28,"end":112,"type":"D"}],"Molecular function":[{"start":28,"end":112,"type":"F"}],"Structural transition":[{"start":28,"end":112,"type":"T"}]}},{"disprot_id":"DP03426","acc":"P25024","creator":"nfarahi","date":"2021-07-13T11:07:09.633Z","features":{"pfam":[{"id":"PF00001","name":"7 transmembrane receptor (rhodopsin family)","start":56,"end":305}],"gene3D":[]},"length":350,"name":"C-X-C chemokine receptor type 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":28,"reference_id":"23086146","reference_source":"pmid","reference_html":"Structure of the chemokine receptor CXCR1 in phospholipid bilayers. <i> Park SH, Das BB, Casagrande F, Tian Y, Nothnagel HJ, Chu M, Kiefer H, Maier K, De Angelis AA, Marassi FM, Opella SJ. </i> Nature, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2LNL"},{"db":"BMRB","id":"18170"}],"region_id":"DP03426r001","statement":[{"text":"Overall, 97% of the backbone resonances for residues 20 to 325 were assigned. The missing resonances are from seven Pro (P22, P93, P170, P180, P185, P214, P257) and one Arg (R285). None of the 15N and 13C signals from the mobile N-and C-termini (residues 1-19 and 326-350) could be detected in the spectra, consistent with our observation of these signals in solid-state NMR experiments designed to detect only signals from mobile sites (Supplementary Fig. 6), as well as our previous analysis of local and global motions of CXCR124.","type":"Article"},{"text":"Supplementary Figure 6. One-dimensional refocused INEPT solid-state NMR MAS spectra of CXCR1 in proteoliposomes. Only\nsignals from mobile sites in the termini are detected.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-29T06:49:15.088Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":326,"end":350,"reference_id":"23086146","reference_source":"pmid","reference_html":"Structure of the chemokine receptor CXCR1 in phospholipid bilayers. <i> Park SH, Das BB, Casagrande F, Tian Y, Nothnagel HJ, Chu M, Kiefer H, Maier K, De Angelis AA, Marassi FM, Opella SJ. </i> Nature, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2LNL"},{"db":"BMRB","id":"18170"}],"region_id":"DP03426r002","statement":[{"text":"Overall, 97% of the backbone resonances for residues 20 to 325 were assigned. The missing resonances are from seven Pro (P22, P93, P170, P180, P185, P214, P257) and one Arg (R285). None of the 15N and 13C signals from the mobile N-and C-termini (residues 1-19 and 326-350) could be detected in the spectra, consistent with our observation of these signals in solid-state NMR experiments designed to detect only signals from mobile sites (Supplementary Fig. 6), as well as our previous analysis of local and global motions of CXCR124.","type":"Article"},{"text":"Supplementary Figure 6. One-dimensional refocused INEPT solid-state NMR MAS spectra of CXCR1 in proteoliposomes. Only\nsignals from mobile sites in the termini are detected.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-29T06:49:12.866Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":29,"reference_id":"30384436","reference_source":"pmid","reference_html":"Dynamics-Derived Insights into Complex Formation between the CXCL8 Monomer and CXCR1 N-Terminal Domain: An NMR Study. <i> Joseph PRB, Spyracopoulos L, Rajarathnam K. </i> Molecules, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03426r003","statement":[{"text":"The CXCR1 N-domain is unstructured in the free state but structured with significant dynamics in the bound state.","type":"Abstract"},{"text":"The relaxation data for the bound state indicate that the CXCR1 N-domain is structured, with distinct differences in dynamic properties at a residue-specific level (Figure 11).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T10:27:55.929Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":1,"end":29,"reference_id":"30384436","reference_source":"pmid","reference_html":"Dynamics-Derived Insights into Complex Formation between the CXCL8 Monomer and CXCR1 N-Terminal Domain: An NMR Study. <i> Joseph PRB, Spyracopoulos L, Rajarathnam K. </i> Molecules, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03426r004","statement":[{"text":"In the unbound state, negative hetNOEs for all residues indicate that the CXCR1 N-domain is unstructured (Figure 10).","type":"Results"},{"text":"Chemical shifts are also characteristic of an unstructured peptide.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-27T10:31:55.140Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":29,"reference_id":"30384436","reference_source":"pmid","reference_html":"Dynamics-Derived Insights into Complex Formation between the CXCL8 Monomer and CXCR1 N-Terminal Domain: An NMR Study. <i> Joseph PRB, Spyracopoulos L, Rajarathnam K. </i> Molecules, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P10145","partner_start":null,"partner_end":null}],"region_id":"DP03426r006","statement":[{"text":"The chemical shift perturbation profile of the CXCL8 (1–66) monomer upon CXCR1 N-domain 29mer binding is shown in Figure 2.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-29T06:49:26.782Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":29,"reference_id":"30384436","reference_source":"pmid","reference_html":"Dynamics-Derived Insights into Complex Formation between the CXCL8 Monomer and CXCR1 N-Terminal Domain: An NMR Study. <i> Joseph PRB, Spyracopoulos L, Rajarathnam K. </i> Molecules, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P10145","partner_start":null,"partner_end":null}],"region_id":"DP03426r007","statement":[{"text":"Isothermal titration calorimetry (ITC) measures binding-induced heat changes from which free energy of binding (∆G), enthalpy (∆H), entropy (∆S), and stoichiometry (n) can be obtained in a straightforward manner [60]. The binding isotherm of the CXCR1 N-domain binding to the CXCL8 monomer is shown in Figure 12. The data fit best to a single-binding site model, yielding a stoichiometry of 0.93 ± 0.03, KD = 8.4 ± 0.5 μM, ΔH = −2.6 ± 0.2 kcal/mol, and T∆S = −4.3 ± 0.2 kcal/mol, indicating both enthalpic and entropic factors promote binding.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-29T06:49:23.858Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":7,"released":"2021_12","sequence":"MSNITDPQMWDFDDLNFTGMPPADEDYSPCMLETETLNKYVVIIAYALVFLLSLLGNSLVMLVILYSRVGRSVTDVYLLNLALADLLFALTLPIWAASKVNGWIFGTFLCKVVSLLKEVNFYSGILLLACISVDRYLAIVHATRTLTQKRHLVKFVCLGCWGLSMNLSLPFFLFRQAYHPNNSSPVCYEVLGNDTAKWRMVLRILPHTFGFIVPLFVMLFCYGFTLRTLFKAHMGQKHRAMRVIFAVVLIFLLCWLPYNLVLLADTLMRTQVIQESCERRNNIGRALDATEILGFLHSCLNPIIYAFIGQNFRHGFLKILAMHGLVSKEFLARHRVTSYTSSSVNVSSNL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000043589","uniref100":"UniRef100_P25024","uniref90":"UniRef90_P25024","uniref50":"UniRef50_P35407","genes":[{"name":{"value":"CXCR1"},"synonyms":[{"value":"CMKAR1"},{"value":"IL8RA"}]}],"alphafold_very_low_content":0.1,"disorder_content":0.15428571428571428,"disprot_consensus":{"full":[{"start":1,"end":29,"type":"T"},{"start":326,"end":350,"type":"D"}],"Structural state":[{"start":1,"end":29,"type":"D"},{"start":326,"end":350,"type":"D"}],"Structural transition":[{"start":1,"end":29,"type":"T"}],"Molecular function":[{"start":1,"end":29,"type":"F"}]}},{"disprot_id":"DP03427","acc":"P31327","creator":"mlmarques","date":"2021-07-14T21:32:14.455Z","features":{"pfam":[{"id":"PF00117","name":"Glutamine amidotransferase class-I","start":222,"end":395},{"id":"PF00988","name":"Carbamoyl-phosphate synthase small chain, CPSase domain","start":48,"end":183},{"id":"PF02142","name":"MGS-like domain","start":1375,"end":1465},{"id":"PF02786","name":"Carbamoyl-phosphate synthase L chain, ATP binding domain","start":546,"end":749},{"id":"PF02786","name":"Carbamoyl-phosphate synthase L chain, ATP binding domain","start":1088,"end":1290},{"id":"PF02787","name":"Carbamoyl-phosphate synthetase large chain, oligomerisation domain","start":797,"end":934},{"id":"PF25596","name":"Carbamoyl phosphate synthase preATP-grasp domain","start":423,"end":542},{"id":"PF25596","name":"Carbamoyl phosphate synthase preATP-grasp domain","start":973,"end":1084}],"gene3D":[]},"length":1500,"name":"Carbamoyl-phosphate synthase [ammonia], mitochondrial","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":779,"end":792,"reference_id":"26592762","reference_source":"pmid","reference_html":"Structure of human carbamoyl phosphate synthetase: deciphering the on/off switch of human ureagenesis. <i> de Cima S, Polo LM, Díez-Fernández C, Martínez AI, Cervera J, Fita I, Rubio V. </i> Sci Rep, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"5DOT"}],"region_id":"DP03427r001","statement":[{"text":"In contrast, in the case of the L1 domain there are ~90 residues that are disordered (and thus that are not seen) in the apo form and that become ordered when the enzyme has the ligands bound to it (Fig. 1c, top panels).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-20T10:09:23.417Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":562,"end":623,"reference_id":"26592762","reference_source":"pmid","reference_html":"Structure of human carbamoyl phosphate synthetase: deciphering the on/off switch of human ureagenesis. <i> de Cima S, Polo LM, Díez-Fernández C, Martínez AI, Cervera J, Fita I, Rubio V. </i> Sci Rep, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"5DOU"},{"db":"PDB","id":"5DOT"}],"region_id":"DP03427r002","statement":[{"text":"Region 562-623 is disordered in the crystal structure of the apo form (PDB:5dot) and becomes ordered upon ligand binding (PDB:5dou).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-20T10:09:26.910Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":779,"end":784,"reference_id":"26592762","reference_source":"pmid","reference_html":"Structure of human carbamoyl phosphate synthetase: deciphering the on/off switch of human ureagenesis. <i> de Cima S, Polo LM, Díez-Fernández C, Martínez AI, Cervera J, Fita I, Rubio V. </i> Sci Rep, 2015","date":"2022-12-06T11:23:40.330Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0030955","term_name":"potassium ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":2,"region_id":"DP03427r003","statement":[{"text":"Residues D779,F781,H782,T784 coordinate the binding of the potassium ion.","type":"Curator statement"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a potassium ion (K+).\" [GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-21T14:47:54.605Z"}},{"start":788,"end":792,"reference_id":"26592762","reference_source":"pmid","reference_html":"Structure of human carbamoyl phosphate synthetase: deciphering the on/off switch of human ureagenesis. <i> de Cima S, Polo LM, Díez-Fernández C, Martínez AI, Cervera J, Fita I, Rubio V. </i> Sci Rep, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0036094","term_name":"small molecule binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"ChEBI","id":"16761","partner_start":null,"partner_end":null}],"region_id":"DP03427r004","statement":[{"text":"Residue S790 coordinates the binding of ADP.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-20T10:09:53.134Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":585,"end":623,"reference_id":"26592762","reference_source":"pmid","reference_html":"Structure of human carbamoyl phosphate synthetase: deciphering the on/off switch of human ureagenesis. <i> de Cima S, Polo LM, Díez-Fernández C, Martínez AI, Cervera J, Fita I, Rubio V. </i> Sci Rep, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0036094","term_name":"small molecule binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"ChEBI","id":"16761","partner_start":null,"partner_end":null}],"region_id":"DP03427r005","statement":[{"text":"Residues M585,R587,L592,G593,G594,G623 coordinate the binding of ADP.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-20T10:09:36.859Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":779,"end":784,"reference_id":"26592762","reference_source":"pmid","reference_html":"Structure of human carbamoyl phosphate synthetase: deciphering the on/off switch of human ureagenesis. <i> de Cima S, Polo LM, Díez-Fernández C, Martínez AI, Cervera J, Fita I, Rubio V. </i> Sci Rep, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"ChEBI","id":"29103","partner_start":null,"partner_end":null}],"region_id":"DP03427r006","statement":[{"text":"Residues D779,F781,H782,T784 coordinate the binding of the potassium ion.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-20T10:09:30.969Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":779,"end":792,"reference_id":"26592762","reference_source":"pmid","reference_html":"Structure of human carbamoyl phosphate synthetase: deciphering the on/off switch of human ureagenesis. <i> de Cima S, Polo LM, Díez-Fernández C, Martínez AI, Cervera J, Fita I, Rubio V. </i> Sci Rep, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03427r007","statement":[{"text":"In contrast, in the case of the L1 domain there are ~90 residues that are disordered (and thus that are not seen) in the apo form and that become ordered when the enzyme has the ligands bound to it (Fig. 1c, top panels).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-20T10:09:25.321Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":562,"end":623,"reference_id":"26592762","reference_source":"pmid","reference_html":"Structure of human carbamoyl phosphate synthetase: deciphering the on/off switch of human ureagenesis. <i> de Cima S, Polo LM, Díez-Fernández C, Martínez AI, Cervera J, Fita I, Rubio V. </i> Sci Rep, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03427r008","statement":[{"text":"Region 562-623 is disordered in the crystal structure of the apo form (PDB:5dot) and becomes ordered upon ligand binding (PDB:5dou).","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"5DOT"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-20T10:09:22.353Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":8,"released":"2021_12","sequence":"MTRILTAFKVVRTLKTGFGFTNVTAHQKWKFSRPGIRLLSVKAQTAHIVLEDGTKMKGYSFGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDTTALDELGLSKYLESNGIKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTMLGKIEFEGQPVDFVDPNKQNLIAEVSTKDVKVYGKGNPTKVVAVDCGIKNNVIRLLVKRGAEVHLVPWNHDFTKMEYDGILIAGGPGNPALAEPLIQNVRKILESDRKEPLFGISTGNLITGLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALDNTLPAGWKPLFVNVNDQTNEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLIKKGKATTITSVLPKPALVASRVEVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEVGLKQADTVYFLPITPQFVTEVIKAEQPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVESIMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAADTIGYPVMIRSAYALGGLGSGICPNRETLMDLSTKAFAMTNQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMGVHTGDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNARLSRSSALASKATGYPLAFIAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDRFHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMCHPSIEGFTPRLPMNKEWPSNLDLRKELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGLNSESMTEETLKRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYVTYNGQEHDVNFDDHGMMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETVSTDFDECDKLYFEELSLERILDIYHQEACGGCIISVGGQIPNNLAVPLYKNGVKIMGTSPLQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSYVLSGSAMNVVFSEDEMKKFLEEATRVSQEHPVVLTKFVEGAREVEMDAVGKDGRVISHAISEHVEDAGVHSGDATLMLPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRASRSFPFVSKTLGVDFIDVATKVMIGENVDEKHLPTLDHPIIPADYVAIKAPMFSWPRLRDADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKGILIGIQQSFRPRFLGVAEQLHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNPSLSSIRKLIRDGSIDLVINLPNNNTKFVHDNYVIRRTAVDSGIPLLTNFQVTKLFAEAVQKSRKVDSKSLFHYRQYSAGKAA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI0000156409","uniref100":"UniRef100_P31327","uniref90":"UniRef90_P31327","uniref50":"UniRef50_P31327","genes":[{"name":{"value":"CPS1"}}],"alphafold_very_low_content":0.03133333333333333,"disorder_content":0.050666666666666665,"disprot_consensus":{"full":[{"start":562,"end":623,"type":"T"},{"start":779,"end":792,"type":"T"}],"Structural state":[{"start":562,"end":623,"type":"D"},{"start":779,"end":792,"type":"D"}],"Structural transition":[{"start":562,"end":623,"type":"T"},{"start":779,"end":792,"type":"T"}],"Molecular function":[{"start":585,"end":623,"type":"F"},{"start":779,"end":784,"type":"F"},{"start":788,"end":792,"type":"F"}]}},{"disprot_id":"DP03428","acc":"P40763","creator":"esalladini","date":"2021-07-19T07:41:07.271Z","features":{"pfam":[{"id":"PF00017","name":"SH2 domain","start":584,"end":651},{"id":"PF01017","name":"STAT transcription factor, coiled-coil domain","start":145,"end":313},{"id":"PF02864","name":"STAT protein, DNA binding domain","start":326,"end":464},{"id":"PF02865","name":"STAT protein, protein interaction domain","start":2,"end":119},{"id":"PF21354","name":"Signal transducer and activator of transcription, linker domain","start":488,"end":565}],"gene3D":[]},"length":770,"name":"Signal transducer and activator of transcription 3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":690,"end":722,"reference_id":"32807795","reference_source":"pmid","reference_html":"Selective inhibition of STAT3 signaling using monobodies targeting the coiled-coil and N-terminal domains. <i> La Sala G, Michiels C, Kükenshöner T, Brandstoetter T, Maurer B, Koide A, Lau K, Pojer F, Koide S, Sexl V, Dumoutier L, Hantschel O. </i> Nat Commun, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6TLC"}],"region_id":"DP03428r001","statement":[{"text":"Even if it is not mentioned in the paper, the 690-722 region was missing from the electron density.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-17T14:45:02.977Z"}},{"start":689,"end":702,"reference_id":"31170499","reference_source":"pmid","reference_html":"Unexpected implications of STAT3 acetylation revealed by genetic encoding of acetyl-lysine. <i> Belo Y, Mielko Z, Nudelman H, Afek A, Ben-David O, Shahar A, Zarivach R, Gordan R, Arbely E. </i> Biochim Biophys Acta Gen Subj, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"6QHD"}],"region_id":"DP03428r002","statement":[{"text":"Within each monomer, electron density map for most of our protein model was well defined, yet as with the crystal structure of pY705 STAT3 (PDB ID: 1BG1)[3], several residues, including loops within the SH2 domain, were poorly defined and consequently were not included in the final model; i.e., the loop connecting α-helices 1 and 2 (185–193), residues 419–427 between β-sheets e and f, a loop at the end of α-helix 7 (536–538), and several residues within the SH2 domain (626–632, 658–665, 689–702; all numbers refer to monomer A).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-17T14:45:03.276Z"}}],"regions_counter":2,"released":"2021_12","sequence":"MAQWNQLQQLDTRYLEQLHQLYSDSFPMELRQFLAPWIESQDWAYAASKESHATLVFHNLLGEIDQQYSRFLQESNVLYQHNLRRIKQFLQSRYLEKPMEIARIVARCLWEESRLLQTAATAAQQGGQANHPTAAVVTEKQQMLEQHLQDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRSIVSELAGLLSAMEYVQKTLTDEELADWKRRQQIACIGGPPNICLDRLENWITSLAESQLQTRQQIKKLEELQQKVSYKGDPIVQHRPMLEERIVELFRNLMKSAFVVERQPCMPMHPDRPLVIKTGVQFTTKVRLLVKFPELNYQLKIKVCIDKDSGDVAALRGSRKFNILGTNTKVMNMEESNNGSLSAEFKHLTLREQRCGNGGRANCDASLIVTEELHLITFETEVYHQGLKIDLETHSLPVVVISNICQMPNAWASILWYNMLTNNPKNVNFFTKPPIGTWDQVAEVLSWQFSSTTKRGLSIEQLTTLAEKLLGPGVNYSGCQITWAKFCKENMAGKGFSFWVWLDNIIDLVKKYILALWNEGYIMGFISKERERAILSTKPPGTFLLRFSESSKEGGVTFTWVEKDISGKTQIQSVEPYTKQQLNNMSFAEIIMGYKIMDATNILVSPLVYLYPDIPKEEAFGKYCRPESQEHPEADPGSAAPYLKTKFICVTPTTCSNTIDLPMSPRTLDSLMQFGNNGEGAEPSAGGQFESLTFDMELTSECATSPM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"UniParc":"UPI00000473FD","uniref100":"UniRef100_P40763","uniref90":"UniRef90_P40763","uniref50":"UniRef50_P40763","genes":[{"name":{"value":"STAT3","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11364","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11364"}}]},"synonyms":[{"value":"APRF","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11364","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11364"}}]}]}],"alphafold_very_low_content":0.1025974025974026,"dataset":["Cancer-related proteins","Condensates-related proteins"],"disorder_content":0.04415584415584416,"disprot_consensus":{"full":[{"start":689,"end":722,"type":"D"}],"Structural state":[{"start":689,"end":722,"type":"D"}]}},{"disprot_id":"DP03429","acc":"P72975","creator":"jssuarez","date":"2021-07-21T09:50:04.202Z","features":{"pfam":[{"id":"PF14105","name":"Domain of unknown function (DUF4278)","start":1,"end":56}],"gene3D":[]},"length":149,"name":"Sll1515 protein","ncbi_taxon_id":1111708,"organism":"Synechocystis sp. (strain PCC 6803 / Kazusa)","regions":[{"start":1,"end":149,"reference_id":"21992216","reference_source":"pmid","reference_html":"The inactivating factor of glutamine synthetase IF17 is an intrinsically disordered protein, which folds upon binding to its target. <i> Saelices L, Galmozzi CV, Florencio FJ, Muro-Pastor MI, Neira JL. </i> Biochemistry, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03429r001","statement":[{"text":"We used far-UV CD in the analysis of the structure and conformational stability of IF17 as a spectroscopic probe that is sensitive to secondary structure.(26, 27) The CD spectrum of IF17, at 25 °C and physiological pH, showed a minimum negative ellipticity at ∼200 nm and a negative shoulder around 222 nm (Figure 1). These results suggest an unfolded protein with a small fraction of α-helix, turn-like, or PPII structures,(28) although the presence of aromatic signals, which also absorb at 222 nm, cannot be ruled out.(27)","type":"Results"},{"text":"The ellipticity of IF17 showed a linear behavior as the temperature was raised (Figure 1C), in agreement with the fluorescence thermal denaturations (see above). This behavior is commonly observed among IDPs, and it is explained as due to a redistribution of the random coil involving a loss of PPII and/or helical conformations.(35)","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-22T15:36:27.759Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":149,"reference_id":"21992216","reference_source":"pmid","reference_html":"The inactivating factor of glutamine synthetase IF17 is an intrinsically disordered protein, which folds upon binding to its target. <i> Saelices L, Galmozzi CV, Florencio FJ, Muro-Pastor MI, Neira JL. </i> Biochemistry, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03429r002","statement":[{"text":"The thermal denaturations of IF17 showed a linear decrease in the fluorescence emission as the temperature was increased (data not shown).","type":"Results"},{"text":"The ellipticity of IF17 showed a linear behavior as the temperature was raised (Figure 1C), in agreement with the fluorescence thermal denaturations (see above). This behavior is commonly observed among IDPs, and it is explained as due to a redistribution of the random coil involving a loss of PPII and/or helical conformations.(35)","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-22T15:36:28.830Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":1,"end":149,"reference_id":"21992216","reference_source":"pmid","reference_html":"The inactivating factor of glutamine synthetase IF17 is an intrinsically disordered protein, which folds upon binding to its target. <i> Saelices L, Galmozzi CV, Florencio FJ, Muro-Pastor MI, Neira JL. </i> Biochemistry, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03429r003","statement":[{"text":"NMR can give information about the general fold of a polypeptide chain in solution at the residue level.(36) The 1D NMR spectrum of IF17 at 25 °C showed a poor chemical shift dispersion: the amide, the aromatic, and the methyl protons (Figure 1D) were clustered in those regions expected for random-coil proteins:(36) namely, between 8.0 and 8.7 ppm (for the amide signals), between 6.8 and 7.3 ppm (for the aromatic protons), and between 0.8 and 1.0 ppm (for the methyl groups).","type":"Results"},{"text":"We also carried out hydrogen-exchange experiments. After 10 min at 20 °C at pH 5.9, all the amide protons of IF17 in the 1D NMR spectrum were exchanged, suggesting the absence of hydrogen bonds.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-22T15:36:29.938Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":149,"reference_id":"21992216","reference_source":"pmid","reference_html":"The inactivating factor of glutamine synthetase IF17 is an intrinsically disordered protein, which folds upon binding to its target. <i> Saelices L, Galmozzi CV, Florencio FJ, Muro-Pastor MI, Neira JL. </i> Biochemistry, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03429r004","statement":[{"text":"Therefore, we decided to determine the R, and the protein oligomerization state of the molecule, from the measurements of the translational diffusion coefficient (D), by DOSY-NMR experiments. The measured D was (7.5 ± 0.1) × 10–7 cm2 s–1, which yields an R = 26 ± 2 Å (with a dioxane D value of (9.3 ± 0.1) × 10–7 cm2 s–1).","type":"Results"},{"text":"The use of the equation for a premolten globule species(37) yields an R value of 29 ± 5 Å, which is similar, within the experimental error, to the measured one. (The R value for a molten globule according to the same equations is 22 ± 8 Å, which is also similar to the experimental value.) These findings suggest that IF17 is a monomer with a molten or premolten globule conformation.","type":"Results"},{"text":"Taken together, these results indicate that the IF17 is more compact than a fully disordered polypeptide chain but is not a fully spherical well-folded globular protein. ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-22T15:36:39.879Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":149,"reference_id":"21992216","reference_source":"pmid","reference_html":"The inactivating factor of glutamine synthetase IF17 is an intrinsically disordered protein, which folds upon binding to its target. <i> Saelices L, Galmozzi CV, Florencio FJ, Muro-Pastor MI, Neira JL. </i> Biochemistry, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03429r005","statement":[{"text":"The far-UV CD spectrum of GS was typical of an α-helical protein, with intense minima at 222 and 208 nm.(11) The addition spectrum obtained by the sum of the spectra of isolated GS and IF17 was different from that of the complex (Figure 3A), thus indicating that there was binding; the same was observed in IF17N/IF7 (Figure 3B). ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-22T15:52:44.060Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":149,"reference_id":"21992216","reference_source":"pmid","reference_html":"The inactivating factor of glutamine synthetase IF17 is an intrinsically disordered protein, which folds upon binding to its target. <i> Saelices L, Galmozzi CV, Florencio FJ, Muro-Pastor MI, Neira JL. </i> Biochemistry, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03429r006","statement":[{"text":"The far-UV CD spectrum of GS was typical of an α-helical protein, with intense minima at 222 and 208 nm.(11) The addition spectrum obtained by the sum of the spectra of isolated GS and IF17 was different from that of the complex (Figure 3A), thus indicating that there was binding; the same was observed in IF17N/IF7 (Figure 3B). ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-22T15:37:45.827Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":149,"reference_id":"21992216","reference_source":"pmid","reference_html":"The inactivating factor of glutamine synthetase IF17 is an intrinsically disordered protein, which folds upon binding to its target. <i> Saelices L, Galmozzi CV, Florencio FJ, Muro-Pastor MI, Neira JL. </i> Biochemistry, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006317","ec_ontology":"ECO","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03429r007","statement":[{"text":"To further confirm binding, we carried out thermal denaturations of GS in the absence and in the presence of the IFs. Binding can be detected by a change in the thermal denaturation midpoint, Tm, of the complex, when compared to that of the isolated GS:(41-43) an increase of the Tm indicates binding of the corresponding IF to the folded state of GS; a decrease of the Tm indicates binding to the unfolded state of GS and/or complex destabilization due to conformational changes. In all the GS–IFs mixtures we observed an increase in the Tm of the complex, either followed by fluorescence or CD (Table 1 and Figure 3C). ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-22T15:52:23.245Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":149,"reference_id":"21992216","reference_source":"pmid","reference_html":"The inactivating factor of glutamine synthetase IF17 is an intrinsically disordered protein, which folds upon binding to its target. <i> Saelices L, Galmozzi CV, Florencio FJ, Muro-Pastor MI, Neira JL. </i> Biochemistry, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006317","ec_ontology":"ECO","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","unpublished":true,"released":"2023_12","version":3,"region_id":"DP03429r008","statement":[{"text":"To further confirm binding, we carried out thermal denaturations of GS in the absence and in the presence of the IFs. Binding can be detected by a change in the thermal denaturation midpoint, Tm, of the complex, when compared to that of the isolated GS:(41-43) an increase of the Tm indicates binding of the corresponding IF to the folded state of GS; a decrease of the Tm indicates binding to the unfolded state of GS and/or complex destabilization due to conformational changes. In all the GS–IFs mixtures we observed an increase in the Tm of the complex, either followed by fluorescence or CD (Table 1 and Figure 3C). ","type":"Results"},{"text":"The Inactivating Factor of Glutamine Synthetase IF17 Is an Intrinsically Disordered Protein, Which Folds upon Binding to Its Target","type":"Title"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-07-22T15:52:44.753Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":8,"released":"2023_12","sequence":"MQLSYRGVKYDYNPPKVETEVLGLAGSYRGLDYRFRRTTTKNVIQPNVNLTYRGVSFNPAQDLQPELYTANKKVEVAAAPSQISFQDRVRARLHSKTQAIKKRQQSLLVRLAEEIGLSGDQAVNSAVRIQGKVLANFRSDYASQGVAMS","taxonomy":["Bacteria","Cyanobacteria","Synechococcales","Merismopediaceae","Synechocystis","unclassified Synechocystis"],"UniParc":"UPI00000C0C61","uniref100":"UniRef100_P72975","uniref90":"UniRef90_P72975","uniref50":"UniRef50_P72975","genes":[{"olnNames":[{"value":"sll1515","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAA16994.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAA16994.1"}}]}]}],"alphafold_very_low_content":0.12080536912751678,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":149,"type":"D"}],"Structural state":[{"start":1,"end":149,"type":"D"}],"Molecular function":[{"start":1,"end":149,"type":"F"}]}},{"disprot_id":"DP03430","acc":"P0AC88","creator":"jnilsson","date":"2021-07-23T12:25:20.656Z","features":{"pfam":[{"id":"PF16363","name":"GDP-mannose 4,6 dehydratase","start":6,"end":346}],"gene3D":[]},"length":373,"name":"GDP-mannose 4,6-dehydratase","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":35,"end":55,"reference_id":"10673432","reference_source":"pmid","reference_html":"Structural and kinetic analysis of Escherichia coli GDP-mannose 4,6 dehydratase provides insights into the enzyme's catalytic mechanism and regulation by GDP-fucose. <i> Somoza JR, Menon S, Schmidt H, Joseph-McCarthy D, Dessen A, Stahl ML, Somers WS, Sullivan FX. </i> Structure, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1DB3"}],"region_id":"DP03430r001","statement":[{"text":"Arg35 is the first residue in a disordered region of the molecule that extends through residue 56.","type":"Results"},{"text":"There were three regions of the structure for which there was no corresponding electron density. These missing regions consisted of residues 35–55, 313–318, and the last 15 residues at the C terminus of the\nenzyme.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-26T14:35:15.198Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":359,"end":372,"reference_id":"10673432","reference_source":"pmid","reference_html":"Structural and kinetic analysis of Escherichia coli GDP-mannose 4,6 dehydratase provides insights into the enzyme's catalytic mechanism and regulation by GDP-fucose. <i> Somoza JR, Menon S, Schmidt H, Joseph-McCarthy D, Dessen A, Stahl ML, Somers WS, Sullivan FX. </i> Structure, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1DB3"}],"region_id":"DP03430r002","statement":[{"text":"There were three regions of the structure for which there was no corresponding electron density. These missing regions consisted of residues 35–55, 313–318, and the last 15 residues at the C terminus of the\nenzyme.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-26T14:35:13.923Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MSKVALITGVTGQDGSYLAEFLLEKGYEVHGIKRRASSFNTERVDHIYQDPHTCNPKFHLHYGDLSDTSNLTRILREVQPDEVYNLGAMSHVAVSFESPEYTADVDAMGTLRLLEAIRFLGLEKKTRFYQASTSELYGLVQEIPQKETTPFYPRSPYAVAKLYAYWITVNYRESYGMYACNGILFNHESPRRGETFVTRKITRAIANIAQGLESCLYLGNMDSLRDWGHAKDYVKMQWMMLQQEQPEDFVIATGVQYSVRQFVEMAAAQLGIKLRFEGTGVEEKGIVVSVTGHDAPGVKPGDVIIAVDPRYFRPAEVETLLGDPTKAHEKLGWKPEITLREMVSEMVANDLEAAKKHSLLKSHGYDVAIALES","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref100":"UniRef100_P0AC90","uniref90":"UniRef90_P0AC90","uniref50":"UniRef50_P0AC90","genes":[{"name":{"value":"gmd","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00955","url":"https://hamap.expasy.org/unirule/MF_00955"}}]},"synonyms":[{"value":"yefA"},{"value":"yefN"}],"olnNames":[{"value":"b2053"},{"value":"JW2038"}]}],"alphafold_very_low_content":0,"disorder_content":0.0938337801608579,"disprot_consensus":{"full":[{"start":35,"end":55,"type":"D"},{"start":359,"end":372,"type":"D"}],"Structural state":[{"start":35,"end":55,"type":"D"},{"start":359,"end":372,"type":"D"}]}},{"disprot_id":"DP03432","acc":"P0DTH5","creator":"esalladini","date":"2021-07-26T07:51:08.178Z","features":{"pfam":[{"id":"PF00693","name":"Thymidine kinase from herpesvirus","start":56,"end":329}],"gene3D":[]},"length":376,"name":"Thymidine kinase","ncbi_taxon_id":10299,"organism":"Human herpesvirus 1 (strain 17)","regions":[{"start":1,"end":45,"reference_id":"15163659","reference_source":"pmid","reference_html":"Biochemical and structural characterization of (South)-methanocarbathymidine that specifically inhibits growth of herpes simplex virus type 1 thymidine kinase-transduced osteosarcoma cells. <i> Schelling P, Claus MT, Johner R, Marquez VE, Schulz GE, Scapozza L. </i> J Biol Chem, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1OF1"}],"region_id":"DP03432r001","statement":[{"text":"Due to a lack of defined density presumably caused by high mobility, some parts of the protein could not be modeled. These comprise residues 1-45, 72-75, 148-152, 266-278, and 375-376 of subunit A and residues 1-45, 148-152, 221-223, 266-273, and 375-376 of subunit B.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-12T13:03:20.886Z"}}],"regions_counter":1,"released":"2021_12","sequence":"MASYPCHQHASAFDQAARSRGHNNRRTALRPRRQQKATEVRLEQKMPTLLRVYIDGPHGMGKTTTTQLLVALGSRDDIVYVPEPMTYWRVLGASETIANIYTTQHRLDQGEISAGDAAVVMTSAQITMGMPYAVTDAVLAPHIGGEAGSSHAPPPALTLIFDRHPIAALLCYPAARYLMGSMTPQAVLAFVALIPPTLPGTNIVLGALPEDRHIDRLAKRQRPGERLDLAMLAAIRRVYGLLANTVRYLQGGGSWREDWGQLSGAAVPPQGAEPQSNAGPRPHIGDTLFTLFRAPELLAPNGDLYNVFAWALDVLAKRLRPMHVFILDYDQSPAGCRDALLQLTSGMVQTHVTTPGSIPTICDLARTFAREMGEAN","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Peploviricota","Herviviricetes","Herpesvirales","Herpesviridae","Alphaherpesvirinae","Simplexvirus"],"uniref100":"UniRef100_P0DTH5","uniref90":"UniRef90_Q9QNF7","uniref50":"UniRef50_Q9QNF7","dataset":["Viral proteins"],"genes":[{"name":{"value":"TK","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04029","url":"https://hamap.expasy.org/unirule/MF_04029"}}]},"olnNames":[{"value":"UL23"}]}],"disorder_content":0.1196808510638298,"disprot_consensus":{"full":[{"start":1,"end":45,"type":"D"}],"Structural state":[{"start":1,"end":45,"type":"D"}]}},{"disprot_id":"DP03433","acc":"Q13153","creator":"eleonardi","date":"2021-07-26T08:49:02.048Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":270,"end":521},{"id":"PF00786","name":"P21-Rho-binding domain","start":74,"end":132}],"gene3D":[]},"length":545,"name":"Serine/threonine-protein kinase PAK 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":492,"end":545,"reference_id":"11438672","reference_source":"pmid","reference_html":"Conformational switch and role of phosphorylation in PAK activation. <i> Buchwald G, Hostinova E, Rudolph MG, Kraemer A, Sickmann A, Meyer HE, Scheffzek K, Wittinghofer A. </i> Mol Cell Biol, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03433r001","statement":[{"text":" In the case of chymotrypsin, however, two proteolysis-resistant, stable fragments are obtained ​(Fig.4). By mass spectrometric analysis and N-terminal sequencing, these fragments can be identified as the N-terminal residues 57 to 200 and the C-terminal residues 201 to 491 from αPAK, which we call the RD and CD, respectively ​(Fig.1).","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T14:47:50.268Z"}},{"start":1,"end":56,"reference_id":"11438672","reference_source":"pmid","reference_html":"Conformational switch and role of phosphorylation in PAK activation. <i> Buchwald G, Hostinova E, Rudolph MG, Kraemer A, Sickmann A, Meyer HE, Scheffzek K, Wittinghofer A. </i> Mol Cell Biol, 2001","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03433r002","statement":[{"text":" In the case of chymotrypsin, however, two proteolysis-resistant, stable fragments are obtained ​(Fig.4). By mass spectrometric analysis and N-terminal sequencing, these fragments can be identified as the N-terminal residues 57 to 200 and the C-terminal residues 201 to 491 from αPAK, which we call the RD and CD, respectively ​(Fig.1).","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T14:47:50.513Z"}},{"start":186,"end":199,"reference_id":"16101281","reference_source":"pmid","reference_html":"Structural analysis of the SH3 domain of beta-PIX and its interaction with alpha-p21 activated kinase (PAK). <i> Mott HR, Nietlispach D, Evetts KA, Owen D. </i> Biochemistry, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"cross_refs":[{"db":"PDB","id":"1ZSG"}],"interaction_partner":[{"db":"UniProt","id":"Q14155","partner_start":null,"partner_end":null}],"region_id":"DP03433r004","statement":[{"text":"Resonances corresponding to residues 195-198 had\nlarger line widths than the rest of the peptide. These residues\nare likely to be undergoing conformational exchange on a\nmillisecond to microsecond time scale","type":"Results"},{"text":"We have determined\nthe structure of the PIX-SH3/PAK peptide complex and shown that it differs from typical Src-like SH3/\npeptide complexes","type":"Abstract"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-16T15:04:39.528Z"}},{"start":150,"end":248,"reference_id":"10975528","reference_source":"pmid","reference_html":"Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch. <i> Lei M, Lu W, Meng W, Parrini MC, Eck MJ, Mayer BJ, Harrison SC. </i> Cell, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03433r010","statement":[{"text":"The hydrodynamic radius of the PAK1(70–545) dimer is significantly larger than that of the four-chain complex, probably because residues 150–248 are in an extended, flexible loop with measurable frictional drag.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T15:20:08.181Z"}},{"start":83,"end":137,"reference_id":"21888918","reference_source":"pmid","reference_html":"Redesign of the PAK1 autoinhibitory domain for enhanced stability and affinity in biosensor applications. <i> Jha RK, Wu YI, Zawistowski JS, MacNevin C, Hahn KM, Kuhlman B. </i> J Mol Biol, 2011","date":"2023-05-09T15:04:51.572Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":3,"region_id":"DP03433r012","statement":[{"text":"We expressed and purified residues 83–137 of PAK1 (WT_IS), which in the crystal structure of autoinhibited PAK1 interact with the C lobe of PAK1 kinase domain and form a small folded domain with three helices and a β-strand (Fig. 1). We did not include residues 138–149 of PAK1, which bind in the active site of the kinase. The circular dichroism spectrum of the purified IS domain showed that the domain does not fold in isolation (Fig. 2).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-09T15:42:38.707Z"}},{"start":83,"end":137,"reference_id":"21888918","reference_source":"pmid","reference_html":"Redesign of the PAK1 autoinhibitory domain for enhanced stability and affinity in biosensor applications. <i> Jha RK, Wu YI, Zawistowski JS, MacNevin C, Hahn KM, Kuhlman B. </i> J Mol Biol, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03433r013","statement":[{"text":"Not surprisingly, the domain was prone to aggregation and proteolysis during expression and purification.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T14:31:52.376Z"}},{"start":47,"end":51,"reference_id":"31391252","reference_source":"pmid","reference_html":"The subcellular localization of type I p21-activated kinases is controlled by the disordered variable region and polybasic sequences. <i> Sun X, Su VL, Calderwood DA. </i> J Biol Chem, 2019","date":"2023-05-09T15:04:22.423Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_06","version":4,"region_id":"DP03433r014","statement":[{"text":"We subsequently mutated the four lysines (residue numbers 48–51) in the polybasic stretch of PAK1(1–107) to alanines to investigate the importance of the polybasic motif. Whereas GFP-PAK(1–107) targets robustly to cell–cell contacts, when the lysines are mutated to alanines, targeting is abolished (Fig. 6, E, H, and I), supporting the importance of the polybasic region for targeting.","type":"Results"}],"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-09T15:42:55.792Z"}},{"start":150,"end":248,"reference_id":"10975528","reference_source":"pmid","reference_html":"Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch. <i> Lei M, Lu W, Meng W, Parrini MC, Eck MJ, Mayer BJ, Harrison SC. </i> Cell, 2000","date":"2023-05-09T15:38:46.191Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP03433r017","statement":[{"text":"(A) Gel filtration profiles on Superdex200 (Pharmacia) for PAK1(70–545) and for PAK1(70–149) plus PAK1(249–545). Elution positions for three calibration standards are shown. Pak70-C elutes at a position corresponding to a relative molecular mass of 160 kDa, larger than the expected dimer mass of 110 kDa, probably due to an extended loop formed by residues 150–248.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-09T15:42:36.505Z"}},{"start":182,"end":203,"reference_id":"9659915","reference_source":"pmid","reference_html":"PAK kinases are directly coupled to the PIX family of nucleotide exchange factors. <i> Manser E, Loo TH, Koh CG, Zhao ZS, Chen XQ, Tan L, Tan I, Leung T, Lim L. </i> Mol Cell, 1998","date":"2023-06-16T14:55:28.246Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","region_id":"DP03433r018","statement":[{"text":"Because sequences surrounding a proline-rich motif in PAK155–207 were conserved in various PAKs (Figure 1D) and SH3 domains were present in the p78-like proteins encoded by cDNA clones (see next section), we tested a 22 residue polypeptide (αPAK182–203) containing the proline-rich core sequence for its binding ability (Figure 1C, right panel). This polypeptide bound the triplet of proteins (arrows) equally well as the larger αPAK1–250.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":18,"released":"2021_12","sequence":"MSNNGLDIQDKPPAPPMRNTSTMIGAGSKDAGTLNHGSKPLPPNPEEKKKKDRFYRSILPGDKTNKKKEKERPEISLPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQKKNPQAVLDVLEFYNSKKTSNSQKYMSFTDKSAEDYNSSNALNVKAVSETPAVPPVSEDEDDDDDDATPPPVIAPRPEHTKSVYTRSVIEPLPVTPTRDVATSPISPTENNTTPPDALTRNTEKQKKKPKMSDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATKNNH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref100":"UniRef100_Q13153","uniref90":"UniRef90_Q13153","uniref50":"UniRef50_Q13153","genes":[{"name":{"value":"PAK1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:8590","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8590"}}]}}],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.30825688073394497,"disorder_content":0.48440366972477067,"disprot_consensus":{"full":[{"start":1,"end":56,"type":"D"},{"start":83,"end":137,"type":"D"},{"start":150,"end":248,"type":"D"},{"start":492,"end":545,"type":"D"}],"Structural state":[{"start":1,"end":56,"type":"D"},{"start":83,"end":137,"type":"D"},{"start":150,"end":248,"type":"D"},{"start":492,"end":545,"type":"D"}],"Molecular function":[{"start":182,"end":203,"type":"F"}],"Disorder function":[{"start":150,"end":248,"type":"F"}],"Biological process":[{"start":47,"end":51,"type":"F"}]}},{"disprot_id":"DP03434","acc":"Q8I295","creator":"esalladini","date":"2021-07-26T10:55:07.214Z","features":{"pfam":[{"id":"PF02401","name":"LytB protein","start":223,"end":498}],"gene3D":[]},"length":535,"name":"4-hydroxy-3-methylbut-2-enyl diphosphate reductase, apicoplast","ncbi_taxon_id":36329,"organism":"Plasmodium falciparum (isolate 3D7)","regions":[{"start":1,"end":217,"reference_id":"24188825","reference_source":"pmid","reference_html":"Structure of the (E)-4-hydroxy-3-methyl-but-2-enyl-diphosphate reductase from Plasmodium falciparum. <i> Rekittke I, Olkhova E, Wiesner J, Demmer U, Warkentin E, Jomaa H, Ermler U. </i> FEBS Lett, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4N7B"}],"region_id":"DP03434r001","statement":[{"text":"The N-terminal region (1-217) is missing even if not mentioned in the article.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T13:45:13.591Z"}}],"regions_counter":1,"released":"2021_12","sequence":"MSVTTFCSLKKTDKCNIYISKRAFSVFLFYLFFFLFFHFYFLCSSSFAVIIHESEKRKNIMRRKRSILQIFENSIKSKEGKCNFTKRYITHYYNIPLKIKKHDLPSVIKYFSHKPNGKHNYVTNMITQKNRKSFLFFFFLYNKYFFGKQEQIRKMNYHEEMNKINIKNDGNRKIYMYPKNDIHEEDGDHKNDVEINQKRNEQNCKSFNDEKNENARDPNKILYLINPRGFCKGVSRAIETVEECLKLFKPPIYVKHKIVHNDIVCKKLEKEGAIFIEDLNDVPDGHILIYSAHGISPQIREIAKKKKLIEIDATCPLVNKVHVYVQMKAKENYDIILIGYKNHVEVIGTYNEAPHCTHIVENVNDVDKLNFPLNKKLFYVTQTTLSMDDCALIVQKLKNKFPHIETIPSGSICYATTNRQTALNKICTKCDLTIVVGSSSSSNAKKLVYSSQIRNVPAVLLNTVHDLDQQILKNVNKIALTSAASTPEQETQKFVNLLTNPPFNYTLQNFDGAHENVPKWKLPKNLLHMIKEREK","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"uniref100":"UniRef100_Q8I295","uniref90":"UniRef90_Q8I295","uniref50":"UniRef50_Q8I295","genes":[{"name":{"value":"LytB","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16289098","url":"http://www.ncbi.nlm.nih.gov/pubmed/16289098","alternativeUrl":"https://europepmc.org/abstract/MED/16289098"}}]},"synonyms":[{"value":"IspH","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16289098","url":"http://www.ncbi.nlm.nih.gov/pubmed/16289098","alternativeUrl":"https://europepmc.org/abstract/MED/16289098"}}]}],"orfNames":[{"value":"PF3D7_0104400","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"CAD49005.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAD49005.1"}}]}]}],"alphafold_very_low_content":0.37009345794392523,"disorder_content":0.405607476635514,"disprot_consensus":{"full":[{"start":1,"end":217,"type":"D"}],"Structural state":[{"start":1,"end":217,"type":"D"}]}},{"disprot_id":"DP03435","acc":"P21109","creator":"nfarahi","date":"2021-07-26T12:29:55.764Z","features":{"pfam":[{"id":"PF00001","name":"7 transmembrane receptor (rhodopsin family)","start":61,"end":310}],"gene3D":[]},"length":355,"name":"C-X-C chemokine receptor type 1","ncbi_taxon_id":9986,"organism":"Oryctolagus cuniculus","regions":[{"start":11,"end":44,"reference_id":"17222184","reference_source":"pmid","reference_html":"Thermodynamic characterization of interleukin-8 monomer binding to CXCR1 receptor N-terminal domain. <i> Fernando H, Nagle GT, Rajarathnam K. </i> FEBS J, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03435r001","statement":[{"text":"On the other hand, our CD data show that the CXCR1 N-domain is unstructured in the free form, and relatively more structured in the bound form (Fig. 5). The N-domain peptide in the free form shows a minimum at 199 nm, which is characteristic of random coil structure, and on binding, the minimum is shifted to ≈ 203 nm and also shows a new peak at ≈ 220 nm.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-26T14:12:32.247Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":11,"end":44,"reference_id":"17222184","reference_source":"pmid","reference_html":"Thermodynamic characterization of interleukin-8 monomer binding to CXCR1 receptor N-terminal domain. <i> Fernando H, Nagle GT, Rajarathnam K. </i> FEBS J, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03435r002","statement":[{"text":"On the other hand, our CD data show that the CXCR1 N-domain is unstructured in the free form, and relatively more structured in the bound form (Fig. 5). The N-domain peptide in the free form shows a minimum at 199 nm, which is characteristic of random coil structure, and on binding, the minimum is shifted to ≈ 203 nm and also shows a new peak at ≈ 220 nm.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-26T14:12:33.609Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":11,"end":44,"reference_id":"17222184","reference_source":"pmid","reference_html":"Thermodynamic characterization of interleukin-8 monomer binding to CXCR1 receptor N-terminal domain. <i> Fernando H, Nagle GT, Rajarathnam K. </i> FEBS J, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"nfarahi","curator_name":"Nazanin Farahi","curator_orcid":"0000-0002-6834-8578","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"interaction_partner":[{"db":"UniProt","id":"P10145","partner_start":null,"partner_end":null}],"region_id":"DP03435r003","statement":[{"text":"On the other hand, our CD data show that the CXCR1 N-domain is unstructured in the free form, and relatively more structured in the bound form (Fig. 5). The N-domain peptide in the free form shows a minimum at 199 nm, which is characteristic of random coil structure, and on binding, the minimum is shifted to ≈ 203 nm and also shows a new peak at ≈ 220 nm.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-26T14:12:34.844Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":3,"released":"2021_12","sequence":"MEVNVWNMTDLWTWFEDEFANATGMPPVEKDYSPCLVVTQTLNKYVVVVIYALVFLLSLLGNSLVMLVILYSRSNRSVTDVYLLNLAMADLLFALTMPIWAVSKEKGWIFGTPLCKVVSLVKEVNFYSGILLLACISVDRYLAIVHATRTLTQKRHLVKFICLGIWALSLILSLPFFLFRQVFSPNNSSPVCYEDLGHNTAKWRMVLRILPHTFGFILPLLVMLFCYGFTLRTLFQAHMGQKHRAMRVIFAVVLIFLLCWLPYNLVLLADTLMRTHVIQETCQRRNDIDRALDATEILGFLHSCLNPIIYAFIGQNFRNGFLKMLAARGLISKEFLTRHRVTSYTSSSTNVPSNL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Lagomorpha","Leporidae","Oryctolagus"],"uniref100":"UniRef100_P21109","uniref90":"UniRef90_P21109","uniref50":"UniRef50_P35407","genes":[{"name":{"value":"CXCR1"},"synonyms":[{"value":"IL8RA"}]}],"alphafold_very_low_content":0.04507042253521127,"disorder_content":0.09577464788732394,"disprot_consensus":{"full":[{"start":11,"end":44,"type":"T"}],"Structural state":[{"start":11,"end":44,"type":"D"}],"Structural transition":[{"start":11,"end":44,"type":"T"}],"Molecular function":[{"start":11,"end":44,"type":"F"}]}},{"disprot_id":"DP03438","acc":"P32131","creator":"jnilsson","date":"2021-07-26T13:49:32.385Z","features":{"pfam":[{"id":"PF04055","name":"Radical SAM superfamily","start":56,"end":227},{"id":"PF06969","name":"HemN C-terminal domain","start":363,"end":432}],"gene3D":[]},"length":457,"name":"Oxygen-independent coproporphyrinogen III oxidase","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":445,"end":457,"reference_id":"14633981","reference_source":"pmid","reference_html":"Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymes. <i> Layer G, Moser J, Heinz DW, Jahn D, Schubert WD. </i> EMBO J, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"1OLT"}],"region_id":"DP03438r001","statement":[{"text":" Overall, 439 of 457 residues have been located in the electron density\nmap. Disordered regions of the polypeptide not included in the final model include the residues 1-3, 19-21 and 446-457.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-28T09:55:34.425Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_12","sequence":"MSVQQIDWDLALIQKYNYSGPRYTSYPTALEFSEDFGEQAFLQAVARYPERPLSLYVHIPFCHKLCYFCGCNKIVTRQQHKADQYLDALEQEIVHRAPLFAGRHVSQLHWGGGTPTYLNKAQISRLMKLLRENFQFNADAEISIEVDPREIELDVLDHLRAEGFNRLSMGVQDFNKEVQRLVNREQDEEFIFALLNHAREIGFTSTNIDLIYGLPKQTPESFAFTLKRVAELNPDRLSVFNYAHLPTIFAAQRKIKDADLPSPQQKLDILQETIAFLTQSGYQFIGMDHFARPDDELAVAQREGVLHRNFQGYTTQGDTDLLGMGVSAISMIGDCYAQNQKELKQYYQQVDEQGNALWRGIALTRDDCIRRDVIKSLICNFRLDYAPIEKQWDLHFADYFAEDLKLLAPLAKDGLVDVDEKGIQVTAKGRLLIRNICMCFDTYLRQKARMQQFSRVI","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref100":"UniRef100_P32131","uniref90":"UniRef90_P32131","uniref50":"UniRef50_P32131","genes":[{"name":{"value":"hemN"},"synonyms":[{"value":"yihJ"}],"olnNames":[{"value":"b3867"},{"value":"JW3838"}]}],"alphafold_very_low_content":0.010940919037199124,"disorder_content":0.028446389496717725,"disprot_consensus":{"full":[{"start":445,"end":457,"type":"D"}],"Structural state":[{"start":445,"end":457,"type":"D"}]}},{"disprot_id":"DP03439","acc":"P28327","creator":"esalladini","date":"2021-07-27T12:17:01.477Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":190,"end":440},{"id":"PF00615","name":"Regulator of G protein signaling domain","start":58,"end":171}],"gene3D":[]},"length":561,"name":"Rhodopsin kinase GRK1","ncbi_taxon_id":9913,"organism":"Bos taurus","regions":[{"start":25,"end":181,"reference_id":"34262173","reference_source":"pmid","reference_html":"Structures of rhodopsin in complex with G-protein-coupled receptor kinase 1. <i> Chen Q, Plasencia M, Li Z, Mukherjee S, Patra D, Chen CL, Klose T, Yao XQ, Kossiakoff AA, Chang L, Andrews PC, Tesmer JJG. </i> Nature, 2021","date":"2023-07-17T15:14:27.071Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":3,"cross_refs":[{"db":"PDB","id":"7MT9"},{"db":"EMDB","id":"23978"}],"region_id":"DP03439r001","statement":[{"text":" In our current model, the αN helix of GRK1 is intrinsically disordered until it binds to activated GPCRs in a form of “molecular fly-casting”44 (Fig. 5).","type":"Discussion"},{"text":"a) Primary structure of C-terminally truncated bovine GRK1 (residues 1–535) used in this study and its crystal structure in complex with ATP (PDB entry 3C4W45), wherein the N-terminus is disordered and the AST loop is partially ordered.","type":"Figure"}],"ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02699"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:14978"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:638015"}]},{"start":475,"end":493,"reference_id":"18339619","reference_source":"pmid","reference_html":"Structures of rhodopsin kinase in different ligand states reveal key elements involved in G protein-coupled receptor kinase activation. <i> Singh P, Wang B, Maeda T, Palczewski K, Tesmer JJ. </i> J Biol Chem, 2008","date":"2023-07-17T15:24:00.377Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3C4Y"}],"region_id":"DP03439r003","statement":[{"text":" The AST is typically disordered in structures of nucleotide-free, open PKA. Consistent with this, the AST of GRK1 is observed only in the nucleotide-bound structures (Fig. 2b), except when displaced by a crystal contact (in one chain of crystal forms I, II, and VI).","type":"Results"}]},{"start":1,"end":29,"reference_id":"18339619","reference_source":"pmid","reference_html":"Structures of rhodopsin kinase in different ligand states reveal key elements involved in G protein-coupled receptor kinase activation. <i> Singh P, Wang B, Maeda T, Palczewski K, Tesmer JJ. </i> J Biol Chem, 2008","date":"2023-07-17T15:28:31.121Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3C4Y"}],"region_id":"DP03439r004","statement":[{"text":"The PDB structure shows this region lacks electron density, indicating this region is disordered. ","type":"Curator statement"}]}],"regions_counter":4,"released":"2021_12","sequence":"MDFGSLETVVANSAFIAARGSFDASSGPASRDRKYLARLKLPPLSKCEALRESLDLGFEGMCLEQPIGKRLFQQFLRTHEQHGPALQLWKDIEDYDTADDALRPQKAQALRAAYLEPQAQLFCSFLDAETVARARAGAGDGLFQPLLRAVLAHLGQAPFQEFLDSLYFLRFLQWKWLEAQPMGEDWFLDFRVLGRGGFGEVFACQMKATGKLYACKKLNKKRLKKRKGYQGAMVEKKILAKVHSRFIVSLAYAFETKTDLCLVMTIMNGGDIRYHIYNVDEDNPGFQEPRAIFYTAQIVSGLEHLHQRNIIYRDLKPENVLLDDDGNVRISDLGLAVELKAGQTKTKGYAGTPGFMAPELLLGEEYDFSVDYFALGVTLYEMIAARGPFRARGEKVENKELKQRVLEQAVTYPDKFSPASKDFCEALLQKDPEKRLGFRDGSCDGLRTHPLFRDISWRQLEAGMLTPPFVPDSRTVYAKNIQDVGAFSTVKGVAFEKADTEFFQEFASGTCPIPWQEEMIETGVFGDLNVWRPDGQMPDDMKGVSGQEAAPSSKSGMCVLS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"uniref100":"UniRef100_P28327","uniref90":"UniRef90_P28327","uniref50":"UniRef50_P28327","genes":[{"name":{"value":"GRK1"},"synonyms":[{"value":"RHOK"}]}],"alphafold_very_low_content":0.044563279857397504,"disorder_content":0.35650623885918004,"disprot_consensus":{"full":[{"start":1,"end":181,"type":"D"},{"start":475,"end":493,"type":"D"}],"Structural state":[{"start":1,"end":181,"type":"D"},{"start":475,"end":493,"type":"D"}]}},{"disprot_id":"DP03440","acc":"P04968","creator":"jnilsson","date":"2021-07-27T15:00:30.989Z","features":{"pfam":[{"id":"PF00291","name":"Pyridoxal-phosphate dependent enzyme","start":29,"end":316},{"id":"PF00585","name":"C-terminal regulatory domain of Threonine dehydratase","start":329,"end":419},{"id":"PF00585","name":"C-terminal regulatory domain of Threonine dehydratase","start":425,"end":512}],"gene3D":[]},"length":514,"name":"L-threonine dehydratase biosynthetic IlvA","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":481,"end":496,"reference_id":"9562556","reference_source":"pmid","reference_html":"Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase. <i> Gallagher DT, Gilliland GL, Xiao G, Zondlo J, Fisher KE, Chinchilla D, Eisenstein E. </i> Structure, 1998","date":"2022-02-14T09:00:00.000Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1TDJ"}],"region_id":"DP03440r001","statement":[{"text":"The zone of missing residues 481–496 is on the exterior of the domain, in a position where a helix would be expected in order to complete the second α+β plait motif.","type":"Results"},{"text":"The regulatory domain is at the top in magenta and orange. The missing zone (residues 481–496) is indicated by a dotted line. (Secondary structure assignments were made using the program DSSP [24].)","type":"Figure"},{"text":"The black spheres show the start and end of the missing zone (residues 481–496) in TD the structure of which may be similar to the rightmost PGD helix.","type":"Figure"},{"text":" The final model lacks residues 1–4 at the N terminus and also lacks residues 481–496. This missing zone in the regulatory domain corresponds to a highly exposed connection between two β strands, where electron-density maps show the presence of the polypeptide but are insufficiently ordered to construct it. The distance between residues 480 and 497 and the extent of the intervening weak density correspond reasonably well with\nthe number of missing residues, and there is no ambiguity about the topology or fold","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-28T09:59:14.747Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MADSQPLSGAPEGAEYLRAVLRAPVYEAAQVTPLQKMEKLSSRLDNVILVKREDRQPVHSFKLRGAYAMMAGLTEEQKAHGVITASAGNHAQGVAFSSARLGVKALIVMPTATADIKVDAVRGFGGEVLLHGANFDEAKAKAIELSQQQGFTWVPPFDHPMVIAGQGTLALELLQQDAHLDRVFVPVGGGGLAAGVAVLIKQLMPQIKVIAVEAEDSACLKAALDAGHPVDLPRVGLFAEGVAVKRIGDETFRLCQEYLDDIITVDSDAICAAMKDLFEDVRAVAEPSGALALAGMKKYIALHNIRGERLAHILSGANVNFHGLRYVSERCELGEQREALLAVTIPEEKGSFLKFCQLLGGRSVTEFNYRFADAKNACIFVGVRLSRGLEERKEILQMLNDGGYSVVDLSDDEMAKLHVRYMVGGRPSHPLQERLYSFEFPESPGALLRFLNTLGTYWNISLFHYRSHGTDYGRVLAAFELGDHEPDFETRLNELGYDCHDETNNPAFRFFLAG","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref100":"UniRef100_P04968","uniref90":"UniRef90_P04968","uniref50":"UniRef50_P04968","genes":[{"name":{"value":"ilvA"},"olnNames":[{"value":"b3772"},{"value":"JW3745"}]}],"alphafold_very_low_content":0.005836575875486381,"disorder_content":0.0311284046692607,"disprot_consensus":{"full":[{"start":481,"end":496,"type":"D"}],"Structural state":[{"start":481,"end":496,"type":"D"}]}},{"disprot_id":"DP03442","acc":"P59635","creator":"fquaglia","date":"2021-07-28T08:34:12.944Z","features":{"pfam":[{"id":"PF08779","name":"Betacoronavirus NS7A protein","start":16,"end":122}],"gene3D":[]},"length":122,"name":"ORF7a protein","ncbi_taxon_id":694009,"organism":"Severe acute respiratory syndrome coronavirus","regions":[{"start":81,"end":94,"reference_id":"16328780","reference_source":"pmid","reference_html":"Solution structure of the X4 protein coded by the SARS related coronavirus reveals an immunoglobulin like fold and suggests a binding activity to integrin I domains. <i> Hänel K, Stangler T, Stoldt M, Willbold D. </i> J Biomed Sci, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1YO4"}],"region_id":"DP03442r002","statement":[{"text":"Residues 66–84 appear to be unstructured, indicated by decreased heteronuclear 1H-15N-NOE values (Figure 3) and the lack of experimental NOE-derived structural data for this part of the protein.","type":"Results"},{"text":"Both 15N T2 and steady-state 1H-15N NOE values support the hypothesis of an unstructured carboxy-terminal region encompassing residues 66–84 in contrast to the well-folded b-sandwich comprising residues 1–65.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-07T11:07:12.083Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MKIILFLTLIVFTSCELYHYQECVRGTTVLLKEPCPSGTYEGNSPFHPLADNKFALTCTSTHFAFACADGTRHTYQLRARSVSPKLFIRQEEVQQELYSPLFLIVAALVFLILCFTIKRKTE","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Nidovirales","Cornidovirineae","Coronaviridae","Orthocoronavirinae","Betacoronavirus","Sarbecovirus"],"uniref100":"UniRef100_P59635","uniref90":"UniRef90_P59635","uniref50":"UniRef50_P59635","dataset":["Viral proteins"],"genes":[{"orfNames":[{"value":"7a"}]}],"disorder_content":0.11475409836065574,"disprot_consensus":{"full":[{"start":81,"end":94,"type":"D"}],"Structural state":[{"start":81,"end":94,"type":"D"}]}},{"disprot_id":"DP03444","acc":"Q9UPP1","creator":"maspromonte","date":"2021-07-28T13:03:27.161Z","features":{"pfam":[{"id":"PF00628","name":"PHD-finger","start":44,"end":89},{"id":"PF02373","name":"JmjC domain, hydroxylase","start":270,"end":370},{"id":"PF17811","name":"Jumonji helical domain","start":374,"end":477}],"gene3D":[]},"length":1060,"name":"Histone lysine demethylase PHF8","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":101,"end":113,"reference_id":"20023638","reference_source":"pmid","reference_html":"Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases. <i> Horton JR, Upadhyay AK, Qi HH, Zhang X, Shi Y, Cheng X. </i> Nat Struct Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03444r001","statement":[{"text":"To  understand  how  H3K4me3  binding  enhances  demethylase activity, we determined the cocrystal structure of PHF81–447 with an H31–24 peptide containing H3K4me3 and H3K9me2 (Fig. 1e) in the presence of Fe2+ and N-oxalylglycine (the cofactor analog) to form a  catalytically  inert  complex  (Table  1).  The  structure,  determined at a resolution of 2.2 Å, shows that the PHD and jumonji domains act in concert in substrate recognition. The first 11 residues of the H3  peptide  were  nearly  buried  in  a  deep  cleft  between  the  PHD and the jumonji domains with a disordered linker (residues 66–78)  (Fig. 1e).","type":"Results"},{"text":"The IDR characterized in the publication and spanning residues 66-78 corresponds residues 102-114 of the canonical sequence in UniProt, since the authors determined a structure of PHF8 without the first 36 aminoacids. ","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"3KV4"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-04T12:16:05.813Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":101,"end":113,"reference_id":"20023638","reference_source":"pmid","reference_html":"Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases. <i> Horton JR, Upadhyay AK, Qi HH, Zhang X, Shi Y, Cheng X. </i> Nat Struct Mol Biol, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3KV4"}],"region_id":"DP03444r002","statement":[{"text":"The first 11 residues of the H3 peptide were nearly buried in a deep cleft between the PHD and the jumonji domains with a disordered linker (residues 66–78) (Fig. 1e).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-04T12:16:04.900Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MNRSRAIVQRGRVLPPPAPLDTTNLAGRRTLQGRAKMASVPVYCLCRLPYDVTRFMIECDMCQDWFHGSCVGVEEEKAADIDLYHCPNCEVLHGPSIMKKRRGSSKGHDTHKGKPVKTGSPTFVRELRSRTFDSSDEVILKPTGNQLTVEFLEENSFSVPILVLKKDGLGMTLPSPSFTVRDVEHYVGSDKEIDVIDVTRQADCKMKLGDFVKYYYSGKREKVLNVISLEFSDTRLSNLVETPKIVRKLSWVENLWPEECVFERPNVQKYCLMSVRDSYTDFHIDFGGTSVWYHVLKGEKIFYLIRPTNANLTLFECWSSSSNQNEMFFGDQVDKCYKCSVKQGQTLFIPTGWIHAVLTPVDCLAFGGNFLHSLNIEMQLKAYEIEKRLSTADLFRFPNFETICWYVGKHILDIFRGLRENRRHPASYLVHGGKALNLAFRAWTRKEALPDHEDEIPETVRTVQLIKDLAREIRLVEDIFQQNVGKTSNIFGLQRIFPAGSIPLTRPAHSTSVSMSRLSLPSKNGSKKKGLKPKELFKKAERKGKESSALGPAGQLSYNLMDTYSHQALKTGSFQKAKFNITGACLNDSDDDSPDLDLDGNESPLALLMSNGSTKRVKSLSKSRRTKIAKKVDKARLMAEQVMEDEFDLDSDDELQIDERLGKEKATLIIRPKFPRKLPRAKPCSDPNRVREPGEVEFDIEEDYTTDEDMVEGVEGKLGNGSGAGGILDLLKASRQVGGPDYAALTEAPASPSTQEAIQGMLCMANLQSSSSSPATSSLQAWWTGGQDRSSGSSSSGLGTVSNSPASQRTPGKRPIKRPAYWRTESEEEEENASLDEQDSLGACFKDAEYIYPSLESDDDDPALKSRPKKKKNSDDAPWSPKARVTPTLPKQDRPVREGTRVASIETGLAAAAAKLAQQELQKAQKKKYIKKKPLLKEVEQPRPQDSNLSLTVPAPTVAATPQLVTSSSPLPPPEPKQEALSGSLADHEYTARPNAFGMAQANRSTTPMAPGVFLTQRRPSVGSQSNQAGQGKRPKKGLATAKQRLGRILKIHRNGKLLL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"uniref100":"UniRef100_Q9UPP1","uniref90":"UniRef90_Q9UPP1","uniref50":"UniRef50_Q9UPP1","genes":[{"name":{"value":"PHF8"},"synonyms":[{"value":"KIAA1111"},{"value":"ZNF422"}]}],"alphafold_very_low_content":0.5386792452830189,"disorder_content":0.012264150943396227,"disprot_consensus":{"full":[{"start":101,"end":113,"type":"D"}],"Structural state":[{"start":101,"end":113,"type":"D"}],"Disorder function":[{"start":101,"end":113,"type":"F"}]}},{"disprot_id":"DP03445","acc":"P0C066","creator":"jnilsson","date":"2021-07-28T13:11:35.312Z","features":{"pfam":[{"id":"PF01464","name":"Transglycosylase SLT domain","start":195,"end":319},{"id":"PF11873","name":"Membrane-bound lytic murein transglycosylase C, N-terminal domain","start":31,"end":191}],"gene3D":[]},"length":359,"name":"Membrane-bound lytic murein transglycosylase C","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":20,"end":29,"reference_id":"24988330","reference_source":"pmid","reference_html":"Structure and cell wall cleavage by modular lytic transglycosylase MltC of Escherichia coli. <i> Artola-Recolons C, Lee M, Bernardo-García N, Blázquez B, Hesek D, Bartual SG, Mahasenan KV, Lastochkin E, Pi H, Boggess B, Meindl K, Usón I, Fisher JF, Mobashery S, Hermoso JA. </i> ACS Chem Biol, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"4C5F"}],"region_id":"DP03445r001","statement":[{"text":"As the MS analysis for the recombinant protein gives the expected mass value (Mr = 38 495 ± 4; predicted mass of Mr = 38 493) for the amino-acid residues 19−259 construct, residues 19−29 are present but are not seen\nin the electron density due to disorder (as is also predicted by the DisEMBL server (http://dis.embl.de/).","type":"Results"},{"text":"We noted that the stretch of amino acids 19−29 in the MltC structure is\ndisordered. ","type":"Results"},{"text":"It is tempting to speculate that the disorder within the residues 19−29 would impart the ability for a rotational motion to MltC to sweep out a large annulus of cleared peptidoglycan per each molecule of enzyme (Figure\n4B), which would enable insertion of a large assembly such as that of the flagellum.","type":"Results"},{"text":"(B) Rotational motion of a single membrane bound MltC with its disordered linker (residues 19−29, depicted in light brown) could create a large annulus of cleared peptidoglycan.","type":"Figure"},{"text":"The N-terminus, the site of attachment of residues 19−29 and the fatty acyl membrane anchor, which is not seen in the electron density, is indicated by an arrow at 11 o’clock.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-02T13:44:52.411Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MKKYLALALIAPLLISCSTTKKGDTYNEAWVKDTNGFDILMGQFAHNIENIWGFKEVVIAGPKDYVKYTDQYQTRSHINFDDGTITIETIAGTEPAAHLRRAIIKTLLMGDDPSSVDLYSDVDDITISKEPFLYGQVVDNTGQPIRWEGRASNFADYLLKNRLKSRSNGLRIIYSVTINMVPNHLDKRAHKYLGMVRQASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHTAGKDVFRSQGKSGTPSRSFLFDPASNIDTGTAYLAMLNNVYLGGIDNPTSRRYAVITAYNGGAGSVLRVFSNDKIQAANIINTMTPGDVYQTLTTRHPSAESRRYLYKVNTAQKSYRRR","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref100":"UniRef100_B7UI10","uniref90":"UniRef90_Q8XCS6","uniref50":"UniRef50_Q8XCS6","genes":[{"name":{"value":"mltC","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01616","url":"https://hamap.expasy.org/unirule/MF_01616"}}]},"synonyms":[{"value":"yggZ"}],"olnNames":[{"value":"b2963"},{"value":"JW5481"}]}],"alphafold_very_low_content":0.08635097493036212,"disorder_content":0.027855153203342618,"disprot_consensus":{"full":[{"start":20,"end":29,"type":"D"}],"Structural state":[{"start":20,"end":29,"type":"D"}]}},{"disprot_id":"DP03446","acc":"Q9NR48","creator":"maspromonte","date":"2021-07-29T09:20:24.339Z","features":{"pfam":[{"id":"PF00439","name":"Bromodomain","start":2461,"end":2535},{"id":"PF00856","name":"SET domain","start":2156,"end":2261},{"id":"PF01426","name":"BAH domain","start":2663,"end":2797},{"id":"PF17907","name":"AWS domain","start":2103,"end":2141},{"id":"PF20826","name":"PhD finger domain","start":2583,"end":2628},{"id":"PF30519","name":"SET-binding protein","start":44,"end":213},{"id":"PF30519","name":"SET-binding protein","start":972,"end":1535},{"id":"PF30519","name":"SET-binding protein","start":1793,"end":1924}],"gene3D":[]},"length":2969,"name":"Histone-lysine N-methyltransferase ASH1L","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":2090,"end":2107,"reference_id":"21239497","reference_source":"pmid","reference_html":"Crystal structure of the human histone methyltransferase ASH1L catalytic domain and its implications for the regulatory mechanism. <i> An S, Yeo KJ, Jeon YH, Song JJ. </i> J Biol Chem, 2011","date":"2022-09-26T15:21:05.675Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03446r001","statement":[{"text":"The AWS domain is composed of mostly loops and two short \u0003-helices. These loops are bound by two zinc atoms and coordinated by eight conserved cysteines in the AWS domain. The fact that the AWS domain in one of the two molecules of the asymmetric unit is partially disordered and that the temperature factor of the AWS domain is high suggests that the AWS domain is highly flexible.","type":"Results"},{"text":"the IDR characterized in the publication and spanning residues 2082-2103 corresponds to region 2090-2107 of the UniProt canonical ASH1L sequence.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-28T15:15:59.160Z"}},{"start":2268,"end":2272,"reference_id":"21239497","reference_source":"pmid","reference_html":"Crystal structure of the human histone methyltransferase ASH1L catalytic domain and its implications for the regulatory mechanism. <i> An S, Yeo KJ, Jeon YH, Song JJ. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000042","term_name":"methylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007704","ec_ontology":"ECO","ec_name":"methylation assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03446r002","statement":[{"text":"We crystallized the Q2265A mutant protein, and preliminary structural analysis of the mutant protein shows that the auto-inhibitory loop is highly disordered. With these mutants, we observed an increased level of HMTase activity for hASH1L, with higher levels of activity observed for Q2265A than for N2197A (Fig. 2D). ","type":"Results"},{"text":"Mutating Asn-2197 or Gln-2265 to alanine (N2197A,Q2265A) increases HMTase activity","type":"Figure"},{"text":"The residue, Gln2265 characterized in the publication corresponds to residue, Gln2270 of the UniProt ASH1L canonical sequence","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-04T10:52:04.081Z"},"ec_go":"IDA","disprot_namespace":"Disorder function"},{"start":2263,"end":2267,"reference_id":"21239497","reference_source":"pmid","reference_html":"Crystal structure of the human histone methyltransferase ASH1L catalytic domain and its implications for the regulatory mechanism. <i> An S, Yeo KJ, Jeon YH, Song JJ. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000042","term_name":"methylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007704","ec_ontology":"ECO","ec_name":"methylation assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03446r003","statement":[{"text":"Unexpectedly, the F2260A mutant showed no activity toward either the nucleosomal array or the mononucleosome substrates. ","type":"Results"},{"text":"Mutating Asn-2197 or Gln-2265 to alanine (N2197A,Q2265A) increases HMTase activity, whereas F2260A or Q2266A mutations abolish the activity.","type":"Figure"},{"text":"The residue, Phe2260 characterized in the publication corresponds to residue, Phe2265 of the UniProt ASH1L canonical sequence","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-04T10:52:04.923Z"},"ec_go":"IDA","disprot_namespace":"Disorder function"},{"start":2269,"end":2273,"reference_id":"21239497","reference_source":"pmid","reference_html":"Crystal structure of the human histone methyltransferase ASH1L catalytic domain and its implications for the regulatory mechanism. <i> An S, Yeo KJ, Jeon YH, Song JJ. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000042","term_name":"methylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007704","ec_ontology":"ECO","ec_name":"methylation assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03446r004","statement":[{"text":"In a third mutant, we mutated the Gln-2266 residue to Ala to perturb the interaction of the protein with AdoMet. In this mutant, we were not able to see any HMTase activity, suggesting that the Gln-2266 residue is critical for activity. ","type":"Results"},{"text":"Mutating Asn-2197 or Gln-2265 to alanine (N2197A,Q2265A) increases HMTase activity, whereas F2260A or Q2266A mutations abolish the activity.","type":"Figure"},{"text":"The residue, Gln2266 characterized in the publication corresponds to residue, Gln2271 of the UniProt ASH1L canonical sequence","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-04T10:52:05.664Z"},"ec_go":"IDA","disprot_namespace":"Disorder function"},{"start":2263,"end":2271,"reference_id":"21239497","reference_source":"pmid","reference_html":"Crystal structure of the human histone methyltransferase ASH1L catalytic domain and its implications for the regulatory mechanism. <i> An S, Yeo KJ, Jeon YH, Song JJ. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000059","term_name":"self-inhibition","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":3,"region_id":"DP03446r005","statement":[{"text":"We refer to the loop occupying the substrate binding pocket as the “auto-inhibitory loop.” The auto-inhibitory loop is highly flexible, as indicated by its high temperature factor, suggesting that the loop can be repositioned upon substrate binding.","type":"Results"},{"text":"The region characterized in the publication and spanning residues 2258-2266 corresponds to region 2263-2271 of the UniProt canonical ASH1L sequence","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-04T10:52:06.670Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":2263,"end":2271,"reference_id":"30827841","reference_source":"pmid","reference_html":"Structural Basis of MRG15-Mediated Activation of the ASH1L Histone Methyltransferase by Releasing an Autoinhibitory Loop. <i> Lee Y, Yoon E, Cho S, Schmähling S, Müller J, Song JJ. </i> Structure, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000059","term_name":"self-inhibition","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":3,"cross_refs":[{"db":"PDB","id":"6AGO"}],"region_id":"DP03446r006","statement":[{"text":"The structure reveals the architecture of the core of the AMC HMTase complex and uncovers an allosteric mechanism by which binding of MRG15 to one interface on the SET domain results in the disordering of the AI loop to permit substrate binding on the opposite surface of this domain. ","type":"Introduction"},{"text":"We find that, in the structure of the  ASH1LSET_MRG15MRG complex, the AI loop is disordered in both molecules in the asymmetric unit of the crystal (Figure 2A). ","type":"Results"},{"text":"(A) The autoinhibitory loop is disordered in the ASH1L_MRG15 (I) complex (left) and partially ordered in the ASH1L_MRG15 (II) complex (right). ","type":"Figure"},{"text":"(B) Superimposition of ASH1L alone and the ASH1L_MRG complexes (I and II), showing the structural changes in the autoinhibitory loop and SET-I loop upon MRG15 binding.","type":"Figure"},{"text":"(A) H2193 near the autoinhibitory loop is displaced from the loop in ASH1L_MRG15 (form I) where the loop is disordered, and H2193 interacts with the loop in the structures where the loop is ordered (form II and alone). ","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-04T10:52:07.456Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":2261,"end":2269,"reference_id":"30827843","reference_source":"pmid","reference_html":"Structural Insights into Stimulation of Ash1L's H3K36 Methyltransferase Activity through Mrg15 Binding. <i> Hou P, Huang C, Liu CP, Yang N, Yu T, Yin Y, Zhu B, Xu RM. </i> Structure, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000059","term_name":"self-inhibition","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":3,"cross_refs":[{"db":"PDB","id":"6INE"}],"region_id":"DP03446r007","statement":[{"text":"The most striking difference between the Mrg15-bound and thefree hAsh1L SET domains occurs at an autoinhibitory loop, whichranges from residues N2257 to K2264 in the post-SET region. It becomes disordered in the hAsh1L-Mrg15 complex (Figure 1B).","type":"Results"},{"text":"The disordered autoinhibitory loop in the hAsh1L-Mrg15 complex indicates that the conformation of this loop is dynamic upon Mrg15 binding, allowing easier access of H3K36 to the active site of hAsh1L for methylation.","type":"Results"},{"text":"The region characterized in the publication and spanning residues 2257-2264 corresponds to region 2261-2269 of the UniProt canonical ASH1L sequence","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-04T10:52:08.584Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":2261,"end":2284,"reference_id":"21239497","reference_source":"pmid","reference_html":"Crystal structure of the human histone methyltransferase ASH1L catalytic domain and its implications for the regulatory mechanism. <i> An S, Yeo KJ, Jeon YH, Song JJ. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":2,"region_id":"DP03446r008","statement":[{"text":"We refer to the loop occupying the substrate binding pocket as the “auto-inhibitory loop.” The auto-inhibitory loop is highly flexible, as indicated by its high temperature factor, suggesting that the loop can be repositioned upon substrate binding","type":"Results"}],"cross_refs":[{"db":"PDB","id":"3OPE"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-04T10:52:10.646Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":2261,"end":2273,"reference_id":"26292256","reference_source":"pmid","reference_html":"Two Loops Undergoing Concerted Dynamics Regulate the Activity of the ASH1L Histone Methyltransferase. <i> Rogawski DS, Ndoj J, Cho HJ, Maillard I, Grembecka J, Cierpicki T. </i> Biochemistry, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000059","term_name":"self-inhibition","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":3,"cross_refs":[{"db":"PDB","id":"4YPU"},{"db":"PDB","id":"4YNM"},{"db":"PDB","id":"4YPA"},{"db":"PDB","id":"4YNP"},{"db":"PDB","id":"4YPE"}],"region_id":"DP03446r009","statement":[{"text":"Using X-ray crystallography and nuclear magnetic resonance (NMR), we found that two loops surrounding the active site of ASH1L, the autoinhibitory loop and a loop in the SET-I subdomain, undergo concerted conformational dynamics.","type":"Introduction"},{"text":"We found that the autoinhibitory loop and the AWS region have the highest B factors, suggesting that these are more mobile regions (Figure 1C). ","type":"Results"},{"text":"The region characterized in the publication and spanning residues 2255-2268 corresponds to region 2261-2273 of the UniProt canonical ASH1L sequence","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-03T12:27:50.224Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":2261,"end":2273,"reference_id":"26292256","reference_source":"pmid","reference_html":"Two Loops Undergoing Concerted Dynamics Regulate the Activity of the ASH1L Histone Methyltransferase. <i> Rogawski DS, Ndoj J, Cho HJ, Maillard I, Grembecka J, Cierpicki T. </i> Biochemistry, 2015","date":"2022-09-08T12:35:45.104Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000059","term_name":"self-inhibition","term_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":3,"region_id":"DP03446r010","statement":[{"text":"Using X-ray crystallography and nuclear magnetic resonance (NMR), we found that two loops surrounding the active site of ASH1L, the autoinhibitory loop and a loop in the SET-I subdomain, undergo concerted conformational dynamics.","type":"Introduction"},{"text":"This observation strongly suggests that the autoinhibitory and SET-I loops surrounding the active site of ASH1L experience conformational dynamics, in agreement with crystallographic data presented above.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-28T15:14:35.303Z"}}],"regions_counter":10,"released":"2023_06","sequence":"MDPRNTAMLGLGSDSEGFSRKSPSAISTGTLVSKREVELEKNTKEEEDLRKRNRERNIEAGKDDGLTDAQQQFSVKETNFSEGNLKLKIGLQAKRTKKPPKNLENYVCRPAIKTTIKHPRKALKSGKMTDEKNEHCPSKRDPSKLYKKADDVAAIECQSEEVIRLHSQGENNPLSKKLSPVHSEMADYINATPSTLLGSRDPDLKDRALLNGGTSVTEKLAQLIATCPPSKSSKTKPKKLGTGTTAGLVSKDLIRKAGVGSVAGIIHKDLIKKPTISTAVGLVTKDPGKKPVFNAAVGLVNKDSVKKLGTGTTAVFINKNLGKKPGTITTVGLLSKDSGKKLGIGIVPGLVHKESGKKLGLGTVVGLVNKDLGKKLGSTVGLVAKDCAKKIVASSAMGLVNKDIGKKLMSCPLAGLISKDAINLKAEALLPTQEPLKASCSTNINNQESQELSESLKDSATSKTFEKNVVRQNKESILEKFSVRKEIINLEKEMFNEGTCIQQDSFSSSEKGSYETSKHEKQPPVYCTSPDFKMGGASDVSTAKSPFSAVGESNLPSPSPTVSVNPLTRSPPETSSQLAPNPLLLSSTTELIEEISESVGKNQFTSESTHLNVGHRSVGHSISIECKGIDKEVNDSKTTHIDIPRISSSLGKKPSLTSESSIHTITPSVVNFTSLFSNKPFLKLGAVSASDKHCQVAESLSTSLQSKPLKKRKGRKPRWTKVVARSTCRSPKGLELERSELFKNVSCSSLSNSNSEPAKFMKNIGPPSFVDHDFLKRRLPKLSKSTAPSLALLADSEKPSHKSFATHKLSSSMCVSSDLLSDIYKPKRGRPKSKEMPQLEGPPKRTLKIPASKVFSLQSKEEQEPPILQPEIEIPSFKQGLSVSPFPKKRGRPKRQMRSPVKMKPPVLSVAPFVATESPSKLESESDNHRSSSDFFESEDQLQDPDDLDDSHRPSVCSMSDLEMEPDKKITKRNNGQLMKTIIRKINKMKTLKRKKLLNQILSSSVESSNKGKVQSKLHNTVSSLAATFGSKLGQQINVSKKGTIYIGKRRGRKPKTVLNGILSGSPTSLAVLEQTAQQAAGSALGQILPPLLPSSASSSEILPSPICSQSSGTSGGQSPVSSDAGFVEPSSVPYLHLHSRQGSMIQTLAMKKASKGRRRLSPPTLLPNSPSHLSELTSLKEATPSPISESHSDETIPSDSGIGTDNNSTSDRAEKFCGQKKRRHSFEHVSLIPPETSTVLSSLKEKHKHKCKRRNHDYLSYDKMKRQKRKRKKKYPQLRNRQDPDFIAELEELISRLSEIRITHRSHHFIPRDLLPTIFRINFNSFYTHPSFPLDPLHYIRKPDLKKKRGRPPKMREAMAEMPFMHSLSFPLSSTGFYPSYGMPYSPSPLTAAPIGLGYYGRYPPTLYPPPPSPSFTTPLPPPSYMHAGHLLLNPAKYHKKKHKLLRQEAFLTTSRTPLLSMSTYPSVPPEMAYGWMVEHKHRHRHKHREHRSSEQPQVSMDTGSSRSVLESLKRYRFGKDAVGERYKHKEKHRCHMSCPHLSPSKSLINREEQWVHREPSESSPLALGLQTPLQIDCSESSPSLSLGGFTPNSEPASSDEHTNLFTSAIGSCRVSNPNSSGRKKLTDSPGLFSAQDTSLNRLHRKESLPSNERAVQTLAGSQPTSDKPSQRPSESTNCSPTRKRSSSESTSSTVNGVPSRSPRLVASGDDSVDSLLQRMVQNEDQEPMEKSIDAVIATASAPPSSSPGRSHSKDRTLGKPDSLLVPAVTSDSCNNSISLLSEKLTSSCSPHHIKRSVVEAMQRQARKMCNYDKILATKKNLDHVNKILKAKKLQRQARTGNNFVKRRPGRPRKCPLQAVVSMQAFQAAQFVNPELNRDEEGAALHLSPDTVTDVIEAVVQSVNLNPEHKKGLKRKGWLLEEQTRKKQKPLPEEEEQENNKSFNEAPVEIPSPSETPAKPSEPESTLQPVLSLIPREKKPPRPPKKKYQKAGLYSDVYKTTDPKSRLIQLKKEKLEYTPGEHEYGLFPAPIHVVFFVSGKYLRQKRIDFQLPYDILWQWKHNQLYKKPDVPLYKKIRSNVYVDVKPLSGYEATTCNCKKPDDDTRKGCVDDCLNRMIFAECSPNTCPCGEQCCNQRIQRHEWVQCLERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMIEQYHNHSDHYCLNLDSGMVIDSYRMGNEARFINHSCDPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVEKQQLCKCGFEKCRGIIGGKSQRVNGLTSSKNSQPMATHKKSGRSKEKRKSKHKLKKRRGHLSEEPSENINTPTRLTPQLQMKPMSNRERNFVLKHHVFLVRNWEKIRQKQEEVKHTSDNIHSASLYTRWNGICRDDGNIKSDVFMTQFSALQTARSVRTRRLAAAEENIEVARAARLAQIFKEICDGIISYKDSSRQALAAPLLNLPPKKKNADYYEKISDPLDLITIEKQILTGYYKTVEAFDADMLKVFRNAEKYYGRKSPVGRDVCRLRKAYYNARHEASAQIDEIVGETASEADSSETSVSEKENGHEKDDDVIRCICGLYKDEGLMIQCDKCMVWQHCDCMGVNSDVEHYLCEQCDPRPVDREVPMIPRPHYAQPGCVYFICLLRDDLLLRQGDCVYLMRDSRRTPDGHPVRQSYRLLSHINRDKLDIFRIEKLWKNEKEERFAFGHHYFRPHETHHSPSRRFYHNELFRVPLYEIIPLEAVVGTCCVLDLYTYCKGRPKGVKEQDVYICDYRLDKSAHLFYKIHRNRYPVCTKPYAFDHFPKKLTPKKDFSPHYVPDNYKRNGGRSSWKSERSKPPLKDLGQEDDALPLIEEVLASQEQAANEIPSLEEPEREGATANVSEGEKKTEESSQEPQSTCTPEERRHNQRERLNQILLNLLEKIPGKNAIDVTYLLEEGSGRKLRRRTLFIPENSFRK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"uniref100":"UniRef100_Q9NR48","uniref90":"UniRef90_Q9NR48","uniref50":"UniRef50_Q9NR48","genes":[{"name":{"value":"ASH1L"},"synonyms":[{"value":"KIAA1420"},{"value":"KMT2H"}]}],"disorder_content":0.014146177164028292,"disprot_consensus":{"full":[{"start":2090,"end":2107,"type":"D"},{"start":2261,"end":2284,"type":"D"}],"Structural state":[{"start":2090,"end":2107,"type":"D"},{"start":2261,"end":2284,"type":"D"}],"Disorder function":[{"start":2261,"end":2273,"type":"F"}]}},{"disprot_id":"DP03447","acc":"Q13177","creator":"eleonardi","date":"2021-07-29T14:57:50.207Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":249,"end":500},{"id":"PF00786","name":"P21-Rho-binding domain","start":73,"end":130}],"gene3D":[]},"length":524,"name":"Serine/threonine-protein kinase PAK 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":108,"reference_id":"31391252","reference_source":"pmid","reference_html":"The subcellular localization of type I p21-activated kinases is controlled by the disordered variable region and polybasic sequences. <i> Sun X, Su VL, Calderwood DA. </i> J Biol Chem, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03447r001","statement":[{"text":"Notably, we also made truncations deleting the kinase domain and variable regions of PAK2 and PAK3, and, similar to what we observed for PAK1, whereas full-length PAK2 and PAK3 do not target to junctions, GFP-PAK2(1–108) and GFP-PAK3(1–109) target very well (Fig. 3D).","type":"Results"},{"text":"Nonetheless, these constructs support the conclusion that the N-terminal and CRIB domain regions of type I PAKs can target to cell–cell boundaries, and the variable region inhibits targeting.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T12:19:58.164Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":71,"end":92,"reference_id":"10320322","reference_source":"pmid","reference_html":"Conformation of a Cdc42/Rac interactive binding peptide in complex with Cdc42 and analysis of the binding interface. <i> Stevens WK, Vranken W, Goudreau N, Xiang H, Xu P, Ni F. </i> Biochemistry, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03447r002","statement":[{"text":"Interaction of PAK2(71−92) with sNBD-labeled Cdc42 (21) was followed by changes in extrinsic fluorescence with the addition of varying amounts of the peptide (0−2.5 μM).","type":"Results"},{"text":"The increment in fluorescence is plotted, and the line represents a fit of the data to a simple model for bimolecular association.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T12:19:54.492Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":71,"end":92,"reference_id":"10320322","reference_source":"pmid","reference_html":"Conformation of a Cdc42/Rac interactive binding peptide in complex with Cdc42 and analysis of the binding interface. <i> Stevens WK, Vranken W, Goudreau N, Xiang H, Xu P, Ni F. </i> Biochemistry, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03447r003","statement":[{"text":"Proton NMR studies of PAK2(71−92) demonstrate structuring of PAK2(71−92) in the presence of GTP-γS-loaded Cdc42, through the observation of many nonsequential transferred NOEs. Structure calculations based on the observed transferred NOEs show that the central portion of the Cdc42-bound CRIB peptide assumes a loop conformation in which the side chains of consensus residues Phe80, His82, Ile84, His85, and Val86 are brought into proximity. ","type":"Abstract"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T12:19:53.114Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":71,"end":92,"reference_id":"10320322","reference_source":"pmid","reference_html":"Conformation of a Cdc42/Rac interactive binding peptide in complex with Cdc42 and analysis of the binding interface. <i> Stevens WK, Vranken W, Goudreau N, Xiang H, Xu P, Ni F. </i> Biochemistry, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03447r004","statement":[{"text":"Proton NMR studies of PAK2(71−92) demonstrate structuring of PAK2(71−92) in the presence of GTP-γS-loaded Cdc42, through the observation of many nonsequential transferred NOEs. Structure calculations based on the observed transferred NOEs show that the central portion of the Cdc42-bound CRIB peptide assumes a loop conformation in which the side chains of consensus residues Phe80, His82, Ile84, His85, and Val86 are brought into proximity. ","type":"Abstract"},{"text":" Interestingly, interaction of PAK2(71−92) with GTP-γS-loaded Cdc42 leads to structuring of this peptide, as evidenced by the appearance of many transferred NOEs. Similar NOEs are not observed in the free peptide, and are significantly attenuated in the presence of GDP-bound Cdc42. Although the structure of the entire peptide is not well defined, residues Pro77−Ala90 fold into a unique conformation upon binding to the “active” form of Cdc42. Structure calculations revealed a loop conformation condensed around a hydrophobic cluster comprised of residues Phe80, His82, Ile84, His85, and Val86.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T12:19:51.533Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":121,"end":136,"reference_id":"21170023","reference_source":"pmid","reference_html":"The assembly of a GTPase-kinase signalling complex by a bacterial catalytic scaffold. <i> Selyunin AS, Sutton SE, Weigele BA, Reddick LE, Orchard RC, Bresson SM, Tomchick DR, Alto NM. </i> Nature, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3PCS"}],"region_id":"DP03447r005","statement":[{"text":"The EspG-binding site on PAK2 was defined to residues 121–136, a highly conserved sequence that encodes the Iα3-helix within the kinase AID (Supplementary Fig. 8). We crystallized EspG in complex with the PAK2 Iα3-helix fragment and solved the structure to a resolution of 2.8 Å (Supplementary Table 1). EspG recognized the initial turn of the Iα3-helix whereas the remainder of the peptide adopted an extended strand conformation that lies orthogonal to the EspG six-stranded β-sheet (Fig. 3a, b).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T12:19:49.448Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":1,"end":17,"reference_id":"10320322","reference_source":"pmid","reference_html":"Conformation of a Cdc42/Rac interactive binding peptide in complex with Cdc42 and analysis of the binding interface. <i> Stevens WK, Vranken W, Goudreau N, Xiang H, Xu P, Ni F. </i> Biochemistry, 1999","date":"2023-07-14T14:42:52.019Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03447r008","statement":[{"text":"The N terminus of inactive dimeric Pak2 was associated with the highest solvent accessibility (80.0%), followed by segments that included the activation loop (52.5%) and the glycine-rich loop (49.5%). The AID (44.7%), the dimerization domain (34.4%), and the magnesium positioning loop (27.6%) were associated with slightly less solvent accessibility.","type":"Results"},{"text":"In addition, caspase cleavage and autophosphorylation dramatically and specifically increased deuteron incorporation into the N-terminal -5–17 fragment by about five deuterons, bringing the level of incorporation to 90% of the maximum, and indicating a region of high solvent exposure/flexibility (Table 1).","type":"Results"}]},{"start":1,"end":76,"reference_id":"10320322","reference_source":"pmid","reference_html":"Conformation of a Cdc42/Rac interactive binding peptide in complex with Cdc42 and analysis of the binding interface. <i> Stevens WK, Vranken W, Goudreau N, Xiang H, Xu P, Ni F. </i> Biochemistry, 1999","date":"2023-07-14T14:59:10.133Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006196","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03447r009","statement":[{"text":"The regions that lack amide H/D exchange information are depicted in gray (Fig. 4b).","type":"Results"}]},{"start":144,"end":227,"reference_id":"10320322","reference_source":"pmid","reference_html":"Conformation of a Cdc42/Rac interactive binding peptide in complex with Cdc42 and analysis of the binding interface. <i> Stevens WK, Vranken W, Goudreau N, Xiang H, Xu P, Ni F. </i> Biochemistry, 1999","date":"2023-07-14T15:00:29.339Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006196","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03447r010","statement":[{"text":"The regions that lack amide H/D exchange information are depicted in gray (Fig. 4b).","type":"Results"}]},{"start":78,"end":147,"reference_id":"10320322","reference_source":"pmid","reference_html":"Conformation of a Cdc42/Rac interactive binding peptide in complex with Cdc42 and analysis of the binding interface. <i> Stevens WK, Vranken W, Goudreau N, Xiang H, Xu P, Ni F. </i> Biochemistry, 1999","date":"2023-07-14T15:09:38.472Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03447r011","statement":[{"text":"The N terminus of inactive dimeric Pak2 was associated with the highest solvent accessibility (80.0%), followed by segments that included the activation loop (52.5%) and the glycine-rich loop (49.5%). The AID (44.7%), the dimerization domain (34.4%), and the magnesium positioning loop (27.6%) were associated with slightly less solvent accessibility.","type":"Results"},{"text":"The AID regions corresponds to the 78-147 region and the dimerization domain to the 79-86 region.","type":"Curator statement"},{"text":" The AID switch domain (83–132) and the N-terminal (1–17) and the C-terminal J-helix (501–514) of autoinhibited Pak2 show that AID occupation of the active site does not prevent ligand binding to the nucleotide pocket located deep in the active-site cleft. This reflects a significant level of conformational flexibility of the AID segment occupying the active-site cleft.","type":"Discussion"}]},{"start":390,"end":403,"reference_id":"10320322","reference_source":"pmid","reference_html":"Conformation of a Cdc42/Rac interactive binding peptide in complex with Cdc42 and analysis of the binding interface. <i> Stevens WK, Vranken W, Goudreau N, Xiang H, Xu P, Ni F. </i> Biochemistry, 1999","date":"2023-07-14T15:12:03.934Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03447r012","statement":[{"text":"The N terminus of inactive dimeric Pak2 was associated with the highest solvent accessibility (80.0%), followed by segments that included the activation loop (52.5%) and the glycine-rich loop (49.5%). The AID (44.7%), the dimerization domain (34.4%), and the magnesium positioning loop (27.6%) were associated with slightly less solvent accessibility.","type":"Results"},{"text":"The activation loop in the active site cleft is a highly solvent-accessible and flexible region (Fig. 4) and is disordered in the x-ray crystal structure of inactive Pak1 (1F3M.PDB).","type":"Discussion"},{"text":"The authors refer to the 390-403 region that comprises the activation loop (391-406).","type":"Curator statement"}]},{"start":210,"end":215,"reference_id":"10320322","reference_source":"pmid","reference_html":"Conformation of a Cdc42/Rac interactive binding peptide in complex with Cdc42 and analysis of the binding interface. <i> Stevens WK, Vranken W, Goudreau N, Xiang H, Xu P, Ni F. </i> Biochemistry, 1999","date":"2023-07-14T15:21:47.543Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000048","term_name":"limited proteolysis display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03447r013","statement":[{"text":"Inactive Pak2 was a single band of 58 kDa. Caspase cleavage of Pak2 was complete and produced two fragments, p27 and p34. Autophosphorylation of cleaved Pak2 was optimal at 7.6 mol/mol.","type":"Results"},{"text":"Caspase cleavage at Asp-212 is associated with increased amide H/D exchange in the active site (glycine-rich loop, C helix, and activation loop), the AID, and the N terminus. The increased amide H/D exchange appears to be the result of breaking two covalent bonds, Asp-212 and Ser-213, in the trans-dimerized conformation.","type":"Discussion"}]},{"start":139,"end":143,"reference_id":"10320322","reference_source":"pmid","reference_html":"Conformation of a Cdc42/Rac interactive binding peptide in complex with Cdc42 and analysis of the binding interface. <i> Stevens WK, Vranken W, Goudreau N, Xiang H, Xu P, Ni F. </i> Biochemistry, 1999","date":"2023-07-14T15:29:56.376Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03447r014","statement":[{"text":"Perturbation of the AID switch by caspase cleavage could disrupt the autoinhibition and lead to autophosphorylation of Thr-402 in the activation loop and Ser-141 downstream of the AID switch.","type":"Results"}]},{"start":399,"end":403,"reference_id":"10320322","reference_source":"pmid","reference_html":"Conformation of a Cdc42/Rac interactive binding peptide in complex with Cdc42 and analysis of the binding interface. <i> Stevens WK, Vranken W, Goudreau N, Xiang H, Xu P, Ni F. </i> Biochemistry, 1999","date":"2023-07-14T15:30:47.062Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03447r015","statement":[{"text":"Perturbation of the AID switch by caspase cleavage could disrupt the autoinhibition and lead to autophosphorylation of Thr-402 in the activation loop and Ser-141 downstream of the AID switch.","type":"Results"}]}],"regions_counter":15,"released":"2021_12","sequence":"MSDNGELEDKPPAPPVRMSSTIFSTGGKDPLSANHSLKPLPSVPEEKKPRHKIISIFSGTEKGSKKKEKERPEISPPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSNTVKQKYLSFTPPEKDGFPSGTPALNAKGTEAPAVVTEEEDDDEETAPPVIAPRPDHTKSIYTRSVIDPVPAPVGDSHVDGAAKSLDKQKKKTKMTDEEIMEKLRTIVSIGDPKKKYTRYEKIGQGASGTVFTATDVALGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSYLVGDELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMEGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLIMAAKEAMKSNR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref100":"UniRef100_Q13177","uniref90":"UniRef90_Q13177","uniref50":"UniRef50_Q13177","genes":[{"name":{"value":"PAK2"}}],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.2881679389312977,"disorder_content":0.4580152671755725,"disprot_consensus":{"full":[{"start":1,"end":70,"type":"D"},{"start":71,"end":92,"type":"T"},{"start":93,"end":120,"type":"D"},{"start":121,"end":136,"type":"T"},{"start":137,"end":227,"type":"D"},{"start":390,"end":403,"type":"D"}],"Structural state":[{"start":1,"end":76,"type":"D"},{"start":78,"end":227,"type":"D"},{"start":390,"end":403,"type":"D"}],"Biological process":[{"start":1,"end":108,"type":"F"}],"Molecular function":[{"start":71,"end":92,"type":"F"}],"Structural transition":[{"start":71,"end":92,"type":"T"},{"start":121,"end":136,"type":"T"}],"Disorder function":[{"start":139,"end":143,"type":"F"},{"start":210,"end":215,"type":"F"},{"start":399,"end":403,"type":"F"}]}},{"disprot_id":"DP03448","acc":"P56524","creator":"maspromonte","date":"2021-07-30T11:38:39.496Z","features":{"pfam":[{"id":"PF00850","name":"Histone deacetylase domain","start":675,"end":992},{"id":"PF12203","name":"Glutamine rich N terminal domain of histone deacetylase 4","start":62,"end":152}],"gene3D":[]},"length":1084,"name":"Histone deacetylase 4","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":130,"end":153,"reference_id":"17360518","reference_source":"pmid","reference_html":"Crystal structure of a conserved N-terminal domain of histone deacetylase 4 reveals functional insights into glutamine-rich domains. <i> Guo L, Han A, Bates DL, Cao J, Chen L. </i> Proc Natl Acad Sci U S A, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2H8N"},{"db":"PDB","id":"2O94"}],"region_id":"DP03448r001","statement":[{"text":"The asymmetric unit contains four copies of HDAC4, each of which folds into a single α-helix from residues 62–129, whereas residues 130–153 are disordered (Fig. 1).","type":"Results"},{"text":"Because the X-shaped diffusive streaks have a cross-angle similar to that of the four-helix bundle, one possibility is that the disordered region between residues 130 and 153 are trapped in the crystal lattice approximately along the same direction of the ordered region (residues 62 to 129) but are rotationally disordered.","type":"Supplementary material"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-03T10:48:16.786Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":729,"end":760,"reference_id":"24261862","reference_source":"pmid","reference_html":"Design, synthesis, and biological evaluation of potent and selective class IIa histone deacetylase (HDAC) inhibitors as a potential therapy for Huntington's disease. <i> Bürli RW, Luckhurst CA, Aziz O, Matthews KL, Yates D, Lyons KA, Beconi M, McAllister G, Breccia P, Stott AJ, Penrose SD, Wall M, Lamers M, Leonard P, Müller I, Richardson CM, Jarvis R, Stones L, Hughes S, Wishart G, Haughan AF, O'Connell C, Mead T, McNeil H, Vann J, Mangette J, Maillard M, Beaumont V, Munoz-Sanjuan I, Dominguez C. </i> J Med Chem, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03448r002","statement":[{"text":"In addition, it was observed that amino acids 729 to 760 were not visible in the electron density maps for any of the three molecules in the asymmetric unit and were omitted\nfrom the model because of disorder.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"4CBT"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-04T10:53:34.727Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MSSQSHPDGLSGRDQPVELLNPARVNHMPSTVDVATALPLQVAPSAVPMDLRLDHQFSLPVAEPALREQQLQQELLALKQKQQIQRQILIAEFQRQHEQLSRQHEAQLHEHIKQQQEMLAMKHQQELLEHQRKLERHRQEQELEKQHREQKLQQLKNKEKGKESAVASTEVKMKLQEFVLNKKKALAHRNLNHCISSDPRYWYGKTQHSSLDQSSPPQSGVSTSYNHPVLGMYDAKDDFPLRKTASEPNLKLRSRLKQKVAERRSSPLLRRKDGPVVTALKKRPLDVTDSACSSAPGSGPSSPNNSSGSVSAENGIAPAVPSIPAETSLAHRLVAREGSAAPLPLYTSPSLPNITLGLPATGPSAGTAGQQDAERLTLPALQQRLSLFPGTHLTPYLSTSPLERDGGAAHSPLLQHMVLLEQPPAQAPLVTGLGALPLHAQSLVGADRVSPSIHKLRQHRPLGRTQSAPLPQNAQALQHLVIQQQHQQFLEKHKQQFQQQQLQMNKIIPKPSEPARQPESHPEETEEELREHQALLDEPYLDRLPGQKEAHAQAGVQVKQEPIESDEEEAEPPREVEPGQRQPSEQELLFRQQALLLEQQRIHQLRNYQASMEAAGIPVSFGGHRPLSRAQSSPASATFPVSVQEPPTKPRFTTGLVYDTLMLKHQCTCGSSSSHPEHAGRIQSIWSRLQETGLRGKCECIRGRKATLEELQTVHSEAHTLLYGTNPLNRQKLDSKKLLGSLASVFVRLPCGGVGVDSDTIWNEVHSAGAARLAVGCVVELVFKVATGELKNGFAVVRPPGHHAEESTPMGFCYFNSVAVAAKLLQQRLSVSKILIVDWDVHHGNGTQQAFYSDPSVLYMSLHRYDDGNFFPGSGAPDEVGTGPGVGFNVNMAFTGGLDPPMGDAEYLAAFRTVVMPIASEFAPDVVLVSSGFDAVEGHPTPLGGYNLSARCFGYLTKQLMGLAGGRIVLALEGGHDLTAICDASEACVSALLGNELDPLPEKVLQQRPNANAVRSMEKVMEIHSKYWRCLQRTTSTAGRSLIEAQTCENEEAETVTAMASLSVGVKPAEKRPDEEPMEEEPPL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"uniref100":"UniRef100_P56524","uniref90":"UniRef90_P56524","uniref50":"UniRef50_P56524","genes":[{"name":{"value":"HDAC4"},"synonyms":[{"value":"KIAA0288"}]}],"alphafold_very_low_content":0.4474169741697417,"disorder_content":0.05166051660516605,"disprot_consensus":{"full":[{"start":130,"end":153,"type":"D"},{"start":729,"end":760,"type":"D"}],"Structural state":[{"start":130,"end":153,"type":"D"},{"start":729,"end":760,"type":"D"}]}},{"disprot_id":"DP03449","acc":"P10902","creator":"jnilsson","date":"2021-07-30T15:19:55.052Z","features":{"pfam":[{"id":"PF00890","name":"FAD binding domain","start":10,"end":392},{"id":"PF02910","name":"Fumarate reductase flavoprotein C-term","start":441,"end":521}],"gene3D":[]},"length":540,"name":"L-aspartate oxidase","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":44,"end":56,"reference_id":"10425677","reference_source":"pmid","reference_html":"Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family. <i> Mattevi A, Tedeschi G, Bacchella L, Coda A, Negri A, Ronchi S. </i> Structure, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"1CHU"}],"region_id":"DP03449r001","statement":[{"text":" The final electron density is continuous from Asn2 to Pro533, except for three protein segments (residues 44–56, 104–141 and 411–413) which lack well-defined density and were not included in the model. These three segments are located on the protein surface: the disorder of residues 44–56 is probably related to the absence of bound FAD in the crystalline enzyme (see below); residues 104–141 form part of a region known to\nbe highly susceptible to proteolysis [21]; and residues 411–413 belong to the linker connecting the FAD-binding domain to the helical domain (Figures 3 and 4a).","type":"Results"},{"text":"Residues 43–57, 103–142 and 410–414 are linked by thin lines, because they are at the border of the disordered polypeptide segments not included in the final model","type":"Figure"},{"text":"In the apoenzyme structure, residues 44–56 are disordered\nand could not be located in the electron-density map\n(Figures 4a and 5).","type":"Results"},{"text":" Various refinement protocols, including unrestrained REFMAC/ARP refinement, were tried in order to localise the regions 44–56 and 104–141. However, these residues could not be located in the density, thus suggesting that they are disordered. ","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-02T13:24:08.843Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":104,"end":141,"reference_id":"10425677","reference_source":"pmid","reference_html":"Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family. <i> Mattevi A, Tedeschi G, Bacchella L, Coda A, Negri A, Ronchi S. </i> Structure, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"PDB","id":"1CHU"}],"region_id":"DP03449r002","statement":[{"text":" The final electron density is continuous from Asn2 to Pro533, except for three protein segments (residues 44–56, 104–141 and 411–413) which lack well-defined density and were not included in the model. These three segments are located on the protein surface: the disorder of residues 44–56 is probably related to the absence of bound FAD in the crystalline enzyme (see below); residues 104–141 form part of a region known to\nbe highly susceptible to proteolysis [21]; and residues 411–413 belong to the linker connecting the FAD-binding domain to the helical domain (Figures 3 and 4a).","type":"Results"},{"text":"Residues 43–57, 103–142 and 410–414 are linked by thin lines, because they are at the border of the disordered polypeptide segments not included in the final model","type":"Figure"},{"text":"In the apoenzyme structure, residues 44–56 are disordered\nand could not be located in the electron-density map\n(Figures 4a and 5).","type":"Results"},{"text":" Various refinement protocols, including unrestrained REFMAC/ARP refinement, were tried in order to localise the regions 44–56 and 104–141. However, these residues could not be located in the density, thus suggesting that they are disordered. ","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-02T13:24:21.903Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2023_12","sequence":"MNTLPEHSCDVLIIGSGAAGLSLALRLADQHQVIVLSKGPVTEGSTFYAQGGIAAVFDETDSIDSHVEDTLIAGAGICDRHAVEFVASNARSCVQWLIDQGVLFDTHIQPNGEESYHLTREGGHSHRRILHAADATGREVETTLVSKALNHPNIRVLERSNAVDLIVSDKIGLPGTRRVVGAWVWNRNKETVETCHAKAVVLATGGASKVYQYTTNPDISSGDGIAMAWRAGCRVANLEFNQFHPTALYHPQARNFLLTEALRGEGAYLKRPDGTRFMPDFDERGELAPRDIVARAIDHEMKRLGADCMFLDISHKPADFIRQHFPMIYEKLLGLGIDLTQEPVPIVPAAHYTCGGVMVDDHGRTDVEGLYAIGEVSYTGLHGANRMASNSLLECLVYGWSAAEDITRRMPYAHDISTLPPWDESRVENPDERVVIQHNWHELRLFMWDYVGIVRTTKRLERALRRITMLQQEIDEYYAHFRVSNNLLELRNLVQVAELIVRCAMMRKESRGLHFTLDYPELLTHSGPSILSPGNHYINR","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref100":"UniRef100_P10902","uniref90":"UniRef90_P10902","uniref50":"UniRef50_P10902","genes":[{"name":{"value":"nadB","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"2841129","url":"http://www.ncbi.nlm.nih.gov/pubmed/2841129","alternativeUrl":"https://europepmc.org/abstract/MED/2841129"}}]},"synonyms":[{"value":"nicB"}],"olnNames":[{"value":"b2574"},{"value":"JW2558"}]}],"alphafold_very_low_content":0.011111111111111112,"disorder_content":0.09444444444444444,"disprot_consensus":{"full":[{"start":44,"end":56,"type":"D"},{"start":104,"end":141,"type":"D"}],"Structural state":[{"start":44,"end":56,"type":"D"},{"start":104,"end":141,"type":"D"}]}},{"disprot_id":"DP03450","acc":"P0DTC4","creator":"fquaglia","date":"2021-08-02T09:27:27.690Z","features":{"pfam":[{"id":"PF02723","name":"Coronavirus small envelope protein E","start":2,"end":67}],"gene3D":[]},"length":75,"name":"Envelope small membrane protein","ncbi_taxon_id":2697049,"organism":"Severe acute respiratory syndrome coronavirus 2","regions":[{"start":61,"end":75,"reference_id":"34003853","reference_source":"pmid","reference_html":"Interactions of SARS-CoV-2 envelope protein with amilorides correlate with antiviral activity. <i> Park SH, Siddiqi H, Castro DV, De Angelis AA, Oom AL, Stoneham CA, Lewinski MK, Clark AE, Croker BA, Carlin AF, Guatelli J, Opella SJ. </i> PLoS Pathog, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03450r001","statement":[{"text":"The 1H/15N heteronuclear NOE data also shows that residues 2–7, before the start of the N-terminal helix, and residues 61–75 following the end of the C-terminal helix exhibit gradients of increasing motion towards the termini, although even the terminal residues do not appear to be highly mobile and unstructured, as is sometimes the case in this class of proteins [32,50].","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-04T13:54:30.375Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MYSFVSEETGTLIVNSVLLFLAFVVFLLVTLAILTALRLCAYCCNIVNVSLVKPSFYVYSRVKNLNSSRVPDLLV","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Nidovirales","Cornidovirineae","Coronaviridae","Orthocoronavirinae","Betacoronavirus","Sarbecovirus"],"uniref100":"UniRef100_P0DTC4","uniref90":"UniRef90_P0DTC4","uniref50":"UniRef50_P0DTC4","dataset":["Viral proteins"],"genes":[{"name":{"value":"E","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04204","url":"https://hamap.expasy.org/unirule/MF_04204"}}]},"orfNames":[{"value":"4"}]}],"disorder_content":0.2,"disprot_consensus":{"full":[{"start":61,"end":75,"type":"D"}],"Structural state":[{"start":61,"end":75,"type":"D"}]}},{"disprot_id":"DP03451","acc":"P21675-1","creator":"maspromonte","date":"2021-08-02T14:25:56.894Z","features":{"pfam":[],"gene3D":[]},"length":1872,"name":"Transcription initiation factor TFIID subunit 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1626,"end":1638,"reference_id":"10827952","reference_source":"pmid","reference_html":"Structure and function of a human TAFII250 double bromodomain module. <i> Jacobson RH, Ladurner AG, King DS, Tjian R. </i> Science, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03451r001","cross_refs":[{"db":"PDB","id":"1EQF"}],"statement":[{"text":"Residues COOH-terminal to the bromodomain motifs (residues 1625 to 1638) were not visible in the experimental map and presumably are disordered. ","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-04T10:53:01.615Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":972,"end":1053,"reference_id":"27007846","reference_source":"pmid","reference_html":"Structure of promoter-bound TFIID and model of human pre-initiation complex assembly. <i> Louder RK, He Y, López-Blanco JR, Fang J, Chacón P, Nogales E. </i> Nature, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5FUR"}],"region_id":"DP03451r002","statement":[{"text":"There is a small protein density contacting the minor groove of the Inr (Fig. 2a, d). We propose that it corresponds to the portion of TAF1 between residues 993–1075, which is disordered in the crystal structure but is well conserved among metazoans and is predicted to be ~50% α-helical (Extended Data Fig. 4c–e).","type":"Results"},{"text":"The IDR chracterized in the publication and spanning residues 993-1075 of the isoform 2 corresponds to region 972-1053 of the canonical sequence, since the isoform 2 differs from the canonical sequence as follows 177-177: G → GVSENGEGIILPSIIAPSSLAS","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-04T10:53:00.876Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MGPGCDLLLRTAATITAAAIMSDTDSDEDSAGGGPFSLAGFLFGNINGAGQLEGESVLDDECKKHLAGLGALGLGSLITELTANEELTGTDGALVNDEGWVRSTEDAVDYSDINEVAEDESRRYQQTMGSLQPLCHSDYDEDDYDADCEDIDCKLMPPPPPPPGPMKKDKDQDSITGEKVDFSSSSDSESEMGPQEATQAESEDGKLTLPLAGIMQHDATKLLPSVTELFPEFRPGKVLRFLRLFGPGKNVPSVWRSARRKRKKKHRELIQEEQIQEVECSVESEVSQKSLWNYDYAPPPPPEQCLSDDEITMMAPVESKFSQSTGDIDKVTDTKPRVAEWRYGPARLWYDMLGVPEDGSGFDYGFKLRKTEHEPVIKSRMIEEFRKLEENNGTDLLADENFLMVTQLHWEDDIIWDGEDVKHKGTKPQRASLAGWLPSSMTRNAMAYNVQQGFAATLDDDKPWYSIFPIDNEDLVYGRWEDNIIWDAQAMPRLLEPPVLTLDPNDENLILEIPDEKEEATSNSPSKESKKESSLKKSRILLGKTGVIKEEPQQNMSQPEVKDPWNLSNDEYYYPKQQGLRGTFGGNIIQHSIPAVELRQPFFPTHMGPIKLRQFHRPPLKKYSFGALSQPGPHSVQPLLKHIKKKAKMREQERQASGGGEMFFMRTPQDLTGKDGDLILAEYSEENGPLMMQVGMATKIKNYYKRKPGKDPGAPDCKYGETVYCHTSPFLGSLHPGQLLQAFENNLFRAPIYLHKMPETDFLIIRTRQGYYIRELVDIFVVGQQCPLFEVPGPNSKRANTHIRDFLQVFIYRLFWKSKDRPRRIRMEDIKKAFPSHSESSIRKRLKLCADFKRTGMDSNWWVLKSDFRLPTEEEIRAMVSPEQCCAYYSMIAAEQRLKDAGYGEKSFFAPEEENEEDFQMKIDDEVRTAPWNTTRAFIAAMKGKCLLEVTGVADPTGCGEGFSYVKIPNKPTQQKDDKEPQPVKKTVTGTDADLRRLSLKNAKQLLRKFGVPEEEIKKLSRWEVIDVVRTMSTEQARSGEGPMSKFARGSRFSVAEHQERYKEECQRIFDLQNKVLSSTEVLSTDTDSSSAEDSDFEEMGKNIENMLQNKKTSSQLSREREEQERKELQRMLLAAGSAASGNNHRDDDTASVTSLNSSATGRCLKIYRTFRDEEGKEYVRCETVRKPAVIDAYVRIRTTKDEEFIRKFALFDEQHREEMRKERRRIQEQLRRLKRNQEKEKLKGPPEKKPKKMKERPDLKLKCGACGAIGHMRTNKFCPLYYQTNAPPSNPVAMTEEQEEELEKTVIHNDNEELIKVEGTKIVLGKQLIESADEVRRKSLVLKFPKQQLPPKKKRRVGTTVHCDYLNRPHKSIHRRRTDPMVTLSSILESIINDMRDLPNTYPFHTPVNAKVVKDYYKIITRPMDLQTLRENVRKRLYPSREEFREHLELIVKNSATYNGPKHSLTQISQSMLDLCDEKLKEKEDKLARLEKAINPLLDDDDQVAFSFILDNIVTQKMMAVPDSWPFHHPVNKKFVPDYYKVIVNPMDLETIRKNISKHKYQSRESFLDDVNLILANSVKYNGPESQYTKTAQEIVNVCYQTLTEYDEHLTQLEKDICTAKEAALEEAELESLDPMTPGPYTPQPPDLYDTNTSLSMSRDASVFQDESNMSVLDIPSATPEKQVTQEGEDGDGDLADEEEGTVQQPQASVLYEDLLMSEGEDDEEDAGSDEEGDNPFSAIQLSESGSDSDVGSGGIRPKQPRMLQENTRMDMENEESMMSYEGDGGEASHGLEDSNISYGSYEEPDPKSNTQDTSFSSIGGYEVSEEEEDEEEEEQRSGPSVLSQVHLSEDEEDSEDFHSIAGDSDLDSDE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"uniref100":"UniRef100_P21675","uniref90":"UniRef90_P21675","uniref50":"UniRef50_P21675","genes":[{"name":{"value":"TAF1"},"synonyms":[{"value":"BA2R"},{"value":"CCG1"},{"value":"CCGS"},{"value":"TAF2A"}]}],"alphafold_very_low_content":0.4188034188034188,"disorder_content":0.05074786324786325,"disprot_consensus":{"full":[{"start":972,"end":1053,"type":"D"},{"start":1626,"end":1638,"type":"D"}],"Structural state":[{"start":972,"end":1053,"type":"D"},{"start":1626,"end":1638,"type":"D"}]}},{"disprot_id":"DP03452","acc":"Q6P1X5","creator":"maspromonte","date":"2021-08-03T15:52:32.127Z","features":{"pfam":[{"id":"PF25316","name":"TAF2 Ig-like domain","start":526,"end":644},{"id":"PF25577","name":"TAF2-like, TPR repeats","start":646,"end":1004}],"gene3D":[]},"length":1199,"name":"Transcription initiation factor TFIID subunit 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":977,"end":1199,"reference_id":"27007846","reference_source":"pmid","reference_html":"Structure of promoter-bound TFIID and model of human pre-initiation complex assembly. <i> Louder RK, He Y, López-Blanco JR, Fang J, Chacón P, Nogales E. </i> Nature, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":2,"cross_refs":[{"db":"PDB","id":"5FUR"}],"region_id":"DP03452r001","statement":[{"text":"b, Domain arrangement of TAF2, including the four subdomains of the APD (D1-4), and the C-terminal intrinsically-disordered region (IDR).","type":"Supplementary material"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-04T20:43:02.017Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MPLTGVEPARMNRKKGDKGFESPRPYKLTHQVVCINNINFQRKSVVGFVELTIFPTVANLNRIKLNSKQCRIYRVRINDLEAAFIYNDPTLEVCHSESKQRNLNYFSNAYAAAVSAVDPDAGNGELCIKVPSELWKHVDELKVLKIHINFSLDQPKGGLHFVVPSVEGSMAERGAHVFSCGYQNSTRFWFPCVDSYSELCTWKLEFTVDAAMVAVSNGDLVETVYTHDMRKKTFHYMLTIPTAASNISLAIGPFEILVDPYMHEVTHFCLPQLLPLLKHTTSYLHEVFEFYEEILTCRYPYSCFKTVFIDEAYVEVAAYASMSIFSTNLLHSAMIIDETPLTRRCLAQSLAQQFFGCFISRMSWSDEWVLKGISGYIYGLWMKKTFGVNEYRHWIKEELDKIVAYELKTGGVLLHPIFGGGKEKDNPASHLHFSIKHPHTLSWEYYSMFQCKAHLVMRLIENRISMEFMLQVFNKLLSLASTASSQKFQSHMWSQMLVSTSGFLKSISNVSGKDIQPLIKQWVDQSGVVKFYGSFAFNRKRNVLELEIKQDYTSPGTQKYVGPLKVTVQELDGSFNHTLQIEENSLKHDIPCHSKSRRNKKKKIPLMNGEEVDMDLSAMDADSPLLWIRIDPDMSVLRKVEFEQADFMWQYQLRYERDVVAQQESILALEKFPTPASRLALTDILEQEQCFYRVRMSACFCLAKIANSMVSTWTGPPAMKSLFTRMFCCKSCPNIVKTNNFMSFQSYFLQKTMPVAMALLRDVHNLCPKEVLTFILDLIKYNDNRKNKFSDNYYRAEMIDALANSVTPAVSVNNEVRTLDNLNPDVRLILEEITRFLNMEKLLPSYRHTITVSCLRAIRVLQKNGHVPSDPALFKSYAEYGHFVDIRIAALEAVVDYTKVDRSYEELQWLLNMIQNDPVPYVRHKILNMLTKNPPFTKNMESPLCNEALVDQLWKLMNSGTSHDWRLRCGAVDLYFTLFGLSRPSCLPLPELGLVLNLKEKKAVLNPTIIPESVAGNQEAANNPSSHPQLVGFQNPFSSSQDEEEIDMDTVHDSQAFISHHLNMLERPSTPGLSKYRPASSRSALIPQHSAGCDSTPTTKPQWSLELARKGTGKEQAPLEMSMHPAASAPLSVFTKESTASKHSDHHHHHHHEHKKKKKKHKHKHKHKHKHDSKEKDKEPFTFSSPASGRSIRSPSLSD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"uniref100":"UniRef100_Q6P1X5","uniref90":"UniRef90_Q6P1X5","uniref50":"UniRef50_Q6P1X5","genes":[{"name":{"value":"TAF2"},"synonyms":[{"value":"CIF150"},{"value":"TAF2B"}]}],"alphafold_very_low_content":0.195162635529608,"disorder_content":0.1859883236030025,"disprot_consensus":{"full":[{"start":977,"end":1199,"type":"D"}],"Structural state":[{"start":977,"end":1199,"type":"D"}]}},{"disprot_id":"DP03453","acc":"P51513","creator":"maspromonte","date":"2021-08-03T16:59:06.318Z","features":{"pfam":[{"id":"PF00013","name":"KH domain","start":53,"end":112},{"id":"PF00013","name":"KH domain","start":174,"end":238},{"id":"PF00013","name":"KH domain","start":424,"end":490}],"gene3D":[]},"length":507,"name":"RNA-binding protein Nova-1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":125,"end":143,"reference_id":"21742260","reference_source":"pmid","reference_html":"Protein-RNA and protein-protein recognition by dual KH1/2 domains of the neuronal splicing factor Nova-1. <i> Teplova M, Malinina L, Darnell JC, Song J, Lu M, Abagyan R, Musunuru K, Teplov A, Burley SK, Darnell RB, Patel DJ. </i> Structure, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2ANN"},{"db":"PDB","id":"2ANR"}],"region_id":"DP03453r001","statement":[{"text":"In Nova KH1-KH2, the interdomain linker is considerably longer (26-aa)  and  partially  disordered  in  the  crystal,  compared  to  a  10-aa  linker  in  IMP1 KH3/4, and a 14-aa linker in PCBP2 KH1/2.","type":"Supplementary material"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-03T12:13:06.609Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MMAAAPIQQNGTHTGVPIDLDPPDSRKRPLEAPPEAGSTKRTNTGEDGQYFLKVLIPSYAAGSIIGKGGQTIVQLQKETGATIKLSKSKDFYPGTTERVCLIQGTVEALNAVHGFIAEKIREMPQNVAKTEPVSILQPQTTVNPDRIKQTLPSSPTTTKSSPSDPMTTSRANQVKIIVPNSTAGLIIGKGGATVKAVMEQSGAWVQLSQKPDGINLQERVVTVSGEPEQNRKAVELIIQKIQEDPQSGSCLNISYANVTGPVANSNPTGSPYANTAEVLPTAAAAAGLLGHANLAGVAAFPAVLSGFTGNDLVAITSALNTLASYGYNLNTLGLGLSQAAATGALAAAAASANPAAAAANLLATYASEASASGSTAGGTAGTFALGSLAAATAATNGYFGAASPLAASAILGTEKSTDGSKDVVEIAVPENLVGAILGKGGKTLVEYQELTGARIQISKKGEFVPGTRNRKVTITGTPAATQAAQYLITQRITYEQGVRAANPQKVG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref100":"UniRef100_P51513","uniref90":"UniRef90_Q9JKN6","uniref50":"UniRef50_Q9JKN6","genes":[{"name":{"value":"NOVA1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:7886","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:7886"}}]}}],"alphafold_very_low_content":0.40631163708086787,"disorder_content":0.03747534516765286,"disprot_consensus":{"full":[{"start":125,"end":143,"type":"D"}],"Structural state":[{"start":125,"end":143,"type":"D"}]}},{"disprot_id":"DP03454","acc":"Q9UBP0","creator":"maspromonte","date":"2021-08-04T09:18:38.908Z","features":{"pfam":[{"id":"PF00004","name":"ATPase family associated with various cellular activities (AAA)","start":378,"end":507},{"id":"PF09336","name":"Vps4 C terminal oligomerisation domain","start":578,"end":612},{"id":"PF17862","name":"AAA+ lid domain","start":534,"end":567}],"gene3D":[]},"length":616,"name":"Spastin","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":228,"end":323,"reference_id":"22446388","reference_source":"pmid","reference_html":"Crystal structure of the human spastin AAA domain. <i> Taylor JL, White SR, Lauring B, Kull FJ. </i> J Struct Biol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"3VFD"}],"region_id":"DP03454r001","statement":[{"text":"The N-terminal 96 residues of the construct used to obtain the crystals in this study were not visible in the final structure. As this region of the protein is predicted to have very little secondary structure (Kabsch, 1983), it was unclear whether the entire construct had been crystallized and simply contained a disordered N-terminus, or the N- terminal amino acids were actually absent.","type":"Results"},{"text":"Additionally, in a sample of purified spastin protein, several low molecular weight bands were detected, indicating that the N-terminus of this construct is degraded or cleaved.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-03T12:02:52.491Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":270,"end":328,"reference_id":"17389232","reference_source":"pmid","reference_html":"Recognition of C-terminal amino acids in tubulin by pore loops in Spastin is important for microtubule severing. <i> White SR, Evans KJ, Lary J, Cole JL, Lauring B. </i> J Cell Biol, 2007","date":"2022-03-08T13:55:58.700Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0001170","ec_ontology":"ECO","ec_name":"cross-linking evidence used in manual assertion","unpublished":true,"released":"2022_03","version":4,"region_id":"DP03454r002","statement":[{"text":"The N-terminal region consists of four subdomains (see Fig. 1 A for schematic): the Atlastin binding domain (Evans et al., 2006), the MIT domain, alternatively spliced exon 4 (Charvin et al., 2003), and as we show in Fig. 2, an MTBD that is both necessary for MT severing and sufficient for MT association.","type":"Results"},{"text":"In contrast, ΔMTBD Spastin neither bound nor severed MTs, demonstrating that aa 270–328 are necessary for MT severing in vitro. ","type":"Results"},{"text":"In contrast, deletion of the first 328 amino acids did abolish severing activity,  as  the  transfected  cell  still  has  an  MT  array.  This  suggested  that  the approximate boundaries for a MTBD are between aa 280 and 328. ","type":"Figure"},{"text":"We next examined whether the MTBD was sufficient to confer MT association both in cells and in vitro. In transfection experiments, 1–328 stop Spastin but not 1–279 stop Spastin \ndecorated  MTs,  suggesting  that  amino  acids  280–328  are  important for MT binding (Fig. 2 C).","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"UniProt","id":"P68363","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-29T20:41:39.344Z"}},{"start":270,"end":328,"reference_id":"17389232","reference_source":"pmid","reference_html":"Recognition of C-terminal amino acids in tubulin by pore loops in Spastin is important for microtubule severing. <i> White SR, Evans KJ, Lary J, Cole JL, Lauring B. </i> J Cell Biol, 2007","date":"2022-03-08T13:56:24.838Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006077","ec_ontology":"ECO","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","unpublished":true,"released":"2022_03","version":4,"region_id":"DP03454r003","statement":[{"text":"In addition to the pore interaction with tubulin, we defi ne an N-terminal MT binding domain (MTBD) in  Spastin  that  mediates  the  attachment  of  Spastin  to  the  MT.  \nThis interaction is also required for severing.","type":"Introduction"},{"text":"In contrast, ∆MTBD Spastin neither bound nor severed MTs, demonstrating that aa 270–328 are necessary for MT severing in vitro","type":"Results"},{"text":"In contrast, deletion of the first 328 amino acids did abolish severing activity,  as  the  transfected  cell  still  has  an  MT  array.","type":"Figure"},{"text":"Our  deletion  analysis  revealed  the  existence  of  an  N-terminal MTBD in Spastin (aa 270–328) that is required for MT-severing activity in vivo and in vitro.","type":"Discussion"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":false,"interaction_partner":[{"db":"UniProt","id":"P68363","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-29T20:41:34.903Z"}},{"start":229,"end":322,"reference_id":"29710391","reference_source":"pmid","reference_html":"The AAA protein spastin possesses two levels of basal ATPase activity. <i> Fan X, Lin Z, Fan G, Lu J, Hou Y, Habai G, Sun L, Yu P, Shen Y, Wen M, Wang C. </i> FEBS Lett, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5Z6Q"}],"region_id":"DP03454r004","statement":[{"text":"Similar to the result of a previous structural study of human spastin [30], only the AAA domain was visible in the electron density, while the MTBD region was not visible. ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-03T12:00:47.032Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":4,"released":"2021_12","sequence":"MNSPGGRGKKKGSGGASNPVPPRPPPPCLAPAPPAAGPAPPPESPHKRNLYYFSYPLFVGFALLRLVAFHLGLLFVWLCQRFSRALMAAKRSSGAAPAPASASAPAPVPGGEAERVRVFHKQAFEYISIALRIDEDEKAGQKEQAVEWYKKGIEELEKGIAVIVTGQGEQCERARRLQAKMMTNLVMAKDRLQLLEKMQPVLPFSKSQTDVYNDSTNLACRNGHLQSESGAVPKRKDPLTHTSNSLPRSKTVMKTGSAGLSGHHRAPSYSGLSMVSGVKQGSGPAPTTHKGTPKTNRTNKPSTPTTATRKKKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQDLAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFIKRVYVSLPNEETRLLLLKNLLCKQGSPLTQKELAQLARMTDGYSGSDLTALAKDAALGPIRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTTV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Age-related disorders proteins"],"uniref100":"UniRef100_Q9UBP0","uniref90":"UniRef90_Q9UBP0","uniref50":"UniRef50_Q9UBP0","genes":[{"name":{"value":"SPAST","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03021","url":"https://hamap.expasy.org/unirule/MF_03021"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11233","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11233"}}]},"synonyms":[{"value":"ADPSP"},{"value":"FSP2"},{"value":"KIAA1083","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10470851","url":"http://www.ncbi.nlm.nih.gov/pubmed/10470851","alternativeUrl":"https://europepmc.org/abstract/MED/10470851"}}]},{"value":"SPG4","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03021","url":"https://hamap.expasy.org/unirule/MF_03021"}}]}]}],"alphafold_very_low_content":0.22727272727272727,"disorder_content":0.15584415584415584,"disprot_consensus":{"full":[{"start":228,"end":323,"type":"D"},{"start":324,"end":328,"type":"F"}],"Structural state":[{"start":228,"end":323,"type":"D"}],"Molecular function":[{"start":270,"end":328,"type":"F"}]}},{"disprot_id":"DP03455","acc":"O00189","creator":"maspromonte","date":"2021-08-04T15:53:09.036Z","features":{"pfam":[{"id":"PF00928","name":"Adaptor complexes medium subunit family","start":175,"end":453},{"id":"PF01217","name":"Clathrin adaptor complex small chain","start":42,"end":130}],"gene3D":[]},"length":453,"name":"AP-4 complex subunit mu-1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":160,"end":184,"reference_id":"24498434","reference_source":"pmid","reference_html":"Structural and functional characterization of cargo-binding sites on the μ4-subunit of adaptor protein complex 4. <i> Ross BH, Lin Y, Corales EA, Burgos PV, Mardones GA. </i> PLoS One, 2014","date":"2022-08-04T15:41:01.572Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":4,"cross_refs":[{"db":"PDB","id":"4MDR"}],"region_id":"DP03455r001","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"A close inspection to the crystal structure of either wild-type μ4 (pdb entry 3l81; [18]) or μ4-D190A revealed that the SDQSQKNEVF sequence is at the end of the disordered N-terminal region, in which only the NEVF portion is visible in the crystal structure (Figure 6E)","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp190Ala","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P05067"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-04T17:55:32.591Z"}},{"start":384,"end":399,"reference_id":"24498434","reference_source":"pmid","reference_html":"Structural and functional characterization of cargo-binding sites on the μ4-subunit of adaptor protein complex 4. <i> Ross BH, Lin Y, Corales EA, Burgos PV, Mardones GA. </i> PLoS One, 2014","date":"2022-08-04T08:21:00.928Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":4,"cross_refs":[{"db":"PDB","id":"4MDR"}],"region_id":"DP03455r002","ec_go":"EXP","disprot_namespace":"Structural state","statement":[{"text":"(B) Sequence alignment of the C-terminal domain of the μ subunits of known crystal structure depicting critical residues at the corresponding μ2- and μ4-binding sites. Disordered loops are in yellow letters, and arrows and cylinders represent β-strands and α-helices, respectively. M.m., Mus musculus; R.n., Rattus norvegicus; H.s., Homo sapiens.","type":"Figure"},{"text":"Likewise, the SASPLGLGPA sequence is part of a disordered loop followed by a well-structured region, with the LGLGPA portion visible in the crystal structure (Figure 6E). ","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp190Ala","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P05067"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-04T17:55:24.780Z"}},{"start":384,"end":399,"reference_id":"20230749","reference_source":"pmid","reference_html":"Sorting of the Alzheimer's disease amyloid precursor protein mediated by the AP-4 complex. <i> Burgos PV, Mardones GA, Rojas AL, daSilva LL, Prabhu Y, Hurley JH, Bonifacino JS. </i> Dev Cell, 2010","date":"2022-08-04T08:16:56.724Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":1,"cross_refs":[{"db":"PDB","id":"3L81"}],"region_id":"DP03455r003","statement":[{"text":"Disordered loops are in green (P388-P399) and red (P430-N 435) letters in µ4 and\nin green (V221-G237) and blue (K256-S259) letters in µ2, and are represented in the respective colors as dashed lines in (A).","type":"Supplementary material"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-04T17:56:29.835Z"}}],"regions_counter":3,"released":"2021_12","sequence":"MISQFFILSSKGDPLIYKDFRGDSGGRDVAELFYRKLTGLPGDESPVVMHHHGRHFIHIRHSGLYLVVTTSENVSPFSLLELLSRLATLLGDYCGSLGEGTISRNVALVYELLDEVLDYGYVQTTSTEMLRNFIQTEAVVSKPFSLFDLSSVGLFGAETQQSKVAPSSAASRPVLSSRSDQSQKNEVFLDVVERLSVLIASNGSLLKVDVQGEIRLKSFLPSGSEMRIGLTEEFCVGKSELRGYGPGIRVDEVSFHSSVNLDEFESHRILRLQPPQGELTVMRYQLSDDLPSPLPFRLFPSVQWDRGSGRLQVYLKLRCDLLSKSQALNVRLHLPLPRGVVSLSQELSSPEQKAELAEGALRWDLPRVQGGSQLSGLFQMDVPGPPGPPSHGLSTSASPLGLGPASLSFELPRHTCSGLQVRFLRLAFRPCGNANPHKWVRHLSHSDAYVIRI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"uniref100":"UniRef100_O00189","uniref90":"UniRef90_O00189","uniref50":"UniRef50_O00189","genes":[{"name":{"value":"AP4M1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:574","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:574"}}]},"synonyms":[{"value":"MUARP2"}]}],"alphafold_very_low_content":0.0728476821192053,"disorder_content":0.09050772626931568,"disprot_consensus":{"full":[{"start":160,"end":184,"type":"D"},{"start":384,"end":399,"type":"D"}],"Structural state":[{"start":160,"end":184,"type":"D"},{"start":384,"end":399,"type":"D"}]}},{"disprot_id":"DP03456","acc":"P27635","creator":"msalas","date":"2021-08-04T20:59:37.346Z","features":{"pfam":[{"id":"PF00252","name":"Ribosomal protein L16p/L10e","start":12,"end":165}],"gene3D":[]},"length":214,"name":"60S ribosomal protein L10","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":95,"end":123,"reference_id":"18258260","reference_source":"pmid","reference_html":"Crystal structure of human ribosomal protein L10 core domain reveals eukaryote-specific motifs in addition to the conserved fold. <i> Nishimura M, Kaminishi T, Takemoto C, Kawazoe M, Yoshida T, Tanaka A, Sugano S, Shirouzu M, Ohkubo T, Yokoyama S, Kobayashi Y. </i> J Mol Biol, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"msalas","curator_name":"Martin Salas","curator_orcid":"0000-0001-6352-1282","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"2PA2"}],"region_id":"DP03456r001","statement":[{"text":"The internal missing part, His95– Gln123, corresponds to the internal loop of the TthL16 NMR structure. ","type":"Results"},{"text":"The invisible electron density of His95–Gln123 implies that the internal loop of eukaryotic L10 is also flexible in the free state and assumes a structure by binding on the ribosome.","type":"Results"},{"text":"The internal disordered region (residues His95–Gln123) is indicated by arrows.","type":"Figure"},{"text":"The internal loop of L10CD, Arg98–Gln123, was removed from the search model in advance because the loop was expected to be unstructured considering the NMR analysis of bacterial L16.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-06T06:52:30.862Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MGRRPARCYRYCKNKPYPKSRFCRGVPDAKIRIFDLGRKKAKVDEFPLCGHMVSDEYEQLSSEALEAARICANKYMVKSCGKDGFHIRVRLHPFHVIRINKMLSCAGADRLQTGMRGAFGKPQGTVARVHIGQVIMSIRTKLQNKEHVIEALRRAKFKFPGRQKIHISKKWGFTKFNADEFEDMVAEKRLIPDGCGVKYIPSRGPLDKWRALHS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref100":"UniRef100_P27635","uniref90":"UniRef90_P27635","uniref50":"UniRef50_P27635","genes":[{"name":{"value":"RPL10","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:10298","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:10298"}}]},"synonyms":[{"value":"DXS648E"},{"value":"QM"}]}],"dataset":["NDDs-related proteins","Cancer-related proteins"],"alphafold_very_low_content":0,"disorder_content":0.13551401869158877,"disprot_consensus":{"full":[{"start":95,"end":123,"type":"D"}],"Structural state":[{"start":95,"end":123,"type":"D"}]}},{"disprot_id":"DP03457","acc":"Q29502","creator":"eleonardi","date":"2021-08-05T08:11:42.700Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":249,"end":500},{"id":"PF00786","name":"P21-Rho-binding domain","start":73,"end":130}],"gene3D":[]},"length":524,"name":"Serine/threonine-protein kinase PAK 2","ncbi_taxon_id":9986,"organism":"Oryctolagus cuniculus","regions":[{"start":125,"end":238,"reference_id":"18984590","reference_source":"pmid","reference_html":"Analysis of conformational changes during activation of protein kinase Pak2 by amide hydrogen/deuterium exchange. <i> Hsu YH, Johnson DA, Traugh JA. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03457r001","statement":[{"text":"The entire mass spectrum of pepsin-digested Pak2 is shown in Fig. 3a. 30 of 42 identified peptides had m/z ratios that were sufficiently different from one another and of sufficient magnitude to use in the amide H/D exchange experiments discussed below. These peptides covered 50% of the primary sequence of Pak2, including all or part of the following regions: the N-terminal region, dimerization domain, AID, glycine-rich loop, C helix, catalytic loop, magnesium-positioning loop, activation loop, and regions without an identified function.","type":"Results"},{"text":"FIGURE 4. Solvent accessibility of inactive Pak2. a, the Pak2 sequence and the peptic peptides identified after 10 min of H/D exchange of Pak2 are color coded according to level of deuterium incorporation into exchangeable amides.","type":"Figure"},{"text":"Figure 4 shows that the region ranging 125-238 is completely digested by pepsin.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T12:14:49.394Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":18,"end":57,"reference_id":"18984590","reference_source":"pmid","reference_html":"Analysis of conformational changes during activation of protein kinase Pak2 by amide hydrogen/deuterium exchange. <i> Hsu YH, Johnson DA, Traugh JA. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03457r002","statement":[{"text":"FIGURE 4. Solvent accessibility of inactive Pak2. a, the Pak2 sequence and the peptic peptides identified after 10 min of H/D exchange of Pak2 are color coded according to level of deuterium incorporation into exchangeable amides.","type":"Figure"},{"text":"The entire mass spectrum of pepsin-digested Pak2 is shown in Fig. 3a. 30 of 42 identified peptides had m/z ratios that were sufficiently different from one another and of sufficient magnitude to use in the amide H/D exchange experiments discussed below. These peptides covered 50% of the primary sequence of Pak2, including all or part of the following regions: the N-terminal region, dimerization domain, AID, glycine-rich loop, C helix, catalytic loop, magnesium-positioning loop, activation loop, and regions without an identified function.","type":"Results"},{"text":"Figure 4 shows that the region ranging 18-57 is completely digested by pepsin.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T12:14:50.170Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":253,"end":281,"reference_id":"18984590","reference_source":"pmid","reference_html":"Analysis of conformational changes during activation of protein kinase Pak2 by amide hydrogen/deuterium exchange. <i> Hsu YH, Johnson DA, Traugh JA. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03457r003","statement":[{"text":"FIGURE 4. Solvent accessibility of inactive Pak2. a, the Pak2 sequence and the peptic peptides identified after 10 min of H/D exchange of Pak2 are color coded according to level of deuterium incorporation into exchangeable amides.","type":"Figure"},{"text":"The entire mass spectrum of pepsin-digested Pak2 is shown in Fig. 3a. 30 of 42 identified peptides had m/z ratios that were sufficiently different from one another and of sufficient magnitude to use in the amide H/D exchange experiments discussed below. These peptides covered 50% of the primary sequence of Pak2, including all or part of the following regions: the N-terminal region, dimerization domain, AID, glycine-rich loop, C helix, catalytic loop, magnesium-positioning loop, activation loop, and regions without an identified function.","type":"Results"},{"text":"Figure 4 shows that the region ranging 253-281 is completely digested by pepsin.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T12:14:52.371Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":310,"end":356,"reference_id":"18984590","reference_source":"pmid","reference_html":"Analysis of conformational changes during activation of protein kinase Pak2 by amide hydrogen/deuterium exchange. <i> Hsu YH, Johnson DA, Traugh JA. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03457r004","statement":[{"text":"FIGURE 4. Solvent accessibility of inactive Pak2. a, the Pak2 sequence and the peptic peptides identified after 10 min of H/D exchange of Pak2 are color coded according to level of deuterium incorporation into exchangeable amides.","type":"Figure"},{"text":"The entire mass spectrum of pepsin-digested Pak2 is shown in Fig. 3a. 30 of 42 identified peptides had m/z ratios that were sufficiently different from one another and of sufficient magnitude to use in the amide H/D exchange experiments discussed below. These peptides covered 50% of the primary sequence of Pak2, including all or part of the following regions: the N-terminal region, dimerization domain, AID, glycine-rich loop, C helix, catalytic loop, magnesium-positioning loop, activation loop, and regions without an identified function.","type":"Results"},{"text":"Figure 4 shows that the region ranging 310-356 is completely digested by pepsin.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T12:14:54.049Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":1,"end":17,"reference_id":"18984590","reference_source":"pmid","reference_html":"Analysis of conformational changes during activation of protein kinase Pak2 by amide hydrogen/deuterium exchange. <i> Hsu YH, Johnson DA, Traugh JA. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03457r005","statement":[{"text":"In addition, caspase cleavage and autophosphorylation dramatically and specifically increased deuteron incorporation into the N-terminal -5–17 fragment by about five deuterons, bringing the level of incorporation to 90% of the maximum, and indicating a region of high solvent exposure/flexibility (Table 1).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T12:14:48.678Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":1,"end":17,"reference_id":"18984590","reference_source":"pmid","reference_html":"Analysis of conformational changes during activation of protein kinase Pak2 by amide hydrogen/deuterium exchange. <i> Hsu YH, Johnson DA, Traugh JA. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03457r006","statement":[{"text":"In addition, caspase cleavage and autophosphorylation dramatically and specifically increased deuteron incorporation into the N-terminal -5–17 fragment by about five deuterons, bringing the level of incorporation to 90% of the maximum, and indicating a region of high solvent exposure/flexibility (Table 1).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-05T13:02:15.347Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":6,"released":"2021_12","sequence":"MSDNGELEDKPPAPPVRMSSTIFSTGGKDPLSANHSLKPLPSVPEEKKPRNKIISIFSGTEKGSKKKEKERPEISPPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSNTVKQKYLSFTPPEKDGFPSGAPALNTKVSETSAVVTEEDDDDEEAAPPVIAPRPDHTKSIYTRSVIDPIPAPVGDSHVDSGAKSSDKQKKKTKMTDEEIMEKLRTIVSIGDPKKKYTRYEKIGQGASGTVFTATDVALGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSYLVGDELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMEGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLIMAAKEAMKSNR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Lagomorpha","Leporidae","Oryctolagus"],"uniref100":"UniRef100_Q29502","uniref90":"UniRef90_Q29502","uniref50":"UniRef50_Q13177","genes":[{"name":{"value":"PAK2"}}],"alphafold_very_low_content":0.28435114503816794,"disorder_content":0.4713740458015267,"disprot_consensus":{"full":[{"start":1,"end":17,"type":"T"},{"start":18,"end":57,"type":"D"},{"start":125,"end":238,"type":"D"},{"start":253,"end":281,"type":"D"},{"start":310,"end":356,"type":"D"}],"Structural state":[{"start":1,"end":57,"type":"D"},{"start":125,"end":238,"type":"D"},{"start":253,"end":281,"type":"D"},{"start":310,"end":356,"type":"D"}],"Structural transition":[{"start":1,"end":17,"type":"T"}]}},{"disprot_id":"DP03458","acc":"P0DMC7","creator":"jnilsson","date":"2021-08-05T12:40:36.656Z","features":{"pfam":[{"id":"PF00072","name":"Response regulator receiver domain","start":6,"end":120},{"id":"PF00196","name":"Bacterial regulatory proteins, luxR family","start":150,"end":202}],"gene3D":[]},"length":216,"name":"Transcriptional regulatory protein RcsB","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":133,"end":147,"reference_id":"27670836","reference_source":"pmid","reference_html":"Crystal structure of nonphosphorylated receiver domain of the stress response regulator RcsB from Escherichia coli. <i> Filippova EV, Wawrzak Z, Ruan J, Pshenychnyi S, Schultz RM, Wolfe AJ, Anderson WF. </i> Protein Sci, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"5I4C"}],"region_id":"DP03458r001","statement":[{"text":" The first N-terminal residue and 15 C-terminal residues comprising part of the inter-domain linker were not ordered in the electron density map. ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-03T08:27:44.223Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MNNMNVIIADDHPIVLFGIRKSLEQIEWVNVVGEFEDSTALINNLPKLDAHVLITDLSMPGDKYGDGITLIKYIKRHFPSLSIIVLTMNNNPAILSAVLDLDIEGIVLKQGAPTDLPKALAALQKGKKFTPESVSRLLEKISAGGYGDKRLSPKESEVLRLFAEGFLVTEIAKKLNRSIKTISSQKKSAMMKLGVENDIALLNYLSSVTLSPADKD","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref100":"UniRef100_P0DMC8","uniref90":"UniRef90_P0DMC8","uniref50":"UniRef50_P0DMC8","genes":[{"name":{"value":"rcsB","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00981","url":"https://hamap.expasy.org/unirule/MF_00981"}}]},"olnNames":[{"value":"b2217"},{"value":"JW2205"}]}],"alphafold_very_low_content":0.027777777777777776,"disorder_content":0.06944444444444445,"disprot_consensus":{"full":[{"start":133,"end":147,"type":"D"}],"Structural state":[{"start":133,"end":147,"type":"D"}]}},{"disprot_id":"DP03459","acc":"Q15542","creator":"maspromonte","date":"2021-08-05T14:22:28.860Z","features":{"pfam":[{"id":"PF00400","name":"WD domain, G-beta repeat","start":468,"end":498},{"id":"PF00400","name":"WD domain, G-beta repeat","start":535,"end":571},{"id":"PF00400","name":"WD domain, G-beta repeat","start":576,"end":612},{"id":"PF00400","name":"WD domain, G-beta repeat","start":618,"end":655},{"id":"PF00400","name":"WD domain, G-beta repeat","start":659,"end":697},{"id":"PF00400","name":"WD domain, G-beta repeat","start":704,"end":739},{"id":"PF04494","name":"WD40 associated region in TFIID subunit, NTD2 domain","start":209,"end":337}],"gene3D":[]},"length":800,"name":"Transcription initiation factor TFIID subunit 5","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":381,"end":416,"reference_id":"30510221","reference_source":"pmid","reference_html":"Chaperonin CCT checkpoint function in basal transcription factor TFIID assembly. <i> Antonova SV, Haffke M, Corradini E, Mikuciunas M, Low TY, Signor L, van Es RM, Gupta K, Scheer E, Vos HR, Tora L, Heck AJR, Timmers HTM, Berger I. </i> Nat Struct Mol Biol, 2018","date":"2022-09-29T08:29:45.879Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":3,"cross_refs":[{"db":"PDB","id":"6F3T"}],"region_id":"DP03459r001","statement":[{"text":"Disordered loops are drawn as grey dashed lines.","type":"Figure"},{"text":"The final model includes residues 207-800 of TAF5 (residues 194-206, 381-416 and 748-753 were not modeled due to poor definition), residues 6-92 of TAF6 and residues 5-120 of TAF9.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P49848"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q16594"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-29T13:14:21.366Z"}},{"start":194,"end":206,"reference_id":"30510221","reference_source":"pmid","reference_html":"Chaperonin CCT checkpoint function in basal transcription factor TFIID assembly. <i> Antonova SV, Haffke M, Corradini E, Mikuciunas M, Low TY, Signor L, van Es RM, Gupta K, Scheer E, Vos HR, Tora L, Heck AJR, Timmers HTM, Berger I. </i> Nat Struct Mol Biol, 2018","date":"2022-09-29T08:30:24.165Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6F3T"}],"region_id":"DP03459r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P49848"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q16594"}],"statement":[{"text":"The final model includes residues 207-800 of TAF5 (residues 194-206, 381-416 and 748-753 were not modeled due to poor definition), residues 6-92 of TAF6 and residues 5-120 of TAF9.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-29T13:14:22.896Z"}}],"regions_counter":2,"released":"2021_12","sequence":"MAALAEEQTEVAVKLEPEGPPTLLPPQAGDGAGEGSGGTTNNGPNGGGGNVAASSSTGGDGGTPKPTVAVSAAAPAGAAPVPAAAPDAGAPHDRQTLLAVLQFLRQSKLREAEEALRREAGLLEEAVAGSGAPGEVDSAGAEVTSALLSRVTASAPGPAAPDPPGTGASGATVVSGSASGPAAPGKVGSVAVEDQPDVSAVLSAYNQQGDPTMYEEYYSGLKHFIECSLDCHRAELSQLFYPLFVHMYLELVYNQHENEAKSFFEKFHGDQECYYQDDLRVLSSLTKKEHMKGNETMLDFRTSKFVLRISRDSYQLLKRHLQEKQNNQIWNIVQEHLYIDIFDGMPRSKQQIDAMVGSLAGEAKREANKSKVFFGLLKEPEIEVPLDDEDEEGENEEGKPKKKKPKKDSIGSKSKKQDPNAPPQNRIPLPELKDSDKLDKIMNMKETTKRVRLGPDCLPSICFYTFLNAYQGLTAVDVTDDSSLIAGGFADSTVRVWSVTPKKLRSVKQASDLSLIDKESDDVLERIMDEKTASELKILYGHSGPVYGASFSPDRNYLLSSSEDGTVRLWSLQTFTCLVGYKGHNYPVWDTQFSPYGYYFVSGGHDRVARLWATDHYQPLRIFAGHLADVNCTRFHPNSNYVATGSADRTVRLWDVLNGNCVRIFTGHKGPIHSLTFSPNGRFLATGATDGRVLLWDIGHGLMVGELKGHTDTVCSLRFSRDGEILASGSMDNTVRLWDAIKAFEDLETDDFTTATGHINLPENSQELLLGTYMTKSTPVVHLHFTRRNLVLAAGAYSPQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref100":"UniRef100_Q15542","uniref90":"UniRef90_Q15542","uniref50":"UniRef50_Q15542","genes":[{"name":{"value":"TAF5"},"synonyms":[{"value":"TAF2D"}]}],"alphafold_very_low_content":0.25875,"disorder_content":0.06125,"disprot_consensus":{"full":[{"start":194,"end":206,"type":"D"},{"start":381,"end":416,"type":"D"}],"Structural state":[{"start":194,"end":206,"type":"D"},{"start":381,"end":416,"type":"D"}]}},{"disprot_id":"DP03460","acc":"P0DTC7","creator":"fquaglia","date":"2021-08-06T07:39:26.582Z","features":{"pfam":[{"id":"PF08779","name":"Betacoronavirus NS7A protein","start":16,"end":121}],"gene3D":[]},"length":121,"name":"ORF7a protein","ncbi_taxon_id":2697049,"organism":"Severe acute respiratory syndrome coronavirus 2","regions":[{"start":83,"end":96,"reference_id":"33615195","reference_source":"pmid","reference_html":"Structural insight reveals SARS-CoV-2 ORF7a as an immunomodulating factor for human CD14<sup>+</sup> monocytes. <i> Zhou Z, Huang C, Zhou Z, Huang Z, Su L, Kang S, Chen X, Chen Q, He S, Rong X, Xiao F, Chen J, Chen S. </i> iScience, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"7CI3"}],"region_id":"DP03460r001","statement":[{"text":"The final structure, with a visible electron density spanning residues 14–82, was refined to R factor and R-free values of 0.201 and 0.246, respectively.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-08-06T08:03:13.055Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MKIILFLALITLATCELYHYQECVRGTTVLLKEPCSSGTYEGNSPFHPLADNKFALTCFSTQFAFACPDGVKHVYQLRARSVSPKLFIRQEEVQELYSPIFLIVAAIVFITLCFTLKRKTE","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Nidovirales","Cornidovirineae","Coronaviridae","Orthocoronavirinae","Betacoronavirus","Sarbecovirus"],"uniref100":"UniRef100_P0DTC7","uniref90":"UniRef90_P0DTC7","uniref50":"UniRef50_P0DTC7","dataset":["Viral proteins"],"genes":[{"orfNames":[{"value":"7a"}]}],"disorder_content":0.11570247933884298,"disprot_consensus":{"full":[{"start":83,"end":96,"type":"D"}],"Structural state":[{"start":83,"end":96,"type":"D"}]}},{"disprot_id":"DP03464","acc":"Q04195","creator":"jpujols","date":"2021-09-03T11:05:01.757Z","features":{"pfam":[{"id":"PF02037","name":"SAP domain","start":35,"end":68},{"id":"PF02891","name":"MIZ/SP-RING zinc finger","start":357,"end":405},{"id":"PF14324","name":"PINIT domain","start":175,"end":312}],"gene3D":[]},"length":904,"name":"E3 SUMO-protein ligase SIZ1","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":445,"end":465,"reference_id":"19748360","reference_source":"pmid","reference_html":"Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA. <i> Yunus AA, Lima CD. </i> Mol Cell, 2009","date":"2022-11-16T15:35:19.939Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3I2D"}],"region_id":"DP03464r002","statement":[{"text":"Amino acids 112–158, 348–352, and 445–465 were present in the crystal and presumed disordered.","type":"Results"}]}],"regions_counter":2,"released":"2023_12","sequence":"MINLEDYWEDETPGPDREPTNELRNEVEETITLMELLKVSELKDICRSVSFPVSGRKAVLQDLIRNFLQNALVVGKSDPYRVQAVKFLIERIRKNEPLPVYKDLWNALRKGTPLSAITVRSMEGPPTVQQQSPSVIRQSPTQRRKTSTTSSTSRAPPPTNPDASSSSSSFAVPTIHFKESPFYKIQRLIPELVMNVEVTGGRGMCSAKFKLSKADYNLLSNPNSKHRLYLFSGMINPLGSRGNEPIQFPFPNELRCNNVQIKDNIRGFKSKPGTAKPADLTPHLKPYTQQNNVELIYAFTTKEYKLFGYIVEMITPEQLLEKVLQHPKIIKQATLLYLKKTLREDEEMGLTTTSTIMSLQCPISYTRMKYPSKSINCKHLQCFDALWFLHSQLQIPTWQCPVCQIDIALENLAISEFVDDILQNCQKNVEQVELTSDGKWTAILEDDDDSDSDSNDGSRSPEKGTSVSDHHCSSSHPSEPIIINLDSDDDEPNGNNPHVTNNHDDSNRHSNDNNNNSIKNNDSHNKNNNNNNNNNNNNNDNNNSIENNDSNSNNKHDHGSRSNTPSHNHTKNLMNDNDDDDDDRLMAEITSNHLKSTNTDILTEKGSSAPSRTLDPKSYNIVASETTTPVTNRVIPEYLGNSSSYIGKQLPNILGKTPLNVTAVDNSSHLISPDVSVSSPTPRNTASNASSSALSTPPLIRMSSLDPRGSTVPDKTIRPPINSNSYTASISDSFVQPQESSVFPPREQNMDMSFPSTVNSRFNDPRLNTTRFPDSTLRGATILSNNGLDQRNNSLPTTEAITRNDVGRQNSTPVLPTLPQNVPIRTNSNKSGLPLINNENSVPNPPNTATIPLQKSRLIVNPFIPRRPYSNVLPQKRQLSNTSSTSPIMGTWKTQDYGKKYNSG","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref50":"UniRef50_Q04195","uniref90":"UniRef90_Q04195","uniref100":"UniRef100_Q04195","genes":[{"name":{"value":"SIZ1"},"synonyms":[{"value":"ULL1"}],"olnNames":[{"value":"YDR409W"}]}],"alphafold_very_low_content":0.5453539823008849,"disorder_content":0.023230088495575223,"disprot_consensus":{"full":[{"start":445,"end":465,"type":"D"}],"Structural state":[{"start":445,"end":465,"type":"D"}]}},{"disprot_id":"DP03465","acc":"Q9T0N8","creator":"ppereira","date":"2021-09-08T13:14:04.816Z","features":{"pfam":[{"id":"PF01565","name":"FAD binding domain","start":69,"end":214},{"id":"PF09265","name":"Cytokinin dehydrogenase 1, FAD and cytokinin binding","start":246,"end":533}],"gene3D":[]},"length":534,"name":"Cytokinin dehydrogenase 1","ncbi_taxon_id":4577,"organism":"Zea mays","regions":[{"start":19,"end":32,"reference_id":"26519657","reference_source":"pmid","reference_html":"Kinetic and structural investigation of the cytokinin oxidase/dehydrogenase active site. <i> Kopečný D, Končitíková R, Popelka H, Briozzo P, Vigouroux A, Kopečná M, Zalabák D, Šebela M, Skopalová J, Frébort I, Moréra S. </i> FEBS J, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3S1C"},{"db":"PDB","id":"3S1D"},{"db":"PDB","id":"3S1F"},{"db":"PDB","id":"3S1E"}],"region_id":"DP03465r001","statement":[{"text":"The region following the signal peptide (1-18) is missing in the coordinates of the 4 structures (see cross references).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T09:03:21.421Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":19,"end":32,"reference_id":"20478354","reference_source":"pmid","reference_html":"Phenyl- and benzylurea cytokinins as competitive inhibitors of cytokinin oxidase/dehydrogenase: a structural study. <i> Kopecný D, Briozzo P, Popelková H, Sebela M, Koncitíková R, Spíchal L, Nisler J, Madzak C, Frébort I, Laloue M, Houba-Hérin N. </i> Biochimie, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2QPM"},{"db":"PDB","id":"2QKN"},{"db":"PDB","id":"3KJM"}],"region_id":"DP03465r002","statement":[{"text":"The region following the signal peptide (1-18) is missing in the coordinates of the 3 structures (see cross references).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T09:53:31.052Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":19,"end":39,"reference_id":"15321719","reference_source":"pmid","reference_html":"Structures of Michaelis and product complexes of plant cytokinin dehydrogenase: implications for flavoenzyme catalysis. <i> Malito E, Coda A, Bilyeu KD, Fraaije MW, Mattevi A. </i> J Mol Biol, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"1W1R"},{"db":"PDB","id":"1W1S"},{"db":"PDB","id":"1W1Q"},{"db":"PDB","id":"1W1O"}],"region_id":"DP03465r003","statement":[{"text":"The N-terminal 40 amino acid residues are not visible in the electron density map, in agreement with the observation that CKX is produced as a precursor protein undergoing an N-terminal cleavage upon processing.","type":"Results"},{"text":"The protein has an 18-residue signal peptide, which is not present in the structure of the mature form. The remaining residues (19-39) are disordered and were not modeled.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T10:45:45.068Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":19,"end":31,"reference_id":"18571199","reference_source":"pmid","reference_html":"Mechanism-based inhibitors of cytokinin oxidase/dehydrogenase attack FAD cofactor. <i> Kopecný D, Sebela M, Briozzo P, Spíchal L, Houba-Hérin N, Masek V, Joly N, Madzak C, Anzenbacher P, Laloue M. </i> J Mol Biol, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3BW7"}],"region_id":"DP03465r004","statement":[{"text":"It was possible to fit to electron density an additional part, GRPWPASLA, at the N-terminus, leaving only 12 amino acids disordered. In addition, the sequence segments DNATAAA (amino acids 337–343) and VAP (amino acids 462–464), all missing in the 1W1O Protein Data Bank (PDB) file, could be constructed.","type":"Results"},{"text":"Since the protein has an 18-residue signal peptide, there are 13 disordered residues for structure 3BW7 and 14 for 3C0P.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T10:38:57.515Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":19,"end":32,"reference_id":"18571199","reference_source":"pmid","reference_html":"Mechanism-based inhibitors of cytokinin oxidase/dehydrogenase attack FAD cofactor. <i> Kopecný D, Sebela M, Briozzo P, Spíchal L, Houba-Hérin N, Masek V, Joly N, Madzak C, Anzenbacher P, Laloue M. </i> J Mol Biol, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3C0P"}],"region_id":"DP03465r005","statement":[{"text":"It was possible to fit to electron density an additional part, GRPWPASLA, at the N-terminus, leaving only 12 amino acids disordered. In addition, the sequence segments DNATAAA (amino acids 337–343) and VAP (amino acids 462–464), all missing in the 1W1O Protein Data Bank (PDB) file, could be constructed.","type":"Results"},{"text":"Since the protein has an 18-residue signal peptide, there are 13 disordered residues for structure 3BW7 and 14 for 3C0P.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T10:38:56.020Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":5,"released":"2021_12","sequence":"MAVVYYLLLAGLIACSHALAAGTPALGDDRGRPWPASLAALALDGKLRTDSNATAAASTDFGNITSALPAAVLYPSSTGDLVALLSAANSTPGWPYTIAFRGRGHSLMGQAFAPGGVVVNMASLGDAAAPPRINVSADGRYVDAGGEQVWIDVLRASLARGVAPRSWNDYLYLTVGGTLSNAGISGQAFRHGPQISNVLEMDVITGHGEMVTCSKQLNADLFDAVLGGLGQFGVITRARIAVEPAPARARWVRFVYTDFAAFSADQERLTAPRPGGGGASFGPMSYVEGSVFVNQSLATDLANTGFFTDADVARIVALAGERNATTVYSIEATLNYDNATAAAAAVDQELASVLGTLSYVEGFAFQRDVAYAAFLDRVHGEEVALNKLGLWRVPHPWLNMFVPRSRIADFDRGVFKGILQGTDIVGPLIVYPLNKSMWDDGMSAATPSEDVFYAVSLLFSSVAPNDLARLQEQNRRILRFCDLAGIQYKTYLARHTDRSDWVRHFGAAKWNRFVEMKNKYDPKRLLSPGQDIFN","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","PACMAD clade","Panicoideae","Andropogonodae","Andropogoneae","Tripsacinae","Zea"],"uniref50":"UniRef50_Q9T0N8","uniref90":"UniRef90_Q9T0N8","uniref100":"UniRef100_Q9T0N8","genes":[{"name":{"value":"CKX1"}}],"alphafold_very_low_content":0.04868913857677903,"disorder_content":0.03932584269662921,"disprot_consensus":{"full":[{"start":19,"end":39,"type":"D"}],"Structural state":[{"start":19,"end":39,"type":"D"}]}},{"disprot_id":"DP03466","acc":"E3T1W8","creator":"ppereira","date":"2021-09-08T14:05:47.444Z","features":{"pfam":[{"id":"PF01565","name":"FAD binding domain","start":66,"end":215},{"id":"PF09265","name":"Cytokinin dehydrogenase 1, FAD and cytokinin binding","start":247,"end":529}],"gene3D":[]},"length":541,"name":"Cytokinin dehydrogenase","ncbi_taxon_id":4577,"organism":"Zea mays","regions":[{"start":292,"end":319,"reference_id":"26519657","reference_source":"pmid","reference_html":"Kinetic and structural investigation of the cytokinin oxidase/dehydrogenase active site. <i> Kopečný D, Končitíková R, Popelka H, Briozzo P, Vigouroux A, Kopečná M, Zalabák D, Šebela M, Skopalová J, Frébort I, Moréra S. </i> FEBS J, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"4OAL"}],"region_id":"DP03466r001","statement":[{"text":"The helix-loop-helix region from residues 294-325 in ZmCKO1 (shown with red arrows) adopts a different conformation in ZmCKO2 (PDB ID: 4ML8, this work) and is disordered in ZmCKO4a (PDB ID 4OAL, this work).","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T09:06:57.242Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":292,"end":319,"reference_id":"26519657","reference_source":"pmid","reference_html":"Kinetic and structural investigation of the cytokinin oxidase/dehydrogenase active site. <i> Kopečný D, Končitíková R, Popelka H, Briozzo P, Vigouroux A, Kopečná M, Zalabák D, Šebela M, Skopalová J, Frébort I, Moréra S. </i> FEBS J, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"4OAL"}],"region_id":"DP03466r002","statement":[{"text":"The helix-loop-helix region from residues 294-325 in ZmCKO1 (shown with red arrows) adopts a different conformation in ZmCKO2 (PDB ID: 4ML8, this work) and is disordered in ZmCKO4a (PDB ID 4OAL, this work).","type":"Figure"},{"text":"This region, which is well defined in the ZmCKO1 structure, is disordered in the high resolution structures of ZmCKO4a and ZmCKO2\nand adopts a different conformation in the low resolution structure of ZmCKO2 (Fig. 4A). The region delineating the substrate entrance comprises residues surrounding the ribose moiety of cytokinin substrate (N303 and T304 in ZmCKO1) and is most likely responsible for the kinetic differences between the E381 variants and the ZmCKO isoforms.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T09:08:11.439Z"},"ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":292,"end":318,"reference_id":"26519657","reference_source":"pmid","reference_html":"Kinetic and structural investigation of the cytokinin oxidase/dehydrogenase active site. <i> Kopečný D, Končitíková R, Popelka H, Briozzo P, Vigouroux A, Kopečná M, Zalabák D, Šebela M, Skopalová J, Frébort I, Moréra S. </i> FEBS J, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"4O95"}],"region_id":"DP03466r003","statement":[{"text":"The helix-loop-helix region from residues 294-325 in ZmCKO1 (shown with red arrows) adopts a different conformation in ZmCKO2 (PDB ID: 4ML8, this work) and is disordered in ZmCKO4a (PDB ID 4OAL, this work).","type":"Figure"},{"text":"This region, which is well defined in the ZmCKO1 structure, is disordered in the high resolution structures of ZmCKO4a and ZmCKO2\nand adopts a different conformation in the low resolution structure of ZmCKO2 (Fig. 4A). The region delineating the substrate entrance comprises residues surrounding the ribose moiety of cytokinin substrate (N303 and T304 in ZmCKO1) and is most likely responsible for the kinetic differences between the E381 variants and the ZmCKO isoforms.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T09:07:56.522Z"},"ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":292,"end":318,"reference_id":"26519657","reference_source":"pmid","reference_html":"Kinetic and structural investigation of the cytokinin oxidase/dehydrogenase active site. <i> Kopečný D, Končitíková R, Popelka H, Briozzo P, Vigouroux A, Kopečná M, Zalabák D, Šebela M, Skopalová J, Frébort I, Moréra S. </i> FEBS J, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"4O95"}],"region_id":"DP03466r004","statement":[{"text":"The helix-loop-helix region from residues 294-325 in ZmCKO1 (shown with red arrows) adopts a different conformation in ZmCKO2 (PDB ID: 4ML8, this work) and is disordered in ZmCKO4a (PDB ID 4OAL, this work).","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T09:06:58.110Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":532,"end":541,"reference_id":"26519657","reference_source":"pmid","reference_html":"Kinetic and structural investigation of the cytokinin oxidase/dehydrogenase active site. <i> Kopečný D, Končitíková R, Popelka H, Briozzo P, Vigouroux A, Kopečná M, Zalabák D, Šebela M, Skopalová J, Frébort I, Moréra S. </i> FEBS J, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"4O95"},{"db":"PDB","id":"4OAL"}],"region_id":"DP03466r005","statement":[{"text":"The C-terminal decapeptide is unmodelled in both structures (see cross references) of this enzyme.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T09:07:34.146Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":22,"end":38,"reference_id":"26519657","reference_source":"pmid","reference_html":"Kinetic and structural investigation of the cytokinin oxidase/dehydrogenase active site. <i> Kopečný D, Končitíková R, Popelka H, Briozzo P, Vigouroux A, Kopečná M, Zalabák D, Šebela M, Skopalová J, Frébort I, Moréra S. </i> FEBS J, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"4O95"},{"db":"PDB","id":"4OAL"}],"region_id":"DP03466r006","statement":[{"text":"The N-terminal segment, following the signal peptide (1-21), is unmodelled in both structures (see cross references) of this enzyme.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T09:04:54.725Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":22,"end":39,"reference_id":"27095406","reference_source":"pmid","reference_html":"Cytokinin metabolism in maize: Novel evidence of cytokinin abundance, interconversions and formation of a new trans-zeatin metabolic product with a weak anticytokinin activity. <i> Hluska T, Dobrev PI, Tarkowská D, Frébortová J, Zalabák D, Kopečný D, Plíhal O, Kokáš F, Briozzo P, Zatloukal M, Motyka V, Galuszka P. </i> Plant Sci, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"5HHZ"}],"region_id":"DP03466r007","statement":[{"text":"The N-terminal segment, following the signal peptide (1-21), is unmodelled in the structure (see cross reference) of this enzyme.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T07:53:06.404Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":295,"end":312,"reference_id":"27095406","reference_source":"pmid","reference_html":"Cytokinin metabolism in maize: Novel evidence of cytokinin abundance, interconversions and formation of a new trans-zeatin metabolic product with a weak anticytokinin activity. <i> Hluska T, Dobrev PI, Tarkowská D, Frébortová J, Zalabák D, Kopečný D, Plíhal O, Kokáš F, Briozzo P, Zatloukal M, Motyka V, Galuszka P. </i> Plant Sci, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"5HHZ"}],"region_id":"DP03466r008","statement":[{"text":"This region is missing from the structural model (see cross reference) of this enzyme.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T07:52:00.352Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":532,"end":541,"reference_id":"27095406","reference_source":"pmid","reference_html":"Cytokinin metabolism in maize: Novel evidence of cytokinin abundance, interconversions and formation of a new trans-zeatin metabolic product with a weak anticytokinin activity. <i> Hluska T, Dobrev PI, Tarkowská D, Frébortová J, Zalabák D, Kopečný D, Plíhal O, Kokáš F, Briozzo P, Zatloukal M, Motyka V, Galuszka P. </i> Plant Sci, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"5HHZ"}],"region_id":"DP03466r009","statement":[{"text":"The C-terminal decapeptide is unmodelled in the structure (see cross reference) of this enzyme.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T07:50:48.622Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":532,"end":541,"reference_id":"27422623","reference_source":"pmid","reference_html":"Novel thidiazuron-derived inhibitors of cytokinin oxidase/dehydrogenase. <i> Nisler J, Kopečný D, Končitíková R, Zatloukal M, Bazgier V, Berka K, Zalabák D, Briozzo P, Strnad M, Spíchal L. </i> Plant Mol Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"5HMR"}],"region_id":"DP03466r010","statement":[{"text":"The C-terminal decapeptide is unmodelled in the structure (see cross reference) of this enzyme.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T07:40:55.570Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":22,"end":39,"reference_id":"27422623","reference_source":"pmid","reference_html":"Novel thidiazuron-derived inhibitors of cytokinin oxidase/dehydrogenase. <i> Nisler J, Kopečný D, Končitíková R, Zatloukal M, Bazgier V, Berka K, Zalabák D, Briozzo P, Strnad M, Spíchal L. </i> Plant Mol Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"5HMR"}],"region_id":"DP03466r011","statement":[{"text":"The N-terminal segment, following the signal peptide (1-21), is unmodelled in the structure (see cross reference) of this enzyme.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T08:38:35.401Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":22,"end":37,"reference_id":"27422623","reference_source":"pmid","reference_html":"Novel thidiazuron-derived inhibitors of cytokinin oxidase/dehydrogenase. <i> Nisler J, Kopečný D, Končitíková R, Zatloukal M, Bazgier V, Berka K, Zalabák D, Briozzo P, Strnad M, Spíchal L. </i> Plant Mol Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"5HQX"}],"region_id":"DP03466r012","statement":[{"text":"The N-terminal segment, following the signal peptide (1-21), is unmodelled in the structure (see cross reference) of this enzyme.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T08:38:32.418Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":293,"end":318,"reference_id":"27422623","reference_source":"pmid","reference_html":"Novel thidiazuron-derived inhibitors of cytokinin oxidase/dehydrogenase. <i> Nisler J, Kopečný D, Končitíková R, Zatloukal M, Bazgier V, Berka K, Zalabák D, Briozzo P, Strnad M, Spíchal L. </i> Plant Mol Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"5HQX"}],"region_id":"DP03466r013","statement":[{"text":"This region is missing from the structural model (see cross reference) of this enzyme.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T08:38:31.217Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":292,"end":318,"reference_id":"27422623","reference_source":"pmid","reference_html":"Novel thidiazuron-derived inhibitors of cytokinin oxidase/dehydrogenase. <i> Nisler J, Kopečný D, Končitíková R, Zatloukal M, Bazgier V, Berka K, Zalabák D, Briozzo P, Strnad M, Spíchal L. </i> Plant Mol Biol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"5HMR"}],"region_id":"DP03466r014","statement":[{"text":"This region is missing from the structural model (see cross reference) of this enzyme.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T08:38:29.841Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":294,"end":318,"reference_id":"32945834","reference_source":"pmid","reference_html":"Diphenylurea-derived cytokinin oxidase/dehydrogenase inhibitors for biotechnology and agriculture. <i> Nisler J, Kopečný D, Pěkná Z, Končitíková R, Koprna R, Murvanidze N, Werbrouck SPO, Havlíček L, De Diego N, Kopečná M, Wimmer Z, Briozzo P, Moréra S, Zalabák D, Spíchal L, Strnad M. </i> J Exp Bot, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"6YAO"},{"db":"PDB","id":"6YAP"}],"region_id":"DP03466r015","statement":[{"text":"A significant difference is the presence of two helices (α10 and α11) above the entrance to the substrate channel, which is similar to the structure of ZmCKX1. On the contrary, the equivalent region is highly disordered in ZmCKX4.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T07:09:39.995Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":22,"end":39,"reference_id":"32945834","reference_source":"pmid","reference_html":"Diphenylurea-derived cytokinin oxidase/dehydrogenase inhibitors for biotechnology and agriculture. <i> Nisler J, Kopečný D, Pěkná Z, Končitíková R, Koprna R, Murvanidze N, Werbrouck SPO, Havlíček L, De Diego N, Kopečná M, Wimmer Z, Briozzo P, Moréra S, Zalabák D, Spíchal L, Strnad M. </i> J Exp Bot, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"6YAO"},{"db":"PDB","id":"6YAP"}],"region_id":"DP03466r016","statement":[{"text":"The N-terminal segment, following the signal peptide (1-21), is unmodelled in both structures (see cross references) of this enzyme.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T07:09:16.671Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":532,"end":541,"reference_id":"32945834","reference_source":"pmid","reference_html":"Diphenylurea-derived cytokinin oxidase/dehydrogenase inhibitors for biotechnology and agriculture. <i> Nisler J, Kopečný D, Pěkná Z, Končitíková R, Koprna R, Murvanidze N, Werbrouck SPO, Havlíček L, De Diego N, Kopečná M, Wimmer Z, Briozzo P, Moréra S, Zalabák D, Spíchal L, Strnad M. </i> J Exp Bot, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"6YAO"},{"db":"PDB","id":"6YAP"}],"region_id":"DP03466r017","statement":[{"text":"The C-terminal decapeptide is unmodelled in both structures (see cross references) of this enzyme.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T07:08:58.155Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":17,"released":"2021_12","sequence":"MTRCLMFTLLFLVSSLISTVGLPVEPPAELLQLGGGDVGGGRLSVDASDIAEASRDFGGVARAEPMAVFHPRAAGDVAGLVGAAFRSARGFRVSARGHGHSISGQAQAAGGVVVDMSRGRGPGAAVARALPVHSAALGGHYVDVWGGELWVDVLNWTLSHGGLAPRSWTDYLYLSVGGTLSNAGISGQAFHHGPQISNVYELDVVTGKGEVVTCSETENPDLFFGVLGGLGQFGIITRARIALERAPKRVRWIRALYSNFSEFTADQERLISLGSGGGRRFDYVEGFVVAAEGLINNWRSSFFSPQNPVKLTSLKHHSSVLYCLEVTKNYDDETAGSVDQDVDTLLGELNFLPGTVFTTDLPYVDFLDRVHKAELKLRAKGMWEVPHPWLNLFVPASRIADFDRGVFRGVLGGRTAGAGGPVLIYPMNKHKWDPRSSAVTPDEEVFYLVAFLRSALPGAPESLEALARQNQRILDFCAGTGIGAKQYLPGHKARHEWAEHFGAARWDRFARLKAEFDPRAILAAGQGIFRPPGSPALAADS","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","PACMAD clade","Panicoideae","Andropogonodae","Andropogoneae","Tripsacinae","Zea"],"uniref50":"UniRef50_Q5ZAY9","uniref90":"UniRef90_A0A1D6NA77","uniref100":"UniRef100_E3T1W8","genes":[{"name":{"value":"CKX4","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ADP38079.1","url":"https://www.ebi.ac.uk/ena/browser/view/ADP38079.1"}}]}}],"alphafold_very_low_content":0.10536044362292052,"disorder_content":0.10351201478743069,"disprot_consensus":{"full":[{"start":22,"end":39,"type":"D"},{"start":292,"end":319,"type":"D"},{"start":532,"end":541,"type":"D"}],"Structural state":[{"start":22,"end":39,"type":"D"},{"start":292,"end":319,"type":"D"},{"start":532,"end":541,"type":"D"}],"Molecular function":[{"start":292,"end":319,"type":"F"}]}},{"disprot_id":"DP03467","acc":"Q709Q5","creator":"ppereira","date":"2021-09-08T14:42:10.893Z","features":{"pfam":[{"id":"PF01565","name":"FAD binding domain","start":63,"end":203},{"id":"PF09265","name":"Cytokinin dehydrogenase 1, FAD and cytokinin binding","start":235,"end":510}],"gene3D":[]},"length":519,"name":"Cytokinin dehydrogenase","ncbi_taxon_id":4577,"organism":"Zea mays","regions":[{"start":293,"end":302,"reference_id":"26519657","reference_source":"pmid","reference_html":"Kinetic and structural investigation of the cytokinin oxidase/dehydrogenase active site. <i> Kopečný D, Končitíková R, Popelka H, Briozzo P, Vigouroux A, Kopečná M, Zalabák D, Šebela M, Skopalová J, Frébort I, Moréra S. </i> FEBS J, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"4MLA"}],"region_id":"DP03467r001","statement":[{"text":"The major difference concerns the region of residues 294–325, which is composed of two helices and a loop and which belongs to the substrate binding domain. This region, which is well defined in the ZmCKO1 structure, is disordered in the high resolution structures of ZmCKO4a and ZmCKO2 and adopts a different conformation in the low resolution structure of ZmCKO2 (Fig. 4A). The region delineating the substrate entrance comprises residues surrounding the ribose moiety of cytokinin substrate (N303 and T304 in ZmCKO1) and is most likely\nresponsible for the kinetic differences between the E381 variants and the ZmCKO isoforms.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T09:14:02.981Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":293,"end":302,"reference_id":"26519657","reference_source":"pmid","reference_html":"Kinetic and structural investigation of the cytokinin oxidase/dehydrogenase active site. <i> Kopečný D, Končitíková R, Popelka H, Briozzo P, Vigouroux A, Kopečná M, Zalabák D, Šebela M, Skopalová J, Frébort I, Moréra S. </i> FEBS J, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"GO:0098772","term_name":"molecular function regulator","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"4MLA"}],"region_id":"DP03467r002","statement":[{"text":"The major difference concerns the region of residues 294–325, which is composed of two helices and a loop and which belongs to the substrate binding domain. This region, which is well defined in the ZmCKO1 structure, is disordered in the high resolution structures of ZmCKO4a and ZmCKO2 and adopts a different conformation in the low resolution structure of ZmCKO2 (Fig. 4A). The region delineating the substrate entrance comprises residues surrounding the ribose moiety of cytokinin substrate (N303 and T304 in ZmCKO1) and is most likely\nresponsible for the kinetic differences between the E381 variants and the ZmCKO isoforms.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T09:14:04.133Z"},"ec_go":"EXP","term_not_annotate":true,"term_is_obsolete":false,"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":2,"released":"2021_12","sequence":"MKPPSLVHCFKLLVLLALARLTMHVPDEDMLSPLGALRLDGHFSFHDVSAMARDFGNQCSFLPAAVLHPGSVSDIAATVRHVFSLGEGSPLTVAARGHGHSLMGQSQAAQGIVVRMESLRGARLQVHDGFVDAPGGELWINVLRETLKHGLAPKSWTDYLHLTVGGTLSNAGVSGQAFRHGPQVSNVNQLEIVTGRGDVVTCSPEDNSDLFYAALGGLGQFGIITRARIALEPAPEMVRWIRVLYSDFESFTEDQEMLIMAENSFDYIEGFVIINRTGILNNWRASFKPQDPVQASHFQSDGRVLYCLELTKNFNSGDTDTMEQEVAVLLSRLRFIQSTLFHTDVTYLEFLDRVHTSELKLRAQSLWEVPHPWLNLLIPRSSIRRFATEVFGRILKDSNNGPILLYPVNKSKWDNKTSVVIPDEEIFYLVGFLSSAPSLSGHGSIAHAMSLNSQIVEFCEEADIGMKQYLAHYTTQEQWKTHFGARWETFERRKHRYDPLAILAPGQRIFPKASLPLSL","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","PACMAD clade","Panicoideae","Andropogonodae","Andropogoneae","Tripsacinae","Zea"],"uniref50":"UniRef50_O22213","uniref90":"UniRef90_K3XGJ8","uniref100":"UniRef100_A0A3L6FK25","genes":[{"name":{"value":"542507","evidences":[{"code":"ECO:0000313","source":{"name":"EnsemblPlants","id":"Zm00001eb141570_P001","url":"http://www.ensemblgenomes.org/id/Zm00001eb141570_P001"}}]},"orfNames":[{"value":"ZEAMMB73_Zm00001d042148","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ONM34650.1","url":"https://www.ebi.ac.uk/ena/browser/view/ONM34650.1"}}]}]}],"alphafold_very_low_content":0.04816955684007707,"disorder_content":0.019267822736030827,"disprot_consensus":{"full":[{"start":293,"end":302,"type":"D"}],"Structural state":[{"start":293,"end":302,"type":"D"}],"Molecular function":[{"start":293,"end":302,"type":"F"}]}},{"disprot_id":"DP03469","acc":"Q8VZS8","creator":"ppereira","date":"2021-09-08T17:10:51.826Z","features":{"pfam":[{"id":"PF10604","name":"Polyketide cyclase / dehydrase and lipid transport","start":64,"end":203}],"gene3D":[]},"length":221,"name":"Abscisic acid receptor PYL1","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":8,"end":30,"reference_id":"19855379","reference_source":"pmid","reference_html":"Structural basis of abscisic acid signalling. <i> Miyazono K, Miyakawa T, Sawano Y, Kubota K, Kang HJ, Asano A, Miyauchi Y, Takahashi M, Zhi Y, Fujita Y, Yoshida T, Kodaira KS, Yamaguchi-Shinozaki K, Tanokura M. </i> Nature, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3JRS"}],"region_id":"DP03469r001","statement":[{"text":"The PYL1 construct composed of 8–211 residues (PYL1(8–211)) was used for the crystallization of PYL1–(1)-ABA, and was also applied to all biochemical assays, such as the ITC, SPR, pull-down binding assay and ABI1 inhibitory assay. ","type":"Methods"},{"text":"Due to the poor electron density, we could not build a structural model of the β6-β7 loops of chains A, B, and C, the β5-β6 loop of chain C, the  α1-β1 loop of chain C, or several terminal residues.","type":"Supplementary material"},{"text":"Residues 8-30 are absent from the structural model (see cross reference).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T10:09:02.238Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":19,"end":30,"reference_id":"19893533","reference_source":"pmid","reference_html":"Structural insights into the mechanism of abscisic acid signaling by PYL proteins. <i> Yin P, Fan H, Hao Q, Yuan X, Wu D, Pang Y, Yan C, Li W, Wang J, Yan N. </i> Nat Struct Mol Biol, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3KDJ"}],"region_id":"DP03469r003","statement":[{"text":"To obtain a stable ABI1–PYL1 complex, the His6-tagged core domain (residues 118–425) of ABI1 was coexpressed with PYL1 (residues 19–210) in E. coli BL21(DE3).","type":"Methods"},{"text":"Residues 19-30 are absent from the structural model (see cross reference).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T10:01:48.683Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2021_12","sequence":"MANSESSSSPVNEEENSQRISTLHHQTMPSDLTQDEFTQLSQSIAEFHTYQLGNGRCSSLLAQRIHAPPETVWSVVRRFDRPQIYKHFIKSCNVSEDFEMRVGCTRDVNVISGLPANTSRERLDLLDDDRRVTGFSITGGEHRLRNYKSVTTVHRFEKEEEEERIWTVVLESYVVDVPEGNSEEDTRLFADTVIRLNLQKLASITEAMNRNNNNNNSSQVR","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"uniref50":"UniRef50_O49686","uniref90":"UniRef90_Q8VZS8","uniref100":"UniRef100_Q8VZS8","genes":[{"name":{"value":"PYL1"},"synonyms":[{"value":"RCAR12"}],"orfNames":[{"value":"MZA15.21"}],"olnNames":[{"value":"At5g46790"}]}],"alphafold_very_low_content":0.07692307692307693,"disorder_content":0.10407239819004525,"disprot_consensus":{"full":[{"start":8,"end":30,"type":"D"}],"Structural state":[{"start":8,"end":30,"type":"D"}]}},{"disprot_id":"DP03470","acc":"P47442","creator":"ppereira","date":"2021-09-08T20:25:32.536Z","features":{"pfam":[{"id":"PF00226","name":"DnaJ domain","start":7,"end":68},{"id":"PF01556","name":"DnaJ C terminal domain","start":403,"end":536},{"id":"PF16713","name":"Enriched in aromatic and glycine Residues box","start":168,"end":200}],"gene3D":[]},"length":601,"name":"DnaJ-like protein MG200","ncbi_taxon_id":243273,"organism":"Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195)","regions":[{"start":124,"end":148,"reference_id":"22925012","reference_source":"pmid","reference_html":"The EAGR box structure: a motif involved in mycoplasma motility. <i> Calisto BM, Broto A, Martinelli L, Querol E, Piñol J, Fita I. </i> Mol Microbiol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"4DCZ"}],"region_id":"DP03470r001","statement":[{"text":"A construct spanning MG200 residues 124–207, which includes the complete MG200 EAGR box, yielded highly pure and soluble protein that was crystallized as trigonal crystals.","type":"Results"},{"text":"The structure determined includes the co-ordinates of residues from Gln149 to Glu203 for the two subunits found in the crystal asymmetric unit (Fig. 1).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-09T09:18:27.783Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_12","sequence":"MAEQKRDYYEVLGITPDADQSEIKKAFRKLAKKYHPDRNNAPDAAKIFAEINEANDVLSNPKKRANYDKYGFDGVDGEPAFNFQADVFQSFFEEIAKSGVFNNQTNPEQKEKKKRYHWFSKKPKQEQPEINLDHVVEQTIKKVQQNQNQNKDPDELRSKVPGEVTASDWEALVGDTRYGYFDETGDWSWKGYFDEQGKWVWNEPVDSETSEVSVEPEPTPVAPEASFEEAQPEINAEPEASFESTPTPEPVAPEASFEEAQPEPTPIPEPIPTPVQVQPLLLDLNLFTIPTKATKDDLLFDNINLTTYEQVVDYLNSQATPNLAKTDGELQTIDGTNPLLLEQCKKIKKQAEQLFKKLFLKKQLPFITQPEVVEESKTSFDENNVNLVYFEKVPEILFINQQPKEVKYTRQVFDGLTNKTTSETITLEIQLLQTPKETVSAIFKGFGNDHGKGCGDLKIVFEKIKSPFFQVNEDGLHSACIIDPLVAYNGGIIDVFGPYTNFQVKVDGEIDINAIMKFEKLGIAKTKRKGDLFVHLYYSSVPKKKLTTNPQVQQFLELLQAEYELLQDNIKSLKYFKNNLVIPKKPLDQQSYQYLSQEPIS","taxonomy":["Bacteria","Tenericutes","Mollicutes","Mycoplasmataceae","Mycoplasma"],"uniref50":"UniRef50_P47442","uniref90":"UniRef90_P47442","uniref100":"UniRef100_P47442","genes":[{"olnNames":[{"value":"MG200"}]}],"alphafold_very_low_content":0.47088186356073214,"disorder_content":0.04159733777038269,"disprot_consensus":{"full":[{"start":124,"end":148,"type":"D"}],"Structural state":[{"start":124,"end":148,"type":"D"}]}},{"disprot_id":"DP03471","acc":"Q81GI3","creator":"ppereira","date":"2021-09-08T20:51:22.921Z","features":{"pfam":[{"id":"PF13561","name":"Enoyl-(Acyl carrier protein) reductase","start":13,"end":253}],"gene3D":[]},"length":256,"name":"Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","ncbi_taxon_id":226900,"organism":"Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)","regions":[{"start":102,"end":117,"reference_id":"20800575","reference_source":"pmid","reference_html":"Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus. <i> Kim SJ, Ha BH, Kim KH, Hong SK, Shin KJ, Suh SW, Kim EE. </i> Biochem Biophys Res Commun, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3OJE"}],"region_id":"DP03471r001","statement":[{"text":"In addition, the residues between 102–117, 149–160, and 197–202 were disordered.","type":"Results"},{"text":"The residues between 102–117, 149–160, and 197–202 are not visible in the electron density maps.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-10T07:17:53.237Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":149,"end":160,"reference_id":"20800575","reference_source":"pmid","reference_html":"Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus. <i> Kim SJ, Ha BH, Kim KH, Hong SK, Shin KJ, Suh SW, Kim EE. </i> Biochem Biophys Res Commun, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3OJE"}],"region_id":"DP03471r002","statement":[{"text":"In addition, the residues between 102–117, 149–160, and 197–202 were disordered.","type":"Results"},{"text":"The residues between 102–117, 149–160, and 197–202 are not visible in the electron density maps.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-10T07:17:51.454Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":149,"end":160,"reference_id":"20800575","reference_source":"pmid","reference_html":"Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus. <i> Kim SJ, Ha BH, Kim KH, Hong SK, Shin KJ, Suh SW, Kim EE. </i> Biochem Biophys Res Commun, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3OJF"}],"region_id":"DP03471r003","statement":[{"text":"The disordered regions in the apo structure become mostly α-helices and loops upon binding of NADP+ and INH (or presumably the substrate).","type":"Results"},{"text":"The three disordered stretches in the apo structure became ordered in the ternary complex, and the residues 149–160 and 197–202 were involved in the interaction with NADP+ as shown in the figure.","type":"Results"},{"text":"The three stretches of residues (residues 102–117, 149–160 and 197–202) that are disordered in the apo structure become well organized in the ternary complex, and the overall structure of the ternary complex is almost identical to other FabIs reported previously.","type":"Conclusion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-10T07:18:11.521Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":102,"end":117,"reference_id":"20800575","reference_source":"pmid","reference_html":"Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus. <i> Kim SJ, Ha BH, Kim KH, Hong SK, Shin KJ, Suh SW, Kim EE. </i> Biochem Biophys Res Commun, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3OJF"}],"region_id":"DP03471r004","statement":[{"text":"The disordered regions in the apo structure become mostly α-helices and loops upon binding of NADP+ and INH (or presumably the substrate).","type":"Results"},{"text":"The three disordered stretches in the apo structure became ordered in the ternary complex, and the residues 149–160 and 197–202 were involved in the interaction with NADP+ as shown in the figure.","type":"Results"},{"text":"The three stretches of residues (residues 102–117, 149–160 and 197–202) that are disordered in the apo structure become well organized in the ternary complex, and the overall structure of the ternary complex is almost identical to other FabIs reported previously.","type":"Conclusion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-10T07:18:07.123Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":102,"end":117,"reference_id":"20800575","reference_source":"pmid","reference_html":"Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus. <i> Kim SJ, Ha BH, Kim KH, Hong SK, Shin KJ, Suh SW, Kim EE. </i> Biochem Biophys Res Commun, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"GO:0036094","term_name":"small molecule binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3OJF"}],"region_id":"DP03471r005","statement":[{"text":"The three stretches disordered in the apo structure are important in the cofactor and the inhibitor binding as well as in tetramer formation.","type":"Abstract"},{"text":"The disordered regions in the apo structure become mostly α-helices and loops upon binding of NADP+ and INH (or presumably the substrate).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-10T07:20:18.289Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":149,"end":160,"reference_id":"20800575","reference_source":"pmid","reference_html":"Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus. <i> Kim SJ, Ha BH, Kim KH, Hong SK, Shin KJ, Suh SW, Kim EE. </i> Biochem Biophys Res Commun, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"GO:0036094","term_name":"small molecule binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3OJF"}],"region_id":"DP03471r006","statement":[{"text":"The three stretches disordered in the apo structure are important in the cofactor and the inhibitor binding as well as in tetramer formation.","type":"Abstract"},{"text":"The disordered regions in the apo structure become mostly α-helices and loops upon binding of NADP+ and INH (or presumably the substrate).","type":"Results"},{"text":"The three disordered stretches in the apo structure became ordered in the ternary complex, and the residues 149–160 and 197–202 were involved in the interaction with NADP+ as shown in the figure.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-10T07:20:23.121Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":149,"end":160,"reference_id":"20800575","reference_source":"pmid","reference_html":"Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus. <i> Kim SJ, Ha BH, Kim KH, Hong SK, Shin KJ, Suh SW, Kim EE. </i> Biochem Biophys Res Commun, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3OJF"}],"region_id":"DP03471r007","statement":[{"text":"The three stretches disordered in the apo structure are important in the cofactor and the inhibitor binding as well as in tetramer formation.","type":"Abstract"},{"text":"The molecules A and D (B and C) form another extensive interface in the ternary complex, and they involve the residues that are disordered in the apo structure and highlighted in cyan.","type":"Figure"},{"text":"The second interface involves interactions between molecules A and D (A:D), and molecules B and C (B:C). These interactions were contributed by the residues from α3 to α7, and the loop β6 which composed of two in the three stretches, namely residues 102–117 and 149–160, disordered in the apo structure (see Fig. 2D and E), i.e., these disordered regions were crucial for tetramer formation.","type":"Results"},{"text":"The apo BcFabL exists as a homo-dimer both in crystal and solution, and the three disordered stretches affect both in the cofactor and the inhibitor binding and in tetramer formation.","type":"Results"},{"text":"Together these suggest that there is a transition from the dimer to tetramer and the three disordered stretches in the apo structure are important not only in binding of the cofactor and the inhibitor but also in the tetramer formation.","type":"Conclusion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-10T07:18:54.159Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":102,"end":117,"reference_id":"20800575","reference_source":"pmid","reference_html":"Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus. <i> Kim SJ, Ha BH, Kim KH, Hong SK, Shin KJ, Suh SW, Kim EE. </i> Biochem Biophys Res Commun, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3OJF"}],"region_id":"DP03471r008","statement":[{"text":"The three stretches disordered in the apo structure are important in the cofactor and the inhibitor binding as well as in tetramer formation.","type":"Abstract"},{"text":"The molecules A and D (B and C) form another extensive interface in the ternary complex, and they involve the residues that are disordered in the apo structure and highlighted in cyan.","type":"Figure"},{"text":"The second interface involves interactions between molecules A and D (A:D), and molecules B and C (B:C). These interactions were contributed by the residues from α3 to α7, and the loop β6 which composed of two in the three stretches, namely residues 102–117 and 149–160, disordered in the apo structure (see Fig. 2D and E), i.e., these disordered regions were crucial for tetramer formation.","type":"Results"},{"text":"The apo BcFabL exists as a homo-dimer both in crystal and solution, and the three disordered stretches affect both in the cofactor and the inhibitor binding and in tetramer formation.","type":"Results"},{"text":"Together these suggest that there is a transition from the dimer to tetramer and the three disordered stretches in the apo structure are important not only in binding of the cofactor and the inhibitor but also in the tetramer formation.","type":"Conclusion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-10T07:19:44.028Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":99,"end":111,"reference_id":"28935372","reference_source":"pmid","reference_html":"Structural insights into the dimer-tetramer transition of FabI from Bacillus anthracis. <i> Kim HT, Kim S, Na BK, Chung J, Hwang E, Hwang KY. </i> Biochem Biophys Res Commun, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"5YCS"},{"db":"PDB","id":"5YCX"}],"region_id":"DP03471r009","statement":[{"text":"In the dimeric form, the substrate-binding loop (SBL, 197–203), the second substrate-binding loop (SBL-2, 99–111), and the active site loop (ASL, 150–160), which play a key role in catalytic activity, were disordered (Fig. 2E).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-10T07:17:37.822Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":150,"end":160,"reference_id":"28935372","reference_source":"pmid","reference_html":"Structural insights into the dimer-tetramer transition of FabI from Bacillus anthracis. <i> Kim HT, Kim S, Na BK, Chung J, Hwang E, Hwang KY. </i> Biochem Biophys Res Commun, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"5YCS"},{"db":"PDB","id":"5YCX"}],"region_id":"DP03471r010","statement":[{"text":"In the dimeric form, the substrate-binding loop (SBL, 197–203), the second substrate-binding loop (SBL-2, 99–111), and the active site loop (ASL, 150–160), which play a key role in catalytic activity, were disordered (Fig. 2E).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-10T07:17:33.802Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":150,"end":160,"reference_id":"28935372","reference_source":"pmid","reference_html":"Structural insights into the dimer-tetramer transition of FabI from Bacillus anthracis. <i> Kim HT, Kim S, Na BK, Chung J, Hwang E, Hwang KY. </i> Biochem Biophys Res Commun, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"5YCR"},{"db":"PDB","id":"5YCV"}],"region_id":"DP03471r011","statement":[{"text":"ASL, which is disordered in the dimer, is rearranged by the helix-helix α7-α7′ interaction (Fig. 4B and C).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-10T07:18:05.755Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":99,"end":111,"reference_id":"28935372","reference_source":"pmid","reference_html":"Structural insights into the dimer-tetramer transition of FabI from Bacillus anthracis. <i> Kim HT, Kim S, Na BK, Chung J, Hwang E, Hwang KY. </i> Biochem Biophys Res Commun, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"5YCR"},{"db":"PDB","id":"5YCV"}],"region_id":"DP03471r012","statement":[{"text":"During the process, SBL-2, which is disordered in the dimeric form, is becomes ordered.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-10T07:18:04.457Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":150,"end":160,"reference_id":"28935372","reference_source":"pmid","reference_html":"Structural insights into the dimer-tetramer transition of FabI from Bacillus anthracis. <i> Kim HT, Kim S, Na BK, Chung J, Hwang E, Hwang KY. </i> Biochem Biophys Res Commun, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"5YCR"},{"db":"PDB","id":"5YCV"}],"region_id":"DP03471r013","statement":[{"text":"In the dimeric form, the substrate-binding loop (SBL, 197–203), the second substrate-binding loop (SBL-2, 99–111), and the active site loop (ASL, 150–160), which play a key role in catalytic activity, were disordered (Fig. 2E).","type":"Results"},{"text":"ASL, which is disordered in the dimer, is rearranged by the helix-helix α7-α7′ interaction (Fig. 4B and C). ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-10T07:20:12.365Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":13,"released":"2021_12","sequence":"MELLQGKTFVVMGVANQRSIAWGIARSLHNAGAKLIFTYAGERLERNVRELADTLEGQESLVLPCDVTNDEELTACFETIKQEVGTIHGVAHCIAFANRDDLKGEFVDTSRDGFLLAQNISAFSLTAVAREAKKVMTEGGNILTLTYLGGERVVKNYNVMGVAKASLEASVKYLANDLGQHGIRVNAISAGPIRTLSAKGVGDFNSILREIEERAPLRRTTTQEEVGDTAVFLFSDLARGVTGENIHVDSGYHILG","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Bacillus","Bacillus cereus group"],"uniref50":"UniRef50_P54616","uniref90":"UniRef90_Q81GI3","uniref100":"UniRef100_Q81GI3","genes":[{"name":{"value":"fabI"},"olnNames":[{"value":"BC_1216"}]}],"alphafold_very_low_content":0,"disorder_content":0.12109375,"disprot_consensus":{"full":[{"start":99,"end":117,"type":"T"},{"start":149,"end":160,"type":"T"}],"Structural state":[{"start":99,"end":117,"type":"D"},{"start":149,"end":160,"type":"D"}],"Structural transition":[{"start":99,"end":117,"type":"T"},{"start":149,"end":160,"type":"T"}],"Molecular function":[{"start":102,"end":117,"type":"F"},{"start":149,"end":160,"type":"F"}],"Disorder function":[{"start":102,"end":117,"type":"F"},{"start":149,"end":160,"type":"F"}]}},{"disprot_id":"DP03472","acc":"Q09535","creator":"ppereira","date":"2021-09-09T10:55:24.712Z","features":{"pfam":[{"id":"PF00004","name":"ATPase family associated with various cellular activities (AAA)","start":175,"end":319},{"id":"PF22107","name":"Pch2 N-terminal domain","start":8,"end":100},{"id":"PF23242","name":"TRIP13-like, AAA+ ATPase lid C-terminal domain","start":326,"end":416}],"gene3D":[]},"length":424,"name":"Putative pachytene checkpoint protein 2","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":108,"end":121,"reference_id":"25918846","reference_source":"pmid","reference_html":"TRIP13 is a protein-remodeling AAA+ ATPase that catalyzes MAD2 conformation switching. <i> Ye Q, Rosenberg SC, Moeller A, Speir JA, Su TY, Corbett KD. </i> Elife, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"4XGU"}],"region_id":"DP03472r002","statement":[{"text":"The final model consists of six PCH-2 monomers, with a total of 2214 residues modeled out of 2544 (6 × 424 residues);","type":"Methods"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-24T14:53:09.473Z"}},{"start":255,"end":273,"reference_id":"25918846","reference_source":"pmid","reference_html":"TRIP13 is a protein-remodeling AAA+ ATPase that catalyzes MAD2 conformation switching. <i> Ye Q, Rosenberg SC, Moeller A, Speir JA, Su TY, Corbett KD. </i> Elife, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"ppereira","curator_name":"Pedro Pereira","curator_orcid":"0000-0003-0969-5438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"4XGU"}],"region_id":"DP03472r003","statement":[{"text":"The final model consists of six PCH-2 monomers, with a total of 2214 residues modeled out of 2544 (6 × 424 residues);","type":"Methods"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-24T14:53:09.177Z"}}],"regions_counter":3,"released":"2021_12","sequence":"MHEPMKTLKNIHAEIRICQKFPKSTVQKRFSEFEELIKAASKNARNWKPISSVELFQGDSSLNELFEKLVIGTCELRDGELFENVNDLTINPSNIHVYKLHKDGPLSQNIGDDDGDESIIGSQLWQLPCVEFDSIWENLIYDSNLKNEVMSYVAALARLSEKHVNTKIINVNRLILLTGPPGTGKTSLCKGLAQHLSIRMNDKYSKSVMLEINSHSLFSKWFSESGKLVQKMFDQIDELAEDEKCMVFVLIDEVESLGMCRESSSSRSEPSDAIRAVNALLTQIDRIRRRDNVLILCTSNLESTLDKALVDRADIVKNVGQPSDFARYSMLKSSIMELARIGVVIDNEVHTDYWPQDICDTKAPRNEFTEILFKIAQEARGLSGRAISMLPTLVYSKSPEETITLPNCMNLFLEAVKERLSRNN","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"uniref50":"UniRef50_Q09535","uniref90":"UniRef90_Q09535","uniref100":"UniRef100_Q09535","genes":[{"name":{"value":"pch-2"},"orfNames":[{"value":"F10B5.5"}]}],"alphafold_very_low_content":0.007075471698113208,"disorder_content":0.07783018867924528,"disprot_consensus":{"full":[{"start":108,"end":121,"type":"D"},{"start":255,"end":273,"type":"D"}],"Structural state":[{"start":108,"end":121,"type":"D"},{"start":255,"end":273,"type":"D"}]}},{"disprot_id":"DP03473","acc":"O94258","creator":"ktsirigos","date":"2021-09-09T11:38:44.323Z","features":{"pfam":[{"id":"PF08389","name":"Exportin 1-like protein","start":101,"end":252},{"id":"PF19282","name":"Exportin-T","start":321,"end":972}],"gene3D":[]},"length":978,"name":"Exportin-T","ncbi_taxon_id":284812,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","regions":[{"start":954,"end":969,"reference_id":"19680239","reference_source":"pmid","reference_html":"Structures of the tRNA export factor in the nuclear and cytosolic states. <i> Cook AG, Fukuhara N, Jinek M, Conti E. </i> Nature, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"ktsirigos","curator_name":"Konstantinos D. Tsirigos","curator_orcid":"0000-0001-5280-1107","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3IBV"}],"region_id":"DP03473r001","statement":[{"text":"The final model contains 941 residues of Xpot and is missing a few disordered loops.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-09-15T07:57:44.058Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":954,"end":969,"reference_id":"19680239","reference_source":"pmid","reference_html":"Structures of the tRNA export factor in the nuclear and cytosolic states. <i> Cook AG, Fukuhara N, Jinek M, Conti E. </i> Nature, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"ktsirigos","curator_name":"Konstantinos D. Tsirigos","curator_orcid":"0000-0001-5280-1107","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3IBV"}],"region_id":"DP03473r002","statement":[{"text":"The final model contains 941 residues of Xpot and is missing a few disordered loops","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-09-15T07:22:19.668Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MSAQDVENAVEAALDPSVGPIIKQQATDFIGSLRSSSTGWKICHEIFSEKTKYKPSTRLICLQTLSEKVREWNNESNLLELQMIRDSVWSYIKELSFLDEPAYISNAVQHLLTLLFLQLYPSNWNDFFASLQGVIAASSQSEFSNFYLKVLLSIGDEIADSLVLKTDVQIQKDNLVKDAIRANDMSDIVSFVYEMMLAYSNAKNYGTVGLCLQVYAQWVSWININLIVNEPCMNLLYSFLQIEELRCAACETMTEIVNKKMKPLEKLNLLNILNLNLFFSKSQEQSTDPNFDEHVAKLINAQGVELVAIKSDPSELSPELKENCSFQLYNLFPYLIRYLSDDYDETSTAVFPFLSDLLVSLRKESSSKELSASLKEFLKSLLEAIIKKMKYDESQEWDDDPDSEEEAEFQEMRKKLKIFQDTINSIDSSLFSSYMYSAITSSLSTAATLSPENSWQLIEFALYETYIFGEGLRGPDAFFNEVDKSPTVLSQILALVTTSQVCRHPHPLVQLLYMEILVRYASFFDYESAAIPALIEYFVGPRGIHNTNERVRPRAWYLFYRFVKSIKKQVVNYTESSLAMLGDLLNISVSPVTDMDAPVPTLNSSIRNSDFNSQLYLFETVGVLISSGNLTPEEQALYCDSLINALIGKANAALSSDLSALENIISVYCSLMAIGNFAKGFPARGSEEVAWLASFNKASDEIFLILDRMGFNEDIRGAVRFTSGRIINVVGPDMLPKVPQLISILLNSIDMNELVDVLSFISQLIHIYKDNMMEITNRMLPTLLMRIFSSLSAAPQGTDDAVKQNDLRKSYISFILQLLNKGFGSILFTEENQVYFDPLINSILHFANLVGEPATQKSSIALVSKMVSLWGGKDGIAGFENFTLSLTPLCFEMPVNPNFNTRDGQSLVVLGELAGLQKIILEKLGDIYKSYLVTVYFPTVNFPDVMASEYLQALSNLDSRSFKQFFQKFIQALKSGNV","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"uniref50":"UniRef50_O94258","uniref90":"UniRef90_O94258","uniref100":"UniRef100_O94258","genes":[{"name":{"value":"los1"},"orfNames":[{"value":"SPBP8B7.09c"}]}],"alphafold_very_low_content":0.0010224948875255625,"dataset":["RNA-binding proteins"],"disorder_content":0.016359918200409,"disprot_consensus":{"full":[{"start":954,"end":969,"type":"T"}],"Structural state":[{"start":954,"end":969,"type":"D"}],"Structural transition":[{"start":954,"end":969,"type":"T"}]}},{"disprot_id":"DP03475","acc":"Q81EJ6","creator":"ktsirigos","date":"2021-09-10T09:37:03.847Z","features":{"pfam":[{"id":"PF01522","name":"Polysaccharide deacetylase","start":66,"end":180}],"gene3D":[]},"length":273,"name":"Peptidoglycan-N-acetylglucosamine deacetylase BC_1974","ncbi_taxon_id":226900,"organism":"Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)","regions":[{"start":1,"end":67,"reference_id":"29257674","reference_source":"pmid","reference_html":"Structures of the Peptidoglycan N-Acetylglucosamine Deacetylase Bc1974 and Its Complexes with Zinc Metalloenzyme Inhibitors. <i> Giastas P, Andreou A, Papakyriakou A, Koutsioulis D, Balomenou S, Tzartos SJ, Bouriotis V, Eliopoulos EE. </i> Biochemistry, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"ktsirigos","curator_name":"Konstantinos D. Tsirigos","curator_orcid":"0000-0001-5280-1107","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"5N1P"},{"db":"PDB","id":"5NEK"},{"db":"PDB","id":"5NCD"},{"db":"PDB","id":"5NC9"},{"db":"PDB","id":"5N1J"},{"db":"PDB","id":"5NC6"},{"db":"PDB","id":"5NEL"}],"region_id":"DP03475r001","statement":[{"text":" Moreover, the crystal structures revealed the structure of the region 68−273, meaning that we could not identify the electron density for the 42 N-terminus residues of the expressed construct.","type":"Methods"},{"text":"Although the expressed construct contained 42 additional residues at the N-terminus, no electron density was observed for those residues, denoting the unstructured nature of the specific region ","type":"Results"},{"text":"The N-terminal region 1-67 of the full length BC_1974 (PDB:5nc6) is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-09-14T22:38:33.445Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MEKALKIKQIVVVLIAIAAVAIGYYMFQSITSPAKAVAKQENVVQLASEQPKVEMNKTAPSRFNGKERKVAYLTFDDGPGKYTAELLNTLKQHDAKATFFLIGANVKEFPDLVKRENAEGHYVGMHSMTHNFAKLYKNGEYVNEMKEDQGLIANIIGKSPKLTRPPYGSMPGLNEGLRNKVVEGGFKVWDWTIDSLDWRYNKMPVDAAAAQIAQNVLTNATKPQEVILMHDIHPQSVAAVPAILKGLKEKGYEFEAYHEESHFPVNFWHDNRM","taxonomy":["Bacteria","Firmicutes","Bacilli","Bacillales","Bacillaceae","Bacillus","Bacillus cereus group"],"uniref50":"UniRef50_Q81EJ6","uniref90":"UniRef90_Q81EJ6","uniref100":"UniRef100_Q81EJ6","genes":[{"olnNames":[{"value":"BC_1974","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAP08945.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAP08945.1"}}]}]}],"alphafold_very_low_content":0.018315018315018316,"disorder_content":0.2454212454212454,"disprot_consensus":{"full":[{"start":1,"end":67,"type":"D"}],"Structural state":[{"start":1,"end":67,"type":"D"}]}},{"disprot_id":"DP03476","acc":"F1QCV2","creator":"ktsirigos","date":"2021-09-10T12:24:17.685Z","features":{"pfam":[{"id":"PF00850","name":"Histone deacetylase domain","start":28,"end":322}],"gene3D":[]},"length":675,"name":"Polyamine deacetylase HDAC10","ncbi_taxon_id":7955,"organism":"Danio rerio","regions":[{"start":365,"end":411,"reference_id":"28516954","reference_source":"pmid","reference_html":"Histone deacetylase 10 structure and molecular function as a polyamine deacetylase. <i> Hai Y, Shinsky SA, Porter NJ, Christianson DW. </i> Nat Commun, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"ktsirigos","curator_name":"Konstantinos D. Tsirigos","curator_orcid":"0000-0001-5280-1107","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"5TD7"}],"region_id":"DP03476r001","statement":[{"text":"Residues omitted from the final model due to disorder included S365-A411 (the nicked interdomain loop) and G435, D436 and H454 in the CDAC domain. ","type":"Methods"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-09-14T15:57:11.433Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MASGSALIFDEEMSRYKLLWTDPACEIEVPERLTVSYEALRTHGLAQRCKAVPVRQATEQEILLAHSEEYLEAVKQTPGMNVEELMAFSKKYNDVYFHQNIYHCAKLAAGATLQLVDSVMKREVRNGMALVRPPGHHSQRSAANGFCVFNNVAIAALYAKKNYNLNRILIVDWDVHHGQGIQYCFEEDPSVLYFSWHRYEHQSFWPNLPESDYSSVGKGKGSGFNINLPWNKVGMTNSDYLAAFFHVLLPVAYEFDPELVIVSAGFDSAIGDPEGEMCALPEIFAHLTHLLMPLAAGKMCVVLEGGYNLTSLGQSVCQTVHSLLGDPTPRISGLGTACDSALESIQNVRNVQSSYWSSFKHLAQSETNPKRPRLDATNGGPKESSEPASESNPKKTAQDIVWPEPLKRMPASVRTVVVPPPGVELTLPKNCQHSGDISESTAKEVQRIRDKHFHDLTDQNILRSLGNIISVLDRMMRSDEVCNGCVVVSDLSVSVQCALQHALTEPAERVLVVYVGDGELPVKTNDGKVFLVQICTKETEDKCVNRLSLCLREGESLTAGFMQALLGLILPVAYEFNPALVLGIVGETAAKTGLMTVWGHMTCLIQGLARGRTLTLLQGYDKDLLELTVSALSGASISPLGPLRALKPEDVEMMEKQRQRLQERWGLLRCTVSES","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Actinopterygii","Neopterygii","Teleostei","Ostariophysi","Cypriniformes","Danionidae","Danioninae","Danio"],"uniref50":"UniRef50_F1QCV2","uniref90":"UniRef90_F1QCV2","uniref100":"UniRef100_F1QCV2","genes":[{"name":{"value":"hdac10"}}],"alphafold_very_low_content":0.045925925925925926,"disorder_content":0.06962962962962962,"disprot_consensus":{"full":[{"start":365,"end":411,"type":"D"}],"Structural state":[{"start":365,"end":411,"type":"D"}]}},{"disprot_id":"DP03477","acc":"Q5GH54","creator":"jglavina","date":"2021-09-10T13:53:00.943Z","features":{"pfam":[{"id":"PF09815","name":"XK-related protein","start":10,"end":345}],"gene3D":[]},"length":373,"name":"XK-related protein","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions":[{"start":68,"end":80,"reference_id":"34263724","reference_source":"pmid","reference_html":"Cryo-EM structures of the caspase-activated protein XKR9 involved in apoptotic lipid scrambling. <i> Straub MS, Alvadia C, Sawicka M, Dutzler R. </i> Elife, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jglavina","curator_name":"Juliana Glavina","curator_orcid":"0000-0001-6336-1290","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"EMDB","id":"EMD-13155"},{"db":"EMDB","id":"EMD-13157"},{"db":"PDB","id":"7P14"},{"db":"PDB","id":"7P16"}],"region_id":"DP03477r001","statement":[{"text":"Although, due to the novelty of the protein fold, model building was challenging, the high quality of the map and the distribution of sidechain density of different volume have ultimately allowed the unambiguous interpretation of residues 1–66, 81–105, 119–344, and 365–373 of rXKR9 encompassing all structured parts of the protein.","type":"Results"},{"text":"rXKR9 comprises eight membrane-spanning helices (TM1–8), which are connected by short loops on the extracellular and longer loops on the intracellular side (Figure 4A–C).","type":"Results"},{"text":"Full-length rXKR9 was built de novo into the cryo-EM density, and cleaved rXKR9 was built using the full-length structure as reference. The cryo-EM density of full-length rXKR9 was of sufficiently high resolution to unambiguously assign residues 1–66, 81–105, 119–344, and 365–373.","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-14T14:00:57.261Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":106,"end":118,"reference_id":"34263724","reference_source":"pmid","reference_html":"Cryo-EM structures of the caspase-activated protein XKR9 involved in apoptotic lipid scrambling. <i> Straub MS, Alvadia C, Sawicka M, Dutzler R. </i> Elife, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jglavina","curator_name":"Juliana Glavina","curator_orcid":"0000-0001-6336-1290","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"EMDB","id":"EMD-13155"},{"db":"EMDB","id":"EMD-13157"},{"db":"PDB","id":"7P14"},{"db":"PDB","id":"7P16"}],"region_id":"DP03477r002","statement":[{"text":"Although, due to the novelty of the protein fold, model building was challenging, the high quality of the map and the distribution of sidechain density of different volume have ultimately allowed the unambiguous interpretation of residues 1–66, 81–105, 119–344, and 365–373 of rXKR9 encompassing all structured parts of the protein.","type":"Results"},{"text":"rXKR9 comprises eight membrane-spanning helices (TM1–8), which are connected by short loops on the extracellular and longer loops on the intracellular side (Figure 4A–C).","type":"Results"},{"text":"Full-length rXKR9 was built de novo into the cryo-EM density, and cleaved rXKR9 was built using the full-length structure as reference. The cryo-EM density of full-length rXKR9 was of sufficiently high resolution to unambiguously assign residues 1–66, 81–105, 119–344, and 365–373.","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-14T14:01:24.884Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":345,"end":364,"reference_id":"34263724","reference_source":"pmid","reference_html":"Cryo-EM structures of the caspase-activated protein XKR9 involved in apoptotic lipid scrambling. <i> Straub MS, Alvadia C, Sawicka M, Dutzler R. </i> Elife, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jglavina","curator_name":"Juliana Glavina","curator_orcid":"0000-0001-6336-1290","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"EMDB","id":"EMD-13155"},{"db":"PDB","id":"7P14"}],"region_id":"DP03477r003","statement":[{"text":"Although, due to the novelty of the protein fold, model building was challenging, the high quality of the map and the distribution of sidechain density of different volume have ultimately allowed the unambiguous interpretation of residues 1–66, 81–105, 119–344, and 365–373 of rXKR9 encompassing all structured parts of the protein.","type":"Results"},{"text":"rXKR9 comprises eight membrane-spanning helices (TM1–8), which are connected by short loops on the extracellular and longer loops on the intracellular side (Figure 4A–C).","type":"Results"},{"text":"In the structure of full-length rXKR9, part of the inhibitory peptide is well-defined, whereas the connecting loop harboring the cleavage site appears unstructured (Figure 2A, Figure 2—figure supplement 4).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-14T14:03:09.070Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":345,"end":373,"reference_id":"34263724","reference_source":"pmid","reference_html":"Cryo-EM structures of the caspase-activated protein XKR9 involved in apoptotic lipid scrambling. <i> Straub MS, Alvadia C, Sawicka M, Dutzler R. </i> Elife, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jglavina","curator_name":"Juliana Glavina","curator_orcid":"0000-0001-6336-1290","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"7P16"},{"db":"EMDB","id":"EMD-13157"}],"region_id":"DP03477r004","statement":[{"text":"In the data of the cleaved rXKR9, the density of the C-terminus is absent, exposing the hydrophobic cleft to the cytoplasm (Figure 2). Apart from smaller changes in the intracellular loop regions, the truncated protein has not changed its conformation, which is illustrated in the low RMSD of 0.72 Å between the two structures (Figure 6B).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-21T07:20:13.357Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":4,"released":"2023_12","sequence":"MKYTICNFMMSVLGIIIYVTDLVADIVLTVRYFYDGQYVFGVLTLSFVLCGTLIVHCFSYSWLKDDLKKAGGENEHYFLLLHCLQGGVFTRYWFVLRTGYHVVFKHSHRTSNFMEEQTDPHKEAIDMATDLSMLRLFETYLEGCPQLILQLYAFLERGQANFSQYMVIMVSCCAISWSTVDYQIALRKSLPDKNLLRGFWPKLTYLFYKLFTLLSWMLSVVLLLFVDVRTVLLLLLFLWTVGFIWAFINHTQFCNSLSMEFLYRLVVGFILVFTFFNIKGQNTKCPMSCYYTVRVLGTLGILTVFWIYPLSIFNSDYFIPISATIVLSLLFGIIFLGVYYGTYHPNINAGTQHDEPDGKAPQRDCRIRYFLMD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref50":"UniRef50_Q5GH62","uniref90":"UniRef90_Q5GH62","uniref100":"UniRef100_Q5GH54","genes":[{"name":{"value":"Xkr9","evidences":[{"code":"ECO:0000313","source":{"name":"Ensembl","id":"ENSRNOP00000058714","url":"https://www.ensembl.org/id/ENSRNOP00000058714"}},{"code":"ECO:0000313","source":{"name":"RGD","id":"1359260","url":"https://rgd.mcw.edu/tools/genes/genes_view.cgi?id=1359260"}}]},"synonyms":[{"value":"XRG9","evidences":[{"code":"ECO:0000313","source":{"name":"RGD","id":"1359260","url":"https://rgd.mcw.edu/tools/genes/genes_view.cgi?id=1359260"}}]}]}],"alphafold_very_low_content":0.08579088471849866,"disorder_content":0.14745308310991956,"disprot_consensus":{"full":[{"start":68,"end":80,"type":"D"},{"start":106,"end":118,"type":"D"},{"start":345,"end":373,"type":"D"}],"Structural state":[{"start":68,"end":80,"type":"D"},{"start":106,"end":118,"type":"D"},{"start":345,"end":373,"type":"D"}]}},{"acc":"P20351","sequence":"MSCPYAGNGNDHDDSAVPLTTEVGKIYGEYLMLDKLLDAQCMLSEEDKRPVHDEHLFIITHQAYELWFKQIIFEFDSIRDMLDAEVIDETKTLEIVKRLNRVVLILKLLVDQVPILETMTPLDFMDFRKYLAPASGFQSLQFRLIENKLGVLTEQRVRYNQKYSDVFSDEEARNSIRNSEKDPSLLELVQRWLERTPGLEESGFNFWAKFQESVDRFLEAQVQSAMEEPVEKAKNYRLMDIEKRREVYRSIFDPAVHDALVRRGDRRFSHRALQGAIMITFYRDEPRFSQPHQLLTLLMDIDSLITKWRYNHVIMVQRMIGSQQLGTGGSSGYQYLRSTLSDRYKVFLDLFNLSTFLIPREAIPPLDETIRKKLINKSV","alphafold_very_low_content":"0.044854881266490766","creator":"ktsirigos","dataset":[],"date":"2021-09-10T16:49:24.270Z","disprot_id":"DP03479","features":{"pfam":[{"id":"PF03301","name":"Tryptophan 2,3-dioxygenase","start":16,"end":357}],"gene3D":[]},"genes":[{"name":{"value":"v","evidences":[{"source":{"id":"MF_03020","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_03020","_id":"685af523b4ac24d5329d9745"},"code":"ECO:0000255","_id":"685af523b4ac24d5329d9744"}],"_id":"685af523b4ac24d5329d9746"},"synonyms":[],"olnNames":[],"orfNames":[{"value":"CG5163","evidences":[],"_id":"685af523b4ac24d5329d9747"}],"_id":"685af523b4ac24d5329d9743"}],"length":379,"name":"Tryptophan 2,3-dioxygenase","ncbi_taxon_id":7227,"organism":"Drosophila melanogaster","regions_counter":2,"released":"2021_12","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref100":"UniRef100_P20351","uniref50":"UniRef50_P48775","uniref90":"UniRef90_P20351","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"4HKA","_id":"685af523b4ac24d5329d973b"}],"curator_id":"ktsirigos","curator_name":"Konstantinos D. Tsirigos","curator_orcid":"0000-0001-5280-1107","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":369,"end":379,"interaction_partner":[],"reference_html":"Crystal structure of Drosophila melanogaster tryptophan 2,3-dioxygenase reveals insights into substrate recognition and catalytic mechanism. <i> Huang W, Gong Z, Li J, Ding J. </i> J Struct Biol, 2013","reference_id":"23333332","region_id":"DP03479r001","released":"2022_03","sample":[],"statement":[],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2021-09-14T22:39:13.826Z","_id":"685af523b4ac24d5329d973c"},"version":1,"_id":"685af523b4ac24d5329d973a","reference_source":"pmid"}],"__v":0,"disorder_content":0.029023746701846966,"disprot_consensus":{"full":[{"start":369,"end":379,"type":"D"}],"Structural state":[{"start":369,"end":379,"type":"D"}]}},{"disprot_id":"DP03480","acc":"P00392","creator":"ktsirigos","date":"2021-09-10T17:03:37.954Z","features":{"pfam":[{"id":"PF00403","name":"Heavy-metal-associated domain","start":4,"end":63},{"id":"PF02852","name":"Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain","start":437,"end":545},{"id":"PF07992","name":"Pyridine nucleotide-disulphide oxidoreductase","start":100,"end":418}],"gene3D":[]},"length":561,"name":"Mercuric reductase","ncbi_taxon_id":287,"organism":"Pseudomonas aeruginosa","regions":[{"start":550,"end":561,"reference_id":"16114877","reference_source":"pmid","reference_html":"NmerA, the metal binding domain of mercuric ion reductase, removes Hg2+ from proteins, delivers it to the catalytic core, and protects cells under glutathione-depleted conditions. <i> Ledwidge R, Patel B, Dong A, Fiedler D, Falkowski M, Zelikova J, Summers AO, Pai EF, Miller SM. </i> Biochemistry, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"ktsirigos","curator_name":"Konstantinos D. Tsirigos","curator_orcid":"0000-0001-5280-1107","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007735","ec_ontology":"ECO","ec_name":"structure determination evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"1ZK7"},{"db":"PDB","id":"1ZX9"}],"region_id":"DP03480r001","statement":[{"text":"In the PEG crystals of the Tn501 protein, the last 11 amino acids were not well ordered and only visible as disconnected patches in the electron density map. ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-09-14T14:45:13.483Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MTHLKITGMTCDSCAAHVKEALEKVPGVQSALVSYPKGTAQLAIVPGTSPDALTAAVAGLGYKATLADAPLADNRVGLLDKVRGWMAAAEKHSGNEPPVQVAVIGSGGAAMAAALKAVEQGAQVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGIAATVPTIDRSKLLAQQQARVDELRHAKYEGILGGNPAITVVHGEARFKDDQSLTVRLNEGGERVVMFDRCLVATGASPAVPPIPGLKESPYWTSTEALASDTIPERLAVIGSSVVALELAQAFARLGSKVTVLARNTLFFREDPAIGEAVTAAFRAEGIEVLEHTQASQVAHMDGEFVLTTTHGELRADKLLVATGRTPNTRSLALDAAGVTVNAQGAIVIDQGMRTSNPNIYAAGDCTDQPQFVYVAAAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRALANFDTRGFIKLVIEEGSHRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVEGLKLAAQTFNKDVKQLSCCAG","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Pseudomonadales","Pseudomonadaceae","Pseudomonas"],"uniref50":"UniRef50_P00392","uniref90":"UniRef90_P00392","uniref100":"UniRef100_P00392","genes":[{"name":{"value":"merA"}}],"alphafold_very_low_content":0.044563279857397504,"disorder_content":0.0213903743315508,"disprot_consensus":{"full":[{"start":550,"end":561,"type":"D"}],"Structural state":[{"start":550,"end":561,"type":"D"}]}},{"disprot_id":"DP03481","acc":"P10674","creator":"ktsirigos","date":"2021-09-10T17:31:22.156Z","features":{"pfam":[{"id":"PF02469","name":"Fasciclin domain","start":32,"end":146},{"id":"PF02469","name":"Fasciclin domain","start":181,"end":311},{"id":"PF02469","name":"Fasciclin domain","start":336,"end":463},{"id":"PF02469","name":"Fasciclin domain","start":479,"end":617}],"gene3D":[]},"length":652,"name":"Fasciclin-1","ncbi_taxon_id":7227,"organism":"Drosophila melanogaster","regions":[{"start":314,"end":330,"reference_id":"12575939","reference_source":"pmid","reference_html":"Novel fold revealed by the structure of a FAS1 domain pair from the insect cell adhesion molecule fasciclin I. <i> Clout NJ, Tisi D, Hohenester E. </i> Structure, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"ktsirigos","curator_name":"Konstantinos D. Tsirigos","curator_orcid":"0000-0001-5280-1107","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"1O70"}],"region_id":"DP03481r001","statement":[{"text":"There is no density for the first 16 and last 5 residues of FasI 3-4, which are presumed to be disordered","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-09-14T14:40:47.272Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MLNAAALLLALLCAANAAAAADLADKLRDDSELSQFYSLLESNQIANSTLSLRSCTIFVPTNEAFQRYKSKTAHVLYHITTEAYTQKRLPNTVSSDMAGNPPLYITKNSNGDIFVNNARIIPSLSVETNSDGKRQIMHIIDEVLEPLTVKAGHSDTPNNPNALKFLKNAEEFNVDNIGVRTYRSQVTMAKKESVYDAAGQHTFLVPVDEGFKLSARSSLVDGKVIDGHVIPNTVIFTAAAQHDDPKASAAFEDLLKVTVSFFKQKNGKMYVKSNTIVGDAKHRVGVVLAEIVKANIPVSNGVVHLIHRPLMIIDTTVTQFLQSFKENAENGALRKFYEVIMDNGGAVLDDINSLTEVTILAPSNEAWNSSNINNVLRDRNKMRQILNMHIIKDRLNVDKIRQKNANLIAQVPTVNNNTFLYFNVRGEGSDTVITVEGGGVNATVIQADVAQTNGYVHIIDHVLGVPYTTVLGKLESDPMMSDTYKMGKFSHFNDQLNNTQRRFTYFVPRDKGWQKTELDYPSAHKKLFMADFSYHSKSILERHLAISDKEYTMKDLVKFSQESGSVILPTFRDSLSIRVEEEAGRYVIIWNYKKINVYRPDVECTNGIIHVIDYPLLEEKDVVVAGGSYLPESSICIILANLIMITVAKFLN","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref50":"UniRef50_P10674","uniref90":"UniRef90_P10674","uniref100":"UniRef100_P10674","genes":[{"name":{"value":"Fas1"},"orfNames":[{"value":"CG6588"}]}],"alphafold_very_low_content":0.029141104294478526,"disorder_content":0.02607361963190184,"disprot_consensus":{"full":[{"start":314,"end":330,"type":"D"}],"Structural state":[{"start":314,"end":330,"type":"D"}]}},{"disprot_id":"DP03482","acc":"P16243","creator":"ktsirigos","date":"2021-09-10T17:50:41.608Z","features":{"pfam":[{"id":"PF00390","name":"Malic enzyme, N-terminal domain","start":161,"end":341},{"id":"PF03949","name":"Malic enzyme, NAD binding domain","start":352,"end":605}],"gene3D":[]},"length":636,"name":"NADP-dependent malic enzyme, chloroplastic","ncbi_taxon_id":4577,"organism":"Zea mays","regions":[{"start":63,"end":79,"reference_id":"31235877","reference_source":"pmid","reference_html":"Molecular adaptations of NADP-malic enzyme for its function in C<sub>4</sub> photosynthesis in grasses. <i> Alvarez CE, Bovdilova A, Höppner A, Wolff CC, Saigo M, Trajtenberg F, Zhang T, Buschiazzo A, Nagel-Steger L, Drincovich MF, Lercher MJ, Maurino VG. </i> Nat Plants, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"ktsirigos","curator_name":"Konstantinos D. Tsirigos","curator_orcid":"0000-0001-5280-1107","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"5OU5"}],"region_id":"DP03482r003","statement":[{"text":"The aforementioned region is not visible in the crystal structure of the construct","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-09-14T22:35:27.447Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2021_12","sequence":"MLSTRTAAVAASASPASPWKLGGRSEGGASCDGCRTYRNTLRRRAAPAKVRALPPRRVDAVAMVSNAETETEKEQEEAAAASEELPVMPWATSVASGYTLLRDPHHNKGLAFTEEERDGHYLRGLLPPAVLSQELQIKKFMNTLRQYQTPLQRYIAMMNLQETDERLFYKLLIDNVVELLPFVYTPTVGEACQKYGSIFGRPQGLYVSLKDKGKVLEVLRNWPHRNIQVICVTDGERILGLGDLGCQGMGIPVGKLALYTALGGVDPSVCLPITIDVGTNNEFLLNDEFYIGLRQKRATGEEYDELIEEFMSAVKQFYGEKVLIQFEDFANHNAFDLLEKYSKSHLVFNDDIQGTASVVLAGLLAALKMVGGTLAEQTYLFLGAGEAGTGIAELIALEISKQTNAPIEECRKKVWLVDSKGLIVDSRKGSLQPFKKPWAHEHEPLKTLYDAVQSIKPTVLIGTSGVGRTFTKEIIEAMSSFNERPIIFSLSNPTSHSECTAEQAYTWSQGRSIFASGSPFAPVEYEGKTFVPGQSNNAYIFPGLGLGLVISGAVRVHEDMLLAASKALADQATQDNFEKGSIFPPFTSIRKISAHIAAAVAGKAYELGLATRLPPPSDLVKYAENCMYTPVYRNYR","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","PACMAD clade","Panicoideae","Andropogonodae","Andropogoneae","Tripsacinae","Zea"],"uniref50":"UniRef50_P16243","uniref90":"UniRef90_P16243","uniref100":"UniRef100_P16243","genes":[{"name":{"value":"MOD1"},"synonyms":[{"value":"ME1"}]}],"alphafold_very_low_content":0.10377358490566038,"disorder_content":0.026729559748427674,"disprot_consensus":{"full":[{"start":63,"end":79,"type":"D"}],"Structural state":[{"start":63,"end":79,"type":"D"}]}},{"disprot_id":"DP03483","acc":"P05661","creator":"ktsirigos","date":"2021-09-10T18:10:21.443Z","features":{"pfam":[{"id":"PF00063","name":"Myosin head (motor domain)","start":89,"end":765},{"id":"PF01576","name":"Myosin tail","start":843,"end":1922},{"id":"PF02736","name":"Myosin N-terminal SH3-like domain","start":25,"end":81}],"gene3D":[]},"length":1962,"name":"Myosin heavy chain, muscle","ncbi_taxon_id":7227,"organism":"Drosophila melanogaster","regions":[{"start":628,"end":641,"reference_id":"31786266","reference_source":"pmid","reference_html":"X-ray Crystallographic and Molecular Dynamic Analyses of Drosophila melanogaster Embryonic Muscle Myosin Define Domains Responsible for Isoform-Specific Properties. <i> Caldwell JT, Mermelstein DJ, Walker RC, Bernstein SI, Huxford T. </i> J Mol Biol, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"ktsirigos","curator_name":"Konstantinos D. Tsirigos","curator_orcid":"0000-0001-5280-1107","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03483r001","statement":[{"text":"For this purpose, a single, nucleotide-free, continuous polypeptide EMB heavy chain model (chain C) was prepared by removing the lever arm and ELC (chain D) and adding residues 628-644 to close the discontinuity in loop 2. ","type":"Results"},{"text":"y far, the most conformationally variable portion in both isoforms resides between amino acids 626 and 645.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-09-14T22:34:29.743Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MPKPVANQEDEDPTPYLFVSLEQRRIDQSKPYDSKKSCWIPDEKEGYLLGEIKATKGDIVSVGLQGGETRDLKKDLLQQVNPPKYEKAEDMSNLTYLNDASVLHNLRQRYYNKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKIMCPKLLQGVEKDKKATEIIIKFIDLPEDQYRLGNTKVFFRAGVLGQMEEFRDERLGKIMSWMQAWARGYLSRKGFKKLQEQRVALKVVQRNLRKYLQLRTWPWYKLWQKVKPLLNVSRIEDEIARLEEKAKKAEELHAAEVKVRKELEALNAKLLAEKTALLDSLSGEKGALQDYQERNAKLTAQKNDLENQLRDIQERLTQEEDARNQLFQQKKKADQEISGLKKDIEDLELNVQKAEQDKATKDHQIRNLNDEIAHQDELINKLNKEKKMQGETNQKTGEELQAAEDKINHLNKVKAKLEQTLDELEDSLEREKKVRGDVEKSKRKVEGDLKLTQEAVADLERNKKELEQTIQRKDKELSSITAKLEDEQVVVLKHQRQIKELQARIEELEEEVEAERQARAKAEKQRADLARELEELGERLEEAGGATSAQIELNKKREAELSKLRRDLEEANIQHESTLANLRKKHNDAVAEMAEQVDQLNKLKAKAEKEKNEYYGQLNDLRAGVDHITNEKAAQEKIAKQLQHTLNEVQSKLDETNRTLNDFDASKKKLSIENSDLLRQLEEAESQVSQLSKIKISLTTQLEDTKRLADEESRERATLLGKFRNLEHDLDNLREQVEEEAEGKADLQRQLSKANAEAQVWRSKYESDGVARSEELEEAKRKLQARLAEAEETIESLNQKCIGLEKTKQRLSTEVEDLQLEVDRANAIANAAEKKQKAFDKIIGEWKLKVDDLAAELDASQKECRNYSTELFRLKGAYEEGQEQLEAVRRENKNLADEVKDLLDQIGEGGRNIHEIEKARKRLEAEKDELQAALEEAEAALEQEENKVLRAQLELSQVRQEIDRRIQEKEEEFENTRKNHQRALDSMQASLEAEAKGKAEALRMKKKLEADINELEIALDHANKANAEAQKNIKRYQQQLKDIQTALEEEQRARDDAREQLGISERRANALQNELEESRTLLEQADRGRRQAEQELADAHEQLNEVSAQNASISAAKRKLESELQTLHSDLDELLNEAKNSEEKAKKAMVDAARLADELRAEQDHAQTQEKLRKALEQQIKELQVRLDEAEANALKGGKKAIQKLEQRVRELENELDGEQRRHADAQKNLRKSERRVKELSFQSEEDRKNHERMQDLVDKLQQKIKTYKRQIEEAEEIAALNLAKFRKAQQELEEAEERADLAEQAISKFRAKGRAGSVGRGASPAPRATSVRPQFDGLAFPPRFDLAPENEF","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref50":"UniRef50_P05661","uniref90":"UniRef90_P05661","uniref100":"UniRef100_P05661","genes":[{"name":{"value":"Mhc"},"orfNames":[{"value":"CG17927"}]}],"alphafold_very_low_content":0.060142711518858305,"disorder_content":0.007135575942915392,"disprot_consensus":{"full":[{"start":628,"end":641,"type":"D"}],"Structural state":[{"start":628,"end":641,"type":"D"}]}},{"disprot_id":"DP03485","acc":"Q9VKJ9","creator":"ktsirigos","date":"2021-09-10T18:35:05.076Z","features":{"pfam":[{"id":"PF00168","name":"C2 domain","start":666,"end":778},{"id":"PF21528","name":"Coiled-coil and C2 domain-containing protein 1, DM14 domain","start":145,"end":200},{"id":"PF21528","name":"Coiled-coil and C2 domain-containing protein 1, DM14 domain","start":265,"end":318},{"id":"PF21528","name":"Coiled-coil and C2 domain-containing protein 1, DM14 domain","start":365,"end":420},{"id":"PF21528","name":"Coiled-coil and C2 domain-containing protein 1, DM14 domain","start":502,"end":557}],"gene3D":[]},"length":816,"name":"Coiled-coil and C2 domain-containing protein 1-like","ncbi_taxon_id":7227,"organism":"Drosophila melanogaster","regions":[{"start":550,"end":574,"reference_id":"30513301","reference_source":"pmid","reference_html":"CC2D1B Coordinates ESCRT-III Activity during the Mitotic Reformation of the Nuclear Envelope. <i> Ventimiglia LN, Cuesta-Geijo MA, Martinelli N, Caballe A, Macheboeuf P, Miguet N, Parnham IM, Olmos Y, Carlton JG, Weissenhorn W, Martin-Serrano J. </i> Dev Cell, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"ktsirigos","curator_name":"Konstantinos D. Tsirigos","curator_orcid":"0000-0001-5280-1107","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"6EI6"}],"region_id":"DP03485r001","statement":[{"text":"The N-terminal 24 residues connecting to the DM14 4 domain and present in the crystallized construct are flexible and disordered in the structure.","type":"Results"},{"text":"N-terminal residues 550 to 576 were disordered in both protomers and 89.79/7.92 % of the residues are within the most favored and allowed regions of a Ramachandran plot ","type":"Results"},{"text":"Flexible linker connecting domain DM14 4 and the C2 domain.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-09-14T22:38:05.625Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":550,"end":574,"reference_id":"30513301","reference_source":"pmid","reference_html":"CC2D1B Coordinates ESCRT-III Activity during the Mitotic Reformation of the Nuclear Envelope. <i> Ventimiglia LN, Cuesta-Geijo MA, Martinelli N, Caballe A, Macheboeuf P, Miguet N, Parnham IM, Olmos Y, Carlton JG, Weissenhorn W, Martin-Serrano J. </i> Dev Cell, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"ktsirigos","curator_name":"Konstantinos D. Tsirigos","curator_orcid":"0000-0001-5280-1107","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"6EI6"}],"region_id":"DP03485r002","statement":[{"text":"The N-terminal 24 residues connecting to the DM14 4 domain and present in the crystallized construct are flexible and disordered in the structure.","type":"Results"},{"text":"N-terminal residues 550 to 576 were disordered in both protomers and 89.79/7.92 % of the residues are within the most favored and allowed regions of a Ramachandran plot","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-09-15T07:22:23.549Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MFSRKKPEPAKRRQHDLSQFGLTEIPDDFDPSAGYGEDDGGDSDLEAELAAITGGEGAKPKPKPKAKLLPASDLDKMIADSLRDVSDDDDDDNLESDPDLLGELSGIGGLEEAEEEEPVAQPPAASEEPVQTFLPTTTVDTLSIIKQRLEMYKQAEANAKTAGDSGKARRFGRGLKTLKDLHRQAAAGKSINVDDIPPEVSVKPIGGQAPPVPAEESPAPSTPASPPPVPSRAAPDPPTPGTPVEPTTSVAPTSPPNPLVTQMRSRQTDYKAAALQSKRSGDISTALQFLKVVKQFDVVIKMCEDGQEVDLSDMPPPPAEFLEFLKKMQEEAAAEAVAEPTAAPEPTPVAPAPVLAAATNMLEALQQRLEKYQSVEAAAKAENNSGKARRFGRIVKQYEDAIKLYKAGKPVPYDELPVPPGFGPLPTADAAPVAPTPSLPTSPTSPPPTASTSAGGTPSSSSATTPTAPRKAPSPPKPKELTTRTSGNQQKNNIAEQQMKLLLERQKEFKLAAIEAKKAGEIDQAKEYLKIFKGFDSLLNAASSGLPVDLSTLPVPPSQRDNLEASFAIVSAEECDPTDDICEIGVRMEEQLAKQLMMCKNTRDHHKAMGDVAGMNRFENLALTVQKDLDLVRYSKRKNEPLPKFHYEKRSFNIVHCNTDLTDSELEIVVVRGISYNVANPKDVDTYVRVEFPLLNDESFKTKTNVIRDTSSPDYDERFKVDIQRTNRQFQRIFKRHGVKFEIYSRGGFLRSDTLIGTVNVKLQPLETKCEIHDTYDLMDGRKQVGGKLEVKIRVRNPILTKQMEHITEKWLVLDA","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref50":"UniRef50_Q9VKJ9","uniref90":"UniRef90_Q9VKJ9","uniref100":"UniRef100_Q9VKJ9","genes":[{"name":{"value":"l(2)gd1"},"synonyms":[{"value":"lgd"}],"orfNames":[{"value":"CG4713"}]}],"alphafold_very_low_content":0.23284313725490197,"disorder_content":0.030637254901960783,"disprot_consensus":{"full":[{"start":550,"end":574,"type":"D"}],"Structural state":[{"start":550,"end":574,"type":"D"}],"Disorder function":[{"start":550,"end":574,"type":"F"}]}},{"disprot_id":"DP03486","acc":"P05031","creator":"ktsirigos","date":"2021-09-10T19:06:34.325Z","features":{"pfam":[{"id":"PF00282","name":"Pyridoxal-dependent decarboxylase conserved domain","start":70,"end":446}],"gene3D":[]},"length":510,"name":"Aromatic-L-amino-acid decarboxylase","ncbi_taxon_id":7227,"organism":"Drosophila melanogaster","regions":[{"start":357,"end":383,"reference_id":"20098687","reference_source":"pmid","reference_html":"Crystal structure and substrate specificity of Drosophila 3,4-dihydroxyphenylalanine decarboxylase. <i> Han Q, Ding H, Robinson H, Christensen BM, Li J. </i> PLoS One, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"ktsirigos","curator_name":"Konstantinos D. Tsirigos","curator_orcid":"0000-0001-5280-1107","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3K40"}],"region_id":"DP03486r001","statement":[{"text":"The fragment of V322 to P348 of both subunits in the structure was highly disordered; therefore, they were not included in the final drDDC model. ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-09-14T22:41:50.730Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MSHIPISNTIPTKQTDGNGKANISPDKLDPKVSIDMEAPEFKDFAKTMVDFIAEYLENIRERRVLPEVKPGYLKPLIPDAAPEKPEKWQDVMQDIERVIMPGVTHWHSPKFHAYFPTANSYPAIVADMLSGAIACIGFTWIASPACTELEVVMMDWLGKMLELPAEFLACSGGKGGGVIQGTASESTLVALLGAKAKKLKEVKELHPEWDEHTILGKLVGYCSDQAHSSVERAGLLGGVKLRSVQSENHRMRGAALEKAIEQDVAEGLIPFYAVVTLGTTNSCAFDYLDECGPVGNKHNLWIHVDAAYAGSAFICPEYRHLMKGIESADSFNFNPHKWMLVNFDCSAMWLKDPSWVVNAFNVDPLYLKHDMQGSAPDYRHWQIPLGRRFRALKLWFVLRLYGVENLQAHIRRHCNFAKQFGDLCVADSRFELAAEINMGLVCFRLKGSNERNEALLKRINGRGHIHLVPAKIKDVYFLRMAICSRFTQSEDMEYSWKEVSAAADEMEQEQ","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"uniref50":"UniRef50_P05031","uniref90":"UniRef90_P05031","uniref100":"UniRef100_P05031","genes":[{"name":{"value":"Ddc"},"orfNames":[{"value":"CG10697"}]}],"alphafold_very_low_content":0.045098039215686274,"disorder_content":0.052941176470588235,"disprot_consensus":{"full":[{"start":357,"end":383,"type":"D"}],"Structural state":[{"start":357,"end":383,"type":"D"}]}},{"disprot_id":"DP03487","acc":"Q9GZZ9","creator":"vsagris","date":"2021-09-11T05:30:49.769Z","features":{"pfam":[{"id":"PF00899","name":"ThiF family","start":53,"end":304}],"gene3D":[]},"length":404,"name":"Ubiquitin-like modifier-activating enzyme 5","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":325,"end":404,"reference_id":"34299007","reference_source":"pmid","reference_html":"A Concerted Action of UBA5 C-Terminal Unstructured Regions Is Important for Transfer of Activated UFM1 to UFC1. <i> Wesch N, Löhr F, Rogova N, Dötsch V, Rogov VV. </i> Int J Mol Sci, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jglavina","curator_name":"Juliana Glavina","curator_orcid":"0000-0001-6336-1290","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"7OVC"},{"db":"BMRB","id":"34638"}],"region_id":"DP03487r001","statement":[{"text":"A Concerted Action of UBA5 C-Terminal Unstructured Regions Is Important for transfer of Activated UFM1 to UFC1","type":"Title"},{"text":"We explored the hypothesis that the unstructured C-terminal region of UBA5 serves as a regulatory region, controlling cellular localization of the elements of the ufmylation cascade and effective interaction between them. We found that the last 20 residues in UBA5 are pivotal for binding to UFC1 and can accelerate the transfer of UFM1 to UFC1. We solved the structure of a complex of UFC1 and a peptide spanning the last 20 residues of UBA5 by NMR spectroscopy. This structure in combination with additional NMR titration and isothermal titration calorimetry experiments revealed the mechanism of interaction and confirmed the importance of the C-terminal unstructured region in UBA5 for the ufmylation cascade.","type":"Abstract"},{"text":"The structures of UBA5 AD (brown), UFM1 (cyan) and UFC1 (grey)\nare represented as ribbon diagrams; the UBA5 unstructured C-terminus containing regions R1 (orange), R2 (green) and R3\n(violet) is shown as dashed lines. The structures were generated from PDB entry 5IAA [29].","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-21T07:21:10.670Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":384,"end":404,"reference_id":"34299007","reference_source":"pmid","reference_html":"A Concerted Action of UBA5 C-Terminal Unstructured Regions Is Important for Transfer of Activated UFM1 to UFC1. <i> Wesch N, Löhr F, Rogova N, Dötsch V, Rogov VV. </i> Int J Mol Sci, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jglavina","curator_name":"Juliana Glavina","curator_orcid":"0000-0001-6336-1290","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"7OVC"},{"db":"BMRB","id":"34638"}],"region_id":"DP03487r002","statement":[{"text":"Residues 394–404 of the R3 region form the predicted [32] α-helix, residues 384–392 are in an extended conformation, well-defined and occupy a specific area on the UFC1 surface. Residues 381–383 seem disordered and do not interact specifically with any UFC1 residues.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-21T07:21:22.424Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":384,"end":404,"reference_id":"34299007","reference_source":"pmid","reference_html":"A Concerted Action of UBA5 C-Terminal Unstructured Regions Is Important for Transfer of Activated UFM1 to UFC1. <i> Wesch N, Löhr F, Rogova N, Dötsch V, Rogov VV. </i> Int J Mol Sci, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jglavina","curator_name":"Juliana Glavina","curator_orcid":"0000-0001-6336-1290","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"7OVC"},{"db":"BMRB","id":"34638"}],"interaction_partner":[{"db":"UniProt","id":"Q9Y3C8","partner_start":null,"partner_end":null}],"region_id":"DP03487r003","statement":[{"text":"Residues 394–404 of the R3 region form the predicted [32] α-helix, residues 384–392 are in an extended conformation, well-defined and occupy a specific area on the UFC1 surface. Residues 381–383 seem disordered and do not interact specifically with any UFC1 residues.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-21T07:22:34.409Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":325,"end":357,"reference_id":"34299007","reference_source":"pmid","reference_html":"A Concerted Action of UBA5 C-Terminal Unstructured Regions Is Important for Transfer of Activated UFM1 to UFC1. <i> Wesch N, Löhr F, Rogova N, Dötsch V, Rogov VV. </i> Int J Mol Sci, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jglavina","curator_name":"Juliana Glavina","curator_orcid":"0000-0001-6336-1290","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"P61960","partner_start":null,"partner_end":null}],"region_id":"DP03487r004","statement":[{"text":"The affinity of UFM1 to the R1-containing peptides (R1-R2-R3 325–404 and R1-R2 325–376, Supplementary Figure S2B and Table 2) does not change significantly compared to the\naffinity of the isolated R1 325 − 357 peptide [31], indicating that this interaction is completely located within the LIR/UFIM containing region.","type":"Results"},{"text":"While UFM1 seems to bind only to the LIR/UFIM region of UBA5, LC3/GABARAP proteins interact with additional residues outside of the of the R1 sequence.","type":"Results"},{"text":"In general, we were able to observe relatively stable interactions between members of the ufmylation cascade only for the R1:UFM1 and R3:UFC1 interactions.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-21T07:22:33.201Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":325,"end":376,"reference_id":"34299007","reference_source":"pmid","reference_html":"A Concerted Action of UBA5 C-Terminal Unstructured Regions Is Important for Transfer of Activated UFM1 to UFC1. <i> Wesch N, Löhr F, Rogova N, Dötsch V, Rogov VV. </i> Int J Mol Sci, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jglavina","curator_name":"Juliana Glavina","curator_orcid":"0000-0001-6336-1290","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"Q9H492","partner_start":null,"partner_end":null}],"region_id":"DP03487r005","statement":[{"text":"In contrast, LC3/GABARAP proteins showed a 10-fold higher affinity to the R1-R2-R3 325–404 and R1-R2 325–376 peptides compared to the isolated LIR/UFIM motif (R1 337 − 348 ) characterized in [31,33]. The K D values for interactions between R1-R2-R3 325–404 and GABARAPL2 (0.17 µM) or LC3B (3.7 µM) indicate the same subfamily-specific preferences that were reported previously (Supplementary Figure S2C,D).","type":"Results"},{"text":"While UFM1 seems to bind only to the LIR/UFIM region of UBA5, LC3/GABARAP proteins interact with additional residues outside of the of the R1 sequence. LC3 and GABARAP subfamily proteins showed a 10-fold higher affinity to the complete UBA5 C-terminus compared to the isolated R1 peptide.","type":"Results"},{"text":"The GABARAP and LC3 subfamilies members were found to bind UBA5 via an atypical LIR (LIR/UFIM), an evolutionary conserved sequence within the UBA5 C-terminal part [31,33]. The ITC and NMR experiments revealed additional interactions next to the known binding site within the R1. UBA5 constructs including both R1 and R2 regions showed a 10fold higher binding affinity to all GABARAP and LC3 protein subfamily members.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-21T07:21:43.151Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":325,"end":376,"reference_id":"34299007","reference_source":"pmid","reference_html":"A Concerted Action of UBA5 C-Terminal Unstructured Regions Is Important for Transfer of Activated UFM1 to UFC1. <i> Wesch N, Löhr F, Rogova N, Dötsch V, Rogov VV. </i> Int J Mol Sci, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jglavina","curator_name":"Juliana Glavina","curator_orcid":"0000-0001-6336-1290","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"Q9GZQ8","partner_start":null,"partner_end":null}],"region_id":"DP03487r006","statement":[{"text":"In contrast, LC3/GABARAP proteins showed a 10-fold higher affinity to the R1-R2-R3 325–404 and R1-R2 325–376 peptides compared to the isolated LIR/UFIM motif (R1 337 − 348 ) characterized in [31,33]. The K D values for interactions between R1-R2-R3 325–404 and GABARAPL2 (0.17 µM) or LC3B (3.7 µM) indicate the same subfamily-specific preferences that were reported previously (Supplementary Figure S2C,D).","type":"Results"},{"text":"While UFM1 seems to bind only to the LIR/UFIM region of UBA5, LC3/GABARAP proteins interact with additional residues outside of the of the R1 sequence. LC3 and GABARAP subfamily proteins showed a 10-fold higher affinity to the complete UBA5 C-terminus compared to the isolated R1 peptide.","type":"Results"},{"text":"The GABARAP and LC3 subfamilies members were found to bind UBA5 via an atypical LIR (LIR/UFIM), an evolutionary conserved sequence within the UBA5 C-terminal part [31,33]. The ITC and NMR experiments revealed additional interactions next to the known binding site within the R1. UBA5 constructs including both R1 and R2 regions showed a 10fold higher binding affinity to all GABARAP and LC3 protein subfamily members.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-21T07:21:41.751Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":359,"end":404,"reference_id":"34299007","reference_source":"pmid","reference_html":"A Concerted Action of UBA5 C-Terminal Unstructured Regions Is Important for Transfer of Activated UFM1 to UFC1. <i> Wesch N, Löhr F, Rogova N, Dötsch V, Rogov VV. </i> Int J Mol Sci, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jglavina","curator_name":"Juliana Glavina","curator_orcid":"0000-0001-6336-1290","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"Q9Y3C8","partner_start":null,"partner_end":null}],"region_id":"DP03487r007","statement":[{"text":"The affinity of the interaction between UBA5 and UFC1 has not been characterized previously. In ITC experiments, the shortest UBA5 peptide spanning the R3 sequence (R3 388–404 ) bound to UFC1 with a K D of >11 µM. The affinity increased 3-fold for R2-R3 359–404 and R1-R2-R3 325–404 peptides (K D of 2.7 and 2.4 µM, respectively; Figure 2A and Table 2).","type":"Results"},{"text":"Taken together, we identified a UFC1-interacting region within the UBA5 C-terminus using ITC and NMR experiments. The region is slightly longer than the conserved R3 sequence which was detected previously and shows a micromolar affinity to UFC1.","type":"Results"},{"text":"Additionally, UFC1 showed interaction outside of the R3 region, binding residues within the R2 region. NMR titrations revealed that UFC1 and GABARAPL2 have a more complex binding mechanism to the UBA5 C-terminus, involving some residues in the R2 region. However, no direct interactions of all tested proteins to the isolated R2 peptide were observed.","type":"Results"},{"text":"Our ITC and NMR titration experiments revealed that the interaction between UFC1 and UBA5 is mediated mostly by the relatively short and evolutionary conserved stretch of UBA5 residues (383–404).","type":"Discussion"},{"text":"The complex structure in combination with the NMR and ITC titration experiments revealed that in addition to the core R3 region, residues in the region R2 contribute to the interaction. While the isolated R2 peptide does not interact with UFC1, the combination of R2 and R3 binds three times tighter than the R3 alone.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-21T07:21:36.421Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":359,"end":404,"reference_id":"34299007","reference_source":"pmid","reference_html":"A Concerted Action of UBA5 C-Terminal Unstructured Regions Is Important for Transfer of Activated UFM1 to UFC1. <i> Wesch N, Löhr F, Rogova N, Dötsch V, Rogov VV. </i> Int J Mol Sci, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jglavina","curator_name":"Juliana Glavina","curator_orcid":"0000-0001-6336-1290","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"Q9Y3C8","partner_start":null,"partner_end":null}],"region_id":"DP03487r008","statement":[{"text":"To understand the role of the UBA5 C-terminal region in coordination of the binding events reported above on the molecular level, we performed NMR titration experiments. In those experiments, we titrated non-labeled UFC1 and GABARAPL2 proteins to a 15 N-labeled R1-R2-R3 325–404 peptide. The NMR experiments revealed that the interaction between UFC1 and UBA5 is mediated mostly by the UBA5 residues 386–404. These residues (in contrast to the vast majority of the R1-R2-R3 325–404 resonances, which are not affected by addition of UFC1) showed a slow-to-intermediate exchange mode. The amide backbone resonances of these residues disappeared with small chemical shift perturbation (CSP) at the earlier stages of titrations and did not appear again up to an 8-fold molar excess of UFC1 (Figure 2B, the full size spectra are presented in Supplementary Figure S3D). UBA5 residues 383–386, 400 and 403 appeared to be in intermediate exchange mode (their amide backbone resonances displayed CSP with intensity change, however, they became visible at the latest titration steps). It seems, that these UBA5 residues form additional interactions with UFC1. Interestingly, a subset of the residues within the R2 region (V370, A371, Y372 and T373) displayed moderate CSPs, however, below standard deviation level (Figure 2C), possibly indicating an influence of the UBA5 A371T mutation on the recognition of UFC1.","type":"Results"},{"text":"Taken together, we identified a UFC1-interacting region within the UBA5 C-terminus using ITC and NMR experiments. The region is slightly longer than the conserved R3 sequence which was detected previously and shows a micromolar affinity to UFC1.","type":"Results"},{"text":"Additionally, UFC1 showed interaction outside of the R3 region, binding residues within the R2 region. NMR titrations revealed that UFC1 and GABARAPL2 have a more complex binding mechanism to the UBA5 C-terminus, involving some residues in the R2 region. However, no direct interactions of all tested proteins to the isolated R2 peptide were observed.","type":"Results"},{"text":"Our ITC and NMR titration experiments revealed that the interaction between UFC1 and UBA5 is mediated mostly by the relatively short and evolutionary conserved stretch of UBA5 residues (383–404).","type":"Discussion"},{"text":"The complex structure in combination with the NMR and ITC titration experiments revealed that in addition to the core R3 region, residues in the region R2 contribute to the interaction. While the isolated R2 peptide does not interact with UFC1, the combination of R2 and R3 binds three times tighter than the R3 alone.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-21T07:21:34.279Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":338,"end":346,"reference_id":"26929408","reference_source":"pmid","reference_html":"Structural and Functional Analysis of a Novel Interaction Motif within UFM1-activating Enzyme 5 (UBA5) Required for Binding to Ubiquitin-like Proteins and Ufmylation. <i> Habisov S, Huber J, Ichimura Y, Akutsu M, Rogova N, Loehr F, McEwan DG, Johansen T, Dikic I, Doetsch V, Komatsu M, Rogov VV, Kirkin V. </i> J Biol Chem, 2016","date":"2022-06-22T15:46:49.332Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_06","version":1,"cross_refs":[{"db":"PDB","id":"5HKH"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P61960","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03487r009","statement":[{"text":"In this study, we described and characterized a combined linear LC3-interacting region/UFM1-interacting motif (LIR/UFIM) within the C terminus of UBA5. This single motif ensures that UBA5 binds both UFM1 and light chain 3/γ-aminobutyric acid receptor-associated proteins (LC3/GABARAP), two ubiquitin (Ub)-like proteins. We demonstrated that LIR/UFIM is required for the full biological activity of UBA5 and for the effective transfer of UFM1 onto UFC1 and a downstream protein substrate both in vitro and in cells. Taken together, our study provides important structural and functional insights into the interaction between UBA5 and Ub-like modifiers, improving the understanding of the biology of the ufmylation pathway.","type":"Abstract"},{"text":"In the current study, we have identified a short linear motif in the C terminus of UBA5 that drives the interaction with either UFM1 or LC3/GABARAP proteins, defining this as a LIR/UFIM (for LC3-interacting region/UFM1-interacting motif). We present structural details for its interaction with UFM1 and model its interaction with GABARAPL2 and LC3B.","type":"Introduction"},{"text":"A key residue, Ile-343, of the LIR/UFIM occupies the hydrophobic pocket (somewhat similar to HP2 in LC3) formed by the residues of Leu-21, Val-23, Val-32, and Phe-35 of UFM1 (Fig. 4, B and C). Additionally, Trp-341 and Val-346 of UBA5 LIR/UFIM interact with Pro-28 and Val-20 of UFM1, respectively (Fig. 4B). Trp-341 does not intercalate into the hydrophobic core of UFM1 but covers a significant part of the nonpolar surface, playing an important role in the complex stabilization. Leu-345 completes the formation of the hydrophobic cluster within the complex by contacts to the hydrophobic side chains of UFM1 (Val-20, Leu-21, and Val-23) (Fig. 4B).","type":"Results"},{"text":"The region includes the non-canonical LIR motif \"WGIELV\".","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:39:47.674Z"}},{"start":338,"end":346,"reference_id":"26929408","reference_source":"pmid","reference_html":"Structural and Functional Analysis of a Novel Interaction Motif within UFM1-activating Enzyme 5 (UBA5) Required for Binding to Ubiquitin-like Proteins and Ufmylation. <i> Habisov S, Huber J, Ichimura Y, Akutsu M, Rogova N, Loehr F, McEwan DG, Johansen T, Dikic I, Doetsch V, Komatsu M, Rogov VV, Kirkin V. </i> J Biol Chem, 2016","date":"2022-06-22T15:46:20.858Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_06","version":1,"ec_go":"EXP","region_id":"DP03487r010","statement":[{"text":"In this study, we described and characterized a combined linear LC3-interacting region/UFM1-interacting motif (LIR/UFIM) within the C terminus of UBA5. This single motif ensures that UBA5 binds both UFM1 and light chain 3/γ-aminobutyric acid receptor-associated proteins (LC3/GABARAP), two ubiquitin (Ub)-like proteins. We demonstrated that LIR/UFIM is required for the full biological activity of UBA5 and for the effective transfer of UFM1 onto UFC1 and a downstream protein substrate both in vitro and in cells. Taken together, our study provides important structural and functional insights into the interaction between UBA5 and Ub-like modifiers, improving the understanding of the biology of the ufmylation pathway.","type":"Abstract"},{"text":"In the current study, we have identified a short linear motif in the C terminus of UBA5 that drives the interaction with either UFM1 or LC3/GABARAP proteins, defining this as a LIR/UFIM (for LC3-interacting region/UFM1-interacting motif). We present structural details for its interaction with UFM1 and model its interaction with GABARAPL2 and LC3B.","type":"Introduction"},{"text":"A key residue, Ile-343, of the LIR/UFIM occupies the hydrophobic pocket (somewhat similar to HP2 in LC3) formed by the residues of Leu-21, Val-23, Val-32, and Phe-35 of UFM1 (Fig. 4, B and C). Additionally, Trp-341 and Val-346 of UBA5 LIR/UFIM interact with Pro-28 and Val-20 of UFM1, respectively (Fig. 4B). Trp-341 does not intercalate into the hydrophobic core of UFM1 but covers a significant part of the nonpolar surface, playing an important role in the complex stabilization. Leu-345 completes the formation of the hydrophobic cluster within the complex by contacts to the hydrophobic side chains of UFM1 (Val-20, Leu-21, and Val-23) (Fig. 4B).","type":"Results"},{"text":"The region includes the non-canonical LIR motif \"WGIELV\".","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:39:49.773Z"}},{"start":338,"end":346,"reference_id":"26929408","reference_source":"pmid","reference_html":"Structural and Functional Analysis of a Novel Interaction Motif within UFM1-activating Enzyme 5 (UBA5) Required for Binding to Ubiquitin-like Proteins and Ufmylation. <i> Habisov S, Huber J, Ichimura Y, Akutsu M, Rogova N, Loehr F, McEwan DG, Johansen T, Dikic I, Doetsch V, Komatsu M, Rogov VV, Kirkin V. </i> J Biol Chem, 2016","date":"2022-06-22T15:45:59.739Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":1,"ec_go":"EXP","region_id":"DP03487r011","statement":[{"text":"In this study, we described and characterized a combined linear LC3-interacting region/UFM1-interacting motif (LIR/UFIM) within the C terminus of UBA5. This single motif ensures that UBA5 binds both UFM1 and light chain 3/γ-aminobutyric acid receptor-associated proteins (LC3/GABARAP), two ubiquitin (Ub)-like proteins. We demonstrated that LIR/UFIM is required for the full biological activity of UBA5 and for the effective transfer of UFM1 onto UFC1 and a downstream protein substrate both in vitro and in cells. Taken together, our study provides important structural and functional insights into the interaction between UBA5 and Ub-like modifiers, improving the understanding of the biology of the ufmylation pathway.","type":"Abstract"},{"text":"In the current study, we have identified a short linear motif in the C terminus of UBA5 that drives the interaction with either UFM1 or LC3/GABARAP proteins, defining this as a LIR/UFIM (for LC3-interacting region/UFM1-interacting motif). We present structural details for its interaction with UFM1 and model its interaction with GABARAPL2 and LC3B. By combining biophysical, biochemical and cellular techniques, we have provided a detailed characterization of the new UBL-binding motif and generated evidence for its role in the ability of UBA5 to mediate UFM1 conjugation in vitro and in cells. Our data suggest that a single UBL-binding element within UBA5 is responsible for both its function as an E1 enzyme in the ufmylation pathway and the interaction with LC3/GABARAP proteins.","type":"Introduction"},{"text":"NMR titration experiments confirmed the ITC data for the UFM1-LIR/UFIM interaction. We observed a typical pattern for interaction of two polypeptides with a KD in the range of 10 μm (Fig. 2D). Chemical shift perturbations (CSPs) induced by titration of the nonlabeled LIR/UFIM peptide into 15N-labeled UFM1 were moderate and mostly in intermediate to slow exchange modes. In particular, CSPs of Val-20, Leu-21, Ser-22, Val-23, Ser-26, Ala-31, Val-32, Leu-33, Ala-36, Glu-39, and Ala-63 indicated strong participation of these residues in the intermolecular contacts. However, some resonances of the UFM1 residues show significant CSP in the fast exchange mode (e.g. Ser-2, Phe-6, Lys-7, Lys-19, Thr-30, Lys-34, Phe-35, Ala-37, and Phe-40) (Fig. 2D and data not shown).","type":"Results"},{"text":"The biggest CSPs are localized within the area composed of β-strand 2 and parts of α-helix 1 (residues 20–23 and 31–36), comprising a hydrophobic spot on the UFM1 surface. The UFM1 residues within long loop 1, connecting β-strands 1 and 2, remained mostly unassigned even after formation of the complex with the LIR/UFIM, in agreement with previous observations (34). However, a few assigned residues within loop 1 showed almost no CSPs, indicating a weak contribution of this element to the interaction.","type":"Results"},{"text":"The region includes the non-canonical LIR motif \"WGIELV\".","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:39:51.816Z"}},{"start":338,"end":346,"reference_id":"26929408","reference_source":"pmid","reference_html":"Structural and Functional Analysis of a Novel Interaction Motif within UFM1-activating Enzyme 5 (UBA5) Required for Binding to Ubiquitin-like Proteins and Ufmylation. <i> Habisov S, Huber J, Ichimura Y, Akutsu M, Rogova N, Loehr F, McEwan DG, Johansen T, Dikic I, Doetsch V, Komatsu M, Rogov VV, Kirkin V. </i> J Biol Chem, 2016","date":"2022-06-22T15:45:29.136Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":1,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P61960","operator":null,"partner_start":20,"partner_end":23},{"db":"UniProt","id":"P61960","operator":"and","partner_start":31,"partner_end":36}],"region_id":"DP03487r012","statement":[{"text":"In this study, we described and characterized a combined linear LC3-interacting region/UFM1-interacting motif (LIR/UFIM) within the C terminus of UBA5. This single motif ensures that UBA5 binds both UFM1 and light chain 3/γ-aminobutyric acid receptor-associated proteins (LC3/GABARAP), two ubiquitin (Ub)-like proteins. We demonstrated that LIR/UFIM is required for the full biological activity of UBA5 and for the effective transfer of UFM1 onto UFC1 and a downstream protein substrate both in vitro and in cells. Taken together, our study provides important structural and functional insights into the interaction between UBA5 and Ub-like modifiers, improving the understanding of the biology of the ufmylation pathway.","type":"Abstract"},{"text":"In the current study, we have identified a short linear motif in the C terminus of UBA5 that drives the interaction with either UFM1 or LC3/GABARAP proteins, defining this as a LIR/UFIM (for LC3-interacting region/UFM1-interacting motif). We present structural details for its interaction with UFM1 and model its interaction with GABARAPL2 and LC3B. By combining biophysical, biochemical and cellular techniques, we have provided a detailed characterization of the new UBL-binding motif and generated evidence for its role in the ability of UBA5 to mediate UFM1 conjugation in vitro and in cells. Our data suggest that a single UBL-binding element within UBA5 is responsible for both its function as an E1 enzyme in the ufmylation pathway and the interaction with LC3/GABARAP proteins.","type":"Introduction"},{"text":"NMR titration experiments confirmed the ITC data for the UFM1-LIR/UFIM interaction. We observed a typical pattern for interaction of two polypeptides with a KD in the range of 10 μm (Fig. 2D). Chemical shift perturbations (CSPs) induced by titration of the nonlabeled LIR/UFIM peptide into 15N-labeled UFM1 were moderate and mostly in intermediate to slow exchange modes. In particular, CSPs of Val-20, Leu-21, Ser-22, Val-23, Ser-26, Ala-31, Val-32, Leu-33, Ala-36, Glu-39, and Ala-63 indicated strong participation of these residues in the intermolecular contacts. However, some resonances of the UFM1 residues show significant CSP in the fast exchange mode (e.g. Ser-2, Phe-6, Lys-7, Lys-19, Thr-30, Lys-34, Phe-35, Ala-37, and Phe-40) (Fig. 2D and data not shown).","type":"Results"},{"text":"The biggest CSPs are localized within the area composed of β-strand 2 and parts of α-helix 1 (residues 20–23 and 31–36), comprising a hydrophobic spot on the UFM1 surface. The UFM1 residues within long loop 1, connecting β-strands 1 and 2, remained mostly unassigned even after formation of the complex with the LIR/UFIM, in agreement with previous observations (34). However, a few assigned residues within loop 1 showed almost no CSPs, indicating a weak contribution of this element to the interaction.","type":"Results"},{"text":"The region includes the non-canonical LIR motif \"WGIELV\".","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:39:54.291Z"}},{"start":338,"end":346,"reference_id":"26929408","reference_source":"pmid","reference_html":"Structural and Functional Analysis of a Novel Interaction Motif within UFM1-activating Enzyme 5 (UBA5) Required for Binding to Ubiquitin-like Proteins and Ufmylation. <i> Habisov S, Huber J, Ichimura Y, Akutsu M, Rogova N, Loehr F, McEwan DG, Johansen T, Dikic I, Doetsch V, Komatsu M, Rogov VV, Kirkin V. </i> J Biol Chem, 2016","date":"2022-06-22T15:45:07.999Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_06","version":1,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"O95166","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9H0R8","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P60520","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P61960","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP03487r013","statement":[{"text":"In this study, we described and characterized a combined linear LC3-interacting region/UFM1-interacting motif (LIR/UFIM) within the C terminus of UBA5. This single motif ensures that UBA5 binds both UFM1 and light chain 3/γ-aminobutyric acid receptor-associated proteins (LC3/GABARAP), two ubiquitin (Ub)-like proteins. We demonstrated that LIR/UFIM is required for the full biological activity of UBA5 and for the effective transfer of UFM1 onto UFC1 and a downstream protein substrate both in vitro and in cells. Taken together, our study provides important structural and functional insights into the interaction between UBA5 and Ub-like modifiers, improving the understanding of the biology of the ufmylation pathway.","type":"Abstract"},{"text":"In the current study, we have identified a short linear motif in the C terminus of UBA5 that drives the interaction with either UFM1 or LC3/GABARAP proteins, defining this as a LIR/UFIM (for LC3-interacting region/UFM1-interacting motif). We present structural details for its interaction with UFM1 and model its interaction with GABARAPL2 and LC3B. By combining biophysical, biochemical and cellular techniques, we have provided a detailed characterization of the new UBL-binding motif and generated evidence for its role in the ability of UBA5 to mediate UFM1 conjugation in vitro and in cells. Our data suggest that a single UBL-binding element within UBA5 is responsible for both its function as an E1 enzyme in the ufmylation pathway and the interaction with LC3/GABARAP proteins.","type":"Introduction"},{"text":"We then characterized the interaction between UBLs and a synthetic peptide spanning the human UBA5 LIR/UFIM sequence by biophysical methods. The ITC experiment using purified UFM1 protein and the LIR/UFIM peptide showed that the affinity of the UFM1-LIR/UFIM interaction (Fig. 2C, left plot, and Table 5) lies in the middle range (KD of 8 μm).","type":"Results"},{"text":"We also analyzed interactions between the LC3/GABARAP proteins and the LIR/UFIM peptide. According to the ITC data, all GABARAP-type proteins had a significant preference for LIR/UFIM binding (Fig. 3A and Table 5), with GABARAPL2 showing the highest affinity for LIR/UFIM (KD of 1.6 μm) followed by GABARAPL1 and GABARAP (with KD of 6 and 16 μm, respectively).","type":"Results"},{"text":"The region includes the non-canonical LIR motif \"WGIELV\".","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:39:56.778Z"}},{"start":338,"end":346,"reference_id":"26929408","reference_source":"pmid","reference_html":"Structural and Functional Analysis of a Novel Interaction Motif within UFM1-activating Enzyme 5 (UBA5) Required for Binding to Ubiquitin-like Proteins and Ufmylation. <i> Habisov S, Huber J, Ichimura Y, Akutsu M, Rogova N, Loehr F, McEwan DG, Johansen T, Dikic I, Doetsch V, Komatsu M, Rogov VV, Kirkin V. </i> J Biol Chem, 2016","date":"2022-06-22T15:44:34.029Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_06","version":1,"ec_go":"IPI","region_id":"DP03487r014","statement":[{"text":"In this study, we described and characterized a combined linear LC3-interacting region/UFM1-interacting motif (LIR/UFIM) within the C terminus of UBA5. This single motif ensures that UBA5 binds both UFM1 and light chain 3/γ-aminobutyric acid receptor-associated proteins (LC3/GABARAP), two ubiquitin (Ub)-like proteins. We demonstrated that LIR/UFIM is required for the full biological activity of UBA5 and for the effective transfer of UFM1 onto UFC1 and a downstream protein substrate both in vitro and in cells. Taken together, our study provides important structural and functional insights into the interaction between UBA5 and Ub-like modifiers, improving the understanding of the biology of the ufmylation pathway.","type":"Abstract"},{"text":"In the current study, we have identified a short linear motif in the C terminus of UBA5 that drives the interaction with either UFM1 or LC3/GABARAP proteins, defining this as a LIR/UFIM (for LC3-interacting region/UFM1-interacting motif). We present structural details for its interaction with UFM1 and model its interaction with GABARAPL2 and LC3B. By combining biophysical, biochemical and cellular techniques, we have provided a detailed characterization of the new UBL-binding motif and generated evidence for its role in the ability of UBA5 to mediate UFM1 conjugation in vitro and in cells. Our data suggest that a single UBL-binding element within UBA5 is responsible for both its function as an E1 enzyme in the ufmylation pathway and the interaction with LC3/GABARAP proteins.","type":"Introduction"},{"text":"We then characterized the interaction between UBLs and a synthetic peptide spanning the human UBA5 LIR/UFIM sequence by biophysical methods. The ITC experiment using purified UFM1 protein and the LIR/UFIM peptide showed that the affinity of the UFM1-LIR/UFIM interaction (Fig. 2C, left plot, and Table 5) lies in the middle range (KD of 8 μm).","type":"Results"},{"text":"We also analyzed interactions between the LC3/GABARAP proteins and the LIR/UFIM peptide. According to the ITC data, all GABARAP-type proteins had a significant preference for LIR/UFIM binding (Fig. 3A and Table 5), with GABARAPL2 showing the highest affinity for LIR/UFIM (KD of 1.6 μm) followed by GABARAPL1 and GABARAP (with KD of 6 and 16 μm, respectively).","type":"Results"},{"text":"The region includes the non-canonical LIR motif \"WGIELV\".","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"O95166","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9H0R8","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P60520","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P61960","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:39:58.633Z"}},{"start":333,"end":348,"reference_id":"30990354","reference_source":"pmid","reference_html":"An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5. <i> Huber J, Obata M, Gruber J, Akutsu M, Löhr F, Rogova N, Güntert P, Dikic I, Kirkin V, Komatsu M, Dötsch V, Rogov VV. </i> Autophagy, 2020","date":"2022-06-22T15:44:13.042Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":1,"cross_refs":[{"db":"PDB","id":"6H8C"}],"ec_go":"EXP","region_id":"DP03487r015","statement":[{"text":"An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5","type":"Title"},{"text":"Structural analysis of GABARAP proteins in complex with the UBA5 LIR peptide reveals a new molecular mechanism of Atg8:LIR interactions","type":"Results"},{"text":"We previously showed that UBA5 has an unusual LIR motif consisting of the core sequence EWGIELVSE, which predominantly interacts with GABARAP proteins [24] and does not align with other known LIR motifs [3]. To understand the molecular mechanism of this interaction, we solved the NMR solution structure of GABARAPL2 in complex with a peptide spanning residues 333–348 of UBA5 (Figure 1(a).).","type":"Results"},{"text":"The region includes the non-canonical LIR motif \"WGIELV\".","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:40:00.996Z"}},{"start":333,"end":348,"reference_id":"30990354","reference_source":"pmid","reference_html":"An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5. <i> Huber J, Obata M, Gruber J, Akutsu M, Löhr F, Rogova N, Güntert P, Dikic I, Kirkin V, Komatsu M, Dötsch V, Rogov VV. </i> Autophagy, 2020","date":"2022-06-22T15:43:46.895Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":1,"cross_refs":[{"db":"PDB","id":"6H8C"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P60520","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03487r016","statement":[{"text":"An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5","type":"Title"},{"text":"Structural analysis of GABARAP proteins in complex with the UBA5 LIR peptide reveals a new molecular mechanism of Atg8:LIR interactions","type":"Results"},{"text":"We previously showed that UBA5 has an unusual LIR motif consisting of the core sequence EWGIELVSE, which predominantly interacts with GABARAP proteins [24] and does not align with other known LIR motifs [3]. To understand the molecular mechanism of this interaction, we solved the NMR solution structure of GABARAPL2 in complex with a peptide spanning residues 333–348 of UBA5 (Figure 1(a).).","type":"Results"},{"text":"The region includes the non-canonical LIR motif \"WGIELV\".","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:40:03.345Z"}},{"start":333,"end":348,"reference_id":"30990354","reference_source":"pmid","reference_html":"An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5. <i> Huber J, Obata M, Gruber J, Akutsu M, Löhr F, Rogova N, Güntert P, Dikic I, Kirkin V, Komatsu M, Dötsch V, Rogov VV. </i> Autophagy, 2020","date":"2022-06-22T15:43:06.118Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001245","ec_ontology":"ECO","ec_name":"peptide array evidence used in manual assertion","unpublished":true,"released":"2022_06","version":1,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp341Phe","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp341Tyr","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp341Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp341Ile","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp341Leu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp341Met","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp341Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile343Phe","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp341Trp","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp341Tyr","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp341Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp341Leu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp341Met","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp341Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu345Phe","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu345Trp","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu345Tyr","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu345Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu345Ile","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu345Met","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu345Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val346Phe","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val346Trp","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val346Tyr","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val346Ile","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val346Leu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val346Met","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val346Ala","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"6H8C"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P60520","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03487r017","statement":[{"text":"An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5","type":"Title"},{"text":"To analyze the importance of each hydrophobic residue within the core UBA5 LIR motif for the binding to GABARAP proteins, we performed peptide arrays, in which we mutated residues W341, I343, L345 and V346 of UBA5 to other hydrophobic amino acids (W, F, Y, I, L, V, M and A). In agreement with our structural analysis, mutations of I343 and L345, which occupy HP1, as well as V346, which occupies HP2, results in a moderate decrease in binding affinity of up to 30% (Figure 1(d)). Thus, these UBA5 LIR residues do not form the critical specific contacts to GABARAPs and could be substituted by any hydrophobic residues without drastic effects. In contrast, W341 appears to be crucial for binding: only aromatic amino acids are tolerated at this position and mutations to any other aliphatic residue abrogated the interaction almost completely (Figure 1(d)). This is in line with our previous results [24], where mutating W341 to alanine (W341A) resulted in a loss of binding of the full-length UBA5 to GABARAPs in pull-down experiments, while the mutations I343A, L345A and V346A only partially reduced the interaction.","type":"Results"},{"text":"The region includes the non-canonical LIR motif \"WGIELV\".","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:40:05.316Z"}},{"start":333,"end":348,"reference_id":"30990354","reference_source":"pmid","reference_html":"An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5. <i> Huber J, Obata M, Gruber J, Akutsu M, Löhr F, Rogova N, Güntert P, Dikic I, Kirkin V, Komatsu M, Dötsch V, Rogov VV. </i> Autophagy, 2020","date":"2022-06-22T15:42:37.084Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0051179","term_name":"localization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005601","ec_ontology":"ECO","ec_name":"immunofluorescence confocal microscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":1,"annotation_extensions":[{"operator":null,"relation":"occurs_in","value":"GO:0005783"}],"cross_refs":[{"db":"PDB","id":"6H8C"}],"ec_go":"IDA","region_id":"DP03487r018","statement":[{"text":"An atypical LIR motif within UBA5 (ubiquitin like modifier activating enzyme 5) interacts with GABARAP proteins and mediates membrane localization of UBA5","type":"Title"},{"text":"The interaction between UBA5 and GABARAP proteins is crucial for UBA5 localization to ER membranes","type":"Results"},{"text":"Taken together, we could show that GABARAP proteins regulates the cellular localization of UBA5 by recruiting it to ER membranes and thus serves as a recruitment factor for UBA5. Consequently, this UBA5 localization predetermined the functional activity of the UFL1/UFBP1 E3 complexes within the ER, highlighting the role of GABARAPs as a signaling scaffold in the ufmylation pathway.","type":"Results"},{"text":"The region includes the non-canonical LIR motif \"WGIELV\".","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.\" [GOC:ai, GOC:dos]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:40:17.509Z"}},{"start":338,"end":346,"reference_id":"26929408","reference_source":"pmid","reference_html":"Structural and Functional Analysis of a Novel Interaction Motif within UFM1-activating Enzyme 5 (UBA5) Required for Binding to Ubiquitin-like Proteins and Ufmylation. <i> Habisov S, Huber J, Ichimura Y, Akutsu M, Rogova N, Loehr F, McEwan DG, Johansen T, Dikic I, Doetsch V, Komatsu M, Rogov VV, Kirkin V. </i> J Biol Chem, 2016","date":"2022-06-22T15:42:07.099Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0071569","term_name":"protein ufmylation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000314","ec_ontology":"ECO","ec_name":"direct assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":1,"ec_go":"IDA","region_id":"DP03487r019","statement":[{"text":"Structural and Functional Analysis of a Novel Interaction Motif within UFM1-activating Enzyme 5 (UBA5) Required for Binding to Ubiquitin-like Proteins and Ufmylation.","type":"Title"},{"text":"Formation of UFM1 conjugates depends on intact LIR/UFIM within UBA5.","type":"Figure"},{"text":"Finally, we tested whether conjugation of UFM1 to target proteins in the cell depended on the intact LIR/UFIM in UBA5. We made use of the cellular ufmylation assay in which FLAG-tagged wild-type and LIR/UFIM mutant forms of UBA5 are co-expressed with the C-terminal glycine-exposed form of FLAG-UFM1 as well as Myc-UFL1 and Myc-UFBP1 (the latter serves as a substrate for ufmylation) in HEK293 cells in which UBA5 was deleted by CRISPR/Cas9 technology (4). UFBP1 is an E3 adaptor protein, dependent on its Lys-267 ufmylation (3); therefore, we used wild-type UFBP1 and its K267R mutant form as a negative control in this experiment. Upon overexpression of wild-type FLAG-UBA5, or the W341A and G342A single mutants, we observed increased formation of ufmylated UFBP1 species (UFBP1-UFM1, Fig. 5B) and the uncharacterized UFM1-protein conjugates (X-UFM1), for which ufmylation in turn depends on ufmylated UFBP1 (Fig. 5B).","type":"Results"},{"text":"We thus concluded that the intact LIR/UFIM is the prerequisite for the full biological activity of UBA5 toward activation and transfer of UFM1 to downstream substrates both in vitro and in cells.","type":"Results"},{"text":"The region includes the non-canonical LIR motif \"WGIELV\".","type":"Curator statement"}],"term_comment":"","term_def":"\"Covalent attachment of the ubiquitin-like protein UFM1 to another protein.\" [GOC:vw, PMID:20018847]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:40:31.830Z"}}],"regions_counter":19,"released":"2021_12","sequence":"MAESVERLQQRVQELERELAQERSLQVPRSGDGGGGRVRIEKMSSEVVDSNPYSRLMALKRMGIVSDYEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTVENFQHFMDRISNGGLEEGKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSENAVSGHIQLIIPGESACFACAPPLVVAANIDEKTLKREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTVSFYLGYNAMQDFFPTMSMKPNPQCDDRNCRKQQEEYKKKVAALPKQEVIQEEEEIIHEDNEWGIELVSEVSEEELKNFSGPVPDLPEGITVAYTIPKKQEDSVTELTVEDSGESLEDLMAKMKNM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref50":"UniRef50_Q9GZZ9","uniref90":"UniRef90_Q9GZZ9","uniref100":"UniRef100_Q9GZZ9","dataset":["Autophagy-related proteins","NDDs-related proteins"],"genes":[{"name":{"value":"UBA5","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15071506","url":"http://www.ncbi.nlm.nih.gov/pubmed/15071506","alternativeUrl":"https://europepmc.org/abstract/MED/15071506"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:23230","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:23230"}}]},"synonyms":[{"value":"UBE1DC1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16328888","url":"http://www.ncbi.nlm.nih.gov/pubmed/16328888","alternativeUrl":"https://europepmc.org/abstract/MED/16328888"}}]}]}],"alphafold_very_low_content":0.04702970297029703,"disorder_content":0.19801980198019803,"disprot_consensus":{"full":[{"start":325,"end":383,"type":"D"},{"start":384,"end":404,"type":"T"}],"Structural state":[{"start":325,"end":404,"type":"D"}],"Structural transition":[{"start":384,"end":404,"type":"T"}],"Molecular function":[{"start":325,"end":404,"type":"F"}],"Biological process":[{"start":333,"end":348,"type":"F"}]}},{"disprot_id":"DP03488","acc":"P43026","creator":"vacs","date":"2021-09-12T12:11:27.072Z","features":{"pfam":[{"id":"PF00019","name":"Transforming growth factor beta like domain","start":399,"end":500},{"id":"PF00688","name":"TGF-beta propeptide","start":166,"end":329}],"gene3D":[]},"length":501,"name":"Growth/differentiation factor 5","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":382,"end":396,"reference_id":"15752764","reference_source":"pmid","reference_html":"Crystal structure of recombinant human growth and differentiation factor 5: evidence for interaction of the type I and type II receptor-binding sites. <i> Schreuder H, Liesum A, Pohl J, Kruse M, Koyama M. </i> Biochem Biophys Res Commun, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"2BHK"}],"region_id":"DP03488r001","statement":[{"text":"The N-terminal residues 1–14 are not visible in the electron density maps, most likely because they are disordered in the solvent.","type":"Results"},{"text":"Region 1-15 is disordered in the crystal, which corresponds to region 382-396 of the amino acid sequence, since the natural precursor form contains a signal peptide (1-27) and a propeptide (28-381).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-14T13:56:08.363Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_12","sequence":"MRLPKLLTFLLWYLAWLDLEFICTVLGAPDLGQRPQGTRPGLAKAEAKERPPLARNVFRPGGHSYGGGATNANARAKGGTGQTGGLTQPKKDEPKKLPPRPGGPEPKPGHPPQTRQATARTVTPKGQLPGGKAPPKAGSVPSSFLLKKAREPGPPREPKEPFRPPPITPHEYMLSLYRTLSDADRKGGNSSVKLEAGLANTITSFIDKGQDDRGPVVRKQRYVFDISALEKDGLLGAELRILRKKPSDTAKPAAPGGGRAAQLKLSSCPSGRQPAALLDVRSVPGLDGSGWEVFDIWKLFRNFKNSAQLCLELEAWERGRAVDLRGLGFDRAARQVHEKALFLVFGRTKKRDLFFNEIKARSGQDDKTVYEYLFSQRRKRRAPLATRQGKRPSKNLKARCSRKALHVNFKDMGWDDWIIAPLEYEAFHCEGLCEFPLRSHLEPTNHAVIQTLMNSMDPESTPPTCCVPTRLSPISILFIDSANNVVYKQYEDMVVESCGCR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref50":"UniRef50_P43026","uniref90":"UniRef90_P43026","uniref100":"UniRef100_P43026","genes":[{"name":{"value":"GDF5"},"synonyms":[{"value":"BMP14"},{"value":"CDMP1"}]}],"alphafold_very_low_content":0.29740518962075846,"disorder_content":0.029940119760479042,"disprot_consensus":{"full":[{"start":382,"end":396,"type":"D"}],"Structural state":[{"start":382,"end":396,"type":"D"}]}},{"disprot_id":"DP03489","acc":"P0DSM4","creator":"jglavina","date":"2021-09-13T19:27:22.898Z","features":{"pfam":[{"id":"PF08024","name":"Ant antimicrobial peptide","start":2,"end":24}],"gene3D":[]},"length":25,"name":"U1-poneritoxin-Na1b","ncbi_taxon_id":2320211,"organism":"Neoponera apicalis","regions":[{"start":1,"end":25,"reference_id":"34302796","reference_source":"pmid","reference_html":"Multipurpose peptides: The venoms of Amazonian stinging ants contain anthelmintic ponericins with diverse predatory and defensive activities. <i> Nixon SA, Robinson SD, Agwa AJ, Walker AA, Choudhary S, Touchard A, Undheim EAB, Robertson A, Vetter I, Schroeder CI, Kotze AC, Herzig V, King GF. </i> Biochem Pharmacol, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"jglavina","curator_name":"Juliana Glavina","curator_orcid":"0000-0001-6336-1290","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03489r001","statement":[{"text":"Circular dichroism spectropolarimetry indicated that the ponericins are unstructured in aqueous solution but adopt α -helical conformations in lipid mimetic environments.","type":"Abstract"},{"text":"CD spectra of the peptides in aqueous solution were typical of disordered protein chains, with a deep spectral minimum below 200 nm. Addition of 20% TFE or 20 mM SDS induced a radical change in the CD spectrum, with minima at 207 and 222 nm and a maximum at 193 nm, features that are characteristic of α-helical sec­ondary structure [38] (Fig. 7A–C).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-21T07:31:28.920Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_12","sequence":"FLGALLKIGAKLLPSVVGLFKKKQQ","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Hymenoptera","Apocrita","Aculeata","Formicoidea","Formicidae","Ponerinae","Ponerini","Neoponera"],"uniref50":"UniRef50_P82423","uniref90":"UniRef90_P0DSM4","uniref100":"UniRef100_P0DSM4","genes":[],"alphafold_very_low_content":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":25,"type":"D"}],"Structural state":[{"start":1,"end":25,"type":"D"}]}},{"disprot_id":"DP03490","acc":"P18075","creator":"vacs","date":"2021-09-14T15:32:41.832Z","features":{"pfam":[{"id":"PF00019","name":"Transforming growth factor beta like domain","start":330,"end":430},{"id":"PF00688","name":"TGF-beta propeptide","start":35,"end":280}],"gene3D":[]},"length":431,"name":"Bone morphogenetic protein 7","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":293,"end":327,"reference_id":"12667445","reference_source":"pmid","reference_html":"The BMP7/ActRII extracellular domain complex provides new insights into the cooperative nature of receptor assembly. <i> Greenwald J, Groppe J, Gray P, Wiater E, Kwiatkowski W, Vale W, Choe S. </i> Mol Cell, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"1LX5"},{"db":"PDB","id":"1LXI"}],"region_id":"DP03490r001","statement":[{"text":"The structural model includes residues 6–100 of ActRII-ECD (out of 1–102) and residues 36–139 of BMP7 (out of 1–139). The N-terminal 35 amino acids of BMP7 remain disordered, as in the unbound ligand (Griffith et al. 1996).","type":"Results"},{"text":"Region 1-35 corresponds to region 293-327 of the amino acid sequence, since the natural precursor form contains a signal peptide (1-29) and a propeptide (30-292).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-20T08:58:33.160Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MHVRSLRAAAPHSFVALWAPLFLLRSALADFSLDNEVHSSFIHRRLRSQERREMQREILSILGLPHRPRPHLQGKHNSAPMFMLDLYNAMAVEEGGGPGGQGFSYPYKAVFSTQGPPLASLQDSHFLTDADMVMSFVNLVEHDKEFFHPRYHHREFRFDLSKIPEGEAVTAAEFRIYKDYIRERFDNETFRISVYQVLQEHLGRESDLFLLDSRTLWASEEGWLVFDITATSNHWVVNPRHNLGLQLSVETLDGQSINPKLAGLIGRHGPQNKQPFMVAFFKATEVHFRSIRSTGSKQRSQNRSKTPKNQEALRMANVAENSSSDQRQACKKHELYVSFRDLGWQDWIIAPEGYAAYYCEGECAFPLNSYMNATNHAIVQTLVHFINPETVPKPCCAPTQLNAISVLYFDDSSNVILKKYRNMVVRACGCH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref50":"UniRef50_P18075","uniref90":"UniRef90_P18075","uniref100":"UniRef100_P18075","genes":[{"name":{"value":"BMP7"},"synonyms":[{"value":"OP1"}]}],"alphafold_very_low_content":0.22041763341067286,"disorder_content":0.08120649651972157,"disprot_consensus":{"full":[{"start":293,"end":327,"type":"D"}],"Structural state":[{"start":293,"end":327,"type":"D"}]}},{"disprot_id":"DP03492","acc":"Q8R426-2","creator":"vnugnes","date":"2021-09-15T13:11:34.500Z","features":{"pfam":[],"gene3D":[]},"length":216,"name":"Isoform 2 of Kv channel-interacting protein 1","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions":[{"start":160,"end":170,"reference_id":"14980206","reference_source":"pmid","reference_html":"Structural insights into the functional interaction of KChIP1 with Shal-type K(+) channels. <i> Zhou W, Qian Y, Kunjilwar K, Pfaffinger PJ, Choe S. </i> Neuron, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03492r001","statement":[{"text":"In  the  final  model,  there  are  two  regions  that  lack sufficient electron density: residues 160–170 of KChIP1 and 21–30 of Kv4.2, likely due to the high conformational flexibility of these regions.","type":"Results"},{"text":"Dots represent residues 160–170  of  KChIP1*  that  lack  electron  density.","type":"Figure"}],"cross_refs":[{"db":"PDB","id":"1S6C"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-15T13:41:09.795Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MGAVMGTFSSLQTKQRRPSKDKIEDDLEMTMVCHRPEGLEQLEAQTNFTKRELQVLYRGFKNECPSGVVNEETFKQIYAQFFPHGDASTYAHYLFNAFDTTQTGSVKFEDFVTALSILLRGTVHEKLRWTFNLYDINKDGYINKEEMMDIVKAIYDMMGKYTYPVLKEDTPRQHVDVFFQKMDKNKDGIVTLDEFLESCQEDDNIMRSLQLFQNVM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref50":"","uniref90":"","uniref100":"","genes":[{"name":{"value":"Kcnip1"},"synonyms":[{"value":"Kchip1"}]}],"disorder_content":0.05092592592592592,"disprot_consensus":{"full":[{"start":160,"end":170,"type":"D"}],"Structural state":[{"start":160,"end":170,"type":"D"}]}},{"disprot_id":"DP03494","acc":"Q04087","creator":"vnugnes","date":"2021-09-16T13:42:46.139Z","features":{"pfam":[{"id":"PF10422","name":"Monopolin complex subunit LRS4","start":5,"end":232}],"gene3D":[]},"length":347,"name":"Monopolin complex subunit LRS4","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":45,"end":102,"reference_id":"20723757","reference_source":"pmid","reference_html":"The monopolin complex crosslinks kinetochore components to regulate chromosome-microtubule attachments. <i> Corbett KD, Yip CK, Ee LS, Walz T, Amon A, Harrison SC. </i> Cell, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"3N7N"}],"region_id":"DP03494r001","statement":[{"text":"From sequence conservation and secondary structure predictions, it appeared that the density probably represented two N-terminal segments of Lrs4, with the remainder of the protein (approximately residues 34-102) disordered in our crystals.","type":"Results"},{"text":"This complex also forms crystals isomorphous to those of the complex with Lrs4 1-102 (data not shown), supporting the inference that Lrs4 residues 34-102 are disordered in the latter crystals and hence do not contribute to the diffraction intensities.","type":"Results"},{"text":"While Lrs4 residues 34-102 were present in the complex as crystallized, they were disordered in the electron density maps.","type":"Results"},{"text":"The region spanning 34-102 corresponds to 45-102 in UniProt.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-16T14:27:51.967Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":45,"end":102,"reference_id":"20723757","reference_source":"pmid","reference_html":"The monopolin complex crosslinks kinetochore components to regulate chromosome-microtubule attachments. <i> Corbett KD, Yip CK, Ee LS, Walz T, Amon A, Harrison SC. </i> Cell, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03494r002","statement":[{"text":"Second, the bulk of the two Lrs4 subunits is either largely disordered in solution or flexibly linked to the rest of the complex. This conclusion is consistent with our observation that residues ∼34-102 were disordered in the crystal structure of Csm1/Lrs4 1-102.","type":"Results"},{"text":"The region spanning 34-102 corresponds to 45-102 in UniProt.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-16T14:27:50.684Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2023_12","sequence":"MTTLLQLLSNYYKAKLDSERIYNEYVQSQYEFASLDKLNNNKGDPKKVVDETLFLQRQIAQLNKQLQLSFQENEKLLSVQKNQKALYQSKLSSKDAFIDDLKLKLKVEQISVDKHNKERTPSTGRDEQQRNSKAAHTSKPTIHLLSPIVNRDKPNNQTNDRGGNDPDSPTSQRRSRGLRSLLSSGKNTIFDSISKNLDDEINENAHIRNDTTSSKIAGKSPSRLSALQKSPELRKERNNMILKEHILRSKDDQNITSSRKLDNIELSSIGDSTAMTSRSSTVNANDILGNEENDGITKLKRVNKLTSSPVKRDCSTNKKRKLTKQRIATLPNSDEELSNNLNVDEFV","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref50":"UniRef50_Q04087","uniref90":"UniRef90_Q04087","uniref100":"UniRef100_Q04087","genes":[{"name":{"value":"LRS4"},"orfNames":[{"value":"D9461.25"}],"olnNames":[{"value":"YDR439W"}]}],"alphafold_very_low_content":0.40057636887608067,"disorder_content":0.16714697406340057,"disprot_consensus":{"full":[{"start":45,"end":102,"type":"D"}],"Structural state":[{"start":45,"end":102,"type":"D"}]}},{"disprot_id":"DP03495","acc":"P63883","creator":"vnugnes","date":"2021-09-17T12:01:34.130Z","features":{"pfam":[{"id":"PF01520","name":"N-acetylmuramoyl-L-alanine amidase","start":190,"end":404},{"id":"PF11741","name":"AMIN domain","start":38,"end":142}],"gene3D":[]},"length":417,"name":"N-acetylmuramoyl-L-alanine amidase AmiC","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":163,"end":174,"reference_id":"23927005","reference_source":"pmid","reference_html":"The crystal structure of the cell division amidase AmiC reveals the fold of the AMIN domain, a new peptidoglycan binding domain. <i> Rocaboy M, Herman R, Sauvage E, Remaut H, Moonens K, Terrak M, Charlier P, Kerff F. </i> Mol Microbiol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"4BIN"}],"region_id":"DP03495r001","statement":[{"text":"The final electron density map shows a clear density for the whole protein except for five disordered segments consisting of the first fifteen residues of the N-terminal purification tag, Asn146-Asp152, Lys163-Gln174, Lys310-Phe321 and the last nine residues at the C-terminus.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-20T09:08:40.106Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":310,"end":321,"reference_id":"23927005","reference_source":"pmid","reference_html":"The crystal structure of the cell division amidase AmiC reveals the fold of the AMIN domain, a new peptidoglycan binding domain. <i> Rocaboy M, Herman R, Sauvage E, Remaut H, Moonens K, Terrak M, Charlier P, Kerff F. </i> Mol Microbiol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"4BIN"}],"region_id":"DP03495r002","statement":[{"text":"The final electron density map shows a clear density for the whole protein except for five disordered segments consisting of the first fifteen residues of the N-terminal purification tag, Asn146-Asp152, Lys163-Gln174, Lys310-Phe321 and the last nine residues at the C-terminus.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-20T09:08:43.701Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2023_12","sequence":"MSGSNTAISRRRLLQGAGAMWLLSVSQVSLAAVSQVVAVRVWPASSYTRVTVESNRQLKYKQFALSNPERVVVDIEDVNLNSVLKGMAAQIRADDPFIKSARVGQFDPQTVRMVFELKQNVKPQLFALAPVAGFKERLVMDLYPANAQDMQDPLLALLEDYNKGDLEKQVPPAQSGPQPGKAGRDRPIVIMLDPGHGGEDSGAVGKYKTREKDVVLQIARRLRSLIEKEGNMKVYMTRNEDIFIPLQVRVAKAQKQRADLFVSIHADAFTSRQPSGSSVFALSTKGATSTAAKYLAQTQNASDLIGGVSKSGDRYVDHTMFDMVQSLTIADSLKFGKAVLNKLGKINKLHKNQVEQAGFAVLKAPDIPSILVETAFISNVEEERKLKTATFQQEVAESILAGIKAYFADGATLARRG","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref50":"UniRef50_P63884","uniref90":"UniRef90_P63884","uniref100":"UniRef100_P63884","genes":[{"name":{"value":"amiC"},"synonyms":[{"value":"ygdN"}],"olnNames":[{"value":"b2817"},{"value":"JW5449"}]}],"alphafold_very_low_content":0.045563549160671464,"disorder_content":0.05755395683453238,"disprot_consensus":{"full":[{"start":163,"end":174,"type":"D"},{"start":310,"end":321,"type":"D"}],"Structural state":[{"start":163,"end":174,"type":"D"},{"start":310,"end":321,"type":"D"}]}},{"disprot_id":"DP03496","acc":"P22515","creator":"vnugnes","date":"2021-09-17T12:41:37.630Z","features":{"pfam":[{"id":"PF00899","name":"ThiF family","start":417,"end":605},{"id":"PF00899","name":"ThiF family","start":857,"end":911},{"id":"PF09358","name":"Ubiquitin fold domain","start":928,"end":1020},{"id":"PF10585","name":"Ubiquitin-activating enzyme, SCCH domain","start":606,"end":856},{"id":"PF16190","name":"Ubiquitin-activating enzyme E1 FCCH domain","start":191,"end":259},{"id":"PF16191","name":"Ubiquitin-activating enzyme E1 four-helix bundle","start":260,"end":329}],"gene3D":[]},"length":1024,"name":"Ubiquitin-activating enzyme E1 1","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":774,"end":796,"reference_id":"33888705","reference_source":"pmid","reference_html":"Crystal structures of an E1-E2-ubiquitin thioester mimetic reveal molecular mechanisms of transthioesterification. <i> Yuan L, Lv Z, Adams MJ, Olsen SK. </i> Nat Commun, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"7K5J"}],"region_id":"DP03496r001","statement":[{"text":"Based on Supplementary Table 2 there is a disordered region between residues 774-796.\n","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-20T09:11:08.353Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MSSNNSGLSAAGEIDESLYSRQLYVLGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVKSMTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVTRAKLAELNAYVPVNVLDSLDDVTQLSQFQVVVATDTVSLEDKVKINEFCHSSGIRFISSETRGLFGNTFVDLGDEFTVLDPTGEEPRTGMVSDIEPDGTVTMLDDNRHGLEDGNFVRFSEVEGLDKLNDGTLFKVEVLGPFAFRIGSVKEYGEYKKGGIFTEVKVPRKISFKSLKQQLSNPEFVFSDFAKFDRAAQLHLGFQALHQFAVRHNGELPRTMNDEDANELIKLVTDLSVQQPEVLGEGVDVNEDLIKELSYQARGDIPGVVAFFGGLVAQEVLKACSGKFTPLKQFMYFDSLESLPDPKNFPRNEKTTQPVNSRYDNQIAVFGLDFQKKIANSKVFLVGSGAIGCEMLKNWALLGLGSGSDGYIVVTDNDSIEKSNLNRQFLFRPKDVGKNKSEVAAEAVCAMNPDLKGKINAKIDKVGPETEEIFNDSFWESLDFVTNALDNVDARTYVDRRCVFYRKPLLESGTLGTKGNTQVIIPRLTESYSSSRDPPEKSIPLCTLRSFPNKIDHTIAWAKSLFQGYFTDSAENVNMYLTQPNFVEQTLKQSGDVKGVLESISDSLSSKPHNFEDCIKWARLEFEKKFNHDIKQLLFNFPKDAKTSNGEPFWSGAKRAPTPLEFDIYNNDHFHFVVAGASLRAYNYGIKSDDSNSKPNVDEYKSVIDHMIIPEFTPNANLKIQVNDDDPDPNANAANGSDEIDQLVSSLPDPSTLAGFKLEPVDFEKDDDTNHHIEFITACSNCRAQNYFIETADRQKTKFIAGRIIPAIATTTSLVTGLVNLELYKLIDNKTDIEQYKNGFVNLALPFFGFSEPIASPKGEYNNKKYDKIWDRFDIKGDIKLSDLIEHFEKDEGLEITMLSYGVSLLYASFFPPKKLKERLNLPITQLVKLVTKKDIPAHVSTMILEICADDKEGEDVEVPFITIHL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref50":"UniRef50_P22515","uniref90":"UniRef90_P22515","uniref100":"UniRef100_P22515","genes":[{"name":{"value":"UBA1"},"olnNames":[{"value":"YKL210W"}]}],"alphafold_very_low_content":0.0107421875,"disorder_content":0.0224609375,"disprot_consensus":{"full":[{"start":774,"end":796,"type":"D"}],"Structural state":[{"start":774,"end":796,"type":"D"}]}},{"disprot_id":"DP03497","acc":"P27361","creator":"vacs","date":"2021-09-18T11:47:49.812Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":42,"end":330}],"gene3D":[]},"length":379,"name":"Mitogen-activated protein kinase 3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":23,"reference_id":"18983981","reference_source":"pmid","reference_html":"Crystal structure of human mono-phosphorylated ERK1 at Tyr204. <i> Kinoshita T, Yoshida I, Nakae S, Okita K, Gouda M, Matsubara M, Yokota K, Ishiguro H, Tada T. </i> Biochem Biophys Res Commun, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2ZOQ"}],"region_id":"DP03497r001","statement":[{"text":"Invisible amino acids in the N- and C-terminal in the refined ERK1 model are shown by gray dot lines.","type":"Figure"},{"text":"The first 23 amino acids are missing in all chains and are presumably disordered.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-20T09:05:26.231Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MAAAAAQGGGGGEPRRTEGVGPGVPGEVEMVKGQPFDVGPRYTQLQYIGEGAYGMVSSAYDHVRKTRVAIKKISPFEHQTYCQRTLREIQILLRFRHENVIGIRDILRASTLEAMRDVYIVQDLMETDLYKLLKSQQLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLINTTCDLKICDFGLARIADPEHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINMKARNYLQSLPSKTKVAWAKLFPKSDSKALDLLDRMLTFNPNKRITVEEALAHPYLEQYYDPTDEPVAEEPFTFAMELDDLPKERLKELIFQETARFQPGVLEAP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref50":"UniRef50_P28482","uniref90":"UniRef90_P27361","uniref100":"UniRef100_P27361","dataset":["Autophagy-related proteins","NDDs-related proteins"],"genes":[{"name":{"value":"MAPK3"},"synonyms":[{"value":"ERK1"},{"value":"PRKM3"}]}],"alphafold_very_low_content":0.079155672823219,"disorder_content":0.06068601583113457,"disprot_consensus":{"full":[{"start":1,"end":23,"type":"D"}],"Structural state":[{"start":1,"end":23,"type":"D"}]}},{"disprot_id":"DP03498","acc":"P06491","creator":"vnugnes","date":"2021-09-20T08:15:09.699Z","features":{"pfam":[{"id":"PF03122","name":"Herpes virus major capsid protein","start":17,"end":1371}],"gene3D":[]},"length":1374,"name":"Major capsid protein","ncbi_taxon_id":10299,"organism":"Human herpesvirus 1 (strain 17)","regions":[{"start":451,"end":483,"reference_id":"12574112","reference_source":"pmid","reference_html":"Structure of the herpesvirus major capsid protein. <i> Bowman BR, Baker ML, Rixon FJ, Chiu W, Quiocho FA. </i> EMBO J, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"1NO7"}],"region_id":"DP03498r001","statement":[{"text":"In both molecules, the residues 451–483, 523–539, 922–924 and 1046–1054 were disordered.","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-21T14:42:56.090Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":523,"end":538,"reference_id":"12574112","reference_source":"pmid","reference_html":"Structure of the herpesvirus major capsid protein. <i> Bowman BR, Baker ML, Rixon FJ, Chiu W, Quiocho FA. </i> EMBO J, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"1NO7"}],"region_id":"DP03498r002","statement":[{"text":"In both molecules, the residues 451–483, 523–539, 922–924 and 1046–1054 were disordered.","type":"Methods"},{"text":"Boundaries of the disorder region for both molecules corresponds to 523-538.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-21T14:42:54.651Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MAAPNRDPPGYRYAAAMVPTGSLLSTIEVASHRRLFDFFSRVRSDANSLYDVEFDALLGSYCNTLSLVRFLELGLSVACVCTKFPELAYMNEGRVQFEVHQPLIARDGPHPIEQPTHNYMTKIIDRRALNAAFSLATEAIALLTGEALDGTGIGAHRQLRAIQQLARNVQAVLGAFERGTADQMLHVLLEKAPPLALLLPMQRYLDNGRLATRVARATLVAELKRSFCETSFFLGKAGHRREAVEAWLVDLTTATQPSVAVPRLTHADTRGRPVDGVLVTTAPIKQRLLQSFLKVEDTEADVPVTYGEMVLNGANLVTALVMGKAVRSLDDVGRHLLEMQEEQLDLNRQTLDELESAPQTTRVRADLVSIGEKLVFLEALEKRIYAATNVPYPLVGAMDLTFVLPLGLFNPVMERFAAHAGDLVPAPGHPDPRAFPPRQLFFWGKDRQVLRLSLEHAIGTVCHPSLMNVDAAVGGLNRDPVEAANPYGAYVAAPAGPAADMQQLFLNAWGQRLAHGRVRWVAEGQMTPEQFMQPDNANLALELHPAFDFFVGVADVELPGGDVPPAGPGEIQATWRVVNGNLPLALCPAAFRDARGLELGVGRHAMAPATIAAVRGAFDDRNYPAVFYLLQAAIHGSEHVFCALARLVVQCITSYWNNTRCAAFVNDYSLVSYVVTYLGGDLPEECMAVYRDLVAHVEALAQLVDDFTLTGPELGGQAQAELNHLMRDPALLPPLVWDCDALMRRAALDRHRDCRVSAGGHDPVYAAACNVATADFNRNDGQLLHNTQARAADAADDRPHRGADWTVHHKIYYYVMVPAFSRGRCCTAGVRFDRVYATLQNMVVPEIAPGEECPSDPVTDPAHPLHPANLVANTVNAMFHNGRVVVDGPAMLTLQVLAHNMAERTTALLCSAAPDAGANTASTTNMRIFDGALHAGILLMAPQHLDHTIQNGDYFYPLPVHALFAGADHVANAPNFPPALRDLSRQVPLVPPALGANYFSSIRQPVVQHVRESAAGENALTYALMAGYFKISPVALHHQLKTGLHPGFGFTVVRQDRFVTENVLFSERASEAYFLGQLQVARHETGGGVNFTLTQPRANVDLGVGYTAVVATATVRNPVTDMGNLPQNFYLGRGAPPLLDNAAAVYLRNAVVAGNRLGPAQPVPVFGCAQVPRRAGMDHGQDAVCEFIATPVSTDVNYFRRPCNPRGRAAGGVYAGDKEGDVTALMYDHGQSDPSRAFAATANPWASQRFSYGDLLYNGAYHLNGASPVLSPCFKFFTSADIAAKHRCLERLIVETGSAVSTATAASDVQFKRPPGCRELVEDPCGLFQEAYPLTCASDPALLRSARNGEAHARETHFAQYLVYDASPLKGLAL","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Peploviricota","Herviviricetes","Herpesvirales","Herpesviridae","Alphaherpesvirinae","Simplexvirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_P06491","uniref90":"UniRef90_P06491","uniref100":"UniRef100_P06491","genes":[{"name":{"value":"MCP","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04016","url":"https://hamap.expasy.org/unirule/MF_04016"}}]}}],"disorder_content":0.03566229985443959,"disprot_consensus":{"full":[{"start":451,"end":483,"type":"D"},{"start":523,"end":538,"type":"D"}],"Structural state":[{"start":451,"end":483,"type":"D"},{"start":523,"end":538,"type":"D"}]}},{"disprot_id":"DP03499","acc":"Q04637-8","creator":"vacs","date":"2021-09-22T20:37:37.888Z","features":{"pfam":[],"gene3D":[]},"length":1600,"name":"Isoform 8 of Eukaryotic translation initiation factor 4 gamma 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1428,"end":1437,"reference_id":"16698552","reference_source":"pmid","reference_html":"Two structurally atypical HEAT domains in the C-terminal portion of human eIF4G support binding to eIF4A and Mnk1. <i> Bellsolell L, Cho-Park PF, Poulin F, Sonenberg N, Burley SK. </i> Structure, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"1UG3"}],"region_id":"DP03499r001","statement":[{"text":"The C-terminal region of human eIF4GI consists of two a-helical domains, 4G/C1 and 4G/C2, joined by a 13 residue linker (Figures 1B and 2).","type":"Results"},{"text":"The linker connecting domains 4G/C1 and 4G/C2 is both highly polar and apparently flexible (10/13 residues were not visible in our electron density maps).","type":"Results"},{"text":"Ten residues in the interdomain linker of 4G/C (left) were not observed in the electron density maps and are shown as a polyalanine trace (violet).","type":"Figure"},{"text":"At the final stages of refinement, NCS operators were re-evaluated, and restrained NCS refinement yielded a final model (residues\n1234–1566, excluding 1428–1437 from the interdomain linker, rmsd = 0.2 A˚ for 323 a-carbon pairs) with an R factor of 24.4% and an R free of 29.2% (Table 1).","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-27T08:31:50.696Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1428,"end":1437,"reference_id":"16698552","reference_source":"pmid","reference_html":"Two structurally atypical HEAT domains in the C-terminal portion of human eIF4G support binding to eIF4A and Mnk1. <i> Bellsolell L, Cho-Park PF, Poulin F, Sonenberg N, Burley SK. </i> Structure, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"1UG3"}],"region_id":"DP03499r002","statement":[{"text":"The C-terminal region of human eIF4GI consists of two a-helical domains, 4G/C1 and 4G/C2, joined by a 13 residue linker (Figures 1B and 2).","type":"Results"},{"text":"The linker connecting domains 4G/C1 and 4G/C2 is both highly polar and apparently flexible (10/13 residues were not visible in our electron density maps).","type":"Results"},{"text":"Ten residues in the interdomain linker of 4G/C (left) were not observed in the electron density maps and are shown as a polyalanine trace (violet).","type":"Figure"},{"text":"At the final stages of refinement, NCS operators were re-evaluated, and restrained NCS refinement yielded a final model (residues\n1234–1566, excluding 1428–1437 from the interdomain linker, rmsd = 0.2 A˚ for 323 a-carbon pairs) with an R factor of 24.4% and an R free of 29.2% (Table 1).","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-27T08:31:53.273Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":1080,"end":1234,"reference_id":"16698552","reference_source":"pmid","reference_html":"Two structurally atypical HEAT domains in the C-terminal portion of human eIF4G support binding to eIF4A and Mnk1. <i> Bellsolell L, Cho-Park PF, Poulin F, Sonenberg N, Burley SK. </i> Structure, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03499r003","statement":[{"text":"Sequence comparisons (Figure 1A), secondary structure predictions (data not shown), and limited proteolysis combined with mass spectrometry (data not shown) permitted identification of a protease-resistant C-terminal portion of human eIF4GI that supports binding to eIF4A and Mnk1 (data not shown). Further truncation (eIF4GI[1235–1572]) yielded a two-domain protein that gives high-quality crystals with two protomers per asymmetric unit (Experimental Procedures).","type":"Results"},{"text":"Limited proteolysis of the C-terminal region of human eIF4GI (residues 1080–1600) with a panel of specific endoproteases yielded a resistant core of approximately 40 kDa, as judged by gel electrophoresis (data not shown). Matrix-assisted laser desorption ionization mass spectrometry and N-terminal sequencing of proteolytic fragments mapped a large number of proteolytic cleavage sites to residues 1080–1234.","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-27T07:28:05.784Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2021_12","sequence":"MNKAPQSTGPPPAPSPGLPQPAFPPGQTAPVVFSTPQATQMNTPSQPRQHFYPSRAQPPSSAASRVQSAAPARPGPAAHVYPAGSQVMMIPSQISYPASQGAYYIPGQGRSTYVVPTQQYPVQPGAPGFYPGASPTEFGTYAGAYYPAQGVQQFPTGVAPTPVLMNQPPQIAPKRERKTIRIRDPNQGGKDITEEIMSGARTASTPTPPQTGGGLEPQANGETPQVAVIVRPDDRSQGAIIADRPGLPGPEHSPSESQPSSPSPTPSPSPVLEPGSEPNLAVLSIPGDTMTTIQMSVEESTPISRETGEPYRLSPEPTPLAEPILEVEVTLSKPVPESEFSSSPLQAPTPLASHTVEIHEPNGMVPSEDLEPEVESSPELAPPPACPSESPVPIAPTAQPEELLNGAPSPPAVDLSPVSEPEEQAKEVTASMAPPTIPSATPATAPSATSPAQEEEMEEEEEEEEGEAGEAGEAESEKGGEELLPPESTPIPANLSQNLEAAAATQVAVSVPKRRRKIKELNKKEAVGDLLDAFKEANPAVPEVENQPPAGSNPGPESEGSGVPPRPEEADETWDSKEDKIHNAENIQPGEQKYEYKSDQWKPLNLEEKKRYDREFLLGFQFIFASMQKPEGLPHISDVVLDKANKTPLRPLDPTRLQGINCGPDFTPSFANLGRTTLSTRGPPRGGPGGELPRGPQAGLGPRRSQQGPRKEPRKIIATVLMTEDIKLNKAEKAWKPSSKRTAADKDRGEEDADGSKTQDLFRRVRSILNKLTPQMFQQLMKQVTQLAIDTEERLKGVIDLIFEKAISEPNFSVAYANMCRCLMALKVPTTEKPTVTVNFRKLLLNRCQKEFEKDKDDDEVFEKKQKEMDEAATAEERGRLKEELEEARDIARRRSLGNIKFIGELFKLKMLTEAIMHDCVVKLLKNHDEESLECLCRLLTTIGKDLDFEKAKPRMDQYFNQMEKIIKEKKTSSRIRFMLQDVLDLRGSNWVPRRGDQGPKTIDQIHKEAEMEEHREHIKVQQLMAKGSDKRRGGPPGPPISRGLPLVDDGGWNTVPISKGSRPIDTSRLTKITKPGSIDSNNQLFAPGGRLSWGKGSSGGSGAKPSDAASEAARPATSTLNRFSALQQAVPTESTDNRRVVQRSSLSRERGEKAGDRGDRLERSERGGDRGDRLDRARTPATKRSFSKEVEERSRERPSQPEGLRKAASLTEDRDRGRDAVKREAALPPVSPLKAALSEEELEKKSKAIIEEYLHLNDMKEAVQCVQELASPSLLFIFVRHGVESTLERSAIAREHMGQLLHQLLCAGHLSTAQYYQGLYEILELAEDMEIDIPHVWLYLAELVTPILQEGGVPMGELFREITKPLRPLGKAASLLLEILGLLCKSMGPKKVGTLWREAGLSWKEFLPEGQDIGAFVAEQKVEYTLGEESEAPGQRALPSEELNRQLEKLLKEGSSNQRVFDWIEANLSEQQIVSNTLVRALMTAVCYSAIIFETPLRVDVAVLKARAKLLQKYLCDEQKELQALYALQALVVTLEQPPNLLRMFFDALYDEDVVKEDAFYSWESSKDPAEQQGKGVALKSVTAFFKWLREAEEESDHN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref50":"","uniref90":"","uniref100":"","genes":[{"name":{"value":"EIF4G1"},"synonyms":[{"value":"EIF4F"},{"value":"EIF4G"},{"value":"EIF4GI"}]}],"disorder_content":0.103125,"disprot_consensus":{"full":[{"start":1080,"end":1234,"type":"D"},{"start":1428,"end":1437,"type":"D"}],"Structural state":[{"start":1080,"end":1234,"type":"D"},{"start":1428,"end":1437,"type":"D"}],"Disorder function":[{"start":1428,"end":1437,"type":"F"}]}},{"disprot_id":"DP03500","acc":"P0AFC7","creator":"tlazar","date":"2021-09-27T15:26:17.525Z","features":{"pfam":[{"id":"PF01058","name":"NADH ubiquinone oxidoreductase, 20 Kd subunit","start":63,"end":171}],"gene3D":[]},"length":220,"name":"NADH-quinone oxidoreductase subunit B","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":1,"end":42,"reference_id":"34308841","reference_source":"pmid","reference_html":"Structure of <i>Escherichia coli</i> respiratory complex I reconstituted into lipid nanodiscs reveals an uncoupled conformation. <i> Kolata P, Efremov RG. </i> Elife, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"7NYR"},{"db":"PDB","id":"7NYU"},{"db":"PDB","id":"7NYV"},{"db":"EMDB","id":"EMD-12653"},{"db":"EMDB","id":"EMD-12654"},{"db":"EMDB","id":"EMD-12655"}],"region_id":"DP03500r001","statement":[{"text":"Table 2. Residues built in the models. Subunit: nuoB; Built residues - Entire complex: 43–76, 86–179, 190–220","type":"Table"},{"text":"Residues 1-42 did not produce interpretable electron densities most probably due to protein disorder.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-29T07:18:51.263Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":180,"end":189,"reference_id":"34308841","reference_source":"pmid","reference_html":"Structure of <i>Escherichia coli</i> respiratory complex I reconstituted into lipid nanodiscs reveals an uncoupled conformation. <i> Kolata P, Efremov RG. </i> Elife, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"7NYR"},{"db":"PDB","id":"7NYU"},{"db":"PDB","id":"7NYV"},{"db":"EMDB","id":"EMD-12653"},{"db":"EMDB","id":"EMD-12654"},{"db":"EMDB","id":"EMD-12655"}],"region_id":"DP03500r002","statement":[{"text":"Table 2. Residues built in the models. Subunit: nuoB; Built residues - Entire complex: 43–76, 86–179, 190–220","type":"Table"},{"text":"Residues 180-189 did not produce interpretable electron densities most probably due to protein disorder.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-29T07:19:02.242Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MDYTLTRIDPNGENDRYPLQKQEIVTDPLEQEVNKNVFMGKLNDMVNWGRKNSIWPYNFGLSCCYVEMVTSFTAVHDVARFGAEVLRASPRQADLMVVAGTCFTKMAPVIQRLYDQMLEPKWVISMGACANSGGMYDIYSVVQGVDKFIPVDVYIPGCPPRPEAYMQALMLLQESIGKERRPLSWVVGDQGVYRANMQSERERKRGERIAVTNLRTPDEI","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref50":"UniRef50_Q8EI30","uniref90":"UniRef90_A1JLG4","uniref100":"UniRef100_A7ZPA1","genes":[{"name":{"value":"nuoB","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01356","url":"https://hamap.expasy.org/unirule/MF_01356"}}]},"olnNames":[{"value":"b2287"},{"value":"JW5875"}]}],"alphafold_very_low_content":0,"disorder_content":0.23636363636363636,"disprot_consensus":{"full":[{"start":1,"end":42,"type":"D"},{"start":180,"end":189,"type":"D"}],"Structural state":[{"start":1,"end":42,"type":"D"},{"start":180,"end":189,"type":"D"}]}},{"disprot_id":"DP03501","acc":"P0AFD1","creator":"tlazar","date":"2021-09-27T15:53:20.602Z","features":{"pfam":[{"id":"PF01257","name":"Thioredoxin-like [2Fe-2S] ferredoxin","start":22,"end":166}],"gene3D":[]},"length":166,"name":"NADH-quinone oxidoreductase subunit E","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":1,"end":10,"reference_id":"34308841","reference_source":"pmid","reference_html":"Structure of <i>Escherichia coli</i> respiratory complex I reconstituted into lipid nanodiscs reveals an uncoupled conformation. <i> Kolata P, Efremov RG. </i> Elife, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"7NYR"},{"db":"PDB","id":"7NYU"},{"db":"PDB","id":"7NYV"},{"db":"PDB","id":"7NZ1"},{"db":"EMDB","id":"EMD-12653"},{"db":"EMDB","id":"EMD-12654"},{"db":"EMDB","id":"EMD-12655"},{"db":"EMDB","id":"EMD-12661"}],"region_id":"DP03501r001","statement":[{"text":"Table 2. Residues built in the models. Subunit: nuoE; Built residues - Entire complex: 11–166","type":"Table"},{"text":"Residues 1-10 did not produce interpretable electron densities most probably due to protein disorder.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-29T07:21:14.939Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MHENQQPQTEAFELSAAEREAIEHEMHHYEDPRAASIEALKIVQKQRGWVPDGAIHAIADVLGIPASDVEGVATFYSQIFRQPVGRHVIRYCDSVVCHINGYQGIQAALEKKLNIKPGQTTFDGRFTLLPTCCLGNCDKGPNMMIDEDTHAHLTPEAIPELLERYK","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref50":"UniRef50_Q9I0J8","uniref90":"UniRef90_P0AFD2","uniref100":"UniRef100_P0AFD2","genes":[{"name":{"value":"nuoE"},"olnNames":[{"value":"b2285"},{"value":"JW2280"}]}],"alphafold_very_low_content":0.04819277108433735,"disorder_content":0.060240963855421686,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"}]}},{"disprot_id":"DP03502","acc":"P0AFD6","creator":"tlazar","date":"2021-09-27T16:09:14.756Z","features":{"pfam":[{"id":"PF12838","name":"4Fe-4S dicluster domain","start":59,"end":113}],"gene3D":[]},"length":180,"name":"NADH-quinone oxidoreductase subunit I","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":1,"end":22,"reference_id":"34308841","reference_source":"pmid","reference_html":"Structure of <i>Escherichia coli</i> respiratory complex I reconstituted into lipid nanodiscs reveals an uncoupled conformation. <i> Kolata P, Efremov RG. </i> Elife, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"7NYR"},{"db":"PDB","id":"7NYU"},{"db":"PDB","id":"7NYV"},{"db":"PDB","id":"7NZ1"},{"db":"EMDB","id":"EMD-12653"},{"db":"EMDB","id":"EMD-12654"},{"db":"EMDB","id":"EMD-12655"},{"db":"EMDB","id":"EMD-12661"}],"region_id":"DP03502r001","statement":[{"text":"Table 2. Residues built in the models. Subunit: nuoI; Built residues - Entire complex: 23–180","type":"Table"},{"text":"Residues 1-22 did not produce interpretable electron densities most probably due to protein disorder.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-29T07:22:57.850Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MTLKELLVGFGTQVRSIWMIGLHAFAKRETRMYPEEPVYLPPRYRGRIVLTRDPDGEERCVACNLCAVACPVGCISLQKAETKDGRWYPEFFRINFSRCIFCGLCEEACPTTAIQLTPDFEMGEYKRQDLVYEKEDLLISGPGKYPEYNFYRMAGMAIDGKDKGEAENEAKPIDVKSLLP","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref50":"UniRef50_Q8RQ74","uniref90":"UniRef90_P0AFD8","uniref100":"UniRef100_P0AFD8","genes":[{"name":{"value":"nuoI"},"olnNames":[{"value":"b2281"},{"value":"JW2276"}]}],"alphafold_very_low_content":0,"disorder_content":0.12222222222222222,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"}],"Structural state":[{"start":1,"end":22,"type":"D"}]}},{"disprot_id":"DP03503","acc":"P0AFE0","creator":"tlazar","date":"2021-09-27T16:18:57.820Z","features":{"pfam":[{"id":"PF00499","name":"NADH-ubiquinone/plastoquinone oxidoreductase chain 6","start":16,"end":157}],"gene3D":[]},"length":184,"name":"NADH-quinone oxidoreductase subunit J","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":165,"end":184,"reference_id":"34308841","reference_source":"pmid","reference_html":"Structure of <i>Escherichia coli</i> respiratory complex I reconstituted into lipid nanodiscs reveals an uncoupled conformation. <i> Kolata P, Efremov RG. </i> Elife, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"7NYR"},{"db":"PDB","id":"7NYU"},{"db":"PDB","id":"7NYV"},{"db":"PDB","id":"7NYH"},{"db":"EMDB","id":"EMD-12653"},{"db":"EMDB","id":"EMD-12654"},{"db":"EMDB","id":"EMD-12655"},{"db":"EMDB","id":"EMD-12652"}],"region_id":"DP03503r001","statement":[{"text":"Table 2. Residues built in the models. Subunit: NuoJ; Built residues - Entire complex: 1–164","type":"Table"},{"text":"Residues 165-184 did not produce interpretable electron densities most probably due to protein disorder.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-29T07:22:10.625Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MEFAFYICGLIAILATLRVITHTNPVHALLYLIISLLAISGVFFSLGAYFAGALEIIVYAGAIMVLFVFVVMMLNLGGSEIEQERQWLKPQVWIGPAILSAIMLVVIVYAILGVNDQGIDGTPISAKAVGITLFGPYVLAVELASMLLLAGLVVAFHVGREERAGEVLSNRKDDSAKRKTEEHA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref50":"UniRef50_P0AFE2","uniref90":"UniRef90_P0AFE2","uniref100":"UniRef100_P0AFE2","genes":[{"name":{"value":"nuoJ"},"olnNames":[{"value":"b2280"},{"value":"JW2275"}]}],"alphafold_very_low_content":0,"disorder_content":0.10869565217391304,"disprot_consensus":{"full":[{"start":165,"end":184,"type":"D"}],"Structural state":[{"start":165,"end":184,"type":"D"}]}},{"disprot_id":"DP03504","acc":"P0AFC3","creator":"tlazar","date":"2021-09-27T16:29:39.582Z","features":{"pfam":[{"id":"PF00507","name":"NADH-ubiquinone/plastoquinone oxidoreductase, chain 3","start":28,"end":125}],"gene3D":[]},"length":147,"name":"NADH-quinone oxidoreductase subunit A","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":1,"end":14,"reference_id":"34308841","reference_source":"pmid","reference_html":"Structure of <i>Escherichia coli</i> respiratory complex I reconstituted into lipid nanodiscs reveals an uncoupled conformation. <i> Kolata P, Efremov RG. </i> Elife, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"7NYR"},{"db":"PDB","id":"7NYU"},{"db":"PDB","id":"7NYV"},{"db":"PDB","id":"7NYH"},{"db":"EMDB","id":"EMD-12653"},{"db":"EMDB","id":"EMD-12654"},{"db":"EMDB","id":"EMD-12655"},{"db":"EMDB","id":"EMD-12652"}],"region_id":"DP03504r001","statement":[{"text":"Table 2. Residues built in the models. Subunit: NuoA; Built residues - Entire complex: 15–38, 60–127","type":"Table"},{"text":"Residues 1-14 did not produce interpretable electron densities most probably due to protein disorder.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-29T07:17:43.793Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":39,"end":59,"reference_id":"34308841","reference_source":"pmid","reference_html":"Structure of <i>Escherichia coli</i> respiratory complex I reconstituted into lipid nanodiscs reveals an uncoupled conformation. <i> Kolata P, Efremov RG. </i> Elife, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"7NYR"},{"db":"PDB","id":"7NYU"},{"db":"PDB","id":"7NYV"},{"db":"PDB","id":"7NYH"},{"db":"EMDB","id":"EMD-12653"},{"db":"EMDB","id":"EMD-12654"},{"db":"EMDB","id":"EMD-12655"},{"db":"EMDB","id":"EMD-12652"}],"region_id":"DP03504r002","statement":[{"text":"Table 2. Residues built in the models. Subunit: NuoA; Built residues - Entire complex: 15–38, 60–127","type":"Table"},{"text":"Residues 39-59 did not produce interpretable electron densities most probably due to protein disorder.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-29T07:17:41.663Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":128,"end":147,"reference_id":"34308841","reference_source":"pmid","reference_html":"Structure of <i>Escherichia coli</i> respiratory complex I reconstituted into lipid nanodiscs reveals an uncoupled conformation. <i> Kolata P, Efremov RG. </i> Elife, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"7NYR"},{"db":"PDB","id":"7NYU"},{"db":"PDB","id":"7NYV"},{"db":"PDB","id":"7NYH"},{"db":"EMDB","id":"EMD-12653"},{"db":"EMDB","id":"EMD-12654"},{"db":"EMDB","id":"EMD-12655"},{"db":"EMDB","id":"EMD-12652"}],"region_id":"DP03504r003","statement":[{"text":"Table 2. Residues built in the models. Subunit: NuoA; Built residues - Entire complex: 15–38, 60–127","type":"Table"},{"text":"Residues 128-147 did not produce interpretable electron densities most probably due to protein disorder.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-29T07:17:06.985Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2021_12","sequence":"MSMSTSTEVIAHHWAFAIFLIVAIGLCCLMLVGGWFLGGRARARSKNVPFESGIDSVGSARLRLSAKFYLVAMFFVIFDVEALYLFAWSTSIRESGWVGFVEAAIFIFVLLAGLVYLVRIGALDWTPARSRRERMNPETNSIANRQR","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"uniref50":"UniRef50_A6TBX4","uniref90":"UniRef90_A7ZPA2","uniref100":"UniRef100_A7ZPA2","genes":[{"name":{"value":"nuoA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01394","url":"https://hamap.expasy.org/unirule/MF_01394"}}]},"olnNames":[{"value":"b2288"},{"value":"JW2283"}]}],"alphafold_very_low_content":0,"disorder_content":0.3741496598639456,"disprot_consensus":{"full":[{"start":1,"end":14,"type":"D"},{"start":39,"end":59,"type":"D"},{"start":128,"end":147,"type":"D"}],"Structural state":[{"start":1,"end":14,"type":"D"},{"start":39,"end":59,"type":"D"},{"start":128,"end":147,"type":"D"}]}},{"acc":"Q77M43","sequence":"MATLLRSLALFKRNKDKPPITSGSGGAIRGIKHIIIVPIPGDSSITTRSRLLDRLVRLIGNPDVSGPKLTGALIGILSLFVESPGQLIQRITDDPDVSIRLLEVVQSDQSQSGLTFASRGTNMEDEADQYFSHDDPISSDQSRFGWFGNKEISDIEVQDPEGFNMILGTILAQIWVLLAKAVTAPDTAADSELRRWIKYTQQRRVVGEFRLERKWLDVVRNRIAEDLSLRRFMVALILDIKRTPGNKPRIAEMICDIDTYIVEAGLASFILTIKFGIETMYPALGLHEFAGELSTLESLMNLYQQMGETAPYMVILENSIQNKFSAGSYPLLWSYAMGVGVELENSMGGLNFGRSYFDPAYFRLGQEMVRRSAGKVSSTLASELGITAEDARLVSEIAMHTTEDKISRAVGPRQAQVSFLHGDQSENELPRLGGKEDRRVKQSRGEARESYRETGPSRASDARAAHLPTGTPLDIDTATESSQDPQDSRRSADALLRLQAMAGISEEQGSDTDTPIVYNDRNLLD","creator":"vnugnes","dataset":["Viral proteins","RNA-binding proteins"],"date":"2021-09-28T12:40:11.476Z","disprot_id":"DP03505","features":{"pfam":[{"id":"PF00973","name":"Paramyxovirus nucleocapsid protein","start":1,"end":399}],"gene3D":[]},"genes":[{"name":{"value":"N","evidences":[],"_id":"685af523b4ac24d5329d9786"},"synonyms":[{"value":"NP","evidences":[],"_id":"685af523b4ac24d5329d9787"}],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d9785"}],"length":525,"name":"Nucleoprotein","ncbi_taxon_id":132484,"organism":"Measles virus (strain Edmonston-Moraten vaccine)","regions_counter":16,"released":"2021_12","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Paramyxoviridae","Orthoparamyxovirinae","Morbillivirus"],"uniref100":"UniRef100_Q77M43","uniref50":"UniRef50_Q89933","uniref90":"UniRef90_Q89933","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":477,"end":505,"interaction_partner":[],"reference_html":"Structural basis for the attachment of a paramyxoviral polymerase to its template. <i> Kingston RL, Hamel DJ, Gay LS, Dahlquist FW, Matthews BW. </i> Proc Natl Acad Sci U S A, 2004","reference_id":"15159535","region_id":"DP03505r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In contrast, in the free state, the same NOEs were not observed, indicating that although not a statistical random coil (Fig. 4), the unbound N is very loosely structured.","_id":"685af523b4ac24d5329d9749"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T13:41:01.531Z","_id":"685af523b4ac24d5329d974a"},"version":1,"_id":"685af523b4ac24d5329d9748","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":486,"end":503,"interaction_partner":[],"reference_html":"Structural basis for the attachment of a paramyxoviral polymerase to its template. <i> Kingston RL, Hamel DJ, Gay LS, Dahlquist FW, Matthews BW. </i> Proc Natl Acad Sci U S A, 2004","reference_id":"15159535","region_id":"DP03505r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In contrast, residues 486–503 were strongly perturbed by binding and showed large downfield shifts in their Cα resonances, consistent with organization of this region into a helix in the bound state.","_id":"685af523b4ac24d5329d974c"},{"type":"Results","text":"Residues 477–484 appear likely to lack any persistent structure in both the free and bound states, whereas residues 486–503 are both perturbed and markedly rigidified on binding","_id":"685af523b4ac24d5329d974d"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T13:41:03.004Z","_id":"685af523b4ac24d5329d974e"},"version":1,"_id":"685af523b4ac24d5329d974b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1T6O","_id":"685af523b4ac24d5329d9754"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":486,"end":505,"interaction_partner":[{"db":"UniProt","id":"Q77M42","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9758"}],"reference_html":"Structural basis for the attachment of a paramyxoviral polymerase to its template. <i> Kingston RL, Hamel DJ, Gay LS, Dahlquist FW, Matthews BW. </i> Proc Natl Acad Sci U S A, 2004","reference_id":"15159535","region_id":"DP03505r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As expected the P–N complex resembles a four-helix bundle, with the helix contributed by N (helix Nα1) packed on the surface created by helices α2 and α3 of the binding domain from P.","_id":"685af523b4ac24d5329d9755"},{"type":"Results","text":"It is clear from consideration of both crystal packing and linker length that the complex observed in the crystal results from an intermolecular association with the N moiety from one protein binding to the P moiety of a separate molecule.","_id":"685af523b4ac24d5329d9756"},{"type":"Curator statement","text":"Crystallographic analysis of a chimeric protein in which amino acids 486–505 from N (N486–505) were fused to the carboxyl terminus of the nucleocapsid-binding domain of P (P457–507). The two binding elements were connected with a flexible linker, (GS)4, designed to be long enough to accommodate either parallel or antiparallel packing of the helix from N.","_id":"685af523b4ac24d5329d9757"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-29T08:04:33.358Z","_id":"685af523b4ac24d5329d9759"},"version":1,"_id":"685af523b4ac24d5329d9753","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":477,"end":505,"interaction_partner":[{"db":"UniProt","id":"Q77M42","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d975c"}],"reference_html":"Structural basis for the attachment of a paramyxoviral polymerase to its template. <i> Kingston RL, Hamel DJ, Gay LS, Dahlquist FW, Matthews BW. </i> Proc Natl Acad Sci U S A, 2004","reference_id":"15159535","region_id":"DP03505r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Typical association rates for protein–protein interactions are in the order of 105 to 106 M-1·s-1 (24), hence association of the measles P-binding domain with the measles N-tail peptide proceeds relatively quickly and is approaching the diffusion-controlled limit.","_id":"685af523b4ac24d5329d975b"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T13:55:02.554Z","_id":"685af523b4ac24d5329d975d"},"version":1,"_id":"685af523b4ac24d5329d975a","reference_source":"pmid"},{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2025-08-18T15:45:16.652Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005640","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","ec_ontology":"ECO","start":495,"end":505,"interaction_partner":[{"db":"UniProt","id":"Q77M42","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d9763"}],"reference_html":"Characterization of nucleocapsid binding by the measles virus and mumps virus phosphoproteins. <i> Kingston RL, Baase WA, Gay LS. </i> J Virol, 2004","reference_id":"15280472","region_id":"DP03505r007","released":"2025_12","statement":[{"type":"Results","text":"Deletions of 10 (MEN374-515) and 20 (MEN374-505) amino acids from the tail had no effect on the ability of the molecules to bind to P in a pulldown assay (Fig.1B). However, a third construct in which 30 amino acids were deleted (MEN374-495) lost the ability to bind the P protein (Fig. ​1B). This suggested that the region from 495 to 505 within the tail of N was critical for binding P.","_id":"685af523b4ac24d5329d9764"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":2,"_id":"685af523b4ac24d5329d9762","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005647","ec_name":"isothermal titration calorimetry evidence used in manual assertion","ec_ontology":"ECO","start":477,"end":505,"interaction_partner":[{"db":"UniProt","id":"Q77M42","partner_start":457,"partner_end":507,"_id":"685af523b4ac24d5329d976b"}],"reference_html":"Characterization of nucleocapsid binding by the measles virus and mumps virus phosphoproteins. <i> Kingston RL, Baase WA, Gay LS. </i> J Virol, 2004","reference_id":"15280472","region_id":"DP03505r009","released":"2022_03","sample":[],"statement":[{"type":"Discussion","text":"Additionally, we have shown that the binding of MEN477-505 to MEP457-507 occurs with low affinity and is entropically disfavored at both temperatures studied. ","_id":"685af523b4ac24d5329d976c"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-29T07:36:13.402Z","_id":"685af523b4ac24d5329d976d"},"version":1,"_id":"685af523b4ac24d5329d976a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":477,"end":505,"interaction_partner":[],"reference_html":"Structural basis for the attachment of a paramyxoviral polymerase to its template. <i> Kingston RL, Hamel DJ, Gay LS, Dahlquist FW, Matthews BW. </i> Proc Natl Acad Sci U S A, 2004","reference_id":"15159535","region_id":"DP03505r014","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Typical association rates for protein–protein interactions are in the order of 105 to 106 M-1·s-1 (24), hence association of the measles P-binding domain with the measles N-tail peptide proceeds relatively quickly and is approaching the diffusion-controlled limit.","_id":"685af523b4ac24d5329d977d"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-29T08:06:31.839Z","_id":"685af523b4ac24d5329d977e"},"version":1,"_id":"685af523b4ac24d5329d977c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1T6O","_id":"685af523b4ac24d5329d9780"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":486,"end":505,"interaction_partner":[],"reference_html":"Structural basis for the attachment of a paramyxoviral polymerase to its template. <i> Kingston RL, Hamel DJ, Gay LS, Dahlquist FW, Matthews BW. </i> Proc Natl Acad Sci U S A, 2004","reference_id":"15159535","region_id":"DP03505r015","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As expected the P–N complex resembles a four-helix bundle, with the helix contributed by N (helix Nα1) packed on the surface created by helices α2 and α3 of the binding domain from P.","_id":"685af523b4ac24d5329d9781"},{"type":"Results","text":"It is clear from consideration of both crystal packing and linker length that the complex observed in the crystal results from an intermolecular association with the N moiety from one protein binding to the P moiety of a separate molecule.","_id":"685af523b4ac24d5329d9782"},{"type":"Curator statement","text":"Crystallographic analysis of a chimeric protein in which amino acids 486–505 from N (N486–505) were fused to the carboxyl terminus of the nucleocapsid-binding domain of P (P457–507). The two binding elements were connected with a flexible linker, (GS)4, designed to be long enough to accommodate either parallel or antiparallel packing of the helix from N.","_id":"685af523b4ac24d5329d9783"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-29T08:06:30.129Z","_id":"685af523b4ac24d5329d9784"},"version":1,"_id":"685af523b4ac24d5329d977f","reference_source":"pmid"},{"start":400,"end":525,"reference_id":"12621042","reference_source":"pmid","reference_html":"The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein. <i> Longhi S, Receveur-Bréchot V, Karlin D, Johansson K, Darbon H, Bhella D, Yeo R, Finet S, Canard B. </i> J Biol Chem, 2003","date":"2025-08-18T15:52:58.623Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2025_12","version":0,"cross_refs":[{"db":"DisProt","id":"DP04423"}],"region_id":"DP03505r016","statement":[{"text":"IDR is 100% identical to the Measles virus (strain Edmonston B), UniProtKB:P0DXN6.","type":"Results"}]}],"__v":0,"disorder_content":0.24,"disprot_consensus":{"full":[{"start":400,"end":485,"type":"D"},{"start":486,"end":503,"type":"T"},{"start":504,"end":525,"type":"D"}],"Structural state":[{"start":400,"end":525,"type":"D"}],"Structural transition":[{"start":486,"end":503,"type":"T"}],"Molecular function":[{"start":477,"end":505,"type":"F"}]}},{"disprot_id":"DP03506","acc":"P33309","creator":"vacs","date":"2021-09-29T09:01:29.563Z","features":{"pfam":[{"id":"PF03464","name":"eRF1 domain 2","start":142,"end":274},{"id":"PF03465","name":"eRF1 domain 3","start":278,"end":376},{"id":"PF26356","name":"Pelota N-terminal domain","start":1,"end":134}],"gene3D":[]},"length":386,"name":"Protein DOM34","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":48,"end":59,"reference_id":"18180287","reference_source":"pmid","reference_html":"Structure of yeast Dom34: a protein related to translation termination factor Erf1 and involved in No-Go decay. <i> Graille M, Chaillet M, van Tilbeurgh H. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2VGM"},{"db":"PDB","id":"2VGN"}],"region_id":"DP03506r001","statement":[{"text":"In the final model, the following Dom34 regions Met1-Phe47, Thr60-Tyr170, and Asp180-Asp382 could be modeled in the electron density as well as 228 water molecules, one phosphate ion from the crystallization solution and two glycerol molecules, which was used as cryoprotectant (supplemental Fig. S1B).","type":"Methods"},{"text":"24 loop residues (Thr48-Ser59, Ser171-Thr179, and Asp383-Glu386) were absent in the final model due to the lack of electron density, reflecting intrinsic flexibility.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-29T12:36:57.425Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MKVISLKKDSFNKGGAVITLLPEDKEDLFTVYQIVDKDDELIFKKKFTSKLDEAGKKKSTDLVKLKIKVISEDFDMKDEYLKYKGVTVTDESGASNVDIPVGKYLSFTLDYVYPFTIIKQNFNKFMQKLLNEACNIEYKSDTAAVVLQEGIAHVCLVTSSSTILKQKIEYSMPKKKRTTDVLKFDEKTEKFYKAIYSAMKKDLNFDKLKTIILCSPGFYAKILMDKIFQYAEEEHNKKILDNKGMFFIAHCSTGYLQGINEVLKNPLYASKLQDTKYSKEIMVMDEFLLHLNKDDDKAWYGEKEVVKAAEYGAISYLLLTDKVLHSDNIAQREEYLKLMDSVESNGGKALVLSTLHSLGEELDQLTGIACILKYPLPDLDEDDGEE","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref50":"UniRef50_P33309","uniref90":"UniRef90_P33309","uniref100":"UniRef100_P33309","genes":[{"name":{"value":"DOM34"},"orfNames":[{"value":"N2016"}],"olnNames":[{"value":"YNL001W"}]}],"alphafold_very_low_content":0.018134715025906734,"disorder_content":0.031088082901554404,"disprot_consensus":{"full":[{"start":48,"end":59,"type":"D"}],"Structural state":[{"start":48,"end":59,"type":"D"}]}},{"disprot_id":"DP03507","acc":"Q9ERC1","creator":"fquaglia","date":"2021-10-01T15:35:02.289Z","features":{"pfam":[{"id":"PF00063","name":"Myosin head (motor domain)","start":404,"end":1132},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":68,"end":156},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":205,"end":282},{"id":"PF15439","name":"Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter","start":1222,"end":1592},{"id":"PF15452","name":"Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter","start":1712,"end":1845}],"gene3D":[]},"length":1912,"name":"Unconventional myosin-XVI","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions":[{"start":1146,"end":1912,"reference_id":"33930467","reference_source":"pmid","reference_html":"The C-terminal tail extension of myosin 16 acts as a molten globule, including intrinsically disordered regions, and interacts with the N-terminal ankyrin. <i> Telek E, Karádi K, Kardos J, Kengyel A, Fekete Z, Halász H, Nyitrai M, Bugyi B, Lukács A. </i> J Biol Chem, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03507r001","statement":[{"text":"In addition, the Myo16Tail possesses high structural flexibility and a solvent-exposed hydrophobic core, indicating the largely unstructured, intrinsically disordered nature of this protein region. Some secondary structure elements were also observed, indicating that the Myo16Tail likely adopts a molten globule-like structure.","type":"Abstract"},{"text":"The CD spectrum of Myo16Tail in the far-UV region revealed the minimum at 205 nm, the positive maximum at 190 nm, and a significant signal in a wide, 215 to 225 nm region (Fig. 9A). This suggests that the protein contains both α-helical and β-structured elements. On the other hand, the large minimum at 205 nm and the relatively weak positive maximum around 190 nm indicate the presence of a significant amount of disordered structure as well.","type":"Results"},{"text":"The thermal behavior of Myo16Tail showing low cooperativity detected by CD measurements supports the idea of lacking a stable globular fold and is characteristic of a molten globule–like state (90). In conclusion, CD spectroscopy analysis indicates the presence of both disordered and structured regions in Myo16Tail, supporting our conclusions from fluorescence spectroscopic measurements according to which the tail of Myo16 might be in a molten globule–like conformation.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-17T18:10:14.822Z"}},{"start":1146,"end":1912,"reference_id":"33930467","reference_source":"pmid","reference_html":"The C-terminal tail extension of myosin 16 acts as a molten globule, including intrinsically disordered regions, and interacts with the N-terminal ankyrin. <i> Telek E, Karádi K, Kardos J, Kengyel A, Fekete Z, Halász H, Nyitrai M, Bugyi B, Lukács A. </i> J Biol Chem, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03507r002","statement":[{"text":"In addition, the Myo16Tail possesses high structural flexibility and a solvent-exposed hydrophobic core, indicating the largely unstructured, intrinsically disordered nature of this protein region. Some secondary structure elements were also observed, indicating that the Myo16Tail likely adopts a molten globule-like structure.","type":"Abstract"},{"text":"The expression and purification results were analyzed and confirmed by SDS-PAGE and Anti-His Western blot (Fig. 4, B and C). We noted that Myo16Tail showed an anomalous electrophoretic migration (Fig. 4, B and C). The apparent molecular weight of Myo16Tail seemed to be ∼120 kDa in SDS-PAGE, which is higher than that calculated based on its amino acid sequence (86.47 kDa, ProtParam) (56). This abnormal electrophoretic mobility is a characteristic feature of IDPs, which could result from poor interaction with SDS molecules because of their irregular amino acid composition (28, 39).","type":"Results"},{"text":"The first experimental indication of the disordered structural characteristics of Myo16Tail is its anomalous migration showing higher apparent molecular mass as revealed by SDS-PAGE, which was confirmed by anti-His Western blot (Fig. 4, B and C). The unusual SDS-PAGE mobility as a characteristic feature of IDPs (28, 39) supports that Myo16Tail or parts of it are intrinsically disordered.","type":"Discussion"}],"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-17T18:07:55.043Z"}},{"start":1146,"end":1912,"reference_id":"33930467","reference_source":"pmid","reference_html":"The C-terminal tail extension of myosin 16 acts as a molten globule, including intrinsically disordered regions, and interacts with the N-terminal ankyrin. <i> Telek E, Karádi K, Kardos J, Kengyel A, Fekete Z, Halász H, Nyitrai M, Bugyi B, Lukács A. </i> J Biol Chem, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005632","ec_ontology":"ECO","ec_name":"fluorescence anisotropy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"interaction_partner":[{"db":"UniProt","id":"Q9ERC1","partner_start":1,"partner_end":403}],"region_id":"DP03507r003","statement":[{"text":"The C-terminal tail extension of myosin 16 acts as a molten globule, including intrinsically disordered regions, and interacts with the N-terminal ankyrin","type":"Title"},{"text":"Our results revealed that the Myo16Tail is functionally active and interacts with the N-terminal ankyrin domain of myosin 16, suggesting an intramolecular binding between the C and N termini of Myo16 as an autoregulatory mechanism involving backfolding of the motor domain.","type":"Abstract"},{"text":"The steady-state anisotropy of fluorescently labeled Alexa568–Myo16Ank (1.2 μM) increased by the addition of an increasing concentration of Myo16Tail as expected for binding interaction. The analysis revealed that the affinity (KD) of Myo16Tail to Myo16Ank is ∼2.5 μM according to Equation 1 (Fig. 5A).","type":"Results"},{"text":"Altogether, on the one hand, our results can confirm the functional activity of the recombinantly produced Myo16Tail and Myo16Tail (−IQ). On the other hand, our anisotropy findings revealed that the tail of Myo16 is dominant in the binding of Myo16Ank; however, the presence of Myo16IQ seems to influence the strength of this interaction. This moderate strength of the interaction of Myo16Tail is relatively common in regulatory functions and consistent with its possible role as a multiple interaction site for PI3K, WRC (17), and Myo16Ank.","type":"Results"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-17T18:19:35.165Z"}},{"start":1146,"end":1912,"reference_id":"33930467","reference_source":"pmid","reference_html":"The C-terminal tail extension of myosin 16 acts as a molten globule, including intrinsically disordered regions, and interacts with the N-terminal ankyrin. <i> Telek E, Karádi K, Kardos J, Kengyel A, Fekete Z, Halász H, Nyitrai M, Bugyi B, Lukács A. </i> J Biol Chem, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0005632","ec_ontology":"ECO","ec_name":"fluorescence anisotropy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03507r004","statement":[{"text":"The C-terminal tail extension of myosin 16 acts as a molten globule, including intrinsically disordered regions, and interacts with the N-terminal ankyrin","type":"Title"},{"text":"Our results revealed that the Myo16Tail is functionally active and interacts with the N-terminal ankyrin domain of myosin 16, suggesting an intramolecular binding between the C and N termini of Myo16 as an autoregulatory mechanism involving backfolding of the motor domain.","type":"Abstract"},{"text":"The steady-state anisotropy of fluorescently labeled Alexa568–Myo16Ank (1.2 μM) increased by the addition of an increasing concentration of Myo16Tail as expected for binding interaction. The analysis revealed that the affinity (KD) of Myo16Tail to Myo16Ank is ∼2.5 μM according to Equation 1 (Fig. 5A).","type":"Results"},{"text":"Altogether, on the one hand, our results can confirm the functional activity of the recombinantly produced Myo16Tail and Myo16Tail (−IQ). On the other hand, our anisotropy findings revealed that the tail of Myo16 is dominant in the binding of Myo16Ank; however, the presence of Myo16IQ seems to influence the strength of this interaction. This moderate strength of the interaction of Myo16Tail is relatively common in regulatory functions and consistent with its possible role as a multiple interaction site for PI3K, WRC (17), and Myo16Ank.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-17T18:19:31.677Z"}},{"start":1146,"end":1912,"reference_id":"33930467","reference_source":"pmid","reference_html":"The C-terminal tail extension of myosin 16 acts as a molten globule, including intrinsically disordered regions, and interacts with the N-terminal ankyrin. <i> Telek E, Karádi K, Kardos J, Kengyel A, Fekete Z, Halász H, Nyitrai M, Bugyi B, Lukács A. </i> J Biol Chem, 2021","date":"2023-07-17T18:28:12.602Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005632","ec_ontology":"ECO","ec_name":"fluorescence anisotropy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03507r006","statement":[{"text":"Importantly, the highest intensity and wavelength maximum of ANS fluorescence of Myo16Tail at low GuHCl (∼480 nm) is in accordance with the maximum values of G-actin in the range of 1 to 2 M GuHCl (∼480 nm), when the latter one is in molten globule conformation (Fig. 7C). Our ANS fluorescence results corroborate that Myo16Tail might have molten globule conformation under native conditions.","type":"Results"}]}],"regions_counter":6,"released":"2023_12","sequence":"MEIDQCLLESLPLGQRQRLVRRMRCEQIKAYYEREKVFQKQEGLLKRIKPGKSQKVRFGLADMIQDAIIHHHDKEVLQLLKEGADPHTLVSSGGSLLHLCARYDNVFIAEVLIDRGVNVNHQDEDFWAPMHIACACDNPDIVLLLILAGANVLLQDVNGNIPLDYAVEGTESSAILLAYLDENGVDLNSLRQIKLQRPLSMLTDVRHFLSSGGDVNEKNDDGVTLLHMACASGYKEVVLLLLEHGGDLNGMDDGYWTPLHLAAKYGQTTLVKLLLAHQANPHLVNCNGEKPSDIAASESIEEMLLKAEIAWEERMKESPSVPSLAQEELYEEILHDLPELSSKLSPLVLPIAKQDSLLEKDIMFKDTTKGLCNQESQDGPPETSMVSSSSKPEQVQLTPPAPSDDLATLSELNDSSLLYEIQKRFGNDQIHTFIGDIFLLVNPFKELPIYSTVVSQMYLSPTGQRSPSLPPHLFSCAERAFHRLFQERRPQNIILSGERGSGKTQASKQIMKHLTSRASSSCTMFDSRFKHAICILEAFGHAKTTLNNVSSCLIQYWELQFCQRRKHVTGARISTYMLEKPRLVAQPPGQGSFLIFSWLMDGLSAEEKCGLHLSNFCAHRYVSQGMREDVSTAERSLNKERLADLKHALNVIGFSALEVENLFAILSAILHIGDIQFTALTEADSAFVSDLQLLEQVADMLQVSTDELASALTTDIQYFKGDVIIRRHTTQIAAFYRDLLAKSLYSRLFGFLINTVNCCLQSQDEYKSLQTLDIGILDIFGFEEFQKNEFEQLCVNLTNEKMHHYIQEVLFLQEQTECVQEGVAMETACSPGNQAGVLDFFFQKPSGFFSLLDEESQAIWSVEPNLPRKLQGLLESSNTNAVYSPMKDGNGNVAFKGQGAAFTVMHYAGRVTYEIRGAVERNKDSLSQNLLFVMKTSENVVISHLFQSKLSPTGSLISSYPSFKFGGHKSSLLSKRIASSMVGVNKNYLELSKLLKKKGTCTFLQRLERGDPATTASQLTKSLADITAKLQKGSPHFILCVKPNTSQLPGVFDHFYVSAQLQYLGVLGLVRLFRYGYPVRPSFEDFLSRYEPLASVLLGEKKGQPAEERCRLVLQRCKLQGWQMGVHKVFLKYWQVDQLGDLWLQMQRKIVTCQKVIRGFLARQHLLQRMSIKQQEVTSIKSFLQSTEDMALKTYDALVIQNASDIAREHDRLRKEVHAAYHRNRQEEGTKRAEDQGGCRHAHSNSVPVPMAVDSLAQALAGPSSRSPSLHSVFSMDDSTGLPSPRKQPPPKPKRDPNTRLSASYEAVSACLSATKDAASEALTRPRPHSDDYSTMKKIPPRKPKRSPHTKLSGSYEEIWGPRPSGTMGQVGKHHAPGTLGVQWASPDSMPQCTPQLPLHLPLPQGDYDDDGEPVYIEMVGNAARAGGSETDSPDQGESVYEEMKYVLPEEGCGPGMLTFLPASPPLFLETRKAIILEAGEGSCQPLKDTCDIPPPFPNLLPHRPPLLVFPPTPVTCSPASDESPLTPLEVKKLPVLETNLKYPVQSEGSSPLSPQYSKAQKGENDQLTSPGFPVFNGPSRISPPATPPPPPGPPPAPCGPPSAPCGPPPAPCGPPPVPCGPPPAPCGPPPAPCGAAPAPCRPPTHFAFPPDSVLVTAAKALTNSDLPRTQPKPSSAPVLGPCSPFVKAPYSPGRTARADLRKASSTFSPPSPYSPPNSRPLSSPLDELASLFNSGRSVLRRSAVGRRIREAEGFETNMNLSSRDEPSSSEMASETQDRNANNHGTQLSSSLSSVVAAENGNPVTNGLAEDDGCSRLCLSGMGTSSFQRHRESHTTQVIHQLRLSENESVALQELLDWRRKLCESREGWQEAMQHPEPRAPPPPPCKKPTLLKKPEGGSCTRLSSQLWDSSI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"uniref50":"UniRef50_Q9ERC1","uniref90":"UniRef90_Q9ERC1","uniref100":"UniRef100_Q9ERC1","genes":[{"name":{"value":"Myo16","evidences":[{"code":"ECO:0000250","source":{"name":"UniProtKB","id":"Q9Y6X6","url":"https://www.uniprot.org/uniprot/Q9Y6X6"}}]},"synonyms":[{"value":"Myr8","evidences":[{"code":"ECO:0000312","source":{"name":"RGD","id":"621561","url":"https://rgd.mcw.edu/tools/genes/genes_view.cgi?id=621561"}}]},{"value":"Nyap3"}]}],"alphafold_very_low_content":0.4309623430962343,"disorder_content":0.40115062761506276,"disprot_consensus":{"full":[{"start":1146,"end":1912,"type":"D"}],"Structural state":[{"start":1146,"end":1912,"type":"D"}],"Molecular function":[{"start":1146,"end":1912,"type":"F"}],"Disorder function":[{"start":1146,"end":1912,"type":"F"}]}},{"disprot_id":"DP03508","acc":"P26662","creator":"vnugnes","date":"2021-10-06T09:27:46.678Z","features":{"pfam":[{"id":"PF00998","name":"Viral RNA dependent RNA polymerase","start":2422,"end":2932},{"id":"PF01001","name":"Hepatitis C virus non-structural protein NS4b","start":1728,"end":1921},{"id":"PF01006","name":"Hepatitis C virus non-structural protein NS4a","start":1658,"end":1711},{"id":"PF01506","name":"Hepatitis C virus non-structural 5a protein membrane anchor","start":1974,"end":1996},{"id":"PF01538","name":"Hepatitis C virus non-structural protein NS2","start":811,"end":1005},{"id":"PF01539","name":"Hepatitis C virus envelope glycoprotein E1","start":193,"end":382},{"id":"PF01542","name":"Hepatitis C virus core protein","start":116,"end":190},{"id":"PF01543","name":"Hepatitis C virus capsid protein","start":2,"end":115},{"id":"PF01560","name":"Hepatitis C virus non-structural protein E2/NS1","start":386,"end":729},{"id":"PF02907","name":"Hepatitis C virus NS3 protease","start":1057,"end":1203},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1293,"end":1355},{"id":"PF08300","name":"Hepatitis C virus non-structural 5a zinc finger domain","start":2006,"end":2067},{"id":"PF08301","name":"Hepatitis C virus non-structural 5a domain 1b","start":2068,"end":2168},{"id":"PF12941","name":"HCV NS5a protein C-terminal region","start":2179,"end":2419},{"id":"PF22027","name":"NS3 RNA helicase, C-terminal helical domain","start":1516,"end":1656}],"gene3D":[]},"length":3010,"name":"Genome polyprotein","ncbi_taxon_id":11116,"organism":"Hepatitis C virus genotype 1b (isolate Japanese)","regions":[{"start":2,"end":169,"reference_id":"18033802","reference_source":"pmid","reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03508r001","statement":[{"text":"The isolated N-terminal domain of HCV core [core(2–117)], as well as the FL HCV and GBV-B core proteins are mostly unstructured in solution, showing an ellipticity minimum at ∼198 nm, characteristically of random-coil like peptides [(36) and Figure 5].","type":"Results"},{"text":"FL HCV core protein comprises the 2-169 region of the Hepatitis C virus genotype 1b (isolate Japanese) polyprotein.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-13T14:34:13.608Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":2,"end":117,"reference_id":"18033802","reference_source":"pmid","reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03508r002","statement":[{"text":"The isolated N-terminal domain of HCV core [core(2–117)], as well as the FL HCV and GBV-B core proteins are mostly unstructured in solution, showing an ellipticity minimum at ∼198 nm, characteristically of random-coil like peptides [(36) and Figure 5].","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-13T14:34:12.693Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":2,"end":117,"reference_id":"18033802","reference_source":"pmid","reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03508r003","statement":[{"text":"The ability of purified proteins to stably bind RNA and DNA was verified by means of mobility shift assays. All four proteins bound both to RNA and DNA without a strict sequence specificity, and they caused complete retention of the nucleic acids at the top of the gel (indicative of the formation of large nucleoprotein complexes) at a protein-to-nucleotide molar ratio of ∼1:20 (data not shown).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-13T14:34:15.842Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":2,"end":117,"reference_id":"18033802","reference_source":"pmid","reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03508r004","statement":[{"text":"The ability of purified proteins to stably bind RNA and DNA was verified by means of mobility shift assays. All four proteins bound both to RNA and DNA without a strict sequence specificity, and they caused complete retention of the nucleic acids at the top of the gel (indicative of the formation of large nucleoprotein complexes) at a protein-to-nucleotide molar ratio of ∼1:20 (data not shown).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-13T14:34:14.576Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":2,"end":169,"reference_id":"18033802","reference_source":"pmid","reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140691","term_name":"RNA folding chaperone","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03508r005","statement":[{"text":"By means of classical in vitro RNA chaperone assays (e.g. strand annealing, strand exchange and ribozyme assays; Figures 2 and ​and3,3, and data not shown), we showed that nucleic acid chaperone activity is also conserved between the two hepacivirus core proteins, and that GBV-B core also efficiently facilitates the formation of the most stable nucleic acid structure. ","type":"Discussion"},{"text":" As expected, all core proteins induced a considerable increase in the cleavage rates, with hepacivirus core proteins demonstrating a higher activity compared to WNV and BVDV cores (Figure 4C).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-13T14:34:17.940Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA or an RNA-containing complex to assist the folding process.\" [PMID:31165735]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":2,"end":117,"reference_id":"18033802","reference_source":"pmid","reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140691","term_name":"RNA folding chaperone","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03508r006","statement":[{"text":"By means of classical in vitro RNA chaperone assays (e.g. strand annealing, strand exchange and ribozyme assays; Figures 2 and ​and3,3, and data not shown), we showed that nucleic acid chaperone activity is also conserved between the two hepacivirus core proteins, and that GBV-B core also efficiently facilitates the formation of the most stable nucleic acid structure. ","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-13T14:34:16.825Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA or an RNA-containing complex to assist the folding process.\" [PMID:31165735]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":2,"end":169,"reference_id":"18033802","reference_source":"pmid","reference_html":"RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. <i> Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. </i> Nucleic Acids Res, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006317","ec_ontology":"ECO","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03508r007","statement":[{"text":"FL HCV and GBV-B core proteins retained most of their chaperone activity after boiling for 5 min (∼75%, based on PhosporImager quantification, see lanes 4–6 versus 7–9 in Figure 4A and lanes 29–31 versus 32–34 in Figure 4B).","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-13T14:34:11.464Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1202,"end":1213,"reference_id":"10702283","reference_source":"pmid","reference_html":"Inhibition of the hepatitis C virus NS3/4A protease. The crystal structures of two protease-inhibitor complexes. <i> Di Marco S, Rizzi M, Volpari C, Walsh MA, Narjes F, Colarusso S, De Francesco R, Matassa VG, Sollazzo M. </i> J Biol Chem, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"cross_refs":[{"db":"PDB","id":"1DY9"},{"db":"PDB","id":"1DY8"},{"db":"PDB","id":"1DXP"}],"region_id":"DP03508r008","statement":[{"text":"The PDB shows the disordered region 1202-1213 of the Serine protease/helicase NS3.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-15T11:03:35.616Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1202,"end":1213,"reference_id":"21113170","reference_source":"pmid","reference_html":"Selective irreversible inhibition of a protease by targeting a noncatalytic cysteine. <i> Hagel M, Niu D, St Martin T, Sheets MP, Qiao L, Bernard H, Karp RM, Zhu Z, Labenski MT, Chaturvedi P, Nacht M, Westlin WF, Petter RC, Singh J. </i> Nat Chem Biol, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"cross_refs":[{"db":"PDB","id":"3OYP"}],"region_id":"DP03508r009","statement":[{"text":"The PDB shows the disordered region 1202-1213 of the Serine protease/helicase NS3.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-15T11:03:54.519Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":9,"released":"2023_06","sequence":"MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARRPEGRTWAQPGYPWPLYGNEGMGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLALLSCLTIPASAYEVRNVSGIYHVTNDCSNSSIVYEAADMIMHTPGCVPCVRESNFSRCWVALTPTLAARNSSIPTTTIRRHVDLLVGAAALCSAMYVGDLCGSVFLVSQLFTFSPRRYETVQDCNCSIYPGHVSGHRMAWDMMMNWSPTTALVVSQLLRIPQAVVDMVAGAHWGVLAGLAYYSMVGNWAKVLIVMLLFAGVDGHTHVTGGRVASSTQSLVSWLSQGPSQKIQLVNTNGSWHINRTALNCNDSLQTGFIAALFYAHRFNASGCPERMASCRPIDEFAQGWGPITHDMPESSDQRPYCWHYAPRPCGIVPASQVCGPVYCFTPSPVVVGTTDRFGAPTYSWGENETDVLLLSNTRPPQGNWFGCTWMNSTGFTKTCGGPPCNIGGVGNNTLVCPTDCFRKHPEATYTKCGSGPWLTPRCMVDYPYRLWHYPCTVNFTVFKVRMYVGGVEHRLNAACNWTRGERCDLEDRDRSELSPLLLSTTEWQILPCSFTTLPALSTGLIHLHRNIVDVQYLYGIGSAVVSFAIKWEYILLLFLLLADARVCACLWMMLLIAQAEATLENLVVLNAASVAGAHGLLSFLVFFCAAWYIKGRLVPGAAYALYGVWPLLLLLLALPPRAYAMDREMAASCGGAVFVGLVLLTLSPYYKVFLARLIWWLQYFITRAEAHLQVWVPPLNVRGGRDAIILLTCAVHPELIFDITKLLLAILGPLMVLQAGITRVPYFVRAQGLIRACMLVRKVAGGHYVQMAFMKLAALTGTYVYDHLTPLRDWAHAGLRDLAVAVEPVVFSDMETKLITWGADTAACGDIISGLPVSARRGKEILLGPADSFGEQGWRLLAPITAYSQQTRGLLGCIITSLTGRDKNQVDGEVQVLSTATQSFLATCVNGVCWTVYHGAGSKTLAGPKGPITQMYTNVDQDLVGWPAPPGARSMTPCTCGSSDLYLVTRHADVVPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPSGHVVGIFRAAVCTRGVAKAVDFIPVESMETTMRSPVFTDNSSPPAVPQTFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIEPNIRTGVRTITTGGPITYSTYCKFLADGGCSGGAYDIIICDECHSTDSTTILGIGTVLDQAETAGARLVVLATATPPGSITVPHPNIEEVALSNTGEIPFYGKAIPIEAIKGGRHLIFCHSKKKCDELAAKLTGLGLNAVAYYRGLDVSVIPTSGDVVVVATDALMTGFTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTLPQDAVSRAQRRGRTGRGRSGIYRFVTPGERPSGMFDSSVLCECYDAGCAWYELTPAETSVRLRAYLNTPGLPVCQDHLEFWESVFTGLTHIDAHFLSQTKQAGDNLPYLVAYQATVCARAQAPPPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEVTLTHPITKYIMACMSADLEVVTSTWVLVGGVLAALAAYCLTTGSVVIVGRIILSGRPAVIPDREVLYQEFDEMEECASHLPYIEQGMQLAEQFKQKALGLLQTATKQAEAAAPVVESKWRALEVFWAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTASITSPLTTQNTLLFNILGGWVAAQLAPPSAASAFVGAGIAGAAVGSIGLGKVLVDILAGYGAGVAGALVAFKVMSGEMPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLIAFASRGNHVSPTHYVPESDAAARVTQILSSLTITQLLKRLHQWINEDCSTPCSGSWLKDVWDWICTVLSDFKTWLQSKLLPRLPGLPFLSCQRGYKGVWRGDGIMQTTCPCGAQITGHVKNGSMRIVGPKTCSNTWHGTFPINAYTTGPCTPSPAPNYSRALWRVAAEEYVEVTRVGDFHYVTGMTTDNVKCPCQVPAPEFFTEVDGVRLHRYAPVCKPLLREEVVFQVGLNQYLVGSQLPCEPEPDVAVLTSMLTDPSHITAETAKRRLARGSPPSLASSSASQLSAPSLKATCTTHHDSPDADLIEANLLWRQEMGGNITRVESENKVVILDSFDPIRAVEDEREISVPAEILRKPRKFPPALPIWARPDYNPPLLESWKDPDYVPPVVHGCPLPSTKAPPIPPPRRKRTVVLTESTVSSALAELATKTFGSSGSSAVDSGTATGPPDQASDDGDKGSDVESYSSMPPLEGEPGDPDLSDGSWSTVSGEAGEDVVCCSMSYTWTGALITPCAAEESKLPINPLSNSLLRHHSMVYSTTSRSASLRQKKVTFDRLQVLDDHYRDVLKEMKAKASTVKARLLSIEEACKLTPPHSAKSKFGYGAKDVRSLSSRAVNHIRSVWEDLLEDTETPIDTTIMAKNEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVSTLPQAVMGPSYGFQYSPGQRVEFLVNTWKSKKCPMGFSYDTRCFDSTVTENDIRTEESIYQCCDLAPEARQAIRSLTERLYVGGPLTNSKGQNCGYRRCRASGVLTTSCGNTLTCYLKATAACRAAKLQDCTMLVNGDDLVVICESAGTQEDAAALRAFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDASGKRVYYLTRDPTTPLARAAWETVRHTPVNSWLGNIIMYAPTLWARMILMTHFFSILLAQEQLEKALDCQIYGACYSIEPLDLPQIIERLHGLSAFSLHSYSPGEINRVASCLRKLGVPPLRVWRHRARSVRAKLLSQGGRAATCGKYLFNWAVKTKLKLTPIPAASQLDLSGWFVAGYNGGDIYHSLSRARPRWFMLCLLLLSVGVGIYLLPNR","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Hepacivirus"],"dataset":["Viral proteins","RNA-binding proteins"],"uniref50":"UniRef50_P27958","uniref90":"UniRef90_P26662","uniref100":"UniRef100_P26662","genes":[],"disorder_content":0.059800664451827246,"disprot_consensus":{"full":[{"start":2,"end":169,"type":"D"},{"start":1202,"end":1213,"type":"D"}],"Structural state":[{"start":2,"end":169,"type":"D"},{"start":1202,"end":1213,"type":"D"}],"Molecular function":[{"start":2,"end":169,"type":"F"}]}},{"disprot_id":"DP03509","acc":"K9MZ21","creator":"fquaglia","date":"2021-10-07T15:10:50.656Z","features":{"pfam":[{"id":"PF03210","name":"Paramyxovirus P/V phosphoprotein C-terminal","start":230,"end":383},{"id":"PF14313","name":"N-terminal region of Paramyxovirinae phosphoprotein (P)","start":2,"end":56}],"gene3D":[]},"length":388,"name":"Phosphoprotein","ncbi_taxon_id":152219,"organism":"Menangle virus","regions":[{"start":267,"end":328,"reference_id":"34578318","reference_source":"pmid","reference_html":"Structural Analysis of the Menangle Virus P Protein Reveals a Soft Boundary between Ordered and Disordered Regions. <i> Webby MN, Herr N, Bulloch EMM, Schmitz M, Keown JR, Goldstone DC, Kingston RL. </i> Viruses, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03509r001","statement":[{"text":"The Linker Sequence Can Be Modeled as A Worm-like Chain and Exhibits Only Weak Local Conformational Preferences RES\nIn contrast, the Kratky plot for the isolated linker (L) increases monotonically with the scattering angle, which is characteristic of unfolded proteins [76].","type":"Results"},{"text":"From the pair distance distribution function P(r) (Figure 4), the radius of gyration (Rg) of the linker is estimated as 26.4 Å by numerical integration. For comparison, the radius of gyration of an intrinsically disordered protein of this chain length (62 residues) is predicted to be 22.7 Å, using a power law expression developed for chemically denatured proteins [77]. Hence, the linker is globally disordered.","type":"Results"}],"cross_refs":[{"db":"SASBDB","id":"SASDLJ9"},{"db":"SASBDB","id":"SASDLH9"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-11T09:40:41.218Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":267,"end":328,"reference_id":"34578318","reference_source":"pmid","reference_html":"Structural Analysis of the Menangle Virus P Protein Reveals a Soft Boundary between Ordered and Disordered Regions. <i> Webby MN, Herr N, Bulloch EMM, Schmitz M, Keown JR, Goldstone DC, Kingston RL. </i> Viruses, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03509r002","statement":[{"text":"As expected, backbone amide resonances associated with the linker (L) showed very limited chemical shift dispersion in the proton dimension, consistent with global disorder, while those associated with the binding domain (BD) were widely dispersed, consistent with overwhelming population of the folded state [61]. The propensity for structure formation in the linker was assessed using the ncSPC algorithm (Figure S4B), based on the weighted deviation of the chemical shifts of five backbone nuclei (1Hα, 13CO, 13Cα, 13Cβ, 15N) from reference values specific for intrinsically disordered proteins [83]. The results are fairly concordant with secondary structure prediction (Figure S4A) and suggest that very weak local structural preferences for extended beta-conformation or alpha-helical conformation do exist, with these preferences alternating along the length of the linker.","type":"Results"},{"text":"Overall, the NMR analysis confirmed that the linker is not uniformly disordered. It contains localized segments with very weak conformational preferences, and there is evidence for conformational exchange occurring in some regions.","type":"Results"}],"cross_refs":[{"db":"BMRB","id":"27634"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-11T09:40:42.974Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MDNPPSDAEISAWIDKGLDTVEHFLSVATDPARSLGKSTIKPGKTQELIRSAEKLAGAVAQSGEKGDRDKAKKEVTTAAPEPAVREKVRPIDVEPSDDIYEEVIPSENSKLIPPVTPKKPPRHKDRIMSMMPLQSDKQLTESMESQVFKRGGKDLRHGPSDIGPGATGGKSQLTGLVGGRESQSGATQYVTQSPSQPSEVTADVEIAPTSAPYVKEIIHYLQTLETRINNLDWKVDKILSQQSVITQIKHEQHAIKAGIATLEGLITTIKIMDPGVGDGATAAKSKRLFKEAPVVVSGPVIGENPIVDADTIQLDELARPSLPKTKSQKTGAASPAALSGYKMTLLALIKECIPNQAQRQKFEMQVGGIRNEQDFKNLRREIIRSAAQ","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Paramyxoviridae","Rubulavirinae","Pararubulavirus","Menangle pararubulavirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_A0A2U8ZTU4","uniref90":"UniRef90_K9MZ21","uniref100":"UniRef100_K9MZ21","genes":[{"name":{"value":"P","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AFY09790.1","url":"https://www.ebi.ac.uk/ena/browser/view/AFY09790.1"}}]},"synonyms":[{"value":"V","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AFY09790.1","url":"https://www.ebi.ac.uk/ena/browser/view/AFY09790.1"}}]}]}],"disorder_content":0.15979381443298968,"disprot_consensus":{"full":[{"start":267,"end":328,"type":"D"}],"Structural state":[{"start":267,"end":328,"type":"D"}]}},{"disprot_id":"DP03510","acc":"P49753","creator":"fquaglia","date":"2021-10-13T07:35:03.141Z","features":{"pfam":[{"id":"PF04775","name":"Acyl-CoA thioester hydrolase/BAAT N-terminal region","start":78,"end":202},{"id":"PF08840","name":"BAAT / Acyl-CoA thioester hydrolase C terminal","start":266,"end":473}],"gene3D":[]},"length":483,"name":"Acyl-coenzyme A thioesterase 2, mitochondrial","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":46,"end":56,"reference_id":"19497300","reference_source":"pmid","reference_html":"Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2). <i> Mandel CR, Tweel B, Tong L. </i> Biochem Biophys Res Commun, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"3HLK"}],"region_id":"DP03510r001","statement":[{"text":"The current model contains residues 58-435 and 443-472 for the first ACOT2 molecule, residues 57-436 and 442-472 for the second ACOT2 molecule, and 442 waters.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-06T15:34:45.298Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":473,"end":483,"reference_id":"19497300","reference_source":"pmid","reference_html":"Crystal structure of human mitochondrial acyl-CoA thioesterase (ACOT2). <i> Mandel CR, Tweel B, Tong L. </i> Biochem Biophys Res Commun, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"3HLK"}],"region_id":"DP03510r002","statement":[{"text":"The current model contains residues 58-435 and 443-472 for the first ACOT2 molecule, residues 57-436 and 442-472 for the second ACOT2 molecule, and 442 waters.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-06T15:34:49.176Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2023_12","sequence":"MSNKLLSPHPHSVVLRSEFKMASSPAVLRASRLYQWSLKSSAQFLGSPQLRQVGQIIRVPARMAATLILEPAGRCCWDEPVRIAVRGLAPEQPVTLRASLRDEKGALFQAHARYRADTLGELDLERAPALGGSFAGLEPMGLLWALEPEKPLVRLVKRDVRTPLAVELEVLDGHDPDPGRLLCQTRHERYFLPPGVRREPVRVGRVRGTLFLPPEPGPFPGIVDMFGTGGGLLEYRASLLAGKGFAVMALAYYNYEDLPKTMETLHLEYFEEAMNYLLSHPEVKGPGVGLLGISKGGELCLSMASFLKGITAAVVINGSVANVGGTLHYKGETLPPVGVNRNRIKVTKDGYADIVDVLNSPLEGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEACKRLQAHGRRKPQIICYPETGHYIEPPYFPLCRASLHALVGSPIIWGGEPRAHAMAQVDAWKQLQTFFHKHLGGHEGTIPSKV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref50":"UniRef50_P49753","uniref90":"UniRef90_P49753","uniref100":"UniRef100_P49753","genes":[{"name":{"value":"ACOT2"},"synonyms":[{"value":"PTE2"},{"value":"PTE2A"}]}],"alphafold_very_low_content":0.12836438923395446,"disorder_content":0.045548654244306416,"disprot_consensus":{"full":[{"start":46,"end":56,"type":"D"},{"start":473,"end":483,"type":"D"}],"Structural state":[{"start":46,"end":56,"type":"D"},{"start":473,"end":483,"type":"D"}]}},{"disprot_id":"DP03511","acc":"Q9WIK7","creator":"vnugnes","date":"2021-10-13T12:36:13.320Z","features":{"pfam":[{"id":"PF00998","name":"Viral RNA dependent RNA polymerase","start":2424,"end":2933},{"id":"PF01001","name":"Hepatitis C virus non-structural protein NS4b","start":1730,"end":1923},{"id":"PF01006","name":"Hepatitis C virus non-structural protein NS4a","start":1660,"end":1713},{"id":"PF01506","name":"Hepatitis C virus non-structural 5a protein membrane anchor","start":1976,"end":1998},{"id":"PF01538","name":"Hepatitis C virus non-structural protein NS2","start":813,"end":1007},{"id":"PF01539","name":"Hepatitis C virus envelope glycoprotein E1","start":193,"end":382},{"id":"PF01542","name":"Hepatitis C virus core protein","start":116,"end":190},{"id":"PF01543","name":"Hepatitis C virus capsid protein","start":2,"end":115},{"id":"PF01560","name":"Hepatitis C virus non-structural protein E2/NS1","start":389,"end":731},{"id":"PF02907","name":"Hepatitis C virus NS3 protease","start":1058,"end":1205},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1296,"end":1357},{"id":"PF08300","name":"Hepatitis C virus non-structural 5a zinc finger domain","start":2008,"end":2069},{"id":"PF08301","name":"Hepatitis C virus non-structural 5a domain 1b","start":2070,"end":2170},{"id":"PF12941","name":"HCV NS5a protein C-terminal region","start":2181,"end":2421},{"id":"PF22027","name":"NS3 RNA helicase, C-terminal helical domain","start":1518,"end":1658}],"gene3D":[]},"length":3012,"name":"Core protein precursor","ncbi_taxon_id":11103,"organism":"Hepacivirus C","regions":[{"start":2282,"end":2301,"reference_id":"26085105","reference_source":"pmid","reference_html":"A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication. <i> Dujardin M, Madan V, Montserret R, Ahuja P, Huvent I, Launay H, Leroy A, Bartenschlager R, Penin F, Lippens G, Hanoulle X. </i> J Biol Chem, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03511r001","statement":[{"text":"Region 2280-2299 is mainly unstructured, as shown by its large negative ellipticity at 200 nm and moderate ellipticity at 190 nm in the far-UV CD spectra (Figure 7).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-13T13:40:34.397Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":2282,"end":2315,"reference_id":"26085105","reference_source":"pmid","reference_html":"A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication. <i> Dujardin M, Madan V, Montserret R, Ahuja P, Huvent I, Launay H, Leroy A, Bartenschlager R, Penin F, Lippens G, Hanoulle X. </i> J Biol Chem, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03511r002","statement":[{"text":"The 1H,15N HSQC spectrum of NS5A-D2 (Con1 strain) displays a narrow 1HN chemical shift dispersion limited to 1 ppm, as expected for a mainly disordered domain (Fig. 1A).","type":"Results"},{"text":"The NS5A fragment used in this publication was derived from the Hepacivirus C. IDR is 100% identical to the Hepatitis C virus genotype 1b (isolate Con1) polyprotein UniProtKB:Q9WMX2.\n","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-13T13:40:36.229Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":2282,"end":2301,"reference_id":"26085105","reference_source":"pmid","reference_html":"A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication. <i> Dujardin M, Madan V, Montserret R, Ahuja P, Huvent I, Launay H, Leroy A, Bartenschlager R, Penin F, Lippens G, Hanoulle X. </i> J Biol Chem, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"interaction_partner":[{"db":"UniProt","id":"P62937","partner_start":null,"partner_end":null}],"region_id":"DP03511r003","statement":[{"text":"The affinity between CypA and the PW turn containing PepD2-WT peptide (KD = 0.5 mm) is three times better than the one involving the random coil PepD2-I315G peptide (KD = 1.4 mm).","type":"Results"},{"text":"PepD2-WT comprises the region 2282-2301 of the Hepatitis C virus genome polyprotein.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-11T11:04:20.406Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":2282,"end":2301,"reference_id":"26085105","reference_source":"pmid","reference_html":"A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication. <i> Dujardin M, Madan V, Montserret R, Ahuja P, Huvent I, Launay H, Leroy A, Bartenschlager R, Penin F, Lippens G, Hanoulle X. </i> J Biol Chem, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"cross_refs":[{"db":"BMRB","id":"19059"},{"db":"PDB","id":"2M5L"}],"region_id":"DP03511r005","statement":[{"text":"The final set of 28 low energy structures that fulfill the experimental restraints displays a well defined small structural motif (from Met313 to Ala317) in PepD2-WT (Fig. 5 and Table 1; PDB code 2M5L), whereas the N and C termini remain highly flexible.","type":"Results"},{"text":"PepD2-WT comprises the region 2282-2301 of the Hepatitis C virus genome polyprotein.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-13T13:40:37.533Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":2282,"end":2301,"reference_id":"26085105","reference_source":"pmid","reference_html":"A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication. <i> Dujardin M, Madan V, Montserret R, Ahuja P, Huvent I, Launay H, Leroy A, Bartenschlager R, Penin F, Lippens G, Hanoulle X. </i> J Biol Chem, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019079","term_name":"viral genome replication","term_namespace":"Biological process","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03511r006","statement":[{"text":"The affinity between CypA and the PW turn containing PepD2-WT peptide (KD = 0.5 mm) is three times better than the one involving the random coil PepD2-I315G peptide (KD = 1.4 mm).","type":"Results"},{"text":"PepD2-WT comprises the region 2282-2301 of the Hepatitis C virus genome polyprotein. ","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-11T11:04:18.509Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process involved directly in viral genome replication, including viral nucleotide metabolism.\" [ISBN:0781702534]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":2287,"end":2291,"reference_id":"26085105","reference_source":"pmid","reference_html":"A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication. <i> Dujardin M, Madan V, Montserret R, Ahuja P, Huvent I, Launay H, Leroy A, Bartenschlager R, Penin F, Lippens G, Hanoulle X. </i> J Biol Chem, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019079","term_name":"viral genome replication","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0005648","ec_ontology":"ECO","ec_name":"luciferase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03511r007","statement":[{"text":" As illustrated in Fig. 8, the sole mutation I315G in NS5A almost completely abolished viral replication that was close to the background as determined with the replicon encoding an inactive NS5B RNA-polymerase (GND mutant). The replication levels corresponding to the I315G and P314A mutations, respectively, were similar. ","type":"Results"},{"text":"Hence, the short PW turn structural motif in the mainly disordered NS5A-D2 domain plays an essential role for HCV RNA replication.","type":"Results"},{"text":"PW turn corresponds to the 2288-2290 region of the core polyprotein (P314 -W316 of the Ns5B protein). Although the authors describes this region as a small structural motif, the region is to short to form any secondary structure so is interpreted as disordered here. ","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-11T11:04:17.302Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process involved directly in viral genome replication, including viral nucleotide metabolism.\" [ISBN:0781702534]","disprot_namespace":"Disorder function","term_is_binding":false}],"regions_counter":7,"released":"2023_06","sequence":"MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARRPEGRAWAQPGYPWPLYGNEGLGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLALLSCLTIPASAYEVRNVSGVYHVTNDCSNSSIVYETADMIMHTPGCVPCVREDNSSRCWVALTPTLAARNGSVPTTAIRRHVDLLVGAAAFCSAMYVGDFCGSVFLVSQLFTLSPRRHETVQECNCSIYPGHVTGHRMAWDMMMNWSPTTALVVSQLLRIPQAVVDMVAGAHWGVLAGLAYYSMVGNWAKLLIVMLLFAGVDGGGPTRTIGGSQAQAASGLVSMFSVGPSQKIQLINTNGSWHINRTALNCNDSLNTGFLAALFYAHKFNSSGCPERMASCRPIDRFAQGWGPITYAEPGSLDQRPYCWHYAPQPCGIVPASEVCGPVYCFTPSPVVVGTTDRSGVPTYRWGDNETDVLLLNNTRPPQGNWFGCTWMNTTGFTKTCGGPPCNIGGLGNNTLICPTDCFRKHSEATYTKCGSGPWLTPRCIVDYPYRLWHYPCTVNFTIFKVRMYVGGIEHRLSAACNWTRGERCNLEDRDRSELSPLLLSTTEWQILPCSFTTLPAPSTGLIHLHQNIVDVQYLYGIGSVLVSFAIKWEYILLLFLLLADARVCACLWMMLLIAQAEAALENLVVLNAASLAGAHGILSFLVFFCAAWYIKGRLVPGAAYALYSVWPLLLLLLALPPRAYAMDREMAASCGGAVFVGLVLLTLSPYYKVFLAKLIWWLQYFITRAEAHLQVWIPPLNVRGGRDAIILLTCAVHPELIFDITKLLLAILGPLMVLQAGIIRAPYFVRAQGLIRACMLVRKVAGGHYVQMAFMKLAALTGTYVYDHLTPLRDWAHAGLRDLAVAVEPVVFSDMETKIITWGADTAACGDIILGLPVSARRGKEILLGPADSLEGQGWRLLAPITAYSQQTRGLLGCIITSLTGRDKNQVEGEVQVVSTATQSFLATCVNGVCWTVYHGAGSKTLAGPKGPITQMYTNVDQDLVGWPAPSGARSLTPCTCGSSDLYLVSRHADVIPVRRRGDSRGSLLSPRPVSYLKGSSGGPLLCPSGHVVGIFRAAVCTRGVAKAVDFVPVESMETTTRSPVFTDNSSPPAVPQTFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLSFGAYMSKAHGVDPSIRTGVRTITTGAPITYSTYGKFLADGGCSGGAYDIIICDECHSTDSTSILGIGTVLDQAETAGARLVVLATATPPGSVTVPHPNIEEVALSNTGEIPFYGKAIPIETIRGGRHLIFCHSKKKCDELAAQLSGLGINAVAYYRGLDVSVIPTSGDVVVVATDALMTGFTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTVPQDAVSRSQRRGRTGRGRRGIYRFVTPGERPSGMFDSSVLCECYDAGCAWYELTPAETSVRLRAYLNTPGLPVCQDHLEFWESVFTGLTHIDAHFLSQTKQAGDNFPYLVAYQATVCARAQAPPPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEVTLTHPVTKYIMACMSADLEVVTSTWVLVGGVLAALAAYCLTTGSVVIVGRIILSGKPAIVPDRGVLYREFDEMEECASHLPYIEQGMQLAEQFKQKALGLLQTATKQAEAAAPVVESKWRALEAFWAKHMWSFISGIQYLAGLSTLPGNPAIASLMAFTASVTSPLTTQHTLLFNILGGWVAAQLAPPSAASAFVGAGIAGAAVGSIGLGKVLVDILAGYGAGVAGALVAFKVMSGEMPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLIAFASRGNHVSPTHYVPESDAAARVTQILSSLTITQLLKRLHQWINEDCSTPCSGSWLRDVWDWICTVLTDFKTWLQSKLLPRLPGVPFFSCQRGYKGVWRGDGIMQTTCPCGAQITGHVKNGSMRIVGPRTCSNTWHGTFPINAYTTGPCTPSPAPNYFRALWRVAAEEYVEVTRVGDFHYVTGMTTDNVKCPCQVPAPEFFTEVDGVRLHRYAPACKPLLREEVTFQVGLNQYLVGSQLPCEPEPGVTVLTSMLTDPSHITAETAKRRLDRGSPPSLASSSASQLSAPSLKATCTTRHDSPDADLIEANLLWRQEMGGNITRVESENKVVILDSFDPLRAEEDEREISVPAEILRRSRKFPRAMPIWARPDYNPPLLESWKDPDYVPPVVHGCPLPPAKAPPVPPPRRKRTVVLTESTVSSALAELATKTFGSSESSAVDSGTATAPPGQPSDGGDTGSDAESCSSMPPLEGEPGDPDLSDGSWSTVSEEASEDVVCCSMSYTWTGALITPCAAEESKLPINALSNSLLRHHNMVYATTSRSASQRQKKVTFDRLQVLDDHYWDVLKEMKAKASTVKARLLSVEEACKLTPPHSAKSKFGYGAKDVRNLSSKAINHINSVWEDLLEDTETPIDTTIMAKNEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVSTLPQAVMGSSYGFQYSPGQRVEFLVKAWSSKKNPMGFAYDTRCFDSTVTENDIRVGESIYQCCDLAPEARQAIRSLTERLYIGGPLTNSKGQNCGYRRCRASGVLTTSCGNTLTCYLKASAACRAAKLQDCTMLVCGDDLVVICESAGTQEDAASLRVFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDASGKRVYYLTRDPTTPLARAAWETARHTPVNSWLGNIIMYAPTLWARMVLMIHFFSILLAQEQLEKALDCQIYGACYSIEPLDLPQIIQRLHGLSAFSLHSYSPGEINRVASCLRKLGVPPLRVWRHRARSVRAKLLSRGGRAATCGKYLFNWAVRTKLKLTPIPAASRLDLSGWFVAGYSGGDIYHSLSPARPRWFMWCLLLLSVGVGIYLLPNR","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Hepacivirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_P27958","uniref90":"UniRef90_P26662","uniref100":"UniRef100_Q9WIK7","genes":[],"disorder_content":0.011288180610889775,"disprot_consensus":{"full":[{"start":2282,"end":2315,"type":"D"}],"Structural state":[{"start":2282,"end":2315,"type":"D"}],"Molecular function":[{"start":2282,"end":2301,"type":"F"}],"Biological process":[{"start":2282,"end":2301,"type":"F"}]}},{"disprot_id":"DP03512","acc":"P18827","creator":"fquaglia","date":"2021-10-18T15:01:17.416Z","features":{"pfam":[{"id":"PF01034","name":"Syndecan domain","start":246,"end":308}],"gene3D":[]},"length":310,"name":"Syndecan-1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":23,"end":254,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03512r001","statement":[{"text":"The molecular weight of the syndecan EDs were higher than the theoretical values when calculated by SDS-PAGE and size-exclusion chromatography but consistent with them and with the existence of a dimer of ED-4 when determined by ESI-MS and SEC-MALLS (Supplementary Table S2 and Supplementary Fig. S1).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:05:30.819Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":23,"end":254,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03512r002","statement":[{"text":"The molecular weight of the syndecan EDs were higher than the theoretical values when calculated by SDS-PAGE and size-exclusion chromatography but consistent with them and with the existence of a dimer of ED-4 when determined by ESI-MS and SEC-MALLS (Supplementary Table S2 and Supplementary Fig. S1).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:05:27.827Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":23,"end":254,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03512r003","statement":[{"text":"To experimentally estimate their amount of intrinsic disorder, the syndecan ectodomains were then analyzed by circular dichroism (Fig. 2A). The largest ectodomains, ED-1 and ED-3, were the most disordered (69 % of random coil), whereas the smallest ones, ED-2 and ED-4, contained 52 % and 44 % of random coil respectively (Fig. 2B). The content in α-helix of the four ectodomains was very low (<3 %), but they contained a significant amount of β-strands, which was higher in ED-2 and ED-4 (26 % and 33 % respectively) than in ED-1 and ED-3 (16 % and 17 % respectively) (Fig. 2B). β-strands were predicted to be located in the C-terminal half of ED-1 and ED-4 but distributed along ED-2 and ED-3 sequences (Supplementary Fig. S2A). Although they are extensively disordered, the syndecan EDs contain a significant amount of hydrophobic residues (37–52 %) of the total amino acid residues, which are usually depleted in IDPs [31].","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:05:16.181Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":23,"end":254,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03512r004","statement":[{"text":"The syndecan ectodomains are highly extended and flexible in solution","type":"Results"},{"text":"The four syndecan ectodomains were analyzed by SEC-small-angle X-ray scattering (SEC-SAXS) (Fig. 3 and Supplementary Fig. S4). ED-2 and the monomeric form of ED-4 had a similar radius of gyration (42.9 ± 0.33 Å and 41.53 ± 0.67 Å respectively), and a similar maximum intramolecular distance Dmax (185 Å and 180 Å respectively) (Table 1 and Supplementary Fig. S5).","type":"Results"},{"text":"The experimental values of the radius of gyration of the four ectodomains were close to the theoretical values calculated using the Flory’s equation for a random coil protein containing the same number of amino acid residues (Table 1). Furthermore, the Flory exponential scaling factors calculated for the syndecan EDs were 0.58 and 0.59, similar to the value calculated for chemically disordered proteins (0.60) which are more extended than IDPs [33].","type":"Results"},{"text":"The shape of the normalized Kratky plots of the four EDs (Fig. 3C) and of the ED4-dimer (Fig. 3D) was consistent with those of IDPs [35]. The Porod exponents of the EDs were similar (1.7 for ED-1, ED-3 and the monomer of ED-4, 1.8 for ED-2, and 1.9 for the dimer of ED-4) indicating that they all are flexible, the Porod exponent being equal to 2 for fully flexible systems [36]. The EDs flexibility was also demonstrated by the plateau observed in the Kratky-Debye plots (Fig. 3E). The syndecan ectodomains are thus disordered, flexible, and extended proteins in solution.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:04:44.824Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":23,"end":254,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03512r005","statement":[{"text":"The hydrodynamic radius (Rh) of the ectodomains, determined by size-exclusion chromatography-dynamic light scattering (SEC-DLS), ranged from 34.1 Å (ED-2) to 50.1 Å (ED-3), and their Rg/Rh ratio, that provides information about protein shape and compactness, ranged from 1.16 (ED-4 monomer) to 1.31 (ED-4 dimer) (Table 1). These values were far higher than those of globular proteins (0.778) and close to those reported for prolate ellipsoids (1.36–2.24) [34] (Table 1).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:04:24.868Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":23,"end":254,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007184","ec_ontology":"ECO","ec_name":"protein mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03512r006","statement":[{"text":"Electrospray ionization-mass spectrometry (ESI-MS) in native conditions provides information on the variable degrees of compactness of IDPs. The charge state distributions (CSDs) determined by ESI-MS are related to the global compactness of proteins upon their transfer from solution to gas phase, the highest charge states corresponding to the most extended conformations [42]. The CSDs of the four ectodomains were trimodal, showing that the ectodomains of syndecans could adopt preferential conformations (Fig. 5A). Gaussian functions were fitted to the CSD envelopes to determine the relative proportions of the three major conformational ensembles. The most extended conformations (i.e. the highest charge states) were the most abundant for ED-1 (86 %), ED-2 (70 %) and ED-4 (85 %) but accounted for only 24 % for ED-3, in which the population with intermediate charge states predominated (Fig. 5B). Most compact conformations were found in minor amount for ED-1 (2 %), ED-2 (4 %), and ED-4 (8 %) and in larger amount for ED-3 (14 %).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:35:50.931Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":6,"released":"2023_12","sequence":"MRRAALWLWLCALALSLQPALPQIVATNLPPEDQDGSGDDSDNFSGSGAGALQDITLSQQTPSTWKDTQLLTAIPTSPEPTGLEATAASTSTLPAGEGPKEGEAVVLPEVEPGLTAREQEATPRPRETTQLPTTHLASTTTATTAQEPATSHPHRDMQPGHHETSTPAGPSQADLHTPHTEDGGPSATERAAEDGASSQLPAAEGSGEQDFTFETSGENTAVVAVEPDRRNQSPVDQGATGASQGLLDRKEVLGGVIAGGLVGLIFAVCLVGFMLYRMKKKDEGSYSLEEPKQANGGAYQKPTKQEEFYA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref50":"UniRef50_P18827","uniref90":"UniRef90_P18827","uniref100":"UniRef100_P18827","genes":[{"name":{"value":"SDC1"},"synonyms":[{"value":"SDC"}]}],"alphafold_very_low_content":0.45806451612903226,"dataset":["Extracellular matrix proteins"],"disorder_content":0.7483870967741936,"disprot_consensus":{"full":[{"start":23,"end":254,"type":"D"}],"Structural state":[{"start":23,"end":254,"type":"D"}]}},{"disprot_id":"DP03513","acc":"P34741","creator":"fquaglia","date":"2021-10-18T15:01:23.781Z","features":{"pfam":[{"id":"PF01034","name":"Syndecan domain","start":138,"end":199}],"gene3D":[]},"length":201,"name":"Syndecan-2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":19,"end":144,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03513r001","statement":[{"text":"The molecular weight of the syndecan EDs were higher than the theoretical values when calculated by SDS-PAGE and size-exclusion chromatography but consistent with them and with the existence of a dimer of ED-4 when determined by ESI-MS and SEC-MALLS (Supplementary Table S2 and Supplementary Fig. S1).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:36:12.565Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":19,"end":144,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03513r002","statement":[{"text":"The molecular weight of the syndecan EDs were higher than the theoretical values when calculated by SDS-PAGE and size-exclusion chromatography but consistent with them and with the existence of a dimer of ED-4 when determined by ESI-MS and SEC-MALLS (Supplementary Table S2 and Supplementary Fig. S1).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:36:10.694Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":19,"end":144,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03513r003","statement":[{"text":"To experimentally estimate their amount of intrinsic disorder, the syndecan ectodomains were then analyzed by circular dichroism (Fig. 2A). The largest ectodomains, ED-1 and ED-3, were the most disordered (69 % of random coil), whereas the smallest ones, ED-2 and ED-4, contained 52 % and 44 % of random coil respectively (Fig. 2B). The content in α-helix of the four ectodomains was very low (<3 %), but they contained a significant amount of β-strands, which was higher in ED-2 and ED-4 (26 % and 33 % respectively) than in ED-1 and ED-3 (16 % and 17 % respectively) (Fig. 2B). β-strands were predicted to be located in the C-terminal half of ED-1 and ED-4 but distributed along ED-2 and ED-3 sequences (Supplementary Fig. S2A). Although they are extensively disordered, the syndecan EDs contain a significant amount of hydrophobic residues (37–52 %) of the total amino acid residues, which are usually depleted in IDPs [31].","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:36:09.741Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":19,"end":144,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03513r004","statement":[{"text":"The syndecan ectodomains are highly extended and flexible in solution","type":"Results"},{"text":"The four syndecan ectodomains were analyzed by SEC-small-angle X-ray scattering (SEC-SAXS) (Fig. 3 and Supplementary Fig. S4). ED-2 and the monomeric form of ED-4 had a similar radius of gyration (42.9 ± 0.33 Å and 41.53 ± 0.67 Å respectively), and a similar maximum intramolecular distance Dmax (185 Å and 180 Å respectively) (Table 1 and Supplementary Fig. S5).","type":"Results"},{"text":"The experimental values of the radius of gyration of the four ectodomains were close to the theoretical values calculated using the Flory’s equation for a random coil protein containing the same number of amino acid residues (Table 1). Furthermore, the Flory exponential scaling factors calculated for the syndecan EDs were 0.58 and 0.59, similar to the value calculated for chemically disordered proteins (0.60) which are more extended than IDPs [33].","type":"Results"},{"text":"The shape of the normalized Kratky plots of the four EDs (Fig. 3C) and of the ED4-dimer (Fig. 3D) was consistent with those of IDPs [35]. The Porod exponents of the EDs were similar (1.7 for ED-1, ED-3 and the monomer of ED-4, 1.8 for ED-2, and 1.9 for the dimer of ED-4) indicating that they all are flexible, the Porod exponent being equal to 2 for fully flexible systems [36]. The EDs flexibility was also demonstrated by the plateau observed in the Kratky-Debye plots (Fig. 3E). The syndecan ectodomains are thus disordered, flexible, and extended proteins in solution.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:36:03.680Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":19,"end":144,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03513r005","statement":[{"text":"The hydrodynamic radius (Rh) of the ectodomains, determined by size-exclusion chromatography-dynamic light scattering (SEC-DLS), ranged from 34.1 Å (ED-2) to 50.1 Å (ED-3), and their Rg/Rh ratio, that provides information about protein shape and compactness, ranged from 1.16 (ED-4 monomer) to 1.31 (ED-4 dimer) (Table 1). These values were far higher than those of globular proteins (0.778) and close to those reported for prolate ellipsoids (1.36–2.24) [34] (Table 1).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:33:13.604Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":19,"end":144,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007184","ec_ontology":"ECO","ec_name":"protein mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03513r006","statement":[{"text":"Electrospray ionization-mass spectrometry (ESI-MS) in native conditions provides information on the variable degrees of compactness of IDPs. The charge state distributions (CSDs) determined by ESI-MS are related to the global compactness of proteins upon their transfer from solution to gas phase, the highest charge states corresponding to the most extended conformations [42]. The CSDs of the four ectodomains were trimodal, showing that the ectodomains of syndecans could adopt preferential conformations (Fig. 5A). Gaussian functions were fitted to the CSD envelopes to determine the relative proportions of the three major conformational ensembles. The most extended conformations (i.e. the highest charge states) were the most abundant for ED-1 (86 %), ED-2 (70 %) and ED-4 (85 %) but accounted for only 24 % for ED-3, in which the population with intermediate charge states predominated (Fig. 5B). Most compact conformations were found in minor amount for ED-1 (2 %), ED-2 (4 %), and ED-4 (8 %) and in larger amount for ED-3 (14 %).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:36:01.559Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":6,"released":"2023_12","sequence":"MRRAWILLTLGLVACVSAESRAELTSDKDMYLDNSSIEEASGVYPIDDDDYASASGSGADEDVESPELTTSRPLPKILLTSAAPKVETTTLNIQNKIPAQTKSPEETDKEKVHLSDSERKMDPAEEDTNVYTEKHSDSLFKRTEVLAAVIAGGVIGFLFAIFLILLLVYRMRKKDEGSYDLGERKPSSAAYQKAPTKEFYA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref50":"UniRef50_P34741","uniref90":"UniRef90_P34741","uniref100":"UniRef100_P34741","genes":[{"name":{"value":"SDC2"},"synonyms":[{"value":"HSPG1"}]}],"alphafold_very_low_content":0.30845771144278605,"dataset":["Extracellular matrix proteins"],"disorder_content":0.6268656716417911,"disprot_consensus":{"full":[{"start":19,"end":144,"type":"D"}],"Structural state":[{"start":19,"end":144,"type":"D"}]}},{"disprot_id":"DP03514","acc":"O75056","creator":"fquaglia","date":"2021-10-18T15:01:34.874Z","features":{"pfam":[{"id":"PF01034","name":"Syndecan domain","start":378,"end":440}],"gene3D":[]},"length":442,"name":"Syndecan-3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":47,"end":387,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03514r001","statement":[{"text":"The molecular weight of the syndecan EDs were higher than the theoretical values when calculated by SDS-PAGE and size-exclusion chromatography but consistent with them and with the existence of a dimer of ED-4 when determined by ESI-MS and SEC-MALLS (Supplementary Table S2 and Supplementary Fig. S1).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:32:46.365Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":47,"end":387,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03514r002","statement":[{"text":"The molecular weight of the syndecan EDs were higher than the theoretical values when calculated by SDS-PAGE and size-exclusion chromatography but consistent with them and with the existence of a dimer of ED-4 when determined by ESI-MS and SEC-MALLS (Supplementary Table S2 and Supplementary Fig. S1).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:32:44.767Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":47,"end":387,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03514r003","statement":[{"text":"To experimentally estimate their amount of intrinsic disorder, the syndecan ectodomains were then analyzed by circular dichroism (Fig. 2A). The largest ectodomains, ED-1 and ED-3, were the most disordered (69 % of random coil), whereas the smallest ones, ED-2 and ED-4, contained 52 % and 44 % of random coil respectively (Fig. 2B). The content in α-helix of the four ectodomains was very low (<3 %), but they contained a significant amount of β-strands, which was higher in ED-2 and ED-4 (26 % and 33 % respectively) than in ED-1 and ED-3 (16 % and 17 % respectively) (Fig. 2B). β-strands were predicted to be located in the C-terminal half of ED-1 and ED-4 but distributed along ED-2 and ED-3 sequences (Supplementary Fig. S2A). Although they are extensively disordered, the syndecan EDs contain a significant amount of hydrophobic residues (37–52 %) of the total amino acid residues, which are usually depleted in IDPs [31].","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:32:42.735Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":47,"end":387,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03514r004","statement":[{"text":"The syndecan ectodomains are highly extended and flexible in solution","type":"Results"},{"text":"The four syndecan ectodomains were analyzed by SEC-small-angle X-ray scattering (SEC-SAXS) (Fig. 3 and Supplementary Fig. S4). ED-2 and the monomeric form of ED-4 had a similar radius of gyration (42.9 ± 0.33 Å and 41.53 ± 0.67 Å respectively), and a similar maximum intramolecular distance Dmax (185 Å and 180 Å respectively) (Table 1 and Supplementary Fig. S5).","type":"Results"},{"text":"The experimental values of the radius of gyration of the four ectodomains were close to the theoretical values calculated using the Flory’s equation for a random coil protein containing the same number of amino acid residues (Table 1). Furthermore, the Flory exponential scaling factors calculated for the syndecan EDs were 0.58 and 0.59, similar to the value calculated for chemically disordered proteins (0.60) which are more extended than IDPs [33].","type":"Results"},{"text":"The shape of the normalized Kratky plots of the four EDs (Fig. 3C) and of the ED4-dimer (Fig. 3D) was consistent with those of IDPs [35]. The Porod exponents of the EDs were similar (1.7 for ED-1, ED-3 and the monomer of ED-4, 1.8 for ED-2, and 1.9 for the dimer of ED-4) indicating that they all are flexible, the Porod exponent being equal to 2 for fully flexible systems [36]. The EDs flexibility was also demonstrated by the plateau observed in the Kratky-Debye plots (Fig. 3E). The syndecan ectodomains are thus disordered, flexible, and extended proteins in solution.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:32:35.992Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":47,"end":387,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03514r005","statement":[{"text":"The hydrodynamic radius (Rh) of the ectodomains, determined by size-exclusion chromatography-dynamic light scattering (SEC-DLS), ranged from 34.1 Å (ED-2) to 50.1 Å (ED-3), and their Rg/Rh ratio, that provides information about protein shape and compactness, ranged from 1.16 (ED-4 monomer) to 1.31 (ED-4 dimer) (Table 1). These values were far higher than those of globular proteins (0.778) and close to those reported for prolate ellipsoids (1.36–2.24) [34] (Table 1).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:32:25.601Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":47,"end":387,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007184","ec_ontology":"ECO","ec_name":"protein mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03514r006","statement":[{"text":"Electrospray ionization-mass spectrometry (ESI-MS) in native conditions provides information on the variable degrees of compactness of IDPs. The charge state distributions (CSDs) determined by ESI-MS are related to the global compactness of proteins upon their transfer from solution to gas phase, the highest charge states corresponding to the most extended conformations [42]. The CSDs of the four ectodomains were trimodal, showing that the ectodomains of syndecans could adopt preferential conformations (Fig. 5A). Gaussian functions were fitted to the CSD envelopes to determine the relative proportions of the three major conformational ensembles. The most extended conformations (i.e. the highest charge states) were the most abundant for ED-1 (86 %), ED-2 (70 %) and ED-4 (85 %) but accounted for only 24 % for ED-3, in which the population with intermediate charge states predominated (Fig. 5B). Most compact conformations were found in minor amount for ED-1 (2 %), ED-2 (4 %), and ED-4 (8 %) and in larger amount for ED-3 (14 %).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:36:57.972Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":6,"released":"2023_12","sequence":"MKPGPPHRAGAAHGAGAGAGAAAGPGARGLLLPPLLLLLLAGRAAGAQRWRSENFERPVDLEGSGDDDSFPDDELDDLYSGSGSGYFEQESGIETAMRFSPDVALAVSTTPAVLPTTNIQPVGTPFEELPSERPTLEPATSPLVVTEVPEEPSQRATTVSTTMATTAATSTGDPTVATVPATVATATPSTPAAPPFTATTAVIRTTGVRRLLPLPLTTVATARATTPEAPSPPTTAAVLDTEAPTPRLVSTATSRPRALPRPATTQEPDIPERSTLPLGTTAPGPTEVAQTPTPETFLTTIRDEPEVPVSGGPSGDFELPEEETTQPDTANEVVAVGGAAAKASSPPGTLPKGARPGPGLLDNAIDSGSSAAQLPQKSILERKEVLVAVIVGGVVGALFAAFLVTLLIYRMKKKDEGSYTLEEPKQASVTYQKPDKQEEFYA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref50":"UniRef50_O75056","uniref90":"UniRef90_O75056","uniref100":"UniRef100_O75056","genes":[{"name":{"value":"SDC3"},"synonyms":[{"value":"KIAA0468"}]}],"alphafold_very_low_content":0.5294117647058824,"dataset":["Extracellular matrix proteins"],"disorder_content":0.7714932126696833,"disprot_consensus":{"full":[{"start":47,"end":387,"type":"D"}],"Structural state":[{"start":47,"end":387,"type":"D"}]}},{"disprot_id":"DP03515","acc":"P31431-2","creator":"fquaglia","date":"2021-10-18T15:01:45.799Z","features":{"pfam":[],"gene3D":[]},"length":153,"name":"Isoform 2 of Syndecan-4","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":19,"end":153,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03515r001","statement":[{"text":"The molecular weight of the syndecan EDs were higher than the theoretical values when calculated by SDS-PAGE and size-exclusion chromatography but consistent with them and with the existence of a dimer of ED-4 when determined by ESI-MS and SEC-MALLS (Supplementary Table S2 and Supplementary Fig. S1).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:32:59.541Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":19,"end":153,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03515r002","statement":[{"text":"The molecular weight of the syndecan EDs were higher than the theoretical values when calculated by SDS-PAGE and size-exclusion chromatography but consistent with them and with the existence of a dimer of ED-4 when determined by ESI-MS and SEC-MALLS (Supplementary Table S2 and Supplementary Fig. S1).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:32:58.720Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":19,"end":153,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03515r003","statement":[{"text":"To experimentally estimate their amount of intrinsic disorder, the syndecan ectodomains were then analyzed by circular dichroism (Fig. 2A). The largest ectodomains, ED-1 and ED-3, were the most disordered (69 % of random coil), whereas the smallest ones, ED-2 and ED-4, contained 52 % and 44 % of random coil respectively (Fig. 2B). The content in α-helix of the four ectodomains was very low (<3 %), but they contained a significant amount of β-strands, which was higher in ED-2 and ED-4 (26 % and 33 % respectively) than in ED-1 and ED-3 (16 % and 17 % respectively) (Fig. 2B). β-strands were predicted to be located in the C-terminal half of ED-1 and ED-4 but distributed along ED-2 and ED-3 sequences (Supplementary Fig. S2A). Although they are extensively disordered, the syndecan EDs contain a significant amount of hydrophobic residues (37–52 %) of the total amino acid residues, which are usually depleted in IDPs [31].","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:32:56.953Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":19,"end":153,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03515r004","sample":[],"statement":[{"text":"The syndecan ectodomains are highly extended and flexible in solution","type":"Results"},{"text":"The four syndecan ectodomains were analyzed by SEC-small-angle X-ray scattering (SEC-SAXS) (Fig. 3 and Supplementary Fig. S4). ED-2 and the monomeric form of ED-4 had a similar radius of gyration (42.9 ± 0.33 Å and 41.53 ± 0.67 Å respectively), and a similar maximum intramolecular distance Dmax (185 Å and 180 Å respectively) (Table 1 and Supplementary Fig. S5).","type":"Results"},{"text":"The experimental values of the radius of gyration of the four ectodomains were close to the theoretical values calculated using the Flory’s equation for a random coil protein containing the same number of amino acid residues (Table 1). Furthermore, the Flory exponential scaling factors calculated for the syndecan EDs were 0.58 and 0.59, similar to the value calculated for chemically disordered proteins (0.60) which are more extended than IDPs [33].","type":"Results"},{"text":"The shape of the normalized Kratky plots of the four EDs (Fig. 3C) and of the ED4-dimer (Fig. 3D) was consistent with those of IDPs [35]. The Porod exponents of the EDs were similar (1.7 for ED-1, ED-3 and the monomer of ED-4, 1.8 for ED-2, and 1.9 for the dimer of ED-4) indicating that they all are flexible, the Porod exponent being equal to 2 for fully flexible systems [36]. The EDs flexibility was also demonstrated by the plateau observed in the Kratky-Debye plots (Fig. 3E). The syndecan ectodomains are thus disordered, flexible, and extended proteins in solution.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:32:54.679Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":19,"end":153,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03515r005","sample":[],"statement":[{"text":"The hydrodynamic radius (Rh) of the ectodomains, determined by size-exclusion chromatography-dynamic light scattering (SEC-DLS), ranged from 34.1 Å (ED-2) to 50.1 Å (ED-3), and their Rg/Rh ratio, that provides information about protein shape and compactness, ranged from 1.16 (ED-4 monomer) to 1.31 (ED-4 dimer) (Table 1). These values were far higher than those of globular proteins (0.778) and close to those reported for prolate ellipsoids (1.36–2.24) [34] (Table 1).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:32:52.882Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":19,"end":153,"reference_id":"34505054","reference_source":"pmid","reference_html":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans. <i> Gondelaud F, Bouakil M, Le Fèvre A, Miele AE, Chirot F, Duclos B, Liwo A, Ricard-Blum S. </i> Matrix Biol Plus, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0007184","ec_ontology":"ECO","ec_name":"protein mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03515r006","statement":[{"text":"Electrospray ionization-mass spectrometry (ESI-MS) in native conditions provides information on the variable degrees of compactness of IDPs. The charge state distributions (CSDs) determined by ESI-MS are related to the global compactness of proteins upon their transfer from solution to gas phase, the highest charge states corresponding to the most extended conformations [42]. The CSDs of the four ectodomains were trimodal, showing that the ectodomains of syndecans could adopt preferential conformations (Fig. 5A). Gaussian functions were fitted to the CSD envelopes to determine the relative proportions of the three major conformational ensembles. The most extended conformations (i.e. the highest charge states) were the most abundant for ED-1 (86 %), ED-2 (70 %) and ED-4 (85 %) but accounted for only 24 % for ED-3, in which the population with intermediate charge states predominated (Fig. 5B). Most compact conformations were found in minor amount for ED-1 (2 %), ED-2 (4 %), and ED-4 (8 %) and in larger amount for ED-3 (14 %).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-19T07:37:03.851Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":6,"released":"2023_12","sequence":"MAPARLFALLLFFVGGVAESIRETEVIDPQDLLEGRYFSGALPDDEDVVGPGQESDDFELSGSGDLDDLEDSMIGPEVVHPLVPLDNHIPERAGSGSQVPTEPKKLEENEVIPKRISPVEESEDVSNKVSMSSTVQGSNIFERTEVLAGCPEH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref50":"","uniref90":"","uniref100":"","genes":[{"name":{"value":"SDC4"}}],"disorder_content":0.8823529411764706,"disprot_consensus":{"full":[{"start":19,"end":153,"type":"D"}],"Structural state":[{"start":19,"end":153,"type":"D"}]}},{"disprot_id":"DP03516","acc":"P30328","creator":"fquaglia","date":"2021-10-20T15:26:30.424Z","features":{"pfam":[{"id":"PF04451","name":"Large eukaryotic DNA virus major capsid protein","start":215,"end":432},{"id":"PF16903","name":"Major capsid protein N-terminus","start":25,"end":212}],"gene3D":[]},"length":437,"name":"Major capsid protein","ncbi_taxon_id":10506,"organism":"Paramecium bursaria Chlorella virus 1","regions":[{"start":1,"end":24,"reference_id":"19889775","reference_source":"pmid","reference_html":"Structural studies of the Sputnik virophage. <i> Sun S, La Scola B, Bowman VD, Ryan CM, Whitelegge JP, Raoult D, Rossmann MG. </i> J Virol, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3KK5"},{"db":"EMDB","id":"1662"}],"region_id":"DP03516r001","statement":[{"text":"Unstructured N-terminal region of Major capsid protein of Paramecium bursaria Chlorella virus 1 (PBCV-1).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T16:01:37.106Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MAGGLSQLVAYGAQDVYLTGNPQITFFKTVYRRYTNFAIESIQQTINGSVGFGNKVSTQISRNGDLITDIVVEFVLTKGGNGGTTYYPAEELLQDVELEIGGQRIDKHYNDWFRTYDALFRMNDDRYNYRRMTDWVNNELVGAQKRFYVPLIFFFNQTPGLALPLIALQYHEVKLYFTLASQVQGVNYNGSSAIAGAAQPTMSVWVDYIFLDTQERTRFAQLPHEYLIEQLQFTGSETATPSATTQASQNIRLNFNHPTKYLAWNFNNPTNYGQYTALANIPGACSGAGTAAATVTTPDYGNTGTYNEQLAVLDSAKIQLNGQDRFATRKGSYFNKVQPYQSIGGVTPAGVYLYSFALKPAGRQPSGTCNFSRIDNATLSLTYKTCSIDATSPAAVLGNTETVTANTATLLTALNIYAKNYNVLRIMSGMGGLAYAN","taxonomy":["Viruses","Varidnaviria","Bamfordvirae","Nucleocytoviricota","Megaviricetes","Algavirales","Phycodnaviridae","Chlorovirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_P30328","uniref90":"UniRef90_P30328","uniref100":"UniRef100_P30328","genes":[{"olnNames":[{"value":"A430L"}]}],"disorder_content":0.05491990846681922,"disprot_consensus":{"full":[{"start":1,"end":24,"type":"D"}],"Structural state":[{"start":1,"end":24,"type":"D"}]}},{"disprot_id":"DP03517","acc":"P03437","creator":"vnugnes","date":"2021-10-21T09:40:15.874Z","features":{"pfam":[{"id":"PF00509","name":"Haemagglutinin","start":29,"end":566}],"gene3D":[]},"length":566,"name":"Hemagglutinin","ncbi_taxon_id":387139,"organism":"Influenza A virus (strain A/Aichi/2/1968 H3N2)","regions":[{"start":508,"end":520,"reference_id":"8072525","reference_source":"pmid","reference_html":"Structure of influenza haemagglutinin at the pH of membrane fusion. <i> Bullough PA, Hughson FM, Skehel JJ, Wiley DC. </i> Nature, 1994","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":5,"statements":[{"type":"Article","text":"At the low pH of endosomes, between pH 5 and pH 6, the fusion potential of the HA is activated2 4 in a process requiring structural changes in HA5,6 (reviewed in ref. I). We report here the results of crystallographic analyses of a soluble fragment from low-pH-treated HA which indicate that the fusion-pH-induced conformation is substantially different from the neutral pH conformation. "}]}],"cross_refs":[{"db":"PDB","id":"1HTM"}],"region_id":"DP03517r001","statement":[{"text":"Residues 141-175 , including helices G and H, which in BHA form a compact unit adjacent to the five-stranded β- sheet and part of helix D, adopt in TBHA2 a more extended, partially disordered conformation running antiparallel to the coiled coil (Fig. 3b-d).","type":"Article"},{"text":"The soluble trimeric fragment considered here, TBHA2 , is prepared from Influenza A virus hemagglutinin at pH 5, since bound virus is internalized by endocytosis and the pH of endosomes is between pH 5 and pH 6.","type":"Curator statement"},{"text":"An a-helix, H, in BHA (159-170) and five residues beyond it, 171-175, appear to be disordered in TBHA2.","type":"Article"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-04-05T10:11:11.517Z"}},{"start":508,"end":520,"reference_id":"8072525","reference_source":"pmid","reference_html":"Structure of influenza haemagglutinin at the pH of membrane fusion. <i> Bullough PA, Hughson FM, Skehel JJ, Wiley DC. </i> Nature, 1994","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"PDB","id":"1HTM"}],"region_id":"DP03517r002","statement":[{"text":"An a-helix, H, in BHA (159-170) and five residues beyond it, 171-175, appear to be disordered in TBHA2.","type":"Article"},{"text":"When incubated at the pH of fusion, BHA undergoes structural changes, two consequences of which are particularly important for investigations of the fusion-activated molecule. ","type":"Article"},{"text":"While TBHA2 is prepared from at pH 5, since bound virus is internalized by endocytosis and the pH of endosomes is between pH 5 and pH 6, BHA represents the Influenza A virus hemagglutinin at a physiological or cellular pH.","type":"Curator statement"}],"states_connection":[{"source":"DP03517r003","target":"DP03517r001"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-10T19:26:00.913Z"}},{"start":508,"end":520,"reference_id":"2329580","reference_source":"pmid","reference_html":"Refinement of the influenza virus hemagglutinin by simulated annealing. <i> Weis WI, Brünger AT, Skehel JJ, Wiley DC. </i> J Mol Biol, 1990","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":2,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7.5,"statements":[{"type":"Curator statement","text":"The BHA is prepared from Influenza A virus hemagglutinin at neutral pH."}]}],"region_id":"DP03517r003","statement":[{"text":"Residues 508-520 are folded in all the structures published.","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"2HMG"},{"db":"PDB","id":"3HMG"},{"db":"PDB","id":"4HMG"},{"db":"PDB","id":"5HMG"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-10T19:26:05.685Z"}}],"regions_counter":3,"released":"2021_12","sequence":"MKTIIALSYIFCLALGQDLPGNDNSTATLCLGHHAVPNGTLVKTITDDQIEVTNATELVQSSSTGKICNNPHRILDGIDCTLIDALLGDPHCDVFQNETWDLFVERSKAFSNCYPYDVPDYASLRSLVASSGTLEFITEGFTWTGVTQNGGSNACKRGPGSGFFSRLNWLTKSGSTYPVLNVTMPNNDNFDKLYIWGIHHPSTNQEQTSLYVQASGRVTVSTRRSQQTIIPNIGSRPWVRGLSSRISIYWTIVKPGDVLVINSNGNLIAPRGYFKMRTGKSSIMRSDAPIDTCISECITPNGSIPNDKPFQNVNKITYGACPKYVKQNTLKLATGMRNVPEKQTRGLFGAIAGFIENGWEGMIDGWYGFRHQNSEGTGQAADLKSTQAAIDQINGKLNRVIEKTNEKFHQIEKEFSEVEGRIQDLEKYVEDTKIDLWSYNAELLVALENQHTIDLTDSEMNKLFEKTRRQLRENAEEMGNGCFKIYHKCDNACIESIRNGTYDHDVYRDEALNNRFQIKGVELKSGYKDWILWISFAISCFLLCVVLLGFIMWACQRGNIRCNICI","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Polyploviricotina","Insthoviricetes","Articulavirales","Orthomyxoviridae","Alphainfluenzavirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_P03436","uniref90":"UniRef90_P03436","uniref100":"UniRef100_P03437","genes":[{"name":{"value":"HA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04072","url":"https://hamap.expasy.org/unirule/MF_04072"}}]}}],"disorder_content":0.022968197879858657,"disprot_consensus":{"full":[{"start":508,"end":520,"type":"T"}],"Structural state":[{"start":508,"end":520,"type":"D"}],"Structural transition":[{"start":508,"end":520,"type":"T"}]}},{"disprot_id":"DP03519","acc":"P27284","creator":"fquaglia","date":"2021-10-21T14:40:00.515Z","features":{"pfam":[{"id":"PF00943","name":"Alphavirus E2 glycoprotein","start":337,"end":737},{"id":"PF00944","name":"Alphavirus core protein","start":104,"end":261},{"id":"PF01563","name":"Alphavirus E3 glycoprotein","start":266,"end":323},{"id":"PF01589","name":"Alphavirus E1 glycoprotein","start":747,"end":1234}],"gene3D":[]},"length":1240,"name":"Structural polyprotein","ncbi_taxon_id":11022,"organism":"Eastern equine encephalitis virus (strain va33[ten broeck])","regions":[{"start":1,"end":80,"reference_id":"30540945","reference_source":"pmid","reference_html":"Cryo-EM Structures of Eastern Equine Encephalitis Virus Reveal Mechanisms of Virus Disassembly and Antibody Neutralization. <i> Hasan SS, Sun C, Kim AS, Watanabe Y, Chen CL, Klose T, Buda G, Crispin M, Diamond MS, Klimstra WB, Rossmann MG. </i> Cell Rep, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"6MX7"}],"region_id":"DP03519r001","statement":[{"text":"The capsid N-terminal domain (NTD) is disordered and binds the negatively charged alphavirus RNA genome (Owen and Kuhn, 1996).","type":"Introduction"},{"text":"Despite the identification of the NTD genome-binding sequence on the capsid protein more than 20 years ago (Owen and Kuhn, 1996), the structure of this domain has remained elusive, probably because the capsid NTD sequence (Met1-Ile116 in EEEV) shows features characteristic of intrinsically disordered proteins (Uversky, 2013) with high concentrations of basic residues Arg and Lys (27% of the sequence) and structure-disrupting Pro and Gly residues (26% of the sequence).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-02T08:56:49.198Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MFPYPTLNYPPMAPINPMAYRDPNPPRQVAPFRPPLAAQIEDLRRSIANLTLKQRAPNPPAGPPAKRKKPAPKPKPAQAKKKRPPPPAKKQKRKPKPGKRQRMCMKLESDKTFPIMLNGQVNGYACVVGGRVFKPLHVEGRIDNEQLAAIKLKKASIYDLEYGDVPQCMKSDTLQYTSDKPPGFYNWHHGAVQYENNRFTVPRGVGGKGDSGRPILDNKGRVVAIVLGGVNEGSRTALSVVTWNQKGVTVKDTPEGSEPWSLATVMCVLANITFPCDQPPCMPCCYEKNPHETLTMLEQNYDSRAYDQLLDAAVKCNARRTRRDLDTHFTQYKLARPYIADCPNCGHSRCDSPIAIEEVRGDAHAGVIRIQTSAMFGLKTDGVDLAYMSFMNGKTQKSIKIDNLHVRTSAPCSLVSHHGYYILAQCPPGDTVTVGFHDGPNRHTCTVAHKVEFRPVGREKYRHPPEHGVELPCNRYTHKRADQGHYVEMHQPGLVADHSLLSIHSAKVKITVPSGAQVKYYCKCPDVREGITSSDHTTTCTDVKQCRAYLIGNKKWVYNSGRLPRGEGDTFKGKLHVPFVPVKAKCIATLAPEPLVEHKHRTLILHLHPDHPTLLTTRSLGSDANPTRQWIERPTTVNFTVTGEGLEYTWGNHPPKRVWAQESGEGNPHGWPHEVVVYYYNRYPLTTIIGLCTCVAIIMVSCVHPCGSFAGLRNLCITPYKLAPNAQVPILLALLCCIKPTRADDTLQVLNYLWNNNQNFFWMQTLIPLAALIVCMRIVRCLFCCGPAFLLVCGAWAAAYEHTAVMPNKVGIPYKALVERPGYAPVHLQIQLVNTSIIPSTNLEYITCKYKTKVPSPVVKCCGATQCTSKPHPDYQCQVFTGVYPFMWGGAYCFCDTENTQMSEAYVERSEECSIDHAKAYKVHTGTVQAMVNITYGSVSWRSADVYVNGETPAKIGDAKLIIGPLSSAWSPFDNKVVVYGHEVYNYDFPEYGTGKAGSFGDLQSRTSTSNDLYANTNLKLQRPQAGIVHTPFTQAPSGFERWKRDKGAPLNDVAPFGCSIALEPLRAENCAVGSIPISIDIPDAAFTRISETPTVSDLECKITECTYASDFGGIATLPTNPVKQETVQFILHQVLQLLKRMTSPLLRAGSFTFHFSTANIHPAFKLQVCTSGVTCKGDCKPPKDHIVDYPAQHTESFTSAISATAWSWLKVLVGGTSAFIVLGLIATAVVALVLFFHRH","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Alsuviricetes","Martellivirales","Togaviridae","Alphavirus"],"dataset":["Viral proteins","RNA-binding proteins"],"uniref50":"UniRef50_P09592","uniref90":"UniRef90_P27284","uniref100":"UniRef100_P27284","genes":[],"disorder_content":0.06451612903225806,"disprot_consensus":{"full":[{"start":1,"end":80,"type":"D"}],"Structural state":[{"start":1,"end":80,"type":"D"}]}},{"disprot_id":"DP03520","acc":"P15183","creator":"fquaglia","date":"2021-10-21T14:50:17.713Z","features":{"pfam":[{"id":"PF00729","name":"Viral coat protein (S domain)","start":68,"end":260}],"gene3D":[]},"length":380,"name":"Capsid protein","ncbi_taxon_id":12143,"organism":"Cucumber necrosis virus","regions":[{"start":1,"end":59,"reference_id":"24006433","reference_source":"pmid","reference_html":"Atomic structure of Cucumber necrosis virus and the role of the capsid in vector transmission. <i> Li M, Kakani K, Katpally U, Johnson S, Rochon D, Smith TJ. </i> J Virol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"4LLF"}],"region_id":"DP03520r001","statement":[{"text":"Each capsid protein is comprised of three domains: the first ~60 residues at the N-terminal region (R), the shell (S) domain, and the protruding (P) domain (Fig. 2A). The first ~90 residues are disordered in the A and B subunits, while the first ~60 residues are disordered in the C subunit.","type":"Introduction"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-02T09:05:45.998Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MALVSRNNNMRTLAKLAAPLATAGTRTIVDNKEAIWNGVKWIWGKLPKGKKGKNGNGALIAHPQAFPGAIAAPISYAYAVKGRKPRFQTAKGSVRITHREYVSVLSGTNGEFLRNNGTGPNNDFSINPLNPFLFPWLVNIAANFDQYKFNSLRFEYVPLVNTTTNGRVALYFDKDSEDPGPDDRAALANYAHLSEISPWAITKLTVPTDNVKRFISDTSSGDPKLINLGQFGWVAYSGPTAELGDIFVEYTVDLFEAQPTSPLLESLFRESASSVQTRMGLPYFSLEVASATDLVWQARVPGTYVVTIIFNSTVGGLTPSISGGGTINSSFSVSTAGSSAYVANITIRVNANLSLSGLTGATNAQLFAVRAITENAVQVV","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Tolucaviricetes","Tolivirales","Tombusviridae","Procedovirinae","Tombusvirus"],"dataset":["Viral proteins","RNA-binding proteins"],"uniref50":"UniRef50_P15183","uniref90":"UniRef90_P15183","uniref100":"UniRef100_P15183","genes":[{"orfNames":[{"value":"ORF2"}]}],"disorder_content":0.15526315789473685,"disprot_consensus":{"full":[{"start":1,"end":59,"type":"D"}],"Structural state":[{"start":1,"end":59,"type":"D"}]}},{"disprot_id":"DP03521","acc":"Q58MU6","creator":"fquaglia","date":"2021-10-21T15:01:58.597Z","features":{"pfam":[{"id":"PF05996","name":"Ferredoxin-dependent bilin reductase","start":36,"end":230}],"gene3D":[]},"length":233,"name":"Phycoerythrobilin synthase","ncbi_taxon_id":268746,"organism":"Prochlorococcus phage P-SSM2","regions":[{"start":1,"end":20,"reference_id":"18662988","reference_source":"pmid","reference_html":"Phycoerythrobilin synthase (PebS) of a marine virus. Crystal structures of the biliverdin complex and the substrate-free form. <i> Dammeyer T, Hofmann E, Frankenberg-Dinkel N. </i> J Biol Chem, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2VCL"}],"region_id":"DP03521r001","statement":[{"text":"In all three structures, the N-terminal 20 residues were found to be disordered.","type":"Results"},{"text":"In the final model, the first 20 residues (18 in the case of chain A) have been omitted due to missing density.","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-02T09:03:01.516Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MTKNPRNNKPKKILDSSYKSKTIWQNYIDALFETFPQLEISEVWAKWDGGNVTKDGGDAKLTANIRTGEHFLKAREAHIVDPNSDIYNTILYPKTGADLPCFGMDLMKFSDKKVIIVFDFQHPREKYLFSVDGLPEDDGKYRFFEMGNHFSKNIFVRYCKPDEVDQYLDTFKLYLTKYKEMIDNNKPVGEDTTVYSDFDTYMTELDPVRGYMKNKFGEGRSEAFVNDFLFSYK","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Uroviricota","Caudoviricetes","Caudovirales","Myoviridae","Salacisavirus","Prochlorococcus virus PSSM2"],"dataset":["Viral proteins"],"uniref50":"UniRef50_Q58MU6","uniref90":"UniRef90_Q58MU6","uniref100":"UniRef100_Q58MU6","genes":[{"name":{"value":"pebS"},"orfNames":[{"value":"PSSM2_058"}]}],"disorder_content":0.08583690987124463,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"D"}],"Structural state":[{"start":1,"end":20,"type":"D"}]}},{"disprot_id":"DP03522","acc":"Q9QR71","creator":"vnugnes","date":"2021-10-22T15:08:03.787Z","features":{"pfam":[{"id":"PF21501","name":"Protein LANA1-like, DNA-binding domain","start":995,"end":1112}],"gene3D":[]},"length":1129,"name":"Protein LANA1","ncbi_taxon_id":868565,"organism":"Human herpesvirus 8 type P (isolate GK18)","regions":[{"start":1077,"end":1129,"reference_id":"27291650","reference_source":"pmid","reference_html":"Structural Mechanism of Transcriptional Regulator NSD3 Recognition by the ET Domain of BRD4. <i> Zhang Q, Zeng L, Shen C, Ju Y, Konuma T, Zhao C, Vakoc CR, Zhou MM. </i> Structure, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"cross_refs":[{"db":"DisProt","id":"DP02334r001"}],"region_id":"DP03522r001","statement":[{"text":"The LANA gene fragment used in this publication was derived from the Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus). IDR is 100% identical and corresponds to 1077-1129 region.","type":"Curator statement"}],"sequence_construct":"DTSKKVQMARLAWEASHPLAGNLQSSIVKFKKPLPLTQPGENQGPGDSPQEMT","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-27T08:51:21.098Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1098,"end":1116,"reference_id":"27291650","reference_source":"pmid","reference_html":"Structural Mechanism of Transcriptional Regulator NSD3 Recognition by the ET Domain of BRD4. <i> Zhang Q, Zeng L, Shen C, Ju Y, Konuma T, Zhao C, Vakoc CR, Zhou MM. </i> Structure, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"cross_refs":[{"db":"DisProt","id":"DP02334r003"},{"db":"BMRB","id":"26042"},{"db":"PDB","id":"2ND0"}],"region_id":"DP03522r002","statement":[{"text":"The LANA gene fragment used in this publication was derived from the Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus). IDR is 100% identical and corresponds to 1098-1116 region.","type":"Curator statement"}],"sequence_construct":"DTSKKVQMARLAWEASHPLAGNLQSSIVKFKKPLPLTQPGENQGPGDSPQEMT","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-27T08:51:30.550Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":1098,"end":1116,"reference_id":"27291650","reference_source":"pmid","reference_html":"Structural Mechanism of Transcriptional Regulator NSD3 Recognition by the ET Domain of BRD4. <i> Zhang Q, Zeng L, Shen C, Ju Y, Konuma T, Zhao C, Vakoc CR, Zhou MM. </i> Structure, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"cross_refs":[{"db":"DisProt","id":"DP02334r004"},{"db":"BMRB","id":"26042"},{"db":"PDB","id":"2ND0"}],"interaction_partner":[{"db":"UniProt","id":"O60885","partner_start":601,"partner_end":683}],"region_id":"DP03522r003","statement":[{"text":"The LANA gene fragment used in this publication was derived from the Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus). IDR is 100% identical and corresponds to 1098-1116 region.","type":"Curator statement"}],"sequence_construct":"DTSKKVQMARLAWEASHPLAGNLQSSIVKFKKPLPLTQPGENQGPGDSPQEMT","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-27T08:51:32.476Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1098,"end":1116,"reference_id":"27291650","reference_source":"pmid","reference_html":"Structural Mechanism of Transcriptional Regulator NSD3 Recognition by the ET Domain of BRD4. <i> Zhang Q, Zeng L, Shen C, Ju Y, Konuma T, Zhao C, Vakoc CR, Zhou MM. </i> Structure, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019058","term_name":"viral life cycle","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"cross_refs":[{"db":"DisProt","id":"DP02334r015"},{"db":"BMRB","id":"26042"},{"db":"PDB","id":"2ND0"}],"region_id":"DP03522r004","statement":[{"text":"The LANA gene fragment used in this publication was derived from the Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus). IDR is 100% identical and corresponds to 1098-1116 region.","type":"Curator statement"}],"sequence_construct":"DTSKKVQMARLAWEASHPLAGNLQSSIVKFKKPLPLTQPGENQGPGDSPQEMT","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-27T08:51:34.004Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A set of processes which all viruses follow to ensure survival; includes attachment and entry of the virus particle, decoding of genome information, translation of viral mRNA by host ribosomes, genome replication, and assembly and release of viral particles containing the genome.\" [ISBN:1555811272]","disprot_namespace":"Disorder function","term_is_binding":false}],"regions_counter":4,"released":"2023_06","sequence":"MAPPGMRLRSGRSTGAPLTRGSCRKRNRSPERCDLGDDLHLQPRRKHVADSVDGRECGPHTLPIPGSPTVFTSGLPAFVSSPTLPVAPIPSPAPATPLPPPALLPPVTTSSSPIPPSHPVSPGTTDTHSPSPALPPTQSPESSQRPPLSSPTGRPDSSTPMRPPPSQQTTPPHSPTTPPPEPPSKSSPDSLAPSTLRSLRKRRLSSPQGPSTLNPICQSPPVSPPRCDFANRSVYPPWATESPIYVGSSSDGDTPPRQPPTSPISIGSSSPSEGSWGDDTAMLVLLAEIAEEASKNEKECSENNQAGEDNGDNEISKESQVDKDDNDNKDDEEEQETDEEDEEDDEEDDEEDDEEDDEEDDEEDDEEDDEEEDEEEDEEEDEEEDEEEEEDEEDDDDEDNEDEEDDEEEDKKEDEEDGGDGNKTLSIQSSQQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQREPQQREPQQREPQQREPQQREPQQREPQQREPQQREPQQREPQQREPQQREPQQREPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQEPQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQQQDEQEQQDEQQQDEQQQQDEQEQQEEQEQQEEQQQDEQQQDEQQQDEQQQDEQEQQDEQQQDEQQQQDEQEQQEEQEQQEEQEQQEEQEQQEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQELEEQEQEQELEEVEEQEQEQEEQELEEVEEQEQEQEEQEEQELEEVEEQEEQELEEVEEQEEQELEEVEEQEQQGVEQQEQETVEEPIILHGSSSEDEMEVDYPVVSTHEQIASSPPGDNTPDDDPQPGPSREYRYVLRTSPPHRPGVRMRRVPVTHPKKPHPRYQQPPVPYRQIDDCPAKARPQHIFYRRFLGKDGRRDPKCQWKFAVIFWGNDPYGLKKLSQAFQFGGVKAGPVSCLPHPGPDQSPITYCVYVYCQNKDTSKKVQMARLAWEASHPLAGNLQSSIVKFKKPLPLTQPGENQGPGDSPQEMT","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Peploviricota","Herviviricetes","Herpesvirales","Herpesviridae","Gammaherpesvirinae","Rhadinovirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_Q9QR71","uniref90":"UniRef90_Q9QR71","uniref100":"UniRef100_Q9QR71","genes":[{"name":{"value":"LANA1"},"orfNames":[{"value":"ORF73"}]}],"disorder_content":0.046944198405668734,"disprot_consensus":{"full":[{"start":1077,"end":1097,"type":"D"},{"start":1098,"end":1116,"type":"T"},{"start":1117,"end":1129,"type":"D"}],"Structural state":[{"start":1077,"end":1129,"type":"D"}],"Structural transition":[{"start":1098,"end":1116,"type":"T"}],"Molecular function":[{"start":1098,"end":1116,"type":"F"}],"Biological process":[{"start":1098,"end":1116,"type":"F"}]}},{"disprot_id":"DP03523","acc":"C4LQ26","creator":"vnugnes","date":"2021-10-25T11:55:41.093Z","features":{"pfam":[{"id":"PF00506","name":"Influenza virus nucleoprotein","start":38,"end":557}],"gene3D":[]},"length":560,"name":"Nucleoprotein","ncbi_taxon_id":554810,"organism":"Influenza B virus","regions":[{"start":127,"end":146,"reference_id":"22496219","reference_source":"pmid","reference_html":"Structural basis for RNA binding and homo-oligomer formation by influenza B virus nucleoprotein. <i> Ng AK, Lam MK, Zhang H, Liu J, Au SW, Chan PK, Wang J, Shaw PC. </i> J Virol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3TJ0"}],"region_id":"DP03523r001","statement":[{"text":"Only aa 125, 126, and 147 to 149 were visible in the density map, showing that this loop is highly flexible.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-25T12:21:56.685Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":70,"reference_id":"22496219","reference_source":"pmid","reference_html":"Structural basis for RNA binding and homo-oligomer formation by influenza B virus nucleoprotein. <i> Ng AK, Lam MK, Zhang H, Liu J, Au SW, Chan PK, Wang J, Shaw PC. </i> J Virol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3TJ0"}],"region_id":"DP03523r002","statement":[{"text":"The electron densities for the first 71 residues of BNP were not visible, indicating that this N-terminal region of the protein is highly flexible.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-25T12:21:54.454Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":70,"reference_id":"22496219","reference_source":"pmid","reference_html":"Structural basis for RNA binding and homo-oligomer formation by influenza B virus nucleoprotein. <i> Ng AK, Lam MK, Zhang H, Liu J, Au SW, Chan PK, Wang J, Shaw PC. </i> J Virol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3TJ0"}],"region_id":"DP03523r003","statement":[{"text":"The electron densities for the first 71 residues of BNP were not visible, indicating that this N-terminal region of the protein is highly flexible.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-25T12:22:11.355Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":127,"end":146,"reference_id":"22496219","reference_source":"pmid","reference_html":"Structural basis for RNA binding and homo-oligomer formation by influenza B virus nucleoprotein. <i> Ng AK, Lam MK, Zhang H, Liu J, Au SW, Chan PK, Wang J, Shaw PC. </i> J Virol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03523r004","statement":[{"text":"Deletion of this loop in BNP resulted in a 14-fold decrease in the RNA-binding affinity, which is significantly more dramatic than the 6.4-fold decrease in the flexible loop-deleted ANP equivalent (21), implying that this loop in BNP contributes more to RNA binding.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-25T12:22:01.929Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":127,"end":146,"reference_id":"22496219","reference_source":"pmid","reference_html":"Structural basis for RNA binding and homo-oligomer formation by influenza B virus nucleoprotein. <i> Ng AK, Lam MK, Zhang H, Liu J, Au SW, Chan PK, Wang J, Shaw PC. </i> J Virol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019058","term_name":"viral life cycle","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03523r005","statement":[{"text":"Deletion of this loop in BNP resulted in a 14-fold decrease in the RNA-binding affinity, which is significantly more dramatic than the 6.4-fold decrease in the flexible loop-deleted ANP equivalent (21), implying that this loop in BNP contributes more to RNA binding.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-25T12:22:09.729Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A set of processes which all viruses follow to ensure survival; includes attachment and entry of the virus particle, decoding of genome information, translation of viral mRNA by host ribosomes, genome replication, and assembly and release of viral particles containing the genome.\" [ISBN:1555811272]","disprot_namespace":"Disorder function","term_is_binding":false}],"regions_counter":5,"released":"2021_12","sequence":"MSNMDIDGINTGTIDKTPEEITSGTSGTTRPIIRPATLAPPSNKRTRNPSPERATTSSEDDVGRKTQKKQTPTEIKKSVYNMVVKLGEFYNQMMVKAGLNDDMERNLIQNAHAVERILLAATDDKKTEFQKKKNARDVKEGREEIDHNKTGGTFYKMVRDDKTIYFSPIRITFLKEEVKTMYKTTMGSDGFSGLNHIMIGHSQMNDVCFQRSKALKRVGLDPSLISTFAGSTIPRRSGATGVAIKGGGTLVAEAIRFIGRAMADRGLLRDIKAKTAYEKILLNLKNKCSAPQQKALVDQVIGSRNPGIADIEDLTLLARSMVVVRPSVASKVVLPISIYAKIPQLGFNVEEYSMVGYEAMALYNMATPVSILRMGDDAKDKSQLFFMSCFGAAYEDLRVLSALTGTEFKPRSALKCKGFHVPAKEQVEGMGAALMSIKLQFWAPMTRSGGNEVGGDGGSGQISCSPVFAVERPIALSKQAVRRMLSMNIEGRDADVKGNLLKMMNDSMAKKTSGNAFIGKKMFQISDKNKTNPVEIPIKQTIPNFFFGRDTAEDYDDLDY","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Polyploviricotina","Insthoviricetes","Articulavirales","Orthomyxoviridae","Betainfluenzavirus"],"dataset":["Viral proteins","RNA-binding proteins"],"uniref50":"UniRef50_P04665","uniref90":"UniRef90_P04665","uniref100":"UniRef100_X2E2I3","genes":[{"name":{"value":"NP","evidences":[{"code":"ECO:0000256","source":{"name":"HAMAP-Rule","id":"MF_04070","url":"https://hamap.expasy.org/unirule/MF_04070"}},{"code":"ECO:0000256","source":{"name":"RuleBase","id":"RU361251","url":"https://www.uniprot.org/unirule/RU361251"}},{"code":"ECO:0000313","source":{"name":"EMBL","id":"ACR15715.1","url":"https://www.ebi.ac.uk/ena/browser/view/ACR15715.1"}}]}}],"disorder_content":0.16071428571428573,"disprot_consensus":{"full":[{"start":1,"end":70,"type":"D"},{"start":127,"end":146,"type":"D"}],"Structural state":[{"start":1,"end":70,"type":"D"},{"start":127,"end":146,"type":"D"}],"Disorder function":[{"start":1,"end":70,"type":"F"}],"Molecular function":[{"start":127,"end":146,"type":"F"}],"Biological process":[{"start":127,"end":146,"type":"F"}]}},{"disprot_id":"DP03524","acc":"A0A140DLX4","creator":"jbergier","date":"2021-10-28T10:00:22.184Z","features":{"pfam":[{"id":"PF00869","name":"Flavivirus glycoprotein, central and dimerisation domains","start":292,"end":592},{"id":"PF00948","name":"Flavivirus non-structural Protein NS1","start":797,"end":1148},{"id":"PF00949","name":"Peptidase S7, Flavivirus NS3 serine protease","start":1519,"end":1669},{"id":"PF00972","name":"Flavivirus RNA-directed RNA polymerase, fingers and palm domains","start":2772,"end":3222},{"id":"PF01002","name":"Flavivirus non-structural protein NS2B","start":1378,"end":1502},{"id":"PF01003","name":"Flavivirus capsid protein C","start":6,"end":122},{"id":"PF01004","name":"Flavivirus envelope glycoprotein M","start":217,"end":290},{"id":"PF01005","name":"Flavivirus non-structural protein NS2A","start":1158,"end":1280},{"id":"PF01349","name":"Flavivirus non-structural protein NS4B","start":2270,"end":2510},{"id":"PF01350","name":"Flavivirus non-structural protein NS4A","start":2126,"end":2268},{"id":"PF01570","name":"Flavivirus polyprotein propeptide","start":130,"end":214},{"id":"PF01728","name":"FtsJ-like methyltransferase","start":2575,"end":2744},{"id":"PF02832","name":"Flavivirus glycoprotein, immunoglobulin-like domain","start":594,"end":692},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1687,"end":1833},{"id":"PF20483","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","start":3226,"end":3389},{"id":"PF20907","name":"Flavivirus NS3 helicase, C-terminal helical domain","start":1975,"end":2117},{"id":"PF21659","name":"Flavivirus envelope glycoprotein E, stem/anchor domain","start":695,"end":789}],"gene3D":[]},"length":3423,"name":"Core protein","ncbi_taxon_id":64320,"organism":"Zika virus","regions":[{"start":1503,"end":1516,"reference_id":"27386922","reference_source":"pmid","reference_html":"Crystal structure of Zika virus NS2B-NS3 protease in complex with a boronate inhibitor. <i> Lei J, Hansen G, Nitsche C, Klein CD, Zhang L, Hilgenfeld R. </i> Science, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03524r001","statement":[{"text":"The PDB shows disorder in the region 1503-1516. ","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"5LC0"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-29T13:44:52.098Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1421,"end":1466,"reference_id":"29080786","reference_source":"pmid","reference_html":"Molecular Recognition Features in Zika Virus Proteome. <i> Mishra PM, Uversky VN, Giri R. </i> J Mol Biol, 2018","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03524r002","statement":[{"text":"We have taken the longest MoRF region of NS2B for this aim. Amino acid sequence of synthesized peptide of NS2B protein residues 49–95 from NS2B–NS3 protease (PDB ID 5LC0 [44]) is [NH2]VDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEDDGPPMA[COOH]. This synthesized peptide contains our region of interest that is MoRF region (56–78) of the sequence [NH2]AGDITWEKDAEVTGNSPRLDVAL[COOH].","type":"Methods"},{"text":"Figure 8 represents the observed far-UV CD spectrum of this peptide and shows that it corresponds to the CD spectrum of a highly disordered, random coil-like polypeptide. This is evidenced by an intensive minimum in the vicinity of 200 nm and the absence of a strong negative signal above 210 nm, which is characteristic of α-helix or β-sheet secondary structure. Therefore, the far-UV CD spectrum of this synthesized NS2B peptide shown in Fig. 8 illustrates the absence of ordered secondary structure, confirming its IDPR nature.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-29T13:44:51.043Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2023_06","sequence":"MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEIIKKFKKDLAAMLRIINARKEKKRRGADTSVGIVGLLLTTAMAAEVTRRGSAYYMYLDRNDAGEAISFPTTLGMNKCYIQIMDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGCVTVMAQDKPTVDIELVSTTVSNMAEVRSYCYEATISDIASDSRCPTQGEAYLDKQSDTQYVCKRTLVDRGWGNGCGLFGKGSLVTCAKFACSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIVNDTGHETDENRAKVEITPNSPRAEATLGGFGSLGLDCEPRTGLDFSDLYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKEALVEFKDAHAKRQTAVVLGSQEGAVHTALAGALEAEMDGAKGRLSSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGSTIGKAFEATVRGAKRMAVLGDTAWDFGSVGGALNSLGKGIHQIFGAAFKSLFGGMSWFSQILIGTLLMWLGLNTKNGSISLMCLALGGVLIFLSTAVSADVGCSVDFSKKETRCGTGVFVYNDVEAWRDRYKYHPDSPRRLAAAVKQAWEDGICGISSVSRMENIMWRSVEGELNAILEENGVQLTVVVGSVKNPMWRGPQRLPVPVNELPHGWKAWGKSYFVRAAKTNNSFVVDGDTLKECPLKHRAWNSFLVEDHGFGVFHTSVWLKVREDYSLECDPAVIGTAVKEKEAVHSDLGYWIESEKNDTWRLKRAHLIEMKTCEWPKSHTLWTDGIEESDLIIPKSLAGPLSHHNTREGYRTQMKGPWHSEELEIRFEECPGTKVHVEETCGTRGPSLRSTTASGRVIEEWCCRECTMPPLSFRAKDGCWYGMEIRPRKEPESNLVRSVVTAGSTDHMDHFSLGVLVILLMVQEGLKKRMTTKIIISTSMAVLVAMILGGFSMSDLAKLAILMGATFAEMNTGGDVAHLALIAAFKVRPALLVSFIFRANWTPRESMLLALASCLLQTAISALEGDLMVLINGFALAWLAIRAMVVPRTDNITLAILAALTPLARGTLLVAWRAGLATCGGFMLLSLKGKGSVKKNLPFVMALGLTAVRLVDPINVVGLLLLTRSGKRSWPPSEVLTAVGLICALAGGFAKADIEMAGPIAAVGLLIVSYVVSGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEDDGPPMREIILKVVLMTICGMNPIAIPFAAGAWYVYVKTGKRSGALWDVPAPKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGSALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWDGHSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGRREEETPVECFEPSMLKKKQLTVLDLHPGAGKTRRVLPEIVREAIKTRLRTVILAPTRVVAAEMEEALRGLPVRYMTTAVNVTHSGTEIVDLMCHATFTSRLLQPIRVPNYNLYIMDEAHFTDPSSIAARGYISTRVEMGEAAAIFMTATPPGTRDAFPDSNSPIMDTEVEVPERAWSSGFDWVTDHSGKTVWFVPSVRNGNEIAACLTKAGKRVIQLSRKTFETEFQKTKHQEWDFVVTTDISEMGANFKADRVIDSRRCLKPVILDGERVILAGPMPVTHASAAQRRGRIGRNPNKPGDEYLYGGGCAETDEDHAHWLEARMLLDNIYLQDGLIASLYRPEADKVAAIEGEFKLRTEQRKTFVELMKRGDLPVWLAYQVASAGITYTDRRWCFDGTTNNTIMEDSVPAEVWTRHGEKRVLKPRWMDARVCSDHAALKSFKEFAAGKRGAAFGVMEALGTLPGHMTERFQEAIDNLAVLMRAETGSRPYKAAAAQLPETLETIMLLGLLGTVSLGIFFVLMRNKGIGKMGFGMVTLGASAWLMWLSEIEPARIACVLIVVFLLLVVLIPEPEKQRSPQDNQMAIIIMVAVGLLGLITANELGWLERTKSDLSHLMGRREEGATIGFSMDIDLRPASAWAIYAALTTFITPAVQHAVTTSYNNYSLMAMATQAGVLFGMGKGMPFYAWDFGVPLLMIGCYSQLTPLTLIVAIILLVAHYMYLIPGLQAAAARAAQKRTAAGIMKNPVVDGIVVTDIDTMTIDPQVEKKMGQVLLIAVAVSSAILSRTAWGWGEAGALITAATSTLWEGSPNKYWNSSTATSLCNIFRGSYLAGASLIYTVTRNAGLVKRRGGGTGETLGEKWKARLNQMSALEFYSYKKSGITEVCREEARRALKDGVATGGHAVSRGSAKLRWLVERGYLQPYGKVIDLGCGRGGWSYYAATIRKVQEVKGYTKGGPGHEEPVLVQSYGWNIVRLKSGVDVFHMAAEPCDTLLCDIGESSSSPEVEEARTLRVLSMVGDWLEKRPGAFCIKVLCPYTSTMMETLERLQRRYGGGLVRVPLSRNSTHEMYWVSGAKSNTIKSVSTTSQLLLGRMDGPRRPVKYEEDVNLGSGTRAVVSCAEAPNMKIIGDRIERIRSEHAETWFFDENHPYRTWAYHGSYEAPTQGSASSLINGVVRLLSKPWDVVTGVTGIAMTDTTPYGQQRVFKEKVDTRVPDPQEGTRQVMSMVSSWLWKELGKHKRPRVCTKEEFINKVRSNAALGAIFEEEKEWKTAVEAVNDPRFWALVDKEREHHLRGECQSCVYNMMGKREKKQGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMGRENSGGGVEGLGLQRLGYVLEEMSRIPGGRMYADDTAGWDTRISRFDLENEALITNQMEKGHRALALAIIKYTYQNKVVKVLRPAEKGKTVMDIISRQDQRGSGQVVTYALNTFTNLVVQLIRNMEAEEVLEMQDLWLLRRSEKVTNWLQSNGWDRLKRMAVSGDDCVVKPIDDRFAHALRFLNDMGKVRKDTQEWKPSTGWDNWEEVPFCSHHFNKLHLKDGRSIVVPCRHQDELIGRARVSPGAGWSIRETACLAKSYAQMWQLLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLVVWNRVWIEENDHMEDKTPVTKWTDIPYLGKREDLWCGSLIGHRPRTTWAENIKNTVNMVRRIIGDEEKYMDYLSTQVRYLGEEGSTPGVL","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Flavivirus"],"dataset":["Viral proteins","Neglected tropical diseases proteins"],"uniref50":"UniRef50_P06935","uniref90":"UniRef90_Q32ZE1","uniref100":"UniRef100_A0A140DLX4","genes":[],"disorder_content":0.017528483786152498,"disprot_consensus":{"full":[{"start":1421,"end":1466,"type":"D"},{"start":1503,"end":1516,"type":"D"}],"Structural state":[{"start":1421,"end":1466,"type":"D"},{"start":1503,"end":1516,"type":"D"}]}},{"disprot_id":"DP03525","acc":"Q8JUX6","creator":"jssuarez","date":"2021-11-02T13:12:21.081Z","features":{"pfam":[{"id":"PF00978","name":"RNA dependent RNA polymerase","start":2015,"end":2461},{"id":"PF01443","name":"Viral superfamily 1 RNA helicase core domain","start":719,"end":957},{"id":"PF01660","name":"Viral methyltransferase","start":16,"end":378},{"id":"PF01661","name":"Macro domain","start":1353,"end":1452},{"id":"PF01707","name":"Peptidase family C9","start":964,"end":1165},{"id":"PF20852","name":"Non-structural protein 3, zinc-binding domain","start":1501,"end":1658},{"id":"PF20896","name":"Tomato mosaic virus helicase, N-terminal domain","start":554,"end":711}],"gene3D":[]},"length":2474,"name":"Polyprotein P1234","ncbi_taxon_id":371094,"organism":"Chikungunya virus (strain S27-African prototype)","regions":[{"start":1728,"end":1744,"reference_id":"27268056","reference_source":"pmid","reference_html":"Structural Basis of the High Affinity Interaction between the Alphavirus Nonstructural Protein-3 (nsP3) and the SH3 Domain of Amphiphysin-2. <i> Tossavainen H, Aitio O, Hellman M, Saksela K, Permi P. </i> J Biol Chem, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03525r001","statement":[{"text":"A, Ensemble of 20 lowest-energy structures. Disordered residues Ser-1728–The-1729, Gly-1740–Thr-1744 of CHIKV, and the side chain of Arg-1738 have been left out for clarity.","type":"Figure"},{"text":"The partially disordered state of nsP3 arginines offers a large binding epitope while minimizing entropic penalty upon binding to amp-SH3.","type":"Discussion"}],"cross_refs":[{"db":"PDB","id":"5I22"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-03T09:08:14.627Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1728,"end":1744,"reference_id":"27268056","reference_source":"pmid","reference_html":"Structural Basis of the High Affinity Interaction between the Alphavirus Nonstructural Protein-3 (nsP3) and the SH3 Domain of Amphiphysin-2. <i> Tossavainen H, Aitio O, Hellman M, Saksela K, Permi P. </i> J Biol Chem, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"cross_refs":[{"db":"PDB","id":"5I22"}],"region_id":"DP03525r002","statement":[{"text":"Further analysis of CHIKV nsP3 binding using ITC (Table 1 and Fig. 3B) showed that the affinity of this viral peptide to amp-SH3 is unusually high, with a Kd of 0.024 μm, clearly among the strongest found for SH3 domains (18).","type":"Results"},{"text":"The partially disordered state of nsP3 arginines offers a large binding epitope while minimizing entropic penalty upon binding to amp-SH3.","type":"Discussion"}],"interaction_partner":[{"db":"UniProt","id":"O00499","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-03T09:35:55.395Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":5,"released":"2023_06","sequence":"MDPVYVDIDADSAFLKALQRAYPMFEVEPRQVTPNDHANARAFSHLAIKLIEQEIDPDSTILDIGSAPARRMMSDRKYHCVCPMRSAEDPERLANYARKLASAAGKVLDRNISGKIGDLQAVMAVPDTETPTFCLHTDVSCRQRADVAIYQDVYAVHAPTSLYHQAIKGVRLAYWVGFDTTPFMYNAMAGAYPSYSTNWADEQVLKAKNIGLCSTDLTEGRRGKLSIMRGKKLEPCDRVLFSVGSTLYPESRKLLKSWHLPSVFHLKGKLSFTCRCDTVVSCEGYVVKRITMSPGLYGKTTGYAVTHHADGFLMCKTTDTVDGERVSFSVCTYVPATICDQMTGILATEVTPEDAQKLLVGLNQRIVVNGRTQRNTNTMKNYMIPVVAQAFSKWAKECRKDMEDEKLLGVRERTLTCCCLWAFKKQKTHTVYKRPDTQSIQKVQAEFDSFVVPSLWSSGLSIPLRTRIKWLLSKVPKTDLTPYSGDAQEARDAEKEAEEEREAELTLEALPPLQAAQEDVQVEIDVEQLEDRAGAGIIETPRGAIKVTAQPTDHVVGEYLVLSPQTVLRSQKLSLIHALAEQVKTCTHSGRAGRYAVEAYDGRVLVPSGYAISPEDFQSLSESATMVYNEREFVNRKLHHIAMHGPALNTDEESYELVRAERTEHEYVYDVDQRRCCKKEEAAGLVLVGDLTNPPYHEFAYEGLKIRPACPYKIAVIGVFGVPGSGKSAIIKNLVTRQDLVTSGKKENCQEITTDVMRQRGLEISARTVDSLLLNGCNRPVDVLYVDEAFACHSGTLLALIALVRPRQKVVLCGDPKQCGFFNMMQMKVNYNHNICTQVYHKSISRRCTLPVTAIVSSLHYEGKMRTTNEYNKPIVVDTTGSTKPDPGDLVLTCFRGWVKQLQIDYRGHEVMTAAASQGLTRKGVYAVRQKVNENPLYASTSEHVNVLLTRTEGKLVWKTLSGDPWIKTLQNPPKGNFKATIKEWEVEHASIMAGICSHQMTFDTFQNKANVCWAKSLVPILETAGIKLNDRQWSQIIQAFKEDKAYSPEVALNEICTRMYGVDLDSGLFSKPLVSVYYADNHWDNRPGGKMFGFNPEAASILERKYPFTKGKWNINKQICVTTRRIEDFNPTTNIIPANRRLPHSLVAEHRPVKGERMEWLVNKINGHHVLLVSGCSLALPTKRVTWVAPLGVRGADYTYNLELGLPATLGRYDLVVINIHTPFRIHHYQQCVDHAMKLQMLGGDSLRLLKPGGSLLIRAYGYADRTSERVICVLGRKFRSSRALKPPCVTSNTEMFFLFSNFDNGRRNFTTHVMNNQLNAAFVGQATRAGCAPSYRVKRMDIAKNDEECVVNAANPRGLPGDGVCKAVYKKWPESFKNSATPVGTAKTVMCGTYPVIHAVGPNFSNYSESEGDRELAAAYREVAKEVTRLGVNSVAIPLLSTGVYSGGKDRLTQSLNHLFTAMDSTDADVVIYCRDKEWEKKISEAIQMRTQVELLDEHISIDCDVVRVHPDSSLAGRKGYSTTEGALYSYLEGTRFHQTAVDMAEIYTMWPKQTEANEQVCLYALGESIESIRQKCPVDDADASSPPKTVPCLCRYAMTPERVTRLRMNHVTSIIVCSSFPLPKYKIEGVQKVKCSKVMLFDHNVPSRVSPREYRPSQESVQEASTTTSLTHSQFDLSVDGKILPVPSDLDADAPALEPALDDGAIHTLPSATGNLAAVSDWVMSTVPVAPPRRRRGRNLTVTCDEREGNITPMASVRFFRAELCPVVQETAETRDTAMSLQAPPSTATELSHPPISFGAPSETFPITFGDFNEGEIESLSSELLTFGDFLPGEVDDLTDSDWSTCSDTDDELRLDRAGGYIFSSDTGPGHLQQKSVRQSVLPVNTLEEVHEEKCYPPKLDEAKEQLLLKKLQESASMANRSRYQSRKVENMKATIIQRLKRGCRLYLMSETPKVPTYRTTYPAPVYSPPINVRLSNPESAVAACNEFLARNYPTVSSYQITDEYDAYLDMVDGSESCLDRATFNPSKLRSYPKQHAYHAPSIRSAVPSPFQNTLQNVLAAATKRNCNVTQMRELPTLDSAVFNVECFKKFACNQEYWEEFAASPIRITTENLTTYVTKLKGPKAAALFAKTHNLLPLQEVPMDRFTVDMKRDVKVTPGTKHTEERPKVQVIQAAEPLATAYLCGIHRELVRRLNAVLLPNVHTLFDMSAEDFDAIIAAHFKPGDTVLETDIASFDKSQDDSLALTALMLLEDLGVDHSLLDLIEAAFGEISSCHLPTGTRFKFGAMMKSGMFLTLFVNTLLNITIASRVLEDRLTKSACAAFIGDDNIIHGVVSDELMAARCATWMNMEVKIIDAVVSQKAPYFCGGFILHDIVTGTACRVADPLKRLFKLGKPLAAGDEQDEDRRRALADEVVRWQRTGLIDELEKAVYSRYEVQGISVVVMSMATFASSRSNFEKLRGPVVTLYGGPK","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Alsuviricetes","Martellivirales","Togaviridae","Alphavirus"],"dataset":["Viral proteins","Neglected tropical diseases proteins","RNA-binding proteins"],"uniref50":"UniRef50_P08411","uniref90":"UniRef90_Q8JUX6","uniref100":"UniRef100_Q8JUX6","genes":[],"disorder_content":0.0068714632174616,"disprot_consensus":{"full":[{"start":1728,"end":1744,"type":"D"}],"Structural state":[{"start":1728,"end":1744,"type":"D"}],"Molecular function":[{"start":1728,"end":1744,"type":"F"}]}},{"disprot_id":"DP03526","acc":"P12504","creator":"vnugnes","date":"2021-11-02T14:42:41.019Z","features":{"pfam":[{"id":"PF00559","name":"Retroviral Vif (Viral infectivity) protein","start":1,"end":192}],"gene3D":[]},"length":192,"name":"Virion infectivity factor","ncbi_taxon_id":11698,"organism":"Human immunodeficiency virus type 1 group M subtype B (isolate NY5)","regions":[{"start":157,"end":176,"reference_id":"18562529","reference_source":"pmid","reference_html":"Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly. <i> Stanley BJ, Ehrlich ES, Short L, Yu Y, Xiao Z, Yu XF, Xiong Y. </i> J Virol, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3DCG"}],"region_id":"DP03526r001","statement":[{"text":"Clear electron density was observed in the 2Fo-Fc map for Vif residues 140 to 155 before their inclusion in the model. These residues correspond to the Vif BC-box helix that includes the consensus sequence of SLQYLA. The C terminus of the Vif construct, containing the Cullin box, was disordered and not observed in the crystal structure.","type":"Results"},{"text":"According to the PDB 157-176 are the correct boundaries for the disordered region.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T12:32:12.013Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":155,"end":172,"reference_id":"24225024","reference_source":"pmid","reference_html":"Insight into the HIV-1 Vif SOCS-box-ElonginBC interaction. <i> Lu Z, Bergeron JR, Atkinson RA, Schaller T, Veselkov DA, Oregioni A, Yang Y, Matthews SJ, Malim MH, Sanderson MR. </i> Open Biol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"construct_alterations":[{"term_namespace":"Tag","term_name":"other tags","term_id":"MI:0507","position":"N-terminal","statements":[{"type":"Results","text":"In order to address the challenges associated with Vif insolubility, we N-terminally fused the Vif SOCS-box to a solubility-enhancement tag that does not increase the molecular weight substantially and therefore is suitable for NMR studies [57]."}]}],"cross_refs":[{"db":"BMRB","id":"19333"},{"db":"PDB","id":"2MA9"}],"region_id":"DP03526r002","statement":[{"text":"The fact that the T1 values of BC-box are consistently the same over the span of residues 144–154 indicates that this region is less dynamic and tumbles isotropically compared with the rest residues of the SOCS-box. However, it is of note that the N-terminal-fused tag attached to this region may also contribute to its limited motion.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-04T12:32:11.175Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MENRWQVMIVWQVDRMRINTWKRLVKHHMYISRKAKDWFYRHHYESTNPKISSEVHIPLGDAKLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPDLADQLIHLHYFDCFSESAIRNTILGRIVSPRCEYQAGHNKVGSLQYLALAALIKPKQIKPPLPSVRKLTEDRWNKPQKTKGHRGSHTMNGH","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"dataset":["Viral proteins","RNA-binding proteins"],"uniref50":"UniRef50_P12504","uniref90":"UniRef90_P12504","uniref100":"UniRef100_P12504","genes":[{"name":{"value":"vif","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04081","url":"https://hamap.expasy.org/unirule/MF_04081"}}]}}],"disorder_content":0.11458333333333333,"disprot_consensus":{"full":[{"start":155,"end":176,"type":"D"}],"Structural state":[{"start":155,"end":176,"type":"D"}]}},{"disprot_id":"DP03528","acc":"P69718","creator":"jbergier","date":"2021-11-04T13:07:52.350Z","features":{"pfam":[{"id":"PF00424","name":"REV protein (anti-repression trans-activator protein)","start":1,"end":91}],"gene3D":[]},"length":116,"name":"Protein Rev","ncbi_taxon_id":11707,"organism":"Human immunodeficiency virus type 1 group M subtype B (isolate HXB3)","regions":[{"start":34,"end":50,"reference_id":"23972852","reference_source":"pmid","reference_html":"The arginine-rich RNA-binding motif of HIV-1 Rev is intrinsically disordered and folds upon RRE binding. <i> Casu F, Duggan BM, Hennig M. </i> Biophys J, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03528r001","statement":[{"text":"To obtain residue-specific information regarding the Rev ARM peptide, we recorded 1HN,15N-HSQC spectra (Fig. 2). In aqueous solution, the peptide shows little dispersion of the resonances (Fig. 2 B), indicative of an unfolded peptide and in accordance with the CD data.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-11T15:59:22.632Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":34,"end":50,"reference_id":"23972852","reference_source":"pmid","reference_html":"The arginine-rich RNA-binding motif of HIV-1 Rev is intrinsically disordered and folds upon RRE binding. <i> Casu F, Duggan BM, Hennig M. </i> Biophys J, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03528r002","statement":[{"text":"CD spectra of the Rev ARM peptide in physiological buffer exhibited a minimum around 200 nm, typical of an unfolded state (Fig. 1 A).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-11T15:59:21.228Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":34,"end":50,"reference_id":"23972852","reference_source":"pmid","reference_html":"The arginine-rich RNA-binding motif of HIV-1 Rev is intrinsically disordered and folds upon RRE binding. <i> Casu F, Duggan BM, Hennig M. </i> Biophys J, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03528r003","statement":[{"text":"Fig. 5 B shows that the [1HN],15N hetNOE values for Rev ARM in aqueous solution at pH 7.4 average 0.47 for residues T34–R50, consistent with a disordered peptide. In contrast, the hetNOEs of the Rev ARM peptide in complex with RRE StemIIB average 0.83 for residues T34–R50, and in 50% TFE average 0.77 for residues T34–R50. These higher hetNOE values indicate higher backbone rigidity and are typical of a well-ordered secondary structure.","type":"Results"},{"text":"RRE StemIIB it's the RNA binding Rev ARM.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-12T09:59:29.119Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":34,"end":50,"reference_id":"23972852","reference_source":"pmid","reference_html":"The arginine-rich RNA-binding motif of HIV-1 Rev is intrinsically disordered and folds upon RRE binding. <i> Casu F, Duggan BM, Hennig M. </i> Biophys J, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP03528r004","statement":[{"text":"Fig. 5 B shows that the [1HN],15N hetNOE values for Rev ARM in aqueous solution at pH 7.4 average 0.47 for residues T34–R50, consistent with a disordered peptide. In contrast, the hetNOEs of the Rev ARM peptide in complex with RRE StemIIB average 0.83 for residues T34–R50, and in 50% TFE average 0.77 for residues T34–R50. These higher hetNOE values indicate higher backbone rigidity and are typical of a well-ordered secondary structure.","type":"Results"},{"text":"RRE StemIIB it's the RNA binding Rev ARM.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-12T09:59:26.625Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":34,"end":50,"reference_id":"18922466","reference_source":"pmid","reference_html":"A solution to limited genomic capacity: using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA. <i> Daugherty MD, D'Orso I, Frankel AD. </i> Mol Cell, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03528r005","statement":[{"text":"We further characterized the differences in IA and IIB binding modes using amide proton chemical shifts from 15N HSQC NMR spectra to monitor changes in the peptide-RNA interfaces. There is little peak dispersion of peptide resonances in the absence of RNA (Figure 5C), indicative of a largely unstructured molecule.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-11T15:59:19.713Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":34,"end":50,"reference_id":"18922466","reference_source":"pmid","reference_html":"A solution to limited genomic capacity: using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA. <i> Daugherty MD, D'Orso I, Frankel AD. </i> Mol Cell, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03528r006","statement":[{"text":"We further characterized the differences in IA and IIB binding modes using amide proton chemical shifts from 15N HSQC NMR spectra to monitor changes in the peptide-RNA interfaces. There is little peak dispersion of peptide resonances in the absence of RNA (Figure 5C), indicative of a largely unstructured molecule. However, we observe substantial amide peak dispersion in the presence of either IIB (red) or IA (blue) RNAs (Figure 5C), including the Hε protons of arginine side chains (Figure 5C inset). The overall upfield shifts observed in both 1H and 15N dimensions is consistent with stabilization of peptide α-helical structure upon binding (Wang and Jardetzky, 2002).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-12T08:58:36.900Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":34,"end":50,"reference_id":"18922466","reference_source":"pmid","reference_html":"A solution to limited genomic capacity: using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA. <i> Daugherty MD, D'Orso I, Frankel AD. </i> Mol Cell, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03528r007","statement":[{"text":"Given, the purine-rich internal loop of IA, we asked if this amino acid also is essential for IA binding. Interestingly, mutation of Asn40 had no effect on IA binding. Conversely, mutation of Arg41, which does not affect IIB binding (Tan et al., 1993), showed a reproducible 2-fold decrease in IA affinity (Figure 5A). R38A and R46A mutants showed similar 2-fold reductions in IA affinity but had no effect on IIB, while R43A, R44A, and W45A mutants bound IA like the wild type peptide. Helical wheel projections clearly show that different surfaces of the helix are used to recognize IIB and IA RNAs (Figure 5B).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-12T08:58:36.235Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":35,"end":50,"reference_id":"14644169","reference_source":"pmid","reference_html":"Analysis of nuclear targeting activities of transport signals in the human immunodeficiency virus Rev protein. <i> Demart S, Ceccherini-Silberstein F, Schlicht S, Walcher S, Wolff H, Neumann M, Erfle V, Brack-Werner R. </i> Exp Cell Res, 2003","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"GO:1990173","term_name":"protein localization to nucleoplasm","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0007106","ec_ontology":"ECO","ec_name":"green fluorescent protein fusion protein localization evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03528r008","statement":[{"text":"Rev–GFP showed typical predominantly nuclear localization (>80% of fluorescence) (Fig. 2A). In contrast, RevM5–GFP fluorescence was apparent mainly in the cytoplasm, with less than 22% of total fluorescence in the nucleus (Fig. 2A).","type":"Results"},{"text":"RevM5 has a mutation in this IDR.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T12:47:45.461Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A process in which a protein is transported to, or maintained in, a location within the nucleoplasm.\" [GOC:mah, PMID:22918952]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":35,"end":46,"reference_id":"9405152","reference_source":"pmid","reference_html":"Interactions between HIV Rev and nuclear import and export factors: the Rev nuclear localisation signal mediates specific binding to human importin-beta. <i> Henderson BR, Percipalle P. </i> J Mol Biol, 1997","date":"2022-03-08T13:53:07.412Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"region_id":"DP03528r010","statement":[{"text":"As shown in a gel mobility shift assay (Figure 2), the addition of Rev normally leads to formation of multimeric complexes with 35S-labelled RRE.","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":true,"interaction_partner":[{"db":"Rfam","id":"RF00036","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-10T19:25:46.060Z"}},{"start":35,"end":46,"reference_id":"9405152","reference_source":"pmid","reference_html":"Interactions between HIV Rev and nuclear import and export factors: the Rev nuclear localisation signal mediates specific binding to human importin-beta. <i> Henderson BR, Percipalle P. </i> J Mol Biol, 1997","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0007688","ec_ontology":"ECO","ec_name":"gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03528r011","statement":[{"text":"The experiment demonstrates the specificity of the Rev-importin-β interaction, as importin-β did not bind to the GST-Rev NLS mutant, or to GST protein. This was an unexpected finding, and identifies Rev as the first protein known to contain an NLS specific for the 97 kDa importin-β receptor, and not importin-α.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T12:47:40.440Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":11,"released":"2021_12","sequence":"MAGRSGDSDEDLLKAVRLIKFLYQSNPPPNPEGTRQARRNRRRRWRERQRQIHSISERILSTYLGRSAEPVPLQLPPLERLTLDCNEDCGTSGTQGVGSPQILVESPTILESGAKE","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"dataset":["Viral proteins","RNA-binding proteins"],"uniref50":"UniRef50_P69718","uniref90":"UniRef90_P69718","uniref100":"UniRef100_P69718","genes":[{"name":{"value":"rev","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04077","url":"https://hamap.expasy.org/unirule/MF_04077"}}]}}],"disorder_content":0.14655172413793102,"disprot_consensus":{"full":[{"start":34,"end":50,"type":"T"}],"Structural state":[{"start":34,"end":50,"type":"D"}],"Structural transition":[{"start":34,"end":50,"type":"T"}],"Molecular function":[{"start":34,"end":50,"type":"F"}],"Biological process":[{"start":35,"end":50,"type":"F"}]}},{"disprot_id":"DP03529","acc":"Q9NP98","creator":"fquaglia","date":"2021-11-08T09:07:23.810Z","features":{"pfam":[{"id":"PF05556","name":"Calcineurin-binding protein (Calsarcin)","start":1,"end":299}],"gene3D":[]},"length":299,"name":"Myozenin-1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":174,"reference_id":"34049882","reference_source":"pmid","reference_html":"Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. <i> Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K. </i> Sci Adv, 2021","date":"2023-07-17T19:14:46.619Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"BMRB","id":"50496"}],"region_id":"DP03529r005","statement":[{"text":"These results, demonstrating the intrinsically disordered/ensemble-state nature of N-FATZ-1 and Δ91-FATZ-1, are further supported by the 1H-15N heteronuclear single-quantum coherence (HSQC) spectra recorded for both constructs, which display a narrow chemical shift range in the proton dimension, as is typical for IDR-containing proteins (fig. S5A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:52:28.027Z"}},{"start":92,"end":299,"reference_id":"34049882","reference_source":"pmid","reference_html":"Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. <i> Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K. </i> Sci Adv, 2021","date":"2023-07-17T19:16:18.063Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"BMRB","id":"50497"}],"region_id":"DP03529r006","statement":[{"text":"These results, demonstrating the intrinsically disordered/ensemble-state nature of N-FATZ-1 and Δ91-FATZ-1, are further supported by the 1H-15N heteronuclear single-quantum coherence (HSQC) spectra recorded for both constructs, which display a narrow chemical shift range in the proton dimension, as is typical for IDR-containing proteins (fig. S5A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:52:30.675Z"}},{"start":1,"end":174,"reference_id":"34049882","reference_source":"pmid","reference_html":"Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. <i> Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K. </i> Sci Adv, 2021","date":"2023-07-17T19:23:44.840Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"SASBDB","id":"SASDJJ6"}],"region_id":"DP03529r007","statement":[{"text":"We further characterized N-FATZ-1 and Δ91-FATZ-1 using SEC combined with SAXS. The resulting scattering profiles and dimensionless Kratky plots are characteristic of intrinsically disordered proteins (IDPs), and subsequent modeling indicates that both constructs are best described as a conformational ensemble (Fig. 1, F to J, and Supplementary Results) (32). In addition, we derived the radius of gyration (Rg) of N-FATZ-1 and Δ91-FATZ-1 from analysis of SAXS data (table S2) and obtained Rg/Rh ratios of 1.1 to 1.2 that are, once again, consistent with the presence of IDRs (33).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:52:33.041Z"}},{"start":92,"end":299,"reference_id":"34049882","reference_source":"pmid","reference_html":"Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. <i> Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K. </i> Sci Adv, 2021","date":"2023-07-17T19:24:07.980Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"SASBDB","id":"SASDJK6"}],"region_id":"DP03529r008","statement":[{"text":"We further characterized N-FATZ-1 and Δ91-FATZ-1 using SEC combined with SAXS. The resulting scattering profiles and dimensionless Kratky plots are characteristic of intrinsically disordered proteins (IDPs), and subsequent modeling indicates that both constructs are best described as a conformational ensemble (Fig. 1, F to J, and Supplementary Results) (32). In addition, we derived the radius of gyration (Rg) of N-FATZ-1 and Δ91-FATZ-1 from analysis of SAXS data (table S2) and obtained Rg/Rh ratios of 1.1 to 1.2 that are, once again, consistent with the presence of IDRs (33).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:52:34.929Z"}},{"start":1,"end":174,"reference_id":"34049882","reference_source":"pmid","reference_html":"Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. <i> Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K. </i> Sci Adv, 2021","date":"2023-07-17T19:39:50.968Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03529r009","statement":[{"text":"The calculation of the compaction index using hydrodynamic radius (Rh) values derived from size exclusion chromatography (SEC) combined with dynamic light scattering (DLS) and viscometry measurements (table S1) (31), together with the analysis of the 222/200 ellipticity ratio, indicated a premolten globule for N-FATZ-1 and an increased content of regular secondary structure for Δ91-FATZ-1.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:52:36.742Z"}},{"start":92,"end":299,"reference_id":"34049882","reference_source":"pmid","reference_html":"Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. <i> Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K. </i> Sci Adv, 2021","date":"2023-07-17T19:40:04.653Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03529r010","statement":[{"text":"The calculation of the compaction index using hydrodynamic radius (Rh) values derived from size exclusion chromatography (SEC) combined with dynamic light scattering (DLS) and viscometry measurements (table S1) (31), together with the analysis of the 222/200 ellipticity ratio, indicated a premolten globule for N-FATZ-1 and an increased content of regular secondary structure for Δ91-FATZ-1.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:52:38.875Z"}},{"start":92,"end":299,"reference_id":"34049882","reference_source":"pmid","reference_html":"Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. <i> Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K. </i> Sci Adv, 2021","date":"2023-07-17T20:37:18.333Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042805","term_name":"actinin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P35609","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P12814","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP03529r011","statement":[{"text":"In relation to the binding of the shorter FATZ-1 constructs, we could not detect complex formation between N-FATZ-1 and rod-α-actinin-2 (Fig. 2C), while Δ91-FATZ-1 formed 2:1, 2:1, and 1:1 complexes with α-actinin-2, rod-α-actinin-2, and hd-α-actinin-2, respectively (Fig. 2D, fig. S6, B and C, and table S1).","type":"Results"},{"text":"In SEC-MALS, we also observed a 2:1 complex between Δ91-FATZ-1 and human (nonmuscle) α-actinin-1 (fig. S6D and table S1).","type":"Results"}],"term_comment":"","term_def":"\"Binding to actinin, any member of a family of proteins that crosslink F-actin.\" [GOC:jl, ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:52:42.613Z"}},{"start":92,"end":299,"reference_id":"34049882","reference_source":"pmid","reference_html":"Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. <i> Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K. </i> Sci Adv, 2021","date":"2023-07-17T20:34:52.868Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042805","term_name":"actinin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P35609","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03529r012","statement":[{"text":"We used isothermal titration calorimetry (ITC) to quantify the interaction affinity. N-FATZ-1 did not interact with rod-α-actinin-2, whereas Δ91-FATZ-1 showed a strong 2:1, 2:1, and 1:1 interaction with α-actinin-2 dimer, dimeric rod-α-actinin-2, and hd-α-actinin-2, respectively, in agreement with SEC-MALS data (Fig. 2, F to H, fig. S6E, and table S3).","type":"Results"}],"term_comment":"","term_def":"\"Binding to actinin, any member of a family of proteins that crosslink F-actin.\" [GOC:jl, ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:52:48.640Z"}},{"start":92,"end":299,"reference_id":"34049882","reference_source":"pmid","reference_html":"Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. <i> Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K. </i> Sci Adv, 2021","date":"2023-07-17T20:35:10.962Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042805","term_name":"actinin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys182Glu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg190Glu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys217Glu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys219Glu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg223Glu","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P35609","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03529r013","statement":[{"text":"We next designed the “fiveE” Δ91-FATZ-1 mutant, based on sequence alignment and metastructure analysis of FATZ proteins, in which five conserved positively charged residues within the CTR were reverted to negatively charged glutamates (K182E+R190E+K217E+K219E+R223E; see Methods). This construct did not form a stable complex with α-actinin-2 as assessed by SEC-MALS (Fig. 2E), in agreement with a very low ITC signal and for which a Kd could not be determined (see Fig. 2I and table S3).","type":"Results"}],"term_comment":"","term_def":"\"Binding to actinin, any member of a family of proteins that crosslink F-actin.\" [GOC:jl, ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:52:53.581Z"}},{"start":119,"end":237,"reference_id":"34049882","reference_source":"pmid","reference_html":"Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. <i> Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K. </i> Sci Adv, 2021","date":"2023-07-17T20:35:28.497Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042805","term_name":"actinin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P35609","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03529r014","statement":[{"text":"LP-MS revealed a protected (i.e., interacting) Δ91-FATZ-1 region spanning residues 119 to 237 (fig. S8). XL-MS, which was performed using a zero-length cross-linker, revealed three specific cross-links, K383/D205, E567/K233, and D893/K176 (see fig. S9; α-actinin-2 residues in italics), supporting the interaction between the CTR of FATZ-1 and the rod of α-actinin-2 (fig. S6E).","type":"Results"}],"term_comment":"","term_def":"\"Binding to actinin, any member of a family of proteins that crosslink F-actin.\" [GOC:jl, ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:52:55.568Z"}},{"start":176,"end":292,"reference_id":"34049882","reference_source":"pmid","reference_html":"Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. <i> Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K. </i> Sci Adv, 2021","date":"2023-07-17T20:36:29.833Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042805","term_name":"actinin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P35609","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03529r015","statement":[{"text":"We could not fully assign Δ91-FATZ-1 due to fast relaxation of cross-peaks in the region comprising residues 177 to 291. We could, however, locate the α-actinin-2–interacting region within the CTR at residues 176 to 292, as the corresponding cross-peaks disappeared or showed a drop in signal intensity (Fig. 2J and fig. S5B). We found a similar signal reduction pattern and thus binding behavior for both α-actinin-2 and hd-α-actinin-2. Further, a decrease in signal intensity upon binding to α-actinin-2 around residues 106 and 128, mapping to the GRR, indicated additional binding site(s) apart from the interacting region found within the CTR, which is in line with ITC and peptide array data (Fig. 2K and figs. S6 and S7).","type":"Results"}],"term_comment":"","term_def":"\"Binding to actinin, any member of a family of proteins that crosslink F-actin.\" [GOC:jl, ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:52:57.547Z"}},{"start":106,"end":128,"reference_id":"34049882","reference_source":"pmid","reference_html":"Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. <i> Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K. </i> Sci Adv, 2021","date":"2023-07-17T20:36:51.237Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042805","term_name":"actinin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P35609","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03529r016","statement":[{"text":"We could not fully assign Δ91-FATZ-1 due to fast relaxation of cross-peaks in the region comprising residues 177 to 291. We could, however, locate the α-actinin-2–interacting region within the CTR at residues 176 to 292, as the corresponding cross-peaks disappeared or showed a drop in signal intensity (Fig. 2J and fig. S5B). We found a similar signal reduction pattern and thus binding behavior for both α-actinin-2 and hd-α-actinin-2. Further, a decrease in signal intensity upon binding to α-actinin-2 around residues 106 and 128, mapping to the GRR, indicated additional binding site(s) apart from the interacting region found within the CTR, which is in line with ITC and peptide array data (Fig. 2K and figs. S6 and S7).","type":"Results"}],"term_comment":"","term_def":"\"Binding to actinin, any member of a family of proteins that crosslink F-actin.\" [GOC:jl, ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:52:59.560Z"}},{"start":180,"end":199,"reference_id":"34049882","reference_source":"pmid","reference_html":"Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. <i> Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K. </i> Sci Adv, 2021","date":"2023-07-17T20:51:06.524Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042805","term_name":"actinin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7A8T"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P35609","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03529r017","statement":[{"text":"In both α-actinin-2/FATZ-1 structures, one can see two identical stretches of amino acids bound to α-actinin-2, which are conserved among FATZ proteins (62 and 71% average identity for LM1 and LM2, respectively) and conform to the definition of eukaryotic linear motifs (ELMs) (Fig. 3, A and B) (36, 37). Accordingly, they are hereafter called LM1 (residues 180 to 199) and LM2 (residues 216 to 240). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to actinin, any member of a family of proteins that crosslink F-actin.\" [GOC:jl, ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false,"sequence_construct":"GPAMKHITVFKTYISPWERAMGVDPQQKMELGIDLLAYGAKAELPKYKSFNRTAMPYGGYEKASKRMTFQMPKFDLGPLLSEPLVLYNQNLS","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:53:01.566Z"}},{"start":216,"end":240,"reference_id":"34049882","reference_source":"pmid","reference_html":"Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. <i> Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K. </i> Sci Adv, 2021","date":"2023-07-17T20:51:26.057Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042805","term_name":"actinin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7A8T"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P35609","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03529r018","statement":[{"text":"In both α-actinin-2/FATZ-1 structures, one can see two identical stretches of amino acids bound to α-actinin-2, which are conserved among FATZ proteins (62 and 71% average identity for LM1 and LM2, respectively) and conform to the definition of eukaryotic linear motifs (ELMs) (Fig. 3, A and B) (36, 37). Accordingly, they are hereafter called LM1 (residues 180 to 199) and LM2 (residues 216 to 240). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to actinin, any member of a family of proteins that crosslink F-actin.\" [GOC:jl, ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false,"sequence_construct":"GPAMKHITVFKTYISPWERAMGVDPQQKMELGIDLLAYGAKAELPKYKSFNRTAMPYGGYEKASKRMTFQMPKFDLGPLLSEPLVLYNQNLS","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:53:04.196Z"}},{"start":200,"end":215,"reference_id":"34049882","reference_source":"pmid","reference_html":"Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. <i> Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K. </i> Sci Adv, 2021","date":"2023-07-17T20:50:50.142Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7A8T"}],"region_id":"DP03529r019","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P35609"}],"statement":[{"text":"LM1 and LM2 are connected by a short 16- and 13-residue linker in rod-α-actinin-2/mini-FATZ-1 and hd-α-actinin-2/Δ91-FATZ-1, respectively, which is not visible in electron density maps and matches the positions of previously identified cross-links (Fig. 3A and fig. S9B).","type":"Results"}],"sequence_construct":"GPAMKHITVFKTYISPWERAMGVDPQQKMELGIDLLAYGAKAELPKYKSFNRTAMPYGGYEKASKRMTFQMPKFDLGPLLSEPLVLYNQNLS","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:53:06.281Z"}},{"start":200,"end":215,"reference_id":"34049882","reference_source":"pmid","reference_html":"Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. <i> Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K. </i> Sci Adv, 2021","date":"2023-07-17T20:45:21.204Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7A8T"}],"region_id":"DP03529r020","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P35609"}],"statement":[{"text":"LM1 and LM2 are connected by a short 16- and 13-residue linker in rod-α-actinin-2/mini-FATZ-1 and hd-α-actinin-2/Δ91-FATZ-1, respectively, which is not visible in electron density maps and matches the positions of previously identified cross-links (Fig. 3A and fig. S9B).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:52:40.558Z"}},{"start":216,"end":240,"reference_id":"34049882","reference_source":"pmid","reference_html":"Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. <i> Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K. </i> Sci Adv, 2021","date":"2023-07-17T20:48:19.722Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042805","term_name":"actinin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P35609","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03529r021","statement":[{"text":"To dissect the contribution of LM1 and LM2 to the binding affinity, we used ITC with one peptide corresponding to each motif. While we could not detect binding between LM1 peptide and α-actinin-2 (Fig. 3D), LM2 peptide bound to α-actinin-2 with a binding stoichiometry of 1.9 and a Kd of 315 nM (Fig. 3E), which fits that of Δ91-FATZ-1–binding to hd-α-actinin-2 (Kd = 260 nM; see table S3). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to actinin, any member of a family of proteins that crosslink F-actin.\" [GOC:jl, ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:53:08.468Z"}},{"start":218,"end":228,"reference_id":"34049882","reference_source":"pmid","reference_html":"Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. <i> Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K. </i> Sci Adv, 2021","date":"2023-07-17T20:52:03.127Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042805","term_name":"actinin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7A8U"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P35609","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03529r022","statement":[{"text":"These diverse binding affinities match the structure of rod-α-actinin-2/Δ91-FATZ-1, which was additionally crystallized and displays only a shorter LM2 bound to α-actinin-2 rod [see fig. S10, A (right) and D, and table S4), revealing LM2 as the major binding site. ","type":"Results"}],"term_comment":"","term_def":"\"Binding to actinin, any member of a family of proteins that crosslink F-actin.\" [GOC:jl, ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false,"sequence_construct":"GPTVGGQLGTAGQGFSYSKSNGRGGSQAGGSGSAGQYGSDQQHHLGSGSGAGGTGGPAGQAGRGGAAGTAGVGETGSGDQAGGEGKHITVFKTYISPWERAMGVDPQQKMELGIDLLAYGAKAELPKYKSFNRTAMPYGGYEKASKRMTFQMPKFDLGPLLSEPLVLYNQNLSNRPSFNRTPIPWLSSGEPVDYNVDIGIPLDGETEEL","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:53:10.317Z"}},{"start":92,"end":299,"reference_id":"34049882","reference_source":"pmid","reference_html":"Order from disorder in the sarcomere: FATZ forms a fuzzy but tight complex and phase-separated condensates with α-actinin. <i> Sponga A, Arolas JL, Schwarz TC, Jeffries CM, Rodriguez Chamorro A, Kostan J, Ghisleni A, Drepper F, Polyansky A, De Almeida Ribeiro E, Pedron M, Zawadzka-Kazimierczuk A, Mlynek G, Peterbauer T, Doto P, Schreiner C, Hollerl E, Mateos B, Geist L, Faulkner G, Kozminski W, Svergun DI, Warscheid B, Zagrovic B, Gautel M, Konrat R, Djinović-Carugo K. </i> Sci Adv, 2021","date":"2023-07-17T21:07:07.911Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007056","ec_ontology":"ECO","ec_name":"differential interference contrast microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP03529r023","statement":[{"text":"Only Δ91-FATZ-1 showed spontaneous condensation (i.e., increased turbidity) when the temperature was increased from 4° to 22° or 37°C, whereas N-FATZ-1 remained transparent (Fig. 5C and fig. S16A). Δ91-FATZ-1 formed round-shaped droplets that were constantly fusing over time and reached up to 20 μm in diameter, as indicated by differential interference contrast (DIC) microscopy (see Fig. 5C, fig. S16B, and movie S4).","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:53:11.861Z"}}],"regions_counter":23,"released":"2021_12","sequence":"MPLSGTPAPNKKRKSSKLIMELTGGGQESSGLNLGKKISVPRDVMLEELSLLTNRGSKMFKLRQMRVEKFIYENHPDVFSDSSMDHFQKFLPTVGGQLGTAGQGFSYSKSNGRGGSQAGGSGSAGQYGSDQQHHLGSGSGAGGTGGPAGQAGRGGAAGTAGVGETGSGDQAGGEGKHITVFKTYISPWERAMGVDPQQKMELGIDLLAYGAKAELPKYKSFNRTAMPYGGYEKASKRMTFQMPKFDLGPLLSEPLVLYNQNLSNRPSFNRTPIPWLSSGEPVDYNVDIGIPLDGETEEL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref50":"UniRef50_Q9NP98","uniref90":"UniRef90_Q9NP98","uniref100":"UniRef100_Q9NP98","genes":[{"name":{"value":"MYOZ1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:13752","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:13752"}}]},"synonyms":[{"value":"MYOZ","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAG24509.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAG24509.1"}}]}]}],"alphafold_very_low_content":0.38461538461538464,"dataset":["Condensates-related proteins"],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":299,"type":"D"}],"Structural state":[{"start":1,"end":299,"type":"D"}],"Molecular function":[{"start":92,"end":299,"type":"F"}],"Disorder function":[{"start":200,"end":215,"type":"F"}]}},{"disprot_id":"DP03530","acc":"P19554","creator":"ewagner","date":"2021-11-08T09:30:30.028Z","features":{"pfam":[{"id":"PF00558","name":"Vpu protein","start":1,"end":77}],"gene3D":[]},"length":81,"name":"Protein Vpu","ncbi_taxon_id":11691,"organism":"Human immunodeficiency virus type 1 group M subtype B (isolate SF162)","regions":[{"start":39,"end":81,"reference_id":"19804408","reference_source":"pmid","reference_html":"NMR structural characterization of HIV-1 virus protein U cytoplasmic domain in the presence of dodecylphosphatidylcholine micelles. <i> Wittlich M, Koenig BW, Stoldt M, Schmidt H, Willbold D. </i> FEBS J, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03530r001","statement":[{"text":"The spectrum obtained in detergent-free buffer showed a pronounced minimum at 199 nm indicative of a predominantly unordered protein.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-11T15:17:57.926Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":39,"end":51,"reference_id":"19804408","reference_source":"pmid","reference_html":"NMR structural characterization of HIV-1 virus protein U cytoplasmic domain in the presence of dodecylphosphatidylcholine micelles. <i> Wittlich M, Koenig BW, Stoldt M, Schmidt H, Willbold D. </i> FEBS J, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"BMRB","id":"15513"},{"db":"PDB","id":"2K7Y"}],"interaction_partner":[{"db":"ChEBI","id":"17239","partner_start":null,"partner_end":null}],"region_id":"DP03530r002","statement":[{"text":"Continuous stretches with prominent chemical shift changes were observed for residues 39–51 and 64–78. In contrast, amide chemical shifts of residues 52–63 were virtually unaffected by the presence of DPC micelles.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-11T15:18:33.628Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":64,"end":78,"reference_id":"19804408","reference_source":"pmid","reference_html":"NMR structural characterization of HIV-1 virus protein U cytoplasmic domain in the presence of dodecylphosphatidylcholine micelles. <i> Wittlich M, Koenig BW, Stoldt M, Schmidt H, Willbold D. </i> FEBS J, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"BMRB","id":"15513"},{"db":"PDB","id":"2K7Y"}],"interaction_partner":[{"db":"ChEBI","id":"17239","partner_start":null,"partner_end":null}],"region_id":"DP03530r003","statement":[{"text":"Continuous stretches with prominent chemical shift changes were observed for residues 39–51 and 64–78. In contrast, amide chemical shifts of residues 52–63 were virtually unaffected by the presence of DPC micelles.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-11T15:18:32.448Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":39,"end":48,"reference_id":"19804408","reference_source":"pmid","reference_html":"NMR structural characterization of HIV-1 virus protein U cytoplasmic domain in the presence of dodecylphosphatidylcholine micelles. <i> Wittlich M, Koenig BW, Stoldt M, Schmidt H, Willbold D. </i> FEBS J, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"BMRB","id":"15513"},{"db":"PDB","id":"2K7Y"}],"region_id":"DP03530r004","statement":[{"text":"In contrast, characteristic secondary shifts of VpUcyt observed in the presence of 100 mm DPC clearly indicated the formation of two helices (Fig. 3, right column).","type":"Results"},{"text":"On the basis of the three sets of secondary shift data in Fig. 3 (right), the helices probably range from I39 to E48 (helix 2) and from L64 to R70 (helix 3).","type":"Results"},{"text":"The fractional helicity of amino acid stretches 39–48 (helix 2) and 64–70 (helix 3) was estimated by comparing the observed average secondary shifts with the values expected for a regular helix. This procedure provided fractional helicities of ∼ 80% (Δδ13Cα) for helix 2 and 40% (Δδ1Hα) for helix 3.","type":"Results"}],"sample":[{"term_id":"IDPO:00489","term_name":"interacting membrane","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":100,"db":"ChEBI","id":"17239","statements":[{"type":"Abstract","text":"The structure and dynamics of VpUcyt were characterized in the presence of membrane simulating dodecylphosphatidylcholine (DPC) micelles by high-resolution liquid state NMR. "}],"entry_name":"CDP"}],"states_connection":[{"source":"DP03530r006","target":"DP03530r005"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-11T15:18:21.247Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":39,"end":48,"reference_id":"19804408","reference_source":"pmid","reference_html":"NMR structural characterization of HIV-1 virus protein U cytoplasmic domain in the presence of dodecylphosphatidylcholine micelles. <i> Wittlich M, Koenig BW, Stoldt M, Schmidt H, Willbold D. </i> FEBS J, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"BMRB","id":"15513"},{"db":"PDB","id":"2K7Y"}],"region_id":"DP03530r005","sample":[{"term_id":"IDPO:00489","term_name":"interacting membranes","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":100,"db":"ChEBI","id":"17239","statements":[{"type":"Abstract","text":"The structure and dynamics of VpUcyt were characterized in the presence of membrane simulating dodecylphosphatidylcholine (DPC) micelles by high-resolution liquid state NMR. "}],"entry_name":"CDP"}],"statement":[{"text":"In contrast, characteristic secondary shifts of VpUcyt observed in the presence of 100 mm DPC clearly indicated the formation of two helices (Fig. 3, right column).","type":"Results"},{"text":"The fractional helicity of amino acid stretches 39–48 (helix 2) and 64–70 (helix 3) was estimated by comparing the observed average secondary shifts with the values expected for a regular helix. This procedure provided fractional helicities of ∼ 80% (Δδ13Cα) for helix 2 and 40% (Δδ1Hα) for helix 3.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-11T15:17:47.555Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":39,"end":81,"reference_id":"19804408","reference_source":"pmid","reference_html":"NMR structural characterization of HIV-1 virus protein U cytoplasmic domain in the presence of dodecylphosphatidylcholine micelles. <i> Wittlich M, Koenig BW, Stoldt M, Schmidt H, Willbold D. </i> FEBS J, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03530r006","statement":[{"text":"VpUcyt appears to be unstructured in buffer.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-11T15:17:45.755Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":39,"end":51,"reference_id":"19804408","reference_source":"pmid","reference_html":"NMR structural characterization of HIV-1 virus protein U cytoplasmic domain in the presence of dodecylphosphatidylcholine micelles. <i> Wittlich M, Koenig BW, Stoldt M, Schmidt H, Willbold D. </i> FEBS J, 2009","date":"2023-08-22T14:02:13.278Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005886","term_name":"plasma membrane","term_namespace":"Cellular component","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"BMRB","id":"15513"}],"region_id":"DP03530r007","sample":[{"term_id":"IDPO:00489","term_name":"interacting membrane","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":100,"db":"ChEBI","id":"17239","statements":[{"type":"Abstract","text":"he structure and dynamics of VpUcyt were characterized in the presence of membrane simulating dodecylphosphatidylcholine (DPC) micelles by high-resolution liquid state NMR."}],"entry_name":"CDP"}],"statement":[{"text":"Continuous stretches with prominent chemical shift changes were observed for residues 39–51 and 64–78.","type":"Results"},{"text":"We propose that the structure of micelle-associated VpUcyt is a reasonable approximation of the physiologically relevant membrane-attached cytoplasmic region of VpU. This view is supported by the experimentally confirmed location of VpUcyt at the micelle–water interface. The polar headgroup of DPC is chemically identical to that of the large fraction of phospholipids in biological membranes that feature a phosphatidylcholine headgroup.","type":"Discussion"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.\" [ISBN:0716731363]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":64,"end":78,"reference_id":"19804408","reference_source":"pmid","reference_html":"NMR structural characterization of HIV-1 virus protein U cytoplasmic domain in the presence of dodecylphosphatidylcholine micelles. <i> Wittlich M, Koenig BW, Stoldt M, Schmidt H, Willbold D. </i> FEBS J, 2009","date":"2023-08-22T14:01:56.055Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005886","term_name":"plasma membrane","term_namespace":"Cellular component","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"BMRB","id":"15513"}],"region_id":"DP03530r008","sample":[{"term_id":"IDPO:00489","term_name":"interacting membrane","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":100,"db":"ChEBI","id":"17239","statements":[{"type":"Abstract","text":"he structure and dynamics of VpUcyt were characterized in the presence of membrane simulating dodecylphosphatidylcholine (DPC) micelles by high-resolution liquid state NMR."}],"entry_name":"CDP"}],"statement":[{"text":"Continuous stretches with prominent chemical shift changes were observed for residues 39–51 and 64–78.","type":"Results"},{"text":"We propose that the structure of micelle-associated VpUcyt is a reasonable approximation of the physiologically relevant membrane-attached cytoplasmic region of VpU. This view is supported by the experimentally confirmed location of VpUcyt at the micelle–water interface. The polar headgroup of DPC is chemically identical to that of the large fraction of phospholipids in biological membranes that feature a phosphatidylcholine headgroup.","type":"Discussion"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.\" [ISBN:0716731363]","disprot_namespace":"Disorder function","term_is_binding":false}],"regions_counter":8,"released":"2021_12","sequence":"MQPLQILAIVALVVAAIIAIVVWTIVYIEYRKILRQRKIDRLIDRITERAEDSGNESEGDQEELSALVERGHLAPWDVDDL","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_P05923","uniref90":"UniRef90_P19554","uniref100":"UniRef100_P19554","genes":[{"name":{"value":"vpu","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04082","url":"https://hamap.expasy.org/unirule/MF_04082"}}]}}],"disorder_content":0.5308641975308642,"disprot_consensus":{"full":[{"start":39,"end":48,"type":"T"},{"start":49,"end":81,"type":"D"}],"Structural state":[{"start":39,"end":81,"type":"D"}],"Molecular function":[{"start":39,"end":51,"type":"F"},{"start":64,"end":78,"type":"F"}],"Structural transition":[{"start":39,"end":48,"type":"T"}],"Cellular component":[{"start":39,"end":51,"type":"F"},{"start":64,"end":78,"type":"F"}]}},{"disprot_id":"DP03531","acc":"P49789","creator":"vacs","date":"2021-11-08T12:13:34.845Z","features":{"pfam":[{"id":"PF01230","name":"HIT domain","start":11,"end":104}],"gene3D":[]},"length":147,"name":"Bis(5'-adenosyl)-triphosphatase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":107,"end":127,"reference_id":"9576908","reference_source":"pmid","reference_html":"Genetic, biochemical, and crystallographic characterization of Fhit-substrate complexes as the active signaling form of Fhit. <i> Pace HC, Garrison PN, Robinson AK, Barnes LD, Draganescu A, Rösler A, Blackburn GM, Siprashvili Z, Croce CM, Huebner K, Brenner C. </i> Proc Natl Acad Sci U S A, 1998","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2FHI"},{"db":"PDB","id":"1FHI"}],"region_id":"DP03531r001","statement":[{"text":"Though it is possible to ‘‘refine’’ the models to working R factors below 20%, the structural models presented herein have good geometry and are at apparent free R-factor minima, values of which are likely limited by disorder that prevents modeling of residues 107–128.","type":"Methods"},{"text":"The Fhit–IB2 structures, like those of the first Fhit structures, contains an amino-terminal b-hairpin not found in Hint and a gap from residue 107 to residue 127 or to 128 that is disordered (Fig. 2).","type":"Results"},{"text":"Residues 107-127 are disordered in all structures.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-16T08:23:31.167Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":112,"end":116,"reference_id":"15007172","reference_source":"pmid","reference_html":"Fhit is a physiological target of the protein kinase Src. <i> Pekarsky Y, Garrison PN, Palamarchuk A, Zanesi N, Aqeilan RI, Huebner K, Barnes LD, Croce CM. </i> Proc Natl Acad Sci U S A, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03531r002","statement":[{"text":"Our data demonstrate that Fhit is a target of tyrosine phosphorylation by the Src protein kinase. We show that Src phosphorylates Y114 of Fhit in vitro and in vivo, providing insight into a biochemical pathway involved in Fhit signaling.","type":"Abstract"},{"text":"Here we report that Fhit is a target of tyrosine phosphorylation by Src protein kinase. We show that Src phosphorylates Y114 of Fhit in vitro and in vivo and therefore provide important clues to biochemical mechanisms involved in Fhit signaling.","type":"Introduction"},{"text":"To identify which tyrosine is phosphorylated, a trypsin digest of fraction 3 was analyzed by HPLC-ion-trap mass spectrometry. Only peptide 110-119 was phosphorylated, and the fragmentation pattern of the peptide was compatible only with Y114 being phosphorylated and not S112 (Fig. 3E).","type":"Results"},{"text":"Thus, the mass spectrometry data demonstrated that fraction 3 is Fhit phosphorylated on Y114 on both subunits.","type":"Results"},{"text":"The data clearly show that Fhit is phosphorylated on tyrosine 114 by Src kinase both in vitro and in vivo.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-16T08:25:35.642Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":112,"end":116,"reference_id":"15007172","reference_source":"pmid","reference_html":"Fhit is a physiological target of the protein kinase Src. <i> Pekarsky Y, Garrison PN, Palamarchuk A, Zanesi N, Aqeilan RI, Huebner K, Barnes LD, Croce CM. </i> Proc Natl Acad Sci U S A, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03531r003","statement":[{"text":"Our data demonstrate that Fhit is a target of tyrosine phosphorylation by the Src protein kinase. We show that Src phosphorylates Y114 of Fhit in vitro and in vivo, providing insight into a biochemical pathway involved in Fhit signaling.","type":"Abstract"},{"text":"Here we report that Fhit is a target of tyrosine phosphorylation by Src protein kinase. We show that Src phosphorylates Y114 of Fhit in vitro and in vivo and therefore provide important clues to biochemical mechanisms involved in Fhit signaling.","type":"Introduction"},{"text":"To determine which tyrosine is phosphorylated in vivo by Src, several Fhit mutants were created, FhitY114F, FhitY145F and FhitY114F, Y145F, individually cotransfected with the activated SRC construct, and checked for tyrosine phosphorylation by Western blotting. Phosphorylated Fhit was detected on expression of WT Fhit or FhitY145F (Fig. 4B Top, lanes 2 and 4) but not FhitY114F or FhitY114F, Y145F (Fig. 4B Top, lanes 3 and 5). The tyrosine phosphorylation was confirmed by using antiphosphotyrosine antibody (Fig. 4B Bottom). These results confirmed that Y114 of Fhit is a target of Src phosphorylation in vivo.","type":"Results"},{"text":"The data clearly show that Fhit is phosphorylated on tyrosine 114 by Src kinase both in vitro and in vivo.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-16T08:25:32.475Z"},"ec_go":"IMP","disprot_namespace":"Disorder function"}],"regions_counter":3,"released":"2021_12","sequence":"MSFRFGQHLIKPSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLRPDEVADLFQTTQRVGTVVEKHFHGTSLTFSMQDGPEAGQTVKHVHVHVLPRKAGDFHRNDSIYEELQKHDKEDFPASWRSEEEMAAEAAALRVYFQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref50":"UniRef50_P49789","uniref90":"UniRef90_P49789","uniref100":"UniRef100_P49789","genes":[{"name":{"value":"FHIT"}}],"dataset":["NDDs-related proteins","Cancer-related proteins"],"alphafold_very_low_content":0,"disorder_content":0.14285714285714285,"disprot_consensus":{"full":[{"start":107,"end":127,"type":"D"}],"Structural state":[{"start":107,"end":127,"type":"D"}],"Disorder function":[{"start":112,"end":116,"type":"F"}]}},{"disprot_id":"DP03532","acc":"Q68J44","creator":"vacs","date":"2021-11-09T12:06:22.281Z","features":{"pfam":[{"id":"PF00782","name":"Dual specificity phosphatase, catalytic domain","start":62,"end":198}],"gene3D":[]},"length":220,"name":"Dual specificity phosphatase 29","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":2,"end":31,"reference_id":"21543850","reference_source":"pmid","reference_html":"Structure of human dual-specificity phosphatase 27 at 2.38 Å resolution. <i> Lountos GT, Tropea JE, Waugh DS. </i> Acta Crystallogr D Biol Crystallogr, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2Y96"}],"region_id":"DP03532r001","statement":[{"text":"Residues 2–31 in the N-terminal region and residues 207–220 in the C-terminal tail were not visible in the electron-density maps and thus were not included in the model.","type":"Results"},{"text":"Residues 2-31 and 207-220 are missing in all chains and are presumably disordered.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-16T08:50:21.390Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":207,"end":220,"reference_id":"21543850","reference_source":"pmid","reference_html":"Structure of human dual-specificity phosphatase 27 at 2.38 Å resolution. <i> Lountos GT, Tropea JE, Waugh DS. </i> Acta Crystallogr D Biol Crystallogr, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2Y96"}],"region_id":"DP03532r002","statement":[{"text":"Residues 2–31 in the N-terminal region and residues 207–220 in the C-terminal tail were not visible in the electron-density maps and thus were not included in the model.","type":"Results"},{"text":"Residues 2-31 and 207-220 are missing in all chains and are presumably disordered.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-16T08:50:20.154Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MTSGEVKTSLKNAYSSAKRLSPKMEEEGEEEDYCTPGAFELERLFWKGSPQYTHVNEVWPKLYIGDEATALDRYRLQKAGFTHVLNAAHGRWNVDTGPDYYRDMDIQYHGVEADDLPTFDLSVFFYPAAAFIDRALSDDHSKILVHCVMGRSRSATLVLAYLMIHKDMTLVDAIQQVAKNRCVLPNRGFLKQLRELDKQLVQQRRRSQRQDGEEEDGREL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref50":"UniRef50_Q68J44","uniref90":"UniRef90_Q68J44","uniref100":"UniRef100_Q68J44","genes":[{"name":{"value":"DUSP29","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:23481","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:23481"}}]},"synonyms":[{"value":"DUPD1"},{"value":"DUSP27","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"17498703","url":"http://www.ncbi.nlm.nih.gov/pubmed/17498703","alternativeUrl":"https://europepmc.org/abstract/MED/17498703"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"21543850","url":"http://www.ncbi.nlm.nih.gov/pubmed/21543850","alternativeUrl":"https://europepmc.org/abstract/MED/21543850"}}]}]}],"alphafold_very_low_content":0.1318181818181818,"disorder_content":0.2,"disprot_consensus":{"full":[{"start":2,"end":31,"type":"D"},{"start":207,"end":220,"type":"D"}],"Structural state":[{"start":2,"end":31,"type":"D"},{"start":207,"end":220,"type":"D"}]}},{"disprot_id":"DP03533","acc":"O95147","creator":"vacs","date":"2021-11-09T12:30:11.179Z","features":{"pfam":[{"id":"PF00782","name":"Dual specificity phosphatase, catalytic domain","start":34,"end":164}],"gene3D":[]},"length":198,"name":"Dual specificity protein phosphatase 14","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":2,"end":23,"reference_id":"19770498","reference_source":"pmid","reference_html":"Overproduction, purification and structure determination of human dual-specificity phosphatase 14. <i> Lountos GT, Tropea JE, Cherry S, Waugh DS. </i> Acta Crystallogr D Biol Crystallogr, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2WGP"}],"region_id":"DP03533r001","statement":[{"text":"No electron density was observed for residues 2–23 of DUSP14, suggesting that this region of the protein is disordered.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-16T08:30:03.504Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MSSRGHSTLPRTLMAPRMISEGDIGGIAQITSSLFLGRGSVASNRHLLQARGITCIVNATIEIPNFNWPQFEYVKVPLADMPHAPIGLYFDTVADKIHSVSRKHGATLVHCAAGVSRSATLCIAYLMKFHNVCLLEAYNWVKARRPVIRPNVGFWRQLIDYERQLFGKSTVKMVQTPYGIVPDVYEKESRHLMPYWGI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref50":"UniRef50_O95147","uniref90":"UniRef90_O95147","uniref100":"UniRef100_O95147","genes":[{"name":{"value":"DUSP14"},"synonyms":[{"value":"MKP6"}]}],"alphafold_very_low_content":0.1414141414141414,"disorder_content":0.1111111111111111,"disprot_consensus":{"full":[{"start":2,"end":23,"type":"D"}],"Structural state":[{"start":2,"end":23,"type":"D"}]}},{"acc":"P12520","sequence":"MEQAPEDQGPQREPYNEWTLELLEELKSEAVRHFPRIWLHNLGQHIYETYGDTWAGVEAIIRILQQLLFIHFRIGCRHSRIGVTRQRRARNGASRS","creator":"fquaglia","dataset":["Viral proteins"],"date":"2021-11-10T12:11:56.370Z","disprot_id":"DP03534","features":{"pfam":[{"id":"PF00522","name":"VPR/VPX protein","start":1,"end":82}],"gene3D":[]},"genes":[{"name":{"value":"vpr","evidences":[{"source":{"id":"MF_04080","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04080","_id":"685af523b4ac24d5329d97b1"},"code":"ECO:0000255","_id":"685af523b4ac24d5329d97b0"}],"_id":"685af523b4ac24d5329d97b2"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"685af523b4ac24d5329d97af"}],"length":96,"name":"Protein Vpr","ncbi_taxon_id":11698,"organism":"Human immunodeficiency virus type 1 group M subtype B (isolate NY5)","regions_counter":9,"released":"2021_12","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"uniref100":"UniRef100_P12520","uniref50":"UniRef50_P12520","uniref90":"UniRef90_P12520","regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5JK7","_id":"685af523b4ac24d5329d97a5"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006222","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","ec_ontology":"ECO","start":1,"end":17,"interaction_partner":[],"reference_html":"The DDB1-DCAF1-Vpr-UNG2 crystal structure reveals how HIV-1 Vpr steers human UNG2 toward destruction. <i> Wu Y, Zhou X, Barnes CO, DeLucia M, Cohen AE, Gronenborn AM, Ahn J, Calero G. </i> Nat Struct Mol Biol, 2016","reference_id":"27571178","region_id":"DP03534r008","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Four structural motifs important for Vpr's interaction with partners are discernible: a random-coil N-terminal tail; a hydrophobic cleft formed by helices α1, α2 and the first turn of α3; the loop connecting α2 and α3 (insert loop); and the C-terminal region of helix α3 (Supplementary Fig. 2a).","_id":"685af523b4ac24d5329d97a6"},{"type":"Curator statement","text":"The PDB has low resolution in the N-terminal tail and the figure shows the disorder of this region of Vpr.","_id":"685af523b4ac24d5329d97a7"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-15T08:34:30.216Z","_id":"685af523b4ac24d5329d97a8"},"version":1,"_id":"685af523b4ac24d5329d97a4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5JK7","_id":"685af523b4ac24d5329d97aa"}],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":17,"interaction_partner":[{"db":"UniProt","id":"Q9Y4B6","partner_start":null,"partner_end":null,"_id":"685af523b4ac24d5329d97ab"}],"reference_html":"The DDB1-DCAF1-Vpr-UNG2 crystal structure reveals how HIV-1 Vpr steers human UNG2 toward destruction. <i> Wu Y, Zhou X, Barnes CO, DeLucia M, Cohen AE, Gronenborn AM, Ahn J, Calero G. </i> Nat Struct Mol Biol, 2016","reference_id":"27571178","region_id":"DP03534r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Vpr interacts with DCAF1 by using its N terminus and helix α3 (described below) and interacts with UNG2 via the insert loop and residues in the hydrophobic cleft, burying a surface area of 1,650 Å2 and 940 Å2, respectively (Supplementary Fig. 2b).","_id":"685af523b4ac24d5329d97ac"},{"type":"Figure","text":"(c) Detailed view of the interaction between the N-terminal tail of Vpr and residues of DCAF1 at the edges of two propeller blades. ","_id":"685af523b4ac24d5329d97ad"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-11-15T08:34:10.610Z","_id":"685af523b4ac24d5329d97ae"},"version":1,"_id":"685af523b4ac24d5329d97a9","reference_source":"pmid"}],"__v":0,"disorder_content":0.17708333333333334,"disprot_consensus":{"full":[{"start":1,"end":17,"type":"D"}],"Structural state":[{"start":1,"end":17,"type":"D"}],"Molecular function":[{"start":1,"end":17,"type":"F"}]}},{"disprot_id":"DP03535","acc":"P69697","creator":"jbergier","date":"2021-11-10T13:07:35.040Z","features":{"pfam":[{"id":"PF00539","name":"Transactivating regulatory protein (Tat)","start":2,"end":64}],"gene3D":[]},"length":86,"name":"Protein Tat","ncbi_taxon_id":11678,"organism":"Human immunodeficiency virus type 1 group M subtype B (isolate BH10)","regions":[{"start":1,"end":86,"reference_id":"30600181","reference_source":"pmid","reference_html":"Conformational diversity in the intrinsically disordered HIV-1 Tat protein induced by zinc and pH. <i> Kunihara T, Hayashi Y, Arai M. </i> Biochem Biophys Res Commun, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03535r001","statement":[{"text":"The CD value at 222 nm of the zinc-free Tat was closer to zero than that of the zinc-bound form. Moreover, a negative peak at ∼202 nm, which is an index of the presence of random-coil structures, is more prominent upon removal of zinc ions.","type":"Results"},{"text":"Authors claim the use of the isolate HXB2 however the sequence they report in Figure 1. corresponds to this Uniprot.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-12T10:35:53.836Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":86,"reference_id":"30600181","reference_source":"pmid","reference_html":"Conformational diversity in the intrinsically disordered HIV-1 Tat protein induced by zinc and pH. <i> Kunihara T, Hayashi Y, Arai M. </i> Biochem Biophys Res Commun, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03535r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","statements":[{"type":"Discussion","text":"To attach zinc ions to Tat, we concentrated the eluates of nickel-affinity chromatography (Supplementary Fig. S1B) and added 0.1 M DTT to reduce the seven Cys residues of Tat that coordinate two zinc ions [12,13]. Subsequently, ZnCl2 at a concentration 16-fold higher than that of Tat was added to the solution. "}],"entry_name":"zinc(2+)"}],"statement":[{"text":"The CD spectrum of the zinc-bound Tat had a minimum at 202 nm and a CD value close to zero at 222 nm, indicating that Tat is largely disordered (Fig. 2A). However, a slightly negative shoulder around 222 nm suggests the presence of residual helical structures. ","type":"Results"},{"text":"Therefore, the structure of zinc-bound Tat at neutral pH corresponds to a pre-molten globule state.","type":"Results"},{"text":"Authors claim the use of the isolate HXB2 however the sequence they report in Figure 1. corresponds to this Uniprot.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-12T10:35:36.427Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":86,"reference_id":"30600181","reference_source":"pmid","reference_html":"Conformational diversity in the intrinsically disordered HIV-1 Tat protein induced by zinc and pH. <i> Kunihara T, Hayashi Y, Arai M. </i> Biochem Biophys Res Commun, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03535r003","statement":[{"text":"The absence of a peak in the Kratky plot of the zinc-bound Tat indicates largely disordered structures (Fig. 3B). However, the presence of a plateau without a linear increase in wide-angle regions suggests that the protein molecule is not completely unfolded [24].","type":"Results"},{"text":"Comparison of the scaling curves with the Rg of Tat shows that the molecular size of Tat is close to but slightly more compact than the fully unfolded state.","type":"Results"},{"text":"Authors claim the use of the isolate HXB2 however the sequence they report in Figure 1. corresponds to this Uniprot.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-12T10:35:14.980Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":86,"reference_id":"30600181","reference_source":"pmid","reference_html":"Conformational diversity in the intrinsically disordered HIV-1 Tat protein induced by zinc and pH. <i> Kunihara T, Hayashi Y, Arai M. </i> Biochem Biophys Res Commun, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03535r004","statement":[{"text":"The one-dimensional 1H NMR spectrum of the zinc-bound Tat showed line broadening due to conformational dynamics in the intermediate exchange regime (Fig. 2B), suggesting structural fluctuation in millisecond time scales.","type":"Results"},{"text":"Authors claim the use of the isolate HXB2 however the sequence they report in Figure 1. corresponds to this Uniprot.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-12T10:35:04.275Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":86,"reference_id":"30600181","reference_source":"pmid","reference_html":"Conformational diversity in the intrinsically disordered HIV-1 Tat protein induced by zinc and pH. <i> Kunihara T, Hayashi Y, Arai M. </i> Biochem Biophys Res Commun, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":4}],"region_id":"DP03535r005","statement":[{"text":"The pH titration of CD spectra at pH values from 7 to 4 showed that the ellipticity at 222 nm increased with decreasing pH and exhibited a cooperative helix unfolding transition around pH 5–5.5 (Fig. 4A and B). The CD spectra below pH 5 were coincident with that of zinc-free Tat (Fig. 2, Fig. 4A,B), indicating that both the decrease in pH and the removal of zinc ions have identical effects on the secondary structure of Tat.","type":"Results"},{"text":"Taken together, the results indicate that Tat at pH 4 is in a random coil-like fully unfolded state.","type":"Results"},{"text":"Authors claim the use of the isolate HXB2 however the sequence they report in Figure 1. corresponds to this Uniprot.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-12T10:34:52.727Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":86,"reference_id":"30600181","reference_source":"pmid","reference_html":"Conformational diversity in the intrinsically disordered HIV-1 Tat protein induced by zinc and pH. <i> Kunihara T, Hayashi Y, Arai M. </i> Biochem Biophys Res Commun, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000019","term_name":"disorder to pre-molten globule","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03535r006","statement":[{"text":"These results indicate that Tat loses residual helices, which were present in the zinc-bound form, and turns into disordered structures upon removal of zinc ions.","type":"Results"},{"text":"Authors claim the use of the isolate HXB2 however the sequence they report in Figure 1. corresponds to this Uniprot.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-12T10:36:04.510Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":1,"end":86,"reference_id":"30600181","reference_source":"pmid","reference_html":"Conformational diversity in the intrinsically disordered HIV-1 Tat protein induced by zinc and pH. <i> Kunihara T, Hayashi Y, Arai M. </i> Biochem Biophys Res Commun, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"ChEBI","id":"29105","partner_start":null,"partner_end":null}],"region_id":"DP03535r007","statement":[{"text":"The ICP-MS measurement revealed that 59.2 ± 0.8 μM zinc ions were present in 25.0 ± 0.2 μM Tat, indicating that the concentration ratio of Tat to zinc ions was 1:2.","type":"Results"},{"text":"Authors claim the use of the isolate HXB2 however the sequence they report in Figure 1. corresponds to this Uniprot.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-12T10:36:12.252Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":7,"released":"2021_12","sequence":"MEPVDPRLEPWKHPGSQPKTACTNCYCKKCCFHCQVCFITKALGISYGRKKRRQRRRPPQGSQTHQVSLSKQPTSQSRGDPTGPKE","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"dataset":["Viral proteins","RNA-binding proteins"],"uniref50":"UniRef50_P04608","uniref90":"UniRef90_P04610","uniref100":"UniRef100_P69697","genes":[{"name":{"value":"tat","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04079","url":"https://hamap.expasy.org/unirule/MF_04079"}}]}}],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":86,"type":"T"}],"Structural state":[{"start":1,"end":86,"type":"D"}],"Structural transition":[{"start":1,"end":86,"type":"T"}],"Molecular function":[{"start":1,"end":86,"type":"F"}]}},{"disprot_id":"DP03536","acc":"Q05318","creator":"fquaglia","date":"2021-11-11T10:21:17.764Z","features":{"pfam":[{"id":"PF00946","name":"Mononegavirales RNA dependent RNA polymerase","start":10,"end":1089},{"id":"PF14318","name":"Mononegavirales mRNA-capping region V","start":1105,"end":1357}],"gene3D":[]},"length":2212,"name":"RNA-directed RNA polymerase L","ncbi_taxon_id":128952,"organism":"Zaire ebolavirus (strain Mayinga-76)","regions":[{"start":1306,"end":1593,"reference_id":"21041632","reference_source":"pmid","reference_html":"Molecular architecture of the vesicular stomatitis virus RNA polymerase. <i> Rahmeh AA, Schenk AD, Danek EI, Kranzusch PJ, Liang B, Liang B, Walz T, Whelan SP. </i> Proc Natl Acad Sci U S A, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03536r001","statement":[{"text":"We favor the hypothesis that CRV (residues 1,069–1,305) constitutes the globule and that the variable region between CRV and CRVI (1,306–1,593) constitutes a largely unstructured hinge region that is not readily discernible by negative stain EM.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T13:08:09.666Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":1306,"end":1593,"reference_id":"21041632","reference_source":"pmid","reference_html":"Molecular architecture of the vesicular stomatitis virus RNA polymerase. <i> Rahmeh AA, Schenk AD, Danek EI, Kranzusch PJ, Liang B, Liang B, Walz T, Whelan SP. </i> Proc Natl Acad Sci U S A, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03536r002","statement":[{"text":"We favor the hypothesis that CRV (residues 1,069–1,305) constitutes the globule and that the variable region between CRV and CRVI (1,306–1,593) constitutes a largely unstructured hinge region that is not readily discernible by negative stain EM.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T13:08:13.238Z"},"ec_go":"IDA","disprot_namespace":"Disorder function"},{"start":1306,"end":1593,"reference_id":"25297996","reference_source":"pmid","reference_html":"Putative domain-domain interactions in the vesicular stomatitis virus L polymerase protein appendage region. <i> Ruedas JB, Perrault J. </i> J Virol, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0097747","term_name":"RNA polymerase activity","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006170","ec_ontology":"ECO","ec_name":"quantitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03536r003","statement":[{"text":"To test whether the bulk of the U region might nonetheless function as a linker, we engineered five additional L protein constructs, each containing an in-frame EGFP insertion at different positions spanning the U segment (positions 1318, 1374, 1472, 1522, and 1577) and assessed effects on polymerase activity along with the wt and the previous construct with the EGFP insertion at position 1595. Surprisingly, none of the newly constructed L-EGFP variants displayed any polymerase activity (Fig. 6). As noted previously for the 1595 construct, all L-EGFP proteins accumulated to levels somewhat lower than the wt, but the reduction was particularly dramatic for the 1522 mutant, which reproducibly accumulated about 10-fold less L protein (Fig. 6), an amount nonetheless sufficient for concluding lack of significant polymerase activity.","type":"Results"},{"text":"Taken together, these findings strongly suggest that the bulk of the U domain does not simply represent an unstructured region between C and M domains but more likely serves some other role in polymerase function.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T13:08:11.807Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Catalysis of the reaction: nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1); the synthesis of RNA from ribonucleotide triphosphates in the presence of a nucleic acid template.\" [GOC:pf]","disprot_namespace":"Disorder function","term_is_binding":false}],"regions_counter":3,"released":"2023_06","sequence":"MATQHTQYPDARLSSPIVLDQCDLVTRACGLYSSYSLNPQLRNCKLPKHIYRLKYDVTVTKFLSDVPVATLPIDFIVPVLLKALSGNGFCPVEPRCQQFLDEIIKYTMQDALFLKYYLKNVGAQEDCVDEHFQEKILSSIQGNEFLHQMFFWYDLAILTRRGRLNRGNSRSTWFVHDDLIDILGYGDYVFWKIPISMLPLNTQGIPHAAMDWYQASVFKEAVQGHTHIVSVSTADVLIMCKDLITCRFNTTLISKIAEIEDPVCSDYPNFKIVSMLYQSGDYLLSILGSDGYKIIKFLEPLCLAKIQLCSKYTERKGRFLTQMHLAVNHTLEEITEMRALKPSQAQKIREFHRTLIRLEMTPQQLCELFSIQKHWGHPVLHSETAIQKVKKHATVLKALRPIVIFETYCVFKYSIAKHYFDSQGSWYSVTSDRNLTPGLNSYIKRNQFPPLPMIKELLWEFYHLDHPPLFSTKIISDLSIFIKDRATAVERTCWDAVFEPNVLGYNPPHKFSTKRVPEQFLEQENFSIENVLSYAQKLEYLLPQYRNFSFSLKEKELNVGRTFGKLPYPTRNVQTLCEALLADGLAKAFPSNMMVVTEREQKESLLHQASWHHTSDDFGEHATVRGSSFVTDLEKYNLAFRYEFTAPFIEYCNRCYGVKNVFNWMHYTIPQCYMHVSDYYNPPHNLTLENRDNPPEGPSSYRGHMGGIEGLQQKLWTSISCAQISLVEIKTGFKLRSAVMGDNQCITVLSVFPLETDADEQEQSAEDNAARVAASLAKVTSACGIFLKPDETFVHSGFIYFGKKQYLNGVQLPQSLKTATRMAPLSDAIFDDLQGTLASIGTAFERSISETRHIFPCRITAAFHTFFSVRILQYHHLGFNKGFDLGQLTLGKPLDFGTISLALAVPQVLGGLSFLNPEKCFYRNLGDPVTSGLFQLKTYLRMIEMDDLFLPLIAKNPGNCTAIDFVLNPSGLNVPGSQDLTSFLRQIVRRTITLSAKNKLINTLFHASADFEDEMVCKWLLSSTPVMSRFAADIFSRTPSGKRLQILGYLEGTRTLLASKIINNNTETPVLDRLRKITLQRWSLWFSYLDHCDNILAEALTQITCTVDLAQILREYSWAHILEGRPLIGATLPCMIEQFKVFWLKPYEQCPQCSNAKQPGGKPFVSVAVKKHIVSAWPNASRISWTIGDGIPYIGSRTEDKIGQPAIKPKCPSAALREAIELASRLTWVTQGSSNSDLLIKPFLEARVNLSVQEILQMTPSHYSGNIVHRYNDQYSPHSFMANRMSNSATRLIVSTNTLGEFSGGGQSARDSNIIFQNVINYAVALFDIKFRNTEATDIQYNRAHLHLTKCCTREVPAQYLTYTSTLDLDLTRYRENELIYDSNPLKGGLNCNISFDNPFFQGKRLNIIEDDLIRLPHLSGWELAKTIMQSIISDSNNSSTDPISSGETRSFTTHFLTYPKIGLLYSFGAFVSYYLGNTILRTKKLTLDNFLYYLTTQIHNLPHRSLRILKPTFKHASVMSRLMSIDPHFSIYIGGAAGDRGLSDAARLFLRTSISSFLTFVKEWIINRGTIVPLWIVYPLEGQNPTPVNNFLYQIVELLVHDSSRQQAFKTTISDHVHPHDNLVYTCKSTASNFFHASLAYWRSRHRNSNRKYLARDSSTGSSTNNSDGHIERSQEQTTRDPHDGTERNLVLQMSHEIKRTTIPQENTHQGPSFQSFLSDSACGTANPKLNFDRSRHNVKFQDHNSASKREGHQIISHRLVLPFFTLSQGTRQLTSSNESQTQDEISKYLRQLRSVIDTTVYCRFTGIVSSMHYKLDEVLWEIESFKSAVTLAEGEGAGALLLIQKYQVKTLFFNTLATESSIESEIVSGMTTPRMLLPVMSKFHNDQIEIILNNSASQITDITNPTWFKDQRARLPKQVEVITMDAETTENINRSKLYEAVYKLILHHIDPSVLKAVVLKVFLSDTEGMLWLNDNLAPFFATGYLIKPITSSARSSEWYLCLTNFLSTTRKMPHQNHLSCKQVILTALQLQIQRSPYWLSHLTQYADCELHLSYIRLGFPSLEKVLYHRYNLVDSKRGPLVSITQHLAHLRAEIRELTNDYNQQRQSRTQTYHFIRTAKGRITKLVNDYLKFFLIVQALKHNGTWQAEFKKLPELISVCNRFYHIRDCNCEERFLVQTLYLHRMQDSEVKLIERLTGLLSLFPDGLYRFD","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Filoviridae","Ebolavirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_Q05318","uniref90":"UniRef90_Q05318","uniref100":"UniRef100_Q05318","genes":[{"name":{"value":"L"}}],"disorder_content":0.1301989150090416,"disprot_consensus":{"full":[{"start":1306,"end":1593,"type":"D"}],"Structural state":[{"start":1306,"end":1593,"type":"D"}],"Disorder function":[{"start":1306,"end":1593,"type":"F"}],"Molecular function":[{"start":1306,"end":1593,"type":"F"}]}},{"disprot_id":"DP03537","acc":"Q05320","creator":"fquaglia","date":"2021-11-11T11:00:59.183Z","features":{"pfam":[{"id":"PF01611","name":"Filovirus glycoprotein","start":15,"end":348},{"id":"PF22307","name":"Envelope glycoprotein GP2-like, HR1-HR2","start":515,"end":595}],"gene3D":[]},"length":676,"name":"Envelope glycoprotein","ncbi_taxon_id":128952,"organism":"Zaire ebolavirus (strain Mayinga-76)","regions":[{"start":524,"end":539,"reference_id":"17545161","reference_source":"pmid","reference_html":"Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts. <i> Freitas MS, Gaspar LP, Lorenzoni M, Almeida FCL, Tinoco LW, Almeida MS, Maia LF, Degrève L, Valente AP, Silva JL. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03537r001","sequence_construct":"GAAIGLAWIPYFGPAA","statement":[{"text":"As shown in Fig. 1A, the peptide assumes a random-coil conformation in aqueous buffer and a more defined structure in the presence of SDS micelles, where it displays a typical helical structure.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:23:43.169Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":524,"end":539,"reference_id":"17545161","reference_source":"pmid","reference_html":"Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts. <i> Freitas MS, Gaspar LP, Lorenzoni M, Almeida FCL, Tinoco LW, Almeida MS, Maia LF, Degrève L, Valente AP, Silva JL. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03537r002","sample":[{"term_id":"IDPO:00489","term_name":"interacting membrane","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":10,"db":"ChEBI","id":"8984","statements":[{"type":"Figure","text":"The SDS and peptide concentrations were 10 mm and 100 μm, respectively."}],"entry_name":"sodium dodecyl sulfate"}],"sequence_construct":"GAAIGLAWIPYFGPAA","statement":[{"text":"As shown in Fig. 1A, the peptide assumes a random-coil conformation in aqueous buffer and a more defined structure in the presence of SDS micelles, where it displays a typical helical structure.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:23:36.030Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":524,"end":539,"reference_id":"17545161","reference_source":"pmid","reference_html":"Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts. <i> Freitas MS, Gaspar LP, Lorenzoni M, Almeida FCL, Tinoco LW, Almeida MS, Maia LF, Degrève L, Valente AP, Silva JL. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03537r003","sample":[{"term_id":"IDPO:00489","term_name":"interacting membrane","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":10,"db":"ChEBI","id":"8984","statements":[{"type":"Figure","text":"The SDS and peptide concentrations were 10 mm and 100 μm, respectively."}],"entry_name":"sodium dodecyl sulfate"}],"sequence_construct":"GAAIGLAWIPYFGPAA","statement":[{"text":"As shown in Fig. 1A, the peptide assumes a random-coil conformation in aqueous buffer and a more defined structure in the presence of SDS micelles, where it displays a typical helical structure.","type":"Results"}],"states_connection":[{"source":"DP03537r001","target":"DP03537r002"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:23:52.213Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":524,"end":539,"reference_id":"17545161","reference_source":"pmid","reference_html":"Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts. <i> Freitas MS, Gaspar LP, Lorenzoni M, Almeida FCL, Tinoco LW, Almeida MS, Maia LF, Degrève L, Valente AP, Silva JL. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"ChEBI","id":"8984","partner_start":null,"partner_end":null}],"region_id":"DP03537r004","sequence_construct":"GAAIGLAWIPYFGPAA","statement":[{"text":"As shown in Fig. 1A, the peptide assumes a random-coil conformation in aqueous buffer and a more defined structure in the presence of SDS micelles, where it displays a typical helical structure.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:25:36.848Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":524,"end":539,"reference_id":"17545161","reference_source":"pmid","reference_html":"Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts. <i> Freitas MS, Gaspar LP, Lorenzoni M, Almeida FCL, Tinoco LW, Almeida MS, Maia LF, Degrève L, Valente AP, Silva JL. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03537r005","sequence_construct":"GAAIGLAWIPYFGPAA","statement":[{"text":"Fluorescence emission in the absence of SDS shows a maximum emission wavelength of ∼337 nm (Fig. 1B). This maximum reflects the tryptophan accessibility and the peptide aggregation because of its high hydrophobicity and random structure.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:23:38.542Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":524,"end":539,"reference_id":"17545161","reference_source":"pmid","reference_html":"Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts. <i> Freitas MS, Gaspar LP, Lorenzoni M, Almeida FCL, Tinoco LW, Almeida MS, Maia LF, Degrève L, Valente AP, Silva JL. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"ChEBI","id":"8984","partner_start":null,"partner_end":null}],"region_id":"DP03537r006","sample":[{"term_id":"IDPO:00489","term_name":"interacting membrane","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":10,"db":"ChEBI","id":"8984","entry_name":"sodium dodecyl sulfate"}],"sequence_construct":"GAAIGLAWIPYFGPAA","statement":[{"text":"In fact, when EBO16 was incubated with SDS micelles, the spectral peak was blue-shifted from 337 to 324 nm (Fig. 1B). The shift of about 13 nm suggests that tryptophan enters a hydrophobic environment in the SDS micelles.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:24:10.455Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":524,"end":539,"reference_id":"17545161","reference_source":"pmid","reference_html":"Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts. <i> Freitas MS, Gaspar LP, Lorenzoni M, Almeida FCL, Tinoco LW, Almeida MS, Maia LF, Degrève L, Valente AP, Silva JL. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006329","ec_ontology":"ECO","ec_name":"static fluorescence quenching evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"ChEBI","id":"8984","partner_start":null,"partner_end":null}],"region_id":"DP03537r007","sample":[{"term_id":"IDPO:00489","term_name":"interacting membrane","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":10,"db":"ChEBI","id":"8984","entry_name":"sodium dodecyl sulfate"}],"sequence_construct":"GAAIGLAWIPYFGPAA","statement":[{"text":"In the absence of SDS micelles, a steep slope is observed (Ksv = 15.8 m-1), whereas in the presence of SDS micelles a reduced slope is obtained (Ksv = 10.2 m-1). The fluorescence data clearly indicate that the single Trp of EBO16 is protected by the micelle from quenching. EBO16 in the micellar environment undergoes structural modifications including intramolecular rearrangements and acquisition of helical structure, showing a tendency to self-associate.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:24:08.553Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":524,"end":539,"reference_id":"17545161","reference_source":"pmid","reference_html":"Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts. <i> Freitas MS, Gaspar LP, Lorenzoni M, Almeida FCL, Tinoco LW, Almeida MS, Maia LF, Degrève L, Valente AP, Silva JL. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"BMRB","id":"11004"},{"db":"PDB","id":"2RLJ"}],"interaction_partner":[{"db":"ChEBI","id":"8984","partner_start":null,"partner_end":null}],"region_id":"DP03537r008","sample":[{"term_id":"IDPO:00489","term_name":"interacting membrane","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":10,"db":"ChEBI","id":"8984","entry_name":"sodium dodecyl sulfate"}],"sequence_construct":"GAAIGLAWIPYFGPAA","statement":[{"text":"Taken together, the NOE connectivities and chemical shift deviation data support the presence of a helix from Leu-6 to Phe-12 (Fig. 2, A and B). This was also observed in 40, 100, and 200 mm SDS, which confirms a stable interaction between the peptide and SDS at concentrations above the critical micellar concentration (data not shown).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:24:02.878Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":524,"end":539,"reference_id":"17545161","reference_source":"pmid","reference_html":"Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts. <i> Freitas MS, Gaspar LP, Lorenzoni M, Almeida FCL, Tinoco LW, Almeida MS, Maia LF, Degrève L, Valente AP, Silva JL. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03537r009","sequence_construct":"GAAIGLAWIPYFGPAA","statement":[{"text":"Because EBO16 is very flexible when free in solution, it did not show NOEs during the 80 ms of mixing time.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:23:24.541Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":529,"end":535,"reference_id":"17545161","reference_source":"pmid","reference_html":"Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts. <i> Freitas MS, Gaspar LP, Lorenzoni M, Almeida FCL, Tinoco LW, Almeida MS, Maia LF, Degrève L, Valente AP, Silva JL. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03537r010","sequence_construct":"GAAIGLAWIPYFGPAA","statement":[{"text":"The NOESY spectrum of EBO16 in the presence of DRMs showed transfer NOEs for all residues ranging from Leu-6 to Phe-12 (Fig. 4A). We also observed transferred NOEs for the residues ranging from Leu-6 to Ile-9 for EBO16 in the presence of LUVs containing PC/PE/PI/Cho.","type":"Results"},{"text":"LUV stands for large unilamellar vesicle, while DRM stands for detergent-resistant membrane fraction, which where obtained from cells.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:23:57.500Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":524,"end":539,"reference_id":"17545161","reference_source":"pmid","reference_html":"Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts. <i> Freitas MS, Gaspar LP, Lorenzoni M, Almeida FCL, Tinoco LW, Almeida MS, Maia LF, Degrève L, Valente AP, Silva JL. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0046718","term_name":"viral entry into host cell","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03537r011","sequence_construct":"GAAIGLAWIPYFGPAA","statement":[{"text":"The NOESY spectrum of EBO16 in the presence of DRMs showed transfer NOEs for all residues ranging from Leu-6 to Phe-12 (Fig. 4A). We also observed transferred NOEs for the residues ranging from Leu-6 to Ile-9 for EBO16 in the presence of LUVs containing PC/PE/PI/Cho.","type":"Results"},{"text":"LUV stands for large unilamellar vesicle, while DRM stands for detergent-resistant membrane fraction, which where obtained from cells.","type":"Curator statement"},{"text":" These data are the first indication that EBO16 can interact with DRMs in an early stage of infection.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:25:53.074Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Viral attachment to the host cell is not part of viral entry in GO because virus attachment does not always lead to viral entry: attachment can also result in the virion being carried by the host cell to another location.","term_def":"\"The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":190,"end":212,"reference_id":"18615077","reference_source":"pmid","reference_html":"Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor. <i> Lee JE, Fusco ML, Hessell AJ, Oswald WB, Burton DR, Saphire EO. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3CSY"}],"region_id":"DP03537r012","statement":[{"text":"No electron density is observed for residues 190-213, 311-312, 464-501 and 600-632. Weak or discontinuous electron density is seen in the loop containing the GP1-GP2 disulfide bridge (residues 49-56) and the outer regions of the GP1 glycan cap (residues 268-278 and 299-310); these regions are modeled as poly-alanine fragments.","type":"Results"},{"text":"Chain O shown in the PDB, lacks electron density up to the 212 residue, for this reason the disorder region is describe in the 190-212 region.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr42Val","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"In an effort to increase sample homogeneity and solubility, deletion of the mucin-like and transmembrane domains (residues 312-462 and 633-676) and mutations of two N-linked glycosylation sites (T42V and T230V) were created by overlap PCR and the QuikChange II site-directed mutagenesis kit, respectively. "}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr230Val","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"In an effort to increase sample homogeneity and solubility, deletion of the mucin-like and transmembrane domains (residues 312-462 and 633-676) and mutations of two N-linked glycosylation sites (T42V and T230V) were created by overlap PCR and the QuikChange II site-directed mutagenesis kit, respectively. "}]}],"sequence_construct":"YPYDVPDYAIEGRGARSIPLGVIHNSVLQVSDVDKLVCRDKLSSTNQLRSVGLNLEGNGVATDVPSATKRWGFRSGVPPKVVNYEAGEWAENCYNLEIKKPDGSECLPAAPDGIRGFPRCRYVHKVSGTGPCAGDFAFHKEGAFFLYDRLASTVIYRGTTFAEGVVAFLILPQAKKDFFSSHPLREPVNATEDPSSGYYSTTIRYQATGFGTNEVEYLFEVDNLTYVQLESRFTPQFLLQLNETIYTSGKRSNTTGKLIWKVNPEIDTTIGEWAFWETKKNLTRKIRSEELSFTVVTHHQDTGEESASSGKLGLITNTIAGVAGLITGGRRTRR","sample":[{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ABCD","id":"ABCD_AD747"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:19:31.584Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":279,"end":298,"reference_id":"18615077","reference_source":"pmid","reference_html":"Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor. <i> Lee JE, Fusco ML, Hessell AJ, Oswald WB, Burton DR, Saphire EO. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3CSY"}],"region_id":"DP03537r013","statement":[{"text":"No electron density is observed for residues 190-213, 311-312, 464-501 and 600-632. Weak or discontinuous electron density is seen in the loop containing the GP1-GP2 disulfide bridge (residues 49-56) and the outer regions of the GP1 glycan cap (residues 268-278 and 299-310); these regions are modeled as poly-alanine fragments.","type":"Results"},{"text":"As shown in the PDB, the region 279-298 lacks electron density.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr42Val","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"In an effort to increase sample homogeneity and solubility, deletion of the mucin-like and transmembrane domains (residues 312-462 and 633-676) and mutations of two N-linked glycosylation sites (T42V and T230V) were created by overlap PCR and the QuikChange II site-directed mutagenesis kit, respectively. "}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr230Val","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"In an effort to increase sample homogeneity and solubility, deletion of the mucin-like and transmembrane domains (residues 312-462 and 633-676) and mutations of two N-linked glycosylation sites (T42V and T230V) were created by overlap PCR and the QuikChange II site-directed mutagenesis kit, respectively. "}]}],"sequence_construct":"YPYDVPDYAIEGRGARSIPLGVIHNSVLQVSDVDKLVCRDKLSSTNQLRSVGLNLEGNGVATDVPSATKRWGFRSGVPPKVVNYEAGEWAENCYNLEIKKPDGSECLPAAPDGIRGFPRCRYVHKVSGTGPCAGDFAFHKEGAFFLYDRLASTVIYRGTTFAEGVVAFLILPQAKKDFFSSHPLREPVNATEDPSSGYYSTTIRYQATGFGTNEVEYLFEVDNLTYVQLESRFTPQFLLQLNETIYTSGKRSNTTGKLIWKVNPEIDTTIGEWAFWETKKNLTRKIRSEELSFTVVTHHQDTGEESASSGKLGLITNTIAGVAGLITGGRRTRR","sample":[{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ABCD","id":"ABCD_AD747"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T13:21:07.425Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":465,"end":501,"reference_id":"18615077","reference_source":"pmid","reference_html":"Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor. <i> Lee JE, Fusco ML, Hessell AJ, Oswald WB, Burton DR, Saphire EO. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr42Val","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"In an effort to increase sample homogeneity and solubility, deletion of the mucin-like and transmembrane domains (residues 312-462 and 633-676) and mutations of two N-linked glycosylation sites (T42V and T230V) were created by overlap PCR and the QuikChange II site-directed mutagenesis kit, respectively. "}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr230Val","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"In an effort to increase sample homogeneity and solubility, deletion of the mucin-like and transmembrane domains (residues 312-462 and 633-676) and mutations of two N-linked glycosylation sites (T42V and T230V) were created by overlap PCR and the QuikChange II site-directed mutagenesis kit, respectively. "}]}],"cross_refs":[{"db":"PDB","id":"3CSY"}],"region_id":"DP03537r014","sequence_construct":"YPYDVPDYAIEGRGARSIPLGVIHNSVLQVSDVDKLVCRDKLSSTNQLRSVGLNLEGNGVATDVPSATKRWGFRSGVPPKVVNYEAGEWAENCYNLEIKKPDGSECLPAAPDGIRGFPRCRYVHKVSGTGPCAGDFAFHKEGAFFLYDRLASTVIYRGTTFAEGVVAFLILPQAKKDFFSSHPLREPVNATEDPSSGYYSTTIRYQATGFGTNEVEYLFEVDNLTYVQLESRFTPQFLLQLNETIYTSGKRSNTTGKLIWKVNPEIDTTIGEWAFWETKKNLTRKIRSEELSFTVVTHHQDTGEESASSGKLGLITNTIAGVAGLITGGRRTRR","statement":[{"text":"No electron density is observed for residues 190-213, 311-312, 464-501 and 600-632. Weak or discontinuous electron density is seen in the loop containing the GP1-GP2 disulfide bridge (residues 49-56) and the outer regions of the GP1 glycan cap (residues 268-278 and 299-310); these regions are modeled as poly-alanine fragments.","type":"Results"},{"text":"As shown in the PDB, the region 465-501 lacks electron density.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ABCD","id":"ABCD_AD747"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T13:11:48.582Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":524,"end":539,"reference_id":"17545161","reference_source":"pmid","reference_html":"Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts. <i> Freitas MS, Gaspar LP, Lorenzoni M, Almeida FCL, Tinoco LW, Almeida MS, Maia LF, Degrève L, Valente AP, Silva JL. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0046718","term_name":"viral entry into host cell","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03537r015","statement":[{"text":"In fact, when EBO16 was incubated with SDS micelles, the spectral peak was blue-shifted from 337 to 324 nm (Fig. 1B). The shift of about 13 nm suggests that tryptophan enters a hydrophobic environment in the SDS micelles.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:25:40.840Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Viral attachment to the host cell is not part of viral entry in GO because virus attachment does not always lead to viral entry: attachment can also result in the virion being carried by the host cell to another location.","term_def":"\"The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":632,"end":641,"reference_id":"28874543","reference_source":"pmid","reference_html":"Structure of the Ebola virus envelope protein MPER/TM domain and its interaction with the fusion loop explains their fusion activity. <i> Lee J, Nyenhuis DA, Nelson EA, Cafiso DS, White JM, Tamm LK. </i> Proc Natl Acad Sci U S A, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"5T42"},{"db":"DisProt","id":"DP03538r001"}],"region_id":"DP03537r017","statement":[{"text":"IDR is 100% identical to the Zaire ebolavirus Kikwit-95 strain (DP035378) assessed in this publication.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":17,"released":"2021_12","sequence":"MGVTGILQLPRDRFKRTSFFLWVIILFQRTFSIPLGVIHNSTLQVSDVDKLVCRDKLSSTNQLRSVGLNLEGNGVATDVPSATKRWGFRSGVPPKVVNYEAGEWAENCYNLEIKKPDGSECLPAAPDGIRGFPRCRYVHKVSGTGPCAGDFAFHKEGAFFLYDRLASTVIYRGTTFAEGVVAFLILPQAKKDFFSSHPLREPVNATEDPSSGYYSTTIRYQATGFGTNETEYLFEVDNLTYVQLESRFTPQFLLQLNETIYTSGKRSNTTGKLIWKVNPEIDTTIGEWAFWETKKNLTRKIRSEELSFTVVSNGAKNISGQSPARTSSDPGTNTTTEDHKIMASENSSAMVQVHSQGREAAVSHLTTLATISTSPQSLTTKPGPDNSTHNTPVYKLDISEATQVEQHHRRTDNDSTASDTPSATTAAGPPKAENTNTSKSTDFLDPATTTSPQNHSETAGNNNTHHQDTGEESASSGKLGLITNTIAGVAGLITGGRRTRREAIVNAQPKCNPNLHYWTTQDEGAAIGLAWIPYFGPAAEGIYIEGLMHNQDGLICGLRQLANETTQALQLFLRATTELRTFSILNRKAIDFLLQRWGGTCHILGPDCCIEPHDWTKNITDKIDQIIHDFVDKTLPDQGDNDNWWTGWRQWIPAGIGVTGVIIAVIALFCICKFVF","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Filoviridae","Ebolavirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_Q05320","uniref90":"UniRef90_Q05320","uniref100":"UniRef100_Q05320","genes":[{"name":{"value":"GP"}}],"disorder_content":0.15680473372781065,"disprot_consensus":{"full":[{"start":190,"end":212,"type":"D"},{"start":279,"end":298,"type":"D"},{"start":465,"end":501,"type":"D"},{"start":524,"end":539,"type":"T"},{"start":632,"end":641,"type":"D"}],"Structural state":[{"start":190,"end":212,"type":"D"},{"start":279,"end":298,"type":"D"},{"start":465,"end":501,"type":"D"},{"start":524,"end":539,"type":"D"},{"start":632,"end":641,"type":"D"}],"Structural transition":[{"start":524,"end":539,"type":"T"}],"Molecular function":[{"start":524,"end":539,"type":"F"}],"Biological process":[{"start":524,"end":539,"type":"F"}]}},{"disprot_id":"DP03538","acc":"P87666","creator":"fquaglia","date":"2021-11-11T11:02:22.350Z","features":{"pfam":[{"id":"PF01611","name":"Filovirus glycoprotein","start":15,"end":348},{"id":"PF22307","name":"Envelope glycoprotein GP2-like, HR1-HR2","start":515,"end":595}],"gene3D":[]},"length":676,"name":"Envelope glycoprotein","ncbi_taxon_id":128951,"organism":"Zaire ebolavirus (strain Kikwit-95)","regions":[{"start":632,"end":641,"reference_id":"28874543","reference_source":"pmid","reference_html":"Structure of the Ebola virus envelope protein MPER/TM domain and its interaction with the fusion loop explains their fusion activity. <i> Lee J, Nyenhuis DA, Nelson EA, Cafiso DS, White JM, Tamm LK. </i> Proc Natl Acad Sci U S A, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"5T42"}],"region_id":"DP03538r001","statement":[{"text":"We found that, independent of pH, EBOV MPER/TM consists of an unstructured N-terminal region and a short helix in the MPER region that is followed by a turn and the TM helix: i.e., MPER/TM forms a helix-turn-helix motif.","type":"Results"},{"text":"The ensemble is characterized by an unstructured N-terminal region (residues D632 to N641), a helical MPER region (D642 to Q650), a turn (W651 to I656), and a TM helical region (G657 to F676).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:26:18.584Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":524,"end":539,"reference_id":"17545161","reference_source":"pmid","reference_html":"Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts. <i> Freitas MS, Gaspar LP, Lorenzoni M, Almeida FCL, Tinoco LW, Almeida MS, Maia LF, Degrève L, Valente AP, Silva JL. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"DisProt","id":"DP03537r009"}],"region_id":"DP03538r002","statement":[{"text":"IDR is 100% identical to the Zaire ebolavirus \nMayinga-76 strain (DP03537) assessed in this publication.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:26:15.671Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":524,"end":539,"reference_id":"17545161","reference_source":"pmid","reference_html":"Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts. <i> Freitas MS, Gaspar LP, Lorenzoni M, Almeida FCL, Tinoco LW, Almeida MS, Maia LF, Degrève L, Valente AP, Silva JL. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"DisProt","id":"DP03537r005"}],"region_id":"DP03538r003","statement":[{"text":"IDR is 100% identical to the Zaire ebolavirus \nMayinga-76 strain (DP03537) assessed in this publication.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:26:12.246Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":524,"end":539,"reference_id":"17545161","reference_source":"pmid","reference_html":"Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts. <i> Freitas MS, Gaspar LP, Lorenzoni M, Almeida FCL, Tinoco LW, Almeida MS, Maia LF, Degrève L, Valente AP, Silva JL. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"DisProt","id":"DP03537r002"}],"region_id":"DP03538r004","statement":[{"text":"IDR is 100% identical to the Zaire ebolavirus \nMayinga-76 strain (DP03537) assessed in this publication.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00489","term_name":"interacting membrane","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":10,"db":"ChEBI","id":"8984","entry_name":"sodium dodecyl sulfate"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:26:11.142Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":524,"end":539,"reference_id":"17545161","reference_source":"pmid","reference_html":"Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts. <i> Freitas MS, Gaspar LP, Lorenzoni M, Almeida FCL, Tinoco LW, Almeida MS, Maia LF, Degrève L, Valente AP, Silva JL. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"DisProt","id":"DP03537r001"}],"region_id":"DP03538r005","statement":[{"text":"IDR is 100% identical to the Zaire ebolavirus \nMayinga-76 strain (DP03537) assessed in this publication.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:26:09.793Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":524,"end":539,"reference_id":"17545161","reference_source":"pmid","reference_html":"Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts. <i> Freitas MS, Gaspar LP, Lorenzoni M, Almeida FCL, Tinoco LW, Almeida MS, Maia LF, Degrève L, Valente AP, Silva JL. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"DisProt","id":"DP03537r003"}],"region_id":"DP03538r006","statement":[{"text":"IDR is 100% identical to the Zaire ebolavirus \nMayinga-76 strain (DP03537) assessed in this publication.","type":"Curator statement"}],"states_connection":[{"source":"DP03538r005","target":"DP03538r004"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:28:15.780Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":524,"end":539,"reference_id":"17545161","reference_source":"pmid","reference_html":"Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts. <i> Freitas MS, Gaspar LP, Lorenzoni M, Almeida FCL, Tinoco LW, Almeida MS, Maia LF, Degrève L, Valente AP, Silva JL. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0007759","ec_ontology":"ECO","ec_name":"curator inference from database used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2RLJ"},{"db":"BMRB","id":"11004"},{"db":"DisProt","id":"DP03537r004"},{"db":"DisProt","id":"DP03537r006"},{"db":"DisProt","id":"DP03537r007"},{"db":"DisProt","id":"DP03537r008"}],"interaction_partner":[{"db":"ChEBI","id":"8984","partner_start":null,"partner_end":null}],"region_id":"DP03538r007","statement":[{"text":"IDR is 100% identical to the Zaire ebolavirus \nMayinga-76 strain (DP03537) assessed in this publication.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:28:18.813Z"},"ec_go":"IC","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":529,"end":535,"reference_id":"17545161","reference_source":"pmid","reference_html":"Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts. <i> Freitas MS, Gaspar LP, Lorenzoni M, Almeida FCL, Tinoco LW, Almeida MS, Maia LF, Degrève L, Valente AP, Silva JL. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"DisProt","id":"DP03537r010"}],"region_id":"DP03538r008","statement":[{"text":"IDR is 100% identical to the Zaire ebolavirus Mayinga-76 strain (DP03537) assessed in this publication.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:28:17.564Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":524,"end":539,"reference_id":"17545161","reference_source":"pmid","reference_html":"Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts. <i> Freitas MS, Gaspar LP, Lorenzoni M, Almeida FCL, Tinoco LW, Almeida MS, Maia LF, Degrève L, Valente AP, Silva JL. </i> J Biol Chem, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0046718","term_name":"viral entry into host cell","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0007759","ec_ontology":"ECO","ec_name":"curator inference from database used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"DisProt","id":"DP03537r016"},{"db":"DisProt","id":"DP03537r015"},{"db":"DisProt","id":"DP03537r011"}],"region_id":"DP03538r009","statement":[{"text":"IDR is 100% identical to the Zaire ebolavirus Mayinga-76 strain (DP03537) assessed in this publication.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:28:20.270Z"},"ec_go":"IC","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"Viral attachment to the host cell is not part of viral entry in GO because virus attachment does not always lead to viral entry: attachment can also result in the virion being carried by the host cell to another location.","term_def":"\"The process that occurs after viral attachment by which a virus, or viral nucleic acid, breaches the plasma membrane or cell envelope and enters the host cell. The process ends when the viral nucleic acid is released into the host cell cytoplasm.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":190,"end":212,"reference_id":"18615077","reference_source":"pmid","reference_html":"Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor. <i> Lee JE, Fusco ML, Hessell AJ, Oswald WB, Burton DR, Saphire EO. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"DisProt","id":"DP03537r012"},{"db":"PDB","id":"3CSY"}],"region_id":"DP03538r010","statement":[{"text":"IDR is 100% identical to the Zaire ebolavirus Mayinga-76 strain (DP03537) assessed in this publication.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:26:08.751Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":279,"end":298,"reference_id":"18615077","reference_source":"pmid","reference_html":"Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor. <i> Lee JE, Fusco ML, Hessell AJ, Oswald WB, Burton DR, Saphire EO. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"DisProt","id":"DP03537r013"},{"db":"PDB","id":"3CSY"}],"region_id":"DP03538r011","statement":[{"text":"IDR is 100% identical to the Zaire ebolavirus Mayinga-76 strain (DP03537) assessed in this publication.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:26:07.837Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":11,"released":"2021_12","sequence":"MGVTGILQLPRDRFKRTSFFLWVIILFQRTFSIPLGVIHNSTLQVSDVDKLVCRDKLSSTNQLRSVGLNLEGNGVATDVPSATKRWGFRSGVPPKVVNYEAGEWAENCYNLEIKKPDGSECLPAAPDGIRGFPRCRYVHKVSGTGPCAGDFAFHKEGAFFLYDRLASTVIYRGTTFAEGVVAFLILPQAKKDFFSSHPLREPVNATEDPSSGYYSTTIRYQATGFGTNETEYLFEVDNLTYVQLESRFTPQFLLQLNETIYTSGKRSNTTGKLIWKVNPEIDTTIGEWAFWETKKNLTRKIRSEELSFTAVSNRAKNISGQSPARTSSDPGTNTTTEDHKIMASENSSAMVQVHSQGREAAVSHLTTLATISTSPQPPTTKPGPDNSTHNTPVYKLDISEATQVEQHHRRTDNDSTASDTPPATTAAGPLKAENTNTSKGTDLLDPATTTSPQNHSETAGNNNTHHQDTGEESASSGKLGLITNTIAGVAGLITGGRRARREAIVNAQPKCNPNLHYWTTQDEGAAIGLAWIPYFGPAAEGIYTEGLMHNQDGLICGLRQLANETTQALQLFLRATTELRTFSILNRKAIDFLLQRWGGTCHILGPDCCIEPHDWTKNITDKIDQIIHDFVDKTLPDQGDNDNWWTGWRQWIPAGIGVTGVIIAVIALFCICKFVF","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Filoviridae","Ebolavirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_Q05320","uniref90":"UniRef90_Q05320","uniref100":"UniRef100_P87666","genes":[{"name":{"value":"GP"}}],"disorder_content":0.10207100591715976,"disprot_consensus":{"full":[{"start":190,"end":212,"type":"D"},{"start":279,"end":298,"type":"D"},{"start":524,"end":539,"type":"T"},{"start":632,"end":641,"type":"D"}],"Structural state":[{"start":190,"end":212,"type":"D"},{"start":279,"end":298,"type":"D"},{"start":524,"end":539,"type":"D"},{"start":632,"end":641,"type":"D"}],"Structural transition":[{"start":524,"end":539,"type":"T"}],"Molecular function":[{"start":524,"end":539,"type":"F"}],"Biological process":[{"start":524,"end":539,"type":"F"}]}},{"disprot_id":"DP03539","acc":"A0A097F4I8","creator":"fquaglia","date":"2021-11-11T14:43:30.928Z","features":{"pfam":[{"id":"PF03854","name":"P-11 zinc finger","start":27,"end":76}],"gene3D":[]},"length":99,"name":"RING finger protein Z","ncbi_taxon_id":11620,"organism":"Lassa mammarenavirus","regions":[{"start":1,"end":24,"reference_id":"34127846","reference_source":"pmid","reference_html":"Cryo-EM structures of Lassa and Machupo virus polymerases complexed with cognate regulatory Z proteins identify targets for antivirals. <i> Xu X, Peng R, Peng Q, Wang M, Xu Y, Liu S, Tian X, Deng H, Tong Y, Hu X, Zhong J, Wang P, Qi J, Gao GF, Shi Y. </i> Nat Microbiol, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03539r001","statement":[{"text":"Importantly, both the N- and C-terminal arms of the Z protein remain highly flexible when bound to the L polymerase, which offers an opportunity for the Z protein to simultaneously interact with multiple binding partners.","type":"Results"},{"text":"The Z protein consists of a stable central RING domain and two flexible arms in the amino (N) and C termini","type":"Results"}],"cross_refs":[{"db":"PDB","id":"7ELA"},{"db":"EMDB","id":"EMD-31178"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-01T13:51:04.650Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":74,"end":99,"reference_id":"34127846","reference_source":"pmid","reference_html":"Cryo-EM structures of Lassa and Machupo virus polymerases complexed with cognate regulatory Z proteins identify targets for antivirals. <i> Xu X, Peng R, Peng Q, Wang M, Xu Y, Liu S, Tian X, Deng H, Tong Y, Hu X, Zhong J, Wang P, Qi J, Gao GF, Shi Y. </i> Nat Microbiol, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03539r002","statement":[{"text":"Importantly, both the N- and C-terminal arms of the Z protein remain highly flexible when bound to the L polymerase, which offers an opportunity for the Z protein to simultaneously interact with multiple binding partners.","type":"Results"},{"text":"The Z protein consists of a stable central RING domain and two flexible arms in the amino (N) and C termini","type":"Results"}],"cross_refs":[{"db":"PDB","id":"7ELA"},{"db":"EMDB","id":"EMD-31178"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-01T13:51:03.653Z"},"ec_go":"IDA","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MGNKQVKAPEARNSPRASLIPDATHLGPQFCKSCWFENKGLVECNNHYLCLNCLTLLLGVSSRCPICKMPLPTRLRPSAAPTAPPAEAGDNTRPPPYSP","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Polyploviricotina","Ellioviricetes","Bunyavirales","Arenaviridae","Mammarenavirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_O73557","uniref90":"UniRef90_A0A097F4I8","uniref100":"UniRef100_A0A097F4I8","genes":[{"name":{"value":"Z","evidences":[{"code":"ECO:0000256","source":{"name":"HAMAP-Rule","id":"MF_04087","url":"https://hamap.expasy.org/unirule/MF_04087"}},{"code":"ECO:0000313","source":{"name":"EMBL","id":"AIT17396.1","url":"https://www.ebi.ac.uk/ena/browser/view/AIT17396.1"}}]}}],"disorder_content":0.5050505050505051,"disprot_consensus":{"full":[{"start":1,"end":24,"type":"D"},{"start":74,"end":99,"type":"D"}],"Structural state":[{"start":1,"end":24,"type":"D"},{"start":74,"end":99,"type":"D"}]}},{"disprot_id":"DP03541","acc":"Q9DQX7","creator":"fquaglia","date":"2021-11-11T15:41:42.726Z","features":{"pfam":[{"id":"PF00843","name":"Arenavirus nucleocapsid N-terminal domain","start":4,"end":339},{"id":"PF17290","name":"Arenavirus nucleocapsid C-terminal domain","start":363,"end":543}],"gene3D":[]},"length":569,"name":"Nucleoprotein","ncbi_taxon_id":11620,"organism":"Lassa mammarenavirus","regions":[{"start":147,"end":157,"reference_id":"21917929","reference_source":"pmid","reference_html":"Structure of the Lassa virus nucleoprotein revealed by X-ray crystallography, small-angle X-ray scattering, and electron microscopy. <i> Brunotte L, Kerber R, Shang W, Hauer F, Hass M, Gabriel M, Lelke M, Busch C, Stark H, Svergun DI, Betzel C, Perbandt M, Günther S. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3R3L"}],"region_id":"DP03541r001","statement":[{"text":"The final model included 513 of the 569 residues (excluding FLAG and His tags) of LASV NP. The regions comprising residues 1–7, 147–157, 339–363, 517–521, and 562–569 were disordered and could not be identified in the electron density.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-01T12:17:55.648Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":339,"end":363,"reference_id":"21917929","reference_source":"pmid","reference_html":"Structure of the Lassa virus nucleoprotein revealed by X-ray crystallography, small-angle X-ray scattering, and electron microscopy. <i> Brunotte L, Kerber R, Shang W, Hauer F, Hass M, Gabriel M, Lelke M, Busch C, Stark H, Svergun DI, Betzel C, Perbandt M, Günther S. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3R3L"}],"region_id":"DP03541r002","statement":[{"text":"The final model included 513 of the 569 residues (excluding FLAG and His tags) of LASV NP. The regions comprising residues 1–7, 147–157, 339–363, 517–521, and 562–569 were disordered and could not be identified in the electron density.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-01T12:17:54.452Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":339,"end":363,"reference_id":"21917929","reference_source":"pmid","reference_html":"Structure of the Lassa virus nucleoprotein revealed by X-ray crystallography, small-angle X-ray scattering, and electron microscopy. <i> Brunotte L, Kerber R, Shang W, Hauer F, Hass M, Gabriel M, Lelke M, Busch C, Stark H, Svergun DI, Betzel C, Perbandt M, Günther S. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3R3L"}],"region_id":"DP03541r003","statement":[{"text":"The final model included 513 of the 569 residues (excluding FLAG and His tags) of LASV NP. The regions comprising residues 1–7, 147–157, 339–363, 517–521, and 562–569 were disordered and could not be identified in the electron density.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-01T12:17:57.442Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":3,"released":"2021_12","sequence":"MSASKEVKSFLWTQSLRRELSGYCSNIKLQVVKDAQALLHGLDFSEVSNVQRLMRKQRRDDSDLKRLRDLNQAVNNLVELKSTQQKSVLRVGTLSSDDLLTLAADLEKLKSKVTRTERPLSSGVYMGNLSSQQLDQRRALLNLIGMTNGSQGSQAGRDGVVRVWDVKNAELLNNQFGTMPSLTLACLTKQGQVDLNDVVQALTDLGLIYTAKYPNTSDLDRLTQSHPILNMIDTKKSSLNISGYNFSLGAAVKAGACMLDGGNMLETIKVSPQSMDGILKSILKVKRALGMFVSDTPGERNPYENILYKICLSGDGWPYIASRTSIVGRAWENTVVDLETDGKPQKIGSGNSNKSLQSAGFSAGLTYSQLMTLKDAMLQLDPNAKTWMDIEGRPEDPVEVALYQPISGCYIHFFREPTDLKQFKQDAKYSHGIDIADLFAAQPGLTSAVIEALPRNMVITCQGSEDIKKLLESQGRKDIKLIDIALSKIDSRKFENAVWDQYKDLCHMHTGVVVEKKKRGGKEEITPHCALMDCIMFDAAVSGGLNTLVLRAVLPRDMVFRTSTPRVVL","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Polyploviricotina","Ellioviricetes","Bunyavirales","Arenaviridae","Mammarenavirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_P13699","uniref90":"UniRef90_P13699","uniref100":"UniRef100_Q9DQX7","genes":[{"name":{"value":"NP","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAG41803.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAG41803.1"}}]},"synonyms":[{"value":"N","evidences":[{"code":"ECO:0000256","source":{"name":"HAMAP-Rule","id":"MF_04085","url":"https://hamap.expasy.org/unirule/MF_04085"}}]}]}],"disorder_content":0.0632688927943761,"disprot_consensus":{"full":[{"start":147,"end":157,"type":"D"},{"start":339,"end":363,"type":"D"}],"Structural state":[{"start":147,"end":157,"type":"D"},{"start":339,"end":363,"type":"D"}],"Disorder function":[{"start":339,"end":363,"type":"F"}]}},{"disprot_id":"DP03542","acc":"P13699","creator":"fquaglia","date":"2021-11-11T16:04:53.413Z","features":{"pfam":[{"id":"PF00843","name":"Arenavirus nucleocapsid N-terminal domain","start":4,"end":339},{"id":"PF17290","name":"Arenavirus nucleocapsid C-terminal domain","start":363,"end":543}],"gene3D":[]},"length":569,"name":"Nucleoprotein","ncbi_taxon_id":11622,"organism":"Lassa virus (strain Mouse/Sierra Leone/Josiah/1976)","regions":[{"start":147,"end":157,"reference_id":"21085117","reference_source":"pmid","reference_html":"Cap binding and immune evasion revealed by Lassa nucleoprotein structure. <i> Qi X, Lan S, Wang W, Schelde LM, Dong H, Wallat GD, Ly H, Liang Y, Dong C. </i> Nature, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3MWP"},{"db":"PDB","id":"3MWT"},{"db":"PDB","id":"3MX2"},{"db":"PDB","id":"3MX5"}],"region_id":"DP03542r001","statement":[{"text":"In the NP protomer structure, 514 residues of the 569-residue LASV NP protein were built into the model (Fig. 1a). The electron densities for residues 1 to 6, 147 to 157, 339 to 363, 518 to 521, 562 to 569 were not well defined.","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-01T12:14:21.200Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":339,"end":363,"reference_id":"21085117","reference_source":"pmid","reference_html":"Cap binding and immune evasion revealed by Lassa nucleoprotein structure. <i> Qi X, Lan S, Wang W, Schelde LM, Dong H, Wallat GD, Ly H, Liang Y, Dong C. </i> Nature, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3MWP"},{"db":"PDB","id":"3MWT"},{"db":"PDB","id":"3MX2"},{"db":"PDB","id":"3MX5"}],"region_id":"DP03542r002","statement":[{"text":"In the NP protomer structure, 514 residues of the 569-residue LASV NP protein were built into the model (Fig. 1a). The electron densities for residues 1 to 6, 147 to 157, 339 to 363, 518 to 521, 562 to 569 were not well defined.","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-01T12:14:22.310Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":339,"end":363,"reference_id":"21085117","reference_source":"pmid","reference_html":"Cap binding and immune evasion revealed by Lassa nucleoprotein structure. <i> Qi X, Lan S, Wang W, Schelde LM, Dong H, Wallat GD, Ly H, Liang Y, Dong C. </i> Nature, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03542r003","statement":[{"text":"In the NP protomer structure, 514 residues of the 569-residue LASV NP protein were built into the model (Fig. 1a). The electron densities for residues 1 to 6, 147 to 157, 339 to 363, 518 to 521, 562 to 569 were not well defined.","type":"Article"},{"text":"Flexible linker connecting the N domain (7-338) and C domain (364-561).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-01T12:14:20.269Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":3,"released":"2021_12","sequence":"MSASKEIKSFLWTQSLRRELSGYCSNIKLQVVKDAQALLHGLDFSEVSNVQRLMRKERRDDNDLKRLRDLNQAVNNLVELKSTQQKSILRVGTLTSDDLLILAADLEKLKSKVIRTERPLSAGVYMGNLSSQQLDQRRALLNMIGMSGGNQGARAGRDGVVRVWDVKNAELLNNQFGTMPSLTLACLTKQGQVDLNDAVQALTDLGLIYTAKYPNTSDLDRLTQSHPILNMIDTKKSSLNISGYNFSLGAAVKAGACMLDGGNMLETIKVSPQTMDGILKSILKVKKALGMFISDTPGERNPYENILYKICLSGDGWPYIASRTSITGRAWENTVVDLESDGKPQKADSNNSSKSLQSAGFTAGLTYSQLMTLKDAMLQLDPNAKTWMDIEGRPEDPVEIALYQPSSGCYIHFFREPTDLKQFKQDAKYSHGIDVTDLFATQPGLTSAVIDALPRNMVITCQGSDDIRKLLESQGRKDIKLIDIALSKTDSRKYENAVWDQYKDLCHMHTGVVVEKKKRGGKEEITPHCALMDCIMFDAAVSGGLNTSVLRAVLPRDMVFRTSTPRVVL","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Polyploviricotina","Ellioviricetes","Bunyavirales","Arenaviridae","Mammarenavirus"],"dataset":["Viral proteins","RNA-binding proteins"],"uniref50":"UniRef50_P13699","uniref90":"UniRef90_P13699","uniref100":"UniRef100_P13699","genes":[{"name":{"value":"N","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04085","url":"https://hamap.expasy.org/unirule/MF_04085"}}]}}],"disorder_content":0.0632688927943761,"disprot_consensus":{"full":[{"start":147,"end":157,"type":"D"},{"start":339,"end":363,"type":"D"}],"Structural state":[{"start":147,"end":157,"type":"D"},{"start":339,"end":363,"type":"D"}],"Disorder function":[{"start":339,"end":363,"type":"F"}]}},{"disprot_id":"DP03543","acc":"Q72500","creator":"ewagner","date":"2021-11-11T16:12:30.407Z","features":{"pfam":[{"id":"PF00522","name":"VPR/VPX protein","start":1,"end":82}],"gene3D":[]},"length":96,"name":"Protein Vpr","ncbi_taxon_id":11676,"organism":"Human immunodeficiency virus 1","regions":[{"start":1,"end":96,"reference_id":"10903315","reference_source":"pmid","reference_html":"Functional and structural characterization of synthetic HIV-1 Vpr that transduces cells, localizes to the nucleus, and induces G2 cell cycle arrest. <i> Henklein P, Bruns K, Sherman MP, Tessmer U, Licha K, Kopp J, de Noronha CM, Greene WC, Wray V, Schubert U. </i> J Biol Chem, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03543r001","statement":[{"text":"Vpr is unstructured at neutral pH, whereas under acidic conditions or upon addition of trifluorethanol it adopts alpha-helical structures.","type":"Abstract"},{"text":"The one- and two-dimensional NMR spectra (Figs. 5 and6) show a further phenomenon; in both pure aqueous as well as 50% TFE solutions the protein has some regions that show particularly broad lines, whereas at least several parts of the molecule appear to be relatively flexible resulting in sharper lines.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-15T08:45:43.813Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":96,"reference_id":"10903315","reference_source":"pmid","reference_html":"Functional and structural characterization of synthetic HIV-1 Vpr that transduces cells, localizes to the nucleus, and induces G2 cell cycle arrest. <i> Henklein P, Bruns K, Sherman MP, Tessmer U, Licha K, Kopp J, de Noronha CM, Greene WC, Wray V, Schubert U. </i> J Biol Chem, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03543r002","statement":[{"text":"Vpr is unstructured at neutral pH, whereas under acidic conditions or upon addition of trifluorethanol it adopts alpha-helical structures.","type":"Abstract"},{"text":"The peptide is completely unstructured at neutral pH, whereas lowering the pH to a critical threshold of pH 5.0 or adding a membrane mimetic, such as TFE, stabilizes secondary structure that is mainly α-helical in character.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-15T08:45:42.089Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":96,"reference_id":"10903315","reference_source":"pmid","reference_html":"Functional and structural characterization of synthetic HIV-1 Vpr that transduces cells, localizes to the nucleus, and induces G2 cell cycle arrest. <i> Henklein P, Bruns K, Sherman MP, Tessmer U, Licha K, Kopp J, de Noronha CM, Greene WC, Wray V, Schubert U. </i> J Biol Chem, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"GO:0044071","term_name":"symbiont-mediated perturbation of host cell cycle progression","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0005580","ec_ontology":"ECO","ec_name":"flow cytometry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03543r003","statement":[{"text":"sVpr Is Transduced Efficiently and Induces G2Cell Cycle Arrest","type":"Results"},{"text":"HeLa cells were incubated with sVpr labeled with a Cy3-like fluorophor that allows effective sorting of the transduced cells. WhensVpr-Cy3 was added at concentrations of 2, 5, and 10 μg ml−1, flow cytometric studies revealed dose-dependent uptake of sVpr-Cy3 from the medium (71, 92, and 97% of the cells, respectively) (Fig.9 A). When cells were incubated with sVpr-Cy3 at 2 μg ml−1 and sorted based on fluorescence, 30% of the positive cells were arrested in the G2/M phase of the cell cycle. In contrast, only 13% of cells of the non-transduced cell population were present in G2/M (Fig. 9 B). These data strongly suggest that sVpr is biologically active and is able to induce G2 cell cycle arrest in susceptible cells.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-15T08:53:42.710Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any viral process that modulates the rate or extent of progression through the cell cycle.\" [GOC:dph, UniProtKB-KW:KW-1121, VZ:1636]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":96,"reference_id":"10903315","reference_source":"pmid","reference_html":"Functional and structural characterization of synthetic HIV-1 Vpr that transduces cells, localizes to the nucleus, and induces G2 cell cycle arrest. <i> Henklein P, Bruns K, Sherman MP, Tessmer U, Licha K, Kopp J, de Noronha CM, Greene WC, Wray V, Schubert U. </i> J Biol Chem, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"GO:0075732","term_name":"viral penetration into host nucleus","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0007042","ec_ontology":"ECO","ec_name":"epifluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03543r004","statement":[{"text":"These studies revealed that sVpr-488 effectively entered cells following its addition in the extracellular medium (in a process termed as protein transduction) and further accumulated in the nucleus of these transduced cells (Fig.7).","type":"Results"},{"text":"Confocal microscopy revealed that in HeLa cells the transduced peptide sVpr-488 appears to be occasionally concentrated in cytosolic spots, whereas the majority of the peptide was clearly localized in the nucleus (Fig. 7,C and D). These data, together with our preliminary observation that sVpr activates HIV-1 replication and is specifically incorporated into budding HIV-1 virions (data not shown), provide evidence that sVpr possesses biological activities similar to those of viral Vpr.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-15T08:53:39.166Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The crossing by the virus of the host nuclear membrane, either as naked viral genome or for small viruses as an intact capsid.\" [PMID:22929056, VZ:989]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":96,"reference_id":"7815499","reference_source":"pmid","reference_html":"Extracellular Vpr protein increases cellular permissiveness to human immunodeficiency virus replication and reactivates virus from latency. <i> Levy DN, Refaeli Y, Weiner DB. </i> J Virol, 1995","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"GO:0019046","term_name":"release from viral latency","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0005581","ec_ontology":"ECO","ec_name":"enzyme-linked immunoabsorbent assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03543r005","statement":[{"text":"Extracellular Vpr protein increases cellular permissiveness to human immunodeficiency virus replication and reactivates virus from latency","type":"Title"},{"text":"In addition, extracellular Vpr reactivated HIV-1 expression in five latently infected cell lines of T-cell, B-cell, and promonocytic origin which normally express very low levels of HIV RNA and protein, indicating an activation of translational or pretranslational events in the virus life cycle.","type":"Abstract"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-15T08:53:24.200Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The process by which a virus begins to replicate following a latency replication decision (switch).\" [GOC:dos, GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":96,"reference_id":"7815499","reference_source":"pmid","reference_html":"Extracellular Vpr protein increases cellular permissiveness to human immunodeficiency virus replication and reactivates virus from latency. <i> Levy DN, Refaeli Y, Weiner DB. </i> J Virol, 1995","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"GO:0019079","term_name":"viral genome replication","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0005581","ec_ontology":"ECO","ec_name":"enzyme-linked immunoabsorbent assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03543r006","statement":[{"text":"Extracellular Vpr protein increases cellular permissiveness to human immunodeficiency virus replication and reactivates virus from latency","type":"Title"},{"text":"Extracellular Vpr also induced efficient HIV-1 replication in newly infected resting peripheral blood mononuclear cells.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-15T08:53:15.398Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process involved directly in viral genome replication, including viral nucleotide metabolism.\" [ISBN:0781702534]","disprot_namespace":"Disorder function","term_is_binding":false}],"regions_counter":12,"released":"2021_12","sequence":"MEQAPEDQGPQREPYNEWTLELLEELKSEAVRHFPRIWLHNLGRHIYETYGDTWAGVEAIIRILQQLPFIHFRIGCRHSRIGVTRQRRARNGASRS","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_P12520","uniref90":"UniRef90_Q72500","uniref100":"UniRef100_Q72500","genes":[{"name":{"value":"vpr","evidences":[{"code":"ECO:0000256","source":{"name":"HAMAP-Rule","id":"MF_04080","url":"https://hamap.expasy.org/unirule/MF_04080"}},{"code":"ECO:0000256","source":{"name":"RuleBase","id":"RU364021","url":"https://www.uniprot.org/unirule/RU364021"}},{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAB60574.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAB60574.1"}}]}}],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":96,"type":"D"}],"Structural state":[{"start":1,"end":96,"type":"D"}],"Biological process":[{"start":1,"end":96,"type":"F"}]}},{"disprot_id":"DP03544","acc":"P08669","creator":"fquaglia","date":"2021-11-11T16:24:08.178Z","features":{"pfam":[{"id":"PF00798","name":"Arenavirus glycoprotein","start":1,"end":484}],"gene3D":[]},"length":491,"name":"Pre-glycoprotein polyprotein GP complex","ncbi_taxon_id":11622,"organism":"Lassa virus (strain Mouse/Sierra Leone/Josiah/1976)","regions":[{"start":1,"end":58,"reference_id":"28572385","reference_source":"pmid","reference_html":"Structural basis for antibody-mediated neutralization of Lassa virus. <i> Hastie KM, Zandonatti MA, Kleinfelter LM, Heinrich ML, Rowland MM, Chandran K, Branco LM, Robinson JE, Garry RF, Saphire EO. </i> Science, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"5VK2"}],"region_id":"DP03544r001","statement":[{"text":"The final model contains residues 59-416 of GP  monomer A, with disordered regions from 171-179, 209-210, 256-259 and 329-330; residues 59- 418 of GP monomer B, with disordered regions from 170-179, 209-210, and 256-259; residues  59-418 of GP monomer C, with disordered regions from 170-179, 209-210, and 256-259 and  329-330 and Fab 37.7H residues 2-225 of the heavy chain (chains D, F and H), with a disordered  region from 159-165 and residues 3-213 of the light chain (chains E, G and L).","type":"Supplementary material"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-01T12:21:23.665Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MGQIVTFFQEVPHVIEEVMNIVLIALSVLAVLKGLYNFATCGLVGLVTFLLLCGRSCTTSLYKGVYELQTLELNMETLNMTMPLSCTKNNSHHYIMVGNETGLELTLTNTSIINHKFCNLSDAHKKNLYDHALMSIISTFHLSIPNFNQYEAMSCDFNGGKISVQYNLSHSYAGDAANHCGTVANGVLQTFMRMAWGGSYIALDSGRGNWDCIMTSYQYLIIQNTTWEDHCQFSRPSPIGYLGLLSQRTRDIYISRRLLGTFTWTLSDSEGKDTPGGYCLTRWMLIEAELKCFGNTAVAKCNEKHDEEFCDMLRLFDFNKQAIQRLKAEAQMSIQLINKAVNALINDQLIMKNHLRDIMGIPYCNYSKYWYLNHTTTGRTSLPKCWLVSNGSYLNETHFSDDIEQQADNMITEMLQKEYMERQGKTPLGLVDLFVFSTSFYLISIFLHLVKIPTHRHIVGKSCPKPHRLNHMGICSCGLYKQPGVPVKWKR","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Polyploviricotina","Ellioviricetes","Bunyavirales","Arenaviridae","Mammarenavirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_P09991","uniref90":"UniRef90_P08669","uniref100":"UniRef100_P08669","genes":[{"name":{"value":"GPC","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04084","url":"https://hamap.expasy.org/unirule/MF_04084"}}]},"synonyms":[{"value":"GP-C"}]}],"disorder_content":0.11812627291242363,"disprot_consensus":{"full":[{"start":1,"end":58,"type":"D"}],"Structural state":[{"start":1,"end":58,"type":"D"}]}},{"disprot_id":"DP03545","acc":"P35256","creator":"fquaglia","date":"2021-11-11T16:43:01.406Z","features":{"pfam":[{"id":"PF06389","name":"Filovirus membrane-associated protein VP24","start":1,"end":253}],"gene3D":[]},"length":253,"name":"Membrane-associated protein VP24","ncbi_taxon_id":33727,"organism":"Lake Victoria marburgvirus (strain Musoke-80)","regions":[{"start":242,"end":253,"reference_id":"24574400","reference_source":"pmid","reference_html":"Crystal structure of Marburg virus VP24. <i> Zhang AP, Bornholdt ZA, Abelson DM, Saphire EO. </i> J Virol, 2014","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03545r001","statement":[{"text":"Missing electron density region in the C-terminus of Marburgvirus VP24.","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"4OR8"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-01T12:24:50.422Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MAELSTRYNLPANVTENSINLDLNSTARWIKEPSVGGWTVKWGNFVFHIPNTGMTLLHHLKSNFVVPEWQQTRNLFSHLFKNPKSTIIEPFLALRILLGVALKDQELQQSLIPGFRSIVHMLSEWLLLEVTSAIHISPNLLGIYLTSDMFKILMAGVKNFFNKMFTLHVVNDHGKPSSIEIKLTGQQIIITRVNMGFLVEVRRIDIEPCCGETVLSESVVFGLVAEAVLREHSQMEKGQPLNLTQYMNSKIAI","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Filoviridae","Marburgvirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_P35256","uniref90":"UniRef90_P35256","uniref100":"UniRef100_P35256","genes":[{"name":{"value":"VP24"}}],"disorder_content":0.04743083003952569,"disprot_consensus":{"full":[{"start":242,"end":253,"type":"D"}],"Structural state":[{"start":242,"end":253,"type":"D"}]}},{"disprot_id":"DP03546","acc":"P35260","creator":"fquaglia","date":"2021-11-11T16:58:20.702Z","features":{"pfam":[{"id":"PF07447","name":"Matrix protein VP40","start":2,"end":283}],"gene3D":[]},"length":303,"name":"Matrix protein VP40","ncbi_taxon_id":33727,"organism":"Lake Victoria marburgvirus (strain Musoke-80)","regions":[{"start":1,"end":35,"reference_id":"26656687","reference_source":"pmid","reference_html":"Crystal Structure of Marburg Virus VP40 Reveals a Broad, Basic Patch for Matrix Assembly and a Requirement of the N-Terminal Domain for Immunosuppression. <i> Oda S, Noda T, Wijesinghe KJ, Halfmann P, Bornholdt ZA, Abelson DM, Armbrust T, Stahelin RV, Kawaoka Y, Saphire EO. </i> J Virol, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"5B0V"}],"region_id":"DP03546r001","statement":[{"text":"The construct crystallized was the complete mVP40, containing residues 1 to 303 (Fig. 1 and ​and2).2). Of these, the N terminus (residues 1 to 37 in molecule 1 and 1 to 35 in molecule 2) and a few short loops (residues 71 to 72, 156 to 157, and 264 to 267 in molecule 1 and residues 216 to 218, 259 to 260, 264 to 269, and 302 to 303 in molecule 2) were disordered.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-01T13:15:19.618Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MASSSNYNTYMQYLNPPPYADHGANQLIPADQLSNQQGITPNYVGDLNLDDQFKGNVCHAFTLEAIIDISAYNERTVKGVPAWLPLGIMSNFEYPLAHTVAALLTGSYTITQFTHNGQKFVRVNRLGTGIPAHPLRMLREGNQAFIQNMVIPRNFSTNQFTYNLTNLVLSVQKLPDDAWRPSKDKLIGNTMHPAVSIHPNLPPIVLPTVKKQAYRQHKNPNNGPLLAISGILHQLRVEKVPEKTSLFRISLPADMFSVKEGMMKKRGENSPVVYFQAPENFPLNGFNNRQVVLAYANPTLSAV","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Filoviridae","Marburgvirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_P35260","uniref90":"UniRef90_P35260","uniref100":"UniRef100_P35260","genes":[{"name":{"value":"VP40"}}],"disorder_content":0.11551155115511551,"disprot_consensus":{"full":[{"start":1,"end":35,"type":"D"}],"Structural state":[{"start":1,"end":35,"type":"D"}]}},{"disprot_id":"DP03547","acc":"P89522","creator":"fquaglia","date":"2021-11-11T17:04:07.296Z","features":{"pfam":[{"id":"PF02477","name":"Nucleocapsid N protein","start":1,"end":441}],"gene3D":[]},"length":482,"name":"Nucleoprotein","ncbi_taxon_id":652961,"organism":"Crimean-Congo hemorrhagic fever virus (strain Nigeria/IbAr10200/1970)","regions":[{"start":183,"end":193,"reference_id":"22951837","reference_source":"pmid","reference_html":"Structure of Crimean-Congo hemorrhagic fever virus nucleoprotein: superhelical homo-oligomers and the role of caspase-3 cleavage. <i> Wang Y, Dutta S, Karlberg H, Devignot S, Weber F, Hao Q, Tan YJ, Mirazimi A, Kotaka M. </i> J Virol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"4AQG"}],"region_id":"DP03547r001","statement":[{"text":"Of the three molecules of CCHFV N in the asymmetric unit, we were able to observe clear electron density only of the flexible linker residues 181 to 195 connecting the stalk domain and the globular body domain in molecule B (see Fig. S2 in the supplemental material). The linker is not visible in molecules B and C, and unobserved disordered residues include 181 to 194 in molecule A and 181 to 195 in molecule C.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T11:54:05.114Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":183,"end":193,"reference_id":"22951837","reference_source":"pmid","reference_html":"Structure of Crimean-Congo hemorrhagic fever virus nucleoprotein: superhelical homo-oligomers and the role of caspase-3 cleavage. <i> Wang Y, Dutta S, Karlberg H, Devignot S, Weber F, Hao Q, Tan YJ, Mirazimi A, Kotaka M. </i> J Virol, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"4AQG"}],"region_id":"DP03547r002","statement":[{"text":"Of the three molecules of CCHFV N in the asymmetric unit, we were able to observe clear electron density only of the flexible linker residues 181 to 195 connecting the stalk domain and the globular body domain in molecule B (see Fig. S2 in the supplemental material). The linker is not visible in molecules B and C, and unobserved disordered residues include 181 to 194 in molecule A and 181 to 195 in molecule C.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T11:54:06.344Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":2,"released":"2021_12","sequence":"MENKIEVNNKDEMNRWFEEFKKGNGLVDTFTNSYSFCESVPNLDRFVFQMASATDDAQKDSIYASALVEATKFCAPIYECAWVSSTGIVKKGLEWFEKNAGTIKSWDESYTELKVDVPKIEQLTGYQQAALKWRKDIGFRVNANTAALSNKVLAEYKVPGEIVMSVKEMLSDMIRRRNLILNRGGDENPRGPVSHEHVDWCREFVKGKYIMAFNPPWGDINKSGRSGIALVATGLAKLAETEGKGIFDEAKKTVEALNGYLDKHKDEVDRASADSMITNLLKHIAKAQELYKNSSALRAQSAQIDTAFSSYYWLYKAGVTPETFPTVSQFLFELGKQPRGTKKMKKALLSTPMKWGKKLYELFADDSFQQNRIYMHPAVLTAGRISEMGVCFGTIPVANPDDAAQGSGHTKSILNLRTNTETNNPCAKTIVKLFEVQKTGFNIQDMDIVASEHLLHQSLVGKQSPFQNAYNVKGNATSANII","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Polyploviricotina","Ellioviricetes","Bunyavirales","Nairoviridae","Orthonairovirus"],"dataset":["Viral proteins","RNA-binding proteins"],"uniref50":"UniRef50_P27318","uniref90":"UniRef90_P27317","uniref100":"UniRef100_P89522","genes":[{"name":{"value":"N"}}],"disorder_content":0.022821576763485476,"disprot_consensus":{"full":[{"start":183,"end":193,"type":"D"}],"Structural state":[{"start":183,"end":193,"type":"D"}],"Disorder function":[{"start":183,"end":193,"type":"F"}]}},{"disprot_id":"DP03548","acc":"P05453","creator":"fquaglia","date":"2021-11-15T08:47:21.793Z","features":{"pfam":[{"id":"PF00009","name":"Elongation factor Tu GTP binding domain","start":258,"end":478},{"id":"PF03144","name":"Elongation factor Tu domain 2","start":502,"end":570},{"id":"PF22594","name":"GTP-eEF1A C-terminal domain-like","start":581,"end":680}],"gene3D":[]},"length":685,"name":"Eukaryotic peptide chain release factor GTP-binding subunit","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":250,"reference_id":"17299036","reference_source":"pmid","reference_html":"A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures. <i> Mukhopadhyay S, Krishnan R, Lemke EA, Lindquist S, Deniz AA. </i> Proc Natl Acad Sci U S A, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03548r001","statement":[{"text":"A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures","type":"Title"},{"text":"These results establish that the monomeric form of NM adopts an ensemble of relatively unordered states with rapid conformational fluctuations.","type":"Results"},{"text":"We have used single-molecule and small-ensemble techniques to directly study the conformational properties of NM in physiological buffers in the non-prion monomeric state. Our results demonstrate that natively unfolded NM is not a completely denatured random coil under these conditions. Instead, it occupies an ensemble of rapidly interconverting compact conformations.","type":"Discussion"},{"text":"Our finding that the N region of native NM is significantly more compact than a corresponding denatured protein (40) then identifies it with the premolten globule class of natively unfolded proteins. It has been noted that a combination of low mean hydrophobicity and high charge is a prerequisite for maintaining a flexible, unstructured state under physiological conditions (49). The amyloid core of Sup35 (N region) contains only 8% hydrophobic and 4% charged amino acids. Our results indicate that the core N region remains compact and flexible despite lacking both hydrophobic and charged residues.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-15T09:42:37.008Z"},"ec_go":"IPI","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVNDMFGGKDHVSLIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREAKDAGRQGWYLSWVMDTNKEERNDGKTIEVGKAYFETEKRRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYETGFERGGQTREHALLAKTQGVNKMVVVVNKMDDPTVNWSKERYDQCVSNVSNFLRAIGYNIKTDVVFMPVSGYSGANLKDHVDPKECPWYTGPTLLEYLDTMNHVDRHINAPFMLPIAAKMKDLGTIVEGKIESGHIKKGQSTLLMPNKTAVEIQNIYNETENEVDMAMCGEQVKLRIKGVEEEDISPGFVLTSPKNPIKSVTKFVAQIAIVELKSIIAAGFSCVMHVHTAIEEVHIVKLLHKLEKGTNRKSKKPPAFAKKGMKVIAVLETEAPVCVETYQDYPQLGRFTLRDQGTTIAIGKIVKIAE","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"uniref50":"UniRef50_P05453","uniref90":"UniRef90_P05453","uniref100":"UniRef100_P05453","genes":[{"name":{"value":"SUP35"},"synonyms":[{"value":"GST1"},{"value":"PNM2"},{"value":"SAL3"},{"value":"SUF12"},{"value":"SUP2"}],"orfNames":[{"value":"YD9395.05"}],"olnNames":[{"value":"YDR172W"}]}],"alphafold_very_low_content":0.32262773722627736,"dataset":["Condensates-related proteins"],"disorder_content":0.36496350364963503,"disprot_consensus":{"full":[{"start":1,"end":250,"type":"D"}],"Structural state":[{"start":1,"end":250,"type":"D"}]}},{"disprot_id":"DP03549","acc":"Q91H74","creator":"vnugnes","date":"2021-11-16T09:20:35.026Z","features":{"pfam":[{"id":"PF00869","name":"Flavivirus glycoprotein, central and dimerisation domains","start":282,"end":576},{"id":"PF00948","name":"Flavivirus non-structural Protein NS1","start":777,"end":1129},{"id":"PF00949","name":"Peptidase S7, Flavivirus NS3 serine protease","start":1492,"end":1643},{"id":"PF00972","name":"Flavivirus RNA-directed RNA polymerase, fingers and palm domains","start":2742,"end":3191},{"id":"PF01002","name":"Flavivirus non-structural protein NS2B","start":1349,"end":1475},{"id":"PF01003","name":"Flavivirus capsid protein C","start":5,"end":113},{"id":"PF01004","name":"Flavivirus envelope glycoprotein M","start":207,"end":279},{"id":"PF01005","name":"Flavivirus non-structural protein NS2A","start":1138,"end":1328},{"id":"PF01349","name":"Flavivirus non-structural protein NS4B","start":2244,"end":2484},{"id":"PF01350","name":"Flavivirus non-structural protein NS4A","start":2099,"end":2240},{"id":"PF01570","name":"Flavivirus polyprotein propeptide","start":120,"end":204},{"id":"PF01728","name":"FtsJ-like methyltransferase","start":2546,"end":2713},{"id":"PF02832","name":"Flavivirus glycoprotein, immunoglobulin-like domain","start":578,"end":673},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1658,"end":1805},{"id":"PF20483","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","start":3196,"end":3358},{"id":"PF20907","name":"Flavivirus NS3 helicase, C-terminal helical domain","start":1949,"end":2091},{"id":"PF21659","name":"Flavivirus envelope glycoprotein E, stem/anchor domain","start":676,"end":770}],"gene3D":[]},"length":3391,"name":"Core protein","ncbi_taxon_id":11060,"organism":"Dengue virus 2","regions":[{"start":2898,"end":2909,"reference_id":"32357182","reference_source":"pmid","reference_html":"A conformation-based intra-molecular initiation factor identified in the flavivirus RNA-dependent RNA polymerase. <i> Wu J, Ye HQ, Zhang QY, Lu G, Zhang B, Gong P. </i> PLoS Pathog, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":1,"cross_refs":[{"db":"PDB","id":"6KR3"},{"db":"PDB","id":"6KR2"}],"region_id":"DP03549r001","statement":[{"text":"This region lacks electron density in both form 1 and 2 of the crystals, indicating this residues are unstructured.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-17T08:38:51.811Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":3377,"end":3391,"reference_id":"32357182","reference_source":"pmid","reference_html":"A conformation-based intra-molecular initiation factor identified in the flavivirus RNA-dependent RNA polymerase. <i> Wu J, Ye HQ, Zhang QY, Lu G, Zhang B, Gong P. </i> PLoS Pathog, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":1,"cross_refs":[{"db":"PDB","id":"6KR3"},{"db":"PDB","id":"6KR2"}],"region_id":"DP03549r002","statement":[{"text":"This region lacks electron density in both form 1 and 2 of the crystals, indicating this residues are unstructured.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-17T08:38:52.912Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":2946,"end":2961,"reference_id":"32357182","reference_source":"pmid","reference_html":"A conformation-based intra-molecular initiation factor identified in the flavivirus RNA-dependent RNA polymerase. <i> Wu J, Ye HQ, Zhang QY, Lu G, Zhang B, Gong P. </i> PLoS Pathog, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":1,"cross_refs":[{"db":"PDB","id":"6KR3"}],"region_id":"DP03549r003","statement":[{"text":"This region lacks electron density in form 2 of the crystals obtained, indicating this residues were unstructured.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-17T09:46:20.289Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2023_06","sequence":"MNNQRKKARNTPFNMLKRERNRVSTVQQLTKRFSLGMLQGRGPLKLFMALVAFLRFLTIPPTAGILKRWGTIKKSKAINVLRGFRKEIGRMLNILNRRRRTAGIIIMMIPTVMAFHLTTRNGEPHMIVSRQEKGKSLLFKTENGVNMCTLMAMDLGELCEDTITYNCPLLRQNEPEDIDCGCHSTSTWVTYGTCTATGEHRREKRSVALVPHVGMGLETRTETWMSSEGAWKHAQRIETWVLRHPGFTIMAAILAYTIGTTYFQRVLIFILLTAVTPSMTMRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPTLDFELVKTEAKHPATLRKYCIEAKLTNTTTASRCPTQGEPSLNEEQDKRFVCKHSMVDRGWGNGCGLFGKGGIVTCAMFTCKKNMEGKVVQPENLEYTIVITPHSGEENAVGNDTGKHGKEIKVTPQSSITEAELTGYGTVTMECSPRTGLDFNEMVLLQMENKAWLVHRQWFLDLPLPWLPGADTQGSNWIQKETLVTFKNPHAKKQDVVVLGSQEGAMHTALTGATEIQMSSGNLLFTGHLKCRLRMDKLQLKGMSYSMCTGKFKVVKEIAETQHGTIVIRVQYEGDGSPCKIPFEIMDLEKRHVLGRLITVNPIVTEKDSPVNIEAEPPFGDSYIIIGVEPGQLKLSWFKKGSSIGQMFETTMRGAKRMAILGDTAWDFGSLGGVFTSIGKALHQVFGAIYGAAFSGVSWTMKILIGVVITWIGMNSRSTSLSVSLVLVGVVTLYLGVMVQADSGCVVSWKNKELKCGSGIFITDNVHTWTEQYKFQPESPSKLASAIQKAHEEGICGIRSVTRLENLMWKQITPELNHILSENEVKLTIMTGDIKGIMQAGKRSLRPQPTELKYSWKAWGKAKMLSTELHNHTFLIDGPETAECPNTNRAWNSLEVEDYGFGVFTTNIWLKLKERQDVFCDSKLMSAAIKDNRAVHADMGYWIESALNDTWKIEKASFIEVKSCHWPKSHTLWSNGVLESEMIIPKNFAGPVSQHNYRPGYHTQTAGPWHLGRLEMDFDFCEGTTVVVTEDCGNRGPSLRTTTASGKLITEWCCRSCTLPPLRYRGEDGCWYGMEIRPLKEKEENLVNSLVTAGHGQIDNFSLGVLGMALFLEEMLRTRVGTKHAILLVAVSFVTLITGNMSFRDLGRVMVMVGATMTDDIGMGVTYLALLAAFKVRPTFAAGLLLRKLTSKELMMTTIGIVLLSQSTIPETILELTDAWALGMMVLKIVRNMEKYQLAVTIMAILCVPNAVILQNAWKVSCTTLAVVSVSPLLLTSSQQKADWIPLALTIKGLNPTAIFLTTLSRTSKKRSWPLNEAIMAVGMVSILASSLLKNDIPMTGPLVAGGLLTVCYVLTGRSADLELERAADVRWEEQAEISGSSPILSITISEDGSMSIKNEEEEQTLTILIRTGLLVISGLFPASIPITAAAWYLWEVKKQRAGVLWDVPSPPPVGKAELEDGAYRIKQKGILGYSQIGAGVYKEGTFHTMWHVTRGAVLMHKGKRIEPSWADVKKDLISYGGGWKLEGEWKEGEEVQVLALEPGKNPRAVQTKPGLFKTNTGTIGAVSLDFSPGTSGSPIVDKKGKVVGLYGNGVVTRSGAYVSAIAQTEKSIEDNPEIEDDIFRKKRLTIMDLHPGAGKTKRYLPAIVREAIKRGLRTLILAPTRVVAAEMEEALRGLPIRYQTPAIRAEHTGREIVDLMCHATFTMRLLSPIRVPNYNLIIMDEAHFTDPASIAARGYISTRVEMGEAAGIFMTATPPGSRDPFPQSNAPIMDEEREIPERSWNSGHEWVTDFKGKTVWFVPSIKAGNDIAACLRKNGKKVIQLSRKTFDSEYIKTRTNDWDFVVTTDISEMGANFKAERVIDPRRCMKPVILTDGEERVILAGPMPVTHSSAAQRRGRVGRNPKNENDQYIYMGEPLENDEDCAHWKEAKMLLDNINTPEGIIPSMFEPEREKVDAIDGEYRLRGEARKTFVDLMRRGDLPVWLAYRVAAEGINYADRRWCFDGVKNNQILEENVEVEIWTKEGERKKLKPRWLDARIYSDPLALKEFKEFAAGRKSLTLNLITEMGRLPTFMTQKARNALDNLAVLHTAEAGGRAYNHALSELPETLETLLLLTLLATVTGGIFLFLMSGKGIGKMTLGMCCIITASILLWYAQIQPHWIAASIILEFFLIVLLIPEPEKQRTPQDNQLTYVVIAILTVVAATMANEMGFLEKTKKDFGLGSIATQQPESNILDIDLRPASAWTLYAVATTFITPMLRHSIENSSVNVSLTAIANQATVLMGLGKGWPLSKMDIGVPLLAIGCYSQVNPITLTAALLLLVAHYAIIGPGLQAKATREAQKRAAAGIMKNPTVDGITVIDLDPIPYDPKFEKQLGQVMLLVLCVTQVLMMRTTWALCEALTLATGPISTLWEGNPGRFWNTTIAVSMANIFRGSYLAGAGLLFSIMKNTANTRRGTGNTGETLGEKWKNRLNALGKSEFQIYKKSGIQEVDRTLAKEGIKRGETDHHAVSRGSAKLRWFVERNLVTPEGKVVDLGCGRGGWSYYCGGLKNVKEVKGLTKGGPGHEEPIPMSTYGWNLVRLQSGVDVFFTPPEKCDTLLCDIGESSPNPTVEAGRTLRVLNLVENWLNNNTQFCIKVLNPYMPSVIEKMEALQRKYGGALVRNPLSRNSTHEMYWVSNASGNIVSSVNMISRMLINRFTMRHKKATYEPDVDLGSGTRNIGIESETPNLDIIGKRIEKIKQEHETSWHYDQDHPYKTWAYHGSYETKQTGSASSMVNGVVRLLTKPWDIIPMVTQMAMTDTTPFGQQRVFKEKVDTRTQEPKEGTKKLMKITAEWLWKELGKKKTPRMCTREEFTRKVRSNAALGAIFTDENKWKSAREAVEDSGFWELVDKERNLHLEGKCETCVYNMMGKREKKLGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWFSRENSLSGVEGEGLHKLGYILRDVSKKEGGAMYADDTAGWDTRITLEDLKNEEMVTNHMEGEHKKLAEAIFKLTYQNKVVRVQRPTPRGTVMDIISRRDQRGSGQVVTYGLNTFTNMEAQLIRQMEGEGVFKSIQHLTVTEEIAVKNWLVRVGRERLSRMAISGDDCVVKPLDDRFASALTALNDMGKVRKDIQQWEPSRGWNDWTQVPFCSHHFHELIMKDGRVLVVPCRNQDELIGRARISQGAGWSLRETACLGKSYAQMWSLMYFHRRDLRLAANAICSAVPSHWVPTSRTTWSIHATHEWMTTEDMLTVWNRVWIQENPWMEDKTPVESWEEIPYLGKREDQWCGSLIGLTSRATWAKNIQTAINQVRSLIGNEEYTDYMPSMKRFRREEEEAGVLW","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Flavivirus"],"dataset":["Viral proteins","Neglected tropical diseases proteins"],"uniref50":"UniRef50_P17763","uniref90":"UniRef90_P29990","uniref100":"UniRef100_Q91H74","genes":[],"disorder_content":0.012680625184311413,"disprot_consensus":{"full":[{"start":2898,"end":2909,"type":"D"},{"start":2946,"end":2961,"type":"D"},{"start":3377,"end":3391,"type":"D"}],"Structural state":[{"start":2898,"end":2909,"type":"D"},{"start":2946,"end":2961,"type":"D"},{"start":3377,"end":3391,"type":"D"}]}},{"disprot_id":"DP03550","acc":"Q703G9","creator":"vnugnes","date":"2021-11-17T16:20:51.837Z","features":{"pfam":[{"id":"PF01766","name":"Birnavirus VP2 protein","start":5,"end":453},{"id":"PF01767","name":"Birnavirus VP3 protein","start":756,"end":937},{"id":"PF01768","name":"Birnavirus VP4 protein","start":455,"end":706}],"gene3D":[]},"length":972,"name":"Structural polyprotein","ncbi_taxon_id":11005,"organism":"Infectious pancreatic necrosis virus (strain Sp)","regions":[{"start":429,"end":442,"reference_id":"20007275","reference_source":"pmid","reference_html":"Crystal structure of an Aquabirnavirus particle: insights into antigenic diversity and virulence determinism. <i> Coulibaly F, Chevalier C, Delmas B, Rey FA. </i> J Virol, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03550r001","statement":[{"text":"The electron density map of the IPNV SVP displays unambiguous density for most of the polypeptide chain, allowing the visualization of residues 6 to 428 of VP2, with a break in density between amino acids 110 to 117 at the distal tip of domain S, which appears disordered (Fig.11 and ​and2C).","type":"Results"}],"cross_refs":[{"db":"PDB","id":"3IDE"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-23T10:02:01.665Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MNTNKATATYLKSIMLPETGPASIPDDITERHILKQETSSYNLEVSESGSGVLVCFPGAPGSRIGAHYRWNANQTGLEFDQWLETSQDLKKAFNYGRLISRKYDIQSSTLPAGLYALNGTLNAATFEGSLSEVESLTYNSLMSLTTNPQDKVNNQLVTKGVTVLNLPTGFDKPYVRLEDETPQGLQSMNGAKMRCTAAIAPRRYEIDLPSQRLPPVPATGTLTTLYEGNADIVNSTTVTGDINFSLAEQPADETKFDFQLDFMGLDNDVPVVTVVSSVLATNDNYRGVSAKMTQSIPTENITKPITRVKLSYKINQQTAIGNVATLGTMGPASVSFSSGNGNVPGVLRPITLVAYEKMTPLSILTVAGVSNYELIPNPELLKNMVTRYGKYDPEGLNYAKMILSHREELDIRTVWRTEEYKERTRVFNEITDFSSDLPTSKAWGWRDIVRGIRKVAAPVLSTLFPMAAPLIGMADQFIGDLTKTNAAGGRYHSMAAGGRYKDVLESWASGGPDGKFSRALKNRLESANYEEVELPPPSKGVIVPVVHTVKSAPGEAFGSLAIIIPGEYPELLDANQQVLSHFANDTGSVWGIGEDIPFEGDNMCYTALPLKEIKRNGNIVVEKIFAGPIMGPSAQLGLSLLVNDIEDGVPRMVFTGEIADDEETIIPICGVDIKAIAAHEQGLPLIGNQPGVDEEVRNTSLAAHLIQTGTLPVQRAKGSNKRIKYLGELMASNASGMDEELQRLLNATMARAKEVQDAEIYKLLKLMAWTRKNDLTDHMYEWSKEDPDALKFGKLISTPPKHPEKPKGPDQHHAQEARATRISLDAVRAGADFATPEWVALNNYRGPSPGQFKYYLITGREPEPGDEYEDYIKQPIVKPTDMNKIRRLANSVYGLPHQEPAPEEFYDAVAAVFAQNGGRGPDQDQMQDLRELARQMKRRPRNADAPRRTRAPAEPAPPGRSRFTPSGDNAEV","taxonomy":["Viruses","Riboviria","Orthornavirae","Birnaviridae","Aquabirnavirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_Q703G9","uniref90":"UniRef90_Q703G9","uniref100":"UniRef100_Q703G9","genes":[],"disorder_content":0.01440329218106996,"disprot_consensus":{"full":[{"start":429,"end":442,"type":"D"}],"Structural state":[{"start":429,"end":442,"type":"D"}]}},{"disprot_id":"DP03551","acc":"P22173","creator":"jbergier","date":"2021-11-18T10:48:46.307Z","features":{"pfam":[{"id":"PF04197","name":"Birnavirus RNA dependent RNA polymerase (VP1), palm domain","start":1,"end":522},{"id":"PF20488","name":"Birnavirus RNA dependent RNA polymerase (VP1), thumb domain","start":523,"end":686},{"id":"PF20489","name":"Birnavirus RNA dependent RNA polymerase (VP1), C-terminal","start":689,"end":793}],"gene3D":[]},"length":845,"name":"RNA-directed RNA polymerase","ncbi_taxon_id":11003,"organism":"Infectious pancreatic necrosis virus (strain Jasper)","regions":[{"start":1,"end":26,"reference_id":"23283942","reference_source":"pmid","reference_html":"Structure of a VP1-VP3 complex suggests how birnaviruses package the VP1 polymerase. <i> Bahar MW, Sarin LP, Graham SC, Pang J, Bamford DH, Stuart DI, Grimes JM. </i> J Virol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03551r001","statement":[{"text":"The crystal structure of the complex between full-length VP1 and VP3 was solved by molecular replacement using the structure of IPNV VP1 (9) as a search model and refined to a resolution of 2.2 Å with residual Rxpct = 0.179 and Rfree = 0.215 (Table 1). The final structure is of high stereochemical quality with 98% of the residues occupying the favored region of the Ramachandran plot. Three copies of VP1 are present in the asymmetric unit (AU) of the crystal, and electron density was observed from residues 27 to 792 for each chain of VP1 (no density was observed for residues 1 to 26 and 793 to 845).","type":"Results"}],"cross_refs":[{"db":"PDB","id":"3ZED"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P05844"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-22T13:07:06.451Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":793,"end":845,"reference_id":"23283942","reference_source":"pmid","reference_html":"Structure of a VP1-VP3 complex suggests how birnaviruses package the VP1 polymerase. <i> Bahar MW, Sarin LP, Graham SC, Pang J, Bamford DH, Stuart DI, Grimes JM. </i> J Virol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03551r002","statement":[{"text":"The crystal structure of the complex between full-length VP1 and VP3 was solved by molecular replacement using the structure of IPNV VP1 (9) as a search model and refined to a resolution of 2.2 Å with residual Rxpct = 0.179 and Rfree = 0.215 (Table 1). The final structure is of high stereochemical quality with 98% of the residues occupying the favored region of the Ramachandran plot. Three copies of VP1 are present in the asymmetric unit (AU) of the crystal, and electron density was observed from residues 27 to 792 for each chain of VP1 (no density was observed for residues 1 to 26 and 793 to 845).","type":"Results"}],"cross_refs":[{"db":"PDB","id":"3ZED"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P05844","statements":[{"type":"Results","text":"Complexes of either full-length VP1 and VP3 or ΔC55 VP1 and VP3 were prepared by mixing individually purified proteins and repurifying by Ni2+ affinity and size exclusion chromatography (Fig. 1B)."}]}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-22T13:07:03.590Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":799,"end":845,"reference_id":"21731487","reference_source":"pmid","reference_html":"The N-terminus of the RNA polymerase from infectious pancreatic necrosis virus is the determinant of genome attachment. <i> Graham SC, Sarin LP, Bahar MW, Myers RA, Stuart DI, Bamford DH, Grimes JM. </i> PLoS Pathog, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2YIB"}],"region_id":"DP03551r003","statement":[{"text":"Despite being crystallized in the presence of Mn2+ and ATP, no metal ions or nucleotides were observed at the active site. While additional electron density was seen connected to the C-terminus of the molecular replacement search model in three of the four copies of VP1 present in the asymmetric unit only eight additional residues (791–798) could be placed, suggesting that residues 799–845 are not ordered.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-22T13:03:17.215Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":793,"end":845,"reference_id":"21731487","reference_source":"pmid","reference_html":"The N-terminus of the RNA polymerase from infectious pancreatic necrosis virus is the determinant of genome attachment. <i> Graham SC, Sarin LP, Bahar MW, Myers RA, Stuart DI, Bamford DH, Grimes JM. </i> PLoS Pathog, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"GO:0019079","term_name":"viral genome replication","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0001254","ec_ontology":"ECO","ec_name":"radioisotope assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03551r004","statement":[{"text":"Both full-length and ΔC55 VP1 yield RNA/DNA hybrids of various heterologous ssRNA templates, ΔC55 being roughly 5-fold more active than the full-length enzyme, while ΔN27C55 VP1 reverse transcriptase activity is extremely low (Table 1, Figure 4).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-22T13:04:26.666Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process involved directly in viral genome replication, including viral nucleotide metabolism.\" [ISBN:0781702534]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":20,"end":30,"reference_id":"21731487","reference_source":"pmid","reference_html":"The N-terminus of the RNA polymerase from infectious pancreatic necrosis virus is the determinant of genome attachment. <i> Graham SC, Sarin LP, Bahar MW, Myers RA, Stuart DI, Bamford DH, Grimes JM. </i> PLoS Pathog, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2YI9"},{"db":"PDB","id":"2YI8"}],"region_id":"DP03551r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":50,"db":"ChEBI","id":"6636","statements":[{"type":"Results","text":"To characterize binding of catalytic metals at the active site of the enzyme, crystals of ΔC55 VP1 were soaked in reservoir solution supplemented with 50 mM MgCl2 and 10 µM GTP and lacking citrate (which chelated metals, frustrating soaking experiments)."}],"entry_name":"magnesium dichloride"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29103","entry_name":"potassium(1+)"}],"statement":[{"text":"The PDB shows disorder in this region when the protein is bound to the ions Mg+2, K+ and Cl- or only K+ and Cl-.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-22T13:03:18.383Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":10,"reference_id":"21731487","reference_source":"pmid","reference_html":"The N-terminus of the RNA polymerase from infectious pancreatic necrosis virus is the determinant of genome attachment. <i> Graham SC, Sarin LP, Bahar MW, Myers RA, Stuart DI, Bamford DH, Grimes JM. </i> PLoS Pathog, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2YI9"},{"db":"PDB","id":"2YI8"}],"region_id":"DP03551r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":50,"db":"ChEBI","id":"6636","statements":[{"type":"Results","text":"To characterize binding of catalytic metals at the active site of the enzyme, crystals of ΔC55 VP1 were soaked in reservoir solution supplemented with 50 mM MgCl2 and 10 µM GTP and lacking citrate (which chelated metals, frustrating soaking experiments)."}],"entry_name":"magnesium dichloride"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29103","entry_name":"potassium(1+)"}],"statement":[{"text":"The PDB shows disorder in this region when the protein is bound to the ions Mg+2, K+ and Cl- or only K+ and Cl-.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-22T13:03:19.460Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":7,"released":"2021_12","sequence":"MSDIFNSPQNKASILTALMKSTTGDVEDVLIPKRFRPAKDPLDSPQAAAQFLKDNKYRILRPRAIPTMVELETDAALPRLRQMVEDGKLKDTVSVPEGTTAFYPKYYPFHKPDHDEVGTFGAPDITLLKQLTFFLLENDFPTGPETLRQVREAIATLQYGSGSYSGQLNRLLAMKGVATGRNPNKTPKTVGYTNEQLAKLLEQTLPINTPKHEDPDLRWAPSWLINYTGDLSTDKSYLPHVTIKSSAGLPYIGKTKGDTTAEALVLADSFIRDLGRAATSADPEAGVKKTITDFWYLSCGLLFPKGERYTQVDWDKKTRNIWSAPYPTHLLLSMVSTPVMNESKLNITNTQTPSLYGFSPFHGGMDRIMTIIRDSLDNDEDLVMIYADNIYILQDNTWYSIDLEKGEANCTPQHMQAMMYYLLTRGWTNEDGSPRYNPTWATFAMNVAPSMVVDSSCLLMNLQLKTYGQGSGNAFTFLNNHLMSTIVVAEWVKAGKPNPMTKEFMDLEEKTGINFKIERELKNLRETIVEAVETAPQDGYLADGSDLPPIRPGKAVELDLLGWSAIYSRQMEMFVPVLENERLIASAAYPKGLENKALARKPGAEIAYQIVRYEAIRLVGGWNNPLLETAAKHMSLDKRKRLEVKGIDVTGFLDDWNNMSEFGGDLEGITLSEPLTNQTLVDINTPLDSFDPKARPQTPRSPKKTLDEVTTAITSGTYKDPKSAVWRLLDQRTKLRVSTLRDQALALKPASSSVDNWAEATEELAQQQQLLMKANNLLKSSLTETREALETIQSDKIIAGKSNPEKNPGTAANPVVGYGEFSEKIPLTPTQKKNAKRREKQRRNQ","taxonomy":["Viruses","Riboviria","Orthornavirae","Birnaviridae","Aquabirnavirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_P22173","uniref90":"UniRef90_P22173","uniref100":"UniRef100_P22173","genes":[{"name":{"value":"VP1"}}],"disorder_content":0.09822485207100591,"disprot_consensus":{"full":[{"start":1,"end":30,"type":"D"},{"start":793,"end":845,"type":"D"}],"Structural state":[{"start":1,"end":30,"type":"D"},{"start":793,"end":845,"type":"D"}],"Biological process":[{"start":793,"end":845,"type":"F"}]}},{"disprot_id":"DP03552","acc":"P10636-2","creator":"esalladini","date":"2021-11-22T08:59:23.636Z","features":{"pfam":[],"gene3D":[]},"length":352,"name":"Isoform Fetal-tau of Microtubule-associated protein tau","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":352,"reference_id":"18771286","reference_source":"pmid","reference_html":"Domain conformation of tau protein studied by solution small-angle X-ray scattering. <i> Mylonas E, Hascher A, Bernadó P, Blackledge M, Mandelkow E, Svergun DI. </i> Biochemistry, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03552r001","statement":[{"text":"All the profiles are featureless, and the Kratky plots [s2I(s) vs s] are without apparent peaks (Supporting Information Figure 3), which is typical for unfolded proteins.","type":"Results"},{"text":"Table 1 indicates that the larger constructs (ht23 and ht40) have Rg values close to or smaller than the predicted random coil values, which are shown by ref 29 to agree well with the experimental data from chemically unfolded proteins (note that as tau constructs are not denatured using chemicals the random coil estimations cannot be considered ideal predictions, but they do provide a useful guidance).","type":"Results"},{"text":"For full length constructs (ht40 and ht23), little difference from the pool distribution was observed (typical models of ht40 selected from the random pools are displayed in Figure 4 to demonstrate that the protein is indeed rather unstructured).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-11-22T14:38:33.671Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref50":"","uniref90":"","uniref100":"","genes":[{"name":{"value":"MAPT","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6893","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6893"}}]},"synonyms":[{"value":"MAPTL"},{"value":"MTBT1"},{"value":"TAU"}]}],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":352,"type":"D"}],"Structural state":[{"start":1,"end":352,"type":"D"}]}},{"disprot_id":"DP03553","acc":"O94829","creator":"vacs","date":"2021-11-22T09:33:28.490Z","features":{"pfam":[{"id":"PF03810","name":"Importin-beta N-terminal domain","start":45,"end":107},{"id":"PF08389","name":"Exportin 1-like protein","start":117,"end":262},{"id":"PF18773","name":"Importin 13 repeat","start":402,"end":441},{"id":"PF18786","name":"Importin 13 repeat","start":584,"end":627},{"id":"PF18786","name":"Importin 13 repeat","start":631,"end":672},{"id":"PF18806","name":"Importin 13 repeat","start":826,"end":899},{"id":"PF24138","name":"Transportin-3/Importin-13 second TPR domain","start":301,"end":398},{"id":"PF24139","name":"Transportin-3/Importin-13 fourth TPR domain","start":675,"end":762},{"id":"PF24140","name":"Transportin-3/Importin-13 third TPR domain","start":503,"end":562}],"gene3D":[]},"length":963,"name":"Importin-13","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":18,"reference_id":"21139563","reference_source":"pmid","reference_html":"Structure of Importin13-Ubc9 complex: nuclear import and release of a key regulator of sumoylation. <i> Grünwald M, Bono F. </i> EMBO J, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"2XWU"}],"region_id":"DP03553r001","statement":[{"text":"In the structure, some disordered stretches of residues at the N- and C-termini of Imp13, as well as a long inter-loop between HEAT 14 and 15 (residues 655–673) and a few residues in loops are missing in the final model; the full-length Ubc9 could be modelled.","type":"Results"},{"text":"Residues 1-18 and 656-673 are disordered in the structure.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-22T12:55:26.986Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":656,"end":673,"reference_id":"21139563","reference_source":"pmid","reference_html":"Structure of Importin13-Ubc9 complex: nuclear import and release of a key regulator of sumoylation. <i> Grünwald M, Bono F. </i> EMBO J, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"2XWU"}],"region_id":"DP03553r002","statement":[{"text":"In the structure, some disordered stretches of residues at the N- and C-termini of Imp13, as well as a long inter-loop between HEAT 14 and 15 (residues 655–673) and a few residues in loops are missing in the final model; the full-length Ubc9 could be modelled.","type":"Results"},{"text":"Residues 1-18 and 656-673 are disordered in the structure.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-22T12:55:48.499Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2023_12","sequence":"MERREEQPGAAGAGAAPALDFTVENVEKALHQLYYDPNIENKNLAQKWLMQAQVSPQAWHFSWQLLQPDKVPEIQYFGASALHIKISRYWSDIPTDQYESLKAQLFTQITRFASGSKIVLTRLCVALASLALSMMPDAWPCAVADMVRLFQAEDSPVDGQGRCLALLELLTVLPEEFQTSRLPQYRKGLVRTSLAVECGAVFPLLEQLLQQPSSPSCVRQKVLKCFSSWVQLEVPLQDCEALIQAAFAALQDSELFDSSVEAIVNAISQPDAQRYVNTLLKLIPLVLGLQEQLRQAVQNGDMETSHGICRIAVALGENHSRALLDQVEHWQSFLALVNMIMFCTGIPGHYPVNETTSSLTLTFWYTLQDDILSFEAEKQAVYQQVYRPVYFQLVDVLLHKAQFPSDEEYGFWSSDEKEQFRIYRVDISDTLMYVYEMLGAELLSNLYDKLGRLLTSSEEPYSWQHTEALLYGFQSIAETIDVNYSDVVPGLIGLIPRISISNVQLADTVMFTIGALSEWLADHPVMINSVLPLVLHALGNPELSVSSVSTLKKICRECKYDLPPYAANIVAVSQDVLMKQIHKTSQCMWLMQALGFLLSALQVEEILKNLHSLISPYIQQLEKLAEEIPNPSNKLAIVHILGLLSNLFTTLDISHHEDDHEGPELRKLPVPQGPNPVVVVLQQVFQLIQKVLSKWLNDAQVVEAVCAIFEKSVKTLLDDFAPMVPQLCEMLGRMYSTIPQASALDLTRQLVHIFAHEPAHFPPIEALFLLVTSVTLTLFQQGPRDHPDIVDSFMQLLAQALKRKPDLFLCERLDVKAVFQCAVLALKFPEAPTVKASCGFFTELLPRCGEVESVGKVVQEDGRMLLIAVLEAIGGQASRSLMDCFADILFALNKHCFSLLSMWIKEALQPPGFPSARLSPEQKDTFSQQILRERVNKRRVKEMVKEFTLLCRGLHGTDYTADY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref50":"UniRef50_O94829","uniref90":"UniRef90_O94829","uniref100":"UniRef100_O94829","genes":[{"name":{"value":"IPO13"},"synonyms":[{"value":"KIAA0724"},{"value":"RANBP13"}]}],"alphafold_very_low_content":0.03842159916926272,"disorder_content":0.037383177570093455,"disprot_consensus":{"full":[{"start":1,"end":18,"type":"D"},{"start":656,"end":673,"type":"D"}],"Structural state":[{"start":1,"end":18,"type":"D"},{"start":656,"end":673,"type":"D"}]}},{"disprot_id":"DP03554","acc":"Q9UKK9","creator":"vacs","date":"2021-11-22T10:24:41.670Z","features":{"pfam":[{"id":"PF00293","name":"NUDIX domain","start":60,"end":180}],"gene3D":[]},"length":219,"name":"ADP-sugar pyrophosphatase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":13,"reference_id":"17052728","reference_source":"pmid","reference_html":"Crystal structures of human NUDT5 reveal insights into the structural basis of the substrate specificity. <i> Zha M, Zhong C, Peng Y, Hu H, Ding J. </i> J Mol Biol, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2DSB"},{"db":"PDB","id":"2DSC"},{"db":"PDB","id":"2DSD"}],"region_id":"DP03554r001","statement":[{"text":"The experimental electron density map is of great quality except that the N-terminal 1–13 residues were disordered without electron density and therefore were omitted in the final model.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-11-22T12:53:42.673Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MESQEPTESSQNGKQYIISEELISEGKWVKLEKTTYMDPTGKTRTWESVKRTTRKEQTADGVAVIPVLQRTLHYECIVLVKQFRPPMGGYCIEFPAGLIDDGETPEAAALRELEEETGYKGDIAECSPAVCMDPGLSNCTIHIVTVTINGDDAENARPKPKPGDGEFVEVISLPKNDLLQRLDALVAEEHLTVDARVYSYALALKHANAKPFEVPFLKF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref50":"UniRef50_Q9UKK9","uniref90":"UniRef90_Q9UKK9","uniref100":"UniRef100_Q9UKK9","genes":[{"name":{"value":"NUDT5"},"synonyms":[{"value":"NUDIX5","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"27257257","url":"http://www.ncbi.nlm.nih.gov/pubmed/27257257","alternativeUrl":"https://europepmc.org/abstract/MED/27257257"}}]}],"orfNames":[{"value":"HSPC115","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11042152","url":"http://www.ncbi.nlm.nih.gov/pubmed/11042152","alternativeUrl":"https://europepmc.org/abstract/MED/11042152"}}]}]}],"alphafold_very_low_content":0.0502283105022831,"disorder_content":0.0593607305936073,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"D"}],"Structural state":[{"start":1,"end":13,"type":"D"}]}},{"disprot_id":"DP03555","acc":"Q8K310","creator":"fquaglia","date":"2021-11-22T16:53:27.929Z","features":{"pfam":[],"gene3D":[]},"length":846,"name":"Matrin-3","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":478,"end":496,"reference_id":"34783967","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N resonance assignments and solution structures of the two RRM domains of Matrin-3. <i> He F, Kuwasako K, Takizawa M, Takahashi M, Tsuda K, Nagata T, Watanabe S, Tanaka A, Kobayashi N, Kigawa T, Güntert P, Shirouzu M, Yokoyama S, Muto Y. </i> Biomol NMR Assign, 2022","date":"2022-08-05T14:19:38.644Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03555r001","statement":[{"text":"As described below, the N-terminal segment spanning residues 478–496 adopted a disordered structure, which caused the missing backbone resonances.","type":"Methods"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-08T17:51:34.563Z"}},{"start":478,"end":496,"reference_id":"34783967","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N resonance assignments and solution structures of the two RRM domains of Matrin-3. <i> He F, Kuwasako K, Takizawa M, Takahashi M, Tsuda K, Nagata T, Watanabe S, Tanaka A, Kobayashi N, Kigawa T, Güntert P, Shirouzu M, Yokoyama S, Muto Y. </i> Biomol NMR Assign, 2022","date":"2022-08-05T14:19:44.338Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03555r002","statement":[{"text":"As described below, the N-terminal segment spanning residues 478–496 adopted a disordered structure, which caused the missing backbone resonances.","type":"Methods"},{"text":"Flexible linker connecting RRM1 and RRM2 of mouse Matrin-3.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-08T17:51:52.149Z"}}],"regions_counter":2,"released":"2023_12","sequence":"MSKSFQQSSLGRDSQGHGRDLSAAGIGLLAAATQSLSMPASLGRMNQGTARLASLMNLGMSSSLNQQGAHSALSSASTSSHNLQSIFNIGSRGPLPLSSQHRGDTDQASNILASFGLSARDLDELSRYPEDKITPENLPQILLQLKRRRTEEGPTLSYGRDGRSATREPPYRVPRDDWEEKRHFRRDSFDDRGPSLNPVLDYDHGSRSQESGYYDRMDYEDDRLRDGERCRDDSFFGETSHNYHKFDSEYERMGRGPGPLQERSLFEKKRGAPPSSNIEDFHGLLPKGYPHLCSICDLPVHSNKEWSQHINGASHSRRCQLLLEIYPEWNPDNDTGHTMGDPFMLQQSTNPAPGILGPPPPSFHLGGPAVGPRGNLGAGNGNLQGPRHMQKGRVETSRVVHIMDFQRGKNLRYQLLQLVEPFGVISNHLILNKINEAFIEMATTEDAQAAVDYYTTTPALVFGKPVRVHLSQKYKRIKKPEGKPDQKFDQKQELGRVIHLSNLPHSGYSDSAVLKLAEPYGKIKNYILMRMKSQAFIEMETREDAMAMVDHCLKKALWFQGRCVKVDLSEKYKKLVLRIPNRGIDLLKKDKSRKRSYSPDGKESPSDKKSKTDAQKTESPAEGKEQEEKSGEDGEKDTKDDQTEQEPSMLLESEDELLVDEEEAAALLESGSSVGDETDLANLGDVSSDGKKEPSDKAVKKDPSASATSKKKLKKVDKIEELDQENEAALENGIKNEENTEPGAESAENADDPNKDTSENADGQNDENKEDYTIPDEYRIGPYQPNVPVGIDYVIPKTGFYCKLCSLFYTNEEVAKNTHCSSLPHYQKLKKFLNKLAEERRQKKET","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"uniref50":"UniRef50_P43243","uniref90":"UniRef90_P43243","uniref100":"UniRef100_Q8K310","genes":[{"name":{"value":"Matr3"}}],"alphafold_very_low_content":0.5543735224586288,"dataset":["RNA-binding proteins"],"disorder_content":0.022458628841607566,"disprot_consensus":{"full":[{"start":478,"end":496,"type":"D"}],"Structural state":[{"start":478,"end":496,"type":"D"}],"Disorder function":[{"start":478,"end":496,"type":"F"}]}},{"disprot_id":"DP03556","acc":"P35813","creator":"vacs","date":"2021-11-23T09:29:57.756Z","features":{"pfam":[{"id":"PF00481","name":"Protein phosphatase 2C","start":23,"end":284},{"id":"PF07830","name":"Protein serine/threonine phosphatase 2C, C-terminal domain","start":285,"end":363}],"gene3D":[]},"length":382,"name":"Protein phosphatase 1A","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":369,"end":382,"reference_id":"9003755","reference_source":"pmid","reference_html":"Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution. <i> Das AK, Helps NR, Cohen PT, Barford D. </i> EMBO J, 1996","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"1A6Q"}],"region_id":"DP03556r001","statement":[{"text":"Two regions of polypeptide that are not visible in the electron density map are assumed to be disordered. These are residues 322-325, which connect the α-helices a7 and a8, and the C-terminal 18 residues.","type":"Results"},{"text":"The last 14 residues are disordered in the structure.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-06T15:28:47.693Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MGAFLDKPKMEKHNAQGQGNGLRYGLSSMQGWRVEMEDAHTAVIGLPSGLESWSFFAVYDGHAGSQVAKYCCEHLLDHITNNQDFKGSAGAPSVENVKNGIRTGFLEIDEHMRVMSEKKHGADRSGSTAVGVLISPQHTYFINCGDSRGLLCRNRKVHFFTQDHKPSNPLEKERIQNAGGSVMIQRVNGSLAVSRALGDFDYKCVHGKGPTEQLVSPEPEVHDIERSEEDDQFIILACDGIWDVMGNEELCDFVRSRLEVTDDLEKVCNEVVDTCLYKGSRDNMSVILICFPNAPKVSPEAVKKEAELDKYLECRVEEIIKKQGEGVPDLVHVMRTLASENIPSLPPGGELASKRNVIEAVYNRLNPYKNDDTDSTSTDDMW","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"uniref50":"UniRef50_P35813","uniref90":"UniRef90_P35813","uniref100":"UniRef100_P35813","genes":[{"name":{"value":"PPM1A"},"synonyms":[{"value":"PPPM1A"}]}],"alphafold_very_low_content":0.034031413612565446,"disorder_content":0.03664921465968586,"disprot_consensus":{"full":[{"start":369,"end":382,"type":"D"}],"Structural state":[{"start":369,"end":382,"type":"D"}]}},{"disprot_id":"DP03557","acc":"Q91AU0","creator":"vnugnes","date":"2021-11-23T10:46:39.056Z","features":{"pfam":[{"id":"PF00998","name":"Viral RNA dependent RNA polymerase","start":2422,"end":2932},{"id":"PF01001","name":"Hepatitis C virus non-structural protein NS4b","start":1728,"end":1921},{"id":"PF01006","name":"Hepatitis C virus non-structural protein NS4a","start":1658,"end":1711},{"id":"PF01506","name":"Hepatitis C virus non-structural 5a protein membrane anchor","start":1974,"end":1996},{"id":"PF01538","name":"Hepatitis C virus non-structural protein NS2","start":811,"end":1005},{"id":"PF01539","name":"Hepatitis C virus envelope glycoprotein E1","start":193,"end":382},{"id":"PF01542","name":"Hepatitis C virus core protein","start":116,"end":190},{"id":"PF01543","name":"Hepatitis C virus capsid protein","start":2,"end":115},{"id":"PF01560","name":"Hepatitis C virus non-structural protein E2/NS1","start":387,"end":729},{"id":"PF02907","name":"Hepatitis C virus NS3 protease","start":1056,"end":1203},{"id":"PF08300","name":"Hepatitis C virus non-structural 5a zinc finger domain","start":2006,"end":2067},{"id":"PF08301","name":"Hepatitis C virus non-structural 5a domain 1b","start":2068,"end":2168},{"id":"PF12941","name":"HCV NS5a protein C-terminal region","start":2179,"end":2419},{"id":"PF22027","name":"NS3 RNA helicase, C-terminal helical domain","start":1516,"end":1656}],"gene3D":[]},"length":3010,"name":"Core protein precursor","ncbi_taxon_id":31647,"organism":"Hepatitis C virus subtype 1b","regions":[{"start":2223,"end":2314,"reference_id":"22720086","reference_source":"pmid","reference_html":"Intrinsically unstructured domain 3 of hepatitis C Virus NS5A forms a \"fuzzy complex\" with VAPB-MSP domain which carries ALS-causing mutations. <i> Gupta G, Qin H, Song J. </i> PLoS One, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03557r001","statement":[{"text":"By contrast, the fragments consisting of D2 or/and D3 domains have far-UV CD spectra typical of proteins of being predominantly disordered, consistent with previous reports on NS5A D2 and D3 of other HCV isolates [36]–[39].","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-06T08:32:00.170Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":2331,"end":2419,"reference_id":"22720086","reference_source":"pmid","reference_html":"Intrinsically unstructured domain 3 of hepatitis C Virus NS5A forms a \"fuzzy complex\" with VAPB-MSP domain which carries ALS-causing mutations. <i> Gupta G, Qin H, Song J. </i> PLoS One, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03557r002","statement":[{"text":"By contrast, the fragments consisting of D2 or/and D3 domains have far-UV CD spectra typical of proteins of being predominantly disordered, consistent with previous reports on NS5A D2 and D3 of other HCV isolates [36]–[39].","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-06T08:31:42.587Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":2331,"end":2419,"reference_id":"22720086","reference_source":"pmid","reference_html":"Intrinsically unstructured domain 3 of hepatitis C Virus NS5A forms a \"fuzzy complex\" with VAPB-MSP domain which carries ALS-causing mutations. <i> Gupta G, Qin H, Song J. </i> PLoS One, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"interaction_partner":[{"db":"UniProt","id":"O95292","partner_start":1,"partner_end":125}],"region_id":"DP03557r003","statement":[{"text":"Remarkably, as shown in Figure 3c, addition of D3 sample not only induced the disappearance of almost the same set of HSQC peaks as induced by NS5A(300–447), but also triggered significant shifts of many extra residues. This implies that the majority of the NS5A residues critical for binding VAPB are located on NS5A-D3. ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-06T08:32:11.498Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":2331,"end":2419,"reference_id":"22720086","reference_source":"pmid","reference_html":"Intrinsically unstructured domain 3 of hepatitis C Virus NS5A forms a \"fuzzy complex\" with VAPB-MSP domain which carries ALS-causing mutations. <i> Gupta G, Qin H, Song J. </i> PLoS One, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03557r004","statement":[{"text":"The recombinant 89-residue NS5A-D3 protein has a far-UV CD spectrum (Figure 4a) typical of highly-unstructured proteins, consistent with previous reports on NS5A-D3 of other HCV isolates [38], [39]. This conclusion is further evident from the very narrow 1H-(1.8 ppm) and 15N-(19.5 ppm) spectral dispersions of its HSQC spectrum (Figure 4b), which also indicate the absence of a tight tertiary packing in D3.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-06T08:31:40.464Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":2379,"end":2398,"reference_id":"22720086","reference_source":"pmid","reference_html":"Intrinsically unstructured domain 3 of hepatitis C Virus NS5A forms a \"fuzzy complex\" with VAPB-MSP domain which carries ALS-causing mutations. <i> Gupta G, Qin H, Song J. </i> PLoS One, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140311","term_name":"protein sequestering activity","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03557r005","statement":[{"text":"These results thus suggest that in the pre-existence of D3B, EphA4 at low concentration is not able to bind to VAPB-MSP but at high concentrations, EphA4 will start to displace the D3B peptide from binding with the MSP fold. Therefore, NS5A does compete with EphA4 in binding with VAPB-MSP.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-06T08:32:23.036Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The selective interaction of a protein with a specific protein, to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:1493333]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":5,"released":"2023_06","sequence":"MSTIPKPQRKTKRNTYRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRATRKTSERSQPRGRRQPIPKARRPEGWAWAQPGYPWPLYGNEGLGWAGWLLSPRGSRPSWGPIDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLALLSCLTIPASAYEVRNASGVYHVTNDCSNSSIVYEAADIIMHTPGCVPCVRENNSSRCWVALTPTLAARNLSVPTTTIRRHVDLLVGAAAFCSAMYVGDLCGSVLLVSQLFTLSPRQHETVQDCNCSLYPGHVTGHRMAWDMMMNWSPTTALVLSQILRIPQTIVDMVAGAHWGVLAGIAYYSMVGNWAKVLVVMLLFAGVDGHTQVMGGSQASTINTLTGIFSPGAKQKIQLINTNGSWHINRTALNCNDSLNTGFLAALFYTHSFNSSGCLERMASCRPIDKFDQGWGPITYDEGPDLDQRPYCWHYAPRSCGIVPASQVCGPVYCFTPSPVVVGTTDRTGAPTYRWGENETDVLILNNTRPPQGNWFGCTWMNSTGFTKTCGGPPCNIGGAGNNTLVCPTDCFRKHPEATYTKCGSGPWLTPRCMVDYPYRPWHYPCTVNFTIFKVRMYVGGVEHRLNAARNWTRGERCDLEDRDRSELSPLLLSTTEWQILPCSFTTLPALSTGLIHLHQNIVDVQYLYGIGSVVVSLVIKWEYVLLSFFLLADARVCACLWMMLLIAQAEAALENLVVLNAASVAGAHGILTFLVFFCAAWYIKGRLVPGAAYAFYGVWPLLLLLLALPPRAYAMDREMAASCGGAVFIGLVLLTLSPHYKVFLARLIWWLQYFTTRAEAILHVWVPPLNVRGGRDAVILLTCAVHPDLIFDITKLLLAVLGPLMVFLAGITRVPYFVRAQGLIRACALARKVAGGHYIQMALMKLAALTGTYLYDHLTPLRDWAHAGLRDLAVAVEPVVFSDMETKIITWGADTAACGDIILGLPVSARRGREILLGPADSLEGQGWRLLAPITAYSQQTRGLLGCIITSLTGRDKNQVEGEVQVVSTATQSFLATCVNGVCWTVFHGAGSKTLAGPKGPITQMYTNVDQDLVGWQAPPGARSLTPCTCGSSDLYLVTRHADVIPVRRRGDNRGSLLSPRPVSYLKGSSGGPLLCPSGHAVGIFRAAVCTRGVAKAVDFIPVESMETTMRSPVFTDNSSPPAVPQTFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGTYMSKAYGVDPNIRTGVRTITTGAPITYSTYGKFLADGGCSGGAYDIIMCDECHSTDSTTVLGIGTVLDQAETAGARLVVLATATPPGSVTVPHPNIEEIALSNTGEIPFYGKAIPIETIKGGRHLIFCHSKKKCDELAAKLSGLGLNAVAYYRGLDVSVIPTSGDVVVVATDALMTGFTGDSDSVIDCNTCVTQTVDFSLDPTFTIETTTVPQDAVSRSQRRGRTGRGRGGIYRFVTPGERPSGMFDSSVLCECYDAGCAWYELTPAETSVRLRAYLNTPGLPVCQDHLEFWESVFTGLTHIDAHFLSQTKQAGDNFPYLVAYQATVCARAQAPPPSWDQMWKSLIRLKPTLHGPTPLLYRLGTVQSEITLTHPVTKYIMACMSADLEVVTSTWVLVSGVLAALAAYCLTTGSVVIVGRIILSGKPAVIPDREVLYREFDEMEECASHLPYIEQGMQLAEQFKQKALGLLQTATKQAEAAAPVVESKWRALEAFWAKHMWNFISGIQYLAGLSTLHGNPAIASLMAFTASITSPLTTQHTLLFNILGGWVAAQLAPPSAASAFVGAGIAGAAVGSIGLGKVLVDVLAGYGAGVAGALVAFKVMSGEVPSTEDLVNLLPAVLSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLIAFASRGNHVSPTHYVPESDAAARVTQILSSLTVTQLLRRLHQWINEDCSTPCSGSWLRDVWDWICTVLTDFKTWLQSKLLPRLPGVPFFSCQRGYRGVWRGDGIMQTTCPCGAQISGHVKNGSMRIVGPRSCSNTWHGTFPINAYTTGPCTPAPAPNYSRALWRVAAEEYVEVTRVGDFHYVTGMTTDNVKCPCQVPAPEFFTEVDGVRLHRYAPACKPLLREEVTFQVGLNQYLVGSQLPCEPEPDVAVLTSMLTDPSHITAETAKRRLDRGSPPSLASSSASQLSAPSLKATCTTRHDSPDAGLIEANLLWRQEMGGNITRVESENKVVILDSFEPLRAEEDEREVSVPAEILRKSRKFPRAMPIWARPDYNPPLLESWKNPDYVPPVVHGCPLPPIKGPPIPPPRRKRTVVLTESTVSSALAELATKTFGSSGSSAVDSGTASAPPDQPSDNGDAGSDAESYSSMPPLEGEPGDPDLSDGSWSTVSEEASEDVVCCSMSYTWTGALITPCAAEESKLPINALSNSLLRHHNMVYATTSRSASQRQKKVTFDRLQVLDDHYRDVLKEMKAKASTVKAKLLSVEEACKLTPPHSAKSKFGYGAKDVRNLSSKAVNHIRSVWKDLLEDTETPIDTTIMAKNEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVSTLPQAVMGSSYGFQYSPGQRVEFLVNAWKSKKSPMGFAYDTRCFDSTVTESDIRVEESIYQCCDLVPEARQAIRSLTERLYVGGPLTNSKGQNCGYRRCRASGVLTTSCGNTLTCYLKASAACRAAKLQDCTMLVCGDDLVVICESAGTQEDAASLRVFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDASGKRVYYLTRDPTTPLARAAWETARHTPVNSWLGNIIMYAPTLWARMILMTHFFSILLAQEQLEKALDCQIYGAYYSIEPLDLPQIIERLHGLSAFSLHSYSPGEINRVASCLRKLGVPPLRAWRHRARSVRAKLLSQGGRAATCGKYLFNWAVKTKLKLTPIPAASQLDLSGWFVAGYGGGDIYHSLSRARPRWFMLCLPLLSVGVGINLLPNR","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Hepacivirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_P27958","uniref90":"UniRef90_Q00269","uniref100":"UniRef100_Q91AU0","genes":[],"disorder_content":0.060132890365448506,"disprot_consensus":{"full":[{"start":2223,"end":2314,"type":"D"},{"start":2331,"end":2419,"type":"D"}],"Structural state":[{"start":2223,"end":2314,"type":"D"},{"start":2331,"end":2419,"type":"D"}],"Molecular function":[{"start":2331,"end":2419,"type":"F"}]}},{"disprot_id":"DP03558","acc":"P04591","creator":"jbergier","date":"2021-11-25T13:42:15.894Z","features":{"pfam":[{"id":"PF00098","name":"Zinc knuckle","start":391,"end":406},{"id":"PF00098","name":"Zinc knuckle","start":412,"end":428},{"id":"PF00540","name":"gag gene protein p17 (matrix protein)","start":2,"end":132},{"id":"PF00607","name":"gag protein p24 N-terminal domain","start":144,"end":251},{"id":"PF08705","name":"Gag protein p6","start":449,"end":486},{"id":"PF19317","name":"Gag protein p24 C-terminal domain","start":276,"end":349}],"gene3D":[]},"length":500,"name":"Gag polyprotein","ncbi_taxon_id":11706,"organism":"Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)","regions":[{"start":110,"end":148,"reference_id":"25713345","reference_source":"pmid","reference_html":"Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy. <i> Deshmukh L, Ghirlando R, Clore GM. </i> Proc Natl Acad Sci U S A, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03558r001","statement":[{"text":"The linker regions in ΔGag exhibit low 15N-{1H} heteronuclear NOE values, close to zero 1DNH RDC values, and nearly random coil chemical shifts (Fig. 4, Table S3, and Fig. S2), indicative of intrinsic disorder and high mobility such that the ordered structural domains are like beads on a string. These regions include the large stretch of residues connecting MA to CA (residues 110–148), the C-terminal tail of CA (residues 353–363) and the SP1 region that connects CA to the N-terminal zinc-knuckle of NC (residues 364–377), and the linker (residues 408–412, especially residues 411 and 412) that connects the N- and C-terminal zinc knuckles of NC. Overall, these flexible, solvent exposed regions are primarily responsible for extreme sensitivity of Gag to proteolysis and conformational heterogeneity that precludes crystallization.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T12:28:55.263Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":353,"end":363,"reference_id":"25713345","reference_source":"pmid","reference_html":"Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy. <i> Deshmukh L, Ghirlando R, Clore GM. </i> Proc Natl Acad Sci U S A, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03558r002","statement":[{"text":"The linker regions in ΔGag exhibit low 15N-{1H} heteronuclear NOE values, close to zero 1DNH RDC values, and nearly random coil chemical shifts (Fig. 4, Table S3, and Fig. S2), indicative of intrinsic disorder and high mobility such that the ordered structural domains are like beads on a string. These regions include the large stretch of residues connecting MA to CA (residues 110–148), the C-terminal tail of CA (residues 353–363) and the SP1 region that connects CA to the N-terminal zinc-knuckle of NC (residues 364–377), and the linker (residues 408–412, especially residues 411 and 412) that connects the N- and C-terminal zinc knuckles of NC. Overall, these flexible, solvent exposed regions are primarily responsible for extreme sensitivity of Gag to proteolysis and conformational heterogeneity that precludes crystallization.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T12:28:51.667Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":364,"end":377,"reference_id":"25713345","reference_source":"pmid","reference_html":"Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy. <i> Deshmukh L, Ghirlando R, Clore GM. </i> Proc Natl Acad Sci U S A, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03558r003","statement":[{"text":"The linker regions in ΔGag exhibit low 15N-{1H} heteronuclear NOE values, close to zero 1DNH RDC values, and nearly random coil chemical shifts (Fig. 4, Table S3, and Fig. S2), indicative of intrinsic disorder and high mobility such that the ordered structural domains are like beads on a string. These regions include the large stretch of residues connecting MA to CA (residues 110–148), the C-terminal tail of CA (residues 353–363) and the SP1 region that connects CA to the N-terminal zinc-knuckle of NC (residues 364–377), and the linker (residues 408–412, especially residues 411 and 412) that connects the N- and C-terminal zinc knuckles of NC. Overall, these flexible, solvent exposed regions are primarily responsible for extreme sensitivity of Gag to proteolysis and conformational heterogeneity that precludes crystallization.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T12:28:28.306Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":133,"end":145,"reference_id":"25713345","reference_source":"pmid","reference_html":"Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy. <i> Deshmukh L, Ghirlando R, Clore GM. </i> Proc Natl Acad Sci U S A, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03558r004","statement":[{"text":"In intact ΔGag, the N-terminal residues of CA (residues 133–145) are intrinsically disordered and exhibit narrow chemical shift dispersion (see above and Fig. S2). As proteolysis of ΔGag proceeds, new 1HN/15N cross-peaks appear in the spectrum and grow in intensity with time (Fig. 5A). A few of these can be readily assigned by reference to the spectrum of isolated CA. Among these Ile134, Val135, Asn137, Gly140, Met142, Val143, His144, and Gln145 are directly involved in the formation of the β-hairpin (residues 133–145) and exhibit completely different chemical shifts (labeled in blue in Fig. 5A) compared with their unstructured counterparts.","type":"Results"}],"states_connection":[{"source":"DP03558r001","target":"DP03558r005"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T12:28:57.492Z"},"ec_go":"EXP","disprot_namespace":"Structural transition"},{"start":133,"end":145,"reference_id":"25713345","reference_source":"pmid","reference_html":"Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy. <i> Deshmukh L, Ghirlando R, Clore GM. </i> Proc Natl Acad Sci U S A, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03558r005","statement":[{"text":"As proteolysis of ΔGag proceeds, new 1HN/15N cross-peaks appear in the spectrum and grow in intensity with time (Fig. 5A). A few of these can be readily assigned by reference to the spectrum of isolated CA. Among these Ile134, Val135, Asn137, Gly140, Met142, Val143, His144, and Gln145 are directly involved in the formation of the β-hairpin (residues 133–145) and exhibit completely different chemical shifts (labeled in blue in Fig. 5A) compared with their unstructured counterparts.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T12:28:25.961Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":5,"released":"2021_12","sequence":"MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAADTGHSNQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNSATIMMQRGNFRNQRKIVKCFNCGKEGHTARNCRAPRKKGCWKCGKEGHQMKDCTERQANFLGKIWPSYKGRPGNFLQSRPEPTAPPEESFRSGVETTTPPQKQEPIDKELYPLTSLRSLFGNDPSSQ","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"dataset":["Viral proteins","Condensates-related proteins","RNA-binding proteins"],"uniref50":"UniRef50_P04591","uniref90":"UniRef90_P04591","uniref100":"UniRef100_P04591","genes":[{"name":{"value":"gag"}}],"disorder_content":0.128,"disprot_consensus":{"full":[{"start":110,"end":132,"type":"D"},{"start":133,"end":145,"type":"T"},{"start":146,"end":148,"type":"D"},{"start":353,"end":377,"type":"D"}],"Structural state":[{"start":110,"end":148,"type":"D"},{"start":353,"end":377,"type":"D"}],"Structural transition":[{"start":133,"end":145,"type":"T"}]}},{"disprot_id":"DP03559","acc":"P04610","creator":"vnugnes","date":"2021-11-30T10:56:49.600Z","features":{"pfam":[{"id":"PF00539","name":"Transactivating regulatory protein (Tat)","start":2,"end":64}],"gene3D":[]},"length":86,"name":"Protein Tat","ncbi_taxon_id":11686,"organism":"Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI)","regions":[{"start":1,"end":86,"reference_id":"11098404","reference_source":"pmid","reference_html":"1H-13C nuclear magnetic resonance assignment and structural characterization of HIV-1 Tat protein. <i> Péloponèse JM, Grégoire C, Opi S, Esquieu D, Sturgis J, Lebrun E, Meurs E, Collette Y, Olive D, Aubertin AM, Witvrow M, Pannecouque C, De Clercq E, Bailly C, Lebreton J, Loret EP. </i> C R Acad Sci III, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"1JFW"}],"region_id":"DP03559r001","statement":[{"text":"The main difficulty in determining the NMR Tat structure was to resolve the sequential assignment [23]. This was due to the high number of peak overlaps in the homonuclear 1H NMR spectra, repetitive sequences and the presence of 11 prolines.","type":"Results"},{"text":"This could be due to the absence of α-helix and β-sheet and the flexibility of the Tat backbone, which induces the poor dispersion of our NMR spectra. However, the nanomolar activities observed with Tat indicate that Tat certainly has a conserved folding. We identified 272 long-range NOEs that would have almost disappeared with a random coil. The long-range NOEs, observed with almost each residue (figure 6), suggest a certain stability of our structure compared to the one studied by Bayer et al.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-03T08:43:20.344Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":86,"reference_id":"21752913","reference_source":"pmid","reference_html":"The HIV-1 Tat protein has a versatile role in activating viral transcription. <i> Das AT, Harwig A, Berkhout B. </i> J Virol, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019080","term_name":"viral gene expression","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0005648","ec_ontology":"ECO","ec_name":"luciferase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03559r002","statement":[{"text":"The Tatwt construct did indeed result in a high level of luciferase expression (Fig. 1C). The TatY26A variant showed an approximately 4-fold-reduced luciferase level, which confirms that the Y26A mutation significantly reduces Tat activity. In agreement with their inability to produce functional Tat protein, the Tatstop and Tatfs constructs resulted in very low luciferase levels that are indistinguishable from the background level obtained upon cotransfection of a control plasmid instead of HIV-rtTA.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-03T08:43:28.625Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A process by which a viral gene is converted into a mature gene product or products (proteins or RNA). This includes viral transcription, processing to produce a mature RNA product, and viral translation.\" [GOC:bf, GOC:jl, ISBN:0121585336]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":86,"reference_id":"10206951","reference_source":"pmid","reference_html":"Full peptide synthesis, purification, and characterization of six Tat variants. Differences observed between HIV-1 isolates from Africa and other continents. <i> Péloponèse JM, Collette Y, Grégoire C, Bailly C, Campèse D, Meurs EF, Olive D, Loret EP. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0001069","term_name":"regulatory region RNA binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"RNAcentral","id":"URS000071DF2D_576904","partner_start":null,"partner_end":null}],"region_id":"DP03559r003","statement":[{"text":"The six synthetic Tat proteins can bind to TAR RNA (Fig.3) and can inhibit PKR (data not shown). ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-03T08:39:52.161Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a RNA region that regulates a nucleic acid-based process. Such processes include transcription, DNA replication, and DNA repair.\" [GOC:txnOH]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":86,"reference_id":"10206951","reference_source":"pmid","reference_html":"Full peptide synthesis, purification, and characterization of six Tat variants. Differences observed between HIV-1 isolates from Africa and other continents. <i> Péloponèse JM, Collette Y, Grégoire C, Bailly C, Campèse D, Meurs EF, Olive D, Loret EP. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03559r004","statement":[{"text":"In aqueous buffer (Fig. 4 A), it can be deduced from the intensity of the negative 200 nm band that nonorganized structures are predominant (29). TableI reveals that there is no α helix in aqueous buffer excepted for Tat Mal and Tat Z2, which could have a short helix of eight to nine residues. ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-03T08:39:49.726Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":86,"reference_id":"10206951","reference_source":"pmid","reference_html":"Full peptide synthesis, purification, and characterization of six Tat variants. Differences observed between HIV-1 isolates from Africa and other continents. <i> Péloponèse JM, Collette Y, Grégoire C, Bailly C, Campèse D, Meurs EF, Olive D, Loret EP. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019080","term_name":"viral gene expression","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0005616","ec_ontology":"ECO","ec_name":"beta-galactosidase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03559r005","statement":[{"text":"In each case, Tat was added to the cell buffer, and therefore expression of β-gal up to the control means that the synthetic Tat was able to cross the cytoplasmic and nucleus membranes, bind TAR, and interact with cellular cofactors.","type":"Figure"},{"text":"Tat Bru can trans-activate HIV-1 LTR whereas Tat Oyi cannot, but they are both phosphorylated by PKR.","type":"Results"},{"text":"At 10 μm, the six Tat were showing levels of trans-activation so high that it was impossible to see differences between them because there was saturation.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-03T08:39:55.094Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A process by which a viral gene is converted into a mature gene product or products (proteins or RNA). This includes viral transcription, processing to produce a mature RNA product, and viral translation.\" [GOC:bf, GOC:jl, ISBN:0121585336]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":86,"reference_id":"10206951","reference_source":"pmid","reference_html":"Full peptide synthesis, purification, and characterization of six Tat variants. Differences observed between HIV-1 isolates from Africa and other continents. <i> Péloponèse JM, Collette Y, Grégoire C, Bailly C, Campèse D, Meurs EF, Olive D, Loret EP. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019080","term_name":"viral gene expression","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0005648","ec_ontology":"ECO","ec_name":"luciferase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03559r006","statement":[{"text":"At 10 μm, the six Tat were showing levels of trans-activation so high that it was impossible to see differences between them because there was saturation.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-03T08:39:53.511Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A process by which a viral gene is converted into a mature gene product or products (proteins or RNA). This includes viral transcription, processing to produce a mature RNA product, and viral translation.\" [GOC:bf, GOC:jl, ISBN:0121585336]","disprot_namespace":"Disorder function","term_is_binding":false}],"regions_counter":6,"released":"2021_12","sequence":"MEPVDPRLEPWKHPGSQPKTACTTCYCKKCCFHCQVCFTTKALGISYGRKKRRQRRRPPQGSQTHQVSLSKQPTSQPRGDPTGPKE","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"dataset":["Viral proteins","RNA-binding proteins"],"uniref50":"UniRef50_P04608","uniref90":"UniRef90_P04610","uniref100":"UniRef100_P04610","genes":[{"name":{"value":"tat","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04079","url":"https://hamap.expasy.org/unirule/MF_04079"}}]}}],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":86,"type":"D"}],"Structural state":[{"start":1,"end":86,"type":"D"}],"Biological process":[{"start":1,"end":86,"type":"F"}],"Molecular function":[{"start":1,"end":86,"type":"F"}]}},{"disprot_id":"DP03560","acc":"P20879","creator":"vnugnes","date":"2021-11-30T14:29:25.893Z","features":{"pfam":[{"id":"PF00539","name":"Transactivating regulatory protein (Tat)","start":2,"end":64}],"gene3D":[]},"length":101,"name":"Protein Tat","ncbi_taxon_id":11688,"organism":"Human immunodeficiency virus type 1 group M subtype B (isolate JRCSF)","regions":[{"start":1,"end":101,"reference_id":"10206951","reference_source":"pmid","reference_html":"Full peptide synthesis, purification, and characterization of six Tat variants. Differences observed between HIV-1 isolates from Africa and other continents. <i> Péloponèse JM, Collette Y, Grégoire C, Bailly C, Campèse D, Meurs EF, Olive D, Loret EP. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03560r001","statement":[{"text":"In aqueous buffer (Fig. 4 A), it can be deduced from the intensity of the negative 200 nm band that nonorganized structures are predominant (29). TableI reveals that there is no α helix in aqueous buffer excepted for Tat Mal and Tat Z2, which could have a short helix of eight to nine residues.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-03T08:39:20.065Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":101,"reference_id":"10206951","reference_source":"pmid","reference_html":"Full peptide synthesis, purification, and characterization of six Tat variants. Differences observed between HIV-1 isolates from Africa and other continents. <i> Péloponèse JM, Collette Y, Grégoire C, Bailly C, Campèse D, Meurs EF, Olive D, Loret EP. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0001069","term_name":"regulatory region RNA binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"RNAcentral","id":"URS000071DF2D_576904","partner_start":null,"partner_end":null}],"region_id":"DP03560r002","statement":[{"text":"The K d values vary from approximately 50 nm for both Tat Eli and Tat Mal to about 140 nmfor Tat Oyi and Tat JR. ","type":"Figure"},{"text":"The six synthetic Tat proteins can bind to TAR RNA (Fig.3) and can inhibit PKR (data not shown).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-03T08:39:21.444Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a RNA region that regulates a nucleic acid-based process. Such processes include transcription, DNA replication, and DNA repair.\" [GOC:txnOH]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":101,"reference_id":"10206951","reference_source":"pmid","reference_html":"Full peptide synthesis, purification, and characterization of six Tat variants. Differences observed between HIV-1 isolates from Africa and other continents. <i> Péloponèse JM, Collette Y, Grégoire C, Bailly C, Campèse D, Meurs EF, Olive D, Loret EP. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019080","term_name":"viral gene expression","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0005616","ec_ontology":"ECO","ec_name":"beta-galactosidase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03560r003","statement":[{"text":"In each case, Tat was added to the cell buffer, and therefore expression of β-gal up to the control means that the synthetic Tat was able to cross the cytoplasmic and nucleus membranes, bind TAR, and interact with cellular cofactors.","type":"Figure"},{"text":"At 10 μm, the six Tat were showing levels of trans-activation so high that it was impossible to see differences between them because there was saturation.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-03T08:39:23.529Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A process by which a viral gene is converted into a mature gene product or products (proteins or RNA). This includes viral transcription, processing to produce a mature RNA product, and viral translation.\" [GOC:bf, GOC:jl, ISBN:0121585336]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":101,"reference_id":"10206951","reference_source":"pmid","reference_html":"Full peptide synthesis, purification, and characterization of six Tat variants. Differences observed between HIV-1 isolates from Africa and other continents. <i> Péloponèse JM, Collette Y, Grégoire C, Bailly C, Campèse D, Meurs EF, Olive D, Loret EP. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019080","term_name":"viral gene expression","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0005648","ec_ontology":"ECO","ec_name":"luciferase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03560r004","statement":[{"text":"At 10 μm, the six Tat were showing levels of trans-activation so high that it was impossible to see differences between them because there was saturation.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-03T08:39:22.406Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A process by which a viral gene is converted into a mature gene product or products (proteins or RNA). This includes viral transcription, processing to produce a mature RNA product, and viral translation.\" [GOC:bf, GOC:jl, ISBN:0121585336]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":41,"end":54,"reference_id":"11080476","reference_source":"pmid","reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","date":"2024-05-03T10:33:16.959Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"GO:1990970","term_name":"trans-activation response element binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"RNAcentral","id":"URS00006B18E8_388826","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03560r005","statement":[{"text":"The results of such an experiment are shown in Fig. 3A, where wild-type peptide 41-54 was capable of binding to TAR RNA (lane 3).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a trans-activation response (TAR) element, a hairpin RNA structure located at the 5' end of all HIV-1 transcripts, and which is required for trans-activation of a viral promoter.\" [GOC:bf, GOC:PARL, PMID:25116364, Wikipedia:Trans-activation_response_element_(TAR)]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-06T12:58:44.442Z"}},{"start":41,"end":54,"reference_id":"11080476","reference_source":"pmid","reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","date":"2024-04-30T15:50:58.990Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000039","term_name":"acetylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001254","ec_ontology":"ECO","ec_name":"radioisotope assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP03560r009","statement":[{"text":"The results of such an experiment are shown in Fig. 1C, where Tat 41-54\npeptide, but not 41-50 peptide (lanes 7±10), was acetylated with GST-HAT.","type":"Results"}]},{"start":41,"end":54,"reference_id":"11080476","reference_source":"pmid","reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","date":"2024-04-30T16:09:32.033Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1905215","term_name":"negative regulation of RNA binding","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007009","ec_ontology":"ECO","ec_name":"radioligand binding assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","start":50,"end":50,"position":"Specific residue"},{"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","start":51,"end":51,"position":"Specific residue"}],"ec_go":"IPI","region_id":"DP03560r010","statement":[{"text":"The results of such an experiment are shown in Fig. 3A, where wild-type peptide 41-54 was capable of binding to TAR RNA (lane 3). The TAR RNA binding is completely abolished when lysines 50 and 51 are acetylated (lanes 6 and 7). We observed no binding of double-acetylated 50 and 51 peptide to TAR RNA at any peptide concentration (data not shown). Similar results were also observed when Tat protein was acetylated with GST-HAT prior to TAR RNA binding (Fig. 3B, lanes 4 and 5).","type":"Results"}],"term_comment":"","term_def":"\"Any process that stops, prevents or reduces the frequency, rate or extent of RNA binding.\" [GO_REF:0000059, GOC:bf, GOC:PARL, GOC:TermGenie]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"RNAcentral","id":"URS00006B18E8_388826","operator":"and","partner_start":null,"partner_end":null}]},{"start":42,"end":54,"reference_id":"11080476","reference_source":"pmid","reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","date":"2024-04-30T17:32:36.398Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006077","ec_ontology":"ECO","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0239","term_name":"biotin","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"We decided to address this question by utilizing affinity pull-down experiments using wild-type or acetylated 42-54 peptides coupled to a biotin moiety."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q92793","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"O60563","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P20226","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP03560r011","statement":[{"text":"The results of such an experiment are shown in Fig. 7A, where 35Slabeled TBP, CBP, and cyclin T could efficiently bind to wild-type but not acetylated 42-50 peptide.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":42,"end":54,"reference_id":"11080476","reference_source":"pmid","reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","date":"2024-04-30T17:50:37.653Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0001223","term_name":"transcription coactivator binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006077","ec_ontology":"ECO","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0239","term_name":"biotin","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"We decided to address this question by utilizing affinity pull-down experiments using wild-type or acetylated 42-54 peptides coupled to a biotin moiety."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q92793","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03560r012","statement":[{"text":"The results of such an experiment are shown in Fig. 7A, where 35Slabeled TBP, CBP, and cyclin T could efficiently bind to wild-type but not acetylated 42-50 peptide.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a transcription coactivator, a protein involved in positive regulation of transcription via protein-protein interactions with transcription factors and other proteins that positively regulate transcription. Transcription coactivators do not bind DNA directly, but rather mediate protein-protein interactions between activating transcription factors and the basal transcription machinery.\" [GOC:krc]","term_is_obsolete":false,"term_not_annotate":false},{"start":42,"end":54,"reference_id":"11080476","reference_source":"pmid","reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","date":"2024-04-30T17:51:33.266Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0030332","term_name":"cyclin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006077","ec_ontology":"ECO","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0239","term_name":"biotin","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"We decided to address this question by utilizing affinity pull-down experiments using wild-type or acetylated 42-54 peptides coupled to a biotin moiety."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"O60563","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03560r013","statement":[{"text":"The results of such an experiment are shown in Fig. 7A, where 35Slabeled TBP, CBP, and cyclin T could efficiently bind to wild-type but not acetylated 42-50 peptide.","type":"Results"}],"term_comment":"","term_def":"\"Binding to cyclins, proteins whose levels in a cell varies markedly during the cell cycle, rising steadily until mitosis, then falling abruptly to zero. As cyclins reach a threshold level, they are thought to drive cells into G2 phase and thus to mitosis.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":42,"end":54,"reference_id":"11080476","reference_source":"pmid","reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","date":"2024-04-30T18:08:54.144Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0043175","term_name":"RNA polymerase core enzyme binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006077","ec_ontology":"ECO","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0239","term_name":"biotin","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"We decided to address this question by utilizing affinity pull-down experiments using wild-type or acetylated 42-54 peptides coupled to a biotin moiety."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P24928","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03560r014","statement":[{"text":"Results from Western blots indicated that wild-type and not acetylated peptide was capable of binding to core-Pol II.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA polymerase core enzyme, containing a specific subunit composition defined as the core enzyme.\" [GOC:jl, GOC:txnOH]","term_is_obsolete":false,"term_not_annotate":false},{"start":42,"end":54,"reference_id":"11080476","reference_source":"pmid","reference_html":"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. <i> Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F. </i> Virology, 2000","date":"2024-04-30T18:28:00.182Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031491","term_name":"nucleosome binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006077","ec_ontology":"ECO","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0239","term_name":"biotin","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"We decided to address this question by utilizing affinity pull-down experiments using wild-type or acetylated 42-54 peptides coupled to a biotin moiety."}]},{"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","start":50,"end":50,"position":"Specific residue","statements":[{"type":"Figure","text":"The synthesized Tat peptides (42-54) with or without acetylated lysines at positions 50 and 51 were labeled with biotin at the N- terminus."}]},{"term_id":"MOD:02078","term_name":"acetylated residue","term_namespace":"Protein modification","start":51,"end":51,"position":"Specific residue","statements":[{"type":"Figure","text":"The synthesized Tat peptides (42-54) with or without acetylated lysines at positions 50 and 51 were labeled with biotin at the N- terminus."}]}],"ec_go":"IPI","region_id":"DP03560r015","statement":[{"text":"The results of such an experiment are shown in Fig. 7B, where acetylated Tat peptide was able to bind to core histones. It is interesting to note that core histones in the absence of DNA did not bind to acetylated Tat, indicating that a fixed conformation of nucleosome is required for Tat to bind to core histones.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a nucleosome, a complex comprised of DNA wound around a multisubunit core and associated proteins, which forms the primary packing unit of DNA into higher order structures.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"P06899","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q6FI13","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q6NXT2","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P62805","operator":"and","partner_start":null,"partner_end":null}]},{"start":48,"end":57,"reference_id":"9733868","reference_source":"pmid","reference_html":"Interaction of human immunodeficiency virus type 1 Tat with the transcriptional coactivators p300 and CREB binding protein. <i> Hottiger MO, Nabel GJ. </i> J Virol, 1998","date":"2024-05-06T14:40:29.935Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0035035","term_name":"histone acetyltransferase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q09472","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03560r016","statement":[{"text":"Only fusion proteins which contained the Tat basic domain (residues 48 to 57) bound p300, including a fusion protein that expressed only this basic domain region (Fig. ​4A, top).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an histone acetyltransferase.\" [GOC:bf]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":16,"released":"2021_12","sequence":"MEPVDPSLEPWKHPGSQPKTACTNCYCKKCCLHCQVCFTTKGLGISYGRKKRRQRRRPPQDSQTHQVSLPKQPSSQQRGDPTGPKESKKKVERETETDPDN","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"dataset":["Viral proteins","RNA-binding proteins"],"uniref50":"UniRef50_P04608","uniref90":"UniRef90_P20879","uniref100":"UniRef100_P20879","genes":[{"name":{"value":"tat","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04079","url":"https://hamap.expasy.org/unirule/MF_04079"}}]}}],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":101,"type":"D"}],"Structural state":[{"start":1,"end":101,"type":"D"}],"Molecular function":[{"start":1,"end":101,"type":"F"}],"Biological process":[{"start":1,"end":101,"type":"F"}],"Disorder function":[{"start":41,"end":54,"type":"F"}]}},{"disprot_id":"DP03562","acc":"P04613","creator":"vnugnes","date":"2021-11-30T14:51:28.824Z","features":{"pfam":[{"id":"PF00539","name":"Transactivating regulatory protein (Tat)","start":3,"end":63}],"gene3D":[]},"length":87,"name":"Protein Tat","ncbi_taxon_id":11697,"organism":"Human immunodeficiency virus type 1 group M subtype A (isolate MAL)","regions":[{"start":1,"end":87,"reference_id":"10206951","reference_source":"pmid","reference_html":"Full peptide synthesis, purification, and characterization of six Tat variants. Differences observed between HIV-1 isolates from Africa and other continents. <i> Péloponèse JM, Collette Y, Grégoire C, Bailly C, Campèse D, Meurs EF, Olive D, Loret EP. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03562r001","statement":[{"text":"In aqueous buffer (Fig. 4 A), it can be deduced from the intensity of the negative 200 nm band that nonorganized structures are predominant (29). TableI reveals that there is no α helix in aqueous buffer excepted for Tat Mal and Tat Z2, which could have a short helix of eight to nine residues.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-03T08:30:37.353Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":87,"reference_id":"10206951","reference_source":"pmid","reference_html":"Full peptide synthesis, purification, and characterization of six Tat variants. Differences observed between HIV-1 isolates from Africa and other continents. <i> Péloponèse JM, Collette Y, Grégoire C, Bailly C, Campèse D, Meurs EF, Olive D, Loret EP. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0001069","term_name":"regulatory region RNA binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"RNAcentral","id":"URS000071DF2D_576904","partner_start":null,"partner_end":null}],"region_id":"DP03562r002","statement":[{"text":"The K d values vary from approximately 50 nm for both Tat Eli and Tat Mal to about 140 nmfor Tat Oyi and Tat JR.","type":"Figure"},{"text":"The six synthetic Tat proteins can bind to TAR RNA (Fig.3) and can inhibit PKR (data not shown).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-03T08:30:40.959Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a RNA region that regulates a nucleic acid-based process. Such processes include transcription, DNA replication, and DNA repair.\" [GOC:txnOH]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":87,"reference_id":"10206951","reference_source":"pmid","reference_html":"Full peptide synthesis, purification, and characterization of six Tat variants. Differences observed between HIV-1 isolates from Africa and other continents. <i> Péloponèse JM, Collette Y, Grégoire C, Bailly C, Campèse D, Meurs EF, Olive D, Loret EP. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019080","term_name":"viral gene expression","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0005616","ec_ontology":"ECO","ec_name":"beta-galactosidase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03562r003","statement":[{"text":"In each case, Tat was added to the cell buffer, and therefore expression of β-gal up to the control means that the synthetic Tat was able to cross the cytoplasmic and nucleus membranes, bind TAR, and interact with cellular cofactors.","type":"Figure"},{"text":"Tat Mal and Tat Eli show a level of trans-activation three to four times higher to that of Tat Bru.","type":"Figure"},{"text":"The major result of trans-activation tests was the high activity of Tat Mal and Tat Eli, which correlates with the high virulence of these two HIV-1 isolates.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-03T08:34:47.216Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A process by which a viral gene is converted into a mature gene product or products (proteins or RNA). This includes viral transcription, processing to produce a mature RNA product, and viral translation.\" [GOC:bf, GOC:jl, ISBN:0121585336]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":87,"reference_id":"10206951","reference_source":"pmid","reference_html":"Full peptide synthesis, purification, and characterization of six Tat variants. Differences observed between HIV-1 isolates from Africa and other continents. <i> Péloponèse JM, Collette Y, Grégoire C, Bailly C, Campèse D, Meurs EF, Olive D, Loret EP. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019080","term_name":"viral gene expression","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0005648","ec_ontology":"ECO","ec_name":"luciferase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03562r004","statement":[{"text":"Similar results were obtained with another transfection assay using luciferase as gene reporter, and Tat Mal and Tat Eli at 1 μm did trans-activate the LTR to a level comparable with that obtained with a transfected pCMV-Tat (data not shown).","type":"Figure"},{"text":"The major result of trans-activation tests was the high activity of Tat Mal and Tat Eli, which correlates with the high virulence of these two HIV-1 isolates.","type":"Results"},{"text":"At 10 μm, the six Tat were showing levels of trans-activation so high that it was impossible to see differences between them because there was saturation.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-03T08:34:37.229Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A process by which a viral gene is converted into a mature gene product or products (proteins or RNA). This includes viral transcription, processing to produce a mature RNA product, and viral translation.\" [GOC:bf, GOC:jl, ISBN:0121585336]","disprot_namespace":"Disorder function","term_is_binding":false}],"regions_counter":4,"released":"2021_12","sequence":"MDPVDPNLEPWNHPGSQPRTPCNKCYCKKCCYHCQMCFITKGLGISYGRKKRRQRRRPPQGNQAHQDPLPEQPSSQHRGDHPTGPKE","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"dataset":["Viral proteins","RNA-binding proteins"],"uniref50":"UniRef50_P04613","uniref90":"UniRef90_P04613","uniref100":"UniRef100_P04613","genes":[{"name":{"value":"tat","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04079","url":"https://hamap.expasy.org/unirule/MF_04079"}}]}}],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":87,"type":"D"}],"Structural state":[{"start":1,"end":87,"type":"D"}],"Molecular function":[{"start":1,"end":87,"type":"F"}],"Biological process":[{"start":1,"end":87,"type":"F"}]}},{"disprot_id":"DP03563","acc":"P04611","creator":"vnugnes","date":"2021-11-30T15:01:01.938Z","features":{"pfam":[{"id":"PF00539","name":"Transactivating regulatory protein (Tat)","start":3,"end":62}],"gene3D":[]},"length":99,"name":"Protein Tat","ncbi_taxon_id":11689,"organism":"Human immunodeficiency virus type 1 group M subtype D (isolate ELI)","regions":[{"start":1,"end":99,"reference_id":"10206951","reference_source":"pmid","reference_html":"Full peptide synthesis, purification, and characterization of six Tat variants. Differences observed between HIV-1 isolates from Africa and other continents. <i> Péloponèse JM, Collette Y, Grégoire C, Bailly C, Campèse D, Meurs EF, Olive D, Loret EP. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03563r001","statement":[{"text":"In aqueous buffer (Fig. 4 A), it can be deduced from the intensity of the negative 200 nm band that nonorganized structures are predominant (29)","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:44:37.967Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":99,"reference_id":"10206951","reference_source":"pmid","reference_html":"Full peptide synthesis, purification, and characterization of six Tat variants. Differences observed between HIV-1 isolates from Africa and other continents. <i> Péloponèse JM, Collette Y, Grégoire C, Bailly C, Campèse D, Meurs EF, Olive D, Loret EP. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0001069","term_name":"regulatory region RNA binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"RNAcentral","id":"URS000071DF2D_576904","partner_start":null,"partner_end":null}],"region_id":"DP03563r002","statement":[{"text":"The K d values vary from approximately 50 nm for both Tat Eli and Tat Mal to about 140 nmfor Tat Oyi and Tat JR. ","type":"Figure"},{"text":"The six synthetic Tat proteins can bind to TAR RNA (Fig.3) and can inhibit PKR (data not shown).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:44:47.483Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a RNA region that regulates a nucleic acid-based process. Such processes include transcription, DNA replication, and DNA repair.\" [GOC:txnOH]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":99,"reference_id":"10206951","reference_source":"pmid","reference_html":"Full peptide synthesis, purification, and characterization of six Tat variants. Differences observed between HIV-1 isolates from Africa and other continents. <i> Péloponèse JM, Collette Y, Grégoire C, Bailly C, Campèse D, Meurs EF, Olive D, Loret EP. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019080","term_name":"viral gene expression","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0006241","ec_ontology":"ECO","ec_name":"galactokinase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03563r003","statement":[{"text":"In each case, Tat was added to the cell buffer, and therefore expression of β-gal up to the control means that the synthetic Tat was able to cross the cytoplasmic and nucleus membranes, bind TAR, and interact with cellular cofactors.","type":"Figure"},{"text":"Tat Mal and Tat Eli show a level of trans-activation three to four times higher to that of Tat Bru.","type":"Figure"},{"text":"The major result of trans-activation tests was the high activity of Tat Mal and Tat Eli, which correlates with the high virulence of these two HIV-1 isolates. Interestingly, the long C-terminal extremity of Tat Eli seems to improve the trans-activation compared with Tat Mal (Fig. 5).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:44:58.123Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A process by which a viral gene is converted into a mature gene product or products (proteins or RNA). This includes viral transcription, processing to produce a mature RNA product, and viral translation.\" [GOC:bf, GOC:jl, ISBN:0121585336]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":99,"reference_id":"10206951","reference_source":"pmid","reference_html":"Full peptide synthesis, purification, and characterization of six Tat variants. Differences observed between HIV-1 isolates from Africa and other continents. <i> Péloponèse JM, Collette Y, Grégoire C, Bailly C, Campèse D, Meurs EF, Olive D, Loret EP. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019080","term_name":"viral gene expression","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0005648","ec_ontology":"ECO","ec_name":"luciferase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03563r004","statement":[{"text":"Similar results were obtained with another transfection assay using luciferase as gene reporter, and Tat Mal and Tat Eli at 1 μm did trans-activate the LTR to a level comparable with that obtained with a transfected pCMV-Tat (data not shown).","type":"Figure"},{"text":"The major result of trans-activation tests was the high activity of Tat Mal and Tat Eli, which correlates with the high virulence of these two HIV-1 isolates. Interestingly, the long C-terminal extremity of Tat Eli seems to improve the trans-activation compared with Tat Mal (Fig. 5).","type":"Results"},{"text":"At 0.2 μm, only Tat Eli was showing a level of trans-activation significantly higher than the base level. At 10 μm, the six Tat were showing levels of trans-activation so high that it was impossible to see differences between them because there was saturation.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:44:53.329Z"},"ec_go":"IEP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A process by which a viral gene is converted into a mature gene product or products (proteins or RNA). This includes viral transcription, processing to produce a mature RNA product, and viral translation.\" [GOC:bf, GOC:jl, ISBN:0121585336]","disprot_namespace":"Disorder function","term_is_binding":false}],"regions_counter":4,"released":"2021_12","sequence":"MDPVDPNLEPWNHPGSQPRTPCNKCHCKKCCYHCPVCFLNKGLGISYGRKKRRQRRGPPQGGQAHQVPIPKQPSSQPRGDPTGPKEQKKKVESEAETDP","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"dataset":["Viral proteins","RNA-binding proteins"],"uniref50":"UniRef50_P0C1J9","uniref90":"UniRef90_P04611","uniref100":"UniRef100_P04611","genes":[{"name":{"value":"tat","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04079","url":"https://hamap.expasy.org/unirule/MF_04079"}}]}}],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":99,"type":"D"}],"Structural state":[{"start":1,"end":99,"type":"D"}],"Molecular function":[{"start":1,"end":99,"type":"F"}],"Biological process":[{"start":1,"end":99,"type":"F"}]}},{"disprot_id":"DP03565","acc":"P20893","creator":"vnugnes","date":"2021-11-30T15:56:59.136Z","features":{"pfam":[{"id":"PF00539","name":"Transactivating regulatory protein (Tat)","start":2,"end":64}],"gene3D":[]},"length":101,"name":"Protein Tat","ncbi_taxon_id":11699,"organism":"Human immunodeficiency virus type 1 group M subtype B (isolate OYI)","regions":[{"start":1,"end":101,"reference_id":"10206951","reference_source":"pmid","reference_html":"Full peptide synthesis, purification, and characterization of six Tat variants. Differences observed between HIV-1 isolates from Africa and other continents. <i> Péloponèse JM, Collette Y, Grégoire C, Bailly C, Campèse D, Meurs EF, Olive D, Loret EP. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03565r001","statement":[{"text":"In aqueous buffer (Fig. 4 A), it can be deduced from the intensity of the negative 200 nm band that nonorganized structures are predominant (29).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:40:02.097Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1,"end":101,"reference_id":"10206951","reference_source":"pmid","reference_html":"Full peptide synthesis, purification, and characterization of six Tat variants. Differences observed between HIV-1 isolates from Africa and other continents. <i> Péloponèse JM, Collette Y, Grégoire C, Bailly C, Campèse D, Meurs EF, Olive D, Loret EP. </i> J Biol Chem, 1999","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0001069","term_name":"regulatory region RNA binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"RNAcentral","id":"URS000071DF2D_576904","partner_start":null,"partner_end":null}],"region_id":"DP03565r002","statement":[{"text":"The K d values vary from approximately 50 nm for both Tat Eli and Tat Mal to about 140 nmfor Tat Oyi and Tat JR.","type":"Figure"},{"text":"The six synthetic Tat proteins can bind to TAR RNA (Fig.3) and can inhibit PKR (data not shown).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:40:09.362Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a RNA region that regulates a nucleic acid-based process. Such processes include transcription, DNA replication, and DNA repair.\" [GOC:txnOH]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":2,"released":"2021_12","sequence":"MEPVDPRLEPWKHPGSQPKTASNNCYCKRCCLHCQVCFTKKGLGISYGRKKRRQRRRAPQDSKTHQVSLSKQPASQPRGDPTGPKESKKKVERETETDPED","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"dataset":["Viral proteins","RNA-binding proteins"],"uniref50":"UniRef50_P04608","uniref90":"UniRef90_P20893","uniref100":"UniRef100_P20893","genes":[{"name":{"value":"tat","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04079","url":"https://hamap.expasy.org/unirule/MF_04079"}}]}}],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":101,"type":"D"}],"Structural state":[{"start":1,"end":101,"type":"D"}],"Molecular function":[{"start":1,"end":101,"type":"F"}]}},{"disprot_id":"DP03566","acc":"P22363","creator":"jbergier","date":"2021-12-01T15:23:39.357Z","features":{"pfam":[{"id":"PF03012","name":"Phosphoprotein","start":1,"end":296}],"gene3D":[]},"length":297,"name":"Phosphoprotein","ncbi_taxon_id":11294,"organism":"Rabies virus (strain CVS-11)","regions":[{"start":1,"end":172,"reference_id":"15476803","reference_source":"pmid","reference_html":"Structure and function of the C-terminal domain of the polymerase cofactor of rabies virus. <i> Mavrakis M, McCarthy AA, Roche S, Blondel D, Ruigrok RW. </i> J Mol Biol, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0001191","ec_ontology":"ECO","ec_name":"in vitro cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03566r001","statement":[{"text":"The domain structure of this recombinant protein was probed by limited protease digestion using trypsin, endoprotease Lys-C and thermolysin. These proteases digest P to protease-resistant fragments that migrate on SDS-PAGE with apparent molecular masses of 15–16 kDa (Figure 3 A–C).","type":"Results"},{"text":"N-terminal sequencing of the fragment obtained after trypsin digestion showed that cleavage had occurred after R172. The apparent mass of the fragment from SDS-PAGE suggests that it contains residues 173–297.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-03T08:19:51.308Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":1,"end":172,"reference_id":"10590095","reference_source":"pmid","reference_html":"The phosphoprotein of rabies virus is phosphorylated by a unique cellular protein kinase and specific isomers of protein kinase C. <i> Gupta AK, Blondel D, Choudhary S, Banerjee AK. </i> J Virol, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0007688","ec_ontology":"ECO","ec_name":"gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":162,"end":162,"position":"Specific residue"}],"region_id":"DP03566r002","sequence_construct":"MSKIFVNPSAIRAGLADLEMAEETVDLINRNIEDNQAHLQGEPIEVDNLPEDMKRLHLDDEKSSNLGEMVRVGEGKYREDFQMDEGEDPNLLFQSYLDNVGVQIVRQMRSGERFLKIWSQTVEEIVSYVTVNFPNPPRRSSEDKSTQTTGRELKKETTSAFSQRESQPSKARMVAQVAPGPPALEWSATNEEDDLSVEAEIAHQIAESFSKKYKFPSRSSGIFLYNFEQLKMNLDDIVKEAKNVPGVTRLAHDGSKIPLRCVLGWVALANSKKFQLLVEADKLSKIMQDDLNRYTSC","statement":[{"text":"We carried out systematic site-directed mutagenesis at those sites, altering S or T to A, expressed the mutant proteins in E. coli, and then purified and tested them for phosphorylation by RVPK and PKC. As shown in Fig. 6, altering S162 and S210 to A resulted in a drastic reduction in the ability of PKC to phosphorylate P protein (95%), whereas phosphorylation by RVPK was reduced by only 25%. These results suggest that PKC phosphorylation sites are probably S162, S210, and S271, which are presumably different from the RVPK sites which may be located at a different domain in the P protein.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-03T08:19:48.261Z"},"ec_go":"IDA","disprot_namespace":"Disorder function"},{"start":132,"end":150,"reference_id":"28680096","reference_source":"pmid","reference_html":"Negri bodies are viral factories with properties of liquid organelles. <i> Nikolic J, Le Bars R, Lama Z, Scrima N, Lagaudrière-Gesbert C, Gaudin Y, Blondel D. </i> Nat Commun, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005601","ec_ontology":"ECO","ec_name":"immunofluorescence confocal microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03566r003","statement":[{"text":"Finally, we delineated more precisely the part of IDD2 domain which is required for phase separation. Deletion of residues 151–181 did not affect P ability to form NB-like structures (Fig. 6e). Therefore, only the amino-terminal part of IDD2 (residues 132–150) is required for this process. This was confirmed by the deletion of residues 139–151, which abolished spherical inclusions formation (Fig. 6e).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-03T08:19:49.455Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","disprot_namespace":"Disorder function","term_is_binding":true}],"regions_counter":3,"released":"2021_12","sequence":"MSKIFVNPSAIRAGLADLEMAEETVDLINRNIEDNQAHLQGEPIEVDNLPEDMKRLHLDDEKSSNLGEMVRVGEGKYREDFQMDEGEDPNLLFQSYLDNVGVQIVRQMRSGERFLKIWSQTVEEIVSYVTVNFPNPPRRSSEDKSTQTTGRELKKETTSAFSQRESQPSKARMVAQVAPGPPALEWSATNEEDDLSVEAEIAHQIAESFSKKYKFPSRSSGIFLYNFEQLKMNLDDIVKEAKNVPGVTRLAHDGSKIPLRCVLGWVALANSKKFQLLVEADKLSKIMQDDLNRYTSC","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Rhabdoviridae","Alpharhabdovirinae","Lyssavirus"],"dataset":["Viral proteins","Neglected tropical diseases proteins","Condensates-related proteins"],"uniref50":"UniRef50_P22363","uniref90":"UniRef90_P22363","uniref100":"UniRef100_P22363","genes":[{"name":{"value":"P"}}],"disorder_content":0.5791245791245792,"disprot_consensus":{"full":[{"start":1,"end":172,"type":"D"}],"Structural state":[{"start":1,"end":172,"type":"D"}],"Disorder function":[{"start":1,"end":172,"type":"F"}],"Molecular function":[{"start":132,"end":150,"type":"F"}]}},{"disprot_id":"DP03567","acc":"P0DOF3","creator":"jbergier","date":"2021-12-02T10:13:48.907Z","features":{"pfam":[{"id":"PF00945","name":"Rhabdovirus nucleocapsid protein","start":11,"end":428}],"gene3D":[]},"length":450,"name":"Nucleoprotein","ncbi_taxon_id":11295,"organism":"Rabies virus (strain ERA)","regions":[{"start":376,"end":397,"reference_id":"16778023","reference_source":"pmid","reference_html":"Crystal structure of the rabies virus nucleoprotein-RNA complex. <i> Albertini AA, Wernimont AK, Muziol T, Ravelli RB, Clapier CR, Schoehn G, Weissenhorn W, Ruigrok RW. </i> Science, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2GTT"}],"region_id":"DP03567r001","statement":[{"text":"Two regions in N (NTD: 105 to 118 and CTD: 376 to 397) are presumably flexible, because they are absent in the structure (Fig. 1C and fig. S1).","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-03T08:24:34.113Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":105,"end":118,"reference_id":"16778023","reference_source":"pmid","reference_html":"Crystal structure of the rabies virus nucleoprotein-RNA complex. <i> Albertini AA, Wernimont AK, Muziol T, Ravelli RB, Clapier CR, Schoehn G, Weissenhorn W, Ruigrok RW. </i> Science, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2GTT"}],"region_id":"DP03567r002","statement":[{"text":"Two regions in N (NTD: 105 to 118 and CTD: 376 to 397) are presumably flexible, because they are absent in the structure (Fig. 1C and fig. S1).","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-03T08:24:33.521Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2021_12","sequence":"MDADKIVFKVNNQVVSLKPEIIVDQHEYKYPAIKDLKKPCITLGKAPDLNKAYKSVLSGMSAAKLDPDDVCSYLAAAMQFFEGTCPEDWTSYGIVIARKGDKITPGSLVEIKRTDVEGNWALTGGMELTRDPTVPEHASLVGLLLSLYRLSKISGQNTGNYKTNIADRIEQIFETAPFVKIVEHHTLMTTHKMCANWSTIPNFRFLAGTYDMFFSRIEHLYSAIRVGTVVTAYEDCSGLVSFTGFIKQINLTAREAILYFFHKNFEEEIRRMFEPGQETAVPHSYFIHFRSLGLSGKSPYSSNAVGHVFNLIHFVGCYMGQVRSLNATVIAACAPHEMSVLGGYLGEEFFGKGTFERRFFRDEKELQEYEAAELTKTDVALADDGTVNSDDEDYFSGETRSPEAVYTRIMMNGGRLKRSHIRRYVSVSSNHQARPNSFAEFLNKTYSSDS","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Rhabdoviridae","Alpharhabdovirinae","Lyssavirus"],"dataset":["Viral proteins","Neglected tropical diseases proteins","RNA-binding proteins"],"uniref50":"UniRef50_P16285","uniref90":"UniRef90_P16285","uniref100":"UniRef100_P0DOF3","genes":[{"name":{"value":"N"}}],"disorder_content":0.08,"disprot_consensus":{"full":[{"start":105,"end":118,"type":"D"},{"start":376,"end":397,"type":"D"}],"Structural state":[{"start":105,"end":118,"type":"D"},{"start":376,"end":397,"type":"D"}]}},{"disprot_id":"DP03568","acc":"Q8JXF6","creator":"jbergier","date":"2021-12-02T10:15:52.141Z","features":{"pfam":[{"id":"PF00945","name":"Rhabdovirus nucleocapsid protein","start":11,"end":428}],"gene3D":[]},"length":450,"name":"Nucleoprotein","ncbi_taxon_id":11294,"organism":"Rabies virus (strain CVS-11)","regions":[{"start":376,"end":397,"reference_id":"16778023","reference_source":"pmid","reference_html":"Crystal structure of the rabies virus nucleoprotein-RNA complex. <i> Albertini AA, Wernimont AK, Muziol T, Ravelli RB, Clapier CR, Schoehn G, Weissenhorn W, Ruigrok RW. </i> Science, 2006","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2GTT"}],"region_id":"DP03568r001","statement":[{"text":"Two regions in N (NTD: 105 to 118 and CTD: 376 to 397) are presumably flexible, because they are absent in the structure (Fig. 1C and fig. S1).","type":"Article"},{"text":"This IDR is 100% identical to the Rabies virus (strain ERA).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-03T08:24:30.833Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MDADKIVFKVNNQVVSLKPEIIVDQYEYKYPAIKDLKKPCITLGKAPDLNKAYKSVLSGMNAAKLDPDDVCSYLAAAMQFFEGTCPEDWTSYGILIARKGDRITPNSLVEIKRTDVDGNWALTGGMELTRDPTVSEHASLVGLLLSLYRLSKISGQNTGNYKTNIADRIEQIFETAPFVKIVEHHTLMTTHKMCANWSTIPNFRFLAGTYDMFFSRIEHLYSAIRVGTVVTAYEDCSGLVSFTGFIKQINLTAREAILYFFHKNFEEEIRRMFEPGQETAVPHSYFIHFRSLGLSGKSPYSSNAVGHVFNLIHFVGCYMGQVRSLNATVIAACAPHEMSVLGGYLGEEFFGKGTFERRFFRDEKELQEYEAAELTKTDVALADDGTVNSDDEDYFSGETRSPEAVYTRIMMNGGRLKRSHIRRYVSVSSNHQARPNSFAEFLNKTYSNDS","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Rhabdoviridae","Alpharhabdovirinae","Lyssavirus"],"dataset":["Viral proteins","Neglected tropical diseases proteins","Condensates-related proteins","RNA-binding proteins"],"uniref50":"UniRef50_P16285","uniref90":"UniRef90_P16285","uniref100":"UniRef100_Q8JXF6","genes":[{"name":{"value":"N"}}],"disorder_content":0.04888888888888889,"disprot_consensus":{"full":[{"start":376,"end":397,"type":"D"}],"Structural state":[{"start":376,"end":397,"type":"D"}]}},{"disprot_id":"DP03569","acc":"F0TTD6","creator":"ewagner","date":"2021-12-02T12:56:54.758Z","features":{"pfam":[{"id":"PF00598","name":"Influenza Matrix protein (M1)","start":2,"end":157},{"id":"PF08289","name":"Influenza Matrix protein (M1) C-terminal domain","start":158,"end":252}],"gene3D":[]},"length":252,"name":"Matrix protein 1","ncbi_taxon_id":760066,"organism":"Influenza A virus","regions":[{"start":159,"end":252,"reference_id":"32908308","reference_source":"pmid","reference_html":"The native structure of the assembled matrix protein 1 of influenza A virus. <i> Peukes J, Xiong X, Erlendsson S, Qu K, Wan W, Calder LJ, Schraidt O, Kummer S, Freund SMV, Kräusslich HG, Briggs JAG. </i> Nature, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03569r001","statement":[{"text":"The NTD adopts the same nine-helix fold as present in previously determined crystal structures 12–14. The CTD, in contrast, is largely disordered, consistent with previous observations 24 and does not adopt detectable tertiary structure when pH is increased (Extended Data Fig. 4c).","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:29:30.575Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":159,"end":252,"reference_id":"32908308","reference_source":"pmid","reference_html":"The native structure of the assembled matrix protein 1 of influenza A virus. <i> Peukes J, Xiong X, Erlendsson S, Qu K, Wan W, Calder LJ, Schraidt O, Kummer S, Freund SMV, Kräusslich HG, Briggs JAG. </i> Nature, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"6Z5J"}],"region_id":"DP03569r002","statement":[{"text":"The PDB shows missing residues for this region.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:29:20.660Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":187,"end":217,"reference_id":"32908308","reference_source":"pmid","reference_html":"The native structure of the assembled matrix protein 1 of influenza A virus. <i> Peukes J, Xiong X, Erlendsson S, Qu K, Wan W, Calder LJ, Schraidt O, Kummer S, Freund SMV, Kräusslich HG, Briggs JAG. </i> Nature, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"6Z5J"}],"interaction_partner":[{"db":"UniProt","id":"F0TTD6","partner_start":8,"partner_end":30}],"region_id":"DP03569r003","statement":[{"text":"The NTD-CTD interface appears to be stabilized by charge complementarity between the negatively charged membrane-distal surface of the NTD (residues Glu-8, Glu-23, Glu-29, Asp-30), and the positively charged interacting surface of the CTD (residues Lys-187, Arg-210, Arg-217), as well as by an inter-molecular salt bridge between Lys-21 and Glu-176 (Fig. 3c).","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:29:33.368Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":159,"end":252,"reference_id":"32908308","reference_source":"pmid","reference_html":"The native structure of the assembled matrix protein 1 of influenza A virus. <i> Peukes J, Xiong X, Erlendsson S, Qu K, Wan W, Calder LJ, Schraidt O, Kummer S, Freund SMV, Kräusslich HG, Briggs JAG. </i> Nature, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"6Z5L"},{"db":"PDB","id":"6Z5J"}],"region_id":"DP03569r004","statement":[{"text":"Polymerization is associated with extension of helix 9 and transition of the CTD from an unfolded to folded state, upon which it interacts with the NTD of the neighboring M1 molecule in the strand.","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:28:57.246Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":159,"end":252,"reference_id":"32908308","reference_source":"pmid","reference_html":"The native structure of the assembled matrix protein 1 of influenza A virus. <i> Peukes J, Xiong X, Erlendsson S, Qu K, Wan W, Calder LJ, Schraidt O, Kummer S, Freund SMV, Kräusslich HG, Briggs JAG. </i> Nature, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"6Z5L"},{"db":"PDB","id":"6Z5J"}],"region_id":"DP03569r005","statement":[{"text":"Polymerization is associated with extension of helix 9 and transition of the CTD from an unfolded to folded state, upon which it interacts with the NTD of the neighboring M1 molecule in the strand.","type":"Article"}],"states_connection":[{"source":"DP03569r002","target":"DP03569r004"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:29:32.023Z"},"ec_go":"IDA","disprot_namespace":"Structural transition"},{"start":159,"end":252,"reference_id":"32908308","reference_source":"pmid","reference_html":"The native structure of the assembled matrix protein 1 of influenza A virus. <i> Peukes J, Xiong X, Erlendsson S, Qu K, Wan W, Calder LJ, Schraidt O, Kummer S, Freund SMV, Kräusslich HG, Briggs JAG. </i> Nature, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"GO:0019068","term_name":"virion assembly","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"6Z5L"},{"db":"PDB","id":"6Z5J"}],"region_id":"DP03569r006","statement":[{"text":" The NTD-CTD interface appears to be stabilized by charge complementarity between the negatively charged membrane-distal surface of the NTD (residues Glu-8, Glu-23, Glu-29, Asp-30), and the positively charged interacting surface of the CTD (residues Lys-187, Arg-210, Arg-217), as well as by an inter-molecular salt bridge between Lys-21 and Glu-176 (Fig. 3c).","type":"Article"},{"text":"This arrangement implies that virus assembly will be processive – binding of M1 into the filament induces conformational changes that create new interfaces promoting binding of the next monomer.","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:29:38.937Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"A late phase of the viral life cycle during which all the components necessary for the formation of a mature virion collect at a particular site in the cell and the basic structure of the virus particle is formed.\" [ISBN:0121585336]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":159,"end":252,"reference_id":"32908308","reference_source":"pmid","reference_html":"The native structure of the assembled matrix protein 1 of influenza A virus. <i> Peukes J, Xiong X, Erlendsson S, Qu K, Wan W, Calder LJ, Schraidt O, Kummer S, Freund SMV, Kräusslich HG, Briggs JAG. </i> Nature, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"6Z5L"},{"db":"PDB","id":"6Z5J"}],"region_id":"DP03569r007","statement":[{"text":" The NTD-CTD interface appears to be stabilized by charge complementarity between the negatively charged membrane-distal surface of the NTD (residues Glu-8, Glu-23, Glu-29, Asp-30), and the positively charged interacting surface of the CTD (residues Lys-187, Arg-210, Arg-217), as well as by an inter-molecular salt bridge between Lys-21 and Glu-176 (Fig. 3c).","type":"Article"},{"text":"This arrangement implies that virus assembly will be processive – binding of M1 into the filament induces conformational changes that create new interfaces promoting binding of the next monomer.","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-02T14:29:36.637Z"},"ec_go":"IDA","disprot_namespace":"Disorder function"}],"regions_counter":11,"released":"2021_12","sequence":"MSLLTEVETYVLSIIPSGPLKAEIAQRLEDVFAGKNTDLEVLMEWLKTRPILSPLTKGILGFVFTLTVPSERGLQRRRFVQNALNGNGDPNNMDKAVKLYRKLKREITFHGAKEISLSYSAGALASCMGLIYNRMGAVTTEVAFGLVCATCEQIADSQHRSHRQMVTTTNPLIRHENRMVLASTTAKAMEQMAGSSEQAAEAMEVASQARQMVQAMRTIGTHPSSSAGLKNDLLENLQAYQKRMGVQMQRFK","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Polyploviricotina","Insthoviricetes","Articulavirales","Orthomyxoviridae","Alphainfluenzavirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_P05777","uniref90":"UniRef90_P05777","uniref100":"UniRef100_B4URD8","genes":[{"name":{"value":"M1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ADX99604.1","url":"https://www.ebi.ac.uk/ena/browser/view/ADX99604.1"}}]},"synonyms":[{"value":"M","evidences":[{"code":"ECO:0000256","source":{"name":"HAMAP-Rule","id":"MF_04068","url":"https://hamap.expasy.org/unirule/MF_04068"}},{"code":"ECO:0000256","source":{"name":"RuleBase","id":"RU362105","url":"https://www.uniprot.org/unirule/RU362105"}}]}]}],"disorder_content":0.373015873015873,"disprot_consensus":{"full":[{"start":159,"end":252,"type":"T"}],"Structural state":[{"start":159,"end":252,"type":"D"}],"Molecular function":[{"start":187,"end":217,"type":"F"}],"Structural transition":[{"start":159,"end":252,"type":"T"}],"Biological process":[{"start":159,"end":252,"type":"F"}],"Disorder function":[{"start":159,"end":252,"type":"F"}]}},{"disprot_id":"DP03571","acc":"P03433","creator":"gbalatti","date":"2021-12-03T11:08:00.151Z","features":{"pfam":[{"id":"PF00603","name":"Influenza RNA-dependent RNA polymerase subunit PA","start":21,"end":714}],"gene3D":[]},"length":716,"name":"Polymerase acidic protein","ncbi_taxon_id":211044,"organism":"Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)","regions":[{"start":372,"end":397,"reference_id":"18660801","reference_source":"pmid","reference_html":"The structural basis for an essential subunit interaction in influenza virus RNA polymerase. <i> Obayashi E, Yoshida H, Kawai F, Shibayama N, Kawaguchi A, Nagata K, Tame JR, Park SY. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"cross_refs":[{"db":"PDB","id":"2ZNL"}],"region_id":"DP03571r001","statement":[{"text":"Eighteen residues at the N terminus and a loop (residues 372–397)\nbetween a3 and a4 are disordered, giving a total of 423 residues of PA\nin the final model, beginning with Ile 257.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-06T11:02:01.047Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_06","sequence":"MEDFVRQCFNPMIVELAEKTMKEYGEDLKIETNKFAAICTHLEVCFMYSDFHFINEQGESIIVELGDPNALLKHRFEIIEGRDRTMAWTVVNSICNTTGAEKPKFLPDLYDYKENRFIEIGVTRREVHIYYLEKANKIKSEKTHIHIFSFTGEEMATKADYTLDEESRARIKTRLFTIRQEMASRGLWDSFRQSERGEETIEERFEITGTMRKLADQSLPPNFSSLENFRAYVDGFEPNGYIEGKLSQMSKEVNARIEPFLKTTPRPLRLPNGPPCSQRSKFLLMDALKLSIEDPSHEGEGIPLYDAIKCMRTFFGWKEPNVVKPHEKGINPNYLLSWKQVLAELQDIENEEKIPKTKNMKKTSQLKWALGENMAPEKVDFDDCKDVGDLKQYDSDEPELRSLASWIQNEFNKACELTDSSWIELDEIGEDVAPIEHIASMRRNYFTSEVSHCRATEYIMKGVYINTALLNASCAAMDDFQLIPMISKCRTKEGRRKTNLYGFIIKGRSHLRNDTDVVNFVSMEFSLTDPRLEPHKWEKYCVLEIGDMLIRSAIGQVSRPMFLYVRTNGTSKIKMKWGMEMRRCLLQSLQQIESMIEAESSVKEKDMTKEFFENKSETWPIGESPKGVEESSIGKVCRTLLAKSVFNSLYASPQLEGFSAESRKLLLIVQALRDNLEPGTFDLGGLYEAIEECLINDPWVLLNASWFNSFLTHALS","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Polyploviricotina","Insthoviricetes","Articulavirales","Orthomyxoviridae","Alphainfluenzavirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_P03433","uniref90":"UniRef90_P03433","uniref100":"UniRef100_P03433","genes":[{"name":{"value":"PA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04063","url":"https://hamap.expasy.org/unirule/MF_04063"}}]}}],"disorder_content":0.036312849162011177,"disprot_consensus":{"full":[{"start":372,"end":397,"type":"D"}],"Structural state":[{"start":372,"end":397,"type":"D"}]}},{"disprot_id":"DP03572","acc":"P03431","creator":"gbalatti","date":"2021-12-03T11:23:29.873Z","features":{"pfam":[{"id":"PF00602","name":"Influenza RNA-dependent RNA polymerase subunit PB1","start":1,"end":741}],"gene3D":[]},"length":757,"name":"RNA-directed RNA polymerase catalytic subunit","ncbi_taxon_id":211044,"organism":"Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)","regions":[{"start":16,"end":81,"reference_id":"18660801","reference_source":"pmid","reference_html":"The structural basis for an essential subunit interaction in influenza virus RNA polymerase. <i> Obayashi E, Yoshida H, Kawai F, Shibayama N, Kawaguchi A, Nagata K, Tame JR, Park SY. </i> Nature, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"2ZNL"}],"region_id":"DP03572r001","statement":[{"text":"Mass spectrometry confirmed that all 81 residues of the PB1-derived peptide are\npresent in the crystal, but most are invisible in the electron density.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-07T08:09:40.246Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2021_12","sequence":"MDVNPTLLFLKVPAQNAISTTFPYTGDPPYSHGTGTGYTMDTVNRTHQYSEKGRWTTNTETGAPQLNPIDGPLPEDNEPSGYAQTDCVLEAMAFLEESHPGIFENSCIETMEVVQQTRVDKLTQGRQTYDWTLNRNQPAATALANTIEVFRSNGLTANESGRLIDFLKDVMESMKKEEMGITTHFQRKRRVRDNMTKKMITQRTIGKKKQRLNKRSYLIRALTLNTMTKDAERGKLKRRAIATPGMQIRGFVYFVETLARSICEKLEQSGLPVGGNEKKAKLANVVRKMMTNSQDTELSFTITGDNTKWNENQNPRMFLAMITYMTRNQPEWFRNVLSIAPIMFSNKMARLGKGYMFESKSMKLRTQIPAEMLASIDLKYFNDSTRKKIEKIRPLLIEGTASLSPGMMMGMFNMLSTVLGVSILNLGQKRYTKTTYWWDGLQSSDDFALIVNAPNHEGIQAGVDRFYRTCKLLGINMSKKKSYINRTGTFEFTSFFYRYGFVANFSMELPSFGVSGINESADMSIGVTVIKNNMINNDLGPATAQMALQLFIKDYRYTYRCHRGDTQIQTRRSFEIKKLWEQTRSKAGLLVSDGGPNLYNIRNLHIPEVCLKWELMDEDYQGRLCNPLNPFVSHKEIESMNNAVMMPAHGPAKNMEYDAVATTHSWIPKRNRSILNTSQRGVLEDEQMYQRCCNLFEKFFPSSSYRRPVGISSMVEAMVSRARIDARIDFESGRIKKEEFTEIMKICSTIEELRRQK","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Polyploviricotina","Insthoviricetes","Articulavirales","Orthomyxoviridae","Alphainfluenzavirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_P03431","uniref90":"UniRef90_P03431","uniref100":"UniRef100_P03431","genes":[{"name":{"value":"PB1","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04065","url":"https://hamap.expasy.org/unirule/MF_04065"}}]}}],"disorder_content":0.08718626155878467,"disprot_consensus":{"full":[{"start":16,"end":81,"type":"D"}],"Structural state":[{"start":16,"end":81,"type":"D"}]}},{"disprot_id":"DP03575","acc":"P03496","creator":"fquaglia","date":"2021-12-03T13:30:56.578Z","features":{"pfam":[{"id":"PF00600","name":"Influenza non-structural protein (NS1)","start":1,"end":217}],"gene3D":[]},"length":230,"name":"Non-structural protein 1","ncbi_taxon_id":211044,"organism":"Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)","regions":[{"start":204,"end":230,"reference_id":"21464929","reference_source":"pmid","reference_html":"A transient homotypic interaction model for the influenza A virus NS1 protein effector domain. <i> Kerry PS, Ayllon J, Taylor MA, Hass C, Lewis A, García-Sastre A, Randall RE, Hale BG, Russell RJ. </i> PLoS One, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3O9R"},{"db":"PDB","id":"3O9Q"},{"db":"PDB","id":"3O9S"},{"db":"PDB","id":"3O9U"},{"db":"PDB","id":"3O9T"}],"region_id":"DP03575r001","statement":[{"text":"The N-terminal 73 amino-acid residues of NS1 form a symmetrical homodimeric RNA-binding domain (RBD) [23], [24], [25], [26], which is connected to the central effector domain (ED; residues 86-204) via an inter-domain linker [27]. The final ~25 residues of NS1 appear to be unstructured, and are termed the C-terminal flexible ‘tail’ (FT) ( Fig. 1A ) [28].","type":"Introduction"},{"text":"Neither the inter-domain linker nor the flexible ‘tail’ have been observed in crystal structures, and are therefore represented schematically.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-06T11:51:28.550Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":73,"end":82,"reference_id":"20133840","reference_source":"pmid","reference_html":"Structural insights into phosphoinositide 3-kinase activation by the influenza A virus NS1 protein. <i> Hale BG, Kerry PS, Jackson D, Precious BL, Gray A, Killip MJ, Randall RE, Russell RJ. </i> Proc Natl Acad Sci U S A, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"3L4Q"}],"region_id":"DP03575r002","statement":[{"text":"Flexible linker connecting the RNA-binding domain (RBD) and the central effector domain (ED).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-06T11:49:34.373Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":73,"end":82,"reference_id":"20133840","reference_source":"pmid","reference_html":"Structural insights into phosphoinositide 3-kinase activation by the influenza A virus NS1 protein. <i> Hale BG, Kerry PS, Jackson D, Precious BL, Gray A, Killip MJ, Randall RE, Russell RJ. </i> Proc Natl Acad Sci U S A, 2010","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP03575r003","statement":[{"text":"Flexible linker connecting the RNA-binding domain (RBD) and the central effector domain (ED).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-06T11:52:26.125Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":3,"released":"2021_12","sequence":"MDPNTVSSFQVDCFLWHVRKRVADQELGDAPFLDRLRRDQKSLRGRGSTLGLDIETATRAGKQIVERILKEESDEALKMTMASVPASRYLTDMTLEEMSRDWSMLIPKQKVAGPLCIRMDQAIMDKNIILKANFSVIFDRLETLILLRAFTEEGAIVGEISPLPSLPGHTAEDVKNAVGVLIGGLEWNDNTVRVSETLQRFAWRSSNENGRPPLTPKQKREMAGTIRSEV","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Polyploviricotina","Insthoviricetes","Articulavirales","Orthomyxoviridae","Alphainfluenzavirus"],"dataset":["Viral proteins","RNA-binding proteins"],"uniref50":"UniRef50_P03495","uniref90":"UniRef90_Q91MA0","uniref100":"UniRef100_B4URE2","genes":[{"name":{"value":"NS","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04066","url":"https://hamap.expasy.org/unirule/MF_04066"}}]}}],"disorder_content":0.1608695652173913,"disprot_consensus":{"full":[{"start":73,"end":82,"type":"D"},{"start":204,"end":230,"type":"D"}],"Structural state":[{"start":73,"end":82,"type":"D"},{"start":204,"end":230,"type":"D"}],"Disorder function":[{"start":73,"end":82,"type":"F"}]}},{"disprot_id":"DP03577","acc":"P15659","creator":"fquaglia","date":"2021-12-03T13:58:20.564Z","features":{"pfam":[{"id":"PF00603","name":"Influenza RNA-dependent RNA polymerase subunit PA","start":21,"end":714}],"gene3D":[]},"length":716,"name":"Polymerase acidic protein","ncbi_taxon_id":381518,"organism":"Influenza A virus (strain A/Wilson-Smith/1933 H1N1)","regions":[{"start":197,"end":257,"reference_id":"25855727","reference_source":"pmid","reference_html":"Temperature-Sensitive Mutants in the Influenza A Virus RNA Polymerase: Alterations in the PA Linker Reduce Nuclear Targeting of the PB1-PA Dimer and Result in Viral Attenuation. <i> Da Costa B, Sausset A, Munier S, Ghounaris A, Naffakh N, Le Goffic R, Delmas B. </i> J Virol, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03577r001","statement":[{"text":"Circular dichroism experiments revealed that the PA linker by itself is structurally disordered.","type":"Abstract"},{"text":"To investigate its structure in the absence of other viral components, the PA linker of the H1N1 A/WSN/33 (WSN) virus was expressed in Escherichia coli and purified to homogeneity. Its secondary structure was estimated using circular dichroism (CD) spectroscopy. The recorded spectra showed shape characteristics of a random coiled conformation with no evidence of stable secondary structures (Fig. 2). Dynamic light scattering analyses showed that the PA linker has a hydrodynamic radius of about 3 nm, suggesting that it exists as a monomer in solution. These data suggest that the PA linker mainly adopts a disordered structure when not associated with other polymerase components and that its conserved residues among influenza A, B, and C viruses are not the mark of intramolecular stable self-folding.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-06T10:48:57.380Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":210,"end":226,"reference_id":"25855727","reference_source":"pmid","reference_html":"Temperature-Sensitive Mutants in the Influenza A Virus RNA Polymerase: Alterations in the PA Linker Reduce Nuclear Targeting of the PB1-PA Dimer and Result in Viral Attenuation. <i> Da Costa B, Sausset A, Munier S, Ghounaris A, Naffakh N, Le Goffic R, Delmas B. </i> J Virol, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0045071","term_name":"negative regulation of viral genome replication","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03577r002","statement":[{"text":"Temperature-Sensitive Mutants in the Influenza A Virus RNA Polymerase: Alterations in the PA Linker Reduce Nuclear Targeting of the PB1-PA Dimer and Result in Viral Attenuation","type":"Title"},{"text":"A large series of PA linker mutants exhibited a temperature-sensitive (ts) phenotype (reduced viral growth at 39.5°C versus 37°C/33°C), suggesting an alteration of folding kinetic parameters. The ts phenotype was associated with a reduced efficiency of replication/transcription of a pseudoviral reporter RNA in a minireplicon assay.","type":"Abstract"},{"text":"Overall, these data indicate that single substitutions in a small subdomain of the PA linker, mapping from positions 210 to 226, allow generation of mutants that display strong or less-pronounced ts phenotypes.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-06T10:59:41.502Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of viral genome replication.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":210,"end":226,"reference_id":"25855727","reference_source":"pmid","reference_html":"Temperature-Sensitive Mutants in the Influenza A Virus RNA Polymerase: Alterations in the PA Linker Reduce Nuclear Targeting of the PB1-PA Dimer and Result in Viral Attenuation. <i> Da Costa B, Sausset A, Munier S, Ghounaris A, Naffakh N, Le Goffic R, Delmas B. </i> J Virol, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0032897","term_name":"negative regulation of viral transcription","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03577r003","statement":[{"text":"Temperature-Sensitive Mutants in the Influenza A Virus RNA Polymerase: Alterations in the PA Linker Reduce Nuclear Targeting of the PB1-PA Dimer and Result in Viral Attenuation","type":"Title"},{"text":"A large series of PA linker mutants exhibited a temperature-sensitive (ts) phenotype (reduced viral growth at 39.5°C versus 37°C/33°C), suggesting an alteration of folding kinetic parameters. The ts phenotype was associated with a reduced efficiency of replication/transcription of a pseudoviral reporter RNA in a minireplicon assay.","type":"Abstract"},{"text":"Overall, these data indicate that single substitutions in a small subdomain of the PA linker, mapping from positions 210 to 226, allow generation of mutants that display strong or less-pronounced ts phenotypes.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-06T10:59:42.996Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of viral transcription.\" [GOC:mah]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":197,"end":257,"reference_id":"25855727","reference_source":"pmid","reference_html":"Temperature-Sensitive Mutants in the Influenza A Virus RNA Polymerase: Alterations in the PA Linker Reduce Nuclear Targeting of the PB1-PA Dimer and Result in Viral Attenuation. <i> Da Costa B, Sausset A, Munier S, Ghounaris A, Naffakh N, Le Goffic R, Delmas B. </i> J Virol, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03577r004","statement":[{"text":"We investigated the structure and function of the PA linker (residues 197 to 256), located between its N-terminal endonuclease domain and its C-terminal structured domain that binds PB1, the polymerase core. Circular dichroism experiments revealed that the PA linker by itself is structurally disordered.","type":"Abstract"},{"text":"To investigate its structure in the absence of other viral components, the PA linker of the H1N1 A/WSN/33 (WSN) virus was expressed in Escherichia coli and purified to homogeneity. Its secondary structure was estimated using circular dichroism (CD) spectroscopy. The recorded spectra showed shape characteristics of a random coiled conformation with no evidence of stable secondary structures (Fig. 2). Dynamic light scattering analyses showed that the PA linker has a hydrodynamic radius of about 3 nm, suggesting that it exists as a monomer in solution. These data suggest that the PA linker mainly adopts a disordered structure when not associated with other polymerase components and that its conserved residues among influenza A, B, and C viruses are not the mark of intramolecular stable self-folding.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-06T10:54:50.427Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"},{"start":197,"end":257,"reference_id":"25855727","reference_source":"pmid","reference_html":"Temperature-Sensitive Mutants in the Influenza A Virus RNA Polymerase: Alterations in the PA Linker Reduce Nuclear Targeting of the PB1-PA Dimer and Result in Viral Attenuation. <i> Da Costa B, Sausset A, Munier S, Ghounaris A, Naffakh N, Le Goffic R, Delmas B. </i> J Virol, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0097747","term_name":"RNA polymerase activity","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03577r005","statement":[{"text":"We first observed that the wild-type polymerase activity was higher at 37°C than at 33°C (with an about 4-fold increase) and 39.5°C (2-fold). Compared to the wild type at a given temperature, all the polymerases reconstituted with a mutant PA had a reduced activity, a feature that was generally less pronounced at 33°C than at 37°C and 39.5°C (Fig. 6 and Table 2). Importantly, mutations T210P, K213P, D216P, F223P, and L226P, which induced a ts phenotype in the context of an infectious virus, also promoted a ts phenotype in the minireplicon assay, with a polymerase activity at 33°C ranging from 7 to 61% of the wild-type activity and less than 2% of the wild-type activity at 39.5°C (and even at 37°C).","type":"Results"},{"text":"Two additional points should be noted: (i) the drop of polymerase activity for the ts mutations was observed at 37°C (and 39.5°C), not only at 39.5°C, while the ts phenotype of the virus mutants was only identified at 39.5°C (and not at 37°C), suggesting that the minigenome test is more sensitive and/or does not strictly mimic the viral RNA polymerase activities in infected cells as previously observed (37); (ii) additional proline substitutions engineered at the extremities of the linker and at conserved positions between influenza A, B, and C viruses (E198, I201, Y232, and M249) were all deleterious for the polymerase activity and did not reveal additional mutations able to confer a ts phenotype in this assay.","type":"Results"},{"text":"The L214P virus mutant failed to be rescued, a hallmark in agreement with the absence of detectable RNA polymerase activity for PA L214P at all the tested temperatures in the minigenome assay (Fig. 6). However, PA L214P exhibited a less-pronounced defect than PA F223P (which allowed virus mutant recovery) in promoting PB1 translocation to the nucleus at 33°C (Fig. 7). These observations suggest that RNA synthesis activity per se may also be affected by the L214P mutation.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-06T10:59:45.206Z"},"ec_go":"IMP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Catalysis of the reaction: nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1); the synthesis of RNA from ribonucleotide triphosphates in the presence of a nucleic acid template.\" [GOC:pf]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":197,"end":257,"reference_id":"25855727","reference_source":"pmid","reference_html":"Temperature-Sensitive Mutants in the Influenza A Virus RNA Polymerase: Alterations in the PA Linker Reduce Nuclear Targeting of the PB1-PA Dimer and Result in Viral Attenuation. <i> Da Costa B, Sausset A, Munier S, Ghounaris A, Naffakh N, Le Goffic R, Delmas B. </i> J Virol, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0006606","term_name":"protein import into nucleus","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03577r006","statement":[{"text":"PA ts (and lethal) mutations block the recruitment and the transport of PB1 toward the nucleus at nonpermissive temperature.","type":"Results"},{"text":"In order to determine whether the ts mutations may interfere with the nuclear import of PA or the formation of the PA-PB1 complex in the cytoplasm and its transport to the nucleus, we generated a series of plasmid constructs to express or coexpress the PA and PB1 subunits. Fluorescently labeled PB1 and PA (wild-type and mutant) subunits were first expressed separately to study their intracellular localization (data not shown). Both types of subunits showed an accumulation in the cytoplasm and a faint localization in the nucleus, in accordance with previous data (5, 6, 7). ","type":"Results"},{"text":"Next, we analyzed the localization of the PB1 subunit when coexpressed with PA (Fig. 7; Table 2). Our experiments confirmed that when the wild-type PA and PB1 were expressed together, PB1 and PA localized into the nucleus, in contrast to what was observed when PB1 or PA was expressed alone. The temperature used during protein expression (33°C, 37°C, or 39.5°C) did not modulate the PB1 targeting to the nucleus: about 80% of the PB1-expressing cells were labeled in the nucleus at any temperature (Fig. 7B).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-12-06T10:49:56.093Z"},"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The directed movement of a protein from the cytoplasm to the nucleus.\" [GOC:jl]","disprot_namespace":"Disorder function","term_is_binding":false}],"regions_counter":6,"released":"2023_06","sequence":"MEDFVRQCFNPMIVELAEKAMKEYGEDLKIETNKFAAICTHLEVCFMYSDFHFIDEQGESIVVELGDPNALLKHRFEIIEGRDRTIAWTVINSICNTTGAEKPKFLPDLYDYKKNRFIEIGVTRREVHIYYLEKANKIKSEKTHIHIFSFTGEEMATKADYTLDEESRARIKTRLFTIRQEMASRGLWDSFRQSERGEETIEERFEITGTMRKLADQSLPPNFSSLENFRAYVDGFEPNGYIEGKLSQMSKEVNARIEPFLKSTPRPLRLPDGPPCSQRSKFLLMDALKLSIEDPSHEGEGIPLYDAIKCMRTFFGWKEPNVVKPHEKGINPNYLLSWKQVLAELQDIENEEKIPRTKNMKKTSQLKWALGENMAPEKVDFDDCKDVGDLKQYDSDEPELRSLASWIQNEFNKACELTDSSWIELDEIGEDAAPIEHIASMRRNYFTAEVSHCRATEYIMKGVYINTALLNASCAAMDDFQLIPMISKCRTKEGRRKTNLYGFIIKGRSHLRNDTDVVNFVSMEFSLTDPRLEPHKWEKYCVLEVGDMLLRSAIGHVSRPMFLYVRTNGTSKIKMKWGMEMRRCLLQSLQQIESMIEAESSVKEKDMTKEFFENKSETWPVGESPKGVEEGSIGKVCRTLLAKSVFNSLYASPQLEGFSAESRKLLLIVQALRDNLEPGTFDLGGLYEAIEECLINDPWVLLNASWFNSFLTHALR","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Polyploviricotina","Insthoviricetes","Articulavirales","Orthomyxoviridae","Alphainfluenzavirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_P03433","uniref90":"UniRef90_P03433","uniref100":"UniRef100_P15659","genes":[{"name":{"value":"PA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04063","url":"https://hamap.expasy.org/unirule/MF_04063"}}]}}],"disorder_content":0.08519553072625698,"disprot_consensus":{"full":[{"start":197,"end":257,"type":"D"}],"Structural state":[{"start":197,"end":257,"type":"D"}],"Biological process":[{"start":197,"end":257,"type":"F"}],"Disorder function":[{"start":197,"end":257,"type":"F"}],"Molecular function":[{"start":197,"end":257,"type":"F"}]}},{"disprot_id":"DP03578","acc":"F8UU09","creator":"gbalatti","date":"2021-12-06T11:06:52.645Z","features":{"pfam":[{"id":"PF00064","name":"Neuraminidase","start":85,"end":462}],"gene3D":[]},"length":469,"name":"Neuraminidase","ncbi_taxon_id":1027873,"organism":"Influenza A virus","regions":[{"start":1,"end":82,"reference_id":"23028314","reference_source":"pmid","reference_html":"H1N1 2009 pandemic influenza virus: resistance of the I223R neuraminidase mutant explained by kinetic and structural analysis. <i> van der Vries E, Collins PJ, Vachieri SG, Xiong X, Liu J, Walker PA, Haire LF, Hay AJ, Schutten M, Osterhaus AD, Martin SR, Boucher CA, Skehel JJ, Gamblin SJ. </i> PLoS Pathog, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_03","version":1,"cross_refs":[{"db":"PDB","id":"4B7N"},{"db":"PDB","id":"4B7J"},{"db":"PDB","id":"4B7M"}],"region_id":"DP03578r001","statement":[{"text":"Missing residues reported at PDB entries 4B7N, 4B7J and 4B7M","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-12T15:41:02.044Z"}}],"regions_counter":1,"released":"2021_12","sequence":"MNPNQKIITIGSVCMTIGMANLILQIGNIISIWISHSIQLGNQNQIETCNQSVITYENNTWVNQTYVNISNTNFAAGQSVVSVKLAGNSSLCPVSGWAIYSKDNSIRIGSKGDVFVIREPFISCSPLECRTFFLTQGALLNDKHSNGTIKDRSPYRTLMSCPIGEVPSPYNSRFESVAWSASACHDGINWLTIGISGPDNGAVAVLKYNGIITDTIKSWRNNRLRTQESECACVNGSCFTVMTDGPSDGQASYKIFRIEKGKIVKSVEMNAPNYHYEECSCYPDSSEITCVCRDNWHGSNRPWVSFNQNLEYQIGYICSGIFGDNPRPNDKTGSCGPVSSNGANGVKGFSFKYGNGVWIGRTKSISSRNGFEMIWDPNGWTGTDNDFSIKQDIVGINEWSGYSGSFVQHPELTGLDCIRPCFWVELIRGRPKENTIWTSGSSISFCGVNSDTVGWSWPDGAELPFTIDK","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Polyploviricotina","Insthoviricetes","Articulavirales","Orthomyxoviridae","Alphainfluenzavirus"],"dataset":["Viral proteins"],"uniref50":"UniRef50_P03470","uniref90":"UniRef90_Q710U6","uniref100":"UniRef100_D8KRX1","genes":[{"name":{"value":"NA","evidences":[{"code":"ECO:0000256","source":{"name":"HAMAP-Rule","id":"MF_04071","url":"https://hamap.expasy.org/unirule/MF_04071"}},{"code":"ECO:0000256","source":{"name":"RuleBase","id":"RU361252","url":"https://www.uniprot.org/unirule/RU361252"}},{"code":"ECO:0000313","source":{"name":"EMBL","id":"AEE69001.1","url":"https://www.ebi.ac.uk/ena/browser/view/AEE69001.1"}}]}}],"disorder_content":0.17484008528784648,"disprot_consensus":{"full":[{"start":1,"end":82,"type":"D"}],"Structural state":[{"start":1,"end":82,"type":"D"}]}},{"disprot_id":"DP03579","acc":"Q9JYY3","creator":"esalladini","date":"2021-12-15T14:28:03.899Z","features":{"pfam":[{"id":"PF06689","name":"ClpX C4-type zinc finger","start":7,"end":43},{"id":"PF07724","name":"AAA domain (Cdc48 subfamily)","start":112,"end":310},{"id":"PF10431","name":"C-terminal, D2-small domain, of ClpB protein","start":316,"end":387}],"gene3D":[]},"length":414,"name":"ATP-dependent Clp protease ATP-binding subunit ClpX","ncbi_taxon_id":122586,"organism":"Neisseria meningitidis serogroup B (strain MC58)","regions":[{"start":1,"end":62,"reference_id":"31916936","reference_source":"pmid","reference_html":"A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery. <i> Ripstein ZA, Vahidi S, Houry WA, Rubinstein JL, Kay LE. </i> Elife, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"6VFX"},{"db":"PDB","id":"6VFS"},{"db":"EMDB","id":"EMD-21187"}],"region_id":"DP03579r001","statement":[{"text":"Even though the full-length constructs of ClpX included the zinc binding domains (residues 1–62), no density was found for these domains in either conformation, likely due to their flexibility.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-12-17T08:49:55.219Z"},"ec_go":"IDA","disprot_namespace":"Structural state"},{"start":1,"end":62,"reference_id":"31916936","reference_source":"pmid","reference_html":"A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery. <i> Ripstein ZA, Vahidi S, Houry WA, Rubinstein JL, Kay LE. </i> Elife, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"6VFX"},{"db":"PDB","id":"6VFS"},{"db":"EMDB","id":"EMD-21187"}],"region_id":"DP03579r002","statement":[{"text":"Even though the full-length constructs of ClpX included the zinc binding domains (residues 1–62), no density was found for these domains in either conformation, likely due to their flexibility.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Disorder function","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:30:00.207Z"}},{"start":265,"end":280,"reference_id":"31916936","reference_source":"pmid","reference_html":"A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery. <i> Ripstein ZA, Vahidi S, Houry WA, Rubinstein JL, Kay LE. </i> Elife, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"6VFX"},{"db":"PDB","id":"6VFS"},{"db":"EMDB","id":"EMD-21187"}],"region_id":"DP03579r003","statement":[{"text":"The lack of density for the IGF loop belonging to protomer X6 in Conformation A (Figure 2—figure supplement 1) is likely due to conformational flexibility and sub-stoichiometric binding of this IGF loop into the ClpP-binding pocket.","type":"Results"},{"text":"All six IGF loops in ClpX adopt different configurations in Conformations A and B (Figure 2—figure supplement 1).","type":"Results"},{"text":"The ClpX residues immediately following where the IGF loops contact ClpP (residues 275–280) show weak or no density, likely indicating flexibility. This property allows the IGF loops to accommodate movement of the ClpX protomers relative to ClpP (Figure 2D–F), analogous to a set of springs.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:29:56.403Z"}},{"start":265,"end":280,"reference_id":"31916936","reference_source":"pmid","reference_html":"A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery. <i> Ripstein ZA, Vahidi S, Houry WA, Rubinstein JL, Kay LE. </i> Elife, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"6VFX"},{"db":"PDB","id":"6VFS"},{"db":"EMDB","id":"EMD-21187"}],"region_id":"DP03579r004","statement":[{"text":"The lack of density for the IGF loop belonging to protomer X6 in Conformation A (Figure 2—figure supplement 1) is likely due to conformational flexibility and sub-stoichiometric binding of this IGF loop into the ClpP-binding pocket.","type":"Results"},{"text":"All six IGF loops in ClpX adopt different configurations in Conformations A and B (Figure 2—figure supplement 1).","type":"Results"},{"text":"The ClpX residues immediately following where the IGF loops contact ClpP (residues 275–280) show weak or no density, likely indicating flexibility. This property allows the IGF loops to accommodate movement of the ClpX protomers relative to ClpP (Figure 2D–F), analogous to a set of springs.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Disorder function","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:30:02.294Z"}}],"regions_counter":4,"released":"2023_12","sequence":"MSNENRTCSFCGKSKSHVKHLIEGENAFICDECVSNCIEILHEDGNDGTPSESAGGEPEESGKLPTPAEIVANLNDHVIGQEQAKKALAVSVYNHYKRLRHPKAGANVELSKSNILLIGPTGSGKTLLAQSLARKLDVPFVMADATTLTEAGYVGEDVEQIITKLLGKCDFDVEKAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKLIEGTVASVPPQGGRKHPNQEFINVDTTNILFICGGAFAGLEKVIRQRTEKGGIGFGASVHSKDENADITKLFGIVEPEDLIKFGLIPELIGRLPVIATLEELDEDALINILTEPKNALVKQYQALFGMENVELEFEEGALRSIARQAMERKTGARGLRSIVERCLLDTMYRLPDLKGLKKVVVGKAVIEEGREPELVFES","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"genes":[{"name":{"value":"clpX","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00175","url":"https://hamap.expasy.org/unirule/MF_00175"}}]},"olnNames":[{"value":"NMB1372"}]}],"alphafold_very_low_content":0.04589371980676329,"disorder_content":0.18840579710144928,"disprot_consensus":{"full":[{"start":1,"end":62,"type":"D"},{"start":265,"end":280,"type":"D"}],"Structural state":[{"start":1,"end":62,"type":"D"},{"start":265,"end":280,"type":"D"}],"Disorder function":[{"start":1,"end":62,"type":"F"},{"start":265,"end":280,"type":"F"}]}},{"disprot_id":"DP03580","acc":"Q9JZ38","creator":"esalladini","date":"2021-12-15T15:22:44.535Z","features":{"pfam":[{"id":"PF00574","name":"Clp protease","start":17,"end":198}],"gene3D":[]},"length":204,"name":"ATP-dependent Clp protease proteolytic subunit","ncbi_taxon_id":122586,"organism":"Neisseria meningitidis serogroup B (strain MC58)","regions":[{"start":11,"end":21,"reference_id":"31754640","reference_source":"pmid","reference_html":"ClpP protease activation results from the reorganization of the electrostatic interaction networks at the entrance pores. <i> Mabanglo MF, Leung E, Vahidi S, Seraphim TV, Eger BT, Bryson S, Bhandari V, Zhou JL, Mao YQ, Rizzolo K, Barghash MM, Goodreid JD, Phanse S, Babu M, Barbosa LRS, Ramos CHI, Batey RA, Kay LE, Pai EF, Houry WA. </i> Commun Biol, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"cross_refs":[{"db":"PDB","id":"6NAQ"}],"region_id":"DP03580r001","sequence_construct":"HHHHHHENLYFQSNMSFDNYLVPTVIEQSGRGERAFDIYSRLLKERIVFLVGPVTDESANLVVAQLLFLESENPDKDIFFYINSPGGSVTAGMSIYDTMNFIKPDVSTLCLGQAASMGAFLLSAGEKGKRFALPNSRIMIHQPLISGGLGGQASDIEIHARELLKIKEKLNRLMAKHCDRDLADLERDTDRDNFMSAEEAKEYGLIDQILENRASLRL","statement":[{"text":"Electron density for N-terminal residues that form the axial loops of EcClpP is unclear in all but one subunit (Chain B). In previously published structures, these axial loops are highly flexible and are usually disordered in the crystal in the absence of activators or through preclusion by crystal packing23.","type":"Results"},{"text":"The structure of apo-NmClpP contains a tetradecamer in the asymmetric unit and shows no clear density for any of the 14 N-terminal axial loops.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:30:27.686Z"}},{"start":1,"end":22,"reference_id":"31754640","reference_source":"pmid","reference_html":"ClpP protease activation results from the reorganization of the electrostatic interaction networks at the entrance pores. <i> Mabanglo MF, Leung E, Vahidi S, Seraphim TV, Eger BT, Bryson S, Bhandari V, Zhou JL, Mao YQ, Rizzolo K, Barghash MM, Goodreid JD, Phanse S, Babu M, Barbosa LRS, Ramos CHI, Batey RA, Kay LE, Pai EF, Houry WA. </i> Commun Biol, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"cross_refs":[{"db":"PDB","id":"6NAH"}],"region_id":"DP03580r002","sequence_construct":"HHHHHHENLYFQSNMSFDNYLVPTVIEQSGRGERAFDIYSRLLKERIVFLVGPVTDESANLVVAQLLFLESENPDKDIFFYINSPGGSVTAGMSIYDTMNFIKPDVSTLCLGQAASMGAFLLSAGEKGKRFALPNSRIMIHQPLISGGLGGQASDIEIHARELLKIKEKLNRLMAKHCDRDLADLERDTDRDNFMSAEEAKEYGLIDQILENRASLRL","statement":[{"text":"No electron density was observed for residues 1–22 of all 28 subunits due to crystal packing (Fig. 1c, Supplementary Fig. 1d).","type":"Results"},{"text":"The structure of apo-NmClpP contains a tetradecamer in the asymmetric unit and shows no clear density for any of the 14 N-terminal axial loops.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:30:29.558Z"}},{"start":6,"end":22,"reference_id":"31754640","reference_source":"pmid","reference_html":"ClpP protease activation results from the reorganization of the electrostatic interaction networks at the entrance pores. <i> Mabanglo MF, Leung E, Vahidi S, Seraphim TV, Eger BT, Bryson S, Bhandari V, Zhou JL, Mao YQ, Rizzolo K, Barghash MM, Goodreid JD, Phanse S, Babu M, Barbosa LRS, Ramos CHI, Batey RA, Kay LE, Pai EF, Houry WA. </i> Commun Biol, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"EMDB","id":"EMD-21187"},{"db":"PDB","id":"6NAQ"},{"db":"PDB","id":"6NAH"},{"db":"EMDB","id":"EMD-21194"}],"region_id":"DP03580r003","statement":[{"text":"These β-hairpins closely resemble the conformation seen in the ADEP-bound structures of NmClpP (Goodreid et al., 2016) and are notably different from the disordered conformations observed in NmClpP when it is not bound to either ClpX or ADEP (Figure 2—figure supplement 2B; Mabanglo et al., 2019). By forming ordered gates, ClpX binding creates a wide entrance pore with a diameter of ~23 Å for substrates to pass through into the ClpP degradation chamber (Figure 2G, left; Figure 2—figure supplement 2). While it has long been suspected that the activating mechanism of ADEPs involves a disorder-to-order transition of these gates (Li et al., 2010), this observation provides direct evidence that ClpX binding has the same effect.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:30:32.726Z"}},{"start":6,"end":22,"reference_id":"31754640","reference_source":"pmid","reference_html":"ClpP protease activation results from the reorganization of the electrostatic interaction networks at the entrance pores. <i> Mabanglo MF, Leung E, Vahidi S, Seraphim TV, Eger BT, Bryson S, Bhandari V, Zhou JL, Mao YQ, Rizzolo K, Barghash MM, Goodreid JD, Phanse S, Babu M, Barbosa LRS, Ramos CHI, Batey RA, Kay LE, Pai EF, Houry WA. </i> Commun Biol, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"EMDB","id":"EMD-21187"},{"db":"PDB","id":"6NAQ"},{"db":"PDB","id":"6NAH"},{"db":"EMDB","id":"EMD-21194"}],"interaction_partner":[{"db":"UniProt","id":"Q9JYY3","partner_start":null,"partner_end":null}],"region_id":"DP03580r004","statement":[{"text":"These β-hairpins closely resemble the conformation seen in the ADEP-bound structures of NmClpP (Goodreid et al., 2016) and are notably different from the disordered conformations observed in NmClpP when it is not bound to either ClpX or ADEP (Figure 2—figure supplement 2B; Mabanglo et al., 2019). By forming ordered gates, ClpX binding creates a wide entrance pore with a diameter of ~23 Å for substrates to pass through into the ClpP degradation chamber (Figure 2G, left; Figure 2—figure supplement 2). While it has long been suspected that the activating mechanism of ADEPs involves a disorder-to-order transition of these gates (Li et al., 2010), this observation provides direct evidence that ClpX binding has the same effect.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":20,"db":"ChEBI","id":"30617","statements":[{"type":"Results","text":"As shown below and in previous work (Joshi et al., 2004; Hersch et al., 2005; Grimaud et al., 1998; Jones et al., 1998), the presence of MgATP is required for tight binding between ClpX and ClpP."}],"entry_name":"MgATP(2-)"}],"ec_go":"IDA","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:30:36.161Z"}},{"start":6,"end":22,"reference_id":"31754640","reference_source":"pmid","reference_html":"ClpP protease activation results from the reorganization of the electrostatic interaction networks at the entrance pores. <i> Mabanglo MF, Leung E, Vahidi S, Seraphim TV, Eger BT, Bryson S, Bhandari V, Zhou JL, Mao YQ, Rizzolo K, Barghash MM, Goodreid JD, Phanse S, Babu M, Barbosa LRS, Ramos CHI, Batey RA, Kay LE, Pai EF, Houry WA. </i> Commun Biol, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03580r005","statement":[{"text":"These β-hairpins closely resemble the conformation seen in the ADEP-bound structures of NmClpP (Goodreid et al., 2016) and are notably different from the disordered conformations observed in NmClpP when it is not bound to either ClpX or ADEP (Figure 2—figure supplement 2B; Mabanglo et al., 2019). By forming ordered gates, ClpX binding creates a wide entrance pore with a diameter of ~23 Å for substrates to pass through into the ClpP degradation chamber (Figure 2G, left; Figure 2—figure supplement 2). While it has long been suspected that the activating mechanism of ADEPs involves a disorder-to-order transition of these gates (Li et al., 2010), this observation provides direct evidence that ClpX binding has the same effect.","type":"Results"}],"states_connection":[{"source":"DP03580r002","target":"DP03580r003"}],"ec_go":"IDA","disprot_namespace":"Structural transition","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:30:34.256Z"}}],"regions_counter":5,"released":"2023_12","sequence":"MSFDNYLVPTVIEQSGRGERAFDIYSRLLKERIVFLVGPVTDESANLVVAQLLFLESENPDKDIFFYINSPGGSVTAGMSIYDTMNFIKPDVSTLCLGQAASMGAFLLSAGEKGKRFALPNSRIMIHQPLISGGLGGQASDIEIHARELLKIKEKLNRLMAKHCDRDLADLERDTDRDNFMSAEEAKEYGLIDQILENRASLRL","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"genes":[{"name":{"value":"clpP","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00444","url":"https://hamap.expasy.org/unirule/MF_00444"}}]},"olnNames":[{"value":"NMB1312"}]}],"alphafold_very_low_content":0.004901960784313725,"disorder_content":0.10784313725490197,"disprot_consensus":{"full":[{"start":1,"end":5,"type":"D"},{"start":6,"end":22,"type":"T"}],"Structural state":[{"start":1,"end":22,"type":"D"}],"Molecular function":[{"start":6,"end":22,"type":"F"}],"Structural transition":[{"start":6,"end":22,"type":"T"}]}},{"disprot_id":"DP03581","acc":"P55127","creator":"esalladini","date":"2021-12-16T15:29:08.702Z","features":{"pfam":[{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":878,"end":909},{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":1011,"end":1041},{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":1070,"end":1103},{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":1211,"end":1241},{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":1270,"end":1303},{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":1413,"end":1441},{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":1470,"end":1503},{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":1611,"end":1641},{"id":"PF00353","name":"RTX calcium-binding nonapeptide repeat (4 copies)","start":1670,"end":1703},{"id":"PF06594","name":"Haemolysin-type calcium binding protein related domain","start":947,"end":990},{"id":"PF06594","name":"Haemolysin-type calcium binding protein related domain","start":1147,"end":1190},{"id":"PF06594","name":"Haemolysin-type calcium binding protein related domain","start":1347,"end":1390},{"id":"PF06594","name":"Haemolysin-type calcium binding protein related domain","start":1547,"end":1590},{"id":"PF26745","name":"SPM domain","start":416,"end":582}],"gene3D":[]},"length":1829,"name":"Iron-regulated protein FrpC","ncbi_taxon_id":135720,"organism":"Neisseria meningitidis serogroup C","regions":[{"start":415,"end":591,"reference_id":"26138689","reference_source":"pmid","reference_html":"NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis. <i> Kubáň V, Nováček J, Bumba L, Žídek L. </i> Biomol NMR Assign, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"BMRB","id":"26530"}],"region_id":"DP03581r001","statement":[{"text":"The 1H−15N1H−15N HSQC spectrum of SPM exhibited a low dispersion of chemical shifts typical for disordered proteins (not shown).","type":"Results"},{"text":"The chemical shifts assigned in this study represent the major source of structural information for intrinsically disordered SPM.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2021-12-17T09:02:46.834Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":430,"end":450,"reference_id":"32184239","reference_source":"pmid","reference_html":"Structural Basis of Ca<sup>2+</sup>-Dependent Self-Processing Activity of Repeat-in-Toxin Proteins. <i> Kuban V, Macek P, Hritz J, Nechvatalova K, Nedbalcova K, Faldyna M, Sebo P, Zidek L, Bumba L. </i> mBio, 2020","date":"2022-02-15T16:18:20.585Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6SJW"},{"db":"PDB","id":"6SJX"},{"db":"BMRB","id":"34424"}],"region_id":"DP03581r002","statement":[{"text":"Conventional triple resonance and nuclear Overhauser effect spectroscopy (NOESY) NMR spectra provided structural information for the whole protein, except of a region of 21 residues between T430 and G450. These residues were affected by conformational or chemical exchange and likely formed a loop lacking a unique structure.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:30:52.757Z"}},{"start":413,"end":417,"reference_id":"32184239","reference_source":"pmid","reference_html":"Structural Basis of Ca<sup>2+</sup>-Dependent Self-Processing Activity of Repeat-in-Toxin Proteins. <i> Kuban V, Macek P, Hritz J, Nechvatalova K, Nedbalcova K, Faldyna M, Sebo P, Zidek L, Bumba L. </i> mBio, 2020","date":"2022-02-15T16:16:33.038Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000048","term_name":"limited proteolysis display site","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro415Ala","start":null,"end":null,"position":null}],"region_id":"DP03581r003","statement":[{"text":"To unravel the mechanistic details of the D414-P415 cleavage, we prepared a cleavage-incompetent mutant of SPM, where the proline residue (P415) of the D414-P415 cleavage site was replaced by an alanine residue (P415A). Unlike Ca-SPM, which represents a stabilized low-energy conformation of SPM after the cleavage and in which the N-terminal sequence begins with the P415 residue (415PLALD419), the SPM-P415A construct possesses the GSDALALD419 sequence at its N terminus.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:30:55.852Z"}},{"start":419,"end":424,"reference_id":"32184239","reference_source":"pmid","reference_html":"Structural Basis of Ca<sup>2+</sup>-Dependent Self-Processing Activity of Repeat-in-Toxin Proteins. <i> Kuban V, Macek P, Hritz J, Nechvatalova K, Nedbalcova K, Faldyna M, Sebo P, Zidek L, Bumba L. </i> mBio, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"6SJW"},{"db":"PDB","id":"6SJX"},{"db":"BMRB","id":"34424"}],"interaction_partner":[{"db":"ChEBI","id":"29108","partner_start":null,"partner_end":null}],"region_id":"DP03581r004","statement":[{"text":"Moreover, the SPM sequence contains a stretch of conserved residues (D419, D421, D423, and G424) that strongly resemble the conserved residues (positions 1, 3, 5, and 6) of an incomplete EF-hand-like motif. These residues form a stable loop in the Ca-SPM structure. Along with the adjacent D456 residue, these can provide two oxygens for calcium coordination and are likely to constitute the fourth Ca2+-binding site in Ca-SPM.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:30:57.130Z"}},{"start":462,"end":532,"reference_id":"32184239","reference_source":"pmid","reference_html":"Structural Basis of Ca<sup>2+</sup>-Dependent Self-Processing Activity of Repeat-in-Toxin Proteins. <i> Kuban V, Macek P, Hritz J, Nechvatalova K, Nedbalcova K, Faldyna M, Sebo P, Zidek L, Bumba L. </i> mBio, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"6SJW"},{"db":"PDB","id":"6SJX"},{"db":"BMRB","id":"34424"}],"interaction_partner":[{"db":"ChEBI","id":"29108","partner_start":null,"partner_end":null}],"region_id":"DP03581r005","statement":[{"text":"Three of the four Ca2+-binding sites are made up of sequential motifs (D462 to E474, D499 to D511, and D521 to E532) that closely resemble that of EF hands, while the fourth Ca2+-binding site consists of a structural motif, where the position 12 of an incomplete EF-hand-like motif (D419 to G424) is structurally supplemented by D456.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:30:58.557Z"}},{"start":415,"end":591,"reference_id":"32184239","reference_source":"pmid","reference_html":"Structural Basis of Ca<sup>2+</sup>-Dependent Self-Processing Activity of Repeat-in-Toxin Proteins. <i> Kuban V, Macek P, Hritz J, Nechvatalova K, Nedbalcova K, Faldyna M, Sebo P, Zidek L, Bumba L. </i> mBio, 2020","date":"2022-02-15T16:19:08.838Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"BMRB","id":"34424"}],"region_id":"DP03581r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":10,"db":"ChEBI","id":"29108","statements":[{"type":"Methods","text":"The collected fractions were mixed with dithiothreitol (DTT) to a final concentration of 10 mM before the protein solution was dialyzed overnight at 4°C in TN buffer supplemented with 10 mM DTT and 10 mM CaCl2."}],"entry_name":"calcium(2+)"}],"statement":[{"text":"As shown in Fig. 1B, the 1H-15N heteronuclear single-quantum coherence (HSQC) spectrum of Ca-SPM exhibited the broad dispersion of backbone amide cross-peaks typical for structured proteins.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:30:54.124Z"}}],"regions_counter":6,"released":"2023_12","sequence":"MNEGEVVLTPEQIQTLRGYASRGDTYGGWRYLANLGDRYADNAAAIVGKDTNLNGLNLWMKKGVENLWDDTVGKKTRLEKFDRVALQHFSQYVDLINKNNGRLPNTSEIERSYYKAVTYHGVSSSAAIDLVINRSLPDMADGYWALGLGIEAERIHNEQAVNNPNGSERDNRKQLISALDKGFDGSFKEKHFTFLQSVMMDLTKLGVEYTIDGWQKIGGWGNGIINDLYKSVVKREWTGIFEIVNNNIKQGNEAFKNEINSLVHDMKAAGKEFGDDLNTQWNNLTQAAEIIYNDIVDNTSQGIEKGVKAIKELSEKMKNAASDLADGSAEKAKQVVEDLAQAAKEAYENAKSTAEKAAQAAREFFKGLPSFKDLAEKFRDLFPNPEGWIDDGHQCFAPWVKETKKRNGKYHVYDPLALDLDGDGIETVATKGFSGSLFDHNRDGIRTATGWVAADDGLLVRDLNGNGIIDNGAELFGDNTKLADGSFAKHGYAALAELDSNGDNIINAADAAFQTLRVWQDLNQDGISQANELRTLEELGIQSLDLAYKDVNKNLGNGNTLAQQGSYTKTDGTTAKMGDLLLAADNLHSRFKDKVELTAEQAKAANLAGIGRLRDLREAAALSGDLANMLKAYSAAETKEAQLALLDNLIHKWAETDSNWGKKSPMRLSTDWTQTANEGIALTPSQVAQLKKNALVSLSDKAKAAIDAARDRIAVLDAYTGQDSSTLYYMSEEDALNIVKVTNDTYDHLAKNIYQNLLFQTRLQPYLNQISFKMENDTFTLDFSGLVQAFNHVKETNPQKAFVDLAEMLAYGELRSWYEGRRLMADYVEEAKKAGKFEDYQKVLGQETVALLAKTSGTQADDILQNVGFGHNKNVSLYGNDGNDTLIGGAGNDYLEGGSGSDTYVFGKGFGQDTVYNYDYATGRKDIIRFTDGITADMLTFTREGNHLLIKAKDDSGQVTVQSYFQNDGSGAYRIDEIHFDNGKVLDVATVKELVQQSTDGSDRLYAYQSGNTLNGGLGDDYLYGADGDDLLNGDAGNDSIYSGNGNDTLNGGEGNDALYGYNGNDALNGGEGNDHLNGEDGNDTLIGGAGNDYLEGGSGSDTYVFGKGFGQDTVYNYDYATGRKDIIRFTDGITADMLTFTREGNHLLIKAKDGSGQVTVQSYFQNDGSGAYRIDEIHFDNGKVLDVATVKELVQQSTDGSDRLYAYQSGNTLNGGLGDDYLYGADGDDLLNGDAGNDSIYSGNGNDTLDGGEGNDALYGYNGNDALNGGEGNDHLNGEDGNDTLIGGAGNDYLEGGSGSDTYVFGKGFGQDTVYNYDYATGRKDIIRFTDGITADMLTFTREGNHLLIKAKDDSGQVTVQSYFQNDGSGAYRIDEIHFDNGKVLDVATVKELVQQSTDGSDRLYAYQSGSTLNGGLGDDYLYGADGDDLLNGDAGNDSIYSGNGNDTLDGGEGNDALYGYNGNDALNGGEGNDHLNGEDGNDTLIGGAGNDYLEGGSGSDTYVFGKGFGQDTVYNYDYATGRKDIIRFTDGITADMLTFTREGNHLLIKAKDGSGQVTVQSYFQNDGSGAYRIDEIHFDNGKVLDVATVKKLVQQSTDGSDRLYAYQSGNTLNGGLGDDYLYGADGDDLLNGDAGNDSIYSGNGNDTLNGGEGNDALYGYNGNDVLNGGEGNDHLNGEDGNDTLIGGAGNDYLEGGSGSDTYVFGKGFGQDTVYNYHVDKNSDTMHFKGFKAADVHFIRSGSDLVLSASEQDNVRISGFFYGENHRVDTFVFDDAAISNPDFAKYINAGNNLVQSMSVFGSNTAATGGNVDANTQSVQQPLLVTPSA","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"genes":[{"name":{"value":"frpC"}}],"alphafold_very_low_content":0.1443411700382723,"dataset":["Unicellular toxins and antitoxins","Bacterial virulence-related proteins","Stress response proteins"],"disorder_content":0.0967741935483871,"disprot_consensus":{"full":[{"start":413,"end":414,"type":"F"},{"start":415,"end":591,"type":"T"}],"Structural state":[{"start":415,"end":591,"type":"D"}],"Disorder function":[{"start":413,"end":417,"type":"F"}],"Molecular function":[{"start":419,"end":424,"type":"F"},{"start":462,"end":532,"type":"F"}],"Structural transition":[{"start":415,"end":591,"type":"T"}]}},{"disprot_id":"DP03582","acc":"Q9JWM8","creator":"esalladini","date":"2021-12-21T13:00:23.260Z","features":{"pfam":[{"id":"PF01625","name":"Peptide methionine sulfoxide reductase","start":200,"end":359},{"id":"PF01641","name":"SelR domain","start":390,"end":505},{"id":"PF08534","name":"Redoxin","start":40,"end":159}],"gene3D":[]},"length":522,"name":"Peptide methionine sulfoxide reductase MsrA/MsrB","ncbi_taxon_id":122587,"organism":"Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 / Z2491)","regions":[{"start":365,"end":389,"reference_id":"18255097","reference_source":"pmid","reference_html":"A structural analysis of the catalytic mechanism of methionine sulfoxide reductase A from Neisseria meningitidis. <i> Ranaivoson FM, Antoine M, Kauffmann B, Boschi-Muller S, Aubry A, Branlant G, Favier F. </i> J Mol Biol, 2008","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"3BQF"},{"db":"PDB","id":"3BQG"},{"db":"PDB","id":"3BQE"},{"db":"PDB","id":"3BQH"}],"region_id":"DP03582r001","statement":[{"text":"Indeed, for all of these structures, no electron density is observed for about the last 25 residues either in the 3Fo − 2Fc or in the Fo − Fc sigma-A weighted electron density maps, indicating an extremely high mobility of the last C-terminal residues in the crystal.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:32:12.120Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MKHRTFFSLCAKFGCLLALGACSPKIVDAGAATVPHTLSTLKTADNRPASVYLKKDKPTLIKFWASWCPLCLSELGQTEKWAQDAKFSSANLITVASPGFLHEKKDGDFQKWYAGLNYPKLPVVTDNGGTIAQSLNISVYPSWALIGKDGDVQRIVKGSINEAQALALIRDPNADLGSLKHSFYKPDTQKKDSKIMNTRTIYLAGGCFWGLEAYFQRIDGVVDAVSGYANGNTKNPSYEDVSYRHTGHAETVKVTYDADKLSLDDILQYFFRVVDPTSLNKQGNDTGTQYRSGVYYTDPAEKAVIAAALKREQQKYQLPLVVENEPLKNFYDAEEYHQDYLIKNPNGYCHIDIRKADEPLPGKTKTAPQGKGFDAATYKKPSDAELKRTLTEEQYQVTQNSATEYAFSHEYDHLFKPGIYVDVVSGEPLFSSADKYDSGCGWPSFTRPIDAKSVTEHDDFSYNMRRTEVRSHAADSHLGHVFPDGPRDKGGLRYCINGASLKFIPLEQMDAAGYGALKSKVK","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"genes":[{"name":{"value":"msrAB"},"synonyms":[{"value":"pilB"}],"olnNames":[{"value":"NMA0290"}]}],"alphafold_very_low_content":0.09578544061302682,"disorder_content":0.04789272030651341,"disprot_consensus":{"full":[{"start":365,"end":389,"type":"D"}],"Structural state":[{"start":365,"end":389,"type":"D"}]}},{"disprot_id":"DP03583","acc":"A1KVD0","creator":"esalladini","date":"2021-12-21T13:14:00.619Z","features":{"pfam":[{"id":"PF04273","name":"Beta-lactamase hydrolase-like protein, phosphatase-like domain","start":19,"end":123}],"gene3D":[]},"length":155,"name":"DUF442 domain-containing protein","ncbi_taxon_id":272831,"organism":"Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)","regions":[{"start":1,"end":13,"reference_id":"17636569","reference_source":"pmid","reference_html":"Crystal structure of NMA1982 from Neisseria meningitidis at 1.5 angstroms resolution provides a structural scaffold for nonclassical, eukaryotic-like phosphatases. <i> Krishna SS, Tautz L, Xu Q, McMullan D, Miller MD, Abdubek P, Ambing E, Astakhova T, Axelrod HL, Carlton D, Chiu HJ, Clayton T, DiDonato M, Duan L, Elsliger MA, Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Koesema E, Morse AT, Mustelin T, Nigoghossian E, Oommachen S, Reyes R, Rife CL, van den Bedem H, Weekes D, White A, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, Wilson IA. </i> Proteins, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"2F46"}],"region_id":"DP03583r001","statement":[{"text":"The residual glycine residue from the TEV protease cleavage site and residues 1-12 of the protein are disordered in both monomers.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:32:22.279Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MPSEKQPQSKGNKMAILKLDEHLYISPQLTKADAEQIAQLGIKTVICNRPDREEESQPDFAQIKQWLEQAGVTGFHHQPVTARDIQKHDVETFRQLIGQAEYPVLAYCRTGTRCSLLWGFRRAAEGMPVDEIIRRAQAAGVNLENFRERLDNARV","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"genes":[{"olnNames":[{"value":"NMC1647","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAM10832.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAM10832.1"}}]}]}],"alphafold_very_low_content":0.08387096774193549,"disorder_content":0.08387096774193549,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"D"}],"Structural state":[{"start":1,"end":13,"type":"D"}]}},{"disprot_id":"DP03584","acc":"M4GGR4","creator":"esalladini","date":"2021-12-21T14:00:34.565Z","features":{"pfam":[{"id":"PF00267","name":"Gram-negative porin","start":42,"end":355}],"gene3D":[]},"length":355,"name":"Outer membrane protein","ncbi_taxon_id":487,"organism":"Neisseria meningitidis","regions":[{"start":1,"end":14,"reference_id":"33675718","reference_source":"pmid","reference_html":"An antibiotic-resistance conferring mutation in a neisserial porin: Structure, ion flux, and ampicillin binding. <i> Bartsch A, Ives CM, Kattner C, Pein F, Diehn M, Tanabe M, Munk A, Zachariae U, Steinem C, Llabrés S. </i> Biochim Biophys Acta Biomembr, 2021","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"7DE8"}],"region_id":"DP03584r001","statement":[{"text":"The N-terminal is missing from the pdb structure but was not mentioned in the paper.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:32:31.991Z"}}],"regions_counter":2,"released":"2023_12","sequence":"MASMTGGQQMGRDLQVTLYGTIKAGVEVSRVKDAGTYKAQGGKSKTATQIADFGSKIGFKGQEDLGNGMKAIWQLEQKASIAGTNSGWGNRQSFIGLKGGFGTVRAGNLNTVLKDSGDNVNAWESGSNTEDVLGLGTIGRVESREISVRYDSPVFAGFSGSVQYVPRDNANDVDKYKHTKSSRESYHAGLKYENAGFFGQYAGSFAKYADLNTDAERVAVNTANAHPVKDYQVHRVVAGYDANDLYVSVAGQYEAAKNNEVGSIKGKKHEQTQVAATAAYRFGNVTPRVSYAHGFKAKVNGVKDANYQYDQVIVGADYDFSKRTSALVSAGWLKQGKGAGKVEQTASMVGLRHKF","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"genes":[],"alphafold_very_low_content":0.04507042253521127,"disorder_content":0.03943661971830986,"disprot_consensus":{"full":[{"start":1,"end":14,"type":"D"}],"Structural state":[{"start":1,"end":14,"type":"D"}]}},{"disprot_id":"DP03585","acc":"P0A0V3","creator":"esalladini","date":"2021-12-21T14:06:32.017Z","features":{"pfam":[{"id":"PF00691","name":"OmpA family","start":104,"end":190}],"gene3D":[]},"length":242,"name":"Outer membrane protein class 4","ncbi_taxon_id":122586,"organism":"Neisseria meningitidis serogroup B (strain MC58)","regions":[{"start":230,"end":242,"reference_id":"14763978","reference_source":"pmid","reference_html":"Structure of the OmpA-like domain of RmpM from Neisseria meningitidis. <i> Grizot S, Buchanan SK. </i> Mol Microbiol, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"1R1M"}],"region_id":"DP03585r001","statement":[{"text":"The last 13 residues are not visible in the electron density map and are probably disordered.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:46:29.112Z"}},{"start":230,"end":242,"reference_id":"14763978","reference_source":"pmid","reference_html":"Structure of the OmpA-like domain of RmpM from Neisseria meningitidis. <i> Grizot S, Buchanan SK. </i> Mol Microbiol, 2004","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"1R1M"}],"region_id":"DP03585r002","statement":[{"text":"The last 13 residues are not visible in the electron density map and are probably disordered.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:46:37.660Z"}}],"regions_counter":2,"released":"2023_12","sequence":"MTKQLKLSALFVALLASGTAVAGEASVQGYTVSGQSNEIVRNNYGECWKNAYFDKASQGRVECGDAVAAPEPEPEPEPAPAPVVVVEQAPQYVDETISLSAKTLFGFDKDSLRAEAQDNLKVLAQRLSRTNVQSVRVEGHTDFMGSDKYNQALSERRAYVVANNLVSNGVPVSRISAVGLGESQAQMTQVCEAEVAKLGAKVSKAKKREALIACIEPDRRVDVKIRSIVTRQVVPAHNHHQH","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"genes":[{"name":{"value":"rmpM","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"2499543","url":"http://www.ncbi.nlm.nih.gov/pubmed/2499543","alternativeUrl":"https://europepmc.org/abstract/MED/2499543"}}]},"olnNames":[{"value":"NMB0382"}]}],"alphafold_very_low_content":0.10330578512396695,"disorder_content":0.05371900826446281,"disprot_consensus":{"full":[{"start":230,"end":242,"type":"D"}],"Structural state":[{"start":230,"end":242,"type":"D"}],"Disorder function":[{"start":230,"end":242,"type":"F"}]}},{"disprot_id":"DP03586","acc":"Q6VRY4","creator":"esalladini","date":"2021-12-21T14:52:02.977Z","features":{"pfam":[{"id":"PF08794","name":"Factor H binding protein, C-terminal","start":147,"end":243},{"id":"PF20937","name":"Factor H binding protein, N-terminal","start":8,"end":79}],"gene3D":[]},"length":260,"name":"Factor H binding protein variant B01_001","ncbi_taxon_id":487,"organism":"Neisseria meningitidis","regions":[{"start":2,"end":17,"reference_id":"19103601","reference_source":"pmid","reference_html":"Structural Basis for the Immunogenic Properties of the Meningococcal Vaccine Candidate LP2086. <i> Mascioni A, Bentley BE, Camarda R, Dilts DA, Fink P, Gusarova V, Hoiseth SK, Jacob J, Lin SL, Malakian K, McNeil LK, Mininni T, Moy F, Murphy E, Novikova E, Sigethy S, Wen Y, Zlotnick GW, Tsao DH. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"2KDY"}],"region_id":"DP03586r001","statement":[{"text":"D, overlay of the structured residues for both domains excluding the interdomain linker; r.m.s. deviation 0.96 Å. b-d, the unfolded N-terminal chain (residues 1-16) has been excluded for purposes of clarity. E, electrostatic surface representation for the entire LP2086-B01.","type":"Figure"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:46:43.554Z"}},{"start":2,"end":17,"reference_id":"19103601","reference_source":"pmid","reference_html":"Structural Basis for the Immunogenic Properties of the Meningococcal Vaccine Candidate LP2086. <i> Mascioni A, Bentley BE, Camarda R, Dilts DA, Fink P, Gusarova V, Hoiseth SK, Jacob J, Lin SL, Malakian K, McNeil LK, Mininni T, Moy F, Murphy E, Novikova E, Sigethy S, Wen Y, Zlotnick GW, Tsao DH. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"2KDY"}],"region_id":"DP03586r002","statement":[{"text":"D, overlay of the structured residues for both domains excluding the interdomain linker; r.m.s. deviation 0.96 Å. b-d, the unfolded N-terminal chain (residues 1-16) has been excluded for purposes of clarity. E, electrostatic surface representation for the entire LP2086-B01.","type":"Figure"}],"ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:46:49.023Z"}},{"start":141,"end":155,"reference_id":"19103601","reference_source":"pmid","reference_html":"Structural Basis for the Immunogenic Properties of the Meningococcal Vaccine Candidate LP2086. <i> Mascioni A, Bentley BE, Camarda R, Dilts DA, Fink P, Gusarova V, Hoiseth SK, Jacob J, Lin SL, Malakian K, McNeil LK, Mininni T, Moy F, Murphy E, Novikova E, Sigethy S, Wen Y, Zlotnick GW, Tsao DH. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"2KDY"}],"region_id":"DP03586r003","statement":[{"text":"A long flexible chain connects the folded part of the protein to the lipid anchor and acts as spacer, making both domains accessible to the host immune system.","type":"Abstract"},{"text":"The two domains are connected by a 15-residue linker (residues 140-154), which contains a short helical turn (α2) and crosses one end of the β-barrel, forming hydrophobic contacts through Phe147.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:46:45.177Z"}},{"start":141,"end":155,"reference_id":"19103601","reference_source":"pmid","reference_html":"Structural Basis for the Immunogenic Properties of the Meningococcal Vaccine Candidate LP2086. <i> Mascioni A, Bentley BE, Camarda R, Dilts DA, Fink P, Gusarova V, Hoiseth SK, Jacob J, Lin SL, Malakian K, McNeil LK, Mininni T, Moy F, Murphy E, Novikova E, Sigethy S, Wen Y, Zlotnick GW, Tsao DH. </i> J Biol Chem, 2009","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"2KDY"}],"region_id":"DP03586r004","statement":[{"text":"A long flexible chain connects the folded part of the protein to the lipid anchor and acts as spacer, making both domains accessible to the host immune system.","type":"Abstract"},{"text":"The two domains are connected by a 15-residue linker (residues 140-154), which contains a short helical turn (α2) and crosses one end of the β-barrel, forming hydrophobic contacts through Phe147.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:46:50.197Z"}},{"start":3,"end":33,"reference_id":"19636959","reference_source":"pmid","reference_html":"Backbone and side-chain assignment of the lipidated and non-lipidated forms of the meningococcal outer membrane protein LP2086. <i> Mascioni A, Jacob J, Moy F, Dilts D, Fink P, Malakian K, Sigethy S, Wen Y, Novikova E, Zlotnick GW, Tsao DH. </i> Biomol NMR Assign, 2009","date":"2022-02-15T12:34:40.240Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"BMRB","id":"16108"}],"region_id":"DP03586r005","statement":[{"text":"As expected, at the higher pH, residues 3–13, 15, 17, 19–22, 25–26, 28, 31–33, 36, 48–49, 60, 73, 207, 235, 245, 249, mostly belonging to unstructured regions, were not observable due to the increased rate of solvent exchange (88% backbone assignment).","type":"Article"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:46:47.417Z"}}],"regions_counter":5,"released":"2023_12","sequence":"CSSGGGGSGGGGVTADIGTGLADALTAPLDHKDKGLKSLTLEDSISQNGTLTLSAQGAEKTYGNGDSLNTGKLKNDKVSRFDFIRQIEVDGQLITLESGEFQVYKQSHSALTALQTEQEQDPEHSEKMVAKRRFRIGDIAGEHTSFDKLPKDVMATYRGTAFGSDDAGGKLTYTIDFAAKQGHGKIEHLKSPELNVDLAVAYIKPDEKHHAVISGSVLYNQDEKGSYSLGIFGEKAQEVAGSAEVETANGIHHIGLAAKQ","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"genes":[{"name":{"value":"fhbp","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAR84481.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAR84481.1"}}]}}],"alphafold_very_low_content":0.057692307692307696,"disorder_content":0.18076923076923077,"disprot_consensus":{"full":[{"start":2,"end":33,"type":"D"},{"start":141,"end":155,"type":"D"}],"Structural state":[{"start":2,"end":33,"type":"D"},{"start":141,"end":155,"type":"D"}],"Disorder function":[{"start":2,"end":17,"type":"F"},{"start":141,"end":155,"type":"F"}]}},{"disprot_id":"DP03587","acc":"Q9JZG1","creator":"esalladini","date":"2021-12-22T08:47:15.143Z","features":{"pfam":[{"id":"PF00682","name":"HMGL-like","start":6,"end":275},{"id":"PF08502","name":"LeuA allosteric (dimerisation) domain","start":372,"end":502},{"id":"PF22617","name":"Homocitrate synthase post-HMGL domain-like","start":289,"end":370}],"gene3D":[]},"length":517,"name":"2-isopropylmalate synthase","ncbi_taxon_id":122586,"organism":"Neisseria meningitidis serogroup B (strain MC58)","regions":[{"start":298,"end":310,"reference_id":"22352945","reference_source":"pmid","reference_html":"Removal of the C-terminal regulatory domain of α-isopropylmalate synthase disrupts functional substrate binding. <i> Huisman FH, Koon N, Bulloch EM, Baker HM, Baker EN, Squire CJ, Parker EJ. </i> Biochemistry, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"3RMJ"}],"region_id":"DP03587r001","statement":[{"text":"In NmeE365Term (PDB entry 3RMJ), each monomer comprised residues 1−364 of the full-length protein, with residues 4−296 and 311−324 being modeled for chain A and residues 4−297 and 311−324 for chain B; no interpretable electron density could be found for the remaining residues, which were presumed to be disordered.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:46:54.756Z"}},{"start":325,"end":364,"reference_id":"22352945","reference_source":"pmid","reference_html":"Removal of the C-terminal regulatory domain of α-isopropylmalate synthase disrupts functional substrate binding. <i> Huisman FH, Koon N, Bulloch EM, Baker HM, Baker EN, Squire CJ, Parker EJ. </i> Biochemistry, 2012","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"3RMJ"}],"region_id":"DP03587r002","statement":[{"text":"In NmeE365Term (PDB entry 3RMJ), each monomer comprised residues 1−364 of the full-length protein, with residues 4−296 and 311−324 being modeled for chain A and residues 4−297 and 311−324 for chain B; no interpretable electron density could be found for the remaining residues, which were presumed to be disordered.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:47:17.436Z"}}],"regions_counter":2,"released":"2023_12","sequence":"MTQTNRVIIFDTTLRDGEQSPGAAMTKEEKIRVARQLEKLGVDIIEAGFAAASPGDFEAVNAIAKTITKSTVCSLSRAIERDIRQAGEAVAPAPKKRIHTFIATSPIHMEYKLKMKPKQVIEAAVKAVKIAREYTDDVEFSCEDALRSEIDFLAEICGAVIEAGATTINIPDTVGYSIPYKTEEFFRELIAKTPNGGKVVWSAHCHNDLGLAVANSLAALKGGARQVECTVNGLGERAGNASVEEIVMALKVRHDLFGLETGIDTTQIVPSSKLVSTITGYPVQPNKAIVGANAFSHESGIHQDGVLKHRETYEIMSAESVGWATNRLSLGKLSGRNAFKTKLADLGIELESEEALNAAFARFKELADKKREIFDEDLHALVSDEMGSMNAESYKFISQKISTETGEEPRADIVFSIKGEEKRASATGSGPVDAIFKAIESVAQSGAALQIYSVNAVTQGTESQGETSVRLARGNRVVNGQGADTDVLVATAKAYLSALSKLEFSAAKPKAQGSGTI","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"genes":[{"name":{"value":"leuA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01025","url":"https://hamap.expasy.org/unirule/MF_01025"}}]},"olnNames":[{"value":"NMB1070"}]}],"alphafold_very_low_content":0.03868471953578337,"disorder_content":0.10251450676982592,"disprot_consensus":{"full":[{"start":298,"end":310,"type":"D"},{"start":325,"end":364,"type":"D"}],"Structural state":[{"start":298,"end":310,"type":"D"},{"start":325,"end":364,"type":"D"}]}},{"disprot_id":"DP03588","acc":"Q96C86","creator":"vacs","date":"2022-01-25T12:17:52.434Z","features":{"pfam":[{"id":"PF05652","name":"Scavenger mRNA decapping enzyme (DcpS) N-terminal","start":45,"end":146},{"id":"PF11969","name":"Scavenger mRNA decapping enzyme C-term binding","start":174,"end":292}],"gene3D":[]},"length":337,"name":"m7GpppX diphosphatase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":37,"reference_id":"15769464","reference_source":"pmid","reference_html":"Crystal structures of human DcpS in ligand-free and m7GDP-bound forms suggest a dynamic mechanism for scavenger mRNA decapping. <i> Chen N, Walsh MA, Liu Y, Parker R, Song H. </i> J Mol Biol, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":1,"cross_refs":[{"db":"PDB","id":"1XMM"},{"db":"PDB","id":"1XML"}],"region_id":"DP03588r001","statement":[{"text":"In the structure of apo-DcpS, residues 1–39, 71–76, 286–293 and 337 for protomer A, and residues 1–39, 70–77, 286–292 and 337 for protomer B were not modeled, as these regions are not visible in the electron density map and are assumed to be disordered. In the structure of m7GDP-DcpS, residues 1–39, 69–77, 111, and 337 for chain A, residues 1–39, 70–78, and 337 for chain B, residues 1–38, 68–76, and 337 for chain C, and residues 1–37, 71–74, 99–101, and 110 for chain D are assumed to be disordered, as interpretable electron densities are not observed for these regions.","type":"Results"},{"text":"Region 1-37 is disordered in all structures.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-07T10:43:00.977Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_06","sequence":"MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"DCPS"},"synonyms":[{"value":"DCS1"},{"value":"HINT5"}],"orfNames":[{"value":"HSPC015"}]}],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.10682492581602374,"disorder_content":0.10979228486646884,"disprot_consensus":{"full":[{"start":1,"end":37,"type":"D"}],"Structural state":[{"start":1,"end":37,"type":"D"}]}},{"disprot_id":"DP03589","acc":"P47897","creator":"vacs","date":"2022-01-25T14:48:06.997Z","features":{"pfam":[{"id":"PF00749","name":"tRNA synthetases class I (E and Q), catalytic domain","start":263,"end":562},{"id":"PF03950","name":"tRNA synthetases class I (E and Q), anti-codon binding domain","start":565,"end":665},{"id":"PF04557","name":"Glutaminyl-tRNA synthetase, non-specific RNA binding region part 2","start":165,"end":254},{"id":"PF04558","name":"Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1","start":7,"end":162},{"id":"PF20974","name":"tRNA synthetases class I (E and Q), anti-codon binding domain","start":677,"end":752}],"gene3D":[]},"length":775,"name":"Glutamine--tRNA ligase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":183,"end":216,"reference_id":"26869582","reference_source":"pmid","reference_html":"The crystal structure of human GlnRS provides basis for the development of neurological disorders. <i> Ognjenović J, Wu J, Matthies D, Baxa U, Subramaniam S, Ling J, Simonović M. </i> Nucleic Acids Res, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":1,"cross_refs":[{"db":"PDB","id":"4YE6"},{"db":"PDB","id":"4YE9"},{"db":"PDB","id":"4YE8"}],"region_id":"DP03589r001","statement":[{"text":"One boomerang wing is composed of an appended NTD (residues 1–182) that is linked to the second wing by a long and flexible hinge domain. An 8-helical bundle (N1) and a 3-helical tail (N2) form a bi-lobed structure of NTD that protrudes from the enzyme body. An 82-residue long hinge connects the N2 subdomain to the catalytic domain (CATD; residues 264–335 and 438–564). While the first part of the hinge, covering residues 183–216, is disordered, the second part adopts a predominantly - helical structure that intimately interacts with CATD (Figure 1A).","type":"Results"},{"text":"Next, we compared structures of other domains in hGlnRS. Because of the partial disorder in our crystal form, we excluded the hinge domain from our analysis.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-07T10:46:14.326Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":183,"end":216,"reference_id":"26869582","reference_source":"pmid","reference_html":"The crystal structure of human GlnRS provides basis for the development of neurological disorders. <i> Ognjenović J, Wu J, Matthies D, Baxa U, Subramaniam S, Ling J, Simonović M. </i> Nucleic Acids Res, 2016","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":1,"region_id":"DP03589r002","statement":[{"text":"One boomerang wing is composed of an appended NTD (residues 1–182) that is linked to the second wing by a long and flexible hinge domain. An 8-helical bundle (N1) and a 3-helical tail (N2) form a bi-lobed structure of NTD that protrudes from the enzyme body. An 82-residue long hinge connects the N2 subdomain to the catalytic domain (CATD; residues 264–335 and 438–564). While the first part of the hinge, covering residues 183–216, is disordered, the second part adopts a predominantly - helical structure that intimately interacts with CATD (Figure 1A).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-07T10:46:15.375Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":2,"released":"2023_06","sequence":"MAALDSLSLFTSLGLSEQKARETLKNSALSAQLREAATQAQQTLGSTIDKATGILLYGLASRLRDTRRLSFLVSYIASKKIHTEPQLSAALEYVRSHPLDPIDTVDFERECGVGVIVTPEQIEEAVEAAINRHRPQLLVERYHFNMGLLMGEARAVLKWADGKMIKNEVDMQVLHLLGPKLEADLEKKFKVAKARLEETDRRTAKDVVENGETADQTLSLMEQLRGEALKFHKPGENYKTPGYVVTPHTMNLLKQHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYTPYKVTYASDYFDQLYAWAVELIRRGLAYVCHQRGEELKGHNTLPSPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVMEDGKMDPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPVQWEYGRLNLHYAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPRAMAVLESLRVIITNFPAAKSLDIQVPNFPADETKGFHQVPFAPIVFIERTDFKEEPEPGFKRLAWGQPVGLRHTGYVIELQHVVKGPSGCVESLEVTCRRADAGEKPKAFIHWVSQPLMCEVRLYERLFQHKNPEDPTEVPGGFLSDLNLASLHVVDAALVDCSVALAKPFDKFQFERLGYFSVDPDSHQGKLVFNRTVTLKEDPGKV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"QARS1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9751","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9751"}}]},"synonyms":[{"value":"QARS"}]}],"dataset":["NDDs-related proteins","RNA-binding proteins"],"alphafold_very_low_content":0.03870967741935484,"disorder_content":0.04387096774193548,"disprot_consensus":{"full":[{"start":183,"end":216,"type":"D"}],"Structural state":[{"start":183,"end":216,"type":"D"}],"Disorder function":[{"start":183,"end":216,"type":"F"}]}},{"disprot_id":"DP03590","acc":"B2RLE7","creator":"fquaglia","date":"2022-01-27T09:40:16.631Z","features":{"pfam":[{"id":"PF19841","name":"Gliding motility associated protein GldN","start":63,"end":291}],"gene3D":[]},"length":359,"name":"Por secretion system protein porN/gldN","ncbi_taxon_id":431947,"organism":"Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)","regions":[{"start":23,"end":54,"reference_id":"35065963","reference_source":"pmid","reference_html":"Structural and functional analyses of the Porphyromonas gingivalis type IX secretion system PorN protein. <i> Fuchsbauer O, Lunar Silva I, Cascales E, Roussel A, Leone P. </i> J Biol Chem, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03590r001","statement":[{"text":"In agreement with in silico analyses, we also found that the N- and C-terminal regions of PorN are intrinsically disordered.","type":"Abstract"},{"text":"PorN presents N- and C-terminal intrinsically disordered regions","type":"Results"},{"text":"Edman sequencing of PorNP-G revealed that the protease resistant folded domain starts at residue 55, and the molecular mass (24,949Da) obtained by mass spectrometry suggested that it ends at residue 265.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-17T15:31:01.364Z"}},{"start":266,"end":359,"reference_id":"35065963","reference_source":"pmid","reference_html":"Structural and functional analyses of the Porphyromonas gingivalis type IX secretion system PorN protein. <i> Fuchsbauer O, Lunar Silva I, Cascales E, Roussel A, Leone P. </i> J Biol Chem, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03590r002","statement":[{"text":"In agreement with in silico analyses, we also found that the N- and C-terminal regions of PorN are intrinsically disordered.","type":"Abstract"},{"text":"PorN presents N- and C-terminal intrinsically disordered regions","type":"Results"},{"text":"Edman sequencing of PorNP-G revealed that the protease resistant folded domain starts at residue 55, and the molecular mass (24,949Da) obtained by mass spectrometry suggested that it ends at residue 265.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-17T15:31:06.304Z"}},{"start":23,"end":54,"reference_id":"35065963","reference_source":"pmid","reference_html":"Structural and functional analyses of the Porphyromonas gingivalis type IX secretion system PorN protein. <i> Fuchsbauer O, Lunar Silva I, Cascales E, Roussel A, Leone P. </i> J Biol Chem, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"interaction_partner":[{"db":"UniProt","id":"B2RLE7","partner_start":null,"partner_end":null}],"region_id":"DP03590r003","statement":[{"text":"Our functional studies showed that the N-terminal disordered region is involved in PorN dimerization while the C-terminal disordered region is involved in the interaction with PorK.","type":"Abstract"},{"text":"Our results show that PorNP and PorNΔC oligomerize but not PorNΔN nor PorNΔNΔC (Fig. 3A), suggesting that the N-terminal region is required for PorN oligomerization. This result was confirmed in vitro. The different PorN constructs, fused to an N-terminal His6 tag, were purified by metal affinity chromatography and gel filtration, and subjected to SEC-MALS experiments. Figure 2 shows that PorNP and PorNΔC are dimeric in solution, whereas, similarly to PorNΔNΔC, PorNΔN is monomeric (Fig. 2). Taken together, the in vivo and in vitro assays demonstrate that PorN dimer formation is mediated by the N-terminal intrinsically disordered region.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-17T15:31:32.429Z"}},{"start":266,"end":358,"reference_id":"35065963","reference_source":"pmid","reference_html":"Structural and functional analyses of the Porphyromonas gingivalis type IX secretion system PorN protein. <i> Fuchsbauer O, Lunar Silva I, Cascales E, Roussel A, Leone P. </i> J Biol Chem, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0007074","ec_ontology":"ECO","ec_name":"bacterial 2-hybrid assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"interaction_partner":[{"db":"UniProt","id":"B2RLF0","partner_start":null,"partner_end":null}],"region_id":"DP03590r004","statement":[{"text":"Our functional studies showed that the N-terminal disordered region is involved in PorN dimerization while the C-terminal disordered region is involved in the interaction with PorK.","type":"Abstract"},{"text":"In addition, all PorN constructs interact with the CTDs of T9SS substrates (Fig. 3C). These results demonstrate that the PorN C-terminal disordered region is required for the interaction with PorK, whereas the PorN central core is sufficient to mediate contacts with PorM and the CTDs.","type":"Results"}],"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-17T15:31:28.992Z"}}],"regions_counter":4,"released":"2023_12","sequence":"MKVFKAVIGAILAATVSIPSVAQENTNNRSPQVGRAPRNTEVEQMTTLSNRAQEFNRRLTQKTDNAPWRRVVYRRVDLMEESNAVLYYPPRPIGDRKNLFSTIFGLINSNSLDVYEYLDGFEAFTDQYKIKFQEFLDRFGIYYQPSTNKNAELFKVADSDIPSAEVKAYYVKEEWYFTPTNSDVDIKIQAICPIMTGQDEFGEVRNQPLFWIPYENIRPYIARERVMLSSLNNTRNSTIDDFFRLNLYKGDIVKTENLHNRALAEYCPTPDSMKMESKRIDKELQGFRDGLFVTQDTTWMKQVETKKSKGKKLEKARGKNITSRTRGQGEGAAETEAVEPKKQKASKNKAATRSVRRRK","taxonomy":["Bacteria","Bacteroidetes","Bacteroidia","Bacteroidales","Porphyromonadaceae","Porphyromonas"],"genes":[{"name":{"value":"porN","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAG34192.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAG34192.1"}}]},"olnNames":[{"value":"PGN_1673","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAG34192.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAG34192.1"}}]}]}],"alphafold_very_low_content":0.24233983286908078,"disorder_content":0.35097493036211697,"disprot_consensus":{"full":[{"start":23,"end":54,"type":"D"},{"start":266,"end":359,"type":"D"}],"Structural state":[{"start":23,"end":54,"type":"D"},{"start":266,"end":359,"type":"D"}],"Molecular function":[{"start":23,"end":54,"type":"F"},{"start":266,"end":358,"type":"F"}]}},{"disprot_id":"DP03591","acc":"P38238","creator":"vacs","date":"2022-01-27T13:57:44.407Z","features":{"pfam":[{"id":"PF01728","name":"FtsJ-like methyltransferase","start":21,"end":207}],"gene3D":[]},"length":310,"name":"tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":213,"end":232,"reference_id":"31586407","reference_source":"pmid","reference_html":"Structure of tRNA methyltransferase complex of Trm7 and Trm734 reveals a novel binding interface for tRNA recognition. <i> Hirata A, Okada K, Yoshii K, Shiraishi H, Saijo S, Yonezawa K, Shimizu N, Hori H. </i> Nucleic Acids Res, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"6JPL"},{"db":"PDB","id":"6JP6"}],"region_id":"DP03591r001","statement":[{"text":"The final model of apo-Trm7–Trm734 contained residues [Trm7 (chain B and D), 9–212 and 233– 259; Trm734 (chain A and C), 1–547, 555–758, 763–992, 997–1013], 310 water molecules, four SO42- molecules and two HEPES molecules, and the Trm7–Trm734–SAM complex contained residues [Trm7 (chain B and D), 9–212 and 233–259; Trm734 (chain A and C), 1–547, 555–758, 763– 992, 997–1013], 511 water molecules, 2 SAM molecules, 10 SO42- molecules and 2 HEPES molecules.","type":"Methods"},{"text":"A structural model of two C-terminal regions of Trm7, W213- L232 and L260-V310, could not be built as these regions were not visible in the electron density (Figure 2B).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-07T10:53:34.882Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":260,"end":310,"reference_id":"31586407","reference_source":"pmid","reference_html":"Structure of tRNA methyltransferase complex of Trm7 and Trm734 reveals a novel binding interface for tRNA recognition. <i> Hirata A, Okada K, Yoshii K, Shiraishi H, Saijo S, Yonezawa K, Shimizu N, Hori H. </i> Nucleic Acids Res, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"6JPL"},{"db":"PDB","id":"6JP6"}],"region_id":"DP03591r002","statement":[{"text":"The final model of apo-Trm7–Trm734 contained residues [Trm7 (chain B and D), 9–212 and 233– 259; Trm734 (chain A and C), 1–547, 555–758, 763–992, 997–1013], 310 water molecules, four SO42- molecules and two HEPES molecules, and the Trm7–Trm734–SAM complex contained residues [Trm7 (chain B and D), 9–212 and 233–259; Trm734 (chain A and C), 1–547, 555–758, 763– 992, 997–1013], 511 water molecules, 2 SAM molecules, 10 SO42- molecules and 2 HEPES molecules.","type":"Methods"},{"text":"A structural model of two C-terminal regions of Trm7, W213- L232 and L260-V310, could not be built as these regions were not visible in the electron density (Figure 2B). The C-terminal region of L260-V310 was not degraded by contaminating proteases during the crystallization because we confirmed by SDS-PAGE analysis that Trm7 in the crystals retained its full length (data not shown). Therefore, the Cterminal region of Trm7 is disordered and likely to reside in the large space (Supplementary Figure S4).","type":"Results"},{"text":"The role of the disordered region (L260-V310) in Trm7 remains unclear because the region is invisible.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-07T10:53:33.691Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":260,"end":310,"reference_id":"31586407","reference_source":"pmid","reference_html":"Structure of tRNA methyltransferase complex of Trm7 and Trm734 reveals a novel binding interface for tRNA recognition. <i> Hirata A, Okada K, Yoshii K, Shiraishi H, Saijo S, Yonezawa K, Shimizu N, Hori H. </i> Nucleic Acids Res, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"SASBDB","id":"SASDDR3"}],"region_id":"DP03591r003","statement":[{"text":"We next performed SAXS analysis to confirm the Trm7–Trm734 heterodimeric complex structure in solution. As shown in Figure 2C, the structural model of Trm7–Trm734 with randomized loops (L260-V310) in the C-terminal Trm7 is superimposed well onto the envelope shape of the solution model generated from SAXS analysis, with good  2 and normalized spatial discrepancy (NSD) values (2.18 and 1.92, Supplementary Figure S5 and Table S4). Thus, these results confirm the heterodimer of the Trm7–Trm734 complex structure in solution as well as in the crystal and suggest the presence of a disordered C-terminal region (L260-V310) of Trm7.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-07T10:53:31.827Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2023_12","sequence":"MGKSSKDKRDLYYRKAKEQGYRARSAFKLLQLNDQFHFLDDPNLKRVVDLCAAPGSWSQVLSRKLFDESPSSDKEDRKIVSVDLQPMSPIPHVTTLQADITHPKTLARILKLFGNEKADFVCSDGAPDVTGLHDLDEYVQQQLIMSALQLTACILKKGGTFVAKIFRGRDIDMLYSQLGYLFDKIVCAKPRSSRGTSLEAFIVCLGYNPPSNWTPKLDVNTSVDEFFQGCFLNKLCISDKLSHWNEEERNIAEFMACGSLQSFDSDATYHDLPSSVAGTSSSLDPVQSPTNPPYKKALELKRSGKLTRSV","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"genes":[{"name":{"value":"TRM7","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03162","url":"https://hamap.expasy.org/unirule/MF_03162"}}]},"orfNames":[{"value":"YBR0527"}],"olnNames":[{"value":"YBR061C"}]}],"alphafold_very_low_content":0.02258064516129032,"disorder_content":0.22903225806451613,"disprot_consensus":{"full":[{"start":213,"end":232,"type":"D"},{"start":260,"end":310,"type":"D"}],"Structural state":[{"start":213,"end":232,"type":"D"},{"start":260,"end":310,"type":"D"}]}},{"disprot_id":"DP03592","acc":"P03317","creator":"fquaglia","date":"2022-01-27T16:03:31.747Z","features":{"pfam":[{"id":"PF00978","name":"RNA dependent RNA polymerase","start":2054,"end":2500},{"id":"PF01443","name":"Viral superfamily 1 RNA helicase core domain","start":724,"end":965},{"id":"PF01660","name":"Viral methyltransferase","start":23,"end":377},{"id":"PF01661","name":"Macro domain","start":1367,"end":1466},{"id":"PF01707","name":"Peptidase family C9","start":972,"end":1179},{"id":"PF20852","name":"Non-structural protein 3, zinc-binding domain","start":1516,"end":1673},{"id":"PF20896","name":"Tomato mosaic virus helicase, N-terminal domain","start":560,"end":716}],"gene3D":[]},"length":2513,"name":"Polyprotein P1234","ncbi_taxon_id":11034,"organism":"Sindbis virus","regions":[{"start":1994,"end":2006,"reference_id":"35037043","reference_source":"pmid","reference_html":"Crystal structures of alphavirus nonstructural protein 4 (nsP4) reveal an intrinsically dynamic RNA-dependent RNA polymerase fold. <i> Tan YB, Lello LS, Liu X, Law YS, Kang C, Lescar J, Zheng J, Merits A, Luo D. </i> Nucleic Acids Res, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":1,"cross_refs":[{"db":"PDB","id":"7VB4"}],"region_id":"DP03592r001","statement":[{"text":"Here, we report crystal structures of alphavirus RdRp from both RRV and SINV determined at 2.6 Å and 1.9 Å resolution respectively (Table 1). Having a dynamic structure, the RRV RdRp contains several disordered segments and some electron density in the RNA binding tunnel remains unassigned. The SINV RdRp adopts an overall fold similar to RRV RdRp but appears more ordered: residues that were disordered in the RRV nsP4 crystal structure are now well resolved in SINV RdRp and almost fully occupy the central RNA binding tunnel.","type":"Introduction"},{"text":"Conversely, missing residues in SINV RdRp are located in N-terminal fingertips (index residues 91–103, flex residues 167–178, pinky residues 206–210, and ring residues 288–307) and C-terminus residues (residues 603–611) (Figure 2). The relatively large number of missing residues of the RRV RdRp structure suggests a highly dynamic structure which is also detected in the HDX measurement (see below, Figure 2).","type":"Results"},{"text":"SINV nsP4FL corresponds to region 1904-2513 while its RdRp domain corresponds to region 1994-2513. This evidence annotates the N-terminal fingertip: 1994-2006.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-06T11:13:01.088Z"}},{"start":2070,"end":2081,"reference_id":"35037043","reference_source":"pmid","reference_html":"Crystal structures of alphavirus nonstructural protein 4 (nsP4) reveal an intrinsically dynamic RNA-dependent RNA polymerase fold. <i> Tan YB, Lello LS, Liu X, Law YS, Kang C, Lescar J, Zheng J, Merits A, Luo D. </i> Nucleic Acids Res, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":1,"cross_refs":[{"db":"PDB","id":"7VB4"}],"region_id":"DP03592r002","statement":[{"text":"Here, we report crystal structures of alphavirus RdRp from both RRV and SINV determined at 2.6 Å and 1.9 Å resolution respectively (Table 1). Having a dynamic structure, the RRV RdRp contains several disordered segments and some electron density in the RNA binding tunnel remains unassigned. The SINV RdRp adopts an overall fold similar to RRV RdRp but appears more ordered: residues that were disordered in the RRV nsP4 crystal structure are now well resolved in SINV RdRp and almost fully occupy the central RNA binding tunnel.","type":"Introduction"},{"text":"Conversely, missing residues in SINV RdRp are located in N-terminal fingertips (index residues 91–103, flex residues 167–178, pinky residues 206–210, and ring residues 288–307) and C-terminus residues (residues 603–611) (Figure 2). The relatively large number of missing residues of the RRV RdRp structure suggests a highly dynamic structure which is also detected in the HDX measurement (see below, Figure 2).","type":"Results"},{"text":"SINV nsP4FL corresponds to region 1904-2513 while its RdRp domain corresponds to region 1994-2513. This evidence annotates the flex residues: 2070-2081.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-06T11:13:02.285Z"}},{"start":2191,"end":2210,"reference_id":"35037043","reference_source":"pmid","reference_html":"Crystal structures of alphavirus nonstructural protein 4 (nsP4) reveal an intrinsically dynamic RNA-dependent RNA polymerase fold. <i> Tan YB, Lello LS, Liu X, Law YS, Kang C, Lescar J, Zheng J, Merits A, Luo D. </i> Nucleic Acids Res, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":1,"cross_refs":[{"db":"PDB","id":"7VB4"}],"region_id":"DP03592r003","statement":[{"text":"Here, we report crystal structures of alphavirus RdRp from both RRV and SINV determined at 2.6 Å and 1.9 Å resolution respectively (Table 1). Having a dynamic structure, the RRV RdRp contains several disordered segments and some electron density in the RNA binding tunnel remains unassigned. The SINV RdRp adopts an overall fold similar to RRV RdRp but appears more ordered: residues that were disordered in the RRV nsP4 crystal structure are now well resolved in SINV RdRp and almost fully occupy the central RNA binding tunnel.","type":"Introduction"},{"text":"Conversely, missing residues in SINV RdRp are located in N-terminal fingertips (index residues 91–103, flex residues 167–178, pinky residues 206–210, and ring residues 288–307) and C-terminus residues (residues 603–611) (Figure 2). The relatively large number of missing residues of the RRV RdRp structure suggests a highly dynamic structure which is also detected in the HDX measurement (see below, Figure 2).","type":"Results"},{"text":"SINV nsP4FL corresponds to region 1904-2513 while its RdRp domain corresponds to region 1994-2513. This evidence annotates the ring residues: 2191-2210.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-06T11:13:03.402Z"}},{"start":1989,"end":2022,"reference_id":"35037043","reference_source":"pmid","reference_html":"Crystal structures of alphavirus nonstructural protein 4 (nsP4) reveal an intrinsically dynamic RNA-dependent RNA polymerase fold. <i> Tan YB, Lello LS, Liu X, Law YS, Kang C, Lescar J, Zheng J, Merits A, Luo D. </i> Nucleic Acids Res, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_12","version":1,"region_id":"DP03592r004","statement":[{"text":"A high percentage of deuteration (D%; hydrogen exchanged to deuterium) reflects the high solvent accessibility and flexibility of the regions on RRV and SINV nsP4.","type":"Results"},{"text":"SINV nsP4FL corresponds to region 1904-2513 while its RdRp domain corresponds to region 1994-2513.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-06T11:13:04.453Z"}},{"start":1906,"end":1958,"reference_id":"35037043","reference_source":"pmid","reference_html":"Crystal structures of alphavirus nonstructural protein 4 (nsP4) reveal an intrinsically dynamic RNA-dependent RNA polymerase fold. <i> Tan YB, Lello LS, Liu X, Law YS, Kang C, Lescar J, Zheng J, Merits A, Luo D. </i> Nucleic Acids Res, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_12","version":1,"region_id":"DP03592r005","statement":[{"text":"A high percentage of deuteration (D%; hydrogen exchanged to deuterium) reflects the high solvent accessibility and flexibility of the regions on RRV and SINV nsP4.","type":"Results"},{"text":"SINV nsP4FL corresponds to region 1904-2513 while its RdRp domain corresponds to region 1994-2513.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-06T11:13:05.921Z"}},{"start":2053,"end":2125,"reference_id":"35037043","reference_source":"pmid","reference_html":"Crystal structures of alphavirus nonstructural protein 4 (nsP4) reveal an intrinsically dynamic RNA-dependent RNA polymerase fold. <i> Tan YB, Lello LS, Liu X, Law YS, Kang C, Lescar J, Zheng J, Merits A, Luo D. </i> Nucleic Acids Res, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_12","version":1,"region_id":"DP03592r006","statement":[{"text":"A high percentage of deuteration (D%; hydrogen exchanged to deuterium) reflects the high solvent accessibility and flexibility of the regions on RRV and SINV nsP4.","type":"Results"},{"text":"SINV nsP4FL corresponds to region 1904-2513 while its RdRp domain corresponds to region 1994-2513.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-06T11:13:07.468Z"}}],"regions_counter":6,"released":"2022_12","sequence":"MEKPVVNVDVDPQSPFVVQLQKSFPQFEVVAQQVTPNDHANARAFSHLASKLIELEVPTTATILDIGSAPARRMFSEHQYHCVCPMRSPEDPDRMMKYASKLAEKACKITNKNLHEKIKDLRTVLDTPDAETPSLCFHNDVTCNMRAEYSVMQDVYINAPGTIYHQAMKGVRTLYWIGFDTTQFMFSAMAGSYPAYNTNWADEKVLEARNIGLCSTKLSEGRTGKLSIMRKKELKPGSRVYFSVGSTLYPEHRASLQSWHLPSVFHLNGKQSYTCRCDTVVSCEGYVVKKITISPGITGETVGYAVTHNSEGFLLCKVTDTVKGERVSFPVCTYIPATICDQMTGIMATDISPDDAQKLLVGLNQRIVINGRTNRNTNTMQNYLLPIIAQGFSKWAKERKDDLDNEKMLGTRERKLTYGCLWAFRTKKVHSFYRPPGTQTCVKVPASFSAFPMSSVWTTSLPMSLRQKLKLALQPKKEEKLLQVSEELVMEAKAAFEDAQEEARAEKLREALPPLVADKGIEAAAEVVCEVEGLQADIGAALVETPRGHVRIIPQANDRMIGQYIVVSPNSVLKNAKLAPAHPLADQVKIITHSGRSGRYAVEPYDAKVLMPAGGAVPWPEFLALSESATLVYNEREFVNRKLYHIAMHGPAKNTEEEQYKVTKAELAETEYVFDVDKKRCVKKEEASGLVLSGELTNPPYHELALEGLKTRPAVPYKVETIGVIGTPGSGKSAIIKSTVTARDLVTSGKKENCREIEADVLRLRGMQITSKTVDSVMLNGCHKAVEVLYVDEAFACHAGALLALIAIVRPRKKVVLCGDPMQCGFFNMMQLKVHFNHPEKDICTKTFYKYISRRCTQPVTAIVSTLHYDGKMKTTNPCKKNIEIDITGATKPKPGDIILTCFRGWVKQLQIDYPGHEVMTAAASQGLTRKGVYAVRQKVNENPLYAITSEHVNVLLTRTEDRLVWKTLQGDPWIKQPTNIPKGNFQATIEDWEAEHKGIIAAINSPTPRANPFSCKTNVCWAKALEPILATAGIVLTGCQWSELFPQFADDKPHSAIYALDVICIKFFGMDLTSGLFSKQSIPLTYHPADSARPVAHWDNSPGTRKYGYDHAIAAELSRRFPVFQLAGKGTQLDLQTGRTRVISAQHNLVPVNRNLPHALVPEYKEKQPGPVKKFLNQFKHHSVLVVSEEKIEAPRKRIEWIAPIGIAGADKNYNLAFGFPPQARYDLVFINIGTKYRNHHFQQCEDHAATLKTLSRSALNCLNPGGTLVVKSYGYADRNSEDVVTALARKFVRVSAARPDCVSSNTEMYLIFRQLDNSRTRQFTPHHLNCVISSVYEGTRDGVGAAPSYRTKRENIADCQEEAVVNAANPLGRPGEGVCRAIYKRWPTSFTDSATETGTARMTVCLGKKVIHAVGPDFRKHPEAEALKLLQNAYHAVADLVNEHNIKSVAIPLLSTGIYAAGKDRLEVSLNCLTTALDRTDADVTIYCLDKKWKERIDAALQLKESVTELKDEDMEIDDELVWIHPDSCLKGRKGFSTTKGKLYSYFEGTKFHQAAKDMAEIKVLFPNDQESNEQLCAYILGETMEAIREKCPVDHNPSSSPPKTLPCLCMYAMTPERVHRLRSNNVKEVTVCSSTPLPKHKIKNVQKVQCTKVVLFNPHTPAFVPARKYIEVPEQPTAPPAQAEEAPEVVATPSPSTADNTSLDVTDISLDMDDSSEGSLFSSFSGSDNSITSMDSWSSGPSSLEIVDRRQVVVADVHAVQEPAPIPPPRLKKMARLAAARKEPTPPASNSSESLHLSFGGVSMSLGSIFDGETARQAAVQPLATGPTDVPMSFGSFSDGEIDELSRRVTESEPVLFGSFEPGEVNSIISSRSAVSFPLRKQRRRRRSRRTEYXLTGVGGYIFSTDTGPGHLQKKSVLQNQLTEPTLERNVLERIHAPVLDTSKEEQLKLRYQMMPTEANKSRYQSRKVENQKAITTERLLSGLRLYNSATDQPECYKITYPKPLYSSSVPANYSDPQFAVAVCNNYLHENYPTVASYQITDEYDAYLDMVDGTVACLDTATFCPAKLRSYPKKHEYRAPNIRSAVPSAMQNTLQNVLIAATKRNCNVTQMRELPTLDSATFNVECFRKYACNDEYWEEFARKPIRITTEFVTAYVARLKGPKAAALFAKTYNLVPLQEVPMDRFVMDMKRDVKVTPGTKHTEERPKVQVIQAAEPLATAYLCGIHRELVRRLTAVLLPNIHTLFDMSAEDFDAIIAEHFKQGDPVLETDIASFDKSQDDAMALTGLMILEDLGVDQPLLDLIECAFGEISSTHLPTGTRFKFGAMMKSGMFLTLFVNTVLNVVIASRVLEERLKTSRCAAFIGDDNIIHGVVSDKEMAERCATWLNMEVKIIDAVIGERPPYFCGGFILQDSVTSTACRVADPLKRLFKLGKPLPADDEQDEDRRRALLDETKAWFRVGITGTLAVAVTTRYEVDNITPVLLALRTFAQSKRAFQAIRGEIKHLYGGPK","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Alsuviricetes","Martellivirales","Togaviridae","Alphavirus"],"dataset":["Viral proteins","RNA-binding proteins"],"genes":[],"disorder_content":0.07162753680859531,"disprot_consensus":{"full":[{"start":1906,"end":1958,"type":"D"},{"start":1989,"end":2022,"type":"D"},{"start":2053,"end":2125,"type":"D"},{"start":2191,"end":2210,"type":"D"}],"Structural state":[{"start":1906,"end":1958,"type":"D"},{"start":1989,"end":2022,"type":"D"},{"start":2053,"end":2125,"type":"D"},{"start":2191,"end":2210,"type":"D"}]}},{"disprot_id":"DP03593","acc":"P13887","creator":"fquaglia","date":"2022-01-28T09:00:10.857Z","features":{"pfam":[{"id":"PF00978","name":"RNA dependent RNA polymerase","start":2021,"end":2467},{"id":"PF01443","name":"Viral superfamily 1 RNA helicase core domain","start":717,"end":955},{"id":"PF01660","name":"Viral methyltransferase","start":16,"end":376},{"id":"PF01661","name":"Macro domain","start":1351,"end":1454},{"id":"PF01707","name":"Peptidase family C9","start":962,"end":1162},{"id":"PF20852","name":"Non-structural protein 3, zinc-binding domain","start":1499,"end":1656},{"id":"PF20896","name":"Tomato mosaic virus helicase, N-terminal domain","start":553,"end":709}],"gene3D":[]},"length":2480,"name":"Polyprotein P1234","ncbi_taxon_id":11031,"organism":"Ross river virus (strain NB5092)","regions":[{"start":2004,"end":2053,"reference_id":"35037043","reference_source":"pmid","reference_html":"Crystal structures of alphavirus nonstructural protein 4 (nsP4) reveal an intrinsically dynamic RNA-dependent RNA polymerase fold. <i> Tan YB, Lello LS, Liu X, Law YS, Kang C, Lescar J, Zheng J, Merits A, Luo D. </i> Nucleic Acids Res, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":1,"cross_refs":[{"db":"PDB","id":"7F0S"}],"region_id":"DP03593r001","statement":[{"text":"Here, we report crystal structures of alphavirus RdRp from both RRV and SINV determined at 2.6 Å and 1.9 Å resolution respectively (Table 1). Having a dynamic structure, the RRV RdRp contains several disordered segments and some electron density in the RNA binding tunnel remains unassigned. The SINV RdRp adopts an overall fold similar to RRV RdRp but appears more ordered: residues that were disordered in the RRV nsP4 crystal structure are now well resolved in SINV RdRp and almost fully occupy the central RNA binding tunnel.","type":"Introduction"},{"text":"The 83 mobile residues in RRV RdRp belong to the N-terminal fingertips and C-terminal thumb subdomains: index finger (residues 135–184; this flexible region is denoted as ‘flex’ region hereafter) (Figures 1, 2A, Supplementary Figures S2C and S3C), pinky, and ring fingers (residues 210–213 and 292–307, respectively) (Figure 2A and Supplementary Figure S2A), and C-terminus of the protein (residues 575–578, 588–593 and 600–611) (Figure 2A and Supplementary Figure S2B).","type":"Results"},{"text":"RRV nsP4FL corresponds to region 1870-2479 (NTD: 1870-1978; RdRP: 1979-2479). This evidence annotates the index finger (‘flex’ region): 2004–2053.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-06T11:13:30.187Z"}},{"start":2161,"end":2176,"reference_id":"35037043","reference_source":"pmid","reference_html":"Crystal structures of alphavirus nonstructural protein 4 (nsP4) reveal an intrinsically dynamic RNA-dependent RNA polymerase fold. <i> Tan YB, Lello LS, Liu X, Law YS, Kang C, Lescar J, Zheng J, Merits A, Luo D. </i> Nucleic Acids Res, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":1,"cross_refs":[{"db":"PDB","id":"7F0S"}],"region_id":"DP03593r002","statement":[{"text":"Here, we report crystal structures of alphavirus RdRp from both RRV and SINV determined at 2.6 Å and 1.9 Å resolution respectively (Table 1). Having a dynamic structure, the RRV RdRp contains several disordered segments and some electron density in the RNA binding tunnel remains unassigned. The SINV RdRp adopts an overall fold similar to RRV RdRp but appears more ordered: residues that were disordered in the RRV nsP4 crystal structure are now well resolved in SINV RdRp and almost fully occupy the central RNA binding tunnel.","type":"Introduction"},{"text":"The 83 mobile residues in RRV RdRp belong to the N-terminal fingertips and C-terminal thumb subdomains: index finger (residues 135–184; this flexible region is denoted as ‘flex’ region hereafter) (Figures 1, 2A, Supplementary Figures S2C and S3C), pinky, and ring fingers (residues 210–213 and 292–307, respectively) (Figure 2A and Supplementary Figure S2A), and C-terminus of the protein (residues 575–578, 588–593 and 600–611) (Figure 2A and Supplementary Figure S2B).","type":"Results"},{"text":"RRV nsP4FL corresponds to region 1870-2479 (NTD: 1870-1978; RdRP: 1979-2479). This evidence annotates the ring finger: 2161–2176.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-06T11:13:31.605Z"}},{"start":2469,"end":2480,"reference_id":"35037043","reference_source":"pmid","reference_html":"Crystal structures of alphavirus nonstructural protein 4 (nsP4) reveal an intrinsically dynamic RNA-dependent RNA polymerase fold. <i> Tan YB, Lello LS, Liu X, Law YS, Kang C, Lescar J, Zheng J, Merits A, Luo D. </i> Nucleic Acids Res, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":1,"cross_refs":[{"db":"PDB","id":"7F0S"}],"region_id":"DP03593r003","statement":[{"text":"Here, we report crystal structures of alphavirus RdRp from both RRV and SINV determined at 2.6 Å and 1.9 Å resolution respectively (Table 1). Having a dynamic structure, the RRV RdRp contains several disordered segments and some electron density in the RNA binding tunnel remains unassigned. The SINV RdRp adopts an overall fold similar to RRV RdRp but appears more ordered: residues that were disordered in the RRV nsP4 crystal structure are now well resolved in SINV RdRp and almost fully occupy the central RNA binding tunnel.","type":"Introduction"},{"text":"The 83 mobile residues in RRV RdRp belong to the N-terminal fingertips and C-terminal thumb subdomains: index finger (residues 135–184; this flexible region is denoted as ‘flex’ region hereafter) (Figures 1, 2A, Supplementary Figures S2C and S3C), pinky, and ring fingers (residues 210–213 and 292–307, respectively) (Figure 2A and Supplementary Figure S2A), and C-terminus of the protein (residues 575–578, 588–593 and 600–611) (Figure 2A and Supplementary Figure S2B).","type":"Results"},{"text":"RRV nsP4FL corresponds to region 1870-2479 (NTD: 1870-1978; RdRP: 1979-2479). This evidence annotates the C-terminus: 2469-2480.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-06T11:13:32.822Z"}},{"start":1870,"end":1922,"reference_id":"35037043","reference_source":"pmid","reference_html":"Crystal structures of alphavirus nonstructural protein 4 (nsP4) reveal an intrinsically dynamic RNA-dependent RNA polymerase fold. <i> Tan YB, Lello LS, Liu X, Law YS, Kang C, Lescar J, Zheng J, Merits A, Luo D. </i> Nucleic Acids Res, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":1,"region_id":"DP03593r004","statement":[{"text":"Based on the high D% HDX profile observed, the NTD of RRV nsP4FL appears quite flexible in solution, except at residues 53–74, where a predicted helix-loop-helix (HLH) substructure is located (Figure 2B–C). The linker between NTD and RdRp appears to have higher D% values, indicating increased dynamics in solution (Figure 2A).","type":"Results"},{"text":"RRV nsP4FL corresponds to region 1870-2479 (NTD: 1870-1978; RdRP: 1979-2479).","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-06T11:13:33.937Z"}},{"start":1943,"end":1978,"reference_id":"35037043","reference_source":"pmid","reference_html":"Crystal structures of alphavirus nonstructural protein 4 (nsP4) reveal an intrinsically dynamic RNA-dependent RNA polymerase fold. <i> Tan YB, Lello LS, Liu X, Law YS, Kang C, Lescar J, Zheng J, Merits A, Luo D. </i> Nucleic Acids Res, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_12","version":1,"region_id":"DP03593r005","statement":[{"text":"Based on the high D% HDX profile observed, the NTD of RRV nsP4FL appears quite flexible in solution, except at residues 53–74, where a predicted helix-loop-helix (HLH) substructure is located (Figure 2B–C). The linker between NTD and RdRp appears to have higher D% values, indicating increased dynamics in solution (Figure 2A).","type":"Results"},{"text":"RRV nsP4FL corresponds to region 1870-2479 (NTD: 1870-1978; RdRP: 1979-2479). This evidence corresponds to the linker between NTD and RdRp.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-06T11:13:35.652Z"}},{"start":1943,"end":1978,"reference_id":"35037043","reference_source":"pmid","reference_html":"Crystal structures of alphavirus nonstructural protein 4 (nsP4) reveal an intrinsically dynamic RNA-dependent RNA polymerase fold. <i> Tan YB, Lello LS, Liu X, Law YS, Kang C, Lescar J, Zheng J, Merits A, Luo D. </i> Nucleic Acids Res, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_12","version":1,"region_id":"DP03593r006","statement":[{"text":"Based on the high D% HDX profile observed, the NTD of RRV nsP4FL appears quite flexible in solution, except at residues 53–74, where a predicted helix-loop-helix (HLH) substructure is located (Figure 2B–C). The linker between NTD and RdRp appears to have higher D% values, indicating increased dynamics in solution (Figure 2A).","type":"Results"},{"text":"RRV nsP4FL corresponds to region 1870-2479 (NTD: 1870-1978; RdRP: 1979-2479). This evidence corresponds to the linker between NTD and RdRp.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-06T11:13:25.997Z"}},{"start":1943,"end":1978,"reference_id":"35037043","reference_source":"pmid","reference_html":"Crystal structures of alphavirus nonstructural protein 4 (nsP4) reveal an intrinsically dynamic RNA-dependent RNA polymerase fold. <i> Tan YB, Lello LS, Liu X, Law YS, Kang C, Lescar J, Zheng J, Merits A, Luo D. </i> Nucleic Acids Res, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":1,"region_id":"DP03593r007","statement":[{"text":"Given its low molecular mass of 12.6 kDa, the recombinant NTD is amenable to structural characterization via NMR in solution. The NTD selected from RRV contains 107 amino acids with an expected number of 99 cross-peaks (excluding Pro residues) in the 1H-15N-HSQC spectrum. From these, ∼60 cross-peaks could be observed, making backbone resonance assignments challenging (Supplementary Figure S6). The narrow dispersion of the cross-peaks in the spectrum suggests that the NTD contains flexible and helical regions that support the NTD homology model and are in agreement with the HDX profile (Figure 2A, C and Supplementary Figure S6).","type":"Results"},{"text":"RRV nsP4FL corresponds to region 1870-2479 (NTD: 1870-1978; RdRP: 1979-2479). This evidence corresponds to the linker between NTD and RdRp.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-06T11:13:28.623Z"}},{"start":1943,"end":1978,"reference_id":"35037043","reference_source":"pmid","reference_html":"Crystal structures of alphavirus nonstructural protein 4 (nsP4) reveal an intrinsically dynamic RNA-dependent RNA polymerase fold. <i> Tan YB, Lello LS, Liu X, Law YS, Kang C, Lescar J, Zheng J, Merits A, Luo D. </i> Nucleic Acids Res, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":1,"region_id":"DP03593r008","statement":[{"text":"Given its low molecular mass of 12.6 kDa, the recombinant NTD is amenable to structural characterization via NMR in solution. The NTD selected from RRV contains 107 amino acids with an expected number of 99 cross-peaks (excluding Pro residues) in the 1H-15N-HSQC spectrum. From these, ∼60 cross-peaks could be observed, making backbone resonance assignments challenging (Supplementary Figure S6). The narrow dispersion of the cross-peaks in the spectrum suggests that the NTD contains flexible and helical regions that support the NTD homology model and are in agreement with the HDX profile (Figure 2A, C and Supplementary Figure S6).","type":"Results"},{"text":"RRV nsP4FL corresponds to region 1870-2479 (NTD: 1870-1978; RdRP: 1979-2479). This evidence corresponds to the linker between NTD and RdRp.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-06T11:13:36.867Z"}},{"start":1870,"end":1922,"reference_id":"35037043","reference_source":"pmid","reference_html":"Crystal structures of alphavirus nonstructural protein 4 (nsP4) reveal an intrinsically dynamic RNA-dependent RNA polymerase fold. <i> Tan YB, Lello LS, Liu X, Law YS, Kang C, Lescar J, Zheng J, Merits A, Luo D. </i> Nucleic Acids Res, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":1,"region_id":"DP03593r009","statement":[{"text":"Given its low molecular mass of 12.6 kDa, the recombinant NTD is amenable to structural characterization via NMR in solution. The NTD selected from RRV contains 107 amino acids with an expected number of 99 cross-peaks (excluding Pro residues) in the 1H-15N-HSQC spectrum. From these, ∼60 cross-peaks could be observed, making backbone resonance assignments challenging (Supplementary Figure S6). The narrow dispersion of the cross-peaks in the spectrum suggests that the NTD contains flexible and helical regions that support the NTD homology model and are in agreement with the HDX profile (Figure 2A, C and Supplementary Figure S6).","type":"Results"},{"text":"RRV nsP4FL corresponds to region 1870-2479 (NTD: 1870-1978; RdRP: 1979-2479).","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-06T11:13:37.737Z"}},{"start":1870,"end":1919,"reference_id":"35037043","reference_source":"pmid","reference_html":"Crystal structures of alphavirus nonstructural protein 4 (nsP4) reveal an intrinsically dynamic RNA-dependent RNA polymerase fold. <i> Tan YB, Lello LS, Liu X, Law YS, Kang C, Lescar J, Zheng J, Merits A, Luo D. </i> Nucleic Acids Res, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_12","version":1,"region_id":"DP03593r010","statement":[{"text":"A high percentage of deuteration (D%; hydrogen exchanged to deuterium) reflects the high solvent accessibility and flexibility of the regions on RRV and SINV nsP4.","type":"Results"},{"text":"RRV nsP4FL corresponds to region 1870-2479 (NTD: 1870-1978; RdRP: 1979-2479).","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-06T11:13:40.641Z"}},{"start":1946,"end":2038,"reference_id":"35037043","reference_source":"pmid","reference_html":"Crystal structures of alphavirus nonstructural protein 4 (nsP4) reveal an intrinsically dynamic RNA-dependent RNA polymerase fold. <i> Tan YB, Lello LS, Liu X, Law YS, Kang C, Lescar J, Zheng J, Merits A, Luo D. </i> Nucleic Acids Res, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_12","version":1,"region_id":"DP03593r011","statement":[{"text":"A high percentage of deuteration (D%; hydrogen exchanged to deuterium) reflects the high solvent accessibility and flexibility of the regions on RRV and SINV nsP4.","type":"Results"},{"text":"RRV nsP4FL corresponds to region 1870-2479 (NTD: 1870-1978; RdRP: 1979-2479).","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-06T11:13:41.654Z"}},{"start":2071,"end":2093,"reference_id":"35037043","reference_source":"pmid","reference_html":"Crystal structures of alphavirus nonstructural protein 4 (nsP4) reveal an intrinsically dynamic RNA-dependent RNA polymerase fold. <i> Tan YB, Lello LS, Liu X, Law YS, Kang C, Lescar J, Zheng J, Merits A, Luo D. </i> Nucleic Acids Res, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_12","version":1,"region_id":"DP03593r012","statement":[{"text":"A high percentage of deuteration (D%; hydrogen exchanged to deuterium) reflects the high solvent accessibility and flexibility of the regions on RRV and SINV nsP4.","type":"Results"},{"text":"RRV nsP4FL corresponds to region 1870-2479 (NTD: 1870-1978; RdRP: 1979-2479).","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-06T11:13:43.121Z"}},{"start":2429,"end":2454,"reference_id":"35037043","reference_source":"pmid","reference_html":"Crystal structures of alphavirus nonstructural protein 4 (nsP4) reveal an intrinsically dynamic RNA-dependent RNA polymerase fold. <i> Tan YB, Lello LS, Liu X, Law YS, Kang C, Lescar J, Zheng J, Merits A, Luo D. </i> Nucleic Acids Res, 2022","date":"2022-02-14T09:00:00.000Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_12","version":1,"region_id":"DP03593r013","statement":[{"text":"A high percentage of deuteration (D%; hydrogen exchanged to deuterium) reflects the high solvent accessibility and flexibility of the regions on RRV and SINV nsP4.","type":"Results"},{"text":"RRV nsP4FL corresponds to region 1870-2479 (NTD: 1870-1978; RdRP: 1979-2479).","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-06T11:13:44.435Z"}}],"regions_counter":13,"released":"2022_12","sequence":"MKVTVDVEADSPFLKALQKAFPAFEVESQQVTPNDHANARAFSHLATKLIEQEVPANITILDVGSAPARRLMSDHSYHCICPMKSAEDPERLANYARKLAKTAGEVLDKNVSGKITDLQDVMATPDLESPTFCLHTDETCRTRAEVAVYQDVXXHAPTSLYHQAMKGVRTVYWIGFDTTPFMFEVVAGAYPTYSTNWADEQVLQARNIGLCATSLSEGHRGKISIMRKKRLRPSDRXMFSVGXTLYIESRRLLKSWHLPSVFHLKGKNSFTCRCDTIVSCEGYVVKKITMSPGTYGKTVGYAVTHHAEGFLMCKVTDTVRGERVSFPVCTYVPATICDQMTGILATDVTPEDAQKLLVGLNQRIVVNGRTQRNTNTMKNYLLPVVAQAFSKWAREAKADMEDEKPLGTRERTLTCCCLWAFKNHKTHTMYKRPDTQTIVKVPSTFDSFVIPSLWSSSLSIGIRQRIKLLLGPKLSRDLPYSGDRNEAREAEKEAEETKEAELTREALPPLVGSNCADDVDQVDVEELTYRAGAGVVETPRNALKVTPQERDQLIGAYLILSPQTVLKSEKLTPIHPLAEQVTIMTHSGRSGRYPVDRYDGRVLVPTGAAIPVSEFQALSESATMVYNEREFINRKLHHIALYGPALNTDEENYEKVRAERAEAEYVFDVDKRTCVKREDASGLVLVGDLINPPFHEFAYEGLKIRPATPFQTTVIGVFGVPGSGKSAIIKSVVTTRDLVASGKKENCQEIVNDVKKQRGLDVTARTVDSILLNGCRRGVENLYVDEAFACHSGTLLALIAMVKPTGKVILCGDPKQCGFFNLMQLKVNFNHDICTQVLHKSISRRCTLPITAIVSTLHYQGKMRTTNLCSAPIQIDTTGTTKPAKGDIVLTCFRXWVKQLQIDYRGHEVMTAAASQGLTRKGVYAVRQKVNENPLYAPSSEHVNVLLTRTENRLVWKTLSGDPWIKVLTNIPKGDFSATLEEWQEEHDNIMNALRERSTAVDPFQNKAKVCWAKCLVQVLETAGIRMTAEEWDTVLAFREDRAYSPEVALNEICTKYYGVDLDSGLFSAQSVSLYYENNHWDNRPGGRMYGFNREVARKFEQRYPFLRGKMDSGLQVNVPERKVQPFNAECNILLLNRRLPHALVTSYQQCRGERVEWLLKKLPGYHLLLVSEYNLALPHKRVFWIAPPHVSGADRIYDLDLGLPLNAGRYDLVFVNIHTEYRTHHYQQCVDHSMKLQMLGGDSLHLLXPGGSLLIRAYGYADRVSEMVVTALARKFSAFRVLRPACVTSNTEVFLLFTNFDNGRRAVTLHQANQRLSSMFACNGLHTAGCAPSYRVRRTDISGHAEEAVVNAANAKGTVGVGVCRAVARKWPDSFKGAATPVGTAKLVQANGMNVIHAVGPNFSTVTEAEGDRELAAAYRAVAGIINASNIKSVAIPLLSTGVFSGGKDRVMQSLNHLFTAMDTTDADVVIYCRDKAWEKKIQEAIDRRTAVELVSEDISLESDLIRVHPDSCLVGRKGYSITDGKLHSYLEGTRFHQTAVDMAEISTLWPKLQDANEQICLYALGESMDSIRTKCPVEDADSSTPPKTVPCLCRYAMTAERVARLRMNNTKAIIVCSSFPLPKYRIEGVQKVKCDRVLIFDQTVPSLVSPRKYIPAAASMHADTVSLDSTVSTGSAWSFPSEATYETMEVVAEVHHSEPPVPPPRRRRAQVTMHHQELLEVSDMHTPIAARVEIPVYDTAVVAERVAIPCTSEYATPIPTPRAVRVVPVPAPRIQRASTYRVSPTPTPRVLRASVCSVTTSAGVEFPWAPEDLEVLTEPVHCEMREPVELPWEPEDVDIQFGDFETPDKIQFGDIDFDQFXLSRAGAYIFSSDTGPGHLQQKSVRQHALPCEMLYAHEEERTYPPALDEAREKLLQAKMQMAPTEANKSRYQSRKVENMKAVIIDRLKDGARTYLAEQSEKIPTYASKYPRPVYSPSVEDSLQSPEVAVAACNAFLEANYPTVASYQITDEYDAYLDMVDGSESCLDRATFCPAKLRCYPKHHAYHQPQVRSAVPSPFQNTLQNVLAAATKRNCNVTQMRELPTLDSAVFNVECFKKFACNGEYWQEFKDDPIRITTENITTYVTRLKGPKAAALFAKTHNLVPLQEVPMDRFVVDMKRDVKVTPGTKHTEERPKVQVIQAAEPLATAYLCGIHRELVRRLKAVLAPNIHTLFDMSAEDFDAIIAAHFQPGDAVLETDIASFDKSQDDSLALTALMLLEDLGVDQELLDLIEEAFGEITSVHLPTGTRFKFGAMMKSGMFLTLFINTLLNIVIACRVLREKLTNSICAAFIGDDNIVHGVRSDPLMAERCASWVNMEVKIIDATMCEKPPYFCGGFILYDNVTGSACRVADPLKRLFKLGKPLPAGDTQDEDRRRALKDETDRWARVGLKSELEIALSSRYEVNGTGNIVRAMATLAKSLKNFKKLRGPIVHLYGGPK","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Alsuviricetes","Martellivirales","Togaviridae","Alphavirus"],"dataset":["Viral proteins","RNA-binding proteins"],"genes":[],"disorder_content":0.09717741935483871,"disprot_consensus":{"full":[{"start":1870,"end":1922,"type":"D"},{"start":1943,"end":2053,"type":"D"},{"start":2071,"end":2093,"type":"D"},{"start":2161,"end":2176,"type":"D"},{"start":2429,"end":2454,"type":"D"},{"start":2469,"end":2480,"type":"D"}],"Structural state":[{"start":1870,"end":1922,"type":"D"},{"start":1943,"end":2053,"type":"D"},{"start":2071,"end":2093,"type":"D"},{"start":2161,"end":2176,"type":"D"},{"start":2429,"end":2454,"type":"D"},{"start":2469,"end":2480,"type":"D"}],"Disorder function":[{"start":1943,"end":1978,"type":"F"}]}},{"disprot_id":"DP03594","acc":"P50579","creator":"vacs","date":"2022-01-28T13:31:12.590Z","features":{"pfam":[{"id":"PF00557","name":"Metallopeptidase family M24","start":169,"end":372}],"gene3D":[]},"length":478,"name":"Methionine aminopeptidase 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":109,"reference_id":"9812898","reference_source":"pmid","reference_html":"Structure of human methionine aminopeptidase-2 complexed with fumagillin. <i> Liu S, Widom J, Kemp CW, Crews CM, Clardy J. </i> Science, 1998","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"1B6A"},{"db":"PDB","id":"1BOA"},{"db":"PDB","id":"1BN5"}],"region_id":"DP03594r001","statement":[{"text":"HsMetAP-2, unlike EcMetAP- I and PfMetAP-2, has a 165-residue NH2-terminal extension, which is not essential for aminopeptidase activity (6). In the structure described here, the NH2-tenninal extension is largely disordered, and clear electron density begins at Lys110 with a disordered loop from residues 138 to 153 (Fig. 3B).","type":"Article"},{"text":"Residues 1-109 and 139-152 are disordered in the structures.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-07T09:41:51.303Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":139,"end":152,"reference_id":"9812898","reference_source":"pmid","reference_html":"Structure of human methionine aminopeptidase-2 complexed with fumagillin. <i> Liu S, Widom J, Kemp CW, Crews CM, Clardy J. </i> Science, 1998","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"1B6A"},{"db":"PDB","id":"1BOA"},{"db":"PDB","id":"1BN5"},{"db":"PDB","id":"1B59"}],"region_id":"DP03594r002","statement":[{"text":"HsMetAP-2, unlike EcMetAP- I and PfMetAP-2, has a 165-residue NH2-terminal extension, which is not essential for aminopeptidase activity (6). In the structure described here, the NH2-tenninal extension is largely disordered, and clear electron density begins at Lys110 with a disordered loop from residues 138 to 153 (Fig. 3B).","type":"Article"},{"text":"Residues 1-109 and 139-152 are disordered in the structures.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-07T09:41:50.432Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2023_12","sequence":"MAGVEEVAASGSHLNGDLDPDDREEGAASTAEEAAKKKRRKKKKSKGPSAAGEQEPDKESGASVDEVARQLERSALEDKERDEDDEDGDGDGDGATGKKKKKKKKKRGPKVQTDPPSVPICDLYPNGVFPKGQECEYPPTQDGRTAAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"METAP2","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03175","url":"https://hamap.expasy.org/unirule/MF_03175"}}]},"synonyms":[{"value":"MNPEP"},{"value":"P67EIF2"}]}],"alphafold_very_low_content":0.19665271966527198,"disorder_content":0.25732217573221755,"disprot_consensus":{"full":[{"start":1,"end":109,"type":"D"},{"start":139,"end":152,"type":"D"}],"Structural state":[{"start":1,"end":109,"type":"D"},{"start":139,"end":152,"type":"D"}]}},{"disprot_id":"DP03595","acc":"P53254","creator":"vacs","date":"2022-01-30T14:02:17.696Z","features":{"pfam":[{"id":"PF03813","name":"Nrap protein domain 1","start":144,"end":355},{"id":"PF17403","name":"Nrap protein PAP/OAS-like domain","start":358,"end":514},{"id":"PF17404","name":"Nrap protein domain 3","start":521,"end":690},{"id":"PF17405","name":"Nrap protein nucleotidyltransferase domain 4","start":705,"end":904},{"id":"PF17406","name":"Nrap protein PAP/OAS1-like domain 5","start":906,"end":1091},{"id":"PF17407","name":"Nrap protein domain 6","start":1093,"end":1232}],"gene3D":[]},"length":1237,"name":"U3 small nucleolar RNA-associated protein 22","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":80,"reference_id":"24130456","reference_source":"pmid","reference_html":"An RNA-binding complex involved in ribosome biogenesis contains a protein with homology to tRNA CCA-adding enzyme. <i> Lin J, Lu J, Feng Y, Sun M, Ye K. </i> PLoS Biol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"4M5D"}],"region_id":"DP03595r001","statement":[{"text":"N-terminal residues 1–80 of Utp22, C-terminal residues 190–297 of Rrp7, and several internal loops of each protein were not visible in the crystal structure, likely due to structural flexibility. SDS-PAGE analysis of dissolved crystals showed that Utp22 was intact and Rrp7 was partially degraded (unpublished data).","type":"Results"},{"text":"The current model contains Utp22 residues 81–274, 282–317, 326–445, 453–983, 1010 1116, and 1128–1237; Rrp7 residues 3–27, 32–105, and 120–189; 764 water molecules; 11 sulfate ions; and three PEG molecules.","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-07T09:27:59.521Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":984,"end":1009,"reference_id":"24130456","reference_source":"pmid","reference_html":"An RNA-binding complex involved in ribosome biogenesis contains a protein with homology to tRNA CCA-adding enzyme. <i> Lin J, Lu J, Feng Y, Sun M, Ye K. </i> PLoS Biol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"4M5D"}],"region_id":"DP03595r002","statement":[{"text":"N-terminal residues 1–80 of Utp22, C-terminal residues 190–297 of Rrp7, and several internal loops of each protein were not visible in the crystal structure, likely due to structural flexibility. SDS-PAGE analysis of dissolved crystals showed that Utp22 was intact and Rrp7 was partially degraded (unpublished data).","type":"Results"},{"text":"The current model contains Utp22 residues 81–274, 282–317, 326–445, 453–983, 1010 1116, and 1128–1237; Rrp7 residues 3–27, 32–105, and 120–189; 764 water molecules; 11 sulfate ions; and three PEG molecules.","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-07T09:27:58.446Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":1117,"end":1127,"reference_id":"24130456","reference_source":"pmid","reference_html":"An RNA-binding complex involved in ribosome biogenesis contains a protein with homology to tRNA CCA-adding enzyme. <i> Lin J, Lu J, Feng Y, Sun M, Ye K. </i> PLoS Biol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"4M5D"}],"region_id":"DP03595r003","statement":[{"text":"N-terminal residues 1–80 of Utp22, C-terminal residues 190–297 of Rrp7, and several internal loops of each protein were not visible in the crystal structure, likely due to structural flexibility. SDS-PAGE analysis of dissolved crystals showed that Utp22 was intact and Rrp7 was partially degraded (unpublished data).","type":"Results"},{"text":"The current model contains Utp22 residues 81–274, 282–317, 326–445, 453–983, 1010 1116, and 1128–1237; Rrp7 residues 3–27, 32–105, and 120–189; 764 water molecules; 11 sulfate ions; and three PEG molecules.","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-07T09:27:57.354Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":3,"released":"2023_12","sequence":"MATSVKRKASETSDQNIVKVQKKHSTQDSTTDNGSKENDHSSQAINERTVPEQENDESDTSPESNEVATNTAATRHNGKVTATESYDIHIARETAELFKSNIFKLQIDELLEQVKLKQKHVLKVEKFLHKLYDILQEIPDWEEKSLAEVDSFFKNKIVSVPFVDPKPIPQNTNYKFNYKKPDISLIGSFALKAGIYQPNGSSIDTLLTMPKELFEKKDFLNFRCLHKRSVYLAYLTHHLLILLKKDKLDSFLQLEYSYFDNDPLLPILRISCSKPTGDSLSDYNFYKTRFSINLLIGFPYKVFEPKKLLPNRNCIRIAQESKEQSLPATPLYNFSVLSSSTHENYLKYLYKTKKQTESFVEATVLGRLWLQQRGFSSNMSHSGSLGGFGTFEFTILMAALLNGGGINSNKILLHGFSSYQLFKGVIKYLATMDLCHDGHLQFHSNPENSSSSPASKYIDEGFQTPTLFDKSTKVNILTKMTVSSYQILKEYAGETLRMLNNVVQDQFSNIFLTNISRFDNLKYDLCYDVQLPLGKYNNLETSLAATFGSMERVKFITLENFLAHKITNVARYALGDRIKYIQIEMVGQKSDFPITKRKVYSNTGGNHFNFDFVRVKLIVNPSECDKLVTKGPAHSETMSTEAAVFKNFWGIKSSLRRFKDGSITHCCVWSTSSSEPIISSIVNFALQKHVSKKAQISNETIKKFHNFLPLPNLPSSAKTSVLNLSSFFNLKKSFDDLYKIIFQMKLPLSVKSILPVGSAFRYTSLCQPVPFAYSDPDFFQDVILEFETSPKWPDEITSLEKAKTAFLLKIQEELSANSSTYRSFFSRDESIPYNLEIVTLNILTPEGYGFKFRVLTERDEILYLRAIANARNELKPELEATFLKFTAKYLASVRHTRTLENISHSYQFYSPVVRLFKRWLDTHLLLGHITDELAELIAIKPFVDPAPYFIPGSLENGFLKVLKFISQWNWKDDPLILDLVKPEDDIRDTFETSIGAGSELDSKTMKKLSERLTLAQYKGIQMNFTNLRNSDPNGTHLQFFVASKNDPSGILYSSGIPLPIATRLTALAKVAVNLLQTHGLNQQTINLLFTPGLKDYDFVVDLRTPIGLKSSCGILSATEFKNITNDQAPSNFPENLNDLSEKMDPTYQLVKYLNLKYKNSLILSSRKYIGVNGGEKGDKNVITGLIKPLFKGAHKFRVNLDCNVKPVDDENVILNKEAIFHEIAAFGNDMVINFETD","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"genes":[{"name":{"value":"UTP22"},"olnNames":[{"value":"YGR090W"}]}],"alphafold_very_low_content":0.0889248181083266,"dataset":["RNA-binding proteins"],"disorder_content":0.09458367016976556,"disprot_consensus":{"full":[{"start":1,"end":80,"type":"D"},{"start":984,"end":1009,"type":"D"},{"start":1117,"end":1127,"type":"D"}],"Structural state":[{"start":1,"end":80,"type":"D"},{"start":984,"end":1009,"type":"D"},{"start":1117,"end":1127,"type":"D"}]}},{"disprot_id":"DP03596","acc":"P25368","creator":"vacs","date":"2022-01-30T14:07:36.092Z","features":{"pfam":[{"id":"PF12923","name":"Ribosomal RNA-processing protein 7 (RRP7) C-terminal domain","start":177,"end":296},{"id":"PF17799","name":"Rrp7 RRM-like N-terminal domain","start":9,"end":161}],"gene3D":[]},"length":297,"name":"Ribosomal RNA-processing protein 7","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":106,"end":119,"reference_id":"24130456","reference_source":"pmid","reference_html":"An RNA-binding complex involved in ribosome biogenesis contains a protein with homology to tRNA CCA-adding enzyme. <i> Lin J, Lu J, Feng Y, Sun M, Ye K. </i> PLoS Biol, 2013","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"4M5D"}],"region_id":"DP03596r001","statement":[{"text":"N-terminal residues 1–80 of Utp22, C-terminal residues 190–297 of Rrp7, and several internal loops of each protein were not visible in the crystal structure, likely due to structural flexibility. SDS-PAGE analysis of dissolved crystals showed that Utp22 was intact and Rrp7 was partially degraded (unpublished data).","type":"Results"},{"text":"In addition, two prominent tentacle-like structures project from the NTD to reach the more distant D6 of Utp22. One tentacle comprises a long loop between strands b4 and b5. This loop is disordered in the C-terminal half and its sequence is highly variable among Rrp7 orthologs (Figure 2B and Text S2).","type":"Results"},{"text":"The current model contains Utp22 residues 81–274, 282–317, 326–445, 453–983, 1010 1116, and 1128–1237; Rrp7 residues 3–27, 32–105, and 120–189; 764 water molecules; 11 sulfate ions; and three PEG molecules.","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-07T09:25:46.525Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_12","sequence":"MGIEDISAMKNGFIVVPFKLPDHKALPKSQEASLHFMFAKRHQSSNSNESDCLFLVNLPLLSNIEHMKKFVGQLCGKYDTVSHVEELLYNDEFGLHEVDLSALTSDLMSSTDVNEKRYTPRNTALLKFVDAASINNCWNALKKYSNLHAKHPNELFEWTYTTPSFTTFVNFYKPLDIDYLKEDIHTHMAIFEQREAQAQEDVQSSIVDEDGFTLVVGKNTKSLNSIRKKILNKNPLSKHENKAKPISNIDKKAKKDFYRFQVRERKKQEINQLLSKFKEDQERIKVMKAKRKFNPYT","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"genes":[{"name":{"value":"RRP7"},"orfNames":[{"value":"YCL184"},{"value":"YCL31C"}],"olnNames":[{"value":"YCL031C"}]}],"alphafold_very_low_content":0.013468013468013467,"disorder_content":0.04713804713804714,"disprot_consensus":{"full":[{"start":106,"end":119,"type":"D"}],"Structural state":[{"start":106,"end":119,"type":"D"}]}},{"disprot_id":"DP03597","acc":"P02994","creator":"vacs","date":"2022-01-31T12:07:41.454Z","features":{"pfam":[{"id":"PF00009","name":"Elongation factor Tu GTP binding domain","start":5,"end":232},{"id":"PF03144","name":"Elongation factor Tu domain 2","start":258,"end":324},{"id":"PF22594","name":"GTP-eEF1A C-terminal domain-like","start":337,"end":437}],"gene3D":[]},"length":458,"name":"Elongation factor 1-alpha","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":442,"end":458,"reference_id":"11106763","reference_source":"pmid","reference_html":"Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha. <i> Andersen GR, Pedersen L, Valente L, Chatterjee I, Kinzy TG, Kjeldgaard M, Nyborg J. </i> Mol Cell, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"1F60"}],"region_id":"DP03597r001","statement":[{"text":"Residues 2–441 in eEF1A and 117–206 in eEF1Bα were modeled, while amino acids 1 and 442–452 in eEF1A and 110–116 in eEF1Bα are disordered. ","type":"Results"},{"text":"Residues 442-458 are disordered in the structure.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-07T09:24:16.547Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":454,"end":458,"reference_id":"10973948","reference_source":"pmid","reference_html":"A novel post-translational modification of yeast elongation factor 1A. Methylesterification at the C terminus. <i> Zobel-Thropp P, Yang MC, Machado L, Clarke S. </i> J Biol Chem, 2000","date":"2022-02-14T09:00:00.000Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000042","term_name":"methylation display site","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0001194","ec_ontology":"ECO","ec_name":"in vitro demethylation assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03597r002","statement":[{"text":"Because the base-labile, volatile [methyl-3H]radioactivity of eEF1A could be released by trypsin treatment but not by carboxypeptidase Y or chymotrypsin treatment, we suggest that the methyl ester is present on the α-carboxyl group of its C-terminal lysine residue.","type":"Abstract"},{"text":"The rapid turnover of the methyl ester suggests that the methylation/demethylation of eEF1A at the C-terminal carboxyl group may represent a novel mode of regulation of the activity of this protein in yeast.","type":"Abstract"},{"text":"However, the existence of the C-terminal carboxyl methyl ester identified in this study has not been previously recognized.","type":"Introduction"},{"text":"Significantly, we found that [3H]methanol was released when the 49-kDa polypeptide was digested by trypsin but that little or no [3H]methanol was released with CPY, chymotrypsin, or buffer alone (Fig. 5A). The C-terminal amino acid residue of yeast eEF1A is lysine (15). Therefore, trypsin would be expected to cleave C-terminally to this residue and, if it is methyl esterified, release methanol (28, 29). Chymotrypsin, with its specificity for aromatic residues, would not be expected to cleave this linkage.","type":"Results"},{"text":"Thus, the data from the in vivo experiments shown in Fig. 5 are consistent with the data from the control experiments from Table I and indicate that the methyl ester on the eEF1A C-terminal lysine residue can be hydrolyzed by trypsin but not by CPY and chymotrypsin. The inability of CPY to cleave the lysine α-carboxyl methyl ester under these conditions may reflect the effect of the positively charged side chain. Taken together, these results indicate that the methyl ester linkage on eEF1A is on the carboxyl group of its C-terminal lysine residue.","type":"Results"},{"text":"We set out to identify novel methylesterified proteins in yeast and identified a major methylated polypeptide as eEF1A that is not only amino-methylated on some internal lysine residues but is also carboxyl methylated at the C terminus.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-07T09:24:14.229Z"},"ec_go":"IDA","disprot_namespace":"Disorder function"}],"regions_counter":2,"released":"2023_12","sequence":"MGKEKSHINVVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYQVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGVGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDSVKWDESRFQEIVKETSNFIKKVGYNPKTVPFVPISGWNGDNMIEATTNAPWYKGWEKETKAGVVKGKTLLEAIDAIEQPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFAPAGVTTEVKSVEMHHEQLEQGVPGDNVGFNVKNVSVKEIRRGNVCGDAKNDPPKGCASFNATVIVLNHPGQISAGYSPVLDCHTAHIACRFDELLEKNDRRSGKKLEDHPKFLKSGDAALVKFVPSKPMCVEAFSEYPPLGRFAVRDMRQTVAVGVIKSVDKTEKAAKVTKAAQKAAKK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"genes":[{"name":{"value":"TEF1"},"orfNames":[{"value":"P9513.7"}],"olnNames":[{"value":"YPR080W"}]},{"name":{"value":"TEF2"},"orfNames":[{"value":"YBR0913"}],"olnNames":[{"value":"YBR118W"}]}],"alphafold_very_low_content":0.004366812227074236,"disorder_content":0.03711790393013101,"disprot_consensus":{"full":[{"start":442,"end":458,"type":"D"}],"Structural state":[{"start":442,"end":458,"type":"D"}],"Disorder function":[{"start":454,"end":458,"type":"F"}]}},{"disprot_id":"DP03598","acc":"Q6VRZ6","creator":"esalladini","date":"2022-01-31T13:51:41.689Z","features":{"pfam":[{"id":"PF08794","name":"Factor H binding protein, C-terminal","start":142,"end":238},{"id":"PF20937","name":"Factor H binding protein, N-terminal","start":1,"end":74}],"gene3D":[]},"length":255,"name":"Factor H binding protein variant B24_010","ncbi_taxon_id":487,"organism":"Neisseria meningitidis","regions":[{"start":101,"end":137,"reference_id":"16407174","reference_source":"pmid","reference_html":"Solution structure of the immunodominant domain of protective antigen GNA1870 of Neisseria meningitidis. <i> Cantini F, Savino S, Scarselli M, Masignani V, Pizza M, Romagnoli G, Swennen E, Veggi D, Banci L, Rappuoli R. </i> J Biol Chem, 2006","date":"2022-02-16T14:36:29.055Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1YS5"},{"db":"BMRB","id":"16058"}],"region_id":"DP03598r001","statement":[{"text":"The protein adopts an eight-stranded β-barrel conformation, which encompasses amino acids 151-255, whereas the remaining residues include a short α-helix (138-141) and a flexible tail (101-137), which probably serves as a linker to the N-terminal A region of the protein.","type":"Introduction"},{"text":"The structure consists of an eight-stranded antiparallel β-barrel overlaid by a short α-helix with an unstructured N-terminal end.","type":"Abstract"},{"text":"The rest of the molecule (101-137) is characterized by a low number of long range NOEs, which determine higher RMSD values (Fig. 2).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:48:06.182Z"}}],"regions_counter":1,"released":"2023_12","sequence":"CSSGGGGVAADIGAGLADALTAPLDHKDKGLQSLTLDQSVRKNEKLKLAAQGAEKTYGNGDSLNTGKLKNDKVSRFDFIRQIEVDGQLITLESGEFQVYKQSHSALTAFQTEQIQDSEHSGKMVAKRQFRIGDIAGEHTSFDKLPEGGRATYRGTAFGSDDAGGKLTYTIDFAAKQGNGKIEHLKSPELNVDLAAADIKPDGKRHAVISGSVLYNQAEKGSYSLGIFGGKAQEVAGSAEVKTVNGIRHIGLAAKQ","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"genes":[{"name":{"value":"fhbp","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAR84469.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAR84469.1"}}]}}],"alphafold_very_low_content":0.03529411764705882,"disorder_content":0.1450980392156863,"disprot_consensus":{"full":[{"start":101,"end":137,"type":"D"}],"Structural state":[{"start":101,"end":137,"type":"D"}]}},{"disprot_id":"DP03599","acc":"Q9JYK4","creator":"esalladini","date":"2022-02-10T09:56:08.361Z","features":{"pfam":[{"id":"PF01298","name":"C-lobe and N-lobe beta barrels of Tf-binding protein B","start":192,"end":361},{"id":"PF01298","name":"C-lobe and N-lobe beta barrels of Tf-binding protein B","start":563,"end":730},{"id":"PF17483","name":"C-lobe handle domain of Tf-binding protein B","start":381,"end":471},{"id":"PF17484","name":"N-Lobe handle Tf-binding protein B","start":43,"end":189}],"gene3D":[]},"length":737,"name":"Transferrin-binding protein B","ncbi_taxon_id":122586,"organism":"Neisseria meningitidis serogroup B (strain MC58)","regions":[{"start":470,"end":546,"reference_id":"34751649","reference_source":"pmid","reference_html":"Structural insight into the dual function of LbpB in mediating Neisserial pathogenesis. <i> Yadav R, Govindan S, Daczkowski C, Mesecar A, Chakravarthy S, Noinaj N. </i> Elife, 2021","date":"2022-02-10T10:11:42.799Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7JRD"}],"region_id":"DP03599r001","statement":[{"text":"The C-lobe of NmLbpB is composed of residues 359–718 and found largely disordered in the crystal structure as evident from higher B-factors for this region compared to the rest of the structure (Figure 3C).","type":"Results"},{"text":"The C-lobe of NmLbpB hashigh B-factors with the large loops of this lobe not observed in our structure; the black arrow indicates the putative location of these loops.","type":"Figure"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:48:20.877Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MCKPNYGGIVLLPLLLASCIGGNFGVQPVVESTPTAYPVTFKSKDVPTPPPAGSSVETTPVNRPAVGAAMRLPRRNIASYKQDGTEIPDKHQAEEHLPLKEKDILFLDGTLKEQADKLKKKINERYSDVRVITSKKEEEKYQYQFVRAGYVFTRAEGKDNEKEKTSDGKEFVNRFSYDGFVYYSGERPSQSLPSAGTVQYSGNWQYMTDAKRHRTGKAVSSTDLGYTTYYGNEIGATSYEARDADDREKHPAEYTVDFDNKTLNGKLIKNQYVQNKSNPNEPKKPLTIYDITATLDGNRFTGSAKVSTEVKTQHADKEYLFFHTDADQRLEGGFFGDNGEELAGRFISNDNSVFGVFAGKQKTETENAADTKPALSSGKHTKILDSLKISVDEASDKNPREFAISSMPDFGHPDKLLVEGREIPLVNKEQTIELADGRKTTIRTCCDFLTYVKIGRMQTERPAAKPKAQDEERDEEDTGVDSVEEGEDEIDDEEGTEDAAVKDEGSEEDEAVEGEDEAEEPEEESPTEEGGSGSDGILPAPEAPKGRNIDLFLKGIRTAETDIPKTGEAHYTGTWEARIGKPIQWDNQADKEAAKAVFTVDFGKKSISGTLTEENGVEPAFHIENGKIEGNGFYATARTRENGINLSGNGSTDPKTFQASNLRVEGGFYGPQAEELGGIIFNNDGKSLGITEGTENKVDVEAEVDAEVDVGKQLESEVKHQFGVVFGAKKDMQEVEK","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"genes":[{"name":{"value":"lbpB","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF41896.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF41896.1"}}]},"olnNames":[{"value":"NMB1541","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF41896.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF41896.1"}}]}]}],"alphafold_very_low_content":0.23609226594301222,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.1044776119402985,"disprot_consensus":{"full":[{"start":470,"end":546,"type":"D"}],"Structural state":[{"start":470,"end":546,"type":"D"}]}},{"disprot_id":"DP03600","acc":"Q9JXV4","creator":"esalladini","date":"2022-02-10T10:21:28.749Z","features":{"pfam":[{"id":"PF08794","name":"Factor H binding protein, C-terminal","start":161,"end":257},{"id":"PF20937","name":"Factor H binding protein, N-terminal","start":8,"end":93}],"gene3D":[]},"length":274,"name":"Lipoprot_C domain-containing protein","ncbi_taxon_id":122586,"organism":"Neisseria meningitidis serogroup B (strain MC58)","regions":[{"start":20,"end":46,"reference_id":"34125873","reference_source":"pmid","reference_html":"Two human antibodies to a meningococcal serogroup B vaccine antigen enhance binding of complement Factor H by stabilizing the Factor H binding site. <i> Sands NA, Beernink PT. </i> PLoS Pathog, 2021","date":"2022-02-16T14:29:33.364Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7LCV"}],"region_id":"DP03600r001","statement":[{"text":"The protein N-terminus (66-92) is missing from the pdb structure.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:48:27.472Z"}},{"start":23,"end":48,"reference_id":"27784765","reference_source":"pmid","reference_html":"Neisseria meningitidis factor H-binding protein bound to monoclonal antibody JAR5: implications for antibody synergy. <i> Malito E, Lo Surdo P, Veggi D, Santini L, Stefek H, Brunelli B, Luzzi E, Bottomley MJ, Beernink PT, Scarselli M. </i> Biochem J, 2016","date":"2022-02-16T14:29:41.705Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5T5F"}],"region_id":"DP03600r002","statement":[{"text":"The protein N-terminus (69-94) is missing from the pdb structure.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:48:28.676Z"}},{"start":23,"end":33,"reference_id":"23396847","reference_source":"pmid","reference_html":"Defining a protective epitope on factor H binding protein, a key meningococcal virulence factor and vaccine antigen. <i> Malito E, Faleri A, Lo Surdo P, Veggi D, Maruggi G, Grassi E, Cartocci E, Bertoldi I, Genovese A, Santini L, Romagnoli G, Borgogni E, Brier S, Lo Passo C, Domina M, Castellino F, Felici F, van der Veen S, Johnson S, Lea SM, Tang CM, Pizza M, Savino S, Norais N, Rappuoli R, Bottomley MJ, Masignani V. </i> Proc Natl Acad Sci U S A, 2013","date":"2022-02-16T14:29:50.435Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2YPV"}],"region_id":"DP03600r003","sample":[{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"ABCD_AG710","statements":[{"type":"Supplementary material","text":"For the purpose of cocrystallization, the complex of fHbp with Fab 12C1 was prepared by coincubation at 4 °C followed by preparative size-exclusion chromatography in 20 mM Tris·HCl and 150 mM NaCl, pH 8.0, using a Superdex 75 (16/60) column (GE Healthcare)."}]}],"statement":[{"text":"The protein N-terminus (69-79) is missing from the pdb structure.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:48:31.972Z"}},{"start":34,"end":48,"reference_id":"23396847","reference_source":"pmid","reference_html":"Defining a protective epitope on factor H binding protein, a key meningococcal virulence factor and vaccine antigen. <i> Malito E, Faleri A, Lo Surdo P, Veggi D, Maruggi G, Grassi E, Cartocci E, Bertoldi I, Genovese A, Santini L, Romagnoli G, Borgogni E, Brier S, Lo Passo C, Domina M, Castellino F, Felici F, van der Veen S, Johnson S, Lea SM, Tang CM, Pizza M, Savino S, Norais N, Rappuoli R, Bottomley MJ, Masignani V. </i> Proc Natl Acad Sci U S A, 2013","date":"2022-02-10T12:52:20.027Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2YPV"}],"region_id":"DP03600r004","sample":[{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ABCD","id":"ABCD_AG710","statements":[{"type":"Supplementary material","text":"For the purpose of cocrystallization, the complex of fHbp with Fab 12C1 was prepared by coincubation at 4 °C followed by preparative size-exclusion chromatography in 20 mM Tris·HCl and 150 mM NaCl, pH 8.0, using a Superdex 75 (16/60) column (GE Healthcare)."}]}],"statement":[{"text":"The region is folded in the pdb but not mentioned in the article.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:48:33.075Z"}},{"start":34,"end":48,"reference_id":"23396847","reference_source":"pmid","reference_html":"Defining a protective epitope on factor H binding protein, a key meningococcal virulence factor and vaccine antigen. <i> Malito E, Faleri A, Lo Surdo P, Veggi D, Maruggi G, Grassi E, Cartocci E, Bertoldi I, Genovese A, Santini L, Romagnoli G, Borgogni E, Brier S, Lo Passo C, Domina M, Castellino F, Felici F, van der Veen S, Johnson S, Lea SM, Tang CM, Pizza M, Savino S, Norais N, Rappuoli R, Bottomley MJ, Masignani V. </i> Proc Natl Acad Sci U S A, 2013","date":"2022-02-10T12:54:10.172Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2YPV"}],"region_id":"DP03600r005","sample":[{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"ABCD_AG710","statements":[{"type":"Supplementary material","text":"For the purpose of cocrystallization, the complex of fHbp with Fab 12C1 was prepared by coincubation at 4 °C followed by preparative size-exclusion chromatography in 20 mM Tris·HCl and 150 mM NaCl, pH 8.0, using a Superdex 75 (16/60) column (GE Healthcare)."}]}],"statement":[{"text":"The region is folded in the pdb but was disordered in absence of the antibody.","type":"Curator statement"}],"states_connection":[{"source":"DP03600r002","target":"DP03600r004"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:48:34.457Z"}}],"regions_counter":5,"released":"2023_12","sequence":"MNRTAFCCLSLTTALILTACSSGGGGVAADIGAGLADALTAPLDHKDKGLQSLTLDQSVRKNEKLKLAAQGAEKTYGNGDSLNTGKLKNDKVSRFDFIRQIEVDGQLITLESGEFQVYKQSHSALTAFQTEQIQDSEHSGKMVAKRQFRIGDIAGEHTSFDKLPEGGRATYRGTAFGSDDAGGKLTYTIDFAAKQGNGKIEHLKSPELNVDLAAADIKPDGKRHAVISGSVLYNQAEKGSYSLGIFGGKAQEVAGSAEVKTVNGIRHIGLAAKQ","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"genes":[{"name":{"value":"fhbP"},"olnNames":[{"value":"NMB1870"}]}],"alphafold_very_low_content":0.228125,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.10583941605839416,"disprot_consensus":{"full":[{"start":20,"end":33,"type":"D"},{"start":34,"end":48,"type":"T"}],"Structural state":[{"start":20,"end":48,"type":"D"}],"Structural transition":[{"start":34,"end":48,"type":"T"}]}},{"disprot_id":"DP03601","acc":"Q9JXP1","creator":"esalladini","date":"2022-02-10T13:04:57.080Z","features":{"pfam":[{"id":"PF01464","name":"Transglycosylase SLT domain","start":460,"end":564},{"id":"PF14718","name":"Soluble lytic murein transglycosylase L domain","start":399,"end":438},{"id":"PF27553","name":"Soluble lytic transglycosylase helical domain","start":575,"end":600}],"gene3D":[]},"length":616,"name":"Putative soluble lytic murein transglycosylase","ncbi_taxon_id":122586,"organism":"Neisseria meningitidis serogroup B (strain MC58)","regions":[{"start":501,"end":516,"reference_id":"32022687","reference_source":"pmid","reference_html":"Defective lytic transglycosylase disrupts cell morphogenesis by hindering cell wall de-<i>O</i>-acetylation in <i>Neisseria meningitidis</i>. <i> Williams AH, Wheeler R, Deghmane AE, Santecchia I, Schaub RE, Hicham S, Moya Nilges M, Malosse C, Chamot-Rooke J, Haouz A, Dillard JP, Robins WP, Taha MK, Gomperts Boneca I. </i> Elife, 2020","date":"2022-02-10T13:23:03.763Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6H5F"}],"region_id":"DP03601r001","statement":[{"text":"In the course of monitoring the LtgA reaction in the crystalline state, we captured a native version of LtgA with a distinctly disordered alpha helix 30 (Figure 1a–b, Video 1).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:49:24.860Z"}},{"start":1,"end":40,"reference_id":"32022687","reference_source":"pmid","reference_html":"Defective lytic transglycosylase disrupts cell morphogenesis by hindering cell wall de-<i>O</i>-acetylation in <i>Neisseria meningitidis</i>. <i> Williams AH, Wheeler R, Deghmane AE, Santecchia I, Schaub RE, Hicham S, Moya Nilges M, Malosse C, Chamot-Rooke J, Haouz A, Dillard JP, Robins WP, Taha MK, Gomperts Boneca I. </i> Elife, 2020","date":"2022-02-10T13:22:51.833Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6H5F"}],"region_id":"DP03601r002","statement":[{"text":"The N-t is missing from the structure.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:49:25.334Z"}},{"start":501,"end":516,"reference_id":"32022687","reference_source":"pmid","reference_html":"Defective lytic transglycosylase disrupts cell morphogenesis by hindering cell wall de-<i>O</i>-acetylation in <i>Neisseria meningitidis</i>. <i> Williams AH, Wheeler R, Deghmane AE, Santecchia I, Schaub RE, Hicham S, Moya Nilges M, Malosse C, Chamot-Rooke J, Haouz A, Dillard JP, Robins WP, Taha MK, Gomperts Boneca I. </i> Elife, 2020","date":"2022-02-10T13:50:45.131Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6H5F"}],"region_id":"DP03601r003","statement":[{"text":"In the course of monitoring the LtgA reaction in the crystalline state, we captured a native version of LtgA with a distinctly disordered alpha helix 30 (Figure 1a–b, Video 1). This represents a newly identified conformational state of LtgA whereby alpha helix 30 transitions from an ordered to a disordered state (Figure 1a–b).","type":"Results"}],"states_connection":[{"source":"DP03601r005","target":"DP03601r001"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:49:36.736Z"}},{"start":501,"end":516,"reference_id":"32022687","reference_source":"pmid","reference_html":"Defective lytic transglycosylase disrupts cell morphogenesis by hindering cell wall de-<i>O</i>-acetylation in <i>Neisseria meningitidis</i>. <i> Williams AH, Wheeler R, Deghmane AE, Santecchia I, Schaub RE, Hicham S, Moya Nilges M, Malosse C, Chamot-Rooke J, Haouz A, Dillard JP, Robins WP, Taha MK, Gomperts Boneca I. </i> Elife, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0003824","term_name":"catalytic activity","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"region_id":"DP03601r004","statement":[{"text":"LtgA is involved in maintaining the structural composition of the peptidoglycan","type":"Results"},{"text":"However, the PG of the ΔltgAltgAΔ30 strain was found to be markedly hyperacetylated when compared to that of the other strains, with a 102% increase in the amount of acetylated GlcNAc-anhMurNAc-tetrapeptide (GM*4), a 39% increase in acetylated GlcNAc-anhMurNAc-tetrapeptide crosslinked with GlcNAc-MurNAc-tetrapeptide (GM*4-GM4), and a 46% increase in doubly acetylated di-GlcNAc-anhMurNAc-tetrapeptide (GM*4 GM*4) (Figure 4, Figure 4b).","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.\" [GOC:vw, ISBN:0198506732]","disprot_namespace":"Disorder function","term_is_binding":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:49:38.264Z"}},{"start":501,"end":516,"reference_id":"29483188","reference_source":"pmid","reference_html":"A step-by-step <b><i>in crystallo</i></b> guide to bond cleavage and 1,6-anhydro-sugar product synthesis by a peptidoglycan-degrading lytic transglycosylase. <i> Williams AH, Wheeler R, Rateau L, Malosse C, Chamot-Rooke J, Haouz A, Taha MK, Boneca IG. </i> J Biol Chem, 2018","date":"2022-02-10T13:49:06.470Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6FPN"},{"db":"PDB","id":"5O2N"},{"db":"PDB","id":"5O24"},{"db":"PDB","id":"5O29"},{"db":"PDB","id":"5O1J"}],"region_id":"DP03601r005","statement":[{"text":"The architecture of the active site of LtgA is formed by a total of 10 α-helices (α28, α29, α30, α31, α32, α33, α34, α35, α36, and α37; Fig. S2, a–d). A six-helix bundle (α29, α30, α31, α32, α33, and α34) constitutes the active site core, which secures the glycan chain.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:49:35.095Z"}}],"regions_counter":5,"released":"2023_12","sequence":"MYLPSMKHSLPLLAALVLAACSSTNTLPAGKTPADNIETADLSASVPTRPAEPERKTLADYGGYPSALDAVKQKNDAAVAAYLENAGDSAMAENVRNEWLKSLGARRQWTLFAQEYAKLEPAGRAQEVECYADSSRNDYTRAAELVKNTGKLPSGCTKLLEQAAASGLLDGNDAWRRVRGLLAGRQTTDARNLAAALGSPFDGGTQGSREYALLNVIGKEARKSPNAAALLSEMESGLSLEQRSFAWGVLGHYQSQNLNVPAALDYYGKVADRRQLTDDQIEWYARAALRARRWDELASVISHMPEKLQKSPTWLYWLARSRAATGNTQEAEKLYKQAAATGRNFYAVLAGEELGRKIDTRNNVPDAGKNSVRRMAEDGAVKRALVLFQNSQSAGDAKMRRQAQAEWRFATRGFDEDKLLTAAQTAFDHGFYDMAVNSAERTDRKLNYTLRYISPFKDTVIRHAQNVNVDPAWVYGLIRQESRFVIGAQSRVGAQGLMQVMPATAREIAGKIGMDAAQLYTADGNIRMGTWYMADTKRRLQNNEVLATAGYNAGPGRARRWQADTPLEGAVYAETIPFSETRDYVKKVMANAAYYAALFGAPHIPLKQRMGIVPAR","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"genes":[{"olnNames":[{"value":"NMB1949","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF42278.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF42278.1"}}]}]}],"alphafold_very_low_content":0.05519480519480519,"disorder_content":0.09090909090909091,"disprot_consensus":{"full":[{"start":1,"end":40,"type":"D"},{"start":501,"end":516,"type":"T"}],"Structural state":[{"start":1,"end":40,"type":"D"},{"start":501,"end":516,"type":"D"}],"Structural transition":[{"start":501,"end":516,"type":"T"}],"Molecular function":[{"start":501,"end":516,"type":"F"}]}},{"disprot_id":"DP03604","acc":"Q93EK7","creator":"esalladini","date":"2022-02-14T14:30:06.148Z","features":{"pfam":[{"id":"PF01501","name":"Glycosyl transferase family 8","start":3,"end":255}],"gene3D":[]},"length":311,"name":"LgtC","ncbi_taxon_id":487,"organism":"Neisseria meningitidis","regions":[{"start":283,"end":311,"reference_id":"15075344","reference_source":"pmid","reference_html":"Intermediate trapping on a mutant retaining alpha-galactosyltransferase identifies an unexpected aspartate residue. <i> Lairson LL, Chiu CP, Ly HD, He S, Wakarchuk WW, Strynadka NC, Withers SG. </i> J Biol Chem, 2004","date":"2022-02-14T14:43:34.549Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gln189Glu","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"1SS9"}],"region_id":"DP03604r001","sequence_construct":"MDIVFAADDNYAAYLCVAAKSVEAAHPDTEIRFHVLDAGISEANRAAVAANLRGGGGNIRFIDVNPEDFAGFPLNIRHISITTYARLKLGEYIADCDKVLYLDIDVLVRDSLTPLWDTDLGDNWLGACIDLFVERQEGYKQKIGMADGEYYFNAGVLLINLKKWRRHDIFKMSCEWVEQYKDVMQYQDEDILNGLFKGGVCYANSRFNFMPTNYAFMANRFASRHTDPLYRDRTNTVMPVAVSHYCGPAKPWHRDCTAWGAERFTELAGSLTTVPEEWRGKLAVPHRMFSTKRMLQRWRRKLSARFLRKIY","statement":[{"text":"The protein C-t is missing from the pdb structure.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-23T14:18:07.306Z"}},{"start":283,"end":311,"reference_id":"15075344","reference_source":"pmid","reference_html":"Intermediate trapping on a mutant retaining alpha-galactosyltransferase identifies an unexpected aspartate residue. <i> Lairson LL, Chiu CP, Ly HD, He S, Wakarchuk WW, Strynadka NC, Withers SG. </i> J Biol Chem, 2004","date":"2022-02-16T14:31:59.997Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1SS9"}],"region_id":"DP03604r002","statement":[{"text":"The protein C-t is missing from the pdb structure.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:49:55.378Z"}}],"regions_counter":2,"released":"2023_12","sequence":"MDIVFAADDNYAAYLCVAAKSVEAAHPDTEIRFHVLDAGISEANRAAVAANLRGGGGNIRFIDVNPEDFAGFPLNIRHISITTYARLKLGEYIADCDKVLYLDIDVLVRDSLTPLWDTDLGDNWLGACIDLFVERQEGYKQKIGMADGEYYFNAGVLLINLKKWRRHDIFKMSCEWVEQYKDVMQYQDQDILNGLFKGGVCYANSRFNFMPTNYAFMANRFASRHTDPLYRDRTNTVMPVAVSHYCGPAKPWHRDCTAWGAERFTELAGSLTTVPEEWRGKLAVPHRMFSTKRMLQRWRRKLSARFLRKIY","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"genes":[{"name":{"value":"lgtC","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAL12839.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAL12839.1"}}]}}],"alphafold_very_low_content":0.04501607717041801,"disorder_content":0.0932475884244373,"disprot_consensus":{"full":[{"start":283,"end":311,"type":"D"}],"Structural state":[{"start":283,"end":311,"type":"D"}],"Disorder function":[{"start":283,"end":311,"type":"F"}]}},{"disprot_id":"DP03605","acc":"Q9JZ55","creator":"esalladini","date":"2022-02-14T15:05:14.810Z","features":{"pfam":[{"id":"PF00793","name":"DAHP synthetase I family","start":5,"end":272}],"gene3D":[]},"length":280,"name":"2-dehydro-3-deoxyphosphooctonate aldolase","ncbi_taxon_id":122586,"organism":"Neisseria meningitidis serogroup B (strain MC58)","regions":[{"start":238,"end":250,"reference_id":"21438567","reference_source":"pmid","reference_html":"Targeting the role of a key conserved motif for substrate selection and catalysis by 3-deoxy-D-manno-octulosonate 8-phosphate synthase. <i> Allison TM, Hutton RD, Cochrane FC, Yeoman JA, Jameson GB, Parker EJ. </i> Biochemistry, 2011","date":"2022-02-14T15:26:21.017Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3QPY"},{"db":"PDB","id":"3QQ0"},{"db":"PDB","id":"3QQ1"},{"db":"PDB","id":"3QPZ"}],"region_id":"DP03605r001","statement":[{"text":"As in the wild-type structure, loops β7α7 and β8α8 are disordered, showing noncontinuous electron density.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:51:01.782Z"}},{"start":240,"end":250,"reference_id":"23746359","reference_source":"pmid","reference_html":"Examining the role of intersubunit contacts in catalysis by 3-deoxy-d-manno-octulosonate 8-phosphate synthase. <i> Allison TM, Cochrane FC, Jameson GB, Parker EJ. </i> Biochemistry, 2013","date":"2022-02-15T09:31:16.159Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4JTL"},{"db":"PDB","id":"4JTF"},{"db":"PDB","id":"4JTE"},{"db":"PDB","id":"4JTK"},{"db":"PDB","id":"4JTI"},{"db":"PDB","id":"4JTJ"},{"db":"PDB","id":"4JTG"}],"region_id":"DP03605r002","statement":[{"text":"The β8-α8 loop (240-250) is missing from the pdb structures due to its flexibility.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:51:02.538Z"}}],"regions_counter":2,"released":"2023_12","sequence":"MDIKINDITLGNNSPFVLFGGINVLESLDSTLQTCAHYVEVTRKLGIPYIFKASFDKANRSSIHSYRGVGLEEGLKIFEKVKAEFGIPVITDVHEPHQCQPVAEVCDVIQLPAFLARQTDLVVAMAKTGNVVNIKKPQFLSPSQMKNIVEKFHEAGNGKLILCERGSSFGYDNLVVDMLGFGVMKQTCGNLPVIFDVTHSLQTRDAGSAASGGRRAQALDLALAGMATRLAGLFLESHPDPKLAKCDGPSALPLHLLEDFLIRIKALDDLIKSQPILTIE","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"genes":[{"name":{"value":"kdsA","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00056","url":"https://hamap.expasy.org/unirule/MF_00056"}}]},"olnNames":[{"value":"NMB1283"}]}],"alphafold_very_low_content":0,"disorder_content":0.04642857142857143,"disprot_consensus":{"full":[{"start":238,"end":250,"type":"D"}],"Structural state":[{"start":238,"end":250,"type":"D"}]}},{"disprot_id":"DP03606","acc":"P0CE18","creator":"fquaglia","date":"2022-02-15T09:14:43.380Z","features":{"pfam":[{"id":"PF05475","name":"Pgp3 C-terminal domain","start":119,"end":264},{"id":"PF20857","name":"Immunodominant antigen Pgp3, helical domain","start":72,"end":110},{"id":"PF20858","name":"Immunodominant antigen Pgp3, N-terminal domain","start":1,"end":68}],"gene3D":[]},"length":264,"name":"Virulence plasmid protein pGP3-D","ncbi_taxon_id":813,"organism":"Chlamydia trachomatis","regions":[{"start":20,"end":99,"reference_id":"30002845","reference_source":"pmid","reference_html":"Chlamydia protein Pgp3 studied at high resolution in a new crystal form. <i> Khurshid S, Govada L, Wills G, McClure MO, Helliwell JR, Chayen NE. </i> IUCrJ, 2018","date":"2022-02-15T09:56:56.575Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6GJT"}],"region_id":"DP03606r001","statement":[{"text":"Since the threefold axes of the THCC and NTD are not collinear with the threefold axis of a CTD, this naturally leads to disorder in the THCC and the portion of the NTD that does not directly interact with the CTD via crystal packing. ","type":"Abstract"},{"text":"The PDB’s validation RSRZ score corroborates the disorder observed in residues 20–99. The disorder becomes a progressive effect when moving away from the interface of the CTD and NTD.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-15T11:43:52.803Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":91,"end":99,"reference_id":"30002845","reference_source":"pmid","reference_html":"Chlamydia protein Pgp3 studied at high resolution in a new crystal form. <i> Khurshid S, Govada L, Wills G, McClure MO, Helliwell JR, Chayen NE. </i> IUCrJ, 2018","date":"2022-02-15T10:02:53.768Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP03606r002","statement":[{"text":"Since the threefold axes of the THCC and NTD are not collinear with the threefold axis of a CTD, this naturally leads to disorder in the THCC and the portion of the NTD that does not directly interact with the CTD via crystal packing. ","type":"Abstract"},{"text":"The PDB’s validation RSRZ score corroborates the disorder observed in residues 20–99. The disorder becomes a progressive effect when moving away from the interface of the CTD and NTD.","type":"Figure"},{"text":"THCC connecting NTD and CTD.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-15T15:23:27.300Z"},"ec_go":"EXP","disprot_namespace":"Disorder function"}],"regions_counter":2,"released":"2023_06","sequence":"MGNSGFYLYNTQNCVFADNIKVGQMTEPLKDQQIILGTTSTPVAAKMTASDGISLTVSNNPSTNASITIGLDAEKAYQLILEKLGDQILGGIADTIVDSTVQDILDKITTDPSLGLLKAFNNFPITNKIQCNGLFTPRNIETLLGGTEIGKFTVTPKSSGSMFLVSADIIASRMEGGVVLALVREGDSKPYAISYGYSSGVPNLCSLRTRIINTGLTPTTYSLRVGGLESGVVWVNALSNGNDILGITNTSNVSFLEVIPQTNA","taxonomy":["Bacteria","Chlamydiae","Chlamydiales","Chlamydiaceae","Chlamydia/Chlamydophila group","Chlamydia"],"dataset":["Neglected tropical diseases proteins"],"genes":[],"alphafold_very_low_content":0,"disorder_content":0.30303030303030304,"disprot_consensus":{"full":[{"start":20,"end":99,"type":"D"}],"Structural state":[{"start":20,"end":99,"type":"D"}],"Disorder function":[{"start":91,"end":99,"type":"F"}]}},{"disprot_id":"DP03607","acc":"Q9K169","creator":"esalladini","date":"2022-02-15T10:16:45.910Z","features":{"pfam":[{"id":"PF00793","name":"DAHP synthetase I family","start":43,"end":335}],"gene3D":[]},"length":351,"name":"Phospho-2-dehydro-3-deoxyheptonate aldolase","ncbi_taxon_id":122586,"organism":"Neisseria meningitidis serogroup B (strain MC58)","regions":[{"start":1,"end":14,"reference_id":"25245459","reference_source":"pmid","reference_html":"Structural analysis of substrate-mimicking inhibitors in complex with Neisseria meningitidis 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase - The importance of accommodating the active site water. <i> Heyes LC, Reichau S, Cross PJ, Jameson GB, Parker EJ. </i> Bioorg Chem, 2014","date":"2022-02-15T10:21:20.586Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4UMB"},{"db":"PDB","id":"4UMC"},{"db":"PDB","id":"4UMA"}],"region_id":"DP03607r001","statement":[{"text":"In all structures, no electron density for the 14 amino acids at the N-terminus of each NmeDAH7PS chain could be found, which is attributed to these residues being part of a conformationally highly flexible allosteric binding loop [17].","type":"Methods"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:51:06.217Z"}},{"start":1,"end":14,"reference_id":"25245459","reference_source":"pmid","reference_html":"Structural analysis of substrate-mimicking inhibitors in complex with Neisseria meningitidis 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase - The importance of accommodating the active site water. <i> Heyes LC, Reichau S, Cross PJ, Jameson GB, Parker EJ. </i> Bioorg Chem, 2014","date":"2022-02-16T14:33:14.682Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4UMA"},{"db":"PDB","id":"4UMC"},{"db":"PDB","id":"4UMB"}],"region_id":"DP03607r002","statement":[{"text":"In all structures, no electron density for the 14 amino acids at the N-terminus of each NmeDAH7PS chain could be found, which is attributed to these residues being part of a conformationally highly flexible allosteric binding loop [17].","type":"Methods"}],"ec_go":"EXP","disprot_namespace":"Disorder function","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:51:07.699Z"}}],"regions_counter":2,"released":"2023_12","sequence":"MTHHYPTDDIKIKEVKELLPPIAHLYELPISKEASGLVHRTRQEISDLVHGRDKRLLVIIGPCSIHDPKAALEYAERLLKLRKQYENELLIVMRVYFEKPRTTVGWKGLINDPHLDGTFDINFGLRQARSLLLSLNNMGMPASTEFLDMITPQYYADLISWGAIGARTTESQVHRELASGLSCPVGFKNGTDGNLKIAIDAIGAASHSHHFLSVTKAGHSAIVHTGGNPDCHVILRGGKEPNYDAEHVSEAAEQLRAAGVTDKLMIDCSHANSRKDYTRQMEVAQDIAAQLEQDGGNIMGVMVESHLVEGRQDKPEVYGKSITDACIGWGATEELLALLAGANKKRMARAS","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"genes":[{"name":{"value":"aroG","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF40753.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF40753.1"}}]},"olnNames":[{"value":"NMB0307","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF40753.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF40753.1"}}]}]}],"alphafold_very_low_content":0,"disorder_content":0.039886039886039885,"disprot_consensus":{"full":[{"start":1,"end":14,"type":"D"}],"Structural state":[{"start":1,"end":14,"type":"D"}],"Disorder function":[{"start":1,"end":14,"type":"F"}]}},{"disprot_id":"DP03608","acc":"A6YID9","creator":"fquaglia","date":"2022-02-15T10:27:16.658Z","features":{"pfam":[{"id":"PF00031","name":"Cystatin domain","start":77,"end":128}],"gene3D":[]},"length":136,"name":"Cystatin-1","ncbi_taxon_id":79923,"organism":"Clonorchis sinensis","regions":[{"start":1,"end":38,"reference_id":"29499196","reference_source":"pmid","reference_html":"Structural basis of the cystein protease inhibitor Clonorchis sinensis Stefin-1. <i> Park SY, Jeong MS, Park SA, Ha SC, Na BK, Jang SB. </i> Biochem Biophys Res Commun, 2018","date":"2022-02-15T15:27:06.155Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03608r001","statement":[{"text":"The structure of CsStefin-1 was determined in amino acid residues 39–136 because the electron density for residues 28–38 on the loop region was poor.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"5ZC1"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-15T15:30:26.913Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_12","sequence":"MTSTRLAFAWRELFSVFCYLLYTSDILAERHNNHPVMPICGGISAARIPTADEKKKLEPVLLQSLYAHLGSKPTSAEVVLVATQVVAGTNYFAKVKVNNDHYIHTRVYEQLPCYGGALELHSVQMNKTDTDPLDYF","taxonomy":["Eukaryota","Metazoa","Spiralia","Lophotrochozoa","Platyhelminthes","Trematoda","Digenea","Opisthorchiida","Opisthorchiata","Opisthorchiidae","Clonorchis"],"genes":[],"alphafold_very_low_content":0.13970588235294118,"dataset":["Neglected tropical diseases proteins"],"disorder_content":0.27941176470588236,"disprot_consensus":{"full":[{"start":1,"end":38,"type":"D"}],"Structural state":[{"start":1,"end":38,"type":"D"}]}},{"disprot_id":"DP03609","acc":"H2L2M0","creator":"fquaglia","date":"2022-02-15T10:30:06.539Z","features":{"pfam":[],"gene3D":[]},"length":117,"name":"Saposin-like protein","ncbi_taxon_id":51031,"organism":"Necator americanus","regions":[{"start":91,"end":117,"reference_id":"21991310","reference_source":"pmid","reference_html":"Insights into the membrane interactions of the saposin-like proteins Na-SLP-1 and Ac-SLP-1 from human and dog hookworm. <i> Willis C, Wang CK, Osman A, Simon A, Pickering D, Mulvenna J, Riboldi-Tunicliffe A, Jones MK, Loukas A, Hofmann A. </i> PLoS One, 2011","date":"2022-02-15T15:27:36.640Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3S63"}],"region_id":"DP03609r001","statement":[{"text":"In the crystal structure of Na-SLP-1, the C-terminal extension of about 30 amino acids, which is attached to the N-terminal Sap domain could not be resolved, which agrees with the results from mass spectrometry.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-15T15:30:14.250Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":91,"end":117,"reference_id":"21991310","reference_source":"pmid","reference_html":"Insights into the membrane interactions of the saposin-like proteins Na-SLP-1 and Ac-SLP-1 from human and dog hookworm. <i> Willis C, Wang CK, Osman A, Simon A, Pickering D, Mulvenna J, Riboldi-Tunicliffe A, Jones MK, Loukas A, Hofmann A. </i> PLoS One, 2011","date":"2022-02-15T10:36:51.375Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP03609r002","statement":[{"text":"Mass spectrometry of Na-SLP-1 indicates that the protein degrades over time, whereas Ac-SLP-1 remains intact (9531 g/mol; theoretical M = 9531 g/mol).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-15T15:30:13.049Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2023_06","sequence":"LTPKETCDLCQIALRTVFGHFGGNIPSRRKLVHQLKHECKRHFNYRRRCLLLMKVNSDLIFREMTDGSFKPMEVCLIMRECNPHDSPLEPEMIDKSGQPEAFALVSSSDDNYDTSEE","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Strongylida","Ancylostomatoidea","Ancylostomatidae","Bunostominae","Necator"],"dataset":["Neglected tropical diseases proteins"],"genes":[],"alphafold_very_low_content":0.13675213675213677,"disorder_content":0.23076923076923078,"disprot_consensus":{"full":[{"start":91,"end":117,"type":"D"}],"Structural state":[{"start":91,"end":117,"type":"D"}]}},{"disprot_id":"DP03610","acc":"O76744","creator":"fquaglia","date":"2022-02-15T10:41:30.298Z","features":{"pfam":[{"id":"PF00188","name":"Cysteine-rich secretory protein family","start":41,"end":177},{"id":"PF00188","name":"Cysteine-rich secretory protein family","start":242,"end":387}],"gene3D":[]},"length":424,"name":"Ancylostoma secreted protein 1","ncbi_taxon_id":51031,"organism":"Necator americanus","regions":[{"start":1,"end":23,"reference_id":"21543848","reference_source":"pmid","reference_html":"Structure of a two-CAP-domain protein from the human hookworm parasite Necator americanus. <i> Asojo OA. </i> Acta Crystallogr D Biol Crystallogr, 2011","date":"2022-02-15T15:27:19.678Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP03610r001","statement":[{"text":"Disordered region comprising the protein signal peptide.","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"3NT8"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-15T15:30:19.764Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_06","sequence":"MFSPVVVSVVFTIAFCNASPARDSFGCSNSGITDSDRQAFLDFHNNARRRVAKGLEDSNSGKLNPAKNMYKLSWDCAMEQQLQDAIQSCPSGFAGIQGVAQNTMSWSSSGGYPDPSVKIEPTLSGWWSGAKKNGVGPDNKYTGGGLFAFSNMVYSETTKLGCAYKVCGTKLAVSCIYNGVGYITNQPMWETGQACQTGADCSTYKNSGCEDGLCTKGPDVPETNQQCPSNTGMTDSVRDTFLSVHNEFRSSVARGLEPDALGGNAPKAAKMLKMVYDCEVEASAIRHGNKCVYQHSHGEDRPGLGENIYKTSVLKFDKNKAAKQASQLWWNELKEYGVGPSNVLTTALWNRPNMQIGHYTQMAWDTTYKLGCAVVFCNDFTFGVCQYGPGGNYMGHVIYTMGQPCSQCSPGATCSVTEGLCSAP","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Strongylida","Ancylostomatoidea","Ancylostomatidae","Bunostominae","Necator"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"name":{"value":"asp1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAD13340.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD13340.1"}}]}}],"alphafold_very_low_content":0.049528301886792456,"disorder_content":0.054245283018867926,"disprot_consensus":{"full":[{"start":1,"end":23,"type":"D"}],"Structural state":[{"start":1,"end":23,"type":"D"}]}},{"disprot_id":"DP03611","acc":"Q9JZN9","creator":"esalladini","date":"2022-02-15T10:44:55.094Z","features":{"pfam":[{"id":"PF00593","name":"TonB dependent receptor-like, beta-barrel","start":320,"end":728},{"id":"PF07715","name":"TonB-dependent Receptor Plug Domain","start":54,"end":154}],"gene3D":[]},"length":758,"name":"Probable TonB-dependent receptor NMB0964","ncbi_taxon_id":122586,"organism":"Neisseria meningitidis serogroup B (strain MC58)","regions":[{"start":267,"end":323,"reference_id":"26282243","reference_source":"pmid","reference_html":"The molecular mechanism of Zinc acquisition by the neisserial outer-membrane transporter ZnuD. <i> Calmettes C, Ing C, Buckwalter CM, El Bakkouri M, Chieh-Lin Lai C, Pogoutse A, Gray-Owen SD, Pomès R, Moraes TF. </i> Nat Commun, 2015","date":"2022-02-15T11:07:17.715Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4RVW"}],"region_id":"DP03611r001","statement":[{"text":"On the other hand, soaking the rigid cadmium-bound conformation of ZnuD with free zinc increased the dynamic flexibility of the protruding loops on interaction with its metal substrate and furthermore identified a potential periplasmic zinc-binding site (Fig. 2c and Supplementary Fig. 5).","type":"Results"},{"text":"Together, resolution of three unique receptor intermediates illustrates the ability of ZnuD to capture its substrate using multiple binding sites on flexible loops and, ultimately, drag zinc ions towards a buried high-affinity binding site.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:51:12.095Z"}},{"start":267,"end":323,"reference_id":"26282243","reference_source":"pmid","reference_html":"The molecular mechanism of Zinc acquisition by the neisserial outer-membrane transporter ZnuD. <i> Calmettes C, Ing C, Buckwalter CM, El Bakkouri M, Chieh-Lin Lai C, Pogoutse A, Gray-Owen SD, Pomès R, Moraes TF. </i> Nat Commun, 2015","date":"2022-02-15T11:21:53.593Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4RDR"}],"region_id":"DP03611r002","statement":[{"text":"On the other hand, soaking the rigid cadmium-bound conformation of ZnuD with free zinc increased the dynamic flexibility of the protruding loops on interaction with its metal substrate and furthermore identified a potential periplasmic zinc-binding site (Fig. 2c and Supplementary Fig. 5).","type":"Results"},{"text":"Together, resolution of three unique receptor intermediates illustrates the ability of ZnuD to capture its substrate using multiple binding sites on flexible loops and, ultimately, drag zinc ions towards a buried high-affinity binding site.","type":"Results"},{"text":"The presence of zinc modulates the dynamic flexibility of the external loops by remodelling an α-helical segment into a pair of β-strand motifs (Fig. 2a,b).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:51:20.195Z"}},{"start":458,"end":480,"reference_id":"26282243","reference_source":"pmid","reference_html":"The molecular mechanism of Zinc acquisition by the neisserial outer-membrane transporter ZnuD. <i> Calmettes C, Ing C, Buckwalter CM, El Bakkouri M, Chieh-Lin Lai C, Pogoutse A, Gray-Owen SD, Pomès R, Moraes TF. </i> Nat Commun, 2015","date":"2022-02-15T11:19:53.388Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4RVW"}],"region_id":"DP03611r003","statement":[{"text":"On the other hand, soaking the rigid cadmium-bound conformation of ZnuD with free zinc increased the dynamic flexibility of the protruding loops on interaction with its metal substrate and furthermore identified a potential periplasmic zinc-binding site (Fig. 2c and Supplementary Fig. 5).","type":"Results"},{"text":"Together, resolution of three unique receptor intermediates illustrates the ability of ZnuD to capture its substrate using multiple binding sites on flexible loops and, ultimately, drag zinc ions towards a buried high-affinity binding site.","type":"Results"},{"text":"The presence of zinc modulates the dynamic flexibility of the external loops by remodelling an α-helical segment into a pair of β-strand motifs (Fig. 2a,b).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:51:14.297Z"}},{"start":458,"end":480,"reference_id":"26282243","reference_source":"pmid","reference_html":"The molecular mechanism of Zinc acquisition by the neisserial outer-membrane transporter ZnuD. <i> Calmettes C, Ing C, Buckwalter CM, El Bakkouri M, Chieh-Lin Lai C, Pogoutse A, Gray-Owen SD, Pomès R, Moraes TF. </i> Nat Commun, 2015","date":"2022-02-15T11:23:35.432Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4RDR"}],"region_id":"DP03611r004","statement":[{"text":"On the other hand, soaking the rigid cadmium-bound conformation of ZnuD with free zinc increased the dynamic flexibility of the protruding loops on interaction with its metal substrate and furthermore identified a potential periplasmic zinc-binding site (Fig. 2c and Supplementary Fig. 5).","type":"Results"},{"text":"Together, resolution of three unique receptor intermediates illustrates the ability of ZnuD to capture its substrate using multiple binding sites on flexible loops and, ultimately, drag zinc ions towards a buried high-affinity binding site.","type":"Results"},{"text":"The presence of zinc modulates the dynamic flexibility of the external loops by remodelling an α-helical segment into a pair of β-strand motifs (Fig. 2a,b).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:51:22.058Z"}},{"start":635,"end":651,"reference_id":"26282243","reference_source":"pmid","reference_html":"The molecular mechanism of Zinc acquisition by the neisserial outer-membrane transporter ZnuD. <i> Calmettes C, Ing C, Buckwalter CM, El Bakkouri M, Chieh-Lin Lai C, Pogoutse A, Gray-Owen SD, Pomès R, Moraes TF. </i> Nat Commun, 2015","date":"2022-02-15T11:24:58.934Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4RVW"}],"region_id":"DP03611r005","statement":[{"text":"On the other hand, soaking the rigid cadmium-bound conformation of ZnuD with free zinc increased the dynamic flexibility of the protruding loops on interaction with its metal substrate and furthermore identified a potential periplasmic zinc-binding site (Fig. 2c and Supplementary Fig. 5).","type":"Results"},{"text":"Together, resolution of three unique receptor intermediates illustrates the ability of ZnuD to capture its substrate using multiple binding sites on flexible loops and, ultimately, drag zinc ions towards a buried high-affinity binding site.","type":"Results"},{"text":"The presence of zinc modulates the dynamic flexibility of the external loops by remodelling an α-helical segment into a pair of β-strand motifs (Fig. 2a,b).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:51:16.708Z"}},{"start":635,"end":651,"reference_id":"26282243","reference_source":"pmid","reference_html":"The molecular mechanism of Zinc acquisition by the neisserial outer-membrane transporter ZnuD. <i> Calmettes C, Ing C, Buckwalter CM, El Bakkouri M, Chieh-Lin Lai C, Pogoutse A, Gray-Owen SD, Pomès R, Moraes TF. </i> Nat Commun, 2015","date":"2022-02-15T11:25:36.686Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4RDR"}],"region_id":"DP03611r006","statement":[{"text":"On the other hand, soaking the rigid cadmium-bound conformation of ZnuD with free zinc increased the dynamic flexibility of the protruding loops on interaction with its metal substrate and furthermore identified a potential periplasmic zinc-binding site (Fig. 2c and Supplementary Fig. 5).","type":"Results"},{"text":"Together, resolution of three unique receptor intermediates illustrates the ability of ZnuD to capture its substrate using multiple binding sites on flexible loops and, ultimately, drag zinc ions towards a buried high-affinity binding site.","type":"Results"},{"text":"The presence of zinc modulates the dynamic flexibility of the external loops by remodelling an α-helical segment into a pair of β-strand motifs (Fig. 2a,b).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural transition","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:51:24.262Z"}},{"start":25,"end":41,"reference_id":"26282243","reference_source":"pmid","reference_html":"The molecular mechanism of Zinc acquisition by the neisserial outer-membrane transporter ZnuD. <i> Calmettes C, Ing C, Buckwalter CM, El Bakkouri M, Chieh-Lin Lai C, Pogoutse A, Gray-Owen SD, Pomès R, Moraes TF. </i> Nat Commun, 2015","date":"2022-02-15T11:29:07.367Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4RDR"},{"db":"PDB","id":"4RVW"},{"db":"PDB","id":"4RDT"}],"region_id":"DP03611r007","statement":[{"text":"The N-t domain is disordered in the crystal structure.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:51:18.752Z"}},{"start":265,"end":275,"reference_id":"26282243","reference_source":"pmid","reference_html":"The molecular mechanism of Zinc acquisition by the neisserial outer-membrane transporter ZnuD. <i> Calmettes C, Ing C, Buckwalter CM, El Bakkouri M, Chieh-Lin Lai C, Pogoutse A, Gray-Owen SD, Pomès R, Moraes TF. </i> Nat Commun, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"4RDR"}],"interaction_partner":[{"db":"ChEBI","id":"48775","partner_start":null,"partner_end":null}],"region_id":"DP03611r008","statement":[{"text":"Cluster #1 (241-HSHEYDDCHAD-251, coloured green) contains two cadmium-binding sites identified within the cadmium co-crystal structure of ZnuD.","type":"Figure"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:51:26.139Z"}},{"start":312,"end":322,"reference_id":"26282243","reference_source":"pmid","reference_html":"The molecular mechanism of Zinc acquisition by the neisserial outer-membrane transporter ZnuD. <i> Calmettes C, Ing C, Buckwalter CM, El Bakkouri M, Chieh-Lin Lai C, Pogoutse A, Gray-Owen SD, Pomès R, Moraes TF. </i> Nat Commun, 2015","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"4RDR"}],"interaction_partner":[{"db":"ChEBI","id":"48775","partner_start":null,"partner_end":null}],"region_id":"DP03611r009","statement":[{"text":"Snapshots from Supplementary Movie 1 illustrate the putative flexibility of the extracellular loop 3 during the MD simulations of ZnuD in lipid bilayer in the absence (a) and presence (b) of 100 mM ZnCl2. The extracellular loop 3 contains two clusters (coloured pink and green) previously suggested as putative zinc-binding sites13 due to the high percentage of histidine, aspartic and glutamic acid residues situated there (drawn in stick representation).","type":"Figure"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-13T20:51:27.955Z"}}],"regions_counter":9,"released":"2023_12","sequence":"MAQTTLKPIVLSILLINTPLLAQAHETEQSVDLETVSVVGKSRPRATSGLLHTSTASDKIISGDTLRQKAVNLGDALDGVPGIHASQYGGGASAPVIRGQTGRRIKVLNHHGETGDMADFSPDHAIMVDTALSQQVEILRGPVTLLYSSGNVAGLVDVADGKIPEKMPENGVSGELGLRLSSGNLEKLTSGGINIGLGKNFVLHTEGLYRKSGDYAVPRYRNLKRLPDSHADSQTGSIGLSWVGEKGFIGVAYSDRRDQYGLPAHSHEYDDCHADIIWQKSLINKRYLQLYPHLLTEEDIDYDNPGLSCGFHDDDNAHAHTHSGRPWIDLRNKRYELRAEWKQPFPGFEALRVHLNRNDYRHDEKAGDAVENFFNNQTQNARIELRHQPIGRLKGSWGVQYLQQKSSALSAISEAVKQPMLLDNKVQHYSFFGVEQANWDNFTLEGGVRVEKQKASIQYDKALIDRENYYNHPLPDLGAHRQTARSFALSGNWYFTPQHKLSLTASHQERLPSTQELYAHGKHVATNTFEVGNKHLNKERSNNIELALGYEGDRWQYNLALYRNRFGNYIYAQTLNDGRGPKSIEDDSEMKLVRYNQSGADFYGAEGEIYFKPTPRYRIGVSGDYVRGRLKNLPSLPGREDAYGNRPFIAQDDQNAPRVPAARLGFHLKASLTDRIDANLDYYRVFAQNKLARYETRTPGHHMLNLGANYRRNTRYGEWNWYVKADNLLNQSVYAHSSFLSDTPQMGRSFTGGVNVKF","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"genes":[{"olnNames":[{"value":"NMB0964"}]}],"alphafold_very_low_content":0.07651715039577836,"disorder_content":0.1503957783641161,"disprot_consensus":{"full":[{"start":25,"end":41,"type":"D"},{"start":265,"end":266,"type":"F"},{"start":267,"end":323,"type":"T"},{"start":458,"end":480,"type":"T"},{"start":635,"end":651,"type":"T"}],"Structural state":[{"start":25,"end":41,"type":"D"},{"start":267,"end":323,"type":"D"},{"start":458,"end":480,"type":"D"},{"start":635,"end":651,"type":"D"}],"Structural transition":[{"start":267,"end":323,"type":"T"},{"start":458,"end":480,"type":"T"},{"start":635,"end":651,"type":"T"}],"Molecular function":[{"start":265,"end":275,"type":"F"},{"start":312,"end":322,"type":"F"}]}},{"disprot_id":"DP03612","acc":"J9ULM6","creator":"fquaglia","date":"2022-02-15T10:49:26.350Z","features":{"pfam":[{"id":"PF00188","name":"Cysteine-rich secretory protein family","start":35,"end":177}],"gene3D":[]},"length":210,"name":"Ancylostoma secreted protein 2","ncbi_taxon_id":51031,"organism":"Necator americanus","regions":[{"start":1,"end":17,"reference_id":"24631931","reference_source":"pmid","reference_html":"Probing the equatorial groove of the hookworm protein and vaccine candidate antigen, Na-ASP-2. <i> Mason L, Tribolet L, Simon A, von Gnielinski N, Nienaber L, Taylor P, Willis C, Jones MK, Sternberg PW, Gasser RB, Loukas A, Hofmann A. </i> Int J Biochem Cell Biol, 2014","date":"2022-02-15T11:01:45.798Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4NUN"},{"db":"PDB","id":"4NUO"},{"db":"PDB","id":"4NUI"},{"db":"PDB","id":"4NUK"}],"region_id":"DP03612r001","statement":[{"text":"Region corresponding to the signal peptide of the protein and unstructured in the crystal structure, as mentioned in Table 1.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-15T11:47:28.786Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_06","sequence":"MMSSITCLVLLSIAAYSKAGCPDNGMSEEARQKFLEMHNSLRSSVALGQAKDGAGGNAPKAAKMKTMAYDCEVEKTAMNNAKQCVFKHSQPNQRKGLGENIFMSSDSGMDKAKAAEQASKAWFGELAEKGVGQNLKLTGGLFSRGVGHYTQMVWQETVKLGCYVEACSNMCYVVCQYGPAGNMMGKDIYEKGEPCSKCENCDKEKGLCSA","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Strongylida","Ancylostomatoidea","Ancylostomatidae","Bunostominae","Necator"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"name":{"value":"ASP2","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AFR68662.1","url":"https://www.ebi.ac.uk/ena/browser/view/AFR68662.1"}}]}}],"alphafold_very_low_content":0.07142857142857142,"disorder_content":0.08095238095238096,"disprot_consensus":{"full":[{"start":1,"end":17,"type":"D"}],"Structural state":[{"start":1,"end":17,"type":"D"}]}},{"disprot_id":"DP03613","acc":"P46434","creator":"fquaglia","date":"2022-02-15T11:09:32.077Z","features":{"pfam":[{"id":"PF02798","name":"Glutathione S-transferase, N-terminal domain","start":39,"end":101},{"id":"PF14497","name":"Glutathione S-transferase, C-terminal domain","start":131,"end":230}],"gene3D":[]},"length":235,"name":"Glutathione S-transferase 1","ncbi_taxon_id":6282,"organism":"Onchocerca volvulus","regions":[{"start":11,"end":33,"reference_id":"18258257","reference_source":"pmid","reference_html":"Structure of the extracellular glutathione S-transferase OvGST1 from the human pathogenic parasite Onchocerca volvulus. <i> Perbandt M, Höppner J, Burmeister C, Lüersen K, Betzel C, Liebau E. </i> J Mol Biol, 2008","date":"2022-02-15T11:10:42.158Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2HNL"}],"region_id":"DP03613r001","statement":[{"text":"The OvGST1 shows an N-terminal 25-amino-acid extension before sequence identity to other σ-class GSTs begins. The extension is not ordered and therefore not defined by the electron density; however, the crystal packing allows enough space to accommodate the extension within the gaps.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-15T11:40:14.291Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":1,"released":"2023_06","sequence":"FITMNFVVEAASSNANQAITSENSIKPKGKLQPQMEKYTLTYFNGRGRAEVIRLLFALANVSYEDNRITRDEWKYLKPRTPFGHVPMLNVSGNVLGESHAIELLLGGRFGLLGTNDWEEAKIMAVVLNIDELFQKLIPWTHEKNTTKKAELFRNLSESDVMPFLGRYEKFLKESTTGHIVGNKVSVADLTVFNMLMTLDDEVKLEEYPQLASFVNKIGQMPGIKEWIKKRPKTYF","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Spirurina","Spiruromorpha","Filarioidea","Onchocercidae","Onchocerca"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"name":{"value":"GST1"},"synonyms":[{"value":"GSTA"}]}],"alphafold_very_low_content":0.11063829787234042,"disorder_content":0.09787234042553192,"disprot_consensus":{"full":[{"start":11,"end":33,"type":"D"}],"Structural state":[{"start":11,"end":33,"type":"D"}]}},{"disprot_id":"DP03614","acc":"Q7DDR9","creator":"esalladini","date":"2022-02-15T13:53:33.889Z","features":{"pfam":[{"id":"PF02661","name":"Fic/DOC family","start":40,"end":125}],"gene3D":[]},"length":191,"name":"Protein adenylyltransferase NmFic","ncbi_taxon_id":122586,"organism":"Neisseria meningitidis serogroup B (strain MC58)","regions":[{"start":59,"end":73,"reference_id":"26787847","reference_source":"pmid","reference_html":"Intrinsic regulation of FIC-domain AMP-transferases by oligomerization and automodification. <i> Stanger FV, Burmann BM, Harms A, Aragão H, Mazur A, Sharpe T, Dehio C, Hiller S, Schirmer T. </i> Proc Natl Acad Sci U S A, 2016","date":"2022-02-15T14:05:16.714Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu156Arg","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"5CGL"}],"region_id":"DP03614r001","statement":[{"text":"The region is missing in the crystal structure.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-12T22:46:39.357Z"}},{"start":178,"end":191,"reference_id":"26787847","reference_source":"pmid","reference_html":"Intrinsic regulation of FIC-domain AMP-transferases by oligomerization and automodification. <i> Stanger FV, Burmann BM, Harms A, Aragão H, Mazur A, Sharpe T, Dehio C, Hiller S, Schirmer T. </i> Proc Natl Acad Sci U S A, 2016","date":"2022-02-15T14:06:49.912Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu156Arg","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu102Arg","start":null,"end":null,"position":null}],"region_id":"DP03614r002","statement":[{"text":"Autoadenylylation of NmFic was monitored in real-time by circular dichroism (CD) spectroscopy. Because NmFicwt shows little autoadenylylation (Fig. 3B), we used NmFicmono (NmFicE102R,E156R) for this and the following analyses. Upon addition of ATP/MgCl2, the CD spectrum of NmFicmono showed a gradual, time-dependent decrease in amplitude of the negative peaks at 208 and 222 nm (Fig. S5A), corresponding to a reduction of α-helical content. This decrease is entirely consistent with (partial) unfolding of the αinh upon autoadenylylation.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-12T22:46:39.241Z"}},{"start":178,"end":191,"reference_id":"26787847","reference_source":"pmid","reference_html":"Intrinsic regulation of FIC-domain AMP-transferases by oligomerization and automodification. <i> Stanger FV, Burmann BM, Harms A, Aragão H, Mazur A, Sharpe T, Dehio C, Hiller S, Schirmer T. </i> Proc Natl Acad Sci U S A, 2016","date":"2022-02-15T14:08:33.594Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu102Arg","start":null,"end":null,"position":null}],"cross_refs":[{"db":"BMRB","id":"26607"}],"region_id":"DP03614r003","statement":[{"text":"αinh of Autoadenylylated NmFic Is Partly Unfolded.","type":"Results"},{"text":"We obtained well-dispersed NMR spectra for an unmodified protein (catalytically inactive NmFicmono,H107A), as well as for autoadenylylated (NmFicmono-AMP) protein.","type":"Results"},{"text":"Furthermore, the amide chemical shifts of residues 178–191 populate the random coil region (7.5–8.5 ppm), indicating an unfolded conformation.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-12T22:46:43.335Z"}},{"start":178,"end":191,"reference_id":"26787847","reference_source":"pmid","reference_html":"Intrinsic regulation of FIC-domain AMP-transferases by oligomerization and automodification. <i> Stanger FV, Burmann BM, Harms A, Aragão H, Mazur A, Sharpe T, Dehio C, Hiller S, Schirmer T. </i> Proc Natl Acad Sci U S A, 2016","date":"2022-02-15T14:19:20.307Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000057","term_name":"self-regulatory activity","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0007159","ec_ontology":"ECO","ec_name":"ATP bioluminescence assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu156Arg","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Tyr183Arg","start":null,"end":null,"position":null}],"region_id":"DP03614r004","statement":[{"text":"We have shown that cis-autoadenylylation of NmFic constitutes an in-built mechanism to covalently modify Y183, resulting in partial unfolding of the αinh.","type":"Results"},{"text":"Thus, to test for any functional role of Y183, we removed its hydroxyl group by introducing an additional Y183F mutation into the alleles of active (i.e., oligomerization-deficient), mutants. Strikingly, the mutation suppressed the growth defect phenotype as efficiently as mutation of the catalytic His (H107A) (Fig. 3A, Right), suggesting a crucial regulatory role for Y183.","type":"Results"},{"text":"Similarly, NmFicE156R,Y183F shows autoadenylylation, although with a considerably slower rate (Fig. 3 D and G). Such an effect of the Y183F mutation was also observed for NmFicmono,Y183F by MS (Fig. S6B). As mentioned above, the modification on residues Y184, Y185, and Y188 is probably not of functional relevance.","type":"Results"}],"ec_go":"IDA","disprot_namespace":"Disorder function","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-12T22:46:40.153Z"}}],"regions_counter":4,"released":"2023_12","sequence":"MPSENPIGKTMKSIDEQSLHNARRLFESGDIDRIEVGTTAGLQQIHRYLFGGLYDFAGQIREDNISKGGFRFANAMYLKEALVKIEQMPERTFEEIIAKYVEMNIAHPFLEGNGRSTRIWLDLVLKKNLKKVVNWQNVSKTLYLQAMERSPVNDLELRFLLKDNLTDDVDNREIIFKGIEQSYYYEGYEKG","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"genes":[{"olnNames":[{"value":"NMB0255"}]}],"alphafold_very_low_content":0.031413612565445025,"disorder_content":0.1518324607329843,"disprot_consensus":{"full":[{"start":59,"end":73,"type":"D"},{"start":178,"end":191,"type":"D"}],"Structural state":[{"start":59,"end":73,"type":"D"},{"start":178,"end":191,"type":"D"}],"Disorder function":[{"start":178,"end":191,"type":"F"}]}},{"disprot_id":"DP03615","acc":"A0A1Y0DDB3","creator":"fquaglia","date":"2022-02-16T10:05:57.505Z","features":{"pfam":[{"id":"PF00334","name":"Nucleoside diphosphate kinase","start":4,"end":137}],"gene3D":[]},"length":151,"name":"Nucleoside diphosphate kinase","ncbi_taxon_id":5659,"organism":"Leishmania amazonensis","regions":[{"start":43,"end":68,"reference_id":"28551817","reference_source":"pmid","reference_html":"Discovery of novel inhibitors for Leishmania nucleoside diphosphatase kinase (NDK) based on its structural and functional characterization. <i> Mishra AK, Singh N, Agnihotri P, Mishra S, Singh SP, Kolli BK, Chang KP, Sahasrabuddhe AA, Siddiqi MI, Pratap JV. </i> J Comput Aided Mol Des, 2017","date":"2022-02-16T10:06:51.723Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5GO1"}],"region_id":"DP03615r001","statement":[{"text":"Two N-terminal residues and 11 C-terminal residues (residues 141–151) and residues of the loop 43–68 could not be modelled due to missing/ambiguous electron density. Significantly, this missing loop region is a common and recurring scenario observed in other NDK crystal structures in the PDB that have been crystallized in the absence of ligand, or when the ligand density is not observed suggesting that in the absence of ligand, this loop is flexible.","type":"Results"},{"text":"In the structure, regions corresponding to residues 43–68 and 141–151 of other NDKs were missing, a fact observed in other non-liganded NDK structures.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-16T12:26:05.734Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":141,"end":151,"reference_id":"28551817","reference_source":"pmid","reference_html":"Discovery of novel inhibitors for Leishmania nucleoside diphosphatase kinase (NDK) based on its structural and functional characterization. <i> Mishra AK, Singh N, Agnihotri P, Mishra S, Singh SP, Kolli BK, Chang KP, Sahasrabuddhe AA, Siddiqi MI, Pratap JV. </i> J Comput Aided Mol Des, 2017","date":"2022-02-16T10:07:04.785Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5GO1"}],"region_id":"DP03615r002","statement":[{"text":"Two N-terminal residues and 11 C-terminal residues (residues 141–151) and residues of the loop 43–68 could not be modelled due to missing/ambiguous electron density. Significantly, this missing loop region is a common and recurring scenario observed in other NDK crystal structures in the PDB that have been crystallized in the absence of ligand, or when the ligand density is not observed suggesting that in the absence of ligand, this loop is flexible.","type":"Results"},{"text":"In the structure, regions corresponding to residues 43–68 and 141–151 of other NDKs were missing, a fact observed in other non-liganded NDK structures.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-02-16T12:26:03.860Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"regions_counter":2,"released":"2023_06","sequence":"MASERTFIAVKPDGVQRGLAGEIICRFERKGYKLVALKMLQPTTEQAEGHYKDLSSKPFFPALVKYFSSGPIVCMVWEGKNVVKGGRMLLGATNPADSHPGTIRGDFAVDVGRNVCHGSDSVESAEREIAFWFKADELACWTSHSVSQIYE","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[],"alphafold_very_low_content":0,"disorder_content":0.24503311258278146,"disprot_consensus":{"full":[{"start":43,"end":68,"type":"D"},{"start":141,"end":151,"type":"D"}],"Structural state":[{"start":43,"end":68,"type":"D"},{"start":141,"end":151,"type":"D"}]}},{"disprot_id":"DP03616","acc":"Q9JZ10","creator":"esalladini","date":"2022-02-16T10:54:14.066Z","features":{"pfam":[{"id":"PF21641","name":"NarE","start":4,"end":123}],"gene3D":[]},"length":145,"name":"Uncharacterized protein","ncbi_taxon_id":122586,"organism":"Neisseria meningitidis serogroup B (strain MC58)","regions":[{"start":20,"end":66,"reference_id":"21367854","reference_source":"pmid","reference_html":"Structural and biochemical characterization of NarE, an iron-containing ADP-ribosyltransferase from Neisseria meningitidis. <i> Koehler C, Carlier L, Veggi D, Balducci E, Di Marcello F, Ferrer-Navarro M, Pizza M, Daura X, Soriani M, Boelens R, Bonvin AM. </i> J Biol Chem, 2011","date":"2022-02-16T11:01:10.282Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2KXI"},{"db":"BMRB","id":"16737"}],"region_id":"DP03616r001","statement":[{"text":"From R1 and R2 relaxation rates as well as heteronuclear Nuclear Overhauser Effects (NOE) we identified a loop region corresponding to residues 20–60, which is characterized by fast motions in the range of μs-ms within the otherwise rigid protein (Fig. 1, A and B).","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-11T20:39:46.198Z"}},{"start":55,"end":59,"reference_id":"21367854","reference_source":"pmid","reference_html":"Structural and biochemical characterization of NarE, an iron-containing ADP-ribosyltransferase from Neisseria meningitidis. <i> Koehler C, Carlier L, Veggi D, Balducci E, Di Marcello F, Ferrer-Navarro M, Pizza M, Daura X, Soriani M, Boelens R, Bonvin AM. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"interaction_partner":[{"db":"ChEBI","id":"29034","partner_start":null,"partner_end":null}],"region_id":"DP03616r002","statement":[{"text":"Another residue affected by iron binding is His-57.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-11T20:39:44.204Z"}},{"start":44,"end":48,"reference_id":"21367854","reference_source":"pmid","reference_html":"Structural and biochemical characterization of NarE, an iron-containing ADP-ribosyltransferase from Neisseria meningitidis. <i> Koehler C, Carlier L, Veggi D, Balducci E, Di Marcello F, Ferrer-Navarro M, Pizza M, Daura X, Soriani M, Boelens R, Bonvin AM. </i> J Biol Chem, 2011","date":"2022-02-14T09:00:00.000Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","term_ontology":"GO","term_go_domain":"F","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"interaction_partner":[{"db":"ChEBI","id":"29105","partner_start":null,"partner_end":null}],"region_id":"DP03616r003","statement":[{"text":"Because of the diamagnetic nature of zinc-II, in contrast to paramagnetic iron-III, the spectra still show a good resolution, which allows the identification of the fourth metal-coordinating residue within NarE namely His-46.","type":"Results"}],"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-11T20:39:44.732Z"}}],"regions_counter":3,"released":"2023_12","sequence":"MGNFLYRGISCQQDEQNNGQLKPKGNKAEVAIRYDGKFKYDGKATHGPSVKNAVYAHQIETGLYDGCYISTTTDKEIAKKFATSSGIENGYIYVLNRDLFGQYSIFEYEVEHPENPNEKEVTIRAEDCGCIPEEVIIAKELIEIN","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"genes":[{"olnNames":[{"value":"NMB1343","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF41718.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF41718.1"}}]}]}],"alphafold_very_low_content":0.22758620689655173,"disorder_content":0.32413793103448274,"disprot_consensus":{"full":[{"start":20,"end":66,"type":"D"}],"Structural state":[{"start":20,"end":66,"type":"D"}],"Molecular function":[{"start":44,"end":48,"type":"F"},{"start":55,"end":59,"type":"F"}]}},{"disprot_id":"DP03617","acc":"Q7BMQ8","creator":"esalladini","date":"2022-02-16T11:12:53.118Z","features":{"pfam":[{"id":"PF03180","name":"NlpA lipoprotein","start":45,"end":279}],"gene3D":[]},"length":287,"name":"Lipoprotein","ncbi_taxon_id":487,"organism":"Neisseria meningitidis","regions":[{"start":1,"end":42,"reference_id":"21188561","reference_source":"pmid","reference_html":"1H, 13C and 15N assignment of the GNA1946 outer membrane lipoprotein from Neisseria meningitidis. <i> Neumoin A, Leonchiks A, Petit P, Vuillard L, Pizza M, Soriani M, Boelens R, Bonvin AM. </i> Biomol NMR Assign, 2011","date":"2022-02-16T11:15:26.976Z","curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"BMRB","id":"17250"}],"region_id":"DP03617r001","statement":[{"text":"The N-termini residues M1 to S9 have not been assigned because of line broadening most likely due to solvent exchange and/or conformational exchange.","type":"Results"},{"text":"The remaining residues from 9 to 42 are described as disordered in Figure 2.","type":"Curator statement"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-12T18:19:42.625Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MKTFFKTLSAAALALILAACGGQKDSAPAASASAAADNGAAKKEIVFGTTVGDFGDMVKEQIQPELEKKGYTVKLVEFTDYVRPNLALAEGELDINVFQHKPYLDDFKKEHNLDITEVFQVPTAPLGLYPGKLKSLEEVKDGSTVSAPNDPSNFARVLVMLDELGWIKLKDGINPLTASKADIAENLKNIKIVELEAAQLPRSRADVDFAVVNGNYAISSGMKLTEALFQEPSFAYVNWSAVKTADKDSQWLKDVTEAYNSDAFKAYAHKRFEGYKSPAAWNEGAAK","taxonomy":["Bacteria","Proteobacteria","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"genes":[{"name":{"value":"gna1946","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF42644.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF42644.1"}}]},"orfNames":[{"value":"B1A92_06690","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"OOG97217.1","url":"https://www.ebi.ac.uk/ena/browser/view/OOG97217.1"}}]}]}],"alphafold_very_low_content":0.10452961672473868,"disorder_content":0.14634146341463414,"disprot_consensus":{"full":[{"start":1,"end":42,"type":"D"}],"Structural state":[{"start":1,"end":42,"type":"D"}]}},{"disprot_id":"DP03619","acc":"Q9NZD4","creator":"vacs","date":"2022-02-18T10:47:04.906Z","features":{"pfam":[{"id":"PF09236","name":"Alpha-haemoglobin stabilising protein","start":5,"end":91}],"gene3D":[]},"length":102,"name":"Alpha-hemoglobin-stabilizing protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":92,"end":102,"reference_id":"15178680","reference_source":"pmid","reference_html":"NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding. <i> Santiveri CM, Pérez-Cañadillas JM, Vadivelu MK, Allen MD, Rutherford TJ, Watkins NA, Bycroft M. </i> J Biol Chem, 2004","date":"2022-02-18T10:52:41.583Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"term_go_domain":null,"ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1W0B"}],"region_id":"DP03619r001","statement":[{"text":"The N-terminal 4 residues and the C-terminal 11 are unstructured in both conformations.","type":"Results"}],"ec_go":"EXP","disprot_namespace":"Structural state","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-05T09:43:11.305Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MALLKANKDLISAGLKEFSVLLNQQVFNDPLVSEEDMVTVVEDWMNFYINYYRQQVTGEPQERDKALQELRQELNTLANPFLAKYRDFLKSHELPSHPPPSS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"AHSP"},"synonyms":[{"value":"EDRF"},{"value":"ERAF"}]}],"alphafold_very_low_content":0,"disorder_content":0.10784313725490197,"disprot_consensus":{"full":[{"start":92,"end":102,"type":"D"}],"Structural state":[{"start":92,"end":102,"type":"D"}]}},{"disprot_id":"DP03620","acc":"Q12051","creator":"vacs","date":"2022-03-18T09:09:13.201Z","features":{"pfam":[{"id":"PF00348","name":"Polyprenyl synthetase","start":21,"end":269}],"gene3D":[]},"length":335,"name":"Geranylgeranyl pyrophosphate synthase BTS1","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":310,"end":322,"reference_id":"16554305","reference_source":"pmid","reference_html":"Crystal structure of type-III geranylgeranyl pyrophosphate synthase from Saccharomyces cerevisiae and the mechanism of product chain length determination. <i> Chang TH, Guo RT, Ko TP, Wang AH, Liang PH. </i> J Biol Chem, 2006","date":"2022-03-18T09:12:33.526Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2DH4"}],"region_id":"DP03620r001","statement":[{"text":"Each monomer of the refined structure encompassed 322 of the 335 total residues of the GGPPs sequence, with a small disordered region of residues 315–327.","type":"Methods"},{"text":"The refined structure of type-III GGPPs in complex with one magnesium ion in each subunit contains amino acid residues 2-314 and 328–340. The electron density map between residues 315 and 327 at the C terminus is not clearly visible.","type":"Results"},{"text":"The IDR characterized in the publication and spanning residues 315-327 corresponds to region 310-322 of the amino acid sequence, since the authors included a five-residue sequence (MTKNK) between the N terminus of GGPPs and the Factor Xa cleavage sequence to expose the protease site for tag removal.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-05T09:45:35.933Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MEAKIDELINNDPVWSSQNESLISKPYNHILLKPGKNFRLNLIVQINRVMNLPKDQLAIVSQIVELLHNSSLLIDDIEDNAPLRRGQTTSHLIFGVPSTINTANYMYFRAMQLVSQLTTKEPLYHNLITIFNEELINLHRGQGLDIYWRDFLPEIIPTQEMYLNMVMNKTGGLFRLTLRLMEALSPSSHHGHSLVPFINLLGIIYQIRDDYLNLKDFQMSSEKGFAEDITEGKLSFPIVHALNFTKTKGQTEQHNEILRILLLRTSDKDIKLKLIQILEFDTNSLAYTKNFINQLVNMIKNDNENKYLPDLASHSDTATNLHDELLYIIDHLSEL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"genes":[{"name":{"value":"BTS1"},"olnNames":[{"value":"YPL069C"}]}],"alphafold_very_low_content":0.005970149253731343,"disorder_content":0.03880597014925373,"disprot_consensus":{"full":[{"start":310,"end":322,"type":"D"}],"Structural state":[{"start":310,"end":322,"type":"D"}]}},{"disprot_id":"DP03621","acc":"P04807","creator":"vacs","date":"2022-03-21T10:13:59.427Z","features":{"pfam":[{"id":"PF00349","name":"Hexokinase","start":27,"end":221},{"id":"PF03727","name":"Hexokinase","start":227,"end":470}],"gene3D":[]},"length":486,"name":"Hexokinase-2","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":17,"reference_id":"10749890","reference_source":"pmid","reference_html":"The high resolution crystal structure of yeast hexokinase PII with the correct primary sequence provides new insights into its mechanism of action. <i> Kuser PR, Krauchenco S, Antunes OA, Polikarpov I. </i> J Biol Chem, 2000","date":"2022-03-21T10:16:23.390Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1IG8"}],"region_id":"DP03621r001","statement":[{"text":"The final model contains residues 18–486 and 442 water molecules. No continuous density can be observed for the first 17 residues of the N terminus. Yeast HK is susceptible to limited proteolysis by endogenous proteases, resulting in loss of the first 11 N-terminal amino acid residues (36, 37), which, together with the thermal disorder, is probably the reason for the lack of electron density at the N terminus.","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-05T09:47:21.024Z"}},{"start":13,"end":17,"reference_id":"8286332","reference_source":"pmid","reference_html":"In vivo phosphorylation site of hexokinase 2 in Saccharomyces cerevisiae. <i> Kriegel TM, Rush J, Vojtek AB, Clifton D, Fraenkel DG. </i> Biochemistry, 1994","date":"2022-03-21T10:28:32.057Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005527","ec_ontology":"ECO","ec_name":"matrix-assisted laser desorption/ionization time-of-flight mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03621r002","statement":[{"text":"The principal and perhaps sole site of phosphorylation is now identified as residue serine-15, by observation of a single tryptic peptide difference, its sequencing and size determination by mass spectrometry, and by mutation to alanine, which prevents phosphorylation in vivo. Although protein kinase A was unlikely to accomplish the phosphorylation in vivo, serine-15 does belong to a protein kinase A consensus phosphorylation sequence, and in vitro phosphorylation by protein kinase A at serine-15 could be shown by labeling and by peptide determination. The alanine-15 mutant enzyme was not phosphorylated in vitro.","type":"Abstract"},{"text":"The present work shows by chemical identification and mutagenesis that for hexokinase 2 it is residue serine-15 which is phosphorylated in vivo in the regime employed. This residue, which is in a protein kinase A consensus sequence, Arg-Lys-Gly-Ser (Kennelly & Krebs, 1991; Denis et al., 1991; Gibbs et al., 1992), is also phosphorylated, albeit slowly, by protein kinase A in vitro, and the alanine-15 mutant protein (S15A) is not.","type":"Article"},{"text":"This is the expected result of the conversion of serine to serine phosphate, producing a derivative that cannot be efficiently extracted from the sequencing support by the apolar organic solvents employed (Meyer et al., 1991). Mass spectrometry of the two peptides, 1 and 2, respectively, showed the nonapeptide masses expected, 936.6 Da with serine unsubstituted and 1015.3 Da with phosphoserine (Figure 5).","type":"Results"},{"text":"This paper identifies serine-15 as a primary residue phosphorylated in vivo in yeast hexokinase 2. The loss of labeling in vivo in the alanine-15 mutant suggests it may even be the only site or be required for phosphorylation of other sites.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-05T09:50:44.470Z"}},{"start":13,"end":17,"reference_id":"8286332","reference_source":"pmid","reference_html":"In vivo phosphorylation site of hexokinase 2 in Saccharomyces cerevisiae. <i> Kriegel TM, Rush J, Vojtek AB, Clifton D, Fraenkel DG. </i> Biochemistry, 1994","date":"2022-03-21T10:44:23.636Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005667","ec_ontology":"ECO","ec_name":"site-directed mutagenesis phenotypic evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03621r003","statement":[{"text":"The principal and perhaps sole site of phosphorylation is now identified as residue serine-15, by observation of a single tryptic peptide difference, its sequencing and size determination by mass spectrometry, and by mutation to alanine, which prevents phosphorylation in vivo. Although protein kinase A was unlikely to accomplish the phosphorylation in vivo, serine-15 does belong to a protein kinase A consensus phosphorylation sequence, and in vitro phosphorylation by protein kinase A at serine-15 could be shown by labeling and by peptide determination. The alanine-15 mutant enzyme was not phosphorylated in vitro.","type":"Abstract"},{"text":"The present work shows by chemical identification and mutagenesis that for hexokinase 2 it is residue serine-15 which is phosphorylated in vivo in the regime employed. This residue, which is in a protein kinase A consensus sequence, Arg-Lys-Gly-Ser (Kennelly & Krebs, 1991; Denis et al., 1991; Gibbs et al., 1992), is also phosphorylated, albeit slowly, by protein kinase A in vitro, and the alanine-15 mutant protein (S15A) is not.","type":"Article"},{"text":"In vivo labeling (Figure 6), i.e., the same regime but including 32P-inorganic phosphate, showed essentially no labeling of hexokinase 2(S15A) (size ~50 kDa) from either 2% or 0.1% glucose (lanes 3 and 4, respectively) as compared with the prominent labeling of the wild-type enzyme (lanes 1 and 2) in the same regime from 0.1% glucose.","type":"Results"},{"text":"Since the present results showed that the residue of hexokinase 2 phosphorylated in vivo was in fact serine-15, in vitro phosphorylation of the S15 A mutant enzyme was tested. Figure 7 (lower panel) shows phosphorylation of wild-type hexokinase 2 fraction HA-I (lanes 1 and 3), but not of fraction HA-II (lane 5), and no phosphorylation of hexokinase 2 mutant S15A (lanes 7 and 9).","type":"Results"},{"text":"This paper identifies serine-15 as a primary residue phosphorylated in vivo in yeast hexokinase 2. The loss of labeling in vivo in the alanine-15 mutant suggests it may even be the only site or be required for phosphorylation of other sites.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-05T09:50:47.218Z"}}],"regions_counter":3,"released":"2023_12","sequence":"MVHLGPKKPQARKGSMADVPKELMQQIENFEKIFTVPTETLQAVTKHFISELEKGLSKKGGNIPMIPGWVMDFPTGKESGDFLAIDLGGTNLRVVLVKLGGDRTFDTTQSKYRLPDAMRTTQNPDELWEFIADSLKAFIDEQFPQGISEPIPLGFTFSFPASQNKINEGILQRWTKGFDIPNIENHDVVPMLQKQITKRNIPIEVVALINDTTGTLVASYYTDPETKMGVIFGTGVNGAYYDVCSDIEKLQGKLSDDIPPSAPMAINCEYGSFDNEHVVLPRTKYDITIDEESPRPGQQTFEKMSSGYYLGEILRLALMDMYKQGFIFKNQDLSKFDKPFVMDTSYPARIEEDPFENLEDTDDLFQNEFGINTTVQERKLIRRLSELIGARAARLSVCGIAAICQKRGYKTGHIAADGSVYNRYPGFKEKAANALKDIYGWTQTSLDDYPIKIVPAEDGSGAGAAVIAALAQKRIAEGKSVGIIGA","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"genes":[{"name":{"value":"HXK2"},"synonyms":[{"value":"HEX1"},{"value":"HKB"}],"orfNames":[{"value":"NRB486"}],"olnNames":[{"value":"YGL253W"}]}],"alphafold_very_low_content":0.00205761316872428,"disorder_content":0.03497942386831276,"disprot_consensus":{"full":[{"start":1,"end":17,"type":"D"}],"Structural state":[{"start":1,"end":17,"type":"D"}],"Disorder function":[{"start":13,"end":17,"type":"F"}]}},{"disprot_id":"DP03622","acc":"Q12962","creator":"maspromonte","date":"2022-04-05T14:51:20.032Z","features":{"pfam":[{"id":"PF03540","name":"Transcription initiation factor TFIID 23-30kDa subunit","start":116,"end":217}],"gene3D":[]},"length":218,"name":"Transcription initiation factor TFIID subunit 10","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":178,"end":191,"reference_id":"25586196","reference_source":"pmid","reference_html":"Cytoplasmic TAF2-TAF8-TAF10 complex provides evidence for nuclear holo-TFIID assembly from preformed submodules. <i> Trowitzsch S, Viola C, Scheer E, Conic S, Chavant V, Fournier M, Papai G, Ebong IO, Schaffitzel C, Zou J, Haffke M, Rappsilber J, Robinson CV, Schultz P, Tora L, Berger I. </i> Nat Commun, 2015","date":"2022-04-06T07:39:34.489Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4WV4"}],"region_id":"DP03622r001","statement":[{"text":"The disordered L2 loop of TAF10 is represented by a dotted line","type":"Figure"},{"text":"The final model includes TAF8 residues 28–120 and TAF10 residues 113–212 with the exception of a flexible loop in TAF10 comprising residues 178–191","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-06T07:48:39.404Z"}},{"start":178,"end":191,"reference_id":"25586196","reference_source":"pmid","reference_html":"Cytoplasmic TAF2-TAF8-TAF10 complex provides evidence for nuclear holo-TFIID assembly from preformed submodules. <i> Trowitzsch S, Viola C, Scheer E, Conic S, Chavant V, Fournier M, Papai G, Ebong IO, Schaffitzel C, Zou J, Haffke M, Rappsilber J, Robinson CV, Schultz P, Tora L, Berger I. </i> Nat Commun, 2015","date":"2022-04-06T07:40:01.285Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4WV4"}],"region_id":"DP03622r002","statement":[{"text":"The disordered L2 loop of TAF10 is represented by a dotted line","type":"Figure"},{"text":"The final model includes TAF8 residues 28–120 and TAF10 residues 113–212 with the exception of a flexible loop in TAF10 comprising residues 178–191","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-06T07:48:40.484Z"}},{"start":1,"end":112,"reference_id":"30442764","reference_source":"pmid","reference_html":"Structure of human TFIID and mechanism of TBP loading onto promoter DNA.  <i> Patel AB, Louder RK, Greber BJ, Grünberg S, Luo J, Fang J, Liu Y, Ranish J, Hahn S, Nogales E. </i> Science, 2018","date":"2022-11-10T14:58:15.672Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6MZD"},{"db":"PDB","id":"6MZC"},{"db":"PDB","id":"6MZM"},{"db":"PDB","id":"6MZL"}],"region_id":"DP03622r003","statement":[{"text":"The electron microscopy structure of the Human transcription factor IID (TFIID) complex shows this region of the subunit 10 lacks electron density, indicating it is disordered. ","type":"Curator statement"}]},{"start":178,"end":191,"reference_id":"30442764","reference_source":"pmid","reference_html":"Structure of human TFIID and mechanism of TBP loading onto promoter DNA.  <i> Patel AB, Louder RK, Greber BJ, Grünberg S, Luo J, Fang J, Liu Y, Ranish J, Hahn S, Nogales E. </i> Science, 2018","date":"2022-11-10T14:59:33.944Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6MZD"},{"db":"PDB","id":"6MZC"},{"db":"PDB","id":"6MZM"},{"db":"PDB","id":"6MZL"}],"region_id":"DP03622r004","statement":[{"text":"The electron microscopy structure of the Human transcription factor IID (TFIID) complex shows this region of the subunit 10 lacks electron density, indicating it is disordered. ","type":"Curator statement"}]},{"start":209,"end":218,"reference_id":"30442764","reference_source":"pmid","reference_html":"Structure of human TFIID and mechanism of TBP loading onto promoter DNA.  <i> Patel AB, Louder RK, Greber BJ, Grünberg S, Luo J, Fang J, Liu Y, Ranish J, Hahn S, Nogales E. </i> Science, 2018","date":"2022-11-10T14:59:09.125Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6MZD"},{"db":"PDB","id":"6MZC"},{"db":"PDB","id":"6MZM"},{"db":"PDB","id":"6MZL"}],"region_id":"DP03622r005","statement":[{"text":"The electron microscopy structure of the Human transcription factor IID (TFIID) complex shows this region of the subunit 10 lacks electron density, indicating it is disordered. ","type":"Curator statement"}]}],"regions_counter":5,"released":"2023_12","sequence":"MSCSGSGADPEAAPASAASAPGPAPPVSAPAALPSSTAAENKASPAGTAGGPGAGAAAGGTGPLAARAGEPAERRGAAPVSAGGAAPPEGAISNGVYVLPSAANGDVKPVVSSTPLVDFLMQLEDYTPTIPDAVTGYYLNRAGFEASDPRIIRLISLAAQKFISDIANDALQHCKMKGTASGSSRSKSKDRKYTLTMEDLTPALSEYGINVKKPHYFT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":[],"genes":[{"name":{"value":"TAF10"},"synonyms":[{"value":"TAF2A"},{"value":"TAF2H"},{"value":"TAFII30"}]}],"alphafold_very_low_content":0.3623853211009174,"disorder_content":0.6238532110091743,"disprot_consensus":{"full":[{"start":1,"end":112,"type":"D"},{"start":178,"end":191,"type":"D"},{"start":209,"end":218,"type":"D"}],"Structural state":[{"start":1,"end":112,"type":"D"},{"start":178,"end":191,"type":"D"},{"start":209,"end":218,"type":"D"}],"Disorder function":[{"start":178,"end":191,"type":"F"}]}},{"disprot_id":"DP03623","acc":"P0DTC1","creator":"tlazar","date":"2022-04-05T20:14:26.531Z","features":{"pfam":[{"id":"PF01661","name":"Macro domain","start":1058,"end":1164},{"id":"PF05409","name":"Coronavirus endopeptidase C30","start":3292,"end":3575},{"id":"PF08710","name":"Coronavirus replicase NSP9","start":4141,"end":4253},{"id":"PF08715","name":"Coronavirus papain-like peptidase","start":1564,"end":1882},{"id":"PF08716","name":"Coronavirus replicase NSP7","start":3860,"end":3942},{"id":"PF08717","name":"Coronavirus replicase NSP8","start":3943,"end":4140},{"id":"PF09401","name":"Coronavirus RNA synthesis protein NSP10","start":4263,"end":4384},{"id":"PF11501","name":"Betacoronavirus replicase NSP1","start":9,"end":131},{"id":"PF11633","name":"Betacoronavirus single-stranded poly(A) binding domain","start":1351,"end":1493},{"id":"PF12124","name":"Betacoronavirus SUD-C domain","start":1498,"end":1561},{"id":"PF12379","name":"Betacoronavirus replicase NSP3, N-terminal","start":880,"end":1050},{"id":"PF16251","name":"Betacoronavirus nucleic acid-binding (NAB)","start":1899,"end":2029},{"id":"PF16348","name":"Coronavirus replicase NSP4, C-terminal","start":3166,"end":3263},{"id":"PF19211","name":"Coronavirus replicase NSP2, N-terminal","start":184,"end":423},{"id":"PF19213","name":"Coronavirus replicase NSP6","start":3599,"end":3859},{"id":"PF19217","name":"Coronavirus replicase NSP4, N-terminal","start":2792,"end":3141},{"id":"PF19218","name":"Coronavirus replicase NSP3, C-terminal","start":2262,"end":2748}],"gene3D":[]},"length":4405,"name":"Replicase polyprotein 1a","ncbi_taxon_id":2697049,"organism":"Severe acute respiratory syndrome coronavirus 2","regions":[{"start":4393,"end":4405,"reference_id":"34119626","reference_source":"pmid","reference_html":"Conformational dynamics of 13 amino acids long NSP11 of SARS-CoV-2 under membrane mimetics and different solvent conditions. <i> Gadhave K, Kumar P, Kumar A, Bhardwaj T, Garg N, Giri R. </i> Microb Pathog, 2021","date":"2022-04-06T13:48:29.805Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP03623r001","statement":[{"text":"The Far-UV CD spectrum of nsp11 protein (theoretical molecular weight is 1.33 kDa) shows a signature minima at 200 nm (Fig. 1A), suggest the spectrum of typical disordered type protein.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-07T07:47:58.146Z"}},{"start":4393,"end":4405,"reference_id":"34119626","reference_source":"pmid","reference_html":"Conformational dynamics of 13 amino acids long NSP11 of SARS-CoV-2 under membrane mimetics and different solvent conditions. <i> Gadhave K, Kumar P, Kumar A, Bhardwaj T, Garg N, Giri R. </i> Microb Pathog, 2021","date":"2022-04-07T16:12:42.714Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP03623r002","statement":[{"text":"Analogous to lipid membranes, the SDS micelles used to mimic the interface between hydrophobic and hydrophilic environments such as the plasma membrane and the cytosol [34]. SDS is a denaturing detergent with folding inducing properties that form micelles (CMC is 1.99 mM in 50 mM phosphate buffer [35])","type":"Results"},{"text":"At higher concentrations (25, 50, and 100 mM) the CD spectra of nsp11 exhibited two minima at 206 and 222 nm suggesting the structural transition from the disordered to ordered conformation (Fig. 3A and B).","type":"Results"},{"text":"With increasing TFE concentration it is evident that the negative ellipticity at 200 nm becomes lesser and negative ellipticities at 208 nm and 222 nm become towards higher value (Fig. 2A and B). The change in the ellipticity at the corresponding wavelength indicates that nsp11 acquires an α-helical structure in presence of TFE.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":"not relevant","value":null,"db":"ChEBI","id":"42330","statements":[{"type":"Results","text":"With increasing TFE concentration it is evident that the negative ellipticity at 200 nm becomes lesser and negative ellipticities at 208 nm and 222 nm become towards higher value (Fig. 2A and B). The change in the ellipticity at the corresponding wavelength indicates that nsp11 acquires an α-helical structure in presence of TFE."},{"type":"Table","text":"TFE 50%: 87.4% [alpha-helix], 12.55% [beta-sheet], 0% [Turn], 0% [Disordered]"}],"entry_name":"2,2,2-trifluoroethanol"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":"not relevant","value":25,"db":"ChEBI","id":"8984","statements":[{"type":"Results","text":"At higher concentrations (25, 50, and 100 mM) the CD spectra of nsp11 exhibited two minima at 206 and 222 nm suggesting the structural transition from the disordered to ordered conformation (Fig. 3A and B)."}],"entry_name":"sodium dodecyl sulfate"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-08T07:18:22.444Z"}},{"start":4393,"end":4405,"reference_id":"34119626","reference_source":"pmid","reference_html":"Conformational dynamics of 13 amino acids long NSP11 of SARS-CoV-2 under membrane mimetics and different solvent conditions. <i> Gadhave K, Kumar P, Kumar A, Bhardwaj T, Garg N, Giri R. </i> Microb Pathog, 2021","date":"2022-04-06T14:17:43.830Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"8984","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03623r003","statement":[{"text":"Analogous to lipid membranes, the SDS micelles used to mimic the interface between hydrophobic and hydrophilic environments such as the plasma membrane and the cytosol [34]. SDS is a denaturing detergent with folding inducing properties that form micelles (CMC is 1.99 mM in 50 mM phosphate buffer [35])","type":"Results"},{"text":"At higher concentrations (25, 50, and 100 mM) the CD spectra of nsp11 exhibited two minima at 206 and 222 nm suggesting the structural transition from the disordered to ordered conformation (Fig. 3A and B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-07T07:48:00.623Z"}}],"regions_counter":3,"released":"2023_06","sequence":"MESLVPGFNEKTHVQLSLPVLQVRDVLVRGFGDSVEEVLSEARQHLKDGTCGLVEVEKGVLPQLEQPYVFIKRSDARTAPHGHVMVELVAELEGIQYGRSGETLGVLVPHVGEIPVAYRKVLLRKNGNKGAGGHSYGADLKSFDLGDELGTDPYEDFQENWNTKHSSGVTRELMRELNGGAYTRYVDNNFCGPDGYPLECIKDLLARAGKASCTLSEQLDFIDTKRGVYCCREHEHEIAWYTERSEKSYELQTPFEIKLAKKFDTFNGECPNFVFPLNSIIKTIQPRVEKKKLDGFMGRIRSVYPVASPNECNQMCLSTLMKCDHCGETSWQTGDFVKATCEFCGTENLTKEGATTCGYLPQNAVVKIYCPACHNSEVGPEHSLAEYHNESGLKTILRKGGRTIAFGGCVFSYVGCHNKCAYWVPRASANIGCNHTGVVGEGSEGLNDNLLEILQKEKVNINIVGDFKLNEEIAIILASFSASTSAFVETVKGLDYKAFKQIVESCGNFKVTKGKAKKGAWNIGEQKSILSPLYAFASEAARVVRSIFSRTLETAQNSVRVLQKAAITILDGISQYSLRLIDAMMFTSDLATNNLVVMAYITGGVVQLTSQWLTNIFGTVYEKLKPVLDWLEEKFKEGVEFLRDGWEIVKFISTCACEIVGGQIVTCAKEIKESVQTFFKLVNKFLALCADSIIIGGAKLKALNLGETFVTHSKGLYRKCVKSREETGLLMPLKAPKEIIFLEGETLPTEVLTEEVVLKTGDLQPLEQPTSEAVEAPLVGTPVCINGLMLLEIKDTEKYCALAPNMMVTNNTFTLKGGAPTKVTFGDDTVIEVQGYKSVNITFELDERIDKVLNEKCSAYTVELGTEVNEFACVVADAVIKTLQPVSELLTPLGIDLDEWSMATYYLFDESGEFKLASHMYCSFYPPDEDEEEGDCEEEEFEPSTQYEYGTEDDYQGKPLEFGATSAALQPEEEQEEDWLDDDSQQTVGQQDGSEDNQTTTIQTIVEVQPQLEMELTPVVQTIEVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYDKLVSSFLEMKSEKQVEQKIAEIPKEEVKPFITESKPSVEQRKQDDKKIKACVEEVTTTLEETKFLTENLLLYIDINGNLHPDSATLVSDIDITFLKKDAPYIVGDVVQEGVLTAVVIPTKKAGGTTEMLAKALRKVPTDNYITTYPGQGLNGYTVEEAKTVLKKCKSAFYILPSIISNEKQEILGTVSWNLREMLAHAEETRKLMPVCVETKAIVSTIQRKYKGIKIQEGVVDYGARFYFYTSKTTVASLINTLNDLNETLVTMPLGYVTHGLNLEEAARYMRSLKVPATVSVSSPDAVTAYNGYLTSSSKTPEEHFIETISLAGSYKDWSYSGQSTQLGIEFLKRGDKSVYYTSNPTTFHLDGEVITFDNLKTLLSLREVRTIKVFTTVDNINLHTQVVDMSMTYGQQFGPTYLDGADVTKIKPHNSHEGKTFYVLPNDDTLRVEAFEYYHTTDPSFLGRYMSALNHTKKWKYPQVNGLTSIKWADNNCYLATALLTLQQIELKFNPPALQDAYYRARAGEAANFCALILAYCNKTVGELGDVRETMSYLFQHANLDSCKRVLNVVCKTCGQQQTTLKGVEAVMYMGTLSYEQFKKGVQIPCTCGKQATKYLVQQESPFVMMSAPPAQYELKHGTFTCASEYTGNYQCGHYKHITSKETLYCIDGALLTKSSEYKGPITDVFYKENSYTTTIKPVTYKLDGVVCTEIDPKLDNYYKKDNSYFTEQPIDLVPNQPYPNASFDNFKFVCDNIKFADDLNQLTGYKKPASRELKVTFFPDLNGDVVAIDYKHYTPSFKKGAKLLHKPIVWHVNNATNKATYKPNTWCIRCLWSTKPVETSNSFDVLKSEDAQGMDNLACEDLKPVSEEVVENPTIQKDVLECNVKTTEVVGDIILKPANNSLKITEEVGHTDLMAAYVDNSSLTIKKPNELSRVLGLKTLATHGLAAVNSVPWDTIANYAKPFLNKVVSTTTNIVTRCLNRVCTNYMPYFFTLLLQLCTFTRSTNSRIKASMPTTIAKNTVKSVGKFCLEASFNYLKSPNFSKLINIIIWFLLLSVCLGSLIYSTAALGVLMSNLGMPSYCTGYREGYLNSTNVTIATYCTGSIPCSVCLSGLDSLDTYPSLETIQITISSFKWDLTAFGLVAEWFLAYILFTRFFYVLGLAAIMQLFFSYFAVHFISNSWLMWLIINLVQMAPISAMVRMYIFFASFYYVWKSYVHVVDGCNSSTCMMCYKRNRATRVECTTIVNGVRRSFYVYANGGKGFCKLHNWNCVNCDTFCAGSTFISDEVARDLSLQFKRPINPTDQSSYIVDSVTVKNGSIHLYFDKAGQKTYERHSLSHFVNLDNLRANNTKGSLPINVIVFDGKSKCEESSAKSASVYYSQLMCQPILLLDQALVSDVGDSAEVAVKMFDAYVNTFSSTFNVPMEKLKTLVATAEAELAKNVSLDNVLSTFISAARQGFVDSDVETKDVVECLKLSHQSDIEVTGDSCNNYMLTYNKVENMTPRDLGACIDCSARHINAQVAKSHNIALIWNVKDFMSLSEQLRKQIRSAAKKNNLPFKLTCATTRQVVNVVTTKIALKGGKIVNNWLKQLIKVTLVFLFVAAIFYLITPVHVMSKHTDFSSEIIGYKAIDGGVTRDIASTDTCFANKHADFDTWFSQRGGSYTNDKACPLIAAVITREVGFVVPGLPGTILRTTNGDFLHFLPRVFSAVGNICYTPSKLIEYTDFATSACVLAAECTIFKDASGKPVPYCYDTNVLEGSVAYESLRPDTRYVLMDGSIIQFPNTYLEGSVRVVTTFDSEYCRHGTCERSEAGVCVSTSGRWVLNNDYYRSLPGVFCGVDAVNLLTNMFTPLIQPIGALDISASIVAGGIVAIVVTCLAYYFMRFRRAFGEYSHVVAFNTLLFLMSFTVLCLTPVYSFLPGVYSVIYLYLTFYLTNDVSFLAHIQWMVMFTPLVPFWITIAYIICISTKHFYWFFSNYLKRRVVFNGVSFSTFEEAALCTFLLNKEMYLKLRSDVLLPLTQYNRYLALYNKYKYFSGAMDTTSYREAACCHLAKALNDFSNSGSDVLYQPPQTSITSAVLQSGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGHSMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFCYMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYEPLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQSAVKRTIKGTHHWLLLTILTSLLVLVQSTQWSLFFFLYENAFLPFAMGIIAMSAFAMMFVKHKHAFLCLFLLPSLATVAYFNMVYMPASWVMRIMTWLDMVDTSLSGFKLKDCVMYASAVVLLILMTARTVYDDGARRVWTLMNVLTLVYKVYYGNALDQAISMWALIISVTSNYSGVVTTVMFLARGIVFMCVEYCPIFFITGNTLQCIMLVYCFLGYFCTCYFGLFCLLNRYFRLTLGVYDYLVSTQEFRYMNSQGLLPPKNSIDAFKLNIKLLGVGGKPCIKVATVQSKMSDVKCTSVVLLSVLQQLRVESSSKLWAQCVQLHNDILLAKDTTEAFEKMVSLLSVLLSMQGAVDINKLCEEMLDNRATLQAIASEFSSLPSYAAFATAQEAYEQAVANGDSEVVLKKLKKSLNVAKSEFDRDAAMQRKLEKMADQAMTQMYKQARSEDKRAKVTSAMQTMLFTMLRKLDNDALNNIINNARDGCVPLNIIPLTTAAKLMVVIPDYNTYKNTCDGTTFTYASALWEIQQVVDADSKIVQLSEISMDNSPNLAWPLIVTALRANSAVKLQNNELSPVALRQMSCAAGTTQTACTDDNALAYYNTTKGGRFVLALLSDLQDLKWARFPKSDGTGTIYTELEPPCRFVTDTPKGPKVKYLYFIKGLNNLNRGMVLGSLAATVRLQAGNATEVPANSTVLSFCAFAVDAAKAYKDYLASGGQPITNCVKMLCTHTGTGQAITVTPEANMDQESFGGASCCLYCRCHIDHPNPKGFCDLKGKYVQIPTTCANDPVGFTLKNTVCTVCGMWKGYGCSCDQLREPMLQSADAQSFLNGFAV","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Nidovirales","Cornidovirineae","Coronaviridae","Orthocoronavirinae","Betacoronavirus","Sarbecovirus"],"dataset":["Viral proteins","RNA-binding proteins"],"genes":[],"disorder_content":0.0029511918274687855,"disprot_consensus":{"full":[{"start":4393,"end":4405,"type":"T"}],"Structural state":[{"start":4393,"end":4405,"type":"D"}],"Structural transition":[{"start":4393,"end":4405,"type":"T"}],"Molecular function":[{"start":4393,"end":4405,"type":"F"}]}},{"disprot_id":"DP03624","acc":"Q6ZMT4","creator":"maspromonte","date":"2022-04-06T14:17:35.701Z","features":{"pfam":[{"id":"PF02373","name":"JmjC domain, hydroxylase","start":269,"end":369},{"id":"PF17811","name":"Jumonji helical domain","start":373,"end":476},{"id":"PF30811","name":"UBR7-like PHD finger","start":38,"end":86}],"gene3D":[]},"length":941,"name":"Lysine-specific demethylase 7A","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":31,"reference_id":"20023638","reference_source":"pmid","reference_html":"Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases. <i> Horton JR, Upadhyay AK, Qi HH, Zhang X, Shi Y, Cheng X. </i> Nat Struct Mol Biol, 2010","date":"2022-04-06T14:34:47.162Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3KV6"},{"db":"PDB","id":"3KV5"}],"region_id":"DP03624r001","statement":[{"text":"The disordered residues include the C-terminal tail (residues 480–488) and the N-\nterminal tail (residues 1–31), the latter of which is absent in the KIAA1718 orthologs of zebrafish and Xenopus laevis (Supplementary Fig. 2) and whose deletion has no impact on activity (Supplementary Fig. 6).","type":"Results"},{"text":"(c) KIAA1718 contains four segments: a disordered alanine-rich sequence followed by a stretch of prolines, a PHD domain (blue) containing two zinc metals (gray balls), a rigid linker (cyan) and a jumonji domain (green) followed by a four-helix bundle.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-07T08:17:08.545Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MAGAAAAVAAGAAAGAAAAAVSVAAPGRASAPPPPPPVYCVCRQPYDVNRFMIECDICKDWFHGSCVGVEEHHAVDIDLYHCPNCAVLHGSSLMKKRRNWHRHDYTEIDDGSKPVQAGTRTFIKELRSRVFPSADEIIIKMHGSQLTQRYLEKHGFDVPIMVPKLDDLGLRLPSPTFSVMDVERYVGGDKVIDVIDVARQADSKMTLHNYVKYFMNPNRPKVLNVISLEFSDTKMSELVEVPDIAKKLSWVENYWPDDSVFPKPFVQKYCLMGVQDSYTDFHIDFGGTSVWYHVLWGEKIFYLIKPTDENLARYESWSSSVTQSEVFFGDKVDKCYKCVVKQGHTLFVPTGWIHAVLTSQDCMAFGGNFLHNLNIGMQLRCYEMEKRLKTPDLFKFPFFEAICWFVAKNLLETLKELREDGFQPQTYLVQGVKALHTALKLWMKKELVSEHAFEIPDNVRPGHLIKELSKVIRAIEEENGKPVKSQGIPIVCPVSRSSNEATSPYHSRRKMRKLRDHNVRTPSNLDILELHTREVLKRLEMCPWEEDILSSKLNGKFNKHLQPSSTVPEWRAKDNDLRLLLTNGRIIKDERQPFADQSLYTADSENEEDKRRTKKAKMKIEESSGVEGVEHEESQKPLNGFFTRVKSELRSRSSGYSDISESEDSGPECTALKSIFTTEESESSGDEKKQEITSNFKEESNVMRNFLQKSQKPSRSEIPIKRECPTSTSTEEEAIQGMLSMAGLHYSTCLQRQIQSTDCSGERNSLQDPSSCHGSNHEVRQLYRYDKPVECGYHVKTEDPDLRTSSWIKQFDTSRFHPQDLSRSQKCIRKEGSSEISQRVQSRNYVDSSGSSLQNGKYMQNSNLTSGACQISNGSLSPERPVGETSFSVPLHPTKRPASNPPPISNQATKGKRPKKGMATAKQRLGKILKLNRNGHARFFV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"KDM7A"},"synonyms":[{"value":"JHDM1D"},{"value":"KDM7"},{"value":"KIAA1718"}]}],"alphafold_very_low_content":0.47396386822529224,"disorder_content":0.03294367693942614,"disprot_consensus":{"full":[{"start":1,"end":31,"type":"D"}],"Structural state":[{"start":1,"end":31,"type":"D"}]}},{"disprot_id":"DP03625","acc":"Q5NCY0","creator":"maspromonte","date":"2022-04-07T10:30:52.540Z","features":{"pfam":[{"id":"PF02373","name":"JmjC domain, hydroxylase","start":1375,"end":1483},{"id":"PF21322","name":"Lysine-specific demethylase 6/UTY, C-terminal helical domain","start":1490,"end":1545},{"id":"PF21326","name":"KDM6, GATA-like","start":1562,"end":1621}],"gene3D":[]},"length":1641,"name":"Lysine-specific demethylase 6B","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":1132,"end":1156,"reference_id":"22842901","reference_source":"pmid","reference_html":"A selective jumonji H3K27 demethylase inhibitor modulates the proinflammatory macrophage response. <i> Kruidenier L, Chung CW, Cheng Z, Liddle J, Che K, Joberty G, Bantscheff M, Bountra C, Bridges A, Diallo H, Eberhard D, Hutchinson S, Jones E, Katso R, Leveridge M, Mander PK, Mosley J, Ramirez-Molina C, Rowland P, Schofield CJ, Sheppard RJ, Smith JE, Swales C, Tanner R, Thomas P, Tumber A, Drewes G, Oppermann U, Patel DJ, Lee K, Wilson DM. </i> Nature, 2012","date":"2022-08-04T15:43:13.694Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03625r001","statement":[{"text":"The free-form crystals of JmjD3 were produced with construct 1132-1641. Since the 1132-1156 segment was disordered in the free JmjD3 structure, a truncated 1157-1641 construct was inserted into the same vector.","type":"Supplementary material"},{"text":"Despite numerous attempts at co-crystallization of mouse JmjD3 with H3K27me3 peptide, we failed to observe density for the peptide in the crystal structure of the complex. In order to get the peptide-bound JmjD3 structure, we used the engineered mouse JmjD3(1157-1641)-H3 construct described above, in which a PreScission protease site, H3(24-34) and a short linker replaced a disordered internal loop spanning amino acids 1293-1323.","type":"Supplementary material"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-04T17:42:18.477Z"}},{"start":1293,"end":1323,"reference_id":"22842901","reference_source":"pmid","reference_html":"A selective jumonji H3K27 demethylase inhibitor modulates the proinflammatory macrophage response. <i> Kruidenier L, Chung CW, Cheng Z, Liddle J, Che K, Joberty G, Bantscheff M, Bountra C, Bridges A, Diallo H, Eberhard D, Hutchinson S, Jones E, Katso R, Leveridge M, Mander PK, Mosley J, Ramirez-Molina C, Rowland P, Schofield CJ, Sheppard RJ, Smith JE, Swales C, Tanner R, Thomas P, Tumber A, Drewes G, Oppermann U, Patel DJ, Lee K, Wilson DM. </i> Nature, 2012","date":"2022-08-04T15:43:33.400Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"region_id":"DP03625r002","statement":[{"text":"This truncated JMJD3 protein encompasses residues 1,157 to 1,641 and includes a cleaved insertion segment that replaces a disordered loop, to facilitate crystal packing and peptide binding (Supplementary Fig. 2a, b).","type":"Results"},{"text":"In this construct, a peptide segment containing a protease cleavage, H3 peptide and linker, replaced a disordered loop segment, with subsequent cleavage at the protease site.","type":"Supplementary material"},{"text":"The gene coding for peptide sequence LEVLFQGP-TKAARKSAPATGG-GSSGS (corresponding to PreScission protease site, histone H3(22-34) and a short linker)\nwas inserted and replaced a structurally disordered coding segment 1293-1323, with this construct designated as engineered mouse JmjD3(1157-1641)","type":"Supplementary material"},{"text":"Despite numerous attempts at co-crystallization of mouse JmjD3 with H3K27me3 peptide, we failed to observe density for the peptide in the crystal structure of the complex. In order to get the peptide-bound JmjD3 structure, we used the engineered mouse JmjD3(1157-1641)-H3 construct described above, in which a PreScission protease site, H3(24-34) and a short linker replaced a disordered internal loop spanning amino acids 1293-1323.","type":"Supplementary material"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-04T17:42:25.590Z"}}],"regions_counter":2,"released":"2023_12","sequence":"MHRAVDPPGARSAREAFALGGLSCAGAWSSCPPHPPPRSSWLPGGRCSASVGQPPLSAPLPPSHGSSSGHPNKPYYAPGTPTPRPLHGKLESLHGCVQALLREPAQPGLWEQLGQLYESEHDSEEAVCCYHRALRYGGSFAELGPRIGRLQQAQLWNFHAGSCQHRAKVLPPLEQVWNLLHLEHKRNYGAKRGGPPVKRSAEPPVVQPMPPAALSGPSGEEGLSPGGKRRRGCSSEQAGLPPGLPLPPPPPPPPPPPPPPPPPPPPLPGLAISPPFQLTKPGLWNTLHGDAWGPERKGSAPPERQEQRHSMPHSYPYPAPAYSAHPPSHRLVPNTPLGPGPRPPGAESHGCLPATRPPGSDLRESRVQRSRMDSSVSPAASTACVPYAPSRPPGLPGTSSSSSSSSSSNNTGLRGVEPSPGIPGADHYQNPALEISPHQARLGPSAHSSRKPFLTAPAATPHLSLPPGTPSSPPPPCPRLLRPPPPPAWMKGSACRAAREDGEILGELFFGAEGPPRPPPPPLPHRDGFLGPPNPRFSVGTQDSHNPPIPPTTTSSSSSSNSHSSSPTGPVPFPPPSYLARSIDPLPRPSSPTLSPQDPPLPPLTLALPPAPPSSCHQNTSGSFRRSESPRPRVSFPKTPEVGQGPPPGPVSKAPQPVPPGVGELPARGPRLFDFPPTPLEDQFEEPAEFKILPDGLANIMKMLDESIRKEEEQQQQQEAGVAPPPPLKEPFASLQPPFPSDTAPATTTAAPTTATTTTTTTTTTTQEEEKKPPPALPPPPPLAKFPPPPQPQPPPPPPASPASLLKSLASVLEGQKYCYRGTGAAVSTRPGSVPATQYSPSPASGATAPPPTSVAPSAQGSPKPSVSSSSQFSTSGGPWAREHRAGEEPAPGPVTPAQLPPPLPLPPARSESEVLEEISRACETLVERVGRSAINPVDTADPVDSGTEPQPPPAQAKEESGGVAVAAAGPGSGKRRQKEHRRHRRACRDSVGRRPREGRAKAKAKAPKEKSRRVLGNLDLQSEEIQGREKARPDVGGVSKVKTPTAPAPPPAPAPAAQPTPPSAPVPGKKTREEAPGPPGVSRADMLKLRSLSEGPPKELKIRLIKVESGDKETFIASEVEERRLRMADLTISHCAADVMRASKNAKVKGKFRESYLSPAQSVKPKINTEEKLPREKLNPPTPSIYLESKRDAFSPVLLQFCTDPRNPITVIRGLAGSLRLNLGLFSTKTLVEASGEHTVEVRTQVQQPSDENWDLTGTRQIWPCESSRSHTTIAKYAQYQASSFQESLQEERESEDEESEEPDSTTGTSPSSAPDPKNHHIIKFGTNIDLSDAKRWKPQLQELLKLPAFMRVTSTGNMLSHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFAVHEHYWETISAFCDRHGVDYLTGSWWPILDDLYASNIPVYRFVQRPGDLVWINAGTVHWVQATGWCNNIAWNVGPLTAYQYQLALERYEWNEVKNVKSIVPMIHVSWNVARTVKISDPDLFKMIKFCLLQSMKHCQVQRESLVRAGKKIAYQGRVKDEPAYYCNECDVEVFNILFVTSENGSRNTYLVHCEGCARRRSAGLQGVVVLEQYRTEELAQAYDAFTLAPASTSR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"genes":[{"name":{"value":"Kdm6b"},"synonyms":[{"value":"Jmjd3"},{"value":"Kiaa0346"}]}],"alphafold_very_low_content":0.5904936014625228,"disorder_content":0.03412553321145643,"disprot_consensus":{"full":[{"start":1132,"end":1156,"type":"D"},{"start":1293,"end":1323,"type":"D"}],"Structural state":[{"start":1132,"end":1156,"type":"D"},{"start":1293,"end":1323,"type":"D"}]}},{"disprot_id":"DP03626","acc":"O15054","creator":"maspromonte","date":"2022-04-07T12:43:42.707Z","features":{"pfam":[{"id":"PF02373","name":"JmjC domain, hydroxylase","start":1377,"end":1485},{"id":"PF21322","name":"Lysine-specific demethylase 6/UTY, C-terminal helical domain","start":1492,"end":1547},{"id":"PF21326","name":"KDM6, GATA-like","start":1564,"end":1623}],"gene3D":[]},"length":1643,"name":"Lysine-specific demethylase 6B","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1141,"end":1176,"reference_id":"22842901","reference_source":"pmid","reference_html":"A selective jumonji H3K27 demethylase inhibitor modulates the proinflammatory macrophage response. <i> Kruidenier L, Chung CW, Cheng Z, Liddle J, Che K, Joberty G, Bantscheff M, Bountra C, Bridges A, Diallo H, Eberhard D, Hutchinson S, Jones E, Katso R, Leveridge M, Mander PK, Mosley J, Ramirez-Molina C, Rowland P, Schofield CJ, Sheppard RJ, Smith JE, Swales C, Tanner R, Thomas P, Tumber A, Drewes G, Oppermann U, Patel DJ, Lee K, Wilson DM. </i> Nature, 2012","date":"2022-04-07T13:32:44.477Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4ASK"},{"db":"PDB","id":"2XUE"}],"region_id":"DP03626r001","statement":[{"text":"Even if the authors didn't specify the disorder state of the region 1141-1176 as well as they described for mouse JmjD3/KDM6B in the same reference, this segment is absent in PDB","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-01T18:25:10.352Z"}},{"start":1293,"end":1322,"reference_id":"22842901","reference_source":"pmid","reference_html":"A selective jumonji H3K27 demethylase inhibitor modulates the proinflammatory macrophage response. <i> Kruidenier L, Chung CW, Cheng Z, Liddle J, Che K, Joberty G, Bantscheff M, Bountra C, Bridges A, Diallo H, Eberhard D, Hutchinson S, Jones E, Katso R, Leveridge M, Mander PK, Mosley J, Ramirez-Molina C, Rowland P, Schofield CJ, Sheppard RJ, Smith JE, Swales C, Tanner R, Thomas P, Tumber A, Drewes G, Oppermann U, Patel DJ, Lee K, Wilson DM. </i> Nature, 2012","date":"2022-08-04T15:44:23.493Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4ASK"},{"db":"PDB","id":"2XUE"}],"region_id":"DP03626r002","statement":[{"text":"Even if the authors didn't specify the disorder state of the loop 1292-1322 as well as they described for mouse JmjD3/KDM6B in the same reference, this segment is absent in PDB","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-04T17:44:29.123Z"}},{"start":1141,"end":1157,"reference_id":"29220567","reference_source":"pmid","reference_html":"Structural Basis of Histone Demethylase KDM6B Histone 3 Lysine 27 Specificity. <i> Jones SE, Olsen L, Gajhede M. </i> Biochemistry, 2018","date":"2022-08-04T15:46:47.893Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5OY3"}],"region_id":"DP03626r003","statement":[{"text":"Even if the authors didn't specify the disorder state of the region 1141-1157, this segment is absent in PDB","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P68431"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-04T17:44:29.716Z"}},{"start":1292,"end":1323,"reference_id":"29220567","reference_source":"pmid","reference_html":"Structural Basis of Histone Demethylase KDM6B Histone 3 Lysine 27 Specificity. <i> Jones SE, Olsen L, Gajhede M. </i> Biochemistry, 2018","date":"2022-08-04T15:47:14.193Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5OY3"}],"region_id":"DP03626r004","statement":[{"text":"Even if the authors didn't specify the disorder state of the region 1292-1323, this segment is absent in PDB","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P68431"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-04T17:43:44.290Z"}}],"regions_counter":4,"released":"2023_06","sequence":"MHRAVDPPGARAAREAFALGGLSCAGAWSSCPPHPPPRSAWLPGGRCSASIGQPPLPAPLPPSHGSSSGHPSKPYYAPGAPTPRPLHGKLESLHGCVQALLREPAQPGLWEQLGQLYESEHDSEEATRCYHSALRYGGSFAELGPRIGRLQQAQLWNFHTGSCQHRAKVLPPLEQVWNLLHLEHKRNYGAKRGGPPVKRAAEPPVVQPVPPAALSGPSGEEGLSPGGKRRRGCNSEQTGLPPGLPLPPPPLPPPPPPPPPPPPPLPGLATSPPFQLTKPGLWSTLHGDAWGPERKGSAPPERQEQRHSLPHPYPYPAPAYTAHPPGHRLVPAAPPGPGPRPPGAESHGCLPATRPPGSDLRESRVQRSRMDSSVSPAATTACVPYAPSRPPGLPGTTTSSSSSSSSNTGLRGVEPNPGIPGADHYQTPALEVSHHGRLGPSAHSSRKPFLGAPAATPHLSLPPGPSSPPPPPCPRLLRPPPPPAWLKGPACRAAREDGEILEELFFGTEGPPRPAPPPLPHREGFLGPPASRFSVGTQDSHTPPTPPTPTTSSSNSNSGSHSSSPAGPVSFPPPPYLARSIDPLPRPPSPAQNPQDPPLVPLTLALPPAPPSSCHQNTSGSFRRPESPRPRVSFPKTPEVGPGPPPGPLSKAPQPVPPGVGELPARGPRLFDFPPTPLEDQFEEPAEFKILPDGLANIMKMLDESIRKEEEQQQHEAGVAPQPPLKEPFASLQSPFPTDTAPTTTAPAVAVTTTTTTTTTTTATQEEEKKPPPALPPPPPLAKFPPPSQPQPPPPPPPSPASLLKSLASVLEGQKYCYRGTGAAVSTRPGPLPTTQYSPGPPSGATALPPTSAAPSAQGSPQPSASSSSQFSTSGGPWARERRAGEEPVPGPMTPTQPPPPLSLPPARSESEVLEEISRACETLVERVGRSATDPADPVDTAEPADSGTERLLPPAQAKEEAGGVAAVSGSCKRRQKEHQKEHRRHRRACKDSVGRRPREGRAKAKAKVPKEKSRRVLGNLDLQSEEIQGREKSRPDLGGASKAKPPTAPAPPSAPAPSAQPTPPSASVPGKKAREEAPGPPGVSRADMLKLRSLSEGPPKELKIRLIKVESGDKETFIASEVEERRLRMADLTISHCAADVVRASRNAKVKGKFRESYLSPAQSVKPKINTEEKLPREKLNPPTPSIYLESKRDAFSPVLLQFCTDPRNPITVIRGLAGSLRLNLGLFSTKTLVEASGEHTVEVRTQVQQPSDENWDLTGTRQIWPCESSRSHTTIAKYAQYQASSFQESLQEEKESEDEESEEPDSTTGTPPSSAPDPKNHHIIKFGTNIDLSDAKRWKPQLQELLKLPAFMRVTSTGNMLSHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFAVHEHYWETISAFCDRHGVDYLTGSWWPILDDLYASNIPVYRFVQRPGDLVWINAGTVHWVQATGWCNNIAWNVGPLTAYQYQLALERYEWNEVKNVKSIVPMIHVSWNVARTVKISDPDLFKMIKFCLLQSMKHCQVQRESLVRAGKKIAYQGRVKDEPAYYCNECDVEVFNILFVTSENGSRNTYLVHCEGCARRRSAGLQGVVVLEQYRTEELAQAYDAFTLAPASTSR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"genes":[{"name":{"value":"KDM6B"},"synonyms":[{"value":"JMJD3"},{"value":"KIAA0346"}]}],"alphafold_very_low_content":0.5934266585514303,"disorder_content":0.041387705416920266,"disprot_consensus":{"full":[{"start":1141,"end":1176,"type":"D"},{"start":1292,"end":1323,"type":"D"}],"Structural state":[{"start":1141,"end":1176,"type":"D"},{"start":1292,"end":1323,"type":"D"}]}},{"disprot_id":"DP03627","acc":"O15550","creator":"maspromonte","date":"2022-04-07T14:29:57.497Z","features":{"pfam":[{"id":"PF02373","name":"JmjC domain, hydroxylase","start":1133,"end":1241},{"id":"PF13181","name":"Tetratricopeptide repeat","start":205,"end":233},{"id":"PF21322","name":"Lysine-specific demethylase 6/UTY, C-terminal helical domain","start":1248,"end":1303},{"id":"PF21326","name":"KDM6, GATA-like","start":1320,"end":1380}],"gene3D":[]},"length":1401,"name":"Lysine-specific demethylase 6A","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1048,"end":1077,"reference_id":"22002947","reference_source":"pmid","reference_html":"Structural basis for histone H3 Lys 27 demethylation by UTX/KDM6A. <i> Sengoku T, Yokoyama S. </i> Genes Dev, 2011","date":"2022-04-07T14:35:25.009Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3AVR"},{"db":"PDB","id":"3AVS"}],"region_id":"DP03627r001","statement":[{"text":"The helical domain, the linker region, the jumonji domain, and the zinc-binding domain are colored pink, orange, blue, and green, respectively. Disordered regions are shown with dashed lines.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-11T11:33:01.133Z"}},{"start":1051,"end":1077,"reference_id":"30226987","reference_source":"pmid","reference_html":"In Silico Identification of JMJD3 Demethylase Inhibitors. <i> Esposito C, Wiedmer L, Caflisch A. </i> J Chem Inf Model, 2018","date":"2022-04-08T09:26:05.336Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6FUL"},{"db":"PDB","id":"6FUK"}],"region_id":"DP03627r002","statement":[{"text":"Even if the authors didn't specify as disordered the region 1051-1077, these residues are absent in PDB","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-11T11:31:26.567Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MKSCGVSLATAAAAAAAFGDEEKKMAAGKASGESEEASPSLTAEEREALGGLDSRLFGFVRFHEDGARTKALLGKAVRCYESLILKAEGKVESDFFCQLGHFNLLLEDYPKALSAYQRYYSLQSDYWKNAAFLYGLGLVYFHYNAFQWAIKAFQEVLYVDPSFCRAKEIHLRLGLMFKVNTDYESSLKHFQLALVDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTENLSAQVKATVLQQLGWMHHTVDLLGDKATKESYAIQYLQKSLEADPNSGQSWYFLGRCYSSIGKVQDAFISYRQSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNATRSKSCSNTSALAARIKYLQAQLCNLPQGSLQNKTKLLPSIEEAWSLPIPAELTSRQGAMNTAQQNTSDNWSGGHAVSHPPVQQQAHSWCLTPQKLQHLEQLRANRNNLNPAQKLMLEQLESQFVLMQQHQMRPTGVAQVRSTGIPNGPTADSSLPTNSVSGQQPQLALTRVPSVSQPGVRPACPGQPLANGPFSAGHVPCSTSRTLGSTDTILIGNNHITGSGSNGNVPYLQRNALTLPHNRTNLTSSAEEPWKNQLSNSTQGLHKGQSSHSAGPNGERPLSSTGPSQHLQAAGSGIQNQNGHPTLPSNSVTQGAALNHLSSHTATSGGQQGITLTKESKPSGNILTVPETSRHTGETPNSTASVEGLPNHVHQMTADAVCSPSHGDSKSPGLLSSDNPQLSALLMGKANNNVGTGTCDKVNNIHPAVHTKTDNSVASSPSSAISTATPSPKSTEQTTTNSVTSLNSPHSGLHTINGEGMEESQSPMKTDLLLVNHKPSPQIIPSMSVSIYPSSAEVLKACRNLGKNGLSNSSILLDKCPPPRPPSSPYPPLPKDKLNPPTPSIYLENKRDAFFPPLHQFCTNPNNPVTVIRGLAGALKLDLGLFSTKTLVEANNEHMVEVRTQLLQPADENWDPTGTKKIWHCESNRSHTTIAKYAQYQASSFQESLREENEKRSHHKDHSDSESTSSDNSGRRRKGPFKTIKFGTNIDLSDDKKWKLQLHELTKLPAFVRVVSAGNLLSHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPEGYWGVLNDFCEKNNLNFLMGSWWPNLEDLYEANVPVYRFIQRPGDLVWINAGTVHWVQAIGWCNNIAWNVGPLTACQYKLAVERYEWNKLQSVKSIVPMVHLSWNMARNIKVSDPKLFEMIKYCLLRTLKQCQTLREALIAAGKEIIWHGRTKEEPAHYCSICEVEVFDLLFVTNESNSRKTYIVHCQDCARKTSGNLENFVVLEQYKMEDLMQVYDQFTLAPPLPSASS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Cancer-related proteins"],"genes":[{"name":{"value":"KDM6A"},"synonyms":[{"value":"UTX"}]}],"alphafold_very_low_content":0.35046395431834404,"disorder_content":0.021413276231263382,"disprot_consensus":{"full":[{"start":1048,"end":1077,"type":"D"}],"Structural state":[{"start":1048,"end":1077,"type":"D"}]}},{"disprot_id":"DP03628","acc":"P52732","creator":"maspromonte","date":"2022-04-08T11:16:16.565Z","features":{"pfam":[{"id":"PF00225","name":"Kinesin motor domain","start":24,"end":359},{"id":"PF13931","name":"Kinesin-associated microtubule-binding","start":916,"end":1053}],"gene3D":[]},"length":1056,"name":"Kinesin-like protein KIF11","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":15,"reference_id":"11328809","reference_source":"pmid","reference_html":"Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker. <i> Turner J, Anderson R, Guo J, Beraud C, Fletterick R, Sakowicz R. </i> J Biol Chem, 2001","date":"2022-04-08T11:19:41.706Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1II6"}],"region_id":"DP03628r001","statement":[{"text":"Residues 1–15, 271–279, and 366 –368 in the first monomer and residues 1–15, 271–284, and 366 –368 in the second were not observed in the electron density.","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-11T11:45:32.170Z"}},{"start":1,"end":16,"reference_id":"16458511","reference_source":"pmid","reference_html":"Inhibitors of human mitotic kinesin Eg5: characterization of the 4-phenyl-tetrahydroisoquinoline lead series. <i> Tarby CM, Kaltenbach RF, Huynh T, Pudzianowski A, Shen H, Ortega-Nanos M, Sheriff S, Newitt JA, McDonnell PA, Burford N, Fairchild CR, Vaccaro W, Chen Z, Borzilleri RM, Naglich J, Lombardo LJ, Gottardis M, Trainor GL, Roussell DL. </i> Bioorg Med Chem Lett, 2006","date":"2022-04-12T15:21:03.314Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2FME"}],"region_id":"DP03628r004","statement":[{"text":"The authors didn't specify the state of the first 16 residues in the first and second monomer, but these residues were not observed in the PDB","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-01T19:38:16.533Z"}},{"start":272,"end":286,"reference_id":"31459302","reference_source":"pmid","reference_html":"Structural and Thermodynamic Basis of the Enhanced Interaction between Kinesin Spindle Protein Eg5 and STLC-type Inhibitors. <i> Yokoyama H, Sawada JI, Sato K, Ogo N, Kamei N, Ishikawa Y, Hara K, Asai A, Hashimoto H. </i> ACS Omega, 2018","date":"2022-09-28T14:48:09.049Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5ZO7"},{"db":"PDB","id":"5ZO9"},{"db":"PDB","id":"5ZO8"}],"region_id":"DP03628r005","statement":[{"text":"Residues 55–58 (L2) and 272–286 (L11) are missing for molecules A and B (Figure 2A). These loop regions are also missing in other Eg5 structures.","type":"Results"},{"text":"Residues 55–60 (L2) and 272–286 (L11) are missing for molecules A and B.","type":"Results"},{"text":"The dotted lines indicate the disordered regions.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-28T15:52:47.037Z"}},{"start":272,"end":286,"reference_id":"30031975","reference_source":"pmid","reference_html":"Crystal structure of the Eg5 - K858 complex and implications for structure-based design of thiadiazole-containing inhibitors. <i> Talapatra SK, Tham CL, Guglielmi P, Cirilli R, Chandrasekaran B, Karpoormath R, Carradori S, Kozielski F. </i> Eur J Med Chem, 2018","date":"2022-04-12T15:45:08.753Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6G6Z"},{"db":"PDB","id":"6G6Y"}],"region_id":"DP03628r006","statement":[{"text":"In the former space group, loops containing residues 56–60, 176–179, 249-243 and 272–286 are missing in the structure, whereas in the latter space group the regions 34–35 and 272–287 are absent.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-01T19:58:41.662Z"}},{"start":108,"end":126,"reference_id":"25622007","reference_source":"pmid","reference_html":"Structural basis of new allosteric inhibition in Kinesin spindle protein Eg5. <i> Yokoyama H, Sawada J, Katoh S, Matsuno K, Ogo N, Ishikawa Y, Hashimoto H, Fujii S, Asai A. </i> ACS Chem Biol, 2015","date":"2022-04-12T16:00:29.529Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3WPN"}],"region_id":"DP03628r007","statement":[{"text":"Four regions corresponding to residues 57–58 (L2), 108–126 (regions of the P-loop, N-terminal α2, and L5), 225–231 (L9), and 270–287 (L11) are missing due to high flexibility (Figure 2A). The large flexible loop, L5, which is typically inserted in the middle of the α2 helix in other Eg5 structures, is absent in Eg5-PVZB1194 (Supporting Information, Figure S1). ","type":"Results"},{"text":"Dotted lines indicate the disordered regions. ","type":"Figure"},{"text":"The ATP-binding pocket mainly consists of P-loop, L9, and L11, which is surrounded by α1, β3, α2, and L5. In the structure of Eg5-PVZB1194, residues Thr107 and Glu129, instead of a nucleotide, occupy the ATP-binding site of Eg5-AMPPNP, although residues 108–126 are disordered (Figure 5A)","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-01T19:42:33.513Z"}},{"start":270,"end":287,"reference_id":"25622007","reference_source":"pmid","reference_html":"Structural basis of new allosteric inhibition in Kinesin spindle protein Eg5. <i> Yokoyama H, Sawada J, Katoh S, Matsuno K, Ogo N, Ishikawa Y, Hashimoto H, Fujii S, Asai A. </i> ACS Chem Biol, 2015","date":"2022-04-12T16:03:03.008Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3WPN"}],"region_id":"DP03628r008","statement":[{"text":"Four regions corresponding to residues 57–58 (L2), 108–126 (regions of the P-loop, N-terminal α2, and L5), 225–231 (L9), and 270–287 (L11) are missing due to high flexibility (Figure 2A). The large flexible loop, L5, which is typically inserted in the middle of the α2 helix in other Eg5 structures, is absent in Eg5-PVZB1194 (Supporting Information, Figure S1). ","type":"Results"},{"text":"Dotted lines indicate the disordered regions. ","type":"Figure"},{"text":"The charged amino acids in L11, missing in the crystal structure due to its high flexibility, are located close to the entrance of the biphenyl-binding pocket (Figure 2A). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-01T19:43:06.142Z"}},{"start":1,"end":14,"reference_id":"25622007","reference_source":"pmid","reference_html":"Structural basis of new allosteric inhibition in Kinesin spindle protein Eg5. <i> Yokoyama H, Sawada J, Katoh S, Matsuno K, Ogo N, Ishikawa Y, Hashimoto H, Fujii S, Asai A. </i> ACS Chem Biol, 2015","date":"2022-08-04T16:06:51.354Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3WPN"}],"region_id":"DP03628r011","statement":[{"text":"The authors didn't specify the state of the first 14 residues, but were not observed in the PDB","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-04T17:47:07.237Z"}}],"regions_counter":11,"released":"2023_06","sequence":"MASQPNSSAKKKEEKGKNIQVVVRCRPFNLAERKASAHSIVECDPVRKEVSVRTGGLADKSSRKTYTFDMVFGASTKQIDVYRSVVCPILDEVIMGYNCTIFAYGQTGTGKTFTMEGERSPNEEYTWEEDPLAGIIPRTLHQIFEKLTDNGTEFSVKVSLLEIYNEELFDLLNPSSDVSERLQMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRTTAATLMNAYSSRSHSVFSVTIHMKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERTPHVPYRESKLTRILQDSLGGRTRTSIIATISPASLNLEETLSTLEYAHRAKNILNKPEVNQKLTKKALIKEYTEEIERLKRDLAAAREKNGVYISEENFRVMSGKLTVQEEQIVELIEKIGAVEEELNRVTELFMDNKNELDQCKSDLQNKTQELETTQKHLQETKLQLVKEEYITSALESTEEKLHDAASKLLNTVEETTKDVSGLHSKLDRKKAVDQHNAEAQDIFGKNLNSLFNNMEELIKDGSSKQKAMLEVHKTLFGNLLSSSVSALDTITTVALGSLTSIPENVSTHVSQIFNMILKEQSLAAESKTVLQELINVLKTDLLSSLEMILSPTVVSILKINSQLKHIFKTSLTVADKIEDQKKELDGFLSILCNNLHELQENTICSLVESQKQCGNLTEDLKTIKQTHSQELCKLMNLWTERFCALEEKCENIQKPLSSVQENIQQKSKDIVNKMTFHSQKFCADSDGFSQELRNFNQEGTKLVEESVKHSDKLNGNLEKISQETEQRCESLNTRTVYFSEQWVSSLNEREQELHNLLEVVSQCCEASSSDITEKSDGRKAAHEKQHNIFLDQMTIDEDKLIAQNLELNETIKIGLTKLNCFLEQDLKLDIPTGTTPQRKSYLYPSTLVRTEPREHLLDQLKRKQPELLMMLNCSENNKEETIPDVDVEEAVLGQYTEEPLSQEPSVDAGVDCSSIGGVPFFQHKKSHGKDKENRGINTLERSKVEETTEHLVTKSRLPLRAQINL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"genes":[{"name":{"value":"KIF11"},"synonyms":[{"value":"EG5"},{"value":"KNSL1"},{"value":"TRIP5"}]}],"alphafold_very_low_content":0.13352272727272727,"disorder_content":0.050189393939393936,"disprot_consensus":{"full":[{"start":1,"end":16,"type":"D"},{"start":108,"end":126,"type":"D"},{"start":270,"end":287,"type":"D"}],"Structural state":[{"start":1,"end":16,"type":"D"},{"start":108,"end":126,"type":"D"},{"start":270,"end":287,"type":"D"}]}},{"disprot_id":"DP03629","acc":"Q9QR99","creator":"tlazar","date":"2022-04-08T12:57:37.299Z","features":{"pfam":[{"id":"PF00077","name":"Retroviral aspartyl protease","start":454,"end":558},{"id":"PF00098","name":"Zinc knuckle","start":356,"end":372},{"id":"PF00607","name":"gag protein p24 N-terminal domain","start":141,"end":256},{"id":"PF02228","name":"Major core protein p19","start":1,"end":92},{"id":"PF19317","name":"Gag protein p24 C-terminal domain","start":258,"end":331}],"gene3D":[]},"length":647,"name":"Pr gag-pro","ncbi_taxon_id":11908,"organism":"Human T-cell leukemia virus type I","regions":[{"start":100,"end":130,"reference_id":"34298060","reference_source":"pmid","reference_html":"Structural Insights into the Mechanism of Human T-cell Leukemia Virus Type 1 Gag Targeting to the Plasma Membrane for Assembly. <i> Herrmann D, Zhou LW, Hanson HM, Willkomm NA, Mansky LM, Saad JS. </i> J Mol Biol, 2021","date":"2022-04-08T13:12:15.474Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP03629r002","statement":[{"text":"The MA structure consists of four a-helices and unstructured N- and C-termini.","type":"Abstract"},{"text":"2D 1H-15N HSQC data obtained for myr(–)MA and myr(–)MA99 confirmed that truncation of the C-terminal 31 residues did not adversely affect the structure and/or fold of the globular domain (Figures 1(A) and S2).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-08T15:12:05.494Z"}},{"start":100,"end":130,"reference_id":"34298060","reference_source":"pmid","reference_html":"Structural Insights into the Mechanism of Human T-cell Leukemia Virus Type 1 Gag Targeting to the Plasma Membrane for Assembly. <i> Herrmann D, Zhou LW, Hanson HM, Willkomm NA, Mansky LM, Saad JS. </i> J Mol Biol, 2021","date":"2022-04-08T13:17:18.234Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP03629r003","statement":[{"text":"The MA structure consists of four a-helices and unstructured N- and C-termini.","type":"Abstract"},{"text":"A gel filtration mobility assay with known protein standards revealed that the estimated molecular weight of myr(–)MA and myr(–) MA99 proteins are ~24 and 10 kDa, respectively (Figure S1). Whereas the estimated molecular weight of myr(–)MA appears to be higher than the calculated monomeric unit (~15 kDa), no evidence for protein self-association was observed at all tested protein concentrations. The migration behavior of myr(–)MA is likely attributed to its shape caused by the unstructured C-terminal 31 residues.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-08T14:57:56.834Z"}}],"regions_counter":4,"released":"2023_06","sequence":"MGQIFSRSASPIPRPPRGLAAHHWLNFLQAAYRLEPGPSSYDFHQLKKFLKIALETPVWICPINYSLLASLLPKGYPGRVNEILHILIQTQAQIPSRPAPPPPSSPTHDPPDSDPQIPPPYVEPTAPQVLPVMHPHGAPPNHRPWQMKDLQAIKQEVSQAAPGSPQFMQTIRLAVQQFDPTAKDLQDLLQYLCSSLVASLHHQQLDSLISEAETRGITGYNPLAGPLRVQANNPQQQGLRREYQQLWLAAFAALPGSAKDPSWASILQGLEEPYHAFVERLNIALDNGLPEGTPKDPILRSLAYSNANKECQKLLQARGHTNSPLGDMLRACQTWTPKDKTKVLVVQPKKPPPNQPCFRCGKAGHWSRDCTQPRPPPGPCPLCQDPTHWKRDCPRLKPTIPEPEPEEDALLLDLPTDIPHPKNLHRGGPPTLQQVLPNQDPASILPVIPLDPARRPVIKAQVDTQTSHPKTIEALLDTGADMTVLPIALFSSNTPLKNTSVLGAGGQTQDHFKLTSLPVLIRLPFRTTPIVLTSCLVDTKNNWAIIGRDALQQCQGVLYLPEAKGPPVILPIQAPAVLGLEHLPRPPEISQFPLNQNASRPCNTWSGRPWRQAISNPTPGQEITQYSQLKRPMEPGDSSTTCGPLTL","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Deltaretrovirus"],"dataset":["Viral proteins"],"genes":[{"name":{"value":"gag-pro","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAD50662.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD50662.1"}}]}}],"disorder_content":0.04791344667697063,"disprot_consensus":{"full":[{"start":100,"end":130,"type":"D"}],"Structural state":[{"start":100,"end":130,"type":"D"}]}},{"disprot_id":"DP03630","acc":"P07197","creator":"tlazar","date":"2022-04-11T08:59:14.811Z","features":{"pfam":[{"id":"PF00038","name":"Intermediate filament protein","start":100,"end":411},{"id":"PF04732","name":"Intermediate filament head (DNA binding) region","start":10,"end":98}],"gene3D":[]},"length":916,"name":"Neurofilament medium polypeptide","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":790,"end":916,"reference_id":"35454150","reference_source":"pmid","reference_html":"Distribution of Charged Residues Affects the Average Size and Shape of Intrinsically Disordered Proteins. <i> Bianchi G, Mangiagalli M, Barbiroli A, Longhi S, Grandori R, Santambrogio C, Brocca S. </i> Biomolecules, 2022","date":"2022-04-25T09:12:47.929Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03630r001","statement":[{"text":"Size-exclusion chromatography was employed to estimate the Rh values of the three sets of model IDPs (Table 2).","type":"Results"},{"text":"The Rh of wt NFM (3.31 ± 0.12) is determined here for the first time.","type":"Results"},{"text":"Experimentally determined Rh is even greater than the theoretical Rh for IDPs [Marsh & Forman-Kay, 2010].","type":"Curator statement"},{"text":"Rt (nm) = 2.54","type":"Table"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-28T13:32:02.464Z"}},{"start":790,"end":916,"reference_id":"35454150","reference_source":"pmid","reference_html":"Distribution of Charged Residues Affects the Average Size and Shape of Intrinsically Disordered Proteins. <i> Bianchi G, Mangiagalli M, Barbiroli A, Longhi S, Grandori R, Santambrogio C, Brocca S. </i> Biomolecules, 2022","date":"2022-04-25T09:12:56.103Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006283","ec_ontology":"ECO","ec_name":"electrospray ionization fourier transform ion cyclotron resonance mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03630r002","statement":[{"text":"Native MS was employed to assess the conformational properties of the three sets of IDPs. In this approach, the CSDs resulting from the nanoESI process reflect the overall compactness and relative amounts of the main conformers in the original solution [17,18,22]. Native-MS spectra obtained under non-denaturing conditions for the three variants of NTAIL (Figure 4a), NFM, and PNT4 (Figure S3) display multimodal CSDs, highlighting the heterogeneous conformational ensemble typical of IDPs.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-28T13:31:55.793Z"}},{"start":790,"end":916,"reference_id":"35454150","reference_source":"pmid","reference_html":"Distribution of Charged Residues Affects the Average Size and Shape of Intrinsically Disordered Proteins. <i> Bianchi G, Mangiagalli M, Barbiroli A, Longhi S, Grandori R, Santambrogio C, Brocca S. </i> Biomolecules, 2022","date":"2022-04-25T09:13:01.005Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03630r003","statement":[{"text":"Figure S2. Far-UV CD spectra of model IDPs. CD spectra of NTAIL (a), NFM (b), and PNT4 (c) variants.","type":"Supplementary material"},{"text":"Typical random coil-like far-UV CD spectrum is displayed for NFM.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-28T13:31:43.450Z"}}],"regions_counter":3,"released":"2023_12","sequence":"MSYTLDSLGNPSAYRRVTETRSSFSRVSGSPSSGFRSQSWSRGSPSTVSSSYKRSMLAPRLAYSSAMLSSAESSLDFSQSSSLLNGGSGPGGDYKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEEASLVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLESHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETRFSTFAGSITGPLYTHRPPITISSKIQKPKVEAPKLKVQHKFVEEIIEETKVEDEKSEMEEALTAITEELAVSMKEEKKEAAEEKEEEPEAEEEEVAAKKSPVKATAPEVKEEEGEKEEEEGQEEEEEEDEGAKSDQAEEGGSEKEGSSEKEEGEQEEGETEAEAEGEEAEAKEEKKVEEKSEEVATKEELVADAKVEKPEKAKSPVPKSPVEEKGKSPVPKSPVEEKGKSPVPKSPVEEKGKSPVPKSPVEEKGKSPVSKSPVEEKAKSPVPKSPVEEAKSKAEVGKGEQKEEEEKEVKEAPKEEKVEKKEEKPKDVPEKKKAESPVKEEAVAEVVTITKSVKVHLEKETKEEGKPLQQEKEKEKAGGEGGSEEEGSDKGAKGSRKEDIAVNGEVEGKEEVEQETKEKGSGREEEKGVVTNGLDLSPADEKKGGDKSEEKVVVTKTVEKITSEGGDGATKYITKSVTVTQKVEEHEETFEEKLVSTKKVEKVTSHAIVKEVTQSD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"NEFM"},"synonyms":[{"value":"NEF3"},{"value":"NFM"}]}],"alphafold_very_low_content":0.574235807860262,"disorder_content":0.13864628820960698,"disprot_consensus":{"full":[{"start":790,"end":916,"type":"D"}],"Structural state":[{"start":790,"end":916,"type":"D"}]}},{"disprot_id":"DP03631","acc":"P0A9J4","creator":"vacs","date":"2022-04-14T15:10:13.861Z","features":{"pfam":[{"id":"PF02558","name":"Ketopantoate reductase PanE/ApbA","start":3,"end":143},{"id":"PF08546","name":"Ketopantoate reductase PanE/ApbA C terminal","start":168,"end":289}],"gene3D":[]},"length":303,"name":"2-dehydropantoate 2-reductase","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":294,"end":303,"reference_id":"15966718","reference_source":"pmid","reference_html":"The crystal structure of Escherichia coli ketopantoate reductase with NADP+ bound. <i> Lobley CM, Ciulli A, Whitney HM, Williams G, Smith AG, Abell C, Blundell TL. </i> Biochemistry, 2005","date":"2022-04-14T15:12:42.784Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1YJQ"}],"region_id":"DP03631r001","statement":[{"text":"The final structure includes residues 1-293 of KPR in complex with one molecule of bound NADP+.","type":"Methods"},{"text":"The C-terminal 10 residues were disordered in the electron density and were not rebuilt. This reflects the situation in the apo crystal structure where the C-terminal 12 residues are disordered (14).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-19T11:31:55.065Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MKITVLGCGALGQLWLTALCKQGHEVQGWLRVPQPYCSVNLVETDGSIFNESLTANDPDFLATSDLLLVTLKAWQVSDAVKSLASTLPVTTPILLIHNGMGTIEELQNIQQPLLMGTTTHAARRDGNVIIHVANGITHIGPARQQDGDYSYLADILQTVLPDVAWHNNIRAELWRKLAVNCVINPLTAIWNCPNGELRHHPQEIMQICEEVAAVIEREGHHTSAEDLRDYVMQVIDATAENISSMLQDIRALRHTEIDYINGFLLRRARAHGIAVPENTRLFEMVKRKESEYERIGTGLPRPW","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"genes":[{"name":{"value":"panE"},"synonyms":[{"value":"apbA"}],"olnNames":[{"value":"b0425"},{"value":"JW0415"}]}],"alphafold_very_low_content":0.026402640264026403,"disorder_content":0.033003300330033,"disprot_consensus":{"full":[{"start":294,"end":303,"type":"D"}],"Structural state":[{"start":294,"end":303,"type":"D"}]}},{"disprot_id":"DP03632","acc":"P49954","creator":"vacs","date":"2022-04-14T15:57:23.325Z","features":{"pfam":[{"id":"PF00795","name":"Carbon-nitrogen hydrolase","start":12,"end":272}],"gene3D":[]},"length":291,"name":"Omega-amidase NIT3","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":132,"end":141,"reference_id":"12833551","reference_source":"pmid","reference_html":"Crystal structure of a putative CN hydrolase from yeast. <i> Kumaran D, Eswaramoorthy S, Gerchman SE, Kycia H, Studier FW, Swaminathan S. </i> Proteins, 2003","date":"2022-04-15T08:32:09.418Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1F89"}],"region_id":"DP03632r001","statement":[{"text":"The two α/β halves of the structure are connected at one end by 28 residues containing helix α4 and a disordered region between β5 and β6, and at the other by a six-residue loop between β11 and β12.","type":"Results"},{"text":"An internal loop region of 10 residues (132–141) and nine C-terminal residues are disordered and are not detected in the electron density of either monomer.","type":"Results"},{"text":"This cysteine is more accessible in P018 (16 Å2) than in DCases (8 Å2). However, this may be an artifact of missing residues 132–141 in P018.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-19T11:32:45.375Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MSASKILSQKIKVALVQLSGSSPDKMANLQRAATFIERAMKEQPDTKLVVLPECFNSPYSTDQFRKYSEVINPKEPSTSVQFLSNLANKFKIILVGGTIPELDPKTDKIYNTSIIFNEDGKLIDKHRKVHLFDVDIPNGISFHESETLSPGEKSTTIDTKYGKFGVGICYDMRFPELAMLSARKGAFAMIYPSAFNTVTGPLHWHLLARSRAVDNQVYVMLCSPARNLQSSYHAYGHSIVVDPRGKIVAEAGEGEEIIYAELDPEVIESFRQAVPLTKQRRFDVYSDVNAH","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"genes":[{"name":{"value":"NIT3"},"orfNames":[{"value":"L9638.5"}],"olnNames":[{"value":"YLR351C"}]}],"alphafold_very_low_content":0.010309278350515464,"disorder_content":0.03436426116838488,"disprot_consensus":{"full":[{"start":132,"end":141,"type":"D"}],"Structural state":[{"start":132,"end":141,"type":"D"}]}},{"disprot_id":"DP03633","acc":"P36421","creator":"vacs","date":"2022-04-19T11:14:25.602Z","features":{"pfam":[{"id":"PF00579","name":"tRNA synthetases class I (W and Y)","start":37,"end":335}],"gene3D":[]},"length":394,"name":"Tyrosine--tRNA ligase, cytoplasmic","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":224,"end":233,"reference_id":"17576676","reference_source":"pmid","reference_html":"Structural basis for recognition of cognate tRNA by tyrosyl-tRNA synthetase from three kingdoms. <i> Tsunoda M, Kusakabe Y, Tanaka N, Ohno S, Nakamura M, Senda T, Moriguchi T, Asai N, Sekine M, Yokogawa T, Nishikawa K, Nakamura KT. </i> Nucleic Acids Res, 2007","date":"2022-04-19T11:22:53.364Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2DLC"}],"region_id":"DP03633r001","statement":[{"text":"Residues 224–233 of SceTyrRS, the base moieties 16, 20, 31, 40, 41 and 46 of tRNATyr, and the whole nucleotides 17, 20a, 20b, 32 and 33 of tRNATyr, were disordered.","type":"Methods"},{"text":"A loop region between the two domains (residues 224–233), including the KMSKS signature motif, which is one of the two consensus motifs conserved among the class I aaRSs, is disordered.","type":"Results"},{"text":"In the present structure of SceTyrRS, residues 224–233, including the KMSAS sequence (Figure 3), are disordered. This flexibility of the loop containing the KMSKS motif would allow the Tyr-AMP to be fully exposed and the 3′-CCA terminus of tRNA to access the aminoacyl transfer center.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-19T11:26:41.355Z"}},{"start":224,"end":233,"reference_id":"17576676","reference_source":"pmid","reference_html":"Structural basis for recognition of cognate tRNA by tyrosyl-tRNA synthetase from three kingdoms. <i> Tsunoda M, Kusakabe Y, Tanaka N, Ohno S, Nakamura M, Senda T, Moriguchi T, Asai N, Sekine M, Yokogawa T, Nishikawa K, Nakamura KT. </i> Nucleic Acids Res, 2007","date":"2022-04-19T11:53:57.887Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2DLC"}],"region_id":"DP03633r002","statement":[{"text":"A loop region between the two domains (residues 224–233), including the KMSKS signature motif, which is one of the two consensus motifs conserved among the class I aaRSs, is disordered.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-04-20T12:22:20.117Z"}}],"regions_counter":2,"released":"2023_12","sequence":"MSSAATVDPNEAFGLITKNLQEVLNPQIIKDVLEVQKRHLKLYWGTAPTGRPHCGYFVPMTKLADFLKAGCEVTVLLADLHAFLDNMKAPLEVVNYRAKYYELTIKAILRSINVPIEKLKFVVGSSYQLTPDYTMDIFRLSNIVSQNDAKRAGADVVKQVANPLLSGLIYPLMQALDEQFLDVDCQFGGVDQRKIFVLAEENLPSLGYKKRAHLMNPMVPGLAQGGKMSASDPNSKIDLLEEPKQVKKKINSAFCSPGNVEENGLLSFVQYVIAPIQELKFGTNHFEFFIDRPEKFGGPITYKSFEEMKLAFKEEKLSPPDLKIGVADAINELLEPIRQEFANNKEFQEASEKGYPVATPQKSKKAKKPKNKGTKYPGATKTNEIATKLEETKL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"genes":[{"name":{"value":"TYS1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8509419","url":"http://www.ncbi.nlm.nih.gov/pubmed/8509419","alternativeUrl":"https://europepmc.org/abstract/MED/8509419"}}]},"synonyms":[{"value":"MGM104"}],"orfNames":[{"value":"G7522"}],"olnNames":[{"value":"YGR185C"}]}],"alphafold_very_low_content":0.08375634517766498,"disorder_content":0.025380710659898477,"disprot_consensus":{"full":[{"start":224,"end":233,"type":"D"}],"Structural state":[{"start":224,"end":233,"type":"D"}],"Disorder function":[{"start":224,"end":233,"type":"F"}]}},{"disprot_id":"DP03634","acc":"Q92784-2","creator":"kmuwonge","date":"2022-04-22T17:24:56.456Z","features":{"pfam":[],"gene3D":[]},"length":357,"name":"Isoform 2 of Zinc finger protein DPF3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":60,"end":200,"reference_id":"35863661","reference_source":"pmid","reference_html":"Structural characterisation of amyloidogenic intrinsically disordered zinc finger protein isoforms DPF3b and DPF3a. <i> Mignon J, Mottet D, Leyder T, Uversky VN, Perpète EA, Michaux C. </i> Int J Biol Macromol, 2022","date":"2024-04-04T16:42:17.755Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP03634r004","statement":[{"text":"Predictions, spectroscopy, and dynamic light scattering have revealed a high content in disorder: prevalence of random coil, aromatic residues partially to fully exposed to the solvent, and large hydrodynamic diameters.","type":"Abstract"},{"text":"From the N-terminus, the disorder profile includes the 2/3 domain (and beyond), which is considered mostly ordered (residues 1 to 90), although disorder scores varying between 0.2 and 0.5 indicate some chain flexibility, especially from residues 60 to 90. This is followed by a 110-residue-long IDR (IDR-1) up to the C2H2 zinc finger (ZnF), where the disorder score drops below the 0.5 threshold (residues 199 to 220), though retaining some flexibility.","type":"Results"},{"text":"Predictions and experimental evidence have been consistent with both isoforms being highly disordered proteins. CD spectroscopy has revealed similar footprints dominated by random coil, and measured hydrodynamic diameters by DLS indicate that they adopt expanded conformations. DPF3a has also exhibited more intrinsic disorder than DPF3b, as highlighted by structural predictors, UV–visible absorption spectroscopy, and the presence of additional IDR and MoRFs in its C-terminal domain.","type":"Conclusion"},{"text":"The boundaries of this disordered region were determined by the combination of the structural predictors used in the publication (PONDR and IUPred), AlphaFold and Mobi DB.","type":"Curator statement"}]},{"start":222,"end":259,"reference_id":"35863661","reference_source":"pmid","reference_html":"Structural characterisation of amyloidogenic intrinsically disordered zinc finger protein isoforms DPF3b and DPF3a. <i> Mignon J, Mottet D, Leyder T, Uversky VN, Perpète EA, Michaux C. </i> Int J Biol Macromol, 2022","date":"2024-04-04T16:44:53.332Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP03634r005","statement":[{"text":"Predictions, spectroscopy, and dynamic light scattering have revealed a high content in disorder: prevalence of random coil, aromatic residues partially to fully exposed to the solvent, and large hydrodynamic diameters.","type":"Abstract"},{"text":"A second shorter 40-residue-long IDR (IDR-2) is found between the C2H2 and PHD1 ZnFs (residues 221–260), followed by a gain in order at the level of the PHD1 finger (residues 261–292).","type":"Results"},{"text":"Predictions and experimental evidence have been consistent with both isoforms being highly disordered proteins. CD spectroscopy has revealed similar footprints dominated by random coil, and measured hydrodynamic diameters by DLS indicate that they adopt expanded conformations. DPF3a has also exhibited more intrinsic disorder than DPF3b, as highlighted by structural predictors, UV–visible absorption spectroscopy, and the presence of additional IDR and MoRFs in its C-terminal domain.","type":"Discussion"},{"text":"The boundaries of this disordered region were determined by the combination of the structural predictors used in the publication (PONDR and IUPred), AlphaFold and Mobi DB.","type":"Curator statement"}]},{"start":293,"end":357,"reference_id":"35863661","reference_source":"pmid","reference_html":"Structural characterisation of amyloidogenic intrinsically disordered zinc finger protein isoforms DPF3b and DPF3a. <i> Mignon J, Mottet D, Leyder T, Uversky VN, Perpète EA, Michaux C. </i> Int J Biol Macromol, 2022","date":"2024-04-04T16:45:58.145Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP03634r006","statement":[{"text":"Predictions, spectroscopy, and dynamic light scattering have revealed a high content in disorder: prevalence of random coil, aromatic residues partially to fully exposed to the solvent, and large hydrodynamic diameters.","type":"Abstract"},{"text":"Towards the C-terminus, where isoforms sequence composition differs, DPF3b remains fully ordered due to the PHD2 ZnF (residues 293–378, Fig. 1B), whilst DPF3a shows a third 60-residue-long IDR (IDR-3) with high disorder scores (residues 293–357, Fig. 2).","type":"Results"},{"text":"Predictions and experimental evidence have been consistent with both isoforms being highly disordered proteins. CD spectroscopy has revealed similar footprints dominated by random coil, and measured hydrodynamic diameters by DLS indicate that they adopt expanded conformations. DPF3a has also exhibited more intrinsic disorder than DPF3b, as highlighted by structural predictors, UV–visible absorption spectroscopy, and the presence of additional IDR and MoRFs in its C-terminal domain.","type":"Discussion"},{"text":"The boundaries of this disordered region were determined by the combination of the structural predictors used in the publication (PONDR and IUPred), AlphaFold and Mobi DB.","type":"Curator statement"}]}],"regions_counter":6,"released":"2023_12","sequence":"MATVIHNPLKALGDQFYKEAIEHCRSYNSRLCAERSVRLPFLDSQTGVAQNNCYIWMEKRHRGPGLAPGQLYTYPARCWRKKRRLHPPEDPKLRLLEIKPEVELPLKKDGFTSESTTLEALLRGEGVEKKVDAREEESIQEIQRVLENDENVEEGNEEEDLEEDIPKRKNRTRGRARGSAGGRRRHDAASQEDHDKPYVCDICGKRYKNRPGLSYHYAHTHLASEEGDEAQDQETRSPPNHRNENHRPQKGPDGTVIPNNYCDFCLGGSNMNKKSGRPEELVSCADCGRSAHLGGEGRKEKEAAAAARTTEDLFGSTSESDTSTFHGFDEDDLEEPRSCRGRRSGRGSPTADKKGSC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"DPF3"},"synonyms":[{"value":"BAF45C"},{"value":"CERD4"}]}],"disorder_content":0.6834733893557423,"disprot_consensus":{"full":[{"start":60,"end":200,"type":"D"},{"start":222,"end":259,"type":"D"},{"start":293,"end":357,"type":"D"}],"Structural state":[{"start":60,"end":200,"type":"D"},{"start":222,"end":259,"type":"D"},{"start":293,"end":357,"type":"D"}]}},{"disprot_id":"DP03635","acc":"P81605","creator":"cpintado","date":"2022-04-25T10:50:02.306Z","features":{"pfam":[{"id":"PF15291","name":"Dermcidin, antibiotic peptide","start":21,"end":98}],"gene3D":[]},"length":110,"name":"Dermcidin","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":77,"end":87,"reference_id":"28888369","reference_source":"pmid","reference_html":"Structure analysis of the membrane-bound dermcidin-derived peptide SSL-25 from human sweat. <i> Mühlhäuser P, Wadhwani P, Strandberg E, Bürck J, Ulrich AS. </i> Biochim Biophys Acta Biomembr, 2017","date":"2022-07-04T11:16:53.370Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2KSG"}],"region_id":"DP03635r001","statement":[{"text":"The α-helical structure of the N-terminal part of the peptide was preserved in membranes of different lipid compositions and at various peptide-to-lipid molar ratios, but the C-terminus was disordered and did not fold into a well-defined α-helical conformation.","type":"Abstract"}],"sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"60723","entry_name":"ditetradecanoyl phosphatidylglycerol"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"241349","entry_name":"dimyristoyl phosphatidylcholine"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-04T13:12:15.572Z"}},{"start":63,"end":87,"reference_id":"28888369","reference_source":"pmid","reference_html":"Structure analysis of the membrane-bound dermcidin-derived peptide SSL-25 from human sweat. <i> Mühlhäuser P, Wadhwani P, Strandberg E, Bürck J, Ulrich AS. </i> Biochim Biophys Acta Biomembr, 2017","date":"2022-07-04T13:28:06.791Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP03635r002","statement":[{"text":"In 10 mM phosphate buffer (PB), a line shape typical of disordered peptides was found with negative ellipticities over the full spectral range from 185 to 260 nm and a pronounced negative CD band at approximately 198 nm.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-05T12:56:43.564Z"}},{"start":63,"end":87,"reference_id":"28888369","reference_source":"pmid","reference_html":"Structure analysis of the membrane-bound dermcidin-derived peptide SSL-25 from human sweat. <i> Mühlhäuser P, Wadhwani P, Strandberg E, Bürck J, Ulrich AS. </i> Biochim Biophys Acta Biomembr, 2017","date":"2022-04-26T15:03:38.041Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"EXP","region_id":"DP03635r003","statement":[{"text":"Structure analysis of the membrane-bound dermcidin-derived peptide SSL-25 from human sweat.","type":"Title"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-01T15:04:00.768Z"}},{"start":63,"end":87,"reference_id":"28888369","reference_source":"pmid","reference_html":"Structure analysis of the membrane-bound dermcidin-derived peptide SSL-25 from human sweat. <i> Mühlhäuser P, Wadhwani P, Strandberg E, Bürck J, Ulrich AS. </i> Biochim Biophys Acta Biomembr, 2017","date":"2022-07-04T13:28:26.974Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP03635r004","statement":[{"text":"Like many AMPs, SSL-25 is unstructured in solution but folds into an amphipathic α-helix after binding to a membrane, as shown here by CD analysis (Fig. 2A).","type":"Discussion"}],"sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"241349","entry_name":"dimyristoyl phosphatidylcholine"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"60723","entry_name":"ditetradecanoyl phosphatidylglycerol"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-05T12:57:04.395Z"}},{"start":63,"end":110,"reference_id":"22262861","reference_source":"pmid","reference_html":"Structure-activity analysis of the dermcidin-derived peptide DCD-1L, an anionic antimicrobial peptide present in human sweat. <i> Paulmann M, Arnold T, Linke D, Özdirekcan S, Kopp A, Gutsmann T, Kalbacher H, Wanke I, Schuenemann VJ, Habeck M, Bürck J, Ulrich AS, Schittek B. </i> J Biol Chem, 2012","date":"2022-07-04T12:26:38.735Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006200","ec_ontology":"ECO","ec_name":"circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP03635r005","statement":[{"text":"A, anionic DCD-1L is unstructured in aqueous solution according to CD and NMR. B, upon binding to a bacterial membrane the peptide folds into an amphiphilic α-helix, which is aligned parallel to the membrane surface according to OCD.","type":"Figure"}],"sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"183654","entry_name":"1,2-diphytanoyl-sn-glycero-3-phosphocholine"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"34080","entry_name":"1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"60286","entry_name":"1-palmitoyl-2-oleoyl phosphatidylethanolamine"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"43769 ","entry_name":"dodecyl beta-D-maltoside"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"131762","entry_name":"dodecyldimethylamine N-oxide"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-04T13:13:56.569Z"}},{"start":63,"end":110,"reference_id":"22262861","reference_source":"pmid","reference_html":"Structure-activity analysis of the dermcidin-derived peptide DCD-1L, an anionic antimicrobial peptide present in human sweat. <i> Paulmann M, Arnold T, Linke D, Özdirekcan S, Kopp A, Gutsmann T, Kalbacher H, Wanke I, Schuenemann VJ, Habeck M, Bürck J, Ulrich AS, Schittek B. </i> J Biol Chem, 2012","date":"2022-07-04T13:22:28.885Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006200","ec_ontology":"ECO","ec_name":"circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"EXP","region_id":"DP03635r006","statement":[{"text":"A, anionic DCD-1L is unstructured in aqueous solution according to CD and NMR. B, upon binding to a bacterial membrane the peptide folds into an amphiphilic α-helix, which is aligned parallel to the membrane surface according to OCD.\nand NMR. Upon binding to a bacterial membrane the peptide folds into an amphiphilic alpha-helix.","type":"Figure"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-04T13:27:15.955Z"}},{"start":63,"end":110,"reference_id":"22262861","reference_source":"pmid","reference_html":"Structure-activity analysis of the dermcidin-derived peptide DCD-1L, an anionic antimicrobial peptide present in human sweat. <i> Paulmann M, Arnold T, Linke D, Özdirekcan S, Kopp A, Gutsmann T, Kalbacher H, Wanke I, Schuenemann VJ, Habeck M, Bürck J, Ulrich AS, Schittek B. </i> J Biol Chem, 2012","date":"2022-07-04T12:30:34.939Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006200","ec_ontology":"ECO","ec_name":"circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP03635r007","statement":[{"text":"B, CD measurements of DCD-1L in water show an unstructured conformation, which changes into an α-helix in the detergents LDAO or DDM.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-04T13:14:24.194Z"}},{"start":63,"end":110,"reference_id":"22262861","reference_source":"pmid","reference_html":"Structure-activity analysis of the dermcidin-derived peptide DCD-1L, an anionic antimicrobial peptide present in human sweat. <i> Paulmann M, Arnold T, Linke D, Özdirekcan S, Kopp A, Gutsmann T, Kalbacher H, Wanke I, Schuenemann VJ, Habeck M, Bürck J, Ulrich AS, Schittek B. </i> J Biol Chem, 2012","date":"2022-07-05T08:29:19.316Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"GO:0042742","term_name":"defense response to bacterium","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001165","ec_ontology":"ECO","ec_name":"colony counting evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IDA","region_id":"DP03635r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"}],"statement":[{"text":"We noticed that addition of divalent (Zn2+, Ca2+, Mg2+) and monovalent (Na+) ions enhances the antimicrobial activity of DCD-1L against S. aureus 113 significantly (Fig. 2C).","type":"Results"}],"term_comment":"","term_def":"\"Reactions triggered in response to the presence of a bacterium that act to protect the cell or organism.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-05T12:57:54.846Z"}},{"start":63,"end":110,"reference_id":"22262861","reference_source":"pmid","reference_html":"Structure-activity analysis of the dermcidin-derived peptide DCD-1L, an anionic antimicrobial peptide present in human sweat. <i> Paulmann M, Arnold T, Linke D, Özdirekcan S, Kopp A, Gutsmann T, Kalbacher H, Wanke I, Schuenemann VJ, Habeck M, Bürck J, Ulrich AS, Schittek B. </i> J Biol Chem, 2012","date":"2022-07-05T08:44:01.349Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"GO:0005216","term_name":"ion channel activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007178","ec_ontology":"ECO","ec_name":"reconstituted bilayer single-channel patch recording evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IDA","region_id":"DP03635r009","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"183654","entry_name":"1,2-diphytanoyl-sn-glycero-3-phosphocholine"}],"statement":[{"text":"The results clearly show that DCD-1L is very potent in ion channel formation after an initial reconstitution, which takes several minutes. An example for a recording at 50 mV is illustrated in Fig. 4A, showing the initial reconstitution of a peptide channel in the black lipid bilayer. Once inserted into the membrane, the current increases stepwise until the membrane finally breaks. The insertion of the first channel appears to trigger subsequent insertions and suggests a self-enhancing, cooperative mechanism of pore formation.","type":"Results"},{"text":"Due to the comparable conductance in either LiCl or potassium acetate, we conclude that the DCD-1L channel is neither anion- nor cation-selective.","type":"Results"}],"term_comment":"","term_def":"\"Enables the facilitated diffusion of an ion (by an energy-independent process) by passage through a transmembrane aqueous pore or channel without evidence for a carrier-mediated mechanism. May be either selective (it enables passage of a specific ion only) or non-selective (it enables passage of two or more ions of same charge but different size).\" [GOC:cy, GOC:mtg_transport, GOC:pr, ISBN:0815340729]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-05T12:57:31.169Z"}}],"regions_counter":9,"released":"2023_06","sequence":"MRFMTLLFLTALAGALVCAYDPEAASAPGSGNPCHEASAAQKENAGEDPGLARQAPKPRKQRSSLLEKGLDGAKKAVGGLGKLGKDAVEDLESVGKGAVHDVKDVLDSVL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Extracellular matrix proteins"],"genes":[{"name":{"value":"DCD","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:14669","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:14669"}}]},"synonyms":[{"value":"AIDD"},{"value":"DSEP","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9736629","url":"http://www.ncbi.nlm.nih.gov/pubmed/9736629","alternativeUrl":"https://europepmc.org/abstract/MED/9736629"}}]}]}],"alphafold_very_low_content":0.23636363636363636,"disorder_content":0.43636363636363634,"disprot_consensus":{"full":[{"start":63,"end":110,"type":"T"}],"Structural state":[{"start":63,"end":110,"type":"D"}],"Molecular function":[{"start":63,"end":110,"type":"F"}],"Structural transition":[{"start":63,"end":110,"type":"T"}],"Biological process":[{"start":63,"end":110,"type":"F"}]}},{"disprot_id":"DP03637","acc":"Q8NC51","creator":"rpancsa","date":"2022-04-25T14:38:07.333Z","features":{"pfam":[{"id":"PF04774","name":"Hyaluronan / mRNA binding family","start":189,"end":313},{"id":"PF16174","name":"Intracellular hyaluronan-binding protein 4 N-terminal","start":5,"end":151}],"gene3D":[]},"length":408,"name":"Plasminogen activator inhibitor 1 RNA-binding protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":149,"end":288,"reference_id":"34631798","reference_source":"pmid","reference_html":"Structural Characterization of the RNA-Binding Protein SERBP1 Reveals Intrinsic Disorder and Atypical RNA Binding Modes. <i> Baudin A, Moreno-Romero AK, Xu X, Selig EE, Penalva LOF, Libich DS. </i> Front Mol Biosci, 2021","date":"2022-07-08T09:41:45.741Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03637r001","statement":[{"text":"Analysis of the Cα, Cβ, C’, HN, N, and Hα chemical shifts using the Secondary Structure Propensity (SSP) algorithm (Marsh et al., 2006) indicate that the majority of SERBP1 189–400 is disordered, except for residues 289–299, which have significant α-helical character (Figure 2A). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T12:51:44.429Z"}},{"start":300,"end":400,"reference_id":"34631798","reference_source":"pmid","reference_html":"Structural Characterization of the RNA-Binding Protein SERBP1 Reveals Intrinsic Disorder and Atypical RNA Binding Modes. <i> Baudin A, Moreno-Romero AK, Xu X, Selig EE, Penalva LOF, Libich DS. </i> Front Mol Biosci, 2021","date":"2022-07-08T09:43:20.905Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03637r002","statement":[{"text":"Analysis of the Cα, Cβ, C’, HN, N, and Hα chemical shifts using the Secondary Structure Propensity (SSP) algorithm (Marsh et al., 2006) indicate that the majority of SERBP1 189–400 is disordered, except for residues 289–299, which have significant α-helical character (Figure 2A).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T12:51:43.246Z"}},{"start":387,"end":400,"reference_id":"34631798","reference_source":"pmid","reference_html":"Structural Characterization of the RNA-Binding Protein SERBP1 Reveals Intrinsic Disorder and Atypical RNA Binding Modes. <i> Baudin A, Moreno-Romero AK, Xu X, Selig EE, Penalva LOF, Libich DS. </i> Front Mol Biosci, 2021","date":"2022-07-08T09:45:05.890Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","region_id":"DP03637r003","statement":[{"text":"Plotting the maximal CSP (Δδmax) against the protein sequence reveals that the RNA interacts with residues spanning from the second RGG box to the C-terminus of SERBP1, with some Δδmax higher than 0.1 ppm (e.g., N383, T388, S394) (Figure 5B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T12:52:15.339Z"}},{"start":149,"end":188,"reference_id":"34631798","reference_source":"pmid","reference_html":"Structural Characterization of the RNA-Binding Protein SERBP1 Reveals Intrinsic Disorder and Atypical RNA Binding Modes. <i> Baudin A, Moreno-Romero AK, Xu X, Selig EE, Penalva LOF, Libich DS. </i> Front Mol Biosci, 2021","date":"2022-07-08T09:49:14.927Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"GO:0043228","term_name":"non-membrane-bounded organelle","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006067","ec_ontology":"ECO","ec_name":"fluorescence recovery after photobleaching evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP03637r004","statement":[{"text":"At neutral pH, SERBP1 149–400 readily phase separates at a concentration of 10 µM in absence of NaCl.","type":"Results"},{"text":"Conversely, SERBP1 189–400 does not phase separate at all under the same physiochemical conditions (Supplementary Figure S8B).","type":"Results"}],"term_comment":"","term_def":"\"Organized structure of distinctive morphology and function, not bounded by a lipid bilayer membrane. Includes ribosomes, the cytoskeleton and chromosomes.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T12:53:02.112Z"}}],"regions_counter":5,"released":"2023_12","sequence":"MPGHLQEGFGCVVTNRFDQLFDDESDPFEVLKAAENKKKEAGGGGVGGPGAKSAAQAAAQTNSNAAGKQLRKESQKDRKNPLPPSVGVVDKKEETQPPVALKKEGIRRVGRRPDQQLQGEGKIIDRRPERRPPRERRFEKPLEEKGEGGEFSVDRPIIDRPIRGRGGLGRGRGGRGRGMGRGDGFDSRGKREFDRHSGSDRSSFSHYSGLKHEDKRGGSGSHNWGTVKDELTESPKYIQKQISYNYSDLDQSNVTEETPEGEEHHPVADTENKENEVEEVKEEGPKEMTLDEWKAIQNKDRAKVEFNIRKPNEGADGQWKKGFVLHKSKSEEAHAEDSVMDHHFRKPANDITSQLEINFGDLGRPGRGGRGGRGGRGRGGRPNRGSRTDKSSASAPDVDDPEAFPALA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Condensates-related proteins","RNA-binding proteins"],"genes":[{"name":{"value":"SERBP1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:17860","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:17860"}}]},"synonyms":[{"value":"PAIRBP1"}],"orfNames":[{"value":"CGI-55","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"28695742","url":"http://www.ncbi.nlm.nih.gov/pubmed/28695742","alternativeUrl":"https://europepmc.org/abstract/MED/28695742"}}]}]}],"alphafold_very_low_content":0.4485294117647059,"disorder_content":0.5906862745098039,"disprot_consensus":{"full":[{"start":149,"end":288,"type":"D"},{"start":300,"end":400,"type":"D"}],"Structural state":[{"start":149,"end":288,"type":"D"},{"start":300,"end":400,"type":"D"}],"Molecular function":[{"start":387,"end":400,"type":"F"}],"Cellular component":[{"start":149,"end":188,"type":"F"}]}},{"disprot_id":"DP03639","acc":"P03101","creator":"cpintado","date":"2022-04-27T13:57:05.086Z","features":{"pfam":[{"id":"PF00500","name":"L1 (late) protein","start":4,"end":502}],"gene3D":[]},"length":505,"name":"Major capsid protein L1","ncbi_taxon_id":333760,"organism":"Human papillomavirus type 16","regions":[{"start":486,"end":505,"reference_id":"33568731","reference_source":"pmid","reference_html":"High resolution cryo EM analysis of HPV16 identifies minor structural protein L2 and describes capsid flexibility. <i> Goetschius DJ, Hartmann SR, Subramanian S, Bator CM, Christensen ND, Hafenstein SL. </i> Sci Rep, 2021","date":"2022-07-08T09:57:17.277Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7KZF"}],"region_id":"DP03639r001","statement":[{"text":"Flexibility analysis suggested that variation in capsid diameter is due to variable contraction or expansion of the flexible C-terminal arms linking the capsomers, which in turn move as rigid bodies.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T12:56:46.052Z"}},{"start":486,"end":505,"reference_id":"33568731","reference_source":"pmid","reference_html":"High resolution cryo EM analysis of HPV16 identifies minor structural protein L2 and describes capsid flexibility. <i> Goetschius DJ, Hartmann SR, Subramanian S, Bator CM, Christensen ND, Hafenstein SL. </i> Sci Rep, 2021","date":"2022-07-08T10:01:57.510Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7KZF"}],"region_id":"DP03639r003","statement":[{"text":"Flexibility analysis suggested that variation in capsid diameter is due to variable contraction or expansion of the flexible C-terminal arms linking the capsomers, which in turn move as rigid bodies.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T12:56:56.181Z"}}],"regions_counter":3,"released":"2023_06","sequence":"MSLWLPSEATVYLPPVPVSKVVSTDEYVARTNIYYHAGTSRLLAVGHPYFPIKKPNNNKILVPKVSGLQYRVFRIHLPDPNKFGFPDTSFYNPDTQRLVWACVGVEVGRGQPLGVGISGHPLLNKLDDTENASAYAANAGVDNRECISMDYKQTQLCLIGCKPPIGEHWGKGSPCTNVAVNPGDCPPLELINTVIQDGDMVDTGFGAMDFTTLQANKSEVPLDICTSICKYPDYIKMVSEPYGDSLFFYLRREQMFVRHLFNRAGAVGENVPDDLYIKGSGSTANLASSNYFPTPSGSMVTSDAQIFNKPYWLQRAQGHNNGICWGNQLFVTVVDTTRSTNMSLCAAISTSETTYKNTNFKEYLRHGEEYDLQFIFQLCKITLTADVMTYIHSMNSTILEDWNFGLQPPPGGTLEDTYRFVTSQAIACQKHTPPAPKEDPLKKYTFWEVNLKEKFSADLDQFPLGRKFLLQAGLKAKPKFTLGKRKATPTTSSTSTTAKRKKRKL","taxonomy":["Viruses","Monodnaviria","Shotokuvirae","Cossaviricota","Papovaviricetes","Zurhausenvirales","Papillomaviridae","Firstpapillomavirinae","Alphapapillomavirus"],"dataset":["Viral proteins"],"genes":[{"name":{"value":"L1","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_04002","url":"https://hamap.expasy.org/unirule/MF_04002"}}]}}],"disorder_content":0.039603960396039604,"disprot_consensus":{"full":[{"start":486,"end":505,"type":"D"}],"Structural state":[{"start":486,"end":505,"type":"D"}],"Disorder function":[{"start":486,"end":505,"type":"F"}]}},{"disprot_id":"DP03641","acc":"Q9AXT8","creator":"cpintado","date":"2022-04-28T16:02:40.720Z","features":{"pfam":[{"id":"PF00145","name":"C-5 cytosine-specific DNA methylase","start":498,"end":863},{"id":"PF00385","name":"Chromo (CHRromatin Organisation MOdifier) domain","start":441,"end":494},{"id":"PF01426","name":"BAH domain","start":186,"end":307}],"gene3D":[]},"length":912,"name":"DNA (cytosine-5)-methyltransferase 1","ncbi_taxon_id":4577,"organism":"Zea mays","regions":[{"start":310,"end":337,"reference_id":"23021223","reference_source":"pmid","reference_html":"Dual binding of chromomethylase domains to H3K9me2-containing nucleosomes directs DNA methylation in plants. <i> Du J, Zhong X, Bernatavichute YV, Stroud H, Feng S, Caro E, Vashisht AA, Terragni J, Chin HG, Tu A, Hetzel J, Wohlschlegel JA, Pradhan S, Patel DJ, Jacobsen SE. </i> Cell, 2012","date":"2022-07-18T09:25:27.140Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4FT2"}],"region_id":"DP03641r001","statement":[{"text":"Some disordered regions were not built in the final model and are shown as dashed lines.","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P68431"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-18T12:37:00.241Z"}},{"start":417,"end":441,"reference_id":"23021223","reference_source":"pmid","reference_html":"Dual binding of chromomethylase domains to H3K9me2-containing nucleosomes directs DNA methylation in plants. <i> Du J, Zhong X, Bernatavichute YV, Stroud H, Feng S, Caro E, Vashisht AA, Terragni J, Chin HG, Tu A, Hetzel J, Wohlschlegel JA, Pradhan S, Patel DJ, Jacobsen SE. </i> Cell, 2012","date":"2022-07-18T09:25:13.824Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4FT2"}],"region_id":"DP03641r002","statement":[{"text":"Some disordered regions were not built in the final model and are shown as dashed lines.","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P68431"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-18T12:36:59.357Z"}},{"start":519,"end":533,"reference_id":"23021223","reference_source":"pmid","reference_html":"Dual binding of chromomethylase domains to H3K9me2-containing nucleosomes directs DNA methylation in plants. <i> Du J, Zhong X, Bernatavichute YV, Stroud H, Feng S, Caro E, Vashisht AA, Terragni J, Chin HG, Tu A, Hetzel J, Wohlschlegel JA, Pradhan S, Patel DJ, Jacobsen SE. </i> Cell, 2012","date":"2022-07-18T09:24:57.375Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4FT2"}],"region_id":"DP03641r003","statement":[{"text":"Some disordered regions were not built in the final model and are shown as dashed lines.","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P68431"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-18T12:36:58.271Z"}},{"start":887,"end":912,"reference_id":"23021223","reference_source":"pmid","reference_html":"Dual binding of chromomethylase domains to H3K9me2-containing nucleosomes directs DNA methylation in plants. <i> Du J, Zhong X, Bernatavichute YV, Stroud H, Feng S, Caro E, Vashisht AA, Terragni J, Chin HG, Tu A, Hetzel J, Wohlschlegel JA, Pradhan S, Patel DJ, Jacobsen SE. </i> Cell, 2012","date":"2022-07-18T09:40:24.878Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4FT2"}],"region_id":"DP03641r006","statement":[{"text":"Some disordered regions were not built in the final model and are shown as dashed lines.","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P68431"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-18T12:36:57.311Z"}},{"start":157,"end":169,"reference_id":"23021223","reference_source":"pmid","reference_html":"Dual binding of chromomethylase domains to H3K9me2-containing nucleosomes directs DNA methylation in plants. <i> Du J, Zhong X, Bernatavichute YV, Stroud H, Feng S, Caro E, Vashisht AA, Terragni J, Chin HG, Tu A, Hetzel J, Wohlschlegel JA, Pradhan S, Patel DJ, Jacobsen SE. </i> Cell, 2012","date":"2022-07-18T09:40:43.379Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4FT2"}],"region_id":"DP03641r007","statement":[{"text":"Some disordered regions were not built in the final model and are shown as dashed lines.","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P68431"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-18T12:36:56.704Z"}}],"regions_counter":7,"released":"2023_12","sequence":"MAPSSPSPAAPTRVSGRKRAAKAEEIHQNKEEEEEVAAASSAKRSRKAASSGKKPKSPPKQAKPGRKKKGDAEMKEPVEDDVCAEEPDEEELAMGEEEAEEQAMQEEVVAVAAGSPGKKRVGRRNAAAAAGDHEPEFIGSPVAADEARSNWPKRYGRSTAAKKPDEEEELKARCHYRSAKVDNVVYCLGDDVYVKAGENEADYIGRITEFFEGTDQCHYFTCRWFFRAEDTVINSLVSISVDGHKHDPRRVFLSEEKNDNVLDCIISKVKIVHVDPNMDPKAKAQLIESCDLYYDMSYSVAYSTFANISSENGQSGSDTASGISSDDVDLETSSSMPTRTATLLDLYSGCGGMSTGLCLGAALSGLKLETRWAVDFNSFACQSLKYNHPQTEVRNEKADEFLALLKEWAVLCKKYVQDVDSNLASSEDQADEDSPLDKDEFVVEKLVGICYGGSDRENGIYFKVQWEGYGPEEDTWEPIDNLSDCPQKIREFVQEGHKRKILPLPGDVDVICGGPPCQGISGFNRYRNRDEPLKDEKNKQMVTFMDIVAYLKPKYVLMENVVDILKFADGYLGKYALSCLVAMKYQARLGMMVAGCYGLPQFRMRVFLWGALSSMVLPKYPLPTYDVVVRGGAPNAFSQCMVAYDETQKPSLKKALLLGDAISDLPKVQNHQPNDVMEYGGSPKTEFQRYIRLSRKDMLDWSFGEGAGPDEGKLLDHQPLRLNNDDYERVQQIPVKKGANFRDLKGVRVGANNIVEWDPEIERVKLSSGKPLVPDYAMSFIKGKSLKPFGRLWWDETVPTVVTRAEPHNQVIIHPTQARVLTIRENARLQGFPDYYRLFGPIKEKYIQVGNAVAVPVARALGYCLGQAYLGESEGSDPLYQLPPSFTSVGGRTAGQARASPVGTPAGEVVEQ","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","PACMAD clade","Panicoideae","Andropogonodae","Andropogoneae","Tripsacinae","Zea"],"genes":[{"name":{"value":"MET2A"}}],"alphafold_very_low_content":0.21929824561403508,"disorder_content":0.11732456140350878,"disprot_consensus":{"full":[{"start":157,"end":169,"type":"D"},{"start":310,"end":337,"type":"D"},{"start":417,"end":441,"type":"D"},{"start":519,"end":533,"type":"D"},{"start":887,"end":912,"type":"D"}],"Structural state":[{"start":157,"end":169,"type":"D"},{"start":310,"end":337,"type":"D"},{"start":417,"end":441,"type":"D"},{"start":519,"end":533,"type":"D"},{"start":887,"end":912,"type":"D"}]}},{"disprot_id":"DP03642","acc":"B4FUM2","creator":"cpintado","date":"2022-04-29T11:22:17.890Z","features":{"pfam":[{"id":"PF00175","name":"Oxidoreductase NAD-binding domain","start":222,"end":336}],"gene3D":[]},"length":369,"name":"Ferredoxin--NADP reductase, chloroplastic","ncbi_taxon_id":4577,"organism":"Zea mays","regions":[{"start":1,"end":73,"reference_id":"22805436","reference_source":"pmid","reference_html":"N-terminal structure of maize ferredoxin:NADP+ reductase determines recruitment into different thylakoid membrane complexes. <i> Twachtmann M, Altmann B, Muraki N, Voss I, Okutani S, Kurisu G, Hase T, Hanke GT. </i> Plant Cell, 2012","date":"2022-07-08T10:05:54.597Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3VO2"}],"region_id":"DP03642r001","statement":[{"text":"In Zm-FNR2, the N-terminal was poorly resolved, presumably due to a high degree of flexibility.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T12:57:53.093Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MAAVTAAAISLSSSSASSPAAAAKAKAASPSSSPCRHLQFLSAASPRRRWRAGARAVRAQVSTTETAAAGPAKTSKKQDEGLVTNKYKPKEPYVGRCLSNTRITGDDAPGETWHMVFSTEGEIPYREGQSIGIIADGEDKNGKPHKLRLYSIASSALGDFGDSKTVSLCVKRLVYTNDQGEIVKGVCSNFLCDLKPGADVKITGPVGKEMLMPKDPNATVIMLATGTGIAPFRSFLWKMFLEEHEDYKFSGLAWLFLGVPTSDSLLYKEELEKMKEMAPDNFRLDFAVSREQTNAAGEKMYIQTRMAEYREELWELLKKDNTYVYMCGLKGMEKGIDDIMLNLAAKDGIDWMQYKKQLKKGEQWNVEVY","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","PACMAD clade","Panicoideae","Andropogonodae","Andropogoneae","Tripsacinae","Zea"],"genes":[{"name":{"value":"100282643","evidences":[{"code":"ECO:0000313","source":{"name":"EnsemblPlants","id":"Zm00001eb362640_P001","url":"http://www.ensemblgenomes.org/id/Zm00001eb362640_P001"}}]},"orfNames":[{"value":"ZEAMMB73_Zm00001d011833","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AQK98108.1","url":"https://www.ebi.ac.uk/ena/browser/view/AQK98108.1"}}]}]}],"alphafold_very_low_content":0.19241192411924118,"disorder_content":0.1978319783197832,"disprot_consensus":{"full":[{"start":1,"end":73,"type":"D"}],"Structural state":[{"start":1,"end":73,"type":"D"}]}},{"disprot_id":"DP03643","acc":"Q6L4L4","creator":"cpintado","date":"2022-05-03T13:59:09.333Z","features":{"pfam":[{"id":"PF00628","name":"PHD-finger","start":117,"end":166},{"id":"PF02037","name":"SAP domain","start":15,"end":45},{"id":"PF02891","name":"MIZ/SP-RING zinc finger","start":360,"end":408}],"gene3D":[]},"length":875,"name":"E3 SUMO-protein ligase SIZ1","ncbi_taxon_id":39947,"organism":"Oryza sativa subsp. japonica","regions":[{"start":87,"end":105,"reference_id":"18831036","reference_source":"pmid","reference_html":"Solution structures and DNA binding properties of the N-terminal SAP domains of SUMO E3 ligases from Saccharomyces cerevisiae and Oryza sativa. <i> Suzuki R, Shindo H, Tase A, Kikuchi Y, Shimizu M, Yamazaki T. </i> Proteins, 2009","date":"2022-07-08T10:11:14.750Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2RNO"},{"db":"BMRB","id":"11030 "}],"region_id":"DP03643r001","statement":[{"text":"The N-terminal 13 residues of ScSiz1 and the C-terminal 19 residues of OsSiz1 that are highly flexible are omitted to make the figures clear.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T12:59:40.553Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MADLVSSCKDKLAYFRIKELKDILNQLGLPKQGKKQDLIDRVLALLTDEQGQRHHGWGRKNSLTKEAVAKIVDDTYRKMQIQCAPDLATRSHSGSDFSFRPIEEAYDSFQPEAKVRCICSSTMVNDSMIQCEDQRCQVWQHLNCVLIPDKPGESAEVPPVFYCELCRLSRADPFWVTAGNPLLPVKFVSSGVTNDGTSVPQSVEKSFQLSRSDRETVQRQEYDLQVWCMLLNDKVQFRMQWPQYAELHVNGISVRVVTRPGSQLLGINGRDDGPLITTCSREGINKICLSRVDARTFCFGVRIAKRRTVAQVLNLVPKEAEGESFEHALARVRRCLGGGDTAENADSDSDLEVVAESVTVNLRCPNSGSRMRIAGRFKPCIHMGCFDLETFVELNQRSRKWQCPICLKNYSLESLMIDPYFNRITSLLRNCNEDVNEVDVKPDGSWRVKGDAASRELSQWHMPDGTLCNPKEDVKPAMQNGNEQMMEGTSDGQKSLKIGIKRNPNGIWEVSSKADDKKPSVVGNRMQNNSGFRALNNIMHMSNSPTSSYRDGEDPSVNQESNRHVDLSLNNGNNEFDSFSLNFGQACNTDDRPQQQHNATDVIVLSDSDEENDAMVCPPAVYDNTTTANGSGFPFTTNGIGYTERYQEDAGVGTSGLGLLSNNVDDFEMNNWQMHSSYQQPEQGFQFFGNDTDVHNTFVGSHNSFGLAPNDYSLDCNVGVEEASVTPALSVCRNSNEMHGSLVDNPLALVGDDPSLQIFLPSQPSSVPLQEELSERANAPNGVQSDDWISLTLAAGGGGNEEPAPADVNSQPQIPSTETGIEPLTDAASAFLSTNIERRSGADLNPRRIENIFSHPRQPRSVRPRLCLSIDTDSE","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","BOP clade","Oryzoideae","Oryzeae","Oryzinae","Oryza","Oryza sativa"],"genes":[{"name":{"value":"SIZ1"},"orfNames":[{"value":"OSJNBb0079L11.3"}],"olnNames":[{"value":"Os05g0125000"},{"value":"LOC_Os05g03430"}]}],"alphafold_very_low_content":0.5017142857142857,"disorder_content":0.021714285714285714,"disprot_consensus":{"full":[{"start":87,"end":105,"type":"D"}],"Structural state":[{"start":87,"end":105,"type":"D"}]}},{"disprot_id":"DP03644","acc":"D3TI84","creator":"cpintado","date":"2022-05-03T14:22:00.261Z","features":{"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":248,"end":419},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":613,"end":731},{"id":"PF11648","name":"C-terminal domain of RIG-I","start":809,"end":926},{"id":"PF16739","name":"Caspase recruitment domain","start":1,"end":92},{"id":"PF16739","name":"Caspase recruitment domain","start":99,"end":186},{"id":"PF18119","name":"RIG-I receptor C-terminal domain","start":462,"end":602}],"gene3D":[]},"length":933,"name":"RNA helicase","ncbi_taxon_id":8839,"organism":"Anas platyrhynchos","regions":[{"start":187,"end":244,"reference_id":"22000019","reference_source":"pmid","reference_html":"Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA. <i> Kowalinski E, Lunardi T, McCarthy AA, Louber J, Brunel J, Grigorov B, Gerlier D, Cusack S. </i> Cell, 2011","date":"2022-07-08T11:14:31.493Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4A2W"}],"region_id":"DP03644r001","statement":[{"text":"Although the ~55 residue linker between CARD2 and Hel1 is invisible in the electron density due to disorder, the monomeric state of free RIG-I (Figure S3) indicates that the CARDs most likely bind to the Hel2i domain of the same molecule, rather than being swapped between monomers. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T13:08:10.514Z"}},{"start":492,"end":503,"reference_id":"22000019","reference_source":"pmid","reference_html":"Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA. <i> Kowalinski E, Lunardi T, McCarthy AA, Louber J, Brunel J, Grigorov B, Gerlier D, Cusack S. </i> Cell, 2011","date":"2022-07-08T11:28:53.952Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4A2W"}],"region_id":"DP03644r002","statement":[{"text":"The PDB shows that this region lacks electron density, therefore indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T13:08:03.152Z"}},{"start":663,"end":690,"reference_id":"22000019","reference_source":"pmid","reference_html":"Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA. <i> Kowalinski E, Lunardi T, McCarthy AA, Louber J, Brunel J, Grigorov B, Gerlier D, Cusack S. </i> Cell, 2011","date":"2022-07-08T11:29:54.040Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4A2W"}],"region_id":"DP03644r003","statement":[{"text":"The PDB shows that this region lacks electron density, therefore indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T13:07:54.605Z"}},{"start":795,"end":933,"reference_id":"22000019","reference_source":"pmid","reference_html":"Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA. <i> Kowalinski E, Lunardi T, McCarthy AA, Louber J, Brunel J, Grigorov B, Gerlier D, Cusack S. </i> Cell, 2011","date":"2022-07-08T11:30:47.993Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4A2W"}],"region_id":"DP03644r004","statement":[{"text":"The PDB shows that this region lacks electron density, therefore indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T13:06:53.424Z"}},{"start":806,"end":899,"reference_id":"22000019","reference_source":"pmid","reference_html":"Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA. <i> Kowalinski E, Lunardi T, McCarthy AA, Louber J, Brunel J, Grigorov B, Gerlier D, Cusack S. </i> Cell, 2011","date":"2022-07-15T10:05:43.794Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4A2W"},{"db":"PDB","id":"4A2X"}],"region_id":"DP03644r005","statement":[{"text":" Conformational change of the dRIG-I helicase\ndomain upon ligand binding. The open state is\nin orange (1–933, chain A), and the closed state\narising from simultaneous dsRNA (red and purple\nstrands) and ADP-AlF3-Mg++ (not shown) binding\nis in black. ","type":"Figure"}],"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-15T13:46:43.354Z"}},{"start":806,"end":933,"reference_id":"22000019","reference_source":"pmid","reference_html":"Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA. <i> Kowalinski E, Lunardi T, McCarthy AA, Louber J, Brunel J, Grigorov B, Gerlier D, Cusack S. </i> Cell, 2011","date":"2022-07-15T09:59:44.227Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4A2X"}],"ec_go":"EXP","region_id":"DP03644r006","statement":[{"text":"Despite the modest resolution, the structure is well defined, with clear electron density for the ADP-AlF3-Mg++ (Figure S2B) and the RNA (Figure S2C).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-15T13:46:55.493Z"}},{"start":905,"end":933,"reference_id":"22000019","reference_source":"pmid","reference_html":"Structural basis for the activation of innate immune pattern-recognition receptor RIG-I by viral RNA. <i> Kowalinski E, Lunardi T, McCarthy AA, Louber J, Brunel J, Grigorov B, Gerlier D, Cusack S. </i> Cell, 2011","date":"2022-07-15T10:08:27.935Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4A2W"},{"db":"PDB","id":"4A2X"}],"region_id":"DP03644r007","statement":[{"text":"Conformational change of the dRIG-I helicase domain upon ligand binding. The open state is in orange (1–933, chain A), and the closed state arising from simultaneous dsRNA (red and purple strands) and ADP-AlF3-Mg++ (not shown) binding is in black. ","type":"Figure"}],"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-15T13:46:41.400Z"}}],"regions_counter":7,"released":"2023_12","sequence":"MTADEKRSLQCYRRYIERSLNPVYVLGNMTDWLPDELRERIRKEEERGVSGAAALFLDAVLQLEARGWFRGMLDAMLAAGYTGLAEAIENWDFSKLEKLELHRQLLKRIEATMLEVDPVALIPYISTCLIDRECEEIQQISENRSKAAGITKLIECLCRSDKEHWPKSLQLALDTTGYYRASELWDIREDNAKDVDSEMTDASEDCLEASMTYSEEAEPDDNLSENLGSAAEGIGKPPPVYETKKARSYQIELAQPAINGKNALICAPTGSGKTFVSILICEHHFQNMPAGRKAKVVFLATKVPVYEQQKNVFKHHFERQGYSVQGISGENFSNVSVEKVIEDSDIIVVTPQILVNSFEDGTLTSLSIFTLMIFDECHNTTGNHPYNVLMTRYLEQKFNSASQLPQILGLTASVGVGNAKNIEETIEHICSLCSYLDIQAISTVRENIQELQRFMNKPEIDVRLVKRRIHNPFAAIISNLMSETEALMRTIYSVDTLSQNSKKDFGTQNYEHWIVVTQRKCRLLQLEDKEEESRICRALFICTEHLRKYNDALIISEDARIIDALSYLTEFFTNVKNGPYTELEQHLTAKFQEKEPELIALSKDETNENPKLEELVCILDDAYRYNPQTRTLLFAKTRALVSALKKCMEENPILNYIKPGVLMGRGRRDQTTGMTLPSQKGVLDAFKTSKDNRLLIATSVADEGIDIVQCNLVVLYEYSGNVTKMIQVRGRGRAAGSKCILVTSKTEVVENEKCNRYKEEMMNKAVEKIQKWDEETFAKKIHNLQMKERVLRDSRRKEIKPKVVEGQKNLLCGKCKAYACSTDDIRIIKDSHHIVLGEAFKERYTTKPHKKPMQFDGFEKKSKMYCRNNNCQHDWGITVKYLTFDNLPVIKIKSFVMESTATGTQMDFQKWKSINSSLKNFDVEEMSNLYPPF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Anseriformes","Anatidae","Anatinae","Anas"],"genes":[{"name":{"value":"RIG-I","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AFK82315.1","url":"https://www.ebi.ac.uk/ena/browser/view/AFK82315.1"}}]}}],"alphafold_very_low_content":0.08788853161843516,"dataset":["RNA-binding proteins"],"disorder_content":0.2540192926045016,"disprot_consensus":{"full":[{"start":187,"end":244,"type":"D"},{"start":492,"end":503,"type":"D"},{"start":663,"end":690,"type":"D"},{"start":795,"end":805,"type":"D"},{"start":806,"end":899,"type":"T"},{"start":900,"end":904,"type":"D"},{"start":905,"end":933,"type":"T"}],"Structural state":[{"start":187,"end":244,"type":"D"},{"start":492,"end":503,"type":"D"},{"start":663,"end":690,"type":"D"},{"start":795,"end":933,"type":"D"}],"Structural transition":[{"start":806,"end":899,"type":"T"},{"start":905,"end":933,"type":"T"}],"Molecular function":[{"start":806,"end":933,"type":"F"}]}},{"disprot_id":"DP03645","acc":"Q9Y4D1","creator":"viglesias","date":"2022-05-13T10:18:12.137Z","features":{"pfam":[{"id":"PF02181","name":"Formin Homology 2 Domain","start":601,"end":983},{"id":"PF06367","name":"Diaphanous FH3 Domain","start":237,"end":433},{"id":"PF06371","name":"Diaphanous GTPase-binding Domain","start":47,"end":232}],"gene3D":[]},"length":1078,"name":"Disheveled-associated activator of morphogenesis 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":654,"end":682,"reference_id":"17482208","reference_source":"pmid","reference_html":"Structure of the FH2 domain of Daam1: implications for formin regulation of actin assembly. <i> Lu J, Meng W, Poy F, Maiti S, Goode BL, Eck MJ. </i> J Mol Biol, 2007","date":"2022-05-13T10:24:20.510Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2J1D"}],"region_id":"DP03645r001","statement":[{"text":"The Daam1 FH2 domain consists of an N-terminal “lasso” segment, a flexible linker that is largely disordered in the present structure, and a rod-shaped domain formed by three sub-domains termed the “knob”, “coiled-coil”, and “post”.","type":"Introduction"},{"text":"Although the linker is disordered, we can unambiguously assign the connectivity as that required to form the head-to-tail dimer shown in Figure 1(c) because the 30 residue linker is not long enough to allow intra-subunit interaction, nor is it long enough to connect the other pairs of subunits related by crystallographic symmetry in this space group (I222). ","type":"Results"},{"text":"The relative orientation of the two hemidimers in the present structure is quite different from that previously observed in Bni1, the divergent orientation is readily accommodated by rearrangement of the disordered linker segment.","type":"Results"},{"text":"The C-terminal tail region, including the DAD domain (residues 1025–1078), and the linker segment (residues 654–682) were not observed in the electron density map and are presumed to be disordered.","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-17T14:01:47.506Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MAPRKRGGRGISFIFCCFRNNDHPEITYRLRNDSNFALQTMEPALPMPPVEELDVMFSELVDELDLTDKHREAMFALPAEKKWQIYCSKKKDQEENKGATSWPEFYIDQLNSMAARKSLLALEKEEEEERSKTIESLKTALRTKPMRFVTRFIDLDGLSCILNFLKTMDYETSESRIHTSLIGCIKALMNNSQGRAHVLAHSESINVIAQSLSTENIKTKVAVLEILGAVCLVPGGHKKVLQAMLHYQKYASERTRFQTLINDLDKSTGRYRDEVSLKTAIMSFINAVLSQGAGVESLDFRLHLRYEFLMLGIQPVIDKLREHENSTLDRHLDFFEMLRNEDELEFAKRFELVHIDTKSATQMFELTRKRLTHSEAYPHFMSILHHCLQMPYKRSGNTVQYWLLLDRIIQQIVIQNDKGQDPDSTPLENFNIKNVVRMLVNENEVKQWKEQAEKMRKEHNELQQKLEKKERECDAKTQEKEEMMQTLNKMKEKLEKETTEHKQVKQQVADLTAQLHELSRRAVCASIPGGPSPGAPGGPFPSSVPGSLLPPPPPPPLPGGMLPPPPPPLPPGGPPPPPGPPPLGAIMPPPGAPMGLALKKKSIPQPTNALKSFNWSKLPENKLEGTVWTEIDDTKVFKILDLEDLERTFSAYQRQQDFFVNSNSKQKEADAIDDTLSSKLKVKELSVIDGRRAQNCNILLSRLKLSNDEIKRAILTMDEQEDLPKDMLEQLLKFVPEKSDIDLLEEHKHELDRMAKADRFLFEMSRINHYQQRLQSLYFKKKFAERVAEVKPKVEAIRSGSEEVFRSGALKQLLEVVLAFGNYMNKGQRGNAYGFKISSLNKIADTKSSIDKNITLLHYLITIVENKYPSVLNLNEELRDIPQAAKVNMTELDKEISTLRSGLKAVETELEYQKSQPPQPGDKFVSVVSQFITVASFSFSDVEDLLAEAKDLFTKAVKHFGEEAGKIQPDEFFGIFDQFLQAVSEAKQENENMRKKKEEEERRARMEAQLKEQRERERKMRKAKENSEESGEFDDLVSALRSGEVFDKDLSKLKRNRKRITNQMTDSSRERPITKLNF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"DAAM1"},"synonyms":[{"value":"KIAA0666"}]}],"alphafold_very_low_content":0.13636363636363635,"disorder_content":0.026901669758812616,"disprot_consensus":{"full":[{"start":654,"end":682,"type":"D"}],"Structural state":[{"start":654,"end":682,"type":"D"}]}},{"disprot_id":"DP03646","acc":"Q76KU6","creator":"cpintado","date":"2022-05-13T13:07:40.437Z","features":{"pfam":[{"id":"PF00145","name":"C-5 cytosine-specific DNA methylase","start":483,"end":597}],"gene3D":[]},"length":608,"name":"DNA methyltransferase","ncbi_taxon_id":4097,"organism":"Nicotiana tabacum","regions":[{"start":567,"end":586,"reference_id":"24855943","reference_source":"pmid","reference_html":"Molecular mechanism of action of plant DRM de novo DNA methyltransferases. <i> Zhong X, Du J, Hale CJ, Gallego-Bartolome J, Feng S, Vashisht AA, Chory J, Wohlschlegel JA, Patel DJ, Jacobsen SE. </i> Cell, 2014","date":"2022-07-08T10:19:57.346Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4ONQ"}],"region_id":"DP03646r001","statement":[{"text":"The disordered catalytic loop (CL) is shown by a dashed line.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"45453","entry_name":"sinefungin"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T13:09:26.274Z"}}],"regions_counter":2,"released":"2023_12","sequence":"MDNNLSGEDNDNIDWDTEDELEIQEIQDTTFSSCMDLRTTGQHTVRCDGEASSSSVPCQSKFIQQFVVMGFPEASIAKAIEQNGEDSDLVLDALLTFKALEDSPEEQPSASPQPCINSDDSSSEYNENLLDDVYEEDSWSSDSDSCRNSAKQCYVKVESSSSSEKEQTLLFLASMGYPAEEASIAMERCGPEASVAELTDFICAAQMARAEDVYLPEDVKPKLNHILNGSGGYKKRKMYNELCKRKKAKAIFEEETIRLPKPMIGFGVPTEPLPAMVRRTLPEQAVGPPFFYYENVALAPKGVWDTISRFLYDIEPEFVDSKYFCAAARKRGYIHNLPVENRFPLFPLAPRTIHEALPLSKKWWPSWDPRTKLNCLQTAIGSAQLTNRIRKAVEDFDGEPPMRVQKFVLDQCRKWNLVWVGRNKVAPLEPDEVEMLLGFPKNHTRGGGISRTDRYKSLGNSFQVDTVAYHLSVLKDLFPGGINVLSLFSGIGGGEVALYRLGIPLNTVVSVEKSEVNRDIVRSWWEQTNQRGNLIHFNDVQQLNGDRLEQLIESFGGFDLVIGGSPCNNLAGSNRVSRDGLEGKESSLFYDYVRILDLVKSIMSRHKH","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","lamiids","Solanales","Solanaceae","Nicotianoideae","Nicotianeae","Nicotiana"],"genes":[{"name":{"value":"NtDRM1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAC67060.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAC67060.1"}}]}}],"alphafold_very_low_content":0.2993421052631579,"disorder_content":0.03289473684210526,"disprot_consensus":{"full":[{"start":567,"end":586,"type":"D"}],"Structural state":[{"start":567,"end":586,"type":"D"}]}},{"disprot_id":"DP03647","acc":"Q9M2T2","creator":"cpintado","date":"2022-05-13T13:36:00.388Z","features":{"pfam":[{"id":"PF00168","name":"C2 domain","start":4,"end":105}],"gene3D":[]},"length":156,"name":"16 kDa phloem protein 1","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":10,"end":55,"reference_id":"29320165","reference_source":"pmid","reference_html":"Solution NMR Structure and Backbone Dynamics of Partially Disordered Arabidopsis thaliana Phloem Protein 16-1, a Putative mRNA Transporter. <i> Sashi P, Singarapu KK, Bhuyan AK. </i> Biochemistry, 2018","date":"2022-05-13T13:46:20.618Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5YQ3"}],"region_id":"DP03647r001","statement":[{"text":"In the solution structure of the protein, secondary structural elements are formed by residues 3–9 (β1), 56–62 (β2), 133–135 (β3), and 96–110 (α-helix). Most of the rest of the chain segments are disordered.","type":"Abstract"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-07T15:53:34.400Z"}},{"start":63,"end":95,"reference_id":"29320165","reference_source":"pmid","reference_html":"Solution NMR Structure and Backbone Dynamics of Partially Disordered Arabidopsis thaliana Phloem Protein 16-1, a Putative mRNA Transporter. <i> Sashi P, Singarapu KK, Bhuyan AK. </i> Biochemistry, 2018","date":"2022-05-13T13:47:38.062Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5YQ3"}],"region_id":"DP03647r002","statement":[{"text":"In the solution structure of the protein, secondary structural elements are formed by residues 3–9 (β1), 56–62 (β2), 133–135 (β3), and 96–110 (α-helix). Most of the rest of the chain segments are disordered.","type":"Abstract"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-07T15:53:36.535Z"}},{"start":111,"end":156,"reference_id":"29320165","reference_source":"pmid","reference_html":"Solution NMR Structure and Backbone Dynamics of Partially Disordered Arabidopsis thaliana Phloem Protein 16-1, a Putative mRNA Transporter. <i> Sashi P, Singarapu KK, Bhuyan AK. </i> Biochemistry, 2018","date":"2022-07-08T10:24:00.628Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5YQ3"}],"region_id":"DP03647r003","statement":[{"text":"In the solution structure of the protein, secondary structural elements are formed by residues 3–9 (β1), 56–62 (β2), 133–135 (β3), and 96–110 (α-helix). Most of the rest of the chain segments are disordered.","type":"Abstract"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T13:11:00.453Z"}}],"regions_counter":4,"released":"2023_12","sequence":"MAVGILEVSLISGKGLKRSDFLGKIDPYVEIQYKGQTRKSSVAKEDGGRNPTWNDKLKWRAEFPGSGADYKLIVKVMDHDTFSSDDFIGEATVHVKELLEMGVEKGTAELRPTKYNIVDSDLSFVGELLIGVSYSLLQDRGMDGEQFGGWKHSQVD","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"genes":[{"name":{"value":"PP16-1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"29320165","url":"http://www.ncbi.nlm.nih.gov/pubmed/29320165","alternativeUrl":"https://europepmc.org/abstract/MED/29320165"}}]},"synonyms":[{"value":"FIERG2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15282545","url":"http://www.ncbi.nlm.nih.gov/pubmed/15282545","alternativeUrl":"https://europepmc.org/abstract/MED/15282545"}}]}],"orfNames":[{"value":"T22E16.130","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"CAB75905.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAB75905.1"}}]}],"olnNames":[{"value":"At3g55470","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT3G55470","url":""}}]}]}],"alphafold_very_low_content":0.09615384615384616,"dataset":["RNA-binding proteins"],"disorder_content":0.8012820512820513,"disprot_consensus":{"full":[{"start":10,"end":55,"type":"D"},{"start":63,"end":95,"type":"D"},{"start":111,"end":156,"type":"D"}],"Structural state":[{"start":10,"end":55,"type":"D"},{"start":63,"end":95,"type":"D"},{"start":111,"end":156,"type":"D"}]}},{"disprot_id":"DP03648","acc":"Q9SL42","creator":"cpintado","date":"2022-05-13T14:04:34.277Z","features":{"pfam":[{"id":"PF00639","name":"PPIC-type PPIASE domain","start":11,"end":118}],"gene3D":[]},"length":119,"name":"Peptidyl-prolyl cis-trans isomerase Pin1","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":20,"end":37,"reference_id":"12079389","reference_source":"pmid","reference_html":"Solution structure of the single-domain prolyl cis/trans isomerase PIN1At from Arabidopsis thaliana. <i> Landrieu I, Wieruszeski JM, Wintjens R, Inzé D, Lippens G. </i> J Mol Biol, 2002","date":"2022-07-08T10:25:57.515Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1J6Y"},{"db":"BMRB","id":"4670"}],"region_id":"DP03648r001","statement":[{"text":"The coordinates of residues in disordered regions 1–6 and 20–37 were not considered.","type":"Table"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T13:24:29.208Z"}},{"start":20,"end":37,"reference_id":"12079389","reference_source":"pmid","reference_html":"Solution structure of the single-domain prolyl cis/trans isomerase PIN1At from Arabidopsis thaliana. <i> Landrieu I, Wieruszeski JM, Wintjens R, Inzé D, Lippens G. </i> J Mol Biol, 2002","date":"2022-07-08T10:28:51.364Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"BMRB","id":"4670"},{"db":"PDB","id":"1J6Y"}],"region_id":"DP03648r003","statement":[{"text":"The PIN1At fold could be superimposed on that of the catalytic domain of hPIN1 and had a 19 residue flexible loop located between strand β1 and helix α1.","type":"Abstract"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T13:24:23.449Z"}}],"regions_counter":3,"released":"2023_12","sequence":"MASRDQVKASHILIKHQGSRRKASWKDPEGKIILTTTREAAVEQLKSIREDIVSGKANFEEVATRVSDCSSAKRGGDLGSFGRGQMQKPFEEATYALKVGDISDIVDTDSGVHIIKRTA","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"genes":[{"name":{"value":"PIN1"},"orfNames":[{"value":"T27K22.9"}],"olnNames":[{"value":"At2g18040"}]}],"alphafold_very_low_content":0.01680672268907563,"disorder_content":0.15126050420168066,"disprot_consensus":{"full":[{"start":20,"end":37,"type":"D"}],"Structural state":[{"start":20,"end":37,"type":"D"}],"Disorder function":[{"start":20,"end":37,"type":"F"}]}},{"disprot_id":"DP03649","acc":"Q9UQ80","creator":"vacs","date":"2022-05-16T11:49:28.967Z","features":{"pfam":[{"id":"PF00557","name":"Metallopeptidase family M24","start":23,"end":197}],"gene3D":[]},"length":394,"name":"Proliferation-associated protein 2G4","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":363,"end":394,"reference_id":"17765895","reference_source":"pmid","reference_html":"The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as binding platform for multiple interactions. <i> Kowalinski E, Bange G, Bradatsch B, Hurt E, Wild K, Sinning I. </i> FEBS Lett, 2007","date":"2022-05-16T11:51:52.761Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2Q8K"}],"region_id":"DP03649r001","statement":[{"text":"In addition to the human MAP2 fold, Ebp1 contains a C-terminal elongation of 57 residues. Part of it is ordered in the crystal structure (residues 340–362) and attaches a short amphipathic α-helix (α10) to the outer face of the second half of the pita-bread fold (1, 4 ).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-17T09:56:48.803Z"}},{"start":364,"end":368,"reference_id":"11325528","reference_source":"pmid","reference_html":"Regulation of the ErbB3 binding protein Ebp1 by protein kinase C. <i> Lessor TJ, Hamburger AW. </i> Mol Cell Endocrinol, 2001","date":"2022-05-16T11:58:17.855Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03649r002","statement":[{"text":"Substitution of Ala at 366Thr resulted in a 90% decrease in phosphorylation.","type":"Results"},{"text":"Our in vitro data indicate that a peptide corresponding to amino acids 361–371 was phosphorylated in vitro, and that mutation of 366Thr, but not 363Ser, decreased phosphorylation. This finding suggests that 366Thr, present in the C-terminal end of the protein necessary for ErbB3 binding and upstream of a putative nuclear localization signal (KKKK) (Lamartine et al., 1997,) may be phosphorylated in vivo by PKC.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-17T09:56:50.273Z"}}],"regions_counter":2,"released":"2023_12","sequence":"MSGEDEQQEQTIAEDLVVTKYKMGGDIANRVLRSLVEASSSGVSVLSLCEKGDAMIMEETGKIFKKEKEMKKGIAFPTSISVNNCVCHFSPLKSDQDYILKEGDLVKIDLGVHVDGFIANVAHTFVVDVAQGTQVTGRKADVIKAAHLCAEAALRLVKPGNQNTQVTEAWNKVAHSFNCTPIEGMLSHQLKQHVIDGEKTIIQNPTDQQKKDHEKAEFEVHEVYAVDVLVSSGEGKAKDAGQRTTIYKRDPSKQYGLKMKTSRAFFSEVERRFDAMPFTLRAFEDEKKARMGVVECAKHELLQPFNVLYEKEGEFVAQFKFTVLLMPNGPMRITSGPFEPDLYKSEMEVQDAELKALLQSSASRKTQKKKKKKASKTAENATSGETLEENEAGD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"PA2G4"},"synonyms":[{"value":"EBP1"}]}],"alphafold_very_low_content":0.04568527918781726,"disorder_content":0.08121827411167512,"disprot_consensus":{"full":[{"start":363,"end":394,"type":"D"}],"Structural state":[{"start":363,"end":394,"type":"D"}],"Disorder function":[{"start":364,"end":368,"type":"F"}]}},{"disprot_id":"DP03650","acc":"Q01484","creator":"vnugnes","date":"2022-05-19T20:26:44.663Z","features":{"pfam":[{"id":"PF00023","name":"Ankyrin repeat","start":129,"end":155},{"id":"PF00023","name":"Ankyrin repeat","start":563,"end":587},{"id":"PF00023","name":"Ankyrin repeat","start":695,"end":725},{"id":"PF00531","name":"Death domain","start":3571,"end":3651},{"id":"PF00791","name":"ZU5 domain","start":970,"end":1044},{"id":"PF00791","name":"ZU5 domain","start":1049,"end":1100},{"id":"PF00791","name":"ZU5 domain","start":1161,"end":1238},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":37,"end":126},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":257,"end":323},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":394,"end":461},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":468,"end":554},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":625,"end":689},{"id":"PF13637","name":"Ankyrin repeats (many copies)","start":196,"end":253},{"id":"PF13637","name":"Ankyrin repeats (many copies)","start":336,"end":385},{"id":"PF13637","name":"Ankyrin repeats (many copies)","start":733,"end":781},{"id":"PF17809","name":"UPA domain","start":1324,"end":1453}],"gene3D":[]},"length":3957,"name":"Ankyrin-2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1113,"end":1122,"reference_id":"22411828","reference_source":"pmid","reference_html":"Structure of the ZU5-ZU5-UPA-DD tandem of ankyrin-B reveals interaction surfaces necessary for ankyrin function. <i> Wang C, Yu C, Ye F, Wei Z, Zhang M. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-05-26T12:42:11.820Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"4D8O"}],"region_id":"DP03650r001","statement":[{"text":"The final structural model contains most of residues from ankyrin-B ZZUD except for a few flexible loops (Fig. 1A).","type":"Results"},{"text":"The Ankyrin-2 fragment used in this publication was derived from the UniProtKB: A0A5F9ZHA, IDR is 100% identical.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ser1211del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"After extensive trials, we discovered that the deletion of a nine-residue fragment in a solvent-exposed loop of ZU5C (Figs. 1A and 2) enabled us to obtain high diffraction-quality crystals of ZZUD. "},{"type":"Supplementary material","text":"The ZZUD mutant used for crystallization with the nine-residue deletion\n(1211SDVMLNGFG1219) was created using the standard PCRbased mutagenesis method."}]},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Asp1212del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Val1213del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1214del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Leu1215del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Asn1216del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gly1217del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Phe1218del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gly1219del","start":null,"end":null,"position":null}],"sequence_construct":"MHHHHHHSSGLEVLFQGPEFSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNT","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T14:35:25.184Z"}},{"start":1113,"end":1122,"reference_id":"22411828","reference_source":"pmid","reference_html":"Structure of the ZU5-ZU5-UPA-DD tandem of ankyrin-B reveals interaction surfaces necessary for ankyrin function. <i> Wang C, Yu C, Ye F, Wei Z, Zhang M. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-05-23T12:55:30.098Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"4D8O"}],"region_id":"DP03650r002","statement":[{"text":"The final structural model contains most of residues from ankyrin-B ZZUD except for a few flexible loops (Fig. 1A).","type":"Results"},{"text":"The Ankyrin-2 fragment used in this publication was derived from the UniProtKB: A0A5F9ZHA, IDR is 100% identical.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T14:35:28.788Z"}},{"start":1457,"end":1476,"reference_id":"22411828","reference_source":"pmid","reference_html":"Structure of the ZU5-ZU5-UPA-DD tandem of ankyrin-B reveals interaction surfaces necessary for ankyrin function. <i> Wang C, Yu C, Ye F, Wei Z, Zhang M. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-05-26T12:48:54.586Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ser1211del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"After extensive trials, we discovered that the deletion of a nine-residue fragment in a solvent-exposed loop of ZU5C (Figs. 1A and ​2) enabled us to obtain high diffraction-quality crystals of ZZUD."},{"type":"Supplementary material","text":"The ZZUD mutant used for crystallization with the nine-residue deletion (1211SDVMLNGFG1219) was created using the standard PCRbased mutagenesis method."}]},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Asp1212del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Val1213del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1214del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Leu1215del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Asn1216del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gly1217del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Phe1218del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gly1219del","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"4D8O"}],"region_id":"DP03650r003","sequence_construct":"MHHHHHHSSGLEVLFQGPEFSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNT","statement":[{"text":"The final structural model contains most of residues from ankyrin-B ZZUD except for a few flexible loops (Fig. 1A).","type":"Results"},{"text":"The Ankyrin-2 fragment used in this publication was derived from the UniProtKB: A0A5F9ZHA, IDR is 100% identical.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T14:35:27.291Z"}},{"start":1457,"end":1476,"reference_id":"22411828","reference_source":"pmid","reference_html":"Structure of the ZU5-ZU5-UPA-DD tandem of ankyrin-B reveals interaction surfaces necessary for ankyrin function. <i> Wang C, Yu C, Ye F, Wei Z, Zhang M. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-05-26T12:49:31.012Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ser1211del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"After extensive trials, we discovered that the deletion of a nine-residue fragment in a solvent-exposed loop of ZU5C (Figs. 1A and ​2) enabled us to obtain high diffraction-quality crystals of ZZUD."},{"type":"Supplementary material","text":"The ZZUD mutant used for crystallization with the nine-residue deletion (1211SDVMLNGFG1219) was created using the standard PCRbased mutagenesis method."}]},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Asp1212del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Val1213del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1214del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Leu1215del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Asn1216del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gly1217del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Phe1218del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gly1219del","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"4D8O"}],"region_id":"DP03650r004","sequence_construct":"MHHHHHHSSGLEVLFQGPEFSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNT","statement":[{"text":"The final structural model contains most of residues from ankyrin-B ZZUD except for a few flexible loops (Fig. 1A).","type":"Results"},{"text":"The Ankyrin-2 fragment used in this publication was derived from the UniProtKB: A0A5F9ZHA, IDR is 100% identical.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T14:35:23.996Z"}},{"start":817,"end":873,"reference_id":"25383926","reference_source":"pmid","reference_html":"Structural basis of diverse membrane target recognitions by ankyrins.  <i> Wang C, Wei Z, Chen K, Ye F, Yu C, Bennett V, Zhang M. </i> Elife, 2014","date":"2022-05-20T13:55:05.019Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":31,"end":31,"position":"Specific residue","statements":[{"type":"Curator statement","text":"The residues 31, 34, 37, 173, 261, 262, 318, 375, 451, 478, 507, 557, 679, 714, 727, 780, 876, 891 of the exact sequence from the experimentwere replaced with selenomethionine."}]}],"cross_refs":[{"db":"PDB","id":"4RLV"}],"region_id":"DP03650r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"sequence_construct":"GPGSEFCADQYWNEVAVIDAIPLAATEHDTMLEMSDMQVWSAGLTPSLVTAEDSGSLVPRGSGSKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKMMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDD","statement":[{"text":"The lack of electron density in this region, as show in the PDB, indicates a disorder region.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-24T12:44:02.935Z"}},{"start":846,"end":873,"reference_id":"28841137","reference_source":"pmid","reference_html":"Autoinhibition of ankyrin-B/G membrane target bindings by intrinsically disordered segments from the tail regions.  <i> Chen K, Li J, Wang C, Wei Z, Zhang M. </i> Elife, 2017","date":"2022-05-20T15:31:05.657Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5Y4F"}],"region_id":"DP03650r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30089","entry_name":"acetate"}],"sequence_construct":"SGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDD","statement":[{"text":"The lack of electron density in this region, shown in the PDB, indicates a disorder region.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-24T12:50:55.561Z"}},{"start":683,"end":693,"reference_id":"28841137","reference_source":"pmid","reference_html":"Autoinhibition of ankyrin-B/G membrane target bindings by intrinsically disordered segments from the tail regions.  <i> Chen K, Li J, Wang C, Wei Z, Zhang M. </i> Elife, 2017","date":"2022-05-20T15:42:55.907Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5Y4D"}],"region_id":"DP03650r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"sequence_construct":"GPGSEFCADQYWNEVAVIDAIPLAATEHDTMLEMSDMQVWSAGDHPPIVSEEDISGSLVPRGSGSKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKMMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTK","statement":[{"text":"The lack of electron density in this region, shown in the PDB, indicates a disorder region.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-24T12:47:30.517Z"}},{"start":1243,"end":1255,"reference_id":"32353364","reference_source":"pmid","reference_html":"Structural Basis Underlying Strong Interactions between Ankyrins and Spectrins. <i> Li J, Chen K, Zhu R, Zhang M. </i> J Mol Biol, 2020","date":"2022-05-20T15:50:29.260Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"6M3Q"}],"region_id":"DP03650r008","sequence_construct":"TENLDNVALSSSPIHSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASSDVMLNGFGGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKE","statement":[{"text":"The lack of electron density in this region, shown in the PDB, indicates a disorder region.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-24T14:04:03.729Z"}}],"regions_counter":8,"released":"2022_06","sequence":"MMNEDAAQKSDSGEKFNGSSQRRKRPKKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKMMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDDSLPSSQFLDGMNYLRYSLEGGRSDSLRSFSSDRSHTLSHASYLRDSAVMDDSVVIPSHQVSTLAKEAERNSYRLSWGTENLDNVALSSSPIHSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGKLHLPTAPPPLNEGESLVSRILQLGPPGTKFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASSDVMLNGFGGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNDETESTETSVLKSHLVNEVPVLASPDLLSEVSEMKQDLIKMTAILTTDVSDKAGSIKVKELVKAAEEEPGEPFEIVERVKEDLEKVNEILRSGTCTRDESSVQSSRSERGLVEEEWVIVSDEEIEEARQKAPLEITEYPCVEVRIDKEIKGKVEKDSTGLVNYLTDDLNTCVPLPKEQLQTVQDKAGKKCEALAVGRSSEKEGKDIPPDETQSTQKQHKPSLGIKKPVRRKLKEKQKQKEEGLQASAEKAELKKGSSEESLGEDPGLAPEPLPTVKATSPLIEETPIGSIKDKVKALQKRVEDEQKGRSKLPIRVKGKEDVPKKTTHRPHPAASPSLKSERHAPGSPSPKTERHSTLSSSAKTERHPPVSPSSKTEKHSPVSPSAKTERHSPASSSSKTEKHSPVSPSTKTERHSPVSSTKTERHPPVSPSGKTDKRPPVSPSGRTEKHPPVSPGRTEKRLPVSPSGRTDKHQPVSTAGKTEKHLPVSPSGKTEKQPPVSPTSKTERIEETMSVRELMKAFQSGQDPSKHKTGLFEHKSAKQKQPQEKGKVRVEKEKGPILTQREAQKTENQTIKRGQRLPVTGTAESKRGVRVSSIGVKKEDAAGGKEKVLSHKIPEPVQSVPEEESHRESEVPKEKMADEQGDMDLQISPDRKTSTDFSEVIKQELEDNDKYQQFRLSEETEKAQLHLDQVLTSPFNTTFPLDYMKDEFLPALSLQSGALDGSSESLKNEGVAGSPCGSLMEGTPQISSEESYKHEGLAETPETSPESLSFSPKKSEEQTGETKESTKTETTTEIRSEKEHPTTKDITGGSEERGATVTEDSETSTESFQKEATLGSPKDTSPKRQDDCTGSCSVALAKETPTGLTEEAACDEGQRTFGSSAHKTQTDSEVQESTATSDETKALPLPEASVKTDTGTESKPQGVIRSPQGLELALPSRDSEVLSAVADDSLAVSHKDSLEASPVLEDNSSHKTPDSLEPSPLKESPCRDSLESSPVEPKMKAGIFPSHFPLPAAVAKTELLTEVASVRSRLLRDPDGSAEDDSLEQTSLMESSGKSPLSPDTPSSEEVSYEVTPKTTDVSTPKPAVIHECAEEDDSENGEKKRFTPEEEMFKMVTKIKMFDELEQEAKQKRDYKKEPKQEESSSSSDPDADCSVDVDEPKHTGSGEDESGVPVLVTSESRKVSSSSESEPELAQLKKGADSGLLPEPVIRVQPPSPLPSSMDSNSSPEEVQFQPVVSKQYTFKMNEDTQEEPGKSEEEKDSESHLAEDRHAVSTEAEDRSYDKLNRDTDQPKICDGHGCEAMSPSSSAAPVSSGLQSPTGDDVDEQPVIYKESLALQGTHEKDTEGEELDVSRAESPQADCPSESFSSSSSLPHCLVSEGKELDEDISATSSIQKTEVTKTDETFENLPKDCPSQDSSITTQTDRFSMDVPVSDLAENDEIYDPQITSPYENVPSQSFFSSEESKTQTDANHTTSFHSSEVYSVTITSPVEDVVVASSSSGTVLSKESNFEGQDIKMESQQESTLWEMQSDSVSSSFEPTMSATTTVVGEQISKVIITKTDVDSDSWSEIREDDEAFEARVKEEEQKIFGLMVDRQSQGTTPDTTPARTPTEEGTPTSEQNPFLFQEGKLFEMTRSGAIDMTKRSYADESFHFFQIGQESREETLSEDVKEGATGADPLPLETSAESLALSESKETVDDEADLLPDDVSEEVEEIPASDAQLNSQMGISASTETPTKEAVSVGTKDLPTVQTGDIPPLSGVKQISCPDSSEPAVQVQLDFSTLTRSVYSDRGDDSPDSSPEEQKSVIEIPTAPMENVPFTESKSKIPVRTMPTSTPAPPSAEYESSVSEDFLSSVDEENKADEAKPKSKLPVKVPLQRVEQQLSDLDTSVQKTVAPQGQDMASIAPDNRSKSESDASSLDSKTKCPVKTRSYTETETESRERAEELELESEEGATRPKILTSRLPVKSRSTTSSCRGGTSPTKESKEHFFDLYRNSIEFFEEISDEASKLVDRLTQSEREQEIVSDDESSSALEVSVIENLPPVETEHSVPEDIFDTRPIWDESIETLIERIPDENGHDHAEDPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNTEPLQERISHSYAEIEQTITLDHSEGFSVLQEELCTAQHKQKEEQAVSKESETCDHPPIVSEEDISVGYSTFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTETSETQKAMIVPSSPSKTPEEVSTPAEEEKLYLQTPTSSERGGSPIIQEPEEPSEHREESSPRKTSLVIVESADNQPETCERLDEDAAFEKGDDMPEIPPETVTEEEYIDEHGHTVVKKVTRKIIRRYVSSEGTEKEEIMVQGMPQEPVNIEEGDGYSKVIKRVVLKSDTEQSEDNNE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins","NDDs-related proteins"],"genes":[{"name":{"value":"ANK2"},"synonyms":[{"value":"ANKB","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"27718357","url":"http://www.ncbi.nlm.nih.gov/pubmed/27718357","alternativeUrl":"https://europepmc.org/abstract/MED/27718357"}}]}]}],"disorder_content":0.028051554207733132,"disprot_consensus":{"full":[{"start":683,"end":693,"type":"D"},{"start":817,"end":873,"type":"D"},{"start":1113,"end":1122,"type":"D"},{"start":1243,"end":1255,"type":"D"},{"start":1457,"end":1476,"type":"D"}],"Structural state":[{"start":683,"end":693,"type":"D"},{"start":817,"end":873,"type":"D"},{"start":1113,"end":1122,"type":"D"},{"start":1243,"end":1255,"type":"D"},{"start":1457,"end":1476,"type":"D"}],"Disorder function":[{"start":1113,"end":1122,"type":"F"},{"start":1457,"end":1476,"type":"F"}]}},{"disprot_id":"DP03651","acc":"Q9MBH1","creator":"cpintado","date":"2022-05-20T10:29:38.354Z","features":{"pfam":[{"id":"PF06094","name":"Gamma-glutamyl cyclotransferase, AIG2-like","start":11,"end":122}],"gene3D":[]},"length":165,"name":"Protein AIG2 C","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":148,"end":165,"reference_id":"18214976","reference_source":"pmid","reference_html":"Solution structure of At3g28950 from Arabidopsis thaliana. <i> de la Cruz NB, Peterson FC, Volkman BF. </i> Proteins, 2008","date":"2022-07-08T10:30:57.877Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2JQV"},{"db":"BMRB","id":"15295"}],"region_id":"DP03651r001","statement":[{"text":"Heteronuclear 15N-1H NOE values shown in Figure 1(E) reflect the relative rigidity of the secondary structure elements and disorder in the C-terminus, specifically beyond the untethered C-terminal α-helix. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T13:31:54.813Z"}},{"start":110,"end":121,"reference_id":"18214976","reference_source":"pmid","reference_html":"Solution structure of At3g28950 from Arabidopsis thaliana. <i> de la Cruz NB, Peterson FC, Volkman BF. </i> Proteins, 2008","date":"2022-07-08T10:33:33.563Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2JQV"},{"db":"BMRB","id":"15295"}],"region_id":"DP03651r002","statement":[{"text":"Residue ranges for secondary structure elements include: α1(19–27), α2(71–81), α3(122–147), α4(152–157), β1(9–13), β2(32–39), β3(42–43), β4(54–55), β5(61–70), β6(86–95) and β7(101–109).","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T13:31:54.276Z"}}],"regions_counter":2,"released":"2023_12","sequence":"MTSSDPQSHNVFVYGSILEPAVAAVILDRTADTVPAVLHGYHRYKLKGLPYPCIVSSDSGKVNGKVITGVSDAELNNFDVIEGNDYERVTVEVVRMDNSEKVKVETYVWVNKDDPRMYGEWDFEEWRVVHAEKFVETFRKMLEWNKNPNGKSMEEAVGSLLSSGD","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"genes":[{"name":{"value":"AIG2C","evidences":[{"code":"ECO:0000305"}]},"orfNames":[{"value":"K5K13.6","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"BAA95746.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAA95746.1"}}]}],"olnNames":[{"value":"At3g28950","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT3G28950","url":""}}]}]}],"alphafold_very_low_content":0.04242424242424243,"disorder_content":0.18181818181818182,"disprot_consensus":{"full":[{"start":110,"end":121,"type":"D"},{"start":148,"end":165,"type":"D"}],"Structural state":[{"start":110,"end":121,"type":"D"},{"start":148,"end":165,"type":"D"}]}},{"disprot_id":"DP03652","acc":"Q9LTJ1","creator":"cpintado","date":"2022-05-20T10:41:36.386Z","features":{"pfam":[{"id":"PF01429","name":"Methyl-CpG binding domain","start":73,"end":176}],"gene3D":[]},"length":225,"name":"Methyl-CpG-binding domain-containing protein 6","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":128,"end":140,"reference_id":"35128234","reference_source":"pmid","reference_html":"Structural Insights into Methylated DNA Recognition by the Methyl-CpG Binding Domain of MBD6 from <i>Arabidopsis thaliana</i>. <i> Mahana Y, Ohki I, Walinda E, Morimoto D, Sugase K, Shirakawa M. </i> ACS Omega, 2022","date":"2022-07-11T15:06:29.207Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7D8K"}],"region_id":"DP03652r001","statement":[{"text":"The obtained 20 minimum energy structures were well defined, as indicated by the root-mean-square deviation (RMSD) for the backbone of 0.6 ± 0.2 Å except for a loop region (residues 93–98) and a disordered C-terminal region (residues 128–140) (Figure2A and Table 2).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T15:13:14.360Z"}},{"start":67,"end":78,"reference_id":"34919920","reference_source":"pmid","reference_html":"Family-wide Characterization of Methylated DNA Binding Ability of Arabidopsis MBDs. <i> Wu Z, Chen S, Zhou M, Jia L, Li Z, Zhang X, Min J, Liu K. </i> J Mol Biol, 2022","date":"2022-11-10T17:57:09.930Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03652r003","statement":[{"text":"The PDB structure of AtMBD6 with methylated DNA shows this region lacks electron density, indicating it is disordered. ","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"7FEF"}]},{"start":127,"end":137,"reference_id":"34919920","reference_source":"pmid","reference_html":"Family-wide Characterization of Methylated DNA Binding Ability of Arabidopsis MBDs. <i> Wu Z, Chen S, Zhou M, Jia L, Li Z, Zhang X, Min J, Liu K. </i> J Mol Biol, 2022","date":"2022-11-10T17:57:30.698Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7FEF"}],"region_id":"DP03652r004","statement":[{"text":"The PDB structure of AtMBD6 with methylated DNA shows this region lacks electron density, indicating it is disordered. ","type":"Curator statement"}]}],"regions_counter":4,"released":"2023_12","sequence":"MSDSVAGDFPPDPLLASGAFISSAGDGTLDSSAKRRPIQGGIGISGSGESVRIGMANGTDQVNHQTESKSRKRAAPGDNWLPPGWRVEDKIRTSGATAGSVDKYYYEPNTGRKFRSRTEVLYYLEHGTSKRGTKKAENTYFNPDHFEGQGSNRVTRTATVPPPPPPPLDFDFKNPPDKVSWSMANAGEEGWIPNIGDVKVQDSVRRDWSTAFTFITSRNPSKVSA","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"genes":[{"name":{"value":"MBD6","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12954765","url":"http://www.ncbi.nlm.nih.gov/pubmed/12954765","alternativeUrl":"https://europepmc.org/abstract/MED/12954765"}}]},"orfNames":[{"value":"F2O15.4","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"BAA97474.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAA97474.1"}}]}],"olnNames":[{"value":"At5g59380","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT5G59380","url":""}}]}]}],"alphafold_very_low_content":0.28888888888888886,"disorder_content":0.11555555555555555,"disprot_consensus":{"full":[{"start":67,"end":78,"type":"D"},{"start":127,"end":140,"type":"D"}],"Structural state":[{"start":67,"end":78,"type":"D"},{"start":127,"end":140,"type":"D"}]}},{"disprot_id":"DP03653","acc":"Q1ECR9","creator":"cpintado","date":"2022-05-20T10:56:20.471Z","features":{"pfam":[{"id":"PF05498","name":"Rapid ALkalinization Factor (RALF)","start":16,"end":75}],"gene3D":[]},"length":82,"name":"Protein RALF-like 8","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":27,"end":82,"reference_id":"31004454","reference_source":"pmid","reference_html":"Function and solution structure of the Arabidopsis thaliana RALF8 peptide. <i> Frederick RO, Haruta M, Tonelli M, Lee W, Cornilescu G, Cornilescu CC, Sussman MR, Markley JL. </i> Protein Sci, 2019","date":"2022-07-08T10:43:24.746Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6NU4"}],"region_id":"DP03653r001","statement":[{"text":"The protein is dynamically disordered with the exception of two ordered loops that are held together by disulfide bridges. The C21–C29 loop (red) is more ordered than the C41–C47 loop (magenta), and the two ordered regions are independently ordered.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T13:41:01.930Z"}},{"start":27,"end":82,"reference_id":"31004454","reference_source":"pmid","reference_html":"Function and solution structure of the Arabidopsis thaliana RALF8 peptide. <i> Frederick RO, Haruta M, Tonelli M, Lee W, Cornilescu G, Cornilescu CC, Sussman MR, Markley JL. </i> Protein Sci, 2019","date":"2022-07-08T10:55:46.766Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"GO:0007204","term_name":"positive regulation of cytosolic calcium ion concentration","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","region_id":"DP03653r003","statement":[{"text":"Purified samples of the native sequence of RALF8 exhibited well-resolved nuclear magnetic resonance (NMR) spectra and also biological activity through interaction with a plant receptor kinase, cytoplasmic calcium mobilization, and in vivo root growth suppression.","type":"Abstract"},{"text":"RALF8 samples were shown to be active by a cytoplasmic calcium mobilization assay [Fig.4(a)] and by a root growth inhibition assay [Fig.4(b,c)].","type":"Results"}],"term_comment":"","term_def":"\"Any process that increases the concentration of calcium ions in the cytosol.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T13:41:57.269Z"}},{"start":27,"end":82,"reference_id":"31004454","reference_source":"pmid","reference_html":"Function and solution structure of the Arabidopsis thaliana RALF8 peptide. <i> Frederick RO, Haruta M, Tonelli M, Lee W, Cornilescu G, Cornilescu CC, Sussman MR, Markley JL. </i> Protein Sci, 2019","date":"2022-07-08T10:52:52.277Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"GO:0010082","term_name":"regulation of root meristem growth","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007119","ec_ontology":"ECO","ec_name":"in vivo assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP03653r004","statement":[{"text":"Purified samples of the native sequence of RALF8 exhibited well-resolved nuclear magnetic resonance (NMR) spectra and also biological activity through interaction with a plant receptor kinase, cytoplasmic calcium mobilization, and in vivo root growth suppression.","type":"Abstract"},{"text":"Wild‐type roots showed 75% growth inhibition at 1μM RALF8 concentration compared with the control condition, whereas fer knockout mutant roots were completely insensitive to RALF8‐caused suppression up to 5μM RALF8, with the highest concentration examined in this study.","type":"Results"}],"term_comment":"","term_def":"\"Any process involved in maintaining the size and shape of a root meristem.\" [GOC:tb]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T13:41:31.418Z"}}],"regions_counter":5,"released":"2023_12","sequence":"MGMSKSIKVILSLALVVFLALAGTKVEASVRYITYPAIDRGDHAVHCDKAHPNTCKKKQANPYRRGCGVLEGCHRETGPKPT","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"genes":[{"name":{"value":"RALFL8"},"orfNames":[{"value":"T25B24"}],"olnNames":[{"value":"At1g61563"}]}],"alphafold_very_low_content":0,"disorder_content":0.6829268292682927,"disprot_consensus":{"full":[{"start":27,"end":82,"type":"D"}],"Structural state":[{"start":27,"end":82,"type":"D"}],"Biological process":[{"start":27,"end":82,"type":"F"}]}},{"disprot_id":"DP03654","acc":"P63104","creator":"vacs","date":"2022-05-20T11:18:46.904Z","features":{"pfam":[{"id":"PF00244","name":"14-3-3 protein","start":9,"end":229}],"gene3D":[]},"length":245,"name":"14-3-3 protein zeta/delta","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":234,"end":245,"reference_id":"21554249","reference_source":"pmid","reference_html":"NMR spectroscopy of 14-3-3ζ reveals a flexible C-terminal extension: differentiation of the chaperone and phosphoserine-binding activities of 14-3-3ζ. <i> Williams DM, Ecroyd H, Goodwin KL, Dai H, Fu H, Woodcock JM, Zhang L, Carver JA. </i> Biochem J, 2011","date":"2022-05-20T11:25:59.157Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03654r001","statement":[{"text":"NMR spectroscopy of 14-3-3ζ reveals a flexible C-terminal extension: differentiation of the chaperone and phosphoserine-binding activities of 14-3-3ζ","type":"Title"},{"text":"1H-NMR spectroscopy revealed the presence of a flexible and unstructured C-terminal extension, 12 amino acids in length, which protrudes from the domain core of 14-3-3ζ and is similar in structure and length to the C-terminal extension of mammalian sHsps. ","type":"Abstract"},{"text":"It is concluded that, like sHsps, 14-3-3ζ has a short C-terminal extension that is flexible, polar and unstructured. Its function is to stabilize and solubilize the protein, and it has no direct role in its chaperone action.","type":"Introduction"},{"text":"Taken together these results indicated that the strongest cross-peaks in the two-dimensional NMR spectra of full-length 14-3-3ζ were attributable to the 12 amino acid residues at the extreme C-terminus of the 14-3-3ζ dimer (i.e. from Gly234 to Asn245), with no cross-peaks being observed for residues preceding Gly234.","type":"Results"},{"text":"From this, it can be inferred that the amino acids from Trp228 to Gln233 (inclusive) form a ‘hinge’ which has decreased conformational flexibility, spanning the region between the domain core of the protein and the 12 amino acids (Gly234–Asn245) at the extreme C-terminus of 14-3-3ζ which have significantly enhanced flexibility. ","type":"Results"},{"text":"The significant overlap of cross-peaks in the TOCSY spectra of 14-3-3ζ from Gly234 to Asn245 with the peptide corresponding to the last 16 amino acids of the protein, the close similarity of α-CH chemical shifts to random coil values [32] and the presence of strong sequential NHi+ 1 to α-CHi nuclear Overhauser effects show that the C-terminus of 14-3-3ζ has an extended conformation with little or no preferred secondary structure, and a much greater degree of conformational flexibility than the rest of the protein. Thus 14-3-3ζ has a flexible C-terminal extension encompassing its last 12 amino acids that is directly comparable with the C-terminal extension of mammalian sHsps in terms of its polar nature and conformational flexibility.","type":"Results"},{"text":"Consistent with folding prediction algorithms, the NMR data indicate that the last 12 C-terminal amino acids of 14-3-3ζ (Gly234–Asp245) are solvent-exposed and exhibit flexibility that is independent of the domain core of the protein, while adopting no preferred secondary structure.","type":"Discussion"},{"text":"Therefore it is concluded that 14-3-3ζ, and by analogy all other 14-3-3 proteins, have a flexible C-terminal extension.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-25T10:09:02.546Z"}},{"start":234,"end":245,"reference_id":"21554249","reference_source":"pmid","reference_html":"NMR spectroscopy of 14-3-3ζ reveals a flexible C-terminal extension: differentiation of the chaperone and phosphoserine-binding activities of 14-3-3ζ. <i> Williams DM, Ecroyd H, Goodwin KL, Dai H, Fu H, Woodcock JM, Zhang L, Carver JA. </i> Biochem J, 2011","date":"2022-05-20T11:30:51.128Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"GO:0031647","term_name":"regulation of protein stability","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","region_id":"DP03654r002","statement":[{"text":"The extension stabilizes 14-3-3ζ, but has no direct role in chaperone action.","type":"Abstract"},{"text":"It is concluded that, like sHsps, 14-3-3ζ has a short C-terminal extension that is flexible, polar and unstructured. Its function is to stabilize and solubilize the protein, and it has no direct role in its chaperone action.","type":"Introduction"},{"text":"Truncation of 14-3-3ζ resulted in a slight decrease in the mean residue elipticity at 208 and 222 nm relative to the WT protein, implying reduced α-helical content for the truncated mutant relative to the WT protein. As our NMR studies indicate that the C-terminal extension of 14-3-3ζ adopts a disordered solvent-exposed structure in solution with no preferred secondary structure, the decreased CD minima observed for truncated 14-3- 3ζ relative to WT suggest that this extension stabilizes the domain core and α-helical content of the 14-3-3ζ dimer.","type":"Results"},{"text":"The far-UV CD spectra of WT (continuous line) and 15C (broken line) 14-3-3ζ illustrating the decreased α-helical structure of the truncated protein at 37◦C, as denoted by the decreased minima at 208 and 222 nm relative to that of WT 14-3-3ζ.","type":"Figure"},{"text":"Thus, on the basis of the yeast two-hybrid studies, SEC, MALLS, CD and DLS analysis, it is concluded that although truncation of 14-3-3ζ does not affect the ability of the protein to form dimers at 25 ◦C, the C-terminal extension is important in maintaining the overall shape, secondary structure and dimeric state of the protein at 37 ◦C.","type":"Results"},{"text":"However, although C-terminal truncation of 14-3-3ζ did not significantly alter the average diameter of the dimer at 25 ◦C, at physiological temperature, the truncated protein aggregated progressively with time. C-terminal truncation also slightly decreased the α-helical content of 14-3-3ζ. Thus the C-terminal extension of 14-3-3ζ is important in maintaining the overall structural integrity of the protein without directly being involved in dimer formation. Consistent with this, C-terminal truncation resulted in a significant decrease in the thermostability of the protein, and enhanced its susceptibility to denaturant.","type":"Discussion"}],"term_comment":"","term_def":"\"Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.\" [GOC:dph, GOC:mah, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-25T10:09:52.570Z"}},{"start":234,"end":245,"reference_id":"21554249","reference_source":"pmid","reference_html":"NMR spectroscopy of 14-3-3ζ reveals a flexible C-terminal extension: differentiation of the chaperone and phosphoserine-binding activities of 14-3-3ζ. <i> Williams DM, Ecroyd H, Goodwin KL, Dai H, Fu H, Woodcock JM, Zhang L, Carver JA. </i> Biochem J, 2011","date":"2022-05-20T11:34:33.851Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"GO:0031647","term_name":"regulation of protein stability","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","region_id":"DP03654r003","statement":[{"text":"The extension stabilizes 14-3-3ζ, but has no direct role in chaperone action.","type":"Abstract"},{"text":"It is concluded that, like sHsps, 14-3-3ζ has a short C-terminal extension that is flexible, polar and unstructured. Its function is to stabilize and solubilize the protein, and it has no direct role in its chaperone action.","type":"Introduction"},{"text":"Thus the truncated mutant has a tendency to aggregate at physiological temperature (Figure 3D, right-hand panel).","type":"Results"},{"text":"DLS profiles of WT (left-hand panel) and 15C (right-hand panel) 14-3-3ζ at 25◦C and 37◦C, where the eluted particle size distribution is shown by number and demonstrates the propensity of 15C 14-3-3ζ to aggregate with time at 37◦C.","type":"Figure"},{"text":"Thus, on the basis of the yeast two-hybrid studies, SEC, MALLS, CD and DLS analysis, it is concluded that although truncation of 14-3-3ζ does not affect the ability of the protein to form dimers at 25 ◦C, the C-terminal extension is important in maintaining the overall shape, secondary structure and dimeric state of the protein at 37 ◦C.","type":"Results"},{"text":"These data are also consistent with the DLS data in Figure 3(D) which highlight the greater tendency for 15C 14-3-3ζ to aggregate compared with the full-length protein.","type":"Results"},{"text":"However, although C-terminal truncation of 14-3-3ζ did not significantly alter the average diameter of the dimer at 25 ◦C, at physiological temperature, the truncated protein aggregated progressively with time. C-terminal truncation also slightly decreased the α-helical content of 14-3-3ζ. Thus the C-terminal extension of 14-3-3ζ is important in maintaining the overall structural integrity of the protein without directly being involved in dimer formation. Consistent with this, C-terminal truncation resulted in a significant decrease in the thermostability of the protein, and enhanced its susceptibility to denaturant.","type":"Discussion"}],"term_comment":"","term_def":"\"Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.\" [GOC:dph, GOC:mah, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-25T10:09:45.848Z"}},{"start":234,"end":245,"reference_id":"21554249","reference_source":"pmid","reference_html":"NMR spectroscopy of 14-3-3ζ reveals a flexible C-terminal extension: differentiation of the chaperone and phosphoserine-binding activities of 14-3-3ζ. <i> Williams DM, Ecroyd H, Goodwin KL, Dai H, Fu H, Woodcock JM, Zhang L, Carver JA. </i> Biochem J, 2011","date":"2022-05-20T11:37:30.265Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"GO:0031647","term_name":"regulation of protein stability","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006317","ec_ontology":"ECO","ec_name":"temperature-induced protein unfolding evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","region_id":"DP03654r004","statement":[{"text":"The extension stabilizes 14-3-3ζ, but has no direct role in chaperone action.","type":"Abstract"},{"text":"It is concluded that, like sHsps, 14-3-3ζ has a short C-terminal extension that is flexible, polar and unstructured. Its function is to stabilize and solubilize the protein, and it has no direct role in its chaperone action.","type":"Introduction"},{"text":"The light-scattering data suggest that C-terminal truncation of 14-3-3ζ decreases its thermostability and hence its C-terminal extension contributes to the stability of the protein. In agreement with this, the far-UV CD-melting profiles also indicated that the truncated protein had decreased thermostability relative to the WT protein, as quantified by a decrease in α-helical content of both proteins at 222 nm with increasing temperature due to unfolding and aggregation (Figure 4B). These data indicated that 15C 14-3-3ζ began to lose α-helical content at 32 ◦C, whereas this did not occur until approximately 37 ◦C for the WT protein.","type":"Results"},{"text":"The melting curve of 15C relative toWT 14-3-3ζ illustrates a decrease from 60◦C to 56◦C at which the mid-point of protein denaturation/unfolding occurs due to C-terminal truncation.","type":"Figure"},{"text":"Thus truncation of the C-terminal extension led to decreased stability of 14-3-3ζ to denaturant. It is therefore concluded that the C-terminal extension of 14-3-3ζ has a role in maintaining the structural integrity of the domain core of the protein.","type":"Results"},{"text":"Thus the C-terminal extension of 14-3-3ζ is important in maintaining the overall structural integrity of the protein without directly being involved in dimer formation. Consistent with this, C-terminal truncation resulted in a significant decrease in the thermostability of the protein, and enhanced its susceptibility to denaturant.","type":"Discussion"}],"term_comment":"","term_def":"\"Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.\" [GOC:dph, GOC:mah, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-25T10:09:34.266Z"}},{"start":234,"end":245,"reference_id":"21554249","reference_source":"pmid","reference_html":"NMR spectroscopy of 14-3-3ζ reveals a flexible C-terminal extension: differentiation of the chaperone and phosphoserine-binding activities of 14-3-3ζ. <i> Williams DM, Ecroyd H, Goodwin KL, Dai H, Fu H, Woodcock JM, Zhang L, Carver JA. </i> Biochem J, 2011","date":"2022-05-20T11:38:58.445Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"GO:0031647","term_name":"regulation of protein stability","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006313","ec_ontology":"ECO","ec_name":"urea-induced protein unfolding evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","region_id":"DP03654r005","statement":[{"text":"The extension stabilizes 14-3-3ζ, but has no direct role in chaperone action.","type":"Abstract"},{"text":"It is concluded that, like sHsps, 14-3-3ζ has a short C-terminal extension that is flexible, polar and unstructured. Its function is to stabilize and solubilize the protein, and it has no direct role in its chaperone action.","type":"Introduction"},{"text":"C-terminal truncation of 14-3-3ζ reduces the half-point of unfolding by 0.33 M urea relative to the full-length protein.","type":"Figure"},{"text":"Thus truncation of the C-terminal extension led to decreased stability of 14-3-3ζ to denaturant. It is\ntherefore concluded that the C-terminal extension of 14-3-3ζ has a role in maintaining the structural integrity of the domain core of the protein.","type":"Results"},{"text":"Thus the C-terminal extension of 14-3-3ζ is important in maintaining the overall structural integrity of the protein without directly being involved in dimer formation. Consistent with this, C-terminal truncation resulted in a significant decrease in the thermostability of the protein, and enhanced its susceptibility to denaturant.","type":"Discussion"}],"term_comment":"","term_def":"\"Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.\" [GOC:dph, GOC:mah, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-25T10:09:25.583Z"}}],"regions_counter":5,"released":"2023_12","sequence":"MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAGEGGEN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"YWHAZ"}}],"alphafold_very_low_content":0.04081632653061224,"disorder_content":0.04897959183673469,"disprot_consensus":{"full":[{"start":234,"end":245,"type":"D"}],"Structural state":[{"start":234,"end":245,"type":"D"}],"Biological process":[{"start":234,"end":245,"type":"F"}]}},{"disprot_id":"DP03655","acc":"Q9SSK9","creator":"cpintado","date":"2022-05-20T11:23:35.268Z","features":{"pfam":[{"id":"PF00407","name":"Pathogenesis-related protein Bet v 1 family","start":21,"end":172},{"id":"PF00407","name":"Pathogenesis-related protein Bet v 1 family","start":183,"end":334}],"gene3D":[]},"length":335,"name":"MLP-like protein 28","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":45,"end":65,"reference_id":"19326460","reference_source":"pmid","reference_html":"Structures of two Arabidopsis thaliana major latex proteins represent novel helix-grip folds. <i> Lytle BL, Song J, de la Cruz NB, Peterson FC, Johnson KA, Bingman CA, Phillips GN, Volkman BF. </i> Proteins, 2009","date":"2022-05-20T11:25:47.004Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2I9Y"}],"region_id":"DP03655r001","statement":[{"text":"The MLP28 structure deviates significantly from the conserved Bet v 1 fold in that the β2 strand and the second short α-helix between strands β1 and β2 of the Bet v 1 fold are replaced by a long, flexible loop comprising residues 45–65.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-07T19:11:04.273Z"}}],"regions_counter":2,"released":"2023_12","sequence":"MADVATKHPMEDEVKKTEASSLVGKLETDVEIKASADKFHHMFAGKPHHVSKASPGNIQGCDLHEGDWGTVGSIVFWNYVHDGEAKVAKERIEAVEPDKNLITFRVIEGDLMKEYKSFLLTIQVTPKPGGPGSIVHWHLEYEKISEEVAHPETLLQFCVEVSKEIDEHLLAEEEEVKTPETPSLVGKLETDVEIKASAEKFHHMFAGKPHHVSKASPGNIQGCDLHEGDWGQVGSIVFWNYVHDREAKVAKERIEAVEPNKNLITFRVIDGDLMKEYKSFLLTIQVTPKLGGPGSIVHWHLEYEKISEEVAHPETLLQFCVEVSKEIDEHLLAEE","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"genes":[{"name":{"value":"MLP28"},"orfNames":[{"value":"F15H11.8"}],"olnNames":[{"value":"At1g70830"}]}],"alphafold_very_low_content":0.06865671641791045,"disorder_content":0.0626865671641791,"disprot_consensus":{"full":[{"start":45,"end":65,"type":"D"}],"Structural state":[{"start":45,"end":65,"type":"D"}]}},{"disprot_id":"DP03656","acc":"Q9SN73","creator":"cpintado","date":"2022-05-20T14:02:03.737Z","features":{"pfam":[{"id":"PF25436","name":"BSD2 cysteine rich domain","start":68,"end":136}],"gene3D":[]},"length":136,"name":"Protein BUNDLE SHEATH DEFECTIVE 2, chloroplastic","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":57,"end":67,"reference_id":"29217567","reference_source":"pmid","reference_html":"Plant RuBisCo assembly in E. coli with five chloroplast chaperones including BSD2. <i> Aigner H, Wilson RH, Bracher A, Calisse L, Bhat JY, Hartl FU, Hayer-Hartl M. </i> Science, 2017","date":"2022-07-08T11:07:59.065Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6EKB"}],"region_id":"DP03656r001","statement":[{"text":"The chain termini (residues 56 to 67 and 130\nto 136) are disordered.","type":"Results"},{"text":"Disordered boundaries are 57-67 since the first residue of the PDB structure reported by the authors (metionine) does not overlap with the first amino acid of UniProt sequence (lysine).","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T13:42:48.752Z"}}],"regions_counter":2,"released":"2023_12","sequence":"MANSLCFFSSPPTFCFQSPSKNPKPSHFFSTNDNTSSLVQKRELLQTSRSQSFEVKAANNNPQGTKPNSLVCANCEGEGCVACSQCKGGGVNLIDHFNGQFKAGALCWLCRGKKEVLCGDCNGAGFIGGFLSTFDE","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"genes":[{"name":{"value":"BSD2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"29217567","url":"http://www.ncbi.nlm.nih.gov/pubmed/29217567","alternativeUrl":"https://europepmc.org/abstract/MED/29217567"}}]},"orfNames":[{"value":"F1P2.200","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"CAB61991.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAB61991.1"}}]}],"olnNames":[{"value":"At3g47650","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT3G47650","url":""}}]}]}],"alphafold_very_low_content":0.25,"disorder_content":0.08088235294117647,"disprot_consensus":{"full":[{"start":57,"end":67,"type":"D"}],"Structural state":[{"start":57,"end":67,"type":"D"}]}},{"disprot_id":"DP03657","acc":"Q9SSA5","creator":"cpintado","date":"2022-05-20T14:26:48.940Z","features":{"pfam":[{"id":"PF00160","name":"Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD","start":258,"end":416},{"id":"PF21329","name":"Peptidyl-prolyl cis-trans isomerase CYP38-like, PsbQ-like domain","start":102,"end":218}],"gene3D":[]},"length":437,"name":"Peptidyl-prolyl cis-trans isomerase CYP38, chloroplastic","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":297,"end":336,"reference_id":"22706283","reference_source":"pmid","reference_html":"Crystal structure of Arabidopsis cyclophilin38 reveals a previously uncharacterized immunophilin fold and a possible autoinhibitory mechanism. <i> Vasudevan D, Fu A, Luan S, Swaminathan K. </i> Plant Cell, 2012","date":"2022-05-20T14:29:11.148Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3RFY"}],"region_id":"DP03657r001","statement":[{"text":"The loops in the cyclophilin domain are quite disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T12:41:13.369Z"}},{"start":350,"end":377,"reference_id":"22706283","reference_source":"pmid","reference_html":"Crystal structure of Arabidopsis cyclophilin38 reveals a previously uncharacterized immunophilin fold and a possible autoinhibitory mechanism. <i> Vasudevan D, Fu A, Luan S, Swaminathan K. </i> Plant Cell, 2012","date":"2022-05-20T14:29:32.832Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3RFY"}],"region_id":"DP03657r002","statement":[{"text":"The loops in the cyclophilin domain are quite disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-11T12:41:12.768Z"}}],"regions_counter":3,"released":"2023_12","sequence":"MAAAFASLPTFSVVNSSRFPRRRIGFSCSKKPLEVRCSSGNTRYTKQRGAFTSLKECAISLALSVGLMVSVPSIALPPNAHAVANPVIPDVSVLISGPPIKDPEALLRYALPIDNKAIREVQKPLEDITDSLKIAGVKALDSVERNVRQASRTLQQGKSIIVAGFAESKKDHGNEMIEKLEAGMQDMLKIVEDRKRDAVAPKQKEILKYVGGIEEDMVDGFPYEVPEEYRNMPLLKGRASVDMKVKIKDNPNIEDCVFRIVLDGYNAPVTAGNFVDLVERHFYDGMEIQRSDGFVVQTGDPEGPAEGFIDPSTEKTRTVPLEIMVTGEKTPFYGSTLEELGLYKAQVVIPFNAFGTMAMAREEFENDSGSSQVFWLLKESELTPSNSNILDGRYAVFGYVTDNEDFLADLKVGDVIESIQVVSGLENLANPSYKIAG","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"genes":[{"name":{"value":"CYP38"},"orfNames":[{"value":"F4P13.3"}],"olnNames":[{"value":"At3g01480"}]}],"alphafold_very_low_content":0.2219679633867277,"disorder_content":0.15560640732265446,"disprot_consensus":{"full":[{"start":297,"end":336,"type":"D"},{"start":350,"end":377,"type":"D"}],"Structural state":[{"start":297,"end":336,"type":"D"},{"start":350,"end":377,"type":"D"}]}},{"disprot_id":"DP03659","acc":"Q14318","creator":"vnugnes","date":"2022-05-20T19:33:47.814Z","features":{"pfam":[{"id":"PF00254","name":"FKBP-type peptidyl-prolyl cis-trans isomerase","start":114,"end":201},{"id":"PF13432","name":"Tetratricopeptide repeat","start":278,"end":339}],"gene3D":[]},"length":412,"name":"Peptidyl-prolyl cis-trans isomerase FKBP8","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":32,"reference_id":"24145868","reference_source":"pmid","reference_html":"Functional role of the flexible N-terminal extension of FKBP38 in catalysis. <i> Kang C, Ye H, Chia J, Choi BH, Dhe-Paganon S, Simon B, Schütz U, Sattler M, Yoon HS. </i> Sci Rep, 2013","date":"2022-05-23T13:42:44.404Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03659r001","statement":[{"text":"The N-terminal tail (residues 1–32) exhibits negative or near zero {1H}-15N hetNOE values, suggesting the unstructured characteristic of this region.","type":"Figure"},{"text":"The N-terminal extension (residues 1–32) is not presented for clarity as it is highly flexible and only a restricted number of NOEs were observed in this region.","type":"Figure"},{"text":"Comparable low heteronuclear NOE values are observed for residues 1–32 in the N-terminal extension for both the free and CaM/Ca2+-bound NTD indicating that this region exhibits increased conformational mobility on (sub)-nanosecond time scales. ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T14:39:46.162Z"}},{"start":1,"end":32,"reference_id":"24145868","reference_source":"pmid","reference_html":"Functional role of the flexible N-terminal extension of FKBP38 in catalysis. <i> Kang C, Ye H, Chia J, Choi BH, Dhe-Paganon S, Simon B, Schütz U, Sattler M, Yoon HS. </i> Sci Rep, 2013","date":"2022-05-20T20:30:08.193Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005516","term_name":"calmodulin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","region_id":"DP03659r002","statement":[{"text":"However, striking differences are observed for the local tumbling correlation times (τc, Fig. 2b) and T2 values (Supplementary Fig. S1) values for residues 11–26 in the N-terminal extension upon binding of the NTD to CaM/Ca2+. This indicates the presence of conformational exchange processes at μs-ms timescales that are linked to the interaction with CaM/Ca2+.","type":"Results"},{"text":"In the reciprocal experiment, addition of unlabeled CaM/Ca2+ to the 15N-labeled NTD generated noticeable changes in the 1H-15N HSQC spectrum, which were mapped primarily to the N-terminal extension of the NTD, mainly for residues Ala16, Arg17 and Phe19 – Glu24 (Fig. 4b,c).","type":"Results"},{"text":"Taken together, these data suggest that the N-terminal extension of FKBP38 is directly involved in a molecular interaction with CaM/Ca2+.","type":"Results"}],"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T14:43:19.565Z"}},{"start":1,"end":32,"reference_id":"24145868","reference_source":"pmid","reference_html":"Functional role of the flexible N-terminal extension of FKBP38 in catalysis. <i> Kang C, Ye H, Chia J, Choi BH, Dhe-Paganon S, Simon B, Schütz U, Sattler M, Yoon HS. </i> Sci Rep, 2013","date":"2022-05-20T20:09:22.646Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q14318","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03659r003","statement":[{"text":"A comparison of the 2D 1H- 15N HSQC spectra of the NTD (residues 1–149) and the FKBD38 (residues 33–149) (Fig. 3a) confirmed the structural similarity of the NTD and the FKDB38. However, differences in chemical shifts are observed for residues in the core domain, consistent with autoinhibitory interactions between the N-terminal extension and the core domain. As summarized in Figs. 3b and 3c, most of these perturbed residues were localized in a defined region, including residues Ser58, Lys62, Gly63 and Gln64 in the β1/β2-loop; Val65 in strand β2; Phe88 and Thr89 in β4; and Asp92, Cys93, Asp94, Val95 and Ile96 in the β4/α1-loop and close to the putative isomerase active site.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T14:41:36.424Z"}},{"start":1,"end":32,"reference_id":"24145868","reference_source":"pmid","reference_html":"Functional role of the flexible N-terminal extension of FKBP38 in catalysis. <i> Kang C, Ye H, Chia J, Choi BH, Dhe-Paganon S, Simon B, Schütz U, Sattler M, Yoon HS. </i> Sci Rep, 2013","date":"2022-05-23T13:54:25.962Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005516","term_name":"calmodulin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005644","ec_ontology":"ECO","ec_name":"immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","region_id":"DP03659r004","term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"P0DP23","operator":"and","partner_start":null,"partner_end":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T14:39:53.265Z"}},{"start":1,"end":32,"reference_id":"24145868","reference_source":"pmid","reference_html":"Functional role of the flexible N-terminal extension of FKBP38 in catalysis. <i> Kang C, Ye H, Chia J, Choi BH, Dhe-Paganon S, Simon B, Schütz U, Sattler M, Yoon HS. </i> Sci Rep, 2013","date":"2022-05-23T13:50:54.396Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000059","term_name":"self-inhibition","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03659r005","statement":[{"text":"As seen in Table 1, consistent with a previous study8, the isomerase activity of the full-length FKBP38 was activated by the addition of CaM/Ca2+. Interestingly, the FKBD38 showed similar levels of PPIase activity in the absence of CaM/Ca2+, suggesting that either the N- or C-terminal extensions were inhibitory and responsive to CaM/Ca2+. We then identified that NTD, a fragment of FKBP38, containing the N-terminal extension, but lacking the C-terminal extension, was activated by the addition of CaM/Ca2+ (Table 1). Taken together, the data suggest that the core isomerase activity of FKBP38 is inhibited by the N-terminal extension residues flanking the isomerase domain and that this inhibition is overcome by the addition of CaM/Ca2+.","type":"Results"},{"text":"The core isomerase activity of FKBP38 is inhibited by transient interactions involving the flexible N-terminal extension that precedes the catalytic domain.","type":"Abstract"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T14:39:52.447Z"}},{"start":1,"end":34,"reference_id":"20707607","reference_source":"pmid","reference_html":"New structural aspects of FKBP38 activation. <i> Maestre-Martínez M, Haupt K, Edlich F, Jahreis G, Jarczowski F, Erdmann F, Fischer G, Lücke C. </i> Biol Chem, 2010","date":"2022-05-23T15:59:13.966Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03659r006","statement":[{"text":"Interestingly, this FKBP381–165 variant showed a considerably higher stability in the presence of Ca2q-CaM compared to FKBP3835–153, but the 1 H/15N-HSQC spectra were dominated by a large number of very strong amide signals with narrow line-width that belong to the evidently non-structured segments Met1-Glu34 and Asp151-Asn165.","type":"Results"}],"sequence_construct":"MASCAEPSEPSAPLPAGVPPLEDFEVLDGVEDAEGEEEEEEEEEEEDDLSELPPLEDMGQPPAEEAEQPGALAREFLAAMEPEPAPAPAPEEWLDILGNGLLRKKTLVPGPPGSSRPVKGQVVTVHLQTSLENGTRVQEEPELVFTLGDCDVIQALDLSVPLMDV","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T14:39:44.752Z"}},{"start":151,"end":165,"reference_id":"20707607","reference_source":"pmid","reference_html":"New structural aspects of FKBP38 activation. <i> Maestre-Martínez M, Haupt K, Edlich F, Jahreis G, Jarczowski F, Erdmann F, Fischer G, Lücke C. </i> Biol Chem, 2010","date":"2022-05-23T15:59:32.371Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03659r007","statement":[{"text":"Interestingly, this FKBP381–165 variant showed a considerably higher stability in the presence of Ca2q-CaM compared to FKBP3835–153, but the 1 H/15N-HSQC spectra were dominated by a large number of very strong amide signals with narrow line-width that belong to the evidently non-structured segments Met1-Glu34 and Asp151-Asn165.","type":"Results"}],"sequence_construct":"MASCAEPSEPSAPLPAGVPPLEDFEVLDGVEDAEGEEEEEEEEEEEDDLSELPPLEDMGQPPAEEAEQPGALAREFLAAMEPEPAPAPAPEEWLDILGNGLLRKKTLVPGPPGSSRPVKGQVVTVHLQTSLENGTRVQEEPELVFTLGDCDVIQALDLSVPLMDV","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T14:39:39.419Z"}},{"start":1,"end":34,"reference_id":"20707607","reference_source":"pmid","reference_html":"New structural aspects of FKBP38 activation. <i> Maestre-Martínez M, Haupt K, Edlich F, Jahreis G, Jarczowski F, Erdmann F, Fischer G, Lücke C. </i> Biol Chem, 2010","date":"2022-05-23T15:58:55.970Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005516","term_name":"calmodulin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","region_id":"DP03659r008","statement":[{"text":"In the reverse experiment, upon titration with Ca2q-CaM strong CSP as well as line-broadening effects were observed at the Glu-rich N-terminus of 15N-labeled FKBP381–165 (Figure 4D), in particular within the segment Ala9-Glu26. The line-broadening effects, which were most pronounced for residues Leu15, Arg17, Leu20, Ala22, Met23 and Glu24, imply that this non-structured Glu-rich region interacts directly with CaM, or more precisely with helix A of the N-terminal CaM lobe which had exhibited additional binding-related effects compared to the experiments with the shorter FKBP3835–153 variant (Figure 4C).","type":"Results"},{"text":"Interestingly, the CSP effects found for 15N-labeled Ca2qCaM in the presence of the FKBP381–165 variant are similarly strong as in the case of FKBP3835–153 (Figure 4C),\nsuggesting that the contribution of the FKBP38 segment Ala9-Glu26 to this protein-protein interaction is only of minor importance.","type":"Results"}],"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","term_is_obsolete":false,"term_not_annotate":false,"sequence_construct":"MASCAEPSEPSAPLPAGVPPLEDFEVLDGVEDAEGEEEEEEEEEEEDDLSELPPLEDMGQPPAEEAEQPGALAREFLAAMEPEPAPAPAPEEWLDILGNGLLRKKTLVPGPPGSSRPVKGQVVTVHLQTSLENGTRVQEEPELVFTLGDCDVIQALDLSVPLMDV","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T14:39:50.862Z"}},{"start":357,"end":380,"reference_id":"28278223","reference_source":"pmid","reference_html":"The structure of FKBP38 in complex with the MEEVD tetratricopeptide binding-motif of Hsp90. <i> Blundell KL, Pal M, Roe SM, Pearl LH, Prodromou C. </i> PLoS One, 2017","date":"2022-05-23T15:38:51.459Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5MGX"}],"region_id":"DP03659r009","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02829","statements":[{"type":"Methods","text":"Crystals of FKBP92-380 in complex with yHsp90 DTEMEEVD peptide were obtained by mixing FKBP92-380 with yHsp90546-709 in a 1:1 molar ratio at 18 mg ml-1 and crystalizing by using the sitting drop vapour diffusion technique."}]}],"statement":[{"text":"The lack of electron density in this region, shown in the PDB, indicates an IDR.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-25T07:54:16.088Z"}},{"start":23,"end":28,"reference_id":"28381481","reference_source":"pmid","reference_html":"FKBP8 recruits LC3A to mediate Parkin-independent mitophagy. <i> Bhujabal Z, Birgisdottir ÅB, Sjøttem E, Brenne HB, Øvervatn A, Habisov S, Kirkin V, Lamark T, Johansen T. </i> EMBO Rep, 2017","date":"2022-05-23T19:03:26.052Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001245","ec_ontology":"ECO","ec_name":"peptide array evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"O95166","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9H492","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP03659r010","statement":[{"text":"Using arrays of overlapping 20‐mer peptides of FKBP8 moved by increments of three amino acids to cover the full‐length sequence, we detected a single LIR motif in the N‐terminus with the core sequence FEVL (Fig 1B).","type":"Results"},{"text":"Taken together, these results allowed the conclusion that FKBP8 contains a canonical N‐terminal LIR motif that interacts preferentially with LC3A in vivo.","type":"Results"},{"text":"LIR motif coresponds to the 24-27 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-25T09:30:10.097Z"}},{"start":23,"end":28,"reference_id":"28381481","reference_source":"pmid","reference_html":"FKBP8 recruits LC3A to mediate Parkin-independent mitophagy. <i> Bhujabal Z, Birgisdottir ÅB, Sjøttem E, Brenne HB, Øvervatn A, Habisov S, Kirkin V, Lamark T, Johansen T. </i> EMBO Rep, 2017","date":"2022-05-23T18:48:40.463Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"O95166","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9H0R8","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9H492","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P60520","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9GZQ8","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9BXW4","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP03659r011","statement":[{"text":"Mutations in the core LIR motif resulted in a significantly reduced FKBP8 binding to the ATG8 proteins (Fig 1C and D). Quantitation of the FKBP8 interactions shows high‐affinity binding toward GABARAPL1 and LC3A (Fig 1D), low‐affinity binding toward GABARAPL2 and LC3C, and intermediary‐affinity binding toward LC3B and GABARAP.","type":"Results"},{"text":"LIR motif coresponds to the 24-27 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-25T09:30:06.398Z"}},{"start":23,"end":28,"reference_id":"28381481","reference_source":"pmid","reference_html":"FKBP8 recruits LC3A to mediate Parkin-independent mitophagy. <i> Bhujabal Z, Birgisdottir ÅB, Sjøttem E, Brenne HB, Øvervatn A, Habisov S, Kirkin V, Lamark T, Johansen T. </i> EMBO Rep, 2017","date":"2022-05-23T19:21:18.043Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9GZQ8","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9H492","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"O95166","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP03659r012","statement":[{"text":"To investigate whether FKBP8 interacts with the ATG8 homologs in vivo, GFP‐tagged ATG8 proteins were co‐expressed with Flag‐tagged wild‐type (WT) or LIR‐mutated FKBP8 in HeLa cells, before immunoprecipitations using a Flag antibody. Efficient co‐precipitation of LC3A, and a weaker but significant co‐precipitation of LC3B were observed (Fig 1E). Surprisingly, only moderate co‐precipitation of GABARAP and no co‐precipitations of GABARAPL1 and GABARAPL2 were detected (Fig 1E). Consistent with the in vitro data, the FKBP8 LIR mutant did not co‐precipitate any of the ATG8 homologs.","type":"Results"},{"text":"LIR motif coresponds to the 24-27 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-25T09:29:59.797Z"}},{"start":23,"end":28,"reference_id":"28381481","reference_source":"pmid","reference_html":"FKBP8 recruits LC3A to mediate Parkin-independent mitophagy. <i> Bhujabal Z, Birgisdottir ÅB, Sjøttem E, Brenne HB, Øvervatn A, Habisov S, Kirkin V, Lamark T, Johansen T. </i> EMBO Rep, 2017","date":"2023-09-27T13:06:58.339Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1901524","term_name":"regulation of mitophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001163","ec_ontology":"ECO","ec_name":"co-localization evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"ec_go":"IDA","region_id":"DP03659r013","statement":[{"text":"To investigate if the co‐localization of LC3A and FKBP8 is mediated by the FKBP8 LIR motif, a Cerulean‐FKBP8 LIR mutant (F24A/L27A, hereafter denoted LIRm) was co‐expressed with EYFP‐LC3A and mCherry‐OMP25TM in the HeLa cells. Strikingly, the FKBP8 LIRm is localized both on the mitochondria and on ER, but it fails completely to co‐localize with LC3A upon CCCP treatment (Fig 3A–C). Instead, LC3A forms visible aggregates that do not overlap with the mCherry‐OMP25TM probe (Fig 3A), similarly as the vector control (Fig EV3A). Together, these results suggest that CCCP treatment induces a LIR‐mediated interaction between FKBP8 and LC3A, and this interaction is important for mitochondrial recruitment of LC3A.","type":"Results"},{"text":"Taken together, our results show that FKBP8 mediates LIR‐dependent recruitment of LC3A to damaged mitochondria.","type":"Results"},{"text":"Importantly, the mitochondrial acidification was LIR dependent, and enhanced when FKBP8 was specifically targeted to the mitochondria (Fig 5B).","type":"Results"},{"text":"We find here that FKBP8 promotes mitophagy by LIR‐dependent recruitment of LC3A, independent of the PINK1‐Parkin pathway.","type":"Discussion"},{"text":"LIR motif coresponds to the 24-27 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of macromitophagy.\" [GOC:TermGenie]","term_is_obsolete":false,"term_not_annotate":false},{"start":23,"end":28,"reference_id":"31908024","reference_source":"pmid","reference_html":"FKBP8 LIRL-dependent mitochondrial fragmentation facilitates mitophagy under stress conditions. <i> Yoo SM, Yamashita SI, Kim H, Na D, Lee H, Kim SJ, Cho DH, Kanki T, Jung YK. </i> FASEB J, 2020","date":"2023-09-27T13:06:43.839Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1901524","term_name":"regulation of mitophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"ec_go":"IDA","region_id":"DP03659r014","statement":[{"text":"These two FKBP8 mutants all showed an impaired ability to degrade mitochondria under normoxic and hypoxic conditions (Figure 5F,G,H).","type":"Results"},{"text":"LIR motif coresponds to the 24-27 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of macromitophagy.\" [GOC:TermGenie]","term_is_obsolete":false,"term_not_annotate":false},{"start":23,"end":28,"reference_id":"31908024","reference_source":"pmid","reference_html":"FKBP8 LIRL-dependent mitochondrial fragmentation facilitates mitophagy under stress conditions. <i> Yoo SM, Yamashita SI, Kim H, Na D, Lee H, Kim SJ, Cho DH, Kanki T, Jung YK. </i> FASEB J, 2020","date":"2022-05-23T20:33:23.221Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9GZQ8","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP03659r015","statement":[{"text":"Expression analysis of those mutants revealed that FKBP8 LIR mutant failed to bind to GFP-LC3B and recruit it onto the mitochondria (Figure 5B,C), consistent with the previous report.","type":"Results"},{"text":"LIR motif coresponds to the 24-27 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-25T09:45:45.996Z"}},{"start":23,"end":28,"reference_id":"31908024","reference_source":"pmid","reference_html":"FKBP8 LIRL-dependent mitochondrial fragmentation facilitates mitophagy under stress conditions. <i> Yoo SM, Yamashita SI, Kim H, Na D, Lee H, Kim SJ, Cho DH, Kanki T, Jung YK. </i> FASEB J, 2020","date":"2022-06-01T13:48:58.475Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0070585","term_name":"protein localization to mitochondrion","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","region_id":"DP03659r016","statement":[{"text":"Expression analysis of those mutants revealed that FKBP8 LIR mutant failed to bind to GFP-LC3B and recruit it onto the mitochondria (Figure 5B,C), consistent with the previous report.","type":"Results"},{"text":"LIR motif coresponds to the 24-27 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"A process in which a protein is transported to, or maintained in, a location within the mitochondrion.\" [GOC:ecd]","term_is_obsolete":false,"term_not_annotate":false,"annotation_extensions":[{"operator":null,"relation":"occurs_in","value":"0005739"}],"interaction_partner":[{"db":"UniProt","id":"Q9GZQ8","operator":null,"partner_start":null,"partner_end":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-01T14:14:07.412Z"}}],"regions_counter":16,"released":"2022_06","sequence":"MASCAEPSEPSAPLPAGVPPLEDFEVLDGVEDAEGEEEEEEEEEEEDDLSELPPLEDMGQPPAEEAEQPGALAREFLAAMEPEPAPAPAPEEWLDILGNGLLRKKTLVPGPPGSSRPVKGQVVTVHLQTSLENGTRVQEEPELVFTLGDCDVIQALDLSVPLMDVGETAMVTADSKYCYGPQGRSPYIPPHAALCLEVTLKTAVDGPDLEMLTGQERVALANRKRECGNAHYQRADFVLAANSYDLAIKAITSSAKVDMTFEEEAQLLQLKVKCLNNLAASQLKLDHYRAALRSCSLVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILRAALKLEPSNKTIHAELSKLVKKHAAQRSTETALYRKMLGNPSRLPAKCPGKGAWSIPWKWLFGATAVALGGVALSVVIAARN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"FKBP8"},"synonyms":[{"value":"FKBP38"}]}],"alphafold_very_low_content":0.20388349514563106,"disorder_content":0.17718446601941748,"disprot_consensus":{"full":[{"start":1,"end":34,"type":"D"},{"start":151,"end":165,"type":"D"},{"start":357,"end":380,"type":"D"}],"Structural state":[{"start":1,"end":34,"type":"D"},{"start":151,"end":165,"type":"D"},{"start":357,"end":380,"type":"D"}],"Molecular function":[{"start":1,"end":34,"type":"F"}],"Disorder function":[{"start":1,"end":32,"type":"F"}],"Biological process":[{"start":23,"end":28,"type":"F"}]}},{"disprot_id":"DP03660","acc":"A0A5F9ZHA1","creator":"vnugnes","date":"2022-05-23T08:29:17.463Z","features":{"pfam":[{"id":"PF00023","name":"Ankyrin repeat","start":108,"end":134},{"id":"PF00023","name":"Ankyrin repeat","start":310,"end":340},{"id":"PF00023","name":"Ankyrin repeat","start":542,"end":566},{"id":"PF00023","name":"Ankyrin repeat","start":674,"end":704},{"id":"PF00531","name":"Death domain","start":1432,"end":1512},{"id":"PF00791","name":"ZU5 domain","start":949,"end":1046},{"id":"PF00791","name":"ZU5 domain","start":1107,"end":1184},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":16,"end":105},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":236,"end":302},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":373,"end":440},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":447,"end":533},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":602,"end":668},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":731,"end":792},{"id":"PF13606","name":"Ankyrin repeat","start":344,"end":372},{"id":"PF13637","name":"Ankyrin repeats (many copies)","start":175,"end":232},{"id":"PF17809","name":"UPA domain","start":1270,"end":1399}],"gene3D":[]},"length":1849,"name":"Ankyrin-2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1403,"end":1430,"reference_id":"22411828","reference_source":"pmid","reference_html":"Structure of the ZU5-ZU5-UPA-DD tandem of ankyrin-B reveals interaction surfaces necessary for ankyrin function. <i> Wang C, Yu C, Ye F, Wei Z, Zhang M. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-05-26T12:39:11.332Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ser1190del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"After extensive trials, we discovered that the deletion of a nine-residue fragment in a solvent-exposed loop of ZU5C (Figs. 1A and ​2) enabled us to obtain high diffraction-quality crystals of ZZUD."},{"type":"Supplementary material","text":"The ZZUD mutant used for crystallization with the nine-residue deletion (1211SDVMLNGFG1219) was created using the standard PCRbased mutagenesis method."}]},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Asp1191del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Val1192del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1193del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Leu1194del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Asn1195del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gly1196del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Phe1197del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gly1198del","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"4D8O"}],"region_id":"DP03660r001","sequence_construct":"MHHHHHHSSGLEVLFQGPEFSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNT","statement":[{"text":"The final structural model contains most of residues from ankyrin-B ZZUD except for a few flexible loops (Fig. 1A)","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T12:55:20.296Z"}},{"start":1403,"end":1430,"reference_id":"22411828","reference_source":"pmid","reference_html":"Structure of the ZU5-ZU5-UPA-DD tandem of ankyrin-B reveals interaction surfaces necessary for ankyrin function. <i> Wang C, Yu C, Ye F, Wei Z, Zhang M. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-05-26T12:38:04.132Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ser1190del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"After extensive trials, we discovered that the deletion of a nine-residue fragment in a solvent-exposed loop of ZU5C (Figs. 1A and ​2) enabled us to obtain high diffraction-quality crystals of ZZUD."},{"type":"Supplementary material","text":"The ZZUD mutant used for crystallization with the nine-residue deletion (1211SDVMLNGFG1219) was created using the standard PCRbased mutagenesis method."}]},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Asp1191del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Val1192del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1193del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Leu1194del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Asn1195del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gly1196del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Phe1197del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gly1198del","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"4D8O"}],"region_id":"DP03660r002","sequence_construct":"MHHHHHHSSGLEVLFQGPEFSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNT","statement":[{"text":"The final structural model contains most of residues from ankyrin-B ZZUD except for a few flexible loops (Fig. 1A)","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T12:55:38.987Z"}},{"start":1059,"end":1068,"reference_id":"22411828","reference_source":"pmid","reference_html":"Structure of the ZU5-ZU5-UPA-DD tandem of ankyrin-B reveals interaction surfaces necessary for ankyrin function. <i> Wang C, Yu C, Ye F, Wei Z, Zhang M. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-05-26T12:38:30.455Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ser1190del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"After extensive trials, we discovered that the deletion of a nine-residue fragment in a solvent-exposed loop of ZU5C (Figs. 1A and ​2) enabled us to obtain high diffraction-quality crystals of ZZUD."},{"type":"Supplementary material","text":"The ZZUD mutant used for crystallization with the nine-residue deletion (1211SDVMLNGFG1219) was created using the standard PCRbased mutagenesis method."}]},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Asp1191del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Val1192del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1193del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Leu1194del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Asn1195del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gly1196del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Phe1197del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gly1198del","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"4D8O"}],"region_id":"DP03660r003","sequence_construct":"MHHHHHHSSGLEVLFQGPEFSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNT","statement":[{"text":"The final structural model contains most of residues from ankyrin-B ZZUD except for a few flexible loops (Fig. 1A)","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T12:55:40.624Z"}},{"start":1059,"end":1068,"reference_id":"22411828","reference_source":"pmid","reference_html":"Structure of the ZU5-ZU5-UPA-DD tandem of ankyrin-B reveals interaction surfaces necessary for ankyrin function. <i> Wang C, Yu C, Ye F, Wei Z, Zhang M. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-05-26T12:37:21.199Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ser1190del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"After extensive trials, we discovered that the deletion of a nine-residue fragment in a solvent-exposed loop of ZU5C (Figs. 1A and ​2) enabled us to obtain high diffraction-quality crystals of ZZUD."},{"type":"Supplementary material","text":"The ZZUD mutant used for crystallization with the nine-residue deletion (1211SDVMLNGFG1219) was created using the standard PCRbased mutagenesis method."}]},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Asp1191del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Val1192del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1193del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Leu1194del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Asn1195del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gly1196del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Phe1197del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gly1198del","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"4D8O"}],"region_id":"DP03660r004","sequence_construct":"MHHHHHHSSGLEVLFQGPEFSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNT","statement":[{"text":"The final structural model contains most of residues from ankyrin-B ZZUD except for a few flexible loops (Fig. 1A)","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T12:55:23.323Z"}},{"start":796,"end":852,"reference_id":"25383926","reference_source":"pmid","reference_html":"Structural basis of diverse membrane target recognitions by ankyrins.  <i> Wang C, Wei Z, Chen K, Ye F, Yu C, Bennett V, Zhang M. </i> Elife, 2014","date":"2022-05-23T13:25:57.949Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"DisProt","id":"DP03650r005"},{"db":"PDB","id":"4RLV"}],"region_id":"DP03660r005","statement":[{"text":"IDR is 100% identical.","type":"Curator statement"}],"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":31,"end":31,"position":"Specific residue","statements":[{"type":"Curator statement","text":"The residues 31, 34, 37, 173, 261, 262, 318, 375, 451, 478, 507, 557, 679, 714, 727, 780, 876, 891 of the exact sequence from the experimentwere replaced with selenomethionine."}]}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"sequence_construct":"GPGSEFCADQYWNEVAVIDAIPLAATEHDTMLEMSDMQVWSAGLTPSLVTAEDSGSLVPRGSGSKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKMMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDD","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-24T12:42:44.527Z"}},{"start":662,"end":672,"reference_id":"28841137","reference_source":"pmid","reference_html":"Autoinhibition of ankyrin-B/G membrane target bindings by intrinsically disordered segments from the tail regions.  <i> Chen K, Li J, Wang C, Wei Z, Zhang M. </i> Elife, 2017","date":"2022-05-23T13:24:07.845Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"DisProt","id":"DP03650r007"},{"db":"PDB","id":"5Y4D"}],"region_id":"DP03660r006","statement":[{"text":"IDR is 100% identical.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"sequence_construct":"GPGSEFCADQYWNEVAVIDAIPLAATEHDTMLEMSDMQVWSAGDHPPIVSEEDISGSLVPRGSGSKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKMMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTK","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-24T12:51:50.055Z"}},{"start":825,"end":852,"reference_id":"28841137","reference_source":"pmid","reference_html":"Autoinhibition of ankyrin-B/G membrane target bindings by intrinsically disordered segments from the tail regions.  <i> Chen K, Li J, Wang C, Wei Z, Zhang M. </i> Elife, 2017","date":"2022-05-23T13:23:22.792Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"DisProt","id":"DP03650r006"},{"db":"PDB","id":"5Y4F"}],"region_id":"DP03660r007","statement":[{"text":"IDR is 100% identical.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30089","entry_name":"acetate"}],"sequence_construct":"SGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGD","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-24T12:51:48.334Z"}},{"start":1189,"end":1201,"reference_id":"32353364","reference_source":"pmid","reference_html":"Structural Basis Underlying Strong Interactions between Ankyrins and Spectrins. <i> Li J, Chen K, Zhu R, Zhang M. </i> J Mol Biol, 2020","date":"2022-05-23T13:17:00.321Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"DisProt","id":"DP03650r008"},{"db":"PDB","id":"6M3Q"}],"region_id":"DP03660r008","statement":[{"text":"IDR is 100% identical.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-24T14:04:44.225Z"}}],"regions_counter":8,"released":"2022_06","sequence":"MTTMLQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKMMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDDSLPSSQFLDGMNYLRYSLEGGRSDSLRSFSSDRSHTLSHASYLRDSAVMDDSVVIPSHQVSTLAKEAERNSYRLSWGTENLDNVALSSSPIHSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASSDVMLNGFGGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNTEPLQERISHSYAEIEQTITLDHSEGFSVLQEELCTAQHKQKEEQAVSKESETCDHPPIVSEEDISVGYSTFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTETSETQKAMIVPSSPSKTPEEVSTPAEEEKLYLQTPTSSERGGSPIIQEPEEPSEHREESSPRKTSLVIVESADNQPETCERLDEDAAFEKELTEELGELEASSDEEAMVTTRVVRRRVIIQGDDMPEIPPETVTEEEYIDEHGHTVVKKVTRKIIRRYVSSEGTEKEEIMVQGMPQEPVNIEEGDGYSKVIKRVVLKSDTEQSEDNNE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"ANK2","evidences":[{"code":"ECO:0000313","source":{"name":"Ensembl","id":"ENSP00000500150","url":"https://www.ensembl.org/id/ENSP00000500150"}}]}}],"disorder_content":0.06435911303407248,"disprot_consensus":{"full":[{"start":662,"end":672,"type":"D"},{"start":796,"end":852,"type":"D"},{"start":1059,"end":1068,"type":"D"},{"start":1189,"end":1201,"type":"D"},{"start":1403,"end":1430,"type":"D"}],"Structural state":[{"start":662,"end":672,"type":"D"},{"start":796,"end":852,"type":"D"},{"start":1059,"end":1068,"type":"D"},{"start":1189,"end":1201,"type":"D"},{"start":1403,"end":1430,"type":"D"}],"Disorder function":[{"start":1059,"end":1068,"type":"F"},{"start":1403,"end":1430,"type":"F"}]}},{"disprot_id":"DP03661","acc":"Q9BY41","creator":"vacs","date":"2022-05-23T13:13:21.567Z","features":{"pfam":[{"id":"PF00850","name":"Histone deacetylase domain","start":35,"end":320}],"gene3D":[]},"length":377,"name":"Histone deacetylase 8","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":12,"reference_id":"21790156","reference_source":"pmid","reference_html":"Structural basis of the antiproliferative activity of largazole, a depsipeptide inhibitor of the histone deacetylases. <i> Cole KE, Dowling DP, Boone MA, Phillips AJ, Christianson DW. </i> J Am Chem Soc, 2011","date":"2022-05-23T13:15:03.899Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3RQD"}],"region_id":"DP03661r001","statement":[{"text":"Disordered segments in the final model include M1-S13, E85-I94, and I378-H389 in monomer A, and M1-Q12, Q84-S93, and E379-H389 in monomer B.","type":"Supplementary material"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-24T14:06:17.272Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MEEPEEPADSGQSLVPVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"HDAC8","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10926844","url":"http://www.ncbi.nlm.nih.gov/pubmed/10926844","alternativeUrl":"https://europepmc.org/abstract/MED/10926844"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:13315","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:13315"}}]},"synonyms":[{"value":"HDACL1"}],"orfNames":[{"value":"CDA07"}]}],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.029177718832891247,"disorder_content":0.03183023872679045,"disprot_consensus":{"full":[{"start":1,"end":12,"type":"D"}],"Structural state":[{"start":1,"end":12,"type":"D"}]}},{"disprot_id":"DP03662","acc":"P0AB71","creator":"vacs","date":"2022-05-24T07:43:19.086Z","features":{"pfam":[{"id":"PF01116","name":"Fructose-bisphosphate aldolase class-II","start":17,"end":355}],"gene3D":[]},"length":359,"name":"Fructose-bisphosphate aldolase class 2","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":178,"end":194,"reference_id":"8939754","reference_source":"pmid","reference_html":"The crystal structure of a class II fructose-1,6-bisphosphate aldolase shows a novel binuclear metal-binding active site embedded in a familiar fold. <i> Cooper SJ, Leonard GA, McSweeney SM, Thompson AW, Naismith JH, Qamar S, Plater A, Berry A, Hunter WN. </i> Structure, 1996","date":"2022-05-24T07:46:08.688Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1ZEN"}],"region_id":"DP03662r001","statement":[{"text":"The model consists of three polypeptide segments, residues 1–176, 194–228 and 230–356. There is no convincing electron density for residues 177–193, 229 or the last two residues in the sequence.","type":"Results"},{"text":"We were never able to locate the remaining selenium, Met190, as it is located on a flexible loop.","type":"Methods"},{"text":"The IDR characterized in the publication and spanning residues 177-193 corresponds to region 178-194 of the amino acid sequence, since the N-terminal methionine is removed from the protein.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-25T10:24:25.077Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MSKIFDFVKPGVITGDDVQKVFQVAKENNFALPAVNCVGTDSINAVLETAAKVKAPVIVQFSNGGASFIAGKGVKSDVPQGAAILGAISGAHHVHQMAEHYGVPVILHTDHCAKKLLPWIDGLLDAGEKHFAATGKPLFSSHMIDLSEESLQENIEICSKYLERMSKIGMTLEIELGCTGGEEDGVDNSHMDASALYTQPEDVDYAYTELSKISPRFTIAASFGNVHGVYKPGNVVLTPTILRDSQEYVSKKHNLPHNSLNFVFHGGSGSTAQEIKDSVSYGVVKMNIDTDTQWATWEGVLNYYKANEAYLQGQLGNPKGEDQPNKKYYDPRVWLRAGQTSMIARLEKAFQELNAIDVL","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"genes":[{"name":{"value":"fbaA"},"synonyms":[{"value":"fba"},{"value":"fda"}],"olnNames":[{"value":"b2925"},{"value":"JW2892"}]}],"alphafold_very_low_content":0.005571030640668524,"disorder_content":0.04735376044568245,"disprot_consensus":{"full":[{"start":178,"end":194,"type":"D"}],"Structural state":[{"start":178,"end":194,"type":"D"}]}},{"disprot_id":"DP03663","acc":"P0A9I5","creator":"vacs","date":"2022-05-24T09:58:21.281Z","features":{"pfam":[{"id":"PF03927","name":"NapD protein","start":5,"end":81}],"gene3D":[]},"length":87,"name":"Chaperone NapD","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":76,"end":87,"reference_id":"17901208","reference_source":"pmid","reference_html":"Structural diversity in twin-arginine signal peptide-binding proteins. <i> Maillard J, Spronk CA, Buchanan G, Lyall V, Richardson DJ, Palmer T, Vuister GW, Sargent F. </i> Proc Natl Acad Sci U S A, 2007","date":"2022-05-24T10:04:26.288Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"BMRB","id":"15381"},{"db":"PDB","id":"2JSX"}],"region_id":"DP03663r001","statement":[{"text":"No resonance assignments were obtained for residues 1, 2, 79, 80, and the C-terminal His tag residues 89–95 because of chemical exchange and flexibility of the N- and C-terminal parts of the NapD structure.","type":"Results"},{"text":"The final β-strand in the NapD fold (residues 69–75) was followed by a flexible, unstructured, carboxyl-terminal tail.","type":"Results"},{"text":"The residues that were least affected upon peptide binding were, in general, localized within the α-helical and turn regions (residues 53–69 and 17–31) on the opposite side of the molecule, or within the flexible C terminus, consistent with the peptide-binding site being located within the β-sheet.","type":"Figure"},{"text":"Of residues 3–78 (backbone rmsd, 1.25 Å), the core region containing the secondary structure elements (residues 6–75) is well defined (backbone rmsd, 0.63 Å) and deemed suitable for detailed structural analysis (Table 1).","type":"Methods"},{"text":"However, the C-terminally truncated NapD (DC-term), which is lacking the final 10 very flexible residues, was partially compromised in its physiological activity, suggesting that the unstructured C-tail may have role in NapD function.","type":"Supplementary material"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-25T10:26:28.984Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MHTNWQVCSLVVQAKSERISDISTQLNAFPGCEVAVSDAPSGQLIVVVEAEDSETLIQTIESVRNVEGVLAVSLVYHQQEEQGEETP","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"genes":[{"name":{"value":"napD","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_02200","url":"https://hamap.expasy.org/unirule/MF_02200"}}]},"synonyms":[{"value":"yojF"}],"olnNames":[{"value":"b2207"},{"value":"JW2195"}]}],"alphafold_very_low_content":0.09195402298850575,"disorder_content":0.13793103448275862,"disprot_consensus":{"full":[{"start":76,"end":87,"type":"D"}],"Structural state":[{"start":76,"end":87,"type":"D"}]}},{"disprot_id":"DP03664","acc":"P0C1C6","creator":"ewagner","date":"2022-05-24T13:12:43.091Z","features":{"pfam":[{"id":"PF14313","name":"N-terminal region of Paramyxovirinae phosphoprotein (P)","start":5,"end":51},{"id":"PF14320","name":"Phosphoprotein P region PNT disordered","start":71,"end":381}],"gene3D":[]},"length":448,"name":"Protein W","ncbi_taxon_id":928303,"organism":"Hendra virus (isolate Horse/Autralia/Hendra/1994)","regions":[{"start":1,"end":448,"reference_id":"35055108","reference_source":"pmid","reference_html":"Experimental Evidence of Intrinsic Disorder and Amyloid Formation by the Henipavirus W Proteins.  <i> Pesce G, Gondelaud F, Ptchelkine D, Nilsson JF, Bignon C, Cartalas J, Fourquet P, Longhi S. </i> Int J Mol Sci, 2022","date":"2022-05-25T17:19:10.216Z","curator_id":"slonghi","curator_name":"Sonia Longhi","curator_orcid":"0000-0002-6829-6771","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03664r001","statement":[{"text":"Under native conditions and neutral pH, both spectra display a large negative peak centered at 200 nm, low intensity in the 220–230 nm region, and low ellipticity at 190 nm (Figure 8A). The spectra are typical of disordered proteins lacking any stable organized secondary structure. For both proteins, spectral deconvolution revealed a high content (about 60%) of unordered structure along with a ~20% content in β-strands (Figure 8B).","type":"Results"},{"text":"According to their ellipticity values at 200 and 222 nm, both W proteins fall in the PMG-like region of the plot (Figure 8C). These results confirm the hints obtained from SEC experiments and support the classification of the W proteins within the PMG-like sub-family of IDPs.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T07:22:49.507Z"}},{"start":1,"end":448,"reference_id":"35055108","reference_source":"pmid","reference_html":"Experimental Evidence of Intrinsic Disorder and Amyloid Formation by the Henipavirus W Proteins.  <i> Pesce G, Gondelaud F, Ptchelkine D, Nilsson JF, Bignon C, Cartalas J, Fourquet P, Longhi S. </i> Int J Mol Sci, 2022","date":"2022-05-25T16:58:07.284Z","curator_id":"slonghi","curator_name":"Sonia Longhi","curator_orcid":"0000-0002-6829-6771","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"SASBDB","id":"SASDLK9"}],"region_id":"DP03664r002","statement":[{"text":"The pairiwse distance distribution, P(r), yielded a maximal dimension, Dmax, of ~240 Å for HeV and ~245 Å for NiV W (Supplementary Figure S6C) with a long tail in the P(r) function, indicating that the proteins assume an overall non-compact conformation [69].","type":"Results"},{"text":"The flexible nature of the W proteins was also qualitatively assessed using the Kratky- Debye and the normalized Kratky plots (Figure 10C,D). The presence of a plateau in the Kratky-Debye plot (Figure 10C) and the shape of the normalized Kratky plot (with no clear maximum) (Figure 10D) indicate that the W proteins are intrinsically disordered.","type":"Results"},{"text":"For both proteins, the resulting final Rg (Figure 10E,F) and Dmax (Supplementary Figure S6D) distributions, are unimodal and close to those of the initial pool, indicating that the W proteins exist in solution as randomly distributed ensembles of non-compact and highly flexible conformations.","type":"Results"},{"text":"In conjunction with all the other experimental lines of evidence presented above, SAXS data definitely demonstrate that the W proteins are intrinsically disordered.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T07:22:47.356Z"}},{"start":1,"end":448,"reference_id":"35055108","reference_source":"pmid","reference_html":"Experimental Evidence of Intrinsic Disorder and Amyloid Formation by the Henipavirus W Proteins.  <i> Pesce G, Gondelaud F, Ptchelkine D, Nilsson JF, Bignon C, Cartalas J, Fourquet P, Longhi S. </i> Int J Mol Sci, 2022","date":"2022-05-25T17:19:20.140Z","curator_id":"slonghi","curator_name":"Sonia Longhi","curator_orcid":"0000-0002-6829-6771","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03664r003","statement":[{"text":"From the elution volume of the major species (16.0 ± 0.08 mL for HeV W and 16.1 ± 0.07 mL for NiV W), as obtained using HBS as elution buffer, the corresponding RS was estimated to be 51.0±0.9Å for HeVW and 50.1±0.8Å for NiVW (Table2). By comparing the mean measured Stokes radius (Rsobs) for HeV and NiV W with the theoretical Stokes radii expected for various conformational states (RsNF: natively folded protein; RSPMG: expected for a PMG; RsU: fully unfolded form; RSIDP: expected for an IDP), the two proteins were found to have RS values ~1.7 times larger than the value expected for a natively folded protein, and close to the one expected for a PMG (Table 2). ","type":"Results"},{"text":"These results, while providing additional experimental evidence for the prevalently disordered nature of both W proteins, indicate the presence of some transiently populated secondary and/or tertiary structure typical of the PMG state, also supported by the expansion effect observed in the presence of urea. ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T07:22:45.338Z"}},{"start":1,"end":448,"reference_id":"35055108","reference_source":"pmid","reference_html":"Experimental Evidence of Intrinsic Disorder and Amyloid Formation by the Henipavirus W Proteins.  <i> Pesce G, Gondelaud F, Ptchelkine D, Nilsson JF, Bignon C, Cartalas J, Fourquet P, Longhi S. </i> Int J Mol Sci, 2022","date":"2022-05-25T17:19:43.914Z","curator_id":"slonghi","curator_name":"Sonia Longhi","curator_orcid":"0000-0002-6829-6771","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006301","ec_ontology":"ECO","ec_name":"protein thermal shift assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03664r004","statement":[{"text":"The experimentally observed profile obtained for both the W proteins does not feature any transition peak, consistent with the lack of a stable 3D structure (Figure 6). These results provide additional support for an overall disordered nature of the W proteins, in line with the in-silico analyses and with the above-described experimental lines of evidence.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T07:22:43.871Z"}},{"start":1,"end":448,"reference_id":"35055108","reference_source":"pmid","reference_html":"Experimental Evidence of Intrinsic Disorder and Amyloid Formation by the Henipavirus W Proteins.  <i> Pesce G, Gondelaud F, Ptchelkine D, Nilsson JF, Bignon C, Cartalas J, Fourquet P, Longhi S. </i> Int J Mol Sci, 2022","date":"2022-05-25T17:19:29.552Z","curator_id":"slonghi","curator_name":"Sonia Longhi","curator_orcid":"0000-0002-6829-6771","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001191","ec_ontology":"ECO","ec_name":"in vitro cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03664r005","statement":[{"text":"As shown in Figure 5, both proteins start to be degraded after 5 minutes of incubation and are extensively degraded after 45 minutes, a behavior that is consistent with the lack of a packed core and with an overall solvent accessibility. ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T07:22:42.592Z"}},{"start":1,"end":448,"reference_id":"35055108","reference_source":"pmid","reference_html":"Experimental Evidence of Intrinsic Disorder and Amyloid Formation by the Henipavirus W Proteins.  <i> Pesce G, Gondelaud F, Ptchelkine D, Nilsson JF, Bignon C, Cartalas J, Fourquet P, Longhi S. </i> Int J Mol Sci, 2022","date":"2022-05-25T17:18:38.498Z","curator_id":"slonghi","curator_name":"Sonia Longhi","curator_orcid":"0000-0002-6829-6771","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03664r006","statement":[{"text":"As shown in Figure 4A, B the final purified W proteins migrate with an apparent molecular mass of ~65 kDa, a value 1.2 times higher than the one expected from the amino acid sequence (~53 kDa). ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T07:22:41.679Z"}},{"start":1,"end":448,"reference_id":"35055108","reference_source":"pmid","reference_html":"Experimental Evidence of Intrinsic Disorder and Amyloid Formation by the Henipavirus W Proteins.  <i> Pesce G, Gondelaud F, Ptchelkine D, Nilsson JF, Bignon C, Cartalas J, Fourquet P, Longhi S. </i> Int J Mol Sci, 2022","date":"2022-05-25T17:24:00.811Z","curator_id":"slonghi","curator_name":"Sonia Longhi","curator_orcid":"0000-0002-6829-6771","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007044","ec_ontology":"ECO","ec_name":"transmission electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP03664r007","statement":[{"text":"Finally, we analyzed the purified W proteins using negative-staining TEM, which unambiguously revealed the presence of fibrils for both HeV and NiV W (Figure 12). ","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T07:22:51.188Z"}},{"start":1,"end":448,"reference_id":"29321677","reference_source":"pmid","reference_html":"Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V. <i> Atkinson SC, Audsley MD, Lieu KG, Marsh GA, Thomas DR, Heaton SM, Paxman JJ, Wagstaff KM, Buckle AM, Moseley GW, Jans DA, Borg NA. </i> Sci Rep, 2018","date":"2024-04-08T13:53:24.224Z","curator_id":"ewagner","curator_name":"Evelyn Wagner","curator_orcid":"0000-0003-4791-7249","term_id":"GO:1901344","term_name":"response to leptomycin B","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007060","ec_ontology":"ECO","ec_name":"confocal laser scanning microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IDA","region_id":"DP03664r008","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0059","entry_name":"Verda reno"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"52646","entry_name":"leptomycin B"}],"statement":[{"text":"As per V, the nuclear localization of HeV W also increased following LMB treatment (p < 0.0001) (Fig. 1a,b), but in contrast the localization of HeV P remained unchanged following LMB treatment (Fig. 1a,b). Thus, the nucleocytoplasmic localization of HeV V and W, but not P, is dependent on an exportin-1-dependent nuclear export sequence (NES).","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a leptomycin B stimulus.\" [GOC:TermGenie]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-08T17:53:39.167Z"}},{"start":1,"end":448,"reference_id":"29321677","reference_source":"pmid","reference_html":"Recognition by host nuclear transport proteins drives disorder-to-order transition in Hendra virus V. <i> Atkinson SC, Audsley MD, Lieu KG, Marsh GA, Thomas DR, Heaton SM, Paxman JJ, Wagstaff KM, Buckle AM, Moseley GW, Jans DA, Borg NA. </i> Sci Rep, 2018","date":"2024-04-08T17:48:02.971Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042025","term_name":"host cell nucleus","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007060","ec_ontology":"ECO","ec_name":"confocal laser scanning microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","region_id":"DP03664r009","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0059","entry_name":"Verda reno"}],"statement":[{"text":"In untreated cells, HeV P and V were excluded from the nucleus, whereas W showed strong nuclear localization, but was excluded from structures consistent with nucleoli (Fig. 1a,b).","type":"Results"}],"term_comment":"","term_def":"\"A membrane-bounded organelle as it is found in the host cell in which chromosomes are housed and replicated. The host is defined as the larger of the organisms involved in a symbiotic interaction.\" [GOC:pamgo_curators]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":9,"released":"2023_12","sequence":"MDKLDLVNDGLDIIDFIQKNQKEIQKTYGRSSIQQPSTKDRTRAWEDFLQSTSGEHEQAEGGMPKNDGGTEGRNVEDLSSVTSSDGTIGQRVSNTRAWAEDPDDIQLDPMVTDVVYHDHGGECTGHGPSSSPERGWSYHMSGTHDGNVRAVPDTKVLPNAPKTTVPEEVREIDLIGLEDKFASAGLNPAAVPFVPKNQSTPTEEPPVIPEYYYGSGRRGDLSKSPPRGNVNLDSIKIYTSDDEDENQLEYEDEFAKSSSEVVIDTTPEDNDSINQEEVVGDPSDQGLEHPFPLGKFPEKEETPDVRRKDSLMQDSCKRGGVPKRLPMLSEEFECSGSDDPIIQELEREGSHPGGSLRLREPPQSSGNSRNQPDRQLKTGDAASPGGVQRPGTPMPKSRIMPIKKGAQTRSLNMLGRKTCLGRRVVQPGMFADYPPTKKARVLLRRMSN","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Paramyxoviridae","Orthoparamyxovirinae","Henipavirus"],"genes":[{"name":{"value":"P/V/C"}}],"dataset":["Viral proteins","Condensates-related proteins"],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":448,"type":"D"}],"Structural state":[{"start":1,"end":448,"type":"D"}],"Biological process":[{"start":1,"end":448,"type":"F"}],"Cellular component":[{"start":1,"end":448,"type":"F"}]}},{"disprot_id":"DP03665","acc":"P33734","creator":"vacs","date":"2022-05-24T13:51:18.450Z","features":{"pfam":[{"id":"PF00117","name":"Glutamine amidotransferase class-I","start":6,"end":210},{"id":"PF00977","name":"Histidine biosynthesis protein","start":239,"end":532}],"gene3D":[]},"length":552,"name":"Imidazole glycerol phosphate synthase hisHF","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":261,"end":275,"reference_id":"11591353","reference_source":"pmid","reference_html":"Crystal structure of imidazole glycerol phosphate synthase: a tunnel through a (beta/alpha)8 barrel joins two active sites. <i> Chaudhuri BN, Lange SC, Myers RS, Chittur SV, Davisson VJ, Smith JL. </i> Structure, 2001","date":"2022-05-24T13:53:44.390Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1JVN"}],"region_id":"DP03665r001","statement":[{"text":"Two exposed loops in the C-terminal cyclase domain (residues 261–275 and 301–304) are disordered and were not modeled.","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-25T10:38:08.723Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MPVVHVIDVESGNLQSLTNAIEHLGYEVQLVKSPKDFNISGTSRLILPGVGNYGHFVDNLFNRGFEKPIREYIESGKPIMGICVGLQALFAGSVESPKSTGLNYIDFKLSRFDDSEKPVPEIGWNSCIPSENLFFGLDPYKRYYFVHSFAAILNSEKKKNLENDGWKIAKAKYGSEEFIAAVNKNNIFATQFHPEKSGKAGLNVIENFLKQQSPPIPNYSAEEKELLMNDYSNYGLTRRIIACLDVRTNDQGDLVVTKGDQYDVREKSDGKGVRNLGKPVQLAQKYYQQGADEVTFLNITSFRDCPLKDTPMLEVLKQAAKTVFVPLTVGGGIKDIVDVDGTKIPALEVASLYFRSGADKVSIGTDAVYAAEKYYELGNRGDGTSPIETISKAYGAQAVVISVDPKRVYVNSQADTKNKVFETEYPGPNGEKYCWYQCTIKGGRESRDLGVWELTRACEALGAGEILLNCIDKDGSNSGYDLELIEHVKDAVKIPVIASSGAGVPEHFEEAFLKTRADACLGAGMFHRGEFTVNDVKEYLLEHGLKVRMDEE","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"genes":[{"name":{"value":"HIS7"},"orfNames":[{"value":"YBR1640"}],"olnNames":[{"value":"YBR248C"}]}],"alphafold_very_low_content":0.02717391304347826,"dataset":["Stress response proteins"],"disorder_content":0.02717391304347826,"disprot_consensus":{"full":[{"start":261,"end":275,"type":"D"}],"Structural state":[{"start":261,"end":275,"type":"D"}]}},{"disprot_id":"DP03666","acc":"Q12983","creator":"vnugnes","date":"2022-05-24T13:54:23.271Z","features":{"pfam":[{"id":"PF06553","name":"BNIP3","start":10,"end":193}],"gene3D":[]},"length":194,"name":"BCL2/adenovirus E1B 19 kDa protein-interacting protein 3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":146,"end":158,"reference_id":"17412696","reference_source":"pmid","reference_html":"Unique dimeric structure of BNip3 transmembrane domain suggests membrane permeabilization as a cell death trigger. <i> Bocharov EV, Pustovalova YE, Pavlov KV, Volynsky PE, Goncharuk MV, Ermolyuk YS, Karpunin DV, Schulga AA, Kirpichnikov MP, Efremov RG, Maslennikov IV, Arseniev AS. </i> J Biol Chem, 2007","date":"2022-05-24T14:16:12.519Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"2J5D"},{"db":"BMRB","id":"7288"}],"region_id":"DP03666r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q12983"}],"sequence_construct":"RNTSVMKKGGIFSAEFLKVFLPSLLLSHLLAIGLGIYIGRRLTTS","statement":[{"text":"Broken lines separate the unfolded regions 146–158 and 188–190 from the α-helical regions 159–165, 166–184, and 185–187 regions that have different flexibility.","type":"Figure"},{"text":"In contrast, the residues 146–158 and 188–190 from the N- and C termini, respectively, have nearly unrestricted mobility, resulting in low and negative 15N{1H} NOEs and decreased local rotation correlation times τR, estimated from the T1/T2 ratio (Fig. 3).","type":"Results"},{"text":"The residues 146-158 of the analized construct coresponds to the 211-223 region of the BCL2/adenovirus E1B 19 kDa protein-interacting protein 3.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-25T10:22:54.594Z"}}],"regions_counter":1,"released":"2022_06","sequence":"MSQNGAPGMQEESLQGSWVELHFSNNGNGGSVPASVSIYNGDMEKILLDAQHESGRSSSKSSHCDSPPRSQTPQDTNRASETDTHSIGEKNSSQSEEDDIERRKEVESILKKNSDWIWDWSSRPENIPPKEFLFKHPKRTATLSMRNTSVMKKGGIFSAEFLKVFLPSLLLSHLLAIGLGIYIGRRLTTSTSTF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"BNIP3","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:1084","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:1084"}}]},"synonyms":[{"value":"NIP3"}]}],"alphafold_very_low_content":0.3281853281853282,"disorder_content":0.06701030927835051,"disprot_consensus":{"full":[{"start":146,"end":158,"type":"D"}],"Structural state":[{"start":146,"end":158,"type":"D"}]}},{"disprot_id":"DP03667","acc":"P0C1C7","creator":"ewagner","date":"2022-05-25T11:01:44.641Z","features":{"pfam":[{"id":"PF14313","name":"N-terminal region of Paramyxovirinae phosphoprotein (P)","start":5,"end":52},{"id":"PF14320","name":"Phosphoprotein P region PNT disordered","start":71,"end":351}],"gene3D":[]},"length":450,"name":"Protein W","ncbi_taxon_id":121791,"organism":"Nipah virus","regions":[{"start":1,"end":450,"reference_id":"35055108","reference_source":"pmid","reference_html":"Experimental Evidence of Intrinsic Disorder and Amyloid Formation by the Henipavirus W Proteins.  <i> Pesce G, Gondelaud F, Ptchelkine D, Nilsson JF, Bignon C, Cartalas J, Fourquet P, Longhi S. </i> Int J Mol Sci, 2022","date":"2022-05-25T16:54:11.225Z","curator_id":"slonghi","curator_name":"Sonia Longhi","curator_orcid":"0000-0002-6829-6771","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03667r001","statement":[{"text":"Under native conditions and neutral pH, both spectra display a large negative peak centered at 200 nm, low intensity in the 220–230 nm region, and low ellipticity at 190 nm (Figure 8A). The spectra are typical of disordered proteins lacking any stable organized secondary structure. For both proteins, spectral deconvolution revealed a high content (about 60%) of unordered structure along with a ~20% content in β-strands (Figure 8B).","type":"Results"},{"text":"According to their ellipticity values at 200 and 222 nm, both W proteins fall in the PMG-like region of the plot (Figure 8C). These results confirm the hints obtained from SEC experiments and support the classification of the W proteins within the PMG-like sub-family of IDPs.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T07:23:05.456Z"}},{"start":1,"end":450,"reference_id":"35055108","reference_source":"pmid","reference_html":"Experimental Evidence of Intrinsic Disorder and Amyloid Formation by the Henipavirus W Proteins.  <i> Pesce G, Gondelaud F, Ptchelkine D, Nilsson JF, Bignon C, Cartalas J, Fourquet P, Longhi S. </i> Int J Mol Sci, 2022","date":"2022-05-25T11:30:32.434Z","curator_id":"slonghi","curator_name":"Sonia Longhi","curator_orcid":"0000-0002-6829-6771","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"SASBDB","id":"SASDLL9"}],"region_id":"DP03667r002","statement":[{"text":"The pairiwse distance distribution, P(r), yielded a maximal dimension, Dmax, of ~240 Å for HeV and ~245 Å for NiV W (Supplementary Figure S6C) with a long tail in the P(r) function, indicating that the proteins assume an overall non-compact conformation [69].","type":"Results"},{"text":"The flexible nature of the W proteins was also qualitatively assessed using the Kratky- Debye and the normalized Kratky plots (Figure 10C,D). The presence of a plateau in the Kratky-Debye plot (Figure 10C) and the shape of the normalized Kratky plot (with no clear maximum) (Figure 10D) indicate that the W proteins are intrinsically disordered.","type":"Results"},{"text":"For both proteins, the resulting final Rg (Figure 10E,F) and Dmax (Supplementary Figure S6D) distributions, are unimodal and close to those of the initial pool, indicating that the W proteins exist in solution as randomly distributed ensembles of non-compact and highly flexible conformations.","type":"Results"},{"text":"In conjunction with all the other experimental lines of evidence presented above, SAXS data definitely demonstrate that the W proteins are intrinsically disordered. ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T07:23:04.071Z"}},{"start":1,"end":450,"reference_id":"35055108","reference_source":"pmid","reference_html":"Experimental Evidence of Intrinsic Disorder and Amyloid Formation by the Henipavirus W Proteins.  <i> Pesce G, Gondelaud F, Ptchelkine D, Nilsson JF, Bignon C, Cartalas J, Fourquet P, Longhi S. </i> Int J Mol Sci, 2022","date":"2022-05-25T16:54:22.484Z","curator_id":"slonghi","curator_name":"Sonia Longhi","curator_orcid":"0000-0002-6829-6771","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006301","ec_ontology":"ECO","ec_name":"protein thermal shift assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03667r003","statement":[{"text":"The experimentally observed profile obtained for both the W proteins does not feature any transition peak, consistent with the lack of a stable 3D structure (Figure 6). These results provide additional support for an overall disordered nature of the W proteins, in line with the in-silico analyses and with the above-described experimental lines of evidence.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T07:23:03.306Z"}},{"start":1,"end":450,"reference_id":"35055108","reference_source":"pmid","reference_html":"Experimental Evidence of Intrinsic Disorder and Amyloid Formation by the Henipavirus W Proteins.  <i> Pesce G, Gondelaud F, Ptchelkine D, Nilsson JF, Bignon C, Cartalas J, Fourquet P, Longhi S. </i> Int J Mol Sci, 2022","date":"2022-05-25T16:54:29.861Z","curator_id":"slonghi","curator_name":"Sonia Longhi","curator_orcid":"0000-0002-6829-6771","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03667r004","statement":[{"text":"From the elution volume of the major species (16.0 ± 0.08 mL for HeV W and 16.1 ± 0.07 mL for NiV W), as obtained using HBS as elution buffer, the corresponding RS was estimated to be 51.0±0.9Å for HeVW and 50.1±0.8Å for NiVW (Table2). By comparing the mean measured Stokes radius (Rsobs) for HeV and NiV W with the theoretical Stokes radii expected for various conformational states (RsNF: natively folded protein; RSPMG: expected for a PMG; RsU: fully unfolded form; RSIDP: expected for an IDP), the two proteins were found to have RS values ~1.7 times larger than the value expected for a natively folded protein, and close to the one expected for a PMG (Table 2).","type":"Results"},{"text":"These results, while providing additional experimental evidence for the prevalently disordered nature of both W proteins, indicate the presence of some transiently populated secondary and/or tertiary structure typical of the PMG state, also supported by the expansion effect observed in the presence of urea. ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T07:22:59.592Z"}},{"start":1,"end":450,"reference_id":"35055108","reference_source":"pmid","reference_html":"Experimental Evidence of Intrinsic Disorder and Amyloid Formation by the Henipavirus W Proteins.  <i> Pesce G, Gondelaud F, Ptchelkine D, Nilsson JF, Bignon C, Cartalas J, Fourquet P, Longhi S. </i> Int J Mol Sci, 2022","date":"2022-05-25T11:34:05.830Z","curator_id":"slonghi","curator_name":"Sonia Longhi","curator_orcid":"0000-0002-6829-6771","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001191","ec_ontology":"ECO","ec_name":"in vitro cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"SASBDB","id":"SASDLL9"}],"region_id":"DP03667r005","statement":[{"text":"As shown in Figure 5, both proteins start to be degraded after 5 minutes of incubation and are extensively degraded after 45 minutes, a behavior that is consistent with the lack of a packed core and with an overall solvent accessibility. ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T07:22:58.479Z"}},{"start":1,"end":450,"reference_id":"35055108","reference_source":"pmid","reference_html":"Experimental Evidence of Intrinsic Disorder and Amyloid Formation by the Henipavirus W Proteins.  <i> Pesce G, Gondelaud F, Ptchelkine D, Nilsson JF, Bignon C, Cartalas J, Fourquet P, Longhi S. </i> Int J Mol Sci, 2022","date":"2022-05-25T17:24:20.101Z","curator_id":"slonghi","curator_name":"Sonia Longhi","curator_orcid":"0000-0002-6829-6771","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007044","ec_ontology":"ECO","ec_name":"transmission electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP03667r006","term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"statement":[{"text":"Finally, we analyzed the purified W proteins using negative-staining TEM, which unambiguously revealed the presence of fibrils for both HeV and NiV W (Figure 12). ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T07:23:06.256Z"}},{"start":1,"end":450,"reference_id":"35055108","reference_source":"pmid","reference_html":"Experimental Evidence of Intrinsic Disorder and Amyloid Formation by the Henipavirus W Proteins.  <i> Pesce G, Gondelaud F, Ptchelkine D, Nilsson JF, Bignon C, Cartalas J, Fourquet P, Longhi S. </i> Int J Mol Sci, 2022","date":"2022-05-25T17:16:11.537Z","curator_id":"slonghi","curator_name":"Sonia Longhi","curator_orcid":"0000-0002-6829-6771","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03667r007","statement":[{"text":"As shown in Figure 4A, B the final purified W proteins migrate with an apparent molecular mass of ~65 kDa, a value 1.2 times higher than the one expected from the amino acid sequence (~53 kDa). ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-26T07:22:57.514Z"}}],"regions_counter":7,"released":"2023_12","sequence":"MDKLELVNDGLNIIDFIQKNQKEIQKTYGRSSIQQPSIKDQTKAWEDFLQCTSGESEQVEGGMSKDDGDVERRNLEDLSSTSPTDGTIGKRVSNTRDWAEGSDDIQLDPVVTDVVYHDHGGECTGYGFTSSPERGWSDYTSGANNGNVCLVSDAKMLSYAPEIAVSKEDRETDLVHLENKLSTTGLNPTAVPFTLRNLSDPAKDSPVIAEHYYGLGVKEQNVGPQTSRNVNLDSIKLYTSDDEEADQLEFEDEFAGSSSEVIVGISPEDEEPSSVGGKPNESIGRTIEGQSIRDNLQAKDNKSTDVPGAGPKDSAVKEEPPQKRLPMLAEEFECSGSEDPIIRELLKENSLINCQQGKDAQPPYHWSIERSISPDKTEIVNGAVQTADRQRPGTPMPKSRGIPIKKGAQTRNIHLLGRKTCLGRRVVQPGMFEDHPPTKKARVSMRRMSN","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Paramyxoviridae","Orthoparamyxovirinae","Henipavirus"],"genes":[{"name":{"value":"P/V/C"}}],"dataset":["Viral proteins","Condensates-related proteins"],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":450,"type":"D"}],"Structural state":[{"start":1,"end":450,"type":"D"}],"Biological process":[{"start":1,"end":450,"type":"F"}]}},{"disprot_id":"DP03669","acc":"Q4LE39","creator":"cpintado","date":"2022-05-26T15:20:01.359Z","features":{"pfam":[{"id":"PF01388","name":"ARID/BRIGHT DNA binding domain","start":308,"end":394},{"id":"PF08169","name":"RBB1NT (NUC162) domain","start":170,"end":262},{"id":"PF11717","name":"RNA binding activity-knot of a chromodomain","start":572,"end":624}],"gene3D":[]},"length":1312,"name":"AT-rich interactive domain-containing protein 4B","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":110,"end":151,"reference_id":"33675746","reference_source":"pmid","reference_html":"Structural basis for the DNA-binding activity of human ARID4B Tudor domain. <i> Ren J, Yao H, Hu W, Perrett S, Gong W, Feng Y. </i> J Biol Chem, 2021","date":"2022-05-26T15:22:43.461Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7DM4"}],"region_id":"DP03669r001","statement":[{"text":"The structure determination, CSI analysis (19), and TALOS-N results all show that residues 110 to 151 are in fact in a disordered conformation (Fig. S1, B and C, and Fig. 2A).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-08T18:08:08.530Z"}},{"start":110,"end":151,"reference_id":"33675746","reference_source":"pmid","reference_html":"Structural basis for the DNA-binding activity of human ARID4B Tudor domain. <i> Ren J, Yao H, Hu W, Perrett S, Gong W, Feng Y. </i> J Biol Chem, 2021","date":"2022-07-15T09:06:50.797Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7DM4"}],"ec_go":"EXP","region_id":"DP03669r002","statement":[{"text":"Besides chemical shift perturbations, addition of dsDNA1 also enhanced NH signal intensities of C-terminal disordered residues of ARID4B TD151, mainly within the sequence 137-GKKTNRGRRS-146 (RGR motif, intensity ratio >3) and Gly110-Ile136 (3 > intensity ratio >1.5) (Fig. 3, D and E).","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-15T13:11:17.714Z"}},{"start":121,"end":151,"reference_id":"33675746","reference_source":"pmid","reference_html":"Structural basis for the DNA-binding activity of human ARID4B Tudor domain. <i> Ren J, Yao H, Hu W, Perrett S, Gong W, Feng Y. </i> J Biol Chem, 2021","date":"2022-07-15T09:11:26.705Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IMP","region_id":"DP03669r003","statement":[{"text":"ARID4B TD121 has an affinity (KD) of ∼110 μM for dsDNA1 estimated by fitting the NMR titration data (Fig. 4, A and B), about five times weaker than ARID4B TD151, which is consistent with the EMSA result. Similarly, the affinity of ARID4B TD121 for dsDNA2 obtained from titration was 237 μM, about three times weaker than ARID4B TD151 (KD 79 μM) (Fig. 4, C–F). Consistent with this, the affinity of ARID4A TD151 with dsDNA1 was measured as 9.7 μM (KD) (Fig. 4, G and H), about 2 to 3 times stronger than ARID4A TD121 (KD 27 μM) (15) and ARID4B TD151 (KD 22 μM). These results confirm that the C-terminal disordered region can enhance DNA-binding affinity of the Tudor domain.","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-15T13:12:11.371Z"}}],"regions_counter":3,"released":"2023_12","sequence":"MKALDEPPYLTVGTDVSAKYRGAFCEAKIKTAKRLVKVKVTFRHDSSTVEVQDDHIKGPLKVGAIVEVKNLDGAYQEAVINKLTDASWYTVVFDDGDEKTLRRSSLCLKGERHFAESETLDQLPLTNPEHFGTPVIGKKTNRGRRSNHIPEEESSSSSSDEDEDDRKQIDELLGKVVCVDYISLDKKKALWFPALVVCPDCSDEIAVKKDNILVRSFKDGKFTSVPRKDVHEITSDTAPKPDAVLKQAFEQALEFHKSRTIPANWKTELKEDSSSSEAEEEEEEEDDEKEKEDNSSEEEEEIEPFPEERENFLQQLYKFMEDRGTPINKRPVLGYRNLNLFKLFRLVHKLGGFDNIESGAVWKQVYQDLGIPVLNSAAGYNVKCAYKKYLYGFEEYCRSANIEFQMALPEKVVNKQCKECENVKEIKVKEENETEIKEIKMEEERNIIPREEKPIEDEIERKENIKPSLGSKKNLLESIPTHSDQEKEVNIKKPEDNENLDDKDDDTTRVDESLNIKVEAEEEKAKSGDETNKEEDEDDEEAEEEEEEEEEEEDEDDDDNNEEEEFECYPPGMKVQVRYGRGKNQKMYEASIKDSDVEGGEVLYLVHYCGWNVRYDEWIKADKIVRPADKNVPKIKHRKKIKNKLDKEKDKDEKYSPKNCKLRRLSKPPFQTNPSPEMVSKLDLTDAKNSDTAHIKSIEITSILNGLQASESSAEDSEQEDERGAQDMDNNGKEESKIDHLTNNRNDLISKEEQNSSSLLEENKVHADLVISKPVSKSPERLRKDIEVLSEDTDYEEDEVTKKRKDVKKDTTDKSSKPQIKRGKRRYCNTEECLKTGSPGKKEEKAKNKESLCMENSSNSSSDEDEEETKAKMTPTKKYNGLEEKRKSLRTTGFYSGFSEVAEKRIKLLNNSDERLQNSRAKDRKDVWSSIQGQWPKKTLKELFSDSDTEAAASPPHPAPEEGVAEESLQTVAEEESCSPSVELEKPPPVNVDSKPIEEKTVEVNDRKAEFPSSGSNSVLNTPPTTPESPSSVTVTEGSRQQSSVTVSEPLAPNQEEVRSIKSETDSTIEVDSVAGELQDLQSEGNSSPAGFDASVSSSSSNQPEPEHPEKACTGQKRVKDAQGGGSSSKKQKRSHKATVVNNKKKGKGTNSSDSEELSAGESITKSQPVKSVSTGMKSHSTKSPARTQSPGKCGKNGDKDPDLKEPSNRLPKVYKWSFQMSDLENMTSAERITILQEKLQEIRKHYLSLKSEVASIDRRRKRLKKKERESAATSSSSSSPSSSSITAAVMLTLAEPSMSSASQNGMSVECR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"ARID4B"},"synonyms":[{"value":"BRCAA1"},{"value":"RBBP1L1"},{"value":"RBP1L1"},{"value":"SAP180"}]}],"alphafold_very_low_content":0.614329268292683,"disorder_content":0.03201219512195122,"disprot_consensus":{"full":[{"start":110,"end":151,"type":"D"}],"Structural state":[{"start":110,"end":151,"type":"D"}],"Molecular function":[{"start":110,"end":151,"type":"F"}]}},{"disprot_id":"DP03670","acc":"P56962","creator":"vnugnes","date":"2022-05-26T18:29:35.363Z","features":{"pfam":[{"id":"PF05739","name":"SNARE domain","start":172,"end":228},{"id":"PF26585","name":"STX17-like, N-terminal domain","start":11,"end":110}],"gene3D":[]},"length":302,"name":"Syntaxin-17","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":142,"end":228,"reference_id":"32817423","reference_source":"pmid","reference_html":"Decoding three distinct states of the Syntaxin17 SNARE motif in mediating autophagosome-lysosome fusion. <i> Li Y, Cheng X, Li M, Wang Y, Fu T, Zhou Z, Wang Y, Gong X, Xu X, Liu J, Pan L. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-05-26T18:35:32.533Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03670r001","statement":[{"text":" It is noteworthy that the isolated SNARE region of STX17 is intrinsically disordered based on the CD analysis (Fig. 5A), consistent with the aforementioned NMR results (SI Appendix, Fig. S2).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T13:39:16.891Z"}},{"start":142,"end":228,"reference_id":"32817423","reference_source":"pmid","reference_html":"Decoding three distinct states of the Syntaxin17 SNARE motif in mediating autophagosome-lysosome fusion. <i> Li Y, Cheng X, Li M, Wang Y, Fu T, Zhou Z, Wang Y, Gong X, Xu X, Liu J, Pan L. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-05-26T18:38:43.892Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03670r002","statement":[{"text":"The small dispersion of the NMR peaks in the 1H dimension of the 1H-15N HSQC spectrum together with the determined secondary structure of this STX17 Qa-SNARE region based on the 13Cα and 13Cβ chemical shift values of each residue after backbone chemical shift assignments indicated that the isolated STX17 Qa-SNARE motif is basically unstructured (SI Appendix, Fig. S2).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T13:39:15.458Z"}},{"start":142,"end":228,"reference_id":"32817423","reference_source":"pmid","reference_html":"Decoding three distinct states of the Syntaxin17 SNARE motif in mediating autophagosome-lysosome fusion. <i> Li Y, Cheng X, Li M, Wang Y, Fu T, Zhou Z, Wang Y, Gong X, Xu X, Liu J, Pan L. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-05-26T18:50:57.251Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P56962","operator":null,"partner_start":1,"partner_end":123}],"region_id":"DP03670r003","statement":[{"text":"Interestingly, titration of the 15N-labeled STX17(142–228) with the unlabeled STX17(1–123) protein showed that a selected set of peaks in the 1H-15N HSQC spectrum of STX17(142–228) underwent significant dose-dependent peak broadening or chemical shift changes (Fig. 1B), indicating that the STX17 Qa-SNARE region can specifically interact with the N-terminal Habc domain of STX17. Further plotting of the peak broadening and amide backbone chemical shift changes as a function of residue number revealed that the significant perturbations are mainly rich in the N-terminal part of the STX17 Qa-SNARE motif (residues 174 to 194) (Fig. 1C), suggesting that this region is the major binding site for interacting with the STX17 Habc domain.","type":"Results"},{"text":"The 1H15N HSQC spectra of STX17 Habc domain saturated with STX17(167-215) and STX17(151-196) are almost identical to that with STX17(142-228), suggesting that STX17(167-196) contains the essential sequences for the binding with STX17 Habc domain.","type":"Supplementary material"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T13:39:31.175Z"}},{"start":94,"end":121,"reference_id":"32817423","reference_source":"pmid","reference_html":"Decoding three distinct states of the Syntaxin17 SNARE motif in mediating autophagosome-lysosome fusion. <i> Li Y, Cheng X, Li M, Wang Y, Fu T, Zhou Z, Wang Y, Gong X, Xu X, Liu J, Pan L. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-05-26T18:42:49.317Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03670r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P56962"}],"statement":[{"text":"Interestingly, we found that the newly appeared NMR peaks arose from residues 94 to 121, which are located in the predicted extreme C-terminal α-helix of the Habc domain (SI Appendix, Fig. S1A), but were demonstrated to be unstructured in the presence of STX17(142–228) based on our NMR analysis (SI Appendix, Fig. S4C).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T13:39:14.272Z"}},{"start":94,"end":121,"reference_id":"32817423","reference_source":"pmid","reference_html":"Decoding three distinct states of the Syntaxin17 SNARE motif in mediating autophagosome-lysosome fusion. <i> Li Y, Cheng X, Li M, Wang Y, Fu T, Zhou Z, Wang Y, Gong X, Xu X, Liu J, Pan L. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-05-26T19:39:43.051Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03670r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P56962"}],"statement":[{"text":"Taken together, all these data clearly demonstrated that the Qa-SNARE motif of STX17 can directly bind to the STX17 Habc domain and alter its conformation by partially unfolding its extreme C-terminal α-helix.","type":"Results"},{"text":"STX17 SNARE region is comprised by the 167-224 residues and the Habc domain by the 1-123 residues.","type":"Curator statement"},{"text":"However, unlike that of Syntaxin1, the binding of the STX17 SNARE motif to its Habc domain can induce a partial unfolding of the extreme C-terminal α-helix of the STX17 Habc domain (Fig. 1D and SI Appendix, Fig. S4C). ","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T13:39:18.960Z"}},{"start":94,"end":121,"reference_id":"32817423","reference_source":"pmid","reference_html":"Decoding three distinct states of the Syntaxin17 SNARE motif in mediating autophagosome-lysosome fusion. <i> Li Y, Cheng X, Li M, Wang Y, Fu T, Zhou Z, Wang Y, Gong X, Xu X, Liu J, Pan L. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-05-26T19:00:18.664Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9H492","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"O95166","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP03670r006","statement":[{"text":"NMR-based analyses showed that both GABARAP and LC3A can interact with STX17(142–228) (Fig. 3A and SI Appendix, Fig. S13A), and the major binding sites on STX17 are located within the N-terminal part (residues 170 to 191) of the STX17 Qa-SNARE motif (Fig. 3B and SI Appendix, Fig. S13B). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T13:39:29.224Z"}},{"start":171,"end":176,"reference_id":"32817423","reference_source":"pmid","reference_html":"Decoding three distinct states of the Syntaxin17 SNARE motif in mediating autophagosome-lysosome fusion. <i> Li Y, Cheng X, Li M, Wang Y, Fu T, Zhou Z, Wang Y, Gong X, Xu X, Liu J, Pan L. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-05-26T19:05:12.753Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9H492","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"O95166","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP03670r007","statement":[{"text":"The obtained ITC results showed that the W172Q mutation dramatically reduces and totally abolishes the interaction of STX17(142–228) with GABARAP and LC3A, respectively (Fig. 3 C and D and SI Appendix, Fig. S13 C and D), while the F189Q mutation does not affect the binding of STX17(142–228) to GABARAP and LC3A (Fig. 3 C and E and SI Appendix, Fig. S13 C and E), confirming that only the first putative LIR motif of STX17 is directly involved in the interactions with GABARAP and LC3A (Fig. 3 A and B and SI Appendix, Fig. S13 A and B).","type":"Results"},{"text":"LIR motif corresponds to the 172-175 “WETL” residues.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T13:39:28.241Z"}},{"start":167,"end":188,"reference_id":"32817423","reference_source":"pmid","reference_html":"Decoding three distinct states of the Syntaxin17 SNARE motif in mediating autophagosome-lysosome fusion. <i> Li Y, Cheng X, Li M, Wang Y, Fu T, Zhou Z, Wang Y, Gong X, Xu X, Liu J, Pan L. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-05-26T19:06:57.504Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"7BV4"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"O95166","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP03670r008","statement":[{"text":"Fortunately, using the purified STX17(167–188)–GABARAP complex, we obtained good crystals that diffracted to 2.0-Å resolution.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T13:39:26.741Z"}},{"start":142,"end":167,"reference_id":"32817423","reference_source":"pmid","reference_html":"Decoding three distinct states of the Syntaxin17 SNARE motif in mediating autophagosome-lysosome fusion. <i> Li Y, Cheng X, Li M, Wang Y, Fu T, Zhou Z, Wang Y, Gong X, Xu X, Liu J, Pan L. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-05-26T19:10:58.713Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"7BV6"}],"region_id":"DP03670r009","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9BV40"}],"statement":[{"text":"Lack of electron density in the PDB shows disordered region.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T13:39:12.325Z"}},{"start":168,"end":228,"reference_id":"32817423","reference_source":"pmid","reference_html":"Decoding three distinct states of the Syntaxin17 SNARE motif in mediating autophagosome-lysosome fusion. <i> Li Y, Cheng X, Li M, Wang Y, Fu T, Zhou Z, Wang Y, Gong X, Xu X, Liu J, Pan L. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-05-26T19:32:04.129Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9BV40","operator":null,"partner_start":8,"partner_end":75},{"db":"UniProt","id":"O95721","operator":"and","partner_start":40,"partner_end":130},{"db":"UniProt","id":"O95721","operator":"and","partner_start":191,"partner_end":258}],"region_id":"DP03670r010","statement":[{"text":"To test this hypothesis, we first purified this autophagic SNARE complex, which includes the SNARE motifs of STX17 and VAMP8 together with their short neck regions, and the Qb- and Qc-SNARE motifs of SNAP29, and then used circular dichroism (CD) spectroscopy to examine its secondary structure features and thermal stability.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T13:39:25.025Z"}},{"start":168,"end":228,"reference_id":"32817423","reference_source":"pmid","reference_html":"Decoding three distinct states of the Syntaxin17 SNARE motif in mediating autophagosome-lysosome fusion. <i> Li Y, Cheng X, Li M, Wang Y, Fu T, Zhou Z, Wang Y, Gong X, Xu X, Liu J, Pan L. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-05-26T19:25:02.159Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"7BV6"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9BV40","operator":null,"partner_start":8,"partner_end":75},{"db":"UniProt","id":"O95721","operator":"and","partner_start":40,"partner_end":130},{"db":"UniProt","id":"O95721","operator":"and","partner_start":191,"partner_end":258}],"region_id":"DP03670r011","statement":[{"text":"Using analytical gel filtration chromatography-based analyses, we showed that the Qb- and Qc-SNARE motifs of SNAP29 alone are unable to interact with or disturb the GABARAP–STX17 complex (SI Appendix, Fig. S18A); however, in the presence of an additional VAMP8 R-SNARE motif, a stable SNARE complex containing the STX17 Qa-SNARE motif, the VAMP8 R-SNARE motif, as well as the Qb- and Qc-SNARE motifs of SNAP29, was readily formed (SI Appendix, Fig. S18 B and C), indicating that SNAP29 and VAMP8 together can easily compete with GABARAP for binding to STX17 to assemble the STX17–SNAP29–VAMP8 SNARE complex.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T13:39:24.142Z"}},{"start":142,"end":228,"reference_id":"32817423","reference_source":"pmid","reference_html":"Decoding three distinct states of the Syntaxin17 SNARE motif in mediating autophagosome-lysosome fusion. <i> Li Y, Cheng X, Li M, Wang Y, Fu T, Zhou Z, Wang Y, Gong X, Xu X, Liu J, Pan L. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-05-26T19:29:11.690Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"7BV6"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9BV40","operator":null,"partner_start":8,"partner_end":75},{"db":"UniProt","id":"O95721","operator":"and","partner_start":40,"partner_end":130},{"db":"UniProt","id":"O95721","operator":"and","partner_start":191,"partner_end":258}],"region_id":"DP03670r012","statement":[{"text":"Using analytical gel filtration chromatography-based analyses, we showed that the Qb- and Qc-SNARE motifs of SNAP29 alone are unable to interact with or disturb the GABARAP–STX17 complex (SI Appendix, Fig. S18A); however, in the presence of an additional VAMP8 R-SNARE motif, a stable SNARE complex containing the STX17 Qa-SNARE motif, the VAMP8 R-SNARE motif, as well as the Qb- and Qc-SNARE motifs of SNAP29, was readily formed (SI Appendix, Fig. S18 B and C), indicating that SNAP29 and VAMP8 together can easily compete with GABARAP for binding to STX17 to assemble the STX17–SNAP29–VAMP8 SNARE complex.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T13:39:21.525Z"}},{"start":142,"end":228,"reference_id":"32817423","reference_source":"pmid","reference_html":"Decoding three distinct states of the Syntaxin17 SNARE motif in mediating autophagosome-lysosome fusion. <i> Li Y, Cheng X, Li M, Wang Y, Fu T, Zhou Z, Wang Y, Gong X, Xu X, Liu J, Pan L. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-05-26T19:36:03.372Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03670r013","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9BV40","statements":[{"type":"Curator statement","text":"Interacting peptide of the 8-75 region."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O95721","statements":[{"type":"Curator statement","text":"Interacting peptide of the 4-130 region  and peptide of the191-258 region."}]}],"statement":[{"text":"In contrast to that of the isolated SNARE regions of STX17 and VAMP8 as well as the full-length SNAP29, the SNARE complex showed significant characteristic α-helical content, as indicated by its CD spectrum (Fig. 5A). ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T13:39:11.057Z"}},{"start":142,"end":228,"reference_id":"32817423","reference_source":"pmid","reference_html":"Decoding three distinct states of the Syntaxin17 SNARE motif in mediating autophagosome-lysosome fusion. <i> Li Y, Cheng X, Li M, Wang Y, Fu T, Zhou Z, Wang Y, Gong X, Xu X, Liu J, Pan L. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-05-26T19:37:45.808Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03670r014","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9BV40","statements":[{"type":"Curator statement","text":"Interacting peptide of the 8-75 region."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O95721","statements":[{"type":"Curator statement","text":"Interacting peptide of the 4-130 region  and peptide of the191-258 region."}]}],"statement":[{"text":"In contrast to that of the isolated SNARE regions of STX17 and VAMP8 as well as the full-length SNAP29, the SNARE complex showed significant characteristic α-helical content, as indicated by its CD spectrum (Fig. 5A). It is noteworthy that the isolated SNARE region of STX17 is intrinsically disordered based on the CD analysis (Fig. 5A), consistent with the aforementioned NMR results (SI Appendix, Fig. S2).","type":"Results"}],"states_connection":[{"source":"DP03670r001","target":"DP03670r013"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T13:39:17.706Z"}},{"start":142,"end":228,"reference_id":"32817423","reference_source":"pmid","reference_html":"Decoding three distinct states of the Syntaxin17 SNARE motif in mediating autophagosome-lysosome fusion. <i> Li Y, Cheng X, Li M, Wang Y, Fu T, Zhou Z, Wang Y, Gong X, Xu X, Liu J, Pan L. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-05-26T19:41:43.576Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000057","term_name":"self-regulatory activity","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03670r015","statement":[{"text":"In this model, STX17 alone is in an autoinhibited closed state and, particularly, its Habc region somehow packs with the N-terminal part of its Qa-SNARE motif to stabilize the intrinsically disordered SNARE motif of STX17, thereby preventing its unnecessary degradation or interactions with other proteins on the autophagosome before assembling the STX17–SNAP29–VAMP8 SNARE complex (Fig. 6). However, in the presence of GABARAP/LC3 family proteins, the mammalian ATG8 ortholog can competitively bind to the N-terminal part of the STX17 Qa-SNARE motif that contains an extended LIR motif and abolish the autoinhibited conformation of STX17 (Fig. 6), thereby releasing the N-terminal Habc domain of STX17 and inducing its conformational rearrangement. ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T13:39:20.490Z"}}],"regions_counter":15,"released":"2022_06","sequence":"MSEDEEKVKLRRLEPAIQKFIKIVIPTDLERLRKHQINIEKYQRCRIWDKLHEEHINAGRTVQQLRSNIREIEKLCLKVRKDDLVLLKRMIDPVKEEASAATAEFLQLHLESVEELKKQFNDEETLLQPPLTRSMTVGGAFHTTEAEASSQSLTQIYALPEIPQDQNAAESWETLEADLIELSQLVTDFSLLVNSQQEKIDSIADHVNSAAVNVEEGTKNLGKAAKYKLAALPVAGALIGGMVGGPIGLLAGFKVAGIAAALGGGVLGFTGGKLIQRKKQKMMEKLTSSCPDLPSQTDKKCS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"STX17","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"21545355","url":"http://www.ncbi.nlm.nih.gov/pubmed/21545355","alternativeUrl":"https://europepmc.org/abstract/MED/21545355"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11432","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11432"}}]}}],"alphafold_very_low_content":0.2947019867549669,"disorder_content":0.38079470198675497,"disprot_consensus":{"full":[{"start":94,"end":121,"type":"T"},{"start":142,"end":228,"type":"T"}],"Structural state":[{"start":94,"end":121,"type":"D"},{"start":142,"end":228,"type":"D"}],"Molecular function":[{"start":94,"end":121,"type":"F"},{"start":142,"end":228,"type":"F"}],"Structural transition":[{"start":94,"end":121,"type":"T"},{"start":142,"end":228,"type":"T"}],"Disorder function":[{"start":142,"end":228,"type":"F"}]}},{"disprot_id":"DP03671","acc":"Q8TDY2","creator":"oantonescu","date":"2022-05-26T19:56:59.053Z","features":{"pfam":[{"id":"PF10377","name":"Autophagy-related protein 11","start":1477,"end":1587}],"gene3D":[]},"length":1594,"name":"RB1-inducible coiled-coil protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1543,"end":1552,"reference_id":"34389544","reference_source":"pmid","reference_html":"Structural and biochemical advances on the recruitment of the autophagy-initiating ULK and TBK1 complexes by autophagy receptor NDP52.  <i> Fu T, Zhang M, Zhou Z, Wu P, Peng C, Wang Y, Gong X, Li Y, Wang Y, Xu X, Li M, Shen L, Pan L. </i> Sci Adv, 2021","date":"2022-05-26T20:13:17.127Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"7EA2"}],"region_id":"DP03671r001","statement":[{"text":"The region lacks electron density, as shown in the PDB, typical of IDR.","type":"Curator statement"}],"sequence_construct":"GPGSEDDICILNHEKGSGSSRHSEKIAIRDFQVGDLVLIILDERHDNYVLFTVSPTLYFLHSESLPALDLKPGEGASGASRRPWVLGKVMEKEYCQAKKAQNRFKVPLGTKFYRVKAVSWNKKV","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16947","statements":[{"type":"Methods","text":"The fresh purified NAP1(6-16) fused with RB1CC1(1490-1594) protein was mixed with equal volumes of reservoir solution containing 0.1 M phosphate/citrate (pH 4.2) and 40% PEG-300."}],"entry_name":"citrate(3-)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46807","statements":[{"type":"Methods","text":" The fresh purified NAP1(6-16) fused with RB1CC1(1490-1594) protein was mixed with equal volumes of reservoir solution containing 0.1 M phosphate/citrate (pH 4.2) and 40% PEG-300."}],"entry_name":"diethylene glycol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"49793","entry_name":"hexaethylene glycol"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T13:57:16.266Z"}}],"regions_counter":5,"released":"2022_06","sequence":"MKLYVFLVNTGTTLTFDTELTVQTVADLKHAIQSKYKIAIQHQVLVVNGGECMAADRRVCTYSAGTDTNPIFLFNKEMILCDRPPAIPKTTFSTENDMEIKVEESLMMPAVFHTVASRTQLALEMYEVAKKLCSFCEGLVHDEHLQHQGWAAIMANLEDCSNSYQKLLFKFESIYSNYLQSIEDIKLKLTHLGTAVSVMAKIPLLECLTRHSYRECLGRLDSLPEHEDSEKAEMKRSTELVLSPDMPRTTNESLLTSFPKSVEHVSPDTADAESGKEIRESCQSTVHQQDETTIDTKDGDLPFFNVSLLDWINVQDRPNDVESLVRKCFDSMSRLDPRIIRPFIAECRQTIAKLDNQNMKAIKGLEDRLYALDQMIASCGRLVNEQKELAQGFLANQKRAENLKDASVLPDLCLSHANQLMIMLQNHRKLLDIKQKCTTAKQELANNLHVRLKWCCFVMLHADQDGEKLQALLRLVIELLERVKIVEALSTVPQMYCLAVVEVVRRKMFIKHYREWAGALVKDGKRLYEAEKSKRESFGKLFRKSFLRNRLFRGLDSWPPSFCTQKPRKFDCELPDISLKDLQFLQSFCPSEVQPFLRVPLLCDFEPLHQHVLALHNLVKAAQSLDEMSQTITDLLSEQKASVSQTSPQSASSPRMESTAGITTTTSPRTPPPLTVQDPLCPAVCPLEELSPDSIDAHTFDFETIPHPNIEQTIHQVSLDLDSLAESPESDFMSAVNEFVIEENLSSPNPISDPQSPEMMVESLYSSVINAIDSRRMQDTNVCGKEDFGDHTSLNVQLERCRVVAQDSHFSIQTIKEDLCHFRTFVQKEQCDFSNSLKCTAVEIRNIIEKVKCSLEITLKEKHQKELLSLKNEYEGKLDGLIKETEENENKIKKLKGELVCLEEVLQNKDNEFALVKHEKEAVICLQNEKDQKLLEMENIMHSQNCEIKELKQSREIVLEDLKKLHVENDEKLQLLRAELQSLEQSHLKELEDTLQVRHIQEFEKVMTDHRVSLEELKKENQQIINQIQESHAEIIQEKEKQLQELKLKVSDLSDTRCKLEVELALKEAETDEIKILLEESRAQQKETLKSLLEQETENLRTEISKLNQKIQDNNENYQVGLAELRTLMTIEKDQCISELISRHEEESNILKAELNKVTSLHNQAFEIEKNLKEQIIELQSKLDSELSALERQKDEKITQQEEKYEAIIQNLEKDRQKLVSSQEQDREQLIQKLNCEKDEAIQTALKEFKLEREVVEKELLEKVKHLENQIAKSPAIDSTRGDSSSLVAELQEKLQEEKAKFLEQLEEQEKRKNEEMQNVRTSLIAEQQTNFNTVLTREKMRKENIINDLSDKLKSTMQQQERDKDLIESLSEDRARLLEEKKKLEEEVSKLRSSSFVPSPYVATAPELYGACAPELPGESDRSAVETADEGRVDSAMETSMMSVQENIHMLSEEKQRIMLLERTLQLKEEENKRLNQRLMSQSMSSVSSRHSEKIAIRDFQVGDLVLIILDERHDNYVLFTVSPTLYFLHSESLPALDLKPGEGASGASRRPWVLGKVMEKEYCQAKKAQNRFKVPLGTKFYRVKAVSWNKKV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"RB1CC1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:15574","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:15574"}}]},"synonyms":[{"value":"KIAA0203"},{"value":"RBICC"}]}],"alphafold_very_low_content":0.20075282308657466,"disorder_content":0.006273525721455458,"disprot_consensus":{"full":[{"start":1543,"end":1552,"type":"D"}],"Structural state":[{"start":1543,"end":1552,"type":"D"}]}},{"disprot_id":"DP03672","acc":"O95197","creator":"vnugnes","date":"2022-05-26T20:36:17.586Z","features":{"pfam":[{"id":"PF02453","name":"Reticulon","start":844,"end":1007}],"gene3D":[]},"length":1032,"name":"Reticulon-3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":27,"reference_id":"19364499","reference_source":"pmid","reference_html":"NMR studies reveal a novel mode for hFADD to bind with the unstructured hRTN3 which initiates the ER-stress activated apoptosis. <i> Liu J, Zhu W, Qin H, Song J. </i> Biochem Biophys Res Commun, 2009","date":"2022-05-26T20:40:19.376Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03672r001","statement":[{"text":"To confirm this, we collected its far-UV CD spectrum at pH 4.0 (Fig. 1A), which has the maximal negative signal located at ∼198 nm, indicating that in solution the hRTN3 N-terminus has no stable secondary structure.","type":"Results"}],"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":4}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T12:07:49.623Z"}},{"start":1,"end":27,"reference_id":"19364499","reference_source":"pmid","reference_html":"NMR studies reveal a novel mode for hFADD to bind with the unstructured hRTN3 which initiates the ER-stress activated apoptosis. <i> Liu J, Zhu W, Qin H, Song J. </i> Biochem Biophys Res Commun, 2009","date":"2022-05-26T20:40:56.105Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03672r002","statement":[{"text":"Moreover, the hRTN3 N-terminus was further 15N isotope-labeled and assessed by 1H–15N NMR HSQC spectroscopy. As clearly seen in Fig. 1B, the hRTN3 N-terminus has a narrowly dispersed HSQC spectrum (∼0.9 ppm for 1H and 20.5 ppm for 15N dimensions). This observation again indicates that hRTN3 C-terminus is also lacking of any tight tertiary packing.","type":"Results"}],"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":4}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T12:07:47.073Z"}},{"start":988,"end":1032,"reference_id":"19364499","reference_source":"pmid","reference_html":"NMR studies reveal a novel mode for hFADD to bind with the unstructured hRTN3 which initiates the ER-stress activated apoptosis. <i> Liu J, Zhu W, Qin H, Song J. </i> Biochem Biophys Res Commun, 2009","date":"2022-05-26T20:46:58.734Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03672r003","statement":[{"text":"For the 44-residue hRTN3 C-terminus, we collected its far-UV CD spectra at both pH 4.0 and 6.5 (Fig. 1C), which had the maximal negative signals are located at ∼199 and ∼198 nm, respectively. This indicates that the hRTN3 C-terminus is also highly disordered without any stable secondary structure.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T12:07:45.992Z"}},{"start":988,"end":1032,"reference_id":"19364499","reference_source":"pmid","reference_html":"NMR studies reveal a novel mode for hFADD to bind with the unstructured hRTN3 which initiates the ER-stress activated apoptosis. <i> Liu J, Zhu W, Qin H, Song J. </i> Biochem Biophys Res Commun, 2009","date":"2022-05-26T20:47:34.179Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03672r004","statement":[{"text":"As seen in Fig. 1D, the hRTN3 C-terminus also has narrowly dispersed HSQC spectra at both pH 4.0 and 6.5 (∼0.65 ppm for 1H and 19.5 ppm for 15N dimensions), suggesting that the hRTN3 C-terminus is also lacking of any tight tertiary packing.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T12:07:45.186Z"}},{"start":988,"end":1032,"reference_id":"19364499","reference_source":"pmid","reference_html":"NMR studies reveal a novel mode for hFADD to bind with the unstructured hRTN3 which initiates the ER-stress activated apoptosis. <i> Liu J, Zhu W, Qin H, Song J. </i> Biochem Biophys Res Commun, 2009","date":"2022-05-26T20:53:12.986Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q13158","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03672r005","statement":[{"text":"As seen in Fig. 3A, the binding of hRTN3-C44 to hFADD was associated with the heat absorbance (endothermic), implying that this binding may be mainly entropy-driven [18].","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T12:08:53.657Z"}},{"start":988,"end":1032,"reference_id":"19364499","reference_source":"pmid","reference_html":"NMR studies reveal a novel mode for hFADD to bind with the unstructured hRTN3 which initiates the ER-stress activated apoptosis. <i> Liu J, Zhu W, Qin H, Song J. </i> Biochem Biophys Res Commun, 2009","date":"2022-05-26T20:55:22.313Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q13158","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03672r006","statement":[{"text":"Fig. 3B presents the superimposition of the HSQC spectra of the 15N-labeled hRTN3-C44 in the absence (blue) and presence of hFADD at ratios of 1:1 (green) and 1:2 (red). The obtained result allowed the successful assignment of the perturbed hRTN3-C44 residues upon binding to hFADD.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T12:08:52.256Z"}}],"regions_counter":6,"released":"2022_06","sequence":"MAEPSAATQSHSISSSSFGAEPSAPGGGGSPGACPALGTKSCSSSCADSFVSSSSSQPVSLFSTSQEGLSSLCSDEPSSEIMTSSFLSSSEIHNTGLTILHGEKSHVLGSQPILAKEGKDHLDLLDMKKMEKPQGTSNNVSDSSVSLAAGVHCDRPSIPASFPEHPAFLSKKIGQVEEQIDKETKNPNGVSSREAKTALDADDRFTLLTAQKPPTEYSKVEGIYTYSLSPSKVSGDDVIEKDSPESPFEVIIDKAAFDKEFKDSYKESTDDFGSWSVHTDKESSEDISETNDKLFPLRNKEAGRYPMSALLSRQFSHTNAALEEVSRCVNDMHNFTNEILTWDLVPQVKQQTDKSSDCITKTTGLDMSEYNSEIPVVNLKTSTHQKTPVCSIDGSTPITKSTGDWAEASLQQENAITGKPVPDSLNSTKEFSIKGVQGNMQKQDDTLAELPGSPPEKCDSLGSGVATVKVVLPDDHLKDEMDWQSSALGEITEADSSGESDDTVIEDITADTSFENNKIQAEKPVSIPSAVVKTGEREIKEIPSCEREEKTSKNFEELVSDSELHQDQPDILGRSPASEAACSKVPDTNVSLEDVSEVAPEKPITTENPKLPSTVSPNVFNETEFSLNVTTSAYLESLHGKNVKHIDDSSPEDLIAAFTETRDKGIVDSERNAFKAISEKMTDFKTTPPVEVLHENESGGSEIKDIGSKYSEQSKETNGSEPLGVFPTQGTPVASLDLEQEQLTIKALKELGERQVEKSTSAQRDAELPSEEVLKQTFTFAPESWPQRSYDILERNVKNGSDLGISQKPITIRETTRVDAVSSLSKTELVKKHVLARLLTDFSVHDLIFWRDVKKTGFVFGTTLIMLLSLAAFSVISVVSYLILALLSVTISFRIYKSVIQAVQKSEEGHPFKAYLDVDITLSSEAFHNYMNAAMVHINRALKLIIRLFLVEDLVDSLKLAVFMWLMTYVGAVFNGITLLILAELLIFSVPIVYEKYKTQIDHYVGIARDQTKSIVEKIQAKLPGIAKKKAE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins","Stress response proteins"],"genes":[{"name":{"value":"RTN3"},"synonyms":[{"value":"ASYIP"},{"value":"NSPL2"}]}],"alphafold_very_low_content":0.7296511627906976,"disorder_content":0.06976744186046512,"disprot_consensus":{"full":[{"start":1,"end":27,"type":"D"},{"start":988,"end":1032,"type":"D"}],"Structural state":[{"start":1,"end":27,"type":"D"},{"start":988,"end":1032,"type":"D"}],"Molecular function":[{"start":988,"end":1032,"type":"F"}]}},{"disprot_id":"DP03674","acc":"Q9S7A9","creator":"cpintado","date":"2022-05-27T10:08:18.374Z","features":{"pfam":[{"id":"PF03110","name":"SBP domain","start":54,"end":127}],"gene3D":[]},"length":174,"name":"Squamosa promoter-binding-like protein 4","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":104,"end":131,"reference_id":"15001351","reference_source":"pmid","reference_html":"A novel zinc-binding motif revealed by solution structures of DNA-binding domains of Arabidopsis SBP-family transcription factors. <i> Yamasaki K, Kigawa T, Inoue M, Tateno M, Yamasaki T, Yabuki T, Aoki M, Seki E, Matsuda T, Nunokawa E, Ishizuka Y, Terada T, Shirouzu M, Osanai T, Tanaka A, Seki M, Shinozaki K, Yokoyama S. </i> J Mol Biol, 2004","date":"2022-07-15T09:20:07.046Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006285","ec_ontology":"ECO","ec_name":"magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1UL4"}],"region_id":"DP03674r001","statement":[{"text":"Flexibility in the C-terminal regions was confirmed by heteronuclear relaxation experiments (data available in Application 1, Image 1, Image 2). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-15T13:12:52.022Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MEGKRSQGQGYMKKKSYLVEEDMETDTDEEEEVGRDRVRGSRGSINRGGSLRLCQVDRCTADMKEAKLYHRRHKVCEVHAKASSVFLSGLNQRFCQQCSRFHDLQEFDEAKRSCRRRLAGHNERRRKSSGESTYGEGSGRRGINGQVVMQNQERSRVEMTLPMPNSSFKRPQIR","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"genes":[{"name":{"value":"SPL4"},"orfNames":[{"value":"F12M16.2"}],"olnNames":[{"value":"At1g53160"}]}],"alphafold_very_low_content":0.10344827586206896,"disorder_content":0.16091954022988506,"disprot_consensus":{"full":[{"start":104,"end":131,"type":"D"}],"Structural state":[{"start":104,"end":131,"type":"D"}]}},{"disprot_id":"DP03675","acc":"F4K4L7","creator":"cpintado","date":"2022-05-27T10:31:51.026Z","features":{"pfam":[{"id":"PF05236","name":"Transcription initiation factor TFIID component TAF4 family","start":537,"end":850},{"id":"PF12174","name":"RCD1-SRO-TAF4 (RST) plant domain","start":188,"end":251}],"gene3D":[]},"length":852,"name":"Transcription initiation factor TFIID subunit 4b","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":182,"end":191,"reference_id":"35452682","reference_source":"pmid","reference_html":"αα-hub coregulator structure and flexibility determine transcription factor binding and selection in regulatory interactomes. <i> Friis Theisen F, Salladini E, Davidsen R, Jo Rasmussen C, Staby L, Kragelund BB, Skriver K. </i> J Biol Chem, 2022","date":"2022-07-15T09:20:50.905Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7AC1"}],"region_id":"DP03675r001","statement":[{"text":"The comparison between the envelope and the NMR structures, with a χ2 = 1.09, confirmed the globular fold of the AtTAF4–RST domain with the addition of a short disordered tail, here originating from the N-terminal end (Fig. 2B).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-15T13:13:39.194Z"}},{"start":182,"end":191,"reference_id":"35452682","reference_source":"pmid","reference_html":"αα-hub coregulator structure and flexibility determine transcription factor binding and selection in regulatory interactomes. <i> Friis Theisen F, Salladini E, Davidsen R, Jo Rasmussen C, Staby L, Kragelund BB, Skriver K. </i> J Biol Chem, 2022","date":"2022-07-15T09:22:51.224Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7AC1"}],"region_id":"DP03675r002","statement":[{"text":"In addition, the pair distance distribution yielded an average maximal internal distance (Dmax) of 44.4 ± 0.7 Å and described a typical globular protein with a short disordered tail, as evidenced by the Gaussian distribution with an asymmetric end (Fig. S1C).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-15T13:13:47.009Z"}}],"regions_counter":2,"released":"2023_12","sequence":"MDPSIFKLLEEDEDESMHSGADVDAFQAALNRDIEGSMTTSIPHVTNPGNNHSSRQQFSTWKNGIGDSNINVQTQHSLESTQMKEQEGSTLENQHQHDLKRANEPHLQHNQPQDLHRAGQLWENPSQVPQSTGLPISEKNPTGNESDRSHNQESESQYMKLQKMSSQQARGVEPPVNPMNVNPINRNPKQVPFAALLPTLMNQLDKDRALQLRTLYARLKKNEIPKEGFTRHMKDIVGDQMLRMAVSKLQQVNYNQGKIGIQAPSTEINNQKSQSDPRAVHLNQLPSSASGTLGSSVPVQGLTKHPQHQMQHPPSSFPMYTTSGSFHSFPGPNTNASGSTLRPHLHDSHMRHVAHNQPMGSTGLGGPPQSTTNMMTMPKFERPSSVNDPSRVQGGATSHFQNSSSLPLNSAPGQGSSVSHVKQESVDQSFEKNNAASMTSNEDLEKESSRMVLSTPNNMAPASSVSPSMTTQLDASTTMNSRGPLGTSQGGANARMPPKKPSVGQKKPLETLGSSPPPPSKKQKVAGNSMDQSIEQLNDVTAVSGVNLREEEEQLFSGAKEDGRVSEASRRVVHEEEERLILQKNPLQRKLAEIMAKAGLKQISNDVERCLSLCVEERMRGLLSHIIRLSKQRVDAEKSRHRTFITSDIRLQINEMNQKVKEEWEKKQAEAEKLKKPSESEEGDGGVDSEKDKEDNRSKGVKGNKEDDDKMRTTAANVAARAAVGGDDAFLKWQLMAEARQKSVSEAGKDGNQKTTSGGGKNSKDRQDGGRRFSGTESSCGVGIVYRVSSSRFWFAMMSFGFLFAGGRRVGKNQGSSLQPKVVRTISVKDVVAVLEREPQMSKSTLMYRLIQ","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"genes":[{"name":{"value":"TAF4B"},"orfNames":[{"value":"AAF24960.1"}],"olnNames":[{"value":"At5g43130"}]}],"alphafold_very_low_content":0.607981220657277,"disorder_content":0.011737089201877934,"disprot_consensus":{"full":[{"start":182,"end":191,"type":"D"}],"Structural state":[{"start":182,"end":191,"type":"D"}]}},{"disprot_id":"DP03676","acc":"D0NBE6","creator":"vsagris","date":"2022-05-27T14:36:16.794Z","features":{"pfam":[{"id":"PF18634","name":"RXLR phytopathogen effector protein WY-domain","start":145,"end":194},{"id":"PF18634","name":"RXLR phytopathogen effector protein WY-domain","start":243,"end":292},{"id":"PF22748","name":"Effector PexRD54, WY-domain","start":102,"end":142},{"id":"PF22748","name":"Effector PexRD54, WY-domain","start":205,"end":240},{"id":"PF22748","name":"Effector PexRD54, WY-domain","start":309,"end":346}],"gene3D":[]},"length":381,"name":"RxLR effector protein 54","ncbi_taxon_id":403677,"organism":"Phytophthora infestans (strain T30-4)","regions":[{"start":370,"end":381,"reference_id":"27458016","reference_source":"pmid","reference_html":"Structural Basis of Host Autophagy-related Protein 8 (ATG8) Binding by the Irish Potato Famine Pathogen Effector Protein PexRD54. <i> Maqbool A, Hughes RK, Dagdas YF, Tregidgo N, Zess E, Belhaj K, Round A, Bozkurt TO, Kamoun S, Banfield MJ. </i> J Biol Chem, 2016","date":"2022-05-27T14:42:25.836Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5L7S"}],"region_id":"DP03676r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"M1C146","statements":[{"type":"Results","text":"Although PexRD54 could be crystallized alone, the crystal that gave rise to the best x-ray dataset was obtained from a sample including both PexRD54 and ATG8CL after co-expression in E. coli (see under “Experimental Procedures”)."}]}],"sequence_construct":"SLSAEEAQLKVWIQSQIHPRELFGVLSLGKRAAKLDDNPDFVQWLRLVKDFRANNGNQAFSDLDIYYLLLKTNSPEQLKLLFETLRHTPGMTKIGASMEKSLSGNWIRKALEQDTYPTIVYNTLRLKDAGTKLDDTPMFRQWLEYVEKYWNKNAGAFFGDTQMLTLFQKTMTEEEDIIKLVHMLRNNPGMKSHADKLERYLLLTSESSHKTMADVWLKARETPEEVFRILRLAEKQTAAADDNRMLNLWLRYTQTYRDKIDKNAFSDAEALQFFRKAKPLDFDWEIV","statement":[{"text":"Five N-terminal residues (92–96), the residues in two loops (248–250 and 331–334), and 11 C-terminal residues (371–381), which include the AIM motif, were not included in the final model due to poor electron density in these regions.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T13:23:05.184Z"}},{"start":377,"end":381,"reference_id":"27458016","reference_source":"pmid","reference_html":"Structural Basis of Host Autophagy-related Protein 8 (ATG8) Binding by the Irish Potato Famine Pathogen Effector Protein PexRD54. <i> Maqbool A, Hughes RK, Dagdas YF, Tregidgo N, Zess E, Belhaj K, Round A, Bozkurt TO, Kamoun S, Banfield MJ. </i> J Biol Chem, 2016","date":"2022-05-27T14:53:24.515Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5L83"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"M1C146","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03676r002","statement":[{"text":" Therefore, to visualize the interaction between PexRD54 and ATG8CL, we determined the crystal structure of ATG8CL in complex with a PexRD54 C-terminal pentapeptide. This pentapeptide includes the AIM motif, with residues Asp-377–Trp-378–Glu-379–Ile-380–Val-381.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T13:23:40.731Z"}},{"start":378,"end":381,"reference_id":"27458016","reference_source":"pmid","reference_html":"Structural Basis of Host Autophagy-related Protein 8 (ATG8) Binding by the Irish Potato Famine Pathogen Effector Protein PexRD54. <i> Maqbool A, Hughes RK, Dagdas YF, Tregidgo N, Zess E, Belhaj K, Round A, Bozkurt TO, Kamoun S, Banfield MJ. </i> J Biol Chem, 2016","date":"2022-06-21T15:18:07.319Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005667","ec_ontology":"ECO","ec_name":"site-directed mutagenesis phenotypic evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","region_id":"DP03676r003","statement":[{"text":"Site-directed mutagenesis of the PexRD54 C-terminal AIM region, and ATG8CL binding to a PexRD54 AIM-based peptide array, mapped the key residues that define the PexRD54-ATG8CL interface.","type":"Introduction"},{"text":"First, we used alanine-scanning mutagenesis to substitute Ala at six positions in the PexRD54 AIM region, Pro-373, Asp-377, Trp-378, Glu-379, Ile-380, and Val-381. Each of these proteins was expressed and purified as described for wild type. We then used analytical gel filtration to qualitatively assay whether these variants support complex formation with ATG8CL. As predicted, we did not observe interaction of PexRD54 W378A with ATG8CL (Fig. 7). For each of the other mutations, we still observed an interaction with ATG8CL, including PexRD54 V381A.","type":"Results"},{"text":"FIGURE 7. Analysis of the interaction between PexRD54 variants and ATG8CL by gel filtration. Analytical gel filtration traces were obtained for PexRD54 variants mutated in the AIM region and incubated with ATG8CL (1:1 mixture). ","type":"Figure"},{"text":"Full-length RFP-PexRD54 and the AIM motif disrupting variant RFP-PexRD54378-AEIA-381 were used as controls.","type":"Results"},{"text":"The functional LIR motif WEIV in positions 378-381 is inside the disordered fragment region in positions 370-381.","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:37:42.532Z"}},{"start":378,"end":381,"reference_id":"27458016","reference_source":"pmid","reference_html":"Structural Basis of Host Autophagy-related Protein 8 (ATG8) Binding by the Irish Potato Famine Pathogen Effector Protein PexRD54. <i> Maqbool A, Hughes RK, Dagdas YF, Tregidgo N, Zess E, Belhaj K, Round A, Bozkurt TO, Kamoun S, Banfield MJ. </i> J Biol Chem, 2016","date":"2022-06-21T15:34:29.070Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005667","ec_ontology":"ECO","ec_name":"site-directed mutagenesis phenotypic evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"M1C146","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03676r004","statement":[{"text":"Site-directed mutagenesis of the PexRD54 C-terminal AIM region, and ATG8CL binding to a PexRD54 AIM-based peptide array, mapped the key residues that define the PexRD54-ATG8CL interface.","type":"Introduction"},{"text":"First, we used alanine-scanning mutagenesis to substitute Ala at six positions in the PexRD54 AIM region, Pro-373, Asp-377, Trp-378, Glu-379, Ile-380, and Val-381. Each of these proteins was expressed and purified as described for wild type. We then used analytical gel filtration to qualitatively assay whether these variants support complex formation with ATG8CL. As predicted, we did not observe interaction of PexRD54 W378A with ATG8CL (Fig. 7). For each of the other mutations, we still observed an interaction with ATG8CL, including PexRD54 V381A.","type":"Results"},{"text":"FIGURE 4. Crystal structure of ATG8CL bound to the PexRD54(377–381)-peptide and specificity of peptide binding. A, schematic representation of ATG8CL/PexRD54(377–381)-peptide complex highlighting key interactions. ATG8CL is shown in magenta schematic representation with the molecular surface that contacts the PexRD54(377–381)-peptide shown in orange. The PexRD54(377–381)-peptide is shown as sticks with yellow carbon atoms. The electron density omit map of the peptide ligand (Fobs − Fcalc map) is shown in blue mesh and contoured at 2 σ. Electrostatic interactions are indicated with black dashed lines. B, results of the peptide array analyzing the effect of single amino acid substitutions (top) at all positions of 10-mer peptide of PexRD54 (Lys-372–Val-381, side). GST-tagged ATG8CL was visualized using an anti-GST-HRP antibody.","type":"Figure"},{"text":"FIGURE 7. Analysis of the interaction between PexRD54 variants and ATG8CL by gel filtration. Analytical gel filtration traces were obtained for PexRD54 variants mutated in the AIM region and incubated with ATG8CL (1:1 mixture). ","type":"Figure"},{"text":"Full-length RFP-PexRD54 and the AIM motif disrupting variant RFP-PexRD54378-AEIA-381 were used as controls.","type":"Results"},{"text":"The functional LIR motif WEIV in positions 378-381 is inside the disordered fragment region in positions 370-381.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:37:45.055Z"}},{"start":378,"end":381,"reference_id":"27458016","reference_source":"pmid","reference_html":"Structural Basis of Host Autophagy-related Protein 8 (ATG8) Binding by the Irish Potato Famine Pathogen Effector Protein PexRD54. <i> Maqbool A, Hughes RK, Dagdas YF, Tregidgo N, Zess E, Belhaj K, Round A, Bozkurt TO, Kamoun S, Banfield MJ. </i> J Biol Chem, 2016","date":"2022-06-21T15:36:53.690Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001247","ec_ontology":"ECO","ec_name":"point mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"M1C146","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03676r005","statement":[{"text":"Site-directed mutagenesis of the PexRD54 C-terminal AIM region, and ATG8CL binding to a PexRD54 AIM-based peptide array, mapped the key residues that define the PexRD54-ATG8CL interface.","type":"Introduction"},{"text":"First, we used alanine-scanning mutagenesis to substitute Ala at six positions in the PexRD54 AIM region, Pro-373, Asp-377, Trp-378, Glu-379, Ile-380, and Val-381. Each of these proteins was expressed and purified as described for wild type. We then used analytical gel filtration to qualitatively assay whether these variants support complex formation with ATG8CL. As predicted, we did not observe interaction of PexRD54 W378A with ATG8CL (Fig. 7). For each of the other mutations, we still observed an interaction with ATG8CL, including PexRD54 V381A.","type":"Results"},{"text":"FIGURE 4. Crystal structure of ATG8CL bound to the PexRD54(377–381)-peptide and specificity of peptide binding. A, schematic representation of ATG8CL/PexRD54(377–381)-peptide complex highlighting key interactions. ATG8CL is shown in magenta schematic representation with the molecular surface that contacts the PexRD54(377–381)-peptide shown in orange. The PexRD54(377–381)-peptide is shown as sticks with yellow carbon atoms. The electron density omit map of the peptide ligand (Fobs − Fcalc map) is shown in blue mesh and contoured at 2 σ. Electrostatic interactions are indicated with black dashed lines. B, results of the peptide array analyzing the effect of single amino acid substitutions (top) at all positions of 10-mer peptide of PexRD54 (Lys-372–Val-381, side). GST-tagged ATG8CL was visualized using an anti-GST-HRP antibody.","type":"Figure"},{"text":"FIGURE 7. Analysis of the interaction between PexRD54 variants and ATG8CL by gel filtration. Analytical gel filtration traces were obtained for PexRD54 variants mutated in the AIM region and incubated with ATG8CL (1:1 mixture). ","type":"Figure"},{"text":"Full-length RFP-PexRD54 and the AIM motif disrupting variant RFP-PexRD54378-AEIA-381 were used as controls.","type":"Results"},{"text":"The functional LIR motif WEIV in positions 378-381 is inside the disordered fragment region in positions 370-381.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:37:47.366Z"}},{"start":378,"end":381,"reference_id":"27458016","reference_source":"pmid","reference_html":"Structural Basis of Host Autophagy-related Protein 8 (ATG8) Binding by the Irish Potato Famine Pathogen Effector Protein PexRD54. <i> Maqbool A, Hughes RK, Dagdas YF, Tregidgo N, Zess E, Belhaj K, Round A, Bozkurt TO, Kamoun S, Banfield MJ. </i> J Biol Chem, 2016","date":"2022-06-21T15:37:08.532Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001247","ec_ontology":"ECO","ec_name":"point mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","region_id":"DP03676r006","statement":[{"text":"Site-directed mutagenesis of the PexRD54 C-terminal AIM region, and ATG8CL binding to a PexRD54 AIM-based peptide array, mapped the key residues that define the PexRD54-ATG8CL interface.","type":"Introduction"},{"text":"First, we used alanine-scanning mutagenesis to substitute Ala at six positions in the PexRD54 AIM region, Pro-373, Asp-377, Trp-378, Glu-379, Ile-380, and Val-381. Each of these proteins was expressed and purified as described for wild type. We then used analytical gel filtration to qualitatively assay whether these variants support complex formation with ATG8CL. As predicted, we did not observe interaction of PexRD54 W378A with ATG8CL (Fig. 7). For each of the other mutations, we still observed an interaction with ATG8CL, including PexRD54 V381A.","type":"Results"},{"text":"FIGURE 4. Crystal structure of ATG8CL bound to the PexRD54(377–381)-peptide and specificity of peptide binding. A, schematic representation of ATG8CL/PexRD54(377–381)-peptide complex highlighting key interactions. ATG8CL is shown in magenta schematic representation with the molecular surface that contacts the PexRD54(377–381)-peptide shown in orange. The PexRD54(377–381)-peptide is shown as sticks with yellow carbon atoms. The electron density omit map of the peptide ligand (Fobs − Fcalc map) is shown in blue mesh and contoured at 2 σ. Electrostatic interactions are indicated with black dashed lines. B, results of the peptide array analyzing the effect of single amino acid substitutions (top) at all positions of 10-mer peptide of PexRD54 (Lys-372–Val-381, side). GST-tagged ATG8CL was visualized using an anti-GST-HRP antibody.","type":"Figure"},{"text":"FIGURE 7. Analysis of the interaction between PexRD54 variants and ATG8CL by gel filtration. Analytical gel filtration traces were obtained for PexRD54 variants mutated in the AIM region and incubated with ATG8CL (1:1 mixture). ","type":"Figure"},{"text":"Full-length RFP-PexRD54 and the AIM motif disrupting variant RFP-PexRD54378-AEIA-381 were used as controls.","type":"Results"},{"text":"The functional LIR motif WEIV in positions 378-381 is inside the disordered fragment region in positions 370-381.","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:37:48.817Z"}},{"start":378,"end":381,"reference_id":"27458016","reference_source":"pmid","reference_html":"Structural Basis of Host Autophagy-related Protein 8 (ATG8) Binding by the Irish Potato Famine Pathogen Effector Protein PexRD54. <i> Maqbool A, Hughes RK, Dagdas YF, Tregidgo N, Zess E, Belhaj K, Round A, Bozkurt TO, Kamoun S, Banfield MJ. </i> J Biol Chem, 2016","date":"2022-06-21T15:42:31.579Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001245","ec_ontology":"ECO","ec_name":"peptide array evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","region_id":"DP03676r007","statement":[{"text":"Site-directed mutagenesis of the PexRD54 C-terminal AIM region, and ATG8CL binding to a PexRD54 AIM-based peptide array, mapped the key residues that define the PexRD54-ATG8CL interface.","type":"Introduction"},{"text":"FIGURE 4. Crystal structure of ATG8CL bound to the PexRD54(377–381)-peptide and specificity of peptide binding. A, schematic representation of ATG8CL/PexRD54(377–381)-peptide complex highlighting key interactions. ATG8CL is shown in magenta schematic representation with the molecular surface that contacts the PexRD54(377–381)-peptide shown in orange. The PexRD54(377–381)-peptide is shown as sticks with yellow carbon atoms. The electron density omit map of the peptide ligand (Fobs − Fcalc map) is shown in blue mesh and contoured at 2 σ. Electrostatic interactions are indicated with black dashed lines. B, results of the peptide array analyzing the effect of single amino acid substitutions (top) at all positions of 10-mer peptide of PexRD54 (Lys-372–Val-381, side). GST-tagged ATG8CL was visualized using an anti-GST-HRP antibody.","type":"Figure"},{"text":"The results of the peptide array clearly highlight the importance of the hydrophobic residues 378 and 381 of the PexRD54 AIM motif (Trp and Val) in binding ATG8CL. For position 378, the strongest binding was seen for Trp and Phe, with limited binding of Tyr and the aliphatic amino acids. Position 381 favors the bulky aliphatic amino acids, with limited binding also observed by bulky hydrophobic residues. Interestingly, with the exception of Pro at position 379, any amino acid can be accommodated at positions 379 and 380, and binding is still observed. Furthermore, any amino acid can be accommodated at positions 372–377 without a significant reduction in binding, suggesting that these residues may only act as a linker between the WY domain region of PexRD54 and the C-terminal AIM motif.","type":"Results"},{"text":"The functional LIR motif WEIV in positions 378-381 is inside the disordered fragment region in positions 370-381.","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:37:58.722Z"}},{"start":378,"end":381,"reference_id":"27458016","reference_source":"pmid","reference_html":"Structural Basis of Host Autophagy-related Protein 8 (ATG8) Binding by the Irish Potato Famine Pathogen Effector Protein PexRD54. <i> Maqbool A, Hughes RK, Dagdas YF, Tregidgo N, Zess E, Belhaj K, Round A, Bozkurt TO, Kamoun S, Banfield MJ. </i> J Biol Chem, 2016","date":"2022-06-21T15:43:14.502Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001245","ec_ontology":"ECO","ec_name":"peptide array evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"M1C146","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03676r008","statement":[{"text":"Site-directed mutagenesis of the PexRD54 C-terminal AIM region, and ATG8CL binding to a PexRD54 AIM-based peptide array, mapped the key residues that define the PexRD54-ATG8CL interface.","type":"Introduction"},{"text":"FIGURE 4. Crystal structure of ATG8CL bound to the PexRD54(377–381)-peptide and specificity of peptide binding. A, schematic representation of ATG8CL/PexRD54(377–381)-peptide complex highlighting key interactions. ATG8CL is shown in magenta schematic representation with the molecular surface that contacts the PexRD54(377–381)-peptide shown in orange. The PexRD54(377–381)-peptide is shown as sticks with yellow carbon atoms. The electron density omit map of the peptide ligand (Fobs − Fcalc map) is shown in blue mesh and contoured at 2 σ. Electrostatic interactions are indicated with black dashed lines. B, results of the peptide array analyzing the effect of single amino acid substitutions (top) at all positions of 10-mer peptide of PexRD54 (Lys-372–Val-381, side). GST-tagged ATG8CL was visualized using an anti-GST-HRP antibody.","type":"Figure"},{"text":"The results of the peptide array clearly highlight the importance of the hydrophobic residues 378 and 381 of the PexRD54 AIM motif (Trp and Val) in binding ATG8CL. For position 378, the strongest binding was seen for Trp and Phe, with limited binding of Tyr and the aliphatic amino acids. Position 381 favors the bulky aliphatic amino acids, with limited binding also observed by bulky hydrophobic residues. Interestingly, with the exception of Pro at position 379, any amino acid can be accommodated at positions 379 and 380, and binding is still observed. Furthermore, any amino acid can be accommodated at positions 372–377 without a significant reduction in binding, suggesting that these residues may only act as a linker between the WY domain region of PexRD54 and the C-terminal AIM motif.","type":"Results"},{"text":"The functional LIR motif WEIV in positions 378-381 is inside the disordered fragment region in positions 370-381.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:38:04.476Z"}},{"start":378,"end":381,"reference_id":"27458016","reference_source":"pmid","reference_html":"Structural Basis of Host Autophagy-related Protein 8 (ATG8) Binding by the Irish Potato Famine Pathogen Effector Protein PexRD54. <i> Maqbool A, Hughes RK, Dagdas YF, Tregidgo N, Zess E, Belhaj K, Round A, Bozkurt TO, Kamoun S, Banfield MJ. </i> J Biol Chem, 2016","date":"2022-06-21T15:55:16.260Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"M1C146","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03676r009","statement":[{"text":"FIGURE 1. Interaction of PexRD54 and ATG8CL proteins in vitro. A, analytical gel filtration traces obtained for PexRD54 (top), ATG8CL (middle), and a 1:1 mixture of the complex (bottom). Insets show SDS-polyacrylamide gels of the fractions collected across the elution peaks. B, gel filtration trace derived from preparative purification of the PexRD54-ATG8CL complex following co-expression in E. coli. Inset, SDS-polyacrylamide gel containing purified complex. C, binding curve derived from SPR single cycle kinetics data for PexRD54 binding to ATG8CL.","type":"Figure"},{"text":"Finally, we used surface plasmon resonance (SPR) to investigate the affinities of complex formation between PexRD54 and ATG8CL (Fig. 1C). Using this technique, we determined that PexRD54 binds to ATG8CL with a Kd of 388 ± 47 nm. The AIM motif disrupting PexRD54378-AEIA-381 variant (where the Trp and Val of the “WEIV” AIM motif are replaced by alanine) did not bind to ATG8CL using SPR, consistent with previous results (35).","type":"Results"},{"text":"The functional LIR motif WEIV in positions 378-381 is inside the disordered fragment region in positions 370-381.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:38:06.278Z"}},{"start":378,"end":381,"reference_id":"27458016","reference_source":"pmid","reference_html":"Structural Basis of Host Autophagy-related Protein 8 (ATG8) Binding by the Irish Potato Famine Pathogen Effector Protein PexRD54. <i> Maqbool A, Hughes RK, Dagdas YF, Tregidgo N, Zess E, Belhaj K, Round A, Bozkurt TO, Kamoun S, Banfield MJ. </i> J Biol Chem, 2016","date":"2022-06-21T15:55:48.656Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"M1C146","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03676r010","statement":[{"text":"FIGURE 1. Interaction of PexRD54 and ATG8CL proteins in vitro. A, analytical gel filtration traces obtained for PexRD54 (top), ATG8CL (middle), and a 1:1 mixture of the complex (bottom). Insets show SDS-polyacrylamide gels of the fractions collected across the elution peaks. B, gel filtration trace derived from preparative purification of the PexRD54-ATG8CL complex following co-expression in E. coli. Inset, SDS-polyacrylamide gel containing purified complex. C, binding curve derived from SPR single cycle kinetics data for PexRD54 binding to ATG8CL.","type":"Figure"},{"text":"Finally, we used surface plasmon resonance (SPR) to investigate the affinities of complex formation between PexRD54 and ATG8CL (Fig. 1C). Using this technique, we determined that PexRD54 binds to ATG8CL with a Kd of 388 ± 47 nm. The AIM motif disrupting PexRD54378-AEIA-381 variant (where the Trp and Val of the “WEIV” AIM motif are replaced by alanine) did not bind to ATG8CL using SPR, consistent with previous results (35).","type":"Results"},{"text":"The functional LIR motif WEIV in positions 378-381 is inside the disordered fragment region in positions 370-381.","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:38:08.182Z"}},{"start":378,"end":381,"reference_id":"27458016","reference_source":"pmid","reference_html":"Structural Basis of Host Autophagy-related Protein 8 (ATG8) Binding by the Irish Potato Famine Pathogen Effector Protein PexRD54. <i> Maqbool A, Hughes RK, Dagdas YF, Tregidgo N, Zess E, Belhaj K, Round A, Bozkurt TO, Kamoun S, Banfield MJ. </i> J Biol Chem, 2016","date":"2022-06-21T16:00:54.378Z","curator_id":"vsagris","curator_name":"Vasileios Sagris","curator_orcid":"0000-0001-6587-8357","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006200","ec_ontology":"ECO","ec_name":"circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"M1C146","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03676r011","statement":[{"text":"The overall fold of the PexRD54378-AEIA-381 variant was equivalent to wild-type protein as assessed by circular dichroism (CD) spectroscopy (Fig. 2).","type":"Results"},{"text":"FIGURE 2.CD spectra of PexRD54. Far-UV CD spectra of wild-type PexRD54 (solid line) and its variant PexRD54378-AEIA-381 (dashed line) confirming similar secondary structure content (predominantly α-helical).","type":"Figure"},{"text":"The functional LIR motif WEIV in positions 378-381 is inside the disordered fragment region in positions 370-381.","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-28T10:38:10.522Z"}}],"regions_counter":11,"released":"2022_06","sequence":"MRFQSIMMLTITCAGTCLAEGLAPSDQAYRPTMTGLKSRLNDPRPLSTATIATSSERFLRFDTVARDTAGNDEERVGPSWLAKVDGLMHKMVTSSLSAEEAQLKVWIQSQIHPRELFGVLSLGKRAAKLDDNPDFVQWLRLVKDFRANNGNQAFSDLDIYYLLLKTNSPEQLKLLFETLRHTPGMTKIGASMEKSLSGNWIRKALEQDTYPTIVYNTLRLKDAGTKLDDTPMFRQWLEYVEKYWNKNAGAFFGDTQMLTLFQKTMTEEEDIIKLVHMLRNNPGMKSHADKLERYLLLTSESSHKTMADVWLKARETPEEVFRILRLAEKQTAAADDNRMLNLWLRYTQTYRDKIDKNAFSDAEALQFFRKAKPLDFDWEIV","taxonomy":["Eukaryota","Sar","Stramenopiles","Oomycota","Peronosporales","Peronosporaceae","Phytophthora"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"PexRD54","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"26765567","url":"http://www.ncbi.nlm.nih.gov/pubmed/26765567","alternativeUrl":"https://europepmc.org/abstract/MED/26765567"}}]},"orfNames":[{"value":"PITG_09316"}]}],"alphafold_very_low_content":0.2230971128608924,"disorder_content":0.031496062992125984,"disprot_consensus":{"full":[{"start":370,"end":381,"type":"D"}],"Structural state":[{"start":370,"end":381,"type":"D"}],"Molecular function":[{"start":377,"end":381,"type":"F"}],"Biological process":[{"start":378,"end":381,"type":"F"}]}},{"disprot_id":"DP03677","acc":"P35193","creator":"vnugnes","date":"2022-05-27T15:39:57.110Z","features":{"pfam":[{"id":"PF12744","name":"Autophagy protein Atg19, Atg8-binding","start":195,"end":413}],"gene3D":[]},"length":415,"name":"Autophagy-related protein 19","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":124,"end":235,"reference_id":"20659891","reference_source":"pmid","reference_html":"Selective transport of alpha-mannosidase by autophagic pathways: structural basis for cargo recognition by Atg19 and Atg34. <i> Watanabe Y, Noda NN, Kumeta H, Suzuki K, Ohsumi Y, Inagaki F. </i> J Biol Chem, 2010","date":"2022-05-27T15:55:58.163Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001191","ec_ontology":"ECO","ec_name":"in vitro cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03677r001","statement":[{"text":"Stable domains in Atg19 were identified by limited proteolysis of the full-length Atg19 (supplemental Fig. S1), which showed that Atg19 comprises at least two structurally stable domains, the N-terminal domain (residues 1–123) and the C-terminal domain (residues 254–367)","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T13:08:48.887Z"}},{"start":124,"end":235,"reference_id":"20659891","reference_source":"pmid","reference_html":"Selective transport of alpha-mannosidase by autophagic pathways: structural basis for cargo recognition by Atg19 and Atg34. <i> Watanabe Y, Noda NN, Kumeta H, Suzuki K, Ohsumi Y, Inagaki F. </i> J Biol Chem, 2010","date":"2022-05-27T17:30:45.028Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"annotation_extensions":[],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P14904","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03677r002","statement":[{"text":"An additional in vitro pulldown assay showed that the coiled coil domain, but not the other two domains, of Atg19 is responsible for binding with the propeptide of prApe1 (Fig. 1B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T13:08:49.769Z"}},{"start":412,"end":415,"reference_id":"27402840","reference_source":"pmid","reference_html":"Accessory Interaction Motifs in the Atg19 Cargo Receptor Enable Strong Binding to the Clustered Ubiquitin-related Atg8 Protein. <i> Abert C, Kontaxis G, Martens S. </i> J Biol Chem, 2016","date":"2024-10-28T15:37:55.264Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0006914","term_name":"autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp412Ala","start":null,"end":null,"position":null}],"cross_refs":[{"db":"LIRcentral","id":"P35193"}],"ec_go":"IMP","region_id":"DP03677r004","statement":[{"text":"We then went on to determine the effect of mutations in the canonical 412WEEL415 LIR on the extent and position of the CSCs in Atg8. To this end, Trp412 was mutated to Ala, and the mutant Atg19 CTD was titrated into labeled Atg8. Consistent with previous data showing that the 412WEEL415 is not essential for Atg8 interaction (24), addition of this mutant CTD still resulted in apparent CSCs (Fig. 3, A and B). Interestingly, the shifts observed for the W412A mutant were in similar positions compared with the wild-type CTD, although Tyr49 of β2 (Lys48-Pro52) was more affected by the W412A mutant Atg19 CTD. This residue is located in the L site and thus may be contacted by the amino acid at position 4 of a LIR motif. It has previously been shown to be involved in receptor binding and autophagic function (26).","type":"Discussion"}],"term_comment":"","term_def":"\"The cellular catabolic process in which cells digest parts of their own cytoplasm; allows for both recycling of macromolecular constituents under conditions of cellular stress and remodeling the intracellular structure for cell differentiation.\" [GOC:autophagy, ISBN:0198547684, PMID:11099404, PMID:9412464]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-11-01T15:38:31.143Z"}},{"start":412,"end":415,"reference_id":"27402840","reference_source":"pmid","reference_html":"Accessory Interaction Motifs in the Atg19 Cargo Receptor Enable Strong Binding to the Clustered Ubiquitin-related Atg8 Protein. <i> Abert C, Kontaxis G, Martens S. </i> J Biol Chem, 2016","date":"2024-10-28T15:41:25.069Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp412Ala","start":null,"end":null,"position":null}],"cross_refs":[{"db":"LIRcentral","id":"P35193"}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P38182","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03677r005","statement":[{"text":"We then went on to determine the effect of mutations in the canonical 412WEEL415 LIR on the extent and position of the CSCs in Atg8. To this end, Trp412 was mutated to Ala, and the mutant Atg19 CTD was titrated into labeled Atg8. Consistent with previous data showing that the 412WEEL415 is not essential for Atg8 interaction (24), addition of this mutant CTD still resulted in apparent CSCs (Fig. 3, A and B). Interestingly, the shifts observed for the W412A mutant were in similar positions compared with the wild-type CTD, although Tyr49 of β2 (Lys48-Pro52) was more affected by the W412A mutant Atg19 CTD. This residue is located in the L site and thus may be contacted by the amino acid at position 4 of a LIR motif. It has previously been shown to be involved in receptor binding and autophagic function (26).","type":"Discussion"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-11-01T15:38:27.848Z"}},{"start":412,"end":415,"reference_id":"19021777","reference_source":"pmid","reference_html":"Structural basis of target recognition by Atg8/LC3 during selective autophagy. <i> Noda NN, Kumeta H, Nakatogawa H, Satoo K, Adachi W, Ishii J, Fujioka Y, Ohsumi Y, Inagaki F. </i> Genes Cells, 2008","date":"2024-10-28T15:47:33.722Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp412Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Furthermore, in vitro pull-down assay using Atg19 mutants showed that both Trp412 and Leu415 residues are required for the interaction with Atg8 (Fig. 2C)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu415Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Furthermore, in vitro pull-down assay using Atg19 mutants showed that both Trp412 and Leu415 residues are required for the interaction with Atg8 (Fig. 2C)."}]}],"cross_refs":[{"db":"LIRcentral","id":"P35193"}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P38182","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03677r006","statement":[{"text":"It was known that the C-terminal six residues of Atg19 are important for the interaction with Atg8 (Shintani et al. 2002). To determine the minimum region of Atg19 required for the interaction with Atg8, we studied their interaction by NMR spectroscopy, which showed that the C-terminal 8 residues are mainly involved in the interaction (Supporting Information Fig. S3A). Furthermore, in vitro pull-down assay using Atg19 mutants showed that both Trp412 and Leu415 residues are required for the interaction with Atg8 (Fig. 2C). In order to further elucidate the interaction between Atg8 and Atg19, we determined the crystal structure of Atg8 complexed with a tetra peptide, WEEL (Fig. 2A, Supporting Information Table S2, Supporting Information Fig. S4).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-11-01T15:38:25.203Z"}},{"start":412,"end":415,"reference_id":"19021777","reference_source":"pmid","reference_html":"Structural basis of target recognition by Atg8/LC3 during selective autophagy. <i> Noda NN, Kumeta H, Nakatogawa H, Satoo K, Adachi W, Ishii J, Fujioka Y, Ohsumi Y, Inagaki F. </i> Genes Cells, 2008","date":"2024-10-28T15:47:51.117Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0006914","term_name":"autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp412Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Furthermore, in vitro pull-down assay using Atg19 mutants showed that both Trp412 and Leu415 residues are required for the interaction with Atg8 (Fig. 2C)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu415Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Furthermore, in vitro pull-down assay using Atg19 mutants showed that both Trp412 and Leu415 residues are required for the interaction with Atg8 (Fig. 2C)."}]}],"cross_refs":[{"db":"LIRcentral","id":"P35193"}],"ec_go":"IMP","region_id":"DP03677r007","statement":[{"text":"It was known that the C-terminal six residues of Atg19 are important for the interaction with Atg8 (Shintani et al. 2002). To determine the minimum region of Atg19 required for the interaction with Atg8, we studied their interaction by NMR spectroscopy, which showed that the C-terminal 8 residues are mainly involved in the interaction (Supporting Information Fig. S3A). Furthermore, in vitro pull-down assay using Atg19 mutants showed that both Trp412 and Leu415 residues are required for the interaction with Atg8 (Fig. 2C). In order to further elucidate the interaction between Atg8 and Atg19, we determined the crystal structure of Atg8 complexed with a tetra peptide, WEEL (Fig. 2A, Supporting Information Table S2, Supporting Information Fig. S4).","type":"Results"}],"term_comment":"","term_def":"\"The cellular catabolic process in which cells digest parts of their own cytoplasm; allows for both recycling of macromolecular constituents under conditions of cellular stress and remodeling the intracellular structure for cell differentiation.\" [GOC:autophagy, ISBN:0198547684, PMID:11099404, PMID:9412464]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-11-01T15:38:24.182Z"}},{"start":364,"end":415,"reference_id":"https://mobidb.org/P35193","reference_source":"mobidb","reference_html":"An Entry Referenced from MobiDB","date":"2024-10-28T15:52:02.725Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008032","ec_ontology":"ECO","ec_name":"curator inference based on intrinsic disorder prediction","unpublished":true,"released":"2024_12","version":0,"region_id":"DP03677r008","statement":[{"text":"Region 364 - 415 is predicted as intrinsically disordered in MobiDB (https://mobidb.org/P35193), as per Annotation source: AlphaFold-disorder.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-11-01T15:38:23.338Z"}}],"regions_counter":8,"released":"2022_06","sequence":"MNNSKTNQQMNTSMGYPLTVYDECNKFQLIVPTLDANIMLWCIGQLSLLNDSNGCKHLFWQPNDKSNVRILLNNYDYGHLFKYLQCQRKCSVYIGEGTLKKYNLTISTSFDNFLDLTPSEEKESLCREDAHEDPVSPKAGSEEEISPNSTSNVVVSRECLDNFMKQLLKLEESLNKLELEQKVTNKEPNHRISGTIDIPEDRSELVNFFTELKTVKQLEDVFQRYHDYERLSQECDSKTEIASDHSKKETKIEVEPPNERSLQITMNQRDNSLYFQLFNNTNSVLAGNCKLKFTDAGDKPTTQIIDMGPHEIGIKEYKEYRYFPYALDLEAGSTIEIENQYGEVIFLGKYGSSPMINLRPPSRLSAESLQASQEPFYSFQIDTLPELDDSSIISTSISLSYDGDDNEKALTWEEL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"dataset":["Autophagy-related proteins","Condensates-related proteins"],"genes":[{"name":{"value":"ATG19"},"synonyms":[{"value":"CVT19"}],"orfNames":[{"value":"O0980"},{"value":"YOL01"}],"olnNames":[{"value":"YOL082W"}]}],"alphafold_very_low_content":0.655421686746988,"disorder_content":0.39518072289156625,"disprot_consensus":{"full":[{"start":124,"end":235,"type":"D"},{"start":364,"end":415,"type":"D"}],"Structural state":[{"start":124,"end":235,"type":"D"},{"start":364,"end":415,"type":"D"}],"Molecular function":[{"start":124,"end":235,"type":"F"},{"start":412,"end":415,"type":"F"}],"Biological process":[{"start":412,"end":415,"type":"F"}]}},{"disprot_id":"DP03680","acc":"P49023","creator":"vnugnes","date":"2022-05-27T18:38:48.313Z","features":{"pfam":[{"id":"PF00412","name":"LIM domain","start":358,"end":413},{"id":"PF00412","name":"LIM domain","start":417,"end":472},{"id":"PF00412","name":"LIM domain","start":476,"end":530},{"id":"PF00412","name":"LIM domain","start":535,"end":590},{"id":"PF03535","name":"Paxillin family","start":5,"end":277}],"gene3D":[]},"length":591,"name":"Paxillin","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":20,"reference_id":"26928467","reference_source":"pmid","reference_html":"Deciphering Mode of Action of Functionally Important Regions in the Intrinsically Disordered Paxillin (Residues 1-313) Using Its Interaction with FAT (Focal Adhesion Targeting Domain of Focal Adhesion Kinase). <i> Neerathilingam M, Bairy SG, Mysore S. </i> PLoS One, 2016","date":"2022-06-07T14:48:09.222Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03680r001","statement":[{"text":"CD spectra of LD1, LD3 and LD5 peptides showed characteristics of random coil (Fig 2a, S3 Table) thus validating that the LD1, LD3 and LD5 motifs could exist as unfolded effector binding sites (not available for interaction) in our study and could fold upon undergoing allosteric changes after binding to their respective targets.","type":"Results"},{"text":"However, LD1, LD3, LD5, B2 and C3 do not show the characteristic peaks of secondary structures, thus may behave as unfolded effector binding sites.","type":"Figure"},{"text":"LD1 region is comprised of residues 1–20.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-08T10:31:51.816Z"}},{"start":213,"end":232,"reference_id":"26928467","reference_source":"pmid","reference_html":"Deciphering Mode of Action of Functionally Important Regions in the Intrinsically Disordered Paxillin (Residues 1-313) Using Its Interaction with FAT (Focal Adhesion Targeting Domain of Focal Adhesion Kinase). <i> Neerathilingam M, Bairy SG, Mysore S. </i> PLoS One, 2016","date":"2022-06-07T14:48:24.414Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03680r002","statement":[{"text":"CD spectra of LD1, LD3 and LD5 peptides showed characteristics of random coil (Fig 2a, S3 Table) thus validating that the LD1, LD3 and LD5 motifs could exist as unfolded effector binding sites (not available for interaction) in our study and could fold upon undergoing allosteric changes after binding to their respective targets.","type":"Results"},{"text":"However, LD1, LD3, LD5, B2 and C3 do not show the characteristic peaks of secondary structures, thus may behave as unfolded effector binding sites.","type":"Figure"},{"text":"LD3 region is cormprised of residues 213–232.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-08T10:31:50.609Z"}},{"start":296,"end":315,"reference_id":"26928467","reference_source":"pmid","reference_html":"Deciphering Mode of Action of Functionally Important Regions in the Intrinsically Disordered Paxillin (Residues 1-313) Using Its Interaction with FAT (Focal Adhesion Targeting Domain of Focal Adhesion Kinase). <i> Neerathilingam M, Bairy SG, Mysore S. </i> PLoS One, 2016","date":"2022-06-08T13:32:46.875Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03680r003","statement":[{"text":"CD spectra of LD1, LD3 and LD5 peptides showed characteristics of random coil (Fig 2a, S3 Table) thus validating that the LD1, LD3 and LD5 motifs could exist as unfolded effector binding sites (not available for interaction) in our study and could fold upon undergoing allosteric changes after binding to their respective targets.","type":"Results"},{"text":"However, LD1, LD3, LD5, B2 and C3 do not show the characteristic peaks of secondary structures, thus may behave as unfolded effector binding sites.","type":"Figure"},{"text":"LD5 region is comprised of residues 296–315.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-08T13:37:57.362Z"}}],"regions_counter":3,"released":"2022_06","sequence":"MDDLDALLADLESTTSHISKRPVFLSEETPYSYPTGNHTYQEIAVPPPVPPPPSSEALNGTILDPLDQWQPSSSRFIHQQPQSSSPVYGSSAKTSSVSNPQDSVGSPCSRVGEEEHVYSFPNKQKSAEPSPTVMSTSLGSNLSELDRLLLELNAVQHNPPGFPADEANSSPPLPGALSPLYGVPETNSPLGGKAGPLTKEKPKRNGGRGLEDVRPSVESLLDELESSVPSPVPAITVNQGEMSSPQRVTSTQQQTRISASSATRELDELMASLSDFKIQGLEQRADGERCWAAGWPRDGGRSSPGGQDEGGFMAQGKTGSSSPPGGPPKPGSQLDSMLGSLQSDLNKLGVATVAKGVCGACKKPIAGQVVTAMGKTWHPEHFVCTHCQEEIGSRNFFERDGQPYCEKDYHNLFSPRCYYCNGPILDKVVTALDRTWHPEHFFCAQCGAFFGPEGFHEKDGKAYCRKDYFDMFAPKCGGCARAILENYISALNTLWHPECFVCRECFTPFVNGSFFEHDGQPYCEVHYHERRGSLCSGCQKPITGRCITAMAKKFHPEHFVCAFCLKQLNKGTFKEQNDKPYCQNCFLKLFC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"PXN"}}],"alphafold_very_low_content":0.4196277495769882,"disorder_content":0.10152284263959391,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"D"},{"start":213,"end":232,"type":"D"},{"start":296,"end":315,"type":"D"}],"Structural state":[{"start":1,"end":20,"type":"D"},{"start":213,"end":232,"type":"D"},{"start":296,"end":315,"type":"D"}]}},{"disprot_id":"DP03681","acc":"P55285","creator":"vnugnes","date":"2022-05-27T19:18:33.854Z","features":{"pfam":[{"id":"PF00028","name":"Cadherin domain","start":68,"end":149},{"id":"PF00028","name":"Cadherin domain","start":164,"end":258},{"id":"PF00028","name":"Cadherin domain","start":273,"end":357},{"id":"PF00028","name":"Cadherin domain","start":390,"end":479},{"id":"PF00028","name":"Cadherin domain","start":492,"end":589},{"id":"PF01049","name":"Cadherin, Y-type LIR-motif","start":723,"end":782}],"gene3D":[]},"length":790,"name":"Cadherin-6","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":592,"end":607,"reference_id":"28526733","reference_source":"pmid","reference_html":"Discovery and Optimization of HKT288, a Cadherin-6-Targeting ADC for the Treatment of Ovarian and Renal Cancers. <i> Bialucha CU, Collins SD, Li X, Saxena P, Zhang X, Dürr C, Lafont B, Prieur P, Shim Y, Mosher R, Lee D, Ostrom L, Hu T, Bilic S, Rajlic IL, Capka V, Jiang W, Wagner JP, Elliott G, Veloso A, Piel JC, Flaherty MM, Mansfield KG, Meseck EK, Rubic-Schneider T, London AS, Tschantz WR, Kurz M, Nguyen D, Bourret A, Meyer MJ, Faris JE, Janatpour MJ, Chan VW, Yoder NC, Catcott KC, McShea MA, Sun X, Gao H, Williams J, Hofmann F, Engelman JA, Ettenberg SA, Sellers WR, Lees E. </i> Cancer Discov, 2017","date":"2022-05-31T12:23:20.820Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5VEB"}],"region_id":"DP03681r001","sample":[{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ABCD","id":"ABCD_AH056","statements":[{"type":"Supplementary material","text":"CDH6 EC5 was sufficient to pull down LTV977 IgG and was used to produce a complex with LTV977 Fab for crystallization."}]}],"sequence_construct":"EFYETFVCEKAKADQLIQTLHAVDKDDPYSGHQFSFSLAPEAASGSNFTIQDNKDNTAGILTRKNGYNRHEMSTYLLPVVISDNDYPVQSSTGTVTVRVCACDHHGNMQSCHAEALIHPLEVLFQ","statement":[{"text":"Lack of electron density in this region, as shown in the PDB, is typical of IDR.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-31T12:25:00.573Z"}}],"regions_counter":1,"released":"2022_06","sequence":"MRTYRYFLLLFWVGQPYPTLSTPLSKRTSGFPAKKRALELSGNSKNELNRSKRSWMWNQFFLLEEYTGSDYQYVGKLHSDQDRGDGSLKYILSGDGAGDLFIINENTGDIQATKRLDREEKPVYILRAQAINRRTGRPVEPESEFIIKIHDINDNEPIFTKEVYTATVPEMSDVGTFVVQVTATDADDPTYGNSAKVVYSILQGQPYFSVESETGIIKTALLNMDRENREQYQVVIQAKDMGGQMGGLSGTTTVNITLTDVNDNPPRFPQSTYQFKTPESSPPGTPIGRIKASDADVGENAEIEYSITDGEGLDMFDVITDQETQEGIITVKKLLDFEKKKVYTLKVEASNPYVEPRFLYLGPFKDSATVRIVVEDVDEPPVFSKLAYILQIREDAQINTTIGSVTAQDPDAARNPVKYSVDRHTDMDRIFNIDSGNGSIFTSKLLDRETLLWHNITVIATEINNPKQSSRVPLYIKVLDVNDNAPEFAEFYETFVCEKAKADQLIQTLHAVDKDDPYSGHQFSFSLAPEAASGSNFTIQDNKDNTAGILTRKNGYNRHEMSTYLLPVVISDNDYPVQSSTGTVTVRVCACDHHGNMQSCHAEALIHPTGLSTGALVAILLCIVILLVTVVLFAALRRQRKKEPLIISKEDIRDNIVSYNDEGGGEEDTQAFDIGTLRNPEAIEDNKLRRDIVPEALFLPRRTPTARDNTDVRDFINQRLKENDTDPTAPPYDSLATYAYEGTGSVADSLSSLESVTTDADQDYDYLSDWGPRFKKLADMYGGVDSDKDS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"CDH6"}}],"alphafold_very_low_content":0.1860759493670886,"disorder_content":0.020253164556962026,"disprot_consensus":{"full":[{"start":592,"end":607,"type":"D"}],"Structural state":[{"start":592,"end":607,"type":"D"}]}},{"disprot_id":"DP03682","acc":"Q13043","creator":"vnugnes","date":"2022-05-27T20:01:54.092Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":31,"end":281},{"id":"PF11629","name":"C terminal SARAH domain of Mst1","start":433,"end":480}],"gene3D":[]},"length":487,"name":"Serine/threonine-protein kinase 4","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":326,"end":401,"reference_id":"17517604","reference_source":"pmid","reference_html":"Structural insight into dimeric interaction of the SARAH domains from Mst1 and RASSF family proteins in the apoptosis pathway. <i> Hwang E, Ryu KS, Pääkkönen K, Güntert P, Cheong HK, Lim DS, Lee JO, Jeon YH, Cheong C. </i> Proc Natl Acad Sci U S A, 2007","date":"2022-05-27T20:07:19.028Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03682r001","statement":[{"text":"We expressed and purified the linker region between the kinase and SARAH domains of Mst1 (residues 326–401), which is also known as the inhibitory domain. By CD and one-dimensional NMR analysis (SI Fig. 8), we found that most of the residues in this region form a disordered structure, which can provide flexibility for domain motions in the Mst1 protein.","type":"Results"},{"text":"The helix and b-sheet contents of the purified linker region of Mst1 were calculated to be 20% and 3%, respectively. These CD data indicate a lack of regular secondary structure in the linker region of human Mst1.","type":"Supplementary material"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T12:05:35.089Z"}},{"start":326,"end":401,"reference_id":"17517604","reference_source":"pmid","reference_html":"Structural insight into dimeric interaction of the SARAH domains from Mst1 and RASSF family proteins in the apoptosis pathway. <i> Hwang E, Ryu KS, Pääkkönen K, Güntert P, Cheong HK, Lim DS, Lee JO, Jeon YH, Cheong C. </i> Proc Natl Acad Sci U S A, 2007","date":"2022-05-27T20:08:38.017Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03682r002","statement":[{"text":"We expressed and purified the linker region between the kinase and SARAH domains of Mst1 (residues 326–401), which is also known as the inhibitory domain. By CD and one-dimensional NMR analysis (SI Fig. 8), we found that most of the residues in this region form a disordered structure, which can provide flexibility for domain motions in the Mst1 protein.","type":"Results"},{"text":"All backbone amide signals appear in a narrow range near 8.0 ppm, and there are no aliphatic signals below 0.7 ppm, indicating the presence of an unfolded structure.","type":"Supplementary material"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T12:05:34.135Z"}},{"start":343,"end":357,"reference_id":"28373298","reference_source":"pmid","reference_html":"MOB1 Mediated Phospho-recognition in the Core Mammalian Hippo Pathway. <i> Couzens AL, Xiong S, Knight JDR, Mao DY, Guettler S, Picaud S, Kurinov I, Filippakopoulos P, Sicheri F, Gingras AC. </i> Mol Cell Proteomics, 2017","date":"2022-05-27T20:34:00.730Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006277","ec_ontology":"ECO","ec_name":"fluorescence polarization evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"annotation_extensions":[],"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":345,"end":345,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":346,"end":346,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":348,"end":348,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":353,"end":353,"position":"Specific residue"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9H8S9","operator":null,"partner_start":2,"partner_end":216}],"region_id":"DP03682r003","sequence_construct":"VASTMTDGANTMIEH","statement":[{"text":"MST1 T353 and T367 peptides displayed high phospho-dependent binding affinities for MOB1A, with Kds of 280 nm and 680 nm for the phosphorylated peptides, respectively, and no detectable binding for the nonphosphorylated peptides (Fig. 2A).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T13:29:12.847Z"}},{"start":358,"end":372,"reference_id":"28373298","reference_source":"pmid","reference_html":"MOB1 Mediated Phospho-recognition in the Core Mammalian Hippo Pathway. <i> Couzens AL, Xiong S, Knight JDR, Mao DY, Guettler S, Picaud S, Kurinov I, Filippakopoulos P, Sicheri F, Gingras AC. </i> Mol Cell Proteomics, 2017","date":"2022-05-31T12:15:59.225Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006277","ec_ontology":"ECO","ec_name":"fluorescence polarization evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"annotation_extensions":[],"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":360,"end":360,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":363,"end":363,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":367,"end":367,"position":"Specific residue"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9H8S9","operator":null,"partner_start":2,"partner_end":216}],"region_id":"DP03682r004","sequence_construct":"DDTLPSQLGTMVINA","statement":[{"text":"MST1 T353 and T367 peptides displayed high phospho-dependent binding affinities for MOB1A, with Kds of 280 nm and 680 nm for the phosphorylated peptides, respectively, and no detectable binding for the nonphosphorylated peptides (Fig. 2A).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-31T12:22:36.122Z"}},{"start":343,"end":357,"reference_id":"28373298","reference_source":"pmid","reference_html":"MOB1 Mediated Phospho-recognition in the Core Mammalian Hippo Pathway. <i> Couzens AL, Xiong S, Knight JDR, Mao DY, Guettler S, Picaud S, Kurinov I, Filippakopoulos P, Sicheri F, Gingras AC. </i> Mol Cell Proteomics, 2017","date":"2022-05-31T12:20:08.258Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"annotation_extensions":[],"cross_refs":[{"db":"PDB","id":"5TWG"},{"db":"PDB","id":"5TWH"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9H8S9","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03682r005","statement":[{"text":"As predicted by prior mutational data, the MST1 pT353 and pT367 phosphopeptides bound to the MOB1A phospho-binding pocket first identified by Rock et al. (22), with the phosphate of the P0 threonine directly coordinated by K153, R154 and R157.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-31T12:22:34.783Z"}}],"regions_counter":5,"released":"2022_06","sequence":"METVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKSPEQRATATQLLQHPFVRSAKGVSILRDLINEAMDVKLKRQESQQREVDQDDEENSEEDEMDSGTMVRAVGDEMGTVRVASTMTDGANTMIEHDDTLPSQLGTMVINAEDEEEEGTMKRRDETMQPAKPSFLEYFEQKEKENQINSFGKSVPGPLKNSSDWKIPQDGDYEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQSKRQPILDAIEAKKRRQQNF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"STK4"},"synonyms":[{"value":"KRS2"},{"value":"MST1"}]}],"alphafold_very_low_content":0.2464065708418891,"disorder_content":0.15605749486652978,"disprot_consensus":{"full":[{"start":326,"end":401,"type":"D"}],"Structural state":[{"start":326,"end":401,"type":"D"}],"Molecular function":[{"start":343,"end":372,"type":"F"}]}},{"disprot_id":"DP03683","acc":"Q13137","creator":"vnugnes","date":"2022-05-27T20:44:59.476Z","features":{"pfam":[{"id":"PF17751","name":"SKICH domain","start":23,"end":125}],"gene3D":[]},"length":446,"name":"Calcium-binding and coiled-coil domain-containing protein 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":365,"end":413,"reference_id":"26506893","reference_source":"pmid","reference_html":"Molecular basis of ubiquitin recognition by the autophagy receptor CALCOCO2. <i> Xie X, Li F, Wang Y, Wang Y, Lin Z, Cheng X, Liu J, Chen C, Pan L. </i> Autophagy, 2015","date":"2022-05-27T20:46:53.239Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"BMRB","id":"25423"}],"region_id":"DP03683r001","statement":[{"text":"In the final structure, we could well define the extreme C-terminal region including the second ‘CPXC’ motif of CALCOCO2 (residues 414–446, referred hereafter as “ZF2”) that consists of 2 anti-parallel β-strands and a C-terminal α-helix, but we could only define a short α-helix in the ZF1 domain due to its intrinsic dynamic property, whereas the remaining region was too flexible to be well defined (Fig. S2C and D).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-30T13:13:17.596Z"}},{"start":127,"end":141,"reference_id":"34389544","reference_source":"pmid","reference_html":"Structural and biochemical advances on the recruitment of the autophagy-initiating ULK and TBK1 complexes by autophagy receptor NDP52.  <i> Fu T, Zhang M, Zhou Z, Wu P, Peng C, Wang Y, Gong X, Li Y, Wang Y, Xu X, Li M, Shen L, Pan L. </i> Sci Adv, 2021","date":"2022-06-01T13:52:38.904Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"7EAA"}],"region_id":"DP03683r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8TDY2"}],"statement":[{"text":"Unfortunately, despite many attempts, we failed to solve the complex structure either using x-ray crystallography or NMR spectroscopy, likely due to the weak and dynamic nature of this RB1CC1 Claw and NDP52 LIR interaction.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T13:00:33.869Z"}},{"start":129,"end":141,"reference_id":"34389544","reference_source":"pmid","reference_html":"Structural and biochemical advances on the recruitment of the autophagy-initiating ULK and TBK1 complexes by autophagy receptor NDP52.  <i> Fu T, Zhang M, Zhou Z, Wu P, Peng C, Wang Y, Gong X, Li Y, Wang Y, Xu X, Li M, Shen L, Pan L. </i> Sci Adv, 2021","date":"2022-06-02T13:47:35.381Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"annotation_extensions":[],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q8TDY2","operator":null,"partner_start":1490,"partner_end":1594},{"db":"UniProt","id":"Q9H0R8","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9BXW4","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"O95166","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P60520","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9H492","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9GZQ8","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP03683r003","statement":[{"text":"Further fragment truncation analyses together with AGFC-based assays elucidated that the LIR region of NDP52 (residues 129 to 141) can specifically interact with RB1CC1 Claw domain (Fig. 3D and fig. S7D).","type":"Results"},{"text":"To further confirm our hypothesis, we designed a series of NDP52 LIR mutations including the E130A, E131A, D132A, I133S, and V136R mutations of NDP52 LIR, which are corresponding to the critical Claw-binding E6, D7, D8, I9, and L12 residues of NAP1 FIR, respectively (Fig. 4A). As expected, using AGFC- and FP-based assays, we demonstrated that those mutations of NDP52 LIR all significantly disrupt the interaction between NDP52 LIR and RB1CC1 Claw (Fig. 3C and fig. S13, B to F).","type":"Results"},{"text":"(A-F) Analytical gel filtration chromatography-based analyses of the interactions of NDP52 LIR with LC3A (A), LC3B (B), LC3C (C), GABARAP (D), GABARAPL1 (E), and GABARAPL2 (F). These results indicate that NDP52 LIR can directly bind to six different mammalian ATG8 family proteins.","type":"Supplementary material"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T13:00:59.800Z"}},{"start":129,"end":141,"reference_id":"34389544","reference_source":"pmid","reference_html":"Structural and biochemical advances on the recruitment of the autophagy-initiating ULK and TBK1 complexes by autophagy receptor NDP52.  <i> Fu T, Zhang M, Zhou Z, Wu P, Peng C, Wang Y, Gong X, Li Y, Wang Y, Xu X, Li M, Shen L, Pan L. </i> Sci Adv, 2021","date":"2022-06-01T14:12:32.309Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"annotation_extensions":[],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q8TDY2","operator":null,"partner_start":1490,"partner_end":1590}],"region_id":"DP03683r004","statement":[{"text":"Further detailed analyses revealed that the NMR peaks corresponding to the LIR region of NDP52 in the 1H-15N HSQC spectrum of NDP52(10-141) show obvious changes when titrated with the Claw domain of RB1CC1 (Fig. 3G) but display little changes in the presence of RB1CC1(1286-1395) (Fig. 3H), further confirming that the LIR region of NDP52 is directly involved in the interaction with RB1CC1 Claw but not RB1CC1(1286-1395). Collectively, all these data clearly demonstrated that the LIR region of NDP52 contains another RB1CC1-binding site, which can specifically interact with the Claw domain of RB1CC1.","type":"Results"},{"text":"The LIR motif corresponds to de 133-136 residues.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T13:00:58.118Z"}},{"start":135,"end":139,"reference_id":"34389544","reference_source":"pmid","reference_html":"Structural and biochemical advances on the recruitment of the autophagy-initiating ULK and TBK1 complexes by autophagy receptor NDP52.  <i> Fu T, Zhang M, Zhou Z, Wu P, Peng C, Wang Y, Gong X, Li Y, Wang Y, Xu X, Li M, Shen L, Pan L. </i> Sci Adv, 2021","date":"2022-06-02T12:38:47.838Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001202","ec_ontology":"ECO","ec_name":"in vitro protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03683r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UHD2"}],"statement":[{"text":"Using in vitro phosphorylation assays, we confirmed that TBK1 can directly phosphorylate NDP52 (fig. S26). Our mass spectrometry (MS) analysis revealed that the conserved T137 residue within the NDP52 LIR region can be readily phosphorylated by TBK1 (Fig. 8A).","type":"Results"},{"text":"Together, all the above biochemical and structural results clearly demonstrated that TBK1-mediated phosphorylation of T137 in the LIR region of NDP52 can regulate the interactions of NDP52 with ATG8 family proteins.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T13:00:56.934Z"}},{"start":128,"end":140,"reference_id":"34389544","reference_source":"pmid","reference_html":"Structural and biochemical advances on the recruitment of the autophagy-initiating ULK and TBK1 complexes by autophagy receptor NDP52.  <i> Fu T, Zhang M, Zhou Z, Wu P, Peng C, Wang Y, Gong X, Li Y, Wang Y, Xu X, Li M, Shen L, Pan L. </i> Sci Adv, 2021","date":"2022-06-02T13:54:06.828Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006277","ec_ontology":"ECO","ec_name":"fluorescence polarization evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"annotation_extensions":[],"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":137,"end":137,"position":"Specific residue"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q8TDY2","operator":null,"partner_start":1490,"partner_end":1590},{"db":"UniProt","id":"Q9BXW4","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9H0R8","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"O95166","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P60520","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9H492","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9GZQ8","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP03683r006","sequence_construct":"ENEEDILVVTTQG","statement":[{"text":"Consistent with our structure and sequence analyses, further quantitative FP assays uncovered that the synthetic T137-phosphorylated NDP52 LIR peptide (“ENEEDILVVpTTQG,” referred to as phos-NDP52 LIR) displays a much stronger binding ability toward ATG8 family protein than that of the unphosphorylated NDP52 LIR peptide (Fig. 8B and fig. S23).","type":"Results"},{"text":"Notably, further FP-based assays revealed that the T137-phosphorylated and unphosphorylated NDP52 LIR peptides display similar binding affinities to the RB1CC1 Claw domain (fig. S27D), and the T137-phosphorylated NDP52 LIR peptide has a much higher binding affinity to LC3C than RB1CC1 (Fig. 8B and fig. S27D).","type":"Results"},{"text":"Supplementary material shows increasing binding affinities with  LC3A, LC3B, GABARAP, GABARAPL1, and GABARAPL2, when residue T137 is phosphorylated.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T13:00:54.378Z"}},{"start":127,"end":141,"reference_id":"34389544","reference_source":"pmid","reference_html":"Structural and biochemical advances on the recruitment of the autophagy-initiating ULK and TBK1 complexes by autophagy receptor NDP52.  <i> Fu T, Zhang M, Zhou Z, Wu P, Peng C, Wang Y, Gong X, Li Y, Wang Y, Xu X, Li M, Shen L, Pan L. </i> Sci Adv, 2021","date":"2022-06-02T13:22:42.437Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03683r007","statement":[{"text":"Since the NDP52 SKICH domain had been well assigned in the 1H-15N HSQC spectrum of NDP52(10-126) in our previous study (36), therefore, we could easily differentiate the NMR peaks corresponding to the LIR region from that of the SKICH domain in the 1H-15N HSQC spectrum of NDP52(10-141) by comparing the two 1H-15N HSQC spectra of NDP52(10-141) and NDP52(10-126) (fig. S8).","type":"Results"},{"text":"Figure S8 indicates that 127-141 is a disorder region.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T13:00:32.556Z"}},{"start":130,"end":140,"reference_id":"23022382","reference_source":"pmid","reference_html":"LC3C, bound selectively by a noncanonical LIR motif in NDP52, is required for antibacterial autophagy. <i> von Muhlinen N, Akutsu M, Ravenhill BJ, Foeglein Á, Bloor S, Rutherford TJ, Freund SM, Komander D, Randow F. </i> Mol Cell, 2012","date":"2022-06-06T12:50:27.152Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9BXW4","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03683r008","statement":[{"text":"Addition of unlabeled LC3C to 15N-labeled NDP52 (both at 150 μM) resulted in intensity attenuation of several resonances in the C-terminal region of NDP52, i.e., residues 130–140 (Figure 3B), indicating specific interaction of LC3C with this region, consistent with domain mapping data (Figure 3A). Quantification of signal intensities revealed that three residues, Leu134, Val135, and Val136, were attenuated most severely, suggesting they directly contribute to LC3C binding (Figure 3C).","type":"Discussion"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T13:00:51.519Z"}},{"start":131,"end":137,"reference_id":"23022382","reference_source":"pmid","reference_html":"LC3C, bound selectively by a noncanonical LIR motif in NDP52, is required for antibacterial autophagy. <i> von Muhlinen N, Akutsu M, Ravenhill BJ, Foeglein Á, Bloor S, Rutherford TJ, Freund SM, Komander D, Randow F. </i> Mol Cell, 2012","date":"2022-06-06T12:50:13.382Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001227","ec_ontology":"ECO","ec_name":"luminescence-based mammalian interactome mapping assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9BXW4","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03683r009","statement":[{"text":"To identify residues essential for the binding of LC3C in vitro, amino acids 132–137 of NDP52 were mutated individually to Ala or Ser in the context of full-length protein. Mutations of Leu134, Val135, or Val136, but not of Ile133 or other surrounding residues abrogated the interaction of NDP52 with LC3C in a LUMIER assay (Figure 3D).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T13:00:50.052Z"}},{"start":131,"end":137,"reference_id":"23022382","reference_source":"pmid","reference_html":"LC3C, bound selectively by a noncanonical LIR motif in NDP52, is required for antibacterial autophagy. <i> von Muhlinen N, Akutsu M, Ravenhill BJ, Foeglein Á, Bloor S, Rutherford TJ, Freund SM, Komander D, Randow F. </i> Mol Cell, 2012","date":"2022-06-06T12:50:41.898Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001585","ec_ontology":"ECO","ec_name":"small interfering RNA knockdown evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q9BXW4","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03683r010","statement":[{"text":"To test the importance of the NDP52-LC3C interaction in vivo, we complemented cells lacking NDP52 with NDP52 alleles that differ in their ability to bind LC3C. Recruitment of LC3C and LC3B to S. Typhimurium was re-established upon complementation with wild-type NDP52 but not with NDP52 V136S, which demonstrates the crucial importance of the NDP52-LC3C interaction for antibacterial autophagy (Figure 3E).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T13:00:48.833Z"}},{"start":131,"end":137,"reference_id":"23022382","reference_source":"pmid","reference_html":"LC3C, bound selectively by a noncanonical LIR motif in NDP52, is required for antibacterial autophagy. <i> von Muhlinen N, Akutsu M, Ravenhill BJ, Foeglein Á, Bloor S, Rutherford TJ, Freund SM, Komander D, Randow F. </i> Mol Cell, 2012","date":"2022-06-06T12:51:08.667Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0098792","term_name":"xenophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001585","ec_ontology":"ECO","ec_name":"small interfering RNA knockdown evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IMP","region_id":"DP03683r011","statement":[{"text":"To test the importance of the NDP52-LC3C interaction in vivo, we complemented cells lacking NDP52 with NDP52 alleles that differ in their ability to bind LC3C. Recruitment of LC3C and LC3B to S. Typhimurium was re-established upon complementation with wild-type NDP52 but not with NDP52 V136S, which demonstrates the crucial importance of the NDP52-LC3C interaction for antibacterial autophagy (Figure 3E).","type":"Results"}],"term_comment":"While making xenophagy a subclass of (macro)autophagy may seem to directly contradict the definition of autophagy (literally self eating), it is clear that the same pathway is involved as in macroautophagy that doesn't target foreign material: formation of double-membrane-bounded autophagosomes that enclose a region of cytoplasm for degradation.","term_def":"\"The selective autophagy process in which a region of cytoplasm containing an intracellular pathogen or some part of an intracellular pathogen (e.g. viral capsid) is enclosed in a double membrane bound autophagosome, which then fuses with the lysosome leading to degradation of the contents.\" [GOC:autophagy, GOC:pad, GOC:PARL, PMID:19802565, PMID:20159618, PMID:25497060]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T13:00:47.733Z"}},{"start":133,"end":137,"reference_id":"23022382","reference_source":"pmid","reference_html":"LC3C, bound selectively by a noncanonical LIR motif in NDP52, is required for antibacterial autophagy. <i> von Muhlinen N, Akutsu M, Ravenhill BJ, Foeglein Á, Bloor S, Rutherford TJ, Freund SM, Komander D, Randow F. </i> Mol Cell, 2012","date":"2022-06-06T12:51:25.682Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9BXW4","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03683r012","statement":[{"text":"These data, in combination with our NMR measurements, define the tripeptide Leu-Val-Val in the linker region between SKICH and coiled-coil domain as the essential CLIR motif for binding to LC3C. This tripeptide is predicted to form a β strand, like the canonical Trp-Xaa-Xaa-Leu LIR motif, but lacks the aromatic residue found in canonical LIR motifs (Figure 3F).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T13:00:46.534Z"}},{"start":128,"end":141,"reference_id":"23022382","reference_source":"pmid","reference_html":"LC3C, bound selectively by a noncanonical LIR motif in NDP52, is required for antibacterial autophagy. <i> von Muhlinen N, Akutsu M, Ravenhill BJ, Foeglein Á, Bloor S, Rutherford TJ, Freund SM, Komander D, Randow F. </i> Mol Cell, 2012","date":"2022-06-06T12:52:14.974Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005632","ec_ontology":"ECO","ec_name":"fluorescence anisotropy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"Q9BXW4","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9H492","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP03683r013","statement":[{"text":"The CLIR peptide bound LC3C with a KD of 1.6 μM, while LC3A was bound with ∼10x lower affinity (15.1 μM) (Figures 5B and 5C). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T13:00:45.401Z"}},{"start":128,"end":141,"reference_id":"23022382","reference_source":"pmid","reference_html":"LC3C, bound selectively by a noncanonical LIR motif in NDP52, is required for antibacterial autophagy. <i> von Muhlinen N, Akutsu M, Ravenhill BJ, Foeglein Á, Bloor S, Rutherford TJ, Freund SM, Komander D, Randow F. </i> Mol Cell, 2012","date":"2022-06-06T12:53:11.578Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile133Trp","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To understand the relative contribution of the aromatic pocket to the binding of LIR and CLIR peptides, we replaced Ile133 in the CLIR peptide with Trp."}]}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q9BXW4","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9H492","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP03683r014","sequence_construct":"ENEEDWLVVTTQGE","statement":[{"text":"LC3C bound CLIRI133W with 14-fold higher affinity than the CLIRWT peptide, resulting in the highest affinity LC3 interaction reported so far (KD = 110 nM) (Figure 5B). Importantly, the CLIRI133W peptide also bound LC3A with high affinity (290 nM), which represents a > 50-fold improvement over CLIRWT (Figure 5C). However, the specificity of NDP52 for LC3C over LC3A, defined as the ratio of KD values, diminished from 10-fold to 3-fold (Figure 5C).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T13:00:43.818Z"}},{"start":128,"end":141,"reference_id":"23022382","reference_source":"pmid","reference_html":"LC3C, bound selectively by a noncanonical LIR motif in NDP52, is required for antibacterial autophagy. <i> von Muhlinen N, Akutsu M, Ravenhill BJ, Foeglein Á, Bloor S, Rutherford TJ, Freund SM, Komander D, Randow F. </i> Mol Cell, 2012","date":"2022-06-06T12:54:04.079Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001227","ec_ontology":"ECO","ec_name":"luminescence-based mammalian interactome mapping assay evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile133Trp","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To understand the relative contribution of the aromatic pocket to the binding of LIR and CLIR peptides, we replaced Ile133 in the CLIR peptide with Trp."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9BXW4","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9H492","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9GZQ8","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"O95166","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9H0R8","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P60520","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP03683r015","sequence_construct":"MEETIKDPPTSAVLLDHCHFSQVIFNSVEKFYIPGGDVTCHYTFTQHFIPRRKDWIGIFRVGWKTTREYYTFMWVTLPIDLNNKSAKQQEVQFKAYYLPKDDEYYQFCYVDEDGVVRGASIPFQFRPENEEDWLVVTTQGEEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLSYMGLDFNSLPYQVPTSDEGGARQNPGLAYGNPYSGIQESSSPSPLSIKKCPICKADDICDHTLEQQQMQPLCFNCPICDKIFPATEKQIFEDHVFC","statement":[{"text":"In contrast to the preferential interaction of wild-type NDP52 with LC3C, we observed strong and nonselective binding of NDP52I133W to all human ATG8 orthologs (Figure 5D). These data show that the NDP52 CLIR motif comprising a Leu-Val-Val sequence is able to distinguish efficiently between LC3C and its paralogs, and that mutation of the CLIR to utilize the aromatic pocket (CLIRI133W) enhances affinity but reduces the specificity for LC3C.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T13:00:39.601Z"}},{"start":134,"end":136,"reference_id":"23022382","reference_source":"pmid","reference_html":"LC3C, bound selectively by a noncanonical LIR motif in NDP52, is required for antibacterial autophagy. <i> von Muhlinen N, Akutsu M, Ravenhill BJ, Foeglein Á, Bloor S, Rutherford TJ, Freund SM, Komander D, Randow F. </i> Mol Cell, 2012","date":"2022-07-12T08:40:49.213Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001227","ec_ontology":"ECO","ec_name":"luminescence-based mammalian interactome mapping assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9BXW4","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03683r016","statement":[{"text":"LC3C, Bound Selectively by a Noncanonical LIR Motif in NDP52, Is Required for Antibacterial Autophagy","type":"Title"},{"text":"To identify residues essential for the binding of LC3C in vitro, amino acids 132–137 of NDP52 were mutated individually to Ala or Ser in the context of full-length protein. Mutations of Leu134, Val135, or Val136, but not of Ile133 or other surrounding residues abrogated the interaction of NDP52 with LC3C in a LUMIER assay (Figure 3D).","type":"Results"},{"text":"Region corresponding to the non canonical LIR motif \"LVV\" at position 134-136","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp132Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile133Ser","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu134Ser","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val135Ser","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val136Ser","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr137Ala","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-18T13:00:06.001Z"}},{"start":134,"end":136,"reference_id":"23022382","reference_source":"pmid","reference_html":"LC3C, bound selectively by a noncanonical LIR motif in NDP52, is required for antibacterial autophagy. <i> von Muhlinen N, Akutsu M, Ravenhill BJ, Foeglein Á, Bloor S, Rutherford TJ, Freund SM, Komander D, Randow F. </i> Mol Cell, 2012","date":"2022-07-12T08:49:40.276Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9BXW4","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03683r019","statement":[{"text":"LC3C, Bound Selectively by a Noncanonical LIR Motif in NDP52, Is Required for Antibacterial Autophagy","type":"Title"},{"text":"Addition of unlabeled LC3C to 15N-labeled NDP52 (both at 150 μM) resulted in intensity attenuation of several resonances in the C-terminal region of NDP52, i.e., residues 130–140 (Figure 3B), indicating specific interaction of LC3C with this region, consistent with domain mapping data (Figure 3A). Quantification of signal intensities revealed that three residues, Leu134, Val135, and Val136, were attenuated most severely, suggesting they directly contribute to LC3C binding (Figure 3C).","type":"Results"},{"text":"Region corresponding to the non canonical LIR motif \"LVV\" at position 134-136","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-18T13:01:33.512Z"}}],"regions_counter":19,"released":"2022_06","sequence":"MEETIKDPPTSAVLLDHCHFSQVIFNSVEKFYIPGGDVTCHYTFTQHFIPRRKDWIGIFRVGWKTTREYYTFMWVTLPIDLNNKSAKQQEVQFKAYYLPKDDEYYQFCYVDEDGVVRGASIPFQFRPENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLSYMGLDFNSLPYQVPTSDEGGARQNPGLAYGNPYSGIQESSSPSPLSIKKCPICKADDICDHTLEQQQMQPLCFNCPICDKIFPATEKQIFEDHVFCHSL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"CALCOCO2"},"synonyms":[{"value":"NDP52","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"7540613","url":"http://www.ncbi.nlm.nih.gov/pubmed/7540613","alternativeUrl":"https://europepmc.org/abstract/MED/7540613"}}]}]}],"alphafold_very_low_content":0.18834080717488788,"disorder_content":0.14349775784753363,"disprot_consensus":{"full":[{"start":127,"end":141,"type":"D"},{"start":365,"end":413,"type":"D"}],"Structural state":[{"start":127,"end":141,"type":"D"},{"start":365,"end":413,"type":"D"}],"Molecular function":[{"start":128,"end":141,"type":"F"}],"Disorder function":[{"start":135,"end":139,"type":"F"}],"Biological process":[{"start":131,"end":137,"type":"F"}]}},{"disprot_id":"DP03684","acc":"P40458","creator":"cpintado","date":"2022-05-30T10:29:42.497Z","features":{"pfam":[{"id":"PF29921","name":"Autophagy-related protein 32 middle domain","start":220,"end":346}],"gene3D":[]},"length":529,"name":"Autophagy-related protein 32","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":200,"end":215,"reference_id":"29909755","reference_source":"pmid","reference_html":"A pseudo-receiver domain in Atg32 is required for mitophagy. <i> Xia X, Katzenell S, Reinhart EF, Bauer KM, Pellegrini M, Ragusa MJ. </i> Autophagy, 2018","date":"2022-05-30T10:30:35.224Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5WLP"}],"region_id":"DP03684r001","statement":[{"text":"The first 16 residues of Atg32[200–341] appeared disordered in the structure.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-27T19:15:40.639Z"}}],"regions_counter":2,"released":"2022_06","sequence":"MVLEYQQREGKGSSSKSMPPDSSSTTIHTCSEAQTGEDKGLLDPHLSVLELLSKTGHSPSPMGQNLVTSIDISGNHNVNDSISGSWQAIQPLDLGASFIPERCSSQTTNGSILSSSDTSEEEQELLQAPAADIINIIKQGQEGANVVSPSHPFKQLQKIISLPLPGKEKTPFNEQDDDGDEDEAFEEDSVTITKSLTSSTNSFVMPKLSLTQKNPVFRLLILGRTGSSFYQSIPKEYQSLFELPKYHDSATFPQYTGIVIIFQELREMVSLLNRIVQYSQGKPVIPICQPGQVIQVKNVLKSFLRNKLVKLLFPPVVVTNKRDLKKMFQRLQDLSLEYGEDVNEEDNDDEAIHTKSRSYCRNKKAENSKKKSPKSNKKPKRKKQKFFTSWFTWGISITIGISFGCCVTYFVTAAYEHQTVKSLSLRPSILASLLSLDSSSDTINTPATASPSSTEQFLWFDKGTLQINFHSDGFIMKSLTIIKETWGKMNTFVLHALSKPLKFLENLNKSSEFSIDESNRILALGYILL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"ATG32"},"synonyms":[{"value":"ECM17"}],"olnNames":[{"value":"YIL146C"}]}],"alphafold_very_low_content":0.5311909262759924,"disorder_content":0.030245746691871456,"disprot_consensus":{"full":[{"start":200,"end":215,"type":"D"}],"Structural state":[{"start":200,"end":215,"type":"D"}]}},{"disprot_id":"DP03685","acc":"P38428","creator":"cpintado","date":"2022-05-30T10:53:25.345Z","features":{"pfam":[{"id":"PF02845","name":"CUE domain","start":67,"end":105},{"id":"PF18499","name":"Ubc7p-binding region of Cue1","start":151,"end":202}],"gene3D":[]},"length":203,"name":"Coupling of ubiquitin conjugation to ER degradation protein 1","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":45,"end":65,"reference_id":"27264873","reference_source":"pmid","reference_html":"The CUE Domain of Cue1 Aligns Growing Ubiquitin Chains with Ubc7 for Rapid Elongation. <i> von Delbrück M, Kniss A, Rogov VV, Pluska L, Bagola K, Löhr F, Güntert P, Sommer T, Dötsch V. </i> Mol Cell, 2016","date":"2022-07-15T09:31:39.595Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2MYX"}],"region_id":"DP03685r001","statement":[{"text":"The PDB structure from NMR indicates that the region 45-65 is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-15T13:26:56.566Z"}}],"regions_counter":2,"released":"2023_12","sequence":"MEDSRLLITLILVFGVIFLKKFFQSNQHPSAQRLSATGVNAHGRPQGSTQNALRRTGRVNGGHPVTTQMVETVQNLAPNLHPEQIRYSLENTGSVEETVERYLRGDEFSFPPGFEPSRAPMGANAAVDNNAAGGGEFNDPRKKNMICAENLLDKFHVDLNEDMSNLSFKDLDIEERKRLLVWQARKNLETKLQSDKDLQSLLT","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"genes":[{"name":{"value":"CUE1"},"synonyms":[{"value":"KIS4"}],"orfNames":[{"value":"YM8156.06"}],"olnNames":[{"value":"YMR264W"}]}],"alphafold_very_low_content":0.1724137931034483,"disorder_content":0.10344827586206896,"disprot_consensus":{"full":[{"start":45,"end":65,"type":"D"}],"Structural state":[{"start":45,"end":65,"type":"D"}]}},{"disprot_id":"DP03686","acc":"Q5ZUV9","creator":"jnilsson","date":"2022-05-30T14:42:55.446Z","features":{"pfam":[{"id":"PF22225","name":"RavZ C-terminal PI3P-binding domain","start":329,"end":429},{"id":"PF24600","name":"RavZ catalytic domain","start":50,"end":307}],"gene3D":[]},"length":502,"name":"Cysteine protease RavZ","ncbi_taxon_id":272624,"organism":"Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)","regions":[{"start":442,"end":458,"reference_id":"26343456","reference_source":"pmid","reference_html":"The Legionella Anti-autophagy Effector RavZ Targets the Autophagosome via PI3P- and Curvature-Sensing Motifs. <i> Horenkamp FA, Kauffman KJ, Kohler LJ, Sherwood RK, Krueger KP, Shteyn V, Roy CR, Melia TJ, Reinisch KM. </i> Dev Cell, 2015","date":"2022-05-31T11:23:09.781Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5CQC"}],"region_id":"DP03686r001","statement":[{"text":"The N- and C-terminal-most residues and four flexible regions (residues 92–95, 249–253, 278–287, and 347–356) of RavZcrystal lacked defined electron density and were not modeled. ","type":"Results"},{"text":"Notice that the crystallization construct RavZ crystal used comprises residues 10–458. It lacks sequences predicted to be disordered, including the N and C termini (residues 1–9 and 459–502) and two loops (residues 23–43 and 430–440).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-31T11:44:03.920Z"}},{"start":1,"end":46,"reference_id":"28395732","reference_source":"pmid","reference_html":"Elucidation of the anti-autophagy mechanism of the Legionella effector RavZ using semisynthetic LC3 proteins.  <i> Yang A, Pantoom S, Wu YW. </i> Elife, 2017","date":"2022-05-31T11:23:49.523Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5MS8"},{"db":"PDB","id":"5MS7"}],"region_id":"DP03686r002","statement":[{"text":"RavZ structures of both fragments are resolved from residues 47 to 433 and 48 to 432, respectively, whereas the missing regions at the N- and C-termini (residues 1–47 and 433–502) might be flexible and disordered.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-31T11:44:00.937Z"}},{"start":433,"end":502,"reference_id":"28395732","reference_source":"pmid","reference_html":"Elucidation of the anti-autophagy mechanism of the Legionella effector RavZ using semisynthetic LC3 proteins.  <i> Yang A, Pantoom S, Wu YW. </i> Elife, 2017","date":"2022-05-31T11:24:16.827Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5MS8"},{"db":"PDB","id":"5MS7"}],"region_id":"DP03686r003","statement":[{"text":"RavZ structures of both fragments are resolved from residues 47 to 433 and 48 to 432, respectively, whereas the missing regions at the N- and C-termini (residues 1–47 and 433–502) might be flexible and disordered.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-31T11:43:59.603Z"}},{"start":10,"end":21,"reference_id":"26343456","reference_source":"pmid","reference_html":"The Legionella Anti-autophagy Effector RavZ Targets the Autophagosome via PI3P- and Curvature-Sensing Motifs. <i> Horenkamp FA, Kauffman KJ, Kohler LJ, Sherwood RK, Krueger KP, Shteyn V, Roy CR, Melia TJ, Reinisch KM. </i> Dev Cell, 2015","date":"2022-05-31T11:08:16.251Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5CQC"}],"region_id":"DP03686r004","statement":[{"text":"The N- and C-terminal-most residues and four flexible regions (residues 92–95, 249–253, 278–287, and 347–356) of RavZcrystal lacked defined electron density and were not modeled.","type":"Results"},{"text":" The crystallization construct RavZcrystal is active in an Atg8/LC3 delipidation assay ((Choy et al., 2012), Figure 1A-B) and comprises residues 10-458. It lacks sequences predicted to be disordered, including the N- and C-termini (residues 1-9, 459-502) and two loops (residues 23-43, 430-440). ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-31T11:43:57.669Z"}},{"start":278,"end":287,"reference_id":"26343456","reference_source":"pmid","reference_html":"The Legionella Anti-autophagy Effector RavZ Targets the Autophagosome via PI3P- and Curvature-Sensing Motifs. <i> Horenkamp FA, Kauffman KJ, Kohler LJ, Sherwood RK, Krueger KP, Shteyn V, Roy CR, Melia TJ, Reinisch KM. </i> Dev Cell, 2015","date":"2022-05-31T11:11:22.530Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5CQC"}],"region_id":"DP03686r005","statement":[{"text":"The N- and C-terminal-most residues and four flexible regions (residues 92–95, 249–253, 278–287, and 347–356) of RavZcrystal lacked defined electron density and were not modeled.","type":"Results"},{"text":" The crystallization construct RavZcrystal is active in an Atg8/LC3 delipidation assay ((Choy et al., 2012), Figure 1A-B) and comprises residues 10-458. It lacks sequences predicted to be disordered, including the N- and C-termini (residues 1-9, 459-502) and two loops (residues 23-43, 430-440). ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-31T11:43:56.353Z"}},{"start":347,"end":357,"reference_id":"26343456","reference_source":"pmid","reference_html":"The Legionella Anti-autophagy Effector RavZ Targets the Autophagosome via PI3P- and Curvature-Sensing Motifs. <i> Horenkamp FA, Kauffman KJ, Kohler LJ, Sherwood RK, Krueger KP, Shteyn V, Roy CR, Melia TJ, Reinisch KM. </i> Dev Cell, 2015","date":"2022-05-31T11:25:23.319Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5CQC"}],"region_id":"DP03686r006","statement":[{"text":"The N- and C-terminal-most residues and four flexible regions (residues 92–95, 249–253, 278–287, and 347–356) of RavZcrystal lacked defined electron density and were not modeled.","type":"Results"},{"text":" The crystallization construct RavZcrystal is active in an Atg8/LC3 delipidation assay ((Choy et al., 2012), Figure 1A-B) and comprises residues 10-458. It lacks sequences predicted to be disordered, including the N- and C-termini (residues 1-9, 459-502) and two loops (residues 23-43, 430-440). ","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-31T11:43:55.092Z"}},{"start":16,"end":17,"reference_id":"27791457","reference_source":"pmid","reference_html":"The 1:2 complex between RavZ and LC3 reveals a mechanism for deconjugation of LC3 on the phagophore membrane. <i> Kwon DH, Kim S, Jung YO, Roh KH, Kim L, Kim BW, Hong SB, Lee IY, Song JH, Lee WC, Choi EJ, Hwang KY, Song HK. </i> Autophagy, 2017","date":"2022-06-28T10:14:02.120Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140321","term_name":"negative regulation by symbiont of host autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","region_id":"DP03686r007","statement":[{"text":"The binding affinity between the N-terminal region of RavZ and LC3 was higher than that between the C-terminal region and LC3, and interestingly the single second LIR (LIR2) peptide had a similar binding affinity to LC3 as the intact N-terminal peptide containing the 2 LIRs, LIR1 and LIR2 (Fig. 1D). Although there are 2 LIR motifs in the N-terminal region, 2 molecules of LC3 cannot bind to this region simultaneously based on the SEC-MALS results, and the SRP data clearly showed that the LIR2 peptide had stronger binding affinity to LC3 than the LIR1 peptide. RavZ containing only the N-terminal LIRs, N-Cat, had similar binding affinity to LC3 as the single LIR2 peptide or N-terminal peptide, and the almost 50-fold stronger binding affinity between RavZ and LC3 might simply reflect a synergistically increased chance of the interaction.","type":"Results"},{"text":"Annotation related to the accessory LIR motif \"FEEL\".","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"Q9GZQ8","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T13:22:19.053Z"}},{"start":29,"end":32,"reference_id":"27791457","reference_source":"pmid","reference_html":"The 1:2 complex between RavZ and LC3 reveals a mechanism for deconjugation of LC3 on the phagophore membrane. <i> Kwon DH, Kim S, Jung YO, Roh KH, Kim L, Kim BW, Hong SB, Lee IY, Song JH, Lee WC, Choi EJ, Hwang KY, Song HK. </i> Autophagy, 2017","date":"2022-06-28T10:14:08.887Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140321","term_name":"negative regulation by symbiont of host autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","region_id":"DP03686r008","statement":[{"text":"The binding affinity between the N-terminal region of RavZ and LC3 was higher than that between the C-terminal region and LC3, and interestingly the single second LIR (LIR2) peptide had a similar binding affinity to LC3 as the intact N-terminal peptide containing the 2 LIRs, LIR1 and LIR2 (Fig. 1D). Although there are 2 LIR motifs in the N-terminal region, 2 molecules of LC3 cannot bind to this region simultaneously based on the SEC-MALS results, and the SRP data clearly showed that the LIR2 peptide had stronger binding affinity to LC3 than the LIR1 peptide. RavZ containing only the N-terminal LIRs, N-Cat, had similar binding affinity to LC3 as the single LIR2 peptide or N-terminal peptide, and the almost 50-fold stronger binding affinity between RavZ and LC3 might simply reflect a synergistically increased chance of the interaction.","type":"Results"},{"text":"Annotation related to the LIR motif \"FDLL\".","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"Q9GZQ8","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T13:22:22.839Z"}},{"start":29,"end":32,"reference_id":"27791457","reference_source":"pmid","reference_html":"The 1:2 complex between RavZ and LC3 reveals a mechanism for deconjugation of LC3 on the phagophore membrane. <i> Kwon DH, Kim S, Jung YO, Roh KH, Kim L, Kim BW, Hong SB, Lee IY, Song JH, Lee WC, Choi EJ, Hwang KY, Song HK. </i> Autophagy, 2017","date":"2022-06-28T10:14:28.031Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9GZQ8","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03686r009","statement":[{"text":"The binding affinity between the N-terminal region of RavZ and LC3 was higher than that between the C-terminal region and LC3, and interestingly the single second LIR (LIR2) peptide had a similar binding affinity to LC3 as the intact N-terminal peptide containing the 2 LIRs, LIR1 and LIR2 (Fig. 1D). Although there are 2 LIR motifs in the N-terminal region, 2 molecules of LC3 cannot bind to this region simultaneously based on the SEC-MALS results, and the SRP data clearly showed that the LIR2 peptide had stronger binding affinity to LC3 than the LIR1 peptide. RavZ containing only the N-terminal LIRs, N-Cat, had similar binding affinity to LC3 as the single LIR2 peptide or N-terminal peptide, and the almost 50-fold stronger binding affinity between RavZ and LC3 might simply reflect a synergistically increased chance of the interaction.","type":"Results"},{"text":"Annotation related to the LIR motif \"FDLL\".","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T12:36:46.914Z"}},{"start":16,"end":19,"reference_id":"27791457","reference_source":"pmid","reference_html":"The 1:2 complex between RavZ and LC3 reveals a mechanism for deconjugation of LC3 on the phagophore membrane. <i> Kwon DH, Kim S, Jung YO, Roh KH, Kim L, Kim BW, Hong SB, Lee IY, Song JH, Lee WC, Choi EJ, Hwang KY, Song HK. </i> Autophagy, 2017","date":"2022-06-28T10:14:58.843Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9GZQ8","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03686r010","statement":[{"text":"The binding affinity between the N-terminal region of RavZ and LC3 was higher than that between the C-terminal region and LC3, and interestingly the single second LIR (LIR2) peptide had a similar binding affinity to LC3 as the intact N-terminal peptide containing the 2 LIRs, LIR1 and LIR2 (Fig. 1D). Although there are 2 LIR motifs in the N-terminal region, 2 molecules of LC3 cannot bind to this region simultaneously based on the SEC-MALS results, and the SRP data clearly showed that the LIR2 peptide had stronger binding affinity to LC3 than the LIR1 peptide. RavZ containing only the N-terminal LIRs, N-Cat, had similar binding affinity to LC3 as the single LIR2 peptide or N-terminal peptide, and the almost 50-fold stronger binding affinity between RavZ and LC3 might simply reflect a synergistically increased chance of the interaction.","type":"Results"},{"text":"Annotation related to the accessory LIR motif \"FEEL\".","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T12:36:49.868Z"}},{"start":16,"end":19,"reference_id":"27791457","reference_source":"pmid","reference_html":"The 1:2 complex between RavZ and LC3 reveals a mechanism for deconjugation of LC3 on the phagophore membrane. <i> Kwon DH, Kim S, Jung YO, Roh KH, Kim L, Kim BW, Hong SB, Lee IY, Song JH, Lee WC, Choi EJ, Hwang KY, Song HK. </i> Autophagy, 2017","date":"2022-06-28T10:24:42.414Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140321","term_name":"negative regulation by symbiont of host autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe16Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu19Ala","start":null,"end":null,"position":null}],"ec_go":"IDA","region_id":"DP03686r011","statement":[{"text":"The LC3-binding N- and C-terminal regions of RavZ are critical for inhibiting autophagy","type":"Results"},{"text":"We also performed the same experiments with point mutants, mutLIR1, mutLIR2 and mutLIR3, which possess a defect in LC3-binding (Fig. 3A). Based on our in vitro data, all double mutants formed a 1:1 complex with LC3 (Fig. 3B), and therefore must have a lower binding affinity compared with RavZ FL. Quantification of the fluorescence data indicated that a milder effect was shown by the point mutants compared with the deletion mutants (Fig. 4C), with different effects being observed with some of the point mutants.","type":"Results"},{"text":"In conclusion, the flexible N- and C-terminal regions in RavZ, and in particular the LIR motifs, are important for the recognition of LC3–PE conjugates and play a critical role in blocking autophagy in cells.","type":"Results"},{"text":"Annotation related to the accessory LIR motif \"FEEL\".","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.\" [GOC:dph, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T13:22:37.588Z"}},{"start":29,"end":32,"reference_id":"27791457","reference_source":"pmid","reference_html":"The 1:2 complex between RavZ and LC3 reveals a mechanism for deconjugation of LC3 on the phagophore membrane. <i> Kwon DH, Kim S, Jung YO, Roh KH, Kim L, Kim BW, Hong SB, Lee IY, Song JH, Lee WC, Choi EJ, Hwang KY, Song HK. </i> Autophagy, 2017","date":"2022-06-28T10:28:26.220Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140321","term_name":"negative regulation by symbiont of host autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe29Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu32Ala","start":null,"end":null,"position":null}],"ec_go":"IDA","region_id":"DP03686r012","statement":[{"text":"The LC3-binding N- and C-terminal regions of RavZ are critical for inhibiting autophagy","type":"Results"},{"text":"We also performed the same experiments with point mutants, mutLIR1, mutLIR2 and mutLIR3, which possess a defect in LC3-binding (Fig. 3A). Based on our in vitro data, all double mutants formed a 1:1 complex with LC3 (Fig. 3B), and therefore must have a lower binding affinity compared with RavZ FL. Quantification of the fluorescence data indicated that a milder effect was shown by the point mutants compared with the deletion mutants (Fig. 4C), with different effects being observed with some of the point mutants.","type":"Results"},{"text":"In conclusion, the flexible N- and C-terminal regions in RavZ, and in particular the LIR motifs, are important for the recognition of LC3–PE conjugates and play a critical role in blocking autophagy in cells.","type":"Results"},{"text":"Annotation related to the LIR motif \"FDLL\".","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.\" [GOC:dph, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T13:22:40.986Z"}},{"start":435,"end":438,"reference_id":"27791457","reference_source":"pmid","reference_html":"The 1:2 complex between RavZ and LC3 reveals a mechanism for deconjugation of LC3 on the phagophore membrane. <i> Kwon DH, Kim S, Jung YO, Roh KH, Kim L, Kim BW, Hong SB, Lee IY, Song JH, Lee WC, Choi EJ, Hwang KY, Song HK. </i> Autophagy, 2017","date":"2022-06-28T10:29:26.965Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140321","term_name":"negative regulation by symbiont of host autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe435Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu438Ala","start":null,"end":null,"position":null}],"ec_go":"IDA","region_id":"DP03686r013","statement":[{"text":"The LC3-binding N- and C-terminal regions of RavZ are critical for inhibiting autophagy","type":"Results"},{"text":"We also performed the same experiments with point mutants, mutLIR1, mutLIR2 and mutLIR3, which possess a defect in LC3-binding (Fig. 3A). Based on our in vitro data, all double mutants formed a 1:1 complex with LC3 (Fig. 3B), and therefore must have a lower binding affinity compared with RavZ FL. Quantification of the fluorescence data indicated that a milder effect was shown by the point mutants compared with the deletion mutants (Fig. 4C), with different effects being observed with some of the point mutants.","type":"Results"},{"text":"In conclusion, the flexible N- and C-terminal regions in RavZ, and in particular the LIR motifs, are important for the recognition of LC3–PE conjugates and play a critical role in blocking autophagy in cells.","type":"Results"},{"text":"Annotation related to the accessory LIR motif \"FVTI\".","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.\" [GOC:dph, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Vasilis J Promponas","curator_id":"vpromp","timestamp":"2022-06-28T13:22:44.476Z"}}],"regions_counter":13,"released":"2022_06","sequence":"MKGKLTGKDKLIVDEFEELGEQESDIDEFDLLEGDEKLPGDSELDKTTSIYPPETSWEVNKGMNSSRLHKLYSLFFDKSSAFYLGDDVSVLEDKPLTGAYGFQSKKNDQQIFLFRPDSDYVAGYHVDAKSDAGWVNDKLDRRLSEISEFCSKATQPATFILPFVEMPTDITKGVQHQVLLTISYDPKSKQLTPTVYDSIGRDTYSESLSSYFKGKYRTTCDEILTQSIEKAIKSTDFTLGKFTRAAYNHQNRLTEGNCGSYTFRTIKEVISSSAQGTEVKIPGSGYITSNSYLTSQHVQDIESCIKYRNLGVVDIESALTEGKTLPVQLSEFIVALEDYGKLRSQQSEKSMLNFIGYSKTAKLTAVELLIGILNDIKGKNEISESQYDKLVKEVDCLMDSSLGKLVQFHLKNLGAESLQKLVLPCVKFDDTIDDFVTIEKDELFDVPDITGEELASKKGIEQGALDKEALLKQKQIKTDLLDLREEDKTGLKKPLHGGIKVK","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Legionellales","Legionellaceae","Legionella"],"dataset":["Autophagy-related proteins","Bacterial virulence-related proteins","Stress response proteins"],"genes":[{"name":{"value":"ravZ","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"20880356","url":"http://www.ncbi.nlm.nih.gov/pubmed/20880356","alternativeUrl":"https://europepmc.org/abstract/MED/20880356"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"23112293","url":"http://www.ncbi.nlm.nih.gov/pubmed/23112293","alternativeUrl":"https://europepmc.org/abstract/MED/23112293"}}]},"olnNames":[{"value":"lpg1683","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAU27763.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAU27763.1"}}]}]}],"alphafold_very_low_content":0.14940239043824702,"disorder_content":0.2729083665338645,"disprot_consensus":{"full":[{"start":1,"end":46,"type":"D"},{"start":278,"end":287,"type":"D"},{"start":347,"end":357,"type":"D"},{"start":433,"end":502,"type":"D"}],"Structural state":[{"start":1,"end":46,"type":"D"},{"start":278,"end":287,"type":"D"},{"start":347,"end":357,"type":"D"},{"start":433,"end":502,"type":"D"}],"Biological process":[{"start":16,"end":19,"type":"F"},{"start":29,"end":32,"type":"F"},{"start":435,"end":438,"type":"F"}],"Molecular function":[{"start":16,"end":19,"type":"F"},{"start":29,"end":32,"type":"F"}]}},{"disprot_id":"DP03687","acc":"O00410","creator":"vnugnes","date":"2022-05-30T18:17:40.829Z","features":{"pfam":[{"id":"PF02985","name":"HEAT repeat","start":907,"end":935},{"id":"PF13513","name":"HEAT-like repeat","start":372,"end":426},{"id":"PF18808","name":"Importin repeat","start":270,"end":357},{"id":"PF18816","name":"Importin repeat","start":1005,"end":1052},{"id":"PF18829","name":"Importin repeat 6","start":765,"end":872},{"id":"PF25574","name":"Importin subunit beta-1-like, TPR repeats","start":490,"end":639},{"id":"PF25780","name":"IPO5-like, TPR repeats","start":102,"end":261}],"gene3D":[]},"length":1097,"name":"Importin-5","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":21,"reference_id":"32222384","reference_source":"pmid","reference_html":"X-ray Structure of the Human Karyopherin RanBP5, an Essential Factor for Influenza Polymerase Nuclear Trafficking. <i> Swale C, Da Costa B, Sedano L, Garzoni F, McCarthy AA, Berger I, Bieniossek C, Ruigrok RWH, Delmas B, Crépin T. </i> J Mol Biol, 2020","date":"2022-05-30T19:31:07.183Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03687r001","sequence_construct":"MPEDQVGKLEATENTISAMAAAAAEQQQFYLLLGNLLSPDNVVRKQAEETYENIPGQSKITFLLQAIRNTTAAEEARQMAAVLLRRLLSSAFDEVYPALPSDVQTAIKSELLMIIQMETQSSMRKKVCDIAAELARNLIDEDGNNQWPEGLKFLFDSVSSQNVGLREAALHIFWNFPGIFGNQQQHYLDVIKRMLVQCMQDQEHPSIRTLSARATAAFILANEHNVALFKHFADLLPGFLQAVNDSCYQNDDSVLKSLVEIADTVPKYLRPHLEATLQLSLKLCGDTSLNNMQRQLALEVIVTLSETAAAMLRKHTNIVAQTIPQMLAMMVDLEEDEDWANADELEDDDFDSNAVAGESALDRMACGLGGKLVLPMIKEHIMQMLQNPDWKYRHAGLMALSAIGEGCHQQMEGILNEIVNFVLLFLQDPHPRVRYAACNAVGQMATDFAPGFQKKFHEKVIAALLQTMEDQGNQRVQAHAAAALINFTEDCPKSLLIPYLDNLVKHLHSIMVLKLQELIQKGTKLVLEQVVTSIASVADTAEEKFVPYYDLFMPSLKHIVENAVQKELRLLRGKTIECISLIGLAVGKEKFMQDASDVMQLLLKTQTDFNDMEDDDPQISYMISAWARMCKILGKEFQQYLPVVMGPLMKTASIKPEVALLDTQDMENMSDDDGWEFVNLGDQQSFGIKTAGLEEKSTACQMLVCYAKELKEGFVEYTEQVVKLMVPLLKFYFHDGVRVAAAESMPLLLECARVRGPEYLTQMWHFMCDALIKAIGTEPDSDVLSEIMHSFAKCIEVMGDGCLNNEHFEELGGILKAKLEEHFKNQELRQVKRQDEDYDEQVEESLQDEDDNDVYILTKVSDILHSIFSSYKEKVLPWFEQLLPLIVNLICPHRPWPDRQWGLCIFDDVIEHCSPASFKYAEYFLRPMLQYVCDNSPEVRQAAAYGLGVMAQYGGDNYRPFCTEALPLLVRVIQSADSKTKENVNATENCISAVGKIMKFKPDCVNVEEVLPHWLSWLPLHEDKEEAVQTFNYLCDLIESNHPIVLGPNNTNLPKIFSIIAEGEMHEAIKHEDPCAKRLANVVRQVQTSGGLWTECIAQLSPEQQAAIQELLNSA","statement":[{"text":"This first crystal form provided a preliminary model and included an N-terminal stretch of 21 amino acid residues, which was presumably unstructured and could not be traced in the electron density.","type":"Article"},{"text":"The peptide used in this study is derivated from the Isoform 3 of this protein.","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"6XU2"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"49786","entry_name":"nickel(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"42820","entry_name":"guanidine"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-31T07:11:10.584Z"}},{"start":316,"end":329,"reference_id":"32222384","reference_source":"pmid","reference_html":"X-ray Structure of the Human Karyopherin RanBP5, an Essential Factor for Influenza Polymerase Nuclear Trafficking. <i> Swale C, Da Costa B, Sedano L, Garzoni F, McCarthy AA, Berger I, Bieniossek C, Ruigrok RWH, Delmas B, Crépin T. </i> J Mol Biol, 2020","date":"2022-05-30T19:30:10.415Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"6XTE"}],"region_id":"DP03687r002","sequence_construct":"AMAAAEQQQFYLLLGNLLSPDNVVRKQAEETYENIPGQSKITFLLQAIRNTTAAEEARQMAAVLLRRLLSSAFDEVYPALPSDVQTAIKSELLMIIQMETQSSMRKKVCDIAAELARNLIDEDGNNQWPEGLKFLFDSVSSQNVGLREAALHIFWNFPGIFGNQQQHYLDVIKRMLVQCMQDQEHPSIRTLSARATAAFILANEHNVALFKHFADLLPGFLQAVNDSCYQNDDSVLKSLVEIADTVPKYLRPHLEATLQLSLKLCGDTSLNNMQRQLALEVIVTLSETAAAMLRKHTNIVAQTIPQMLAMMVDLEEDEDWANADELEDDDFDSNAVAGESALDRMACGLGGKLVLPMIKEHIMQMLQNPDWKYRHAGLMALSAIGEGCHQQMEGILNEIVNFVLLFLQDPHPRVRYAACNAVGQMATDFAPGFQKKFHEKVIAALLQTMEDQGNQRVQAHAAAALINFTEDCPKSLLIPYLDNLVKHLHSIMVLKLQELIQKGTKLVLEQVVTSIASVADTAEEKFVPYYDLFMPSLKHIVENAVQKELRLLRGKTIECISLIGLAVGKEKFMQDASDVMQLLLKTQTDFNDMEDDDPQISYMISAWARMCKILGKEFQQYLPVVMGPLMKTASIKPEVALLDTQDMENMSDDDGWEFVNLGDQQSFGIKTAGLEEKSTACQMLVCYAKELKEGFVEYTEQVVKLMVPLLKFYFHDGVRVAAAESMPLLLECARVRGPEYLTQMWHFMCDALIKAIGTEPDSDVLSEIMHSFAKCIEVMGDGCLNNEHFEELGGILKAKLEEHFKNQELRQVKRQDEDYDEQVEESLQDEDDNDVYILTKVSDILHSIFSSYKEKVLPWFEQLLPLIVNLICPHRPWPDRQWGLCIFDDVIEHCSPASFKYAEYFLRPMLQYVCDNSPEVRQAAAYGLGVMAQYGGDNYRPFCTEALPLLVRVIQSADSKTKENVNATENCISAVGKIMKFKPDCVNVEEVLPHWLSWLPLHEDKEEAVQTFNYLCDLIESNHPIVLGPNNTNLPKIFSIIAEGEMHEAIKHEDPCAKRLANVVRQVQTSGGLWTECIAQLSPEQQAAIQELLNSA","statement":[{"text":"This region of the Isoform 1 lacks electron density, as shown in the PDB, typical of IDR.","type":"Curator statement"}],"construct_alterations":[{"term_id":"MOD:00677","term_name":"hydroxylated residue","term_namespace":"Protein modification","start":873,"end":873,"position":"Specific residue"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"42820","entry_name":"guanidine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"49786","entry_name":"nickel(2+)"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-31T07:11:12.274Z"}}],"regions_counter":2,"released":"2022_06","sequence":"MAAAAAEQQQFYLLLGNLLSPDNVVRKQAEETYENIPGQSKITFLLQAIRNTTAAEEARQMAAVLLRRLLSSAFDEVYPALPSDVQTAIKSELLMIIQMETQSSMRKKVCDIAAELARNLIDEDGNNQWPEGLKFLFDSVSSQNVGLREAALHIFWNFPGIFGNQQQHYLDVIKRMLVQCMQDQEHPSIRTLSARATAAFILANEHNVALFKHFADLLPGFLQAVNDSCYQNDDSVLKSLVEIADTVPKYLRPHLEATLQLSLKLCGDTSLNNMQRQLALEVIVTLSETAAAMLRKHTNIVAQTIPQMLAMMVDLEEDEDWANADELEDDDFDSNAVAGESALDRMACGLGGKLVLPMIKEHIMQMLQNPDWKYRHAGLMALSAIGEGCHQQMEGILNEIVNFVLLFLQDPHPRVRYAACNAVGQMATDFAPGFQKKFHEKVIAALLQTMEDQGNQRVQAHAAAALINFTEDCPKSLLIPYLDNLVKHLHSIMVLKLQELIQKGTKLVLEQVVTSIASVADTAEEKFVPYYDLFMPSLKHIVENAVQKELRLLRGKTIECISLIGLAVGKEKFMQDASDVMQLLLKTQTDFNDMEDDDPQISYMISAWARMCKILGKEFQQYLPVVMGPLMKTASIKPEVALLDTQDMENMSDDDGWEFVNLGDQQSFGIKTAGLEEKSTACQMLVCYAKELKEGFVEYTEQVVKLMVPLLKFYFHDGVRVAAAESMPLLLECARVRGPEYLTQMWHFMCDALIKAIGTEPDSDVLSEIMHSFAKCIEVMGDGCLNNEHFEELGGILKAKLEEHFKNQELRQVKRQDEDYDEQVEESLQDEDDNDVYILTKVSDILHSIFSSYKEKVLPWFEQLLPLIVNLICPHRPWPDRQWGLCIFDDVIEHCSPASFKYAEYFLRPMLQYVCDNSPEVRQAAAYGLGVMAQYGGDNYRPFCTEALPLLVRVIQSADSKTKENVNATENCISAVGKIMKFKPDCVNVEEVLPHWLSWLPLHEDKEEAVQTFNYLCDLIESNHPIVLGPNNTNLPKIFSIIAEGEMHEAIKHEDPCAKRLANVVRQVQTSGGLWTECIAQLSPEQQAAIQELLNSA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"IPO5"},"synonyms":[{"value":"KPNB3"},{"value":"RANBP5"}]}],"alphafold_very_low_content":0.0009115770282588879,"disorder_content":0.03190519598906107,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"},{"start":316,"end":329,"type":"D"}],"Structural state":[{"start":1,"end":21,"type":"D"},{"start":316,"end":329,"type":"D"}]}},{"disprot_id":"DP03688","acc":"Q6DD88","creator":"jnilsson","date":"2022-05-30T19:52:05.122Z","features":{"pfam":[{"id":"PF02263","name":"Guanylate-binding protein, N-terminal domain","start":37,"end":305},{"id":"PF02841","name":"Guanylate-binding protein, C-terminal domain","start":313,"end":434}],"gene3D":[]},"length":541,"name":"Atlastin-3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":21,"reference_id":"34546351","reference_source":"pmid","reference_html":"The hypervariable region of atlastin-1 is a site for intrinsic and extrinsic regulation.  <i> Kelly CM, Byrnes LJ, Neela N, Sondermann H, O'Donnell JP. </i> J Cell Biol, 2021","date":"2022-05-30T20:47:08.462Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"6XJO"}],"region_id":"DP03688r001","statement":[{"text":"In all preceding structures, the N-terminal residues leading from the initiator\nmethionine to the G domain were largely disordered. The conservation of this region across different species is strong within distinct isoforms, but highly divergent when isoforms within a particular species are compared with each other (Fig. 1 A).","type":"Results"},{"text":"Figure 9. Phosphorylation of conserved serine residues in the ATL1 HVR. (A) Cartoon representation of the ATL1 catalytic core structure presented in Fig. 1 (G domain, blue; middle domain, purple; structured portion of the HVR spanning residues 18–31, pink; S22 and S23, red; residues 1–17, disordered).","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-05-31T11:44:22.619Z"}}],"regions_counter":1,"released":"2022_06","sequence":"MLSPQRVAAAASRGADDAMESSKPGPVQVVLVQKDQHSFELDEKALASILLQDHIRDLDVVVVSVAGAFRKGKSFILDFMLRYLYSQKESGHSNWLGDPEEPLTGFSWRGGSDPETTGIQIWSEVFTVEKPGGKKVAVVLMDTQGAFDSQSTVKDCATIFALSTMTSSVQIYNLSQNIQEDDLQQLQLFTEYGRLAMDEIFQKPFQTLMFLVRDWSFPYEYSYGLQGGMAFLDKRLQVKEHQHEEIQNVRNHIHSCFSDVTCFLLPHPGLQVATSPDFDGKLKDIAGEFKEQLQALIPYVLNPSKLMEKEINGSKVTCRGLLEYFKAYIKIYQGEDLPHPKSMLQATAEANNLAAAASAKDIYYNNMEEVCGGEKPYLSPDILEEKHCEFKQLALDHFKKTKKMGGKDFSFRYQQELEEEIKELYENFCKHNGSKNVFSTFRTPAVLFTGIVALYIASGLTGFIGLEVVAQLFNCMVGLLLIALLTWGYIRYSGQYRELGGAIDFGAAYVLEQASSHIGNSTQATVRDAVVGRPSMDKKAQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Autophagy-related proteins"],"genes":[{"name":{"value":"ATL3"}}],"alphafold_very_low_content":0.05545286506469501,"disorder_content":0.038817005545286505,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"}],"Structural state":[{"start":1,"end":21,"type":"D"}]}},{"disprot_id":"DP03689","acc":"P07250","creator":"vacs","date":"2022-05-31T11:36:39.402Z","features":{"pfam":[{"id":"PF03770","name":"Inositol polyphosphate kinase","start":114,"end":352}],"gene3D":[]},"length":355,"name":"Inositol polyphosphate multikinase","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":287,"end":316,"reference_id":"17050532","reference_source":"pmid","reference_html":"Crystal structure of inositol phosphate multikinase 2 and implications for substrate specificity. <i> Holmes W, Jogl G. </i> J Biol Chem, 2006","date":"2022-05-31T11:41:10.106Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2IF8"},{"db":"PDB","id":"2IEW"}],"region_id":"DP03689r001","statement":[{"text":"Several loop regions in the Ipk2 structure are disordered, and we have not included the corresponding residues in our current model. These loop regions comprise residues 1-26, 46-57 (between α1 and α2), and 76-110 (between β2 and β3) in the N-terminal domain and 287-316 in the C-terminal domain. Not surprisingly, the unique aspartate-rich poly-D loop region between residues 287 and 316 is disordered in our structure and was omitted from the final model.","type":"Results"},{"text":"The position of the disordered poly-D loop is indicated by a black line.","type":"Figure"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-01T07:34:23.190Z"}},{"start":76,"end":110,"reference_id":"17050532","reference_source":"pmid","reference_html":"Crystal structure of inositol phosphate multikinase 2 and implications for substrate specificity. <i> Holmes W, Jogl G. </i> J Biol Chem, 2006","date":"2022-05-31T11:42:03.825Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2IF8"},{"db":"PDB","id":"2IEW"}],"region_id":"DP03689r002","statement":[{"text":"Several loop regions in the Ipk2 structure are disordered, and we have not included the corresponding residues in our current model. These loop regions comprise residues 1-26, 46-57 (between α1 and α2), and 76-110 (between β2 and β3) in the N-terminal domain and 287-316 in the C-terminal domain.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-01T07:34:20.182Z"}},{"start":46,"end":57,"reference_id":"17050532","reference_source":"pmid","reference_html":"Crystal structure of inositol phosphate multikinase 2 and implications for substrate specificity. <i> Holmes W, Jogl G. </i> J Biol Chem, 2006","date":"2022-05-31T11:42:38.409Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2IF8"},{"db":"PDB","id":"2IEW"}],"region_id":"DP03689r003","statement":[{"text":"Several loop regions in the Ipk2 structure are disordered, and we have not included the corresponding residues in our current model. These loop regions comprise residues 1-26, 46-57 (between α1 and α2), and 76-110 (between β2 and β3) in the N-terminal domain and 287-316 in the C-terminal domain.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-01T07:33:44.124Z"}},{"start":1,"end":24,"reference_id":"17050532","reference_source":"pmid","reference_html":"Crystal structure of inositol phosphate multikinase 2 and implications for substrate specificity. <i> Holmes W, Jogl G. </i> J Biol Chem, 2006","date":"2022-05-31T11:43:49.977Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2IF8"},{"db":"PDB","id":"2IEW"}],"region_id":"DP03689r004","statement":[{"text":"Several loop regions in the Ipk2 structure are disordered, and we have not included the corresponding residues in our current model. These loop regions comprise residues 1-26, 46-57 (between α1 and α2), and 76-110 (between β2 and β3) in the N-terminal domain and 287-316 in the C-terminal domain.","type":"Results"},{"text":"However, the first 26 residues are disordered in both Ipk2 structures, and we did not observe a similar order-disorder transition between the apoenzyme and the ADP-bound form.","type":"Discussion"},{"text":"Residues 1-24 are disordered in all structures.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-01T07:33:33.607Z"}},{"start":287,"end":303,"reference_id":"12828642","reference_source":"pmid","reference_html":"Arg82p is a bifunctional protein whose inositol polyphosphate kinase activity is essential for nitrogen and PHO gene expression but not for Mcm1p chaperoning in yeast. <i> El Alami M, Messenguy F, Scherens B, Dubois E. </i> Mol Microbiol, 2003","date":"2022-05-31T11:48:11.882Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"GO:0050821","term_name":"protein stabilization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"annotation_extensions":[],"ec_go":"IMP","region_id":"DP03689r005","statement":[{"text":"We show here that Mcm1p and Arg80p chaperoning by Arg82p does not involve the inositol polyphosphate kinase activity of Arg82p, but requires its polyaspartate domain. Our results indicate that Arg82p is a bifunctional protein whose inositol kinase activity plays a role in multiple signalling cascades, and whose acidic domain protects two MADS-box proteins against degradation.","type":"Abstract"},{"text":"In this study we also show that the control of NCR and PHO genes require the kinase domains of Arg82p and Kcs1p, but not the polyaspartate stretch in Arg82p involved in Mcm1p stabilization.","type":"Introduction"},{"text":"A mutation in Arg82p (D131A) abolishing its IP kinase activity had no effect on the expression of MFα1 (lane 6), whereas the deletion of the polyaspartate residues (lane 5) impaired its expression.","type":"Results"},{"text":"The polyaspartate domain of Arg82p was shown to be crucial for its role in the arginine regulation (Qiu et al., 1990; Dubois et al., 2000) indicating that this region could be important for the interaction between Arg82p and the MADS-box proteins Mcm1p and Arg80p. To address this point, two-hybrid assays were used to examine the interaction between Arg80p or Mcm1p and arg82p mutated proteins (arg82D131A, arg82Δ282-303). Deletion of the polyaspartate domain and not mutation impairing the IP kinase activity caused a significant decrease in the interaction with Mcm1p or Arg80p (Table 2).","type":"Results"},{"text":"The stability of Mcm1p and Arg80p was impaired in the arg82Δasp strain to the same extent as in a arg82Δ strain.","type":"Results"},{"text":"One function requires the presence of the polyaspartate domain, essential for Mcm1p and Arg80p stabilization, suggesting a role of chaperone for Arg82p, and the other function which is to produce inositol polyphosphates, is independent of the polyaspartate domain.","type":"Discussion"}],"term_comment":"","term_def":"\"Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-01T07:40:36.705Z"}}],"regions_counter":5,"released":"2023_12","sequence":"MDTVNNYRVLEHKAAGHDGTLTDGDGLLIFKPAFPQELEFYKAIQVRDVSRRKSSADGDAPLCSWMPTYLGVLNEGAKIEQSGDAALLKIDERLSDSTDNLDSIPVKSEKSKQYLVLENLLYGFSKPNILDIKLGKTLYDSKASLEKRERMKRVSETTTSGSLGFRICGMKIQKNPSVLNQLSLEYYEEEADSDYIFINKLYGRSRTDQNVSDAIELYFNNPHLSDARKHQLKKTFLKRLQLFYNTMLEEEVRMISSSLLFIYEGDPERWELLNDVDKLMRDDFIDDDDDDDDNDDDDDDDAEGSSEGPKDKKTTGSLSSMSLIDFAHSEITPGKGYDENVIEGVETLLDIFMKF","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"genes":[{"name":{"value":"ARG82"},"synonyms":[{"value":"ARGR3"},{"value":"GSL3","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10390371","url":"http://www.ncbi.nlm.nih.gov/pubmed/10390371","alternativeUrl":"https://europepmc.org/abstract/MED/10390371"}}]},{"value":"IPK2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10720331","url":"http://www.ncbi.nlm.nih.gov/pubmed/10720331","alternativeUrl":"https://europepmc.org/abstract/MED/10720331"}}]}],"orfNames":[{"value":"YD9395.06C"}],"olnNames":[{"value":"YDR173C"}]}],"alphafold_very_low_content":0.17746478873239438,"disorder_content":0.28450704225352114,"disprot_consensus":{"full":[{"start":1,"end":24,"type":"D"},{"start":46,"end":57,"type":"D"},{"start":76,"end":110,"type":"D"},{"start":287,"end":316,"type":"D"}],"Structural state":[{"start":1,"end":24,"type":"D"},{"start":46,"end":57,"type":"D"},{"start":76,"end":110,"type":"D"},{"start":287,"end":316,"type":"D"}],"Biological process":[{"start":287,"end":303,"type":"F"}]}},{"disprot_id":"DP03690","acc":"P30518","creator":"rpancsa","date":"2022-05-31T11:47:16.013Z","features":{"pfam":[{"id":"PF00001","name":"7 transmembrane receptor (rhodopsin family)","start":55,"end":325}],"gene3D":[]},"length":371,"name":"Vasopressin V2 receptor","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":343,"end":371,"reference_id":"35625550","reference_source":"pmid","reference_html":"Structural Insights into the Intrinsically Disordered GPCR C-Terminal Region, Major Actor in Arrestin-GPCR Interaction. <i> Guillien M, Mouhand A, Fournet A, Gontier A, Martí Navia A, Cordeiro TN, Allemand F, Thureau A, Banères JL, Bernadó P, Sibille N. </i> Biomolecules, 2022","date":"2022-05-31T13:26:25.720Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"(His)6-GST-tagged proteins were expressed in self-inducible medium N5052 or in minimal medium M9 by adding 2 mM IPTG when the OD600 reached 0.6."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"(His)6-GST-tagged proteins were expressed in self-inducible medium N5052 or in minimal medium M9 by adding 2 mM IPTG when the OD600 reached 0.6."}]}],"region_id":"DP03690r001","statement":[{"text":"far-UV circular dichroism (CD) spectra (colored lines) present a minimum around 200 nm (black dashed line) and a shoulder at 220 nm (black dashed and dotted line) characteristic of disordered proteins with transient secondary structure content","type":"Figure"},{"text":"In addition, far UV CD spectra showed a minimum around 198 nm, characteristic of unfolded proteins [58] (Figure 2b), and a negative shoulder around 222 nm, suggesting the presence of residual secondary structures [59] (Figure 2b).","type":"Results"}],"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":20,"statements":[{"type":"Methods","text":"Far UV-spectra of the C-termini were recorded in a quartz cuvette (path length 0.1 cm) at 0.08 mg/mL in H2O at 20 °C using a Chirascan."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-05-31T15:47:51.120Z"}},{"start":343,"end":371,"reference_id":"35625550","reference_source":"pmid","reference_html":"Structural Insights into the Intrinsically Disordered GPCR C-Terminal Region, Major Actor in Arrestin-GPCR Interaction. <i> Guillien M, Mouhand A, Fournet A, Gontier A, Martí Navia A, Cordeiro TN, Allemand F, Thureau A, Banères JL, Bernadó P, Sibille N. </i> Biomolecules, 2022","date":"2022-05-31T13:24:13.172Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":20,"statements":[{"type":"Figure","text":"HSQCs were recorded on 300 µM samples at 700 MHz and 20 °C, in 50 mM Bis-Tris pH 6.7, 150 mM NaCl buffer."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.7,"statements":[{"type":"Figure","text":"HSQCs were recorded on 300 µM samples at 700 MHz and 20 °C, in 50 mM Bis-Tris pH 6.7, 150 mM NaCl buffer."}]}],"construct_alterations":[{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"(His)6-GST-tagged proteins were expressed in self-inducible medium N5052 or in minimal medium M9 by adding 2 mM IPTG when the OD600 reached 0.6."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"(His)6-GST-tagged proteins were expressed in self-inducible medium N5052 or in minimal medium M9 by adding 2 mM IPTG when the OD600 reached 0.6."}]}],"region_id":"DP03690r002","statement":[{"text":"15N-HSQC spectra display a low proton spectral dispersion (~1 ppm) typical of IDPs.","type":"Figure"},{"text":"Additionally, 15N-HSQC spectra of the three C-terminal regions showed a reduced amide proton spectral dispersion (around 1 ppm) typical of a disordered protein (Figure 2c) [18,19].","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-05-31T15:48:04.365Z"}},{"start":343,"end":371,"reference_id":"35625550","reference_source":"pmid","reference_html":"Structural Insights into the Intrinsically Disordered GPCR C-Terminal Region, Major Actor in Arrestin-GPCR Interaction. <i> Guillien M, Mouhand A, Fournet A, Gontier A, Martí Navia A, Cordeiro TN, Allemand F, Thureau A, Banères JL, Bernadó P, Sibille N. </i> Biomolecules, 2022","date":"2022-05-31T13:28:31.225Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"(His)6-GST-tagged proteins were expressed in self-inducible medium N5052 or in minimal medium M9 by adding 2 mM IPTG when the OD600 reached 0.6."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"(His)6-GST-tagged proteins were expressed in self-inducible medium N5052 or in minimal medium M9 by adding 2 mM IPTG when the OD600 reached 0.6."}]}],"region_id":"DP03690r003","statement":[{"text":"The Kratky plots extracted from SAXS data were typical of disordered regions with no clear maximum and a monotonic increase along the momentum transfer range.","type":"Results"}],"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":15,"statements":[{"type":"Methods","text":"Samples were measured at 15 °C and at two concentrations, 5 mg/mL and 10 mg/mL, for all GPCR-Cters, in 50 mM BisTris pH 6.7, 50 mM NaCl and 2 mM DTT buffer."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.7,"statements":[{"type":"Methods","text":"Samples were measured at 15 °C and at two concentrations, 5 mg/mL and 10 mg/mL, for all GPCR-Cters, in 50 mM BisTris pH 6.7, 50 mM NaCl and 2 mM DTT buffer."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-05-31T15:48:25.702Z"}}],"regions_counter":3,"released":"2023_12","sequence":"MLMASTTSAVPGHPSLPSLPSNSSQERPLDTRDPLLARAELALLSIVFVAVALSNGLVLAALARRGRRGHWAPIHVFIGHLCLADLAVALFQVLPQLAWKATDRFRGPDALCRAVKYLQMVGMYASSYMILAMTLDRHRAICRPMLAYRHGSGAHWNRPVLVAWAFSLLLSLPQLFIFAQRNVEGGSGVTDCWACFAEPWGRRTYVTWIALMVFVAPTLGIAACQVLIFREIHASLVPGPSERPGGRRRGRRTGSPGEGAHVSAAVAKTVRMTLVIVVVYVLCWAPFFLVQLWAAWDPEAPLEGAPFVLLMLLASLNSCTNPWIYASFSSSVSSELRSLLCCARGRTPPSLGPQDESCTTASSSLAKDTSS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"AVPR2"},"synonyms":[{"value":"ADHR"},{"value":"DIR"},{"value":"DIR3"},{"value":"V2R"}]}],"alphafold_very_low_content":0.18059299191374664,"disorder_content":0.07816711590296496,"disprot_consensus":{"full":[{"start":343,"end":371,"type":"D"}],"Structural state":[{"start":343,"end":371,"type":"D"}]}},{"disprot_id":"DP03691","acc":"Q92847","creator":"rpancsa","date":"2022-05-31T13:29:19.137Z","features":{"pfam":[{"id":"PF00001","name":"7 transmembrane receptor (rhodopsin family)","start":60,"end":323}],"gene3D":[]},"length":366,"name":"Growth hormone secretagogue receptor type 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":339,"end":366,"reference_id":"35625550","reference_source":"pmid","reference_html":"Structural Insights into the Intrinsically Disordered GPCR C-Terminal Region, Major Actor in Arrestin-GPCR Interaction. <i> Guillien M, Mouhand A, Fournet A, Gontier A, Martí Navia A, Cordeiro TN, Allemand F, Thureau A, Banères JL, Bernadó P, Sibille N. </i> Biomolecules, 2022","date":"2022-05-31T13:33:36.530Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":20,"statements":[{"type":"Methods","text":"Far UV-spectra of the C-termini were recorded in a quartz cuvette (path length 0.1 cm) at 0.08 mg/mL in H2O at 20 °C using a Chirascan."}]}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Vectors were transfected into E. Coli BL21 DE3 strain (Fisher Scientific S.A.S., Illkirch, France) and (His)6-GST-tagged proteins were expressed in self-inducible medium N5052 or in minimal medium M9 by adding 2 mM IPTG when the OD600 reached 0.6."}]},{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Vectors were transfected into E. Coli BL21 DE3 strain (Fisher Scientific S.A.S., Illkirch, France) and (His)6-GST-tagged proteins were expressed in self-inducible medium N5052 or in minimal medium M9 by adding 2 mM IPTG when the OD600 reached 0.6."}]}],"region_id":"DP03691r001","statement":[{"text":"In addition, far UV CD spectra showed a minimum around 198 nm, characteristic of unfolded proteins [58] (Figure 2b), and a negative shoulder around 222 nm, suggesting the presence of residual secondary structures [59] (Figure 2b).","type":"Results"},{"text":"far-UV circular dichroism (CD) spectra (colored lines) present a minimum around 200 nm (black dashed line) and a shoulder at 220 nm (black dashed and dotted line) characteristic of disordered proteins with transient secondary structure content","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-05-31T15:48:54.278Z"}},{"start":339,"end":366,"reference_id":"35625550","reference_source":"pmid","reference_html":"Structural Insights into the Intrinsically Disordered GPCR C-Terminal Region, Major Actor in Arrestin-GPCR Interaction. <i> Guillien M, Mouhand A, Fournet A, Gontier A, Martí Navia A, Cordeiro TN, Allemand F, Thureau A, Banères JL, Bernadó P, Sibille N. </i> Biomolecules, 2022","date":"2022-05-31T13:36:44.739Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":20,"statements":[{"type":"Figure","text":"15N-HSQC spectra display a low proton spectral dispersion (~1 ppm) typical of IDPs. HSQCs were recorded on 300 µM samples at 700 MHz and 20 °C, in 50 mM Bis-Tris pH 6.7, 150 mM NaCl buffer."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.7,"statements":[{"type":"Figure","text":"15N-HSQC spectra display a low proton spectral dispersion (~1 ppm) typical of IDPs. HSQCs were recorded on 300 µM samples at 700 MHz and 20 °C, in 50 mM Bis-Tris pH 6.7, 150 mM NaCl buffer."}]}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Vectors were transfected into E. Coli BL21 DE3 strain (Fisher Scientific S.A.S., Illkirch, France) and (His)6-GST-tagged proteins were expressed in self-inducible medium N5052 or in minimal medium M9 by adding 2 mM IPTG when the OD600 reached 0.6."}]},{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Vectors were transfected into E. Coli BL21 DE3 strain (Fisher Scientific S.A.S., Illkirch, France) and (His)6-GST-tagged proteins were expressed in self-inducible medium N5052 or in minimal medium M9 by adding 2 mM IPTG when the OD600 reached 0.6."}]}],"region_id":"DP03691r002","statement":[{"text":"Additionally, 15N-HSQC spectra of the three C-terminal regions showed a reduced amide proton spectral dispersion (around 1 ppm) typical of a disordered protein.","type":"Results"},{"text":"15N-HSQC spectra display a low proton spectral dispersion (~1 ppm) typical of IDPs. HSQCs were recorded on 300 µM samples at 700 MHz and 20 °C, in 50 mM Bis-Tris pH 6.7, 150 mM NaCl buffer.","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-05-31T15:48:55.149Z"}},{"start":339,"end":366,"reference_id":"35625550","reference_source":"pmid","reference_html":"Structural Insights into the Intrinsically Disordered GPCR C-Terminal Region, Major Actor in Arrestin-GPCR Interaction. <i> Guillien M, Mouhand A, Fournet A, Gontier A, Martí Navia A, Cordeiro TN, Allemand F, Thureau A, Banères JL, Bernadó P, Sibille N. </i> Biomolecules, 2022","date":"2022-05-31T13:39:07.766Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":15,"statements":[{"type":"Methods","text":"Samples were measured at 15 °C and at two concentrations, 5 mg/mL and 10 mg/mL, for all GPCR-Cters, in 50 mM BisTris pH 6.7, 50 mM NaCl and 2 mM DTT buffer."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.7,"statements":[{"type":"Methods","text":"Samples were measured at 15 °C and at two concentrations, 5 mg/mL and 10 mg/mL, for all GPCR-Cters, in 50 mM BisTris pH 6.7, 50 mM NaCl and 2 mM DTT buffer."}]}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Vectors were transfected into E. Coli BL21 DE3 strain (Fisher Scientific S.A.S., Illkirch, France) and (His)6-GST-tagged proteins were expressed in self-inducible medium N5052 or in minimal medium M9 by adding 2 mM IPTG when the OD600 reached 0.6."}]},{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Vectors were transfected into E. Coli BL21 DE3 strain (Fisher Scientific S.A.S., Illkirch, France) and (His)6-GST-tagged proteins were expressed in self-inducible medium N5052 or in minimal medium M9 by adding 2 mM IPTG when the OD600 reached 0.6."}]}],"region_id":"DP03691r003","statement":[{"text":"The Kratky plots extracted from SAXS data were typical of disordered regions with no clear maximum and a monotonic increase along the momentum transfer range.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-05-31T15:48:56.624Z"}}],"regions_counter":3,"released":"2023_12","sequence":"MWNATPSEEPGFNLTLADLDWDASPGNDSLGDELLQLFPAPLLAGVTATCVALFVVGIAGNLLTMLVVSRFRELRTTTNLYLSSMAFSDLLIFLCMPLDLVRLWQYRPWNFGDLLCKLFQFVSESCTYATVLTITALSVERYFAICFPLRAKVVVTKGRVKLVIFVIWAVAFCSAGPIFVLVGVEHENGTDPWDTNECRPTEFAVRSGLLTVMVWVSSIFFFLPVFCLTVLYSLIGRKLWRRRRGDAVVGASLRDQNHKQTVKMLAVVVFAFILCWLPFHVGRYLFSKSFEPGSLEIAQISQYCNLVSFVLFYLSAAINPILYNIMSKKYRVAVFRLLGFEPFSQRKLSTLKDESSRAWTESSINT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"GHSR"}}],"alphafold_very_low_content":0.1092896174863388,"disorder_content":0.07650273224043716,"disprot_consensus":{"full":[{"start":339,"end":366,"type":"D"}],"Structural state":[{"start":339,"end":366,"type":"D"}]}},{"disprot_id":"DP03692","acc":"P07550","creator":"ireményi","date":"2022-05-31T13:41:21.449Z","features":{"pfam":[{"id":"PF00001","name":"7 transmembrane receptor (rhodopsin family)","start":50,"end":326}],"gene3D":[]},"length":413,"name":"Beta-2 adrenergic receptor","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":342,"end":413,"reference_id":"35625550","reference_source":"pmid","reference_html":"Structural Insights into the Intrinsically Disordered GPCR C-Terminal Region, Major Actor in Arrestin-GPCR Interaction. <i> Guillien M, Mouhand A, Fournet A, Gontier A, Martí Navia A, Cordeiro TN, Allemand F, Thureau A, Banères JL, Bernadó P, Sibille N. </i> Biomolecules, 2022","date":"2022-05-31T13:45:13.530Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":20,"statements":[{"type":"Methods","text":"Far UV-spectra of the C-termini were recorded in a quartz cuvette (path length 0.1 cm) at 0.08 mg/mL in H2O at 20 °C using a Chirascan."}]}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Vectors were transfected into E. Coli BL21 DE3 strain (Fisher Scientific S.A.S., Illkirch, France) and (His)6-GST-tagged proteins were expressed in self-inducible medium N5052 or in minimal medium M9 by adding 2 mM IPTG when the OD600 reached 0.6."}]},{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Vectors were transfected into E. Coli BL21 DE3 strain (Fisher Scientific S.A.S., Illkirch, France) and (His)6-GST-tagged proteins were expressed in self-inducible medium N5052 or in minimal medium M9 by adding 2 mM IPTG when the OD600 reached 0.6."}]}],"region_id":"DP03692r001","statement":[{"text":"In addition, far UV CD spectra showed a minimum around 198 nm, characteristic of unfolded proteins, and a negative shoulder around 222 nm, suggesting the presence of residual secondary structures.","type":"Results"},{"text":"far-UV circular dichroism (CD) spectra (colored lines) present a minimum around 200 nm (black dashed line) and a shoulder at 220 nm (black dashed and dotted line) characteristic of disordered proteins with transient secondary structure content","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-01T12:26:23.162Z"}},{"start":342,"end":413,"reference_id":"35625550","reference_source":"pmid","reference_html":"Structural Insights into the Intrinsically Disordered GPCR C-Terminal Region, Major Actor in Arrestin-GPCR Interaction. <i> Guillien M, Mouhand A, Fournet A, Gontier A, Martí Navia A, Cordeiro TN, Allemand F, Thureau A, Banères JL, Bernadó P, Sibille N. </i> Biomolecules, 2022","date":"2022-05-31T13:47:25.358Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":20,"statements":[{"type":"Figure","text":"15N-HSQC spectra display a low proton spectral dispersion (~1 ppm) typical of IDPs. HSQCs were recorded on 300 µM samples at 700 MHz and 20 °C, in 50 mM Bis-Tris pH 6.7, 150 mM NaCl buffer."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.7,"statements":[{"type":"Figure","text":"15N-HSQC spectra display a low proton spectral dispersion (~1 ppm) typical of IDPs. HSQCs were recorded on 300 µM samples at 700 MHz and 20 °C, in 50 mM Bis-Tris pH 6.7, 150 mM NaCl buffer."}]}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Vectors were transfected into E. Coli BL21 DE3 strain (Fisher Scientific S.A.S., Illkirch, France) and (His)6-GST-tagged proteins were expressed in self-inducible medium N5052 or in minimal medium M9 by adding 2 mM IPTG when the OD600 reached 0.6."}]},{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Vectors were transfected into E. Coli BL21 DE3 strain (Fisher Scientific S.A.S., Illkirch, France) and (His)6-GST-tagged proteins were expressed in self-inducible medium N5052 or in minimal medium M9 by adding 2 mM IPTG when the OD600 reached 0.6."}]}],"region_id":"DP03692r002","statement":[{"text":"Additionally, 15N-HSQC spectra of the three C-terminal regions showed a reduced amide proton spectral dispersion (around 1 ppm) typical of a disordered protein.","type":"Results"},{"text":"15N-HSQC spectra display a low proton spectral dispersion (~1 ppm) typical of IDPs. HSQCs were recorded on 300 µM samples at 700 MHz and 20 °C, in 50 mM Bis-Tris pH 6.7, 150 mM NaCl buffer.","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-05-31T15:49:04.353Z"}},{"start":342,"end":413,"reference_id":"35625550","reference_source":"pmid","reference_html":"Structural Insights into the Intrinsically Disordered GPCR C-Terminal Region, Major Actor in Arrestin-GPCR Interaction. <i> Guillien M, Mouhand A, Fournet A, Gontier A, Martí Navia A, Cordeiro TN, Allemand F, Thureau A, Banères JL, Bernadó P, Sibille N. </i> Biomolecules, 2022","date":"2022-05-31T13:49:35.370Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":15,"statements":[{"type":"Methods","text":"Samples were measured at 15 °C and at two concentrations, 5 mg/mL and 10 mg/mL, for all GPCR-Cters, in 50 mM BisTris pH 6.7, 50 mM NaCl and 2 mM DTT buffer."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.7,"statements":[{"type":"Methods","text":"Samples were measured at 15 °C and at two concentrations, 5 mg/mL and 10 mg/mL, for all GPCR-Cters, in 50 mM BisTris pH 6.7, 50 mM NaCl and 2 mM DTT buffer."}]}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Vectors were transfected into E. Coli BL21 DE3 strain (Fisher Scientific S.A.S., Illkirch, France) and (His)6-GST-tagged proteins were expressed in self-inducible medium N5052 or in minimal medium M9 by adding 2 mM IPTG when the OD600 reached 0.6."}]},{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Vectors were transfected into E. Coli BL21 DE3 strain (Fisher Scientific S.A.S., Illkirch, France) and (His)6-GST-tagged proteins were expressed in self-inducible medium N5052 or in minimal medium M9 by adding 2 mM IPTG when the OD600 reached 0.6."}]}],"region_id":"DP03692r003","statement":[{"text":"The Kratky plots extracted from SAXS data were typical of disordered regions with no clear maximum and a monotonic increase along the momentum transfer range.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-05-31T15:49:03.665Z"}}],"regions_counter":3,"released":"2023_12","sequence":"MGQPGNGSAFLLAPNGSHAPDHDVTQERDEVWVVGMGIVMSLIVLAIVFGNVLVITAIAKFERLQTVTNYFITSLACADLVMGLAVVPFGAAHILMKMWTFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYFAITSPFKYQSLLTKNKARVIILMVWIVSGLTSFLPIQMHWYRATHQEAINCYANETCCDFFTNQAYAIASSIVSFYVPLVIMVFVYSRVFQEAKRQLQKIDKSEGRFHVQNLSQVEQDGRTGHGLRRSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIQDNLIRKEVYILLNWIGYVNSGFNPLIYCRSPDFRIAFQELLCLRRSSLKAYGNGYSSNGNTGEQSGYHVEQEKENKLLCEDLPGTEDFVGHQGTVPSDNIDSQGRNCSTNDSLL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"ADRB2"},"synonyms":[{"value":"ADRB2R"},{"value":"B2AR"}]}],"alphafold_very_low_content":0.20823244552058112,"disorder_content":0.17433414043583534,"disprot_consensus":{"full":[{"start":342,"end":413,"type":"D"}],"Structural state":[{"start":342,"end":413,"type":"D"}]}},{"disprot_id":"DP03693","acc":"P01732","creator":"rpancsa","date":"2022-05-31T14:01:58.183Z","features":{"pfam":[{"id":"PF07686","name":"Immunoglobulin V-set domain","start":27,"end":131}],"gene3D":[]},"length":235,"name":"T-cell surface glycoprotein CD8 alpha chain","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":128,"end":182,"reference_id":"35617919","reference_source":"pmid","reference_html":"The CD8α hinge is intrinsically disordered with a dynamic exchange that includes proline cis-trans isomerization. <i> Chen X, Mirazee JM, Skorupka KA, Matsuo H, Youkharibache P, Taylor N, Walters KJ. </i> J Magn Reson, 2022","date":"2022-06-01T10:54:07.749Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03693r001","statement":[{"text":"A 1H, 15N HSQC experiment performed on 15N-labeled CD8α H was acquired to detect the amide groups. The resulting spectrum lacked chemical shift dispersion, with clustering of CD8α signals in the center of the spectrum (Fig. 2D, with ubiquitin for comparison on the right [56]. This phenomenon reflects lack of secondary structure, as we observed previously for other intrinsically disordered proteins [53], [54] and is consistent with the AF2 prediction (Fig. 1E).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-01T12:26:17.284Z"}},{"start":128,"end":182,"reference_id":"35617919","reference_source":"pmid","reference_html":"The CD8α hinge is intrinsically disordered with a dynamic exchange that includes proline cis-trans isomerization. <i> Chen X, Mirazee JM, Skorupka KA, Matsuo H, Youkharibache P, Taylor N, Walters KJ. </i> J Magn Reson, 2022","date":"2022-06-01T10:55:32.412Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Methods","text":"Far-UV range CD spectra (260–190 nm) of CD8α H (10 μM) were recorded on a Jasco J-1500CD spectrometer using a quartz cuvette with 1.0 mm path length and temperature controlled at 25 ± 0.1 °C."}]}],"region_id":"DP03693r002","statement":[{"text":"Similarly, CD spectroscopy, which informs on secondary structure, indicated intrinsic disorder both with and without DTT, with negative ellipticity observed near 200 nm and low ellipticity at 190 and 222 nm (Fig. 3E), similar to the intrinsically disordered proteins Pup and SocB [53], [54].","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-01T12:26:18.345Z"}}],"regions_counter":2,"released":"2023_12","sequence":"MALPVTALLLPLALLLHAARPSQFRVSPLDRTWNLGETVELKCQVLLSNPTSGCSWLFQPRGAAASPTFLLYLSQNKPKAAEGLDTQRFSGKRLGDTFVLTLSDFRRENEGYYFCSALSNSIMYFSHFVPVFLPAKPTTTPAPRPPTPAPTIASQPLSLRPEACRPAAGGAVHTRGLDFACDIYIWAPLAGTCGVLLLSLVITLYCNHRNRRRVCKCPRPVVKSGDKPSLSARYV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"CD8A"},"synonyms":[{"value":"MAL"}]}],"alphafold_very_low_content":0.12340425531914893,"disorder_content":0.23404255319148937,"disprot_consensus":{"full":[{"start":128,"end":182,"type":"D"}],"Structural state":[{"start":128,"end":182,"type":"D"}]}},{"disprot_id":"DP03694","acc":"Q8IY63","creator":"rpancsa","date":"2022-05-31T14:25:55.426Z","features":{"pfam":[{"id":"PF12240","name":"Angiomotin C terminal","start":605,"end":810}],"gene3D":[]},"length":956,"name":"Angiomotin-like protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":178,"end":384,"reference_id":"35481651","reference_source":"pmid","reference_html":"Multivalent Angiomotin-like 1 and Yes-associated protein form a dynamic complex. <i> Vogel A, Crawford A, Nyarko A. </i> Protein Sci, 2022","date":"2022-06-01T10:48:53.304Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Methods","text":"Far UV circular dichroism (CD) measurements were recorded at 25°C on a JASCO 720 spectrophotometer using a path length of 1 mm, and a bandwidth of 1.0 nm."}]}],"region_id":"DP03694r001","statement":[{"text":"The far ultra-violet (UV) circular dichroism (CD) spectrum of A123 (Figure 1b) shows a strong signal at 204 nm, suggestive of random coil-like structure, and a relatively weak signal at 222 nm indicative of nascent helical structure.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-01T12:26:10.296Z"}},{"start":178,"end":384,"reference_id":"35481651","reference_source":"pmid","reference_html":"Multivalent Angiomotin-like 1 and Yes-associated protein form a dynamic complex. <i> Vogel A, Crawford A, Nyarko A. </i> Protein Sci, 2022","date":"2022-06-01T10:59:41.318Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":10,"statements":[{"type":"Methods","text":"NMR experiments were performed at 10°C on a Bruker Avance III, 800 MHz spectrometer (Bruker BioSpin) equipped with a triple resonance cryogenic probe. Data were collected on isotopically labeled A123 at concentrations of 75 or 200 μM and in a pH 6.8 buffer composed of 50 mM sodium phosphate, 100 mM NaCl, 50 mM arginine, 50 mM glutamate, 1 mM NaN3, and 2 mM tris(2-carboxyethyl) phosphine."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.8,"statements":[{"type":"Methods","text":"NMR experiments were performed at 10°C on a Bruker Avance III, 800 MHz spectrometer (Bruker BioSpin) equipped with a triple resonance cryogenic probe. Data were collected on isotopically labeled A123 at concentrations of 75 or 200 μM and in a pH 6.8 buffer composed of 50 mM sodium phosphate, 100 mM NaCl, 50 mM arginine, 50 mM glutamate, 1 mM NaN3, and 2 mM tris(2-carboxyethyl) phosphine."}]}],"region_id":"DP03694r002","statement":[{"text":"The 1H-15N heteronuclear single quantum coherence (HSQC) spectrum of A123 shows poor dispersion in the NH-region, as expected for a protein with random coil-like and/or helical structure (Figure 2a).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-01T12:26:11.177Z"}},{"start":186,"end":204,"reference_id":"35481651","reference_source":"pmid","reference_html":"Multivalent Angiomotin-like 1 and Yes-associated protein form a dynamic complex. <i> Vogel A, Crawford A, Nyarko A. </i> Protein Sci, 2022","date":"2022-05-31T15:04:38.763Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"annotation_extensions":[],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P46937-2","operator":null,"partner_start":157,"partner_end":277}],"region_id":"DP03694r003","statement":[{"text":"A123 residues involved in binding YWWTD were mapped by NMR titration experiments in which unlabeled YWWTD and isotopically labeled A123 were mixed at molar ratios in the range of 0.25:1–2:1 (YWWTD:A123). As a reporter of the binding interactions, we monitored changes in the intensities of peaks corresponding to the tyrosine residues, Y191, Y313, and Y370, at the 3 PPxY sites.","type":"Results"},{"text":"At the 0.75:1 molar ratio (Figure 3b, upper panel), missing cross-peaks map to residues in the sequence vicinity of P1 (186–204), H2 (261, 265, 268 and 273), P2 (305–317), P3 (365–371), and the linker segment between P2 and P3 (322, 335, 340, 342).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-05-31T15:43:15.050Z"}},{"start":305,"end":317,"reference_id":"35481651","reference_source":"pmid","reference_html":"Multivalent Angiomotin-like 1 and Yes-associated protein form a dynamic complex. <i> Vogel A, Crawford A, Nyarko A. </i> Protein Sci, 2022","date":"2022-05-31T15:04:50.611Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"annotation_extensions":[],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P46937-2","operator":null,"partner_start":157,"partner_end":277}],"region_id":"DP03694r004","statement":[{"text":"A123 residues involved in binding YWWTD were mapped by NMR titration experiments in which unlabeled YWWTD and isotopically labeled A123 were mixed at molar ratios in the range of 0.25:1–2:1 (YWWTD:A123). As a reporter of the binding interactions, we monitored changes in the intensities of peaks corresponding to the tyrosine residues, Y191, Y313, and Y370, at the 3 PPxY sites.","type":"Results"},{"text":"At the 0.75:1 molar ratio (Figure 3b, upper panel), missing cross-peaks map to residues in the sequence vicinity of P1 (186–204), H2 (261, 265, 268 and 273), P2 (305–317), P3 (365–371), and the linker segment between P2 and P3 (322, 335, 340, 342).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-05-31T15:45:33.559Z"}},{"start":365,"end":371,"reference_id":"35481651","reference_source":"pmid","reference_html":"Multivalent Angiomotin-like 1 and Yes-associated protein form a dynamic complex. <i> Vogel A, Crawford A, Nyarko A. </i> Protein Sci, 2022","date":"2022-05-31T15:05:17.141Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"annotation_extensions":[],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P46937-2","operator":null,"partner_start":157,"partner_end":277}],"region_id":"DP03694r005","statement":[{"text":"A123 residues involved in binding YWWTD were mapped by NMR titration experiments in which unlabeled YWWTD and isotopically labeled A123 were mixed at molar ratios in the range of 0.25:1–2:1 (YWWTD:A123). As a reporter of the binding interactions, we monitored changes in the intensities of peaks corresponding to the tyrosine residues, Y191, Y313, and Y370, at the 3 PPxY sites.","type":"Results"},{"text":"At the 0.75:1 molar ratio (Figure 3b, upper panel), missing cross-peaks map to residues in the sequence vicinity of P1 (186–204), H2 (261, 265, 268 and 273), P2 (305–317), P3 (365–371), and the linker segment between P2 and P3 (322, 335, 340, 342).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-05-31T15:45:34.788Z"}},{"start":261,"end":273,"reference_id":"35481651","reference_source":"pmid","reference_html":"Multivalent Angiomotin-like 1 and Yes-associated protein form a dynamic complex. <i> Vogel A, Crawford A, Nyarko A. </i> Protein Sci, 2022","date":"2022-05-31T15:06:03.607Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"annotation_extensions":[],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P46937-2","operator":null,"partner_start":157,"partner_end":277}],"region_id":"DP03694r006","statement":[{"text":"A123 residues involved in binding YWWTD were mapped by NMR titration experiments in which unlabeled YWWTD and isotopically labeled A123 were mixed at molar ratios in the range of 0.25:1–2:1 (YWWTD:A123). As a reporter of the binding interactions, we monitored changes in the intensities of peaks corresponding to the tyrosine residues, Y191, Y313, and Y370, at the 3 PPxY sites.","type":"Results"},{"text":"At the 0.75:1 molar ratio (Figure 3b, upper panel), missing cross-peaks map to residues in the sequence vicinity of P1 (186–204), H2 (261, 265, 268 and 273), P2 (305–317), P3 (365–371), and the linker segment between P2 and P3 (322, 335, 340, 342).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-05-31T15:45:37.915Z"}},{"start":178,"end":384,"reference_id":"35481651","reference_source":"pmid","reference_html":"Multivalent Angiomotin-like 1 and Yes-associated protein form a dynamic complex. <i> Vogel A, Crawford A, Nyarko A. </i> Protein Sci, 2022","date":"2022-05-31T15:11:13.394Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"annotation_extensions":[],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P46937-2","operator":null,"partner_start":157,"partner_end":277}],"region_id":"DP03694r007","statement":[{"text":"Binding of the two proteins is enthalpically driven, occurs with a binding stoichiometry (N) close to 1:1 and has an effective dissociation constant (Kd) of 0.26 ± 0.01 μM. Because there are two putative binding sites on the YWWTD polypeptide (2 WW domains) and three putative binding sites on the A123 polypeptide (3 PPxY motifs), binding of a single WW-PPxY site or of both WW sites to two PPxY sites will result in a binding stoichiometry of 1:1.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-05-31T15:45:39.377Z"}}],"regions_counter":7,"released":"2023_12","sequence":"MWRAKLRRGTCEPAVKGSPSACYSPSSPVQVLEDSTYFSPDFQLYSGRHETSALTVEATSSIREKVVEDPLCNFHSPNFLRISEVEMRGSEDAAAGTVLQRLIQEQLRYGTPTENMNLLAIQHQATGSAGPAHPTNNFSSTENLTQEDPQMVYQSARQEPQGQEHQVDNTVMEKQVRSTQPQQNNEELPTYEEAKAQSQFFRGQQQQQQQQGAVGHGYYMAGGTSQKSRTEGRPTVNRANSGQAHKDEALKELKQGHVRSLSERIMQLSLERNGAKQHLPGSGNGKGFKVGGGPSPAQPAGKVLDPRGPPPEYPFKTKQMMSPVSKTQEHGLFYGDQHPGMLHEMVKPYPAPQPVRTDVAVLRYQPPPEYGVTSRPCQLPFPSTMQQHSPMSSQTSSASGPLHSVSLPLPLPMALGAPQPPPAASPSQQLGPDAFAIVERAQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKHGNGQPANMPEYNAPALLELVREKEERILALEADMTKWEQKYLEESTIRHFAMNAAATAAAERDTTIINHSRNGSYGESSLEAHIWQEEEEVVQANRRCQDMEYTIKNLHAKIIEKDAMIKVLQQRSRKDAGKTDSSSLRPARSVPSIAAATGTHSRQTSLTSSQLAEEKKEEKTWKGSIGLLLGKEHHEHASAPLLPPPPTSALSSIASTTAASSAHAKTGSKDSSTQTDKSAELFWPSMASLPSRGRLSTTPAHSPVLKHPAAKGTAEKLENSPGHGKSPDHRGRVSSLLHKPEFPDGEMMEVLI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"AMOTL1"}}],"alphafold_very_low_content":0.5543933054393305,"disorder_content":0.21652719665271966,"disprot_consensus":{"full":[{"start":178,"end":384,"type":"D"}],"Structural state":[{"start":178,"end":384,"type":"D"}],"Molecular function":[{"start":178,"end":384,"type":"F"}]}},{"disprot_id":"DP03695","acc":"P70365","creator":"vnugnes","date":"2022-05-31T14:41:25.989Z","features":{"pfam":[{"id":"PF00989","name":"PAS fold","start":115,"end":172},{"id":"PF07469","name":"Nuclear receptor coactivator, DUF1518","start":1155,"end":1211},{"id":"PF07469","name":"Nuclear receptor coactivator, DUF1518","start":1218,"end":1274},{"id":"PF08815","name":"Nuclear receptor coactivator","start":930,"end":979},{"id":"PF08832","name":"Steroid receptor coactivator","start":634,"end":712},{"id":"PF14598","name":"PAS domain","start":260,"end":369},{"id":"PF16665","name":"Unstructured region on nuclear receptor coactivator protein","start":469,"end":590},{"id":"PF23172","name":"Nuclear receptor coactivators bHLH domain","start":1,"end":77}],"gene3D":[]},"length":1447,"name":"Nuclear receptor coactivator 1","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":368,"end":385,"reference_id":"14757047","reference_source":"pmid","reference_html":"Structure of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif of the STAT6 transactivation domain. <i> Razeto A, Ramakrishnan V, Litterst CM, Giller K, Griesinger C, Carlomagno T, Lakomek N, Heimburg T, Lodrini M, Pfitzner E, Becker S. </i> J Mol Biol, 2004","date":"2022-05-31T14:45:20.858Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"1OJ5"}],"region_id":"DP03695r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P42226","statements":[{"type":"Methods","text":"Crystals of NCoA-1 PAS-B domain fragment 257–385 in complex with the STAT6(794–814) peptide were obtained at 20 °C by the hanging drop vapor diffusion technique using 0.2 M LiCl and 20% PEG3350 as precipitant."}]}],"sequence_construct":"GHMTGVESFMTKQDTTGKIISIDTSSLRAAGRTGWEDLVRKCIYAFFQPQGREPSYARQLFQEVMTRGTASSPSYRFILNDGTMLSAHTRCKLCYPQSPDMQPFIMGIHIIDREHSGLSPQDDTNSGMSIPR","statement":[{"text":"The lack of electron density, as shown in the PDB, indicates this region is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-01T08:54:55.009Z"}},{"start":371,"end":385,"reference_id":"14757047","reference_source":"pmid","reference_html":"Structure of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif of the STAT6 transactivation domain. <i> Razeto A, Ramakrishnan V, Litterst CM, Giller K, Griesinger C, Carlomagno T, Lakomek N, Heimburg T, Lodrini M, Pfitzner E, Becker S. </i> J Mol Biol, 2004","date":"2022-05-31T14:49:34.272Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03695r002","sequence_construct":"GHMTGVESFMTKQDTTGKIISIDTSSLRAAGRTGWEDLVRKCIYAFFQPQGREPSYARQLFQEVMTRGTASSPSYRFILNDGTMLSAHTRCKLCYPQSPDMQPFIMGIHIIDREHSGLSPQDDTNSGMSIPR","statement":[{"text":"Solution state NMR revealed that the C-terminal residues from Leu371 show very sharp 15N as well as 1H lines indicative of a highly flexible C-terminal part (data not shown).","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-01T08:55:04.036Z"}},{"start":367,"end":385,"reference_id":"29203888","reference_source":"pmid","reference_html":"Insight into the molecular recognition mechanism of the coactivator NCoA1 by STAT6. <i> Russo L, Giller K, Pfitzner E, Griesinger C, Becker S. </i> Sci Rep, 2017","date":"2022-05-31T14:58:32.353Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5NWX"}],"region_id":"DP03695r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P42226","statements":[{"type":"Methods","text":"In order to understand the increase of affinity of the STAT6783–814 peptide compared to the STAT6794–814 peptide in complex with NCoA1 by a factor of 10 we first solved the crystal structure of the NCoA-1 PAS-B domain in complex with the STAT6783–814 peptide (PDB ID: 5NWX) (SI Tables 2 and 3)."}]}],"sequence_construct":"GHMTGVESFMTKQDTTGKIISIDTSSLRAAGRTGWEDLVRKCIYAFFQPQGREPSYARQLFQEVMTRGTASSPSYRFILNDGTMLSAHTRCKLCYPQSPDMQPFIMGIHIIDREHSGLSPQDDTNSGMSIPR","statement":[{"text":"All RDC values throughout the entire protein, apart from the additional C-terminal tail, which is missing in the crystal structure, are in good agreement with the crystal structure as reflected by the Q factor value (Q = 0.20) and by the Pearson’s correlation coefficient (R = 0.96) (Fig. 4C).","type":"Curator statement"}]},{"start":368,"end":385,"reference_id":"29203888","reference_source":"pmid","reference_html":"Insight into the molecular recognition mechanism of the coactivator NCoA1 by STAT6. <i> Russo L, Giller K, Pfitzner E, Griesinger C, Becker S. </i> Sci Rep, 2017","date":"2022-05-31T15:19:18.937Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03695r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P42226","statements":[{"type":"Methods","text":"In order to understand the increase of affinity of the STAT6783–814 peptide compared to the STAT6794–814 peptide in complex with NCoA1 by a factor of 10 we first solved the crystal structure of the NCoA-1 PAS-B domain in complex with the STAT6783–814 peptide (PDB ID: 5NWX) (SI Tables 2 and 3)."}]}],"sequence_construct":"GHMTGVESFMTKQDTTGKIISIDTSSLRAAGRTGWEDLVRKCIYAFFQPQGREPSYARQLFQEVMTRGTASSPSYRFILNDGTMLSAHTRCKLCYPQSPDMQPFIMGIHIIDREHSGLSPQDDTNSGMSIPR","statement":[{"text":"In the complex the PAS-B domain adopts a well-defined globular fold (rmsdBackboneAtoms 260–367 = 0.485 Å) (Fig. 6A) ranging from Glu260 to Glu367 and a dynamically disordered tail at the C-terminus as confirmed by 15N-1H heteronuclear NOE values (SI Fig. 4).","type":"Curator statement"}]}],"regions_counter":4,"released":"2022_06","sequence":"MSGLGDSSSDPANPDSHKRKGSPCDTLASSTEKRRREQENKYLEELAELLSANISDIDSLSVKPDKCKILKKTVDQIQLMKRMEQEKSTTDDDVQKSDISSSSQGVIEKESLGPLLLEALDGFFFVVNCEGRIVFVSENVTSYLGYNQEELMNTSVYSILHVGDHAEFVKNLLPKSLVNGVPWPQEATRRNSHTFNCRMLIHPPEDPGTENQEACQRYEVMQCFTVSQPKSIQEDGEDFQSCLICIARRLPRPPAITGVESFMTKQDTTGKIISIDTSSLRAAGRTGWEDLVRKCIYAFFQPQGREPSYARQLFQEVMTRGTASSPSYRFILNDGTMLSAHTKCKLCYPQSPDMQPFIMGIHIIDREHSGLSPQDDSNSGMSIPRINPSVNPGISPAHGVTRSSTLPPSNNNMVSARVNRQQSSDLNSSSSHTNSSNNQGNFGCSPGNQIVANVALNQGQAGSQSSNPSLNLNNSPMEGTGIALSQFMSPRRQANSGLATRARMSNNSFPPNIPTLSSPVGITSGACNNNNRSYSNIPVTSLQGMNEGPNNSVGFSAGSPVLRQMSSQNSPSRLSMQPAKAESKDSKEIASILNEMIQSDNSDNSANEGKPLDSGLLHNNDRLSEGDSKYSQTSHKLVQLLTTTAEQQLRHADIDTSCKDVLSCTGTSSSASSNPSGGTCPSSHSSLTERHKILHRLLQEGSPSDITTLSVEPEKKDSVPASTAVSVSGQSQGSASIKLELDAAKKKESKDHQLLRYLLDKDEKDLRSTPNLCLDDVKVKVEKKEQMDPCNTNPTPMTKPAPEEVKLESQSQFTADLDQFDQLLPTLEKAAQLPSLCETDRMDGAVTGVSIKAEVLPASLQPTTARAAPRLSRLPELELEAIDNQFGQPGAGDQIPWANNTLTTINQNKPEDQCISSQLDELLCPPTTVEGRNDEKALLEQLVSFLSGKDETELAELDRALGIDKLVQGGGLDVLSERFPPQQATPPLMMEDRPTLYSQPYSSPSPTAGLSGPFQGMVRQKPSLGAMPVQVTPPRGTFSPNMGMQPRQTLNRPPAAPNQLRLQLQQRLQGQQQLMHQNRQAILNQFAANAPVGMNMRSGMQQQITPQPPLNAQMLAQRQRELYSQQHRQRQIIQQQRAMLMRHQSFGNNIPPSSGLPVQMGTPRLPQGAPQQFPYPPNYGTNPGTPPASTSPFSQLAANPEASLATRSSMVNRGMAGNMGGQFGAGISPQMQQNVFQYPGPGLVPQGEATFAPSLSPGSSMVPMPVPPPQSSLLQQTPPTSGYQSPDMKAWQQGTMGNNNVFSQAVQSQPAPAQPGVYNNMSITVSMAGGNANIQNMNPMMGQMQMSSLQMPGMNTVCSEQMNDPALRHTGLYCNQLSSTDLLKTDADGNQQVQQVQVFADVQCTVNLVGGDPYLNQPGPLGTQKPTSGPQTPQAQQKSLLQQLLTE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"Ncoa1"},"synonyms":[{"value":"Src1"}]}],"alphafold_very_low_content":0.718728403593642,"disorder_content":0.013130615065653075,"disprot_consensus":{"full":[{"start":367,"end":385,"type":"D"}],"Structural state":[{"start":367,"end":385,"type":"D"}]}},{"disprot_id":"DP03697","acc":"Q07820","creator":"vnugnes","date":"2022-05-31T18:45:02.494Z","features":{"pfam":[{"id":"PF00452","name":"Apoptosis regulator proteins, Bcl-2 family","start":213,"end":312}],"gene3D":[]},"length":350,"name":"Induced myeloid leukemia cell differentiation protein Mcl-1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":192,"end":201,"reference_id":"29339518","reference_source":"pmid","reference_html":"Iterative optimization yields Mcl-1-targeting stapled peptides with selective cytotoxicity to Mcl-1-dependent cancer cells. <i> Rezaei Araghi R, Bird GH, Ryan JA, Jenson JM, Godes M, Pritz JR, Grant RA, Letai A, Walensky LD, Keating AE. </i> Proc Natl Acad Sci U S A, 2018","date":"2022-05-31T19:05:48.060Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5W89"}],"region_id":"DP03697r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"We determined the crystal structures of SAH-MS1-14 and SAH-MS1-18 in complex with Mcl-1 at 1.9 Å and 1.4 Å resolution (SI Appendix, Table S5), respectively, to probe how hydrocarbon stapling achieved the observed affinity enhancements."},{"type":"Curator statement","text":"SAH-MS1-18 corresponds to a modified Bim BH3 peptide \"XIWLLQELLRLGDEINARYARX\"."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"sequence_construct":"GDELYRQSLEIISRYLREQATGAKDTKPMGRSGATSRKALETLRRVGDGVQRNHETAFQGMLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQESCIEPLAESITDVLVRTKRDWLVKQRGWDGFVEFFHV","statement":[{"text":"The lack of electron density in this region, as shown in the PDB, indicates it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-01T09:45:10.762Z"}},{"start":192,"end":201,"reference_id":"26878343","reference_source":"pmid","reference_html":"Discovery of 2-Indole-acylsulfonamide Myeloid Cell Leukemia 1 (Mcl-1) Inhibitors Using Fragment-Based Methods. <i> Pelz NF, Bian Z, Zhao B, Shaw S, Tarr JC, Belmar J, Gregg C, Camper DV, Goodwin CM, Arnold AL, Sensintaffar JL, Friberg A, Rossanese OW, Lee T, Olejniczak ET, Fesik SW. </i> J Med Chem, 2016","date":"2022-06-08T14:59:30.434Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5FC4"}],"region_id":"DP03697r002","sequence_construct":"GDELYRQSLEIISRYLREQATGAKDTKPMGRAGATSRKALETLRRVGDGVQRNHETAFQGMLRKLDIANEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQESCIAPLAESITDVLVRTKRDWLVAQRGWDGFVEFFH","statement":[{"text":"The lack of electron density in this region, as shown in the PDB, indicates it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEMBL","id":"90085661"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEMBL","id":"762936"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-08T15:28:35.567Z"}},{"start":193,"end":203,"reference_id":"20392693","reference_source":"pmid","reference_html":"Apoptotic regulation by MCL-1 through heterodimerization. <i> Liu Q, Moldoveanu T, Sprules T, Matta-Camacho E, Mansur-Azzam N, Gehring K. </i> J Biol Chem, 2010","date":"2022-05-31T20:06:07.667Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"2KBW"}],"region_id":"DP03697r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P55957","statements":[{"type":"Methods","text":"In titration studies, unlabeled ligands were added to 15N-labeled cMCL-1 or cBID until saturation."}]}],"sequence_construct":"TPPPAEEEEDELYRQSLEIISRYLREQATGAKDTKPMGRSGATSRKALETLRRVGDGVQRNHETAFQGMLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQESCIEPLAESITDVLVRTKRDWLVKQRGWDGFVEFFHVEDLEG","statement":[{"text":"The final ensemble (Fig. 4C) of structures with the lowest energies and the fewest violations had a mean root mean square deviation from the average of 0.38 Å for backbone atoms, excluding the residues at the termini (residues 167–172 and 320–326 in cMCL-1; residues 76–78 and 100–106 in BID-BH3) and the ones in the disordered loop between helices α1 and α2 (cMCL-1 residues 193–203).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-01T09:01:31.145Z"}}],"regions_counter":3,"released":"2022_06","sequence":"MFGLKRNAVIGLNLYCGGAGLGAGSGGATRPGGRLLATEKEASARREIGGGEAGAVIGGSAGASPPSTLTPDSRRVARPPPIGAEVPDVTATPARLLFFAPTRRAAPLEEMEAPAADAIMSPEEELDGYEPEPLGKRPAVLPLLELVGESGNNTSTDGSLPSTPPPAEEEEDELYRQSLEIISRYLREQATGAKDTKPMGRSGATSRKALETLRRVGDGVQRNHETAFQGMLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQESCIEPLAESITDVLVRTKRDWLVKQRGWDGFVEFFHVEDLEGGIRNVLLAFAGVAGVGAGLAYLIR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"MCL1"},"synonyms":[{"value":"BCL2L3"}]}],"alphafold_very_low_content":0.47714285714285715,"disorder_content":0.03428571428571429,"disprot_consensus":{"full":[{"start":192,"end":203,"type":"D"}],"Structural state":[{"start":192,"end":203,"type":"D"}]}},{"disprot_id":"DP03698","acc":"Q8IEU1","creator":"gbalatti","date":"2022-05-31T21:20:30.317Z","features":{"pfam":[{"id":"PF09716","name":"Malarial early transcribed membrane protein (ETRAMP)","start":1,"end":88},{"id":"PF11567","name":"Plasmodium falciparum UIS3 membrane protein","start":129,"end":229}],"gene3D":[]},"length":229,"name":"Early transcribed membrane protein 13","ncbi_taxon_id":36329,"organism":"Plasmodium falciparum (isolate 3D7)","regions":[{"start":130,"end":148,"reference_id":"18577521","reference_source":"pmid","reference_html":"Crystal structure of soluble domain of malaria sporozoite protein UIS3 in complex with lipid. <i> Sharma A, Yogavel M, Akhouri RR, Gill J, Sharma A. </i> J Biol Chem, 2008","date":"2022-06-14T00:27:36.918Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006222","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":20,"statements":[{"type":"Methods","text":"crystals were obtained at 20 °C by hanging drop vapor diffusion method using 1 μl each of PfUIS3130-229 (10 mg ml-1) and 0.1 m MES, pH 6.5, 12% polyethylene glycol 20,000, 0.01 m dithiothreitol (mother liquor)."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":6.5,"statements":[{"type":"Methods","text":"crystals were obtained at 20 °C by hanging drop vapor diffusion method using 1 μl each of PfUIS3130-229 (10 mg ml-1) and 0.1 m MES, pH 6.5, 12% polyethylene glycol 20,000, 0.01 m dithiothreitol (mother liquor)."}]}],"cross_refs":[{"db":"PDB","id":"2VWA"}],"region_id":"DP03698r001","statement":[{"text":"Residues from 130 –148 form a random coil (C1) at the N terminus, and this is followed by an alpha-helix (H1, residues 149 –169).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-14T22:30:38.447Z"}},{"start":83,"end":129,"reference_id":"18577521","reference_source":"pmid","reference_html":"Crystal structure of soluble domain of malaria sporozoite protein UIS3 in complex with lipid. <i> Sharma A, Yogavel M, Akhouri RR, Gill J, Sharma A. </i> J Biol Chem, 2008","date":"2022-06-14T02:14:42.113Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001191","ec_ontology":"ECO","ec_name":"in vitro cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2VWA"}],"region_id":"DP03698r003","statement":[{"text":"Analysis of the PfUIS3 dimer-monomer transition using gel filtration chromatography and SDS-PAGE suggested that dimeric PfUIS3 underwent proteolysis and reduced to a stable, soluble domain spanning residues 130 –229 (Fig. 1a).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-14T22:30:17.829Z"}},{"start":83,"end":129,"reference_id":"18577521","reference_source":"pmid","reference_html":"Crystal structure of soluble domain of malaria sporozoite protein UIS3 in complex with lipid. <i> Sharma A, Yogavel M, Akhouri RR, Gill J, Sharma A. </i> J Biol Chem, 2008","date":"2022-06-14T02:18:19.485Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001191","ec_ontology":"ECO","ec_name":"in vitro cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2VWA"}],"region_id":"DP03698r004","statement":[{"text":"Analysis of the PfUIS3 dimer-monomer transition using gel filtration chromatography and SDS-PAGE suggested that dimeric PfUIS3 underwent proteolysis and reduced to a stable, soluble domain spanning residues 130 –229 (Fig. 1a). This suggests that residues within residues 83–129 of PfUIS3\nare likely to be involved in dimerization of PfUIS3.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-14T22:31:05.198Z"}},{"start":83,"end":129,"reference_id":"18577521","reference_source":"pmid","reference_html":"Crystal structure of soluble domain of malaria sporozoite protein UIS3 in complex with lipid. <i> Sharma A, Yogavel M, Akhouri RR, Gill J, Sharma A. </i> J Biol Chem, 2008","date":"2022-06-14T21:15:01.656Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2VWA"}],"region_id":"DP03698r005","statement":[{"text":"Purified PfUIS3 (residues 83–229) was dimeric in solution\nas shown by protein cross-linking experiments and gel filtration\nchromatography (Fig. 1).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-14T22:31:00.284Z"}}],"regions_counter":5,"released":"2023_12","sequence":"MKVSKLVLFAHIFFIINILCQYICLNASKVNKKGKIAEEKKRKNIKNIDKAIEEHNKRKKLIYYSLIASGAIASVAAILGLGYYGYKKSREDDLYYNKYLEYRNGEYNIKYQDGAIASTSEFYIEPEGINKINLNKPIIENKNNVDVSIKRYNNFVDIARLSIQKHFEHLSNDQKDSHVNNMEYMQKFVQGLQENRNISLSKYQENKAVMDLKYHLQKVYANYLSQEEN","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"genes":[{"orfNames":[{"value":"PF3D7_1302200","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAD52157.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAD52157.1"}}]}]}],"alphafold_very_low_content":0.22270742358078602,"disorder_content":0.28820960698689957,"disprot_consensus":{"full":[{"start":83,"end":148,"type":"D"}],"Structural state":[{"start":83,"end":148,"type":"D"}],"Disorder function":[{"start":83,"end":129,"type":"F"}]}},{"disprot_id":"DP03700","acc":"Q9H9R9","creator":"rpancsa","date":"2022-06-01T12:17:44.746Z","features":{"pfam":[{"id":"PF04440","name":"Dysbindin (Dystrobrevin binding protein 1)","start":17,"end":148}],"gene3D":[]},"length":158,"name":"Dysbindin domain-containing protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":158,"reference_id":"35474152","reference_source":"pmid","reference_html":"Backbone and side chain resonance assignment of the intrinsically disordered human DBNDD1 protein.  <i> Wiedemann C, Obika KB, Liebscher S, Jirschitzka J, Ohlenschläger O, Bordusa F. </i> Biomol NMR Assign, 2022","date":"2022-06-01T12:28:21.158Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.5,"statements":[{"type":"Figure","text":"[1H,15N]-HSQC spectrum of 13C,15N-labeled human DBNDD1 in 10 mM NaPi, pH 6.5, 150 mM NaCl, 0.1 mM DSS, 90% H2O/10% D2O at 283.2 K, recorded at 700.5 MHz."}]}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Article","text":"Of note, the used construct has a thrombin cleavage site between the N-terminal His6 tag and the native human DBNDD1 sequence. Although no canonical thrombin cleavage site is predicted within human DBNDD1 sequence, the addition of thrombin led to the rapid protein degradation. Therefore, the removal of the purification tag was omitted, and the amino acid numbering is as follows: −19 to 0 indicates the purification tag, the native human DBNDD1 sequence starts with methionine number 1."}]}],"cross_refs":[{"db":"BMRB","id":"51301"}],"region_id":"DP03700r001","statement":[{"text":"In agreement with a predicted low overall secondary structure content, the [1H,15N]-HSQC spectrum of human DBNDD1 shows limited signal dispersion in the 1HN dimension (Fig. 2).","type":"Article"},{"text":"An overall intrinsic disorder of DBNDD1 is supported by the application of secondary chemical shifts and the sequence specific SSP method.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T13:21:26.514Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MEPPEGAGTGEIVKEAEVPQAALGVPAQGTGDNGHTPVEEEVGGIPVPAPGLLQVTERRQPLSSVSSLEVHFDLLDLTELTDMSDQELAEVFADSDDENLNTESPAGLHPLPRAGYLRSPSWTRTRAEQSHEKQPLGDPERQATVLDTFLTVERPQED","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"DBNDD1"}}],"alphafold_very_low_content":0.22784810126582278,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":158,"type":"D"}],"Structural state":[{"start":1,"end":158,"type":"D"}]}},{"disprot_id":"DP03701","acc":"Q9HBA0","creator":"rpancsa","date":"2022-06-01T12:33:51.586Z","features":{"pfam":[{"id":"PF00023","name":"Ankyrin repeat","start":238,"end":267},{"id":"PF00520","name":"Ion transport protein","start":475,"end":729}],"gene3D":[]},"length":871,"name":"Transient receptor potential cation channel subfamily V member 4","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":2,"end":148,"reference_id":"35451798","reference_source":"pmid","reference_html":"Backbone NMR assignments of the extensive human and chicken TRPV4 N-terminal intrinsically disordered regions as important players in ion channel regulation.  <i> Goretzki B, Tebbe F, Mitrovic SA, Hellmich UA. </i> Biomol NMR Assign, 2022","date":"2022-06-01T12:45:04.360Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"decreased","value":4.5,"statements":[{"type":"Article","text":"Presumably due to the absence of secondary structure, strong solvent exchange and subsequent line broadening at pH 7 and 298 K substantially hampered protein backbone NMR assignments of the IDR (data not shown). To suppress solvent exchange, all spectra were thus recorded at pH 4.5 with the standard set of triple-resonance NMR experiments (Fig. 2 A, B). Importantly, the decrease in pH did not affect the overall chemical shift dispersion in the [1H, 15N]-TROSY-HSQC spectra of both chicken and human TRPV4-IDR, thus indicating that the folding state of the proteins are not significantly influenced by the change in pH."}]}],"region_id":"DP03701r001","statement":[{"text":"In line with a low overall secondary structure content, the [1H, 15N]-TROSY-HSQC spectra of 13C, 15N-labeled human and chicken TRPV4-IDR (Fig. 2 A, B) show a narrow chemical shift dispersion.","type":"Article"},{"text":"The finding that both human and chicken TRPV4-IDR are highly disordered is further supported by the single residue-specific secondary structure propensities (SSP) calculated from the Cα, Cβ and Hα chemical shifts.","type":"Article"}],"cross_refs":[{"db":"BMRB","id":"51147"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T14:08:14.929Z"}},{"start":2,"end":68,"reference_id":"37443299","reference_source":"pmid","reference_html":"Crosstalk between regulatory elements in disordered TRPV4 N-terminus modulates lipid-dependent channel activity. <i> Goretzki B, Wiedemann C, McCray BA, Schäfer SL, Jansen J, Tebbe F, Mitrovic SA, Nöth J, Cabezudo AC, Donohue JK, Jeffries CM, Steinchen W, Stengel F, Sumner CJ, Hummer G, Hellmich UA. </i> Nat Commun, 2023","date":"2023-08-12T12:02:29.426Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000059","term_name":"self-inhibition","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007634","ec_ontology":"ECO","ec_name":"experimental phenotypic evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03701r002","statement":[{"text":" In contrast, hsTRPV4ΔN68 was hypersensitive to osmotic stimuli and its Ca2+ influx far exceeded that of the native channel, indicating that the IDR N-terminus acts as a dominant autoinhibitory element.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-25T14:57:12.686Z"}},{"start":1,"end":134,"reference_id":"30244966","reference_source":"pmid","reference_html":"Structural Basis of TRPV4 N Terminus Interaction with Syndapin/PACSIN1-3 and PIP<sub>2</sub>. <i> Goretzki B, Glogowski NA, Diehl E, Duchardt-Ferner E, Hacker C, Gaudet R, Hellmich UA. </i> Structure, 2018","date":"2023-08-26T10:43:23.237Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03701r003","statement":[{"text":"With increasing length of the N-terminus, the degree of unstructured contributions increases, indicating that the regions preceding the ARD are largely unstructured. The comparison with the respective N-terminal constructs from chicken and human TRPV4 confirms that this architecture is observed across species (Fig. 1, S1).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-28T14:16:58.679Z"}}],"regions_counter":3,"released":"2023_12","sequence":"MADSSEGPRAGPGEVAELPGDESGTPGGEAFPLSSLANLFEGEDGSLSPSPADASRPAGPGDGRPNLRMKFQGAFRKGVPNPIDLLESTLYESSVVPGPKKAPMDSLFDYGTYRHHSSDNKRWRKKIIEKQPQSPKAPAPQPPPILKVFNRPILFDIVSRGSTADLDGLLPFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSNGRNDTIPVLLDIAERTGNMREFINSPFRDIYYRGQTALHIAIERRCKHYVELLVAQGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPHIVNYLTENPHKKADMRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLLKCARLFPDSNLEAVLNNDGLSPLMMAAKTGKIGIFQHIIRREVTDEDTRHLSRKFKDWAYGPVYSSLYDLSSLDTCGEEASVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYINVVSYLCAMVIFTLTAYYQPLEGTPPYPYRTTVDYLRLAGEVITLFTGVLFFFTNIKDLFMKKCPGVNSLFIDGSFQLLYFIYSVLVIVSAALYLAGIEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCANMKVCNEDQTNCTVPTYPSCRDSETFSTFLLDLFKLTIGMGDLEMLSSTKYPVVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTILDIERSFPVFLRKAFRSGEMVTVGKSSDGTPDRRWCFRVDEVNWSHWNQNLGIINEDPGKNETYQYYGFSHTVGRLRRDRWSSVVPRVVELNKNSNPDEVVVPLDSMGNPRCDGHQQGYPRKWRTDDAPL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"TRPV4"},"synonyms":[{"value":"VRL2"},{"value":"VROAC"}]}],"alphafold_very_low_content":0.25832376578645233,"disorder_content":0.16991963260619977,"disprot_consensus":{"full":[{"start":1,"end":148,"type":"D"}],"Structural state":[{"start":1,"end":148,"type":"D"}],"Disorder function":[{"start":2,"end":68,"type":"F"}]}},{"disprot_id":"DP03702","acc":"A0A1D5PXA5","creator":"rpancsa","date":"2022-06-01T12:41:18.058Z","features":{"pfam":[{"id":"PF00023","name":"Ankyrin repeat","start":224,"end":253},{"id":"PF00520","name":"Ion transport protein","start":462,"end":715}],"gene3D":[]},"length":852,"name":"Transient receptor potential cation channel subfamily V member 4","ncbi_taxon_id":9031,"organism":"Gallus gallus","regions":[{"start":2,"end":134,"reference_id":"35451798","reference_source":"pmid","reference_html":"Backbone NMR assignments of the extensive human and chicken TRPV4 N-terminal intrinsically disordered regions as important players in ion channel regulation.  <i> Goretzki B, Tebbe F, Mitrovic SA, Hellmich UA. </i> Biomol NMR Assign, 2022","date":"2022-06-01T12:44:23.904Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"decreased","value":4.5,"statements":[{"type":"Article","text":"Presumably due to the absence of secondary structure, strong solvent exchange and subsequent line broadening at pH 7 and 298 K substantially hampered protein backbone NMR assignments of the IDR (data not shown). To suppress solvent exchange, all spectra were thus recorded at pH 4.5 with the standard set of triple-resonance NMR experiments (Fig. 2 A, B). Importantly, the decrease in pH did not affect the overall chemical shift dispersion in the [1H, 15N]-TROSY-HSQC spectra of both chicken and human TRPV4-IDR, thus indicating that the folding state of the proteins are not significantly influenced by the change in pH."}]}],"cross_refs":[{"db":"BMRB","id":"51172"}],"region_id":"DP03702r001","statement":[{"text":"In line with a low overall secondary structure content, the [1H, 15N]-TROSY-HSQC spectra of 13C, 15N-labeled human and chicken TRPV4-IDR (Fig. 2 A, B) show a narrow chemical shift dispersion.","type":"Article"},{"text":"The finding that both human and chicken TRPV4-IDR are highly disordered is further supported by the single residue-specific secondary structure propensities (SSP) calculated from the Cα, Cβ and Hα chemical shifts.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T14:08:28.689Z"}},{"start":2,"end":134,"reference_id":"37443299","reference_source":"pmid","reference_html":"Crosstalk between regulatory elements in disordered TRPV4 N-terminus modulates lipid-dependent channel activity. <i> Goretzki B, Wiedemann C, McCray BA, Schäfer SL, Jansen J, Tebbe F, Mitrovic SA, Nöth J, Cabezudo AC, Donohue JK, Jeffries CM, Steinchen W, Stengel F, Sumner CJ, Hummer G, Hellmich UA. </i> Nat Commun, 2023","date":"2023-08-12T11:40:03.161Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03702r002","statement":[{"text":"Analytical size-exclusion chromatography (SEC) and SEC-MALS (SEC multi-angle light scattering) showed that these constructs are monomeric, while circular dichroism (CD) spectroscopy and the narrow chemical shift dispersion of the [1H, 15N]-TROSY-HSQC NMR spectra of the 15N-labeled TRPV4 IDR in isolation or in the context of the NTD confirmed its high amount of disorder5 (Fig. 1c–e; Supplementary Fig. 2). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-25T15:12:49.906Z"}},{"start":2,"end":134,"reference_id":"37443299","reference_source":"pmid","reference_html":"Crosstalk between regulatory elements in disordered TRPV4 N-terminus modulates lipid-dependent channel activity. <i> Goretzki B, Wiedemann C, McCray BA, Schäfer SL, Jansen J, Tebbe F, Mitrovic SA, Nöth J, Cabezudo AC, Donohue JK, Jeffries CM, Steinchen W, Stengel F, Sumner CJ, Hummer G, Hellmich UA. </i> Nat Commun, 2023","date":"2023-08-12T15:53:08.936Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03702r003","statement":[{"text":"Analytical size-exclusion chromatography (SEC) and SEC-MALS (SEC multi-angle light scattering) showed that these constructs are monomeric, while circular dichroism (CD) spectroscopy and the narrow chemical shift dispersion of the [1H, 15N]-TROSY-HSQC NMR spectra of the 15N-labeled TRPV4 IDR in isolation or in the context of the NTD confirmed its high amount of disorder5 (Fig. 1c–e; Supplementary Fig. 2).  Chemical shift based secondary structure predictions showed that the TRPV4 IDR contains no appreciable secondary structure5.","type":"Results"}],"cross_refs":[{"db":"BMRB","id":"51172"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-25T15:12:50.215Z"}},{"start":2,"end":134,"reference_id":"37443299","reference_source":"pmid","reference_html":"Crosstalk between regulatory elements in disordered TRPV4 N-terminus modulates lipid-dependent channel activity. <i> Goretzki B, Wiedemann C, McCray BA, Schäfer SL, Jansen J, Tebbe F, Mitrovic SA, Nöth J, Cabezudo AC, Donohue JK, Jeffries CM, Steinchen W, Stengel F, Sumner CJ, Hummer G, Hellmich UA. </i> Nat Commun, 2023","date":"2023-08-12T11:42:12.019Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03702r004","statement":[{"text":"Small angle X-ray scattering (SAXS) probes the molecular shape of a molecule in solution. An IDR-containing protein is best described as a structural ensemble, rather than as a single structure, which can be analyzed by SEC-coupled small-angle X-ray scattering (SEC-SAXS) and subsequent Ensemble Optimization Method (EOM) analysis37,38. The isolated TRPV4 IDR is highly flexible and fluctuates between numerous conformations that, as a population, produce a skewed real-space scattering pair-distance distribution function, or p(r) profile that extends to ~12.5–15 nm (Fig. 1f, Supplementary Fig. 3). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-25T15:11:58.666Z"}},{"start":2,"end":134,"reference_id":"37443299","reference_source":"pmid","reference_html":"Crosstalk between regulatory elements in disordered TRPV4 N-terminus modulates lipid-dependent channel activity. <i> Goretzki B, Wiedemann C, McCray BA, Schäfer SL, Jansen J, Tebbe F, Mitrovic SA, Nöth J, Cabezudo AC, Donohue JK, Jeffries CM, Steinchen W, Stengel F, Sumner CJ, Hummer G, Hellmich UA. </i> Nat Commun, 2023","date":"2023-08-12T11:43:15.130Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03702r005","statement":[{"text":"For the IDR, rapid high HDX was apparent in the resolved parts (residues 3–24, 29–55, and 72–105) substantiating its unstructured character.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-25T15:12:00.482Z"}},{"start":2,"end":134,"reference_id":"37443299","reference_source":"pmid","reference_html":"Crosstalk between regulatory elements in disordered TRPV4 N-terminus modulates lipid-dependent channel activity. <i> Goretzki B, Wiedemann C, McCray BA, Schäfer SL, Jansen J, Tebbe F, Mitrovic SA, Nöth J, Cabezudo AC, Donohue JK, Jeffries CM, Steinchen W, Stengel F, Sumner CJ, Hummer G, Hellmich UA. </i> Nat Commun, 2023","date":"2023-08-26T10:48:27.802Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001164","ec_ontology":"ECO","ec_name":"co-sedimentation assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03702r006","statement":[{"text":"Indeed, neither the isolated ARD, nor NTDΔN120, also containing the proline-rich region, interacted with POPC/POPG liposomes in a sedimentation assay (Fig. 7a, b, Supplementary Fig. 10a, b). In contrast, ~75% of the native NTD was found bound to liposomes.","type":"Results"}],"ec_go":"IPI","term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"ChEBI","id":"34080","operator":"and","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"73001","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-28T14:17:19.220Z"}},{"start":2,"end":134,"reference_id":"37443299","reference_source":"pmid","reference_html":"Crosstalk between regulatory elements in disordered TRPV4 N-terminus modulates lipid-dependent channel activity. <i> Goretzki B, Wiedemann C, McCray BA, Schäfer SL, Jansen J, Tebbe F, Mitrovic SA, Nöth J, Cabezudo AC, Donohue JK, Jeffries CM, Steinchen W, Stengel F, Sumner CJ, Hummer G, Hellmich UA. </i> Nat Commun, 2023","date":"2023-08-26T10:46:10.934Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","region_id":"DP03702r007","statement":[{"text":"NMR chemical shift perturbation assays allowed identification of the lipid-interacting IDR residues (Fig. 7c–e, see Supplementary Fig. 11 for 13C, 15N-labeled IDRAAWAA backbone assignments). In the native IDR, ~75% of all residues showed line-broadening in the presence of POPG-containing liposomes.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"ChEBI","id":"34080","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-28T14:17:19.845Z"}},{"start":1,"end":134,"reference_id":"30244966","reference_source":"pmid","reference_html":"Structural Basis of TRPV4 N Terminus Interaction with Syndapin/PACSIN1-3 and PIP<sub>2</sub>. <i> Goretzki B, Glogowski NA, Diehl E, Duchardt-Ferner E, Hacker C, Gaudet R, Hellmich UA. </i> Structure, 2018","date":"2023-08-26T10:43:51.848Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03702r008","statement":[{"text":"With increasing length of the N-terminus, the degree of unstructured contributions increases, indicating that the regions preceding the ARD are largely unstructured. The comparison with the respective N-terminal constructs from chicken and human TRPV4 confirms that this architecture is observed across species (Fig. 1, S1).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-28T14:17:11.621Z"}},{"start":121,"end":134,"reference_id":"30244966","reference_source":"pmid","reference_html":"Structural Basis of TRPV4 N Terminus Interaction with Syndapin/PACSIN1-3 and PIP<sub>2</sub>. <i> Goretzki B, Glogowski NA, Diehl E, Duchardt-Ferner E, Hacker C, Gaudet R, Hellmich UA. </i> Structure, 2018","date":"2023-08-12T16:02:08.436Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03702r009","statement":[{"text":"Neither the isolated PRR (residues 121–134) nor the PRR with the PBD (PBD-PRR, residues 105–134) contain α-helices or β-sheets (Fig. S2).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-17T16:22:05.187Z"}},{"start":105,"end":134,"reference_id":"30244966","reference_source":"pmid","reference_html":"Structural Basis of TRPV4 N Terminus Interaction with Syndapin/PACSIN1-3 and PIP<sub>2</sub>. <i> Goretzki B, Glogowski NA, Diehl E, Duchardt-Ferner E, Hacker C, Gaudet R, Hellmich UA. </i> Structure, 2018","date":"2023-08-12T16:02:15.821Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03702r010","statement":[{"text":"Neither the isolated PRR (residues 121–134) nor the PRR with the PBD (PBD-PRR, residues 105–134) contain α-helices or β-sheets (Fig. S2).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-17T16:21:52.232Z"}},{"start":105,"end":134,"reference_id":"30244966","reference_source":"pmid","reference_html":"Structural Basis of TRPV4 N Terminus Interaction with Syndapin/PACSIN1-3 and PIP<sub>2</sub>. <i> Goretzki B, Glogowski NA, Diehl E, Duchardt-Ferner E, Hacker C, Gaudet R, Hellmich UA. </i> Structure, 2018","date":"2023-08-12T16:32:10.568Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03702r011","statement":[{"text":"The absence of α-helices or β-sheets in the TRPV4-PBD-PRR region is also supported by the secondary structure analysis based on the PBD-PRR NMR backbone assignment. Here, the chemical shift-based prediction of the torsion angles indicates that a polyproline helix contribution may be present (Fig. S3).","type":"Results"},{"text":"As expected for an unstructured peptide, the PBD-PRR peptide shows overall high flexibility in the absence of the PACSIN3 SH3 domain, with very high mobility in the C-terminus. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-17T16:21:27.873Z"}},{"start":121,"end":134,"reference_id":"30244966","reference_source":"pmid","reference_html":"Structural Basis of TRPV4 N Terminus Interaction with Syndapin/PACSIN1-3 and PIP<sub>2</sub>. <i> Goretzki B, Glogowski NA, Diehl E, Duchardt-Ferner E, Hacker C, Gaudet R, Hellmich UA. </i> Structure, 2018","date":"2023-08-12T16:26:44.502Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0017124","term_name":"SH3 domain binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val131Ile","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"A chicken TRPV4-PRR with a single substitution (V131I) was used for structure determination."}]}],"cross_refs":[{"db":"PDB","id":"6F55"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q1G1I6","operator":null,"partner_start":374,"partner_end":437},{"db":"UniProt","id":"O13154","operator":"and","partner_start":388,"partner_end":448},{"db":"UniProt","id":"A0A8V1AAI8","operator":"and","partner_start":386,"partner_end":445}],"region_id":"DP03702r012","statement":[{"text":"To obtain a high-resolution view of the interaction of TRPV4 with a desensitizing protein, we determined the solution NMR structure of the chicken PACSIN3 SH3 domain in complex with the TRPV4-PRR (Fig. 3A, S4, Table 1).","type":"Results"},{"text":"Using 15N-labeled PACSIN1 and 2 SH3 domains as reporters, we performed chemical shift perturbation experiments to map the TRPV4-PRR interacting residues. All three PACSIN SH3 domains share the same binding interface with the TRPV4-PRR. ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins.\" [GOC:go_curators, Pfam:PF00018]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-25T15:08:16.746Z"}},{"start":105,"end":134,"reference_id":"30244966","reference_source":"pmid","reference_html":"Structural Basis of TRPV4 N Terminus Interaction with Syndapin/PACSIN1-3 and PIP<sub>2</sub>. <i> Goretzki B, Glogowski NA, Diehl E, Duchardt-Ferner E, Hacker C, Gaudet R, Hellmich UA. </i> Structure, 2018","date":"2023-08-12T16:35:10.702Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0017124","term_name":"SH3 domain binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","region_id":"DP03702r013","statement":[{"text":"Upon binding of PACSIN3 SH3, the entire peptide becomes less flexible. In agreement with the complex structure, the effects are most pronounced in the PRR, particularly for K122, G123, A125 and N127. ","type":"Results"},{"text":"As expected, PACSIN3 SH3 domain binding to the 15N-TRPV4-PBD-PRR induces chemical shift changes for residues in the PRR, particularly K122, G123, A125 and N127 (Fig. 4A, red line). Chemical shift perturbations are also observed for residues in the linker between the PBD and PRR (e.g. V120 and R112) and even within the PBD (e.g. W109). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins.\" [GOC:go_curators, Pfam:PF00018]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-25T15:00:47.008Z"}},{"start":107,"end":111,"reference_id":"30244966","reference_source":"pmid","reference_html":"Structural Basis of TRPV4 N Terminus Interaction with Syndapin/PACSIN1-3 and PIP<sub>2</sub>. <i> Goretzki B, Glogowski NA, Diehl E, Duchardt-Ferner E, Hacker C, Gaudet R, Hellmich UA. </i> Structure, 2018","date":"2023-08-12T16:39:19.856Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0035091","term_name":"phosphatidylinositol binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","region_id":"DP03702r014","statement":[{"text":"In contrast to the effects of the PACSIN3 SH3 domain, when PIP2 is added, it exclusively affects residues in and around the previously identified PIP2 binding domain (107KRWRR111) in the PBD-PRR (Garcia-Elias et al., 2013), as indicated by strong shifts and peak broadening of the corresponding NMR resonances (Fig. 4A, yellow line).","type":"Results"},{"text":"PI(4,5)P2 gives rise to three peaks in the 31P spectrum corresponding to the three phosphate groups at the 1, 4, and 5 positions of the lipid headgroup (Fig. 4E-G). PIP2 was titrated with PBDKRWRR-PRR or the mutant PBDAAWAA-PRR. While the PBDKRWRR-PRR peptide interacts with PIP2 with a KD in the μM range (139.8±1.9 μM), the PBDAAWAA-PRR affinity is more than one order of magnitude lower (2.7±0.1 mM) (Fig. 4D). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to an inositol-containing glycerophospholipid, i.e. phosphatidylinositol (PtdIns) and its phosphorylated derivatives.\" [GOC:bf, ISBN:0198506732, PMID:11395417]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-25T15:00:14.517Z"}}],"regions_counter":14,"released":"2023_12","sequence":"MADPEDPRDAGDVLGDDSFPLSSLANLFEVEDTPSPAEPSRGPPGAVDGKQNLRMKFHGAFRKGPPKPMELLESTIYESSVVPAPKKAPMDSLFDYGTYRQHPSENKRWRRRVVEKPVAGTKGPAPNPPPILKVFNRPILFDIVSRGSPDGLEGLLSFLLTHKKRLTDEEFREPSTGKTCLPKALLNLSAGRNDTIPILLDIAEKTGNMREFINSPFRDVYYRGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFFQPKDEGGYFYFGELPLSLAACTNQPHIVHYLTENGHKQADLRRQDSRGNTVLHALVAIADNTRENTKFVTKMYDLLLIKCAKLFPDTNLEALLNNDGLSPLMMAAKTGKIGIFQHIIRREIADEDVRHLSRKFKDWAYGPVYSSLYDLSSLDTCGEEVSVLEILVYNSKIENRHEMLAVEPINELLRDKWRKFGAVSFYISVVSYLCAMIIFTLIAYYRPMEGPPPYPYTTTIDYLRLAGEIITLLTGILFFFSNIKDLFMKKCPGVNSFFIDGSFQLLYFIYSVLVIVTAGLYLGGVEAYLAVMVFALVLGWMNALYFTRGLKLTGTYSIMIQKILFKDLFRFLLVYLLFMIGYASALVSLLNPCPSSESCSEDHSNCTLPTYPSCRDSQTFSTFLLDLFKLTIGMGDLEMLESAKYPGVFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKHIWKLQWATTILDIERSFPLFLRRVFRSGEMVTVGKGTDGTPDRRWCFRVDEVNWSHWNQNLGIISEDPGKSDTYQYYGFSHTVGRLRRDRWSTVVPRVVELNKSCPTEDVVVPLGTMGTAEARERRHGQTPSSPL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Phasianinae","Gallus"],"genes":[{"name":{"value":"TRPV4"}}],"alphafold_very_low_content":0.23591549295774647,"disorder_content":0.1572769953051643,"disprot_consensus":{"full":[{"start":1,"end":134,"type":"D"}],"Structural state":[{"start":1,"end":134,"type":"D"}],"Molecular function":[{"start":2,"end":134,"type":"F"}]}},{"disprot_id":"DP03703","acc":"Q8N660","creator":"rpancsa","date":"2022-06-01T12:58:47.992Z","features":{"pfam":[{"id":"PF06758","name":"Olduvai domain","start":179,"end":240},{"id":"PF06758","name":"Olduvai domain","start":262,"end":325},{"id":"PF06758","name":"Olduvai domain","start":335,"end":400},{"id":"PF06758","name":"Olduvai domain","start":410,"end":476},{"id":"PF06758","name":"Olduvai domain","start":484,"end":550},{"id":"PF06758","name":"Olduvai domain","start":579,"end":644}],"gene3D":[]},"length":670,"name":"Neuroblastoma breakpoint family member 15","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":174,"end":247,"reference_id":"35098449","reference_source":"pmid","reference_html":"Solution NMR backbone assignments of disordered Olduvai protein domain CON1 employing Hα-detected experiments. <i> Paukovich N, Henen MA, Hussain A, Issaian A, Sikela JM, Hansen KC, Vögeli B. </i> Biomol NMR Assign, 2022","date":"2022-06-01T13:04:56.221Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Figure","text":"CON1 1H-15N HSQC at 25 °C."}]}],"cross_refs":[{"db":"BMRB","id":"51015"}],"region_id":"DP03703r001","statement":[{"text":"We confirmed the disordered nature of CON1 due to the limited peak dispersion shown in the 15N-1H HSQC (Figs. 2a and 3a). The CON1 sequence has low complexity and comprises many stretches of repeated residues or repeated sequences of amino acids. Due to this there is poor dispersion and many overlapping peaks.","type":"Article"},{"text":"The Secondary Structure Propensity score (SSP) (Marsh et al. 2006) gives an estimation of the secondary structure of a protein using available chemical shifts (a score of 1 indicates a fully formed α-helix, while a score of -1 indicates a fully formed β-sheet). IDPs often have scores between − 0.2 and 0.2 indicating no secondary structure elements are present. The SSP scores for CON1, calculated using HN, N, Cα, and Cβ atoms, both at 25 °C and 5 °C show most residues fall within this disordered range (Fig. 4a).","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T14:00:07.214Z"}},{"start":338,"end":552,"reference_id":"31264103","reference_source":"pmid","reference_html":"Solution NMR backbone assignment reveals interaction-free tumbling of human lineage-specific Olduvai protein domains. <i> Issaian A, Schmitt L, Born A, Nichols PJ, Sikela J, Hansen K, Vögeli B, Henen MA. </i> Biomol NMR Assign, 2019","date":"2022-06-01T13:26:18.932Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03703r002","statement":[{"text":"The 15N-1H HSQC of the HSL1-3 triplet showed a peak dispersion characteristic of a disordered protein.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T14:00:08.689Z"}},{"start":338,"end":412,"reference_id":"31264103","reference_source":"pmid","reference_html":"Solution NMR backbone assignment reveals interaction-free tumbling of human lineage-specific Olduvai protein domains. <i> Issaian A, Schmitt L, Born A, Nichols PJ, Sikela J, Hansen K, Vögeli B, Henen MA. </i> Biomol NMR Assign, 2019","date":"2022-06-01T13:36:53.407Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Figure","text":"Top: Sequence alignment between the three assigned NBPF15-HLS domains (HLS1, 2, and 3). Residues corresponding to cloning artefacts and tags are highlighted with a black box, while relevant residues belonging to the protein are highlighted with a red box."}]}],"cross_refs":[{"db":"BMRB","id":"27569"}],"region_id":"DP03703r003","sequence_construct":"SAAAASSASLEKEDQEATGPRLSRELLDEKEPEVLQDSLDRCYSTPSGCLELTDSCQPYRSAFYVLEQQRVGLAIDMDEIEKYQEVLEHHHHHH","statement":[{"text":"The 15N-1H HSQC of the HSL1-3 triplet showed a peak dispersion characteristic of a disordered protein.","type":"Article"},{"text":"We divided the triplet into its three domains HLS1, 2 and 3, while keeping the adjacent linker sequences in all the constructs. Owing to the moderate dispersion of the resonances the assignments success was 90 ± 5% (Table 1) with HLS1 higher than HLS2 and 3.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T14:00:10.141Z"}},{"start":401,"end":487,"reference_id":"31264103","reference_source":"pmid","reference_html":"Solution NMR backbone assignment reveals interaction-free tumbling of human lineage-specific Olduvai protein domains. <i> Issaian A, Schmitt L, Born A, Nichols PJ, Sikela J, Hansen K, Vögeli B, Henen MA. </i> Biomol NMR Assign, 2019","date":"2022-06-01T13:43:11.276Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Figure","text":"Top: Sequence alignment between the three assigned NBPF15-HLS domains (HLS1, 2, and 3). Residues corresponding to cloning artefacts and tags are highlighted with a black box, while relevant residues belonging to the protein are highlighted with a red box."}]}],"region_id":"DP03703r004","sequence_construct":"SAAAASSASLEIDMDEIEKYQEVEEDQDPSCPRLSRELLDEKEPEVLQDSLDRCYSTPSDYLELPDLGQPYSSAVYSLEEQYLGLALDVDRIKKDQEELEHHHHHH","statement":[{"text":"The 15N-1H HSQC of the HSL1-3 triplet showed a peak dispersion characteristic of a disordered protein.","type":"Article"},{"text":"We divided the triplet into its three domains HLS1, 2 and 3, while keeping the adjacent linker sequences in all the constructs. Owing to the moderate dispersion of the resonances the assignments success was 90 ± 5% (Table 1) with HLS1 higher than HLS2 and 3.","type":"Article"}],"cross_refs":[{"db":"BMRB","id":"27533"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T14:00:11.137Z"}},{"start":478,"end":552,"reference_id":"31264103","reference_source":"pmid","reference_html":"Solution NMR backbone assignment reveals interaction-free tumbling of human lineage-specific Olduvai protein domains. <i> Issaian A, Schmitt L, Born A, Nichols PJ, Sikela J, Hansen K, Vögeli B, Henen MA. </i> Biomol NMR Assign, 2019","date":"2022-06-01T13:42:18.376Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Figure","text":"Top: Sequence alignment between the three assigned NBPF15-HLS domains (HLS1, 2, and 3). Residues corresponding to cloning artefacts and tags are highlighted with a black box, while relevant residues belonging to the protein are highlighted with a red box."}]}],"cross_refs":[{"db":"BMRB","id":"27775"}],"region_id":"DP03703r005","sequence_construct":"SAAAASSASLEVDRIKKDQEEEEDQGPPCPRLSRELLEVVEPEVLQDSLDRCYSTPSSCLEQPDSCQPYGSSFYALEEKHVGFSLDLEHHHHHH","statement":[{"text":"The 15N-1H HSQC of the HSL1-3 triplet showed a peak dispersion characteristic of a disordered protein.","type":"Article"},{"text":"We divided the triplet into its three domains HLS1, 2 and 3, while keeping the adjacent linker sequences in all the constructs. Owing to the moderate dispersion of the resonances the assignments success was 90 ± 5% (Table 1) with HLS1 higher than HLS2 and 3.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T14:00:12.825Z"}}],"regions_counter":5,"released":"2023_12","sequence":"MVVSAGPLSSEKAEMNILEINEKLRPQLAEKKQQFRNLKEKCFLTQLAGFLANRQKKYKYEECKDLIKFMLRNERQFKEEKLAEQLKQAEELRQYKVLVHAQERELTQLREKLREGRDASRSLNEHLQALLTPDEPDKSQGQDLQEQLAEGCRLTQHLVQKLSPENDNDDDEDVQVEVAEKVQKSSAPREMQKAEEKEVPEDSLEECAITCSNSHGPYDSNQPHKKTKITFEEDKVDSTLIGSSSHVEWEDAVHIIPENESDDEEEEEKGPVSPRNLQESEEEEVPQESWDEGYSTLSIPPEMLASYQSYSSTFHSLEEQQVCMAVDIGRHRWDQVKKEDQEATGPRLSRELLDEKEPEVLQDSLDRCYSTPSGCLELTDSCQPYRSAFYVLEQQRVGLAIDMDEIEKYQEVEEDQDPSCPRLSRELLDEKEPEVLQDSLDRCYSTPSDYLELPDLGQPYSSAVYSLEEQYLGLALDVDRIKKDQEEEEDQGPPCPRLSRELLEVVEPEVLQDSLDRCYSTPSSCLEQPDSCQPYGSSFYALEEKHVGFSLDVGEIEKKGKGKKRRGRRSKKKRRRGRKEGEDDNPPCPRLYGVLMEVEEPEVLQDSLDRCYSTPSMYFEQPDSFQHYRSVFYSFEEEHISFALYVDNRFFTLTVTSLHLVFQMGVIFPQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"NBPF15","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:28791","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:28791"}}]},"synonyms":[{"value":"NBPF16","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:28791","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:28791"}}]}]}],"alphafold_very_low_content":0.746268656716418,"disorder_content":0.43134328358208956,"disprot_consensus":{"full":[{"start":174,"end":247,"type":"D"},{"start":338,"end":552,"type":"D"}],"Structural state":[{"start":174,"end":247,"type":"D"},{"start":338,"end":552,"type":"D"}]}},{"disprot_id":"DP03704","acc":"A0A1B0GTR3","creator":"rpancsa","date":"2022-06-01T13:54:43.702Z","features":{"pfam":[{"id":"PF27987","name":"Spermatid nuclear transition protein","start":1,"end":104}],"gene3D":[]},"length":108,"name":"Uncharacterized protein CXorf51A","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":108,"reference_id":"34415548","reference_source":"pmid","reference_html":"Backbone and nearly complete side-chain chemical shift assignments reveal the human uncharacterized protein CXorf51A as intrinsically disordered. <i> Wiedemann C, Obika KB, Liebscher S, Jirschitzka J, Ohlenschlãger O, Bordusa F. </i> Biomol NMR Assign, 2021","date":"2022-06-01T14:00:10.300Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.5,"statements":[{"type":"Figure","text":"[1H,15N]-HSQC spectrum of 13C,15N-labeled human CX05A in 10mM Na2HPO4, pH 6.5, 150 mM NaCl, 0.1 mM DSS, 90% H2O/10% D2O at 283.2 K."}]}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Article","text":"Of note, the used construct has a thrombin cleavage site between the N-terminal His6 tag and the native human CX05A sequence. Although no further thrombin cleavage site is predicted within human CX05A sequence, the addition of thrombin led to the rapid degradation of the protein. Therefore, the removal of the purification tag was omitted and the amino acid numbering is as follows: −19 to 0 indicates the purification tag, the native human CX05A sequence starts with methionine number 1."}]}],"cross_refs":[{"db":"BMRB","id":"50944"}],"region_id":"DP03704r001","statement":[{"text":"The signal dispersion in the 1HN dimension is reduced to the region between 8.1 and 8.6 ppm (Fig. ​(Fig.3).3). This limited 1HN chemical shift range is typically observed for proteins or protein parts without a well-defined three-dimensional structure. Therefore, the fast inter-conversion between different conformers or transient states results in ensemble-averaged random coil chemical shift values.","type":"Article"},{"text":"In agreement with the [1H,15N]-HSQC spectrum (Fig. ​(Fig.3),3), the CSI 3.0 web server (Hafsa et al. 2015) predicts an all-coil conformation for CX05A based on our chemical shift assignments (data not shown).","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T09:20:57.687Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MAKVTSEPQKPNEDVDEQTPSTSSTKGRKKGKTPRQRRSRSGVKGLKTTRKAKRPLRGSSSQKAGETNTPAGKPKKARGPILRGRYHRLKEKMKKEEADKEQSETSVL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"CXorf51A","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:30533","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:30533"}}]},"synonyms":[{"value":"CXorf51","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:30533","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:30533"}}]}]}],"alphafold_very_low_content":0.027777777777777776,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":108,"type":"D"}],"Structural state":[{"start":1,"end":108,"type":"D"}]}},{"disprot_id":"DP03705","acc":"O05312","creator":"rpancsa","date":"2022-06-01T21:18:14.243Z","features":{"pfam":[{"id":"PF11314","name":"Protein of unknown function (DUF3117)","start":24,"end":73}],"gene3D":[]},"length":75,"name":"Conserved protein","ncbi_taxon_id":83332,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","regions":[{"start":1,"end":75,"reference_id":"35468422","reference_source":"pmid","reference_html":"Highly conserved protein Rv1211 in Mycobacterium tuberculosis is a natively unfolded protein that binds to a calmodulin antagonist, trifluoperazine. <i> Choo M, Oh S, Jo S, Jin X, Song Y, Wen H, Park S, Kang S. </i> Biochem Biophys Res Commun, 2022","date":"2022-06-01T21:22:52.395Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03705r001","statement":[{"text":"During the purification, we noticed that Rv1211 eluted much faster (70 min) than expected by the molecular weight (7.9 kDa) from the size exclusion column.","type":"Results"},{"text":"In addition, Rv1211 eluted much later than the void volume (49 min), excluding it from being a non-specific aggregate. These results suggested that Rv1211 is either a multimer or a natively-unfolded protein. It is well known that a natively-unfolded protein behaves like a much larger protein during a size exclusion chromatography.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T08:14:44.856Z"}},{"start":1,"end":75,"reference_id":"35468422","reference_source":"pmid","reference_html":"Highly conserved protein Rv1211 in Mycobacterium tuberculosis is a natively unfolded protein that binds to a calmodulin antagonist, trifluoperazine. <i> Choo M, Oh S, Jo S, Jin X, Song Y, Wen H, Park S, Kang S. </i> Biochem Biophys Res Commun, 2022","date":"2022-06-01T21:24:57.340Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03705r002","statement":[{"text":"To characterize the structure of Rv1211 experimentally, we next carried out circular dichroism (CD) spectroscopy which can give information on secondary structure. The spectrum was typical of an unfolded protein (Fig. 2A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T08:14:47.421Z"}},{"start":1,"end":75,"reference_id":"35468422","reference_source":"pmid","reference_html":"Highly conserved protein Rv1211 in Mycobacterium tuberculosis is a natively unfolded protein that binds to a calmodulin antagonist, trifluoperazine. <i> Choo M, Oh S, Jo S, Jin X, Song Y, Wen H, Park S, Kang S. </i> Biochem Biophys Res Commun, 2022","date":"2022-06-01T21:33:41.039Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03705r003","statement":[{"text":"Therefore, we obtained the NMR spectrum of Rv1211 in the absence and presence of Ca2+. The data show that Rv1211's spectrum did not change appreciably according to the presence of Ca2+ (Fig. 3A). In addition, there were no peaks upfield of 0.5 ppm, which is the diagnostic character of natively unfolded proteins, consistent with our CD data. To further confirm the absence of spectral changes by Ca2+ with higher resolution, we obtained two-dimensional 1H–15N HSQC spectra in the presence and absence of Ca2+. The spectra were nearly identical, confirming the absence of Ca2+ binding (Fig. 3B). Again, the narrow chemical shift dispersion on the proton amide region showed that Rv1211 is a natively unfolded protein.","type":"Results"}],"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Methods","text":"All experiments were performed at 25 °C in NMR sample buffer (100 mM Tris-HCl, 50 mM NaCl, pH 7.0)."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":7,"statements":[{"type":"Methods","text":"All experiments were performed at 25 °C in NMR sample buffer (100 mM Tris-HCl, 50 mM NaCl, pH 7.0)."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T08:14:58.228Z"}},{"start":61,"end":74,"reference_id":"35468422","reference_source":"pmid","reference_html":"Highly conserved protein Rv1211 in Mycobacterium tuberculosis is a natively unfolded protein that binds to a calmodulin antagonist, trifluoperazine. <i> Choo M, Oh S, Jo S, Jin X, Song Y, Wen H, Park S, Kang S. </i> Biochem Biophys Res Commun, 2022","date":"2022-06-01T21:46:21.389Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0036094","term_name":"small molecule binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"annotation_extensions":[],"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"45951","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03705r004","statement":[{"text":"Since we already expressed 15N labeled Rv1211, we employed a 1H–15N HSQC NMR assay to monitor the binding.","type":"Results"},{"text":"To identify the binding site between Rv1211 and TFP, we prepared 15N,13C-uniformly double-labeled protein and obtained triple resonance NMR spectra: HNCA, HN(CO)CA, HNCACB, CBCA(CO)NH, HN(CA)CO, and HNCO. The analysis of these three-dimensional spectra led to the assignment of the peak on the 2D 1H–15N HSQC spectrum. Therefore, the peaks that disappeared upon TFP binding (see Fig. 4A) were identified as originating from residues 61D, 63A, 65A, 67G, 68D, 70L, 72G, 73 V, and 74T. These residues are all in the C-terminal part of the protein (Fig. 4B), which is consistent with the binding as a natively unfolded protein.","type":"Results"}],"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T08:15:05.905Z"}},{"start":1,"end":75,"reference_id":"35468422","reference_source":"pmid","reference_html":"Highly conserved protein Rv1211 in Mycobacterium tuberculosis is a natively unfolded protein that binds to a calmodulin antagonist, trifluoperazine. <i> Choo M, Oh S, Jo S, Jin X, Song Y, Wen H, Park S, Kang S. </i> Biochem Biophys Res Commun, 2022","date":"2022-06-01T21:49:31.545Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0036094","term_name":"small molecule binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"annotation_extensions":[],"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"45951","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03705r005","statement":[{"text":"The binding affinity and stoichiometry were also studied using ITC (Fig. 4C). Notably, the binding was endothermic, giving the downward curve. The data analysis shows that the dissociation constant (Kd) is 41 μM, and the binding occurs with a molar ratio of 1 : 2 for Rv1211 and TFP.","type":"Results"}],"term_comment":"Small molecules in GO include monosaccharides but exclude disaccharides and polysaccharides.","term_def":"\"Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule.\" [GOC:curators, GOC:pde, GOC:pm]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T08:15:16.934Z"}}],"regions_counter":5,"released":"2023_12","sequence":"MLGADQARAGGPARIWREHSMAAMKPRTGDGPLEATKEGRGIVMRVPLEGGGRLVVELTPDEAAALGDELKGVTS","taxonomy":["Bacteria","Actinobacteria","Corynebacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"genes":[{"olnNames":[{"value":"Rv1211","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CCP43967.1","url":"https://www.ebi.ac.uk/ena/browser/view/CCP43967.1"}}]}]}],"alphafold_very_low_content":0.013333333333333334,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":75,"type":"D"}],"Structural state":[{"start":1,"end":75,"type":"D"}],"Molecular function":[{"start":1,"end":75,"type":"F"}]}},{"disprot_id":"DP03706","acc":"Q13480","creator":"rpancsa","date":"2022-06-01T21:55:33.997Z","features":{"pfam":[{"id":"PF00169","name":"PH domain","start":6,"end":115}],"gene3D":[]},"length":694,"name":"GRB2-associated-binding protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":613,"end":694,"reference_id":"34929201","reference_source":"pmid","reference_html":"Macromolecular Crowding Induces a Binding Competent Transient Structure in Intrinsically Disordered Gab1. <i> Gruber T, Lewitzky M, Machner L, Weininger U, Feller SM, Balbach J. </i> J Mol Biol, 2022","date":"2022-06-01T21:59:19.624Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Figure","text":"(A) Far-UV CD spectra of Gab1613–694 in 20 mM sodium phosphate, at pH 7.4 and 25 °C."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":7.4,"statements":[{"type":"Figure","text":"(A) Far-UV CD spectra of Gab1613–694 in 20 mM sodium phosphate, at pH 7.4 and 25 °C."}]}],"region_id":"DP03706r001","statement":[{"text":"The far-UV CD spectrum of Gab1613–694 showed a characteristic spectrum of an IDP with a weak negative ellipticity between 210 and 240 nm and a minimum around 200 nm (Figure 2(A), left). This indicates that Gab1613–694 is disordered under these conditions.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T08:38:27.709Z"}},{"start":613,"end":694,"reference_id":"34929201","reference_source":"pmid","reference_html":"Macromolecular Crowding Induces a Binding Competent Transient Structure in Intrinsically Disordered Gab1. <i> Gruber T, Lewitzky M, Machner L, Weininger U, Feller SM, Balbach J. </i> J Mol Biol, 2022","date":"2022-06-01T22:07:29.947Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Methods","text":"NMR experiments were performed on a Bruker Avance III 800 MHz spectrometer equipped with a CP-TCI cryoprobe at 25 °C and a Bruker DRK spectrometer with a proton frequency of 500 MHz. Samples contained 0.2–1 mM Gab1613–694 in 20 mM sodium citrate, 50 mM sodium chloride in 10%(v/v), pH 6.2 and DSS used for chemical shift referencing."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.2,"statements":[{"type":"Methods","text":"NMR experiments were performed on a Bruker Avance III 800 MHz spectrometer equipped with a CP-TCI cryoprobe at 25 °C and a Bruker DRK spectrometer with a proton frequency of 500 MHz. Samples contained 0.2–1 mM Gab1613–694 in 20 mM sodium citrate, 50 mM sodium chloride in 10%(v/v), pH 6.2 and DSS used for chemical shift referencing."}]}],"region_id":"DP03706r002","statement":[{"text":"To investigate the presumed disordered character of Gab613–694 at residue resolution, we measured 1H-15N HSQC spectra. The spectra of nonphosphorylated (Figure S3(A)) and phosphorylated Gab1613–694 (Figure S3(B)) show a low chemical-shift dispersion of the amide protons, which is also indicative of disorder.","type":"Results"}],"cross_refs":[{"db":"BMRB","id":"51019"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T08:38:29.121Z"}},{"start":613,"end":694,"reference_id":"34929201","reference_source":"pmid","reference_html":"Macromolecular Crowding Induces a Binding Competent Transient Structure in Intrinsically Disordered Gab1. <i> Gruber T, Lewitzky M, Machner L, Weininger U, Feller SM, Balbach J. </i> J Mol Biol, 2022","date":"2022-06-01T22:23:07.889Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Methods","text":"NMR experiments were performed on a Bruker Avance III 800 MHz spectrometer equipped with a CP-TCI cryoprobe at 25 °C and a Bruker DRK spectrometer with a proton frequency of 500 MHz. Samples contained 0.2–1 mM Gab1613–694 in 20 mM sodium citrate, 50 mM sodium chloride in 10%(v/v), pH 6.2 and DSS used for chemical shift referencing."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.2,"statements":[{"type":"Methods","text":"NMR experiments were performed on a Bruker Avance III 800 MHz spectrometer equipped with a CP-TCI cryoprobe at 25 °C and a Bruker DRK spectrometer with a proton frequency of 500 MHz. Samples contained 0.2–1 mM Gab1613–694 in 20 mM sodium citrate, 50 mM sodium chloride in 10%(v/v), pH 6.2 and DSS used for chemical shift referencing."}]}],"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":627,"end":627,"position":"Specific residue","statements":[{"type":"Results","text":"The spectra of nonphosphorylated (Figure S3(A)) and phosphorylated Gab1613–694 (Figure S3(B)) show a low chemical-shift dispersion of the amide protons, which is also indicative of disorder."},{"type":"Discussion","text":"Phosphorylation of Y627 and Y659 did not change the R2/R1 relaxation rates, from which we conclude that the number of microstates is not affected by this PTM although both phosphorylations are required for a high affinity binding of Gab1613–694 and the SHP2 tandem domain."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":659,"end":659,"position":"Specific residue","statements":[{"type":"Results","text":"The spectra of nonphosphorylated (Figure S3(A)) and phosphorylated Gab1613–694 (Figure S3(B)) show a low chemical-shift dispersion of the amide protons, which is also indicative of disorder."},{"type":"Discussion","text":"Phosphorylation of Y627 and Y659 did not change the R2/R1 relaxation rates, from which we conclude that the number of microstates is not affected by this PTM although both phosphorylations are required for a high affinity binding of Gab1613–694 and the SHP2 tandem domain."}]}],"cross_refs":[{"db":"BMRB","id":"51018"}],"region_id":"DP03706r003","statement":[{"text":"To investigate the presumed disordered character of Gab613–694 at residue resolution, we measured 1H-15N HSQC spectra. The spectra of nonphosphorylated (Figure S3(A)) and phosphorylated Gab1613–694 (Figure S3(B)) show a low chemical-shift dispersion of the amide protons, which is also indicative of disorder.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T08:38:31.178Z"}},{"start":613,"end":694,"reference_id":"34929201","reference_source":"pmid","reference_html":"Macromolecular Crowding Induces a Binding Competent Transient Structure in Intrinsically Disordered Gab1. <i> Gruber T, Lewitzky M, Machner L, Weininger U, Feller SM, Balbach J. </i> J Mol Biol, 2022","date":"2022-06-01T22:32:37.617Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"annotation_extensions":[],"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":627,"end":627,"position":"Specific residue","statements":[{"type":"Results","text":"The spectra of nonphosphorylated (Figure S3(A)) and phosphorylated Gab1613–694 (Figure S3(B)) show a low chemical-shift dispersion of the amide protons, which is also indicative of disorder."},{"type":"Discussion","text":"Phosphorylation of Y627 and Y659 did not change the R2/R1 relaxation rates, from which we conclude that the number of microstates is not affected by this PTM although both phosphorylations are required for a high affinity binding of Gab1613–694 and the SHP2 tandem domain."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":659,"end":659,"position":"Specific residue","statements":[{"type":"Results","text":"The spectra of nonphosphorylated (Figure S3(A)) and phosphorylated Gab1613–694 (Figure S3(B)) show a low chemical-shift dispersion of the amide protons, which is also indicative of disorder."},{"type":"Discussion","text":"Phosphorylation of Y627 and Y659 did not change the R2/R1 relaxation rates, from which we conclude that the number of microstates is not affected by this PTM although both phosphorylations are required for a high affinity binding of Gab1613–694 and the SHP2 tandem domain."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q06124","operator":null,"partner_start":1,"partner_end":216}],"region_id":"DP03706r004","statement":[{"text":"The affinity between nonphosphorylated or double phosphorylated Gab1613–694 and SHP21–216 was investigated by ITC in absence of any crowders (Figure 5(A and B)). The phosphorylated protein shows a high affinity binding with a KDvalue of 4 ± 1 nM and a 1:1 stoichiometry (n = 0.90 ± 0.01), an enthalpic change of –169.3 ± 0.6 kJ/mol, and an entropy loss of –407 ± 34 J/(mol·K).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T08:38:39.735Z"}},{"start":117,"end":694,"reference_id":"21935523","reference_source":"pmid","reference_html":"Order and disorder in large multi-site docking proteins of the Gab family--implications for signalling complex formation and inhibitor design strategies. <i> Simister PC, Feller SM. </i> Mol Biosyst, 2012","date":"2022-11-10T17:19:24.389Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03706r005","statement":[{"text":"The one common feature of LMD proteins is their structural composition. They have folded N-termini, consisting of a small domain module i.e. pleckstrin homology, PH (Gab1–4), phosphotyrosine-binding, PTB (FRS-2α and 2β) or Src homology 3, SH3 (p130Cas family) domains. A slight variation to this is seen with IRS-1, -2 and -4, and DOK1–7, which have two adjacent folded N-terminal domains (PH and PTB). Beyond the folded N-terminus, there is a long C-terminal extension ostensibly devoid of major structural elements, and hence LMD proteins represent lesser-studied examples of intrinsically disordered (or unstructured) proteins (IDPs or IUPs). ","type":"Introduction"},{"text":"Authors state that the pleckstrin homology (PH) domain, comprised by the 5-116 residues, is the only structured region in GRB2-associated-binding protein 1 (Gab1).","type":"Curator statement"}]}],"regions_counter":5,"released":"2023_12","sequence":"MSGGEVVCSGWLRKSPPEKKLKRYAWKRRWFVLRSGRLTGDPDVLEYYKNDHAKKPIRIIDLNLCQQVDAGLTFNKKEFENSYIFDINTIDRIFYLVADSEEEMNKWVRCICDICGFNPTEEDPVKPPGSSLQAPADLPLAINTAPPSTQADSSSATLPPPYQLINVPPHLETLGIQEDPQDYLLLINCQSKKPEPTRTHADSAKSTSSETDCNDNVPSHKNPASSQSKHGMNGFFQQQMIYDSPPSRAPSASVDSSLYNLPRSYSHDVLPKVSPSSTEADGELYVFNTPSGTSSVETQMRHVSISYDIPPTPGNTYQIPRTFPEGTLGQTSKLDTIPDIPPPRPPKPHPAHDRSPVETCSIPRTASDTDSSYCIPTAGMSPSRSNTISTVDLNKLRKDASSQDCYDIPRAFPSDRSSSLEGFHNHFKVKNVLTVGSVSSEELDENYVPMNPNSPPRQHSSSFTEPIQEANYVPMTPGTFDFSSFGMQVPPPAHMGFRSSPKTPPRRPVPVADCEPPPVDRNLKPDRKVKPAPLEIKPLPEWEELQAPVRSPITRSFARDSSRFPMSPRPDSVHSTTSSSDSHDSEENYVPMNPNLSSEDPNLFGSNSLDGGSSPMIKPKGDKQVEYLDLDLDSGKSTPPRKQKSSGSGSSVADERVDYVVVDQQKTLALKSTREAWTDGRQSTESETPAKSVK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"GAB1"}}],"alphafold_very_low_content":0.6325648414985591,"disorder_content":0.8328530259365994,"disprot_consensus":{"full":[{"start":117,"end":694,"type":"D"}],"Structural state":[{"start":117,"end":694,"type":"D"}],"Molecular function":[{"start":613,"end":694,"type":"F"}]}},{"disprot_id":"DP03707","acc":"P17706-2","creator":"rpancsa","date":"2022-06-02T06:41:51.404Z","features":{"pfam":[],"gene3D":[]},"length":387,"name":"Isoform 2 of Tyrosine-protein phosphatase non-receptor type 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":303,"end":387,"reference_id":"35013194","reference_source":"pmid","reference_html":"The catalytic activity of TCPTP is auto-regulated by its intrinsically disordered tail and activated by Integrin alpha-1. <i> Singh JP, Li Y, Chen YY, Hsu SD, Page R, Peti W, Meng TC. </i> Nat Commun, 2022","date":"2022-06-02T06:48:53.337Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03707r001","statement":[{"text":"The 2D [1H,15N] TROSY spectra of TCPTPCAT (TCPTP catalytic domain residues 1–302; Fig. 1a, b) is of high quality, which allowed the sequence-specific backbone assignment to be readily completed.","type":"Results"},{"text":"We then compared the 2D [1H,15N] TROSY spectra of TCPTPCAT and TCPTP (Fig. 1b; full-length TCPTP residues 1–387; Fig. 1a). The HN/N cross-peaks of TCPTPCAT overlap well with their corresponding peaks in the TCPTP spectrum, demonstrating that the conformation of TCPTPCAT is identical in both constructs. Further, the spectra showed additional peaks in the TCPTP spectrum that clustered in the center of the spectrum between 7.5 and 8.5 ppm (1H dimension). This is typical for flexible, mostly unstructured amino acids, demonstrating that the C-terminal tail of TCPTP is an intrinsically disordered region (IDR) and thus mirrors the behavior of the C-terminal tail of PTP1B.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T08:32:30.678Z"}},{"start":303,"end":387,"reference_id":"35013194","reference_source":"pmid","reference_html":"The catalytic activity of TCPTP is auto-regulated by its intrinsically disordered tail and activated by Integrin alpha-1. <i> Singh JP, Li Y, Chen YY, Hsu SD, Page R, Peti W, Meng TC. </i> Nat Commun, 2022","date":"2022-06-02T06:51:24.631Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03707r002","statement":[{"text":"In contrast, the Rg value for TCPTP was 37.3 ± 0.1 Å, ~10 Å larger than that measured for TCPTPCAT and larger than that expected for a mostly globular protein of ~45 kDa. Thus, these SAXS data are in full agreement with the NMR data and confirm that the TCPTP C-terminal IDR region is extended and dynamic in solution (Supplementary Fig. 2a, b and Supplementary Table 1).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T08:32:33.964Z"}},{"start":303,"end":387,"reference_id":"35013194","reference_source":"pmid","reference_html":"The catalytic activity of TCPTP is auto-regulated by its intrinsically disordered tail and activated by Integrin alpha-1. <i> Singh JP, Li Y, Chen YY, Hsu SD, Page R, Peti W, Meng TC. </i> Nat Commun, 2022","date":"2022-06-02T07:34:48.386Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000059","term_name":"self-inhibition","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03707r003","statement":[{"text":"For both substrate peptides, the rate of dephosphorylation by TCPTP was ~3-fold slower than that measured for TCPTPCAT (Fig. 2a and Supplementary Fig. 3a). Michaelis-Menten analysis revealed that the C-terminal tail of TCPTP affects both the kcat and KM (Table 1 and Supplementary Table 2). These data are consistent with an autoinhibitory function of the TCPTP C-terminal tail and suggest that the change in activity is not achieved by completely blocking the TCPTP active site, but instead via a yet unknown mechanism.","type":"Results"},{"text":"An in trans interaction of the IDR C-terminal tail of TCPTP leads to a dose-dependent inhibition of the TCPTP catalytic activity29.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T08:33:15.336Z"}},{"start":344,"end":385,"reference_id":"35013194","reference_source":"pmid","reference_html":"The catalytic activity of TCPTP is auto-regulated by its intrinsically disordered tail and activated by Integrin alpha-1. <i> Singh JP, Li Y, Chen YY, Hsu SD, Page R, Peti W, Meng TC. </i> Nat Commun, 2022","date":"2022-06-02T07:07:16.374Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"annotation_extensions":[],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P17706-2","operator":null,"partner_start":1,"partner_end":302}],"region_id":"DP03707r004","statement":[{"text":"An in trans interaction of the IDR C-terminal tail of TCPTP leads to a dose-dependent inhibition of the TCPTP catalytic activity29. Thus, we tested if the TCPTPTail peptide interacts directly, in trans, with TCPTPCAT. The addition of increasing amounts of TCPTPCAT (1:0 to 1:20, TCPTPTAIL: TCPTPCAT) resulted in reduced intensities of multiple peaks, corresponding to residues 344–385, in the 2D [1H,15N] HSQC spectrum of TCPTPTail (Supplementary Fig. 4).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T08:33:17.218Z"}},{"start":344,"end":385,"reference_id":"35013194","reference_source":"pmid","reference_html":"The catalytic activity of TCPTP is auto-regulated by its intrinsically disordered tail and activated by Integrin alpha-1. <i> Singh JP, Li Y, Chen YY, Hsu SD, Page R, Peti W, Meng TC. </i> Nat Commun, 2022","date":"2022-06-02T07:32:30.718Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001170","ec_ontology":"ECO","ec_name":"cross-linking evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"annotation_extensions":[],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P17706-2","operator":null,"partner_start":1,"partner_end":302}],"region_id":"DP03707r005","statement":[{"text":"Finally, the lysine residues in the C-terminal tail observed to be cross-linked most frequently to lysines in TCPTPCAT correspond to K358, K364 and K369, i.e., the same residues determined to bind TCPTPCAT using NMR spectroscopy (residues 344–385). Together, the cross-linking and NMR-based interaction studies show that TCPTP dynamic C-terminal IDR residues 344–385 interact directly with the TCPTPCAT domain.","type":"Results"},{"text":"As a final control, we repeated the cross-linking experiment between the autoinhibitory and catalytic domains in trans using the individual TCPTPCAT and TCPTPTail domains, i.e. in an experimental manner identical to that used for the NMR experiments. As expected, the results were fully consistent with both the NMR spectroscopy and the in cis cross-linking data. Namely, as observed for full-length TCPTP, TCPTPCAT residues K38, K107, and K118 were again cross-linked to multiple lysines in the TCPTPTail peptides, with the greatest number of cross-links observed for TCPTPTail residues K358, K364, and K369 (cross-links were also observed for K290 and K294, but this is likely due to the increased accessibility of these residues in the free IDP [TCPTPTail] versus the same residues within the context of the full-length protein) (Supplementary Fig. 5a, b and Supplementary Table 4).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T08:33:22.793Z"}}],"regions_counter":5,"released":"2023_12","sequence":"MPTTIEREFEELDTQRRWQPLYLEIRNESHDYPHRVAKFPENRNRNRYRDVSPYDHSRVKLQNAENDYINASLVDIEEAQRSYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKESVKCAQYWPTDDQEMLFKETGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLNPDHGPAVIHCSAGIGRSGTFSLVDTCLVLMEKGDDINIKQVLLNMRKYRMGLIQTPDQLRFSYMAIIEGAKCIKGDSSIQKRWKELSKEDLSPAFDHSPNKIMTEKYNGNRIGLEEEKLTGDRCTGLSSKMQDTMEENSESALRKRIREDRKATTAQKVQQMKQRLNENERKRKRPRLTDT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"PTPN2"},"synonyms":[{"value":"PTPT"}]}],"disorder_content":0.21963824289405684,"disprot_consensus":{"full":[{"start":303,"end":387,"type":"D"}],"Structural state":[{"start":303,"end":387,"type":"D"}],"Disorder function":[{"start":303,"end":387,"type":"F"}],"Molecular function":[{"start":344,"end":385,"type":"F"}]}},{"disprot_id":"DP03709","acc":"O96018","creator":"rpancsa","date":"2022-06-02T11:28:08.048Z","features":{"pfam":[{"id":"PF00595","name":"PDZ domain","start":394,"end":477},{"id":"PF00595","name":"PDZ domain","start":493,"end":557},{"id":"PF00640","name":"Phosphotyrosine interaction domain (PTB/PID)","start":221,"end":358}],"gene3D":[]},"length":575,"name":"Amyloid-beta A4 precursor protein-binding family A member 3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":214,"reference_id":"34655613","reference_source":"pmid","reference_html":"Structural and thermodynamical insights into the binding and inhibition of FIH-1 by the N-terminal disordered region of Mint3. <i> Ten T, Nagatoishi S, Maeda R, Hoshino M, Nakayama Y, Seiki M, Sakamoto T, Tsumoto K. </i> J Biol Chem, 2021","date":"2022-06-02T11:30:28.560Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03709r001","statement":[{"text":"Circular dichroism (CD) experiments were performed to measure the composition of the secondary structure of Mint3NT. Consequently, a negative peak at 200 nm, which is the hallmark of the random coil, was observed, and significant peaks that originate in secondary structures, especially α-helices and β-sheets, could not be observed (Fig. 1B). The result is suggesting that the isolated N-terminus of Mint3 is mostly composed of a random coil (10).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T08:45:22.198Z"}},{"start":1,"end":214,"reference_id":"34655613","reference_source":"pmid","reference_html":"Structural and thermodynamical insights into the binding and inhibition of FIH-1 by the N-terminal disordered region of Mint3. <i> Ten T, Nagatoishi S, Maeda R, Hoshino M, Nakayama Y, Seiki M, Sakamoto T, Tsumoto K. </i> J Biol Chem, 2021","date":"2022-06-02T11:31:20.333Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006232","ec_ontology":"ECO","ec_name":"differential scanning calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03709r002","statement":[{"text":"Following that, differential scanning calorimetry (DSC) was performed to analyze the protein folding of Mint3NT. No significant peak caused by the collapse of the higher-order structure was observed in the thermal denaturation experiment (Fig. S1).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T08:45:27.189Z"}},{"start":1,"end":214,"reference_id":"34655613","reference_source":"pmid","reference_html":"Structural and thermodynamical insights into the binding and inhibition of FIH-1 by the N-terminal disordered region of Mint3. <i> Ten T, Nagatoishi S, Maeda R, Hoshino M, Nakayama Y, Seiki M, Sakamoto T, Tsumoto K. </i> J Biol Chem, 2021","date":"2022-06-02T11:34:40.147Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03709r003","statement":[{"text":"We measured the 1H-15N HSQC spectrum of Mint3NT and found that the dispersion of resonance peaks was very poor particularly along the 1H-axis, suggesting the absence of strong hydrogen-bonding interactions (Fig. 1D). Furthermore, the superposition of two HSQC spectra separately recorded for the fragment proteins of Mint3NT (Mint3(1–117) and Mint3(101–214)), Figure 1E reproduced the spectrum of whole protein (Mint3NT) very well, suggesting the absence of significant interaction between the N- and C-terminal regions of Mint3NT.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T08:45:25.964Z"}},{"start":1,"end":214,"reference_id":"34655613","reference_source":"pmid","reference_html":"Structural and thermodynamical insights into the binding and inhibition of FIH-1 by the N-terminal disordered region of Mint3. <i> Ten T, Nagatoishi S, Maeda R, Hoshino M, Nakayama Y, Seiki M, Sakamoto T, Tsumoto K. </i> J Biol Chem, 2021","date":"2022-06-02T11:37:05.914Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03709r004","statement":[{"text":"To determine the structural molecular details of the N-terminal regions of Mint3, hydrogen/deuterium exchange–mass spectrometry (HDX-MS) and nuclear magnetic resonance (NMR) spectroscopy were conducted. In the HDX-MS analysis, the exchange events are mediated by the conformational fluctuation of the protein. The exchange rate of amide hydrogen is influenced by the formation of a hydrogen bond, pH, and to a minor degree the temperature (11, 12). In this experiment, the deuteration processes were performed under the condition that the pH and the temperature are well controlled, so that we can focus on the influence of the formation of a hydrogen bond. Therefore, the amide hydrogen of an extended/flexible region will be replaced by solvent deuterium at a higher rate, as compared with that of a folded/rigid region. In fact, the exchange rates of the whole Mint3NT were observed as an immediate saturation in the deuteration level, suggesting an intrinsically disordered state in solution (Figs. 1C and S2A, Table S1A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-07T08:45:29.789Z"}}],"regions_counter":10,"released":"2023_12","sequence":"MDFPTISRSPSGPPAMDLEGPRDILVPSEDLTPDSQWDPMPGGPGSLSRMELDESSLQELVQQFEALPGDLVGPSPGGAPCPLHIATGHGLASQEIADAHGLLSAEAGRDDLLGLLHCEECPPSQTGPEEPLEPAPRLLQPPEDPDEDSDSPEWVEGASAEQEGSRSSSSSPEPWLETVPLVTPEEPPAGAQSPETLASYPAPQEVPGPCDHEDLLDGVIFGARYLGSTQLVSERNPPTSTRMAQAREAMDRVKAPDGETQPMTEVDLFVSTKRIKVLTADSQEAMMDHALHTISYTADIGCVLVLMARRRLARRPAPQDHGRRLYKMLCHVFYAEDAQLIAQAIGQAFAAAYSQFLRESGIDPSQVGVHPSPGACHLHNGDLDHFSNSDNCREVHLEKRRGEGLGVALVESGWGSLLPTAVIANLLHGGPAERSGALSIGDRLTAINGTSLVGLPLAACQAAVRETKSQTSVTLSIVHCPPVTTAIIHRPHAREQLGFCVEDGIICSLLRGGIAERGGIRVGHRIIEINGQSVVATPHARIIELLTEAYGEVHIKTMPAATYRLLTGQEQPVYL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"APBA3"},"synonyms":[{"value":"MINT3"},{"value":"X11L2"}]}],"alphafold_very_low_content":0.391304347826087,"disorder_content":0.37217391304347824,"disprot_consensus":{"full":[{"start":1,"end":214,"type":"D"}],"Structural state":[{"start":1,"end":214,"type":"D"}]}},{"disprot_id":"DP03710","acc":"Q8NEB9","creator":"jnilsson","date":"2022-06-02T13:29:16.985Z","features":{"pfam":[{"id":"PF00454","name":"Phosphatidylinositol 3- and 4-kinase","start":631,"end":831},{"id":"PF00613","name":"Phosphoinositide 3-kinase family, accessory domain (PIK domain)","start":285,"end":521},{"id":"PF00792","name":"Phosphoinositide 3-kinase C2","start":54,"end":198}],"gene3D":[]},"length":887,"name":"Phosphatidylinositol 3-kinase catalytic subunit type 3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":422,"end":469,"reference_id":"33692360","reference_source":"pmid","reference_html":"Structural basis for VPS34 kinase activation by Rab1 and Rab5 on membranes. <i> Tremel S, Ohashi Y, Morado DR, Bertram J, Perisic O, Brandt LTL, von Wrisberg MK, Chen ZA, Maslen SL, Kovtun O, Skehel M, Rappsilber J, Lang K, Munro S, Briggs JAG, Williams RL. </i> Nat Commun, 2021","date":"2023-04-26T12:37:09.537Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":1,"cross_refs":[{"db":"PDB","id":"7BL1"}],"region_id":"DP03710r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9P2Y5","statements":[{"type":"Curator statement","text":"human complex II-BATS bound to membrane-attached Rab5a-GTP"}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q99570","statements":[{"type":"Curator statement","text":"human complex II-BATS bound to membrane-attached Rab5a-GTP"}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q14457","statements":[{"type":"Curator statement","text":"human complex II-BATS bound to membrane-attached Rab5a-GTP"}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P20339"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15996","statements":[{"type":"Curator statement","text":"human complex II-BATS bound to membrane-attached Rab5a-GTP"}],"entry_name":"GTP"}],"statement":[{"text":"The PDB shows this region lacks electron density indicating it is disordered","type":"Curator statement"}],"sequence_construct":"MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGKAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTKTPGRTSSTLSEDQMSRLAKLTKAHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDGDESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNAATRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQSSVSENVSNSGINSAEIDSSQIITSPLPSVSSPPPASKTKEVPDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSENGPNGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-26T12:41:53.117Z"}},{"start":873,"end":887,"reference_id":"33692360","reference_source":"pmid","reference_html":"Structural basis for VPS34 kinase activation by Rab1 and Rab5 on membranes. <i> Tremel S, Ohashi Y, Morado DR, Bertram J, Perisic O, Brandt LTL, von Wrisberg MK, Chen ZA, Maslen SL, Kovtun O, Skehel M, Rappsilber J, Lang K, Munro S, Briggs JAG, Williams RL. </i> Nat Commun, 2021","date":"2022-06-02T15:18:59.054Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"7BL1"}],"region_id":"DP03710r002","statement":[{"text":"The PDB shows this region lacks electron density indicating it is disordered","type":"Curator statement"},{"text":"Human complex II-BATS bound to membrane-attached Rab5a-GTP","type":"Curator statement"}],"sequence_construct":"MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGKAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTKTPGRTSSTLSEDQMSRLAKLTKAHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDGDESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNAATRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQSSVSENVSNSGINSAEIDSSQIITSPLPSVSSPPPASKTKEVPDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSENGPNGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-03T18:06:36.071Z"}},{"start":246,"end":260,"reference_id":"33692360","reference_source":"pmid","reference_html":"Structural basis for VPS34 kinase activation by Rab1 and Rab5 on membranes. <i> Tremel S, Ohashi Y, Morado DR, Bertram J, Perisic O, Brandt LTL, von Wrisberg MK, Chen ZA, Maslen SL, Kovtun O, Skehel M, Rappsilber J, Lang K, Munro S, Briggs JAG, Williams RL. </i> Nat Commun, 2021","date":"2022-06-02T15:19:13.972Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"7BL1"}],"region_id":"DP03710r003","statement":[{"text":"The PDB shows this region lacks electron density indicating it is disordered","type":"Curator statement"},{"text":"Human complex II-BATS bound to membrane-attached Rab5a-GTP","type":"Curator statement"}],"sequence_construct":"MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGKAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTKTPGRTSSTLSEDQMSRLAKLTKAHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDGDESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNAATRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQSSVSENVSNSGINSAEIDSSQIITSPLPSVSSPPPASKTKEVPDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPENGPNGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK\n","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-03T18:05:49.029Z"}},{"start":418,"end":470,"reference_id":"25327288","reference_source":"pmid","reference_html":"Selective VPS34 inhibitor blocks autophagy and uncovers a role for NCOA4 in ferritin degradation and iron homeostasis in vivo. <i> Dowdle WE, Nyfeler B, Nagel J, Elling RA, Liu S, Triantafellow E, Menon S, Wang Z, Honda A, Pardee G, Cantwell J, Luu C, Cornella-Taracido I, Harrington E, Fekkes P, Lei H, Fang Q, Digan ME, Burdick D, Powers AF, Helliwell SB, D'Aquin S, Bastien J, Wang H, Wiederschain D, Kuerth J, Bergman P, Schwalb D, Thomas J, Ugwonali S, Harbinski F, Tallarico J, Wilson CJ, Myer VE, Porter JA, Bussiere DE, Finan PM, Labow MA, Mao X, Hamann LG, Manning BD, Valdez RA, Nicholson T, Schirle M, Knapp MS, Keaney EP, Murphy LO. </i> Nat Cell Biol, 2014","date":"2022-06-02T15:16:46.491Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"4PH4"}],"region_id":"DP03710r004","statement":[{"text":"The PDB shows this region lacks electron density indicating it is disordered","type":"Curator statement"},{"text":"The crystal structure of Human VPS34 in complex with PIK-III","type":"Curator statement"}],"sequence_construct":"MSYYHHHHHHDYDIPTTENLYFQGAMGSGIRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQSSVSENVSNSGINSAEIDSSQIITSPLPSVSSPPPASKTKEVPDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSENGPNGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-03T18:16:12.110Z"}},{"start":872,"end":887,"reference_id":"25327288","reference_source":"pmid","reference_html":"Selective VPS34 inhibitor blocks autophagy and uncovers a role for NCOA4 in ferritin degradation and iron homeostasis in vivo. <i> Dowdle WE, Nyfeler B, Nagel J, Elling RA, Liu S, Triantafellow E, Menon S, Wang Z, Honda A, Pardee G, Cantwell J, Luu C, Cornella-Taracido I, Harrington E, Fekkes P, Lei H, Fang Q, Digan ME, Burdick D, Powers AF, Helliwell SB, D'Aquin S, Bastien J, Wang H, Wiederschain D, Kuerth J, Bergman P, Schwalb D, Thomas J, Ugwonali S, Harbinski F, Tallarico J, Wilson CJ, Myer VE, Porter JA, Bussiere DE, Finan PM, Labow MA, Mao X, Hamann LG, Manning BD, Valdez RA, Nicholson T, Schirle M, Knapp MS, Keaney EP, Murphy LO. </i> Nat Cell Biol, 2014","date":"2022-06-02T15:17:04.920Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"4PH4"}],"region_id":"DP03710r005","statement":[{"text":"The PDB shows this region lacks electron density indicating it is disordered","type":"Curator statement"},{"text":"The crystal structure of Human VPS34 in complex with PIK-III","type":"Curator statement"}],"sequence_construct":"MSYYHHHHHHDYDIPTTENLYFQGAMGSGIRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQSSVSENVSNSGINSAEIDSSQIITSPLPSVSSPPPASKTKEVPDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSENGPNGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-03T18:02:34.842Z"}},{"start":418,"end":434,"reference_id":"25326666","reference_source":"pmid","reference_html":"A highly potent and selective Vps34 inhibitor alters vesicle trafficking and autophagy. <i> Ronan B, Flamand O, Vescovi L, Dureuil C, Durand L, Fassy F, Bachelot MF, Lamberton A, Mathieu M, Bertrand T, Marquette JP, El-Ahmad Y, Filoche-Romme B, Schio L, Garcia-Echeverria C, Goulaouic H, Pasquier B. </i> Nat Chem Biol, 2014","date":"2022-06-02T15:15:24.350Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"4OYS"}],"region_id":"DP03710r006","statement":[{"text":"The PDB shows this region lacks electron density indicating it is disordered.","type":"Curator statement"},{"text":"CRYSTAL STRUCTURE OF VPS34 IN COMPLEX WITH SAR405.","type":"Curator statement"}],"sequence_construct":"GAMSDHDLKPNAATRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQSSVSENVSNSGINSAEIDSSQIITSPLPSVSSPPPASKTKEVPDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSENGPNGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIH","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-03T17:56:15.889Z"}},{"start":452,"end":469,"reference_id":"25326666","reference_source":"pmid","reference_html":"A highly potent and selective Vps34 inhibitor alters vesicle trafficking and autophagy. <i> Ronan B, Flamand O, Vescovi L, Dureuil C, Durand L, Fassy F, Bachelot MF, Lamberton A, Mathieu M, Bertrand T, Marquette JP, El-Ahmad Y, Filoche-Romme B, Schio L, Garcia-Echeverria C, Goulaouic H, Pasquier B. </i> Nat Chem Biol, 2014","date":"2022-06-02T15:15:05.854Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"4OYS"}],"region_id":"DP03710r007","statement":[{"text":"The PDB shows this region lacks electron density indicating it is disordered.","type":"Curator statement"},{"text":"CRYSTAL STRUCTURE OF VPS34 IN COMPLEX WITH SAR405.","type":"Curator statement"}],"sequence_construct":"GAMSDHDLKPNAATRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQSSVSENVSNSGINSAEIDSSQIITSPLPSVSSPPPASKTKEVPDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSENGPNGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIH","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-03T17:56:25.279Z"}},{"start":250,"end":253,"reference_id":"30767700","reference_source":"pmid","reference_html":"Members of the autophagy class III phosphatidylinositol 3-kinase complex I interact with GABARAP and GABARAPL1 via LIR motifs. <i> Birgisdottir ÅB, Mouilleron S, Bhujabal Z, Wirth M, Sjøttem E, Evjen G, Zhang W, Lee R, O'Reilly N, Tooze SA, Lamark T, Johansen T. </i> Autophagy, 2019","date":"2022-07-11T16:17:29.929Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe250Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val253Ala","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP03710r008","statement":[{"text":"For PIK3C3, point mutations of both the aromatic residue and the conserved hydrophobic position (F250A, V253A) of the core LIR-F250 motif (FELV, amino acids 250–253) appeared to significantly reduce binding to the Atg8 homologs.","type":"Results"},{"text":"Region corresponding to the LIR motif \"FELV\" at position 250-253","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-26T12:41:19.952Z"}},{"start":250,"end":253,"reference_id":"30767700","reference_source":"pmid","reference_html":"Members of the autophagy class III phosphatidylinositol 3-kinase complex I interact with GABARAP and GABARAPL1 via LIR motifs. <i> Birgisdottir ÅB, Mouilleron S, Bhujabal Z, Wirth M, Sjøttem E, Evjen G, Zhang W, Lee R, O'Reilly N, Tooze SA, Lamark T, Johansen T. </i> Autophagy, 2019","date":"2022-07-13T08:31:53.694Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe250Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val253Ala","start":null,"end":null,"position":null}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9H492","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9GZQ8","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9BXW4","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"O95166","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9H0R8","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P60520","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP03710r009","statement":[{"text":"Here, the different Atg8 homologs were expressed as GST fusions in E. coli and then tested for interaction with in vitro translated PIK3C3, BECN1 and ATG14, respectively. All the members of PtdIns3K-C1, except PIK3R4, were able to interact with the Atg8 homologs (Figure 2). PIK3C3 and ATG14 showed significant interaction with LC3C and GABARAPL2, but the strongest interaction was seen with GABARAP and GABARAPL1. BECN1 only bound with significant affinity to GABARAP and GABARAPL1. Taken together, PIK3C3, BECN1 and ATG14 all interacted with the Atg8 homologs and appear to have a preference for binding to the GABARAP and GABARAPL1. For PIK3C3, point mutations of both the aromatic residue and the conserved hydrophobic position (F250A, V253A) of the core LIR-F250 motif (FELV, amino acids 250–253) appeared to significantly reduce binding to the Atg8 homologs. In contrast, mutating the core LIR-F198 motif (FREI, amino acids 198–201) in a similar manner (F198A, V201A) did not affect binding of PIK3C3 (Figure 2). This indicates that LIR-F250 of PIK3C3 is the functional LIR motif.","type":"Results"},{"text":"Region corresponding to the LIR motif \"FELV\" at position 250-253","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-26T12:41:20.197Z"}},{"start":250,"end":253,"reference_id":"30767700","reference_source":"pmid","reference_html":"Members of the autophagy class III phosphatidylinositol 3-kinase complex I interact with GABARAP and GABARAPL1 via LIR motifs. <i> Birgisdottir ÅB, Mouilleron S, Bhujabal Z, Wirth M, Sjøttem E, Evjen G, Zhang W, Lee R, O'Reilly N, Tooze SA, Lamark T, Johansen T. </i> Autophagy, 2019","date":"2022-07-13T08:33:26.485Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0061912","term_name":"selective autophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe250Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val253Ala","start":null,"end":null,"position":null}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9H492","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9GZQ8","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9BXW4","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"O95166","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9H0R8","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P60520","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP03710r010","statement":[{"text":"Here, the different Atg8 homologs were expressed as GST fusions in E. coli and then tested for interaction with in vitro translated PIK3C3, BECN1 and ATG14, respectively. All the members of PtdIns3K-C1, except PIK3R4, were able to interact with the Atg8 homologs (Figure 2). PIK3C3 and ATG14 showed significant interaction with LC3C and GABARAPL2, but the strongest interaction was seen with GABARAP and GABARAPL1. BECN1 only bound with significant affinity to GABARAP and GABARAPL1. Taken together, PIK3C3, BECN1 and ATG14 all interacted with the Atg8 homologs and appear to have a preference for binding to the GABARAP and GABARAPL1. For PIK3C3, point mutations of both the aromatic residue and the conserved hydrophobic position (F250A, V253A) of the core LIR-F250 motif (FELV, amino acids 250–253) appeared to significantly reduce binding to the Atg8 homologs. In contrast, mutating the core LIR-F198 motif (FREI, amino acids 198–201) in a similar manner (F198A, V201A) did not affect binding of PIK3C3 (Figure 2). This indicates that LIR-F250 of PIK3C3 is the functional LIR motif.","type":"Results"},{"text":"Region corresponding to the LIR motif \"FELV\" at position 250-253","type":"Curator statement"}],"term_comment":"","term_def":"\"The macroautophagy process in which specific structures are targeted by the autophagy process.\" [PMID:20484971, PMID:21997368, PMID:22966490]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-26T12:41:23.415Z"}}],"regions_counter":10,"released":"2022_06","sequence":"MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGKAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTKTPGRTSSTLSEDQMSRLAKLTKAHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDGDESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNAATRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQSSVSENVSNSGINSAEIDSSQIITSPLPSVSSPPPASKTKEVPDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSENGPNGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"PIK3C3","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:8974","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8974"}}]},"synonyms":[{"value":"VPS34","evidences":[{"code":"ECO:0000305"}]}]}],"alphafold_very_low_content":0.0834272829763247,"disorder_content":0.09470124013528748,"disprot_consensus":{"full":[{"start":246,"end":260,"type":"D"},{"start":418,"end":470,"type":"D"},{"start":872,"end":887,"type":"D"}],"Structural state":[{"start":246,"end":260,"type":"D"},{"start":418,"end":470,"type":"D"},{"start":872,"end":887,"type":"D"}],"Biological process":[{"start":250,"end":253,"type":"F"}],"Molecular function":[{"start":250,"end":253,"type":"F"}]}},{"disprot_id":"DP03711","acc":"Q9BXW4","creator":"vnugnes","date":"2022-06-02T15:09:45.098Z","features":{"pfam":[{"id":"PF02991","name":"Autophagy protein Atg8 ubiquitin like","start":22,"end":126}],"gene3D":[]},"length":147,"name":"Microtubule-associated proteins 1A/1B light chain 3C","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":12,"reference_id":"23022382","reference_source":"pmid","reference_html":"LC3C, bound selectively by a noncanonical LIR motif in NDP52, is required for antibacterial autophagy. <i> von Muhlinen N, Akutsu M, Ravenhill BJ, Foeglein Á, Bloor S, Rutherford TJ, Freund SM, Komander D, Randow F. </i> Mol Cell, 2012","date":"2022-06-02T15:11:55.308Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"3VVW"}],"region_id":"DP03711r001","statement":[{"text":"The N-terminal α1 helix of LC3C is disordered in our structure; it is possible that this helix is stabilized by acidic residues upstream of canonical LIRs (Noda et al., 2010).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T10:48:08.629Z"}}],"regions_counter":1,"released":"2022_06","sequence":"MPPPQKIPSVRPFKQRKSLAIRQEEVAGIRAKFPNKIPVVVERYPRETFLPPLDKTKFLVPQELTMTQFLSIIRSRMVLRATEAFYLLVNNKSLVSMSATMAEIYRDYKDEDGFVYMTYASQETFGCLESAAPRDGSSLEDRPCNPL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"MAP1LC3C"}}],"alphafold_very_low_content":0.10884353741496598,"disorder_content":0.08163265306122448,"disprot_consensus":{"full":[{"start":1,"end":12,"type":"D"}],"Structural state":[{"start":1,"end":12,"type":"D"}]}},{"disprot_id":"DP03712","acc":"Q99623","creator":"vnugnes","date":"2022-06-02T20:04:11.112Z","features":{"pfam":[{"id":"PF01145","name":"SPFH domain / Band 7 family","start":42,"end":220}],"gene3D":[]},"length":299,"name":"Prohibitin-2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":246,"end":265,"reference_id":"31522117","reference_source":"pmid","reference_html":"Structural Basis of Mitochondrial Scaffolds by Prohibitin Complexes: Insight into a Role of the Coiled-Coil Region. <i> Yoshinaka T, Kosako H, Yoshizumi T, Furukawa R, Hirano Y, Kuge O, Tamada T, Koshiba T. </i> iScience, 2019","date":"2022-06-02T20:11:29.451Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"6IQE"}],"region_id":"DP03712r001","statement":[{"text":"Tha lack of electron density in this region, as shown in the PDB, indicates disorder.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:17:53.398Z"}}],"regions_counter":1,"released":"2022_06","sequence":"MAQNLKDLAGRLPAGPRGMGTALKLLLGAGAVAYGVRESVFTVEGGHRAIFFNRIGGVQQDTILAEGLHFRIPWFQYPIIYDIRARPRKISSPTGSKDLQMVNISLRVLSRPNAQELPSMYQRLGLDYEERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVEAKQVAQQEAQRAQFLVEKAKQEQRQKIVQAEGEAEAAKMLGEALSKNPGYIKLRKIRAAQNISKTIATSQNRIYLTADNLVLNLQDESFTRGSDSLIKGKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"PHB2","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAH14766.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAH14766.1"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:30306","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:30306"}}]},"synonyms":[{"value":"BAP","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAB51324.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAB51324.1"}}]},{"value":"REA","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAD38042.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD38042.1"}}]}]}],"alphafold_very_low_content":0.023411371237458192,"disorder_content":0.06688963210702341,"disprot_consensus":{"full":[{"start":246,"end":265,"type":"D"}],"Structural state":[{"start":246,"end":265,"type":"D"}]}},{"disprot_id":"DP03713","acc":"Q9H0E2","creator":"vnugnes","date":"2022-06-02T20:20:31.329Z","features":{"pfam":[{"id":"PF00168","name":"C2 domain","start":53,"end":154},{"id":"PF02845","name":"CUE domain","start":231,"end":270}],"gene3D":[]},"length":274,"name":"Toll-interacting protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":53,"reference_id":"26320582","reference_source":"pmid","reference_html":"Tom1 Modulates Binding of Tollip to Phosphatidylinositol 3-Phosphate via a Coupled Folding and Binding Mechanism. <i> Xiao S, Brannon MK, Zhao X, Fread KI, Ellena JF, Bushweller JH, Finkielstein CV, Armstrong GS, Capelluto DGS. </i> Structure, 2015","date":"2022-06-06T12:41:03.257Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"BMRB","id":"26573"},{"db":"PDB","id":"2N31"},{"db":"BMRB","id":"25632"}],"region_id":"DP03713r001","sequence_construct":"GPLGSMATTVSTQRGPVYIGELPQDFLRITPTQQQRQVQLDAQAAQQLQYGGAVGTVG","statement":[{"text":"The 1H-15N heteronuclear single-quantum coherence (HSQC) spectrum of Tollip TBD was characteristic of an unstructured protein as indicated by the narrow dispersion in the 1HN dimension (Figure 1B).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T12:41:46.545Z"}},{"start":1,"end":53,"reference_id":"26320582","reference_source":"pmid","reference_html":"Tom1 Modulates Binding of Tollip to Phosphatidylinositol 3-Phosphate via a Coupled Folding and Binding Mechanism. <i> Xiao S, Brannon MK, Zhao X, Fread KI, Ellena JF, Bushweller JH, Finkielstein CV, Armstrong GS, Capelluto DGS. </i> Structure, 2015","date":"2022-06-02T20:36:54.649Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03713r002","sequence_construct":"GPLGSMATTVSTQRGPVYIGELPQDFLRITPTQQQRQVQLDAQAAQQLQYGGAVGTVG","statement":[{"text":"Likewise, the far-UV circular dichroism (CD) spectrum of Tollip TBD displayed a minimum at 200 nm, a feature of unstructured protein spectra (Figure 1B, inset).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:11:49.551Z"}},{"start":1,"end":53,"reference_id":"26320582","reference_source":"pmid","reference_html":"Tom1 Modulates Binding of Tollip to Phosphatidylinositol 3-Phosphate via a Coupled Folding and Binding Mechanism. <i> Xiao S, Brannon MK, Zhao X, Fread KI, Ellena JF, Bushweller JH, Finkielstein CV, Armstrong GS, Capelluto DGS. </i> Structure, 2015","date":"2022-06-02T20:37:07.472Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"O60784","operator":null,"partner_start":215,"partner_end":309}],"region_id":"DP03713r003","sequence_construct":"GPLGSMATTVSTQRGPVYIGELPQDFLRITPTQQQRQVQLDAQAAQQLQYGGAVGTVG","statement":[{"text":"Titration of the unlabeled Tom1 GAT domain into the 15N-labeled Tollip TBD resulted in dramatic improvement in resonance dispersion (Figure 1C). Resonance perturbations clustered in the first half of Tollip TBD including two N-terminal β strands. The largest chemical-shift perturbations were observed in residues Arg9, Val12, Ile14, Asp20, and Arg23 (Figure 1D). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:15:29.370Z"}},{"start":23,"end":53,"reference_id":"26320582","reference_source":"pmid","reference_html":"Tom1 Modulates Binding of Tollip to Phosphatidylinositol 3-Phosphate via a Coupled Folding and Binding Mechanism. <i> Xiao S, Brannon MK, Zhao X, Fread KI, Ellena JF, Bushweller JH, Finkielstein CV, Armstrong GS, Capelluto DGS. </i> Structure, 2015","date":"2022-06-02T20:37:44.062Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03713r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60784"}],"sequence_construct":"GPLGSMATTVSTQRGPVYIGELPQDFLRITPTQQQRQVQLDAQAAQQLQYGGAVGTVG","statement":[{"text":"We therefore measured the internal backbone motions of Tom1 GAT-bound Tollip TBD by analysis of the 1H-15N heteronuclear NOEs and the 15N relaxation times. The 1H-15N NOE profile showed that the first 22 residues of Tollip TBD were highly ordered, whereas the C-terminal half of the protein was disordered (Figure S2A).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:11:44.619Z"}},{"start":1,"end":22,"reference_id":"26320582","reference_source":"pmid","reference_html":"Tom1 Modulates Binding of Tollip to Phosphatidylinositol 3-Phosphate via a Coupled Folding and Binding Mechanism. <i> Xiao S, Brannon MK, Zhao X, Fread KI, Ellena JF, Bushweller JH, Finkielstein CV, Armstrong GS, Capelluto DGS. </i> Structure, 2015","date":"2022-06-02T20:37:56.633Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03713r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60784"}],"sequence_construct":"GPLGSMATTVSTQRGPVYIGELPQDFLRITPTQQQRQVQLDAQAAQQLQYGGAVGTVG","statement":[{"text":"We therefore measured the internal backbone motions of Tom1 GAT-bound Tollip TBD by analysis of the 1H-15N heteronuclear NOEs and the 15N relaxation times. The 1H-15N NOE profile showed that the first 22 residues of Tollip TBD were highly ordered, whereas the C-terminal half of the protein was disordered (Figure S2A).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:11:30.052Z"}},{"start":1,"end":22,"reference_id":"26320582","reference_source":"pmid","reference_html":"Tom1 Modulates Binding of Tollip to Phosphatidylinositol 3-Phosphate via a Coupled Folding and Binding Mechanism. <i> Xiao S, Brannon MK, Zhao X, Fread KI, Ellena JF, Bushweller JH, Finkielstein CV, Armstrong GS, Capelluto DGS. </i> Structure, 2015","date":"2022-06-02T20:41:37.635Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03713r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60784"}],"sequence_construct":"GPLGSMATTVSTQRGPVYIGELPQDFLRITPTQQQRQVQLDAQAAQQLQYGGAVGTVG","statement":[{"text":"Together, these data suggest that the conserved N-terminal Tollip TBD becomes ordered upon Tom1 GAT binding, whereas its C-terminal region remains relatively disordered.","type":"Results"},{"text":"Tollip TBD Is Intrinsically Disordered and Partially Folds upon Binding to the Tom1 GAT Domain.","type":"Results"}],"states_connection":[{"source":"DP03713r001","target":"DP03713r005"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:14:52.229Z"}},{"start":1,"end":53,"reference_id":"26320582","reference_source":"pmid","reference_html":"Tom1 Modulates Binding of Tollip to Phosphatidylinositol 3-Phosphate via a Coupled Folding and Binding Mechanism. <i> Xiao S, Brannon MK, Zhao X, Fread KI, Ellena JF, Bushweller JH, Finkielstein CV, Armstrong GS, Capelluto DGS. </i> Structure, 2015","date":"2022-06-02T20:47:38.116Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"O60784","operator":null,"partner_start":215,"partner_end":309}],"region_id":"DP03713r007","sequence_construct":"GPLGSMATTVSTQRGPVYIGELPQDFLRITPTQQQRQVQLDAQAAQQLQYGGAVGTVG","statement":[{"text":"Tollip TBD bound immobilized Tom1 GAT with high association and low dissociation rates, and with an estimated dissociation constant (KD) of 0.67 nM (Table 2 and Figure S4A).","type":"Results"},{"text":"Alanine mutations in Tollip TBD Arg9/Val12 and Asp20/Arg23 reduced Tom1 GAT binding (Table 2 and Figures S4K–S4L). Notably, mutation in Phe21, a conserved residue in Tollip (Figure S1A) that forms several intermolecular NOEs, and its NH backbone resonance is shifted when bound to the Tom1 GAT domain, reducing binding affinity by ∼20,000-fold (Table 2 and Figure S4M). Consequently, the affinity of Tom1 GAT N230A for Tollip TBD F21A showed ∼60,000-fold reduction in the equilibrium constant Kb (data not shown) leading to ∼95,000-fold reduction in binding (Table 2 and Figure S4N), suggesting that these residues reduce the affinity in the initial binding event, and consequently are critical for Tom1-Tollip complex formation.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:15:22.747Z"}}],"regions_counter":7,"released":"2022_06","sequence":"MATTVSTQRGPVYIGELPQDFLRITPTQQQRQVQLDAQAAQQLQYGGAVGTVGRLNITVVQAKLAKNYGMTRMDPYCRLRLGYAVYETPTAHNGAKNPRWNKVIHCTVPPGVDSFYLEIFDERAFSMDDRIAWTHITIPESLRQGKVEDKWYSLSGRQGDDKEGMINLVMSYALLPAAMVMPPQPVVLMPTVYQQGVGYVPITGMPAVCSPGMVPVALPPAAVNAQPRCSEEDLKAIQDMFPNMDQEVIRSVLEAQRGNKDAAINSLLQMGEEP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"TOLLIP"}}],"alphafold_very_low_content":0.12043795620437957,"disorder_content":0.19343065693430658,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"T"},{"start":23,"end":53,"type":"D"}],"Structural state":[{"start":1,"end":53,"type":"D"}],"Molecular function":[{"start":1,"end":53,"type":"F"}],"Structural transition":[{"start":1,"end":22,"type":"T"}]}},{"disprot_id":"DP03714","acc":"Q12142","creator":"vnugnes","date":"2022-06-03T13:53:06.024Z","features":{"pfam":[{"id":"PF04109","name":"Autophagy protein ATG9","start":295,"end":776}],"gene3D":[]},"length":997,"name":"Autophagy-related protein 9","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":285,"reference_id":"35007534","reference_source":"pmid","reference_html":"Mechanism of Atg9 recruitment by Atg11 in the cytoplasm-to-vacuole targeting pathway. <i> Coudevylle N, Banaś B, Baumann V, Schuschnig M, Zawadzka-Kazimierczuk A, Koźmiński W, Martens S. </i> J Biol Chem, 2022","date":"2022-06-03T14:19:44.306Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"BMRB","id":"51011"}],"region_id":"DP03714r001","statement":[{"text":"Using isotopically labeled samples and 1H-15N HSQC NMR, we concluded that, as predicted, the Atg9 NTD (residues 1–285) is largely disordered in solution (Fig. 1C).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:21:24.362Z"}},{"start":158,"end":171,"reference_id":"35007534","reference_source":"pmid","reference_html":"Mechanism of Atg9 recruitment by Atg11 in the cytoplasm-to-vacuole targeting pathway. <i> Coudevylle N, Banaś B, Baumann V, Schuschnig M, Zawadzka-Kazimierczuk A, Koźmiński W, Martens S. </i> J Biol Chem, 2022","date":"2022-06-03T14:45:48.297Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"Q12527","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03714r002","statement":[{"text":"As expected, we observed a robust recruitment of Atg9-NTD(1–255) to the beads coated with EGFP-Atg11 (Fig. 3, A and B). Mutation of the first PLF motif (M1) severely reduced the interaction, and mutation of the second PLF motif (M2) reduced the recruitment of the Atg9-NTD to the EGFP-Atg11-coated beads (Fig. 3, A and B) to a similar extent. Upon mutation of both motifs (M1+M2), the interaction between the Atg9-NTD and Atg11 became undetectable (Fig. 3, A and B).","type":"Results"},{"text":"M1 motiff is comprised of the 158-171 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:23:43.266Z"}},{"start":158,"end":171,"reference_id":"35007534","reference_source":"pmid","reference_html":"Mechanism of Atg9 recruitment by Atg11 in the cytoplasm-to-vacuole targeting pathway. <i> Coudevylle N, Banaś B, Baumann V, Schuschnig M, Zawadzka-Kazimierczuk A, Koźmiński W, Martens S. </i> J Biol Chem, 2022","date":"2022-06-03T14:46:15.079Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q12527","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03714r003","statement":[{"text":"Titration of the wild-type Atg9-NTD(1–255) into full-length Atg11 yielded a robust signal, fitting of which resulted in a KD of around 1 μM and a stoichiometry of 1 (KD = 1,086 ± 0,006 μM, n = 0,931 ± 0,004, Fig. S4). The affinity of the Atg9-NTD(1–255) M1 and M2 mutants for Atg11 was too low to be measured accurately by ITC.","type":"Results"},{"text":"M1 motiff is comprised of the 158-171 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:22:27.019Z"}},{"start":183,"end":196,"reference_id":"35007534","reference_source":"pmid","reference_html":"Mechanism of Atg9 recruitment by Atg11 in the cytoplasm-to-vacuole targeting pathway. <i> Coudevylle N, Banaś B, Baumann V, Schuschnig M, Zawadzka-Kazimierczuk A, Koźmiński W, Martens S. </i> J Biol Chem, 2022","date":"2022-06-03T14:44:47.377Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q12527","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03714r004","statement":[{"text":"Titration of the wild-type Atg9-NTD(1–255) into full-length Atg11 yielded a robust signal, fitting of which resulted in a KD of around 1 μM and a stoichiometry of 1 (KD = 1,086 ± 0,006 μM, n = 0,931 ± 0,004, Fig. S4). The affinity of the Atg9-NTD(1–255) M1 and M2 mutants for Atg11 was too low to be measured accurately by ITC.","type":"Results"},{"text":"M2 motiff is comprised of the 183-196 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:22:19.049Z"}},{"start":183,"end":196,"reference_id":"35007534","reference_source":"pmid","reference_html":"Mechanism of Atg9 recruitment by Atg11 in the cytoplasm-to-vacuole targeting pathway. <i> Coudevylle N, Banaś B, Baumann V, Schuschnig M, Zawadzka-Kazimierczuk A, Koźmiński W, Martens S. </i> J Biol Chem, 2022","date":"2022-06-03T14:45:20.658Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"Q12527","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03714r005","statement":[{"text":"As expected, we observed a robust recruitment of Atg9-NTD(1–255) to the beads coated with EGFP-Atg11 (Fig. 3, A and B). Mutation of the first PLF motif (M1) severely reduced the interaction, and mutation of the second PLF motif (M2) reduced the recruitment of the Atg9-NTD to the EGFP-Atg11-coated beads (Fig. 3, A and B) to a similar extent. Upon mutation of both motifs (M1+M2), the interaction between the Atg9-NTD and Atg11 became undetectable (Fig. 3, A and B).","type":"Results"},{"text":"M2 motiff is comprised of the 183-196 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:22:17.320Z"}},{"start":183,"end":196,"reference_id":"35007534","reference_source":"pmid","reference_html":"Mechanism of Atg9 recruitment by Atg11 in the cytoplasm-to-vacuole targeting pathway. <i> Coudevylle N, Banaś B, Baumann V, Schuschnig M, Zawadzka-Kazimierczuk A, Koźmiński W, Martens S. </i> J Biol Chem, 2022","date":"2022-06-03T14:48:31.416Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q12527","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03714r006","statement":[{"text":"This titration in combination with the assignment allowed us to identify the putative binding site for Atg11 in the Atg9 NTD, which consists of two short stretches (Fig. 2A), both being centered on a PLF motif (Fig. 2B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:22:04.148Z"}},{"start":158,"end":171,"reference_id":"35007534","reference_source":"pmid","reference_html":"Mechanism of Atg9 recruitment by Atg11 in the cytoplasm-to-vacuole targeting pathway. <i> Coudevylle N, Banaś B, Baumann V, Schuschnig M, Zawadzka-Kazimierczuk A, Koźmiński W, Martens S. </i> J Biol Chem, 2022","date":"2022-06-03T14:48:48.080Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q12527","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03714r007","statement":[{"text":"This titration in combination with the assignment allowed us to identify the putative binding site for Atg11 in the Atg9 NTD, which consists of two short stretches (Fig. 2A), both being centered on a PLF motif (Fig. 2B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T11:22:02.900Z"}}],"regions_counter":7,"released":"2022_06","sequence":"MERDEYQLPNSHGKNTFLSRIFGLQSDEVNPSLNSQEMSNFPLPDIERGSSLLHSTNDSREDVDENDLRVPESDQGTSTEEEDEVDEEQVQAYAPQISDGLDGDHQLNSVTSKENVLETEKSNLERLVEGSTDDSVPKVGQLSSEEEEDNEFINNDGFDDDTPLFQKSKIHEFSSKKSNTIEDGKRPLFFRHILQNNRPQRDTQKLFTSSNAIHHDKDKSANNGPRNINGNQKHGTKYFGSATQPRFTGSPLNNTNRFTKLFPLRKPNLLSNISVLNNTPEDRINTLSVKERALWKWANVENLDIFLQDVYNYYLGNGFYCIILEKILNICTLLFVVFVSTYMGHCVDYSKLPTSHRVSDIIIDKCYSNSITGFTKFFLWMFYFFVILKIVQLYFDVQKLSELQNFYKYLLNISDDELQTLPWQNVIQQLMYLKDQNAMTANVVEVKAKNRIDAHDVANRIMRRENYLIALYNSDILNLSLPIPLFRTNVLTKTLEWNINLCVMGFVFNESGFIKQSILKPSQREFTREELQKRFMLAGFLNIILAPFLVTYFVLLYFFRYFNEYKTSPGSIGARQYTPIAEWKFREYNELYHIFKKRISLSTTLANKYVDQFPKEKTNLFLKFVSFICGSFVAILAFLTVFDPENFLNFEITSDRSVIFYITILGAIWSVSRNTITQEYHVFDPEETLKELYEYTHYLPKEWEGRYHKEEIKLEFCKLYNLRIVILLRELTSLMITPFVLWFSLPSSAGRIVDFFRENSEYVDGLGYVCKYAMFNMKNIDGEDTHSMDEDSLTKKIAVNGSHTLNSKRRSKFTAEDHSDKDLANNKMLQSYVYFMDDYSNSENLTGKYQLPAKKGYPNNEGDSFLNNKYSWRKQFQPGQKPELFRIGKHALGPGHNISPAIYSTRNPGKNWDNNNNGDDIKNGTNNATAKNDDNNGNNDHEYVLTESFLDSGAFPNHDVIDHNKMLNSNYNGNGILNKGGVLGLVKEYYKKSDVGR","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"ATG9","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"14536056","url":"http://www.ncbi.nlm.nih.gov/pubmed/14536056","alternativeUrl":"https://europepmc.org/abstract/MED/14536056"}}]},"synonyms":[{"value":"APG9","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8224160","url":"http://www.ncbi.nlm.nih.gov/pubmed/8224160","alternativeUrl":"https://europepmc.org/abstract/MED/8224160"}}]},{"value":"AUT9","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8663607","url":"http://www.ncbi.nlm.nih.gov/pubmed/8663607","alternativeUrl":"https://europepmc.org/abstract/MED/8663607"}}]},{"value":"CVT7","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"7593182","url":"http://www.ncbi.nlm.nih.gov/pubmed/7593182","alternativeUrl":"https://europepmc.org/abstract/MED/7593182"}}]}],"orfNames":[{"value":"D1560","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8972581","url":"http://www.ncbi.nlm.nih.gov/pubmed/8972581","alternativeUrl":"https://europepmc.org/abstract/MED/8972581"}}]}],"olnNames":[{"value":"YDL149W","evidences":[{"code":"ECO:0000312","source":{"name":"SGD","id":"S000002308","url":"https://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000002308"}}]}]}],"alphafold_very_low_content":0.4493480441323972,"disorder_content":0.2858575727181545,"disprot_consensus":{"full":[{"start":1,"end":285,"type":"D"}],"Structural state":[{"start":1,"end":285,"type":"D"}],"Molecular function":[{"start":158,"end":171,"type":"F"},{"start":183,"end":196,"type":"F"}]}},{"disprot_id":"DP03715","acc":"Q02948","creator":"fquaglia","date":"2022-06-05T15:27:07.670Z","features":{"pfam":[{"id":"PF04111","name":"Apg6 BARA domain","start":317,"end":535},{"id":"PF17675","name":"Apg6 coiled-coil region","start":180,"end":314}],"gene3D":[]},"length":557,"name":"Vacuolar protein sorting-associated protein 30","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":156,"reference_id":"26450213","reference_source":"pmid","reference_html":"Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes. <i> Rostislavleva K, Soler N, Ohashi Y, Zhang L, Pardon E, Burke JE, Masson GR, Johnson C, Steyaert J, Ktistakis NT, Williams RL. </i> Science, 2015","date":"2022-06-05T15:29:22.153Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5DFZ"}],"region_id":"DP03715r001","statement":[{"text":"Interestingly, Vps30 and Vps38 show similar architectures except for their N-terminal domains, where Vps38 has a C2 domain, while Vps30 is mostly unstructured (fig. S3, A and B).","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T10:42:07.172Z"}},{"start":423,"end":432,"reference_id":"26450213","reference_source":"pmid","reference_html":"Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes. <i> Rostislavleva K, Soler N, Ohashi Y, Zhang L, Pardon E, Burke JE, Masson GR, Johnson C, Steyaert J, Ktistakis NT, Williams RL. </i> Science, 2015","date":"2022-06-05T15:31:01.890Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5DFZ"}],"region_id":"DP03715r002","statement":[{"text":"Missing electron density region of VPS30.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T10:42:08.394Z"}},{"start":463,"end":488,"reference_id":"26450213","reference_source":"pmid","reference_html":"Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes. <i> Rostislavleva K, Soler N, Ohashi Y, Zhang L, Pardon E, Burke JE, Masson GR, Johnson C, Steyaert J, Ktistakis NT, Williams RL. </i> Science, 2015","date":"2022-06-05T15:40:37.292Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5DFZ"}],"region_id":"DP03715r003","statement":[{"text":"Missing electron density region of VPS30.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T10:42:09.695Z"}},{"start":541,"end":557,"reference_id":"26450213","reference_source":"pmid","reference_html":"Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes. <i> Rostislavleva K, Soler N, Ohashi Y, Zhang L, Pardon E, Burke JE, Masson GR, Johnson C, Steyaert J, Ktistakis NT, Williams RL. </i> Science, 2015","date":"2022-06-05T15:40:56.920Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5DFZ"}],"region_id":"DP03715r004","statement":[{"text":"Missing electron density region of VPS30.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T10:42:10.977Z"}}],"regions_counter":4,"released":"2022_06","sequence":"MKCQTCHLPLQLDPSLEGLSLTQRNLLLSNNSIITATNENVISNKGIEAADNCGPQIPKERLRRLGEIQNIKDLNLKDDKLITDSFVFLNHDDDDNANITSNSREDQRYGNANGNDNKKANSDTSDGTSTFRDHDEEEQEATDEDENQQIQLNSKTLSTQVNAMTNVFNILSSQTNIDFPICQDCCNILINRLKSEYDDAIKERDTYAQFLSKLESQNKEISESNKEKQYSHNLSEKENLKKEEERLLDQLLRLEMTDDDLDGELVRLQEKKVQLENEKLQKLSDQNLMDLNNIQFNKNLQSLKLQYELSLNQLDKLRKINIFNATFKISHSGPFATINGLRLGSIPESVVPWKEINAALGQLILLLATINKNLKINLVDYELQPMGSFSKIKKRMVNSVEYNNSTTNAPGDWLILPVYYDENFNLGRIFRKETKFDKSLETTLEIISEITRQLSTIASSYSSQTLTTSQDESSMNNANDVENSTSILELPYIMNKDKINGLSVKLHGSSPNLEWTTAMKFLLTNVKWLLAFSSNLLSKSITLSPTVNYNDKTISGN","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"VPS30"},"synonyms":[{"value":"APG6"},{"value":"ATG6"},{"value":"VPT30"}],"orfNames":[{"value":"LPH7"}],"olnNames":[{"value":"YPL120W"}]}],"alphafold_very_low_content":0.26570915619389585,"disorder_content":0.3752244165170557,"disprot_consensus":{"full":[{"start":1,"end":156,"type":"D"},{"start":423,"end":432,"type":"D"},{"start":463,"end":488,"type":"D"},{"start":541,"end":557,"type":"D"}],"Structural state":[{"start":1,"end":156,"type":"D"},{"start":423,"end":432,"type":"D"},{"start":463,"end":488,"type":"D"},{"start":541,"end":557,"type":"D"}]}},{"disprot_id":"DP03716","acc":"P22219","creator":"fquaglia","date":"2022-06-05T15:43:58.730Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":46,"end":294},{"id":"PF22956","name":"PIK3R4-like, middle domain","start":425,"end":773}],"gene3D":[]},"length":1454,"name":"Serine/threonine-protein kinase VPS15","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":170,"end":193,"reference_id":"26450213","reference_source":"pmid","reference_html":"Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes. <i> Rostislavleva K, Soler N, Ohashi Y, Zhang L, Pardon E, Burke JE, Masson GR, Johnson C, Steyaert J, Ktistakis NT, Williams RL. </i> Science, 2015","date":"2022-06-05T15:50:27.888Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5DFZ"}],"region_id":"DP03716r001","statement":[{"text":"Missing electron density region of VPS15.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T10:41:13.861Z"}},{"start":378,"end":401,"reference_id":"26450213","reference_source":"pmid","reference_html":"Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes. <i> Rostislavleva K, Soler N, Ohashi Y, Zhang L, Pardon E, Burke JE, Masson GR, Johnson C, Steyaert J, Ktistakis NT, Williams RL. </i> Science, 2015","date":"2022-06-05T15:51:16.530Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5DFZ"}],"region_id":"DP03716r002","statement":[{"text":"Missing electron density region of VPS15.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T10:41:12.675Z"}},{"start":808,"end":833,"reference_id":"26450213","reference_source":"pmid","reference_html":"Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes. <i> Rostislavleva K, Soler N, Ohashi Y, Zhang L, Pardon E, Burke JE, Masson GR, Johnson C, Steyaert J, Ktistakis NT, Williams RL. </i> Science, 2015","date":"2022-06-05T16:27:26.261Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5DFZ"}],"region_id":"DP03716r003","statement":[{"text":"Missing electron density region of VPS15.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T10:41:11.310Z"}},{"start":887,"end":985,"reference_id":"26450213","reference_source":"pmid","reference_html":"Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes. <i> Rostislavleva K, Soler N, Ohashi Y, Zhang L, Pardon E, Burke JE, Masson GR, Johnson C, Steyaert J, Ktistakis NT, Williams RL. </i> Science, 2015","date":"2022-06-05T16:17:27.373Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5DFZ"}],"region_id":"DP03716r004","statement":[{"text":"Most of the Vps15 linker between the solenoid and WD40 is disordered (residues 889-985), except for an extended section (residues 986-1050) threading along the surface of Vps34-C2.","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T10:41:09.493Z"}},{"start":887,"end":985,"reference_id":"26450213","reference_source":"pmid","reference_html":"Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes. <i> Rostislavleva K, Soler N, Ohashi Y, Zhang L, Pardon E, Burke JE, Masson GR, Johnson C, Steyaert J, Ktistakis NT, Williams RL. </i> Science, 2015","date":"2022-06-05T16:17:48.576Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5DFZ"}],"region_id":"DP03716r005","statement":[{"text":"Most of the Vps15 linker between the solenoid and WD40 is disordered (residues 889-985), except for an extended section (residues 986-1050) threading along the surface of Vps34-C2.","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T10:41:15.027Z"}}],"regions_counter":5,"released":"2022_06","sequence":"MGAQLSLVVQASPSIAIFSYIDVLEEVHYVSQLNSSRFLKTCKALDPNGEIVIKVFIKPKDQYSLRPFLQRIRAQSFKLGQLPHVLNYSKLIETNRAGYMIRQHLKNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKPVYLPEDNPGEFLFYFDTSKRRTCYLAPERFNSKLYQDGKSNNGRLTKEMDIFSLGCVIAEIFAEGRPIFNLSQLFKYKSNSYDVNREFLMEEMNSTDLRNLVLDMIQLDPSKRLSCDELLNKYRGIFFPDYFYTFIYDYFRNLVTMTTSTPISDNTCTNSTLEDNVKLLDETTEKIYRDFSQICHCLDFPLIKDGGEIGSDPPILESYKIEIEISRFLNTNLYFPQNYHLVLQQFTKVSEKIKSVKEECALLFISYLSHSIRSIVSTATKLKNLELLAVFAQFVSDENKIDRVVPYFVCCFEDSDQDVQALSLLTLIQVLTSVRKLNQLNENIFVDYLLPRLKRLLISNRQNTNYLRIVFANCLSDLAIIINRFQEFTFAQHCNDNSMDNNTEIMESSTKYSAKLIQSVEDLTVSFLTDNDTYVKMALLQNILPLCKFFGRERTNDIILSHLITYLNDKDPALRVSLIQTISGISILLGTVTLEQYILPLLIQTITDSEELVVISVLQSLKSLFKTGLIRKKYYIDISKTTSPLLLHPNNWIRQFTLMIIIEIINKLSKAEVYCILYPIIRPFFEFDVEFNFKSMISCCKQPVSRSVYNLLCSWSVRASKSLFWKKIITNHVDSFGNNRIEFITKNYSSKNYGFNKRDTKSSSSLKGIKTSSTVYSHDNKEIPLTAEDRNWIDKFHIIGLTEKDIWKIVALRGYVIRTARVMAANPDFPYNNSNYRPLVQNSPPNLNLTNIMPRNIFFDVEFAEESTSEGQDSNLENQQIYKYDESEKDSNKLNINGSKQLSTVMDINGSLIFKNKSIATTTSNLKNVFVQLEPTSYHMHSPNHGLKDNANVKPERKVVVSNSYEGDVESIEKFLSTFKILPPLRDYKEFGPIQEIVRSPNMGNLRGKLIATLMENEPNSITSSAVSPGETPYLITGSDQGVIKIWNLKEIIVGEVYSSSLTYDCSSTVTQITMIPNFDAFAVSSKDGQIIVLKVNHYQQESEVKFLNCECIRKINLKNFGKNEYAVRMRAFVNEEKSLLVALTNLSRVIIFDIRTLERLQIIENSPRHGAVSSICIDEECCVLILGTTRGIIDIWDIRFNVLIRSWSFGDHAPITHVEVCQFYGKNSVIVVGGSSKTFLTIWNFVKGHCQYAFINSDEQPSMEHFLPIEKGLEELNFCGIRSLNALSTISVSNDKILLTDEATSSIVMFSLNELSSSKAVISPSRFSDVFIPTQVTANLTMLLRKMKRTSTHSVDDSLYHHDIINSISTCEVDETPLLVACDNSGLIGIFQ","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"VPS15"},"synonyms":[{"value":"GRD8"},{"value":"VAC4"},{"value":"VPL19"}],"orfNames":[{"value":"YBR0825"}],"olnNames":[{"value":"YBR097W"}]}],"alphafold_very_low_content":0.1375515818431912,"disorder_content":0.11898211829436038,"disprot_consensus":{"full":[{"start":170,"end":193,"type":"D"},{"start":378,"end":401,"type":"D"},{"start":808,"end":833,"type":"D"},{"start":887,"end":985,"type":"D"}],"Structural state":[{"start":170,"end":193,"type":"D"},{"start":378,"end":401,"type":"D"},{"start":808,"end":833,"type":"D"},{"start":887,"end":985,"type":"D"}],"Disorder function":[{"start":887,"end":985,"type":"F"}]}},{"disprot_id":"DP03717","acc":"P22543","creator":"fquaglia","date":"2022-06-05T16:21:40.178Z","features":{"pfam":[{"id":"PF00454","name":"Phosphatidylinositol 3- and 4-kinase","start":619,"end":821},{"id":"PF00613","name":"Phosphoinositide 3-kinase family, accessory domain (PIK domain)","start":295,"end":532},{"id":"PF00792","name":"Phosphoinositide 3-kinase C2","start":53,"end":184}],"gene3D":[]},"length":875,"name":"Phosphatidylinositol 3-kinase VPS34","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":226,"end":273,"reference_id":"26450213","reference_source":"pmid","reference_html":"Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes. <i> Rostislavleva K, Soler N, Ohashi Y, Zhang L, Pardon E, Burke JE, Masson GR, Johnson C, Steyaert J, Ktistakis NT, Williams RL. </i> Science, 2015","date":"2022-06-05T16:34:50.826Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5DFZ"}],"region_id":"DP03717r001","statement":[{"text":"Here, most of the C2/HELCAT linker appeared disordered, however a conserved Linker Helix (Fig. 3C) nestles in a crook between the Vps15 and Vps34, where it could provide a pivot for Vps34-HELCAT motions.","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T10:39:30.394Z"}},{"start":226,"end":273,"reference_id":"26450213","reference_source":"pmid","reference_html":"Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes. <i> Rostislavleva K, Soler N, Ohashi Y, Zhang L, Pardon E, Burke JE, Masson GR, Johnson C, Steyaert J, Ktistakis NT, Williams RL. </i> Science, 2015","date":"2022-06-05T16:35:02.397Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5DFZ"}],"region_id":"DP03717r002","statement":[{"text":"Here, most of the C2/HELCAT linker appeared disordered, however a conserved Linker Helix (Fig. 3C) nestles in a crook between the Vps15 and Vps34, where it could provide a pivot for Vps34-HELCAT motions.","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T10:39:29.123Z"}},{"start":438,"end":477,"reference_id":"26450213","reference_source":"pmid","reference_html":"Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes. <i> Rostislavleva K, Soler N, Ohashi Y, Zhang L, Pardon E, Burke JE, Masson GR, Johnson C, Steyaert J, Ktistakis NT, Williams RL. </i> Science, 2015","date":"2022-06-05T16:36:40.711Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5DFZ"}],"region_id":"DP03717r003","statement":[{"text":"Missing electron density region of VPS34.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T10:39:31.795Z"}}],"regions_counter":3,"released":"2022_06","sequence":"MSLNNITFCVSQDLDVPLKVKIKSLEGHKPLLKPSQKILNPELMLIGSNVFPSSDLIVSLQVFDKERNRNLTLPIYTPYIPFRNSRTWDYWLTLPIRIKQLTFSSHLRIILWEYNGSKQIPFFNLETSIFNLKDCTLKRGFESLKFRYDVIDHCEVVTDNKDQENLNKYFQGEFTRLPWLDEITISKLRKQRENRTWPQGTFVLNLEFPMLELPVVFIEREIMNTQMNIPTLKNNPGLSTDLREPNRNDPQIKISLGDKYHSTLKFYDPDQPNNDPIEEKYRRLERASKNANLDKQVKPDIKKRDYLNKIINYPPGTKLTAHEKGSIWKYRYYLMNNKKALTKLLQSTNLREESERVEVLELMDSWAEIDIDDALELLGSTFKNLSVRSYAVNRLKKASDKELELYLLQLVEAVCFENLSTFSDKSNSEFTIVDAVSSQKLSGDSMLLSTSHANQKLLKSISSESETSGTESLPIVISPLAEFLIRRALVNPRLGSFFYWYLKSESEDKPYLDQILSSFWSRLDKKSRNILNDQVRLINVLRECCETIKRLKDTTAKKMELLVHLLETKVRPLVKVRPIALPLDPDVLICDVCPETSKVFKSSLSPLKITFKTTLNQPYHLMFKVGDDLRQDQLVVQIISLMNELLKNENVDLKLTPYKILATGPQEGAIEFIPNDTLASILSKYHGILGYLKLHYPDENATLGVQGWVLDNFVKSCAGYCVITYILGVGDRHLDNLLVTPDGHFFHADFGYILGQDPKPFPPLMKLPPQIIEAFGGAESSNYDKFRSYCFVAYSILRRNAGLILNLFELMKTSNIPDIRIDPNGAILRVRERFNLNMSEEDATVHFQNLINDSVNALLPIVIDHLHNLAQYWRT","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"VPS34"},"synonyms":[{"value":"END12"},{"value":"PEP15"},{"value":"VPL7"},{"value":"VPT29"}],"orfNames":[{"value":"L9672.10"}],"olnNames":[{"value":"YLR240W"}]}],"alphafold_very_low_content":0.12685714285714286,"disorder_content":0.10057142857142858,"disprot_consensus":{"full":[{"start":226,"end":273,"type":"D"},{"start":438,"end":477,"type":"D"}],"Structural state":[{"start":226,"end":273,"type":"D"},{"start":438,"end":477,"type":"D"}],"Disorder function":[{"start":226,"end":273,"type":"F"}]}},{"disprot_id":"DP03718","acc":"Q05919","creator":"fquaglia","date":"2022-06-05T16:38:45.260Z","features":{"pfam":[{"id":"PF17649","name":"Vacuolar protein sorting 38","start":1,"end":436}],"gene3D":[]},"length":439,"name":"Vacuolar protein sorting-associated protein 38","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":19,"reference_id":"26450213","reference_source":"pmid","reference_html":"Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes. <i> Rostislavleva K, Soler N, Ohashi Y, Zhang L, Pardon E, Burke JE, Masson GR, Johnson C, Steyaert J, Ktistakis NT, Williams RL. </i> Science, 2015","date":"2022-06-05T16:47:14.615Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5DFZ"}],"region_id":"DP03718r001","statement":[{"text":"Missing electron density region of VPS38.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T10:38:43.844Z"}},{"start":91,"end":110,"reference_id":"26450213","reference_source":"pmid","reference_html":"Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes. <i> Rostislavleva K, Soler N, Ohashi Y, Zhang L, Pardon E, Burke JE, Masson GR, Johnson C, Steyaert J, Ktistakis NT, Williams RL. </i> Science, 2015","date":"2022-06-05T16:47:38.604Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5DFZ"}],"region_id":"DP03718r002","statement":[{"text":"Missing electron density region of VPS38.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T10:38:42.593Z"}},{"start":152,"end":183,"reference_id":"26450213","reference_source":"pmid","reference_html":"Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes. <i> Rostislavleva K, Soler N, Ohashi Y, Zhang L, Pardon E, Burke JE, Masson GR, Johnson C, Steyaert J, Ktistakis NT, Williams RL. </i> Science, 2015","date":"2022-06-05T16:48:07.622Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5DFZ"}],"region_id":"DP03718r003","statement":[{"text":"Missing electron density region of VPS38.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T10:38:41.510Z"}},{"start":322,"end":344,"reference_id":"26450213","reference_source":"pmid","reference_html":"Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes. <i> Rostislavleva K, Soler N, Ohashi Y, Zhang L, Pardon E, Burke JE, Masson GR, Johnson C, Steyaert J, Ktistakis NT, Williams RL. </i> Science, 2015","date":"2022-06-05T16:48:32.920Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5DFZ"}],"region_id":"DP03718r004","statement":[{"text":"Missing electron density region of VPS38.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T10:38:39.333Z"}},{"start":152,"end":183,"reference_id":"26450213","reference_source":"pmid","reference_html":"Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes. <i> Rostislavleva K, Soler N, Ohashi Y, Zhang L, Pardon E, Burke JE, Masson GR, Johnson C, Steyaert J, Ktistakis NT, Williams RL. </i> Science, 2015","date":"2022-06-05T16:50:37.196Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5DFZ"}],"region_id":"DP03718r005","statement":[{"text":"Linker connecting the C2 and CC1 domains of VPS38.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-06T10:38:44.543Z"}}],"regions_counter":5,"released":"2022_06","sequence":"MKRFLLSRRQRHLRMICFHNISLFRANGDSKLIKEYGDGFIPCFFILESIRGELLYVSEVQSGSLRKLSFQELPKLTGASTMIVLKLVGLVPSDILCTISSDKNGIIDDKWCVLCTYTIDLNKLQPINEDTVLITGTNAPVLDLIDGSYTLAAEKIKPLKGLVSSHKRNISQVKIKFSLAYSSLLKLNKLLEYSSQVHEEINEISSKIEDDFLSLKNQNHWYMRTVQKSIETLEKEVLQRKKSKKNIEMAQLESNDTINHSKTELSLMSQDESINDDYGSIYSRFVQIKDRLDQLRFKKLYQLIGIFHSTDLFNSDRGYIYFEKPSSVNDVINRLKLKPLNIEILLRQAGESTKHREYVNSQLGYYLLFLHLTAIQIFKAPLPYRLMYYGSTSVIDSQYPLYFTDQMISKHQAKLIKAIHYFNADILQFKQILENYRPT","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"VPS38"},"synonyms":[{"value":"VPL17"}],"orfNames":[{"value":"L8039.11"}],"olnNames":[{"value":"YLR360W"}]}],"alphafold_very_low_content":0.09567198177676538,"disorder_content":0.214123006833713,"disprot_consensus":{"full":[{"start":1,"end":19,"type":"D"},{"start":91,"end":110,"type":"D"},{"start":152,"end":183,"type":"D"},{"start":322,"end":344,"type":"D"}],"Structural state":[{"start":1,"end":19,"type":"D"},{"start":91,"end":110,"type":"D"},{"start":152,"end":183,"type":"D"},{"start":322,"end":344,"type":"D"}],"Disorder function":[{"start":152,"end":183,"type":"F"}]}},{"disprot_id":"DP03719","acc":"O15392","creator":"vnugnes","date":"2022-06-06T12:30:59.896Z","features":{"pfam":[{"id":"PF00653","name":"Inhibitor of Apoptosis domain","start":18,"end":87}],"gene3D":[]},"length":142,"name":"Baculoviral IAP repeat-containing protein 5","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":10,"reference_id":"22032967","reference_source":"pmid","reference_html":"Structural basis for the recognition of phosphorylated histone h3 by the survivin subunit of the chromosomal passenger complex. <i> Jeyaprakash AA, Basquin C, Jayachandran U, Conti E. </i> Structure, 2011","date":"2022-06-06T13:01:32.104Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"4A0N"}],"region_id":"DP03719r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P68431","statements":[{"type":"Curator statement","text":"Phosphorylated N-terminal peptide from the tail of histone H3, with sequence \"ARTKQT\"."}]}],"statement":[{"text":"This region lacks electron density, as shown in the PDB, indicating it's disordered.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-08T10:43:22.855Z"}},{"start":1,"end":99,"reference_id":"22032967","reference_source":"pmid","reference_html":"Structural basis for the recognition of phosphorylated histone h3 by the survivin subunit of the chromosomal passenger complex. <i> Jeyaprakash AA, Basquin C, Jayachandran U, Conti E. </i> Structure, 2011","date":"2022-06-06T13:04:16.795Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"BMRB","id":"6342"}],"region_id":"DP03719r002","sequence_construct":"MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLG","statement":[{"text":"Truncated forms of survivin with only the BIR domain (residues 1−99) have been reported not to interact with Smac/Diablo ( 8) or to localize to the mitotic spindle ( 17). To understand the role of the C-terminal helix for the function of survivin, we cloned and expressed the (residues 1−99) BIR domain only construct. [15N,1H]HSQC spectra for the (residues 1−99) construct did not have the same well- resolved resonances found for full length survivin or our survivin(1−120) construct (data not shown). The lack of well-resolved resonances is characteristic of unfolded or aggregated proteins. This result suggests that the (1−99) construct of survivin is not properly folded. This conclusion is consistent with the structure of the survivin dimer. In the structure, residues 99−110 are involved in making contacts across the dimer interface. These contacts are likely to be important for dimer formation and thus also for protein stability. Removing these key residues is likely to interfere with proper folding of the protein.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-08T10:43:51.952Z"}}],"regions_counter":2,"released":"2022_06","sequence":"MGAPTLPPAWQPFLKDHRISTFKNWPFLEGCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDDPIEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins","Condensates-related proteins"],"genes":[{"name":{"value":"BIRC5"},"synonyms":[{"value":"API4"},{"value":"IAP4"}]}],"alphafold_very_low_content":0.007042253521126761,"disorder_content":0.6971830985915493,"disprot_consensus":{"full":[{"start":1,"end":99,"type":"D"}],"Structural state":[{"start":1,"end":99,"type":"D"}]}},{"disprot_id":"DP03721","acc":"Q9W1M7","creator":"vnugnes","date":"2022-06-06T15:08:47.670Z","features":{"pfam":[{"id":"PF00454","name":"Phosphatidylinositol 3- and 4-kinase","start":692,"end":893},{"id":"PF00613","name":"Phosphoinositide 3-kinase family, accessory domain (PIK domain)","start":286,"end":578},{"id":"PF00792","name":"Phosphoinositide 3-kinase C2","start":55,"end":198}],"gene3D":[]},"length":949,"name":"Phosphatidylinositol 3-kinase catalytic subunit type 3","ncbi_taxon_id":7227,"organism":"Drosophila melanogaster","regions":[{"start":422,"end":531,"reference_id":"20339072","reference_source":"pmid","reference_html":"Shaping development of autophagy inhibitors with the structure of the lipid kinase Vps34. <i> Miller S, Tavshanjian B, Oleksy A, Perisic O, Houseman BT, Shokat KM, Williams RL. </i> Science, 2010","date":"2022-06-08T13:34:25.937Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"2X6H"}],"region_id":"DP03721r001","statement":[{"text":"The lack of electron density in this region indicates it's disordered.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-08T13:51:08.076Z"}},{"start":423,"end":531,"reference_id":"20339072","reference_source":"pmid","reference_html":"Shaping development of autophagy inhibitors with the structure of the lipid kinase Vps34. <i> Miller S, Tavshanjian B, Oleksy A, Perisic O, Houseman BT, Shokat KM, Williams RL. </i> Science, 2010","date":"2022-06-08T13:34:16.428Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"2X6F"}],"region_id":"DP03721r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"38635","entry_name":"3-methyladenine"}],"statement":[{"text":"The lack of electron density in this region indicates it's disordered.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-08T13:51:07.266Z"}}],"regions_counter":2,"released":"2022_06","sequence":"MDQPDDHFRYIHSSSLHERVQIKVGTLEGKKRQPDYEKLLEDPILRFSGLYSEEHPSFQVRLQVFNQGRPYCLPVTSSYKAFGKRWSWNEWVTLPLQFSDLPRSAMLVLTILDCSGAGQTTVIGGTSISMFGKDGMFRQGMYDLRVWLGVEGDGNFPSRTPGKGKESSKSQMQRLGKLAKKHRNGQVQKVDWLDRLTFREIEVINEREKRMSDYMFLMIEFPAIVVDDMYNYAVVYFEPEGDVKYKLPAKPKLVSVPDSEIQMENLVERKHHRLARSERSGISDRDAKPTASIRDQLHTIVYRYPPTYVLSSEEQDLVWKFRFYLSSHKKALTKFLKCINWKLEDEVTQALWMLANWAPMDVEDALELLSPTFTHPQVRKYAVSRLAQAPDEDLLLYLLQLVQALKYEDPRHIVHLHGCIFPERDVVRSILDDNGSLLDQSSLSDLSATSSGLHGSVIPANQRAASVLAAIKSDKSVSPGSAGGSGSGGQGSVALPNPSAPATPGSSSLPCDSNSNALMLAEGISFGSVPANLCTFLIQRACTNATLANYFYWYLSIEVEEVESVRKQDERAHDMYAMVLKMFLKVLENGNFNLRGIFYNLRKQRRFIDELVKLVKLVAKEPGNRNKKTEKFQKLLAEQDMFKVNFTNFEPIPFPLDPEIYITKIVPMRTSLFKSALMPAKLTFVTSIAHHEYAAIFKHGDDLRQDQLILQMITLMDKLLRRENLDLKLTPYKVLATSSKHGFLQYVDSCTVAEVLAREGNIHNFFRKHHPCDNGPYGISAEVMDTYIKSCAGYCVITYLLGVGDRHLDNLLLTTNGKLFHIDFGYILGRDPKPMPPPMKLSKEMVEAMGGISSEHHHEFRKQCYTAYLHLRRHANVMLNLFSLMVDATVPDIALEPDKAVKKVEENLQLGLTDEEAVQHLQSLLDVSITAVMPALVEQIHRFTQYWRK","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"Pi3K59F","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47030.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47030.2"}},{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0015277","url":"http://flybase.org/reports/FBgn0015277.html"}}]},"synonyms":[{"value":"Dmel\\CG5373","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47030.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47030.2"}}]},{"value":"DmVps34","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47030.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47030.2"}}]},{"value":"dPI3K","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47030.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47030.2"}}]},{"value":"dVps34","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47030.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47030.2"}}]},{"value":"PI(3)K","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47030.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47030.2"}}]},{"value":"PI3K","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47030.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47030.2"}}]},{"value":"PI3K-59F","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47030.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47030.2"}}]},{"value":"PI3K59F","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47030.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47030.2"}}]},{"value":"Pi3k59F","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47030.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47030.2"}}]},{"value":"PI3K_59F","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47030.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47030.2"}}]},{"value":"Pi3K_59F","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47030.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47030.2"}}]},{"value":"PI[[3]]K","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47030.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47030.2"}}]},{"value":"PIK359F","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47030.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47030.2"}}]},{"value":"VPS34","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47030.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47030.2"}}]},{"value":"Vps34","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47030.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47030.2"}}]},{"value":"vps34","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47030.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47030.2"}}]}],"orfNames":[{"value":"CG5373","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47030.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47030.2"}},{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0015277","url":"http://flybase.org/reports/FBgn0015277.html"}}]},{"value":"Dmel_CG5373","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF47030.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF47030.2"}}]}]}],"alphafold_very_low_content":0.13066385669125394,"disorder_content":0.11591148577449947,"disprot_consensus":{"full":[{"start":422,"end":531,"type":"D"}],"Structural state":[{"start":422,"end":531,"type":"D"}]}},{"disprot_id":"DP03722","acc":"P01089","creator":"cpintado","date":"2022-06-07T12:46:19.895Z","features":{"pfam":[{"id":"PF00234","name":"Protease inhibitor/seed storage/LTP family","start":61,"end":151},{"id":"PF00234","name":"Protease inhibitor/seed storage/LTP family","start":167,"end":255}],"gene3D":[]},"length":258,"name":"2S seed storage albumin protein","ncbi_taxon_id":3988,"organism":"Ricinus communis","regions":[{"start":36,"end":45,"reference_id":"14636051","reference_source":"pmid","reference_html":"Solution structure of RicC3, a 2S albumin storage protein from Ricinus communis. <i> Pantoja-Uceda D, Bruix M, Giménez-Gallego G, Rico M, Santoro J. </i> Biochemistry, 2003","date":"2022-07-15T09:33:15.380Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1PSY"}],"region_id":"DP03722r001","statement":[{"text":"The first 14 residues, highly disordered, are not represented.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-15T13:27:41.026Z"}},{"start":68,"end":92,"reference_id":"14636051","reference_source":"pmid","reference_html":"Solution structure of RicC3, a 2S albumin storage protein from Ricinus communis. <i> Pantoja-Uceda D, Bruix M, Giménez-Gallego G, Rico M, Santoro J. </i> Biochemistry, 2003","date":"2022-07-15T09:34:39.181Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1PSY"}],"region_id":"DP03722r002","statement":[{"text":"Between helix Ib and helix II, there is a long unstructured loop encompassing the residues corresponding to the linker.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-15T13:27:47.913Z"}}],"regions_counter":2,"released":"2023_12","sequence":"MAKLIPTIALVSVLLFIIANASFAYRTTITTIEIDESKGEREGSSSQQCRQEVQRKDLSSCERYLRQSSSRRSPGEEVLRMPGDENQQQESQQLQQCCNQVKQVRDECQCEAIKYIAEDQIQQGQLHGEESERVAQRAGEIVSSCGVRCMRQTRTNPSQQGCRGQIQEQQNLRQCQEYIKQQVSGQGPRRSDNQERSLRGCCDHLKQMQSQCRCEGLRQAIEQQQSQGQLQGQDVFEAFRTAANLPSMCGVSPTECRF","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","fabids","Malpighiales","Euphorbiaceae","Acalyphoideae","Acalypheae","Ricinus"],"genes":[],"alphafold_very_low_content":0.13953488372093023,"disorder_content":0.13565891472868216,"disprot_consensus":{"full":[{"start":36,"end":45,"type":"D"},{"start":68,"end":92,"type":"D"}],"Structural state":[{"start":36,"end":45,"type":"D"},{"start":68,"end":92,"type":"D"}]}},{"disprot_id":"DP03723","acc":"P23110","creator":"cpintado","date":"2022-06-07T13:14:10.321Z","features":{"pfam":[{"id":"PF00234","name":"Protease inhibitor/seed storage/LTP family","start":49,"end":139}],"gene3D":[]},"length":141,"name":"Albumin-8","ncbi_taxon_id":4232,"organism":"Helianthus annuus","regions":[{"start":39,"end":48,"reference_id":"15170335","reference_source":"pmid","reference_html":"Solution structure of a methionine-rich 2S albumin from sunflower seeds: relationship to its allergenic and emulsifying properties. <i> Pantoja-Uceda D, Shewry PR, Bruix M, Tatham AS, Santoro J, Rico M. </i> Biochemistry, 2004","date":"2022-06-07T13:16:43.759Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1S6D"}],"region_id":"DP03723r001","statement":[{"text":"The average rmsd from the mean for backbone atoms of the most structured regions are 0.52 and 1.01 Å for all heavy atoms, excluding unstructured regions at the N- and C-termini (residues 1−10 and 102 and 103, respectively) and the region between residues 31 and 45.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-13T18:57:21.558Z"}},{"start":68,"end":87,"reference_id":"15170335","reference_source":"pmid","reference_html":"Solution structure of a methionine-rich 2S albumin from sunflower seeds: relationship to its allergenic and emulsifying properties. <i> Pantoja-Uceda D, Shewry PR, Bruix M, Tatham AS, Santoro J, Rico M. </i> Biochemistry, 2004","date":"2022-06-07T13:18:46.546Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1S6D"}],"region_id":"DP03723r002","statement":[{"text":"A long, unstructured loop region (L2) is present between helices Ib and II, encompassing residues Lys30−Gln49. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-13T18:57:21.092Z"}}],"regions_counter":2,"released":"2023_12","sequence":"MARFSIVFAAAGVLLLVAMAPVSEASTTTIITTIIEENPYGRGRTESGCYQQMEEAEMLNHCGMYLMKNLGERSQVSPRMREEDHKQLCCMQLKNLDEKCMCPAIMMMLNEPMWIRMRDQVMSMAHNLPIECNLMSQPCQM","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","campanulids","Asterales","Asteraceae","Asteroideae","Heliantheae alliance","Heliantheae","Helianthus"],"genes":[],"alphafold_very_low_content":0.18439716312056736,"disorder_content":0.2127659574468085,"disprot_consensus":{"full":[{"start":39,"end":48,"type":"D"},{"start":68,"end":87,"type":"D"}],"Structural state":[{"start":39,"end":48,"type":"D"},{"start":68,"end":87,"type":"D"}]}},{"disprot_id":"DP03724","acc":"A0A396GSL0","creator":"cpintado","date":"2022-06-07T13:28:42.490Z","features":{"pfam":[{"id":"PF07127","name":"Late nodulin domain","start":7,"end":62}],"gene3D":[]},"length":68,"name":"Putative Late nodulin","ncbi_taxon_id":3880,"organism":"Medicago truncatula","regions":[{"start":33,"end":55,"reference_id":"32571919","reference_source":"pmid","reference_html":"Antifungal symbiotic peptide NCR044 exhibits unique structure and multifaceted mechanisms of action that confer plant protection. <i> Velivelli SLS, Czymmek KJ, Li H, Shaw JB, Buchko GW, Shah DM. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-07-15T09:44:44.616Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6U6G"}],"region_id":"DP03724r001","statement":[{"text":"NCR044 contains one short (A23 to R25, G28 to C30) antiparallel β-sheet and a “whiff” (S11 to E14) of an α-helix. The rest of the peptide was largely disordered and dynamic, even with the tethering afforded by the two disulfide bonds. ","type":"Results"},{"text":"The short helix found between residues 48-52 is too short to be considered as ordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-15T13:28:30.869Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MQRVKNMTETLKFVYILILFIFIFLVLMVCDSAFIQLSKPCISDKECSIVKNYRARCRKGYCVRRRIR","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","fabids","Fabales","Fabaceae","Papilionoideae","50 kb inversion clade","NPAAA clade","Hologalegina","IRL clade","Trifolieae","Medicago"],"genes":[{"orfNames":[{"value":"MtrunA17_Chr7g0216231","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"RHN44149.1","url":"https://www.ebi.ac.uk/ena/browser/view/RHN44149.1"}}]}]}],"alphafold_very_low_content":0,"disorder_content":0.3382352941176471,"disprot_consensus":{"full":[{"start":33,"end":55,"type":"D"}],"Structural state":[{"start":33,"end":55,"type":"D"}]}},{"disprot_id":"DP03726","acc":"P40939","creator":"vnugnes","date":"2022-06-07T14:27:04.097Z","features":{"pfam":[{"id":"PF00378","name":"Enoyl-CoA hydratase/isomerase","start":47,"end":222},{"id":"PF00725","name":"3-hydroxyacyl-CoA dehydrogenase, C-terminal domain","start":544,"end":639},{"id":"PF00725","name":"3-hydroxyacyl-CoA dehydrogenase, C-terminal domain","start":676,"end":755},{"id":"PF02737","name":"3-hydroxyacyl-CoA dehydrogenase, NAD binding domain","start":364,"end":541}],"gene3D":[]},"length":763,"name":"Trifunctional enzyme subunit alpha, mitochondrial","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":637,"end":647,"reference_id":"29915090","reference_source":"pmid","reference_html":"Cryo-EM structure of human mitochondrial trifunctional protein. <i> Liang K, Li N, Wang X, Dai J, Liu P, Wang C, Chen XW, Gao N, Xiao J. </i> Proc Natl Acad Sci U S A, 2018","date":"2022-06-07T14:37:40.805Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"5ZQZ"},{"db":"PDB","id":"5ZRV"}],"region_id":"DP03726r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P55084"}],"statement":[{"text":"Residues 261–265 and 637–647 in TFPα and residues 187–192 in TFPβ were not built, due to the lack of densities in these regions.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-08T10:19:15.017Z"}}],"regions_counter":1,"released":"2022_06","sequence":"MVACRAIGILSRFSAFRILRSRGYICRNFTGSSALLTRTHINYGVKGDVAVVRINSPNSKVNTLSKELHSEFSEVMNEIWASDQIRSAVLISSKPGCFIAGADINMLAACKTLQEVTQLSQEAQRIVEKLEKSTKPIVAAINGSCLGGGLEVAISCQYRIATKDRKTVLGTPEVLLGALPGAGGTQRLPKMVGVPAALDMMLTGRSIRADRAKKMGLVDQLVEPLGPGLKPPEERTIEYLEEVAITFAKGLADKKISPKRDKGLVEKLTAYAMTIPFVRQQVYKKVEEKVRKQTKGLYPAPLKIIDVVKTGIEQGSDAGYLCESQKFGELVMTKESKALMGLYHGQVLCKKNKFGAPQKDVKHLAILGAGLMGAGIAQVSVDKGLKTILKDATLTALDRGQQQVFKGLNDKVKKKALTSFERDSIFSNLTGQLDYQGFEKADMVIEAVFEDLSLKHRVLKEVEAVIPDHCIFASNTSALPISEIAAVSKRPEKVIGMHYFSPVDKMQLLEIITTEKTSKDTSASAVAVGLKQGKVIIVVKDGPGFYTTRCLAPMMSEVIRILQEGVDPKKLDSLTTSFGFPVGAATLVDEVGVDVAKHVAEDLGKVFGERFGGGNPELLTQMVSKGFLGRKSGKGFYIYQEGVKRKDLNSDMDSILASLKLPPKSEVSSDEDIQFRLVTRFVNEAVMCLQEGILATPAEGDIGAVFGLGFPPCLGGPFRFVDLYGAQKIVDRLKKYEAAYGKQFTPCQLLADHANSPNKKFYQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"HADHA"},"synonyms":[{"value":"HADH"}]}],"alphafold_very_low_content":0.045871559633027525,"disorder_content":0.014416775884665793,"disprot_consensus":{"full":[{"start":637,"end":647,"type":"D"}],"Structural state":[{"start":637,"end":647,"type":"D"}]}},{"disprot_id":"DP03727","acc":"A7KHA7","creator":"cpintado","date":"2022-06-07T15:13:55.090Z","features":{"pfam":[{"id":"PF07127","name":"Late nodulin domain","start":1,"end":56}],"gene3D":[]},"length":61,"name":"Nodule Cysteine-Rich (NCR) secreted peptide","ncbi_taxon_id":3880,"organism":"Medicago truncatula","regions":[{"start":24,"end":50,"reference_id":"33972675","reference_source":"pmid","reference_html":"Structure and antimicrobial activity of NCR169, a nodule-specific cysteine-rich peptide of Medicago truncatula. <i> Isozumi N, Masubuchi Y, Imamura T, Mori M, Koga H, Ohki S. </i> Sci Rep, 2021","date":"2022-07-15T09:47:32.644Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7CKD"},{"db":"PDB","id":"7CKE"}],"region_id":"DP03727r001","statement":[{"text":"The chemical shift differences between NCR169-ox1 and -ox2 revealed structural differences derived from different disulfide linkage patterns (Supplementary Fig. S6B). As shown in Fig. 2B,C a major difference between the two structures was found in the position of the unstructured N-terminal region.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-15T13:30:02.795Z"}},{"start":39,"end":50,"reference_id":"33972675","reference_source":"pmid","reference_html":"Structure and antimicrobial activity of NCR169, a nodule-specific cysteine-rich peptide of Medicago truncatula. <i> Isozumi N, Masubuchi Y, Imamura T, Mori M, Koga H, Ohki S. </i> Sci Rep, 2021","date":"2022-07-18T09:07:37.190Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"GO:0042742","term_name":"defense response to bacterium","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007084","ec_ontology":"ECO","ec_name":"zone of inhibition evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP03727r002","statement":[{"text":"NCR169M and NCR169CL-ox had stronger activity than NCR169CS-ox. This result suggested that the region corresponding to NCR169M containing lysine residues contributes the most to the antimicrobial activity, as predicted.","type":"Results"},{"text":"NCR169M showed the highest antimicrobial activity against the symbiotic partner, S. meliloti.","type":"Results"},{"text":"Thus, the disordered conformation of the central Lys-rich region of NCR169 is a unique property that is key to membrane binding and antimicrobial activity.","type":"Results"}],"term_comment":"","term_def":"\"Reactions triggered in response to the presence of a bacterium that act to protect the cell or organism.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-18T12:37:55.851Z"}},{"start":24,"end":39,"reference_id":"33972675","reference_source":"pmid","reference_html":"Structure and antimicrobial activity of NCR169, a nodule-specific cysteine-rich peptide of Medicago truncatula. <i> Isozumi N, Masubuchi Y, Imamura T, Mori M, Koga H, Ohki S. </i> Sci Rep, 2021","date":"2022-07-18T09:06:46.326Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006200","ec_ontology":"ECO","ec_name":"circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03727r003","statement":[{"text":"Furthermore, CD spectra suggested that NCR169N-ox and NCR169M have random structures, whereas NCR169CS-ox and NCR169CL-ox contain β-sheets (Supplementary Fig. S10B and S11A). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-18T12:37:58.841Z"}},{"start":39,"end":50,"reference_id":"33972675","reference_source":"pmid","reference_html":"Structure and antimicrobial activity of NCR169, a nodule-specific cysteine-rich peptide of Medicago truncatula. <i> Isozumi N, Masubuchi Y, Imamura T, Mori M, Koga H, Ohki S. </i> Sci Rep, 2021","date":"2022-07-18T09:07:05.934Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006200","ec_ontology":"ECO","ec_name":"circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03727r004","statement":[{"text":"Furthermore, CD spectra suggested that NCR169N-ox and NCR169M have random structures, whereas NCR169CS-ox and NCR169CL-ox contain β-sheets (Supplementary Fig. S10B and S11A). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-18T12:38:00.844Z"}},{"start":39,"end":50,"reference_id":"33972675","reference_source":"pmid","reference_html":"Structure and antimicrobial activity of NCR169, a nodule-specific cysteine-rich peptide of Medicago truncatula. <i> Isozumi N, Masubuchi Y, Imamura T, Mori M, Koga H, Ohki S. </i> Sci Rep, 2021","date":"2022-07-18T09:07:54.423Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","region_id":"DP03727r005","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"138360","entry_name":"ditetradecanoyl phosphatidylglycerol(1-)"}],"statement":[{"text":"As expected, NCR169M, NCR169CS-ox, and NCR169CL-ox bound to DMPG liposomes, but NCR169N-ox did not (Supplementary Figs. S11B and S12). This result suggested that the region corresponding to NCR169M, at least residues 24 to 27, is involved in binding to DMPG.","type":"Results"},{"text":"Thus, the disordered conformation of the central Lys-rich region of NCR169 is a unique property that is key to membrane binding and antimicrobial activity.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-18T12:37:55.272Z"}}],"regions_counter":5,"released":"2023_12","sequence":"MGEMFKFIYTFILFVHLFLVVIFEDIGHIKYCGIVDDCYKSKKPLFKIWKCVENVCVLWYK","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","fabids","Fabales","Fabaceae","Papilionoideae","50 kb inversion clade","NPAAA clade","Hologalegina","IRL clade","Trifolieae","Medicago"],"genes":[{"olnNames":[{"value":"MTR_7g029760","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AES78393.2","url":"https://www.ebi.ac.uk/ena/browser/view/AES78393.2"}}]}]}],"alphafold_very_low_content":0.09836065573770492,"disorder_content":0.4426229508196721,"disprot_consensus":{"full":[{"start":24,"end":50,"type":"D"}],"Structural state":[{"start":24,"end":50,"type":"D"}],"Biological process":[{"start":39,"end":50,"type":"F"}],"Molecular function":[{"start":39,"end":50,"type":"F"}]}},{"disprot_id":"DP03728","acc":"Q6CSX2","creator":"fquaglia","date":"2022-06-07T17:34:52.017Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":21,"end":318},{"id":"PF12063","name":"Atg1-like, MIT domain 1","start":566,"end":724},{"id":"PF21127","name":"ATG1-like, MIT domain 2","start":736,"end":830}],"gene3D":[]},"length":831,"name":"Serine/threonine-protein kinase ATG1","ncbi_taxon_id":284590,"organism":"Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)","regions":[{"start":562,"end":831,"reference_id":"25139988","reference_source":"pmid","reference_html":"Assembly and dynamics of the autophagy-initiating Atg1 complex. <i> Stjepanovic G, Davies CW, Stanley RE, Ragusa MJ, Kim DJ, Hurley JH. </i> Proc Natl Acad Sci U S A, 2014","date":"2022-06-07T19:02:02.391Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"region_id":"DP03728r001","statement":[{"text":"To gain insights into the dynamic properties of Atg1EAT in solution, we performed continuous-labeling HDX-MS (29–31). We initially measured deuteron incorporation into isolated Atg1EAT to analyze the overall kinetics of the HDX reaction. Atg1EAT exchanged about 60% of its exchangeable amide hydrogens within 10 s in D2O (Fig. 2 and Figs. S2–S4). The overall exchange characteristics indicate the presence of a large fraction of highly dynamic, solvent-accessible structure.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-01T19:13:00.664Z"}},{"start":562,"end":831,"reference_id":"25139988","reference_source":"pmid","reference_html":"Assembly and dynamics of the autophagy-initiating Atg1 complex. <i> Stjepanovic G, Davies CW, Stanley RE, Ragusa MJ, Kim DJ, Hurley JH. </i> Proc Natl Acad Sci U S A, 2014","date":"2022-06-07T21:12:35.877Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:1990316","term_name":"Atg1/ULK1 kinase complex","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2022_06","version":0,"ec_go":"EXP","region_id":"DP03728r002","statement":[{"text":"On the basis of the SEC-MALS, a molecular mass of 234 kDa was independently obtained (Fig. S6B and Table S1), consistent with a predominant population of Atg1EAT–Atg13350–525–Atg17–Atg31–Atg29 dimers. Taken together with the ITC and HDX-MS data, these results led us to a model for the pathway of Atg1 complex assembly (Fig. 5).","type":"Results"}],"term_comment":"","term_def":"\"A protein complex consisting of Atg1 (or Atg1 homologs e.g. ULK1, ULK2 in mammals) and Atg13 along with other proteins that regulate its function (e.g. Atg17 in yeast or RB1CC1(FIP200) in mammals). This complex has serine/threonine protein kinase activity and is involved in autophagosome formation.\" [GOC:bhm, GOC:DOS, GOC:rb, PMID:15743910, PMID:19211835, PMID:19258318, PMID:19597335, PMID:22885598]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-01T19:14:03.356Z"}}],"regions_counter":2,"released":"2022_06","sequence":"MSSESHDKVVAKAIRLPTENYSVEKEIGKGSFAVVYKGLSLRDGRNIAIKAVSRSKLKNKKLLENLEVEIAILKKIKHPHIVGLIDCERTSSDFYLIMEYCALGDLTFFIKKRKNLVLKHPLIKTVFEHYPPPSTEHNGLNRVLVVNYLQQLSSALKFLRSKNLVHRDIKPQNLLLCTPLLDYNDPKTFHELGFVGIYNLPILKIADFGFARFLPNTSLAETLCGSPLYMAPEILNYQKYNAKADLWSVGTVLYEMCCGRPPFKASNHLELFQKIKKANDEITVPSNCYIEPKLFNLIRGLLTFDPDSRMGFTDFFNNEVVTEDLTRYEQSYEPDLESKSKDVAESNMFVSEYLVKPLKQQESAHIPPTQTDENTSVQTGVRRTSGKERLATNHPPHQQIHPEDNSQNPEQSYQSASQKRLKSSYNDLILEKEYVVVEKKTVEVNSLADDFANNGPITNNQGAQVIKPLRYRTSSSSDASGGRRASLVERRLSISSLSPSNALSKALGLASVRLFGYQHNTKATSSPPQQTLLNPQIFQELTENAVLRADHKLNPFSEQMLDSNITPAVESLAAKAFVMYSFAEMKFSQILPTPPSSTDYDPLSDKRLSNGSCAIEDEEDLDQGRPPSNQTLTSATTKISSATNVDTQIPAPELKKLCTESLLLYLKALTILAASMKLTSKWWYENESKNCTLKLNILVQWIRDRFNECLDKAEFLRLKLHAINTSPNSQWSDDDPVIFVEKLIYDRALDISRNAARMEMESGNYNTCELAYATSLWMLEILLDENFQFNEVYDDEYASNITSLDESDKEMIKKYISSIANRLKALKSKMV","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Kluyveromyces"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"ATG1","evidences":[{"code":"ECO:0000250","source":{"name":"UniProtKB","id":"P53104","url":"https://www.uniprot.org/uniprot/P53104"}}]},"olnNames":[{"value":"KLLA0C17160g","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15229592","url":"http://www.ncbi.nlm.nih.gov/pubmed/15229592","alternativeUrl":"https://europepmc.org/abstract/MED/15229592"}}]}]}],"alphafold_very_low_content":0.29362214199759323,"disorder_content":0.3249097472924188,"disprot_consensus":{"full":[{"start":562,"end":831,"type":"D"}],"Structural state":[{"start":562,"end":831,"type":"D"}],"Cellular component":[{"start":562,"end":831,"type":"F"}]}},{"disprot_id":"DP03729","acc":"Q8IYT8","creator":"vnugnes","date":"2022-06-08T14:37:02.026Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":9,"end":271},{"id":"PF12063","name":"Atg1-like, MIT domain 1","start":863,"end":945},{"id":"PF21127","name":"ATG1-like, MIT domain 2","start":956,"end":1029}],"gene3D":[]},"length":1036,"name":"Serine/threonine-protein kinase ULK2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":168,"end":177,"reference_id":"30782972","reference_source":"pmid","reference_html":"Conservation of structure, function and inhibitor binding in UNC-51-like kinase 1 and 2 (ULK1/2). <i> Chaikuad A, Koschade SE, Stolz A, Zivkovic K, Pohl C, Shaid S, Ren H, Lambert LJ, Cosford NDP, Brandts CH, Knapp S. </i> Biochem J, 2019","date":"2022-06-08T14:43:51.005Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_06","version":0,"cross_refs":[{"db":"PDB","id":"6QAT"}],"region_id":"DP03729r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"70726","entry_name":"hesperadin"}],"sequence_construct":"GGGSMEVVGDFEYSKRDLVGHGAFAVVFRGRHRQKTDWEVAIKSINKKNLSKSQILLGKEIKILKELQHENIVALYDVQELPNSVFLVMEYCNGGDLADYLQAKGTLSEDTIRVFLHQIAAAMRILHSKGIIHRDLKPQNILLSYANRRKSSVSGIRIKIADFGFARYLHSNMMAADLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKNRSLMPSIPRETSPYLANLLLGLLQRNQKDRMDFEAFFSHPFLEQGPV","statement":[{"text":"The lack of electron density indicates this region is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2022-06-13T09:10:24.918Z"}}],"regions_counter":1,"released":"2022_06","sequence":"MEVVGDFEYSKRDLVGHGAFAVVFRGRHRQKTDWEVAIKSINKKNLSKSQILLGKEIKILKELQHENIVALYDVQELPNSVFLVMEYCNGGDLADYLQAKGTLSEDTIRVFLHQIAAAMRILHSKGIIHRDLKPQNILLSYANRRKSSVSGIRIKIADFGFARYLHSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKNRSLMPSIPRETSPYLANLLLGLLQRNQKDRMDFEAFFSHPFLEQGPVKKSCPVPVPMYSGSVSGSSCGSSPSCRFASPPSLPDMQHIQEENLSSPPLGPPNYLQVSKDSASTSSKNSSCDTDDFVLVPHNISSDHSCDMPVGTAGRRASNEFLVCGGQCQPTVSPHSETAPIPVPTQIRNYQRIEQNLTSTASSGTNVHGSPRSAVVRRSNTSPMGFLRPGSCSPVPADTAQTVGRRLSTGSSRPYSPSPLVGTIPEQFSQCCCGHPQGHDSRSRNSSGSPVPQAQSPQSLLSGARLQSAPTLTDIYQNKQKLRKQHSDPVCPSHTGAGYSYSPQPSRPGSLGTSPTKHLGSSPRSSDWFFKTPLPTIIGSPTKTTAPFKIPKTQASSNLLALVTRHGPAEEQSKDGNEPRECAHCLLVQGSERQRAEQQSKAVFGRSVSTGKLSDQQGKTPICRHQGSTDSLNTERPMDIAPAGACGGVLAPPAGTAASSKAVLFTVGSPPHSAAAPTCTHMFLRTRTTSVGPSNSGGSLCAMSGRVCVGSPPGPGFGSSPPGAEAAPSLRYVPYGASPPSLEGLITFEAPELPEETLMEREHTDTLRHLNVMLMFTECVLDLTAMRGGNPELCTSAVSLYQIQESVVVDQISQLSKDWGRVEQLVLYMKAAQLLAASLHLAKAQIKSGKLSPSTAVKQVVKNLNERYKFCITMCKKLTEKLNRFFSDKQRFIDEINSVTAEKLIYNCAVEMVQSAALDEMFQQTEDIVYRYHKAALLLEGLSRILQDPADIENVHKYKCSIERRLSALCHSTATV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins"],"genes":[{"name":{"value":"ULK2"},"synonyms":[{"value":"KIAA0623"}]}],"alphafold_very_low_content":0.525096525096525,"disorder_content":0.009652509652509652,"disprot_consensus":{"full":[{"start":168,"end":177,"type":"D"}],"Structural state":[{"start":168,"end":177,"type":"D"}]}},{"disprot_id":"DP03730","acc":"Q13627","creator":"maspromonte","date":"2022-06-09T12:54:24.676Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":159,"end":479}],"gene3D":[]},"length":763,"name":"Dual specificity tyrosine-phosphorylation-regulated kinase 1A","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":481,"end":490,"reference_id":"30095246","reference_source":"pmid","reference_html":"Novel Scaffolds for Dual Specificity Tyrosine-Phosphorylation-Regulated Kinase (DYRK1A) Inhibitors. <i> Czarna A, Wang J, Zelencova D, Liu Y, Deng X, Choi HG, Zhang T, Zhou W, Chang JW, Kildalsen H, Seternes OM, Gray NS, Engh RA, Rothweiler U. </i> J Med Chem, 2018","date":"2022-09-02T10:22:14.063Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6EIV"},{"db":"PDB","id":"6EJ4"},{"db":"PDB","id":"6EIJ"},{"db":"PDB","id":"6EIL"},{"db":"PDB","id":"6EIP"},{"db":"PDB","id":"6EIQ"},{"db":"PDB","id":"6EIR"},{"db":"PDB","id":"6EIS"}],"region_id":"DP03730r001","statement":[{"text":"The authors described \"a DYRK1A construct comprising the kinase domain (126–490)\", however in the PDB the residues between 480-490 are missing","type":"Curator statement"}],"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":321,"end":321,"position":"Specific residue"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-02T12:46:33.673Z"}},{"start":481,"end":490,"reference_id":"27736065","reference_source":"pmid","reference_html":"Probing the ATP-Binding Pocket of Protein Kinase DYRK1A with Benzothiazole Fragment Molecules. <i> Rothweiler U, Stensen W, Brandsdal BO, Isaksson J, Leeson FA, Engh RA, Svendsen JS. </i> J Med Chem, 2016","date":"2022-09-02T11:11:03.735Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":1,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":321,"end":321,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"5A4L"},{"db":"PDB","id":"5A4E"},{"db":"PDB","id":"5A4Q"},{"db":"PDB","id":"5A4T"},{"db":"PDB","id":"5A54"}],"region_id":"DP03730r005","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-02T12:46:32.660Z"}}],"regions_counter":5,"released":"2023_06","sequence":"MHTGGETSACKPSSVRLAPSFSFHAAGLQMAGQMPHSHQYSDRRQPNISDQQVSALSYSDQIQQPLTNQVMPDIVMLQRRMPQTFRDPATAPLRKLSVDLIKTYKHINEVYYAKKKRRHQQGQGDDSSHKKERKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFEKLPDGTWNLKKTKDGKREYKPPGTRKLHNILGVETGGPGGRRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKKTADEGTNTSNSVSTSPAMEQSQSSGTTSSTSSSSGGSSGTSNSGRARSDPTHQHRHSGGHFTAAVQAMDCETHSPQVRQQFPAPLGWSGTEAPTQVTVETHPVQETTFHVAPQQNALHHHHGNSSHHHHHHHHHHHHHGQQALGNRTRPRVYNSPTNSSSTQDSMEVGHSHHSMTSLSSSTTSSSTSSSSTGNQGNQAYQNRPVAANTLDFGQNGAMDVNLTVYSNPRQETGIAGHPTYQFSANTGPAHYMTEGHLTMRQGADREESPMTGVCVQQSPVASS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"DYRK1A"},"synonyms":[{"value":"DYRK"},{"value":"MNB"},{"value":"MNBH"}]}],"dataset":["NDDs-related proteins","Condensates-related proteins"],"alphafold_very_low_content":0.4705111402359109,"disorder_content":0.01310615989515072,"disprot_consensus":{"full":[{"start":481,"end":490,"type":"D"}],"Structural state":[{"start":481,"end":490,"type":"D"}]}},{"disprot_id":"DP03731","acc":"Q9UHK0","creator":"vnugnes","date":"2022-06-09T13:02:53.528Z","features":{"pfam":[{"id":"PF10453","name":"FMR1-interacting protein 1 (NUFIP1)","start":216,"end":267}],"gene3D":[]},"length":495,"name":"Nuclear fragile X mental retardation-interacting protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":486,"end":495,"reference_id":"27594683","reference_source":"pmid","reference_html":"Structural Features of the Box C/D snoRNP Pre-assembly Process Are Conserved through Species. <i> Quinternet M, Chagot ME, Rothé B, Tiotiu D, Charpentier B, Manival X. </i> Structure, 2016","date":"2022-07-27T15:34:04.081Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":1,"region_id":"DP03731r001","statement":[{"text":"Not surprisingly, per-residue analysis revealed high T1 and T2 values for the unstructured tails of each partner (i.e., segments 84–85 and 149–155 in ZNHIT3 and segment 486–495 in NUFIP1) but also a significant increase in the α3-α4 loop of ZNHIT3.","type":"Results"}],"sequence_construct":"DIRHERNVILQCVRYIIKKDFFGLDTNSAKSKDV","cross_refs":[{"db":"PDB","id":"5L85"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-08-16T10:57:08.171Z"}}],"regions_counter":3,"released":"2022_06","sequence":"MAEPTSDFETPIGWHASPELTPTLGPLSDTAPPRDSWMFWAMLPPPPPPLTSSLPAAGSKPSSESQPPMEAQSLPGAPPPFDAQILPGAQPPFDAQSPLDSQPQPSGQPWNFHASTSWYWRQSSDRFPRHQKSFNPAVKNSYYPRKYDAKFTDFSLPPSRKQKKKKRKEPVFHFFCDTCDRGFKNQEKYDKHMSEHTKCPELDCSFTAHEKIVQFHWRNMHAPGMKKIKLDTPEEIARWREERRKNYPTLANIERKKKLKLEKEKRGAVLTTTQYGKMKGMSRHSQMAKIRSPGKNHKWKNDNSRQRAVTGSGSHLCDLKLEGPPEANADPLGVLINSDSESDKEEKPQHSVIPKEVTPALCSLMSSYGSLSGSESEPEETPIKTEADVLAENQVLDSSAPKSPSQDVKATVRNFSEAKSENRKKSFEKTNPKRKKDYHNYQTLFEPRTHHPYLLEMLLAPDIRHERNVILQCVRYIIKKDFFGLDTNSAKSKDV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Autophagy-related proteins","RNA-binding proteins"],"genes":[{"name":{"value":"NUFIP1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:8057","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8057"}}]}}],"alphafold_very_low_content":0.5656565656565656,"disorder_content":0.020202020202020204,"disprot_consensus":{"full":[{"start":486,"end":495,"type":"D"}],"Structural state":[{"start":486,"end":495,"type":"D"}]}},{"disprot_id":"DP03732","acc":"Q8NER1","creator":"rpancsa","date":"2022-06-12T08:57:10.691Z","features":{"pfam":[{"id":"PF00023","name":"Ankyrin repeat","start":249,"end":282},{"id":"PF00520","name":"Ion transport protein","start":435,"end":694},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":120,"end":230}],"gene3D":[]},"length":839,"name":"Transient receptor potential cation channel subfamily V member 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":2,"end":100,"reference_id":"35666427","reference_source":"pmid","reference_html":"Extent of intrinsic disorder and NMR chemical shift assignments of the distal N-termini from human TRPV1, TRPV2 and TRPV3 ion channels. <i> Wiedemann C, Goretzki B, Merz ZN, Tebbe F, Schmitt P, Hellmich UA. </i> Biomol NMR Assign, 2022","date":"2022-06-12T09:14:48.677Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"BMRB","id":"51353"}],"region_id":"DP03732r001","statement":[{"text":"In agreement with a predicted low overall secondary structure content, the [1H, 15N]-TROSY-HSQC-spectra of human TRPV1-IDR, hsTRPV2 and TRPV3-IDR show limited signal dispersion in the 1HN dimension (Fig. 2 A-C), indicating a similar chemical environment of all 1HN nuclei and an inherent lack of stable structural elements.","type":"Article"}],"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Figure","text":"[1H, 15N]-TROSY-HSQC spectra of 13C, 15N-labeled human TRPV1-IDR (residues 2-100) (A), TRPV2-IDR (residues 2–73) (B) and TRPV3-IDR (residues 2-119) (C) recorded at 600 MHz and 25 °C."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":7,"statements":[{"type":"Figure","text":"Human TRPV1-IDR and TRPV2-IDR were measured in 10 mM Tris-HCl pH 7, 100 mM NaCl and hsTRPV3-IDR was measured in 10 mM NaPi pH 6.2, 300 mM NaCl, 1 mM DTT."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-14T09:06:10.827Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MKKWSSTDLGAAADPLQKDTCPDPLDGDPNSRPPPAKPQLSTAKSRTRLFGKGDSEEAFPVDCPHEEGELDSCPTITVSPVITIQRPGDGPTGARLLSQDSVAASTEKTLRLYDRRSIFEAVAQNNCQDLESLLLFLQKSKKHLTDNEFKDPETGKTCLLKAMLNLHDGQNTTIPLLLEIARQTDSLKELVNASYTDSYYKGQTALHIAIERRNMALVTLLVENGADVQAAAHGDFFKKTKGRPGFYFGELPLSLAACTNQLGIVKFLLQNSWQTADISARDSVGNTVLHALVEVADNTADNTKFVTSMYNEILMLGAKLHPTLKLEELTNKKGMTPLALAAGTGKIGVLAYILQREIQEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFVKRIFYFNFLVYCLYMIIFTMAAYYRPVDGLPPFKMEKTGDYFRVTGEILSVLGGVYFFFRGIQYFLQRRPSMKTLFVDSYSEMLFFLQSLFMLATVVLYFSHLKEYVASMVFSLALGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYIVFLFGFSTAVVTLIEDGKNDSLPSESTSHRWRGPACRPPDSSYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAFRSGKLLQVGYTPDGKDDYRWCFRVDEVNWTTWNTNVGIINEDPGNCEGVKRTLSFSLRSSRVSGRHWKNFALVPLLREASARDRQSAQPEEVYLRQFSGSLKPEDAEVFKSPAASGEK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"TRPV1"},"synonyms":[{"value":"VR1"}]}],"alphafold_very_low_content":0.25148986889153757,"disorder_content":0.11799761620977355,"disprot_consensus":{"full":[{"start":2,"end":100,"type":"D"}],"Structural state":[{"start":2,"end":100,"type":"D"}]}},{"disprot_id":"DP03733","acc":"Q9Y5S1","creator":"rpancsa","date":"2022-06-12T09:01:30.776Z","features":{"pfam":[{"id":"PF00520","name":"Ion transport protein","start":399,"end":653},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":108,"end":192}],"gene3D":[]},"length":764,"name":"Transient receptor potential cation channel subfamily V member 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":2,"end":73,"reference_id":"35666427","reference_source":"pmid","reference_html":"Extent of intrinsic disorder and NMR chemical shift assignments of the distal N-termini from human TRPV1, TRPV2 and TRPV3 ion channels. <i> Wiedemann C, Goretzki B, Merz ZN, Tebbe F, Schmitt P, Hellmich UA. </i> Biomol NMR Assign, 2022","date":"2022-06-12T09:16:17.565Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"BMRB","id":"51354"}],"region_id":"DP03733r001","statement":[{"text":"In agreement with a predicted low overall secondary structure content, the [1H, 15N]-TROSY-HSQC-spectra of human TRPV1-IDR, hsTRPV2 and TRPV3-IDR show limited signal dispersion in the 1HN dimension (Fig. 2 A-C), indicating a similar chemical environment of all 1HN nuclei and an inherent lack of stable structural elements.","type":"Article"}],"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Figure","text":"[1H, 15N]-TROSY-HSQC spectra of 13C, 15N-labeled human TRPV1-IDR (residues 2-100) (A), TRPV2-IDR (residues 2–73) (B) and TRPV3-IDR (residues 2-119) (C) recorded at 600 MHz and 25 °C."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":7,"statements":[{"type":"Figure","text":"Human TRPV1-IDR and TRPV2-IDR were measured in 10 mM Tris-HCl pH 7, 100 mM NaCl and hsTRPV3-IDR was measured in 10 mM NaPi pH 6.2, 300 mM NaCl, 1 mM DTT."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-14T09:08:11.399Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MTSPSSSPVFRLETLDGGQEDGSEADRGKLDFGSGLPPMESQFQGEDRKFAPQIRVNLNYRKGTGASQPDPNRFDRDRLFNAVSRGVPEDLAGLPEYLSKTSKYLTDSEYTEGSTGKTCLMKAVLNLKDGVNACILPLLQIDRDSGNPQPLVNAQCTDDYYRGHSALHIAIEKRSLQCVKLLVENGANVHARACGRFFQKGQGTCFYFGELPLSLAACTKQWDVVSYLLENPHQPASLQATDSQGNTVLHALVMISDNSAENIALVTSMYDGLLQAGARLCPTVQLEDIRNLQDLTPLKLAAKEGKIEIFRHILQREFSGLSHLSRKFTEWCYGPVRVSLYDLASVDSCEENSVLEIIAFHCKSPHRHRMVVLEPLNKLLQAKWDLLIPKFFLNFLCNLIYMFIFTAVAYHQPTLKKQAAPHLKAEVGNSMLLTGHILILLGGIYLLVGQLWYFWRRHVFIWISFIDSYFEILFLFQALLTVVSQVLCFLAIEWYLPLLVSALVLGWLNLLYYTRGFQHTGIYSVMIQKVILRDLLRFLLIYLVFLFGFAVALVSLSQEAWRPEAPTGPNATESVQPMEGQEDEGNGAQYRGILEASLELFKFTIGMGELAFQEQLHFRGMVLLLLLAYVLLTYILLLNMLIALMSETVNSVATDSWSIWKLQKAISVLEMENGYWWCRKKQRAGVMLTVGTKPDGSPDERWCFRVEEVNWASWEQTLPTLCEDPSGAGVPRTLENPVLASPPKEDEDGASEENYVPVQLLQSN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"TRPV2"},"synonyms":[{"value":"VRL"}]}],"alphafold_very_low_content":0.13481675392670156,"disorder_content":0.09424083769633508,"disprot_consensus":{"full":[{"start":2,"end":73,"type":"D"}],"Structural state":[{"start":2,"end":73,"type":"D"}]}},{"disprot_id":"DP03734","acc":"Q8NET8","creator":"rpancsa","date":"2022-06-12T09:05:13.164Z","features":{"pfam":[{"id":"PF00023","name":"Ankyrin repeat","start":262,"end":293},{"id":"PF00023","name":"Ankyrin repeat","start":340,"end":362},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":125,"end":243},{"id":"PF23317","name":"Calcium channel YVC1-like, C-terminal","start":519,"end":703}],"gene3D":[]},"length":790,"name":"Transient receptor potential cation channel subfamily V member 3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":2,"end":119,"reference_id":"35666427","reference_source":"pmid","reference_html":"Extent of intrinsic disorder and NMR chemical shift assignments of the distal N-termini from human TRPV1, TRPV2 and TRPV3 ion channels. <i> Wiedemann C, Goretzki B, Merz ZN, Tebbe F, Schmitt P, Hellmich UA. </i> Biomol NMR Assign, 2022","date":"2022-06-12T09:09:59.013Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Figure","text":"[1H, 15N]-TROSY-HSQC spectra of 13C, 15N-labeled human TRPV1-IDR (residues 2-100) (A), TRPV2-IDR (residues 2–73) (B) and TRPV3-IDR (residues 2-119) (C) recorded at 600 MHz and 25 °C."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.2,"statements":[{"type":"Figure","text":"Human TRPV1-IDR and TRPV2-IDR were measured in 10 mM Tris-HCl pH 7, 100 mM NaCl and hsTRPV3-IDR was measured in 10 mM NaPi pH 6.2, 300 mM NaCl, 1 mM DTT."}]}],"cross_refs":[{"db":"BMRB","id":"51355"}],"region_id":"DP03734r001","statement":[{"text":"In agreement with a predicted low overall secondary structure content, the [1H, 15N]-TROSY-HSQC-spectra of human TRPV1-IDR, hsTRPV2 and TRPV3-IDR show limited signal dispersion in the 1HN dimension (Fig. 2 A-C), indicating a similar chemical environment of all 1HN nuclei and an inherent lack of stable structural elements.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-14T09:09:56.241Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MKAHPKEMVPLMGKRVAAPSGNPAILPEKRPAEITPTKKSAHFFLEIEGFEPNPTVAKTSPPVFSKPMDSNIRQCISGNCDDMDSPQSPQDDVTETPSNPNSPSAQLAKEEQRRKKRRLKKRIFAAVSEGCVEELVELLVELQELCRRRHDEDVPDFLMHKLTASDTGKTCLMKALLNINPNTKEIVRILLAFAEENDILGRFINAEYTEEAYEGQTALNIAIERRQGDIAALLIAAGADVNAHAKGAFFNPKYQHEGFYFGETPLALAACTNQPEIVQLLMEHEQTDITSRDSRGNNILHALVTVAEDFKTQNDFVKRMYDMILLRSGNWELETTRNNDGLTPLQLAAKMGKAEILKYILSREIKEKRLRSLSRKFTDWAYGPVSSSLYDLTNVDTTTDNSVLEITVYNTNIDNRHEMLTLEPLHTLLHMKWKKFAKHMFFLSFCFYFFYNITLTLVSYYRPREEEAIPHPLALTHKMGWLQLLGRMFVLIWAMCISVKEGIAIFLLRPSDLQSILSDAWFHFVFFIQAVLVILSVFLYLFAYKEYLACLVLAMALGWANMLYYTRGFQSMGMYSVMIQKVILHDVLKFLFVYIVFLLGFGVALASLIEKCPKDNKDCSSYGSFSDAVLELFKLTIGLGDLNIQQNSKYPILFLFLLITYVILTFVLLLNMLIALMGETVENVSKESERIWRLQRARTILEFEKMLPEWLRSRFRMGELCKVAEDDFRLCLRINEVKWTEWKTHVSFLNEDPGPVRRTDFNKIQDSSRNNSKTTLNAFEEVEEFPETSV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"TRPV3"}}],"alphafold_very_low_content":0.17341772151898735,"disorder_content":0.14936708860759493,"disprot_consensus":{"full":[{"start":2,"end":119,"type":"D"}],"Structural state":[{"start":2,"end":119,"type":"D"}]}},{"disprot_id":"DP03735","acc":"Q9ET78","creator":"rpancsa","date":"2022-06-12T09:24:59.069Z","features":{"pfam":[{"id":"PF02493","name":"MORN repeat","start":14,"end":34},{"id":"PF02493","name":"MORN repeat","start":38,"end":59},{"id":"PF02493","name":"MORN repeat","start":60,"end":76},{"id":"PF02493","name":"MORN repeat","start":82,"end":101},{"id":"PF02493","name":"MORN repeat","start":106,"end":128},{"id":"PF02493","name":"MORN repeat","start":129,"end":146},{"id":"PF02493","name":"MORN repeat","start":285,"end":306},{"id":"PF02493","name":"MORN repeat","start":308,"end":330}],"gene3D":[]},"length":696,"name":"Junctophilin-2","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":331,"end":413,"reference_id":"35665900","reference_source":"pmid","reference_html":"NMR resonance assignments of the DNA binding domain of mouse Junctophilin-2. <i> Yu L, Hall DD, Zhao W, Song LS. </i> Biomol NMR Assign, 2022","date":"2022-06-12T09:32:19.770Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":20,"statements":[{"type":"Article","text":"NMR spectra were acquired on a Bruker Avance Neo 600 MHz NMR spectrometer at 20 °C using 0.8 mM uniformly [13C,15N]-labeled mouse JP2 DNA binding domain in a buffer composed of 20 mM BisTris, 40 mM NaCl, and pH 6.0 in 90% H2O/10% D2O."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6,"statements":[{"type":"Article","text":"NMR spectra were acquired on a Bruker Avance Neo 600 MHz NMR spectrometer at 20 °C using 0.8 mM uniformly [13C,15N]-labeled mouse JP2 DNA binding domain in a buffer composed of 20 mM BisTris, 40 mM NaCl, and pH 6.0 in 90% H2O/10% D2O."}]}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Article","text":"It is noted that our protein construct contains an N-terminal 6xHis-tag (MGSSHHHHHHSSG, 13 residues numbered as 318 to 330), mouse JP2 DNA-binding domain (residues 331 to 413), and a C-terminal Strep tag II (WSHPQFEK, 8 residues numbered as 414 to 421)."}]},{"term_id":"MI:0988","term_name":"STREP","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Article","text":"It is noted that our protein construct contains an N-terminal 6xHis-tag (MGSSHHHHHHSSG, 13 residues numbered as 318 to 330), mouse JP2 DNA-binding domain (residues 331 to 413), and a C-terminal Strep tag II (WSHPQFEK, 8 residues numbered as 414 to 421)."}]}],"cross_refs":[{"db":"BMRB","id":"51405"}],"region_id":"DP03735r001","sequence_construct":"MGSSHHHHHHSSGEEGKYRHNVLVKGTKRRVLPLKSSKVRQKVEHGVEGAQRAAAIARQKAEIAASRTSHAKAKAEAAEQAALAANQESNIARTLAWSHPQFEK","statement":[{"text":"The 15N/1H HSQC spectrum of JP2 DNA binding domain is shown in Fig. 1. Clearly, the cross-peaks in the HSQC spectrum are not well dispersed as typically observed for a well folded protein. Instead, the cross-peaks are clustered in a narrow strip with the backbone amide NH protons resonated in a narrow 1H range from 7.89 to 8.73 ppm, indicating that this JP2 domain is an intrinsically disordered protein (IDP).","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-14T09:12:38.455Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MSGGRFDFDDGGAYCGGWEGGKAHGHGLCTGPKGQGEYSGSWNFGFEVAGVYTWPSGNTFEGYWSQGKRHGLGIETKGRWLYKGEWTHGFKGRYGIRQSTNSGAKYEGTWNNGLQDGYGTETYADGGTYQGQFTNGMRHGYGVRQSVPYGMAVVVRSPLRTSLSSLRSEHSNGTVAPDSPAADGPMLPSPPVPRGGFALTLLATAEAARPQGLFTRGTLLGRLRRSESRTSLGSQRSRLSFLKSELSSGASDAASTGSLAEGAEGPDDAAAPFDADIDATTTETYMGEWKNDKRSGFGVSERSSGLRYEGEWLDNLRHGYGRTTLPDGHREEGKYRHNVLVKGTKRRVLPLKSSKVRQKVEHGVEGAQRAAAIARQKAEIAASRTSHAKAKAEAAEQAALAANQESNIARTLAKELAPDFYQPGPEYQKRRLLQEILENSESLLEPPERGLGTGLPERPRESPQLHERETPQPEGGPPSPAGTPPQPKRPRPGASKDGLLSPGSWNGEPGGEGSRPATPSDGAGRRSPARPASEHMAIEALQPPPAPSQEPEVAMYRGYHSYAVRTGPPEPPPLEDEQEPEPEPEPEVRRSDSAPPSPVSATVPEEEPPAPRSPVPAKQATLEPKPIVPKAEPKAKARKTEARGLSKAGAKKKGRKEVAQAKEAEVEVEEVPNTVLICMVILLNIGLAILFVHLLT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"genes":[{"name":{"value":"Jph2","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:1891496","url":"http://www.informatics.jax.org/marker/MGI:1891496"}}]},"synonyms":[{"value":"Jp2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10949023","url":"http://www.ncbi.nlm.nih.gov/pubmed/10949023","alternativeUrl":"https://europepmc.org/abstract/MED/10949023"}}]}]}],"alphafold_very_low_content":0.4755747126436782,"disorder_content":0.11925287356321838,"disprot_consensus":{"full":[{"start":331,"end":413,"type":"D"}],"Structural state":[{"start":331,"end":413,"type":"D"}]}},{"disprot_id":"DP03737","acc":"Q8NE35-2","creator":"rpancsa","date":"2022-06-12T10:08:39.725Z","features":{"pfam":[],"gene3D":[]},"length":684,"name":"Isoform 2 of Cytoplasmic polyadenylation element-binding protein 3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":426,"reference_id":"35658951","reference_source":"pmid","reference_html":"Conformational dynamics in the disordered region of human CPEB3 linked to memory consolidation. <i> Ramírez de Mingo D, Pantoja-Uceda D, Hervás R, Carrión-Vázquez M, Laurents DV. </i> BMC Biol, 2022","date":"2022-06-12T10:12:07.101Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03737r001","statement":[{"text":"The far UV CD spectra of the hCPEB3 IDR also shows the hallmarks of a disordered protein, namely a minimum near 200 nm [27]. No spectral features indicative of α-helix and β-sheet; namely, minima at 208, 218, or 222 nm and no maximum at 195 nm, are evident.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-14T09:18:38.792Z"}},{"start":1,"end":426,"reference_id":"35658951","reference_source":"pmid","reference_html":"Conformational dynamics in the disordered region of human CPEB3 linked to memory consolidation. <i> Ramírez de Mingo D, Pantoja-Uceda D, Hervás R, Carrión-Vázquez M, Laurents DV. </i> BMC Biol, 2022","date":"2022-06-12T10:14:29.882Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03737r002","statement":[{"text":"Its fluorescence emission spectra, recorded at temperatures ranging from 2 to 70 °C, show emission maximum > 350 nm. This is consistent with its six Trp residues being solvent exposed and not buried in the hydrophobic core of a folded domain.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-14T09:18:39.683Z"}},{"start":1,"end":426,"reference_id":"35658951","reference_source":"pmid","reference_html":"Conformational dynamics in the disordered region of human CPEB3 linked to memory consolidation. <i> Ramírez de Mingo D, Pantoja-Uceda D, Hervás R, Carrión-Vázquez M, Laurents DV. </i> BMC Biol, 2022","date":"2022-06-12T10:18:08.711Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03737r003","statement":[{"text":"The 1D 1H and 2D 1H-1H NOESY spectra show 1H signals clustered into narrow bands near the values observed for short, unstructured peptides.","type":"Results"},{"text":"2D 1H-1H NOESY spectrum of the hCPEB3 IDR recorded at 25 ºC showing the 1HN crosspeak region.  The small chemical shift dispersion in 1HN (8.6 to 7.9 ppm) is a typical feature of disordered and unfolded proteins [27].","type":"Supplementary material"}],"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Supplementary material","text":"2D 1H-1H NOESY spectrum of the hCPEB3 IDR recorded at 25 ºC showing the 1HN crosspeak region.  The small chemical shift dispersion in 1HN (8.6 to 7.9 ppm) is a typical feature of disordered and unfolded proteins [27]."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-06-14T09:18:40.842Z"}}],"regions_counter":3,"released":"2023_12","sequence":"MQDDLLMDKSKTQPQPQQQQRQQQQPQPESSVSEAPSTPLSSETPKPEENSAVPALSPAAAPPAPNGPDKMQMESPLLPGLSFHQPPQQPPPPQEPAAPGASLSPSFGSTWSTGTTNAVEDSFFQGITPVNGTMLFQNFPHHVNPVFGGTFSPQIGLAQTQHHQQPPPPAPAPQPAQPAQPPQAQPPQQRRSPASPSQAPYAQRSAAAAYGHQPIMTSKPSSSSAVAAAAAAAAASSASSSWNTHQSVNAAWSAPSNPWGGLQAGRDPRRAVGVGVGVGVGVPSPLNPISPLKKPFSSNVIAPPKFPRAAPLTSKSWMEDNAFRTDNGNNLLPFQDRSRPYDTFNLHSLENSLMDMIRTDHEPLKGRMGINFHHPGTDNIMALNSRSSLFPFEDAFLDDSHGDQALSSGLSSPTRCQNGERVERYSRKVFVGGLPPDIDEDEITASFRRFGPLVVDWPHKAESKSYFPPKGYAFLLFQEESSVQALIDACLEEDGKLYLCVSSPTIKDKPVQIRPWNLSDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHNDIDKRVEVKPYVLDDQMCDECQGTRCGGKFAPFFCANVTCLQYYCEYCWASIHSRAGREFHKPLVKEGGDRPRHVPFRWS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"CPEB3"},"synonyms":[{"value":"KIAA0940"}]}],"disorder_content":0.6228070175438597,"disprot_consensus":{"full":[{"start":1,"end":426,"type":"D"}],"Structural state":[{"start":1,"end":426,"type":"D"}]}},{"disprot_id":"DP03739","acc":"P24588","creator":"fquaglia","date":"2022-06-15T09:05:58.506Z","features":{"pfam":[{"id":"PF03832","name":"WSK motif","start":77,"end":101}],"gene3D":[]},"length":427,"name":"A-kinase anchor protein 5","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":300,"end":427,"reference_id":"35697294","reference_source":"pmid","reference_html":"Hidden multivalency in phosphatase recruitment by a disordered AKAP scaffold.  <i> Watson M, Almeida TB, Ray A, Hanack C, Elston R, Btesh J, McNaughton PA, Stott K. </i> J Mol Biol, 2022","date":"2022-06-15T09:08:51.521Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03739r001","statement":[{"text":"AKAP5 is an IDP with a well-characterised PxIxIT SLiM that anchors Calcineurin.","type":"Article"},{"text":"The AKAP5c scaffold is highly disordered and monomeric","type":"Results"},{"text":"Two spectroscopic techniques were deployed to assess and delineate regions of nascent structure and to probe the backbone dynamics in AKAP5c: nuclear magnetic resonance (NMR) and circular dichroism (CD). The 15N-HSQC spectrum (Fig. 1b) displays the low 1HN chemical-shift dispersion (0.7 ppm) and narrow line widths typical of disordered proteins.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-16T15:57:18.471Z"}},{"start":300,"end":427,"reference_id":"35697294","reference_source":"pmid","reference_html":"Hidden multivalency in phosphatase recruitment by a disordered AKAP scaffold.  <i> Watson M, Almeida TB, Ray A, Hanack C, Elston R, Btesh J, McNaughton PA, Stott K. </i> J Mol Biol, 2022","date":"2022-06-15T09:09:17.038Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03739r002","statement":[{"text":"AKAP5 is an IDP with a well-characterised PxIxIT SLiM that anchors Calcineurin.","type":"Article"},{"text":"The AKAP5c scaffold is highly disordered and monomeric","type":"Results"},{"text":"CD spectroscopy also showed AKAP5c to be predominantly disordered (Fig. 1d): the signature large negative ellipticity at 200 nm was dominant, and although there were indications of some secondary structure (as evidenced by the weak shoulder at 222 nm), this is likely to be transiently populated given the results from NMR.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-16T15:54:16.284Z"}},{"start":404,"end":413,"reference_id":"35697294","reference_source":"pmid","reference_html":"Hidden multivalency in phosphatase recruitment by a disordered AKAP scaffold.  <i> Watson M, Almeida TB, Ray A, Hanack C, Elston R, Btesh J, McNaughton PA, Stott K. </i> J Mol Biol, 2022","date":"2022-06-15T10:35:49.819Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q08209","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63098","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP03739r003","statement":[{"text":"Three distinct sections with pronounced dips in intensity were seen, 361QFLIS365, 390TLLIET395 and 404IQLSIEQLVN413, which we termed secondary sites 1, 2 and 3, respectively. Binding to these sites therefore does not depend on the presence of the PIAIIIT site.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Pro337_Thr343del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Given the involvement of PxIxIT-flanking and distal regions of AKAP5c in binding to Calcineurin, we investigated binding to AKAP5c in which the PIAIIIT site had been deleted: AKAP5cΔPIAIIIT."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-16T17:25:38.149Z"}},{"start":390,"end":395,"reference_id":"35697294","reference_source":"pmid","reference_html":"Hidden multivalency in phosphatase recruitment by a disordered AKAP scaffold.  <i> Watson M, Almeida TB, Ray A, Hanack C, Elston R, Btesh J, McNaughton PA, Stott K. </i> J Mol Biol, 2022","date":"2022-06-15T10:34:27.973Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q08209","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63098","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP03739r005","statement":[{"text":"Three distinct sections with pronounced dips in intensity were seen, 361QFLIS365, 390TLLIET395 and 404IQLSIEQLVN413, which we termed secondary sites 1, 2 and 3, respectively. Binding to these sites therefore does not depend on the presence of the PIAIIIT site.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Pro337_Thr343del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Given the involvement of PxIxIT-flanking and distal regions of AKAP5c in binding to Calcineurin, we investigated binding to AKAP5c in which the PIAIIIT site had been deleted: AKAP5cΔPIAIIIT."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-16T17:25:47.443Z"}},{"start":361,"end":365,"reference_id":"35697294","reference_source":"pmid","reference_html":"Hidden multivalency in phosphatase recruitment by a disordered AKAP scaffold.  <i> Watson M, Almeida TB, Ray A, Hanack C, Elston R, Btesh J, McNaughton PA, Stott K. </i> J Mol Biol, 2022","date":"2022-06-15T10:33:22.253Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q08209","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63098","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP03739r006","statement":[{"text":"Three distinct sections with pronounced dips in intensity were seen, 361QFLIS365, 390TLLIET395 and 404IQLSIEQLVN413, which we termed secondary sites 1, 2 and 3, respectively. Binding to these sites therefore does not depend on the presence of the PIAIIIT site.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Pro337_Thr343del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Given the involvement of PxIxIT-flanking and distal regions of AKAP5c in binding to Calcineurin, we investigated binding to AKAP5c in which the PIAIIIT site had been deleted: AKAP5cΔPIAIIIT."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-16T17:25:51.240Z"}},{"start":371,"end":375,"reference_id":"35697294","reference_source":"pmid","reference_html":"Hidden multivalency in phosphatase recruitment by a disordered AKAP scaffold.  <i> Watson M, Almeida TB, Ray A, Hanack C, Elston R, Btesh J, McNaughton PA, Stott K. </i> J Mol Biol, 2022","date":"2022-06-15T10:10:38.909Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q08209","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63098","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP03739r008","statement":[{"text":"A small extra region of non-PIAIIIT interaction was apparent in AKAPILVF->SA in the absence of the secondary sites: 371VGVFA375, which contains three bulky hydrophobic residues but no isoleucine, and there were also weaker dips corresponding to regions containing just one or two hydrophobic residues: 378NGFED382, 386EQYET390, 398SLVKN402 and 424NLLQ427 (shown by asterisks in Fig. 5b). We hereon refer to these as ‘mini-SLiMs’ in order to differentiate them from the primary and secondary sites.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe362Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Therefore, a further AKAP mutant was tested: AKAPILVF->SA, in which the PIAIIIT site was present, but all the hydrophobic I, L, V and F residues in the three secondary sites were mutated to S or A to give 361QASAS365, 390TASAET395 and 404AQSSAEQSAN413."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu363Ser","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Therefore, a further AKAP mutant was tested: AKAPILVF->SA, in which the PIAIIIT site was present, but all the hydrophobic I, L, V and F residues in the three secondary sites were mutated to S or A to give 361QASAS365, 390TASAET395 and 404AQSSAEQSAN413."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile364Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Therefore, a further AKAP mutant was tested: AKAPILVF->SA, in which the PIAIIIT site was present, but all the hydrophobic I, L, V and F residues in the three secondary sites were mutated to S or A to give 361QASAS365, 390TASAET395 and 404AQSSAEQSAN413."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu391Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Therefore, a further AKAP mutant was tested: AKAPILVF->SA, in which the PIAIIIT site was present, but all the hydrophobic I, L, V and F residues in the three secondary sites were mutated to S or A to give 361QASAS365, 390TASAET395 and 404AQSSAEQSAN413."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu392Ser","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Therefore, a further AKAP mutant was tested: AKAPILVF->SA, in which the PIAIIIT site was present, but all the hydrophobic I, L, V and F residues in the three secondary sites were mutated to S or A to give 361QASAS365, 390TASAET395 and 404AQSSAEQSAN413."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile393Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Therefore, a further AKAP mutant was tested: AKAPILVF->SA, in which the PIAIIIT site was present, but all the hydrophobic I, L, V and F residues in the three secondary sites were mutated to S or A to give 361QASAS365, 390TASAET395 and 404AQSSAEQSAN413."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile404Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Therefore, a further AKAP mutant was tested: AKAPILVF->SA, in which the PIAIIIT site was present, but all the hydrophobic I, L, V and F residues in the three secondary sites were mutated to S or A to give 361QASAS365, 390TASAET395 and 404AQSSAEQSAN413."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu406Ser","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Therefore, a further AKAP mutant was tested: AKAPILVF->SA, in which the PIAIIIT site was present, but all the hydrophobic I, L, V and F residues in the three secondary sites were mutated to S or A to give 361QASAS365, 390TASAET395 and 404AQSSAEQSAN413."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile408Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Therefore, a further AKAP mutant was tested: AKAPILVF->SA, in which the PIAIIIT site was present, but all the hydrophobic I, L, V and F residues in the three secondary sites were mutated to S or A to give 361QASAS365, 390TASAET395 and 404AQSSAEQSAN413."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu411Ser","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Therefore, a further AKAP mutant was tested: AKAPILVF->SA, in which the PIAIIIT site was present, but all the hydrophobic I, L, V and F residues in the three secondary sites were mutated to S or A to give 361QASAS365, 390TASAET395 and 404AQSSAEQSAN413."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val412Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Therefore, a further AKAP mutant was tested: AKAPILVF->SA, in which the PIAIIIT site was present, but all the hydrophobic I, L, V and F residues in the three secondary sites were mutated to S or A to give 361QASAS365, 390TASAET395 and 404AQSSAEQSAN413."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-16T17:26:08.577Z"}},{"start":337,"end":343,"reference_id":"35697294","reference_source":"pmid","reference_html":"Hidden multivalency in phosphatase recruitment by a disordered AKAP scaffold.  <i> Watson M, Almeida TB, Ray A, Hanack C, Elston R, Btesh J, McNaughton PA, Stott K. </i> J Mol Biol, 2022","date":"2022-06-15T10:45:30.170Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q08209","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63098","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP03739r009","statement":[{"text":"The Calcineurin anchoring site in AKAP5c is at 337PIAIIIT343, a near-consensus PxIxIT SLiM [19], [20], in which 338I takes the position of the consensus proline.","type":"Results"},{"text":"To investigate the involvement of more distal flanking regions, we titrated Calcineurin into 15N-labelled AKAP5c and followed binding by 15N HSQC (Fig. 2a). Many peaks showed a progressive decrease in intensity. At one molar equivalent, the reductions were significant, including those expected from residues 338IAIIIT343 (shown boxed).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-16T17:26:33.034Z"}},{"start":300,"end":425,"reference_id":"35697294","reference_source":"pmid","reference_html":"Hidden multivalency in phosphatase recruitment by a disordered AKAP scaffold.  <i> Watson M, Almeida TB, Ray A, Hanack C, Elston R, Btesh J, McNaughton PA, Stott K. </i> J Mol Biol, 2022","date":"2022-06-21T13:54:33.722Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q08209","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63098","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP03739r010","statement":[{"text":"Nevertheless, the trend in apparent Kd is clear: AKAP5c binds Calcineurin about twice as tightly compared to AKAP5cILVF->SA, (Kd ∼0.3 vs 0.6 μM), and both PIAIIIT-containing AKAP constructs bind Calcineurin with at least ten-fold higher affinity than AKAP5cΔPIAIIIT, which has a Kd of ∼ 10 μM. Estimation of the total surface capacity for Calcineurin (Rmax) is also instructive as it gives information on the stoichiometry of binding under saturating conditions. From extrapolation of the binding curves, it appears that AKAP5c can accommodate significantly more Calcineurin than AKAP5cILVF->SA (62 vs 42 RU; Fig. 6d). The secondary sites appear to account for at least some of this ‘extra’ capacity, since Rmax for AKAP5cΔPIAIIIT is (very approximately) 12 RU.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-23T13:37:22.013Z"}},{"start":337,"end":343,"reference_id":"35697294","reference_source":"pmid","reference_html":"Hidden multivalency in phosphatase recruitment by a disordered AKAP scaffold.  <i> Watson M, Almeida TB, Ray A, Hanack C, Elston R, Btesh J, McNaughton PA, Stott K. </i> J Mol Biol, 2022","date":"2022-06-15T10:52:49.589Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q08209","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63098","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP03739r011","statement":[{"text":"Binding was also investigated by isothermal titration calorimetry (ITC). Titration of AKAP5c and AKAP5cILVF->SA into Calcineurin gave clear sigmoidal binding curves (Fig. 6e). Low heats prevented detection of binding to AKAP5cΔPIAIIIT (not shown), presumably due to insufficient binding at the attainable concentrations of free Calcineurin or small ΔH, or both.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-16T17:18:34.070Z"}},{"start":390,"end":417,"reference_id":"35697294","reference_source":"pmid","reference_html":"Hidden multivalency in phosphatase recruitment by a disordered AKAP scaffold. <i> Watson M, Almeida TB, Ray A, Hanack C, Elston R, Btesh J, McNaughton PA, Stott K. </i> J Mol Biol, 2022","date":"2022-06-21T13:53:51.823Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005516","term_name":"calmodulin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","region_id":"DP03739r012","statement":[{"text":"However, on addition of Calmodulin, while no further changes to PIAIIIT were observed, some non-PIAIIIT peaks in the region 390-417 showed an additional loss in intensity over that induced by Calcineurin (Fig. 3b), and in addition, were observed to shift (Fig. 3c&d), indicative of a faster exchange regime and weaker binding than to Calcineurin. In order to establish whether these changes were Calcineurin-dependent, a further titration was performed in which Ca2+ and Calmodulin were added directly to AKAP5c in the absence of Calcineurin (Fig. 3c&d). A similar pattern of chemical shift changes was seen for 390-417, indicating that they result from direct binding to Calmodulin.","type":"Results"}],"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-06-23T13:37:07.684Z"}}],"regions_counter":12,"released":"2023_12","sequence":"METTISEIHVENKDEKRSAEGSPGAERQKEKASMLCFKRRKKAAKALKPKAGSEAADVARKCPQEAGASDQPEPTRGAWASLKRLVTRRKRSESSKQQKPLEGEMQPAINAEDADLSKKKAKSRLKIPCIKFPRGPKRSNHSKIIEDSDCSIKVQEEAEILDIQTQTPLNDQATKAKSTQDLSEGISRKDGDEVCESNVSNSTTSGEKVISVELGLDNGHSAIQTGTLILEEIETIKEKQDVQPQQASPLETSETDHQQPVLSDVPPLPAIPDQQIVEEASNSTLESAPNGKDYESTEIVAEETKPKDTELSQESDFKENGITEEKSKSEESKRMEPIAIIITDTEISEFDVTKSKNVPKQFLISAENEQVGVFANDNGFEDRTSEQYETLLIETASSLVKNAIQLSIEQLVNEMASDDNKINNLLQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"AKAP5"},"synonyms":[{"value":"AKAP79"}]}],"alphafold_very_low_content":0.5339578454332553,"dataset":["Stress response proteins"],"disorder_content":0.2997658079625293,"disprot_consensus":{"full":[{"start":300,"end":427,"type":"D"}],"Structural state":[{"start":300,"end":427,"type":"D"}],"Molecular function":[{"start":300,"end":425,"type":"F"}]}},{"disprot_id":"DP03740","acc":"Q9C6B8","creator":"fquaglia","date":"2022-06-15T11:03:48.859Z","features":{"pfam":[{"id":"PF03547","name":"Membrane transport protein","start":9,"end":617}],"gene3D":[]},"length":622,"name":"Auxin efflux carrier component 1","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":289,"end":451,"reference_id":"35683031","reference_source":"pmid","reference_html":"The Hydrophilic Loop of <i>Arabidopsis</i> PIN1 Auxin Efflux Carrier Harbors Hallmarks of an Intrinsically Disordered Protein. <i> Bilanovičová V, Rýdza N, Koczka L, Hess M, Feraru E, Friml J, Nodzyński T. </i> Int J Mol Sci, 2022","date":"2022-06-15T11:12:41.277Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"E. coli strain BL21 (DE3) was transformed with pET28a (Abcam, Cambridge, UK) vector encoding wild-type sequence of PIN1–HL, amino acids 289–451 with C-terminal 6xHis."}]}],"region_id":"DP03740r001","statement":[{"text":"The measured spectra of PIN1 HL–1 (Figure 1C) reached the first minimum at 229 nm, followed by negative maxima at 220 nm. Later, up to 200 nm, the signal was only decreasing. When compared with the control measurement of poly–L–lysine, which at pH seven is completely unstructured (Figure 1B, black line), the spectral curves of PIN1 HL–1 and control do not overlap, indicating that the HL is not completely unstructured. What is more, the PIN1 HL–1 spectrum corresponds neither to the spectra of poly–L–Lys in the α–helical nor in the β-sheet state (Figure 1B, red and blue lines, respectively), pointing out that PIN1 HL–1 cannot be defined as completely structured either. Unfortunately, the CD cannot provide precise structural data, only a gross composition with the share of alpha, beta, and unstructured regions without determining their exact locations. Therefore, we decided to zoom in on particular areas testing shorter fragments also outside the HL–1 to get more complete coverage of the whole PIN1 HL.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-08-01T19:02:18.104Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MITAADFYHVMTAMVPLYVAMILAYGSVKWWKIFTPDQCSGINRFVALFAVPLLSFHFIAANNPYAMNLRFLAADSLQKVIVLSLLFLWCKLSRNGSLDWTITLFSLSTLPNTLVMGIPLLKGMYGNFSGDLMVQIVVLQCIIWYTLMLFLFEYRGAKLLISEQFPDTAGSIVSIHVDSDIMSLDGRQPLETEAEIKEDGKLHVTVRRSNASRSDIYSRRSQGLSATPRPSNLTNAEIYSLQSSRNPTPRGSSFNHTDFYSMMASGGGRNSNFGPGEAVFGSKGPTPRPSNYEEDGGPAKPTAAGTAAGAGRFHYQSGGSGGGGGAHYPAPNPGMFSPNTGGGGGTAAKGNAPVVGGKRQDGNGRDLHMFVWSSSASPVSDVFGGGGGNHHADYSTATNDHQKDVKISVPQGNSNDNQYVEREEFSFGNKDDDSKVLATDGGNNISNKTTQAKVMPPTSVMTRLILIMVWRKLIRNPNSYSSLFGITWSLISFKWNIEMPALIAKSISILSDAGLGMAMFSLGLFMALNPRIIACGNRRAAFAAAMRFVVGPAVMLVASYAVGLRGVLLHVAIIQAALPQGIVPFVFAKEYNVHPDILSTAVIFGMLIALPITLLYYILLGL","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"genes":[{"name":{"value":"PIN1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9856939","url":"http://www.ncbi.nlm.nih.gov/pubmed/9856939","alternativeUrl":"https://europepmc.org/abstract/MED/9856939"}}]},"orfNames":[{"value":"F6D5.2","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAG51807.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAG51807.1"}}]}],"olnNames":[{"value":"At1g73590","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT1G73590","url":""}}]}]}],"alphafold_very_low_content":0.387459807073955,"dataset":["Stress response proteins"],"disorder_content":0.2620578778135048,"disprot_consensus":{"full":[{"start":289,"end":451,"type":"D"}],"Structural state":[{"start":289,"end":451,"type":"D"}]}},{"disprot_id":"DP03741","acc":"P03300","creator":"cpintado","date":"2022-06-15T13:32:06.636Z","features":{"pfam":[{"id":"PF00073","name":"picornavirus capsid protein","start":93,"end":308},{"id":"PF00073","name":"picornavirus capsid protein","start":370,"end":529},{"id":"PF00073","name":"picornavirus capsid protein","start":637,"end":799},{"id":"PF00548","name":"3C cysteine protease (picornain 3C)","start":1566,"end":1731},{"id":"PF00680","name":"Viral RNA-dependent RNA polymerase","start":1775,"end":2185},{"id":"PF00910","name":"RNA helicase","start":1253,"end":1350},{"id":"PF00947","name":"Picornavirus core protein 2A","start":899,"end":1025},{"id":"PF01552","name":"Picornavirus 2B protein","start":1030,"end":1128},{"id":"PF02226","name":"Picornavirus coat protein (VP4)","start":2,"end":69},{"id":"PF08727","name":"Poliovirus 3A protein like","start":1457,"end":1515}],"gene3D":[]},"length":2209,"name":"Genome polyprotein","ncbi_taxon_id":12081,"organism":"Poliovirus type 1 (strain Mahoney)","regions":[{"start":1457,"end":1469,"reference_id":"12823963","reference_source":"pmid","reference_html":"Towards an understanding of the poliovirus replication complex: the solution structure of the soluble domain of the poliovirus 3A protein. <i> Strauss DM, Glustrom LW, Wuttke DS. </i> J Mol Biol, 2003","date":"2022-06-15T13:34:44.874Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1NG7"}],"region_id":"DP03741r001","statement":[{"text":"Negative heteronuclear NOE values are observed for contiguous regions at both the N- and C termini (Figure 3(b)), indicating that these regions are disordered in solution. Consistent with this observation, long range NOE's were observed only for residues 15–45 (Figure 3(c)).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-14T15:26:25.146Z"}},{"start":1501,"end":1515,"reference_id":"12823963","reference_source":"pmid","reference_html":"Towards an understanding of the poliovirus replication complex: the solution structure of the soluble domain of the poliovirus 3A protein. <i> Strauss DM, Glustrom LW, Wuttke DS. </i> J Mol Biol, 2003","date":"2022-06-15T13:35:27.681Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1NG7"}],"region_id":"DP03741r002","statement":[{"text":"Negative heteronuclear NOE values are observed for contiguous regions at both the N- and C termini (Figure 3(b)), indicating that these regions are disordered in solution. Consistent with this observation, long range NOE's were observed only for residues 15–45 (Figure 3(c)).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-14T15:26:22.811Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MGAQVSSQKVGAHENSNRAYGGSTINYTTINYYRDSASNAASKQDFSQDPSKFTEPIKDVLIKTAPMLNSPNIEACGYSDRVLQLTLGNSTITTQEAANSVVAYGRWPEYLRDSEANPVDQPTEPDVAACRFYTLDTVSWTKESRGWWWKLPDALRDMGLFGQNMYYHYLGRSGYTVHVQCNASKFHQGALGVFAVPEMCLAGDSNTTTMHTSYQNANPGEKGGTFTGTFTPDNNQTSPARRFCPVDYLLGNGTLLGNAFVFPHQIINLRTNNCATLVLPYVNSLSIDSMVKHNNWGIAILPLAPLNFASESSPEIPITLTIAPMCCEFNGLRNITLPRLQGLPVMNTPGSNQYLTADNFQSPCALPEFDVTPPIDIPGEVKNMMELAEIDTMIPFDLSATKKNTMEMYRVRLSDKPHTDDPILCLSLSPASDPRLSHTMLGEILNYYTHWAGSLKFTFLFCGFMMATGKLLVSYAPPGADPPKKRKEAMLGTHVIWDIGLQSSCTMVVPWISNTTYRQTIDDSFTEGGYISVFYQTRIVVPLSTPREMDILGFVSACNDFSVRLLRDTTHIEQKALAQGLGQMLESMIDNTVRETVGAATSRDALPNTEASGPTHSKEIPALTAVETGATNPLVPSDTVQTRHVVQHRSRSESSIESFFARGACVTIMTVDNPASTTNKDKLFAVWKITYKDTVQLRRKLEFFTYSRFDMELTFVVTANFTETNNGHALNQVYQIMYVPPGAPVPEKWDDYTWQTSSNPSIFYTYGTAPARISVPYVGISNAYSHFYDGFSKVPLKDQSAALGDSLYGAASLNDFGILAVRVVNDHNPTKVTSKIRVYLKPKHIRVWCPRPPRAVAYYGPGVDYKDGTLTPLSTKDLTTYGFGHQNKAVYTAGYKICNYHLATQDDLQNAVNVMWSRDLLVTESRAQGTDSIARCNCNAGVYYCESRRKYYPVSFVGPTFQYMEANNYYPARYQSHMLIGHGFASPGDCGGILRCHHGVIGIITAGGEGLVAFSDIRDLYAYEEEAMEQGITNYIESLGAAFGSGFTQQISDKITELTNMVTSTITEKLLKNLIKIISSLVIITRNYEDTTTVLATLALLGCDASPWQWLRKKACDVLEIPYVIKQGDSWLKKFTEACNAAKGLEWVSNKISKFIDWLKEKIIPQARDKLEFVTKLRQLEMLENQISTIHQSCPSQEHQEILFNNVRWLSIQSKRFAPLYAVEAKRIQKLEHTINNYIQFKSKHRIEPVCLLVHGSPGTGKSVATNLIARAIAERENTSTYSLPPDPSHFDGYKQQGVVIMDDLNQNPDGADMKLFCQMVSTVEFIPPMASLEEKGILFTSNYVLASTNSSRISPPTVAHSDALARRFAFDMDIQVMNEYSRDGKLNMAMATEMCKNCHQPANFKRCCPLVCGKAIQLMDKSSRVRYSIDQITTMIINERNRRSNIGNCMEALFQGPLQYKDLKIDIKTSPPPECINDLLQAVDSQEVRDYCEKKGWIVNITSQVQTERNINRAMTILQAVTTFAAVAGVVYVMYKLFAGHQGAYTGLPNKKPNVPTIRTAKVQGPGFDYAVAMAKRNIVTATTSKGEFTMLGVHDNVAILPTHASPGESIVIDGKEVEILDAKALEDQAGTNLEITIITLKRNEKFRDIRPHIPTQITETNDGVLIVNTSKYPNMYVPVGAVTEQGYLNLGGRQTARTLMYNFPTRAGQCGGVITCTGKVIGMHVGGNGSHGFAAALKRSYFTQSQGEIQWMRPSKEVGYPIINAPSKTKLEPSAFHYVFEGVKEPAVLTKNDPRLKTDFEEAIFSKYVGNKITEVDEYMKEAVDHYAGQLMSLDINTEQMCLEDAMYGTDGLEALDLSTSAGYPYVAMGKKKRDILNKQTRDTKEMQKLLDTYGINLPLVTYVKDELRSKTKVEQGKSRLIEASSLNDSVAMRMAFGNLYAAFHKNPGVITGSAVGCDPDLFWSKIPVLMEEKLFAFDYTGYDASLSPAWFEALKMVLEKIGFGDRVDYIDYLNHSHHLYKNKTYCVKGGMPSGCSGTSIFNSMINNLIIRTLLLKTYKGIDLDHLKMIAYGDDVIASYPHEVDASLLAQSGKDYGLTMTPADKSATFETVTWENVTFLKRFFRADEKYPFLIHPVMPMKEIHESIRWTKDPRNTQDHVRSLCLLAWHNGEEEYNKFLAKIRSVPIGRALLLPEYSTLYRRWLDSF","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Picornavirales","Picornaviridae","Enterovirus","Enterovirus C"],"dataset":["Viral proteins","RNA-binding proteins","Stress response proteins"],"genes":[],"disorder_content":0.012675418741511997,"disprot_consensus":{"full":[{"start":1457,"end":1469,"type":"D"},{"start":1501,"end":1515,"type":"D"}],"Structural state":[{"start":1457,"end":1469,"type":"D"},{"start":1501,"end":1515,"type":"D"}]}},{"disprot_id":"DP03742","acc":"P04584","creator":"cpintado","date":"2022-06-15T14:01:00.055Z","features":{"pfam":[{"id":"PF00075","name":"RNase H","start":1048,"end":1167},{"id":"PF00077","name":"Retroviral aspartyl protease","start":519,"end":610},{"id":"PF00078","name":"Reverse transcriptase (RNA-dependent DNA polymerase)","start":675,"end":846},{"id":"PF00098","name":"Zinc knuckle","start":390,"end":405},{"id":"PF00098","name":"Zinc knuckle","start":411,"end":426},{"id":"PF00540","name":"gag gene protein p17 (matrix protein)","start":2,"end":123},{"id":"PF00552","name":"Integrase DNA binding domain","start":1396,"end":1439},{"id":"PF00607","name":"gag protein p24 N-terminal domain","start":146,"end":272},{"id":"PF00665","name":"Integrase core domain","start":1228,"end":1316},{"id":"PF02022","name":"Integrase Zinc binding domain","start":1179,"end":1216},{"id":"PF06815","name":"Reverse transcriptase connection domain","start":930,"end":1030},{"id":"PF06817","name":"Reverse transcriptase thumb domain","start":853,"end":916},{"id":"PF19317","name":"Gag protein p24 C-terminal domain","start":278,"end":351}],"gene3D":[]},"length":1464,"name":"Gag-Pol polyprotein","ncbi_taxon_id":11720,"organism":"Human immunodeficiency virus type 2 subtype A (isolate ROD)","regions":[{"start":111,"end":135,"reference_id":"18657545","reference_source":"pmid","reference_html":"Structure of the myristylated human immunodeficiency virus type 2 matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in membrane targeting. <i> Saad JS, Ablan SD, Ghanam RH, Kim A, Andrews K, Nagashima K, Soheilian F, Freed EO, Summers MF. </i> J Mol Biol, 2008","date":"2022-07-15T09:52:11.483Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2K4E"}],"region_id":"DP03742r001","statement":[{"text":"The 25 C-terminal residues appear to be disordered, based on the absence of significant amide-to-amide (i to i + 1 and i to i − 1) and amide–side-chain NOEs, as well as near-zero residual dipolar couplings (RDCs). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-15T13:44:12.353Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MGARNSVLRGKKADELERIRLRPGGKKKYRLKHIVWAANKLDRFGLAESLLESKEGCQKILTVLDPMVPTGSENLKSLFNTVCVIWCIHAEEKVKDTEGAKQIVRRHLVAETGTAEKMPSTSRPTAPSSEKGGNYPVQHVGGNYTHIPLSPRTLNAWVKLVEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINEEAAEWDVQHPIPGPLPAGQLREPRGSDIAGTTSTVEEQIQWMFRPQNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDIKQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMTQTLLVQNANPDCKLVLKGLGMNPTLEEMLTACQGVGGPGQKARLMAEALKEVIGPAPIPFAAAQQRKAFKCWNCGKEGHSARQCRAPRRQGCWKCGKPGHIMTNCPDRQAGFLRTGPLGKEAPQLPRGPSSAGADTNSTPSGSSSGSTGEIYAAREKTERAERETIQGSDRGLTAPRAGGDTIQGATNRGLAAPQFSLWKRPVVTAYIEGQPVEVLLDTGADDSIVAGIELGNNYSPKIVGGIGGFINTKEYKNVEIEVLNKKVRATIMTGDTPINIFGRNILTALGMSLNLPVAKVEPIKIMLKPGKDGPKLRQWPLTKEKIEALKEICEKMEKEGQLEEAPPTNPYNTPTFAIKKKDKNKWRMLIDFRELNKVTQDFTEIQLGIPHPAGLAKKRRITVLDVGDAYFSIPLHEDFRPYTAFTLPSVNNAEPGKRYIYKVLPQGWKGSPAIFQHTMRQVLEPFRKANKDVIIIQYMDDILIASDRTDLEHDRVVLQLKELLNGLGFSTPDEKFQKDPPYHWMGYELWPTKWKLQKIQLPQKEIWTVNDIQKLVGVLNWAAQLYPGIKTKHLCRLIRGKMTLTEEVQWTELAEAELEENRIILSQEQEGHYYQEEKELEATVQKDQENQWTYKIHQEEKILKVGKYAKVKNTHTNGIRLLAQVVQKIGKEALVIWGRIPKFHLPVEREIWEQWWDNYWQVTWIPDWDFVSTPPLVRLAFNLVGDPIPGAETFYTDGSCNRQSKEGKAGYVTDRGKDKVKKLEQTTNQQAELEAFAMALTDSGPKVNIIVDSQYVMGISASQPTESESKIVNQIIEEMIKKEAIYVAWVPAHKGIGGNQEVDHLVSQGIRQVLFLEKIEPAQEEHEKYHSNVKELSHKFGIPNLVARQIVNSCAQCQQKGEAIHGQVNAELGTWQMDCTHLEGKIIIVAVHVASGFIEAEVIPQESGRQTALFLLKLASRWPITHLHTDNGANFTSQEVKMVAWWIGIEQSFGVPYNPQSQGVVEAMNHHLKNQISRIREQANTIETIVLMAIHCMNFKRRGGIGDMTPSERLINMITTEQEIQFLQAKNSKLKDFRVYFREGRDQLWKGPGELLWKGEGAVLVKVGTDIKIIPRRKAKIIRDYGGRQEMDSGSHLEGAREDGEMA","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Lentivirus"],"genes":[{"name":{"value":"gag-pol"}}],"dataset":["Viral proteins","RNA-binding proteins"],"disorder_content":0.01707650273224044,"disprot_consensus":{"full":[{"start":111,"end":135,"type":"D"}],"Structural state":[{"start":111,"end":135,"type":"D"}]}},{"disprot_id":"DP03743","acc":"Q96QZ7","creator":"cpintado","date":"2022-06-15T14:40:45.786Z","features":{"pfam":[{"id":"PF00397","name":"WW domain","start":302,"end":331},{"id":"PF00397","name":"WW domain","start":361,"end":390},{"id":"PF00595","name":"PDZ domain","start":476,"end":541},{"id":"PF00595","name":"PDZ domain","start":644,"end":720},{"id":"PF00595","name":"PDZ domain","start":847,"end":921},{"id":"PF00595","name":"PDZ domain","start":999,"end":1090},{"id":"PF00595","name":"PDZ domain","start":1153,"end":1228},{"id":"PF00625","name":"Guanylate kinase","start":139,"end":190},{"id":"PF16663","name":"Unstructured region on MAGI","start":202,"end":261},{"id":"PF16666","name":"Unstructured region on MAGI","start":728,"end":840}],"gene3D":[]},"length":1491,"name":"Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":555,"end":580,"reference_id":"21238461","reference_source":"pmid","reference_html":"The structural and dynamic response of MAGI-1 PDZ1 with noncanonical domain boundaries to the binding of human papillomavirus E6. <i> Charbonnier S, Nominé Y, Ramírez J, Luck K, Chapelle A, Stote RH, Travé G, Kieffer B, Atkinson RA. </i> J Mol Biol, 2011","date":"2022-07-15T09:57:39.820Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2KPL"},{"db":"PDB","id":"2KPK"},{"db":"BMRB","id":"16558 "},{"db":"BMRB","id":"16559 "}],"region_id":"DP03743r001","statement":[{"text":"Experimental evidence shows that this 25-residue tail tends slowly towards greater disorder in the unliganded domain, as expected for an unstructured polypeptide chain attached to a structured domain.","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P03126"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-15T13:45:44.794Z"}}],"regions_counter":3,"released":"2023_12","sequence":"MSKVIQKKNHWTSRVHECTVKRGPQGELGVTVLGGAEHGEFPYVGAVAAVEAAGLPGGGEGPRLGEGELLLEVQGVRVSGLPRYDVLGVIDSCKEAVTFKAVRQGGRLNKDLRHFLNQRFQKGSPDHELQQTIRDNLYRHAVPCTTRSPREGEVPGVDYNFLTVKEFLDLEQSGTLLEVGTYEGNYYGTPKPPSQPVSGKVITTDALHSLQSGSKQSTPKRTKSYNDMQNAGIVHAENEEEDDVPEMNSSFTADSGEQEEHTLQETALPPVNSSIIAAPITDPSQKFPQYLPLSAEDNLGPLPENWEMAYTENGEVYFIDHNTKTTSWLDPRCLNKQQKPLEECEDDEGVHTEELDSELELPAGWEKIEDPVYGIYYVDHINRKTQYENPVLEAKRKKQLEQQQQQQQQQQQQQQQQQQQQTEEWTEDHSALVPPVIPNHPPSNPEPAREVPLQGKPFFTRNPSELKGKFIHTKLRKSSRGFGFTVVGGDEPDEFLQIKSLVLDGPAALDGKMETGDVIVSVNDTCVLGHTHAQVVKIFQSIPIGASVDLELCRGYPLPFDPDDPNTSLVTSVAILDKEPIIVNGQETYDSPASHSSKTGKVNGMKDARPSSPADVASNSSHGYPNDTVSLASSIATQPELITVHIVKGPMGFGFTIADSPGGGGQRVKQIVDSPRCRGLKEGDLIVEVNKKNVQALTHNQVVDMLVECPKGSEVTLLVQRGGLPVPKKSPKSQPLERKDSQNSSQHSVSSHRSLHTASPSHSTQVLPEFPPAEAQAPDQTDSSGQKKPDPFKIWAQSRSMYENRPMSPSPASGLSKGEREREINSTNFGECPIPDYQEQDIFLWRKETGFGFRILGGNEPGEPIYIGHIVPLGAADTDGRLRSGDELICVDGTPVIGKSHQLVVQLMQQAAKQGHVNLTVRRKVVFAVPKTENEVPSPASSHHSSNQPASLTEEKRTPQGSQNSLNTVSSGSGSTSGIGSGGGGGSGVVSTVVQPYDVEIRRGENEGFGFVIVSSVSRPEAGTTFAGNACVAMPHKIGRIIEGSPADRCGKLKVGDRILAVNGCSITNKSHSDIVNLIKEAGNTVTLRIIPGDESSNATLLTNAEKIATITTTHTPSQQGTQETRNTTKPKQESQFEFKAPQATQEQDFYTVELERGAKGFGFSLRGGREYNMDLYVLRLAEDGPAERCGKMRIGDEILEINGETTKNMKHSRAIELIKNGGRRVRLFLKRGDGSVPEYDPSSDRHGPATGPQGVPEVRAGPDRRQHPSLESSYPPDLHKSSPHGEKRAHARDPKGSREYSRQPNEHHTWNGTSRKPDSGACRPKDRAPEGRRDAQAERAAAANGPKRRSPEKRREGTRSADNTLERREKHEKRRDVSPERRRERSPTRRRDGSPSRRRRSLERLLEQRRSPERRRGGSPERRAKSTDRRRARSPERRRERSLDKRNREDRASHREREEANLKQDAGRSSRHPPEQRRRPYKECSTDLSI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"MAGI1"},"synonyms":[{"value":"AIP3"},{"value":"BAIAP1"},{"value":"BAP1"},{"value":"TNRC19"}]}],"alphafold_very_low_content":0.4862508383635144,"disorder_content":0.017437961099932932,"disprot_consensus":{"full":[{"start":555,"end":580,"type":"D"}],"Structural state":[{"start":555,"end":580,"type":"D"}]}},{"disprot_id":"DP03744","acc":"Q9VVJ7","creator":"cpintado","date":"2022-06-17T10:41:00.145Z","features":{"pfam":[{"id":"PF08806","name":"Sep15/SelM redox domain","start":74,"end":148}],"gene3D":[]},"length":178,"name":"CG7484 protein","ncbi_taxon_id":7227,"organism":"Drosophila melanogaster","regions":[{"start":150,"end":178,"reference_id":"16319061","reference_source":"pmid","reference_html":"NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family. <i> Ferguson AD, Labunskyy VM, Fomenko DE, Araç D, Chelliah Y, Amezcua CA, Rizo J, Gladyshev VN, Deisenhofer J. </i> J Biol Chem, 2006","date":"2022-06-17T10:43:07.991Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2A4H"}],"region_id":"DP03744r001","statement":[{"text":"Residues 62-70 (including an uncleaved N-terminal hexahistidine tag) and residues 150-178 of Sep15 are not shown because these regions are also flexible.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-14T15:38:39.627Z"}},{"start":17,"end":61,"reference_id":"16319061","reference_source":"pmid","reference_html":"NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family. <i> Ferguson AD, Labunskyy VM, Fomenko DE, Araç D, Chelliah Y, Amezcua CA, Rizo J, Gladyshev VN, Deisenhofer J. </i> J Biol Chem, 2006","date":"2022-07-15T09:54:28.960Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2A4H"}],"region_id":"DP03744r003","statement":[{"text":"By comparing the 1H,15N HSQC spectra of Sep15 with different construct boundaries, we determined that the N terminus of Sep15 (residues 17-61) was disordered. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-15T13:44:57.082Z"}}],"regions_counter":3,"released":"2023_12","sequence":"MHKCAIFLLLALSCQQIQAELTAADCRALGFIKAQLMCSSCEKLDDFGLDTIKPQCKQCCTLDQQPAAQRTYAKAILEVCTCKFRAYPQIQAFIQSGRPAKFPNLQIKYVRGLDPVVKLLDASGKVQETLSITKWNTDTVEEFFETHLAKDGAGKNSYSVVEDADGDDDEDYLRTNRI","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"genes":[{"name":{"value":"Sep15","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF49314.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF49314.2"}}]},"synonyms":[{"value":"BcDNA:SD16138","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF49314.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF49314.2"}}]},{"value":"Dmel\\CG7484","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF49314.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF49314.2"}}]},{"value":"Prise 8","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF49314.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF49314.2"}}]}],"orfNames":[{"value":"CG7484","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF49314.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF49314.2"}},{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0036745","url":"http://flybase.org/reports/FBgn0036745.html"}}]},{"value":"Dmel_CG7484","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAF49314.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAF49314.2"}}]}]}],"alphafold_very_low_content":0.05056179775280899,"disorder_content":0.4157303370786517,"disprot_consensus":{"full":[{"start":17,"end":61,"type":"D"},{"start":150,"end":178,"type":"D"}],"Structural state":[{"start":17,"end":61,"type":"D"},{"start":150,"end":178,"type":"D"}]}},{"disprot_id":"DP03745","acc":"Q8VHC3","creator":"cpintado","date":"2022-06-17T10:49:15.794Z","features":{"pfam":[{"id":"PF08806","name":"Sep15/SelM redox domain","start":41,"end":114}],"gene3D":[]},"length":145,"name":"Selenoprotein M","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":25,"end":34,"reference_id":"16319061","reference_source":"pmid","reference_html":"NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family. <i> Ferguson AD, Labunskyy VM, Fomenko DE, Araç D, Chelliah Y, Amezcua CA, Rizo J, Gladyshev VN, Deisenhofer J. </i> J Biol Chem, 2006","date":"2022-06-17T10:51:32.225Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2A2P"}],"region_id":"DP03745r001","statement":[{"text":"Residues 25-34 and residues 121-145 (including an uncleaved C-terminal hexahistidine tag) of SelM are not shown because these regions are flexible. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-14T15:44:18.344Z"}},{"start":121,"end":145,"reference_id":"16319061","reference_source":"pmid","reference_html":"NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family. <i> Ferguson AD, Labunskyy VM, Fomenko DE, Araç D, Chelliah Y, Amezcua CA, Rizo J, Gladyshev VN, Deisenhofer J. </i> J Biol Chem, 2006","date":"2022-06-17T10:51:44.007Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2A2P"}],"region_id":"DP03745r002","statement":[{"text":"Residues 25-34 and residues 121-145 (including an uncleaved C-terminal hexahistidine tag) of SelM are not shown because these regions are flexible. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-07-14T15:44:19.049Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MSILLSPPSLLLLLAALVAPATSTTNYRPDWNRLRGLARGRVETCGGUQLNRLKEVKAFVTEDIQLYHNLVMKHLPGADPELVLLSRNYQELERIPLSQMTRDEINALVQELGFYRKSAPEAQVPPEYLWAPAKPPEEASEHDDL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"genes":[{"name":{"value":"Selenom","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:2149786","url":"http://www.informatics.jax.org/marker/MGI:2149786"}}]}}],"disorder_content":0.2413793103448276,"disprot_consensus":{"full":[{"start":25,"end":34,"type":"D"},{"start":121,"end":145,"type":"D"}],"Structural state":[{"start":25,"end":34,"type":"D"},{"start":121,"end":145,"type":"D"}]}},{"disprot_id":"DP03747","acc":"S8F2K7","creator":"viglesias","date":"2022-07-07T08:41:27.273Z","features":{"pfam":[{"id":"PF22784","name":"Swiss Army Knife protein, DSP-PTPase phosphatase domain","start":352,"end":479}],"gene3D":[]},"length":523,"name":"Serine/threonine specific protein phosphatase","ncbi_taxon_id":508771,"organism":"Toxoplasma gondii (strain ATCC 50611 / Me49)","regions":[{"start":66,"end":175,"reference_id":"35640720","reference_source":"pmid","reference_html":"The Toxoplasma glucan phosphatase TgLaforin utilizes a distinct functional mechanism that can be exploited by therapeutic inhibitors. <i> Murphy RD, Chen T, Lin J, He R, Wu L, Pearson CR, Sharma S, Vander Kooi CD, Sinai AP, Zhang ZY, Vander Kooi CW, Gentry MS. </i> J Biol Chem, 2022","date":"2026-03-30T17:00:49.895Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"region_id":"DP03747r001","statement":[{"text":"Critically, the core CBM20 β-sandwich exhibited low uptake of deuterium, while the CBM insert regions that were modeled with low confidence displayed much higher rates of deuterium uptake.","type":"Results"},{"text":"These regions with high deuterium exchange are thus more mobile and less structured.","type":"Results"},{"text":"Supplementary figure S3 shows this region has a high percent of deuteration intake, indicating it is disordered.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T17:29:47.752Z"}},{"start":218,"end":254,"reference_id":"35640720","reference_source":"pmid","reference_html":"The Toxoplasma glucan phosphatase TgLaforin utilizes a distinct functional mechanism that can be exploited by therapeutic inhibitors. <i> Murphy RD, Chen T, Lin J, He R, Wu L, Pearson CR, Sharma S, Vander Kooi CD, Sinai AP, Zhang ZY, Vander Kooi CW, Gentry MS. </i> J Biol Chem, 2022","date":"2026-03-30T17:15:40.555Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP03747r002","statement":[{"text":"Critically, the core CBM20 β-sandwich exhibited low uptake of deuterium, while the CBM insert regions that were modeled with low confidence displayed much higher rates of deuterium uptake.","type":"Results"},{"text":"These regions with high deuterium exchange are thus more mobile and less structured.","type":"Results"},{"text":"In agreement with our sequence predictions and site-directed mutagenesis experiments, the computational prediction of AlphaFold2 suggested that TgLaforin’s CBM20 folds into a central core β-sandwich with large unstructured loops outside of this core.","type":"Discussion"},{"text":"This split-CBM20 contains discreet regions of homology to other CBM20s, separated by long linker regions with high solvent accessibility.","type":"Discussion"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T17:32:27.231Z"}},{"start":66,"end":175,"reference_id":"35640720","reference_source":"pmid","reference_html":"The Toxoplasma glucan phosphatase TgLaforin utilizes a distinct functional mechanism that can be exploited by therapeutic inhibitors. <i> Murphy RD, Chen T, Lin J, He R, Wu L, Pearson CR, Sharma S, Vander Kooi CD, Sinai AP, Zhang ZY, Vander Kooi CW, Gentry MS. </i> J Biol Chem, 2022","date":"2026-03-30T17:02:39.401Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006216","ec_ontology":"ECO","ec_name":"author inference used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP03747r003","statement":[{"text":"The three regions of the TgLaforin CBM20-domain, split over 325 amino acids and interrupted by linker regions, each contain a part of the key consensus amino acids predicted to be critical to glucan binding.","type":"Results"},{"text":"The model predicts that the unusual inserts form large unstructured linker regions connecting the core structured CBM regions (Fig. 2B).","type":"Results"},{"text":"Supplementary figure S3 shows this region has a high percent of deuteration intake, indicating it is disordered.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T17:29:41.764Z"}},{"start":218,"end":254,"reference_id":"35640720","reference_source":"pmid","reference_html":"The Toxoplasma glucan phosphatase TgLaforin utilizes a distinct functional mechanism that can be exploited by therapeutic inhibitors. <i> Murphy RD, Chen T, Lin J, He R, Wu L, Pearson CR, Sharma S, Vander Kooi CD, Sinai AP, Zhang ZY, Vander Kooi CW, Gentry MS. </i> J Biol Chem, 2022","date":"2026-03-30T17:31:06.315Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP03747r005","statement":[{"text":"The three regions of the TgLaforin CBM20-domain, split over 325 amino acids and interrupted by linker regions, each contain a part of the key consensus amino acids predicted to be critical to glucan binding.","type":"Results"},{"text":"Each of the constructs encoding individual portions of this region were either not expressed, not folded, or aggregated (Fig. S2, D and E). However, we were able to express and purify the predicted full CBM comprising all three subdomains with the two linkers, TgCBM123 (referred to simply as “TgCBM”) (Fig. S2E).","type":"Results"},{"text":"Supplementary figure S3 shows this region has a high percent of deuteration intake, indicating it is disordered.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T17:32:16.433Z"}},{"start":388,"end":413,"reference_id":"35640720","reference_source":"pmid","reference_html":"The Toxoplasma glucan phosphatase TgLaforin utilizes a distinct functional mechanism that can be exploited by therapeutic inhibitors. <i> Murphy RD, Chen T, Lin J, He R, Wu L, Pearson CR, Sharma S, Vander Kooi CD, Sinai AP, Zhang ZY, Vander Kooi CW, Gentry MS. </i> J Biol Chem, 2022","date":"2026-03-30T17:14:48.057Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"region_id":"DP03747r006","statement":[{"text":"Within the DSP domain, core structural elements had low uptake, while elements of the DSP active site, known to undergo conformational changes required for substrate interaction (44, 49), displayed higher uptake. These active site regions included the recognition domain, variable loop, D-loop, PTP-loop, and R-motif (Figs. 2D and S3) that have previously been reported as exhibiting higher solvent accessibility in SEX4 and laforin (44, 50).","type":"Results"},{"text":"Supplementary figure S3 shows this region has a high percent of deuteration intake, indicating it is disordered.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T17:33:56.143Z"}},{"start":318,"end":344,"reference_id":"35640720","reference_source":"pmid","reference_html":"The Toxoplasma glucan phosphatase TgLaforin utilizes a distinct functional mechanism that can be exploited by therapeutic inhibitors. <i> Murphy RD, Chen T, Lin J, He R, Wu L, Pearson CR, Sharma S, Vander Kooi CD, Sinai AP, Zhang ZY, Vander Kooi CW, Gentry MS. </i> J Biol Chem, 2022","date":"2026-03-30T17:05:24.444Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP03747r007","statement":[{"text":"Critically, the core CBM20 β-sandwich exhibited low uptake of deuterium, while the CBM insert regions that were modeled with low confidence displayed much higher rates of deuterium uptake.","type":"Results"},{"text":"Supplementary figure S3 shows this region has a high percent of deuteration intake, indicating it is disordered.","type":"Curator statement"},{"text":"Within the DSP domain, core structural elements had low uptake, while elements of the DSP active site, known to undergo conformational changes required for substrate interaction (44, 49), displayed higher uptake. These active site regions included the recognition domain, variable loop, D-loop, PTP-loop, and R-motif (Figs. 2D and S3) that have previously been reported as exhibiting higher solvent accessibility in SEX4 and laforin (44, 50).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":512,"end":523,"reference_id":"35640720","reference_source":"pmid","reference_html":"The Toxoplasma glucan phosphatase TgLaforin utilizes a distinct functional mechanism that can be exploited by therapeutic inhibitors. <i> Murphy RD, Chen T, Lin J, He R, Wu L, Pearson CR, Sharma S, Vander Kooi CD, Sinai AP, Zhang ZY, Vander Kooi CW, Gentry MS. </i> J Biol Chem, 2022","date":"2026-03-30T17:24:27.088Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP03747r008","statement":[{"text":"Critically, the core CBM20 β-sandwich exhibited low uptake of deuterium, while the CBM insert regions that were modeled with low confidence displayed much higher rates of deuterium uptake.","type":"Results"},{"text":"Supplementary figure S3 shows this region has a high percent of deuteration intake, indicating it is disordered.","type":"Curator statement"},{"text":"Within the DSP domain, core structural elements had low uptake, while elements of the DSP active site, known to undergo conformational changes required for substrate interaction (44, 49), displayed higher uptake. These active site regions included the recognition domain, variable loop, D-loop, PTP-loop, and R-motif (Figs. 2D and S3) that have previously been reported as exhibiting higher solvent accessibility in SEX4 and laforin (44, 50).","type":"Results"}]},{"start":512,"end":523,"reference_id":"35640720","reference_source":"pmid","reference_html":"The Toxoplasma glucan phosphatase TgLaforin utilizes a distinct functional mechanism that can be exploited by therapeutic inhibitors. <i> Murphy RD, Chen T, Lin J, He R, Wu L, Pearson CR, Sharma S, Vander Kooi CD, Sinai AP, Zhang ZY, Vander Kooi CW, Gentry MS. </i> J Biol Chem, 2022","date":"2026-03-30T17:24:37.468Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP03747r009","statement":[{"text":"Critically, the core CBM20 β-sandwich exhibited low uptake of deuterium, while the CBM insert regions that were modeled with low confidence displayed much higher rates of deuterium uptake.","type":"Results"},{"text":"Supplementary figure S3 shows this region has a high percent of deuteration intake, indicating it is disordered.","type":"Curator statement"},{"text":"Within the DSP domain, core structural elements had low uptake, while elements of the DSP active site, known to undergo conformational changes required for substrate interaction (44, 49), displayed higher uptake. These active site regions included the recognition domain, variable loop, D-loop, PTP-loop, and R-motif (Figs. 2D and S3) that have previously been reported as exhibiting higher solvent accessibility in SEX4 and laforin (44, 50).","type":"Results"}]}],"regions_counter":9,"released":"2026_06","sequence":"MRVRFSVTAFVPPNAQLGVVGSAPFLGEWKLEHCVPLMPYSAPHPQGLEPSLWFRDIDLDPASCPNDTNDVHSTAAVSASCSADRRRCDLSRQSPHCFPSARSASPYMVEVSRGDCPFAVELMSTSQHVLSEFSKHNSPVYSAGEQRFRRSLPSSASFSSCTSSGSAVAATKCVWDAAAYRVATRAPEVQAVLESHPLRHCAFEYKFVLWYPPNGEIAVPYVPTTAGEEVPITYAGDSEVLNEESEGGARRRSWRKWLFPPSPSRCPAPPGPSESIVWEGFGPDSNRKFCFDPFDVVVDVNELGDLECLYICRIAHFRDPRAGGVGEYDLTTRFYNSVKSECRMHYSTIFPRFFVGSCPRQLKHIRHLKEELKVTCVVNLQTEQDLCNNYPDPIASSRSAEAVSQLYDGSGLRYVWLPTADMCDSARKIAVANAAFLLLGLFQSGHSVYMHCNAGVGRSVAAACAFLCFAVGLDLRKVNFLICARRPVAYWDEKAMKYGIGDYQAKFGHCRVVGEEAEERQHA","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Conoidasida","Coccidia","Eucoccidiorida","Eimeriorina","Sarcocystidae","Toxoplasma"],"genes":[{"orfNames":[{"value":"TGME49_205290","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EPT29986.1","url":"https://www.ebi.ac.uk/ena/browser/view/EPT29986.1"}}]}]}],"alphafold_very_low_content":0.27151051625239003,"disorder_content":0.40535372848948376,"disprot_consensus":{"full":[{"start":66,"end":175,"type":"D"},{"start":218,"end":254,"type":"D"},{"start":318,"end":344,"type":"D"},{"start":388,"end":413,"type":"D"},{"start":512,"end":523,"type":"D"}],"Structural state":[{"start":66,"end":175,"type":"D"},{"start":218,"end":254,"type":"D"},{"start":318,"end":344,"type":"D"},{"start":388,"end":413,"type":"D"},{"start":512,"end":523,"type":"D"}],"Disorder function":[{"start":66,"end":175,"type":"F"},{"start":218,"end":254,"type":"F"},{"start":512,"end":523,"type":"F"}]}},{"disprot_id":"DP03748","acc":"P75862","creator":"vacs","date":"2022-07-12T13:28:04.231Z","features":{"pfam":[{"id":"PF07126","name":"Cell-division protein ZapC, C-terminal","start":90,"end":168},{"id":"PF21083","name":"Cell-division protein ZapC, N-terminal","start":3,"end":89}],"gene3D":[]},"length":180,"name":"Cell division protein ZapC","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":169,"end":180,"reference_id":"26655719","reference_source":"pmid","reference_html":"Structural and Functional Analyses Reveal Insights into the Molecular Properties of the Escherichia coli Z Ring Stabilizing Protein, ZapC. <i> Schumacher MA, Zeng W, Huang KH, Tchorzewski L, Janakiraman A. </i> J Biol Chem, 2016","date":"2022-07-12T13:30:36.766Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5E1L"}],"region_id":"DP03748r001","statement":[{"text":"The final model includes ZapC residues 2–168 (residues 169–180 were disordered) and 109 solvent molecules.","type":"Methods"},{"text":"Only C-terminal residues 169–180 are disordered in the structure, consistent with the fact that although the ZapC C-terminal region is relatively conserved among enteric bacteria, this region shows significant diversity in both length and sequence among ZapC homologs in other bacteria (Fig. 1D).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-13T09:19:47.389Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MRIKPDDNWRWYYDEEHDRMMLDLANGMLFRSRFARKMLTPDAFSPAGFCVDDAALYFSFEEKCRDFNLSKEQKAELVLNALVAIRYLKPQMPKSWHFVSHGEMWVPMPGDAACVWLSDTHEQVNLLVVESGENAALCLLAQPCVVIAGRAMQLGDAIKIMNDRLKPQVNVDSFSLEQAV","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"genes":[{"name":{"value":"zapC","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00906","url":"https://hamap.expasy.org/unirule/MF_00906"}}]},"synonyms":[{"value":"ycbW"}],"olnNames":[{"value":"b0946"},{"value":"JW5125"}]}],"alphafold_very_low_content":0.05,"disorder_content":0.06666666666666667,"disprot_consensus":{"full":[{"start":169,"end":180,"type":"D"}],"Structural state":[{"start":169,"end":180,"type":"D"}]}},{"disprot_id":"DP03749","acc":"Q92871","creator":"vacs","date":"2022-07-13T11:00:18.637Z","features":{"pfam":[{"id":"PF03332","name":"Eukaryotic phosphomannomutase","start":36,"end":255}],"gene3D":[]},"length":262,"name":"Phosphomannomutase 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":11,"reference_id":"29695157","reference_source":"pmid","reference_html":"Structural Basis of the Molecular Switch between Phosphatase and Mutase Functions of Human Phosphomannomutase 1 under Ischemic Conditions. <i> Ji T, Zhang C, Zheng L, Dunaway-Mariano D, Allen KN. </i> Biochemistry, 2018","date":"2022-07-13T11:02:03.663Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6CFV"},{"db":"PDB","id":"6CFS"},{"db":"PDB","id":"6CFT"},{"db":"PDB","id":"6CFR"},{"db":"PDB","id":"6CFU"}],"region_id":"DP03749r001","statement":[{"text":"Similar to the native PMM1 structure, the first 11 residues of the N-terminus and the last six residues of the C-terminus were disordered; the electron density for the remainder of the protein was clear and ordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-07-13T14:11:25.337Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MAVTAQAARRKERVLCLFDVDGTLTPARQKIDPEVAAFLQKLRSRVQIGVVGGSDYCKIAEQLGDGDEVIEKFDYVFAENGTVQYKHGRLLSKQTIQNHLGEELLQDLINFCLSYMALLRLPKKRGTFIEFRNGMLNISPIGRSCTLEERIEFSELDKKEKIREKFVEALKTEFAGKGLRFSRGGMISFDVFPEGWDKRYCLDSLDQDSFDTIHFFGNETSPGGNDFEIFADPRTVGHSVVSPQDTVQRCREIFFPETAHEA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"PMM1"},"synonyms":[{"value":"PMMH22"}]}],"alphafold_very_low_content":0.026717557251908396,"disorder_content":0.04198473282442748,"disprot_consensus":{"full":[{"start":1,"end":11,"type":"D"}],"Structural state":[{"start":1,"end":11,"type":"D"}]}},{"disprot_id":"DP03750","acc":"P0ABT5","creator":"vacs","date":"2022-07-18T09:20:31.090Z","features":{"pfam":[{"id":"PF01207","name":"Dihydrouridine synthase (Dus)","start":14,"end":319}],"gene3D":[]},"length":321,"name":"tRNA-dihydrouridine synthase B","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":43,"end":61,"reference_id":"29294097","reference_source":"pmid","reference_html":"Unveiling structural and functional divergences of bacterial tRNA dihydrouridine synthases: perspectives on the evolution scenario. <i> Bou-Nader C, Montémont H, Guérineau V, Jean-Jean O, Brégeon D, Hamdane D. </i> Nucleic Acids Res, 2018","date":"2022-07-18T09:22:41.772Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"6EI9"}],"region_id":"DP03750r001","statement":[{"text":"Coral or bunch were used to construct the 19 missing residues (44–62) not observed in the X-ray structure (28,29).","type":"Methods"},{"text":"The residues S43 to I61 located between β3–β4 are disordered.","type":"Results"},{"text":"The crystal structure being incomplete, we generated the 19 missing amino acids between S43 and I61 using bunch or coral (both gave similar results). As shown in Figure 2C, the theoretical SAXS curve of the resulting model fits well the experimental data with a  χ2 ∼1.8. This indicates that the crystal structure of\nmonomeric DusB is a relevant form in solution.","type":"Results"},{"text":"The missing residues (44–62), not observed in the X-ray structure, are indicated as a dashed line.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-23T15:01:43.753Z"}}],"regions_counter":1,"released":"2026_06","sequence":"MRIGQYQLRNRLIAAPMAGITDRPFRTLCYEMGAGLTVSEMMSSNPQVWESDKSRLRMVHIDEPGIRTVQIAGSDPKEMADAARINVESGAQIIDINMGCPAKKVNRKLAGSALLQYPDVVKSILTEVVNAVDVPVTLKIRTGWAPEHRNCEEIAQLAEDCGIQALTIHGRTRACLFNGEAEYDSIRAVKQKVSIPVIANGDITDPLKARAVLDYTGADALMIGRAAQGRPWIFREIQHYLDTGELLPPLPLAEVKRLLCAHVRELHDFYGPAKGYRIARKHVSWYLQEHAPNDQFRRTFNAIEDASEQLEALEAYFENFA","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"genes":[{"name":{"value":"dusB","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_02042","url":"https://hamap.expasy.org/unirule/MF_02042"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"11983710","url":"http://www.ncbi.nlm.nih.gov/pubmed/11983710","alternativeUrl":"https://europepmc.org/abstract/MED/11983710"}}]},"synonyms":[{"value":"yhdG"}],"olnNames":[{"value":"b3260"},{"value":"JW3228"}]}],"alphafold_very_low_content":0,"dataset":["RNA-binding proteins"],"disorder_content":0.059190031152647975,"disprot_consensus":{"full":[{"start":43,"end":61,"type":"D"}],"Structural state":[{"start":43,"end":61,"type":"D"}]}},{"disprot_id":"DP03751","acc":"Q9XZT6","creator":"vacs","date":"2022-07-18T12:27:35.796Z","features":{"pfam":[{"id":"PF01712","name":"Deoxynucleoside kinase","start":24,"end":218}],"gene3D":[]},"length":250,"name":"Deoxynucleoside kinase","ncbi_taxon_id":7227,"organism":"Drosophila melanogaster","regions":[{"start":221,"end":250,"reference_id":"10692477","reference_source":"pmid","reference_html":"Functional expression of a multisubstrate deoxyribonucleoside kinase from Drosophila melanogaster and its C-terminal deletion mutants. <i> Munch-Petersen B, Knecht W, Lenz C, Søndergaard L, Piskur J. </i> J Biol Chem, 2000","date":"2023-02-22T14:04:37.003Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019136","term_name":"deoxynucleoside kinase activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"ec_go":"IMP","region_id":"DP03751r003","statement":[{"text":"The C-terminal 20 amino acids were dispensable for phosphorylation of deoxyribonucleosides but necessary for full activity with purine ribonucleosides. Removal of the C-terminal 20 amino acids increased the specific activity 2-fold, but 99% of the activity was lost after removal of the C-terminal 30 amino acids.","type":"Abstract"},{"text":"In the present paper, we describe a cDNA from D. melanogaster with homology to the cDNA of mammalian TK2, dCK, and dGK but with a unique C-terminal amino acid sequence that appeared to be important for the catalytic activity.","type":"Introduction"},{"text":"Comparison of the specific activities (Table I) shows that rDm-dNKΔC30 had about 1% of the specific activity of rDm-dNK.","type":"Results"},{"text":"As compared with rDm-dNK, the relative activities of rDm-dNKΔC10 and rDm-dNKΔC20 with deoxyribonucleosides remained largely unchanged, whereas there was a substantial decrease in the phosphorylation of the purine ribonucleosides adenosine and guanosine, as well as of all dideoxyribonucleosides and AZT (Table III). ","type":"Results"},{"text":"The very C-terminal part of the enzyme, the terminal 10 amino acids, harboring a putative phosphorylation and nuclear localization signal, did not influence catalytic efficiency for thymidine but reduced the phosphorylation of purine-dideoxyribo- and ribonucleosides. C-terminal truncation of 20 amino acids changed the thymidine turnover unexpectedly toward higher rates. This suggests that the C-terminal domain of Dm-dNK has an inhibitory effect on phosphorylation of deoxyribonucleosides, although on the other hand promoting phosphorylation of other substrates, such as purine ribo- and dideoxyribonucleosides. The terminal 20 amino acids seemed to be essential for phosphorylation of purine ribonucleosides and dideoxyadenosine. Thus, this deletion reduced the broad substrate specificity (Table III). Deletion of 30 amino acids at the C terminus decreased the activity to about 1% of rDm-dNK, indicating the loss of a domain essential for catalysis. ","type":"Discussion"}],"term_comment":"","term_def":"\"Catalysis of the reaction: ATP + 2'-deoxynucleoside = ADP + 2'-deoxynucleoside 5'-phosphate.\" [EC:2.7.1.145]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-02-23T08:42:57.532Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MAEAASCARKGTKYAEGTQPFTVLIEGNIGSGKTTYLNHFEKYKNDICLLTEPVEKWRNVNGVNLLELMYKDPKKWAMPFQSYVTLTMLQSHTAPTNKKLKIMERSIFSARYCFVENMRRNGSLEQGMYNTLEEWYKFIEESIHVQADLIIYLRTSPEVAYERIRQRARSEESCVPLKYLQELHELHEDWLIHQRRPQSCKVLVLDADLNLENIGTEYQRSESSIFDAISSNQQPSPVLVSPSKRQRVAR","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"genes":[{"name":{"value":"dnk"},"orfNames":[{"value":"CG5452"}]}],"alphafold_very_low_content":0.104,"disorder_content":0,"disprot_consensus":{"full":[{"start":221,"end":250,"type":"F"}],"Structural state":[],"Molecular function":[{"start":221,"end":250,"type":"F"}]}},{"disprot_id":"DP03756","acc":"P36888","creator":"vnugnes","date":"2022-07-29T17:36:59.879Z","features":{"pfam":[{"id":"PF00047","name":"Immunoglobulin domain","start":259,"end":341},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":610,"end":942}],"gene3D":[]},"length":993,"name":"Receptor-type tyrosine-protein kinase FLT3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":762,"end":782,"reference_id":"14759363","reference_source":"pmid","reference_html":"The structural basis for autoinhibition of FLT3 by the juxtamembrane domain. <i> Griffith J, Black J, Faerman C, Swenson L, Wynn M, Lu F, Lippke J, Saxena K. </i> Mol Cell, 2004","date":"2022-07-29T17:49:34.937Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"1RJB"}],"region_id":"DP03756r001","statement":[{"text":"The PDB shows this region lacks electron density and is disordered.","type":"Curator statement"}]},{"start":948,"end":958,"reference_id":"14759363","reference_source":"pmid","reference_html":"The structural basis for autoinhibition of FLT3 by the juxtamembrane domain. <i> Griffith J, Black J, Faerman C, Swenson L, Wynn M, Lu F, Lippke J, Saxena K. </i> Mol Cell, 2004","date":"2022-07-29T18:44:11.784Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"1RJB"}],"region_id":"DP03756r002","statement":[{"text":"The PDB shows this region lacks electron density and is disordered.","type":"Curator statement"}]}],"regions_counter":2,"released":"2022_12","sequence":"MPALARDGGQLPLLVVFSAMIFGTITNQDLPVIKCVLINHKNNDSSVGKSSSYPMVSESPEDLGCALRPQSSGTVYEAAAVEVDVSASITLQVLVDAPGNISCLWVFKHSSLNCQPHFDLQNRGVVSMVILKMTETQAGEYLLFIQSEATNYTILFTVSIRNTLLYTLRRPYFRKMENQDALVCISESVPEPIVEWVLCDSQGESCKEESPAVVKKEEKVLHELFGTDIRCCARNELGRECTRLFTIDLNQTPQTTLPQLFLKVGEPLWIRCKAVHVNHGFGLTWELENKALEEGNYFEMSTYSTNRTMIRILFAFVSSVARNDTGYYTCSSSKHPSQSALVTIVEKGFINATNSSEDYEIDQYEEFCFSVRFKAYPQIRCTWTFSRKSFPCEQKGLDNGYSISKFCNHKHQPGEYIFHAENDDAQFTKMFTLNIRRKPQVLAEASASQASCFSDGYPLPSWTWKKCSDKSPNCTEEITEGVWNRKANRKVFGQWVSSSTLNMSEAIKGFLVKCCAYNSLGTSCETILLNSPGPFPFIQDNISFYATIGVCLLFIVVLTLLICHKYKKQFRYESQLQMVQVTGSSDNEYFYVDFREYEYDLKWEFPRENLEFGKVLGSGAFGKVMNATAYGISKTGVSIQVAVKMLKEKADSSEREALMSELKMMTQLGSHENIVNLLGACTLSGPIYLIFEYCCYGDLLNYLRSKREKFHRTWTEIFKEHNFSFYPTFQSHPNSSMPGSREVQIHPDSDQISGLHGNSFHSEDEIEYENQKRLEEEEDLNVLTFEDLLCFAYQVAKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFGLARDIMSDSNYVVRGNARLPVKWMAPESLFEGIYTIKSDVWSYGILLWEIFSLGVNPYPGIPVDANFYKLIQNGFKMDQPFYATEEIYIIMQSCWAFDSRKRPSFPNLTSFLGCQLADAEEAMYQNVDGRVSECPHTYQNRRPFSREMDLGLLSPQAQVEDS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Cancer-related proteins"],"genes":[{"name":{"value":"FLT3"},"synonyms":[{"value":"CD135"},{"value":"FLK2"},{"value":"STK1"}]}],"alphafold_very_low_content":0.16515609264853978,"disorder_content":0.032225579053373615,"disprot_consensus":{"full":[{"start":762,"end":782,"type":"D"},{"start":948,"end":958,"type":"D"}],"Structural state":[{"start":762,"end":782,"type":"D"},{"start":948,"end":958,"type":"D"}]}},{"disprot_id":"DP03758","acc":"Q96ST2","creator":"tlazar","date":"2022-08-05T16:45:41.716Z","features":{"pfam":[{"id":"PF08711","name":"TFIIS helical bundle-like domain","start":637,"end":689}],"gene3D":[]},"length":819,"name":"Protein IWS1 homolog","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":352,"end":548,"reference_id":"26245978","reference_source":"pmid","reference_html":"Multiple cellular proteins interact with LEDGF/p75 through a conserved unstructured consensus motif. <i> Tesina P, Čermáková K, Hořejší M, Procházková K, Fábry M, Sharma S, Christ F, Demeulemeester J, Debyser Z, Rijck J, Veverka V, Řezáčová P. </i> Nat Commun, 2015","date":"2022-11-08T14:08:41.395Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03758r006","statement":[{"text":"(e) 2D 15N/1H HSQC NMR spectra obtained for IWS1352–548. The unstructured character of IWS1352–548 is illustrated by the poor dispersion of amide signals.","type":"Figure"},{"text":"The unstructured character of the fragment was verified experimentally using CD spectroscopy, DSF and 1D 1H and 2D 15N/1H HSQC NMR spectra (Fig. 5e, Supplementary Figs 2 and 4c,d).","type":"Results"}]},{"start":352,"end":548,"reference_id":"26245978","reference_source":"pmid","reference_html":"Multiple cellular proteins interact with LEDGF/p75 through a conserved unstructured consensus motif. <i> Tesina P, Čermáková K, Hořejší M, Procházková K, Fábry M, Sharma S, Christ F, Demeulemeester J, Debyser Z, Rijck J, Veverka V, Řezáčová P. </i> Nat Commun, 2015","date":"2022-11-08T14:08:55.925Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03758r007","statement":[{"text":"The unstructured character of the fragment was verified experimentally using CD spectroscopy, DSF and 1D 1H and 2D 15N/1H HSQC NMR spectra (Fig. 5e, Supplementary Figs 2 and 4c,d).","type":"Results"}]},{"start":352,"end":548,"reference_id":"26245978","reference_source":"pmid","reference_html":"Multiple cellular proteins interact with LEDGF/p75 through a conserved unstructured consensus motif. <i> Tesina P, Čermáková K, Hořejší M, Procházková K, Fábry M, Sharma S, Christ F, Demeulemeester J, Debyser Z, Rijck J, Veverka V, Řezáčová P. </i> Nat Commun, 2015","date":"2022-11-08T14:52:17.770Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001236","ec_ontology":"ECO","ec_name":"multiplex bead-based immunoassay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"O75475","operator":null,"partner_start":347,"partner_end":429}],"region_id":"DP03758r008","statement":[{"text":"IWS1 interacts exclusively with LEDGF/p75 constructs containing the IBD. Recombinant GST-LEDGF/p75, GST-LEDGF/p75325–530, GST-IBD, GST-PWWP or GST-LEDGF/p52 were titrated against 20 nM His-IWS1 in AlphaScreen. ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":352,"end":548,"reference_id":"26245978","reference_source":"pmid","reference_html":"Multiple cellular proteins interact with LEDGF/p75 through a conserved unstructured consensus motif. <i> Tesina P, Čermáková K, Hořejší M, Procházková K, Fábry M, Sharma S, Christ F, Demeulemeester J, Debyser Z, Rijck J, Veverka V, Řezáčová P. </i> Nat Commun, 2015","date":"2022-11-08T14:55:21.052Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"O75475","operator":null,"partner_start":347,"partner_end":429}],"region_id":"DP03758r009","statement":[{"text":"Under optimal conditions (25 mM Tris-HCl, pH 8.5, 150 mM NaCl, 0.05% BME), the IBD-IWS1352–548 complex could readily be isolated using analytical SEC (Supplementary Fig. 4d), and the affinity of the interaction was determined using ITC (Fig. 5f). We calculated a Kd value of 6.7±2.0 μM and a 1:1 binding stoichiometry (N=0.96).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":352,"end":548,"reference_id":"26245978","reference_source":"pmid","reference_html":"Multiple cellular proteins interact with LEDGF/p75 through a conserved unstructured consensus motif. <i> Tesina P, Čermáková K, Hořejší M, Procházková K, Fábry M, Sharma S, Christ F, Demeulemeester J, Debyser Z, Rijck J, Veverka V, Řezáčová P. </i> Nat Commun, 2015","date":"2022-11-08T14:55:49.666Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"O75475","operator":null,"partner_start":347,"partner_end":429}],"region_id":"DP03758r010","statement":[{"text":"We followed the formation of the IBD-IWS1352–548 complexes via chemical shift perturbations of the IBD backbone signals (1H, 15N, 13C′; Fig. 5g) in the 3D HNCO spectra, analogous to our experiments with JPO21–130 and PogZ1117–1410. The specific changes induced by IWS1352–548 were localized to residues K360–D369, K402–V408, I412 and M413 of the IBD and overlap with those found for JPO2, PogZ and MLL1 (Fig. 5h). Overall, these experiments unambiguously confirm a novel IBM-mediated interaction between IWS1 and the LEDGF/p75 IBD.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":10,"released":"2024_06","sequence":"MDSEYYSGDQSDDGGATPVQDERDSGSDGEDDVNEQHSGSDTGSVERHSENETSDREDGLPKGHHVTDSENDEPLNLNASDSESEELHRQKDSDSESEERAEPPASDSENEDVNQHGSDSESEETRKLPGSDSENEELLNGHASDSENEDVGKHPASDSEIEELQKSPASDSETEDALKPQISDSESEEPPRHQASDSENEEPPKPRMSDSESEELPKPQVSDSESEEPPRHQASDSENEELPKPRISDSESEDPPRHQASDSENEELPKPRISDSESEDPPRNQASDSENEELPKPRVSDSESEGPQKGPASDSETEDASRHKQKPESDDDSDRENKGEDTEMQNDSFHSDSHMDRKKFHSSDSEEEEHKKQKMDSDEDEKEGEEEKVAKRKAAVLSDSEDEEKASAKKSRVVSDADDSDSDAVSDKSGKREKTIASDSEEEAGKELSDKKNEEKDLFGSDSESGNEEENLIADIFGESGDEEEEEFTGFNQEDLEEEKGETQVKEAEDSDSDDNIKRGKHMDFLSDFEMMLQRKKSMSGKRRRNRDGGTFISDADDVVSAMIVKMNEAAEEDRQLNNQKKPALKKLTLLPAVVMHLKKQDLKETFIDSGVMSAIKEWLSPLPDRSLPALKIREELLKILQELPSVSQETLKHSGIGRAVMYLYKHPKESRSNKDMAGKLINEWSRPIFGLTSNYKGMTREEREQRDLEQMPQRRRMNSTGGQTPRRDLEKVLTGEEKALRPGDPGFCARARVPMPSNKDYVVRPKWNVEMESSRFQATSKKGISRLDKQMRKFTDIRKKSRSAHAVKISIEGNKMPL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"genes":[{"name":{"value":"IWS1"},"synonyms":[{"value":"IWS1L"}]}],"alphafold_very_low_content":0.608058608058608,"disorder_content":0.24053724053724054,"disprot_consensus":{"full":[{"start":352,"end":548,"type":"D"}],"Structural state":[{"start":352,"end":548,"type":"D"}],"Molecular function":[{"start":352,"end":548,"type":"F"}]}},{"disprot_id":"DP03759","acc":"P25454","creator":"vnugnes","date":"2022-08-24T17:56:38.700Z","features":{"pfam":[{"id":"PF08423","name":"Rad51","start":153,"end":395},{"id":"PF14520","name":"SAM-like Helix-hairpin-helix tandem","start":86,"end":137}],"gene3D":[]},"length":400,"name":"DNA repair protein RAD51","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":329,"end":344,"reference_id":"15235592","reference_source":"pmid","reference_html":"Crystal structure of a Rad51 filament. <i> Conway AB, Lynch TW, Zhang Y, Fortin GS, Fung CW, Symington LS, Rice PA. </i> Nat Struct Mol Biol, 2004","date":"2022-08-24T18:27:21.284Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile345Thr","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"A truncation (Δ1–79) of the Rad51 I345T protein from Saccharomyces cerevisiae was used in this study."}]}],"cross_refs":[{"db":"PDB","id":"1SZP"}],"region_id":"DP03759r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"sequence_construct":"MVPIEKLQVNGITMADVKKLRESGLHTAEAVAYAPRKDLLEIKGISEAKADKLLNEAARLVPMGFVTAADFHMRRSELICLTTGSKNLDTLLGGGVETGSITELFGEFRTGKSQLCHTLAVTCQIPLDIGGGEGKCLYIDTEGTFRPVRLVSIAQRFGLDPDDALNNVAYARAYNADHQLRLLDAAAQMMSESRFSLIVVDSVMALYRTDFSGRGELSARQMHLAKFMRALQRLADQFGVAVVVTNQVVAQVDGGMAFNPDPKKPTGGNIMAHSSTTRLGFKKGKGCQRLCKVVDSPCLPEAECVFAIYEDGVGDPREEDE","statement":[{"text":"This region lacks electron density in PDB, indicating it is disordered.","type":"Curator statement"}]},{"start":1,"end":77,"reference_id":"20371520","reference_source":"pmid","reference_html":"Insights into the mechanism of Rad51 recombinase from the structure and properties of a filament interface mutant. <i> Chen J, Villanueva N, Rould MA, Morrical SW. </i> Nucleic Acids Res, 2010","date":"2022-08-24T18:36:25.208Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.His352Tyr","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Rad51 H352Y crystals were grown in hanging drop by vapor diffusion."}]}],"region_id":"DP03759r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"}],"sequence_construct":"MSQVQEQHISESQLQYGNGSLMSTVPADLSQSVVDGNGNGSSEDIEATNGSGDGGGLQEQAEAQGEMEDEAYDEAALGSFVPIEKLQVNGITMADVKKLRESGLHTAEAVAYAPRKDLLEIKGISEAKADKLLNEAARLVPMGFVTAADFHMRRSELICLTTGSKNLDTLLGGGVETGSITELFGEFRTGKSQLCHTLAVTCQIPLDIGGGEGKCLYIDTEGTFRPVRLVSIAQRFGLDPDDALNNVAYARAYNADHQLRLLDAAAQMMSESRFSLIVVDSVMALYRTDFSGRGELSARQMHLAKFMRALQRLADQFGVAVVVTNQVVAQVDGGMAFNPDPKKPIGGNIMAYSSTTRLGFKKGKGCQRLCKVVDSPCLPEAECVFAIYEDGVGDPREEDE","statement":[{"text":"The yeast-specific N-terminal extension (residues 1–79), which is present in our protein but disordered within the crystal, and which was deleted in order to obtain crystals of I345T, likewise does not affect the structure of the DNA-free, nucleotide-free Rad51 filament.","type":"Discussion"},{"text":"The PDB shows that the disordered region is 1-77.","type":"Curator statement"}]},{"start":328,"end":347,"reference_id":"20371520","reference_source":"pmid","reference_html":"Insights into the mechanism of Rad51 recombinase from the structure and properties of a filament interface mutant. <i> Chen J, Villanueva N, Rould MA, Morrical SW. </i> Nucleic Acids Res, 2010","date":"2022-08-24T18:37:42.388Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.His352Tyr","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Rad51 H352Y crystals were grown in hanging drop by vapor diffusion."}]}],"region_id":"DP03759r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"}],"sequence_construct":"MSQVQEQHISESQLQYGNGSLMSTVPADLSQSVVDGNGNGSSEDIEATNGSGDGGGLQEQAEAQGEMEDEAYDEAALGSFVPIEKLQVNGITMADVKKLRESGLHTAEAVAYAPRKDLLEIKGISEAKADKLLNEAARLVPMGFVTAADFHMRRSELICLTTGSKNLDTLLGGGVETGSITELFGEFRTGKSQLCHTLAVTCQIPLDIGGGEGKCLYIDTEGTFRPVRLVSIAQRFGLDPDDALNNVAYARAYNADHQLRLLDAAAQMMSESRFSLIVVDSVMALYRTDFSGRGELSARQMHLAKFMRALQRLADQFGVAVVVTNQVVAQVDGGMAFNPDPKKPIGGNIMAYSSTTRLGFKKGKGCQRLCKVVDSPCLPEAECVFAIYEDGVGDPREEDE","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"regions_counter":3,"released":"2024_06","sequence":"MSQVQEQHISESQLQYGNGSLMSTVPADLSQSVVDGNGNGSSEDIEATNGSGDGGGLQEQAEAQGEMEDEAYDEAALGSFVPIEKLQVNGITMADVKKLRESGLHTAEAVAYAPRKDLLEIKGISEAKADKLLNEAARLVPMGFVTAADFHMRRSELICLTTGSKNLDTLLGGGVETGSITELFGEFRTGKSQLCHTLAVTCQIPLDIGGGEGKCLYIDTEGTFRPVRLVSIAQRFGLDPDDALNNVAYARAYNADHQLRLLDAAAQMMSESRFSLIVVDSVMALYRTDFSGRGELSARQMHLAKFMRALQRLADQFGVAVVVTNQVVAQVDGGMAFNPDPKKPIGGNIMAHSSTTRLGFKKGKGCQRLCKVVDSPCLPEAECVFAIYEDGVGDPREEDE","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"genes":[{"name":{"value":"RAD51"},"olnNames":[{"value":"YER095W"}]}],"alphafold_very_low_content":0.19,"disorder_content":0.2425,"disprot_consensus":{"full":[{"start":1,"end":77,"type":"D"},{"start":328,"end":347,"type":"D"}],"Structural state":[{"start":1,"end":77,"type":"D"},{"start":328,"end":347,"type":"D"}]}},{"disprot_id":"DP03760","acc":"P26332","creator":"vnugnes","date":"2022-09-12T18:11:02.619Z","features":{"pfam":[{"id":"PF00913","name":"Trypanosome variant surface glycoprotein (A-type)","start":13,"end":376},{"id":"PF29633","name":"Variant surface glycoprotein ETAT","start":420,"end":476}],"gene3D":[]},"length":476,"name":"Variant surface glycoprotein MITAT 1.2","ncbi_taxon_id":5702,"organism":"Trypanosoma brucei brucei","regions":[{"start":385,"end":400,"reference_id":"15557330","reference_source":"pmid","reference_html":"Structure of the C-terminal domain from Trypanosoma brucei variant surface glycoprotein MITat1.2. <i> Chattopadhyay A, Jones NG, Nietlispach D, Nielsen PR, Voorheis HP, Mott HR, Carrington M. </i> J Biol Chem, 2005","date":"2022-09-12T18:21:44.186Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"1XU6"}],"region_id":"DP03760r001","statement":[{"text":"Outside the structured core, no long range distance restraints were observed for residues from Glu-359 to Ala-374 or from Glu-417 to Ser-433. The heteronuclear NOE values for these residues were less than 0.1 (Fig. 4), indicating that they are disordered in solution.","type":"Results"},{"text":"The authors are not considering the signal peptide, therefore the disordered region they mention corresponds to residues 385-400 and 443-459 of the Uniprot.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:16:29.334Z"}},{"start":443,"end":459,"reference_id":"15557330","reference_source":"pmid","reference_html":"Structure of the C-terminal domain from Trypanosoma brucei variant surface glycoprotein MITat1.2. <i> Chattopadhyay A, Jones NG, Nietlispach D, Nielsen PR, Voorheis HP, Mott HR, Carrington M. </i> J Biol Chem, 2005","date":"2022-09-12T18:22:00.358Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"1XU6"}],"region_id":"DP03760r002","statement":[{"text":"Outside the structured core, no long range distance restraints were observed for residues from Glu-359 to Ala-374 or from Glu-417 to Ser-433. The heteronuclear NOE values for these residues were less than 0.1 (Fig. 4), indicating that they are disordered in solution.","type":"Results"},{"text":"The authors are not considering the signal peptide, therefore the disordered region they mention corresponds to residues 385-400 and 443-459 of the Uniprot.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:16:40.249Z"}}],"regions_counter":2,"released":"2022_12","sequence":"MPSNQEARLFLAVLVLAQVLPILVDSAAEKGFKQAFWQPLCQVSEELDDQPKGALFTLQAAASKIQKMRDAALRASIYAEINHGTNRAKAAVIVANHYAMKADSGLEALKQTLSSQEVTATATASYLKGRIDEYLNLLLQTKESGTSGCMMDTSGTNTVTKAGGTIGGVPCKLQLSPIQPKRPAATYLGKAGYVGLTRQADAANNFHDNDAECRLASGHNTNGLGKSGQLSAAVTMAAGYVTVANSQTAVTVQALDALQEASGAAHQPWIDAWKAKKALTGAETAEFRNETAGIAGKTGVTKLVEEALLKKKDSEASEIQTELKKYFSGHENEQWTAIEKLISEQPVAQNLVGDNQPTKLGELEGNAKLTTILAYYRMETAGKFEVLTQKHKPAESQQQAAETEGSCNKKDQNECKSPCKWHNDAENKKCTLDKEEAKKVADETAKDGKTGNTNTTGSSNSFVISKTPLWLAVLLF","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Trypanosoma"],"dataset":["Neglected tropical diseases proteins"],"genes":[],"alphafold_very_low_content":0.1323529411764706,"disorder_content":0.06932773109243698,"disprot_consensus":{"full":[{"start":385,"end":400,"type":"D"},{"start":443,"end":459,"type":"D"}],"Structural state":[{"start":385,"end":400,"type":"D"},{"start":443,"end":459,"type":"D"}]}},{"disprot_id":"DP03761","acc":"Q9GU80","creator":"vnugnes","date":"2022-09-12T18:46:07.693Z","features":{"pfam":[{"id":"PF00027","name":"Cyclic nucleotide-binding domain","start":262,"end":343},{"id":"PF00027","name":"Cyclic nucleotide-binding domain","start":383,"end":465}],"gene3D":[]},"length":499,"name":"Protein kinase A regulatory subunit","ncbi_taxon_id":5691,"organism":"Trypanosoma brucei","regions":[{"start":187,"end":211,"reference_id":"33359563","reference_source":"pmid","reference_html":"Disorder and partial folding in the regulatory subunit hinge region of Trypanosoma brucei protein kinase A: The C-linker portion inhibits the parasite's protein kinase A. <i> Araujo NA, Bruix M, Laurents DV. </i> Arch Biochem Biophys, 2021","date":"2022-09-12T19:06:12.864Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP03761r001","statement":[{"text":"The CD spectra of peptides 1 and 2 show minima between 195 and 200 nm (Fig. 3), which is characteristic of statistical coils [[28], [29], [30]].","type":"Results"},{"text":"The Protein kinase A regulatory subunit peptides used in this publication were derived from the Trypanosoma brucei brucei (strain 927/4 GUTat10.1) (Uniprot Q385V6) which is 100% identical to this Uniprot.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:17:05.055Z"}},{"start":198,"end":223,"reference_id":"33359563","reference_source":"pmid","reference_html":"Disorder and partial folding in the regulatory subunit hinge region of Trypanosoma brucei protein kinase A: The C-linker portion inhibits the parasite's protein kinase A. <i> Araujo NA, Bruix M, Laurents DV. </i> Arch Biochem Biophys, 2021","date":"2022-09-12T19:06:25.753Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP03761r002","statement":[{"text":"The CD spectra of peptides 1 and 2 show minima between 195 and 200 nm (Fig. 3), which is characteristic of statistical coils [[28], [29], [30]].","type":"Results"},{"text":"The Protein kinase A regulatory subunit peptides used in this publication were derived from the Trypanosoma brucei brucei (strain 927/4 GUTat10.1) (Uniprot Q385V6) which is 100% identical to this Uniprot.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:17:06.695Z"}},{"start":187,"end":211,"reference_id":"33359563","reference_source":"pmid","reference_html":"Disorder and partial folding in the regulatory subunit hinge region of Trypanosoma brucei protein kinase A: The C-linker portion inhibits the parasite's protein kinase A. <i> Araujo NA, Bruix M, Laurents DV. </i> Arch Biochem Biophys, 2021","date":"2022-09-12T19:06:33.725Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"BMRB","id":"50627"}],"region_id":"DP03761r003","statement":[{"text":"The amide 1H region (7.6–9.0 ppm) of the 1H NMR spectra in water at pH 5.1 and 5 °C shows little dispersion (Sup. Fig. 3A), suggesting that this peptide does not adopt a stable secondary structure in these conditions.","type":"Results"},{"text":" Moreover, taking the 1HN signal of S4 at 8.6 ppm in water as a local reference for peptide 1, the lack of change in the chemical shifts suggests that the presence of the DPC micelles does not alter the chemical environment of peptide 1 (Sup. Fig. 6).","type":"Results"},{"text":"The Protein kinase A regulatory subunit peptides used in this publication were derived from the Trypanosoma brucei brucei (strain 927/4 GUTat10.1) (Uniprot Q385V6) which is 100% identical to this Uniprot.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:17:07.756Z"}},{"start":198,"end":223,"reference_id":"33359563","reference_source":"pmid","reference_html":"Disorder and partial folding in the regulatory subunit hinge region of Trypanosoma brucei protein kinase A: The C-linker portion inhibits the parasite's protein kinase A. <i> Araujo NA, Bruix M, Laurents DV. </i> Arch Biochem Biophys, 2021","date":"2022-09-12T19:06:46.467Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"BMRB","id":"50630"},{"db":"BMRB","id":"50631"}],"region_id":"DP03761r004","statement":[{"text":"Next, we recorded 1D and 2D NMR spectra on peptide 2. The 1D 1H NMR spectrum in aqueous solution at pH 5.0, 5 °C shows little dispersion in the amide 1H region (8.50–8.75 ppm) (Sup. Fig. 3B), suggesting that peptide 2, like peptide 1, does not adopt a stable secondary structure.","type":"Results"},{"text":"The 1D 1H NMR spectrum of peptide 2 recorded in the presence of DPC micelles also reveals poor signal dispersion in the amide region, as shown in Sup. Fig. 5B. Interestingly, the presence of DPC micelles shifts all the 1HN resonances to higher field, including the signals of the glycines. This is shown in Sup. Fig. 8 which uses the 1HN signal of S21 at 8.24 ppm as a local reference. The analysis of the 1Hα, 13Cα and 13Cβ conformational chemical shifts, displayed in Fig. 5B and Table 1, indicates that peptide 2 partially adopts a helical conformation. The helical population is 22% considering the whole peptide and reaches 53% for the segment spanning residues P16 to Y22 (Table 1).","type":"Results"},{"text":"The Protein kinase A regulatory subunit peptides used in this publication were derived from the Trypanosoma brucei brucei (strain 927/4 GUTat10.1) (Uniprot Q385V6) which is 100% identical to this Uniprot.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:17:09.504Z"}}],"regions_counter":4,"released":"2022_12","sequence":"MSEKGTSLNLFLAACQKEGVKQPNTFLVEFFTKKPELSEVEEIDLSKNYIGNRGILALLDVISELPCFRFLNCSNQKLYNTDLNEDSVRGNATIDRIVDVFKSHPTANALDLSHNPISNYAGRRLLLLTQNNKRICRVELVDTRIDFELRSRITQQCEKNTIAIWESQAQEKEEERAFGESVTWVPTQTSADLTAIGGGRKRRTTVRGEGIDPEKAKSYVAPYFEKSEDETALILKLLTYNVLFSFLDSRDLMTVAGAMWRVEFKQDDCIMEAGQTTCDKLYIIQDGKADIIKEGQKVYLKVEGTAVGELELMYQTPTVATVKVCTPELIAWALDRDTYRHLVMGSAIRRRETYIQFLTNIPFLSGLDNYEKLQLADALSSDEFEPGDYIIRYGEEGEWLYIILEGSVDVVGRDDDGNEKHVWEFGKGDHVGELEFLNNHANVADVVAKTHVVTAKLNRRHFEMCLGPVIDVLKRTSQQPNYEYYQSKLKTTLRAEGRK","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Trypanosoma"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"name":{"value":"PKA-R","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAG16958.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAG16958.1"}}]}}],"alphafold_very_low_content":0.10020040080160321,"disorder_content":0.07414829659318638,"disprot_consensus":{"full":[{"start":187,"end":223,"type":"D"}],"Structural state":[{"start":187,"end":223,"type":"D"}]}},{"disprot_id":"DP03764","acc":"A4HN55","creator":"vnugnes","date":"2022-09-13T15:06:18.772Z","features":{"pfam":[{"id":"PF00227","name":"Proteasome subunit","start":27,"end":207}],"gene3D":[]},"length":254,"name":"Proteasome subunit beta","ncbi_taxon_id":5660,"organism":"Leishmania braziliensis","regions":[{"start":1,"end":29,"reference_id":"30962368","reference_source":"pmid","reference_html":"Preclinical candidate for the treatment of visceral leishmaniasis that acts through proteasome inhibition. <i> Wyllie S, Brand S, Thomas M, De Rycker M, Chung CW, Pena I, Bingham RP, Bueren-Calabuig JA, Cantizani J, Cebrian D, Craggs PD, Ferguson L, Goswami P, Hobrath J, Howe J, Jeacock L, Ko EJ, Korczynska J, MacLean L, Manthri S, Martinez MS, Mata-Cantero L, Moniz S, Nühs A, Osuna-Cabello M, Pinto E, Riley J, Robinson S, Rowland P, Simeons FRC, Shishikura Y, Spinks D, Stojanovski L, Thomas J, Thompson S, Viayna Gaza E, Wall RJ, Zuccotto F, Horn D, Ferguson MAJ, Fairlamb AH, Fiandor JM, Martin J, Gray DW, Miles TJ, Gilbert IH, Read KD, Marco M, Wyatt PG. </i> Proc Natl Acad Sci U S A, 2019","date":"2022-09-13T19:07:36.435Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6QM7"}],"region_id":"DP03764r001","statement":[{"text":"The electron microscopy evidence of the proteasome 20S subunit complexed with a imidazo[1,2-a]pyrimidine shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:17:22.769Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MPGFNFENVQRNLNLEAEGYSAPRTLKTGTTIVGVVYQDGVVLGADTRATEGSIVADKHCRKIHYMAPNIMCCGAGTSADTEAVTNMVSSHLALHRLETGKQSRVLEALTLLKRHLYRYQGHVSAALVLGGVDVEGPFLATIAPHGSTDRLPFVTMGSGSIAAMAQMETAYKDNMTCEEAKELVASAIRKGIFNDPYSGTQVDVCVITKDKTEVMIGYDKPNERMYPRQEIVLRPGTTPVLKEEIRQLVDIVEV","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania","Leishmania braziliensis species complex"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"orfNames":[{"value":"LBRM_34_3820","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAM43599.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAM43599.1"}}]}]}],"alphafold_very_low_content":0.003937007874015748,"disorder_content":0.1141732283464567,"disprot_consensus":{"full":[{"start":1,"end":29,"type":"D"}],"Structural state":[{"start":1,"end":29,"type":"D"}]}},{"disprot_id":"DP03765","acc":"A0A109NYM0","creator":"vnugnes","date":"2022-09-13T15:21:01.337Z","features":{"pfam":[{"id":"PF00071","name":"Ras family","start":15,"end":195}],"gene3D":[]},"length":235,"name":"Rab5a","ncbi_taxon_id":5661,"organism":"Leishmania donovani","regions":[{"start":1,"end":10,"reference_id":"33135673","reference_source":"pmid","reference_html":"Crystal structure of the GDP-bound GTPase domain of Rab5a from Leishmania donovani. <i> Zohib M, Maheshwari D, Pal RK, Freitag-Pohl S, Biswal BK, Pohl E, Arora A. </i> Acta Crystallogr F Struct Biol Commun, 2020","date":"2022-09-13T15:24:48.552Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6L6O"}],"region_id":"DP03765r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17552","entry_name":"GDP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":"glycerol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30089","entry_name":"acetate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"}],"statement":[{"text":"In the crystal structure, no electron density was found for the initial ten residues (Met1–Glu10) at the N-terminus, which were omitted from the structure.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:20:32.780Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MNTHPPQLMEATSAKIVMLGESGAGKSSIALRFTRNEFLANQETTIGAAFLSKTVMIPPPRGAAAAPGGATSAHALQQMRALKYEIWDTAGQERFRSLAPIYYRGACGALVVYDITNSESLKKAQTWIKELRANADPSLIIVLVGNKKDLGSLRQVSFEDGQRLAAEEQLAAFYEASAKDNNNVEQVFLDLAAKLLDQGLGNRGGAAGGARGGVVAPRGERVEQSNESASQSTCC","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"name":{"value":"Rab5a","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AKQ62390.1","url":"https://www.ebi.ac.uk/ena/browser/view/AKQ62390.1"}}]}}],"alphafold_very_low_content":0.19148936170212766,"disorder_content":0.0425531914893617,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"}]}},{"disprot_id":"DP03766","acc":"A4IDD0","creator":"vnugnes","date":"2022-09-13T19:00:18.333Z","features":{"pfam":[{"id":"PF00227","name":"Proteasome subunit","start":29,"end":216},{"id":"PF10584","name":"Proteasome subunit A N-terminal signature","start":6,"end":28}],"gene3D":[]},"length":264,"name":"Proteasome subunit alpha type","ncbi_taxon_id":5671,"organism":"Leishmania infantum","regions":[{"start":242,"end":264,"reference_id":"30962368","reference_source":"pmid","reference_html":"Preclinical candidate for the treatment of visceral leishmaniasis that acts through proteasome inhibition. <i> Wyllie S, Brand S, Thomas M, De Rycker M, Chung CW, Pena I, Bingham RP, Bueren-Calabuig JA, Cantizani J, Cebrian D, Craggs PD, Ferguson L, Goswami P, Hobrath J, Howe J, Jeacock L, Ko EJ, Korczynska J, MacLean L, Manthri S, Martinez MS, Mata-Cantero L, Moniz S, Nühs A, Osuna-Cabello M, Pinto E, Riley J, Robinson S, Rowland P, Simeons FRC, Shishikura Y, Spinks D, Stojanovski L, Thomas J, Thompson S, Viayna Gaza E, Wall RJ, Zuccotto F, Horn D, Ferguson MAJ, Fairlamb AH, Fiandor JM, Martin J, Gray DW, Miles TJ, Gilbert IH, Read KD, Marco M, Wyatt PG. </i> Proc Natl Acad Sci U S A, 2019","date":"2022-09-14T15:10:03.934Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6QM8"},{"db":"PDB","id":"6QM7"}],"region_id":"DP03766r001","sequence_construct":"MQSRKGEGWRDTGTDSLPPFSFCCSPAFSSPLAFGGEGADGCAYILTHVCRYACIAALTLHSEGAERHMRVCVCVRRCAYNEMVLHQVVAFASLAPALHPLSPLPLPCMATTHACCGLRVRSFSLKKSEKKNQQRRLQAPDLSQKTRTRTQKEKQTLQIYLRCVMFKNEYDSDITTWSPTGRLFQIEYANEAVNNGSATVGVKGKNFVVLAALKRSPVAELSSYQEKVFEIDEHVGMSISGLVADGRVLARYLRTECMNYRYMYSNGMPMNQMADMIGEKHQRHIQCSGKRPFGVGLLLAGYDRQGPHLYQTVPSGDVYDYKATAMGVRSQASRTYLERHFEHFSDCTLDELVTHALKALASATSEGIELNVKNTTIAIVGKDTPFTIFEEESARKYLDGFKMRPEDRVAVAEEDEEMLHEQPLDVEE","statement":[{"text":"The electron microscopy evidences of the proteasome 20S subunit complexed with a imidazo[1,2-a]pyrimidine and the proteasome 20S subunit apo structures, shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:21:58.303Z"}},{"start":242,"end":264,"reference_id":"32667203","reference_source":"pmid","reference_html":"Discovery and Characterization of Clinical Candidate LXE408 as a Kinetoplastid-Selective Proteasome Inhibitor for the Treatment of Leishmaniases. <i> Nagle A, Biggart A, Be C, Srinivas H, Hein A, Caridha D, Sciotti RJ, Pybus B, Kreishman-Deitrick M, Bursulaya B, Lai YH, Gao MY, Liang F, Mathison CJN, Liu X, Yeh V, Smith J, Lerario I, Xie Y, Chianelli D, Gibney M, Berman A, Chen YL, Jiricek J, Davis LC, Liu X, Ballard J, Khare S, Eggimann FK, Luneau A, Groessl T, Shapiro M, Richmond W, Johnson K, Rudewicz PJ, Rao SPS, Thompson C, Tuntland T, Spraggon G, Glynne RJ, Supek F, Wiesmann C, Molteni V. </i> J Med Chem, 2020","date":"2022-09-14T16:00:01.895Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"EMDB","id":"10462"},{"db":"PDB","id":"6TCZ"}],"region_id":"DP03766r002","statement":[{"text":"The electron microscopy evidences of the proteasome 20S subunit complexed with the inhibitory compounds LXE408 and bortezomib shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"sequence_construct":"MQSRKGEGWRDTGTDSLPPFSFCCSPAFSSPLAFGGEGADGCAYILTHVCRYACIAALTLHSEGAERHMRVCVCVRRCAYNEMVLHQVVAFASLAPALHPLSPLPLPCMATTHACCGLRVRSFSLKKSEKKNQQRRLQAPDLSQKTRTRTQKEKQTLQIYLRCVMFKNEYDSDITTWSPTGRLFQIEYANEAVNNGSATVGVKGKNFVVLAALKRSPVAELSSYQEKVFEIDEHVGMSISGLVADGRVLARYLRTECMNYRYMYSNGMPMNQMADMIGEKHQRHIQCSGKRPFGVGLLLAGYDRQGPHLYQTVPSGDVYDYKATAMGVRSQASRTYLERHFEHFSDCTLDELVTHALKALASATSEGIELNVKNTTIAIVGKDTPFTIFEEESARKYLDGFKMRPEDRVAVAEEDEEMLHEQPLDVEE","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:22:06.376Z"}}],"regions_counter":2,"released":"2022_12","sequence":"MFKNEYDSDITTWSPTGRLFQIEYANEAVNNGSATVGVKGRDFVVLAALKRSPVAELSSYQEKVFEVDEHVGMSISGLVADGRVLARFLRTECMNYRYMYSHGMPMNQMADMIGEKHQRHIQFSGKRPFGVGLLLAGYDRQGPHLYQTVPSGDVYDYKATAMGVRSQASRTYLEKHFEHFTDCTLDELVAHALKALASATSEGVELNVKNTTIAIVGKDTPFTIFEEESARRYLDGFKMRPEDRVAAADDEEEVLHEQPLDVEE","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"orfNames":[{"value":"LINJ_36_1670","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAM72861.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAM72861.1"}}]}]}],"alphafold_very_low_content":0.04924242424242424,"disorder_content":0.08712121212121213,"disprot_consensus":{"full":[{"start":242,"end":264,"type":"D"}],"Structural state":[{"start":242,"end":264,"type":"D"}]}},{"disprot_id":"DP03767","acc":"A4HV47","creator":"vnugnes","date":"2022-09-13T19:15:20.258Z","features":{"pfam":[{"id":"PF00227","name":"Proteasome subunit","start":51,"end":229}],"gene3D":[]},"length":283,"name":"Proteasome subunit beta","ncbi_taxon_id":5671,"organism":"Leishmania infantum","regions":[{"start":1,"end":54,"reference_id":"30962368","reference_source":"pmid","reference_html":"Preclinical candidate for the treatment of visceral leishmaniasis that acts through proteasome inhibition. <i> Wyllie S, Brand S, Thomas M, De Rycker M, Chung CW, Pena I, Bingham RP, Bueren-Calabuig JA, Cantizani J, Cebrian D, Craggs PD, Ferguson L, Goswami P, Hobrath J, Howe J, Jeacock L, Ko EJ, Korczynska J, MacLean L, Manthri S, Martinez MS, Mata-Cantero L, Moniz S, Nühs A, Osuna-Cabello M, Pinto E, Riley J, Robinson S, Rowland P, Simeons FRC, Shishikura Y, Spinks D, Stojanovski L, Thomas J, Thompson S, Viayna Gaza E, Wall RJ, Zuccotto F, Horn D, Ferguson MAJ, Fairlamb AH, Fiandor JM, Martin J, Gray DW, Miles TJ, Gilbert IH, Read KD, Marco M, Wyatt PG. </i> Proc Natl Acad Sci U S A, 2019","date":"2022-09-13T19:18:20.915Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6QM7"},{"db":"PDB","id":"6QM8"}],"region_id":"DP03767r001","statement":[{"text":"The electron microscopy evidences of the proteasome 20S subunit complexed with a imidazo[1,2-a]pyrimidine and the proteasome 20S subunit apo structures, shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:22:22.628Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MLQRPDHTLLQDPSYPKDIEQKLTENGPAQAGKQLFQPDLAVIDPQLSEAVSLGTTILAVSYKGGVVLAADSRTSSGTYVVNRASNKLTKLTEKIYCCRSGSAADTQALAERVSNYLGSYQTDIGADVNVATAANLFHKMCYVNRWNISAGIIVAGYDPINGGSVYSIPSGGSCVKLDYALGGSGSIFLYSFFDANYKPGMSKGECVAFCQRAVAHAYSRDGSSGGLIRTITLDAEEAEDLTVPWKRSPYCMEKDPKYQVQAVQNPPFSSSAKVTGNRMSSTG","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"orfNames":[{"value":"LINJ.12.0003","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAM66312.2","url":"https://www.ebi.ac.uk/ena/browser/view/CAM66312.2"}}]}]}],"alphafold_very_low_content":0.13780918727915195,"disorder_content":0.19081272084805653,"disprot_consensus":{"full":[{"start":1,"end":54,"type":"D"}],"Structural state":[{"start":1,"end":54,"type":"D"}]}},{"disprot_id":"DP03768","acc":"A4IDD6","creator":"vnugnes","date":"2022-09-13T19:21:42.956Z","features":{"pfam":[{"id":"PF00227","name":"Proteasome subunit","start":96,"end":278}],"gene3D":[]},"length":302,"name":"Proteasome subunit beta","ncbi_taxon_id":5671,"organism":"Leishmania infantum","regions":[{"start":1,"end":99,"reference_id":"30962368","reference_source":"pmid","reference_html":"Preclinical candidate for the treatment of visceral leishmaniasis that acts through proteasome inhibition. <i> Wyllie S, Brand S, Thomas M, De Rycker M, Chung CW, Pena I, Bingham RP, Bueren-Calabuig JA, Cantizani J, Cebrian D, Craggs PD, Ferguson L, Goswami P, Hobrath J, Howe J, Jeacock L, Ko EJ, Korczynska J, MacLean L, Manthri S, Martinez MS, Mata-Cantero L, Moniz S, Nühs A, Osuna-Cabello M, Pinto E, Riley J, Robinson S, Rowland P, Simeons FRC, Shishikura Y, Spinks D, Stojanovski L, Thomas J, Thompson S, Viayna Gaza E, Wall RJ, Zuccotto F, Horn D, Ferguson MAJ, Fairlamb AH, Fiandor JM, Martin J, Gray DW, Miles TJ, Gilbert IH, Read KD, Marco M, Wyatt PG. </i> Proc Natl Acad Sci U S A, 2019","date":"2022-09-13T19:22:59.045Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6QM7"},{"db":"PDB","id":"6QM8"}],"region_id":"DP03768r001","statement":[{"text":"The electron microscopy evidences of the proteasome 20S subunit complexed with a imidazo[1,2-a]pyrimidine and the proteasome 20S subunit apo structures, shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:23:06.477Z"}},{"start":1,"end":99,"reference_id":"32667203","reference_source":"pmid","reference_html":"Discovery and Characterization of Clinical Candidate LXE408 as a Kinetoplastid-Selective Proteasome Inhibitor for the Treatment of Leishmaniases. <i> Nagle A, Biggart A, Be C, Srinivas H, Hein A, Caridha D, Sciotti RJ, Pybus B, Kreishman-Deitrick M, Bursulaya B, Lai YH, Gao MY, Liang F, Mathison CJN, Liu X, Yeh V, Smith J, Lerario I, Xie Y, Chianelli D, Gibney M, Berman A, Chen YL, Jiricek J, Davis LC, Liu X, Ballard J, Khare S, Eggimann FK, Luneau A, Groessl T, Shapiro M, Richmond W, Johnson K, Rudewicz PJ, Rao SPS, Thompson C, Tuntland T, Spraggon G, Glynne RJ, Supek F, Wiesmann C, Molteni V. </i> J Med Chem, 2020","date":"2022-09-14T15:29:39.859Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"EMDB","id":"10462"},{"db":"PDB","id":"6TCZ"}],"region_id":"DP03768r002","statement":[{"text":"The electron microscopy evidences of the proteasome 20S subunit complexed with an inhibitory compound (LXE408) shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:23:08.502Z"}}],"regions_counter":2,"released":"2022_12","sequence":"MFADFESVMSSNFTLDDCPRVGPFTYHNMDEDTLEEPLSLCSYRRAPQQTTERSPASCDAVTADPLDSSRYLHGENRCWTLTASCPVPRAIPKIDMKKGTTTLAFRFNGGIIVAVDSRASTGQYIASQTVLKVLEINDYLLGTLAGGAADCQYWERVLGMECRLWELRNGSRITVAAASKILANITYAYRNHGLSMGTMLAGWDQFGPSLYYVDDKGSRVKQDLFSVGSGSIYAYGVLDTGYRKDLSVEDACDLARRSIFHATYRDGASGGIVTVYHVHEKGWTKISRDDQTKLYDRYFPSQ","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"orfNames":[{"value":"LINJ_36_1730","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAM72867.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAM72867.1"}}]}]}],"alphafold_very_low_content":0.271523178807947,"disorder_content":0.32781456953642385,"disprot_consensus":{"full":[{"start":1,"end":99,"type":"D"}],"Structural state":[{"start":1,"end":99,"type":"D"}]}},{"disprot_id":"DP03769","acc":"A4HSQ5","creator":"vnugnes","date":"2022-09-13T19:26:30.690Z","features":{"pfam":[{"id":"PF00227","name":"Proteasome subunit","start":40,"end":232}],"gene3D":[]},"length":247,"name":"Proteasome subunit beta","ncbi_taxon_id":5671,"organism":"Leishmania infantum","regions":[{"start":1,"end":33,"reference_id":"30962368","reference_source":"pmid","reference_html":"Preclinical candidate for the treatment of visceral leishmaniasis that acts through proteasome inhibition. <i> Wyllie S, Brand S, Thomas M, De Rycker M, Chung CW, Pena I, Bingham RP, Bueren-Calabuig JA, Cantizani J, Cebrian D, Craggs PD, Ferguson L, Goswami P, Hobrath J, Howe J, Jeacock L, Ko EJ, Korczynska J, MacLean L, Manthri S, Martinez MS, Mata-Cantero L, Moniz S, Nühs A, Osuna-Cabello M, Pinto E, Riley J, Robinson S, Rowland P, Simeons FRC, Shishikura Y, Spinks D, Stojanovski L, Thomas J, Thompson S, Viayna Gaza E, Wall RJ, Zuccotto F, Horn D, Ferguson MAJ, Fairlamb AH, Fiandor JM, Martin J, Gray DW, Miles TJ, Gilbert IH, Read KD, Marco M, Wyatt PG. </i> Proc Natl Acad Sci U S A, 2019","date":"2022-09-13T19:29:09.032Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6QM7"},{"db":"PDB","id":"6QM8"}],"region_id":"DP03769r001","sequence_construct":"MASSSPPLLPFSSFVVAVVAIHLSFRVFCVGAQSLCKCCSCVPACALPLCFSSSPSVSAEDVALALFAHPKVLTHRPTARYSPILSLLHYAVMIEDHAEYGHNYYPQKLASSTLTLPQQGAKQQQWSPYQDNGGTTAAIAGKDFVILAGDTRLNGDFCLHSRHDQSKIFQLTPYTYMASNGMQADRLQLQQMLKYRVKWYKYNNGGKVPSTKAIAQLMSTMLYHRRFFPYYTFNMVVGLDEEGHGVCYSYDAVGSTEPFLYGTRGSAASFVEPLLDCLINRQHMTSQAPPEMTKEETLAMLKNAFTGAAERDIYTGDSVSFFIITKDGVQQESFELRKD","statement":[{"text":"The electron microscopy evidences of the proteasome 20S subunit complexed with a imidazo[1,2-a]pyrimidine and the proteasome 20S subunit apo structures, shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:23:27.447Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MIEDHAEYGHNHYPQKLASSTLTLPKQGAKQQQWSPYQDNGGTTAAIAGKDFVILAGDTRLNGDYCLHSRHDQSKIFQLTPYTYMASNGMQADRLQLQQMLKYRVKWYQYNNGGRVPPTKAIAQLMSTLLYHRRFFPYYTFNMVVGLDEEGHGVCYSYDAVGSTEPFLYGTRGSAASFLEPVLDCLINRQHMTAQAPPEMTKEETLAMLKNAFTGAAERDIYTGDSVSFFIITKDGVQRESFELRKD","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"orfNames":[{"value":"LINJ_06_0140","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAM65445.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAM65445.1"}}]}]}],"alphafold_very_low_content":0.06882591093117409,"disorder_content":0.13360323886639677,"disprot_consensus":{"full":[{"start":1,"end":33,"type":"D"}],"Structural state":[{"start":1,"end":33,"type":"D"}]}},{"disprot_id":"DP03770","acc":"A4IBS2","creator":"vnugnes","date":"2022-09-13T19:33:05.857Z","features":{"pfam":[{"id":"PF00227","name":"Proteasome subunit","start":27,"end":207}],"gene3D":[]},"length":254,"name":"Proteasome subunit beta","ncbi_taxon_id":5671,"organism":"Leishmania infantum","regions":[{"start":1,"end":29,"reference_id":"30962368","reference_source":"pmid","reference_html":"Preclinical candidate for the treatment of visceral leishmaniasis that acts through proteasome inhibition. <i> Wyllie S, Brand S, Thomas M, De Rycker M, Chung CW, Pena I, Bingham RP, Bueren-Calabuig JA, Cantizani J, Cebrian D, Craggs PD, Ferguson L, Goswami P, Hobrath J, Howe J, Jeacock L, Ko EJ, Korczynska J, MacLean L, Manthri S, Martinez MS, Mata-Cantero L, Moniz S, Nühs A, Osuna-Cabello M, Pinto E, Riley J, Robinson S, Rowland P, Simeons FRC, Shishikura Y, Spinks D, Stojanovski L, Thomas J, Thompson S, Viayna Gaza E, Wall RJ, Zuccotto F, Horn D, Ferguson MAJ, Fairlamb AH, Fiandor JM, Martin J, Gray DW, Miles TJ, Gilbert IH, Read KD, Marco M, Wyatt PG. </i> Proc Natl Acad Sci U S A, 2019","date":"2022-09-13T19:34:26.807Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6QM8"}],"region_id":"DP03770r001","statement":[{"text":"The electron microscopy evidences of the proteasome 20S subunit apo structure shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:23:54.805Z"}},{"start":1,"end":29,"reference_id":"32667203","reference_source":"pmid","reference_html":"Discovery and Characterization of Clinical Candidate LXE408 as a Kinetoplastid-Selective Proteasome Inhibitor for the Treatment of Leishmaniases. <i> Nagle A, Biggart A, Be C, Srinivas H, Hein A, Caridha D, Sciotti RJ, Pybus B, Kreishman-Deitrick M, Bursulaya B, Lai YH, Gao MY, Liang F, Mathison CJN, Liu X, Yeh V, Smith J, Lerario I, Xie Y, Chianelli D, Gibney M, Berman A, Chen YL, Jiricek J, Davis LC, Liu X, Ballard J, Khare S, Eggimann FK, Luneau A, Groessl T, Shapiro M, Richmond W, Johnson K, Rudewicz PJ, Rao SPS, Thompson C, Tuntland T, Spraggon G, Glynne RJ, Supek F, Wiesmann C, Molteni V. </i> J Med Chem, 2020","date":"2022-09-14T15:25:10.507Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6TCZ"},{"db":"EMDB","id":"10462"}],"region_id":"DP03770r002","statement":[{"text":"The electron microscopy evidences of the proteasome 20S subunit complexed with an inhibitory compound (LXE408) shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:24:00.909Z"}}],"regions_counter":2,"released":"2022_12","sequence":"MPGFNFENVQRNLSLENEGYSAPRTLKTGTTIVGVVYKDGVVLGADTRATEGSIVADKCCRKIHYMAPNIMCCGAGTSADTEAVTNMVSSHLALHRLETGKQSRVLEALTLLKRHLYRYQGHVSAALVLGGVDVEGPFLATIAPHGSTDRLPFVTMGSGSIAAMAQLEVAYKDNMTCEEAKELVTSAIHKGIFNDPYSGTQVDVCVITKDKTELMIGYDTPNKRMHPRQEVMLPPGTTPVLKEEIRHLVDIVDV","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"orfNames":[{"value":"LINJ_35_3880","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAM72293.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAM72293.1"}}]}]}],"alphafold_very_low_content":0.007874015748031496,"disorder_content":0.1141732283464567,"disprot_consensus":{"full":[{"start":1,"end":29,"type":"D"}],"Structural state":[{"start":1,"end":29,"type":"D"}]}},{"disprot_id":"DP03771","acc":"Q8WQM6","creator":"vnugnes","date":"2022-09-13T19:48:46.470Z","features":{"pfam":[{"id":"PF14370","name":"C-terminal topoisomerase domain","start":195,"end":262}],"gene3D":[]},"length":262,"name":"DNA topoisomerase I-like protein","ncbi_taxon_id":5661,"organism":"Leishmania donovani","regions":[{"start":201,"end":210,"reference_id":"16487540","reference_source":"pmid","reference_html":"The structure of the transition state of the heterodimeric topoisomerase I of Leishmania donovani as a vanadate complex with nicked DNA. <i> Davies DR, Mushtaq A, Interthal H, Champoux JJ, Hol WG. </i> J Mol Biol, 2006","date":"2022-09-13T19:57:24.881Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"2B9S"}],"region_id":"DP03771r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9GPZ9"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46442","statements":[{"type":"Results","text":"The vanadate worked exactly as designed: the catalytic tyrosine residue of LdTOP1S is covalently joined via vanadate to the two strands of DNA that were designed to mimic the nicked scissile strand of the duplex."}],"entry_name":"vanadate(3-)"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"The “nicked” duplex DNA for the LdTOP1LS–vanadate–DNA complex was prepared by annealing three oligonucleotides with the sequences 5′ AAAAAGACTT 3′, 5′ AGAAAAATTTTT 3′, and 5′ AAAAATTTTTCTAAGTCTTTTT 3′."}]}],"statement":[{"text":"The LdTOP1S(201-262) model extends from Lys211 to Phe262, with 11 disordered side-chains.","type":"Results"}],"sequence_construct":"ENIIRIKDDNKAVSLGTSKINYIDPRIICSWAKAQDVPINKIFSATIQKKFPWAMNAENFDF","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:24:25.082Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MQPVQSPPVAPPSVPVAAPKKTPIDISALKLKMSPSVRATLAAAGVLGQCPRPIEAADEDALLKLKPMKTMVPSVKKVVAPVATTAPPPKVRRVESSSSSSSDSSSSSSDDDSSTDDSSGSDSSSYSSDDRSSSSAESVVSGEATLFHIAQSQGLVNKEVLTQEEEEVPTLVPPRPPVVRSFPNDIGKALERYRERLNREENIIRIKDDNKAVSLGTSKINYIDPRIICSWAKAQDVPINKIFSATIQKKFPWAMNAENFDF","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[],"alphafold_very_low_content":0.3511450381679389,"disorder_content":0.03816793893129771,"disprot_consensus":{"full":[{"start":201,"end":210,"type":"D"}],"Structural state":[{"start":201,"end":210,"type":"D"}]}},{"disprot_id":"DP03772","acc":"D0AB09","creator":"vnugnes","date":"2022-09-13T20:06:06.258Z","features":{"pfam":[{"id":"PF01233","name":"Myristoyl-CoA:protein N-myristoyltransferase, N-terminal domain","start":36,"end":213},{"id":"PF02799","name":"Myristoyl-CoA:protein N-myristoyltransferase, C-terminal domain","start":229,"end":412}],"gene3D":[]},"length":421,"name":"Glycylpeptide N-tetradecanoyltransferase","ncbi_taxon_id":5661,"organism":"Leishmania donovani","regions":[{"start":1,"end":10,"reference_id":"20036251","reference_source":"pmid","reference_html":"N-myristoyltransferase from Leishmania donovani: structural and functional characterisation of a potential drug target for visceral leishmaniasis. <i> Brannigan JA, Smith BA, Yu Z, Brzozowski AM, Hodgkinson MR, Maroof A, Price HP, Meier F, Leatherbarrow RJ, Tate EW, Smith DF, Wilkinson AJ. </i> J Mol Biol, 2010","date":"2022-09-13T20:13:34.319Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"2WUU"}],"region_id":"DP03772r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEMBL","id":"448516"}],"statement":[{"text":"There is a single LdNMT molecule in the asymmetric unit and the chain is well defined in the electron density maps, with the exception of residues 1–10 at the amino terminus and residues 83–85 and 334–339, which are not defined by the maps and assumed to be disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:24:43.787Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MSRNPSNSDAAHAFWSTQPVPQTEDETEKIVFAGPMDEPKTVADIPEEPYPIASTFEWWTPNMEAADDIHAIYELLRDNYVEDDDSMFRFNYSEEFLQWALCPPSYIPDWHVAVRRKADKKLLAFIAGVPVTLRMGTPKYMKVKAQEKGQEEEAAKYDAPRHICEINFLCVHKQLREKRLAPILIKEVTRRVNRTNVWQAVYTAGVLLPTPYASGQYFHRSLNPEKLVEIRFSGIPAQYQKFQNPMAMLKRNYQLPNAPKNSGLREMKPSDVPQVRRILMNYLDNFDVGPVFSDAEISHYLLPRDGVVFTYVVENDKKVTDFFSFYRIPSTVIGNSNYNILNAAYVHYYAATSMPLHQLILDLLIVAHSRGFDVCNMVEILDNRSFVEQLKFGAGDGHLRYYFYNWAYPKIKPSQVALVML","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"name":{"value":"nmt","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CBG76455.1","url":"https://www.ebi.ac.uk/ena/browser/view/CBG76455.1"}}]}}],"alphafold_very_low_content":0.021377672209026127,"disorder_content":0.023752969121140142,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"}]}},{"disprot_id":"DP03773","acc":"A0A024B7W1","creator":"fquaglia","date":"2022-09-14T10:33:40.820Z","features":{"pfam":[{"id":"PF00869","name":"Flavivirus glycoprotein, central and dimerisation domains","start":292,"end":592},{"id":"PF00948","name":"Flavivirus non-structural Protein NS1","start":797,"end":1148},{"id":"PF00949","name":"Peptidase S7, Flavivirus NS3 serine protease","start":1519,"end":1669},{"id":"PF00972","name":"Flavivirus RNA-directed RNA polymerase, fingers and palm domains","start":2772,"end":3222},{"id":"PF01002","name":"Flavivirus non-structural protein NS2B","start":1378,"end":1502},{"id":"PF01003","name":"Flavivirus capsid protein C","start":6,"end":122},{"id":"PF01004","name":"Flavivirus envelope glycoprotein M","start":217,"end":290},{"id":"PF01005","name":"Flavivirus non-structural protein NS2A","start":1158,"end":1280},{"id":"PF01349","name":"Flavivirus non-structural protein NS4B","start":2270,"end":2510},{"id":"PF01350","name":"Flavivirus non-structural protein NS4A","start":2126,"end":2268},{"id":"PF01570","name":"Flavivirus polyprotein propeptide","start":130,"end":214},{"id":"PF01728","name":"FtsJ-like methyltransferase","start":2575,"end":2744},{"id":"PF02832","name":"Flavivirus glycoprotein, immunoglobulin-like domain","start":594,"end":692},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1687,"end":1833},{"id":"PF20483","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","start":3226,"end":3389},{"id":"PF20907","name":"Flavivirus NS3 helicase, C-terminal helical domain","start":1975,"end":2117},{"id":"PF21659","name":"Flavivirus envelope glycoprotein E, stem/anchor domain","start":695,"end":789}],"gene3D":[]},"length":3423,"name":"Genome polyprotein","ncbi_taxon_id":2043570,"organism":"Zika virus (isolate ZIKV/Human/French Polynesia/10087PF/2013)","regions":[{"start":2396,"end":2434,"reference_id":"36037701","reference_source":"pmid","reference_html":"Investigating the conformational dynamics of Zika virus NS4B protein. <i> Bhardwaj T, Kumar P, Giri R. </i> Virology, 2022","date":"2022-09-16T08:04:32.836Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP03773r001","statement":[{"text":"Further, using a series of circular dichroism spectroscopic experiments, we validate the cytosolic region as an intrinsically disordered protein region. ","type":"Abstract"},{"text":"We experimentally validated NS4B-CR peptide to remain in disordered conformation in buffered conditions. Far-UV CD spectrum where negative ellipticity near 198 nm is indicative of its flexible nature is shown in Fig. 8A.","type":"Results"},{"text":"The cytosolic region NS4B-CR (residues 131–169) of Zika virus NS4B protein corresponds to residues 2396-2434 of Zika virus Genome polyprotein.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-16T14:01:02.167Z"}},{"start":2396,"end":2434,"reference_id":"36037701","reference_source":"pmid","reference_html":"Investigating the conformational dynamics of Zika virus NS4B protein. <i> Bhardwaj T, Kumar P, Giri R. </i> Virology, 2022","date":"2022-09-16T08:07:21.812Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP03773r002","statement":[{"text":"To analyze the ability of NS4B-CR peptide to interact with cellular lipid molecules, we studied its behavior in the presence of lipids and artificial membrane forming SDS micelles (Tulumello and Deber, 2009). As shown in Fig. 9A and B, the maximum negative ellipticity of CD spectra of NS4B-CR peptide under the influence of SDS micelles shifts from wavelength 198.5 nm to 201.6 nm. This indicates the formation of a pre-molten globule structure in SDS.","type":"Results"},{"text":"The cytosolic region NS4B-CR (residues 131–169) of Zika virus NS4B protein corresponds to residues 2396-2434 of Zika virus Genome polyprotein.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"8984","entry_name":"sodium dodecyl sulfate"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-16T13:59:59.495Z"}},{"start":2396,"end":2434,"reference_id":"36037701","reference_source":"pmid","reference_html":"Investigating the conformational dynamics of Zika virus NS4B protein. <i> Bhardwaj T, Kumar P, Giri R. </i> Virology, 2022","date":"2022-09-16T08:07:07.344Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000019","term_name":"disorder to pre-molten globule","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP03773r003","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"8984","entry_name":"sodium dodecyl sulfate"}],"statement":[{"text":"To analyze the ability of NS4B-CR peptide to interact with cellular lipid molecules, we studied its behavior in the presence of lipids and artificial membrane forming SDS micelles (Tulumello and Deber, 2009). As shown in Fig. 9A and B, the maximum negative ellipticity of CD spectra of NS4B-CR peptide under the influence of SDS micelles shifts from wavelength 198.5 nm to 201.6 nm. This indicates the formation of a pre-molten globule structure in SDS.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-16T14:01:07.631Z"}},{"start":2396,"end":2434,"reference_id":"36037701","reference_source":"pmid","reference_html":"Investigating the conformational dynamics of Zika virus NS4B protein. <i> Bhardwaj T, Kumar P, Giri R. </i> Virology, 2022","date":"2022-09-16T08:11:06.532Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","region_id":"DP03773r004","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"8984","entry_name":"sodium dodecyl sulfate"}],"statement":[{"text":"To analyze the ability of NS4B-CR peptide to interact with cellular lipid molecules, we studied its behavior in the presence of lipids and artificial membrane forming SDS micelles (Tulumello and Deber, 2009). As shown in Fig. 9A and B, the maximum negative ellipticity of CD spectra of NS4B-CR peptide under the influence of SDS micelles shifts from wavelength 198.5 nm to 201.6 nm. This indicates the formation of a pre-molten globule structure in SDS.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-16T14:01:32.748Z"}},{"start":2927,"end":2941,"reference_id":"32796069","reference_source":"pmid","reference_html":"Non-nucleoside Inhibitors of Zika Virus RNA-Dependent RNA Polymerase.  <i> Gharbi-Ayachi A, Santhanakrishnan S, Wong YH, Chan KWK, Tan ST, Bates RW, Vasudevan SG, El Sahili A, Lescar J. </i> J Virol, 2020","date":"2022-10-11T14:39:58.968Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6LD1"}],"region_id":"DP03773r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":"ethylene glycol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"The PDB evidence of the free Zika NS5 polymerase domain shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:27:38.456Z"}},{"start":2979,"end":2992,"reference_id":"32796069","reference_source":"pmid","reference_html":"Non-nucleoside Inhibitors of Zika Virus RNA-Dependent RNA Polymerase.  <i> Gharbi-Ayachi A, Santhanakrishnan S, Wong YH, Chan KWK, Tan ST, Bates RW, Vasudevan SG, El Sahili A, Lescar J. </i> J Virol, 2020","date":"2022-10-11T14:40:25.881Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6LD1"}],"region_id":"DP03773r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":"ethylene glycol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"The PDB evidence of the free Zika NS5 polymerase domain shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:27:40.784Z"}},{"start":966,"end":1065,"reference_id":"33414219","reference_source":"pmid","reference_html":"A broadly protective antibody that targets the flavivirus NS1 protein. <i> Modhiran N, Song H, Liu L, Bletchly C, Brillault L, Amarilla AA, Xu X, Qi J, Chai Y, Cheung STM, Traves R, Setoh YX, Bibby S, Scott CAP, Freney ME, Newton ND, Khromykh AA, Chappell KJ, Muller DA, Stacey KJ, Landsberg MJ, Shi Y, Gao GF, Young PR, Watterson D. </i> Science, 2021","date":"2022-10-11T15:13:56.613Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"7BSD"}],"region_id":"DP03773r007","sample":[{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting antibody 1G5.3 Fab."}]}],"statement":[{"text":"For ZIKV, the first half of NS1c and the terminal residues beyond 339 were not resolved (Fig. 1C).","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:27:42.607Z"}}],"regions_counter":7,"released":"2022_12","sequence":"MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEIIKKFKKDLAAMLRIINARKEKKRRGADTSVGIVGLLLTTAMAAEVTRRGSAYYMYLDRNDAGEAISFPTTLGMNKCYIQIMDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGCVTVMAQDKPTVDIELVTTTVSNMAEVRSYCYEASISDMASDSRCPTQGEAYLDKQSDTQYVCKRTLVDRGWGNGCGLFGKGSLVTCAKFACSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIVNDTGHETDENRAKVEITPNSPRAEATLGGFGSLGLDCEPRTGLDFSDLYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKEALVEFKDAHAKRQTVVVLGSQEGAVHTALAGALEAEMDGAKGRLSSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGSTIGKAFEATVRGAKRMAVLGDTAWDFGSVGGALNSLGKGIHQIFGAAFKSLFGGMSWFSQILIGTLLMWLGLNTKNGSISLMCLALGGVLIFLSTAVSADVGCSVDFSKKETRCGTGVFVYNDVEAWRDRYKYHPDSPRRLAAAVKQAWEDGICGISSVSRMENIMWRSVEGELNAILEENGVQLTVVVGSVKNPMWRGPQRLPVPVNELPHGWKAWGKSYFVRAAKTNNSFVVDGDTLKECPLKHRAWNSFLVEDHGFGVFHTSVWLKVREDYSLECDPAVIGTAVKGKEAVHSDLGYWIESEKNDTWRLKRAHLIEMKTCEWPKSHTLWTDGIEESDLIIPKSLAGPLSHHNTREGYRTQMKGPWHSEELEIRFEECPGTKVHVEETCGTRGPSLRSTTASGRVIEEWCCRECTMPPLSFRAKDGCWYGMEIRPRKEPESNLVRSMVTAGSTDHMDHFSLGVLVILLMVQEGLKKRMTTKIIISTSMAVLVAMILGGFSMSDLAKLAILMGATFAEMNTGGDVAHLALIAAFKVRPALLVSFIFRANWTPRESMLLALASCLLQTAISALEGDLMVLINGFALAWLAIRAMVVPRTDNITLAILAALTPLARGTLLVAWRAGLATCGGFMLLSLKGKGSVKKNLPFVMALGLTAVRLVDPINVVGLLLLTRSGKRSWPPSEVLTAVGLICALAGGFAKADIEMAGPMAAVGLLIVSYVVSGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEDDGPPMREIILKVVLMTICGMNPIAIPFAAGAWYVYVKTGKRSGALWDVPAPKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGSALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWDGHSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGRREEETPVECFEPSMLKKKQLTVLDLHPGAGKTRRVLPEIVREAIKTRLRTVILAPTRVVAAEMEEALRGLPVRYMTTAVNVTHSGTEIVDLMCHATFTSRLLQPIRVPNYNLYIMDEAHFTDPSSIAARGYISTRVEMGEAAAIFMTATPPGTRDAFPDSNSPIMDTEVEVPERAWSSGFDWVTDHSGKTVWFVPSVRNGNEIAACLTKAGKRVIQLSRKTFETEFQKTKHQEWDFVVTTDISEMGANFKADRVIDSRRCLKPVILDGERVILAGPMPVTHASAAQRRGRIGRNPNKPGDEYLYGGGCAETDEDHAHWLEARMLLDNIYLQDGLIASLYRPEADKVAAIEGEFKLRTEQRKTFVELMKRGDLPVWLAYQVASAGITYTDRRWCFDGTTNNTIMEDSVPAEVWTRHGEKRVLKPRWMDARVCSDHAALKSFKEFAAGKRGAAFGVMEALGTLPGHMTERFQEAIDNLAVLMRAETGSRPYKAAAAQLPETLETIMLLGLLGTVSLGIFFVLMRNKGIGKMGFGMVTLGASAWLMWLSEIEPARIACVLIVVFLLLVVLIPEPEKQRSPQDNQMAIIIMVAVGLLGLITANELGWLERTKSDLSHLMGRREEGATIGFSMDIDLRPASAWAIYAALTTFITPAVQHAVTTSYNNYSLMAMATQAGVLFGMGKGMPFYAWDFGVPLLMIGCYSQLTPLTLIVAIILLVAHYMYLIPGLQAAAARAAQKRTAAGIMKNPVVDGIVVTDIDTMTIDPQVEKKMGQVLLIAVAVSSAILSRTAWGWGEAGALITAATSTLWEGSPNKYWNSSTATSLCNIFRGSYLAGASLIYTVTRNAGLVKRRGGGTGETLGEKWKARLNQMSALEFYSYKKSGITEVCREEARRALKDGVATGGHAVSRGSAKLRWLVERGYLQPYGKVIDLGCGRGGWSYYAATIRKVQEVKGYTKGGPGHEEPMLVQSYGWNIVRLKSGVDVFHMAAEPCDTLLCDIGESSSSPEVEEARTLRVLSMVGDWLEKRPGAFCIKVLCPYTSTMMETLERLQRRYGGGLVRVPLSRNSTHEMYWVSGAKSNTIKSVSTTSQLLLGRMDGPRRPVKYEEDVNLGSGTRAVVSCAEAPNMKIIGNRIERIRSEHAETWFFDENHPYRTWAYHGSYEAPTQGSASSLINGVVRLLSKPWDVVTGVTGIAMTDTTPYGQQRVFKEKVDTRVPDPQEGTRQVMSMVSSWLWKELGKHKRPRVCTKEEFINKVRSNAALGAIFEEEKEWKTAVEAVNDPRFWALVDKEREHHLRGECQSCVYNMMGKREKKQGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMGRENSGGGVEGLGLQRLGYVLEEMSRIPGGRMYADDTAGWDTRISRFDLENEALITNQMEKGHRALALAIIKYTYQNKVVKVLRPAEKGKTVMDIISRQDQRGSGQVVTYALNTFTNLVVQLIRNMEAEEVLEMQDLWLLRRSEKVTNWLQSNGWDRLKRMAVSGDDCVVKPIDDRFAHALRFLNDMGKVRKDTQEWKPSTGWDNWEEVPFCSHHFNKLHLKDGRSIVVPCRHQDELIGRARVSPGAGWSIRETACLAKSYAQMWQLLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLVVWNRVWIEENDHMEDKTPVTKWTDIPYLGKREDLWCGSLIGHRPRTTWAENIKNTVNMVRRIIGDEEKYMDYLSTQVRYLGEEGSTPGVL","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Flavivirus"],"dataset":["Viral proteins","Neglected tropical diseases proteins","RNA-binding proteins"],"genes":[],"disorder_content":0.049079754601226995,"disprot_consensus":{"full":[{"start":966,"end":1065,"type":"D"},{"start":2396,"end":2434,"type":"T"},{"start":2927,"end":2941,"type":"D"},{"start":2979,"end":2992,"type":"D"}],"Structural state":[{"start":966,"end":1065,"type":"D"},{"start":2396,"end":2434,"type":"D"},{"start":2927,"end":2941,"type":"D"},{"start":2979,"end":2992,"type":"D"}],"Structural transition":[{"start":2396,"end":2434,"type":"T"}],"Molecular function":[{"start":2396,"end":2434,"type":"F"}]}},{"disprot_id":"DP03774","acc":"A0A504X6A3","creator":"vnugnes","date":"2022-09-14T15:11:18.827Z","features":{"pfam":[{"id":"PF00227","name":"Proteasome subunit","start":51,"end":229}],"gene3D":[]},"length":283,"name":"Proteasome subunit beta","ncbi_taxon_id":5661,"organism":"Leishmania donovani","regions":[{"start":1,"end":54,"reference_id":"32667203","reference_source":"pmid","reference_html":"Discovery and Characterization of Clinical Candidate LXE408 as a Kinetoplastid-Selective Proteasome Inhibitor for the Treatment of Leishmaniases. <i> Nagle A, Biggart A, Be C, Srinivas H, Hein A, Caridha D, Sciotti RJ, Pybus B, Kreishman-Deitrick M, Bursulaya B, Lai YH, Gao MY, Liang F, Mathison CJN, Liu X, Yeh V, Smith J, Lerario I, Xie Y, Chianelli D, Gibney M, Berman A, Chen YL, Jiricek J, Davis LC, Liu X, Ballard J, Khare S, Eggimann FK, Luneau A, Groessl T, Shapiro M, Richmond W, Johnson K, Rudewicz PJ, Rao SPS, Thompson C, Tuntland T, Spraggon G, Glynne RJ, Supek F, Wiesmann C, Molteni V. </i> J Med Chem, 2020","date":"2022-09-14T15:13:35.300Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"EMDB","id":"10462"},{"db":"PDB","id":"6TCZ"}],"region_id":"DP03774r001","statement":[{"text":"The electron microscopy evidences of the proteasome 20S subunit complexed with an inhibitory compound (LXE408) shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:28:26.546Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MLQRPDHTLLQDPSYPKDIEQKLTENGPAQAGKQLFQPDLAVIDPQLSEAVSLGTTILAVSYKGGVVLAADSRTSSGTYVVNRASNKLTKLTEKIYCCRSGSAADTQALAERVSNYLGSYQTDIGADVNVATAANLFHKMCYVNRWNISAGIIVAGYDPINGGSVYSIPSGGSCVKLDYALGGSGSIFLYSFFDANYKPGMSKSECVAFCQRAVAHAYSRDGSSGGLIRTITLDAEEAEDLTVPWKRSPYCMEKDPKYQVQAVQNPPFSSSAKVTGNRMSSTG","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"orfNames":[{"value":"CGC20_24015","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TPP44280.1","url":"https://www.ebi.ac.uk/ena/browser/view/TPP44280.1"}}]},{"value":"CGC21_10040","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TPP43155.1","url":"https://www.ebi.ac.uk/ena/browser/view/TPP43155.1"}}]},{"value":"LDHU3_12.0050","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAC5428242.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAC5428242.1"}}]}]}],"alphafold_very_low_content":0.17314487632508835,"disorder_content":0.19081272084805653,"disprot_consensus":{"full":[{"start":1,"end":54,"type":"D"}],"Structural state":[{"start":1,"end":54,"type":"D"}]}},{"disprot_id":"DP03775","acc":"A0A3S7WPD8","creator":"vnugnes","date":"2022-09-14T15:30:12.627Z","features":{"pfam":[{"id":"PF00227","name":"Proteasome subunit","start":40,"end":232}],"gene3D":[]},"length":247,"name":"Proteasome subunit beta","ncbi_taxon_id":5661,"organism":"Leishmania donovani","regions":[{"start":1,"end":33,"reference_id":"32667203","reference_source":"pmid","reference_html":"Discovery and Characterization of Clinical Candidate LXE408 as a Kinetoplastid-Selective Proteasome Inhibitor for the Treatment of Leishmaniases. <i> Nagle A, Biggart A, Be C, Srinivas H, Hein A, Caridha D, Sciotti RJ, Pybus B, Kreishman-Deitrick M, Bursulaya B, Lai YH, Gao MY, Liang F, Mathison CJN, Liu X, Yeh V, Smith J, Lerario I, Xie Y, Chianelli D, Gibney M, Berman A, Chen YL, Jiricek J, Davis LC, Liu X, Ballard J, Khare S, Eggimann FK, Luneau A, Groessl T, Shapiro M, Richmond W, Johnson K, Rudewicz PJ, Rao SPS, Thompson C, Tuntland T, Spraggon G, Glynne RJ, Supek F, Wiesmann C, Molteni V. </i> J Med Chem, 2020","date":"2022-09-14T15:48:16.002Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6TD5"},{"db":"PDB","id":"6TCZ"},{"db":"EMDB","id":"10462"}],"region_id":"DP03775r001","sequence_construct":"MASSSPPLLPFSSFVVAVVAIHLSFRVFCVGAQSLCKCCSCVPACALPLCFSSSPSVSAEDVALALFAHPKVLTHRPTARYSPILSLLHYAVMIEDHAEYGHNYYPQKLASSTLTLPQQGAKQQQWSPYQDNGGTTAAIAGKDFVILAGDTRLNGDFCLHSRHDQSKIFQLTPYTYMASNGMQADRLQLQQMLKYRVKWYKYNNGGKVPSTKAIAQLMSTMLYHRRFFPYYTFNMVVGLDEEGHGVCYSYDAVGSTEPFLYGTRGSAASFVEPLLDCLINRQHMTSQAPPEMTKEETLAMLKNAFTGAAERDIYTGDSVSFFIITKDGVQQESFELRKD","statement":[{"text":"The electron microscopy evidences of the proteasome 20S subunit complexed with the inhibitory compounds LXE408 and bortezomib shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:28:58.546Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MIEDHAEYGHNHYPQKLASSTLTLPKQGAKQQQWSPYQDNGGTTAAIAGKDFVILAGDTRLNGDYCLHSRHDQSKIFQLTPYTYMASNGMQADRLQLQQMLKYRVKWYQYNNGGRVPPTKAIAQLMSTMLYHRRFFPYYTFNMVVGLDEEGHGVCYSYDAVGSTEPFLYGTRGSAASFLEPVLDCLINRQHMTAQAPPEMTKEETLAMLKNAFTGAAERDIYTGDSVSFFIITKDGVQRESFELRKD","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"orfNames":[{"value":"CGC20_20280","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TPP49814.1","url":"https://www.ebi.ac.uk/ena/browser/view/TPP49814.1"}}]},{"value":"CGC21_24485","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TPP54890.1","url":"https://www.ebi.ac.uk/ena/browser/view/TPP54890.1"}}]},{"value":"LdCL_060006300","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AYU76043.1","url":"https://www.ebi.ac.uk/ena/browser/view/AYU76043.1"}}]},{"value":"LDHU3_06.0180","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAC5427394.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAC5427394.1"}}]}]}],"alphafold_very_low_content":0.06477732793522267,"disorder_content":0.13360323886639677,"disprot_consensus":{"full":[{"start":1,"end":33,"type":"D"}],"Structural state":[{"start":1,"end":33,"type":"D"}]}},{"disprot_id":"DP03776","acc":"A0A504Y5E1","creator":"vnugnes","date":"2022-09-14T15:51:15.478Z","features":{"pfam":[{"id":"PF00227","name":"Proteasome subunit","start":29,"end":221},{"id":"PF10584","name":"Proteasome subunit A N-terminal signature","start":5,"end":27}],"gene3D":[]},"length":285,"name":"Proteasome subunit alpha type","ncbi_taxon_id":5661,"organism":"Leishmania donovani","regions":[{"start":274,"end":285,"reference_id":"32667203","reference_source":"pmid","reference_html":"Discovery and Characterization of Clinical Candidate LXE408 as a Kinetoplastid-Selective Proteasome Inhibitor for the Treatment of Leishmaniases. <i> Nagle A, Biggart A, Be C, Srinivas H, Hein A, Caridha D, Sciotti RJ, Pybus B, Kreishman-Deitrick M, Bursulaya B, Lai YH, Gao MY, Liang F, Mathison CJN, Liu X, Yeh V, Smith J, Lerario I, Xie Y, Chianelli D, Gibney M, Berman A, Chen YL, Jiricek J, Davis LC, Liu X, Ballard J, Khare S, Eggimann FK, Luneau A, Groessl T, Shapiro M, Richmond W, Johnson K, Rudewicz PJ, Rao SPS, Thompson C, Tuntland T, Spraggon G, Glynne RJ, Supek F, Wiesmann C, Molteni V. </i> J Med Chem, 2020","date":"2022-09-14T16:01:33.390Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6TD5"},{"db":"PDB","id":"6TCZ"},{"db":"EMDB","id":"10462"}],"region_id":"DP03776r001","statement":[{"text":"The electron microscopy evidences of the proteasome 20S subunit complexed with the inhibitory compounds LXE408 and bortezomib shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:29:26.965Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MSHRYDSRTTTFSPEGRLYQVEYAVEAIQQAGTVIGVCTKDGVVLAGEKMVPHPLFDSENMQDKNTSGEKMYKIAEHIGCSVAGVTSDAYALLNYARLSALRHQYTFQEPMAIEDLCRILCDEKQLYTQYGGVRPYGVSFLLVGWDRYYGYQLYSTEPSGDYSAWSAYAIGQNDQVAHSLLKKDWHENMTLEDGMLLALRVLGKTMDTAKIDLGRVEVAVMRKVPASNVDQLLDPFKHHPKTTPQFQILALSELKPHAERADQAREAEEQAEAERQRQQEQALES","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"orfNames":[{"value":"CGC20_38795","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TPP53520.1","url":"https://www.ebi.ac.uk/ena/browser/view/TPP53520.1"}}]},{"value":"LDHU3_14.0400","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAC5428569.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAC5428569.1"}}]}]}],"alphafold_very_low_content":0,"disorder_content":0.042105263157894736,"disprot_consensus":{"full":[{"start":274,"end":285,"type":"D"}],"Structural state":[{"start":274,"end":285,"type":"D"}]}},{"disprot_id":"DP03777","acc":"Q9TXA6","creator":"vnugnes","date":"2022-09-14T17:51:32.220Z","features":{"pfam":[{"id":"PF00366","name":"Ribosomal protein S17","start":56,"end":124},{"id":"PF16205","name":"Ribosomal_S17 N-terminal","start":7,"end":54}],"gene3D":[]},"length":141,"name":"40S ribosomal protein S11, putative","ncbi_taxon_id":5661,"organism":"Leishmania donovani","regions":[{"start":129,"end":141,"reference_id":"29150609","reference_source":"pmid","reference_html":"Atomic resolution snapshot of Leishmania ribosome inhibition by the aminoglycoside paromomycin. <i> Shalev-Benami M, Zhang Y, Rozenberg H, Nobe Y, Taoka M, Matzov D, Zimmerman E, Bashan A, Isobe T, Jaffe CL, Yonath A, Skiniotis G. </i> Nat Commun, 2017","date":"2022-09-14T17:55:16.798Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"EMDB","id":"7024"},{"db":"PDB","id":"6AZ1"}],"region_id":"DP03777r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"7934","entry_name":"paromomycin"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"}],"statement":[{"text":"The electron microscopy evidences of the small subunit of Leishmania ribosome bound to paromomycin shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:30:03.963Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MHRPSRKHVNKSGHIRYSKKIGLGFKTPAKALNGKYIDRKCPFTSNVVIRGRILRGVVHSTKMHRTIIIRRNYLHFIKKYQRYQKRHKSLAVHCSPAFDPKQGDEVVIGQCRPLSKTIRYNVLEVVSKSSADKMGKKFAKN","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"orfNames":[{"value":"LdCL_200021000","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AYU78444.1","url":"https://www.ebi.ac.uk/ena/browser/view/AYU78444.1"}}]},{"value":"LdCL_210023700","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AYU78644.1","url":"https://www.ebi.ac.uk/ena/browser/view/AYU78644.1"}}]},{"value":"LDHU3_20.1990","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAC5429717.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAC5429717.1"}}]},{"value":"LDHU3_21.2120","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAC5429914.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAC5429914.1"}}]}]}],"alphafold_very_low_content":0.028368794326241134,"disorder_content":0.09219858156028368,"disprot_consensus":{"full":[{"start":129,"end":141,"type":"D"}],"Structural state":[{"start":129,"end":141,"type":"D"}]}},{"disprot_id":"DP03778","acc":"O44012","creator":"vnugnes","date":"2022-09-14T17:55:55.886Z","features":{"pfam":[{"id":"PF01092","name":"Ribosomal protein S6e","start":1,"end":129}],"gene3D":[]},"length":249,"name":"40S ribosomal protein S6","ncbi_taxon_id":5671,"organism":"Leishmania infantum","regions":[{"start":239,"end":249,"reference_id":"29150609","reference_source":"pmid","reference_html":"Atomic resolution snapshot of Leishmania ribosome inhibition by the aminoglycoside paromomycin. <i> Shalev-Benami M, Zhang Y, Rozenberg H, Nobe Y, Taoka M, Matzov D, Zimmerman E, Bashan A, Isobe T, Jaffe CL, Yonath A, Skiniotis G. </i> Nat Commun, 2017","date":"2022-09-14T17:57:22.297Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"EMDB","id":"7024"},{"db":"PDB","id":"6AZ1"}],"region_id":"DP03778r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"7934","entry_name":"paromomycin"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"}],"statement":[{"text":"The electron microscopy evidences of the small subunit of Leishmania ribosome bound to paromomycin shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:30:25.373Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MYLNIAYPRNGTVKQFEISDEVLRRVQLQDYRLGNEVDGAIFGSEFKGYIFRLRGGSDKDGFPMVPGVLASSRVSLLVKRGAIGFNTFRGYQGERRRKNVRGCVLASDIALVNVTISKVGDQPIEGVTDTTAPRRLGPKRASKIRKLFNLSRTEDVRKYVVRRRVVKSGKKDRLKAPKIQRLITPRVKARRAKKAKDAIAKVRASAAERREYLRLIASNRRALRQRDHSKKHTQKVHAQRAEVAAFQKK","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"name":{"value":"RPS6"},"synonyms":[{"value":"RS6"}]}],"alphafold_very_low_content":0,"disorder_content":0.04417670682730924,"disprot_consensus":{"full":[{"start":239,"end":249,"type":"D"}],"Structural state":[{"start":239,"end":249,"type":"D"}]}},{"disprot_id":"DP03779","acc":"A4IDS4","creator":"vnugnes","date":"2022-09-14T17:58:17.696Z","features":{"pfam":[{"id":"PF00318","name":"Ribosomal protein S2","start":116,"end":184}],"gene3D":[]},"length":246,"name":"40S ribosomal protein SA","ncbi_taxon_id":5671,"organism":"Leishmania infantum","regions":[{"start":212,"end":246,"reference_id":"29150609","reference_source":"pmid","reference_html":"Atomic resolution snapshot of Leishmania ribosome inhibition by the aminoglycoside paromomycin. <i> Shalev-Benami M, Zhang Y, Rozenberg H, Nobe Y, Taoka M, Matzov D, Zimmerman E, Bashan A, Isobe T, Jaffe CL, Yonath A, Skiniotis G. </i> Nat Commun, 2017","date":"2022-09-14T17:59:50.920Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"EMDB","id":"7024"},{"db":"PDB","id":"6AZ1"}],"region_id":"DP03779r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"7934","entry_name":"paromomycin"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"}],"statement":[{"text":"The electron microscopy evidences of the small subunit of Leishmania ribosome bound to paromomycin shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:30:45.215Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MTAVESGSKVLRMKESDAQKLLAMRCHIGTRNQSSAMKKYIYGRTAEGSHIIDLHMMWEKLILAARVIAAVENPKDVCVCSSRLYGTRAIYKFSQHVGTSFHGGRFIPGTFTNQIQKKFVQPRVLVVTDPRTDHQAIREASLVNIPVIALCDTDAPLEYVDIAIPCNNRGIKSIGMMYWLLAREVLRLRGTIVRSVPWEEKVDLFFYRDPNEAAEEKAAAAAAAPAAEAEEGFGWVERNDDNAWEA","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"orfNames":[{"value":"LinJ36.5570"},{"value":"LinJ_36_5240"}]},{"orfNames":[{"value":"LinJ36.5680"},{"value":"LinJ_36_5350"}]}],"alphafold_very_low_content":0.10975609756097561,"disorder_content":0.14227642276422764,"disprot_consensus":{"full":[{"start":212,"end":246,"type":"D"}],"Structural state":[{"start":212,"end":246,"type":"D"}]}},{"disprot_id":"DP03780","acc":"D1M863","creator":"vnugnes","date":"2022-09-14T18:21:44.007Z","features":{"pfam":[{"id":"PF00276","name":"Ribosomal protein L23","start":64,"end":124}],"gene3D":[]},"length":145,"name":"60S ribosomal protein L23a","ncbi_taxon_id":5661,"organism":"Leishmania donovani","regions":[{"start":1,"end":25,"reference_id":"27752045","reference_source":"pmid","reference_html":"Structures and stabilization of kinetoplastid-specific split rRNAs revealed by comparing leishmanial and human ribosomes. <i> Zhang X, Lai M, Chang W, Yu I, Ding K, Mrazek J, Ng HL, Yang OO, Maslov DA, Zhou ZH. </i> Nat Commun, 2016","date":"2022-09-14T18:23:40.286Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"EMDB","id":"8343"},{"db":"PDB","id":"5T2A"}],"region_id":"DP03780r001","statement":[{"text":"The electron microscopy evidences of the small subunit of the Leishmania donovani 80S ribosome shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:31:52.627Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MPPAQKTVKKAAPKDAKATKVVKVSTRKAYTRPQFRRPHTYRKPATAKPSNRVTVESKDIAAFNVIRYPLTTDKAMKKIEENNTLTFIVDARANKTEIKKAIRKLYQVKAVKVNTLIRPDGLKKAYIRLSAAHDALDTANKIGLV","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[],"alphafold_very_low_content":0.10344827586206896,"disorder_content":0.1724137931034483,"disprot_consensus":{"full":[{"start":1,"end":25,"type":"D"}],"Structural state":[{"start":1,"end":25,"type":"D"}]}},{"disprot_id":"DP03781","acc":"Q6QDB5","creator":"vnugnes","date":"2022-09-14T19:11:53.012Z","features":{"pfam":[{"id":"PF00106","name":"short chain dehydrogenase","start":8,"end":70},{"id":"PF13561","name":"Enoyl-(Acyl carrier protein) reductase","start":83,"end":284}],"gene3D":[]},"length":288,"name":"Pteridine reductase","ncbi_taxon_id":5661,"organism":"Leishmania donovani","regions":[{"start":70,"end":80,"reference_id":"21206018","reference_source":"pmid","reference_html":"Structure of recombinant Leishmania donovani pteridine reductase reveals a disordered active site. <i> Barrack KL, Tulloch LB, Burke LA, Fyfe PK, Hunter WN. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2011","date":"2022-09-14T19:15:25.667Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"2XOX"}],"region_id":"DP03781r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"Missing segments include residues 70–80 (the loop linking β3 and α3), 112–132 (the β4–α4 loop) and 227–254 (the β6–α6 loop).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-12T08:45:00.899Z"}},{"start":112,"end":132,"reference_id":"21206018","reference_source":"pmid","reference_html":"Structure of recombinant Leishmania donovani pteridine reductase reveals a disordered active site. <i> Barrack KL, Tulloch LB, Burke LA, Fyfe PK, Hunter WN. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2011","date":"2022-09-14T19:15:36.061Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"2XOX"}],"region_id":"DP03781r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"Missing segments include residues 70–80 (the loop linking β3 and α3), 112–132 (the β4–α4 loop) and 227–254 (the β6–α6 loop).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-12T08:45:02.420Z"}},{"start":227,"end":254,"reference_id":"21206018","reference_source":"pmid","reference_html":"Structure of recombinant Leishmania donovani pteridine reductase reveals a disordered active site. <i> Barrack KL, Tulloch LB, Burke LA, Fyfe PK, Hunter WN. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2011","date":"2022-09-14T19:15:48.283Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"2XOX"}],"region_id":"DP03781r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"Missing segments include residues 70–80 (the loop linking β3 and α3), 112–132 (the β4–α4 loop) and 227–254 (the β6–α6 loop).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-12T08:45:04.141Z"}}],"regions_counter":3,"released":"2022_12","sequence":"MTAPTVPVALVTGAAKRLGSGIAEGLHAEGYAVCLHYHRSAAEANTLAATLNARRPNSAITVQADLSNVAKAPAGGADGAAPVTLFKRCADLVAACYTHWGRCDVLVNNASSFYPTPLLRKDEDGHVPCVGDREAMEAAAADLFGSNAMAPYFLIKAFAHRVADTPAEQRGTNYSIVNMVDAMTSQPLLGYTIYTMAKGALEGLTRSAALELAPLQIRVNGVGPGLSVLADDMPPAVREDYRSKVPLYQRDSSAAEVSDVVIFLCSSKAKYVTGTCVKVDGGYSLTRA","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[],"alphafold_very_low_content":0.010416666666666666,"disorder_content":0.20833333333333334,"disprot_consensus":{"full":[{"start":70,"end":80,"type":"D"},{"start":112,"end":132,"type":"D"},{"start":227,"end":254,"type":"D"}],"Structural state":[{"start":70,"end":80,"type":"D"},{"start":112,"end":132,"type":"D"},{"start":227,"end":254,"type":"D"}]}},{"disprot_id":"DP03782","acc":"B5TV91","creator":"vnugnes","date":"2022-09-15T13:10:13.828Z","features":{"pfam":[{"id":"PF00705","name":"Proliferating cell nuclear antigen, N-terminal domain","start":1,"end":124},{"id":"PF02747","name":"Proliferating cell nuclear antigen, C-terminal domain","start":127,"end":196},{"id":"PF02747","name":"Proliferating cell nuclear antigen, C-terminal domain","start":227,"end":287}],"gene3D":[]},"length":292,"name":"Proliferating cell nuclear antigen","ncbi_taxon_id":5661,"organism":"Leishmania donovani","regions":[{"start":186,"end":226,"reference_id":"28844736","reference_source":"pmid","reference_html":"Structure and binding studies of proliferating cell nuclear antigen from Leishmania donovani. <i> Yadav SP, Singh PK, Sharma P, Iqbal N, Kaur P, Sharma S, Singh TP. </i> Biochim Biophys Acta Proteins Proteom, 2017","date":"2022-09-15T13:12:19.081Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"5H0T"}],"region_id":"DP03782r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46807","entry_name":"diethylene glycol"}],"statement":[{"text":"The whole molecule was traced with help of electron density map but there was a poor electron density for 41-residue long segment (186–226) and hence it could not be defined.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:34:16.557Z"}},{"start":118,"end":134,"reference_id":"28844736","reference_source":"pmid","reference_html":"Structure and binding studies of proliferating cell nuclear antigen from Leishmania donovani. <i> Yadav SP, Singh PK, Sharma P, Iqbal N, Kaur P, Sharma S, Singh TP. </i> Biochim Biophys Acta Proteins Proteom, 2017","date":"2022-09-15T13:16:00.334Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006222","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"5H0T"}],"region_id":"DP03782r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46807","entry_name":"diethylene glycol"}],"statement":[{"text":"The average value of the B-factor for the atoms of the IDCL loop in LdPCNA is 114 Å2 whereas as the average B-factor for rest of the protein atoms is 74 Å2 indicating that the IDCL loop is a highly flexible structure.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:34:18.242Z"}},{"start":118,"end":134,"reference_id":"28844736","reference_source":"pmid","reference_html":"Structure and binding studies of proliferating cell nuclear antigen from Leishmania donovani. <i> Yadav SP, Singh PK, Sharma P, Iqbal N, Kaur P, Sharma S, Singh TP. </i> Biochim Biophys Acta Proteins Proteom, 2017","date":"2022-09-15T13:17:13.206Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006222","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"5H0T"}],"region_id":"DP03782r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46807","entry_name":"diethylene glycol"}],"statement":[{"text":"The average value of the B-factor for the atoms of the IDCL loop in LdPCNA is 114 Å2 whereas as the average B-factor for rest of the protein atoms is 74 Å2 indicating that the IDCL loop is a highly flexible structure.","type":"Results"},{"text":"Domain-1 and Domain-2 are connected by a flexible 17-residue loop known as inter-domain connecting loop (IDCL) (residues, Leu118-Arg134).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:34:19.977Z"}}],"regions_counter":3,"released":"2022_12","sequence":"MLEAQVQFASLWKRLVECINGLVNEANFDCNPGGLSVQAMDSSHVALVHMLLRDDCFVKYQCGRNSILGLNLASLSKVLKIVDSNDSLSLRHDDDSDVVTLTSENPEKTRKCEYQLKLLEIEAESMGIPEMDYRSTVTLNSAEFAKIVRDMQVFGDTVTIAISKEGVKFSSSGDVGQGYTFLQAAGVSDRSTKSEVKAEVKAEARDDDEEPLSRKYGKADSSANAIGVEVTMEEPITLSFALRFMGIFAKGSTLSERVTLKFAKDSPCMVEYGIDNVGYLRYYLAPKVDDAE","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"name":{"value":"PCNA","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ACH92667.1","url":"https://www.ebi.ac.uk/ena/browser/view/ACH92667.1"}}]}}],"alphafold_very_low_content":0.13356164383561644,"disorder_content":0.19863013698630136,"disprot_consensus":{"full":[{"start":118,"end":134,"type":"D"},{"start":186,"end":226,"type":"D"}],"Structural state":[{"start":118,"end":134,"type":"D"},{"start":186,"end":226,"type":"D"}],"Disorder function":[{"start":118,"end":134,"type":"F"}]}},{"disprot_id":"DP03783","acc":"Q4Q5S8","creator":"vnugnes","date":"2022-09-15T13:36:36.493Z","features":{"pfam":[{"id":"PF01233","name":"Myristoyl-CoA:protein N-myristoyltransferase, N-terminal domain","start":36,"end":213},{"id":"PF02799","name":"Myristoyl-CoA:protein N-myristoyltransferase, C-terminal domain","start":229,"end":412}],"gene3D":[]},"length":421,"name":"Glycylpeptide N-tetradecanoyltransferase","ncbi_taxon_id":5664,"organism":"Leishmania major","regions":[{"start":1,"end":10,"reference_id":"32575985","reference_source":"pmid","reference_html":"Novel Thienopyrimidine Inhibitors of <i>Leishmania N</i>-Myristoyltransferase with On-Target Activity in Intracellular Amastigotes. <i> Bell AS, Yu Z, Hutton JA, Wright MH, Brannigan JA, Paape D, Roberts SM, Sutherell CL, Ritzefeld M, Wilkinson AJ, Smith DF, Leatherbarrow RJ, Tate EW. </i> J Med Chem, 2020","date":"2022-09-15T13:41:49.608Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6QDE"},{"db":"PDB","id":"6QDA"},{"db":"PDB","id":"6QDB"},{"db":"PDB","id":"6QD9"},{"db":"PDB","id":"6QDH"},{"db":"PDB","id":"6QDF"},{"db":"PDB","id":"6QDD"},{"db":"PDB","id":"6QDC"},{"db":"PDB","id":"6QDG"}],"region_id":"DP03783r001","statement":[{"text":"The PDBs structures of the major N-myristoyltransferase in complex with a variety of inhibitors show this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:34:40.496Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MSRNPSNSDAAHAFWSTQPVPQTEDETEKIVFAGPMDEPKTVADIPEEPYPIASTFEWWTPNMEAADDIHAIYELLRDNYVEDDDSMFRFNYSEEFLQWALCPPNYIPDWHVAVRRKADKKLLAFIAGVPVTLRMGTPKYMKVKAQEKGEGEEAAKYDEPRHICEINFLCVHKQLREKRLAPILIKEATRRVNRTNVWQAVYTAGVLLPTPYASGQYFHRSLNPEKLVEIRFSGIPAQYQKFQNPMAMLKRNYQLPSAPKNSGLREMKPSDVPQVRRILMNYLDSFDVGPVFSDAEISHYLLPRDGVVFTYVVENDKKVTDFFSFYRIPSTVIGNSNYNLLNAAYVHYYAATSIPLHQLILDLLIVAHSRGFDVCNMVEILDNRSFVEQLKFGAGDGHLRYYFYNWAYPKIKPSQVALVML","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"name":{"value":"NMT","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAJ08448.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAJ08448.1"}}]},"orfNames":[{"value":"LMJF_32_0080","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAJ08448.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAJ08448.1"}}]}]}],"alphafold_very_low_content":0.023752969121140142,"disorder_content":0.023752969121140142,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"}]}},{"disprot_id":"DP03784","acc":"Q4QCD2","creator":"vnugnes","date":"2022-09-15T14:37:31.615Z","features":{"pfam":[{"id":"PF09334","name":"tRNA synthetases class I (M)","start":212,"end":585},{"id":"PF19303","name":"Anticodon binding domain of methionyl tRNA ligase","start":597,"end":734}],"gene3D":[]},"length":747,"name":"Methionine--tRNA ligase","ncbi_taxon_id":5664,"organism":"Leishmania major","regions":[{"start":737,"end":747,"reference_id":"21144880","reference_source":"pmid","reference_html":"Structure of Leishmania major methionyl-tRNA synthetase in complex with intermediate products methionyladenylate and pyrophosphate. <i> Larson ET, Kim JE, Zucker FH, Kelley A, Mueller N, Napuli AJ, Verlinde CL, Fan E, Buckner FS, Van Voorhis WC, Merritt EA, Hol WG. </i> Biochimie, 2011","date":"2022-09-26T12:44:29.411Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"3KFL"}],"region_id":"DP03784r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"45212","entry_name":"diphosphate(2-)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":"ethylene glycol"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30751","entry_name":"formic acid"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:10672297"}],"statement":[{"text":"Residues 207 to 736 are well defined in the electron density map; only the 22 amino acid N-terminal expression tag, residue 206, and the final 11 residues at the C-terminus, Thr737-Gln747, are absent from the structure.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:35:09.155Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MLKFFTEKANHQALKAVLCAVFVQKPLEVTLGSTYSTPYLQLPKSRALLYSCNEAARLIWSTHAAPLPADNSLEGEAEWLEWESTVLTPALTPLYTHRRITGEAEAALKKLDSTIEEHQGTVAVKGAPSSTSFLVDSVLFASLLPALCEGGLLPAAQAARVPHLVKWFQAFQAEHAELIASAFDVLSVQECGDFLRVPQTYEVSPKKQKVFFATTPIYYVNASPHIGHVYSTLIVDVLGRYHRVKGEEVFVMTGTDEHGQKVAEAAAKQGVSPMDFTTSVSSEFKQCFQEMNYDMNYFIRTTNPTHEKLVQDIWKKLAAKGDIYLGKYEGWYSVSDESFLTAQNVADGVDRDGKPCKVSLESGHVVTWVEEENYMFRLSAFRERLLKYFHDHPNCIVPEFRRREVIKTVEKGLFDLSISRKRESVMNWSIPVPGDERHCIYVWLDALFNYYTGALTRVATDGTETLDEDHHALNRWPADVHVVGKDILKFHAIYWPAFLMSAELPLPERLVSHGWWTKDHKKISKSLGNAFDPVEKAKEFGIDALKYFLMRESNFQDDGDYSDKNMVARLNGELADTLGNLVSRCVAPKINVNGMWPEPAEYSESDKTLIASLNNLAGTVDHYYCLPDIQHALIAIFDVLRSLNAYVTENAPWKLVKMDTARLGTVLYVTMEGLRICTMFLQPVMPQKAKEIMDALGVPEAARVGMENYLFGIVKPGTKIAGLAEGQVVFQKVTLPTEEGERSSKGQ","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"orfNames":[{"value":"LMJF_21_0810","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAJ04288.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAJ04288.1"}}]}]}],"alphafold_very_low_content":0.2784471218206158,"disorder_content":0.014725568942436412,"disprot_consensus":{"full":[{"start":737,"end":747,"type":"D"}],"Structural state":[{"start":737,"end":747,"type":"D"}]}},{"disprot_id":"DP03786","acc":"A0A175WC91","creator":"vnugnes","date":"2022-09-15T15:41:41.928Z","features":{"pfam":[{"id":"PF13577","name":"SnoaL-like domain","start":20,"end":159}],"gene3D":[]},"length":243,"name":"Pea pathogenicity protein 2","ncbi_taxon_id":100816,"organism":"Madurella mycetomatis","regions":[{"start":118,"end":132,"reference_id":"33542397","reference_source":"pmid","reference_html":"Crystal structures of non-oxidative decarboxylases reveal a new mechanism of action with a catalytic dyad and structural twists. <i> Zeug M, Markovic N, Iancu CV, Tripp J, Oreb M, Choe JY. </i> Sci Rep, 2021","date":"2022-09-15T15:47:52.627Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":85,"end":85,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":106,"end":106,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":224,"end":224,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":228,"end":228,"position":"Specific residue","statements":[{"type":"Methods","text":"For selenomethionine labeled protein expression, cells were grown in M9 media with amino acid supplements as previously described46."}]}],"cross_refs":[{"db":"PDB","id":"7JMR"}],"region_id":"DP03786r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29103","entry_name":"potassium(1+)"}],"statement":[{"text":"The main difference arises from an additional flexible, 17 residue-loop between β-strands β4 and β5 of PPP2, which had no associated electron density in the crystal structure.","type":"Results"},{"text":"The star indicates the equivalent position of the additional flexible loop in PPP2, with missing electron density.","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-12T09:37:41.652Z"}},{"start":118,"end":132,"reference_id":"33542397","reference_source":"pmid","reference_html":"Crystal structures of non-oxidative decarboxylases reveal a new mechanism of action with a catalytic dyad and structural twists. <i> Zeug M, Markovic N, Iancu CV, Tripp J, Oreb M, Choe JY. </i> Sci Rep, 2021","date":"2022-09-15T15:48:04.928Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":85,"end":85,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":106,"end":106,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":224,"end":224,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":228,"end":228,"position":"Specific residue","statements":[{"type":"Methods","text":"For selenomethionine labeled protein expression, cells were grown in M9 media with amino acid supplements as previously described46."}]}],"cross_refs":[{"db":"PDB","id":"7JMR"}],"region_id":"DP03786r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29103","entry_name":"potassium(1+)"}],"statement":[{"text":"The main difference arises from an additional flexible, 17 residue-loop between β-strands β4 and β5 of PPP2, which had no associated electron density in the crystal structure.","type":"Results"},{"text":"The star indicates the equivalent position of the additional flexible loop in PPP2, with missing electron density.","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-12T09:37:53.730Z"}},{"start":118,"end":133,"reference_id":"33542397","reference_source":"pmid","reference_html":"Crystal structures of non-oxidative decarboxylases reveal a new mechanism of action with a catalytic dyad and structural twists. <i> Zeug M, Markovic N, Iancu CV, Tripp J, Oreb M, Choe JY. </i> Sci Rep, 2021","date":"2022-09-15T15:52:58.683Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":85,"end":85,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":106,"end":106,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":224,"end":224,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":228,"end":228,"position":"Specific residue","statements":[{"type":"Methods","text":"For selenomethionine labeled protein expression, cells were grown in M9 media with amino acid supplements as previously described46."}]}],"cross_refs":[{"db":"PDB","id":"7JMV"}],"region_id":"DP03786r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29103","entry_name":"potassium(1+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16318","entry_name":"4-nitrocatechol"}],"statement":[{"text":"The main difference arises from an additional flexible, 17 residue-loop between β-strands β4 and β5 of PPP2, which had no associated electron density in the crystal structure.","type":"Results"},{"text":"The star indicates the equivalent position of the additional flexible loop in PPP2, with missing electron density.","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-12T09:38:01.786Z"}},{"start":118,"end":133,"reference_id":"33542397","reference_source":"pmid","reference_html":"Crystal structures of non-oxidative decarboxylases reveal a new mechanism of action with a catalytic dyad and structural twists. <i> Zeug M, Markovic N, Iancu CV, Tripp J, Oreb M, Choe JY. </i> Sci Rep, 2021","date":"2022-09-15T15:53:09.955Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":85,"end":85,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":106,"end":106,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":224,"end":224,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":228,"end":228,"position":"Specific residue","statements":[{"type":"Methods","text":"For selenomethionine labeled protein expression, cells were grown in M9 media with amino acid supplements as previously described46."}]}],"cross_refs":[{"db":"PDB","id":"7JMV"}],"region_id":"DP03786r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29103","entry_name":"potassium(1+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16318","entry_name":"4-nitrocatechol"}],"statement":[{"text":"The main difference arises from an additional flexible, 17 residue-loop between β-strands β4 and β5 of PPP2, which had no associated electron density in the crystal structure.","type":"Results"},{"text":"The star indicates the equivalent position of the additional flexible loop in PPP2, with missing electron density.","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-12T09:37:54.051Z"}}],"regions_counter":4,"released":"2022_12","sequence":"MTSPLDPHSKCYSHINGSAEELLDRLAVSELCKGWPVYRDASEWKNYRSLFTEDATVWTTWSGPRPVDEFITISKAGKEQGVFIMHRECGTLVELSPQQGRAIGKMKATITQRFSFPAASGAATNGTTGTTSDAIEFDVDCDCRFIFFCEKDTASGAWKAKYVKLFYEKDKVVSVDGHQAPKFTKDELAKYPQGYRYLGAAQARLGYDIDLQLPTSSGQLWDRMYGEMENWLGGNKVDLFWEH","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Sordariomycetidae","Sordariales","Sordariales incertae sedis","Madurella"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"orfNames":[{"value":"MMYC01_201259","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"KXX82489.1","url":"https://www.ebi.ac.uk/ena/browser/view/KXX82489.1"}}]},{"value":"MMYC01_203104","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"KXX81388.1","url":"https://www.ebi.ac.uk/ena/browser/view/KXX81388.1"}}]}]}],"alphafold_very_low_content":0,"disorder_content":0.06584362139917696,"disprot_consensus":{"full":[{"start":118,"end":133,"type":"D"}],"Structural state":[{"start":118,"end":133,"type":"D"}],"Disorder function":[{"start":118,"end":133,"type":"F"}]}},{"disprot_id":"DP03787","acc":"A0A1B0XTC8","creator":"vnugnes","date":"2022-09-15T16:00:40.300Z","features":{"pfam":[{"id":"PF00869","name":"Flavivirus glycoprotein, central and dimerisation domains","start":292,"end":592},{"id":"PF00948","name":"Flavivirus non-structural Protein NS1","start":797,"end":1148},{"id":"PF00949","name":"Peptidase S7, Flavivirus NS3 serine protease","start":1519,"end":1669},{"id":"PF00972","name":"Flavivirus RNA-directed RNA polymerase, fingers and palm domains","start":2772,"end":3222},{"id":"PF01002","name":"Flavivirus non-structural protein NS2B","start":1378,"end":1502},{"id":"PF01003","name":"Flavivirus capsid protein C","start":6,"end":122},{"id":"PF01004","name":"Flavivirus envelope glycoprotein M","start":217,"end":290},{"id":"PF01005","name":"Flavivirus non-structural protein NS2A","start":1158,"end":1280},{"id":"PF01349","name":"Flavivirus non-structural protein NS4B","start":2270,"end":2510},{"id":"PF01350","name":"Flavivirus non-structural protein NS4A","start":2126,"end":2268},{"id":"PF01570","name":"Flavivirus polyprotein propeptide","start":130,"end":214},{"id":"PF01728","name":"FtsJ-like methyltransferase","start":2575,"end":2744},{"id":"PF02832","name":"Flavivirus glycoprotein, immunoglobulin-like domain","start":594,"end":692},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1687,"end":1833},{"id":"PF20483","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","start":3226,"end":3389},{"id":"PF20907","name":"Flavivirus NS3 helicase, C-terminal helical domain","start":1975,"end":2117},{"id":"PF21659","name":"Flavivirus envelope glycoprotein E, stem/anchor domain","start":695,"end":789}],"gene3D":[]},"length":3423,"name":"Genome polyprotein","ncbi_taxon_id":64320,"organism":"Zika virus","regions":[{"start":437,"end":451,"reference_id":"27974667","reference_source":"pmid","reference_html":"Molecular determinants of human neutralizing antibodies isolated from a patient infected with Zika virus. <i> Wang Q, Yang H, Liu X, Dai L, Ma T, Qi J, Wong G, Peng R, Liu S, Li J, Li S, Song J, Liu J, He J, Yuan H, Xiong Y, Liao Y, Li J, Yang J, Tong Z, Griffin BD, Bi Y, Liang M, Xu X, Qin C, Cheng G, Zhang X, Wang P, Qiu X, Kobinger G, Shi Y, Yan J, Gao GF. </i> Sci Transl Med, 2016","date":"2022-09-15T16:06:00.894Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"5GZO"}],"region_id":"DP03787r001","sample":[{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ABCD","id":"AD796"}],"statement":[{"text":"The PDB structure of the Zika envelope protein bound to a neutralizing antibody shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:36:14.019Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEIIKKFKKDLAAMLRIINARKEKKRRGADTNVGIVGLLLTTAMAAEVTRRGSAYYMYLDRNDAGEAISFPTTLGMNKCYIQIMDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGCVTVMAQDKPTVDIELVTTTVSNMAEVRSYCYEASISDMASDSRCPTQGEAYLDKQSDTQYVCKRTLVDRGWGNGCGLFGKGSLVTCAKFACSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIVNDTGHETDENRAKVEITPNSPRAEATLGGFGSLGLDCEPRTGLDFSDLYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKEALVEFKDAHAKRQTVVVLGSQEGAVHTALAGALEAEMDGAKGRLSSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGSTIGKAFEATVRGARRMAVLGDTAWDFGSVGGALNSLGKGIHQIFGAAFKSLFGGMSWFSQILIGTLLMWLGLNTKNGSISLMCLALGGVLIFLSTAVSADVGCSVDFSKKETRCGTGVFVYNDVEAWRDRYKYHPDSPRRLAAAVKQAWEDGICGISSVSRMENIMWRSVEGELNAILEENGVQLTVVVGSVKNPMWRGPQRLPVPVNELPHGWKAWGKSYFVRAAKTNNSFVVDGDTLKECPLKHRAWNSFLVEDHGFGVFHTSVWLKVREDYSLECDPAVIGTAVKGKEAVHSDLGYWIESEKNDTWRLKRAHLIEMKTCEWPKSHTLWTDGIEESDLIIPKSLAGPLSHHNTREGYRTQMKGPWHSEELEIRFEECPGTKVHVEETCGTRGPSLRSTTASGRVIEEWCCRECTMPPLSFQAKDGCWYGMEIRPRKEPESNLVRSMVTAGSTDHMDHFSLGVLVILLMVQEGLKKRMTTKIIISTSMAVLVAMILGGFSMSDLAKLAILMGATFAEMNTGGDVAHLALIAAFKVRPALLVSFIFRANWTPRESMLLALASCLLQTAISALEGDLMVLINGFALAWLAIRAMVVPRTDNITLAILAALTPLARGTLLVAWRAGLATCGGFMLLSLKGKGSVKKNLPXVMALGLTAVRLVDPINVVGLLLLTRSGKRSWPPSEVLTAVGLICALAGGFAKADIEMAGPMAAVGLLIVSYVVSGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEDDGPPMREIILKVVLMTICGMNPIAIPFAAGAWYVYVKTGKRSGALWDVPAPKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGSALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWDGHSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGRREEETPVECFEPSMLKKKQLTVLDLHPGAGKTRRVLPEIVREAIKTRLRTVILAPTRVVAAEMEEALRGLPVRYMTTAVNVTHSGTEIVDLMCHATFTSRLLQPIRVPNYNLYIMDEAHFTDPSSIAARGYISTRVEMGEAAAIFMTATPPGTRDAFPDSNSPIMDTEVEVPERAWSSGFDWVTDHSGKTVWFVPSVRNGNEIAACLTKAGKRVIQLSRKTFETEFQKTKHQEWDFVVTTDISEMGANFKADRVIDSRRCLKPVILDGERVILAGPMPVTHASAAQRRGRIGRNPNKPGDEYLYGGGCAETDEDHAHWLEARMLLDNIYLQDGLIASLYRPEADKVAAIEGEFKLRTEQRKTFVELMKRGDLPVWLAYQVASAGITYTDRRWCFDGTTNNTIMEDSVPAEVWTRHGEKRVLKPRWMDARVCSDHAALKSFKEFAAGKRGAAFGVMEALGTLPGHMTERFQEAIDNLAVLMRAETGSRPYKAAAAQLPETLETIMLLGLLGTVSLGIFFVLMRNKGIGKMGFGMVTLGASAWLMWLSEIEPARIACVLIVVFLLLVVLIPEPEKQRSPQDNQMAIIIMVAVGLLGLITANELGWLERTKSDLSHLMGRREEGATIGFSMDIDLRPASAWAIYAALTTFITPAVQHAVTTSYNNYSLMAMATQAGVLFGMGKGMPFYAWDFGVPLLMIGCYSQLTPLTLIVAIILLVAHYMYLIPGLQAAAARAAQKRTAAGIMKNPVVDGIVVTDIDTMTIDPQVEKKMGQVLLIAVAVSSAILSRTAWGWGEAGALITAATSTLWEGSPNKYWNSSTATSLCNIFRGSYLAGASLIYTVTRNAGLVKRRGGGTGETLGEKWKARLNQMSALEFYSYKKSGITEVCREEARRALKDGVATGGHAVSRGSAKLRWLVERGYLQPYGKVIDLGCGRGGWSYYAATIRKVQEVKGYTKGGPGHEEPMLVQSYGWNIVRLKSGVDVFHMAAEPCDTLLCDIGESSSSPEVEEARTLRVLSMVGDWLEKRPGAFCIKVLCPYTSTMMETLERLQRRYGGGLVRVPLSRNSTHEMYWVSGAKSNTIKSVSTTSQLLLGRMDGPRRPVKYEEDVNLGSGTRAVVSCAEAPNMKIIGNRIERIRSEHAETWFFDENHPYRTWAYHGSYEAPTQGSASSLINGVVRLLSKPWDVVTGVTGIAMTDTTPYGQQRVFKEKVDTRVPDPQEGTRQVMSMVSSWLWKELGKHKRPRVCTKEEFINKVRSNAALGAIFEEEKEWKTAVEAVNDPRFWALVDKEREHHLRGECQSCVYNMMGKREKKQGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMGRENSGGGVEGLGLQRLGYVLEEMSRIPGGRMYADDTAGWDTRISRFDLENEALITNQMEKGHRALALAIIKYTYQNKVVKVLRPAEKGKTVMDIISRQDQRGSGQVVTYALNTFTNLVVQLIRSMEAEEVLEMQDLWLLRRSEKVTNWLQSNGWDRLKRMAVSGDDCVVRPIDDRFAHALRFLNDMGKVRKDTQEWKPSTGWDNWEEVPFCSHHFNKLHLKDGRSIVVPCRHQDELIGRARVSPGAGWSIRETACLAKSYAQMWQLLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLVVWNRVWIEENDHMEDKTPVTKWTDIPYLGKREDLWCGSLIGHRPRTTWAENIKNTVNMVRRIIGDEEKYMDYLSTQVRYLGEEGSTPGVL","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Flavivirus"],"dataset":["Neglected tropical diseases proteins","Viral proteins"],"genes":[],"disorder_content":0.0043821209465381246,"disprot_consensus":{"full":[{"start":437,"end":451,"type":"D"}],"Structural state":[{"start":437,"end":451,"type":"D"}]}},{"disprot_id":"DP03788","acc":"A0A109PRQ3","creator":"vnugnes","date":"2022-09-15T16:54:25.688Z","features":{"pfam":[{"id":"PF00869","name":"Flavivirus glycoprotein, central and dimerisation domains","start":292,"end":592},{"id":"PF00948","name":"Flavivirus non-structural Protein NS1","start":797,"end":1148},{"id":"PF00949","name":"Peptidase S7, Flavivirus NS3 serine protease","start":1519,"end":1669},{"id":"PF00972","name":"Flavivirus RNA-directed RNA polymerase, fingers and palm domains","start":2772,"end":3222},{"id":"PF01002","name":"Flavivirus non-structural protein NS2B","start":1378,"end":1502},{"id":"PF01003","name":"Flavivirus capsid protein C","start":6,"end":122},{"id":"PF01004","name":"Flavivirus envelope glycoprotein M","start":217,"end":290},{"id":"PF01005","name":"Flavivirus non-structural protein NS2A","start":1158,"end":1280},{"id":"PF01349","name":"Flavivirus non-structural protein NS4B","start":2270,"end":2510},{"id":"PF01350","name":"Flavivirus non-structural protein NS4A","start":2126,"end":2268},{"id":"PF01570","name":"Flavivirus polyprotein propeptide","start":130,"end":214},{"id":"PF01728","name":"FtsJ-like methyltransferase","start":2575,"end":2744},{"id":"PF02832","name":"Flavivirus glycoprotein, immunoglobulin-like domain","start":594,"end":692},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1687,"end":1833},{"id":"PF20483","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","start":3226,"end":3389},{"id":"PF20907","name":"Flavivirus NS3 helicase, C-terminal helical domain","start":1975,"end":2117},{"id":"PF21659","name":"Flavivirus envelope glycoprotein E, stem/anchor domain","start":695,"end":789}],"gene3D":[]},"length":3423,"name":"Genome polyprotein","ncbi_taxon_id":64320,"organism":"Zika virus","regions":[{"start":2927,"end":2944,"reference_id":"28254839","reference_source":"pmid","reference_html":"The crystal structure of Zika virus NS5 reveals conserved drug targets. <i> Duan W, Song H, Wang H, Chai Y, Su C, Qi J, Shi Y, Gao GF. </i> EMBO J, 2017","date":"2022-09-15T16:57:45.065Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"5WZ3"}],"region_id":"DP03788r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"There are four flexible loops in the fingers subdomain (β1‐α2 loop, α3‐α4 loop, α6‐α7 loop and α7‐α8 loop), which are disordered in our structure and other flavivirus RdRp structures.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:36:30.354Z"}},{"start":2976,"end":2995,"reference_id":"28254839","reference_source":"pmid","reference_html":"The crystal structure of Zika virus NS5 reveals conserved drug targets. <i> Duan W, Song H, Wang H, Chai Y, Su C, Qi J, Shi Y, Gao GF. </i> EMBO J, 2017","date":"2022-09-15T16:58:18.288Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"5WZ3"}],"region_id":"DP03788r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"There are four flexible loops in the fingers subdomain (β1‐α2 loop, α3‐α4 loop, α6‐α7 loop and α7‐α8 loop), which are disordered in our structure and other flavivirus RdRp structures.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:36:31.882Z"}},{"start":2785,"end":2794,"reference_id":"28254839","reference_source":"pmid","reference_html":"The crystal structure of Zika virus NS5 reveals conserved drug targets. <i> Duan W, Song H, Wang H, Chai Y, Su C, Qi J, Shi Y, Gao GF. </i> EMBO J, 2017","date":"2022-09-15T17:07:48.387Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"5WZ1"},{"db":"PDB","id":"5WZ2"}],"region_id":"DP03788r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"67040","entry_name":"S-adenosyl-L-methioninate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"157762","entry_name":"N(7)-methyl-GpppA"}],"statement":[{"text":"The PDB structure of theZika virus NS5 methyltransferase bound to s-adenosylmethionine and a RNA analogue (m7GpppA) shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:36:34.204Z"}}],"regions_counter":3,"released":"2022_12","sequence":"MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEIIKKFKKDLAAMLRIINARKEKKRRGADTSVGIVGLLLTTAMAAEVTRRGSAYYMYLDRNDAGEAISFPTTLGMNKCYIQIMDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGCVTVMAQDKPTVDIELVTTTVSNMAEVRSYCYEASISDMASDSRCPTQGEAYLDKQSDTQYVCKRTLVDRGWGNGCGLFGKGSLVTCAKFACSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIVNDTGHETDENRAKVEITPNSPRAEATLGGFGSLGLDCEPRTGLDFSDLYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKEALVEFKDAHAKRQTVVVLGSQEGAVHTALAGALEAEMDGAKGRLSSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGSTIGKAFEATVRGAKRMAVLGDTAWDFGSVGGALNSLGKGIHQIFGAAFKSLFGGMSWFSQILIGTLLMWLGLNTKNGSISLMCLALGGVLIFLSTAVSADVGCSVDFSKKETRCGTGVFVYNDVEAWRDRYKYHPDSPRRLAAAVKQAWEDGICGISSVSRMENIMWRSVEGELNAILEENGVQLTVVVGSVKNPMWRGPQRLPVPVNELPHGWKAWGKSYFVRAAKTNNSFVVDGDTLKECPLKHRAWNSFLVEDHGFGVFHTSVWLKVREDYSLECDPAVIGTAVKGKEAVHSDLGYWIESEKNDTWRLKRAHLIEMKTCEWPKSHTLWTDGIEESDLIIPKSLAGPLSHHNTREGYRTQMKGPWHSEELEIRFEECPGTKVHVEETCGTRGPSLRSTTASGRVIEEWCCRECTMPPLSFRAKDGCWYGMEIRPRKEPESNLVRSMVTAGSTDHMDHFSLGVLVILLMVQEGLKKRMTTKIIISTSMAVLVAMILGGFSMSDLAKLAILMGATFAEMNTGGDVAHLALIAAFKVRPALLVSFIFRANWTPRESMLLALASCLLQTAISALEGDLMVLINGFALAWLAIRAMVVPRTDNITLAILAALTPLARGTLLVAWRAGLATCGGFMLLSLKGKGSVKKNLPFVMALGLTAVRLVDPINVVGLLLLTRSGKRSWPPSEVLTAVGLICALAGGFAKADIEMAGPMAAVGLLIVSYVVSGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEDDGPPMREIILKVVLMTICGMNPIAIPFAAGAWYVYVKTGKRSGALWDVPAPKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGSALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWDGHSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGRREEETPVECFEPSMLKKKQLTVLDLHPGAGKTRRVLPEIVREAIKTRLRTVILAPTRVVAAEMEEALRGLPVRYMTTAVNVTHSGTEIVDLMCHATFTSRLLQPIRVPNYNLYIMDEAHFTDPSSIAARGYISTRVEMGEAAAIFMTATPPGTRDAFPDSNSPIMDTEVEVPERAWSSGFDWVTDHSGKTVWFVPSVRNGNEIAACLTKAGKRVIQLSRKTFETEFQKTKHQEWDFVVTTDISEMGANFKADRVIDSRRCLKPVILDGERVILAGPMPVTHASAAQRRGRIGRNPNKPGDEYLYGGGCAETDEDHAHWLEARMLLDNIYLQDGLIASLYRPEADKVAAIEGEFKLRTEQRKTFVELMKRGDLPVWLAYQVASAGITYTDRRWCFDGTTNNTIMEDSVPAEVWTRHGEKRVLKPRWMDARVCSDHAALKSFKEFAAGKRGAAFGVMEALGTLPGHMTERFQEAIDNLAVLMRAETGSRPYKAAAAQLPETLETIMLLGLLGTVSLGIFFVLMRNKGIGKMGFGMVTLGASAWLMWLSEIEPARIACVLIVVFLLLVVLIPEPEKQRSPQDNQMAIIIMVAVGLLGLITANELGWLERTKSDLSHLMGRREEGATIGFSMDIDLRPASAWAIYAALTTFITPAVQHAVTTSYNNYSLMAMATQAGVLFGMGKGMPFYAWDFGVPLLMIGCYSQLTPLTLIVAIILLVAHYMYLIPGLQAAAARAAQKRTAAGIMKNPVVDGIVVTDIDTMTIDPQVEKKMGQVLLIAVAVSSAILSRTAWGWGEAGALITAATSTLWEGSPNKYWNSSTATSLCNIFRGSYLAGASLIYTVTRNAGLVKRRGGGTGETLGEKWKARLNQMSALEFYSYKKSGITEVCREEARRALKDGVATGGHAVSRGSAKLRWLVERGYLQPYGKVIDLGCGRGGWSYYAATIRKVQEVKGYTKGGPGHEEPVLVQSYGWNIVRLKSGVDVFHMAAEPCDTLLCDIGESSSSPEVEEARTLRVLSMVGDWLEKRPGAFCIKVLCPYTSTMMETLERLQRRYGGGLVRVPLSRNSTHEMYWVSGAKSNTIKSVSTTSQLLLGRMDGPRRPVKYEEDVNLGSGTRAVVSCAEAPNMKIIGNRIERIRSEHAETWFFDENHPYRTWAYHGSYEAPTQGSASSLINGVVRLLSKPWDVVTGVTGIAMTDTTPYGQQRVFKEKVDTRVPDPQEGTRQVMSMVSSWLWKELGKHKRPRVCTKEEFINKVRSNAALGAIFEEEKEWKTAVEAVNDPRFWALVDKEREHHLRGECQSCVYNMMGKREKKQGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMGRENSGGGVEGLGLQRLGYVLEEMSRIPGGRMYADDTAGWDTRISRFDLENEALITNQMEKGHRALALAIIKYTYQNKVVKVLRPAEKGKTVMDIISRQDQRGSGQVVTYALNTFTNLVVQLIRNMEAEEVLEMQDLWLLRRSEKVTNWLQSNGWDRLKRMAVSGDDCVVKPIDDRFAHALRFLNDMGKVRKDTQEWKPSTGWDNWEEVPFCSHHFNKLHLKDGRSIVVPCRHQDELIGRARVSPGAGWSIRETACLAKSYAQMWQLLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLVVWNRVWIEENDHMEDKTPVTKWTDIPYLGKREDLWCGSLIGHRPRTTWAENIKNTVNMVRRIIGDEEKYMDYLSTQVRYLGEEGSTPGVL","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Flavivirus"],"dataset":["Neglected tropical diseases proteins","Viral proteins"],"genes":[],"disorder_content":0.014022787028921999,"disprot_consensus":{"full":[{"start":2785,"end":2794,"type":"D"},{"start":2927,"end":2944,"type":"D"},{"start":2976,"end":2995,"type":"D"}],"Structural state":[{"start":2785,"end":2794,"type":"D"},{"start":2927,"end":2944,"type":"D"},{"start":2976,"end":2995,"type":"D"}]}},{"disprot_id":"DP03789","acc":"A0A1V0E2H9","creator":"vnugnes","date":"2022-09-19T18:30:24.086Z","features":{"pfam":[{"id":"PF00869","name":"Flavivirus glycoprotein, central and dimerisation domains","start":292,"end":592},{"id":"PF00948","name":"Flavivirus non-structural Protein NS1","start":797,"end":1148},{"id":"PF00949","name":"Peptidase S7, Flavivirus NS3 serine protease","start":1519,"end":1669},{"id":"PF00972","name":"Flavivirus RNA-directed RNA polymerase, fingers and palm domains","start":2772,"end":3222},{"id":"PF01002","name":"Flavivirus non-structural protein NS2B","start":1378,"end":1502},{"id":"PF01003","name":"Flavivirus capsid protein C","start":6,"end":122},{"id":"PF01004","name":"Flavivirus envelope glycoprotein M","start":217,"end":290},{"id":"PF01005","name":"Flavivirus non-structural protein NS2A","start":1158,"end":1280},{"id":"PF01349","name":"Flavivirus non-structural protein NS4B","start":2270,"end":2510},{"id":"PF01350","name":"Flavivirus non-structural protein NS4A","start":2126,"end":2268},{"id":"PF01570","name":"Flavivirus polyprotein propeptide","start":130,"end":214},{"id":"PF01728","name":"FtsJ-like methyltransferase","start":2575,"end":2744},{"id":"PF02832","name":"Flavivirus glycoprotein, immunoglobulin-like domain","start":594,"end":692},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1687,"end":1833},{"id":"PF20483","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","start":3226,"end":3389},{"id":"PF20907","name":"Flavivirus NS3 helicase, C-terminal helical domain","start":1975,"end":2117},{"id":"PF21659","name":"Flavivirus envelope glycoprotein E, stem/anchor domain","start":695,"end":789}],"gene3D":[]},"length":3423,"name":"Genome polyprotein","ncbi_taxon_id":64320,"organism":"Zika virus","regions":[{"start":1,"end":23,"reference_id":"31034208","reference_source":"pmid","reference_html":"Dynamics of Zika Virus Capsid Protein in Solution: The Properties and Exposure of the Hydrophobic Cleft Are Controlled by the α-Helix 1 Sequence. <i> Morando MA, Barbosa GM, Cruz-Oliveira C, Da Poian AT, Almeida FCL. </i> Biochemistry, 2019","date":"2022-09-19T18:40:34.332Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"BMRB","id":"30397"},{"db":"PDB","id":"6C44"}],"region_id":"DP03789r001","statement":[{"text":"We measured the 15N relaxation parameters (Figure S2), which is typical of a dimer and allowed us to distinguish different dynamic regions: (i) a highly flexible disordered region observed for residues 1–23, (ii) a transition disordered region from residue 24 to 35, (iii) a globular ordered region from residue 36 to 98, and (iv) a flexible C-terminus (residues 99–104).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:37:04.248Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MKNPKKKSGGFRIVNMLKRGVARVSPFGGLKRLPAGLLLGHGPIRMVLAILAFLRFTAIKPSLGLINRWGSVGKKEAMEIIKKFKKDLAAMLRIINARKEKKRRGADTSVGIVGLLLTTAMAAEVTRRGSAYYMYLDRNDAGEAISFPTTLGMNKCYIQIMDLGHMCDATMSYECPMLDEGVEPDDVDCWCNTTSTWVVYGTCHHKKGEARRSRRAVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNPGFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYSIRCIGVSNRDFVEGMSGGTWVDVVLEHGGCVTVMAQDKPTVDIELVTTTVSNMAEVRSYCYEASISDMASDSRCPTQGEAYLDKQSDTQYVCKRTLVDRGWGNGCGLFGKGSLVTCAKFACSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIVNDTGHETDENRAKVEITPNSPRAEATLGGFGSLGLDCEPRTGLDFSDLYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKEALVEFKDAHAKRQTVVVLGSQEGAVHTALAGALEAEMDGAKGRLSSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKIPAETLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLITANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHWHRSGSTIGKAFEATVRGAKRMAVLGDTAWDFGSVGGALNSLGKGIHQIFXAAFKSLFGGMSWFSQILIGTLLMWLGLNTKNGSISLMCLALGGVLIFLSTAVSADVGCSVDFSKKETRCGTGVFVYNDVEAWRDRYKYHPDSPRRLAAAVKQAWEDGICGISSVSRMENIMWRSVEGELNAILEENGVQLTVVVGSVKNPMWRGPQRLPVPVNELPHGWKAWGKSYFVRAAKTNNSFVVDGDTLKECPLKHRAWNSFLVEDHGFGVFHTSVWLKVREDYSLECDPAVIGTAVKGKEAVHSDLGYWIESEKNDTWRLKRAHLIEMKTCEWPKSHTLWTDGIEESDLIIPKSLAGPLSHHNTREGYRTQMKXPWHSEELEIRFEECPGTKVHVEETCGTRGPSLRSTTASGRVIEEWCCRECTMPPLSFRAKDGCWYGMEIRPRKEPESNLVRSVVTAGSTDHMDHFSLGVLVILLMVQEGLKKRMTTKIIISTSMAVLVAMILGGFSMSDLAKLAILMGATFAEMNTGGDVAHLALIAAFKVRPALLVSFIFRANWTPRESMLLALASCLLQTAISALEGDLMVLINGFALAWLAIRAMVVPRTDNITLAILAALTPLARGTLLVAWRAGLATCGGFMLLSLKGKGSVKKNLPFVMALGLTAVRLVDPINVVGLLLLTRSGKRSWPPSEVLTAVGLICALAGGFAKADIEMAGPMAAVGLLIVSYVVSGKSVDMYIERAGDITWEKDAEVTGNSPRLDVALDESGDFSLVEDDGPPMREIILKVVLMTICGMNPIAIPFAAGAWYVYVKTGKRSGALWDVPAPKEVKKGETTDGVYRVMTRRLLGSTQVGVGVMQEGVFHTMWHVTKGSALRSGEGRLDPYWGDVKQDLVSYCGPWKLDAAWDGHSEVQLLAVPPGERARNIQTLPGIFKTKDGDIGAVALDYPAGTSGSPILDKCGRVIGLYGNGVVIKNGSYVSAITQGRREEETPVECFEPSMLKKKQLTVLDLHPGAGKTRRVLPEIVREAIKTRLRTVILAPTRVVAAEMEEALRGLPVRYMTTAVNVTHSGTEIVDLMCHATFTSRLLQPIRVPNYNLYIMDEAHFTDPSSIAARGYISTRVEMGEAAAIFMTATPPGTRDAFPDSNSPIMDTEVEVPERAWSSGFDWVTDHSGKTVWFVPSVRNGNEIAACLTKAGKRVIQLSRKTFETEFQKTKHQEWDFVVTTDISEMGANFKADRVIDSRRCLKPVILDGERVILAGPMPVTHASAAQRRGRIGRNPNKPGDEYLYGGGCAETDEDHAHWLEARMLLDNIYLQDGLIASLYRPEADKVAAIEGEFKLRTEQRKTFVELMKRGDLPVWLAYQVASAGITYTDRRWCFDGTTNNTIMEDSVPAEVWTRHGEKRVLKPRWMDARVCSDHAALKSFKEFAAGKRGAAFGVMEALGTLPGHMTERFQEAIDNLAVLMRAETGSRPYKAAAAQLPETLETIMLLGLLGTVSLGIFFVLMRNKGIGKMGFGMVTLGASAWLMWLSEIEPARIACVLIVVFLLLVVLIPEPEKQRSPQDNQMAIIIMVAVGLLGLITANELGWLERTKSDLSHLMGRREEGATIGFSMDIDLRPASAWAIYAALTTFITPAVQHAVTTSYNNYSLMAMATQAGVLFGMGKGMPFYAWDFGVPLLMIGCYSQLTPLTLIVAIILLVAHYMYLIPGLQAAAARAAQKRTAAGIMKNPVVDGIVVTDIDTMTIDPQVEKKMGQXLLIAVAVSSAILSRTAWGWGEAGALITAATSTLWEGSPNKYWNSSTATSLCNIFRGSYLAGASLIYTVTRNAGLVKRRGGGTGETLGEKWKARLNQMSALEFYSYKKSGITEVCREEARRALKXGVATGGHAVSRGSAKLRWLVERGYLQPYGKVIDLGCGRGGWSYYAATIRKVQEVKGYTKGGPGHEEPVLVQSYGWNIVRLKSGVDVFHMAAEPCDTLLCDIGESSSSPEVEEARTLRVLSMVGDWLEKRPGAFCIKVLCPYTSTMMETLERLQRRYGGGLVRVPLSRNSTHEMYWVSGAKSNTIKSVSTTSQLLLGRMDGPRRPVKYEEDVNLGSGTRAVVSCAEAPNMKIIGNRIERIRSEHAETWFVDENHPYRTWAYHGSYEAPTQGSASSLVNGVVRLLSKPWDVVTGVTGIAMTDTTPYGQQRVFKEKVDTRVPDPQEGTRQVMSMVSSWLWKELGKHKRPRVCTKEEFINKVRSNAALGAIFEEEKEWKTAVEAVNDPRFWALVDKEREHHLRGECQSCVYNMMGKREKKQGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWMGRENSGGGVEGLGLQRLGYVLEEMSRIPGGRMYADDTAGWDTRISRFDLENEALITNQMEKGHRALALAIIKYTYQNKVVKVLRPAEKGKTVMDIISRQDQRGSGQVVTYALNTFTNLVVQLIRNMEAEEVLEMQDLWLLRRSEKVTNWLQSNGWDRLKRMAVSGDDCVVKPIDDRFAHALRFLNDMGKVRKDTQEWKPSTGWDNWEEVPFCSHHFNKLHLKDGRSIVVPCRHQDELIGRARVSPGAGWSIRETACLAXSYAQMWQLLYFHRRDLRLMANAICSSVPVDWVPTGRTTWSIHGKGEWMTTEDMLVVWNRVWIEENDHMEDKTPVTKWTDIPYLGKREDLWCGSLIGHRPRTTWAENIKNTVNMVRRIIGEEEKYMDYLSTQVRYLGEEGSTPGVL","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Flavivirus"],"dataset":["Neglected tropical diseases proteins","Viral proteins"],"genes":[],"disorder_content":0.006719252118025124,"disprot_consensus":{"full":[{"start":1,"end":23,"type":"D"}],"Structural state":[{"start":1,"end":23,"type":"D"}]}},{"disprot_id":"DP03790","acc":"A9LID6","creator":"vnugnes","date":"2022-09-19T18:56:52.552Z","features":{"pfam":[{"id":"PF00869","name":"Flavivirus glycoprotein, central and dimerisation domains","start":282,"end":574},{"id":"PF00948","name":"Flavivirus non-structural Protein NS1","start":776,"end":1128},{"id":"PF00949","name":"Peptidase S7, Flavivirus NS3 serine protease","start":1490,"end":1641},{"id":"PF00972","name":"Flavivirus RNA-directed RNA polymerase, fingers and palm domains","start":2740,"end":3190},{"id":"PF01002","name":"Flavivirus non-structural protein NS2B","start":1347,"end":1473},{"id":"PF01003","name":"Flavivirus capsid protein C","start":6,"end":112},{"id":"PF01004","name":"Flavivirus envelope glycoprotein M","start":207,"end":279},{"id":"PF01005","name":"Flavivirus non-structural protein NS2A","start":1136,"end":1314},{"id":"PF01349","name":"Flavivirus non-structural protein NS4B","start":2243,"end":2483},{"id":"PF01350","name":"Flavivirus non-structural protein NS4A","start":2097,"end":2238},{"id":"PF01570","name":"Flavivirus polyprotein propeptide","start":120,"end":204},{"id":"PF01728","name":"FtsJ-like methyltransferase","start":2545,"end":2712},{"id":"PF02832","name":"Flavivirus glycoprotein, immunoglobulin-like domain","start":576,"end":671},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1658,"end":1804},{"id":"PF20483","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","start":3194,"end":3356},{"id":"PF20907","name":"Flavivirus NS3 helicase, C-terminal helical domain","start":1950,"end":2090},{"id":"PF21659","name":"Flavivirus envelope glycoprotein E, stem/anchor domain","start":674,"end":768}],"gene3D":[]},"length":3390,"name":"Genome polyprotein","ncbi_taxon_id":11069,"organism":"Dengue virus 3","regions":[{"start":674,"end":773,"reference_id":"30471923","reference_source":"pmid","reference_html":"Mechanism of Enhanced Immature Dengue Virus Attachment to Endosomal Membrane Induced by prM Antibody. <i> Wirawan M, Fibriansah G, Marzinek JK, Lim XX, Ng TS, Sim AYL, Zhang Q, Kostyuchenko VA, Shi J, Smith SA, Verma CS, Anand G, Crowe JE, Bond PJ, Lok SM. </i> Structure, 2019","date":"2022-09-19T19:07:16.096Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":5}],"cross_refs":[{"db":"PDB","id":"6IDK"},{"db":"PDB","id":"6IDL"}],"region_id":"DP03790r001","sample":[{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ABCD","id":"AW356"}],"statement":[{"text":"The electron microscopy evidences of the Immature Dengue virus serotype 3 enveloprotein in complex with human antibody 1H10 Fab at pH 5.0 shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:37:33.981Z"}},{"start":194,"end":280,"reference_id":"30471923","reference_source":"pmid","reference_html":"Mechanism of Enhanced Immature Dengue Virus Attachment to Endosomal Membrane Induced by prM Antibody. <i> Wirawan M, Fibriansah G, Marzinek JK, Lim XX, Ng TS, Sim AYL, Zhang Q, Kostyuchenko VA, Shi J, Smith SA, Verma CS, Anand G, Crowe JE, Bond PJ, Lok SM. </i> Structure, 2019","date":"2022-09-19T19:08:32.633Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":5}],"cross_refs":[{"db":"PDB","id":"6IDK"},{"db":"PDB","id":"6IDL"}],"region_id":"DP03790r002","sample":[{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ABCD","id":"AW356"}],"statement":[{"text":"The electron microscopy evidences of the Immature Dengue virus serotype 3 premembrane protein in complex with human antibody 1H10 Fab at pH 5.0 shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:37:35.214Z"}}],"regions_counter":2,"released":"2022_12","sequence":"MNNQRKKTGKPSINMLKRVRNRVSTGSQLAKRFSKELLNGQGPMKLVMAFIAFLRFLAIPPTAGVLARWGTFKKSGAIKVLKGFKKEISNMLSIINKRKKTSLCLMMILPAALAFHLTSRDGEPRMIVGKNERGKSLLFKTASGINMCTLIAMDLGEMCDDTVTYKCPHITEVEPEDIDCWCNLTSTWVTYGTCNQAGEHRRDKRSVALAPHVGMGLDTRTQTWMSAEGAWRQVEKVETWALRHPGFTILALFLAHYIGTSLTQKVVIFILLMLVTPSMTMRCVGVGNRDFVEGLSGATWVDVVLEHGGCVTTMAKNKPTLDIELQKTEATQLATLRKLCIEGKITNITTDSRCPTQGEAVLPEEQDQNYVCKHTYVDRGWGNGCGLFGKGSLVTCAKFQCLEPIEGKVVQYENLKYTVIITVHTGDQHQVGNETQGVTAEITPQASTTEAILPEYGTLGLECSPRTGLDFNEMILLTMKNKAWMVHRQWFFDLPLPWASGATTETPTWNRKELLVTFKNAHAKKQEVVVLGSQEGAMHTALTGATEIQNSGGTSIFAGHLKCRLKMDKLELKGMSYAMCTNTFVLKKEVSETQHGTILIKVEYKGEDAPCKIPFSTEDGQGKAHNGRLITANPVVTKKEEPVNIEAEPPFGESNIVIGIGDNALKINWYKKGSSIGKMFEATARGARRMAILGDTAWDFGSVGGVLNSLGKMVHQIFGSAYTALFSGVSWVMKIGIGVLLTWIGLNSKNTSMSFSCIAIGIITLYLGAVVQADMGCVINWKGKELKCGSGIFVTNEVHTWTEQYKFQADSPKRLATAIAGAWENGVCGIRSTTRMENLLWKQIANELNYILWENNIKLTVVVGDTIGVLEQGKRTLTPQPMELKYSWKTWGKAKIVTAETQNSSFIIDGPNTPECPSASRAWNVWEVEDYGFGVFTTNIWLKLREVYTQLCDHRLMSAAVKDERAVHADMGYWIESQKNGSWKLEKASLIEVKTCTWPKSHTLWSNGVLESDMIIPKSLAGPISQHNYRPGYHTQTAGPWHLGKLELDFNYCEGTTVVITESCGTRGPSLRTTTVSGKLIHEWCCRSCTLPPLRYMGEDGCWYGMEIRPISEKEENMVKSLVSAGSGKVDNFTMGVLCLAILFEEVMRGKFGKKHMIAGVFFTFVLLLSGQITWRDMAHTLIMIGSNASDRMGMGVTYLALIATFKIQPFLALGFFLRKLTSRENLLLGVGLAMATTLQLPEDIEQMANGIALGLMALKLITQFETYQLWTALVSLTCSNTIFTLTVAWRTATLILAGVSLLPVCQSSSMRKTDWLPMTVAAMGVPPLPLFIFSLKDTLKRRSWPLNEGVMAVGLVSILASSLLRNDVPMAGPLVAGGLLIACYVITGTSADLTVEKAADVTWEEEAEQTGVSHNLMITVDDDGTMRIKDDETENILTVLLKTALLIVSGIFPYSIPATLLVWHTWQKQTQRSGVLWDVPSPPETQKAELEEGVYRIKQQGIFGKTQVGVGVQKEGVFHTMWHVTRGAVLTHNGKRLEPNWASVKKDLISYGGGWRLSAQWQKGEEVQVIAVEPGKNPKNFQTMPGTFQTTTGEIGAIALDFKPGTSGSPIINREGKVVGLYGNGVVTKNGGYVSGIAQTNAEPDGPTPELEEEMFKKRNLTIMDLHPGSGKTRKYLPAIVREAIKRRLRTLILAPTRVVAAEMEEALKGLPIRYQTTATKSEHTGREIVDLMCHATFTMRLLSPVRVPNYNLIIMDEAHFTDPASIAARGYISTRVGMGEAAAIFMTATPPGTADAFPQSNAPIQDEERDIPERSWNSGNEWITDFAGKTVWFVPSIKAGNDIANCLRKNGKKVIQLSRKTFDTEYQKTKLNDWDFVVTTDISEMGANFKADRVIDPRRCLKPVILTDGPERVILAGPMPVTAASAAQRRGRVGRNPQKENDQYIFTGQPLNNDEDHAHWTEAKMLLDNINTPEGIIPALFEPEREKSAAIDGEYRLKGESRKTFVELMRRGDLPVWLAHKVASEGIKYTDRKWCFDGQRNNQILEENMDVEIWTKEGEKKKLRPRWLDARTYSDPLALKEFKDFAAGRKSIALDLVTEIGRVPSHLAHRTRNALDNLVMLHTSEHGGRAYRHAVEELPETMETLLLLGLMILLTGGAMLFLISGKGIGKTSIGLICVIASSGMLWMAEVPLQWIASAIVLEFFMMVLLIPEPEKQRTPQDNQLAYVVIGILTLAAIIAANEMGLLETTKRDLGMSKEPGVVSPTSYLDVDLHPASAWTLYAVATTVITPMLRHTIENSTANVSLAAIANQAVVLMGLDKGWPISKMDLGVPLLALGCYSQVNPLTLTAAVLLLITHYAIIGPGLQAKATREAQKRTAAGIMKNPTVDGIMTIDLDPVIYDSKFEKQLGQVMLLVLCAVQLLLMRTSWALCEALTLATGPITTLWEGSPGKFWNTTIAVSMANIFRGSYLAGAGLAFSIMKSVGTGKRGTGSQGETLGEKWKKKLNQLSRKEFDLYKKSGITEVDRTEAKEGLKRGETTHHAVSRGSAKLQWFVERNMVIPEGRVIDLGCGRGGWSYYCAGLKKVTEVRGYTKGGPGHEEPVPMSTYGWNIVKLMSGKDVFYLPPEKCDTLLCDIGESSPSPTVEESRTIRVLKMVEPWLKNNQFCIKVLNPYMPTVIEHLERLQRKHGGMLVRNPLSRNSTHEMYWISNGTGNIVSSVNMVSRLLLNRFTMTHRRPTIEKDVDLGAGTRHVNAEPETPNMDVIGERIKRIKEEHNSTWHYDDENPYKTWAYHGSYEVKATGSASSMINGVVKLLTKPWDVVPMVTQMAMTDTTPFGQQRVFKEKVDTRTPRPMPGTRKVMEITAEWLWRTLGRNKRPRLCTREEFTKKVRTNAAMGAVFTEENQWDSAKAAVEDEEFWKLVDRERELHKLGKCGSCVYNMMGKREKKLGEFGKAKGSRAIWYMWLGARYLEFEALGFLNEDHWFSRENSYSGVEGEGLHKLGYILRDISKIPGGAMYADDTAGWDTRITEDDLHNEEKIIQQMDPEHRQLANAIFKLTYQNKVVKVQRPTPTGTVMDIISRKDQRGSGQVGTYGLNTFTNMEAQLVRQMEGEGVLTKADLENPHLLEKKITQWLETKGVERLKRMAISGDDCVVKPIDDRFANALLALNDMGKVRKDIPQWQPSKGWHDWQQVPFCSHHFHELIMKDGRKLVVPCRPQDELIGRARISQGAGWSLRETACLGKAYAQMWSLMYFHRRDLRLASNAICSAVPVHWVPTSRTTWSIHAHHQWMTTEDMLTVWNRVWIEENPWMEDKTPVTTWENVPYLGKREDQWCGSLIGLTSRATWAQNIPTAIQQVRSLIGNEEFLDYMPSMKRFRKEEELEGAIW","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Flavivirus"],"dataset":["Neglected tropical diseases proteins","Viral proteins"],"genes":[],"disorder_content":0.055162241887905604,"disprot_consensus":{"full":[{"start":194,"end":280,"type":"D"},{"start":674,"end":773,"type":"D"}],"Structural state":[{"start":194,"end":280,"type":"D"},{"start":674,"end":773,"type":"D"}]}},{"disprot_id":"DP03791","acc":"Q26502","creator":"vnugnes","date":"2022-09-19T19:31:34.802Z","features":{"pfam":[{"id":"PF00079","name":"Serpin (serine protease inhibitor)","start":20,"end":402}],"gene3D":[]},"length":406,"name":"Serine protease inhibitor","ncbi_taxon_id":6185,"organism":"Schistosoma haematobium","regions":[{"start":1,"end":15,"reference_id":"22683791","reference_source":"pmid","reference_html":"Three-dimensional structure of a schistosome serpin revealing an unusual configuration of the helical subdomain. <i> Granzin J, Huang Y, Topbas C, Huang W, Wu Z, Misra S, Hazen SL, Blanton RE, Lee X, Weiergräber OH. </i> Acta Crystallogr D Biol Crystallogr, 2012","date":"2022-09-19T19:35:47.988Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":71,"end":71,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":89,"end":89,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":186,"end":186,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":224,"end":224,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":225,"end":225,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":231,"end":231,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":392,"end":392,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":395,"end":395,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":400,"end":400,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"3STO"}],"region_id":"DP03791r001","sequence_construct":"MGILFTPENDDPYANISSHKAFTHAYLSTVTADFGGDNFLTCPLGILFTLGILLGSGGAQGRTGYQIGKTMRLKSTSSSWNSSEAQQEMKSLYQELNNSLTSEKTFLNEKEENVVRISTGIFVEKTYEVERRFNESIANDSEGELKQVDFSNRTSATVDINDWVDQQSNGLLEKFFTDDIPDDTAMILVNVFYFRDFWQSPFEPHYTRKEDFYISPDRQITVDMMTQEGVMKYGKFEDEGFEIVSKPLNNTRFTFVIVLPLEKWSLNGATELLNGNKVLSEYVKNLKETTVSLRLPKFTLKNTLDLVPTLKSIGVVDLFDPVKSDLSGITPNPNLYVNEFIQTNVLKLNESGIEATTVTSPIFVPFSAIIPEVDFHVTHPFICFIYDQQLTMPIMAAKVMNPVLQS","statement":[{"text":"Several portions of the structure were not traceable owing to poor observed electron density; in addition to the extreme termini (residues 1–15 and 404–406, respectively), this also applies to loop segments 108–110 and 173–180.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-12T09:44:46.436Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MGILFTPENDDPYANISSHKAFTHAYLSTVTADFGGDNFLTCPLGILFTLGILLGSGGAQGRTGYQIGKTMRLKSTSSSWNSSEAQQEMKSLYQELNNSLTSEKTFLNEKEENVVRISTGIFVEKTYEVERRFNESIANDSEGELKQVDFSNRTSATVDINDWVDQQSNGLLEKFFTDDIPDDTAMILVNVFYFRDFWQSPFEPHYTRKEDFYISPDRQITVDMMTQEGVMKYGKFEDEGFEIVSKPLNNTRFTFVIVLPLEKWSLNGATELLNGNKVLSEYVKNLKETTVSLRLPKFTLKNTLDLVPTLKSIGVVDLFDPVKSDLSGITPNPNLYVNEFIQTNVLKLNESGIEATTVTSPIFVPFSAIIPEVDFHVTHPFICFIYDQQLTMPIMAAKVMNPVLQS","taxonomy":["Eukaryota","Metazoa","Spiralia","Lophotrochozoa","Platyhelminthes","Trematoda","Digenea","Strigeidida","Schistosomatoidea","Schistosomatidae","Schistosoma"],"dataset":["Neglected tropical diseases proteins"],"genes":[],"alphafold_very_low_content":0.059113300492610835,"disorder_content":0.03694581280788178,"disprot_consensus":{"full":[{"start":1,"end":15,"type":"D"}],"Structural state":[{"start":1,"end":15,"type":"D"}]}},{"disprot_id":"DP03792","acc":"G4VQX9","creator":"vnugnes","date":"2022-09-19T19:49:42.323Z","features":{"pfam":[{"id":"PF00206","name":"Lyase","start":92,"end":299},{"id":"PF10397","name":"Adenylosuccinate lyase C-terminus","start":373,"end":455}],"gene3D":[]},"length":480,"name":"Adenylosuccinate lyase","ncbi_taxon_id":6183,"organism":"Schistosoma mansoni","regions":[{"start":280,"end":289,"reference_id":"28347672","reference_source":"pmid","reference_html":"Structural and kinetic analysis of Schistosoma mansoni Adenylosuccinate Lyase (SmADSL). <i> Romanello L, Serrão VHB, Torini JR, Bird LE, Nettleship JE, Rada H, Reddivari Y, Owens RJ, DeMarco R, Brandão-Neto J, Pereira HD. </i> Mol Biochem Parasitol, 2017","date":"2022-09-19T19:53:01.866Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"5EYV"}],"region_id":"DP03792r001","statement":[{"text":"Furthermore, the domain II carries unresolved portion of the structure: residues 281QIGSSA286 (SmADSL-AMP) and 281QIGSSAMPY289 (SmADSL-Apo) are on a disordered loop. This loop contains the signature sequence 281Q*GSS*MP*K*NP293 unique to the β-elimination superfamily [12].","type":"Results"},{"text":"The PDB shows the region 280-289 lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-12T09:45:22.557Z"}},{"start":280,"end":289,"reference_id":"28347672","reference_source":"pmid","reference_html":"Structural and kinetic analysis of Schistosoma mansoni Adenylosuccinate Lyase (SmADSL). <i> Romanello L, Serrão VHB, Torini JR, Bird LE, Nettleship JE, Rada H, Reddivari Y, Owens RJ, DeMarco R, Brandão-Neto J, Pereira HD. </i> Mol Biochem Parasitol, 2017","date":"2022-09-19T19:54:28.267Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"5EYV"}],"region_id":"DP03792r002","statement":[{"text":"Furthermore, the domain II carries unresolved portion of the structure: residues 281QIGSSA286 (SmADSL-AMP) and 281QIGSSAMPY289 (SmADSL-Apo) are on a disordered loop. This loop contains the signature sequence 281Q*GSS*MP*K*NP293 unique to the β-elimination superfamily [12].","type":"Results"},{"text":"The PDB shows the region 280-289 lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-12T09:44:38.992Z"}}],"regions_counter":2,"released":"2022_12","sequence":"MDEFEEYRNPLTKRYASREMVCNFGEKRKVILWRQLWIWLAETQKELGFDITDEQINEMKSQRDSVDFGTAAAEEKARRHDVMAHVYTFALACPKAAPIIHLGATSCFVGDNADLIMLKDGLNILLPKVARCIDRLAKKAMLHKSLICLARTHLQPAQPTTMGRRICMWIQDLLLDLENLERLKNHTIRFRGAKGAVGTQASFMDLFQGDHQKVIKLDEILTKKSGFQRSWCVTGQTYPRKVDIEITNALSNIGATVHKICTDIRLLSSFHEVEEPFETKQIGSSAMPYKRNPIRSERACSLARYLMHISTSMVSTVSVQWLERSLDDSAIRRIVLPEAFLAADACLTLLQNIAEGLIVYPMVMEANLNSELPFLVVERILVKMVSEGAANRQECHERLRKHSHEAAAEIKLKGLKNSLMDKLLNDYYFAPIHSLLPTVLDPSYMIGRAVEQVEVFLNTEVDPAIHSYKDCLALNSNITI","taxonomy":["Eukaryota","Metazoa","Spiralia","Lophotrochozoa","Platyhelminthes","Trematoda","Digenea","Strigeidida","Schistosomatoidea","Schistosomatidae","Schistosoma"],"dataset":["Neglected tropical diseases proteins"],"genes":[],"alphafold_very_low_content":0,"disorder_content":0.020833333333333332,"disprot_consensus":{"full":[{"start":280,"end":289,"type":"D"}],"Structural state":[{"start":280,"end":289,"type":"D"}],"Disorder function":[{"start":280,"end":289,"type":"F"}]}},{"disprot_id":"DP03793","acc":"Q6WVP6","creator":"vnugnes","date":"2022-09-19T20:03:11.600Z","features":{"pfam":[{"id":"PF00491","name":"Arginase family","start":25,"end":332}],"gene3D":[]},"length":364,"name":"Arginase","ncbi_taxon_id":6183,"organism":"Schistosoma mansoni","regions":[{"start":1,"end":17,"reference_id":"25007099","reference_source":"pmid","reference_html":"Crystal structure of Schistosoma mansoni arginase, a potential drug target for the treatment of schistosomiasis. <i> Hai Y, Edwards JE, Van Zandt MC, Hoffmann KF, Christianson DW. </i> Biochemistry, 2014","date":"2022-09-19T20:08:26.858Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"4Q3P"}],"region_id":"DP03793r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29035","entry_name":"manganese(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":"glycerol"}],"statement":[{"text":"Disordered segments excluded from the final models include the N-terminal hexahistidine tag and its linker segment, residues M1–P17, surface loop K111–S119, and T362–Q364 at the C-terminus.","type":"Methods"},{"text":"The N-terminal extension (17 residues with the hexahistidine tag and its linker segment) and the inserted loop lack clearly defined electron density and are presumed to be disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-10-12T09:44:00.247Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MLKSVATPYYPIQDEKPKLLYTSANFLGIPTNRGQPKIGTYQGPELIRKSNFFQLVAEDGIQLTDCGDIIPVELNEAEDPQRFGMKWSRSFSLTTLRIAERVEELMKQSNKHTVELSGSKSTPLVIVGGDHSMATGTILGHAEAKPDLCVLWIDAHGDINTPLNSASGNMHGMPLSFLVKELQDQIPWLDDFEGIKPCLNASNIAYIGLRDLDAHETHDIRKHGIAYFTMLDVDRMGIEAVIKEALLAVNPRLEKAIHLSFDIDALDPLVAPSTGTAVPGGLTLREGLRICEEVSATGKLSVVELAELNPLLGSQEDVLKTQSSAVHILRACLGHCRSGHLPFKVRNLTDQGIMSRAAHMQTKQ","taxonomy":["Eukaryota","Metazoa","Spiralia","Lophotrochozoa","Platyhelminthes","Trematoda","Digenea","Strigeidida","Schistosomatoidea","Schistosomatidae","Schistosoma"],"dataset":["Neglected tropical diseases proteins"],"genes":[],"alphafold_very_low_content":0.0989010989010989,"disorder_content":0.046703296703296704,"disprot_consensus":{"full":[{"start":1,"end":17,"type":"D"}],"Structural state":[{"start":1,"end":17,"type":"D"}]}},{"disprot_id":"DP03794","acc":"Q5SBG8","creator":"vnugnes","date":"2022-09-19T20:20:50.190Z","features":{"pfam":[{"id":"PF00869","name":"Flavivirus glycoprotein, central and dimerisation domains","start":293,"end":589},{"id":"PF00948","name":"Flavivirus non-structural Protein NS1","start":794,"end":1143},{"id":"PF00949","name":"Peptidase S7, Flavivirus NS3 serine protease","start":1523,"end":1672},{"id":"PF00972","name":"Flavivirus RNA-directed RNA polymerase, fingers and palm domains","start":2781,"end":3233},{"id":"PF01002","name":"Flavivirus non-structural protein NS2B","start":1380,"end":1499},{"id":"PF01003","name":"Flavivirus capsid protein C","start":6,"end":123},{"id":"PF01004","name":"Flavivirus envelope glycoprotein M","start":218,"end":290},{"id":"PF01005","name":"Flavivirus non-structural protein NS2A","start":1155,"end":1308},{"id":"PF01349","name":"Flavivirus non-structural protein NS4B","start":2274,"end":2519},{"id":"PF01350","name":"Flavivirus non-structural protein NS4A","start":2129,"end":2271},{"id":"PF01570","name":"Flavivirus polyprotein propeptide","start":133,"end":214},{"id":"PF01728","name":"FtsJ-like methyltransferase","start":2583,"end":2752},{"id":"PF02832","name":"Flavivirus glycoprotein, immunoglobulin-like domain","start":592,"end":689},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1690,"end":1836},{"id":"PF20483","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","start":3237,"end":3400},{"id":"PF20907","name":"Flavivirus NS3 helicase, C-terminal helical domain","start":1980,"end":2122},{"id":"PF21659","name":"Flavivirus envelope glycoprotein E, stem/anchor domain","start":692,"end":786}],"gene3D":[]},"length":3433,"name":"Genome polyprotein","ncbi_taxon_id":11082,"organism":"West Nile virus","regions":[{"start":900,"end":920,"reference_id":"25286855","reference_source":"pmid","reference_html":"Use of massively multiple merged data for low-resolution S-SAD phasing and refinement of flavivirus NS1. <i> Akey DL, Brown WC, Konwerski JR, Ogata CM, Smith JL. </i> Acta Crystallogr D Biol Crystallogr, 2014","date":"2022-09-19T20:28:43.367Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"4TPL"}],"region_id":"DP03794r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"506227","entry_name":"N-acetyl-D-glucosamine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"CAS Registry Number","id":"9041-29-6"}],"statement":[{"text":"The NS1 structure is complete with the exception of one internal 20-residue disordered loop.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:39:33.770Z"}},{"start":900,"end":920,"reference_id":"25286855","reference_source":"pmid","reference_html":"Use of massively multiple merged data for low-resolution S-SAD phasing and refinement of flavivirus NS1. <i> Akey DL, Brown WC, Konwerski JR, Ogata CM, Smith JL. </i> Acta Crystallogr D Biol Crystallogr, 2014","date":"2022-09-19T20:29:00.929Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"4TPL"}],"region_id":"DP03794r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"506227","entry_name":"N-acetyl-D-glucosamine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"CAS Registry Number","id":"9041-29-6"}],"statement":[{"text":"The NS1 structure is complete with the exception of one internal 20-residue disordered loop.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:39:38.858Z"}}],"regions_counter":2,"released":"2022_12","sequence":"MSKKPGGPGKSRAVNMLKRGMPRVLSLIGLKRAMLSLIDGKGPIRFVLALLAFFRFTAIAPTRAVLDRWRGVNKQTAMKHLLSFKKELGTLTSAINRRSSKQKKRGGKTGIAVMIGLIASVGAVTLSDFQGKVMMTVNATDVTDVITIPTAAGKNLCIVRAMDVGYMCDDTITYECPVLSAGNDPEDIDCWCTKSAVYVRYGRCTKTRHSRRSRRSLTVQTHGESTLANKKGAWMDSTKATRYLVKTESWILRNPGYALVAAVIGWMLGSNTMQRVVFVVLLLLVAPAYSFNCLGMSNRDFLEGVSGATWVDLVLEGDSCVTIMSKDKPTIDVKMMNMEAANLAEVRSYCYLATVSDLSTKAACPTMGEAHNDKRADPAFVCRQGVVDRGWGNGCGLFGKGSIDTCAKFACSTKAIGRTILKENIKYEVAIFVHGPTTVESHGNYSTQAGATQAGRFSITPAAPSYTLKLGEYGEVTVDCEPRSGIDTNAYYVMTVGTKTFLVHREWFMDLNLPWSSAGSTVWRNRETLMEFEEPHATKQSVIALGSQEGALHQALAGAIPVEFSSNTVKLTSGHLKCRVKMEKLQLKGTTYGVCSKAFKFLGTPADTGHGTVVLELQYTGTDGPCKVPISSVASLNDLTPVGRLVTVNPFVSVATANAKVLIELEPPFGDSYIVVGRGEQQINHHWHKSGSSIGKAFTTTLKGAQRLAALGDTAWDFGSVGGVFTSVGKAVHQVFGGAFRSLFGGMSWITQGLLGALLLWMGINARDRSIALTFLAVGGVLLFLSVNVHADTGCAIDISRQELRCGSGVFIHNDVEAWMDRYKYYPETPQGLAKIIQKAHKEGVCGLRSVSRLEHQMWEAVKDELNTLLKENGVDLSVVVEKQEGMYKSAPKRLTATTEKLEIGWKAWGKSILFAPELANNTFVVDGPETKECPTQNRAWNSLEVEDFGFGLTSTRMFLKVRESNTTECDSKIIGTAVKNNLAIHSDLSYWIESRLNDTWKLERAVLGEVKSCTWPETHTLWGDGILESDLIIPVTLAGPRSNHNRRPGYKTQNQGPWDEGRVEIDFDYCPGTTVTLSESCGHRGPATRTTTESGKLITDWCCRSCTLPPLRYQTDSGCWYGMEIRPQRHDEKTLVQSQVNAYNADMIDPFQLGLLVVFLATQEVLRKRWTAKISMPAILIALLVLVFGGITYTDVLRYVILVGAAFAESNSGGDVVHLALMATFKIQPVFMVASFLKARWTNQENILLMLAAVFFQMAYHDARQILLWEIPDVLNSLAVAWMILRAITFTTTSNVVVPLLALLTPGLRCLNLDVYRILLLMVGIGSLIREKRSAAAKKKGASLLCLALASTGLFNPMILAAGLIACDPNRKRGWPATEVMTAVGLMFAIVGGLAELDIDSMAIPMTIAGLMFAAFVISGKSTDMWIERTADISWESDAEITGSSERVDVRLDDDGNFQLMNDPGAPWKIWMLRMVCLAISAYTPWAILPSVVGFWITLQYTKRGGVLWDTPSPKEYKKGDTTTGVYRIMTRGLLGSYQAGAGVMVEGVFHTLWHTTKGAALMSGEGRLDPYWGSVKEDRLCYGGPWKLQHKWNGQDEVQMIVVEPGKNVKNVQTKPGVFKTPEGEIGAVTLDFPTGTSGSPIVDKNGDVIGLYGNGVIMPNGSYISAIVQGERMDEPIPAGFEPEMLRKKQITVLDLHPGAGKTRRILPQIIKEAINRRLRTAVLAPTRVVAAEMAEALRGLPIRYQTSAVPREHNGNEIVDVMCHATLTHRLMSPHRVPNYNLFVMDEAHFTDPASIAARGYISTKVELGEAAAIFMTATPPGTSDPFPESNSPISDLQTEIPDRAWNSGYEWITEYTGKTVWFVPSVKMGNEIALCLQRAGKKVVQLNRKSYETEYPKCKNDDWDFVITTDISEMGANFKASRVIDSRKSVKPTIITEGEGRVILGEPSAVTAASAAQRRGRIGRNPSQVGDEYCYGGHTNEDDSNFAHWTEARIMLDNINMPNGLIAQFYQPEREKVYTMDGEYRLRGEERKNFLELLRTADLPVWLAYKVAAAGVSYHDRRWCFDGPRTNTILEDNNEVEVITKLGERKILRPRWIDARVYSDHQALKAFKDFASGKRSQIGLIEVLGKMPEHFMGKTWEALDTMYVVATAEKGGRAHRMALEELPDALQTIALIALLSVMTMGVFFLLMQRKGIGKIGLGGAVLGVATFFCWMAEVPGTKIAGMLLLSLLLMIVLIPEPEKQRSQTDNQLAVFLICVMTLVSAVAANEMGWLDKTKSDISSLFGQRIEVKENFSMGEFLLDLRPATAWSLYAVTTAVLTPLLKHLITSDYINTSLTSINVQASALFTLARGFPFVDVGVSALLLAAGCWGQVTLTVTVTAATLLFCHYAYMVPGWQAEAMRSAQRRTAAGIMKNAVVDGIVATDVPELERTTPIMQKKVGQIMLILVSLAAVVVNPSVKTVREAGILITAAAVTLWENGASSVWNATTAIGLCHIMRGGWLSCLSIAWTLIKNMEKPGLKRGGAKGRTLGEVWKERLNQMTKEEFTRYRKEAIIEVDRSAAKHARKEGNVTGGHPVSRGTAKLRWLVERRFLEPVGKVIDLGCGRGGWCYYMATQKRVQEVRGYTKGGPGHEEPQLVQSYGWNIVTMKSGVDVFYRPSECCDTLLCDIGESSSSAEVEEHRTIRVLEMVEDWLHRGPREFCVKVLCPYMPKVIEKMELLQRRYGGGLVRNPLSRNSTHEMYWVSRASGNVVHSVNMTSQVLLGRMEKRTWKGPQYEEDVNLGSGTRAVGKPLLNSDTSKIKNRIERLRREYSSTWHYDENHPYRTWNYHGSYDVKPTGSASSLVNGVVRLLSKPWDTITNVTTMAMTDTTPFGQQRVFKEKVDTKAPEPPEGVKYVLNETTNWLWAFLAREKRPRMCSREEFIRKVNSNAALGAMFEEQNQWRSAREAVEDPKFWEMVDEEREAHLRGECHTCIYNMMGKREKKPGEFGKAKGSRAIWFMWLGARFLEFEALGFLNEDHWLGRKNSGGGVEGLGLQKLGYILREVGTRPGGKIYADDTAGWDTRITRADLENEAKVLELLDGEHRRLARAIIELTYRHKVVKVMRPAADGRTVMDVISREDQRGSGQVVTYALNTFTNLAVQLVRMMEGEGVIGPDDVEKLTKGKGPKVRTWLFENGEERLSRMAVSGDDCVVKPLDDRFATSLHFLNAMSKVRKDIQEWKPSTGWYDWQQVPFCSNHFTELIMKDGRTLVVPCRGQDELVGRARISPGAGWNVRDTACLAKSYAQMWLLLYFHRRDLRLMANAICSAVPVNWVPTGRTTWSIHAGGEWMTTEDMLEVWNRVWIEENEWMEDKTPVEKWSDVPYSGKREDIWCGSLIGTRARATWAENIQVAINQVRAIIGDEKYVDYMSSLKRYEDTTLVEDTVL","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Flavivirus"],"dataset":["Neglected tropical diseases proteins","Viral proteins"],"genes":[],"disorder_content":0.006117098747451209,"disprot_consensus":{"full":[{"start":900,"end":920,"type":"D"}],"Structural state":[{"start":900,"end":920,"type":"D"}],"Disorder function":[{"start":900,"end":920,"type":"F"}]}},{"disprot_id":"DP03797","acc":"Q4QDS0","creator":"vnugnes","date":"2022-09-21T13:49:45.504Z","features":{"pfam":[{"id":"PF00587","name":"tRNA synthetase class II core domain (G, H, P, S and T)","start":319,"end":492},{"id":"PF03129","name":"Anticodon binding domain","start":511,"end":603},{"id":"PF04073","name":"Aminoacyl-tRNA editing domain","start":28,"end":157},{"id":"PF09180","name":"Prolyl-tRNA synthetase, C-terminal","start":639,"end":731}],"gene3D":[]},"length":731,"name":"Proline--tRNA ligase","ncbi_taxon_id":5664,"organism":"Leishmania major","regions":[{"start":288,"end":328,"reference_id":"28867614","reference_source":"pmid","reference_html":"Targeting Prolyl-tRNA Synthetase to Accelerate Drug Discovery against Malaria, Leishmaniasis, Toxoplasmosis, Cryptosporidiosis, and Coccidiosis. <i> Jain V, Yogavel M, Kikuchi H, Oshima Y, Hariguchi N, Matsumoto M, Goel P, Touquet B, Jumani RS, Tacchini-Cottier F, Harlos K, Huston CD, Hakimi MA, Sharma A. </i> Structure, 2017","date":"2022-09-21T13:53:45.401Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"5XIL"}],"region_id":"DP03797r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30089","entry_name":"acetate"}],"statement":[{"text":"The PDB structure shows this region lacks electron density, indicanting it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:40:40.660Z"}},{"start":676,"end":687,"reference_id":"28867614","reference_source":"pmid","reference_html":"Targeting Prolyl-tRNA Synthetase to Accelerate Drug Discovery against Malaria, Leishmaniasis, Toxoplasmosis, Cryptosporidiosis, and Coccidiosis. <i> Jain V, Yogavel M, Kikuchi H, Oshima Y, Hariguchi N, Matsumoto M, Goel P, Touquet B, Jumani RS, Tacchini-Cottier F, Harlos K, Huston CD, Hakimi MA, Sharma A. </i> Structure, 2017","date":"2022-09-21T13:55:57.742Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"5XIL"}],"region_id":"DP03797r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30089","entry_name":"acetate"}],"statement":[{"text":"The PDB structure shows this region lacks electron density, indicanting it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:40:41.975Z"}}],"regions_counter":2,"released":"2022_12","sequence":"MSAKDCRGEPELLALLKELNIELPTISHGEMHTVEEANRELVQFGTPCVGTKNMFLKSKKGELVLLTAVHTTKTDMHAIEKAAGTRNLRFAPAEILSENLAVVQGCVTPFALINNIEKHNVTVLLDKNLKDSPIPFVLHPCRNDKSSLVVFEQLERFLEKVGYAYKLVDFGAASADAAVTGGAAAPAPKPKKAPADAAAAKRGGGGGGAAAPASAQSGETKLGIAAKREENFSAWYIDVITKAEMIEYYDVSGCYIIRPWAYYVWKCVQRFLGGKIEKLGVEDCYFPMFVSRSCLEREKDHIEGFAPEVAWVTRAGDTELEQPVAVRPTSETVMYPYYAKWIRSHRDLPVRLNMWNNVIRWEFSHPTPFIRTREFLWQEGHCAWAKAEECAKEVLEILECYASVYEQLLAVPVVRGRKTEKEKFAGGDYTTTVETFIEAVGRGCQGATSHNLGQNFGKMFDIRFQDPENNEQTLIPWQNSWGLSTRVIGVMIMVHGDNRGMVMPPRVASTQVIIIPVGITKDTTEEARQELLASCWRLESELCEGGVRARCDLRDNYSPGWRFNHWEVKGVPLRVELGPRELAERSLAVAVRHSGARHSVAWDAQTPAAVAALLEDVHAQMYARAKETMETHRVRVTEWTEFVPTLNRKCLILAPWCGAMECENQVKKDSAEESKVAQAQETREDARAPSMGAKTLCIPFEQPEEPAEGHECICKGCTKPATTWVLFGRSY","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"orfNames":[{"value":"LMJF_18_1220","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAJ04056.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAJ04056.1"}}]}]}],"alphafold_very_low_content":0.07934336525307797,"disorder_content":0.07250341997264022,"disprot_consensus":{"full":[{"start":288,"end":328,"type":"D"},{"start":676,"end":687,"type":"D"}],"Structural state":[{"start":288,"end":328,"type":"D"},{"start":676,"end":687,"type":"D"}]}},{"disprot_id":"DP03798","acc":"Q711P7","creator":"vnugnes","date":"2022-09-21T14:08:51.439Z","features":{"pfam":[{"id":"PF03738","name":"Glutathionylspermidine synthase preATP-grasp","start":276,"end":631},{"id":"PF05257","name":"CHAP domain","start":53,"end":148}],"gene3D":[]},"length":652,"name":"Putative trypanothione synthetase","ncbi_taxon_id":5664,"organism":"Leishmania major","regions":[{"start":252,"end":262,"reference_id":"18420578","reference_source":"pmid","reference_html":"Leishmania trypanothione synthetase-amidase structure reveals a basis for regulation of conflicting synthetic and hydrolytic activities. <i> Fyfe PK, Oza SL, Fairlamb AH, Hunter WN. </i> J Biol Chem, 2008","date":"2022-09-21T14:16:47.256Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP03798r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"}],"statement":[{"text":"Molecule A has three disordered, presumably flexible loops, comprising residues 251-263, 551-579, 614-625. Molecule B has five loops missing, between 227 and 234, 250 and 263, 551 and 578, 617 and 625, and 632 and 637.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"2VOB"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:41:23.168Z"}},{"start":552,"end":577,"reference_id":"18420578","reference_source":"pmid","reference_html":"Leishmania trypanothione synthetase-amidase structure reveals a basis for regulation of conflicting synthetic and hydrolytic activities. <i> Fyfe PK, Oza SL, Fairlamb AH, Hunter WN. </i> J Biol Chem, 2008","date":"2022-09-21T14:16:56.623Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP03798r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"}],"statement":[{"text":"Molecule A has three disordered, presumably flexible loops, comprising residues 251-263, 551-579, 614-625. Molecule B has five loops missing, between 227 and 234, 250 and 263, 551 and 578, 617 and 625, and 632 and 637.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"2VOB"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:41:24.810Z"}}],"regions_counter":2,"released":"2022_12","sequence":"MSSLQRASVSFNKPGHIPFGAVQGYAPGGVPAYSNKHDHYFSGERNIEDNIFFGFKYQCVEFARRWLLVRKGLLLPDVNWACHIFQLKEVRDAATTESFAVLQVRNGTTTKPEADALLVYPSTDANPVGHVGTITEVGDDYVCVADQNYRFHKWESSCAYKLKLDHRDGIWTIIDDIDADEIEIPLGWLTFPGRANRPEGAPPVALHPSLHFKEPPKPYLLRRNFLPTESKANWLDMNNPAERLFVEEFGMDVSRTRLEEKVVSYYESNHEFHLRCVAYGTQLHAIFMEATAQVIESDEKLRLFAIPEEFWPRIRHSWKYQQTYISGRFDFAFNNETGEVKCFEYNADSASTLLECGLIQQKWAESVGLDKQDTRGSGFAVERNLKMAWANSGATGRVHFCVDEEREEQYTALYCMQAAEAVGLEGKLCILFDEFRFDDNGHVVDSDGVRVRNVWKTWMWESAITDYYAAREERGENWKPSPKDKVRLCDLLLGDDWEILYFEPMWKVIPSNKAILPMIYHNHPEHPAILKAEYELTDELRKHGYAKKPIVGRVGSNVIITSGDGVVHAESGGKYGKRNMIYQQLFELKKQDDYYAIIGGWMIGDAFSGTGIREDKSVITGVDSPFAAVRIKTDKLPHPVTLKDIDKMAEDE","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"name":{"value":"tryS","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAC83968.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAC83968.1"}}]},"synonyms":[{"value":"TRYS","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CBZ12255.1","url":"https://www.ebi.ac.uk/ena/browser/view/CBZ12255.1"}}]}],"orfNames":[{"value":"LMJF_27_1870","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CBZ12255.1","url":"https://www.ebi.ac.uk/ena/browser/view/CBZ12255.1"}}]}]}],"alphafold_very_low_content":0.024539877300613498,"disorder_content":0.05674846625766871,"disprot_consensus":{"full":[{"start":252,"end":262,"type":"D"},{"start":552,"end":577,"type":"D"}],"Structural state":[{"start":252,"end":262,"type":"D"},{"start":552,"end":577,"type":"D"}]}},{"disprot_id":"DP03799","acc":"Q9U5N6","creator":"vnugnes","date":"2022-09-21T14:37:13.641Z","features":{"pfam":[{"id":"PF00274","name":"Fructose-bisphosphate aldolase class-I","start":24,"end":371}],"gene3D":[]},"length":371,"name":"Fructose-bisphosphate aldolase","ncbi_taxon_id":5665,"organism":"Leishmania mexicana","regions":[{"start":358,"end":370,"reference_id":"10891264","reference_source":"pmid","reference_html":"Structures of type 2 peroxisomal targeting signals in two trypanosomatid aldolases. <i> Chudzik DM, Michels PA, de Walque S, Hol WG. </i> J Mol Biol, 2000","date":"2022-09-21T14:38:35.788Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"1EPX"}],"region_id":"DP03799r001","statement":[{"text":"In both the T. brucei and L. mexicana aldolases, the 11 Cterminal residues were not visible in the density of any subunit.","type":"Methods"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:41:56.087Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MSRVTVLQSQLPAYNRLKTPYESELIATVKKLTTPGKGLLAADESIGSCTKRFQPIGLSNTEEHRRQYRALMLEAEGFEQYISGVILHDETVGQKASNGQTFPEYLTARGVVPGIKTDMGLCPLLEGAEGEQMTEGLDGYVKRASAYYKKGCRFCKWRNVYKIQNGTVSESAVRFNAETLARYAILSQMSGLVPIVEPEVMIDGKHDIDTCQRVSEHVWREVVAALQRHGVIWEGCLLKPNMVVPGAESGKTAAPEQVAHYTVMTLARTMPAMLPGVMFLSGGLSEVQASEYLNAINNSPLPRPYFLSFSYARALQSSALKAWGGKESGLAAGRRAFLHRARMNSMAQLGKYKRSDDDASSSSLYVKGNTY","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"name":{"value":"ald","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAB55315.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAB55315.1"}}]}}],"alphafold_very_low_content":0.01078167115902965,"disorder_content":0.03504043126684636,"disprot_consensus":{"full":[{"start":358,"end":370,"type":"D"}],"Structural state":[{"start":358,"end":370,"type":"D"}]}},{"disprot_id":"DP03800","acc":"P42861","creator":"vnugnes","date":"2022-09-21T15:22:11.402Z","features":{"pfam":[{"id":"PF00342","name":"Phosphoglucose isomerase","start":101,"end":596}],"gene3D":[]},"length":605,"name":"Glucose-6-phosphate isomerase","ncbi_taxon_id":5665,"organism":"Leishmania mexicana","regions":[{"start":1,"end":48,"reference_id":"15206941","reference_source":"pmid","reference_html":"The crystal structure of glucose-6-phosphate isomerase from Leishmania mexicana reveals novel active site features. <i> Cordeiro AT, Michels PA, Delboni LF, Thiemann OH. </i> Eur J Biochem, 2004","date":"2022-09-21T15:24:59.644Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"1T10"}],"region_id":"DP03800r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16084","entry_name":"beta-D-fructofuranose 6-phosphate"}],"statement":[{"text":"For the first 44 and the last residue – Leu605 – of PGI-Lm (Fig. 2), no electron density was distinguishable in the 2σA|Fo|-D|Fc| map of both chains of the homodimer. The absence of continuous electron density for residues 1–44 indicates that the N-terminal sequence is not ordered. Based on the electron density map and sequence alignment, four additional residues (Val45 to Ser48) could be added to that region of PGI-Lm (Fig. 2).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:44:04.653Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MSDYFSKLKEHVVESTEINGCTPSIATATFNAPYEVARKTKMLGVTDSSLLNLPAWKRLQSLYEKYGNDSILSHFEKDHQRFQRYSIEIDLHSDDNFLFLDYSKSHINDEIKDALVALAEERGVRAFAKAMFDGQRVNSTENRAVLHVALRNRSNRPIIVDGKDVMSDVNNVLAQMKDFTERVRSGEWKGQTGKSIYNIVNIGIGGSDLGPVMVTEALKPFSKRDLHCFFVSNVDGTHMAEVLKQVNLEETIFIIASKTFTTQETLTNAMSARNALMSYLKENGISTDGAVAKHFVALSTNTEKVREFGIDTVNMFAFWDWVGGRYSVWSAIGLSVMLSIGYDNFVEFLTGAHVMDNHFASTPTEQNLPMMLALVGIWYNNFFGSETQAVLPYDQYLWRLPAYLQQLDMESNGKGVTKKSGAVAVQTGPIVFGEAGTNGQHAFYQLIHQGTKIIPCDFIGCVQTQNRVGDHHRTLMSNFFAQTEALMVGKNAEEVRQELVKSGMSGDAIENMIPHKTFTGSRPSNSILVNALTPRALGAIIAMYEHKVLVQGAIWGINSYDQWGVELGKVLAKSILPQLKSGNIVSDHDGSTNGLINMFNTRAHL","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"name":{"value":"PGI"}}],"alphafold_very_low_content":0,"disorder_content":0.07933884297520662,"disprot_consensus":{"full":[{"start":1,"end":48,"type":"D"}],"Structural state":[{"start":1,"end":48,"type":"D"}]}},{"disprot_id":"DP03801","acc":"O97193","creator":"vnugnes","date":"2022-09-21T15:36:46.257Z","features":{"pfam":[{"id":"PF00316","name":"Fructose-1-6-bisphosphatase, N-terminal domain","start":11,"end":204},{"id":"PF18913","name":"Fructose-1-6-bisphosphatase, C-terminal domain","start":208,"end":333}],"gene3D":[]},"length":351,"name":"Fructose-bisphosphatase","ncbi_taxon_id":5664,"organism":"Leishmania major","regions":[{"start":340,"end":351,"reference_id":"28882541","reference_source":"pmid","reference_html":"Structures of Leishmania Fructose-1,6-Bisphosphatase Reveal Species-Specific Differences in the Mechanism of Allosteric Inhibition. <i> Yuan M, Vásquez-Valdivieso MG, McNae IW, Michels PAM, Fothergill-Gilmore LA, Walkinshaw MD. </i> J Mol Biol, 2017","date":"2022-09-21T16:03:44.005Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"5OEZ"},{"db":"PDB","id":"5OFU"},{"db":"PDB","id":"5OEY"}],"region_id":"DP03801r001","statement":[{"text":"The terminal residues 1–7 and 336–350 as well as the C-terminal His-tag were not built into the structure models due to the lack of interpretable electron density","type":"Results"},{"text":"The PDB shows this region constitutes the IDR conserved by all chains obtained.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:44:30.613Z"}},{"start":52,"end":70,"reference_id":"28882541","reference_source":"pmid","reference_html":"Structures of Leishmania Fructose-1,6-Bisphosphatase Reveal Species-Specific Differences in the Mechanism of Allosteric Inhibition. <i> Yuan M, Vásquez-Valdivieso MG, McNae IW, Michels PAM, Fothergill-Gilmore LA, Walkinshaw MD. </i> J Mol Biol, 2017","date":"2022-09-21T15:46:31.220Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"5OEZ"}],"region_id":"DP03801r002","statement":[{"text":"The dynamic loop (residues 52–71) was found to adopt an engaged conformation (Fig. 4b), in contrast to the apoenzyme structure where the dynamic loop was found to be disordered in two of the chains.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:44:32.026Z"}},{"start":52,"end":61,"reference_id":"28882541","reference_source":"pmid","reference_html":"Structures of Leishmania Fructose-1,6-Bisphosphatase Reveal Species-Specific Differences in the Mechanism of Allosteric Inhibition. <i> Yuan M, Vásquez-Valdivieso MG, McNae IW, Michels PAM, Fothergill-Gilmore LA, Walkinshaw MD. </i> J Mol Biol, 2017","date":"2022-09-21T15:58:25.273Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"5OFU"}],"region_id":"DP03801r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16084","entry_name":"beta-D-fructofuranose 6-phosphate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16027","entry_name":"adenosine 5'-monophosphate"}],"statement":[{"text":"As a result of this rotation, the dynamic loop (residues 52–71) is pulled out from the active site in a canonical “disengaged conformation” [33], which is stabilized by the diagonal subunit.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:44:44.086Z"}},{"start":61,"end":70,"reference_id":"28882541","reference_source":"pmid","reference_html":"Structures of Leishmania Fructose-1,6-Bisphosphatase Reveal Species-Specific Differences in the Mechanism of Allosteric Inhibition. <i> Yuan M, Vásquez-Valdivieso MG, McNae IW, Michels PAM, Fothergill-Gilmore LA, Walkinshaw MD. </i> J Mol Biol, 2017","date":"2022-09-21T16:04:47.206Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"5OFU"}],"region_id":"DP03801r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16084","entry_name":"beta-D-fructofuranose 6-phosphate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16027","entry_name":"adenosine 5'-monophosphate"}],"statement":[{"text":"As a result of this rotation, the dynamic loop (residues 52–71) is pulled out from the active site in a canonical “disengaged conformation” [33], which is stabilized by the diagonal subunit.","type":"Results"},{"text":"The “disengaged-conformation” (in which most of the loop is disordered in the AMP-bound structure) is prevented from adopting an active conformation by the strong hydrogen bonded network around Arg48 which hydrogen bonds to the dynamic loop (residue 52) (Fig. 5d) and pointing the remainder of the loop out into solvent.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2022-12-15T17:44:38.477Z"}}],"regions_counter":4,"released":"2022_12","sequence":"MDVRRTPTPTTLTQYIIKSQPPHSRGDFTLLMMAIQTSVKVIEKNIRRAGMKGMLGYIAGQSANATGDHQAKLDVISNIAFKAYLLSSTSVCVLGSEEEEQMIIAESGRRGDYLIFFDPLDGSSNIDANVSVGSIWGVWRLPKDTTINSVEDANAVIRMLKGTDMVSAGYAVYGSATNLVLTSGHGVDGFTLDPNIGEFILTHPHISIPKKRSIYSVNEGNYGKWEPWFKEYIDYLKMNKTTRYSARYIGSMVGDIHRTLLYGGIFCYPKDANQVEGKLRLLYEAAPMAMIVEQAGGKAVGSNGRILEQSITRLHQRTPVYFGSRQEVDLCMAFRDRNVKTEALAPTSSKL","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"genes":[{"name":{"value":"FBP","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAC22660.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAC22660.1"}}]},"orfNames":[{"value":"LMJF_04_1160","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAC22660.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAC22660.1"}}]}]}],"alphafold_very_low_content":0.02849002849002849,"disorder_content":0.08831908831908832,"disprot_consensus":{"full":[{"start":52,"end":61,"type":"T"},{"start":62,"end":70,"type":"D"},{"start":340,"end":351,"type":"D"}],"Structural state":[{"start":52,"end":70,"type":"D"},{"start":340,"end":351,"type":"D"}],"Structural transition":[{"start":52,"end":61,"type":"T"}]}},{"disprot_id":"DP03802","acc":"A0A1L8HGL2","creator":"cpintado","date":"2022-09-22T08:23:12.325Z","features":{"pfam":[{"id":"PF00638","name":"RanBP1 domain","start":1183,"end":1303},{"id":"PF00638","name":"RanBP1 domain","start":1896,"end":2014},{"id":"PF00638","name":"RanBP1 domain","start":2185,"end":2305},{"id":"PF00638","name":"RanBP1 domain","start":2775,"end":2895},{"id":"PF00641","name":"Zn-finger in Ran binding protein and others","start":1411,"end":1435},{"id":"PF00641","name":"Zn-finger in Ran binding protein and others","start":1470,"end":1498},{"id":"PF00641","name":"Zn-finger in Ran binding protein and others","start":1530,"end":1558},{"id":"PF00641","name":"Zn-finger in Ran binding protein and others","start":1590,"end":1619},{"id":"PF00641","name":"Zn-finger in Ran binding protein and others","start":1657,"end":1686},{"id":"PF12185","name":"Nup358/RanBP2 E3 ligase domain","start":2493,"end":2555},{"id":"PF12185","name":"Nup358/RanBP2 E3 ligase domain","start":2578,"end":2633}],"gene3D":[]},"length":2905,"name":"ranBP2-like and GRIP domain-containing protein 3 isoform X2","ncbi_taxon_id":8355,"organism":"Xenopus laevis","regions":[{"start":738,"end":1171,"reference_id":"35679404","reference_source":"pmid","reference_html":"Structure of the cytoplasmic ring of the <i>Xenopus laevis</i> nuclear pore complex. <i> Zhu X, Huang G, Zeng C, Zhan X, Liang K, Xu Q, Zhao Y, Wang P, Wang Q, Zhou Q, Tao Q, Liu M, Lei J, Yan C, Shi Y. </i> Science, 2022","date":"2022-09-29T09:19:06.493Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7FIL"},{"db":"EMDB","id":"31602 "}],"region_id":"DP03802r001","statement":[{"text":"(B) Cryo-EM structure of Nup358-NTD2 at 3.0-Å resolution. Left: Resolution map of Nup358-NTD2. The local resolutions might be slightly inflated due to a variety of factors. Please refer to fig. S7C for representative densities. Right: Domain structure of Nup358. UR, unstructured region; FR, functional region. The terminal residues are labeled. Four surface motifs of Nup358-NTD2 (N-hook, loop-1, clip helices, loop-2), which mediate the cross-talk between Nup358-NTD2 and ACE1 proteins within the CR, are color coded.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-29T20:38:35.083Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MRRSKAEIQRYVENAQNSASSPREKSMKGFLFARLYYEAKEYELAKRSVSSYISVQERDPKAHRFLGQLFEIEGNVEKAVGCYKRSLELNPTQKDLTLRIAELICTLNIKDGRAEYWVERASKLFPGSPEIYRLKEQLLSSQGEAGWNQLFDLIQAELFARPNDVYVNLKLVDLFLSNQRLEEAVLHCLKPERRALRTDIEWCSCVVRVFKEYLASKQGQKNTNMRMITKELLLAQCDVVFLTLSKKDVQKSKEALERFDQALLSVKQSVSGTDASDLSVTFYEMRGHYYMHAGTLLLKMAQSCEVQWKALIEPAALCYLLAYQVPKPKSKPVKGDDNGQGFLEELAFDRQSKSGHLLLTLSHGKQNFISEIIETFANQCGQSILLKFLFEDNLSMQDSFMGSDDISYVENRVPDLSELSQHDNGSLRIHNGDLQHLTWLGLQWHFLSTLPPLRKWLKQIFPRVPQETSRLESNIPESICLLDLEVFLLAVVQTSYLQLQDNNTTADPNRPRCLPLPICKQLFTDRQRSWWDAVYSLITKKALPGTSAKLRSVIQHDLTTLRAQEKHGLQPAVLVNWARGLHKTGYSLNSFYDQKEYMGRCVHYWKKLLPLLDLVKQKKSIPEPVDPLFKHFHNKDIKVSEVKDLEDEACIAFATLDLVDGKTEDAIIAFESVKNVVAYWNLALIYQRKAEEIENDCLPAEEQEEFQECLLKCKGFLKMICDEYSAYPSIATSLPVPVETVFEMLDSVKQSLGEAMDDHSPAFMENHSVLTTSAIKHSTPSPTKLTISPSKSARFSPKTPPRWAEDQKSLLEVLCNKVEALKKEVQELKHNNSNANVSPHRWPNEGFESDTVADSYQGTQNFYTVPLTVSTSGPAAYYGQSPAYNSQHLLRPAANITPTKTSVYAMNRLPPQQHMYTYPQQMHTPPTQQSSAGCVFPQEIYGPPLRFESPAAAILSPHNEEFYNYNVPPASTNPPLPEPGYFTKPSTAMQHSKQEVPKVSDFGKGCLGQSTSEGQKPSPFTVPMQSTPASSTFKFNSNFKSNDGDFTFSSSHAGASSAYTGSESLLGLLTSDRPTQEQGKKSDFENIASDEKNMFRFGEKSFSPGFTVTGTQSQDKNPLVFGQSENIFTFKTPGKSTFKPPTFGTQTKDAHNHSVESDAGSEHVADDDGPHFEPIIPLPEKVEVKTGEEDEEEMFCNRAKLFRFDAETKEWKERGIGNVKILRHRLSGKIRLLMRREQVLKICANHYINADMKLKPNATSDKSYVWHAYDYADEMPKPEQLAIRFKTVDEAAHFKAKFEEAQRLLAMAEAPAISAQHKNAKDNLKLDASKVKEAPLPFGSQFILKRGEWQCDCCLATNAPTSTSCVCCQTPNKNKSSSISSVCISAPSFTFVKESATNKLAFGQQLLKDKDQWTCSKCSQKNDAGVSHCSSCQTQSQAKAGISQPNIASSGFTNNTSAQGDNLAAVFGKKAGQWDCDVCYVRNEPSANKCISCQNTKPLSKVSGTQAASFSFAAGADNSQKNFGAQFAKKEGQWDCDACYVRNEPLATKCISCQNTKLLSKTTGTQAASFSFAAAADNSQKNFGGQFAKKEGQWDCSSCLVRNEASAPNCVACHSANPQITNKDVVPPALTPSGFKFGHNAEVGKTQQSLSAMFSCKQGQWECSTCLVINDAAKDTCAACQAAKPGSSASQSKEVPSTFGIKANSSQNFGQPAAGFNCGFSAKGFKFGISDEKASASNFTFKAPATNEETKMVKDGFNFPVSAGSLSFKFGISEPDKTKEMSTGFMKGTSTNNKGSETAETTAQAEKIQQSPDKVLGQSVQSFSFADIAKSTEGIEFGKADPNFKGFSGAGQKLFTSSNQVNASNAQEAADDLYKTEERDDIHFEPIVQLPDKVDLITGEEDEKTLYSQRVKLYRFDATSGQWKERGVGNLKILKNEVNGKLRVLMRREQVLKVCANHWITTTMNLKPLTGSDRAWMWLANDFSEGDAKLEQLAVKFKTPEQAEEFKIKFDQCQCLLLDIPLQTPHKLVDTGRTAHLIQKAEEMKTGLKDLKTFLTDKAKPLDDSNAINTTDLEKQALADGTEPTYEWDTYDMRGDAHEETLDDSVYASPLASSPEKKNLFRFGDLSTSGFNFSFQPEPSPSKSPTKLNHSRVSVGTDEESDVTQEEERDGQYFEPVVPLPDLVEVTSGEENEQAIFCHRAKLYRFDKDSNQWKERGIGDLKILQRLDNKSARVVMRRDQVLKLCANHRITTDINLQPMKGAERAWVWTAHDFSEGEGKVECFAVRFKLQEAADLFKEVFEEAKEAQAKDCLLTPVSSRGTTPRAASCGKAAIAILEETTKERTDQQPEEDTSLTEASTPSPTDQPAKALVSPANFTFGSDVVKNIFGSEKQVPFAFGNTSSTGSLFGFSFNASQSQGQQVQKQPPKVTLDFNATFKDAETTNALQKPSQSSGQSPIVSSLSSSSSSSSSTLMQPMPARDKAADVPDADSSSDVLIVYVATPTPEQKALAETLLLPLTFFCYKNKPGYVSDESDIDDEDFETAVKNLNGILYTEDKKDKASSRLSGCSKEPTAESDQDCIIVWEKKPTPEEKAKADSLKLPPTFFCGLGSDTDEDKDNLEDFDTEVRKVKEAKGVPEADVTSSPEAAIVSAAETSVSLPPKQEPDSTTSISQEPVDLSSKQELPKTDSKGFSTPSFSFGLGEVSGVSFADLASTNSGDFAFGSKDTNFQWANTGAAVFGTLSQNKKGEDADGSDEEVVHSDDVHFEPIVSLPEVEVKSGEEDEEILFKERAKLYRWDRAVGQWKERGVGDIKILFHKEKGYYRVLMRRDQVLKVCANHVISTEIKISTLSTSNNSLVWTATDYSDGEGKVEQLAVRFKTKELTDSFQNKFEECQHNLQEESNPQH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Amphibia","Batrachia","Anura","Pipoidea","Pipidae","Xenopodinae","Xenopus","Xenopus"],"genes":[{"name":{"value":"ranbp2.L","evidences":[{"code":"ECO:0000313","source":{"name":"RefSeq","id":"XP_018102541.1","url":"https://www.ncbi.nlm.nih.gov/protein/XP_018102541.1"}},{"code":"ECO:0000313","source":{"name":"Xenbase","id":"XB-GENE-6252429","url":"https://www.xenbase.org/gene/showgene.do?method=display&geneId=XB-GENE-6252429"}}]}}],"disorder_content":0.1493975903614458,"disprot_consensus":{"full":[{"start":738,"end":1171,"type":"D"}],"Structural state":[{"start":738,"end":1171,"type":"D"}]}},{"disprot_id":"DP03803","acc":"Q24459","creator":"cpintado","date":"2022-09-22T14:37:43.025Z","features":{"pfam":[{"id":"PF14061","name":"Polycomb-like MTF2 factor 2","start":985,"end":1033},{"id":"PF30898","name":"Polycomb-like middle domain","start":578,"end":659}],"gene3D":[]},"length":1043,"name":"Polycomb protein Pcl","ncbi_taxon_id":7227,"organism":"Drosophila melanogaster","regions":[{"start":339,"end":354,"reference_id":"20669242","reference_source":"pmid","reference_html":"Structure of an atypical Tudor domain in the Drosophila Polycomblike protein. <i> Friberg A, Oddone A, Klymenko T, Müller J, Sattler M. </i> Protein Sci, 2010","date":"2022-09-29T09:18:30.237Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2XK0"},{"db":"BMRB","id":"17050"}],"region_id":"DP03803r001","statement":[{"text":"C: {1H-}-15N heteronuclear NOE indicates flexible N- and C-termini of Pcl-Tudor. ","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-29T20:38:27.889Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MMNNHFHLQHDHPPQNVAHPFMQQPSTAVPSAPPATYGYLAQPAGQQPQWMTTTYQILPPSVGPATVAKRYYATTGPQTTHPTHPSTIQITNSFAQQSTPPKQQAATSCSPFKANNIRIISTAPSVYSLNKPPQEAHSTYAPVQSYYLPSGGGQTAGQINLLAASGTGKQLQPPPLVPVTNSTSPPSTVVLDRINICINNHYTETPTSLSSSLTTAQQPSPIIPAIQHKAILPLIDSSTADSSSCSSSSVSSSSYSGTATTSAAVVIVDEPDSTTTTPQTPPTTPEAMSSPGKSSPSPPLLATQSLLKGVNSMKPSFKTVEAAPPTPPTPPSPPPPPPAPPVAAPSPAVTYALQEDVFIKCNDGRFYLGTIIDQTSDQYLIRFDDQSEQWCEPDKLRKLGGGSSITAGGGGASTTESTNTSPSGPMCVACKRSDIEDVVEICERCGRGYHRGCTVEIVTGSGIWSCKRCAKPMKMQQPVSHKITKPAGICRQLPYHADKLSWDEKHRVNEEQIYCYCGKPGKFDHNMLQCCKCRNWFHTQCMQNFKKKLLRGDMFFVFCCTVCNNGIEFVRRMQIEWVDVLHIALYNLRKHQHQKYHHLLNDIWPFILEQRHQLPICEKWRTLPETALMERLKQTLKDYSDRFVCGREFKRAPAFYALRHSGPPHIPKVFLEPHEELSDELLEKRFKLMLMPEEPDEGANELPKRVPKDVYEFNTDEDDPVETSEDEIPIKQIIEKAKKQAAQKADKHDELPLKPDLADDNANDGDPGKLPAPIPPLLDANSSRKRKAFRLSKRYDNSRNHCDLSSDENSSSSRGTSSLDLIIPPPVNFLGRNNPFLMATPKKASQGRSISVGTGVGVNGIINSIFKLKGTSKEQPRMVRTIKRRLSAKDITIGPNQEVRRRRTRRLTTAIEVISTTTINPIPSHYLPIYAKDLQPPAPPMGKPTHGRLLRQRPQKQSPSQSRRNSTSSTATSSSSNGIGAPGHSMLDLKQSVNKYFGGAMNRIDAGEPFAIRAKRRMGNGQVQYLVEWGGDTATTAIGLLGN","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"genes":[{"name":{"value":"Pcl"},"orfNames":[{"value":"CG5109"}]}],"alphafold_very_low_content":0.5848513902205177,"disorder_content":0.015340364333652923,"disprot_consensus":{"full":[{"start":339,"end":354,"type":"D"}],"Structural state":[{"start":339,"end":354,"type":"D"}]}},{"disprot_id":"DP03804","acc":"Q9VVI2","creator":"cpintado","date":"2022-09-22T14:48:10.225Z","features":{"pfam":[{"id":"PF09532","name":"FDF domain","start":342,"end":390},{"id":"PF12701","name":"Scd6-like Sm domain","start":7,"end":69}],"gene3D":[]},"length":680,"name":"Enhancer of mRNA-decapping protein 3","ncbi_taxon_id":7227,"organism":"Drosophila melanogaster","regions":[{"start":71,"end":101,"reference_id":"17923697","reference_source":"pmid","reference_html":"A divergent Sm fold in EDC3 proteins mediates DCP1 binding and P-body targeting. <i> Tritschler F, Eulalio A, Truffault V, Hartmann MD, Helms S, Schmidt S, Coles M, Izaurralde E, Weichenrieder O. </i> Mol Cell Biol, 2007","date":"2022-09-29T09:19:38.709Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2RM4"},{"db":"BMRB","id":"11009"}],"region_id":"DP03804r001","statement":[{"text":"The remaining C-terminal extension (30 residues) is unstructured.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-29T20:38:22.755Z"}},{"start":71,"end":101,"reference_id":"17923697","reference_source":"pmid","reference_html":"A divergent Sm fold in EDC3 proteins mediates DCP1 binding and P-body targeting. <i> Tritschler F, Eulalio A, Truffault V, Hartmann MD, Helms S, Schmidt S, Coles M, Izaurralde E, Weichenrieder O. </i> Mol Cell Biol, 2007","date":"2022-09-29T09:42:52.292Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"BMRB","id":"11009"},{"db":"PDB","id":"2RM4"}],"region_id":"DP03804r002","statement":[{"text":"The two structures confirm and confine the EDC3 LSm domain as an independent folding unit and suggest that residues beyond HsP68 and DmA71 are part of the unstructured region of EDC3 which links the LSm domain to the predicted FDF domain.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-09-29T20:38:22.177Z"}},{"start":101,"end":338,"reference_id":"17923697","reference_source":"pmid","reference_html":"A divergent Sm fold in EDC3 proteins mediates DCP1 binding and P-body targeting. <i> Tritschler F, Eulalio A, Truffault V, Hartmann MD, Helms S, Schmidt S, Coles M, Izaurralde E, Weichenrieder O. </i> Mol Cell Biol, 2007","date":"2023-08-17T14:11:23.801Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006216","ec_ontology":"ECO","ec_name":"author inference used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03804r003","statement":[{"text":"Members of the EDC3 protein family have a modular domain organization made up of an N-terminal LSm domain, a central FDF domain and a C-terminal YjeF-N domain (Fig.1A). The LSm and FDF domains are connected by a sequence rich in glutamine, asparagine, glycine, and arginine residues, which is likely to be unstructured (Fig.1A, linker) (1, 2).","type":"Results"},{"text":"(A) Domain architecture of EDC3. EDC3 orthologs contain three classified globular domains: an LSm domain, an FDF domain, and a YjeF-N-type Rossman fold domain. The LSm and FDF domains are connected by a low-complexity linker region. ","type":"Figure"},{"text":"The two structures confirm and confine the EDC3 LSm domain as an independent folding unit and suggest that residues beyond HsP68 and DmA71 are part of the unstructured region of EDC3 which links the LSm domain to the predicted FDF domain.","type":"Results"}]},{"start":101,"end":338,"reference_id":"17923697","reference_source":"pmid","reference_html":"A divergent Sm fold in EDC3 proteins mediates DCP1 binding and P-body targeting. <i> Tritschler F, Eulalio A, Truffault V, Hartmann MD, Helms S, Schmidt S, Coles M, Izaurralde E, Weichenrieder O. </i> Mol Cell Biol, 2007","date":"2022-11-17T15:19:37.337Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006216","ec_ontology":"ECO","ec_name":"author inference used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03804r004","statement":[{"text":"Members of the EDC3 protein family have a modular domain organization made up of an N-terminal LSm domain, a central FDF domain and a C-terminal YjeF-N domain (Fig. ​(Fig.1A).1A). The LSm and FDF domains are connected by a sequence rich in glutamine, asparagine, glycine, and arginine residues, which is likely to be unstructured (Fig. ​(Fig.1A,1A, linker) (1, 2).","type":"Results"},{"text":"(A) Domain architecture of EDC3. EDC3 orthologs contain three classified globular domains: an LSm domain, an FDF domain, and a YjeF-N-type Rossman fold domain. The LSm and FDF domains are connected by a low-complexity linker region. ","type":"Figure"},{"text":"The two structures confirm and confine the EDC3 LSm domain as an independent folding unit and suggest that residues beyond HsP68 and DmA71 are part of the unstructured region of EDC3 which links the LSm domain to the predicted FDF domain.","type":"Results"}]}],"regions_counter":4,"released":"2024_06","sequence":"MGPTDQDWIGCAVSIACDEVLGVFQGLIKQISAEEITIVRAFRNGVPLRKQNAEVVLKCTDIRSIDLIEPAKQDLDGHTAPPPVVNKPTPVKLPHFSNILGKQQQLQLQQQQQQLQLQQQQKQQFQEQEREQDLPSTPRSRANDNGRVAAGGASSSSGPRGNFNSALSDKMHQLKLIETNGSNGTLRTPQTSRASSAQQQPQISTTPNSVAAFFGNMIPPKVEVKLGSYVSNTRESYCSSSGDSGEATGLSLGSSKPIDIVSNGDGFYKQTAASSYGNTNGNVRRNGNANNNGNGTGNGSYTNGNGNGNGKNKRNRVRRESSMRQQQVQLTFGSEADDPLIHEDFDFEGNLALFDKQAIWDDIESTTQKPDVVRHIVNNHHHKPEQKYRHDENILASKPLQLRQIESMFGGSQDFVTDDGLIIPTIPAYVRNKIEISADKAGLSLQRQIDILARGASDLAITLLGGARRLTPANNHQWPKIAIICDGGKNMRTINIGAATGRQLASHGLTVLLYVEQAKLLEQNSSSPEISLFKATDNVIVHSVDALPTPDLVILSTNTANLSDAIRKWLSVNRASVLAIDPPPCGINEVAIKYSILPILPLNGISTATTSSSSSAAATPTPIASTSAAASATKSAASTNNCGKLYLCNLGIPDKFYRDCGIKYKSPYGHKYVIPIHSKD","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"genes":[{"name":{"value":"Edc3"},"orfNames":[{"value":"CG6311"}]}],"alphafold_very_low_content":0.36176470588235293,"disorder_content":0.3941176470588235,"disprot_consensus":{"full":[{"start":71,"end":338,"type":"D"}],"Structural state":[{"start":71,"end":338,"type":"D"}],"Disorder function":[{"start":71,"end":338,"type":"F"}]}},{"disprot_id":"DP03805","acc":"Q15858","creator":"maspromonte","date":"2022-09-28T12:33:01.574Z","features":{"pfam":[{"id":"PF00520","name":"Ion transport protein","start":125,"end":410},{"id":"PF00520","name":"Ion transport protein","start":744,"end":975},{"id":"PF00520","name":"Ion transport protein","start":1191,"end":1466},{"id":"PF00520","name":"Ion transport protein","start":1515,"end":1770},{"id":"PF06512","name":"Sodium ion transport-associated","start":982,"end":1187},{"id":"PF11933","name":"Cytoplasmic domain of voltage-gated Na+ ion channel","start":535,"end":694},{"id":"PF24609","name":"SCN5A-like, C-terminal IQ motif","start":1882,"end":1913}],"gene3D":[]},"genes":[{"name":{"value":"SCN9A","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:10597","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:10597"}}]},"synonyms":[{"value":"NENA"}]}],"length":1988,"name":"Sodium channel protein type 9 subunit alpha","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":417,"end":725,"reference_id":"30765606","reference_source":"pmid","reference_html":"Structures of human Na<sub>v</sub>1.7 channel in complex with auxiliary subunits and animal toxins. <i> Shen H, Liu D, Wu K, Lei J, Yan N. </i> Science, 2019","date":"2022-10-04T15:14:28.465Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6J8H"},{"db":"PDB","id":"6J8I"},{"db":"PDB","id":"6J8J"},{"db":"PDB","id":"6J8G"}],"region_id":"DP03805r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60939","statements":[{"type":"Introduction","text":"In this study, we report the structures of\nhuman Nav1.7 in the presence of both β1 and β2 subunits at resolutions of 3.2 Å determined using single-particle cryo-EM."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":" Q07699","statements":[{"type":"Introduction","text":"In this study, we report the structures of\nhuman Nav1.7 in the presence of both β1 and β2 subunits at resolutions of 3.2 Å determined using single-particle cryo-EM."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139","statements":[{"type":"Introduction","text":"Two combinations of toxins were supplemented, ProTx-II with TTX\nand HWTX-IV with STX. "}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"34970","statements":[{"type":"Introduction","text":"Two combinations of toxins were supplemented, ProTx-II with TTX\nand HWTX-IV with STX. "}],"entry_name":"saxitoxin"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"9506 ","entry_name":"tetrodotoxin"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:90488904"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:223365906"}],"statement":[{"text":"For both structures, side chains could be assigned for residues 114 to 1768 except for the intracellular linkers I-II (residues 418 to 725) and II-III (residues 973 to 1174).","type":"Results"},{"text":"In total, 1140 residues for Nav 1.7, 173 residues for β1, and 120 residues for β2 were assigned with side chains, and 10 sugar moieties were built. The N-terminal 113 residues, intracellular I-II linker (residues 418-725), II-III linker (residues 973-1174), and C-terminal sequences after Glu1768 are invisible in Na v1.7.","type":"Supplementary material"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu406Lys","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Whole-cell electrophysiolog-ical characterization of Nav1.7 in the presenceofb1andb2 subunits shows that Nav1.7 (E406K)exhibits a hyperpolarizing shift in activation(−10.6 mV) and prolonged fast-inactivation du-ration compared with the wild type (Fig. 1A, fig.S2, and table S2)."},{"type":"Supplementary material","text":"The brown square indicates Glu406 that was mutated to Lys in this study."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-04T18:36:48.893Z"}},{"start":973,"end":1174,"reference_id":"30765606","reference_source":"pmid","reference_html":"Structures of human Na<sub>v</sub>1.7 channel in complex with auxiliary subunits and animal toxins. <i> Shen H, Liu D, Wu K, Lei J, Yan N. </i> Science, 2019","date":"2022-10-04T15:15:18.903Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6J8H"},{"db":"PDB","id":"6J8I"},{"db":"PDB","id":"6J8J"},{"db":"PDB","id":"6J8G"}],"region_id":"DP03805r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60939","statements":[{"type":"Introduction","text":"In this study, we report the structures of human Nav1.7 in the presence of both β1 and β2 subunits at resolutions of 3.2 Å determined using single-particle cryo-EM."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q07699","statements":[{"type":"Introduction","text":"In this study, we report the structures of human Nav1.7 in the presence of both β1 and β2 subunits at resolutions of 3.2 Å determined using single-particle cryo-EM."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139","statements":[{"type":"Introduction","text":"Two combinations of toxins were supplemented, ProTx-II with TTX and HWTX-IV with STX."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"34970","statements":[{"type":"Introduction","text":"Two combinations of toxins were supplemented, ProTx-II with TTX and HWTX-IV with STX."}],"entry_name":"saxitoxin"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"9506 ","entry_name":"tetrodotoxin"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:90488904"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:223365906"}],"statement":[{"text":"For both structures, side chains could be assigned for residues 114 to 1768 except for the intracellular linkers I-II (residues 418 to 725) and II-III (residues 973 to 1174).","type":"Results"},{"text":"In total, 1140 residues for Nav 1.7, 173 residues for β1, and 120 residues for β2 were assigned with side chains, and 10 sugar moieties were built. The N-terminal 113 residues, intracellular I-II linker (residues 418-725), II-III linker (residues 973-1174), and C-terminal sequences after Glu1768 are invisible in Na v1.7.","type":"Supplementary material"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly406Lys","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Whole-cell electrophysiolog-ical characterization of Nav1.7 in the presenceofb1andb2 subunits shows that Nav1.7 (E406K)exhibits a hyperpolarizing shift in activation(−10.6 mV) and prolonged fast-inactivation du-ration compared with the wild type (Fig. 1A, fig.S2, and table S2)."},{"type":"Supplementary material","text":"The brown square indicates Glu406 that was mutated to Lys in this study."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-04T18:36:24.530Z"}},{"start":973,"end":1174,"reference_id":"30765606","reference_source":"pmid","reference_html":"Structures of human Na<sub>v</sub>1.7 channel in complex with auxiliary subunits and animal toxins. <i> Shen H, Liu D, Wu K, Lei J, Yan N. </i> Science, 2019","date":"2022-10-04T15:16:02.649Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6J8H"},{"db":"PDB","id":"6J8I"},{"db":"PDB","id":"6J8J"},{"db":"PDB","id":"6J8G"}],"region_id":"DP03805r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60939","statements":[{"type":"Introduction","text":"In this study, we report the structures of human Nav1.7 in the presence of both β1 and β2 subunits at resolutions of 3.2 Å determined using single-particle cryo-EM."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q07699","statements":[{"type":"Introduction","text":"In this study, we report the structures of human Nav1.7 in the presence of both β1 and β2 subunits at resolutions of 3.2 Å determined using single-particle cryo-EM."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139","statements":[{"type":"Introduction","text":"Two combinations of toxins were supplemented, ProTx-II with TTX and HWTX-IV with STX."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"34970","statements":[{"type":"Introduction","text":"Two combinations of toxins were supplemented, ProTx-II with TTX and HWTX-IV with STX."}],"entry_name":"saxitoxin"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"9506 ","entry_name":"tetrodotoxin"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:90488904"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:223365906"}],"statement":[{"text":"For both structures, side chains could be assigned for residues 114 to 1768 except for the intracellular linkers I-II (residues 418 to 725) and II-III (residues 973 to 1174).","type":"Results"},{"text":"In total, 1140 residues for Nav 1.7, 173 residues for β1, and 120 residues for β2 were assigned with side chains, and 10 sugar moieties were built. The N-terminal 113 residues, intracellular I-II linker (residues 418-725), II-III linker (residues 973-1174), and C-terminal sequences after Glu1768 are invisible in Na v1.7.","type":"Supplementary material"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu406Lys","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Whole-cell electrophysiolog-ical characterization of Nav1.7 in the presenceofb1andb2 subunits shows that Nav1.7 (E406K)exhibits a hyperpolarizing shift in activation(−10.6 mV) and prolonged fast-inactivation du-ration compared with the wild type (Fig. 1A, fig.S2, and table S2)."},{"type":"Supplementary material","text":"The brown square indicates Glu406 that was mutated to Lys in this study"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-04T18:36:44.588Z"}},{"start":417,"end":725,"reference_id":"30765606","reference_source":"pmid","reference_html":"Structures of human Na<sub>v</sub>1.7 channel in complex with auxiliary subunits and animal toxins. <i> Shen H, Liu D, Wu K, Lei J, Yan N. </i> Science, 2019","date":"2022-10-04T15:17:02.499Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6J8H"},{"db":"PDB","id":"6J8I"},{"db":"PDB","id":"6J8J"},{"db":"PDB","id":"6J8G"}],"region_id":"DP03805r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60939","statements":[{"type":"Introduction","text":"In this study, we report the structures of human Nav1.7 in the presence of both β1 and β2 subunits at resolutions of 3.2 Å determined using single-particle cryo-EM."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q07699","statements":[{"type":"Introduction","text":"In this study, we report the structures of human Nav1.7 in the presence of both β1 and β2 subunits at resolutions of 3.2 Å determined using single-particle cryo-EM."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139","statements":[{"type":"Introduction","text":"Two combinations of toxins were supplemented, ProTx-II with TTX and HWTX-IV with STX."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"34970","statements":[{"type":"Introduction","text":"Two combinations of toxins were supplemented, ProTx-II with TTX and HWTX-IV with STX."}],"entry_name":"saxitoxin"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"9506 ","entry_name":"tetrodotoxin"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:90488904"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:223365906"}],"statement":[{"text":"For both structures, side chains could be assigned for residues 114 to 1768 except for the intracellular linkers I-II (residues 418 to 725) and II-III (residues 973 to 1174).","type":"Results"},{"text":"In total, 1140 residues for Nav 1.7, 173 residues for β1, and 120 residues for β2 were assigned with side chains, and 10 sugar moieties were built. The N-terminal 113 residues, intracellular I-II linker (residues 418-725), II-III linker (residues 973-1174), and C-terminal sequences after Glu1768 are invisible in Na v1.7.","type":"Supplementary material"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu406Lys","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Whole-cell electrophysiolog-ical characterization of Nav1.7 in the presenceofb1andb2 subunits shows that Nav1.7 (E406K)exhibits a hyperpolarizing shift in activation(−10.6 mV) and prolonged fast-inactivation du-ration compared with the wild type (Fig. 1A, fig.S2, and table S2)"},{"type":"Supplementary material","text":"The brown square indicates Glu406 that was mutated to Lys in this study"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-04T18:36:45.768Z"}},{"start":1,"end":113,"reference_id":"30765606","reference_source":"pmid","reference_html":"Structures of human Na<sub>v</sub>1.7 channel in complex with auxiliary subunits and animal toxins. <i> Shen H, Liu D, Wu K, Lei J, Yan N. </i> Science, 2019","date":"2022-10-04T15:28:32.565Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6J8H"},{"db":"PDB","id":"6J8I"},{"db":"PDB","id":"6J8J"},{"db":"PDB","id":"6J8G"}],"region_id":"DP03805r005","statement":[{"text":"In total, 1140 residues for Nav 1.7, 173 residues for β1, and 120 residues for β2 were assigned with side chains, and 10 sugar moieties were built. The N-terminal 113 residues, intracellular I-II linker (residues 418-725), II-III linker (residues 973-1174), and C-terminal sequences after Glu1768 are invisible in Na v1.7.","type":"Supplementary material"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu406Lys","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60939","statements":[{"type":"Introduction","text":"In this study, we report the structures of human Nav1.7 in the presence of both β1 and β2 subunits at resolutions of 3.2 Å determined using single-particle cryo-EM."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q07699","statements":[{"type":"Introduction","text":"In this study, we report the structures of human Nav1.7 in the presence of both β1 and β2 subunits at resolutions of 3.2 Å determined using single-particle cryo-EM."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139","statements":[{"type":"Introduction","text":"Two combinations of toxins were supplemented, ProTx-II with TTX and HWTX-IV with STX."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"34970","statements":[{"type":"Introduction","text":"Two combinations of toxins were supplemented, ProTx-II with TTX and HWTX-IV with STX"}],"entry_name":"saxitoxin"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"9506","entry_name":"tetrodotoxin"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:90488904"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:223365906"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-04T18:36:09.406Z"}},{"start":1769,"end":1988,"reference_id":"30765606","reference_source":"pmid","reference_html":"Structures of human Na<sub>v</sub>1.7 channel in complex with auxiliary subunits and animal toxins. <i> Shen H, Liu D, Wu K, Lei J, Yan N. </i> Science, 2019","date":"2022-10-04T15:37:58.218Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu406Lys","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Whole-cell electrophysiolog-ical characterization of Nav1.7 in the presenceofb1andb2 subunits shows that Nav1.7 (E406K)exhibits a hyperpolarizing shift in activation(−10.6 mV) and prolonged fast-inactivation du-ration compared with the wild type (Fig. 1A, fig.S2, and table S2)"},{"type":"Supplementary material","text":"The brown square indicates Glu406 that was mutated to Lys in this study"}]}],"cross_refs":[{"db":"PDB","id":"6J8H"},{"db":"PDB","id":"6J8I"},{"db":"PDB","id":"6J8J"},{"db":"PDB","id":"6J8G"}],"region_id":"DP03805r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60939","statements":[{"type":"Introduction","text":"In this study, we report the structures of human Nav1.7 in the presence of both β1 and β2 subunits at resolutions of 3.2 Å determined using single-particle cryo-EM."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q07699","statements":[{"type":"Introduction","text":"In this study, we report the structures of human Nav1.7 in the presence of both β1 and β2 subunits at resolutions of 3.2 Å determined using single-particle cryo-EM."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139","statements":[{"type":"Introduction","text":"Two combinations of toxins were supplemented, ProTx-II with TTX and HWTX-IV with STX."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"34970","statements":[{"type":"Introduction","text":"Two combinations of toxins were supplemented, ProTx-II with TTX and HWTX-IV with STX."}],"entry_name":"saxitoxin"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"9506","entry_name":"tetrodotoxin"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:90488904"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:223365906"}],"statement":[{"text":"In total, 1140 residues for Nav 1.7, 173 residues for β1, and 120 residues for β2 were assigned with side chains, and 10 sugar moieties were built. The N-terminal 113 residues, intracellular I-II linker (residues 418-725), II-III linker (residues 973-1174), and C-terminal sequences after Glu1768 are invisible in Na v1.7.","type":"Supplementary material"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-04T18:36:16.064Z"}}],"regions_counter":6,"released":"2023_06","sequence":"MAMLPPPGPQSFVHFTKQSLALIEQRIAERKSKEPKEEKKDDDEEAPKPSSDLEAGKQLPFIYGDIPPGMVSEPLEDLDPYYADKKTFIVLNKGKTIFRFNATPALYMLSPFSPLRRISIKILVHSLFSMLIMCTILTNCIFMTMNNPPDWTKNVEYTFTGIYTFESLVKILARGFCVGEFTFLRDPWNWLDFVVIVFAYLTEFVNLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLKHKCFRNSLENNETLESIMNTLESEEDFRKYFYYLEGSKDALLCGFSTDSGQCPEGYTCVKIGRNPDYGYTSFDTFSWAFLALFRLMTQDYWENLYQQTLRAAGKTYMIFFVVVIFLGSFYLINLILAVVAMAYEEQNQANIEEAKQKELEFQQMLDRLKKEQEEAEAIAAAAAEYTSIRRSRIMGLSESSSETSKLSSKSAKERRNRRKKKNQKKLSSGEEKGDAEKLSKSESEDSIRRKSFHLGVEGHRRAHEKRLSTPNQSPLSIRGSLFSARRSSRTSLFSFKGRGRDIGSETEFADDEHSIFGDNESRRGSLFVPHRPQERRSSNISQASRSPPMLPVNGKMHSAVDCNGVVSLVDGRSALMLPNGQLLPEVIIDKATSDDSGTTNQIHKKRRCSSYLLSEDMLNDPNLRQRAMSRASILTNTVEELEESRQKCPPWWYRFAHKFLIWNCSPYWIKFKKCIYFIVMDPFVDLAITICIVLNTLFMAMEHHPMTEEFKNVLAIGNLVFTGIFAAEMVLKLIAMDPYEYFQVGWNIFDSLIVTLSLVELFLADVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKINDDCTLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQAMCLIVYMMVMVIGNLVVLNLFLALLLSSFSSDNLTAIEEDPDANNLQIAVTRIKKGINYVKQTLREFILKAFSKKPKISREIRQAEDLNTKKENYISNHTLAEMSKGHNFLKEKDKISGFGSSVDKHLMEDSDGQSFIHNPSLTVTVPIAPGESDLENMNAEELSSDSDSEYSKVRLNRSSSSECSTVDNPLPGEGEEAEAEPMNSDEPEACFTDGCVWRFSCCQVNIESGKGKIWWNIRKTCYKIVEHSWFESFIVLMILLSSGALAFEDIYIERKKTIKIILEYADKIFTYIFILEMLLKWIAYGYKTYFTNAWCWLDFLIVDVSLVTLVANTLGYSDLGPIKSLRTLRALRPLRALSRFEGMRVVVNALIGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYECINTTDGSRFPASQVPNRSECFALMNVSQNVRWKNLKVNFDNVGLGYLSLLQVATFKGWTIIMYAAVDSVNVDKQPKYEYSLYMYIYFVVFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPGNKIQGCIFDLVTNQAFDISIMVLICLNMVTMMVEKEGQSQHMTEVLYWINVVFIILFTGECVLKLISLRHYYFTVGWNIFDFVVVIISIVGMFLADLIETYFVSPTLFRVIRLARIGRILRLVKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKKEDGINDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSKPPDCDPKKVHPGSSVEGDCGNPSVGIFYFVSYIIISFLVVVNMYIAVILENFSVATEESTEPLSEDDFEMFYEVWEKFDPDATQFIEFSKLSDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDSLRSQMEERFMSANPSKVSYEPITTTLKRKQEDVSATVIQRAYRRYRLRQNVKNISSIYIKDGDRDDDLLNKKDMAFDNVNENSSPEKTDATSSTTSPPSYDSVTKPDKEKYEQDRTEKEDKGKDSKESKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.2515090543259557,"disorder_content":0.4245472837022133,"disprot_consensus":{"full":[{"start":1,"end":113,"type":"D"},{"start":417,"end":725,"type":"D"},{"start":973,"end":1174,"type":"D"},{"start":1769,"end":1988,"type":"D"}],"Structural state":[{"start":1,"end":113,"type":"D"},{"start":417,"end":725,"type":"D"},{"start":973,"end":1174,"type":"D"},{"start":1769,"end":1988,"type":"D"}],"Disorder function":[{"start":417,"end":725,"type":"F"},{"start":973,"end":1174,"type":"F"}]}},{"disprot_id":"DP03806","acc":"Q3U8S1","creator":"vnugnes","date":"2022-09-28T16:22:42.541Z","features":{"pfam":[{"id":"PF00193","name":"Extracellular link domain","start":36,"end":124}],"gene3D":[]},"genes":[{"name":{"value":"Cd44","evidences":[{"code":"ECO:0000313","source":{"name":"Ensembl","id":"ENSMUSP00000097265","url":"https://www.ensembl.org/id/ENSMUSP00000097265"}},{"code":"ECO:0000313","source":{"name":"MGI","id":"MGI:88338","url":"http://www.informatics.jax.org/marker/MGI:88338"}}]}}],"length":365,"name":"CD44 antigen","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":293,"end":365,"reference_id":"25572402","reference_source":"pmid","reference_html":"Phosphatidylinositol 4,5-bisphosphate clusters the cell adhesion molecule CD44 and assembles a specific CD44-Ezrin heterocomplex, as revealed by small angle neutron scattering. <i> Chen X, Khajeh JA, Ju JH, Gupta YK, Stanley CB, Do C, Heller WT, Aggarwal AK, Callaway DJ, Bu Z. </i> J Biol Chem, 2015","date":"2022-09-28T16:31:09.756Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The entire cytoplasmic domain including amino acid residues 293–365 of mouse CD44 transcript variant 3 (CD44ct) was subcloned into a pET-32a vector that expresses a fusion protein of a His6 plus thioredoxin tag at the N-terminal end of CD44ct."}]},{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The entire cytoplasmic domain including amino acid residues 293–365 of mouse CD44 transcript variant 3 (CD44ct) was subcloned into a pET-32a vector that expresses a fusion protein of a His6 plus thioredoxin tag at the N-terminal end of CD44ct."}]}],"region_id":"DP03806r001","statement":[{"text":"CD spectroscopy shows that CD44ct is largely disordered without apparent secondary structure features (Fig. 1D). ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-16T13:23:35.707Z"}},{"start":293,"end":365,"reference_id":"25572402","reference_source":"pmid","reference_html":"Phosphatidylinositol 4,5-bisphosphate clusters the cell adhesion molecule CD44 and assembles a specific CD44-Ezrin heterocomplex, as revealed by small angle neutron scattering. <i> Chen X, Khajeh JA, Ju JH, Gupta YK, Stanley CB, Do C, Heller WT, Aggarwal AK, Callaway DJ, Bu Z. </i> J Biol Chem, 2015","date":"2022-09-28T16:32:36.864Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006214","ec_ontology":"ECO","ec_name":"small-angle neutron scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The entire cytoplasmic domain including amino acid residues 293–365 of mouse CD44 transcript variant 3 (CD44ct) was subcloned into a pET-32a vector that expresses a fusion protein of a His6 plus thioredoxin tag at the N-terminal end of CD44ct."}]},{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The entire cytoplasmic domain including amino acid residues 293–365 of mouse CD44 transcript variant 3 (CD44ct) was subcloned into a pET-32a vector that expresses a fusion protein of a His6 plus thioredoxin tag at the N-terminal end of CD44ct."}]}],"region_id":"DP03806r002","statement":[{"text":"The disorder in CD44ct is also exhibited in the SANS data. The relatively large Rg and Dmax of the 72-residue dCD44ct as compared with a well folded theoredoxin of 109 residues indicate that dCD44ct is not a compact globular structure (Fig. 1G and Table 1).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-16T13:23:37.695Z"}},{"start":293,"end":365,"reference_id":"25572402","reference_source":"pmid","reference_html":"Phosphatidylinositol 4,5-bisphosphate clusters the cell adhesion molecule CD44 and assembles a specific CD44-Ezrin heterocomplex, as revealed by small angle neutron scattering. <i> Chen X, Khajeh JA, Ju JH, Gupta YK, Stanley CB, Do C, Heller WT, Aggarwal AK, Callaway DJ, Bu Z. </i> J Biol Chem, 2015","date":"2022-09-28T18:39:09.381Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The entire cytoplasmic domain including amino acid residues 293–365 of mouse CD44 transcript variant 3 (CD44ct) was subcloned into a pET-32a vector that expresses a fusion protein of a His6 plus thioredoxin tag at the N-terminal end of CD44ct."}]},{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The entire cytoplasmic domain including amino acid residues 293–365 of mouse CD44 transcript variant 3 (CD44ct) was subcloned into a pET-32a vector that expresses a fusion protein of a His6 plus thioredoxin tag at the N-terminal end of CD44ct."}]}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P26040","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03806r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18348","entry_name":"1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate"}],"statement":[{"text":"The gel filtration results show that CD44ct does not interact with Ezrin(T567D) in solution but forms a complex with Ezrin(T567D) only in the presence of PIP2 (Fig. 3A).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-16T13:23:45.299Z"}},{"start":293,"end":365,"reference_id":"25572402","reference_source":"pmid","reference_html":"Phosphatidylinositol 4,5-bisphosphate clusters the cell adhesion molecule CD44 and assembles a specific CD44-Ezrin heterocomplex, as revealed by small angle neutron scattering. <i> Chen X, Khajeh JA, Ju JH, Gupta YK, Stanley CB, Do C, Heller WT, Aggarwal AK, Callaway DJ, Bu Z. </i> J Biol Chem, 2015","date":"2022-09-28T18:40:24.948Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The entire cytoplasmic domain including amino acid residues 293–365 of mouse CD44 transcript variant 3 (CD44ct) was subcloned into a pET-32a vector that expresses a fusion protein of a His6 plus thioredoxin tag at the N-terminal end of CD44ct."}]},{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The entire cytoplasmic domain including amino acid residues 293–365 of mouse CD44 transcript variant 3 (CD44ct) was subcloned into a pET-32a vector that expresses a fusion protein of a His6 plus thioredoxin tag at the N-terminal end of CD44ct."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P26040","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03806r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18348","entry_name":"1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate"}],"statement":[{"text":"Instead, only in the presence of PIP2, do CD44ct and FERM form a complex, as shown by gel filtration and pulldown experiments (Fig. 3, C and D). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-16T13:23:41.450Z"}}],"regions_counter":4,"released":"2024_06","sequence":"MDKFWWHTAWGLCLLQLSLAHPHQQIDLNVTCRYAGVFHVEKNGRYSISRTEAADLCQAFNSTLPTMDQMKLALSKGFETCRYGFIEGNVVIPRIHPNAICAANHTGVYILVTSNTSHYDTYCFNASAPPEEDCTSVTDLPNSFDGPVTITIVNRDGTRYSKKGEYRTHQEDIDASNIIDDDVSSGSTIEKSTPESYILHTYLPTEQPTGDQDDSFFIRSTLATRDRDSSKDSRGSSRTVTHGSELAGHSSANQDSGVTTTSGPMRRPQIPEWLIILASLLALALILAVCIAVNSRRRCGQKKKLVINGGNGTVEDRKPSELNGEASKSQEMVHLVNKEPSETPDQCMTADETRNLQSVDMKIGV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"alphafold_very_low_content":0.4054794520547945,"disorder_content":0.2,"disprot_consensus":{"full":[{"start":293,"end":365,"type":"D"}],"Structural state":[{"start":293,"end":365,"type":"D"}],"Molecular function":[{"start":293,"end":365,"type":"F"}]}},{"disprot_id":"DP03807","acc":"A8K2U0","creator":"vnugnes","date":"2022-09-30T16:08:20.988Z","features":{"pfam":[{"id":"PF00207","name":"Alpha-2-macroglobulin family","start":736,"end":825},{"id":"PF01835","name":"MG2 domain","start":122,"end":201},{"id":"PF07677","name":"A-macroglobulin receptor binding domain","start":1361,"end":1450},{"id":"PF07678","name":"A-macroglobulin TED domain","start":946,"end":1251},{"id":"PF07703","name":"Alpha-2-macroglobulin bait region domain","start":459,"end":601},{"id":"PF17789","name":"Macroglobulin domain MG4","start":342,"end":439},{"id":"PF17791","name":"Macroglobulin domain MG3","start":213,"end":302}],"gene3D":[]},"genes":[{"name":{"value":"A2ML1","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAI12132.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAI12132.1"}}]},"synonyms":[{"value":"CPAMD9","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:23336","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:23336"}}]}]}],"length":1454,"name":"Alpha-2-macroglobulin-like protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":634,"end":668,"reference_id":"35641520","reference_source":"pmid","reference_html":"Cryo-EM structures of human A2ML1 elucidate the protease-inhibitory mechanism of the A2M family. <i> Nielsen NS, Zarantonello A, Harwood SL, Jensen KT, Kjøge K, Thøgersen IB, Schauser L, Karlsen JL, Andersen GR, Enghild JJ. </i> Nat Commun, 2022","date":"2022-09-30T16:20:15.912Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7Q1yY"}],"region_id":"DP03807r001","statement":[{"text":"Residues 634–668 in A2ML1’s LNK region could not be modeled, suggesting that this region adopts multiple conformations.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"506227","entry_name":"N-acetyl-D-glucosamine"}]},{"start":696,"end":726,"reference_id":"35641520","reference_source":"pmid","reference_html":"Cryo-EM structures of human A2ML1 elucidate the protease-inhibitory mechanism of the A2M family. <i> Nielsen NS, Zarantonello A, Harwood SL, Jensen KT, Kjøge K, Thøgersen IB, Schauser L, Karlsen JL, Andersen GR, Enghild JJ. </i> Nat Commun, 2022","date":"2022-09-30T16:20:32.816Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7Q1yY"}],"region_id":"DP03807r002","statement":[{"text":"In both the EM and the X-ray structures of native A2ML1, it is not possible to model residues His696-Asp726, suggesting substantial flexibility of the intact bait region in accordance with its accessibility toward proteases (Fig. 1E, F).","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"506227","entry_name":"N-acetyl-D-glucosamine"}]}],"regions_counter":2,"released":"2023_12","sequence":"MWAQLLLGMLALSPAIAEELPNYLVTLPARLNFPSVQKVCLDLSPGYSDVKFTVTLETKDKTQKLLEYSGLKKRHLHCISFLVPPPAGGTEEVATIRVSGVGNNISFEEKKKVLIQRQGNGTFVQTDKPLYTPGQQVYFRIVTMDSNFVPVNDKYSMVELQDPNSNRIAQWLEVVPEQGIVDLSFQLAPEAMLGTYTVAVAEGKTFGTFSVEEYVLPKFKVEVVEPKELSTVQESFLVKICCRYTYGKPMLGAVQVSVCQKANTYWYREVEREQLPDKCRNLSGQTDKTGCFSAPVDMATFDLIGYAYSHQINIVATVVEEGTGVEANATQNIYISPQMGSMTFEDTSNFYHPNFPFSGKIRVRGHDDSFLKNHLVFLVIYGTNGTFNQTLVTDNNGLAPFTLETSGWNGTDVSLEGKFQMEDLVYNPEQVPRYYQNAYLHLRPFYSTTRSFLGIHRLNGPLKCGQPQEVLVDYYIDPADASPDQEISFSYYLIGKGSLVMEGQKHLNSKKKGLKASFSLSLTFTSRLAPDPSLVIYAIFPSGGVVADKIQFSVEMCFDNQVSLGFSPSQQLPGAEVELQLQAAPGSLCALRAVDESVLLLRPDRELSNRSVYGMFPFWYGHYPYQVAEYDQCPVSGPWDFPQPLIDPMPQGHSSQRSIIWRPSFSEGTDLFSFFRDVGLKILSNAKIKKPVDCSHRSPEYSTAMGAGGGHPEAFESSTPLHQAEDSQVRQYFPETWLWDLFPIGNSGKEAVHVTVPDAITEWKAMSFCTSQSRGFGLSPTVGLTAFKPFFVDLTLPYSVVRGESFRLTATIFNYLKDCIRVQTDLAKSHEYQLESWADSQTSSCLCADDAKTHHWNITAVKLGHINFTISTKILDSNEPCGGQKGFVPQKGRSDTLIKPVLVKPEGVLVEKTHSSLLCPKGKVASESVSLELPVDIVPDSTKAYVTVLGDIMGTALQNLDGLVQMPSGCGEQNMVLFAPIIYVLQYLEKAGLLTEEIRSRAVGFLEIGYQKELMYKHSNGSYSAFGERDGNGNTWLTAFVTKCFGQAQKFIFIDPKNIQDALKWMAGNQLPSGCYANVGNLLHTAMKGGVDDEVSLTAYVTAALLEMGKDVDDPMVSQGLRCLKNSATSTTNLYTQALLAYIFSLAGEMDIRNILLKQLDQQAIISGESIYWSQKPTPSSNASPWSEPAAVDVELTAYALLAQLTKPSLTQKEIAKATSIVAWLAKQHNAYGGFSSTQDTVVALQALAKYATTAYMPSEEINLVVKSTENFQRTFNIQSVNRLVFQQDTLPNVPGMYTLEASGQGCVYVQTVLRYNILPPTNMKTFSLSVEIGKARCEQPTSPRSLTLTIHTSYVGSRSSSNMAIVEVKMLSGFSPMEGTNQLLLQQPLVKKVEFGTDTLNIYLDELIKNTQTYTFTISQSVLVTNLKPATIKVYDYYLPDEQATIQYSDPCE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.06946354883081156,"dataset":["Extracellular matrix proteins"],"disorder_content":0.0453920220082531,"disprot_consensus":{"full":[{"start":634,"end":668,"type":"D"},{"start":696,"end":726,"type":"D"}],"Structural state":[{"start":634,"end":668,"type":"D"},{"start":696,"end":726,"type":"D"}]}},{"disprot_id":"DP03809","acc":"B6VDJ7","creator":"gbalatti","date":"2022-10-05T20:09:28.659Z","features":{"pfam":[{"id":"PF20483","name":"Flavivirus RNA-directed RNA polymerase, thumb domain","start":1,"end":51}],"gene3D":[]},"genes":[],"length":85,"name":"Nonstructural protein 5","ncbi_taxon_id":11069,"organism":"Dengue virus 3","regions":[{"start":50,"end":65,"reference_id":"27622521","reference_source":"pmid","reference_html":"The C-terminal 18 Amino Acid Region of Dengue Virus NS5 Regulates its Subcellular Localization and Contains a Conserved Arginine Residue Essential for Infectious Virus Production. <i> Tay MY, Smith K, Ng IH, Chan KW, Zhao Y, Ooi EE, Lescar J, Luo D, Jans DA, Forwood JK, Vasudevan SG. </i> PLoS Pathog, 2016","date":"2022-10-17T18:02:05.727Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"5FC8"}],"region_id":"DP03809r001","statement":[{"text":"Missing residues in X-ray diffraction pattern interpretation.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P52293","statements":[{"type":"Abstract","text":"The low micromolar binding affinity between NS5 Cter18 and the nuclear import receptor importin-alpha (Impα), allowed their molecular complex to be purified, crystallised and visualized at\n2.2 Å resolution using x-ray crystallography."},{"type":"Methods","text":"All protein structure coordinates and structure factor files for DENV2 C-terminal NLS and DENV3 C-terminal NLS complexes with importin alpha are available from the Protein Data Bank database (accession numbers: 5HHG and 5FC8, respectively)."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-17T18:47:31.272Z"}}],"regions_counter":1,"released":"2022_12","sequence":"VWIEDNPWMEDKTPVTTWENVPYLGKREDQWCGSLIGLTSRATWAQNIPTAIQQVRSLIGNEEFLDYMPSMKRFRKEEESEGAIW","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Flavivirus"],"dataset":["Neglected tropical diseases proteins","Viral proteins"],"disorder_content":0.18823529411764706,"disprot_consensus":{"full":[{"start":50,"end":65,"type":"D"}],"Structural state":[{"start":50,"end":65,"type":"D"}]}},{"disprot_id":"DP03810","acc":"P0AFI0","creator":"vacs","date":"2022-10-06T10:37:23.071Z","features":{"pfam":[{"id":"PF00205","name":"Thiamine pyrophosphate enzyme, central domain","start":202,"end":327},{"id":"PF02775","name":"Thiamine pyrophosphate enzyme, C-terminal TPP binding domain","start":403,"end":540},{"id":"PF02776","name":"Thiamine pyrophosphate enzyme, N-terminal TPP binding domain","start":9,"end":125}],"gene3D":[]},"genes":[{"name":{"value":"oxc"},"synonyms":[{"value":"yfdU"}],"olnNames":[{"value":"b2373"},{"value":"JW2370"}]}],"length":564,"name":"Oxalyl-CoA decarboxylase","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":552,"end":564,"reference_id":"20553497","reference_source":"pmid","reference_html":"New insights into structure-function relationships of oxalyl CoA decarboxylase from Escherichia coli. <i> Werther T, Zimmer A, Wille G, Golbik R, Weiss MS, König S. </i> FEBS J, 2010","date":"2022-10-06T10:40:46.050Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2Q27"},{"db":"PDB","id":"2Q28"},{"db":"PDB","id":"2Q29"}],"region_id":"DP03810r001","statement":[{"text":"For most of the polypeptide chains, the electron density is well defined, excluding residues 1–4 and 551–564 (555–564 for the ADP complex) in both chains.","type":"Results"},{"text":"However, four additional amino acid residues at the C-terminus were pinpointed in the presence of the activator ADP that are not defined in the absence of this ligand.","type":"Results"},{"text":"In both enzyme species, the C-terminal part of the subunits is not involved in crystal packing contacts.","type":"Discussion"},{"text":"Residues 552-564 are disordered in all structures in the absence of ADP.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-06T13:46:27.368Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MSDQLQMTDGMHIIVEALKQNNIDTIYGVVGIPVTDMARHAQAEGIRYIGFRHEQSAGYAAAASGFLTQKPGICLTVSAPGFLNGLTALANATVNGFPMIMISGSSDRAIVDLQQGDYEELDQMNAAKPYAKAAFRVNQPQDLGIALARAIRVSVSGRPGGVYLDLPANVLAATMEKDEALTTIVKVENPSPALLPCPKSVTSAISLLAKAERPLIILGKGAAYSQADEQLREFIESAQIPFLPMSMAKGILEDTHPLSAAAARSFALANADVVMLVGARLNWLLAHGKKGWAADTQFIQLDIEPQEIDSNRPIAVPVVGDIASSMQGMLAELKQNTFTTPLVWRDILNIHKQQNAQKMHEKLSTDTQPLNYFNALSAVRDVLRENQDIYLVNEGANTLDNARNIIDMYKPRRRLDCGTWGVMGIGMGYAIGASVTSGSPVVAIEGDSAFGFSGMEIETICRYNLPVTIVIFNNGGIYRGDGVDLSGAGAPSPTDLLHHARYDKLMDAFRGVGYNVTTTDELRHALTTGIQSRKPTIINVVIDPAAGTESGHITKLNPKQVAGN","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"alphafold_very_low_content":0.005319148936170213,"disorder_content":0.02304964539007092,"disprot_consensus":{"full":[{"start":552,"end":564,"type":"D"}],"Structural state":[{"start":552,"end":564,"type":"D"}]}},{"disprot_id":"DP03811","acc":"Q00266","creator":"vacs","date":"2022-10-06T11:39:26.991Z","features":{"pfam":[{"id":"PF00438","name":"S-adenosylmethionine synthetase, N-terminal domain","start":18,"end":115},{"id":"PF02772","name":"S-adenosylmethionine synthetase, central domain","start":130,"end":250},{"id":"PF02773","name":"S-adenosylmethionine synthetase, C-terminal domain","start":252,"end":388}],"gene3D":[]},"genes":[{"name":{"value":"MAT1A"},"synonyms":[{"value":"AMS1"},{"value":"MATA1"}]}],"length":395,"name":"S-adenosylmethionine synthase isoform type-1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":13,"reference_id":"32496220","reference_source":"pmid","reference_html":"Structural basis of the dominant inheritance of hypermethioninemia associated with the Arg264His mutation in the MAT1A gene. <i> Panmanee J, Antonyuk SV, Hasnain SS. </i> Acta Crystallogr D Struct Biol, 2020","date":"2022-10-06T11:42:11.771Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6SW5"},{"db":"PDB","id":"6SW6"}],"region_id":"DP03811r001","statement":[{"text":"The first region is the N-terminal region Met1–Glu15, which has been found to be missing in most reported MAT structures owing to its flexibility.","type":"Results"},{"text":"Chain B contains three invisible regions, the N-terminus (Met1–Glu15), the gating loop (Asp116–Glu127) and the Phe250–Gly257 region, while chain A contains an ordered gating loop and the Phe250–Gly257 region shows a clear electron-density map.","type":"Results"},{"text":"Region 1-13 is disordered in all structures.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-06T13:57:35.462Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MNGPVDGLCDHSLSEGVFMFTSESVGEGHPDKICDQISDAVLDAHLKQDPNAKVACETVCKTGMVLLCGEITSMAMVDYQRVVRDTIKHIGYDDSAKGFDFKTCNVLVALEQQSPDIAQCVHLDRNEEDVGAGDQGLMFGYATDETEECMPLTIILAHKLNARMADLRRSGLLPWLRPDSKTQVTVQYMQDNGAVIPVRIHTIVISVQHNEDITLEEMRRALKEQVIRAVVPAKYLDEDTVYHLQPSGRFVIGGPQGDAGVTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKAGLCRRVLVQVSYAIGVAEPLSISIFTYGTSQKTERELLDVVHKNFDLRPGVIVRDLDLKKPIYQKTACYGHFGRSEFPWEVPRKLVF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.02278481012658228,"disorder_content":0.03291139240506329,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"D"}],"Structural state":[{"start":1,"end":13,"type":"D"}]}},{"disprot_id":"DP03812","acc":"P33371","creator":"vacs","date":"2022-10-07T10:19:20.062Z","features":{"pfam":[{"id":"PF01207","name":"Dihydrouridine synthase (Dus)","start":4,"end":307}],"gene3D":[]},"genes":[{"name":{"value":"dusC","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_02043","url":"https://hamap.expasy.org/unirule/MF_02043"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"11983710","url":"http://www.ncbi.nlm.nih.gov/pubmed/11983710","alternativeUrl":"https://europepmc.org/abstract/MED/11983710"}}]},"synonyms":[{"value":"yohI"}],"olnNames":[{"value":"b2140"},{"value":"JW2128"}]}],"length":315,"name":"tRNA-dihydrouridine(16) synthase","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":99,"end":111,"reference_id":"23908023","reference_source":"pmid","reference_html":"Structure of dihydrouridine synthase C (DusC) from Escherichia coli. <i> Chen M, Yu J, Tanaka Y, Tanaka M, Tanaka I, Yao M. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2013","date":"2022-10-07T10:21:45.028Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3W9Z"}],"region_id":"DP03812r001","statement":[{"text":"Owing to poor electron density, the regions Pro99–Thr111, Lys261–Tyr268, Lys297–Asn299 and Leu315–His322 were not modelled.","type":"Results"},{"text":"In the structure of EcoDusC, the adjacent loop above the active site (Pro99–Thr111) was disordered instead of this loop, suggesting that a different loop is used for tRNA recognition in TthDus and EcoDusC.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-11T18:33:48.102Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MRVLLAPMEGVLDSLVRELLTEVNDYDLCITEFVRVVDQLLPVKVFHRICPELQNASRTPSGTLVRVQLLGQFPQWLAENAARAVELGSWGVDLNCGCPSKTVNGSGGGATLLKDPELIYQGAKAMREAVPAHLPVSVKVRLGWDSGEKKFEIADAVQQAGATELVVHGRTKEQGYRAEHIDWQAIGDIRQRLNIPVIANGEIWDWQSAQQCMAISGCDAVMIGRGALNIPNLSRVVKYNEPRMPWPEVVALLQKYTRLEKQGDTGLYHVARIKQWLSYLRKEYDEATELFQHVRVLNNSPDIARAIQAIDIEKL","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"alphafold_very_low_content":0,"dataset":["RNA-binding proteins"],"disorder_content":0.04126984126984127,"disprot_consensus":{"full":[{"start":99,"end":111,"type":"D"}],"Structural state":[{"start":99,"end":111,"type":"D"}]}},{"disprot_id":"DP03813","acc":"P0A6B7","creator":"vacs","date":"2022-10-07T10:55:36.505Z","features":{"pfam":[{"id":"PF00266","name":"Aminotransferase class-V","start":5,"end":368}],"gene3D":[]},"genes":[{"name":{"value":"iscS","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00331","url":"https://hamap.expasy.org/unirule/MF_00331"}}]},"synonyms":[{"value":"nuvC"},{"value":"yfhO"},{"value":"yzzO"}],"olnNames":[{"value":"b2530"},{"value":"JW2514"}]}],"length":404,"name":"Cysteine desulfurase IscS","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":393,"end":404,"reference_id":"12860127","reference_source":"pmid","reference_html":"Crystal structure of IscS, a cysteine desulfurase from Escherichia coli. <i> Cupp-Vickery JR, Urbina H, Vickery LE. </i> J Mol Biol, 2003","date":"2022-10-07T10:57:24.189Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1P3W"}],"region_id":"DP03813r001","statement":[{"text":"The refined model consists of 385 residues/monomer (of 404 residues total) with residues 328–333 and 393–404 omitted due to poor electron density in these regions.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-11T18:35:56.356Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MKLPIYLDYSATTPVDPRVAEKMMQFMTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLVGADPREIVFTSGATESDNLAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRVRIEAQMHGGGHERGMRSGTLPVHQIVGMGEAYRIAKEEMATEMERLRGLRNRLWNGIKDIEEVYLNGDLEHGAPNILNVSFNYVEGESLIMALKDLAVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYTIELVRKSIGRLRDLSPLWEMYKQGVDLNSIEWAHH","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"alphafold_very_low_content":0.019801980198019802,"disorder_content":0.0297029702970297,"disprot_consensus":{"full":[{"start":393,"end":404,"type":"D"}],"Structural state":[{"start":393,"end":404,"type":"D"}]}},{"disprot_id":"DP03814","acc":"Q9BU02","creator":"vacs","date":"2022-10-08T11:35:40.838Z","features":{"pfam":[{"id":"PF01928","name":"CYTH domain","start":6,"end":189}],"gene3D":[]},"genes":[{"name":{"value":"THTPA"}}],"length":230,"name":"Thiamine-triphosphatase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":215,"end":230,"reference_id":"23707715","reference_source":"pmid","reference_html":"Structural determinants of specificity and catalytic mechanism in mammalian 25-kDa thiamine triphosphatase. <i> Delvaux D, Kerff F, Murty MR, Lakaye B, Czerniecki J, Kohn G, Wins P, Herman R, Gabelica V, Heuze F, Tordoir X, Marée R, Matagne A, Charlier P, De Pauw E, Bettendorff L. </i> Biochim Biophys Acta, 2013","date":"2022-10-08T11:37:02.718Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3TVL"}],"region_id":"DP03814r001","statement":[{"text":"A few residues are not sufficiently defined at the N and C terminal ends as well as in the loop connecting β6 and β7. In monomer A, residues 4 to 132 and 140 to 214 could be built in the electronic density while residues 5 to 132 and 141 to 211 of monomer B are present in the model.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-11T18:37:14.456Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MAQGLIEVERKFLPGPGTEERLQELGGTLEYRVTFRDTYYDTPELSLMQADHWLRRREDSGWELKCPGAAGVLGPHTEYKELTAEPTIVAQLCKVLRADGLGAGDVAAVLGPLGLQEVASFVTKRSAWKLVLLGADEEEPQLRVDLDTADFGYAVGEVEALVHEEAEVPTALEKIHRLSSMLGVPAQETAPAKLIVYLQRFRPQDYQRLLEVNSSRERPQETEDPDHCLG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.05652173913043478,"disorder_content":0.06956521739130435,"disprot_consensus":{"full":[{"start":215,"end":230,"type":"D"}],"Structural state":[{"start":215,"end":230,"type":"D"}]}},{"disprot_id":"DP03815","acc":"P32449","creator":"vacs","date":"2022-10-08T12:04:36.215Z","features":{"pfam":[{"id":"PF00793","name":"DAHP synthetase I family","start":55,"end":354}],"gene3D":[]},"genes":[{"name":{"value":"ARO4"},"orfNames":[{"value":"YBR1701"}],"olnNames":[{"value":"YBR249C"}]}],"length":370,"name":"Phospho-2-dehydro-3-deoxyheptonate aldolase, tyrosine-inhibited","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":22,"reference_id":"12540830","reference_source":"pmid","reference_html":"Evolution of feedback-inhibited beta /alpha barrel isoenzymes by gene duplication and a single mutation. <i> Hartmann M, Schneider TR, Pfeil A, Heinrich G, Lipscomb WN, Braus GH. </i> Proc Natl Acad Sci U S A, 2003","date":"2022-10-08T12:07:39.831Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1HFB"}],"region_id":"DP03815r001","statement":[{"text":"For all eight monomers, no electron density was found for residues M1 to D22.","type":"Methods"},{"text":"The N-terminal region, found to be unstructured in both crystals of the E. coli and the yeast enzyme, was shown to become structured after the binding of an effector molecule and forming a lid supporting the coordination of the effector (26).","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-11T18:39:29.147Z"}},{"start":1,"end":20,"reference_id":"12540830","reference_source":"pmid","reference_html":"Evolution of feedback-inhibited beta /alpha barrel isoenzymes by gene duplication and a single mutation. <i> Hartmann M, Schneider TR, Pfeil A, Heinrich G, Lipscomb WN, Braus GH. </i> Proc Natl Acad Sci U S A, 2003","date":"2022-10-08T12:27:18.582Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"GO:0043085","term_name":"positive regulation of catalytic activity","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IMP","region_id":"DP03815r002","statement":[{"text":"Stable deletion of the N-terminal 20 amino acids resulted in an unregulated DAHP synthase with lowered activity in comparison to WT (11%).","type":"Results"}],"term_comment":"","term_def":"\"Any process that activates or increases the activity of an enzyme.\" [GOC:ebc, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-11T18:39:41.808Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MSESPMFAANGMPKVNQGAEEDVRILGYDPLASPALLQVQIPATPTSLETAKRGRREAIDIITGKDDRVLVIVGPCSIHDLEAAQEYALRLKKLSDELKGDLSIIMRAYLEKPRTTVGWKGLINDPDVNNTFNINKGLQSARQLFVNLTNIGLPIGSEMLDTISPQYLADLVSFGAIGARTTESQLHRELASGLSFPVGFKNGTDGTLNVAVDACQAAAHSHHFMGVTKHGVAAITTTKGNEHCFVILRGGKKGTNYDAKSVAEAKAQLPAGSNGLMIDYSHGNSNKDFRNQPKVNDVVCEQIANGENAITGVMIESNINEGNQGIPAEGKAGLKYGVSITDACIGWETTEDVLRKLAAAVRQRREVNKK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.013513513513513514,"dataset":["Stress response proteins"],"disorder_content":0.05945945945945946,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"}],"Structural state":[{"start":1,"end":22,"type":"D"}],"Biological process":[{"start":1,"end":20,"type":"F"}]}},{"disprot_id":"DP03816","acc":"Q99986","creator":"fkordevani","date":"2022-10-13T12:36:13.648Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":41,"end":272}],"gene3D":[]},"genes":[{"name":{"value":"VRK1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9344656","url":"http://www.ncbi.nlm.nih.gov/pubmed/9344656","alternativeUrl":"https://europepmc.org/abstract/MED/9344656"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:12718","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:12718"}}]}}],"length":396,"name":"Serine/threonine-protein kinase VRK1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":20,"reference_id":"21543316","reference_source":"pmid","reference_html":"NMR solution structure of human vaccinia-related kinase 1 (VRK1) reveals the C-terminal tail essential for its structural stability and autocatalytic activity. <i> Shin J, Chakraborty G, Bharatham N, Kang C, Tochio N, Koshiba S, Kigawa T, Kim W, Kim KT, Yoon HS. </i> J Biol Chem, 2011","date":"2022-10-14T08:33:37.956Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"BMRB","id":"16738"},{"db":"PDB","id":"2LAV"}],"region_id":"DP03816r001","statement":[{"text":"The N-terminal tail (residues 1–20) is unstructured in solution as evidenced by the lack of medium and long range nuclear Overhauser effects (NOEs) in this region.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-14T12:44:35.394Z"}},{"start":343,"end":364,"reference_id":"30461091","reference_source":"pmid","reference_html":"Crystal structure of human vaccinia-related kinase 1 in complex with AMP-PNP, a non-hydrolyzable ATP analog. <i> Ngow YS, Rajan S, Ye H, Yoon HS. </i> Protein Sci, 2019","date":"2023-05-05T14:25:01.908Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6AC9"}],"region_id":"DP03816r002","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:33113"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:8200"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T13:41:32.255Z"}},{"start":342,"end":353,"reference_id":"21543316","reference_source":"pmid","reference_html":"NMR solution structure of human vaccinia-related kinase 1 (VRK1) reveals the C-terminal tail essential for its structural stability and autocatalytic activity. <i> Shin J, Chakraborty G, Bharatham N, Kang C, Tochio N, Koshiba S, Kigawa T, Kim W, Kim KT, Yoon HS. </i> J Biol Chem, 2011","date":"2023-05-05T14:00:24.366Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"GO:0016301","term_name":"kinase activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001202","ec_ontology":"ECO","ec_name":"in vitro protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IDA","region_id":"DP03816r003","statement":[{"text":"Our data showed that S342A and T353A mutants reduce the autocatalytic activities of VRK1, indicating that those residues play key roles in the kinase activity (supplemental Fig. S3).","type":"Results"}],"term_comment":"Note that this term encompasses all activities that transfer a single phosphate group; although ATP is by far the most common phosphate donor, reactions using other phosphate donors are included in this term.","term_def":"\"Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.\" [ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser342Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr353Ala","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T13:41:25.291Z"}},{"start":342,"end":364,"reference_id":"28790404","reference_source":"pmid","reference_html":"Structural characterization of human Vaccinia-Related Kinases (VRK) bound to small-molecule inhibitors identifies different P-loop conformations. <i> Couñago RM, Allerston CK, Savitsky P, Azevedo H, Godoi PH, Wells CI, Mascarello A, de Souza Gama FH, Massirer KB, Zuercher WJ, Guimarães CRW, Gileadi O. </i> Sci Rep, 2017","date":"2023-05-05T14:22:04.746Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5UVF"},{"db":"PDB","id":"3OP5"},{"db":"PDB","id":"5UKF"}],"region_id":"DP03816r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:45111332"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:174"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:44141268"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1061"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:124222743"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:8117"}],"statement":[{"text":"Nevertheless, the most complete polypeptide chain in this model contains an intact P-loop (chain A, residues 22–341; used for the structural comparisons below).","type":"Results"},{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T13:48:24.950Z"}}],"regions_counter":4,"released":"2023_06","sequence":"MPRVKAAQAGRQSSAKRHLAEQFAVGEIITDMAKKEWKVGLPIGQGGFGCIYLADMNSSESVGSDAPCVVKVEPSDNGPLFTELKFYQRAAKPEQIQKWIRTRKLKYLGVPKYWGSGLHDKNGKSYRFMIMDRFGSDLQKIYEANAKRFSRKTVLQLSLRILDILEYIHEHEYVHGDIKASNLLLNYKNPDQVYLVDYGLAYRYCPEGVHKEYKEDPKRCHDGTIEFTSIDAHNGVAPSRRGDLEILGYCMIQWLTGHLPWEDNLKDPKYVRDSKIRYRENIASLMDKCFPEKNKPGEIAKYMETVKLLDYTEKPLYENLRDILLQGLKAIGSKDDGKLDLSVVENGGLKAKTITKKRKKEIEESKEPGVEDTEWSNTQTEEAIQTRSRTRKRVQK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.1691919191919192,"disorder_content":0.10858585858585859,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"D"},{"start":342,"end":364,"type":"D"}],"Structural state":[{"start":1,"end":20,"type":"D"},{"start":342,"end":364,"type":"D"}],"Molecular function":[{"start":342,"end":353,"type":"F"}]}},{"disprot_id":"DP03817","acc":"P42658","creator":"fkordevani","date":"2022-10-13T14:00:49.511Z","features":{"pfam":[{"id":"PF00326","name":"Prolyl oligopeptidase family","start":642,"end":848},{"id":"PF00930","name":"Dipeptidyl peptidase IV (DPP IV) N-terminal region","start":195,"end":561}],"gene3D":[]},"genes":[{"name":{"value":"DPP6"}}],"length":865,"name":"Dipeptidyl aminopeptidase-like protein 6","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":117,"end":126,"reference_id":"15476821","reference_source":"pmid","reference_html":"Structure of a human A-type potassium channel interacting protein DPPX, a member of the dipeptidyl aminopeptidase family. <i> Strop P, Bankovich AJ, Hansen KC, Garcia KC, Brunger AT. </i> J Mol Biol, 2004","date":"2022-10-14T08:32:43.320Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1XFD"}],"region_id":"DP03817r001","statement":[{"text":"The first ten and last 16 residues of the extracellular domain of DPPX were disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-14T12:47:04.482Z"}},{"start":850,"end":865,"reference_id":"15476821","reference_source":"pmid","reference_html":"Structure of a human A-type potassium channel interacting protein DPPX, a member of the dipeptidyl aminopeptidase family. <i> Strop P, Bankovich AJ, Hansen KC, Garcia KC, Brunger AT. </i> J Mol Biol, 2004","date":"2022-10-13T14:08:40.966Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1XFD"}],"region_id":"DP03817r002","statement":[{"text":"The first ten and last 16 residues of the extracellular domain of DPPX were disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-13T16:09:55.631Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MASLYQRFTGKINTSRSFPAPPEASHLLGGQGPEEDGGAGAKPLGPRAQAAAPRERGGGGGGAGGRPRFQYQARSDGDEEDELVGSNPPQRNWKGIAIALLVILVICSLIVTSVILLTPAEDNSLSQKKKVTVEDLFSEDFKIHDPEAKWISDTEFIYREQKGTVRLWNVETNTSTVLIEGKKIESLRAIRYEISPDREYALFSYNVEPIYQHSYTGYYVLSKIPHGDPQSLDPPEVSNAKLQYAGWGPKGQQLIFIFENNIYYCAHVGKQAIRVVSTGKEGVIYNGLSDWLYEEEILKTHIAHWWSPDGTRLAYAAINDSRVPIMELPTYTGSIYPTVKPYHYPKAGSENPSISLHVIGLNGPTHDLEMMPPDDPRMREYYITMVKWATSTKVAVTWLNRAQNVSILTLCDATTGVCTKKHEDESEAWLHRQNEEPVFSKDGRKFFFIRAIPQGGRGKFYHITVSSSQPNSSNDNIQSITSGDWDVTKILAYDEKGNKIYFLSTEDLPRRRQLYSANTVGNFNRQCLSCDLVENCTYFSASFSHSMDFFLLKCEGPGVPMVTVHNTTDKKKMFDLETNEHVKKAINDRQMPKVEYRDIEIDDYNLPMQILKPATFTDTTHYPLLLVVDGTPGSQSVAEKFEVSWETVMVSSHGAVVVKCDGRGSGFQGTKLLHEVRRRLGLLEEKDQMEAVRTMLKEQYIDRTRVAVFGKDYGGYLSTYILPAKGENQGQTFTCGSALSPITDFKLYASAFSERYLGLHGLDNRAYEMTKVAHRVSALEEQQFLIIHPTADEKIHFQHTAELITQLIRGKANYSLQIYPDESHYFTSSSLKQHLYRSIINFFVECFRIQDKLLTVTAKEDEEED","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.11791907514450867,"disorder_content":0.03005780346820809,"disprot_consensus":{"full":[{"start":117,"end":126,"type":"D"},{"start":850,"end":865,"type":"D"}],"Structural state":[{"start":117,"end":126,"type":"D"},{"start":850,"end":865,"type":"D"}]}},{"disprot_id":"DP03818","acc":"P57104","creator":"ldobson","date":"2022-10-13T15:06:32.262Z","features":{"pfam":[],"gene3D":[]},"genes":[],"length":13,"name":"Temporin-1Tl","ncbi_taxon_id":8407,"organism":"Rana temporaria","regions":[{"start":1,"end":13,"reference_id":"11991956","reference_source":"pmid","reference_html":"Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence. <i> Zhao H, Kinnunen PK. </i> J Biol Chem, 2002","date":"2022-10-13T15:08:38.188Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03818r001","statement":[{"text":"In an aqueous solution, temporin L adopts a random coil conformation, revealed by the single minimum at 200 nm (Fig.1).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-13T18:15:57.464Z"}},{"start":1,"end":13,"reference_id":"11991956","reference_source":"pmid","reference_html":"Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence. <i> Zhao H, Kinnunen PK. </i> J Biol Chem, 2002","date":"2022-10-15T17:30:40.703Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03818r002","statement":[{"text":"However, in the presence of small unilamellar vesicles, the peptide is α-helical, with the characteristic double minima at 210 and 222 nm. Compared with the zwitterionic SOPC small unilamellar vesicles, the helical conformation is more pronounced in the presence of the negatively charged phospholipid POPG, with the calculated helical content increasing from 69 to 89% at X POPG = 0 and 0.4, respectively.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-17T12:39:12.306Z"}},{"start":1,"end":13,"reference_id":"11991956","reference_source":"pmid","reference_html":"Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence. <i> Zhao H, Kinnunen PK. </i> J Biol Chem, 2002","date":"2022-10-13T15:13:32.643Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","region_id":"DP03818r003","statement":[{"text":"However, in the presence of small unilamellar vesicles, the peptide is α-helical, with the characteristic double minima at 210 and 222 nm.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-13T18:20:43.207Z"}},{"start":1,"end":13,"reference_id":"11991956","reference_source":"pmid","reference_html":"Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence. <i> Zhao H, Kinnunen PK. </i> J Biol Chem, 2002","date":"2022-10-13T15:18:57.901Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP03818r004","statement":[{"text":"Upon the addition of SOPC liposomes, a blue shift of the fluorescence emission maximum of Trp4 was observed (Fig. 2 A), whereas the emission intensity (F) was attenuated (Fig. 2 A). Instead, pronounced increase in F and a blue shift were evident in the presence of POPG (Fig. 2 A), the increase being progressively enhanced with increasing X POPG in the membranes (Fig.2 B).","type":"Results"},{"text":"Fluorescence of Trp4decreased in a concentration-dependent manner by the addition of acrylamide to the peptide solution both in the absence and presence of liposomes, without other effects on the spectra (data not shown). However, in the presence of liposomes, less decrement in fluorescence intensity was evident, thus revealing that Trp4 is less accessible to the quencher in the presence of LUVs.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-13T18:21:15.477Z"}},{"start":1,"end":13,"reference_id":"12133008","reference_source":"pmid","reference_html":"Temporin L: antimicrobial, haemolytic and cytotoxic activities, and effects on membrane permeabilization in lipid vesicles. <i> Rinaldi AC, Mangoni ML, Rufo A, Luzi C, Barra D, Zhao H, Kinnunen PK, Bozzi A, Di Giulio A, Simmaco M. </i> Biochem J, 2002","date":"2022-10-15T17:32:52.403Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0042742","term_name":"defense response to bacterium","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007634","ec_ontology":"ECO","ec_name":"experimental phenotypic evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","region_id":"DP03818r005","statement":[{"text":"Temporin L also displayed very good activity against Gram-negative bacterial strains such as E. coli D21 and Ps. aeruginosa A.T.C.C. 15692, with LC values of 1.5 and 3.6 µM respectively.","type":"Results"},{"text":"Temporin L, like temporin B, showed increasing antibacterial potency against cell-wall-defective mutant strains of E. coli D21, i.e. D21 e7, D21 f1 and D21 f2, which have lost increasing amounts of sugar residues of their lipopolysaccharide (LPS) chain [33]","type":"Results"}],"term_comment":"","term_def":"\"Reactions triggered in response to the presence of a bacterium that act to protect the cell or organism.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-17T12:39:28.745Z"}},{"start":1,"end":13,"reference_id":"12133008","reference_source":"pmid","reference_html":"Temporin L: antimicrobial, haemolytic and cytotoxic activities, and effects on membrane permeabilization in lipid vesicles. <i> Rinaldi AC, Mangoni ML, Rufo A, Luzi C, Barra D, Zhao H, Kinnunen PK, Bozzi A, Di Giulio A, Simmaco M. </i> Biochem J, 2002","date":"2022-10-13T16:40:23.637Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0044179","term_name":"hemolysis in another organism","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007634","ec_ontology":"ECO","ec_name":"experimental phenotypic evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","region_id":"DP03818r006","statement":[{"text":"The effects of increasing temporin L concentrations on the haemolysis of human erythrocytes are reported in Figure 4. Beyond 2 µM, considerable haemolysis was observed, with 100% lysis at approx. 55 µM.","type":"Results"}],"term_comment":"","term_def":"\"The cytolytic destruction of red blood cells, with the release of intracellular hemoglobin, in one organism by another.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-13T18:34:59.006Z"}},{"start":1,"end":13,"reference_id":"16261508","reference_source":"pmid","reference_html":"Conformational behavior of temporin A and temporin L in aqueous solution: a computational/experimental study. <i> D'Abramo M, Rinaldi AC, Bozzi A, Amadei A, Mignogna G, Di Nola A, Aschi M. </i> Biopolymers, 2006","date":"2022-10-13T16:46:50.645Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03818r007","statement":[{"text":"The experiments demonstrate that for both peptides an increase in TFE concentration caused a progressive change from a random coil to an α-helical structure (Figure 1). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-13T18:26:55.611Z"}},{"start":1,"end":13,"reference_id":"12133008","reference_source":"pmid","reference_html":"Temporin L: antimicrobial, haemolytic and cytotoxic activities, and effects on membrane permeabilization in lipid vesicles. <i> Rinaldi AC, Mangoni ML, Rufo A, Luzi C, Barra D, Zhao H, Kinnunen PK, Bozzi A, Di Giulio A, Simmaco M. </i> Biochem J, 2002","date":"2022-10-15T17:34:22.187Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0050832","term_name":"defense response to fungus","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007634","ec_ontology":"ECO","ec_name":"experimental phenotypic evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","region_id":"DP03818r009","statement":[{"text":"Against Candida species, the potency of temporin L was of the same order as that reported for temporin B, and approx. 2–9 times lower than that indicated for amphotericin B (with the exception of C. guillier-mondii, which is totally resistant to the latter compound).","type":"Results"}],"term_comment":"","term_def":"\"Reactions triggered in response to the presence of a fungus that act to protect the cell or organism.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-17T12:39:21.071Z"}},{"start":1,"end":13,"reference_id":"31358802","reference_source":"pmid","reference_html":"Temporin L and aurein 2.5 have identical conformations but subtly distinct membrane and antibacterial activities. <i> Manzo G, Ferguson PM, Hind CK, Clifford M, Gustilo VB, Ali H, Bansal SS, Bui TT, Drake AF, Atkinson RA, Sutton JM, Lorenz CD, Phoenix DA, Mason AJ. </i> Sci Rep, 2019","date":"2024-05-07T14:28:19.511Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"6GS5"}],"region_id":"DP03818r010","statement":[{"text":"In SDS, both the far-UV CD and the NMR structures agree that both peptides adopt ordered α-helix conformations.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:3423265"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-24T15:39:12.706Z"}},{"start":1,"end":13,"reference_id":"31358802","reference_source":"pmid","reference_html":"Temporin L and aurein 2.5 have identical conformations but subtly distinct membrane and antibacterial activities. <i> Manzo G, Ferguson PM, Hind CK, Clifford M, Gustilo VB, Ali H, Bansal SS, Bui TT, Drake AF, Atkinson RA, Sutton JM, Lorenz CD, Phoenix DA, Mason AJ. </i> Sci Rep, 2019","date":"2024-05-07T14:30:04.064Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP03818r011","statement":[{"text":"After binding to lipid bilayers, in the steady-state far-UV CD again indicates similar ordered α-helix conformations are adopted by both peptides; in the absence of lipid both peptides adopt disordered conformations (Fig. S4).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-24T15:40:03.741Z"}},{"start":1,"end":13,"reference_id":"31358802","reference_source":"pmid","reference_html":"Temporin L and aurein 2.5 have identical conformations but subtly distinct membrane and antibacterial activities. <i> Manzo G, Ferguson PM, Hind CK, Clifford M, Gustilo VB, Ali H, Bansal SS, Bui TT, Drake AF, Atkinson RA, Sutton JM, Lorenz CD, Phoenix DA, Mason AJ. </i> Sci Rep, 2019","date":"2024-05-07T14:32:07.259Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP03818r013","statement":[{"text":"This shows that, while secondary amphipathic α-helix conformations are a vital element in the binding and disruption of bacterial plasma membranes, individual amino acids in the distinct structures make important structural and dynamic contributions that determine the precise mechanism of action, potency and species selectivity of AMPs.","type":"Discussion"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-24T16:50:12.836Z"}},{"start":1,"end":13,"reference_id":"31358802","reference_source":"pmid","reference_html":"Temporin L and aurein 2.5 have identical conformations but subtly distinct membrane and antibacterial activities. <i> Manzo G, Ferguson PM, Hind CK, Clifford M, Gustilo VB, Ali H, Bansal SS, Bui TT, Drake AF, Atkinson RA, Sutton JM, Lorenz CD, Phoenix DA, Mason AJ. </i> Sci Rep, 2019","date":"2025-03-24T16:22:09.250Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0050830","term_name":"defense response to Gram-positive bacterium","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007699","ec_ontology":"ECO","ec_name":"cell growth assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","region_id":"DP03818r014","statement":[{"text":"In the present study, temporin L is shown to be more potent than aurein 2.5 against all strains included in both the Gram-positive and Gram-negative bacteria panels and Candida albicans (Table 2). For the Gram-positive strains, aurein 2.5 is outperformed by temporin L with, on average a 7.6-fold greater potency for the latter. For the Gram-negative strains, the difference between the potency of aurein 2.5 and temporin L is less, notably for both Acinetobacter baumannii isolates.","type":"Results"}],"term_comment":"","term_def":"\"Reactions triggered in response to the presence of a Gram-positive bacterium that act to protect the cell or organism.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":13,"reference_id":"31358802","reference_source":"pmid","reference_html":"Temporin L and aurein 2.5 have identical conformations but subtly distinct membrane and antibacterial activities. <i> Manzo G, Ferguson PM, Hind CK, Clifford M, Gustilo VB, Ali H, Bansal SS, Bui TT, Drake AF, Atkinson RA, Sutton JM, Lorenz CD, Phoenix DA, Mason AJ. </i> Sci Rep, 2019","date":"2025-03-24T16:22:20.760Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0050829","term_name":"defense response to Gram-negative bacterium","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007699","ec_ontology":"ECO","ec_name":"cell growth assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","region_id":"DP03818r015","statement":[{"text":"In the present study, temporin L is shown to be more potent than aurein 2.5 against all strains included in both the Gram-positive and Gram-negative bacteria panels and Candida albicans (Table 2). For the Gram-positive strains, aurein 2.5 is outperformed by temporin L with, on average a 7.6-fold greater potency for the latter. For the Gram-negative strains, the difference between the potency of aurein 2.5 and temporin L is less, notably for both Acinetobacter baumannii isolates.","type":"Results"}],"term_comment":"","term_def":"\"Reactions triggered in response to the presence of a Gram-negative bacterium that act to protect the cell or organism.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":13,"reference_id":"31358802","reference_source":"pmid","reference_html":"Temporin L and aurein 2.5 have identical conformations but subtly distinct membrane and antibacterial activities. <i> Manzo G, Ferguson PM, Hind CK, Clifford M, Gustilo VB, Ali H, Bansal SS, Bui TT, Drake AF, Atkinson RA, Sutton JM, Lorenz CD, Phoenix DA, Mason AJ. </i> Sci Rep, 2019","date":"2025-03-24T16:38:48.580Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0035915","term_name":"pore formation in membrane of another organism","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP03818r016","statement":[{"text":"In the present study, temporin L is shown to be more potent than aurein 2.5 against all strains included in both the Gram-positive and Gram-negative bacteria panels and Candida albicans (Table 2). For the Gram-positive strains, aurein 2.5 is outperformed by temporin L with, on average a 7.6-fold greater potency for the latter. For the Gram-negative strains, the difference between the potency of aurein 2.5 and temporin L is less, notably for both Acinetobacter baumannii isolates.","type":"Results"},{"text":"In contrast, in the present study both aurein 2.5 and temporin L were found to be capable of inducing channel like activity (Fig. 6). For aurein 2.5 this was observed in both membrane types (Fig. 6A,B) whereas for temporin L this was only found when challenging membranes formed from DPhPG (Fig. 6D).","type":"Results"},{"text":"This shows that, while secondary amphipathic α-helix conformations are a vital element in the binding and disruption of bacterial plasma membranes, individual amino acids in the distinct structures make important structural and dynamic contributions that determine the precise mechanism of action, potency and species selectivity of AMPs.","type":"Conclusion"},{"text":"The resulting estimated pore size indicates that temporin L is capable of creating pores that are at least twice the diameter of a chloride ion.","type":"Results"}],"term_comment":"","term_def":"\"The aggregation, arrangement and bonding together of a set of components by an organism to form a pore complex in a membrane of another organism.\" [GOC:bf, GOC:fj, PMID:21549739]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":13,"reference_id":"31358802","reference_source":"pmid","reference_html":"Temporin L and aurein 2.5 have identical conformations but subtly distinct membrane and antibacterial activities. <i> Manzo G, Ferguson PM, Hind CK, Clifford M, Gustilo VB, Ali H, Bansal SS, Bui TT, Drake AF, Atkinson RA, Sutton JM, Lorenz CD, Phoenix DA, Mason AJ. </i> Sci Rep, 2019","date":"2025-03-24T16:46:12.220Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0015267","term_name":"channel activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006006","ec_ontology":"ECO","ec_name":"electrophysiology assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","region_id":"DP03818r017","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:449312","statements":[{"type":"Curator statement","text":"DPhPG bilayers mimick Gram-positive bacteria cytoplasmic membranes."}]}],"statement":[{"text":"Similar to aurein 2.5, temporin L has channel like activity when challenging DPhPG membranes.","type":"Results"},{"text":"In contrast, in the present study both aurein 2.5 and temporin L were found to be capable of inducing channel like activity (Fig. 6). For aurein 2.5 this was observed in both membrane types (Fig. 6A,B) whereas for temporin L this was only found when challenging membranes formed from DPhPG (Fig. 6D).","type":"Results"}],"term_comment":"","term_def":"\"Enables the energy-independent facilitated diffusion, mediated by passage of a solute through a transmembrane aqueous pore or channel. Stereospecificity is not exhibited but this transport may be specific for a particular molecular species or class of molecules.\" [GOC:mtg_transport, ISBN:0815340729]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":17,"released":"2024_06","sequence":"FVQWFSKFLGRIL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Amphibia","Batrachia","Anura","Neobatrachia","Ranoidea","Ranidae","Rana","Rana"],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"T"}],"Structural state":[{"start":1,"end":13,"type":"D"}],"Structural transition":[{"start":1,"end":13,"type":"T"}],"Molecular function":[{"start":1,"end":13,"type":"F"}],"Biological process":[{"start":1,"end":13,"type":"F"}]}},{"disprot_id":"DP03819","acc":"P56917","creator":"jssuarez","date":"2022-10-14T07:23:51.145Z","features":{"pfam":[],"gene3D":[]},"genes":[],"length":13,"name":"Temporin-1Ta","ncbi_taxon_id":8407,"organism":"Rana temporaria","regions":[{"start":1,"end":13,"reference_id":"16261508","reference_source":"pmid","reference_html":"Conformational behavior of temporin A and temporin L in aqueous solution: a computational/experimental study. <i> D'Abramo M, Rinaldi AC, Bozzi A, Amadei A, Mignogna G, Di Nola A, Aschi M. </i> Biopolymers, 2006","date":"2022-10-14T07:25:35.840Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03819r001","statement":[{"text":"The experiments demonstrate that for both peptides an increase in TFE concentration caused a progressive change from a random coil to an α-helical structure (Figure 1).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-14T16:10:04.061Z"}}],"regions_counter":2,"released":"2024_06","sequence":"FLPLIGRVLSGIL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Amphibia","Batrachia","Anura","Neobatrachia","Ranoidea","Ranidae","Rana","Rana"],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"D"}],"Structural state":[{"start":1,"end":13,"type":"D"}]}},{"disprot_id":"DP03820","acc":"P26196","creator":"fkordevani","date":"2022-10-14T09:17:15.986Z","features":{"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":120,"end":286},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":321,"end":429}],"gene3D":[]},"genes":[{"name":{"value":"DDX6"},"synonyms":[{"value":"HLR2"},{"value":"RCK"}]}],"length":483,"name":"Probable ATP-dependent RNA helicase DDX6","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":81,"end":93,"reference_id":"16611246","reference_source":"pmid","reference_html":"Structural insight of human DEAD-box protein rck/p54 into its substrate recognition with conformational changes. <i> Matsui T, Hogetsu K, Usukura J, Sato T, Kumasaka T, Akao Y, Tanaka N. </i> Genes Cells, 2006","date":"2022-10-14T14:03:46.949Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1VEC"}],"region_id":"DP03820r001","statement":[{"text":"No electron density was seen for residues 70-82 on either chain.","type":"Results"},{"text":"The numbering of residues on the paper conflicts with the starting amino acids from Uniprot and the paper has dismissed the first 11 amino acids for some reason. The region the authors are describing corresponds to the 81-93 residues of the Uniprot.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-14T14:10:21.726Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MSTARTENPVIMGLSSQNGQLRGPVKPTGGPGGGGTQTQQQMNQLKNTNTINNGTQQQAQSMTTTIKPGDDWKKTLKLPPKDLRIKTSDVTSTKGNEFEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKKDNIQAMVIVPTRELALQVSQICIQVSKHMGGAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFVQIMEDIILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEINLMEELTLKGVTQYYAYVTERQKVHCLNTLFSRLQINQSIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLAETYLHRIGRSGRFGHLGLAINLITYDDRFNLKSIEEQLGTEIKPIPSNIDKSLYVAEYHSEPVEDEKP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Cancer-related proteins","Condensates-related proteins"],"alphafold_very_low_content":0.15527950310559005,"disorder_content":0.026915113871635612,"disprot_consensus":{"full":[{"start":81,"end":93,"type":"D"}],"Structural state":[{"start":81,"end":93,"type":"D"}]}},{"disprot_id":"DP03821","acc":"Q9UL18","creator":"fkordevani","date":"2022-10-14T12:28:15.598Z","features":{"pfam":[{"id":"PF02170","name":"PAZ domain","start":246,"end":362},{"id":"PF02171","name":"Piwi domain","start":515,"end":815},{"id":"PF08699","name":"Argonaute linker 1 domain","start":174,"end":224},{"id":"PF16486","name":"N-terminal domain of argonaute","start":34,"end":164},{"id":"PF16487","name":"Mid domain of argonaute","start":427,"end":508},{"id":"PF16488","name":"Argonaute linker 2 domain","start":372,"end":418}],"gene3D":[]},"genes":[{"name":{"value":"AGO1"},"synonyms":[{"value":"EIF2C1"}]}],"length":857,"name":"Protein argonaute-1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":21,"reference_id":"23809764","reference_source":"pmid","reference_html":"Eukaryote-specific insertion elements control human ARGONAUTE slicer activity. <i> Nakanishi K, Ascano M, Gogakos T, Ishibe-Murakami S, Serganov AA, Briskin D, Morozov P, Tuschl T, Patel DJ. </i> Cell Rep, 2013","date":"2022-10-14T15:08:29.675Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4KXT"}],"region_id":"DP03821r001","statement":[{"text":"Given that the N-terminal 1–21 aa segment is disordered in our crystal structure, we are unable to comment on the specific function of the N-terminus in target-RNA accommodation and cleavage.","type":"Results"}],"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS000080E2CC_7108"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-14T15:17:31.363Z"}},{"start":113,"end":126,"reference_id":"23809764","reference_source":"pmid","reference_html":"Eukaryote-specific insertion elements control human ARGONAUTE slicer activity. <i> Nakanishi K, Ascano M, Gogakos T, Ishibe-Murakami S, Serganov AA, Briskin D, Morozov P, Tuschl T, Patel DJ. </i> Cell Rep, 2013","date":"2022-10-14T15:09:07.475Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4KXT"}],"region_id":"DP03821r002","statement":[{"text":"The majority of the hAGO1 protein chain could be traced except for amino acid (aa) segments 1–21, 113–126 and 819–834.","type":"Results"}],"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS000080E2CC_7108"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-14T15:17:31.944Z"}},{"start":819,"end":834,"reference_id":"23809764","reference_source":"pmid","reference_html":"Eukaryote-specific insertion elements control human ARGONAUTE slicer activity. <i> Nakanishi K, Ascano M, Gogakos T, Ishibe-Murakami S, Serganov AA, Briskin D, Morozov P, Tuschl T, Patel DJ. </i> Cell Rep, 2013","date":"2022-10-14T15:09:31.705Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4KXT"}],"region_id":"DP03821r003","statement":[{"text":"The majority of the hAGO1 protein chain could be traced except for amino acid (aa) segments 1–21, 113–126 and 819–834.","type":"Results"}],"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS000080E2CC_7108"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-14T15:17:33.130Z"}}],"regions_counter":3,"released":"2023_06","sequence":"MEAGPSGAAAGAYLPPLQQVFQAPRRPGIGTVGKPIKLLANYFEVDIPKIDVYHYEVDIKPDKCPRRVNREVVEYMVQHFKPQIFGDRKPVYDGKKNIYTVTALPIGNERVDFEVTIPGEGKDRIFKVSIKWLAIVSWRMLHEALVSGQIPVPLESVQALDVAMRHLASMRYTPVGRSFFSPPEGYYHPLGGGREVWFGFHQSVRPAMWKMMLNIDVSATAFYKAQPVIEFMCEVLDIRNIDEQPKPLTDSQRVRFTKEIKGLKVEVTHCGQMKRKYRVCNVTRRPASHQTFPLQLESGQTVECTVAQYFKQKYNLQLKYPHLPCLQVGQEQKHTYLPLEVCNIVAGQRCIKKLTDNQTSTMIKATARSAPDRQEEISRLMKNASYNLDPYIQEFGIKVKDDMTEVTGRVLPAPILQYGGRNRAIATPNQGVWDMRGKQFYNGIEIKVWAIACFAPQKQCREEVLKNFTDQLRKISKDAGMPIQGQPCFCKYAQGADSVEPMFRHLKNTYSGLQLIIVILPGKTPVYAEVKRVGDTLLGMATQCVQVKNVVKTSPQTLSNLCLKINVKLGGINNILVPHQRSAVFQQPVIFLGADVTHPPAGDGKKPSITAVVGSMDAHPSRYCATVRVQRPRQEIIEDLSYMVRELLIQFYKSTRFKPTRIIFYRDGVPEGQLPQILHYELLAIRDACIKLEKDYQPGITYIVVQKRHHTRLFCADKNERIGKSGNIPAGTTVDTNITHPFEFDFYLCSHAGIQGTSRPSHYYVLWDDNRFTADELQILTYQLCHTYVRCTRSVSIPAPAYYARLVAFRARYHLVDKEHDSGEGSHISGQSNGRDPQALAKAVQVHQDTLRTMYFA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","RNA-binding proteins"],"alphafold_very_low_content":0.040840140023337225,"disorder_content":0.059509918319719954,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"},{"start":113,"end":126,"type":"D"},{"start":819,"end":834,"type":"D"}],"Structural state":[{"start":1,"end":21,"type":"D"},{"start":113,"end":126,"type":"D"},{"start":819,"end":834,"type":"D"}]}},{"disprot_id":"DP03822","acc":"P78563","creator":"fkordevani","date":"2022-10-14T14:17:32.936Z","features":{"pfam":[{"id":"PF00035","name":"Double-stranded RNA binding motif","start":79,"end":140},{"id":"PF00035","name":"Double-stranded RNA binding motif","start":244,"end":294},{"id":"PF02137","name":"Adenosine-deaminase (editase) domain","start":370,"end":731}],"gene3D":[]},"genes":[{"name":{"value":"ADARB1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:226","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:226"}}]},"synonyms":[{"value":"ADAR2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"32220291","url":"http://www.ncbi.nlm.nih.gov/pubmed/32220291","alternativeUrl":"https://europepmc.org/abstract/MED/32220291"}}]},{"value":"DRADA2"},{"value":"RED1"}]}],"length":741,"name":"Double-stranded RNA-specific editase 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":462,"end":473,"reference_id":"16141067","reference_source":"pmid","reference_html":"Inositol hexakisphosphate is bound in the ADAR2 core and required for RNA editing. <i> Macbeth MR, Schubert HL, Vandemark AP, Lingam AT, Hill CP, Bass BL. </i> Science, 2005","date":"2022-10-14T14:24:02.164Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1ZY7"}],"region_id":"DP03822r001","statement":[{"text":"The refined hADAR2-D model contains residues 306 to 461 and 474 to 700 (462 to 473 are disordered), one zinc ion, and one molecule of inositol hexakisphosphate (IP6).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-14T15:55:48.266Z"}},{"start":299,"end":316,"reference_id":"27065196","reference_source":"pmid","reference_html":"Structures of human ADAR2 bound to dsRNA reveal base-flipping mechanism and basis for site selectivity. <i> Matthews MM, Thomas JM, Zheng Y, Tran K, Phelps KJ, Scott AI, Havel J, Fisher AJ, Beal PA. </i> Nat Struct Mol Biol, 2016","date":"2022-10-14T16:06:37.841Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5ED2"}],"region_id":"DP03822r002","statement":[{"text":"In each of these complexes, the first 17 residues of the deaminase domain (residues 299–316) as well as a C-terminal proline (Pro701) are disordered and were therefore not included in the model.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-14T16:07:08.930Z"}},{"start":454,"end":477,"reference_id":"27065196","reference_source":"pmid","reference_html":"Structures of human ADAR2 bound to dsRNA reveal base-flipping mechanism and basis for site selectivity. <i> Matthews MM, Thomas JM, Zheng Y, Tran K, Phelps KJ, Scott AI, Havel J, Fisher AJ, Beal PA. </i> Nat Struct Mol Biol, 2016","date":"2022-10-14T16:04:54.536Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5ED1"},{"db":"PDB","id":"5ED2"},{"db":"PDB","id":"5HP3"},{"db":"PDB","id":"5HP2"}],"region_id":"DP03822r004","statement":[{"text":"RNA binding leads to an ordering of the 454–477 loop, which was disordered in the RNA-free hADAR2d structure (Fig. 1d, green) (Supplementary Video 2).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-14T16:06:09.088Z"}},{"start":454,"end":477,"reference_id":"27065196","reference_source":"pmid","reference_html":"Structures of human ADAR2 bound to dsRNA reveal base-flipping mechanism and basis for site selectivity. <i> Matthews MM, Thomas JM, Zheng Y, Tran K, Phelps KJ, Scott AI, Havel J, Fisher AJ, Beal PA. </i> Nat Struct Mol Biol, 2016","date":"2022-10-14T16:05:03.460Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5ED1"},{"db":"PDB","id":"5ED2"},{"db":"PDB","id":"5HP3"},{"db":"PDB","id":"5HP2"}],"ec_go":"EXP","region_id":"DP03822r005","statement":[{"text":"RNA binding leads to an ordering of the 454–477 loop, which was disordered in the RNA-free hADAR2d structure(Fig. 1d, green) (Supplementary Video 2).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-14T16:06:40.183Z"}},{"start":215,"end":233,"reference_id":"32597966","reference_source":"pmid","reference_html":"Asymmetric dimerization of adenosine deaminase acting on RNA facilitates substrate recognition. <i> Thuy-Boun AS, Thomas JM, Grajo HL, Palumbo CM, Park S, Nguyen LT, Fisher AJ, Beal PA. </i> Nucleic Acids Res, 2020","date":"2022-10-14T14:45:08.365Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6VFF"}],"region_id":"DP03822r006","statement":[{"text":"The whole of the double stranded RNA binding domain (residues 215–318) of monomer A, as well as the C-terminal residues 700 and 701 were disordered and were therefore not included in the model. The first 20 residues (215–233), 5′ binding loop residues 462–475 and C-terminal proline (701) of monomer B were disordered and were therefore not included in the model.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-14T15:18:56.101Z"}}],"regions_counter":6,"released":"2023_06","sequence":"MDIEDEENMSSSSTDVKENRNLDNVSPKDGSTPGPGEGSQLSNGGGGGPGRKRPLEEGSNGHSKYRLKKRRKTPGPVLPKNALMQLNEIKPGLQYTLLSQTGPVHAPLFVMSVEVNGQVFEGSGPTKKKAKLHAAEKALRSFVQFPNASEAHLAMGRTLSVNTDFTSDQADFPDTLFNGFETPDKAEPPFYVGSNGDDSFSSSGDLSLSASPVPASLAQPPLPVLPPFPPPSGKNPVMILNELRPGLKYDFLSESGESHAKSFVMSVVVDGQFFEGSGRNKKLAKARAAQSALAAIFNLHLDQTPSRQPIPSEGLQLHLPQVLADAVSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSLLRFLYTQLELYLNNKDDQKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEGSRSYTQAGVQWCNHGSLQPRPPGLLSDPSTSTFQGAGTTEPADRHPNRKARGQLRTKIESGEGTIPVRSNASIQTWDGVLQGERLLTMSCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAPNFSVNWTVGDSAIEVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSHLLRSKITKPNVYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEKPTEQDQFSLTP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","RNA-binding proteins"],"alphafold_very_low_content":0.27530364372469635,"disorder_content":0.06612685560053981,"disprot_consensus":{"full":[{"start":215,"end":233,"type":"D"},{"start":299,"end":316,"type":"D"},{"start":454,"end":477,"type":"T"}],"Structural state":[{"start":215,"end":233,"type":"D"},{"start":299,"end":316,"type":"D"},{"start":462,"end":473,"type":"D"}],"Structural transition":[{"start":454,"end":477,"type":"T"}],"Molecular function":[{"start":454,"end":477,"type":"F"}]}},{"disprot_id":"DP03823","acc":"P55011","creator":"jssuarez","date":"2022-10-17T11:08:08.765Z","features":{"pfam":[{"id":"PF00324","name":"Amino acid permease","start":290,"end":792},{"id":"PF03522","name":"Solute carrier family 12","start":801,"end":1212},{"id":"PF08403","name":"Amino acid permease N-terminal","start":202,"end":253}],"gene3D":[]},"genes":[{"name":{"value":"SLC12A2"},"synonyms":[{"value":"NKCC1"}]}],"length":1212,"name":"Solute carrier family 12 member 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":283,"reference_id":"36239040","reference_source":"pmid","reference_html":"Cryo-EM structure of the human NKCC1 transporter reveals mechanisms of ion coupling and specificity. <i> Neumann C, Rosenbaek LL, Flygaard RK, Habeck M, Karlsen JL, Wang Y, Lindorff-Larsen K, Gad HH, Hartmann R, Lyons JA, Fenton RA, Nissen P. </i> EMBO J, 2022","date":"2022-10-18T16:40:55.090Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7ZGO"},{"db":"EMDB","id":"14709"}],"region_id":"DP03823r001","statement":[{"text":"Similar to other NKCC1 cryo-EM structures (Chew et al, 2019; Yang et al, 2020; Zhang et al, 2021), the N-terminal domain could not be identified on the map.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T14:44:19.631Z"}},{"start":1,"end":285,"reference_id":"32081947","reference_source":"pmid","reference_html":"Structure of the human cation-chloride cotransporter NKCC1 determined by single-particle electron cryo-microscopy. <i> Yang X, Wang Q, Cao E. </i> Nat Commun, 2020","date":"2022-10-18T16:40:27.032Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6PZT"},{"db":"EMDB","id":"20537"}],"region_id":"DP03823r002","statement":[{"text":"The final map shows well-resolved densities for the transmembrane domain, large extracellular domains, and loops connecting membrane-spanning helices; however, it lacks interpretable densities for the cytosolic domains, consistent with reference free 2D class averages that show merely a cloud of fuzz densities for the cytosolic domains (Supplementary Fig. 2).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T14:44:09.161Z"}},{"start":1,"end":286,"reference_id":"33597714","reference_source":"pmid","reference_html":"The structural basis of function and regulation of neuronal cotransporters NKCC1 and KCC2. <i> Zhang S, Zhou J, Zhang Y, Liu T, Friedel P, Zhuo W, Somasekharan S, Roy K, Zhang L, Liu Y, Meng X, Deng H, Zeng W, Li G, Forbush B, Yang M. </i> Commun Biol, 2021","date":"2022-10-18T16:05:56.143Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7D10"},{"db":"EMDB","id":"30542"}],"region_id":"DP03823r003","statement":[{"text":"The activating phosphorylation sites of NKCC1 are in the N-terminal domain32—this region is predicted to be largely disordered and indeed the N terminus is absent from both NKCC1 structures40,41.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T14:43:22.727Z"}},{"start":557,"end":572,"reference_id":"33597714","reference_source":"pmid","reference_html":"The structural basis of function and regulation of neuronal cotransporters NKCC1 and KCC2. <i> Zhang S, Zhou J, Zhang Y, Liu T, Friedel P, Zhuo W, Somasekharan S, Roy K, Zhang L, Liu Y, Meng X, Deng H, Zeng W, Li G, Forbush B, Yang M. </i> Commun Biol, 2021","date":"2022-10-18T16:39:49.211Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7D10"},{"db":"EMDB","id":"30542"}],"region_id":"DP03823r004","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T14:43:44.687Z"}}],"regions_counter":4,"released":"2023_06","sequence":"MEPRPTAPSSGAPGLAGVGETPSAAALAAARVELPGTAVPSVPEDAAPASRDGGGVRDEGPAAAGDGLGRPLGPTPSQSRFQVDLVSENAGRAAAAAAAAAAAAAAAGAGAGAKQTPADGEASGESEPAKGSEEAKGRFRVNFVDPAASSSAEDSLSDAAGVGVDGPNVSFQNGGDTVLSEGSSLHSGGGGGSGHHQHYYYDTHTNTYYLRTFGHNTMDAVPRIDHYRHTAAQLGEKLLRPSLAELHDELEKEPFEDGFANGEESTPTRDAVVTYTAESKGVVKFGWIKGVLVRCMLNIWGVMLFIRLSWIVGQAGIGLSVLVIMMATVVTTITGLSTSAIATNGFVRGGGAYYLISRSLGPEFGGAIGLIFAFANAVAVAMYVVGFAETVVELLKEHSILMIDEINDIRIIGAITVVILLGISVAGMEWEAKAQIVLLVILLLAIGDFVIGTFIPLESKKPKGFFGYKSEIFNENFGPDFREEETFFSVFAIFFPAATGILAGANISGDLADPQSAIPKGTLLAILITTLVYVGIAVSVGSCVVRDATGNVNDTIVTELTNCTSAACKLNFDFSSCESSPCSYGLMNNFQVMSMVSGFTPLISAGIFSATLSSALASLVSAPKIFQALCKDNIYPAFQMFAKGYGKNNEPLRGYILTFLIALGFILIAELNVIAPIISNFFLASYALINFSVFHASLAKSPGWRPAFKYYNMWISLLGAILCCIVMFVINWWAALLTYVIVLGLYIYVTYKKPDVNWGSSTQALTYLNALQHSIRLSGVEDHVKNFRPQCLVMTGAPNSRPALLHLVHDFTKNVGLMICGHVHMGPRRQAMKEMSIDQAKYQRWLIKNKMKAFYAPVHADDLREGAQYLMQAAGLGRMKPNTLVLGFKKDWLQADMRDVDMYINLFHDAFDIQYGVVVIRLKEGLDISHLQGQEELLSSQEKSPGTKDVVVSVEYSKKSDLDTSKPLSEKPITHKVEEEDGKTATQPLLKKESKGPIVPLNVADQKLLEASTQFQKKQGKNTIDVWWLFDDGGLTLLIPYLLTTKKKWKDCKIRVFIGGKINRIDHDRRAMATLLSKFRIDFSDIMVLGDINTKPKKENIIAFEEIIEPYRLHEDDKEQDIADKMKEDEPWRITDNELELYKTKTYRQIRLNELLKEHSSTANIIVMSLPVARKGAVSSALYMAWLEALSKDLPPILLVRGNHQSVLTFYS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.2566006600660066,"disorder_content":0.24917491749174916,"disprot_consensus":{"full":[{"start":1,"end":286,"type":"D"},{"start":557,"end":572,"type":"D"}],"Structural state":[{"start":1,"end":286,"type":"D"},{"start":557,"end":572,"type":"D"}]}},{"disprot_id":"DP03824","acc":"A0A0G2KTI4","creator":"jssuarez","date":"2022-10-17T14:07:41.695Z","features":{"pfam":[{"id":"PF00324","name":"Amino acid permease","start":212,"end":717},{"id":"PF03522","name":"Solute carrier family 12","start":726,"end":1136},{"id":"PF08403","name":"Amino acid permease N-terminal","start":124,"end":175}],"gene3D":[]},"genes":[{"name":{"value":"slc12a2","evidences":[{"code":"ECO:0000312","source":{"name":"ZFIN","id":"ZDB-GENE-040625-53","url":"http://zfin.org/cgi-bin/webdriver?MIval=aa-markerview.apg&OID=ZDB-GENE-040625-53"}}]},"synonyms":[{"value":"nkcc1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"19633174","url":"http://www.ncbi.nlm.nih.gov/pubmed/19633174","alternativeUrl":"https://europepmc.org/abstract/MED/19633174"}}]}]}],"length":1136,"name":"Solute carrier family 12 member 2","ncbi_taxon_id":7955,"organism":"Danio rerio","regions":[{"start":1,"end":205,"reference_id":"31367042","reference_source":"pmid","reference_html":"Structure and mechanism of the cation-chloride cotransporter NKCC1. <i> Chew TA, Orlando BJ, Zhang J, Latorraca NR, Wang A, Hollingsworth SA, Chen DH, Dror RO, Liao M, Feng L. </i> Nature, 2019","date":"2022-10-18T16:02:41.472Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"0475"}],"region_id":"DP03824r001","statement":[{"text":"In the 3D reconstruction of full-length NKCC1, the NTD lacked discernible density, indicating disordered structure or conformational flexibility.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T14:45:18.466Z"}},{"start":856,"end":925,"reference_id":"31367042","reference_source":"pmid","reference_html":"Structure and mechanism of the cation-chloride cotransporter NKCC1. <i> Chew TA, Orlando BJ, Zhang J, Latorraca NR, Wang A, Hollingsworth SA, Chen DH, Dror RO, Liao M, Feng L. </i> Nature, 2019","date":"2022-10-18T16:03:57.698Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6NPJ"},{"db":"PDB","id":"6NPL"},{"db":"EMDB","id":"0471"},{"db":"EMDB","id":"0473"}],"region_id":"DP03824r002","statement":[{"text":"The final CTD model contains all residues except an un-structured loop (856–925).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T14:45:45.890Z"}},{"start":856,"end":925,"reference_id":"31367042","reference_source":"pmid","reference_html":"Structure and mechanism of the cation-chloride cotransporter NKCC1. <i> Chew TA, Orlando BJ, Zhang J, Latorraca NR, Wang A, Hollingsworth SA, Chen DH, Dror RO, Liao M, Feng L. </i> Nature, 2019","date":"2022-10-18T16:04:43.200Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6NPJ"},{"db":"PDB","id":"6NPL"},{"db":"EMDB","id":"0473"},{"db":"EMDB","id":"0471"}],"region_id":"DP03824r003","statement":[{"text":"The final CTD model contains all residues except an un-structured loop (856–925).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T14:46:04.554Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MSASPPISAGDYLSAPEPDALKPAGPTPSQSRFQVDLVTESAGDGETTVGFDSSPPEYVAEPPPDGLRDSVSGGEEAKGRFRVVNFAASSPDAAPAETAQNGDTVMSEGSLHSSTGGQQHHHYDTHTNTYYLRTFGHNTIDAVPKIDFYRQTAAPLGEKLIRPTLSELHDELDKEPFEDGFANGEELTPAEESAAKDVSESKGVVKFGWIKGVLVRCMLNIWGVMLFIRMTWIVGQAGIAYSCIIVIMATVVTTITGCSTSAIATNGFVRGGGAYYLISRSLGPEFGGSIGLIFAFANAVAVAMYVVGFAETVVELLMDSGLLMIDQTNDIRVIGTITVILLLGISVAGMEWEAKAQIFLLVILITAIFNYFIGSFIAVDSKKKFGFFSYDAGILAENFGPDFRGQTFFSVFSIFFPAATGILAGANISGDLADPQMAIPKGTLLAILITGLVYVGVAISAGACIVRDATGIESNFTLISNCTDAACKYGYDFSSCRPTVEGEVSSCKFGLHNDFQVMSVVSGFSPLISAGIFSATLSSALASLVSAPKVFQALCKDNIYPGIAIFGKGYGKNNEPLRGYFLTFGIALAFILIAELNVIAPIISNFFLASYALINFSVFHASLANSPGWRPSFKYYNMWASLAGAILCCVVMFIINWWAALLTNVIVLSLYIYVSYKKPDVNWGSSTQALTYHQALTHSLQLCGVADHIKTFRPQCLVMTGAPNSRPAILHLVHAFTKNVGLMLCGHVRISSRRPNFKELNSDMLRYQRWLLNNNSKAFYTCVVAEDLRQGTQYMLQAAGLGRLRPNTLVIGFKNDWRTGDIKEVETYINLIHDAFDFQYGVVILRLREGLDISHIQGQDDSSGMKDVVVSVDISKDSDGDSSKPSSKATSVQNSPAVQKDEDDDGKAHTQPLLKKDKKSPTVPLNVADQRLLDASQQFQQKQGKGTVDVWWLFDDGGLTLLIPYLIANKKKWKDCKIRVFIGGKINRIDHDRRAMATLLSKFRIDFSDITVLGDINTKPKSEGLTEFAEMIEPYKLREDDMEQEAAEKLKSEEPWRITDNELELYKAKGNRQIRLNELLKEHSSTANLIVMSMPLARKGAVSSALYMAWLDTLSKDLPPILLVRGNHQSVLTFYS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Actinopterygii","Neopterygii","Teleostei","Ostariophysi","Cypriniformes","Danionidae","Danioninae","Danio"],"alphafold_very_low_content":0.21038732394366197,"disorder_content":0.2420774647887324,"disprot_consensus":{"full":[{"start":1,"end":205,"type":"D"},{"start":856,"end":925,"type":"D"}],"Structural state":[{"start":1,"end":205,"type":"D"},{"start":856,"end":925,"type":"D"}],"Disorder function":[{"start":856,"end":925,"type":"F"}]}},{"disprot_id":"DP03825","acc":"P15056","creator":"fkordevani","date":"2022-10-17T14:29:13.681Z","features":{"pfam":[{"id":"PF00130","name":"Phorbol esters/diacylglycerol binding domain (C1 domain)","start":235,"end":281},{"id":"PF02196","name":"Raf-like Ras-binding domain","start":157,"end":226},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":457,"end":712}],"gene3D":[]},"genes":[{"name":{"value":"BRAF","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:1097","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:1097"}}]},"synonyms":[{"value":"BRAF1"},{"value":"RAFB1"}]}],"length":766,"name":"Serine/threonine-protein kinase B-raf","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":600,"end":611,"reference_id":"15035987","reference_source":"pmid","reference_html":"Mechanism of activation of the RAF-ERK signaling pathway by oncogenic mutations of B-RAF. <i> Wan PT, Garnett MJ, Roe SM, Lee S, Niculescu-Duvaz D, Good VM, Jones CM, Marshall CJ, Springer CJ, Barford D, Marais R, Cancer Genome Project. </i> Cell, 2004","date":"2022-10-17T14:38:46.637Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001171","ec_ontology":"ECO","ec_name":"crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1UWH"}],"region_id":"DP03825r001","statement":[{"text":"Residues 600–611 of the activation loop are disordered (dashed lines). (Figure 4)","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-18T18:13:47.553Z"}},{"start":601,"end":613,"reference_id":"17145850","reference_source":"pmid","reference_html":"Demonstration of a genetic therapeutic index for tumors expressing oncogenic BRAF by the kinase inhibitor SB-590885. <i> King AJ, Patrick DR, Batorsky RS, Ho ML, Do HT, Zhang SY, Kumar R, Rusnak DW, Takle AK, Wilson DM, Hugger E, Wang L, Karreth F, Lougheed JC, Lee J, Chau D, Stout TJ, May EW, Rominger CM, Schaber MD, Luo L, Lakdawala AS, Adams JL, Contractor RG, Smalley KS, Herlyn M, Morrissey MM, Tuveson DA, Huang PS. </i> Cancer Res, 2006","date":"2022-10-19T08:48:47.348Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2FB8"}],"region_id":"DP03825r003","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-19T13:14:34.184Z"}},{"start":597,"end":613,"reference_id":"18287029","reference_source":"pmid","reference_html":"Discovery of a selective inhibitor of oncogenic B-Raf kinase with potent antimelanoma activity. <i> Tsai J, Lee JT, Wang W, Zhang J, Cho H, Mamo S, Bremer R, Gillette S, Kong J, Haass NK, Sproesser K, Li L, Smalley KS, Fong D, Zhu YL, Marimuthu A, Nguyen H, Lam B, Liu J, Cheung I, Rice J, Suzuki Y, Luu C, Settachatgul C, Shellooe R, Cantwell J, Kim SH, Schlessinger J, Zhang KY, West BL, Powell B, Habets G, Zhang C, Ibrahim PN, Hirth P, Artis DR, Herlyn M, Bollag G. </i> Proc Natl Acad Sci U S A, 2008","date":"2022-10-18T07:47:16.482Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3C4C"}],"region_id":"DP03825r004","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-18T18:05:09.301Z"}},{"start":600,"end":610,"reference_id":"19864136","reference_source":"pmid","reference_html":"Non-hinge-binding pyrazolo[1,5-a]pyrimidines as potent B-Raf kinase inhibitors. <i> Berger DM, Torres N, Dutia M, Powell D, Ciszewski G, Gopalsamy A, Levin JI, Kim KH, Xu W, Wilhelm J, Hu Y, Collins K, Feldberg L, Kim S, Frommer E, Wojciechowicz D, Mallon R. </i> Bioorg Med Chem Lett, 2009","date":"2022-10-18T07:45:58.854Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3II5"}],"region_id":"DP03825r005","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-19T15:11:54.680Z"}},{"start":601,"end":614,"reference_id":"20823850","reference_source":"pmid","reference_html":"Clinical efficacy of a RAF inhibitor needs broad target blockade in BRAF-mutant melanoma. <i> Bollag G, Hirth P, Tsai J, Zhang J, Ibrahim PN, Cho H, Spevak W, Zhang C, Zhang Y, Habets G, Burton EA, Wong B, Tsang G, West BL, Powell B, Shellooe R, Marimuthu A, Nguyen H, Zhang KY, Artis DR, Schlessinger J, Su F, Higgins B, Iyer R, D'Andrea K, Koehler A, Stumm M, Lin PS, Lee RJ, Grippo J, Puzanov I, Kim KB, Ribas A, McArthur GA, Sosman JA, Chapman PB, Flaherty KT, Xu X, Nathanson KL, Nolop K. </i> Nature, 2010","date":"2022-10-19T08:54:06.072Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3OG7"}],"region_id":"DP03825r006","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-19T13:15:27.053Z"}},{"start":601,"end":611,"reference_id":"21251822","reference_source":"pmid","reference_html":"Non-oxime inhibitors of B-Raf(V600E) kinase. <i> Ren L, Wenglowsky S, Miknis G, Rast B, Buckmelter AJ, Ely RJ, Schlachter S, Laird ER, Randolph N, Callejo M, Martinson M, Galbraith S, Brandhuber BJ, Vigers G, Morales T, Voegtli WC, Lyssikatos J. </i> Bioorg Med Chem Lett, 2011","date":"2022-10-19T08:47:18.798Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3PPK"},{"db":"PDB","id":"3PRI"},{"db":"PDB","id":"3PRF"},{"db":"PDB","id":"3PPJ"}],"region_id":"DP03825r007","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-19T13:14:50.752Z"}},{"start":432,"end":447,"reference_id":"21251822","reference_source":"pmid","reference_html":"Non-oxime inhibitors of B-Raf(V600E) kinase. <i> Ren L, Wenglowsky S, Miknis G, Rast B, Buckmelter AJ, Ely RJ, Schlachter S, Laird ER, Randolph N, Callejo M, Martinson M, Galbraith S, Brandhuber BJ, Vigers G, Morales T, Voegtli WC, Lyssikatos J. </i> Bioorg Med Chem Lett, 2011","date":"2022-10-19T08:47:37.936Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3PPJ"},{"db":"PDB","id":"3PRF"},{"db":"PDB","id":"3PPK"},{"db":"PDB","id":"3PRI"}],"region_id":"DP03825r008","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-19T13:14:51.318Z"}},{"start":432,"end":447,"reference_id":"19864136","reference_source":"pmid","reference_html":"Non-hinge-binding pyrazolo[1,5-a]pyrimidines as potent B-Raf kinase inhibitors. <i> Berger DM, Torres N, Dutia M, Powell D, Ciszewski G, Gopalsamy A, Levin JI, Kim KH, Xu W, Wilhelm J, Hu Y, Collins K, Feldberg L, Kim S, Frommer E, Wojciechowicz D, Mallon R. </i> Bioorg Med Chem Lett, 2009","date":"2022-10-19T08:51:27.859Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3II5"}],"region_id":"DP03825r009","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-19T13:14:16.884Z"}}],"regions_counter":9,"released":"2023_06","sequence":"MAALSGGGGGGAEPGQALFNGDMEPEAGAGAGAAASSAADPAIPEEVWNIKQMIKLTQEHIEALLDKFGGEHNPPSIYLEAYEEYTSKLDALQQREQQLLESLGNGTDFSVSSSASMDTVTSSSSSSLSVLPSSLSVFQNPTDVARSNPKSPQKPIVRVFLPNKQRTVVPARCGVTVRDSLKKALMMRGLIPECCAVYRIQDGEKKPIGWDTDISWLTGEELHVEVLENVPLTTHNFVRKTFFTLAFCDFCRKLLFQGFRCQTCGYKFHQRCSTEVPLMCVNYDQLDLLFVSKFFEHHPIPQEEASLAETALTSGSSPSAPASDSIGPQILTSPSPSKSIPIPQPFRPADEDHRNQFGQRDRSSSAPNVHINTIEPVNIDDLIRDQGFRGDGGSTTGLSATPPASLPGSLTNVKALQKSPGPQRERKSSSSSEDRNRMKTLGRRDSSDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARSLPKIHRSASEPSLNRAGFQTEDFSLYACASPKTPIQAGGYGAFPVH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Cancer-related proteins","Condensates-related proteins"],"alphafold_very_low_content":0.3825065274151436,"disorder_content":0.044386422976501305,"disprot_consensus":{"full":[{"start":432,"end":447,"type":"D"},{"start":597,"end":614,"type":"D"}],"Structural state":[{"start":432,"end":447,"type":"D"},{"start":597,"end":614,"type":"D"}]}},{"disprot_id":"DP03826","acc":"Q91V14","creator":"jssuarez","date":"2022-10-17T15:06:41.023Z","features":{"pfam":[{"id":"PF00324","name":"Amino acid permease","start":126,"end":298},{"id":"PF00324","name":"Amino acid permease","start":421,"end":698},{"id":"PF03522","name":"Solute carrier family 12","start":712,"end":830},{"id":"PF03522","name":"Solute carrier family 12","start":843,"end":975},{"id":"PF03522","name":"Solute carrier family 12","start":1070,"end":1138}],"gene3D":[]},"genes":[{"name":{"value":"Slc12a5"},"synonyms":[{"value":"Kcc2"},{"value":"Kiaa1176"}]}],"length":1138,"name":"Solute carrier family 12 member 5","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":1,"end":84,"reference_id":"33597714","reference_source":"pmid","reference_html":"The structural basis of function and regulation of neuronal cotransporters NKCC1 and KCC2. <i> Zhang S, Zhou J, Zhang Y, Liu T, Friedel P, Zhuo W, Somasekharan S, Roy K, Zhang L, Liu Y, Meng X, Deng H, Zeng W, Li G, Forbush B, Yang M. </i> Commun Biol, 2021","date":"2022-10-18T16:42:00.707Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7D14"},{"db":"EMDB","id":"30543"}],"region_id":"DP03826r001","statement":[{"text":"We successfully built most of the mKCC2 structure except for relatively disordered regions in the N terminus and extracellular and intracellular loops (Fig. 1d, e and Supplementary Fig. 3c).","type":"Results"},{"text":"The activating phosphorylation sites of NKCC1 are in the N-terminal domain32—this region is predicted to be largely disordered and indeed the N terminus is absent from both NKCC1 structures40,41.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T15:17:16.216Z"}},{"start":952,"end":1074,"reference_id":"33597714","reference_source":"pmid","reference_html":"The structural basis of function and regulation of neuronal cotransporters NKCC1 and KCC2. <i> Zhang S, Zhou J, Zhang Y, Liu T, Friedel P, Zhuo W, Somasekharan S, Roy K, Zhang L, Liu Y, Meng X, Deng H, Zeng W, Li G, Forbush B, Yang M. </i> Commun Biol, 2021","date":"2022-10-18T16:41:49.304Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7D14"},{"db":"EMDB","id":"30543"}],"region_id":"DP03826r002","statement":[{"text":"The phosphorylation sites in mKCC2 that deactivate the transport protein (T929 and T1029)50 are in a large loop of the C terminus intervening β9 and α7—the ends of this loop are highlighted in Supplementary Fig. 7, but the majority of the loop is unresolved in our mKCC2 structure. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T15:17:16.999Z"}},{"start":1027,"end":1031,"reference_id":"33597714","reference_source":"pmid","reference_html":"The structural basis of function and regulation of neuronal cotransporters NKCC1 and KCC2. <i> Zhang S, Zhou J, Zhang Y, Liu T, Friedel P, Zhuo W, Somasekharan S, Roy K, Zhang L, Liu Y, Meng X, Deng H, Zeng W, Li G, Forbush B, Yang M. </i> Commun Biol, 2021","date":"2022-10-18T16:42:24.102Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7D14"},{"db":"EMDB","id":"30543"}],"region_id":"DP03826r003","statement":[{"text":"In the case of mKCC2, using mass spectrometry we confirmed phosphorylation at the two sites in the C terminus (T929 and T1029) (Supplementary Fig. 6b, c) whose phosphorylation appears necessary and possibly sufficient to inactivate KCC transport function; additional evidence will be seen below from the blocked pore in the mKCC2 structure.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T15:17:15.149Z"}}],"regions_counter":6,"released":"2024_06","sequence":"MSRRFTVTSLPPAASAASADPESRRHSVADPRRLPREDVKGDGNPKESSPFINSTDTEKGREYDGRNMALFEEEMDTSPMVSSLLSGLANYTNLPQGSREHEEAENNEGGKKKPVQAPRMGTFMGVYLPCLQNIFGVILFLRLTWVVGIAGIMESFCMVFICCSCTMLTAISMSAIATNGVVPAGGSYYMISRSLGPEFGGAVGLCFYLGTTFAGAMYILGTIEILLAYLFPAMAIFKAEDASGEAAAMLNNMRVYGTCVLTCMATVVFVGVKYVNKFALVFLGCVILSILAIYAGVIKSAFDPPNFPICLLGNRTLSRHGFDVCAKLAWEGNETVTTRLWGLFCSSRLLNATCDEYFTRNNVTEIQGIPGAASGLIKENLWSSYLTKGVIVERRGMPSVGLADGTPVDMDHPYVFSDMTSYFTLLVGIYFPSVTGIMAGSNRSGDLRDAQKSIPTGTILAIATTSAVYISSVVLFGACIEGVVLRDKFGEAVNGNLVVGTLAWPSPWVIVIGSFFSTCGAGLQSLTGAPRLLQAISRDGIVPFLQVFGHGKANGEPTWALLLTACICEIGILIASLDEVAPILSMFFLMCYMFVNLACAVQTLLRTPNWRPRFRYYHWTLSFLGMSLCLALMFICSWYYALVAMLIAGLIYKYIEYRGAEKEWGDGIRGLSLSAARYALLRLEEGPPHTKNWRPQLLVLVRVDQDQNVVHPQLLSLTSQLKAGKGLTIVGSVLEGTFLDNHPQAQRAEESIRRLMEAEKVKGFCQVVISSNLRDGVSHLIQSGGLGGLQHNTVLVGWPRNWRQKEDHQTWRNFIELVRETTAGHLALLVTKNVSMFPGNPERFSEGSIDVWWIVHDGGMLMLLPFLLRHHKVWRKCKMRIFTVAQMDDNSIQMKKDLTTFLYHLRITAEVEVVEMHESDISAYTYEKTLVMEQRSQILKQMHLTKNEREREIQSITDESRGSIRRKNPANPRLRLNVPEETACDNEEKPEEEVQLIHDQSAPSCPSSSPSPGEEPEGERETDPEVHLTWTKDKSVAEKNKGPSPVSSEGIKDFFSMKPEWENLNQSNVRRMHTAVRLNEVIVNKSRDAKLVLLNMPGPPRNRNGDENYMEFLEVLTEQLDRVMLVRGGGREVITIYS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"alphafold_very_low_content":0.16608084358523725,"disorder_content":0.18189806678383127,"disprot_consensus":{"full":[{"start":1,"end":84,"type":"D"},{"start":952,"end":1074,"type":"D"}],"Structural state":[{"start":1,"end":84,"type":"D"},{"start":952,"end":1074,"type":"D"}],"Disorder function":[{"start":1027,"end":1031,"type":"F"}]}},{"disprot_id":"DP03828","acc":"Q9U4H7","creator":"gbalatti","date":"2022-10-17T21:12:49.793Z","features":{"pfam":[{"id":"PF01777","name":"Ribosomal L27e protein family","start":9,"end":133}],"gene3D":[]},"genes":[{"orfNames":[{"value":"C3747_12g1558c","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"PWV18898.1","url":"https://www.ebi.ac.uk/ena/browser/view/PWV18898.1"}}]},{"value":"C3747_12g1559c","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"PWV18896.1","url":"https://www.ebi.ac.uk/ena/browser/view/PWV18896.1"}}]},{"value":"C4B63_9g2155c","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"PWU99367.1","url":"https://www.ebi.ac.uk/ena/browser/view/PWU99367.1"}}]},{"value":"C4B63_9g2158c","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"PWU99365.1","url":"https://www.ebi.ac.uk/ena/browser/view/PWU99365.1"}}]}]}],"length":133,"name":"60S ribosomal protein L27","ncbi_taxon_id":5693,"organism":"Trypanosoma cruzi","regions":[{"start":87,"end":106,"reference_id":"27791004","reference_source":"pmid","reference_html":"Structure and assembly model for the Trypanosoma cruzi 60S ribosomal subunit. <i> Liu Z, Gutierrez-Vargas C, Wei J, Grassucci RA, Ramesh M, Espina N, Sun M, Tutuncuoglu B, Madison-Antenucci S, Woolford JL, Tong L, Frank J. </i> Proc Natl Acad Sci U S A, 2016","date":"2022-10-19T18:42:01.556Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"5T5H"}],"region_id":"DP03828r001","statement":[{"text":"Structure of residues 87-106 is unresolved in the cryo-EM reconstructions, showing its intrinsic flexibility.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Co-crystallization with other 38 protein sequences"}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Co-crystallization with other 8 ribonucleotide molecules"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-20T14:25:02.127Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MKFLKPGKVVIVTSGRYAGKKAVIVQNTDSKSKERPYGHSLIAGMKKYPKKVVRGMSKRTIQRRSRVGVFLRVVNHKHFLPTRYNMDLSRELRGRINVSDASKKAKSKQLVRKLFQARYNAGSNRWFFQRLRF","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Trypanosoma","Schizotrypanum"],"dataset":["Neglected tropical diseases proteins"],"alphafold_very_low_content":0,"disorder_content":0.15037593984962405,"disprot_consensus":{"full":[{"start":87,"end":106,"type":"D"}],"Structural state":[{"start":87,"end":106,"type":"D"}]}},{"disprot_id":"DP03829","acc":"Q00534","creator":"fkordevani","date":"2022-10-18T07:59:54.563Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":13,"end":300}],"gene3D":[]},"genes":[{"name":{"value":"CDK6"},"synonyms":[{"value":"CDKN6"}]}],"length":326,"name":"Cyclin-dependent kinase 6","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":11,"reference_id":"21038853","reference_source":"pmid","reference_html":"4-(Pyrazol-4-yl)-pyrimidines as selective inhibitors of cyclin-dependent kinase 4/6. <i> Cho YS, Borland M, Brain C, Chen CH, Cheng H, Chopra R, Chung K, Groarke J, He G, Hou Y, Kim S, Kovats S, Lu Y, O'Reilly M, Shen J, Smith T, Trakshel G, Vögtle M, Xu M, Xu M, Sung MJ. </i> J Med Chem, 2010","date":"2022-10-18T08:02:36.501Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3NUP"}],"region_id":"DP03829r001","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-19T15:05:02.812Z"}},{"start":46,"end":55,"reference_id":"21038853","reference_source":"pmid","reference_html":"4-(Pyrazol-4-yl)-pyrimidines as selective inhibitors of cyclin-dependent kinase 4/6. <i> Cho YS, Borland M, Brain C, Chen CH, Cheng H, Chopra R, Chung K, Groarke J, He G, Hou Y, Kim S, Kovats S, Lu Y, O'Reilly M, Shen J, Smith T, Trakshel G, Vögtle M, Xu M, Xu M, Sung MJ. </i> J Med Chem, 2010","date":"2022-10-18T08:03:02.227Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3NUP"}],"region_id":"DP03829r002","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-19T15:05:29.239Z"}},{"start":167,"end":180,"reference_id":"21038853","reference_source":"pmid","reference_html":"4-(Pyrazol-4-yl)-pyrimidines as selective inhibitors of cyclin-dependent kinase 4/6. <i> Cho YS, Borland M, Brain C, Chen CH, Cheng H, Chopra R, Chung K, Groarke J, He G, Hou Y, Kim S, Kovats S, Lu Y, O'Reilly M, Shen J, Smith T, Trakshel G, Vögtle M, Xu M, Xu M, Sung MJ. </i> J Med Chem, 2010","date":"2022-10-19T15:36:23.365Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3NUP"},{"db":"PDB","id":"3NUX"}],"region_id":"DP03829r003","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-19T15:45:16.635Z"}},{"start":45,"end":56,"reference_id":"24900493","reference_source":"pmid","reference_html":"Fragment-Based Discovery of 7-Azabenzimidazoles as Potent, Highly Selective, and Orally Active CDK4/6 Inhibitors. <i> Cho YS, Angove H, Brain C, Chen CH, Cheng H, Cheng R, Chopra R, Chung K, Congreve M, Dagostin C, Davis DJ, Feltell R, Giraldes J, Hiscock SD, Kim S, Kovats S, Lagu B, Lewry K, Loo A, Lu Y, Luzzio M, Maniara W, McMenamin R, Mortenson PN, Benning R, O'Reilly M, Rees DC, Shen J, Smith T, Wang Y, Williams G, Woolford AJ, Wrona W, Xu M, Yang F, Howard S. </i> ACS Med Chem Lett, 2012","date":"2022-10-19T14:19:35.202Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4AUA"},{"db":"PDB","id":"4EZ5"}],"region_id":"DP03829r004","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-19T14:41:52.370Z"}},{"start":168,"end":181,"reference_id":"24900493","reference_source":"pmid","reference_html":"Fragment-Based Discovery of 7-Azabenzimidazoles as Potent, Highly Selective, and Orally Active CDK4/6 Inhibitors. <i> Cho YS, Angove H, Brain C, Chen CH, Cheng H, Cheng R, Chopra R, Chung K, Congreve M, Dagostin C, Davis DJ, Feltell R, Giraldes J, Hiscock SD, Kim S, Kovats S, Lagu B, Lewry K, Loo A, Lu Y, Luzzio M, Maniara W, McMenamin R, Mortenson PN, Benning R, O'Reilly M, Rees DC, Shen J, Smith T, Wang Y, Williams G, Woolford AJ, Wrona W, Xu M, Yang F, Howard S. </i> ACS Med Chem Lett, 2012","date":"2022-10-19T14:19:47.285Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4AUA"},{"db":"PDB","id":"4EZ5"}],"region_id":"DP03829r005","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-19T14:41:49.633Z"}},{"start":1,"end":10,"reference_id":"24900493","reference_source":"pmid","reference_html":"Fragment-Based Discovery of 7-Azabenzimidazoles as Potent, Highly Selective, and Orally Active CDK4/6 Inhibitors. <i> Cho YS, Angove H, Brain C, Chen CH, Cheng H, Cheng R, Chopra R, Chung K, Congreve M, Dagostin C, Davis DJ, Feltell R, Giraldes J, Hiscock SD, Kim S, Kovats S, Lagu B, Lewry K, Loo A, Lu Y, Luzzio M, Maniara W, McMenamin R, Mortenson PN, Benning R, O'Reilly M, Rees DC, Shen J, Smith T, Wang Y, Williams G, Woolford AJ, Wrona W, Xu M, Yang F, Howard S. </i> ACS Med Chem Lett, 2012","date":"2022-10-19T14:23:26.903Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4EZ5"},{"db":"PDB","id":"4AUA"}],"region_id":"DP03829r006","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-19T14:41:45.918Z"}}],"regions_counter":6,"released":"2023_06","sequence":"MEKDGLCRADQQYECVAEIGEGAYGKVFKARDLKNGGRFVALKRVRVQTGEEGMPLSTIREVAVLRHLETFEHPNVVRLFDVCTVSRTDRETKLTLVFEHVDQDLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDVIGLPGEEDWPRDVALPRQAFHSKSAQPIEKFVTDIDELGKDLLLKCLTFNPAKRISAYSALSHPYFQDLERCKENLDSHLPPSQNTSELNTA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Cancer-related proteins"],"alphafold_very_low_content":0.09815950920245399,"disorder_content":0.1165644171779141,"disprot_consensus":{"full":[{"start":1,"end":11,"type":"D"},{"start":45,"end":56,"type":"D"},{"start":167,"end":181,"type":"D"}],"Structural state":[{"start":1,"end":11,"type":"D"},{"start":45,"end":56,"type":"D"},{"start":167,"end":181,"type":"D"}]}},{"disprot_id":"DP03830","acc":"Q9Y5P4","creator":"fkordevani","date":"2022-10-18T08:15:10.673Z","features":{"pfam":[{"id":"PF00169","name":"PH domain","start":24,"end":115},{"id":"PF01852","name":"START domain","start":415,"end":618}],"gene3D":[]},"genes":[{"name":{"value":"CERT1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:2205","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:2205"}}]},"synonyms":[{"value":"CERT"},{"value":"COL4A3BP","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:2205","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:2205"}}]},{"value":"STARD11"}]}],"length":624,"name":"Ceramide transfer protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":344,"end":361,"reference_id":"18184806","reference_source":"pmid","reference_html":"Structural basis for specific lipid recognition by CERT responsible for nonvesicular trafficking of ceramide. <i> Kudo N, Kumagai K, Tomishige N, Yamaji T, Wakatsuki S, Nishijima M, Hanada K, Kato R. </i> Proc Natl Acad Sci U S A, 2008","date":"2022-10-19T15:38:58.366Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2E3M"}],"region_id":"DP03830r001","statement":[{"text":"Electron density for the first 12 or 13 residues was not observed in all cases, because of disorder.","type":"Results"},{"text":"According to the PDB, residues 1 to 18 (corresponding to 344 to 361 on the protein sequence) are not mapped, hence, disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-19T15:45:48.881Z"}},{"start":344,"end":362,"reference_id":"18184806","reference_source":"pmid","reference_html":"Structural basis for specific lipid recognition by CERT responsible for nonvesicular trafficking of ceramide. <i> Kudo N, Kumagai K, Tomishige N, Yamaji T, Wakatsuki S, Nishijima M, Hanada K, Kato R. </i> Proc Natl Acad Sci U S A, 2008","date":"2022-10-19T15:40:51.268Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2Z9Y"},{"db":"PDB","id":"2E3P"},{"db":"PDB","id":"2E3N"},{"db":"PDB","id":"2E3O"},{"db":"PDB","id":"2E3R"},{"db":"PDB","id":"2E3S"},{"db":"PDB","id":"2E3Q"},{"db":"PDB","id":"2Z9Z"}],"region_id":"DP03830r002","statement":[{"text":"Electron density for the first 12 or 13 residues was not observed in all cases, because of disorder.","type":"Results"},{"text":"According to the PDB, residues 1 to 19 (corresponding to 344 to 362 on the protein sequence) are not mapped, hence, disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-19T15:46:40.865Z"}},{"start":187,"end":218,"reference_id":"36976648","reference_source":"pmid","reference_html":"CERT1 mutations perturb human development by disrupting sphingolipid homeostasis. <i> Gehin C, Lone MA, Lee W, Capolupo L, Ho S, Adeyemi AM, Gerkes EH, Stegmann AP, López-Martín E, Bermejo-Sánchez E, Martínez-Delgado B, Zweier C, Kraus C, Popp B, Strehlow V, Gräfe D, Knerr I, Jones ER, Zamuner S, Abriata LA, Kunnathully V, Moeller BE, Vocat A, Rommelaere S, Bocquete JP, Ruchti E, Limoni G, Van Campenhoudt M, Bourgeat S, Henklein P, Gilissen C, van Bon BW, Pfundt R, Willemsen MH, Schieving JH, Leonardi E, Soli F, Murgia A, Guo H, Zhang Q, Xia K, Fagerberg CR, Beier CP, Larsen MJ, Valenzuela I, Fernández-Álvarez P, Xiong S, Śmigiel R, López-González V, Armengol L, Morleo M, Selicorni A, Torella A, Blyth M, Cooper NS, Wilson V, Oegema R, Herenger Y, Garde A, Bruel AL, Tran Mau-Them F, Maddocks AB, Bain JM, Bhat MA, Costain G, Kannu P, Marwaha A, Champaigne NL, Friez MJ, Richardson EB, Gowda VK, Srinivasan VM, Gupta Y, Lim TY, Sanna-Cherchi S, Lemaitre B, Yamaji T, Hanada K, Burke JE, Jakšić AM, McCabe BD, De Los Rios P, Hornemann T, D'Angelo G, Gennarino VA. </i> J Clin Invest, 2023","date":"2023-09-07T11:27:05.294Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7.5},{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":20}],"region_id":"DP03830r003","sequence_construct":"MSDNQSWNSSGSEEDPETESGPPVERCGVLSKWTNYIHGWQDRWVVLKNNALSYYKSEDETEYGCRGSICLSKAVITPHDFDECRFDISVNDSVWYLRAQDPDHRQQWIDAIEQHKTESGYGSESSLRRHGSMVSLVSGASGYSATSTSSFKKGHSLREKLAEMETFRDILCRQVDTLQKYFDACADAVSKDELQRDKVVEDDEDDFPTTRSDGDFLHSTNGNKEKLFPHVTPKGINGIDFKGEAITFKATTAGILATLSHCIELMVKREDSWQKRLDKETEKKRRTEEAYKNAMTELKKKSHFGGPDYEEGPNSLINEEEFFDAVEAALDRQDKIEEQSQSEKVRLHWPTSLPSGDAFSSVGTHRFVQKPYSRSSSMSSIDLVSASDDVHRFSSQVEEMVQNHMTYSLQDVGGDANWQLVVEEGEMKVYRREVEENGIVLDPLKATHAVKGVTGHEVCNYFWNVDVRNDWETTIENFHVVETLADNAIIIYQTHKRVWPASQRDVLYLSVIRKIPALTENDPETWIVCNFSVDHDSAPLNNRCVRAKINVAMICQTLVSPPEGNQEISRDNILCKITYVANVNPGGWAPASVLRAVAKREYPKFLKRFTSYVQEKTAGKPILF","statement":[{"text":"The areas from aa 187 to 218 and from aa 300 to 381 were highly accessible to solvent and therefore probably contained no or a very dynamic secondary structure.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-01-29T14:50:40.367Z"}},{"start":300,"end":381,"reference_id":"36976648","reference_source":"pmid","reference_html":"CERT1 mutations perturb human development by disrupting sphingolipid homeostasis. <i> Gehin C, Lone MA, Lee W, Capolupo L, Ho S, Adeyemi AM, Gerkes EH, Stegmann AP, López-Martín E, Bermejo-Sánchez E, Martínez-Delgado B, Zweier C, Kraus C, Popp B, Strehlow V, Gräfe D, Knerr I, Jones ER, Zamuner S, Abriata LA, Kunnathully V, Moeller BE, Vocat A, Rommelaere S, Bocquete JP, Ruchti E, Limoni G, Van Campenhoudt M, Bourgeat S, Henklein P, Gilissen C, van Bon BW, Pfundt R, Willemsen MH, Schieving JH, Leonardi E, Soli F, Murgia A, Guo H, Zhang Q, Xia K, Fagerberg CR, Beier CP, Larsen MJ, Valenzuela I, Fernández-Álvarez P, Xiong S, Śmigiel R, López-González V, Armengol L, Morleo M, Selicorni A, Torella A, Blyth M, Cooper NS, Wilson V, Oegema R, Herenger Y, Garde A, Bruel AL, Tran Mau-Them F, Maddocks AB, Bain JM, Bhat MA, Costain G, Kannu P, Marwaha A, Champaigne NL, Friez MJ, Richardson EB, Gowda VK, Srinivasan VM, Gupta Y, Lim TY, Sanna-Cherchi S, Lemaitre B, Yamaji T, Hanada K, Burke JE, Jakšić AM, McCabe BD, De Los Rios P, Hornemann T, D'Angelo G, Gennarino VA. </i> J Clin Invest, 2023","date":"2023-09-07T11:27:36.426Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7.5},{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":20}],"region_id":"DP03830r004","sequence_construct":"MSDNQSWNSSGSEEDPETESGPPVERCGVLSKWTNYIHGWQDRWVVLKNNALSYYKSEDETEYGCRGSICLSKAVITPHDFDECRFDISVNDSVWYLRAQDPDHRQQWIDAIEQHKTESGYGSESSLRRHGSMVSLVSGASGYSATSTSSFKKGHSLREKLAEMETFRDILCRQVDTLQKYFDACADAVSKDELQRDKVVEDDEDDFPTTRSDGDFLHSTNGNKEKLFPHVTPKGINGIDFKGEAITFKATTAGILATLSHCIELMVKREDSWQKRLDKETEKKRRTEEAYKNAMTELKKKSHFGGPDYEEGPNSLINEEEFFDAVEAALDRQDKIEEQSQSEKVRLHWPTSLPSGDAFSSVGTHRFVQKPYSRSSSMSSIDLVSASDDVHRFSSQVEEMVQNHMTYSLQDVGGDANWQLVVEEGEMKVYRREVEENGIVLDPLKATHAVKGVTGHEVCNYFWNVDVRNDWETTIENFHVVETLADNAIIIYQTHKRVWPASQRDVLYLSVIRKIPALTENDPETWIVCNFSVDHDSAPLNNRCVRAKINVAMICQTLVSPPEGNQEISRDNILCKITYVANVNPGGWAPASVLRAVAKREYPKFLKRFTSYVQEKTAGKPILF","statement":[{"text":"The areas from aa 187 to 218 and from aa 300 to 381 were highly accessible to solvent and therefore probably contained no or a very dynamic secondary structure.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-01-29T14:50:40.641Z"}}],"regions_counter":4,"released":"2023_06","sequence":"MSDNQSWNSSGSEEDPETESGPPVERCGVLSKWTNYIHGWQDRWVVLKNNALSYYKSEDETEYGCRGSICLSKAVITPHDFDECRFDISVNDSVWYLRAQDPDHRQQWIDAIEQHKTESGYGSESSLRRHGSMVSLVSGASGYSATSTSSFKKGHSLREKLAEMETFRDILCRQVDTLQKYFDACADAVSKDELQRDKVVEDDEDDFPTTRSDGDFLHSTNGNKEKLFPHVTPKGINGIDFKGEAITFKATTAGILATLSHCIELMVKREDSWQKRLDKETEKKRRTEEAYKNAMTELKKKSHFGGPDYEEGPNSLINEEEFFDAVEAALDRQDKIEEQSQSEKVRLHWPTSLPSGDAFSSVGTHRFVQKPYSRSSSMSSIDLVSASDDVHRFSSQVEEMVQNHMTYSLQDVGGDANWQLVVEEGEMKVYRREVEENGIVLDPLKATHAVKGVTGHEVCNYFWNVDVRNDWETTIENFHVVETLADNAIIIYQTHKRVWPASQRDVLYLSVIRKIPALTENDPETWIVCNFSVDHDSAPLNNRCVRAKINVAMICQTLVSPPEGNQEISRDNILCKITYVANVNPGGWAPASVLRAVAKREYPKFLKRFTSYVQEKTAGKPILF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.20993589743589744,"disorder_content":0.18269230769230768,"disprot_consensus":{"full":[{"start":187,"end":218,"type":"D"},{"start":300,"end":381,"type":"D"}],"Structural state":[{"start":187,"end":218,"type":"D"},{"start":300,"end":381,"type":"D"}]}},{"disprot_id":"DP03832","acc":"Q16740","creator":"fkordevani","date":"2022-10-18T12:12:08.230Z","features":{"pfam":[{"id":"PF00574","name":"Clp protease","start":68,"end":246}],"gene3D":[]},"genes":[{"name":{"value":"CLPP"}}],"length":277,"name":"ATP-dependent Clp protease proteolytic subunit, mitochondrial","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":57,"end":72,"reference_id":"30129683","reference_source":"pmid","reference_html":"Selective Activation of Human Caseinolytic Protease P (ClpP). <i> Stahl M, Korotkov VS, Balogh D, Kick LM, Gersch M, Pahl A, Kielkowski P, Richter K, Schneider S, Sieber SA. </i> Angew Chem Int Ed Engl, 2018","date":"2022-10-18T12:21:52.429Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6H23"}],"region_id":"DP03832r001","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-19T16:08:12.482Z"}},{"start":250,"end":277,"reference_id":"30129683","reference_source":"pmid","reference_html":"Selective Activation of Human Caseinolytic Protease P (ClpP). <i> Stahl M, Korotkov VS, Balogh D, Kick LM, Gersch M, Pahl A, Kielkowski P, Richter K, Schneider S, Sieber SA. </i> Angew Chem Int Ed Engl, 2018","date":"2022-10-18T12:23:57.447Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6H23"}],"region_id":"DP03832r002","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-19T16:08:22.476Z"}}],"regions_counter":3,"released":"2023_06","sequence":"MWPGILVGGARVASCRYPALGPRLAAHFPAQRPPQRTLQNGLALQRCLHATATRALPLIPIVVEQTGRGERAYDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNKKPIHMYINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAASMGSLLLAAGTPGMRHSLPNSRIMIHQPSGGARGQATDIAIQAEEIMKLKKQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILDKVLVHPPQDGEDEPTLVQKEPVEAAPAAEPVPAST","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.1588447653429603,"disorder_content":0.1588447653429603,"disprot_consensus":{"full":[{"start":57,"end":72,"type":"D"},{"start":250,"end":277,"type":"D"}],"Structural state":[{"start":57,"end":72,"type":"D"},{"start":250,"end":277,"type":"D"}]}},{"disprot_id":"DP03833","acc":"Q9H9E3","creator":"fkordevani","date":"2022-10-18T12:27:56.399Z","features":{"pfam":[{"id":"PF08318","name":"COG4 transport protein, middle alpha-helical bundle","start":217,"end":497},{"id":"PF20662","name":"Conserved oligomeric Golgi complex subunit 4, C-terminal","start":544,"end":767},{"id":"PF20663","name":"Conserved oligomeric Golgi complex subunit 4, N-terminal","start":76,"end":170}],"gene3D":[]},"genes":[{"name":{"value":"COG4"}}],"length":785,"name":"Conserved oligomeric Golgi complex subunit 4","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":525,"end":536,"reference_id":"19651599","reference_source":"pmid","reference_html":"Structural basis for a human glycosylation disorder caused by mutation of the COG4 gene. <i> Richardson BC, Smith RD, Ungar D, Nakamura A, Jeffrey PD, Lupashin VV, Hughson FM. </i> Proc Natl Acad Sci U S A, 2009","date":"2022-10-20T14:09:00.988Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3HR0"}],"region_id":"DP03833r001","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"},{"text":"The final model includes residues 536–785 of one monomer and 537–785 of the other monomer, with the remaining N-terminal residues, for which no interpretable electron density was observed, likely disordered in the crystals.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-20T15:05:04.010Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MADLDSPPKLSGVQQPSEGVGGGRCSEISAELIRSLTELQELEAVYERLCGEEKVVERELDALLEQQNTIESKMVTLHRMGPNLQLIEGDAKQLAGMITFTCNLAENVSSKVRQLDLAKNRLYQAIQRADDILDLKFCMDGVQTALRSEDYEQAAAHTHRYLCLDKSVIELSRQGKEGSMIDANLKLLQEAEQRLKAIVAEKFAIATKEGDLPQVERFFKIFPLLGLHEEGLRKFSEYLCKQVASKAEENLLMVLGTDMSDRRAAVIFADTLTLLFEGIARIVETHQPIVETYYGPGRLYTLIKYLQVECDRQVEKVVDKFIKQRDYHQQFRHVQNNLMRNSTTEKIEPRELDPILTEVTLMNARSELYLRFLKKRISSDFEVGDSMASEEVKQEHQKCLDKLLNNCLLSCTMQELIGLYVTMEEYFMRETVNKAVALDTYEKGQLTSSMVDDVFYIVKKCIGRALSSSSIDCLCAMINLATTELESDFRDVLCNKLRMGFPATTFQDIQRGVTSAVNIMHSSLQQGKFDTKGIESTDEAKMSFLVTLNNVEVCSENISTLKKTLESDCTKLFSQGIGGEQAQAKFDSCLSDLAAVSNKFRDLLQEGLTELNSTAIKPQVQPWINSFFSVSHNIEEEEFNDYEANDPWVQQFILNLEQQMAEFKASLSPVIYDSLTGLMTSLVAVELEKVVLKSTFNRLGGLQFDKELRSLIAYLTTVTTWTIRDKFARLSQMATILNLERVTEILDYWGPNSGPLTWRLTPAEVRQVLALRIDFRSEDIKRLRL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.06751592356687898,"disorder_content":0.015286624203821656,"disprot_consensus":{"full":[{"start":525,"end":536,"type":"D"}],"Structural state":[{"start":525,"end":536,"type":"D"}]}},{"disprot_id":"DP03834","acc":"A4D126","creator":"fkordevani","date":"2022-10-18T12:33:51.726Z","features":{"pfam":[{"id":"PF01128","name":"2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase","start":47,"end":278},{"id":"PF18706","name":"D-ribitol-5-phosphate cytidylyltransferase C-terminal domain","start":283,"end":430}],"gene3D":[]},"genes":[{"name":{"value":"CRPPA","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:37276","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:37276"}}]},"synonyms":[{"value":"ISPD","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:37276","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:37276"}}]}]}],"length":451,"name":"D-ribitol-5-phosphate cytidylyltransferase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":319,"end":334,"reference_id":"26687144","reference_source":"pmid","reference_html":"Human ISPD Is a Cytidyltransferase Required for Dystroglycan O-Mannosylation. <i> Riemersma M, Froese DS, van Tol W, Engelke UF, Kopec J, van Scherpenzeel M, Ashikov A, Krojer T, von Delft F, Tessari M, Buczkowska A, Swiezewska E, Jae LT, Brummelkamp TR, Manya H, Endo T, van Bokhoven H, Yue WW, Lefeber DJ. </i> Chem Biol, 2015","date":"2023-05-04T08:12:11.564Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4CVH"}],"region_id":"DP03834r001","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"},{"text":"Residues 55–60, 319–334, and 345–347 are disordered in the electron density map, and not modeled in the final model.","type":"Methods"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:12375"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T13:18:36.460Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MEAGPPGSARPAEPGPCLSGQRGADHTASASLQSVAGTEPGRHPQAVAAVLPAGGCGERMGVPTPKQFCPILERPLISYTLQALERVCWIKDIVVAVTGENMEVMKSIIQKYQHKRISLVEAGVTRHRSIFNGLKALAEDQINSKLSKPEVVIIHDAVRPFVEEGVLLKVVTAAKEHGAAGAIRPLVSTVVSPSADGCLDYSLERARHRASEMPQAFLFDVIYEAYQQCSDYDLEFGTECLQLALKYCCTKAKLVEGSPDLWKVTYKRDLYAAESIIKERISQEICVVMDTEEDNKHVGHLLEEVLKSELNHVKVTSEALGHAGRHLQQIILDQCYNFVCVNVTTSDFQETQKLLSMLEESSLCILYPVVVVSVHFLDFKLVPPSQKMENLMQIREFAKEVKERNILLYGLLISYPQDDQKLQESLRQGAIIIASLIKERNSGLIGQLLIA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.09090909090909091,"disorder_content":0.03547671840354767,"disprot_consensus":{"full":[{"start":319,"end":334,"type":"D"}],"Structural state":[{"start":319,"end":334,"type":"D"}]}},{"disprot_id":"DP03835","acc":"P14868","creator":"fkordevani","date":"2022-10-18T12:41:38.891Z","features":{"pfam":[{"id":"PF00152","name":"tRNA synthetases class II (D, K and N)","start":175,"end":495},{"id":"PF01336","name":"OB-fold nucleic acid binding domain","start":60,"end":145}],"gene3D":[]},"genes":[{"name":{"value":"DARS1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:2678","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:2678"}}]},"synonyms":[{"value":"DARS"}],"orfNames":[{"value":"PIG40"}]}],"length":501,"name":"Aspartate--tRNA ligase, cytoplasmic","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":224,"end":247,"reference_id":"23609930","reference_source":"pmid","reference_html":"Crystal structure of human cytosolic aspartyl-tRNA synthetase, a component of multi-tRNA synthetase complex. <i> Kim KR, Park SH, Kim HS, Rhee KH, Kim BG, Kim DG, Park MS, Kim HJ, Kim S, Han BW. </i> Proteins, 2013","date":"2022-10-20T09:10:19.015Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4J15"}],"region_id":"DP03835r001","statement":[{"text":"In addition, residues 224–247 in the flipping loop and residues 273–282 in the Motif 2 could not be observed in our crystal structure [Fig. 1(B)]. These regions are known to be dynamic without its cognate tRNA and recognize its tRNA in an induced-fit manner.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-20T15:09:15.283Z"}},{"start":1,"end":20,"reference_id":"23609930","reference_source":"pmid","reference_html":"Crystal structure of human cytosolic aspartyl-tRNA synthetase, a component of multi-tRNA synthetase complex. <i> Kim KR, Park SH, Kim HS, Rhee KH, Kim BG, Kim DG, Park MS, Kim HJ, Kim S, Han BW. </i> Proteins, 2013","date":"2022-10-20T08:54:24.971Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4J15"}],"region_id":"DP03835r002","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"},{"text":"In our crystal structure, the C-terminal end of the α-helix in the N-terminal extension was observed, comprising Lys26, Glu27, and Arg28 although the N-terminal region was less-ordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-20T15:13:07.480Z"}},{"start":273,"end":282,"reference_id":"23609930","reference_source":"pmid","reference_html":"Crystal structure of human cytosolic aspartyl-tRNA synthetase, a component of multi-tRNA synthetase complex. <i> Kim KR, Park SH, Kim HS, Rhee KH, Kim BG, Kim DG, Park MS, Kim HJ, Kim S, Han BW. </i> Proteins, 2013","date":"2022-10-20T09:14:21.616Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4J15"}],"region_id":"DP03835r003","statement":[{"text":"In addition, residues 224–247 in the flipping loop and residues 273–282 in the Motif 2 could not be observed in our crystal structure [Fig. 1(B)]. These regions are known to be dynamic without its cognate tRNA and recognize its tRNA in an induced-fit manner.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-20T15:09:38.294Z"}},{"start":163,"end":172,"reference_id":"23609930","reference_source":"pmid","reference_html":"Crystal structure of human cytosolic aspartyl-tRNA synthetase, a component of multi-tRNA synthetase complex. <i> Kim KR, Park SH, Kim HS, Rhee KH, Kim BG, Kim DG, Park MS, Kim HJ, Kim S, Han BW. </i> Proteins, 2013","date":"2022-10-20T09:14:34.904Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4J15"}],"region_id":"DP03835r004","statement":[{"text":"The hinge region (residues, 156–188) plays an essential role in the connection of the anticodon-binding domain and the catalytic domain. In the middle of the hinge region, residues 163–172 could not be modeled owing to the lack of the electron density and the disordered residues are considered as a part of binding region to the ribose-phosphate backbone in the D-stem of tRNAAsp, compared with the known S. cerevisiae DRS–tRNAAsp complex structure.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-20T15:10:12.396Z"}},{"start":163,"end":172,"reference_id":"23609930","reference_source":"pmid","reference_html":"Crystal structure of human cytosolic aspartyl-tRNA synthetase, a component of multi-tRNA synthetase complex. <i> Kim KR, Park SH, Kim HS, Rhee KH, Kim BG, Kim DG, Park MS, Kim HJ, Kim S, Han BW. </i> Proteins, 2013","date":"2022-10-20T09:15:24.491Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4J15"}],"region_id":"DP03835r005","statement":[{"text":"In addition, residues 224–247 in the flipping loop and residues 273–282 in the Motif 2 could not be observed in our crystal structure [Fig. 1(B)]. These regions are known to be dynamic without its cognate tRNA and recognize its tRNA in an induced-fit manner.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-20T15:10:21.318Z"}},{"start":237,"end":241,"reference_id":"23609930","reference_source":"pmid","reference_html":"Crystal structure of human cytosolic aspartyl-tRNA synthetase, a component of multi-tRNA synthetase complex. <i> Kim KR, Park SH, Kim HS, Rhee KH, Kim BG, Kim DG, Park MS, Kim HJ, Kim S, Han BW. </i> Proteins, 2013","date":"2022-10-20T15:49:30.077Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001582","ec_ontology":"ECO","ec_name":"liquid chromatography coupled with tandem mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4J15"}],"region_id":"DP03835r006","statement":[{"text":"Our liquid chromatography tandem mass spectrometry (MS) analysis revealed two phosphorylation sites (Tyr239 and Ser249) and six acetylation sites (Lys55, 110, 213, 241, 330, and 453), respectively.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-20T18:14:06.561Z"}},{"start":239,"end":243,"reference_id":"23609930","reference_source":"pmid","reference_html":"Crystal structure of human cytosolic aspartyl-tRNA synthetase, a component of multi-tRNA synthetase complex. <i> Kim KR, Park SH, Kim HS, Rhee KH, Kim BG, Kim DG, Park MS, Kim HJ, Kim S, Han BW. </i> Proteins, 2013","date":"2022-10-20T15:49:44.925Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000039","term_name":"acetylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001582","ec_ontology":"ECO","ec_name":"liquid chromatography coupled with tandem mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4J15"}],"region_id":"DP03835r007","statement":[{"text":"Our liquid chromatography tandem mass spectrometry (MS) analysis revealed two phosphorylation sites (Tyr239 and Ser249) and six acetylation sites (Lys55, 110, 213, 241, 330, and 453), respectively.","type":"Results"},{"text":"For instance, although Lys241 was identified with its acetylation modification in our analysis, collected six independent MS analysis data of ubiquitin branch motif (K-e-GG) immunoaffinity beads purification studies showed that Lys241 is also modified with ubiquitin.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-20T18:14:05.499Z"}}],"regions_counter":7,"released":"2023_06","sequence":"MPSASASRKSQEKPREIMDAAEDYAKERYGISSMIQSQEKPDRVLVRVRDLTIQKADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMVKFAANINKESIVDVEGVVRKVNQKIGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAVRPEAEGEEEGRATVNQDTRLDNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICADFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVMEEIADTMVQIFKGLQERFQTEIQTVNKQFPCEPFKFLEPTLRLEYCEALAMLREAGVEMGDEDDLSTPNEKLLGHLVKEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.03992015968063872,"disorder_content":0.1277445109780439,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"D"},{"start":163,"end":172,"type":"D"},{"start":224,"end":247,"type":"D"},{"start":273,"end":282,"type":"D"}],"Structural state":[{"start":1,"end":20,"type":"D"},{"start":163,"end":172,"type":"D"},{"start":224,"end":247,"type":"D"},{"start":273,"end":282,"type":"D"}],"Disorder function":[{"start":163,"end":172,"type":"F"},{"start":237,"end":243,"type":"F"}]}},{"disprot_id":"DP03836","acc":"Q6PI48","creator":"fkordevani","date":"2022-10-18T12:45:24.668Z","features":{"pfam":[{"id":"PF00152","name":"tRNA synthetases class II (D, K and N)","start":167,"end":356},{"id":"PF00152","name":"tRNA synthetases class II (D, K and N)","start":453,"end":606},{"id":"PF01336","name":"OB-fold nucleic acid binding domain","start":66,"end":149},{"id":"PF02938","name":"GAD domain","start":357,"end":452}],"gene3D":[]},"genes":[{"name":{"value":"DARS2"}}],"length":645,"name":"Aspartate--tRNA ligase, mitochondrial","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":631,"end":645,"reference_id":"23275545","reference_source":"pmid","reference_html":"Thermodynamic properties distinguish human mitochondrial aspartyl-tRNA synthetase from bacterial homolog with same 3D architecture. <i> Neuenfeldt A, Lorber B, Ennifar E, Gaudry A, Sauter C, Sissler M, Florentz C. </i> Nucleic Acids Res, 2013","date":"2022-10-20T08:55:30.303Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4AH6"}],"region_id":"DP03836r001","statement":[{"text":"Refinement using a dynamic elastic network (DEN) as implemented in CNS 1.3 (33) led to a reorientation of the insertions and to a dramatic improvement of the electron density map. All residues of HsaDRS2 were built except the 26 C-terminal amino acids (including the 6-His tag), which are disordered.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-20T15:14:37.899Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MYFPSWLSQLYRGLSRPIRRTTQPIWGSLYRSLLQSSQRRIPEFSSFVVRTNTCGELRSSHLGQEVTLCGWIQYRRQNTFLVLRDFDGLVQVIIPQDESAASVKKILCEAPVESVVQVSGTVISRPAGQENPKMPTGEIEIKVKTAELLNACKKLPFEIKNFVKKTEALRLQYRYLDLRSFQMQYNLRLRSQMVMKMREYLCNLHGFVDIETPTLFKRTPGGAKEFLVPSREPGKFYSLPQSPQQFKQLLMVGGLDRYFQVARCYRDEGSRPDRQPEFTQIDIEMSFVDQTGIQSLIEGLLQYSWPNDKDPVVVPFPTMTFAEVLATYGTDKPDTRFGMKIIDISDVFRNTEIGFLQDALSKPHGTVKAICIPEGAKYLKRKDIESIRNFAADHFNQEILPVFLNANRNWNSPVANFIMESQRLELIRLMETQEEDVVLLTAGEHNKACSLLGKLRLECADLLETRGVVLRDPTLFSFLWVVDFPLFLPKEENPRELESAHHPFTAPHPSDIHLLYTEPKKARSQHYDLVLNGNEIGGGSIRIHNAELQRYILATLLKEDVKMLSHLLQALDYGAPPHGGIALGLDRLICLVTGSPSIRDVIAFPKSFRGHDLMSNTPDSVPPEELKPYHIRVSKPTDSKAERAH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","RNA-binding proteins"],"alphafold_very_low_content":0.07441860465116279,"disorder_content":0.023255813953488372,"disprot_consensus":{"full":[{"start":631,"end":645,"type":"D"}],"Structural state":[{"start":631,"end":645,"type":"D"}]}},{"disprot_id":"DP03837","acc":"P49366","creator":"fkordevani","date":"2022-10-18T12:49:41.472Z","features":{"pfam":[{"id":"PF01916","name":"Deoxyhypusine synthase","start":45,"end":353}],"gene3D":[]},"genes":[{"name":{"value":"DHPS"},"synonyms":[{"value":"DS"}]}],"length":369,"name":"Deoxyhypusine synthase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":76,"end":92,"reference_id":"9493264","reference_source":"pmid","reference_html":"Crystal structure of the NAD complex of human deoxyhypusine synthase: an enzyme with a ball-and-chain mechanism for blocking the active site. <i> Liao DI, Wolff EC, Park MH, Davies DR. </i> Structure, 1998","date":"2022-10-18T12:52:01.985Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1DHS"}],"region_id":"DP03837r001","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-19T20:08:16.951Z"}},{"start":1,"end":27,"reference_id":"32142284","reference_source":"pmid","reference_html":"Discovery of Novel Allosteric Inhibitors of Deoxyhypusine Synthase. <i> Tanaka Y, Kurasawa O, Yokota A, Klein MG, Ono K, Saito B, Matsumoto S, Okaniwa M, Ambrus-Aikelin G, Morishita D, Kitazawa S, Uchiyama N, Ogawa K, Kimura H, Imamura S. </i> J Med Chem, 2020","date":"2022-10-20T15:18:37.419Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6P4V"}],"region_id":"DP03837r002","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"13389","entry_name":"NAD"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"133366","entry_name":"2-(7-aminoheptyl)guanidine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"44224","entry_name":"(4S)-2-methylpentane-2,4-diol"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-20T15:21:10.712Z"}},{"start":1,"end":12,"reference_id":"32142284","reference_source":"pmid","reference_html":"Discovery of Novel Allosteric Inhibitors of Deoxyhypusine Synthase. <i> Tanaka Y, Kurasawa O, Yokota A, Klein MG, Ono K, Saito B, Matsumoto S, Okaniwa M, Ambrus-Aikelin G, Morishita D, Kitazawa S, Uchiyama N, Ogawa K, Kimura H, Imamura S. </i> J Med Chem, 2020","date":"2023-11-28T14:40:34.099Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":1,"cross_refs":[{"db":"PDB","id":"6PGR"}],"region_id":"DP03837r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:146014943"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}]}],"regions_counter":3,"released":"2023_06","sequence":"MEGSLEREAPAGALAAVLKHSSTLPPESTQVRGYDFNRGVNYRALLEAFGTTGFQATNFGRAVQQVNAMIEKKLEPLSQDEDQHADLTQSRRPLTSCTIFLGYTSNLISSGIRETIRYLVQHNMVDVLVTTAGGVEEDLIKCLAPTYLGEFSLRGKELRENGINRIGNLLVPNENYCKFEDWLMPILDQMVMEQNTEGVKWTPSKMIARLGKEINNPESVYYWAQKNHIPVFSPALTDGSLGDMIFFHSYKNPGLVLDIVEDLRLINTQAIFAKCTGMIILGGGVVKHHIANANLMRNGADYAVYINTAQEFDGSDSGARPDEAVSWGKIRVDAQPVKVYADASLVFPLLVAETFAQKMDAFMHEKNED","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.02168021680216802,"disorder_content":0.11924119241192412,"disprot_consensus":{"full":[{"start":1,"end":27,"type":"D"},{"start":76,"end":92,"type":"D"}],"Structural state":[{"start":1,"end":27,"type":"D"},{"start":76,"end":92,"type":"D"}]}},{"disprot_id":"DP03838","acc":"O00548","creator":"fkordevani","date":"2022-10-18T12:59:56.475Z","features":{"pfam":[{"id":"PF00008","name":"EGF-like domain","start":293,"end":323},{"id":"PF00008","name":"EGF-like domain","start":332,"end":361},{"id":"PF00008","name":"EGF-like domain","start":370,"end":399},{"id":"PF00008","name":"EGF-like domain","start":409,"end":439},{"id":"PF00008","name":"EGF-like domain","start":447,"end":477},{"id":"PF00008","name":"EGF-like domain","start":485,"end":515},{"id":"PF01414","name":"Delta serrate ligand","start":179,"end":224},{"id":"PF07657","name":"N terminus of Notch ligand C2-like domain","start":22,"end":177},{"id":"PF21700","name":"Delta-like/Jagged, EGF-like domain","start":264,"end":289}],"gene3D":[]},"genes":[{"name":{"value":"DLL1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:2908","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:2908"}}]},"orfNames":[{"value":"UNQ146/PRO172"}]}],"length":723,"name":"Delta-like protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":443,"end":551,"reference_id":"25715738","reference_source":"pmid","reference_html":"Notch ligand delta-like1: X-ray crystal structure and binding affinity. <i> Kershaw NJ, Church NL, Griffin MD, Luo CS, Adams TE, Burgess AW. </i> Biochem J, 2015","date":"2022-10-19T08:43:00.418Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4XBM"}],"region_id":"DP03838r001","statement":[{"text":"In one copy of Dll-1, residues 21–442 were visible, comprising the C2 domain, DSL domain and EGF-like repeats 1–6 (i.e. missing the last two EGF-like repeats); in the second copy, only the C2, DSL and first two EGF domains were visible (residues 22–291). The two copies of Dll-1 in the asymmetric unit overlay with an RMSD of 2.3 Å.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu498Gln","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg502Gly","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly510Ser","start":null,"end":null,"position":null}],"sequence_construct":"SSGVFELKLQEFVNKKGLLGNRNCCRGGAGPPPCACRTFFRVCLKHYQASVSPEPPCTYGSAVTPVLGVDSFSLPDGGGADSAFSNPIRFPFGFTWPGTFSLIIEALHTDSPDDLATENPERLISRLATQRHLTVGEEWSQDLHSSGRTDLKYSYRFVCDEHYYGEGCSVFCRPRDDAFGHFTCGERGEKVCNPGWKGPYCTEPICLPGCDEQHGFCDKPGECKCRVGWQGRYCDECIRYPGCLHGTCQQPWQCNCQEGWGGLFCNQDLNYCTHHKPCKNGATCTNTGQGSYTCSCRPGYTGATCELGIDECDPSPCKNGGSCTDLENSYSCTCPPGFYGKICELSAMTCADGPCFNGGRCSDSPDGGYSCRCPVGYSGFNCEKKIDYCSSSPCSNGAKCVDLGDAYLCRCQAGFSGRHCDDNVDDCASSPCANGGTCRDGVNDFSCTCPPGYTGRNCSAPVSRCEHAPCHNGATCHQRGHGYVCECARSYGGPNCQFLLPELPPGPAVVDLTEKLEGQGGPFPWENLYFQ","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-19T13:16:45.372Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MGSRCALALAVLSALLCQVWSSGVFELKLQEFVNKKGLLGNRNCCRGGAGPPPCACRTFFRVCLKHYQASVSPEPPCTYGSAVTPVLGVDSFSLPDGGGADSAFSNPIRFPFGFTWPGTFSLIIEALHTDSPDDLATENPERLISRLATQRHLTVGEEWSQDLHSSGRTDLKYSYRFVCDEHYYGEGCSVFCRPRDDAFGHFTCGERGEKVCNPGWKGPYCTEPICLPGCDEQHGFCDKPGECKCRVGWQGRYCDECIRYPGCLHGTCQQPWQCNCQEGWGGLFCNQDLNYCTHHKPCKNGATCTNTGQGSYTCSCRPGYTGATCELGIDECDPSPCKNGGSCTDLENSYSCTCPPGFYGKICELSAMTCADGPCFNGGRCSDSPDGGYSCRCPVGYSGFNCEKKIDYCSSSPCSNGAKCVDLGDAYLCRCQAGFSGRHCDDNVDDCASSPCANGGTCRDGVNDFSCTCPPGYTGRNCSAPVSRCEHAPCHNGATCHERGHRYVCECARGYGGPNCQFLLPELPPGPAVVDLTEKLEGQGGPFPWVAVCAGVILVLMLLLGCAAVVVCVRLRLQKHRPPADPCRGETETMNNLANCQREKDISVSIIGATQIKNTNKKADFHGDHSADKNGFKARYPAVDYNLVQDLKGDDTAVRDAHSKRDTKCQPQGSSGEEKGTPTTLRGGEASERKRPDSGCSTSKDTKYQSVYVISEEKDECVIATEV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.22130013831258644,"disorder_content":0.1507607192254495,"disprot_consensus":{"full":[{"start":443,"end":551,"type":"D"}],"Structural state":[{"start":443,"end":551,"type":"D"}]}},{"disprot_id":"DP03839","acc":"Q92785","creator":"fkordevani","date":"2022-10-18T13:38:43.141Z","features":{"pfam":[{"id":"PF00628","name":"PHD-finger","start":273,"end":327},{"id":"PF00628","name":"PHD-finger","start":330,"end":374},{"id":"PF14051","name":"DPF1-3, N-terminal","start":14,"end":84}],"gene3D":[]},"genes":[{"name":{"value":"DPF2"},"synonyms":[{"value":"BAF45D"},{"value":"REQ"},{"value":"UBID4"}]}],"length":391,"name":"Zinc finger protein ubi-d4","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":235,"end":249,"reference_id":"21888896","reference_source":"pmid","reference_html":"Crystal structure of the Cys2His2-type zinc finger domain of human DPF2. <i> Zhang W, Xu C, Bian C, Tempel W, Crombet L, MacKenzie F, Min J, Liu Z, Qi C. </i> Biochem Biophys Res Commun, 2011","date":"2022-10-18T13:41:05.910Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3IUF"}],"region_id":"DP03839r001","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-19T20:18:12.697Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MAAVVENVVKLLGEQYYKDAMEQCHNYNARLCAERSVRLPFLDSQTGVAQSNCYIWMEKRHRGPGLASGQLYSYPARRWRKKRRAHPPEDPRLSFPSIKPDTDQTLKKEGLISQDGSSLEALLRTDPLEKRGAPDPRVDDDSLGEFPVTNSRARKRILEPDDFLDDLDDEDYEEDTPKRRGKGKSKGKGVGSARKKLDASILEDRDKPYACDICGKRYKNRPGLSYHYAHSHLAEEEGEDKEDSQPPTPVSQRSEEQKSKKGPDGLALPNNYCDFCLGDSKINKKTGQPEELVSCSDCGRSGHPSCLQFTPVMMAAVKTYRWQCIECKCCNICGTSENDDQLLFCDDCDRGYHMYCLTPSMSEPPEGSWSCHLCLDLLKEKASIYQNQNSS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.3145780051150895,"disorder_content":0.03836317135549872,"disprot_consensus":{"full":[{"start":235,"end":249,"type":"D"}],"Structural state":[{"start":235,"end":249,"type":"D"}]}},{"disprot_id":"DP03841","acc":"P07814","creator":"fkordevani","date":"2022-10-18T14:00:10.450Z","features":{"pfam":[{"id":"PF00458","name":"WHEP-TRS domain","start":753,"end":805},{"id":"PF00458","name":"WHEP-TRS domain","start":826,"end":878},{"id":"PF00458","name":"WHEP-TRS domain","start":904,"end":955},{"id":"PF00587","name":"tRNA synthetase class II core domain (G, H, P, S and T)","start":1113,"end":1284},{"id":"PF00749","name":"tRNA synthetases class I (E and Q), catalytic domain","start":197,"end":501},{"id":"PF03129","name":"Anticodon binding domain","start":1303,"end":1403},{"id":"PF03950","name":"tRNA synthetases class I (E and Q), anti-codon binding domain","start":504,"end":594},{"id":"PF09180","name":"Prolyl-tRNA synthetase, C-terminal","start":1430,"end":1512},{"id":"PF20974","name":"tRNA synthetases class I (E and Q), anti-codon binding domain","start":606,"end":681},{"id":"PF21972","name":"Nuclear-export cofactor Arc1p","start":92,"end":155}],"gene3D":[]},"genes":[{"name":{"value":"EPRS1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:3418","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:3418"}}]},"synonyms":[{"value":"EPRS"},{"value":"GLNS"},{"value":"PARS"},{"value":"QARS"},{"value":"QPRS"}],"orfNames":[{"value":"PIG32"}]}],"length":1512,"name":"Bifunctional glutamate/proline--tRNA ligase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1003,"end":1014,"reference_id":"23263184","reference_source":"pmid","reference_html":"ATP-directed capture of bioactive herbal-based medicine on human tRNA synthetase. <i> Zhou H, Sun L, Yang XL, Schimmel P. </i> Nature, 2013","date":"2022-10-18T14:02:33.695Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4HVC"}],"region_id":"DP03841r001","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-19T20:40:14.951Z"}},{"start":1464,"end":1473,"reference_id":"23263184","reference_source":"pmid","reference_html":"ATP-directed capture of bioactive herbal-based medicine on human tRNA synthetase. <i> Zhou H, Sun L, Yang XL, Schimmel P. </i> Nature, 2013","date":"2022-10-18T14:03:13.176Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4HVC"}],"region_id":"DP03841r002","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-19T20:40:26.648Z"}},{"start":998,"end":1015,"reference_id":"28501621","reference_source":"pmid","reference_html":"Discovery of a novel prolyl-tRNA synthetase inhibitor and elucidation of its binding mode to the ATP site in complex with l-proline. <i> Adachi R, Okada K, Skene R, Ogawa K, Miwa M, Tsuchinaga K, Ohkubo S, Henta T, Kawamoto T. </i> Biochem Biophys Res Commun, 2017","date":"2022-10-20T09:03:34.074Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5VAD"}],"region_id":"DP03841r003","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-20T15:21:50.690Z"}},{"start":1464,"end":1473,"reference_id":"28501621","reference_source":"pmid","reference_html":"Discovery of a novel prolyl-tRNA synthetase inhibitor and elucidation of its binding mode to the ATP site in complex with l-proline. <i> Adachi R, Okada K, Skene R, Ogawa K, Miwa M, Tsuchinaga K, Ohkubo S, Henta T, Kawamoto T. </i> Biochem Biophys Res Commun, 2017","date":"2022-10-18T14:06:23.538Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5VAD"}],"region_id":"DP03841r004","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-19T20:35:54.391Z"}},{"start":1001,"end":1014,"reference_id":"34360555","reference_source":"pmid","reference_html":"Towards Novel 3-Aminopyrazinamide-Based Prolyl-tRNA Synthetase Inhibitors: In Silico Modelling, Thermal Shift Assay and Structural Studies.  <i> Pang L, Weeks SD, Juhás M, Strelkov SV, Zitko J, Van Aerschot A. </i> Int J Mol Sci, 2021","date":"2022-10-20T09:02:39.678Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7OSY"},{"db":"PDB","id":"7OT0"},{"db":"PDB","id":"7OT1"},{"db":"PDB","id":"7OT2"},{"db":"PDB","id":"7OT3"},{"db":"PDB","id":"7OSZ"}],"region_id":"DP03841r005","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-20T15:21:39.030Z"}}],"regions_counter":5,"released":"2023_06","sequence":"MATLSLTVNSGDPPLGALLAVEHVKDDVSISVEEGKENILHVSENVIFTDVNSILRYLARVATTAGLYGSNLMEHTEIDHWLEFSATKLSSCDSFTSTINELNHCLSLRTYLVGNSLSLADLCVWATLKGNAAWQEQLKQKKAPVHVKRWFGFLEAQQAFQSVGTKWDVSTTKARVAPEKKQDVGKFVELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFETIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIDSKHRKNPIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEVIPVNVPEAQEEMKEVAKHPKNPEVGLKPVWYSPKVFIEGADAETFSEGEMVTFINWGNLNITKIHKNADGKIISLDAKLNLENKDYKKTTKVTWLAETTHALPIPVICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDQPYEPVSPYSCKEAPCVLIYIPDGHTKEMPTSGSKEKTKVEATKNETSAPFKERPTPSLNNNCTTSEDSLVLYNRVAVQGDVVRELKAKKAPKEDVDAAVKQLLSLKAEYKEKTGQEYKPGNPPAEIGQNISSNSSASILESKSLYDEVAAQGEVVRKLKAEKSPKAKINEAVECLLSLKAQYKEKTGKEYIPGQPPLSQSSDSSPTRNSEPAGLETPEAKVLFDKVASQGEVVRKLKTEKAPKDQVDIAVQELLQLKAQYKSLIGVEYKPVSATGAEDKDKKKKEKENKSEKQNKPQKQNDGQRKDPSKNQGGGLSSSGAGEGQGPKKQTRLGLEAKKEENLADWYSQVITKSEMIEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKTHVADFAPEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVRWEFKHPQPFLRTREFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFAGGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPKIPGEKQFAYQNSWGLTTRTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGITNALSEEDKEALIAKCNDYRRRLLSVNIRVRADLRDNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVAENEAETKLQAILEDIQVTLFTRASEDLKTHMVVANTMEDFQKILDSGKIVQIPFCGEIDCEDWIKKTTARDQDLEPGAPSMGAKSLCIPFKPLCELQPGAKCVCGKNPAKYYTLFGRSY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","RNA-binding proteins"],"alphafold_very_low_content":0.10383597883597884,"disorder_content":0.018518518518518517,"disprot_consensus":{"full":[{"start":998,"end":1015,"type":"D"},{"start":1464,"end":1473,"type":"D"}],"Structural state":[{"start":998,"end":1015,"type":"D"},{"start":1464,"end":1473,"type":"D"}]}},{"disprot_id":"DP03842","acc":"P37268","creator":"fkordevani","date":"2022-10-18T14:12:56.358Z","features":{"pfam":[{"id":"PF00494","name":"Squalene/phytoene synthase","start":48,"end":319}],"gene3D":[]},"genes":[{"name":{"value":"FDFT1"}}],"length":417,"name":"Squalene synthase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":315,"end":327,"reference_id":"10896663","reference_source":"pmid","reference_html":"Crystal structure of human squalene synthase. A key enzyme in cholesterol biosynthesis. <i> Pandit J, Danley DE, Schulte GK, Mazzalupo S, Pauly TA, Hayward CM, Hamanaka ES, Thompson JF, Harwood HJ. </i> J Biol Chem, 2000","date":"2022-10-20T09:06:26.605Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1EZF"}],"region_id":"DP03842r001","statement":[{"text":"Electron density for residues 315–327 and for the NH2-terminal seven residues was not seen, so they were not included in the final model.","type":"Methods"},{"text":"It is also the most flexible part of the structure, indeed residues 315–327 are so disordered that they were not seen in the electron density maps calculated for the CP-320473 structure.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-20T15:22:23.373Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MEFVKCLGHPEEFYNLVRFRIGGKRKVMPKMDQDSLSSSLKTCYKYLNQTSRSFAAVIQALDGEMRNAVCIFYLVLRALDTLEDDMTISVEKKVPLLHNFHSFLYQPDWRFMESKEKDRQVLEDFPTISLEFRNLAEKYQTVIADICRRMGIGMAEFLDKHVTSEQEWDKYCHYVAGLVGIGLSRLFSASEFEDPLVGEDTERANSMGLFLQKTNIIRDYLEDQQGGREFWPQEVWSRYVKKLGDFAKPENIDLAVQCLNELITNALHHIPDVITYLSRLRNQSVFNFCAIPQVMAIATLAACYNNQQVFKGAVKIRKGQAVTLMMDATNMPAVKAIIYQYMEEIYHRIPDSDPSSSKTRQIISTIRTQNLPNCQLISRSHYSPIYLSFVMLLAALSWQYLTTLSQVTEDYVQTGEH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.02877697841726619,"disorder_content":0.03117505995203837,"disprot_consensus":{"full":[{"start":315,"end":327,"type":"D"}],"Structural state":[{"start":315,"end":327,"type":"D"}]}},{"disprot_id":"DP03843","acc":"Q9BYC5","creator":"fkordevani","date":"2022-10-18T14:22:57.500Z","features":{"pfam":[{"id":"PF14604","name":"Variant SH3 domain","start":509,"end":558},{"id":"PF19745","name":"Alpha-(1,6)-fucosyltransferase N- and catalytic domains","start":2,"end":498}],"gene3D":[]},"genes":[{"name":{"value":"FUT8"}}],"length":575,"name":"Alpha-(1,6)-fucosyltransferase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":68,"end":107,"reference_id":"17172260","reference_source":"pmid","reference_html":"Crystal structure of mammalian alpha1,6-fucosyltransferase, FUT8. <i> Ihara H, Ikeda Y, Toma S, Wang X, Suzuki T, Gu J, Miyoshi E, Tsukihara T, Honke K, Matsumoto A, Nakagawa A, Taniguchi N. </i> Glycobiology, 2007","date":"2022-10-21T08:03:54.756Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2DE0"}],"region_id":"DP03843r001","statement":[{"text":"As illustrated in Figure 2, the residues of Leu-108 to Glu-572 are modeled, however, the N-terminus (residues 68–107), C-terminus (residues 573–575), and the residues 368–372 are disordered in this structure.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T13:17:52.802Z"}},{"start":41,"end":107,"reference_id":"33004438","reference_source":"pmid","reference_html":"Characterizing human α-1,6-fucosyltransferase (FUT8) substrate specificity and structural similarities with related fucosyltransferases. <i> Boruah BM, Kadirvelraj R, Liu L, Ramiah A, Li C, Zong G, Bosman GP, Yang JY, Wang LX, Boons GJ, Wood ZA, Moremen KW. </i> J Biol Chem, 2020","date":"2022-10-21T08:03:02.625Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6X5H"},{"db":"PDB","id":"6X5T"},{"db":"PDB","id":"6X5R"},{"db":"PDB","id":"6X5U"}],"region_id":"DP03843r002","statement":[{"text":"The NH2-terminus (residues 41-107) and the C-terminal residue Lys575 were disordered and left unmodeled.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T13:17:33.095Z"}}],"regions_counter":3,"released":"2023_06","sequence":"MRPWTGSWRWIMLILFAWGTLLFYIGGHLVRDNDHPDHSSRELSKILAKLERLKQQNEDLRRMAESLRIPEGPIDQGPAIGRVRVLEEQLVKAKEQIENYKKQTRNGLGKDHEILRRRIENGAKELWFFLQSELKKLKNLEGNELQRHADEFLLDLGHHERSIMTDLYYLSQTDGAGDWREKEAKDLTELVQRRITYLQNPKDCSKAKKLVCNINKGCGYGCQLHHVVYCFMIAYGTQRTLILESQNWRYATGGWETVFRPVSETCTDRSGISTGHWSGEVKDKNVQVVELPIVDSLHPRPPYLPLAVPEDLADRLVRVHGDPAVWWVSQFVKYLIRPQPWLEKEIEEATKKLGFKHPVIGVHVRRTDKVGTEAAFHPIEEYMVHVEEHFQLLARRMQVDKKRVYLATDDPSLLKEAKTKYPNYEFISDNSISWSAGLHNRYTENSLRGVILDIHFLSQADFLVCTFSSQVCRVAYEIMQTLHPDASANFHSLDDIYYFGGQNAHNQIAIYAHQPRTADEIPMEPGDIIGVAGNHWDGYSKGVNRKLGRTGLYPSYKVREKIETVKYPTYPEAEK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.017391304347826087,"disorder_content":0.11652173913043479,"disprot_consensus":{"full":[{"start":41,"end":107,"type":"D"}],"Structural state":[{"start":41,"end":107,"type":"D"}]}},{"disprot_id":"DP03845","acc":"P07902","creator":"fkordevani","date":"2022-10-19T12:20:59.432Z","features":{"pfam":[{"id":"PF01087","name":"Galactose-1-phosphate uridyl transferase, N-terminal domain","start":23,"end":196},{"id":"PF02744","name":"Galactose-1-phosphate uridyl transferase, C-terminal domain","start":203,"end":368}],"gene3D":[]},"genes":[{"name":{"value":"GALT"}}],"length":379,"name":"Galactose-1-phosphate uridylyltransferase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":21,"reference_id":"27005423","reference_source":"pmid","reference_html":"Molecular basis of classic galactosemia from the structure of human galactose 1-phosphate uridylyltransferase. <i> McCorvie TJ, Kopec J, Pey AL, Fitzpatrick F, Patel D, Chalk R, Shrestha L, Yue WW. </i> Hum Mol Genet, 2016","date":"2022-10-21T07:55:50.441Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5IN3"}],"region_id":"DP03845r001","statement":[{"text":"There was no interpretable electron density for residues 1–27, 49–63, 367–379 in chain A and residues 1–23, 49–63, 365–379 in chain B.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T13:15:23.037Z"}},{"start":49,"end":63,"reference_id":"27005423","reference_source":"pmid","reference_html":"Molecular basis of classic galactosemia from the structure of human galactose 1-phosphate uridylyltransferase. <i> McCorvie TJ, Kopec J, Pey AL, Fitzpatrick F, Patel D, Chalk R, Shrestha L, Yue WW. </i> Hum Mol Genet, 2016","date":"2022-10-21T07:55:11.753Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5IN3"}],"region_id":"DP03845r002","statement":[{"text":"Residues 49–63, corresponding to a surface-exposed loop involved in UDP-hexose binding, are disordered in the structure, suggesting its mobility in the absence of this ligand.","type":"Results"},{"text":"There was no interpretable electron density for residues 1–27, 49–63, 367–379 in chain A and residues 1–23, 49–63, 365–379 in chain B.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T13:14:33.845Z"}},{"start":367,"end":379,"reference_id":"27005423","reference_source":"pmid","reference_html":"Molecular basis of classic galactosemia from the structure of human galactose 1-phosphate uridylyltransferase. <i> McCorvie TJ, Kopec J, Pey AL, Fitzpatrick F, Patel D, Chalk R, Shrestha L, Yue WW. </i> Hum Mol Genet, 2016","date":"2022-10-21T07:57:35.906Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5IN3"}],"region_id":"DP03845r004","statement":[{"text":"There was no interpretable electron density for residues 1–27, 49–63, 367–379 in chain A and residues 1–23, 49–63, 365–379 in chain B.\"","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T13:15:47.497Z"}}],"regions_counter":5,"released":"2023_06","sequence":"MSRSGTDPQQRQQASEADAAAATFRANDHQHIRYNPLQDEWVLVSAHRMKRPWQGQVEPQLLKTVPRHDPLNPLCPGAIRANGEVNPQYDSTFLFDNDFPALQPDAPSPGPSDHPLFQAKSARGVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQYPWVQIFENKGAMMGCSNPHPHCQVWASSFLPDIAQREERSQQAYKSQHGEPLLMEYSRQELLRKERLVLTSEHWLVLVPFWATWPYQTLLLPRRHVRRLPELTPAERDDLASIMKKLLTKYDNLFETSFPYSMGWHGAPTGSEAGANWNHWQLHAHYYPPLLRSATVRKFMVGYEMLAQAQRDLTPEQAAERLRALPEVHYHLGQKDRETATIA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.0316622691292876,"disorder_content":0.12928759894459102,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"},{"start":49,"end":63,"type":"D"},{"start":367,"end":379,"type":"D"}],"Structural state":[{"start":1,"end":21,"type":"D"},{"start":49,"end":63,"type":"D"},{"start":367,"end":379,"type":"D"}]}},{"disprot_id":"DP03847","acc":"O94925","creator":"fkordevani","date":"2022-10-19T12:37:00.244Z","features":{"pfam":[{"id":"PF04960","name":"Glutaminase","start":244,"end":530},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":557,"end":645},{"id":"PF17959","name":"EF-hand domain","start":140,"end":222}],"gene3D":[]},"genes":[{"name":{"value":"GLS"},"synonyms":[{"value":"GLS1"},{"value":"KIAA0838"}]}],"length":669,"name":"Glutaminase kidney isoform, mitochondrial","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":71,"end":135,"reference_id":"22049910","reference_source":"pmid","reference_html":"Full-length human glutaminase in complex with an allosteric inhibitor. <i> DeLaBarre B, Gross S, Fang C, Gao Y, Jha A, Jiang F, Song J J, Wei W, Hurov JB. </i> Biochemistry, 2011","date":"2022-10-21T08:01:14.285Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3UNW"},{"db":"PDB","id":"3UO9"}],"region_id":"DP03847r001","statement":[{"text":"Both the N- and C-termini exhibit disorder in this structure, which results in the N-terminal helical domain being flanked by two regions of disordered residues, 71–135 and 547–598.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T13:16:48.464Z"}},{"start":72,"end":135,"reference_id":"26988803","reference_source":"pmid","reference_html":"Design and evaluation of novel glutaminase inhibitors. <i> McDermott LA, Iyer P, Vernetti L, Rimer S, Sun J, Boby M, Yang T, Fioravanti M, O'Neill J, Wang L, Drakes D, Katt W, Huang Q, Cerione R. </i> Bioorg Med Chem, 2016","date":"2022-10-19T13:01:56.561Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5FI2"},{"db":"PDB","id":"5I94"},{"db":"PDB","id":"5FI7"},{"db":"PDB","id":"5FI6"}],"region_id":"DP03847r005","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-20T19:07:44.512Z"}},{"start":646,"end":669,"reference_id":"28526749","reference_source":"pmid","reference_html":"The origin and evolution of human glutaminases and their atypical C-terminal ankyrin repeats. <i> Pasquali CC, Islam Z, Adamoski D, Ferreira IM, Righeto RD, Bettini J, Portugal RV, Yue WW, Gonzalez A, Dias SMG, Ambrosio ALB. </i> J Biol Chem, 2017","date":"2022-10-21T07:59:50.435Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5U0I"},{"db":"PDB","id":"5U0J"}],"region_id":"DP03847r006","statement":[{"text":"The majority of the C-terminal region of KGA adjacent to the ANK repeats (residues Thr647-Leu669) is likely heterogeneous in conformation and therefore could not be modeled.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T13:16:32.759Z"}},{"start":72,"end":136,"reference_id":"29317493","reference_source":"pmid","reference_html":"Characterization of the interactions of potent allosteric inhibitors with glutaminase C, a key enzyme in cancer cell glutamine metabolism. <i> Huang Q, Stalnecker C, Zhang C, McDermott LA, Iyer P, O'Neill J, Reimer S, Cerione RA, Katt WP. </i> J Biol Chem, 2018","date":"2022-10-21T07:58:57.705Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5WJ6"}],"region_id":"DP03847r007","statement":[{"text":"In both structures, only part of the N terminus of GAC is resolved (beginning at Pro-137), and the majority of the C terminus is not visible (ending at Gly-546).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T13:16:21.550Z"}}],"regions_counter":8,"released":"2023_06","sequence":"MMRLRGSGMLRDLLLRSPAGVSATLRRAQPLVTLCRRPRGGGRPAAGPAAAARLHPWWGGGGWPAEPLARGLSSSPSEILQELGKGSTHPQPGVSPPAAPAAPGPKDGPGETDAFGNSEGKELVASGENKIKQGLLPSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQTTSDGVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSTGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHFAKKLDPRREGGDQRVKSVINLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRWNNTPMDEALHFGHHDVFKILQEYQVQYTPQGDSDNGKENQTVHKNLDGLL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.23019431988041852,"disorder_content":0.13452914798206278,"disprot_consensus":{"full":[{"start":71,"end":136,"type":"D"},{"start":646,"end":669,"type":"D"}],"Structural state":[{"start":71,"end":136,"type":"D"},{"start":646,"end":669,"type":"D"}]}},{"disprot_id":"DP03848","acc":"Q9NQX3","creator":"fkordevani","date":"2022-10-19T13:33:03.298Z","features":{"pfam":[{"id":"PF00994","name":"Probable molybdopterin binding domain","start":18,"end":164},{"id":"PF00994","name":"Probable molybdopterin binding domain","start":502,"end":645},{"id":"PF03453","name":"MoeA N-terminal region (domain I and II)","start":325,"end":489},{"id":"PF03454","name":"MoeA C-terminal region (domain IV)","start":658,"end":732}],"gene3D":[]},"genes":[{"name":{"value":"GPHN","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:15465","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:15465"}}]},"synonyms":[{"value":"GPH"},{"value":"KIAA1385"}]}],"length":736,"name":"Gephyrin","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":12,"reference_id":"11554796","reference_source":"pmid","reference_html":"Crystal structures of human gephyrin and plant Cnx1 G domains: comparative analysis and functional implications. <i> Schwarz G, Schrader N, Mendel RR, Hecht HJ, Schindelin H. </i> J Mol Biol, 2001","date":"2022-10-21T08:01:49.419Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1JLJ"}],"region_id":"DP03848r001","statement":[{"text":"Residues 1-12 of Geph-G and residues 459-461 of Cnx1-G are not present in the model and appear to be disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T13:17:02.580Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MATEGMILTNHDHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDPSLLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTGFAPRDVTPEATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPHAIDLLRDAIVKVKEVHDELEDLPSPPPPLSPPPTTSPHKQTEDKGVQCEEEEEEKKDSGVASTEDSSSSHITAAAIAAKIPDSIISRGVQVLPRDTASLSTTPSESPRAQATSRLSTASCPTPKVQSRCSSKENILRASHSAVDITKVARRHRMSPFPLTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTQTVMPGQVMRVTTGAPIPCGADAVVQVEDTELIRESDDGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGEKDYLKQVLDIDLHAQIHFGRVFMKPGLPTTFATLDIDGVRKIIFALPGNPVSAVVTCNLFVVPALRKMQGILDPRPTIIKARLSCDVKLDPRPEYHRCILTWHHQEPLPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEQYVELHKGEVVDVMVIGRL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Cancer-related proteins"],"alphafold_very_low_content":0.17255434782608695,"disorder_content":0.016304347826086956,"disprot_consensus":{"full":[{"start":1,"end":12,"type":"D"}],"Structural state":[{"start":1,"end":12,"type":"D"}]}},{"disprot_id":"DP03849","acc":"P00492","creator":"fkordevani","date":"2022-10-19T15:53:56.260Z","features":{"pfam":[{"id":"PF00156","name":"Phosphoribosyl transferase domain","start":42,"end":195}],"gene3D":[]},"genes":[{"name":{"value":"HPRT1"},"synonyms":[{"value":"HPRT"}]}],"length":218,"name":"Hypoxanthine-guanine phosphoribosyltransferase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":104,"end":123,"reference_id":"23907213","reference_source":"pmid","reference_html":"Role of human hypoxanthine guanine phosphoribosyltransferase in activation of the antiviral agent T-705 (favipiravir). <i> Naesens L, Guddat LW, Keough DT, van Kuilenburg AB, Meijer J, Vande Voorde J, Balzarini J. </i> Mol Pharmacol, 2013","date":"2022-10-21T14:13:36.242Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4KN6"}],"region_id":"DP03849r001","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T14:14:15.643Z"}},{"start":104,"end":113,"reference_id":"25494538","reference_source":"pmid","reference_html":"Aza-acyclic nucleoside phosphonates containing a second phosphonate group as inhibitors of the human, Plasmodium falciparum and vivax 6-oxopurine phosphoribosyltransferases and their prodrugs as antimalarial agents. <i> Keough DT, Hocková D, Janeba Z, Wang TH, Naesens L, Edstein MD, Chavchich M, Guddat LW. </i> J Med Chem, 2015","date":"2022-10-19T16:02:41.147Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP03849r002","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"4RAB"},{"db":"PDB","id":"4RAC"},{"db":"PDB","id":"4RAN"},{"db":"PDB","id":"4RAQ"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T13:29:26.149Z"}},{"start":103,"end":119,"reference_id":"26368337","reference_source":"pmid","reference_html":"Synthesis and Evaluation of Novel Acyclic Nucleoside Phosphonates as Inhibitors of Plasmodium falciparum and Human 6-Oxopurine Phosphoribosyltransferases. <i> Kaiser MM, Hocková D, Wang TH, Dračínský M, Poštová-Slavětínská L, Procházková E, Edstein MD, Chavchich M, Keough DT, Guddat LW, Janeba Z. </i> ChemMedChem, 2015","date":"2022-10-19T16:06:56.366Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5BRN"}],"region_id":"DP03849r003","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T13:25:59.167Z"}},{"start":102,"end":121,"reference_id":"26368337","reference_source":"pmid","reference_html":"Synthesis and Evaluation of Novel Acyclic Nucleoside Phosphonates as Inhibitors of Plasmodium falciparum and Human 6-Oxopurine Phosphoribosyltransferases. <i> Kaiser MM, Hocková D, Wang TH, Dračínský M, Poštová-Slavětínská L, Procházková E, Edstein MD, Chavchich M, Keough DT, Guddat LW, Janeba Z. </i> ChemMedChem, 2015","date":"2022-10-19T16:07:21.624Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5BSK"}],"region_id":"DP03849r004","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T13:25:58.667Z"}}],"regions_counter":4,"released":"2023_06","sequence":"MATRSPGVVISDDEPGYDLDLFCIPNHYAEDLERVFIPHGLIMDRTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIKALNRNSDRSIPMTVDFIRLKSYCNDQSTGDIKVIGGDDLSTLTGKNVLIVEDIIDTGKTMQTLLSLVRQYNPKMVKVASLLVKRTPRSVGYKPDFVGFEIPDKFVVGYALDYNEYFRDLNHVCVISETGKAKYKA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Age-related disorders proteins"],"alphafold_very_low_content":0.04128440366972477,"disorder_content":0.10091743119266056,"disprot_consensus":{"full":[{"start":102,"end":123,"type":"D"}],"Structural state":[{"start":102,"end":123,"type":"D"}]}},{"disprot_id":"DP03850","acc":"E9AD06","creator":"gbalatti","date":"2022-10-19T19:24:40.208Z","features":{"pfam":[{"id":"PF00550","name":"Phosphopantetheine attachment site","start":77,"end":143}],"gene3D":[]},"genes":[{"name":{"value":"ACP","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CBZ12089.1","url":"https://www.ebi.ac.uk/ena/browser/view/CBZ12089.1"}}]},"orfNames":[{"value":"LMJF_27_0290","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CBZ12089.1","url":"https://www.ebi.ac.uk/ena/browser/view/CBZ12089.1"}}]}]}],"length":150,"name":"Acyl carrier protein","ncbi_taxon_id":5664,"organism":"Leishmania major","regions":[{"start":1,"end":66,"reference_id":"33168716","reference_source":"pmid","reference_html":"Structure of the mature kinetoplastids mitoribosome and insights into its large subunit biogenesis. <i> Soufari H, Waltz F, Parrot C, Durrieu-Gaillard S, Bochler A, Kuhn L, Sissler M, Hashem Y. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-10-21T17:58:09.092Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"7AM2"}],"region_id":"DP03850r001","statement":[{"text":"Structure of residues 1-66 is unresolved in the cryo-EM reconstructions, showing its intrinsic flexibility when this protein takes part in the Large subunit from major mitochondrial ribosome.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T21:14:19.649Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MQRQVIRRLGNRSAFPLVAAVARSSQIRGAVRGDSGSRARVIPSFMCSLRAYSGGHHEEPSSRSGQYLLDKSDVLTRVLEVVKNFEKVDASKVTPESHFVKDLGLNSLDVVEVVFAIEQEFILDIPDHDAEKIQSIPDAVEYIAQNPMAK","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"alphafold_very_low_content":0.35333333333333333,"disorder_content":0.44,"disprot_consensus":{"full":[{"start":1,"end":66,"type":"D"}],"Structural state":[{"start":1,"end":66,"type":"D"}]}},{"disprot_id":"DP03851","acc":"P14678","creator":"maspromonte","date":"2022-10-20T10:10:29.062Z","features":{"pfam":[{"id":"PF01423","name":"LSM domain","start":9,"end":81}],"gene3D":[]},"genes":[{"name":{"value":"SNRPB"},"synonyms":[{"value":"COD"},{"value":"SNRPB1"}]}],"length":240,"name":"Small nuclear ribonucleoprotein-associated proteins B and B'","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":90,"end":229,"reference_id":"30315277","reference_source":"pmid","reference_html":"Structures of the human pre-catalytic spliceosome and its precursor spliceosome. <i> Zhan X, Yan C, Zhang X, Lei J, Shi Y. </i> Cell Res, 2018","date":"2022-10-21T14:20:39.430Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6AH0"},{"db":"EMDB","id":"EMD-9621"}],"region_id":"DP03851r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17401","entry_name":"myo-inositol hexakisphosphate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15996","entry_name":"GTP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"}],"statement":[{"text":"The electron microscopy structure of the Precusor of Human Pre-catalytic Spliceosome (pre-B complex) shows this region of the Small nuclear ribonucleoprotein-associated proteins B and B' lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T14:21:45.310Z"}},{"start":50,"end":62,"reference_id":"30315277","reference_source":"pmid","reference_html":"Structures of the human pre-catalytic spliceosome and its precursor spliceosome. <i> Zhan X, Yan C, Zhang X, Lei J, Shi Y. </i> Cell Res, 2018","date":"2022-10-21T14:20:29.489Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6AH0"},{"db":"EMDB","id":"EMD-9621"}],"region_id":"DP03851r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17401","entry_name":"myo-inositol hexakisphosphate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15996","entry_name":"GTP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"}],"statement":[{"text":"The electron microscopy structure of the Precusor of Human Pre-catalytic Spliceosome (pre-B complex) shows this region of the Small nuclear ribonucleoprotein-associated proteins B and B' lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T14:21:44.729Z"}},{"start":92,"end":240,"reference_id":"30975767","reference_source":"pmid","reference_html":"Mechanism of 5' splice site transfer for human spliceosome activation. <i> Charenton C, Wilkinson ME, Nagai K. </i> Science, 2019","date":"2022-10-21T14:17:24.493Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-4658"},{"db":"PDB","id":"6QW6"},{"db":"PDB","id":"6QX9"},{"db":"EMDB","id":"EMD-4665"}],"region_id":"DP03851r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17401","entry_name":"myo-inositol hexakisphosphate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15996","entry_name":"GTP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"The electron microscopy structure of the Precusor of Human Pre-catalytic Spliceosome (pre-B complex) shows this region of the Small nuclear ribonucleoprotein-associated proteins B and B' lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T14:19:50.918Z"}},{"start":88,"end":174,"reference_id":"19325628","reference_source":"pmid","reference_html":"Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution. <i> Pomeranz Krummel DA, Oubridge C, Leung AK, Li J, Nagai K. </i> Nature, 2009","date":"2022-10-20T12:23:51.233Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3CW1"}],"region_id":"DP03851r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"The X-ray structure of the Human Spliceosomal U1 snRNP shows this region of the Small nuclear ribonucleoprotein-associated proteins B and B' lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T13:49:04.660Z"}},{"start":46,"end":64,"reference_id":"19325628","reference_source":"pmid","reference_html":"Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution. <i> Pomeranz Krummel DA, Oubridge C, Leung AK, Li J, Nagai K. </i> Nature, 2009","date":"2023-06-23T12:28:25.415Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3CW1"}],"region_id":"DP03851r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"The X-ray structure of the Human Spliceosomal U1 snRNP shows this region of the Small nuclear ribonucleoprotein-associated proteins B and B' lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-23T13:39:09.529Z"}}],"regions_counter":5,"released":"2023_06","sequence":"MTVGKSSKMLQHIDYRMRCILQDGRIFIGTFKAFDKHMNLILCDCDEFRKIKPKNSKQAEREEKRVLGLVLLRGENLVSMTVEGPPPKDTGIARVPLAGAAGGPGIGRAAGRGIPAGVPMPQAPAGLAGPVRGVGGPSQQVMTPQGRGTVAAAAAAATASIAGAPTQYPPGRGGPPPPMGRGAPPPGMMGPPPGMRPPMGPPMGIPPGRGTPMGMPPPGMRPPPPGMRGPPPPGMRPPRP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","RNA-binding proteins"],"alphafold_very_low_content":0.14583333333333334,"disorder_content":0.7166666666666667,"disprot_consensus":{"full":[{"start":46,"end":64,"type":"D"},{"start":88,"end":240,"type":"D"}],"Structural state":[{"start":46,"end":64,"type":"D"},{"start":88,"end":240,"type":"D"}]}},{"disprot_id":"DP03852","acc":"P0ABK7","creator":"jssuarez","date":"2022-10-20T10:51:16.408Z","features":{"pfam":[{"id":"PF07012","name":"Curlin associated repeat","start":53,"end":86},{"id":"PF07012","name":"Curlin associated repeat","start":97,"end":130}],"gene3D":[]},"genes":[{"name":{"value":"csgB"},"olnNames":[{"value":"b1041"},{"value":"JW1024"}]}],"length":151,"name":"Minor curlin subunit","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":1,"end":151,"reference_id":"22493266","reference_source":"pmid","reference_html":"The E. coli CsgB nucleator of curli assembles to β-sheet oligomers that alter the CsgA fibrillization mechanism. <i> Shu Q, Crick SL, Pinkner JS, Ford B, Hultgren SJ, Frieden C. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-10-20T10:53:58.297Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP03852r001","statement":[{"text":"Immediately after removal of Gdn and initiating the aggregation process, the CD spectra of both CsgA and CsgB are characteristic of a random coil with a minimum close to 200 nm and little signal elsewhere.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T15:32:53.817Z"}},{"start":1,"end":151,"reference_id":"22493266","reference_source":"pmid","reference_html":"The E. coli CsgB nucleator of curli assembles to β-sheet oligomers that alter the CsgA fibrillization mechanism. <i> Shu Q, Crick SL, Pinkner JS, Ford B, Hultgren SJ, Frieden C. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-10-20T10:56:36.321Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP03852r002","statement":[{"text":"In contrast, the CD signal of CsgB rapidly increased at 200 nm and decreased at 216 nm, indicating the appearance of β-sheet structure (Fig. 3B). The CD change of CsgB at either 200 nm or 216 nm could be fit by a single exponential function with a half-time of 180 min (Fig. 3E and Table 1).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T15:32:55.423Z"}},{"start":1,"end":151,"reference_id":"22493266","reference_source":"pmid","reference_html":"The E. coli CsgB nucleator of curli assembles to β-sheet oligomers that alter the CsgA fibrillization mechanism. <i> Shu Q, Crick SL, Pinkner JS, Ford B, Hultgren SJ, Frieden C. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-10-20T10:57:31.934Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP03852r003","statement":[{"text":"However, the intrinsic fluorescence of CsgB alone, excited at 280 nm, shows an exponential decrease as a function of time (Fig. 6F) with a rate constant similar to the change in CD signal (Fig. 3E), confirming that the structure of CsgB rapidly changes with a single exponential rate during its aggregation.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T15:32:54.960Z"}},{"start":1,"end":151,"reference_id":"22493266","reference_source":"pmid","reference_html":"The E. coli CsgB nucleator of curli assembles to β-sheet oligomers that alter the CsgA fibrillization mechanism. <i> Shu Q, Crick SL, Pinkner JS, Ford B, Hultgren SJ, Frieden C. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-10-20T11:06:57.406Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","region_id":"DP03852r004","statement":[{"text":"Fig. 1A shows the time dependence for CsgB aggregation as a function of CsgB concentration.","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"cross_refs":[{"db":"AmyPro","id":"AP00037"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T15:33:00.872Z"}},{"start":1,"end":151,"reference_id":"22493266","reference_source":"pmid","reference_html":"The E. coli CsgB nucleator of curli assembles to β-sheet oligomers that alter the CsgA fibrillization mechanism. <i> Shu Q, Crick SL, Pinkner JS, Ford B, Hultgren SJ, Frieden C. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-10-20T11:02:43.217Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:1905906","term_name":"regulation of amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","region_id":"DP03852r005","statement":[{"text":"Seeds (oligomers) of CsgB abolished the lag phase of CsgA and of CsgB (Fig. 2 A and B). The results suggest that CsgB oligomers accelerate CsgA aggregation.","type":"Results"},{"text":"CsgA is unable to polymerize in the absence of CsgB; thus, in the absence of either CsgA or CsgB, no surface structures are observed (5). ","type":"Discussion"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"Any process that modulates the frequency, rate or extent of amyloid fibril formation.\" [GO_REF:0000058, GOC:aruk, GOC:bc, GOC:TermGenie, PMID:23106396]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T15:32:57.425Z"}},{"start":1,"end":151,"reference_id":"22493266","reference_source":"pmid","reference_html":"The E. coli CsgB nucleator of curli assembles to β-sheet oligomers that alter the CsgA fibrillization mechanism. <i> Shu Q, Crick SL, Pinkner JS, Ford B, Hultgren SJ, Frieden C. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-10-20T11:04:05.877Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:1905906","term_name":"regulation of amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","region_id":"DP03852r006","statement":[{"text":"In these experiments the CD changes were fit by a two-exponential function (Table 1). Interestingly, the rate constant for the first phase is near that of CsgB alone (Table 1), suggesting that this fast phase is mostly due to the rapid polymerization of CsgB. Thus, it is clear that CsgB rapidly forms oligomers that change the aggregation mechanism of CsgA.","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"Any process that modulates the frequency, rate or extent of amyloid fibril formation.\" [GO_REF:0000058, GOC:aruk, GOC:bc, GOC:TermGenie, PMID:23106396]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T15:32:56.299Z"}}],"regions_counter":6,"released":"2022_12","sequence":"MKNKLLFMMLTILGAPGIAAAAGYDLANSEYNFAVNELSKSSFNQAAIIGQAGTNNSAQLRQGGSKLLAVVAQEGSSNRAKIDQTGDYNLAYIDQAGSANDASISQGAYGNTAMIIQKGSGNKANITQYGTQKTAIVVQRQSQMAIRVTQR","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":["Extracellular matrix proteins","Condensates-related proteins"],"alphafold_very_low_content":0.26490066225165565,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":151,"type":"T"}],"Structural state":[{"start":1,"end":151,"type":"D"}],"Structural transition":[{"start":1,"end":151,"type":"T"}],"Biological process":[{"start":1,"end":151,"type":"F"}]}},{"disprot_id":"DP03853","acc":"P28307","creator":"jssuarez","date":"2022-10-20T11:04:50.934Z","features":{"pfam":[{"id":"PF07012","name":"Curlin associated repeat","start":40,"end":74},{"id":"PF07012","name":"Curlin associated repeat","start":86,"end":119}],"gene3D":[]},"genes":[{"name":{"value":"csgA"},"olnNames":[{"value":"b1042"},{"value":"JW1025"}]}],"length":151,"name":"Major curlin subunit","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":1,"end":151,"reference_id":"22493266","reference_source":"pmid","reference_html":"The E. coli CsgB nucleator of curli assembles to β-sheet oligomers that alter the CsgA fibrillization mechanism. <i> Shu Q, Crick SL, Pinkner JS, Ford B, Hultgren SJ, Frieden C. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-10-20T11:07:35.490Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP03853r001","statement":[{"text":"Immediately after removal of Gdn and initiating the aggregation process, the CD spectra of both CsgA and CsgB are characteristic of a random coil with a minimum close to 200 nm and little signal elsewhere.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T15:35:16.902Z"}},{"start":1,"end":151,"reference_id":"22493266","reference_source":"pmid","reference_html":"The E. coli CsgB nucleator of curli assembles to β-sheet oligomers that alter the CsgA fibrillization mechanism. <i> Shu Q, Crick SL, Pinkner JS, Ford B, Hultgren SJ, Frieden C. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-10-20T11:11:45.993Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","region_id":"DP03853r002","statement":[{"text":"The effect of monomeric CsgB on the aggregation of CsgA was investigated using the ThT assay. A 1:1 mixture of monomeric CsgA and CsgB (4 μM each) was observed to have a lag phase similar to that of CsgB alone over the first 100 min (Fig. 1B). Thus, the lag phase typical of CsgA alone disappeared (Fig. 1B). ","type":"Results"},{"text":"The intrinsic fluorescence of CsgA alone, excited at 280 nm, shows a small linear decrease over time, monitored by either tyrosine or tryptophan signal (Fig. 6E), which is probably due to the loss of soluble protein during the aggregation process.","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"cross_refs":[{"db":"AmyPro","id":"AP00036"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T15:37:46.956Z"}},{"start":1,"end":151,"reference_id":"22493266","reference_source":"pmid","reference_html":"The E. coli CsgB nucleator of curli assembles to β-sheet oligomers that alter the CsgA fibrillization mechanism. <i> Shu Q, Crick SL, Pinkner JS, Ford B, Hultgren SJ, Frieden C. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-10-20T11:11:09.478Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP03853r003","statement":[{"text":"At very long times (9–13 d), the CD spectrum of CsgA shows a weak minimum signal at ~220 nm, rather than at 216 nm, but probably characteristic of some β-sheet structures (Fig. 3 C and D).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T15:36:06.678Z"}},{"start":1,"end":151,"reference_id":"11823641","reference_source":"pmid","reference_html":"Role of Escherichia coli curli operons in directing amyloid fiber formation. <i> Chapman MR, Robinson LS, Pinkner JS, Roth R, Heuser J, Hammar M, Normark S, Hultgren SJ. </i> Science, 2002","date":"2022-10-20T11:14:27.336Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP03853r004","statement":[{"text":"Immediately after elution from the nitrilotriacetic acid (NTA) agarose column, solutions containing purified CsgA-his were clear with no evidence of aggregation, and EM of this material revealed no fibers (9). CD analysis of this material indicated that soluble CsgA-his, unlike curli, was not rich in β-sheet secondary structure (Fig. 4C).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T16:13:54.186Z"}},{"start":1,"end":151,"reference_id":"11823641","reference_source":"pmid","reference_html":"Role of Escherichia coli curli operons in directing amyloid fiber formation. <i> Chapman MR, Robinson LS, Pinkner JS, Roth R, Heuser J, Hammar M, Normark S, Hultgren SJ. </i> Science, 2002","date":"2022-11-02T09:01:22.559Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","region_id":"DP03853r005","statement":[{"text":"However, after prolonged incubation (4°C for 4 to 12 hours), the CsgA-his solutions became opaque and noticeably viscous. EM analysis revealed that fibers had formed that were similar to those produced by wild-type bacteria (Fig. 4D).","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"cross_refs":[{"db":"AmyPro","id":"AP00036"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-16T15:46:39.918Z"}},{"start":1,"end":151,"reference_id":"17164238","reference_source":"pmid","reference_html":"In vitro polymerization of a functional Escherichia coli amyloid protein. <i> Wang X, Smith DR, Jones JW, Chapman MR. </i> J Biol Chem, 2007","date":"2022-10-20T11:33:48.996Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP03853r006","statement":[{"text":"Circular dichroism spectrum indicated that immediately after purification, CsgA was largely unstructured (Fig. 1B). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T15:54:01.436Z"}},{"start":1,"end":151,"reference_id":"17164238","reference_source":"pmid","reference_html":"In vitro polymerization of a functional Escherichia coli amyloid protein. <i> Wang X, Smith DR, Jones JW, Chapman MR. </i> J Biol Chem, 2007","date":"2022-10-20T11:35:53.292Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP03853r007","statement":[{"text":"Circular dichroism spectrum indicated that immediately after purification, CsgA was largely unstructured (Fig. 1B). However, CsgA adopted a β-sheet-rich structure after 2 days of incubation at room temperature (Fig. 1B). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T15:54:21.336Z"}},{"start":1,"end":151,"reference_id":"32398666","reference_source":"pmid","reference_html":"NMR insights into the pre-amyloid ensemble and secretion targeting of the curli subunit CsgA. <i> Sewell L, Stylianou F, Xu Y, Taylor J, Sefer L, Matthews S. </i> Sci Rep, 2020","date":"2022-11-02T08:50:43.434Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP03853r008","statement":[{"text":"Use of higher strength magnetic fields (950 MHz) improved resolution for regions with the limited dispersion that is typical of IDPs.","type":"Results"},{"text":"Backbone assignment of the disordered, pre-fibril CsgA.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-12T15:11:24.074Z"}},{"start":1,"end":22,"reference_id":"32398666","reference_source":"pmid","reference_html":"NMR insights into the pre-amyloid ensemble and secretion targeting of the curli subunit CsgA. <i> Sewell L, Stylianou F, Xu Y, Taylor J, Sefer L, Matthews S. </i> Sci Rep, 2020","date":"2022-10-24T07:59:48.138Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P0AEA2","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03853r010","statement":[{"text":"Our N22 peptide data showed a specific interaction with a dissociation constant in the micromolar range (0.53 μM; Fig. 3).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T15:48:16.387Z"}},{"start":1,"end":151,"reference_id":"17164238","reference_source":"pmid","reference_html":"In vitro polymerization of a functional Escherichia coli amyloid protein. <i> Wang X, Smith DR, Jones JW, Chapman MR. </i> J Biol Chem, 2007","date":"2022-11-02T09:03:26.469Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007044","ec_ontology":"ECO","ec_name":"transmission electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"AmyPro","id":"AP00036"}],"ec_go":"IDA","region_id":"DP03853r011","statement":[{"text":"Immediately after purification, there was no apparent fiber formation or aggregation by TEM (Fig. 1C). Two hours after purification, regular, unbranched fibers were readily observed (Fig. 1D). Dense fiber aggregates were also observed 7 days after purification (Fig. 1E).","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-12T15:12:55.541Z"}},{"start":43,"end":65,"reference_id":"17164238","reference_source":"pmid","reference_html":"In vitro polymerization of a functional Escherichia coli amyloid protein. <i> Wang X, Smith DR, Jones JW, Chapman MR. </i> J Biol Chem, 2007","date":"2022-11-02T09:06:12.390Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007044","ec_ontology":"ECO","ec_name":"transmission electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","region_id":"DP03853r012","statement":[{"text":"Peptides corresponding to repeating unit 1, 3 or 5 (R1, R3, or R5) produced a ThT-positive signal and self-assembled into fibers as evidenced by TEM when incubated at 0.2 mg/ml (Fig. 4, B–E).","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-12T15:13:23.145Z"}},{"start":43,"end":65,"reference_id":"17164238","reference_source":"pmid","reference_html":"In vitro polymerization of a functional Escherichia coli amyloid protein. <i> Wang X, Smith DR, Jones JW, Chapman MR. </i> J Biol Chem, 2007","date":"2022-11-02T09:06:24.741Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","region_id":"DP03853r013","statement":[{"text":"Peptides corresponding to repeating unit 1, 3 or 5 (R1, R3, or R5) produced a ThT-positive signal and self-assembled into fibers as evidenced by TEM when incubated at 0.2 mg/ml (Fig. 4, B–E).","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-12T15:13:39.950Z"}},{"start":88,"end":110,"reference_id":"17164238","reference_source":"pmid","reference_html":"In vitro polymerization of a functional Escherichia coli amyloid protein. <i> Wang X, Smith DR, Jones JW, Chapman MR. </i> J Biol Chem, 2007","date":"2022-11-02T09:06:32.386Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","region_id":"DP03853r014","statement":[{"text":"Peptides corresponding to repeating unit 1, 3 or 5 (R1, R3, or R5) produced a ThT-positive signal and self-assembled into fibers as evidenced by TEM when incubated at 0.2 mg/ml (Fig. 4, B–E).","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-12T15:13:52.223Z"}},{"start":88,"end":110,"reference_id":"17164238","reference_source":"pmid","reference_html":"In vitro polymerization of a functional Escherichia coli amyloid protein. <i> Wang X, Smith DR, Jones JW, Chapman MR. </i> J Biol Chem, 2007","date":"2022-11-02T09:06:48.640Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007044","ec_ontology":"ECO","ec_name":"transmission electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","region_id":"DP03853r015","statement":[{"text":"Peptides corresponding to repeating unit 1, 3 or 5 (R1, R3, or R5) produced a ThT-positive signal and self-assembled into fibers as evidenced by TEM when incubated at 0.2 mg/ml (Fig. 4, B–E).","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-12T15:13:55.717Z"}},{"start":133,"end":151,"reference_id":"17164238","reference_source":"pmid","reference_html":"In vitro polymerization of a functional Escherichia coli amyloid protein. <i> Wang X, Smith DR, Jones JW, Chapman MR. </i> J Biol Chem, 2007","date":"2022-11-02T09:06:55.905Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007044","ec_ontology":"ECO","ec_name":"transmission electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","region_id":"DP03853r016","statement":[{"text":"Peptides corresponding to repeating unit 1, 3 or 5 (R1, R3, or R5) produced a ThT-positive signal and self-assembled into fibers as evidenced by TEM when incubated at 0.2 mg/ml (Fig. 4, B–E).","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-12T15:13:59.177Z"}},{"start":133,"end":151,"reference_id":"17164238","reference_source":"pmid","reference_html":"In vitro polymerization of a functional Escherichia coli amyloid protein. <i> Wang X, Smith DR, Jones JW, Chapman MR. </i> J Biol Chem, 2007","date":"2022-11-02T09:07:11.077Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","region_id":"DP03853r017","statement":[{"text":"Peptides corresponding to repeating unit 1, 3 or 5 (R1, R3, or R5) produced a ThT-positive signal and self-assembled into fibers as evidenced by TEM when incubated at 0.2 mg/ml (Fig. 4, B–E).","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-12T15:14:00.565Z"}},{"start":66,"end":87,"reference_id":"17164238","reference_source":"pmid","reference_html":"In vitro polymerization of a functional Escherichia coli amyloid protein. <i> Wang X, Smith DR, Jones JW, Chapman MR. </i> J Biol Chem, 2007","date":"2022-11-02T09:08:25.966Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007044","ec_ontology":"ECO","ec_name":"transmission electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","region_id":"DP03853r018","statement":[{"text":"Neither R2 nor R4 showed evidence of amyloidogenesis when resuspended at a concentration of 0.2 mg/ml, although fibers were observed by TEM when R2 or R4 was incubated at 2 mg/ml (Fig. 4B and data not shown)","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-12T15:17:08.503Z"}},{"start":111,"end":132,"reference_id":"17164238","reference_source":"pmid","reference_html":"In vitro polymerization of a functional Escherichia coli amyloid protein. <i> Wang X, Smith DR, Jones JW, Chapman MR. </i> J Biol Chem, 2007","date":"2022-11-02T09:08:45.198Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007044","ec_ontology":"ECO","ec_name":"transmission electron microscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","region_id":"DP03853r019","statement":[{"text":"Neither R2 nor R4 showed evidence of amyloidogenesis when resuspended at a concentration of 0.2 mg/ml, although fibers were observed by TEM when R2 or R4 was incubated at 2 mg/ml (Fig. 4B and data not shown)","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-12T15:17:09.798Z"}},{"start":1,"end":151,"reference_id":"17164238","reference_source":"pmid","reference_html":"In vitro polymerization of a functional Escherichia coli amyloid protein. <i> Wang X, Smith DR, Jones JW, Chapman MR. </i> J Biol Chem, 2007","date":"2022-11-02T09:10:25.839Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:1905906","term_name":"regulation of amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"IDA","region_id":"DP03853r020","statement":[{"text":"We tested the hypothesis that preformed CsgA fibers could catalyze CsgA polymerization. The addition of 2.5% (w/w) sonicated CsgA fibers to freshly purified, soluble CsgA resulted in a significant reduction of the lag phase (Fig. 3A).","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"Any process that modulates the frequency, rate or extent of amyloid fibril formation.\" [GO_REF:0000058, GOC:aruk, GOC:bc, GOC:TermGenie, PMID:23106396]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-12T15:17:19.105Z"}}],"regions_counter":20,"released":"2022_12","sequence":"MKLLKVAAIAAIVFSGSALAGVVPQYGGGGNHGGGGNNSGPNSELNIYQYGGGNSALALQTDARNSDLTITQHGGGNGADVGQGSDDSSIDLTQRGFGNSATLDQWNGKNSEMTVKQFGGGNGAAVDQTASNSSVNVTQVGFGNNATAHQY","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"dataset":["Extracellular matrix proteins","Condensates-related proteins"],"alphafold_very_low_content":0.2052980132450331,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":151,"type":"T"}],"Structural state":[{"start":1,"end":151,"type":"D"}],"Biological process":[{"start":1,"end":151,"type":"F"}],"Structural transition":[{"start":1,"end":151,"type":"T"}],"Molecular function":[{"start":1,"end":22,"type":"F"}]}},{"disprot_id":"DP03854","acc":"Q99714","creator":"fkordevani","date":"2022-10-20T14:20:59.775Z","features":{"pfam":[{"id":"PF00106","name":"short chain dehydrogenase","start":12,"end":211}],"gene3D":[]},"genes":[{"name":{"value":"HSD17B10"},"synonyms":[{"value":"ERAB"},{"value":"HADH2"},{"value":"MRPP2"},{"value":"SCHAD"},{"value":"SDR5C1"},{"value":"XH98G2"}]}],"length":261,"name":"3-hydroxyacyl-CoA dehydrogenase type-2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":95,"end":113,"reference_id":"15087549","reference_source":"pmid","reference_html":"ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease. <i> Lustbader JW, Cirilli M, Lin C, Xu HW, Takuma K, Wang N, Caspersen C, Chen X, Pollak S, Chaney M, Trinchese F, Liu S, Gunn-Moore F, Lue LF, Walker DG, Kuppusamy P, Zewier ZL, Arancio O, Stern D, Yan SS, Wu H. </i> Science, 2004","date":"2022-10-20T14:40:32.572Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1SO8"}],"region_id":"DP03854r001","statement":[{"text":"However, no electron density is observed for Aβ, suggesting that Aβ itself and the region of ABAD that binds to Aβ must be disordered in the crystal.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-25T16:34:40.408Z"}},{"start":208,"end":228,"reference_id":"15087549","reference_source":"pmid","reference_html":"ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease. <i> Lustbader JW, Cirilli M, Lin C, Xu HW, Takuma K, Wang N, Caspersen C, Chen X, Pollak S, Chaney M, Trinchese F, Liu S, Gunn-Moore F, Lue LF, Walker DG, Kuppusamy P, Zewier ZL, Arancio O, Stern D, Yan SS, Wu H. </i> Science, 2004","date":"2022-10-27T08:13:10.784Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1SO8"}],"region_id":"DP03854r002","statement":[{"text":"The majority of the LD loop, the beginning of the following αD helix, and the latter part of the LF loop of human ABAD are disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-02T12:41:45.855Z"}},{"start":97,"end":102,"reference_id":"15087549","reference_source":"pmid","reference_html":"ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease. <i> Lustbader JW, Cirilli M, Lin C, Xu HW, Takuma K, Wang N, Caspersen C, Chen X, Pollak S, Chaney M, Trinchese F, Liu S, Gunn-Moore F, Lue LF, Walker DG, Kuppusamy P, Zewier ZL, Arancio O, Stern D, Yan SS, Wu H. </i> Science, 2004","date":"2022-10-27T08:13:34.477Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IMP","region_id":"DP03854r003","statement":[{"text":"Site-directed mutagenesis within and beyond the disordered LD loop region (residues 95 to 113) specifically located two stretches of ABAD residues important for Aβ binding: residues S98 to Y101 (10) and residues T108 to T110. An ABAD mutant bearing Ser98->Ala98 (S98A), K99A, and Y101A mutations exhibited no specific interaction to Aβ in a surface plasmon resonance experiment, although wild-type ABAD displayed dosedependent interaction with Aβ (Fig. 3A)","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-02T12:41:47.673Z"}}],"regions_counter":3,"released":"2023_06","sequence":"MAAACRSVKGLVAVITGGASGLGLATAERLVGQGASAVLLDLPNSGGEAQAKKLGNNCVFAPADVTSEKDVQTALALAKGKFGRVDVAVNCAGIAVASKTYNLKKGQTHTLEDFQRVLDVNLMGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGIRVMTIAPGLFGTPLLTSLPEKVCNFLASQVPFPSRLGDPAEYAHLVQAIIENPFLNGEVIRLDGAIRMQP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.0038314176245210726,"disorder_content":0.1532567049808429,"disprot_consensus":{"full":[{"start":95,"end":113,"type":"D"},{"start":208,"end":228,"type":"D"}],"Structural state":[{"start":95,"end":113,"type":"D"},{"start":208,"end":228,"type":"D"}],"Molecular function":[{"start":97,"end":102,"type":"F"}]}},{"disprot_id":"DP03856","acc":"P35475","creator":"fkordevani","date":"2022-10-20T14:54:35.963Z","features":{"pfam":[{"id":"PF01229","name":"Glycosyl hydrolases family 39","start":30,"end":525},{"id":"PF21200","name":"Alpha-L-iduronidase C-terminal domain","start":552,"end":640}],"gene3D":[]},"genes":[{"name":{"value":"IDUA"}}],"length":653,"name":"Alpha-L-iduronidase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":643,"end":653,"reference_id":"24036510","reference_source":"pmid","reference_html":"Insights into mucopolysaccharidosis I from the structure and action of α-L-iduronidase. <i> Bie H, Yin J, He X, Kermode AR, Goddard-Borger ED, Withers SG, James MN. </i> Nat Chem Biol, 2013","date":"2022-10-24T08:21:39.717Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4MJ2"},{"db":"PDB","id":"4MJ4"},{"db":"PDB","id":"4KGL"},{"db":"PDB","id":"4KGJ"},{"db":"PDB","id":"4KH2"}],"region_id":"DP03856r002","statement":[{"text":"The last residue that is visible in our electron density maps is Pro642. The remaining 11 residues are disordered in the present structures (from Val643 to Pro653).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-25T12:58:01.970Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MRPLRPRAALLALLASLLAAPPVAPAEAPHLVHVDAARALWPLRRFWRSTGFCPPLPHSQADQYVLSWDQQLNLAYVGAVPHRGIKQVRTHWLLELVTTRGSTGRGLSYNFTHLDGYLDLLRENQLLPGFELMGSASGHFTDFEDKQQVFEWKDLVSSLARRYIGRYGLAHVSKWNFETWNEPDHHDFDNVSMTMQGFLNYYDACSEGLRAASPALRLGGPGDSFHTPPRSPLSWGLLRHCHDGTNFFTGEAGVRLDYISLHRKGARSSISILEQEKVVAQQIRQLFPKFADTPIYNDEADPLVGWSLPQPWRADVTYAAMVVKVIAQHQNLLLANTTSAFPYALLSNDNAFLSYHPHPFAQRTLTARFQVNNTRPPHVQLLRKPVLTAMGLLALLDEEQLWAEVSQAGTVLDSNHTVGVLASAHRPQGPADAWRAAVLIYASDDTRAHPNRSVAVTLRLRGVPPGPGLVYVTRYLDNGLCSPDGEWRRLGRPVFPTAEQFRRMRAAEDPVAAAPRPLPAGGRLTLRPALRLPSLLLVHVCARPEKPPGQVTRLRALPLTQGQLVLVWSDEHVGSKCLWTYEIQFSQDGKAYTPVSRKPSTFNLFVFSPDTGAVSGSYRVRALDYWARPGPFSDPVPYLEVPVPRGPPSPGNP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.036753445635528334,"disorder_content":0.016845329249617153,"disprot_consensus":{"full":[{"start":643,"end":653,"type":"D"}],"Structural state":[{"start":643,"end":653,"type":"D"}]}},{"disprot_id":"DP03857","acc":"P05019","creator":"fkordevani","date":"2022-10-20T15:01:06.765Z","features":{"pfam":[{"id":"PF00049","name":"Insulin/IGF/Relaxin family","start":51,"end":109}],"gene3D":[]},"genes":[{"name":{"value":"IGF1"},"synonyms":[{"value":"IBP1"}]}],"length":195,"name":"Insulin-like growth factor I","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":70,"end":90,"reference_id":"30242155","reference_source":"pmid","reference_html":"Structures of insect Imp-L2 suggest an alternative strategy for regulating the bioavailability of insulin-like hormones. <i> Roed NK, Viola CM, Kristensen O, Schluckebier G, Norrman M, Sajid W, Wade JD, Andersen AS, Kristensen C, Ganderton TR, Turkenburg JP, De Meyts P, Brzozowski AM. </i> Nat Commun, 2018","date":"2022-10-20T15:04:07.041Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6FF3"}],"region_id":"DP03857r001","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T15:54:45.811Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MGKISSLPTQLFKCCFCDFLKVKMHTMSSSHLFYLALCLLTFTSSATAGPETLCGAELVDALQFVCGDRGFYFNKPTGYGSSSRRAPQTGIVDECCFRSCDLRRLEMYCAPLKPAKSARSVRAQRHTDMPKTQKYQPPSTNKNTKSQRRKGWPKTHPGGEQKEGTEASLQIRGKKKEQRREIGSRNAECRGKKGK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.2717948717948718,"disorder_content":0.1076923076923077,"disprot_consensus":{"full":[{"start":70,"end":90,"type":"D"}],"Structural state":[{"start":70,"end":90,"type":"D"}]}},{"disprot_id":"DP03859","acc":"Q2M1P5","creator":"fkordevani","date":"2022-10-21T08:26:42.036Z","features":{"pfam":[{"id":"PF00225","name":"Kinesin motor domain","start":21,"end":349},{"id":"PF25764","name":"KIF21A-like domain","start":690,"end":866}],"gene3D":[]},"genes":[{"name":{"value":"KIF7"},"orfNames":[{"value":"UNQ340/PRO539"}]}],"length":1343,"name":"Kinesin-like protein KIF7","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":349,"end":543,"reference_id":"35725768","reference_source":"pmid","reference_html":"Cytoskeletal regulation of a transcription factor by DNA mimicry via coiled-coil interactions. <i> Haque F, Freniere C, Ye Q, Mani N, Wilson-Kubalek EM, Ku PI, Milligan RA, Subramanian R. </i> Nat Cell Biol, 2022","date":"2022-10-21T08:31:50.942Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7RX0"}],"region_id":"DP03859r001","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T16:12:18.366Z"}},{"start":349,"end":398,"reference_id":"31031197","reference_source":"pmid","reference_html":"Interplay between the Kinesin and Tubulin Mechanochemical Cycles Underlies Microtubule Tip Tracking by the Non-motile Ciliary Kinesin Kif7. <i> Jiang S, Mani N, Wilson-Kubalek EM, Ku PI, Milligan RA, Subramanian R. </i> Dev Cell, 2019","date":"2022-10-25T13:04:49.257Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6MLR"},{"db":"PDB","id":"6MLQ"}],"region_id":"DP03859r002","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-25T13:18:04.277Z"}},{"start":261,"end":273,"reference_id":"22281744","reference_source":"pmid","reference_html":"Structural insights into human Kif7, a kinesin involved in Hedgehog signalling. <i> Klejnot M, Kozielski F. </i> Acta Crystallogr D Biol Crystallogr, 2012","date":"2023-05-15T15:11:51.745Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2XT3"},{"db":"PDB","id":"4A14"}],"region_id":"DP03859r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"}],"statement":[{"text":"The final structure included residues 12–347 (missing regions: 107–114, 207–211, 230–241, 260–273) with bound Mg2+ADP (octahedrally co­ordinated) in the catalytic site and 328 water molecules.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-15T15:28:07.213Z"}},{"start":230,"end":241,"reference_id":"22281744","reference_source":"pmid","reference_html":"Structural insights into human Kif7, a kinesin involved in Hedgehog signalling. <i> Klejnot M, Kozielski F. </i> Acta Crystallogr D Biol Crystallogr, 2012","date":"2023-05-15T15:12:31.234Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4A14"}],"region_id":"DP03859r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"}],"statement":[{"text":"The final structure included residues 12–347 (missing regions: 107–114, 207–211, 230–241, 260–273) with bound Mg2+ADP (octahedrally co­ordinated) in the catalytic site and 328 water molecules.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-15T15:28:08.606Z"}}],"regions_counter":4,"released":"2023_06","sequence":"MGLEAQRLPGAEEAPVRVALRVRPLLPKELLHGHQSCLQVEPGLGRVTLGRDRHFGFHVVLAEDAGQEAVYQACVQPLLEAFFEGFNATVFAYGQTGSGKTYTMGEASVASLLEDEQGIVPRAMAEAFKLIDENDLLDCLVHVSYLEVYKEEFRDLLEVGTASRDIQLREDERGNVVLCGVKEVDVEGLDEVLSLLEMGNAARHTGATHLNHLSSRSHTVFTVTLEQRGRAPSRLPRPAPGQLLVSKFHFVDLAGSERVLKTGSTGERLKESIQINSSLLALGNVISALGDPQRRGSHIPYRDSKITRILKDSLGGNAKTVMIACVSPSSSDFDETLNTLNYASRAQNIRNRATVNWRPEAERPPEETASGARGPPRHRSETRIIHRGRRAPGPATASAAAAMRLGAECARYRACTDAAYSLLRELQAEPGLPGAAARKVRDWLCAVEGERSALSSASGPDSGIESASVEDQAAQGAGGRKEDEGAQQLLTLQNQVARLEEENRDFLAALEDAMEQYKLQSDRLREQQEEMVELRLRLELVRPGWGGPRLLNGLPPGSFVPRPHTAPLGGAHAHVLGMVPPACLPGDEVGSEQRGEQVTNGREAGAELLTEVNRLGSGSSAASEEEEEEEEPPRRTLHLRRNRISNCSQRAGARPGSLPERKGPELCLEELDAAIPGSRAVGGSKARVQARQVPPATASEWRLAQAQQKIRELAINIRMKEELIGELVRTGKAAQALNRQHSQRIRELEQEAEQVRAELSEGQRQLRELEGKELQDAGERSRLQEFRRRVAAAQSQVQVLKEKKQATERLVSLSAQSEKRLQELERNVQLMRQQQGQLQRRLREETEQKRRLEAEMSKRQHRVKELELKHEQQQKILKIKTEEIAAFQRKRRSGSNGSVVSLEQQQKIEEQKKWLDQEMEKVLQQRRALEELGEELHKREAILAKKEALMQEKTGLESKRLRSSQALNEDIVRVSSRLEHLEKELSEKSGQLRQGSAQSQQQIRGEIDSLRQEKDSLLKQRLEIDGKLRQGSLLSPEEERTLFQLDEAIEALDAAIEYKNEAITCRQRVLRASASLLSQCEMNLMAKLSYLSSSETRALLCKYFDKVVTLREEQHQQQIAFSELEMQLEEQQRLVYWLEVALERQRLEMDRQLTLQQKEHEQNMQLLLQQSRDHLGEGLADSRRQYEARIQALEKELGRYMWINQELKQKLGGVNAVGHSRGGEKRSLCSEGRQAPGNEDELHLAPELLWLSPLTEGAPRTREETRDLVHAPLPLTWKRSSLCGEEQGSPEELRQREAAEPLVGRVLPVGEAGLPWNFGPLSKPRRELRRASPGMIDVRKNPL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.2933730454206999,"disorder_content":0.16381236038719285,"disprot_consensus":{"full":[{"start":230,"end":241,"type":"D"},{"start":261,"end":273,"type":"D"},{"start":349,"end":543,"type":"D"}],"Structural state":[{"start":230,"end":241,"type":"D"},{"start":261,"end":273,"type":"D"},{"start":349,"end":543,"type":"D"}]}},{"disprot_id":"DP03860","acc":"P01116","creator":"fkordevani","date":"2022-10-21T08:39:12.369Z","features":{"pfam":[{"id":"PF00071","name":"Ras family","start":5,"end":164}],"gene3D":[]},"genes":[{"name":{"value":"KRAS"},"synonyms":[{"value":"KRAS2"},{"value":"RASK2"}]}],"length":189,"name":"GTPase KRas","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":174,"end":189,"reference_id":"30093669","reference_source":"pmid","reference_html":"Small molecule inhibitors of RAS-effector protein interactions derived using an intracellular antibody fragment. <i> Quevedo CE, Cruz-Migoni A, Bery N, Miller A, Tanaka T, Petch D, Bataille CJR, Lee LYW, Fallon PS, Tulmin H, Ehebauer MT, Fernandez-Fuentes N, Russell AJ, Carr SB, Phillips SEV, Rabbitts TH. </i> Nat Commun, 2018","date":"2023-05-22T13:21:53.249Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5OCG"}],"region_id":"DP03860r001","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:135403657"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:73424803"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:8117"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-22T13:22:36.000Z"}},{"start":167,"end":189,"reference_id":"35522713","reference_source":"pmid","reference_html":"Structural insights into Ras regulation by SIN1. <i> Zheng Y, Ding L, Meng X, Potter M, Kearney AL, Zhang J, Sun J, James DE, Yang G, Zhou C. </i> Proc Natl Acad Sci U S A, 2022","date":"2022-10-24T08:28:48.732Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7VVB"}],"region_id":"DP03860r002","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-25T13:17:12.339Z"}},{"start":60,"end":70,"reference_id":"26037647","reference_source":"pmid","reference_html":"Biochemical and Structural Analysis of Common Cancer-Associated KRAS Mutations. <i> Hunter JC, Manandhar A, Carrasco MA, Gurbani D, Gondi S, Westover KD. </i> Mol Cancer Res, 2015","date":"2022-10-21T08:54:20.296Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4WA7"}],"region_id":"DP03860r003","statement":[{"text":"The structure of Q61L mutant form of KRAS showed good density for all regions of the protein except for residues 60 to 70 (including L61) on switch 2 that were disordered and the density was insufficient to build this region into our model.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T16:27:30.741Z"}},{"start":60,"end":64,"reference_id":"26037647","reference_source":"pmid","reference_html":"Biochemical and Structural Analysis of Common Cancer-Associated KRAS Mutations. <i> Hunter JC, Manandhar A, Carrasco MA, Gurbani D, Gondi S, Westover KD. </i> Mol Cancer Res, 2015","date":"2022-10-25T13:08:28.487Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"GO:0003924","term_name":"GTPase activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IMP","region_id":"DP03860r004","statement":[{"text":"The G12C mutation had minimal impact on the intrinsic hydrolysis rate while mutation of G12 to A or R and mutation of Q61 to H or L lead to an approximately 40- to 80-fold decrease in GTP hydrolysis rate.","type":"Results"}],"term_comment":"","term_def":"\"Catalysis of the reaction: GTP + H2O = GDP + phosphate.\" [ISBN:0198547684, PMID:26832457, PMID:27218782]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-25T13:17:18.357Z"}}],"regions_counter":4,"released":"2023_06","sequence":"MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCIIM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Cancer-related proteins","Condensates-related proteins"],"alphafold_very_low_content":0.010582010582010581,"disorder_content":0.17989417989417988,"disprot_consensus":{"full":[{"start":60,"end":70,"type":"D"},{"start":167,"end":189,"type":"D"}],"Structural state":[{"start":60,"end":70,"type":"D"},{"start":167,"end":189,"type":"D"}],"Molecular function":[{"start":60,"end":64,"type":"F"}]}},{"disprot_id":"DP03861","acc":"P36776","creator":"fkordevani","date":"2022-10-21T08:59:14.791Z","features":{"pfam":[{"id":"PF00004","name":"ATPase family associated with various cellular activities (AAA)","start":519,"end":656},{"id":"PF02190","name":"ATP-dependent protease La (LON) substrate-binding domain","start":124,"end":368},{"id":"PF05362","name":"Lon protease (S16) C-terminal proteolytic domain","start":737,"end":947},{"id":"PF22667","name":"Lon protease AAA+ ATPase lid domain","start":682,"end":733}],"gene3D":[]},"genes":[{"name":{"value":"LONP1","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03120","url":"https://hamap.expasy.org/unirule/MF_03120"}}]},"synonyms":[{"value":"PRSS15"}]}],"length":959,"name":"Lon protease homolog, mitochondrial","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":122,"reference_id":"35870450","reference_source":"pmid","reference_html":"Catalytic cycling of human mitochondrial Lon protease. <i> Mohammed I, Schmitz KA, Schenck N, Balasopoulos D, Topitsch A, Maier T, Abrahams JP. </i> Structure, 2022","date":"2022-10-27T08:11:12.095Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7OXO"}],"region_id":"DP03861r001","statement":[{"text":"All three models indicated residues 355-407 to form a long α-helix extending away from the globular domain and residues 1-123 and 221-272 to form unstructured loops.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-02T12:47:35.317Z"}},{"start":222,"end":271,"reference_id":"35870450","reference_source":"pmid","reference_html":"Catalytic cycling of human mitochondrial Lon protease. <i> Mohammed I, Schmitz KA, Schenck N, Balasopoulos D, Topitsch A, Maier T, Abrahams JP. </i> Structure, 2022","date":"2022-10-27T08:11:41.145Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7OXO"},{"db":"PDB","id":"7NG4"},{"db":"PDB","id":"7NGP"},{"db":"PDB","id":"7NGQ"},{"db":"PDB","id":"7NG5"},{"db":"PDB","id":"7NFY"}],"region_id":"DP03861r002","statement":[{"text":"All three models indicated residues 355-407 to form a long α-helix extending away from the globular domain and residues 1-123 and 221-272 to form unstructured loops.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-02T12:48:12.632Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MAASTGYVRLWGAARCWVLRRPMLAAAGGRVPTAAGAWLLRGQRTCDASPPWALWGRGPAIGGQWRGFWEASSRGGGAFSGGEDASEGGAEEGAGGAGGSAGAGEGPVITALTPMTIPDVFPHLPLIAITRNPVFPRFIKIIEVKNKKLVELLRRKVRLAQPYVGVFLKRDDSNESDVVESLDEIYHTGTFAQIHEMQDLGDKLRMIVMGHRRVHISRQLEVEPEEPEAENKHKPRRKSKRGKKEAEDELSARHPAELAMEPTPELPAEVLMVEVENVVHEDFQVTEEVKALTAEIVKTIRDIIALNPLYRESVLQMMQAGQRVVDNPIYLSDMGAALTGAESHELQDVLEETNIPKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLILIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSAYKIVSGEAESVEVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRRPQDKDAKGDKDGSLEVTGQLGEVMKESARIAYTFARAFLMQHAPANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVLPAENKKDFYDLAAFITEGLEVHFVEHYREIFDIAFPDEQAEALAVER","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.16996871741397288,"disorder_content":0.17935349322210636,"disprot_consensus":{"full":[{"start":1,"end":122,"type":"D"},{"start":222,"end":271,"type":"D"}],"Structural state":[{"start":1,"end":122,"type":"D"},{"start":222,"end":271,"type":"D"}]}},{"disprot_id":"DP03862","acc":"P21397","creator":"fkordevani","date":"2022-10-21T09:04:05.800Z","features":{"pfam":[{"id":"PF01593","name":"Flavin containing amine oxidoreductase","start":23,"end":460}],"gene3D":[]},"genes":[{"name":{"value":"MAOA","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6833","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6833"}}]}}],"length":527,"name":"Amine oxidase [flavin-containing] A","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":465,"end":527,"reference_id":"16129825","reference_source":"pmid","reference_html":"Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B. <i> De Colibus L, Li M, Binda C, Lustig A, Edmondson DE, Mattevi A. </i> Proc Natl Acad Sci U S A, 2005","date":"2022-10-21T09:06:25.772Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2BXR"}],"region_id":"DP03862r001","statement":[{"text":" In crystal form X1, the C-terminal residues are disordered after residue 464 (hMAO A contains 527 residues) most likely because of crystal-packing interactions.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-03T13:49:33.461Z"}},{"start":1,"end":11,"reference_id":"16129825","reference_source":"pmid","reference_html":"Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B. <i> De Colibus L, Li M, Binda C, Lustig A, Edmondson DE, Mattevi A. </i> Proc Natl Acad Sci U S A, 2005","date":"2022-11-03T09:38:22.610Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2BXR"},{"db":"PDB","id":"2BXS"}],"region_id":"DP03862r002","statement":[{"text":"Residues 1–12, 111–115, and 507–527 are not visible in the electron density map.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-03T13:49:40.316Z"}},{"start":507,"end":527,"reference_id":"16129825","reference_source":"pmid","reference_html":"Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B. <i> De Colibus L, Li M, Binda C, Lustig A, Edmondson DE, Mattevi A. </i> Proc Natl Acad Sci U S A, 2005","date":"2022-11-03T09:39:51.840Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2BXS"}],"region_id":"DP03862r003","statement":[{"text":"Residues 1–12, 111–115, and 507–527 are not visible in the electron density map.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-03T13:49:40.616Z"}}],"regions_counter":3,"released":"2023_06","sequence":"MENQEKASIAGHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHVDYVDVGGAYVGPTQNRILRLSKELGIETYKVNVSERLVQYVKGKTYPFRGAFPPVWNPIAYLDYNNLWRTIDNMGKEIPTDAPWEAQHADKWDKMTMKELIDKICWTKTARRFAYLFVNINVTSEPHEVSALWFLWYVKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKLNHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPMGAVIKCMMYYKEAFWKKKDYCGCMIIEDEDAPISITLDDTKPDGSLPAIMGFILARKADRLAKLHKEIRKKKICELYAKVLGSQEALHPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYGRVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLGKVTEKDIWVQEPESKDVPAVEITHTFWERNLPSVSGLLKIIGFSTSVTALGFVLYKYKLLPRS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.017077798861480076,"disorder_content":0.14041745730550284,"disprot_consensus":{"full":[{"start":1,"end":11,"type":"D"},{"start":465,"end":527,"type":"D"}],"Structural state":[{"start":1,"end":11,"type":"D"},{"start":465,"end":527,"type":"D"}]}},{"disprot_id":"DP03863","acc":"O43318","creator":"fkordevani","date":"2022-10-21T12:15:17.913Z","features":{"pfam":[{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":36,"end":283},{"id":"PF27575","name":"MAP3K7 C-terminal coiled coil","start":513,"end":604}],"gene3D":[]},"genes":[{"name":{"value":"MAP3K7","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"28397838","url":"http://www.ncbi.nlm.nih.gov/pubmed/28397838","alternativeUrl":"https://europepmc.org/abstract/MED/28397838"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6859","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6859"}}]},"synonyms":[{"value":"TAK1"}]}],"length":606,"name":"Mitogen-activated protein kinase kinase kinase 7","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":66,"end":80,"reference_id":"28011204","reference_source":"pmid","reference_html":"Structure-guided development of covalent TAK1 inhibitors. <i> Tan L, Gurbani D, Weisberg EL, Hunter JC, Li L, Jones DS, Ficarro SB, Mowafy S, Tam CP, Rao S, Du G, Griffin JD, Sorger PK, Marto JA, Westover KD, Gray NS. </i> Bioorg Med Chem, 2017","date":"2022-10-21T12:18:01.442Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5E7R"}],"region_id":"DP03863r001","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-02T15:49:26.791Z"}},{"start":178,"end":190,"reference_id":"28011204","reference_source":"pmid","reference_html":"Structure-guided development of covalent TAK1 inhibitors. <i> Tan L, Gurbani D, Weisberg EL, Hunter JC, Li L, Jones DS, Ficarro SB, Mowafy S, Tam CP, Rao S, Du G, Griffin JD, Sorger PK, Marto JA, Westover KD, Gray NS. </i> Bioorg Med Chem, 2017","date":"2022-11-03T09:44:21.814Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5E7R"},{"db":"PDB","id":"5JH6"},{"db":"PDB","id":"5J8I"},{"db":"PDB","id":"5J7S"},{"db":"PDB","id":"5J9I"},{"db":"PDB","id":"5JK3"}],"region_id":"DP03863r002","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-03T13:51:58.141Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MSTASAASSSSSSSAGEMIEAPSQVLNFEEIDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFPGADEPLQYPCQYSDEGQSNSATSTGSFMDIASTNTSNKSDTNMEQVPATNDTIKRLESKLLKNQAKQQSESGRLSLGASRGSSVESLPPTSEGKRMSADMSEIEARIAATTAYSKPKRGHRKTASFGNILDVPEIVISGNGQPRRRSIQDLTVTGTEPGQVSSRSSSPSVRMITTSGPTSEKPTRSHPWTPDDSTDTNGSDNSIPMAYLTLDHQLQPLAPCPNSKESMAVFEQHCKMAQEYMKVQTEIALLLQRKQELVAELDQDEKDQQNTSRLVQEHKKLLDENKSLSTYYQQCKKQLEVIRSQQQKRQGTS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Stress response proteins"],"alphafold_very_low_content":0.37293729372937295,"disorder_content":0.0462046204620462,"disprot_consensus":{"full":[{"start":66,"end":80,"type":"D"},{"start":178,"end":190,"type":"D"}],"Structural state":[{"start":66,"end":80,"type":"D"},{"start":178,"end":190,"type":"D"}]}},{"disprot_id":"DP03864","acc":"P28482","creator":"fkordevani","date":"2022-10-21T12:22:59.375Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":25,"end":313}],"gene3D":[]},"genes":[{"name":{"value":"MAPK1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:6871","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6871"}}]},"synonyms":[{"value":"ERK2"},{"value":"PRKM1"},{"value":"PRKM2"}]}],"length":360,"name":"Mitogen-activated protein kinase 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":15,"reference_id":"9827991","reference_source":"pmid","reference_html":"A single amino acid substitution makes ERK2 susceptible to pyridinyl imidazole inhibitors of p38 MAP kinase. <i> Fox T, Coll JT, Xie X, Ford PJ, Germann UA, Porter MD, Pazhanisamy S, Fleming MA, Galullo V, Su MS, Wilson KP. </i> Protein Sci, 1998","date":"2022-11-03T09:46:24.579Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1PME"}],"region_id":"DP03864r001","statement":[{"text":"The PDB shows the protein lacks electron density in residues 1-15, indicating this region is disordered.","type":"Curator statement"},{"text":"No electron density was observed for ERK2(5X) amino acids 1-13, 31-33, and 328-335, so these residues were not included in the  model.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-03T13:53:36.290Z"}},{"start":175,"end":189,"reference_id":"26144345","reference_source":"pmid","reference_html":"Ligand efficient tetrahydro-pyrazolopyridines as inhibitors of ERK2 kinase. <i> Bagdanoff JT, Jain R, Han W, Poon D, Lee PS, Bellamacina C, Lindvall M. </i> Bioorg Med Chem Lett, 2015","date":"2022-10-21T12:28:07.691Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5BUE"},{"db":"PDB","id":"5BUJ"}],"region_id":"DP03864r002","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-02T16:59:55.329Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MAAAAAAGAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKISPFEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Autophagy-related proteins","Cancer-related proteins"],"alphafold_very_low_content":0.041666666666666664,"disorder_content":0.08333333333333333,"disprot_consensus":{"full":[{"start":1,"end":15,"type":"D"},{"start":175,"end":189,"type":"D"}],"Structural state":[{"start":1,"end":15,"type":"D"},{"start":175,"end":189,"type":"D"}]}},{"disprot_id":"DP03865","acc":"O95822","creator":"fkordevani","date":"2022-10-21T12:33:15.889Z","features":{"pfam":[{"id":"PF05292","name":"Malonyl-CoA decarboxylase C-terminal domain","start":193,"end":489},{"id":"PF17408","name":"Malonyl-CoA decarboxylase N-terminal domain","start":95,"end":190}],"gene3D":[]},"genes":[{"name":{"value":"MLYCD","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:7150","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:7150"}}]}}],"length":493,"name":"Malonyl-CoA decarboxylase, mitochondrial","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":344,"end":371,"reference_id":"23791943","reference_source":"pmid","reference_html":"Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations. <i> Froese DS, Forouhar F, Tran TH, Vollmar M, Kim YS, Lew S, Neely H, Seetharaman J, Shen Y, Xiao R, Acton TB, Everett JK, Cannone G, Puranik S, Savitsky P, Krojer T, Pilka ES, Kiyani W, Lee WH, Marsden BD, von Delft F, Allerston CK, Spagnolo L, Gileadi O, Montelione GT, Oppermann U, Yue WW, Tong L. </i> Structure, 2013","date":"2022-10-21T12:35:14.631Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2YGW"}],"region_id":"DP03865r001","statement":[{"text":"Residues 60–65, 115 and 116, 276–281, and 344–371, which represent surface-exposed regions in the structure, are disordered and not modeled.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-10-21T16:48:24.155Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MRGFGPGLTARRLLPLRLPPRPPGPRLASGQAAGALERAMDELLRRAVPPTPAYELREKTPAPAEGQCADFVSFYGGLAETAQRAELLGRLARGFGVDHGQVAEQSAGVLHLRQQQREAAVLLQAEDRLRYALVPRYRGLFHHISKLDGGVRFLVQLRADLLEAQALKLVEGPDVREMNGVLKGMLSEWFSSGFLNLERVTWHSPCEVLQKISEAEAVHPVKNWMDMKRRVGPYRRCYFFSHCSTPGEPLVVLHVALTGDISSNIQAIVKEHPPSETEEKNKITAAIFYSISLTQQGLQGVELGTFLIKRVVKELQREFPHLGVFSSLSPIPGFTKWLLGLLNSQTKEHGRNELFTDSECKEISEITGGPINETLKLLLSSSEWVQSEKLVRALQTPLMRLCAWYLYGEKHRGYALNPVANFHLQNGAVLWRINWMADVSLRGITGSCGLMANYRYFLEETGPNSTSYLGSKIIKASEQVLSLVAQFQKNSKL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.06693711967545639,"disorder_content":0.056795131845841784,"disprot_consensus":{"full":[{"start":344,"end":371,"type":"D"}],"Structural state":[{"start":344,"end":371,"type":"D"}]}},{"disprot_id":"DP03866","acc":"Q8IVH4","creator":"fkordevani","date":"2022-10-21T12:37:25.789Z","features":{"pfam":[{"id":"PF03308","name":"Methylmalonyl Co-A mutase-associated GTPase MeaB","start":101,"end":382}],"gene3D":[]},"genes":[{"name":{"value":"MMAA","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:18871","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:18871"}}]}}],"length":418,"name":"Methylmalonic aciduria type A protein, mitochondrial","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":182,"end":197,"reference_id":"20876572","reference_source":"pmid","reference_html":"Structures of the human GTPase MMAA and vitamin B12-dependent methylmalonyl-CoA mutase and insight into their complex formation. <i> Froese DS, Kochan G, Muniz JR, Wu X, Gileadi C, Ugochukwu E, Krysztofinska E, Gravel RA, Oppermann U, Yue WW. </i> J Biol Chem, 2010","date":"2022-11-03T09:50:21.421Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2WWW"}],"region_id":"DP03866r001","statement":[{"text":"Several loops connecting the G-domain β-strands are disordered, suggesting their intrinsic flexibility. These include aa 182–197 (L1, Switch I motif), aa 212–220 (L2), aa 246–248 (L3, part of Switch II motif), and aa 268–279 (L4).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-03T13:54:24.755Z"}},{"start":268,"end":279,"reference_id":"20876572","reference_source":"pmid","reference_html":"Structures of the human GTPase MMAA and vitamin B12-dependent methylmalonyl-CoA mutase and insight into their complex formation. <i> Froese DS, Kochan G, Muniz JR, Wu X, Gileadi C, Ugochukwu E, Krysztofinska E, Gravel RA, Oppermann U, Yue WW. </i> J Biol Chem, 2010","date":"2022-10-21T12:41:21.859Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2WWW"}],"region_id":"DP03866r002","statement":[{"text":"Several loops connecting the G-domain β-strands are disordered, suggesting their intrinsic flexibility. These include aa 182–197 (L1, Switch I motif), aa 212–220 (L2), aa 246–248 (L3, part of Switch II motif), and aa 268–279 (L4).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-02T17:11:31.853Z"}},{"start":182,"end":197,"reference_id":"20876572","reference_source":"pmid","reference_html":"Structures of the human GTPase MMAA and vitamin B12-dependent methylmalonyl-CoA mutase and insight into their complex formation. <i> Froese DS, Kochan G, Muniz JR, Wu X, Gileadi C, Ugochukwu E, Krysztofinska E, Gravel RA, Oppermann U, Yue WW. </i> J Biol Chem, 2010","date":"2022-11-03T09:49:19.112Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2WWW"}],"region_id":"DP03866r003","statement":[{"text":"Several loops connecting the G-domain β-strands are disordered, suggesting their intrinsic flexibility. These include aa 182–197 (L1, Switch I motif), aa 212–220 (L2), aa 246–248 (L3, part of Switch II motif), and aa 268–279 (L4).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-03T13:54:09.680Z"}},{"start":268,"end":279,"reference_id":"20876572","reference_source":"pmid","reference_html":"Structures of the human GTPase MMAA and vitamin B12-dependent methylmalonyl-CoA mutase and insight into their complex formation. <i> Froese DS, Kochan G, Muniz JR, Wu X, Gileadi C, Ugochukwu E, Krysztofinska E, Gravel RA, Oppermann U, Yue WW. </i> J Biol Chem, 2010","date":"2022-11-03T09:49:48.312Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2WWW"}],"region_id":"DP03866r004","statement":[{"text":"Several loops connecting the G-domain β-strands are disordered, suggesting their intrinsic flexibility. These include aa 182–197 (L1, Switch I motif), aa 212–220 (L2), aa 246–248 (L3, part of Switch II motif), and aa 268–279 (L4).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-03T13:54:09.982Z"}}],"regions_counter":4,"released":"2023_06","sequence":"MPMLLPHPHQHFLKGLLRAPFRCYHFIFHSSTHLGSGIPCAQPFNSLGLHCTKWMLLSDGLKRKLCVQTTLKDHTEGLSDKEQRFVDKLYTGLIQGQRACLAEAITLVESTHSRKKELAQVLLQKVLLYHREQEQSNKGKPLAFRVGLSGPPGAGKSTFIEYFGKMLTERGHKLSVLAVDPSSCTSGGSLLGDKTRMTELSRDMNAYIRPSPTRGTLGGVTRTTNEAILLCEGAGYDIILIETVGVGQSEFAVADMVDMFVLLLPPAGGDELQGIKRGIIEMADLVAVTKSDGDLIVPARRIQAEYVSALKLLRKRSQVWKPKVIRISARSGEGISEMWDKMKDFQDLMLASGELTAKRRKQQKVWMWNLIQESVLEHFRTHPTVREQIPLLEQKVLIGALSPGLAADFLLKAFKSRD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.18899521531100477,"disorder_content":0.06698564593301436,"disprot_consensus":{"full":[{"start":182,"end":197,"type":"D"},{"start":268,"end":279,"type":"D"}],"Structural state":[{"start":182,"end":197,"type":"D"},{"start":268,"end":279,"type":"D"}],"Disorder function":[{"start":182,"end":197,"type":"F"},{"start":268,"end":279,"type":"F"}]}},{"disprot_id":"DP03867","acc":"Q9Y4U1","creator":"fkordevani","date":"2022-10-21T12:44:00.859Z","features":{"pfam":[{"id":"PF16690","name":"Methylmalonic aciduria and homocystinuria type C family","start":20,"end":234}],"gene3D":[]},"genes":[{"name":{"value":"MMACHC","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:24525","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:24525"}}]}}],"length":282,"name":"Cyanocobalamin reductase / alkylcobalamin dealkylase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":231,"end":282,"reference_id":"22642810","reference_source":"pmid","reference_html":"Structure of MMACHC reveals an arginine-rich pocket and a domain-swapped dimer for its B12 processing function. <i> Froese DS, Krojer T, Wu X, Shrestha R, Kiyani W, von Delft F, Gravel RA, Oppermann U, Yue WW. </i> Biochemistry, 2012","date":"2022-10-21T12:45:44.359Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3SOM"}],"region_id":"DP03867r001","statement":[{"text":"The refined monomeric model comprises aa 5–230 (Figure 1a), while the C-terminal 52 residues (aa 231–282), encompassing a Pro-rich region absent in many MMACHC orthologues (Figure S1 of the Supporting Information), are disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-02T17:19:41.853Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MEPKVAELKQKIEDTLCPFGFEVYPFQVAWYNELLPPAFHLPLPGPTLAFLVLSTPAMFDRALKPFLQSCHLRMLTDPVDQCVAYHLGRVRESLPELQIEIIADYEVHPNRRPKILAQTAAHVAGAAYYYQRQDVEADPWGNQRISGVCIHPRFGGWFAIRGVVLLPGIEVPDLPPRKPHDCVPTRADRIALLEGFNFHWRDWTYRDAVTPQERYSEEQKAYFSTPPAQRLALLGLAQPSEKPSSPSPDLPFTTPAPKKPGNPSRARSWLSPRVSPPASPGP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.15602836879432624,"disorder_content":0.18439716312056736,"disprot_consensus":{"full":[{"start":231,"end":282,"type":"D"}],"Structural state":[{"start":231,"end":282,"type":"D"}]}},{"disprot_id":"DP03868","acc":"Q9H3L0","creator":"fkordevani","date":"2022-10-21T12:48:41.284Z","features":{"pfam":[{"id":"PF10229","name":"Methylmalonic aciduria and homocystinuria type D protein","start":24,"end":293}],"gene3D":[]},"genes":[{"name":{"value":"MMADHC","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:25221","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:25221"}}]},"synonyms":[{"value":"C2orf25"},{"value":"CL25022"}],"orfNames":[{"value":"HSPC161"},{"value":"My011"}]}],"length":296,"name":"Cobalamin trafficking protein CblD","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":108,"end":133,"reference_id":"26364851","reference_source":"pmid","reference_html":"Structure of Human B12 Trafficking Protein CblD Reveals Molecular Mimicry and Identifies a New Subfamily of Nitro-FMN Reductases. <i> Yamada K, Gherasim C, Banerjee R, Koutmos M. </i> J Biol Chem, 2015","date":"2022-11-03T09:55:56.409Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5CUZ"},{"db":"PDB","id":"5CV0"}],"region_id":"DP03868r001","statement":[{"text":"The N-terminal region (residues 108–131), with the exception of a very short polypeptide (118–122) in one of the molecules in the asymmetric unit, was not modeled because no visible electron density corresponding to this region could be discerned. Therefore, the N-terminal region even in the truncated CblDΔN108 variant is unstructured and disordered.\n","type":"Results"},{"text":"Even though the authors made an exception for 188-122 region, it is still disordered in the PDB structure and the 118-122 region is too short to be ordered so the IDR is considered to be 108-133.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-03T14:11:38.426Z"}},{"start":108,"end":132,"reference_id":"32871076","reference_source":"pmid","reference_html":"An Interprotein Co-S Coordination Complex in the B<sub>12</sub>-Trafficking Pathway. <i> Li Z, Mascarenhas R, Twahir UT, Kallon A, Deb A, Yaw M, Penner-Hahn J, Koutmos M, Warncke K, Banerjee R. </i> J Am Chem Soc, 2020","date":"2022-11-03T09:51:59.382Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6X8Z"}],"region_id":"DP03868r002","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-03T14:10:51.969Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MANVLCNRARLVSYLPGFCSLVKRVVNPKAFSTAGSSGSDESHVAAAPPDICSRTVWPDETMGPFGPQDQRFQLPGNIGFDCHLNGTASQKKSLVHKTLPDVLAEPLSSERHEFVMAQYVNEFQGNDAPVEQEINSAETYFESARVECAIQTCPELLRKDFESLFPEVANGKLMILTVTQKTKNDMTVWSEEVEIEREVLLEKFINGAKEICYALRAEGYWADFIDPSSGLAFFGPYTNNTLFETDERYRHLGFSVDDLGCCKVIRHSLWGTHVVVGSIFTNATPDSHIMKKLSGN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.17229729729729729,"disorder_content":0.08783783783783784,"disprot_consensus":{"full":[{"start":108,"end":133,"type":"D"}],"Structural state":[{"start":108,"end":133,"type":"D"}]}},{"disprot_id":"DP03869","acc":"P22033","creator":"fkordevani","date":"2022-10-21T13:06:35.467Z","features":{"pfam":[{"id":"PF01642","name":"Methylmalonyl-CoA mutase","start":63,"end":575},{"id":"PF02310","name":"B12 binding domain","start":616,"end":728}],"gene3D":[]},"genes":[{"name":{"value":"MMUT","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:7526","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:7526"}}]},"synonyms":[{"value":"MUT","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:7526","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:7526"}}]}]}],"length":750,"name":"Methylmalonyl-CoA mutase, mitochondrial","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":12,"end":35,"reference_id":"20876572","reference_source":"pmid","reference_html":"Structures of the human GTPase MMAA and vitamin B12-dependent methylmalonyl-CoA mutase and insight into their complex formation. <i> Froese DS, Kochan G, Muniz JR, Wu X, Gileadi C, Ugochukwu E, Krysztofinska E, Gravel RA, Oppermann U, Yue WW. </i> J Biol Chem, 2010","date":"2022-11-03T09:57:58.831Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2XIJ"},{"db":"PDB","id":"2XIQ"}],"region_id":"DP03869r001","statement":[{"text":"The PDB shows that when bounded to adenosylcobalamin the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-07T14:24:09.532Z"}},{"start":12,"end":26,"reference_id":"20876572","reference_source":"pmid","reference_html":"Structures of the human GTPase MMAA and vitamin B12-dependent methylmalonyl-CoA mutase and insight into their complex formation. <i> Froese DS, Kochan G, Muniz JR, Wu X, Gileadi C, Ugochukwu E, Krysztofinska E, Gravel RA, Oppermann U, Yue WW. </i> J Biol Chem, 2010","date":"2022-11-03T10:01:16.240Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3BIC"}],"region_id":"DP03869r002","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-07T14:24:09.995Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MLRAKNQLFLLSPHYLRQVKESSGSRLIQQRLLHQQQPLHPEWAALAKKQLKGKNPEDLIWHTPEGISIKPLYSKRDTMDLPEELPGVKPFTRGPYPTMYTFRPWTIRQYAGFSTVEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPVLANFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFEYTAKHMPKFNSISISGYHMQEAGADAILELAYTLADGLEYSRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKMRAGRRLWAHLIEKMFQPKNSKSLLLRAHCQTSGWSLTEQDPYNNIVRTAIEAMAAVFGGTQSLHTNSFDEALGLPTVKSARIARNTQIIIQEESGIPKVADPWGGSYMMECLTNDVYDAALKLINEIEEMGGMAKAVAEGIPKLRIEECAARRQARIDSGSEVIVGVNKYQLEKEDAVEVLAIDNTSVRNRQIEKLKKIKSSRDQALAERCLAALTECAASGDGNILALAVDASRARCTVGEITDALKKVFGEHKANDRMVSGAYRQEFGESKEITSAIKRVHKFMEREGRRPRLLVAKMGQDGHDRGAKVIATGFADLGFDVDIGPLFQTPREVAQQAVDADVHAVGISTLAAGHKTLVPELIKELNSLGRPDILVMCGGVIPPQDYEFLFEVGVSNVFGPGTRIPKAAVQVLDDIEKCLEKKQQSV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.042666666666666665,"disorder_content":0.032,"disprot_consensus":{"full":[{"start":12,"end":35,"type":"D"}],"Structural state":[{"start":12,"end":35,"type":"D"}]}},{"disprot_id":"DP03870","acc":"A0A6L0XH39","creator":"jssuarez","date":"2022-10-24T10:13:18.962Z","features":{"pfam":[{"id":"PF02146","name":"Sir2 family","start":39,"end":223}],"gene3D":[]},"genes":[{"name":{"value":"SIR2RP1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAM68740.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAM68740.1"}}]},"synonyms":[{"value":"SIR2","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAM68740.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAM68740.1"}}]},{"value":"TbSIR2","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAM68740.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAM68740.1"}}]},{"value":"TbSIR2RP1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAM68740.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAM68740.1"}}]}],"orfNames":[{"value":"LINJ_26_0200","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAM68740.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAM68740.1"}}]}]}],"length":373,"name":"NAD-dependent protein deacetylase","ncbi_taxon_id":5671,"organism":"Leishmania infantum","regions":[{"start":304,"end":323,"reference_id":"29543820","reference_source":"pmid","reference_html":"The crystal structure of the Leishmania infantum Silent Information Regulator 2 related protein 1: Implications to protein function and drug design. <i> Ronin C, Costa DM, Tavares J, Faria J, Ciesielski F, Ciapetti P, Smith TK, MacDougall J, Cordeiro-da-Silva A, Pemberton IK. </i> PLoS One, 2018","date":"2022-10-24T10:21:50.709Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP03870r001","statement":[{"text":"Moreover, additionally to region P253-E303 removed from the recombinant protein, electron density was missing for residues A304 to P323 in both monomers, suggesting potential flexibility of this region.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"5OL0"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T19:08:55.539Z"}},{"start":268,"end":284,"reference_id":"29543820","reference_source":"pmid","reference_html":"The crystal structure of the Leishmania infantum Silent Information Regulator 2 related protein 1: Implications to protein function and drug design. <i> Ronin C, Costa DM, Tavares J, Faria J, Ciesielski F, Ciapetti P, Smith TK, MacDougall J, Cordeiro-da-Silva A, Pemberton IK. </i> PLoS One, 2018","date":"2022-11-02T09:11:55.048Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP03870r002","statement":[{"text":"These results suggest LiSir2rp1 is composed of two tightly associated proteolytically stable polypeptides (nominally 29 kDa N-terminal and 9 kDa C-terminal) linked minimally by a 17 residue surface-exposed, serine-rich peptide region 268–284, EGRSSSSQSRSPSASPR.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-05T15:33:36.084Z"}},{"start":268,"end":284,"reference_id":"29543820","reference_source":"pmid","reference_html":"The crystal structure of the Leishmania infantum Silent Information Regulator 2 related protein 1: Implications to protein function and drug design. <i> Ronin C, Costa DM, Tavares J, Faria J, Ciesielski F, Ciapetti P, Smith TK, MacDougall J, Cordeiro-da-Silva A, Pemberton IK. </i> PLoS One, 2018","date":"2022-11-02T09:12:06.797Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP03870r003","statement":[{"text":"These results suggest LiSir2rp1 is composed of two tightly associated proteolytically stable polypeptides (nominally 29 kDa N-terminal and 9 kDa C-terminal) linked minimally by a 17 residue surface-exposed, serine-rich peptide region 268–284, EGRSSSSQSRSPSASPR.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-05T15:33:34.712Z"}},{"start":361,"end":373,"reference_id":"29543820","reference_source":"pmid","reference_html":"The crystal structure of the Leishmania infantum Silent Information Regulator 2 related protein 1: Implications to protein function and drug design. <i> Ronin C, Costa DM, Tavares J, Faria J, Ciesielski F, Ciapetti P, Smith TK, MacDougall J, Cordeiro-da-Silva A, Pemberton IK. </i> PLoS One, 2018","date":"2022-11-02T09:30:08.285Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"5OL0"}],"region_id":"DP03870r004","statement":[{"text":"In addition to a small number of residues missing at both N- and C- terminal ends of the protein (N-ter M1-R6 and C-ter A371-T373 are missing in both monomers), region R52-P70 could not be modeled in monomer B.","type":"Results"},{"text":"Authors are referring to the 361-373 region, that lacks electron density in the PDB: 5OL0.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-05T15:34:23.584Z"}}],"regions_counter":4,"released":"2022_12","sequence":"MTASPRAPHQEHVLGEPTLEGLAHYIREKNVRRILVLVGAGASVAAGIPDFRSPDTGIYANLGKYNLEDPTDAFSLTLLREKPEIFYSIARELNLWPGHFQPTAVHHFIRLLQDEGRLLRCCTQNIDGLEKAAGVSPELLVEAHGSFAAAACIECHTPFSIEQNYLEAMSGTVSRCSTCGGIVKPNVVFFGENLPDAFFDALHHDAPIAELVIIIGTSMQVHPFALLPCVVPKSVPRVVMNRERVGGLLFRFPDDPLNTVHEDAVAKEGRSSSSQSRSPSASPRREEGGTEDSPSSPNEEVEEASTSSSSDGYGQYGDYHAHPDVCRDVLFRGDCQENVVTLAEYLGLSEALAKRMRLSDAAPATAQRAPNET","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"disorder_content":0.13404825737265416,"disprot_consensus":{"full":[{"start":268,"end":284,"type":"D"},{"start":304,"end":323,"type":"D"},{"start":361,"end":373,"type":"D"}],"Structural state":[{"start":268,"end":284,"type":"D"},{"start":304,"end":323,"type":"D"},{"start":361,"end":373,"type":"D"}],"Disorder function":[{"start":268,"end":284,"type":"F"}]}},{"disprot_id":"DP03871","acc":"O77299","creator":"jssuarez","date":"2022-10-24T10:39:15.744Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"HASPA","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAA09787.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA09787.1"}}]}}],"length":80,"name":"HASPA protein","ncbi_taxon_id":5661,"organism":"Leishmania donovani","regions":[{"start":1,"end":80,"reference_id":"28634775","reference_source":"pmid","reference_html":"Hydrophilic Acylated Surface Protein A (HASPA) of Leishmania donovani: Expression, Purification and Biophysico-Chemical Characterization. <i> Kumar M, Ranjan K, Singh V, Pathak C, Pappachan A, Singh DD. </i> Protein J, 2017","date":"2022-10-24T10:42:24.934Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP03871r001","statement":[{"text":"The average CD spectrum obtained for r-LdHASPA showed a major negative band with maximum dip at around 200 nm, which indicated that secondary structure of r-LdHASPA consists of random coils or unstructured regions.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T19:09:51.606Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MGSSCTKDSAKESQKRADNIDTTTRSDEKDGIHVQESAGPVQENFGDAQEKNEDGHNVGDGANGNEDGNDNQPKEHAAGN","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"alphafold_very_low_content":0.2125,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":80,"type":"D"}],"Structural state":[{"start":1,"end":80,"type":"D"}]}},{"disprot_id":"DP03872","acc":"O75970","creator":"fkordevani","date":"2022-10-24T14:10:09.641Z","features":{"pfam":[{"id":"PF00595","name":"PDZ domain","start":142,"end":220},{"id":"PF00595","name":"PDZ domain","start":263,"end":333},{"id":"PF00595","name":"PDZ domain","start":379,"end":459},{"id":"PF00595","name":"PDZ domain","start":560,"end":629},{"id":"PF00595","name":"PDZ domain","start":701,"end":783},{"id":"PF00595","name":"PDZ domain","start":1009,"end":1076},{"id":"PF00595","name":"PDZ domain","start":1156,"end":1235},{"id":"PF00595","name":"PDZ domain","start":1351,"end":1427},{"id":"PF00595","name":"PDZ domain","start":1486,"end":1560},{"id":"PF00595","name":"PDZ domain","start":1630,"end":1708},{"id":"PF00595","name":"PDZ domain","start":1726,"end":1803},{"id":"PF00595","name":"PDZ domain","start":1863,"end":1944},{"id":"PF00595","name":"PDZ domain","start":1988,"end":2068},{"id":"PF09045","name":"L27_2","start":6,"end":63},{"id":"PF16667","name":"Unstructured region 10 on multiple PDZ protein","start":1562,"end":1626}],"gene3D":[]},"genes":[{"name":{"value":"MPDZ"},"synonyms":[{"value":"MUPP1"}]}],"length":2070,"name":"Multiple PDZ domain protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1171,"end":1183,"reference_id":"17384233","reference_source":"pmid","reference_html":"Structure of PICK1 and other PDZ domains obtained with the help of self-binding C-terminal extensions. <i> Elkins JM, Papagrigoriou E, Berridge G, Yang X, Phillips C, Gileadi C, Savitsky P, Doyle DA. </i> Protein Sci, 2007","date":"2022-10-24T14:14:16.534Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2FCF"}],"region_id":"DP03872r001","statement":[{"text":"In each of the four protein chains the position 0 residue is slightly disordered, in particular with significantly weaker electron density around the C-terminal carboxylate (Fig. 5A).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-02T18:12:33.613Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MLEAIDKNRALHAAERLQTKLRERGDVANEDKLSLLKSVLQSPLFSQILSLQTSVQQLKDQVNIATSATSNIEYAHVPHLSPAVIPTLQNESFLLSPNNGNLEALTGPGIPHINGKPACDEFDQLIKNMAQGRHVEVFELLKPPSGGLGFSVVGLRSENRGELGIFVQEIQEGSVAHRDGRLKETDQILAINGQALDQTITHQQAISILQKAKDTVQLVIARGSLPQLVSPIVSRSPSAASTISAHSNPVHWQHMETIELVNDGSGLGFGIIGGKATGVIVKTILPGGVADQHGRLCSGDHILKIGDTDLAGMSSEQVAQVLRQCGNRVKLMIARGAIEERTAPTALGITLSSSPTSTPELRVDASTQKGEESETFDVELTKNVQGLGITIAGYIGDKKLEPSGIFVKSITKSSAVEHDGRIQIGDQIIAVDGTNLQGFTNQQAVEVLRHTGQTVLLTLMRRGMKQEAELMSREDVTKDADLSPVNASIIKENYEKDEDFLSSTRNTNILPTEEEGYPLLSAEIEEIEDAQKQEAALLTKWQRIMGINYEIVVAHVSKFSENSGLGISLEATVGHHFIRSVLPEGPVGHSGKLFSGDELLEVNGITLLGENHQDVVNILKELPIEVTMVCCRRTVPPTTQSELDSLDLCDIELTEKPHVDLGEFIGSSETEDPVLAMTDAGQSTEEVQAPLAMWEAGIQHIELEKGSKGLGFSILDYQDPIDPASTVIIIRSLVPGGIAEKDGRLLPGDRLMFVNDVNLENSSLEEAVEALKGAPSGTVRIGVAKPLPLSPEEGYVSAKEDSFLYPPHSCEEAGLADKPLFRADLALVGTNDADLVDESTFESPYSPENDSIYSTQASILSLHGSSCGDGLNYGSSLPSSPPKDVIENSCDPVLDLHMSLEELYTQNLLQRQDENTPSVDISMGPASGFTINDYTPANAIEQQYECENTIVWTESHLPSEVISSAELPSVLPDSAGKGSEYLLEQSSLACNAECVMLQNVSKESFERTINIAKGNSSLGMTVSANKDGLGMIVRSIIHGGAISRDGRIAIGDCILSINEESTISVTNAQARAMLRRHSLIGPDIKITYVPAEHLEEFKISLGQQSGRVMALDIFSSYTGRDIPELPEREEGEGEESELQNTAYSNWNQPRRVELWREPSKSLGISIVGGRGMGSRLSNGEVMRGIFIKHVLEDSPAGKNGTLKPGDRIVEVDGMDLRDASHEQAVEAIRKAGNPVVFMVQSIINRPRKSPLPSLLHNLYPKYNFSSTNPFADSLQINADKAPSQSESEPEKAPLCSVPPPPPSAFAEMGSDHTQSSASKISQDVDKEDEFGYSWKNIRERYGTLTGELHMIELEKGHSGLGLSLAGNKDRSRMSVFIVGIDPNGAAGKDGRLQIADELLEINGQILYGRSHQNASSIIKCAPSKVKIIFIRNKDAVNQMAVCPGNAVEPLPSNSENLQNKETEPTVTTSDAAVDLSSFKNVQHLELPKDQGGLGIAISEEDTLSGVIIKSLTEHGVAATDGRLKVGDQILAVDDEIVVGYPIEKFISLLKTAKMTVKLTIHAENPDSQAVPSAAGAASGEKKNSSQSLMVPQSGSPEPESIRNTSRSSTPAIFASDPATCPIIPGCETTIEISKGRTGLGLSIVGGSDTLLGAIIIHEVYEEGAACKDGRLWAGDQILEVNGIDLRKATHDEAINVLRQTPQRVRLTLYRDEAPYKEEEVCDTLTIELQKKPGKGLGLSIVGKRNDTGVFVSDIVKGGIADADGRLMQGDQILMVNGEDVRNATQEAVAALLKCSLGTVTLEVGRIKAGPFHSERRPSQSSQVSEGSLSSFTFPLSGSSTSESLESSSKKNALASEIQGLRTVEMKKGPTDSLGISIAGGVGSPLGDVPIFIAMMHPTGVAAQTQKLRVGDRIVTICGTSTEGMTHTQAVNLLKNASGSIEMQVVAGGDVSVVTGHQQEPASSSLSFTGLTSSSIFQDDLGPPQCKSITLERGPDGLGFSIVGGYGSPHGDLPIYVKTVFAKGAASEDGRLKRGDQIIAVNGQSLEGVTHEEAVAILKRTKGTVTLMVLS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.37777777777777777,"disorder_content":0.006280193236714976,"disprot_consensus":{"full":[{"start":1171,"end":1183,"type":"D"}],"Structural state":[{"start":1171,"end":1183,"type":"D"}]}},{"disprot_id":"DP03873","acc":"P42898","creator":"fkordevani","date":"2022-10-24T14:16:09.376Z","features":{"pfam":[{"id":"PF02219","name":"Methylenetetrahydrofolate reductase","start":48,"end":337},{"id":"PF21895","name":"MTHFR, SAM-binding regulatory domain","start":344,"end":644}],"gene3D":[]},"genes":[{"name":{"value":"MTHFR","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:7436","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:7436"}}]}}],"length":656,"name":"Methylenetetrahydrofolate reductase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":161,"end":171,"reference_id":"29891918","reference_source":"pmid","reference_html":"Structural basis for the regulation of human 5,10-methylenetetrahydrofolate reductase by phosphorylation and S-adenosylmethionine inhibition. <i> Froese DS, Kopec J, Rembeza E, Bezerra GA, Oberholzer AE, Suormala T, Lutz S, Chalk R, Borkowska O, Baumgartner MR, Yue WW. </i> Nat Commun, 2018","date":"2022-11-03T10:03:48.883Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6FCX"}],"region_id":"DP03873r001","statement":[{"text":" In fact, this is reflected in our structure whereby the catalytic domain of one dimer subunit (chain A) is ordered, while that of the other dimer subunit (chain B) is highly disordered, to the extent that only main chain atoms of the amino acid 40–58, 129–134 and 155–342 in chain B could be modelled.","type":"Results"},{"text":"The 129-134 region the authors mention corresponds to the residues 161-171 of the Uniprot sequence that lacks electron density in the PDB.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-03T14:12:08.911Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MVNEARGNSSLNPCLEGSASSGSESSKDSSRCSTPGLDPERHERLREKMRRRLESGDKWFSLEFFPPRTAEGAVNLISRFDRMAAGGPLYIDVTWHPAGDPGSDKETSSMMIASTAVNYCGLETILHMTCCRQRLEEITGHLHKAKQLGLKNIMALRGDPIGDQWEEEEGGFNYAVDLVKHIRSEFGDYFDICVAGYPKGHPEAGSFEADLKHLKEKVSAGADFIITQLFFEADTFFRFVKACTDMGITCPIVPGIFPIQGYHSLRQLVKLSKLEVPQEIKDVIEPIKDNDAAIRNYGIELAVSLCQELLASGLVPGLHFYTLNREMATTEVLKRLGMWTEDPRRPLPWALSAHPKRREEDVRPIFWASRPKSYIYRTQEWDEFPNGRWGNSSSPAFGELKDYYLFYLKSKSPKEELLKMWGEELTSEESVFEVFVLYLSGEPNRNGHKVTCLPWNDEPLAAETSLLKEELLRVNRQGILTINSQPNINGKPSSDPIVGWGPSGGYVFQKAYLEFFTSRETAEALLQVLKKYELRVNYHLVNVKGENITNAPELQPNAVTWGIFPGREIIQPTVVDPVSFMFWKDEAFALWIERWGKLYEEESPSRTIIQYIHDNYFLVNLVDNDFPLDNCLWQVVEDTLELLNRPTQNARETEAP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.06859756097560976,"disorder_content":0.01676829268292683,"disprot_consensus":{"full":[{"start":161,"end":171,"type":"D"}],"Structural state":[{"start":161,"end":171,"type":"D"}]}},{"disprot_id":"DP03874","acc":"P42345","creator":"fkordevani","date":"2022-10-24T14:22:51.454Z","features":{"pfam":[{"id":"PF00454","name":"Phosphatidylinositol 3- and 4-kinase","start":2182,"end":2430},{"id":"PF02259","name":"FAT domain","start":1513,"end":1908},{"id":"PF02260","name":"FATC domain","start":2519,"end":2549},{"id":"PF08771","name":"FKBP12-rapamycin binding domain","start":2015,"end":2113},{"id":"PF11865","name":"Serine/threonine-protein kinase mTOR domain","start":854,"end":1024},{"id":"PF23593","name":"Serine/threonine-protein kinase ATR-like, HEAT repeats","start":1919,"end":2010}],"gene3D":[]},"genes":[{"name":{"value":"MTOR","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:3942","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:3942"}}]},"synonyms":[{"value":"FRAP"},{"value":"FRAP1"},{"value":"FRAP2"},{"value":"RAFT1"},{"value":"RAPT1"}]}],"length":2549,"name":"Serine/threonine-protein kinase mTOR","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":290,"end":355,"reference_id":"33158864","reference_source":"pmid","reference_html":"The 3.2-Å resolution structure of human mTORC2.  <i> Scaiola A, Mangia F, Imseng S, Boehringer D, Berneiser K, Shimobayashi M, Stuttfeld E, Hall MN, Ban N, Maier T. </i> Sci Adv, 2020","date":"2022-11-03T10:07:03.392Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6ZWM"}],"region_id":"DP03874r001","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-03T14:13:03.110Z"}},{"start":904,"end":926,"reference_id":"33158864","reference_source":"pmid","reference_html":"The 3.2-Å resolution structure of human mTORC2.  <i> Scaiola A, Mangia F, Imseng S, Boehringer D, Berneiser K, Shimobayashi M, Stuttfeld E, Hall MN, Ban N, Maier T. </i> Sci Adv, 2020","date":"2022-10-24T14:43:58.443Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6ZWO"},{"db":"PDB","id":"6ZWM"}],"region_id":"DP03874r002","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-02T18:37:07.221Z"}},{"start":1239,"end":1262,"reference_id":"33158864","reference_source":"pmid","reference_html":"The 3.2-Å resolution structure of human mTORC2.  <i> Scaiola A, Mangia F, Imseng S, Boehringer D, Berneiser K, Shimobayashi M, Stuttfeld E, Hall MN, Ban N, Maier T. </i> Sci Adv, 2020","date":"2022-10-24T14:44:25.435Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6ZWO"},{"db":"PDB","id":"6ZWM"}],"region_id":"DP03874r003","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-02T18:37:32.885Z"}},{"start":1811,"end":1872,"reference_id":"33158864","reference_source":"pmid","reference_html":"The 3.2-Å resolution structure of human mTORC2.  <i> Scaiola A, Mangia F, Imseng S, Boehringer D, Berneiser K, Shimobayashi M, Stuttfeld E, Hall MN, Ban N, Maier T. </i> Sci Adv, 2020","date":"2022-10-24T14:44:45.165Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6ZWO"},{"db":"PDB","id":"6ZWM"}],"region_id":"DP03874r004","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-02T18:37:48.104Z"}},{"start":2434,"end":2491,"reference_id":"33158864","reference_source":"pmid","reference_html":"The 3.2-Å resolution structure of human mTORC2.  <i> Scaiola A, Mangia F, Imseng S, Boehringer D, Berneiser K, Shimobayashi M, Stuttfeld E, Hall MN, Ban N, Maier T. </i> Sci Adv, 2020","date":"2022-10-24T14:45:02.174Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6ZWO"},{"db":"PDB","id":"6ZWM"}],"region_id":"DP03874r005","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-02T18:38:36.584Z"}}],"regions_counter":5,"released":"2023_06","sequence":"MLGTGPAAATTAATTSSNVSVLQQFASGLKSRNEETRAKAAKELQHYVTMELREMSQEESTRFYDQLNHHIFELVSSSDANERKGGILAIASLIGVEGGNATRIGRFANYLRNLLPSNDPVVMEMASKAIGRLAMAGDTFTAEYVEFEVKRALEWLGADRNEGRRHAAVLVLRELAISVPTFFFQQVQPFFDNIFVAVWDPKQAIREGAVAALRACLILTTQREPKEMQKPQWYRHTFEEAEKGFDETLAKEKGMNRDDRIHGALLILNELVRISSMEGERLREEMEEITQQQLVHDKYCKDLMGFGTKPRHITPFTSFQAVQPQQSNALVGLLGYSSHQGLMGFGTSPSPAKSTLVESRCCRDLMEEKFDQVCQWVLKCRNSKNSLIQMTILNLLPRLAAFRPSAFTDTQYLQDTMNHVLSCVKKEKERTAAFQALGLLSVAVRSEFKVYLPRVLDIIRAALPPKDFAHKRQKAMQVDATVFTCISMLARAMGPGIQQDIKELLEPMLAVGLSPALTAVLYDLSRQIPQLKKDIQDGLLKMLSLVLMHKPLRHPGMPKGLAHQLASPGLTTLPEASDVGSITLALRTLGSFEFEGHSLTQFVRHCADHFLNSEHKEIRMEAARTCSRLLTPSIHLISGHAHVVSQTAVQVVADVLSKLLVVGITDPDPDIRYCVLASLDERFDAHLAQAENLQALFVALNDQVFEIRELAICTVGRLSSMNPAFVMPFLRKMLIQILTELEHSGIGRIKEQSARMLGHLVSNAPRLIRPYMEPILKALILKLKDPDPDPNPGVINNVLATIGELAQVSGLEMRKWVDELFIIIMDMLQDSSLLAKRQVALWTLGQLVASTGYVVEPYRKYPTLLEVLLNFLKTEQNQGTRREAIRVLGLLGALDPYKHKVNIGMIDQSRDASAVSLSESKSSQDSSDYSTSEMLVNMGNLPLDEFYPAVSMVALMRIFRDQSLSHHHTMVVQAITFIFKSLGLKCVQFLPQVMPTFLNVIRVCDGAIREFLFQQLGMLVSFVKSHIRPYMDEIVTLMREFWVMNTSIQSTIILLIEQIVVALGGEFKLYLPQLIPHMLRVFMHDNSPGRIVSIKLLAAIQLFGANLDDYLHLLLPPIVKLFDAPEAPLPSRKAALETVDRLTESLDFTDYASRIIHPIVRTLDQSPELRSTAMDTLSSLVFQLGKKYQIFIPMVNKVLVRHRINHQRYDVLICRIVKGYTLADEEEDPLIYQHRMLRSGQGDALASGPVETGPMKKLHVSTINLQKAWGAARRVSKDDWLEWLRRLSLELLKDSSSPSLRSCWALAQAYNPMARDLFNAAFVSCWSELNEDQQDELIRSIELALTSQDIAEVTQTLLNLAEFMEHSDKGPLPLRDDNGIVLLGERAAKCRAYAKALHYKELEFQKGPTPAILESLISINNKLQQPEAAAGVLEYAMKHFGELEIQATWYEKLHEWEDALVAYDKKMDTNKDDPELMLGRMRCLEALGEWGQLHQQCCEKWTLVNDETQAKMARMAAAAAWGLGQWDSMEEYTCMIPRDTHDGAFYRAVLALHQDLFSLAQQCIDKARDLLDAELTAMAGESYSRAYGAMVSCHMLSELEEVIQYKLVPERREIIRQIWWERLQGCQRIVEDWQKILMVRSLVVSPHEDMRTWLKYASLCGKSGRLALAHKTLVLLLGVDPSRQLDHPLPTVHPQVTYAYMKNMWKSARKIDAFQHMQHFVQTMQQQAQHAIATEDQQHKQELHKLMARCFLKLGEWQLNLQGINESTIPKVLQYYSAATEHDRSWYKAWHAWAVMNFEAVLHYKHQNQARDEKKKLRHASGANITNATTAATTAATATTTASTEGSNSESEAESTENSPTPSPLQKKVTEDLSKTLLMYTVPAVQGFFRSISLSRGNNLQDTLRVLTLWFDYGHWPDVNEALVEGVKAIQIDTWLQVIPQLIARIDTPRPLVGRLIHQLLTDIGRYHPQALIYPLTVASKSTTTARHNAANKILKNMCEHSNTLVQQAMMVSEELIRVAILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRISKQLPQLTSLELQYVSPKLLMCRDLELAVPGTYDPNQPIIRIQSIAPSLQVITSKQRPRKLTLMGSNGHEFVFLLKGHEDLRQDERVMQLFGLVNTLLANDPTSLRKNLSIQRYAVIPLSTNSGLIGWVPHCDTLHALIRDYREKKKILLNIEHRIMLRMAPDYDHLTLMQKVEVFEHAVNNTAGDDLAKLLWLKSPSSEVWFDRRTNYTRSLAVMSMVGYILGLGDRHPSNLMLDRLSGKILHIDFGDCFEVAMTREKFPEKIPFRLTRMLTNAMEVTGLDGNYRITCHTVMEVLREHKDSVMAVLEAFVYDPLLNWRLMDTNTKGNKRSRTRTDSYSAGQSVEILDGVELGEPAHKKTGTTVPESIHSFIGDGLVKPEALNKKAIQIINRVRDKLTGRDFSHDDTLDVPTQVELLIKQATSHENLCQCYIGWCPFW","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Autophagy-related proteins","Cancer-related proteins"],"alphafold_very_low_content":0.10435464888191448,"disorder_content":0.09140839544919577,"disprot_consensus":{"full":[{"start":290,"end":355,"type":"D"},{"start":904,"end":926,"type":"D"},{"start":1239,"end":1262,"type":"D"},{"start":1811,"end":1872,"type":"D"},{"start":2434,"end":2491,"type":"D"}],"Structural state":[{"start":290,"end":355,"type":"D"},{"start":904,"end":926,"type":"D"},{"start":1239,"end":1262,"type":"D"},{"start":1811,"end":1872,"type":"D"},{"start":2434,"end":2491,"type":"D"}]}},{"disprot_id":"DP03875","acc":"Q92913-2","creator":"maspromonte","date":"2022-10-24T15:28:07.303Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"FGF13","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:3670","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:3670"}}]},"synonyms":[{"value":"FHF2"}]}],"length":192,"name":"Isoform 2 of Fibroblast growth factor 13","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":159,"end":192,"reference_id":"22705208","reference_source":"pmid","reference_html":"Crystal structure of the ternary complex of a NaV C-terminal domain, a fibroblast growth factor homologous factor, and calmodulin. <i> Wang C, Chung BC, Yan H, Lee SY, Pitt GS. </i> Structure, 2012","date":"2022-10-26T12:40:52.404Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4DCK"}],"region_id":"DP03875r001","statement":[{"text":"The PDB evidence shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0DP23"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q14524"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T14:14:29.713Z"}},{"start":159,"end":192,"reference_id":"25232683","reference_source":"pmid","reference_html":"Structural analyses of Ca²⁺/CaM interaction with NaV channel C-termini reveal mechanisms of calcium-dependent regulation. <i> Wang C, Chung BC, Yan H, Wang HG, Lee SY, Pitt GS. </i> Nat Commun, 2014","date":"2022-10-26T14:05:42.696Z","curator_id":"maspromonte","curator_name":"Maria Cristina Aspromonte","curator_orcid":"0000-0002-4937-6952","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4JPZ"}],"region_id":"DP03875r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q99250"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0DP23"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"The PDB evidence shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T14:12:18.552Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MALLRKSYSEPQLKGIVTKLYSRQGYHLQLQADGTIDGTKDEDSTYTLFNLIPVGLRVVAIQGVQTKLYLAMNSEGYLYTSELFTPECKFKESVFENYYVTYSSMIYRQQQSGRGWYLGLNKEGEIMKGNHVKKNKPAAHFLPKPLKVAMYKEPSLHDLTEFSRSGSGTPTKSRSVSGVLNGGKSMSHNEST","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"disorder_content":0.17708333333333334,"disprot_consensus":{"full":[{"start":159,"end":192,"type":"D"}],"Structural state":[{"start":159,"end":192,"type":"D"}]}},{"disprot_id":"DP03876","acc":"Q9UBK8","creator":"fkordevani","date":"2022-10-25T07:50:55.492Z","features":{"pfam":[{"id":"PF00175","name":"Oxidoreductase NAD-binding domain","start":542,"end":661},{"id":"PF00258","name":"Flavodoxin","start":6,"end":142},{"id":"PF00667","name":"FAD binding domain","start":271,"end":492}],"gene3D":[]},"genes":[{"name":{"value":"MTRR","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:7473","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:7473"}}]}}],"length":698,"name":"Methionine synthase reductase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":165,"end":216,"reference_id":"17892308","reference_source":"pmid","reference_html":"Mechanism of coenzyme binding to human methionine synthase reductase revealed through the crystal structure of the FNR-like module and isothermal titration calorimetry. <i> Wolthers KR, Lou X, Toogood HS, Leys D, Scrutton NS. </i> Biochemistry, 2007","date":"2022-10-25T07:53:59.883Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2QTL"},{"db":"PDB","id":"2QTZ"}],"region_id":"DP03876r001","statement":[{"text":"The first 54 residues are disordered, as are flexible regions Leu258−Asp271, Gln502−Ala515, and Val615−Ala620.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-02T18:44:52.526Z"}},{"start":258,"end":271,"reference_id":"17892308","reference_source":"pmid","reference_html":"Mechanism of coenzyme binding to human methionine synthase reductase revealed through the crystal structure of the FNR-like module and isothermal titration calorimetry. <i> Wolthers KR, Lou X, Toogood HS, Leys D, Scrutton NS. </i> Biochemistry, 2007","date":"2022-10-25T07:54:25.090Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2QTL"},{"db":"PDB","id":"2QTZ"}],"region_id":"DP03876r002","statement":[{"text":"The first 54 residues are disordered, as are flexible regions Leu258−Asp271, Gln502−Ala515, and Val615−Ala620.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-02T18:44:59.366Z"}},{"start":502,"end":515,"reference_id":"17892308","reference_source":"pmid","reference_html":"Mechanism of coenzyme binding to human methionine synthase reductase revealed through the crystal structure of the FNR-like module and isothermal titration calorimetry. <i> Wolthers KR, Lou X, Toogood HS, Leys D, Scrutton NS. </i> Biochemistry, 2007","date":"2022-11-03T10:07:36.623Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2QTL"},{"db":"PDB","id":"2QTZ"}],"region_id":"DP03876r003","statement":[{"text":"The first 54 residues are disordered, as are flexible regions Leu258−Asp271, Gln502−Ala515, and Val615−Ala620.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-03T14:13:22.496Z"}}],"regions_counter":3,"released":"2023_06","sequence":"MRRFLLLYATQQGQAKAIAEEICEQAVVHGFSADLHCISESDKYDLKTETAPLVVVVSTTGTGDPPDTARKFVKEIQNQTLPVDFFAHLRYGLLGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADDCVGLELVVEPWIAGLWPALRKHFRSSRGQEEISGALPVASPASSRTDLVKSELLHIESQVELLRFDDSGRKDSEVLKQNAVNSNQSNVVIEDFESSLTRSVPPLSQASLNIPGLPPEYLQVHLQESLGQEESQVSVTSADPVFQVPISKAVQLTTNDAIKTTLLVELDISNTDFSYQPGDAFSVICPNSDSEVQSLLQRLQLEDKREHCVLLKIKADTKKKGATLPQHIPAGCSLQFIFTWCLEIRAIPKKAFLRALVDYTSDSAEKRRLQELCSKQGAADYSRFVRDACACLLDLLLAFPSCQPPLSLLLEHLPKLQPRPYSCASSSLFHPGKLHFVFNIVEFLSTATTEVLRKGVCTGWLALLVASVLQPNIHASHEDSGKALAPKISISPRTTNSFHLPDDPSIPIIMVGPGTGIAPFIGFLQHREKLQEQHPDGNFGAMWLFFGCRHKDRDYLFRKELRHFLKHGILTHLKVSFSRDAPVGEEEAPAKYVQDNIQLHGQQVARILLQENGHIYVCGDAKNMAKDVHDALVQIISKEVGVEKLEAMKTLATLKEEKRYLQDIWS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.10458452722063037,"disorder_content":0.11461318051575932,"disprot_consensus":{"full":[{"start":165,"end":216,"type":"D"},{"start":258,"end":271,"type":"D"},{"start":502,"end":515,"type":"D"}],"Structural state":[{"start":165,"end":216,"type":"D"},{"start":258,"end":271,"type":"D"},{"start":502,"end":515,"type":"D"}]}},{"disprot_id":"DP03877","acc":"O43776","creator":"fkordevani","date":"2022-10-25T08:01:36.455Z","features":{"pfam":[{"id":"PF00152","name":"tRNA synthetases class II (D, K and N)","start":226,"end":541},{"id":"PF01336","name":"OB-fold nucleic acid binding domain","start":128,"end":207},{"id":"PF20917","name":"Asparaginal-tRNA synthetase, N-terminal domain","start":21,"end":110}],"gene3D":[]},"genes":[{"name":{"value":"NARS1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:7643","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:7643"}}]},"synonyms":[{"value":"NARS"},{"value":"NRS","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"30171954","url":"http://www.ncbi.nlm.nih.gov/pubmed/30171954","alternativeUrl":"https://europepmc.org/abstract/MED/30171954"}}]}]}],"length":548,"name":"Asparagine--tRNA ligase, cytoplasmic","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":98,"end":110,"reference_id":"30171954","reference_source":"pmid","reference_html":"Unique N-terminal extension domain of human asparaginyl-tRNA synthetase elicits CCR3-mediated chemokine activity. <i> Park JS, Park MC, Lee KY, Goughnour PC, Jeong SJ, Kim HS, Kim HJ, Lee BJ, Kim S, Han BW. </i> Int J Biol Macromol, 2018","date":"2022-10-25T08:03:47.945Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5XIX"}],"region_id":"DP03877r001","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-02T18:50:49.157Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MVLAELYVSDREGSDATGDGTKEKPFKTGLKALMTVGKEPFPTIYVDSQKENERWNVISKSQLKNIKKMWHREQMKSESREKKEAEDSLRREKNLEEAKKITIKNDPSLPEPKCVKIGALEGYRGQRVKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLADELCQCYNGVLLSTESSVAVYGMLNLTPKGKQAPGGHELSCDFWELIGLAPAGGADNLINEESDVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILKSPAGSIVHELNPNFQPPKRPFKRMNYSDAIVWLKEHDVKKEDGTFYEFGEDIPEAPERLMTDTINEPILLCRFPVEIKSFYMQRCPEDSRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQRCTP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","RNA-binding proteins"],"alphafold_very_low_content":0.0018248175182481751,"disorder_content":0.023722627737226276,"disprot_consensus":{"full":[{"start":98,"end":110,"type":"D"}],"Structural state":[{"start":98,"end":110,"type":"D"}]}},{"disprot_id":"DP03878","acc":"Q15233","creator":"fkordevani","date":"2022-10-25T08:07:51.712Z","features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":76,"end":140},{"id":"PF00076","name":"RNA recognition motif","start":150,"end":210},{"id":"PF08075","name":"NOPS (NUC059) domain","start":221,"end":272}],"gene3D":[]},"genes":[{"name":{"value":"NONO","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9393982","url":"http://www.ncbi.nlm.nih.gov/pubmed/9393982","alternativeUrl":"https://europepmc.org/abstract/MED/9393982"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:7871","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:7871"}}]},"synonyms":[{"value":"NRB54","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9341872","url":"http://www.ncbi.nlm.nih.gov/pubmed/9341872","alternativeUrl":"https://europepmc.org/abstract/MED/9341872"}}]}]}],"length":471,"name":"Non-POU domain-containing octamer-binding protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":54,"end":65,"reference_id":"35245601","reference_source":"pmid","reference_html":"Crystal structure of SFPQ-NONO heterodimer. <i> Schell B, Legrand P, Fribourg S. </i> Biochimie, 2022","date":"2022-10-25T08:09:27.127Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7PU5"}],"region_id":"DP03878r001","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-02T19:00:51.956Z"}},{"start":53,"end":65,"reference_id":"22416126","reference_source":"pmid","reference_html":"Structure of the heterodimer of human NONO and paraspeckle protein component 1 and analysis of its role in subnuclear body formation. <i> Passon DM, Lee M, Rackham O, Stanley WA, Sadowska A, Filipovska A, Fox AH, Bond CS. </i> Proc Natl Acad Sci U S A, 2012","date":"2022-11-03T10:08:34.816Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3SDE"}],"region_id":"DP03878r002","statement":[{"text":"The asymmetric unit contains a single heterodimer, residues 66–320 of PSPC1 and residues 66–304 of NONO (494 aa), 470 waters, and 11 ethylene glycol molecules.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-03T14:13:59.011Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MQSNKTFNLEKQNHTPRKHHQHHHQQQHHQQQQQQPPPPPIPANGQQASSQNEGLTIDLKNFRKPGEKTFTQRSRLFVGNLPPDITEEEMRKLFEKYGKAGEVFIHKDKGFGFIRLETRTLAEIAKVELDNMPLRGKQLRVRFACHSASLTVRNLPQYVSNELLEEAFSVFGQVERAVVIVDDRGRPSGKGIVEFSGKPAARKALDRCSEGSFLLTTFPRPVTVEPMDQLDDEEGLPEKLVIKNQQFHKEREQPPRFAQPGSFEYEYAMRWKALIEMEKQQQDQVDRNIKEAREKLEMEMEAARHEHQVMLMRQDLMRRQEELRRMEELHNQEVQKRKQLELRQEEERRRREEEMRRQQEEMMRRQQEGFKGTFPDAREQEIRMGQMAMGGAMGINNRGAMPPAPVPAGTPAPPGPATMMPDGTLGLTPPTTERFGQAATMEGIGAIGGTPPAFNRAAPGAEFAPNKRRRY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Cancer-related proteins","Condensates-related proteins"],"alphafold_very_low_content":0.2632696390658174,"disorder_content":0.027600849256900213,"disprot_consensus":{"full":[{"start":53,"end":65,"type":"D"}],"Structural state":[{"start":53,"end":65,"type":"D"}]}},{"disprot_id":"DP03879","acc":"E9AE57","creator":"jssuarez","date":"2022-10-25T10:34:26.047Z","features":{"pfam":[{"id":"PF05681","name":"Fumarate hydratase (Fumerase)","start":79,"end":353},{"id":"PF05683","name":"Fumarase C-terminus","start":360,"end":565}],"gene3D":[]},"genes":[{"name":{"value":"FH2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"22569531","url":"http://www.ncbi.nlm.nih.gov/pubmed/22569531","alternativeUrl":"https://europepmc.org/abstract/MED/22569531"}}]},"orfNames":[{"value":"LMJF_29_1960","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"CBZ12536.1","url":"https://www.ebi.ac.uk/ena/browser/view/CBZ12536.1"}}]}]}],"length":568,"name":"Fumarate hydratase 2","ncbi_taxon_id":5664,"organism":"Leishmania major","regions":[{"start":1,"end":21,"reference_id":"31743022","reference_source":"pmid","reference_html":"Structural and Biochemical Investigations of the [4Fe-4S] Cluster-Containing Fumarate Hydratase from Leishmania major. <i> Feliciano PR, Drennan CL. </i> Biochemistry, 2019","date":"2022-10-25T10:44:31.567Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"6UNZ"},{"db":"PDB","id":"6UO0"},{"db":"PDB","id":"6UOI"},{"db":"PDB","id":"6UOJ"}],"region_id":"DP03879r001","statement":[{"text":"The residues visualized in each structure, of 568 residues, are listed in Table S5. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-05T15:36:13.811Z"}}],"regions_counter":2,"released":"2022_12","sequence":"MSLCDQCEIGCRRVGIKDIEDASAVNADFHFSAIFQPTDPHHHQTEFAKVEGSEKYVEEVEVFGRQALKVNPEALTILAHRAFSDVHHFFRKDHLEGWRRAIEDPEASDNDRYVATTLLKNACIAAGRVLPSCQDTGTAIVLGKRGELCWTGGEDEKYLSKGIWNAYRYHNLRYSQTAALDMFKECNTGDNLPAQLDLLAVPGSDYEFLFIAKGGGSANKAYLYQETKALLNPKSLRAFIEEKLKTLGTAACPPYHIALVIGGTSAEMTMKTVKLASCRYYDSLPTTGDKYGRAFRDPEWEKIVMEVAQKSGIGAQFGGKYFAHQARVIRLPRHGASCPVGLAVSCSADRQILAHINKSGIYIEQLEQNPAQYLPDIPEVHLSTTSVKVDLKRPIDKVRQQLSQYPVGTRVMLNGTLIVARDIAHAKIKEMMDNGEPLPEYMKTSPIYYAGPAKTPEGYASGSFGPTTAGRMDSYVDLFQSHGGSYITLAKGNRSKQVTDACKKHGGFYLGSIGGPAAILAKDSIKQVTCLAFPELGMEAVWKIEVEDFPAFIVVDDKGNDMYSKTLA","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"alphafold_very_low_content":0.022887323943661973,"disorder_content":0.03697183098591549,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"}],"Structural state":[{"start":1,"end":21,"type":"D"}]}},{"disprot_id":"DP03880","acc":"P27913","creator":"jssuarez","date":"2022-10-25T11:06:52.771Z","features":{"pfam":[{"id":"PF00869","name":"Flavivirus glycoprotein, central and dimerisation domains","start":282,"end":576},{"id":"PF01003","name":"Flavivirus capsid protein C","start":6,"end":113},{"id":"PF01004","name":"Flavivirus envelope glycoprotein M","start":207,"end":280},{"id":"PF01570","name":"Flavivirus polyprotein propeptide","start":120,"end":204},{"id":"PF02832","name":"Flavivirus glycoprotein, immunoglobulin-like domain","start":578,"end":673},{"id":"PF21659","name":"Flavivirus envelope glycoprotein E, stem/anchor domain","start":676,"end":770}],"gene3D":[]},"genes":[],"length":791,"name":"Genome polyprotein","ncbi_taxon_id":11058,"organism":"Dengue virus type 1 (strain Jamaica/CV1636/1977)","regions":[{"start":14,"end":23,"reference_id":"25412346","reference_source":"pmid","reference_html":"Understanding dengue virus capsid protein disordered N-Terminus and pep14-23-based inhibition. <i> Faustino AF, Guerra GM, Huber RG, Hollmann A, Domingues MM, Barbosa GM, Enguita FJ, Bond PJ, Castanho MA, Da Poian AT, Almeida FC, Santos NC, Martins IC. </i> ACS Chem Biol, 2015","date":"2022-10-25T11:16:01.774Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP03880r001","statement":[{"text":"As the corresponding DENV C domain, the peptide is intrinsically disordered in aqueous solution (Figure 2C) but gains structure upon binding to the DPC micelles (Figure 3A), forming an α-helix spanning from Met2 to Ala6.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T19:41:33.729Z"}},{"start":15,"end":19,"reference_id":"25412346","reference_source":"pmid","reference_html":"Understanding dengue virus capsid protein disordered N-Terminus and pep14-23-based inhibition. <i> Faustino AF, Guerra GM, Huber RG, Hollmann A, Domingues MM, Barbosa GM, Enguita FJ, Bond PJ, Castanho MA, Da Poian AT, Almeida FC, Santos NC, Martins IC. </i> ACS Chem Biol, 2015","date":"2022-11-02T09:37:35.080Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","region_id":"DP03880r002","statement":[{"text":"As the corresponding DENV C domain, the peptide is intrinsically disordered in aqueous solution (Figure 2C) but gains structure upon binding to the DPC micelles (Figure 3A), forming an α-helix spanning from Met2 to Ala6.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"ChEBI","id":"78018","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-12T15:24:01.687Z"}},{"start":14,"end":23,"reference_id":"25412346","reference_source":"pmid","reference_html":"Understanding dengue virus capsid protein disordered N-Terminus and pep14-23-based inhibition. <i> Faustino AF, Guerra GM, Huber RG, Hollmann A, Domingues MM, Barbosa GM, Enguita FJ, Bond PJ, Castanho MA, Da Poian AT, Almeida FC, Santos NC, Martins IC. </i> ACS Chem Biol, 2015","date":"2023-08-14T19:20:33.276Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006048","ec_ontology":"ECO","ec_name":"field potential recording evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"ec_go":"IDA","region_id":"DP03880r003","statement":[{"text":"Both ΔΠ and zeta potential show that pep14-23 interacts with POPG-containing lipid systems (Figure 2A and B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"ChEBI","id":"34080","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-16T14:18:16.536Z"}},{"start":14,"end":23,"reference_id":"25412346","reference_source":"pmid","reference_html":"Understanding dengue virus capsid protein disordered N-Terminus and pep14-23-based inhibition. <i> Faustino AF, Guerra GM, Huber RG, Hollmann A, Domingues MM, Barbosa GM, Enguita FJ, Bond PJ, Castanho MA, Da Poian AT, Almeida FC, Santos NC, Martins IC. </i> ACS Chem Biol, 2015","date":"2022-11-02T09:36:58.093Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"ec_go":"EXP","region_id":"DP03880r004","statement":[{"text":"It was observed that the most negatively charged pure POPG vesicles induce a small α-helical conformational switch at that concentration.","type":"Results"},{"text":"The data shows that electrostatic forces play a significant role in the positively charged pep14-23 (net charge +5) interaction with negatively charged POPG vesicles.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"ChEBI","id":"34080","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-12T15:18:59.847Z"}},{"start":14,"end":23,"reference_id":"25412346","reference_source":"pmid","reference_html":"Understanding dengue virus capsid protein disordered N-Terminus and pep14-23-based inhibition. <i> Faustino AF, Guerra GM, Huber RG, Hollmann A, Domingues MM, Barbosa GM, Enguita FJ, Bond PJ, Castanho MA, Da Poian AT, Almeida FC, Santos NC, Martins IC. </i> ACS Chem Biol, 2015","date":"2022-10-25T11:27:20.033Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"region_id":"DP03880r005","statement":[{"text":"It was observed that the most negatively charged pure POPG vesicles induce a small α-helical conformational switch at that concentration.","type":"Results"},{"text":"The data shows that electrostatic forces play a significant role in the positively charged pep14-23 (net charge +5) interaction with negatively charged POPG vesicles.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T19:41:35.132Z"}}],"regions_counter":5,"released":"2022_12","sequence":"MNNQRKKTGRPSFNMLKRARNRVSTGSQLAKRFSKGLLSGQGPMKLVMAFIAFLRFLAIPPTAGILARWSSFKKNGAIKVLRGFKKEISSMLNIMNRRKRSVTMLLMLLPTALAFHLTTRGGEPTLIVSKQERGKSLLFKTSAGVNMCTLIAMDLGELCEDTMTYKCPRITERQPDDVDCWCNATDTWVTYGTCSQTGEHRRDKRSVALAPHVGLGLETRTETWMSSEGAWKQIQKVETWALRHPGFTVIGLFLAHAIGTSITQKGIIFILLMLVTPSMAMRCVGIGNRDFVEGLSGATWVDVVLEHGSCVTTMAKNKPTLDIELLKTEVTNPAVLRKLCIEAKISNTTTDSRCPTQGEATLVEEQDANFVCRRTFVDRGWGNGCGLFGKGSFLTCAKFKCVTKLEGKIVQYENLKYSVIVTVHTGDQHQVGNETTEHGTIATITPQAPTSEIQLTDYGALTLDCSPRTGLDFNRVVLLTMKKKSWLVHKQWFLDLPLPWTSGASTSQETWNRQDLLVTFKTAHAKKQEVVVLGSQEGAMHTALTGATEIQTSGTTTIFAGHLKCRLKMDKLTLKGMSYVMCTGSFKLEKEVAETQHGTVLVQVKYEGTDAPCKIPFSSQDEKGVTQNGRLITANPIVIDKEKPVNIEAEPPFGESYIVVGSGEKALKLSWFKKGSSIGKMFEATARGARRMAILGDTAWDFGSIGGVFTSVGKLIHQIFGTAYGILFSGVSWTMKIGIGILLTWLGLNSRSTSLSMTCIAVGMVTLYLGVMVQADSGCVINWKGKELKCG","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Flavivirus"],"dataset":["Neglected tropical diseases proteins","Viral proteins"],"disorder_content":0.012642225031605562,"disprot_consensus":{"full":[{"start":14,"end":23,"type":"T"}],"Structural state":[{"start":14,"end":23,"type":"D"}],"Molecular function":[{"start":14,"end":23,"type":"F"}],"Structural transition":[{"start":14,"end":23,"type":"T"}]}},{"disprot_id":"DP03881","acc":"O15118","creator":"fkordevani","date":"2022-10-25T15:03:04.624Z","features":{"pfam":[{"id":"PF12349","name":"Sterol-sensing domain of SREBP cleavage-activation","start":650,"end":802},{"id":"PF16414","name":"Niemann-Pick C1 N terminus","start":23,"end":266},{"id":"PF22314","name":"NPC1, middle luminal domain","start":392,"end":607}],"gene3D":[]},"genes":[{"name":{"value":"NPC1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:7897","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:7897"}}]}}],"length":1278,"name":"NPC intracellular cholesterol transporter 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":605,"end":620,"reference_id":"26771495","reference_source":"pmid","reference_html":"Ebola Viral Glycoprotein Bound to Its Endosomal Receptor Niemann-Pick C1. <i> Wang H, Shi Y, Song J, Qi J, Lu G, Yan J, Gao GF. </i> Cell, 2016","date":"2022-11-03T10:14:08.635Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5F18"},{"db":"PDB","id":"5F1B"}],"region_id":"DP03881r001","statement":[{"text":"In our crystal structure, only residues 384 to 624 are visible, and the secondary structures are labeled. We cannot see the electron density for the N-terminal 12 amino acids and C-terminal 16 amino acids, indicating these disordered regions might be flexible loops.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-03T14:17:00.712Z"}},{"start":374,"end":383,"reference_id":"26771495","reference_source":"pmid","reference_html":"Ebola Viral Glycoprotein Bound to Its Endosomal Receptor Niemann-Pick C1. <i> Wang H, Shi Y, Song J, Qi J, Lu G, Yan J, Gao GF. </i> Cell, 2016","date":"2022-11-03T10:14:33.737Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5F18"},{"db":"PDB","id":"5F1B"}],"region_id":"DP03881r002","statement":[{"text":"In our crystal structure, only residues 384 to 624 are visible, and the secondary structures are labeled. We cannot see the electron density for the N-terminal 12 amino acids and C-terminal 16 amino acids, indicating these disordered regions might be flexible loops.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-03T14:16:55.249Z"}},{"start":288,"end":333,"reference_id":"31919352","reference_source":"pmid","reference_html":"Structural basis for itraconazole-mediated NPC1 inhibition. <i> Long T, Qi X, Hassan A, Liang Q, De Brabander JK, Li X. </i> Nat Commun, 2020","date":"2022-11-03T10:12:21.033Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6UOX"}],"region_id":"DP03881r004","statement":[{"text":"The densities of residues 23, 288–333, 642–649, 797–813, and 1256–1278 of NPC1 were not resolved nor built.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-03T14:14:34.065Z"}},{"start":797,"end":813,"reference_id":"31919352","reference_source":"pmid","reference_html":"Structural basis for itraconazole-mediated NPC1 inhibition. <i> Long T, Qi X, Hassan A, Liang Q, De Brabander JK, Li X. </i> Nat Commun, 2020","date":"2022-11-03T10:12:14.273Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6UOX"}],"region_id":"DP03881r005","statement":[{"text":"The densities of residues 23, 288–333, 642–649, 797–813, and 1256–1278 of NPC1 were not resolved nor built.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-03T14:14:34.664Z"}},{"start":1256,"end":1278,"reference_id":"31919352","reference_source":"pmid","reference_html":"Structural basis for itraconazole-mediated NPC1 inhibition. <i> Long T, Qi X, Hassan A, Liang Q, De Brabander JK, Li X. </i> Nat Commun, 2020","date":"2022-11-03T10:12:07.593Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6UOX"}],"region_id":"DP03881r006","statement":[{"text":"The densities of residues 23, 288–333, 642–649, 797–813, and 1256–1278 of NPC1 were not resolved nor built.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-03T14:14:35.235Z"}},{"start":289,"end":329,"reference_id":"27238017","reference_source":"pmid","reference_html":"Structural Insights into the Niemann-Pick C1 (NPC1)-Mediated Cholesterol Transfer and Ebola Infection. <i> Gong X, Qian H, Zhou X, Wu J, Wan T, Cao P, Huang W, Zhao X, Wang X, Wang P, Shi Y, Gao GF, Zhou Q, Yan N. </i> Cell, 2016","date":"2022-10-25T15:15:45.738Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5JNX"}],"region_id":"DP03881r007","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-02T19:54:50.130Z"}},{"start":773,"end":803,"reference_id":"27238017","reference_source":"pmid","reference_html":"Structural Insights into the Niemann-Pick C1 (NPC1)-Mediated Cholesterol Transfer and Ebola Infection. <i> Gong X, Qian H, Zhou X, Wu J, Wan T, Cao P, Huang W, Zhao X, Wang X, Wang P, Shi Y, Gao GF, Zhou Q, Yan N. </i> Cell, 2016","date":"2022-11-03T10:11:17.170Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5JNX"}],"region_id":"DP03881r008","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-03T14:15:39.559Z"}},{"start":960,"end":983,"reference_id":"27238017","reference_source":"pmid","reference_html":"Structural Insights into the Niemann-Pick C1 (NPC1)-Mediated Cholesterol Transfer and Ebola Infection. <i> Gong X, Qian H, Zhou X, Wu J, Wan T, Cao P, Huang W, Zhao X, Wang X, Wang P, Shi Y, Gao GF, Zhou Q, Yan N. </i> Cell, 2016","date":"2022-11-03T10:11:29.731Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5JNX"}],"region_id":"DP03881r009","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-03T14:15:39.860Z"}},{"start":1252,"end":1278,"reference_id":"27238017","reference_source":"pmid","reference_html":"Structural Insights into the Niemann-Pick C1 (NPC1)-Mediated Cholesterol Transfer and Ebola Infection. <i> Gong X, Qian H, Zhou X, Wu J, Wan T, Cao P, Huang W, Zhao X, Wang X, Wang P, Shi Y, Gao GF, Zhou Q, Yan N. </i> Cell, 2016","date":"2022-11-03T10:11:43.374Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5JNX"}],"region_id":"DP03881r010","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-03T14:15:41.270Z"}}],"regions_counter":10,"released":"2023_06","sequence":"MTARGLALGLLLLLLCPAQVFSQSCVWYGECGIAYGDKRYNCEYSGPPKPLPKDGYDLVQELCPGFFFGNVSLCCDVRQLQTLKDNLQLPLQFLSRCPSCFYNLLNLFCELTCSPRQSQFLNVTATEDYVDPVTNQTKTNVKELQYYVGQSFANAMYNACRDVEAPSSNDKALGLLCGKDADACNATNWIEYMFNKDNGQAPFTITPVFSDFPVHGMEPMNNATKGCDESVDEVTAPCSCQDCSIVCGPKPQPPPPPAPWTILGLDAMYVIMWITYMAFLLVFFGAFFAVWCYRKRYFVSEYTPIDSNIAFSVNASDKGEASCCDPVSAAFEGCLRRLFTRWGSFCVRNPGCVIFFSLVFITACSSGLVFVRVTTNPVDLWSAPSSQARLEKEYFDQHFGPFFRTEQLIIRAPLTDKHIYQPYPSGADVPFGPPLDIQILHQVLDLQIAIENITASYDNETVTLQDICLAPLSPYNTNCTILSVLNYFQNSHSVLDHKKGDDFFVYADYHTHFLYCVRAPASLNDTSLLHDPCLGTFGGPVFPWLVLGGYDDQNYNNATALVITFPVNNYYNDTEKLQRAQAWEKEFINFVKNYKNPNLTISFTAERSIEDELNRESDSDVFTVVISYAIMFLYISLALGHMKSCRRLLVDSKVSLGIAGILIVLSSVACSLGVFSYIGLPLTLIVIEVIPFLVLAVGVDNIFILVQAYQRDERLQGETLDQQLGRVLGEVAPSMFLSSFSETVAFFLGALSVMPAVHTFSLFAGLAVFIDFLLQITCFVSLLGLDIKRQEKNRLDIFCCVRGAEDGTSVQASESCLFRFFKNSYSPLLLKDWMRPIVIAIFVGVLSFSIAVLNKVDIGLDQSLSMPDDSYMVDYFKSISQYLHAGPPVYFVLEEGHDYTSSKGQNMVCGGMGCNNDSLVQQIFNAAQLDNYTRIGFAPSSWIDDYFDWVKPQSSCCRVDNITDQFCNASVVDPACVRCRPLTPEGKQRPQGGDFMRFLPMFLSDNPNPKCGKGGHAAYSSAVNILLGHGTRVGATYFMTYHTVLQTSADFIDALKKARLIASNVTETMGINGSAYRVFPYSVFYVFYEQYLTIIDDTIFNLGVSLGAIFLVTMVLLGCELWSAVIMCATIAMVLVNMFGVMWLWGISLNAVSLVNLVMSCGISVEFCSHITRAFTVSMKGSRVERAEEALAHMGSSVFSGITLTKFGGIVVLAFAKSQIFQIFYFRMYLAMVLLGATHGLIFLPVLLSYIGPSVNKAKSCATEERYKGTERERLLNF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Autophagy-related proteins"],"alphafold_very_low_content":0.03834115805946792,"disorder_content":0.12832550860719874,"disprot_consensus":{"full":[{"start":288,"end":333,"type":"D"},{"start":374,"end":383,"type":"D"},{"start":605,"end":620,"type":"D"},{"start":773,"end":813,"type":"D"},{"start":960,"end":983,"type":"D"},{"start":1252,"end":1278,"type":"D"}],"Structural state":[{"start":288,"end":333,"type":"D"},{"start":374,"end":383,"type":"D"},{"start":605,"end":620,"type":"D"},{"start":773,"end":813,"type":"D"},{"start":960,"end":983,"type":"D"},{"start":1252,"end":1278,"type":"D"}]}},{"disprot_id":"DP03882","acc":"P01111","creator":"fkordevani","date":"2022-10-25T15:17:27.940Z","features":{"pfam":[{"id":"PF00071","name":"Ras family","start":5,"end":164}],"gene3D":[]},"genes":[{"name":{"value":"NRAS"},"synonyms":[{"value":"HRAS1"}]}],"length":189,"name":"GTPase NRas","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":59,"end":70,"reference_id":"31390567","reference_source":"pmid","reference_html":"Isoform-Specific Destabilization of the Active Site Reveals a Molecular Mechanism of Intrinsic Activation of KRas G13D. <i> Johnson CW, Lin YJ, Reid D, Parker J, Pavlopoulos S, Dischinger P, Graveel C, Aguirre AJ, Steensma M, Haigis KM, Mattos C. </i> Cell Rep, 2019","date":"2022-10-25T15:19:17.949Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6E6H"}],"region_id":"DP03882r001","statement":[{"text":"However, in Ka13GNP, there is significant adjustment of ϕ,ψ torsions associated with P loop residues, the γ-phosphate of GppNHp is shifted toward switch I, and switch II is disordered from residue 59 to 70. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-07T14:30:02.594Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNSKSFADINLYREQIKRVKDSDDVPMVLVGNKCDLPTRTVDTKQAHELAKSYGIPFIETSAKTRQGVEDAFYTLVREIRQYRMKKLNSSDDGTQGCMGLPCVVM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Cancer-related proteins"],"alphafold_very_low_content":0.037037037037037035,"disorder_content":0.06349206349206349,"disprot_consensus":{"full":[{"start":59,"end":70,"type":"D"}],"Structural state":[{"start":59,"end":70,"type":"D"}]}},{"disprot_id":"DP03884","acc":"O96028","creator":"fkordevani","date":"2022-10-27T08:33:11.920Z","features":{"pfam":[{"id":"PF00505","name":"HMG (high mobility group) box","start":457,"end":506},{"id":"PF00628","name":"PHD-finger","start":834,"end":872},{"id":"PF00855","name":"PWWP domain","start":223,"end":303},{"id":"PF00855","name":"PWWP domain","start":882,"end":969},{"id":"PF00856","name":"SET domain","start":1074,"end":1180},{"id":"PF17907","name":"AWS domain","start":1022,"end":1060},{"id":"PF17982","name":"NSD Cys-His rich domain","start":1282,"end":1327},{"id":"PF22908","name":"Histone-lysine N-methyltransferase NSD-like, PHD zinc finger","start":714,"end":762},{"id":"PF23004","name":"Histone-lysine N-methyltransferase NSD-like, variant PHD zinc finger","start":764,"end":816},{"id":"PF23011","name":"Histone-lysine N-methyltransferase NSD-like, PHD zinc finger 1","start":663,"end":711},{"id":"PF23011","name":"Histone-lysine N-methyltransferase NSD-like, PHD zinc finger 1","start":1239,"end":1280}],"gene3D":[]},"genes":[{"name":{"value":"NSD2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:12766","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:12766"}}]},"synonyms":[{"value":"KIAA1090"},{"value":"MMSET"},{"value":"TRX5"},{"value":"WHSC1"}]}],"length":1365,"name":"Histone-lysine N-methyltransferase NSD2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":661,"end":986,"reference_id":"33361816","reference_source":"pmid","reference_html":"Molecular basis of nucleosomal H3K36 methylation by NSD methyltransferases. <i> Li W, Tian W, Yuan G, Deng P, Sengupta D, Cheng Z, Cao Y, Ren J, Qin Y, Zhou Y, Jia Y, Gozani O, Patel DJ, Wang Z. </i> Nature, 2021","date":"2022-12-07T15:14:46.419Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7CRO"}],"region_id":"DP03884r001","statement":[{"text":"The PDB shows the protein lacks electron density in this region when in complex with 187-bp nucleosome core particles, indicating it is disordered.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu1099Lys","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr1150Ala","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-07T15:18:59.227Z"}},{"start":1206,"end":1365,"reference_id":"33361816","reference_source":"pmid","reference_html":"Molecular basis of nucleosomal H3K36 methylation by NSD methyltransferases. <i> Li W, Tian W, Yuan G, Deng P, Sengupta D, Cheng Z, Cao Y, Ren J, Qin Y, Zhou Y, Jia Y, Gozani O, Patel DJ, Wang Z. </i> Nature, 2021","date":"2022-12-07T15:15:32.722Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7CRO"}],"region_id":"DP03884r002","statement":[{"text":"The PDB shows the protein lacks electron density in this region when in complex with 187-bp nucleosome core particles, indicating it is disordered.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu1099Lys","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr1150Ala","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-07T15:19:00.885Z"}},{"start":1221,"end":1226,"reference_id":"24595546","reference_source":"pmid","reference_html":"A Basic Post-SET Extension of NSDs Is Essential for Nucleosome Binding In Vitro. <i> Allali-Hassani A, Kuznetsova E, Hajian T, Wu H, Dombrovski L, Li Y, Gräslund S, Arrowsmith CH, Schapira M, Vedadi M. </i> J Biomol Screen, 2014","date":"2023-05-08T08:07:48.479Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"GO:0046975","term_name":"histone methyltransferase activity (H3-K36 specific)","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IMP","region_id":"DP03884r003","statement":[{"text":"The essential sequence was further narrowed down for NSD2 to residues 1221 to 1226 (TKKKTR), the deletion of which abolished the ability of NSD2 to methylate nucleosome.","type":"Discussion"}],"term_comment":"","term_def":"\"Catalysis of the reaction: S-adenosyl-L-methionine + histone H3 L-lysine (position 36) = S-adenosyl-L-homocysteine + histone H3 N6-methyl-L-lysine (position 36). This reaction is the addition of a methyl group onto lysine at position 36 of the histone H3 protein.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Thr1221-Arg1226del","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T13:10:06.432Z"}}],"regions_counter":3,"released":"2023_06","sequence":"MEFSIKQSPLSVQSVVKCIKMKQAPEILGSANGKTPSCEVNRECSVFLSKAQLSSSLQEGVMQKFNGHDALPFIPADKLKDLTSRVFNGEPGAHDAKLRFESQEMKGIGTPPNTTPIKNGSPEIKLKITKTYMNGKPLFESSICGDSAADVSQSEENGQKPENKARRNRKRSIKYDSLLEQGLVEAALVSKISSPSDKKIPAKKESCPNTGRDKDHLLKYNVGDLVWSKVSGYPWWPCMVSADPLLHSYTKLKGQKKSARQYHVQFFGDAPERAWIFEKSLVAFEGEGQFEKLCQESAKQAPTKAEKIKLLKPISGKLRAQWEMGIVQAEEAASMSVEERKAKFTFLYVGDQLHLNPQVAKEAGIAAESLGEMAESSGVSEEAAENPKSVREECIPMKRRRRAKLCSSAETLESHPDIGKSTPQKTAEADPRRGVGSPPGRKKTTVSMPRSRKGDAASQFLVFCQKHRDEVVAEHPDASGEEIEELLRSQWSLLSEKQRARYNTKFALVAPVQAEEDSGNVNGKKRNHTKRIQDPTEDAEAEDTPRKRLRTDKHSLRKRDTITDKTARTSSYKAMEAASSLKSQAATKNLSDACKPLKKRNRASTAASSALGFSKSSSPSASLTENEVSDSPGDEPSESPYESADETQTEVSVSSKKSERGVTAKKEYVCQLCEKPGSLLLCEGPCCGAFHLACLGLSRRPEGRFTCSECASGIHSCFVCKESKTDVKRCVVTQCGKFYHEACVKKYPLTVFESRGFRCPLHSCVSCHASNPSNPRPSKGKMMRCVRCPVAYHSGDACLAAGCSVIASNSIICTAHFTARKGKRHHAHVNVSWCFVCSKGGSLLCCESCPAAFHPDCLNIEMPDGSWFCNDCRAGKKLHFQDIIWVKLGNYRWWPAEVCHPKNVPPNIQKMKHEIGEFPVFFFGSKDYYWTHQARVFPYMEGDRGSRYQGVRGIGRVFKNALQEAEARFREIKLQREARETQESERKPPPYKHIKVNKPYGKVQIYTADISEIPKCNCKPTDENPCGFDSECLNRMLMFECHPQVCPAGEFCQNQCFTKRQYPETKIIKTDGKGWGLVAKRDIRKGEFVNEYVGELIDEEECMARIKHAHENDITHFYMLTIDKDRIIDAGPKGNYSRFMNHSCQPNCETLKWTVNGDTRVGLFAVCDIPAGTELTFNYNLDCLGNEKTVCRCGASNCSGFLGDRPKTSTTLSSEEKGKKTKKKTRRRRAKGEGKRQSEDECFRCGDGGQLVLCDRKFCTKAYHLSCLGLGKRPFGKWECPWHHCDVCGKPSTSFCHLCPNSFCKEHQDGTAFSCTPDGRSYCCEHDLGAASVRSTKTEKPPPEPGKPKGKRRRRRGWRRVTEGK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Cancer-related proteins","Condensates-related proteins"],"alphafold_very_low_content":0.38974358974358975,"disorder_content":0.35604395604395606,"disprot_consensus":{"full":[{"start":661,"end":986,"type":"D"},{"start":1206,"end":1365,"type":"D"}],"Structural state":[{"start":661,"end":986,"type":"D"},{"start":1206,"end":1365,"type":"D"}],"Molecular function":[{"start":1221,"end":1226,"type":"F"}]}},{"disprot_id":"DP03885","acc":"P49902","creator":"fkordevani","date":"2022-10-27T13:22:56.668Z","features":{"pfam":[{"id":"PF05761","name":"5' nucleotidase family","start":35,"end":488}],"gene3D":[]},"genes":[{"name":{"value":"NT5C2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:8022","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8022"}}]},"synonyms":[{"value":"NT5B"},{"value":"NT5CP"},{"value":"PNT5"}]}],"length":561,"name":"Cytosolic purine 5'-nucleotidase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":489,"end":536,"reference_id":"21396942","reference_source":"pmid","reference_html":"Structural basis for the allosteric regulation and substrate recognition of human cytosolic 5'-nucleotidase II. <i> Walldén K, Nordlund P. </i> J Mol Biol, 2011","date":"2022-12-15T14:20:03.899Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2XCW"},{"db":"PDB","id":"2XJD"},{"db":"PDB","id":"2XJF"},{"db":"PDB","id":"2XCV"},{"db":"PDB","id":"2XJE"},{"db":"PDB","id":"2XJB"},{"db":"PDB","id":"2XJC"}],"region_id":"DP03885r001","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-16T12:56:51.528Z"}},{"start":399,"end":419,"reference_id":"21396942","reference_source":"pmid","reference_html":"Structural basis for the allosteric regulation and substrate recognition of human cytosolic 5'-nucleotidase II. <i> Walldén K, Nordlund P. </i> J Mol Biol, 2011","date":"2022-10-27T13:38:58.315Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2XCW"},{"db":"PDB","id":"2XJD"},{"db":"PDB","id":"2XJF"},{"db":"PDB","id":"2XCX"},{"db":"PDB","id":"2XCV"},{"db":"PDB","id":"2XJE"},{"db":"PDB","id":"2XJB"},{"db":"PDB","id":"2XJC"}],"region_id":"DP03885r002","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-16T13:13:22.571Z"}},{"start":1,"end":23,"reference_id":"29990496","reference_source":"pmid","reference_html":"Structure and Mechanisms of NT5C2 Mutations Driving Thiopurine Resistance in Relapsed Lymphoblastic Leukemia. <i> Dieck CL, Tzoneva G, Forouhar F, Carpenter Z, Ambesi-Impiombato A, Sánchez-Martín M, Kirschner-Schwabe R, Lew S, Seetharaman J, Tong L, Ferrando AA. </i> Cancer Cell, 2018","date":"2022-12-15T14:50:08.164Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6DDQ"},{"db":"PDB","id":"6DDK"},{"db":"PDB","id":"6DDC"},{"db":"PDB","id":"6DDO"},{"db":"PDB","id":"6DDB"},{"db":"PDB","id":"6DDL"}],"region_id":"DP03885r003","statement":[{"text":"The Crystal structure of the NT5C2 protein in the active state shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-16T13:00:54.496Z"}},{"start":489,"end":561,"reference_id":"29990496","reference_source":"pmid","reference_html":"Structure and Mechanisms of NT5C2 Mutations Driving Thiopurine Resistance in Relapsed Lymphoblastic Leukemia. <i> Dieck CL, Tzoneva G, Forouhar F, Carpenter Z, Ambesi-Impiombato A, Sánchez-Martín M, Kirschner-Schwabe R, Lew S, Seetharaman J, Tong L, Ferrando AA. </i> Cancer Cell, 2018","date":"2022-12-15T14:49:07.678Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6DE3"},{"db":"PDB","id":"6DE1"},{"db":"PDB","id":"6DE2"}],"region_id":"DP03885r004","statement":[{"text":"The N- and C-termini amino acids (L24 and D552), and the termini amino acids (T510 and P541) of the disordered region in the C segment are also labeled.","type":"Results"},{"text":"Of note, this tightly closed conformation is released in the allosterically activated structure of NT5C2 in which the C-terminal is no longer visible at the dimer interface and is also displaced from the surface of the neighboring subunit by the N-terminal segment (Figure S5B).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-16T13:11:11.769Z"}},{"start":403,"end":419,"reference_id":"29990496","reference_source":"pmid","reference_html":"Structure and Mechanisms of NT5C2 Mutations Driving Thiopurine Resistance in Relapsed Lymphoblastic Leukemia. <i> Dieck CL, Tzoneva G, Forouhar F, Carpenter Z, Ambesi-Impiombato A, Sánchez-Martín M, Kirschner-Schwabe R, Lew S, Seetharaman J, Tong L, Ferrando AA. </i> Cancer Cell, 2018","date":"2022-12-15T14:25:12.074Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6DE1"},{"db":"PDB","id":"6DD3"},{"db":"PDB","id":"6DE0"},{"db":"PDB","id":"6DDY"}],"region_id":"DP03885r005","statement":[{"text":"The N- and C-termini amino acids (S4 and S488), and the termini amino acids (L402 and R421) of the disordered region in the arm segment are also labeled.","type":"Figure"},{"text":"Specifically, the loop at the tip of the helical arm segment of NT5C2 establishes intimate contacts with the other monomer in the basal structure, yet these contacts are lost upon activation with the helical arm pivoting away from the other monomer and the tip region becoming disordered upon allosteric activation supporting a role for this element in NT5C2 regulation (Figure 2A–F).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-16T12:58:41.118Z"}},{"start":403,"end":419,"reference_id":"29990496","reference_source":"pmid","reference_html":"Structure and Mechanisms of NT5C2 Mutations Driving Thiopurine Resistance in Relapsed Lymphoblastic Leukemia. <i> Dieck CL, Tzoneva G, Forouhar F, Carpenter Z, Ambesi-Impiombato A, Sánchez-Martín M, Kirschner-Schwabe R, Lew S, Seetharaman J, Tong L, Ferrando AA. </i> Cancer Cell, 2018","date":"2022-12-15T14:54:39.138Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6DDL"},{"db":"PDB","id":"6DE1"},{"db":"PDB","id":"6DD3"},{"db":"PDB","id":"6DE0"},{"db":"PDB","id":"6DDY"},{"db":"PDB","id":"6DDO"},{"db":"PDB","id":"6DDC"},{"db":"PDB","id":"6DDB"},{"db":"PDB","id":"6DDQ"},{"db":"PDB","id":"6DDK"}],"region_id":"DP03885r006","statement":[{"text":"The N- and C-termini amino acids (S4 and S488), and the termini amino acids (L402 and R421) of the disordered region in the arm segment are also labeled.","type":"Figure"},{"text":"Specifically, the loop at the tip of the helical arm segment of NT5C2 establishes intimate contacts with the other monomer in the basal structure, yet these contacts are lost upon activation with the helical arm pivoting away from the other monomer and the tip region becoming disordered upon allosteric activation supporting a role for this element in NT5C2 regulation (Figure 2A–F).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-16T12:59:55.345Z"}},{"start":1,"end":23,"reference_id":"29990496","reference_source":"pmid","reference_html":"Structure and Mechanisms of NT5C2 Mutations Driving Thiopurine Resistance in Relapsed Lymphoblastic Leukemia. <i> Dieck CL, Tzoneva G, Forouhar F, Carpenter Z, Ambesi-Impiombato A, Sánchez-Martín M, Kirschner-Schwabe R, Lew S, Seetharaman J, Tong L, Ferrando AA. </i> Cancer Cell, 2018","date":"2022-12-20T14:01:21.878Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6DD3"},{"db":"PDB","id":"6DDX"},{"db":"PDB","id":"6DE1"},{"db":"PDB","id":"6DDZ"},{"db":"PDB","id":"6DE3"},{"db":"PDB","id":"6DDY"},{"db":"PDB","id":"6DDB"},{"db":"PDB","id":"6DDH"},{"db":"PDB","id":"6DE2"},{"db":"PDB","id":"6DDY"},{"db":"PDB","id":"6DE0"},{"db":"PDB","id":"6DDQ"},{"db":"PDB","id":"6DDK"},{"db":"PDB","id":"6DDC"},{"db":"PDB","id":"6DDO"},{"db":"PDB","id":"6DDL"}],"region_id":"DP03885r007","statement":[{"text":"As a result, NT5C2 must undergo structural rearrangement in order to switch to an active configuration. This transition to an active state, involves the organization of the N-terminal segment of the protein in a helical configuration.","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-20T14:51:00.912Z"}},{"start":489,"end":510,"reference_id":"29990496","reference_source":"pmid","reference_html":"Structure and Mechanisms of NT5C2 Mutations Driving Thiopurine Resistance in Relapsed Lymphoblastic Leukemia. <i> Dieck CL, Tzoneva G, Forouhar F, Carpenter Z, Ambesi-Impiombato A, Sánchez-Martín M, Kirschner-Schwabe R, Lew S, Seetharaman J, Tong L, Ferrando AA. </i> Cancer Cell, 2018","date":"2022-12-20T14:01:57.696Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6DE2"},{"db":"PDB","id":"6DE3"},{"db":"PDB","id":"6DE1"},{"db":"PDB","id":"6DDO"},{"db":"PDB","id":"6DDQ"},{"db":"PDB","id":"6DDK"}],"region_id":"DP03885r008","statement":[{"text":"In the absence of an allosteric regulator, the C-terminal segment of one NT5C2 subunit (residues 479–510 and 537–553) folds over the base of the arm segment of the neighboring protomer so that the acidic C-terminal tail introduces itself into the positively charged inter-subunit pocket promoting a compact dimer and a tightly-associated NT5C2 tetramer conformation (Figure 6C, 6D and Figure S5A). Of note, this tightly closed conformation is released in the allosterically activated structure of NT5C2 in which the C-terminal is no longer visible at the dimer interface and is also displaced from the surface of the neighboring subunit by the N-terminal segment (Figure S5B).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-20T14:51:11.117Z"}},{"start":537,"end":553,"reference_id":"29990496","reference_source":"pmid","reference_html":"Structure and Mechanisms of NT5C2 Mutations Driving Thiopurine Resistance in Relapsed Lymphoblastic Leukemia. <i> Dieck CL, Tzoneva G, Forouhar F, Carpenter Z, Ambesi-Impiombato A, Sánchez-Martín M, Kirschner-Schwabe R, Lew S, Seetharaman J, Tong L, Ferrando AA. </i> Cancer Cell, 2018","date":"2022-12-20T14:02:21.192Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6DE2"},{"db":"PDB","id":"6DE3"},{"db":"PDB","id":"6DE1"},{"db":"PDB","id":"6DDO"},{"db":"PDB","id":"6DDQ"},{"db":"PDB","id":"6DDK"}],"region_id":"DP03885r009","statement":[{"text":"In the absence of an allosteric regulator, the C-terminal segment of one NT5C2 subunit (residues 479–510 and 537–553) folds over the base of the arm segment of the neighboring protomer so that the acidic C-terminal tail introduces itself into the positively charged inter-subunit pocket promoting a compact dimer and a tightly-associated NT5C2 tetramer conformation (Figure 6C, 6D and Figure S5A). Of note, this tightly closed conformation is released in the allosterically activated structure of NT5C2 in which the C-terminal is no longer visible at the dimer interface and is also displaced from the surface of the neighboring subunit by the N-terminal segment (Figure S5B).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-20T14:51:15.363Z"}}],"regions_counter":9,"released":"2023_06","sequence":"MSTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVYKSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLVCAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTSCETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMKEVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGTVLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKSKKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQRRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAAHVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLAPQEITHCHDEDDDEEEEEEEE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Cancer-related proteins"],"alphafold_very_low_content":0.0213903743315508,"disorder_content":0.20855614973262032,"disprot_consensus":{"full":[{"start":1,"end":23,"type":"T"},{"start":399,"end":402,"type":"D"},{"start":403,"end":419,"type":"T"},{"start":489,"end":510,"type":"T"},{"start":511,"end":536,"type":"D"},{"start":537,"end":553,"type":"T"},{"start":554,"end":561,"type":"D"}],"Structural state":[{"start":1,"end":23,"type":"D"},{"start":399,"end":419,"type":"D"},{"start":489,"end":561,"type":"D"}],"Structural transition":[{"start":1,"end":23,"type":"T"},{"start":403,"end":419,"type":"T"},{"start":489,"end":510,"type":"T"},{"start":537,"end":553,"type":"T"}]}},{"disprot_id":"DP03886","acc":"Q4Q159","creator":"jssuarez","date":"2022-10-28T14:03:04.262Z","features":{"pfam":[{"id":"PF00291","name":"Pyridoxal-phosphate dependent enzyme","start":15,"end":301}],"gene3D":[]},"genes":[{"orfNames":[{"value":"LMJF_36_3590","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAJ09322.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAJ09322.1"}}]}]}],"length":333,"name":"Cysteine synthase","ncbi_taxon_id":5664,"organism":"Leishmania major","regions":[{"start":214,"end":240,"reference_id":"22750854","reference_source":"pmid","reference_html":"Structure of Leishmania major cysteine synthase. <i> Fyfe PK, Westrop GD, Ramos T, Müller S, Coombs GH, Hunter WN. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012","date":"2022-10-28T14:06:58.807Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"4AIR"}],"region_id":"DP03886r001","statement":[{"text":"A surface loop from residues 214 to 241 is disordered and is therefore missing from the model. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T19:44:42.730Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MAAPFDKSRNVAQSIDQLIGQTPALYLNKLNNTKAKVVLKMECENPMASVKDRLGFAIYDKAEKEGKLIPGKSVVVESSSGNTGVSLAHLGAIRGYKVIITMPESMSLERRCLLRIFGAEVILTPAALGMKGAVTMAKKIVTANPNAVLADQFATKYNALIHEETTGPEIWEQTNHNVDCFIAGVGTGGTLTGVARALKKMGSHARIVAVEPMESPVLSGGKPGAHKIQGIGPGFVPDVLDRSLIDEVFCVAGDDAIETALKLTRSDGVFCGFSGGANVYAALKIAERPEMEGKTIVTIIPSFGERYLSTALYRSVRDEVSSLPVVDASELQD","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"alphafold_very_low_content":0.003003003003003003,"disorder_content":0.08108108108108109,"disprot_consensus":{"full":[{"start":214,"end":240,"type":"D"}],"Structural state":[{"start":214,"end":240,"type":"D"}]}},{"disprot_id":"DP03887","acc":"Q01782","creator":"jssuarez","date":"2022-10-28T14:16:26.883Z","features":{"pfam":[{"id":"PF00106","name":"short chain dehydrogenase","start":8,"end":69},{"id":"PF13561","name":"Enoyl-(Acyl carrier protein) reductase","start":84,"end":284}],"gene3D":[]},"genes":[{"name":{"value":"PTR1"},"synonyms":[{"value":"HMTXR"}],"orfNames":[{"value":"L1063.01"},{"value":"LmjF23.0270"},{"value":"LmjF_23_0270"}]}],"length":288,"name":"Pteridine reductase 1","ncbi_taxon_id":5664,"organism":"Leishmania major","regions":[{"start":120,"end":132,"reference_id":"11373620","reference_source":"pmid","reference_html":"Pteridine reductase mechanism correlates pterin metabolism with drug resistance in trypanosomatid parasites. <i> Gourley DG, Schüttelkopf AW, Leonard GA, Luba J, Hardy LW, Beverley SM, Hunter WN. </i> Nat Struct Biol, 2001","date":"2022-11-02T09:42:09.181Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"1E7W"}],"region_id":"DP03887r001","statement":[{"text":"Missing electron density corresponding to a loop region.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-05T15:42:46.455Z"}},{"start":121,"end":133,"reference_id":"18245389","reference_source":"pmid","reference_html":"Discovery of potent pteridine reductase inhibitors to guide antiparasite drug development. <i> Cavazzuti A, Paglietti G, Hunter WN, Gamarro F, Piras S, Loriga M, Allecca S, Corona P, McLuskey K, Tulloch L, Gibellini F, Ferrari S, Costi MP. </i> Proc Natl Acad Sci U S A, 2008","date":"2022-11-02T09:42:34.198Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"2QHX"}],"region_id":"DP03887r002","statement":[{"text":"Missing electron density corresponding to a loop region.","type":"Curator statement"},{"text":"We assume that a combination of static and conformational disorder is present and that the R-work and R-free values likely contain a significant contribution from the density that we have been unable to model.","type":"Supplementary material"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-05T15:42:45.269Z"}}],"regions_counter":2,"released":"2022_12","sequence":"MTAPTVPVALVTGAAKRLGRSIAEGLHAEGYAVCLHYHRSAAEANALSATLNARRPNSAITVQADLSNVATAPVSGADGSAPVTLFTRCAELVAACYTHWGRCDVLVNNASSFYPTPLLRNDEDGHEPCVGDREAMETATADLFGSNAIAPYFLIKAFAHRFAGTPAKHRGTNYSIINMVDAMTNQPLLGYTIYTMAKGALEGLTRSAALELAPLQIRVNGVGPGLSVLVDDMPPAVWEGHRSKVPLYQRDSSAAEVSDVVIFLCSSKAKYITGTCVKVDGGYSLTRA","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"alphafold_very_low_content":0.03819444444444445,"disorder_content":0.04861111111111111,"disprot_consensus":{"full":[{"start":120,"end":133,"type":"D"}],"Structural state":[{"start":120,"end":133,"type":"D"}]}},{"disprot_id":"DP03888","acc":"P61956","creator":"jssuarez","date":"2022-10-31T11:48:16.047Z","features":{"pfam":[{"id":"PF11976","name":"Ubiquitin-2 like Rad60 SUMO-like","start":18,"end":86}],"gene3D":[]},"genes":[{"name":{"value":"SUMO2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11125","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11125"}}]},"synonyms":[{"value":"SMT3B","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10692421","url":"http://www.ncbi.nlm.nih.gov/pubmed/10692421","alternativeUrl":"https://europepmc.org/abstract/MED/10692421"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11125","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11125"}}]},{"value":"SMT3H2"}]}],"length":95,"name":"Small ubiquitin-related modifier 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":14,"reference_id":"24564702","reference_source":"pmid","reference_html":"N-terminal protein tails act as aggregation protective entropic bristles: the SUMO case. <i> Graña-Montes R, Marinelli P, Reverter D, Ventura S. </i> Biomacromolecules, 2014","date":"2022-10-31T11:50:12.864Z","curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03888r001","statement":[{"text":" As expected, SUMO2 elutes first than ΔNt-SUMO2 (Figure 4). However, the calculated difference in apparent molecular weight between the two proteins is ∼10 kDa, which is much higher than the one expected for a tail of only 14 residues (∼1.5 kDa). This suggests that the large difference in hydrodynamic volume between the two proteins can be attributed to the disordered nature of SUMO2 N-terminal extension.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-11-01T19:56:13.859Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MADEKPKEGVKTENNDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYCERQGLSMRQIRFRFDGQPINETDTPAQLEMEDEDTIDVFQQQTGGVY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.05263157894736842,"disorder_content":0.14736842105263157,"disprot_consensus":{"full":[{"start":1,"end":14,"type":"D"}],"Structural state":[{"start":1,"end":14,"type":"D"}]}},{"disprot_id":"DP03889","acc":"Q16625","creator":"fkordevani","date":"2022-11-02T10:50:41.843Z","features":{"pfam":[{"id":"PF01284","name":"Membrane-associating domain","start":57,"end":263},{"id":"PF07303","name":"Occludin homology domain","start":420,"end":519}],"gene3D":[]},"genes":[{"name":{"value":"OCLN"}}],"length":522,"name":"Occludin","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":383,"end":415,"reference_id":"16081103","reference_source":"pmid","reference_html":"Structure of the conserved cytoplasmic C-terminal domain of occludin: identification of the ZO-1 binding surface. <i> Li Y, Fanning AS, Anderson JM, Lavie A. </i> J Mol Biol, 2005","date":"2022-11-02T10:54:30.833Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1XAW"}],"region_id":"DP03889r001","statement":[{"text":"Crystals grown using an occludin fragment that contains the C-terminal ∼140 amino acid residues that traditionally have defined this domain (383–522) reveal that only the last 106 residues form an ordered structure. The 34 N-terminal residues had no observable electron density, implying a disordered region. ","type":"Introduction"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-12T17:11:43.212Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MSSRPLESPPPYRPDEFKPNHYAPSNDIYGGEMHVRPMLSQPAYSFYPEDEILHFYKWTSPPGVIRILSMLIIVMCIAIFACVASTLAWDRGYGTSLLGGSVGYPYGGSGFGSYGSGYGYGYGYGYGYGGYTDPRAAKGFMLAMAAFCFIAALVIFVTSVIRSEMSRTRRYYLSVIIVSAILGIMVFIATIVYIMGVNPTAQSSGSLYGSQIYALCNQFYTPAATGLYVDQYLYHYCVVDPQEAIAIVLGFMIIVAFALIIFFAVKTRRKMDRYDKSNILWDKEHIYDEQPPNVEEWVKNVSAGTQDVPSPPSDYVERVDSPMAYSSNGKVNDKRFYPESSYKSTPVPEVVQELPLTSPVDDFRQPRYSSGGNFETPSKRAPAKGRAGRSKRTEQDHYETDYTTGGESCDELEEDWIREYPPITSDQQRQLYKRNFDTGLQEYKSLQSELDEINKELSRLDKELDDYREESEEYMAAADEYNRLKQVKGSADYKSKKNHCKQLKSKLSHIKKMVGDYDRQKT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.3716475095785441,"disorder_content":0.06321839080459771,"disprot_consensus":{"full":[{"start":383,"end":415,"type":"D"}],"Structural state":[{"start":383,"end":415,"type":"D"}]}},{"disprot_id":"DP03890","acc":"Q01968","creator":"fkordevani","date":"2022-11-02T10:58:19.426Z","features":{"pfam":[{"id":"PF00620","name":"RhoGAP domain","start":735,"end":872},{"id":"PF16726","name":"Inositol polyphosphate 5-phosphatase clathrin binding domain","start":18,"end":117},{"id":"PF21310","name":"Inositol polyphosphate 5-phosphatase OCRL-like, ASH domain","start":567,"end":675},{"id":"PF22669","name":"Endonuclease/Exonuclease/phosphatase family 2","start":245,"end":529}],"gene3D":[]},"genes":[{"name":{"value":"OCRL","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:8108","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8108"}}]},"synonyms":[{"value":"OCRL1","evidences":[{"code":"ECO:0000303","source":{"name":"Citation","id":"Ref.2","url":"https://www.uniprot.org/uniprot/null#ref2"}}]}]}],"length":901,"name":"Inositol polyphosphate 5-phosphatase OCRL","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":697,"end":729,"reference_id":"21666675","reference_source":"pmid","reference_html":"Recognition of the F&H motif by the Lowe syndrome protein OCRL. <i> Pirruccello M, Swan LE, Folta-Stogniew E, De Camilli P. </i> Nat Struct Mol Biol, 2011","date":"2022-12-15T15:00:27.151Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3QIS"}],"region_id":"DP03890r002","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-16T13:14:01.020Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MEPPLPVGAQPLATVEGMEMKGPLREPCALTLAQRNGQYELIIQLHEKEQHVQDIIPINSHFRCVQEAEETLLIDIASNSGCKIRVQGDWIRERRFEIPDEEHCLKFLSAVLAAQKAQSQLLVPEQKDSSSWYQKLDTKDKPSVFSGLLGFEDNFSSMNLDKKINSQNQPTGIHREPPPPPFSVNKMLPREKEASNKEQPKVTNTMRKLFVPNTQSGQREGLIKHILAKREKEYVNIQTFRFFVGTWNVNGQSPDSGLEPWLNCDPNPPDIYCIGFQELDLSTEAFFYFESVKEQEWSMAVERGLHSKAKYKKVQLVRLVGMMLLIFARKDQCRYIRDIATETVGTGIMGKMGNKGGVAVRFVFHNTTFCIVNSHLAAHVEDFERRNQDYKDICARMSFVVPNQTLPQLNIMKHEVVIWLGDLNYRLCMPDANEVKSLINKKDLQRLLKFDQLNIQRTQKKAFVDFNEGEIKFIPTYKYDSKTDRWDSSGKCRVPAWCDRILWRGTNVNQLNYRSHMELKTSDHKPVSALFHIGVKVVDERRYRKVFEDSVRIMDRMENDFLPSLELSRREFVFENVKFRQLQKEKFQISNNGQVPCHFSFIPKLNDSQYCKPWLRAEPFEGYLEPNETVDISLDVYVSKDSVTILNSGEDKIEDILVLHLDRGKDYFLTISGNYLPSCFGTSLEALCRMKRPIREVPVTKLIDLEEDSFLEKEKSLLQMVPLDEGASERPLQVPKEIWLLVDHLFKYACHQEDLFQTPGMQEELQQIIDCLDTSIPETIPGSNHSVAEALLIFLEALPEPVICYELYQRCLDSAYDPRICRQVISQLPRCHRNVFRYLMAFLRELLKFSEYNSVNANMIATLFTSLLLRPPPNLMARQTPSDRQRAIQFLLGFLLGSEED","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.13540510543840178,"disorder_content":0.03662597114317425,"disprot_consensus":{"full":[{"start":697,"end":729,"type":"D"}],"Structural state":[{"start":697,"end":729,"type":"D"}]}},{"disprot_id":"DP03891","acc":"O15294","creator":"fkordevani","date":"2022-11-02T11:03:06.512Z","features":{"pfam":[{"id":"PF00515","name":"Tetratricopeptide repeat","start":191,"end":224},{"id":"PF00515","name":"Tetratricopeptide repeat","start":259,"end":292},{"id":"PF13181","name":"Tetratricopeptide repeat","start":163,"end":189},{"id":"PF13181","name":"Tetratricopeptide repeat","start":226,"end":258},{"id":"PF13414","name":"TPR repeat","start":96,"end":136},{"id":"PF13414","name":"TPR repeat","start":373,"end":408},{"id":"PF13414","name":"TPR repeat","start":438,"end":471},{"id":"PF13424","name":"Tetratricopeptide repeat","start":295,"end":358},{"id":"PF13844","name":"Glycosyl transferase family 41","start":476,"end":1016}],"gene3D":[]},"genes":[{"name":{"value":"OGT"}}],"length":1046,"name":"UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":757,"end":771,"reference_id":"30285435","reference_source":"pmid","reference_html":"Structure-Based Evolution of Low Nanomolar O-GlcNAc Transferase Inhibitors. <i> Martin SES, Tan ZW, Itkonen HM, Duveau DY, Paulo JA, Janetzko J, Boutz PL, Törk L, Moss FA, Thomas CJ, Gygi SP, Lazarus MB, Walker S. </i> J Am Chem Soc, 2018","date":"2023-02-13T09:58:55.550Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6MA1"},{"db":"PDB","id":"6MA2"},{"db":"PDB","id":"6MA3"},{"db":"PDB","id":"6MA4"},{"db":"PDB","id":"6MA5"}],"region_id":"DP03891r005","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:134820950"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P51610"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:134820951"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:134820952"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:134820953"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:134820954"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-13T16:11:21.229Z"}}],"regions_counter":5,"released":"2023_06","sequence":"MASSVGNVADSTEPTKRMLSFQGLAELAHREYQAGDFEAAERHCMQLWRQEPDNTGVLLLLSSIHFQCRRLDRSAHFSTLAIKQNPLLAEAYSNLGNVYKERGQLQEAIEHYRHALRLKPDFIDGYINLAAALVAAGDMEGAVQAYVSALQYNPDLYCVRSDLGNLLKALGRLEEAKACYLKAIETQPNFAVAWSNLGCVFNAQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARIFDRAVAAYLRALSLSPNHAVVHGNLACVYYEQGLIDLAIDTYRRAIELQPHFPDAYCNLANALKEKGSVAEAEDCYNTALRLCPTHADSLNNLANIKREQGNIEEAVRLYRKALEVFPEFAAAHSNLASVLQQQGKLQEALMHYKEAIRISPTFADAYSNMGNTLKEMQDVQGALQCYTRAIQINPAFADAHSNLASIHKDSGNIPEAIASYRTALKLKPDFPDAYCNLAHCLQIVCDWTDYDERMKKLVSIVADQLEKNRLPSVHPHHSMLYPLSHGFRKAIAERHGNLCLDKINVLHKPPYEHPKDLKLSDGRLRVGYVSSDFGNHPTSHLMQSIPGMHNPDKFEVFCYALSPDDGTNFRVKVMAEANHFIDLSQIPCNGKAADRIHQDGIHILVNMNGYTKGARNELFALRPAPIQAMWLGYPGTSGALFMDYIITDQETSPAEVAEQYSEKLAYMPHTFFIGDHANMFPHLKKKAVIDFKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVKMKCPDGGDNADSSNTALNMPVIPMNTIAEAVIEMINRGQIQITINGFSISNGLATTQINNKAATGEEVPRTIIVTTRSQYGLPEDAIVYCNFNQLYKIDPSTLQMWANILKRVPNSVLWLLRFPAVGEPNIQQYAQNMGLPQNRIIFSPVAPKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAASQLTCLGCLELIAKNRQEYEDIAVKLGTDLEYLKKVRGKVWKQRISSPLFNTKQYTMELERLYLQMWEHYAAGNKPDHMIKPVEVTESA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.03154875717017208,"disorder_content":0.014340344168260038,"disprot_consensus":{"full":[{"start":757,"end":771,"type":"D"}],"Structural state":[{"start":757,"end":771,"type":"D"}]}},{"disprot_id":"DP03892","acc":"P00439","creator":"fkordevani","date":"2022-11-02T11:13:25.670Z","features":{"pfam":[{"id":"PF00351","name":"Biopterin-dependent aromatic amino acid hydroxylase","start":119,"end":449},{"id":"PF01842","name":"ACT domain","start":36,"end":98}],"gene3D":[]},"genes":[{"name":{"value":"PAH"}}],"length":452,"name":"Phenylalanine-4-hydroxylase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":20,"reference_id":"31118288","reference_source":"pmid","reference_html":"Structure of full-length human phenylalanine hydroxylase in complex with tetrahydrobiopterin. <i> Flydal MI, Alcorlo-Pagés M, Johannessen FG, Martínez-Caballero S, Skjærven L, Fernandez-Leiro R, Martinez A, Hermoso JA. </i> Proc Natl Acad Sci U S A, 2019","date":"2023-05-04T08:18:29.160Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6HYC"}],"region_id":"DP03892r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:135398654"}],"statement":[{"text":"Mammalian PAH is tetrameric, and its 52 kDa subunits are composed of a regulatory domain (RD, residues 1–110) with an unstructured N-terminal tail (N term; residues 1–29), a catalytic domain (CD, residues 111–410), and an oligomerization domain (OD, residues 411–452) responsible for dimerization and subsequent tetramerization (SI Appendix, Fig. S1).","type":"Abstract"},{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T13:19:25.083Z"}}],"regions_counter":3,"released":"2023_06","sequence":"MSTAVLENPGLGRKLSDFGQETSYIEDNCNQNGAISLIFSLKEEVGALAKVLRLFEENDVNLTHIESRPSRLKKDEYEFFTHLDKRSLPALTNIIKILRHDIGATVHELSRDKKKDTVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYCLSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVLDNTQQLKILADSINSEIGILCSALQKIK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.0420353982300885,"disorder_content":0.04424778761061947,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"D"}],"Structural state":[{"start":1,"end":20,"type":"D"}]}},{"disprot_id":"DP03894","acc":"O75151","creator":"fkordevani","date":"2022-11-02T13:34:37.792Z","features":{"pfam":[{"id":"PF00628","name":"PHD-finger","start":8,"end":53},{"id":"PF02373","name":"JmjC domain, hydroxylase","start":236,"end":336},{"id":"PF17811","name":"Jumonji helical domain","start":340,"end":443}],"gene3D":[]},"genes":[{"name":{"value":"PHF2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:8920","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8920"}}]},"synonyms":[{"value":"CENP-35","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"20813266","url":"http://www.ncbi.nlm.nih.gov/pubmed/20813266","alternativeUrl":"https://europepmc.org/abstract/MED/20813266"}}]},{"value":"KIAA0662"}]}],"length":1096,"name":"Lysine-specific demethylase PHF2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":60,"end":79,"reference_id":"21167174","reference_source":"pmid","reference_html":"Structural basis for human PHF2 Jumonji domain interaction with metal ions. <i> Horton JR, Upadhyay AK, Hashimoto H, Zhang X, Cheng X. </i> J Mol Biol, 2011","date":"2022-11-02T13:36:37.176Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3PU3"},{"db":"PDB","id":"3PUA"},{"db":"PDB","id":"3PTR"},{"db":"PDB","id":"3PU8"},{"db":"PDB","id":"3PUS"}],"region_id":"DP03894r001","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-13T15:46:35.690Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MATVPVYCVCRLPYDVTRFMIECDACKDWFHGSCVGVEEEEAPDIDIYHCPNCEKTHGKSTLKKKRTWHKHGPGQAPDVKPVQNGSQLFIKELRSRTFPSAEDVVARVPGSQLTLGYMEEHGFTEPILVPKKDGLGLAVPAPTFYVSDVENYVGPERSVDVTDVTKQKDCKMKLKEFVDYYYSTNRKRVLNVTNLEFSDTRMSSFVEPPDIVKKLSWVENYWPDDALLAKPKVTKYCLICVKDSYTDFHIDSGGASAWYHVLKGEKTFYLIRPASANISLYERWRSASNHSEMFFADQVDKCYKCIVKQGQTLFIPSGWIYATLTPVDCLAFAGHFLHSLSVEMQMRAYEVERRLKLGSLTQFPNFETACWYMGKHLLEAFKGSHKSGKQLPPHLVQGAKILNGAFRSWTKKQALAEHEDELPEHFKPSQLIKDLAKEIRLSENASKAVRPEVNTVASSDEVCDGDREKEEPPSPIEATPPQSLLEKVSKKKTPKTVKMPKPSKIPKPPKPPKPPRPPKTLKLKDGGKKKGKKSRESASPTIPNLDLLEAHTKEALTKMEPPKKGKATKSVLSVPNKDVVHMQNDVERLEIREQTKSKSEAKWKYKNSKPDSLLKMEEEQKLEKSPLAGNKDNKFSFSFSNKKLLGSKALRPPTSPGVFGALQNFKEDKPKPVRDEYEYVSDDGELKIDEFPIRRKKNAPKRDLSFLLDKKAVLPTPVTKPKLDSAAYKSDDSSDEGSLHIDTDTKPGRNARVKKESGSSAAGILDLLQASEEVGALEYNPSSQPPASPSTQEAIQGMLSMANLQASDSCLQTTWGAGQAKGSSLAAHGARKNGGGSGKSAGKRLLKRAAKNSVDLDDYEEEQDHLDACFKDSDYVYPSLESDEDNPIFKSRSKKRKGSDDAPYSPTARVGPSVPRQDRPVREGTRVASIETGLAAAAAKLSQQEEQKSKKKKSAKRKLTPNTTSPSTSTSISAGTTSTSTTPASTTPASTTPASTSTASSQASQEGSSPEPPPESHSSSLADHEYTAAGTFTGAQAGRTSQPMAPGVFLTQRRPSASSPNNNTAAKGKRTKKGMATAKQRLGKILKIHRNGKLLL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.5228102189781022,"disorder_content":0.01824817518248175,"disprot_consensus":{"full":[{"start":60,"end":79,"type":"D"}],"Structural state":[{"start":60,"end":79,"type":"D"}]}},{"disprot_id":"DP03896","acc":"Q13635","creator":"fkordevani","date":"2022-11-02T14:15:51.421Z","features":{"pfam":[{"id":"PF12349","name":"Sterol-sensing domain of SREBP cleavage-activation","start":464,"end":615},{"id":"PF27572","name":"Transformer protein 2 N-terminal domain","start":156,"end":297}],"gene3D":[]},"genes":[{"name":{"value":"PTCH1"},"synonyms":[{"value":"PTCH"}]}],"length":1447,"name":"Protein patched homolog 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":75,"reference_id":"29995851","reference_source":"pmid","reference_html":"Structures of human Patched and its complex with native palmitoylated sonic hedgehog. <i> Qi X, Schmiege P, Coutavas E, Wang J, Li X. </i> Nature, 2018","date":"2022-12-15T15:05:59.759Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6OEV"},{"db":"PDB","id":"6OEU"}],"region_id":"DP03896r001","statement":[{"text":"The density of residues 1–75 (N-terminal domain), 608–618 and 721–729 (TM6-TM7 linker), 888–901 (in ECD-II) and 1177–1188 (C-terminus) is not resolved nor built.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-08T17:41:53.495Z"}},{"start":608,"end":730,"reference_id":"29995851","reference_source":"pmid","reference_html":"Structures of human Patched and its complex with native palmitoylated sonic hedgehog. <i> Qi X, Schmiege P, Coutavas E, Wang J, Li X. </i> Nature, 2018","date":"2022-12-15T15:06:20.072Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6OEV"},{"db":"PDB","id":"6OEU"}],"region_id":"DP03896r002","statement":[{"text":"The density of residues 1–75 (N-terminal domain), 608–618 and 721–729 (TM6-TM7 linker), 888–901 (in ECD-II) and 1177–1188 (C-terminus) is not resolved nor built.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-08T17:41:56.732Z"}},{"start":888,"end":901,"reference_id":"29995851","reference_source":"pmid","reference_html":"Structures of human Patched and its complex with native palmitoylated sonic hedgehog. <i> Qi X, Schmiege P, Coutavas E, Wang J, Li X. </i> Nature, 2018","date":"2022-12-15T15:06:36.281Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6OEV"},{"db":"PDB","id":"6OEU"}],"region_id":"DP03896r003","statement":[{"text":"The density of residues 1–75 (N-terminal domain), 608–618 and 721–729 (TM6-TM7 linker), 888–901 (in ECD-II) and 1177–1188 (C-terminus) is not resolved nor built.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-08T17:41:51.849Z"}},{"start":1177,"end":1447,"reference_id":"29995851","reference_source":"pmid","reference_html":"Structures of human Patched and its complex with native palmitoylated sonic hedgehog. <i> Qi X, Schmiege P, Coutavas E, Wang J, Li X. </i> Nature, 2018","date":"2022-12-15T15:07:02.788Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6OEV"},{"db":"PDB","id":"6OEU"}],"region_id":"DP03896r004","statement":[{"text":"The density of residues 1–75 (N-terminal domain), 608–618 and 721–729 (TM6-TM7 linker), 888–901 (in ECD-II) and 1177–1188 (C-terminus) is not resolved nor built.","type":"Results"},{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.\"","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-08T17:41:51.556Z"}},{"start":614,"end":728,"reference_id":"31555730","reference_source":"pmid","reference_html":"Structural basis of sterol recognition by human hedgehog receptor PTCH1. <i> Qi C, Di Minin G, Vercellino I, Wutz A, Korkhov VM. </i> Sci Adv, 2019","date":"2023-05-04T08:49:47.912Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Tyr645Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":" Thus, we designed the PTCH1 expression construct to maximize the protein yield by removing the two PPXY motifs; the C-terminally truncated version of the protein, PTCH1-C (residues 1 to 1188), and the construct PTCH1Δ (comprising the residues 1 to 1188, with a mutation Y645A) were generated by polymerase chain reaction (PCR)."}]},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"The synthetic DNA fragment (Genewiz) encoding the human wild-type full-length PTCH1 protein (UniProt ID: Q13635) was cloned into pcDNA3.1 vector modified to contain a C-terminal green fluorescent protein (GFP)–10xHis tag fusion protein."}]}],"cross_refs":[{"db":"PDB","id":"6RMG"},{"db":"EMDB","id":"EMD-4936"}],"region_id":"DP03896r008","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15465"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:65082"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"}],"statement":[{"text":"The atomic model of PTCH1Δ-ShhNC24II covers the sequence of PTCH1 residues D46-P1186, with an unresolved loop region comprising residues F614-T728.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T13:27:20.619Z"}}],"regions_counter":8,"released":"2023_06","sequence":"MASAGNAAEPQDRGGGGSGCIGAPGRPAGGGRRRRTGGLRRAAAPDRDYLHRPSYCDAAFALEQISKGKATGRKAPLWLRAKFQRLLFKLGCYIQKNCGKFLVVGLLIFGAFAVGLKAANLETNVEELWVEVGGRVSRELNYTRQKIGEEAMFNPQLMIQTPKEEGANVLTTEALLQHLDSALQASRVHVYMYNRQWKLEHLCYKSGELITETGYMDQIIEYLYPCLIITPLDCFWEGAKLQSGTAYLLGKPPLRWTNFDPLEFLEELKKINYQVDSWEEMLNKAEVGHGYMDRPCLNPADPDCPATAPNKNSTKPLDMALVLNGGCHGLSRKYMHWQEELIVGGTVKNSTGKLVSAHALQTMFQLMTPKQMYEHFKGYEYVSHINWNEDKAAAILEAWQRTYVEVVHQSVAQNSTQKVLSFTTTTLDDILKSFSDVSVIRVASGYLLMLAYACLTMLRWDCSKSQGAVGLAGVLLVALSVAAGLGLCSLIGISFNAATTQVLPFLALGVGVDDVFLLAHAFSETGQNKRIPFEDRTGECLKRTGASVALTSISNVTAFFMAALIPIPALRAFSLQAAVVVVFNFAMVLLIFPAILSMDLYRREDRRLDIFCCFTSPCVSRVIQVEPQAYTDTHDNTRYSPPPPYSSHSFAHETQITMQSTVQLRTEYDPHTHVYYTTAEPRSEISVQPVTVTQDTLSCQSPESTSSTRDLLSQFSDSSLHCLEPPCTKWTLSSFAEKHYAPFLLKPKAKVVVIFLFLGLLGVSLYGTTRVRDGLDLTDIVPRETREYDFIAAQFKYFSFYNMYIVTQKADYPNIQHLLYDLHRSFSNVKYVMLEENKQLPKMWLHYFRDWLQGLQDAFDSDWETGKIMPNNYKNGSDDGVLAYKLLVQTGSRDKPIDISQLTKQRLVDADGIINPSAFYIYLTAWVSNDPVAYAASQANIRPHRPEWVHDKADYMPETRLRIPAAEPIEYAQFPFYLNGLRDTSDFVEAIEKVRTICSNYTSLGLSSYPNGYPFLFWEQYIGLRHWLLLFISVVLACTFLVCAVFLLNPWTAGIIVMVLALMTVELFGMMGLIGIKLSAVPVVILIASVGIGVEFTVHVALAFLTAIGDKNRRAVLALEHMFAPVLDGAVSTLLGVLMLAGSEFDFIVRYFFAVLAILTILGVLNGLVLLPVLLSFFGPYPEVSPANGLNRLPTPSPEPPPSVVRFAMPPGHTHSGSDSSDSEYSSQTTVSGLSEELRHYEAQQGAGGPAHQVIVEATENPVFAHSTVVHPESRHHPPSNPRQQPHLDSGSLPPGRQGQQPRRDPPREGLWPPPYRPRRDAFEISTEGHSGPSNRARWGPRGARSHNPRNPASTAMGSSVPGYCQPITTVTASASVTVAVHPPPVPGPGRNPRGGLCPGYPETDHGLFEDPHVPFHVRCERRDSKVEVIELQDVECEERPRGSSSN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Cancer-related proteins"],"alphafold_very_low_content":0.27021423635107117,"disorder_content":0.3337940566689703,"disprot_consensus":{"full":[{"start":1,"end":75,"type":"D"},{"start":608,"end":730,"type":"D"},{"start":888,"end":901,"type":"D"},{"start":1177,"end":1447,"type":"D"}],"Structural state":[{"start":1,"end":75,"type":"D"},{"start":608,"end":730,"type":"D"},{"start":888,"end":901,"type":"D"},{"start":1177,"end":1447,"type":"D"}]}},{"disprot_id":"DP03897","acc":"Q9UII6","creator":"vacs","date":"2022-11-03T12:07:33.133Z","features":{"pfam":[{"id":"PF00782","name":"Dual specificity phosphatase, catalytic domain","start":53,"end":186}],"gene3D":[]},"genes":[{"name":{"value":"DUSP13"},"synonyms":[{"value":"DUSP13B"},{"value":"TMDP"}]}],"length":198,"name":"Dual specificity protein phosphatase 13 isoform B","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":24,"reference_id":"17044055","reference_source":"pmid","reference_html":"Crystal structure of human TMDP, a testis-specific dual specificity protein phosphatase: implications for substrate specificity. <i> Kim SJ, Jeong DG, Yoon TS, Son JH, Cho SK, Ryu SE, Kim JH. </i> Proteins, 2007","date":"2022-11-03T12:10:43.273Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2GWO"}],"region_id":"DP03897r001","statement":[{"text":"The final model included residues 25−193 of monomer A and monomer B, residues 25–198 of monomer C and monomer D, and 260 water molecules.","type":"Methods"},{"text":"TMDP (25–198) is found to be folded into a compact and globular molecule with approximate dimensions of 40 × 35 × 30 Å3.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-16T14:06:53.540Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MDSLQKQDLRRPKIHGAVQASPYQPPTLASLQRLLWVRQAATLNHIDEVWPSLFLGDAYAARDKSKLIQLGITHVVNAAAGKFQVDTGAKFYRGMSLEYYGIEADDNPFFDLSVYFLPVARYIRAALSVPQGRVLVHCAMGVSRSATLVLAFLMICENMTLVEAIQTVQAHRNICPNSGFLRQLQVLDNRLGRETGRF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.05555555555555555,"disorder_content":0.12121212121212122,"disprot_consensus":{"full":[{"start":1,"end":24,"type":"D"}],"Structural state":[{"start":1,"end":24,"type":"D"}]}},{"disprot_id":"DP03898","acc":"P80041","creator":"vacs","date":"2022-11-07T09:32:40.487Z","features":{"pfam":[{"id":"PF00282","name":"Pyridoxal-dependent decarboxylase conserved domain","start":35,"end":414}],"gene3D":[]},"genes":[{"name":{"value":"DDC"}}],"length":486,"name":"Aromatic-L-amino-acid decarboxylase","ncbi_taxon_id":9823,"organism":"Sus scrofa","regions":[{"start":328,"end":339,"reference_id":"11685243","reference_source":"pmid","reference_html":"Structural insight into Parkinson's disease treatment from drug-inhibited DOPA decarboxylase. <i> Burkhard P, Dominici P, Borri-Voltattorni C, Jansonius JN, Malashkevich VN. </i> Nat Struct Biol, 2001","date":"2022-11-07T09:34:30.324Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1JS3"},{"db":"PDB","id":"1JS6"}],"region_id":"DP03898r001","statement":[{"text":"In the structures of all three crystal forms of DDC, a short stretch of 11 amino acids (residues 328–339) is invisible in the electron density map. These residues belong to a mobile loop that seems to be important for the catalytic mechanism29,30.","type":"Article"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-27T13:33:44.893Z"}},{"start":477,"end":486,"reference_id":"11685243","reference_source":"pmid","reference_html":"Structural insight into Parkinson's disease treatment from drug-inhibited DOPA decarboxylase. <i> Burkhard P, Dominici P, Borri-Voltattorni C, Jansonius JN, Malashkevich VN. </i> Nat Struct Biol, 2001","date":"2022-11-07T09:36:00.321Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1JS3"},{"db":"PDB","id":"1JS6"}],"region_id":"DP03898r002","statement":[{"text":"Residues 477–486 are completely missing in the structure and are presumably disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-27T13:33:46.060Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MNASDFRRRGKEMVDYMADYLEGIEGRQVYPDVQPGYLRPLIPATAPQEPDTFEDILQDVEKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMDWLGKMLQLPEAFLAGEAGEGGGVIQGSASEATLVALLAARTKVVRRLQAASPGLTQGAVLEKLVAYASDQAHSSVERAGLIGGVKLKAIPSDGKFAMRASALQEALERDKAAGLIPFFVVATLGTTSCCSFDNLLEVGPICHEEDIWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFNPHKWLLVNFDCSAMWVKRRTDLTGAFKLDPVYLKHSHQGSGLITDYRHWQLPLGRRFRSLKMWFVFRMYGVKGLQAYIRKHVQLSHEFEAFVLQDPRFEVCAEVTLGLVCFRLKGSDGLNEALLERINSARKIHLVPCRLRGQFVLRFAICSRKVESGHVRLAWEHIRGLAAELLAAEEGKAEIKS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Suina","Suidae","Sus"],"alphafold_very_low_content":0,"disorder_content":0.04526748971193416,"disprot_consensus":{"full":[{"start":328,"end":339,"type":"D"},{"start":477,"end":486,"type":"D"}],"Structural state":[{"start":328,"end":339,"type":"D"},{"start":477,"end":486,"type":"D"}]}},{"disprot_id":"DP03899","acc":"A0A2V2WGW5","creator":"gbalatti","date":"2022-11-09T22:53:32.970Z","features":{"pfam":[{"id":"PF01176","name":"Translation initiation factor 1A / IF-1","start":27,"end":121}],"gene3D":[]},"genes":[{"orfNames":[{"value":"C3747_106g25","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"PWV07053.1","url":"https://www.ebi.ac.uk/ena/browser/view/PWV07053.1"}}]},{"value":"C3747_186g29","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"PWV02863.1","url":"https://www.ebi.ac.uk/ena/browser/view/PWV02863.1"}}]}]}],"length":170,"name":"Putative eukaryotic translation initiation factor 1A","ncbi_taxon_id":5693,"organism":"Trypanosoma cruzi","regions":[{"start":5,"end":23,"reference_id":"33357443","reference_source":"pmid","reference_html":"Structural Differences in Translation Initiation between Pathogenic Trypanosomatids and Their Mammalian Hosts. <i> Bochler A, Querido JB, Prilepskaja T, Soufari H, Simonetti A, Del Cistia ML, Kuhn L, Ribeiro AR, Valášek LS, Hashem Y. </i> Cell Rep, 2020","date":"2022-12-14T14:04:25.870Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"EMDB","id":"11893"},{"db":"PDB","id":"7ASE"}],"region_id":"DP03899r001","statement":[{"text":"Importantly, structures of terminal tails of several essential eIFs in most of the available cryo-EM reconstructions are also lacking, mainly due to their intrinsic flexibility. Among them stand out the terminal tails of the c and d subunits of eIF3, eIF2β, eIF1, and eIF1A, which are all critically involved in scanning and AUG recognition.","type":"Introduction"},{"text":"The Putative eukaryotic translation initiation factor 1A (eIF1A) takes part in the 43S preinitiation complex from Trypanosoma cruzi with the kDDX60 helicase and the  cryo-EM reconstruction corresponds to the entire complex.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":10,"db":"ChEBI","id":"78408","statements":[{"type":"Methods","text":"The parasites were harvested, put in buffer I (20 mM HEPES-KOH pH 7.4, 100 mM KOAc, 4 mM Mg (OAc)2, 2 mM DTT, EDTA free protease inhibitor cocktail and RNasin inhibitor) and subjected to\nlysis by freeze-thaw cycles. After the centrifugation at 12,000 g for 30 min at 4°C, the supernatant was incubated in the presence of 10 mM GMP-PNP (the non-hydrolyzable analog of GTP) for 10 min at 28°C"}],"entry_name":"guanosine 5'-[beta,gamma-imido]triphosphate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":5,"db":"ChEBI","id":"18420","statements":[{"type":"Methods","text":"The fractions containing 48S ICs were collected and pooled according the UV absorbance profile. Buffer was exchanged by precipitating ribosomal\ncomplexes and re-suspending them in sucrose-free buffer II (10 mM HEPES-KOH pH 7.4, 50 mM KOAc, 10 mM NH4Cl, 5 mM Mg(OAc)2, and 2 mM DTT). For the ATP supplemented 43S PIC, the protocol above was repeated for T. cruzi with an addition of 10 mM of ATP."}],"entry_name":"magnesium(2+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-14T15:42:21.140Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MPKNMGKGGKSFKAGNAKGIMQNQKRDIVYADPQEGEEYAQVKKALGNLRLELQLADGSKAIGSIRGAMVRKVWIGQGDVVLVSKRSFNKNDIVDVIHRYNPAEVRALVKDEVIPRDFRSSDERDAKNAHSDYVFVAENDDDGGADDDDQNVLDRNKVVLDDPLATFDEL","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Trypanosoma","Schizotrypanum"],"dataset":["Neglected tropical diseases proteins"],"alphafold_very_low_content":0.12352941176470589,"disorder_content":0.11176470588235295,"disprot_consensus":{"full":[{"start":5,"end":23,"type":"D"}],"Structural state":[{"start":5,"end":23,"type":"D"}]}},{"disprot_id":"DP03900","acc":"P16641","creator":"jnilsson","date":"2022-11-10T18:14:43.449Z","features":{"pfam":[{"id":"PF00217","name":"ATP:guanido phosphotransferase, C-terminal catalytic domain","start":175,"end":381},{"id":"PF00217","name":"ATP:guanido phosphotransferase, C-terminal catalytic domain","start":538,"end":744},{"id":"PF02807","name":"ATP:guanido phosphotransferase, N-terminal domain","start":48,"end":111},{"id":"PF02807","name":"ATP:guanido phosphotransferase, N-terminal domain","start":412,"end":475}],"gene3D":[]},"genes":[{"orfNames":[{"value":"Smp_194770"}]}],"length":746,"name":"Taurocyamine kinase","ncbi_taxon_id":6183,"organism":"Schistosoma mansoni","regions":[{"start":701,"end":710,"reference_id":"25837252","reference_source":"pmid","reference_html":"The substrate-free and -bound crystal structures of the duplicated taurocyamine kinase from the human parasite Schistosoma mansoni. <i> Merceron R, Awama AM, Montserret R, Marcillat O, Gouet P. </i> J Biol Chem, 2015","date":"2022-12-12T13:36:08.316Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006222","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"4WO8"},{"db":"PDB","id":"4WOD"}],"region_id":"DP03900r001","statement":[{"text":"The flexible loop at 671–680 was rarely observed in electron density maps and was not included in the final models of SmTK chain A, SmTK-Arg chain A, and SmTK-TSA chain B.","type":"Methods"},{"text":"Segment 671–680 of the C-terminal region of D2 is not visible in electron density maps (Fig. 1B).","type":"Results"},{"text":"The loop is delineated by two glycine residues (Gly670–Gly681) that account for its high flexibility.","type":"Results"},{"text":"The flexible loop is in red in D1 and shown with a dotted line in D2 because it is not observed in the electronic density maps. ","type":"Figure"},{"text":"A Mg2+ ion is only observed in the active site of D1, and the flexible loop is disordered in both lobes.","type":"Results"},{"text":"The disordered conformation of this loop observed in D2 allows equal access to the active site and is consistent with solution NMR measurements performed with AK (68) and CK (30).","type":"Discussion"},{"text":"The region 671-680 referred to by the authors corresponds to 701-710 residues of the UniProt sequence.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-12T15:02:42.709Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MTCTSAFIKVVRFIQVVIDTREIRSLCTIRMQVESLQNLQAKIRNDERNHSLTKKYLTDDIVKKYQATKTSLGGTLAQCVNTNAYNPGALLPRSCDLNAYETFRDFFDAVIADYHKVPDGKIQHPKSNFGDLKSLSFTDLNTYGNLVVSTRVRLGRTVEGFGFGPTLTKETRIELENKISTALHNLSGEYEGTYYPLTGMSEEDRIKLVNDHFLFRNDDNVLRDAGGYIDWPTGRGIFINKQKNFLVWINEEDHIRVISMQKGGDLIAVYKRLADAIQELSKSLKFAFNDRLGFITFCPSNLGTTLRASVHAKIPMLASLPNFKEICEKHGIQPRGTHGEHTESVGGIYDLSNKRRLGLTELDAVTEMHSGVRALLELEVMLQEYNKGAPEGVMPVEPLTYLAKLLEGASIEKCYTRKYLTPEIIKKYDGKRTTHGATLAHMIRNGAYNNRSICPRTGEAECYSTFIDYLDPLICDYHGVKDSAFKHPAPTFGDLSKLPFGDLDPTGKFIVSTRVRVGRSVEDFLFPTIMSKTDRIKLEQVISGALKGLTGEHAGTYYPLTDMKEEDRKQLVEDHFLFKNDDPVLRDAGGYRDWPVGRGIFHNNSKTFLVWVCEEDHMRIISMQQGGNLAAVYKRLIEGINAIGKSMKFAHSDKYGYITCCPSNLGTSMRASVLLKIPKLSSQPKKLDEICAKYMLQARGLYGEHTESPDGTYDISNKRRLGLTELQAAHEMAEGVAKMIEIEKGL","taxonomy":["Eukaryota","Metazoa","Spiralia","Lophotrochozoa","Platyhelminthes","Trematoda","Digenea","Strigeidida","Schistosomatoidea","Schistosomatidae","Schistosoma"],"dataset":["Neglected tropical diseases proteins"],"alphafold_very_low_content":0.04155495978552279,"disorder_content":0.013404825737265416,"disprot_consensus":{"full":[{"start":701,"end":710,"type":"D"}],"Structural state":[{"start":701,"end":710,"type":"D"}]}},{"disprot_id":"DP03901","acc":"A0A504XZ90","creator":"gbalatti","date":"2022-11-10T21:47:21.418Z","features":{"pfam":[],"gene3D":[]},"genes":[{"orfNames":[{"value":"CGC21_38360","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TPP53821.1","url":"https://www.ebi.ac.uk/ena/browser/view/TPP53821.1"}}]}]}],"length":301,"name":"Uncharacterized protein","ncbi_taxon_id":5661,"organism":"Leishmania donovani","regions":[{"start":1,"end":29,"reference_id":"33168716","reference_source":"pmid","reference_html":"Structure of the mature kinetoplastids mitoribosome and insights into its large subunit biogenesis. <i> Soufari H, Waltz F, Parrot C, Durrieu-Gaillard S, Bochler A, Kuhn L, Sissler M, Hashem Y. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-12-14T14:27:45.855Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"7AM2"},{"db":"EMDB","id":"11821"}],"region_id":"DP03901r001","statement":[{"text":"Structure of residues 1-29 is unresolved in the cryo-EM reconstructions, showing its intrinsic flexibility when this protein takes part in the Large subunit from Leishmania major mitochondrial ribosome","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15996","entry_name":"GTP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15422","entry_name":"ATP"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-14T15:42:47.308Z"}},{"start":184,"end":237,"reference_id":"33168716","reference_source":"pmid","reference_html":"Structure of the mature kinetoplastids mitoribosome and insights into its large subunit biogenesis. <i> Soufari H, Waltz F, Parrot C, Durrieu-Gaillard S, Bochler A, Kuhn L, Sissler M, Hashem Y. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-12-14T14:27:32.045Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"7AM2"},{"db":"EMDB","id":"11821"}],"region_id":"DP03901r002","statement":[{"text":"Structure of residues 184-237 is unresolved in the cryo-EM reconstructions, showing its intrinsic flexibility when this protein takes part in the Large subunit from Leishmania major mitochondrial ribosome","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15996","entry_name":"GTP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15422","entry_name":"ATP"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-14T15:42:46.707Z"}}],"regions_counter":2,"released":"2022_12","sequence":"MILITSNCARVAAFARKAACRGALCDRHRCISGGGRGDLFTRHASAFKPPAFGVLRGLTHSSQTTHPQTGQLRARKLIQHAMHDRTLSGSGHHRTAVATWSYLLPSLRQNVEQAVPDTLYEKLLTDEVPLTPAESRQLADAHRLLRFELQKRIGLLEDSLADAALPYLLQWPALFQRAWLRLPMDQGSASVTDAKRDAVVPAPPSFVHAPAALPITEWAPTLSPASPSACSNGLIGRGALVPRLAQLTRHVIRCVEEDLGRLEHGSEPREDGAPRSRRQVTLEAAWRAQWASLLSWHAGTS","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"alphafold_very_low_content":0.2558139534883721,"disorder_content":0.2757475083056478,"disprot_consensus":{"full":[{"start":1,"end":29,"type":"D"},{"start":184,"end":237,"type":"D"}],"Structural state":[{"start":1,"end":29,"type":"D"},{"start":184,"end":237,"type":"D"}]}},{"disprot_id":"DP03902","acc":"A0A504WW14","creator":"gbalatti","date":"2022-11-10T22:10:43.601Z","features":{"pfam":[],"gene3D":[]},"genes":[{"orfNames":[{"value":"CGC21_25710","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TPP39988.1","url":"https://www.ebi.ac.uk/ena/browser/view/TPP39988.1"}}]}]}],"length":1347,"name":"Flagellar attachment zone protein 1","ncbi_taxon_id":5661,"organism":"Leishmania donovani","regions":[{"start":1,"end":1259,"reference_id":"33168716","reference_source":"pmid","reference_html":"Structure of the mature kinetoplastids mitoribosome and insights into its large subunit biogenesis. <i> Soufari H, Waltz F, Parrot C, Durrieu-Gaillard S, Bochler A, Kuhn L, Sissler M, Hashem Y. </i> Proc Natl Acad Sci U S A, 2020","date":"2022-12-14T14:46:29.016Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"7AM2"},{"db":"EMDB","id":"11821"},{"db":"PDB","id":"7AIH"},{"db":"EMDB","id":"11796"}],"region_id":"DP03902r001","statement":[{"text":"Structure of residues 1-1259 is unresolved in the cryo-EM reconstructions, showing its intrinsic flexibility when this protein takes part in the Large subunit from Leishmania major mitochondrial ribosome","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15996","entry_name":"GTP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15422","entry_name":"ATP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"13389","entry_name":"NAD"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-14T15:43:26.400Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MLARYLDPSVHPLRVGQVVAYDYLHAAKTWQWTLGTVREIKDYTAVVQQWGLHTGDIDTLRSILLKEVDTENGRMKNYHDMLAIAREKLASIRRSNEDRVSHVRGHFDKAREKVELIDEVDLRKVTAQAAPSPVAVAVLKAVWAVAKCDPTAVEFYEWADVQLEYRKPAALDEIAKTDVLAKLYPSAESLQQSLEQDPKLNYKAAARDSPVVASLHAWVITALAYQQAYNLLAHDKRIQEQNDAIAAAIAGMKACRAKIAKLKDELSSKDTAALPGQVTSFTRTSVLVTIPLSAVISPVNVDTDVKRCVLTKDEVEQIPIDAKITRYAQKQKLAITGSHLLDQYAAATTTHIYVTELEDRLFFFQHYMASALRDAQTAAVDAHQRLAVSLHELEAFRQKRHDAKKARAAEPELADADGVEPSSGPTSSRSPTGRAAPRGQSAAPRGTASQQHKLLGPAYQSIDPATIANEPLYAVTIEEYKAKDAAGERAMDEAERMADEVQRLAVELEDAKAAADKLAEELAAKDEELAAHRQKRHDAQQARASDPALAAADAVAPRSGKGAASPHVGAVQRQAVDPATVPVAPAVIAEEPLYVATAEELQHVRDFADQLAEELEAFRQKRHDAKKARAAEPELADADGVEPSSGPTSSRSPTGRAAPRGQSAAPRGTASQQHKLLGPAYQSIDPATIANEPLYAVTIEEYKAKDAAGERAMDEAERMADEVQRLAVELEDAKAAADKLAEELAAKDEELAAHRQKRHDAQQARASDPALAAADAVAPRSGKGAASPHVGAVQRQAVDPATVPVAPAVIAEEPLYVATAEELQHVRDFADQLAEELEAFRQKRHDAKKARAAEPELADADGVEPSSGPTSSRSPTGRAAPRGQSAAPRGTASQQHKLLGPAYQSIDPATIANEPLYAVTIEEYKAKDAAGERAMDEAERMADEVQRLAVELEDAKAAADKLAEELAAKDEELAAHRQKRHDAQQARASDPALAAADAVAPRSGKGAASPHVGAVQRQAVDPATVPVAPAVIAEEPLYVATAEELQHVRDFADQAAHDAATREAEVAGTVENLRNELDDVREMNAKLEDEVFALKEQLSDAEDAYKKLAGALVVAEDERQELCDDLEAALDELEQKKDEYDELLGNLEEVQGLLEAADVAGRTAVEALEQRNRDMADLQGELANALDASKENENLRALLDAKEREIDRLKEYNSFWTDTVGTGKQKVTHRLTKIFDGDWTRLMRHRPEALKAAFVIDSSNACHVPGDQIFLVSNSFTRRLLTRTDHCPKCDRLSTFRFMSVSGMVGRMPYKPVDTPGPSYATLYWRKQRSGKIASQPLNEVCNKNEF","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"disorder_content":0.9346696362286563,"disprot_consensus":{"full":[{"start":1,"end":1259,"type":"D"}],"Structural state":[{"start":1,"end":1259,"type":"D"}]}},{"disprot_id":"DP03903","acc":"Q869A5","creator":"gbalatti","date":"2022-11-10T22:31:23.884Z","features":{"pfam":[{"id":"PF00255","name":"Glutathione peroxidase","start":15,"end":123}],"gene3D":[]},"genes":[{"name":{"value":"gpx3","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAC83349.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAC83349.1"}}]}}],"length":176,"name":"Glutathione peroxidase","ncbi_taxon_id":5691,"organism":"Trypanosoma brucei","regions":[{"start":76,"end":116,"reference_id":"18684708","reference_source":"pmid","reference_html":"Structural basis for a distinct catalytic mechanism in Trypanosoma brucei tryparedoxin peroxidase. <i> Melchers J, Diechtierow M, Fehér K, Sinning I, Tews I, Krauth-Siegel RL, Muhle-Goll C. </i> J Biol Chem, 2008","date":"2022-12-14T15:04:09.358Z","curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys76Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The mitochondrial signal sequence of Px III was removed, and Cys76 was replaced by a serine residue which resulted in a fully active peroxidase "}]}],"cross_refs":[{"db":"PDB","id":"2RM6"},{"db":"PDB","id":"2RM5"}],"region_id":"DP03903r001","sequence_construct":"GMGSSIFDFEVLDADHKPYNLVQHKGSPLLIYNVASKCGYTKGGYETATTLYNKYKSQGFTVLAFPSNQFGGQEPGNEEEIKEFVCTKFKAEFPIMAKINVNGENAHPLYEYMKKTKPGILATKAIKWNFTSFLIDRDGVPVERFSPGASVKDIEEKLIPLLGSARL","statement":[{"text":"In both oxidized and reduced Px III, the peroxidatic Cys47 is located on the first loop (L1) between β-strand 1 and α-helix 1, whereas the resolving Cys95 is part of the long loop 2 (L2) between β-sheet 2 and α-helix 2 that is relatively disordered in the bundle of NMR structures (Figs. 2, B and C).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-16T14:00:23.769Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MLRSSRKKMSAASSIFDFEVLDADHKPYNLVQHKGSPLLIYNVASKCGYTKGGYETATALYNKYKSQGFTVLAFPCNQFGGQEPGTEEEIKEFVCTKFKAEFPIMAKINVNGENAHPLYEYMKKTKPGILATKAIKWNFTSFLIDRDGVPVERFSPGASVKDIEEKLIPLLGSARL","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Trypanosoma"],"dataset":["Neglected tropical diseases proteins"],"alphafold_very_low_content":0.028409090909090908,"disorder_content":0.23295454545454544,"disprot_consensus":{"full":[{"start":76,"end":116,"type":"D"}],"Structural state":[{"start":76,"end":116,"type":"D"}]}},{"disprot_id":"DP03907","acc":"Q8TDP1","creator":"fkordevani","date":"2022-11-23T14:38:27.083Z","features":{"pfam":[{"id":"PF08615","name":"Ribonuclease H2 non-catalytic subunit (Ylr154p-like)","start":28,"end":157}],"gene3D":[]},"genes":[{"name":{"value":"RNASEH2C"},"synonyms":[{"value":"AYP1"}]}],"length":164,"name":"Ribonuclease H2 subunit C","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":13,"reference_id":"21177854","reference_source":"pmid","reference_html":"The structure of the human RNase H2 complex defines key interaction interfaces relevant to enzyme function and human disease. <i> Reijns MA, Bubeck D, Gibson LC, Graham SC, Baillie GS, Jones EY, Jackson AP. </i> J Biol Chem, 2011","date":"2022-12-15T15:09:21.723Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3P56"}],"region_id":"DP03907r001","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75792"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q5TBB1"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-26T14:37:55.716Z"}},{"start":87,"end":117,"reference_id":"21177854","reference_source":"pmid","reference_html":"The structure of the human RNase H2 complex defines key interaction interfaces relevant to enzyme function and human disease. <i> Reijns MA, Bubeck D, Gibson LC, Graham SC, Baillie GS, Jones EY, Jackson AP. </i> J Biol Chem, 2011","date":"2022-12-15T15:09:56.973Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3P56"}],"region_id":"DP03907r002","statement":[{"text":"Therefore, our structural, biochemical and primary sequence analyses are all consistent with RNASEH2C residues 87–117 forming a disordered loop, while RNASEH2C residues 118–160 comprise an integral part of the heterotrimer, essential for complex formation and enzymatic activity.","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75792"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q5TBB1"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-26T14:37:56.019Z"}},{"start":93,"end":107,"reference_id":"21177858","reference_source":"pmid","reference_html":"The structural and biochemical characterization of human RNase H2 complex reveals the molecular basis for substrate recognition and Aicardi-Goutières syndrome defects. <i> Figiel M, Chon H, Cerritelli SM, Cybulska M, Crouch RJ, Nowotny M. </i> J Biol Chem, 2011","date":"2022-12-15T15:10:37.162Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3PUF"}],"region_id":"DP03907r003","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75792"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q5TBB1"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-26T14:37:56.452Z"}}],"regions_counter":3,"released":"2023_06","sequence":"MESGDEAAIERHRVHLRSATLRDAVPATLHLLPCEVAVDGPAPVGRFFTPAIRQGPEGLEVSFRGRCLRGEEVAVPPGLVGYVMVTEEKKVSMGKPDPLRDSGTDDQEEEPLERDFDRFIGATANFSRFTLWGLETIPGPDAKVRGALTWPSLAAAIHAQVPED","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","RNA-binding proteins"],"alphafold_very_low_content":0.12804878048780488,"disorder_content":0.2682926829268293,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"D"},{"start":87,"end":117,"type":"D"}],"Structural state":[{"start":1,"end":13,"type":"D"},{"start":87,"end":117,"type":"D"}]}},{"disprot_id":"DP03908","acc":"P84243","creator":"ndeutsch","date":"2022-11-23T14:45:42.363Z","features":{"pfam":[{"id":"PF00125","name":"Core histone H2A/H2B/H3/H4 domain","start":44,"end":131}],"gene3D":[]},"genes":[{"name":{"value":"H3-3A","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4764","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4764"}}]},"synonyms":[{"value":"H3.3A"},{"value":"H3F3"},{"value":"H3F3A"}],"orfNames":[{"value":"PP781"}]},{"name":{"value":"H3-3B","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4765","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4765"}}]},"synonyms":[{"value":"H3.3B"},{"value":"H3F3B"}]}],"length":136,"name":"Histone H3.3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":38,"reference_id":"30287617","reference_source":"pmid","reference_html":"Structural basis of the nucleosome transition during RNA polymerase II passage. <i> Kujirai T, Ehara H, Fujino Y, Shirouzu M, Sekine SI, Kurumizaka H. </i> Science, 2018","date":"2022-12-15T15:26:37.220Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6INQ"},{"db":"PDB","id":"6A5O"},{"db":"PDB","id":"6A5L"},{"db":"PDB","id":"6A5T"},{"db":"PDB","id":"6A5U"},{"db":"PDB","id":"6A5R"},{"db":"PDB","id":"6A5P"}],"region_id":"DP03908r001","statement":[{"text":"The x-ray structures of the RNA polymerase II elongation complex stalled at different SHL show this region of the Histone H3.3 lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-19T13:04:03.535Z"}}],"regions_counter":9,"released":"2023_06","sequence":"MARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Cancer-related proteins"],"alphafold_very_low_content":0.007352941176470588,"disorder_content":0.27941176470588236,"disprot_consensus":{"full":[{"start":1,"end":38,"type":"D"}],"Structural state":[{"start":1,"end":38,"type":"D"}]}},{"disprot_id":"DP03909","acc":"P36156","creator":"vacs","date":"2022-11-24T11:55:21.288Z","features":{"pfam":[{"id":"PF13409","name":"Glutathione S-transferase, N-terminal domain","start":45,"end":183},{"id":"PF13410","name":"Glutathione S-transferase, C-terminal domain","start":233,"end":324}],"gene3D":[]},"genes":[{"name":{"value":"ECM4"},"synonyms":[{"value":"GTO2"}],"olnNames":[{"value":"YKR076W"}]}],"length":370,"name":"Glutathione S-transferase omega-like 2","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":10,"reference_id":"27736955","reference_source":"pmid","reference_html":"Crystal Structure of Saccharomyces cerevisiae ECM4, a Xi-Class Glutathione Transferase that Reacts with Glutathionyl-(hydro)quinones. <i> Schwartz M, Didierjean C, Hecker A, Girardet JM, Morel-Rouhier M, Gelhaye E, Favier F. </i> PLoS One, 2016","date":"2022-11-24T11:57:26.171Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5LKB"},{"db":"PDB","id":"5LKD"}],"region_id":"DP03909r001","statement":[{"text":"Due to absence or weakness of electron density in some regions, all monomers built in the structures lacked about thirty residues at similar positions, namely the ten first N-terminal ones (fifteen in monomer B of ScECM4-SG), the 6 histidine residues from the C-terminal tag and residues between D83 and L95.","type":"Results"},{"text":"The lack of electron density upstream G11 suggested a relative flexibility of the first residues.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-19T13:01:46.507Z"}},{"start":84,"end":93,"reference_id":"27736955","reference_source":"pmid","reference_html":"Crystal Structure of Saccharomyces cerevisiae ECM4, a Xi-Class Glutathione Transferase that Reacts with Glutathionyl-(hydro)quinones. <i> Schwartz M, Didierjean C, Hecker A, Girardet JM, Morel-Rouhier M, Gelhaye E, Favier F. </i> PLoS One, 2016","date":"2022-11-24T11:58:58.077Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5LKB"},{"db":"PDB","id":"5LKD"}],"region_id":"DP03909r002","statement":[{"text":"Due to absence or weakness of electron density in some regions, all monomers built in the structures lacked about thirty residues at similar positions, namely the ten first N-terminal ones (fifteen in monomer B of ScECM4-SG), the 6 histidine residues from the C-terminal tag and residues between D83 and L95.","type":"Results"},{"text":"Residues 84-93 are missing in all chains.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-19T13:01:46.815Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MSKQWASGTNGAFKRQVSSFRETISKQHPIYKPAKGRYWLYVSLACPWAHRTLITRALKGLTSVIGCSVVHWHLDEKGWRFLDMEKQLEDSEDFLEHWHDVAGGIRTAKEDSSKSFAEIKNDSQRFMVDATNEPHYGYKRISDLYYKSDPQYSARFTVPVLWDLETQTIVNNESSEIIRILNSSAFDEFVDDDHKKTDLVPAQLKTQIDDFNSWVYDSINNGVYKTGFAEKAEVYESEVNNVFEHLDKVEKILSDKYSKLKAKYGEEDRQKILGEFFTVGDQLTEADIRLYTTVIRFDPVYVQHFKCNFTSIRAGYPFIHLWVRNLYWNYDAFRYTTDFDHIKLHYTRSHTRINPLGITPLGPKPDIRPL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.013513513513513514,"disorder_content":0.05405405405405406,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"},{"start":84,"end":93,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":84,"end":93,"type":"D"}]}},{"disprot_id":"DP03910","acc":"Q8WQX9","creator":"jnilsson","date":"2022-12-12T18:58:29.911Z","features":{"pfam":[{"id":"PF00233","name":"3'5'-cyclic nucleotide phosphodiesterase","start":668,"end":903},{"id":"PF01590","name":"GAF domain","start":238,"end":374},{"id":"PF01590","name":"GAF domain","start":407,"end":547}],"gene3D":[]},"genes":[{"name":{"value":"PDEB1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAK33016.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAK33016.1"}}]}}],"length":930,"name":"Phosphodiesterase","ncbi_taxon_id":5691,"organism":"Trypanosoma brucei","regions":[{"start":576,"end":585,"reference_id":"23409953","reference_source":"pmid","reference_html":"Discovery of novel Trypanosoma brucei phosphodiesterase B1 inhibitors by virtual screening against the unliganded TbrPDEB1 crystal structure. <i> Jansen C, Wang H, Kooistra AJ, de Graaf C, Orrling KM, Tenor H, Seebeck T, Bailey D, de Esch IJ, Ke H, Leurs R. </i> J Med Chem, 2013","date":"2022-12-13T15:57:15.521Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"4I15"}],"region_id":"DP03910r001","statement":[{"text":"Following crystallization, the TbrPDEB1 structure with residues 586–918 could be resolved by X-ray diffraction at a resolution of 1.65 Å (Table 1).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-14T12:39:17.772Z"}},{"start":565,"end":585,"reference_id":"29672041","reference_source":"pmid","reference_html":"Targeting a Subpocket in Trypanosoma brucei Phosphodiesterase B1 (TbrPDEB1) Enables the Structure-Based Discovery of Selective Inhibitors with Trypanocidal Activity. <i> Blaazer AR, Singh AK, de Heuvel E, Edink E, Orrling KM, Veerman JJN, van den Bergh T, Jansen C, Balasubramaniam E, Mooij WJ, Custers H, Sijm M, Tagoe DNA, Kalejaiye TD, Munday JC, Tenor H, Matheeussen A, Wijtmans M, Siderius M, de Graaf C, Maes L, de Koning HP, Bailey DS, Sterk GJ, de Esch IJP, Brown DG, Leurs R. </i> J Med Chem, 2018","date":"2022-12-13T15:55:42.132Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"5G2B"},{"db":"PDB","id":"5G57"},{"db":"PDB","id":"5L8Y"},{"db":"PDB","id":"5L8C"},{"db":"PDB","id":"5L9H"},{"db":"PDB","id":"5G5V"}],"region_id":"DP03910r002","statement":[{"text":"The PDB structure shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-14T12:39:25.273Z"}}],"regions_counter":2,"released":"2022_12","sequence":"MFMNKPFGSKRCEPFHESEHLCEAFAITEAILARYQRGKRSFTSSEKSGLAALIKRIPYDILVEVLDQSGFTPTSNATPPVDYLAMMEHTMTHGASITHALQYLNDLMTKCTGCPGIRTYYHNPNDDVLADPVHDTAALIDETTAVGKSVVTKQYLNIAGAHYIPLIHGDIVVGCVEVPRFSGNLEKLPSFPSLIRAVTCTAHKFIEEARINWNREKAEAMLQMATRLARDNLDETVLASSIMNTVKSLTESARCSLFLVKDDKLEAHFEDGNVVSIPKGTGIVGYVAQTGETVNIVDAYADDRFNREVDKATGYRTKTILCMPVMYEGTIVAVTQLINKLDLTTESGLRLPRVFGKRDEELFQTFSMFAGASLRNCRINDRLLKEKKKSDVILDVVTVLSNTDIRDVDGIVRHALHGAKKLLNADRSTLFLVDKERNELCSRMADSVAGKEIRFPCGQGIAGTVAASGVGENIQDAYQDPRFNREVDKQLGYRTQTILCEPIILNGEILAVVQLVNKLDTSGEVTVFTEDDRDTFRVFSLFAGISINNSHLLEFAVKAGREVMELNEHRATLFNKNVPSRAVKRVTAITKVEREAVLVCELPSFDVTDVEFDLFRARESTDKPLDVAAAIAYRLLLGSGLPQKFGCSDEVLLNFILQCRKKYRNVPYHNFYHVVDVCQTIHTFLYRGNVYEKLTELECFVLLITALVHDLDHMGLNNSFYLKTESPLGILSSASGNTSVLEVHHCNLAVEILSDPESDVFDGLEGAERTLAFRSMIDCVLATDMAKHGSALEAFLASAADQSSDEAAFHRMTMEIILKAGDISNVTKPFDISRQWAMAVTEEFYRQGDMEKERGVEVLPMFDRSKNMELAKGQIGFIDFVAAPFFQKIVDACLQGMQWTVDRIKSNRAQWERVLETRLSTSSGNNSSTR","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Trypanosoma"],"dataset":["Neglected tropical diseases proteins"],"alphafold_very_low_content":0.10967741935483871,"disorder_content":0.02258064516129032,"disprot_consensus":{"full":[{"start":565,"end":585,"type":"D"}],"Structural state":[{"start":565,"end":585,"type":"D"}]}},{"disprot_id":"DP03911","acc":"Q86C09","creator":"jnilsson","date":"2022-12-14T13:47:49.645Z","features":{"pfam":[{"id":"PF00348","name":"Polyprenyl synthetase","start":34,"end":319}],"gene3D":[]},"genes":[],"length":367,"name":"Farnesyl pyrophosphate synthase","ncbi_taxon_id":5691,"organism":"Trypanosoma brucei","regions":[{"start":64,"end":73,"reference_id":"18442135","reference_source":"pmid","reference_html":"Structures of a potent phenylalkyl bisphosphonate inhibitor bound to farnesyl and geranylgeranyl diphosphate synthases. <i> Cao R, Chen CK, Guo RT, Wang AH, Oldfield E. </i> Proteins, 2008","date":"2022-12-16T15:40:23.691Z","curator_id":"jnilsson","curator_name":"Juliet Nilsson","curator_orcid":"0000-0003-4203-5263","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2022_12","version":0,"cross_refs":[{"db":"PDB","id":"2P1C"}],"region_id":"DP03911r001","statement":[{"text":"The PDB structure shows this region lacks electron density, indicating it is disordered","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-16T15:42:51.583Z"}}],"regions_counter":1,"released":"2022_12","sequence":"MPMQMFMQVYDEIQMFLLEELELKFDMDPNRVRYLRKMMDTTCLGGKYNRGLTVIDVAESLLSLSPNNNGEEDDGARRKRVLHDACVCGWMIEFLQAHYLVEDDIMDNSVTRRGKPCWYRHPDVTVQCAINDGLLLKSWTHMMAMHFFADRPFLQDLLCRFNRVDYTTAVGQLYDVTSMFDSNKLDPDVSQPTTTDFAEFTLSNYKRIVKYKTAYYTYLLPLVMGLIVSEALPTVDMGVTEELAMLMGEYFQVQDDVMDCFTPPERLGKVGTDIQDAKCSWLAVTFLAKASSAQVAEFKANYGSGDSEKVATVRRLYEEADLQGDYVAYEAAVAEQVKELIEKLRLCSPGFAASVETLWGKTYKRQK","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Trypanosoma"],"dataset":["Neglected tropical diseases proteins"],"alphafold_very_low_content":0.005449591280653951,"disorder_content":0.027247956403269755,"disprot_consensus":{"full":[{"start":64,"end":73,"type":"D"}],"Structural state":[{"start":64,"end":73,"type":"D"}]}},{"disprot_id":"DP03912","acc":"P77526","creator":"vacs","date":"2022-12-16T10:47:04.640Z","features":{"pfam":[{"id":"PF00043","name":"Glutathione S-transferase, C-terminal domain","start":135,"end":197},{"id":"PF02798","name":"Glutathione S-transferase, N-terminal domain","start":4,"end":81}],"gene3D":[]},"genes":[{"name":{"value":"yfcG"},"olnNames":[{"value":"b2302"},{"value":"JW2299"}]}],"length":215,"name":"Disulfide-bond oxidoreductase YfcG","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":205,"end":215,"reference_id":"19537707","reference_source":"pmid","reference_html":"Analysis of the structure and function of YfcG from Escherichia coli reveals an efficient and unique disulfide bond reductase. <i> Wadington MC, Ladner JE, Stourman NV, Harp JM, Armstrong RN. </i> Biochemistry, 2009","date":"2022-12-16T10:49:24.484Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3GX0"}],"region_id":"DP03912r001","statement":[{"text":"Ten residues at the C-terminal are not seen in the electron density map.","type":"Supplementary material"},{"text":"The last 11 residues are missing in the structure and are presumably disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-19T12:56:53.246Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MIDLYFAPTPNGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSPADGGEPLSLFESGAILLYLAEKTGLFLSHETRERAATLQWLFWQVGGLGPMLGQNHHFNHAAPQTIPYAIERYQVETQRLYHVLNKRLENSPWLGGENYSIADIACWPWVNAWTRQRIDLAMYPAVKNWHERIRSRPATGQALLKAQLGDERSDS","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"alphafold_very_low_content":0.027906976744186046,"disorder_content":0.05116279069767442,"disprot_consensus":{"full":[{"start":205,"end":215,"type":"D"}],"Structural state":[{"start":205,"end":215,"type":"D"}]}},{"disprot_id":"DP03913","acc":"P0AFW0","creator":"vacs","date":"2022-12-19T19:45:34.684Z","features":{"pfam":[{"id":"PF02357","name":"Transcription termination factor nusG","start":3,"end":96}],"gene3D":[]},"genes":[{"name":{"value":"rfaH","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00951","url":"https://hamap.expasy.org/unirule/MF_00951"}}]},"synonyms":[{"value":"hlyT"},{"value":"sfrB"}],"olnNames":[{"value":"b3842"},{"value":"JW3818"}]}],"length":162,"name":"Transcription antitermination protein RfaH","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":101,"end":114,"reference_id":"17434131","reference_source":"pmid","reference_html":"Structural basis for converting a general transcription factor into an operon-specific virulence regulator. <i> Belogurov GA, Vassylyeva MN, Svetlov V, Klyuyev S, Grishin NV, Vassylyev DG, Artsimovitch I. </i> Mol Cell, 2007","date":"2022-12-19T19:49:26.801Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2OUG"}],"region_id":"DP03913r001","statement":[{"text":"The asymmetric unit contains two molecules of RfaH (see Figure S1 in the Supplemental Data available with this article online); each protomer consists of two domains (N and C terminal) connected by a 14 residue-long flexible linker that lacks electron density and thus appears to be disordered in the crystal (Figure 1A).","type":"Results"},{"text":"The C domain was then added through extension of the N-domain C-terminal α helix, with the interdomain linker (disordered in the crystals) modeled in an α-helical conformation.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-20T15:02:38.262Z"}},{"start":101,"end":114,"reference_id":"17434131","reference_source":"pmid","reference_html":"Structural basis for converting a general transcription factor into an operon-specific virulence regulator. <i> Belogurov GA, Vassylyeva MN, Svetlov V, Klyuyev S, Grishin NV, Vassylyev DG, Artsimovitch I. </i> Mol Cell, 2007","date":"2022-12-19T19:52:34.433Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2OUG"}],"region_id":"DP03913r002","statement":[{"text":"The asymmetric unit contains two molecules of RfaH (see Figure S1 in the Supplemental Data available with this article online); each protomer consists of two domains (N and C terminal) connected by a 14 residue-long flexible linker that lacks electron density and thus appears to be disordered in the crystal (Figure 1A).","type":"Results"},{"text":"The overall structural similarity between RfaH and NusG might be extended to the long flexible linkers connecting the C and N domains.","type":"Results"},{"text":"The C domain was then added through extension of the N-domain C-terminal α helix, with the interdomain linker (disordered in the crystals) modeled in an α-helical conformation.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2022-12-20T15:02:58.360Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MQSWYLLYCKRGQLQRAQEHLERQAVNCLAPMITLEKIVRGKRTAVSEPLFPNYLFVEFDPEVIHTTTINATRGVSHFVRFGASPAIVPSAVIHQLSVYKPKDIVDPATPYPGDKVIITEGAFEGFQAIFTEPDGEARSMLLLNLINKEIKHSVKNTEFRKL","taxonomy":["Bacteria","Proteobacteria","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"alphafold_very_low_content":0.14814814814814814,"disorder_content":0.08641975308641975,"disprot_consensus":{"full":[{"start":101,"end":114,"type":"D"}],"Structural state":[{"start":101,"end":114,"type":"D"}],"Disorder function":[{"start":101,"end":114,"type":"F"}]}},{"disprot_id":"DP03914","acc":"G0SCF1","creator":"vnugnes","date":"2022-12-22T13:40:57.041Z","features":{"pfam":[{"id":"PF00400","name":"WD domain, G-beta repeat","start":489,"end":528},{"id":"PF28639","name":"Dynein axonemal intermediate chain 3 WD40 domain","start":279,"end":393}],"gene3D":[]},"genes":[{"orfNames":[{"value":"CTHT_0056990","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EGS19077.1","url":"https://www.ebi.ac.uk/ena/browser/view/EGS19077.1"}}]}]}],"length":707,"name":"Putative dynein intermediate chain protein","ncbi_taxon_id":759272,"organism":"Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)","regions":[{"start":31,"end":88,"reference_id":"32814057","reference_source":"pmid","reference_html":"Interplay of Disorder and Sequence Specificity in the Formation of Stable Dynein-Dynactin Complexes. <i> Loening NM, Saravanan S, Jespersen NE, Jara K, Barbar E. </i> Biophys J, 2020","date":"2022-12-22T14:12:25.079Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6PQT"}],"region_id":"DP03914r001","statement":[{"text":"Secondary chemical shift analysis (Fig. 4 C) clearly indicates an α-helical structure for residues 1–30 (the SAH region) and a nascent α-helix for residues 50–64 (the H2 region). Other residues with secondary chemical shift values close to zero are intrinsically disordered.","type":"Results"},{"text":"Three-bond HN-Hα scalar coupling constants (3JHN-Hα) for IC88 (Fig. 4 D) are in the range of 4–6 Hz for residues 1–30, which implies that this region has an α-helical secondary structure. The remaining residues have coupling values that are, for the most part, between 6 and 8 Hz, which is consistent with these residues lacking a fixed secondary structure. ","type":"Results"},{"text":"Both the 3JHN-Hα and the 1DHN coupling values support our prediction that the H2 region forms a nascent, rather than a fully formed, α-helix.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-27T08:33:30.237Z"}},{"start":31,"end":88,"reference_id":"32814057","reference_source":"pmid","reference_html":"Interplay of Disorder and Sequence Specificity in the Formation of Stable Dynein-Dynactin Complexes. <i> Loening NM, Saravanan S, Jespersen NE, Jara K, Barbar E. </i> Biophys J, 2020","date":"2022-12-22T14:51:52.089Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","region_id":"DP03914r002","statement":[{"text":"In comparison, the thermogram for IC35 binding to p150ABC (Fig. 7 A, middle) showed that removing H2 and the disordered linker regions surrounding it (residues 30–50 and 60–88) drastically diminished the second step.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"G0RYI7","operator":"and","partner_start":478,"partner_end":680}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-27T08:33:14.240Z"}},{"start":50,"end":64,"reference_id":"32814057","reference_source":"pmid","reference_html":"Interplay of Disorder and Sequence Specificity in the Formation of Stable Dynein-Dynactin Complexes. <i> Loening NM, Saravanan S, Jespersen NE, Jara K, Barbar E. </i> Biophys J, 2020","date":"2022-12-22T15:02:04.952Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"G0RYI7","operator":null,"partner_start":478,"partner_end":680}],"region_id":"DP03914r003","statement":[{"text":"An NMR titration of 15N-labeled IC37–88 with unlabeled p150ABC (Fig. 7 D) shows a complete loss of signal for the H2 region and that signal for the linker regions diminishes depending on how close the linker residues are to the H2 region. This confirms that the H2 region directly interacts with p150ABC and strongly suggests that reduced peak volumes for residues in the linker regions (as seen in Figs. 6 C and ​and77 D) are a result of the reduced mobility of these residues due to their proximity to regions that bind p150ABC rather than due to a direct interaction between these residues and p150ABC.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-27T08:33:17.309Z"}},{"start":77,"end":161,"reference_id":"36416224","reference_source":"pmid","reference_html":"Multivalency, autoinhibition, and protein disorder in the regulation of interactions of dynein intermediate chain with dynactin and the nuclear distribution protein. <i> Jara KA, Loening NM, Reardon PN, Yu Z, Woonnimani P, Brooks C, Vesely CH, Barbar EJ. </i> Elife, 2022","date":"2022-12-22T16:45:29.479Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03914r004","statement":[{"text":"The limited chemical shift dispersion at 10°C (Figure 4B), along with appearance of the majority of the peaks in the CLEANEX experiment at this temperature (Figure 4C), indicates that the peaks observed in the spectra are for the disordered regions of IC1-260.","type":"Results"},{"text":"Assigned residues are in black in the sequence above the plot (and unassigned residues in gray); all assigned residues are from disordered regions of IC1-260.","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-27T08:33:56.111Z"}}],"regions_counter":4,"released":"2024_06","sequence":"MQARREELLAKKARLAEIKRQRELRAQQAAGRSITPSELVSPTPSRANSRREIESLIDSILSSSAGANSPRRGSRPNSVISTGELSTDNASEITATTTGQLPSQPQPLSTVPLQTVYECPPSPVKEIISYSKGVQTTEEWTPRKSRGVGDSDDEDLGAAASPSKRLSRRERDREEELREKIRKEIEEELKATKELVADGVLKQSGAQNFPVRALTAEELDAVTKSVEFMDFIDRSTKVIEKALDQEYDILTDYTLQVHDVEDEDEQSGNVGGKGRRKVREIAQFYDERWSKKRMISSIDFSPKFSELLLASYTKNPTAPHDPDGIVQVWNLHLHDRPEFVFHAQSDILTAKFSPFHPNLIIGGAYSGQVLLWDTRARSAPVQKTPLTGSGHTHPVYCIDIVGTQNANNIISCSTDGAVCGWSVDMLAQPQESLTLLAPLPAKSEDLSPTCMAFPQADPTFFLVGTEEGTIYPCHRYDRAGAKAGVDPRVSYRGHAGPVMSVAFHPARGPVDLGDLVLSSSLDWSVKLWKVRAPAATSGVLSSGSVTSPSAAAAAAAAAAAVTAPLPGSTTGSLDSQVTPLLDLVREDVVYDAAWSPIKPGVFGLVDGAGTLEIWDITVETEEPVARVVPTPRKDRGALLGMKSLNKVAWEPSEGKRLATGGLDGVVSMFEVGPDLGGKEGLRNEDWGTVKKLVNRLEAGGSVDGVGM","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Sordariomycetidae","Sordariales","Chaetomiaceae","Thermochaetoides"],"alphafold_very_low_content":0.26449787835926447,"disorder_content":0.18528995756718528,"disprot_consensus":{"full":[{"start":31,"end":161,"type":"D"}],"Structural state":[{"start":31,"end":161,"type":"D"}],"Molecular function":[{"start":31,"end":88,"type":"F"}]}},{"disprot_id":"DP03915","acc":"P22108","creator":"vacs","date":"2023-01-06T13:05:52.163Z","features":{"pfam":[{"id":"PF09830","name":"ATP adenylyltransferase C-terminal domain","start":198,"end":313},{"id":"PF19327","name":"Ap4A phosphorylase N-terminal domain","start":4,"end":169}],"gene3D":[]},"genes":[{"name":{"value":"APA2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"2174863","url":"http://www.ncbi.nlm.nih.gov/pubmed/2174863","alternativeUrl":"https://europepmc.org/abstract/MED/2174863"}}]},"orfNames":[{"value":"D9719.33"}],"olnNames":[{"value":"YDR530C","evidences":[{"code":"ECO:0000312","source":{"name":"SGD","id":"S000002938","url":"https://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000002938"}}]}]}],"length":325,"name":"Diadenosine 5',5'''-P1,P4-tetraphosphate phosphorylase 2","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":53,"end":63,"reference_id":"23628156","reference_source":"pmid","reference_html":"Structures of yeast Apa2 reveal catalytic insights into a canonical AP₄A phosphorylase of the histidine triad superfamily. <i> Hou WT, Li WZ, Chen Y, Jiang YL, Zhou CZ. </i> J Mol Biol, 2013","date":"2023-03-27T13:52:10.746Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4I5W"},{"db":"PDB","id":"4I5T"}],"region_id":"DP03915r001","statement":[{"text":"In the apo-Apa2 model, residues Lys53–Glu65 and Lys134–Thr139 in molecule A and Lys53–Lys63 in molecule B are missing due to their poor electron density.","type":"Results"},{"text":"Notably, the missing residues (Lys53–Glu65) from three structures of Apa2 were probably located across the Ap4A-binding cleft, suggesting that these residues might be adjacent to the Ap4A entrance tunnel and thus are relatively flexible.","type":"Results"},{"text":"Residues 53-63 are disordered in both the apo-Apa2 and Apa2-AMP structures.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-05T15:23:23.408Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MIEENLKQKIHDKFVAAKKNGHLKVTHAESKKLKDPQTTTQYWVTFAPSLALKPDANKNSDSKAEDPFANPDEELVVTEDLNGDGEYKLLLNKFPVVPEHSLLVTSEFKDQRSALTPSDLMTAYNVLCSLQGDKDDDVTCERYLVFYNCGPHSGSSQDHKHLQIMQMPEKFIPFQDVLCNGKDHFLPTFNAEPLQDDKVSFAHFVLPLPESSDQVDEDLLAMCYVSLMQRALTFFQDWTNESPELTKSYNVLLTKKWICVVPRSHAKSGPPLMLNINSTGYCGMILVKDREKLENLTEDPHLVDKSLLQCGFPNTAGQKPTEYHY","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.024615384615384615,"disorder_content":0.033846153846153845,"disprot_consensus":{"full":[{"start":53,"end":63,"type":"D"}],"Structural state":[{"start":53,"end":63,"type":"D"}]}},{"disprot_id":"DP03916","acc":"Q3E7B7","creator":"rpancsa","date":"2023-01-16T12:21:46.454Z","features":{"pfam":[{"id":"PF04419","name":"Small EDRK-rich factor 1/2-like, N-terminal","start":1,"end":35}],"gene3D":[]},"genes":[{"olnNames":[{"value":"YDL085C-A"}]}],"length":68,"name":"SERF-like protein YDL085C-A","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":35,"reference_id":"35713792","reference_source":"pmid","reference_html":"Backbone resonance assignments and dynamics of S. cerevisiae SERF. <i> Liu Y, Wang C, Jin Y, Jiang G, He L, Liu M. </i> Biomol NMR Assign, 2022","date":"2023-01-16T14:08:45.534Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.5,"statements":[{"type":"Article","text":"The limited dispersion of the 1 H–15 N HSQC peaks, especially in the 1 H dimension (between 7.6 and 8.5 ppm), indicated at least part of the ScSERF segments was in an unfolded state in the NMR experimental buffer condition (20mM phosphate, 50mM NaCl, pH 6.5)."}]},{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":null,"value":298,"statements":[{"type":"Article","text":"All NMR experiments were recorded at 298 K on a 600 MHz Bruker Avance spectrometer equipped with a triple-resonance cryogenic probe."}]}],"cross_refs":[{"db":"BMRB","id":"51051"},{"db":"BMRB","id":"51287"}],"region_id":"DP03916r001","statement":[{"text":"The limited dispersion of the 1 H–15 N HSQC peaks, especially in the 1 H dimension (between 7.6 and 8.5 ppm), indicated at least part of the ScSERF segments was in an unfolded state in the NMR experimental buffer condition (20mM phosphate, 50mM NaCl, pH 6.5). In a next step, secondary chemical shift deviations were calculated and are shown in Fig. 3. Consistent with the dispersion of peaks in 1 H dimension, the N terminal segments of residues 1–35 yielded a secondary chemical shift deviation close to 0, corresponding to a random coil structure. However, the segment of residues spanning 36–65 showed a clear helical secondary structure propensity based on its consecutive positive secondary chemical shift deviation.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-19T18:04:13.295Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MARGNQRDLARQKNLKKQKDMAKNQKKSGDPKKRMESDAEILRQKQAAADARREAEKLEKLKAEKTRR","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0,"disorder_content":0.5147058823529411,"disprot_consensus":{"full":[{"start":1,"end":35,"type":"D"}],"Structural state":[{"start":1,"end":35,"type":"D"}]}},{"disprot_id":"DP03917","acc":"Q14011","creator":"viglesias","date":"2023-01-16T12:36:10.687Z","features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":8,"end":78}],"gene3D":[]},"genes":[{"name":{"value":"CIRBP"},"synonyms":[{"value":"A18HNRNP"},{"value":"CIRP"}]}],"length":172,"name":"Cold-inducible RNA-binding protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":90,"end":172,"reference_id":"36539586","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>13</sup>C, and <sup>15</sup>N assignments of the mRNA binding protein hnRNP A18. <i> Coburn KM, Roth B, Varney KM, Carrier F, Weber DJ. </i> Biomol NMR Assign, 2022","date":"2023-01-16T14:08:00.909Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":5.2,"statements":[{"type":"Article","text":"The 2D 1 H,15 N-edited HSQC spectrum of hnRNP A18 (residues 1-172) was recorded on a Bruker 600 MHz spectrometer at pH 5.2 and 25 oC."}]},{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Article","text":"The 2D 1 H,15 N-edited HSQC spectrum of hnRNP A18 (residues 1-172) was recorded on a Bruker 600 MHz spectrometer at pH 5.2 and 25 oC."}]}],"cross_refs":[{"db":"BMRB","id":"51517"}],"region_id":"DP03917r001","statement":[{"text":"The IDD of hnRNP A18 (aa. 90–172) contained chemical shift values consistent with random coil and did not suggest strong secondary structural characteristics at any location. In accordance with chemical shifts suggestive of random coil, the Random Coil Index (RCI) order parameter (RCI-S2) values for the IDD were lower than the values for the RRM. This analyses suggests the backbone of the IDD is significantly more flexible than the backbone of the RRM.","type":"Article"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Article","text":"His6-hnRNP A18 expression was induced by the addition of 1 mM IPTG (isopropyl-β-D-1-thiogalactopyranoside), and cells were grown for an additional 16 h."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-19T18:06:27.513Z"}}],"regions_counter":2,"released":"2023_12","sequence":"MASDEGKLFVGGLSFDTNEQSLEQVFSKYGQISEVVVVKDRETQRSRGFGFVTFENIDDAKDAMMAMNGKSVDGRQIRVDQAGKSSDNRSRGYRGGSAGGRGFFRGGRGRGRGFSRGGGDRGYGGNRFESRSGGYGGSRDYYSSRSQSGGYSDRSSGGSYRDSYDSYATHNE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.4069767441860465,"dataset":["Condensates-related proteins","RNA-binding proteins","Stress response proteins"],"disorder_content":0.48255813953488375,"disprot_consensus":{"full":[{"start":90,"end":172,"type":"D"}],"Structural state":[{"start":90,"end":172,"type":"D"}]}},{"disprot_id":"DP03919","acc":"O15151","creator":"rpancsa","date":"2023-01-16T13:48:15.839Z","features":{"pfam":[{"id":"PF00641","name":"Zn-finger in Ran binding protein and others","start":300,"end":329},{"id":"PF13920","name":"Zinc finger, C3HC4 type (RING finger)","start":436,"end":482}],"gene3D":[]},"genes":[{"name":{"value":"MDM4"},"synonyms":[{"value":"MDMX"}]}],"length":490,"name":"Protein Mdm4","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":181,"end":300,"reference_id":"35359247","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>15</sup>N and <sup>13</sup>C backbone resonance assignments of the acidic domain of the human MDMX protein. <i> Song Q, Liu XQ, Rainey JK. </i> Biomol NMR Assign, 2022","date":"2023-01-16T14:11:33.466Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":7,"statements":[{"type":"Article","text":"Samples were dialyzed against NMR buffer (20 mM NaH2PO4, 40 mM NaCl, pH 7.0 (uncorrected for deuterium isotope effects)) overnight at room temperature (RT ~ 21 °C)."}]},{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":"within normal range","value":293,"statements":[{"type":"Article","text":"NMR spectra were recorded at 293 K on a Bruker NMR spectrometer (Avance III HD 800 MHz) equipped with a Bruker 5 mm TCI z-axis gradient cryogenic probe."}]}],"cross_refs":[{"db":"BMRB","id":"51090"}],"region_id":"DP03919r001","statement":[{"text":"The chemical shift data are consistent with a scenario where the AD is an intrinsically disordered region, as the sequence has significant random-coil propensity.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-19T18:07:49.893Z"}},{"start":181,"end":300,"reference_id":"35359247","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>15</sup>N and <sup>13</sup>C backbone resonance assignments of the acidic domain of the human MDMX protein. <i> Song Q, Liu XQ, Rainey JK. </i> Biomol NMR Assign, 2022","date":"2023-01-16T14:01:10.923Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":7,"statements":[{"type":"Article","text":"Samples were dialyzed against NMR buffer (20 mM NaH2PO4, 40 mM NaCl, pH 7.0 (uncorrected for deuterium isotope effects)) overnight at room temperature (RT ~ 21 °C)."}]},{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":"within normal range","value":293,"statements":[{"type":"Article","text":"NMR spectra were recorded at 293 K on a Bruker NMR spectrometer (Avance III HD 800 MHz) equipped with a Bruker 5 mm TCI z-axis gradient cryogenic probe."}]}],"cross_refs":[{"db":"BMRB","id":"51090"}],"region_id":"DP03919r002","statement":[{"text":"The 1H-15N HSQC spectrum exhibits narrow dispersion in the proton dimension (Fig. 3). This is characteristic of an intrinsically disordered protein, with most resonances occupying the central part of the spectrum.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-19T18:07:52.494Z"}},{"start":181,"end":300,"reference_id":"35359247","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>15</sup>N and <sup>13</sup>C backbone resonance assignments of the acidic domain of the human MDMX protein. <i> Song Q, Liu XQ, Rainey JK. </i> Biomol NMR Assign, 2022","date":"2023-01-16T14:04:07.689Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":20,"statements":[{"type":"Article","text":"Far-UV CD spectra for the AD were recorded at 20 °C using a DSM 20 CD spectrophotometer (Olis)."}]}],"region_id":"DP03919r003","statement":[{"text":"The far-UV CD spectra of intrinsically disordered proteins typically have a negative band at ~ 200 nm and an ellipticity close to zero at 222 nm, features that are distinct from folded proteins and which make it possible to identify partially or fully disordered proteins. Consistent with this, the CD spectrum of the AD exhibited a strong negative band at ~ 202 nm, suggesting that the AD contains a significant proportion of disordered content.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-19T18:07:53.450Z"}}],"regions_counter":3,"released":"2023_12","sequence":"MTSFSTSAQCSTSDSACRISPGQINQVRPKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGELLGRQSFSVKDPSPLYDMLRKNLVTLATATTDAAQTLALAQDHSMDIPSQDQLKQSAEESSTSRKRTTEDDIPTLPTSEHKCIHSREDEDLIENLAQDETSRLDLGFEEWDVAGLPWWFLGNLRSNYTPRSNGSTDLQTNQDVGTAIVSDTTDDLWFLNESVSEQLGVGIKVEAADTEQTSEEVGKVSDKKVIEVGKNDDLEDSKSLSDDTDVEVTSEDEWQCTECKKFNSPSKRYCFRCWALRKDWYSDCSKLTHSLSTSDITAIPEKENEGNDVPDCRRTISAPVVRPKDAYIKKENSKLFDPCNSVEFLDLAHSSESQETISSMGEQLDNLSEQRTDTENMEDCQNLLKPCSLCEKRPRDGNIIHGRTGHLVTCFHCARRLKKAGASCPICKKEIQLVIKVFIA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.5510204081632653,"dataset":["Cancer-related proteins"],"disorder_content":0.24489795918367346,"disprot_consensus":{"full":[{"start":181,"end":300,"type":"D"}],"Structural state":[{"start":181,"end":300,"type":"D"}]}},{"disprot_id":"DP03920","acc":"D8SB57","creator":"rpancsa","date":"2023-01-18T07:27:38.223Z","features":{"pfam":[{"id":"PF00642","name":"Zinc finger C-x8-C-x5-C-x3-H type (and similar)","start":11,"end":37},{"id":"PF00642","name":"Zinc finger C-x8-C-x5-C-x3-H type (and similar)","start":49,"end":73}],"gene3D":[]},"genes":[{"orfNames":[{"value":"SELMODRAFT_112852","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EFJ18334.1","url":"https://www.ebi.ac.uk/ena/browser/view/EFJ18334.1"}}]}]}],"length":119,"name":"C3H1-type domain-containing protein","ncbi_taxon_id":88036,"organism":"Selaginella moellendorffii","regions":[{"start":39,"end":52,"reference_id":"35279790","reference_source":"pmid","reference_html":"Backbone and sidechain <sup>1</sup>H, <sup>15</sup>N and <sup>13</sup>C resonance assignments of the free and RNA-bound tandem zinc finger domain of the tristetraprolin family member from Selaginella moellendorffii. <i> Hicks SN, Venters RA, Blackshear PJ. </i> Biomol NMR Assign, 2022","date":"2023-01-18T07:37:21.545Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Article","text":"Three additional residues, serine, asparagine, and alanine, are added to the N-terminus of the TZF domain, due to a TEV cleavage site that was introduced for removal of a tandem 6 residue histidine and MBP tag for affinity purification."}]}],"cross_refs":[{"db":"BMRB","id":"51209"},{"db":"BMRB","id":"51210"}],"region_id":"DP03920r001","sequence_construct":"SNALYKTELCRSWEETGSCRYGNKCQFAHGKEDLRPVNRHPKYKTEVCRTFSAAGTCPYGKRCRFIHATP","statement":[{"text":"Furthermore, the linker region between the two fingers in the TZF domain of spikemoss is unstructured (residues D39 - E52), in both the presence and absence of RNA, similar to the linker region in the TIS11d-RNA complex (Fig. 2).","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-19T18:09:09.127Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MAEESDASKLYKTELCRSWEETGSCRYGNKCQFAHGKEDLRPVNRHPKYKTEVCRTFSAAGTCPYGKRCRFIHATPKLSDVKLPPLVAPAMNLTKLLLHDNAAAMAPRSRLPVFREICL","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Lycopodiopsida","Selaginellales","Selaginellaceae","Selaginella"],"alphafold_very_low_content":0.025210084033613446,"disorder_content":0.11764705882352941,"disprot_consensus":{"full":[{"start":39,"end":52,"type":"D"}],"Structural state":[{"start":39,"end":52,"type":"D"}]}},{"disprot_id":"DP03921","acc":"A5Y0M2","creator":"rpancsa","date":"2023-01-18T08:43:27.456Z","features":{"pfam":[],"gene3D":[]},"genes":[],"length":270,"name":"B6 protein","ncbi_taxon_id":2730554,"organism":"Trichonephila antipodiana","regions":[{"start":92,"end":112,"reference_id":"34436735","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>15</sup>N and <sup>13</sup>C resonance assignments of a repetitive domain of tubuliform spidroin 2. <i> Fan T, Zhang Y, Fan JS, Yuan W, Lin Z. </i> Biomol NMR Assign, 2021","date":"2023-01-18T08:51:51.411Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":"within normal range","value":300,"statements":[{"type":"Figure","text":"1H–15N HSQC spectrum of TuSp2-RP acquired at 800 MHz and 300 K."}]}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Article","text":"The recombinant protein has a 6 × His tag (MHHHHHHSSGLVPRGS) at the N-terminus."}]}],"cross_refs":[{"db":"BMRB","id":"36395"}],"region_id":"DP03921r001","sequence_construct":"MHHHHHHSSGLVPRGSNLSIGDTTSIIQLFKNFTGPPSVATFISNFHSIVQSSKTLLNLFDVAEENPLEFAKCMYELVLKSANSLGVLNPHLIANNIYQSVVSNLDILHSSAMVNLYANAMAGSLFLEGILNSDNAATLAKKCANDMEAFAKKMVEIG","statement":[{"text":"Analysis of Cα and Cβ chemical shifts indicated that TuSp2-RP consists of at least six α-helices (Fig. 2) and the first 37-residues (including the His-tag) exist in a random coil form.","type":"Article"},{"text":"Excluding the first 16 residues of the N-terminal His-tag and the four proline residues from the 158-residue recombinant TuSp2-RP sequence, 132 out of a total of 138 residues (~ 96%) were assigned in the 1H–15N HSQC spectrum.","type":"Article"},{"text":"The authors specify that the construct has a 16 residue N-terminal His tag, then they claim that the first 37-residues (including the His-tag) are disordered, therefore the first 21 residues of the protein construct are disordered that is residues 92-112 of the UniProt sequence.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-19T18:09:50.191Z"}}],"regions_counter":1,"released":"2024_06","sequence":"EFAKCMYELVLKSANSLGVLNPHLIANNIYQSIVSNLDILHSSVMINLYANAMARNLFHEGFLNLDNAATLAKKCANDMEAFAKKMVETGPNLSIGDTTSIIQLFKNFTGPPSVATFISNFHSIVQSSKTLLNLFDVAEENPLEFAKCMYELVLKSANSLGVLNPHLIANNIYQSVVSNLDILHSSAMVNLYANAMAGSLFLEGILNSDNAATLAKKCANDMEAFAKKMVEIGNSISNIQDFPDVSARILGNLSLPLLDDVLDLLSSFLP","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Chelicerata","Arachnida","Araneae","Araneomorphae","Entelegynae","Araneoidea","Nephilidae","Trichonephila"],"alphafold_very_low_content":0.8407407407407408,"disorder_content":0.07777777777777778,"disprot_consensus":{"full":[{"start":92,"end":112,"type":"D"}],"Structural state":[{"start":92,"end":112,"type":"D"}]}},{"disprot_id":"DP03922","acc":"Q13586","creator":"rpancsa","date":"2023-01-18T09:02:58.216Z","features":{"pfam":[{"id":"PF07647","name":"SAM domain (Sterile alpha motif)","start":131,"end":194},{"id":"PF16533","name":"STIM1 Orai1-activating region","start":341,"end":441},{"id":"PF25578","name":"Stromal interaction molecule 1-like, EF-hand","start":47,"end":125}],"gene3D":[]},"genes":[{"name":{"value":"STIM1"},"synonyms":[{"value":"GOK","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9377559","url":"http://www.ncbi.nlm.nih.gov/pubmed/9377559","alternativeUrl":"https://europepmc.org/abstract/MED/9377559"}}]}]}],"length":685,"name":"Stromal interaction molecule 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":395,"end":404,"reference_id":"34417953","reference_source":"pmid","reference_html":"Resonance assignment of coiled-coil 3 (CC3) domain of human STIM1. <i> Gupta A, Kitzler CM, Rathner P, Fahrner M, Grabmayr H, Rathner A, Romanin C, Müller N. </i> Biomol NMR Assign, 2021","date":"2023-01-18T09:20:07.523Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6,"statements":[{"type":"Figure","text":"Assigned 1H–15 N HSQC spectrum of human wild-type STIM1 CC3 acquired in 20 mM Bis–Tris, 17.5 % TFE, pH 6.0 at 310 K at a protein concentration of 0.5 mM."}]},{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":"increased","value":310,"statements":[{"type":"Figure","text":"Assigned 1H–15 N HSQC spectrum of human wild-type STIM1 CC3 acquired in 20 mM Bis–Tris, 17.5 % TFE, pH 6.0 at 310 K at a protein concentration of 0.5 mM."}]}],"cross_refs":[{"db":"BMRB","id":"50683"}],"region_id":"DP03922r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":"increased","value":null,"db":"ChEBI","id":"42330","statements":[{"type":"Article","text":"Finally, the aggregation tendency of the CC3 domain was overcome upon addition of 17.5 % v/v 2,2,2-TFE at 310 K."}],"entry_name":"2,2,2-trifluoroethanol"}],"statement":[{"text":"The main structural features are a short (single turn) α-helix at the N-terminus followed by approximately 10 amino acids in a disordered loop region (H395 to D404) and a longer (ca. 6 turn) α-helix (V405 to L427). ","type":"Article"},{"text":"In the monomeric state, a short disordered segment (H395 to D404) interrupts the α-helix close to the N-terminus.","type":"Conclusion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-19T18:10:05.609Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MDVCVRLALWLLWGLLLHQGQSLSHSHSEKATGTSSGANSEESTAAEFCRIDKPLCHSEDEKLSFEAVRNIHKLMDDDANGDVDVEESDEFLREDLNYHDPTVKHSTFHGEDKLISVEDLWKAWKSSEVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFGPPLLTRHNHLKDFMLVVSIVIGVGGCWFAYIQNRYSKEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTAALRERLHRWQQIEILCGFQIVNNPGIHSLVAALNIDPSWMGSTRPNPAHFIMTDDVDDMDEEIVSPLSMQSPSLQSSVRQRLTEPQHGLGSQRDLTHSDSESSLHMSDRQRVAPKPPQMSRAADEALNAMTSNGSHRLIEGVHPGSLVEKLPDSPALAKKALLALNHGLDKAHSLMELSPSAPPGGSPHLDSSRSHSPSSPDPDTPSPVGDSRALQASRNTRIPHLAGKKAVAEEDNGSIGEETDSSPGRKKFPLKIFKKPLKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.345985401459854,"disorder_content":0.014598540145985401,"disprot_consensus":{"full":[{"start":395,"end":404,"type":"D"}],"Structural state":[{"start":395,"end":404,"type":"D"}]}},{"disprot_id":"DP03923","acc":"Q9R825","creator":"rpancsa","date":"2023-01-18T09:56:02.097Z","features":{"pfam":[{"id":"PF02352","name":"Decorin binding protein","start":6,"end":147}],"gene3D":[]},"genes":[{"name":{"value":"p17","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAA10544.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA10544.1"}}]}}],"length":150,"name":"p17 protein","ncbi_taxon_id":29518,"organism":"Borreliella afzelii","regions":[{"start":31,"end":48,"reference_id":"34357583","reference_source":"pmid","reference_html":"Resonance assignment and secondary structure of DbpA protein from the European species, Borrelia afzelii. <i> Hejduk L, Rathner P, Strnad M, Grubhoffer L, Sterba J, Rego ROM, Müller N, Rathner A. </i> Biomol NMR Assign, 2021","date":"2023-01-18T10:14:50.692Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The gene coding sequence for DbpA from B. afzelii (strain A91) without the transmembrane part of the protein was cloned into pQE30 plasmid, which includes the sequence for His6 tag directly attached to N-terminus of the protein (full amino acid sequence of the recombinant protein can be found in Fig. 2a)."}]}],"cross_refs":[{"db":"BMRB","id":"50751"}],"region_id":"DP03923r001","sequence_construct":"HHHHHHGSSLTGKARLESSVKDITNEIEKAIKEAEDAGVKTDAFTETQTGGKVGGSQIRAAKIRVADLTIKFLEATEEETITFKENGAGEEDFSGIYDLILNAAKAVEKIGMQGMKQAVEEAAKEKPKTTADGIIAIVKVMKAKVENIKEKQTKNQK","statement":[{"text":"The longest loop (res. G38 – G55) of B. afzelii DbpA contains a small approx. one-turn alpha helix just like DbpA from B. burgdorferi s.s., whereas in the more sequentially related B. garinii DbpA one found a long alpha helix in the same place.","type":"Article"},{"text":"The authors apply an 8 aa long His tag in place of the initiating Met residue, therefore their numbering is shifted by 7 residues. G38-G55 corresponds to G31-G48 in the UniProt sequence. ","type":"Curator statement"},{"text":"Besides the statement of the authors that the region is a loop, there are also markedly decreased RCI S2 values, R1/R2 values and N{H} NOE values in this region as shown in Figure 2b and c, especially between residues 33 and 48.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-19T18:11:08.833Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MSLTGKARLESSVKDITNEIEKAIKEAEDAGVKTDAFTETQTGGKVGGSQIRAAKIRVADLTIKFLEATEEETITFKENGAGEEDFSGIYDLILNAAKAVEKIGMQGMKQAVEEAAKEKPKTTADGIIAIVKVMKAKVENIKEKQTKNQK","taxonomy":["Bacteria","Spirochaetes","Spirochaetales","Borreliaceae","Borreliella"],"alphafold_very_low_content":0.04,"disorder_content":0.12,"disprot_consensus":{"full":[{"start":31,"end":48,"type":"D"}],"Structural state":[{"start":31,"end":48,"type":"D"}]}},{"disprot_id":"DP03924","acc":"P78352","creator":"rpancsa","date":"2023-01-18T12:50:17.613Z","features":{"pfam":[{"id":"PF00018","name":"SH3 domain","start":434,"end":490},{"id":"PF00595","name":"PDZ domain","start":65,"end":149},{"id":"PF00595","name":"PDZ domain","start":161,"end":243},{"id":"PF00595","name":"PDZ domain","start":314,"end":388},{"id":"PF00625","name":"Guanylate kinase","start":534,"end":710},{"id":"PF10600","name":"PDZ-associated domain of NMDA receptors","start":245,"end":312},{"id":"PF10608","name":"Polyubiquitination (PEST) N-terminal domain of MAGUK","start":31,"end":64}],"gene3D":[]},"genes":[{"name":{"value":"DLG4","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:2903","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:2903"}}]},"synonyms":[{"value":"PSD95"}]}],"length":724,"name":"Disks large homolog 4","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":71,"reference_id":"33929702","reference_source":"pmid","reference_html":"Chemical shift assignments of the N-terminal domain of PSD95 (PSD95-NT). <i> Zhang Y, Hell JW, Ames JB. </i> Biomol NMR Assign, 2021","date":"2023-01-18T13:01:06.231Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"decreased","value":5,"statements":[{"type":"Methods","text":"Protein samples of 15 N- or 13C/15 N-labeled PSD95-NT were exchanged into NMR buffer containing 25 mM CD3COONa (pH 5.0) with 1 mM EDTA-d12, 1 mM DTT-d10 and 95% H2O/5% D2O."}]},{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":"within normal range","value":285,"statements":[{"type":"Methods","text":"All NMR experiments were performed at 285 K on a Bruker Avance III 800 MHz spectrometer equipped with a four-channel interface and triple resonance cryogenic (TCI) probe."}]}],"cross_refs":[{"db":"BMRB","id":"50752"}],"region_id":"DP03924r001","statement":[{"text":"The amide proton chemical shifts exhibited very narrow chemical shift dispersion (within 8.0–8.7 ppm), suggesting a solvent exposed random coil conformation for the entire 71-residue peptide chain, which is consistent with a lack of any ring-current shifted amide or methyl resonances.","type":"Article"},{"text":"The secondary structure of PSD95-NT in the absence of calmodulin (calculated by chemical shift index (Wishart et al. 1992)) indicates a random coil conformation for the entire 71-residue peptide (Fig. 2) that we suggest may increase the exposure and availability of Cys3 and Cys5 for palmitoylation by palmitoyl transferase enzymes.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-19T18:11:18.083Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MDCLCIVTTKKYRYQDEDTPPLEHSPAHLPNQANSPPVIVNTDTLEAPGYELQVNGTEGEMEYEEITLERGNSGLGFSIAGGTDNPHIGDDPSIFITKIIPGGAAAQDGRLRVNDSILFVNEVDVREVTHSAAVEALKEAGSIVRLYVMRRKPPAEKVMEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAHKDGRLQIGDKILAVNSVGLEDVMHEDAVAALKNTYDVVYLKVAKPSNAYLSDSYAPPDITTSYSQHLDNEISHSSYLGTDYPTAMTPTSPRRYSPVAKDLLGEEDIPREPRRIVIHRGSTGLGFNIVGGEDGEGIFISFILAGGPADLSGELRKGDQILSVNGVDLRNASHEQAAIALKNAGQTVTIIAQYKPEEYSRFEAKIHDLREQLMNSSLGSGTASLRSNPKRGFYIRALFDYDKTKDCGFLSQALSFRFGDVLHVIDASDEEWWQARRVHSDSETDDIGFIPSKRRVERREWSRLKAKDWGSSSGSQGREDSVLSYETVTQMEVHYARPIIILGPTKDRANDDLLSEFPDKFGSCVPHTTRPKREYEIDGRDYHFVSSREKMEKDIQAHKFIEAGQYNSHLYGTSVQSVREVAEQGKHCILDVSANAVRRLQAAHLHPIAIFIRPRSLENVLEINKRITEEQARKAFDRATKLEQEFTECFSAIVEGDSFEEIYHKVKRVIEDLSGPYIWVPARERL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Condensates-related proteins"],"alphafold_very_low_content":0.19751381215469613,"disorder_content":0.09806629834254144,"disprot_consensus":{"full":[{"start":1,"end":71,"type":"D"}],"Structural state":[{"start":1,"end":71,"type":"D"}]}},{"disprot_id":"DP03925","acc":"Q4Q5U3","creator":"rpancsa","date":"2023-01-18T15:54:58.796Z","features":{"pfam":[{"id":"PF00289","name":"Biotin carboxylase, N-terminal domain","start":13,"end":121},{"id":"PF00364","name":"Biotin-requiring enzyme","start":618,"end":682},{"id":"PF02785","name":"Biotin carboxylase C-terminal domain","start":353,"end":464},{"id":"PF02786","name":"Carbamoyl-phosphate synthase L chain, ATP binding domain","start":127,"end":339}],"gene3D":[]},"genes":[{"orfNames":[{"value":"LMJF_31_3130","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAJ08598.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAJ08598.1"}}]}]}],"length":687,"name":"Methylcrotonoyl-coa carboxylase biotinylated subunitprotein-like protein","ncbi_taxon_id":5664,"organism":"Leishmania major","regions":[{"start":602,"end":617,"reference_id":"33751378","reference_source":"pmid","reference_html":"Chemical shift assignments of the biotin carboxyl carrier protein domain of L. major Methylcrotonyl-CoA carboxylase. <i> Rajak MK, Sundd M. </i> Biomol NMR Assign, 2021","date":"2023-01-18T16:11:59.589Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":8,"statements":[{"type":"Figure","text":"1H15N HSQC spectrum of the L. major MCCC BCCP domain at pH 8.0, 25 °C."}]},{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Figure","text":"1H15N HSQC spectrum of the L. major MCCC BCCP domain at pH 8.0, 25 °C."}]}],"cross_refs":[{"db":"BMRB","id":"50309"}],"region_id":"DP03925r001","sequence_construct":"MLTDGFGDASMAGGTSAKIVSPMPGKVSKFLVNSGDFVEKGQALMIVEAMKMEHPVKALQDGQVSFLVKEGEVVGSDHVLATVVQKE","statement":[{"text":"However, of the 87 non proline residues expressed, only 66 amide peaks were visible in the HSQC spectrum, (Fig. 2), suggesting that the first 16 residues are not structured. Consequently, the backbone amides for the first 16 residues, 3 prolines (namely Pro 22, Pro 24, and Pro 55) could not be observed in the 15N HSQC.","type":"Article"},{"text":"Interestingly, the first 16 residues predicted to form a helix in LmMCCC BCCP were not visible in the 1H15N HSQC spectrum, at pH 8.0, which led us to speculate that the region is probably not folded.","type":"Article"},{"text":"Moreover, the amino acid sequence of LmMCCC BCCP domain (2LTDGFGDASMAGGTSA16) also suggests that the region should be unstructured, as there are numerous glycines present, that are established helix breakers.","type":"Article"},{"text":"The authors used a construct where the residues 602-687 of the protein are preceded by a single Met residue. Their numbering is valid for their construct, so it has to be shifted by 600 to get the corresponding UniProt positions.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-19T18:11:45.427Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MLRRTDRCGQRKVEKLLVANRGEIACRVFRTCREMHIRTVALFCEAERNAKHVVEADEAVCIGPPPAVNSYLRGDHIISVAKQLNVDAIHPGYGFLSENADFAEAVTRSGIEFIGPPASAISLMGSKSESKRIMEAAGVPVVPGYYGENQNVSFLAEEANRVGFPILIKAVSGGGGKGMKIVERPEDFAFMLESAKREAANFFKDDRVILERYVKRPRHIECQIFFDKHGRGVFFFERDCSVQRRYQKVLEEAPAPHLSMEMRQRIGEVALQAAKAVGYVGAGTVEFIFDTSTGDFYFMEMNTRLQVEHPVTEEVCRIKGAPLDLVKLQIKTAMGKPLTFSQEDVALVGSCIEARVYAESPERGFLPESGPLTFIREPFQGVRGPTRTRLDTGFCEGDNVLIHYDPMLAKVISWGRNREDALKGLRQALGEYKVAGINTNIEFLKRCCEAPEFARGGVTTNFISEHEKQLLNAPAVTPKVAAMAATAWLLNRCDNWRGAFRLNGDTSATVHFYIDNRPVEVRLHTEGANYHKIFFSVWDHEGSFAVGSGPVTSKHRDQRSIVNGFTFLFENGMRHTVLAVATEGDVTIIGSFGLHQIRLLPLTDGFGDASMAGGTSAKIVSPMPGKVSKFLVNSGDFVEKGQALMIVEAMKMEHPVKALQDGQVSFLVKEGEVVGSDHVLATVVQKE","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"alphafold_very_low_content":0.03784570596797671,"disorder_content":0.023289665211062592,"disprot_consensus":{"full":[{"start":602,"end":617,"type":"D"}],"Structural state":[{"start":602,"end":617,"type":"D"}]}},{"disprot_id":"DP03926","acc":"P81274","creator":"fkordevani","date":"2023-01-18T16:20:08.277Z","features":{"pfam":[{"id":"PF02188","name":"GoLoco motif","start":490,"end":509},{"id":"PF02188","name":"GoLoco motif","start":545,"end":566},{"id":"PF02188","name":"GoLoco motif","start":595,"end":615},{"id":"PF02188","name":"GoLoco motif","start":629,"end":650},{"id":"PF13176","name":"Tetratricopeptide repeat","start":204,"end":238},{"id":"PF13181","name":"Tetratricopeptide repeat","start":323,"end":353},{"id":"PF13374","name":"Tetratricopeptide repeat","start":63,"end":93},{"id":"PF13424","name":"Tetratricopeptide repeat","start":102,"end":157},{"id":"PF13424","name":"Tetratricopeptide repeat","start":243,"end":314}],"gene3D":[]},"genes":[{"name":{"value":"GPSM2"},"synonyms":[{"value":"LGN"}]}],"length":684,"name":"G-protein-signaling modulator 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":355,"end":421,"reference_id":"25664792","reference_source":"pmid","reference_html":"Structural basis for the recognition of the scaffold protein Frmpd4/Preso1 by the TPR domain of the adaptor protein LGN. <i> Takayanagi H, Yuzawa S, Sumimoto H. </i> Acta Crystallogr F Struct Biol Commun, 2015","date":"2023-02-13T10:39:28.349Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4WNG"},{"db":"PDB","id":"4WNE"},{"db":"PDB","id":"4WND"}],"region_id":"DP03926r001","statement":[{"text":"Apart from the capping helix next to TPR8, which is visible in the LGN–mInsc complex (Yuzawa et al., 2011 ) but not in the LGN–Frmpd4 complex (Fig. 5 a), they share a similar TPR structure, with r.m.s.d.s of 0.87 Å for TPR2–6 (204 Cα atoms) and 2.38 Å for TPR1–8 (320 Cα atoms).","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q14CM0"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-13T16:12:49.235Z"}},{"start":275,"end":421,"reference_id":"25664792","reference_source":"pmid","reference_html":"Structural basis for the recognition of the scaffold protein Frmpd4/Preso1 by the TPR domain of the adaptor protein LGN. <i> Takayanagi H, Yuzawa S, Sumimoto H. </i> Acta Crystallogr F Struct Biol Commun, 2015","date":"2023-02-13T10:38:03.523Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4WNF"}],"region_id":"DP03926r002","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered. Furthermore, it should be noted the crystal structure describes the protein in oxidized form. ","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q14CM0"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-13T16:12:49.836Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MEENLISMREDHSFHVRYRMEASCLELALEGERLCKSGDCRAGVSFFEAAVQVGTEDLKTLSAIYSQLGNAYFYLHDYAKALEYHHHDLTLARTIGDQLGEAKASGNLGNTLKVLGNFDEAIVCCQRHLDISRELNDKVGEARALYNLGNVYHAKGKSFGCPGPQDVGEFPEEVRDALQAAVDFYEENLSLVTALGDRAAQGRAFGNLGNTHYLLGNFRDAVIAHEQRLLIAKEFGDKAAERRAYSNLGNAYIFLGEFETASEYYKKTLLLARQLKDRAVEAQSCYSLGNTYTLLQDYEKAIDYHLKHLAIAQELNDRIGEGRACWSLGNAYTALGNHDQAMHFAEKHLEISREVGDKSGELTARLNLSDLQMVLGLSYSTNNSIMSENTEIDSSLNGVRPKLGRRHSMENMELMKLTPEKVQNWNSEILAKQKPLIAKPSAKLLFVNRLKGKKYKTNSSTKVLQDASNSIDHRIPNSQRKISADTIGDEGFFDLLSRFQSNRMDDQRCCLQEKNCHTASTTTSSTPPKMMLKTSSVPVVSPNTDEFLDLLASSQSRRLDDQRASFSNLPGLRLTQNSQSVLSHLMTNDNKEADEDFFDILVKCQGSRLDDQRCAPPPATTKGPTVPDEDFFSLILRSQGKRMDEQRVLLQRDQNRDTDFGLKDFLQNNALLEFKNSGKKSADH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.46637426900584794,"disorder_content":0.2149122807017544,"disprot_consensus":{"full":[{"start":275,"end":421,"type":"D"}],"Structural state":[{"start":275,"end":421,"type":"D"}]}},{"disprot_id":"DP03927","acc":"W1J0W9","creator":"rpancsa","date":"2023-01-18T16:30:36.436Z","features":{"pfam":[{"id":"PF00501","name":"AMP-binding enzyme","start":483,"end":837},{"id":"PF00550","name":"Phosphopantetheine attachment site","start":999,"end":1063},{"id":"PF00668","name":"Condensation domain","start":10,"end":463},{"id":"PF13193","name":"AMP-binding enzyme C-terminal domain","start":896,"end":971}],"gene3D":[]},"genes":[{"name":{"value":"paxA","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CDL83105.1","url":"https://www.ebi.ac.uk/ena/browser/view/CDL83105.1"}}]},"orfNames":[{"value":"XCR1_180002","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CDL83105.1","url":"https://www.ebi.ac.uk/ena/browser/view/CDL83105.1"}}]}]}],"length":1084,"name":"Peptide synthetase PaxA","ncbi_taxon_id":1427517,"organism":"Xenorhabdus cabanillasii JM26","regions":[{"start":982,"end":1027,"reference_id":"33675014","reference_source":"pmid","reference_html":"NMR resonance assignments for a docking domain pair with an attached thiolation domain from the PAX peptide-producing NRPS from Xenorhabdus cabanillasii. <i> Watzel J, Sarawi S, Duchardt-Ferner E, Bode HB, Wöhnert J. </i> Biomol NMR Assign, 2021","date":"2023-01-18T16:41:11.106Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":"within normal range","value":293,"statements":[{"type":"Figure","text":"The spectra were recorded at 293 K on a 600 MHz Bruker Avance III spectrometer. "}]}],"cross_refs":[{"db":"BMRB","id":"50594"},{"db":"BMRB","id":"34575"}],"region_id":"DP03927r001","statement":[{"text":"No backbone amide signals were detectable for residues H982 and S1027 most likely due to fast exchange of the respective amide protons with the solvent or due to conformational exchange.","type":"Article"},{"text":"The backbone resonances of PaxA T1-CDD bound to the PaxB NDD could be assigned with the same degree of completeness as for the free protein. All expected backbone amide signals except those for H982 and S1027 (99/101, 98.0%; Fig. ​Fig.2a,2a, top) and all Cα (104/104), 99% of all Cβ (99/100), 95% of all CO (99/104), all Hα (104/104) and 99% of all Hβ (99/100) chemical shifts were assigned.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-19T18:12:39.137Z"}},{"start":1070,"end":1084,"reference_id":"33675014","reference_source":"pmid","reference_html":"NMR resonance assignments for a docking domain pair with an attached thiolation domain from the PAX peptide-producing NRPS from Xenorhabdus cabanillasii. <i> Watzel J, Sarawi S, Duchardt-Ferner E, Bode HB, Wöhnert J. </i> Biomol NMR Assign, 2021","date":"2023-01-18T16:52:29.344Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":"within normal range","value":293,"statements":[{"type":"Figure","text":"The spectra were recorded at 293 K on a 600 MHz Bruker Avance III spectrometer. "}]}],"cross_refs":[{"db":"BMRB","id":"50594"}],"region_id":"DP03927r002","statement":[{"text":"According to TALOS-N the C-terminus including the predicted CDD of the PaxA T1-CDD construct is unstructured.","type":"Article"},{"text":"The authors do not write down exact boundaries for the disordered C-terminus, but from figure 1a it can be clearly seen that helical propensity drops down at residue 1070 and there are no stable secondary structure elements following it.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-19T18:12:41.591Z"}},{"start":1073,"end":1082,"reference_id":"33675014","reference_source":"pmid","reference_html":"NMR resonance assignments for a docking domain pair with an attached thiolation domain from the PAX peptide-producing NRPS from Xenorhabdus cabanillasii. <i> Watzel J, Sarawi S, Duchardt-Ferner E, Bode HB, Wöhnert J. </i> Biomol NMR Assign, 2021","date":"2023-01-18T16:51:29.041Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":"within normal range","value":293,"statements":[{"type":"Figure","text":"The spectra were recorded at 293 K on a 600 MHz Bruker Avance III spectrometer. "}]}],"cross_refs":[{"db":"BMRB","id":"50594"},{"db":"BMRB","id":"34575"}],"region_id":"DP03927r003","statement":[{"text":"According to TALOS-N the C-terminus including the predicted CDD of the PaxA T1-CDD construct is unstructured.","type":"Article"},{"text":"The authors do not write down exact boundaries for the disordered C-terminus, but from figure 1a it can be clearly seen that helical propensity drops down at residue 1070 and there are no stable secondary structure elements following it.","type":"Curator statement"},{"text":"The analysis of the backbone chemical shifts of the PaxA T1-CDD with TALOS-N in its bound state suggests that its secondary structure is very similar to that in its free state but that there is now an additional α-helix present at the very C-terminus suggesting that the predicted docking domain becomes structured upon binding (Fig. ​(Fig.2a,2a, bottom).","type":"Article"},{"text":"In figure 2a that depics the structural properties of the protein in the complex, a new helix is formed between residues 1073-1082 that was not present in the unbound form (Figure 1a).","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-19T18:12:44.300Z"}},{"start":1073,"end":1082,"reference_id":"33675014","reference_source":"pmid","reference_html":"NMR resonance assignments for a docking domain pair with an attached thiolation domain from the PAX peptide-producing NRPS from Xenorhabdus cabanillasii. <i> Watzel J, Sarawi S, Duchardt-Ferner E, Bode HB, Wöhnert J. </i> Biomol NMR Assign, 2021","date":"2023-01-18T17:03:10.216Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":"within normal range","value":293,"statements":[{"type":"Figure","text":"The spectra were recorded at 293 K on a 600 MHz Bruker Avance III spectrometer. "}]}],"cross_refs":[{"db":"BMRB","id":"34575"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"W1IPT8","operator":null,"partner_start":1,"partner_end":30}],"region_id":"DP03927r004","statement":[{"text":"PaxA T1-CDD and PaxB NDD form a stable 1:1 complex according to analytical gel filtration and NMR titration experiments which is in slow exchange on the NMR time scale. ","type":"Article"},{"text":"The analysis of the backbone chemical shifts of the PaxA T1-CDD with TALOS-N in its bound state suggests that its secondary structure is very similar to that in its free state but that there is now an additional α-helix present at the very C-terminus suggesting that the predicted docking domain becomes structured upon binding (Fig. ​(Fig.2a,2a, bottom).","type":"Article"},{"text":"In figure 2a that depics the structural properties of the protein in the complex, a new helix is formed between residues 1073-1082 that was not present in the unbound form (Figure 1a).","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-19T18:12:46.591Z"}}],"regions_counter":4,"released":"2024_06","sequence":"MNYPDTLKSFALSEAQSSRWFQYQINPAQRGQNNSAFCARVKGLTAEKLEDALNHLIKRHPMLRASFGQYDGKLGYQIAENAVIKITRHNARDLSEETLQQVVRNDCWHAFDLNNPLRVYASWYQCDDQESVMVLTFDHLAVDGWSYWILLEELGKLLTEQELPPAPERSYQDYVIWQQQWLNSNNAKKQQQFWCDNLSGHLTELQLPASNKPVINQSPSATDKITVPGKLSDTLARKLLVMAEKYGNSLFAIFLAAYQILLHRYTGQDDIFIGSIMPGRSRAPWGKLVGEFVNPVALRGQINDEMTVQEHILQAAKTIRQAIENQKYPFPKILEQIKVQRHADTHPVFQTIMTFQQPRYISNLVSLWMDQSSSTTVHWGGAELRSFPYPYYAEMPVPLMVNVIEVDQQINCGFHYDTKLFDAELITQLMNNFFNLLTAMADDEQQTIDSLPLMNESERQRILYNFNATDISYPQNVLLHQLFEQQVNYTPAAIALICDNHQLTYEELNRQANKLAHAFVAAGIQADNRIGLCMERSPEMVIALLGILKAGAAYVPLDPEYPADRLRHILTDSEPALVLSHHGLQSHLPDTSVPLWIWESGEFQATITEQQEDNLSITDLGLTSRNLAYVLYTSGSTGLPKGVMNEHRGIVNRLLWAKDEYQLNPNDLVLQKTPFSFDVSVWEFFLPLLAGAQLVMARPGGHKDPLYLLEEIESRGITTLHFVPSMLQSFIHLTPAERCPSLRQILCSGEALPYSLQQQCLSHFPHSELHNLYGPTEAAIDVTSWRCGSEKYVDLVPIGHPIANTQIYILDKLGRLVPIGVTGEIHIGGIGVARGYLNRPELTAERFVHDPFSNLPDARMYKTGDLGRWLPDGSIDYLGRNDFQVKIRGNRIELEEIETRLAQCAGVQQVVVVARAYDSADTRLIAYIIPQSGTTLNIPELREQLGNSLPDYMIPGAFVMLDTFPLTLSGKLDRRALPIPDHSSVITQEYAAPQGEIEEQLADIWQTILKIDRIGRYDNFFELGGHSLLVLQLQSRINEIFDVDISIQQLFAHPSICQLEECIINAQLLQFDADSLQDIYKSME","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Morganellaceae","Xenorhabdus"],"alphafold_very_low_content":0.03413284132841329,"disorder_content":0.05627306273062731,"disprot_consensus":{"full":[{"start":982,"end":1027,"type":"D"},{"start":1070,"end":1072,"type":"D"},{"start":1073,"end":1082,"type":"T"},{"start":1083,"end":1084,"type":"D"}],"Structural state":[{"start":982,"end":1027,"type":"D"},{"start":1070,"end":1084,"type":"D"}],"Structural transition":[{"start":1073,"end":1082,"type":"T"}],"Molecular function":[{"start":1073,"end":1082,"type":"F"}]}},{"disprot_id":"DP03928","acc":"Q7RTN6","creator":"fkordevani","date":"2023-01-18T16:37:29.479Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":69,"end":379}],"gene3D":[]},"genes":[{"name":{"value":"STRADA"},"synonyms":[{"value":"LYK5","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAP42280.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAP42280.1"}}]},{"value":"STRAD"}]}],"length":431,"name":"STE20-related kinase adapter protein alpha","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":292,"end":347,"reference_id":"19513107","reference_source":"pmid","reference_html":"ATP and MO25alpha regulate the conformational state of the STRADalpha pseudokinase and activation of the LKB1 tumour suppressor. <i> Zeqiraj E, Filippi BM, Goldie S, Navratilova I, Boudeau J, Deak M, Alessi DR, van Aalten DM. </i> PLoS Biol, 2009","date":"2023-02-13T13:17:47.036Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3GNI"}],"region_id":"DP03928r001","statement":[{"text":"STRADα residues 292–347, 383–385, and 402–424, and MO25α residues 337–341 were not associated with clear electron density and were not included in the model.","type":"Methods"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y376"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:311"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5957"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-13T16:19:55.397Z"}},{"start":300,"end":347,"reference_id":"19892943","reference_source":"pmid","reference_html":"Structure of the LKB1-STRAD-MO25 complex reveals an allosteric mechanism of kinase activation. <i> Zeqiraj E, Filippi BM, Deak M, Alessi DR, van Aalten DM. </i> Science, 2009","date":"2023-02-13T16:19:27.279Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2WTK"}],"region_id":"DP03928r002","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y376"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:33113"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15831"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-13T16:24:40.540Z"}},{"start":402,"end":424,"reference_id":"19513107","reference_source":"pmid","reference_html":"ATP and MO25alpha regulate the conformational state of the STRADalpha pseudokinase and activation of the LKB1 tumour suppressor. <i> Zeqiraj E, Filippi BM, Goldie S, Navratilova I, Boudeau J, Deak M, Alessi DR, van Aalten DM. </i> PLoS Biol, 2009","date":"2023-02-13T13:25:59.996Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3GNI"}],"region_id":"DP03928r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y376"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:311"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5957"}],"statement":[{"text":"STRADα residues 292–347, 383–385, and 402–424, and MO25α residues 337–341 were not associated with clear electron density and were not included in the model.","type":"Methods"},{"text":"Whereas clear electron density is present for the last six amino acids of STRADα (residues 426–431, including the WEF motif that interacts with MO25α, Figure S3A), residues 402–425 of STRADα were not visible in the electron density maps, and it was thus not possible to directly identify the appropriate symmetry mates of STRADα and MO25α that make up the biologically relevant binary complex.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-13T16:20:24.283Z"}}],"regions_counter":3,"released":"2023_06","sequence":"MSFLVSKPERIRRWVSEKFIVEGLRDLELFGEQPPGDTRRKTNDASSESIASFSKQEVMSSFLPEGGCYELLTVIGKGFEDLMTVNLARYKPTGEYVTVRRINLEACSNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHFMDGMNELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLRSNLSMISHGQRQRVVHDFPKYSVKVLPWLSPEVLQQNLQGYDAKSDIYSVGITACELANGHVPFKDMPATQMLLEKLNGTVPCLLDTSTIPAEELTMSPSRSVANSGLSDSLTTSTPRPSNGDSPSHPYHRTFSPHFHHFVEQCLQRNPDARPSASTLLNHSFFKQIKRRASEALPELLRPVTPITNFEGSQSQDHSGIFGLVTNLEELEVDDWEF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.21345707656612528,"disorder_content":0.18329466357308585,"disprot_consensus":{"full":[{"start":292,"end":347,"type":"D"},{"start":402,"end":424,"type":"D"}],"Structural state":[{"start":292,"end":347,"type":"D"},{"start":402,"end":424,"type":"D"}]}},{"disprot_id":"DP03929","acc":"Q9U1W1","creator":"fquaglia","date":"2023-01-20T11:43:26.213Z","features":{"pfam":[{"id":"PF00564","name":"PB1 domain","start":13,"end":88}],"gene3D":[]},"genes":[{"name":{"value":"tfg-1","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"Y63D3A.5","url":"https://www.wormbase.org/db/seq/sequence?name=Y63D3A.5;class=Transcript"}}]},"orfNames":[{"value":"Y63D3A.5","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"Y63D3A.5","url":"https://www.wormbase.org/db/seq/sequence?name=Y63D3A.5;class=Transcript"}}]}]}],"length":486,"name":"Protein tfg-1","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":195,"end":486,"reference_id":"25586378","reference_source":"pmid","reference_html":"TFG clusters COPII-coated transport carriers and promotes early secretory pathway organization. <i> Johnson A, Bhattacharya N, Hanna M, Pennington JG, Schuh AL, Wang L, Otegui MS, Stagg SM, Audhya A. </i> EMBO J, 2015","date":"2023-01-20T12:00:15.049Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03929r001","statement":[{"text":"Circular dichroism spectroscopy was used to characterize the carboxyl-terminus of C. elegans TFG (amino acids 195-486). Samples were analyzed at different concentrations, and the data were normalized relative to one another. CD spectra were collected at 25°C in 25 mM sodium phosphate (pH 7.2) using a 1 mm path length quartz cell. The spectra are characteristic of an intrinsically disordered protein.","type":"Figure"}],"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":25,"statements":[{"type":"Figure","text":"CD spectra were collected at 25°C in 25 mM sodium phosphate (pH 7.2) using a 1 mm path length quartz cell."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7.2,"statements":[{"type":"Figure","text":"CD spectra were collected at 25°C in 25 mM sodium phosphate (pH 7.2) using a 1 mm path length quartz cell."}]}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":25,"db":"ChEBI","id":"37586","statements":[{"type":"Figure","text":"CD spectra were collected at 25°C in 25 mM sodium phosphate (pH 7.2) using a 1 mm path length quartz cell."}],"entry_name":"sodium phosphate"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-20T20:11:22.179Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MVHSNGAITSTILKARHADVVRKTSLHHANDLTLIDLVLNVQRLLALPSDANFVLKYKDEEGDLVTLAEDSDLLLALHTSGATLDVTVVVDSRAREAVHDVQKQVEQIKLDVGKLLGALSALDVAQIAEQSNTSVANLSAPKQSHHDNIVFQKSFEAAPPSPVPSEKAELPATIQPSVHEQFNHRPAHVEEEIPLENHYAPPPHQQIPDDLNTSFSSQPPPPIEQFGAIPPPNATIPSFPTSNAASPPVQEFAPPPPQQQQQQFQAPPPPMASHSSISSTPVQQQGFAPPQQFGGPPPSGPPSEYGGYAPPQQQQQQFGAPPPQGAPQQGFGAPPQGPPQGGPPQGSFGAPPPQQFHAPSPQSFGGPPPPVSSAPGNFAPPPQSGPPGAFAPPPSAFGAPQGPGGPGGYGPPPPGGPGAPGSYGPPQGGPGGFGPPPPGGPGAYGPPPTGFPPVGAPPPGAAGAPGGNPFARGPSATGYRQSPYQQ","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"alphafold_very_low_content":0.3683127572016461,"disorder_content":0.6008230452674898,"disprot_consensus":{"full":[{"start":195,"end":486,"type":"D"}],"Structural state":[{"start":195,"end":486,"type":"D"}]}},{"disprot_id":"DP03930","acc":"Q811T9","creator":"vnugnes","date":"2023-01-20T14:00:18.192Z","features":{"pfam":[{"id":"PF28234","name":"DISC1 C-terminal domain","start":783,"end":826},{"id":"PF30493","name":"DISC1 domain","start":327,"end":699}],"gene3D":[]},"genes":[{"name":{"value":"Disc1","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:2447658","url":"http://www.informatics.jax.org/marker/MGI:2447658"}}]}}],"length":852,"name":"Disrupted in schizophrenia 1 homolog","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":728,"end":852,"reference_id":"29103808","reference_source":"pmid","reference_html":"DISC1 Regulates Neurogenesis via Modulating Kinetochore Attachment of Ndel1/Nde1 during Mitosis. <i> Ye F, Kang E, Yu C, Qian X, Jacob F, Yu C, Mao M, Poon RYC, Kim J, Song H, Ming GL, Zhang M. </i> Neuron, 2017","date":"2023-01-20T14:05:11.304Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03930r001","statement":[{"text":"The nuclear magnetic resonance (NMR) spectra of 15N-labeled DISC1 728–852 also revealed that this fragment is largely unstructured in solution (Figure S3G).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-20T16:58:14.692Z"}},{"start":774,"end":829,"reference_id":"29103808","reference_source":"pmid","reference_html":"DISC1 Regulates Neurogenesis via Modulating Kinetochore Attachment of Ndel1/Nde1 during Mitosis. <i> Ye F, Kang E, Yu C, Qian X, Jacob F, Yu C, Mao M, Poon RYC, Kim J, Song H, Ming GL, Zhang M. </i> Neuron, 2017","date":"2025-06-16T13:31:00.649Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"cross_refs":[{"db":"PDB","id":"5YI4"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9ERR1","operator":null,"partner_start":238,"partner_end":284}],"region_id":"DP03930r002","sequence_construct":"GSEFGPWKEDSHIVSAEVGEKCEAIGVKLLHLEDQLLGAMYSHDEALFQSLQGELQTVKETLQAMILQLQPTKEAGEASASYPTAGAQETEALVPRGSGFGTSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQASRK","statement":[{"text":"We next determined the high-resolution complex structure of DISC1 765–852/Ndel1 CT-CC by NMR spectroscopy (Figures S2C and S2E; Table S1).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":765,"end":835,"reference_id":"29103808","reference_source":"pmid","reference_html":"DISC1 Regulates Neurogenesis via Modulating Kinetochore Attachment of Ndel1/Nde1 during Mitosis. <i> Ye F, Kang E, Yu C, Qian X, Jacob F, Yu C, Mao M, Poon RYC, Kim J, Song H, Ming GL, Zhang M. </i> Neuron, 2017","date":"2023-01-20T14:09:45.162Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5YI4"}],"region_id":"DP03930r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9ERR1"}],"sequence_construct":"GSEFGPWKEDSHIVSAEVGEKCEAIGVKLLHLEDQLLGAMYSHDEALFQSLQGELQTVKETLQAMILQLQPTKEAGEASASYPTAGAQETEALVPRGSGFGTSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQASRK","statement":[{"text":"In the complex, DISC1 765–835 contained two helices that formed an antiparallel hairpin, and Ndel1 CT-CC adopted a single α helix that packed with the DISC1 helix hairpin to form a three-helix bundle through canonical coiled-coil interactions (Figures 2A and 2B). The extension sequence (DISC1 835–852) used to link Ndel1 CT-CC adopted a random coil structure, showing that the covalent linking does not alter the structure of the complex.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-20T16:58:20.010Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MQGGGPRGAPIHSPSHGADSGHGLPPAVAPQRRRLTRRPGYMRSTAGSGIGFLSPAVGMPHPSSAGLTGQQSQHSQSKAGQCGLDPGSHCQASLVGKPFLKSSLVPAVASEGHLHPAQRSMRKRPVHFAVHSKNDSRQSERLTGSFKPGDSGFWQELLSSDSFKSLAPSLDAPWNKGSRGLKTVKPLASPALNGPADIASLPGFQDTFTSSFSFIQLSLGAAGERGEAEGCLPSREAEPLHQRPQEMAAEASSSDRPHGDPRHLWTFSLHAAPGLADLAQVTRSSSRQSECGTVSSSSSDTGFSSQDASSAGGRGDQGGGWADAHGWHTLLREWEPMLQDYLLSNRRQLEVTSLILKLQKCQEKVVEDGDYDTAETLRQRLEELEQEKGRLSWALPSQQPALRSFLGYLAAQIQVALHGATQRAGSDDPEAPLEGQLRTTAQDSLPASITRRDWLIREKQRLQKEIEALQARMSALEAKEKRLSQELEEQEVLLRWPGCDLMALVAQMSPGQLQEVSKALGETLTSANQAPFQVEPPETLRSLRERTKSLNLAVRELTAQVCSGEKLCSSLRRRLSDLDTRLPALLEAKMLALSGSCFSTAKELTEEIWALSSEREGLEMFLGRLLALSSRNSRRLGIVKEDHLRCRQDLALQDAAHKTRMKANTVKCMEVLEGQLSSCRCPLLGRVWKADLETCQLLMQSLQLQEAGSSPHAEDEEQVHSTGEAAQTAALAVPRTPHPEEEKSPLQVLQEWDTHSALSPHCAAGPWKEDSHIVSAEVGEKCEAIGVKLLHLEDQLLGAMYSHDEALFQSLQGELQTVKETLQAMILQLQPTKEAGEASASYPTAGAQETEA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"alphafold_very_low_content":0.45774647887323944,"disorder_content":0.1467136150234742,"disprot_consensus":{"full":[{"start":728,"end":764,"type":"D"},{"start":765,"end":835,"type":"T"},{"start":836,"end":852,"type":"D"}],"Structural state":[{"start":728,"end":852,"type":"D"}],"Molecular function":[{"start":774,"end":829,"type":"F"}],"Structural transition":[{"start":765,"end":835,"type":"T"}]}},{"disprot_id":"DP03931","acc":"Q9NRI5","creator":"vnugnes","date":"2023-01-20T14:19:38.572Z","features":{"pfam":[{"id":"PF28234","name":"DISC1 C-terminal domain","start":783,"end":826},{"id":"PF30493","name":"DISC1 domain","start":326,"end":702}],"gene3D":[]},"genes":[{"name":{"value":"DISC1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:2888","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:2888"}}]},"synonyms":[{"value":"KIAA0457"}]}],"length":854,"name":"Disrupted in schizophrenia 1 protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":718,"end":771,"reference_id":"28249940","reference_source":"pmid","reference_html":"A structural organization for the Disrupted in Schizophrenia 1 protein, identified by high-throughput screening, reveals distinctly folded regions, which are bisected by mental illness-related mutations. <i> Yerabham ASK, Mas PJ, Decker C, Soares DC, Weiergräber OH, Nagel-Steger L, Willbold D, Hart DJ, Bradshaw NJ, Korth C. </i> J Biol Chem, 2017","date":"2023-01-20T14:22:39.186Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03931r001","statement":[{"text":"An additional construct lies within the N-terminal half of the C region, representing AA 718–771 of DISC1. This fragment is also predicted as monomeric by SEC (Fig. 3G), whereas CD revealed a lack of regular secondary structure (Fig. 3H).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-20T16:57:39.218Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MPGGGPQGAPAAAGGGGVSHRAGSRDCLPPAACFRRRRLARRPGYMRSSTGPGIGFLSPAVGTLFRFPGGVSGEESHHSESRARQCGLDSRGLLVRSPVSKSAAAPTVTSVRGTSAHFGIQLRGGTRLPDRLSWPCGPGSAGWQQEFAAMDSSETLDASWEAACSDGARRVRAAGSLPSAELSSNSCSPGCGPEVPPTPPGSHSAFTSSFSFIRLSLGSAGERGEAEGCPPSREAESHCQSPQEMGAKAASLDGPHEDPRCLSRPFSLLATRVSADLAQAARNSSRPERDMHSLPDMDPGSSSSLDPSLAGCGGDGSSGSGDAHSWDTLLRKWEPVLRDCLLRNRRQMEVISLRLKLQKLQEDAVENDDYDKAETLQQRLEDLEQEKISLHFQLPSRQPALSSFLGHLAAQVQAALRRGATQQASGDDTHTPLRMEPRLLEPTAQDSLHVSITRRDWLLQEKQQLQKEIEALQARMFVLEAKDQQLRREIEEQEQQLQWQGCDLTPLVGQLSLGQLQEVSKALQDTLASAGQIPFHAEPPETIRSLQERIKSLNLSLKEITTKVCMSEKFCSTLRKKVNDIETQLPALLEAKMHAISGNHFWTAKDLTEEIRSLTSEREGLEGLLSKLLVLSSRNVKKLGSVKEDYNRLRREVEHQETAYETSVKENTMKYMETLKNKLCSCKCPLLGKVWEADLEACRLLIQSLQLQEARGSLSVEDERQMDDLEGAAPPIPPRLHSEDKRKTPLKVLEEWKTHLIPSLHCAGGEQKEESYILSAELGEKCEDIGKKLLYLEDQLHTAIHSHDEDLIQSLRRELQMVKETLQAMILQLQPAKEAGEREAAASCMTAGVHEAQA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.47423887587822017,"disorder_content":0.06323185011709602,"disprot_consensus":{"full":[{"start":718,"end":771,"type":"D"}],"Structural state":[{"start":718,"end":771,"type":"D"}]}},{"disprot_id":"DP03933","acc":"Q9TU17","creator":"vnugnes","date":"2023-01-20T15:21:10.599Z","features":{"pfam":[{"id":"PF00029","name":"Connexin","start":3,"end":224}],"gene3D":[]},"genes":[{"name":{"value":"GJA3"}}],"length":413,"name":"Gap junction alpha-3 protein","ncbi_taxon_id":9940,"organism":"Ovis aries","regions":[{"start":98,"end":141,"reference_id":"30542154","reference_source":"pmid","reference_html":"Structure of native lens connexin 46/50 intercellular channels by cryo-EM. <i> Myers JB, Haddad BG, O'Neill SE, Chorev DS, Yoshioka CC, Robinson CV, Zuckerman DM, Reichow SL. </i> Nature, 2018","date":"2023-01-20T15:28:17.805Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6MHQ"},{"db":"EMDB","id":"9116"}],"region_id":"DP03933r001","statement":[{"text":"Density for Met1 is not observed in the cryo-EM maps and was shown, by tandem mass spectrometry (MS/MS), to be removed in both Cx46 and Cx50. The resulting N-terminal glycine (G2) is partially acetylated (Extended Data Fig. 1), as shown for the bovine isoforms15,16. The intracellular loop (ICL) connecting TM2–TM3 and the cytoplasmic C-terminal domain (CTD) containing the native cleavage sites of Cx46 and Cx50 are also not resolved16. ","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-20T17:01:39.668Z"}},{"start":223,"end":348,"reference_id":"30542154","reference_source":"pmid","reference_html":"Structure of native lens connexin 46/50 intercellular channels by cryo-EM. <i> Myers JB, Haddad BG, O'Neill SE, Chorev DS, Yoshioka CC, Robinson CV, Zuckerman DM, Reichow SL. </i> Nature, 2018","date":"2023-01-20T15:28:06.765Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6MHQ"},{"db":"EMDB","id":"9116"}],"region_id":"DP03933r002","statement":[{"text":"Density for Met1 is not observed in the cryo-EM maps and was shown, by tandem mass spectrometry (MS/MS), to be removed in both Cx46 and Cx50. The resulting N-terminal glycine (G2) is partially acetylated (Extended Data Fig. 1), as shown for the bovine isoforms15,16. The intracellular loop (ICL) connecting TM2–TM3 and the cytoplasmic C-terminal domain (CTD) containing the native cleavage sites of Cx46 and Cx50 are also not resolved16. ","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-20T17:01:45.530Z"}},{"start":110,"end":136,"reference_id":"32859914","reference_source":"pmid","reference_html":"Connexin-46/50 in a dynamic lipid environment resolved by CryoEM at 1.9 Å. <i> Flores JA, Haddad BG, Dolan KA, Myers JB, Yoshioka CC, Copperman J, Zuckerman DM, Reichow SL. </i> Nat Commun, 2020","date":"2023-01-20T15:53:25.267Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7JN0"},{"db":"PDB","id":"7JKC"},{"db":"PDB","id":"7JMD"},{"db":"PDB","id":"7JN1"}],"region_id":"DP03933r003","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"241349","statements":[{"type":"Results","text":"Freshly purified channels were reconstituted into self-assembling lipid nanodiscs containing pure dimyristoyl phosphatidylcholine (DMPC) at room temperature (~25 °C), supported by the membrane scaffold protein 1E1 (MSP1E1)17 (see “Methods”)."}],"entry_name":"dimyristoyl phosphatidylcholine"}],"statement":[{"text":"The intracellular loop (ICL) and C-terminal domain (CTD) remain unresolved, presumably due to intrinsic disorder of these regulatory domains16,18,19.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-20T17:01:52.937Z"}},{"start":225,"end":413,"reference_id":"32859914","reference_source":"pmid","reference_html":"Connexin-46/50 in a dynamic lipid environment resolved by CryoEM at 1.9 Å. <i> Flores JA, Haddad BG, Dolan KA, Myers JB, Yoshioka CC, Copperman J, Zuckerman DM, Reichow SL. </i> Nat Commun, 2020","date":"2023-01-20T15:53:44.008Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7JN0"},{"db":"PDB","id":"7JKC"},{"db":"PDB","id":"7JMD"},{"db":"PDB","id":"7JN1"}],"region_id":"DP03933r004","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"241349","statements":[{"type":"Results","text":"Freshly purified channels were reconstituted into self-assembling lipid nanodiscs containing pure dimyristoyl phosphatidylcholine (DMPC) at room temperature (~25 °C), supported by the membrane scaffold protein 1E1 (MSP1E1)17 (see “Methods”)."}],"entry_name":"dimyristoyl phosphatidylcholine"}],"statement":[{"text":"The intracellular loop (ICL) and C-terminal domain (CTD) remain unresolved, presumably due to intrinsic disorder of these regulatory domains16,18,19.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-20T17:01:54.888Z"}}],"regions_counter":4,"released":"2024_06","sequence":"MGDWSFLGRLLENAQEHSTVIGKVWLTVLFIFRILVLGAAAEEVWGDEQSDFTCNTQQPGCENVCYDRAFPISHVRFWVLQIIFVSTPTLIYLGHVLHLVRMEEKRKEREEEPPKAAGPAEEHQDPAPVRDDRGKVRIAGALLRTYVFNIIFKTLFEVGFIAGQYFLYGFQLKPLYRCDRWPCPNTVDCFISRPTEKTIFILFMLAVACVSLLLNVLEIYHLGWKKLKQGMTSPFRPDTPGSRAGSAKPMGGSPLLLPPNSAPPAVTIGFPPYYAPSASSLGQASAPGYPEPPLPAALPGTPGTPGTPGTLGGGGGNQGLRAPAQNCANREAEPQTSARKASPPASTPPAAPAGGPQQFLPGGAAGSSGDSDGEGAVTAVELHAPPEPPADPGRSSKASKSSGGRARAADLAI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Caprinae","Ovis"],"alphafold_very_low_content":0.4213075060532688,"disorder_content":0.5690072639225182,"disprot_consensus":{"full":[{"start":98,"end":141,"type":"D"},{"start":223,"end":413,"type":"D"}],"Structural state":[{"start":98,"end":141,"type":"D"},{"start":223,"end":413,"type":"D"}]}},{"disprot_id":"DP03934","acc":"P55917","creator":"vnugnes","date":"2023-01-20T15:21:37.715Z","features":{"pfam":[{"id":"PF00029","name":"Connexin","start":3,"end":235},{"id":"PF03509","name":"Gap junction alpha-8 protein (Cx50)","start":267,"end":333}],"gene3D":[]},"genes":[{"name":{"value":"GJA8"}}],"length":440,"name":"Gap junction alpha-8 protein","ncbi_taxon_id":9940,"organism":"Ovis aries","regions":[{"start":98,"end":153,"reference_id":"30542154","reference_source":"pmid","reference_html":"Structure of native lens connexin 46/50 intercellular channels by cryo-EM. <i> Myers JB, Haddad BG, O'Neill SE, Chorev DS, Yoshioka CC, Robinson CV, Zuckerman DM, Reichow SL. </i> Nature, 2018","date":"2023-01-20T15:27:14.063Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6MHY"},{"db":"EMDB","id":"9116"}],"region_id":"DP03934r001","statement":[{"text":"Density for Met1 is not observed in the cryo-EM maps and was shown, by tandem mass spectrometry (MS/MS), to be removed in both Cx46 and Cx50. The resulting N-terminal glycine (G2) is partially acetylated (Extended Data Fig. 1), as shown for the bovine isoforms15,16. The intracellular loop (ICL) connecting TM2–TM3 and the cytoplasmic C-terminal domain (CTD) containing the native cleavage sites of Cx46 and Cx50 are also not resolved16. ","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-20T17:08:03.007Z"}},{"start":235,"end":440,"reference_id":"30542154","reference_source":"pmid","reference_html":"Structure of native lens connexin 46/50 intercellular channels by cryo-EM. <i> Myers JB, Haddad BG, O'Neill SE, Chorev DS, Yoshioka CC, Robinson CV, Zuckerman DM, Reichow SL. </i> Nature, 2018","date":"2023-01-20T15:27:01.853Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6MHY"},{"db":"EMDB","id":"9116"}],"region_id":"DP03934r002","statement":[{"text":"Density for Met1 is not observed in the cryo-EM maps and was shown, by tandem mass spectrometry (MS/MS), to be removed in both Cx46 and Cx50. The resulting N-terminal glycine (G2) is partially acetylated (Extended Data Fig. 1), as shown for the bovine isoforms15,16. The intracellular loop (ICL) connecting TM2–TM3 and the cytoplasmic C-terminal domain (CTD) containing the native cleavage sites of Cx46 and Cx50 are also not resolved16. ","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-20T17:08:05.164Z"}},{"start":110,"end":148,"reference_id":"32859914","reference_source":"pmid","reference_html":"Connexin-46/50 in a dynamic lipid environment resolved by CryoEM at 1.9 Å. <i> Flores JA, Haddad BG, Dolan KA, Myers JB, Yoshioka CC, Copperman J, Zuckerman DM, Reichow SL. </i> Nat Commun, 2020","date":"2023-01-20T15:54:59.676Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7JMC"},{"db":"PDB","id":"7JM9"},{"db":"PDB","id":"7JJP"},{"db":"PDB","id":"7JLW"}],"region_id":"DP03934r003","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"241349","statements":[{"type":"Results","text":"Freshly purified channels were reconstituted into self-assembling lipid nanodiscs containing pure dimyristoyl phosphatidylcholine (DMPC) at room temperature (~25 °C), supported by the membrane scaffold protein 1E1 (MSP1E1)17 (see “Methods”)."}],"entry_name":"dimyristoyl phosphatidylcholine"}],"statement":[{"text":"The intracellular loop (ICL) and C-terminal domain (CTD) remain unresolved, presumably due to intrinsic disorder of these regulatory domains16,18,19.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-20T17:08:25.028Z"}},{"start":237,"end":440,"reference_id":"32859914","reference_source":"pmid","reference_html":"Connexin-46/50 in a dynamic lipid environment resolved by CryoEM at 1.9 Å. <i> Flores JA, Haddad BG, Dolan KA, Myers JB, Yoshioka CC, Copperman J, Zuckerman DM, Reichow SL. </i> Nat Commun, 2020","date":"2023-01-20T15:55:36.847Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7JMC"},{"db":"PDB","id":"7JM9"},{"db":"PDB","id":"7JJP"},{"db":"PDB","id":"7JLW"}],"region_id":"DP03934r004","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"241349","statements":[{"type":"Results","text":"Freshly purified channels were reconstituted into self-assembling lipid nanodiscs containing pure dimyristoyl phosphatidylcholine (DMPC) at room temperature (~25 °C), supported by the membrane scaffold protein 1E1 (MSP1E1)17 (see “Methods”)."}],"entry_name":"dimyristoyl phosphatidylcholine"}],"statement":[{"text":"The intracellular loop (ICL) and C-terminal domain (CTD) remain unresolved, presumably due to intrinsic disorder of these regulatory domains16,18,19.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-20T17:08:32.573Z"}}],"regions_counter":4,"released":"2024_06","sequence":"MGDWSFLGNILEEVNEHSTVIGRVWLTVLFIFRILILGTAAEFVWGDEQSDFVCNTQQPGCENVCYDEAFPISHIRLWVLQIIFVSTPSLVYVGHAVHHVRMEEKRKEREAEELSQQSPGNGGERAPLAADQGSVKKSSSSSKGTKKFRLEGTLLRTYVCHIIFKTLFEVGFIVGHYFLYGFRILPLYRCSRWPCPNVVDCFVSRPTEKTIFILFMLSVASVSLFLNILEMSHLGLKKIRSAFKRPVEQPLGEIPEKSLHSIAVSSIQKAKGYQLLEEEKIVSHYFPLTEVGMVEASPLSAKPFSQFEEKVGPGPLGDLSRAYQETLPSYAQVGAQEGVEEEQPIEAAAEPEVGDKSQEAERVSTEGEETLAVLEEEKVEPPEVEKEAEKEETPPEKVSKQELTPEKAPSLCAELPGEDTRPLSRLSKASSRARSDDLTV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Caprinae","Ovis"],"alphafold_very_low_content":0.4863636363636364,"disorder_content":0.5954545454545455,"disprot_consensus":{"full":[{"start":98,"end":153,"type":"D"},{"start":235,"end":440,"type":"D"}],"Structural state":[{"start":98,"end":153,"type":"D"},{"start":235,"end":440,"type":"D"}]}},{"disprot_id":"DP03935","acc":"P28234","creator":"vnugnes","date":"2023-01-20T16:01:53.524Z","features":{"pfam":[{"id":"PF00029","name":"Connexin","start":3,"end":230},{"id":"PF16791","name":"Connexin 40 C-terminal domain","start":257,"end":356}],"gene3D":[]},"genes":[{"name":{"value":"Gja5"},"synonyms":[{"value":"Cxn-40"}]}],"length":356,"name":"Gap junction alpha-5 protein","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions":[{"start":252,"end":356,"reference_id":"19808665","reference_source":"pmid","reference_html":"Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains. <i> Bouvier D, Spagnol G, Chenavas S, Kieken F, Vitrac H, Brownell S, Kellezi A, Forge V, Sorgen PL. </i> J Biol Chem, 2009","date":"2023-01-20T16:02:56.484Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2K7M"}],"region_id":"DP03935r001","statement":[{"text":"The overall structure of the Cx40CT (Ser-251–Val-355), as calculated from using 1123 NOE restraints, is intrinsically disordered or random-coiled.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-20T17:09:21.695Z"}},{"start":252,"end":356,"reference_id":"19808665","reference_source":"pmid","reference_html":"Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains. <i> Bouvier D, Spagnol G, Chenavas S, Kieken F, Vitrac H, Brownell S, Kellezi A, Forge V, Sorgen PL. </i> J Biol Chem, 2009","date":"2023-01-20T16:05:25.958Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03935r002","statement":[{"text":"A major band appears at 1643 cm−1, which is consistent with random coil structure. A weaker absorption at 1659 cm−1 may correspond to a very dynamic α-helix accessible to the solvent. Also, a very broad band at 1670 cm−1 corresponds to turns typically present in dynamic and unfolded proteins.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-20T17:09:24.014Z"}},{"start":252,"end":356,"reference_id":"19808665","reference_source":"pmid","reference_html":"Characterization of the structure and intermolecular interactions between the connexin40 and connexin43 carboxyl-terminal and cytoplasmic loop domains. <i> Bouvier D, Spagnol G, Chenavas S, Kieken F, Vitrac H, Brownell S, Kellezi A, Forge V, Sorgen PL. </i> J Biol Chem, 2009","date":"2023-01-20T16:08:27.854Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03935r003","statement":[{"text":"As expected from the NMR data, Cx40CT and Cx43CT at pH 6.0 present a high proportion of random-coiled structure (major absorption at 200 nm for Cx40CT and 201 nm for Cx43CT) (Fig. 3A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-20T17:09:27.096Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MGDWSFLGEFLEEVHKHSTVIGKVWLTVLFIFRMLVLGTAAESSWGDEQADFRCDTIQPGCQNVCYDQAFPISHIRYWVLQIIFVSTPSLVYMGHAMHTVRMQEKQKLREAEKAKEAGGTGTYEYLAEKAELSCWKEVNGKIVLQGTLLNTYVCTILIRTAMEVAFMVGQYLLYGIFLDTLHVCRRSPCPHPVNCYVSRPTEKNVFIVFMMAVAGLSLFLSLAELYHLGWKKIRQRLAKSRQGDKHQLLGPSTSLVQGLTPPPDFNQCLKNSPDEKFFSDFSNNMGSRKNPDPLATEEVPNQEQIPEEGFIHTQYGQKPEQPSGASAGHRFPQGYHSDKRRLSKASSKARSDDLSV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"alphafold_very_low_content":0.3089887640449438,"disorder_content":0.2949438202247191,"disprot_consensus":{"full":[{"start":252,"end":356,"type":"D"}],"Structural state":[{"start":252,"end":356,"type":"D"}]}},{"disprot_id":"DP03937","acc":"Q03190","creator":"vnugnes","date":"2023-01-20T16:43:08.976Z","features":{"pfam":[{"id":"PF00029","name":"Connexin","start":3,"end":233}],"gene3D":[]},"genes":[{"name":{"value":"Gja4"},"synonyms":[{"value":"Cxn-37"}]}],"length":333,"name":"Gap junction alpha-4 protein","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions":[{"start":270,"end":333,"reference_id":"24133065","reference_source":"pmid","reference_html":"Carboxy terminus and pore-forming domain properties specific to Cx37 are necessary for Cx37-mediated suppression of insulinoma cell proliferation. <i> Nelson TK, Sorgen PL, Burt JM. </i> Am J Physiol Cell Physiol, 2013","date":"2023-01-20T16:45:36.476Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03937r001","statement":[{"text":"B: circular dichroism shows Cx37-CT is disordered at both pH 7.4 and 5.8.","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-20T17:11:33.973Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MGDWGFLEKLLDQVQEHSTVVGKIWLTVLFIFRILILGLAGESVWGDEQSDFECNTAQPGCTNVCYDQAFPISHIRYWVLQFLFVSTPTLIYLGHVIYLSRREERLRQKEGELRALPSKDPHVERALAAIEHQMAKISVAEDGRLRIRGALMGTYVISVLCKSVLEAGFLYGQWRLYGWTMEPVFVCQRAPCPHVVDCYVSRPTEKTIFIIFMLVVGVISLVLNLLELVHLLCRCVSREIKARRDHDTRPAQGSASDPYPEQVFFYLPMGEGPSSPPCPTYNGLSSTEQNWANLTTEERLTSTRPPPFVNAAPQGGQKSSSRPNSSASKKQYV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"alphafold_very_low_content":0.2072072072072072,"disorder_content":0.1921921921921922,"disprot_consensus":{"full":[{"start":270,"end":333,"type":"D"}],"Structural state":[{"start":270,"end":333,"type":"D"}]}},{"disprot_id":"DP03938","acc":"P29353-2","creator":"vnugnes","date":"2023-01-23T15:07:55.911Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"SHC1"},"synonyms":[{"value":"SHC"},{"value":"SHCA"}]}],"length":473,"name":"Isoform p52Shc of SHC-transforming protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":41,"reference_id":"12906822","reference_source":"pmid","reference_html":"Coupling of folding and binding in the PTB domain of the signaling protein Shc. <i> Farooq A, Zeng L, Yan KS, Ravichandran KS, Zhou MM. </i> Structure, 2003","date":"2023-01-23T15:11:38.016Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Briefly, each cDNA construct was subcloned into the bacterial expression vector pET15b (Novagen) with a His tag at the N terminus of the recombinant protein and expressed in Escherichia coli BL21(DE3)."}]}],"cross_refs":[{"db":"PDB","id":"1N3H"},{"db":"PDB","id":"1OY2"}],"region_id":"DP03938r001","statement":[{"text":"As expected, the residues 1–41 were structurally disordered and did not appear to have any effect on the structured core region of the domain.","type":"Results"},{"text":"No NOEs were observed between the N- and C-terminal residues 17–41 and 192–207, and the core region of the domain in the free form of the Shc PTB domain.","type":"Results"},{"text":"The structure of PTB domain from the construct 1–207 was virtually superimposable with that obtained from the construct 17–207 in the free form.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-24T10:32:22.885Z"}},{"start":192,"end":207,"reference_id":"12906822","reference_source":"pmid","reference_html":"Coupling of folding and binding in the PTB domain of the signaling protein Shc. <i> Farooq A, Zeng L, Yan KS, Ravichandran KS, Zhou MM. </i> Structure, 2003","date":"2023-01-23T15:12:27.919Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Briefly, each cDNA construct was subcloned into the bacterial expression vector pET15b (Novagen) with a His tag at the N terminus of the recombinant protein and expressed in Escherichia coli BL21(DE3)."}]}],"cross_refs":[{"db":"PDB","id":"1N3H"},{"db":"PDB","id":"1OY2"}],"region_id":"DP03938r002","statement":[{"text":"No NOEs were observed between the N- and C-terminal residues 17–41 and 192–207, and the core region of the domain in the free form of the Shc PTB domain.","type":"Results"},{"text":"The structure of PTB domain from the construct 1–207 was virtually superimposable with that obtained from the construct 17–207 in the free form.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-24T10:32:24.928Z"}},{"start":17,"end":34,"reference_id":"8524391","reference_source":"pmid","reference_html":"Structure and ligand recognition of the phosphotyrosine binding domain of Shc. <i> Zhou MM, Ravichandran KS, Olejniczak EF, Petros AM, Meadows RP, Sattler M, Harlan JE, Wade WS, Burakoff SJ, Fesik SW. </i> Nature, 1995","date":"2023-01-23T15:30:13.271Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1SHC"}],"region_id":"DP03938r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04629","statements":[{"type":"Article","text":"The NMR studies were conducted using a I : I complex of an N-terminal fragment of She (residues 17- 207) and a 12-residue tyrosine-phosphorylated peptide (HIIENPQpYFSDA) derived from the sole She binding site (phosphotyrosine 490) of the nerve growth factor receptor TrkA."}]}],"statement":[{"text":"For clarity, the Nterminal residues of the PTB domain (17-34) that were illdefined by the NMR data are not shown. These residues do not exhibit any long-range NOEs to the rest of the protein and are probably not part of the PTB domain. ","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-24T10:32:26.688Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MNKLSGGGGRRTRVEGGQLGGEEWTRHGSFVNKPTRGWLHPNDKVMGPGVSYLVRYMGCVEVLQSMRALDFNTRTQVTREAISLVCEAVPGAKGATRRRKPCSRPLSSILGRSNLKFAGMPITLTVSTSSLNLMAADCKQIIANHHMQSISFASGGDPDTAEYVAYVAKDPVNQRACHILECPEGLAQDVISTIGQAFELRFKQYLRNPPKLVTPHDRMAGFDGSAWDEEEEEPPDHQYYNDFPGKEPPLGGVVDMRLREGAAPGAARPTAPNAQTPSHLGATLPVGQPVGGDPEVRKQMPPPPPCPGRELFDDPSYVNVQNLDKARQAVGGAGPPNPAINGSAPRDLFDMKPFEDALRVPPPPQSVSMAEQLRGEPWFHGKLSRREAEALLQLNGDFLVRESTTTPGQYVLTGLQSGQPKHLLLVDPEGVVRTKDHRFESVSHLISYHMDNHLPIISAGSELCLQQPVERKL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"disorder_content":0.12050739957716702,"disprot_consensus":{"full":[{"start":1,"end":41,"type":"D"},{"start":192,"end":207,"type":"D"}],"Structural state":[{"start":1,"end":41,"type":"D"},{"start":192,"end":207,"type":"D"}]}},{"disprot_id":"DP03939","acc":"B0JEU3","creator":"cpintado","date":"2023-01-23T15:55:31.181Z","features":{"pfam":[{"id":"PF00190","name":"Cupin","start":187,"end":299},{"id":"PF00190","name":"Cupin","start":347,"end":522},{"id":"PF04702","name":"Vicilin N terminal region","start":31,"end":142}],"gene3D":[]},"genes":[{"name":{"value":"vicilin","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAP69670.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAP69670.1"}}]}}],"length":569,"name":"Vicilin","ncbi_taxon_id":4081,"organism":"Solanum lycopersicum","regions":[{"start":418,"end":450,"reference_id":"31753489","reference_source":"pmid","reference_html":"Comparative study of 7S globulin from Corylus avellana and Solanum lycopersicum revealed importance of salicylic acid and Cu-binding loop in modulating their function. <i> Shikhi M, Jain A, Salunke DM. </i> Biochem Biophys Res Commun, 2020","date":"2023-01-31T16:34:58.816Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6L4M"}],"region_id":"DP03939r001","statement":[{"text":"Two regions, one from residue number 201 to 209\nand another from 282 to 316 were found to be disordered with poor\nelectron density in the case of SL80.1.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29036","entry_name":"copper(2+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-31T18:42:46.408Z"}},{"start":543,"end":569,"reference_id":"31753489","reference_source":"pmid","reference_html":"Comparative study of 7S globulin from Corylus avellana and Solanum lycopersicum revealed importance of salicylic acid and Cu-binding loop in modulating their function. <i> Shikhi M, Jain A, Salunke DM. </i> Biochem Biophys Res Commun, 2020","date":"2023-01-31T18:42:43.601Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03939r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29036","entry_name":"copper(2+)"}],"statement":[{"text":"Nine residues from N-terminal and 27 residues from C-terminal could not be traced in the crystal structure as the electron density for these residues was missing.","type":"Results"}]}],"regions_counter":2,"released":"2024_06","sequence":"MAIFTKPKLLFIFFLILSLVLVSQCYDQNPRGYQDPQEKLRECQQRCERQQPGQQKQLCKQRCEQQYRKEQQQQHGGETGEDDLGNRGPDKSYKRLQECQRRCQSEQQGQRLQECQQRCQQEYQREKGQHQGETNPQWEQQEKSNNPYLFESQRFRSRFRASHGDFRILERFNQRSQLLKGIEKYRVAILELEPQSFVLPHHCDGEAIYVVVKGQGVINIAEQDNKNSFNLQKGDVIRLFAGSNVYLLNKDNNEKLFVYVLAKSVNAPGNLQEYFSAGGQNPESFYRAFSSDILESAFNNPRDKLERLFGQHKEGIIIKASEEQIRAISEHASRSTQQTRGRTQGPFNLMKERPVFESRFGQFFEARPERYEQLRDLDAAVGFMNINQGGMVLPYYNTKSTKLVMVIEGNARFEMACPHLGRQSQSPWSRGQGREQEREQEQEQEEGDVHYQKIRGNLNVGDVLVIPAGHPITFVATGNSNLRIVGFGVDAENNKKNFLAGKQNIWRNIDREAKELSFSMPGREVEEIFQRQDQSYFVAGPEHRQQRERGEEGRRGQDQYLSSILDFVF","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","lamiids","Solanales","Solanaceae","Solanoideae","Solaneae","Solanum","Solanum subgen. Lycopersicon"],"alphafold_very_low_content":0.1634446397188049,"disorder_content":0.1054481546572935,"disprot_consensus":{"full":[{"start":418,"end":450,"type":"D"},{"start":543,"end":569,"type":"D"}],"Structural state":[{"start":418,"end":450,"type":"D"},{"start":543,"end":569,"type":"D"}]}},{"disprot_id":"DP03940","acc":"Q8S4P9","creator":"cpintado","date":"2023-01-23T16:05:29.892Z","features":{"pfam":[{"id":"PF00190","name":"Cupin","start":107,"end":174},{"id":"PF00190","name":"Cupin","start":264,"end":416}],"gene3D":[]},"genes":[],"length":448,"name":"Vicilin Cor a 11.0101","ncbi_taxon_id":13451,"organism":"Corylus avellana","regions":[{"start":25,"end":59,"reference_id":"31753489","reference_source":"pmid","reference_html":"Comparative study of 7S globulin from Corylus avellana and Solanum lycopersicum revealed importance of salicylic acid and Cu-binding loop in modulating their function. <i> Shikhi M, Jain A, Salunke DM. </i> Biochem Biophys Res Commun, 2020","date":"2023-01-31T13:58:01.701Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6L4C"}],"region_id":"DP03940r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29036","entry_name":"copper(2+)"}],"statement":[{"text":"All the three independent monomers in the case of HZ.1 had 12 residues missing from the N-terminal end and 16 residues missing from the C-terminal end.","type":"Results"}]},{"start":433,"end":448,"reference_id":"31753489","reference_source":"pmid","reference_html":"Comparative study of 7S globulin from Corylus avellana and Solanum lycopersicum revealed importance of salicylic acid and Cu-binding loop in modulating their function. <i> Shikhi M, Jain A, Salunke DM. </i> Biochem Biophys Res Commun, 2020","date":"2023-01-31T13:58:20.368Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6L4C"}],"region_id":"DP03940r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29036","entry_name":"copper(2+)"}],"statement":[{"text":"All the three independent monomers in the case of HZ.1 had 12 residues missing from the N-terminal end and 16 residues missing from the C-terminal end.","type":"Results"}]}],"regions_counter":3,"released":"2024_06","sequence":"MLPKEDPELKKCKHKCRDERQFDEQQRRDGKQICEEKARERQQEEGNSSEESYGKEQEENPYVFQDEHFESRVKTEEGRVQVLENFTKRSRLLSGIENFRLAILEANPHTFISPAHFDAELVLFVAKGRATITMVREEKRESFNVEHGDIIRIPAGTPVYMINRDENEKLFIVKILQPVSAPGHFEAFYGAGGEDPESFYRAFSWEVLEAALKVRREQLEKVFGEQSKGSIVKASREKIRALSQHEEGPPRIWPFGGESSGPINLLHKHPSQSNQFGRLYEAHPDDHKQLQDLDLMVSFANITKGSMAGPYYNSRATKISVVVEGEGFFEMACPHLSSSSGSYQKISARLRRGVVFVAPAGHPVAVIASQNNNLQVLCFEVNAHGNSRFPLAGKGNIVNEFERDAKELAFNLPSREVERIFKNQDQAFFFPGPNKQQEEGGRGGRAFE","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","fabids","Fagales","Betulaceae","Corylus"],"alphafold_very_low_content":0.078125,"disorder_content":0.11383928571428571,"disprot_consensus":{"full":[{"start":25,"end":59,"type":"D"},{"start":433,"end":448,"type":"D"}],"Structural state":[{"start":25,"end":59,"type":"D"},{"start":433,"end":448,"type":"D"}]}},{"disprot_id":"DP03941","acc":"Q20010","creator":"fquaglia","date":"2023-01-26T15:42:41.323Z","features":{"pfam":[{"id":"PF21518","name":"Spindle assembly abnormal protein 5, implico domain","start":211,"end":254}],"gene3D":[]},"genes":[{"name":{"value":"sas-5"},"orfNames":[{"value":"F35B12.5"}]}],"length":404,"name":"Spindle assembly abnormal protein 5","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":2,"end":122,"reference_id":"26023830","reference_source":"pmid","reference_html":"The Caenorhabditis elegans protein SAS-5 forms large oligomeric assemblies critical for centriole formation. <i> Rogala KB, Dynes NJ, Hatzopoulos GN, Yan J, Pong SK, Robinson CV, Deane CM, Gönczy P, Vakonakis I. </i> Elife, 2015","date":"2023-01-26T15:48:29.859Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":10,"statements":[{"type":"Figure","text":"Overlaid CD spectra of SAS-5 N-terminal (residues 2–122) and C-terminal (residues 269–404) fragments recorded at 10°C."}]}],"region_id":"DP03941r001","statement":[{"text":"The SAS-5 N- and C-terminal segments are unstructured in isolation.","type":"Figure"},{"text":"Overlaid CD spectra of SAS-5 N-terminal (residues 2–122) and C-terminal (residues 269–404) fragments recorded at 10°C. The semi-quantitative contribution of secondary structure elements in each spectrum is deconvoluted in the bar chart left. Grey colour corresponds to random coil, green to β-strand and red to α-helical segments.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-26T16:01:14.079Z"}},{"start":269,"end":404,"reference_id":"26023830","reference_source":"pmid","reference_html":"The Caenorhabditis elegans protein SAS-5 forms large oligomeric assemblies critical for centriole formation. <i> Rogala KB, Dynes NJ, Hatzopoulos GN, Yan J, Pong SK, Robinson CV, Deane CM, Gönczy P, Vakonakis I. </i> Elife, 2015","date":"2023-01-26T15:48:37.062Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":10,"statements":[{"type":"Figure","text":"Overlaid CD spectra of SAS-5 N-terminal (residues 2–122) and C-terminal (residues 269–404) fragments recorded at 10°C."}]}],"region_id":"DP03941r002","statement":[{"text":"The SAS-5 N- and C-terminal segments are unstructured in isolation.","type":"Figure"},{"text":"Overlaid CD spectra of SAS-5 N-terminal (residues 2–122) and C-terminal (residues 269–404) fragments recorded at 10°C. The semi-quantitative contribution of secondary structure elements in each spectrum is deconvoluted in the bar chart left. Grey colour corresponds to random coil, green to β-strand and red to α-helical segments.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-26T16:01:13.496Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MNNYDDLPCSIYFKKPTVQEFVDQPRVFEDSEVPAFQEVLQLPQERTKPPVPSTQPIVAAVEVAKKKSCLSAPKPRKEPPSHPALRQKTVAFGKTVNVSQTVEGTSRNSKKVLASTMSAQNTTTTEEQAAENWRDAMKTELQTIRTEIQEETARRQEELNAQNLVKMQELMSNFFQKITIPKQQAIEPVEKDKENFHESPRQSRQQKPASKIASAREVIKRDGVIPPEALTIIEQRLRSDPMFRQQIDNVLADAECDANRAAYSPPPPMSEVRYGSGVNPALMRETLTVERSIRYDNGLASIDSRQWTNERRDNRAPDSYRTYEPDQPCHSLYQKGQSISYYPSEAAGKTTARNNRTGYYVEDSSDHEEDVVVNKRGQNYHEQAVPETPAERERRIREKYARRK","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"alphafold_very_low_content":0.49257425742574257,"disorder_content":0.6361386138613861,"disprot_consensus":{"full":[{"start":2,"end":122,"type":"D"},{"start":269,"end":404,"type":"D"}],"Structural state":[{"start":2,"end":122,"type":"D"},{"start":269,"end":404,"type":"D"}]}},{"disprot_id":"DP03942","acc":"P34413","creator":"vnugnes","date":"2023-01-27T18:13:08.112Z","features":{"pfam":[{"id":"PF10034","name":"Q-cell neuroblast polarisation","start":37,"end":683}],"gene3D":[]},"genes":[{"name":{"value":"dpy-19"},"orfNames":[{"value":"F22B7.10"}]}],"length":683,"name":"C-mannosyltransferase dpy-19","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":1,"end":22,"reference_id":"36604564","reference_source":"pmid","reference_html":"Structure, sequon recognition and mechanism of tryptophan C-mannosyltransferase. <i> Bloch JS, John A, Mao R, Mukherjee S, Boilevin J, Irobalieva RN, Darbre T, Scott NE, Reymond JL, Kossiakoff AA, Goddard-Borger ED, Locher KP. </i> Nat Chem Biol, 2023","date":"2023-01-27T18:32:56.780Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"14782"},{"db":"EMDB","id":"14779"},{"db":"EMDB","id":"14781"},{"db":"PDB","id":"7ZLI"},{"db":"PDB","id":"7ZLH"},{"db":"PDB","id":"7ZLG"},{"db":"PDB","id":"7ZLJ"},{"db":"EMDB","id":"14780"}],"region_id":"DP03942r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q7Z3Y4"}],"statement":[{"text":"Regions that were disordered in the structures are indicated with dashed lines.","type":"Figure"},{"text":"The cryo-EM structure of C-mannosyltransferase CeDPY19, in complex with Dol25-P-Man and bound to CMT2-Fab and anti-Fab nanobody (whether alone or with Dol25-P-C-Man and/or an acceptor peptide, shows this region is disordered. ","type":"Curator statement"}]}],"regions_counter":1,"released":"2024_06","sequence":"MAKKPKNSPEKSKYSSDTSSSLYSQTWLASVVIIGLLVGYINYQHVYTLFENDKHFSHLADFEREMAYRTEMGLYYSYYKTIINAPSFLEGVQEITHDTVTEHGHEINTLNRFNLYPEVILAFLYRPFRAFAKSANWQIELCWQVNRGELRPVESCEGIGNPHYFYITGVFIVAGTVASSIFYLGVLVSDSIFGGFLSVLCFAFNHGEATRVQWTPPLRESFAFPFIIGHIAILTFVIKYKKSGHSMILLLTSMAVPALLFWQFTQFAFFTQICSIFLAFSLDLIPFSTAKTVIHSHIISFLIGFLLLFGNEMMITALYFPSILALGMIIYISPLLSNLKFRPAYVLFLAIIFASITLGLKIGLSKGLGIEDDAHIFDILRSKFTSFANFHTRLYTCSAEFDFIQYSTIEKLCGTLLIPLALISLVTFVFNFVKNTNLLWRNSEEIGENGEILYNVVQLCCSTVMAFLIMRLKLFMTPHLCIVAALFANSKLLGGDRISKTIRVSALVGVIAILFYRGIPNIRQQLNVKGEYSNPDQEMLFDWIQHNTKQDAVFAGTMPVMANVKLTTLRPIVNHPHYEHVGIRERTLKVYSMFSKKPIAEVHKIMKEMGVNYFVFQLMNCSNDERRPECVYRGMWDEEDPKNSGRTALCDLWILAANSKDNSRIAPFKIVYNANRNYIVLKI","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"alphafold_very_low_content":0.02635431918008785,"disorder_content":0.032210834553440704,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"}],"Structural state":[{"start":1,"end":22,"type":"D"}]}},{"disprot_id":"DP03943","acc":"A7M6E7","creator":"cpintado","date":"2023-01-30T12:08:06.243Z","features":{"pfam":[{"id":"PF06792","name":"Uncharacterised protein family (UPF0261) N-terminal domain","start":9,"end":196},{"id":"PF09370","name":"Phosphoenolpyruvate hydrolase-like","start":486,"end":751},{"id":"PF23189","name":"Uncharacterised protein family (UPF0261) C-terminal domain","start":211,"end":428}],"gene3D":[]},"genes":[{"name":{"value":"Tm-1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"17699618","url":"http://www.ncbi.nlm.nih.gov/pubmed/17699618","alternativeUrl":"https://europepmc.org/abstract/MED/17699618"}}]}}],"length":754,"name":"ToMV resistance protein Tm-1(GCR237)","ncbi_taxon_id":4081,"organism":"Solanum lycopersicum","regions":[{"start":80,"end":89,"reference_id":"25092327","reference_source":"pmid","reference_html":"Structural basis for the recognition-evasion arms race between Tomato mosaic virus and the resistance gene Tm-1. <i> Ishibashi K, Kezuka Y, Kobayashi C, Kato M, Inoue T, Nonaka T, Ishikawa M, Matsumura H, Katoh E. </i> Proc Natl Acad Sci U S A, 2014","date":"2023-01-31T15:00:06.976Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3WRW"}],"region_id":"DP03943r001","statement":[{"text":"The region under positive selection (T79–D112; shown in red in Fig. 1B) forms part of the Tm-1 surface and contains α3 and residues L80–A89, which, because this sequence has no interpretable electron density, may be a disordered loop.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-31T15:20:45.524Z"}},{"start":80,"end":89,"reference_id":"25092327","reference_source":"pmid","reference_html":"Structural basis for the recognition-evasion arms race between Tomato mosaic virus and the resistance gene Tm-1. <i> Ishibashi K, Kezuka Y, Kobayashi C, Kato M, Inoue T, Nonaka T, Ishikawa M, Matsumura H, Katoh E. </i> Proc Natl Acad Sci U S A, 2014","date":"2023-01-31T15:04:54.991Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3WRW"},{"db":"PDB","id":"3WRY"},{"db":"PDB","id":"3WRX"}],"region_id":"DP03943r002","statement":[{"text":"No dramatic structural differences were found for free and ToMV-Hel–bound Tm-1(431) (Cα rmsd, 1.004 Å), although a disorder-to-order transition involving residues L80–A89 and changes in the orientations of the side chains involved in ATPγS binding were observed (Fig. 4A). ","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P03587"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-01-31T15:20:45.130Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MATAQSNSPRVFCIGTADTKFDELRFLSEHVRSSLNSFSNKSSFKVGVTVVDVSTSWKETNSCADFDFVPSKDVLSCHTLGEETMGTFADIRGLAIAIMSKALETFLSIANDEQNLAGVIGLGGSGGTSLLSSAFRSLPIGIPKVIISTVASGQTESYIGTSDLVLFPSVVDICGINNVSKVVLSNAGAAFAGMVIGRLESSKEHSITNGKFTVGVTMFGVTTPCVNAVKERLVKEGYETLVFHATGVGGRAMEDLVRGGFIQGVLDITTTEVADYVVGGVMACDSSRFDAILEKKIPLVLSVGALDMVNFGPKTTIPPEFQQRKIHEHNEQVSLMRTTVGENKKFAAFIAEKLNKASSSVCVCLPEKGVSALDAPGKDFYDPEATSCLTRELQMLLENNERCQVKVLPYHINDAEFANALVDSFLEISPKSRHVECQPAESKSIQDIQNDNAVLEKYPSCNGKNFSRLNDFPNAKPETLQKRTVILQKLKDQISKGKPIIGAGAGTGISAKFEEAGGVDLIVLYNSGRFRMAGRGSLAGLLPFADANAIVLEMANEVLPVVKEVAVLAGVCATDPFRRMDNFLKQLESVGFCGVQNFPTVGLFDGNFRQNLEETGMGYGLEVEMIAAAHRMGLLTTPYAFCPDEAVAMAEAGADIIVAHMGLTTSGSIGAKTAVSLEESVTCVQAIADATHRIYPDAIVLCHGGPISSPEEAAYVLKRTTGVHGFYGASSMERLPVEQAITATVQQYKSISME","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","lamiids","Solanales","Solanaceae","Solanoideae","Solaneae","Solanum","Solanum subgen. Lycopersicon"],"alphafold_very_low_content":0.0649867374005305,"dataset":["Stress response proteins"],"disorder_content":0.013262599469496022,"disprot_consensus":{"full":[{"start":80,"end":89,"type":"T"}],"Structural state":[{"start":80,"end":89,"type":"D"}],"Structural transition":[{"start":80,"end":89,"type":"T"}]}},{"disprot_id":"DP03944","acc":"P19525","creator":"fkordevani","date":"2023-02-06T15:40:22.812Z","features":{"pfam":[{"id":"PF00035","name":"Double-stranded RNA binding motif","start":13,"end":75},{"id":"PF00035","name":"Double-stranded RNA binding motif","start":101,"end":164},{"id":"PF00069","name":"Protein kinase domain","start":267,"end":534}],"gene3D":[]},"genes":[{"name":{"value":"EIF2AK2"},"synonyms":[{"value":"PKR"},{"value":"PRKR"}]}],"length":551,"name":"Interferon-induced, double-stranded RNA-activated protein kinase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":229,"end":255,"reference_id":"31246429","reference_source":"pmid","reference_html":"Structural Basis of Protein Kinase R Autophosphorylation. <i> Mayo CB, Erlandsen H, Mouser DJ, Feinstein AG, Robinson VL, May ER, Cole JL. </i> Biochemistry, 2019","date":"2023-02-13T13:32:10.749Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6D3K"},{"db":"PDB","id":"6D3L"}],"region_id":"DP03944r001","statement":[{"text":"Residues 256–257, 441–450, and 335–355 from chain A, 255, 334–355, and 439–451 from chain B, and 334–356, 441–444, and 449 from chain C were inserted and Prime version 1 (Schrödinger, LLC)44 was used to generate a configuration of the missing loops.","type":"Methods"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1061"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-13T16:23:53.937Z"}},{"start":337,"end":355,"reference_id":"31246429","reference_source":"pmid","reference_html":"Structural Basis of Protein Kinase R Autophosphorylation. <i> Mayo CB, Erlandsen H, Mouser DJ, Feinstein AG, Robinson VL, May ER, Cole JL. </i> Biochemistry, 2019","date":"2023-02-13T13:33:31.232Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6D3K"},{"db":"PDB","id":"6D3L"}],"region_id":"DP03944r002","statement":[{"text":"Residues 256–257, 441–450, and 335–355 from chain A, 255, 334–355, and 439–451 from chain B, and 334–356, 441–444, and 449 from chain C were inserted and Prime version 1 (Schrödinger, LLC)44 was used to generate a configuration of the missing loops.","type":"Methods"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1061"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-13T16:23:58.563Z"}},{"start":441,"end":451,"reference_id":"31246429","reference_source":"pmid","reference_html":"Structural Basis of Protein Kinase R Autophosphorylation. <i> Mayo CB, Erlandsen H, Mouser DJ, Feinstein AG, Robinson VL, May ER, Cole JL. </i> Biochemistry, 2019","date":"2023-05-19T08:55:19.893Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6D3K"},{"db":"PDB","id":"6D3L"}],"region_id":"DP03944r003","statement":[{"text":"Thus, it is noteworthy that helix αG occupies that same position in the absence of substrate. As is typical of structures of unphosphorylated protein kinases, portions of the activation loop are disordered (A: 441–450, B:440–450), but in chain C a shorter region is disordered (447–449). ","type":"Results"},{"text":"Residues 256–257, 441–450, and 335–355 from chain A, 255, 334–355, and 439–451 from chain B, and 334–356, 441–444, and 449 from chain C were inserted and Prime version 1 (Schrödinger, LLC)44 was used to generate a configuration of the missing loops.","type":"Methods"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1061"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-19T15:31:21.627Z"}},{"start":542,"end":551,"reference_id":"31246429","reference_source":"pmid","reference_html":"Structural Basis of Protein Kinase R Autophosphorylation. <i> Mayo CB, Erlandsen H, Mouser DJ, Feinstein AG, Robinson VL, May ER, Cole JL. </i> Biochemistry, 2019","date":"2023-02-13T13:39:17.708Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6D3L"}],"region_id":"DP03944r004","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-13T16:24:10.599Z"}},{"start":170,"end":251,"reference_id":"17284445","reference_source":"pmid","reference_html":"Molecular framework for the activation of RNA-dependent protein kinase. <i> McKenna SA, Lindhout DA, Kim I, Liu CW, Gelev VM, Wagner G, Puglisi JD. </i> J Biol Chem, 2007","date":"2023-05-19T08:54:08.949Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP03944r005","statement":[{"text":"The 81-amino-acid linker (residues 170-251) is acidic (estimated pI of 4.3) and hydrophilic, with 24 serines and threonines. Both the kinase and the dsRBD domains are basic and structured. Our NMR data strongly suggest that the linker region is mainly unstructured in PKR.","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-19T15:30:59.843Z"}},{"start":170,"end":251,"reference_id":"17284445","reference_source":"pmid","reference_html":"Molecular framework for the activation of RNA-dependent protein kinase. <i> McKenna SA, Lindhout DA, Kim I, Liu CW, Gelev VM, Wagner G, Puglisi JD. </i> J Biol Chem, 2007","date":"2023-05-19T08:53:53.226Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP03944r006","statement":[{"text":"The 81-amino-acid linker (residues 170-251) is acidic (estimated pI of 4.3) and hydrophilic, with 24 serines and threonines. Both the kinase and the dsRBD domains are basic and structured. Our NMR data strongly suggest that the linker region is mainly unstructured in PKR.","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-19T15:30:55.890Z"}},{"start":80,"end":100,"reference_id":"9736623","reference_source":"pmid","reference_html":"Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation. <i> Nanduri S, Carpick BW, Yang Y, Williams BR, Qin J. </i> EMBO J, 1998","date":"2023-05-19T08:53:16.834Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP03944r007","statement":[{"text":"The linker between the two dsRBMs was found to be long and highly flexible, as shown by the random chemical shift nature, small and negative heteronuclear amide 1H{15N} nuclear Overhauser effects (NOEs) in this region (Figure 3). In fact, no long-range NOEs and few medium-range NOEs were identified in this region due to its high flexibility.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"1QU6"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-19T15:30:41.184Z"}},{"start":80,"end":100,"reference_id":"9736623","reference_source":"pmid","reference_html":"Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation. <i> Nanduri S, Carpick BW, Yang Y, Williams BR, Qin J. </i> EMBO J, 1998","date":"2023-05-19T08:53:28.559Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP03944r008","statement":[{"text":"The linker between the two dsRBMs was found to be long and highly flexible, as shown by the random chemical shift nature, small and negative heteronuclear amide 1H{15N} nuclear Overhauser effects (NOEs) in this region (Figure 3). In fact, no long-range NOEs and few medium-range NOEs were identified in this region due to its high flexibility.","type":"Results"},{"text":"The structure of dsRBD exhibits a dumb-bell shape, with the two dsRBMs flanking a 22 residue linker region (Figure 2A).","type":"Results"}],"cross_refs":[{"db":"PDB","id":"1QU6"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-19T15:30:45.702Z"}},{"start":444,"end":448,"reference_id":"17284445","reference_source":"pmid","reference_html":"Molecular framework for the activation of RNA-dependent protein kinase. <i> McKenna SA, Lindhout DA, Kim I, Liu CW, Gelev VM, Wagner G, Puglisi JD. </i> J Biol Chem, 2007","date":"2023-05-19T09:02:29.284Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr446Ala","start":null,"end":null,"position":null}],"region_id":"DP03944r009","statement":[{"text":"Finally, mutations at either or both of two key phosphorylation sites in the activation loop (T446A and T451A) result in attenuation of phosphorylation by PKRP.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-19T15:56:50.353Z"}},{"start":446,"end":451,"reference_id":"17284445","reference_source":"pmid","reference_html":"Molecular framework for the activation of RNA-dependent protein kinase. <i> McKenna SA, Lindhout DA, Kim I, Liu CW, Gelev VM, Wagner G, Puglisi JD. </i> J Biol Chem, 2007","date":"2023-05-19T09:03:25.453Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr451Ala","start":null,"end":null,"position":null}],"region_id":"DP03944r010","statement":[{"text":"Finally, mutations at either or both of two key phosphorylation sites in the activation loop (T446A and T451A) result in attenuation of phosphorylation by PKRP.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-19T15:32:16.144Z"}}],"regions_counter":10,"released":"2023_06","sequence":"MAGDLSAGFFMEELNTYRQKQGVVLKYQELPNSGPPHDRRFTFQVIIDGREFPEGEGRSKKEAKNAAAKLAVEILNKEKKAVSPLLLTTTNSSEGLSMGNYIGLINRIAQKKRLTVNYEQCASGVHGPEGFHYKCKMGQKEYSIGTGSTKQEAKQLAAKLAYLQILSEETSVKSDYLSSGSFATTCESQSNSLVTSTLASESSSEGDFSADTSEINSNSDSLNSSSLLMNGLRNNQRKAKRSLAPRFDLPDMKETKYTVDKRFGMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKLDHVNIVHYNGCWDGFDYDPETSDDSLESSDYDPENSKNSSRSKTKCLFIQMEFCDKGTLEQWIEKRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETSKFFTDLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEILRTLTVWKKSPEKNERHTC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Autophagy-related proteins","RNA-binding proteins"],"alphafold_very_low_content":0.20508166969147004,"disorder_content":0.26678765880217786,"disprot_consensus":{"full":[{"start":80,"end":100,"type":"D"},{"start":170,"end":255,"type":"D"},{"start":337,"end":355,"type":"D"},{"start":441,"end":451,"type":"D"},{"start":542,"end":551,"type":"D"}],"Structural state":[{"start":80,"end":100,"type":"D"},{"start":170,"end":255,"type":"D"},{"start":337,"end":355,"type":"D"},{"start":441,"end":451,"type":"D"},{"start":542,"end":551,"type":"D"}],"Disorder function":[{"start":80,"end":100,"type":"F"},{"start":170,"end":251,"type":"F"},{"start":444,"end":451,"type":"F"}]}},{"disprot_id":"DP03945","acc":"Q16620","creator":"fkordevani","date":"2023-02-06T16:22:33.188Z","features":{"pfam":[{"id":"PF01462","name":"Leucine rich repeat N-terminal domain","start":31,"end":60},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":204,"end":283},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":306,"end":374},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":539,"end":806},{"id":"PF13855","name":"Leucine rich repeat","start":92,"end":149},{"id":"PF16920","name":"Leucine rich repeat C-terminal motif","start":151,"end":195}],"gene3D":[]},"genes":[{"name":{"value":"NTRK2"},"synonyms":[{"value":"TRKB"}]}],"length":822,"name":"BDNF/NT-3 growth factors receptor","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":385,"end":426,"reference_id":"28351853","reference_source":"pmid","reference_html":"Pharmaceutical Characterization of Tropomyosin Receptor Kinase B-Agonistic Antibodies on Human Induced Pluripotent Stem (hiPS) Cell-Derived Neurons. <i> Traub S, Stahl H, Rosenbrock H, Simon E, Florin L, Hospach L, Hörer S, Heilker R. </i> J Pharmacol Exp Ther, 2017","date":"2023-02-13T13:41:19.244Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5MO9"}],"region_id":"DP03945r001","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ABCD","id":"ABCD_AG424"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-13T16:25:16.315Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MSSWIRWHGPAMARLWGFCWLVVGFWRAAFACPTSCKCSASRIWCSDPSPGIVAFPRLEPNSVDPENITEIFIANQKRLEIINEDDVEAYVGLRNLTIVDSGLKFVAHKAFLKNSNLQHINFTRNKLTSLSRKHFRHLDLSELILVGNPFTCSCDIMWIKTLQEAKSSPDTQDLYCLNESSKNIPLANLQIPNCGLPSANLAAPNLTVEEGKSITLSCSVAGDPVPNMYWDVGNLVSKHMNETSHTQGSLRITNISSDDSGKQISCVAENLVGEDQDSVNLTVHFAPTITFLESPTSDHHWCIPFTVKGNPKPALQWFYNGAILNESKYICTKIHVTNHTEYHGCLQLDNPTHMNNGDYTLIAKNEYGKDEKQISAHFMGWPGIDDGANPNYPDVIYEDYGTAANDIGDTTNRSNEIPSTDVTDKTGREHLSVYAVVVIASVVGFCLLVMLFLLKLARHSKFGMKGPASVISNDDDSASPLHHISNGSNTPSSSEGGPDAVIIGMTKIPVIENPQYFGITNSQLKPDTFVQHIKRHNIVLKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLKDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMAEGNPPTELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTCPQEVYELMLGCWQREPHMRKNIKGIHTLLQNLAKASPVYLDILG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.18856447688564476,"disorder_content":0.051094890510948905,"disprot_consensus":{"full":[{"start":385,"end":426,"type":"D"}],"Structural state":[{"start":385,"end":426,"type":"D"}]}},{"disprot_id":"DP03946","acc":"Q9Y6K1","creator":"fkordevani","date":"2023-02-07T15:32:04.498Z","features":{"pfam":[{"id":"PF00145","name":"C-5 cytosine-specific DNA methylase","start":634,"end":766},{"id":"PF00855","name":"PWWP domain","start":293,"end":374},{"id":"PF17980","name":"DNMT3, cysteine rich ADD domain, GATA1-like zinc finger","start":475,"end":530},{"id":"PF21255","name":"DNMT3, ADD PHD zinc finger","start":537,"end":586},{"id":"PF22855","name":"DNA (cytosine-5-)-methyltransferase, N-terminal","start":4,"end":284}],"gene3D":[]},"genes":[{"name":{"value":"DNMT3A"}}],"length":912,"name":"DNA (cytosine-5)-methyltransferase 3A","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":831,"end":846,"reference_id":"25383530","reference_source":"pmid","reference_html":"Structural insight into autoinhibition and histone H3-induced activation of DNMT3A. <i> Guo X, Wang L, Li J, Ding Z, Xiao J, Yin X, He S, Shi P, Dong L, Li G, Tian C, Wang J, Cong Y, Xu Y. </i> Nature, 2015","date":"2023-05-18T15:22:59.798Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4U7T"},{"db":"PDB","id":"4U7P"}],"region_id":"DP03946r001","statement":[{"text":"Residues on the missing loop (residues 831–846) were mutated for the in vitro DNA methyltransferase activity assay.","type":"Supplementary material"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UJW3"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:439155"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84243"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-19T15:30:06.278Z"}},{"start":455,"end":473,"reference_id":"25383530","reference_source":"pmid","reference_html":"Structural insight into autoinhibition and histone H3-induced activation of DNMT3A. <i> Guo X, Wang L, Li J, Ding Z, Xiao J, Yin X, He S, Shi P, Dong L, Li G, Tian C, Wang J, Cong Y, Xu Y. </i> Nature, 2015","date":"2023-02-13T13:48:44.930Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4U7P"}],"region_id":"DP03946r002","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UJW3"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:439155"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-13T16:28:48.662Z"}},{"start":831,"end":846,"reference_id":"29414941","reference_source":"pmid","reference_html":"Structural basis for DNMT3A-mediated de novo DNA methylation. <i> Zhang ZM, Lu R, Wang P, Yu Y, Chen D, Gao L, Liu S, Ji D, Rothbart SB, Wang Y, Wang GG, Song J. </i> Nature, 2018","date":"2023-05-22T13:00:24.796Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6F57"},{"db":"PDB","id":"5YX2"},{"db":"DisProt","id":"DP03946r001"}],"region_id":"DP03946r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:439155"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"For the covalent DNMT3A–DNMT3L–DNA complex (PDB 6F57), a 11-mer single-stranded DNA that was in-house synthesized to contain 2′-deoxy-Zebularine (5′- CATGdZGCTCTC -3′, dZ = 2′-deoxy-Zebularine) annealed to a 10-mer single-stranded DNA (5′- AGAGCGCATG -3′). For the Crystal structure of DNMT3A-DNMT3L in complex with DNA containing two CpG sites (PDB 5YX2) a 25-mer Zebularine-containing DNA (5′- GCATGZGTTCTAATTAGAACGCATG -3′, Z = Zebularine) was self-annealed."}]}],"statement":[{"text":"DNMT3A binding to DNA is mainly mediated by a loop from the target recognition domain (TRD) (residues R831-F848), the catalytic loop (residues G707-K721) and the homodimeric interface of DNMT3A, which together create a continuous DNA-binding surface (Fig. 1d, 2a).  Accordingly, these segments exhibit the most prominent structural changes upon DNA binding – the TRD loop lacked electron density in the DNA-free structure of DNMT3A–DNMT3L11, 12, but became well defined upon DNA binding and penetrated into the DNA major groove for intermolecular contacts (Fig. 2a–c); additionally, the TRD loop is stabilized through hydrogen-bonding interactions with R882, the DNMT3A mutational hotspot among leukemias9, 10, and Q886 from an adjacent helix (Fig. 2c).","type":"Results"},{"text":"The authors are referring to the 831–846 region described in the cited publication (PMID 25383530) as disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-22T13:15:27.183Z"}},{"start":831,"end":846,"reference_id":"29414941","reference_source":"pmid","reference_html":"Structural basis for DNMT3A-mediated de novo DNA methylation. <i> Zhang ZM, Lu R, Wang P, Yu Y, Chen D, Gao L, Liu S, Ji D, Rothbart SB, Wang Y, Wang GG, Song J. </i> Nature, 2018","date":"2023-05-22T13:05:02.311Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6F57"},{"db":"PDB","id":"5YX2"}],"ec_go":"EXP","region_id":"DP03946r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:439155"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"}],"statement":[{"text":"DNMT3A binding to DNA is mainly mediated by a loop from the target recognition domain (TRD) (residues R831-F848), the catalytic loop (residues G707-K721) and the homodimeric interface of DNMT3A, which together create a continuous DNA-binding surface (Fig. 1d, 2a). Accordingly, these segments exhibit the most prominent structural changes upon DNA binding – the TRD loop lacked electron density in the DNA-free structure of DNMT3A–DNMT3L11, 12, but became well defined upon DNA binding and penetrated into the DNA major groove for intermolecular contacts (Fig. 2a–c); additionally, the TRD loop is stabilized through hydrogen-bonding interactions with R882, the DNMT3A mutational hotspot among leukemias9, 10, and Q886 from an adjacent helix (Fig. 2c).","type":"Results"},{"text":"The authors are referring to the 831–846 region described in the cited publication (PMID 25383530) as disordered.","type":"Curator statement"},{"text":"For the covalent DNMT3A–DNMT3L–DNA complex (PDB 6F57), a 11-mer single-stranded DNA that was in-house synthesized to contain 2′-deoxy-Zebularine (5′- CATGdZGCTCTC -3′, dZ = 2′-deoxy-Zebularine) annealed to a 10-mer single-stranded DNA (5′- AGAGCGCATG -3′). For the Crystal structure of DNMT3A-DNMT3L in complex with DNA containing two CpG sites (PDB 5YX2) a 25-mer Zebularine-containing DNA (5′- GCATGZGTTCTAATTAGAACGCATG -3′, Z = Zebularine) was self-annealed.","type":"Curator statement"},{"text":"Formation of the DNMT3A–DNA complex is also supported by various protein–DNA interactions flanking CpG, which involve electrostatic and/or hydrogen-bonding interactions of the TRD residues (R831, T832, T835, N838 and K841), catalytic loop residues (N711, S714 and I715) and DNMT3A–DNMT3A homodimeric interface residues (S881, R882, L883 and R887) with various DNA backbone or base sites (Fig. 2a and Extended Data Fig. 3a–f).","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-22T13:15:23.814Z"}},{"start":831,"end":846,"reference_id":"29414941","reference_source":"pmid","reference_html":"Structural basis for DNMT3A-mediated de novo DNA methylation. <i> Zhang ZM, Lu R, Wang P, Yu Y, Chen D, Gao L, Liu S, Ji D, Rothbart SB, Wang Y, Wang GG, Song J. </i> Nature, 2018","date":"2023-05-22T13:01:06.645Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"GO:0045322","term_name":"unmethylated CpG binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6F57"},{"db":"PDB","id":"5YX2"}],"ec_go":"EXP","region_id":"DP03946r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:439155"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"}],"statement":[{"text":"DNMT3A binding to DNA is mainly mediated by a loop from the target recognition domain (TRD) (residues R831-F848), the catalytic loop (residues G707-K721) and the homodimeric interface of DNMT3A, which together create a continuous DNA-binding surface (Fig. 1d, 2a).  Accordingly, these segments exhibit the most prominent structural changes upon DNA binding – the TRD loop lacked electron density in the DNA-free structure of DNMT3A–DNMT3L11, 12, but became well defined upon DNA binding and penetrated into the DNA major groove for intermolecular contacts (Fig. 2a–c); additionally, the TRD loop is stabilized through hydrogen-bonding interactions with R882, the DNMT3A mutational hotspot among leukemias9, 10, and Q886 from an adjacent helix (Fig. 2c).","type":"Results"},{"text":"Recognition of CpG dinucleotides by DNMT3A is mediated by both catalytic and TRD loops. In particular, guanine of the target strand, G6 (G19′), is specified by a hydrogen bond between its O6 atom and the Nε atom of R836 from the TRD loop, as well as water-mediated hydrogen bonds between its N7 atom and the Nε and Oγ atoms of R836 and T834, respectively (Fig. 3a).","type":"Results"},{"text":"For the covalent DNMT3A–DNMT3L–DNA complex (PDB 6F57), a 11-mer single-stranded DNA that was in-house synthesized to contain 2′-deoxy-Zebularine (5′- CATGdZGCTCTC -3′, dZ = 2′-deoxy-Zebularine) annealed to a 10-mer single-stranded DNA (5′- AGAGCGCATG -3′). For the Crystal structure of DNMT3A-DNMT3L in complex with DNA containing two CpG sites (PDB 5YX2) a 25-mer Zebularine-containing DNA (5′- GCATGZGTTCTAATTAGAACGCATG -3′, Z = Zebularine) was self-annealed. Zebularine is a cytidine analog that acts as a methylation inhibitor.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to uan nmethylated CpG motif. Unmethylated CpG dinucleotides are often associated with gene promoters.\" [GOC:ai, PMID:10688657]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-22T13:15:23.191Z"}}],"regions_counter":6,"released":"2023_06","sequence":"MPAMPSSGPGDTSSSAAEREEDRKDGEEQEEPRGKEERQEPSTTARKVGRPGRKRKHPPVESGDTPKDPAVISKSPSMAQDSGASELLPNGDLEKRSEPQPEEGSPAGGQKGGAPAEGEGAAETLPEASRAVENGCCTPKEGRGAPAEAGKEQKETNIESMKMEGSRGRLRGGLGWESSLRQRPMPRLTFQAGDPYYISKRKRDEWLARWKREAEKKAKVIAGMNAVEENQGPGESQKVEEASPPAVQQPTDPASPTVATTPEPVGSDAGDKNATKAGDDEPEYEDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPMYRKAIYEVLQVASSRAGKLFPVCHDSDESDTAKAVEVQNKPMIEWALGGFQPSGPKGLEPPEEEKNPYKEVYTDMWVEPEAAAYAPPPPAKKPRKSTAEKPKVKEIIDERTRERLVYEVRQKCRNIEDICISCGSLNVTLEHPLFVGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLVGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHDQEFDPPKVYPPVPAEKRKPIRVLSLFDGIATGLLVLKDLGIQVDRYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEWGPFDLVIGGSPCNDLSIVNPARKGLYEGTGRLFFEFYRLLHDARPKEGDDRPFFWLFENVVAMGVSDKRDISRFLESNPVMIDAKEVSAAHRARYFWGNLPGMNRPLASTVNDKLELQECLEHGRIAKFSKVRTITTRSNSIKQGKDQHFPVFMNEKEDILWCTEMERVFGFPVHYTDVSNMSRLARQRLLGRSWSVPVIRHLFAPLKEYFACV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Cancer-related proteins"],"alphafold_very_low_content":0.3190789473684211,"disorder_content":0.03837719298245614,"disprot_consensus":{"full":[{"start":455,"end":473,"type":"D"},{"start":831,"end":846,"type":"T"}],"Structural state":[{"start":455,"end":473,"type":"D"},{"start":831,"end":846,"type":"D"}],"Structural transition":[{"start":831,"end":846,"type":"T"}],"Molecular function":[{"start":831,"end":846,"type":"F"}]}},{"disprot_id":"DP03947","acc":"P0A8J8","creator":"vnugnes","date":"2023-02-07T16:44:07.826Z","features":{"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":33,"end":206},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":242,"end":351}],"gene3D":[]},"genes":[{"name":{"value":"rhlB","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00661","url":"https://hamap.expasy.org/unirule/MF_00661"}}]},"synonyms":[{"value":"mmrA"}],"olnNames":[{"value":"b3780"},{"value":"JW3753"}]}],"length":421,"name":"ATP-dependent RNA helicase RhlB","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":404,"end":421,"reference_id":"15236960","reference_source":"pmid","reference_html":"Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. <i> Callaghan AJ, Aurikko JP, Ilag LL, Günter Grossmann J, Chandran V, Kühnel K, Poljak L, Carpousis AJ, Robinson CV, Symmons MF, Luisi BF. </i> J Mol Biol, 2004","date":"2023-02-07T16:48:21.074Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03947r001","statement":[{"text":"Limited protease digestion shows that the highly basic C-terminal 2 kDa fragment of the helicase is readily cleaved by trypsin (residues 403–420, confirmed by mass spectrometry analysis) and that the core of the protein is comparatively more resistant to further digestion (results not shown).","type":"Results"},{"text":"Authors are referring to the 404-421 region since they are not considering the first Met residue.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-02-13T13:22:32.314Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MSKTHLTEQKFSDFALHPKVVEALEKKGFHNCTPIQALALPLTLAGRDVAGQAQTGTGKTMAFLTSTFHYLLSHPAIADRKVNQPRALIMAPTRELAVQIHADAEPLAEATGLKLGLAYGGDGYDKQLKVLESGVDILIGTTGRLIDYAKQNHINLGAIQVVVLDEADRMYDLGFIKDIRWLFRRMPPANQRLNMLFSATLSYRVRELAFEQMNNAEYIEVEPEQKTGHRIKEELFYPSNEEKMRLLQTLIEEEWPDRAIIFANTKHRCEEIWGHLAADGHRVGLLTGDVAQKKRLRILDEFTRGDLDILVATDVAARGLHIPAVTHVFNYDLPDDCEDYVHRIGRTGRAGASGHSISLACEEYALNLPAIETYIGHSIPVSKYNPDALMTDLPKPLRLTRPRTGNGPRRTGAPRNRRRSG","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"alphafold_very_low_content":0.04513064133016627,"dataset":["RNA-binding proteins"],"disorder_content":0.04275534441805225,"disprot_consensus":{"full":[{"start":404,"end":421,"type":"D"}],"Structural state":[{"start":404,"end":421,"type":"D"}]}},{"disprot_id":"DP03948","acc":"Q8WQM8","creator":"cpintado","date":"2023-02-08T14:41:38.949Z","features":{"pfam":[{"id":"PF00210","name":"Ferritin-like domain","start":34,"end":170}],"gene3D":[]},"genes":[{"name":{"value":"Artn","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAL55397.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAL55397.1"}}]}}],"length":230,"name":"Ferritin","ncbi_taxon_id":6661,"organism":"Artemia franciscana","regions":[{"start":1,"end":28,"reference_id":"36518848","reference_source":"pmid","reference_html":"Cryo-EM structure of the diapause chaperone artemin. <i> Parvate AD, Powell SM, Brookreson JT, Moser TH, Novikova IV, Zhou M, Evans JE. </i> Front Mol Biosci, 2022","date":"2023-04-25T15:39:41.536Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7RVB"},{"db":"EMDB","id":"24706"}],"region_id":"DP03948r001","statement":[{"text":"Major differences arise due to artemin having a 28 residue long disordered N-terminus region as well as an additional helix (F) and a second long disordered loop (L′) (Figure 2A, Supplementary Figure S3).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-25T15:43:26.076Z"}},{"start":194,"end":214,"reference_id":"36518848","reference_source":"pmid","reference_html":"Cryo-EM structure of the diapause chaperone artemin. <i> Parvate AD, Powell SM, Brookreson JT, Moser TH, Novikova IV, Zhou M, Evans JE. </i> Front Mol Biosci, 2022","date":"2023-04-25T15:39:52.605Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7RVB"},{"db":"EMDB","id":"24706"}],"region_id":"DP03948r002","statement":[{"text":"Major differences arise due to artemin having a 28 residue long disordered N-terminus region as well as an additional helix (F) and a second long disordered loop (L′) (Figure 2A, Supplementary Figure S3).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-25T15:43:28.359Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MATEGARNIGQSAPEGKVQMDCPSRHNFDPECEKAFVEHIHLELASSYHAWSMWAFYARDCKAAVGMTRLCEWASHVSAQRARRMAAYVLTRGGHVDYKEIPAPKKQGWDNFEDAFSHCVANKKRILTSLQSLYQCCQSKDAHCSNFIQTDMMDEVIAWNKFLSDCLSNLHCIGSQGMGPWVFDRWLARIVMSKFKHPKIPSLSTSDLESNIPNELFDAEGDMVRAIKKL","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Crustacea","Branchiopoda","Anostraca","Artemiidae","Artemia"],"alphafold_very_low_content":0.22608695652173913,"disorder_content":0.21304347826086956,"disprot_consensus":{"full":[{"start":1,"end":28,"type":"D"},{"start":194,"end":214,"type":"D"}],"Structural state":[{"start":1,"end":28,"type":"D"},{"start":194,"end":214,"type":"D"}]}},{"disprot_id":"DP03949","acc":"O15294-3","creator":"fkordevani","date":"2023-02-13T10:01:30.607Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"OGT"}}],"length":1036,"name":"Isoform 1 of UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":747,"end":760,"reference_id":"34764280","reference_source":"pmid","reference_html":"Cryo-EM structure provides insights into the dimer arrangement of the O-linked β-N-acetylglucosamine transferase OGT. <i> Meek RW, Blaza JN, Busmann JA, Alteen MG, Vocadlo DJ, Davies GJ. </i> Nat Commun, 2021","date":"2023-02-14T12:46:26.447Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7NTF"}],"region_id":"DP03949r004","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-14T13:08:34.748Z"}},{"start":1,"end":78,"reference_id":"34764280","reference_source":"pmid","reference_html":"Cryo-EM structure provides insights into the dimer arrangement of the O-linked β-N-acetylglucosamine transferase OGT. <i> Meek RW, Blaza JN, Busmann JA, Alteen MG, Vocadlo DJ, Davies GJ. </i> Nat Commun, 2021","date":"2023-02-13T10:15:45.289Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7NTF"}],"region_id":"DP03949r005","statement":[{"text":"We note that without crystal formation, TPR units N-terminal of the dimer interface exhibit considerably conformational heterogeneity and could only be partly resolved by particle subtraction, hinting that flexibility in this section may play a role in how OGT selects larger substrates.","type":"Discussion"},{"text":"Early maps generated during data processing provided density into which only the catalytic domain appended to TPR units 6-13.5 could be modelled, TPR units N-terminal of the dimer interface (TPRs 1–5) exhibited high heterogeneity, suggestive of flexibility in the TPR units of this region.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-02-13T16:46:37.896Z"}}],"regions_counter":5,"released":"2023_06","sequence":"MASSVGNVADSTGLAELAHREYQAGDFEAAERHCMQLWRQEPDNTGVLLLLSSIHFQCRRLDRSAHFSTLAIKQNPLLAEAYSNLGNVYKERGQLQEAIEHYRHALRLKPDFIDGYINLAAALVAAGDMEGAVQAYVSALQYNPDLYCVRSDLGNLLKALGRLEEAKACYLKAIETQPNFAVAWSNLGCVFNAQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARIFDRAVAAYLRALSLSPNHAVVHGNLACVYYEQGLIDLAIDTYRRAIELQPHFPDAYCNLANALKEKGSVAEAEDCYNTALRLCPTHADSLNNLANIKREQGNIEEAVRLYRKALEVFPEFAAAHSNLASVLQQQGKLQEALMHYKEAIRISPTFADAYSNMGNTLKEMQDVQGALQCYTRAIQINPAFADAHSNLASIHKDSGNIPEAIASYRTALKLKPDFPDAYCNLAHCLQIVCDWTDYDERMKKLVSIVADQLEKNRLPSVHPHHSMLYPLSHGFRKAIAERHGNLCLDKINVLHKPPYEHPKDLKLSDGRLRVGYVSSDFGNHPTSHLMQSIPGMHNPDKFEVFCYALSPDDGTNFRVKVMAEANHFIDLSQIPCNGKAADRIHQDGIHILVNMNGYTKGARNELFALRPAPIQAMWLGYPGTSGALFMDYIITDQETSPAEVAEQYSEKLAYMPHTFFIGDHANMFPHLKKKAVIDFKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVKMKCPDGGDNADSSNTALNMPVIPMNTIAEAVIEMINRGQIQITINGFSISNGLATTQINNKAATGEEVPRTIIVTTRSQYGLPEDAIVYCNFNQLYKIDPSTLQMWANILKRVPNSVLWLLRFPAVGEPNIQQYAQNMGLPQNRIIFSPVAPKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAASQLTCLGCLELIAKNRQEYEDIAVKLGTDLEYLKKVRGKVWKQRISSPLFNTKQYTMELERLYLQMWEHYAAGNKPDHMIKPVEVTESA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"disorder_content":0.0888030888030888,"disprot_consensus":{"full":[{"start":1,"end":78,"type":"D"},{"start":747,"end":760,"type":"D"}],"Structural state":[{"start":1,"end":78,"type":"D"},{"start":747,"end":760,"type":"D"}]}},{"disprot_id":"DP03950","acc":"Q02020","creator":"vnugnes","date":"2023-02-15T14:59:24.108Z","features":{"pfam":[{"id":"PF00147","name":"Fibrinogen beta and gamma chains, C-terminal globular domain","start":212,"end":460},{"id":"PF08702","name":"Fibrinogen alpha/beta chain family","start":65,"end":208}],"gene3D":[]},"genes":[{"name":{"value":"FGB"}}],"length":463,"name":"Fibrinogen beta chain","ncbi_taxon_id":9031,"organism":"Gallus gallus","regions":[{"start":1,"end":61,"reference_id":"11601975","reference_source":"pmid","reference_html":"Crystal structure of native chicken fibrinogen at 2.7 A resolution. <i> Yang Z, Kollman JM, Pandi L, Doolittle RF. </i> Biochemistry, 2001","date":"2023-02-15T15:05:47.385Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1M1J"}],"region_id":"DP03950r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P14448"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"28009","entry_name":"N-acetyl-beta-D-glucosamine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"44278","entry_name":"N-acetyl-alpha-D-glucosamine"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O93568"}],"statement":[{"text":"The amino-terminal segments of the α and β chains, including fibrinopeptides A and B, are not visible in electron density maps, however, and must be highly disordered.","type":"Abstract"},{"text":"Electron density maps barely reveal the outlines of the disordered carboxyl regions of the α chains (Figure 2), and the amino-terminal segments of the α and β chains, including fibrinopeptides A and B, could not be resolved. The reasonable R-factors found after refinement (Table 1) indicate that these parts of the molecule do not contribute significantly to the diffraction and must be highly disordered. That the missing portions had not been lost to degradation during incubations leading to crystallization was ascertained by SDS gels and amino-terminal sequencing.","type":"Results"}]}],"regions_counter":1,"released":"2024_06","sequence":"ASVEYDNEEDSPQIDARAHRPLDKRQEAAPTLRPVAPPISGTGYQPRPPKQDKQAMKKGPIIYPDAGGCKHPLDELGVLCPTGCELQTTLLKQEKTVKPVLRDLKDRVAKFSDTSTTMYQYVNMIDNKLVKTQKQRKDNDIILSEYNTEMELHYNYIKDNLDNNIPSSLRVLRAVIDSLHKKIQKLENAIATQTDYCRSPCVASCNIPVVSGRECEDIYRKGGETSEMYIIQPDPFTTPYRVYCDMETDNGGWTLIQNRQDGSVNFGRAWDEYKRGFGNIAKSGGKKYCDTPGEYWLGNDKISQLTKIGPTKVLIEMEDWNGDKVSALYGGFTIHNEGNKYQLSVSNYKGNAGNALMEGASQLYGENRTMTIHNGMYFSTYDRDNDGWLTTDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGTYSWDMAKHGTDDGIVWMNWKGSWYSMKKMSMKIKPYFPD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Phasianinae","Gallus"],"alphafold_very_low_content":0.13390928725701945,"disorder_content":0.13174946004319654,"disprot_consensus":{"full":[{"start":1,"end":61,"type":"D"}],"Structural state":[{"start":1,"end":61,"type":"D"}]}},{"disprot_id":"DP03951","acc":"O93568","creator":"vnugnes","date":"2023-02-15T15:11:08.715Z","features":{"pfam":[{"id":"PF00147","name":"Fibrinogen beta and gamma chains, C-terminal globular domain","start":176,"end":414},{"id":"PF08702","name":"Fibrinogen alpha/beta chain family","start":31,"end":172}],"gene3D":[]},"genes":[],"length":435,"name":"Fibrinogen gamma chain","ncbi_taxon_id":9031,"organism":"Gallus gallus","regions":[{"start":420,"end":435,"reference_id":"11601975","reference_source":"pmid","reference_html":"Crystal structure of native chicken fibrinogen at 2.7 A resolution. <i> Yang Z, Kollman JM, Pandi L, Doolittle RF. </i> Biochemistry, 2001","date":"2023-02-15T15:17:50.744Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1M1J"}],"region_id":"DP03951r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P14448"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q02020"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"28009","entry_name":"N-acetyl-beta-D-glucosamine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"44278","entry_name":"N-acetyl-alpha-D-glucosamine"}],"statement":[{"text":"As such, almost 30% of the residues are missing (Table 1), mostly from the αC domain (272 residues), but also the amino-terminal segments of the three chains (96 residues all told) and the γ chain carboxyl-terminal segment (16 residues).","type":"Discussion"}]},{"start":30,"end":111,"reference_id":"11601975","reference_source":"pmid","reference_html":"Crystal structure of native chicken fibrinogen at 2.7 A resolution. <i> Yang Z, Kollman JM, Pandi L, Doolittle RF. </i> Biochemistry, 2001","date":"2023-02-15T15:48:11.849Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1M1J"}],"region_id":"DP03951r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P14448"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q02020"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"28009","entry_name":"N-acetyl-beta-D-glucosamine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"44278","entry_name":"N-acetyl-alpha-D-glucosamine"}],"statement":[{"text":"This region has high B-factor values, indicating this region is highly flexible and presumed as disordered. ","type":"Curator statement"}]}],"regions_counter":2,"released":"2024_06","sequence":"MMGVKSVTSRLAVGDLLSLLFSTSMAYIATRENCCILDERFGSYCPTTCGIADFFNKYRLTTDGELLEIEGLLQQATNSTGSIEYLIQHIKTIYPSEKQTLPQSIEQLTQKSKKIIEEIIRYENTILAHENTIQQLTDMHIMNSNKITQLKQKIAQLESHCQEPCKDTAEIQETTGRDCQDIANKGARKSGLYFIKPQKAKQSFLVYCEIDTYGNGWTVLQRRLDGSEDFRRNWVQYKEGFGHLSPDDTTEFWLGNEKIHLITTQSTLPYALRIELEDWSGKKGTADYAVFKVGTEEDKYRLTYAYFIGGERGDAFDGFNFGDDPSDKSYTYHNGMRFSTFDNDNDNFEGNCAEQDGSGWWMNRCHAGHLNGPYYIGGVYSRDTGTNSYDNGIIWATWRDRWYSMKKTTMKIIPFNRLSIDGQQHSGGLKQVGDS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Archelosauria","Archosauria","Dinosauria","Saurischia","Theropoda","Coelurosauria","Aves","Neognathae","Galloanserae","Galliformes","Phasianidae","Phasianinae","Gallus"],"alphafold_very_low_content":0.09195402298850575,"disorder_content":0.22528735632183908,"disprot_consensus":{"full":[{"start":30,"end":111,"type":"D"},{"start":420,"end":435,"type":"D"}],"Structural state":[{"start":30,"end":111,"type":"D"},{"start":420,"end":435,"type":"D"}]}},{"disprot_id":"DP03952","acc":"Q13224","creator":"fkordevani","date":"2023-02-21T09:24:49.642Z","features":{"pfam":[{"id":"PF00060","name":"Ligand-gated ion channel","start":556,"end":829},{"id":"PF01094","name":"Receptor family ligand binding region","start":108,"end":316},{"id":"PF10565","name":"N-methyl D-aspartate receptor 2B3 C-terminus","start":840,"end":1484},{"id":"PF10613","name":"Ligated ion channel L-glutamate- and glycine-binding site","start":455,"end":540}],"gene3D":[]},"genes":[{"name":{"value":"GRIN2B"},"synonyms":[{"value":"NMDAR2B"}]}],"length":1484,"name":"Glutamate receptor ionotropic, NMDA 2B","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":33,"reference_id":"34321660","reference_source":"pmid","reference_html":"Structural basis of ketamine action on human NMDA receptors. <i> Zhang Y, Ye F, Zhang T, Lv S, Zhou L, Du D, Lin H, Guo F, Luo C, Zhu S. </i> Nature, 2021","date":"2023-05-04T08:53:35.217Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7EU8"},{"db":"EMDB","id":"EMD-31309"}],"region_id":"DP03952r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q05586 "},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:182137"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T13:54:18.587Z"}},{"start":201,"end":212,"reference_id":"34321660","reference_source":"pmid","reference_html":"Structural basis of ketamine action on human NMDA receptors. <i> Zhang Y, Ye F, Zhang T, Lv S, Zhou L, Du D, Lin H, Guo F, Luo C, Zhu S. </i> Nature, 2021","date":"2023-05-04T08:54:08.308Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7EU8"},{"db":"EMDB","id":"EMD-31309"}],"region_id":"DP03952r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q05586 "},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:182137"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T13:54:18.831Z"}},{"start":393,"end":402,"reference_id":"34321660","reference_source":"pmid","reference_html":"Structural basis of ketamine action on human NMDA receptors. <i> Zhang Y, Ye F, Zhang T, Lv S, Zhou L, Du D, Lin H, Guo F, Luo C, Zhu S. </i> Nature, 2021","date":"2023-05-04T08:54:30.188Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7EU8"},{"db":"EMDB","id":"EMD-31309"}],"region_id":"DP03952r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q05586 "},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:182137"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T13:54:20.226Z"}},{"start":580,"end":599,"reference_id":"34321660","reference_source":"pmid","reference_html":"Structural basis of ketamine action on human NMDA receptors. <i> Zhang Y, Ye F, Zhang T, Lv S, Zhou L, Du D, Lin H, Guo F, Luo C, Zhu S. </i> Nature, 2021","date":"2023-05-04T08:54:44.477Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7EU8"},{"db":"EMDB","id":"EMD-31309"}],"region_id":"DP03952r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q05586 "},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:182137"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T13:54:21.616Z"}}],"regions_counter":4,"released":"2023_06","sequence":"MKPRAECCSPKFWLVLAVLAVSGSRARSQKSPPSIGIAVILVGTSDEVAIKDAHEKDDFHHLSVVPRVELVAMNETDPKSIITRICDLMSDRKIQGVVFADDTDQEAIAQILDFISAQTLTPILGIHGGSSMIMADKDESSMFFQFGPSIEQQASVMLNIMEEYDWYIFSIVTTYFPGYQDFVNKIRSTIENSFVGWELEEVLLLDMSLDDGDSKIQNQLKKLQSPIILLYCTKEEATYIFEVANSVGLTGYGYTWIVPSLVAGDTDTVPAEFPTGLISVSYDEWDYGLPARVRDGIAIITTAASDMLSEHSFIPEPKSSCYNTHEKRIYQSNMLNRYLINVTFEGRNLSFSEDGYQMHPKLVIILLNKERKWERVGKWKDKSLQMKYYVWPRMCPETEEQEDDHLSIVTLEEAPFVIVESVDPLSGTCMRNTVPCQKRIVTENKTDEEPGYIKKCCKGFCIDILKKISKSVKFTYDLYLVTNGKHGKKINGTWNGMIGEVVMKRAYMAVGSLTINEERSEVVDFSVPFIETGISVMVSRSNGTVSPSAFLEPFSADVWVMMFVMLLIVSAVAVFVFEYFSPVGYNRCLADGREPGGPSFTIGKAIWLLWGLVFNNSVPVQNPKGTTSKIMVSVWAFFAVIFLASYTANLAAFMIQEEYVDQVSGLSDKKFQRPNDFSPPFRFGTVPNGSTERNIRNNYAEMHAYMGKFNQRGVDDALLSLKTGKLDAFIYDAAVLNYMAGRDEGCKLVTIGSGKVFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALWLTGICHNEKNEVMSSQLDIDNMAGVFYMLGAAMALSLITFICEHLFYWQFRHCFMGVCSGKPGMVFSISRGIYSCIHGVAIEERQSVMNSPTATMNNTHSNILRLLRTAKNMANLSGVNGSPQSALDFIRRESSVYDISEHRRSFTHSDCKSYNNPPCEENLFSDYISEVERTFGNLQLKDSNVYQDHYHHHHRPHSIGSASSIDGLYDCDNPPFTTQSRSISKKPLDIGLPSSKHSQLSDLYGKFSFKSDRYSGHDDLIRSDVSDISTHTVTYGNIEGNAAKRRKQQYKDSLKKRPASAKSRREFDEIELAYRRRPPRSPDHKRYFRDKEGLRDFYLDQFRTKENSPHWEHVDLTDIYKERSDDFKRDSVSGGGPCTNRSHIKHGTGDKHGVVSGVPAPWEKNLTNVEWEDRSGGNFCRSCPSKLHNYSTTVTGQNSGRQACIRCEACKKAGNLYDISEDNSLQELDQPAAPVAVTSNASTTKYPQSPTNSKAQKKNRNKLRRQHSYDTFVDLQKEEAALAPRSVSLKDKGRFMDGSPYAHMFEMSAGESTFANNKSSVPTAGHHHHNNPGGGYMLSKSLYPDRVTQNPFIPTFGDDQCLLHGSKSYFFRQPTVAGASKARPDFRALVTNKPVVSALHGAVPARFQKDICIGNQSNPCVPNNKNPRAFNGSSNGHVYEKLSSIESDV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Age-related disorders proteins"],"alphafold_very_low_content":0.4440700808625337,"disorder_content":0.05053908355795148,"disprot_consensus":{"full":[{"start":1,"end":33,"type":"D"},{"start":201,"end":212,"type":"D"},{"start":393,"end":402,"type":"D"},{"start":580,"end":599,"type":"D"}],"Structural state":[{"start":1,"end":33,"type":"D"},{"start":201,"end":212,"type":"D"},{"start":393,"end":402,"type":"D"},{"start":580,"end":599,"type":"D"}]}},{"disprot_id":"DP03953","acc":"P43034","creator":"fkordevani","date":"2023-02-21T09:55:10.249Z","features":{"pfam":[{"id":"PF00400","name":"WD domain, G-beta repeat","start":102,"end":136},{"id":"PF00400","name":"WD domain, G-beta repeat","start":142,"end":178},{"id":"PF00400","name":"WD domain, G-beta repeat","start":183,"end":219},{"id":"PF00400","name":"WD domain, G-beta repeat","start":224,"end":261},{"id":"PF00400","name":"WD domain, G-beta repeat","start":267,"end":324},{"id":"PF00400","name":"WD domain, G-beta repeat","start":329,"end":366},{"id":"PF00400","name":"WD domain, G-beta repeat","start":371,"end":407},{"id":"PF24951","name":"PAC1 LisH domain","start":5,"end":39}],"gene3D":[]},"genes":[{"name":{"value":"PAFAH1B1","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03141","url":"https://hamap.expasy.org/unirule/MF_03141"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:8574","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8574"}}]},"synonyms":[{"value":"LIS1","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03141","url":"https://hamap.expasy.org/unirule/MF_03141"}}]},{"value":"MDCR"},{"value":"MDS"},{"value":"PAFAHA"}]}],"length":410,"name":"Platelet-activating factor acetylhydrolase IB subunit beta","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":298,"end":307,"reference_id":"36692009","reference_source":"pmid","reference_html":"Structures of human dynein in complex with the lissencephaly 1 protein, LIS1. <i> Reimer JM, DeSantis ME, Reck-Peterson SL, Leschziner AE. </i> Elife, 2023","date":"2023-05-04T08:57:51.464Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"8DYU"},{"db":"PDB","id":"8DYV"},{"db":"EMDB","id":"EMD-27783"},{"db":"EMDB","id":"EMD-27782"}],"region_id":"DP03953r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5957"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q14204"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T13:55:08.817Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDVNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHSGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.014634146341463415,"disorder_content":0.024390243902439025,"disprot_consensus":{"full":[{"start":298,"end":307,"type":"D"}],"Structural state":[{"start":298,"end":307,"type":"D"}]}},{"disprot_id":"DP03955","acc":"P33897","creator":"fkordevani","date":"2023-02-21T10:15:30.301Z","features":{"pfam":[{"id":"PF00005","name":"ABC transporter","start":492,"end":633},{"id":"PF06472","name":"ABC transporter transmembrane region 2","start":78,"end":352}],"gene3D":[]},"genes":[{"name":{"value":"ABCD1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:61","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:61"}}]},"synonyms":[{"value":"ALD"}]}],"length":745,"name":"ATP-binding cassette sub-family D member 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":2,"end":63,"reference_id":"34754073","reference_source":"pmid","reference_html":"Structural basis of acyl-CoA transport across the peroxisomal membrane by human ABCD1. <i> Wang R, Qin Y, Li X. </i> Cell Res, 2022","date":"2023-05-04T09:03:52.639Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7SHM"},{"db":"PDB","id":"7SHN"},{"db":"EMDB","id":"EMD-25130"},{"db":"EMDB","id":"EMD-25131"}],"region_id":"DP03955r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5957"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5497111"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"},{"text":"The N-terminal residues 1–66, a loop region (residues 357–365), and the C-terminal residues 708–745 were not resolved. Additionally, the hinge region (residues 437–462) between TMD and NBD was invisible in the electron density probably due to flexibility.","type":"Article"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T13:58:10.238Z"}},{"start":437,"end":461,"reference_id":"34754073","reference_source":"pmid","reference_html":"Structural basis of acyl-CoA transport across the peroxisomal membrane by human ABCD1. <i> Wang R, Qin Y, Li X. </i> Cell Res, 2022","date":"2023-05-04T09:02:51.332Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7SHM"},{"db":"PDB","id":"7SHN"},{"db":"EMDB","id":"EMD-25130"},{"db":"EMDB","id":"EMD-25131"}],"region_id":"DP03955r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5957"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5497111"}],"statement":[{"text":"The N-terminal residues 1–66, a loop region (residues 357–365), and the C-terminal residues 708–745 were not resolved. Additionally, the hinge region (residues 437–462) between TMD and NBD was invisible in the electron density probably due to flexibility.","type":"Article"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T13:58:12.308Z"}},{"start":353,"end":375,"reference_id":"34754073","reference_source":"pmid","reference_html":"Structural basis of acyl-CoA transport across the peroxisomal membrane by human ABCD1. <i> Wang R, Qin Y, Li X. </i> Cell Res, 2022","date":"2023-05-04T09:07:32.856Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7SHM"},{"db":"EMDB","id":"EMD-25130"}],"region_id":"DP03955r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5957"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"},{"text":"The N-terminal residues 1–66, a loop region (residues 357–365), and the C-terminal residues 708–745 were not resolved. Additionally, the hinge region (residues 437–462) between TMD and NBD was invisible in the electron density probably due to flexibility.","type":"Article"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T13:58:15.154Z"}},{"start":684,"end":745,"reference_id":"34754073","reference_source":"pmid","reference_html":"Structural basis of acyl-CoA transport across the peroxisomal membrane by human ABCD1. <i> Wang R, Qin Y, Li X. </i> Cell Res, 2022","date":"2023-05-04T09:06:57.478Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7SHM"},{"db":"EMDB","id":"EMD-25130"}],"region_id":"DP03955r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5957"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"},{"text":"The N-terminal residues 1–66, a loop region (residues 357–365), and the C-terminal residues 708–745 were not resolved. Additionally, the hinge region (residues 437–462) between TMD and NBD was invisible in the electron density probably due to flexibility.","type":"Article"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T13:58:13.978Z"}}],"regions_counter":4,"released":"2023_06","sequence":"MPVLSRPRPWRGNTLKRTAVLLALAAYGAHKVYPLVRQCLAPARGLQAPAGEPTQEASGVAAAKAGMNRVFLQRLLWLLRLLFPRVLCRETGLLALHSAALVSRTFLSVYVARLDGRLARCIVRKDPRAFGWQLLQWLLIALPATFVNSAIRYLEGQLALSFRSRLVAHAYRLYFSQQTYYRVSNMDGRLRNPDQSLTEDVVAFAASVAHLYSNLTKPLLDVAVTSYTLLRAARSRGAGTAWPSAIAGLVVFLTANVLRAFSPKFGELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQRSYQDLASQINLILLERLWYVMLEQFLMKYVWSASGLLMVAVPIITATGYSESDAEAVKKAALEKKEEELVSERTEAFTIARNLLTAAADAIERIMSSYKEVTELAGYTARVHEMFQVFEDVQRCHFKRPRELEDAQAGSGTIGRSGVRVEGPLKIRGQVVDVEQGIICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSVGSLRDQVIYPDSVEDMQRKGYSEQDLEAILDVVHLHHILQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKDAGIALLSITHRPSLWKYHTHLLQFDGEGGWKFEKLDSAARLSLTEEKQRLEQQLAGIPKMQRRLQELCQILGEAVAPAHVPAPSPQGPGGLQGAST","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.10335570469798658,"disorder_content":0.23087248322147652,"disprot_consensus":{"full":[{"start":2,"end":63,"type":"D"},{"start":353,"end":375,"type":"D"},{"start":437,"end":461,"type":"D"},{"start":684,"end":745,"type":"D"}],"Structural state":[{"start":2,"end":63,"type":"D"},{"start":353,"end":375,"type":"D"},{"start":437,"end":461,"type":"D"},{"start":684,"end":745,"type":"D"}]}},{"disprot_id":"DP03956","acc":"O14678","creator":"fkordevani","date":"2023-02-21T10:24:49.734Z","features":{"pfam":[{"id":"PF00005","name":"ABC transporter","start":405,"end":552},{"id":"PF06472","name":"ABC transporter transmembrane region 2","start":27,"end":294}],"gene3D":[]},"genes":[{"name":{"value":"ABCD4","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:68","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:68"}}]},"synonyms":[{"value":"PXMP1L"}]}],"length":606,"name":"Lysosomal cobalamin transporter ABCD4","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":2,"end":12,"reference_id":"31467407","reference_source":"pmid","reference_html":"Cryo-EM structure of human lysosomal cobalamin exporter ABCD4. <i> Xu D, Feng Z, Hou WT, Jiang YL, Wang L, Sun L, Zhou CZ, Chen Y. </i> Cell Res, 2019","date":"2023-05-04T09:13:47.117Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6JBJ"},{"db":"EMDB","id":"EMD-9791"}],"region_id":"DP03956r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5957"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"},{"text":"The final model composed of residues Arg13-Lys604, except for a 27-aa linker region (residues Lys357-Ala383), was refined against the EM density to an excellent geometry and statistics (Supplementary information, Fig. S2f and Table S1).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T13:59:26.059Z"}},{"start":357,"end":383,"reference_id":"31467407","reference_source":"pmid","reference_html":"Cryo-EM structure of human lysosomal cobalamin exporter ABCD4. <i> Xu D, Feng Z, Hou WT, Jiang YL, Wang L, Sun L, Zhou CZ, Chen Y. </i> Cell Res, 2019","date":"2023-05-04T09:14:18.541Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6JBJ"},{"db":"EMDB","id":"EMD-9791"}],"region_id":"DP03956r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5957"}],"statement":[{"text":"The final model composed of residues Arg13-Lys604, except for a 27-aa linker region (residues Lys357-Ala383), was refined against the EM density to an excellent geometry and statistics (Supplementary information, Fig. S2f and Table S1).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T13:59:25.469Z"}},{"start":357,"end":383,"reference_id":"31467407","reference_source":"pmid","reference_html":"Cryo-EM structure of human lysosomal cobalamin exporter ABCD4. <i> Xu D, Feng Z, Hou WT, Jiang YL, Wang L, Sun L, Zhou CZ, Chen Y. </i> Cell Res, 2019","date":"2023-05-04T09:16:18.597Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6JBJ"},{"db":"EMDB","id":"EMD-9791"}],"region_id":"DP03956r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5957"}],"statement":[{"text":"The final model composed of residues Arg13-Lys604, except for a 27-aa linker region (residues Lys357-Ala383), was refined against the EM density to an excellent geometry and statistics (Supplementary information, Fig. S2f and Table S1).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T13:59:27.146Z"}}],"regions_counter":3,"released":"2023_06","sequence":"MAVAGPAPGAGARPRLDLQFLQRFLQILKVLFPSWSSQNALMFLTLLCLTLLEQFVIYQVGLIPSQYYGVLGNKDLEGFKTLTFLAVMLIVLNSTLKSFDQFTCNLLYVSWRKDLTEHLHRLYFRGRAYYTLNVLRDDIDNPDQRISQDVERFCRQLSSMASKLIISPFTLVYYTYQCFQSTGWLGPVSIFGYFILGTVVNKTLMGPIVMKLVHQEKLEGDFRFKHMQIRVNAEPAAFYRAGHVEHMRTDRRLQRLLQTQRELMSKELWLYIGINTFDYLGSILSYVVIAIPIFSGVYGDLSPAELSTLVSKNAFVCIYLISCFTQLIDLSTTLSDVAGYTHRIGQLRETLLDMSLKSQDCEILGESEWGLDTPPGWPAAEPADTAFLLERVSISAPSSDKPLIKDLSLKISEGQSLLITGNTGTGKTSLLRVLGGLWTSTRGSVQMLTDFGPHGVLFLPQKPFFTDGTLREQVIYPLKEVYPDSGSADDERILRFLELAGLSNLVARTEGLDQQVDWNWYDVLSPGEMQRLSFARLFYLQPKYAVLDEATSALTEEVESELYRIGQQLGMTFISVGHRQSLEKFHSLVLKLCGGGRWELMRIKVE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.054455445544554455,"disorder_content":0.0627062706270627,"disprot_consensus":{"full":[{"start":2,"end":12,"type":"D"},{"start":357,"end":383,"type":"D"}],"Structural state":[{"start":2,"end":12,"type":"D"},{"start":357,"end":383,"type":"D"}],"Disorder function":[{"start":357,"end":383,"type":"F"}]}},{"disprot_id":"DP03957","acc":"P60709","creator":"fkordevani","date":"2023-02-21T10:41:50.807Z","features":{"pfam":[{"id":"PF00022","name":"Actin","start":3,"end":375}],"gene3D":[]},"genes":[{"name":{"value":"ACTB"}}],"length":375,"name":"Actin, cytoplasmic 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":33,"end":78,"reference_id":"32001526","reference_source":"pmid","reference_html":"Structure of nucleosome-bound human BAF complex. <i> He S, Wu Z, Tian Y, Yu Z, Yu J, Wang X, Li J, Liu B, Xu Y. </i> Science, 2020","date":"2023-05-04T14:13:18.141Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6LTJ"},{"db":"EMDB","id":"EMD-0974"}],"region_id":"DP03957r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered. Furthermore, electron microscopy demonstrates nucleosome-bound human BAF complex where multiple proteins and DNA molecules are interacting.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T14:17:24.320Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0,"disorder_content":0.12266666666666666,"disprot_consensus":{"full":[{"start":33,"end":78,"type":"D"}],"Structural state":[{"start":33,"end":78,"type":"D"}]}},{"disprot_id":"DP03958","acc":"O96019","creator":"fkordevani","date":"2023-02-21T15:38:59.187Z","features":{"pfam":[{"id":"PF00022","name":"Actin","start":8,"end":429}],"gene3D":[]},"genes":[{"name":{"value":"ACTL6A"},"synonyms":[{"value":"BAF53"},{"value":"BAF53A"},{"value":"INO80K"}]}],"length":429,"name":"Actin-like protein 6A","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":45,"end":67,"reference_id":"32001526","reference_source":"pmid","reference_html":"Structure of nucleosome-bound human BAF complex. <i> He S, Wu Z, Tian Y, Yu Z, Yu J, Wang X, Li J, Liu B, Xu Y. </i> Science, 2020","date":"2023-05-04T14:13:48.066Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6LTJ"},{"db":"EMDB","id":"EMD-0974"}],"region_id":"DP03958r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered. Furthermore, the structure demonstrates a nucleosome-bound human BAF complex where multiple proteins and DNA molecules are interacting.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T14:20:15.102Z"}},{"start":216,"end":245,"reference_id":"32001526","reference_source":"pmid","reference_html":"Structure of nucleosome-bound human BAF complex. <i> He S, Wu Z, Tian Y, Yu Z, Yu J, Wang X, Li J, Liu B, Xu Y. </i> Science, 2020","date":"2023-05-04T14:13:58.805Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6LTJ"},{"db":"EMDB","id":"EMD-0974"}],"region_id":"DP03958r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered. Furthermore, the structure demonstrates a nucleosome-bound human BAF complex where multiple proteins and DNA molecules are interacting.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T14:20:14.027Z"}},{"start":312,"end":322,"reference_id":"32001526","reference_source":"pmid","reference_html":"Structure of nucleosome-bound human BAF complex. <i> He S, Wu Z, Tian Y, Yu Z, Yu J, Wang X, Li J, Liu B, Xu Y. </i> Science, 2020","date":"2023-05-04T14:14:07.312Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6LTJ"},{"db":"EMDB","id":"EMD-0974"}],"region_id":"DP03958r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered. Furthermore, the structure demonstrates a nucleosome-bound human BAF complex where multiple proteins and DNA molecules are interacting.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T14:20:13.303Z"}},{"start":1,"end":11,"reference_id":"35477757","reference_source":"pmid","reference_html":"Structure of human chromatin-remodelling PBAF complex bound to a nucleosome. <i> Yuan J, Chen K, Zhang W, Chen Z. </i> Nature, 2022","date":"2023-05-04T10:07:13.857Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7VDV"}],"region_id":"DP03958r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:23624244"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered. Furthermore, the electron microscopy structure is associated with the 12-subunit human chromatin-remodelling polybromo-associated BRG1-associated factor (PBAF) complex bound to the nucleosome.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T14:09:50.777Z"}},{"start":45,"end":67,"reference_id":"35477757","reference_source":"pmid","reference_html":"Structure of human chromatin-remodelling PBAF complex bound to a nucleosome. <i> Yuan J, Chen K, Zhang W, Chen Z. </i> Nature, 2022","date":"2023-05-04T10:07:44.508Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7VDV"}],"region_id":"DP03958r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:23624244"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered. Furthermore, the electron microscopy structure is associated with the 12-subunit human chromatin-remodelling polybromo-associated BRG1-associated factor (PBAF) complex bound to the nucleosome.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T14:09:53.652Z"}},{"start":216,"end":245,"reference_id":"35477757","reference_source":"pmid","reference_html":"Structure of human chromatin-remodelling PBAF complex bound to a nucleosome. <i> Yuan J, Chen K, Zhang W, Chen Z. </i> Nature, 2022","date":"2023-05-04T10:07:57.729Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7VDV"}],"region_id":"DP03958r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:23624244"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered. Furthermore, the electron microscopy structure is associated with the 12-subunit human chromatin-remodelling polybromo-associated BRG1-associated factor (PBAF) complex bound to the nucleosome.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T14:09:54.673Z"}},{"start":312,"end":322,"reference_id":"35477757","reference_source":"pmid","reference_html":"Structure of human chromatin-remodelling PBAF complex bound to a nucleosome. <i> Yuan J, Chen K, Zhang W, Chen Z. </i> Nature, 2022","date":"2023-05-04T10:08:08.254Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7VDV"}],"region_id":"DP03958r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:23624244"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered. Furthermore, the electron microscopy structure is associated with the 12-subunit human chromatin-remodelling polybromo-associated BRG1-associated factor (PBAF) complex bound to the nucleosome.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T14:09:57.536Z"}},{"start":418,"end":429,"reference_id":"35477757","reference_source":"pmid","reference_html":"Structure of human chromatin-remodelling PBAF complex bound to a nucleosome. <i> Yuan J, Chen K, Zhang W, Chen Z. </i> Nature, 2022","date":"2023-05-04T10:08:18.021Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7VDV"}],"region_id":"DP03958r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:23624244"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered. Furthermore, the electron microscopy structure is associated with the 12-subunit human chromatin-remodelling polybromo-associated BRG1-associated factor (PBAF) complex bound to the nucleosome.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T14:09:59.690Z"}}],"regions_counter":8,"released":"2023_06","sequence":"MSGGVYGGDEVGALVFDIGSYTVRAGYAGEDCPKVDFPTAIGMVVERDDGSTLMEIDGDKGKQGGPTYYIDTNALRVPRENMEAISPLKNGMVEDWDSFQAILDHTYKMHVKSEASLHPVLMSEAPWNTRAKREKLTELMFEHYNIPAFFLCKTAVLTAFANGRSTGLILDSGATHTTAIPVHDGYVLQQGIVKSPLAGDFITMQCRELFQEMNIELVPPYMIASKEAVREGSPANWKRKEKLPQVTRSWHNYMCNCVIQDFQASVLQVSDSTYDEQVAAQMPTVHYEFPNGYNCDFGAERLKIPEGLFDPSNVKGLSGNTMLGVSHVVTTSVGMCDIDIRPGLYGSVIVAGGNTLIQSFTDRLNRELSQKTPPSMRLKLIANNTTVERRFSSWIGGSILASLGTFQQMWISKQEYEEGGKQCVERKCP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.055944055944055944,"disorder_content":0.20279720279720279,"disprot_consensus":{"full":[{"start":1,"end":11,"type":"D"},{"start":45,"end":67,"type":"D"},{"start":216,"end":245,"type":"D"},{"start":312,"end":322,"type":"D"},{"start":418,"end":429,"type":"D"}],"Structural state":[{"start":1,"end":11,"type":"D"},{"start":45,"end":67,"type":"D"},{"start":216,"end":245,"type":"D"},{"start":312,"end":322,"type":"D"},{"start":418,"end":429,"type":"D"}]}},{"disprot_id":"DP03959","acc":"Q9Y653","creator":"fkordevani","date":"2023-02-21T15:57:56.222Z","features":{"pfam":[{"id":"PF00002","name":"7 transmembrane receptor (Secretin family)","start":403,"end":654},{"id":"PF01825","name":"GAIN subdomain B","start":236,"end":392},{"id":"PF18587","name":"PTX/LNS-Like (PLL) domain","start":29,"end":162},{"id":"PF18619","name":"GPCR-Autoproteolysis-INducing (GAIN) subdomain A","start":173,"end":220}],"gene3D":[]},"genes":[{"name":{"value":"ADGRG1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4512","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4512"}}]},"synonyms":[{"value":"GPR56"},{"value":"TM7LN4"},{"value":"TM7XN1"}],"orfNames":[{"value":"UNQ540/PRO1083"}]}],"length":693,"name":"Adhesion G-protein coupled receptor G1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":549,"end":559,"reference_id":"35418682","reference_source":"pmid","reference_html":"The tethered peptide activation mechanism of adhesion GPCRs. <i> Barros-Álvarez X, Nwokonko RM, Vizurraga A, Matzov D, He F, Papasergi-Scott MM, Robertson MJ, Panova O, Yardeni EH, Seven AB, Kwarcinski FE, Su H, Peroto MC, Meyerowitz JG, Shalev-Benami M, Tall GG, Skiniotis G. </i> Nature, 2022","date":"2023-02-21T16:01:38.855Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7SF8"}],"region_id":"DP03959r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q14344 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62873"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P59768"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-03T16:36:51.034Z"}},{"start":664,"end":693,"reference_id":"35418682","reference_source":"pmid","reference_html":"The tethered peptide activation mechanism of adhesion GPCRs. <i> Barros-Álvarez X, Nwokonko RM, Vizurraga A, Matzov D, He F, Papasergi-Scott MM, Robertson MJ, Panova O, Yardeni EH, Seven AB, Kwarcinski FE, Su H, Peroto MC, Meyerowitz JG, Shalev-Benami M, Tall GG, Skiniotis G. </i> Nature, 2022","date":"2023-02-21T16:01:55.578Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7SF8"}],"region_id":"DP03959r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q14344 "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62873"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P59768"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-03T16:36:51.332Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MTPQSLLQTTLFLLSLLFLVQGAHGRGHREDFRFCSQRNQTHRSSLHYKPTPDLRISIENSEEALTVHAPFPAAHPASRSFPDPRGLYHFCLYWNRHAGRLHLLYGKRDFLLSDKASSLLCFQHQEESLAQGPPLLATSVTSWWSPQNISLPSAASFTFSFHSPPHTAAHNASVDMCELKRDLQLLSQFLKHPQKASRRPSAAPASQQLQSLESKLTSVRFMGDMVSFEEDRINATVWKLQPTAGLQDLHIHSRQEEEQSEIMEYSVLLPRTLFQRTKGRSGEAEKRLLLVDFSSQALFQDKNSSQVLGEKVLGIVVQNTKVANLTEPVVLTFQHQLQPKNVTLQCVFWVEDPTLSSPGHWSSAGCETVRRETQTSCFCNHLTYFAVLMVSSVEVDAVHKHYLSLLSYVGCVVSALACLVTIAAYLCSRVPLPCRRKPRDYTIKVHMNLLLAVFLLDTSFLLSEPVALTGSEAGCRASAIFLHFSLLTCLSWMGLEGYNLYRLVVEVFGTYVPGYLLKLSAMGWGFPIFLVTLVALVDVDNYGPIILAVHRTPEGVIYPSMCWIRDSLVSYITNLGLFSLVFLFNMAMLATMVVQILRLRPHTQKWSHVLTLLGLSLVLGLPWALIFFSFASGTFQLVVLYLFSIITSFQGFLIFIWYWSMRLQARGGPSPLKSNSDSARLPISSGSTSSSRI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.10245310245310245,"disorder_content":0.05916305916305916,"disprot_consensus":{"full":[{"start":549,"end":559,"type":"D"},{"start":664,"end":693,"type":"D"}],"Structural state":[{"start":549,"end":559,"type":"D"},{"start":664,"end":693,"type":"D"}]}},{"disprot_id":"DP03960","acc":"P55263","creator":"fkordevani","date":"2023-02-21T16:06:32.788Z","features":{"pfam":[{"id":"PF00294","name":"pfkB family carbohydrate kinase","start":45,"end":356}],"gene3D":[]},"genes":[{"name":{"value":"ADK","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:257","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:257"}}]}}],"length":362,"name":"Adenosine kinase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":348,"end":362,"reference_id":"17154503","reference_source":"pmid","reference_html":"Crystal structures of human adenosine kinase inhibitor complexes reveal two distinct binding modes. <i> Muchmore SW, Smith RA, Stewart AO, Cowart MD, Gomtsyan A, Matulenko MA, Yu H, Severin JM, Bhagwat SS, Lee CH, Kowaluk EA, Jarvis MF, Jakob CL. </i> J Med Chem, 2006","date":"2023-05-04T10:12:10.427Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2I6B"}],"region_id":"DP03960r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:11987868"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region when bound to an inhibitor, indicating it is disordered.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala20Ser","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu21Val","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T14:10:49.594Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MAAAEEEPKPKKLKVEAPQALRENILFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHKAATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEKHLDLEKNWMLVEKARVCYIAGFFLTVSPESVLKVAHHASENNRIFTLNLSAPFISQFYKESLMKVMPYVDILFGNETEAATFAREQGFETKDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCTFPEKPDFH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.04419889502762431,"disorder_content":0.04143646408839779,"disprot_consensus":{"full":[{"start":348,"end":362,"type":"D"}],"Structural state":[{"start":348,"end":362,"type":"D"}]}},{"disprot_id":"DP03961","acc":"Q9NX46","creator":"fkordevani","date":"2023-02-21T16:13:49.554Z","features":{"pfam":[{"id":"PF03747","name":"ADP-ribosylglycohydrolase","start":19,"end":361}],"gene3D":[]},"genes":[{"name":{"value":"ADPRS","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:21304","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:21304"}}]},"synonyms":[{"value":"ADPRHL2"},{"value":"ARH3","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16278211","url":"http://www.ncbi.nlm.nih.gov/pubmed/16278211","alternativeUrl":"https://europepmc.org/abstract/MED/16278211"}}]}]}],"length":363,"name":"ADP-ribosylhydrolase ARH3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":13,"reference_id":"33894202","reference_source":"pmid","reference_html":"Structural and biochemical analysis of human ADP-ribosyl-acceptor hydrolase 3 reveals the basis of metal selectivity and different roles for the two magnesium ions. <i> Pourfarjam Y, Ma Z, Kurinov I, Moss J, Kim IK. </i> J Biol Chem, 2021","date":"2023-05-04T10:14:11.207Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7L9F"},{"db":"PDB","id":"7L9H"},{"db":"PDB","id":"7L9I"}],"region_id":"DP03961r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:447048"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp77Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp314Ala","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T14:11:59.847Z"}},{"start":60,"end":69,"reference_id":"33894202","reference_source":"pmid","reference_html":"Structural and biochemical analysis of human ADP-ribosyl-acceptor hydrolase 3 reveals the basis of metal selectivity and different roles for the two magnesium ions. <i> Pourfarjam Y, Ma Z, Kurinov I, Moss J, Kim IK. </i> J Biol Chem, 2021","date":"2023-05-04T10:14:49.265Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7L9F"},{"db":"PDB","id":"7L9H"}],"region_id":"DP03961r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:447048"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp77Ala","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T14:12:02.435Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MAAAAMAAAAGGGAGAARSLSRFRGCLAGALLGDCVGSFYEAHDTVDLTSVLRHVQSLEPDPGTPGSERTEALYYTDDTAMARALVQSLLAKEAFDEVDMAHRFAQEYKKDPDRGYGAGVVTVFKKLLNPKCRDVFEPARAQFNGKGSYGNGGAMRVAGISLAYSSVQDVQKFARLSAQLTHASSLGYNGAILQALAVHLALQGESSSEHFLKQLLGHMEDLEGDAQSVLDARELGMEERPYSSRLKKIGELLDQASVTREEVVSELGNGIAAFESVPTAIYCFLRCMEPDPEIPSAFNSLQRTLIYSISLGGDTDTIATMAGAIAGAYYGMDQVPESWQQSCEGYEETDILAQSLHRVFQKS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.03856749311294766,"disorder_content":0.06336088154269973,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"D"},{"start":60,"end":69,"type":"D"}],"Structural state":[{"start":1,"end":13,"type":"D"},{"start":60,"end":69,"type":"D"}]}},{"disprot_id":"DP03962","acc":"P30566","creator":"fkordevani","date":"2023-02-21T16:40:06.958Z","features":{"pfam":[{"id":"PF00206","name":"Lyase","start":98,"end":308},{"id":"PF10397","name":"Adenylosuccinate lyase C-terminus","start":378,"end":460}],"gene3D":[]},"genes":[{"name":{"value":"ADSL"},"synonyms":[{"value":"AMPS"}]}],"length":484,"name":"Adenylosuccinate lyase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":283,"end":294,"reference_id":"22812634","reference_source":"pmid","reference_html":"Structural and biochemical characterization of human adenylosuccinate lyase (ADSL) and the R303C ADSL deficiency-associated mutation. <i> Ray SP, Deaton MK, Capodagli GC, Calkins LA, Sawle L, Ghosh K, Patterson D, Pegan SD. </i> Biochemistry, 2012","date":"2023-05-04T10:17:02.458Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4FFX"}],"region_id":"DP03962r001","statement":[{"text":"Similar to the ADSL-R303C and ADSL-SAMP, electron density for residues 283–293 (β3-α10 loop) was not observed.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gln63Arg","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T14:14:20.467Z"}},{"start":475,"end":484,"reference_id":"22812634","reference_source":"pmid","reference_html":"Structural and biochemical characterization of human adenylosuccinate lyase (ADSL) and the R303C ADSL deficiency-associated mutation. <i> Ray SP, Deaton MK, Capodagli GC, Calkins LA, Sawle L, Ghosh K, Patterson D, Pegan SD. </i> Biochemistry, 2012","date":"2023-05-04T10:17:18.840Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4FFX"}],"region_id":"DP03962r002","statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"},{"text":"Electron density was observed for the majority of all 5–476 ADSL residues in all monomers, with residues 5–112 forming domain 1, residues 113–364 as domain 2, and 364–476 as domain 3.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gln63Arg","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T14:14:19.301Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MAAGGDHGSPDSYRSPLASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLPITDEQIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLASLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKQEGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGRASQQVQRFLEEEVYPLLKPYESVMKVKAELCL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.010330578512396695,"disorder_content":0.045454545454545456,"disprot_consensus":{"full":[{"start":283,"end":294,"type":"D"},{"start":475,"end":484,"type":"D"}],"Structural state":[{"start":283,"end":294,"type":"D"},{"start":475,"end":484,"type":"D"}]}},{"disprot_id":"DP03963","acc":"O95831","creator":"fkordevani","date":"2023-02-22T10:19:46.378Z","features":{"pfam":[{"id":"PF07992","name":"Pyridine nucleotide-disulphide oxidoreductase","start":136,"end":461},{"id":"PF14721","name":"Apoptosis-inducing factor, mitochondrion-associated, C-term","start":465,"end":594}],"gene3D":[]},"genes":[{"name":{"value":"AIFM1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:8768","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8768"}}]},"synonyms":[{"value":"AIF"},{"value":"PDCD8"}]}],"length":613,"name":"Apoptosis-inducing factor 1, mitochondrial","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":78,"end":125,"reference_id":"27818101","reference_source":"pmid","reference_html":"Defining NADH-Driven Allostery Regulating Apoptosis-Inducing Factor. <i> Brosey CA, Ho C, Long WZ, Singh S, Burnett K, Hura GL, Nix JC, Bowman GR, Ellenberger T, Tainer JA. </i> Structure, 2016","date":"2023-04-11T14:47:25.343Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5KVI"},{"db":"PDB","id":"5KVH"}],"region_id":"DP03963r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:643975"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:23831"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"}],"statement":[{"text":"To test whether the crystallographic monomer and dimer accurately reveal AIF architecture in solution or reflect crystal packing, we collected SAXS data on soluble constructs with increasing NADH concentrations: AIF78 (residues 78–613, the intact mitochondrial protein save the 24-residue transmembrane insert, residues 54–77), and AIF121 (residues 121–613, excluding the disordered N-terminal linker to the membrane) (Figure 1A, S2).","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu413Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To complement the SAXS analysis, we biochemically validated the crystallographic dimerization surface. Targeted mutation of residues acting in AIF’s dimer interface (E413A/R422A/R430A) disrupts dimerization (Ferreira et al., 2014)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg422Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To complement the SAXS analysis, we biochemically validated the crystallographic dimerization surface. Targeted mutation of residues acting in AIF’s dimer interface (E413A/R422A/R430A) disrupts dimerization (Ferreira et al., 2014)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg430Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To complement the SAXS analysis, we biochemically validated the crystallographic dimerization surface. Targeted mutation of residues acting in AIF’s dimer interface (E413A/R422A/R430A) disrupts dimerization (Ferreira et al., 2014)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp196Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"AIF78 W196A forms the dimeric interface seen in the wild-type AIF-CTC crystal structure (PDB: 4BUR) and is missing density for the displaced C-loop insert (Figure 3A). However, several key side chain rearrangements seen in the active site of wild-type AIF-CTC are absent in the W196A mutant."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T15:06:56.549Z"}},{"start":511,"end":559,"reference_id":"27818101","reference_source":"pmid","reference_html":"Defining NADH-Driven Allostery Regulating Apoptosis-Inducing Factor. <i> Brosey CA, Ho C, Long WZ, Singh S, Burnett K, Hura GL, Nix JC, Bowman GR, Ellenberger T, Tainer JA. </i> Structure, 2016","date":"2023-04-13T08:59:36.349Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5KVH"}],"region_id":"DP03963r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:643975"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"}],"statement":[{"text":"AIF78 W196A forms the dimeric interface seen in the wild-type AIF-CTC crystal structure (PDB: 4BUR) and is missing density for the displaced C-loop insert (Figure 3A).","type":"Results"},{"text":"Point mutations along the C-loop backbone promoted partial C-loop exposure without ligand and more efficient protein dimerization at lower NADH levels relative to wild-type protein (Figures 2C–D, top).","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp196Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"AIF78 W196A forms the dimeric interface seen in the wild-type AIF-CTC crystal structure (PDB: 4BUR) and is missing density for the displaced C-loop insert (Figure 3A). However, several key side chain rearrangements seen in the active site of wild-type AIF-CTC are absent in the W196A mutant."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-19T14:30:18.208Z"}},{"start":545,"end":556,"reference_id":"27818101","reference_source":"pmid","reference_html":"Defining NADH-Driven Allostery Regulating Apoptosis-Inducing Factor. <i> Brosey CA, Ho C, Long WZ, Singh S, Burnett K, Hura GL, Nix JC, Bowman GR, Ellenberger T, Tainer JA. </i> Structure, 2016","date":"2023-04-13T09:02:45.170Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5KVI"}],"region_id":"DP03963r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:643975"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:23831"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu413Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To complement the SAXS analysis, we biochemically validated the crystallographic dimerization surface. Targeted mutation of residues acting in AIF’s dimer interface (E413A/R422A/R430A) disrupts dimerization (Ferreira et al., 2014)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg422Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To complement the SAXS analysis, we biochemically validated the crystallographic dimerization surface. Targeted mutation of residues acting in AIF’s dimer interface (E413A/R422A/R430A) disrupts dimerization (Ferreira et al., 2014)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg430Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To complement the SAXS analysis, we biochemically validated the crystallographic dimerization surface. Targeted mutation of residues acting in AIF’s dimer interface (E413A/R422A/R430A) disrupts dimerization (Ferreira et al., 2014)."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-19T14:30:47.059Z"}},{"start":78,"end":121,"reference_id":"27818101","reference_source":"pmid","reference_html":"Defining NADH-Driven Allostery Regulating Apoptosis-Inducing Factor. <i> Brosey CA, Ho C, Long WZ, Singh S, Burnett K, Hura GL, Nix JC, Bowman GR, Ellenberger T, Tainer JA. </i> Structure, 2016","date":"2023-04-13T09:03:26.232Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP03963r004","statement":[{"text":"Corresponding values derived from AIF78 (Rg 28.9 Å and Vp 101,858 Å3) are elevated relative to the crystal structure, consistent with added scattering volume from the 43-residue N-terminus.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-19T14:30:59.245Z"}},{"start":546,"end":558,"reference_id":"24914854","reference_source":"pmid","reference_html":"Structural insights into the coenzyme mediated monomer-dimer transition of the pro-apoptotic apoptosis inducing factor. <i> Ferreira P, Villanueva R, Martínez-Júlvez M, Herguedas B, Marcuello C, Fernandez-Silva P, Cabon L, Hermoso JA, Lostao A, Susin SA, Medina M. </i> Biochemistry, 2014","date":"2023-04-11T15:37:51.386Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4BV6"}],"region_id":"DP03963r005","statement":[{"text":"Residues following these two α-helices are organized in a loop (533–545) and, high flexibility beyond position 546 makes the rest of the region not visible (546–558).","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:643975"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T15:42:27.397Z"}},{"start":517,"end":550,"reference_id":"24914854","reference_source":"pmid","reference_html":"Structural insights into the coenzyme mediated monomer-dimer transition of the pro-apoptotic apoptosis inducing factor. <i> Ferreira P, Villanueva R, Martínez-Júlvez M, Herguedas B, Marcuello C, Fernandez-Silva P, Cabon L, Hermoso JA, Lostao A, Susin SA, Medina M. </i> Biochemistry, 2014","date":"2023-04-13T09:24:01.563Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4BUR"}],"region_id":"DP03963r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5892"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:643975"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"}],"statement":[{"text":"The four chains of the asymmetric unit present a similar overall fold: r.m.s.d. of 0.28 Å (412 Cα, chain B), 0.24 Å (373 Cα, C), and 0.30 Å (384 Cα, D) regarding chain A. The final atomic model contains residues 128–516 and 551–611 in chain A, 125–516 and 553–610 in B, 127–517 and 558–612 in C, and 128–509 and 559–611 in D, and electron density was clear to position one FAD and two NAD(H) molecules per hAIFΔ1–102 protomer with 100% occupancy (Figure 2).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-19T14:50:56.851Z"}},{"start":103,"end":127,"reference_id":"24914854","reference_source":"pmid","reference_html":"Structural insights into the coenzyme mediated monomer-dimer transition of the pro-apoptotic apoptosis inducing factor. <i> Ferreira P, Villanueva R, Martínez-Júlvez M, Herguedas B, Marcuello C, Fernandez-Silva P, Cabon L, Hermoso JA, Lostao A, Susin SA, Medina M. </i> Biochemistry, 2014","date":"2023-04-27T13:37:09.760Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4BUR"}],"region_id":"DP03963r007","statement":[{"text":"The four chains of the asymmetric unit present a similar overall fold: r.m.s.d. of 0.28 Å (412 Cα, chain B), 0.24 Å (373 Cα, C), and 0.30 Å (384 Cα, D) regarding chain A. The final atomic model contains residues 128–516 and 551–611 in chain A, 125–516 and 553–610 in B, 127–517 and 558–612 in C, and 128–509 and 559–611 in D, and electron density was clear to position one FAD and two NAD(H) molecules per hAIFΔ1–102 protomer with 100% occupancy (Figure 2).","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5892"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:643975"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-27T14:31:55.013Z"}},{"start":517,"end":545,"reference_id":"24914854","reference_source":"pmid","reference_html":"Structural insights into the coenzyme mediated monomer-dimer transition of the pro-apoptotic apoptosis inducing factor. <i> Ferreira P, Villanueva R, Martínez-Júlvez M, Herguedas B, Marcuello C, Fernandez-Silva P, Cabon L, Hermoso JA, Lostao A, Susin SA, Medina M. </i> Biochemistry, 2014","date":"2023-04-27T13:47:26.812Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4BV6"},{"db":"PDB","id":"4BUR"}],"region_id":"DP03963r008","statement":[{"text":"Upon coenzyme binding and/or reduction R201 results are displaced by forming a H-bond with the main chains of Y204 and S202, thus, contributing to the unfolding of the short helices, allowing NAD(H)B stabilization and releasing the orientation of the 190–202 β-hairpin to the solvent. Overall, these results uncover that at a molecular level, the oxido-reduction and/or coenzyme-bound status of hAIF modulates the conformation of its C-terminal proapoptotic domain.","type":"Results"}],"states_connection":[{"source":"DP03963r009","target":"DP03963r006"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5892"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:643975"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-27T14:38:03.431Z"}},{"start":517,"end":545,"reference_id":"24914854","reference_source":"pmid","reference_html":"Structural insights into the coenzyme mediated monomer-dimer transition of the pro-apoptotic apoptosis inducing factor. <i> Ferreira P, Villanueva R, Martínez-Júlvez M, Herguedas B, Marcuello C, Fernandez-Silva P, Cabon L, Hermoso JA, Lostao A, Susin SA, Medina M. </i> Biochemistry, 2014","date":"2023-04-27T13:46:10.984Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4BV6"}],"region_id":"DP03963r009","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:643975"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"}],"statement":[{"text":"In hAIFox the 517–533 region is stabilized by direct interaction with the 190–202 β-hairpin, particularly by a H-bond and a salt-bridge between the side-chain of R201 and those of T526 and E531, respectively.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-27T14:38:05.399Z"}}],"regions_counter":9,"released":"2023_06","sequence":"MFRCGGLAAGALKQKLVPLVRTVCVRSPRQRNRLPGNLFQRWHVPLELQMTRQMASSGASGGKIDNSVLVLIVGLSTVGAGAYAYKTMKEDEKRYNERISGLGLTPEQKQKKAALSASEGEEVPQDKAPSHVPFLLIGGGTAAFAAARSIRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPNVTKTLRFKQWNGKERSIYFQPPSFYVSAQDLPHIENGGVAVLTGKKVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPRSLSAIDRAGAEVKSRTTLFRKIGDFRSLEKISREVKSITIIGGGFLGSELACALGRKARALGTEVIQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLIKLKDGRKVETDHIVAAVGLEPNVELAKTGGLEIDSDFGGFRVNAELQARSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRLAGENMTGAAKPYWHQSMFWSDLGPDVGYEAIGLVDSSLPTVGVFAKATAQDNPKSATEQSGTGIRSESETESEASEITIPPSTPAVPQAPVQGEDYGKGVIFYLRDKVVVGIVLWNIFNRMPIARKIIKDGEQHEDLNEVAKLFNIHED","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.14192495921696574,"disorder_content":0.16150081566068517,"disprot_consensus":{"full":[{"start":78,"end":127,"type":"D"},{"start":511,"end":516,"type":"D"},{"start":517,"end":545,"type":"T"},{"start":546,"end":559,"type":"D"}],"Structural state":[{"start":78,"end":127,"type":"D"},{"start":511,"end":559,"type":"D"}],"Structural transition":[{"start":517,"end":545,"type":"T"}]}},{"disprot_id":"DP03964","acc":"P47895","creator":"fkordevani","date":"2023-02-22T10:46:22.270Z","features":{"pfam":[{"id":"PF00171","name":"Aldehyde dehydrogenase family","start":40,"end":503}],"gene3D":[]},"genes":[{"name":{"value":"ALDH1A3"},"synonyms":[{"value":"ALDH6","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"7698756","url":"http://www.ncbi.nlm.nih.gov/pubmed/7698756","alternativeUrl":"https://europepmc.org/abstract/MED/7698756"}}]}]}],"length":512,"name":"Aldehyde dehydrogenase family 1 member A3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":26,"reference_id":"32435412","reference_source":"pmid","reference_html":"Progress in the Field of Aldehyde Dehydrogenase Inhibitors: Novel Imidazo[1,2-<i>a</i>]pyridines against the 1A Family. <i> Quattrini L, Gelardi ELM, Petrarolo G, Colombo G, Ferraris DM, Picarazzi F, Rizzi M, Garavaglia S, La Motta C. </i> ACS Med Chem Lett, 2020","date":"2023-02-22T10:50:09.737Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6TRY"}],"region_id":"DP03964r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5892"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:155294454"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-03T16:29:55.491Z"}},{"start":1,"end":19,"reference_id":"35418200","reference_source":"pmid","reference_html":"Structural and biochemical evidence that ATP inhibits the cancer biomarker human aldehyde dehydrogenase 1A3. <i> Castellví A, Pequerul R, Barracco V, Juanhuix J, Parés X, Farrés J. </i> Commun Biol, 2022","date":"2023-02-22T10:56:11.884Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7QK8"},{"db":"PDB","id":"7QK7"}],"region_id":"DP03964r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5892"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:8117"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:449607"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-03T16:22:19.531Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MATANGAVENGQPDRKPPALPRPIRNLEVKFTKIFINNEWHESKSGKKFATCNPSTREQICEVEEGDKPDVDKAVEAAQVAFQRGSPWRRLDALSRGRLLHQLADLVERDRATLAALETMDTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPWNFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTVGAAISSHPQINKIAFTGSTEVGKLVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVECAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQKQFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPILKFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGFKMSGNGRELGEYALAEYTEVKTVTIKLGDKNP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Stress response proteins"],"alphafold_very_low_content":0.03125,"disorder_content":0.05078125,"disprot_consensus":{"full":[{"start":1,"end":26,"type":"D"}],"Structural state":[{"start":1,"end":26,"type":"D"}]}},{"disprot_id":"DP03965","acc":"P30038","creator":"fkordevani","date":"2023-02-22T10:58:35.938Z","features":{"pfam":[{"id":"PF00171","name":"Aldehyde dehydrogenase family","start":81,"end":545}],"gene3D":[]},"genes":[{"name":{"value":"ALDH4A1"},"synonyms":[{"value":"ALDH4"},{"value":"P5CDH"}]}],"length":563,"name":"Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":512,"end":537,"reference_id":"22516612","reference_source":"pmid","reference_html":"The three-dimensional structural basis of type II hyperprolinemia. <i> Srivastava D, Singh RK, Moxley MA, Henzl MT, Becker DF, Tanner JJ. </i> J Mol Biol, 2012","date":"2023-04-11T15:51:26.308Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3V9I"}],"region_id":"DP03965r001","statement":[{"text":"The active site of S352L, however, is highly perturbed. In particular, the catalytic loop adopts a non-native conformation (Fig. 7a).","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser352Leu","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:05:32.858Z"}},{"start":552,"end":563,"reference_id":"24502590","reference_source":"pmid","reference_html":"Structural studies of yeast Δ(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): active site flexibility and oligomeric state. <i> Pemberton TA, Srivastava D, Sanyal N, Henzl MT, Becker DF, Tanner JJ. </i> Biochemistry, 2014","date":"2023-04-13T09:07:38.652Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4OE5"}],"region_id":"DP03965r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:62551"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"}],"statement":[{"text":"As in the Put2p structure, electron density for the aldehyde anchor peptide of monoclinic HsP5CDH (residues 514–535) is very weak (Figure3C). Electron density for these residues is essentially absent in chains A and D, and the entire loop was omitted. In the other two chains in the asymmetric unit, the binding of Mg2+ from the crystallization buffer stabilizes residues 522–535 in a non-native conformation, but the other residues of the loop remain disordered. Thus, the disordered active site is not limited to Put2p.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-19T14:57:24.899Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MLLPAPALRRALLSRPWTGAGLRWKHTSSLKVANEPVLAFTQGSPERDALQKALKDLKGRMEAIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSLWPQIKGRLLEEHSRIKVGDPAEDFGTFFSAVIDAKSFARIKKWLEHARSSPSLTILAGGKCDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDKYKETLQLVDSTTSYGLTGAVFSQDKDVVQEATKVLRNAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILRWTSPQVIKETHKPLGDWSYAYMQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.028419182948490232,"disorder_content":0.0674955595026643,"disprot_consensus":{"full":[{"start":512,"end":537,"type":"D"},{"start":552,"end":563,"type":"D"}],"Structural state":[{"start":512,"end":537,"type":"D"},{"start":552,"end":563,"type":"D"}]}},{"disprot_id":"DP03966","acc":"P49419","creator":"fkordevani","date":"2023-02-22T11:11:55.093Z","features":{"pfam":[{"id":"PF00171","name":"Aldehyde dehydrogenase family","start":64,"end":520}],"gene3D":[]},"genes":[{"name":{"value":"ALDH7A1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:877","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:877"}}]},"synonyms":[{"value":"ATQ1"}]}],"length":539,"name":"Alpha-aminoadipic semialdehyde dehydrogenase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":487,"end":509,"reference_id":"26260980","reference_source":"pmid","reference_html":"Structural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1. <i> Luo M, Tanner JJ. </i> Biochemistry, 2015","date":"2023-04-12T08:13:46.706Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4ZVY"},{"db":"PDB","id":"4ZVX"}],"region_id":"DP03966r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5892"}],"statement":[{"text":"The tetragonal structures, which were determined in the absence of bound AA, suggest a more severe conformational variation of the active site. In these structures, electron density for the 12 C-terminal residues (500–511) is absent in both chains in the asymmetric unit. Similarly, electron density for the long interdomain linker (residues 459–481) is missing.","type":"Results"},{"text":"The authors are referring to the 528-539 and 487-509 regions of the UniProt sequence.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:09:03.442Z"}},{"start":528,"end":539,"reference_id":"26260980","reference_source":"pmid","reference_html":"Structural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1. <i> Luo M, Tanner JJ. </i> Biochemistry, 2015","date":"2023-04-12T08:19:26.689Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4ZVY"},{"db":"PDB","id":"4ZVX"}],"region_id":"DP03966r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5892"}],"statement":[{"text":"The tetragonal structures, which were determined in the absence of bound AA, suggest a more severe conformational variation of the active site. In these structures, electron density for the 12 C-terminal residues (500–511) is absent in both chains in the asymmetric unit. Similarly, electron density for the long interdomain linker (residues 459–481) is missing.","type":"Results"},{"text":"The authors are referring to the 528-539 and 487-509 regions of the UniProt sequence.","type":"Curator statement"},{"text":"Thus, the P4212 lattice seems to be compatible with the open (and closed) conformation of the C-terminus. The absence of electron density implies that the C-terminus adopts multiple conformations in the P4212 crystal. Apparently, the solvent channel is large enough to accommodate multiple, diverse conformations of the C-terminus.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:09:37.935Z"}},{"start":487,"end":509,"reference_id":"26260980","reference_source":"pmid","reference_html":"Structural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1. <i> Luo M, Tanner JJ. </i> Biochemistry, 2015","date":"2023-04-13T09:09:49.929Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4ZVX"},{"db":"PDB","id":"4ZVY"}],"region_id":"DP03966r003","statement":[{"text":"The tetragonal structures, which were determined in the absence of bound AA, suggest a more severe conformational variation of the active site. In these structures, electron density for the 12 C-terminal residues (500–511) is absent in both chains in the asymmetric unit. Similarly, electron density for the long interdomain linker (residues 459–481) is missing.","type":"Results"},{"text":"The authors are referring to the 528-539 and 487-509 regions of the UniProt sequence.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5892"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-19T14:58:25.099Z"}}],"regions_counter":3,"released":"2023_06","sequence":"MWRLPRALCVHAAKTSKLSGPWSRPAAFMSTLLINQPQYAWLKELGLREENEGVYNGSWGGRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVGNPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHDASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGIVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINYSKDLPLAQGIKFQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Stress response proteins"],"alphafold_very_low_content":0.05380333951762523,"disorder_content":0.06493506493506493,"disprot_consensus":{"full":[{"start":487,"end":509,"type":"D"},{"start":528,"end":539,"type":"D"}],"Structural state":[{"start":487,"end":509,"type":"D"},{"start":528,"end":539,"type":"D"}],"Disorder function":[{"start":487,"end":509,"type":"F"}]}},{"disprot_id":"DP03967","acc":"Q96BT7","creator":"fkordevani","date":"2023-02-22T14:30:45.036Z","features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":50,"end":105},{"id":"PF08241","name":"Methyltransferase domain","start":412,"end":501},{"id":"PF09004","name":"Alkylated DNA repair protein alkB homolog 8, N-terminal","start":1,"end":37},{"id":"PF13532","name":"2OG-Fe(II) oxygenase superfamily","start":150,"end":334}],"gene3D":[]},"genes":[{"name":{"value":"ALKBH8"},"synonyms":[{"value":"ABH8"}]}],"length":664,"name":"Alkylated DNA repair protein alkB homolog 8","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":159,"end":173,"reference_id":"22065580","reference_source":"pmid","reference_html":"Crystal structure and RNA binding properties of the RNA recognition motif (RRM) and AlkB domains in human AlkB homolog 8 (ABH8), an enzyme catalyzing tRNA hypermodification. <i> Pastore C, Topalidou I, Forouhar F, Yan AC, Levy M, Hunt JF. </i> J Biol Chem, 2012","date":"2023-04-12T08:31:04.399Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3THP"},{"db":"PDB","id":"3THT"}],"region_id":"DP03967r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:27854"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:51"}],"statement":[{"text":"Residues 156–174 and 181–192 in the AlkB domain (dotted green lines), which are topologically equivalent to the segments forming the nucleotide-binding lid in E. coli AlkB, are disordered in ABH8.","type":"Figure"}],"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"Although lead crystals were obtained for an RRM/AlkB construct containing the intact N terminus (i.e. 1–354), excision of the first 24 N-terminal residues and retention of the C-terminal hexahistidine tag yielded much stronger diffraction. "}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":76,"end":76,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":138,"end":138,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":151,"end":151,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":224,"end":224,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":260,"end":260,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":273,"end":273,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":282,"end":282,"position":"Specific residue"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:18:26.842Z"}},{"start":182,"end":191,"reference_id":"22065580","reference_source":"pmid","reference_html":"Crystal structure and RNA binding properties of the RNA recognition motif (RRM) and AlkB domains in human AlkB homolog 8 (ABH8), an enzyme catalyzing tRNA hypermodification. <i> Pastore C, Topalidou I, Forouhar F, Yan AC, Levy M, Hunt JF. </i> J Biol Chem, 2012","date":"2023-04-13T09:15:34.243Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3THP"}],"region_id":"DP03967r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:27854"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:51"}],"statement":[{"text":"Residues 156–174 and 181–192 in the AlkB domain (dotted green lines), which are topologically equivalent to the segments forming the nucleotide-binding lid in E. coli AlkB, are disordered in ABH8.","type":"Figure"}],"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"Although lead crystals were obtained for an RRM/AlkB construct containing the intact N terminus (i.e. 1–354), excision of the first 24 N-terminal residues and retention of the C-terminal hexahistidine tag yielded much stronger diffraction."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":76,"end":76,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":138,"end":138,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":151,"end":151,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":224,"end":224,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":260,"end":260,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":273,"end":273,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":282,"end":282,"position":"Specific residue"}],"sequence_construct":"AKHTLLRHEGIETVSYATQSLVVANGGLGNGVSRNQLLPVLEKCGLVDALLMPPNKPYSFARYRTTEESKRAYVTLNGKEVVDDLGQKITLYLNFVEKVQWKELRPQALPPGLMVVEEIISSEEEKMLLESVDWTEDTDNQNSQKSLKHRRVKHFGYEFHYENNNVDKDKPLSGGLPDICESFLEKWLRKGYIKHKPDQMTINQYEPGQGIPAHIDTHSAFEDEIVSLSLGSEIVMDFKHPDGIAVPVMLPRRSLLVMTGESRYLWTHGITCRKFDTVQASESLKSGIITSDVGDLTLSKRGLRTSFTFRKVRQTPCNCSYPLVCDSQRKENLYFQGLEHHHHHH","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-19T14:58:45.844Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MDSNHQSNYKLSKTEKKFLRKQIKAKHTLLRHEGIETVSYATQSLVVANGGLGNGVSRNQLLPVLEKCGLVDALLMPPNKPYSFARYRTTEESKRAYVTLNGKEVVDDLGQKITLYLNFVEKVQWKELRPQALPPGLMVVEEIISSEEEKMLLESVDWTEDTDNQNSQKSLKHRRVKHFGYEFHYENNNVDKDKPLSGGLPDICESFLEKWLRKGYIKHKPDQMTINQYEPGQGIPAHIDTHSAFEDEIVSLSLGSEIVMDFKHPDGIAVPVMLPRRSLLVMTGESRYLWTHGITCRKFDTVQASESLKSGIITSDVGDLTLSKRGLRTSFTFRKVRQTPCNCSYPLVCDSQRKETPPSFPESDKEASRLEQEYVHQVYEEIAGHFSSTRHTPWPHIVEFLKALPSGSIVADIGCGNGKYLGINKELYMIGCDRSQNLVDICRERQFQAFVCDALAVPVRSGSCDACISIAVIHHFATAERRVAALQEIVRLLRPGGKALIYVWAMEQEYNKQKSKYLRGNRNSQGKKEEMNSDTSVQRSLVEQMRDMGSRDSASSVPRINDSQEGGCNSRQVSNSKLPVHVNRTSFYSQDVLVPWHLKGNPDKGKPVEPFGPIGSQDPSPVFHRYYHVFREGELEGACRTVSDVRILQSYYDQGNWCVILQKA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.13855421686746988,"disorder_content":0.03765060240963856,"disprot_consensus":{"full":[{"start":159,"end":173,"type":"D"},{"start":182,"end":191,"type":"D"}],"Structural state":[{"start":159,"end":173,"type":"D"},{"start":182,"end":191,"type":"D"}]}},{"disprot_id":"DP03968","acc":"Q01433","creator":"fkordevani","date":"2023-02-22T14:42:54.883Z","features":{"pfam":[{"id":"PF19326","name":"AMP deaminase","start":163,"end":806}],"gene3D":[]},"genes":[{"name":{"value":"AMPD2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:469","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:469"}}]}}],"length":825,"name":"AMP deaminase 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":229,"end":248,"reference_id":"36563792","reference_source":"pmid","reference_html":"The discovery of 3,3-dimethyl-1,2,3,4-tetrahydroquinoxaline-1-carboxamides as AMPD2 inhibitors with a novel mechanism of action. <i> Kitao Y, Saito T, Watanabe S, Ohe Y, Takahashi K, Akaki T, Adachi T, Doi S, Yamanaka K, Murai Y, Oba M, Suzuki T. </i> Bioorg Med Chem Lett, 2023","date":"2023-02-22T14:47:08.031Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"8HUB"}],"region_id":"DP03968r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:166451149"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-04T13:54:00.986Z"}},{"start":390,"end":441,"reference_id":"36563792","reference_source":"pmid","reference_html":"The discovery of 3,3-dimethyl-1,2,3,4-tetrahydroquinoxaline-1-carboxamides as AMPD2 inhibitors with a novel mechanism of action. <i> Kitao Y, Saito T, Watanabe S, Ohe Y, Takahashi K, Akaki T, Adachi T, Doi S, Yamanaka K, Murai Y, Oba M, Suzuki T. </i> Bioorg Med Chem Lett, 2023","date":"2023-04-12T08:35:26.637Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"8HUB"}],"region_id":"DP03968r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:166451149"}],"statement":[{"text":"The structural information revealed that compound 8 is accommodated in a new pocket upon the conformational change in the AMPD2-AMP co-structure, while the flexible loop was not visible.","type":"Article"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:18:55.172Z"}},{"start":228,"end":248,"reference_id":"36563792","reference_source":"pmid","reference_html":"The discovery of 3,3-dimethyl-1,2,3,4-tetrahydroquinoxaline-1-carboxamides as AMPD2 inhibitors with a novel mechanism of action. <i> Kitao Y, Saito T, Watanabe S, Ohe Y, Takahashi K, Akaki T, Adachi T, Doi S, Yamanaka K, Murai Y, Oba M, Suzuki T. </i> Bioorg Med Chem Lett, 2023","date":"2023-02-22T14:50:47.853Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"8HU6"}],"region_id":"DP03968r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6083"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-04T13:53:48.121Z"}}],"regions_counter":3,"released":"2023_06","sequence":"MASYPSGSGKPKAKYPFKKRASLQASTAAPEARGGLGAPPLQSARSLPGPAPCLKHFPLDLRTSMDGKCKEIAEELFTRSLAESELRSAPYEFPEESPIEQLEERRQRLERQISQDVKLEPDILLRAKQDFLKTDSDSDLQLYKEQGEGQGDRSLRERDVLEREFQRVTISGEEKCGVPFTDLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQGPDTPVSADAPVHPPALEQHPYEHCEPSTMPGDLGLGLRMVRGVVHVYTRREPDEHCSEVELPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALITQAVQSEMLETIPEEAGITMSPGPQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Stress response proteins"],"alphafold_very_low_content":0.2229806598407281,"disorder_content":0.08848484848484849,"disprot_consensus":{"full":[{"start":228,"end":248,"type":"D"},{"start":390,"end":441,"type":"D"}],"Structural state":[{"start":228,"end":248,"type":"D"},{"start":390,"end":441,"type":"D"}]}},{"disprot_id":"DP03969","acc":"Q9H1A4","creator":"fkordevani","date":"2023-02-22T14:56:21.906Z","features":{"pfam":[{"id":"PF12859","name":"Anaphase-promoting complex subunit 1 WD40 beta-propeller domain","start":81,"end":200},{"id":"PF12859","name":"Anaphase-promoting complex subunit 1 WD40 beta-propeller domain","start":589,"end":664},{"id":"PF18122","name":"Anaphase-promoting complex sub unit 1 C-terminal domain","start":1736,"end":1895},{"id":"PF20518","name":"Anaphase-promoting complex subunit 1 middle domain","start":666,"end":985},{"id":"PF21282","name":"APC1 beta sandwich domain","start":1617,"end":1702},{"id":"PF27562","name":"APC1 fourth domain","start":1024,"end":1216},{"id":"PF29300","name":"APC1 fifth domain","start":1223,"end":1615}],"gene3D":[]},"genes":[{"name":{"value":"ANAPC1"},"synonyms":[{"value":"TSG24"}]}],"length":1944,"name":"Anaphase-promoting complex subunit 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":10,"reference_id":"27259151","reference_source":"pmid","reference_html":"Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C. <i> Brown NG, VanderLinden R, Watson ER, Weissmann F, Ordureau A, Wu KP, Zhang W, Yu S, Mercredi PY, Harrison JS, Davidson IF, Qiao R, Lu Y, Dube P, Brunner MR, Grace CRR, Miller DJ, Haselbach D, Jarvis MA, Yamaguchi M, Yanishevski D, Petzold G, Sidhu SS, Kuhlman B, Kirschner MW, Harper JW, Peters JM, Stark H, Schulman BA. </i> Cell, 2016","date":"2023-04-12T09:43:56.434Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5L9U"},{"db":"PDB","id":"5L9T"},{"db":"EMDB","id":"3432"},{"db":"EMDB","id":"3433"}],"region_id":"DP03969r001","statement":[{"text":"The electron microscopy of the human Anaphase-promoting complex/Cyclosome with E2 UBE2S and UBE2C shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:20:30.337Z"}},{"start":33,"end":70,"reference_id":"27259151","reference_source":"pmid","reference_html":"Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C. <i> Brown NG, VanderLinden R, Watson ER, Weissmann F, Ordureau A, Wu KP, Zhang W, Yu S, Mercredi PY, Harrison JS, Davidson IF, Qiao R, Lu Y, Dube P, Brunner MR, Grace CRR, Miller DJ, Haselbach D, Jarvis MA, Yamaguchi M, Yanishevski D, Petzold G, Sidhu SS, Kuhlman B, Kirschner MW, Harper JW, Peters JM, Stark H, Schulman BA. </i> Cell, 2016","date":"2023-04-12T09:44:14.909Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5L9U"},{"db":"PDB","id":"5L9T"},{"db":"EMDB","id":"3432"},{"db":"EMDB","id":"3433"}],"region_id":"DP03969r002","statement":[{"text":"The electron microscopy of the human Anaphase-promoting complex/Cyclosome with E2 UBE2S and UBE2C shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:20:29.790Z"}},{"start":134,"end":145,"reference_id":"27259151","reference_source":"pmid","reference_html":"Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C. <i> Brown NG, VanderLinden R, Watson ER, Weissmann F, Ordureau A, Wu KP, Zhang W, Yu S, Mercredi PY, Harrison JS, Davidson IF, Qiao R, Lu Y, Dube P, Brunner MR, Grace CRR, Miller DJ, Haselbach D, Jarvis MA, Yamaguchi M, Yanishevski D, Petzold G, Sidhu SS, Kuhlman B, Kirschner MW, Harper JW, Peters JM, Stark H, Schulman BA. </i> Cell, 2016","date":"2023-04-12T09:44:33.988Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5L9U"},{"db":"PDB","id":"5L9T"},{"db":"EMDB","id":"3432"},{"db":"EMDB","id":"3433"}],"region_id":"DP03969r003","statement":[{"text":"The electron microscopy of the human Anaphase-promoting complex/Cyclosome with E2 UBE2S and UBE2C shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:20:28.401Z"}},{"start":193,"end":205,"reference_id":"27259151","reference_source":"pmid","reference_html":"Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C. <i> Brown NG, VanderLinden R, Watson ER, Weissmann F, Ordureau A, Wu KP, Zhang W, Yu S, Mercredi PY, Harrison JS, Davidson IF, Qiao R, Lu Y, Dube P, Brunner MR, Grace CRR, Miller DJ, Haselbach D, Jarvis MA, Yamaguchi M, Yanishevski D, Petzold G, Sidhu SS, Kuhlman B, Kirschner MW, Harper JW, Peters JM, Stark H, Schulman BA. </i> Cell, 2016","date":"2023-04-12T09:44:52.759Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5L9U"},{"db":"PDB","id":"5L9T"},{"db":"EMDB","id":"3432"},{"db":"EMDB","id":"3433"}],"region_id":"DP03969r004","statement":[{"text":"The electron microscopy of the human Anaphase-promoting complex/Cyclosome with E2 UBE2S and UBE2C shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:20:27.348Z"}},{"start":277,"end":403,"reference_id":"27259151","reference_source":"pmid","reference_html":"Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C. <i> Brown NG, VanderLinden R, Watson ER, Weissmann F, Ordureau A, Wu KP, Zhang W, Yu S, Mercredi PY, Harrison JS, Davidson IF, Qiao R, Lu Y, Dube P, Brunner MR, Grace CRR, Miller DJ, Haselbach D, Jarvis MA, Yamaguchi M, Yanishevski D, Petzold G, Sidhu SS, Kuhlman B, Kirschner MW, Harper JW, Peters JM, Stark H, Schulman BA. </i> Cell, 2016","date":"2023-04-12T09:45:11.897Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5L9U"},{"db":"PDB","id":"5L9T"},{"db":"EMDB","id":"3432"},{"db":"EMDB","id":"3433"}],"region_id":"DP03969r005","statement":[{"text":"The electron microscopy of the human Anaphase-promoting complex/Cyclosome with E2 UBE2S and UBE2C shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:20:26.306Z"}},{"start":513,"end":580,"reference_id":"27259151","reference_source":"pmid","reference_html":"Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C. <i> Brown NG, VanderLinden R, Watson ER, Weissmann F, Ordureau A, Wu KP, Zhang W, Yu S, Mercredi PY, Harrison JS, Davidson IF, Qiao R, Lu Y, Dube P, Brunner MR, Grace CRR, Miller DJ, Haselbach D, Jarvis MA, Yamaguchi M, Yanishevski D, Petzold G, Sidhu SS, Kuhlman B, Kirschner MW, Harper JW, Peters JM, Stark H, Schulman BA. </i> Cell, 2016","date":"2023-04-12T09:45:36.840Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5L9U"},{"db":"PDB","id":"5L9T"},{"db":"EMDB","id":"3432"},{"db":"EMDB","id":"3433"}],"region_id":"DP03969r006","statement":[{"text":"The electron microscopy of the human Anaphase-promoting complex/Cyclosome with E2 UBE2S and UBE2C shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:20:25.088Z"}},{"start":671,"end":703,"reference_id":"27259151","reference_source":"pmid","reference_html":"Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C. <i> Brown NG, VanderLinden R, Watson ER, Weissmann F, Ordureau A, Wu KP, Zhang W, Yu S, Mercredi PY, Harrison JS, Davidson IF, Qiao R, Lu Y, Dube P, Brunner MR, Grace CRR, Miller DJ, Haselbach D, Jarvis MA, Yamaguchi M, Yanishevski D, Petzold G, Sidhu SS, Kuhlman B, Kirschner MW, Harper JW, Peters JM, Stark H, Schulman BA. </i> Cell, 2016","date":"2023-04-12T09:45:54.339Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5L9U"},{"db":"PDB","id":"5L9T"},{"db":"EMDB","id":"3432"},{"db":"EMDB","id":"3433"}],"region_id":"DP03969r007","statement":[{"text":"The electron microscopy of the human Anaphase-promoting complex/Cyclosome with E2 UBE2S and UBE2C shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:20:23.920Z"}},{"start":732,"end":756,"reference_id":"27259151","reference_source":"pmid","reference_html":"Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C. <i> Brown NG, VanderLinden R, Watson ER, Weissmann F, Ordureau A, Wu KP, Zhang W, Yu S, Mercredi PY, Harrison JS, Davidson IF, Qiao R, Lu Y, Dube P, Brunner MR, Grace CRR, Miller DJ, Haselbach D, Jarvis MA, Yamaguchi M, Yanishevski D, Petzold G, Sidhu SS, Kuhlman B, Kirschner MW, Harper JW, Peters JM, Stark H, Schulman BA. </i> Cell, 2016","date":"2023-04-12T09:46:12.118Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5L9U"},{"db":"PDB","id":"5L9T"},{"db":"EMDB","id":"3432"},{"db":"EMDB","id":"3433"}],"region_id":"DP03969r008","statement":[{"text":"The electron microscopy of the human Anaphase-promoting complex/Cyclosome with E2 UBE2S and UBE2C shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:20:22.638Z"}},{"start":815,"end":838,"reference_id":"27259151","reference_source":"pmid","reference_html":"Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C. <i> Brown NG, VanderLinden R, Watson ER, Weissmann F, Ordureau A, Wu KP, Zhang W, Yu S, Mercredi PY, Harrison JS, Davidson IF, Qiao R, Lu Y, Dube P, Brunner MR, Grace CRR, Miller DJ, Haselbach D, Jarvis MA, Yamaguchi M, Yanishevski D, Petzold G, Sidhu SS, Kuhlman B, Kirschner MW, Harper JW, Peters JM, Stark H, Schulman BA. </i> Cell, 2016","date":"2023-04-12T09:50:35.372Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5L9U"},{"db":"PDB","id":"5L9T"},{"db":"EMDB","id":"3432"},{"db":"EMDB","id":"3433"}],"region_id":"DP03969r009","statement":[{"text":"The electron microscopy of the human Anaphase-promoting complex/Cyclosome with E2 UBE2S and UBE2C shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:20:21.170Z"}},{"start":883,"end":923,"reference_id":"27259151","reference_source":"pmid","reference_html":"Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C. <i> Brown NG, VanderLinden R, Watson ER, Weissmann F, Ordureau A, Wu KP, Zhang W, Yu S, Mercredi PY, Harrison JS, Davidson IF, Qiao R, Lu Y, Dube P, Brunner MR, Grace CRR, Miller DJ, Haselbach D, Jarvis MA, Yamaguchi M, Yanishevski D, Petzold G, Sidhu SS, Kuhlman B, Kirschner MW, Harper JW, Peters JM, Stark H, Schulman BA. </i> Cell, 2016","date":"2023-04-12T09:50:18.945Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5L9U"},{"db":"PDB","id":"5L9T"},{"db":"EMDB","id":"3432"},{"db":"EMDB","id":"3433"}],"region_id":"DP03969r010","statement":[{"text":"The electron microscopy of the human Anaphase-promoting complex/Cyclosome with E2 UBE2S and UBE2C shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:20:20.309Z"}},{"start":987,"end":1012,"reference_id":"27259151","reference_source":"pmid","reference_html":"Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C. <i> Brown NG, VanderLinden R, Watson ER, Weissmann F, Ordureau A, Wu KP, Zhang W, Yu S, Mercredi PY, Harrison JS, Davidson IF, Qiao R, Lu Y, Dube P, Brunner MR, Grace CRR, Miller DJ, Haselbach D, Jarvis MA, Yamaguchi M, Yanishevski D, Petzold G, Sidhu SS, Kuhlman B, Kirschner MW, Harper JW, Peters JM, Stark H, Schulman BA. </i> Cell, 2016","date":"2023-04-12T09:49:55.803Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5L9T"},{"db":"PDB","id":"5L9U"},{"db":"EMDB","id":"3432"},{"db":"EMDB","id":"3433"}],"region_id":"DP03969r011","statement":[{"text":"The electron microscopy of the human Anaphase-promoting complex/Cyclosome with E2 UBE2S and UBE2C shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:20:19.320Z"}},{"start":1334,"end":1346,"reference_id":"27259151","reference_source":"pmid","reference_html":"Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C. <i> Brown NG, VanderLinden R, Watson ER, Weissmann F, Ordureau A, Wu KP, Zhang W, Yu S, Mercredi PY, Harrison JS, Davidson IF, Qiao R, Lu Y, Dube P, Brunner MR, Grace CRR, Miller DJ, Haselbach D, Jarvis MA, Yamaguchi M, Yanishevski D, Petzold G, Sidhu SS, Kuhlman B, Kirschner MW, Harper JW, Peters JM, Stark H, Schulman BA. </i> Cell, 2016","date":"2023-04-12T09:49:40.571Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5L9T"},{"db":"PDB","id":"5L9U"},{"db":"EMDB","id":"3432"},{"db":"EMDB","id":"3433"}],"region_id":"DP03969r012","statement":[{"text":"The electron microscopy of the human Anaphase-promoting complex/Cyclosome with E2 UBE2S and UBE2C shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:20:18.453Z"}},{"start":1438,"end":1451,"reference_id":"27259151","reference_source":"pmid","reference_html":"Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C. <i> Brown NG, VanderLinden R, Watson ER, Weissmann F, Ordureau A, Wu KP, Zhang W, Yu S, Mercredi PY, Harrison JS, Davidson IF, Qiao R, Lu Y, Dube P, Brunner MR, Grace CRR, Miller DJ, Haselbach D, Jarvis MA, Yamaguchi M, Yanishevski D, Petzold G, Sidhu SS, Kuhlman B, Kirschner MW, Harper JW, Peters JM, Stark H, Schulman BA. </i> Cell, 2016","date":"2023-04-12T09:48:23.057Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5L9T"},{"db":"PDB","id":"5L9U"},{"db":"EMDB","id":"3432"},{"db":"EMDB","id":"3433"}],"region_id":"DP03969r013","statement":[{"text":"The electron microscopy of the human Anaphase-promoting complex/Cyclosome with E2 UBE2S and UBE2C shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:20:17.549Z"}},{"start":1705,"end":1746,"reference_id":"27259151","reference_source":"pmid","reference_html":"Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C. <i> Brown NG, VanderLinden R, Watson ER, Weissmann F, Ordureau A, Wu KP, Zhang W, Yu S, Mercredi PY, Harrison JS, Davidson IF, Qiao R, Lu Y, Dube P, Brunner MR, Grace CRR, Miller DJ, Haselbach D, Jarvis MA, Yamaguchi M, Yanishevski D, Petzold G, Sidhu SS, Kuhlman B, Kirschner MW, Harper JW, Peters JM, Stark H, Schulman BA. </i> Cell, 2016","date":"2023-04-12T09:48:05.066Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5L9T"},{"db":"PDB","id":"5L9U"},{"db":"EMDB","id":"3432"},{"db":"EMDB","id":"3433"}],"region_id":"DP03969r014","statement":[{"text":"The electron microscopy of the human Anaphase-promoting complex/Cyclosome with E2 UBE2S and UBE2C shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:20:16.666Z"}},{"start":1756,"end":1769,"reference_id":"27259151","reference_source":"pmid","reference_html":"Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C. <i> Brown NG, VanderLinden R, Watson ER, Weissmann F, Ordureau A, Wu KP, Zhang W, Yu S, Mercredi PY, Harrison JS, Davidson IF, Qiao R, Lu Y, Dube P, Brunner MR, Grace CRR, Miller DJ, Haselbach D, Jarvis MA, Yamaguchi M, Yanishevski D, Petzold G, Sidhu SS, Kuhlman B, Kirschner MW, Harper JW, Peters JM, Stark H, Schulman BA. </i> Cell, 2016","date":"2023-04-12T09:47:47.096Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5L9T"},{"db":"PDB","id":"5L9U"},{"db":"EMDB","id":"3432"},{"db":"EMDB","id":"3433"}],"region_id":"DP03969r015","statement":[{"text":"The electron microscopy of the human Anaphase-promoting complex/Cyclosome with E2 UBE2S and UBE2C shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:20:15.556Z"}},{"start":1828,"end":1838,"reference_id":"27259151","reference_source":"pmid","reference_html":"Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C. <i> Brown NG, VanderLinden R, Watson ER, Weissmann F, Ordureau A, Wu KP, Zhang W, Yu S, Mercredi PY, Harrison JS, Davidson IF, Qiao R, Lu Y, Dube P, Brunner MR, Grace CRR, Miller DJ, Haselbach D, Jarvis MA, Yamaguchi M, Yanishevski D, Petzold G, Sidhu SS, Kuhlman B, Kirschner MW, Harper JW, Peters JM, Stark H, Schulman BA. </i> Cell, 2016","date":"2023-04-12T09:47:29.508Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5L9T"},{"db":"PDB","id":"5L9U"},{"db":"EMDB","id":"3432"},{"db":"EMDB","id":"3433"}],"region_id":"DP03969r016","statement":[{"text":"The electron microscopy of the human Anaphase-promoting complex/Cyclosome with E2 UBE2S and UBE2C shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:20:14.508Z"}},{"start":1896,"end":1907,"reference_id":"27259151","reference_source":"pmid","reference_html":"Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C. <i> Brown NG, VanderLinden R, Watson ER, Weissmann F, Ordureau A, Wu KP, Zhang W, Yu S, Mercredi PY, Harrison JS, Davidson IF, Qiao R, Lu Y, Dube P, Brunner MR, Grace CRR, Miller DJ, Haselbach D, Jarvis MA, Yamaguchi M, Yanishevski D, Petzold G, Sidhu SS, Kuhlman B, Kirschner MW, Harper JW, Peters JM, Stark H, Schulman BA. </i> Cell, 2016","date":"2023-04-12T09:47:11.519Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5L9U"},{"db":"PDB","id":"5L9T"},{"db":"EMDB","id":"3432"},{"db":"EMDB","id":"3433"}],"region_id":"DP03969r017","statement":[{"text":"The electron microscopy of the human Anaphase-promoting complex/Cyclosome with E2 UBE2S and UBE2C shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:20:13.706Z"}},{"start":1933,"end":1944,"reference_id":"27259151","reference_source":"pmid","reference_html":"Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C. <i> Brown NG, VanderLinden R, Watson ER, Weissmann F, Ordureau A, Wu KP, Zhang W, Yu S, Mercredi PY, Harrison JS, Davidson IF, Qiao R, Lu Y, Dube P, Brunner MR, Grace CRR, Miller DJ, Haselbach D, Jarvis MA, Yamaguchi M, Yanishevski D, Petzold G, Sidhu SS, Kuhlman B, Kirschner MW, Harper JW, Peters JM, Stark H, Schulman BA. </i> Cell, 2016","date":"2023-04-12T09:46:54.365Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5L9U"},{"db":"PDB","id":"5L9T"},{"db":"EMDB","id":"3432"},{"db":"EMDB","id":"3433"}],"region_id":"DP03969r018","statement":[{"text":"The electron microscopy of the human Anaphase-promoting complex/Cyclosome with E2 UBE2S and UBE2C shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:20:13.071Z"}}],"regions_counter":18,"released":"2023_06","sequence":"MSNFYEERTTMIAARDLQEFVPFGRDHCKHHPNALNLQLRQLQPASELWSSDGAAGLVGSLQEVTIHEKQKESWQLRKGVSEIGEDVDYDEELYVAGNMVIWSKGSKSQALAVYKAFTVDSPVQQALWCDFIISQDKSEKAYSSNEVEKCICILQSSCINMHSIEGKDYIASLPFQVANVWPTKYGLLFERSASSHEVPPGSPREPLPTMFSMLHPLDEITPLVCKSGSLFGSSRVQYVVDHAMKIVFLNTDPSIVMTYDAVQNVHSVWTLRRVKSEEENVVLKFSEQGGTPQNVATSSSLTAHLRSLSKGDSPVTSPFQNYSSIHSQSRSTSSPSLHSRSPSISNMAALSRAHSPALGVHSFSGVQRFNISSHNQSPKRHSISHSPNSNSNGSFLAPETEPIVPELCIDHLWTETITNIREKNSQASKVFITSDLCGQKFLCFLVESQLQLRCVKFQESNDKTQLIFGSVTNIPAKDAAPVEKIDTMLVLEGSGNLVLYTGVVRVGKVFIPGLPAPSLTMSNTMPRPSTPLDGVSTPKPLSKLLGSLDEVVLLSPVPELRDSSKLHDSLYNEDCTFQQLGTYIHSIRDPVHNRVTLELSNGSMVRITIPEIATSELVQTCLQAIKFILPKEIAVQMLVKWYNVHSAPGGPSYHSEWNLFVTCLMNMMGYNTDRLAWTRNFDFEGSLSPVIAPKKARPSETGSDDDWEYLLNSDYHQNVESHLLNRSLCLSPSEASQMKDEDFSQNLSLDSSTLLFTHIPAIFFVLHLVYEELKLNTLMGEGICSLVELLVQLARDLKLGPYVDHYYRDYPTLVRTTGQVCTIDPGQTGFMHHPSFFTSEPPSIYQWVSSCLKGEGMPPYPYLPGICERSRLVVLSIALYILGDESLVSDESSQYLTRITIAPQKLQVEQEENRFSFRHSTSVSSLAERLVVWMTNVGFTLRDLETLPFGIALPIRDAIYHCREQPASDWPEAVCLLIGRQDLSKQACEGNLPKGKSVLSSDVPSGTETEEEDDGMNDMNHEVMSLIWSEDLRVQDVRRLLQSAHPVRVNVVQYPELSDHEFIEEKENRLLQLCQRTMALPVGRGMFTLFSYHPVPTEPLPIPKLNLTGRAPPRNTTVDLNSGNIDVPPNMTSWASFHNGVAAGLKIAPASQIDSAWIVYNKPKHAELANEYAGFLMALGLNGHLTKLATLNIHDYLTKGHEMTSIGLLLGVSAAKLGTMDMSITRLLSIHIPALLPPTSTELDVPHNVQVAAVVGIGLVYQGTAHRHTAEVLLAEIGRPPGPEMEYCTDRESYSLAAGLALGMVCLGHGSNLIGMSDLNVPEQLYQYMVGGHRRFQTGMHREKHKSPSYQIKEGDTINVDVTCPGATLALAMIYLKTNNRSIADWLRAPDTMYLLDFVKPEFLLLRTLARCLILWDDILPNSKWVDSNVPQIIRENSISLSEIELPCSEDLNLETLSQAHVYIIAGACLSLGFRFAGSENLSAFNCLHKFAKDFMTYLSAPNASVTGPHNLETCLSVVLLSLAMVMAGSGNLKVLQLCRFLHMKTGGEMNYGFHLAHHMALGLLFLGGGRYSLSTSNSSIAALLCALYPHFPAHSTDNRYHLQALRHLYVLAAEPRLLVPVDVDTNTPCYALLEVTYKGTQWYEQTKEELMAPTLLPELHLLKQIKVKGPRYWELLIDLSKGTQHLKSILSKDGVLYVKLRAGQLSYKEDPMGWQSLLAQTVANRNSEARAFKPETISAFTSDPALLSFAEYFCKPTVNMGQKQEILDLFSSVLYECVTQETPEMLPAYIAMDQAIRRLGRREMSETSELWQIKLVLEFFSSRSHQERLQNHPKRGLFMNSEFLPVVKCTIDNTLDQWLQVGGDMCVHAYLSGQPLEESQLSMLACFLVYHSVPAPQHLPPIGLEGSTSFAELLFKFKQLKMPVRALLRLAPLLLGNPQPMVM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Stress response proteins"],"alphafold_very_low_content":0.16203703703703703,"disorder_content":0.2752057613168724,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"},{"start":33,"end":70,"type":"D"},{"start":134,"end":145,"type":"D"},{"start":193,"end":205,"type":"D"},{"start":277,"end":403,"type":"D"},{"start":513,"end":580,"type":"D"},{"start":671,"end":703,"type":"D"},{"start":732,"end":756,"type":"D"},{"start":815,"end":838,"type":"D"},{"start":883,"end":923,"type":"D"},{"start":987,"end":1012,"type":"D"},{"start":1334,"end":1346,"type":"D"},{"start":1438,"end":1451,"type":"D"},{"start":1705,"end":1746,"type":"D"},{"start":1756,"end":1769,"type":"D"},{"start":1828,"end":1838,"type":"D"},{"start":1896,"end":1907,"type":"D"},{"start":1933,"end":1944,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":33,"end":70,"type":"D"},{"start":134,"end":145,"type":"D"},{"start":193,"end":205,"type":"D"},{"start":277,"end":403,"type":"D"},{"start":513,"end":580,"type":"D"},{"start":671,"end":703,"type":"D"},{"start":732,"end":756,"type":"D"},{"start":815,"end":838,"type":"D"},{"start":883,"end":923,"type":"D"},{"start":987,"end":1012,"type":"D"},{"start":1334,"end":1346,"type":"D"},{"start":1438,"end":1451,"type":"D"},{"start":1705,"end":1746,"type":"D"},{"start":1756,"end":1769,"type":"D"},{"start":1828,"end":1838,"type":"D"},{"start":1896,"end":1907,"type":"D"},{"start":1933,"end":1944,"type":"D"}]}},{"disprot_id":"DP03970","acc":"Q9NW15","creator":"fkordevani","date":"2023-02-22T15:51:33.219Z","features":{"pfam":[{"id":"PF04547","name":"Calcium-activated chloride channel","start":200,"end":626}],"gene3D":[]},"genes":[{"name":{"value":"ANO10"},"synonyms":[{"value":"TMEM16K"}]}],"length":660,"name":"Anoctamin-10","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":12,"reference_id":"31477691","reference_source":"pmid","reference_html":"The structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K. <i> Bushell SR, Pike ACW, Falzone ME, Rorsman NJG, Ta CM, Corey RA, Newport TD, Christianson JC, Scofano LF, Shintre CA, Tessitore A, Chu A, Wang Q, Shrestha L, Mukhopadhyay SMM, Love JD, Burgess-Brown NA, Sitsapesan R, Stansfeld PJ, Huiskonen JT, Tammaro P, Accardi A, Carpenter EP. </i> Nat Commun, 2019","date":"2023-04-12T10:28:30.644Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6R7Y"},{"db":"PDB","id":"6R7Z"},{"db":"PDB","id":"6R7X"},{"db":"PDB","id":"6R65"},{"db":"EMDB","id":"4746"},{"db":"EMDB","id":"4747"},{"db":"EMDB","id":"4748"}],"region_id":"DP03970r001","statement":[{"text":"The final model encompasses all residues from Ser13-Lys641 and three Ca2+ ions per monomer (Supplementary Table 3).","type":"Methods"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271","statements":[{"type":"Results","text":"To understand whether TMEM16K can adopt alternative conformations and how changes in Ca2+ concentration affect the structure, we obtained three electron cryomicroscopy (cryo-EM) structures for TMEM16K in the presence of (i) 2mM (‘high’) Ca2+, (ii) 430nM (‘low’) Ca2+ and (iii) in the absence of Ca2+ (in 10mM ethylene glycol-bis(β-aminoethyl ether)-N,N,N′,N′-tetraacetic acid (EGTA), ‘Ca2+-free’)."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5287971"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:447793","statements":[{"type":"Results","text":"All the protein samples used in cryo-EM were purified in the detergent undecyl maltoside (UDM) with cholesteryl hemisuccinate (CHS) added to improve protein stability: the same lipid detergent combination that was used for the VD crystallization."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:65082","statements":[{"type":"Results","text":"All the protein samples used in cryo-EM were purified in the detergent undecyl maltoside (UDM) with cholesteryl hemisuccinate (CHS) added to improve protein stability: the same lipid detergent combination that was used for the VD crystallization."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:38:11.402Z"}},{"start":642,"end":660,"reference_id":"31477691","reference_source":"pmid","reference_html":"The structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K. <i> Bushell SR, Pike ACW, Falzone ME, Rorsman NJG, Ta CM, Corey RA, Newport TD, Christianson JC, Scofano LF, Shintre CA, Tessitore A, Chu A, Wang Q, Shrestha L, Mukhopadhyay SMM, Love JD, Burgess-Brown NA, Sitsapesan R, Stansfeld PJ, Huiskonen JT, Tammaro P, Accardi A, Carpenter EP. </i> Nat Commun, 2019","date":"2023-04-12T10:28:56.429Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6R7Y"},{"db":"PDB","id":"6R7Z"},{"db":"PDB","id":"6R7X"},{"db":"PDB","id":"6R65"},{"db":"EMDB","id":"4746"},{"db":"EMDB","id":"4747"},{"db":"EMDB","id":"4748"}],"region_id":"DP03970r002","statement":[{"text":"The final model encompasses all residues from Ser13-Lys641 and three Ca2+ ions per monomer (Supplementary Table 3).","type":"Methods"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271","statements":[{"type":"Results","text":"To understand whether TMEM16K can adopt alternative conformations and how changes in Ca2+ concentration affect the structure, we obtained three electron cryomicroscopy (cryo-EM) structures for TMEM16K in the presence of (i) 2mM (‘high’) Ca2+, (ii) 430nM (‘low’) Ca2+ and (iii) in the absence of Ca2+ (in 10mM ethylene glycol-bis(β-aminoethyl ether)-N,N,N′,N′-tetraacetic acid (EGTA), ‘Ca2+-free’)."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5287971"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:447793","statements":[{"type":"Results","text":"All the protein samples used in cryo-EM were purified in the detergent undecyl maltoside (UDM) with cholesteryl hemisuccinate (CHS) added to improve protein stability: the same lipid detergent combination that was used for the VD crystallization."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:65082","statements":[{"type":"Results","text":"All the protein samples used in cryo-EM were purified in the detergent undecyl maltoside (UDM) with cholesteryl hemisuccinate (CHS) added to improve protein stability: the same lipid detergent combination that was used for the VD crystallization."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:37:59.311Z"}},{"start":463,"end":474,"reference_id":"31477691","reference_source":"pmid","reference_html":"The structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K. <i> Bushell SR, Pike ACW, Falzone ME, Rorsman NJG, Ta CM, Corey RA, Newport TD, Christianson JC, Scofano LF, Shintre CA, Tessitore A, Chu A, Wang Q, Shrestha L, Mukhopadhyay SMM, Love JD, Burgess-Brown NA, Sitsapesan R, Stansfeld PJ, Huiskonen JT, Tammaro P, Accardi A, Carpenter EP. </i> Nat Commun, 2019","date":"2023-04-12T10:31:07.950Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6R7Z"},{"db":"EMDB","id":"4748"}],"region_id":"DP03970r003","statement":[{"text":"The cytoplasmic α7−α8 region was poorly resolved and truncated between residues 463–474.","type":"Methods"}],"sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:447793","statements":[{"type":"Results","text":"All the protein samples used in cryo-EM were purified in the detergent undecyl maltoside (UDM) with cholesteryl hemisuccinate (CHS) added to improve protein stability: the same lipid detergent combination that was used for the VD crystallization."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:65082","statements":[{"type":"Results","text":"All the protein samples used in cryo-EM were purified in the detergent undecyl maltoside (UDM) with cholesteryl hemisuccinate (CHS) added to improve protein stability: the same lipid detergent combination that was used for the VD crystallization."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:37:09.306Z"}},{"start":1,"end":13,"reference_id":"31477691","reference_source":"pmid","reference_html":"The structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K. <i> Bushell SR, Pike ACW, Falzone ME, Rorsman NJG, Ta CM, Corey RA, Newport TD, Christianson JC, Scofano LF, Shintre CA, Tessitore A, Chu A, Wang Q, Shrestha L, Mukhopadhyay SMM, Love JD, Burgess-Brown NA, Sitsapesan R, Stansfeld PJ, Huiskonen JT, Tammaro P, Accardi A, Carpenter EP. </i> Nat Commun, 2019","date":"2023-04-13T09:17:49.296Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5OC9"}],"region_id":"DP03970r004","statement":[{"text":"The final LCP model encompasses residues Ser14 to Gln639.","type":"Methods"}],"sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:74627694"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-12T15:09:05.259Z"}},{"start":640,"end":660,"reference_id":"31477691","reference_source":"pmid","reference_html":"The structural basis of lipid scrambling and inactivation in the endoplasmic reticulum scramblase TMEM16K. <i> Bushell SR, Pike ACW, Falzone ME, Rorsman NJG, Ta CM, Corey RA, Newport TD, Christianson JC, Scofano LF, Shintre CA, Tessitore A, Chu A, Wang Q, Shrestha L, Mukhopadhyay SMM, Love JD, Burgess-Brown NA, Sitsapesan R, Stansfeld PJ, Huiskonen JT, Tammaro P, Accardi A, Carpenter EP. </i> Nat Commun, 2019","date":"2023-04-12T10:26:05.184Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5OC9"}],"region_id":"DP03970r005","statement":[{"text":"The final LCP model encompasses residues Ser14 to Gln639.","type":"Methods"}],"sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:74627694"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:36:24.937Z"}}],"regions_counter":5,"released":"2023_06","sequence":"MKVTLSALDTSESSFTPLVVIELAQDVKEETKEWLKNRIIAKKKDGGAQLLFRPLLNKYEQETLENQNLYLVGASKIRMLLGAEAVGLVKECNDNTMRAFTYRTRQNFKGFDDNNDDFLTMAECQFIIKHELENLRAKDEKMIPGYPQAKLYPGKSLLRRLLTSGIVIQVFPLHDSEALKKLEDTWYTRFALKYQPIDSIRGYFGETIALYFGFLEYFTFALIPMAVIGLPYYLFVWEDYDKYVIFASFNLIWSTVILELWKRGCANMTYRWGTLLMKRKFEEPRPGFHGVLGINSITGKEEPLYPSYKRQLRIYLVSLPFVCLCLYFSLYVMMIYFDMEVWALGLHENSGSEWTSVLLYVPSIIYAIVIEIMNRLYRYAAEFLTSWENHRLESAYQNHLILKVLVFNFLNCFASLFYIAFVLKDMKLLRQSLATLLITSQILNQIMESFLPYWLQRKHGVRVKRKVQALKADIDATLYEQVILEKEMGTYLGTFDDYLELFLQFGYVSLFSCVYPLAAAFAVLNNFTEVNSDALKMCRVFKRPFSEPSANIGVWQLAFETMSVISVVTNCALIGMSPQVNAVFPESKADLILIVVAVEHALLALKFILAFAIPDKPRHIQMKLARLEFESLEALKQQQMKLVTENLKEEPMESGKEKAT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Stress response proteins"],"alphafold_very_low_content":0.022727272727272728,"disorder_content":0.0696969696969697,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"D"},{"start":463,"end":474,"type":"D"},{"start":640,"end":660,"type":"D"}],"Structural state":[{"start":1,"end":13,"type":"D"},{"start":463,"end":474,"type":"D"},{"start":640,"end":660,"type":"D"}]}},{"disprot_id":"DP03971","acc":"Q10567","creator":"fkordevani","date":"2023-02-23T09:20:08.630Z","features":{"pfam":[{"id":"PF01602","name":"Adaptin N terminal region","start":12,"end":533},{"id":"PF02883","name":"Adaptin C-terminal domain","start":721,"end":826},{"id":"PF09066","name":"Beta2-adaptin appendage, C-terminal sub-domain","start":836,"end":947}],"gene3D":[]},"genes":[{"name":{"value":"AP1B1"},"synonyms":[{"value":"ADTB1"},{"value":"BAM22"},{"value":"CLAPB2"}]}],"length":949,"name":"AP-1 complex subunit beta-1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":13,"reference_id":"36261523","reference_source":"pmid","reference_html":"Clathrin-associated AP-1 controls termination of STING signalling. <i> Liu Y, Xu P, Rivara S, Liu C, Ricci J, Ren X, Hurley JH, Ablasser A. </i> Nature, 2022","date":"2023-04-12T09:53:28.846Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7R4H"}],"region_id":"DP03971r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84077"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P22892"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q86WV6"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P35585"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q96PC3"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:135398633"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-12T16:39:16.577Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MTDSKYFTTTKKGEIFELKAELNSDKKEKKKEAVKKVIASMTVGKDVSALFPDVVNCMQTDNLELKKLVYLYLMNYAKSQPDMAIMAVNTFVKDCEDPNPLIRALAVRTMGCIRVDKITEYLCEPLRKCLKDEDPYVRKTAAVCVAKLHDINAQLVEDQGFLDTLKDLISDSNPMVVANAVAALSEIAESHPSSNLLDLNPQSINKLLTALNECTEWGQIFILDCLANYMPKDDREAQSICERVTPRLSHANSAVVLSAVKVLMKFMEMLSKDLDYYGTLLKKLAPPLVTLLSAEPELQYVALRNINLIVQKRPEILKHEMKVFFVKYNDPIYVKLEKLDIMIRLASQANIAQVLAELKEYATEVDVDFVRKAVRAIGRCAIKVEQSAERCVSTLLDLIQTKVNYVVQEAIVVIKDIFRKYPNKYESVIATLCENLDSLDEPEARAAMIWIVGEYAERIDNADELLESFLEGFHDESTQVQLQLLTAIVKLFLKKPTETQELVQQVLSLATQDSDNPDLRDRGYIYWRLLSTDPVAAKEVVLAEKPLISEETDLIEPTLLDELICYIGTLASVYHKPPSAFVEGGRGVVHKSLPPRTASSESAESPETAPTGAPPGEQPDVIPAQGDLLGDLLNLDLGPPVSGPPLATSSVQMGAVDLLGGGLDSLMGDEPEGIGGTNFVAPPTAAVPANLGAPIGSGLSDLFDLTSGVGTLSGSYVAPKAVWLPAMKAKGLEISGTFTRQVGSISMDLQLTNKALQVMTDFAIQFNRNSFGLAPAAPLQVHAPLSPNQTVEISLPLSTVGSVMKMEPLNNLQVAVKNNIDVFYFSTLYPLHILFVEDGKMDRQMFLATWKDIPNENEAQFQIRDCPLNAEAASSKLQSSNIFTVAKRNVEGQDMLYQSLKLTNGIWVLAELRIQPGNPSCTDLELSLKCRAPEVSQHVYQAYETILKN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.1327713382507903,"disorder_content":0.0136986301369863,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"D"}],"Structural state":[{"start":1,"end":13,"type":"D"}]}},{"disprot_id":"DP03972","acc":"Q62768","creator":"zskalman","date":"2023-03-02T10:14:03.629Z","features":{"pfam":[{"id":"PF00130","name":"Phorbol esters/diacylglycerol binding domain (C1 domain)","start":567,"end":616},{"id":"PF00168","name":"C2 domain","start":4,"end":98},{"id":"PF00168","name":"C2 domain","start":690,"end":798},{"id":"PF00168","name":"C2 domain","start":1578,"end":1687},{"id":"PF06292","name":"MUN domain","start":1007,"end":1525}],"gene3D":[]},"genes":[{"name":{"value":"Unc13a","evidences":[{"code":"ECO:0000312","source":{"name":"RGD","id":"619722","url":"https://rgd.mcw.edu/tools/genes/genes_view.cgi?id=619722"}}]},"synonyms":[{"value":"Unc13h1"}]}],"length":1735,"name":"Protein unc-13 homolog A","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions":[{"start":1341,"end":1351,"reference_id":"22000513","reference_source":"pmid","reference_html":"The crystal structure of a Munc13 C-terminal module exhibits a remarkable similarity to vesicle tethering factors. <i> Li W, Ma C, Guan R, Xu Y, Tomchick DR, Rizo J. </i> Structure, 2011","date":"2023-03-02T10:18:56.095Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3SWH"}],"region_id":"DP03972r001","statement":[{"text":"Some of the loops connecting the helices did not yield interpretable electron density, suggesting that they are disordered. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-04T16:31:20.183Z"}},{"start":1458,"end":1467,"reference_id":"22000513","reference_source":"pmid","reference_html":"The crystal structure of a Munc13 C-terminal module exhibits a remarkable similarity to vesicle tethering factors. <i> Li W, Ma C, Guan R, Xu Y, Tomchick DR, Rizo J. </i> Structure, 2011","date":"2023-03-02T10:38:13.875Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3SWH"}],"region_id":"DP03972r002","statement":[{"text":"Some of the loops connecting the helices did not yield interpretable electron density, suggesting that they are disordered. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-04T16:31:29.479Z"}},{"start":1517,"end":1531,"reference_id":"22000513","reference_source":"pmid","reference_html":"The crystal structure of a Munc13 C-terminal module exhibits a remarkable similarity to vesicle tethering factors. <i> Li W, Ma C, Guan R, Xu Y, Tomchick DR, Rizo J. </i> Structure, 2011","date":"2023-03-02T10:39:09.831Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3SWH"}],"region_id":"DP03972r003","statement":[{"text":"Missing residues, by chain A: 1148-1155, 1341-1351, 1459-1468, 1515-1531\nB: 1148-1155, 1341-1351, 1458-1467, 1517-1531","type":"Table"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-04T16:31:40.852Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MSLLCVGVKKAKFDGAQEKFNTYVTLKVQNVKSTTIAVRGSQPSWEQDFMFEINRLDLGLTVEVWNKGLIWDTMVGTVWIPLRTIRQSNEEGPGEWLTLDSQAIMADSEICGTKDPTFHRILLDAHFELPLDIPEEEARYWAKKLEQLNAMRDQDEYSFQDQQDKPLPVPSSQCCNWNYFGWGEQNDDPDSAVDDRDSDYRSETSNSIPPPYYTTSQPNASVHQYSVRPPPLGSRESYSDSMHSYEEFSEPRALSPTGSSRYASSGELSQGSSQLSEDFDPDEHSLQGSELDDERDRDSYHSCHSSVSYHKDSPRWDQDEEDLEDLEDLEDEELPEEEELEEEELEEEEELEEEELELEEEEEVPDDLASYTQQEDTTVAEPKEFKRISFPTAAPQKEDKVSAVPIEAPDVSKGIPKAATPEEKAAAECAQEAEPPKSEESFRSREAEEGQEGQDAMSRAKANWLRAFNKVRMQLQEARGEGEMSKSLWFKGGPGGGLIIIDSMPDIRKRKPIPLVSDLAMSLVQSRKAGITSALASSTLNNEELKNHVYKKTLQALIYPISCTTPHNFEVWTATTPTYCYECEGLLWGIARQGMRCTECGVKCHEKCQDLLNADCLQRAAEKSSKHGAEDRTQNIIMVLKDRMKIRERNKPEIFELIQEVFAVTKSAHTQQMKAVKQSVLDGTSKWSAKISITVVCAQGLQAKDKTGSSDPYVTVQVGKTKKRTKTIYGNLNPVWEENFHFECHNSSDRIKVRVLDEDDDIKSRVKQRFKRESDDFLGQTIIEVRTLSGEMDVWYNLDKRTDKSAVSGAIRLHISVEIKGEEKVAPYHVQYTCLHENLFHFVTDVQNNGVVKIPDAKGDDAWKVYYDETAQEIVDEFAMRYGVESIYQAMTHFACLSSKYMCPGVPAVMSTLLANINAYYAHTTASTNVSASDRFAASNFGKERFVKLLDQLHNSLRIDLSMYRNNFPASSPERLQDLKSTVDLLTSITFFRMKVQELQSPPRASQVVKDCVKACLNSTYEYIFNNCHELYGREYQTDPAKKGEVPPEEQGPSIKNLDFWSKLITLIVSIIEEDKNSYTPCLNQFPQELNVGKISAEVMWSLFAQDMKYAMEEHDKHRLCKSADYMNLHFKVKWLYNEYVAELPTFKDRVPEYPAWFEPFVIQWLDENEEVSRDFLHGALERDKKDGFQQTSEHALFSCSVVDVFSQLNQSFEIIKKLECPDPQIVGHYMRRFAKTISNVLLQYADIVSKDFASYCSKEKEKVPCILMNNTQQLRVQLEKMFEAMGGKELDAEASGTLKELQVKLNNVLDELSHVFATSFQPHIEECVRQMGDILSQVKGTGNVPASACSSVAQDADNVLQPIMDLLDSNLTLFAKICEKTVLKRVLKELWKLVMNTMERTIVLPPLTDQTMIGTLLRKHGKGLEKGRVKLPSHSDGTQMIFNAAKELGQLSKLKDHMVREEAKSLTPKQCAVVELALDTIKQYFHAGGVGLKKTFLEKSPDLQSLRYALSLYTQATDLLIKTFVQTQSAQVHGGKGTRFTLSEDVCPEMGSGVEDPVGEVSVHVELFTHPGTGEQKVTVKVVAANDLKWQTSGIFRPFIEVNIVGPQLSDKKRKFATKSKNNSWAPKYNESFQFSLSADAGPECYELQVCVKDYCFAREDRTVELAVLQLRELAQRGSAACWLPLGRRIHMDDTGLTVLRILSQRSNDEVAKEFVKLKSDTRSAEEGGAAPAP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"alphafold_very_low_content":0.24553314121037464,"disorder_content":0.0207492795389049,"disprot_consensus":{"full":[{"start":1341,"end":1351,"type":"D"},{"start":1458,"end":1467,"type":"D"},{"start":1517,"end":1531,"type":"D"}],"Structural state":[{"start":1341,"end":1351,"type":"D"},{"start":1458,"end":1467,"type":"D"},{"start":1517,"end":1531,"type":"D"}]}},{"disprot_id":"DP03973","acc":"P33891","creator":"zskalman","date":"2023-03-02T10:44:56.829Z","features":{"pfam":[{"id":"PF04437","name":"RINT-1/TIP-1 family","start":239,"end":695}],"gene3D":[]},"genes":[{"name":{"value":"TIP20"},"synonyms":[{"value":"TIP1"}],"olnNames":[{"value":"YGL145W"}]}],"length":701,"name":"Protein transport protein TIP20","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":217,"end":234,"reference_id":"19151722","reference_source":"pmid","reference_html":"Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex. <i> Tripathi A, Ren Y, Jeffrey PD, Hughson FM. </i> Nat Struct Mol Biol, 2009","date":"2023-03-02T10:48:52.044Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3FHN"}],"region_id":"DP03973r001","statement":[{"text":"The final model (Supplementary Fig. 3) spans nearly the entire molecule, comprising residues 5-701, with residues 217-234 and 546-551 missing because of disordered loops that are not visible in any electron density map.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-04T16:45:48.438Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MNGIDDLLNINDRIKQVQNERNELASKLQNLKQSLASNDTEVALSEVIAQDIIEVGASVEGLEQLRAKYGDLQILNKLEKVAVQQTQMQAGVDKLDSFERQLDELAEQPPDQFTLDDVKALHSKLTSVFATVPQINNIDSQYAAYNKLKSKVTGKYNDVIIQRLATNWSNTFDQKLLEAQWDTQKFASTSVGLVKCLRENSTKLYQLSLLYLPLEEETQNGDSERPLSRSNNNQEPVLWNFKSLANNFNVRFTYHFHATSSSSKIETYFQFLNDYLAENLYKCINIFHDDCNGLTKPVIHEQFINYVLQPIRDKVRSTLFQNDLKTLIVLISQILATDKNLLNSFHYHGLGLVSLISDEVWEKWINYEVEMANRQFINITKNPEDFPKSSQNFVKLINKIYDYLEPFYDLDFDLLVRYKLMTCSLIFMNLTSSYLDYILTVDSLNETRTKEQELYQTMAKLQHVNFVYRKIKSLSSNFIFIQLTDIVNSTESKKYNSLFQNVENDYEKAMSTDMQNSIVHRIQKLLKETLRNYFKISTWSTLEMSVDENIGPSSVPSAELVNSINVLRRLINKLDSMDIPLAISLKVKNELLNVIVNYFTESILKLNKFNQNGLNQFLHDFKSLSSILSLPSHATNYKCMSLHELVKILKLKYDPNNQQFLNPEYIKTGNFTSLKEAYSIKYLKDTKIQDALYRIIYGNIL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.04136947218259629,"disorder_content":0.025677603423680456,"disprot_consensus":{"full":[{"start":217,"end":234,"type":"D"}],"Structural state":[{"start":217,"end":234,"type":"D"}]}},{"disprot_id":"DP03974","acc":"P53847","creator":"zskalman","date":"2023-03-02T11:03:55.681Z","features":{"pfam":[{"id":"PF11988","name":"Retrograde transport protein Dsl1 N terminal","start":6,"end":360},{"id":"PF11989","name":"Retrograde transport protein Dsl1 C terminal","start":560,"end":753}],"gene3D":[]},"genes":[{"name":{"value":"DSL1"},"orfNames":[{"value":"N0842"}],"olnNames":[{"value":"YNL258C"}]}],"length":754,"name":"Protein transport protein DSL1","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":36,"reference_id":"19151722","reference_source":"pmid","reference_html":"Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex. <i> Tripathi A, Ren Y, Jeffrey PD, Hughson FM. </i> Nat Struct Mol Biol, 2009","date":"2023-03-02T11:08:07.485Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3ETU"}],"region_id":"DP03974r001","statement":[{"text":"We were able to produce soluble full-length yeast Dsl1p (residues 1-754), but could not generate diffraction-quality crystals, perhaps because the full-length protein contains a central region (residues 388-467) with an unusual concentration of charged residues28 and an absence of predicted regular secondary structure.","type":"Results"},{"text":"No electron density was discernable for the first 36 residues of Dsl1ΔC, suggesting that the extreme N-terminus, while present, is not crystallographically well ordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-04T16:55:20.335Z"}},{"start":388,"end":467,"reference_id":"19151722","reference_source":"pmid","reference_html":"Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex. <i> Tripathi A, Ren Y, Jeffrey PD, Hughson FM. </i> Nat Struct Mol Biol, 2009","date":"2023-03-02T11:08:39.126Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3ETU"}],"region_id":"DP03974r002","statement":[{"text":"We were able to produce soluble full-length yeast Dsl1p (residues 1-754), but could not generate diffraction-quality crystals, perhaps because the full-length protein contains a central region (residues 388-467) with an unusual concentration of charged residues28 and an absence of predicted regular secondary structure.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-04T16:55:19.190Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MESLFPNKGEIIRELLKDPLILKNDSKRSNGSELELDSSDLLQREAILANELNILDNLKTFLNLIKEVKTNLNILELENCYYSLQSLRKKMRNNAAYLKQSFNFQQSISTYVDTLHLELVSTLYKILTNGFWKITENSIQFTPTVEWGKDKVHIEYDTFMDFVAQQYFPKGSLDNQAWFILDMTSADSQEQVRAKLNTIMKEYMNLSRIVSMIKNSIFISGKEISYENEKNILVFSKSSSHGQHCVSTVLTSFEAVCDFMLDGLAFRDRKTLSYELGPLFNTEFTKFVKNNASIILESLDSPLKNLVSVINNKLTRLVAKSEVTNWTHSGKEIQDLLMNKQLYYNLLLDKVLESHISEIRSIFEDPKKSWQNLEVVELTTSNTNTMSEKIGKNDSDVQNEKELHNAVSKDDDWNWEVEDDDADAWGDEIDVNIDDEEEKTNQEKEKEPEEEENAWDEAWAIDENIDDASLENGKEHLKAHDVGSLDKDHIEVTQLPKLFLAISQNFKSSFADSHVDEQYFAYKYNLLQTSYMAMCTANFSHNWCQLYVDMRYLIERDEKLYRIKELTRNLLETKLNMKYRIVCQLIRHQLTEFRENERNPSWDATIEKLLPYILKEIVRPLQKIRGEEGSRYLLSFLNFLYNDCVTKEILKWQIISEVNSENLGELVSLLVNNTDIQLLAKEPSYKKMREKFATMGKFLPLHLKEIMEMFYNGDFYLFATDELIQWIELLFADTPLRRNAIDDIYEIRGTALDD","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.17108753315649866,"disorder_content":0.15384615384615385,"disprot_consensus":{"full":[{"start":1,"end":36,"type":"D"},{"start":388,"end":467,"type":"D"}],"Structural state":[{"start":1,"end":36,"type":"D"},{"start":388,"end":467,"type":"D"}]}},{"disprot_id":"DP03975","acc":"P14867","creator":"zskalman","date":"2023-03-02T11:26:25.545Z","features":{"pfam":[{"id":"PF02931","name":"Neurotransmitter-gated ion-channel ligand binding domain","start":43,"end":250},{"id":"PF02932","name":"Neurotransmitter-gated ion-channel transmembrane region","start":257,"end":341},{"id":"PF02932","name":"Neurotransmitter-gated ion-channel transmembrane region","start":372,"end":439}],"gene3D":[]},"genes":[{"name":{"value":"GABRA1"}}],"length":456,"name":"Gamma-aminobutyric acid receptor subunit alpha-1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":351,"end":410,"reference_id":"30602789","reference_source":"pmid","reference_html":"Cryo-EM structure of the human α1β3γ2 GABA<sub>A</sub> receptor in a lipid bilayer. <i> Laverty D, Desai R, Uchański T, Masiulis S, Stec WJ, Malinauskas T, Zivanov J, Pardon E, Steyaert J, Miller KW, Aricescu AR. </i> Nature, 2019","date":"2023-04-20T14:08:35.409Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6I53"},{"db":"EMDB","id":"EMD-4411"}],"region_id":"DP03975r001","statement":[{"text":"Beyond this level, the intracellular M3-M4 loops are largely disordered, possibly because interacting post-synaptic proteins were not included.","type":"Abstract"},{"text":"Intracellular domains (ICD), largely disordered in the absence of interacting post-synaptic proteins, could only be partially modelled (Extended Data Fig. 3m, Supplementary Video 2).","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P28472","statements":[{"type":"Introduction","text":"Three-dimensional reconstruction of the α1β3γ2L-Mb38 complex led to a cryo-EM map at 3.2 Å nominal resolution, which allowed model building for the ECD and TMD of all GABAAR subunits, and for the nanobody domain of Mb38 (Fig. 1, Extended Data Fig. 1a and d-g, Extended Data Fig. 3a-l, Supplementary Video 2)."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P18507","statements":[{"type":"Introduction","text":"Three-dimensional reconstruction of the α1β3γ2L-Mb38 complex led to a cryo-EM map at 3.2 Å nominal resolution, which allowed model building for the ECD and TMD of all GABAAR subunits, and for the nanobody domain of Mb38 (Fig. 1, Extended Data Fig. 1a and d-g, Extended Data Fig. 3a-l, Supplementary Video 2)."}]},{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ABCD","id":"AW309","statements":[{"type":"Introduction","text":"Three-dimensional reconstruction of the α1β3γ2L-Mb38 complex led to a cryo-EM map at 3.2 Å nominal resolution, which allowed model building for the ECD and TMD of all GABAAR subunits, and for the nanobody domain of Mb38 (Fig. 1, Extended Data Fig. 1a and d-g, Extended Data Fig. 3a-l, Supplementary Video 2)."},{"type":"Supplementary material","text":"The alpa1beta3gamma2L structure was solved in the presence of the Mb38 megabody, essential to circumvent preferential orientation in ice (Extended Data Figs. 1c, 5a, and 5b). Like nanobody Nb387, Mb38 is a positive allosteric modulator of GABA-induced currents (Extended Data Fig. 5c), with an EC50 of 2 ± 1 μM, (n = 3 - 5 cells at each concentration). Mb38 binds at the alpha+/beta– interface, predominantly to the alpha1 subunit (buried surface area 846 Å2, versus 241 Å2 buried through beta3 subunit contacts)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:10908846"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:9543520"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T15:53:08.693Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MRKSPGLSDCLWAWILLLSTLTGRSYGQPSLQDELKDNTTVFTRILDRLLDGYDNRLRPGLGERVTEVKTDIFVTSFGPVSDHDMEYTIDVFFRQSWKDERLKFKGPMTVLRLNNLMASKIWTPDTFFHNGKKSVAHNMTMPNKLLRITEDGTLLYTMRLTVRAECPMHLEDFPMDAHACPLKFGSYAYTRAEVVYEWTREPARSVVVAEDGSRLNQYDLLGQTVDSGIVQSSTGEYVVMTTHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRGYAWDGKSVVPEKPKKVKDPLIKKNNTYAPTATSYTPNLARGDPGLATIAKSATIEPKEVKPETKPPEPKKTFNSVSKIDRLSRIAFPLLFGIFNLVYWATYLNREPQLKAPTPHQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.16228070175438597,"disorder_content":0.13157894736842105,"disprot_consensus":{"full":[{"start":351,"end":410,"type":"D"}],"Structural state":[{"start":351,"end":410,"type":"D"}]}},{"disprot_id":"DP03976","acc":"P28472","creator":"zskalman","date":"2023-03-02T11:33:07.693Z","features":{"pfam":[{"id":"PF02931","name":"Neurotransmitter-gated ion-channel ligand binding domain","start":39,"end":242},{"id":"PF02932","name":"Neurotransmitter-gated ion-channel transmembrane region","start":250,"end":468}],"gene3D":[]},"genes":[{"name":{"value":"GABRB3"}}],"length":473,"name":"Gamma-aminobutyric acid receptor subunit beta-3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":338,"end":439,"reference_id":"30602789","reference_source":"pmid","reference_html":"Cryo-EM structure of the human α1β3γ2 GABA<sub>A</sub> receptor in a lipid bilayer. <i> Laverty D, Desai R, Uchański T, Masiulis S, Stec WJ, Malinauskas T, Zivanov J, Pardon E, Steyaert J, Miller KW, Aricescu AR. </i> Nature, 2019","date":"2023-04-20T14:07:39.254Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6I53"},{"db":"EMDB","id":"EMD-4411"}],"region_id":"DP03976r001","statement":[{"text":"Beyond this level, the intracellular M3-M4 loops are largely disordered, possibly because interacting post-synaptic proteins were not included.","type":"Abstract"},{"text":"Intracellular domains (ICD), largely disordered in the absence of interacting post-synaptic proteins, could only be partially modelled (Extended Data Fig. 3m, Supplementary Video 2).","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P14867","statements":[{"type":"Introduction","text":"Three-dimensional reconstruction of the α1β3γ2L-Mb38 complex led to a cryo-EM map at 3.2 Å nominal resolution, which allowed model building for the ECD and TMD of all GABAAR subunits, and for the nanobody domain of Mb38 (Fig. 1, Extended Data Fig. 1a and d-g, Extended Data Fig. 3a-l, Supplementary Video 2)."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P18507","statements":[{"type":"Introduction","text":"Three-dimensional reconstruction of the α1β3γ2L-Mb38 complex led to a cryo-EM map at 3.2 Å nominal resolution, which allowed model building for the ECD and TMD of all GABAAR subunits, and for the nanobody domain of Mb38 (Fig. 1, Extended Data Fig. 1a and d-g, Extended Data Fig. 3a-l, Supplementary Video 2)."}]},{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ABCD","id":"AW309","statements":[{"type":"Introduction","text":"\nThree-dimensional reconstruction of the α1β3γ2L-Mb38 complex led to a cryo-EM map at 3.2 Å nominal resolution, which allowed model building for the ECD and TMD of all GABAAR subunits, and for the nanobody domain of Mb38 (Fig. 1, Extended Data Fig. 1a and d-g, Extended Data Fig. 3a-l, Supplementary Video 2).\n"},{"type":"Supplementary material","text":"The alpha1beta3gamma2L structure was solved in the presence of the Mb38 megabody, essential to circumvent preferential orientation in ice (Extended Data Figs. 1c, 5a, and 5b). Like nanobody Nb387, Mb38 is a positive allosteric modulator of GABA-induced currents (Extended Data Fig. 5c), with an EC50 of 2 ± 1 μM, (n = 3 - 5 cells at each concentration). Mb38 binds at the alpha+/beta– interface, predominantly to the alpha1 subunit (buried surface area 846 Å2, versus 241 Å2 buried through beta3 subunit contacts)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:10908846"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:9543520"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T15:54:15.156Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MWGLAGGRLFGIFSAPVLVAVVCCAQSVNDPGNMSFVKETVDKLLKGYDIRLRPDFGGPPVCVGMNIDIASIDMVSEVNMDYTLTMYFQQYWRDKRLAYSGIPLNLTLDNRVADQLWVPDTYFLNDKKSFVHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWRGGDKAVTGVERIELPQFSIVEHRLVSRNVVFATGAYPRLSLSFRLKRNIGYFILQTYMPSILITILSWVSFWINYDASAARVALGITTVLTMTTINTHLRETLPKIPYVKAIDMYLMGCFVFVFLALLEYAFVNYIFFGRGPQRQKKLAEKTAKAKNDRSKSESNRVDAHGNILLTSLEVHNEMNEVSGGIGDTRNSAISFDNSGIQYRKQSMPREGHGRFLGDRSLPHKKTHLRRRSSQLKIKIPDLTDVNAIDRWSRIVFPFTFSLFNLVYWLYYVN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.1839323467230444,"disorder_content":0.2156448202959831,"disprot_consensus":{"full":[{"start":338,"end":439,"type":"D"}],"Structural state":[{"start":338,"end":439,"type":"D"}]}},{"disprot_id":"DP03977","acc":"P18507","creator":"zskalman","date":"2023-03-02T11:38:49.023Z","features":{"pfam":[{"id":"PF02931","name":"Neurotransmitter-gated ion-channel ligand binding domain","start":69,"end":272},{"id":"PF02932","name":"Neurotransmitter-gated ion-channel transmembrane region","start":279,"end":469}],"gene3D":[]},"genes":[{"name":{"value":"GABRG2"}}],"length":475,"name":"Gamma-aminobutyric acid receptor subunit gamma-2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":363,"end":444,"reference_id":"30602789","reference_source":"pmid","reference_html":"Cryo-EM structure of the human α1β3γ2 GABA<sub>A</sub> receptor in a lipid bilayer. <i> Laverty D, Desai R, Uchański T, Masiulis S, Stec WJ, Malinauskas T, Zivanov J, Pardon E, Steyaert J, Miller KW, Aricescu AR. </i> Nature, 2019","date":"2023-04-20T14:06:56.259Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6I53"},{"db":"EMDB","id":"EMD-4411"}],"region_id":"DP03977r001","statement":[{"text":"Beyond this level, the intracellular M3-M4 loops are largely disordered, possibly because interacting post-synaptic proteins were not included.","type":"Abstract"},{"text":"Intracellular domains (ICD), largely disordered in the absence of interacting post-synaptic proteins, could only be partially modelled (Extended Data Fig. 3m, Supplementary Video 2).","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P28472","statements":[{"type":"Introduction","text":"Three-dimensional reconstruction of the α1β3γ2L-Mb38 complex led to a cryo-EM map at 3.2 Å nominal resolution, which allowed model building for the ECD and TMD of all GABAAR subunits, and for the nanobody domain of Mb38 (Fig. 1, Extended Data Fig. 1a and d-g, Extended Data Fig. 3a-l, Supplementary Video 2)."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P14867","statements":[{"type":"Introduction","text":"Three-dimensional reconstruction of the α1β3γ2L-Mb38 complex led to a cryo-EM map at 3.2 Å nominal resolution, which allowed model building for the ECD and TMD of all GABAAR subunits, and for the nanobody domain of Mb38 (Fig. 1, Extended Data Fig. 1a and d-g, Extended Data Fig. 3a-l, Supplementary Video 2)."}]},{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ABCD","id":"AW309","statements":[{"type":"Introduction","text":"Three-dimensional reconstruction of the α1β3γ2L-Mb38 complex led to a cryo-EM map at 3.2 Å nominal resolution, which allowed model building for the ECD and TMD of all GABAAR subunits, and for the nanobody domain of Mb38 (Fig. 1, Extended Data Fig. 1a and d-g, Extended Data Fig. 3a-l, Supplementary Video 2)."},{"type":"Supplementary material","text":"The alpha1beta3gamma2L structure was solved in the presence of the Mb38 megabody, essential to circumvent preferential orientation in ice (Extended Data Figs. 1c, 5a, and 5b). Like nanobody Nb387, Mb38 is a positive allosteric modulator of GABA-induced currents (Extended Data Fig. 5c), with an EC50 of 2 ± 1 μM, (n = 3 - 5 cells at each concentration). Mb38 binds at the alpha+/beta– interface, predominantly to the alpha1 subunit (buried surface area 846 Å2, versus 241 Å2 buried through beta3 subunit contacts)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:10908846"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:9543520"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T15:54:30.119Z"}},{"start":1,"end":65,"reference_id":"30602789","reference_source":"pmid","reference_html":"Cryo-EM structure of the human α1β3γ2 GABA<sub>A</sub> receptor in a lipid bilayer. <i> Laverty D, Desai R, Uchański T, Masiulis S, Stec WJ, Malinauskas T, Zivanov J, Pardon E, Steyaert J, Miller KW, Aricescu AR. </i> Nature, 2019","date":"2024-06-27T16:21:33.091Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"6I53"}],"region_id":"DP03977r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P28472"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P14867"},{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ABCD","id":"AW309"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"10908846"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"9543520"}],"statement":[{"text":"This region lacks electron density in the the CRYO EM structure, indicating it is disordered.","type":"Curator statement"}]}],"regions_counter":2,"released":"2023_06","sequence":"MSSPNIWSTGSSVYSTPVFSQKMTVWILLLLSLYPGFTSQKSDDDYEDYASNKTWVLTPKVPEGDVTVILNNLLEGYDNKLRPDIGVKPTLIHTDMYVNSIGPVNAINMEYTIDIFFAQTWYDRRLKFNSTIKVLRLNSNMVGKIWIPDTFFRNSKKADAHWITTPNRMLRIWNDGRVLYTLRLTIDAECQLQLHNFPMDEHSCPLEFSSYGYPREEIVYQWKRSSVEVGDTRSWRLYQFSFVGLRNTTEVVKTTSGDYVVMSVYFDLSRRMGYFTIQTYIPCTLIVVLSWVSFWINKDAVPARTSLGITTVLTMTTLSTIARKSLPKVSYVTAMDLFVSVCFIFVFSALVEYGTLHYFVSNRKPSKDKDKKKKNPLLRMFSFKAPTIDIRPRSATIQMNNATHLQERDEEYGYECLDGKDCASFFCCFEDCRTGAWRHGRIHIRIAKMDSYARIFFPTAFCLFNLVYWVSYLYL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.25267665952890794,"disorder_content":0.3094736842105263,"disprot_consensus":{"full":[{"start":1,"end":65,"type":"D"},{"start":363,"end":444,"type":"D"}],"Structural state":[{"start":1,"end":65,"type":"D"},{"start":363,"end":444,"type":"D"}]}},{"disprot_id":"DP03978","acc":"P19658","creator":"zskalman","date":"2023-03-02T13:50:17.747Z","features":{"pfam":[{"id":"PF03081","name":"Exo70 exocyst complex subunit C-terminal","start":237,"end":620},{"id":"PF20669","name":"Exocyst complex component Exo70 N-terminal","start":67,"end":155}],"gene3D":[]},"genes":[{"name":{"value":"EXO70"},"orfNames":[{"value":"J0932"}],"olnNames":[{"value":"YJL085W"}]}],"length":623,"name":"Exocyst complex component EXO70","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":222,"end":233,"reference_id":"16249794","reference_source":"pmid","reference_html":"The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif. <i> Dong G, Hutagalung AH, Fu C, Novick P, Reinisch KM. </i> Nat Struct Mol Biol, 2005","date":"2023-04-26T11:41:56.312Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2B1E"}],"region_id":"DP03978r001","statement":[{"text":"The refined structure consists of residues 67–623 (with the exception of residues in disordered regions 117–120, 222–233, 296–300 and 415–418) and 261 water molecules.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T12:16:40.447Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MPAEIDIDEADVLVLSQELQKTSKLTFEINKSLKKIAATSNQSSQLFTPILARNNVLTTLQRNIESTLNSVASVKDLANEASKYEIILQKGINQVGLKQYTQVVHKLDDMLEDIQSGQANREENSEFHGILTHLEQLIKRSEAQLRVYFISILNSIKPFDPQINITKKMPFPYYEDQQLGALSWILDYFHGNSEGSIIQDILVGERSKLILKCMAFLEPFAKEISTAKNAPYEKGSSGMNSYTEALLGFIANEKSLVDDLYSQYTESKPHVLSQILSPLISAYAKLFGANLKIVRSNLENFGFFSFELVESINDVKKSLRGKELQNYNLLQDCTQEVRQVTQSLFRDAIDRIIKKANSISTIPSNNGVTEATVDTMSRLRKFSEYKNGCLGAMDNITRENWLPSNYKEKEYTLQNEALNWEDHNVLLSCFISDCIDTLAVNLERKAQIALMPNQEPDVANPNSSKNKHKQRIGFFILMNLTLVEQIVEKSELNLMLAGEGHSRLERLKKRYISYMVSDWRDLTANLMDSVFIDSSGKKSKDKEQIKEKFRKFNEGFEDLVSKTKQYKLSDPSLKVTLKSEIISLVMPMYERFYSRYKDSFKNPRKHIKYTPDELTTVLNQLVR","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.014446227929373997,"disorder_content":0.019261637239165328,"disprot_consensus":{"full":[{"start":222,"end":233,"type":"D"}],"Structural state":[{"start":222,"end":233,"type":"D"}]}},{"disprot_id":"DP03979","acc":"F2SDI0","creator":"eficho","date":"2023-03-03T08:49:47.767Z","features":{"pfam":[{"id":"PF28334","name":"pH-response transcription factor pacC/RIM101 helical domain","start":491,"end":691}],"gene3D":[]},"genes":[{"orfNames":[{"value":"TERG_00838","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EGD84560.1","url":"https://www.ebi.ac.uk/ena/browser/view/EGD84560.1"}}]}]}],"length":815,"name":"pH-response transcription factor pacC/RIM101","ncbi_taxon_id":559305,"organism":"Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892)","regions":[{"start":585,"end":815,"reference_id":"36643486","reference_source":"pmid","reference_html":"Biophysical Characterization of the C-Terminal Tail of <i>T. rubrum</i> PacC Reveals an Inherent Intrinsically Disordered Structure with pH-Induced Structural Plasticity. <i> Dey SS, Chakraborty R, Taneja B. </i> ACS Omega, 2023","date":"2023-05-19T14:24:50.797Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03979r001","statement":[{"text":"However, PacCΔ1−584, with a predicted Mw of 24.7 kDa, exhibited an anomalous migration on SDS-PAGE of ∼35 kDa, possibly due to the enrichment of charged residues in these proteins, as also observed in many IDPs.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T09:57:24.570Z"}},{"start":585,"end":815,"reference_id":"36643486","reference_source":"pmid","reference_html":"Biophysical Characterization of the C-Terminal Tail of <i>T. rubrum</i> PacC Reveals an Inherent Intrinsically Disordered Structure with pH-Induced Structural Plasticity. <i> Dey SS, Chakraborty R, Taneja B. </i> ACS Omega, 2023","date":"2023-05-19T14:28:09.719Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03979r002","statement":[{"text":"Size-exclusion chromatography (SEC) of PacCΔ1−584 was next performed to estimate its hydrodynamic properties. Again, although the protein eluted as one major peak over the Superdex 200 10/300 GL column, the apparent Mw was found to be ∼five-fold higher than that of the monomer, that is, 126 ± 0.88 kDa (Figure 3A). A nearly four- to six-fold increase in their apparent Mw is often seen for IDPs\nhaving an extended random coil conformation, suggesting a possible similar conformation for PacCΔ1−584 as well.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T09:57:09.963Z"}},{"start":585,"end":815,"reference_id":"36643486","reference_source":"pmid","reference_html":"Biophysical Characterization of the C-Terminal Tail of <i>T. rubrum</i> PacC Reveals an Inherent Intrinsically Disordered Structure with pH-Induced Structural Plasticity. <i> Dey SS, Chakraborty R, Taneja B. </i> ACS Omega, 2023","date":"2023-05-19T14:29:04.283Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03979r003","statement":[{"text":"In order to monitor the secondary structure of PacCΔ1−584, far-UV CD spectrum was recorded at alkaline ambient pH 8.0 (Figure 4A). The CD spectrum shows a negative peak at 200 nm, similar to the spectrum shown by intrinsically disordered proteins.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T09:56:31.806Z"}},{"start":585,"end":815,"reference_id":"36643486","reference_source":"pmid","reference_html":"Biophysical Characterization of the C-Terminal Tail of <i>T. rubrum</i> PacC Reveals an Inherent Intrinsically Disordered Structure with pH-Induced Structural Plasticity. <i> Dey SS, Chakraborty R, Taneja B. </i> ACS Omega, 2023","date":"2023-05-19T14:30:21.714Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006336","ec_ontology":"ECO","ec_name":"intrinsic fluorescence-based protein conformation evidence","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03979r004","statement":[{"text":"The intrinsic fluorescence spectrum of PacCΔ1−584 is suggestive of a fully exposed environment for tryptophan between pH 2 and 12, with λmax of 355−357 nm\n(Figure S2), limiting the estimation of thermodynamic parameters to far-UV CD measurements.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T09:55:33.606Z"}}],"regions_counter":4,"released":"2024_06","sequence":"MSSTQDQDHSALAQHQQQHPPSQHQQQSQQQQHQHQQAAAGSQSEQTQAQAQQPRSQMQSAPSLQQQPPQQQQPQQQGQQGQQGQQQQPTSQTVQSVPVQASLQHAAAAAAAVAPPGVQQVAPSSPNAPGSLECQWQGCQELCPTPEALYEHVCERHVGRKSTNNLNLTCGWSNCRTTTVKRDHITSHIRVHVPLKPHKCDFCGKAFKRPQDLKKHVKTHADDSVLMRSPEPGAGQRQQPPTGMFGVGLGPDGKPAHFFEGSLGPVPQAYGHPPPQYYQPQPPQQQPNPSYGNVYYAVGHDAAHQASYESKKRGYDALNEFFGDLKRRQFDPTSYAAVGQRLLNLHGLPLPLTHAGAVPEYQPMPAMVSVGGGHSGYQSAGPIPTQSYHLPPMGNLRTKADLMNIDQFLEQMQSTVYESDENVAAAGVAQPGAHYVQGPLSYRTTNSPPTHHQSHHHHPHATATTATTTTAATTASMISTPAAATPASSVSAASRSPHASTPALTPPSSAQSYTSGRSPISLASSHGMSPSHHPSTAGMYPTLPATTGQDSLSSSGYPTTVSSAAPPSTLSSIFDDDRRRYTGGMLQRSRPDIDLSTPSIKRDADAAAAAAAKDEPKLSSSVIDPALSRASADMDEDAAPRRSPSSTPTPTATTAAAAGPDDRQPVGEQQWVENVRLLQRLRDYVLERLNNGDYVDEDKQEDSDKEEDAKTDKASPGSASASDAATRAGEYPSIKMHGMEAIAAAAVAHEEGRDSQMPRDDEDQESPSTPTARSTTTMLDAEEEAKQAGENLYPVLKMAVDDDGADTDGDEKMGQ","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Eurotiomycetes","Eurotiomycetidae","Onygenales","Arthrodermataceae","Trichophyton"],"alphafold_very_low_content":0.6993865030674846,"disorder_content":0.28343558282208586,"disprot_consensus":{"full":[{"start":585,"end":815,"type":"D"}],"Structural state":[{"start":585,"end":815,"type":"D"}]}},{"disprot_id":"DP03980","acc":"Q80U30-3","creator":"eficho","date":"2023-03-03T09:59:31.317Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"Clec16a","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:1921624","url":"http://www.informatics.jax.org/marker/MGI:1921624"}}]},"synonyms":[{"value":"Kiaa0350"}]}],"length":912,"name":"Isoform 3 of Protein CLEC16A","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":347,"end":472,"reference_id":"36822331","reference_source":"pmid","reference_html":"Reciprocal regulatory balance within the CLEC16A-RNF41 mitophagy complex depends on an intrinsically disordered protein region. <i> Gingerich MA, Zhu J, Chai B, Vincent MP, Xie N, Sidarala V, Kotov NA, Sahu D, Klionsky DJ, Schnell S, Soleimanpour SA. </i> J Biol Chem, 2023","date":"2023-05-19T14:34:57.053Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03980r001","statement":[{"text":"IDPRs characteristically demonstrate slow migration in SDS-polyacrylamide gels due to their expanded nature and greater number of charged residues which leads to weak binding to SDS (26, 43). Full-length WT CLEC16A and the CLEC16A ΔIDPR mutant migrated at their expected molecular mass (Fig. 6A). However, the internal CLEC16A putative IDPR alone (AA 347–472) migrated a shorter distance than what is expected, visualized as a band 1.6-times greater than the expected size, consistent with an IDPR (Fig. 6A).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T10:02:02.167Z"}},{"start":347,"end":472,"reference_id":"36822331","reference_source":"pmid","reference_html":"Reciprocal regulatory balance within the CLEC16A-RNF41 mitophagy complex depends on an intrinsically disordered protein region. <i> Gingerich MA, Zhu J, Chai B, Vincent MP, Xie N, Sidarala V, Kotov NA, Sahu D, Klionsky DJ, Schnell S, Soleimanpour SA. </i> J Biol Chem, 2023","date":"2023-05-19T14:36:05.487Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03980r002","statement":[{"text":"Notably, the heteronuclear single quantum coherence-NMR spectra of the CLEC16A putative internal IDPR was tightly clustered near 8 ppm, supporting the hypothesis that CLEC16A contains an internal IDPR (Fig. 6B).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T10:01:24.837Z"}},{"start":347,"end":472,"reference_id":"36822331","reference_source":"pmid","reference_html":"Reciprocal regulatory balance within the CLEC16A-RNF41 mitophagy complex depends on an intrinsically disordered protein region. <i> Gingerich MA, Zhu J, Chai B, Vincent MP, Xie N, Sidarala V, Kotov NA, Sahu D, Klionsky DJ, Schnell S, Soleimanpour SA. </i> J Biol Chem, 2023","date":"2023-05-19T14:36:58.964Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03980r003","statement":[{"text":"Conversely, the CD spectra of the putative internal CLEC16A IDPR had a single minimum near 200 nm, in line with lack of secondary structure (Fig. 6D).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T09:59:30.324Z"}},{"start":347,"end":472,"reference_id":"36822331","reference_source":"pmid","reference_html":"Reciprocal regulatory balance within the CLEC16A-RNF41 mitophagy complex depends on an intrinsically disordered protein region. <i> Gingerich MA, Zhu J, Chai B, Vincent MP, Xie N, Sidarala V, Kotov NA, Sahu D, Klionsky DJ, Schnell S, Soleimanpour SA. </i> J Biol Chem, 2023","date":"2023-05-19T14:38:20.652Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006301","ec_ontology":"ECO","ec_name":"protein thermal shift assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03980r004","statement":[{"text":"Further, while heating full-length CLEC16A irreversibly disrupted its alpha-helical secondary structure, heating the internal CLEC16A fragment did not substantially change its spectral features (Fig. 6, C and D). This result confirmed that the internal CLEC16A fragment lacks secondary structure and is indeed an IDPR (Fig. 6, C and D). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T09:59:05.689Z"}},{"start":347,"end":472,"reference_id":"36822331","reference_source":"pmid","reference_html":"Reciprocal regulatory balance within the CLEC16A-RNF41 mitophagy complex depends on an intrinsically disordered protein region. <i> Gingerich MA, Zhu J, Chai B, Vincent MP, Xie N, Sidarala V, Kotov NA, Sahu D, Klionsky DJ, Schnell S, Soleimanpour SA. </i> J Biol Chem, 2023","date":"2023-05-19T14:53:58.858Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005644","ec_ontology":"ECO","ec_name":"immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q8BH75","operator":null,"partner_start":1,"partner_end":317}],"region_id":"DP03980r005","statement":[{"text":"We find that the internal IDPR of CLEC16A is crucial for its degradation. CLEC16A turnover was promoted by RNF41, which binds and acts upon the internal IDPR to destabilize CLEC16A.","type":"Abstract"},{"text":"Truncating the CLEC16A internal IDPR, or shuffling its residues, reduced CLEC16A binding and ubiquitination of RNF41 compared to WT CLEC16A, following overexpression of the similar protein levels of CLEC16A (Fig. 5A). Mutating the CLEC16A internal IDPR also impaired assembly of the tripartite mitophagy complex, as we found reduced binding between CLEC16A and RNF41 as well as RNF41 and USP8 (Fig. 5B).","type":"Results"},{"text":"Indeed, overexpression of the CLEC16A internal IDPR fragment alone (AA 347–472; IDPR1 only) was sufficient to bind RNF41 (Fig. 5C).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T10:47:39.211Z"}},{"start":347,"end":472,"reference_id":"36822331","reference_source":"pmid","reference_html":"Reciprocal regulatory balance within the CLEC16A-RNF41 mitophagy complex depends on an intrinsically disordered protein region. <i> Gingerich MA, Zhu J, Chai B, Vincent MP, Xie N, Sidarala V, Kotov NA, Sahu D, Klionsky DJ, Schnell S, Soleimanpour SA. </i> J Biol Chem, 2023","date":"2023-06-16T15:40:06.281Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0032434","term_name":"regulation of proteasomal ubiquitin-dependent protein catabolic process","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005644","ec_ontology":"ECO","ec_name":"immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","region_id":"DP03980r006","statement":[{"text":"We found that the CLEC16A internal IDPR contains an enrichment of lysine residues that are predicted to be ubiquitinated with high confidence (Fig. 2D). We therefore generated a CLEC16A mutant construct insensitive to ubiquitination with lysine-to-arginine mutagenesis of the internal IDPR (IDPR K-to-R), which is a substitution strategy that retains a similar residue structure and charge. The CLEC16A IDPR K-to-R mutant had increased protein levels and was significantly more stable than WT CLEC16A and achieved similar levels and stability to CLEC16A mutants bearing a shuffled or truncated internal IDPR (Fig. 2, E and F).","type":"Results"},{"text":"Interestingly, the CLEC16A mutant lacking the internal IDPR maintained higher protein levels and was more stable than WT CLEC16A, indicating that the internal IDPR destabilized CLEC16A (Fig. 2C).","type":"Results"},{"text":"While overexpressing RNF41 led to reduced levels of WT CLEC16A as expected, shuffling or truncating the internal IDPR prevented RNF41 from reducing CLEC16A protein levels (Fig. 4D). Further, overexpression of a dominant negative RNF41 lacking its RING domain (dnRNF41) to inhibit RNF41 action led to an elevation in the levels of WT CLEC16A, but this did not occur following truncation of the internal IDPR (Fig. 4E). These results suggest that RNF41 acts upon the CLEC16A internal IDPR to destabilize CLEC16A and that this action depends upon the CLEC16A IDPR amino acid sequence order.","type":"Results"},{"text":"Moreover, RNF41 also did not reduce levels of the ubiquitination-resistant CLEC16A\ninternal IDPR mutant (IDPR K-to-R), suggesting that CLEC16A internal IDPR lysine residues are vital for RNF41 to destabilize CLEC16A (Fig. 4D).","type":"Results"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"Q8BH75","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-16T19:27:06.252Z"}},{"start":347,"end":472,"reference_id":"36822331","reference_source":"pmid","reference_html":"Reciprocal regulatory balance within the CLEC16A-RNF41 mitophagy complex depends on an intrinsically disordered protein region. <i> Gingerich MA, Zhu J, Chai B, Vincent MP, Xie N, Sidarala V, Kotov NA, Sahu D, Klionsky DJ, Schnell S, Soleimanpour SA. </i> J Biol Chem, 2023","date":"2023-06-14T10:10:28.113Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031648","term_name":"protein destabilization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Phe347-Asn472del","start":null,"end":null,"position":null},{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"ec_go":"IMP","region_id":"DP03980r007","statement":[{"text":"Interestingly, the CLEC16A mutant lacking the internal IDPR maintained higher protein levels and was more stable than WT CLEC16A, indicating that the internal IDPR destabilized CLEC16A (Fig. 2C).","type":"Results"}],"term_comment":"","term_def":"\"Any process that decreases the stability of a protein, making it more vulnerable to degradative processes or aggregation.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":7,"released":"2024_06","sequence":"MFGRSRSWVGGGHSKSSRNIHSLDHLKYLYHVLTKNTTVTEQNRNLLVETIRSITEILIWGDQNDSSVFDFFLEKNMFVFFLNILRQKSGRYVCVQLLQTLNILFENISHETSLYYLLSNNYVNSIIVHKFDFSDEEIMAYYISFLKTLSLKLNNHTVHFFYNEHTNDFALYTEAIKFFNHPESMVRIAVRTITLNVYKVDNQAMLHYIRDKTAVPYFSNLVWFIGSHVIELDNCVQTDEEHRNRGKLSDLVAEHLDHLHYLNDILIINCEFLNDVLTDHLLNRLFLPLYVYSLENPDKGGERPKISLPVSLYLLSQVFLIIHHAPLVNSLAEVILNGDLSETYTKPAQDVPRSSAKPSIRCFIKPTETLERSLEMNKHKGKKRMQKRPNYKNVGEEEDEERGSAEDAQEDAEKTKGTEGGSKSMKTSGEREEIEMVIMKLGKLSEVAAAGTSVQEQNTTDEEKSAATNSENAQWSRPFLDMVYHALDSPDDDYHALFVLCLLYAMSHNKGMDPEKLKRIQLPVPSEAEKTTYNHLLAERLIRIMNNAAQPDGRIRLATLELSCLLLKQQVLTSSGCVIKDVHLACLEGAREESVHLVRHFYKGEEIFLDMFEDEYRSMTIKPMNVEYLMMDASILLPPTGTPLTGIDFVKRLPCGDVEKTRRAIRVFFMLRSLSLQLRGEPETQLPLTREEDLIKTDDVLDLNNSDLIACTVITKDGGMVQRFLAVDIYQMSLVEPDVSRLGWGVVKFAGLLQDMQVTGVEDDSRALNITIHKPASSPHSKPFPILQATFVFSDHIRCIIAKQRLAKGRIQARRMKMQRIAALLDLPIQPTTEVLGFGLCSSSSSSQHLPFRFYEQCRRGSSDPTVQRSVFASVDKVPGKPHLLLGTQAAFLLSPLEAFLSESRLLAALAS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"disorder_content":0.13815789473684212,"disprot_consensus":{"full":[{"start":347,"end":472,"type":"D"}],"Structural state":[{"start":347,"end":472,"type":"D"}],"Molecular function":[{"start":347,"end":472,"type":"F"}],"Biological process":[{"start":347,"end":472,"type":"F"}]}},{"disprot_id":"DP03982","acc":"Q7Y1A0","creator":"eficho","date":"2023-03-03T10:03:15.166Z","features":{"pfam":[],"gene3D":[]},"genes":[],"length":210,"name":"25 kDa protein dehydrin","ncbi_taxon_id":52705,"organism":"Solanum sogarandinum","regions":[{"start":1,"end":210,"reference_id":"36512982","reference_source":"pmid","reference_html":"The cationic nature of lysine-rich segments modulates the structural and biochemical properties of wild potato FSK<sub>3</sub> dehydrin. <i> Szabała BM. </i> Plant Physiol Biochem, 2023","date":"2023-05-19T15:04:26.401Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03982r001","statement":[{"text":"In aqueous buffers, the spectrum of the proteins in the far-UV region (190–250 nm) exhibited a strong negative band at ~199 nm, and weak negative ellipticity at 222 nm, which indicated that the proteins were predominantly in a random coil conformation, lacking a well-defined secondary structure (Fig. 5A–D).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T11:01:44.224Z"}},{"start":1,"end":210,"reference_id":"36512982","reference_source":"pmid","reference_html":"The cationic nature of lysine-rich segments modulates the structural and biochemical properties of wild potato FSK<sub>3</sub> dehydrin. <i> Szabała BM. </i> Plant Physiol Biochem, 2023","date":"2023-05-19T15:07:09.526Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03982r002","statement":[{"text":"Since a large number of unfolded proteins undergo induced folding upon interactions with their binding partner, the intrinsic propensity of the analyzed proteins to adopt α-helical structures was examined in the presence of negatively charged SDS micelles that have previously been used to model the lipoprotein environment (Rozek et al., 1995, Tulumello and Deber, 2009). Upon incubation with SDS, DHN24 exhibited a pronounced increase in its helical content (Fig. 5A). The negative band shifted from 199 to 204 nm. The CD spectra also contained a stronger negative shoulder at 208–222 nm and positive bands at 190–192 nm, which were characteristics of α-helical structures.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T11:02:19.183Z"}},{"start":1,"end":210,"reference_id":"36512982","reference_source":"pmid","reference_html":"The cationic nature of lysine-rich segments modulates the structural and biochemical properties of wild potato FSK<sub>3</sub> dehydrin. <i> Szabała BM. </i> Plant Physiol Biochem, 2023","date":"2023-05-19T15:15:55.913Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0005543","term_name":"phospholipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IEP","region_id":"DP03982r003","statement":[{"text":"Since dehydrins can bind to acidic phospholipids (Kovacs et al., 2008; Koag et al., 2009; Clarke et al., 2015), it was examined whether the cationic nature of the lysine-rich segments of DHN24 could modulate potential interactions with negatively charged phospholipids. Before the examination, immunoblot analysis was performed using polyclonal anti-DHN24 antibodies to assess the quality of the detected signal of recombinant DHN24 and its mutant variants: dM1, dsM2, and dsM3. The antibodies detected all the proteins with similar affinity (Fig. 7A). Mutant proteins exhibited a slower migration in SDS-PAGE than DHN24 which may be due to the lower content of lysine residues, possibly reducing association with negatively charged SDS","type":"Results"}],"term_comment":"","term_def":"\"Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester.\" [ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T11:06:41.164Z"}},{"start":1,"end":210,"reference_id":"36512982","reference_source":"pmid","reference_html":"The cationic nature of lysine-rich segments modulates the structural and biochemical properties of wild potato FSK<sub>3</sub> dehydrin. <i> Szabała BM. </i> Plant Physiol Biochem, 2023","date":"2023-05-19T15:17:23.872Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0005543","term_name":"phospholipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007122","ec_ontology":"ECO","ec_name":"in vitro assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP03982r004","statement":[{"text":"After the experiments, lipid-protein interaction assays were performed. Anionic PA was immobilized on a nitrocellulose membrane along with neutral phospholipid LPC since zwitterionic lipids are less attracted to dehydrins (Koag et al., 2009; Clarke et al., 2015). DHN24 and dM1 were found to bind to PA upon incubation, but binding to LPC was very weak (Fig. 7B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester.\" [ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T11:06:32.053Z"}}],"regions_counter":4,"released":"2024_06","sequence":"MADQYEQNKPSVEETVGANVEATDRGLFDFIGKKEEEKPSHAHEEEAISSEFCEKVKVSEEEEHKEKEKKEEKKLHRSSSSSSSSSDEEEEIGEDGQIIKKKKKKGLKEKIKEKISGDHKEEVKTEDTSVPVEKYEETEEKKGFLEKIKEKLPGGGHKKTEEVAAPPPPPPAAVDHEAEGKEKKGFLDKIKEKLPGYHSKTEEEKEKEKD","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","lamiids","Solanales","Solanaceae","Solanoideae","Solaneae","Solanum"],"alphafold_very_low_content":0.4238095238095238,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":210,"type":"T"}],"Structural state":[{"start":1,"end":210,"type":"D"}],"Structural transition":[{"start":1,"end":210,"type":"T"}],"Molecular function":[{"start":1,"end":210,"type":"F"}]}},{"disprot_id":"DP03984","acc":"Q9Z4N3","creator":"eficho","date":"2023-03-03T10:05:56.266Z","features":{"pfam":[{"id":"PF27346","name":"Probable copper-binding protein PcoE","start":3,"end":139}],"gene3D":[]},"genes":[{"name":{"value":"silE"}}],"length":143,"name":"Silver-binding protein SilE","ncbi_taxon_id":90371,"organism":"Salmonella typhimurium","regions":[{"start":21,"end":143,"reference_id":"36617868","reference_source":"pmid","reference_html":"Structural and dynamical insights into SilE silver binding from combined analytical probes. <i> Monneau Y, Arrault C, Duroux C, Martin M, Chirot F, Mac Aleese L, Girod M, Comby-Zerbino C, Hagège A, Walker O, Hologne M. </i> Phys Chem Chem Phys, 2023","date":"2023-09-06T15:22:42.478Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03984r001","statement":[{"text":"Resonances are dispersed in a narrow spectral range from 8 to 8.7 ppm, which is the hallmark of an intrinsically disordered protein.14 The observed chemical shifts result from the average of a conformational ensemble the protein may adopt if the exchange time scale is much faster than the chemical shift time\nscale.","type":"Results"},{"text":"The N- and C-termini present highly negative hetNOE values indicating high flexibility.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-09-07T13:26:17.183Z"}},{"start":21,"end":143,"reference_id":"36617868","reference_source":"pmid","reference_html":"Structural and dynamical insights into SilE silver binding from combined analytical probes. <i> Monneau Y, Arrault C, Duroux C, Martin M, Chirot F, Mac Aleese L, Girod M, Comby-Zerbino C, Hagège A, Walker O, Hologne M. </i> Phys Chem Chem Phys, 2023","date":"2023-09-07T13:59:07.303Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005586","ec_ontology":"ECO","ec_name":"high throughput mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03984r002","statement":[{"text":"Along this line, the HRMS observation suggests that silver-bound SilE is generally less disordered than silver-free SilE, which is consistent with the NMR and CD\ndata.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"49468","entry_name":"silver(1+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-09-07T18:17:19.965Z"}},{"start":110,"end":122,"reference_id":"36617868","reference_source":"pmid","reference_html":"Structural and dynamical insights into SilE silver binding from combined analytical probes. <i> Monneau Y, Arrault C, Duroux C, Martin M, Chirot F, Mac Aleese L, Girod M, Comby-Zerbino C, Hagège A, Walker O, Hologne M. </i> Phys Chem Chem Phys, 2023","date":"2025-06-16T13:50:06.411Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"49468","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03984r003","statement":[{"text":"Additionally, we have detected measurable shifts in the regions H80 to M90 and M59 to M72 before the signal disappearance where 3 HxxM and 1 MxxH motifs are present.","type":"Results"},{"text":"Large variations of CSP are observed for residues E110 to N122 and residues H129 to S141.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":110,"end":123,"reference_id":"36617868","reference_source":"pmid","reference_html":"Structural and dynamical insights into SilE silver binding from combined analytical probes. <i> Monneau Y, Arrault C, Duroux C, Martin M, Chirot F, Mac Aleese L, Girod M, Comby-Zerbino C, Hagège A, Walker O, Hologne M. </i> Phys Chem Chem Phys, 2023","date":"2023-09-06T15:29:01.316Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03984r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"49468","entry_name":"silver(1+)"}],"statement":[{"text":"The secondary structure propensities15 calculated from the backbone chemical shift assignment for each residue of the silver-bound SilE in the presence of 6 equivalents of Ag+ in solution further confirmed the α-helix folding upon silver addition (Fig. 4(B)). The folded area encompasses more residues compared to the free form (segments 110–123 + 128–142 vs. 112–117 + 132–139 without silver) and the α-helix propensity increases from 18% in the free state up to 65% in the bound state.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-09-07T13:32:07.219Z"}},{"start":128,"end":142,"reference_id":"36617868","reference_source":"pmid","reference_html":"Structural and dynamical insights into SilE silver binding from combined analytical probes. <i> Monneau Y, Arrault C, Duroux C, Martin M, Chirot F, Mac Aleese L, Girod M, Comby-Zerbino C, Hagège A, Walker O, Hologne M. </i> Phys Chem Chem Phys, 2023","date":"2023-09-06T15:29:31.928Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03984r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"49468","entry_name":"silver(1+)"}],"statement":[{"text":"The secondary structure propensities15 calculated from the backbone chemical shift assignment for each residue of the silver-bound SilE in the presence of 6 equivalents of Ag+ in solution further confirmed the α-helix folding upon silver addition (Fig. 4(B)). The folded area encompasses more residues compared to the free form (segments 110–123 + 128–142 vs. 112–117 + 132–139 without silver) and the α-helix propensity increases from 18% in the free state up to 65% in the bound state.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-09-07T13:32:15.450Z"}},{"start":57,"end":95,"reference_id":"36617868","reference_source":"pmid","reference_html":"Structural and dynamical insights into SilE silver binding from combined analytical probes. <i> Monneau Y, Arrault C, Duroux C, Martin M, Chirot F, Mac Aleese L, Girod M, Comby-Zerbino C, Hagège A, Walker O, Hologne M. </i> Phys Chem Chem Phys, 2023","date":"2023-09-06T15:30:42.492Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03984r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"49468","entry_name":"silver(1+)"}],"statement":[{"text":"A series of CD experiments were performed and confirmed the formation of α-helix upon silver binding for this shorter construct (Fig. S6, ESI†) as observed for the full-length SilE.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-09-07T13:33:03.273Z"}},{"start":21,"end":143,"reference_id":"36617868","reference_source":"pmid","reference_html":"Structural and dynamical insights into SilE silver binding from combined analytical probes. <i> Monneau Y, Arrault C, Duroux C, Martin M, Chirot F, Mac Aleese L, Girod M, Comby-Zerbino C, Hagège A, Walker O, Hologne M. </i> Phys Chem Chem Phys, 2023","date":"2023-09-07T13:58:01.816Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03984r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"49468","entry_name":"silver(1+)"}],"statement":[{"text":"Through the Guinier plot analysis, we derived a radius of gyration Rg = 37.7 ± 0.7 Å for free SilE and Rg = 32.9 ± 0.2 Å for SilE + 6 equivalents Ag+. Therefore, we can conclude the compactness of the structure in the presence of silver as observed in IM-MS experiments.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-09-07T18:17:11.311Z"}},{"start":80,"end":90,"reference_id":"36617868","reference_source":"pmid","reference_html":"Structural and dynamical insights into SilE silver binding from combined analytical probes. <i> Monneau Y, Arrault C, Duroux C, Martin M, Chirot F, Mac Aleese L, Girod M, Comby-Zerbino C, Hagège A, Walker O, Hologne M. </i> Phys Chem Chem Phys, 2023","date":"2025-06-16T13:49:38.064Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"49468","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03984r008","statement":[{"text":"Additionally, we have detected measurable shifts in the regions H80 to M90 and M59 to M72 before the signal disappearance where 3 HxxM and 1 MxxH motifs are present.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":59,"end":72,"reference_id":"36617868","reference_source":"pmid","reference_html":"Structural and dynamical insights into SilE silver binding from combined analytical probes. <i> Monneau Y, Arrault C, Duroux C, Martin M, Chirot F, Mac Aleese L, Girod M, Comby-Zerbino C, Hagège A, Walker O, Hologne M. </i> Phys Chem Chem Phys, 2023","date":"2025-06-16T13:49:53.513Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"49468","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03984r009","statement":[{"text":"Additionally, we have detected measurable shifts in the regions H80 to M90 and M59 to M72 before the signal disappearance where 3 HxxM and 1 MxxH motifs are present.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":129,"end":141,"reference_id":"36617868","reference_source":"pmid","reference_html":"Structural and dynamical insights into SilE silver binding from combined analytical probes. <i> Monneau Y, Arrault C, Duroux C, Martin M, Chirot F, Mac Aleese L, Girod M, Comby-Zerbino C, Hagège A, Walker O, Hologne M. </i> Phys Chem Chem Phys, 2023","date":"2025-06-16T13:50:18.272Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0046872","term_name":"metal ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"49468","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03984r010","statement":[{"text":"Additionally, we have detected measurable shifts in the regions H80 to M90 and M59 to M72 before the signal disappearance where 3 HxxM and 1 MxxH motifs are present.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a metal ion.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":10,"released":"2024_06","sequence":"MKNIVLASLLGFGLISSAWATETVNIHERVNNAQAPAHQMQSAAAPVGIQGTAPRMAGMDQHEQAIIAHETMTNGSADAHQKMVESHQRMMGSQTVSPTGPSKSLAAMNEHERAAVAHEFMNNGQSGPHQAMAEAHRRMLSAG","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"],"alphafold_very_low_content":0.18181818181818182,"disorder_content":0.8601398601398601,"disprot_consensus":{"full":[{"start":21,"end":143,"type":"T"}],"Structural state":[{"start":21,"end":143,"type":"D"}],"Structural transition":[{"start":21,"end":143,"type":"T"}],"Molecular function":[{"start":59,"end":72,"type":"F"},{"start":80,"end":90,"type":"F"},{"start":110,"end":122,"type":"F"},{"start":129,"end":141,"type":"F"}]}},{"disprot_id":"DP03985","acc":"Q922S8","creator":"zskalman","date":"2023-03-03T11:36:39.061Z","features":{"pfam":[{"id":"PF00225","name":"Kinesin motor domain","start":260,"end":583},{"id":"PF22923","name":"Kinesin-like protein KIF2A-like, N-terminal","start":6,"end":58}],"gene3D":[]},"genes":[{"name":{"value":"Kif2c"}}],"length":721,"name":"Kinesin-like protein KIF2C","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":183,"end":223,"reference_id":"14980225","reference_source":"pmid","reference_html":"A common mechanism for microtubule destabilizers-M type kinesins stabilize curling of the protofilament using the class-specific neck and loops. <i> Ogawa T, Nitta R, Okada Y, Hirokawa N. </i> Cell, 2004","date":"2023-04-20T14:17:03.191Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1V8J"}],"region_id":"DP03985r001","statement":[{"text":"The distal half of the neck, Ser183–Phe223, is predicted to form a helical structure, but this region was disordered and it was not possible to trace. ","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888","statements":[{"type":"Results","text":"The well-conserved nucleotide binding pocket is occupied by Mg-ADP for the crystal with ADP in the mother liquid and by Mg-AMP-PNP for the crystal with AMP-PNP."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:197","statements":[{"type":"Results","text":"The well-conserved nucleotide binding pocket is occupied by Mg-ADP for the crystal with ADP in the mother liquid and by Mg-AMP-PNP for the crystal with AMP-PNP."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T15:55:21.694Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MESLHARLFPGLSINIQRSNGLIHPANISTVNVEKSCVSVEWIEGGTTKGKEIDIDDVAAINPELLQLLPLRPKDSLPLQENVTVPKQKRKSVNSKIPALKEGLRSRSTRMSTVSEVRIPAQENEMEVELPVPTNSRKQFAIPSHPRASCSTVTELPLLMVSEEAEEQAHSTRSTSSANPGNSVRRKSCIVKEMEKMKNKREEKRAQNSELRIKRAQEYDSSFPNWEFARMIKEFRVTMECSPLTVTDPIEEHRICVCVRKRPLNKQELAKKEIDVISVPSKCLLLVHEPKLKVDLTKYLENQAFCFDFAFDETASNEVVYRFTARPLVQTIFEGGKATCFAYGQTGSGKTHTMGGDLSGKSQNASKGIYAMASRDVFLLKNQPRYRNLNLEVYVTFFEIYNGKVFDLLNKKAKLRVLEDSRQQVQVVGLQEYLVTCADDVIKMINMGSACRTSGQTFANSNSSRSHACFQILLRTKGRLHGKFSLVDLAGNERGADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHTPFRESKLTQVLRDSFIGENSRTCMIAMISPGISSCEYTLNTLRYADRVKELSPHSGPSGEQPVQMETEVMEASSNGTSLTGNEEEELSSQMSSFNEAMTQIRELEERALEELREIIQQGPNWLELSEMTDQPDYDLETFVNKAESALTQQAKQAKHFSALREVIKALRLAMQLEEQASKQINSKKRHQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"alphafold_very_low_content":0.21359223300970873,"disorder_content":0.056865464632454926,"disprot_consensus":{"full":[{"start":183,"end":223,"type":"D"}],"Structural state":[{"start":183,"end":223,"type":"D"}]}},{"disprot_id":"DP03988","acc":"Q86WX3","creator":"eficho","date":"2023-03-03T12:39:42.904Z","features":{"pfam":[{"id":"PF15684","name":"Active regulator of SIRT1, or 40S ribosomal protein S19-binding 1","start":34,"end":134}],"gene3D":[]},"genes":[{"name":{"value":"RPS19BP1"},"synonyms":[{"value":"AROS"}]}],"length":136,"name":"Active regulator of SIRT1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":136,"reference_id":"36361557","reference_source":"pmid","reference_html":"Molecular Mechanism of Sirtuin 1 Modulation by the AROS Protein. <i> Weiss S, Adolph RS, Schweimer K, DiFonzo A, Meleshin M, Schutkowski M, Steegborn C. </i> Int J Mol Sci, 2022","date":"2023-08-26T18:43:27.833Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03988r001","statement":[{"text":"For a more detailed structural analysis of AROS, we then performed 2D-NMR spectroscopy. The [1H,15N]-HSQC spectrum of AROS (Figure 2E) displays poor signal dispersion in the 1H dimension, indicating that AROS lacks a stable and complete tertiary structure in absence of relevant factors such as an interaction partner or crowding environment.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-09-06T15:34:22.593Z"}},{"start":1,"end":136,"reference_id":"36361557","reference_source":"pmid","reference_html":"Molecular Mechanism of Sirtuin 1 Modulation by the AROS Protein. <i> Weiss S, Adolph RS, Schweimer K, DiFonzo A, Meleshin M, Schutkowski M, Steegborn C. </i> Int J Mol Sci, 2022","date":"2023-08-26T18:45:02.547Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03988r002","statement":[{"text":"Native PAGE experiments showed a single band corresponding to the molecular mass of an AROS monomer (Figure 1D), showing that the protein is monomeric in solution and thus apparently non-globular due to partly unfolded regions.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-09-06T15:33:38.542Z"}},{"start":1,"end":136,"reference_id":"36361557","reference_source":"pmid","reference_html":"Molecular Mechanism of Sirtuin 1 Modulation by the AROS Protein. <i> Weiss S, Adolph RS, Schweimer K, DiFonzo A, Meleshin M, Schutkowski M, Steegborn C. </i> Int J Mol Sci, 2022","date":"2023-09-06T15:20:18.490Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0150066","term_name":"negative regulation of deacetylase activity","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001192","ec_ontology":"ECO","ec_name":"in vitro deacetylation assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP03988r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q96EB6"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8IXJ6"}],"sequence_construct":"MGHHHHHHAENLYFQGHMSAALLRRGLELLAASEAPRDPPGQAKPRGAPVKRPRKTKAIQAQKLRNSAKGKVPKSALDEYRKRECRDHLRVNLKFLTRTRSTVAESVSQQILRQNRGRKACDRPVAKTKKKKAEGTVFTEEDFQKFQQEYFGS","statement":[{"text":"To analyze the functional effect of AROS on Sirt1, we performed Sirt1 activity assays using the p53-derived, fluorogenic Fluor-de-Lys (FdL) 1 substrate peptide [27]. Titrating in AROS protein caused a concentration-dependent, potent inhibition of full-length Sirt1 with an IC50 of 11 ± 2 µM (Figure 3B). The inhibition was confirmed in an absorption-based coupled enzymatic assay (Supplementary Figure S2C) employing a p53-derived substrate peptide devoid of FdL’s non-physiological fluorophore modification, which can artificially influence Sirtuin/ligand interactions [27]. We then analyzed the mechanism of AROS-dependent Sirt1 inhibition through competition experiments with the Sirt1 substrates, acetylated peptide, and NAD+. Adding 40 µM AROS caused only moderate changes in vmax in titrations of either substrate (Figure 3C,D). It increased KM only slightly in the NAD+ titration, but more significantly (~3-fold) in the peptide titration, suggesting a mixed-type inhibition involving competition with the acyl substrate but not with the nucleotide cosubstrate.","type":"Results"},{"text":"Analyzing the FdL deacetylation activity of Sirt1, Sirt2, Sirt3, respective desuccinylation activity of Sirt5, in the absence and presence of 100 μM AROS, revealed that the protein inhibits all isoforms, albeit with varying potency (Figure 4C). It potently inhibits Sirt1, only weakly Sirt2 and Sirt5, and it shows a medium potency against Sirt3.","type":"Results"},{"text":"The AROS effects on Sirt3 and Sirt5 are unlikely to be physiologically relevant due to the mitochondrial localization of these isoforms.","type":"Results"}],"term_comment":"","term_def":"\"Any process that stops, prevents or reduces the frequency, rate or extent of deacetylase activity.\" [GOC:aruk, GOC:bc, PMID:19457097]","term_is_obsolete":false,"term_not_annotate":false},{"start":62,"end":71,"reference_id":"36361557","reference_source":"pmid","reference_html":"Molecular Mechanism of Sirtuin 1 Modulation by the AROS Protein. <i> Weiss S, Adolph RS, Schweimer K, DiFonzo A, Meleshin M, Schutkowski M, Steegborn C. </i> Int J Mol Sci, 2022","date":"2025-06-16T14:04:43.575Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q96EB6","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03988r004","statement":[{"text":"Partial assignment of AROS in the complex indicated that the very N- and C-terminal parts of AROS and the middle region from 57 to 89 are involved in binding to Sirt1 (Figure 4A; Supplementary Figure S3).","type":"Results"},{"text":"The center of AROS (62–71) appears to be key to the interaction, apparently at least in part through contacts to the Sirt1-SBD, but outside regions in AROS and Sirt1 seem to contribute to their affinity (Table 2).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":136,"reference_id":"36361557","reference_source":"pmid","reference_html":"Molecular Mechanism of Sirtuin 1 Modulation by the AROS Protein. <i> Weiss S, Adolph RS, Schweimer K, DiFonzo A, Meleshin M, Schutkowski M, Steegborn C. </i> Int J Mol Sci, 2022","date":"2023-09-06T15:21:55.357Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006303","ec_ontology":"ECO","ec_name":"microscale thermophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","region_id":"DP03988r005","statement":[{"text":"Full-length AROS bound to mini-Sirt1ex687 with a Kd of 1.3 ± 0.2 μM, which is one order of magnitude below the IC50 and thus consistent with competition between AROS and substrate peptide.","type":"Results"},{"text":"These results indicate that N- and C-terminus of AROS contribute to binding, as well as the Sirt1 N-terminus/SBD and the catalytic core.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"Q96EB6","operator":"and","partner_start":null,"partner_end":null}]},{"start":1,"end":136,"reference_id":"36361557","reference_source":"pmid","reference_html":"Molecular Mechanism of Sirtuin 1 Modulation by the AROS Protein. <i> Weiss S, Adolph RS, Schweimer K, DiFonzo A, Meleshin M, Schutkowski M, Steegborn C. </i> Int J Mol Sci, 2022","date":"2023-09-06T15:23:49.952Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001170","ec_ontology":"ECO","ec_name":"cross-linking evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IPI","region_id":"DP03988r006","statement":[{"text":"DSSO treatment of a mixture of Sirtuin and AROS, but not of either protein alone, led to the formation of a potential complex band (MW of the complex: 58 kDa; Figure 4B).","type":"Results"},{"text":"We thus conclude that both halves of AROS contribute to binding to Sirt1, which employs its catalytic core for this interaction, supported by the SBD.","type":"Results"},{"text":"Consistently, CL experiments with Sirt3 and Sirt5 resulted in clear bands for linked complexes with AROS (Figure 4D,E).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"Q96EB6","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9NXA8","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9NTG7","operator":"or","partner_start":null,"partner_end":null}]}],"regions_counter":6,"released":"2024_06","sequence":"MSAALLRRGLELLAASEAPRDPPGQAKPRGAPVKRPRKTKAIQAQKLRNSAKGKVPKSALDEYRKRECRDHLRVNLKFLTRTRSTVAESVSQQILRQNRGRKACDRPVAKTKKKKAEGTVFTEEDFQKFQQEYFGS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.11029411764705882,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":136,"type":"D"}],"Structural state":[{"start":1,"end":136,"type":"D"}],"Biological process":[{"start":1,"end":136,"type":"F"}],"Molecular function":[{"start":1,"end":136,"type":"F"}]}},{"disprot_id":"DP03989","acc":"Q2YLR6","creator":"eficho","date":"2023-03-03T12:40:37.468Z","features":{"pfam":[{"id":"PF02974","name":"Protease inhibitor Inh","start":87,"end":177}],"gene3D":[]},"genes":[{"name":{"value":"omp19"},"olnNames":[{"value":"BAB1_1930"}]}],"length":177,"name":"Outer membrane lipoprotein omp19","ncbi_taxon_id":359391,"organism":"Brucella abortus (strain 2308)","regions":[{"start":22,"end":85,"reference_id":"36187929","reference_source":"pmid","reference_html":"A disordered region retains the full protease inhibitor activity and the capacity to induce CD8<sup>+</sup> T cells <i>in vivo</i> of the oral vaccine adjuvant U-Omp19. <i> Laura Darriba M, Castro CP, Coria LM, Bruno L, Laura Cerutti M, Otero LH, Chemes LB, Rasia RM, Klinke S, Cassataro J, Pasquevich KA. </i> Comput Struct Biotechnol J, 2022","date":"2023-09-11T13:43:56.361Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03989r001","statement":[{"text":"Analysis of the backbone secondary chemical shifts along the U-Omp19 sequence confirmed that the first 65 residues are disordered, while the rest of the protein adopts mostly b-sheet folding (Fig. 3B).\n","type":"Results"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"sequence_construct":"MQSSRLGNLDNVSPPPPPAPVNAVPAGTVQKGNLDSPTQFPNAPSTDMSAQSGTQVASLPPASAPDLTPGAVAGVWNASLGGQSCKIATPQTKYGQGYRAGPLRCPGELANLASWAVNGKQLVLYDANGGTVASLYSSGQGRFDGQTTGGQAVTLSRLEHHHHHH","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-09-11T17:26:30.035Z"}},{"start":22,"end":61,"reference_id":"36187929","reference_source":"pmid","reference_html":"A disordered region retains the full protease inhibitor activity and the capacity to induce CD8<sup>+</sup> T cells <i>in vivo</i> of the oral vaccine adjuvant U-Omp19. <i> Laura Darriba M, Castro CP, Coria LM, Bruno L, Laura Cerutti M, Otero LH, Chemes LB, Rasia RM, Klinke S, Cassataro J, Pasquevich KA. </i> Comput Struct Biotechnol J, 2022","date":"2023-09-12T12:39:35.664Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0010466","term_name":"negative regulation of peptidase activity","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03989r002","statement":[{"text":"The isolated N-terminal fragment U-Omp19(1–60) presented anomalous electrophoretic mobility in SDS-PAGE. Although anomalous migration in SDS-PAGE can be attributed to the high content of acidic residues and thus low binding of SDS [63], other parameters such as expansion in solution [64] and a high proline content [65] can contribute to anomalous migration. This is probably\nthe case for U-Omp19(1–60), since its acidic content does not differ significantly from that of globular proteins and its expansion inferred from SEC experiments is compatible with a random coil conformation [55]. This intrinsically disordered and highly expanded U-Omp19(1–60) N-terminal fragment has demonstrated\nto be necessary and sufficient to encode the full inhibitory activity of U-Omp19 towards pancreatic elastase (serine-protease), papain (cysteine-protease) and pepsin (aspartic-protease).","type":"Discussion"},{"text":"Surprisingly, U-Omp19(1–60) retained the full inhibitory activity of full-length U-Omp19 against pancreatic elastase, papain (Fig. 9E) and pepsin (Fig. S6), indicating that this region is not only required, but is also sufficient for the protease inhibitor activity of U-Omp19.","type":"Results"}],"ec_go":"IDA","sequence_construct":"MQSSRLGNLDNVSPPPPPAPVNAVPAGTVQKGNLDSPTQFPNAPSTDMSAQSGTQVASLPENLYFQ","term_comment":"","term_def":"\"Any process that stops or reduces the rate of peptidase activity, the hydrolysis of peptide bonds within proteins.\" [GOC:dph, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-10-09T13:55:28.033Z"}},{"start":22,"end":81,"reference_id":"36187929","reference_source":"pmid","reference_html":"A disordered region retains the full protease inhibitor activity and the capacity to induce CD8<sup>+</sup> T cells <i>in vivo</i> of the oral vaccine adjuvant U-Omp19. <i> Laura Darriba M, Castro CP, Coria LM, Bruno L, Laura Cerutti M, Otero LH, Chemes LB, Rasia RM, Klinke S, Cassataro J, Pasquevich KA. </i> Comput Struct Biotechnol J, 2022","date":"2023-09-12T12:35:44.453Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03989r003","statement":[{"text":"The Far-UV CD spectrum of U-Omp19(1–60) was compatible with that of an IDP with a minimum near 200 nm and low ellipticity at 222 nm (Fig. 9D). However, the small negative signal at 222 nm suggests some residual secondary structure content. Analysis of the ellipticity at 222 vs 200 nm allowed to classify U-Omp19(1–60) within the random coil subclass of IDPs [55].","type":"Results"}],"sequence_construct":"MQSSRLGNLDNVSPPPPPAPVNAVPAGTVQKGNLDSPTQFPNAPSTDMSAQSGTQVASLPENLYFQ","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-10-09T13:54:36.936Z"}},{"start":22,"end":81,"reference_id":"36187929","reference_source":"pmid","reference_html":"A disordered region retains the full protease inhibitor activity and the capacity to induce CD8<sup>+</sup> T cells <i>in vivo</i> of the oral vaccine adjuvant U-Omp19. <i> Laura Darriba M, Castro CP, Coria LM, Bruno L, Laura Cerutti M, Otero LH, Chemes LB, Rasia RM, Klinke S, Cassataro J, Pasquevich KA. </i> Comput Struct Biotechnol J, 2022","date":"2023-09-07T18:14:06.863Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0050778","term_name":"positive regulation of immune response","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007119","ec_ontology":"ECO","ec_name":"in vivo assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP03989r004","sequence_construct":"MQSSRLGNLDNVSPPPPPAPVNAVPAGTVQKGNLDSPTQFPNAPSTDMSAQSGTQVASLPENLYFQ","statement":[{"text":"The adjuvant activity of U-Omp19 was evidenced by the significant increase in the proliferation of OVA-specific CD8+ T cells in OVA + U-Omp19 compared to OVA alone-immunized mice. U-Omp19(1–60) fully conserved this adjuvanticity since the increase in proliferation was similar when OVA was co-delivered either with U-Omp19 or U-Omp19(1–60). In contrast, U-Omp19(60-159) was not able to increase the assessed proliferation (Fig. 10).","type":"Results"}],"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of the immune response, the immunological reaction of an organism to an immunogenic stimulus.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":22,"end":81,"reference_id":"36187929","reference_source":"pmid","reference_html":"A disordered region retains the full protease inhibitor activity and the capacity to induce CD8<sup>+</sup> T cells <i>in vivo</i> of the oral vaccine adjuvant U-Omp19. <i> Laura Darriba M, Castro CP, Coria LM, Bruno L, Laura Cerutti M, Otero LH, Chemes LB, Rasia RM, Klinke S, Cassataro J, Pasquevich KA. </i> Comput Struct Biotechnol J, 2022","date":"2023-10-14T21:35:21.995Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007688","ec_ontology":"ECO","ec_name":"gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03989r005","statement":[{"text":"Also, U-Omp19(1–60) showed an-omalous electrophoretic mobility as revealed by Western blot (Fig. 9A). Although U-Omp19(1–60) presented the electrophoretic migration of a globular protein of ∼15 kDa (Fig. 9A), mass spectrometry studies indicated a MW of 6836.4 Da (data not shown), compatible with its theoretical MWTHEO of 6835.6 Da.","type":"Results"}],"sequence_construct":"MQSSRLGNLDNVSPPPPPAPVNAVPAGTVQKGNLDSPTQFPNAPSTDMSAQSGTQVASLPENLYFQ","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-10-19T09:02:32.832Z"}},{"start":22,"end":81,"reference_id":"36187929","reference_source":"pmid","reference_html":"A disordered region retains the full protease inhibitor activity and the capacity to induce CD8<sup>+</sup> T cells <i>in vivo</i> of the oral vaccine adjuvant U-Omp19. <i> Laura Darriba M, Castro CP, Coria LM, Bruno L, Laura Cerutti M, Otero LH, Chemes LB, Rasia RM, Klinke S, Cassataro J, Pasquevich KA. </i> Comput Struct Biotechnol J, 2022","date":"2023-10-09T13:53:41.343Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP03989r006","sequence_construct":"MQSSRLGNLDNVSPPPPPAPVNAVPAGTVQKGNLDSPTQFPNAPSTDMSAQSGTQVASLPENLYFQ","statement":[{"text":"SEC analysis showed a single and symmetric peak that eluted as a globular protein of higher MW (Fig. 9B) with a high MWSEC/MWTHEO ratio of 3.36 ± 0.05 (Fig. 9C) that is consistent with the IDP character of U-Omp19(1–60).","type":"Results"}]}],"regions_counter":6,"released":"2024_06","sequence":"MGISKASLLSLAAAGIVLAGCQSSRLGNLDNVSPPPPPAPVNAVPAGTVQKGNLDSPTQFPNAPSTDMSAQSGTQVASLPPASAPDLTPGAVAGVWNASLGGQSCKIATPQTKYGQGYRAGPLRCPGELANLASWAVNGKQLVLYDANGGTVASLYSSGQGRFDGQTTGGQAVTLSR","taxonomy":["Bacteria","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Brucellaceae","Brucella/Ochrobactrum group","Brucella"],"alphafold_very_low_content":0.06779661016949153,"disorder_content":0.3615819209039548,"disprot_consensus":{"full":[{"start":22,"end":85,"type":"D"}],"Structural state":[{"start":22,"end":85,"type":"D"}],"Biological process":[{"start":22,"end":81,"type":"F"}]}},{"disprot_id":"DP03990","acc":"Q92597","creator":"eficho","date":"2023-03-03T12:41:52.542Z","features":{"pfam":[{"id":"PF03096","name":"Ndr family","start":34,"end":316}],"gene3D":[]},"genes":[{"name":{"value":"NDRG1"},"synonyms":[{"value":"CAP43"},{"value":"DRG1"},{"value":"RTP"}]}],"length":394,"name":"Protein NDRG1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":312,"end":394,"reference_id":"36139110","reference_source":"pmid","reference_html":"The Ni(II)-Binding Activity of the Intrinsically Disordered Region of Human NDRG1, a Protein Involved in Cancer Development. <i> Beniamino Y, Cenni V, Piccioli M, Ciurli S, Zambelli B. </i> Biomolecules, 2022","date":"2024-08-29T08:44:10.654Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP03990r001","statement":[{"text":"The CD spectrum of hNDRG1*C is typical of an intrinsically disordered protein, with a pronounced negative peak around 198 nm and a quantitative analysis of the spectrum confirming the low amount of secondary structure, with 6.6% α-helices, 26.3% β-strands and 67% unordered (Figure 3).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:39:43.543Z"}},{"start":312,"end":394,"reference_id":"36139110","reference_source":"pmid","reference_html":"The Ni(II)-Binding Activity of the Intrinsically Disordered Region of Human NDRG1, a Protein Involved in Cancer Development. <i> Beniamino Y, Cenni V, Piccioli M, Ciurli S, Zambelli B. </i> Biomolecules, 2022","date":"2024-08-29T08:45:42.566Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP03990r002","statement":[{"text":"The BEST-TROSY 1H-15N HSQC spectrum of hNDRG1*C at pH 6.5 (Figure 4A) features a narrow 1H chemical shift dispersion (8.0–8.6 ppm) typically seen for intrinsically disordered proteins (IDPs). ","type":"Results"},{"text":"The 1H 15N HSQC spectra of hNDRG1*C are characteristic of an intrinsically disordered protein, with low signal dispersion in the 1H dimension. This observation is maintained from pH 6.5 to 7.5 and confirms that this region is dominated by random coil conformations, lacking a well-defined structure, as predicted by the in silico disorder prediction analysis.","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:40:01.284Z"}},{"start":338,"end":394,"reference_id":"36139110","reference_source":"pmid","reference_html":"The Ni(II)-Binding Activity of the Intrinsically Disordered Region of Human NDRG1, a Protein Involved in Cancer Development. <i> Beniamino Y, Cenni V, Piccioli M, Ciurli S, Zambelli B. </i> Biomolecules, 2022","date":"2025-06-16T14:08:11.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0016151","term_name":"nickel cation binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"49786","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03990r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"53001","entry_name":"nickel sulfate"}],"statement":[{"text":"Overall, the picture that can be drawn from the NMR spectra analysis indicates the involvement of the side chains of Asp338, His345, Glu348, His355, Glu358, His365, Glu368, His371, Asp373, Asn377 and Cys394 in the uptake of Ni(II) by hNDRG1*C.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a nickel (Ni) cation.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":312,"end":394,"reference_id":"36139110","reference_source":"pmid","reference_html":"The Ni(II)-Binding Activity of the Intrinsically Disordered Region of Human NDRG1, a Protein Involved in Cancer Development. <i> Beniamino Y, Cenni V, Piccioli M, Ciurli S, Zambelli B. </i> Biomolecules, 2022","date":"2024-08-29T08:50:59.792Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0016151","term_name":"nickel cation binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"49786","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP03990r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"53001","entry_name":"nickel sulfate"}],"statement":[{"text":"The binding parameters, obtained from the fit of four binding isotherms (Figure 2B) and by averaging the results of the fits, indicate that the protein presents a single binding event (n = 1.4 ± 0.5) with affinity in the micromolar range (KA = 1.4 ± 0.3 × 104; KD = 70 ± 1 µM) and enthalpically driven (ΔH = −9 ± 6 kcal mol−1 and ΔS = −19 ± 13 cal mol−1 K−1).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a nickel (Ni) cation.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:40:46.026Z"}}],"regions_counter":4,"released":"2024_12","sequence":"MSREMQDVDLAEVKPLVEKGETITGLLQEFDVQEQDIETLHGSVHVTLCGTPKGNRPVILTYHDIGMNHKTCYNPLFNYEDMQEITQHFAVCHVDAPGQQDGAASFPAGYMYPSMDQLAEMLPGVLQQFGLKSIIGMGTGAGAYILTRFALNNPEMVEGLVLINVNPCAEGWMDWAASKISGWTQALPDMVVSHLFGKEEMQSNVEVVHTYRQHIVNDMNPGNLHLFINAYNSRRDLEIERPMPGTHTVTLQCPALLVVGDSSPAVDAVVECNSKLDPTKTTLLKMADCGGLPQISQPAKLAEAFKYFVQGMGYMPSASMTRLMRSRTASGSSVTSLDGTRSRSHTSEGTRSRSHTSEGTRSRSHTSEGAHLDITPNSGAAGNSAGPKSMEVSC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.2563451776649746,"dataset":["Cancer-related proteins","Age-related disorders proteins"],"disorder_content":0.21065989847715735,"disprot_consensus":{"full":[{"start":312,"end":394,"type":"D"}],"Structural state":[{"start":312,"end":394,"type":"D"}],"Molecular function":[{"start":312,"end":394,"type":"F"}]}},{"disprot_id":"DP03991","acc":"Q9UN86","creator":"zskalman","date":"2023-03-03T13:39:12.361Z","features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":333,"end":389},{"id":"PF02136","name":"Nuclear transport factor 2 (NTF2) domain","start":11,"end":133}],"gene3D":[]},"genes":[{"name":{"value":"G3BP2"},"synonyms":[{"value":"KIAA0660"}]}],"length":482,"name":"Ras GTPase-activating protein-binding protein 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":45,"end":54,"reference_id":"26410532","reference_source":"pmid","reference_html":"Crystal structure of the G3BP2 NTF2-like domain in complex with a canonical FGDF motif peptide. <i> Kristensen O. </i> Biochem Biophys Res Commun, 2015","date":"2023-04-20T14:20:06.236Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5DRV"}],"region_id":"DP03991r001","statement":[{"text":"The asymmetric unit of the space group, H32, contains a single G3BP2 NTF2 polypeptide chain that could be traced from residue 1 to 139 except for a disordered loop region, residues 45-54.","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08411","statements":[{"type":"Results","text":"The crystal structure of the G3BP2 NTF2-like domain in complex\nwith a FGDF peptide contains 60% solvent and was solved by molecular\nreplacement and refined at a resolution of 2.75 Å with R and\nR-free values of 23% and 29%, respectively.\n"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T15:55:49.249Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MVMEKPSPLLVGREFVRQYYTLLNKAPEYLHRFYGRNSSYVHGGVDASGKPQEAVYGQNDIHHKVLSLNFSECHTKIRHVDAHATLSDGVVVQVMGLLSNSGQPERKFMQTFVLAPEGSVPNKFYVHNDMFRYEDEVFGDSEPELDEESEDEVEEEQEERQPSPEPVQENANSGYYEAHPVTNGIEEPLEESSHEPEPEPESETKTEELKPQVEEKNLEELEEKSTTPPPAEPVSLPQEPPKAFSWASVTSKNLPPSGTVSSSGIPPHVKAPVSQPRVEAKPEVQSQPPRVREQRPRERPGFPPRGPRPGRGDMEQNDSDNRRIIRYPDSHQLFVGNLPHDIDENELKEFFMSFGNVVELRINTKGVGGKLPNFGFVVFDDSEPVQRILIAKPIMFRGEVRLNVEEKKTRAARERETRGGGDDRRDIRRNDRGPGGPRGIVGGGMMRDRDGRGPPPRGGMAQKLGSGRGTGQMEGRFTGQRR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.42323651452282157,"dataset":["Condensates-related proteins","RNA-binding proteins"],"disorder_content":0.02074688796680498,"disprot_consensus":{"full":[{"start":45,"end":54,"type":"D"}],"Structural state":[{"start":45,"end":54,"type":"D"}]}},{"disprot_id":"DP03992","acc":"P0A7I7","creator":"vacs","date":"2023-03-04T11:04:13.915Z","features":{"pfam":[{"id":"PF00925","name":"GTP cyclohydrolase II","start":5,"end":170}],"gene3D":[]},"genes":[{"name":{"value":"ribA"},"olnNames":[{"value":"b1277"},{"value":"JW1269"}]}],"length":196,"name":"GTP cyclohydrolase-2","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":175,"end":196,"reference_id":"16115872","reference_source":"pmid","reference_html":"GTP cyclohydrolase II structure and mechanism. <i> Ren J, Kotaka M, Lockyer M, Lamb HK, Hawkins AR, Stammers DK. </i> J Biol Chem, 2005","date":"2023-03-04T11:06:21.020Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2BZ1"},{"db":"PDB","id":"2BZ0"}],"region_id":"DP03992r001","statement":[{"text":"Indeed, automated model building with Arp/warp resulted in the fitting of 167 of 173 ordered residues, there being no density visible for the C-terminal region.","type":"Results"},{"text":"Residues 175-196 are disordered in both structures.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T08:57:55.827Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MQLKRVAEAKLPTPWGDFLMVGFEELATGHDHVALVYGDISGHTPVLARVHSECLTGDALFSLRCDCGFQLEAALTQIAEEGRGILLYHRQEGRNIGLLNKIRAYALQDQGYDTVEANHQLGFAADERDFTLCADMFKLLGVNEVRLLTNNPKKVEILTEAGINIVERVPLIVGRNPNNEHYLDTKAEKMGHLLNK","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"alphafold_very_low_content":0,"disorder_content":0.11224489795918367,"disprot_consensus":{"full":[{"start":175,"end":196,"type":"D"}],"Structural state":[{"start":175,"end":196,"type":"D"}]}},{"disprot_id":"DP03993","acc":"Q12395","creator":"vacs","date":"2023-03-05T10:59:26.330Z","features":{"pfam":[{"id":"PF03556","name":"Cullin binding","start":145,"end":263},{"id":"PF22566","name":"UBA-like domain","start":12,"end":56}],"gene3D":[]},"genes":[{"name":{"value":"DCN1"},"orfNames":[{"value":"L3111"}],"olnNames":[{"value":"YLR128W"}]}],"length":269,"name":"Defective in cullin neddylation protein 1","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":11,"reference_id":"18206966","reference_source":"pmid","reference_html":"Dcn1 functions as a scaffold-type E3 ligase for cullin neddylation. <i> Kurz T, Chou YC, Willems AR, Meyer-Schaller N, Hecht ML, Tyers M, Peter M, Sicheri F. </i> Mol Cell, 2008","date":"2023-03-05T11:00:51.999Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3BQ3"}],"region_id":"DP03993r001","statement":[{"text":"Residues 1–11 and the interdomain linker corresponding to residues 56–65 in the final ScDcn1 model were not modeled due to disorder.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-05T16:14:07.153Z"}},{"start":56,"end":65,"reference_id":"18206966","reference_source":"pmid","reference_html":"Dcn1 functions as a scaffold-type E3 ligase for cullin neddylation. <i> Kurz T, Chou YC, Willems AR, Meyer-Schaller N, Hecht ML, Tyers M, Peter M, Sicheri F. </i> Mol Cell, 2008","date":"2023-04-05T16:16:56.560Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":136,"end":136,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":145,"end":145,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":203,"end":203,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":230,"end":230,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"3BQ3"}],"region_id":"DP03993r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"}],"statement":[{"text":"Residues 1–11 and the interdomain linker corresponding to residues 56–65 in the final ScDcn1 model were not modeled due to disorder.","type":"Methods"}]}],"regions_counter":2,"released":"2024_06","sequence":"MSNNKIKRKDASPEQEAIESFTSLTKCDPKVSRKYLQRNHWNINYALNDYYDKEIGTFTDEVSTVAHPPVYPKELTQVFEHYINNNLFDIDSLVKFIEELGYNLEDLATLCLAHLLGYKKLEEPLKREDFLSTWFMQGCSTISDMQECIKTLDVKLHEDLQYFTQIYNYAFNLILDPNRKDIDTDEGIQYWKLFFQPEYPVRMEPDLLEAWFRFLRDEGKTTISKDTWRMLLLFFKRYPTIQKIISDYDETAAWPFIIDEFYECLQDQQ","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.07434944237918216,"disorder_content":0.07806691449814127,"disprot_consensus":{"full":[{"start":1,"end":11,"type":"D"},{"start":56,"end":65,"type":"D"}],"Structural state":[{"start":1,"end":11,"type":"D"},{"start":56,"end":65,"type":"D"}]}},{"disprot_id":"DP03994","acc":"P42641","creator":"eficho","date":"2023-03-17T16:26:48.807Z","features":{"pfam":[{"id":"PF01018","name":"GTP1/OBG","start":4,"end":157},{"id":"PF01926","name":"50S ribosome-binding GTPase","start":162,"end":284}],"gene3D":[]},"genes":[{"name":{"value":"obgE","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11555285","url":"http://www.ncbi.nlm.nih.gov/pubmed/11555285","alternativeUrl":"https://europepmc.org/abstract/MED/11555285"}}]},"synonyms":[{"value":"cgtA","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12402086","url":"http://www.ncbi.nlm.nih.gov/pubmed/12402086","alternativeUrl":"https://europepmc.org/abstract/MED/12402086"}}]},{"value":"obg","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01454","url":"https://hamap.expasy.org/unirule/MF_01454"}}]},{"value":"yhbZ"}],"olnNames":[{"value":"b3183"},{"value":"JW3150"}]}],"length":390,"name":"GTPase ObgE/CgtA","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":361,"end":382,"reference_id":"36864742","reference_source":"pmid","reference_html":"YbiB: a novel interactor of the GTPase ObgE.  <i> Deckers B, Vercauteren S, De Kock V, Martin C, Lazar T, Herpels P, Dewachter L, Verstraeten N, Peeters E, Ballet S, Michiels J, Michiels J, Galicia C, Versées W. </i> Nucleic Acids Res, 2023","date":"2023-08-26T21:40:32.828Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP03994r001","statement":[{"text":"Intrinsically disordered regions often fold upon binding to partner proteins (72). To verify whether the intrinsically disordered C-terminus of ObgE folds upon binding to YbiB, far-UV CDspectra were recorded for peptide1, YbiB and the YbiB-peptide1 complex (1:1 molar ratio) (Figure 3D). As expected, the CD spectrum of peptide1 shows a minimum around 200 nm, which is characteristic for a disordered peptide. On the other hand, the CD spectrum of YbiB displays the characteristics of a helical fold (minima around 208 and 222 nm), corresponding to its high -helix content as shown by the crystal structure (41).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-06T17:20:52.096Z"}},{"start":361,"end":382,"reference_id":"36864742","reference_source":"pmid","reference_html":"YbiB: a novel interactor of the GTPase ObgE.  <i> Deckers B, Vercauteren S, De Kock V, Martin C, Lazar T, Herpels P, Dewachter L, Verstraeten N, Peeters E, Ballet S, Michiels J, Michiels J, Galicia C, Versées W. </i> Nucleic Acids Res, 2023","date":"2023-08-26T22:19:58.720Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"8BFT"}],"region_id":"DP03994r002","statement":[{"text":"Intrinsically disordered regions often fold upon binding to partner proteins (72). To verify whether the intrinsically disordered C-terminus of ObgE folds upon binding to YbiB, far-UV CDspectra were recorded for peptide1, YbiB and the YbiB-peptide1 complex (1:1 molar ratio) (Figure 3D). As expected, the CD spectrum of peptide1 shows a minimum around 200 nm, which is characteristic for a disordered peptide. On the other hand, the CD spectrum of YbiB displays the characteristics of a helical fold (minima around 208 and 222 nm), corresponding to its high -helix content as shown by the crystal structure (41).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-06T17:20:51.791Z"}},{"start":338,"end":390,"reference_id":"24844575","reference_source":"pmid","reference_html":"Structural and functional insights into the mode of action of a universally conserved Obg GTPase. <i> Feng B, Mandava CS, Guo Q, Wang J, Cao W, Li N, Zhang Y, Zhang Y, Wang Z, Wu J, Sanyal S, Lei J, Gao N. </i> PLoS Biol, 2014","date":"2024-05-06T17:18:26.108Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"4CSU"}],"region_id":"DP03994r003","statement":[{"text":"However, we did not find extra densities that could be attributed to the CTD of ObgE, indicating that this domain is highly flexible.","type":"Results"},{"text":"The obtained Cryo-EM structure corresponds to ObgE bound to the 50S ribosome subunit.","type":"Curator statement"}]}],"regions_counter":3,"released":"2024_06","sequence":"MKFVDEASILVVAGDGGNGCVSFRREKYIPKGGPDGGDGGDGGDVWMEADENLNTLIDYRFEKSFRAERGQNGASRDCTGKRGKDVTIKVPVGTRVIDQGTGETMGDMTKHGQRLLVAKGGWHGLGNTRFKSSVNRTPRQKTNGTPGDKRELLLELMLLADVGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKSFVVADIPGLIEGAAEGAGLGIRFLKHLERCRVLLHLIDIDPIDGTDPVENARIIISELEKYSQDLATKPRWLVFNKIDLLDKVEAEEKAKAIAEALGWEDKYYLISAASGLGVKDLCWDVMTFIIENPVVQAEEAKQPEKVEFMWDDYHRQQLEEIAEEDDEDWDDDWDEDDEEGVEFIYKR","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"alphafold_very_low_content":0.12307692307692308,"dataset":["RNA-binding proteins"],"disorder_content":0.1358974358974359,"disprot_consensus":{"full":[{"start":338,"end":360,"type":"D"},{"start":361,"end":382,"type":"T"},{"start":383,"end":390,"type":"D"}],"Structural state":[{"start":338,"end":390,"type":"D"}],"Structural transition":[{"start":361,"end":382,"type":"T"}]}},{"disprot_id":"DP03995","acc":"P40484","creator":"ldobson","date":"2023-03-20T09:36:22.521Z","features":{"pfam":[{"id":"PF03637","name":"Mob1/phocein family","start":134,"end":304}],"gene3D":[]},"genes":[{"name":{"value":"MOB1"},"olnNames":[{"value":"YIL106W"}]}],"length":314,"name":"DBF2 kinase activator protein MOB1","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":114,"end":125,"reference_id":"16934835","reference_source":"pmid","reference_html":"Structural and functional analysis of Saccharomyces cerevisiae Mob1. <i> Mrkobrada S, Boucher L, Ceccarelli DF, Tyers M, Sicheri F. </i> J Mol Biol, 2006","date":"2023-04-28T06:48:10.067Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2HJN"}],"region_id":"DP03995r001","statement":[{"text":"The linker between the Mob1 core and helix H0 (residues 140–142), and the linker between helix H0 and strand S0 (residues 113–125) are disordered and hence could not be modeled in the crystal structure. ","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"}],"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":79,"end":79,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":133,"end":133,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":170,"end":170,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":187,"end":187,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":218,"end":218,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":309,"end":309,"position":"Specific residue"}],"sequence_construct":"MSPVLTTPKRHAPPPEQLQNVTDFNYTPSHQKPFLQPQAGTTVTTHQDIKQIVEMTLGSEGVLNQAVKLPRGEDENEWLAVHCVDFYNQINMLYGSITEFCSPQTCPRMIATNEYEYLWAFQKGQPPVSVSAPKYVECLMRWCQDQFDDESLFPSKVTGTFPEGFIQRVIQPILRRLFRVYAHIYCHHFNEILELNLQTVLNTSFRHFCLFAQEFELLRPADFGPLLELVMELRDR\n","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T16:55:40.358Z"}},{"start":86,"end":97,"reference_id":"16934835","reference_source":"pmid","reference_html":"Structural and functional analysis of Saccharomyces cerevisiae Mob1. <i> Mrkobrada S, Boucher L, Ceccarelli DF, Tyers M, Sicheri F. </i> J Mol Biol, 2006","date":"2023-04-28T06:47:35.866Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2HJN"}],"region_id":"DP03995r002","statement":[{"text":"The linker joining strands S-1 and S0 (residues 86–97) was disordered and could not be modeled.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"}],"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":79,"end":79,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":133,"end":133,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":170,"end":170,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":187,"end":187,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":218,"end":218,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":309,"end":309,"position":"Specific residue"}],"sequence_construct":"MSPVLTTPKRHAPPPEQLQNVTDFNYTPSHQKPFLQPQAGTTVTTHQDIKQIVEMTLGSEGVLNQAVKLPRGEDENEWLAVHCVDFYNQINMLYGSITEFCSPQTCPRMIATNEYEYLWAFQKGQPPVSVSAPKYVECLMRWCQDQFDDESLFPSKVTGTFPEGFIQRVIQPILRRLFRVYAHIYCHHFNEILELNLQTVLNTSFRHFCLFAQEFELLRPADFGPLLELVMELRDR","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T16:55:41.435Z"}},{"start":114,"end":125,"reference_id":"16934835","reference_source":"pmid","reference_html":"Structural and functional analysis of Saccharomyces cerevisiae Mob1. <i> Mrkobrada S, Boucher L, Ceccarelli DF, Tyers M, Sicheri F. </i> J Mol Biol, 2006","date":"2023-04-26T06:46:38.561Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2HJN"}],"region_id":"DP03995r003","statement":[{"text":"The linker between the Mob1 core and helix H0 (residues 140–142), and the linker between helix H0 and strand S0 (residues 113–125) are disordered and hence could not be modeled in the crystal structure. ","type":"Results"}],"sequence_construct":"MSPVLTTPKRHAPPPEQLQNVTDFNYTPSHQKPFLQPQAGTTVTTHQDIKQIVEMTLGSEGVLNQAVKLPRGEDENEWLAVHCVDFYNQINMLYGSITEFCSPQTCPRMIATNEYEYLWAFQKGQPPVSVSAPKYVECLMRWCQDQFDDESLFPSKVTGTFPEGFIQRVIQPILRRLFRVYAHIYCHHFNEILELNLQTVLNTSFRHFCLFAQEFELLRPADFGPLLELVMELRDR","construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":79,"end":79,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":133,"end":133,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":170,"end":170,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":187,"end":187,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":218,"end":218,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":309,"end":309,"position":"Specific residue"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-27T14:05:36.486Z"}},{"start":86,"end":97,"reference_id":"16934835","reference_source":"pmid","reference_html":"Structural and functional analysis of Saccharomyces cerevisiae Mob1. <i> Mrkobrada S, Boucher L, Ceccarelli DF, Tyers M, Sicheri F. </i> J Mol Biol, 2006","date":"2023-04-26T06:46:51.958Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2HJN"}],"region_id":"DP03995r004","statement":[{"text":"The linker between the Mob1 core and helix H0 (residues 140–142), and the linker between helix H0 and strand S0 (residues 113–125) are disordered and hence could not be modeled in the crystal structure. ","type":"Results"}],"sequence_construct":"MSPVLTTPKRHAPPPEQLQNVTDFNYTPSHQKPFLQPQAGTTVTTHQDIKQIVEMTLGSEGVLNQAVKLPRGEDENEWLAVHCVDFYNQINMLYGSITEFCSPQTCPRMIATNEYEYLWAFQKGQPPVSVSAPKYVECLMRWCQDQFDDESLFPSKVTGTFPEGFIQRVIQPILRRLFRVYAHIYCHHFNEILELNLQTVLNTSFRHFCLFAQEFELLRPADFGPLLELVMELRDR","construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":79,"end":79,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":133,"end":133,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":170,"end":170,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":187,"end":187,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":218,"end":218,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":309,"end":309,"position":"Specific residue"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-27T14:05:39.304Z"}}],"regions_counter":4,"released":"2024_06","sequence":"MSFLQNFHISPGQTIRSTRGFKWNTANAANNAGSVSPTKATPHNNTINGNNNNANTINNRADFTNNPVNGYNESDHGRMSPVLTTPKRHAPPPEQLQNVTDFNYTPSHQKPFLQPQAGTTVTTHQDIKQIVEMTLGSEGVLNQAVKLPRGEDENEWLAVHCVDFYNQINMLYGSITEFCSPQTCPRMIATNEYEYLWAFQKGQPPVSVSAPKYVECLMRWCQDQFDDESLFPSKVTGTFPEGFIQRVIQPILRRLFRVYAHIYCHHFNEILELNLQTVLNTSFRHFCLFAQEFELLRPADFGPLLELVMELRDR","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.3821656050955414,"disorder_content":0.07643312101910828,"disprot_consensus":{"full":[{"start":86,"end":97,"type":"D"},{"start":114,"end":125,"type":"D"}],"Structural state":[{"start":86,"end":97,"type":"D"},{"start":114,"end":125,"type":"D"}],"Disorder function":[{"start":86,"end":97,"type":"F"},{"start":114,"end":125,"type":"F"}]}},{"disprot_id":"DP03996","acc":"C0IR59","creator":"ldobson","date":"2023-03-20T10:15:54.498Z","features":{"pfam":[{"id":"PF02430","name":"Apical membrane antigen 1","start":99,"end":503}],"gene3D":[]},"genes":[],"length":606,"name":"Apical membrane antigen 1","ncbi_taxon_id":32595,"organism":"Babesia divergens","regions":[{"start":173,"end":193,"reference_id":"23169033","reference_source":"pmid","reference_html":"Babesia divergens and Neospora caninum apical membrane antigen 1 structures reveal selectivity and plasticity in apicomplexan parasite host cell invasion. <i> Tonkin ML, Crawford J, Lebrun ML, Boulanger MJ. </i> Protein Sci, 2013","date":"2023-04-26T06:51:36.072Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4APM"}],"region_id":"DP03996r001","statement":[{"text":"The final model of BdAMA1 incorporates residue 93 through 510, with two apical surface loops and a portion of the DII loop disordered. ","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5288834"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:175"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-27T14:06:47.257Z"}},{"start":258,"end":271,"reference_id":"23169033","reference_source":"pmid","reference_html":"Babesia divergens and Neospora caninum apical membrane antigen 1 structures reveal selectivity and plasticity in apicomplexan parasite host cell invasion. <i> Tonkin ML, Crawford J, Lebrun ML, Boulanger MJ. </i> Protein Sci, 2013","date":"2023-04-26T06:51:46.992Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4APM"}],"region_id":"DP03996r002","statement":[{"text":"The final model of BdAMA1 incorporates residue 93 through 510, with two apical surface loops and a portion of the DII loop disordered. ","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5288834"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:175"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-27T14:06:46.664Z"}},{"start":353,"end":391,"reference_id":"23169033","reference_source":"pmid","reference_html":"Babesia divergens and Neospora caninum apical membrane antigen 1 structures reveal selectivity and plasticity in apicomplexan parasite host cell invasion. <i> Tonkin ML, Crawford J, Lebrun ML, Boulanger MJ. </i> Protein Sci, 2013","date":"2023-04-26T06:52:04.614Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4APM"}],"region_id":"DP03996r003","statement":[{"text":"The final model of BdAMA1 incorporates residue 93 through 510, with two apical surface loops and a portion of the DII loop disordered. ","type":"Results"},{"text":"The tip of the BdAMA1 DII loop is disordered [Fig. 2(B top)], which is not surprising given that the corresponding region is completely disordered in PvAMA1,45 only partially modeled in PfAMA1,43 and displaced from the apical groove in Tg/PfAMA1 upon Tg/PfRON2 binding.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5288834"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:175"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-27T14:06:48.394Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MEATTTAKTGIWKKYLTLVVPILCVVILSGEVVPTEAAFHIRENEPKRRTSRRDGGRSSRRQTTNSRLSADDDDSDDGDDSDRPRGRQQSSKSTPKDIWGRYMAKFDLAKSHGSGIYVDLGGTERVGATQHRMPTGKCPVMGKVINLGNNADFLNRISAENPQDRGLAFPDTAVAVTRNSNARNRAAAEKTEIILSPVSAADLVRWGYDGNDVANCAEYAGNIIPASDTATKYRYPCVYDAKEEMCHILFTPMQYNRGSRYCDNDGSQDEGTSSLLCMEPMKSGIDAHLYYGSSRVDKKWEENCPMYPVKDAIFGRGANGSCVAIESAFEEFTRDAEECSALMFENAAADLEIDEEADNFDELKTLSDGLRNIKASKIAQALFSPIAKAGTSAKNSKGVGMNWANYDSNTGLCRVIEETPNCLIIDAGSFAMTAVGSPLEQDAVPFPCDIVTNGYIEPRPRSRHRNTTPIFEVTTALSREALKCSKYVHEKYSESCGTYYYCSEEKPSSWAFWRNLDWKRVAKYVMSLIAIAILYMAIHWTYKRLWTTKAKPESDEYERFMSKYDYDEGIHTKGHMDQQLRSDAYVWGEAAARPSDVTPVHLSKVQ","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Piroplasmida","Babesiidae","Babesia"],"alphafold_very_low_content":0.297029702970297,"disorder_content":0.12211221122112212,"disprot_consensus":{"full":[{"start":173,"end":193,"type":"D"},{"start":258,"end":271,"type":"D"},{"start":353,"end":391,"type":"D"}],"Structural state":[{"start":173,"end":193,"type":"D"},{"start":258,"end":271,"type":"D"},{"start":353,"end":391,"type":"D"}]}},{"disprot_id":"DP03997","acc":"A0A3Q7EK40","creator":"ldobson","date":"2023-03-20T10:36:27.684Z","features":{"pfam":[{"id":"PF00931","name":"NB-ARC domain","start":206,"end":375},{"id":"PF18052","name":"Rx N-terminal domain","start":50,"end":136},{"id":"PF23559","name":"Disease resistance protein Winged helix domain","start":461,"end":530},{"id":"PF23598","name":"Leucine-rich repeat region","start":580,"end":909}],"gene3D":[]},"genes":[],"length":932,"name":"NB-ARC domain-containing protein","ncbi_taxon_id":4081,"organism":"Solanum lycopersicum","regions":[{"start":275,"end":287,"reference_id":"31461469","reference_source":"pmid","reference_html":"Structural and biochemical studies of an NB-ARC domain from a plant NLR immune receptor. <i> Steele JFC, Hughes RK, Banfield MJ. </i> PLoS One, 2019","date":"2023-04-28T11:44:24.535Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6S2P"}],"region_id":"DP03997r001","statement":[{"text":"The initial autobuilding placed 171 residues in 15 fragments. Iterative manual rebuilding and refinement resulted in a final structure consisting of 252 of a total 346 residues present in the expressed protein construct. Several regions of the protein could not be modelled due to discontinuous electron density, including much of the ARC1 subdomain, and the solvent-exposed ɑ-helices of the NB domain.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T16:14:15.661Z"}},{"start":374,"end":391,"reference_id":"31461469","reference_source":"pmid","reference_html":"Structural and biochemical studies of an NB-ARC domain from a plant NLR immune receptor. <i> Steele JFC, Hughes RK, Banfield MJ. </i> PLoS One, 2019","date":"2023-04-28T11:47:33.708Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6S2P"}],"region_id":"DP03997r002","statement":[{"text":"The initial autobuilding placed 171 residues in 15 fragments. Iterative manual rebuilding and refinement resulted in a final structure consisting of 252 of a total 346 residues present in the expressed protein construct. Several regions of the protein could not be modelled due to discontinuous electron density, including much of the ARC1 subdomain, and the solvent-exposed ɑ-helices of the NB domain.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T16:14:17.528Z"}},{"start":416,"end":435,"reference_id":"31461469","reference_source":"pmid","reference_html":"Structural and biochemical studies of an NB-ARC domain from a plant NLR immune receptor. <i> Steele JFC, Hughes RK, Banfield MJ. </i> PLoS One, 2019","date":"2023-04-28T11:43:57.668Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6S2P"}],"region_id":"DP03997r003","statement":[{"text":"The initial autobuilding placed 171 residues in 15 fragments. Iterative manual rebuilding and refinement resulted in a final structure consisting of 252 of a total 346 residues present in the expressed protein construct. Several regions of the protein could not be modelled due to discontinuous electron density, including much of the ARC1 subdomain, and the solvent-exposed ɑ-helices of the NB domain.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T16:14:18.583Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MIIYPSQLSKMQTNCLHNTHFSSSSEHNSLLLQEINRKKKKENNMVDVGVEFLLENLKQLVLDNVELIGGAKDEIENLRDDLSEFNAFLKQAAMVRSENPVLKELVRSIRKVVNRAEDAVDKFVIEAKVHKDKGFKGVFDKPGHYRRVRDAAVEIKGIRDKMREIRQNKAHGLQALLQDHDDSISRGGEERQPPVVEEDDVVGFDDEAQTVIDRLLEGSGDLEVIPVVGMPGLGKTTLATKIFKHPKIEYEFFTRLWLYVSQSYKTRELYLNIISKFTGNTKHCRDMSEKDLALKVQEILEEGGKYLIVLDDVWSTDAWDRIKIAFPKNDKGNRVLLTTRDHRVARYCNRSPHDLKFLTDEESWILLEKRAFHKAKCLPELETNGKSIARKCKGLPLAIVVIAGALIGKSKTIKEWEQVDQSVGEHFINRDQPNSCDKLVRMSYDVLPYDWKACFLYFGTFPRGYLIPARKLIRLWIAEGFIQYRGDLSPECKAEEYLNELVNRNLVMVMQRTVDGQIKTCRVHDMLYEFCWQEATTEENLFHEVKFGGEQSVREVSTHRRLCIHSSVVEFISKKPSGEHVRSFLCFSPEKIDTPPTVSANISKAFPLLRVFDTESIKINRFCKEFFQLYHLRYIAFSFDSIKVIPKHVGELWNVQTLIVNTQQINLDIQADILNMPRLRHLLTNTSAKLPALANPKTSKTTLVNQSLQTLSTIAPESCTEYVLSRAPNLKKLGIRGKIAKLMEPSQSVLLNNVKRLQFLENLKLINVGQIDQTQLRLPPASIFPTKLRKLTLLDTWLEWDDMSVLKQLENLQVLKLKDNAFKGENWELNDGGFPFLQVLCIERANLVSWNASGDHFPRLKHLHISCDKLEKIPIGLADICSLQVMDLRNSTKSAAKSAREIQAKKNKLQPAKSQKFELSVFPPDSDVQTAS","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","lamiids","Solanales","Solanaceae","Solanoideae","Solaneae","Solanum","Solanum subgen. Lycopersicon"],"alphafold_very_low_content":0.12875536480686695,"disorder_content":0.05472103004291846,"disprot_consensus":{"full":[{"start":275,"end":287,"type":"D"},{"start":374,"end":391,"type":"D"},{"start":416,"end":435,"type":"D"}],"Structural state":[{"start":275,"end":287,"type":"D"},{"start":374,"end":391,"type":"D"},{"start":416,"end":435,"type":"D"}]}},{"disprot_id":"DP03998","acc":"O25119","creator":"ldobson","date":"2023-03-20T13:04:20.785Z","features":{"pfam":[{"id":"PF01706","name":"FliG C-terminal domain","start":229,"end":334},{"id":"PF14841","name":"FliG middle domain","start":127,"end":200},{"id":"PF14842","name":"FliG N-terminal domain","start":15,"end":116}],"gene3D":[]},"genes":[{"name":{"value":"fliG","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AFV41574.1","url":"https://www.ebi.ac.uk/ena/browser/view/AFV41574.1"}}]},"olnNames":[{"value":"C694_01785"},{"value":"HP_0352"}]}],"length":343,"name":"Flagellar motor switch protein FliG","ncbi_taxon_id":85962,"organism":"Helicobacter pylori (strain ATCC 700392 / 26695)","regions":[{"start":86,"end":117,"reference_id":"22325779","reference_source":"pmid","reference_html":"Multiple conformations of the FliG C-terminal domain provide insight into flagellar motor switching. <i> Lam KH, Ip WS, Lam YW, Chan SO, Ling TK, Au SW. </i> Structure, 2012","date":"2023-03-20T13:06:29.854Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3USW"}],"region_id":"DP03998r001","statement":[{"text":"Residues 86–117 of the N-terminal domain, residues 197–203 of LoopC, residues 336–343 of the C terminus of HpFliGMC1, and residues 337–343 of HpFliGMC2 were disordered and thus were excluded from the structural models. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-10T16:18:33.210Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MATKLTPKQKAQLDELSMSEKIAILLIQVGEDTTGEILRHLDIDSITEISKQIVQLNGTDKQIGAAVLEEFFAIFQSNQYINTGGLEYARELLTRTLGSEEAKKVMDKLTKSLQTQKNFAYLGKIKPQQLADFIINEHPQTIALILAHMEAPNAAETLSYFPDEMKAEISIRMANLGEISPQVVKRVSTVLENKLESLTSYKIEVGGLRAVAEIFNRLGQKSAKTTLARIESVDNKLAGAIKEMMFTFEDIVKLDNFAIREILKVADKKDLSLALKTSTKDLTDKFLNNMSSRAAEQFVEEMQYLGAVKIKDVDVAQRKIIEIVQSLQEKGVIQTGEEEDVIE","taxonomy":["Bacteria","Pseudomonadota","Epsilonproteobacteria","Campylobacterales","Helicobacteraceae","Helicobacter"],"alphafold_very_low_content":0.037900874635568516,"disorder_content":0.09329446064139942,"disprot_consensus":{"full":[{"start":86,"end":117,"type":"D"}],"Structural state":[{"start":86,"end":117,"type":"D"}]}},{"disprot_id":"DP03999","acc":"Q8IL97","creator":"ldobson","date":"2023-03-20T13:08:01.674Z","features":{"pfam":[{"id":"PF01230","name":"HIT domain","start":32,"end":122}],"gene3D":[]},"genes":[{"orfNames":[{"value":"PF3D7_1436900","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CZU00067.1","url":"https://www.ebi.ac.uk/ena/browser/view/CZU00067.1"}}]}]}],"length":200,"name":"Bis(5'-adenosyl)-triphosphatase","ncbi_taxon_id":36329,"organism":"Plasmodium falciparum (isolate 3D7)","regions":[{"start":126,"end":174,"reference_id":"26472355","reference_source":"pmid","reference_html":"Gift from Nature: Cyclomarin A Kills Mycobacteria and Malaria Parasites by Distinct Modes of Action. <i> Bürstner N, Roggo S, Ostermann N, Blank J, Delmas C, Freuler F, Gerhartz B, Hinniger A, Hoepfner D, Liechty B, Mihalic M, Murphy J, Pistorius D, Rottmann M, Thomas JR, Schirle M, Schmitt EK. </i> Chembiochem, 2015","date":"2023-04-28T11:49:51.638Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5CS2"}],"region_id":"DP03999r001","statement":[{"text":"Interestingly, the long insertion is structurally not defined and is not represented in the X-ray structure (see Figure S2).","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:10772429"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T16:15:40.499Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MEKYKNILEKLEWYKNKSSEKYEFGIYEIDKREVFITTKYSYGFVNNKPLLPGHILLTTLKKKKHYNDLDIEEIIDINLLCNFMCYIMGNLFNTTDFSIAIQDGKEAGQTVDHVHIHIIPRKINDYKNNDNIYNDMNKINLGYGKNIICNSCNNTINVCSQNEIERNFKLEEFNTSIRSIEQMEEEANLIKSYINEKFSS","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"alphafold_very_low_content":0.06,"disorder_content":0.245,"disprot_consensus":{"full":[{"start":126,"end":174,"type":"D"}],"Structural state":[{"start":126,"end":174,"type":"D"}]}},{"disprot_id":"DP04000","acc":"Q9U7C3","creator":"ldobson","date":"2023-03-20T13:17:09.611Z","features":{"pfam":[{"id":"PF13432","name":"Tetratricopeptide repeat","start":355,"end":410},{"id":"PF13432","name":"Tetratricopeptide repeat","start":514,"end":567}],"gene3D":[]},"genes":[],"length":655,"name":"Peroxisome targeting signal 1 receptor PEX5","ncbi_taxon_id":5691,"organism":"Trypanosoma brucei","regions":[{"start":453,"end":473,"reference_id":"18598704","reference_source":"pmid","reference_html":"Structural insights into the recognition of peroxisomal targeting signal 1 by Trypanosoma brucei peroxin 5. <i> Sampathkumar P, Roach C, Michels PA, Hol WG. </i> J Mol Biol, 2008","date":"2023-05-24T17:18:48.423Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3CVL"},{"db":"PDB","id":"3CVP"}],"region_id":"DP04000r001","statement":[{"text":"All helices of the seven TPR motifs, with the exception of helix 4A of the “linker TPR4,” are well defined in our structures.","type":"Results"},{"text":"The five structures described in PMID: 18598704 are mapped to two different Uniprot entries, Q57W55 (3CV0, 3CVP, 3CVQ) and Q9U7C3 (3CVL, 3CVN), although the publication does refer to one protein. The differences between the two sequences are in amino acids 143 [T (Q57W55), A (Q9U7C3)], 158 [N (Q57W55), S (Q9U7C3)] and 163 [S (Q57W55), N (Q9U7C3)].","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys378Ala","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"Both structures"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu379Ala","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"Both structures"}]}],"sequence_construct":"GHMLQNNTDYPFEANNPYMYHENPMEEGLSMLKLANLAEAALAFEAVCQAAPEREEAWRSLGLTQAENEKDGLAIIALNHARMLDPKDIAVHAALAVSHTNEHNANAALASLRAWLLSQPQYEQLGSVNLQADVDIDDLNVQSEDFFFAAPNEYRECRTLLHAALEMNPNDAQLHASLGVLYNLSNNYDSAAANLRRAVELRPDDAQLWNKLGATLANGNRPQEALDAYNRALDINPGYVRVMYNMAVSYSNMSQYDLAAKQLVRAIYMQVGGTTPTGEASREATRSMWDFFRMLLNVMNRPDLVELTYAQNVEPFAKEFGLQSMLL","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O15648","statements":[{"type":"Curator statement","text":"PDB:3CVL"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-29T16:37:48.071Z"}},{"start":459,"end":473,"reference_id":"18598704","reference_source":"pmid","reference_html":"Structural insights into the recognition of peroxisomal targeting signal 1 by Trypanosoma brucei peroxin 5. <i> Sampathkumar P, Roach C, Michels PA, Hol WG. </i> J Mol Biol, 2008","date":"2023-05-24T17:33:01.296Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3CVN"},{"db":"PDB","id":"3CV0"},{"db":"PDB","id":"3CVQ"}],"region_id":"DP04000r002","statement":[{"text":"All helices of the seven TPR motifs, with the exception of helix 4A of the “linker TPR4,” are well defined in our structures. ","type":"Results"},{"text":"The five structures described in PMID: 18598704 are mapped to two different Uniprot entries, Q57W55 (3CV0, 3CVP, 3CVQ) and Q9U7C3 (3CVL, 3CVN), although the publication does refer to one protein. The differences between the two sequences are in amino acids 143 [T (Q57W55), A (Q9U7C3)], 158 [N (Q57W55), S (Q9U7C3)] and 163 [S (Q57W55), N (Q9U7C3)].","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:174"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P22512"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753","statements":[{"type":"Curator statement","text":"PDB:3CVQ"}]}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys378Ala","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"PDB: 3CVN and 3CV0"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu379Ala","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"PDB: 3CVN and 3CV0"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met411Ala","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"PDB:3CVQ"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys415Ala","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"PDB:3CVQ"}]}],"sequence_construct":"GHMLQNNTDYPFEANNPYMYHENPMEEGLSMLKLANLAEAALAFEAVCQAAPEREEAWRSLGLTQAENEKDGLAIIALNHARMLDPKDIAVHAALAVSHTNEHNANAALASLRAWLLSQPQYEQLGSVNLQADVDIDDLNVQSEDFFFAAPNEYRECRTLLHAALEMNPNDAQLHASLGVLYNLSNNYDSAAANLRRAVELRPDDAQLWNKLGATLANGNRPQEALDAYNRALDINPGYVRVMYNMAVSYSNMSQYDLAAKQLVRAIYMQVGGTTPTGEASREATRSMWDFFRMLLNVMNRPDLVELTYAQNVEPFAKEFGLQSMLL","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-29T16:37:47.558Z"}},{"start":600,"end":611,"reference_id":"18598704","reference_source":"pmid","reference_html":"Structural insights into the recognition of peroxisomal targeting signal 1 by Trypanosoma brucei peroxin 5. <i> Sampathkumar P, Roach C, Michels PA, Hol WG. </i> J Mol Biol, 2008","date":"2023-05-24T17:35:37.971Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3CVP"},{"db":"PDB","id":"3CVQ"}],"region_id":"DP04000r003","statement":[{"text":"No observable electron density for this region in the structures.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753","statements":[{"type":"Curator statement","text":"PDB:3CVQ"}]}],"sequence_construct":"GHMLQNNTDYPFEANNPYMYHENPMEEGLSMLKLANLAEAALAFEAVCQAAPEREEAWRSLGLTQAENEKDGLAIIALNHARMLDPKDIAVHAALAVSHTNEHNANAALASLRAWLLSQPQYEQLGSVNLQADVDIDDLNVQSEDFFFAAPNEYRECRTLLHAALEMNPNDAQLHASLGVLYNLSNNYDSAAANLRRAVELRPDDAQLWNKLGATLANGNRPQEALDAYNRALDINPGYVRVMYNMAVSYSNMSQYDLAAKQLVRAIYMQVGGTTPTGEASREATRSMWDFFRMLLNVMNRPDLVELTYAQNVEPFAKEFGLQSMLL","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys378Ala","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"PDB:3CVP"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu379Ala","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"PDB:3CVP"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met411Ala","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"PDB:3CVQ"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys415Ala","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"PDB:3CVQ"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-29T16:35:10.720Z"}}],"regions_counter":3,"released":"2023_06","sequence":"MDCGAGFALGQQLAKDALHMQGGVRPGTTGNVEQDALMTGMMVPPTGPMEDWAQHFAAHQHHHQQHQQMMMQRQHNDALMIQQQHRDMEEAFRASARAGAPQQANAGPLMMPPGPMMMAGGMAPMMHAGGFMMGGMPQMMPCAPMGMNMGMAPVATMSPATTNTVSGAREGATAVSSAAPGVVDLGGDSAWAEKLHQAEWGQDYKDVEVHTVEGSTAQTVEEHAKTSKFYEFMDKIRKKELLVDEDSGEVVQGPGPDPDVEADTEYLARLAAMEGINVPPSVMDHMQGQDGVQRGTDEDMEGMMGDDVYDPSADVEQWAQEYAQMQAMQERLQNNTDYPFEANNPYMYHENPMEEGLSMLKLANLAEAALAFEAVCQKEPEREEAWRSLGLTQAENEKDGLAIIALNHARMLDPKDIAVHAALAVSHTNEHNANAALASLRAWLLSQPQYEQLGSVNLQADVDIDDLNVQSEDFFFAAPNEYRECRTLLHAALEMNPNDAQLHASLGVLYNLSNNYDSAAANLRRAVELRPDDAQLWNKLGATLANGNRPQEALDAYNRALDINPGYVRVMYNMAVSYSNMSQYDLAAKQLVRAIYMQVGGTTPTGEASREATRSMWDFFRMLLNVMNRPDLVELTYAQNVEPFAKEFGLQSMLL","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Trypanosoma"],"dataset":["Neglected tropical diseases proteins"],"alphafold_very_low_content":0.416793893129771,"disorder_content":0.050381679389312976,"disprot_consensus":{"full":[{"start":453,"end":473,"type":"D"},{"start":600,"end":611,"type":"D"}],"Structural state":[{"start":453,"end":473,"type":"D"},{"start":600,"end":611,"type":"D"}]}},{"disprot_id":"DP04002","acc":"Q71RI2","creator":"eficho","date":"2023-03-20T14:52:05.640Z","features":{"pfam":[{"id":"PF02902","name":"Ulp1 protease family, C-terminal catalytic domain","start":319,"end":490}],"gene3D":[]},"genes":[{"name":{"value":"Semp2l2a","evidences":[{"code":"ECO:0000313","source":{"name":"MGI","id":"MGI:2667157","url":"http://www.informatics.jax.org/marker/MGI:2667157"}}]},"synonyms":[{"value":"AF366264","evidences":[{"code":"ECO:0000313","source":{"name":"MGI","id":"MGI:2667157","url":"http://www.informatics.jax.org/marker/MGI:2667157"}}]}]}],"length":499,"name":"SUMO-1-specific protease","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":201,"end":300,"reference_id":"28000315","reference_source":"pmid","reference_html":"The Mechanism of p53 Rescue by SUSP4. <i> Kim DH, Lee C, Lee SH, Kim KT, Han JJ, Cha EJ, Lim JE, Cho YJ, Hong SH, Han KH. </i> Angew Chem Int Ed Engl, 2017","date":"2023-06-16T15:40:49.797Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04002r001","statement":[{"text":"Figure 1 shows an interesting fact, namely that P4-201 is intrinsically disordered except for the p53 rescue motif forming segment.","type":"Article"},{"text":"Figure 1A shows the HSQC spectrum of the free state of P4-201 (residues 201-300 of SUSP4).","type":"Curator statement"}],"cross_refs":[{"db":"BMRB","id":"26961"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-16T19:27:55.293Z"}},{"start":263,"end":291,"reference_id":"28000315","reference_source":"pmid","reference_html":"The Mechanism of p53 Rescue by SUSP4. <i> Kim DH, Lee C, Lee SH, Kim KT, Han JJ, Cha EJ, Lim JE, Cho YJ, Hong SH, Han KH. </i> Angew Chem Int Ed Engl, 2017","date":"2023-05-18T14:45:03.057Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P23804","operator":null,"partner_start":3,"partner_end":109}],"region_id":"DP04002r002","statement":[{"text":"The SSP scores and chemical shift perturbation data (Figure 3) indicate that the\nfull p53 rescue motif peptide has a binding pattern and affinity for mdm2 similar to the long-turn peptide of p53 TAD identified previously.[6] The shorter 19-residue peptide without the N-terminal affinity enhancer exhibits a much weaker binding.","type":"Article"},{"text":"Results indicate that the NMR resonances of several hydrophobic residues in P4-201 are affected upon addition of mdm2(3–109) (Figure 1).","type":"Article"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T11:17:35.220Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MWQPKLPGLEMKPEASAIGQTRKYHDESGTEIESEALGQEPKRKCQDGSGMVFKEPGKAQKKTSQEPQDLELPREQPSKGQVRKPQGKTPKQLKPLELTEGPPEQAVTGRKPADGGKGHKRPYSVMEEDEQSPQKEKYGRLLQHLQCDQDVRSDQHRPHPILTNTWKIKGGESGDSHGSETTQRDREQSTVVALKECLSPEEREKWCSEEKCVTEKKGCVKGEGRRGNSLEPGTRAQIILDRGRGNSLLPNKMAVLAAEKKPLTDQEKGREMYQILVITEDIEKEIENALGPGPQEEILSSRFKLQISRGDIQTLENGQWLNDEVINFYMNLLVERNENQGYPALHVFSTFFYPMLKHSGYSSVKRWTRGINLFEKELILVPIHQNVHWSLVVIDLRKRSIVYLDSVGETGKSICETIFQYLQNESKTRRNIELDPLEWKQYSVTSEEIPLQQNGSDCGMFTCKYADYIARDQPVTFSQQRMPTFRKRMVWAILHSHLL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"alphafold_very_low_content":0.5210420841683366,"disorder_content":0.20040080160320642,"disprot_consensus":{"full":[{"start":201,"end":300,"type":"D"}],"Structural state":[{"start":201,"end":300,"type":"D"}],"Molecular function":[{"start":263,"end":291,"type":"F"}]}},{"disprot_id":"DP04003","acc":"P0C746","creator":"eficho","date":"2023-03-20T14:53:02.766Z","features":{"pfam":[{"id":"PF27831","name":"HTLV-1 basic zipper factor","start":10,"end":202}],"gene3D":[]},"genes":[{"name":{"value":"HBZ"}}],"length":209,"name":"HTLV-1 basic zipper factor","ncbi_taxon_id":11926,"organism":"Human T-cell leukemia virus 1 (strain Japan ATK-1 subtype A)","regions":[{"start":3,"end":77,"reference_id":"30232260","reference_source":"pmid","reference_html":"Structural basis for cooperative regulation of KIX-mediated transcription pathways by the HTLV-1 HBZ activation domain. <i> Yang K, Stanfield RL, Martinez-Yamout MA, Dyson HJ, Wilson IA, Wright PE. </i> Proc Natl Acad Sci U S A, 2018","date":"2023-06-16T15:42:46.113Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04003r001","statement":[{"text":"Far-UV circular dichroism (CD) and NMR 1H-15N heteronuclear single quantum coherence (HSQC) spectra show that the full-length and truncated HBZ AD constructs are almost entirely disordered in their free forms (SI Appendix, Fig. S1)","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-16T19:50:26.844Z"}},{"start":3,"end":77,"reference_id":"30232260","reference_source":"pmid","reference_html":"Structural basis for cooperative regulation of KIX-mediated transcription pathways by the HTLV-1 HBZ activation domain. <i> Yang K, Stanfield RL, Martinez-Yamout MA, Dyson HJ, Wilson IA, Wright PE. </i> Proc Natl Acad Sci U S A, 2018","date":"2023-06-16T15:41:55.294Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04003r002","statement":[{"text":"Far-UV circular dichroism (CD) and NMR 1H-15N heteronuclear single quantum coherence (HSQC) spectra show that the full-length and truncated HBZ AD constructs are almost entirely disordered in their free forms (SI Appendix, Fig. S1).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-16T19:50:24.895Z"}},{"start":3,"end":77,"reference_id":"30232260","reference_source":"pmid","reference_html":"Structural basis for cooperative regulation of KIX-mediated transcription pathways by the HTLV-1 HBZ activation domain. <i> Yang K, Stanfield RL, Martinez-Yamout MA, Dyson HJ, Wilson IA, Wright PE. </i> Proc Natl Acad Sci U S A, 2018","date":"2023-05-19T07:47:26.125Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6DMX"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P06876","operator":null,"partner_start":284,"partner_end":315},{"db":"UniProt","id":"P45481","operator":"and","partner_start":586,"partner_end":683}],"region_id":"DP04003r003","statement":[{"text":"To elucidate the structural basis for the interactions among the HBZ AD, KIX, and the transactivation domain of c-Myb (residues 284–315), we determined the crystal\nstructures of the ternary complexes KIX:c-Myb:HBZ (3–77) and KIX:c-Myb:HBZ (3–56) at 2.35 Å and 2.80 Å, respectively (SI Appendix, Table S1).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T12:33:03.851Z"}},{"start":3,"end":77,"reference_id":"30232260","reference_source":"pmid","reference_html":"Structural basis for cooperative regulation of KIX-mediated transcription pathways by the HTLV-1 HBZ activation domain. <i> Yang K, Stanfield RL, Martinez-Yamout MA, Dyson HJ, Wilson IA, Wright PE. </i> Proc Natl Acad Sci U S A, 2018","date":"2023-05-19T07:51:33.601Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6DMX"}],"region_id":"DP04003r004","statement":[{"text":"Surprisingly, the intrinsically disordered HBZ AD folds upon binding to form a single continuous a-helix, where the N-terminal (AD1) and C-terminal (AD2) subdomains each bind to one molecule of KIX.","type":"Introduction"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T12:32:16.904Z"}},{"start":33,"end":56,"reference_id":"30232260","reference_source":"pmid","reference_html":"Structural basis for cooperative regulation of KIX-mediated transcription pathways by the HTLV-1 HBZ activation domain. <i> Yang K, Stanfield RL, Martinez-Yamout MA, Dyson HJ, Wilson IA, Wright PE. </i> Proc Natl Acad Sci U S A, 2018","date":"2023-05-19T07:52:59.621Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04003r005","statement":[{"text":"The 1H-15N HSQC spectrum of fully bound 15N-labeled HBZ (33–56) shows increased dispersion in the 1H dimension compared with the free peptide, indicating folding of AD2 upon binding to KIX (SI Appendix, Fig. S4A).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T12:33:16.846Z"}}],"regions_counter":5,"released":"2023_12","sequence":"MVNFVSAGLFRCLPVSCPEDLLVEELVDGLLSLEEELKDKEEEEAVLDGLLSLEEESRGRLRRGPPGEKAPPRGETHRDRQRRAEEKRKRKKEREKEEEKQTAEYLKRKEEEKARRRRRAEKKAADVARRKQEEQERRERKWRQGAEKAKQHSARKEKMQELGIDGYTRQLEGEVESLEAERRKLLQEKEDLMGEVNYWQGRLEAMWLQ","taxonomy":["Viruses","Riboviria","Pararnavirae","Artverviricota","Revtraviricetes","Ortervirales","Retroviridae","Orthoretrovirinae","Deltaretrovirus"],"dataset":["Viral proteins"],"disorder_content":0.3588516746411483,"disprot_consensus":{"full":[{"start":3,"end":77,"type":"T"}],"Structural state":[{"start":3,"end":77,"type":"D"}],"Molecular function":[{"start":3,"end":77,"type":"F"}],"Structural transition":[{"start":3,"end":77,"type":"T"}]}},{"disprot_id":"DP04005","acc":"Q9WID3","creator":"eficho","date":"2023-03-20T14:55:46.152Z","features":{"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":1233,"end":1367},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":1404,"end":1513},{"id":"PF00680","name":"Viral RNA-dependent RNA polymerase","start":2324,"end":2738},{"id":"PF00767","name":"Potyvirus coat protein","start":2853,"end":3086},{"id":"PF00851","name":"Helper component proteinase","start":321,"end":758},{"id":"PF00863","name":"Peptidase family C4","start":2038,"end":2270},{"id":"PF01577","name":"Potyvirus P1 protease","start":60,"end":299},{"id":"PF08440","name":"Potyviridae polyprotein","start":1540,"end":1820},{"id":"PF13608","name":"Protein P3 of Potyviral polyprotein","start":772,"end":1207}],"gene3D":[]},"genes":[],"length":3088,"name":"Genome polyprotein","ncbi_taxon_id":52280,"organism":"Chilli veinal mottle virus","regions":[{"start":1849,"end":1870,"reference_id":"30138835","reference_source":"pmid","reference_html":"Mapping the domain of interaction of PVBV VPg with NIa-Pro: Role of N-terminal disordered region of VPg in the modulation of structure and function. <i> Sabharwal P, Srinivas S, Savithri HS. </i> Virology, 2018","date":"2023-08-26T21:02:59.251Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04005r001","statement":[{"text":"To further investigate the influence of disordered region of VPg on its secondary structure, the far-UV CD spectra of purified VPg and the truncated proteins were recorded. The CD profile of VPg (Fig. 5A) showed a negative peak at around 200 nm similar to that observed for IDPs (Rantalainen et al., 2009, Satheshkumar et al., 2005)with 11.53% α-helical content (Fig. 5A, inset) as per K2D2 analysis (Perez-Iratxeta and Andrade-Navarro, 2008). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-08-19T12:52:56.106Z"}},{"start":1849,"end":1870,"reference_id":"30138835","reference_source":"pmid","reference_html":"Mapping the domain of interaction of PVBV VPg with NIa-Pro: Role of N-terminal disordered region of VPg in the modulation of structure and function. <i> Sabharwal P, Srinivas S, Savithri HS. </i> Virology, 2018","date":"2023-08-26T21:03:42.821Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001164","ec_ontology":"ECO","ec_name":"co-sedimentation assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04005r002","statement":[{"text":"The f/f0 value between 1.2 and 1.5 is an indicative of a well folded protein, between 1.5 and 2.5 define an intrinsically disordered protein while that above 3 indicates a highly elongated protein (Erickson, 2009).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-08-19T12:52:57.941Z"}}],"regions_counter":2,"released":"2024_12","sequence":"MAAQVIFSYLKSGSGVTTDACRAQAMQFTFGSFTPGKVNWNTLSSAMIEEYETRQESFELACEKFRKERTDMRIVRRKETFQYSPKTKYQLKGARRKERKEEQERKFLASSDTIVARIVFPPEAMKVEAPVEPIRFPPVVVRKVRKQPRPNITRVSTGSFSLFIKELVNTCDDRQIPLEMIANKRERVHVRIRRFTPSHRCAQVKTLHHRGIYQNVDFECPIALKSLFGLIAQHAWKGQDVDELKISIGDSGLCIPHGKLIGRVLSGDSDFFTVRGRYGSLLIDSQAYLPKKIISRINHYSAGELFWKGFDREFKTHRTTPVIHAGMNTMNVEECGSVAAIVCQALMPCCRITCTVCAKANVDQGTSGLQERLIHSLETGIKELEDRYKSFPHAAQLLKGHLSSYKKPNPNHEATSKVQFLIGDRKEQPFSYILEVNEVLIRGGRATSEEFSRASDCLLELARFHKNRVESLKKGSLHLFRNKVTSKSHINPSLMCDNQLDANGNFIWGKRGYHAKRFFSNYFELIQPTDGYDKYVIRKFPNGTRKLATIGNLILSTNLDQLRKQLEGESIEAMPLTQQCVSKRYESFIHPCCCVTYDDGSPVLSEFKAPTKNHLVLGNTGDSKYLDLPAEISENLYIAKEGYCYVNIFLAMLVDVDEKDAKDFTKWVRDIIVQQLGQWPTMTDVALACYQLSVLFPSTRSAELPRILVDHKTMTMHVIDSFGSLTTGYHVLKANTTSQLILFASDTLESEMKMYRVGGEETQSIPGFKTRLMRSVYRPSVFEQLMIDEPLTLTLALASPTLLNEFYTNGSLYEAMEFVGHTQMPVRVAVTKILELAQKVNRAESIYEQASLISNHLSELHGIIDQMPCRSASICCVLEFLLTSQLDTECDGELNAIGFRTLKHKSLHIMEKIYKEDLRALWCELSWSEKLRFKLHVLRSRKQYIRDSREIISGTLKEALHCSTRFVQEKIVLIPTPLRYVSGKIGCGIAKVRKNVWSIIYGRAVHNFRDALRFIHTLAILSILLTVYTNIVDIKNKHKKMNLLHIEEQEMKIQSRINKHYNDLTLLHNSPPSEVEFIQYVREHDPSALAYWSTQEKSVDHQASKRPSEAKLEQIVAFVALMMMVFDTDRSDCVYKVLNKLRNVMGVVDNDAVNHQSLDTILENFDERDEMIEFEITAPDAKSIAYKSSTFQVWWDNQLALNNVISHYRTEGHFVEFTRDTSAQVASDIANSDMKDFLVRGAVGSGKSTGLPSALCKRGRVLLLEPTRPLAENVHAQLSASPFHLNPTLMMRNKSVFGSTPITVMTSGYALHYLANDAQRLKEFSFILFDECHVLDASAMAFKSLLVDREFEGKILKVSATPPGRETEFSTQYPVQLKTEEHLSFQQFVDAQGTGVNADVTSIADNILVYVSSYNEVDQLSKLLTDKKFKVTKVDGRTMKSGATEIKTVGSKHRKHFIVATNIIENGVTIDIEAVVDFGLKVSAVVDADLRMVRILKVHSIMEKNSALGRVGRTKPGCALRIGHTNKGVEAIPTMIANEAAFLCLIYGLPVMTAQVSTSLISNCTVQQARTMALFELPFYFTQDYVSADGSLHPAIHALLRIQLRESEILLNNFQYHTQQSASGCQCASTTNAPKQLDMDPDVKLSFYVKEVPEELYEKLWHCVQENKGDAGFKKLRTHNAAKIAHKLRTDDMAIQRTILLIDQLIANEMQKKEHFDSLVNANTSSLSFTLQSVSNLIRSRHARIFGANPSVLHAARAQLVEFNNLHSDEIHEVCHQYMPLRDHIIDCGAMETVMHQSTDGISKCLKLKGTWNGSLITRDVLIAAGVACGGAWMIYQYFIDNERVDHQAQKKNKRQKQKLKFRDAHDQKVGRIIVDDDSGAVEHFFGSAYTKKGKSKGKTHGMGKKNRRFVNMYGFDPTEYSFIRFVDPVTGEMLDESVMADVMLVQEHFNDLRFEYLGDDKIESARLYSNPGIQAYFVKDKVSPVLKVDLTQHVPLKVCDNSSTIAGFPEREGEFRQTGQATKVNYDELPSREGVEHEARSLNRGLRDHNQVSKLICKLENDSDDCVTSIHGVGFGSIIITNRHLLKRNNGTLRVKTAHGDFKVANTKEMKVFPVEKHDILLIRLPKDFPPFPVKSKFREPKVNDSICLVGTNFQEKFLSSLISADSTTSPVSGSKFWRHWIDTKDGHCGLPLVARDDGAIVGFHSLTSINTEQNYFAAVPEAFMELIAQVETLEWRKSWVYNPNEIGWGSLKLKSDQPTGMFKIEKLIEDIQSAFVREQASDKWLYAQFQGFLKAVPKSESQLVPKHIVKGPCPLFHLYLSTHREARQFFQPFMGAYGKSRLNRIAYAKDILKYSTEIEVGKVDTCALELPVDDVIADLHAVKFDTCNYVTDEEEIFQSLNMKAAVGALYKGKKREYFETYTQQDKERILFESCLRLYKGNLGVWNGSIKAELRPIEKVRANKTRTFTAAPLDTLLAGKVCVDDFNNQFYSKHTLAPWSVGISKFSGGWDRLLRKLPDGWIYCSADGSRFDSSLTPYLINAVASIRLKFMEPWGIGEQMLMRNLYAEIIYTPILTADGTIVKKSKGNNSGQPSTVVDNTLMVLVAMKYSLRRLGIIIRIKNDRGVFFANGDDLIVSVPPSDEWILDSLQDRSSELGLSYDFNERTTDRSELWFMSHQGILIENQYIPKLEPERIVSILEWDRAEQPEHRLEAICASMIEAWGHKELLYEIRLFYKWVIEQAPYSQIVSEGKAPYISETALRCLNMSEHGENDINPYLRALIEGAKREELDDDGGEVAHQAGESVDAGSVKGEDSSSKSADKQATEKKNKVSGQAQPQSRQSEMEVPQVRDRDVNVGTSGTFTIPRLKGIFSKLTIPKVKTKAVVNLEHLLDYAPDQIHLSNTRALQSQFASWYEGVKNDYDVTDEQMQIILNGLMVWCIENGTSPNINGYWVMMDGDEQVEYPIKPLIDHAKPSFRQIMAHFSNLAEAYIEKRNSEKPYMPRYGLQRNLTDMSLARYAFDLYEMTSKTPVRAREAHIQMKAAALRGVSNRMFGLDGRVGTQEEDTERHTAEDVNRNMHNLLGVRGL","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Stelpaviricetes","Patatavirales","Potyviridae","Potyvirus"],"dataset":["Viral proteins"],"disorder_content":0.007124352331606218,"disprot_consensus":{"full":[{"start":1849,"end":1870,"type":"D"}],"Structural state":[{"start":1849,"end":1870,"type":"D"}]}},{"disprot_id":"DP04006","acc":"Q9RV58","creator":"eficho","date":"2023-03-20T14:57:15.540Z","features":{"pfam":[],"gene3D":[]},"genes":[{"olnNames":[{"value":"DR_1172"}]}],"length":298,"name":"Protein DR_1172","ncbi_taxon_id":243230,"organism":"Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)","regions":[{"start":104,"end":245,"reference_id":"31012266","reference_source":"pmid","reference_html":"Functional assessment of hydrophilic domains of late embryogenesis abundant proteins from distant organisms. <i> Liu Y, Zhang H, Han J, Jiang S, Geng X, Xue D, Chen Y, Zhang C, Zhou Z, Zhang W, Chen M, Lin M, Wang J. </i> Microb Biotechnol, 2019","date":"2023-05-19T13:42:57.432Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006200","ec_ontology":"ECO","ec_name":"circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04006r001","statement":[{"text":"We compared four different HD orthologs from distant organisms: (i) DrHD from the extremophilic bacterium Deinococcus radiodurans; (ii) CeHD from the nematode Caenorhabditis elegans; (iii) YlHD from the yeast Yarrowia lipolytica; and (iv) BnHD from the plant Brassica napus. Circular dichroism spectroscopy showed that all four HDs were intrinsically disordered in phosphate buffer and\nthen folded into a-helical structures with the addition of glycerol or trifluoroethanol.","type":"Article"},{"text":"The residue boundaries of the investigated protein constructs were taken from Table 1 column 5.","type":"Curator statement"},{"text":"The proteins were analysed by far-UV circular dichroism (CD) spectroscopy. The spectra of all four HDs had a negative peak at 198 nm in phosphate buffer, indicating that DrHD, CeHD, BnHD and YlHD are natively unstructured in solution (Fig. 1A).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T12:53:08.714Z"}},{"start":104,"end":245,"reference_id":"31012266","reference_source":"pmid","reference_html":"Functional assessment of hydrophilic domains of late embryogenesis abundant proteins from distant organisms. <i> Liu Y, Zhang H, Han J, Jiang S, Geng X, Xue D, Chen Y, Zhang C, Zhou Z, Zhang W, Chen M, Lin M, Wang J. </i> Microb Biotechnol, 2019","date":"2023-05-19T13:47:20.301Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04006r002","statement":[{"text":"However, according to the SDS-PAGE results, the HDs migrated to a higher molecular mass due to their hydrophilic character, which is often used to identify IDPs (Tompa, 2002; Chakrabortee et al., 2010).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T12:48:05.972Z"}},{"start":104,"end":245,"reference_id":"31012266","reference_source":"pmid","reference_html":"Functional assessment of hydrophilic domains of late embryogenesis abundant proteins from distant organisms. <i> Liu Y, Zhang H, Han J, Jiang S, Geng X, Xue D, Chen Y, Zhang C, Zhou Z, Zhang W, Chen M, Lin M, Wang J. </i> Microb Biotechnol, 2019","date":"2023-05-19T14:00:10.654Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0044183","term_name":"protein folding chaperone","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P13491","operator":null,"partner_start":1,"partner_end":332}],"region_id":"DP04006r003","statement":[{"text":"It was clear to see that LDH marked aggregation subjected to cycles of desiccation (Fig. 3A), addition of HDs can significantly decrease the aggregation of LDH compared to BSA mixture and negative control (only LDH), respectively, even after four cycles of desiccation, suggesting their aggregation-preventing ability. Noticeably, DrHD displayed the better job inhibiting the aggregation of LDH. The enzymatic activity of LDH was impaired under the dry conditions, especially after four cycles, and < 20% of the undried LDH activity was retained. Conspicuously, the loss of LDH enzymatic activity was significantly neutralized with the additional HDs and BSA. DrHD and CeHD performed excellently, preserving up to 60% of the LDH activity, and even BnHD protected up to 40% of the activity, which was slightly higher than the 38% protected by BSA (Fig. 3B). The HD protection of LDH enzymatic activity under oxidation stress followed a trend similar to that in desiccation (Fig. S5). DrHD and CeHD clearly exhibited the strongest protection ability (over 65% of LDH activity retained) of the HDs.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T12:54:58.318Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MFERDEHHFPVKRLLLLGALVGAGAYYLSREQNRKALDAKLAELGLKDAAQDVGSSVTKGWEKTKDAAQNAGSVIADKAQDVAGEVKSAVAGATAEIKDAGKEVADTAKDAGQNVGQNVKREAADLADQAKDKAQDVKADVSKAADQAKDKAQDVAQNVQAGAQQAAANVKDKVQDVKADASKAADQAKDKAQDVAQNVKQGAQQAASDAKDKVQDVKADASRAADQAKDKAQDVAQNVKQSAQDAKTDVDAKAKSWAFDLRTDAEAGKQGGQTGSTTNNAGTAGNTGMTGNTNTRKN","taxonomy":["Bacteria","Deinococcus-Thermus","Deinococci","Deinococcales","Deinococcaceae","Deinococcus"],"alphafold_very_low_content":0.7080536912751678,"disorder_content":0.47651006711409394,"disprot_consensus":{"full":[{"start":104,"end":245,"type":"D"}],"Structural state":[{"start":104,"end":245,"type":"D"}],"Molecular function":[{"start":104,"end":245,"type":"F"}]}},{"disprot_id":"DP04007","acc":"G5EFU3","creator":"eficho","date":"2023-03-20T14:58:21.558Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"lea-1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAB05543.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAB05543.1"}},{"code":"ECO:0000313","source":{"name":"WormBase","id":"K08H10.1a","url":"https://www.wormbase.org/db/seq/sequence?name=K08H10.1a;class=Transcript"}}]},"synonyms":[{"value":"lea","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAB69446.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAB69446.1"}}]}],"orfNames":[{"value":"CELE_K08H10.1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAB05543.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAB05543.1"}}]},{"value":"K08H10.1","evidences":[{"code":"ECO:0000313","source":{"name":"WormBase","id":"K08H10.1a","url":"https://www.wormbase.org/db/seq/sequence?name=K08H10.1a;class=Transcript"}}]}]}],"length":733,"name":"Ce-LEA","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":226,"end":702,"reference_id":"31012266","reference_source":"pmid","reference_html":"Functional assessment of hydrophilic domains of late embryogenesis abundant proteins from distant organisms. <i> Liu Y, Zhang H, Han J, Jiang S, Geng X, Xue D, Chen Y, Zhang C, Zhou Z, Zhang W, Chen M, Lin M, Wang J. </i> Microb Biotechnol, 2019","date":"2023-05-19T17:01:02.119Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04007r001","statement":[{"text":"We compared four different HD orthologs from distant organisms: (i) DrHD from the extremophilic bacterium Deinococcus radiodurans; (ii) CeHD from the nematode Caenorhabditis elegans; (iii) YlHD from the yeast Yarrowia lipolytica; and (iv) BnHD from the plant Brassica napus. Circular dichroism spectroscopy showed that all four HDs were intrinsically disordered in phosphate buffer and then folded into a-helical structures with the addition of glycerol or trifluoroethanol.","type":"Article"},{"text":"The proteins were analysed by far-UV circular dichroism (CD) spectroscopy. The spectra of all four HDs had a negative peak at 198 nm in phosphate buffer, indicating that DrHD, CeHD, BnHD and YlHD are natively unstructured in solution (Fig. 1A).","type":"Results"},{"text":"The residue boundaries of the investigated protein constructs were taken from Table 1 column 5.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T12:53:44.143Z"}},{"start":226,"end":702,"reference_id":"31012266","reference_source":"pmid","reference_html":"Functional assessment of hydrophilic domains of late embryogenesis abundant proteins from distant organisms. <i> Liu Y, Zhang H, Han J, Jiang S, Geng X, Xue D, Chen Y, Zhang C, Zhou Z, Zhang W, Chen M, Lin M, Wang J. </i> Microb Biotechnol, 2019","date":"2023-05-19T17:01:57.891Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04007r002","statement":[{"text":"However, according to the SDS-PAGE results, the HDs migrated to a higher molecular mass due to their hydrophilic character, which is often used to identify IDPs (Tompa, 2002; Chakrabortee et al., 2010).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T12:48:45.261Z"}},{"start":226,"end":702,"reference_id":"31012266","reference_source":"pmid","reference_html":"Functional assessment of hydrophilic domains of late embryogenesis abundant proteins from distant organisms. <i> Liu Y, Zhang H, Han J, Jiang S, Geng X, Xue D, Chen Y, Zhang C, Zhou Z, Zhang W, Chen M, Lin M, Wang J. </i> Microb Biotechnol, 2019","date":"2023-05-19T17:04:22.294Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0044183","term_name":"protein folding chaperone","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P13491","operator":null,"partner_start":1,"partner_end":332}],"region_id":"DP04007r003","statement":[{"text":"It was clear to see that LDH marked aggregation subjected to cycles of desiccation (Fig. 3A), addition of HDs can significantly decrease the aggregation of LDH compared to BSA mixture and negative control (only LDH), respectively, even after four cycles of desiccation, suggesting their aggregation-preventing ability. Noticeably, DrHD displayed the better job inhibiting the aggregation of LDH. The enzymatic activity of LDH was impaired under the dry conditions, especially after four cycles, and < 20% of the undried LDH activity was retained. Conspicuously, the loss of LDH enzymatic activity was significantly neutralized with the additional HDs and BSA. DrHD and CeHD performed excellently, preserving up to 60% of the LDH activity, and even BnHD protected up to 40% of the activity, which was slightly higher than the 38% protected by BSA (Fig. 3B). The HD protection of LDH enzymatic activity under oxidation stress followed a trend similar to that in desiccation (Fig. S5). DrHD and CeHD clearly exhibited the strongest protection ability (over 65% of LDH activity retained) of the HDs.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T12:55:02.723Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MSFMDKVKDTANSAYESVENTAVGAKDGVVGAFNTVGEKIGGAYDSTKQYASDKVSAAGDYASEAGKKVGDAEDSMIQGAYDAKDSAKESASNAGNKISNAFTSLKDSITGDNAHKTGEALNDNYESVKESASEAADRLKEPAQNTADNAKDLANQTGEEMSDAFESVKQLTSDTAENAKENAHDAADTAKSYKDKAGEKASGILDSFKAHASDAKDSVENKASDAYNSAKDKAGDAWDSTKDAAGDAKDKTKSFTEKVGDKISGAYDSVKEKASDVADSFKAHSTDSKDNVENKAADAYNTAKDKASDAWDKTKDKAGEAKDKMGDAWDTTKDKAGDAWDTTKDKAGDGKGKAGDAWDTTKDKASDAWDTTKDKAGEAKDKMGEAWDHTKDKAGEAKDKASDAADDAQGKSKSMTEKIGDSISGAWESTKDTAVSAKDKTAEAAGKVGDSISGAYDTVKEKASDIADSFKAHSTDSKDNVENKAADAYNSAKDKASDAWDKTKDKAGDAKDKAADAWDTTKDKAGDAWDSTKDHAADAKDKASDAAGDAKDKSKSLTEKAGDAISGAYDSVKEKASDIADSFKAHSTNSKDNVENKASDAYNSAKDKASDAWDKTKDKAGEAKDKAGDAWDNTKDKAGNAWDSTKDKASDAWDTTKDKASDAKESAGDAADSAKDKSKSITETIGDKISGAYDSVKEKASDVADSFKAHSSDAQDTVEVSHHKYFNVFSSFE","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"alphafold_very_low_content":0.9781718963165075,"disorder_content":0.6507503410641201,"disprot_consensus":{"full":[{"start":226,"end":702,"type":"D"}],"Structural state":[{"start":226,"end":702,"type":"D"}],"Molecular function":[{"start":226,"end":702,"type":"F"}]}},{"disprot_id":"DP04008","acc":"Q8S8Z3","creator":"eficho","date":"2023-03-20T14:59:29.326Z","features":{"pfam":[{"id":"PF27970","name":"LEA protein 1/2/D7/Stress-induced protein KIN2","start":145,"end":196}],"gene3D":[]},"genes":[{"name":{"value":"ME-leaN4","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAB88877.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAB88877.1"}}]}}],"length":226,"name":"Late embryogenesis-abundant protein","ncbi_taxon_id":3708,"organism":"Brassica napus","regions":[{"start":42,"end":162,"reference_id":"31012266","reference_source":"pmid","reference_html":"Functional assessment of hydrophilic domains of late embryogenesis abundant proteins from distant organisms. <i> Liu Y, Zhang H, Han J, Jiang S, Geng X, Xue D, Chen Y, Zhang C, Zhou Z, Zhang W, Chen M, Lin M, Wang J. </i> Microb Biotechnol, 2019","date":"2023-05-19T17:01:20.277Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04008r001","statement":[{"text":"We compared four different HD orthologs from distant organisms: (i) DrHD from the extremophilic bacterium Deinococcus radiodurans; (ii) CeHD from the nematode Caenorhabditis elegans; (iii) YlHD from the yeast Yarrowia lipolytica; and (iv) BnHD from the plant Brassica napus. Circular dichroism spectroscopy showed that all four HDs were intrinsically disordered in phosphate buffer and then folded into a-helical structures with the addition of glycerol or trifluoroethanol.","type":"Article"},{"text":"The proteins were analysed by far-UV circular dichroism (CD) spectroscopy. The spectra of all four HDs had a negative peak at 198 nm in phosphate buffer, indicating that DrHD, CeHD, BnHD and YlHD are natively unstructured in solution (Fig. 1A).","type":"Results"},{"text":"The residue boundaries of the investigated protein constructs were taken from Table 1 column 5.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T12:53:16.600Z"}},{"start":42,"end":162,"reference_id":"31012266","reference_source":"pmid","reference_html":"Functional assessment of hydrophilic domains of late embryogenesis abundant proteins from distant organisms. <i> Liu Y, Zhang H, Han J, Jiang S, Geng X, Xue D, Chen Y, Zhang C, Zhou Z, Zhang W, Chen M, Lin M, Wang J. </i> Microb Biotechnol, 2019","date":"2023-05-19T17:02:20.690Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04008r002","statement":[{"text":"However, according to the SDS-PAGE results, the HDs migrated to a higher molecular mass due to their hydrophilic character, which is often used to identify IDPs (Tompa, 2002; Chakrabortee et al., 2010).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T12:48:22.449Z"}},{"start":42,"end":162,"reference_id":"31012266","reference_source":"pmid","reference_html":"Functional assessment of hydrophilic domains of late embryogenesis abundant proteins from distant organisms. <i> Liu Y, Zhang H, Han J, Jiang S, Geng X, Xue D, Chen Y, Zhang C, Zhou Z, Zhang W, Chen M, Lin M, Wang J. </i> Microb Biotechnol, 2019","date":"2023-05-19T17:05:24.293Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0044183","term_name":"protein folding chaperone","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","region_id":"DP04008r003","statement":[{"text":"It was clear to see that LDH marked aggregation subjected to cycles of desiccation (Fig. 3A), addition of HDs can significantly decrease the aggregation of LDH compared to BSA mixture and negative control (only LDH), respectively, even after four cycles of desiccation, suggesting their aggregation-preventing ability. Noticeably, DrHD displayed the better job inhibiting the aggregation of LDH. The enzymatic activity of LDH was impaired under the dry conditions, especially after four cycles, and < 20% of the undried LDH activity was retained. Conspicuously, the loss of LDH enzymatic activity was significantly neutralized with the additional HDs and BSA. DrHD and CeHD performed excellently, preserving up to 60% of the LDH activity, and even BnHD protected up to 40% of the activity, which was slightly higher than the 38% protected by BSA (Fig. 3B). The HD protection of LDH enzymatic activity under oxidation stress followed a trend similar to that in desiccation (Fig. S5). DrHD and CeHD clearly exhibited the strongest protection ability (over 65% of LDH activity retained) of the HDs.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T12:55:00.645Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MASNQQSYKAGETKRKTQEKTGQAMGAMRDKAEEGKDKTSQTAQKAQQKAQETAQAAKDKTSQAAQTTQQKAQETAQAAKDKTSQAAQTTQQKAHETTQSSKEKTSQAAQTAQEKARETKDKTGSYLSETGEAVKQKAQDAAQYTKETAQNAAQYTKETAEAGKDKTGGFLSQTGEHVKQMAMGAADAVKHTFGMATEEEDREHYPGTTTCTTQSTDPTRHTYERK","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Brassiceae","Brassica"],"alphafold_very_low_content":0.7831858407079646,"disorder_content":0.5353982300884956,"disprot_consensus":{"full":[{"start":42,"end":162,"type":"D"}],"Structural state":[{"start":42,"end":162,"type":"D"}],"Molecular function":[{"start":42,"end":162,"type":"F"}]}},{"disprot_id":"DP04009","acc":"O64820","creator":"eficho","date":"2023-03-20T15:00:43.818Z","features":{"pfam":[{"id":"PF10714","name":"Late embryogenesis abundant protein 18","start":4,"end":89}],"gene3D":[]},"genes":[{"orfNames":[{"value":"AT2G23110","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AEC07411.1","url":"https://www.ebi.ac.uk/ena/browser/view/AEC07411.1"}}]},{"value":"F21P24.17","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AEC07411.1","url":"https://www.ebi.ac.uk/ena/browser/view/AEC07411.1"}}]},{"value":"F21P24_17","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AEC07411.1","url":"https://www.ebi.ac.uk/ena/browser/view/AEC07411.1"}}]}],"olnNames":[{"value":"At2g23110","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAX55122.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAX55122.1"}}]},{"value":"At2g23110/F21P24.17","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAK62434.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAK62434.1"}}]}]}],"length":92,"name":"At2g23110","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":1,"end":92,"reference_id":"22155233","reference_source":"pmid","reference_html":"Influence of drying on the secondary structure of intrinsically disordered and globular proteins. <i> Hundertmark M, Popova AV, Rausch S, Seckler R, Hincha DK. </i> Biochem Biophys Res Commun, 2012","date":"2023-05-18T13:20:34.485Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04009r001","statement":[{"text":" In solution the spectrum of LEA15 (Fig. 2A) showed typical features of a largely unstructured protein with a well defined minimal ellipticity at around 200 nm.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-14T12:57:36.696Z"}},{"start":1,"end":92,"reference_id":"22155233","reference_source":"pmid","reference_html":"Influence of drying on the secondary structure of intrinsically disordered and globular proteins. <i> Hundertmark M, Popova AV, Rausch S, Seckler R, Hincha DK. </i> Biochem Biophys Res Commun, 2012","date":"2023-06-16T15:43:45.533Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04009r003","statement":[{"text":"The Amide I peaks from all hydrated proteins were situated between 1646 and 1650 cm−1 in agreement with the CD spectra indicating them to be largely unstructured.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T08:59:26.031Z"}}],"regions_counter":4,"released":"2024_06","sequence":"MEDQKKPPTTEQEVKEVKNDDLESIKTPYLDYDNLEDYKMKGYGAQGHQEPKLGMGGGATDAPTPSGGLGRGGGAASTDLSSTDAINRQGVP","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"alphafold_very_low_content":0.2391304347826087,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":92,"type":"D"}],"Structural state":[{"start":1,"end":92,"type":"D"}]}},{"disprot_id":"DP04010","acc":"Q94K79","creator":"eficho","date":"2023-03-20T15:01:08.632Z","features":{"pfam":[{"id":"PF10714","name":"Late embryogenesis abundant protein 18","start":11,"end":76}],"gene3D":[]},"genes":[{"olnNames":[{"value":"At2g23120","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAK44026.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAK44026.1"}}]}]}],"length":83,"name":"Uncharacterized protein At2g23120","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":1,"end":83,"reference_id":"22155233","reference_source":"pmid","reference_html":"Influence of drying on the secondary structure of intrinsically disordered and globular proteins. <i> Hundertmark M, Popova AV, Rausch S, Seckler R, Hincha DK. </i> Biochem Biophys Res Commun, 2012","date":"2023-06-16T19:07:31.664Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04010r001","statement":[{"text":"In solution the spectrum of LEA15 (Fig. 2A) showed typical features of a largely unstructured protein with a well defined minimal ellipticity at around 200 nm.\nAfter drying the spectrum was massively changed, indicating a gain of structure. However, the CD spectrum of LEA15 did not exhibit the double minimum at 208 and 222 nm characteristic of predominantly a-helical proteins. The CD spectra of the other investigated LEA proteins, both in the hydrated and dry state, were\nsimilar to those presented in Fig. 2A and are therefore not shown.","type":"Results"},{"text":"Secondary structure estimates derived from these CD spectra indicated that the hydrated LEA proteins were between 61% (LEA17) and 68% (LEA20) unstructured (Fig. 2B). In addition, they contained around 20% b-sheet and only a negligible fraction of a-helices.","type":"Results"},{"text":"Based on the statement of the authors and figure 2B, the structural composition of the five investigated LEA proteins are similar to each other, both in the hydrated and dry state.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T09:01:09.429Z"}},{"start":1,"end":83,"reference_id":"22155233","reference_source":"pmid","reference_html":"Influence of drying on the secondary structure of intrinsically disordered and globular proteins. <i> Hundertmark M, Popova AV, Rausch S, Seckler R, Hincha DK. </i> Biochem Biophys Res Commun, 2012","date":"2023-06-16T15:44:38.437Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04010r004","statement":[{"text":"The Amide I peaks from all hydrated proteins were situated between 1646 and 1650 cm−1 in agreement with the CD spectra indicating them to be largely unstructured.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T09:00:18.710Z"}}],"regions_counter":4,"released":"2024_06","sequence":"MEAGKTPPTTTTTTEKKTEQVKDNDLPTDSPYMATGTLEDHKLKAYGAEGHQEPTPGLGGGSTDAPTPSGDAPAATTTDAKAP","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"alphafold_very_low_content":0.2891566265060241,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":83,"type":"D"}],"Structural state":[{"start":1,"end":83,"type":"D"}]}},{"disprot_id":"DP04012","acc":"Q02973","creator":"eficho","date":"2023-03-20T15:01:56.805Z","features":{"pfam":[{"id":"PF00477","name":"Small hydrophilic plant seed protein","start":2,"end":59}],"gene3D":[]},"genes":[{"name":{"value":"EM6"},"synonyms":[{"value":"ATEM6"},{"value":"D19H"}],"orfNames":[{"value":"T7M7.23"}],"olnNames":[{"value":"At2g40170"}]}],"length":92,"name":"Em-like protein GEA6","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":1,"end":92,"reference_id":"22155233","reference_source":"pmid","reference_html":"Influence of drying on the secondary structure of intrinsically disordered and globular proteins. <i> Hundertmark M, Popova AV, Rausch S, Seckler R, Hincha DK. </i> Biochem Biophys Res Commun, 2012","date":"2023-06-16T19:08:19.313Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04012r001","statement":[{"text":"In solution the spectrum of LEA15 (Fig. 2A) showed typical features of a largely unstructured protein with a well defined minimal ellipticity at around 200 nm. After drying the spectrum was massively changed, indicating a gain of structure. However, the CD spectrum of LEA15 did not exhibit the double minimum at 208 and 222 nm characteristic of predominantly a-helical proteins. The CD spectra of the other investigated LEA proteins, both in the hydrated and dry state, were similar to those presented in Fig. 2A and are therefore not shown.","type":"Results"},{"text":"Secondary structure estimates derived from these CD spectra indicated that the hydrated LEA proteins were between 61% (LEA17) and 68% (LEA20) unstructured (Fig. 2B). In addition, they contained around 20% b-sheet and only a negligible fraction of a-helices.","type":"Results"},{"text":"Based on the statement of the authors and figure 2B, the structural composition of the five investigated LEA proteins are similar to each other, both in the hydrated and dry state.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T09:04:08.178Z"}},{"start":1,"end":92,"reference_id":"22155233","reference_source":"pmid","reference_html":"Influence of drying on the secondary structure of intrinsically disordered and globular proteins. <i> Hundertmark M, Popova AV, Rausch S, Seckler R, Hincha DK. </i> Biochem Biophys Res Commun, 2012","date":"2023-06-16T15:46:21.378Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04012r003","statement":[{"text":"The Amide I peaks from all hydrated proteins were situated between 1646 and 1650 cm−1 in agreement with the CD spectra indicating them to be largely unstructured.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T09:04:09.545Z"}}],"regions_counter":4,"released":"2024_06","sequence":"MASQQEKKQLDERAKKGETVVPGGTGGKSFEAQQHLAEGRSRGGQTRKEQLGTEGYQQMGRKGGLSTGDKPGGEHAEEEGVEIDESKFRTKT","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"alphafold_very_low_content":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":92,"type":"D"}],"Structural state":[{"start":1,"end":92,"type":"D"}]}},{"disprot_id":"DP04014","acc":"Q9LL46","creator":"eficho","date":"2023-03-20T15:03:10.474Z","features":{"pfam":[{"id":"PF10714","name":"Late embryogenesis abundant protein 18","start":2,"end":81}],"gene3D":[]},"genes":[],"length":82,"name":"LEA-18","ncbi_taxon_id":3885,"organism":"Phaseolus vulgaris","regions":[{"start":1,"end":82,"reference_id":"25271167","reference_source":"pmid","reference_html":"A group 6 late embryogenesis abundant protein from common bean is a disordered protein with extended helical structure and oligomer-forming properties. <i> Rivera-Najera LY, Saab-Rincón G, Battaglia M, Amero C, Pulido NO, García-Hernández E, Solórzano RM, Reyes JL, Covarrubias AA. </i> J Biol Chem, 2014","date":"2023-09-14T14:54:21.364Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04014r001","statement":[{"text":"To test the disordered nature predicted for PvLEA6 protein, its secondary structure in aqueous solution at pH 8.0 (10 mM potassium phosphate) was explored by CD spectroscopy in the far-UV light. The spectrum showed a strong minimum ellipticity around 200 nm, indicative of a largely unordered conformation (Fig. 2B).","type":"Results"},{"text":"An alternative and likely explanation for the temperature induced changes in the rPvLEA6 far-UV CD spectra is the formation of secondary structure promoted by the increasing temperatures, which has been proposed to be driven by hydrophobic interactions and has also been reported for various IDPs (43, 44).","type":"Discussion"},{"text":"In this report, analysis by circular dichroism (CD) and nuclear magnetic resonance (NMR) shows the disordered structure of the PvLEA6 protein in aqueous solution, as well as the potential of this protein to acquire up to 40% α-helix.","type":"Introduction"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-10-09T13:57:59.902Z"}},{"start":1,"end":82,"reference_id":"25271167","reference_source":"pmid","reference_html":"A group 6 late embryogenesis abundant protein from common bean is a disordered protein with extended helical structure and oligomer-forming properties. <i> Rivera-Najera LY, Saab-Rincón G, Battaglia M, Amero C, Pulido NO, García-Hernández E, Solórzano RM, Reyes JL, Covarrubias AA. </i> J Biol Chem, 2014","date":"2023-09-14T14:53:31.676Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04014r002","statement":[{"text":"The low level of chemical shift dispersion apparent in the 1H dimension clustered between 7.7 and 8.5 ppm (Fig. 5A) was indicative of structural disordered state for this protein under native conditions in aqueous solution.","type":"Results"},{"text":"In this report, analysis by circular dichroism (CD) and nuclear magnetic resonance (NMR) shows the disordered structure of the PvLEA6 protein in aqueous solution, as well as the potential of this protein to acquire up to 40% α-helix.","type":"Introduction"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-10-09T13:57:53.048Z"}},{"start":1,"end":82,"reference_id":"25271167","reference_source":"pmid","reference_html":"A group 6 late embryogenesis abundant protein from common bean is a disordered protein with extended helical structure and oligomer-forming properties. <i> Rivera-Najera LY, Saab-Rincón G, Battaglia M, Amero C, Pulido NO, García-Hernández E, Solórzano RM, Reyes JL, Covarrubias AA. </i> J Biol Chem, 2014","date":"2023-08-26T20:56:17.411Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04014r003","statement":[{"text":"The differences between the molecular masses estimated by SDS-PAGE (see above) and gel filtration chromatography with those obtained by mass spectrometry suggested that oligomeric forms maintain the monomer structural disorder.","type":"Results"},{"text":"The first indications of the unstructured nature of PvLEA6 were observed during initial characterization of the protein. rPvLEA6 protein was produced and purified from E. coli, from which a highly pure native protein was obtained that migrated in SDS-PAGE with an apparent molecular mass of 14 kDa (Fig. 2A; see “Experimental Procedures” for details). The molecular mass and amino acid sequence of the purified rPvLEA protein were proven by LC-MS, showing a molecular mass of 8.76 kDa (data not shown), in agreement with informatic predictions, and the same amino acid sequence as that deduced from its open reading frame, as reported previously (18). Therefore, indicating that the difference in its molecular mass obtained by SDS-PAGE migration or by LC-MS is likely due to the absence of hydrophobic clusters and therefore a low interaction with SDS (Fig. 1), and it is consistent with its predicted structural disorder, which usually gives rise to large protein hydrodynamic dimensions (34).\n","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-09-11T16:24:14.119Z"}},{"start":1,"end":82,"reference_id":"25271167","reference_source":"pmid","reference_html":"A group 6 late embryogenesis abundant protein from common bean is a disordered protein with extended helical structure and oligomer-forming properties. <i> Rivera-Najera LY, Saab-Rincón G, Battaglia M, Amero C, Pulido NO, García-Hernández E, Solórzano RM, Reyes JL, Covarrubias AA. </i> J Biol Chem, 2014","date":"2026-01-07T16:57:16.609Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0042802","term_name":"identical protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005527","ec_ontology":"ECO","ec_name":"matrix-assisted laser desorption/ionization time-of-flight mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"ec_go":"EXP","region_id":"DP04014r004","statement":[{"text":"To have a more precise determination of the molecular mass of these rPvLEA6 oligomers, a cross-linked sample was subjected to MALDI-TOF-MS analysis. The spectrum, obtained only for protein molecules smaller than 50,000 Da, showed three peaks at 8760, 17,520, and 26,280 Da, corresponding to monomer, dimer, and trimer, respectively (Fig. 8C).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein or proteins.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"Q9LL46","operator":"and","partner_start":1,"partner_end":82}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-01-07T16:57:18.873Z"}},{"start":1,"end":82,"reference_id":"25271167","reference_source":"pmid","reference_html":"A group 6 late embryogenesis abundant protein from common bean is a disordered protein with extended helical structure and oligomer-forming properties. <i> Rivera-Najera LY, Saab-Rincón G, Battaglia M, Amero C, Pulido NO, García-Hernández E, Solórzano RM, Reyes JL, Covarrubias AA. </i> J Biol Chem, 2014","date":"2026-01-07T16:57:28.382Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0042802","term_name":"identical protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":1,"ec_go":"IPI","region_id":"DP04014r005","statement":[{"text":"The measurements (carried out in triplicate) yielded a Kd = 60 ± 20 μm and a dissociation enthalpy, ΔHd, = 1.0 ± 0.3 kcal/mol. This information allowed estimation of the following thermodynamic parameters for dimer formation (30 °C): ΔGa = −5.9 kcal/mol; ΔHa = −1.0 kcal/mol; and TΔSa = 4.9 kcal/mol, consistent with a low affinity, mainly entropically driven interaction between rPvLEA6 monomers under these conditions.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein or proteins.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"Q9LL46","operator":"and","partner_start":1,"partner_end":82}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-01-07T16:57:30.739Z"}},{"start":1,"end":82,"reference_id":"25271167","reference_source":"pmid","reference_html":"A group 6 late embryogenesis abundant protein from common bean is a disordered protein with extended helical structure and oligomer-forming properties. <i> Rivera-Najera LY, Saab-Rincón G, Battaglia M, Amero C, Pulido NO, García-Hernández E, Solórzano RM, Reyes JL, Covarrubias AA. </i> J Biol Chem, 2014","date":"2026-01-07T17:01:56.703Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0042802","term_name":"identical protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007107","ec_ontology":"ECO","ec_name":"yellow fluorescent protein fusion protein localization evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"ec_go":"IDA","region_id":"DP04014r006","statement":[{"text":"As shown in Fig. 11, fluorescence was detected only when the mixture containing the YFPN43-PvLEA6 and YFPC43-PvLEA6 was infiltrated but not when any of these were individually introduced into plant cells, indicating that the two nonfluorescent YFP fragments were brought together by the interaction between PvLEA6 monomers, hence forming a fluorescent complex.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein or proteins.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"Q9LL46","operator":"and","partner_start":1,"partner_end":82}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-01-07T17:08:01.335Z"}}],"regions_counter":6,"released":"2024_06","sequence":"MEKEKKTESEQGKVNLEGLPTEDSPYVKYKDLEDYKQQGYGTQGHQEPKTGRGAGATEAPTLSGAAFSSKSQATATGATNHK","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","fabids","Fabales","Fabaceae","Papilionoideae","50 kb inversion clade","NPAAA clade","indigoferoid/millettioid clade","Phaseoleae","Phaseolus"],"alphafold_very_low_content":0.14634146341463414,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":82,"type":"D"}],"Structural state":[{"start":1,"end":82,"type":"D"}],"Molecular function":[{"start":1,"end":82,"type":"F"}]}},{"disprot_id":"DP04015","acc":"Q9ZPQ7","creator":"eficho","date":"2023-03-20T15:04:19.454Z","features":{"pfam":[{"id":"PF28971","name":"Cold-regulated 15 domain","start":1,"end":160}],"gene3D":[]},"genes":[{"orfNames":[{"value":"AT2G03740","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AEC05744.1","url":"https://www.ebi.ac.uk/ena/browser/view/AEC05744.1"}}]},{"value":"F19B11.19","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AEC05744.1","url":"https://www.ebi.ac.uk/ena/browser/view/AEC05744.1"}}]},{"value":"F19B11_19","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AEC05744.1","url":"https://www.ebi.ac.uk/ena/browser/view/AEC05744.1"}}]}],"olnNames":[{"value":"At2g03740","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ABE65800.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABE65800.1"}}]}]}],"length":189,"name":"At2g03740","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":50,"end":189,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins.  <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2023-08-27T19:24:37.470Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04015r002","statement":[{"text":"We therefore monitored secondary structure of the six LEA_4 proteins in response to decreasing relative humidity (RH) using the Amide I band of Fourier-transform infrared (FTIR) spectra (Figure 6). This absorbance band mainly results from the C=O stretching vibration and is directly related to the protein backbone conformation.\nA maximum at 1650–1640 cm􀀀1 indicated that all proteins were mainly disordered at 100% RH, which is in line with the CD data.","type":"Results"},{"text":"Figure S5 shows FTIR spectra of the six LEA_4 proteins in EG concentrations ranging from 0 to 12 osM. Similar to decreasing RH, increasing osmolarity induces coil-helix transitions, indicated by a shift of the Amide I maxima to higher wavenumbers.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T08:56:23.796Z"}},{"start":50,"end":189,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins.  <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2023-08-27T19:22:00.963Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04015r003","statement":[{"text":"Simultaneous static and dynamic light scattering (SLS/DLS) measurements were conducted to determine the apparent average single particle mass (Mapp) and the apparent average hydrodynamic radius (RS) of the proteins in solution as a function of concentration (Figure S4, [30]). Absolute molecular mass and RS were obtained by extrapolation of apparent molecular mass and RS to infinite dilution. All investigated LEA proteins are essentially monomeric under fully hydrated conditions. Compared to globular proteins, RS of all investigated LEA proteins was rather large, indicating their expanded, non-compact nature.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-08-16T15:17:39.280Z"}},{"start":50,"end":189,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins.  <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2024-08-28T11:30:22.947Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04015r005","statement":[{"text":"Figure S5 shows FTIR spectra of the six LEA_4 proteins in EG concentrations ranging from 0 to 12 osM. Similar to decreasing RH, increasing osmolarity induces coil-helix transitions, indicated by a shift of the Amide I maxima to higher wavenumbers","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":" 30742","entry_name":"ethylene glycol"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:00:11.506Z"}},{"start":50,"end":189,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among <i>Arabidopsis thaliana</i> LEA_4 Proteins. <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2024-08-28T16:39:28.508Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0009409","term_name":"response to cold","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IDA","region_id":"DP04015r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"39073","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}],"entry_name":"6-carboxyfluorescein"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"170453367","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"10724471","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"56842030","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"45109789","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]}],"statement":[{"text":"Therefore, we analyzed the stability of liposomes modeling the lipid composition of inner chloroplast membranes (ICMM) after a freeze/thaw cycle and a dehydration/rehydration cycle in the ethylene glycolpresence of all six LEA_4 proteins at different LEA protein: lipid mass ratios (Figure 13).","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cold stimulus, a temperature stimulus below the optimal temperature for that organism.\" [GOC:lr]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:01:52.640Z"}}],"regions_counter":6,"released":"2024_12","sequence":"MSISGAVLSGLGPSFLISGGKRSGVGGGAMKVGRKNVIIAPQRKKSWVSAAVKGAGNSPNDPKWLDDASEKASGYVKEKGSEVGNVSAQKGQELQNQMERAKDYIFGKAGEAMDSVAENAKRASDFVTEKGKEVKEETTSRTDKAKDFIVEKAGDVKDTAMDMRNKTSKYVGDKATEAKEAILPPKTDA","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"alphafold_very_low_content":0.8201058201058201,"disorder_content":0.7407407407407407,"disprot_consensus":{"full":[{"start":50,"end":189,"type":"T"}],"Structural state":[{"start":50,"end":189,"type":"D"}],"Structural transition":[{"start":50,"end":189,"type":"T"}],"Biological process":[{"start":50,"end":189,"type":"F"}]}},{"disprot_id":"DP04016","acc":"Q9SIN3","creator":"eficho","date":"2023-03-20T15:04:45.357Z","features":{"pfam":[{"id":"PF28971","name":"Cold-regulated 15 domain","start":258,"end":320}],"gene3D":[]},"genes":[{"orfNames":[{"value":"AT2G42560","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AEC10139.1","url":"https://www.ebi.ac.uk/ena/browser/view/AEC10139.1"}}]},{"value":"F14N22.17","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AEC10139.1","url":"https://www.ebi.ac.uk/ena/browser/view/AEC10139.1"}}]},{"value":"F14N22_17","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AEC10139.1","url":"https://www.ebi.ac.uk/ena/browser/view/AEC10139.1"}}]}],"olnNames":[{"value":"At2g42560","evidences":[{"code":"ECO:0000313","source":{"name":"Araport","id":"AT2G42560","url":""}}]}]}],"length":635,"name":"Late embryogenesis abundant domain-containing protein / LEA domain-containing protein","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":1,"end":635,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins.  <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2023-07-21T14:45:09.382Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04016r001","statement":[{"text":"Simultaneous static and dynamic light scattering (SLS/DLS) measurements were conducted to determine the apparent average single particle mass (Mapp) and the apparent average hydrodynamic radius (RS) of the proteins in solution as a function of concentration (Figure S4, [30]). Absolute molecular mass and RS were obtained by extrapolation of apparent molecular mass and RS to infinite dilution. All investigated LEA proteins are essentially monomeric under fully hydrated conditions. Compared to globular proteins, RS of all investigated LEA proteins was rather large, indicating their expanded, non-compact nature.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-08-19T12:52:17.704Z"}},{"start":1,"end":635,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins.  <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2023-07-21T14:51:09.153Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04016r002","statement":[{"text":"We therefore monitored secondary structure of the six LEA_4 proteins in response to decreasing relative humidity (RH) using the Amide I band of Fourier-transform infrared (FTIR) spectra (Figure 6). This absorbance band mainly results from the C=O stretching vibration and is directly related to the protein backbone conformation. \nA maximum at 1650–1640 cm-1 indicated that all proteins were mainly disordered at 100% RH, which is in line with the CD data.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:02:20.534Z"}},{"start":1,"end":635,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins.  <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2024-10-06T09:48:24.060Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04016r003","statement":[{"text":"Figure S5 shows FTIR spectra of the six LEA_4 proteins in EG concentrations ranging from 0 to 12 osM. Similar to decreasing RH, increasing osmolarity induces coil-helix transitions, indicated by a shift of the Amide I maxima to higher wavenumbers.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":"ethylene glycol"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-09T09:20:06.562Z"}},{"start":1,"end":635,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among <i>Arabidopsis thaliana</i> LEA_4 Proteins. <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2024-10-06T09:47:59.046Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0009409","term_name":"response to cold","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IDA","region_id":"DP04016r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"39073","entry_name":"6-carboxyfluorescein"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"170453367","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"10724471","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"45109789","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"56842030","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]}],"statement":[{"text":"Therefore, we analyzed the stability of liposomes modeling the lipid composition of inner chloroplast membranes (ICMM) after a freeze/thaw cycle and a dehydration/rehydration cycle in the ethylene glycolpresence of all six LEA_4 proteins at different LEA protein: lipid mass ratios (Figure 13).","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cold stimulus, a temperature stimulus below the optimal temperature for that organism.\" [GOC:lr]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-09T09:20:04.692Z"}}],"regions_counter":5,"released":"2024_12","sequence":"MASEQARRENKVTEREVQVEKDRVPKMTSHFESMAEKGKDSDTHRHQTEGGGTQFVSLSDKGSNMPVSDEGEGETKMKRTQMPHSVGKFVTSSDSGTGKKKDEKEEHEKASLEDIHGYRANAQQKSMDSIKAAEERYNKAKESLSHSGQEARGGRGEEMVGKGRDSGVRVSHVGAVGGGGGGEEKESGVHGFHGEKARHAELLAAGGEEMREREGKESAGGVGGRSVKDTVAEKGQQAKESVGEGAQKAGSATSEKAQRASEYATEKGKEAGNMTAEQAARAKDYALQKAVEAKETAAEKAQRASEYMKETGSTAAEQAARAKDYTLQKAVEAKDVAAEKAQRASEYMTETGKQAGNVAAQKGQEAASMTAKAKDYTVQKAGEAAGYIKETTVEGGKGAAHYAGVAAEKAAAVGWTAAHFTTEKVVQGTKAVAGTVEGAVGYAGHKAVEVGSKAVDLTKEKAAVAADTVVGYTARKKEEAQHRDQEMHQGGEEEKQPGFVSGARRDFGEEYGEERGSEKDVYGYGAKGIPGEGRGDVGEAEYGRGSEKDVFGYGPKGTVEEARRDVGEEYGGGRGSERYVEEEGVGAGGVLGAIGETIAEIAQTTKNIVIGDAPVRTHEHGTTDPDYMRREHGQR","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"alphafold_very_low_content":0.8614173228346457,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":635,"type":"T"}],"Structural state":[{"start":1,"end":635,"type":"D"}],"Structural transition":[{"start":1,"end":635,"type":"T"}],"Biological process":[{"start":1,"end":635,"type":"F"}]}},{"disprot_id":"DP04017","acc":"Q6UNL8","creator":"eficho","date":"2023-03-20T15:05:44.579Z","features":{"pfam":[],"gene3D":[]},"genes":[],"length":554,"name":"Dehydrin","ncbi_taxon_id":3218,"organism":"Physcomitrium patens","regions":[{"start":1,"end":554,"reference_id":"33781743","reference_source":"pmid","reference_html":"Multiple copies of a novel amphipathic α-helix forming segment in Physcomitrella patens dehydrin play a key role in abiotic stress mitigation. <i> Upadhyaya G, Das A, Basu C, Agarwal T, Basak C, Chakraborty C, Halder T, Basu G, Ray S. </i> J Biol Chem, 2021","date":"2023-08-26T20:17:39.864Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04017r001","statement":[{"text":"CD spectroscopic analysis was carried out to probe the secondary structure of the proteins. The purified proteins (PpDHNA and deletion mutants Y11D11, Y6D6, Y6DM6, Y1K, K, and Y1) were analyzed by CD. As shown in Figure 2, A–G, all\nprotein variants (the uppermost black curve in each panel) were found to be disordered in an aqueous buffer. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-09-08T15:24:43.076Z"}},{"start":1,"end":554,"reference_id":"33781743","reference_source":"pmid","reference_html":"Multiple copies of a novel amphipathic α-helix forming segment in Physcomitrella patens dehydrin play a key role in abiotic stress mitigation. <i> Upadhyaya G, Das A, Basu C, Agarwal T, Basak C, Chakraborty C, Halder T, Basu G, Ray S. </i> J Biol Chem, 2021","date":"2023-09-11T15:08:48.482Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0050821","term_name":"protein stabilization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":54}],"ec_go":"IDA","region_id":"DP04017r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P13491","statements":[{"type":"Methods","text":"A mixture of 100 μl v/v LDH with or without additive proteins (variable molar ratio) was incubated for 10 min at 54 °C. After the stress treatment, the LDH activity was measured by diluting the mixture to 1 ml of reaction mix containing 1.1 mM pyruvic acid and 0.13 mM NADH. Oxidation of NADH was measured by recording the A340 for 5 min."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":1.1,"db":"PubChem","id":"CID:1060","statements":[{"type":"Methods","text":"A mixture of 100 μl v/v LDH with or without additive proteins (variable molar ratio) was incubated for 10 min at 54 °C. After the stress treatment, the LDH activity was measured by diluting the mixture to 1 ml of reaction mix containing 1.1 mM pyruvic acid and 0.13 mM NADH. Oxidation of NADH was measured by recording the A340 for 5 min."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":0.13,"db":"PubChem","id":"CID:439153","statements":[{"type":"Methods","text":"A mixture of 100 μl v/v LDH with or without additive proteins (variable molar ratio) was incubated for 10 min at 54 °C. After the stress treatment, the LDH activity was measured by diluting the mixture to 1 ml of reaction mix containing 1.1 mM pyruvic acid and 0.13 mM NADH. Oxidation of NADH was measured by recording the A340 for 5 min."}]}],"statement":[{"text":"Upon high-temperature treatment at 54 °C for 10 min, LDH lost most of its activity, retaining only about 5% of its initial activity (100%). However, the presence of a minimal concentration of ∼1250 nM of PpDHNA (1:4 molar ratio of LDH:additive protein) could restore its original activity.","type":"Results"},{"text":"The protective activity increased as the molar ratios of the additive proteins were increased (Fig. 3B).","type":"Results"}],"term_comment":"","term_def":"\"Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":554,"reference_id":"33781743","reference_source":"pmid","reference_html":"Multiple copies of a novel amphipathic α-helix forming segment in Physcomitrella patens dehydrin play a key role in abiotic stress mitigation. <i> Upadhyaya G, Das A, Basu C, Agarwal T, Basak C, Chakraborty C, Halder T, Basu G, Ray S. </i> J Biol Chem, 2021","date":"2023-09-11T15:13:39.949Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0050821","term_name":"protein stabilization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006331","ec_ontology":"ECO","ec_name":"Congo red staining evidence","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":54,"statements":[{"type":"Methods","text":"LDH was subjected to high-temperature stress at 54 °C at different time intervals (10, 20, 30 min) in the presence and absence of PpDHNA, its deletion mutants, and BSA at a 1:4 molar ratio."}]}],"region_id":"DP04017r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P13491","statements":[{"type":"Methods","text":"LDH was subjected to high-temperature stress at 54 °C at different time intervals (10, 20, 30 min) in the presence and absence of PpDHNA, its deletion mutants, and BSA at a 1:4 molar ratio."}]}],"statement":[{"text":"LDH loses its activity at high-temperature forming aggregates, which could be visualized by staining with Congo red (40). LDH was found to lose its maximum activity (∼95%) at 54 °C when incubated for 10 min. LDH showed substantial aggregation as compared with the control (Fig. 3D). The results obtained were also quantified fluorometrically (Fig. 3E). However, in presence of PpDHNA, the aggregate formation was significantly less.","type":"Results"}],"term_comment":"","term_def":"\"Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":554,"reference_id":"33781743","reference_source":"pmid","reference_html":"Multiple copies of a novel amphipathic α-helix forming segment in Physcomitrella patens dehydrin play a key role in abiotic stress mitigation. <i> Upadhyaya G, Das A, Basu C, Agarwal T, Basak C, Chakraborty C, Halder T, Basu G, Ray S. </i> J Biol Chem, 2021","date":"2023-09-11T15:32:38.313Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0050821","term_name":"protein stabilization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007684","ec_ontology":"ECO","ec_name":"protein separation evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":54,"statements":[{"type":"Methods","text":"Then the cells were incubated at 54 °C for another 20 min to impart high-temperature stress."}]}],"ec_go":"IDA","region_id":"DP04017r005","statement":[{"text":"The control cells showed a higher amount of protein in the pellet fraction as compared with the supernatant. However, E. coli cells overexpressing PpDHNA protein showed a higher amount of protein in the supernatant (211 μg) (Fig. 4C).","type":"Results"},{"text":"The presence of the proteins in the soluble fraction under temperature stress conditions correlated well with the cell survivability dataset. These data highlight the importance of the D-segment in imparting high-temperature tolerance through proteome protection.","type":"Results"}],"term_comment":"","term_def":"\"Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":554,"reference_id":"33781743","reference_source":"pmid","reference_html":"Multiple copies of a novel amphipathic α-helix forming segment in Physcomitrella patens dehydrin play a key role in abiotic stress mitigation. <i> Upadhyaya G, Das A, Basu C, Agarwal T, Basak C, Chakraborty C, Halder T, Basu G, Ray S. </i> J Biol Chem, 2021","date":"2023-09-11T15:39:59.590Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0009408","term_name":"response to heat","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007703","ec_ontology":"ECO","ec_name":"cell viability assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":54,"statements":[{"type":"Methods","text":"Then the cells were incubated at 54 °C for another 20 min to impart high-temperature stress."}]}],"ec_go":"IDA","region_id":"DP04017r006","statement":[{"text":"However, E. coli cells overexpressing D-segment bearing proteins PpDHNA, Y11D11, and Y6D6 showed better cell viability of 77%, 57%, and 42%, respectively.","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism.\" [GOC:lr]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":554,"reference_id":"33781743","reference_source":"pmid","reference_html":"Multiple copies of a novel amphipathic α-helix forming segment in Physcomitrella patens dehydrin play a key role in abiotic stress mitigation. <i> Upadhyaya G, Das A, Basu C, Agarwal T, Basak C, Chakraborty C, Halder T, Basu G, Ray S. </i> J Biol Chem, 2021","date":"2023-09-11T15:47:36.434Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0033555","term_name":"multicellular organismal response to stress","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006049","ec_ontology":"ECO","ec_name":"genetic transformation evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":46,"statements":[{"type":"Methods","text":" Three randomly selected lines were subjected to high-temperature (32–46 °C) along with desiccation stress for 14 days at 12 h light and 12 h dark with a photon flux of 100 μmol m−2 s−1 at 65% relative humidity. High-temperature stress was subjected according to the stress regime as shown in Fig. S12. The stress regime was repeated each day and continued for 14 days on a stretch without any watering to generate high-temperature coupled with desiccation stress."}]}],"ec_go":"IMP","region_id":"DP04017r007","statement":[{"text":"D-segments enhanced the stress tolerance in transformed tobacco plants","type":"Results"},{"text":"Upon stress treatment, PpDHNA, Y11D11, and Y6D6 showed lesser wilting conditions and recovered quickly after the stress was removed.","type":"Results"},{"text":"Upon stress, the chlorophyll content (Fig. 5B) of the transformed plants decreased in the order PpDHNA, Y11D11, Y6D6 and the rest (Y6DM6, Y1K, K, and Y1) showed similar values. Thus, the first three coped with stress the best. This result correlated with the soluble sugar and proline content, both indicators of how good the plant is coping with stress.","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a multicellular organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating the organism is under stress. The stress is usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation).\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":554,"reference_id":"33781743","reference_source":"pmid","reference_html":"Multiple copies of a novel amphipathic α-helix forming segment in Physcomitrella patens dehydrin play a key role in abiotic stress mitigation. <i> Upadhyaya G, Das A, Basu C, Agarwal T, Basak C, Chakraborty C, Halder T, Basu G, Ray S. </i> J Biol Chem, 2021","date":"2023-09-11T15:54:17.082Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007107","ec_ontology":"ECO","ec_name":"yellow fluorescent protein fusion protein localization evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"Q6UNL8","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04017r008","statement":[{"text":"To investigate whether the DHN molecule can self-interact and to understand the role of amphipathic α-helices for the same, a bimolecular fluorescence complementation (BiFC) assay was performed. The analysis showed a strong YFP signal, localized at the plasma membrane transiently coexpressing PpDHNA/PpDHNA and Y11D11/Y11D11 (Fig. 7, A, B, and J).","type":"Results"},{"text":"These results indicated that PpDHNA could self-associate with amphipathic α-helices, whether its K- or D-segment, being the major contributor behind such interactions.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":9,"released":"2024_06","sequence":"MNQYGREQQDTGLVGSGTGHRDEYGNPRQEGIMDKVKNAVGMGPSSGTGYNNQPGYDNYGNPRQEGLVDKAKDAVGMGPSLGTGYNNQPGYDSYGNREGIVDRAKDAVGMGPNSGTGYNNQPGYDNYGDRRHEGLADRAKDAVGMGPNSGYNHQPGYDNYGNREGVVDKAKDAVGMGPNSGTGYNNQPGYDSYGTRRQEGLVDRAKDAVGMGPNSGTGYNNQPGYDNYGNPRREGVVDRAKDAVGMGPNSGYNNQPGYDNYGNREGIVDKAKDAVGVGPHSGTGYHNQPSYDNYGNPRQEGIVDRAKDAVGMGPNSGTGYNNQSDYDSYGNPRHEGMLDKAKDDFDMGPNSGTGYNNRPGYDTYGDRKHEGIGDKVRDAIGTGPNSGYDSRTPTGTDAYVHGNHPPGMQDRITGVNEPSILGGRENVDRHGFGHDGRQHHGLLDNVTLQSGHIPETMVGGRRVEPGYDMTKSAGHHLTDLGHHGNDSGVTGLGHHDTDYDERRGKGFEDPIDNKTGLGSDYDTTETGSGYGATDTGAAPHKKGIITKIKEKLHH","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Bryophyta","Bryophytina","Bryopsida","Funariidae","Funariales","Funariaceae","Physcomitrium"],"alphafold_very_low_content":1,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":554,"type":"D"}],"Structural state":[{"start":1,"end":554,"type":"D"}],"Biological process":[{"start":1,"end":554,"type":"F"}],"Molecular function":[{"start":1,"end":554,"type":"F"}]}},{"disprot_id":"DP04018","acc":"Q9LW12","creator":"grivas","date":"2023-03-20T15:07:05.053Z","features":{"pfam":[{"id":"PF27970","name":"LEA protein 1/2/D7/Stress-induced protein KIN2","start":139,"end":192}],"gene3D":[]},"genes":[{"name":{"value":"LEA29","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"18318901","url":"http://www.ncbi.nlm.nih.gov/pubmed/18318901","alternativeUrl":"https://europepmc.org/abstract/MED/18318901"}}]},"synonyms":[{"value":"LEA76","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"18931353","url":"http://www.ncbi.nlm.nih.gov/pubmed/18931353","alternativeUrl":"https://europepmc.org/abstract/MED/18931353"}}]}],"orfNames":[{"value":"MSJ11.7","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"BAB02298.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAB02298.1"}}]}],"olnNames":[{"value":"At3g15670","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT3G15670","url":""}}]}]}],"length":225,"name":"Late embryogenesis abundant protein 29","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":1,"end":225,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins.  <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2024-08-28T11:32:19.905Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04018r001","statement":[{"text":"Figure S5 shows FTIR spectra of the six LEA_4 proteins in EG concentrations ranging from 0 to 12 osM. Similar to decreasing RH, increasing osmolarity induces coil-helix transitions, indicated by a shift of the Amide I maxima to higher wavenumbers.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":"ethylene glycol"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:16:05.382Z"}},{"start":1,"end":225,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins.  <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2024-08-28T11:32:54.260Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04018r002","statement":[{"text":"All proteins showed typical random coil spectra in dilute solution. With increasing concentrations of each of the co-solvents, the changes in the spectral shape report on the formation of ordered secondary structure.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":"ethylene glycol"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:16:02.699Z"}},{"start":1,"end":225,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins.  <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2023-08-27T19:34:44.860Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04018r003","statement":[{"text":"Simultaneous static and dynamic light scattering (SLS/DLS) measurements were conducted to determine the apparent average single particle mass (Mapp) and the apparent average hydrodynamic radius (RS) of the proteins in solution as a function of concentration (Figure S4, [30]). Absolute molecular mass and RS were obtained by extrapolation of apparent molecular mass and RS to infinite dilution. All investigated LEA proteins are essentially monomeric under fully hydrated conditions. Compared to globular proteins, RS of all investigated LEA proteins was rather large, indicating their expanded, non-compact nature.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-08-19T12:52:42.002Z"}},{"start":1,"end":225,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins.  <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2023-08-27T19:35:47.177Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04018r004","statement":[{"text":"We therefore monitored secondary structure of the six LEA_4 proteins in response to decreasing relative humidity (RH) using the Amide I band of Fourier-transform infrared (FTIR) spectra (Figure 6). This absorbance band mainly results from the C=O stretching vibration and is directly related to the protein backbone conformation. A maximum at 1650–1640 cm-1 indicated that all proteins were mainly disordered at 100% RH, which is in line with the CD data.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:16:35.436Z"}},{"start":1,"end":225,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among <i>Arabidopsis thaliana</i> LEA_4 Proteins. <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2024-10-06T09:49:29.226Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0009409","term_name":"response to cold","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IDA","region_id":"DP04018r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"39073","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}],"entry_name":"6-carboxyfluorescein"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"170453367","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"10724471","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"56842030","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"45109789","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]}],"statement":[{"text":"Therefore, we analyzed the stability of liposomes modeling the lipid composition of inner chloroplast membranes (ICMM) after a freeze/thaw cycle and a dehydration/rehydration cycle in the ethylene glycolpresence of all six LEA_4 proteins at different LEA protein: lipid mass ratios (Figure 13).","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cold stimulus, a temperature stimulus below the optimal temperature for that organism.\" [GOC:lr]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-09T09:20:39.156Z"}}],"regions_counter":6,"released":"2024_12","sequence":"MASNQQSYKAGETRGKAQEKTGQAMGTMRDKAEEGRDKTSQTAQTAQQKAHETAQSAKDKTSQTAQAAQQKAHETAQSAKEKTSQTAQTAQQKAHETTQAAKEKTSQAGDKAREAKDKAGSYLSETGEAIKNKAQDAAQYTKETAQGAAQYTKETAEAGRDKTGGFLSQTGEHVKQMAMGAADAVKHTFGMATEEEDKEHYPGSTTTTTATTRTTDPTHQTYQRK","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"alphafold_very_low_content":0.27111111111111114,"dataset":["Stress response proteins"],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":225,"type":"T"}],"Structural state":[{"start":1,"end":225,"type":"D"}],"Structural transition":[{"start":1,"end":225,"type":"T"}],"Biological process":[{"start":1,"end":225,"type":"F"}]}},{"disprot_id":"DP04019","acc":"Q9T0H6","creator":"eficho","date":"2023-03-20T15:08:19.041Z","features":{"pfam":[{"id":"PF27970","name":"LEA protein 1/2/D7/Stress-induced protein KIN2","start":43,"end":107}],"gene3D":[]},"genes":[{"name":{"value":"NAD-ME1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AEE83293.1","url":"https://www.ebi.ac.uk/ena/browser/view/AEE83293.1"}}]},"synonyms":[{"value":"NAD-dependent malic enzyme 1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AEE83293.1","url":"https://www.ebi.ac.uk/ena/browser/view/AEE83293.1"}}]},{"value":"UNE15","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AEE83293.1","url":"https://www.ebi.ac.uk/ena/browser/view/AEE83293.1"}}]},{"value":"unfertilized embryo sac 15","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AEE83293.1","url":"https://www.ebi.ac.uk/ena/browser/view/AEE83293.1"}}]}],"orfNames":[{"value":"AT4G13560","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AEE83293.1","url":"https://www.ebi.ac.uk/ena/browser/view/AEE83293.1"}}]},{"value":"T6G15.110","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAB41114.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAB41114.1"}}]},{"value":"T6G15_110","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AEE83293.1","url":"https://www.ebi.ac.uk/ena/browser/view/AEE83293.1"}}]}],"olnNames":[{"value":"At4g13560","evidences":[{"code":"ECO:0000313","source":{"name":"Araport","id":"AT4G13560","url":""}}]},{"value":"At4g13560/T6G15_110","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAC42956.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAC42956.1"}}]}]}],"length":109,"name":"Late embryogenesis abundant protein (LEA) family protein","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":1,"end":109,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins.  <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2023-08-27T19:37:19.279Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04019r001","statement":[{"text":"We therefore monitored secondary structure of the six LEA_4 proteins in response to decreasing relative humidity (RH) using the Amide I band of Fourier-transform infrared (FTIR) spectra (Figure 6). This absorbance band mainly results from the C=O stretching vibration and is directly related to the protein backbone conformation. A maximum at 1650–1640 cm-1 indicated that all proteins were mainly disordered at 100% RH, which is in line with the CD data.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:17:23.645Z"}},{"start":1,"end":109,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins.  <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2023-08-27T19:37:37.998Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04019r002","statement":[{"text":"Simultaneous static and dynamic light scattering (SLS/DLS) measurements were conducted to determine the apparent average single particle mass (Mapp) and the apparent average hydrodynamic radius (RS) of the proteins in solution as a function of concentration (Figure S4, [30]). Absolute molecular mass and RS were obtained by extrapolation of apparent molecular mass and RS to infinite dilution. All investigated LEA proteins are essentially monomeric under fully hydrated conditions. Compared to globular proteins, RS of all investigated LEA proteins was rather large, indicating their expanded, non-compact nature.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-08-12T15:19:38.179Z"}},{"start":1,"end":109,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins.  <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2024-08-28T11:37:03.362Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04019r003","statement":[{"text":"All proteins showed typical random coil spectra in dilute solution. With increasing concentrations of each of the co-solvents, the changes in the spectral shape report on the formation of ordered secondary structure.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":"ethylene glycol"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:17:44.644Z"}},{"start":1,"end":109,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins.  <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2024-08-28T11:36:33.950Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04019r004","statement":[{"text":"Figure S5 shows FTIR spectra of the six LEA_4 proteins in EG concentrations ranging from 0 to 12 osM. Similar to decreasing RH, increasing osmolarity induces coil-helix transitions, indicated by a shift of the Amide I maxima to higher wavenumbers.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":"ethylene glycol"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:17:34.455Z"}},{"start":1,"end":109,"reference_id":"32316452","reference_source":"pmid","reference_html":"Similar Yet Different-Structural and Functional Diversity among <i>Arabidopsis thaliana</i> LEA_4 Proteins. <i> Knox-Brown P, Rindfleisch T, Günther A, Balow K, Bremer A, Walther D, Miettinen MS, Hincha DK, Thalhammer A. </i> Int J Mol Sci, 2020","date":"2024-08-29T08:38:25.795Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0009409","term_name":"response to cold","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IDA","region_id":"DP04019r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"39073","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}],"entry_name":"6-carboxyfluorescein"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"170453367","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"10724471","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"56842030","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"45109789","statements":[{"type":"Figure","text":"The integrity of large unilamellar ICMM vesicles, composed of 40% monogalactosyldiacylglycerol (MGDG), 30% digalactosyldiacylglycerol (DGDG), 15% sulfoquinovosyldiacylglycerol (SQDG) and 15% egg phosphatidylglycerol (EPG) (A,B) or of pure 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC) (C) was assayed as leakage of the soluble marker CF."}]}],"statement":[{"text":"Therefore, we analyzed the stability of liposomes modeling the lipid composition of inner chloroplast membranes (ICMM) after a freeze/thaw cycle and a dehydration/rehydration cycle in the ethylene glycolpresence of all six LEA_4 proteins at different LEA protein: lipid mass ratios (Figure 13).","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cold stimulus, a temperature stimulus below the optimal temperature for that organism.\" [GOC:lr]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:17:51.815Z"}}],"regions_counter":5,"released":"2024_12","sequence":"MSQQQFNAGQNRGQAQEKAEQWTESAKQTAQSACDKTADLTQSARDKAADLTQSARDKTADGSHSANKSAQHNQEQAAGLFGQTGESVKNMAQGALDGVKNSLGMNEKK","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"alphafold_very_low_content":0.03669724770642202,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":109,"type":"T"}],"Structural state":[{"start":1,"end":109,"type":"D"}],"Structural transition":[{"start":1,"end":109,"type":"T"}],"Biological process":[{"start":1,"end":109,"type":"F"}]}},{"disprot_id":"DP04020","acc":"A0A7G5VWW1","creator":"eficho","date":"2023-03-20T15:13:24.929Z","features":{"pfam":[{"id":"PF00257","name":"Dehydrin","start":137,"end":201}],"gene3D":[]},"genes":[{"name":{"value":"ST10","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"UUZ30945.1","url":"https://www.ebi.ac.uk/ena/browser/view/UUZ30945.1"}}]}}],"length":222,"name":"DHN1","ncbi_taxon_id":3879,"organism":"Medicago sativa","regions":[{"start":1,"end":222,"reference_id":"34363255","reference_source":"pmid","reference_html":"Dehydrin MsDHN1 improves aluminum tolerance of alfalfa (Medicago sativa L.) by affecting oxalate exudation from root tips. <i> Lv A, Wen W, Fan N, Su L, Zhou P, An Y. </i> Plant J, 2021","date":"2023-08-26T20:24:52.737Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04020r001","statement":[{"text":"The CD spectra of MsDHN1 showed a minimal peak close to 209 nm (Figure S3), and contained a considerable amount of random coil structure (accounting for 65% of the total). These are typical characteristics of intrinsically disordered proteins (IDPs), which have a large negative peak at approximately 200 nm and a high ratio of coil conformation (Receveur-Br\u0013echot et al., 2005). These results demonstrate that MsDHN1 is a highly disordered protein.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-08-19T12:53:16.486Z"}},{"start":1,"end":222,"reference_id":"34363255","reference_source":"pmid","reference_html":"Dehydrin MsDHN1 improves aluminum tolerance of alfalfa (Medicago sativa L.) by affecting oxalate exudation from root tips. <i> Lv A, Wen W, Fan N, Su L, Zhou P, An Y. </i> Plant J, 2021","date":"2023-09-15T11:44:37.338Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"EXP","region_id":"DP04020r003","statement":[{"text":"Circular dichroism (CD) analysis showed that a negative band occurred at 228 nm in the CD spectrum, which supported our finding that MsDHN1\nformed dimers in vitro (Figure S3). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-08-19T12:53:25.141Z"}},{"start":1,"end":222,"reference_id":"34363255","reference_source":"pmid","reference_html":"Dehydrin MsDHN1 improves aluminum tolerance of alfalfa (Medicago sativa L.) by affecting oxalate exudation from root tips. <i> Lv A, Wen W, Fan N, Su L, Zhou P, An Y. </i> Plant J, 2021","date":"2023-09-15T11:47:20.398Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IDA","region_id":"DP04020r004","statement":[{"text":"In order to demonstrate that this MsDHN1 dimerization also occurs in plants, a\nbimolecular fluorescence complementation (BiFC) analysis was performed in tobacco leaves. Fluorescence signals were detected in the cytoplasm when MsDHN1-cYFP (the C-terminal fragment of YFP) and MsDHN1-nYFP (the Nterminal fragment of YFP) co-transformed in tobacco leaves (Figure 1k), indicating that the MsDHN1 protein is able to interact with itself and form homodimers in plant cells.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-08-19T12:54:09.035Z"}},{"start":1,"end":222,"reference_id":"34363255","reference_source":"pmid","reference_html":"Dehydrin MsDHN1 improves aluminum tolerance of alfalfa (Medicago sativa L.) by affecting oxalate exudation from root tips. <i> Lv A, Wen W, Fan N, Su L, Zhou P, An Y. </i> Plant J, 2021","date":"2024-09-18T09:10:41.038Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IDA","region_id":"DP04020r005","statement":[{"text":"The results showed that the 50-kD polypeptide was an MsDHN1 homodimer (Figure 1j).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":222,"reference_id":"34363255","reference_source":"pmid","reference_html":"Dehydrin MsDHN1 improves aluminum tolerance of alfalfa (Medicago sativa L.) by affecting oxalate exudation from root tips. <i> Lv A, Wen W, Fan N, Su L, Zhou P, An Y. </i> Plant J, 2021","date":"2024-09-18T09:15:35.274Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005829","term_name":"cytosol","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IDA","region_id":"DP04020r006","statement":[{"text":"Unexpectedly, MsDHN1 protein showed only a cytoplasmic localization in epidermal cells of tobacco leaves or in cells of hairy roots (Figure 1b–f).","type":"Results"}],"term_comment":"","term_def":"\"The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.\" [GOC:hjd, GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":222,"reference_id":"34363255","reference_source":"pmid","reference_html":"Dehydrin MsDHN1 improves aluminum tolerance of alfalfa (Medicago sativa L.) by affecting oxalate exudation from root tips. <i> Lv A, Wen W, Fan N, Su L, Zhou P, An Y. </i> Plant J, 2021","date":"2024-09-18T09:23:33.279Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0033555","term_name":"multicellular organismal response to stress","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IMP","region_id":"DP04020r007","statement":[{"text":"Compared with the WT or the vector line, growth rates of hairy roots (Figure 2c,d) or plant seedlings (Figures 2e and S5) were significant higher in MsDHN1-OE lines and lower in MsDHN1-RNAi lines under Al stress, respectively. These results indicate that MsDHN1 positively affects alfalfa tolerance to Al stress.","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a multicellular organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating the organism is under stress. The stress is usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation).\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":222,"reference_id":"34363255","reference_source":"pmid","reference_html":"Dehydrin MsDHN1 improves aluminum tolerance of alfalfa (Medicago sativa L.) by affecting oxalate exudation from root tips. <i> Lv A, Wen W, Fan N, Su L, Zhou P, An Y. </i> Plant J, 2021","date":"2024-09-18T09:27:25.961Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"B9VV95","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P42067","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04020r008","statement":[{"text":"We applied the pull-down approach to identify putative MsDHN1-interacting proteins to elucidate the molecular basis for MsDHN1 influence on oxalic acid secretion.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":222,"reference_id":"34363255","reference_source":"pmid","reference_html":"Dehydrin MsDHN1 improves aluminum tolerance of alfalfa (Medicago sativa L.) by affecting oxalate exudation from root tips. <i> Lv A, Wen W, Fan N, Su L, Zhou P, An Y. </i> Plant J, 2021","date":"2024-09-18T09:28:33.364Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005805","ec_ontology":"ECO","ec_name":"yeast 2-hybrid evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"B9VV95","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P42067","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04020r009","statement":[{"text":"Then, a series of yeast-two-hybrid (Y2H) assays was implemented between MsDHN1 and candidate proteins. Two positive clones (MsPIP2;1 and MsTIP1;1) that encoded AQP were found finally (Figure S9).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":222,"reference_id":"34363255","reference_source":"pmid","reference_html":"Dehydrin MsDHN1 improves aluminum tolerance of alfalfa (Medicago sativa L.) by affecting oxalate exudation from root tips. <i> Lv A, Wen W, Fan N, Su L, Zhou P, An Y. </i> Plant J, 2021","date":"2024-09-18T09:32:42.176Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006293","ec_ontology":"ECO","ec_name":"protein fragment functional complementation evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"B9VV95","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P42067","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04020r010","statement":[{"text":"BiFC assays were performed to verify the MsDHN1-MsPIP2;1 or MsTIP1;1 interaction in plant cells. When MsDHN1-cYFP was transiently co-expressed with MsPIP2;1/MsTIP1;1-nYFP in Nicotiana benthamiana leaf cells, reconstituted YFP fluorescence was observed in the cytomembrane. Similarly, YFP fluorescence was observed when MsDHN1-nYFP co-expressed with MsPIP2;1/MsTIP1;1-cYFP (Figure 4b).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":222,"reference_id":"34363255","reference_source":"pmid","reference_html":"Dehydrin MsDHN1 improves aluminum tolerance of alfalfa (Medicago sativa L.) by affecting oxalate exudation from root tips. <i> Lv A, Wen W, Fan N, Su L, Zhou P, An Y. </i> Plant J, 2021","date":"2024-09-18T09:34:56.125Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"B9VV95","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P42067","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04020r011","statement":[{"text":"Co-immunoprecipitation (Co-IP) assays further demonstrated that MsDHN1 associated with AQPs in N. benthamiana leaf cells (Figure 4c). These results suggest that MsDHN1 interacts with AQPs in plant.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":222,"reference_id":"34363255","reference_source":"pmid","reference_html":"Dehydrin MsDHN1 improves aluminum tolerance of alfalfa (Medicago sativa L.) by affecting oxalate exudation from root tips. <i> Lv A, Wen W, Fan N, Su L, Zhou P, An Y. </i> Plant J, 2021","date":"2024-09-18T09:37:56.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0097501","term_name":"stress response to metal ion","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IMP","region_id":"DP04020r012","statement":[{"text":"Organic acid has the function of chelating Al to alleviate Al toxicity in plants","type":"Results"},{"text":"Compared with the WT or the vector line, significantly increased oxalate exudation was observed from root tips exposed to 100 μm AlCl3 in MsDHN1-OE lines (Figure 3g,i); in contrast, significantly decreased oxalate exudation was observed in MsDHN1-RNAi lines (Figures 3h and S7).","type":"Results"},{"text":"MsDHN1 modulates Al accumulations in root tips via oxalic acid secretion","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a disturbance in organismal or cellular homeostasis caused by a metal ion stimulus.\" [GOC:kmv]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":12,"released":"2024_12","sequence":"MAEENQNKYEETTATNSETEIKDRGVFDFLGGKKKDEEHIKPQEDAVATDFSHKVTLYEAPSETKVEEKEEGEKKHTSLLEKLHRSDSSSSSSSEEEVDGERRKKKKKEKKEKKEDTSVPVEKVDVVDGTTASTEEKKGFLDKIKEKLPGHKKTDDVTTPPPVVVAPAVPSAETTTTTASHDQGEKKGILEKIKEKIPGYHPKTATEHEDNKDHHKDETTSH","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","fabids","Fabales","Fabaceae","Papilionoideae","50 kb inversion clade","NPAAA clade","Hologalegina","IRL clade","Trifolieae","Medicago"],"alphafold_very_low_content":0.5,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":222,"type":"D"}],"Structural state":[{"start":1,"end":222,"type":"D"}],"Molecular function":[{"start":1,"end":222,"type":"F"}],"Cellular component":[{"start":1,"end":222,"type":"F"}],"Biological process":[{"start":1,"end":222,"type":"F"}]}},{"disprot_id":"DP04022","acc":"Q6BDI9","creator":"zskalman","date":"2023-03-21T10:07:15.910Z","features":{"pfam":[{"id":"PF15208","name":"Rab15 effector","start":6,"end":235}],"gene3D":[]},"genes":[{"name":{"value":"REP15"}}],"length":236,"name":"Rab15 effector protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":14,"reference_id":"35871249","reference_source":"pmid","reference_html":"Rep15 interacts with several Rab GTPases and has a distinct fold for a Rab effector. <i> Rai A, Singh AK, Bleimling N, Posern G, Vetter IR, Goody RS. </i> Nat Commun, 2022","date":"2023-04-20T09:36:04.107Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"8A4A"}],"region_id":"DP04022r001","statement":[{"text":"No electron density was observed\nfor the first 14 amino acids, the middle 117 to 130 amino acids\nand for the last residue.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asn101Asp","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Rep15 is composed of 236 amino acids (UniProt ID: Q6BDI9) and in the present work, a naturally occurring N101D Rep15 variant (VAR_039548) was used (Supplementary Fig. 1a)."}]}],"sequence_construct":"GHMGQKASQQLALKDSKEVPVVCEVVSEAIVHAAQKLKEYLGFEYPPSKLCPAANTLNEIFLIHFITFCQEKGVDEWLTTTKMTKHQAFLFGADWIWTFWGSDKQIKLQLAVQTLQMSSPPPVESKPCDLSNPESRVEESSWKKSRFDKLEEFCNLIGEDCLGLFIIFGMPGKPKDIRGVVLDSVKSQMVRSHLPGGKAVAQFVLETEDCVFIKELLRNCLSKKDGLREVGKVYISIL","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P10949","statements":[{"type":"Introduction","text":"To decipher the\nbinding mode, we have determined the structure of Rep15:Rab3B\nand Rep15:Rab3C complexes, respectively."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:135403657","statements":[{"type":"Methods","text":"The complex of\nRep15 (human): Rab3CGppNHp_Q222H_10-227 (bovine) (150 μM of 1:1 complex) was\ncrystallized in 0.1M MES pH 6.0 and 10% (w/v) PEG 6000."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888","statements":[{"type":"Figure","text":"Mg2+ ion is shown as a green sphere and GppNHp is shown in stick representation"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T15:58:42.260Z"}},{"start":117,"end":130,"reference_id":"35871249","reference_source":"pmid","reference_html":"Rep15 interacts with several Rab GTPases and has a distinct fold for a Rab effector. <i> Rai A, Singh AK, Bleimling N, Posern G, Vetter IR, Goody RS. </i> Nat Commun, 2022","date":"2023-04-20T09:35:13.768Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"8A4A"}],"region_id":"DP04022r002","statement":[{"text":"No electron density was observed\nfor the first 14 amino acids, the middle 117 to 130 amino acids\nand for the last residue.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asn101Asp","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Rep15 is composed of 236 amino acids (UniProt ID: Q6BDI9) and in the present work, a naturally occurring N101D Rep15 variant (VAR_039548) was used (Supplementary Fig. 1a)."}]}],"sequence_construct":"GHMGQKASQQLALKDSKEVPVVCEVVSEAIVHAAQKLKEYLGFEYPPSKLCPAANTLNEIFLIHFITFCQEKGVDEWLTTTKMTKHQAFLFGADWIWTFWGSDKQIKLQLAVQTLQMSSPPPVESKPCDLSNPESRVEESSWKKSRFDKLEEFCNLIGEDCLGLFIIFGMPGKPKDIRGVVLDSVKSQMVRSHLPGGKAVAQFVLETEDCVFIKELLRNCLSKKDGLREVGKVYISIL","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":"not relevant","value":null,"db":"UniProt","id":"P10949","statements":[{"type":"Introduction","text":"To decipher the\nbinding mode, we have determined the structure of Rep15:Rab3B\nand Rep15:Rab3C complexes, respectively."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:135403657","statements":[{"type":"Methods","text":"The complex of\nRep15 (human): Rab3CGppNHp_Q222H_10-227 (bovine) (150 μM of 1:1 complex) was\ncrystallized in 0.1M MES pH 6.0 and 10% (w/v) PEG 6000."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888","statements":[{"type":"Figure","text":"Mg2+ ion is shown as a green sphere and GppNHp is shown in stick representation."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T15:58:37.021Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MGQKASQQLALKDSKEVPVVCEVVSEAIVHAAQKLKEYLGFEYPPSKLCPAANTLNEIFLIHFITFCQEKGVDEWLTTTKMTKHQAFLFGADWIWTFWGSNKQIKLQLAVQTLQMSSPPPVESKPCDLSNPESRVEESSWKKSRFDKLEEFCNLIGEDCLGLFIIFGMPGKPKDIRGVVLDSVKSQMVRSHLPGGKAVAQFVLETEDCVFIKELLRNCLSKKDGLREVGKVYISIL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.13135593220338984,"disorder_content":0.11864406779661017,"disprot_consensus":{"full":[{"start":1,"end":14,"type":"D"},{"start":117,"end":130,"type":"D"}],"Structural state":[{"start":1,"end":14,"type":"D"},{"start":117,"end":130,"type":"D"}]}},{"disprot_id":"DP04023","acc":"P10949","creator":"zskalman","date":"2023-03-21T10:10:25.513Z","features":{"pfam":[{"id":"PF00071","name":"Ras family","start":32,"end":191}],"gene3D":[]},"genes":[{"name":{"value":"RAB3C"}}],"length":227,"name":"Ras-related protein Rab-3C","ncbi_taxon_id":9913,"organism":"Bos taurus","regions":[{"start":10,"end":25,"reference_id":"35871249","reference_source":"pmid","reference_html":"Rep15 interacts with several Rab GTPases and has a distinct fold for a Rab effector. <i> Rai A, Singh AK, Bleimling N, Posern G, Vetter IR, Goody RS. </i> Nat Commun, 2022","date":"2023-04-20T09:45:04.657Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"8A4A"}],"region_id":"DP04023r001","statement":[{"text":"No\nelectron density was observed for the first 16 amino acids and the\nlast 30 amino acids of Rab3CGppNHP_Q222H_10-227 (bovine).","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6BDI9 ","statements":[{"type":"Results","text":"To decipher the binding mode, we have determined the structure of Rep15:Rab3B and Rep15:Rab3C complexes, respectively."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:135403657","statements":[{"type":"Methods","text":"The complex of Rep15 (human): Rab3CGppNHp_Q222H_10-227 (bovine) (150 μM of 1:1 complex) was crystallized in 0.1M MES pH 6.0 and 10% (w/v) PEG 6000."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888","statements":[{"type":"Figure","text":"Mg2+ ion is shown as a green sphere and GppNHp is shown in stick representation."}]}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gln222His","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The complex of Rep15 (human): Rab3CGppNHp_Q222H_10-227 (bovine) (150 μM of 1:1 complex) was\ncrystallized in 0.1M MES pH 6.0 and 10% (w/v) PEG 6000.\n"}]}],"sequence_construct":"MAHHHHHHSSGASAQDARYGQKDSSDQNFDYMFKLLIIGNSSVGKTSFLFRYADDSFTSAFVSTVGIDFKVKTVFKNEKRIKLQIWDTAGQERYRTITTAYYRGAMGFILMYDITNEESFNAVQDWSTQIKTYSWDNAQVILVGNKCDMEDERVISTERGQHLGEQLGFEFFETSAKDNINVKQTFERLVDIICDKMSESLETDPAITAAKQNTRLKETPPPPHPNCGC","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T15:59:30.162Z"}},{"start":198,"end":227,"reference_id":"35871249","reference_source":"pmid","reference_html":"Rep15 interacts with several Rab GTPases and has a distinct fold for a Rab effector. <i> Rai A, Singh AK, Bleimling N, Posern G, Vetter IR, Goody RS. </i> Nat Commun, 2022","date":"2023-04-20T09:44:11.925Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"8A4A"}],"region_id":"DP04023r002","statement":[{"text":"No\nelectron density was observed for the first 16 amino acids and the\nlast 30 amino acids of Rab3CGppNHP_Q222H_10-227 (bovine).","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6BDI9","statements":[{"type":"Results","text":"To decipher the binding mode, we have determined the structure of Rep15:Rab3B and Rep15:Rab3C complexes, respectively."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:135403657","statements":[{"type":"Methods","text":"The complex of Rep15 (human): Rab3CGppNHp_Q222H_10-227 (bovine) (150 μM of 1:1 complex) was crystallized in 0.1M MES pH 6.0 and 10% (w/v) PEG 6000."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888","statements":[{"type":"Figure","text":"Mg2+ ion is shown as a green sphere and GppNHp is shown in stick representation."}]}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gln222His","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The complex of Rep15 (human): Rab3CGppNHp_Q222H_10-227 (bovine) (150 μM of 1:1 complex) was\ncrystallized in 0.1M MES pH 6.0 and 10% (w/v) PEG 6000.\n"}]}],"sequence_construct":"MAHHHHHHSSGASAQDARYGQKDSSDQNFDYMFKLLIIGNSSVGKTSFLFRYADDSFTSAFVSTVGIDFKVKTVFKNEKRIKLQIWDTAGQERYRTITTAYYRGAMGFILMYDITNEESFNAVQDWSTQIKTYSWDNAQVILVGNKCDMEDERVISTERGQHLGEQLGFEFFETSAKDNINVKQTFERLVDIICDKMSESLETDPAITAAKQNTRLKETPPPPHPNCGC","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T15:59:26.428Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MRHEAPMQMASAQDARYGQKDSSDQNFDYMFKLLIIGNSSVGKTSFLFRYADDSFTSAFVSTVGIDFKVKTVFKNEKRIKLQIWDTAGQERYRTITTAYYRGAMGFILMYDITNEESFNAVQDWSTQIKTYSWDNAQVILVGNKCDMEDERVISTERGQHLGEQLGFEFFETSAKDNINVKQTFERLVDIICDKMSESLETDPAITAAKQNTRLKETPPPPQPNCGC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"alphafold_very_low_content":0.16740088105726872,"disorder_content":0.2026431718061674,"disprot_consensus":{"full":[{"start":10,"end":25,"type":"D"},{"start":198,"end":227,"type":"D"}],"Structural state":[{"start":10,"end":25,"type":"D"},{"start":198,"end":227,"type":"D"}]}},{"disprot_id":"DP04024","acc":"P63040","creator":"zskalman","date":"2023-03-21T10:13:05.739Z","features":{"pfam":[{"id":"PF05835","name":"Synaphin protein","start":1,"end":132}],"gene3D":[]},"genes":[{"name":{"value":"Cplx1"}}],"length":134,"name":"Complexin-1","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":71,"end":134,"reference_id":"35777466","reference_source":"pmid","reference_html":"Membrane Binding Induces Distinct Structural Signatures in the Mouse Complexin-1C-Terminal Domain. <i> Grasso EM, Terakawa MS, Lai AL, Xue Xie Y, Ramlall TF, Freed JH, Eliezer D. </i> J Mol Biol, 2023","date":"2023-04-20T12:42:52.472Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04024r001","statement":[{"text":"In the absence of lipids, the CD spectrum of the\nmCpx1 CTD is consistent with the protein being\nlargely disordered in solution, but a slight\ndecrease in signal around 220 nm that indicates\nthe unbound protein contains some helical\nstructure (Figure 3(A)). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T15:59:47.052Z"}},{"start":71,"end":134,"reference_id":"35777466","reference_source":"pmid","reference_html":"Membrane Binding Induces Distinct Structural Signatures in the Mouse Complexin-1C-Terminal Domain. <i> Grasso EM, Terakawa MS, Lai AL, Xue Xie Y, Ramlall TF, Freed JH, Eliezer D. </i> J Mol Biol, 2023","date":"2023-03-21T10:24:42.308Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"BMRB","id":"51396"}],"region_id":"DP04024r002","statement":[{"text":"These observations are further corroborated by\nps-ns backbone relaxation data collected on both\nfree and micelle-bound mCpx1 CTD. In the\nabsence of micelles,15N R1 and R2\nmeasurements, along with heteronuclear {1H-15N}\nNOE (hetNOE) data are consistent with the\nprotein being disordered in solution (Figure 4, S4).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-11T15:06:49.804Z"}},{"start":114,"end":134,"reference_id":"35777466","reference_source":"pmid","reference_html":"Membrane Binding Induces Distinct Structural Signatures in the Mouse Complexin-1C-Terminal Domain. <i> Grasso EM, Terakawa MS, Lai AL, Xue Xie Y, Ramlall TF, Freed JH, Eliezer D. </i> J Mol Biol, 2023","date":"2023-04-11T15:07:32.019Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"BMRB","id":"51397"}],"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"78018","operator":null,"partner_start":null,"partner_end":null},{"db":"ChEBI","id":"52360","operator":"or","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"60285","operator":"and","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"60568","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04024r003","statement":[{"text":"Comparison of 2D {15N-1H} HSQC spectra for free and DPC-bound mCpx1 CTD revealed that spectroscopic changes between the two states are limited to specific residues in the protein (Figure 2(A)).","type":"Results"},{"text":"Residues that are significantly affected by the presence of micelles all fall in the C-terminus of the CTD, specifically the terminal ∼ 20 residues (114–134). These residues exhibit both chemical shift perturbations (CSPs) (Figure 2(B)) and attenuated signal intensities (Figure 2(C)) in the presence of micelles. Together, these data suggest that the C-terminus of the mCpx1 CTD is interacting with DPC-micelles while the N-terminal regions of the CTD are largely unaffected.","type":"Results"},{"text":"Comparison of 2D {15N-1H} HSQC spectra for the mCpx1 CTD free or bound to SUVs with two different lipid compositions (60% DOPC/25% DOPE/15% DOPS and 85% POPC/15% POPS) revealed significant attenuation of peak heights in the presence of SUVs (Figure 5(A)), without detectable chemical shift changes. There is a global decrease in signal intensity for all peaks in the SUV-bound spectra, but the C-terminal 20 residues show a greater decrease in intensity for both SUV compositions (Figure 5(B)) indicating that this region is interacting strongly with SUVs irrespective of their composition.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":114,"end":134,"reference_id":"35777466","reference_source":"pmid","reference_html":"Membrane Binding Induces Distinct Structural Signatures in the Mouse Complexin-1C-Terminal Domain. <i> Grasso EM, Terakawa MS, Lai AL, Xue Xie Y, Ramlall TF, Freed JH, Eliezer D. </i> J Mol Biol, 2023","date":"2023-04-11T15:03:48.588Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"BMRB","id":"51397"}],"region_id":"DP04024r004","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"78018","entry_name":"dodecylphosphocholine"}],"statement":[{"text":"In the presence of DPC-micelles, two distinct regions in the C-terminus of the mCpx1 CTD, encompassing residues 116–124 and 128–133, form stable helical structure (Figure 3(C), Figure S3(B-C)) that is not observed in the absence of micelles.","type":"Results"},{"text":"Residues spanning the regions from ∼ 114–124 and 128–133 showed clear NH-NH NOEs from residue i to i ± 1, characteristic of helical structure, consistent with the regions defined as helical in the TALOS-N predictions. Residues 125–127 consist of Pro-Gly-Pro, precluding the observation of NH-NH i to i + 1 NOEs. However, this sequence is highly unfavorable for helical structure and likely represents a break between the two helices, as indicated by the chemical shift-based prediction.","type":"Results"},{"text":"Notably, residues 125–127, constituting the non-helical PGP linker between the AH- and CT-motif helices, does not exhibit indications of increase mobility, suggesting that in the micelle-bound conformation, the linker conformation, while non-helical, may be relatively fixed.","type":"Results"}]}],"regions_counter":4,"released":"2024_06","sequence":"MEFVMKQALGGATKDMGKMLGGDEEKDPDAAKKEEERQEALRQAEEERKAKYAKMEAEREVMRQGIRDKYGIKKKEEREAEAQAAMEANSEGSLTRPKKAIPPGCGDEPEEEDESILDTVIKYLPGPLQDMFKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"alphafold_very_low_content":0.05970149253731343,"disorder_content":0.47761194029850745,"disprot_consensus":{"full":[{"start":71,"end":113,"type":"D"},{"start":114,"end":134,"type":"T"}],"Structural state":[{"start":71,"end":134,"type":"D"}],"Molecular function":[{"start":114,"end":134,"type":"F"}],"Structural transition":[{"start":114,"end":134,"type":"T"}]}},{"disprot_id":"DP04026","acc":"P53228","creator":"zskalman","date":"2023-03-21T14:57:28.086Z","features":{"pfam":[{"id":"PF00923","name":"Transaldolase/Fructose-6-phosphate aldolase","start":26,"end":327}],"gene3D":[]},"genes":[{"name":{"value":"NQM1"},"olnNames":[{"value":"YGR043C"}]}],"length":333,"name":"Transaldolase NQM1","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":11,"reference_id":"18831051","reference_source":"pmid","reference_html":"The crystal structure and identification of NQM1/YGR043C, a transaldolase from Saccharomyces cerevisiae. <i> Huang H, Rong H, Li X, Tong S, Zhu Z, Niu L, Teng M. </i> Proteins, 2008","date":"2023-04-20T12:51:15.962Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3CQ0"}],"region_id":"DP04026r001","statement":[{"text":"The final\nmodel displayed excellent geometry except for the first\neleven amino acids (amino acids 1–11 at the N-terminus,\nboth in molecule A and B) and a region of an outside\nloop (203–205 in molecule A and 202–206 in molecule\nB), which were disordered in the crystal.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEMBL","id":"8200","statements":[{"type":"Methods","text":"During the data collection, the crystal was maintained at 100 K using nitrogen gas with cryoprotection\n(1.2 M potassium citrate, 8% polyethylene glycol 200, 1% ethylene glycol, 0.09 mM HEPES, pH 7.3, and 15% glycerol)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:174","statements":[{"type":"Methods","text":"During the data collection, the crystal was maintained at 100 K using nitrogen gas with cryoprotection\n(1.2 M potassium citrate, 8% polyethylene glycol 200, 1% ethylene glycol, 0.09 mM HEPES, pH 7.3, and 15% glycerol)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753","statements":[{"type":"Methods","text":"During the data collection, the crystal was maintained at 100 K using nitrogen gas with cryoprotection\n(1.2 M potassium citrate, 8% polyethylene glycol 200, 1% ethylene glycol, 0.09 mM HEPES, pH 7.3, and 15% glycerol).\n"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T16:01:10.241Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MSEPSEKKQKVATSSLEQLKKAGTHVVADSGDFEAISKYEPQDSTTNPSLILAASKLEKYARFIDAAVEYGRKHGKTDHEKIENAMDKILVEFGTQILKVVPGRVSTEVDARLSFDKKATVKKALHIIKLYKDAGVPKERVLIKIASTWEGIQAARELEVKHGIHCNMTLLFSFTQAVACAEANVTLISPFVGRIMDFYKALSGKDYTAETDPGVLSVKKIYSYYKRHGYATEVMAASFRNLDELKALAGIDNMTLPLNLLEQLYESTDPIENKLNSESAKEEGVEKVSFINDEPHFRYVLNEDQMATEKLSDGIRKFSADIEALYKLVEEKM","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.02702702702702703,"disorder_content":0.03303303303303303,"disprot_consensus":{"full":[{"start":1,"end":11,"type":"D"}],"Structural state":[{"start":1,"end":11,"type":"D"}]}},{"disprot_id":"DP04027","acc":"P37837","creator":"zskalman","date":"2023-03-21T14:59:43.550Z","features":{"pfam":[{"id":"PF00923","name":"Transaldolase/Fructose-6-phosphate aldolase","start":24,"end":325}],"gene3D":[]},"genes":[{"name":{"value":"TALDO1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11559","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11559"}}]},"synonyms":[{"value":"TAL"},{"value":"TALDO"},{"value":"TALDOR"}]}],"length":337,"name":"Transaldolase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":10,"reference_id":"10869557","reference_source":"pmid","reference_html":"The three-dimensional structure of human transaldolase. <i> Thorell S, Gergely P, Banki K, Perl A, Schneider G. </i> FEBS Lett, 2000","date":"2023-05-24T16:00:37.323Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1F05"}],"region_id":"DP04027r001","statement":[{"text":"In the electron density maps, the polypeptide chain is well defined except for 10 residues at the N-terminus and five residues at the C-terminus.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T17:15:46.643Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MSSSPVKRQRMESALDQLKQFTTVVADTGDFHAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGRKLGGSQEDQIKNAIDKLFVLFGAEILKKIPGRVSTEVDARLSFDKDAMVARARRLIELYKEAGISKDRILIKLSSTWEGIQAGKELEEQHGIHCNMTLLFSFAQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPLEDPGVKSVTKIYNYYKKFSYKTIVMGASFRNTGEIKALAGCDFLTISPKLLGELLQDNAKLVPVLSAKAAQASDLEKIHLDEKSFRWLHNEDQMAVEKLSDGIRKFAADAVKLERMLTERMFNAENGK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.026706231454005934,"disorder_content":0.02967359050445104,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"}]}},{"disprot_id":"DP04028","acc":"Q9CA59","creator":"zskalman","date":"2023-03-21T15:17:48.183Z","features":{"pfam":[{"id":"PF00956","name":"Nucleosome assembly protein (NAP)","start":75,"end":215}],"gene3D":[]},"genes":[{"name":{"value":"NRP1"},"synonyms":[{"value":"NFA6"}],"orfNames":[{"value":"F1M20.24"}],"olnNames":[{"value":"At1g74560"}]}],"length":256,"name":"NAP1-related protein 1","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":225,"end":255,"reference_id":"33199628","reference_source":"pmid","reference_html":"NAP1-Related Protein 1 (NRP1) has multiple interaction modes for chaperoning histones H2A-H2B. <i> Luo Q, Wang B, Wu Z, Jiang W, Wang Y, Du K, Zhou N, Zheng L, Gan J, Shen WH, Ma J, Dong A. </i> Proc Natl Acad Sci U S A, 2020","date":"2023-05-24T07:48:56.466Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7C7X"}],"region_id":"DP04028r001","statement":[{"text":"Although our previous study showed that\nNRP1 CTAD (amino acids 225 to 255) contributes to H2A-H2B\nbinding and is important for the function of NRP1 in planta (18),\nthe CTAD domain was disordered in the NRP1-H2A-H2B\ncomplex.","type":"Results"},{"text":"The CTAD domain is invisible in the electron density map.","type":"Figure"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9LQQ4","statements":[{"type":"Introduction","text":"Finally, we solved three crystal structures of C-terminal acidic domains (CTADs) of NRP1 and\nhuman NAP1 in complex with H2A-H2B, revealing a conserved histone binding mode among NAP1 family proteins.\n"}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9LD28","statements":[{"type":"Introduction","text":"Finally, we solved three crystal structures of C-terminal acidic domains (CTADs) of NRP1 and\nhuman NAP1 in complex with H2A-H2B, revealing a conserved histone binding mode among NAP1 family proteins.\n"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753","statements":[{"type":"Supplementary material","text":"Crystals were flash-frozen in the mother solution supplemented with 25% glycerol."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T12:45:03.845Z"}},{"start":226,"end":232,"reference_id":"33199628","reference_source":"pmid","reference_html":"NAP1-Related Protein 1 (NRP1) has multiple interaction modes for chaperoning histones H2A-H2B. <i> Luo Q, Wang B, Wu Z, Jiang W, Wang Y, Du K, Zhou N, Zheng L, Gan J, Shen WH, Ma J, Dong A. </i> Proc Natl Acad Sci U S A, 2020","date":"2023-04-20T13:26:59.536Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"GO:0042393","term_name":"histone binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7BP6"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9LD28","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9LQQ4","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04028r002","statement":[{"text":"Finally, we solved three crystal\nstructures of C-terminal acidic domains (CTADs) of NRP1 and\nhuman NAP1 in complex with H2A-H2B, revealing a conserved\nhistone binding mode among NAP1 family proteins.","type":"Introduction"},{"text":"To reveal how NRP1 CTAD interacts with H2A-H2B, we solved the structure of H2A-H2B in complex with CTAD peptide D226-F232 (SI Appendix, Table S2). All seven residues (D226 to F232) of CTAD are well ordered in the cocrystal structure and engage H2A L2 and H2B L1 (Fig. 4A), and electronegative residues D228, E229, E230, and D231 within NRP1 CTAD are cocooned by the positively charged groove of H2A-H2B (SI Appendix, Fig. S6A).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a histone, any of a group of water-soluble proteins found in association with the DNA of eukaroytic chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in nonspecific suppression of gene activity.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T12:45:12.103Z"}},{"start":165,"end":184,"reference_id":"33199628","reference_source":"pmid","reference_html":"NAP1-Related Protein 1 (NRP1) has multiple interaction modes for chaperoning histones H2A-H2B. <i> Luo Q, Wang B, Wu Z, Jiang W, Wang Y, Du K, Zhou N, Zheng L, Gan J, Shen WH, Ma J, Dong A. </i> Proc Natl Acad Sci U S A, 2020","date":"2023-05-24T07:49:15.248Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7C7X"}],"region_id":"DP04028r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9LQQ4","statements":[{"type":"Introduction","text":"Finally, we solved three crystal structures of C-terminal acidic domains (CTADs) of NRP1 and\nhuman NAP1 in complex with H2A-H2B, revealing a conserved histone binding mode among NAP1 family proteins.\n"}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9LD28","statements":[{"type":"Introduction","text":"Finally, we solved three crystal structures of C-terminal acidic domains (CTADs) of NRP1 and\nhuman NAP1 in complex with H2A-H2B, revealing a conserved histone binding mode among NAP1 family proteins.\n"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753","statements":[{"type":"Supplementary material","text":"Crystals were flash-frozen in the mother solution supplemented with 25% glycerol."}]}],"statement":[{"text":"The structure deposited in PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T12:45:10.224Z"}},{"start":194,"end":203,"reference_id":"33199628","reference_source":"pmid","reference_html":"NAP1-Related Protein 1 (NRP1) has multiple interaction modes for chaperoning histones H2A-H2B. <i> Luo Q, Wang B, Wu Z, Jiang W, Wang Y, Du K, Zhou N, Zheng L, Gan J, Shen WH, Ma J, Dong A. </i> Proc Natl Acad Sci U S A, 2020","date":"2023-05-24T07:48:40.101Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7C7X"}],"region_id":"DP04028r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9LQQ4","statements":[{"type":"Introduction","text":"Finally, we solved three crystal structures of C-terminal acidic domains (CTADs) of NRP1 and\nhuman NAP1 in complex with H2A-H2B, revealing a conserved histone binding mode among NAP1 family proteins.\n"}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9LD28","statements":[{"type":"Introduction","text":"Finally, we solved three crystal structures of C-terminal acidic domains (CTADs) of NRP1 and\nhuman NAP1 in complex with H2A-H2B, revealing a conserved histone binding mode among NAP1 family proteins.\n"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753","statements":[{"type":"Supplementary material","text":"Crystals were flash-frozen in the mother solution supplemented with 25% glycerol."}]}],"statement":[{"text":"The structure deposited in PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T12:45:01.718Z"}}],"regions_counter":4,"released":"2024_06","sequence":"MVADKSKKSKIEEKGEEENLEQIDAELVLSIEKLQEIQDDLEKINEKASDEVLEVEQKYNVIRKPVYDKRNEVIQSIPGFWMTAFLSHPALGDLLTEEDQKIFKYLNSLEVEDAKDVKSGYSITFHFTSNPFFEDAKLTKTFTFLEEGTTKITATPIKWKEGKGLPNGVNHDDKKGNKRALPEESFFTWFTDAQHKEDAGDEIHDEVADIIKEDLWSNPLTYFNNDADEEDFDGDDDGDEEGEEDDDDEEEEDGEE","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"alphafold_very_low_content":0.171875,"disorder_content":0.23828125,"disprot_consensus":{"full":[{"start":165,"end":184,"type":"D"},{"start":194,"end":203,"type":"D"},{"start":225,"end":255,"type":"D"}],"Structural state":[{"start":165,"end":184,"type":"D"},{"start":194,"end":203,"type":"D"},{"start":225,"end":255,"type":"D"}],"Molecular function":[{"start":226,"end":232,"type":"F"}]}},{"disprot_id":"DP04029","acc":"Q94A79","creator":"zskalman","date":"2023-03-21T16:10:07.050Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"DMS3"},"synonyms":[{"value":"IDN1"}],"orfNames":[{"value":"F2K15.110"}],"olnNames":[{"value":"At3g49250"}]}],"length":420,"name":"Protein DEFECTIVE IN MERISTEM SILENCING 3","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":1,"end":42,"reference_id":"31477705","reference_source":"pmid","reference_html":"CryoEM structures of Arabidopsis DDR complexes involved in RNA-directed DNA methylation. <i> Wongpalee SP, Liu S, Gallego-Bartolomé J, Leitner A, Aebersold R, Liu W, Yen L, Nohales MA, Kuo PH, Vashisht AA, Wohlschlegel JA, Feng S, Kay SA, Zhou ZH, Jacobsen SE. </i> Nat Commun, 2019","date":"2023-11-24T13:40:05.284Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6OIT"},{"db":"PDB","id":"6OIS"}],"region_id":"DP04029r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9LUJ3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9SIW2"}],"statement":[{"text":"N-terminal region aa. 1–42 and C-terminal region aa. 410–420 were not visible in all DMS3 monomers of our structures, probably due to flexibility.","type":"Results"}]},{"start":410,"end":420,"reference_id":"31477705","reference_source":"pmid","reference_html":"CryoEM structures of Arabidopsis DDR complexes involved in RNA-directed DNA methylation. <i> Wongpalee SP, Liu S, Gallego-Bartolomé J, Leitner A, Aebersold R, Liu W, Yen L, Nohales MA, Kuo PH, Vashisht AA, Wohlschlegel JA, Feng S, Kay SA, Zhou ZH, Jacobsen SE. </i> Nat Commun, 2019","date":"2023-11-24T13:39:56.571Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6OIT"},{"db":"PDB","id":"6OIS"}],"region_id":"DP04029r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9LUJ3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9SIW2"}],"statement":[{"text":"N-terminal region aa. 1–42 and C-terminal region aa. 410–420 were not visible in all DMS3 monomers of our structures, probably due to flexibility.","type":"Results"}]}],"regions_counter":5,"released":"2024_06","sequence":"MYPTGQQISFQTTPLNVQDPTRMMNLDQSSPVARNETQNGGGIAHAEFAMFNSKRLESDLEAMGNKIKQHEDNLKFLKSQKNKMDEAIVDLQVHMSKLNSSPTPRSENSDNSLQGEDINAQILRHENSAAGVLSLVETLHGAQASQLMLTKGVVGVVAKLGKVNDENLSQILSNYLGTRSMLAVVCRNYESVTALEAYDNHGNIDINAGLHCLGSSIGREIGDSFDAICLENLRPYVGQHIADDLQRRLDLLKPKLPNGECPPGFLGFAVNMIQIDPAYLLCVTSYGYGLRETLFYNLFSRLQVYKTRADMISALPCISDGAVSLDGGIIRKTGIFNLGNRDEVNVRFAKPTASRTMDNYSEAEKKMKELKWKKEKTLEDIKREQVLREHAVFNFGKKKEEFVRCLAQSSCTNQPMNTPR","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"alphafold_very_low_content":0.15,"disorder_content":0.1261904761904762,"disprot_consensus":{"full":[{"start":1,"end":42,"type":"D"},{"start":410,"end":420,"type":"D"}],"Structural state":[{"start":1,"end":42,"type":"D"},{"start":410,"end":420,"type":"D"}]}},{"disprot_id":"DP04030","acc":"P41743","creator":"zskalman","date":"2023-03-22T12:23:50.370Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":255,"end":521},{"id":"PF00130","name":"Phorbol esters/diacylglycerol binding domain (C1 domain)","start":141,"end":192},{"id":"PF00433","name":"Protein kinase C terminal domain","start":546,"end":584},{"id":"PF00564","name":"PB1 domain","start":26,"end":107}],"gene3D":[]},"genes":[{"name":{"value":"PRKCI"},"synonyms":[{"value":"DXS1179E"}]}],"length":596,"name":"Protein kinase C iota type","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":233,"end":248,"reference_id":"16125198","reference_source":"pmid","reference_html":"Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif. <i> Messerschmidt A, Macieira S, Velarde M, Bädeker M, Benda C, Jestel A, Brandstetter H, Neuefeind T, Blaesse M. </i> J Mol Biol, 2005","date":"2023-05-24T08:16:14.109Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006222","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1ZRZ"}],"region_id":"DP04030r001","statement":[{"text":"Amino acid stretches with\nhigh B-values and therefore poorly defined electron\ndensity are: residues 224–239 from the N terminus,\n446–454 from the PKCi extended loop, 533–551 from\nthe turn motif and 580–587 at the very C terminus.","type":"Methods"},{"text":"The numbering of the amino acids in the structure is shifted compared to the reference sequence in Uniprot.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:2396","statements":[{"type":"Methods","text":"The final model contains protein residues 240–445,\n455–532, and 552–579, two phosphate groups attached\nto Thr403 and Thr555, one bis(indolyl)maleimide 1\nmolecule, and 42 water molecules, and constitutes a\nwell-defined structure.\n"}]}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu485Met","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.His508Leu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro560Arg","start":null,"end":null,"position":null},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":412,"end":412,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":564,"end":564,"position":"Specific residue"}],"sequence_construct":"EKEAMNTRESGKASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTDRIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIRIPRSMSVKAASVLKSFLNKDPKERLGCLPQTGFADIQGHPFFRNVDWDMMEQKQVVPPFKPNISGEFGLDNFDSQFTNERVQLTPDDDDIVRKIDQSEFEGFEYINPLLMSAEECV","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T12:46:46.549Z"}},{"start":542,"end":560,"reference_id":"16125198","reference_source":"pmid","reference_html":"Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif. <i> Messerschmidt A, Macieira S, Velarde M, Bädeker M, Benda C, Jestel A, Brandstetter H, Neuefeind T, Blaesse M. </i> J Mol Biol, 2005","date":"2023-05-24T08:14:48.101Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006222","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1ZRZ"}],"region_id":"DP04030r002","statement":[{"text":"Amino acid stretches with\nhigh B-values and therefore poorly defined electron\ndensity are: residues 224–239 from the N terminus,\n446–454 from the PKCi extended loop, 533–551 from\nthe turn motif and 580–587 at the very C terminus.","type":"Methods"},{"text":"The numbering of the amino acids in the structure is shifted compared to the reference sequence in Uniprot.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:2396","statements":[{"type":"Methods","text":"The final model contains protein residues 240–445,\n455–532, and 552–579, two phosphate groups attached\nto Thr403 and Thr555, one bis(indolyl)maleimide 1\nmolecule, and 42 water molecules, and constitutes a\nwell-defined structure.\n"}]}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu485Met","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.His508Leu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro560Arg","start":null,"end":null,"position":null},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":412,"end":412,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":564,"end":564,"position":"Specific residue"}],"sequence_construct":"EKEAMNTRESGKASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTDRIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIRIPRSMSVKAASVLKSFLNKDPKERLGCLPQTGFADIQGHPFFRNVDWDMMEQKQVVPPFKPNISGEFGLDNFDSQFTNERVQLTPDDDDIVRKIDQSEFEGFEYINPLLMSAEECV","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T12:46:45.253Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MPTQRDSSTMSHTVAGGGSGDHSHQVRVKAYYRGDIMITHFEPSISFEGLCNEVRDMCSFDNEQLFTMKWIDEEGDPCTVSSQLELEEAFRLYELNKDSELLIHVFPCVPERPGMPCPGEDKSIYRRGARRWRKLYCANGHTFQAKRFNRRAHCAICTDRIWGLGRQGYKCINCKLLVHKKCHKLVTIECGRHSLPQEPVMPMDQSSMHSDHAQTVIPYNPSSHESLDQVGEEKEAMNTRESGKASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTDRIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIRIPRSLSVKAASVLKSFLNKDPKERLGCHPQTGFADIQGHPFFRNVDWDMMEQKQVVPPFKPNISGEFGLDNFDSQFTNEPVQLTPDDDDIVRKIDQSEFEGFEYINPLLMSAEECV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.13590604026845637,"disorder_content":0.0587248322147651,"disprot_consensus":{"full":[{"start":233,"end":248,"type":"D"},{"start":542,"end":560,"type":"D"}],"Structural state":[{"start":233,"end":248,"type":"D"},{"start":542,"end":560,"type":"D"}]}},{"disprot_id":"DP04032","acc":"Q6ZT98","creator":"zskalman","date":"2023-03-22T15:30:44.946Z","features":{"pfam":[{"id":"PF03133","name":"Tubulin-tyrosine ligase family","start":90,"end":378}],"gene3D":[]},"genes":[{"name":{"value":"TTLL7","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:26242","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:26242"}}]}}],"length":887,"name":"Tubulin polyglutamylase TTLL7","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":236,"end":268,"reference_id":"25959773","reference_source":"pmid","reference_html":"Multivalent Microtubule Recognition by Tubulin Tyrosine Ligase-like Family Glutamylases. <i> Garnham CP, Vemu A, Wilson-Kubalek EM, Yu I, Szyk A, Lander GC, Milligan RA, Roll-Mecak A. </i> Cell, 2015","date":"2023-05-24T07:38:41.610Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4YLR"},{"db":"PDB","id":"4YLS"}],"region_id":"DP04032r001","statement":[{"text":"Ribbon representation of the TTLL7 core bound to ADP. Nucleotide shown as a stick model. Spheres represent disordered polypeptide chain regions. c-MTBD residues, orange spheres.","type":"Figure"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:33113","statements":[{"type":"Curator statement","text":"PDB:4YLS"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022","statements":[{"type":"Curator statement","text":"PDB:4YLR"}]}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu349Gln","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"In both structures."}]}],"sequence_construct":"GSFTKKKGTITANVAGTKFEIVRLVIDEMGFMKTPDEDETSNLIWCDSAVQQEKISELQNYQRINHFPGMGEICRKDFLARNMTKMIKSRPLDYTFVPRTWIFPAEYTQFQNYVKELKKKRKQKTFIVKPANGAMGHGISLIRNGDKLPSQDHLIVQEYIEKPFLMEGYKFDLRIYILVTSCDPLKIFLYHDGLVRMGTEKYIPPNESNLTQLYMHLTNYSVNKHNEHFERDETENKGSKRSIKWFTEFLQANQHDVAKFWSDISELVVKTLIVAEPHVLHAYRMCRPGQPPGSESVCFEVLGFDILLDRKLKPWLLQINRAPSFGTDQKIDYDVKRGVLLNALKLLNIRTSDKRRNLAKQKAEAQRRLYGQNSIKRLLPGSSDWEQQRHQLERRKEELKERLAQVRKQISREEHENRHMGNYRRIYPPEDKALLEKYENLLAVAFQTFLSGRAASFQRELNNPLKRMKEEDILDLLEQCEIDDEKL","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T12:40:53.601Z"}},{"start":383,"end":450,"reference_id":"25959773","reference_source":"pmid","reference_html":"Multivalent Microtubule Recognition by Tubulin Tyrosine Ligase-like Family Glutamylases. <i> Garnham CP, Vemu A, Wilson-Kubalek EM, Yu I, Szyk A, Lander GC, Milligan RA, Roll-Mecak A. </i> Cell, 2015","date":"2023-05-24T07:38:06.135Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4YLR"},{"db":"PDB","id":"4YLS"}],"region_id":"DP04032r002","statement":[{"text":"Ribbon representation of the TTLL7 core bound to ADP. Nucleotide shown as a stick model. Spheres represent disordered polypeptide chain regions. c-MTBD residues, orange spheres.","type":"Figure"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022","statements":[{"type":"Curator statement","text":"PDB:4YLR"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:33113","statements":[{"type":"Curator statement","text":"PDB:4YLS"}]}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu349Gln","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"In both structures."}]}],"sequence_construct":"GSFTKKKGTITANVAGTKFEIVRLVIDEMGFMKTPDEDETSNLIWCDSAVQQEKISELQNYQRINHFPGMGEICRKDFLARNMTKMIKSRPLDYTFVPRTWIFPAEYTQFQNYVKELKKKRKQKTFIVKPANGAMGHGISLIRNGDKLPSQDHLIVQEYIEKPFLMEGYKFDLRIYILVTSCDPLKIFLYHDGLVRMGTEKYIPPNESNLTQLYMHLTNYSVNKHNEHFERDETENKGSKRSIKWFTEFLQANQHDVAKFWSDISELVVKTLIVAEPHVLHAYRMCRPGQPPGSESVCFEVLGFDILLDRKLKPWLLQINRAPSFGTDQKIDYDVKRGVLLNALKLLNIRTSDKRRNLAKQKAEAQRRLYGQNSIKRLLPGSSDWEQQRHQLERRKEELKERLAQVRKQISREEHENRHMGNYRRIYPPEDKALLEKYENLLAVAFQTFLSGRAASFQRELNNPLKRMKEEDILDLLEQCEIDDEKL","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T12:40:54.524Z"}},{"start":485,"end":518,"reference_id":"25959773","reference_source":"pmid","reference_html":"Multivalent Microtubule Recognition by Tubulin Tyrosine Ligase-like Family Glutamylases. <i> Garnham CP, Vemu A, Wilson-Kubalek EM, Yu I, Szyk A, Lander GC, Milligan RA, Roll-Mecak A. </i> Cell, 2015","date":"2023-05-24T08:43:40.760Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4YLR"},{"db":"PDB","id":"4YLS"}],"region_id":"DP04032r003","statement":[{"text":"Ribbon representation of the TTLL7 core bound to ADP. Nucleotide shown as a stick model. Spheres represent disordered polypeptide chain regions. c-MTBD residues, orange spheres.","type":"Figure"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:33113","statements":[{"type":"Curator statement","text":"PDB:4YLS"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022","statements":[{"type":"Curator statement","text":"PDB:4YLR"}]}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu349Gln","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"In both structures."}]}],"sequence_construct":"GSFTKKKGTITANVAGTKFEIVRLVIDEMGFMKTPDEDETSNLIWCDSAVQQEKISELQNYQRINHFPGMGEICRKDFLARNMTKMIKSRPLDYTFVPRTWIFPAEYTQFQNYVKELKKKRKQKTFIVKPANGAMGHGISLIRNGDKLPSQDHLIVQEYIEKPFLMEGYKFDLRIYILVTSCDPLKIFLYHDGLVRMGTEKYIPPNESNLTQLYMHLTNYSVNKHNEHFERDETENKGSKRSIKWFTEFLQANQHDVAKFWSDISELVVKTLIVAEPHVLHAYRMCRPGQPPGSESVCFEVLGFDILLDRKLKPWLLQINRAPSFGTDQKIDYDVKRGVLLNALKLLNIRTSDKRRNLAKQKAEAQRRLYGQNSIKRLLPGSSDWEQQRHQLERRKEELKERLAQVRKQISREEHENRHMGNYRRIYPPEDKALLEKYENLLAVAFQTFLSGRAASFQRELNNPLKRMKEEDILDLLEQCEIDDEKL","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T12:40:52.357Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MPSLPQEGVIQGPSPLDLNTELPYQSTMKRKVRKKKKKGTITANVAGTKFEIVRLVIDEMGFMKTPDEDETSNLIWCDSAVQQEKISELQNYQRINHFPGMGEICRKDFLARNMTKMIKSRPLDYTFVPRTWIFPAEYTQFQNYVKELKKKRKQKTFIVKPANGAMGHGISLIRNGDKLPSQDHLIVQEYIEKPFLMEGYKFDLRIYILVTSCDPLKIFLYHDGLVRMGTEKYIPPNESNLTQLYMHLTNYSVNKHNEHFERDETENKGSKRSIKWFTEFLQANQHDVAKFWSDISELVVKTLIVAEPHVLHAYRMCRPGQPPGSESVCFEVLGFDILLDRKLKPWLLEINRAPSFGTDQKIDYDVKRGVLLNALKLLNIRTSDKRRNLAKQKAEAQRRLYGQNSIKRLLPGSSDWEQQRHQLERRKEELKERLAQVRKQISREEHENRHMGNYRRIYPPEDKALLEKYENLLAVAFQTFLSGRAASFQRELNNPLKRMKEEDILDLLEQCEIDDEKLMGKTTKTRGPKPLCSMPESTEIMKRPKYCSSDSSYDSSSSSSESDENEKEEYQNKKREKQVTYNLKPSNHYKLIQQPSSIRRSVSCPRSISAQSPSSGDTRPFSAQQMISVSRPTSASRSHSLNRASSYMRHLPHSNDACSTNSQVSESLRQLKTKEQEDDLTSQTLFVLKDMKIRFPGKSDAESELLIEDIIDNWKYHKTKVASYWLIKLDSVKQRKVLDIVKTSIRTVLPRIWKVPDVEEVNLYRIFNRVFNRLLWSRGQGLWNCFCDSGSSWESIFNKSPEVVTPLQLQCCQRLVELCKQCLLVVYKYATDKRGSLSGIGPDWGNSRYLLPGSTQFFLRTPTYNLKYNSPGMTRSNVLFTSRYGHL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.27959413754227735,"disorder_content":0.15219842164599776,"disprot_consensus":{"full":[{"start":236,"end":268,"type":"D"},{"start":383,"end":450,"type":"D"},{"start":485,"end":518,"type":"D"}],"Structural state":[{"start":236,"end":268,"type":"D"},{"start":383,"end":450,"type":"D"},{"start":485,"end":518,"type":"D"}]}},{"disprot_id":"DP04033","acc":"O15431","creator":"eficho","date":"2023-03-23T09:50:31.031Z","features":{"pfam":[{"id":"PF04145","name":"Ctr copper transporter family","start":45,"end":175}],"gene3D":[]},"genes":[{"name":{"value":"SLC31A1"},"synonyms":[{"value":"COPT1"},{"value":"CTR1"}]}],"length":190,"name":"High affinity copper uptake protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":52,"reference_id":"36409899","reference_source":"pmid","reference_html":"Intrinsically disordered ectodomain modulates ion permeation through a metal transporter. <i> Aupič J, Lapenta F, Janoš P, Magistrato A. </i> Proc Natl Acad Sci U S A, 2022","date":"2024-08-29T08:52:06.124Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04033r001","statement":[{"text":"The measured spectra were in good agreement with the theoretical spectra predicted for the conformational ensembles obtained with HREX, validating the identified structures. In the absence of Cu(I) ions, the experimental CD spectrum exhibited a strong negative band at 200 nm, in agreement with that calculated for the Nterm in the unfolded state.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:41:24.235Z"}},{"start":1,"end":52,"reference_id":"36409899","reference_source":"pmid","reference_html":"Intrinsically disordered ectodomain modulates ion permeation through a metal transporter. <i> Aupič J, Lapenta F, Janoš P, Magistrato A. </i> Proc Natl Acad Sci U S A, 2022","date":"2024-08-29T08:54:24.493Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04033r002","statement":[{"text":"Conversely, measuring in the presence of sodium dodecyl sulfate (SDS) micelles, previously reported to affect Nterm conformation (19), resulted in an additional negative peak at 220 nm, corresponding to the CD spectrum predicted for the alpha state. Taken together, this suggests the conformation of the Nterm is modulated by the presence of Cu(I) ions and lipid molecules. While Cu(I) binding promotes the transition of the Nterm from the unfolded to the beta conformation, the interaction with lipid molecules leads to the formation of α-helical fragments as seen in the alpha state. ","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"8984","entry_name":"sodium dodecyl sulfate"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:42:07.549Z"}},{"start":1,"end":52,"reference_id":"36409899","reference_source":"pmid","reference_html":"Intrinsically disordered ectodomain modulates ion permeation through a metal transporter. <i> Aupič J, Lapenta F, Janoš P, Magistrato A. </i> Proc Natl Acad Sci U S A, 2022","date":"2024-05-13T21:39:10.084Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04033r003","statement":[{"text":"The measured spectra were in good agreement with the theoretical spectra predicted for the conformational ensembles obtained with HREX, validating the identified structures. In the absence of Cu(I) ions, the experimental CD spectrum exhibited a strong negative band at 200 nm, in agreement with that calculated for the Nterm in the unfolded state.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-08-19T12:55:26.037Z"}},{"start":1,"end":52,"reference_id":"36409899","reference_source":"pmid","reference_html":"Intrinsically disordered ectodomain modulates ion permeation through a metal transporter. <i> Aupič J, Lapenta F, Janoš P, Magistrato A. </i> Proc Natl Acad Sci U S A, 2022","date":"2024-08-29T08:53:41.117Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04033r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"49552","entry_name":"copper(1+)"}],"statement":[{"text":"The addition of Cu(I) ions reduced the depth of the minimum, so that the experimental CD spectrum matched that calculated for the beta state.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:41:43.460Z"}},{"start":1,"end":52,"reference_id":"36409899","reference_source":"pmid","reference_html":"Intrinsically disordered ectodomain modulates ion permeation through a metal transporter. <i> Aupič J, Lapenta F, Janoš P, Magistrato A. </i> Proc Natl Acad Sci U S A, 2022","date":"2024-09-17T09:44:55.250Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005507","term_name":"copper ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"49552","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04033r005","statement":[{"text":"While Cu(I) binding promotes the transition of the Nterm from the unfolded to the beta conformation, the interaction with lipid molecules leads to the formation of α-helical fragments as seen in the alpha state.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a copper (Cu) ion.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":5,"released":"2024_12","sequence":"MDHSHHMGMSYMDSNSTMQPSHHHPTTSASHSHGGGDSSMMMMPMTFYFGFKNVELLFSGLVINTAGEMAGAFVAVFLLAMFYEGLKIARESLLRKSQVSIRYNSMPVPGPNGTILMETHKTVGQQMLSFPHLLQTVLHIIQVVISYFLMLIFMTYNGYLCIAVAAGAGTGYFLFSWKKAVVVDITEHCH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.14210526315789473,"disorder_content":0.2736842105263158,"disprot_consensus":{"full":[{"start":1,"end":52,"type":"T"}],"Structural state":[{"start":1,"end":52,"type":"D"}],"Structural transition":[{"start":1,"end":52,"type":"T"}],"Disorder function":[{"start":1,"end":52,"type":"F"}],"Molecular function":[{"start":1,"end":52,"type":"F"}]}},{"disprot_id":"DP04035","acc":"Q8RN04","creator":"ldobson","date":"2023-03-24T15:19:20.231Z","features":{"pfam":[{"id":"PF00067","name":"Cytochrome P450","start":218,"end":369}],"gene3D":[]},"genes":[{"name":{"value":"cyp165B3"},"synonyms":[{"value":"oxyB"}]}],"length":398,"name":"Cytochrome P450 165B3","ncbi_taxon_id":31958,"organism":"Amycolatopsis orientalis","regions":[{"start":70,"end":82,"reference_id":"12207020","reference_source":"pmid","reference_html":"Crystal structure of OxyB, a cytochrome P450 implicated in an oxidative phenol coupling reaction during vancomycin biosynthesis. <i> Zerbe K, Pylypenko O, Vitali F, Zhang W, Rouset S, Heck M, Vrijbloed JW, Bischoff D, Bister B, Süssmuth RD, Pelzer S, Wohlleben W, Robinson JA, Schlichting I. </i> J Biol Chem, 2002","date":"2023-03-24T15:22:15.542Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1LFK"}],"region_id":"DP04035r001","statement":[{"text":"There\nis very weak electron density for most of the region corresponding\nto the B'-helix in one of the AS crystal forms, whereas in the\nPEG crystal form the residues between Arg65 and Glu83 are\nmissing.","type":"Results"},{"text":"Table 1 also indicates missing residues.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-19T15:24:23.893Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MSEDDPRPLHIRRQGLDPADELLAAGALTRVTIGSGADAETHWMATAHAVVRQVMGDHQQFSTRRRWDPRDEIGGKGIFRPRELVGNLMDYDPPEHTRLRRKLTPGFTLRKMQRMAPYIEQIVNDRLDEMERAGSPADLIAFVADKVPGAVLCELVGVPRDDRDMFMKLCHGHLDASLSQKRRAALGDKFSRYLLAMIARERKEPGEGMIGAVVAEYGDDATDEELRGFCVQVMLAGDDNISGMIGLGVLAMLRHPEQIDAFRGDEQSAQRAVDELIRYLTVPYSPTPRIAREDLTLAGQEIKKGDSVICSLPAANRDPALAPDVDRLDVTREPIPHVAFGHGVHHCLGAALARLELRTVFTELWRRFPALRLADPAQDTEFRLTTPAYGLTELMVAW","taxonomy":["Bacteria","Actinomycetota","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"],"alphafold_very_low_content":0.007537688442211055,"disorder_content":0.032663316582914576,"disprot_consensus":{"full":[{"start":70,"end":82,"type":"D"}],"Structural state":[{"start":70,"end":82,"type":"D"}]}},{"disprot_id":"DP04036","acc":"Q6FML9","creator":"ldobson","date":"2023-03-24T15:24:20.625Z","features":{"pfam":[{"id":"PF01541","name":"GIY-YIG catalytic domain","start":11,"end":88},{"id":"PF21202","name":"Structure-specific endonuclease subunit SLX1, C-terminal","start":218,"end":292}],"gene3D":[]},"genes":[{"name":{"value":"SLX1","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_03100","url":"https://hamap.expasy.org/unirule/MF_03100"}}]},"olnNames":[{"value":"CAGL0K06941g"}]}],"length":312,"name":"Structure-specific endonuclease subunit SLX1","ncbi_taxon_id":5478,"organism":"Candida glabrata","regions":[{"start":227,"end":236,"reference_id":"25753413","reference_source":"pmid","reference_html":"Structural and Mechanistic Analysis of the Slx1-Slx4 Endonuclease. <i> Gaur V, Wyatt HDM, Komorowska W, Szczepanowski RH, de Sanctis D, Gorecka KM, West SC, Nowotny M. </i> Cell Rep, 2015","date":"2023-04-28T08:11:17.112Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4XM5"}],"region_id":"DP04036r001","statement":[{"text":"Dotted lines\nindicate the loop regions, which were not observed in the electron density\nmaps.","type":"Figure"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T16:27:47.724Z"}},{"start":92,"end":105,"reference_id":"25753413","reference_source":"pmid","reference_html":"Structural and Mechanistic Analysis of the Slx1-Slx4 Endonuclease. <i> Gaur V, Wyatt HDM, Komorowska W, Szczepanowski RH, de Sanctis D, Gorecka KM, West SC, Nowotny M. </i> Cell Rep, 2015","date":"2023-04-28T08:09:53.751Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4XLG"}],"region_id":"DP04036r002","statement":[{"text":"Dotted lines\nindicate the loop regions, which were not observed in the electron density\nmaps.","type":"Figure"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6FJQ6"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T16:28:11.667Z"}},{"start":301,"end":312,"reference_id":"25753413","reference_source":"pmid","reference_html":"Structural and Mechanistic Analysis of the Slx1-Slx4 Endonuclease. <i> Gaur V, Wyatt HDM, Komorowska W, Szczepanowski RH, de Sanctis D, Gorecka KM, West SC, Nowotny M. </i> Cell Rep, 2015","date":"2023-04-28T08:09:15.499Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4XLG"}],"region_id":"DP04036r003","statement":[{"text":"Dotted lines\nindicate the loop regions, which were not observed in the electron density\nmaps.","type":"Figure"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6FJQ6"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T16:27:41.225Z"}}],"regions_counter":4,"released":"2024_06","sequence":"MEEFQQIPDFYGCYLLQSISKRQSFYIGSTPNPVRRLRQHNGSLSRGGAYRTKRDGTRPWEMVAIVYGFPSRIAALQFEHAWQHGYQTRYIKSQDRVVKTRKGGRSIHHKLAMITSLLKNEYFRYMDLTLHFFNQKVEEIWKNDKFNVSQTQESIDNNYTVSLSQDALTEINNDTIDDIMDVNEKNMELVQNLYSTTLAEKTKTLLLYKEKIDTGINTCQFCNKIIKHNLSGNISENLFAFCRDTSCTFVSHLACAYRYFMSNTELPKEDTIIPQSPKCPKCYTLLKWCDVIYYSIKLNKDNTTADDKKKTI","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Nakaseomyces","Nakaseomyces/Candida clade"],"alphafold_very_low_content":0.016025641025641024,"disorder_content":0.11538461538461539,"disprot_consensus":{"full":[{"start":92,"end":105,"type":"D"},{"start":227,"end":236,"type":"D"},{"start":301,"end":312,"type":"D"}],"Structural state":[{"start":92,"end":105,"type":"D"},{"start":227,"end":236,"type":"D"},{"start":301,"end":312,"type":"D"}]}},{"disprot_id":"DP04037","acc":"E9ADE1","creator":"ldobson","date":"2023-03-24T15:40:48.323Z","features":{"pfam":[{"id":"PF01652","name":"Eukaryotic initiation factor 4E","start":17,"end":212}],"gene3D":[]},"genes":[{"name":{"value":"EIF4E1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CBZ12229.1","url":"https://www.ebi.ac.uk/ena/browser/view/CBZ12229.1"}}]},"orfNames":[{"value":"LMJF_27_1620","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CBZ12229.1","url":"https://www.ebi.ac.uk/ena/browser/view/CBZ12229.1"}}]}]}],"length":214,"name":"Putative eukaryotic translation initiation factor eIF-4E","ncbi_taxon_id":5664,"organism":"Leishmania major","regions":[{"start":101,"end":121,"reference_id":"29562352","reference_source":"pmid","reference_html":"Structural basis for LeishIF4E-1 modulation by an interacting protein in the human parasite Leishmania major. <i> Meleppattu S, Arthanari H, Zinoviev A, Boeszoermenyi A, Wagner G, Shapira M, Léger-Abraham M. </i> Nucleic Acids Res, 2018","date":"2023-04-28T08:13:50.337Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5WB5"}],"region_id":"DP04037r001","statement":[{"text":"LeishIF4E-1 has\na 17 residue insertion in Loop 1 (L1, 104–120) and a 7\nresidue insertion in Loop 2 (L2, 151–157) (Supplementary\nFigure S1A), which are disordered in our crystal structure\n(residues 101–121, residues 149–155).","type":"Results"},{"text":"Disordered segments in loops (L1 and L2) from LeishIF4E-1 are shown in dashed\nlines.","type":"Figure"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"E9AFM3"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:8117"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T16:28:41.976Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MSAPSSVPPHKMANLHKLQRAWTLWYDSPSTYNTENWEMSLVPIMTVHSVEEFFVMLRYMKPLHALRTSSQYHFFQEGVKPMWEDPANKKGGKLWVNLDITSANGRSSNNNTSGTSAADGSAAEAKTDLDKAWENVLMATVGEYLDCVDKKDTPTEPFVTGIVMSKRKYHNRLAVWVSDASATDKIEALKKALTKEASLAPIASMVFTKHGEAS","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"alphafold_very_low_content":0.13551401869158877,"disorder_content":0.09813084112149532,"disprot_consensus":{"full":[{"start":101,"end":121,"type":"D"}],"Structural state":[{"start":101,"end":121,"type":"D"}]}},{"disprot_id":"DP04038","acc":"Q06069","creator":"ldobson","date":"2023-03-24T15:47:43.331Z","features":{"pfam":[{"id":"PF00067","name":"Cytochrome P450","start":35,"end":379}],"gene3D":[]},"genes":[{"name":{"value":"cyp106A2"}}],"length":410,"name":"Cytochrome P450(MEG)","ncbi_taxon_id":1404,"organism":"Priestia megaterium","regions":[{"start":68,"end":80,"reference_id":"28633515","reference_source":"pmid","reference_html":"Crystal Structure and Functional Characterization of a Cytochrome P450 (<i>Ba</i>CYP106A2) from <i>Bacillus</i> sp. PAMC 23377. <i> Kim KH, Lee CW, Dangi B, Park SH, Park H, Oh TJ, Lee JH. </i> J Microbiol Biotechnol, 2017","date":"2023-03-24T16:22:19.867Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5XNT"}],"region_id":"DP04038r001","statement":[{"text":"The N-terminal region (residues 1–6) and the loop\nregion (residues 68–80) between α3 and α4 were disordered\nbecause the electron density was too weak to be detected\nfor building a structural model in those regions. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-19T15:38:19.841Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MKEVIAVKEITRFKTRTEEFSPYAWCKRMLENDPVSYHEGTDTWNVFKYEDVKRVLSDYKHFSSVRKRTTISVGTDSEEGSVPEKIQITESDPPDHRKRRSLLAAAFTPRSLQNWEPRIQEIADELIGQMDGGTEIDIVASLASPLPIIVMADLMGVPSKDRLLFKKWVDTLFLPFDREKQEEVDKLKQVAAKEYYQYLYPIVVQKRLNPADDIISDLLKSEVDGEMFTDDEVVRTTMLILGAGVETTSHLLANSFYSLLYDDKEVYQELHENLDLVPQAVEEMLRFRFNLIKLDRTVKEDNDLLGVELKEGDSVVVWMSAANMDEEMFEDPFTLNIHRPNNKKHLTFGNGPHFCLGAPLARLEAKIALTAFLKKFKHIEAVPSFQLEENLTDSATGQTLTSLPLKASRM","taxonomy":["Bacteria","Bacillota","Bacilli","Bacillales","Bacillaceae","Priestia"],"alphafold_very_low_content":0,"disorder_content":0.03170731707317073,"disprot_consensus":{"full":[{"start":68,"end":80,"type":"D"}],"Structural state":[{"start":68,"end":80,"type":"D"}]}},{"disprot_id":"DP04039","acc":"Q4QF76","creator":"ldobson","date":"2023-03-24T17:53:47.786Z","features":{"pfam":[{"id":"PF00578","name":"AhpC/TSA family","start":9,"end":141},{"id":"PF10417","name":"C-terminal domain of 1-Cys peroxiredoxin","start":162,"end":198}],"gene3D":[]},"genes":[{"name":{"value":"TRYP3","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAJ03334.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAJ03334.1"}}]},"synonyms":[{"value":"PXN3","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAJ03334.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAJ03334.1"}}]},{"value":"TSA","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAJ03334.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAJ03334.1"}}]},{"value":"TXNPX","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAJ03334.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAJ03334.1"}}]}],"orfNames":[{"value":"LMJF_15_1080","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAJ03334.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAJ03334.1"}}]}]}],"length":199,"name":"Tryparedoxin peroxidase","ncbi_taxon_id":5664,"organism":"Leishmania major","regions":[{"start":170,"end":199,"reference_id":"22928053","reference_source":"pmid","reference_html":"The crystal structures of the tryparedoxin-tryparedoxin peroxidase couple unveil the structural determinants of Leishmania detoxification pathway. <i> Fiorillo A, Colotti G, Boffi A, Baiocco P, Ilari A. </i> PLoS Negl Trop Dis, 2012","date":"2023-04-28T11:30:29.661Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3TUE"}],"region_id":"DP04039r001","statement":[{"text":"The so-called resolving cysteine Cys173, the second residue essential for activity,\nis not visible since it is located in the C-terminal portion of the\npolypeptide that is disordered in all the monomers.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met104Ile","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser111Asn","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala181Asp","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr183Gly","start":null,"end":null,"position":null}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSHMSCGNAKINSPAPSFEEVALMPNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEVIAFSDSVSRFNELNCEVLACSIDSEYAHLQWTLQDRKKGGLGTMAIPILADKTKNIARSYGVLEESQGVAYRGLFIIDPHGMLRQITVNDMPVGRSVEEVLRLLEAFQFVEKHGEVCPANWKKGDPGMKPEPNASVEGYFSKQ","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T16:29:14.976Z"}},{"start":170,"end":199,"reference_id":"25951439","reference_source":"pmid","reference_html":"Structure-based discovery of the first non-covalent inhibitors of Leishmania major tryparedoxin peroxidase by high throughput docking. <i> Brindisi M, Brogi S, Relitti N, Vallone A, Butini S, Gemma S, Novellino E, Colotti G, Angiulli G, Di Chiaro F, Fiorillo A, Ilari A, Campiani G. </i> Sci Rep, 2015","date":"2023-04-20T17:14:08.206Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met104Ile","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser111Asn","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala181Asp","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr183Gly","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"4K1F"}],"region_id":"DP04039r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:8172"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:8117"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:78798"}],"statement":[{"text":"We previously reported a lower resolution (3.00 Å) structure of the same protein in the reduced form and LU conformation (LmTXNPs-LU; PDB ID: 3TUE)11.","type":"Results"},{"text":"The significant gain in resolution may be ascribed to the reduced flexibility of the 169–199 region, which is fully visible in the FF conformation structure here presented and absent in the previously reported LU conformation structure.","type":"Results"},{"text":"Since the oxidized LmTXNPx state is generally associated with the LU conformation, structure comparison between the here reported LmTXNPx-FF and the previously solved LmTXNPx-LU structures provided us with the opportunity to infer the mechanism underlying the transition from FF to LU conformation that occurs upon protein oxidation.","type":"Results"},{"text":"Protein oxidation promotes a transition to a locally unfolded (LU) conformation, where: i) the α-helical turn containing Cp unwinds and rotates toward the solvent; and ii) the C-terminal tail unfolds and becomes disordered.","type":"Abstract"}]},{"start":170,"end":199,"reference_id":"25951439","reference_source":"pmid","reference_html":"Structure-based discovery of the first non-covalent inhibitors of Leishmania major tryparedoxin peroxidase by high throughput docking. <i> Brindisi M, Brogi S, Relitti N, Vallone A, Butini S, Gemma S, Novellino E, Colotti G, Angiulli G, Di Chiaro F, Fiorillo A, Ilari A, Campiani G. </i> Sci Rep, 2015","date":"2023-04-20T17:14:53.335Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met104Ile","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser111Asn","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala181Asp","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr183Gly","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"4K1F"},{"db":"PDB","id":"3TUE"}],"region_id":"DP04039r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:8172"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:8117"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:78798"}],"statement":[{"text":"We previously reported a lower resolution (3.00 Å) structure of the same protein in the reduced form and LU conformation (LmTXNPs-LU; PDB ID: 3TUE)11.","type":"Results"},{"text":"The significant gain in resolution may be ascribed to the reduced flexibility of the 169–199 region, which is fully visible in the FF conformation structure here presented and absent in the previously reported LU conformation structure.","type":"Results"},{"text":"Since the oxidized LmTXNPx state is generally associated with the LU conformation, structure comparison between the here reported LmTXNPx-FF and the previously solved LmTXNPx-LU structures provided us with the opportunity to infer the mechanism underlying the transition from FF to LU conformation that occurs upon protein oxidation.","type":"Results"},{"text":"Protein oxidation promotes a transition to a locally unfolded (LU) conformation, where: i) the α-helical turn containing Cp unwinds and rotates toward the solvent; and ii) the C-terminal tail unfolds and becomes disordered.","type":"Abstract"}],"states_connection":[{"source":"DP04039r001","target":"DP04039r003"}]}],"regions_counter":4,"released":"2023_06","sequence":"MSCGNAKINSPAPSFEEVALMPNGSFKKISLSSYKGKWVVLFFYPLDFTFVCPTEVIAFSDSVSRFNELNCEVLACSIDSEYAHLQWTLQDRKKGGLGTMAIPMLADKTKSIARSYGVLEESQGVAYRGLFIIDPHGMLRQITVNDMPVGRSVEEVLRLLEAFQFVEKHGEVCPANWKKGAPTMKPEPNASVEGYFSKQ","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"alphafold_very_low_content":0,"disorder_content":0.1507537688442211,"disprot_consensus":{"full":[{"start":170,"end":199,"type":"T"}],"Structural state":[{"start":170,"end":199,"type":"D"}],"Structural transition":[{"start":170,"end":199,"type":"T"}]}},{"disprot_id":"DP04040","acc":"Q9TZX2","creator":"ldobson","date":"2023-03-24T18:18:47.586Z","features":{"pfam":[{"id":"PF00578","name":"AhpC/TSA family","start":10,"end":141},{"id":"PF10417","name":"C-terminal domain of 1-Cys peroxiredoxin","start":162,"end":181}],"gene3D":[]},"genes":[{"name":{"value":"TryP","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAC72300.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAC72300.1"}}]}}],"length":188,"name":"Tryparedoxin peroxidase","ncbi_taxon_id":5656,"organism":"Crithidia fasciculata","regions":[{"start":179,"end":188,"reference_id":"10891277","reference_source":"pmid","reference_html":"The structure of reduced tryparedoxin peroxidase reveals a decamer and insight into reactivity of 2Cys-peroxiredoxins. <i> Alphey MS, Bond CS, Tetaud E, Fairlamb AH, Hunter WN. </i> J Mol Biol, 2000","date":"2023-05-14T16:11:38.717Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1E2Y"}],"region_id":"DP04040r001","statement":[{"text":"The 18 residues of C-terminal form a flexible tail containing an essential conserved Cys173. Subunits B, C, G, H and I were modelled up to or beyond residue Cys173 allowing the position of this important residue to be determined.","type":"Results"},{"text":"A b-hairpin (b6 and\nb7) completes the b-sheet and leads to helix a4,\nthen finally a disordered C-terminal loop.","type":"Results"},{"text":"As it is also mention in the main text: \"Subunits B, C,\nG, H and I were modelled up to or beyond residue\nCys173 allowing the position of this important residue\nto be determined.\" disordered region in the distinct chains starts differently.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"}],"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":18,"end":18,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":21,"end":21,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":46,"end":46,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":100,"end":100,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":104,"end":104,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":147,"end":147,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue"}],"sequence_construct":"MSCGAAKLNHPAPEFDDMALMPNGTFKKVSLSSYKGKYVVLFFYPMDFTFVCPTEIIQFSDDAKRFAEINTEVISCSCDSEYSHLQWTSVDRKKGGLGPMAIPMLADKTKAIARAYGVLDEDSGVAYRGVFIIDPNGKLRQIIINDMPIGRNVEEVIRLVEALQFVEEHGEVCPANWKKGDAKKKEGH","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-17T13:15:41.726Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MSCGAAKLNHPAPEFDDMALMPNGTFKKVSLSSYKGKYVVLFFYPMDFTFVCPTEIIQFSDDAKRFAEINTEVISCSCDSEYSHLQWTSVDRKKGGLGPMAIPMLADKTKAIARAYGVLDEDSGVAYRGVFIIDPNGKLRQIIINDMPIGRNVEEVIRLVEALQFVEEHGEVCPANWKKGDAKKKEGH","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Crithidia"],"alphafold_very_low_content":0.010638297872340425,"disorder_content":0.05319148936170213,"disprot_consensus":{"full":[{"start":179,"end":188,"type":"D"}],"Structural state":[{"start":179,"end":188,"type":"D"}]}},{"disprot_id":"DP04041","acc":"O77103","creator":"ldobson","date":"2023-03-24T18:49:22.613Z","features":{"pfam":[{"id":"PF00156","name":"Phosphoribosyl transferase domain","start":45,"end":176}],"gene3D":[]},"genes":[{"name":{"value":"aprt","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAC36208.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAC36208.1"}}]},"orfNames":[{"value":"LtaPh_2601300","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"GET89368.1","url":"https://www.ebi.ac.uk/ena/browser/view/GET89368.1"}}]}]}],"length":235,"name":"Adenine phosphoribosyltransferase","ncbi_taxon_id":5689,"organism":"Leishmania tarentolae","regions":[{"start":218,"end":235,"reference_id":"14726202","reference_source":"pmid","reference_html":"Crystal structure of adenine phosphoribosyltransferase from Leishmania tarentolae: potential implications for APRT catalytic mechanism. <i> Silva M, Silva CH, Iulek J, Oliva G, Thiemann OH. </i> Biochim Biophys Acta, 2004","date":"2023-04-28T11:39:55.083Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1MZV"}],"region_id":"DP04041r001","statement":[{"text":"In such structure, the region beyond residue 217 was found to be\ndisordered, yet several attempts to model ordered protein\natoms throughout it were unsuccessful.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6083"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1061"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T16:31:01.031Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MSLKEIGPNSLLLEDSHSLSQLLKKNYRWYSPIFSPRNVPRFADVSSITESPETLKAIRDFLVERYRTMSPAPTHILGFDARGFLFGPMIAVELGIPFVLMRKADKNAGLLIRSEPYEKEYKEAAPEVMTIRHGSIGKNSRVVLIDDVLATGGTALSGLQLVEASGAEVVEMVSILTIPFLKAAERIHSTAGGRYKNVRFIGLLSEDVLTEANCGDLNDYTGPRVLSCSDLLVNQ","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania","lizard Leishmania"],"dataset":["Neglected tropical diseases proteins"],"alphafold_very_low_content":0.00851063829787234,"disorder_content":0.07659574468085106,"disprot_consensus":{"full":[{"start":218,"end":235,"type":"D"}],"Structural state":[{"start":218,"end":235,"type":"D"}]}},{"disprot_id":"DP04042","acc":"O00834","creator":"ldobson","date":"2023-03-27T09:55:02.958Z","features":{"pfam":[{"id":"PF10564","name":"Sialic-acid binding micronemal adhesive repeat","start":41,"end":138},{"id":"PF10564","name":"Sialic-acid binding micronemal adhesive repeat","start":148,"end":213},{"id":"PF11476","name":"Toxoplasma gondii micronemal protein 1 TgMIC1","start":336,"end":450}],"gene3D":[]},"genes":[{"name":{"value":"MIC1","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"CAA96466.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAA96466.1"}}]}}],"length":456,"name":"Micronemal protein 1","ncbi_taxon_id":5811,"organism":"Toxoplasma gondii","regions":[{"start":17,"end":27,"reference_id":"17491595","reference_source":"pmid","reference_html":"Atomic resolution insight into host cell recognition by Toxoplasma gondii. <i> Blumenschein TM, Friedrich N, Childs RA, Saouros S, Carpenter EP, Campanero-Rhodes MA, Simpson P, Chai W, Koutroukides T, Blackman MJ, Feizi T, Soldati-Favre D, Matthews S. </i> EMBO J, 2007","date":"2023-05-14T16:14:06.047Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2JH1"}],"region_id":"DP04042r001","statement":[{"text":"Residues 17–28 and 262 likely\nexhibit a degree of flexibility and therefore could not be\nobserved in the crystal structure.","type":"Results"},{"text":"In this structure, the last missing amino acid is His27 instead of Ser28 like in the two other structures.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:175"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-17T13:16:02.966Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MGQALFLTVLLPVLFGVGPEAYGEASHSHSPASGRYIQQMLDQRCQEIAAELCQSGLRKMCVPSSRIVARNAVGITHQNTLQWRCFDTASLLESNQENNGVNCVDDCGHTIPCPGGVHRQNSNHATRHEILSKLVEEGVQRFCSPYQASANKYCNDKFPGTIARRSKGFGNNVEVAWRCYEKASLLYSVYAECASNCGTTWYCPGGRRGTSTELDKRHYTEEEGIRQAIGSVDSPCSEVEVCLPKDENPPLCLDESGQISRTGGGPPSQPPEMQQPADRSDERGGGKEQSPGGEAQPDHPTKGGNIDLPEKSTSPEKTPKTEIHGDSTKATLEEGQQLTLTFISTKLDVAVGSCHSLVANFLDGFLKFQTGSNSAFDVVEVEEPAGPAVLTIGLGHKGRLAVVLDYTRLNAALGSAAYVVEDSGCSSSEEVSFQGVGSGATLVVTTLGESPTAVSA","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Conoidasida","Coccidia","Eucoccidiorida","Eimeriorina","Sarcocystidae","Toxoplasma"],"alphafold_very_low_content":0.15789473684210525,"disorder_content":0.02412280701754386,"disprot_consensus":{"full":[{"start":17,"end":27,"type":"D"}],"Structural state":[{"start":17,"end":27,"type":"D"}]}},{"disprot_id":"DP04044","acc":"P50489","creator":"ldobson","date":"2023-03-27T11:01:15.012Z","features":{"pfam":[{"id":"PF02430","name":"Apical membrane antigen 1","start":110,"end":580}],"gene3D":[]},"genes":[{"name":{"value":"AMA-1"},"synonyms":[{"value":"PF83"}]}],"length":622,"name":"Apical membrane antigen 1","ncbi_taxon_id":5835,"organism":"Plasmodium falciparum (isolate Camp / Malaysia)","regions":[{"start":351,"end":387,"reference_id":"22737069","reference_source":"pmid","reference_html":"Structural and functional insights into the malaria parasite moving junction complex. <i> Vulliez-Le Normand B, Tonkin ML, Lamarque MH, Langer S, Hoos S, Roques M, Saul FA, Faber BW, Bentley GA, Boulanger MJ, Lebrun M. </i> PLoS Pathog, 2012","date":"2023-05-14T16:17:08.926Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3SRI"}],"region_id":"DP04044r001","statement":[{"text":"Similarly,\nexposing a functional receptor-binding groove on AMA1 requires\ndisplacement of the extended non-polymorphic DII loop, which\nadopts a disordered state (not modeled between Lys351 to\nAla387); this region is stabilized by DI in apo PfAMA1 (Fig. 2B).","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8IKV6"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asn162Lys","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr288Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser373Asp","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asn422Asp","start":null,"end":null,"position":null},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"sequence_construct":"EFIEIVERSNYMGNPWTEYMAKYDIEEVHGSGIRVDLGEDAEVAGTQYRLPSGKCPVFGKGIIIENSKTTFLKPVATGNQDLKDGGFAFPPTEPLISPMTLNGMRDFYKNNEYVKNLDELTLCSRHAGNMNPDKDENSNYKYPAVYDDKDKKCHILYIAAQENNGPRYCNKDESKRNSMFCFRPAKDKSFQNYVYLSKNVVDNWEKVCPRKNLENAKFGLWVDGNCEDIPHVNEFSANDLFECNKLVFELSASDQPKQYEQHLTDYEKIKEGFKNKNADMIKSAFLPTGAFKADRYKSHGKGYNWGNYNRKTHKCEIFNVKPTCLINDKSYIATTALSHPIEVENNFPMVPRAAAAASFLEQKLISEEDLNSAVDHHHHHH","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-17T13:16:32.299Z"}},{"start":261,"end":272,"reference_id":"22737069","reference_source":"pmid","reference_html":"Structural and functional insights into the malaria parasite moving junction complex. <i> Vulliez-Le Normand B, Tonkin ML, Lamarque MH, Langer S, Hoos S, Roques M, Saul FA, Faber BW, Bentley GA, Boulanger MJ, Lebrun M. </i> PLoS Pathog, 2012","date":"2023-05-14T16:16:09.029Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3SRI"}],"region_id":"DP04044r002","statement":[{"text":"This region is not mentioned in the publication, but the structure deposited in PDB indicates this region is unstructured.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asn162Lys","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr288Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser373Asp","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asn422Asp","start":null,"end":null,"position":null},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"sequence_construct":"EFIEIVERSNYMGNPWTEYMAKYDIEEVHGSGIRVDLGEDAEVAGTQYRLPSGKCPVFGKGIIIENSKTTFLKPVATGNQDLKDGGFAFPPTEPLISPMTLNGMRDFYKNNEYVKNLDELTLCSRHAGNMNPDKDENSNYKYPAVYDDKDKKCHILYIAAQENNGPRYCNKDESKRNSMFCFRPAKDKSFQNYVYLSKNVVDNWEKVCPRKNLENAKFGLWVDGNCEDIPHVNEFSANDLFECNKLVFELSASDQPKQYEQHLTDYEKIKEGFKNKNADMIKSAFLPTGAFKADRYKSHGKGYNWGNYNRKTHKCEIFNVKPTCLINDKSYIATTALSHPIEVENNFPMVPRAAAAASFLEQKLISEEDLNSAVDHHHHHH","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8IKV6"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-17T13:16:32.883Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MRKLYCVLLLSAFEFTYMINFGRGQNYWEHPYQNSNVYHPINEHREHPKEYQYPLHQEHTYQQEDSGEDENTLQHAYPIDHEGAEPAPQEQNLFSSIEIVERSNYMGNPWTEYMAKYDIEEVHGSGIRVDLGEDAEVAGTQYRLPSGKCPVFGKGIIIENSNTTFLKPVATGNQDLKDGGFAFPPTEPLISPMTLNGMRDFYKNNEYVKNLDELTLCSRHAGNMNPDKDENSNYKYPAVYDDKDKKCHILYIAAQENNGPRYCNKDESKRNSMFCFRPAKDKSFQNYTYLSKNVVDNWEKVCPRKNLENAKFGLWVDGNCEDIPHVNEFSANDLFECNKLVFELSASDQPKQYEQHLTDYEKIKEGFKNKNASMIKSAFLPTGAFKADRYKSHGKGYNWGNYNRKTHKCEIFNVKPTCLINNSSYIATTALSHPIEVENNFPCSLYKNEIMKEIERESKRIKLNDNDDEGNKKIIAPRIFISDDKDSLKCPCDPEMVSNSTCRFFVCKCVERRAEVTSNNEVVVKEEYKDEYADIPEHKPTYDNMKIIIASSAAVAVLATILMVYLYKRKGNAEKYDKMDQPQDYGKSTSRNDEMLDPEASFWGEEKRASHTTPVLMEKPYY","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"alphafold_very_low_content":0.23311897106109325,"disorder_content":0.07877813504823152,"disprot_consensus":{"full":[{"start":261,"end":272,"type":"D"},{"start":351,"end":387,"type":"D"}],"Structural state":[{"start":261,"end":272,"type":"D"},{"start":351,"end":387,"type":"D"}]}},{"disprot_id":"DP04045","acc":"Q7KQK5","creator":"ldobson","date":"2023-03-27T11:20:31.205Z","features":{"pfam":[{"id":"PF02430","name":"Apical membrane antigen 1","start":110,"end":580}],"gene3D":[]},"genes":[{"orfNames":[{"value":"PF3D7_1133400","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CZT98996.1","url":"https://www.ebi.ac.uk/ena/browser/view/CZT98996.1"}}]}]}],"length":622,"name":"Apical membrane antigen 1","ncbi_taxon_id":36329,"organism":"Plasmodium falciparum (isolate 3D7)","regions":[{"start":351,"end":387,"reference_id":"22737069","reference_source":"pmid","reference_html":"[Production of monoclonal antibodies against human bladder cancer cells and application to immunohistochemical analysis of bladder cancer]. <i> Saiki S, Meguro N, Morita T, Tomooka Y, Maeda O, Kinouchi T, Kuroda M, Miki T, Usami M, Kotake T. </i> Nihon Hinyokika Gakkai Zasshi, 1990","date":"2023-04-28T07:17:51.325Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3ZWZ"}],"region_id":"DP04045r001","statement":[{"text":"Similarly,\nexposing a functional receptor-binding groove on AMA1 requires\ndisplacement of the extended non-polymorphic DII loop, which\nadopts a disordered state (not modeled between Lys351 to\nAla387); this region is stabilized by DI in apo PfAMA1 (Fig. 2B).","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8IKV6"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser103Gly","start":null,"end":null,"position":null}],"sequence_construct":"GSAMGNYMGNPWTEYMAKYDIEEVHGSGIRVDLGEDAEVAGTQYRLPSGKCPVFGKGIIIENSNTTFLTPVATGNQYLKDGGFAFPPTEPLMSPMTLDEMRHFYKDNKYVKNLDELTLCSRHAGNMIPDNDKNSNYKYPAVYDDKDKKCHILYIAAQENNGPRYCNKDESKRNSMFCFRPAKDISFQNYTYLSKNVVDNWEKVCPRKNLQNAKFGLWVDGNCEDIPHVNEFPAIDLFECNKLVFELSASDQPKQYEQHLTDYEKIKEGFKNKNASMIKSAFLPTGAFKADRYKSHGKGYNWGNYNTETQKCEIFNVKPTCLINNSSYIATTALSHPIEVEAAALVPR","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T16:33:43.513Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MRKLYCVLLLSAFEFTYMINFGRGQNYWEHPYQNSDVYRPINEHREHPKEYEYPLHQEHTYQQEDSGEDENTLQHAYPIDHEGAEPAPQEQNLFSSIEIVERSNYMGNPWTEYMAKYDIEEVHGSGIRVDLGEDAEVAGTQYRLPSGKCPVFGKGIIIENSNTTFLTPVATGNQYLKDGGFAFPPTEPLMSPMTLDEMRHFYKDNKYVKNLDELTLCSRHAGNMIPDNDKNSNYKYPAVYDDKDKKCHILYIAAQENNGPRYCNKDESKRNSMFCFRPAKDISFQNYTYLSKNVVDNWEKVCPRKNLQNAKFGLWVDGNCEDIPHVNEFPAIDLFECNKLVFELSASDQPKQYEQHLTDYEKIKEGFKNKNASMIKSAFLPTGAFKADRYKSHGKGYNWGNYNTETQKCEIFNVKPTCLINNSSYIATTALSHPIEVENNFPCSLYKDEIMKEIERESKRIKLNDNDDEGNKKIIAPRIFISDDKDSLKCPCDPEMVSNSTCRFFVCKCVERRAEVTSNNEVVVKEEYKDEYADIPEHKPTYDKMKIIIASSAAVAVLATILMVYLYKRKGNAEKYDKMDEPQDYGKSNSRNDEMLDPEASFWGEEKRASHTTPVLMEKPYY","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"alphafold_very_low_content":0.25241157556270094,"disorder_content":0.0594855305466238,"disprot_consensus":{"full":[{"start":351,"end":387,"type":"D"}],"Structural state":[{"start":351,"end":387,"type":"D"}]}},{"disprot_id":"DP04046","acc":"P62368","creator":"ldobson","date":"2023-03-27T11:54:46.422Z","features":{"pfam":[{"id":"PF02542","name":"YgbB family","start":64,"end":235}],"gene3D":[]},"genes":[{"name":{"value":"IspF","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"24410837","url":"http://www.ncbi.nlm.nih.gov/pubmed/24410837","alternativeUrl":"https://europepmc.org/abstract/MED/24410837"}}]},"orfNames":[{"value":"PF3D7_0209300"},{"value":"PFB0420w"}]}],"length":240,"name":"2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, apicoplast","ncbi_taxon_id":36329,"organism":"Plasmodium falciparum (isolate 3D7)","regions":[{"start":82,"end":97,"reference_id":"24410837","reference_source":"pmid","reference_html":"Crystal structures of IspF from Plasmodium falciparum and Burkholderia cenocepacia: comparisons inform antimicrobial drug target assessment. <i> O'Rourke PE, Kalinowska-Tłuścik J, Fyfe PK, Dawson A, Hunter WN. </i> BMC Struct Biol, 2014","date":"2023-04-28T07:20:24.092Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4C82"},{"db":"PDB","id":"4C81"}],"region_id":"DP04046r001","statement":[{"text":"Electron density is\nabsent or poorly defined for the loop linking α2 to α3 in\nmany of the IspF structures. ","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6132"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T16:39:34.861Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MFLKGYTSNVVLIILTFFILLTKEEKNIKNNISGYCFLNFGLKKNAIIKKREKQNLKLFCYNGIRIGQGYDIHKIKVLDEEYNTYANNDFNKNEQSFKTLTLGGVKINNVLVLSHSDGDIIYHSIVDSILGALGSLDIGTLFPDKDEKNKNKNSAIFLRYARLLIYKKNYDIGNVDINVIAQVPKISNIRKNIIKNISTVLNIDESQISVKGKTHEKLGVIGEKKAIECFANILLIPKNS","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"alphafold_very_low_content":0.225,"disorder_content":0.06666666666666667,"disprot_consensus":{"full":[{"start":82,"end":97,"type":"D"}],"Structural state":[{"start":82,"end":97,"type":"D"}]}},{"disprot_id":"DP04048","acc":"Q9U1D9","creator":"ldobson","date":"2023-03-27T13:26:35.990Z","features":{"pfam":[{"id":"PF02970","name":"Tubulin binding cofactor A","start":22,"end":114}],"gene3D":[]},"genes":[{"name":{"value":"L1648.09","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAB55371.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAB55371.1"}}]},"orfNames":[{"value":"LMJF_32_2970","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAJ08825.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAJ08825.1"}}]}]}],"length":125,"name":"Tubulin-specific chaperone A","ncbi_taxon_id":5664,"organism":"Leishmania major","regions":[{"start":1,"end":18,"reference_id":"25945706","reference_source":"pmid","reference_html":"The structure of tubulin-binding cofactor A from Leishmania major infers a mode of association during the early stages of microtubule assembly. <i> Barrack KL, Fyfe PK, Hunter WN. </i> Acta Crystallogr F Struct Biol Commun, 2015","date":"2023-04-28T07:22:00.802Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4CQI"}],"region_id":"DP04048r001","statement":[{"text":"There\nwas no reliable electron density for the first 18 residues and\nthe model comprises residues Glu19–Ser125.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T16:40:11.301Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MSDSTESTNRFASNVRQAEAPNEKTLRIKVSALKRTIKDLEFAKREVERELQRLDTLCQSDPDRVPQQTKVVDEAQMMVPHSVNRIMASVKDLSDYLEKEGSTVSNEELLDLARATMADGQAAVS","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"dataset":["Neglected tropical diseases proteins"],"alphafold_very_low_content":0.048,"disorder_content":0.144,"disprot_consensus":{"full":[{"start":1,"end":18,"type":"D"}],"Structural state":[{"start":1,"end":18,"type":"D"}]}},{"disprot_id":"DP04049","acc":"Q86MV5","creator":"bjuhasz","date":"2023-03-27T15:50:30.604Z","features":{"pfam":[{"id":"PF03828","name":"Cid1 family poly A polymerase","start":365,"end":425},{"id":"PF18528","name":"RNA editing 3' terminal uridylyl transferase 2 middle domain","start":166,"end":258},{"id":"PF22600","name":"Poly(A) RNA polymerase, mitochondrial-like, central palm domain","start":53,"end":152}],"gene3D":[]},"genes":[{"name":{"value":"KRET2","evidences":[{"code":"ECO:0000305"}]},"synonyms":[{"value":"MP57","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAO63567.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAO63567.1"}}]}]}],"length":487,"name":"Terminal uridylyltransferase 2","ncbi_taxon_id":5702,"organism":"Trypanosoma brucei brucei","regions":[{"start":20,"end":29,"reference_id":"16281058","reference_source":"pmid","reference_html":"Structural basis for UTP specificity of RNA editing TUTases from Trypanosoma brucei. <i> Deng J, Ernst NL, Turley S, Stuart KD, Hol WG. </i> EMBO J, 2005","date":"2023-05-14T16:19:07.424Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2B51"},{"db":"PDB","id":"2B56"},{"db":"PDB","id":"2B4V"}],"region_id":"DP04049r001","statement":[{"text":"In all, 10 residues from the\nN-terminus as well as 14 residues from the C-terminus were\ndisordered and not incorporated into the structures.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6133","statements":[{"type":"Curator statement","text":"2B51 and 2B56"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:27854","statements":[{"type":"Curator statement","text":"2B51"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1172","statements":[{"type":"Curator statement","text":"2B56"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888","statements":[{"type":"Curator statement","text":"2B56"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:813","statements":[{"type":"Curator statement","text":"2B4V"}]}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp94Arg","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"2B51 and 2B56"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp122Arg","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"2B51 and 2B56"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp207Arg","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"2B51 and 2B56"}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":44,"end":44,"position":"Specific residue","statements":[{"type":"Curator statement","text":"2B4V"}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":56,"end":56,"position":"Specific residue","statements":[{"type":"Curator statement","text":"2B4V"}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":86,"end":86,"position":"Specific residue","statements":[{"type":"Curator statement","text":"2B4V"}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":92,"end":92,"position":"Specific residue","statements":[{"type":"Curator statement","text":"2B4V"}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":94,"end":94,"position":"Specific residue","statements":[{"type":"Curator statement","text":"2B4V"}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":103,"end":103,"position":"Specific residue","statements":[{"type":"Curator statement","text":"2B4V"}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":122,"end":122,"position":"Specific residue","statements":[{"type":"Curator statement","text":"2B4V"}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":198,"end":198,"position":"Specific residue","statements":[{"type":"Curator statement","text":"2B4V"}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":207,"end":207,"position":"Specific residue","statements":[{"type":"Curator statement","text":"2B4V"}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":227,"end":227,"position":"Specific residue","statements":[{"type":"Curator statement","text":"2B4V"}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":240,"end":240,"position":"Specific residue","statements":[{"type":"Curator statement","text":"2B4V"}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":244,"end":244,"position":"Specific residue","statements":[{"type":"Curator statement","text":"2B4V"}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":261,"end":261,"position":"Specific residue","statements":[{"type":"Curator statement","text":"2B4V"}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":263,"end":263,"position":"Specific residue","statements":[{"type":"Curator statement","text":"2B4V"}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":297,"end":297,"position":"Specific residue","statements":[{"type":"Curator statement","text":"2B4V"}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":315,"end":315,"position":"Specific residue","statements":[{"type":"Curator statement","text":"2B4V"}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":324,"end":324,"position":"Specific residue","statements":[{"type":"Curator statement","text":"2B4V"}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":456,"end":456,"position":"Specific residue","statements":[{"type":"Curator statement","text":"2B4V"}]}],"sequence_construct":"SPLSLPSTKLNPSPDHYAVWGKAIMAENNRRVGPEHMFRTAIRAQQQLQGLADKWTPDAKVYCCGSMVTYGQMERGSDLDLACMFDDPYPSHEVQAKRTDKLRTVIKRYVPHYLRNNLLGLTEARTPVVKLRFANDEKVARARYTPLSEEEDRKARTALLDVRNQCVGDNDVEYIAEKMGRDNVEGIRVDRTTYGCRIAIQCTSKEQMIEAIGFFPDGKIMTRGMREDYTRDVLDVRFVPEMFMYRWDISFVGYGVKNSYLIRHYLHNGPVAARHTAMAVKAWGKATNVGAGSGAMLTSYAVTVMFIYYLLVTRQVLWVDPWSLPHPAHLPRYPDFSPLYDCDPTELGRLLHGFFIFYAHHFDYEREVVSLNRNRRSYRSDIGWNFPQNKKGTFSYNFCIEDPYEDVGTGGLNLVRHLHPAKFQLVKQEFLRAAQCMERFLPTNAPEKSILGVKRADLRHFERDRDRE","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-17T13:17:33.214Z"}},{"start":474,"end":487,"reference_id":"16281058","reference_source":"pmid","reference_html":"Structural basis for UTP specificity of RNA editing TUTases from Trypanosoma brucei. <i> Deng J, Ernst NL, Turley S, Stuart KD, Hol WG. </i> EMBO J, 2005","date":"2023-05-14T16:18:42.010Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2B56"},{"db":"PDB","id":"2B51"}],"region_id":"DP04049r003","statement":[{"text":"In all, 10 residues from the\nN-terminus as well as 14 residues from the C-terminus were\ndisordered and not incorporated into the structures.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6133","statements":[{"type":"Curator statement","text":"2B51 and 2B56"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:27854","statements":[{"type":"Curator statement","text":"2B51"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1172","statements":[{"type":"Curator statement","text":"2B56"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888","statements":[{"type":"Curator statement","text":"2B56"}]}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp94Arg","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"2B51 and 2B56"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp122Arg","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"2B51 and 2B56"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp207Arg","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"2B51 and 2B56"}]}],"sequence_construct":"SPLSLPSTKLNPSPDHYAVWGKAIMAENNRRVGPEHMFRTAIRAQQQLQGLADKWTPDAKVYCCGSMVTYGQMERGSDLDLACMFDDPYPSHEVQAKRTDKLRTVIKRYVPHYLRNNLLGLTEARTPVVKLRFANDEKVARARYTPLSEEEDRKARTALLDVRNQCVGDNDVEYIAEKMGRDNVEGIRVDRTTYGCRIAIQCTSKEQMIEAIGFFPDGKIMTRGMREDYTRDVLDVRFVPEMFMYRWDISFVGYGVKNSYLIRHYLHNGPVAARHTAMAVKAWGKATNVGAGSGAMLTSYAVTVMFIYYLLVTRQVLWVDPWSLPHPAHLPRYPDFSPLYDCDPTELGRLLHGFFIFYAHHFDYEREVVSLNRNRRSYRSDIGWNFPQNKKGTFSYNFCIEDPYEDVGTGGLNLVRHLHPAKFQLVKQEFLRAAQCMERFLPTNAPEKSILGVKRADLRHFERDRDRE","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-17T13:17:38.578Z"}}],"regions_counter":3,"released":"2023_06","sequence":"MLMHTAPWLHMRLSRLFRQSPLSLPSTKLNPSPDHYAVWGKAIMAENNRRVGPEHMFRTAIRAQQQLQGLADKWTPDAKVYCCGSMVTYGQMEWGSDLDLACMFDDPYPSHEVQAKRTDKLWTVIKRYVPHYLRNNLLGLTEARTPVVKLRFANDEKVARARYTPLSEEEDRKARTALLDVRNQCVGDNDVEYIAEKMGRDNVEGIWVDRTTYGCRIAIQCTSKEQMIEAIGFFPDGKIMTRGMREDYTRDVLDVRFVPEMFMYRWDISFVGYGVKNSYLIRHYLHNGPVAARHTAMAVKAWGKATNVGAGSGAMLTSYAVTVMFIYYLLVTRQVLWVDPWSLPHPAHLPRYPDFSPLYDCDPTELGRLLHGFFIFYAHHFDYEREVVSLNRNRRSYRSDIGWNFPQNKKGTFSYNFCIEDPYEDVGTGGLNLVRHLHPAKFQLVKQEFLRAAQCMERFLPTNAPEKSILGVKRADLRHFERDRDRE","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Trypanosoma"],"dataset":["Neglected tropical diseases proteins","RNA-binding proteins"],"alphafold_very_low_content":0.07186858316221766,"disorder_content":0.049281314168377825,"disprot_consensus":{"full":[{"start":20,"end":29,"type":"D"},{"start":474,"end":487,"type":"D"}],"Structural state":[{"start":20,"end":29,"type":"D"},{"start":474,"end":487,"type":"D"}]}},{"disprot_id":"DP04050","acc":"Q257B3","creator":"ldobson","date":"2023-03-27T15:56:42.899Z","features":{"pfam":[{"id":"PF18542","name":"Transcription factor IIB C-terminal module 1","start":96,"end":193},{"id":"PF22108","name":"Transcription factor IIB C-terminal module 2","start":203,"end":308},{"id":"PF22109","name":"Transcription factor IIB, zinc ribbon, Trypanosome","start":1,"end":40}],"gene3D":[]},"genes":[{"name":{"value":"TFIIB-like","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAJ84438.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAJ84438.1"}}]}}],"length":345,"name":"Transcription factor TFIIB-like","ncbi_taxon_id":5702,"organism":"Trypanosoma brucei brucei","regions":[{"start":314,"end":345,"reference_id":"19666603","reference_source":"pmid","reference_html":"Structure of the C-terminal domain of transcription factor IIB from Trypanosoma brucei. <i> Ibrahim BS, Kanneganti N, Rieckhof GE, Das A, Laurents DV, Palenchar JB, Bellofatto V, Wah DA. </i> Proc Natl Acad Sci U S A, 2009","date":"2023-04-28T06:38:33.609Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3H4C"}],"region_id":"DP04050r001","statement":[{"text":"The 32-residue C-terminal extension of tTFIIBC\n(residues 314–345) is not visible in the crystal, suggesting that it is\nunstructured.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:174"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T16:47:36.690Z"}},{"start":262,"end":274,"reference_id":"19666603","reference_source":"pmid","reference_html":"Structure of the C-terminal domain of transcription factor IIB from Trypanosoma brucei. <i> Ibrahim BS, Kanneganti N, Rieckhof GE, Das A, Laurents DV, Palenchar JB, Bellofatto V, Wah DA. </i> Proc Natl Acad Sci U S A, 2009","date":"2023-04-28T06:38:17.696Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3H4C"}],"region_id":"DP04050r002","statement":[{"text":"The linker (residues 162–174), which\nconnects H3'A to H4', is not visible in the electron density,\nsuggesting that it is unstructured.","type":"Results"},{"text":"The numbering is incorrect in the text, but correct in Fig.2C.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:174"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T16:47:35.037Z"}},{"start":262,"end":274,"reference_id":"19666603","reference_source":"pmid","reference_html":"Structure of the C-terminal domain of transcription factor IIB from Trypanosoma brucei. <i> Ibrahim BS, Kanneganti N, Rieckhof GE, Das A, Laurents DV, Palenchar JB, Bellofatto V, Wah DA. </i> Proc Natl Acad Sci U S A, 2009","date":"2023-04-28T06:40:41.756Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3H4C"}],"region_id":"DP04050r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:174"}],"statement":[{"text":"The linker (residues 162–174), which connects H3'A to H4', is not visible in the electron density, suggesting that it is unstructured.","type":"Results"},{"text":"The numbering is incorrect in the text, but correct in Fig.2C.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T16:47:46.504Z"}}],"regions_counter":3,"released":"2023_06","sequence":"MSTTTDFVGRNCPHCSAVDSLQTDDVMGEVACTACALVVAMGLEENVFTRYNENATYEDVDHHRERNANPTAATSAAGSLSAADPHMSSTSSKVVLHPTMLNCMRGLHKKAVLPEPVLDRGIELARAFVGGRRARGQRVERQPDVAAACLMIAAEEAQQPLPLAEVRCLDSSLGDVELRRADIVRELHLEDSERRLRDTFADNLLVKYILKLGLQVSLYLPHCKRLLTALGRVEALAGLTVADRVTTALLLARTAQTLSWEQGTHISKGKECDLGMEAIYANFSSKAHLEVTKVNKIMHLAVDVLPLIQAAFQDCGEPTAGKRKVDKNSEPEASGGTKRVKREET","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Trypanosoma"],"dataset":["Neglected tropical diseases proteins"],"alphafold_very_low_content":0.18840579710144928,"disorder_content":0.13043478260869565,"disprot_consensus":{"full":[{"start":262,"end":274,"type":"D"},{"start":314,"end":345,"type":"D"}],"Structural state":[{"start":262,"end":274,"type":"D"},{"start":314,"end":345,"type":"D"}],"Disorder function":[{"start":262,"end":274,"type":"F"}]}},{"disprot_id":"DP04051","acc":"Q8IJ45","creator":"ldobson","date":"2023-03-27T16:47:07.408Z","features":{"pfam":[{"id":"PF05424","name":"Duffy binding domain","start":201,"end":348},{"id":"PF07133","name":"Merozoite surface protein (SPAM)","start":571,"end":762}],"gene3D":[]},"genes":[{"orfNames":[{"value":"PF3D7_1036300","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CZT98618.1","url":"https://www.ebi.ac.uk/ena/browser/view/CZT98618.1"}}]}]}],"length":762,"name":"Duffy binding-like merozoite surface protein 2","ncbi_taxon_id":36329,"organism":"Plasmodium falciparum (isolate 3D7)","regions":[{"start":375,"end":389,"reference_id":"22843685","reference_source":"pmid","reference_html":"Insights into Duffy binding-like domains through the crystal structure and function of the merozoite surface protein MSPDBL2 from Plasmodium falciparum. <i> Hodder AN, Czabotar PE, Uboldi AD, Clarke OB, Lin CS, Healer J, Smith BJ, Cowman AF. </i> J Biol Chem, 2012","date":"2023-04-26T06:24:31.858Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3VUU"},{"db":"PDB","id":"3VUV"}],"region_id":"DP04051r001","statement":[{"text":"The loop\nbetween helices 6 and 7 (residues 374 –388) was disordered (Fig. 6), as has been observed for other DBL structures (e.g.\nPfEMP1 VAR2CSA DBL 6ε,, PDB code 2WAU) (38).","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312","statements":[{"type":"Curator statement","text":"3VUU"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051","statements":[{"type":"Curator statement","text":"3VUV"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T16:57:15.914Z"}},{"start":375,"end":389,"reference_id":"22843685","reference_source":"pmid","reference_html":"Insights into Duffy binding-like domains through the crystal structure and function of the merozoite surface protein MSPDBL2 from Plasmodium falciparum. <i> Hodder AN, Czabotar PE, Uboldi AD, Clarke OB, Lin CS, Healer J, Smith BJ, Cowman AF. </i> J Biol Chem, 2012","date":"2023-04-28T06:52:48.797Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3VUU"},{"db":"PDB","id":"3VUV"}],"region_id":"DP04051r002","statement":[{"text":"The loop between helices 6 and 7 (residues 374 –388) was disordered (Fig. 6), as has been observed for other DBL structures (e.g. PfEMP1 VAR2CSA DBL 6ε,, PDB code 2WAU) (38).","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312","statements":[{"type":"Curator statement","text":"3VUU"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051","statements":[{"type":"Curator statement","text":"3VUV"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T16:57:16.533Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MIYILSIVFYIFFLHIDIYVNIYSTCFVVNEGNPNLRNNIINDDELKGKAYNNTIDANNQNIEYNKNLKHNVNSSHISKFSDIMDQEDKGDNENSHDIKFEEKKNINKSLDAESNYGINEISITGNDSNSDNSNQNIFPDGSELAGGIPRSIYTINLGFNKCPTEEICKDFSNLPQCRKNVHERNNWLGSSVKNFSSDNKGVLVPPRRQSLCLRITLQDFRTKKKKEGDFEKFIYSYASSEARKLRTIHNNNLEKAHQAIRYSFADIGNIIRGDDMMDTPTSKETITYLEKVLKIYNENNDKPKDAKKWWTENRHHVWEAMMCGYQSAQKDNQCTGYGNIDDIPQFLRWFREWGTYVCEESEKNMNTLKAVCFPKQPRTEANPALTVHENEMCSSTLKKYEEWYNKRKTEWTEQSIKYNNDKINYTDIKTLSPSEYLIEKCPECKCTKKNLQDVFELTFDGKALLEKLKKEESPVSNSVNALPEPGQITLPDPSLKQTTQQENQPVVETPVTTAVINEHQGQTEPNKGDNNNERENHESNVGSIQEVNQGSVSEESHSKTIDPSKIDDRLELSSGSSSLEQHSKEDVKKGCALELVPLSLSDIEQIANESEDVLEEIEEEINTDGEIEYITEEEIKEDIEEETEEDIEEETEEETEEETEEEADEETVKEIEDKPEQEIKNKSLEEKQIDKNTDTSEKKGFNNSEKDEKARNLISKNYKNYNELDKNVHTLVNSIISLLEEGNGSDSTLNSLSKDITNLFKN","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"alphafold_very_low_content":0.4540682414698163,"disorder_content":0.01968503937007874,"disprot_consensus":{"full":[{"start":375,"end":389,"type":"D"}],"Structural state":[{"start":375,"end":389,"type":"D"}],"Disorder function":[{"start":375,"end":389,"type":"F"}]}},{"disprot_id":"DP04052","acc":"Q8I639","creator":"ldobson","date":"2023-03-27T16:55:26.621Z","features":{"pfam":[{"id":"PF03011","name":"PFEMP1 DBL domain","start":1448,"end":1570},{"id":"PF05424","name":"Duffy binding domain","start":95,"end":277},{"id":"PF05424","name":"Duffy binding domain","start":580,"end":759},{"id":"PF05424","name":"Duffy binding domain","start":1253,"end":1432},{"id":"PF05424","name":"Duffy binding domain","start":1603,"end":1769},{"id":"PF05424","name":"Duffy binding domain","start":2030,"end":2192},{"id":"PF05424","name":"Duffy binding domain","start":2365,"end":2512},{"id":"PF15445","name":"acidic terminal segments, variant surface antigen of PfEMP1","start":2650,"end":3011},{"id":"PF15448","name":"N-terminal segments of P. falciparum erythrocyte membrane protein","start":1,"end":50}],"gene3D":[]},"genes":[{"orfNames":[{"value":"PF3D7_1200600","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CZT99168.1","url":"https://www.ebi.ac.uk/ena/browser/view/CZT99168.1"}}]}]}],"length":3056,"name":"Erythrocyte membrane protein 1, PfEMP1","ncbi_taxon_id":36329,"organism":"Plasmodium falciparum (isolate 3D7)","regions":[{"start":2333,"end":2349,"reference_id":"19695262","reference_source":"pmid","reference_html":"Structural comparison of two CSPG-binding DBL domains from the VAR2CSA protein important in malaria during pregnancy. <i> Khunrae P, Philip JM, Bull DR, Higgins MK. </i> J Mol Biol, 2009","date":"2023-04-28T06:55:36.216Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2WAU"}],"region_id":"DP04052r001","statement":[{"text":"Subdomain 1 of DBL6ε consists of residues 2333–2390 with residues 2333–2348 disordered in the crystal.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys2480Ser","start":null,"end":null,"position":null}],"sequence_construct":"ICNKYKNINVNMKKNNDDTWTDLVKNSSDINKGVLLPPRRKNLFLKIDESDICKYKRDPKLFKDFIYSSAISEVERLKKVYGEAKTKVVHAMKYSFADIGSIIKGDDMMENNSSDKIGKILGDGVGQNEKRKKWWDMNKYHIWESMLSGYKHAYGNISENDRKMLDIPNNDDEHQFLRWFQEWTENFCTKRNELYENMVTACNSAKCNTSNGSVDKKECTEACKNYSNFILIKKKEYQSLNSQYDMNYKETKAEKKESPEYFKDKCNGECSCLSEYFKDETRWKNPYETLDDTEVKNNCMCK","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T18:01:06.894Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MDKSSIANKIEAYLGAKSDDSKIDQSLKADPSEVQYYGSGGDGYYLRKNICKITVNHSDSGTNDPCDRIPPPYGDNDQWKCAIILSKVSEKPENVFVPPRRQRMCINNLEKLNVDKIRDKHAFLADVLLTARNEGERIVQNHPDTNSSNVCNALERSFADIADIIRGTDLWKGTNSNLEQNLKQMFAKIRENDKVLQDKYPKDQNYRKLREDWWNANRQKVWEVITCGARSNDLLIKRGWRTSGKSNGDNKLELCRKCGHYEEKVPTKLDYVPQFLRWLTEWIEDFYREKQNLIDDMERHREECTSEDHKSKEGTSYCSTCKDKCKKYCECVKKWKSEWENQKNKYTELYQQNKNETSQKNTSRYDDYVKDFFKKLEANYSSLENYIKGDPYFAEYATKLSFILNSSDANNPSEKIQKNNDEVCNCNESGIASVEQEQISDPSSNKTCITHSSIKANKKKVCKHVKLGVRENDKDLRVCVIEHTSLSGVENCCCQDFLRILQENCSDNKSGSSSNGSCNNKNQEACEKNLEKVLASLTNCYKCDKCKSEQSKKNNKNWIWKKSSGKEGGLQKEYANTIGLPPRTQSLCLVVCLDEKGKKTQELKNIRTNSELLKEWIIAAFHEGKNLKPSHEKKNDDNGKKLCKALEYSFADYGDLIKGTSIWDNEYTKDLELNLQKIFGKLFRKYIKKNNTAEQDTSYSSLDELRESWWNTNKKYIWLAMKHGAGMNSTTCCGDGSVTGSGSSCDDIPTIDLIPQYLRFLQEWVEHFCKQRQEKVKPVIENCKSCKESGGTCNGECKTECKNKCEVYKKFIEDCKGGDGTAGSSWVKRWDQIYKRYSKYIEDAKRNRKAGTKNCGPSSTTNAAENKCVQSDIDSFFKHLIDIGLTTPSSYLSIVLDDNICGADKAPWTTYTTYTTTEKCNKETDKSKLQQCNTAVVVNVPSPLGNTPHGYKYACQCKIPTNEETCDDRKEYMNQWSCGSARTMKRGYKNDNYELCKYNGVDVKPTTVRSNSSKLDDKDVTFFNLFEQWNKEIQYQIEQYMTNTKISCNNEKNVLSRVSDEAAQPKFSDNERDRNSITHEDKNCKEKCKCYSLWIEKINDQWDKQKDNYNKFQRKQIYDANKGSQNKKVVSLSNFLFFSCWEEYIQKYFNGDWSKIKNIGSDTFEFLIKKCGNDSGDGETIFSEKLNNAEKKCKENESTNNKMKSSETSCDCSEPIYIRGCQPKIYDGKIFPGKGGEKQWICKDTIIHGDTNGACIPPRTQNLCVGELWDKRYGGRSNIKNDTKESLKQKIKNAIQKETELLYEYHDKGTAIISRNPMKGQKEKEEKNNDSNGLPKGFCHAVQRSFIDYKNMILGTSVNIYEYIGKLQEDIKKIIEKGTTKQNGKTVGSGAENVNAWWKGIEGEMWDAVRCAITKINKKQKKNGTFSIDECGIFPPTGNDEDQSVSWFKEWSEQFCIERLQYEKNIRDACTNNGQGDKIQGDCKRKCEEYKKYISEKKQEWDKQKTKYENKYVGKSASDLLKENYPECISANFDFIFNDNIEYKTYYPYGDYSSICSCEQVKYYEYNNAEKKNNKSLCHEKGNDRTWSKKYIKKLENGRTLEGVYVPPRRQQLCLYELFPIIIKNKNDITNAKKELLETLQIVAEREAYYLWKQYHAHNDTTYLAHKKACCAIRGSFYDLEDIIKGNDLVHDEYTKYIDSKLNEIFDSSNKNDIETKRARTDWWENEAIAVPNITGANKSDPKTIRQLVWDAMQSGVRKAIDEEKEKKKPNENFPPCMGVQHIGIAKPQFIRWLEEWTNEFCEKYTKYFEDMKSNCNLRKGADDCDDNSNIECKKACANYTNWLNPKRIEWNGMSNYYNKIYRKSNKESEDGKDYSMIMEPTVIDYLNKRCNGEINGNYICCSCKNIGENSTSGTVNKKLQKKETQCEDNKGPLDLMNKVLNKMDPKYSEHKMKCTEVYLEHVEEQLKEIDNAIKDYKLYPLDRCFDDKSKMKVCDLIGDAIGCKHKTKLDELDEWNDVDMRDPYNKYKGVLIPPRRRQLCFSRIVRGPANLRNLKEFKEEILKGAQSEGKFLGNYYNEDKDKEKALEAMKNSFYDYEYIIKGSDMLTNIQFKDIKRKLDRLLEKETNNTEKVDDWWETNKKSIWNAMLCGYKKSGNKIIDPSWCTIPTTETPPQFLRWIKEWGTNVCIQKEEHKEYVKSKCSNVTNLGAQESESKNCTSEIKKYQEWSRKRSIQWEAISEGYKKYKGMDEFKNTFKNIKEPDANEPNANEYLKKHCSKCPCGFNDMQEITKYTNIGNEAFKQIKEQVDIPAELEDVIYRLKHHEYDKGNDYICNKYKNINVNMKKNNDDTWTDLVKNSSDINKGVLLPPRRKNLFLKIDESDICKYKRDPKLFKDFIYSSAISEVERLKKVYGEAKTKVVHAMKYSFADIGSIIKGDDMMENNSSDKIGKILGDGVGQNEKRKKWWDMNKYHIWESMLCGYKHAYGNISENDRKMLDIPNNDDEHQFLRWFQEWTENFCTKRNELYENMVTACNSAKCNTSNGSVDKKECTEACKNYSNFILIKKKEYQSLNSQYDMNYKETKAEKKESPEYFKDKCNGECSCLSEYFKDETRWKNPYETLDDTEVKNNCMCKPPPPASNNTSDILQKTIPFGIALALGSIAFLFMKKKPKTPVDLLRVLDIPKGDYGIPTPKSSNRYIPYASDRYKGKTYIYMEGDTSGDDDKYIWDLSSSDITSSESEYEEVDINDIYVPSFPKYKTFIELVLEPSKRDTFNTSSGDTFTNKLTDDEWNQLKQDFIEQYLQNIQKDFILHDSMDEKPFITQIQDRFLDSSHEEVTYNIDWNVPENINRITNNMDDPKYCSNNMYTGTDLINDSLNGNQYIDIYDEMLKRKENELFGTYHTKYTTFNSVSKQTPSDPIINQLDLYHKWIDKHRDICEQWKTKEDMLYKLNEVWNMERKEYLLDIQPSTLDDIHKINDETYNIISTNNIYDHPSQETPLQLLGSTNIIPSYITTEQNNGLRTNISMDTYIDETNNNNVVATSIIGDDQMENSYNC","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"disorder_content":0.00556282722513089,"disprot_consensus":{"full":[{"start":2333,"end":2349,"type":"D"}],"Structural state":[{"start":2333,"end":2349,"type":"D"}]}},{"disprot_id":"DP04054","acc":"Q57WT9","creator":"ldobson","date":"2023-03-27T17:31:35.928Z","features":{"pfam":[{"id":"PF03590","name":"Aspartate-ammonia ligase","start":13,"end":347}],"gene3D":[]},"genes":[{"name":{"value":"Tb07.27M11.260","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAZ12176.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAZ12176.1"}}]},"orfNames":[{"value":"Tb927.7.1110","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAX69960.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAX69960.1"}}]}]}],"length":351,"name":"Asparagine synthetase a, putative","ncbi_taxon_id":185431,"organism":"Trypanosoma brucei brucei (strain 927/4 GUTat10.1)","regions":[{"start":210,"end":246,"reference_id":"24610810","reference_source":"pmid","reference_html":"Identification and functional characterization of a novel bacterial type asparagine synthetase A: a tRNA synthetase paralog from Leishmania donovani. <i> Manhas R, Tripathi P, Khan S, Sethu Lakshmi B, Lal SK, Gowri VS, Sharma A, Madhubala R. </i> J Biol Chem, 2014","date":"2023-03-27T17:32:43.029Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4LNS"}],"region_id":"DP04054r001","statement":[{"text":"The final electron density for the\nTbASNA model is well defined except for loop 1 (residues\n51–57) and loop 2 (residues 210–250; Figs. 7–9).","type":"Results"},{"text":"The significance of this insertion at this location in the\nstructure of TbASNA is unclear because in the crystal structure\nof apo-TbASNA this loop is completely disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T14:58:07.288Z"}},{"start":210,"end":246,"reference_id":"24610810","reference_source":"pmid","reference_html":"Identification and functional characterization of a novel bacterial type asparagine synthetase A: a tRNA synthetase paralog from Leishmania donovani. <i> Manhas R, Tripathi P, Khan S, Sethu Lakshmi B, Lal SK, Gowri VS, Sharma A, Madhubala R. </i> J Biol Chem, 2014","date":"2023-04-28T06:43:49.093Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4LNS"}],"region_id":"DP04054r002","statement":[{"text":"The final electron density for the TbASNA model is well defined except for loop 1 (residues 51–57) and loop 2 (residues 210–250; Figs. 7–9).","type":"Results"},{"text":"The significance of this insertion at this location in the structure of TbASNA is unclear because in the crystal structure of apo-TbASNA this loop is completely disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-02T16:48:10.157Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MGDDGYSSYVLLQEQILTVKRSFSEALEKELNLVEVRAPILFRVGDGTQDNLSGFEKAVQVPVKAIPNASFEVVHSLAKWKRRTLANYKFAPGHGLYTHMTALRVDDVLDNIHSVVVDQWDWEMVMKDDQRNLAFLKEVVCKVYAAIRKTELAVCEKYKQKPILPETIQFVHAEHLLLAYPNLTAKEREREIAREYGAVFLIGIGAVLSSGDRHDARAPDYDDWTSPVEASQVVFPRTSKPIPTMNSLSSLKGLNGDILLYNPTLDDSLEVSSMGIRVNAEALRHQISLTGDDSLLKSEWHQQLLNGEFPQTVGGGIGQSRMVMFMLRKKHIGEVQCSVWPEEIRKKHNLL","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Trypanosoma"],"dataset":["Neglected tropical diseases proteins"],"alphafold_very_low_content":0.014245014245014245,"disorder_content":0.10541310541310542,"disprot_consensus":{"full":[{"start":210,"end":246,"type":"D"}],"Structural state":[{"start":210,"end":246,"type":"D"}],"Disorder function":[{"start":210,"end":246,"type":"F"}]}},{"disprot_id":"DP04055","acc":"Q2WF71","creator":"zskalman","date":"2023-03-28T11:59:16.512Z","features":{"pfam":[{"id":"PF00041","name":"Fibronectin type III domain","start":428,"end":502},{"id":"PF07679","name":"Immunoglobulin I-set domain","start":308,"end":387},{"id":"PF13855","name":"Leucine rich repeat","start":66,"end":125},{"id":"PF13855","name":"Leucine rich repeat","start":164,"end":222}],"gene3D":[]},"genes":[{"name":{"value":"Lrfn1"},"synonyms":[{"value":"Salm2"},{"value":"Semo1"}]}],"length":766,"name":"Leucine-rich repeat and fibronectin type III domain-containing protein 1","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":233,"end":242,"reference_id":"29348429","reference_source":"pmid","reference_html":"Structural basis of trans-synaptic interactions between PTPδ and SALMs for inducing synapse formation. <i> Goto-Ito S, Yamagata A, Sato Y, Uemura T, Shiroshima T, Maeda A, Imai A, Mori H, Yoshida T, Fukai S. </i> Nat Commun, 2018","date":"2023-05-24T07:41:40.077Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5XWU"}],"region_id":"DP04055r001","statement":[{"text":"Ten\nresidues between the seventh and eighth repeats were disordered.","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q64487","statements":[{"type":"Results","text":"We\ndetermined the crystal structures of apo-SALM5 (LRR–Ig), and\nPTPδ (Ig1–Ig3)–SALM2 (LRR–Ig) and PTPδ (Ig1–Fn1)–SALM5\n(LRR–Ig) complexes at 3.08, 3.16, and 4.18 Å resolutions,\nrespectively (Fig. 1 and Table 1)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:4478249","statements":[{"type":"Methods","text":"For the crystallization of the PTPδ–SALM2 complex, SALM2 LRR–Ig was mixed with PTPδ Ig1–Ig3 at the final concentration of 57 µM each and co-crystallized using the sitting drop vapor diffusion method at 20 °C by mixing 0.5 µL of the complex solution and 0.5 µL of the reservoir solution containing 7% PEG20000 and 0.1 M MES (pH 6.0)."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T12:41:47.984Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MAPGPFSSGLFSPPPAALPFLLLLWAGASRGQPCPGRCICQNVAPTLTMLCAKTGLLFVPPAIDRRVVELRLTDNFIAAVRRRDFANMTSLVHLTLSRNTIGQVAAGAFADLRALRALHLDSNRLAEVRGDQLRGLGNLRHLILGNNQIRKVESAAFDAFLSTVEDLDLSYNNLEALPWEAVGQMVNLNTLTLDHNLIDHIAEGTFVQLHKLVRLDMTSNRLHKLPPDGLFLRSQGGGPKPPTPLTVSFGGNPLHCNCELLWLRRLTREDDLETCATPEHLTDRYFWSIPEEEFLCEPPLITRQAGGRALVVEGQAVSLRCRAVGDPEPVVHWVAPDGRLLGNSSRTRVRGDGTLDVTITTLRDSGTFTCIASNAAGEATAPVEVCVVPLPLMAPPPAAPPPLTEPGSSDIATPGRPGANDSTSERRLVAAELTSSSVLIRWPAQRPVPGIRMYQVQYNSSADDSLVYRMIPSTSQTFLVNDLAAGRAYDLCVLAVYDDGATALPATRVVGCVQFTTAGDPAPCRPLRAHFLGGTMIIAIGGVIVASVLVFIVLLMIRYKVYGDGDSRRIKGTSRTPPRVSHVCSQTNGAGAQQASAPPAPDRYEALREVAVPAAIEAKAMEAEATSTELEVVLGRSLGGSATSLCLLPSEETSGEESRAMTGPRRSRSGALGPPTSAPPTLALVPGGAPARPRPQQRYSFDGDYGALFQSHSYPRRARRTKRHRSTPHLDGAGGGAAGEDGDLGLGSARARLAFTSTEWMLESTV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"alphafold_very_low_content":0.3342036553524804,"disorder_content":0.013054830287206266,"disprot_consensus":{"full":[{"start":233,"end":242,"type":"D"}],"Structural state":[{"start":233,"end":242,"type":"D"}]}},{"disprot_id":"DP04056","acc":"Q96NI6","creator":"zskalman","date":"2023-03-28T12:06:30.510Z","features":{"pfam":[{"id":"PF13855","name":"Leucine rich repeat","start":99,"end":159},{"id":"PF13855","name":"Leucine rich repeat","start":172,"end":213},{"id":"PF13927","name":"Immunoglobulin domain","start":286,"end":361}],"gene3D":[]},"genes":[{"name":{"value":"LRFN5"},"synonyms":[{"value":"C14orf146"},{"value":"SALM5"}]}],"length":719,"name":"Leucine-rich repeat and fibronectin type-III domain-containing protein 5","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":222,"end":231,"reference_id":"29348429","reference_source":"pmid","reference_html":"Structural basis of trans-synaptic interactions between PTPδ and SALMs for inducing synapse formation. <i> Goto-Ito S, Yamagata A, Sato Y, Uemura T, Shiroshima T, Maeda A, Imai A, Mori H, Yoshida T, Fukai S. </i> Nat Commun, 2018","date":"2023-04-21T12:06:01.956Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5XWT"}],"region_id":"DP04056r001","statement":[{"text":"Ten\nresidues between the seventh and eighth repeats were disordered.","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q64487","statements":[{"type":"Results","text":"We\ndetermined the crystal structures of apo-SALM5 (LRR–Ig), and\nPTPδ (Ig1–Ig3)–SALM2 (LRR–Ig) and PTPδ (Ig1–Fn1)–SALM5\n(LRR–Ig) complexes at 3.08, 3.16, and 4.18 Å resolutions,\nrespectively (Fig. 1 and Table 1).\n"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T15:09:50.139Z"}},{"start":292,"end":378,"reference_id":"29348429","reference_source":"pmid","reference_html":"Structural basis of trans-synaptic interactions between PTPδ and SALMs for inducing synapse formation. <i> Goto-Ito S, Yamagata A, Sato Y, Uemura T, Shiroshima T, Maeda A, Imai A, Mori H, Yoshida T, Fukai S. </i> Nat Commun, 2018","date":"2023-03-28T12:09:19.062Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5XWS"}],"region_id":"DP04056r002","statement":[{"text":"In the apo-SALM5 structure,\nthe electron density of the Ig domain was mostly invisible,\nprobably owing to the structural disorder.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T15:08:14.090Z"}},{"start":292,"end":378,"reference_id":"29348429","reference_source":"pmid","reference_html":"Structural basis of trans-synaptic interactions between PTPδ and SALMs for inducing synapse formation. <i> Goto-Ito S, Yamagata A, Sato Y, Uemura T, Shiroshima T, Maeda A, Imai A, Mori H, Yoshida T, Fukai S. </i> Nat Commun, 2018","date":"2023-04-21T12:06:43.964Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5XWS"},{"db":"PDB","id":"5XWT"}],"region_id":"DP04056r003","statement":[{"text":"The electron densities\nof the Ig domains of SALM2 and SALM5 became relatively clear\nupon binding to PTPδ, suggesting that the Ig domains of SALM2\nand SALM5 were partly stabilized by the interaction with PTPδ.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q64487","statements":[{"type":"Results","text":"We\ndetermined the crystal structures of apo-SALM5 (LRR–Ig), and\nPTPδ (Ig1–Ig3)–SALM2 (LRR–Ig) and PTPδ (Ig1–Fn1)–SALM5\n(LRR–Ig) complexes at 3.08, 3.16, and 4.18 Å resolutions,\nrespectively (Fig. 1 and Table 1).\n"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T15:10:29.581Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MEKILFYLFLIGIAVKAQICPKRCVCQILSPNLATLCAKKGLLFVPPNIDRRTVELRLADNFVTNIKRKDFANMTSLVDLTLSRNTISFITPHAFADLRNLRALHLNSNRLTKITNDMFSGLSNLHHLILNNNQLTLISSTAFDDVFALEELDLSYNNLETIPWDAVEKMVSLHTLSLDHNMIDNIPKGTFSHLHKMTRLDVTSNKLQKLPPDPLFQRAQVLATSGIISPSTFALSFGGNPLHCNCELLWLRRLSREDDLETCASPPLLTGRYFWSIPEEEFLCEPPLITRHTHEMRVLEGQRATLRCKARGDPEPAIHWISPEGKLISNATRSLVYDNGTLDILITTVKDTGAFTCIASNPAGEATQIVDLHIIKLPHLLNSTNHIHEPDPGSSDISTSTKSGSNTSSSNGDTKLSQDKIVVAEATSSTALLKFNFQRNIPGIRMFQIQYNGTYDDTLVYRMIPPTSKTFLVNNLAAGTMYDLCVLAIYDDGITSLTATRVVGCIQFTTEQDYVRCHFMQSQFLGGTMIIIIGGIIVASVLVFIIILMIRYKVCNNNGQHKVTKVSNVYSQTNGAQIQGCSVTLPQSVSKQAVGHEENAQCCKATSDNVIQSSETCSSQDSSTTTSALPPSWTSSTSVSQKQKRKTGTKPSTEPQNEAVTNVESQNTNRNNSTALQLASRPPDSVTEGPTSKRAHIKPNALLTNVDQIVQETQRLELI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.29346314325452016,"disorder_content":0.1349095966620306,"disprot_consensus":{"full":[{"start":222,"end":231,"type":"D"},{"start":292,"end":378,"type":"T"}],"Structural state":[{"start":222,"end":231,"type":"D"},{"start":292,"end":378,"type":"D"}],"Structural transition":[{"start":292,"end":378,"type":"T"}]}},{"disprot_id":"DP04057","acc":"Q8BPQ7","creator":"zskalman","date":"2023-03-28T12:22:50.433Z","features":{"pfam":[{"id":"PF00566","name":"Rab-GTPase-TBC domain","start":878,"end":1049},{"id":"PF02759","name":"RUN domain","start":44,"end":187},{"id":"PF12068","name":"Rab-binding domain (RBD)","start":255,"end":391}],"gene3D":[]},"genes":[{"name":{"value":"Sgsm1"},"synonyms":[{"value":"Rutbc2"}]}],"length":1093,"name":"Small G protein signaling modulator 1","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":390,"end":413,"reference_id":"25220469","reference_source":"pmid","reference_html":"Crystal structure of the Rab9A-RUTBC2 RBD complex reveals the molecular basis for the binding specificity of Rab9A with RUTBC2. <i> Zhang Z, Wang S, Shen T, Chen J, Ding J. </i> Structure, 2014","date":"2023-05-24T08:45:00.736Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4QXA"}],"region_id":"DP04057r001","statement":[{"text":"Residues 254–424 of RUTBC2 RBD are well\ndefined except for the loop before the last ß strand (residues\n390–413).","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9R0M6","statements":[{"type":"Results","text":"The results showed that a minimal fragment of RUTBC2\n(residues 254–425) could form a stable complex with the GTPbound\nconstitutively active Rab9A Q66L mutant (residues 1–\n199)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:135398633","statements":[{"type":"Results","text":"The bound GTP and Mg2+ at the active site are also\nclearly defined."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888","statements":[{"type":"Results","text":"The bound GTP and Mg2+ at the active site are also\nclearly defined."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T12:42:30.497Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MASVPAEAETRQRLLRTVKKEVKQIMEEAVTRKFVHEDSSHIISFCAAVEACVLHGLRRRAAGFLRSNKIAALFMKVGKGFPPAEELSRKVQELEQLIESARNQIQGLQENVRKLPKLPNLSPLAIKHLWIRTALFGRVLDKIVHYLVENSSKYYEKEALLMDPVDGPILASLLVGPCALEYTKMKTADHFWTDPSADELVQRHRIHSSHLRQDSPTKRPALCIQKRHSSGSMDDRPSISARDYVESLHQDSRATLLYGKNNVLVQPRDDMEAVPGYLSLHQTADVMTLKWTPNQLMNGSVGDLDYEKSVYWDYAVTIRLEEIVYLHCHQQVDSGGTVVLVSQDGIQRPPFRFPKGGHLLQFLSCLENGLLPHGQLDPPLWSQRGKGKVFPKLRKRSPQGSSESTSSDKEDDEATDYVFRIIYPGTQSEFVPQDLMDVSMNNLPPLWQPSPRKSSCSSCSQSGSADGGSTNGCNHERAPLKLLCDNMKYQILSRAFYGWLAYCRHLSTVRTHLSALVNHMIVSPDLPCDAGQGLTASIWEKYIQDSTTYPEQELLRLIYYGGVQPEIRRAVWPFLLGHYQFGMTEMERKEVDEQIHACYAQTMSEWLGCEAIVRQRERESHAAALAKCSSGASLDSHLHRMLHRDSTISNESSQSCSSGRQNLRLQSDSSSSTQVFESVDEVEQTEAEGRSEEKHPKIPNGNPANGTCSPDSGHPSSHNFSSGLSEHSEPSLSTEDSVLDAQRSLPAVFRPGDSSVEDGQSSEATTSRDEAPREELAVQDSLESDLLANESLEEFMSIPGSLDVALPEKDGAVMDGWPGEADKPSRADSEDNLSEEPEMESLFPALASLAVTSSANNEASPVSSSGVTYSPELLDLYTVNLHRIEKDVQRCDRSYWYFTAANLEKLRNIMCSYIWQHIEIGYVQGMCDLLAPLLVILDDEALAFSCFTELMKRMNQNFPHGGAMDTHFANMRSLIQILDSELFELMHQNGDYTHFYFCYRWFLLDFKRELVYDDVFSVWETIWAAKHVSSAHYVLFIALALVEVYRDIILENNMDFTDIIKFFNEMAERHNAKQILQLARDLVHKVQILIENK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"alphafold_very_low_content":0.35681610247026535,"disorder_content":0.021957913998170174,"disprot_consensus":{"full":[{"start":390,"end":413,"type":"D"}],"Structural state":[{"start":390,"end":413,"type":"D"}]}},{"disprot_id":"DP04058","acc":"Q9R0M6","creator":"zskalman","date":"2023-03-28T12:25:34.445Z","features":{"pfam":[{"id":"PF00071","name":"Ras family","start":9,"end":173}],"gene3D":[]},"genes":[{"name":{"value":"Rab9a"},"synonyms":[{"value":"Rab9"},{"value":"Sid99"}]}],"length":201,"name":"Ras-related protein Rab-9A","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":178,"end":199,"reference_id":"25220469","reference_source":"pmid","reference_html":"Crystal structure of the Rab9A-RUTBC2 RBD complex reveals the molecular basis for the binding specificity of Rab9A with RUTBC2. <i> Zhang Z, Wang S, Shen T, Chen J, Ding J. </i> Structure, 2014","date":"2023-04-21T11:52:24.327Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4QXA"}],"region_id":"DP04058r001","statement":[{"text":"The C-terminal\nhypervariable region of Rab9A is disordered\nand thus not required for RUTBC2 binding.","type":"Abstract"},{"text":"Residues 6–177 of Rab9A are well defined and\nthe C-terminal hypervariable region (residues 178–199) is disordered.","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8BPQ7","statements":[{"type":"Results","text":"The results showed that a minimal fragment of RUTBC2\n(residues 254–425) could form a stable complex with the GTPbound\nconstitutively active Rab9A Q66L mutant (residues 1–\n199).\n"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:135398633","statements":[{"type":"Results","text":"The bound GTP and Mg2+ at the active site are also\nclearly defined.\n"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888","statements":[{"type":"Results","text":"The bound GTP and Mg2+ at the active site are also\nclearly defined.\n"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T15:21:33.378Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MAGKSSLFKIILLGDGGVGKSSLMNRYVTNKFDSQLFHTIGVEFLNKDLEVDGHFVTMQIWDTAGQERFRSLRTPFYRGSDCCLLTFSVDDSQSFQNLSNWKKEFIYYADVKEPESFPFVILGNKTDIKERQVSTEEAQAWCKDNGDYPYFETSAKDSTNVAAAFEEAVRRILATEDRSEHLIQTDTVNLHRKPKPNSSCC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"alphafold_very_low_content":0.009950248756218905,"disorder_content":0.10945273631840796,"disprot_consensus":{"full":[{"start":178,"end":199,"type":"D"}],"Structural state":[{"start":178,"end":199,"type":"D"}]}},{"disprot_id":"DP04059","acc":"Q8BXA0","creator":"zskalman","date":"2023-03-28T12:43:00.282Z","features":{"pfam":[{"id":"PF07679","name":"Immunoglobulin I-set domain","start":289,"end":374},{"id":"PF13855","name":"Leucine rich repeat","start":99,"end":159},{"id":"PF13855","name":"Leucine rich repeat","start":172,"end":213}],"gene3D":[]},"genes":[{"name":{"value":"Lrfn5"},"synonyms":[{"value":"Kiaa4208"},{"value":"Salm5"}]}],"length":719,"name":"Leucine-rich repeat and fibronectin type-III domain-containing protein 5","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":216,"end":233,"reference_id":"29897575","reference_source":"pmid","reference_html":"The structure of SALM5 suggests a dimeric assembly for the presynaptic RPTP ligand recognition. <i> Karki S, Paudel P, Sele C, Shkumatov AV, Kajander T. </i> Protein Eng Des Sel, 2018","date":"2023-03-28T12:43:48.390Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6F2O"}],"region_id":"DP04059r001","statement":[{"text":"It starts with an unusual large insertion, disordered\nin the crystal structure (Gln216-Phe233) before the last\nβ-strand of the extended LRR domain β-sheet; the first ordered residue\nis Ala234 (marked in Fig. 1).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T15:25:24.360Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MEKFLFYLFLIGIAVRAQICPKRCVCQILSPNLATLCAKKGLLFVPPNIDRRTVELRLADNFVTNIKRKDFANMTSLVDLTLSRNTISFITPHAFADLRNLRALHLNSNRLTKITNDMFSGLSNLHHLILNNNQLTLISSTAFDDVFALEELDLSYNNLETIPWDAVEKMVSLHTLSLDHNMIDNIPKGTFSHLHKMTRLDVTSNKLQKLPPDPLFQRAQVLATSGIISPSTFALSFGGNPLHCNCELLWLRRLSREDDLETCASPALLTGRYFWSIPEEEFLCEPPLITRHTHEMRVLEGQRATLRCKARGDPEPAIHWISPEGKLISNATRSLVYDNGTLDILITTVKDTGAFTCIASNPAGEATQTVDLHIIKLPHLLNSTNHIHEPDPGSSDISTSTKSGSNASSSNGDTKMSQDKIVVAEATSSTALLKFNFQRNIPGIRMFQIQYNGTYDDTLVYRMIPPTSKTFLVNNLASGTMYDLCVLAIYDDGITSLTATRVVGCIQFTTEQDYVRCHFMQSQFLGGTMIIIIGGIIVASVLVFIIILMIRYKVCNNNGQHKVTKVSNVYSQTNGAQMQGCSVTLPQSMSKQAMGHEENAQCCKVASDNAIQSSETCSSQDSSTTTSALPPTWTSSAPVSQKQKRKTGTKPSAEPQSEAVTNVESQNTNRNNSTALQLASCPPDSVTEGPTSQRAHTKPNALLTNVDQNVQETQRLESI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"alphafold_very_low_content":0.28929068150208626,"disorder_content":0.025034770514603615,"disprot_consensus":{"full":[{"start":216,"end":233,"type":"D"}],"Structural state":[{"start":216,"end":233,"type":"D"}]}},{"disprot_id":"DP04060","acc":"Q8LGG8","creator":"zskalman","date":"2023-03-28T13:33:50.910Z","features":{"pfam":[{"id":"PF00582","name":"Universal stress protein family","start":23,"end":162}],"gene3D":[]},"genes":[{"orfNames":[{"value":"F4P13.7"}],"olnNames":[{"value":"At3g01520"}]}],"length":175,"name":"Universal stress protein A-like protein","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":56,"end":65,"reference_id":"25921306","reference_source":"pmid","reference_html":"Crystal structure of the protein At3g01520, a eukaryotic universal stress protein-like protein from Arabidopsis thaliana in complex with AMP. <i> Kim DJ, Bitto E, Bingman CA, Kim HJ, Han BW, Phillips GN. </i> Proteins, 2015","date":"2023-04-21T12:30:49.986Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2GM3"}],"region_id":"DP04060r001","statement":[{"text":"Loops\ncomprising residues 56–65 and 137–145 are missing in all\nthe chains in the asymmetric unit, suggesting that these are\nhighly flexible regions.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6083","statements":[{"type":"Results","text":"We have determined the crystal structure of the protein\nAt3g01520 in complex with AMP."}]}],"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":9,"end":9,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":77,"end":77,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":159,"end":159,"position":"Specific residue"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T15:28:26.441Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MGSEPTKVMVAVNASTIKDYPNPSISCKRAFEWTLEKIVRSNTSDFKILLLHVQVVDEDGFDDVDSIYASPEDFRDMRQSNKAKGLHLLEFFVNKCHEIGVGCEAWIKTGDPKDVICQEVKRVRPDFLVVGSRGLGRFQKVFVGTVSAFCVKHAECPVMTIKRNADETPSDPADD","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"alphafold_very_low_content":0.03428571428571429,"disorder_content":0.05714285714285714,"disprot_consensus":{"full":[{"start":56,"end":65,"type":"D"}],"Structural state":[{"start":56,"end":65,"type":"D"}]}},{"disprot_id":"DP04061","acc":"P29617","creator":"zskalman","date":"2023-03-28T13:41:46.843Z","features":{"pfam":[{"id":"PF05044","name":"Homeo-prospero domain","start":1547,"end":1699}],"gene3D":[]},"genes":[{"name":{"value":"pros"},"orfNames":[{"value":"CG17228"}]}],"length":1703,"name":"Homeobox protein prospero","ncbi_taxon_id":7227,"organism":"Drosophila melanogaster","regions":[{"start":1614,"end":1626,"reference_id":"12429095","reference_source":"pmid","reference_html":"Structure of the DNA binding region of prospero reveals a novel homeo-prospero domain. <i> Ryter JM, Doe CQ, Matthews BW. </i> Structure, 2002","date":"2023-04-21T12:32:57.858Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1MIJ"}],"region_id":"DP04061r001","statement":[{"text":"A disordered region from residues 1314–1326 is not delineated.","type":"Figure"},{"text":"The experimental electron density for residues 1245–1396 was readily traceable despite absent density for the disordered loop residues 1314–1326.","type":"Methods"}],"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1551,"end":1551,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1559,"end":1559,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1573,"end":1573,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1603,"end":1603,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1685,"end":1685,"position":"Specific residue"}],"sequence_construct":"SSTLTPMHLRKAKLMFFWVRYPSSAVLKMYFPDIKFNKNNTAQLVKWFSNFREFYYIQMEKYARQAVTEGIKTPDDLLIAGDSELYRVLNLHYNRNNHIEVPQNFRFVVESTLREFFRAIQGGKDTEQSWKKSIYKIISRMDDPVPEYFKSP","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T15:30:49.175Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MMSSEEYEADCFGLYSDENNVLLKANEPETTAATKQQHQPQFQQQQQQQQQQQQHHHQHQQPPPSSNGHTSPIPSQVNGDGSAANCGESGKTNTNTGSHSHSNSGNTNTDADKEQEREKAKEKANEEESEDSDDDVVVVLEGCEGNASSSSSSSNSNSNASSNNHKAAATTTTTATTANHCNRSGGSSRSHRSARSSRQISQSTAVGKTTTCAAKKPTAAQATTTTAKNSNSNSNVNVNVNVNSNGSGNGNANSKVNRRSRQRSLSKDINNQPASSNSNSNSSNNSSNSNGGATATAAGFMSSAAAAAAGAAGGGALFQPQSVSTANSSSSNNNNSSTPAALATHSPTSNSPVSGASSASSLLTAAFGNLFGGSSAKMLNELFGRQMKQAQDATSGLPQSLDNAMLAAAMETATSAELLIGSLNSTSKLLQQQHNNNSIAPANSTPMSNGTNASISPGSAHSSSHSHQGVSPKGSRRVSACSDRSLEAAAADVAGGSPPRAASVSSLNGGASSGEQHQSQLQHDLVAHHMLRNILQGKKELMQLDQELRTAMQQQQQQLQEKEQLHSKLNNNNNNNIAATANNNNNTTMESINLIDDSEMADIKIKSEPQTAPQPQQSPHGSSHSSRSGSGSGSHSSMASDGSLRRKSSDSLDSHGAQDDAQDEEDAAPTGQRSESRAPEEPQLPTKKESVDDMLDEVELLGLHSRGSDMDSLASPSHSDMMLLDKDDVLDEDDDDDCVEQKTSGSGCLKKPGMDLKRARVENIVSGMRCSPSSGLAQAGQLQVNGCKKRKLYQPQQHAMERYVAAAAGLNFGLNLQSMMLDQEDSESNELESPQIQQKRVEKNALKSQLRSMQEQLAEMQQKYVQLCSRMEQESECQELDQDQDVEQEQEPDNGSSDHIELSPSPTLTGDGDVSPNHKEETGQERPGSSSPSPSPLKPKTSLGESSDSGANMLSQMMSKMMSGKLHNPLVGVGHPALPQGFPPLLQHMGDMSHAAAMYQQFFFEQEARMAKEAAEQQQQQQQQQQQQQQQQQQEQQRRFEQEQQEQQRRKEEQQQQIQRQQQHLQQLQQQQMEQQHVATAAPRPQMHHPAPARLPTRMGGAAGHTALKSELSEKFQMLRANNNSSMMRMSGTDLEGLADVLKSEITTSLSALVDTIVTRFVHQRRLFSKQADSVTAAAEQLNKDLLLASQILDRKSPRTKVADRPQNGPTPATQSAAAMFQAPKTPQGMNPVAAAALYNSMTGPFCLPPDQQQQQQTAQQQQSAQQQQQSSQQTQQQLEQNEALSLVVTPKKKRHKVTDTRITPRTVSRILAQDGVVPPTGGPPSTPQQQQQQQQQQQQQQQQQQQQASNGGNSNATPAQSPTRSSGGAAYHPQPPPPPPPMMPVSLPTSVAIPNPSLHESKVFSPYSPFFNPHAAAGQATAAQLHQHHQQHHPHHQSMQLSSSPPGSLGALMDSRDSPPLPHPPSMLHPALLAAAHHGGSPDYKTCLRAVMDAQDRQSECNSADMQFDGMAPTISFYKQMQLKTEHQESLMAKHCESLTPLHSSTLTPMHLRKAKLMFFWVRYPSSAVLKMYFPDIKFNKNNTAQLVKWFSNFREFYYIQMEKYARQAVTEGIKTPDDLLIAGDSELYRVLNLHYNRNNHIEVPQNFRFVVESTLREFFRAIQGGKDTEQSWKKSIYKIISRMDDPVPEYFKSPNFLEQLE","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"alphafold_very_low_content":0.7545507927187316,"dataset":["Condensates-related proteins"],"disorder_content":0.007633587786259542,"disprot_consensus":{"full":[{"start":1614,"end":1626,"type":"D"}],"Structural state":[{"start":1614,"end":1626,"type":"D"}]}},{"disprot_id":"DP04062","acc":"Q9Y4B6","creator":"zskalman","date":"2023-03-28T15:57:17.491Z","features":{"pfam":[{"id":"PF27600","name":"DCAF1 helical domain","start":518,"end":733},{"id":"PF27601","name":"DCAF1 fourth domain","start":739,"end":834},{"id":"PF27635","name":"Mahjong helical domain","start":139,"end":433},{"id":"PF27670","name":"DCAF1 N-terminal domain","start":11,"end":115}],"gene3D":[]},"genes":[{"name":{"value":"DCAF1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:30911","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:30911"}}]},"synonyms":[{"value":"KIAA0800"},{"value":"RIP"},{"value":"VPRBP"}]}],"length":1507,"name":"DDB1- and CUL4-associated factor 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1486,"end":1499,"reference_id":"24706749","reference_source":"pmid","reference_html":"Structural basis of the binding of Merlin FERM domain to the E3 ubiquitin ligase substrate adaptor DCAF1. <i> Li Y, Wei Z, Zhang J, Yang Z, Zhang M. </i> J Biol Chem, 2014","date":"2023-05-24T07:45:43.982Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4P7I"}],"region_id":"DP04062r001","statement":[{"text":"The two beta-strands of DCAF1-FBD are\nwell defined, whereas the loop connecting the hairpin is completely\ndisordered (Fig. 2, A and B).","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P46662","statements":[{"type":"Results","text":"Crystals of the Merlin-FERM:DCAF1-FBD complex were obtained by hanging drop vapor diffusion\nmethod at 16 °C within 5 days.\n"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753","statements":[{"type":"Methods","text":"Before diffraction\nexperiments, crystals were soaked in crystallization solution containing\n30% glycerol for cryoprotection."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T12:42:57.778Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MTTVVVHVDSKAELTTLLEQWEKEHGSGQDMVPILTRMSQLIEKETEEYRKGDPDPFDDRHPGRADPECMLGHLLRILFKNDDFMNALVNAYVMTSREPPLNTAACRLLLDIMPGLETAVVFQEKEGIVENLFKWAREADQPLRTYSTGLLGGAMENQDIAANYRDENSQLVAIVLRRLRELQLQEVALRQENKRPSPRKLSSEPLLPLDEEAVDMDYGDMAVDVVDGDQEEASGDMEISFHLDSGHKTSSRVNSTTKPEDGGLKKNKSAKQGDRENFRKAKQKLGFSSSDPDRMFVELSNSSWSEMSPWVIGTNYTLYPMTPAIEQRLILQYLTPLGEYQELLPIFMQLGSRELMMFYIDLKQTNDVLLTFEALKHLASLLLHNKFATEFVAHGGVQKLLEIPRPSMAATGVSMCLYYLSYNQDAMERVCMHPHNVLSDVVNYTLWLMECSHASGCCHATMFFSICFSFRAVLELFDRYDGLRRLVNLISTLEILNLEDQGALLSDDEIFASRQTGKHTCMALRKYFEAHLAIKLEQVKQSLQRTEGGILVHPQPPYKACSYTHEQIVEMMEFLIEYGPAQLYWEPAEVFLKLSCVQLLLQLISIACNWKTYYARNDTVRFALDVLAILTVVPKIQLQLAESVDVLDEAGSTVSTVGISIILGVAEGEFFIHDAEIQKSALQIIINCVCGPDNRISSIGKFISGTPRRKLPQNPKSSEHTLAKMWNVVQSNNGIKVLLSLLSIKMPITDADQIRALACKALVGLSRSSTVRQIISKLPLFSSCQIQQLMKEPVLQDKRSDHVKFCKYAAELIERVSGKPLLIGTDVSLARLQKADVVAQSRISFPEKELLLLIRNHLISKGLGETATVLTKEADLPMTAASHSSAFTPVTAAASPVSLPRTPRIANGIATRLGSHAAVGASAPSAPTAHPQPRPPQGPLALPGPSYAGNSPLIGRISFIRERPSPCNGRKIRVLRQKSDHGAYSQSPAIKKQLDRHLPSPPTLDSIITEYLREQHARCKNPVATCPPFSLFTPHQCPEPKQRRQAPINFTSRLNRRASFPKYGGVDGGCFDRHLIFSRFRPISVFREANEDESGFTCCAFSARERFLMLGTCTGQLKLYNVFSGQEEASYNCHNSAITHLEPSRDGSLLLTSATWSQPLSALWGMKSVFDMKHSFTEDHYVEFSKHSQDRVIGTKGDIAHIYDIQTGNKLLTLFNPDLANNYKRNCATFNPTDDLVLNDGVLWDVRSAQAIHKFDKFNMNISGVFHPNGLEVIINTEIWDLRTFHLLHTVPALDQCRVVFNHTGTVMYGAMLQADDEDDLMEERMKSPFGSSFRTFNATDYKPIATIDVKRNIFDLCTDTKDCYLAVIENQGSMDALNMDTVCRLYEVGRQRLAEDEDEEEDQEEEEQEEEDDDEDDDDTDDLDELDTDQLLEAELEEDDNNENAGEDGDNDFSPSDEELANLLEEGEDGEDEDSDADEEVELILGDTDSSDNSDLEDDIILSLNE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.24419376244193763,"disorder_content":0.0092899800928998,"disprot_consensus":{"full":[{"start":1486,"end":1499,"type":"D"}],"Structural state":[{"start":1486,"end":1499,"type":"D"}]}},{"disprot_id":"DP04063","acc":"P07275","creator":"vnugnes","date":"2023-04-03T17:21:48.036Z","features":{"pfam":[{"id":"PF00171","name":"Aldehyde dehydrogenase family","start":74,"end":556}],"gene3D":[]},"genes":[{"name":{"value":"PUT2"},"olnNames":[{"value":"YHR037W"}]}],"length":575,"name":"Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":524,"end":546,"reference_id":"24502590","reference_source":"pmid","reference_html":"Structural studies of yeast Δ(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): active site flexibility and oligomeric state. <i> Pemberton TA, Srivastava D, Sanyal N, Henzl MT, Becker DF, Tanner JJ. </i> Biochemistry, 2014","date":"2023-04-03T17:27:28.516Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4OE6"}],"region_id":"DP04063r001","statement":[{"text":"Electron density for the 23-residue aldehyde substrate-binding loop is absent, implying substantial conformational flexibility in solution. We furthermore report a new crystal form of human ALDH4A1 (42% identical to Put2p) that also shows disorder in this loop.","type":"Abstract"},{"text":"The most conspicuous feature of the Put2p structure is that which is unseen. ALDHs have an ∼25-residue peptide that connects the last strand of the catalytic domain to the second piece of the oligomerization domain. This section corresponds to residues 523–547 of Put2p. Electron density for these residues is very weak, implying substantial conformational disorder (Figure ​3A).","type":"Results"}]},{"start":23,"end":42,"reference_id":"24502590","reference_source":"pmid","reference_html":"Structural studies of yeast Δ(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): active site flexibility and oligomeric state. <i> Pemberton TA, Srivastava D, Sanyal N, Henzl MT, Becker DF, Tanner JJ. </i> Biochemistry, 2014","date":"2023-11-21T12:01:06.324Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4OE6"}],"region_id":"DP04063r002","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered. ","type":"Curator statement"}]},{"start":379,"end":390,"reference_id":"24502590","reference_source":"pmid","reference_html":"Structural studies of yeast Δ(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): active site flexibility and oligomeric state. <i> Pemberton TA, Srivastava D, Sanyal N, Henzl MT, Becker DF, Tanner JJ. </i> Biochemistry, 2014","date":"2023-11-21T12:01:12.331Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4OE6"}],"region_id":"DP04063r003","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered. ","type":"Curator statement"}]},{"start":566,"end":575,"reference_id":"24502590","reference_source":"pmid","reference_html":"Structural studies of yeast Δ(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): active site flexibility and oligomeric state. <i> Pemberton TA, Srivastava D, Sanyal N, Henzl MT, Becker DF, Tanner JJ. </i> Biochemistry, 2014","date":"2023-11-21T12:01:17.472Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4OE6"}],"region_id":"DP04063r004","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered. ","type":"Curator statement"}]},{"start":379,"end":395,"reference_id":"24502590","reference_source":"pmid","reference_html":"Structural studies of yeast Δ(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): active site flexibility and oligomeric state. <i> Pemberton TA, Srivastava D, Sanyal N, Henzl MT, Becker DF, Tanner JJ. </i> Biochemistry, 2014","date":"2023-11-21T12:01:25.901Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4OE4"}],"region_id":"DP04063r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5892"}],"statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered. ","type":"Curator statement"}]}],"regions_counter":5,"released":"2024_06","sequence":"MLSARCLKSIYFKRSFSQLGHIKPPKHIRNEPVKPFRNIDLKDWDLLRASLMKFKSSSLEVPLVINGERIYDNNERALFPQTNPANHQQVLANVTQATEKDVMNAVKAAKDAKKDWYNLPFYDRSAIFLKAADLISTKYRYDMLAATMLGQGKNVYQAEIDCITELSDFFRYYVKYASDLYAQQPVESADGTWNKAEYRPLEGFVYAVSPFNFTAIAANLIGAPALMGNTVVWKPSQTAALSNYLLMTVLEEAGLPKGVINFIPGDPVQVTDQVLADKDFGALHFTGSTNVFKSLYGKIQSGVVEGKYRDYPRIIGETGGKNFHLVHPSANISHAVLSTIRGTFEFQGQKCSAASRLYLPESKSEEFLSDMFGILQSQNVVPMNTSASPISGGNLRGFMGPVIHEQSFDKLVKVIEDAKKDPELEILYGGQYDKSQGWFVGPTVIKAKRPDHPYMSTEFFGPILTVYEYPDTEFNEICDIIDNTSQYALTGAIFAKDRKAIEYADEKLKFSAGNFYINDKCTGAVVSQQWFGGARMSGTDDKAGGPNILSRFVSIRNTKENFYELTDFKYPSNYE","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.02608695652173913,"disorder_content":0.12173913043478261,"disprot_consensus":{"full":[{"start":23,"end":42,"type":"D"},{"start":379,"end":395,"type":"D"},{"start":524,"end":546,"type":"D"},{"start":566,"end":575,"type":"D"}],"Structural state":[{"start":23,"end":42,"type":"D"},{"start":379,"end":395,"type":"D"},{"start":524,"end":546,"type":"D"},{"start":566,"end":575,"type":"D"}]}},{"disprot_id":"DP04064","acc":"Q62765-2","creator":"vnugnes","date":"2023-04-05T14:50:14.216Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"Nlgn1"}}],"length":814,"name":"Isoform 2 of Neuroligin-1","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions":[{"start":548,"end":562,"reference_id":"18093522","reference_source":"pmid","reference_html":"Structures of neuroligin-1 and the neuroligin-1/neurexin-1 beta complex reveal specific protein-protein and protein-Ca2+ interactions. <i> Araç D, Boucard AA, Ozkan E, Strop P, Newell E, Südhof TC, Brunger AT. </i> Neuron, 2007","date":"2023-11-28T14:43:59.246Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3BIW"}],"region_id":"DP04064r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q63372"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"}],"statement":[{"text":"Inspection of the electron density maps revealed weak electron density for the following loops: NL1 577–591, NL1 637–642, NL1 445–450, Nrx1β 289–291.","type":"Methods"},{"text":"The region 577-591 that the authors mention corresponds to the 548-562 region of the Isoform 2 of Neuroligin-1 that was assessed.","type":"Curator statement"}]},{"start":548,"end":562,"reference_id":"18093522","reference_source":"pmid","reference_html":"Structures of neuroligin-1 and the neuroligin-1/neurexin-1 beta complex reveal specific protein-protein and protein-Ca2+ interactions. <i> Araç D, Boucard AA, Ozkan E, Strop P, Newell E, Südhof TC, Brunger AT. </i> Neuron, 2007","date":"2023-11-28T14:49:43.448Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3BIW"},{"db":"PDB","id":"3BIX"}],"region_id":"DP04064r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q63372"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:174"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:934"}],"statement":[{"text":"Inspection of the electron density maps revealed weak electron density for the following loops: NL1 577–591, NL1 637–642, NL1 445–450, Nrx1β 289–291.","type":"Methods"},{"text":"The region 577-591 that the authors mention corresponds to the 548-562 region of the Isoform 2 of Neuroligin-1 that was assessed.","type":"Curator statement"},{"text":"PDB structures show this region is disordered when forming a complex with  Neurexin-1, but ordered when the proteins is in solution.","type":"Curator statement"}],"states_connection":[{"source":"DP04064r003","target":"DP04064r001"}]},{"start":548,"end":562,"reference_id":"18093522","reference_source":"pmid","reference_html":"Structures of neuroligin-1 and the neuroligin-1/neurexin-1 beta complex reveal specific protein-protein and protein-Ca2+ interactions. <i> Araç D, Boucard AA, Ozkan E, Strop P, Newell E, Südhof TC, Brunger AT. </i> Neuron, 2007","date":"2023-11-28T14:49:07.849Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3BIX"}],"region_id":"DP04064r003","statement":[{"text":"PDB structures show this region is disordered when forming a complex with Neurexin-1, but ordered when the proteins is in solution.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:174"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:934"}]}],"regions_counter":3,"released":"2024_06","sequence":"MALPRCMWPNYVWRAMMACVVHRGSGAPLTLCLLGCLLQTFHVLSQKLDDVDPLVTTNFGKIRGIKKELNNEILGPVIQFLGVPYAAPPTGEHRFQPPEPPSPWSDIRNATQFAPVCPQNIIDGRLPEVMLPVWFTNNLDVVSSYVQDQSEDCLYLNIYVPTEDDIRDSGGPKPVMVYIHGGSYMEGTGNLYDGSVLASYGNVIVITVNYRLGVLGFLSTGDQAAKGNYGLLDLIQALRWTSENIGFFGGDPLRITVFGSGAGGSCVNLLTLSHYSEGLFQRAIAQSGTALSSWAVSFQPAKYARILATKVGCNVSDTVELVECLQKKPYKELVDQDVQPARYHIAFGPVIDGDVIPDDPQILMEQGEFLNYDIMLGVNQGEGLKFVENIVDSDDGVSASDFDFAVSNFVDNLYGYPEGKDVLRETIKFMYTDWADRHNPETRRKTLLALFTDHQWVAPAVATADLHSNFGSPTYFYAFYHHCQTDQVPAWADAAHGDEVPYVLGIPMIGPTELFPCNFSKNDVMLSAVVMTYWTNFAKTGDPNQPVPQDTKFIHTKPNRFEEVAWTRYSQKDQLYLHIGLKPRVKEHYRANKVNLWLELVPHLHNLNDISQYTSTTTKVPSTDITLRPTRKNSTPVTSAFPTAKQDDPKQQPSPFSVDQRDYSTELSVTIAVGASLLFLNILAFAALYYKKDKRRHDVHRRCSPQRTTTNDLTHAPEEEIMSLQMKHTDLDHECESIHPHEVVLRTACPPDYTLAMRRSPDDVPLMTPNTITMIPNTIPGIQPLHTFNTFTGGQNNTLPHPHPHPHSHSTTRV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"disorder_content":0.018427518427518427,"disprot_consensus":{"full":[{"start":548,"end":562,"type":"T"}],"Structural state":[{"start":548,"end":562,"type":"D"}],"Structural transition":[{"start":548,"end":562,"type":"T"}]}},{"disprot_id":"DP04065","acc":"P38319","creator":"vacs","date":"2023-04-06T10:40:45.970Z","features":{"pfam":[{"id":"PF06087","name":"Tyrosyl-DNA phosphodiesterase","start":84,"end":529}],"gene3D":[]},"genes":[{"name":{"value":"TDP1"},"orfNames":[{"value":"YBR1520"}],"olnNames":[{"value":"YBR223C"}]}],"length":544,"name":"Tyrosyl-DNA phosphodiesterase 1","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":67,"reference_id":"17707402","reference_source":"pmid","reference_html":"Mutation of a conserved active site residue converts tyrosyl-DNA phosphodiesterase I into a DNA topoisomerase I-dependent poison. <i> He X, van Waardenburg RCAM, Babaoglu K, Price AC, Nitiss KC, Nitiss JL, Bjornsti MA, White SW. </i> J Mol Biol, 2007","date":"2023-04-06T10:47:57.065Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001191","ec_ontology":"ECO","ec_name":"in vitro cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04065r001","statement":[{"text":"During crystallization trials of full-length yTdp1, protein degradation was observed from the N terminus, but limited trypsin digestion revealed that the N-terminal 67 residues could be removed to generate a stable molecule.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T15:46:09.026Z"}},{"start":68,"end":78,"reference_id":"17707402","reference_source":"pmid","reference_html":"Mutation of a conserved active site residue converts tyrosyl-DNA phosphodiesterase I into a DNA topoisomerase I-dependent poison. <i> He X, van Waardenburg RCAM, Babaoglu K, Price AC, Nitiss KC, Nitiss JL, Bjornsti MA, White SW. </i> J Mol Biol, 2007","date":"2023-04-21T16:24:48.048Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04065r002","statement":[{"text":"The structure revealed that 11 and five additional residues could be removed from the N terminus and the C terminus, respectively, and Tdp1-Δ2 yielded superior crystals that generated the final 2.0 Å structure.","type":"Results"},{"text":"The crystal structure of an equivalent fragment of human Tdp1 allowed some missing segments to be added,25 but we were unable to locate any electron density for N-terminal residues 68–78 or Cterminal residues 540–544.","type":"Methods"}],"cross_refs":[{"db":"PDB","id":"1Q32"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T16:28:56.479Z"}},{"start":342,"end":352,"reference_id":"17707402","reference_source":"pmid","reference_html":"Mutation of a conserved active site residue converts tyrosyl-DNA phosphodiesterase I into a DNA topoisomerase I-dependent poison. <i> He X, van Waardenburg RCAM, Babaoglu K, Price AC, Nitiss KC, Nitiss JL, Bjornsti MA, White SW. </i> J Mol Biol, 2007","date":"2023-04-06T10:51:43.462Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1Q32"}],"region_id":"DP04065r003","statement":[{"text":"All four molecules contain five peripheral regions that are not visible in the electron density map and are presumably disordered (Figure 1(a) and (b)).","type":"Results"},{"text":"Residues 342-352 are missing in all chains and are presumably disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T15:46:12.120Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MSRETNFNGTKRKRSDVAEKVAQRWKSVRYSAEMENMAPVNSNNDSDDCVIVSESKIIDLTNQEQDLSERIETNDTAKGAVFKLMKSDFYEREDFMGEVEDMITLKDIFGTETLKRSILFSFQYELDFLLRQFHQNVENITIVGQKGTIMPIEARAMDATLAVILKKVKLIEITMPPFASHHTKLIINFYDNGECKIFLPSNNFTSMETNLPQQVCWCSPLLKIGKEGLPVPFKRSLIEYLNSYHLKDIDELITKSVEEVNFAPLSELEFVYSTPSKFQSSGLLSFYNKLEKLSAGTSASDTAKHYLCQTSSIGTSLSRARDENLWTHLMIPLFTGIMSPPAKDTAGRKKAEILPTNSLINEYSQRKIKPYIIFPTEQEFVTSPLKWSSSGWFHFQYLQKKSYYEMLRNKFKVFYKQDPAMVTRRRGTTPAHSKFYMHCATNSAGPCDASQVFKELEWCLYTSANLSQTAWGTVSRKPRNYEAGVLYHSRRLANTRKVTCRTFTRDRRGCAGNPTHVAVPFTLPVIPYDLAEDECFCLARHEND","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.14338235294117646,"disorder_content":0.1636029411764706,"disprot_consensus":{"full":[{"start":1,"end":78,"type":"D"},{"start":342,"end":352,"type":"D"}],"Structural state":[{"start":1,"end":78,"type":"D"},{"start":342,"end":352,"type":"D"}]}},{"disprot_id":"DP04066","acc":"P0A8P8","creator":"vacs","date":"2023-04-09T13:52:01.282Z","features":{"pfam":[{"id":"PF00589","name":"Phage integrase family","start":112,"end":285},{"id":"PF02899","name":"Phage integrase, N-terminal SAM-like domain","start":8,"end":90}],"gene3D":[]},"genes":[{"name":{"value":"xerD"},"synonyms":[{"value":"xprB"}],"olnNames":[{"value":"b2894"},{"value":"JW2862"}]}],"length":298,"name":"Tyrosine recombinase XerD","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":101,"end":110,"reference_id":"9311978","reference_source":"pmid","reference_html":"Crystal structure of the site-specific recombinase, XerD. <i> Subramanya HS, Arciszewska LK, Baker RA, Bird LE, Sherratt DJ, Wigley DB. </i> EMBO J, 1997","date":"2023-04-09T13:53:40.384Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1A0P"}],"region_id":"DP04066r001","statement":[{"text":"The missing residues are located at the N- and C-termini and in three disordered surface loops.","type":"Results"},{"text":"Residues that are not defined are located at the N- and C-termini and in three disordered loops (residues 64–70, 101–110 and 269–270).","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T15:50:20.679Z"}},{"start":101,"end":110,"reference_id":"9311978","reference_source":"pmid","reference_html":"Crystal structure of the site-specific recombinase, XerD. <i> Subramanya HS, Arciszewska LK, Baker RA, Bird LE, Sherratt DJ, Wigley DB. </i> EMBO J, 1997","date":"2023-04-09T13:55:14.289Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1A0P"}],"region_id":"DP04066r002","statement":[{"text":"The enzyme comprises two domains: domain 1 consists of residues 1–107, while domain 2 comprises residues 108–298 (Figure 1).","type":"Results"},{"text":"Based on the structure, loop 101-110 is a flexible linker region between the two domains of the protein.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-21T15:50:20.780Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MKQDLARIEQFLDALWLEKNLAENTLNAYRRDLSMMVEWLHHRGLTLATAQSDDLQALLAERLEGGYKATSSARLLSAVRRLFQYLYREKFREDDPSAHLASPKLPQRLPKDLSEAQVERLLQAPLIDQPLELRDKAMLEVLYATGLRVSELVGLTMSDISLRQGVVRVIGKGNKERLVPLGEEAVYWLETYLEHGRPWLLNGVSIDVLFPSQRAQQMTRQTFWHRIKHYAVLAGIDSEKLSPHVLRHAFATHLLNHGADLRVVQMLLGHSDLSTTQIYTHVATERLRQLHQQHHPRA","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"alphafold_very_low_content":0.04697986577181208,"disorder_content":0.03355704697986577,"disprot_consensus":{"full":[{"start":101,"end":110,"type":"D"}],"Structural state":[{"start":101,"end":110,"type":"D"}],"Disorder function":[{"start":101,"end":110,"type":"F"}]}},{"disprot_id":"DP04067","acc":"Q9H078","creator":"cpintado","date":"2023-04-24T15:31:32.063Z","features":{"pfam":[{"id":"PF07724","name":"AAA domain (Cdc48 subfamily)","start":376,"end":565},{"id":"PF10431","name":"C-terminal, D2-small domain, of ClpB protein","start":574,"end":650},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":130,"end":196},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":258,"end":323}],"gene3D":[]},"genes":[{"name":{"value":"CLPB"},"synonyms":[{"value":"HSP78"},{"value":"SKD3"}]}],"length":707,"name":"Caseinolytic peptidase B protein homolog","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":208,"end":227,"reference_id":"37041140","reference_source":"pmid","reference_html":"Structural basis of impaired disaggregase function in the oxidation-sensitive SKD3 mutant causing 3-methylglutaconic aciduria. <i> Lee S, Lee SB, Sung N, Xu WW, Chang C, Kim HE, Catic A, Tsai FTF. </i> Nat Commun, 2023","date":"2023-04-24T15:38:24.268Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"8DEH"}],"region_id":"DP04067r001","statement":[{"text":"The long β-hairpin of Ank2 is labeled with the disordered regions flanking helix α5 (brown) indicated by dashed lines. ","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-04-25T15:47:50.071Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MLGSLVLRRKALAPRLLLRLLRSPTLRGHGGASGRNVTTGSLGEPQWLRVATGGRPGTSPALFSGRGAATGGRQGGRFDTKCLAAATWGRLPGPEETLPGQDSWNGVPSRAGLGMCALAAALVVHCYSKSPSNKDAALLEAARANNMQEVSRLLSEGADVNAKHRLGWTALMVAAINRNNSVVQVLLAAGADPNLGDDFSSVYKTAKEQGIHSLEDGGQDGASRHITNQWTSALEFRRWLGLPAGVLITREDDFNNRLNNRASFKGCTALHYAVLADDYRTVKELLDGGANPLQRNEMGHTPLDYAREGEVMKLLRTSEAKYQEKQRKREAEERRRFPLEQRLKEHIIGQESAIATVGAAIRRKENGWYDEEHPLVFLFLGSSGIGKTELAKQTAKYMHKDAKKGFIRLDMSEFQERHEVAKFIGSPPGYVGHEEGGQLTKKLKQCPNAVVLFDEVDKAHPDVLTIMLQLFDEGRLTDGKGKTIDCKDAIFIMTSNVASDEIAQHALQLRQEALEMSRNRIAENLGDVQISDKITISKNFKENVIRPILKAHFRRDEFLGRINEIVYFLPFCHSELIQLVNKELNFWAKRAKQRHNITLLWDREVADVLVDGYNVHYGARSIKHEVERRVVNQLAAAYEQDLLPGGCTLRITVEDSDKQLLKSPELPSPQAEKRLPKLRLEIIDKDSKTRRLDIRAPLHPEKVCNTI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.25035360678925034,"disorder_content":0.028288543140028287,"disprot_consensus":{"full":[{"start":208,"end":227,"type":"D"}],"Structural state":[{"start":208,"end":227,"type":"D"}]}},{"disprot_id":"DP04068","acc":"P19632","creator":"zskalman","date":"2023-04-26T12:35:23.098Z","features":{"pfam":[{"id":"PF02114","name":"Phosducin","start":1,"end":244}],"gene3D":[]},"genes":[{"name":{"value":"PDC"}}],"length":245,"name":"Phosducin","ncbi_taxon_id":9913,"organism":"Bos taurus","regions":[{"start":36,"end":67,"reference_id":"9739091","reference_source":"pmid","reference_html":"Phosducin induces a structural change in transducin beta gamma. <i> Loew A, Ho YK, Blundell T, Bax B. </i> Structure, 1998","date":"2023-05-24T08:18:14.185Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1A0R"}],"region_id":"DP04068r001","statement":[{"text":"Residues P35–P65 of phosducin are largely disordered and do not make contact with the top of the β propeller of Gtβ. Instead, residues in this loop make contact with a symmetry-related molecule (1/2–x,1–y,1/2+z).","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62871","statements":[{"type":"Results","text":"The structure of the phosducin–Gtβ1γ1 complex was determined by molecular replacement."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02698","statements":[{"type":"Results","text":"The structure of the phosducin–Gtβ1γ1 complex was determined by molecular replacement."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:444108","statements":[{"type":"Results","text":"The current model of the bovine retinal phosducin–Gtβ1γ1 complex (crystal variant A — space group P212121; a = 76.09, b = 87.91, c = 98.74 å) consisting of some 592 amino acids, 21 waters and a farnesyl group has an R factor (R free) of 22.2% (26.1%) for data (F > 2σ) to 2.8 å."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T12:47:55.419Z"}},{"start":1,"end":12,"reference_id":"9739091","reference_source":"pmid","reference_html":"Phosducin induces a structural change in transducin beta gamma. <i> Loew A, Ho YK, Blundell T, Bax B. </i> Structure, 1998","date":"2023-05-24T08:30:15.291Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04068r002","statement":[{"text":"Residues not in bold type have poor electron density in phosducin (and may be quite mobile parts of the structure), or are regions in the rat phosducin-like protein and the two yeast phosducin-like proteins that are likely to have a different structure to that observed in phosducin.","type":"Figure"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62871","statements":[{"type":"Results","text":"The structure of the phosducin–Gtβ1γ1 complex was determined by molecular replacement."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02698","statements":[{"type":"Results","text":"The structure of the phosducin–Gtβ1γ1 complex was determined by molecular replacement."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:444108","statements":[{"type":"Results","text":"The current model of the bovine retinal phosducin–Gtβ1γ1 complex (crystal variant A — space group P212121; a = 76.09, b = 87.91, c = 98.74 å) consisting of some 592 amino acids, 21 waters and a farnesyl group has an R factor (R free) of 22.2% (26.1%) for data (F > 2σ) to 2.8 å."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T12:47:54.568Z"}},{"start":231,"end":245,"reference_id":"9739091","reference_source":"pmid","reference_html":"Phosducin induces a structural change in transducin beta gamma. <i> Loew A, Ho YK, Blundell T, Bax B. </i> Structure, 1998","date":"2023-05-24T08:28:30.787Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1A0R"}],"region_id":"DP04068r003","statement":[{"text":"Residues not in bold type have poor electron density in phosducin (and may be quite mobile parts of the structure), or are regions in the rat phosducin-like protein and the two yeast phosducin-like proteins that are likely to have a different structure to that observed in phosducin.","type":"Figure"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62871","statements":[{"type":"Results","text":"The structure of the phosducin–Gtβ1γ1 complex was determined by molecular replacement."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02698","statements":[{"type":"Results","text":"The structure of the phosducin–Gtβ1γ1 complex was determined by molecular replacement."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:444108","statements":[{"type":"Results","text":"The current model of the bovine retinal phosducin–Gtβ1γ1 complex (crystal variant A — space group P212121; a = 76.09, b = 87.91, c = 98.74 å) consisting of some 592 amino acids, 21 waters and a farnesyl group has an R factor (R free) of 22.2% (26.1%) for data (F > 2σ) to 2.8 å."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T12:47:53.935Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MEKAKSQSLEEDFEGQASHTGPKGVINDWRKFKLESEDSDSVAHSKKEILRQMSSPQSRDDKDSKERFSRKMSVQEYELIHKDKEDENCLRKYRRQCMQDMHQKLSFGPRYGFVYELESGEQFLETIEKEQKITTIVVHIYEDGIKGCDALNSSLICLAAEYPMVKFCKIKASNTGAGDRFSSDVLPTLLVYKGGELLSNFISVTEQLAEEFFTGDVESFLNEYGLLPEKEMHVLEQTNMEEDME","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"alphafold_very_low_content":0.10612244897959183,"disorder_content":0.24081632653061225,"disprot_consensus":{"full":[{"start":1,"end":12,"type":"D"},{"start":36,"end":67,"type":"D"},{"start":231,"end":245,"type":"D"}],"Structural state":[{"start":1,"end":12,"type":"D"},{"start":36,"end":67,"type":"D"},{"start":231,"end":245,"type":"D"}]}},{"disprot_id":"DP04070","acc":"Q96F81","creator":"fkordevani","date":"2023-05-04T08:27:03.887Z","features":{"pfam":[{"id":"PF03176","name":"MMPL family","start":973,"end":1123},{"id":"PF12349","name":"Sterol-sensing domain of SREBP cleavage-activation","start":525,"end":662}],"gene3D":[]},"genes":[{"name":{"value":"DISP1"},"synonyms":[{"value":"DISPA"}]}],"length":1524,"name":"Protein dispatched homolog 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":254,"end":291,"reference_id":"32646883","reference_source":"pmid","reference_html":"Structure of human Dispatched-1 provides insights into Hedgehog ligand biogenesis.  <i> Chen H, Liu Y, Li X. </i> Life Sci Alliance, 2020","date":"2023-05-04T08:31:11.703Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6XE6"}],"region_id":"DP04070r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:65082"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"}],"statement":[{"text":"On the other hand, the loop between residues 253–292, which is absent in both PTCH1 and NPC1, is disordered in the map (Fig 2B and C), indicating that the flexibility of this large loop permits it to be accessible to Furin and the cleavage by Furin may release this internal loop to facilitate the endosomal trafficking of DISP1 (Stewart et al, 2018).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T13:25:52.583Z"}},{"start":254,"end":291,"reference_id":"32646883","reference_source":"pmid","reference_html":"Structure of human Dispatched-1 provides insights into Hedgehog ligand biogenesis.  <i> Chen H, Liu Y, Li X. </i> Life Sci Alliance, 2020","date":"2023-05-04T08:31:34.766Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6XE6"}],"region_id":"DP04070r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:65082"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"}],"statement":[{"text":"On the other hand, the loop between residues 253–292, which is absent in both PTCH1 and NPC1, is disordered in the map (Fig 2B and C), indicating that the flexibility of this large loop permits it to be accessible to Furin and the cleavage by Furin may release this internal loop to facilitate the endosomal trafficking of DISP1 (Stewart et al, 2018).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T13:25:56.622Z"}},{"start":390,"end":414,"reference_id":"32646883","reference_source":"pmid","reference_html":"Structure of human Dispatched-1 provides insights into Hedgehog ligand biogenesis.  <i> Chen H, Liu Y, Li X. </i> Life Sci Alliance, 2020","date":"2023-05-04T08:33:47.163Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6XE6"}],"region_id":"DP04070r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:65082"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"}],"statement":[{"text":"The densities of residues 172–178, 253–294, 306–312, 337–347, 390–414, 442–446, 477–484, 663–687, 771–777, 866–871, 897–902, and 1,145–1,249 were not resolved nor built.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T13:25:20.804Z"}},{"start":663,"end":687,"reference_id":"32646883","reference_source":"pmid","reference_html":"Structure of human Dispatched-1 provides insights into Hedgehog ligand biogenesis.  <i> Chen H, Liu Y, Li X. </i> Life Sci Alliance, 2020","date":"2023-05-04T08:34:21.237Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6XE6"}],"region_id":"DP04070r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:65082"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"}],"statement":[{"text":"The densities of residues 172–178, 253–294, 306–312, 337–347, 390–414, 442–446, 477–484, 663–687, 771–777, 866–871, 897–902, and 1,145–1,249 were not resolved nor built.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T13:25:10.182Z"}},{"start":1145,"end":1249,"reference_id":"32646883","reference_source":"pmid","reference_html":"Structure of human Dispatched-1 provides insights into Hedgehog ligand biogenesis.  <i> Chen H, Liu Y, Li X. </i> Life Sci Alliance, 2020","date":"2023-05-04T08:34:41.564Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6XE6"}],"region_id":"DP04070r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:65082"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"}],"statement":[{"text":"The densities of residues 172–178, 253–294, 306–312, 337–347, 390–414, 442–446, 477–484, 663–687, 771–777, 866–871, 897–902, and 1,145–1,249 were not resolved nor built.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-04T13:24:01.954Z"}},{"start":1,"end":180,"reference_id":"34845226","reference_source":"pmid","reference_html":"Structural insights into proteolytic activation of the human Dispatched1 transporter for Hedgehog morphogen release. <i> Li W, Wang L, Wierbowski BM, Lu M, Dong F, Liu W, Li S, Wang P, Salic A, Gong X. </i> Nat Commun, 2021","date":"2023-05-05T12:54:30.820Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7E2I"}],"region_id":"DP04070r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:65082"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"}],"statement":[{"text":"An N-terminal cytoplasmic segment consisting of 180 amino acid residues preceding TM1, and the C-terminal cytoplasmic segment consisting of 380 residues following TM12 were not resolved in either cryo-EM density map (Fig. 2c and Supplementary Fig. 4c), likely due to their intrinsic flexibility.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp572Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp573Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp1051Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T13:20:02.562Z"}},{"start":1149,"end":1524,"reference_id":"34845226","reference_source":"pmid","reference_html":"Structural insights into proteolytic activation of the human Dispatched1 transporter for Hedgehog morphogen release. <i> Li W, Wang L, Wierbowski BM, Lu M, Dong F, Liu W, Li S, Wang P, Salic A, Gong X. </i> Nat Commun, 2021","date":"2023-05-05T12:55:52.693Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7E2I"}],"region_id":"DP04070r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:65082"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"}],"statement":[{"text":"An N-terminal cytoplasmic segment consisting of 180 amino acid residues preceding TM1, and the C-terminal cytoplasmic segment consisting of 380 residues following TM12 were not resolved in either cryo-EM density map (Fig. 2c and Supplementary Fig. 4c), likely due to their intrinsic flexibility.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp572Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp573Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp1051Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T13:20:07.790Z"}},{"start":263,"end":280,"reference_id":"34845226","reference_source":"pmid","reference_html":"Structural insights into proteolytic activation of the human Dispatched1 transporter for Hedgehog morphogen release. <i> Li W, Wang L, Wierbowski BM, Lu M, Dong F, Liu W, Li S, Wang P, Salic A, Gong X. </i> Nat Commun, 2021","date":"2023-05-08T13:34:10.798Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000048","term_name":"limited proteolysis display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP04070r008","statement":[{"text":"Purified hDisp1NNN migrated on SDS-PAGE as two larger bands with apparent molecular weights of ~175 and ~145kDa, and two smaller bands with apparent molecular weights of ~35 and ~30kDa (Fig. 1b, left panel). Western blotting indicated that the 175kDa band corresponds to FL hDisp1NNN, as it contained both the N-terminal Flag tag and C-terminal His tag, the 145kDa band corresponds to a cleaved product with only the C-terminal His tag (hDisp1NNN-C145), while the two smaller bands correspond to cleaved products with only the N-terminal Flag tag (hDisp1NNN-N35 and hDisp1NNN-N30) (Fig. 1b, right panel). This cleavage pattern of hDisp1NNN is consistent with the recently reported partial cleavage of mouse and Drosophila Disp proteins by Furin protease31.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp572Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp573Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp1051Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T14:02:54.429Z"}},{"start":1,"end":180,"reference_id":"34845226","reference_source":"pmid","reference_html":"Structural insights into proteolytic activation of the human Dispatched1 transporter for Hedgehog morphogen release. <i> Li W, Wang L, Wierbowski BM, Lu M, Dong F, Liu W, Li S, Wang P, Salic A, Gong X. </i> Nat Commun, 2021","date":"2023-05-08T13:25:39.909Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp572Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp573Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp1051Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]}],"cross_refs":[{"db":"PDB","id":"7E2I"}],"region_id":"DP04070r009","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:65082"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"}],"statement":[{"text":"Disp homologues contain 12 transmembrane segments (TMs), two large extracellular domains (ECD1 and ECD2), as well as flexible N- and C-terminal intracellular domains.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T13:28:59.839Z"}},{"start":1145,"end":1524,"reference_id":"34845226","reference_source":"pmid","reference_html":"Structural insights into proteolytic activation of the human Dispatched1 transporter for Hedgehog morphogen release. <i> Li W, Wang L, Wierbowski BM, Lu M, Dong F, Liu W, Li S, Wang P, Salic A, Gong X. </i> Nat Commun, 2021","date":"2023-05-08T13:25:48.442Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp572Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp573Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp1051Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]}],"cross_refs":[{"db":"PDB","id":"7E2I"}],"region_id":"DP04070r010","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:65082"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"}],"statement":[{"text":"Disp homologues contain 12 transmembrane segments (TMs), two large extracellular domains (ECD1 and ECD2), as well as flexible N- and C-terminal intracellular domains.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T13:29:00.470Z"}},{"start":662,"end":686,"reference_id":"34845226","reference_source":"pmid","reference_html":"Structural insights into proteolytic activation of the human Dispatched1 transporter for Hedgehog morphogen release. <i> Li W, Wang L, Wierbowski BM, Lu M, Dong F, Liu W, Li S, Wang P, Salic A, Gong X. </i> Nat Commun, 2021","date":"2023-05-05T13:13:29.744Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp572Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp573Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp1051Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]}],"cross_refs":[{"db":"PDB","id":"7E2I"}],"region_id":"DP04070r011","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:65082"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"}],"statement":[{"text":"The PDB shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T13:29:30.576Z"}},{"start":263,"end":285,"reference_id":"34845226","reference_source":"pmid","reference_html":"Structural insights into proteolytic activation of the human Dispatched1 transporter for Hedgehog morphogen release. <i> Li W, Wang L, Wierbowski BM, Lu M, Dong F, Liu W, Li S, Wang P, Salic A, Gong X. </i> Nat Commun, 2021","date":"2023-05-05T13:10:11.104Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp572Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp573Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp1051Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]}],"cross_refs":[{"db":"PDB","id":"7E2I"}],"region_id":"DP04070r012","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:65082"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"}],"statement":[{"text":"A connecting loop between residues 263–285 in ECD1 (named the C-loop, for protease cleavage) is not well-resolved in our reconstruction, indicating its flexibility; we speculate that this permits its accessibility to Furin or 3C protease cleavage (Fig. 2b). While the absence of density for the C-loop creates the appearance of a large cavity between the two ECDs (Fig. 2a, b), it is important to emphasize that the C-loop, though unstructured, still occupies this space in uncleaved hDisp1NNN-3C (see below).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T13:28:51.957Z"}},{"start":263,"end":285,"reference_id":"34845226","reference_source":"pmid","reference_html":"Structural insights into proteolytic activation of the human Dispatched1 transporter for Hedgehog morphogen release. <i> Li W, Wang L, Wierbowski BM, Lu M, Dong F, Liu W, Li S, Wang P, Salic A, Gong X. </i> Nat Commun, 2021","date":"2023-05-05T13:10:26.966Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp572Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp573Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp1051Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]}],"cross_refs":[{"db":"PDB","id":"7E2I"}],"region_id":"DP04070r013","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:65082"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"}],"statement":[{"text":"A connecting loop between residues 263–285 in ECD1 (named the C-loop, for protease cleavage) is not well-resolved in our reconstruction, indicating its flexibility; we speculate that this permits its accessibility to Furin or 3C protease cleavage (Fig. 2b). While the absence of density for the C-loop creates the appearance of a large cavity between the two ECDs (Fig. 2a, b), it is important to emphasize that the C-loop, though unstructured, still occupies this space in uncleaved hDisp1NNN-3C (see below).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T13:29:59.039Z"}},{"start":263,"end":280,"reference_id":"34845226","reference_source":"pmid","reference_html":"Structural insights into proteolytic activation of the human Dispatched1 transporter for Hedgehog morphogen release. <i> Li W, Wang L, Wierbowski BM, Lu M, Dong F, Liu W, Li S, Wang P, Salic A, Gong X. </i> Nat Commun, 2021","date":"2023-05-08T13:34:46.111Z","curator_id":"fkordevani","curator_name":"Fatemeh Kordevani","curator_orcid":"0000-0002-2473-6747","term_id":"IDPO:0000048","term_name":"limited proteolysis display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP04070r014","statement":[{"text":"To this end, we replaced the region in hDisp1 recognized by Furin (residues 263–280) with a cleavage site for the highly specific 3C protease (Fig. 1c), and we purified to homogeneity the resulting hDisp1NNN-3C protein (Supplementary Fig. 1c). Purified hDisp1NNN-3C migrated as a single band on SDS-PAGE, of the same molecular weight as FL hDisp1NNN (Fig. 1d). Notably, the hDisp1NNN-3C preparation was devoid of the low molecular weight species found in purified hDisp1NNN (Fig. 1d), indicating that Furin cleavage had been successfully abolished.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp572Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp573Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp1051Asn","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Ultimately, a triple-point mutant (hereafter hDisp1NNN) in which three conserved aspartate residues located in transmembrane helices TM4 and TM10 (Asp572, Asp573, and Asp1051) are mutated to asparagine, showed sufficient expression and was well behaved biochemically after purification in detergent (Supplementary Fig. 1a); this Disp1 mutant is known to bind Shh stronger than WT Disp114."}]},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Lys263-Arg280del","start":null,"end":null,"position":null,"statements":[{"type":"Curator statement","text":"Region 263-280 of the protein was replaced by the sequence SSLEVLFQGPGS which is recognized by the 3C protease."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-08T14:02:47.195Z"}}],"regions_counter":14,"released":"2023_06","sequence":"MAMSNGNNDFVVLSNSSIATSAANPSPLTPCDGDHAAQQLTPKEATRTKVSPNGCLQLNGTVKSSFLPLDNQRMPQMLPQCCHPCPYHHPLTSHSSHQECHPEAGPAAPSALASCCMQPHSEYSASLCPNHSPVYQTTCCLQPSPSFCLHHPWPDHFQHQPVQQHIANIRPSRPFKLPKSYAALIADWPVVVLGMCTMFIVVCALVGVLVPELPDFSDPLLGFEPRGTAIGQRLVTWNNMVKNTGYKATLANYPFKYADEQAKSHRDDRWSDDHYEREKREVDWNFHKDSFFCDVPSDRYSRVVFTSSGGETLWNLPAIKSMCNVDNSRIRSHPQFGDLCQRTTAASCCPSWTLGNYIAILNNRSSCQKIVERDVSHTLKLLRTCAKHYQNGTLGPDCWDMAARRKDQLKCTNVPRKCTKYNAVYQILHYLVDKDFMTPKTADYATPALKYSMLFSPTEKGESMMNIYLDNFENWNSSDGVTTITGIEFGIKHSLFQDYLLMDTVYPAIAIVIVLLVMCVYTKSMFITLMTMFAIISSLIVSYFLYRVVFHFEFFPFMNLTALIILVGIGADDAFVLCDVWNYTKFDKPHAETSETVSITLQHAALSMFVTSFTTAAAFYANYVSNITAIRCFGVYAGTAILVNYVLMVTWLPAVVVLHERYLLNIFTCFKKPQQQIYDNKSCWTVACQKCHKVLFAISEASRIFFEKVLPCIVIKFRYLWLFWFLALTVGGAYIVCINPKMKLPSLELSEFQVFRSSHPFERYDAEYKKLFMFERVHHGEELHMPITVIWGVSPEDNGNPLNPKSKGKLTLDSSFNIASPASQAWILHFCQKLRNQTFFYQTDEQDFTSCFIETFKQWMENQDCDEPALYPCCSHWSFPYKQEIFELCIKRAIMELERSTGYHLDSKTPGPRFDINDTIRAVVLEFQSTYLFTLAYEKMHQFYKEVDSWISSELSSAPEGLSNGWFVSNLEFYDLQDSLSDGTLIAMGLSVAVAFSVMLLTTWNIIISLYAIISIAGTIFVTVGSLVLLGWELNVLESVTISVAVGLSVDFAVHYGVAYRLAPDPDREGKVIFSLSRVGSAMAMAALTTFVAGAMMMPSTVLAYTQLGTFMMLIMCISWAFATFFFQCMCRCLGPQGTCGQIPLPKKLQCSAFSHALSTSPSDKGQSKTHTINAYHLDPRGPKSELEHEFYELEPLASHSCTAPEKTTYEETHICSEFFNSQAKNLGMPVHAAYNSELSKSTESDAGSALLQPPLEQHTVCHFFSLNQRCSCPDAYKHLNYGPHSCQQMGDCLCHQCSPTTSSFVQIQNGVAPLKATHQAVEGFVHPITHIHHCPCLQGRVKPAGMQNSLPRNFFLHPVQHIQAQEKIGKTNVHSLQRSIEEHLPKMAEPSSFVCRSTGSLLKTCCDPENKQRELCKNRDVSNLESSGGTENKAGGKVELSLSQTDASVNSEHFNQNEPKVLFNHLMGEAGCRSCPNNSQSCGRIVRVKCNSVDCQMPNMEANVPAVLTHSELSGESLLIKTL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.38910761154855644,"disorder_content":0.4258530183727034,"disprot_consensus":{"full":[{"start":1,"end":180,"type":"D"},{"start":254,"end":291,"type":"D"},{"start":390,"end":414,"type":"D"},{"start":662,"end":687,"type":"D"},{"start":1145,"end":1524,"type":"D"}],"Structural state":[{"start":1,"end":180,"type":"D"},{"start":254,"end":291,"type":"D"},{"start":390,"end":414,"type":"D"},{"start":662,"end":687,"type":"D"},{"start":1145,"end":1524,"type":"D"}],"Disorder function":[{"start":1,"end":180,"type":"F"},{"start":254,"end":291,"type":"F"},{"start":1145,"end":1524,"type":"F"}]}},{"disprot_id":"DP04072","acc":"Q12402","creator":"viglesias","date":"2023-05-04T13:55:29.971Z","features":{"pfam":[{"id":"PF03134","name":"TB2/DP1, HVA22 family","start":71,"end":147}],"gene3D":[]},"genes":[{"name":{"value":"YOP1"},"synonyms":[{"value":"YIP2"}],"orfNames":[{"value":"YP9367.08"}],"olnNames":[{"value":"YPR028W"}]}],"length":180,"name":"Protein YOP1","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":79,"end":88,"reference_id":"25646439","reference_source":"pmid","reference_html":"A conserved amphipathic helix is required for membrane tubule formation by Yop1p. <i> Brady JP, Claridge JK, Smith PG, Schnell JR. </i> Proc Natl Acad Sci U S A, 2015","date":"2023-05-12T11:36:51.664Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04072r001","statement":[{"text":"As expected, the amide cross-peaks of the N- and C-terminal residues, the loop between TM1 and TM2 (comprising the GGVG motif), the flexible region connecting TM2 and TM3, and the region connecting the C-terminal end of TM4 and the APH were broadened, indicating exposure to the water-soluble Mn+2EDDA (Fig. 3B).","type":"Results"},{"text":"Compared with the C terminus, the next most flexible region is the region of the 10-residue loop connecting TM2 to TM3.","type":"Results"},{"text":"In Figure 3 authors state residues 79-88 constitute a linker region","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-12T15:11:19.847Z"}},{"start":79,"end":88,"reference_id":"25646439","reference_source":"pmid","reference_html":"A conserved amphipathic helix is required for membrane tubule formation by Yop1p. <i> Brady JP, Claridge JK, Smith PG, Schnell JR. </i> Proc Natl Acad Sci U S A, 2015","date":"2023-05-12T11:35:28.820Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04072r002","statement":[{"text":"As expected, the amide cross-peaks of the N- and C-terminal residues, the loop between TM1 and TM2 (comprising the GGVG motif), the flexible region connecting TM2 and TM3, and the region connecting the C-terminal end of TM4 and the APH were broadened, indicating exposure to the water-soluble Mn+2EDDA (Fig. 3B)","type":"Results"},{"text":"Compared with the C terminus, the next most flexible region is the region of the 10-residue loop connecting TM2 to TM3.","type":"Results"},{"text":"In Figure 3 authors state residues 79-88 constitute a linker region.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-12T15:11:20.485Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MSEYASSIHSQMKQFDTKYSGNRILQQLENKTNLPKSYLVAGLGFAYLLLIFINVGGVGEILSNFAGFVLPAYLSLVALKTPTSTDDTQLLTYWIVFSFLSVIEFWSKAILYLIPFYWFLKTVFLIYIALPQTGGARMIYQKIVAPLTDRYILRDVSKTEKDEIRASVNEASKATGASVH","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0,"disorder_content":0.05555555555555555,"disprot_consensus":{"full":[{"start":79,"end":88,"type":"D"}],"Structural state":[{"start":79,"end":88,"type":"D"}],"Disorder function":[{"start":79,"end":88,"type":"F"}]}},{"disprot_id":"DP04073","acc":"P63103","creator":"zskalman","date":"2023-05-05T09:00:00.000Z'","features":{"pfam":[{"id":"PF00244","name":"14-3-3 protein","start":9,"end":229}],"gene3D":[]},"genes":[{"name":{"value":"YWHAZ"}}],"length":245,"name":"14-3-3 protein zeta/delta","ncbi_taxon_id":9913,"organism":"Bos taurus","regions":[{"start":204,"end":215,"reference_id":"7603574","reference_source":"pmid","reference_html":"Crystal structure of the zeta isoform of the 14-3-3 protein. <i> Liu D, Bienkowska J, Petosa C, Collier RJ, Fu H, Liddington R. </i> Nature, 1995","date":"2023-05-24T18:01:00.843Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1A4O"}],"region_id":"DP04073r001","statement":[{"text":"The disordered loop formed by residues 203 to 216 is shown schematically as a thin ribbon.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-29T16:22:48.161Z"}},{"start":229,"end":245,"reference_id":"7603574","reference_source":"pmid","reference_html":"Crystal structure of the zeta isoform of the 14-3-3 protein. <i> Liu D, Bienkowska J, Petosa C, Collier RJ, Fu H, Liddington R. </i> Nature, 1995","date":"2023-05-24T18:04:47.386Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1A4O"}],"region_id":"DP04073r002","statement":[{"text":"Surface-charge representation of a monomer of 14-3-3 calculated with the program GRASP21 , after removal of the C-terminal loop (231 to 245).","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-29T16:24:26.592Z"}},{"start":229,"end":245,"reference_id":"7603574","reference_source":"pmid","reference_html":"Crystal structure of the zeta isoform of the 14-3-3 protein. <i> Liu D, Bienkowska J, Petosa C, Collier RJ, Fu H, Liddington R. </i> Nature, 1995","date":"2023-06-14T13:11:49.195Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1A4O"}],"region_id":"DP04073r003","statement":[{"text":"Surface-charge representation of a monomer of 14-3-3 calculated with the program GRASP21 , after removal of the C-terminal loop (231 to 245).","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-15T11:09:39.450Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQAESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAGEGGEN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"alphafold_very_low_content":0.04081632653061224,"disorder_content":0.11836734693877551,"disprot_consensus":{"full":[{"start":204,"end":215,"type":"D"},{"start":229,"end":245,"type":"D"}],"Structural state":[{"start":204,"end":215,"type":"D"},{"start":229,"end":245,"type":"D"}],"Disorder function":[{"start":229,"end":245,"type":"F"}]}},{"disprot_id":"DP04074","acc":"Q9Y6X9","creator":"mgoncalves","date":"2023-05-05T10:14:32.376Z","features":{"pfam":[{"id":"PF07496","name":"CW-type Zinc Finger","start":496,"end":541},{"id":"PF13589","name":"Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase","start":30,"end":169},{"id":"PF17942","name":"Morc6 ribosomal protein S5 domain 2-like","start":329,"end":451},{"id":"PF23327","name":"ATPase MORC2, chromo domain-like","start":792,"end":855}],"gene3D":[]},"genes":[{"name":{"value":"MORC2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:23573","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:23573"}}]},"synonyms":[{"value":"KIAA0852"},{"value":"ZCWCC1"}]}],"length":1032,"name":"ATPase MORC2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":551,"end":603,"reference_id":"29440755","reference_source":"pmid","reference_html":"Neuropathic MORC2 mutations perturb GHKL ATPase dimerization dynamics and epigenetic silencing by multiple structural mechanisms. <i> Douse CH, Bloor S, Liu Y, Shamin M, Tchasovnikarova IA, Timms RT, Lehner PJ, Modis Y. </i> Nat Commun, 2018","date":"2023-05-10T10:34:44.583Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5OF9"}],"region_id":"DP04074r001","statement":[{"text":"We did not observe electron density for the second predicted coiled coil, CC2 (residues 551–603).","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:33113"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-11T13:15:28.507Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MAFTNYSSLNRAQLTFEYLHTNSTTHEFLFGALAELVDNARDADATRIDIYAERREDLRGGFMLCFLDDGAGMDPSDAASVIQFGKSAKRTPESTQIGQYGNGLKSGSMRIGKDFILFTKKEDTMTCLFLSRTFHEEEGIDEVIVPLPTWNARTREPVTDNVEKFAIETELIYKYSPFRTEEEVMTQFMKIPGDSGTLVIIFNLKLMDNGEPELDIISNPRDIQMAETSPEGTKPERRSFRAYAAVLYIDPRMRIFIHGHKVQTKRLSCCLYKPRMYKYTSSRFKTRAEQEVKKAEHVARIAEEKAREAESKARTLEVRLGGDLTRDSRVMLRQVQNRAITLRREADVKKRIKEAKQRALKEPKELNFVFGVNIEHRDLDGMFIYNCSRLIKMYEKVGPQLEGGMACGGVVGVVDVPYLVLEPTHNKQDFADAKEYRHLLRAMGEHLAQYWKDIAIAQRGIIKFWDEFGYLSANWNQPPSSELRYKRRRAMEIPTTIQCDLCLKWRTLPFQLSSVEKDYPDTWVCSMNPDPEQDRCEASEQKQKVPLGTFRKDMKTQEEKQKQLTEKIRQQQEKLEALQKTTPIRSQADLKKLPLEVTTRPSTEEPVRRPQRPRSPPLPAVIRNAPSRPPSLPTPRPASQPRKAPVISSTPKLPALAAREEASTSRLLQPPEAPRKPANTLVKTASRPAPLVQQLSPSLLPNSKSPREVPSPKVIKTPVVKKTESPIKLSPATPSRKRSVAVSDEEEVEEEAERRKERCKRGRFVVKEEKKDSNELSDSAGEEDSADLKRAQKDKGLHVEVRVNREWYTGRVTAVEVGKHVVRWKVKFDYVPTDTTPRDRWVEKGSEDVRLMKPPSPEHQSLDTQQEGGEEEVGPVAQQAIAVAEPSTSECLRIEPDTTALSTNHETIDLLVQILRNCLRYFLPPSFPISKKQLSAMNSDELISFPLKEYFKQYEVGLQNLCNSYQSRADSRAKASEESLRTSERKLRETEEKLQKLRTNIVALLQKVQEDIDINTDDELDAYIEDLITKGD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.23449612403100775,"disorder_content":0.05135658914728682,"disprot_consensus":{"full":[{"start":551,"end":603,"type":"D"}],"Structural state":[{"start":551,"end":603,"type":"D"}]}},{"disprot_id":"DP04075","acc":"Q9Y2M5","creator":"mgoncalves","date":"2023-05-05T13:02:49.240Z","features":{"pfam":[{"id":"PF00651","name":"BTB/POZ domain","start":59,"end":164},{"id":"PF01344","name":"Kelch motif","start":496,"end":540},{"id":"PF01344","name":"Kelch motif","start":543,"end":587},{"id":"PF07707","name":"BTB And C-terminal Kelch","start":170,"end":270},{"id":"PF24681","name":"KLHDC2/KLHL20/DRC7 Kelch-repeats domain","start":316,"end":495}],"gene3D":[]},"genes":[{"name":{"value":"KLHL20"},"synonyms":[{"value":"KLEIP"},{"value":"KLHLX"}]}],"length":609,"name":"Kelch-like protein 20","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":303,"end":316,"reference_id":"31279627","reference_source":"pmid","reference_html":"Structural Basis for Recruitment of DAPK1 to the KLHL20 E3 Ligase. <i> Chen Z, Picaud S, Filippakopoulos P, D'Angiolella V, Bullock AN. </i> Structure, 2019","date":"2023-05-10T14:40:59.887Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6GY5"}],"region_id":"DP04075r001","statement":[{"text":"The structure was refined at 1.1-Å resolution and traced the full KLHL20 Kelch domain from residues 317 to 601 (Figure 3A).","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu302Ser","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:923"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:174"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P53355"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-11T13:16:01.569Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MEGKPMRRCTNIRPGETGMDVTSRCTLGDPNKLPEGVPQPARMPYISDKHPRQTLEVINLLRKHRELCDVVLVVGAKKIYAHRVILSACSPYFRAMFTGELAESRQTEVVIRDIDERAMELLIDFAYTSQITVEEGNVQTLLPAACLLQLAEIQEACCEFLKRQLDPSNCLGIRAFADTHSCRELLRIADKFTQHNFQEVMESEEFMLLPANQLIDIISSDELNVRSEEQVFNAVMAWVKYSIQERRPQLPQVLQHVRLPLLSPKFLVGTVGSDPLIKSDEECRDLVDEAKNYLLLPQERPLMQGPRTRPRKPIRCGEVLFAVGGWCSGDAISSVERYDPQTNEWRMVASMSKRRCGVGVSVLDDLLYAVGGHDGSSYLNSVERYDPKTNQWSSDVAPTSTCRTSVGVAVLGGFLYAVGGQDGVSCLNIVERYDPKENKWTRVASMSTRRLGVAVAVLGGFLYAVGGSDGTSPLNTVERYNPQENRWHTIAPMGTRRKHLGCAVYQDMIYAVGGRDDTTELSSAERYNPRTNQWSPVVAMTSRRSGVGLAVVNGQLMAVGGFDGTTYLKTIEVFDPDANTWRLYGGMNYRRLGGGVGVIKMTHCESHIW","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.06239737274220033,"disorder_content":0.022988505747126436,"disprot_consensus":{"full":[{"start":303,"end":316,"type":"D"}],"Structural state":[{"start":303,"end":316,"type":"D"}]}},{"disprot_id":"DP04076","acc":"P35790","creator":"mgoncalves","date":"2023-05-09T11:04:34.506Z","features":{"pfam":[{"id":"PF01633","name":"Choline/ethanolamine kinase","start":114,"end":449}],"gene3D":[]},"genes":[{"name":{"value":"CHKA"},"synonyms":[{"value":"CHK"},{"value":"CKI","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"1618328","url":"http://www.ncbi.nlm.nih.gov/pubmed/1618328","alternativeUrl":"https://europepmc.org/abstract/MED/1618328"}}]}]}],"length":457,"name":"Choline kinase alpha","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":151,"end":173,"reference_id":"20299452","reference_source":"pmid","reference_html":"Crystal structures of human choline kinase isoforms in complex with hemicholinium-3: single amino acid near the active site influences inhibitor sensitivity. <i> Hong BS, Allali-Hassani A, Tempel W, Finerty PJ, Mackenzie F, Dimov S, Vedadi M, Park HW. </i> J Biol Chem, 2010","date":"2023-05-10T11:27:06.100Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3G15"}],"region_id":"DP04076r001","statement":[{"text":"In the ΔN-ChoKα1 ternary complex, for instance, the region flanking the segment (residues 155–172), which is missing in ChoKα2 due to alternative splicing (Fig. 1), was invisible in our maps.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:25023712"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-11T13:18:11.172Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MKTKFCTGGEAEPSPLGLLLSCGSGSAAPAPGVGQQRDAASDLESKQLGGQQPPLALPPPPPLPLPLPLPQPPPPQPPADEQPEPRTRRRAYLWCKEFLPGAWRGLREDEFHISVIRGGLSNMLFQCSLPDTTATLGDEPRKVLLRLYGAILQMRSCNKEGSEQAQKENEFQGAEAMVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKYLKEVLRIKFTEESRIKKLHKLLSYNLPLELENLRSLLESTPSPVVFCHNDCQEGNILLLEGRENSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRANIRKYPTKKQQLHFISSYLPAFQNDFENLSTEEKSIIKEEMLLEVNRFALASHFLWGLWSIVQAKISSIEFGYMDYAQARFDAYFHQKRKLGV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.19912472647702406,"disorder_content":0.05032822757111598,"disprot_consensus":{"full":[{"start":151,"end":173,"type":"D"}],"Structural state":[{"start":151,"end":173,"type":"D"}]}},{"disprot_id":"DP04077","acc":"Q9UQ13","creator":"mgoncalves","date":"2023-05-09T12:54:38.536Z","features":{"pfam":[{"id":"PF13855","name":"Leucine rich repeat","start":124,"end":181},{"id":"PF23598","name":"Leucine-rich repeat region","start":209,"end":338},{"id":"PF23598","name":"Leucine-rich repeat region","start":444,"end":526}],"gene3D":[]},"genes":[{"name":{"value":"SHOC2"},"synonyms":[{"value":"KIAA0862"}]}],"length":582,"name":"Leucine-rich repeat protein SHOC-2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":85,"reference_id":"35768504","reference_source":"pmid","reference_html":"Structural basis for SHOC2 modulation of RAS signalling. <i> Liau NPD, Johnson MC, Izadi S, Gerosa L, Hammel M, Bruning JM, Wendorff TJ, Phung W, Hymowitz SG, Sudhamsu J. </i> Nature, 2022","date":"2023-05-09T13:03:55.459Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7SD1"}],"region_id":"DP04077r001","statement":[{"text":"High-resolution x-ray crystal structures of this region from other PP1C binding partners overlay well with this density (Extended Data Fig. 6d–f), whereas the rest of the SHOC2 N terminus (residues 1–85) was disordered (Extended Data Figs. 3e and 5d).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-09T15:02:29.140Z"}},{"start":1,"end":85,"reference_id":"35768504","reference_source":"pmid","reference_html":"Structural basis for SHOC2 modulation of RAS signalling. <i> Liau NPD, Johnson MC, Izadi S, Gerosa L, Hammel M, Bruning JM, Wendorff TJ, Phung W, Hymowitz SG, Sudhamsu J. </i> Nature, 2022","date":"2023-05-10T11:39:56.332Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP04077r002","statement":[{"text":"All proteins show an extended tail at high r values indicative of the unfolded SHOC2 N terminus.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-11T13:19:44.147Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MSSSLGKEKDSKEKDPKVPSAKEREKEAKASGGFGKESKEKEPKTKGKDAKDGKKDSSAAQPGVAFSVDNTIKRPNPAPGTRKKSSNAEVIKELNKCREENSMRLDLSKRSIHILPSSIKELTQLTELYLYSNKLQSLPAEVGCLVNLMTLALSENSLTSLPDSLDNLKKLRMLDLRHNKLREIPSVVYRLDSLTTLYLRFNRITTVEKDIKNLSKLSMLSIRENKIKQLPAEIGELCNLITLDVAHNQLEHLPKEIGNCTQITNLDLQHNELLDLPDTIGNLSSLSRLGLRYNRLSAIPRSLAKCSALEELNLENNNISTLPESLLSSLVKLNSLTLARNCFQLYPVGGPSQFSTIYSLNMEHNRINKIPFGIFSRAKVLSKLNMKDNQLTSLPLDFGTWTSMVELNLATNQLTKIPEDVSGLVSLEVLILSNNLLKKLPHGLGNLRKLRELDLEENKLESLPNEIAYLKDLQKLVLTNNQLTTLPRGIGHLTNLTHLGLGENLLTHLPEEIGTLENLEELYLNDNPNLHSLPFELALCSKLSIMSIENCPLSHLPPQIVAGGPSFIIQFLKMQGPYRAMV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.14432989690721648,"disorder_content":0.14604810996563575,"disprot_consensus":{"full":[{"start":1,"end":85,"type":"D"}],"Structural state":[{"start":1,"end":85,"type":"D"}]}},{"disprot_id":"DP04078","acc":"P35790-2","creator":"mgoncalves","date":"2023-05-10T10:51:50.617Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"CHKA"},"synonyms":[{"value":"CHK"},{"value":"CKI","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"1618328","url":"http://www.ncbi.nlm.nih.gov/pubmed/1618328","alternativeUrl":"https://europepmc.org/abstract/MED/1618328"}}]}]}],"length":439,"name":"Isoform 2 of Choline kinase alpha","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":50,"end":81,"reference_id":"17007874","reference_source":"pmid","reference_html":"Elucidation of human choline kinase crystal structures in complex with the products ADP or phosphocholine. <i> Malito E, Sekulic N, Too WC, Konrad M, Lavie A. </i> J Mol Biol, 2006","date":"2023-05-24T10:17:09.982Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP04078r001","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1014"}],"statement":[{"text":"The N-terminal 30 amino acids (residues 49–80) of our construct are not visible in the electron density maps of all three structures, indicating that they are disordered in the crystals.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"2CKQ"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met154Val","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-12T17:56:17.314Z"}},{"start":50,"end":85,"reference_id":"17007874","reference_source":"pmid","reference_html":"Elucidation of human choline kinase crystal structures in complex with the products ADP or phosphocholine. <i> Malito E, Sekulic N, Too WC, Konrad M, Lavie A. </i> J Mol Biol, 2006","date":"2023-05-24T10:50:42.426Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2CKO"},{"db":"PDB","id":"2CKP"}],"region_id":"DP04078r002","statement":[{"text":"The N-terminal 30 amino acids (residues 49–80) of our construct are not visible in the electron density maps of all three structures, indicating that they are disordered in the crystals.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met154Val","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:439196","statements":[{"type":"Curator statement","text":"Small molecule related to PDB 2CKO."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022","statements":[{"type":"Curator statement","text":"Small molecule related to PDB 2CKP."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-12T17:56:59.395Z"}},{"start":131,"end":140,"reference_id":"17007874","reference_source":"pmid","reference_html":"Elucidation of human choline kinase crystal structures in complex with the products ADP or phosphocholine. <i> Malito E, Sekulic N, Too WC, Konrad M, Lavie A. </i> J Mol Biol, 2006","date":"2023-05-24T10:51:53.831Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2CKO"}],"region_id":"DP04078r003","statement":[{"text":"PDB structure 2CKO shows that this region is ordered, compared to PDB 2CKP (hCKADP) which presents the lack of traceable electron density described in evidence DP04078r004.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met154Val","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:439196"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-12T17:58:42.694Z"}},{"start":131,"end":140,"reference_id":"17007874","reference_source":"pmid","reference_html":"Elucidation of human choline kinase crystal structures in complex with the products ADP or phosphocholine. <i> Malito E, Sekulic N, Too WC, Konrad M, Lavie A. </i> J Mol Biol, 2006","date":"2023-05-24T09:33:07.782Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2CKP"}],"region_id":"DP04078r004","statement":[{"text":"Note that a lack of traceable electron density in some regions of the hCKADP structure prevented us from modelling ~25% of the residues in comparison to the apo-structure. Specifically, residues 131–139, 149–175 (missing insertion in all pdbs), 262–268, 314–326 in chain A; 87–91, 118–121, 131–141, 148–176, 256–277, 317–323, 388–389, 424–440 in chain B.","type":"Methods"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met154Val","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-12T17:57:30.110Z"}},{"start":131,"end":140,"reference_id":"17007874","reference_source":"pmid","reference_html":"Elucidation of human choline kinase crystal structures in complex with the products ADP or phosphocholine. <i> Malito E, Sekulic N, Too WC, Konrad M, Lavie A. </i> J Mol Biol, 2006","date":"2023-05-24T10:15:32.627Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2CKP"},{"db":"PDB","id":"2CKO"}],"region_id":"DP04078r005","statement":[{"text":"Note that a lack of traceable electron density in some regions of the hCKADP structure prevented us from modelling ~25% of the residues in comparison to the apo-structure. Specifically, residues 131–139, 149–175 (missing insertion in all pdbs), 262–268, 314–326 in chain A; 87–91, 118–121, 131–141, 148–176, 256–277, 317–323, 388–389, 424–440 in chain B.","type":"Results"},{"text":"The region gets disordered when the protein interacts with ADP.","type":"Curator statement"}],"states_connection":[{"source":"DP04078r003","target":"DP04078r004"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met154Val","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:439196","statements":[{"type":"Curator statement","text":"Small molecule related to PDB 2CKO."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022","statements":[{"type":"Curator statement","text":"Small molecule related to PDB 2CKP."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-12T17:59:35.670Z"}},{"start":296,"end":308,"reference_id":"17007874","reference_source":"pmid","reference_html":"Elucidation of human choline kinase crystal structures in complex with the products ADP or phosphocholine. <i> Malito E, Sekulic N, Too WC, Konrad M, Lavie A. </i> J Mol Biol, 2006","date":"2023-06-20T08:24:11.770Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2CKP"}],"region_id":"DP04078r006","statement":[{"text":"Note that a lack of traceable electron density in some regions of the hCKADP structure prevented us from modelling ~25% of the residues in comparison to the apo-structure. Specifically, residues 131–139, 149–175 (missing insertion in all pdbs), 262–268, 314–326 in chain A; 87–91, 118–121, 131–141, 148–176, 256–277, 317–323, 388–389, 424–440 in chain B.","type":"Methods"},{"text":"The region 314-326 mentioned by the author corresponds to residues 296-308 of this isoform.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met154Val","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T09:44:03.993Z"}},{"start":296,"end":308,"reference_id":"17007874","reference_source":"pmid","reference_html":"Elucidation of human choline kinase crystal structures in complex with the products ADP or phosphocholine. <i> Malito E, Sekulic N, Too WC, Konrad M, Lavie A. </i> J Mol Biol, 2006","date":"2023-06-20T08:24:44.072Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2CKO"}],"region_id":"DP04078r007","statement":[{"text":"PDB structure 2CKO shows that this region is ordered, compared to PDB 2CKP (hCKADP) which presents the lack of traceable electron density described in evidence DP04078r006.","type":"Curator statement"},{"text":"The region 314-326 mentioned by the author corresponds to residues 296-308 of this isoform.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met154Val","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:439196"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T09:44:02.868Z"}},{"start":296,"end":308,"reference_id":"17007874","reference_source":"pmid","reference_html":"Elucidation of human choline kinase crystal structures in complex with the products ADP or phosphocholine. <i> Malito E, Sekulic N, Too WC, Konrad M, Lavie A. </i> J Mol Biol, 2006","date":"2023-06-20T08:23:35.506Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2CKO"},{"db":"PDB","id":"2CKP"}],"region_id":"DP04078r008","statement":[{"text":"Note that a lack of traceable electron density in some regions of the hCKADP structure prevented us from modelling ~25% of the residues in comparison to the apo-structure. Specifically, residues 131–139, 149–175 (missing insertion in all pdbs), 262–268, 314–326 in chain A; 87–91, 118–121, 131–141, 148–176, 256–277, 317–323, 388–389, 424–440 in chain B.","type":"Results"},{"text":"The region gets disordered when the protein interacts with ADP.","type":"Curator statement"},{"text":"The region 314-326 mentioned by the author corresponds to residues 296-308 of this isoform.","type":"Curator statement"}],"states_connection":[{"source":"DP04078r007","target":"DP04078r006"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met154Val","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:439196","statements":[{"type":"Curator statement","text":"Small molecule related to PDB 2CKO."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6022","statements":[{"type":"Curator statement","text":"Small molecule related to PDB 2CKP."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T09:44:08.102Z"}}],"regions_counter":8,"released":"2023_06","sequence":"MKTKFCTGGEAEPSPLGLLLSCGSGSAAPAPGVGQQRDAASDLESKQLGGQQPPLALPPPPPLPLPLPLPQPPPPQPPADEQPEPRTRRRAYLWCKEFLPGAWRGLREDEFHISVIRGGLSNMLFQCSLPDTTATLGDEPRKVLLRLYGAILQMGAEAMVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKYLKEVLRIKFTEESRIKKLHKLLSYNLPLELENLRSLLESTPSPVVFCHNDCQEGNILLLEGRENSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRANIRKYPTKKQQLHFISSYLPAFQNDFENLSTEEKSIIKEEMLLEVNRFALASHFLWGLWSIVQAKISSIEFGYMDYAQARFDAYFHQKRKLGV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"disorder_content":0.13439635535307518,"disprot_consensus":{"full":[{"start":50,"end":85,"type":"D"},{"start":131,"end":140,"type":"T"},{"start":296,"end":308,"type":"T"}],"Structural state":[{"start":50,"end":85,"type":"D"},{"start":131,"end":140,"type":"D"},{"start":296,"end":308,"type":"D"}],"Structural transition":[{"start":131,"end":140,"type":"T"},{"start":296,"end":308,"type":"T"}]}},{"disprot_id":"DP04080","acc":"Q9ULK4","creator":"mgoncalves","date":"2023-05-10T12:11:46.888Z","features":{"pfam":[{"id":"PF11573","name":"Mediator complex subunit 23","start":2,"end":1307}],"gene3D":[]},"genes":[{"name":{"value":"MED23"},"synonyms":[{"value":"ARC130"},{"value":"CRSP3"},{"value":"DRIP130"},{"value":"KIAA1216"},{"value":"SUR2"}]}],"length":1368,"name":"Mediator of RNA polymerase II transcription subunit 23","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1335,"end":1368,"reference_id":"30140054","reference_source":"pmid","reference_html":"Crystal structure of human Mediator subunit MED23. <i> Monté D, Clantin B, Dewitte F, Lens Z, Rucktooa P, Pardon E, Steyaert J, Verger A, Villeret V. </i> Nat Commun, 2018","date":"2023-05-10T15:27:07.865Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6H02"}],"region_id":"DP04080r001","statement":[{"text":"The final model is complete, with the exception of the last 30 residues, which have no visible electron density.","type":"Methods"}],"sample":[{"term_id":"IDPO:00491","term_name":"interacting antibody","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ABCD","id":"AL608"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-23T14:39:26.685Z"}}],"regions_counter":1,"released":"2023_06","sequence":"METQLQSIFEEVVKTEVIEEAFPGMFMDTPEDEKTKLISCLGAFRQFWGGLSQESHEQCIQWIVKFIHGQHSPKRISFLYDCLAMAVETGLLPPRLVCESLINSDTLEWERTQLWALTFKLVRKIIGGVDYKGVRDLLKVILEKILTIPNTVSSAVVQQLLAAREVIAYILERNACLLPAYFAVTEIRKLYPEGKLPHWLLGNLVSDFVDTFRPTARINSICGRCSLLPVVNNSGAICNSWKLDPATLRFPLKGLLPYDKDLFEPQTALLRYVLEQPYSRDMVCNMLGLNKQHKQRCPVLEDQLVDLVVYAMERSETEEKFDDGGTSQLLWQHLSSQLIFFVLFQFASFPHMVLSLHQKLAGRGLIKGRDHLMWVLLQFISGSIQKNALADFLPVMKLFDLLYPEKEYIPVPDINKPQSTHAFAMTCIWIHLNRKAQNDNSKLQIPIPHSLRLHHEFLQQSLRNKSLQMNDYKIALLCNAYSTNSECFTLPMGALVETIYGNGIMRIPLPGTNCMASGSITPLPMNLLDSLTVHAKMSLIHSIATRVIKLAHAKSSVALAPALVETYSRLLVYMEIESLGIKGFISQLLPTVFKSHAWGILHTLLEMFSYRMHHIQPHYRVQLLSHLHTLAAVAQTNQNQLHLCVESTALRLITALGSSEVQPQFTRFLSDPKTVLSAESEELNRALILTLARATHVTDFFTGSDSIQGTWCKDILQTIMSFTPHNWASHTLSCFPGPLQAFFKQNNVPQESRFNLKKNVEEEYRKWKSMSNENDIITHFSMQGSPPLFLCLLWKMLLETDHINQIGYRVLERIGARALVAHVRTFADFLVYEFSTSAGGQQLNKCIEILNDMVWKYNIVTLDRLILCLAMRSHEGNEAQVCYFIIQLLLLKPNDFRNRVSDFVKENSPEHWLQNDWHTKHMNYHKKYPEKLYFEGLAEQVDPPVQIQSPYLPIYFGNVCLRFLPVFDIVIHRFLELLPVSKSLETLLDHLGGLYKFHDRPVTYLYNTLHYYEMHLRDRAFLKRKLVHAIIGSLKDNRPQGWCLSDTYLKCAMNAREENPWVPDDTYYCRLIGRLVDTMAGKSPGPFPNCDWRFNEFPNPAAHALHVTCVELMALAVSGKEVGNALLNVVLKSQPLVPRENITAWMNAIGLIITALPEPYWIVLHDRIVSVISSPSLTSETEWVGYPFRLFDFTACHQSYSEMSCSYTLALAHAVWHHSSIGQLSLIPKFLTEVLLPIVKTEFQLLYVYHLVGPFLQRFQQERTRCMIEIGVAFYDMLLNVDQCSTHLNYMDPICDFLYHMKYMFTGDSVKEQVEKIICNLKPALKLRLRFITHISKMEPAAVPPQAMNSGSPAPQSNQVPVSLPVTQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.031432748538011694,"disorder_content":0.024853801169590642,"disprot_consensus":{"full":[{"start":1335,"end":1368,"type":"D"}],"Structural state":[{"start":1335,"end":1368,"type":"D"}]}},{"disprot_id":"DP04081","acc":"Q9UIW2","creator":"mgoncalves","date":"2023-05-10T13:52:05.610Z","features":{"pfam":[{"id":"PF01403","name":"Sema domain","start":312,"end":492},{"id":"PF01437","name":"Plexin repeat","start":514,"end":556},{"id":"PF01437","name":"Plexin repeat","start":809,"end":861},{"id":"PF01833","name":"IPT/TIG domain","start":864,"end":957},{"id":"PF01833","name":"IPT/TIG domain","start":961,"end":1044},{"id":"PF01833","name":"IPT/TIG domain","start":1048,"end":1110},{"id":"PF01833","name":"IPT/TIG domain","start":1166,"end":1232},{"id":"PF08337","name":"Plexin cytoplasmic RasGAP domain","start":1318,"end":1487},{"id":"PF08337","name":"Plexin cytoplasmic RasGAP domain","start":1601,"end":1866},{"id":"PF17960","name":"TIG domain","start":569,"end":659},{"id":"PF18020","name":"TIG domain found in plexin","start":714,"end":807},{"id":"PF20170","name":"Plexin cytoplasmic RhoGTPase-binding domain","start":1488,"end":1600},{"id":"PF24479","name":"Plexin A/B, PSI domain","start":667,"end":693}],"gene3D":[]},"genes":[{"name":{"value":"PLXNA1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:9099","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:9099"}}]},"synonyms":[{"value":"NOV"},{"value":"PLXN1"}]}],"length":1896,"name":"Plexin-A1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":25,"end":38,"reference_id":"36156831","reference_source":"pmid","reference_html":"Hybrid in vitro/in silico analysis of low-affinity protein-protein interactions that regulate signal transduction by Sema6D. <i> Tanaka T, Ekimoto T, Nagatomo M, Neyazaki M, Shimoji E, Yamane T, Kanagawa S, Oi R, Mihara E, Takagi J, Akashi S, Ikeguchi M, Nogi T. </i> Protein Sci, 2022","date":"2023-05-10T14:06:26.641Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7Y4P"}],"region_id":"DP04081r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"}],"statement":[{"text":"Missing residues (residues 25–38 in Plexin-A1, and residues 19–22, 47–54, 479–483, 545–553, and 569–570 in Sema6D) were added using MODELLER.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-23T14:43:13.557Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MPLPPRSLQVLLLLLLLLLLLPGMWAEAGLPRAGGGSQPPFRTFSASDWGLTHLVVHEQTGEVYVGAVNRIYKLSGNLTLLRAHVTGPVEDNEKCYPPPSVQSCPHGLGSTDNVNKLLLLDYAANRLLACGSASQGICQFLRLDDLFKLGEPHHRKEHYLSSVQEAGSMAGVLIAGPPGQGQAKLFVGTPIDGKSEYFPTLSSRRLMANEEDADMFGFVYQDEFVSSQLKIPSDTLSKFPAFDIYYVYSFRSEQFVYYLTLQLDTQLTSPDAAGEHFFTSKIVRLCVDDPKFYSYVEFPIGCEQAGVEYRLVQDAYLSRPGRALAHQLGLAEDEDVLFTVFAQGQKNRVKPPKESALCLFTLRAIKEKIKERIQSCYRGEGKLSLPWLLNKELGCINSPLQIDDDFCGQDFNQPLGGTVTIEGTPLFVDKDDGLTAVAAYDYRGRTVVFAGTRSGRIRKILVDLSNPGGRPALAYESVVAQEGSPILRDLVLSPNHQYLYAMTEKQVTRVPVESCVQYTSCELCLGSRDPHCGWCVLHSICSRRDACERADEPQRFAADLLQCVQLTVQPRNVSVTMSQVPLVLQAWNVPDLSAGVNCSFEDFTESESVLEDGRIHCRSPSAREVAPITRGQGDQRVVKLYLKSKETGKKFASVDFVFYNCSVHQSCLSCVNGSFPCHWCKYRHVCTHNVADCAFLEGRVNVSEDCPQILPSTQIYVPVGVVKPITLAARNLPQPQSGQRGYECLFHIPGSPARVTALRFNSSSLQCQNSSYSYEGNDVSDLPVNLSVVWNGNFVIDNPQNIQAHLYKCPALRESCGLCLKADPRFECGWCVAERRCSLRHHCAADTPASWMHARHGSSRCTDPKILKLSPETGPRQGGTRLTITGENLGLRFEDVRLGVRVGKVLCSPVESEYISAEQIVCEIGDASSVRAHDALVEVCVRDCSPHYRALSPKRFTFVTPTFYRVSPSRGPLSGGTWIGIEGSHLNAGSDVAVSVGGRPCSFSWRNSREIRCLTPPGQSPGSAPIIININRAQLTNPEVKYNYTEDPTILRIDPEWSINSGGTLLTVTGTNLATVREPRIRAKYGGIERENGCLVYNDTTMVCRAPSVANPVRSPPELGERPDELGFVMDNVRSLLVLNSTSFLYYPDPVLEPLSPTGLLELKPSSPLILKGRNLLPPAPGNSRLNYTVLIGSTPCTLTVSETQLLCEAPNLTGQHKVTVRAGGFEFSPGTLQVYSDSLLTLPAIVGIGGGGGLLLLVIVAVLIAYKRKSRDADRTLKRLQLQMDNLESRVALECKEAFAELQTDIHELTNDLDGAGIPFLDYRTYAMRVLFPGIEDHPVLKEMEVQANVEKSLTLFGQLLTKKHFLLTFIRTLEAQRSFSMRDRGNVASLIMTALQGEMEYATGVLKQLLSDLIEKNLESKNHPKLLLRRTESVAEKMLTNWFTFLLYKFLKECAGEPLFMLYCAIKQQMEKGPIDAITGEARYSLSEDKLIRQQIDYKTLTLNCVNPENENAPEVPVKGLDCDTVTQAKEKLLDAAYKGVPYSQRPKAADMDLEWRQGRMARIILQDEDVTTKIDNDWKRLNTLAHYQVTDGSSVALVPKQTSAYNISNSSTFTKSLSRYESMLRTASSPDSLRSRTPMITPDLESGTKLWHLVKNHDHLDQREGDRGSKMVSEIYLTRLLATKGTLQKFVDDLFETIFSTAHRGSALPLAIKYMFDFLDEQADKHQIHDADVRHTWKSNCLPLRFWVNVIKNPQFVFDIHKNSITDACLSVVAQTFMDSCSTSEHKLGKDSPSNKLLYAKDIPNYKSWVERYYADIAKMPAISDQDMSAYLAEQSRLHLSQFNSMSALHEIYSYITKYKDEILAALEKDEQARRQRLRSKLEQVVDTMALSS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Extracellular matrix proteins"],"alphafold_very_low_content":0.05959915611814346,"disorder_content":0.007383966244725738,"disprot_consensus":{"full":[{"start":25,"end":38,"type":"D"}],"Structural state":[{"start":25,"end":38,"type":"D"}]}},{"disprot_id":"DP04082","acc":"Q9NXG6","creator":"mgoncalves","date":"2023-05-11T08:41:35.799Z","features":{"pfam":[{"id":"PF13499","name":"EF-hand domain pair","start":192,"end":251},{"id":"PF13640","name":"2OG-Fe(II) oxygenase superfamily","start":314,"end":458}],"gene3D":[]},"genes":[{"name":{"value":"P4HTM"},"synonyms":[{"value":"PH4"}]}],"length":502,"name":"Transmembrane prolyl 4-hydroxylase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":88,"end":106,"reference_id":"33334883","reference_source":"pmid","reference_html":"Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains. <i> Myllykoski M, Sutinen A, Koski MK, Kallio JP, Raasakka A, Myllyharju J, Wierenga RK, Koivunen P. </i> J Biol Chem, 2021","date":"2023-05-24T10:58:28.561Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"Including the 6xHis tag, there are 25 disordered residues in the N-terminus that are not visible in the electron density."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala99Val","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"6TP5"}],"region_id":"DP04082r001","sequence_construct":"HHHHHHDESSDPGPQHRVQGPGPEPTLGPLTRLEGIKVGHERKVQLVTDRDHFIRTLSLKPLLFEIPGFLTDEECRLIIHLAQMKGLQRSQILPTEEYEEAMSTMQVSQLDLFRLLDQNRDGHLQLREVLAQTRLGNGWWMTPESIQEMYAAIKADPDGDGVLSLQEFSNMDLRDFHKYMRSHKAESSELVRNSHHTWLYQGEGAHHIMRAIRQRVLRLTRLSPEIVELSEPLQVVRYGEGGHYHAHVDSGPVYPETICSHTKLVANESVPFETSCRYMTVLFYLNNVTGGGETVFPVADNRTYDEMSLIQDDVDLRDTRRHCDKGNLRVKPQQGTAVFWYNYLPDGQGWVGDVDDYSLHGGCLVTRGTKWIANNWINVDPSRARQALFQQEMARLAREGGTDSQPEWALDRAYRDARVEL","statement":[{"text":"The first visible P4H-TM residues are Thr107 and Leu108 in chains A and B, respectively. Including the 6xHis tag, there are 25 disordered residues in the N-terminus that are not visible in the electron density.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:3080614"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:27284"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6386"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:750"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-12T19:50:44.956Z"}},{"start":482,"end":502,"reference_id":"33334883","reference_source":"pmid","reference_html":"Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains. <i> Myllykoski M, Sutinen A, Koski MK, Kallio JP, Raasakka A, Myllyharju J, Wierenga RK, Koivunen P. </i> J Biol Chem, 2021","date":"2023-05-24T11:06:07.442Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala99Val","start":null,"end":null,"position":null},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"Including the 6xHis tag, there are 25 disordered residues in the N-terminus that are not visible in the electron density."}]}],"cross_refs":[{"db":"PDB","id":"6TP5"}],"region_id":"DP04082r002","statement":[{"text":"The last 21 residues of P4H-TM are not visible in the electron density.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:3080614"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:27284"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:6386"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:750"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-12T19:50:46.820Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MAAAAVTGQRPETAAAEEASRPQWAPPDHCQAQAAAGLGDGEDAPVRPLCKPRGICSRAYFLVLMVFVHLYLGNVLALLLFVHYSNGDESSDPGPQHRAQGPGPEPTLGPLTRLEGIKVGHERKVQLVTDRDHFIRTLSLKPLLFEIPGFLTDEECRLIIHLAQMKGLQRSQILPTEEYEEAMSTMQVSQLDLFRLLDQNRDGHLQLREVLAQTRLGNGWWMTPESIQEMYAAIKADPDGDGVLSLQEFSNMDLRDFHKYMRSHKAESSELVRNSHHTWLYQGEGAHHIMRAIRQRVLRLTRLSPEIVELSEPLQVVRYGEGGHYHAHVDSGPVYPETICSHTKLVANESVPFETSCRYMTVLFYLNNVTGGGETVFPVADNRTYDEMSLIQDDVDLRDTRRHCDKGNLRVKPQQGTAVFWYNYLPDGQGWVGDVDDYSLHGGCLVTRGTKWIANNWINVDPSRARQALFQQEMARLAREGGTDSQPEWALDRAYRDARVEL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.19123505976095617,"disorder_content":0.0796812749003984,"disprot_consensus":{"full":[{"start":88,"end":106,"type":"D"},{"start":482,"end":502,"type":"D"}],"Structural state":[{"start":88,"end":106,"type":"D"},{"start":482,"end":502,"type":"D"}]}},{"disprot_id":"DP04083","acc":"Q9BPU6","creator":"mgoncalves","date":"2023-05-11T09:30:33.914Z","features":{"pfam":[{"id":"PF01979","name":"Amidohydrolase family","start":57,"end":445}],"gene3D":[]},"genes":[{"name":{"value":"DPYSL5"},"synonyms":[{"value":"CRMP5"},{"value":"ULIP6"}]}],"length":564,"name":"Dihydropyrimidinase-related protein 5","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":493,"end":564,"reference_id":"23373749","reference_source":"pmid","reference_html":"Insights into the oligomerization of CRMPs: crystal structure of human collapsin response mediator protein 5. <i> Ponnusamy R, Lohkamp B. </i> J Neurochem, 2013","date":"2023-05-11T09:53:29.393Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4B90"}],"region_id":"DP04083r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:174"}],"statement":[{"text":"For WT CRMP-5, residues 1–6, 492–564, and 1–7, 493–564 of chains A and B, respectively, as well as all 23 residues added to the N-termini by the cloning procedure could not be traced.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-23T15:14:42.174Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MLANSASVRILIKGGKVVNDDCTHEADVYIENGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVDDFYHGTKAALVGGTTMIIGHVLPDKETSLVDAYEKCRGLADPKVCCDYALHVGITWWAPKVKAEMETLVREKGVNSFQMFMTYKDLYMLRDSELYQVLHACKDIGAIARVHAENGELVAEGAKEALDLGITGPEGIEISRPEELEAEATHRVITIANRTHCPIYLVNVSSISAGDVIAAAKMQGKVVLAETTTAHATLTGLHYYHQDWSHAAAYVTVPPLRLDTNTSTYLMSLLANDTLNIVASDHRPFTTKQKAMGKEDFTKIPHGVSGVQDRMSVIWERGVVGGKMDENRFVAVTSSNAAKLLNLYPRKGRIIPGADADVVVWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENGVFMCAEGTGKFCPLRSFPDTVYKKLVQREKTLKVRGVDRTPYLGDVAVVVHPGKKEMGTPLADTPTRPVTRHGGMRDLHESSFSLSGSQIDDHVPKRASARILAPPGGRSSGIW","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.07801418439716312,"disorder_content":0.1276595744680851,"disprot_consensus":{"full":[{"start":493,"end":564,"type":"D"}],"Structural state":[{"start":493,"end":564,"type":"D"}]}},{"disprot_id":"DP04084","acc":"P37093","creator":"ldobson","date":"2023-05-14T15:39:50.816Z","features":{"pfam":[{"id":"PF00437","name":"Type II/IV secretion system protein","start":116,"end":498},{"id":"PF22341","name":"GSPII protein E, N1E domain","start":16,"end":80}],"gene3D":[]},"genes":[{"name":{"value":"epsE"},"olnNames":[{"value":"VC_2732"}]}],"length":503,"name":"Type II secretion system ATPase E","ncbi_taxon_id":243277,"organism":"Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)","regions":[{"start":1,"end":13,"reference_id":"15843017","reference_source":"pmid","reference_html":"The X-ray structure of the type II secretion system complex formed by the N-terminal domain of EpsE and the cytoplasmic domain of EpsL of Vibrio cholerae. <i> Abendroth J, Murphy P, Sandkvist M, Bagdasarian M, Hol WG. </i> J Mol Biol, 2005","date":"2023-05-14T15:41:49.511Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2BH1"}],"region_id":"DP04084r001","statement":[{"text":"Both the N-terminal 13 residues and the C-terminal 15 residues of N1-EpsE had no representative electron density and most are likely disordered in the crystal.","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P45782"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-29T18:02:37.676Z"}},{"start":82,"end":96,"reference_id":"15843017","reference_source":"pmid","reference_html":"The X-ray structure of the type II secretion system complex formed by the N-terminal domain of EpsE and the cytoplasmic domain of EpsL of Vibrio cholerae. <i> Abendroth J, Murphy P, Sandkvist M, Bagdasarian M, Hol WG. </i> J Mol Biol, 2005","date":"2023-05-14T15:43:39.952Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2BH1"}],"region_id":"DP04084r002","statement":[{"text":"Both the N-terminal 13 residues and the C-terminal 15 residues of N1-EpsE had no representative electron density and most are likely disordered in the crystal.","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P45782"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-29T18:02:40.567Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MTEMVISPAERQSIRRLPFSFANRFKLVLDWNEDFSQASIYYLAPLSMEALVETKRVVKHAFQLIELSQAEFESKLTQVYQRDSSEARQLMEDIGADSDDFFSLAEELPQNEDLLESEDDAPIIKLINAMLGEAIKEGASDIHIETFEKTLSIRFRVDGVLREVLAPSRKLSSLLVSRVKVMAKLDIAEKRVPQDGRISLRIGGRAVDVRVSTMPSSHGERVVMRLLDKNATRLDLHSLGMTAHNHDNFRRLIKRPHGIILVTGPTGSGKSTTLYAGLQELNSSERNILTVEDPIEFDIDGIGQTQVNPRVDMTFARGLRAILRQDPDVVMVGEIRDLETAQIAVQASLTGHLVMSTLHTNTAVGAVTRLRDMGIEPFLISSSLLGVLAQRLVRTLCPDCKEPYEADKEQRKLFDSKKKEPLILYRATGCPKCNHKGYRGRTGIHELLLVDDALQELIHSEAGEQAMEKHIRATTPSIRDDGLDKVRQGITSLEEVMRVTKES","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Vibrionales","Vibrionaceae","Vibrio"],"alphafold_very_low_content":0.07554671968190854,"disorder_content":0.055666003976143144,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"D"},{"start":82,"end":96,"type":"D"}],"Structural state":[{"start":1,"end":13,"type":"D"},{"start":82,"end":96,"type":"D"}]}},{"disprot_id":"DP04086","acc":"P54577","creator":"ldobson","date":"2023-05-14T16:01:47.274Z","features":{"pfam":[{"id":"PF00579","name":"tRNA synthetases class I (W and Y)","start":32,"end":321},{"id":"PF01588","name":"Putative tRNA binding domain","start":370,"end":465}],"gene3D":[]},"genes":[{"name":{"value":"YARS1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:12840","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:12840"}}]},"synonyms":[{"value":"YARS","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16429158","url":"http://www.ncbi.nlm.nih.gov/pubmed/16429158","alternativeUrl":"https://europepmc.org/abstract/MED/16429158"}}]}]}],"length":528,"name":"Tyrosine--tRNA ligase, cytoplasmic","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":343,"end":364,"reference_id":"12427973","reference_source":"pmid","reference_html":"Crystal structure of a human aminoacyl-tRNA synthetase cytokine. <i> Yang XL, Skene RJ, McRee DE, Schimmel P. </i> Proc Natl Acad Sci U S A, 2002","date":"2023-05-14T16:26:19.308Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1N3L"}],"region_id":"DP04086r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"}],"statement":[{"text":"The three N-terminal amino acids and 22 residues from Asp-343 to Ile-364 were disordered.","type":"Results"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"sequence_construct":"MGDAPSPEEKLHLITRNLQEVLGEEKLKEILKERELKIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKAPWELLELRVSYYENVIKAMLESIGVPLEKLKFIKGTDYQLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVDAQFGGIDQRKIFTFAEKYLPALGYSKRVHLMNPMVPGLTGSKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSVEVALNKLLDPIREKFNTPALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVILEHHHHHH","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-29T17:55:00.434Z"}},{"start":343,"end":364,"reference_id":"12427973","reference_source":"pmid","reference_html":"Crystal structure of a human aminoacyl-tRNA synthetase cytokine. <i> Yang XL, Skene RJ, McRee DE, Schimmel P. </i> Proc Natl Acad Sci U S A, 2002","date":"2023-06-08T08:20:22.073Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"1N3L"}],"region_id":"DP04086r002","statement":[{"text":"This disordered segment is the linker that joins the 169-aa, EMAP II-like C domain of native TyrRS to the body of the enzyme (mini-TyrRS).","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"sequence_construct":"MGDAPSPEEKLHLITRNLQEVLGEEKLKEILKERELKIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKAPWELLELRVSYYENVIKAMLESIGVPLEKLKFIKGTDYQLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVDAQFGGIDQRKIFTFAEKYLPALGYSKRVHLMNPMVPGLTGSKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSVEVALNKLLDPIREKFNTPALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVILEHHHHHH\n","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T15:54:19.747Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MGDAPSPEEKLHLITRNLQEVLGEEKLKEILKERELKIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKAPWELLELRVSYYENVIKAMLESIGVPLEKLKFIKGTDYQLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVDAQFGGIDQRKIFTFAEKYLPALGYSKRVHLMNPMVPGLTGSKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSVEVALNKLLDPIREKFNTPALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRQVEPLDPPAGSAPGEHVFVKGYEKGQPDEELKPKKKVFEKLQADFKISEECIAQWKQTNFMTKLGSISCKSLKGGNIS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","RNA-binding proteins"],"alphafold_very_low_content":0.030303030303030304,"disorder_content":0.041666666666666664,"disprot_consensus":{"full":[{"start":343,"end":364,"type":"D"}],"Structural state":[{"start":343,"end":364,"type":"D"}],"Disorder function":[{"start":343,"end":364,"type":"F"}]}},{"disprot_id":"DP04087","acc":"P07206","creator":"ldobson","date":"2023-05-15T12:06:05.168Z","features":{"pfam":[{"id":"PF02922","name":"Carbohydrate-binding module 48 (Isoamylase N-terminal domain)","start":304,"end":388},{"id":"PF03714","name":"Bacterial pullanase-associated domain","start":76,"end":168},{"id":"PF11852","name":"Alpha-1,6-glucosidases, pullulanase-type, C-terminal","start":913,"end":1073},{"id":"PF17967","name":"Pullulanase N2 domain","start":184,"end":293},{"id":"PF18494","name":"Pullulanase Ins domain","start":489,"end":562}],"gene3D":[]},"genes":[{"name":{"value":"pulA"}}],"length":1090,"name":"Pullulanase","ncbi_taxon_id":573,"organism":"Klebsiella pneumoniae","regions":[{"start":21,"end":38,"reference_id":"26688215","reference_source":"pmid","reference_html":"Structural Basis of Pullulanase Membrane Binding and Secretion Revealed by X-Ray Crystallography, Molecular Dynamics and Biochemical Analysis. <i> East A, Mechaly AE, Huysmans GHM, Bernarde C, Tello-Manigne D, Nadeau N, Pugsley AP, Buschiazzo A, Alzari PM, Bond PJ, Francetic O. </i> Structure, 2016","date":"2023-05-15T12:36:12.702Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2YOC"}],"region_id":"DP04087r001","statement":[{"text":"The 19-residue N-terminal tether or linker, which connects the lipid anchor with the structured parts of the protein, was completely disordered and invisible in the structure, although its presence in purified PulANA was confirmed by Edman degradation.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":241,"end":241,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":342,"end":342,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":368,"end":368,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":418,"end":418,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":431,"end":431,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":466,"end":466,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":594,"end":594,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":604,"end":604,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":608,"end":608,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":660,"end":660,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":686,"end":686,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":795,"end":795,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":804,"end":804,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":848,"end":848,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":865,"end":865,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":874,"end":874,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":921,"end":921,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":940,"end":940,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":952,"end":952,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":978,"end":978,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":997,"end":997,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1003,"end":1003,"position":"Specific residue"},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys20Met","start":null,"end":null,"position":null}],"sequence_construct":"MDNGSSSSSSGNPDTPDNQDVVVRLPDVAVPGEAVTAVENQAVIHLVDIAGITSSSAADYSSKNLYLWNNETCDALSAPVADWNDVSTTPSGSDKYGPYWVIPLNKESGCINVIVRDGTDKLIDSDLRVAFGDFTDRTVSVIAGNSAVYDSRADAFRAAFGVALAEAHWVDKNTLLWPGGQDKPIVRLYYSHSSKVAADGEGKFTDRYLKLTPTTVSQQVSMRFPHLSSYAAFKLPDNANVDELLQGETVAIAAAEDGILISATQVQTAGVLDDAYAEAAEALSYGAQLADGGVTFRVWAPTAQQVDVVVYSADKKVIGSHPMTRDSASGAWSWQGGSDLKGAFYRYAMTVYHPQSRKVEQYEVTDPYAHSLSTNSEYSQVVDLNDSALKPDGWDNLTMPHAQKTKADLAKMTIHESHIRDLSAWDQTVPAELRGKYLALTAGDSNMVQHLKTLSASGVTHVELLPVFDLATVNEFSDKVADIQQPFSRLCEVNSAVKSSEFAGYCDSGSTVEEVLNQLKQSDSQDNPQVQALNTLVAQTDSYNWGYDPFHYTVPEGSYATDPEGTTRIKEFRTMIQAIKQDLGMNVIMDVVYNHTNAAGPTDRTSVLDKIVPWYYQRLNETTGSVESATCCSDSAPEHRMFAKLIADSLAVWTTDYKIDGFRFDLMGYHPKAQILSAWERIKALNPDIYFFGEGWDSNQSDRFEIASQINLKGTGIGTFSDRLRDSVRGGGPFDSGDALRQNQGIGSGAGVLPNELASLSDDQVRHLADLTRLGMAGNLADFVMIDKDGAAKKGSEIDYNGAPGGYAADPTEVVNYVSKHDNQTLWDMISYKASQEADLATRVRMQAVSLATVMLGQGIAFDQQGSELLRSKSFTRDSYDSGDWFNRVDYSLQDNNYNVGMPRISDDGSNYEVITRVKEMVATPGEAELKQMTAFYQELTELRKSSPLFTLGDGSAVMKRVDFRNTGSDQQAGLLVMTVDDGMKAGASLDSRLDGLVVAINAAPESRTLNEFAGETLQLSAIQQTAGENSLANGVQIAADGTVTLPAWSVAVLELPQGEAQGAGLPVSSYYHHHHHH","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-29T17:48:32.407Z"}},{"start":21,"end":38,"reference_id":"26688215","reference_source":"pmid","reference_html":"Structural Basis of Pullulanase Membrane Binding and Secretion Revealed by X-Ray Crystallography, Molecular Dynamics and Biochemical Analysis. <i> East A, Mechaly AE, Huysmans GHM, Bernarde C, Tello-Manigne D, Nadeau N, Pugsley AP, Buschiazzo A, Alzari PM, Bond PJ, Francetic O. </i> Structure, 2016","date":"2023-05-15T12:33:51.536Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2YOC"}],"region_id":"DP04087r002","statement":[{"text":"The 19-residue N-terminal tether or linker, which connects the lipid anchor with the structured parts of the protein, was completely disordered and invisible in the structure, although its presence in purified PulANA was confirmed by Edman degradation.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1117"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys20Met","start":null,"end":null,"position":null},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":241,"end":241,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":342,"end":342,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":368,"end":368,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":418,"end":418,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":431,"end":431,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":466,"end":466,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":594,"end":594,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":604,"end":604,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":608,"end":608,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":660,"end":660,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":686,"end":686,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":795,"end":795,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":804,"end":804,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":848,"end":848,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":865,"end":865,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":874,"end":874,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":921,"end":921,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":940,"end":940,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":952,"end":952,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":978,"end":978,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":997,"end":997,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1003,"end":1003,"position":"Specific residue"}],"sequence_construct":"MDNGSSSSSSGNPDTPDNQDVVVRLPDVAVPGEAVTAVENQAVIHLVDIAGITSSSAADYSSKNLYLWNNETCDALSAPVADWNDVSTTPSGSDKYGPYWVIPLNKESGCINVIVRDGTDKLIDSDLRVAFGDFTDRTVSVIAGNSAVYDSRADAFRAAFGVALAEAHWVDKNTLLWPGGQDKPIVRLYYSHSSKVAADGEGKFTDRYLKLTPTTVSQQVSMRFPHLSSYAAFKLPDNANVDELLQGETVAIAAAEDGILISATQVQTAGVLDDAYAEAAEALSYGAQLADGGVTFRVWAPTAQQVDVVVYSADKKVIGSHPMTRDSASGAWSWQGGSDLKGAFYRYAMTVYHPQSRKVEQYEVTDPYAHSLSTNSEYSQVVDLNDSALKPDGWDNLTMPHAQKTKADLAKMTIHESHIRDLSAWDQTVPAELRGKYLALTAGDSNMVQHLKTLSASGVTHVELLPVFDLATVNEFSDKVADIQQPFSRLCEVNSAVKSSEFAGYCDSGSTVEEVLNQLKQSDSQDNPQVQALNTLVAQTDSYNWGYDPFHYTVPEGSYATDPEGTTRIKEFRTMIQAIKQDLGMNVIMDVVYNHTNAAGPTDRTSVLDKIVPWYYQRLNETTGSVESATCCSDSAPEHRMFAKLIADSLAVWTTDYKIDGFRFDLMGYHPKAQILSAWERIKALNPDIYFFGEGWDSNQSDRFEIASQINLKGTGIGTFSDRLRDSVRGGGPFDSGDALRQNQGIGSGAGVLPNELASLSDDQVRHLADLTRLGMAGNLADFVMIDKDGAAKKGSEIDYNGAPGGYAADPTEVVNYVSKHDNQTLWDMISYKASQEADLATRVRMQAVSLATVMLGQGIAFDQQGSELLRSKSFTRDSYDSGDWFNRVDYSLQDNNYNVGMPRISDDGSNYEVITRVKEMVATPGEAELKQMTAFYQELTELRKSSPLFTLGDGSAVMKRVDFRNTGSDQQAGLLVMTVDDGMKAGASLDSRLDGLVVAINAAPESRTLNEFAGETLQLSAIQQTAGENSLANGVQIAADGTVTLPAWSVAVLELPQGEAQGAGLPVSSYYHHHHHH","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-29T17:48:32.707Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MLRYTRNALVLGSLVLLSGCDNGSSSSSSGNPDTPDNQDVVVRLPDVAVPGEAVTAVENQAVIHLVDIAGITSSSAADYSSKNLYLWNNETCDALSAPVADWNDVSTTPSGSDKYGPYWVIPLNKESGCINVIVRDGTDKLIDSDLRVAFGDFTDRTVSVIAGNSAVYDSRADAFRAAFGVALAEAHWVDKNTLLWPGGQDKPIVRLYYSHSSKVAADGEGKFTDRYLKLTPTTVSQQVSMRFPHLSSYAAFKLPDNANVDELLQGETVAIAAAEDGILISATQVQTAGVLDDAYAEAAEALSYGAQLADGGVTFRVWAPTAQQVDVVVYSADKKVIGSHPMTRDSASGAWSWQGGSDLKGAFYRYAMTVYHPQSRKVEQYEVTDPYAHSLSTNSEYSQVVDLNDSALKPDGWDNLTMPHAQKTKADLAKMTIHESHIRDLSAWDQTVPAELRGKYLALTAGDSNMVQHLKTLSASGVTHVELLPVFDLATVNEFSDKVADIQQPFSRLCEVNSAVKSSEFAGYCDSGSTVEEVLNQLKQSDSQDNPQVQALNTLVAQTDSYNWGYDPFHYTVPEGSYATDPEGTTRIKEFRTMIQAIKQDLGMNVIMDVVYNHTNAAGPTDRTSVLDKIVPWYYQRLNETTGSVESATCCSDSAPEHRMFAKLIADSLAVWTTDYKIDGFRFDLMGYHPKAQILSAWERIKALNPDIYFFGEGWDSNQSDRFEIASQINLKGTGIGTFSDRLRDSVRGGGPFDSGDALRQNQGIGSGAGVLPNELASLSDDQVRHLADLTRLGMAGNLADFVMIDKDGAAKKGSEIDYNGAPGGYAADPTEVVNYVSKHDNQTLWDMISYKASQEADLATRVRMQAVSLATVMLGQGIAFDQQGSELLRSKSFTRDSYDSGDWFNRVDYSLQDNNYNVGMPRISDDGSNYEVITRVKEMVATPGEAELKQMTAFYQELTELRKSSPLFTLGDGSAVMKRVDFRNTGSDQQAGLLVMTVDDGMKAGASLDSRLDGLVVAINAAPESRTLNEFAGETLQLSAIQQTAGENSLANGVQIAADGTVTLPAWSVAVLELPQGEAQGAGLPVSSK","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Klebsiella/Raoultella group","Klebsiella"],"alphafold_very_low_content":0.03394495412844037,"disorder_content":0.01651376146788991,"disprot_consensus":{"full":[{"start":21,"end":38,"type":"D"}],"Structural state":[{"start":21,"end":38,"type":"D"}],"Disorder function":[{"start":21,"end":38,"type":"F"}]}},{"disprot_id":"DP04088","acc":"Q7Y3F1","creator":"ldobson","date":"2023-05-15T12:44:28.006Z","features":{"pfam":[{"id":"PF05257","name":"CHAP domain","start":331,"end":438},{"id":"PF21480","name":"PlyCA, N-terminal domain","start":5,"end":189}],"gene3D":[]},"genes":[{"name":{"value":"orf11","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAP42310.2","url":"https://www.ebi.ac.uk/ena/browser/view/AAP42310.2"}}]}}],"length":465,"name":"PlyCA","ncbi_taxon_id":230871,"organism":"Fischettivirus C1","regions":[{"start":289,"end":308,"reference_id":"22807482","reference_source":"pmid","reference_html":"X-ray crystal structure of the streptococcal specific phage lysin PlyC. <i> McGowan S, Buckle AM, Mitchell MS, Hoopes JT, Gallagher DT, Heselpoth RD, Shen Y, Reboul CF, Law RH, Fischetti VA, Whisstock JC, Nelson DC. </i> Proc Natl Acad Sci U S A, 2012","date":"2023-05-15T12:46:44.953Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4F88"}],"region_id":"DP04088r001","statement":[{"text":"Linker regions between the central helical bundle and the two terminal domains showed partial disorder in electron density, consistent with limited proteolysis data that demonstrated that both domains could be readily dissociated from the holoenzyme.","type":"Results"},{"text":"The Cα atoms of the model show the N-terminal residues 1–205 in light blue, the disordered linker 1 (residues 206–227) in red, the helical structure (residues 226–288) that docks PlyCA to PlyCB in yellow, the second disordered linker 2 (residues 289–308) in a dashed red line, and the CHAP domain (residues 309–465) in green.","type":"Figure"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q7Y3F3"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-29T17:39:54.700Z"}},{"start":289,"end":308,"reference_id":"22807482","reference_source":"pmid","reference_html":"X-ray crystal structure of the streptococcal specific phage lysin PlyC. <i> McGowan S, Buckle AM, Mitchell MS, Hoopes JT, Gallagher DT, Heselpoth RD, Shen Y, Reboul CF, Law RH, Fischetti VA, Whisstock JC, Nelson DC. </i> Proc Natl Acad Sci U S A, 2012","date":"2023-06-08T08:17:10.689Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4F88"}],"region_id":"DP04088r002","statement":[{"text":"Linker regions between the central helical bundle and the two terminal domains showed partial disorder in electron density, consistent with limited proteolysis data that demonstrated that both domains could be readily dissociated from the holoenzyme.","type":"Results"},{"text":"The Cα atoms of the model show the N-terminal residues 1–205 in light blue, the disordered linker 1 (residues 206–227) in red, the helical structure (residues 226–288) that docks PlyCA to PlyCB in yellow, the second disordered linker 2 (residues 289–308) in a dashed red line, and the CHAP domain (residues 309–465) in green.","type":"Figure"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q7Y3F3"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T15:55:35.000Z"}}],"regions_counter":2,"released":"2023_12","sequence":"MSKKYTQQQYEKYLAQPANNTFGLSPQQVADWFMGQAGARPVINSYGVNASNLVSTYIPKMQEYGVSYTLFLMYTVFEGGGAGNWINHYMYDTGSNGLECLEHDLQYIHGVWETYFPPALSAPECYPATEDNAGALDRFYQSLPGRTWGDVMIPSTMAGNAWVWAYNYCVNNQGAAPLVYFGNPYDSQIDSLLAMGADPFTGGSITGDGKNPSVGTGNATVSASSEANREKLKKALTDLFNNNLEHLSGEFYGNQVLNAMKYGTILKCDLTDDGLNAILQLIADVNLQTNPNPDKPTVQSPGQNDLGSGSDRVAANLANAQAQVGKYIGDGQCYAWVGWWSARVCGYSISYSTGDPMLPLIGDGMNAHSIHLGWDWSIANTGIVNYPVGTVGRKEDLRVGAIWCATAFSGAPFYTGQYGHTGIIESWSDTTVTVLEQNILGSPVIRSTYDLNTFLSTLTGLITFK","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Uroviricota","Caudoviricetes","Rountreeviridae","Fischettivirus"],"dataset":["Viral proteins"],"disorder_content":0.043010752688172046,"disprot_consensus":{"full":[{"start":289,"end":308,"type":"D"}],"Structural state":[{"start":289,"end":308,"type":"D"}],"Disorder function":[{"start":289,"end":308,"type":"F"}]}},{"disprot_id":"DP04089","acc":"P0AGD7","creator":"ldobson","date":"2023-05-15T12:48:40.429Z","features":{"pfam":[{"id":"PF00448","name":"SRP54-type protein, GTPase domain","start":100,"end":296},{"id":"PF02881","name":"SRP54-type protein, helical bundle domain","start":5,"end":82},{"id":"PF02978","name":"Signal peptide binding domain","start":310,"end":445}],"gene3D":[]},"genes":[{"name":{"value":"ffh","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00306","url":"https://hamap.expasy.org/unirule/MF_00306"}}]},"olnNames":[{"value":"b2610"},{"value":"JW5414"}]}],"length":453,"name":"Signal recognition particle protein","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":341,"end":368,"reference_id":"11243816","reference_source":"pmid","reference_html":"Structural and energetic analysis of RNA recognition by a universally conserved protein from the signal recognition particle. <i> Batey RT, Sagar MB, Doudna JA. </i> J Mol Biol, 2001","date":"2023-06-08T08:16:23.543Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1HQ1"}],"region_id":"DP04089r001","statement":[{"text":"Despite the presence of RNA, however, a 33-amino acid residue segment (338–370) within the M-domain was disordered within the original co-crystal structure (Batey et al., 2000).","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:813"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS000080DD2B_32630"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T15:56:00.828Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MFDNLTDRLSRTLRNISGRGRLTEDNVKDTLREVRMALLEADVALPVVREFINRVKEKAVGHEVNKSLTPGQEFVKIVRNELVAAMGEENQTLNLAAQPPAVVLMAGLQGAGKTTSVGKLGKFLREKHKKKVLVVSADVYRPAAIKQLETLAEQVGVDFFPSDVGQKPVDIVNAALKEAKLKFYDVLLVDTAGRLHVDEAMMDEIKQVHASINPVETLFVVDAMTGQDAANTAKAFNEALPLTGVVLTKVDGDARGGAALSIRHITGKPIKFLGVGEKTEALEPFHPDRIASRILGMGDVLSLIEDIESKVDRAQAEKLASKLKKGDGFDLNDFLEQLRQMKNMGGMASLMGKLPGMGQIPDNVKSQMDDKVLVRMEAIINSMTMKERAKPEIIKGSRKRRIAAGCGMQVQDVNRLLKQFDDMQRMMKKMKKGGMAKMMRSMKGMMPPGFPGR","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"alphafold_very_low_content":0.017660044150110375,"dataset":["RNA-binding proteins"],"disorder_content":0.06181015452538632,"disprot_consensus":{"full":[{"start":341,"end":368,"type":"D"}],"Structural state":[{"start":341,"end":368,"type":"D"}]}},{"disprot_id":"DP04090","acc":"P26949","creator":"ldobson","date":"2023-05-15T12:59:53.385Z","features":{"pfam":[{"id":"PF00577","name":"Outer membrane usher protein","start":186,"end":740},{"id":"PF13953","name":"PapC C-terminal domain","start":750,"end":815},{"id":"PF13954","name":"PapC N-terminal domain","start":25,"end":169}],"gene3D":[]},"genes":[{"name":{"value":"caf1A"},"olnNames":[{"value":"YPMT1.83"},{"value":"Y1099"},{"value":"YP_pMT083"}]}],"length":833,"name":"F1 capsule-anchoring protein","ncbi_taxon_id":632,"organism":"Yersinia pestis","regions":[{"start":23,"end":39,"reference_id":"22981947","reference_source":"pmid","reference_html":"Allosteric mechanism controls traffic in the chaperone/usher pathway. <i> Di Yu X, Dubnovitsky A, Pudney AF, Macintyre S, Knight SD, Zavialov AV. </i> Structure, 2012","date":"2023-05-15T13:02:44.336Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4B0E"}],"region_id":"DP04090r001","statement":[{"text":"The asymmetric unit contains four Caf1AN molecules\nwith very similar structures. None of the molecules have electron\ndensity for the N- and C-terminal parts of Caf1AN before Asp18\nand after Phe124, respectively, suggesting that these sequences\nare not structured in Caf1AN.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-29T17:21:22.269Z"}},{"start":23,"end":39,"reference_id":"22981947","reference_source":"pmid","reference_html":"Allosteric mechanism controls traffic in the chaperone/usher pathway. <i> Di Yu X, Dubnovitsky A, Pudney AF, Macintyre S, Knight SD, Zavialov AV. </i> Structure, 2012","date":"2023-05-15T13:06:56.502Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4B0E"},{"db":"PDB","id":"4B0M"}],"region_id":"DP04090r002","statement":[{"text":"The structures of Caf1M:Caf1 and the core of Caf1AN remain\nessentially unchanged after binding. The largest conformational\nchange occurs in the N-terminal 1-17 amino acid sequence of\nCaf1AN, which becomes ordered in Caf1AN:Caf1M:Caf1 (Figure\n2A; Figure S1E).","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P26948"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P26926"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-29T17:21:21.735Z"}},{"start":145,"end":158,"reference_id":"22981947","reference_source":"pmid","reference_html":"Allosteric mechanism controls traffic in the chaperone/usher pathway. <i> Di Yu X, Dubnovitsky A, Pudney AF, Macintyre S, Knight SD, Zavialov AV. </i> Structure, 2012","date":"2023-05-15T13:07:36.393Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4B0E"}],"region_id":"DP04090r003","statement":[{"text":"The asymmetric unit contains four Caf1AN molecules\nwith very similar structures. None of the molecules have electron\ndensity for the N- and C-terminal parts of Caf1AN before Asp18\nand after Phe124, respectively, suggesting that these sequences\nare not structured in Caf1AN.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-29T17:21:22.936Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MRYSKLFLCAGLTLATLPCWGRAYTFDSTMLDTNSGESIDVSLFNQGLQLPGNYFVNVFVNGRKVDSGNIDFRLEKHNGKELLWPCLSSLQLTKYGIDIDKYPDLIKSGTEQCVDLLAIPHSDVQFYFNQQKLSLIVPPQALLPRFDGIMPMQLWDDGIPALFMNYNTNMQTRKFREGGKSLDSYYAQLQPGLNIGAWRFRSSTSWWKQQGWQRSYIYAERGLNTIKSRLTLGETYSDSSIFDSIPIKGIKIASDESMVPYYQWNFAPVVRGIARTQARVEVLRDGYTVSNELVPSGPFELANLPLGGGSGELKVIIHESDGTKQVFTVPYDTPAVALRKGYFEYSMMGGEYRPANDLTQTSYVGALGMKYGLPRNLTLYGGLQGSQNYHAAALGIGAMLGDFGAISTDVTQADSQKNKQKKESGQRWRVRYNKYLQSGTSLNIASEEYATEGFNKLADTLNTYCKPNTRNDCRFDYAKPKNKVQFNLSQSIPGSGTLNFSGYRKNYWRDSRSTTSFSVGYNHFFRNGMSLTLNLSKTQNINKYGEKTSELLSNIWLSFPLSRWLGNNSINSNYQMTSDSHGNTTHEVGVYGEAFDRQLYWDVRERFNEKGRKYTSNALNLNYRGTYGEISGNYSYDQTQSQLGIGVNGNMVITQYGITAGQKTGDTIALVQAPDISGASVGYWPGMKTDFRGYTNYGYLTPYRENKVEINPVTLPNDAEITNNIVSVIPTKGAVVLAKFNARIGGRLFLHLKRSDNKPVPFGSIVTIEGQSSSSGIVGDNSGVYLTGLPKKSKILVKWGRDKNQSCSSNVVLPEKTDISGAYRLSTTCILNN","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"],"alphafold_very_low_content":0.008403361344537815,"disorder_content":0.03721488595438175,"disprot_consensus":{"full":[{"start":23,"end":39,"type":"T"},{"start":145,"end":158,"type":"D"}],"Structural state":[{"start":23,"end":39,"type":"D"},{"start":145,"end":158,"type":"D"}],"Structural transition":[{"start":23,"end":39,"type":"T"}]}},{"disprot_id":"DP04091","acc":"P26926","creator":"ldobson","date":"2023-05-15T13:10:38.587Z","features":{"pfam":[{"id":"PF00345","name":"Pili and flagellar-assembly chaperone, PapD N-terminal domain","start":36,"end":170},{"id":"PF02753","name":"Pili assembly chaperone PapD, C-terminal domain","start":178,"end":250}],"gene3D":[]},"genes":[{"name":{"value":"caf1M"},"olnNames":[{"value":"YPMT1.82"},{"value":"Y1098"},{"value":"YP_pMT084"}]}],"length":258,"name":"Chaperone protein caf1M","ncbi_taxon_id":632,"organism":"Yersinia pestis","regions":[{"start":130,"end":145,"reference_id":"22981947","reference_source":"pmid","reference_html":"Allosteric mechanism controls traffic in the chaperone/usher pathway. <i> Di Yu X, Dubnovitsky A, Pudney AF, Macintyre S, Knight SD, Zavialov AV. </i> Structure, 2012","date":"2023-05-15T13:15:34.796Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4B0M"}],"region_id":"DP04091r001","statement":[{"text":"The disordered part of the F1G1 loop in Caf1M (not observed in crystal structures) is indicated with a dashed line.","type":"Figure"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P26948"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P26949"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-29T17:14:03.052Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MILNRLSTLGIITFGMLSFAANSAQPDIKFASKEYGVTIGESRIIYPLDAAGVMVSVKNTQDYPVLIQSRIYDENKEKESEDPFVVTPPLFRLDAKQQNSLRIAQAGGVFPRDKESLKWLCVKGIPPKDEDIWVDDATNKQKFNPDKDVGVFVQFAINNCIKLLVRPNELKGTPIQFAENLSWKVDGGKLIAENPSPFYMNIGELTFGGKSIPSHYIPPKSTWAFDLPKGLAGARNVSWRIINDQGGLDRLYSKNVTL","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"],"alphafold_very_low_content":0.10077519379844961,"disorder_content":0.06201550387596899,"disprot_consensus":{"full":[{"start":130,"end":145,"type":"D"}],"Structural state":[{"start":130,"end":145,"type":"D"}]}},{"disprot_id":"DP04092","acc":"P02710","creator":"vnugnes","date":"2023-05-15T15:02:00.142Z","features":{"pfam":[{"id":"PF02931","name":"Neurotransmitter-gated ion-channel ligand binding domain","start":28,"end":233},{"id":"PF02932","name":"Neurotransmitter-gated ion-channel transmembrane region","start":242,"end":450}],"gene3D":[]},"genes":[{"name":{"value":"CHRNA1"}}],"length":461,"name":"Acetylcholine receptor subunit alpha","ncbi_taxon_id":7787,"organism":"Tetronarce californica","regions":[{"start":205,"end":222,"reference_id":"12133834","reference_source":"pmid","reference_html":"NMR-based binding screen and structural analysis of the complex formed between alpha-cobratoxin and an 18-mer cognate peptide derived from the alpha 1 subunit of the nicotinic acetylcholine receptor from Torpedo californica. <i> Zeng H, Hawrot E. </i> J Biol Chem, 2002","date":"2023-05-15T15:05:51.234Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04092r001","statement":[{"text":"From the HSQC titration, it is clear that the free peptide (Fig. 2 A) is largely unstructured.","type":"Results"}]},{"start":205,"end":222,"reference_id":"12133834","reference_source":"pmid","reference_html":"NMR-based binding screen and structural analysis of the complex formed between alpha-cobratoxin and an 18-mer cognate peptide derived from the alpha 1 subunit of the nicotinic acetylcholine receptor from Torpedo californica. <i> Zeng H, Hawrot E. </i> J Biol Chem, 2002","date":"2023-05-15T15:06:45.941Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1LXG"},{"db":"PDB","id":"1LXH"}],"region_id":"DP04092r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P01391"}],"statement":[{"text":"Upon binding to Cbtx, the chemical shift positions of the HN resonances for the bound peptide are altered due to complex formation but remain fixed in position and do not vary as a function of the Cbtx concentration (Fig. 2, B–D).","type":"Results"}]},{"start":205,"end":222,"reference_id":"12133834","reference_source":"pmid","reference_html":"NMR-based binding screen and structural analysis of the complex formed between alpha-cobratoxin and an 18-mer cognate peptide derived from the alpha 1 subunit of the nicotinic acetylcholine receptor from Torpedo californica. <i> Zeng H, Hawrot E. </i> J Biol Chem, 2002","date":"2023-05-15T15:07:08.394Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1LXG"},{"db":"PDB","id":"1LXH"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P01391","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04092r003","statement":[{"text":"Upon binding to Cbtx, the chemical shift positions of the HN resonances for the bound peptide are altered due to complex formation but remain fixed in position and do not vary as a function of the Cbtx concentration (Fig. 2, B–D).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":356,"end":393,"reference_id":"32275860","reference_source":"pmid","reference_html":"Structure of the Native Muscle-type Nicotinic Receptor and Inhibition by Snake Venom Toxins. <i> Rahman MM, Teng J, Worrell BT, Noviello CM, Lee M, Karlin A, Stowell MHB, Hibbs RE. </i> Neuron, 2020","date":"2023-11-24T13:40:52.562Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"20928"},{"db":"PDB","id":"6UWZ"}],"region_id":"DP04092r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P60615"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02714"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02712"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02718"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:356"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:10908846"}],"statement":[{"text":"The PDB of the cryo-EM structure of Torpedo acetylcholine receptor in complex with alpha-bungarotoxin shows this region lacks electron density, indicating it is disordered. ","type":"Curator statement"}]}],"regions_counter":4,"released":"2024_06","sequence":"MILCSYWHVGLVLLLFSCCGLVLGSEHETRLVANLLENYNKVIRPVEHHTHFVDITVGLQLIQLISVDEVNQIVETNVRLRQQWIDVRLRWNPADYGGIKKIRLPSDDVWLPDLVLYNNADGDFAIVHMTKLLLDYTGKIMWTPPAIFKSYCEIIVTHFPFDQQNCTMKLGIWTYDGTKVSISPESDRPDLSTFMESGEWVMKDYRGWKHWVYYTCCPDTPYLDITYHFIMQRIPLYFVVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMIFVISSIIITVVVINTHHRSPSTHTMPQWVRKIFIDTIPNVMFFSTMKRASKEKQENKIFADDIDISDISGKQVTGEVIFQTPLIKNPDVKSAIEGVKYIAEHMKSDEESSNAAEEWKYVAMVIDHILLCVFMLICIIGTVSVFAGRLIELSQEG","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Chondrichthyes","Elasmobranchii","Batoidea","Torpediniformes","Torpedinidae","Tetronarce"],"alphafold_very_low_content":0.05856832971800434,"disorder_content":0.12147505422993492,"disprot_consensus":{"full":[{"start":205,"end":222,"type":"T"},{"start":356,"end":393,"type":"D"}],"Structural state":[{"start":205,"end":222,"type":"D"},{"start":356,"end":393,"type":"D"}],"Structural transition":[{"start":205,"end":222,"type":"T"}],"Molecular function":[{"start":205,"end":222,"type":"F"}]}},{"disprot_id":"DP04093","acc":"P30531","creator":"mgoncalves","date":"2023-05-17T07:17:59.678Z","features":{"pfam":[{"id":"PF00209","name":"Sodium:neurotransmitter symporter family","start":44,"end":558}],"gene3D":[]},"genes":[{"name":{"value":"SLC6A1"},"synonyms":[{"value":"GABATR"},{"value":"GABT1"},{"value":"GAT1"}]}],"length":599,"name":"Sodium- and chloride-dependent GABA transporter 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":46,"reference_id":"35676483","reference_source":"pmid","reference_html":"Structural basis of GABA reuptake inhibition. <i> Motiwala Z, Aduri NG, Shaye H, Han GW, Lam JH, Katritch V, Cherezov V, Gati C. </i> Nature, 2022","date":"2023-05-17T07:20:34.849Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7SK2"}],"region_id":"DP04093r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:60648"}],"statement":[{"text":"Although a full-length construct of human GAT1 was used for structure determination, the N terminus (residues 1–46) and C terminus (residues 578–599) are disordered and were not observed in our reconstruction.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-23T15:19:19.635Z"}},{"start":578,"end":599,"reference_id":"35676483","reference_source":"pmid","reference_html":"Structural basis of GABA reuptake inhibition. <i> Motiwala Z, Aduri NG, Shaye H, Han GW, Lam JH, Katritch V, Cherezov V, Gati C. </i> Nature, 2022","date":"2023-06-21T09:27:12.863Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7SK2"}],"region_id":"DP04093r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:60648"}],"statement":[{"text":"Although a full-length construct of human GAT1 was used for structure determination, the N terminus (residues 1–46) and C terminus (residues 578–599) are disordered and were not observed in our reconstruction.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T11:56:34.893Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MATNGSKVADGQISTEVSEAPVANDKPKTLVVKVQKKAADLPDRDTWKGRFDFLMSCVGYAIGLGNVWRFPYLCGKNGGGAFLIPYFLTLIFAGVPLFLLECSLGQYTSIGGLGVWKLAPMFKGVGLAAAVLSFWLNIYYIVIISWAIYYLYNSFTTTLPWKQCDNPWNTDRCFSNYSMVNTTNMTSAVVEFWERNMHQMTDGLDKPGQIRWPLAITLAIAWILVYFCIWKGVGWTGKVVYFSATYPYIMLIILFFRGVTLPGAKEGILFYITPNFRKLSDSEVWLDAATQIFFSYGLGLGSLIALGSYNSFHNNVYRDSIIVCCINSCTSMFAGFVIFSIVGFMAHVTKRSIADVAASGPGLAFLAYPEAVTQLPISPLWAILFFSMLLMLGIDSQFCTVEGFITALVDEYPRLLRNRRELFIAAVCIISYLIGLSNITQGGIYVFKLFDYYSASGMSLLFLVFFECVSISWFYGVNRFYDNIQEMVGSRPCIWWKLCWSFFTPIIVAGVFIFSAVQMTPLTMGNYVFPKWGQGVGWLMALSSMVLIPGYMAYMFLTLKGSLKQRIQVMVQPSEDIVRPENGPEQPQAGSSTSKEAYI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.09015025041736227,"disorder_content":0.11352253756260434,"disprot_consensus":{"full":[{"start":1,"end":46,"type":"D"},{"start":578,"end":599,"type":"D"}],"Structural state":[{"start":1,"end":46,"type":"D"},{"start":578,"end":599,"type":"D"}]}},{"disprot_id":"DP04094","acc":"P35219","creator":"mgoncalves","date":"2023-05-17T07:28:44.077Z","features":{"pfam":[{"id":"PF00194","name":"Eukaryotic-type carbonic anhydrase","start":36,"end":288}],"gene3D":[]},"genes":[{"name":{"value":"CA8"},"synonyms":[{"value":"CALS"}]}],"length":290,"name":"Carbonic anhydrase-related protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":22,"reference_id":"19360879","reference_source":"pmid","reference_html":"Crystal structure of human carbonic anhydrase-related protein VIII reveals the basis for catalytic silencing. <i> Picaud SS, Muniz JR, Kramm A, Pilka ES, Kochan G, Oppermann U, Yue WW. </i> Proteins, 2009","date":"2023-05-24T11:30:50.531Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2W2J"}],"region_id":"DP04094r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"}],"statement":[{"text":"The first 23 residues were not observed in the electron density map and are presumably disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T12:16:10.391Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MADLSFIEDTVAFPEKEEDEEEEEEGVEWGYEEGVEWGLVFPDANGEYQSPINLNSREARYDPSLLDVRLSPNYVVCRDCEVTNDGHTIQVILKSKSVLSGGPLPQGHEFELYEVRFHWGRENQRGSEHTVNFKAFPMELHLIHWNSTLFGSIDEAVGKPHGIAIIALFVQIGKEHVGLKAVTEILQDIQYKGKSKTIPCFNPNTLLPDPLLRDYWVYEGSLTIPPCSEGVTWILFRYPLTISQLQIEEFRRLRTHVKGAELVEGCDGILGDNFRPTQPLSDRVIRAAFQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.08620689655172414,"disorder_content":0.07586206896551724,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"}],"Structural state":[{"start":1,"end":22,"type":"D"}]}},{"disprot_id":"DP04095","acc":"P49758","creator":"mgoncalves","date":"2023-05-17T09:56:23.795Z","features":{"pfam":[{"id":"PF00610","name":"Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP)","start":43,"end":113},{"id":"PF00615","name":"Regulator of G protein signaling domain","start":336,"end":450},{"id":"PF00631","name":"GGL domain","start":256,"end":317},{"id":"PF18148","name":"Regulator of G-protein signalling DHEX domain","start":116,"end":217}],"gene3D":[]},"genes":[{"name":{"value":"RGS6"}}],"length":472,"name":"Regulator of G-protein signaling 6","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":453,"end":470,"reference_id":"18434541","reference_source":"pmid","reference_html":"Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits. <i> Soundararajan M, Willard FS, Kimple AJ, Turnbull AP, Ball LJ, Schoch GA, Gileadi C, Fedorov OY, Dowler EF, Higman VA, Hutsell SQ, Sundström M, Doyle DA, Siderovski DP. </i> Proc Natl Acad Sci U S A, 2008","date":"2023-05-17T10:01:43.980Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2ES0"}],"region_id":"DP04095r001","statement":[{"text":"The PDB shows that the protein lacks electron density in this region, indicating it is disordered at the C-terminal.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-23T15:45:25.010Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MAQGSGDQRAVGVADPEESSPNMIVYCKIEDIITKMQDDKTGGVPIRTVKSFLSKIPSVVTGTDIVQWLMKNLSIEDPVEAIHLGSLIAAQGYIFPISDHVLTMKDDGTFYRFQAPYFWPSNCWEPENTDYAIYLCKRTMQNKARLELADYEAENLARLQRAFARKWEFIFMQAEAQVKIDRKKDKTERKILDSQERAFWDVHRPVPGCVNTTEMDIRKCRRLKNPQKVKKSVYGVTEESQAQSPVHVLSQPIRKTTKEDIRKQITFLNAQIDRHCLKMSKVAESLIAYTEQYVEYDPLITPAEPSNPWISDDVALWDIEMSKEPSQQRVKRWGFSFDEILKDQVGRDQFLRFLESEFSSENLRFWLAVQDLKKQPLQDVAKRVEEIWQEFLAPGAPSAINLDSHSYEITSQNVKDGGRYTFEDAQEHIYKLMKSDSYARFLRSNAYQDLLLAKKKGKSLAGKRLTGLMQSS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.1038135593220339,"disorder_content":0.038135593220338986,"disprot_consensus":{"full":[{"start":453,"end":470,"type":"D"}],"Structural state":[{"start":453,"end":470,"type":"D"}]}},{"disprot_id":"DP04096","acc":"A0A0B4JDC9","creator":"zskalman","date":"2023-05-17T10:23:41.788Z","features":{"pfam":[{"id":"PF07653","name":"Variant SH3 domain","start":1319,"end":1381},{"id":"PF07653","name":"Variant SH3 domain","start":1447,"end":1505},{"id":"PF14604","name":"Variant SH3 domain","start":634,"end":676},{"id":"PF25523","name":"RIMBP2-like, immunoglobulin-like domain","start":946,"end":1044}],"gene3D":[]},"genes":[{"name":{"value":"Rbp","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ADV37318.1","url":"https://www.ebi.ac.uk/ena/browser/view/ADV37318.1"}},{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0262483","url":"http://flybase.org/reports/FBgn0262483.html"}}]},"synonyms":[{"value":"CG14867","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ADV37318.1","url":"https://www.ebi.ac.uk/ena/browser/view/ADV37318.1"}}]},{"value":"CG31302","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ADV37318.1","url":"https://www.ebi.ac.uk/ena/browser/view/ADV37318.1"}}]},{"value":"CG5143","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ADV37318.1","url":"https://www.ebi.ac.uk/ena/browser/view/ADV37318.1"}}]},{"value":"CG5152","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ADV37318.1","url":"https://www.ebi.ac.uk/ena/browser/view/ADV37318.1"}}]},{"value":"Dmel\\CG43073","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ADV37318.1","url":"https://www.ebi.ac.uk/ena/browser/view/ADV37318.1"}}]},{"value":"DRBP","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ADV37318.1","url":"https://www.ebi.ac.uk/ena/browser/view/ADV37318.1"}}]},{"value":"drbp","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ADV37318.1","url":"https://www.ebi.ac.uk/ena/browser/view/ADV37318.1"}}]},{"value":"RBP","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ADV37318.1","url":"https://www.ebi.ac.uk/ena/browser/view/ADV37318.1"}}]},{"value":"rbp","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ADV37318.1","url":"https://www.ebi.ac.uk/ena/browser/view/ADV37318.1"}}]},{"value":"rim-bp","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ADV37318.1","url":"https://www.ebi.ac.uk/ena/browser/view/ADV37318.1"}}]}],"orfNames":[{"value":"CG43073","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ADV37318.1","url":"https://www.ebi.ac.uk/ena/browser/view/ADV37318.1"}},{"code":"ECO:0000313","source":{"name":"FlyBase","id":"FBgn0262483","url":"http://flybase.org/reports/FBgn0262483.html"}}]},{"value":"Dmel_CG43073","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ADV37318.1","url":"https://www.ebi.ac.uk/ena/browser/view/ADV37318.1"}}]}]}],"length":1844,"name":"RIM-binding protein, isoform F","ncbi_taxon_id":7227,"organism":"Drosophila melanogaster","regions":[{"start":909,"end":935,"reference_id":"32369542","reference_source":"pmid","reference_html":"RIM-binding protein couples synaptic vesicle recruitment to release sites.  <i> Petzoldt AG, Götz TWB, Driller JH, Lützkendorf J, Reddy-Alla S, Matkovic-Rachid T, Liu S, Knoche E, Mertel S, Ugorets V, Lehmann M, Ramesh N, Beuschel CB, Kuropka B, Freund C, Stelzl U, Loll B, Liu F, Wahl MC, Sigrist SJ. </i> J Cell Biol, 2020","date":"2023-05-24T08:33:52.313Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6Q9M"}],"region_id":"DP04096r001","statement":[{"text":"A structural cartoon representation of molecule “B” of the three FN-III domains in RIM-BP. Linker regions are colored in sand and β-strands in red, and unmodeled linker regions are indicated by dashed lines. ","type":"Figure"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1061"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T17:16:54.284Z"}},{"start":909,"end":935,"reference_id":"32369542","reference_source":"pmid","reference_html":"RIM-binding protein couples synaptic vesicle recruitment to release sites.  <i> Petzoldt AG, Götz TWB, Driller JH, Lützkendorf J, Reddy-Alla S, Matkovic-Rachid T, Liu S, Knoche E, Mertel S, Ugorets V, Lehmann M, Ramesh N, Beuschel CB, Kuropka B, Freund C, Stelzl U, Loll B, Liu F, Wahl MC, Sigrist SJ. </i> J Cell Biol, 2020","date":"2023-05-24T08:35:46.215Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6Q9M"}],"region_id":"DP04096r002","statement":[{"text":"A structural cartoon representation of molecule “B” of the three FN-III domains in RIM-BP. Linker regions are colored in sand and β-strands in red, and unmodeled linker regions are indicated by dashed lines.","type":"Figure"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1061"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-24T17:16:53.991Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MHLCEFPSANVEEENRRPEKAAAAASKKQKHKQQKSRPRGSHSMPYESMHHHQSAAAAVAAGTTPNGMLDALSLQLRDAEMRRTEIERAHQETLAQIRNLSGSARPDAEAVENLQSRARELEKKVALENVRCEELQIELTSALKAKQASRSACSGMGSVSSGGGATIPTSASSSTVTWAPTISHQDQGSEIDIIMAKIEQDNRVLAELEQPRTSASASMSALPPSSMLSTVNSEFRTISKSELEEELNRYKRAVLGGSGGGGGGVGGGGGGVSALSSGYSSLPQSLASTLPNGGASTSLSGTSLGSHSAAAAAAAHSVSAGSGGVVGGGGQGGLSSISALVPNSISGISSSLSSHAIQSMQYGTGQTSVEKLLSGTSGITGIPPLPVNIHTMKAMPTALSQRGTIQLYNLQSTTMPLLSLNSHNLPPAGSTSYSALGAGGGTSLTHPTMANLGLLDTGTLLGSTGLSGLGVGPSVGGITGATSLYGLSGGGGGAGGLGSSYGPPFLDVASSASYPFTAAALRQASKMKMLDEIDIPLTRYNRSSPCSPIPPNNWGLDEFTDGLSVSMMHNRGGLALGALDLDTRNHGLNGASEPQVDMLDIPGKGRCCVFIARFPYDPPDVHNEFLSMPCREAEGELSLCAGDYLLVWTSGEPQGGYLDAELLDGRRGLVPASFVQRLVGDDLLEFHQAVLSTLRDAEDGSMQCDTTSLPSLPPHNPLLTHTHEDLARLSETHTDLEHDQDDISDNVPAPKHLTLERQLNKSVLIGWSPPEPVGYNLIDSYHVYVDGVLKVTVKANERTRALIEGVDSTRPHRISVRSVTQNRQTSRDAACTMIIGRDTAHLGPSAVRASHITCSSAVISWLPANSNHQHVVCVNNVEVRTVKPGMYRHTITGLAPSTQYRVTVRAKHLRAVGQHAANVGQTGGAGRPGQEEAPGAYADFRTLTKGLPDPPQEIQLEAGPQDGTILVTWQPVNRPTSTGPVTGYAVYADGKKVTDINSPTGDHALIDIGKLGVFNPRAVTIRTKSRDSQSADSAPILIPNTVRNAVARRGPNQMGMGPQLPQGPHGMTVQQQMGGMPGQPGQQGQHMMGGQQDHGQYDPNQMQQQQQQQGQPGQPGHQPDAGSGLLGGLLGGLFSKPTQNQVNQNGYQPGQPGAQRGMVPIPGRPQGPQQQQQQPYGPQGPMGGPRFRGPVPGQLNMQGQQMQGQMQGQMQGQMQGQMSGQMPGQMPGQMPGQMPGQMAGQMAGQMPGQMPGQMPGQMSGQMPGQMMGPRGPLNQQQQQQQQMQQGQMMPGQQAGQQQAQPGQPGQPGQMPGAQKKPRYFVAMFDYDPSTMSPNPDGCDEELPFQEGDTIKVFGDKDADGFYWGELRGRRGYVPHNMVSEVEDTTASMTAGGQMPGQMPGQMGQGQGVGVGGTAQVMPGQGAPQQSMRNVSRDRWGDIYANMPVKRMIALYDYDPQELSPNVDAEQVELCFKTGEIILVYGDMDEDGFYMGELDGVRGLVPSNFLADAPDQYNNQMGPGGVAGRGGLSQRGRGQGPGARGPPPPPRDNMMPGMGGRGQPGKNARPASPTLLDNTGHPAPDHQTQGMIGRVGNVGLQQQQQQQQQQQQLQQQQQYGQQQTQMGQQQQQQQQMGQPGMMGQQMGQPMGQQMGQMGQMGQMGQQQMGQQQMGQQQQPPTTQAQTGGLFSGATSLLSGATSAATGGLFGSKQPPKTDPMQPQGGVQPAQQQANAFGAQQPGMGMQQQGGMQSGMQQGMQQGMQQGMQQGMQQGMQQGMQQGMQQGMQPGMQQQQQQPQQVPPQAQAPPPGPGAGLLGGLKGIAAAAPGGDVLSKGKDLFGKFGFGFGK","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"alphafold_very_low_content":0.6496746203904555,"disorder_content":0.014642082429501085,"disprot_consensus":{"full":[{"start":909,"end":935,"type":"D"}],"Structural state":[{"start":909,"end":935,"type":"D"}],"Disorder function":[{"start":909,"end":935,"type":"F"}]}},{"disprot_id":"DP04097","acc":"P46097","creator":"zskalman","date":"2023-05-17T11:06:32.077Z","features":{"pfam":[{"id":"PF00168","name":"C2 domain","start":158,"end":263},{"id":"PF00168","name":"C2 domain","start":288,"end":393}],"gene3D":[]},"genes":[{"name":{"value":"Syt2","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:99666","url":"http://www.informatics.jax.org/marker/MGI:99666"}}]}}],"length":422,"name":"Synaptotagmin-2","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":8,"end":41,"reference_id":"23807078","reference_source":"pmid","reference_html":"Structure of dual receptor binding to botulinum neurotoxin B. <i> Berntsson RP, Peng L, Dong M, Stenmark P. </i> Nat Commun, 2013","date":"2023-05-17T11:14:10.679Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4KBB"}],"region_id":"DP04097r001","statement":[{"text":"The remainder of the fused Syt-II was disordered and not visible in the electron density. The asymmetric unit contained two BoNT/B molecules, which were virtually identical (r.m.s.d. of 0.4 Å).","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P10844"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"sequence_construct":"EGWTENQEPNVAPATTTATMPLAPVAPADNSTESTGPGESQEDMFAKLKEKFFNEINKIVLEHHHHHH","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-23T15:55:48.301Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MRNIFKRNQEPNVAPATTTATMPLAPVAPADNSTESTGPGESQEDMFAKLKEKFFNEINKIPLPPWALIAMAVVAGLLLLTCCFCICKKCCCKKKKNKKEKGKGMKNAMNMKDMKGGQDDDDAETGLTEGEGEGEEEKEPENLGKLQFSLDYDFQANQLTVGVLQAAELPALDMGGTSDPYVKVFLLPDKKKKYETKVHRKTLNPAFNETFTFKVPYQELAGKTLVMAIYDFDRFSKHDIIGEVKVPMNTVDLGQPIEEWRDLQGGEKEEPEKLGDICTSLRYVPTAGKLTVCILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTVKKKTLNPYFNESFSFEIPFEQIQKVQVVVTVLDYDKLGKNEAIGKIFVGSNATGTELRHWSDMLANPRRPIAQWHSLKPEEEVDALLGKNK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"alphafold_very_low_content":0.1990521327014218,"disorder_content":0.08056872037914692,"disprot_consensus":{"full":[{"start":8,"end":41,"type":"D"}],"Structural state":[{"start":8,"end":41,"type":"D"}]}},{"disprot_id":"DP04098","acc":"P49802","creator":"mgoncalves","date":"2023-05-17T11:43:53.758Z","features":{"pfam":[{"id":"PF00610","name":"Domain found in Dishevelled, Egl-10, and Pleckstrin (DEP)","start":40,"end":110},{"id":"PF00615","name":"Regulator of G protein signaling domain","start":334,"end":447},{"id":"PF00631","name":"GGL domain","start":254,"end":316},{"id":"PF18148","name":"Regulator of G-protein signalling DHEX domain","start":113,"end":214}],"gene3D":[]},"genes":[{"name":{"value":"RGS7"}}],"length":495,"name":"Regulator of G-protein signaling 7","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":451,"end":463,"reference_id":"18434541","reference_source":"pmid","reference_html":"Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits. <i> Soundararajan M, Willard FS, Kimple AJ, Turnbull AP, Ball LJ, Schoch GA, Gileadi C, Fedorov OY, Dowler EF, Higman VA, Hutsell SQ, Sundström M, Doyle DA, Siderovski DP. </i> Proc Natl Acad Sci U S A, 2008","date":"2023-05-24T11:43:38.973Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"2A72"}],"region_id":"DP04098r001","statement":[{"text":"The PDB shows that the protein lacks electron density in this region, indicating it is disordered at the C-terminal.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:312"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.His409Gln","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T11:58:45.808Z"}},{"start":1,"end":17,"reference_id":"34815401","reference_source":"pmid","reference_html":"Structure of the class C orphan GPCR GPR158 in complex with RGS7-Gβ5. <i> Jeong E, Kim Y, Jeong J, Cho Y. </i> Nat Commun, 2021","date":"2023-06-21T09:31:34.138Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7EWP"},{"db":"EMDB","id":"31360"},{"db":"PDB","id":"7EWR"},{"db":"EMDB","id":"31363"}],"region_id":"DP04098r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O14775"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q5T848"}],"statement":[{"text":"The electron microscopy of the class C orphan GPCR GPR158 (Q5T848) in complex with RGS7(P49802)-Gβ5(O14775) shows that this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T11:58:56.440Z"}},{"start":219,"end":255,"reference_id":"34815401","reference_source":"pmid","reference_html":"Structure of the class C orphan GPCR GPR158 in complex with RGS7-Gβ5. <i> Jeong E, Kim Y, Jeong J, Cho Y. </i> Nat Commun, 2021","date":"2023-06-21T09:37:25.933Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7EWP"},{"db":"EMDB","id":"31360"},{"db":"PDB","id":"7EWR"},{"db":"EMDB","id":"31363"}],"region_id":"DP04098r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O14775"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q5T848"}],"statement":[{"text":"In both complexes, structures of GPR158 and the four domains of RGS7 DEP (Dishevelled, Egl10, Pleckstrin), DHEX (DEP helical extension), GGL linker, and the RGS domain, and the Gβ5 subunit were clearly visible and their models fitted well into the cryo-EM maps (Supplementary Fig. 9o, p).","type":"Results"},{"text":"The electron microscopy of the class C orphan GPCR GPR158 (Q5T848) in complex with RGS7(P49802)-Gβ5(O14775) shows that this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T11:59:10.952Z"}},{"start":451,"end":495,"reference_id":"34815401","reference_source":"pmid","reference_html":"Structure of the class C orphan GPCR GPR158 in complex with RGS7-Gβ5. <i> Jeong E, Kim Y, Jeong J, Cho Y. </i> Nat Commun, 2021","date":"2023-06-21T09:31:20.011Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7EWP"},{"db":"EMDB","id":"31360"},{"db":"PDB","id":"7EWR"},{"db":"EMDB","id":"31363"}],"region_id":"DP04098r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O14775"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q5T848"}],"statement":[{"text":"The electron microscopy of the class C orphan GPCR GPR158 (Q5T848) in complex with RGS7(P49802)-Gβ5(O14775) shows that this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T11:59:25.008Z"}}],"regions_counter":5,"released":"2023_06","sequence":"MAQGNNYGQTSNGVADESPNMLVYRKMEDVIARMQDEKNGIPIRTVKSFLSKIPSVFSGSDIVQWLIKNLTIEDPVEALHLGTLMAAHGYFFPISDHVLTLKDDGTFYRFQTPYFWPSNCWEPENTDYAVYLCKRTMQNKARLELADYEAESLARLQRAFARKWEFIFMQAEAQAKVDKKRDKIERKILDSQERAFWDVHRPVPGCVNTTEVDIKKSSRMRNPHKTRKSVYGLQNDIRSHSPTHTPTPETKPPTEDELQQQIKYWQIQLDRHRLKMSKVADSLLSYTEQYLEYDPFLLPPDPSNPWLSDDTTFWELEASKEPSQQRVKRWGFGMDEALKDPVGREQFLKFLESEFSSENLRFWLAVEDLKKRPIKEVPSRVQEIWQEFLAPGAPSAINLDSKSYDKTTQNVKEPGRYTFEDAQEHIYKLMKSDSYPRFIRSSAYQELLQAKKKSGNSMDRRTSFEKFAQNVGRNIPIFPCHKNCTPTLRASTNLL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Cancer-related proteins"],"alphafold_very_low_content":0.14747474747474748,"disorder_content":0.2,"disprot_consensus":{"full":[{"start":1,"end":17,"type":"D"},{"start":219,"end":255,"type":"D"},{"start":451,"end":495,"type":"D"}],"Structural state":[{"start":1,"end":17,"type":"D"},{"start":219,"end":255,"type":"D"},{"start":451,"end":495,"type":"D"}]}},{"disprot_id":"DP04100","acc":"O00584","creator":"mgoncalves","date":"2023-05-17T12:12:53.296Z","features":{"pfam":[{"id":"PF00445","name":"Ribonuclease T2 family","start":34,"end":213}],"gene3D":[]},"genes":[{"name":{"value":"RNASET2"},"synonyms":[{"value":"RNASE6PL"}]}],"length":256,"name":"Ribonuclease T2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":215,"end":234,"reference_id":"22735700","reference_source":"pmid","reference_html":"Structure and activity of the only human RNase T2. <i> Thorn A, Steinfeld R, Ziegenbein M, Grapp M, Hsiao HH, Urlaub H, Sheldrick GM, Gärtner J, Krätzner R. </i> Nucleic Acids Res, 2012","date":"2023-05-17T12:14:28.727Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"3T0O"}],"region_id":"DP04100r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:24139"}],"statement":[{"text":"No model could be built for residues 188–192 and 214–235 as well as the terminal ends as they were disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-23T16:14:01.819Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MRPAALRGALLGCLCLALLCLGGADKRLRDNHEWKKLIMVQHWPETVCEKIQNDCRDPPDYWTIHGLWPDKSEGCNRSWPFNLEEIKDLLPEMRAYWPDVIHSFPNRSRFWKHEWEKHGTCAAQVDALNSQKKYFGRSLELYRELDLNSVLLKLGIKPSINYYQVADFKDALARVYGVIPKIQCLPPSQDEEVQTIGQIELCLTKQDQQLQNCTEPGEQPSPKQEVWLANGAAESRGLRVCEDGPVFYPPPKKTKH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","RNA-binding proteins"],"alphafold_very_low_content":0.0859375,"disorder_content":0.078125,"disprot_consensus":{"full":[{"start":215,"end":234,"type":"D"}],"Structural state":[{"start":215,"end":234,"type":"D"}]}},{"disprot_id":"DP04101","acc":"Q9H0W8","creator":"vacs","date":"2023-05-18T05:23:59.356Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"SMG9","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:25763","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:25763"}}]},"synonyms":[{"value":"C19orf61","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:25763","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:25763"}}]}]}],"length":520,"name":"Nonsense-mediated mRNA decay factor SMG9","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":11,"reference_id":"20817927","reference_source":"pmid","reference_html":"Characterization of SMG-9, an essential component of the nonsense-mediated mRNA decay SMG1C complex. <i> Fernández IS, Yamashita A, Arias-Palomo E, Bamba Y, Bartolomé RA, Canales MA, Teixidó J, Ohno S, Llorca O. </i> Nucleic Acids Res, 2011","date":"2023-05-18T05:33:11.769Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP04101r001","statement":[{"text":"Here, we have characterized SMG-9, showing that it comprises an N-terminal 180 residue intrinsically disordered region (IDR) followed by a well-folded C-terminal domain.","type":"Abstract"},{"text":"The N-terminal domain is an intrinsically disordered region (IDR) essential for the maintenance of the structural integrity of the SMG-1:SMG-8:SMG-9 complex.","type":"Introduction"},{"text":"In standard conditions, GST-NT-SMG-9 was expressed as a soluble protein, but 20–30% of the recovered protein from the GST column was non-specifically proteolysed. We identified the non-specific cleavage site by sequencing of the N-terminus and by mass spectrometry of the spontaneous truncated product. We found that the first 11 amino acids of NT-SMG-9 were removed non-specifically during purification and we therefore recloned the fragment without these residues in the GST vector to produce a more stable product. This construct, GST-NT-SMG-912–180, missing the first 11 amino acids, expressed as a soluble protein and was entirely stable after performing the purification steps described earlier (Figure 2A).","type":"Results"},{"text":"Here, we show that SMG-9 comprises an N-terminal domain with the characteristic features of the so-called intrinsically disordered regions (IDRs) and a well-folded C-terminal domain (12).","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-19T10:11:58.010Z"}},{"start":12,"end":180,"reference_id":"20817927","reference_source":"pmid","reference_html":"Characterization of SMG-9, an essential component of the nonsense-mediated mRNA decay SMG1C complex. <i> Fernández IS, Yamashita A, Arias-Palomo E, Bamba Y, Bartolomé RA, Canales MA, Teixidó J, Ohno S, Llorca O. </i> Nucleic Acids Res, 2011","date":"2023-05-18T05:38:53.605Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006200","ec_ontology":"ECO","ec_name":"circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP04101r002","statement":[{"text":"Here, we have characterized SMG-9, showing that it comprises an N-terminal 180 residue intrinsically disordered region (IDR) followed by a well-folded C-terminal domain.","type":"Abstract"},{"text":"The N-terminal domain is an intrinsically disordered region (IDR) essential for the maintenance of the structural integrity of the SMG-1:SMG-8:SMG-9 complex.","type":"Introduction"},{"text":"Whereas completely unfolded polypeptides are characterized by a well-defined CD spectrum with a minimum in the vicinity of 200 nm and an ellipticity close to zero in the vicinity of 222 nm, the CD-spectra of NT-SMG-912–180 showed a minimum at 205 nm and negative values of ellipticity from ∼235 to 200 nm (Figure 3A). This suggested the presence of certain content in secondary structure.","type":"Results"},{"text":"Here, we show that SMG-9 comprises an N-terminal domain with the characteristic features of the so-called intrinsically disordered regions (IDRs) and a well-folded C-terminal domain (12).","type":"Discussion"},{"text":"We have purified a protein comprising the N-terminal domain and several biophysical approaches (gel filtration chromatography, analytical ultracentrifugation, CD, and UV-spectroscopy) have confirmed unambiguously that this region behaves as a compact 20 kDa domain with the paradigmatic characteristics of unstructured domains as well as a limited presence of secondary structure.","type":"Discussion"},{"text":"Furthermore, the combination of NMR data and the spectroscopy studies suggests that the conformation of the NT-SMG-9 domain most likely fits into the category of intrinsically unstructured proteins termed ‘pre-molten globules’, where a limited degree of secondary structure could be localized.","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-19T09:34:07.188Z"}},{"start":12,"end":180,"reference_id":"20817927","reference_source":"pmid","reference_html":"Characterization of SMG-9, an essential component of the nonsense-mediated mRNA decay SMG1C complex. <i> Fernández IS, Yamashita A, Arias-Palomo E, Bamba Y, Bartolomé RA, Canales MA, Teixidó J, Ohno S, Llorca O. </i> Nucleic Acids Res, 2011","date":"2023-05-18T05:48:10.264Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP04101r003","statement":[{"text":"Here, we have characterized SMG-9, showing that it comprises an N-terminal 180 residue intrinsically disordered region (IDR) followed by a well-folded C-terminal domain.","type":"Abstract"},{"text":"The N-terminal domain is an intrinsically disordered region (IDR) essential for the maintenance of the structural integrity of the SMG-1:SMG-8:SMG-9 complex.","type":"Introduction"},{"text":"In addition, fluorescence spectra with an excitation wavelength of 295 nm revealed a significant increase in the fluorescence emission upon denaturation of NT-SMG-912–180 using 6 M guanidinium hydrochloride compared to native conditions (Figure 3B), strongly suggesting the presence of a certain degree of secondary structure quenching the fluorescence of the two tryptophans of NT-SMG-912–180 in the native protein.","type":"Results"},{"text":"Here, we show that SMG-9 comprises an N-terminal domain with the characteristic features of the so-called intrinsically disordered regions (IDRs) and a well-folded C-terminal domain (12).","type":"Discussion"},{"text":"We have purified a protein comprising the N-terminal domain and several biophysical approaches (gel filtration chromatography, analytical ultracentrifugation, CD, and UV-spectroscopy) have confirmed unambiguously that this region behaves as a compact 20 kDa domain with the paradigmatic characteristics of unstructured domains as well as a limited presence of secondary structure.","type":"Discussion"},{"text":"Furthermore, the combination of NMR data and the spectroscopy studies suggests that the conformation of the NT-SMG-9 domain most likely fits into the category of intrinsically unstructured proteins termed ‘pre-molten globules’, where a limited degree of secondary structure could be localized.","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-19T09:33:53.006Z"}},{"start":12,"end":180,"reference_id":"20817927","reference_source":"pmid","reference_html":"Characterization of SMG-9, an essential component of the nonsense-mediated mRNA decay SMG1C complex. <i> Fernández IS, Yamashita A, Arias-Palomo E, Bamba Y, Bartolomé RA, Canales MA, Teixidó J, Ohno S, Llorca O. </i> Nucleic Acids Res, 2011","date":"2023-05-18T05:57:33.157Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"region_id":"DP04101r004","statement":[{"text":"Here, we have characterized SMG-9, showing that it comprises an N-terminal 180 residue intrinsically disordered region (IDR) followed by a well-folded C-terminal domain.","type":"Abstract"},{"text":"The N-terminal domain is an intrinsically disordered region (IDR) essential for the maintenance of the structural integrity of the SMG-1:SMG-8:SMG-9 complex.","type":"Introduction"},{"text":"A 1H 1D spectrum of NT-SMG-912–180 showed two groups of signals, a first group of thin, well-resolved peaks (6.5–8 ppm) and a group of superposed signals accumulating between 8 and 8.5 ppm (Figure 4A). This spectrum would be compatible with an unfolded polypeptide, being the first group of sharp peaks those signals corresponding to the flexible lateral side chains and the aromatic protons whereas the N–H backbone would appear as those signals between 8 and 8.5 ppm. We also performed 1H-15N-HSQC 2D experiments after labelling NT-SMG-912–180 with 15N (Figure 4B), and we found that the majority of the signals attributable to the N-H backbone overlapped within a very narrow 1H chemical shift, ranging from 7.75 to 8.5 ppm. This is a typical spectrum for intrinsically disordered regions, where defined signals (in contrast to aggregated protein) are concentrated in a narrow range (in contrast to folded proteins). Signals of the two tryptophans present in NT-SMG-912–180 were detected at 10.25, 128.89 ppm and 10.1, 127.48 ppm, 1H, 15N chemical shifts, respectively. These chemical shifts are characteristic of solvent exposed tryptophan residues as the amino acids of a disordered protein. In addition, the HSQC spectrum showed several well-dispersed peaks typical of a folded structure, suggesting the presence of some residual structure as previously suggested by CD and fluorescence spectroscopy data.","type":"Results"},{"text":"1H-15N HSQC spectrum of 15N-labelled NT-SMG-912–180 unambiguously identified this domain as inherently unstructured due to the absence of well dispersed cross peaks.","type":"Figure"},{"text":"Here, we show that SMG-9 comprises an N-terminal domain with the characteristic features of the so-called intrinsically disordered regions (IDRs) and a well-folded C-terminal domain (12).","type":"Discussion"},{"text":"The results obtained by NMR spectroscopy represent the formal proof that the N-terminus of SMG-9 is an IDR.","type":"Discussion"},{"text":"Furthermore, the combination of NMR data and the spectroscopy studies suggests that the conformation of the NT-SMG-9 domain most likely fits into the category of intrinsically unstructured proteins termed ‘pre-molten globules’, where a limited degree of secondary structure could be localized.","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-19T08:59:03.386Z"}},{"start":2,"end":180,"reference_id":"20817927","reference_source":"pmid","reference_html":"Characterization of SMG-9, an essential component of the nonsense-mediated mRNA decay SMG1C complex. <i> Fernández IS, Yamashita A, Arias-Palomo E, Bamba Y, Bartolomé RA, Canales MA, Teixidó J, Ohno S, Llorca O. </i> Nucleic Acids Res, 2011","date":"2023-05-22T07:29:01.728Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006074","ec_ontology":"ECO","ec_name":"co-purification evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q96Q15","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04101r005","statement":[{"text":"Both domains are required for SMG-1 binding and the integrity of the SMG1C complex, whereas the C-terminus is sufficient to interact with SMG-8.","type":"Abstract"},{"text":"The N-terminal domain is an intrinsically disordered region (IDR) essential for the maintenance of the structural integrity of the SMG-1:SMG-8:SMG-9 complex.","type":"Introduction"},{"text":"Whereas each product was adequately expressed, only full-length SMG-9 co-purified with SMG-1 and SMG-8 in presence of RNaseA. These experiments indicated that both the N- and C-terminal domains of SMG-9 are necessary for the integrity of the SMG1C complex.","type":"Results"},{"text":"We demonstrate that both the N-terminal IDR and the C-terminal domain of SMG-9 are required for the integrity of the SMG1C complex. Both domains are implicated in SMG-1 binding, since removal of either domain disrupts, totally or partially, the interaction of SMG-9 with SMG-1.","type":"Discussion"},{"text":"The N-terminal disordered domain of SMG-9 participates in the recognition of SMG-1, and it would be the characteristic malleability of IDRs an adequate structural property to allow the transit of SMG-9 through these distinct macromolecular complexes.","type":"Discussion"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-19T10:12:00.861Z"}},{"start":2,"end":180,"reference_id":"20817927","reference_source":"pmid","reference_html":"Characterization of SMG-9, an essential component of the nonsense-mediated mRNA decay SMG1C complex. <i> Fernández IS, Yamashita A, Arias-Palomo E, Bamba Y, Bartolomé RA, Canales MA, Teixidó J, Ohno S, Llorca O. </i> Nucleic Acids Res, 2011","date":"2023-05-18T06:08:28.461Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"GO:0043066","term_name":"negative regulation of apoptotic process","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005802","ec_ontology":"ECO","ec_name":"cell transfection experiment evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"ec_go":"EXP","region_id":"DP04101r006","statement":[{"text":"Accordingly, we found that interfering with SMG-9 by expressing NT-SMG-9 and CT-SMG-9 truncated products, affected the normal response of cells to genotoxic stress and increased susceptibility to apoptosis (Supplementary Figure S4 and Supplementary Data), in agreement with the role described for these complexes in genome stability and apoptosis (3,13).","type":"Results"},{"text":"Cis-platin treatment led to a dose-dependent increase in cell apoptosis that was of higher extent in cells over-expressing the N-terminal or C-terminal domains of SMG-9 than in cells expressing the full length protein or than in mock cells.","type":"Results"},{"text":"Thus, SMG-1 has been shown to participate in the cellular stress response (14,16–18), and we find that the expression of truncated versions of SMG-9 increased the susceptibility to apoptosis (Supplementary Figure S4).","type":"Discussion"}],"term_comment":"This term should only be used when it is not possible to determine which phase or subtype of the apoptotic process is negatively regulated by a gene product. Whenever detailed information is available, the more granular children terms should be used.","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.\" [GOC:jl, GOC:mtg_apoptosis]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-19T10:11:58.975Z"}}],"regions_counter":6,"released":"2023_06","sequence":"MSESGHSQPGLYGIERRRRWKEPGSGGPQNLSGPGGRERDYIAPWERERRDASEETSTSVMQKTPIILSKPPAERSKQPPPPTAPAAPPAPAPLEKPIVLMKPREEGKGPVAVTGASTPEGTAPPPPAAPAPPKGEKEGQRPTQPVYQIQNRGMGTAAPAAMDPVVGQAKLLPPERMKHSIKLVDDQMNWCDSAIEYLLDQTDVLVVGVLGLQGTGKSMVMSLLSANTPEEDQRTYVFRAQSAEMKERGGNQTSGIDFFITQERIVFLDTQPILSPSILDHLINNDRKLPPEYNLPHTYVEMQSLQIAAFLFTVCHVVIVVQDWFTDLSLYRFLQTAEMVKPSTPSPSHESSSSSGSDEGTEYYPHLVFLQNKARREDFCPRKLRQMHLMIDQLMAHSHLRYKGTLSMLQCNVFPGLPPDFLDSEVNLFLVPFMDSEAESENPPRAGPGSSPLFSLLPGYRGHPSFQSLVSKLRSQVMSMARPQLSHTILTEKNWFHYAARIWDGVRKSSALAEYSRLLA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","RNA-binding proteins"],"alphafold_very_low_content":0.35384615384615387,"disorder_content":0.34615384615384615,"disprot_consensus":{"full":[{"start":1,"end":180,"type":"D"}],"Structural state":[{"start":1,"end":180,"type":"D"}],"Molecular function":[{"start":2,"end":180,"type":"F"}],"Biological process":[{"start":2,"end":180,"type":"F"}]}},{"disprot_id":"DP04102","acc":"P17993","creator":"vacs","date":"2023-05-19T09:49:23.928Z","features":{"pfam":[{"id":"PF13489","name":"Methyltransferase domain","start":57,"end":170}],"gene3D":[]},"genes":[{"name":{"value":"ubiG","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_00472","url":"https://hamap.expasy.org/unirule/MF_00472"}}]},"synonyms":[{"value":"pufX"},{"value":"yfaB"}],"olnNames":[{"value":"b2232"},{"value":"JW2226"}]}],"length":240,"name":"Ubiquinone biosynthesis O-methyltransferase","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":1,"end":15,"reference_id":"26251450","reference_source":"pmid","reference_html":"Structural and biochemical studies reveal UbiG/Coq3 as a class of novel membrane-binding proteins. <i> Zhu Y, Wu B, Zhang X, Fan X, Niu L, Li X, Wang J, Teng M. </i> Biochem J, 2015","date":"2023-05-19T09:52:32.345Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4KDC"}],"region_id":"DP04102r001","statement":[{"text":"In the final model, the N-terminal 17 residues and residues 181–189 could not be traced because of insufficient electron density.","type":"Results"},{"text":"Residues 1-15 are missing in the structure and are presumably disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-16T15:24:20.198Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MNAEKSPVNHNVDHEEIAKFEAVASRWWDLEGEFKPLHRINPLRLGYIAERAGGLFGKKVLDVGCGGGILAESMAREGATVTGLDMGFEPLQVAKLHALESGIQVDYVQETVEEHAAKHAGQYDVVTCMEMLEHVPDPQSVVRACAQLVKPGGDVFFSTLNRNGKSWLMAVVGAEYILRMVPKGTHDVKKFIKPAELLGWVDQTSLKERHITGLHYNPITNTFKLGPGVDVNYMLHTQNK","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"alphafold_very_low_content":0.03333333333333333,"disorder_content":0.0625,"disprot_consensus":{"full":[{"start":1,"end":15,"type":"D"}],"Structural state":[{"start":1,"end":15,"type":"D"}]}},{"disprot_id":"DP04103","acc":"P0AC51","creator":"vacs","date":"2023-05-22T08:13:04.241Z","features":{"pfam":[{"id":"PF01475","name":"Ferric uptake regulator family","start":20,"end":138}],"gene3D":[]},"genes":[{"name":{"value":"zur"},"synonyms":[{"value":"yjbK"}],"olnNames":[{"value":"b4046"},{"value":"JW5714"}]}],"length":171,"name":"Zinc uptake regulation protein","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":153,"end":171,"reference_id":"25369000","reference_source":"pmid","reference_html":"Structural and mechanistic basis of zinc regulation across the E. coli Zur regulon. <i> Gilston BA, Wang S, Marcus MD, Canalizo-Hernández MA, Swindell EP, Xue Y, Mondragón A, O'Halloran TV. </i> PLoS Biol, 2014","date":"2023-05-22T08:15:08.170Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"4MTD"},{"db":"PDB","id":"4MTE"}],"region_id":"DP04103r001","statement":[{"text":"Figure 1 shows the final model which includes amino acid residues 5–152 of four protein monomer chains (designated chains A, B, C, D), eight zinc ions, and two 31 bp strands of DNA (designated chains Y and Z) in the asymmetric unit.","type":"Results"},{"text":"However, we cannot rule out the potential for the disordered C-terminal tail of EcZur to bind a third zinc ion thus leaving any role for this site in EcZur as an open question.","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-16T15:26:38.160Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MEKTTTQELLAQAEKICAQRNVRLTPQRLEVLRLMSLQDGAISAYDLLDLLREAEPQAKPPTVYRALDFLLEQGFVHKVESTNSYVLCHLFDQPTHTSAMFICDRCGAVKEECAEGVEDIMHTLAAKMGFALRHNVIEAHGLCAACVEVEACRHPEQCQHDHSVQVKKKPR","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"alphafold_very_low_content":0.029239766081871343,"disorder_content":0.1111111111111111,"disprot_consensus":{"full":[{"start":153,"end":171,"type":"D"}],"Structural state":[{"start":153,"end":171,"type":"D"}]}},{"disprot_id":"DP04104","acc":"Q9NRA2","creator":"mgoncalves","date":"2023-05-22T09:01:30.028Z","features":{"pfam":[{"id":"PF07690","name":"Major Facilitator Superfamily","start":47,"end":441}],"gene3D":[]},"genes":[{"name":{"value":"SLC17A5"}}],"length":495,"name":"Sialin","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":31,"reference_id":"36662855","reference_source":"pmid","reference_html":"The molecular mechanism of sialic acid transport mediated by Sialin. <i> Hu W, Chi C, Song K, Zheng H. </i> Sci Adv, 2023","date":"2023-05-24T14:46:56.679Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"8DWI"},{"db":"EMDB","id":"27755"}],"region_id":"DP04104r001","statement":[{"text":"There are three patches of residues unresolved in Sialin: N-terminal residues 1 to 31, long luminal loop (L2) between TM1 and TM2 containing residues 69 to 101, and C-terminal residues 489 to 496, because of their poor experimental densities.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T12:31:04.706Z"}},{"start":69,"end":101,"reference_id":"36662855","reference_source":"pmid","reference_html":"The molecular mechanism of sialic acid transport mediated by Sialin. <i> Hu W, Chi C, Song K, Zheng H. </i> Sci Adv, 2023","date":"2023-06-21T09:40:18.349Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"8DWI"},{"db":"EMDB","id":"27755"}],"region_id":"DP04104r002","statement":[{"text":"There are three patches of residues unresolved in Sialin: N-terminal residues 1 to 31, long luminal loop (L2) between TM1 and TM2 containing residues 69 to 101, and C-terminal residues 489 to 496, because of their poor experimental densities.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T12:00:07.246Z"}},{"start":69,"end":101,"reference_id":"36662855","reference_source":"pmid","reference_html":"The molecular mechanism of sialic acid transport mediated by Sialin. <i> Hu W, Chi C, Song K, Zheng H. </i> Sci Adv, 2023","date":"2023-05-24T14:49:06.218Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"8DWI"},{"db":"EMDB","id":"27755"}],"region_id":"DP04104r003","statement":[{"text":"There are three patches of residues unresolved in Sialin: N-terminal residues 1 to 31, long luminal loop (L2) between TM1 and TM2 containing residues 69 to 101, and C-terminal residues 489 to 496, because of their poor experimental densities.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T12:31:06.814Z"}}],"regions_counter":3,"released":"2023_06","sequence":"MRSPVRDLARNDGEESTDRTPLLPGAPRAEAAPVCCSARYNLAILAFFGFFIVYALRVNLSVALVDMVDSNTTLEDNRTSKACPEHSAPIKVHHNQTGKKYQWDAETQGWILGSFFYGYIITQIPGGYVASKIGGKMLLGFGILGTAVLTLFTPIAADLGVGPLIVLRALEGLGEGVTFPAMHAMWSSWAPPLERSKLLSISYAGAQLGTVISLPLSGIICYYMNWTYVFYFFGTIGIFWFLLWIWLVSDTPQKHKRISHYEKEYILSSLRNQLSSQKSVPWVPILKSLPLWAIVVAHFSYNWTFYTLLTLLPTYMKEILRFNVQENGFLSSLPYLGSWLCMILSGQAADNLRAKWNFSTLCVRRIFSLIGMIGPAVFLVAAGFIGCDYSLAVAFLTISTTLGGFCSSGFSINHLDIAPSYAGILLGITNTFATIPGMVGPVIAKSLTPDNTVGEWQTVFYIAAAINVFGAIFFTLFAKGEVQNWALNDHHGHRH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.08282828282828283,"disorder_content":0.1292929292929293,"disprot_consensus":{"full":[{"start":1,"end":31,"type":"D"},{"start":69,"end":101,"type":"D"}],"Structural state":[{"start":1,"end":31,"type":"D"},{"start":69,"end":101,"type":"D"}],"Disorder function":[{"start":69,"end":101,"type":"F"}]}},{"disprot_id":"DP04105","acc":"O43747","creator":"mgoncalves","date":"2023-05-22T09:12:04.750Z","features":{"pfam":[{"id":"PF01602","name":"Adaptin N terminal region","start":23,"end":573},{"id":"PF02883","name":"Adaptin C-terminal domain","start":706,"end":817}],"gene3D":[]},"genes":[{"name":{"value":"AP1G1"},"synonyms":[{"value":"ADTG"},{"value":"CLAPG1"}]}],"length":822,"name":"AP-1 complex subunit gamma-1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":677,"end":699,"reference_id":"12042876","reference_source":"pmid","reference_html":"Structural basis for the accessory protein recruitment by the gamma-adaptin ear domain. <i> Nogi T, Shiba Y, Kawasaki M, Shiba T, Matsugaki N, Igarashi N, Suzuki M, Kato R, Takatsu H, Nakayama K, Wakatsuki S. </i> Nat Struct Biol, 2002","date":"2023-05-24T14:53:40.339Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.His685Pro","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"1IU1"}],"region_id":"DP04105r001","sequence_construct":"SVPQISQPHFLLDGLSSQPLFNDIAAGIPSITAYSKNGLKIEFTFERSNTNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSIVPAFNTGTITQVIKVLNPQKQQLRMRIKLTYNHKGSAMQDLAEVNNFPPQSWQ","statement":[{"text":"No model could be built for the N-terminal hinge region, residues 677–699, due to disorder in the electron density, which might account for the relatively high R-factors; the final values for working and test sets are 22.6 and 24.8% at 1.8 Å resolution, respectively.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T12:31:46.686Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MPAPIRLRELIRTIRTARTQAEEREMIQKECAAIRSSFREEDNTYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFTDKRIGYLGAMLLLDERQDVHLLMTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRKVPELMEMFLPATKNLLNEKNHGVLHTSVVLLTEMCERSPDMLAHFRKLVPQLVRILKNLIMSGYSPEHDVSGISDPFLQVRILRLLRILGRNDDDSSEAMNDILAQVATNTETSKNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNNDKNIRYVALTSLLKTVQTDHNAVQRHRSTIVDCLKDLDVSIKRRAMELSFALVNGNNIRGMMKELLYFLDSCEPEFKADCASGIFLAAEKYAPSKRWHIDTIMRVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILGDYSQQPLVQVAAWCIGEYGDLLVSGQCEEEEPIQVTEDEVLDILESVLISNMSTSVTRGYALTAIMKLSTRFTCTVNRIKKVVSIYGSSIDVELQQRAVEYNALFKKYDHMRSALLERMPVMEKVTTNGPTEIVQTNGETEPAPLETKPPPSGPQPTSQANDLLDLLGGNDITPVIPTAPTSKPSSAGGELLDLLGDINLTGAPAAAPAPASVPQISQPPFLLDGLSSQPLFNDIAAGIPSITAYSKNGLKIEFTFERSNTNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSIVPAFNTGTITQVIKVLNPQKQQLRMRIKLTYNHKGSAMQDLAEVNNFPPQSWQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.1362530413625304,"disorder_content":0.027980535279805353,"disprot_consensus":{"full":[{"start":677,"end":699,"type":"D"}],"Structural state":[{"start":677,"end":699,"type":"D"}]}},{"disprot_id":"DP04107","acc":"O95470","creator":"mgoncalves","date":"2023-05-22T09:40:22.346Z","features":{"pfam":[{"id":"PF00282","name":"Pyridoxal-dependent decarboxylase conserved domain","start":196,"end":448}],"gene3D":[]},"genes":[{"name":{"value":"SGPL1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:10817","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:10817"}}]},"synonyms":[{"value":"KIAA1252","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10574462","url":"http://www.ncbi.nlm.nih.gov/pubmed/10574462","alternativeUrl":"https://europepmc.org/abstract/MED/10574462"}}]}]}],"length":568,"name":"Sphingosine-1-phosphate lyase 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":62,"end":109,"reference_id":"24809814","reference_source":"pmid","reference_html":"Orally active 7-substituted (4-benzylphthalazin-1-yl)-2-methylpiperazin-1-yl]nicotinonitriles as active-site inhibitors of sphingosine 1-phosphate lyase for the treatment of multiple sclerosis. <i> Weiler S, Braendlin N, Beerli C, Bergsdorf C, Schubart A, Srinivas H, Oberhauser B, Billich A. </i> J Med Chem, 2014","date":"2023-06-21T09:03:38.990Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4Q6R"}],"region_id":"DP04107r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1110"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:73729049"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1061"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1051","statements":[{"type":"Results","text":"These two subunits form a tightly intertwined dimer with both chains contributing to the catalytic cavity defined by the covalently bound cofactor pyridoxal phosphate (PLP)."}]}],"statement":[{"text":"In each subunit the N-terminal regions spanning residues 62–109 and the C-terminal 18 residues (554 to 568) were disordered, corresponding to absence or poor electron density.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T12:02:38.721Z"}},{"start":554,"end":568,"reference_id":"24809814","reference_source":"pmid","reference_html":"Orally active 7-substituted (4-benzylphthalazin-1-yl)-2-methylpiperazin-1-yl]nicotinonitriles as active-site inhibitors of sphingosine 1-phosphate lyase for the treatment of multiple sclerosis. <i> Weiler S, Braendlin N, Beerli C, Bergsdorf C, Schubart A, Srinivas H, Oberhauser B, Billich A. </i> J Med Chem, 2014","date":"2023-06-21T09:03:19.957Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4Q6R"}],"region_id":"DP04107r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1110"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:753"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:73729049"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1061"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:1051","statements":[{"type":"Results","text":"These two subunits form a tightly intertwined dimer with both chains contributing to the catalytic cavity defined by the covalently bound cofactor pyridoxal phosphate (PLP)."}]}],"statement":[{"text":"In each subunit the N-terminal regions spanning residues 62–109 and the C-terminal 18 residues (554 to 568) were disordered, corresponding to absence or poor electron density.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T12:02:41.337Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MPSTDLLMLKAFEPYLEILEVYSTKAKNYVNGHCTKYEPWQLIAWSVVWTLLIVWGYEFVFQPESLWSRFKKKCFKLTRKMPIIGRKIQDKLNKTKDDISKNMSFLKVDKEYVKALPSQGLSSSAVLEKLKEYSSMDAFWQEGRASGTVYSGEEKLTELLVKAYGDFAWSNPLHPDIFPGLRKIEAEIVRIACSLFNGGPDSCGCVTSGGTESILMACKAYRDLAFEKGIKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTAMLVCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEKAGYPLEHPFDFRVKGVTSISADTHKYGYAPKGSSLVLYSDKKYRNYQFFVDTDWQGGIYASPTIAGSRPGGISAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKGIFVFGNPQLSVIALGSRDFDIYRLSNLMTAKGWNLNQLQFPPSIHFCITLLHARKRVAIQFLKDIRESVTQIMKNPKAKTTGMGAIYGMAQTTVDRNMVAELSSVFLDSLYSTDTVTQGSQMNGSPKPH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.02464788732394366,"disorder_content":0.11091549295774648,"disprot_consensus":{"full":[{"start":62,"end":109,"type":"D"},{"start":554,"end":568,"type":"D"}],"Structural state":[{"start":62,"end":109,"type":"D"},{"start":554,"end":568,"type":"D"}]}},{"disprot_id":"DP04108","acc":"P52306-2","creator":"mgoncalves","date":"2023-05-22T10:46:15.802Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"RAP1GDS1","evidences":[{"code":"ECO:0000303","source":{"name":"Citation","id":"Ref.3","url":"https://www.uniprot.org/uniprot/null#ref3"}}]},"synonyms":[{"value":"SMGGDS","evidences":[{"code":"ECO:0000303","source":{"name":"Citation","id":"Ref.3","url":"https://www.uniprot.org/uniprot/null#ref3"}}]}]}],"length":558,"name":"Isoform 2 of Rap1 GTPase-GDP dissociation stimulator 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":61,"end":78,"reference_id":"28630045","reference_source":"pmid","reference_html":"Structure-based analysis of the guanine nucleotide exchange factor SmgGDS reveals armadillo-repeat motifs and key regions for activity and GTPase binding. <i> Shimizu H, Toma-Fukai S, Saijo S, Shimizu N, Kontani K, Katada T, Shimizu T. </i> J Biol Chem, 2017","date":"2023-05-22T10:47:43.290Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"5XGC"}],"region_id":"DP04108r001","statement":[{"text":"In the N-terminal region, 18 residues (aa 61–78) were disordered, and side chains for 66 C-terminal amino acid residues were not assigned owing to the poor electron density. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-23T16:33:45.867Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MDNLSDTLKKLKITAVDKTEDSLEGCLDCLLQALAQNNTETSEKIQASGILQLFASLLTPQSSCKAKVANIIAEVAKNEFMRIPCVDAGLISPLVQLLNSKDQEVLLQTGRALGNICYDSHSLQAQLINMGVIPTLVKLLGIHCQNAALTEMCLVAFGNLAELESSKEQFASTNIAEELVKLFKKQIEHDKREMIFEVLAPLAENDAIKLQLVEAGLVECLLEIVQQKVDSDKEDDITELKTGSDLMVLLLLGDESMQKLFEGGKGSVFQRVLSWIPSNNHQLQLAGALAIANFARNDANCIHMVDNGIVEKLMDLLDRHVEDGNVTVQHAALSALRNLAIPVINKAKMLSAGVTEAVLKFLKSEMPPVQFKLLGTLRMLIDAQAEAAEQLGKNVKLVERLVEWCEAKDHAGVMGESNRLLSALIRHSKSKDVIKTIVQSGGIKHLVTMATSEHVIMQNEALVALALIAALELGTAEKDLESAKLVQILHRLLADERSAPEIKYNSMVLICALMGSECLHKEVQDLAFLDVVSKLRSHENKSVAQQASLTEQRLTVES","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"disorder_content":0.03225806451612903,"disprot_consensus":{"full":[{"start":61,"end":78,"type":"D"}],"Structural state":[{"start":61,"end":78,"type":"D"}]}},{"disprot_id":"DP04109","acc":"Q15326","creator":"mgoncalves","date":"2023-05-22T10:58:15.591Z","features":{"pfam":[{"id":"PF00439","name":"Bromodomain","start":182,"end":241},{"id":"PF00855","name":"PWWP domain","start":282,"end":350},{"id":"PF21524","name":"SAM domain-containing protein 1, WH domain","start":19,"end":67},{"id":"PF23461","name":"ZMYND11 protein coiled-coil","start":466,"end":518},{"id":"PF24324","name":"ZMYND11/ZMYD8, MYND zinc finger","start":563,"end":598}],"gene3D":[]},"genes":[{"name":{"value":"ZMYND11","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:16966","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:16966"}}]},"synonyms":[{"value":"BRAM1"},{"value":"BS69","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"24675531","url":"http://www.ncbi.nlm.nih.gov/pubmed/24675531","alternativeUrl":"https://europepmc.org/abstract/MED/24675531"}}]}]}],"length":602,"name":"Zinc finger MYND domain-containing protein 11","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":172,"end":195,"reference_id":"24675531","reference_source":"pmid","reference_html":"Crystal structure of human BS69 Bromo-ZnF-PWWP reveals its role in H3K36me3 nucleosome binding. <i> Wang J, Qin S, Li F, Li S, Zhang W, Peng J, Zhang Z, Gong Q, Wu J, Shi Y. </i> Cell Res, 2014","date":"2023-05-24T15:00:00.975Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4NS5"}],"region_id":"DP04109r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"}],"statement":[{"text":"PDB structure shows the protein lacks electron density in this region, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T12:32:57.783Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MARLTKRRQADTKAIQHLWAAIEIIRNQKQIANIDRITKYMSRVHGMHPKETTRQLSLAVKDGLIVETLTVGCKGSKAGIEQEGYWLPGDEIDWETENHDWYCFECHLPGEVLICDLCFRVYHSKCLSDEFRLRDSSSPWQCPVCRSIKKKNTNKQEMGTYLRFIVSRMKERAIDLNKKGKDNKHPMYRRLVHSAVDVPTIQEKVNEGKYRSYEEFKADAQLLLHNTVIFYGADSEQADIARMLYKDTCHELDELQLCKNCFYLSNARPDNWFCYPCIPNHELVWAKMKGFGFWPAKVMQKEDNQVDVRFFGHHHQRAWIPSENIQDITVNIHRLHVKRSMGWKKACDELELHQRFLREGRFWKSKNEDRGEEEAESSISSTSNEQLKVTQEPRAKKGRRNQSVEPKKEEPEPETEAVSSSQEIPTMPQPIEKVSVSTQTKKLSASSPRMLHRSTQTTNDGVCQSMCHDKYTKIFNDFKDRMKSDHKRETERVVREALEKLRSEMEEEKRQAVNKAVANMQGEMDRKCKQVKEKCKEEFVEEIKKLATQHKQLISQTKKKQWCYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.15946843853820597,"disorder_content":0.03986710963455149,"disprot_consensus":{"full":[{"start":172,"end":195,"type":"D"}],"Structural state":[{"start":172,"end":195,"type":"D"}]}},{"disprot_id":"DP04110","acc":"P0A8W0","creator":"vacs","date":"2023-05-22T11:31:04.933Z","features":{"pfam":[{"id":"PF00392","name":"Bacterial regulatory proteins, gntR family","start":32,"end":95},{"id":"PF07729","name":"FCD domain","start":126,"end":246}],"gene3D":[]},"genes":[{"name":{"value":"nanR","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01236","url":"https://hamap.expasy.org/unirule/MF_01236"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"9864311","url":"http://www.ncbi.nlm.nih.gov/pubmed/9864311","alternativeUrl":"https://europepmc.org/abstract/MED/9864311"}}]},"synonyms":[{"value":"yhcK"}],"olnNames":[{"value":"b3226"},{"value":"JW3195"}]}],"length":263,"name":"HTH-type transcriptional repressor NanR","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":1,"end":29,"reference_id":"33790291","reference_source":"pmid","reference_html":"Mechanism of NanR gene repression and allosteric induction of bacterial sialic acid metabolism. <i> Horne CR, Venugopal H, Panjikar S, Wood DM, Henrickson A, Brookes E, North RA, Murphy JM, Friemann R, Griffin MDW, Ramm G, Demeler B, Dobson RCJ. </i> Nat Commun, 2021","date":"2023-05-22T11:34:53.165Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6ON4"}],"region_id":"DP04110r001","statement":[{"text":"No density was visible for residues 1–30 and 247–263 in chain A or for residues 1–30 and 245–263 in chain B—presumably these were cleaved by proteolysis or disordered.","type":"Methods"},{"text":"Residues 1-29 are missing in both chains and are presumably disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T09:07:09.433Z"}},{"start":247,"end":263,"reference_id":"33790291","reference_source":"pmid","reference_html":"Mechanism of NanR gene repression and allosteric induction of bacterial sialic acid metabolism. <i> Horne CR, Venugopal H, Panjikar S, Wood DM, Henrickson A, Brookes E, North RA, Murphy JM, Friemann R, Griffin MDW, Ramm G, Demeler B, Dobson RCJ. </i> Nat Commun, 2021","date":"2023-05-22T11:36:12.030Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6ON4"}],"region_id":"DP04110r002","statement":[{"text":"No density was visible for residues 1–30 and 247–263 in chain A or for residues 1–30 and 245–263 in chain B—presumably these were cleaved by proteolysis or disordered.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T09:07:02.566Z"}},{"start":1,"end":20,"reference_id":"33790291","reference_source":"pmid","reference_html":"Mechanism of NanR gene repression and allosteric induction of bacterial sialic acid metabolism. <i> Horne CR, Venugopal H, Panjikar S, Wood DM, Henrickson A, Brookes E, North RA, Murphy JM, Friemann R, Griffin MDW, Ramm G, Demeler B, Dobson RCJ. </i> Nat Commun, 2021","date":"2023-05-22T11:43:11.381Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6WFQ"},{"db":"PDB","id":"6WG7"},{"db":"EMDB","id":"21652"},{"db":"EMDB","id":"21661"}],"region_id":"DP04110r003","statement":[{"text":"Although the resolution of this dataset (Supplementary Fig. 10b) does not allow us to accurately locate the N-terminal extensions or confidently define their role in the assembly process, we note that they would be well placed to form protein–protein interactions with the adjacent NanR dimers to stabilize the complex (Fig. 7f).","type":"Results"},{"text":"Residues 1-20 are missing in all structures and are presumably disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T09:06:41.572Z"}},{"start":249,"end":263,"reference_id":"33790291","reference_source":"pmid","reference_html":"Mechanism of NanR gene repression and allosteric induction of bacterial sialic acid metabolism. <i> Horne CR, Venugopal H, Panjikar S, Wood DM, Henrickson A, Brookes E, North RA, Murphy JM, Friemann R, Griffin MDW, Ramm G, Demeler B, Dobson RCJ. </i> Nat Commun, 2021","date":"2023-05-22T11:44:39.752Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6WG7"},{"db":"PDB","id":"6WFQ"},{"db":"EMDB","id":"21652"},{"db":"EMDB","id":"21661"}],"region_id":"DP04110r004","statement":[{"text":"Density for the α10-helix extended further than the crystal structure, allowing additional residues of the C-terminus in both monomers to be modeled.","type":"Results"},{"text":"Residues 249-263 are missing in all structures and are presumably disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T09:06:42.424Z"}},{"start":1,"end":29,"reference_id":"33790291","reference_source":"pmid","reference_html":"Mechanism of NanR gene repression and allosteric induction of bacterial sialic acid metabolism. <i> Horne CR, Venugopal H, Panjikar S, Wood DM, Henrickson A, Brookes E, North RA, Murphy JM, Friemann R, Griffin MDW, Ramm G, Demeler B, Dobson RCJ. </i> Nat Commun, 2021","date":"2023-06-21T11:23:14.593Z","curator_id":"vacs","curator_name":"Veronika Ács","curator_orcid":"0000-0001-6260-7287","term_id":"GO:0031334","term_name":"positive regulation of protein-containing complex assembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"EXP","region_id":"DP04110r005","statement":[{"text":"Such an interaction allows cooperative protein-protein interactions between NanR dimers via their N-terminal extensions.","type":"Abstract"},{"text":"Here we report that three NanR dimers cooperatively bind to the (GGTATA)3-repeat operator and that cooperativity is mediated by a 32-residue N-terminal extension.","type":"Introduction"},{"text":"A comparative sequence analysis of homologous proteins (Supplementary Fig. 2) revealed that NanR has a 32-residue N-terminal extension within the DNA-binding domain. To test whether this extension plays a role in cooperativity, we generated a truncated NanR construct (NanR33–263) and determined the effect of this truncation on (GGTATA)3-repeat binding using analytical ultracentrifugation. Whereas for wild-type NanR, several species were evident at 7–9 S (Fig. 2d, blue traces, and Supplementary Table 3), for NanR33–263 at the same concentrations only a single smaller species was evident at 4–5.5 S (Fig. 2d, red traces), demonstrating that although NanR33–263 can bind DNA, it is unable to form the higher-order hetero-complexes. Together, these data implicate the N-terminal extension as a crucial determinant of cooperative assembly.","type":"Results"},{"text":"Collectively, our data show that NanR binds the (GGTATA)3-repeat operator with nanomolar affinity and that binding is cooperative, which is mediated by a unique N-terminal extension.","type":"Results"},{"text":"We defined the region of NanR that is responsible for cooperative binding to within the 32-residue N-terminal extension of the DNA-binding domain, as removal of this extension abolished assembly of the higher-order oligomers.","type":"Discussion"},{"text":"To repress gene expression, dimers of NanR cooperatively and with nanomolar affinity bind to each of the three GGTATA repeats to form a NanR-dimer3/DNA hetero-complex through rearrangement of their N-terminal DNA-binding domains. This cooperative assembly is believed to be mediated by an N-terminal extension, unique to NanR among closely related GntR-type regulators.","type":"Figure"}],"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of protein complex assembly.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T11:34:09.105Z"}}],"regions_counter":5,"released":"2024_06","sequence":"MGLMNAFDSQTEDSSPAIGRNLRSRPLARKKLSEMVEEELEQMIRRREFGEGEQLPSERELMAFFNVGRPSVREALAALKRKGLVQINNGERARVSRPSADTIIGELSGMAKDFLSHPGGIAHFEQLRLFFESSLVRYAAEHATDEQIDLLAKALEINSQSLDNNAAFIRSDVDFHRVLAEIPGNPIFMAIHVALLDWLIAARPTVTDQALHEHNNVSYQQHIAIVDAIRRHDPDEADRALQSHLNSVSATWHAFGQTTNKKK","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"alphafold_very_low_content":0.057034220532319393,"disorder_content":0.17490494296577946,"disprot_consensus":{"full":[{"start":1,"end":29,"type":"D"},{"start":247,"end":263,"type":"D"}],"Structural state":[{"start":1,"end":29,"type":"D"},{"start":247,"end":263,"type":"D"}],"Biological process":[{"start":1,"end":29,"type":"F"}]}},{"disprot_id":"DP04111","acc":"Q96C36","creator":"mgoncalves","date":"2023-05-23T08:54:44.674Z","features":{"pfam":[{"id":"PF03807","name":"NADP oxidoreductase coenzyme F420-dependent","start":3,"end":98},{"id":"PF14748","name":"Pyrroline-5-carboxylate reductase dimerisation","start":164,"end":268}],"gene3D":[]},"genes":[{"name":{"value":"PYCR2"}}],"length":320,"name":"Pyrroline-5-carboxylate reductase 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":274,"end":300,"reference_id":"32330411","reference_source":"pmid","reference_html":"Loss of PYCR2 Causes Neurodegeneration by Increasing Cerebral Glycine Levels via SHMT2. <i> Escande-Beillard N, Loh A, Saleem SN, Kanata K, Hashimoto Y, Altunoglu U, Metoska A, Grandjean J, Ng FM, Pomp O, Baburajendran N, Wong J, Hill J, Beillard E, Cozzone P, Zaki M, Kayserili H, Hamada H, Shiratori H, Reversade B. </i> Neuron, 2020","date":"2023-05-24T15:02:12.962Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6LHM"}],"region_id":"DP04111r001","statement":[{"text":"The PDB structure shows that the protein lacks electronic density in this region in the 5 generated monomers, indicating that it is disordered.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr239Ile","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T12:33:22.847Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MSVGFIGAGQLAYALARGFTAAGILSAHKIIASSPEMNLPTVSALRKMGVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLMAFQPAPKVIRCMTNTPVVVQEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFMALDALADGGVKMGLPRRLAIQLGAQALLGAAKMLLDSEQHPCQLKDNVCSPGGATIHALHFLESGGFRSLLINAVEASCIRTRELQSMADQEKISPAALKKTLLDRVKLESPTVSTLTPSSPGKLLTRSLALGGKKD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.115625,"disorder_content":0.084375,"disprot_consensus":{"full":[{"start":274,"end":300,"type":"D"}],"Structural state":[{"start":274,"end":300,"type":"D"}]}},{"disprot_id":"DP04112","acc":"Q3SYG4","creator":"mgoncalves","date":"2023-05-23T09:17:44.768Z","features":{"pfam":[{"id":"PF14727","name":"PTHB1 N-terminal","start":1,"end":363},{"id":"PF14728","name":"PTHB1 GAE domain","start":437,"end":527},{"id":"PF23337","name":"PTHB1 platform domain","start":530,"end":637},{"id":"PF23338","name":"PTHB1 hairpin","start":639,"end":742},{"id":"PF23339","name":"PTHB1 C-terminal helix bundle","start":744,"end":819}],"gene3D":[]},"genes":[{"name":{"value":"BBS9"},"synonyms":[{"value":"PTHB1"}]}],"length":887,"name":"Protein PTHB1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":219,"end":232,"reference_id":"26085087","reference_source":"pmid","reference_html":"Structural Characterization of Bardet-Biedl Syndrome 9 Protein (BBS9). <i> Knockenhauer KE, Schwartz TU. </i> J Biol Chem, 2015","date":"2023-05-24T15:06:30.036Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4YD8"}],"region_id":"DP04112r001","statement":[{"text":"Exceptions to this include the protein termini, as residues 1–2 and 370–407 are disordered, as well as several loop regions, where residues 113–117, 219–232, and 254–255 could not be built with confidence.","type":"Results"}],"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":5,"end":5,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":50,"end":50,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":96,"end":96,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":127,"end":127,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":130,"end":130,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":142,"end":142,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":162,"end":162,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":164,"end":164,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":166,"end":166,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":284,"end":284,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":315,"end":315,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":389,"end":389,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":408,"end":408,"position":"Specific residue"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T12:34:06.627Z"}},{"start":370,"end":407,"reference_id":"26085087","reference_source":"pmid","reference_html":"Structural Characterization of Bardet-Biedl Syndrome 9 Protein (BBS9). <i> Knockenhauer KE, Schwartz TU. </i> J Biol Chem, 2015","date":"2023-05-24T15:08:42.662Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"4YD8"}],"region_id":"DP04112r002","statement":[{"text":"Exceptions to this include the protein termini, as residues 1–2 and 370–407 are disordered, as well as several loop regions, where residues 113–117, 219–232, and 254–255 could not be built with confidence.","type":"Results"}],"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":5,"end":5,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":50,"end":50,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":96,"end":96,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":127,"end":127,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":130,"end":130,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":142,"end":142,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":162,"end":162,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":164,"end":164,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":166,"end":166,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":284,"end":284,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":315,"end":315,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":389,"end":389,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":408,"end":408,"position":"Specific residue"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T12:34:08.077Z"}},{"start":210,"end":232,"reference_id":"31951201","reference_source":"pmid","reference_html":"Structure of the human BBSome core complex.  <i> Klink BU, Gatsogiannis C, Hofnagel O, Wittinghofer A, Raunser S. </i> Elife, 2020","date":"2023-05-24T15:12:20.956Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6XT9"},{"db":"EMDB","id":"10617"}],"region_id":"DP04112r003","statement":[{"text":"Besides BBS5 that was only sub-stoichiometrically bound (Figure 1—figure supplement 1A), all domains were well resolved with only some connecting loops and N-and C-terminal regions missing (Figure 1A, Figure 1—figure supplements 1 and 2).","type":"Results"},{"text":"The electron microscopy of the human BBSome core complex shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8NFJ9"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q96RK4"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A0C4DGY3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A8MTZ0"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T12:34:45.542Z"}},{"start":801,"end":887,"reference_id":"31951201","reference_source":"pmid","reference_html":"Structure of the human BBSome core complex.  <i> Klink BU, Gatsogiannis C, Hofnagel O, Wittinghofer A, Raunser S. </i> Elife, 2020","date":"2023-05-24T15:13:01.756Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6XT9"},{"db":"EMDB","id":"10617"}],"region_id":"DP04112r004","statement":[{"text":"Besides BBS5 that was only sub-stoichiometrically bound (Figure 1—figure supplement 1A), all domains were well resolved with only some connecting loops and N-and C-terminal regions missing (Figure 1A, Figure 1—figure supplements 1 and 2).","type":"Results"},{"text":"The electron microscopy of the human BBSome core complex shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8NFJ9"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q96RK4"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A0C4DGY3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A8MTZ0"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T12:34:49.408Z"}}],"regions_counter":4,"released":"2023_06","sequence":"MSLFKARDWWSTILGDKEEFDQGCLCLANVDNSGNGQDKIIVGSFMGYLRIFSPHPAKTGDGAQAEDLLLEVDLRDPVLQVEVGKFVSGTEMLHLAVLHSRKLCVYSVSGTLGNVEHGNQCQMKLMYEHNLQRTACNMTYGSFGGVKGRDLICIQSMDGMLMVFEQESYAFGRFLPGFLLPGPLAYSSRTDSFLTVSSCQQVESYKYQVLAFATDADKRQETEQQKLGSGKRLVVDWTLNIGEQALDICIVSFNQSASSVFVLGERNFFCLKDNGQIRFMKKLDWSPSCFLPYCSVSEGTINTLIGNHNNMLHIYQDVTLKWATQLPHIPVAVRVGCLHDLKGVIVTLSDDGHLQCSYLGTDPSLFQAPNVQSRELNYDELDVEMKELQKIIKDVNKSQGVWPMTEREDDLNVSVVVSPNFDSVSQATDVEVGTDLVPSVTVKVTLQNRVILQKAKLSVYVQPPLELTCDQFTFEFMTPDLTRTVSFSVYLKRSYTPSELEGNAVVSYSRPTDRNPDGIPRVIQCKFRLPLKLICLPGQPSKTASHKITIDTNKSPVSLLSLFPGFASQSDDDQVNVMGFHFLGGARITVLASKTSQRYRIQSEQFEDLWLITNELILRLQEYFEKQGVKDFACSFSGSIPLQEYFELIDHHFELRINGEKLEELLSERAVQFRAIQRRLLARFKDKTPAPLQHLDTLLDGTYKQVIALADAVEENQGNLFQSFTRLKSATHLVILLIALWQKLSADQVAILEAAFLPLQEDTQELGWEETVDAAISHLLKTCLSKSSKEQALNLNSQLNIPKDTSQLKKHITLLCDRLSKGGRLCLSTDAAAPQTMVMPGGCTTIPESDLEERSVEQDSTELFTNHRHLTAETPRPEVSPLQGVSE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.08793686583990981,"disorder_content":0.1668545659526494,"disprot_consensus":{"full":[{"start":210,"end":232,"type":"D"},{"start":370,"end":407,"type":"D"},{"start":801,"end":887,"type":"D"}],"Structural state":[{"start":210,"end":232,"type":"D"},{"start":370,"end":407,"type":"D"},{"start":801,"end":887,"type":"D"}]}},{"disprot_id":"DP04113","acc":"Q8NFJ9","creator":"mgoncalves","date":"2023-05-23T09:55:51.742Z","features":{"pfam":[{"id":"PF14779","name":"Ciliary BBSome complex subunit 1","start":23,"end":276},{"id":"PF23304","name":"Bardet-Biedl syndrome 1 protein, GAE domain","start":486,"end":587}],"gene3D":[]},"genes":[{"name":{"value":"BBS1"},"synonyms":[{"value":"BBS2L2"}]}],"length":593,"name":"Bardet-Biedl syndrome 1 protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":20,"reference_id":"31951201","reference_source":"pmid","reference_html":"Structure of the human BBSome core complex.  <i> Klink BU, Gatsogiannis C, Hofnagel O, Wittinghofer A, Raunser S. </i> Elife, 2020","date":"2023-05-24T15:15:31.243Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6XT9"},{"db":"EMDB","id":"10617"}],"region_id":"DP04113r001","statement":[{"text":"Besides BBS5 that was only sub-stoichiometrically bound (Figure 1—figure supplement 1A), all domains were well resolved with only some connecting loops and N-and C-terminal regions missing (Figure 1A, Figure 1—figure supplements 1 and 2).","type":"Results"},{"text":"The electron microscopy of the human BBSome core complex shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q3SYG4"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q96RK4"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A0C4DGY3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A8MTZ0"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T12:36:17.381Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MAAASSSDSDACGAESNEANSKWLDAHYDPMANIHTFSACLALADLHGDGEYKLVVGDLGPGGQQPRLKVLKGPLVMTESPLPALPAAAATFLMEQHEPRTPALALASGPCVYVYKNLRPYFKFSLPQLPPNPLEQDLWNQAKEDRIDPLTLKEMLESIRETAEEPLSIQSLRFLQLELSEMEAFVNQHKSNSIKRQTVITTMTTLKKNLADEDAVSCLVLGTENKELLVLDPEAFTILAKMSLPSVPVFLEVSGQFDVEFRLAAACRNGNIYILRRDSKHPKYCIELSAQPVGLIRVHKVLVVGSTQDSLHGFTHKGKKLWTVQMPAAILTMNLLEQHSRGLQAVMAGLANGEVRIYRDKALLNVIHTPDAVTSLCFGRYGREDNTLIMTTRGGGLIIKILKRTAVFVEGGSEVGPPPAQAMKLNVPRKTRLYVDQTLREREAGTAMHRAFQTDLYLLRLRAARAYLQALESSLSPLSTTAREPLKLHAVVQGLGPTFKLTLHLQNTSTTRPVLGLLVCFLYNEALYSLPRAFFKVPLLVPGLNYPLETFVESLSNKGISDIIKVLVLREGQSAPLLSAHVNMPGSEGLAAA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.04047217537942664,"disorder_content":0.03372681281618887,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"D"}],"Structural state":[{"start":1,"end":20,"type":"D"}]}},{"disprot_id":"DP04114","acc":"A0A0C4DGY3","creator":"mgoncalves","date":"2023-05-23T09:58:50.388Z","features":{"pfam":[{"id":"PF13181","name":"Tetratricopeptide repeat","start":220,"end":243},{"id":"PF13181","name":"Tetratricopeptide repeat","start":284,"end":314},{"id":"PF13432","name":"Tetratricopeptide repeat","start":391,"end":447}],"gene3D":[]},"genes":[{"name":{"value":"TTC8","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ALQ34308.1","url":"https://www.ebi.ac.uk/ena/browser/view/ALQ34308.1"}},{"code":"ECO:0000313","source":{"name":"Ensembl","id":"ENSP00000482721.1","url":"https://www.ensembl.org/id/ENSP00000482721.1"}}]}}],"length":505,"name":"Tetratricopeptide repeat domain 8","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":78,"end":180,"reference_id":"31951201","reference_source":"pmid","reference_html":"Structure of the human BBSome core complex.  <i> Klink BU, Gatsogiannis C, Hofnagel O, Wittinghofer A, Raunser S. </i> Elife, 2020","date":"2023-05-24T15:19:13.182Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6XT9"},{"db":"EMDB","id":"10617"}],"region_id":"DP04114r001","statement":[{"text":"Besides BBS5 that was only sub-stoichiometrically bound (Figure 1—figure supplement 1A), all domains were well resolved with only some connecting loops and N-and C-terminal regions missing (Figure 1A, Figure 1—figure supplements 1 and 2).","type":"Results"},{"text":"The electron microscopy of the human BBSome core complex shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q3SYG4"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8NFJ9"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q96RK4"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A8MTZ0"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T12:37:23.675Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MSSEMEPLLLAWSYFRRRKFQLCADLCTQMLEKSPYDQAAWILKARALTEMVYIDEIDVDQEGIAEMMLDENAIAQVPRPGTSLKLPGTNQTGGPSQAVRPITQAGRPITGFLRPSTQSGRPGTMEQAIRTPRTAYTARPITSSSGRFVRLGTASMLTSPDGPFINLSRLNLTKYSQKPKLAKALFEYIFHHENDVKTALDLAALSTEHSQYKDWWWKVQIGKCYYRLGMYREAEKQFKSALKQQEMVDTFLYLAKVYVSLDQPVTALNLFKQGLDKFPGEVTLLCGIARIYEEMNNMSSAAEYYKEVLKQDNTHVEAIACIGSNHFYSDQPEIALRFYRRLLQMGIYNGQLFNNLGLCCFYAQQYDMTLTSFERALSLAENEEEAADVWYNLGHVAVGIGDTNLAHQCFRLALVNNNNHAEAYNNLAVLEMRKGHVEQARALLQTASSLAPHMYEPHFNFATISDKIGDLQRSYVAAQKSEAAFPDHVDTQHLIKQLRQHFAML","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.0297029702970297,"disorder_content":0.20396039603960395,"disprot_consensus":{"full":[{"start":78,"end":180,"type":"D"}],"Structural state":[{"start":78,"end":180,"type":"D"}]}},{"disprot_id":"DP04115","acc":"Q96RK4","creator":"mgoncalves","date":"2023-05-23T10:03:09.537Z","features":{"pfam":[{"id":"PF13181","name":"Tetratricopeptide repeat","start":272,"end":301},{"id":"PF13181","name":"Tetratricopeptide repeat","start":306,"end":336},{"id":"PF13414","name":"TPR repeat","start":110,"end":145},{"id":"PF13414","name":"TPR repeat","start":175,"end":216},{"id":"PF13432","name":"Tetratricopeptide repeat","start":344,"end":398}],"gene3D":[]},"genes":[{"name":{"value":"BBS4"}}],"length":519,"name":"Bardet-Biedl syndrome 4 protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":27,"reference_id":"31951201","reference_source":"pmid","reference_html":"Structure of the human BBSome core complex.  <i> Klink BU, Gatsogiannis C, Hofnagel O, Wittinghofer A, Raunser S. </i> Elife, 2020","date":"2023-05-24T15:16:44.906Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6XT9"},{"db":"EMDB","id":"10617"}],"region_id":"DP04115r001","statement":[{"text":"Besides BBS5 that was only sub-stoichiometrically bound (Figure 1—figure supplement 1A), all domains were well resolved with only some connecting loops and N-and C-terminal regions missing (Figure 1A, Figure 1—figure supplements 1 and 2).","type":"Results"},{"text":"The electron microscopy of the human BBSome core complex shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q3SYG4"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8NFJ9"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A0C4DGY3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A8MTZ0"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T12:38:10.538Z"}},{"start":424,"end":519,"reference_id":"31951201","reference_source":"pmid","reference_html":"Structure of the human BBSome core complex.  <i> Klink BU, Gatsogiannis C, Hofnagel O, Wittinghofer A, Raunser S. </i> Elife, 2020","date":"2023-05-24T15:17:42.997Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6XT9"},{"db":"EMDB","id":"10617"}],"region_id":"DP04115r002","statement":[{"text":"Besides BBS5 that was only sub-stoichiometrically bound (Figure 1—figure supplement 1A), all domains were well resolved with only some connecting loops and N-and C-terminal regions missing (Figure 1A, Figure 1—figure supplements 1 and 2).","type":"Results"},{"text":"The electron microscopy of the human BBSome core complex shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q3SYG4"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8NFJ9"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A0C4DGY3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A8MTZ0"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T12:38:20.806Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MAEERVATRTQFPVSTESQKPRQKKAPEFPILEKQNWLIHLHYIRKDYEACKAVIKEQLQETQGLCEYAIYVQALIFRLEGNIQESLELFQTCAVLSPQSADNLKQVARSLFLLGKHKAAIEVYNEAAKLNQKDWEISHNLGVCYIYLKQFNKAQDQLHNALNLNRHDLTYIMLGKIHLLEGDLDKAIEVYKKAVEFSPENTELLTTLGLLYLQLGIYQKAFEHLGNALTYDPTNYKAILAAGSMMQTHGDFDVALTKYRVVACAVPESPPLWNNIGMCFFGKKKYVAAISCLKRANYLAPFDWKILYNLGLVHLTMQQYASAFHFLSAAINFQPKMGELYMLLAVALTNLEDIENAKRAYAEAVHLDKCNPLVNLNYAVLLYNQGEKKNALAQYQEMEKKVSLLKDNSSLEFDSEMVEMAQKLGAALQVGEALVWTKPVKDPKSKHQTTSTSKPASFQQPLGSNQALGQAMSSAAAYRTLPSGAGGTSQFTKPPSLPLEPEPAVESSPTETSEQIREK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.17341040462427745,"disorder_content":0.23699421965317918,"disprot_consensus":{"full":[{"start":1,"end":27,"type":"D"},{"start":424,"end":519,"type":"D"}],"Structural state":[{"start":1,"end":27,"type":"D"},{"start":424,"end":519,"type":"D"}]}},{"disprot_id":"DP04116","acc":"A8MTZ0","creator":"mgoncalves","date":"2023-05-23T10:07:03.231Z","features":{"pfam":[{"id":"PF14777","name":"Cilia BBSome complex subunit 10","start":23,"end":85}],"gene3D":[]},"genes":[{"name":{"value":"BBIP1"},"synonyms":[{"value":"BBIP10"},{"value":"NCRNA00081"}]}],"length":92,"name":"BBSome-interacting protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":25,"reference_id":"31951201","reference_source":"pmid","reference_html":"Structure of the human BBSome core complex.  <i> Klink BU, Gatsogiannis C, Hofnagel O, Wittinghofer A, Raunser S. </i> Elife, 2020","date":"2023-05-24T15:20:45.951Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6XT9"},{"db":"EMDB","id":"10617"}],"region_id":"DP04116r001","statement":[{"text":"Besides BBS5 that was only sub-stoichiometrically bound (Figure 1—figure supplement 1A), all domains were well resolved with only some connecting loops and N-and C-terminal regions missing (Figure 1A, Figure 1—figure supplements 1 and 2).","type":"Results"},{"text":"The electron microscopy of the human BBSome core complex shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q3SYG4"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8NFJ9"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q96RK4"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A0C4DGY3"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T12:39:31.577Z"}},{"start":81,"end":92,"reference_id":"31951201","reference_source":"pmid","reference_html":"Structure of the human BBSome core complex.  <i> Klink BU, Gatsogiannis C, Hofnagel O, Wittinghofer A, Raunser S. </i> Elife, 2020","date":"2023-05-24T15:21:33.217Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6XT9"},{"db":"EMDB","id":"10617"}],"region_id":"DP04116r002","statement":[{"text":"Besides BBS5 that was only sub-stoichiometrically bound (Figure 1—figure supplement 1A), all domains were well resolved with only some connecting loops and N-and C-terminal regions missing (Figure 1A, Figure 1—figure supplements 1 and 2).","type":"Results"},{"text":"The electron microscopy of the human BBSome core complex shows this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q3SYG4"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8NFJ9"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q96RK4"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A0C4DGY3"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T12:39:29.774Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MLKAAAKRPELSGKNTISNNSDMAEVKSMFREVLPKQGPLFVEDIMTMVLCKPKLLPLKSLTLEKLEKMHQAAQNTIRQQEMAEKDQRQITH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.021739130434782608,"disorder_content":0.40217391304347827,"disprot_consensus":{"full":[{"start":1,"end":25,"type":"D"},{"start":81,"end":92,"type":"D"}],"Structural state":[{"start":1,"end":25,"type":"D"},{"start":81,"end":92,"type":"D"}]}},{"disprot_id":"DP04117","acc":"Q8N3I7","creator":"mgoncalves","date":"2023-05-23T10:10:23.330Z","features":{"pfam":[{"id":"PF07289","name":"Bardet-Biedl syndrome 5 protein N-terminal PH-like domain","start":28,"end":133},{"id":"PF29715","name":"Bardet-Biedl syndrome 5 protein second PH-like domain","start":141,"end":267}],"gene3D":[]},"genes":[{"name":{"value":"BBS5"}}],"length":341,"name":"Bardet-Biedl syndrome 5 protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":135,"end":148,"reference_id":"31951201","reference_source":"pmid","reference_html":"Structure of the human BBSome core complex.  <i> Klink BU, Gatsogiannis C, Hofnagel O, Wittinghofer A, Raunser S. </i> Elife, 2020","date":"2023-05-24T15:26:56.384Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6XTB"},{"db":"EMDB","id":"10618"}],"region_id":"DP04117r001","statement":[{"text":"The parts of the primary structure that could be assigned in the density is shown in full colors, while non-modeled regions are represented in opaque colors.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-12T17:54:49.512Z"}},{"start":254,"end":341,"reference_id":"31951201","reference_source":"pmid","reference_html":"Structure of the human BBSome core complex.  <i> Klink BU, Gatsogiannis C, Hofnagel O, Wittinghofer A, Raunser S. </i> Elife, 2020","date":"2023-05-24T15:27:22.077Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"6XTB"},{"db":"EMDB","id":"10618"}],"region_id":"DP04117r002","statement":[{"text":"The parts of the primary structure that could be assigned in the density is shown in full colors, while non-modeled regions are represented in opaque colors.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-12T17:54:47.941Z"}}],"regions_counter":2,"released":"2023_06","sequence":"MSVLDALWEDRDVRFDLSAQQMKTRPGEVLIDCLDSIEDTKGNNGDRGRLLVTNLRILWHSLALSRVNVSVGYNCILNITTRTANSKLRGQTEALYILTKCNSTRFEFIFTNLVPGSPRLFTSVMAVHRAYETSKMYRDFKLRSALIQNKQLRLLPQEHVYDKINGVWNLSSDQGNLGTFFITNVRIVWHANMNDSFNVSIPYLQIRSIKIRDSKFGLALVIESSQQSGGYVLGFKIDPVEKLQESVKEINSLHKVYSASPIFGVDYEMEEKPQPLEALTVEQIQDDVEIDSDGHTDAFVAYFADGNKQQDREPVFSEELGLAIEKLKDGFTLQGLWEVMS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.026392961876832845,"disorder_content":0.2991202346041056,"disprot_consensus":{"full":[{"start":135,"end":148,"type":"D"},{"start":254,"end":341,"type":"D"}],"Structural state":[{"start":135,"end":148,"type":"D"},{"start":254,"end":341,"type":"D"}]}},{"disprot_id":"DP04118","acc":"O43665","creator":"vnugnes","date":"2023-05-23T15:24:22.297Z","features":{"pfam":[{"id":"PF00615","name":"Regulator of G protein signaling domain","start":41,"end":154}],"gene3D":[]},"genes":[{"name":{"value":"RGS10"}}],"length":181,"name":"Regulator of G-protein signaling 10","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":98,"end":116,"reference_id":"18434541","reference_source":"pmid","reference_html":"Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits. <i> Soundararajan M, Willard FS, Kimple AJ, Turnbull AP, Ball LJ, Schoch GA, Gileadi C, Fedorov OY, Dowler EF, Higman VA, Hutsell SQ, Sundström M, Doyle DA, Siderovski DP. </i> Proc Natl Acad Sci U S A, 2008","date":"2023-05-23T15:34:13.947Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2I59"}],"region_id":"DP04118r001","statement":[{"text":"In our RGS10 solution structure (PDB ID 2I59), the region Leu-90 to Glu-108 (Fig. S4A) shows high flexibility as reflected by low 15N-1H nuclear Overhauser effect (NOE) values (0.5–0.6) and a reduced T1/T2 ratio compared with well ordered parts of the structure (data not shown).","type":"Results"},{"text":"Authors are referring to the 98-116 region of the UniProt sequence.","type":"Curator statement"}]},{"start":111,"end":121,"reference_id":"18434541","reference_source":"pmid","reference_html":"Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits. <i> Soundararajan M, Willard FS, Kimple AJ, Turnbull AP, Ball LJ, Schoch GA, Gileadi C, Fedorov OY, Dowler EF, Higman VA, Hutsell SQ, Sundström M, Doyle DA, Siderovski DP. </i> Proc Natl Acad Sci U S A, 2008","date":"2023-05-23T15:42:28.373Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2IHB"}],"region_id":"DP04118r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08754 "},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:135398619"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5311325"}],"statement":[{"text":"Eleven amino acids within RGS10, including αVI, are disordered in the Gαi3-bound complex (Fig. S4A). ","type":"Results"}]},{"start":10,"end":31,"reference_id":"18434541","reference_source":"pmid","reference_html":"Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits. <i> Soundararajan M, Willard FS, Kimple AJ, Turnbull AP, Ball LJ, Schoch GA, Gileadi C, Fedorov OY, Dowler EF, Higman VA, Hutsell SQ, Sundström M, Doyle DA, Siderovski DP. </i> Proc Natl Acad Sci U S A, 2008","date":"2023-05-23T15:43:11.543Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2IHB"}],"region_id":"DP04118r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08754 "},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:135398619"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5311325"}],"statement":[{"text":"This region lacks electron density in the PDB structure indicating it is disordered.  ","type":"Results"}]}],"regions_counter":3,"released":"2024_06","sequence":"MFNRAVSRLSRKRPPSDIHDSDGSSSSSHQSLKSTAKWAASLENLLEDPEGVKRFREFLKKEFSEENVLFWLACEDFKKMQDKTQMQEKAKEIYMTFLSSKASSQVNVEGQSRLNEKILEEPHPLMFQKLQDQIFNLMKYDSYSRFLKSDLFLKHKRTEEEEEDLPDAQTAAKRASRIYNT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.1270718232044199,"disorder_content":0.2541436464088398,"disprot_consensus":{"full":[{"start":10,"end":31,"type":"D"},{"start":98,"end":121,"type":"D"}],"Structural state":[{"start":10,"end":31,"type":"D"},{"start":98,"end":121,"type":"D"}]}},{"disprot_id":"DP04119","acc":"Q01105-2","creator":"mgoncalves","date":"2023-05-24T08:12:49.023Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"SET"}}],"length":277,"name":"Isoform 2 of Protein SET","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":168,"end":188,"reference_id":"17360516","reference_source":"pmid","reference_html":"Relationship between the structure of SET/TAF-Ibeta/INHAT and its histone chaperone activity. <i> Muto S, Senda M, Akai Y, Sato L, Suzuki T, Nagai R, Senda T, Horikoshi M. </i> Proc Natl Acad Sci U S A, 2007","date":"2023-05-24T08:27:54.029Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe3Gln","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu104Met","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu145Met","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu166Met","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"2E50"}],"region_id":"DP04119r001","sequence_construct":"MSAQAAKVSKKELNSNHDGADETSEKEQQEAIEHIDEVQNEIDRLNEQASEEILKVEQKYNKLRQPFFQKRSELIAKIPNFWVTTFVNHPQVSALLGEEDEEAMHYLTRVEVTEFEDIKSGYRIDFYFDENPYFENKVLSKEFHMNESGDPSSKSTEIKWKSGKDMTKRSSQTQNKASRKRQHEEPESFFTWFTDHSDAGADELGEVIKDDIWPNPLQYYLVPDM","statement":[{"text":"The electron density of the residues between the β4-strand and α6-helix (residues 168–188) could not be observed (Fig. 2A), which suggests that the lower part of the earmuff domain is highly mobile in aqueous solution. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-31T14:11:58.277Z"}}],"regions_counter":3,"released":"2023_06","sequence":"MSAPAAKVSKKELNSNHDGADETSEKEQQEAIEHIDEVQNEIDRLNEQASEEILKVEQKYNKLRQPFFQKRSELIAKIPNFWVTTFVNHPQVSALLGEEDEEALHYLTRVEVTEFEDIKSGYRIDFYFDENPYFENKVLSKEFHLNESGDPSSKSTEIKWKSGKDLTKRSSQTQNKASRKRQHEEPESFFTWFTDHSDAGADELGEVIKDDIWPNPLQYYLVPDMDDEEGEGEEDDDDDEEEEGLEDIDEEGDEDEGEEDEDDDEGEEGEEDEGEDD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"disorder_content":0.07581227436823104,"disprot_consensus":{"full":[{"start":168,"end":188,"type":"D"}],"Structural state":[{"start":168,"end":188,"type":"D"}]}},{"disprot_id":"DP04120","acc":"O14775","creator":"mgoncalves","date":"2023-05-24T13:10:40.179Z","features":{"pfam":[{"id":"PF25391","name":"G protein beta WD-40 repeat protein","start":54,"end":394}],"gene3D":[]},"genes":[{"name":{"value":"GNB5"}}],"length":395,"name":"Guanine nucleotide-binding protein subunit beta-5","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":56,"reference_id":"34815401","reference_source":"pmid","reference_html":"Structure of the class C orphan GPCR GPR158 in complex with RGS7-Gβ5. <i> Jeong E, Kim Y, Jeong J, Cho Y. </i> Nat Commun, 2021","date":"2023-05-31T14:19:03.966Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7EWP"},{"db":"EMDB","id":"31360"},{"db":"PDB","id":"7EWR"},{"db":"EMDB","id":"31363"}],"region_id":"DP04120r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P49802"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q5T848"}],"statement":[{"text":"The electron microscopy of the class C orphan GPCR GPR158 (Q5T848) in complex with RGS7(P49802)-Gβ5(O14775) shows that this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-31T14:24:37.436Z"}}],"regions_counter":1,"released":"2023_06","sequence":"MCDQTFLVNVFGSCDKCFKQRALRPVFKKSQQLSYCSTCAEIMATEGLHENETLASLKSEAESLKGKLEEERAKLHDVELHQVAERVEALGQFVMKTRRTLKGHGNKVLCMDWCKDKRRIVSSSQDGKVIVWDSFTTNKEHAVTMPCTWVMACAYAPSGCAIACGGLDNKCSVYPLTFDKNENMAAKKKSVAMHTNYLSACSFTNSDMQILTASGDGTCALWDVESGQLLQSFHGHGADVLCLDLAPSETGNTFVSGGCDKKAMVWDMRSGQCVQAFETHESDINSVRYYPSGDAFASGSDDATCRLYDLRADREVAIYSKESIIFGASSVDFSLSGRLLFAGYNDYTINVWDVLKGSRVSILFGHENRVSTLRVSPDGTAFCSGSWDHTLRVWA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.015189873417721518,"disorder_content":0.14177215189873418,"disprot_consensus":{"full":[{"start":1,"end":56,"type":"D"}],"Structural state":[{"start":1,"end":56,"type":"D"}]}},{"disprot_id":"DP04121","acc":"Q5T848","creator":"mgoncalves","date":"2023-05-24T13:41:00.158Z","features":{"pfam":[{"id":"PF00003","name":"7 transmembrane sweet-taste receptor of 3 GCPR","start":413,"end":666},{"id":"PF22572","name":"GPR158/179 extracellular domain","start":264,"end":359}],"gene3D":[]},"genes":[{"name":{"value":"GPR158"},"synonyms":[{"value":"KIAA1136"}]}],"length":1215,"name":"Probable G-protein coupled receptor 158","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":69,"reference_id":"34815401","reference_source":"pmid","reference_html":"Structure of the class C orphan GPCR GPR158 in complex with RGS7-Gβ5. <i> Jeong E, Kim Y, Jeong J, Cho Y. </i> Nat Commun, 2021","date":"2023-06-21T09:43:32.165Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7EWP"},{"db":"EMDB","id":"31360"},{"db":"PDB","id":"7EWR"},{"db":"EMDB","id":"31363"}],"region_id":"DP04121r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P49802"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O14775"}],"statement":[{"text":"The electron microscopy of the class C orphan GPCR GPR158 (Q5T848) in complex with RGS7(P49802)-Gβ5(O14775) shows that this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T12:09:28.773Z"}},{"start":221,"end":260,"reference_id":"34815401","reference_source":"pmid","reference_html":"Structure of the class C orphan GPCR GPR158 in complex with RGS7-Gβ5. <i> Jeong E, Kim Y, Jeong J, Cho Y. </i> Nat Commun, 2021","date":"2023-06-21T09:43:41.543Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7EWP"},{"db":"EMDB","id":"31360"},{"db":"PDB","id":"7EWR"},{"db":"EMDB","id":"31363"}],"region_id":"DP04121r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P49802"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O14775"}],"statement":[{"text":"The electron microscopy of the class C orphan GPCR GPR158 (Q5T848) in complex with RGS7(P49802)-Gβ5(O14775) shows that this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T12:09:30.126Z"}},{"start":362,"end":388,"reference_id":"34815401","reference_source":"pmid","reference_html":"Structure of the class C orphan GPCR GPR158 in complex with RGS7-Gβ5. <i> Jeong E, Kim Y, Jeong J, Cho Y. </i> Nat Commun, 2021","date":"2023-06-21T09:43:10.253Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7EWP"},{"db":"EMDB","id":"31360"},{"db":"PDB","id":"7EWR"},{"db":"EMDB","id":"31363"}],"region_id":"DP04121r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P49802"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O14775"}],"statement":[{"text":"The electron microscopy of the class C orphan GPCR GPR158 (Q5T848) in complex with RGS7(P49802)-Gβ5(O14775) shows that this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T12:09:31.447Z"}},{"start":24,"end":70,"reference_id":"34815401","reference_source":"pmid","reference_html":"Structure of the class C orphan GPCR GPR158 in complex with RGS7-Gβ5. <i> Jeong E, Kim Y, Jeong J, Cho Y. </i> Nat Commun, 2021","date":"2023-06-21T10:40:36.205Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7EWL"},{"db":"EMDB","id":"31351"}],"region_id":"DP04121r004","statement":[{"text":"The electron microscopy of apo GPR158 shows that this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T12:09:35.453Z"}},{"start":221,"end":261,"reference_id":"34815401","reference_source":"pmid","reference_html":"Structure of the class C orphan GPCR GPR158 in complex with RGS7-Gβ5. <i> Jeong E, Kim Y, Jeong J, Cho Y. </i> Nat Commun, 2021","date":"2023-06-21T10:40:23.726Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7EWL"},{"db":"EMDB","id":"31351"}],"region_id":"DP04121r005","statement":[{"text":"The electron microscopy of apo GPR158 shows that this protein region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T12:09:36.643Z"}},{"start":512,"end":524,"reference_id":"34815401","reference_source":"pmid","reference_html":"Structure of the class C orphan GPCR GPR158 in complex with RGS7-Gβ5. <i> Jeong E, Kim Y, Jeong J, Cho Y. </i> Nat Commun, 2021","date":"2023-05-24T14:15:32.560Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7EWL"},{"db":"EMDB","id":"31351"}],"region_id":"DP04121r006","statement":[{"text":"The disordered ICL2 (10 residues) and the cytoplasmic tip of TM3 in apo GPR158 becomes ordered upon binding of RGS7 (Fig. 5b and Supplementary Fig. 9q).","type":"Results"},{"text":"ICL2 residues are described in Fig. 5b.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-13T12:50:27.513Z"}},{"start":512,"end":524,"reference_id":"34815401","reference_source":"pmid","reference_html":"Structure of the class C orphan GPCR GPR158 in complex with RGS7-Gβ5. <i> Jeong E, Kim Y, Jeong J, Cho Y. </i> Nat Commun, 2021","date":"2023-06-21T09:42:52.546Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7EWR"},{"db":"EMDB","id":"31363"}],"region_id":"DP04121r007","statement":[{"text":"The disordered ICL2 (10 residues) and the cytoplasmic tip of TM3 in apo GPR158 becomes ordered upon binding of RGS7 (Fig. 5b and Supplementary Fig. 9q).","type":"Results"},{"text":"ICL2 residues are described in Fig. 5b. ","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P49802"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O14775"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T12:09:39.271Z"}},{"start":512,"end":524,"reference_id":"34815401","reference_source":"pmid","reference_html":"Structure of the class C orphan GPCR GPR158 in complex with RGS7-Gβ5. <i> Jeong E, Kim Y, Jeong J, Cho Y. </i> Nat Commun, 2021","date":"2023-06-21T09:43:21.923Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7EWR"},{"db":"EMDB","id":"31363"},{"db":"PDB","id":"7EWL"},{"db":"EMDB","id":"31351"}],"region_id":"DP04121r008","statement":[{"text":"The disordered ICL2 (10 residues) and the cytoplasmic tip of TM3 in apo GPR158 becomes ordered upon binding of RGS7 (Fig. 5b and Supplementary Fig. 9q).","type":"Results"},{"text":"ICL2 residues are described in Fig. 5b.","type":"Curator statement"}],"states_connection":[{"source":"DP04121r006","target":"DP04121r007"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P49802"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O14775"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T12:09:27.649Z"}},{"start":669,"end":702,"reference_id":"34815401","reference_source":"pmid","reference_html":"Structure of the class C orphan GPCR GPR158 in complex with RGS7-Gβ5. <i> Jeong E, Kim Y, Jeong J, Cho Y. </i> Nat Commun, 2021","date":"2023-06-21T09:42:43.901Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7EWP"},{"db":"EMDB","id":"31360"},{"db":"PDB","id":"7EWR"},{"db":"EMDB","id":"31363"}],"region_id":"DP04121r009","statement":[{"text":"However, most of the cytoplasmic domain of GPR158 (residues 669 to 863) is disordered except for a coiled-coil (Ha and Hb) comprising 61 residues (Supplementary Figs. 4d and 9s).","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P49802"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O14775"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T12:09:40.439Z"}},{"start":764,"end":863,"reference_id":"34815401","reference_source":"pmid","reference_html":"Structure of the class C orphan GPCR GPR158 in complex with RGS7-Gβ5. <i> Jeong E, Kim Y, Jeong J, Cho Y. </i> Nat Commun, 2021","date":"2023-06-21T09:42:30.927Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7EWP"},{"db":"EMDB","id":"31360"},{"db":"PDB","id":"7EWR"},{"db":"EMDB","id":"31363"}],"region_id":"DP04121r010","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P49802"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O14775"}],"statement":[{"text":"However, most of the cytoplasmic domain of GPR158 (residues 669 to 863) is disordered except for a coiled-coil (Ha and Hb) comprising 61 residues (Supplementary Figs. 4d and 9s).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T12:09:44.658Z"}},{"start":669,"end":710,"reference_id":"34815401","reference_source":"pmid","reference_html":"Structure of the class C orphan GPCR GPR158 in complex with RGS7-Gβ5. <i> Jeong E, Kim Y, Jeong J, Cho Y. </i> Nat Commun, 2021","date":"2023-06-21T10:42:05.841Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7EWL"},{"db":"EMDB","id":"31351"}],"region_id":"DP04121r011","statement":[{"text":"Segments lacking regular secondary structures and disordered regions are represented as solid lines and dotted lines, respectively.","type":"Supplementary material"},{"text":"The citation above is available in Supplementary Fig. 4c.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T12:09:49.518Z"}}],"regions_counter":11,"released":"2023_06","sequence":"MGAMAYPLLLCLLLAQLGLGAVGASRDPQGRPDSPRERTPKGKPHAQQPGRASASDSSAPWSRSTDGTILAQKLAEEVPMDVASYLYTGDSHQLKRANCSGRYELAGLPGKWPALASAHPSLHRALDTLTHATNFLNVMLQSNKSREQNLQDDLDWYQALVWSLLEGEPSISRAAITFSTDSLSAPAPQVFLQATREESRILLQDLSSSAPHLANATLETEWFHGLRRKWRPHLHRRGPNQGPRGLGHSWRRKDGLGGDKSHFKWSPPYLECENGSYKPGWLVTLSSAIYGLQPNLVPEFRGVMKVDINLQKVDIDQCSSDGWFSGTHKCHLNNSECMPIKGLGFVLGAYECICKAGFYHPGVLPVNNFRRRGPDQHISGSTKDVSEEAYVCLPCREGCPFCADDSPCFVQEDKYLRLAIISFQALCMLLDFVSMLVVYHFRKAKSIRASGLILLETILFGSLLLYFPVVILYFEPSTFRCILLRWARLLGFATVYGTVTLKLHRVLKVFLSRTAQRIPYMTGGRVMRMLAVILLVVFWFLIGWTSSVCQNLEKQISLIGQGKTSDHLIFNMCLIDRWDYMTAVAEFLFLLWGVYLCYAVRTVPSAFHEPRYMAVAVHNELIISAIFHTIRFVLASRLQSDWMLMLYFAHTHLTVTVTIGLLLIPKFSHSSNNPRDDIATEAYEDELDMGRSGSYLNSSINSAWSEHSLDPEDIRDELKKLYAQLEIYKRKKMITNNPHLQKKRCSKKGLGRSIMRRITEIPETVSRQCSKEDKEGADHGTAKGTALIRKNPPESSGNTGKSKEETLKNRVFSLKKSHSTYDHVRDQTEESSSLPTESQEEETTENSTLESLSGKKLTQKLKEDSEAESTESVPLVCKSASAHNLSSEKKTGHPRTSMLQKSLSVIASAKEKTLGLAGKTQTAGVEERTKSQKPLPKDKETNRNHSNSDNTETKDPAPQNSNPAEEPRKPQKSGIMKQQRVNPTTANSDLNPGTTQMKDNFDIGEVCPWEVYDLTPGPVPSESKVQKHVSIVASEMEKNPTFSLKEKSHHKPKAAEVCQQSNQKRIDKAEVCLWESQGQSILEDEKLLISKTPVLPERAKEENGGQPRAANVCAGQSEELPPKAVASKTENENLNQIGHQEKKTSSSEENVRGSYNSSNNFQQPLTSRAEVCPWEFETPAQPNAGRSVALPASSALSANKIAGPRKEEIWDSFKV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.47983539094650207,"disorder_content":0.2411522633744856,"disprot_consensus":{"full":[{"start":1,"end":70,"type":"D"},{"start":221,"end":261,"type":"D"},{"start":362,"end":388,"type":"D"},{"start":512,"end":524,"type":"T"},{"start":669,"end":710,"type":"D"},{"start":764,"end":863,"type":"D"}],"Structural state":[{"start":1,"end":70,"type":"D"},{"start":221,"end":261,"type":"D"},{"start":362,"end":388,"type":"D"},{"start":512,"end":524,"type":"D"},{"start":669,"end":710,"type":"D"},{"start":764,"end":863,"type":"D"}],"Structural transition":[{"start":512,"end":524,"type":"T"}]}},{"disprot_id":"DP04122","acc":"P93343","creator":"zskalman","date":"2023-05-24T18:07:39.756Z","features":{"pfam":[{"id":"PF00244","name":"14-3-3 protein","start":14,"end":238}],"gene3D":[]},"genes":[],"length":260,"name":"14-3-3-like protein C","ncbi_taxon_id":4097,"organism":"Nicotiana tabacum","regions":[{"start":241,"end":260,"reference_id":"12606564","reference_source":"pmid","reference_html":"Structural view of a fungal toxin acting on a 14-3-3 regulatory complex. <i> Würtele M, Jelich-Ottmann C, Wittinghofer A, Oecking C. </i> EMBO J, 2003","date":"2023-06-14T13:08:13.801Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1O9D"},{"db":"PDB","id":"1O9E"},{"db":"PDB","id":"1O9F"},{"db":"PDB","id":"1O9C"}],"region_id":"DP04122r001","statement":[{"text":"The structure of tobacco 14-3-3c was solved by molecular replacement using phases from human 14-3-3ζ (Liu et al., 1995), and shows 235 from a total of 260 residues.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:311","statements":[{"type":"Curator statement","text":"PDB:1O9C"}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q40409","statements":[{"type":"Curator statement","text":"PDB:1O9D"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:447573","statements":[{"type":"Curator statement","text":"PDB:1O9E and PDB:1O9F."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:31348","statements":[{"type":"Curator statement","text":"PDB:1O9E and PDB:1O9C."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-15T11:07:51.978Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MAVAPTAREENVYMAKLAEQAERYEEMVEFMEKVSNSLGSEELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNEEHVNSIREYRSKIENELSKICDGILKLLDAKLIPSAASGDSKVFYLKMKGDYHRYLAEFKTGAERKEAAESTLTAYKAAQDIATTELAPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAIAELDTLGEESYKDSTLIMQLLRDNLTLWTSDMQDDGADEIKEDPKPDEAKN","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","lamiids","Solanales","Solanaceae","Nicotianoideae","Nicotianeae","Nicotiana"],"alphafold_very_low_content":0.05384615384615385,"disorder_content":0.07692307692307693,"disprot_consensus":{"full":[{"start":241,"end":260,"type":"D"}],"Structural state":[{"start":241,"end":260,"type":"D"}]}},{"disprot_id":"DP04123","acc":"Q5HYA8","creator":"mgoncalves","date":"2023-05-30T15:01:49.577Z","features":{"pfam":[{"id":"PF09773","name":"Meckelin (Transmembrane protein 67)","start":168,"end":995}],"gene3D":[]},"genes":[{"name":{"value":"TMEM67"},"synonyms":[{"value":"MKS3"}]}],"length":995,"name":"Meckelin","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":36,"reference_id":"34731008","reference_source":"pmid","reference_html":"Structure of the human Meckel-Gruber protein Meckelin. <i> Liu D, Qian D, Shen H, Gong D. </i> Sci Adv, 2021","date":"2023-05-30T15:03:56.941Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7FH1"},{"db":"EMDB","id":"31584"}],"region_id":"DP04123r001","statement":[{"text":"The orange dashed line indicates the invisible region in the structure, reflecting flexibility.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-31T14:32:02.175Z"}},{"start":644,"end":665,"reference_id":"34731008","reference_source":"pmid","reference_html":"Structure of the human Meckel-Gruber protein Meckelin. <i> Liu D, Qian D, Shen H, Gong D. </i> Sci Adv, 2021","date":"2023-05-30T15:04:17.701Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7FH1"},{"db":"EMDB","id":"31584"}],"region_id":"DP04123r002","statement":[{"text":"The orange dashed line indicates the invisible region in the structure, reflecting flexibility.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-31T14:32:00.957Z"}},{"start":793,"end":827,"reference_id":"34731008","reference_source":"pmid","reference_html":"Structure of the human Meckel-Gruber protein Meckelin. <i> Liu D, Qian D, Shen H, Gong D. </i> Sci Adv, 2021","date":"2023-05-30T15:04:31.501Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7FH1"},{"db":"EMDB","id":"31584"}],"region_id":"DP04123r003","statement":[{"text":"The orange dashed line indicates the invisible region in the structure, reflecting flexibility.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-31T14:31:59.926Z"}},{"start":849,"end":867,"reference_id":"34731008","reference_source":"pmid","reference_html":"Structure of the human Meckel-Gruber protein Meckelin. <i> Liu D, Qian D, Shen H, Gong D. </i> Sci Adv, 2021","date":"2023-05-30T15:04:57.059Z","curator_id":"mgoncalves","curator_name":"Mariane Goncalves Kulik","curator_orcid":"0009-0000-5432-3524","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_06","version":0,"cross_refs":[{"db":"PDB","id":"7FH1"},{"db":"EMDB","id":"31584"}],"region_id":"DP04123r004","statement":[{"text":"The orange dashed line indicates the invisible region in the structure, reflecting flexibility.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-05-31T14:31:59.652Z"}}],"regions_counter":4,"released":"2023_06","sequence":"MATRGGAGVAMAVWSLLSARAVTAFLLLFLPRFLQAQTFSFPFQQPEKCDNNQYFDISALSCVPCGANQRQDARGTSCVCLPGFQMISNNGGPAIICKKCPENMKGVTEDGWNCISCPSDLTAEGKCHCPIGHILVERDINGTLLSQATCELCDGNENSFMVVNALGDRCVRCEPTFVNTSRSCACSEPNILTGGLCFSSTGNFPLRRISAARYGEVGMSLTSEWFAKYLQSSAAACWVYANLTSCQALGNMCVMNMNSYDFATFDACGLFQFIFENTAGLSTVHSISFWRQNLPWLFYGDQLGLAPQVLSSTSLPTNFSFKGENQNTKLKFVAASYDIRGNFLKWQTLEGGVLQLCPDTETRLNAAYSFGTTYQQNCEIPISKILIDFPTPIFYDVYLEYTDENQHQYILAVPVLNLNLQHNKIFVNQDSNSGKWLLTRRIFLVDAVSGRENDLGTQPRVIRVATQISLSVHLVPNTINGNIYPPLITIAYSDIDIKDANSQSVKVSFSVTYEMDHGEAHVQTDIALGVLGGLAVLASLLKTAGWKRRIGSPMIDLQTVVKFLVYYAGDLANVFFIITVGTGLYWLIFFKAQKSVSVLLPMPIQEERFVTYVGCAFALKALQFLHKLISQITIDVFFIDWERPKGKVLKAVEGEGGVRSATVPVSIWRTYFVANEWNEIQTVRKINSLFQVLTVLFFLEVVGFKNLALMDSSSSLSRNPPSYIAPYSCILRYAVSAALWLAIGIIQVVFFAVFYERFIEDKIRQFVDLCSMSNISVFLLSHKCFGYYIHGRSVHGHADTNMEEMNMNLKREAENLCSQRGLVPNTDGQTFEIAISNQMRQHYDRIHETLIRKNGPARLLSSSASTFEQSIKAYHMMNKFLGSFIDHVHKEMDYFIKDKLLLERILGMEFMEPMEKSIFYNDEGYSFSSVLYYGNEATLLIFDLLFFCVVDLACQNFILASFLTYLQQEIFRYIRNTVGQKNLASKTLVDQRFLI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"alphafold_very_low_content":0.035175879396984924,"disorder_content":0.11256281407035176,"disprot_consensus":{"full":[{"start":1,"end":36,"type":"D"},{"start":644,"end":665,"type":"D"},{"start":793,"end":827,"type":"D"},{"start":849,"end":867,"type":"D"}],"Structural state":[{"start":1,"end":36,"type":"D"},{"start":644,"end":665,"type":"D"},{"start":793,"end":827,"type":"D"},{"start":849,"end":867,"type":"D"}]}},{"disprot_id":"DP04124","acc":"C1JEX5","creator":"cpintado","date":"2023-07-11T15:51:36.294Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"RAP1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ACM24769.1","url":"https://www.ebi.ac.uk/ena/browser/view/ACM24769.1"}}]}}],"length":855,"name":"Repressor activator protein 1","ncbi_taxon_id":5702,"organism":"Trypanosoma brucei brucei","regions":[{"start":734,"end":761,"reference_id":"36949076","reference_source":"pmid","reference_html":"The RRM-mediated RNA binding activity in T. brucei RAP1 is essential for VSG monoallelic expression. <i> Gaurav AK, Afrin M, Yang X, Saha A, Sayeed SKA, Pan X, Ji Z, Wong KB, Zhang M, Zhao Y, Li B. </i> Nat Commun, 2023","date":"2023-07-11T15:54:20.174Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7XRW"}],"region_id":"DP04124r001","statement":[{"text":"The DB domain (aa 734–761) at the C-terminus of TbRAP1639-761 forms a long and flexible loop (Supplementary Fig. 1b, left).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-13T15:25:48.057Z"}}],"regions_counter":1,"released":"2023_12","sequence":"MTDVDGGSGASWKRLRFFVCADTLLTFQPVDSSHLEGRPGQPEQRYLLVDGEYRPITSYPTSSLFLETLKLAGSTVVVIAPWKRAKTKKLLSLFGWTAFDEIRSIHPEPGRDKLHLACIGCSADEYSTSVIVATSRADWSPSMYPQLVEVKHGVNQVPHSLALLRALSSCLRLAEWQVRLPHVPISSCATLCRSRLFSHCRFFLEPVASEDATVALSINEHGGYIVTRREDATHCVVSGSLPNLPGDISNLPPGGCAAKAVKECSVLPTSAEGRSAEPKSAKVDTDSVSLVKNQVDESDDSIKDEFSYSAGNAATAMVECGDEGVWNEENADDEDPVTMIPPGTFSEDDEDDAPGGLEEADGETVTTVTTQWLKDCAEGLFMYPPQVSHTSKDGSDWNITGLLLATILPTSDAEPLLLSSFNTFAERSGFEPLQLNSADEGGLAEVMQRQWGGVLCMEEKDGDFLLSQTNIYTEAFSDEMDKHLTFVANRFCEAWKDAVQRRRALLGSDAGTQTTVSITVTFGTNTEVEVAPSVQPPPPPPPAPQPTTASAAANEGSKESATPALPFLMRALGPAEWAKEVEAPRSPPPSAVPDIPLKQDPVPSGEGVATAENSVGNDQKESTSRQVAGDAGDTANVAEATEEIAALDQPFEKCFIPTEALGSDREGLDRTQLERQLPFRNYPIKLNVSKSGIFCQFPTVSDAKRFYEEGTVEILNRSLPIKPVFEKRNETVAPAERKRRRSVSPGGVHPQTAAVSALSRRGIQGATYARTQRSRTDNGWKAEGDRNPFVLTEEENSLLTSLGITYTYALENVPLLEHYAQKDLSSKVYRKEKGVLVKMLEKLKAVKGTTSKAPQ","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Trypanosoma"],"alphafold_very_low_content":0.4502923976608187,"dataset":["Neglected tropical diseases proteins"],"disorder_content":0.03274853801169591,"disprot_consensus":{"full":[{"start":734,"end":761,"type":"D"}],"Structural state":[{"start":734,"end":761,"type":"D"}]}},{"disprot_id":"DP04125","acc":"P06702","creator":"cpintado","date":"2023-07-14T14:39:26.433Z","features":{"pfam":[{"id":"PF01023","name":"S-100/ICaBP type calcium binding domain","start":8,"end":51}],"gene3D":[]},"genes":[{"name":{"value":"S100A9","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12626582","url":"http://www.ncbi.nlm.nih.gov/pubmed/12626582","alternativeUrl":"https://europepmc.org/abstract/MED/12626582"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:10499","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:10499"}}]},"synonyms":[{"value":"CAGB"},{"value":"CFAG"},{"value":"MRP14","evidences":[{"code":"ECO:0000303","source":{"name":"Citation","id":"Ref.4","url":"https://www.uniprot.org/uniprot/null#ref4"}}]}]}],"length":114,"name":"Protein S100-A9","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":87,"end":114,"reference_id":"36194634","reference_source":"pmid","reference_html":"Evolution avoids a pathological stabilizing interaction in the immune protein S100A9. <i> Harman JL, Reardon PN, Costello SM, Warren GD, Phillips SR, Connor PJ, Marqusee S, Harms MJ. </i> Proc Natl Acad Sci U S A, 2022","date":"2023-07-14T15:31:14.602Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7UI5"}],"region_id":"DP04125r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:271"}],"statement":[{"text":"The majority of unassigned peaks are within the S100A9 disordered C-terminal tail, most of which are also unassigned in the wild-type hS100A9 structure (27).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-17T15:36:34.828Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MTCKMSQLERNIETIINTFHQYSVKLGHPDTLNQGEFKELVRKDLQNFLKKENKNEKVIEHIMEDLDTNADKQLSFEEFIMLMARLTWASHEKMHEGDEGPGHHHKPGLGEGTP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.008771929824561403,"dataset":["Extracellular matrix proteins"],"disorder_content":0.24561403508771928,"disprot_consensus":{"full":[{"start":87,"end":114,"type":"D"}],"Structural state":[{"start":87,"end":114,"type":"D"}]}},{"disprot_id":"DP04126","acc":"P95493","creator":"cpintado","date":"2023-07-17T09:46:29.160Z","features":{"pfam":[{"id":"PF01364","name":"Peptidase family C25","start":236,"end":575},{"id":"PF03785","name":"Peptidase family C25, C terminal ig-like domain","start":586,"end":661},{"id":"PF08126","name":"Propeptide_C25","start":25,"end":222},{"id":"PF18630","name":"Peptidase M60 C-terminal domain","start":673,"end":730}],"gene3D":[]},"genes":[{"name":{"value":"rgpB"},"synonyms":[{"value":"prtRII"},{"value":"rgp2"}],"olnNames":[{"value":"PG_0506"}]}],"length":736,"name":"Gingipain R2","ncbi_taxon_id":242619,"organism":"Porphyromonas gingivalis (strain ATCC BAA-308 / W83)","regions":[{"start":662,"end":673,"reference_id":"36404438","reference_source":"pmid","reference_html":"Structural Model of a Porphyromonas gingivalis type IX Secretion System Shuttle Complex. <i> Dorgan B, Liu Y, Wang S, Aduse-Opoku J, Whittaker SB, Roberts MAJ, Lorenz CD, Curtis MA, Garnett JA. </i> J Mol Biol, 2022","date":"2023-07-17T09:50:15.536Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"7PQ4"}],"region_id":"DP04126r001","statement":[{"text":"A single NMR structure of RgpB-CTD (residues 674–736) was used as the starting model, with the N-terminal 15 residue His-tag and RgpB-CTD residues 662–673 kept unstructured. ","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-17T15:42:40.649Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MKKNFSRIVSIVAFSSLLGGMAFAQPAERGRNPQVRLLSAEQSMSKVQFRMDNLQFTGVQTSKGVAQVPTFTEGVNISEKGTPILPILSRSLAVSETRAMKVEVVSSKFIEKKDVLIAPSKGVISRAENPDQIPYVYGQSYNEDKFFPGEIATLSDPFILRDVRGQVVNFAPLQYNPVTKTLRIYTEIVVAVSETAEAGQNTISLVKNSTFTGFEDIYKSVFMNYEATRYTPVEEKENGRMIVIVPKKYEEDIEDFVDWKNQRGLRTEVKVAEDIASPVTANAIQQFVKQEYEKEGNDLTYVLLVGDHKDIPAKITPGIKSDQVYGQIVGNDHYNEVFIGRFSCESKEDLKTQIDRTIHYERNITTEDKWLGQALCIASAEGGPSADNGESDIQHENIIANLLTQYGYTKIIKCYDPGVTPKNIIDAFNGGISLANYTGHGSETAWGTSHFGTTHVKQLTNSNQLPFIFDVACVNGDFLYNVPCFAEALMRAQKDGKPTGTVAIIASTINQSWASPMRGQDEMNEILCEKHPNNIKRTFGGVTMNGMFAMVEKYKKDGEKMLDTWTVFGDPSLLVRTLVPTKMQVTAPANISASAQTFEVACDYNGAIATLSDDGDMVGTAIVKDGKAIIKLNESIADETNLTLTVVGYNKVTVIKDVKVEGTSIADVANDKPYTVAVSGKTITVESPAAGLTIFDMNGRRVATAKNRMVFEAQNGVYAVRIATEGKTYTEKVIVK","taxonomy":["Bacteria","Bacteroidota","Bacteroidia","Bacteroidales","Porphyromonadaceae","Porphyromonas"],"alphafold_very_low_content":0.06114130434782609,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.016304347826086956,"disprot_consensus":{"full":[{"start":662,"end":673,"type":"D"}],"Structural state":[{"start":662,"end":673,"type":"D"}]}},{"disprot_id":"DP04127","acc":"W1QJK4","creator":"cpintado","date":"2023-07-17T14:40:03.237Z","features":{"pfam":[{"id":"PF10341","name":"Shelterin complex subunit, TPP1/ACD","start":36,"end":148}],"gene3D":[]},"genes":[{"orfNames":[{"value":"HPODL_02192","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ESX02878.1","url":"https://www.ebi.ac.uk/ena/browser/view/ESX02878.1"}}]}]}],"length":175,"name":"Telomere replication protein EST3","ncbi_taxon_id":871575,"organism":"Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1)","regions":[{"start":1,"end":19,"reference_id":"32632130","reference_source":"pmid","reference_html":"Insights into the structure and function of Est3 from the Hansenula polymorpha telomerase. <i> Shepelev NM, Mariasina SS, Mantsyzov AB, Malyavko AN, Efimov SV, Petrova OA, Rodina EV, Zvereva MI, Dontsova OA, Polshakov VI. </i> Sci Rep, 2020","date":"2023-07-17T14:44:25.034Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6Q44"}],"region_id":"DP04127r001","statement":[{"text":"The protein consists of the structured β-barrel core (residues 22–172) and disordered N and C-terminal tails (residues 1–22 and 173–178) (see Fig. 3b). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-17T15:55:41.922Z"}},{"start":47,"end":56,"reference_id":"32632130","reference_source":"pmid","reference_html":"Insights into the structure and function of Est3 from the Hansenula polymorpha telomerase. <i> Shepelev NM, Mariasina SS, Mantsyzov AB, Malyavko AN, Efimov SV, Petrova OA, Rodina EV, Zvereva MI, Dontsova OA, Polshakov VI. </i> Sci Rep, 2020","date":"2023-07-18T09:31:23.348Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6Q44"}],"region_id":"DP04127r002","statement":[{"text":"There are several loops which have increased internal mobility in the ps-ns time scale (Fig. 5a). Among them are the loop L12 (residues 50–59), the loop L45, which separates helix α4 and strand β5 (residues 118–131), and the residues 144–161 between strand β5 and helix α6, including helix α5 in the middle (see Fig. 4d).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-18T12:25:48.052Z"}},{"start":115,"end":128,"reference_id":"32632130","reference_source":"pmid","reference_html":"Insights into the structure and function of Est3 from the Hansenula polymorpha telomerase. <i> Shepelev NM, Mariasina SS, Mantsyzov AB, Malyavko AN, Efimov SV, Petrova OA, Rodina EV, Zvereva MI, Dontsova OA, Polshakov VI. </i> Sci Rep, 2020","date":"2023-07-18T09:32:02.948Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6Q44"}],"region_id":"DP04127r003","statement":[{"text":"There are several loops which have increased internal mobility in the ps-ns time scale (Fig. 5a). Among them are the loop L12 (residues 50–59), the loop L45, which separates helix α4 and strand β5 (residues 118–131), and the residues 144–161 between strand β5 and helix α6, including helix α5 in the middle (see Fig. 4d).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-18T12:25:48.364Z"}},{"start":141,"end":158,"reference_id":"32632130","reference_source":"pmid","reference_html":"Insights into the structure and function of Est3 from the Hansenula polymorpha telomerase. <i> Shepelev NM, Mariasina SS, Mantsyzov AB, Malyavko AN, Efimov SV, Petrova OA, Rodina EV, Zvereva MI, Dontsova OA, Polshakov VI. </i> Sci Rep, 2020","date":"2023-07-18T09:32:20.512Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6Q44"}],"region_id":"DP04127r004","statement":[{"text":"There are several loops which have increased internal mobility in the ps-ns time scale (Fig. 5a). Among them are the loop L12 (residues 50–59), the loop L45, which separates helix α4 and strand β5 (residues 118–131), and the residues 144–161 between strand β5 and helix α6, including helix α5 in the middle (see Fig. 4d).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-18T12:25:49.565Z"}},{"start":141,"end":158,"reference_id":"32632130","reference_source":"pmid","reference_html":"Insights into the structure and function of Est3 from the Hansenula polymorpha telomerase. <i> Shepelev NM, Mariasina SS, Mantsyzov AB, Malyavko AN, Efimov SV, Petrova OA, Rodina EV, Zvereva MI, Dontsova OA, Polshakov VI. </i> Sci Rep, 2020","date":"2023-07-18T09:34:19.651Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6Q44"}],"region_id":"DP04127r005","statement":[{"text":"There are several loops which have increased internal mobility in the ps-ns time scale (Fig. 5a). Among them are the loop L12 (residues 50–59), the loop L45, which separates helix α4 and strand β5 (residues 118–131), and the residues 144–161 between strand β5 and helix α6, including helix α5 in the middle (see Fig. 4d).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-18T12:26:41.202Z"}},{"start":115,"end":128,"reference_id":"32632130","reference_source":"pmid","reference_html":"Insights into the structure and function of Est3 from the Hansenula polymorpha telomerase. <i> Shepelev NM, Mariasina SS, Mantsyzov AB, Malyavko AN, Efimov SV, Petrova OA, Rodina EV, Zvereva MI, Dontsova OA, Polshakov VI. </i> Sci Rep, 2020","date":"2023-07-18T09:34:33.243Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6Q44"}],"region_id":"DP04127r006","statement":[{"text":"There are several loops which have increased internal mobility in the ps-ns time scale (Fig. 5a). Among them are the loop L12 (residues 50–59), the loop L45, which separates helix α4 and strand β5 (residues 118–131), and the residues 144–161 between strand β5 and helix α6, including helix α5 in the middle (see Fig. 4d).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-18T12:26:35.894Z"}},{"start":47,"end":56,"reference_id":"32632130","reference_source":"pmid","reference_html":"Insights into the structure and function of Est3 from the Hansenula polymorpha telomerase. <i> Shepelev NM, Mariasina SS, Mantsyzov AB, Malyavko AN, Efimov SV, Petrova OA, Rodina EV, Zvereva MI, Dontsova OA, Polshakov VI. </i> Sci Rep, 2020","date":"2023-07-18T09:34:55.978Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6Q44"}],"region_id":"DP04127r007","statement":[{"text":"There are several loops which have increased internal mobility in the ps-ns time scale (Fig. 5a). Among them are the loop L12 (residues 50–59), the loop L45, which separates helix α4 and strand β5 (residues 118–131), and the residues 144–161 between strand β5 and helix α6, including helix α5 in the middle (see Fig. 4d).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-18T12:25:53.294Z"}}],"regions_counter":7,"released":"2024_06","sequence":"MPPSSRDAVRVTASAHMKHWLEPVLCEAGLGHNYKVDKVLKVLRIYPRSNTLSSLPLCLCDANYKILAFANYKAIAAFERKERRRVTQNLLNSEIMIHSFTIRFYNDDQVQGFFDGLKFKQKASLFPGYLVLEINDFSMFNRDQLILSNAGTIEFLYGTPRYIARFIEQEFSDEE","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Pichiaceae","Ogataea"],"alphafold_very_low_content":0.08571428571428572,"disorder_content":0.3485714285714286,"disprot_consensus":{"full":[{"start":1,"end":19,"type":"D"},{"start":47,"end":56,"type":"D"},{"start":115,"end":128,"type":"D"},{"start":141,"end":158,"type":"D"}],"Structural state":[{"start":1,"end":19,"type":"D"},{"start":47,"end":56,"type":"D"},{"start":115,"end":128,"type":"D"},{"start":141,"end":158,"type":"D"}],"Disorder function":[{"start":47,"end":56,"type":"F"},{"start":115,"end":128,"type":"F"},{"start":141,"end":158,"type":"F"}]}},{"disprot_id":"DP04128","acc":"P15126","creator":"vnugnes","date":"2023-07-17T14:55:33.664Z","features":{"pfam":[{"id":"PF14204","name":"Ribosomal L18 C-terminal region","start":236,"end":289},{"id":"PF17144","name":"Ribosomal large subunit proteins 60S L5, and 50S L18","start":14,"end":176}],"gene3D":[]},"genes":[{"name":{"value":"rpl5-b"}}],"length":296,"name":"Large ribosomal subunit protein uL18B","ncbi_taxon_id":8355,"organism":"Xenopus laevis","regions":[{"start":1,"end":43,"reference_id":"12860121","reference_source":"pmid","reference_html":"Mutual induced fit binding of Xenopus ribosomal protein L5 to 5S rRNA. <i> DiNitto JP, Huber PW. </i> J Mol Biol, 2003","date":"2023-07-17T15:05:19.096Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04128r001","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS000025A4B6_8355"}],"statement":[{"text":"The extreme sensitivity of the N-terminal region of L5 (up to residue 44) in the 5 S RNP complex to chymotrypsin indicates that the predicted disorder in this region of L5 persists when the protein is bound to 5 S rRNA.","type":"Results"}]}],"regions_counter":1,"released":"2024_06","sequence":"MGFVKVVKNKAYFKRYQVKFRRRREGKTDYYARKRLVIQDKNKYNTPKYRMIVRVTNRDIICQIAYARIEGDMIVCAAYAHELPKYGVKVGLTNYAAAYCTGLLLARRLLNKFGLDKVYEGQVEVTGDEYNVESVDGEPGAFTCYLDAGLTRTTTGNKVFGALKGAVDGGLSIPHSTKRFPGYDSESKEFNPEVHRKHIFAQNIAEYMRLLMEEDEDAYKKQFSQYIKNGVAADQLEDIYKKAHAGIRENPVHEKKPKKEVKKKRWNRAKLSLEQKKDRVAQKKASFLRAQEKADS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Amphibia","Batrachia","Anura","Pipoidea","Pipidae","Xenopodinae","Xenopus","Xenopus"],"alphafold_very_low_content":0,"dataset":["RNA-binding proteins"],"disorder_content":0.14527027027027026,"disprot_consensus":{"full":[{"start":1,"end":43,"type":"D"}],"Structural state":[{"start":1,"end":43,"type":"D"}]}},{"disprot_id":"DP04129","acc":"P42858","creator":"tlazar","date":"2023-07-17T17:51:47.999Z","features":{"pfam":[{"id":"PF12372","name":"Huntingtin, N-terminal HEAT","start":756,"end":1631},{"id":"PF20925","name":"Huntingtin, bridge","start":1785,"end":2062},{"id":"PF20926","name":"Huntingtin, N-terminal HEAT 1","start":132,"end":282},{"id":"PF20927","name":"Huntingtin, C-terminal HEAT","start":2092,"end":3098}],"gene3D":[]},"genes":[{"name":{"value":"HTT"},"synonyms":[{"value":"HD"},{"value":"IT15"}]}],"length":3142,"name":"Huntingtin","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":17,"reference_id":"19270701","reference_source":"pmid","reference_html":"Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism. <i> Thakur AK, Jayaraman M, Mishra R, Thakur M, Chellgren VM, Byeon IJ, Anjum DH, Kodali R, Creamer TP, Conway JF, Gronenborn AM, Wetzel R. </i> Nat Struct Mol Biol, 2009","date":"2023-07-17T21:44:47.352Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r001","statement":[{"text":"The CD spectrum of httNT at 35 °C (Fig. 4A) and the 35 °C – 5 °C difference spectrum (not shown) lack strong secondary structure features, suggesting the absence of a stable structure. At the same time, deconvolution analysis of the 35 °C spectrum predicts significant α-helix (see legend, Fig. 4), consistent with projections based on amino acid sequence 23,35.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-19T15:58:39.909Z"}},{"start":1,"end":17,"reference_id":"19270701","reference_source":"pmid","reference_html":"Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism. <i> Thakur AK, Jayaraman M, Mishra R, Thakur M, Chellgren VM, Byeon IJ, Anjum DH, Kodali R, Creamer TP, Conway JF, Gronenborn AM, Wetzel R. </i> Nat Struct Mol Biol, 2009","date":"2023-07-17T21:48:23.952Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r002","statement":[{"text":"The CD dichotomy was clarified by high resolution NMR analysis (Fig. 5), which strongly suggests the absence of stably folded structure. Two-dimensional proton TOCSY and NOESY NMR analyses show that httNT adopts predominantly unfolded, random-coil conformations, characterized by small spectral dispersion, small secondary chemical shifts, and strong sequential Hα(i)-HN(i+1) NOEs with few sequential HN(i)-HN(i+1) or medium-range NOEs.","type":"Results"},{"text":"Despite this slight propensity, there is clearly no stable α-helix in this peptide in solution under physiological conditions. Thus, in the absence of an expanded polyQ, httNT adopts a conformation lacking significant secondary and tertiary structural features, while at the same time being in a collapsed state.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-19T15:58:52.760Z"}},{"start":19,"end":29,"reference_id":"19748341","reference_source":"pmid","reference_html":"Secondary structure of Huntingtin amino-terminal region. <i> Kim MW, Chelliah Y, Kim SW, Otwinowski Z, Bezprozvanny I. </i> Structure, 2009","date":"2023-08-09T09:32:03.690Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"3IOR"}],"region_id":"DP04129r003","statement":[{"text":"The unstructured random coil portion of polyQ region (Gln389-Gln399) is shown on Fig 1d as a striped orange loop. The remaining carboxy-terminal polyQ region (Gln400-Gln404) is resolved in the extended loop conformation (Orange stick model).","type":"Results"},{"text":"(d) The complete structure of B molecule of Htt17Q-EX1 monomer from c95 crystal. The striped orange loops are for the random coil region between Gln389 and Gln399, which is invisible on the map.","type":"Figure"}],"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Figure","text":"Figure 1. Secondary Structure of Htt17Q-EX1\n(A) Amino acid sequence of MBP-Htt17Q-EX1. MBP3A denotes the maltose binding protein followed by a 3Ala linker. M371 to Q430 is the sequence of Htt17Q- EX1, which is subdivided into a 17 aa N-terminal region (M371 to F387), poly17Q region (Q388 to Q404), poly11P region (P405 to P415), and 15 aa mixed P/Q region (Q416 to Q430). The sequence from Q431 to the C terminus is the 19 aa tag added to facilitate crystallization."}]},{"term_id":"IDPO:00483","term_name":"insertion","term_namespace":"Protein mutation","value":"p.Gln64_Pro65insGlnSerTyrGlnIleThrAlaGlyLysLeuGlyThrGlyArgArgPheThrThrSer","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Following Gln430 in the MBP-Htt17Q-EX1 sequence, the 19 aa carboxy-terminal (C-terminal) tag (QSYQITAGKLGTGRRFTTS) was added to facilitate crystallization."}]}],"sequence_construct":"KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAALAAAQTNAAAMATLEKLMKAFESLKSFQQQQQQQQQQQQQQQQQPPPPPPPPPPPQLPQPPPQAQPLLPQQSYQITAGKLGTGRRFTTS","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-14T15:21:07.026Z"}},{"start":1,"end":34,"reference_id":"28085263","reference_source":"pmid","reference_html":"Structure and Dynamics of the Huntingtin Exon-1 N-Terminus: A Solution NMR Perspective. <i> Baias M, Smith PE, Shen K, Joachimiak LA, Żerko S, Koźmiński W, Frydman J, Frydman L. </i> J Am Chem Soc, 2017","date":"2023-08-25T12:04:50.634Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r004","statement":[{"text":"The availability of 1H, 15N, and 13C chemical shifts for various residues enables one to estimate the fractional populations of secondary structural elements in N17Q17. This analysis was initially accomplished using the Secondary Structure Propensity (SSP) program (68) with the 13C chemical shift values identified for the Cα and Cβ sites of the various residues as inputs, as it has been demonstrated before that these chemical shifts are more relevant for predicting secondary structure propensities of intrinsically disordered proteins.","type":"Results"},{"text":"At low pH, the N17Q17 ensemble of conformers exhibits a clear propensity for α-helical structures forming in the central region of the peptide. This trend changes as pH increases, culminating with a structurally disordered structure—even one exhibiting slight β-sheet propensity—at physiological pH.","type":"Results"},{"text":"To this end, the 13CO, 13Cα, and 13Cβ chemical shifts extracted from 3D BEST NMR experiments at low and neutral pH were fed into CS-ROSETTA; Figure 8 shows the lowest score structures that emerge from this program. As had been observed using SSP and PONDR, this approach also reveals a low pH α-helical structure in the core region of the peptide, between residues Leu14 and Gln26 (Figure 8a). Also in agreement with the SSP and PONDR calculations, CS-ROSETTA shows that N17 helicity is lost when moving to neutral pH, where two separate sets of CS-ROSETTA simulations reveal disordered, coiled conformations for the entire peptide (Figure 8b).","type":"Results"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Figure","text":"Figure 1. Exon 1 fragment of huntingtin containing the entire N17 domain, a polyQ tract with 17 glutamines, a short polyproline region and an LEC linker before the hexahistidine tag at the C-terminus."}]},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gln35_Gln38del","start":null,"end":null,"position":null,"statements":[{"type":"Figure","text":"Figure 1. Exon 1 fragment of huntingtin containing the entire N17 domain, a polyQ tract with 17 glutamines, a short polyproline region and an LEC linker before the hexahistidine tag at the C-terminus."}]}],"cross_refs":[{"db":"BMRB","id":"26965"}],"sequence_construct":"MATLEKLMKAFESLKSFQQQQQQQQQQQQQQQQQPPPPPPLECHHHHHH","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-25T14:46:31.762Z"}},{"start":1,"end":17,"reference_id":"20026071","reference_source":"pmid","reference_html":"Modulation of polyglutamine conformations and dimer formation by the N-terminus of huntingtin. <i> Williamson TE, Vitalis A, Crick SL, Pappu RV. </i> J Mol Biol, 2010","date":"2023-07-18T10:10:31.243Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r005","statement":[{"text":"The results presented above provide support for the hypothesis that Ac-Nt17-QN-Nme peptides become disordered as polyglutamine length increases. Before moving on to further analysis of the conformational characteristics and intermolecular associations of these constructs, we present an experimental assessment of α-helical content. We performed UV circular dichroism (CD) measurements on the Nt17 peptide and compared the estimates obtained from these experiments to those presented in Fig. 1a.","type":"Results"},{"text":"We conclude that 34% is a reasonable estimate of the helical content for the Nt17 peptide in aqueous solution at 298 K.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-31T16:01:16.281Z"}},{"start":39,"end":88,"reference_id":"28937758","reference_source":"pmid","reference_html":"Monomeric Huntingtin Exon 1 Has Similar Overall Structural Features for Wild-Type and Pathological Polyglutamine Lengths. <i> Warner JB, Ruff KM, Tan PS, Lemke EA, Pappu RV, Lashuel HA. </i> J Am Chem Soc, 2017","date":"2023-07-18T11:19:41.927Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r006","statement":[{"text":"We find that the relative error in the calculated ⟨EFRET⟩ values increases with increasing sequence separation of dyes. The relative errors are as high as 13%. Comparatively, a protein that is uniformly expanded shows a mean relative error that is typically less than 4%. (33) These results suggest that the scaling determined from the A60C dye pair underestimates the distance between dyes for the remaining dye pairs, and this underestimation increases for longer sequence separations. Such a result is consistent with the N-terminus being more compact than the C-terminus of Httex1, as would be expected if the polyQ domain adopts compact conformations, whereas the PR domain adopts expanded conformations.","type":"Results"},{"text":"(1) the general distance preferences are conserved across polyQ repeat lengths and dye positions; (2) the combination of Nt17 and polyQ domains adopt compact conformations as highlighted by small values for average distances between all pairs of residues within these domains; and (3) the PR domain predominantly adopts extended conformations, although there is a minor, temperature-dependent population characterized mainly by contacts between the flexible linker between polyproline modules of the PR domain and the surface of the polyQ domain (Supporting Information, Figure S6). Overall, these features suggest that Httex1 constructs adopt tadpole-like conformations for all polyQ repeat lengths. The tadpole-like architecture is defined by a globular “head”, consisting of Nt17 adsorbed to polyQ, and a semi-flexible “tail”, which refers to the PR domain.","type":"Results"},{"text":"(o) Two-dimensional histogram of Rg/N1/3 and δ for the polyQ-PR domains of Httex1 49Q. The red rectangle corresponds to the region that corresponds to globular conformations as defined above. For all polyQ lengths the probability of polyQ-PR domains adopting globular conformations is negligible.","type":"Figure"},{"text":"We performed a similar analysis over polyQ-PR domains and found that for all polyQ lengths and dye pairs a negligible percentage of the conformations were observed to be globular. An example, two-dimensional histogram of Httex1 49Q is shown in Figure 4o. Most of the density was observed outside the region that corresponds to globular conformations.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-31T16:17:14.846Z"}},{"start":1,"end":38,"reference_id":"28937758","reference_source":"pmid","reference_html":"Monomeric Huntingtin Exon 1 Has Similar Overall Structural Features for Wild-Type and Pathological Polyglutamine Lengths. <i> Warner JB, Ruff KM, Tan PS, Lemke EA, Pappu RV, Lashuel HA. </i> J Am Chem Soc, 2017","date":"2023-08-09T09:37:55.577Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r007","statement":[{"text":"We find that the relative error in the calculated ⟨EFRET⟩ values increases with increasing sequence separation of dyes. The relative errors are as high as 13%. Comparatively, a protein that is uniformly expanded shows a mean relative error that is typically less than 4%. (33) These results suggest that the scaling determined from the A60C dye pair underestimates the distance between dyes for the remaining dye pairs, and this underestimation increases for longer sequence separations. Such a result is consistent with the N-terminus being more compact than the C-terminus of Httex1, as would be expected if the polyQ domain adopts compact conformations, whereas the PR domain adopts expanded conformations.","type":"Results"},{"text":"(1) the general distance preferences are conserved across polyQ repeat lengths and dye positions; (2) the combination of Nt17 and polyQ domains adopt compact conformations as highlighted by small values for average distances between all pairs of residues within these domains; and (3) the PR domain predominantly adopts extended conformations, although there is a minor, temperature-dependent population characterized mainly by contacts between the flexible linker between polyproline modules of the PR domain and the surface of the polyQ domain (Supporting Information, Figure S6). Overall, these features suggest that Httex1 constructs adopt tadpole-like conformations for all polyQ repeat lengths. The tadpole-like architecture is defined by a globular “head”, consisting of Nt17 adsorbed to polyQ, and a semi-flexible “tail”, which refers to the PR domain.","type":"Results"},{"text":"Figure 4m shows the results of the least-squares regression analysis for ln(N) versus ln(⟨Rg⟩). The parameters for the slope and intercept, obtained from the regression analysis, are found to be 0.36 and 2.62 Å, respectively. This implies that the polyQ domain maintains its intrinsic preference for globular conformations in the context of Httex1. These globular conformations are likely to be more stable as polyQ length increases because the surface-to-volume ratio decreases as N–1/3 as N increases.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-14T15:22:08.038Z"}},{"start":1,"end":90,"reference_id":"29627459","reference_source":"pmid","reference_html":"Tadpole-like Conformations of Huntingtin Exon 1 Are Characterized by Conformational Heterogeneity that Persists regardless of Polyglutamine Length. <i> Newcombe EA, Ruff KM, Sethi A, Ormsby AR, Ramdzan YM, Fox A, Purcell AW, Gooley PR, Pappu RV, Hatters DM. </i> J Mol Biol, 2018","date":"2023-08-09T09:42:40.012Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r008","statement":[{"text":"The 25Q form of Httex1 lacks persistent protection from exchange by NMR at pH 7.5, suggesting an absence of persistent hydrogen bonds (Fig. S2).","type":"Results"},{"text":"Fig. 2. Httex1 lacks persistent hydrogen bonding with 25Q or 46Q. (a) 1H,15N HSQC of Httex1 25Q protein fragment in H2O versus D2O-based sodium acetate buffer (150 mM; pH 4).","type":"Figure"},{"text":" The first four residues within Httex1 have negative NOE values, which is consistent with high mobility of the N-terminus (Fig. 3c). The next 13 acids N-terminal to the polyQ region as well as the arc of glutamine backbone resonances displayed positive NOE values mostly between 0.4 and 0.6. The C-terminal proline-rich region shows 15N{1H}-NOE values that are < 0.4. These observations suggest that, while the N17 and polyQ tract are not ordered in the canonical sense, there is a persistent preference for conformational rigidity implying low-amplitude conformational fluctuations, especially within the N17 and polyQ regions.","type":"Results"},{"text":"Analysis of the smoothed ΔCα–ΔCβ values [40] indicated localized regions of distinct secondary structure (values ≥ 1) and regions lacking stable structure but with a tendency toward some α-helical structure throughout the N-terminal and polyQ regions of Httex1 (Fig. 3b) [39], [40], [41]. This result is consistent with findings that portions of the polyQ region are able to form α-helices [20], [42], [43].","type":"Results"},{"text":"The C-terminal sequence displayed clear preferences for extended structures (Fig. 3b). Overall, these results suggest that Httex1 adopts a heterogeneous ensemble of conformations with localized preferences for specific secondary structure motifs.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00483","term_name":"insertion","term_namespace":"Protein mutation","value":"p.Gln38_Pro39insGlnGlnGlnGln","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"The 25Q form of Httex1 lacks persistent protection from exchange by NMR at pH 7.5, suggesting an absence of persistent hydrogen bonds (Fig. S2)."}]}],"cross_refs":[{"db":"BMRB","id":"27161"}],"sequence_construct":"GHMATLEKLMKAFESLKSFQQQQQQQQQQQQQQQQQQQQQQQQQPPPPPPPPPPPQLPQPPPQAQPLLPQPQPPPPPPPPPPGPAVAEEPLHRPKKW","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-14T15:22:43.296Z"}},{"start":1,"end":90,"reference_id":"29627459","reference_source":"pmid","reference_html":"Tadpole-like Conformations of Huntingtin Exon 1 Are Characterized by Conformational Heterogeneity that Persists regardless of Polyglutamine Length. <i> Newcombe EA, Ruff KM, Sethi A, Ormsby AR, Ramdzan YM, Fox A, Purcell AW, Gooley PR, Pappu RV, Hatters DM. </i> J Mol Biol, 2018","date":"2023-08-09T09:45:32.828Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r009","statement":[{"text":"Fig. 2. Httex1 lacks persistent hydrogen bonding with 25Q or 46Q. (a) 1H,15N HSQC of Httex1 25Q protein fragment in H2O versus D2O-based sodium acetate buffer (150 mM; pH 4). Labeled residues are observed after HDX. (b) HDX of Httex1 25Q and 46Q were measured over 10 min using MS at both pH 7.5 and pH 4. Exchange plateaued at ~ 80% (due to back-exchange in the protonated solvent during chromatography separation prior to MS).","type":"Figure"},{"text":"Given that the HDX-MS results for both 25Q and 46Q forms imply a lack of stable hydrogen bonding, we focused on the 25Q variant for the remainder of our biophysical assays to probe additional structural details within Httex1. In an effort to rule out weak hydrogen bonding, we also investigated HDX combined with NMR of Httex1 25Q at pH 4. Under these conditions, the exchange of a freely exposed peptide group is approximately 3 orders of magnitude slower than at pH 7.5 [26]. For Httex1 25Q, seven backbone amide hydrogens were found to be protected from deuteration at pH 4.","type":"Results"},{"text":"Our HDX data are consistent with a lack of persistent hydrogen bonding. This lack of hydrogen bonding may result from conformational heterogeneity within the polyQ domain and throughout Httex1, as predicted by the simulations, or from fully solvated, rod-like geometries with a preference for polyproline II conformations.","type":"Results"},{"text":"By measuring HDX-MS, we find that there is no clear evidence for changes in solvent protection, to imply the presence of stable beta-sheeted hydrogen bonds, with increased polyQ length.","type":"Discussion"}],"construct_alterations":[{"term_id":"IDPO:00483","term_name":"insertion","term_namespace":"Protein mutation","value":"p.Gln38_Pro39insGlnGlnGlnGln","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Given that the HDX-MS results for both 25Q and 46Q forms imply a lack of stable hydrogen bonding, we focused on the 25Q variant for the remainder of our biophysical assays to probe additional structural details within Httex1."}]}],"sequence_construct":"GHMATLEKLMKAFESLKSFQQQQQQQQQQQQQQQQQQQQQQQQQPPPPPPPPPPPQLPQPPPQAQPLLPQPQPPPPPPPPPPGPAVAEEPLHRPKKW","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-14T15:22:59.298Z"}},{"start":1,"end":87,"reference_id":"25464275","reference_source":"pmid","reference_html":"Polyglutamine- and temperature-dependent conformational rigidity in mutant huntingtin revealed by immunoassays and circular dichroism spectroscopy. <i> Fodale V, Kegulian NC, Verani M, Cariulo C, Azzollini L, Petricca L, Daldin M, Boggio R, Padova A, Kuhn R, Pacifici R, Macdonald D, Schoenfeld RC, Park H, Isas JM, Langen R, Weiss A, Caricasole A. </i> PLoS One, 2014","date":"2023-08-09T09:51:19.848Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r010","statement":[{"text":"The difference spectra for both proteins exhibit characteristic minima at 208 and 222 nm indicating increased formation of alpha-helical structure at lower temperatures, which is more pronounced for Q46 HTT protein (Fig. 6A), and all spectra (Fig. 5B and C) show an isosbestic point near 203 nm, which is commonly observed for conversions between random coil and alpha-helical structure.","type":"Results"},{"text":"The consistent isosbestic point across temperatures (Fig. 5B and C and 6B and C) together with the typically alpha-helical difference spectra (Fig. 6A and D) suggest that the conformational changes are dominated by a helix-coil transition.","type":"Results"},{"text":"Our CD studies indicate that HTT exon 1 can take up an extensive helical structure that likely includes the N17 as well as substantial portions of the polyQ region. This notion is in agreement with prior crystallographic studies, which showed that alpha-helical structure could extend from the N17 into the polyQ region in some, but not all structures [24] [25 [24]]. Our data indicate that the observed alpha-helical and unfolded structures are in equilibrium with one another.","type":"Discussion"}],"construct_alterations":[{"term_id":"IDPO:00483","term_name":"insertion","term_namespace":"Protein mutation","value":"p.Gln38_Pro39insGlnGlnGlnGln","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Using this model, we estimate that on the order of 23 and 31 residues become helical upon cooling for the Q25 and Q46 constructs, respectively (Table 1A)."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-14T15:23:10.754Z"}},{"start":1,"end":87,"reference_id":"12193654","reference_source":"pmid","reference_html":"A linear lattice model for polyglutamine in CAG-expansion diseases. <i> Bennett MJ, Huey-Tubman KE, Herr AB, West AP, Ross SA, Bjorkman PJ. </i> Proc Natl Acad Sci U S A, 2002","date":"2023-08-09T09:59:50.267Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r011","statement":[{"text":"In contrast to TRX-tag alone, the exon 1 fusion proteins with normal or expanded poly(Gln) are nonglobular by several measures, including anomalous migration in size exclusion chromatography and high frictional ratios (f/f0) in sedimentation velocity ultracentrifugation (Table 1).","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"In contrast to TRX-tag alone, the exon 1 fusion proteins with normal or expanded poly(Gln) are nonglobular by several measures, including anomalous migration in size exclusion chromatography and high frictional ratios (f/f0) in sedimentation velocity ultracentrifugation (Table 1)."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"Constructs contained the TRX gene, a linker segment (GSGSGERQHMDSPDLGTDDDDK), the HD exon 1 insert, and a His6 tag (Fig. 1a)."}]},{"term_id":"IDPO:00483","term_name":"insertion","term_namespace":"Protein mutation","value":"p.Gln38_Pro39insGlnGlnGlnGln","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"We expressed TRX fusion proteins containing HD exon 1 with 16, 25, 39, or 46 glutamines (Fig. 1a)."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-14T15:24:59.782Z"}},{"start":1,"end":87,"reference_id":"12193654","reference_source":"pmid","reference_html":"A linear lattice model for polyglutamine in CAG-expansion diseases. <i> Bennett MJ, Huey-Tubman KE, Herr AB, West AP, Ross SA, Bjorkman PJ. </i> Proc Natl Acad Sci U S A, 2002","date":"2023-08-09T10:01:37.820Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r012","statement":[{"text":"The CD spectra of HD exon 1 with different lengths of poly(Gln) (Fig. 2a) resemble the spectra of disordered proteins. In particular, the spectra are reminiscent of denatured collagen (21), which has a similar high imino acid (e.g., proline) content.","type":"Results"},{"text":"These results are consistent with a random-coil structure for both normal and expanded poly(Gln) tracts within HD exon 1. Moreover, the data suggest that flanking sequences in HD exon 1 (17 residues at the N terminus and 49 residues at the C terminus) do not adopt stable α or β secondary structures and that their presence does not induce a global transition in the poly(Gln) tract above the pathologic threshold.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"In contrast to TRX-tag alone, the exon 1 fusion proteins with normal or expanded poly(Gln) are nonglobular by several measures, including anomalous migration in size exclusion chromatography and high frictional ratios (f/f0) in sedimentation velocity ultracentrifugation (Table 1)."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"Constructs contained the TRX gene, a linker segment (GSGSGERQHMDSPDLGTDDDDK), the HD exon 1 insert, and a His6 tag (Fig. 1a)."}]},{"term_id":"IDPO:00483","term_name":"insertion","term_namespace":"Protein mutation","value":"p.Gln38_Pro39insGlnGlnGlnGln","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"We expressed TRX fusion proteins containing HD exon 1 with 16, 25, 39, or 46 glutamines (Fig. 1a)."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-14T15:25:32.000Z"}},{"start":1,"end":87,"reference_id":"26047735","reference_source":"pmid","reference_html":"Anti-PolyQ Antibodies Recognize a Short PolyQ Stretch in Both Normal and Mutant Huntingtin Exon 1. <i> Owens GE, New DM, West AP, Bjorkman PJ. </i> J Mol Biol, 2015","date":"2023-08-09T08:53:34.289Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r013","statement":[{"text":"During purification of huntingtin exon 1 fusion proteins, we observed anomalous migration by gel filtration chromatography such that huntingtin exon 1 fusion proteins appeared to migrate as higher molecular weight proteins (e.g., dimers) when compared with molecular weight standards of globular proteins.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Figure","text":"Figure 1: (a) Trx: 1-109; Linker: 109-132; Huntingtin exon 1: 132-214; Linker: 214-217; His6: 217-222"}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Figure","text":"Figure 1: (a) Trx: 1-109; Linker: 109-132; Huntingtin exon 1: 132-214; Linker: 214-217; His6: 217-222"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-14T15:26:12.929Z"}},{"start":1,"end":87,"reference_id":"26047735","reference_source":"pmid","reference_html":"Anti-PolyQ Antibodies Recognize a Short PolyQ Stretch in Both Normal and Mutant Huntingtin Exon 1. <i> Owens GE, New DM, West AP, Bjorkman PJ. </i> J Mol Biol, 2015","date":"2023-08-09T08:53:45.633Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r014","statement":[{"text":"By contrast, the Kratky plots for HD-16Q and HD-39Q were broader, with less degrease at higher scattering angles, consistent with flexible or unfolded proteins [21, 22] (Fig. 5b).","type":"Results"},{"text":"(b) HD-16Q and HD-39Q showed a plateau at higher q values, suggesting that these proteins include disordered regions, with decreasing globular character as the polyQ repeat length increased.","type":"Figure"},{"text":"Thus a combination of equilibrium gel filtration chromatography, DLS, and SAXS data are consistent with a linear lattice mode of recognition of unstructured polyQ for both 3B5H10 and MW1 antibodies.","type":"Discussion"}],"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Figure","text":"Figure 1: (a) Trx: 1-109; Linker: 109-132; Huntingtin exon 1: 132-214; Linker: 214-217; His6: 217-222"}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Figure","text":"Figure 1: (a) Trx: 1-109; Linker: 109-132; Huntingtin exon 1: 132-214; Linker: 214-217; His6: 217-222"}]},{"term_id":"IDPO:00483","term_name":"insertion","term_namespace":"Protein mutation","value":"p.Gln38_Pro39insGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGln","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"By contrast, the Kratky plots for HD-16Q and HD-39Q were broader, with less degrease at higher scattering angles, consistent with flexible or unfolded proteins [21, 22] (Fig. 5b)."}]},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gln34_Gln38del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"By contrast, the Kratky plots for HD-16Q and HD-39Q were broader, with less degrease at higher scattering angles, consistent with flexible or unfolded proteins [21, 22] (Fig. 5b)."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-14T15:26:24.768Z"}},{"start":1,"end":87,"reference_id":"30315108","reference_source":"pmid","reference_html":"The folding equilibrium of huntingtin exon 1 monomer depends on its polyglutamine tract. <i> Bravo-Arredondo JM, Kegulian NC, Schmidt T, Pandey NK, Situ AJ, Ulmer TS, Langen R. </i> J Biol Chem, 2018","date":"2023-08-07T15:34:13.847Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r015","statement":[{"text":"Next, we used the MREHttex1 values to estimate the number of nominal residues that convert from a random coil into an α-helical conformation when transitioning from 37 to −10 °C. These estimates were gradually increasing with Q-length and ranged from 11 amino acids for Q7 to 32 amino acids for Q55 (Fig. 1f). Inasmuch as the number of residues becoming α-helical was often larger than 17 (for Q25 and higher), regions outside of the N17 must have contributed to the observed helicity.","type":"Results"},{"text":"Still most amino acids in the construct remain to be classified as random coil.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Figure","text":"Figure 1. CD of Trx–Httex1 with different Q-lengths as function of temperature."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"Bead binding of spin-labeled Httex1 monomers was medi- ated by a His tag that was appended at the C-terminal end of Httex1 in the Trx–Httex1 fusion protein (19)."}]},{"term_id":"IDPO:00483","term_name":"insertion","term_namespace":"Protein mutation","value":"p.Gln38_Pro39insGlnGlnGlnGln","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Next, we used the MREHttex1 values to estimate the number of nominal residues that convert from a random coil into an α-helical conformation when transitioning from 37 to −10 °C. These estimates were gradually increasing with Q-length and ranged from 11 amino acids for Q7 to 32 amino acids for Q55 (Fig. 1f). Inasmuch as the number of residues becoming α-helical was often larger than 17 (for Q25 and higher), regions outside of the N17 must have contributed to the observed helicity."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-08T13:36:44.939Z"}},{"start":1,"end":87,"reference_id":"30315108","reference_source":"pmid","reference_html":"The folding equilibrium of huntingtin exon 1 monomer depends on its polyglutamine tract. <i> Bravo-Arredondo JM, Kegulian NC, Schmidt T, Pandey NK, Situ AJ, Ulmer TS, Langen R. </i> J Biol Chem, 2018","date":"2023-08-07T15:37:23.905Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006289","ec_ontology":"ECO","ec_name":"site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r016","statement":[{"text":"The spectra for 11R1 (N17) and 35R1 (polyQ) shared the interesting similarity that they had multiple components that became more clearly resolved at lower temperatures. One of these spectral components indicated a highly mobile structural state (Fig. 2b, denoted m), whereas another one is characteristic of a more immobilized and stable structural state (denoted i). In contrast, 81R1 lacked the immobilized spectral component and was dominated solely by the mobile spectral component.","type":"Results"},{"text":"The lack of immobilization for these sites indicated relatively dynamic regions that do not engage in significant tertiary packing interactions. The collective occurrence of pronounced multicomponent EPR spectra that were exclusively found at all N-terminal sites up to residue 35 strongly suggested that this region was characterized by at least two co-existing structural populations. One of these populations was dynamic and largely disordered, and the other was more ordered, likely corresponding to the α-helical structure observed by CD.","type":"Results"},{"text":"When comparing amplitudes obtained at the same temperature, the labeling sites in the N17 (Fig. 2c, blue) tended to have the lowest amplitudes, indicative of lowest mobility/highest order in this region. In contrast, the largest amplitudes (highest mobilities) were found in the PRD.","type":"Results"},{"text":"EPR spin-labeling analysis of Trx–Httex1(Q46) reveals the co-existence of two structural states in the N17 and the adjacent N-terminal portion of polyQ. One of these states is highly dynamic and largely disordered, whereas the other state is ordered, consistent with α-helical structure.","type":"Discussion"}],"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Figure","text":"Figure 1. CD of Trx–Httex1 with different Q-lengths as function of temperature."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"Bead binding of spin-labeled Httex1 monomers was medi- ated by a His tag that was appended at the C-terminal end of Httex1 in the Trx–Httex1 fusion protein (19)."}]},{"term_id":"IDPO:00483","term_name":"insertion","term_namespace":"Protein mutation","value":"p.Gln38_Pro39insGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGln","start":null,"end":null,"position":null,"statements":[{"type":"Discussion","text":"EPR spin-labeling analysis of Trx–Httex1(Q46) reveals the co-existence of two structural states in the N17 and the adjacent N-terminal portion of polyQ. One of these states is highly dynamic and largely disordered, whereas the other state is ordered, consistent with α-helical structure."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-08T13:37:30.741Z"}},{"start":1,"end":87,"reference_id":"30315108","reference_source":"pmid","reference_html":"The folding equilibrium of huntingtin exon 1 monomer depends on its polyglutamine tract. <i> Bravo-Arredondo JM, Kegulian NC, Schmidt T, Pandey NK, Situ AJ, Ulmer TS, Langen R. </i> J Biol Chem, 2018","date":"2023-08-07T15:42:32.601Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r017","statement":[{"text":"If all polyQ residues of Trx–Httex1(Q46) were structurally homogeneous, a single intense resonance would dominate the NMR spectra. In Trx–Httex1(Q46), dominating backbone HN and side-chain H2N resonances were indeed detected (Fig. S3). However, the strongest HN backbone resonance clearly was not 46 times stronger than signals from other residues, suggesting that the polyQ region was not structurally homogeneous.","type":"Results"},{"text":"As a simple measure of relative backbone dynamics along the Trx–Httex1(Q7) sequence, we compared signal intensities (Fig. 5a). The linker resonances exhibited the highest intensities, verifying the efficient uncoupling of the Trx domain from Httex1(Q7) already indicated in the aforementioned EPR (Fig. S2) and NMR (Fig. 3) experiments. The PRD also exhibited high albeit variable dynamics in overall accordance with EPR analysis (Fig. 2).","type":"Results"},{"text":"NMR spectroscopy further reveals that polyQ partakes in this temperature-dependent α-helix formation. However, helical structure is not uniformly adopted throughout the polyQ region. Rather, multiple NMR resonances are observed for the polyQ region, each arising from sequence populations of different helical content.","type":"Discussion"}],"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Figure","text":"Figure 1. CD of Trx–Httex1 with different Q-lengths as function of temperature."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"Bead binding of spin-labeled Httex1 monomers was medi- ated by a His tag that was appended at the C-terminal end of Httex1 in the Trx–Httex1 fusion protein (19)."}]},{"term_id":"IDPO:00483","term_name":"insertion","term_namespace":"Protein mutation","value":"p.Gln38_Pro39insGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGln","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"In Trx–Httex1(Q46), dominating backbone HN and side-chain H2N resonances were indeed detected (Fig. S3). However, the strongest HN backbone resonance clearly was not 46 times stronger than signals from other residues, suggesting that the polyQ region was not structurally homogeneous."}]},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gln25_Gln38del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"As a simple measure of relative backbone dynamics along the Trx–Httex1(Q7) sequence, we compared signal intensities (Fig. 5a). The linker resonances exhibited the highest intensities, verifying the efficient uncoupling of the Trx domain from Httex1(Q7) already indicated in the aforementioned EPR (Fig. S2) and NMR (Fig. 3) experiments. The PRD also exhibited high albeit variable dynamics in overall accordance with EPR analysis (Fig. 2)."}]}],"cross_refs":[{"db":"BMRB","id":"27636"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-08T13:38:05.271Z"}},{"start":1,"end":88,"reference_id":"32402249","reference_source":"pmid","reference_html":"Flanking Regions Determine the Structure of the Poly-Glutamine in Huntingtin through Mechanisms Common among Glutamine-Rich Human Proteins. <i> Urbanek A, Popovic M, Morató A, Estaña A, Elena-Real CA, Mier P, Fournet A, Allemand F, Delbecq S, Andrade-Navarro MA, Cortés J, Sibille N, Bernadó P. </i> Structure, 2020","date":"2023-08-09T08:55:36.961Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r018","statement":[{"text":"The secondary chemical shift (SCS) analysis using a neighbor-corrected random coil database (Nielsen and Mulder, 2018) indicates that both N17 and the poly-Q tract are enriched in α-helical conformations, although this propensity is not homogeneous (Figure 2D). Helicity increases along N17, reaching its maximum at the first glutamine, Q18, and subsequently decreases smoothly. A transition is observed at Q29, which adopts a small and negative SCS value. This extends to the following three glutamines, indicating the presence of random coil or slightly extended conformations.","type":"Results"},{"text":"Three of these ensembles present α helices that encompass the last residues of N17 and the first residues of the poly-Q. No persistent turns in the residues connecting both domains are observed, which would otherwise yield a strong signature in the CS profile. As a consequence, H16 should be considered as an elongated flexible particle, in contrast to the previously proposed compact tadpole-like model (Newcombe et al., 2018, Warner et al., 2017).","type":"Results"},{"text":"This observation demonstrates that the poly-P tract in httex1 exerts a strong conformational perturbation on the neighboring glutamines by enriching the ensemble with extended conformations, which break the inherent helical propensity of the poly-Q.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gln34_Gln38del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"As a consequence, H16 should be considered as an elongated flexible particle, in contrast to the previously proposed compact tadpole-like model (Newcombe et al., 2018, Warner et al., 2017)."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-14T15:26:37.258Z"}},{"start":1,"end":88,"reference_id":"36864173","reference_source":"pmid","reference_html":"The structure of pathogenic huntingtin exon 1 defines the bases of its aggregation propensity. <i> Elena-Real CA, Sagar A, Urbanek A, Popovic M, Morató A, Estaña A, Fournet A, Doucet C, Lund XL, Shi ZD, Costa L, Thureau A, Allemand F, Swenson RE, Milhiet PE, Crehuet R, Barducci A, Cortés J, Sinnaeve D, Sibille N, Bernadó P. </i> Nat Struct Mol Biol, 2023","date":"2023-08-07T16:07:36.784Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r019","statement":[{"text":"To further confirm that the overall extendedness is inherent to httex1, we performed an equivalent SAXS analysis for H16 (FigS. 3a, S3 and Table S2). Not surprisingly, the resulting SAXS profile of H16 indicated that the protein is a smaller particle (Rg=32.9 ± 0.2 Å and Dmax = 126 Å) in solution than H46 (Table S2). Importantly, H16 retained SAXS features corresponding to an extended and flexible particle observed for H46.","type":"Supplementary material"}],"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gln34_Gln38del","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"Importantly, H16 retained SAXS features corresponding to an extended and flexible particle observed for H46."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-08T13:43:56.246Z"}},{"start":1,"end":88,"reference_id":"36864173","reference_source":"pmid","reference_html":"The structure of pathogenic huntingtin exon 1 defines the bases of its aggregation propensity. <i> Elena-Real CA, Sagar A, Urbanek A, Popovic M, Morató A, Estaña A, Fournet A, Doucet C, Lund XL, Shi ZD, Costa L, Thureau A, Allemand F, Swenson RE, Milhiet PE, Crehuet R, Barducci A, Cortés J, Sinnaeve D, Sibille N, Bernadó P. </i> Nat Struct Mol Biol, 2023","date":"2023-08-07T16:05:34.902Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r020","statement":[{"text":"Similar to H16 (ref. 23), which also contained a fused sfGFP, the spectrum revealed that, while peaks from N17 and the PRR were well dispersed, glutamine frequencies remained poorly resolved (Fig. 1b).","type":"Results"},{"text":"After modeling the sfGFP and the C-terminal His-tag to the individual conformations, the NMR-optimized ensemble was further refined by integrating the SAXS data with the ensemble optimization method (EOM)30,31. Subensembles selected with EOM yielded an excellent fit to the experimental profile (χ2 = 0.2) (Fig. 3a). The resulting radius of gyration (Rg) distribution was broad, indicating that H46 is a highly flexible particle in solution and slightly more extended than the CS-derived ensemble (Extended Data Fig. 3).","type":"Results"},{"text":"The refined ensemble indicates that H46 is a flexible elongated particle in solution and that the overall size is correlated with the length of the poly-Q (Fig. 3c). Our structural model is in contradiction to previously reported compact models of httex1 stabilized by extensive fuzzy contacts between N17 and poly-Q14,15,46,47. Despite the overall extendedness of httex1, our description requires a large degree of disorder, explaining the fluorescence transfer efficiency observed in smFRET14 and the lack of permanent hydrogen bonds in NMR hydrogen deuterium exchange experiments, which have been argued to support the compact model15.","type":"Discussion"}],"construct_alterations":[{"term_id":"IDPO:00483","term_name":"insertion","term_namespace":"Protein mutation","value":"p.Gln38_Pro39insGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGln","start":null,"end":null,"position":null,"statements":[{"type":"Discussion","text":"The synergistic combination of NMR and SAXS data has enabled the elucidation of an ensemble model of H46[57], showing that the presence of long α-helices determines the overall shape of httex1. The refined ensemble indicates that H46 is a flexible elongated particle in solution and that the overall size is correlated with the length of the poly-Q tract (Fig. 3c)."}]},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"All genes were cloned into pIVEX 2.3d as previously described23, giving rise to pIVEX-httex1–3C-sfGFP-His6."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"All genes were cloned into pIVEX 2.3d as previously described23, giving rise to pIVEX-httex1–3C-sfGFP-His6."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-08T13:44:47.266Z"}},{"start":1,"end":87,"reference_id":"33096080","reference_source":"pmid","reference_html":"Structural Model of the Proline-Rich Domain of Huntingtin Exon-1 Fibrils. <i> Falk AS, Bravo-Arredondo JM, Varkey J, Pacheco S, Langen R, Siemer AB. </i> Biophys J, 2020","date":"2023-08-07T16:17:01.375Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r021","statement":[{"text":"This assignment allowed us to also measure site-specific 15N R1 and R2 relaxation rates as well as residual 1H-15N dipolar couplings that confirmed the highly dynamic nature of these residues in the context of the fibril (15).","type":"Results"},{"text":"Overall, the PRD stays relatively extended throughout the simulations with two stable PPII helices, P10 and P11, a more variable L17 linker region, and a very flexible C-terminal C12 region. Nevertheless, the L17 and, to a lesser extent, the C12 region have average dihedral angles compatible with a PPII helical or β-sheet conformation and are extended for most of the simulation, indicating that these regions are rather imperfect PPII helices than completely disordered. This extended PRD is also compatible with our previous observation that unbundled huntingtin (HTT) fibrils are spaced consistent with fibrils being held apart by extended polyproline bristles (12).","type":"Discussion"},{"text":"Our finding that the PRD is mostly extended is compatible with the tadpole model of the HTTex1 monomer by Newcombe and co-workers in which the N17 and polyQ domains are more compact, and the PRD forms the extended tail of a tadpole-like structure (24).","type":"Discussion"}],"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"In short, the thioredoxin fusion protein of HTTex1 was recombinantly expressed in a pET32a vector using Escherichia coli BL21 (DE3) cells."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Figure","text":"The N17 region is highlighted in orange, the polyQ domain in blue, the Pro-rich C-terminus in green, and the His-tag in black."},{"type":"Figure","text":"Figure 1: MATLEKLMKAFESLKSF[Q]45Q[P]11QLPQPPPQAQPLLPQPQ[P]10GPAVAEEPLHRPHHHHHH"}]},{"term_id":"IDPO:00483","term_name":"insertion","term_namespace":"Protein mutation","value":"p.Gln38_Pro39insGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGlnGln","start":null,"end":null,"position":null,"statements":[{"type":"Figure","text":"Figure 1: MATLEKLMKAFESLKSF[Q]45Q[P]11QLPQPPPQAQPLLPQPQ[P]10GPAVAEEPLHRPHHHHHH"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-08T13:45:47.004Z"}},{"start":1718,"end":1732,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-07-27T10:12:32.998Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6RMH"},{"db":"EMDB","id":"EMD-4937"}],"region_id":"DP04129r022","statement":[{"text":"To gain further insight into the structure of Q23-HTT in the apo state, we generated and fitted atomic models to our cryo-EM map of Q23-HTT utilizing the structure of HTTHAP40 in complex with HAP40 via an integrative modeling strategy. The HTTHAP40 model was split into three rigid domains, N-HEAT, Bridge, and C-HEAT, based on the fact that these three domains are weakly connected by unresolved flexible regions (residues 1,713–1,729 separating N-HEAT and Bridge domains, and residues 2,062–2,092 separating Bridge and C-HEAT domains) in HTT HAP40 structure.","type":"Results"},{"text":"UniProt numbering is slightly different from the authors' numbering.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T13:30:29.154Z"}},{"start":1718,"end":1732,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-07-27T10:12:49.584Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6RMH"},{"db":"EMDB","id":"EMD-4937"}],"region_id":"DP04129r023","statement":[{"text":"To gain further insight into the structure of Q23-HTT in the apo state, we generated and fitted atomic models to our cryo-EM map of Q23-HTT utilizing the structure of HTTHAP40 in complex with HAP40 via an integrative modeling strategy. The HTTHAP40 model was split into three rigid domains, N-HEAT, Bridge, and C-HEAT, based on the fact that these three domains are weakly connected by unresolved flexible regions (residues 1,713–1,729 separating N-HEAT and Bridge domains, and residues 2,062–2,092 separating Bridge and C-HEAT domains) in HTT HAP40 structure.","type":"Results"},{"text":"UniProt numbering is slightly different from the authors' numbering.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T13:52:25.833Z"}},{"start":2067,"end":2095,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-07-27T10:15:45.007Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6RMH"},{"db":"EMDB","id":"EMD-4937"}],"region_id":"DP04129r024","statement":[{"text":"To gain further insight into the structure of Q23-HTT in the apo state, we generated and fitted atomic models to our cryo-EM map of Q23-HTT utilizing the structure of HTTHAP40 in complex with HAP40 via an integrative modeling strategy. The HTTHAP40 model was split into three rigid domains, N-HEAT, Bridge, and C-HEAT, based on the fact that these three domains are weakly connected by unresolved flexible regions (residues 1,713–1,729 separating N-HEAT and Bridge domains, and residues 2,062–2,092 separating Bridge and C-HEAT domains) in HTT HAP40 structure.","type":"Results"},{"text":"UniProt numbering is slightly different from the authors' numbering.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T13:30:46.593Z"}},{"start":2067,"end":2095,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-07-27T10:14:46.814Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"6RMH"},{"db":"EMDB","id":"EMD-4937"}],"region_id":"DP04129r025","statement":[{"text":"To gain further insight into the structure of Q23-HTT in the apo state, we generated and fitted atomic models to our cryo-EM map of Q23-HTT utilizing the structure of HTTHAP40 in complex with HAP40 via an integrative modeling strategy. The HTTHAP40 model was split into three rigid domains, N-HEAT, Bridge, and C-HEAT, based on the fact that these three domains are weakly connected by unresolved flexible regions (residues 1,713–1,729 separating N-HEAT and Bridge domains, and residues 2,062–2,092 separating Bridge and C-HEAT domains) in HTT HAP40 structure.","type":"Results"},{"text":"UniProt numbering is slightly different from the authors' numbering.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T13:52:31.245Z"}},{"start":2067,"end":2090,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-07-27T10:15:23.245Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r026","statement":[{"text":"Another region showing high exchange rate is around aa 2,000–2,200 and is located at the interface between the Bridge and C-HEAT domains, which is consistent with our observation that the Bridge domain serves as pivot joints making HTT conformationally flexible.","type":"Results"},{"text":"Figure S5. Related to Figure 5. HDX-MS Experiments. (A) The HDX-MS deuteration map of Q23- (A), and Q78-HTT (B). Total 147 peptides detected and the coverage was 42.7%. The N-HEAT, bridge, and the C-HEAT domain were indicated by blue, orange, and red boxes, respectively.","type":"Supplementary material"},{"text":"The authors refer to a 200 residues long region of high exchange rate, but for the stringency of the annotation only a shorter region with higher than 60% exchange rate after 45 min was curated. This greatly overlaps with the missing electron densities in the cryo-EM map (c.f. DP04129r024), which validates the interpretation.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T13:31:44.345Z"}},{"start":2067,"end":2090,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-07-27T10:06:01.655Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r027","statement":[{"text":"Another region showing high exchange rate is around aa 2,000–2,200 and is located at the interface between the Bridge and C-HEAT domains, which is consistent with our observation that the Bridge domain serves as pivot joints making HTT conformationally flexible.","type":"Results"},{"text":"Figure S5. Related to Figure 5. HDX-MS Experiments. (A) The HDX-MS deuteration map of Q23- (A), and Q78-HTT (B). Total 147 peptides detected and the coverage was 42.7%. The N-HEAT, bridge, and the C-HEAT domain were indicated by blue, orange, and red boxes, respectively.","type":"Supplementary material"},{"text":"The authors refer to a 200 residues long region of high exchange rate, but for the stringency of the annotation only a shorter region with higher than 60% exchange rate after 45 min was curated. This greatly overlaps with the missing electron densities in the cryo-EM map (c.f. DP04129r024), which validates the interpretation.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T13:52:39.855Z"}},{"start":407,"end":664,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-07-27T10:29:16.202Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-4937"},{"db":"PDB","id":"6RMH"}],"region_id":"DP04129r028","statement":[{"text":"Besides the polyQ tract, a large portion of N-HEAT domain (aa 409–666 in Q23-HTT) in the high-resolution cryo-EM structure is unstructured in addition to several small regions in other domains.","type":"Discussion"},{"text":"UniProt numbering is slightly different from the authors' numbering.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T13:37:22.701Z"}},{"start":419,"end":432,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-08-07T16:37:13.679Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001582","ec_ontology":"ECO","ec_name":"liquid chromatography coupled with tandem mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r029","statement":[{"text":"Besides the polyQ tract, a large portion of N-HEAT domain (aa 409–666 in Q23-HTT) in the high-resolution cryo-EM structure is unstructured in addition to several small regions in other domains.","type":"Discussion"},{"text":"UniProt numbering is slightly different from the authors' numbering.","type":"Curator statement"},{"text":"Interestingly, many residues in the large unstructured region in N-HEAT domain are shown to be phosphorylated, and these modifications seem to modify HTT function.","type":"Discussion"},{"text":"Several HTT phosphorylation sites were identified by MS and are listed along the length of the HTT amino acid sequence.","type":"Figure"},{"text":"Phosphosites on Figure 6A in the IDR streching between aa. 407-664 within the N-HEAT domain: pS421 and pS434. With UniProt numbering these correspond to pS419 and pS432.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-08T13:49:38.674Z"}},{"start":1179,"end":1199,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-08-07T16:37:26.192Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001582","ec_ontology":"ECO","ec_name":"liquid chromatography coupled with tandem mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r030","statement":[{"text":"Besides the polyQ tract, a large portion of N-HEAT domain (aa 409–666 in Q23-HTT) in the high-resolution cryo-EM structure is unstructured in addition to several small regions in other domains.","type":"Discussion"},{"text":"Interestingly, many residues in the large unstructured region in N-HEAT domain are shown to be phosphorylated, and these modifications seem to modify HTT function.","type":"Discussion"},{"text":"Several HTT phosphorylation sites were identified by MS and are listed along the length of the HTT amino acid sequence.","type":"Figure"},{"text":"Phosphosites on Figure 6A in the IDR streching between aa. 1162-1226 within the N-HEAT domain: pS1181 and pS1201. With UniProt numbering these correspond to pS1179 and pS1199.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-08T13:49:39.569Z"}},{"start":1162,"end":1226,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-07-27T10:59:02.687Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-4937"},{"db":"PDB","id":"6RMH"}],"region_id":"DP04129r031","statement":[{"text":"Besides the polyQ tract, a large portion of N-HEAT domain (aa 409–666 in Q23-HTT) in the high-resolution cryo-EM structure is unstructured in addition to several small regions in other domains.","type":"Discussion"},{"text":"One of these additional smaller IDRs streches between aa. 1162-1226 within the N-HEAT domain.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T13:46:46.835Z"}},{"start":1,"end":94,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-07-27T11:04:29.494Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-4937"},{"db":"PDB","id":"6RMH"}],"region_id":"DP04129r032","statement":[{"text":"Besides the polyQ tract, a large portion of N-HEAT domain (aa 409–666 in Q23-HTT) in the high-resolution cryo-EM structure is unstructured in addition to several small regions in other domains.","type":"Discussion"},{"text":"The N-terminal disordered tail encompassing the polyQ tract and missing from the density map includes the first 94 residues.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T13:47:21.306Z"}},{"start":1323,"end":1351,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-07-27T11:20:33.428Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-4937"},{"db":"PDB","id":"6RMH"}],"region_id":"DP04129r033","statement":[{"text":"Besides the polyQ tract, a large portion of N-HEAT domain (aa 409–666 in Q23-HTT) in the high-resolution cryo-EM structure is unstructured in addition to several small regions in other domains.","type":"Discussion"},{"text":"One of these additional smaller IDRs streches between aa. 1323-1351 within the N-HEAT domain.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T13:47:39.378Z"}},{"start":1376,"end":1422,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-07-27T11:21:01.142Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-4937"},{"db":"PDB","id":"6RMH"}],"region_id":"DP04129r034","statement":[{"text":"Besides the polyQ tract, a large portion of N-HEAT domain (aa 409–666 in Q23-HTT) in the high-resolution cryo-EM structure is unstructured in addition to several small regions in other domains.","type":"Discussion"},{"text":"One of these additional smaller IDRs streches between aa. 1376-1422 within the N-HEAT domain.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T13:47:53.668Z"}},{"start":1859,"end":1885,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-07-27T11:21:40.380Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-4937"},{"db":"PDB","id":"6RMH"}],"region_id":"DP04129r035","statement":[{"text":"Besides the polyQ tract, a large portion of N-HEAT domain (aa 409–666 in Q23-HTT) in the high-resolution cryo-EM structure is unstructured in addition to several small regions in other domains.","type":"Discussion"},{"text":"One of these additional smaller IDRs streches between aa. 1859-1885 within the Bridge domain.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T13:48:08.526Z"}},{"start":2329,"end":2351,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-07-27T11:22:13.154Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-4937"},{"db":"PDB","id":"6RMH"}],"region_id":"DP04129r036","statement":[{"text":"Besides the polyQ tract, a large portion of N-HEAT domain (aa 409–666 in Q23-HTT) in the high-resolution cryo-EM structure is unstructured in addition to several small regions in other domains.","type":"Discussion"},{"text":"One of these additional smaller IDRs streches between aa. 2329-2351 within the C-HEAT domain.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T13:48:21.743Z"}},{"start":2631,"end":2664,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-08-07T16:26:36.494Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-4937"},{"db":"PDB","id":"6RMH"}],"region_id":"DP04129r037","statement":[{"text":"Besides the polyQ tract, a large portion of N-HEAT domain (aa 409–666 in Q23-HTT) in the high-resolution cryo-EM structure is unstructured in addition to several small regions in other domains.","type":"Discussion"},{"text":"One of these additional smaller IDRs streches between aa. 2631-2664 within the C-HEAT domain.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-08T13:46:06.857Z"}},{"start":3103,"end":3142,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-07-27T11:24:07.147Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-4937"},{"db":"PDB","id":"6RMH"}],"region_id":"DP04129r038","statement":[{"text":"Besides the polyQ tract, a large portion of N-HEAT domain (aa 409–666 in Q23-HTT) in the high-resolution cryo-EM structure is unstructured in addition to several small regions in other domains.","type":"Discussion"},{"text":"One of these additional smaller IDRs streches between aa. 3103-3142 within the C-HEAT domain.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T13:51:48.371Z"}},{"start":1862,"end":1874,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-08-07T16:37:40.387Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001582","ec_ontology":"ECO","ec_name":"liquid chromatography coupled with tandem mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r039","statement":[{"text":"Besides the polyQ tract, a large portion of N-HEAT domain (aa 409–666 in Q23-HTT) in the high-resolution cryo-EM structure is unstructured in addition to several small regions in other domains.","type":"Discussion"},{"text":"Most phosphorylation sites except S2114, S2116, S2423, and S2550 located in the C-HEAT domain are located in disordered regions in the cryo-EM structures.","type":"Results"},{"text":"Several HTT phosphorylation sites were identified by MS and are listed along the length of the HTT amino acid sequence.","type":"Figure"},{"text":"Phosphosites on Figure 6A in the IDR streching between aa. 1859-1885 within the Bridge domain: pS1864 and pS1876. With UniProt numbering these correspond to pS1862 and pS1874.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-08T13:49:40.346Z"}},{"start":2333,"end":2337,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-08-07T16:37:49.713Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001582","ec_ontology":"ECO","ec_name":"liquid chromatography coupled with tandem mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r040","statement":[{"text":"Besides the polyQ tract, a large portion of N-HEAT domain (aa 409–666 in Q23-HTT) in the high-resolution cryo-EM structure is unstructured in addition to several small regions in other domains.","type":"Discussion"},{"text":"Most phosphorylation sites except S2114, S2116, S2423, and S2550 located in the C-HEAT domain are located in disordered regions in the cryo-EM structures.","type":"Results"},{"text":"Several HTT phosphorylation sites were identified by MS and are listed along the length of the HTT amino acid sequence.","type":"Figure"},{"text":"Phosphosite on Figure 6A and Suppl. fig. S5A in the IDR streching between aa. 2329-2351 within the C-HEAT domain: pT2337. With UniProt numbering this corresponds to pT2335. The curated phosphorylation display site was annotated with 2-residue flanking regions in both direction.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-08T13:50:22.755Z"}},{"start":327,"end":346,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-08-07T16:33:25.115Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-4937"},{"db":"PDB","id":"6RMH"}],"region_id":"DP04129r041","statement":[{"text":"Besides the polyQ tract, a large portion of N-HEAT domain (aa 409–666 in Q23-HTT) in the high-resolution cryo-EM structure is unstructured in addition to several small regions in other domains.","type":"Discussion"},{"text":"One of these additional smaller IDRs streches between aa. 327-346 within the N-HEAT domain.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-08T13:46:34.083Z"}},{"start":964,"end":981,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-08-07T16:33:50.434Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-4937"},{"db":"PDB","id":"6RMH"}],"region_id":"DP04129r042","statement":[{"text":"Besides the polyQ tract, a large portion of N-HEAT domain (aa 409–666 in Q23-HTT) in the high-resolution cryo-EM structure is unstructured in addition to several small regions in other domains.","type":"Discussion"},{"text":"One of these additional smaller IDRs streches between aa. 964-981 within the N-HEAT domain.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-08T13:46:36.775Z"}},{"start":1107,"end":1124,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-08-07T16:35:13.359Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-4937"},{"db":"PDB","id":"6RMH"}],"region_id":"DP04129r043","statement":[{"text":"Besides the polyQ tract, a large portion of N-HEAT domain (aa 409–666 in Q23-HTT) in the high-resolution cryo-EM structure is unstructured in addition to several small regions in other domains.","type":"Discussion"},{"text":"One of these additional smaller IDRs streches between aa. 1107-1124 within the N-HEAT domain.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-08T13:46:39.769Z"}},{"start":2476,"end":2494,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-08-07T16:35:36.076Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-4937"},{"db":"PDB","id":"6RMH"}],"region_id":"DP04129r044","statement":[{"text":"Besides the polyQ tract, a large portion of N-HEAT domain (aa 409–666 in Q23-HTT) in the high-resolution cryo-EM structure is unstructured in addition to several small regions in other domains.","type":"Discussion"},{"text":"One of these additional smaller IDRs streches between aa. 2476-2494 within the C-HEAT domain.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-08T13:46:47.189Z"}},{"start":2930,"end":2948,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-08-07T16:36:00.658Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-4937"},{"db":"PDB","id":"6RMH"}],"region_id":"DP04129r045","statement":[{"text":"Besides the polyQ tract, a large portion of N-HEAT domain (aa 409–666 in Q23-HTT) in the high-resolution cryo-EM structure is unstructured in addition to several small regions in other domains.","type":"Discussion"},{"text":"One of these additional smaller IDRs streches between aa. 2930-2948 within the C-HEAT domain.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-08T13:46:51.587Z"}},{"start":2338,"end":2342,"reference_id":"32668197","reference_source":"pmid","reference_html":"The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain. <i> Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ. </i> Structure, 2020","date":"2023-08-07T17:55:20.176Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001582","ec_ontology":"ECO","ec_name":"liquid chromatography coupled with tandem mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04129r046","statement":[{"text":"Besides the polyQ tract, a large portion of N-HEAT domain (aa 409–666 in Q23-HTT) in the high-resolution cryo-EM structure is unstructured in addition to several small regions in other domains.","type":"Discussion"},{"text":"Most phosphorylation sites except S2114, S2116, S2423, and S2550 located in the C-HEAT domain are located in disordered regions in the cryo-EM structures.","type":"Results"},{"text":"Several HTT phosphorylation sites were identified by MS and are listed along the length of the HTT amino acid sequence.","type":"Figure"},{"text":"Phosphosite on Figure 6A and Suppl. fig. S5A in the IDR streching between aa. 2329-2351 within the C-HEAT domain: pS2342. With UniProt numbering this corresponds to pS2340. The curated phosphorylation display site was annotated with 2-residue flanking regions in both direction.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-08T13:50:21.716Z"}}],"regions_counter":46,"released":"2023_12","sequence":"MATLEKLMKAFESLKSFQQQQQQQQQQQQQQQQQQQQQPPPPPPPPPPPQLPQPPPQAQPLLPQPQPPPPPPPPPPGPAVAEEPLHRPKKELSATKKDRVNHCLTICENIVAQSVRNSPEFQKLLGIAMELFLLCSDDAESDVRMVADECLNKVIKALMDSNLPRLQLELYKEIKKNGAPRSLRAALWRFAELAHLVRPQKCRPYLVNLLPCLTRTSKRPEESVQETLAAAVPKIMASFGNFANDNEIKVLLKAFIANLKSSSPTIRRTAAGSAVSICQHSRRTQYFYSWLLNVLLGLLVPVEDEHSTLLILGVLLTLRYLVPLLQQQVKDTSLKGSFGVTRKEMEVSPSAEQLVQVYELTLHHTQHQDHNVVTGALELLQQLFRTPPPELLQTLTAVGGIGQLTAAKEESGGRSRSGSIVELIAGGGSSCSPVLSRKQKGKVLLGEEEALEDDSESRSDVSSSALTASVKDEISGELAASSGVSTPGSAGHDIITEQPRSQHTLQADSVDLASCDLTSSATDGDEEDILSHSSSQVSAVPSDPAMDLNDGTQASSPISDSSQTTTEGPDSAVTPSDSSEIVLDGTDNQYLGLQIGQPQDEDEEATGILPDEASEAFRNSSMALQQAHLLKNMSHCRQPSDSSVDKFVLRDEATEPGDQENKPCRIKGDIGQSTDDDSAPLVHCVRLLSASFLLTGGKNVLVPDRDVRVSVKALALSCVGAAVALHPESFFSKLYKVPLDTTEYPEEQYVSDILNYIDHGDPQVRGATAILCGTLICSILSRSRFHVGDWMGTIRTLTGNTFSLADCIPLLRKTLKDESSVTCKLACTAVRNCVMSLCSSSYSELGLQLIIDVLTLRNSSYWLVRTELLETLAEIDFRLVSFLEAKAENLHRGAHHYTGLLKLQERVLNNVVIHLLGDEDPRVRHVAAASLIRLVPKLFYKCDQGQADPVVAVARDQSSVYLKLLMHETQPPSHFSVSTITRIYRGYNLLPSITDVTMENNLSRVIAAVSHELITSTTRALTFGCCEALCLLSTAFPVCIWSLGWHCGVPPLSASDESRKSCTVGMATMILTLLSSAWFPLDLSAHQDALILAGNLLAASAPKSLRSSWASEEEANPAATKQEEVWPALGDRALVPMVEQLFSHLLKVINICAHVLDDVAPGPAIKAALPSLTNPPSLSPIRRKGKEKEPGEQASVPLSPKKGSEASAASRQSDTSGPVTTSKSSSLGSFYHLPSYLKLHDVLKATHANYKVTLDLQNSTEKFGGFLRSALDVLSQILELATLQDIGKCVEEILGYLKSCFSREPMMATVCVQQLLKTLFGTNLASQFDGLSSNPSKSQGRAQRLGSSSVRPGLYHYCFMAPYTHFTQALADASLRNMVQAEQENDTSGWFDVLQKVSTQLKTNLTSVTKNRADKNAIHNHIRLFEPLVIKALKQYTTTTCVQLQKQVLDLLAQLVQLRVNYCLLDSDQVFIGFVLKQFEYIEVGQFRESEAIIPNIFFFLVLLSYERYHSKQIIGIPKIIQLCDGIMASGRKAVTHAIPALQPIVHDLFVLRGTNKADAGKELETQKEVVVSMLLRLIQYHQVLEMFILVLQQCHKENEDKWKRLSRQIADIILPMLAKQQMHIDSHEALGVLNTLFEILAPSSLRPVDMLLRSMFVTPNTMASVSTVQLWISGILAILRVLISQSTEDIVLSRIQELSFSPYLISCTVINRLRDGDSTSTLEEHSEGKQIKNLPEETFSRFLLQLVGILLEDIVTKQLKVEMSEQQHTFYCQELGTLLMCLIHIFKSGMFRRITAAATRLFRSDGCGGSFYTLDSLNLRARSMITTHPALVLLWCQILLLVNHTDYRWWAEVQQTPKRHSLSSTKLLSPQMSGEEEDSDLAAKLGMCNREIVRRGALILFCDYVCQNLHDSEHLTWLIVNHIQDLISLSHEPPVQDFISAVHRNSAASGLFIQAIQSRCENLSTPTMLKKTLQCLEGIHLSQSGAVLTLYVDRLLCTPFRVLARMVDILACRRVEMLLAANLQSSMAQLPMEELNRIQEYLQSSGLAQRHQRLYSLLDRFRLSTMQDSLSPSPPVSSHPLDGDGHVSLETVSPDKDWYVHLVKSQCWTRSDSALLEGAELVNRIPAEDMNAFMMNSEFNLSLLAPCLSLGMSEISGGQKSALFEAAREVTLARVSGTVQQLPAVHHVFQPELPAEPAAYWSKLNDLFGDAALYQSLPTLARALAQYLVVVSKLPSHLHLPPEKEKDIVKFVVATLEALSWHLIHEQIPLSLDLQAGLDCCCLALQLPGLWSVVSSTEFVTHACSLIYCVHFILEAVAVQPGEQLLSPERRTNTPKAISEEEEEVDPNTQNPKYITAACEMVAEMVESLQSVLALGHKRNSGVPAFLTPLLRNIIISLARLPLVNSYTRVPPLVWKLGWSPKPGGDFGTAFPEIPVEFLQEKEVFKEFIYRINTLGWTSRTQFEETWATLLGVLVTQPLVMEQEESPPEEDTERTQINVLAVQAITSLVLSAMTVPVAGNPAVSCLEQQPRNKPLKALDTRFGRKLSIIRGIVEQEIQAMVSKRENIATHHLYQAWDPVPSLSPATTGALISHEKLLLQINPERELGSMSYKLGQVSIHSVWLGNSITPLREEEWDEEEEEEADAPAPSSPPTSPVNSRKHRAGVDIHSCSQFLLELYSRWILPSSSARRTPAILISEVVRSLLVVSDLFTERNQFELMYVTLTELRRVHPSEDEILAQYLVPATCKAAAVLGMDKAVAEPVSRLLESTLRSSHLPSRVGALHGVLYVLECDLLDDTAKQLIPVISDYLLSNLKGIAHCVNIHSQQHVLVMCATAFYLIENYPLDVGPEFSASIIQMCGVMLSGSEESTPSIIYHCALRGLERLLLSEQLSRLDAESLVKLSVDRVNVHSPHRAMAALGLMLTCMYTGKEKVSPGRTSDPNPAAPDSESVIVAMERVSVLFDRIRKGFPCEARVVARILPQFLDDFFPPQDIMNKVIGEFLSNQQPYPQFMATVVYKVFQTLHSTGQSSMVRDWVMLSLSNFTQRAPVAMATWSLSCFFVSASTSPWVAAILPHVISRMGKLEQVDVNLFCLVATDFYRHQIEEELDRRAFQSVLEVVAAPGSPYHRLLTCLRNVHKVTTC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins","Condensates-related proteins"],"disorder_content":0.24029280712921705,"disprot_consensus":{"full":[{"start":1,"end":94,"type":"D"},{"start":327,"end":346,"type":"D"},{"start":407,"end":664,"type":"D"},{"start":964,"end":981,"type":"D"},{"start":1107,"end":1124,"type":"D"},{"start":1162,"end":1226,"type":"D"},{"start":1323,"end":1351,"type":"D"},{"start":1376,"end":1422,"type":"D"},{"start":1718,"end":1732,"type":"D"},{"start":1859,"end":1885,"type":"D"},{"start":2067,"end":2095,"type":"D"},{"start":2329,"end":2351,"type":"D"},{"start":2476,"end":2494,"type":"D"},{"start":2631,"end":2664,"type":"D"},{"start":2930,"end":2948,"type":"D"},{"start":3103,"end":3142,"type":"D"}],"Structural state":[{"start":1,"end":94,"type":"D"},{"start":327,"end":346,"type":"D"},{"start":407,"end":664,"type":"D"},{"start":964,"end":981,"type":"D"},{"start":1107,"end":1124,"type":"D"},{"start":1162,"end":1226,"type":"D"},{"start":1323,"end":1351,"type":"D"},{"start":1376,"end":1422,"type":"D"},{"start":1718,"end":1732,"type":"D"},{"start":1859,"end":1885,"type":"D"},{"start":2067,"end":2095,"type":"D"},{"start":2329,"end":2351,"type":"D"},{"start":2476,"end":2494,"type":"D"},{"start":2631,"end":2664,"type":"D"},{"start":2930,"end":2948,"type":"D"},{"start":3103,"end":3142,"type":"D"}],"Disorder function":[{"start":419,"end":432,"type":"F"},{"start":1179,"end":1199,"type":"F"},{"start":1718,"end":1732,"type":"F"},{"start":1862,"end":1874,"type":"F"},{"start":2067,"end":2095,"type":"F"},{"start":2333,"end":2342,"type":"F"}]}},{"disprot_id":"DP04130","acc":"P32911","creator":"cpintado","date":"2023-07-19T10:36:58.682Z","features":{"pfam":[{"id":"PF01253","name":"Translation initiation factor SUI1","start":23,"end":97}],"gene3D":[]},"genes":[{"name":{"value":"SUI1"},"synonyms":[{"value":"RFR1"}],"orfNames":[{"value":"N0905"}],"olnNames":[{"value":"YNL244C"}]}],"length":108,"name":"Eukaryotic translation initiation factor eIF-1","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":25,"reference_id":"28297669","reference_source":"pmid","reference_html":"Molecular Landscape of the Ribosome Pre-initiation Complex during mRNA Scanning: Structural Role for eIF3c and Its Control by eIF5. <i> Obayashi E, Luna RE, Nagata T, Martin-Marcos P, Hiraishi H, Singh CR, Erzberger JP, Zhang F, Arthanari H, Morris J, Pellarin R, Moore C, Harmon I, Papadopoulos E, Yoshida H, Nasr ML, Unzai S, Thompson B, Aube E, Hustak S, Stengel F, Dagraca E, Ananbandam A, Gao P, Urano T, Hinnebusch AG, Wagner G, Asano K. </i> Cell Rep, 2017","date":"2023-07-19T10:38:55.900Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"2RVH"}],"region_id":"DP04130r001","statement":[{"text":"eIF1 comprises an unstructured N-terminal tail (NTT) and a globular domain with a β1-β2-α1-β3-β4-α2-β5 fold (Fletcher et al., 1999, Reibarkh et al., 2008) (Figure 3A; Table S4).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-19T14:45:11.648Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MSIENLKSFDPFADTGDDETATSNYIHIRIQQRNGRKTLTTVQGVPEEYDLKRILKVLKKDFACNGNIVKDPEMGEIIQLQGDQRAKVCEFMISQLGLQKKNIKIHGF","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.07407407407407407,"disorder_content":0.23148148148148148,"disprot_consensus":{"full":[{"start":1,"end":25,"type":"D"}],"Structural state":[{"start":1,"end":25,"type":"D"}]}},{"disprot_id":"DP04131","acc":"Q5TDH0","creator":"cpintado","date":"2023-07-19T10:47:25.703Z","features":{"pfam":[{"id":"PF00240","name":"Ubiquitin family","start":13,"end":77},{"id":"PF09668","name":"Aspartyl protease","start":227,"end":335},{"id":"PF24669","name":"Ddi2 HDD domain","start":133,"end":198}],"gene3D":[]},"genes":[{"name":{"value":"DDI2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:24578","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:24578"}}]}}],"length":399,"name":"Protein DDI1 homolog 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":116,"end":133,"reference_id":"27461074","reference_source":"pmid","reference_html":"Human DNA-Damage-Inducible 2 Protein Is Structurally and Functionally Distinct from Its Yeast Ortholog. <i> Sivá M, Svoboda M, Veverka V, Trempe JF, Hofmann K, Kožíšek M, Hexnerová R, Sedlák F, Belza J, Brynda J, Šácha P, Hubálek M, Starková J, Flaisigová I, Konvalinka J, Šašková KG. </i> Sci Rep, 2016","date":"2023-07-19T10:49:26.673Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5K57"}],"region_id":"DP04131r001","statement":[{"text":"Both the N- and C-terminal parts of HDD form unstructured linker regions, allowing flexibility between the individual structured domains of hDdi2.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-19T14:56:54.434Z"}},{"start":116,"end":133,"reference_id":"27461074","reference_source":"pmid","reference_html":"Human DNA-Damage-Inducible 2 Protein Is Structurally and Functionally Distinct from Its Yeast Ortholog. <i> Sivá M, Svoboda M, Veverka V, Trempe JF, Hofmann K, Kožíšek M, Hexnerová R, Sedlák F, Belza J, Brynda J, Šácha P, Hubálek M, Starková J, Flaisigová I, Konvalinka J, Šašková KG. </i> Sci Rep, 2016","date":"2023-07-19T10:49:47.556Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5K57"}],"region_id":"DP04131r002","statement":[{"text":"Both the N- and C-terminal parts of HDD form unstructured linker regions, allowing flexibility between the individual structured domains of hDdi2.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-19T14:56:57.291Z"}},{"start":192,"end":212,"reference_id":"27461074","reference_source":"pmid","reference_html":"Human DNA-Damage-Inducible 2 Protein Is Structurally and Functionally Distinct from Its Yeast Ortholog. <i> Sivá M, Svoboda M, Veverka V, Trempe JF, Hofmann K, Kožíšek M, Hexnerová R, Sedlák F, Belza J, Brynda J, Šácha P, Hubálek M, Starková J, Flaisigová I, Konvalinka J, Šašková KG. </i> Sci Rep, 2016","date":"2023-07-19T10:50:44.874Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5K57"}],"region_id":"DP04131r003","statement":[{"text":"Both the N- and C-terminal parts of HDD form unstructured linker regions, allowing flexibility between the individual structured domains of hDdi2.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-19T14:56:55.822Z"}},{"start":192,"end":212,"reference_id":"27461074","reference_source":"pmid","reference_html":"Human DNA-Damage-Inducible 2 Protein Is Structurally and Functionally Distinct from Its Yeast Ortholog. <i> Sivá M, Svoboda M, Veverka V, Trempe JF, Hofmann K, Kožíšek M, Hexnerová R, Sedlák F, Belza J, Brynda J, Šácha P, Hubálek M, Starková J, Flaisigová I, Konvalinka J, Šašková KG. </i> Sci Rep, 2016","date":"2023-07-19T10:50:58.891Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"5K57"}],"region_id":"DP04131r004","statement":[{"text":"Both the N- and C-terminal parts of HDD form unstructured linker regions, allowing flexibility between the individual structured domains of hDdi2.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-07-19T14:56:51.919Z"}}],"regions_counter":4,"released":"2024_06","sequence":"MLLTVYCVRRDLSEVTFSLQVDADFELHNFRALCELESGIPAAESQIVYAERPLTDNHRSLASYGLKDGDVVILRQKENADPRPPVQFPNLPRIDFSSIAVPGTSSPRQRQPPGTQQSHSSPGEITSSPQGLDNPALLRDMLLANPHELSLLKERNPPLAEALLSGDLEKFSRVLVEQQQDRARREQERIRLFSADPFDLEAQAKIEEDIRQQNIEENMTIAMEEAPESFGQVVMLYINCKVNGHPVKAFVDSGAQMTIMSQACAERCNIMRLVDRRWAGIAKGVGTQKIIGRVHLAQVQIEGDFLPCSFSILEEQPMDMLLGLDMLKRHQCSIDLKKNVLVIGTTGSQTTFLPEGELPECARLAYGAGREDVRPEEIADQELAEALQKSAEDAERQKP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.15538847117794485,"disorder_content":0.09774436090225563,"disprot_consensus":{"full":[{"start":116,"end":133,"type":"D"},{"start":192,"end":212,"type":"D"}],"Structural state":[{"start":116,"end":133,"type":"D"},{"start":192,"end":212,"type":"D"}],"Disorder function":[{"start":116,"end":133,"type":"F"},{"start":192,"end":212,"type":"F"}]}},{"disprot_id":"DP04132","acc":"Q9NZC2","creator":"tlazar","date":"2023-08-04T17:56:40.719Z","features":{"pfam":[{"id":"PF07686","name":"Immunoglobulin V-set domain","start":23,"end":128}],"gene3D":[]},"genes":[{"name":{"value":"TREM2"}}],"length":230,"name":"Triggering receptor expressed on myeloid cells 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":131,"end":174,"reference_id":"29794134","reference_source":"pmid","reference_html":"Molecular basis for the loss-of-function effects of the Alzheimer's disease-associated R47H variant of the immune receptor TREM2. <i> Sudom A, Talreja S, Danao J, Bragg E, Kegel R, Min X, Richardson J, Zhang Z, Sharkov N, Marcora E, Thibault S, Bradley J, Wood S, Lim AC, Chen H, Wang S, Foltz IN, Sambashivan S, Wang Z. </i> J Biol Chem, 2018","date":"2023-08-04T18:23:40.074Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asn20Asp","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"For the WT TREM2 protein, the TREM2 gene encoding the human TREM2 signal peptide and extracellular domain (residues 1–174) with the N20D mutation to eliminate glycosylation and improve protein stability was subcloned into a pTT5 vector with a C-terminal tobacco etch virus cleavage site and His6 tag."}]},{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"For the WT TREM2 protein, the TREM2 gene encoding the human TREM2 signal peptide and extracellular domain (residues 1–174) with the N20D mutation to eliminate glycosylation and improve protein stability was subcloned into a pTT5 vector with a C-terminal tobacco etch virus cleavage site and His6 tag."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"For the WT TREM2 protein, the TREM2 gene encoding the human TREM2 signal peptide and extracellular domain (residues 1–174) with the N20D mutation to eliminate glycosylation and improve protein stability was subcloned into a pTT5 vector with a C-terminal tobacco etch virus cleavage site and His6 tag."}]}],"cross_refs":[{"db":"PDB","id":"6B8O"}],"region_id":"DP04132r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":1,"db":"PubChem","id":"CID:49859737","statements":[{"type":"Methods","text":"WT TREM2 crystals were then soaked with 1 mm PS for 3 h before being frozen for data collection."}]}],"sequence_construct":"HDTTVFQGVAGQSLQVSCPYDSMKHWGRRKAWCRQLGEKGPCQRVVSTHNLWLLSFLRRWNGSTAITDDTLGGTLTITLRNLQPHDAGLYQCQSLHGSEADTLRKVLVEVLADPLDHRDAGDLWFPGESESFEDAHVEHSISRSLLEGEIPFPPTSENLYFQGHHHHHH","statement":[{"text":"Residues 19–21 and 130–140 were also disordered in the PS-soaked structure.","type":"Results"},{"text":"Residue 130 was only modeled in one chain, residues 131-174 were not resolvable in any of the protein chains due their disordered nature.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-08T13:59:32.292Z"}},{"start":189,"end":206,"reference_id":"32830336","reference_source":"pmid","reference_html":"γ-Secretase cleavage of the Alzheimer risk factor TREM2 is determined by its intrinsic structural dynamics. <i> Steiner A, Schlepckow K, Brunner B, Steiner H, Haass C, Hagn F. </i> EMBO J, 2020","date":"2023-08-07T18:11:33.095Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"BMRB","id":"50263"},{"db":"PDB","id":"6Z0G"}],"region_id":"DP04132r002","statement":[{"text":"As determined here for TREM2, an unfolded region manifested by an extreme drop in the order parameter can be intrinsically present in a substrate TMH and oriented toward the outside of the hydrophobic membrane interior. The most critical amino acid residue in TREM2‐TMH is the positively charged K186, that is located within the hydrophobic interior of the membrane and which is required for complex formation with DAP12 (Fig 2). Without DAP12, the presence of an unpaired charge in the membrane leads to the formation of a partially unwound helical region with increased conformational dynamics.","type":"Discussion"},{"text":"S2 values of around 0.9 for the ordered first half of the TMH, of around 0.6 for the unstructured kink region, and 0.7 for the C‐terminal helix can be extracted.","type":"Results"},{"text":"Strikingly, the site of intramembrane cleavage of wt TREM2 correlates well with the observed enhanced dynamics between amino acids 189 and 193 (Fig 3A).","type":"Results"},{"text":"Taken together, these data establish that structural dynamics of TREM2 at the C‐terminal end of the TMH determine the site where the initial ε‐cleavage takes place.","type":"Results"}],"sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":300,"db":"ChEBI","id":"78018","statements":[{"type":"Results","text":"Next, using a U-2H, 13C, 15N-labeled TREM2-TMH (aa 161–206) sample in 300 mM DPC micelles, NMR backbone resonance assignments were obtained for 88% or all non-proline residues using a set of 3D-triple resonance experiments at 37°C (Fig 1B)."}],"entry_name":"dodecylphosphocholine"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-08T13:58:46.906Z"}},{"start":189,"end":198,"reference_id":"32830336","reference_source":"pmid","reference_html":"γ-Secretase cleavage of the Alzheimer risk factor TREM2 is determined by its intrinsic structural dynamics. <i> Steiner A, Schlepckow K, Brunner B, Steiner H, Haass C, Hagn F. </i> EMBO J, 2020","date":"2023-08-07T18:15:12.073Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"BMRB","id":"50263"},{"db":"BMRB","id":"50265"},{"db":"PDB","id":"6Z0G"},{"db":"PDB","id":"6Z0I"}],"region_id":"DP04132r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O43914","statements":[{"type":"Results","text":"TREM2‐TMH structure is stabilized by binding to DAP12 or by charge removal"}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":300,"db":"ChEBI","id":"78018","statements":[{"type":"Results","text":"Next, using a U-2H, 13C, 15N-labeled TREM2-TMH (aa 161–206) sample in 300 mM DPC micelles, NMR backbone resonance assignments were obtained for 88% or all non-proline residues using a set of 3D-triple resonance experiments at 37°C (Fig 1B)."}],"entry_name":"dodecylphosphocholine"}],"statement":[{"text":"TREM2‐TMH structure is stabilized by binding to DAP12 or by charge removal","type":"Results"},{"text":"In line with the previous finding that DAP12 binding leads to TREM2‐CTF stabilization (Zhong et al, 2015), we here were able to show that this interaction leads to the formation of a continuous α‐helix ranging from residues 173 to 198 without the previously kinked region (Fig 2D, Table 1). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-08T14:00:24.667Z"}},{"start":190,"end":194,"reference_id":"32830336","reference_source":"pmid","reference_html":"γ-Secretase cleavage of the Alzheimer risk factor TREM2 is determined by its intrinsic structural dynamics. <i> Steiner A, Schlepckow K, Brunner B, Steiner H, Haass C, Hagn F. </i> EMBO J, 2020","date":"2023-08-07T18:18:16.591Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000048","term_name":"limited proteolysis display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007184","ec_ontology":"ECO","ec_name":"protein mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04132r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P49768"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P49810"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q96BI3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NZ42"}],"statement":[{"text":"Immunoprecipitation of the soluble fraction using an anti‐HA antibody revealed γ‐secretase‐dependent generation of the TREM2 ICD (Fig 5B). Immunoprecipitated ICDs were subjected to mass spectrometry as described previously (Fleck et al, 2016). This revealed a major peak at 5596,20 Da for wt TREM2, which was absent at 4°C and reduced upon treatment with L‐685,458 (Fig 5C). This peak corresponds to a major ε‐cleavage site after amino acid 192 within the TMH (Fig 5C–E).","type":"Results"},{"text":"MALDI MS analysis of the ε‐cleavage sites of wt and mutant TREM2 C‐terminal fragments. Mass spectrometry reveals ε‐cleavage C‐terminal of A192 for the wt CTF.","type":"Figure"},{"text":"Interestingly, the K186A mutation, which strongly stabilizes the α‐helical structure of the TREM2 TMH, abolishes cleavage after amino acid 192 and shifts the ε‐cleavage to a new site after amino acid 195 and to a lower extent to 193 (Fig 5C–E).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-08T14:00:37.103Z"}}],"regions_counter":5,"released":"2024_06","sequence":"MEPLRLLILLFVTELSGAHNTTVFQGVAGQSLQVSCPYDSMKHWGRRKAWCRQLGEKGPCQRVVSTHNLWLLSFLRRWNGSTAITDDTLGGTLTITLRNLQPHDAGLYQCQSLHGSEADTLRKVLVEVLADPLDHRDAGDLWFPGESESFEDAHVEHSISRSLLEGEIPFPPTSILLLLACIFLIKILAASALWAAAWHGQKPGTHPPSELDCGHDPGYQLQTLPGLRDT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.22608695652173913,"dataset":["Age-related disorders proteins"],"disorder_content":0.26956521739130435,"disprot_consensus":{"full":[{"start":131,"end":174,"type":"D"},{"start":189,"end":198,"type":"T"},{"start":199,"end":206,"type":"D"}],"Structural state":[{"start":131,"end":174,"type":"D"},{"start":189,"end":206,"type":"D"}],"Structural transition":[{"start":189,"end":198,"type":"T"}],"Disorder function":[{"start":190,"end":194,"type":"F"}]}},{"disprot_id":"DP04133","acc":"P02649","creator":"tlazar","date":"2023-08-04T20:45:02.376Z","features":{"pfam":[{"id":"PF01442","name":"Apolipoprotein A1/A4/E domain","start":81,"end":288}],"gene3D":[]},"genes":[{"name":{"value":"APOE","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:613","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:613"}}]}}],"length":317,"name":"Apolipoprotein E","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":19,"end":40,"reference_id":"8756331","reference_source":"pmid","reference_html":"Novel mechanism for defective receptor binding of apolipoprotein E2 in type III hyperlipoproteinemia. <i> Dong LM, Parkin S, Trakhanov SD, Rupp B, Simmons T, Arnold KS, Newhouse YM, Innerarity TL, Weisgraber KH. </i> Nat Struct Biol, 1996","date":"2023-08-04T20:54:57.051Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1NFN"}],"region_id":"DP04133r001","statement":[{"text":"The apoE3 model contains residues 23-81 and 92-164 whereas the apoE2 Ala-154 model is truncated at glutamine 163. The missing residues, which constitute about 30% of the full 22,000 M, fragment are all located at one extreme of the four-helix bundle. We believe them to be completely disordered and thus indicate a likely cause of the rather high terminal R-values.","type":"Methods"},{"text":"The numbering applied by the authors is without the 18-residue-long signal peptide.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T14:43:35.209Z"}},{"start":100,"end":109,"reference_id":"8756331","reference_source":"pmid","reference_html":"Novel mechanism for defective receptor binding of apolipoprotein E2 in type III hyperlipoproteinemia. <i> Dong LM, Parkin S, Trakhanov SD, Rupp B, Simmons T, Arnold KS, Newhouse YM, Innerarity TL, Weisgraber KH. </i> Nat Struct Biol, 1996","date":"2023-08-04T20:56:04.616Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1NFN"}],"region_id":"DP04133r002","statement":[{"text":"The apoE3 model contains residues 23-81 and 92-164 whereas the apoE2 Ala-154 model is truncated at glutamine 163. The missing residues, which constitute about 30% of the full 22,000 M, fragment are all located at one extreme of the four-helix bundle. We believe them to be completely disordered and thus indicate a likely cause of the rather high terminal R-values.","type":"Methods"},{"text":"The numbering applied by the authors is without the 18-residue-long signal peptide.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T14:43:43.015Z"}},{"start":183,"end":209,"reference_id":"8756331","reference_source":"pmid","reference_html":"Novel mechanism for defective receptor binding of apolipoprotein E2 in type III hyperlipoproteinemia. <i> Dong LM, Parkin S, Trakhanov SD, Rupp B, Simmons T, Arnold KS, Newhouse YM, Innerarity TL, Weisgraber KH. </i> Nat Struct Biol, 1996","date":"2023-08-04T20:57:31.308Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1NFN"}],"region_id":"DP04133r003","statement":[{"text":"The apoE3 model contains residues 23-81 and 92-164 whereas the apoE2 Ala-154 model is truncated at glutamine 163. The missing residues, which constitute about 30% of the full 22,000 M, fragment are all located at one extreme of the four-helix bundle. We believe them to be completely disordered and thus indicate a likely cause of the rather high terminal R-values.","type":"Methods"},{"text":"The numbering applied by the authors is without the 18-residue-long signal peptide.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T14:43:49.742Z"}},{"start":184,"end":242,"reference_id":"3360781","reference_source":"pmid","reference_html":"Human apolipoprotein E3 in aqueous solution. I. Evidence for two structural domains. <i> Wetterau JR, Aggerbeck LP, Rall SC, Weisgraber KH. </i> J Biol Chem, 1988","date":"2023-08-04T21:32:28.575Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001191","ec_ontology":"ECO","ec_name":"in vitro cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04133r004","statement":[{"text":"The results clearly demonstrate that apoE3 contains two proteolytic-resistant regions separated by a region, residues 166-224, that is highly susceptible to proteolysis. The results are consistent with apoE3 containing two domains, an amino-terminal domain containing residues 20-165 and a carboxyl-terminal domain containing residues 225-299.","type":"Methods"},{"text":"The numbering applied by the authors is without the 18-residue-long signal peptide.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T14:45:49.755Z"}},{"start":19,"end":41,"reference_id":"36749730","reference_source":"pmid","reference_html":"Apolipoprotein E4 has extensive conformational heterogeneity in lipid-free and lipid-bound forms. <i> Stuchell-Brereton MD, Zimmerman MI, Miller JJ, Mallimadugula UL, Incicco JJ, Roy D, Smith LG, Cubuk J, Baban B, DeKoster GT, Frieden C, Bowman GR, Soranno A. </i> Proc Natl Acad Sci U S A, 2023","date":"2023-08-04T21:51:28.514Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04133r005","statement":[{"text":"ApoE comprises four different regions: the N-terminal tail (residues 1 to 23), the four-helix bundle (24 to 167) (20–22), the hinge region (168 to 205), and the C-terminal domain (206 to 299) (Fig. 1).","type":"Results"},{"text":"Conversely, the population at higher transfer efficiency follows the expected trend of a dynamic conformational ensemble, that is, an ensemble of interdye distances that are sampled in a timescale much shorter than the residence time of the protein in the confocal volume. Interestingly, the results are better described using a wormlike chain distribution with persistence length lp (an estimate of the minimal flexible segment) equal to 2.5 nm and contour length lc (the maximum extension of the probed region) equal to 7.7 nm (SI Appendix, Fig. S2).","type":"Results"},{"text":"The numbering applied by the authors is without the 18-residue-long signal peptide.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T14:47:12.512Z"}},{"start":186,"end":223,"reference_id":"36749730","reference_source":"pmid","reference_html":"Apolipoprotein E4 has extensive conformational heterogeneity in lipid-free and lipid-bound forms. <i> Stuchell-Brereton MD, Zimmerman MI, Miller JJ, Mallimadugula UL, Incicco JJ, Roy D, Smith LG, Cubuk J, Baban B, DeKoster GT, Frieden C, Bowman GR, Soranno A. </i> Proc Natl Acad Sci U S A, 2023","date":"2023-08-04T21:51:40.852Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04133r006","statement":[{"text":"ApoE comprises four different regions: the N-terminal tail (residues 1 to 23), the four-helix bundle (24 to 167) (20–22), the hinge region (168 to 205), and the C-terminal domain (206 to 299) (Fig. 1).","type":"Results"},{"text":"The population associated with lower mean transfer efficiency (E = 0.62 ± 0.02) accounts for 60% of the observed molecules, whereas the high transfer efficiency population (E = 0.83 ± 0.02) accounts for the remaining 40%, corresponding to a free energy difference between these states of 1.0 ± 0.2 RT (SI Appendix, Tables S1 and S2). The asymmetry of the distribution persists with increasing denaturant concentrations, with both populations shifting toward lower transfer efficiencies (Fig. 3), as expected for disordered or partially disordered regions (31). Comparing lifetime and transfer efficiency indicates that both populations reflect dynamic averages that, similar to the case of the N-terminal tail, we can describe in terms of a wormlike chain (SI Appendix, Fig. S2).","type":"Results"},{"text":"The numbering applied by the authors is without the 18-residue-long signal peptide.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T14:47:32.160Z"}},{"start":19,"end":40,"reference_id":"2063194","reference_source":"pmid","reference_html":"Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E. <i> Wilson C, Wardell MR, Weisgraber KH, Mahley RW, Agard DA. </i> Science, 1991","date":"2023-08-04T22:08:34.450Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1LPE"}],"region_id":"DP04133r007","statement":[{"text":"Our final model lacks amino acid residues 1 to 22 and 167 to 191. At both ends of the modeled region, density is well determined but quickly disappears outside the model. Electrophoresis of the crystalized protein demonstrated that the complete 22-kD fragment was present; that is,the missing regions were not absent as a result of proteolysis. We believe residues 1 to 22 and 167 to 191 are disordered in the crystal and are not missing because of systematic phasing errors","type":"Results"},{"text":"The numbering applied by the authors is without the 18-residue-long signal peptide.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T14:48:36.172Z"}},{"start":185,"end":209,"reference_id":"2063194","reference_source":"pmid","reference_html":"Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E. <i> Wilson C, Wardell MR, Weisgraber KH, Mahley RW, Agard DA. </i> Science, 1991","date":"2023-08-04T22:08:48.292Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"PDB","id":"1LPE"}],"region_id":"DP04133r008","statement":[{"text":"Our final model lacks amino acid residues 1 to 22 and 167 to 191. At both ends of the modeled region, density is well determined but quickly disappears outside the model. Electrophoresis of the crystalized protein demonstrated that the complete 22-kD fragment was present; that is,the missing regions were not absent as a result of proteolysis. We believe residues 1 to 22 and 167 to 191 are disordered in the crystal and are not missing because of systematic phasing errors","type":"Results"},{"text":"The numbering applied by the authors is without the 18-residue-long signal peptide.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T14:48:37.034Z"}},{"start":183,"end":209,"reference_id":"2063194","reference_source":"pmid","reference_html":"Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E. <i> Wilson C, Wardell MR, Weisgraber KH, Mahley RW, Agard DA. </i> Science, 1991","date":"2023-08-04T22:11:59.137Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001191","ec_ontology":"ECO","ec_name":"in vitro cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04133r009","statement":[{"text":"Digestion of apoE with a battery of proteases shows that amino acids 1 to 20 and 165 to 191 are susceptible to proteolysis and thus likely to be unstructured (Fig.1) (2).","type":"Results"},{"text":"The numbering applied by the authors is without the 18-residue-long signal peptide.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T14:51:00.121Z"}},{"start":19,"end":38,"reference_id":"2063194","reference_source":"pmid","reference_html":"Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E. <i> Wilson C, Wardell MR, Weisgraber KH, Mahley RW, Agard DA. </i> Science, 1991","date":"2023-08-04T22:12:15.018Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001191","ec_ontology":"ECO","ec_name":"in vitro cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04133r010","statement":[{"text":"Digestion of apoE with a battery of proteases shows that amino acids 1 to 20 and 165 to 191 are susceptible to proteolysis and thus likely to be unstructured (Fig.1) (2).","type":"Results"},{"text":"The numbering applied by the authors is without the 18-residue-long signal peptide.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-08-07T14:51:01.605Z"}}],"regions_counter":10,"released":"2024_06","sequence":"MKVLWAALLVTFLAGCQAKVEQAVETEPEPELRQQTEWQSGQRWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELRALMDETMKELKAYKSELEEQLTPVAEETRARLSKELQAAQARLGADMEDVCGRLVQYRGEVQAMLGQSTEELRVRLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGLSAIRERLGPLVEQGRVRAATVGSLAGQPLQERAQAWGERLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQIRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGTSAAPVPSDNH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.14826498422712933,"dataset":["Condensates-related proteins","Age-related disorders proteins"],"disorder_content":0.29337539432176657,"disprot_consensus":{"full":[{"start":19,"end":41,"type":"D"},{"start":100,"end":109,"type":"D"},{"start":183,"end":242,"type":"D"}],"Structural state":[{"start":19,"end":41,"type":"D"},{"start":100,"end":109,"type":"D"},{"start":183,"end":242,"type":"D"}]}},{"disprot_id":"DP04134","acc":"O54918-2","creator":"vnugnes","date":"2023-08-22T17:02:32.797Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"Bcl2l11"},"synonyms":[{"value":"Bim"}]}],"length":140,"name":"Isoform BimL of Bcl-2-like protein 11","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":1,"end":113,"reference_id":"16645638","reference_source":"pmid","reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2023-08-22T17:05:14.176Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04134r001","statement":[{"text":"During purification, BimLΔC27 was observed to be highly protease sensitive and behaved as a larger protein, migrating in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) as an approximately 16 kDa protein and eluting from gel filtration columns with an apparent molecular weight of ∼25 kDa (see Figure 3a).","type":"Results"},{"text":"Elution as a larger protein when analyzed by size exclusion chromatography, and sensitivity to proteases, are both properties commonly observed for IUPs and suggest that BimLΔC27 may be disordered in solution.","type":"Results"}]},{"start":1,"end":113,"reference_id":"16645638","reference_source":"pmid","reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2023-08-22T17:05:26.387Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04134r002","statement":[{"text":"During purification, BimLΔC27 was observed to be highly protease sensitive and behaved as a larger protein, migrating in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) as an approximately 16 kDa protein and eluting from gel filtration columns with an apparent molecular weight of ∼25 kDa (see Figure 3a).","type":"Results"},{"text":"Elution as a larger protein when analyzed by size exclusion chromatography, and sensitivity to proteases, are both properties commonly observed for IUPs and suggest that BimLΔC27 may be disordered in solution.","type":"Results"}]},{"start":1,"end":113,"reference_id":"16645638","reference_source":"pmid","reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2023-08-22T17:06:39.563Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04134r003","statement":[{"text":"The CD spectra obtained for BimLΔC27 over the range 5–65°C is characteristic of an unstructured protein, although the slight inflection near 222 nm may indicate some residual α-helical structure, but this is not enhanced at lower temperatures as seen for some proteins (Figure 2b).","type":"Results"}]},{"start":1,"end":113,"reference_id":"16645638","reference_source":"pmid","reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2023-08-22T17:07:18.055Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04134r004","statement":[{"text":"In the 1H-15N-HSQC spectrum (Figure 2c), the backbone amide resonances fall between 8.0 and 8.5 p.p.m., and there is little dispersion in the aliphatic region in the 1D 1H NMR spectrum (data not shown). The sharp resonances and lack of chemical shift dispersion reflect the intrinsic mobility and lack of long-range order in BimLΔC27.","type":"Results"}]},{"start":76,"end":113,"reference_id":"16645638","reference_source":"pmid","reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2023-08-22T17:15:50.661Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P70345","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04134r005","statement":[{"text":"When Bcl-wΔC10 and BimLΔC27 were mixed before trypsin digestion, a different proteolytic profile was obtained (Figure 3b, lanes 8 and 9). Mass spectrometry analysis of the peptide mixtures revealed changes consistent with complex formation. ","type":"Results"},{"text":"The mass of the new peptide corresponds to that expected for a peptide derived from the C-terminus of BimLΔC27 (sequence shown at the bottom of Figure 3b). This peptide includes the BH3 domain and suggests that interaction with the hydrophobic binding groove protects the BH3 domain and the hydrophobic groove of Bcl-w from proteolysis.","type":"Results"},{"text":"Together, these results suggest that Bim remains largely unstructured in the presence of prosurvival proteins and that only a limited conformational change of just the BH3 domain is associated with binding.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":76,"end":113,"reference_id":"16645638","reference_source":"pmid","reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2023-11-21T12:13:00.628Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04134r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P70345"}],"statement":[{"text":"When Bcl-wΔC10 and BimLΔC27 were mixed before trypsin digestion, a different proteolytic profile was obtained (Figure 3b, lanes 8 and 9). Mass spectrometry analysis of the peptide mixtures revealed changes consistent with complex formation.","type":"Results"},{"text":"The mass of the new peptide corresponds to that expected for a peptide derived from the C-terminus of BimLΔC27 (sequence shown at the bottom of Figure 3b). This peptide includes the BH3 domain and suggests that interaction with the hydrophobic binding groove protects the BH3 domain and the hydrophobic groove of Bcl-w from proteolysis.","type":"Results"},{"text":"Together, these results suggest that Bim remains largely unstructured in the presence of prosurvival proteins and that only a limited conformational change of just the BH3 domain is associated with binding.","type":"Results"}],"states_connection":[{"source":"DP04134r001","target":"DP04134r010"}]},{"start":83,"end":108,"reference_id":"16645638","reference_source":"pmid","reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2023-11-21T12:10:30.601Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04134r007","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P70345"}],"statement":[{"text":"A localized conformational change is supported by comparison of the 1H-15N-HSQC spectra for 15N-labeled BimLΔC27 in the presence and absence of Bcl-w (Figure 3c).","type":"Results"},{"text":"The new peaks in the 15N-BimLΔC27/Bcl-wΔC10 complex spectra primarily arise from interaction of the BH3 domain with Bcl-w as addition of Bcl-wΔC10 to 15N-labeled BimBH3 (a peptide including residues 83–108 of mouse BimL) results in similar shifts (Figure 3d).","type":"Results"},{"text":"The few differences seen are likely due to end effects. The comparable binding constants observed for Bcl-w binding to BimLΔC27 protein (32 nM) and the BimBH3 peptide (22 nM)29 supports this conclusion.","type":"Results"}],"states_connection":[{"source":"DP04134r004","target":"DP04134r009"}]},{"start":83,"end":108,"reference_id":"16645638","reference_source":"pmid","reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2025-06-16T14:18:23.658Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P70345","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04134r008","statement":[{"text":"A localized conformational change is supported by comparison of the 1H-15N-HSQC spectra for 15N-labeled BimLΔC27 in the presence and absence of Bcl-w (Figure 3c).","type":"Results"},{"text":"The new peaks in the 15N-BimLΔC27/Bcl-wΔC10 complex spectra primarily arise from interaction of the BH3 domain with Bcl-w as addition of Bcl-wΔC10 to 15N-labeled BimBH3 (a peptide including residues 83–108 of mouse BimL) results in similar shifts (Figure 3d). ","type":"Results"},{"text":"The few differences seen are likely due to end effects. The comparable binding constants observed for Bcl-w binding to BimLΔC27 protein (32 nM) and the BimBH3 peptide (22 nM)29 supports this conclusion.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":83,"end":108,"reference_id":"16645638","reference_source":"pmid","reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2023-11-21T12:10:08.899Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04134r009","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P70345"}],"statement":[{"text":"A localized conformational change is supported by comparison of the 1H-15N-HSQC spectra for 15N-labeled BimLΔC27 in the presence and absence of Bcl-w (Figure 3c).","type":"Results"},{"text":"The new peaks in the 15N-BimLΔC27/Bcl-wΔC10 complex spectra primarily arise from interaction of the BH3 domain with Bcl-w as addition of Bcl-wΔC10 to 15N-labeled BimBH3 (a peptide including residues 83–108 of mouse BimL) results in similar shifts (Figure 3d).","type":"Results"}]},{"start":76,"end":113,"reference_id":"16645638","reference_source":"pmid","reference_html":"Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. <i> Hinds MG, Smits C, Fredericks-Short R, Risk JM, Bailey M, Huang DC, Day CL. </i> Cell Death Differ, 2007","date":"2023-11-21T12:12:35.095Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04134r010","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P70345"}],"statement":[{"text":"When Bcl-wΔC10 and BimLΔC27 were mixed before trypsin digestion, a different proteolytic profile was obtained (Figure 3b, lanes 8 and 9). Mass spectrometry analysis of the peptide mixtures revealed changes consistent with complex formation.","type":"Results"},{"text":"The mass of the new peptide corresponds to that expected for a peptide derived from the C-terminus of BimLΔC27 (sequence shown at the bottom of Figure 3b). This peptide includes the BH3 domain and suggests that interaction with the hydrophobic binding groove protects the BH3 domain and the hydrophobic groove of Bcl-w from proteolysis.","type":"Results"},{"text":"Together, these results suggest that Bim remains largely unstructured in the presence of prosurvival proteins and that only a limited conformational change of just the BH3 domain is associated with binding.","type":"Results"}]}],"regions_counter":10,"released":"2024_06","sequence":"MAKQPSDVSSECDREGGQLQPAERPPQLRPGAPTSLQTEPQDRSPAPMSCDKSTQTPSPPCQAFNHYLSAMASIRQSQEEPEDLRPEIRIAQELRRIGDEFNETYTRRVFANDYREAEDHPQMVILQLLRFIFRLVWRRH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"disorder_content":0.8071428571428572,"disprot_consensus":{"full":[{"start":1,"end":75,"type":"D"},{"start":76,"end":113,"type":"T"}],"Structural state":[{"start":1,"end":113,"type":"D"}],"Molecular function":[{"start":76,"end":113,"type":"F"}],"Structural transition":[{"start":76,"end":113,"type":"T"}]}},{"disprot_id":"DP04135","acc":"Q92800","creator":"eleonardi","date":"2023-08-30T12:50:48.232Z","features":{"pfam":[{"id":"PF00856","name":"SET domain","start":624,"end":727},{"id":"PF11616","name":"WD repeat binding protein EZH2","start":39,"end":68},{"id":"PF18118","name":"Polycomb repressive complex 2 tri-helical domain","start":159,"end":262},{"id":"PF18264","name":"CXC domain","start":560,"end":591},{"id":"PF21358","name":"Ezh2, MCSS domain","start":270,"end":322}],"gene3D":[]},"genes":[{"name":{"value":"EZH1"},"synonyms":[{"value":"KIAA0388"}]}],"length":747,"name":"Histone-lysine N-methyltransferase EZH1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":30,"reference_id":"33514705","reference_source":"pmid","reference_html":"Structures of monomeric and dimeric PRC2:EZH1 reveal flexible modules involved in chromatin compaction. <i> Grau D, Zhang Y, Lee CH, Valencia-Sánchez M, Zhang J, Wang M, Holder M, Svetlov V, Tan D, Nudler E, Reinberg D, Walz T, Armache KJ. </i> Nat Commun, 2021","date":"2023-09-05T14:41:02.193Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-23021"},{"db":"PDB","id":"7KSO"}],"region_id":"DP04135r001","statement":[{"text":"This region lacks electron density in the PDB structure of the Polycomb Repressive Complex 2 (PRC2:EZH1) bound to AEBP2 and JARID2, indicating it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":"not relevant","value":null,"db":"UniProt","id":"Q09028","statements":[{"type":"Results","text":"Using a five-component PRC2 containing human EZH1, EED, SUZ12, RBAP48, and AEBP2 (Fig. 1a), we determined a structure at 4.1-Å resolution (Supplementary Fig. 1). The addition of a biologically active fragment of JARID2, containing residues 96–367 (Fig. 1a), allowed us to improve the resolution to 3.9 Å (Fig. 1b and Supplementary Figs. 2, 3a–c)15,18."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":"not relevant","value":null,"db":"UniProt","id":"Q15022","statements":[{"type":"Results","text":"Using a five-component PRC2 containing human EZH1, EED, SUZ12, RBAP48, and AEBP2 (Fig. 1a), we determined a structure at 4.1-Å resolution (Supplementary Fig. 1). The addition of a biologically active fragment of JARID2, containing residues 96–367 (Fig. 1a), allowed us to improve the resolution to 3.9 Å (Fig. 1b and Supplementary Figs. 2, 3a–c)15,18."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":"not relevant","value":null,"db":"UniProt","id":"O75530","statements":[{"type":"Results","text":"Using a five-component PRC2 containing human EZH1, EED, SUZ12, RBAP48, and AEBP2 (Fig. 1a), we determined a structure at 4.1-Å resolution (Supplementary Fig. 1). The addition of a biologically active fragment of JARID2, containing residues 96–367 (Fig. 1a), allowed us to improve the resolution to 3.9 Å (Fig. 1b and Supplementary Figs. 2, 3a–c)15,18."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":"not relevant","value":null,"db":"ChEBI","id":"29105","statements":[{"type":"Methods","text":"Zinc atoms were rigid-body fit into the appropriate density based on PDB: 5HYN."}],"entry_name":"zinc(2+)"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92833"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6ZN18"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-10-09T13:46:34.656Z"}},{"start":728,"end":747,"reference_id":"33514705","reference_source":"pmid","reference_html":"Structures of monomeric and dimeric PRC2:EZH1 reveal flexible modules involved in chromatin compaction. <i> Grau D, Zhang Y, Lee CH, Valencia-Sánchez M, Zhang J, Wang M, Holder M, Svetlov V, Tan D, Nudler E, Reinberg D, Walz T, Armache KJ. </i> Nat Commun, 2021","date":"2023-09-05T08:36:33.203Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-23021"},{"db":"PDB","id":"7KSO"}],"region_id":"DP04135r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09028"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15022"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75530"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92833"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6ZN18"}],"statement":[{"text":"This region lacks electron density in the PDB structure of the Polycomb Repressive Complex 2 (PRC2:EZH1) bound to AEBP2 and JARID2, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-09-05T13:38:18.948Z"}},{"start":125,"end":271,"reference_id":"33514705","reference_source":"pmid","reference_html":"Structures of monomeric and dimeric PRC2:EZH1 reveal flexible modules involved in chromatin compaction. <i> Grau D, Zhang Y, Lee CH, Valencia-Sánchez M, Zhang J, Wang M, Holder M, Svetlov V, Tan D, Nudler E, Reinberg D, Walz T, Armache KJ. </i> Nat Commun, 2021","date":"2023-09-05T08:33:16.260Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-23021"},{"db":"PDB","id":"7KSO"}],"region_id":"DP04135r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09028"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15022"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75530"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92833"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6ZN18"}],"statement":[{"text":"Aside from a different build of AEBP2 (Supplementary Fig. 3f, g), the overall structure of PRC2:EZH1 is very similar to that of PRC2:EZH228. However, we did note that several loops are disordered in both PRC2:EZH1 and PRC2:EZH2, making us wonder whether any functional differences could be explained by differences contained in these loops (Supplementary Fig. 4a, b).","type":"Results"},{"text":"Supplementary Fig. 4: Regulatory domains of EZH1 are flexible.\na, Cartoon representation of domains that are visible in the cryo-EM density of EZH1. b, Depiction of the key\nunstructured loops in EZH1. Labels indicate the last structured residues flanking the flexible loops in EZH1. c,\nSequence comparison of the flexible loops in EZH1 and EZH2. Underlined sequences represent regions rich in\nbasic (blue) or acidic residues (red), RNA-interaction domains (purple), and automethylation sites (green). Acidic\nor basic regions are based on manual inspection of the EZH1/2 sequences. RNA-interaction domains and\nautomethylation sites are based on reports describing EZH2 features63-66.","type":"Supplementary material"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-09-05T13:38:03.996Z"}},{"start":323,"end":431,"reference_id":"33514705","reference_source":"pmid","reference_html":"Structures of monomeric and dimeric PRC2:EZH1 reveal flexible modules involved in chromatin compaction. <i> Grau D, Zhang Y, Lee CH, Valencia-Sánchez M, Zhang J, Wang M, Holder M, Svetlov V, Tan D, Nudler E, Reinberg D, Walz T, Armache KJ. </i> Nat Commun, 2021","date":"2023-09-05T08:32:18.311Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-23021"},{"db":"PDB","id":"7KSO"}],"region_id":"DP04135r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09028"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15022"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75530"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92833"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6ZN18"}],"statement":[{"text":"Aside from a different build of AEBP2 (Supplementary Fig. 3f, g), the overall structure of PRC2:EZH1 is very similar to that of PRC2:EZH228. However, we did note that several loops are disordered in both PRC2:EZH1 and PRC2:EZH2, making us wonder whether any functional differences could be explained by differences contained in these loops (Supplementary Fig. 4a, b).","type":"Results"},{"text":"Supplementary Fig. 4: Regulatory domains of EZH1 are flexible.\na, Cartoon representation of domains that are visible in the cryo-EM density of EZH1. b, Depiction of the key\nunstructured loops in EZH1. Labels indicate the last structured residues flanking the flexible loops in EZH1. c,\nSequence comparison of the flexible loops in EZH1 and EZH2. Underlined sequences represent regions rich in\nbasic (blue) or acidic residues (red), RNA-interaction domains (purple), and automethylation sites (green). Acidic\nor basic regions are based on manual inspection of the EZH1/2 sequences. RNA-interaction domains and\nautomethylation sites are based on reports describing EZH2 features63-66.","type":"Supplementary material"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-09-05T13:37:38.313Z"}},{"start":478,"end":517,"reference_id":"33514705","reference_source":"pmid","reference_html":"Structures of monomeric and dimeric PRC2:EZH1 reveal flexible modules involved in chromatin compaction. <i> Grau D, Zhang Y, Lee CH, Valencia-Sánchez M, Zhang J, Wang M, Holder M, Svetlov V, Tan D, Nudler E, Reinberg D, Walz T, Armache KJ. </i> Nat Commun, 2021","date":"2023-09-05T08:31:06.493Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2023_12","version":0,"cross_refs":[{"db":"EMDB","id":"EMD-23021"},{"db":"PDB","id":"7KSO"}],"region_id":"DP04135r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09028"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15022"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75530"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92833"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6ZN18"}],"statement":[{"text":"Aside from a different build of AEBP2 (Supplementary Fig. 3f, g), the overall structure of PRC2:EZH1 is very similar to that of PRC2:EZH228. However, we did note that several loops are disordered in both PRC2:EZH1 and PRC2:EZH2, making us wonder whether any functional differences could be explained by differences contained in these loops (Supplementary Fig. 4a, b).","type":"Results"},{"text":"Supplementary Fig. 4: Regulatory domains of EZH1 are flexible.\na, Cartoon representation of domains that are visible in the cryo-EM density of EZH1. b, Depiction of the key\nunstructured loops in EZH1. Labels indicate the last structured residues flanking the flexible loops in EZH1. c,\nSequence comparison of the flexible loops in EZH1 and EZH2. Underlined sequences represent regions rich in\nbasic (blue) or acidic residues (red), RNA-interaction domains (purple), and automethylation sites (green). Acidic\nor basic regions are based on manual inspection of the EZH1/2 sequences. RNA-interaction domains and\nautomethylation sites are based on reports describing EZH2 features63-66.","type":"Supplementary material"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-09-05T13:37:25.803Z"}},{"start":323,"end":431,"reference_id":"33514705","reference_source":"pmid","reference_html":"Structures of monomeric and dimeric PRC2:EZH1 reveal flexible modules involved in chromatin compaction. <i> Grau D, Zhang Y, Lee CH, Valencia-Sánchez M, Zhang J, Wang M, Holder M, Svetlov V, Tan D, Nudler E, Reinberg D, Walz T, Armache KJ. </i> Nat Commun, 2021","date":"2023-09-05T09:31:28.283Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"GO:0031491","term_name":"nucleosome binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005667","ec_ontology":"ECO","ec_name":"site-directed mutagenesis phenotypic evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IMP","region_id":"DP04135r008","statement":[{"text":"Since this loop contains a patch of basic amino acids, we wondered if it plays a role in nucleosome interactions and/or the methyltransferase activity of PRC2:EZH1 (Fig. 2b). To test this possibility, we generated an EZH1 version in which we mutated the five consecutive arginines in the basic patch (green box in Fig. 2b) to alanines (5RtoA mutation).","type":"Results"},{"text":"PRC2:EZH15RtoA showed severely decreased nucleosome-binding activity and no detectable methyltransferase activity (Fig. 2c).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a nucleosome, a complex comprised of DNA wound around a multisubunit core and associated proteins, which forms the primary packing unit of DNA into higher order structures.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg360Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test this possibility, we generated an EZH1 version in which we mutated the five consecutive arginines in the basic patch (green box in Fig. 2b) to alanines (5RtoA mutation). "}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg361Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test this possibility, we generated an EZH1 version in which we mutated the five consecutive arginines in the basic patch (green box in Fig. 2b) to alanines (5RtoA mutation). "}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg362Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test this possibility, we generated an EZH1 version in which we mutated the five consecutive arginines in the basic patch (green box in Fig. 2b) to alanines (5RtoA mutation). "}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg363Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test this possibility, we generated an EZH1 version in which we mutated the five consecutive arginines in the basic patch (green box in Fig. 2b) to alanines (5RtoA mutation). "}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg364Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test this possibility, we generated an EZH1 version in which we mutated the five consecutive arginines in the basic patch (green box in Fig. 2b) to alanines (5RtoA mutation). "}]}],"sequence_construct":"MEIPNPPTSKCITYWKRKVKSEYMRLRQLKRLQANMGAKALYVANFAKVQEKTQILNEEWKKLRVQPVQSMKPVSGHPFLKKCTIESIFPGFASQHMLMRSLNTVALVPIMYSWSPLQQNFMVEDETVLCNIPYMGDEVKEEDETFIEELINNYDGKVHGEEEMIPGSVLISDAVFLELVDALNQYSDEEEEGHNDTSDGKQDDSKEDLPVTRKRKRHAIEGNKKSSKKQFPNDMIFSAIASMFPENGVPDDMKERYRELTEMSDPNALPPQCTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNVYKRKNKEIKIEPEPCGTDCFLLLEGAKEYAMLHNPRSKCSGAAAAAHHIVSASCSNASASAVAETKEGDSDRDTGNDWASSSSEANSRCQTPTKQKASPAPPQLCVVEAPSEPVEWTGAEESLFRVFHGTYFNNFCSIARLLGTKTCKQVFQFAVKESLILKLPTDELMNPSQKKKRKHRLWAAHCRKIQLKKDNSSTQVYNYQPCDHPDRPCDSTCPCIMTQNFCEKFCQCNPDCQNRFPGCRCKTQCNTKQCPCYLAVRECDPDLCLTCGASEHWDCKVVSCKNCSIQRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYDKYMSSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVVMVNGDHRIGIFAKRAIQAGEELFFDYRYSQADALKYVGIERETDVL","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75530"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09028"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15022"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-09-05T14:12:19.743Z"}},{"start":323,"end":431,"reference_id":"33514705","reference_source":"pmid","reference_html":"Structures of monomeric and dimeric PRC2:EZH1 reveal flexible modules involved in chromatin compaction. <i> Grau D, Zhang Y, Lee CH, Valencia-Sánchez M, Zhang J, Wang M, Holder M, Svetlov V, Tan D, Nudler E, Reinberg D, Walz T, Armache KJ. </i> Nat Commun, 2021","date":"2023-09-05T09:29:20.958Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"GO:0046976","term_name":"histone methyltransferase activity (H3-K27 specific)","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005667","ec_ontology":"ECO","ec_name":"site-directed mutagenesis phenotypic evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"ec_go":"IMP","region_id":"DP04135r009","statement":[{"text":"PRC2:EZH15RtoA showed severely decreased nucleosome-binding activity and no detectable methyltransferase activity (Fig. 2c).","type":"Results"}],"term_comment":"","term_def":"\"Catalysis of the reaction: S-adenosyl-L-methionine + histone H3 L-lysine (position 27) = S-adenosyl-L-homocysteine + histone H3 N6-methyl-L-lysine (position 27). This reaction is the addition of a methyl group onto lysine at position 27 of the histone H3 protein.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg360Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test this possibility, we generated an EZH1 version in which we mutated the five consecutive arginines in the basic patch (green box in Fig. 2b) to alanines (5RtoA mutation). "}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg361Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test this possibility, we generated an EZH1 version in which we mutated the five consecutive arginines in the basic patch (green box in Fig. 2b) to alanines (5RtoA mutation). "}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg362Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test this possibility, we generated an EZH1 version in which we mutated the five consecutive arginines in the basic patch (green box in Fig. 2b) to alanines (5RtoA mutation). "}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg363Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test this possibility, we generated an EZH1 version in which we mutated the five consecutive arginines in the basic patch (green box in Fig. 2b) to alanines (5RtoA mutation). "}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg364Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test this possibility, we generated an EZH1 version in which we mutated the five consecutive arginines in the basic patch (green box in Fig. 2b) to alanines (5RtoA mutation). "}]}],"sequence_construct":"MEIPNPPTSKCITYWKRKVKSEYMRLRQLKRLQANMGAKALYVANFAKVQEKTQILNEEWKKLRVQPVQSMKPVSGHPFLKKCTIESIFPGFASQHMLMRSLNTVALVPIMYSWSPLQQNFMVEDETVLCNIPYMGDEVKEEDETFIEELINNYDGKVHGEEEMIPGSVLISDAVFLELVDALNQYSDEEEEGHNDTSDGKQDDSKEDLPVTRKRKRHAIEGNKKSSKKQFPNDMIFSAIASMFPENGVPDDMKERYRELTEMSDPNALPPQCTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNVYKRKNKEIKIEPEPCGTDCFLLLEGAKEYAMLHNPRSKCSGAAAAAHHIVSASCSNASASAVAETKEGDSDRDTGNDWASSSSEANSRCQTPTKQKASPAPPQLCVVEAPSEPVEWTGAEESLFRVFHGTYFNNFCSIARLLGTKTCKQVFQFAVKESLILKLPTDELMNPSQKKKRKHRLWAAHCRKIQLKKDNSSTQVYNYQPCDHPDRPCDSTCPCIMTQNFCEKFCQCNPDCQNRFPGCRCKTQCNTKQCPCYLAVRECDPDLCLTCGASEHWDCKVVSCKNCSIQRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYDKYMSSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVVMVNGDHRIGIFAKRAIQAGEELFFDYRYSQADALKYVGIERETDVL","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75530"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09028"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15022"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-09-05T14:12:27.467Z"}},{"start":323,"end":431,"reference_id":"33514705","reference_source":"pmid","reference_html":"Structures of monomeric and dimeric PRC2:EZH1 reveal flexible modules involved in chromatin compaction. <i> Grau D, Zhang Y, Lee CH, Valencia-Sánchez M, Zhang J, Wang M, Holder M, Svetlov V, Tan D, Nudler E, Reinberg D, Walz T, Armache KJ. </i> Nat Commun, 2021","date":"2023-09-05T14:42:32.876Z","curator_id":"eleonardi","curator_name":"Emanuela Leonardi","curator_orcid":"0000-0001-8486-8461","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg360Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test this possibility, we generated an EZH1 version in which we mutated the five consecutive arginines in the basic patch (green box in Fig. 2b) to alanines (5RtoA mutation)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg361Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test this possibility, we generated an EZH1 version in which we mutated the five consecutive arginines in the basic patch (green box in Fig. 2b) to alanines (5RtoA mutation)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg362Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test this possibility, we generated an EZH1 version in which we mutated the five consecutive arginines in the basic patch (green box in Fig. 2b) to alanines (5RtoA mutation)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg363Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test this possibility, we generated an EZH1 version in which we mutated the five consecutive arginines in the basic patch (green box in Fig. 2b) to alanines (5RtoA mutation)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg364Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test this possibility, we generated an EZH1 version in which we mutated the five consecutive arginines in the basic patch (green box in Fig. 2b) to alanines (5RtoA mutation)."}]}],"ec_go":"IMP","region_id":"DP04135r010","sequence_construct":"MEIPNPPTSKCITYWKRKVKSEYMRLRQLKRLQANMGAKALYVANFAKVQEKTQILNEEWKKLRVQPVQSMKPVSGHPFLKKCTIESIFPGFASQHMLMRSLNTVALVPIMYSWSPLQQNFMVEDETVLCNIPYMGDEVKEEDETFIEELINNYDGKVHGEEEMIPGSVLISDAVFLELVDALNQYSDEEEEGHNDTSDGKQDDSKEDLPVTRKRKRHAIEGNKKSSKKQFPNDMIFSAIASMFPENGVPDDMKERYRELTEMSDPNALPPQCTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNVYKRKNKEIKIEPEPCGTDCFLLLEGAKEYAMLHNPRSKCSGAAAAAHHIVSASCSNASASAVAETKEGDSDRDTGNDWASSSSEANSRCQTPTKQKASPAPPQLCVVEAPSEPVEWTGAEESLFRVFHGTYFNNFCSIARLLGTKTCKQVFQFAVKESLILKLPTDELMNPSQKKKRKHRLWAAHCRKIQLKKDNSSTQVYNYQPCDHPDRPCDSTCPCIMTQNFCEKFCQCNPDCQNRFPGCRCKTQCNTKQCPCYLAVRECDPDLCLTCGASEHWDCKVVSCKNCSIQRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYDKYMSSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVVMVNGDHRIGIFAKRAIQAGEELFFDYRYSQADALKYVGIERETDVL","statement":[{"text":"We wondered if the MS2L basic patch contributed to the activity of PRC2:EZH1 dimers. Since the 5RtoA mutation severely inhibited the nucleosome-binding and methyltransferase activities of the PRC2:EZH1 core complex (Fig. 2), we decided to test if this mutation also impacts nucleosome-array compaction. When we tested the mutant complex, we observed no promotion of nucleosome-array compaction by the monomeric complex at the highest PRC2:EZH1 concentration tested, and we saw a fourfold reduction in the activity of the dimeric complex, consistent with the basic patch of PRC2 being involved in promoting chromatin compaction (Fig. 3d). ","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75530"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09028"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15022"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-10-09T13:46:48.229Z"}}],"regions_counter":10,"released":"2023_12","sequence":"MEIPNPPTSKCITYWKRKVKSEYMRLRQLKRLQANMGAKALYVANFAKVQEKTQILNEEWKKLRVQPVQSMKPVSGHPFLKKCTIESIFPGFASQHMLMRSLNTVALVPIMYSWSPLQQNFMVEDETVLCNIPYMGDEVKEEDETFIEELINNYDGKVHGEEEMIPGSVLISDAVFLELVDALNQYSDEEEEGHNDTSDGKQDDSKEDLPVTRKRKRHAIEGNKKSSKKQFPNDMIFSAIASMFPENGVPDDMKERYRELTEMSDPNALPPQCTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNVYKRKNKEIKIEPEPCGTDCFLLLEGAKEYAMLHNPRSKCSGRRRRRHHIVSASCSNASASAVAETKEGDSDRDTGNDWASSSSEANSRCQTPTKQKASPAPPQLCVVEAPSEPVEWTGAEESLFRVFHGTYFNNFCSIARLLGTKTCKQVFQFAVKESLILKLPTDELMNPSQKKKRKHRLWAAHCRKIQLKKDNSSTQVYNYQPCDHPDRPCDSTCPCIMTQNFCEKFCQCNPDCQNRFPGCRCKTQCNTKQCPCYLAVRECDPDLCLTCGASEHWDCKVVSCKNCSIQRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYDKYMSSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVVMVNGDHRIGIFAKRAIQAGEELFFDYRYSQADALKYVGIERETDVL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.214190093708166,"dataset":["NDDs-related proteins","Condensates-related proteins"],"disorder_content":0.46318607764390896,"disprot_consensus":{"full":[{"start":1,"end":30,"type":"D"},{"start":125,"end":271,"type":"D"},{"start":323,"end":431,"type":"D"},{"start":478,"end":517,"type":"D"},{"start":728,"end":747,"type":"D"}],"Structural state":[{"start":1,"end":30,"type":"D"},{"start":125,"end":271,"type":"D"},{"start":323,"end":431,"type":"D"},{"start":478,"end":517,"type":"D"},{"start":728,"end":747,"type":"D"}],"Molecular function":[{"start":323,"end":431,"type":"F"}]}},{"disprot_id":"DP04137","acc":"O43561-2","creator":"vnugnes","date":"2023-11-23T10:03:23.298Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"LAT"}}],"length":233,"name":"Isoform 2 of Linker for activation of T-cells family member 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":30,"end":233,"reference_id":"19115140","reference_source":"pmid","reference_html":"Phosphotyrosine-dependent in vitro reconstitution of recombinant LAT-nucleated multiprotein signalling complexes on liposomes. <i> Sangani D, Venien-Bryan C, Harder T. </i> Mol Membr Biol, 2009","date":"2023-11-23T10:04:24.663Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04137r001","statement":[{"text":"The 1H-15N HSQC two dimensional spectrum of this LAT protein segment (Figure 6) is characteristic of a largely disordered polypeptide.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:47:26.347Z"}},{"start":30,"end":233,"reference_id":"33080222","reference_source":"pmid","reference_html":"Coupled membrane lipid miscibility and phosphotyrosine-driven protein condensation phase transitions. <i> Chung JK, Huang WYC, Carbone CB, Nocka LM, Parikh AN, Vale RD, Groves JT. </i> Biophys J, 2021","date":"2023-11-28T14:34:35.707Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0036398","term_name":"TCR signalosome","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"The cytoplasmic domain of LAT was purified with an N-terminal His6 tag and labeled with Alexa Fluor 555 (AF555) at Cys146 via maleimide-thiol chemistry. LAT was phosphorylated by the kinase domain of Hck in solution. Then, phosphorylated LAT (pLAT) was linked to the membrane by the binding of the His6 tag to the Ni-nitrilotriacetic-acid lipids in the membrane."}]},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":146,"end":null,"position":"Specific residue","statements":[{"type":"Results","text":"The cytoplasmic domain of LAT was purified with an N-terminal His6 tag and labeled with Alexa Fluor 555 (AF555) at Cys146 via maleimide-thiol chemistry. LAT was phosphorylated by the kinase domain of Hck in solution. Then, phosphorylated LAT (pLAT) was linked to the membrane by the binding of the His6 tag to the Ni-nitrilotriacetic-acid lipids in the membrane."}]}],"ec_go":"IDA","region_id":"DP04137r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62993"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"52360","statements":[{"type":"Supplementary material","text":"Formation of giant unilamellar vesicles (GUVs) GUVs of various compositions, primarily of\nDOPC, DPPC, and cholesterol (Avanti Polar Lipids, Alabaster, CA) were prepared by\nelectroformation, closely following a published protocol (3)."}],"entry_name":"1,2-dioleoyl-sn-glycero-3-phosphocholine(1+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"40265","statements":[{"type":"Supplementary material","text":"Formation of giant unilamellar vesicles (GUVs) GUVs of various compositions, primarily of\nDOPC, DPPC, and cholesterol (Avanti Polar Lipids, Alabaster, CA) were prepared by\nelectroformation, closely following a published protocol (3)."}],"entry_name":"1,2-di-O-palmitoyl-sn-glycero-3-phosphocholine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16113","statements":[{"type":"Supplementary material","text":"Formation of giant unilamellar vesicles (GUVs) GUVs of various compositions, primarily of\nDOPC, DPPC, and cholesterol (Avanti Polar Lipids, Alabaster, CA) were prepared by\nelectroformation, closely following a published protocol (3)."}],"entry_name":"cholesterol"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q07889"}],"statement":[{"text":"The addition of full-length Grb2 and the proline-rich domains of SOS leads to the networked condensation of LAT:Grb2:SOS on the membrane surface of GUVs, as shown in Fig. 2 (top row). Here, the condensates are visualized as concentrated regions of pLAT-AF555 fluorescence on GUVs by confocal microscopy. This condensate is mediated by tyrosine phosphorylation on LAT and is reversible (Fig. 2, bottom row). ","type":"Results"}],"term_comment":"","term_def":"\"A multi-protein complex containing at least the T-cell receptor complex and the LAT (linker for activation of T cells) scaffold protein. Also contains a variety of signaling proteins including co-receptors, kinases, phosphatases and adaptors such as CD8. Connects events on the plasma membrane to distal signaling cascades to ultimately modulate T cell biology.\" [GOC:krc, PMID:17534068, PMID:20107804, PMID:22426112]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:47:27.817Z"}},{"start":30,"end":233,"reference_id":"33080222","reference_source":"pmid","reference_html":"Coupled membrane lipid miscibility and phosphotyrosine-driven protein condensation phase transitions. <i> Chung JK, Huang WYC, Carbone CB, Nocka LM, Parikh AN, Vale RD, Groves JT. </i> Biophys J, 2021","date":"2023-11-28T14:35:17.143Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"The cytoplasmic domain of LAT was purified with an N-terminal His6 tag and labeled with Alexa Fluor 555 (AF555) at Cys146 via maleimide-thiol chemistry. LAT was phosphorylated by the kinase domain of Hck in solution. Then, phosphorylated LAT (pLAT) was linked to the membrane by the binding of the His6 tag to the Ni-nitrilotriacetic-acid lipids in the membrane."}]},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":146,"end":null,"position":"Specific residue","statements":[{"type":"Results","text":"The cytoplasmic domain of LAT was purified with an N-terminal His6 tag and labeled with Alexa Fluor 555 (AF555) at Cys146 via maleimide-thiol chemistry. LAT was phosphorylated by the kinase domain of Hck in solution. Then, phosphorylated LAT (pLAT) was linked to the membrane by the binding of the His6 tag to the Ni-nitrilotriacetic-acid lipids in the membrane."}]}],"ec_go":"IDA","region_id":"DP04137r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62993"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"52360","statements":[{"type":"Supplementary material","text":"Formation of giant unilamellar vesicles (GUVs) GUVs of various compositions, primarily of\nDOPC, DPPC, and cholesterol (Avanti Polar Lipids, Alabaster, CA) were prepared by\nelectroformation, closely following a published protocol (3)."}],"entry_name":"1,2-dioleoyl-sn-glycero-3-phosphocholine(1+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"40265","statements":[{"type":"Supplementary material","text":"Formation of giant unilamellar vesicles (GUVs) GUVs of various compositions, primarily of\nDOPC, DPPC, and cholesterol (Avanti Polar Lipids, Alabaster, CA) were prepared by\nelectroformation, closely following a published protocol (3)."}],"entry_name":"1,2-di-O-palmitoyl-sn-glycero-3-phosphocholine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16113","statements":[{"type":"Supplementary material","text":"Formation of giant unilamellar vesicles (GUVs) GUVs of various compositions, primarily of\nDOPC, DPPC, and cholesterol (Avanti Polar Lipids, Alabaster, CA) were prepared by\nelectroformation, closely following a published protocol (3)."}],"entry_name":"cholesterol"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q07889"}],"statement":[{"text":"The addition of full-length Grb2 and the proline-rich domains of SOS leads to the networked condensation of LAT:Grb2:SOS on the membrane surface of GUVs, as shown in Fig. 2 (top row). Here, the condensates are visualized as concentrated regions of pLAT-AF555 fluorescence on GUVs by confocal microscopy. This condensate is mediated by tyrosine phosphorylation on LAT and is reversible (Fig. 2, bottom row). ","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:47:34.636Z"}},{"start":30,"end":233,"reference_id":"33080222","reference_source":"pmid","reference_html":"Coupled membrane lipid miscibility and phosphotyrosine-driven protein condensation phase transitions. <i> Chung JK, Huang WYC, Carbone CB, Nocka LM, Parikh AN, Vale RD, Groves JT. </i> Biophys J, 2021","date":"2023-11-28T14:35:50.419Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031580","term_name":"membrane raft distribution","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"In the imaging chamber maintained at 31°C, the pLAT-associated vesicle membranes exhibit a homogeneous distribution of fluorescent markers (TR-DHPE and OG-DHPE), as expected because this temperature is slightly above the Tmisc of 29°C. The addition of Grb2-AF647 and SOS triggers a rapid LAT:Grb2:SOS condensation on the membrane surface, which is readily visualized by the appearance of concentrated regions of 647-nm fluorescence, tracking Grb2. This is accompanied by a clear partitioning of TR-DHPE (yellow) and OG-DHPE (blue), indicating a miscibility phase transition within the lipids has also occurred, although under isothermal conditions here."}]},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":146,"end":null,"position":"Specific residue","statements":[{"type":"Results","text":"The cytoplasmic domain of LAT was purified with an N-terminal His6 tag and labeled with Alexa Fluor 555 (AF555) at Cys146 via maleimide-thiol chemistry. LAT was phosphorylated by the kinase domain of Hck in solution. Then, phosphorylated LAT (pLAT) was linked to the membrane by the binding of the His6 tag to the Ni-nitrilotriacetic-acid lipids in the membrane."}]}],"ec_go":"IDA","region_id":"DP04137r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62993"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"52360","statements":[{"type":"Supplementary material","text":"Formation of giant unilamellar vesicles (GUVs) GUVs of various compositions, primarily of\nDOPC, DPPC, and cholesterol (Avanti Polar Lipids, Alabaster, CA) were prepared by\nelectroformation, closely following a published protocol (3)."}],"entry_name":"1,2-dioleoyl-sn-glycero-3-phosphocholine(1+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"40265","statements":[{"type":"Supplementary material","text":"Formation of giant unilamellar vesicles (GUVs) GUVs of various compositions, primarily of\nDOPC, DPPC, and cholesterol (Avanti Polar Lipids, Alabaster, CA) were prepared by\nelectroformation, closely following a published protocol (3)."}],"entry_name":"1,2-di-O-palmitoyl-sn-glycero-3-phosphocholine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16113","statements":[{"type":"Supplementary material","text":"Formation of giant unilamellar vesicles (GUVs) GUVs of various compositions, primarily of\nDOPC, DPPC, and cholesterol (Avanti Polar Lipids, Alabaster, CA) were prepared by\nelectroformation, closely following a published protocol (3)."}],"entry_name":"cholesterol"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q07889"}],"statement":[{"text":"In the imaging chamber maintained at 31°C, the pLAT-associated vesicle membranes exhibit a homogeneous distribution of fluorescent markers (TR-DHPE and OG-DHPE), as expected because this temperature is slightly above the Tmisc of 29°C. The addition of Grb2-AF647 and SOS triggers a rapid LAT:Grb2:SOS condensation on the membrane surface, which is readily visualized by the appearance of concentrated regions of 647-nm fluorescence, tracking Grb2. This is accompanied by a clear partitioning of TR-DHPE (yellow) and OG-DHPE (blue), indicating a miscibility phase transition within the lipids has also occurred, although under isothermal conditions here.","type":"Results"},{"text":"We observed that the formation of protein condensate can drive the lipid phase transition under isothermal conditions, redistributing lipids in a signal-dependent manner.","type":"Discussion"}],"term_comment":"","term_def":"\"The process that establishes the spatial arrangement of membrane rafts within a cellular membrane.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-12-05T17:47:36.523Z"}}],"regions_counter":4,"released":"2023_12","sequence":"MEEAILVPCVLGLLLLPILAMLMALCVHCHRLPGSYDSTSSDSLYPRGIQFKRPHTVAPWPPAYPPVTSYPPLSQPDLLPIPRSPQPLGGSHRTPSSRRDSDGANSVASYENEEPACEDADEDEDDYHNPGYLVVLPDSTPATSTAAPSAPALSTPGIRDSAFSMESIDDYVNVPESGESAEASLDGSREYVNVSQELHPGAAKTEPAALSSQEAEEVEEEGAPDYENLQELN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["Condensates-related proteins"],"disorder_content":0.8755364806866953,"disprot_consensus":{"full":[{"start":30,"end":233,"type":"D"}],"Structural state":[{"start":30,"end":233,"type":"D"}],"Cellular component":[{"start":30,"end":233,"type":"F"}],"Molecular function":[{"start":30,"end":233,"type":"F"}],"Biological process":[{"start":30,"end":233,"type":"F"}]}},{"disprot_id":"DP04138","acc":"P19597","creator":"fquaglia","date":"2023-12-15T16:08:28.025Z","features":{"pfam":[{"id":"PF00090","name":"Thrombospondin type 1 domain","start":326,"end":374}],"gene3D":[]},"genes":[{"name":{"value":"CSP","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"32451496","url":"http://www.ncbi.nlm.nih.gov/pubmed/32451496","alternativeUrl":"https://europepmc.org/abstract/MED/32451496"}}]}}],"length":397,"name":"Circumsporozoite protein","ncbi_taxon_id":5843,"organism":"Plasmodium falciparum (isolate NF54)","regions":[{"start":19,"end":105,"reference_id":"38059674","reference_source":"pmid","reference_html":"Biophysical characterization of the Plasmodium falciparum circumsporozoite protein's N-terminal domain. <i> Geens R, Stanisich J, Beyens O, D'Hondt S, Thiberge JM, Ryckebosch A, Groot A, Magez S, Vertommen D, Amino R, Winter H, Volkov AN, Tompa P, Sterckx YG. </i> Protein Sci, 2023","date":"2023-12-15T16:26:04.177Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04138r001","statement":[{"text":"AGF and DLS were employed to investigate the hydrodynamic behavior of PfCSP N . Both techniques demonstrate that the apparent molecular mass (MM app) and hydrodynamic radius (Rh,app ) are higher than the theoretical values for globular proteins of the same size (1.8 and 1.2 times, respectively; Figures 4A and 4B). This discrepancy is characteristic of an IDP and suggests that PfCSP N adopts a nonglobular conformation (Csizmók et al., 2006).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-18T15:14:48.624Z"}},{"start":19,"end":105,"reference_id":"38059674","reference_source":"pmid","reference_html":"Biophysical characterization of the Plasmodium falciparum circumsporozoite protein's N-terminal domain. <i> Geens R, Stanisich J, Beyens O, D'Hondt S, Thiberge JM, Ryckebosch A, Groot A, Magez S, Vertommen D, Amino R, Winter H, Volkov AN, Tompa P, Sterckx YG. </i> Protein Sci, 2023","date":"2023-12-15T16:26:15.700Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04138r002","statement":[{"text":"AGF and DLS were employed to investigate the hydrodynamic behavior of PfCSP N . Both techniques demonstrate that the apparent molecular mass (MM app) and hydrodynamic radius (Rh,app ) are higher than the theoretical values for globular proteins of the same size (1.8 and 1.2 times, respectively; Figures 4A and 4B). This discrepancy is characteristic of an IDP and suggests that PfCSP N adopts a nonglobular conformation (Csizmók et al., 2006).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-18T15:14:49.231Z"}},{"start":19,"end":105,"reference_id":"38059674","reference_source":"pmid","reference_html":"Biophysical characterization of the Plasmodium falciparum circumsporozoite protein's N-terminal domain. <i> Geens R, Stanisich J, Beyens O, D'Hondt S, Thiberge JM, Ryckebosch A, Groot A, Magez S, Vertommen D, Amino R, Winter H, Volkov AN, Tompa P, Sterckx YG. </i> Protein Sci, 2023","date":"2023-12-15T16:15:44.187Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04138r003","statement":[{"text":"To further examine the structural features of PfCSP N , a far-UV CD spectrum was collected (Figure 4C). The spectrum is typical for a protein with a significant amount of intrinsic disorder with a dominant negative peak at 205 nm (Tompa, 2002). However, completely disordered proteins have a mean residue ellipticity (MRE) value close to zero around 220 nm. This is clearly not the case for PfCSP N , suggesting that the protein contains some secondary structure elements despite being mainly disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-18T15:14:49.536Z"}},{"start":19,"end":105,"reference_id":"38059674","reference_source":"pmid","reference_html":"Biophysical characterization of the Plasmodium falciparum circumsporozoite protein's N-terminal domain. <i> Geens R, Stanisich J, Beyens O, D'Hondt S, Thiberge JM, Ryckebosch A, Groot A, Magez S, Vertommen D, Amino R, Winter H, Volkov AN, Tompa P, Sterckx YG. </i> Protein Sci, 2023","date":"2023-12-15T16:20:51.786Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04138r004","statement":[{"text":"The IDP nature of PfCSP N was further confirmed by investigating its in-solution structural parameters using SAXS (Figures 4E and 4F). Macromolecular flexibility in solution is readily visualized by the normalized Kratky plot (Figure 4E, inset). While a globular protein displays a bell-shaped curve with a maximum at (1.732, 1.104), the curve of a completely unfolded protein behaving like a random chain increases steeply until it reaches a plateau at ~2 (Durand et al., 2010). The normalized Kratky plot of PfCSP N undoubtedly illustrates that it behaves like a highly flexible protein.To further examine the structural features of PfCSP N , a far-UV CD spectrum was collected (Figure 4C). The spectrum is typical for a protein with a significant amount of intrinsic disorder with a dominant negative peak at 205 nm (Tompa, 2002). However, completely disordered proteins have a mean residue ellipticity (MRE) value close to zero around 220 nm. This is clearly not the case for PfCSP N , suggesting that the protein contains some secondary structure elements despite being mainly disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-18T15:14:50.012Z"}},{"start":19,"end":105,"reference_id":"38059674","reference_source":"pmid","reference_html":"Biophysical characterization of the Plasmodium falciparum circumsporozoite protein's N-terminal domain. <i> Geens R, Stanisich J, Beyens O, D'Hondt S, Thiberge JM, Ryckebosch A, Groot A, Magez S, Vertommen D, Amino R, Winter H, Volkov AN, Tompa P, Sterckx YG. </i> Protein Sci, 2023","date":"2023-12-15T16:22:47.654Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04138r005","statement":[{"text":"The high degree of structural disorder is further illustrated by solution NMR spectroscopy. In particular, the 1 H- 15 N HSQC spectrum of 15 N labeled PfCSP N exhibits poor signal dispersion, with most of the peaks confined to a narrow spectral region (Figure 4D, blue). Such a cluttered 1 H- 15 N HSQC spectrum indicates that PfCSP N backbone amides sample a range of random-coil chemical shift values and is a salient feature of many IDPs (Burke et al., 2015; Conicella et al., 2016; Ryan et al., 2018).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-18T15:14:54.899Z"}}],"regions_counter":5,"released":"2023_12","sequence":"MMRKLAILSVSSFLFVEALFQEYQCYGSSSNTRVLNELNYDNAGTNLYNELEMNYYGKQENWYSLKKNSRSLGENDDGNNEDNEKLRKPKHKKLKQPADGNPDPNANPNVDPNANPNVDPNANPNVDPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNVDPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNANPNKNNQGNGQGHNMPNDPNRNVDENANANSAVKNNNNEEPSDKHIKEYLNKIQNSLSTEWSPCSVTCGNGIQVRIKPGSANKPKDELDYANDIEKKICKMEKCSSVFNVVNSSIGLIMVLSFLFLN","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"alphafold_very_low_content":0.5214105793450882,"dataset":["Neglected tropical diseases proteins"],"disorder_content":0.21914357682619648,"disprot_consensus":{"full":[{"start":19,"end":105,"type":"D"}],"Structural state":[{"start":19,"end":105,"type":"D"}]}},{"disprot_id":"DP04139","acc":"O14497","creator":"fquaglia","date":"2023-12-15T16:37:42.096Z","features":{"pfam":[{"id":"PF01388","name":"ARID/BRIGHT DNA binding domain","start":1020,"end":1104},{"id":"PF12031","name":"SWI/SNF-like complex subunit BAF250/Osa","start":1976,"end":2231}],"gene3D":[]},"genes":[{"name":{"value":"ARID1A"},"synonyms":[{"value":"BAF250"},{"value":"BAF250A"},{"value":"C1orf4"},{"value":"OSA1"},{"value":"SMARCF1"}]}],"length":2285,"name":"AT-rich interactive domain-containing protein 1A","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":1016,"reference_id":"37788668","reference_source":"pmid","reference_html":"A disordered region controls cBAF activity via condensation and partner recruitment. <i> Patil A, Strom AR, Paulo JA, Collings CK, Ruff KM, Shinn MK, Sankar A, Cervantes KS, Wauer T, St Laurent JD, Xu G, Becker LA, Gygi SP, Pappu RV, Brangwynne CP, Kadoch C. </i> Cell, 2023","date":"2024-01-05T16:54:09.597Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007013","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04139r001","statement":[{"text":"Human cBAF complex (PDBDEV_00000056) with putative ARID1A N-terminal region of unassigned cryoelectron microscopy (cryo-EM) density and C-terminal CBR highlighted.","type":"Figure"},{"text":"Region corresponding to IDR1 of ARID1A.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-04T15:50:11.293Z"}},{"start":1124,"end":1611,"reference_id":"37788668","reference_source":"pmid","reference_html":"A disordered region controls cBAF activity via condensation and partner recruitment. <i> Patil A, Strom AR, Paulo JA, Collings CK, Ruff KM, Shinn MK, Sankar A, Cervantes KS, Wauer T, St Laurent JD, Xu G, Becker LA, Gygi SP, Pappu RV, Brangwynne CP, Kadoch C. </i> Cell, 2023","date":"2024-01-05T16:54:20.648Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007013","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04139r002","statement":[{"text":"Human cBAF complex (PDBDEV_00000056) with putative ARID1A N-terminal region of unassigned cryoelectron microscopy (cryo-EM) density and C-terminal CBR highlighted.","type":"Figure"},{"text":"Region corresponding to IDR2 of ARID1A.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-04T15:50:11.650Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MAAQVAPAAASSLGNPPPPPPSELKKAEQQQREEAGGEAAAAAAAERGEMKAAAGQESEGPAVGPPQPLGKELQDGAESNGGGGGGGAGSGGGPGAEPDLKNSNGNAGPRPALNNNLTEPPGGGGGGSSDGVGAPPHSAAAALPPPAYGFGQPYGRSPSAVAAAAAAVFHQQHGGQQSPGLAALQSGGGGGLEPYAGPQQNSHDHGFPNHQYNSYYPNRSAYPPPAPAYALSSPRGGTPGSGAAAAAGSKPPPSSSASASSSSSSFAQQRFGAMGGGGPSAAGGGTPQPTATPTLNQLLTSPSSARGYQGYPGGDYSGGPQDGGAGKGPADMASQCWGAAAAAAAAAAASGGAQQRSHHAPMSPGSSGGGGQPLARTPQPSSPMDQMGKMRPQPYGGTNPYSQQQGPPSGPQQGHGYPGQPYGSQTPQRYPMTMQGRAQSAMGGLSYTQQIPPYGQQGPSGYGQQGQTPYYNQQSPHPQQQQPPYSQQPPSQTPHAQPSYQQQPQSQPPQLQSSQPPYSQQPSQPPHQQSPAPYPSQQSTTQQHPQSQPPYSQPQAQSPYQQQQPQQPAPSTLSQQAAYPQPQSQQSQQTAYSQQRFPPPQELSQDSFGSQASSAPSMTSSKGGQEDMNLSLQSRPSSLPDLSGSIDDLPMGTEGALSPGVSTSGISSSQGEQSNPAQSPFSPHTSPHLPGIRGPSPSPVGSPASVAQSRSGPLSPAAVPGNQMPPRPPSGQSDSIMHPSMNQSSIAQDRGYMQRNPQMPQYSSPQPGSALSPRQPSGGQIHTGMGSYQQNSMGSYGPQGGQYGPQGGYPRQPNYNALPNANYPSAGMAGGINPMGAGGQMHGQPGIPPYGTLPPGRMSHASMGNRPYGPNMANMPPQVGSGMCPPPGGMNRKTQETAVAMHVAANSIQNRPPGYPNMNQGGMMGTGPPYGQGINSMAGMINPQGPPYSMGGTMANNSAGMAASPEMMGLGDVKLTPATKMNNKADGTPKTESKSKKSSSSTTTNEKITKLYELGGEPERKMWVDRYLAFTEEKAMGMTNLPAVGRKPLDLYRLYVSVKEIGGLTQVNKNKKWRELATNLNVGTSSSAASSLKKQYIQCLYAFECKIERGEDPPPDIFAAADSKKSQPKIQPPSPAGSGSMQGPQTPQSTSSSMAEGGDLKPPTPASTPHSQIPPLPGMSRSNSVGIQDAFNDGSDSTFQKRNSMTPNPGYQPSMNTSDMMGRMSYEPNKDPYGSMRKAPGSDPFMSSGQGPNGGMGDPYSRAAGPGLGNVAMGPRQHYPYGGPYDRVRTEPGIGPEGNMSTGAPQPNLMPSNPDSGMYSPSRYPPQQQQQQQQRHDSYGNQFSTQGTPSGSPFPSQQTTMYQQQQQNYKRPMDGTYGPPAKRHEGEMYSVPYSTGQGQPQQQQLPPAQPQPASQQQAAQPSPQQDVYNQYGNAYPATATAATERRPAGGPQNQFPFQFGRDRVSAPPGTNAQQNMPPQMMGGPIQASAEVAQQGTMWQGRNDMTYNYANRQSTGSAPQGPAYHGVNRTDEMLHTDQRANHEGSWPSHGTRQPPYGPSAPVPPMTRPPPSNYQPPPSMQNHIPQVSSPAPLPRPMENRTSPSKSPFLHSGMKMQKAGPPVPASHIAPAPVQPPMIRRDITFPPGSVEATQPVLKQRRRLTMKDIGTPEAWRVMMSLKSGLLAESTWALDTINILLYDDNSIMTFNLSQLPGLLELLVEYFRRCLIEIFGILKEYEVGDPGQRTLLDPGRFSKVSSPAPMEGGEEEEELLGPKLEEEEEEEVVENDEEIAFSGKDKPASENSEEKLISKFDKLPVKIVQKNDPFVVDCSDKLGRVQEFDSGLLHWRIGGGDTTEHIQTHFESKTELLPSRPHAPCPPAPRKHVTTAEGTPGTTDQEGPPPDGPPEKRITATMDDMLSTRSSTLTEDGAKSSEAIKESSKFPFGISPAQSHRNIKILEDEPHSKDETPLCTLLDWQDSLAKRCVCVSNTIRSLSFVPGNDFEMSKHPGLLLILGKLILLHHKHPERKQAPLTYEKEEEQDQGVSCNKVEWWWDCLEMLRENTLVTLANISGQLDLSPYPESICLPVLDGLLHWAVCPSAEAQDPFSTLGPNAVLSPQRLVLETLSKLSIQDNNVDLILATPPFSRLEKLYSTMVRFLSDRKNPVCREMAVVLLANLAQGDSLAARAIAVQKGSIGNLLGFLEDSLAATQFQQSQASLLHMQNPPFEPTSVDMMRRAARALLALAKVDENHSEFTLYESRLLDISVSPLMNSLVSQVICDVLFLIGQS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.737417943107221,"dataset":["Cancer-related proteins","NDDs-related proteins"],"disorder_content":0.6582056892778994,"disprot_consensus":{"full":[{"start":1,"end":1016,"type":"D"},{"start":1124,"end":1611,"type":"D"}],"Structural state":[{"start":1,"end":1016,"type":"D"},{"start":1124,"end":1611,"type":"D"}]}},{"disprot_id":"DP04140","acc":"Q8R4E9","creator":"tlazar","date":"2023-12-18T12:24:53.345Z","features":{"pfam":[{"id":"PF08839","name":"DNA replication factor CDT1 like","start":199,"end":361},{"id":"PF16679","name":"DNA replication factor Cdt1 C-terminal domain","start":434,"end":528}],"gene3D":[]},"genes":[{"name":{"value":"Cdt1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11850834","url":"http://www.ncbi.nlm.nih.gov/pubmed/11850834","alternativeUrl":"https://europepmc.org/abstract/MED/11850834"}}]},"synonyms":[{"value":"Ris2","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:1914427","url":"http://www.informatics.jax.org/marker/MGI:1914427"}}]}]}],"length":557,"name":"DNA replication factor Cdt1","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":420,"end":451,"reference_id":"19722278","reference_source":"pmid","reference_html":"Structure of the Cdt1 C-terminal domain: conservation of the winged helix fold in replication licensing factors. <i> Khayrutdinov BI, Bae WJ, Yun YM, Lee JH, Tsuyama T, Kim JJ, Hwang E, Ryu KS, Cheong HK, Cheong C, Ko JS, Enomoto T, Karplus PA, Güntert P, Tada S, Jeon YH, Cho Y. </i> Protein Sci, 2009","date":"2023-12-18T12:33:41.178Z","curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"2KLO"}],"region_id":"DP04140r001","statement":[{"text":"The mCdt1CL structure can be divided into the two parts; the first 31 residues form an N-terminal arm (residues 420 to 451), which is highly flexible [Fig. 1(A)]. The Cα and Cβ chemical shift values and the sequential and medium range NOEs of the backbone amide protons confirmed that this N-terminal region also contains a well-defined helical structure [residues 431 to 442; Fig. 1(B,C)].","type":"Results"},{"text":"The flexible linker between the N-terminal arm and the core of mCdt1CL allows significant movement of the N-terminal arm relative to the mCdt1 core and the end to end distance between the N-terminal ends of solution NMR structures could move more than 50 Å [Fig. 1(A)].","type":"Results"},{"text":"The red square marked for the residues from helix H0 in the flexible N-terminal part.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-01-03T16:34:07.118Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MAQSRVTDFYACRRPGLTTPRAKSICLTPSPGGLVAPAFTRSSSRKRARPPAEPGSDQPAPLARRRLRLPGLDSCPSSLPEPSSPAEPSPPADPSPPADPGSPVCPSPVKRTKSTTVYVGQQPGKIPSEDSVSELQSCLRRARKLGAQARALRARVQENAVEPSTPDAKVPTEQPCVEKAPAYQRFHALAQPGLPGLVLPYKYQVLVEMFRSMDTIVSMLHNRSETVTFAKVKQGVQEMMRKRFEERNVGQIKTVYPTSYRFRQECNVPTFKDSIKRSDYQLTIEPLLGQEAGGATQLTATCLLQRRQVFRQNLVERVKEQHKVFLASLNPPMAVPDDQLTRWHPRFNVDEVPDIEPAELPQPPVTEKLTTAQEVLARARSLMTPKMEKALSNLALRSAEPGSPGTSTPPLPATPPATPPAASPSALKGVSQALLERIRAKEVQKQLARMTRCPEQELRLQRLERLPELARVLRNVFVSERKPALTMEVVCARMVDSCQTALSPGEMEKHLVLLAELLPDWLSLHRIRTDTYVKLDKAVDLAGLTARLAHHVHAEGL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"alphafold_very_low_content":0.2746858168761221,"disorder_content":0.05745062836624776,"disprot_consensus":{"full":[{"start":420,"end":451,"type":"D"}],"Structural state":[{"start":420,"end":451,"type":"D"}]}},{"disprot_id":"DP04141","acc":"Q96E09","creator":"vnugnes","date":"2024-01-02T14:52:19.480Z","features":{"pfam":[{"id":"PF27638","name":"PABIR N-terminal helical domain","start":86,"end":169}],"gene3D":[]},"genes":[{"name":{"value":"PABIR1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"33108758","url":"http://www.ncbi.nlm.nih.gov/pubmed/33108758","alternativeUrl":"https://europepmc.org/abstract/MED/33108758"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:23490","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:23490"}}]},"synonyms":[{"value":"C9orf42"},{"value":"FAM122A","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"33108758","url":"http://www.ncbi.nlm.nih.gov/pubmed/33108758","alternativeUrl":"https://europepmc.org/abstract/MED/33108758"}}]}]}],"length":287,"name":"PPP2R1A-PPP2R2A-interacting phosphatase regulator 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":124,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-02T15:28:47.052Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"BMRB","id":"51828"}],"region_id":"DP04141r001","statement":[{"text":"The 2D 1H,15N heteronuclear single quantum coherence (HSQC) spectra of unbound ARPP1921,22 and FAM122ANterm confirmed that both are IDPs with multiple regions of amino acids with preferred α-helical propensities (using chemical shift index (CSI) analysis; Extended Data Fig. 3a–f).","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:22:03.446Z"}},{"start":30,"end":115,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T15:35:18.986Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051721","term_name":"protein phosphatase 2A binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P67775","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63151","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P30153","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04141r002","statement":[{"text":"Similar NMR interaction experiments with FAM122ANterm showed that the intensities of around 85 cross-peaks (residues 30–115) were reduced with PP2A:B55 (Fig. 1e and Extended Data Fig. 4e). On the basis of these data, we created FAM122AID (amino acids 29–120), which includes all PP2A:B55 interacting residues (Extended Data Figs. 3d–f and 4f,g).","type":"Article"}],"term_comment":"","term_def":"\"Binding to protein phosphatase 2A.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:22:13.309Z"}},{"start":73,"end":95,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T15:35:50.810Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051721","term_name":"protein phosphatase 2A binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P63151","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04141r003","statement":[{"text":"An overlay of the 2D 1H,15N HSQC spectrum of FAM122AID with and without B55LL (Fig. 1h and Extended Data Fig. 5c) showed that N/HN cross-peaks with reduced intensities correspond to FAM122A residues 73–95, which bind solely to B55. ","type":"Article"}],"term_comment":"","term_def":"\"Binding to protein phosphatase 2A.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:22:15.328Z"}},{"start":81,"end":111,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T16:05:19.264Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051721","term_name":"protein phosphatase 2A binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P67775","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63151","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04141r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:29936"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P30153"}],"statement":[{"text":"FAM122A also binds exclusively to B55 and PP2Ac and does so, again, using helices (pre-populated in free FAM122A; Extended Data Fig. 3d,f). FAM122A binds a short surface on B55 (the B55 binding platform) and across the PP2Ac active site; the interaction buries 2,700 Å2 solvent-accessible surface area.","type":"Article"}],"term_comment":"","term_def":"\"Binding to protein phosphatase 2A.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"cross_refs":[{"db":"PDB","id":"8SO0"},{"db":"EMDB","id":"40644"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:22:17.194Z"}},{"start":81,"end":111,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T13:40:45.247Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04141r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:29936"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P67775"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63153"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63151"}],"statement":[{"text":"FAM122A also binds exclusively to B55 and PP2Ac and does so, again, using helices (pre-populated in free FAM122A; Extended Data Fig. 3d,f).","type":"Article"},{"text":"The interaction of FAM122A with PP2A:B55 is different to that of ARPP19, with FAM122A residues 81–111 binding PP2A:B55 with two helices (Fig. 4a).","type":"Article"}],"cross_refs":[{"db":"PDB","id":"8SO0"},{"db":"EMDB","id":"40644"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:22:05.378Z"}},{"start":81,"end":111,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T13:39:50.531Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04141r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:29936"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P67775"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63153"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63151"}],"statement":[{"text":"FAM122A also binds exclusively to B55 and PP2Ac and does so, again, using helices (pre-populated in free FAM122A; Extended Data Fig. 3d,f).","type":"Article"},{"text":"The interaction of FAM122A with PP2A:B55 is different to that of ARPP19, with FAM122A residues 81–111 binding PP2A:B55 with two helices (Fig. 4a).","type":"Article"}],"states_connection":[{"source":"DP04141r001","target":"DP04141r005"}],"cross_refs":[{"db":"PDB","id":"8SO0"},{"db":"EMDB","id":"40644"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:22:10.587Z"}},{"start":29,"end":80,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T13:42:11.304Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"8SO0"},{"db":"EMDB","id":"40644"}],"region_id":"DP04141r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:29936"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P67775"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63153"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63151"}],"statement":[{"text":"The lack of electron density shows this region is disordered.","type":"Article"},{"text":"Although FAM122A residues 29–66 were not sufficiently ordered to be modelled, our NMR and binding data suggest that they contribute to binding via a dynamic (fuzzy) charge–charge interaction24,31,32 (Extended Data Table 2 and Extended Data Fig. 2b).","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:22:07.442Z"}},{"start":84,"end":89,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T15:36:45.318Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051721","term_name":"protein phosphatase 2A binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P67775","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63151","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P30153","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04141r008","statement":[{"text":"Mutating the basic–hydrophobic residue pairs—that is, 84RLHQIKQEE92 to 84AAHQIKQEE92 (84AA85) and 84RLHQAAQEE92 (88AA89)—reduced FAM122A binding by 1.6- and 2.0-fold, respectively (Fig. 4g and Extended Data Table 2). Pull-down assays using PP2A:B55 lysates incubated with 84AA85 and 88AA89 FAM122A showed similar reductions in binding compared with the wild-type protein (Fig. 4h). Consistent with their weaker affinities, the IC50 values of the 84AA85 and 88AA89 variants increased by 38- and 48-fold, respectively (Fig. 4g and Extended Data Table 1).","type":"Article"}],"term_comment":"","term_def":"\"Binding to protein phosphatase 2A.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg84Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu85Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile88Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys89Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser120Cys","start":null,"end":null,"position":null},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":120,"end":120,"position":"Specific residue","statements":[{"type":"Methods","text":"Following the instructions of the manufacturer, 100 µM of FAM122AID(S120C) (or variants) or ARPP19(S10C) was labelled with Alexa Fluor 488 C5 Maleimide (ThermoFisher) using 1:10 protein to fluorophore ratio."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:22:19.153Z"}},{"start":90,"end":95,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T15:37:09.646Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051721","term_name":"protein phosphatase 2A binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu91Lys","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu92Lys","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser120Cys","start":null,"end":null,"position":null},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":120,"end":null,"position":"Specific residue","statements":[{"type":"Methods","text":"Following the instructions of the manufacturer, 100 µM of FAM122AID(S120C) (or variants) or ARPP19(S10C) was labelled with Alexa Fluor 488 C5 Maleimide (ThermoFisher) using 1:10 protein to fluorophore ratio."}]}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P67775","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63151","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P30153","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04141r009","statement":[{"text":"Because the FAM122A E92K mutation was identified in cancer tissues (cBioPortal), we also generated E91K and E92K variants and showed they also bound PP2A:B55 less strongly and were less potent inhibitors of PP2A:B55 (Extended Data Tables 1 and 2 and Extended Data Fig. 2a,b).","type":"Article"}],"term_comment":"","term_def":"\"Binding to protein phosphatase 2A.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:22:20.733Z"}},{"start":97,"end":111,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T14:49:35.046Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0004864","term_name":"protein phosphatase inhibitor activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"8SO0"},{"db":"EMDB","id":"40644"}],"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P67775","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04141r010","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:29936"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P67775"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63153"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63151"}],"statement":[{"text":"FAM122A residues C-terminal to the B55 helix form a sharp turn with helix α2 (97INRETVHEREVQTAM111, the inhibition helix; Extended Data Fig. 9i) binding and blocking the PP2Ac active site. ","type":"Article"}],"term_comment":"","term_def":"\"Binds to and stops, prevents or reduces the activity of a protein phosphatase, an enzyme that hydrolyzes phosphate groups from phosphorylated proteins.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:22:22.723Z"}},{"start":104,"end":108,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T14:54:24.268Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0004864","term_name":"protein phosphatase inhibitor activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg105Leu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val107Gly","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P67775","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04141r011","statement":[{"text":"cBioPortal34 highlighted that FAM122A R105L, V107G variants are present in different cancers (FAM122A is a tumour suppressor, as patients with cancer who express low levels of FAM122A have significantly worse overall survival than those with high levels of expression8). FAM122A R105L and V107G variants showed 11- and 6-fold less inhibition than the wild-type protein, respectively (Fig. 4l and Extended Data Table 1), demonstrating that the probable mode of action of these cancer variants is due to a weaker inhibition of PP2A:B55, thereby disrupting PP2A:B55 cellular functions.","type":"Article"}],"term_comment":"","term_def":"\"Binds to and stops, prevents or reduces the activity of a protein phosphatase, an enzyme that hydrolyzes phosphate groups from phosphorylated proteins.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:22:24.982Z"}},{"start":1,"end":124,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T15:37:37.073Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051721","term_name":"protein phosphatase 2A binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P67775","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63151","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P30153","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04141r012","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P56211"}],"statement":[{"text":"We also performed a pull-down competition assay by affinity purification of PP2A:B55 (using GFP–B55) in the presence of FAM122A alone or FAM122A with a fivefold excess of tpARPP19 (Extended Data Fig. 10d)","type":"Article"}],"term_comment":"","term_def":"\"Binding to protein phosphatase 2A.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:22:26.938Z"}},{"start":97,"end":111,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T16:05:50.908Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051721","term_name":"protein phosphatase 2A binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"8SO0"},{"db":"EMDB","id":"40644"}],"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P67775","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04141r013","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63151"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63153"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:29936"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:32051"}],"statement":[{"text":"FAM122A residues C-terminal to the B55 helix form a sharp turn with helix α2 (97INRETVHEREVQTAM111, the inhibition helix; Extended Data Fig. 9i) binding and blocking the PP2Ac active site.","type":"Article"}],"term_comment":"","term_def":"\"Binding to protein phosphatase 2A.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:22:29.318Z"}},{"start":1,"end":124,"reference_id":"38123684","reference_source":"pmid","reference_html":"Cryo-EM structures of PP2A:B55-FAM122A and PP2A:B55-ARPP19. <i> Padi SKR, Vos MR, Godek RJ, Fuller JR, Kruse T, Hein JB, Nilsson J, Kelker MS, Page R, Peti W. </i> Nature, 2023","date":"2024-01-03T16:16:55.341Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0004864","term_name":"protein phosphatase inhibitor activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P67775","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P63151","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P30153","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04141r014","statement":[{"text":"We quantified PP2A:B55 inhibition by ARPP19, thiophosphorylated ARPP19 (full-length (amino acids 1–112) and phosphorylated with ATPγS using MASTL kinase) and FAM122A (N-terminal domain (amino acids 1–124) (FAM122ANterm)) (Fig. 1b). Whereas PP2A:B55 was only moderately inhibited by ARPP19, it was strongly inhibited by both thiophosphorylated ARPP19 and FAM122ANterm (Extended Data Table 1 and Extended Data Fig. 2a), with thiophosphorylated ARPP19 inhibiting PP2A:B55 around 250-fold more potently than FAM122A.","type":"Article"}],"term_comment":"","term_def":"\"Binds to and stops, prevents or reduces the activity of a protein phosphatase, an enzyme that hydrolyzes phosphate groups from phosphorylated proteins.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-04T09:22:31.492Z"}}],"regions_counter":15,"released":"2024_06","sequence":"MAQEKMELDLELPPGTGGSPAEGGGSGGGGGLRRSNSAPLIHGLSDTSPVFQAEAPSARRNSTTFPSRHGLLLPASPVRMHSSRLHQIKQEEGMDLINRETVHEREVQTAMQISHSWEESFSLSDNDVEKSASPKRIDFIPVSPAPSPTRGIGKQCFSPSLQSFVSSNGLPPSPIPSPTTRFTTRRSQSPINCIRPSVLGPLKRKCEMETEYQPKRFFQGITNMLSSDVAQLSDPGVCVSSDTLDGNSSSAGSSCNSPAKVSTTTDSPVSPAQAASPFIPLDELSSK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.26480836236933797,"disorder_content":0.43205574912891986,"disprot_consensus":{"full":[{"start":1,"end":80,"type":"D"},{"start":81,"end":111,"type":"T"},{"start":112,"end":124,"type":"D"}],"Structural state":[{"start":1,"end":124,"type":"D"}],"Molecular function":[{"start":1,"end":124,"type":"F"}],"Structural transition":[{"start":81,"end":111,"type":"T"}]}},{"disprot_id":"DP04142","acc":"Q09312","creator":"fquaglia","date":"2024-01-04T09:33:27.392Z","features":{"pfam":[{"id":"PF00806","name":"Pumilio-family RNA binding repeat","start":197,"end":228},{"id":"PF00806","name":"Pumilio-family RNA binding repeat","start":234,"end":249},{"id":"PF00806","name":"Pumilio-family RNA binding repeat","start":278,"end":296},{"id":"PF00806","name":"Pumilio-family RNA binding repeat","start":316,"end":336},{"id":"PF00806","name":"Pumilio-family RNA binding repeat","start":353,"end":375},{"id":"PF00806","name":"Pumilio-family RNA binding repeat","start":404,"end":426},{"id":"PF00806","name":"Pumilio-family RNA binding repeat","start":443,"end":475},{"id":"PF00806","name":"Pumilio-family RNA binding repeat","start":494,"end":511}],"gene3D":[]},"genes":[{"name":{"value":"fbf-2","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"F21H12.5","url":"https://www.wormbase.org/db/seq/sequence?name=F21H12.5;class=Transcript"}}]},"orfNames":[{"value":"F21H12.5","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"F21H12.5","url":"https://www.wormbase.org/db/seq/sequence?name=F21H12.5;class=Transcript"}}]}]}],"length":632,"name":"Fem-3 mRNA-binding factor 2","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":570,"end":632,"reference_id":"37953271","reference_source":"pmid","reference_html":"Intra- and inter-molecular regulation by intrinsically-disordered regions governs PUF protein RNA binding. <i> Qiu C, Zhang Z, Wine RN, Campbell ZT, Zhang J, Hall TMT. </i> Nat Commun, 2023","date":"2024-01-04T10:44:49.544Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04142r001","statement":[{"text":"Here, we report that an intrinsically disordered region (IDR) at the C-terminus of FBF-2 autoinhibits its RNA-binding affinity by increasing the off rate for RNA binding.","type":"Abstract"},{"text":"We report a 2.1-Å crystal structure of FBF-2 in complex with RNA that identifies a PIM within the intrinsically disordered FBF-2 C-terminal tail (CT) bound to the same site on the RBD as LST-1.","type":"Introduction"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-24T14:49:03.044Z"}},{"start":605,"end":615,"reference_id":"37953271","reference_source":"pmid","reference_html":"Intra- and inter-molecular regulation by intrinsically-disordered regions governs PUF protein RNA binding. <i> Qiu C, Zhang Z, Wine RN, Campbell ZT, Zhang J, Hall TMT. </i> Nat Commun, 2023","date":"2024-01-04T10:50:09.598Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"8SJ7"}],"region_id":"DP04142r002","statement":[{"text":"To explore possible roles of the FBF-2 CT, we expressed and purified an FBF-2 fragment containing both RBD and CT (FBF-2164–632). This FBF-2 RBD + CT had increased thermal stability compared to the RBD alone (Supplementary Table 1). We determined a crystal structure of FBF-2 RBD + CT in complex with a cFBE RNA (5′-CUGUGAAUG-3′) at 2.1 Å resolution (Supplementary Table 2, Fig. 1c). The electron density map revealed new density, not present in the previous RBD structures. This additional density appeared near a loop in the RBD that connects repeats 7 and 8 (Fig. 1d). This R7-R8 loop (residues 476-489) also binds to both LST-1 A and LST-1 B peptides in crystal structures of FBF-2 RBD in complex with LST-1 (Fig. 1c)17,18. The sequence of FBF-2 CT residues 607-613 matched this new electron density, but other C-terminal residues (aa 570-606 and 614-632) were disordered.","type":"Results"},{"text":"This evidence include the seven visible FBF-2 CT residues (SLMLEPR 607–613).","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Results","text":"We determined a crystal structure of FBF-2 RBD + CT in complex with a cFBE RNA (5′-CUGUGAAUG-3′) at 2.1 Å resolution (Supplementary Table 2, Fig. 1c)."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-24T14:49:03.619Z"}},{"start":605,"end":615,"reference_id":"37953271","reference_source":"pmid","reference_html":"Intra- and inter-molecular regulation by intrinsically-disordered regions governs PUF protein RNA binding. <i> Qiu C, Zhang Z, Wine RN, Campbell ZT, Zhang J, Hall TMT. </i> Nat Commun, 2023","date":"2024-01-04T10:50:23.294Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"8SJ7"}],"region_id":"DP04142r003","statement":[{"text":"To explore possible roles of the FBF-2 CT, we expressed and purified an FBF-2 fragment containing both RBD and CT (FBF-2164–632). This FBF-2 RBD + CT had increased thermal stability compared to the RBD alone (Supplementary Table 1). We determined a crystal structure of FBF-2 RBD + CT in complex with a cFBE RNA (5′-CUGUGAAUG-3′) at 2.1 Å resolution (Supplementary Table 2, Fig. 1c). The electron density map revealed new density, not present in the previous RBD structures. This additional density appeared near a loop in the RBD that connects repeats 7 and 8 (Fig. 1d). This R7-R8 loop (residues 476-489) also binds to both LST-1 A and LST-1 B peptides in crystal structures of FBF-2 RBD in complex with LST-1 (Fig. 1c)17,18. The sequence of FBF-2 CT residues 607-613 matched this new electron density, but other C-terminal residues (aa 570-606 and 614-632) were disordered.","type":"Results"},{"text":"This evidence include the seven visible FBF-2 CT residues (SLMLEPR 607–613).","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Results","text":"We determined a crystal structure of FBF-2 RBD + CT in complex with a cFBE RNA (5′-CUGUGAAUG-3′) at 2.1 Å resolution (Supplementary Table 2, Fig. 1c)."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-24T14:48:59.087Z"}},{"start":605,"end":615,"reference_id":"37953271","reference_source":"pmid","reference_html":"Intra- and inter-molecular regulation by intrinsically-disordered regions governs PUF protein RNA binding. <i> Qiu C, Zhang Z, Wine RN, Campbell ZT, Zhang J, Hall TMT. </i> Nat Commun, 2023","date":"2024-01-04T11:00:33.501Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"8SJ7"}],"ec_go":"EXP","region_id":"DP04142r004","statement":[{"text":"To explore possible roles of the FBF-2 CT, we expressed and purified an FBF-2 fragment containing both RBD and CT (FBF-2164–632). This FBF-2 RBD + CT had increased thermal stability compared to the RBD alone (Supplementary Table 1). We determined a crystal structure of FBF-2 RBD + CT in complex with a cFBE RNA (5′-CUGUGAAUG-3′) at 2.1 Å resolution (Supplementary Table 2, Fig. 1c). The electron density map revealed new density, not present in the previous RBD structures. This additional density appeared near a loop in the RBD that connects repeats 7 and 8 (Fig. 1d). This R7-R8 loop (residues 476-489) also binds to both LST-1 A and LST-1 B peptides in crystal structures of FBF-2 RBD in complex with LST-1 (Fig. 1c)17,18. The sequence of FBF-2 CT residues 607-613 matched this new electron density, but other C-terminal residues (aa 570-606 and 614-632) were disordered.","type":"Results"},{"text":"This evidence include the seven visible FBF-2 CT residues (SLMLEPR 607–613).","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-24T14:48:27.683Z"}},{"start":607,"end":613,"reference_id":"37953271","reference_source":"pmid","reference_html":"Intra- and inter-molecular regulation by intrinsically-disordered regions governs PUF protein RNA binding. <i> Qiu C, Zhang Z, Wine RN, Campbell ZT, Zhang J, Hall TMT. </i> Nat Commun, 2023","date":"2024-01-04T11:38:35.379Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q09312","operator":null,"partner_start":164,"partner_end":575}],"region_id":"DP04142r005","statement":[{"text":"FBF-2 CT binds FBF-2 RBD on the same surface as LST-1","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-24T14:48:29.253Z"}},{"start":570,"end":632,"reference_id":"37953271","reference_source":"pmid","reference_html":"Intra- and inter-molecular regulation by intrinsically-disordered regions governs PUF protein RNA binding. <i> Qiu C, Zhang Z, Wine RN, Campbell ZT, Zhang J, Hall TMT. </i> Nat Commun, 2023","date":"2024-01-04T13:28:01.307Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q09312","operator":null,"partner_start":164,"partner_end":575}],"region_id":"DP04142r006","statement":[{"text":"FBF-2 CT and partner proteins compete for binding to the RBD","type":"Results"},{"text":"We found that the FBF-2 CT greatly reduced FBF-2 affinity for LST-1 A and LST-1 B. Binding of LST-1 A to FBF-2 RBD + CT was too weak to be detected by ITC (Fig. 2c) and thus considerably weaker than the affinity of LST-1 A to the RBD alone (Kd = 2.1 µM)18. The binding of LST-1 B to RBD + CT was ~50-fold weaker than to the RBD alone (Kd = 2.7 µM for RBD + CT vs 0.05 µM for RBD, Fig. 2b, d)18. The lower protein interaction affinities for LST-1 A and LST-1 B caused by the FBF-2 CT suggested that the CT and LST-1 compete for binding to the RBD.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-24T14:48:47.389Z"}},{"start":570,"end":632,"reference_id":"37953271","reference_source":"pmid","reference_html":"Intra- and inter-molecular regulation by intrinsically-disordered regions governs PUF protein RNA binding. <i> Qiu C, Zhang Z, Wine RN, Campbell ZT, Zhang J, Hall TMT. </i> Nat Commun, 2023","date":"2024-01-04T13:29:49.333Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu610Ala","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q09312","operator":null,"partner_start":164,"partner_end":575}],"region_id":"DP04142r007","statement":[{"text":"FBF-2 CT and partner proteins compete for binding to the RBD","type":"Results"},{"text":"To examine this idea, we next asked if the reduced binding affinity for LST-1 relies on the CT interaction with RBD. L610 in the FBF-2 CT is equivalent to the key leucines in LST-1 PIMs. Mutation of the key leucines in LST-1 disrupt interaction with FBF-217, and the L610A mutation was designed to test the importance of the interaction between the RBD and CT. We confirmed that the L610A mutation disrupts interaction with the FBF-2 RBD by ITC (Fig. 2e, Supplementary Table 3). The L610A substitution decreased the thermal stability of FBF-2 RBD + CT with a melting temperature of the mutated protein near that of the RBD alone (Supplementary Table 1), suggesting that interaction of the CT with the RBD is stabilizing. We found that FBF-2 RBD + CT L610A bound to LST-1 A and B with affinities similar to the FBF-2 RBD alone (Kd = 2.4 µM for LST-1 A and Kd = 0.06 µM for LST-1 B, Fig. 2b, f, g). Therefore, the interaction between the FBF-2 CT and RBD via L610 is critical for the reduced affinity of RBD + CT for LST-1 A and B, apparently by competing with LST-1 interaction.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-24T14:48:47.697Z"}},{"start":570,"end":632,"reference_id":"37953271","reference_source":"pmid","reference_html":"Intra- and inter-molecular regulation by intrinsically-disordered regions governs PUF protein RNA binding. <i> Qiu C, Zhang Z, Wine RN, Campbell ZT, Zhang J, Hall TMT. </i> Nat Commun, 2023","date":"2024-01-04T13:50:34.592Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000059","term_name":"self-inhibition","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu610Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Like L610A, the Y479A substitution decreased the thermal stability of FBF-2 RBD + CT (Supplementary Table 1)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu592Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test the importance of the cluster of charged residues and predicted repulsion, we substituted the relevant acidic residues in the CT (Fig. 4b) with alanine, and we refer to this mutated protein as RBD + CT Loop6A to refer to the six alanine mutations in the loop."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp594Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test the importance of the cluster of charged residues and predicted repulsion, we substituted the relevant acidic residues in the CT (Fig. 4b) with alanine, and we refer to this mutated protein as RBD + CT Loop6A to refer to the six alanine mutations in the loop."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu597Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test the importance of the cluster of charged residues and predicted repulsion, we substituted the relevant acidic residues in the CT (Fig. 4b) with alanine, and we refer to this mutated protein as RBD + CT Loop6A to refer to the six alanine mutations in the loop."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu599Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test the importance of the cluster of charged residues and predicted repulsion, we substituted the relevant acidic residues in the CT (Fig. 4b) with alanine, and we refer to this mutated protein as RBD + CT Loop6A to refer to the six alanine mutations in the loop."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu604Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test the importance of the cluster of charged residues and predicted repulsion, we substituted the relevant acidic residues in the CT (Fig. 4b) with alanine, and we refer to this mutated protein as RBD + CT Loop6A to refer to the six alanine mutations in the loop."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu605Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test the importance of the cluster of charged residues and predicted repulsion, we substituted the relevant acidic residues in the CT (Fig. 4b) with alanine, and we refer to this mutated protein as RBD + CT Loop6A to refer to the six alanine mutations in the loop."}]}],"region_id":"DP04142r008","statement":[{"text":"FBF-2 CT autoinhibits RNA-binding affinity","type":"Results"},{"text":"The FBF-2 CT autoinhibits RNA-binding affinity.","type":"Figure"},{"text":"Indeed, FBF-2 RBD + CT had a nearly 5-fold weaker affinity for gld-1 FBEa RNA than FBF-2 RBD alone (Kd = 334 nM for FBF-2 RBD + CT and 70 nM for RBD alone). This substantial decrease is greater than the effect of LST-1 B on RBD (Kd = 176 nM, Supplementary Fig. 1a), and the CT effect is intramolecular.","type":"Results"},{"text":"To confirm that the reduced RNA-binding affinity was due to the CT interacting with the RBD, we also measured RNA-binding affinity of FBF-2 RBD + CT proteins mutated in the R7-R8 loop (Y479A) or in the C-terminal tail (L610A). Y479 is a critical part of the hydrophobic pocket that binds to key leucine residues in partner proteins (Fig. 1f), and its mutation to an alanine (Y479A) disrupts interaction between FBF-2 and LST-117. Like L610A, the Y479A substitution decreased the thermal stability of FBF-2 RBD + CT (Supplementary Table 1).","type":"Results"},{"text":"We conclude that tethering of the FBF-2 CT to the RBD is autoinhibitory for RNA binding.","type":"Results"},{"text":"Electrostatic repulsion by acidic residues in the FBF-2 CT reduces RNA-binding affinity","type":"Results"},{"text":"The reduced negative charge in the FBF-2 CT loop increased binding affinity to RNA (Kd = 334 nM for RBD + CT vs 101 nM for RBD + CT Loop6A, Fig. 4d) and thus diminished CT autoinhibition. Therefore, both tethering of the CT and the cluster of charged residues contribute to CT autoinhibition.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-24T14:49:01.561Z"}},{"start":570,"end":632,"reference_id":"37953271","reference_source":"pmid","reference_html":"Intra- and inter-molecular regulation by intrinsically-disordered regions governs PUF protein RNA binding. <i> Qiu C, Zhang Z, Wine RN, Campbell ZT, Zhang J, Hall TMT. </i> Nat Commun, 2023","date":"2024-01-04T13:45:58.208Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000059","term_name":"self-inhibition","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu610Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"We therefore measured the binding kinetics of FBF-2 RBD + CT mutants, Y479A, L610A, and Loop6A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu592Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"We therefore measured the binding kinetics of FBF-2 RBD + CT mutants, Y479A, L610A, and Loop6A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp594Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"We therefore measured the binding kinetics of FBF-2 RBD + CT mutants, Y479A, L610A, and Loop6A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu597Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"We therefore measured the binding kinetics of FBF-2 RBD + CT mutants, Y479A, L610A, and Loop6A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu599Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"We therefore measured the binding kinetics of FBF-2 RBD + CT mutants, Y479A, L610A, and Loop6A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu604Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"We therefore measured the binding kinetics of FBF-2 RBD + CT mutants, Y479A, L610A, and Loop6A."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu605Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"We therefore measured the binding kinetics of FBF-2 RBD + CT mutants, Y479A, L610A, and Loop6A."}]}],"region_id":"DP04142r009","statement":[{"text":"FBF-2 CT accelerates dissociation from the RNA","type":"Results"},{"text":"To further examine the effect of the CT on RNA-binding activity of FBF-2, we performed surface plasmon resonance (SPR) assays to measure the kinetics of FBF-2 binding to gld-1 FBEa RNA. We first compared the binding kinetics of FBF-2 RBD and FBF-2 RBD + CT. We found that the on rate for FBF-2 RBD binding was slightly faster than for RBD + CT: 13.6 × 104 M−1 s−1 vs 7.1 × 104 M−1 s−1. In contrast, the off rate for RBD + CT was ~5-fold faster than for RBD: 4.42 × 10−3 s−1 vs 0.86 × 10−3 s−1 (Fig. 5), indicating that the CT accelerates dissociation from the gld-1 FBEa RNA. We therefore measured the binding kinetics of FBF-2 RBD + CT mutants, Y479A, L610A, and Loop6A. Consistent with the differences in off rate for FBF-2 RBD vs RBD + CT and our EMSA results above, the off rates for the RBD + CT mutants were all slower than for wild type RBD + CT and similar to the off rate of FBF-2 RBD alone (Fig. 5c, Supplementary Fig. 3)","type":"Results"},{"text":"The SPR data further support the conclusion that the FBF-2 CT lowers RNA-binding affinity and does so by destabilizing protein-RNA interaction and accelerating dissociation.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-24T14:48:59.551Z"}}],"regions_counter":9,"released":"2024_06","sequence":"MDQSKMRRTNQFRKTSQKPPSTGIDSYPTPAQSPMAQHETPMWDFNSLNPYFSMLNMNDGINYARHQQNHIVTSRPPTPLTDLMSLRSFQSFPNVFMPVSRSRTSSFIQSDTDSSRLESDDFSQNVRCFSADIDRSKSYGSSKHYHLKYSRPALSRNSRSFTRSNNVLPTWSLDSNGEMRSRLSLSEVLDSGDLMKFAVDKTGCQFLEKAVKGSLTSYQKFQLFEQVIGRKDDFLKLSTNIFGNYLVQSVIGISLATNDDGYTKRQEKLKNFISSQMTDMCLDKFACRVIQSSLQNMDLSLACKLVQALPRDARLIAICVDQNANHVIQKVVAVIPLKNWEFIVDFVATPEHLRQICSDKYGCRVVQTIIEKLTADSMNVDLTSAAQNLRERALQRLMTSVTNRCQELATNEYANYIIQHIVSNDDLAVYRECIIEKCLMRNLLSLSQEKFASHVVEKAFLHAPLELLAEMMDEIFDGYIPHPDTGKDALDIMMFHQFGNYVVQCMLTICCDAVSGRRQTKEGGYDHAISFQDWLKKLHSRVTKERHRLSRFSSGKKMIETLANLRSTHPIYELQSSGHDSFKTDYFSTASEHDGPELEKNGIEEGSLMLEPRSNKSSVSVKFSSSGSHGDD","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"alphafold_very_low_content":0.34177215189873417,"dataset":["RNA-binding proteins"],"disorder_content":0.09968354430379747,"disprot_consensus":{"full":[{"start":570,"end":604,"type":"D"},{"start":605,"end":615,"type":"T"},{"start":616,"end":632,"type":"D"}],"Structural state":[{"start":570,"end":632,"type":"D"}],"Structural transition":[{"start":605,"end":615,"type":"T"}],"Molecular function":[{"start":570,"end":632,"type":"F"}],"Disorder function":[{"start":570,"end":632,"type":"F"}]}},{"disprot_id":"DP04144","acc":"P21707","creator":"fquaglia","date":"2024-01-05T09:19:15.433Z","features":{"pfam":[{"id":"PF00168","name":"C2 domain","start":157,"end":262},{"id":"PF00168","name":"C2 domain","start":287,"end":392}],"gene3D":[]},"genes":[{"name":{"value":"Syt1"}}],"length":421,"name":"Synaptotagmin-1","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions":[{"start":80,"end":142,"reference_id":"38177243","reference_source":"pmid","reference_html":"The juxtamembrane linker of synaptotagmin 1 regulates Ca<sup>2+</sup> binding via liquid-liquid phase separation. <i> Mehta N, Mondal S, Watson ET, Cui Q, Chapman ER. </i> Nat Commun, 2024","date":"2024-01-12T17:40:59.808Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007013","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04144r001","statement":[{"text":"Analysis of the linker, using the VL-XT algorithm and PONDR software47, revealed that residues 82-133 form an intrinsically disordered region (IDR; Fig. 2a). These structural predictions were further confirmed using AlphaFold48,49 (Supplementary Fig. 2).","type":"Results"},{"text":"Intrinsic disorder for the Syt 1 linker was experimentally confirmed in human (PMID: 27191789).","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-04T15:54:21.390Z"}},{"start":80,"end":142,"reference_id":"38177243","reference_source":"pmid","reference_html":"The juxtamembrane linker of synaptotagmin 1 regulates Ca<sup>2+</sup> binding via liquid-liquid phase separation. <i> Mehta N, Mondal S, Watson ET, Cui Q, Chapman ER. </i> Nat Commun, 2024","date":"2024-01-12T17:44:18.237Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:1901877","term_name":"negative regulation of calcium ion binding","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"29108","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04144r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","statements":[{"type":"Results","text":"In the first series of experiments, we addressed the ability of the complete cytoplasmic domain to bind Ca2+."}],"entry_name":"calcium(2+)"}],"statement":[{"text":"Juxtamembrane linker of syt1 inhibits Ca2+ binding to the C2-domains","type":"Results"},{"text":"Intriguingly, inclusion of the complete linker resulted in a significant reduction in the intrinsic affinity for Ca2+ of all five sites compared to the construct lacking residues 80–95. In the case of the highest affinity site, the KD increased from 23.5 ± 2.1 to 80.0 ± 3.9 µM for Ca2+ upon removal of residues 80–95 (Fig. 1c, d, Table 1). Removal of the entire linker, resulting in the 143–421 construct, yielded relatively flat ITC traces due to the cancellation of the endo- and exothermic signals from each C2-domain, respectively, as documented previously46, precluding a determination of Ca2+ affinity (Fig. 1e).","type":"Results"},{"text":"These findings reveal that the juxtamembrane linker can negatively affect the Ca2+ binding activity of syt1 via a process that is disrupted by the lysine mutations.","type":"Results"}],"term_comment":"","term_def":"\"Any process that stops, prevents or reduces the frequency, rate or extent of calcium ion binding.\" [GOC:BHF, GOC:rl, GOC:TermGenie, PMID:16432188]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-01-18T15:03:15.579Z"}},{"start":80,"end":142,"reference_id":"38177243","reference_source":"pmid","reference_html":"The juxtamembrane linker of synaptotagmin 1 regulates Ca<sup>2+</sup> binding via liquid-liquid phase separation. <i> Mehta N, Mondal S, Watson ET, Cui Q, Chapman ER. </i> Nat Commun, 2024","date":"2024-03-08T09:43:15.151Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","region_id":"DP04144r003","statement":[{"text":"The juxtamembrane linker of syt1 mediates LLPS in vitro","type":"Results"},{"text":"These findings reveal that the lysine residues in the juxtamembrane linker are crucial for the cytoplasmic domain of syt1 to undergo LLPS. To confirm these results, we labeled both the complete and truncated cytoplasmic domain of syt1 (residues 80–421 and 143–421, respectively) with an organic dye (fluorescein) at native Cys residues 82 and 277. As expected, we observed droplet formation with the complete cytoplasmic domain of syt1 but not for the truncated protein lacking the linker (Supplementary Fig. 5). To assess whether the juxtamembrane linker alone is capable of undergoing LLPS, we subjected the constructs in Fig. 3b to the same conditions that were used in Fig. 3c. Interestingly, we found that the GFP-tagged juxtamembrane linker (80–142) formed droplets, and this activity was, again, abolished in the JuxtaK mutant (Fig. 3d). Hence, the juxtamembrane linker alone is sufficient to undergo LLPS, in a lysine residue-dependent manner. GFP alone failed to form droplets under any conditions tested (Fig. 3d).","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":82,"end":82,"position":"Specific residue","statements":[{"type":"Results","text":"To confirm these results, we labeled both the complete and truncated cytoplasmic domain of syt1 (residues 80–421 and 143–421, respectively) with an organic dye (fluorescein) at native Cys residues 82 and 277."}]},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"},{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":277,"end":277,"position":"Specific residue","statements":[{"type":"Results","text":"To confirm these results, we labeled both the complete and truncated cytoplasmic domain of syt1 (residues 80–421 and 143–421, respectively) with an organic dye (fluorescein) at native Cys residues 82 and 277."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-08T14:50:47.927Z"}},{"start":80,"end":142,"reference_id":"38177243","reference_source":"pmid","reference_html":"The juxtamembrane linker of synaptotagmin 1 regulates Ca<sup>2+</sup> binding via liquid-liquid phase separation. <i> Mehta N, Mondal S, Watson ET, Cui Q, Chapman ER. </i> Nat Commun, 2024","date":"2024-03-08T09:36:11.828Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","region_id":"DP04144r004","statement":[{"text":"As an independent measure of droplet formation, we conducted dynamic light scattering (DLS) experiments, again using the constructs shown in Fig. 3a, b, and found that WT syt1 C2AB, bearing the juxtamembrane linker, as well as the isolated juxtamembrane linker (residues 80–142), yielded two distinct peaks with diameters corresponding to monomers as well as higher ordered structures. In sharp contrast, a single peak, corresponding to monomers, was observed for the other constructs, as shown and quantified in Supplementary Fig. 6a, b, and Supplementary Table 3, respectively. These findings are consistent with the microscopy experiments in Fig. 3c, d. Since our DLS approach cannot discriminate between sizes above 1 µm, we returned to microscopy to establish the relationship between [syt1 C2AB (80–421)-GFP] and droplet size. As expected, based on LLPS of various proteins58, we observed that droplet size increased with protein concentration (Supplementary Fig. 7a–e). Because the droplet number is confounded by droplet-droplet fusion, this parameter was not further analyzed.","type":"Results"},{"text":"These additional findings, combined with results in Fig. 2, provide compelling evidence that the lysine-rich motif in the juxtamembrane linker of syt1 predominantly mediates LLPS.","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEMBL","id":"CHEMBL1201478","statements":[{"type":"Results","text":"The isolated linker, GFP-syt1(80–142), also formed droplets, albeit at higher protein and PEG 8000 concentrations (Fig. 3f). Furthermore, we analyzed the syt1 C2AB constructs with truncated or mutated juxtamembrane linkers, as well as isolated JuxtaK mutant linker, and found that none of these constructs formed droplets, even at high protein and PEG 8000 concentrations (Supplementary Fig. 8a–c). "}]}],"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-08T14:50:51.345Z"}},{"start":80,"end":142,"reference_id":"38177243","reference_source":"pmid","reference_html":"The juxtamembrane linker of synaptotagmin 1 regulates Ca<sup>2+</sup> binding via liquid-liquid phase separation. <i> Mehta N, Mondal S, Watson ET, Cui Q, Chapman ER. </i> Nat Commun, 2024","date":"2024-01-12T17:52:21.924Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006067","ec_ontology":"ECO","ec_name":"fluorescence recovery after photobleaching evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","region_id":"DP04144r005","statement":[{"text":"Furthermore, we conducted fluorescence recovery after photobleaching (FRAP) experiment on the syt1 droplets; a time series of representative FRAP images are shown in Fig. 4b (see Supplementary Movie 5 for the video), clearly demonstrating recovery. The fluorescence recovery curve was best fitted with a hyperbolic function, yielding a t1/2 of 64 ± 2 s (Fig. 4c; see Methods for analysis details), which is characteristic of the protein mobility in bona fide LLPS droplets. Together, these droplet fusions and FRAP results confirm that syt1 C2AB (80–421)-GFP undergoes LLPS.","type":"Results"},{"text":"Syt1 droplets fuse with each other, and recover after photobleaching.","type":"Figure"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Figure","text":"Time series showing two droplets of syt1 C2AB (80–421)-GFP (3 µM protein, 3% PEG 8000) fuse and relax into a larger droplet."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-01-18T15:08:10.121Z"}},{"start":80,"end":142,"reference_id":"38177243","reference_source":"pmid","reference_html":"The juxtamembrane linker of synaptotagmin 1 regulates Ca<sup>2+</sup> binding via liquid-liquid phase separation. <i> Mehta N, Mondal S, Watson ET, Cui Q, Chapman ER. </i> Nat Commun, 2024","date":"2024-03-08T09:37:42.650Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"GO:0140694","term_name":"non-membrane-bounded organelle assembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Figure","text":"Immunoblot to estimate syt1 C2AB (80–421)-GFP expression levels in HEK293T cells compared to endogenous syt1 in cultured rat hippocampal neuronal lysates, probed using an anti-syt1 antibody. β-actin again served as a loading control; n = 2."}]}],"ec_go":"IDA","region_id":"DP04144r006","statement":[{"text":"Syt1 undergoes LLPS in cells","type":"Results"},{"text":"Upon overexpression, droplet formation by syt1 C2AB (80–421)-GFP was observed in the HEK293T cells; as shown in Fig. 6a, ~5–10 droplets formed in the cytoplasm of each cell. Consistent with our in vitro biochemical assays (see Fig. 3c), truncation of the linker, or substitution of the lysine residues within the linker, abolished droplet formation (Fig. 6b).","type":"Results"},{"text":"Together, these experiments demonstrate that the cytoplasmic domain of syt1 forms droplets in cells, including neurons where syt1 is normally expressed.","type":"Results"}],"term_comment":"","term_def":"\"The aggregation, arrangement and bonding together of a set of components to form a non-membrane-bounded organelle.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","statements":[{"type":"Results","text":"Upon overexpression, droplet formation by syt1 C2AB (80–421)-GFP was observed in the HEK293T cells; as shown in Fig. 6a, ~5–10 droplets formed in the cytoplasm of each cell."}],"entry_name":"Human Embryonic Kidney 293T"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-08T14:50:45.448Z"}},{"start":80,"end":142,"reference_id":"38177243","reference_source":"pmid","reference_html":"The juxtamembrane linker of synaptotagmin 1 regulates Ca<sup>2+</sup> binding via liquid-liquid phase separation. <i> Mehta N, Mondal S, Watson ET, Cui Q, Chapman ER. </i> Nat Commun, 2024","date":"2024-01-10T17:56:58.317Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042802","term_name":"identical protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P21707","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04144r009","statement":[{"text":"As an independent measure of droplet formation, we conducted dynamic light scattering (DLS) experiments, again using the constructs shown in Fig. 3a, b, and found that WT syt1 C2AB, bearing the juxtamembrane linker, as well as the isolated juxtamembrane linker (residues 80–142), yielded two distinct peaks with diameters corresponding to monomers as well as higher ordered structures.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein or proteins.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-12T17:44:22.188Z"}},{"start":86,"end":139,"reference_id":"24001110","reference_source":"pmid","reference_html":"The synaptotagmin 1 linker may function as an electrostatic zipper that opens for docking but closes for fusion pore opening. <i> Lai Y, Lou X, Jho Y, Yoon TY, Shin YK. </i> Biochem J, 2013","date":"2024-01-11T19:18:50.671Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031338","term_name":"regulation of vesicle fusion","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys86Glu","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test if the asymmetric charge distribution in the Syt1 linker region influences vesicle fusion, we investigated the effect of those Syt1 mutants we made (K86E, K86E/K90E and K86E/K90E/K95E and E131K, E131K/E135K and E131K/E135K/E139K) on vesicle docking and content mixing."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys90Glu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys95Glu","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test if the asymmetric charge distribution in the Syt1 linker region influences vesicle fusion, we investigated the effect of those Syt1 mutants we made (K86E, K86E/K90E and K86E/K90E/K95E and E131K, E131K/E135K and E131K/E135K/E139K) on vesicle docking and content mixing."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu131Lys","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test if the asymmetric charge distribution in the Syt1 linker region influences vesicle fusion, we investigated the effect of those Syt1 mutants we made (K86E, K86E/K90E and K86E/K90E/K95E and E131K, E131K/E135K and E131K/E135K/E139K) on vesicle docking and content mixing."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu135Lys","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test if the asymmetric charge distribution in the Syt1 linker region influences vesicle fusion, we investigated the effect of those Syt1 mutants we made (K86E, K86E/K90E and K86E/K90E/K95E and E131K, E131K/E135K and E131K/E135K/E139K) on vesicle docking and content mixing."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu139Lys","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test if the asymmetric charge distribution in the Syt1 linker region influences vesicle fusion, we investigated the effect of those Syt1 mutants we made (K86E, K86E/K90E and K86E/K90E/K95E and E131K, E131K/E135K and E131K/E135K/E139K) on vesicle docking and content mixing."}]}],"ec_go":"IMP","region_id":"DP04144r010","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:92974"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5497103"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5997"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:643960"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:11968038"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:16212738"}],"statement":[{"text":"However, for the double or triple mutants we clearly observed the impairment of fusion pore opening (Figure 3B, middle and right-hand panels) in the presence of 500 μM Ca2+. The quantitative analysis revealed that after 1 min, content mixing for the double mutants was reduced by 20~30% when compared with that of wild-type Syt1, whereas the triple mutants had as much as a 50% reduction (Figure 3C). Thus the results of the present study suggest that the bipolar charge distribution contributes to fusion pore opening in a positive way.","type":"Results"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of vesicle fusion.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-12T17:44:20.940Z"}},{"start":80,"end":139,"reference_id":"24001110","reference_source":"pmid","reference_html":"The synaptotagmin 1 linker may function as an electrostatic zipper that opens for docking but closes for fusion pore opening. <i> Lai Y, Lou X, Jho Y, Yoon TY, Shin YK. </i> Biochem J, 2013","date":"2024-01-18T16:39:11.148Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0048278","term_name":"vesicle docking","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006077","ec_ontology":"ECO","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys277Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"A native cysteine residue at position 277 in wild-type Syt1 was mutated to an alanine, followed by mutation of Gly92 and Gly130 to cysteine."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly92Cys","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"A native cysteine residue at position 277 in wild-type Syt1 was mutated to an alanine, followed by mutation of Gly92 and Gly130 to cysteine."},{"type":"Results","text":"The double cysteine residue mutant was cross-linked with 1 mM H2O2."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly130Cys","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"A native cysteine residue at position 277 in wild-type Syt1 was mutated to an alanine, followed by mutation of Gly92 and Gly130 to cysteine."},{"type":"Results","text":"The double cysteine residue mutant was cross-linked with 1 mM H2O2."}]}],"ec_go":"IPI","region_id":"DP04144r011","statement":[{"text":"We found that the cross-linked Syt1 mutants could reduce vesicle docking by approximately 40%. Although the changes appear to be statistically insignificant, the inhibition of vesicle docking could be recovered when the sample was treated with DTT within experimental errors (Figure 4B). Thus the results suggest that the flexibility of the linker region is favourable for Syt1 in assisting vesicle docking.","type":"Results"},{"text":"Thus the results of the present study support the notion that an extended and flexible linker region is preferred for Syt1 to induce vesicle docking to the plasma membrane, whereas a shorter linker region is favoured for Syt1 to drive fusion pore opening.","type":"Results"}],"term_comment":"","term_def":"\"The initial attachment of a transport vesicle membrane to the target membrane, mediated by proteins protruding from the membrane of the vesicle and the target membrane. Docking requires only that the two membranes come close enough for these proteins to interact and adhere.\" [GOC:ai, GOC:jid]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"Ensembl","id":"92974","operator":"and","partner_start":null,"partner_end":null},{"db":"Ensembl","id":"16212738","operator":"and","partner_start":null,"partner_end":null},{"db":"Ensembl","id":"11968038","operator":"and","partner_start":null,"partner_end":null},{"db":"Ensembl","id":"643960","operator":"and","partner_start":null,"partner_end":null},{"db":"Ensembl","id":"5997","operator":"and","partner_start":null,"partner_end":null},{"db":"Ensembl","id":"5497103","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-08T09:37:45.320Z"}},{"start":80,"end":139,"reference_id":"24001110","reference_source":"pmid","reference_html":"The synaptotagmin 1 linker may function as an electrostatic zipper that opens for docking but closes for fusion pore opening. <i> Lai Y, Lou X, Jho Y, Yoon TY, Shin YK. </i> Biochem J, 2013","date":"2024-01-18T16:39:25.453Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006906","term_name":"vesicle fusion","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys277Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"A native cysteine residue at position 277 in wild-type Syt1 was mutated to an alanine, followed by mutation of Gly92 and Gly130 to cysteine."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly92Cys","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"A native cysteine residue at position 277 in wild-type Syt1 was mutated to an alanine, followed by mutation of Gly92 and Gly130 to cysteine."},{"type":"Results","text":"The double cysteine residue mutant was cross-linked with 1 mM H2O2."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly130Cys","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"A native cysteine residue at position 277 in wild-type Syt1 was mutated to an alanine, followed by mutation of Gly92 and Gly130 to cysteine."},{"type":"Results","text":"The double cysteine residue mutant was cross-linked with 1 mM H2O2."}]}],"ec_go":"IDA","region_id":"DP04144r012","statement":[{"text":"In contrast, in the content-mixing assay, cross-linked Syt1 enhanced fusion pore opening compared with wild-type Syt1 by approximately 50% (Figures 4C and 4D), which also could be negated by DTT. Thus the results show that the folded linker region is preferable for Syt1/Ca2+ to drive opening of the fusion pore for content mixing.","type":"Results"},{"text":"Thus the results of the present study support the notion that an extended and flexible linker region is preferred for Syt1 to induce vesicle docking to the plasma membrane, whereas a shorter linker region is favoured for Syt1 to drive fusion pore opening.","type":"Results"}],"term_comment":"","term_def":"\"Fusion of the membrane of a transport vesicle with its target membrane.\" [GOC:jid]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-08T09:37:49.541Z"}},{"start":99,"end":140,"reference_id":"24001110","reference_source":"pmid","reference_html":"The synaptotagmin 1 linker may function as an electrostatic zipper that opens for docking but closes for fusion pore opening. <i> Lai Y, Lou X, Jho Y, Yoon TY, Shin YK. </i> Biochem J, 2013","date":"2024-01-18T16:16:25.162Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0048278","term_name":"vesicle docking","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Asp99Glu130del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04144r013","statement":[{"text":"To further substantiate this observation, we made the linker of Syt1 shorter by deleting 40 amino acids [Δ(99–140)aa]. As expected, the truncated mutant of Syt1 reduced the vesicle docking by ~50%, but enhanced fusion pore opening by more than 40% (Figure 4E). Thus the results of the present study support the notion that an extended and flexible linker region is preferred for Syt1 to induce vesicle docking to the plasma membrane, whereas a shorter linker region is favoured for Syt1 to drive fusion pore opening.","type":"Results"}],"term_comment":"","term_def":"\"The initial attachment of a transport vesicle membrane to the target membrane, mediated by proteins protruding from the membrane of the vesicle and the target membrane. Docking requires only that the two membranes come close enough for these proteins to interact and adhere.\" [GOC:ai, GOC:jid]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-08T09:37:51.355Z"}},{"start":99,"end":140,"reference_id":"24001110","reference_source":"pmid","reference_html":"The synaptotagmin 1 linker may function as an electrostatic zipper that opens for docking but closes for fusion pore opening. <i> Lai Y, Lou X, Jho Y, Yoon TY, Shin YK. </i> Biochem J, 2013","date":"2024-01-18T16:17:20.590Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006906","term_name":"vesicle fusion","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007092","ec_ontology":"ECO","ec_name":"gain-of-function mutant phenotypic evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Asp99Glu130del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04144r014","statement":[{"text":"To further substantiate this observation, we made the linker of Syt1 shorter by deleting 40 amino acids [Δ(99–140)aa]. As expected, the truncated mutant of Syt1 reduced the vesicle docking by ~50%, but enhanced fusion pore opening by more than 40% (Figure 4E). Thus the results of the present study support the notion that an extended and flexible linker region is preferred for Syt1 to induce vesicle docking to the plasma membrane, whereas a shorter linker region is favoured for Syt1 to drive fusion pore opening.","type":"Results"}],"term_comment":"","term_def":"\"Fusion of the membrane of a transport vesicle with its target membrane.\" [GOC:jid]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-08T09:37:54.526Z"}},{"start":80,"end":139,"reference_id":"24001110","reference_source":"pmid","reference_html":"The synaptotagmin 1 linker may function as an electrostatic zipper that opens for docking but closes for fusion pore opening. <i> Lai Y, Lou X, Jho Y, Yoon TY, Shin YK. </i> Biochem J, 2013","date":"2024-01-18T16:39:40.235Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0061891","term_name":"calcium ion sensor activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006289","ec_ontology":"ECO","ec_name":"site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly130Cys","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To examine whether t-vesicle binding in the absence or presence of Ca2+ could induce conformation changes in the linker of Syt1, we used SDSL and the EPR analysis of the spin-labelled Syt1 G130C mutant."}]}],"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"29108","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04144r015","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":"16212738"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:11968038"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:643960"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5997"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:92974"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"We found that the linker was in a flexible conformation when reconstituted on v-vesicles (Figure 5A, □). Upon binding to t-vesicles in the absence of Ca2+, the linker region became slightly more flexible as the EPR lines got somewhat narrower (Figure 5A, ○). However, an opposite conformation change happened when Syt1 bound to t-vesicles with Ca2+ (Figure 5A, △), which indicated a conformation change from flexible to restricted.","type":"Results"}],"term_comment":"","term_def":"\"Binding to and responding, e.g. by conformational change, to changes in the cellular level of calcium ions (Ca2+).\" [PMID:16005298, PMID:17020874, PMID:28151650]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-08T09:37:56.172Z"}},{"start":80,"end":139,"reference_id":"24001110","reference_source":"pmid","reference_html":"The synaptotagmin 1 linker may function as an electrostatic zipper that opens for docking but closes for fusion pore opening. <i> Lai Y, Lou X, Jho Y, Yoon TY, Shin YK. </i> Biochem J, 2013","date":"2024-01-18T16:39:48.848Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Asp99Glu130del","start":null,"end":null,"position":null}],"region_id":"DP04144r016","statement":[{"text":"The 60-residue-long linker can theoretically extend as much as 30 nm, which will allow the C2AB domain to reach out to bind t-SNARE on the target membrane [16,17].","type":"Discussion"},{"text":"To further substantiate this observation, we made the linker of Syt1 shorter by deleting 40 amino acids [Δ(99–140)aa]. As expected, the truncated mutant of Syt1 reduced the vesicle docking by ~50%, but enhanced fusion pore opening by more than 40% (Figure 4E). Thus the results of the present study support the notion that an extended and flexible linker region is preferred for Syt1 to induce vesicle docking to the plasma membrane, whereas a shorter linker region is favoured for Syt1 to drive fusion pore opening.","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-08T09:37:57.881Z"}}],"regions_counter":16,"released":"2024_06","sequence":"MVSASHPEALAAPVTTVATLVPHNATEPASPGEGKEDAFSKLKQKFMNELHKIPLPPWALIAIAIVAVLLVVTCCFCVCKKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKLGKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEFKVPMNTVDFGHVTEEWRDLQSAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVFVGYNSTGAELRHWSDMLANPRRPIAQWHTLQVEEEVDAMLAVKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"alphafold_very_low_content":0.1496437054631829,"dataset":["Condensates-related proteins"],"disorder_content":0.1496437054631829,"disprot_consensus":{"full":[{"start":80,"end":142,"type":"D"}],"Structural state":[{"start":80,"end":142,"type":"D"}],"Biological process":[{"start":80,"end":142,"type":"F"}],"Molecular function":[{"start":80,"end":142,"type":"F"}],"Disorder function":[{"start":80,"end":139,"type":"F"}]}},{"disprot_id":"DP04145","acc":"P21579","creator":"vnugnes","date":"2024-01-10T14:18:46.950Z","features":{"pfam":[{"id":"PF00168","name":"C2 domain","start":158,"end":263},{"id":"PF00168","name":"C2 domain","start":288,"end":393}],"gene3D":[]},"genes":[{"name":{"value":"SYT1"},"synonyms":[{"value":"SVP65"},{"value":"SYT"}]}],"length":422,"name":"Synaptotagmin-1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":81,"end":142,"reference_id":"27191789","reference_source":"pmid","reference_html":"Synaptotagmin I's Intrinsically Disordered Region Interacts with Synaptic Vesicle Lipids and Exerts Allosteric Control over C2A. <i> Fealey ME, Mahling R, Rice AM, Dunleavy K, Kobany SE, Lohese KJ, Horn B, Hinderliter A. </i> Biochemistry, 2016","date":"2024-01-10T14:23:09.568Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"For nuclear magnetic resonance experiments, a linker region gene encoding residues 81–142, with additional codons for a single C-terminal tryptophan followed by a His tag, was designed: KKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKWHHHHHH."}]}],"region_id":"DP04145r001","sequence_construct":"KKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKWHHHHHH","statement":[{"text":"Regardless, we were still able to assess residual secondary structure from the residues examined by subtracting IDP/IDR-specific random coil chemical shifts from the observed Cα, Cβ, and carbonyl carbon chemical shifts. (25) In a majority of assigned residues subjected to this secondary structure analysis, there appears to be no strong preference for residual structure; both Cα–Cβ and carbonyl carbon chemical shift differences alternate between positive and negative values, indicating this linker region is largely random coil in solution (Figure 3B,C).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-12T17:59:12.791Z"}},{"start":81,"end":142,"reference_id":"27191789","reference_source":"pmid","reference_html":"Synaptotagmin I's Intrinsically Disordered Region Interacts with Synaptic Vesicle Lipids and Exerts Allosteric Control over C2A. <i> Fealey ME, Mahling R, Rice AM, Dunleavy K, Kobany SE, Lohese KJ, Horn B, Hinderliter A. </i> Biochemistry, 2016","date":"2024-01-10T14:23:25.593Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"For nuclear magnetic resonance experiments, a linker region gene encoding residues 81–142, with additional codons for a single C-terminal tryptophan followed by a His tag, was designed: KKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKWHHHHHH."}]}],"region_id":"DP04145r002","sequence_construct":"KKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKWHHHHHH","statement":[{"text":"Regardless, we were still able to assess residual secondary structure from the residues examined by subtracting IDP/IDR-specific random coil chemical shifts from the observed Cα, Cβ, and carbonyl carbon chemical shifts. (25) In a majority of assigned residues subjected to this secondary structure analysis, there appears to be no strong preference for residual structure; both Cα–Cβ and carbonyl carbon chemical shift differences alternate between positive and negative values, indicating this linker region is largely random coil in solution (Figure 3B,C). ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-12T17:59:21.506Z"}},{"start":81,"end":142,"reference_id":"27191789","reference_source":"pmid","reference_html":"Synaptotagmin I's Intrinsically Disordered Region Interacts with Synaptic Vesicle Lipids and Exerts Allosteric Control over C2A. <i> Fealey ME, Mahling R, Rice AM, Dunleavy K, Kobany SE, Lohese KJ, Horn B, Hinderliter A. </i> Biochemistry, 2016","date":"2024-01-10T15:01:06.142Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04145r003","sequence_construct":"KKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKLGKLQYSLDYDFQNN","statement":[{"text":"This finding is consistent with circular dichroism measurements of the IDR (Figure 3D) and predictions of Composition Profiler (Table S2). However, there may still be minor residual helical content given that equilibration with increasing concentrations of urea results in the absorption profile of the juxtamembrane linker more closely resembling that of random coil (Figure 3D).","type":"Results"},{"text":"For DSC and CD experiments for which small quantities of protein are needed, the linker region peptide specifically encoding residues 81–157 was produced via solid state synthesis through the University of Minnesota Genomics Center: KKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKLGKLQYSLDYDFQNN. Inclusion of residues 143–157, which corresponds to part of C2A’s first β-strand, was done so that the peptide would contain absorbing residues for measuring concentration.","type":"Methods"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-12T17:59:24.250Z"}},{"start":81,"end":142,"reference_id":"27191789","reference_source":"pmid","reference_html":"Synaptotagmin I's Intrinsically Disordered Region Interacts with Synaptic Vesicle Lipids and Exerts Allosteric Control over C2A. <i> Fealey ME, Mahling R, Rice AM, Dunleavy K, Kobany SE, Lohese KJ, Horn B, Hinderliter A. </i> Biochemistry, 2016","date":"2024-01-10T15:01:14.657Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04145r004","sequence_construct":"KKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKLGKLQYSLDYDFQNN","statement":[{"text":"This finding is consistent with circular dichroism measurements of the IDR (Figure 3D) and predictions of Composition Profiler (Table S2). However, there may still be minor residual helical content given that equilibration with increasing concentrations of urea results in the absorption profile of the juxtamembrane linker more closely resembling that of random coil (Figure 3D).","type":"Results"},{"text":"For DSC and CD experiments for which small quantities of protein are needed, the linker region peptide specifically encoding residues 81–157 was produced via solid state synthesis through the University of Minnesota Genomics Center: KKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKLGKLQYSLDYDFQNN. Inclusion of residues 143–157, which corresponds to part of C2A’s first β-strand, was done so that the peptide would contain absorbing residues for measuring concentration.","type":"Methods"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-01-12T17:59:15.368Z"}},{"start":81,"end":142,"reference_id":"27191789","reference_source":"pmid","reference_html":"Synaptotagmin I's Intrinsically Disordered Region Interacts with Synaptic Vesicle Lipids and Exerts Allosteric Control over C2A. <i> Fealey ME, Mahling R, Rice AM, Dunleavy K, Kobany SE, Lohese KJ, Horn B, Hinderliter A. </i> Biochemistry, 2016","date":"2025-06-18T15:08:32.313Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006232","ec_ontology":"ECO","ec_name":"differential scanning calorimetry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"ec_go":"IDA","interaction_partner":[{"db":"ChEBI","id":"16113","operator":"and","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"73215","operator":"and","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"79098","operator":"and","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"73124","operator":"and","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"73001","operator":"and","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"75038","operator":"and","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"78266","operator":"and","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"78260","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04145r005","sequence_construct":"KKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKLGKLQYSLDYDFQNN","statement":[{"text":"These results suggest that, with a synaptic vesicle-like environment, Syt I’s juxtamembrane IDR can exist in a membrane-associated state that has measurable heat capacity. While DSC does not provide direct information about the type of folded structure, the small endotherm (particularly on the reversibility scan, dashed light green) does indicate weak intramolecular interactions within the IDR when it is membrane-associated.","type":"Results"},{"text":"For DSC and CD experiments for which small quantities of protein are needed, the linker region peptide specifically encoding residues 81–157 was produced via solid state synthesis through the University of Minnesota Genomics Center: KKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKLGKLQYSLDYDFQNN. Inclusion of residues 143–157, which corresponds to part of C2A’s first β-strand, was done so that the peptide would contain absorbing residues for measuring concentration.","type":"Methods"},{"text":"In the presence of a complex lipid mixture that mimics the outer leaflet of a synaptic vesicle (Figure 1B), we found through DSC (Figure 2) and NMR (Figure 4) measurements that the IDR experiences endotherm and chemical shift changes, respectively, consistent with IDR–synaptic lipid interactions, though in a mostly disordered structural state.","type":"Discussion"},{"text":"Synaptic vesicle mimic were prepared in a final cholesterol content of ∼31% of total lipid and with the lipids: 1-stearoyl-2-docosahexaenoyl-sn-glycero-3-phosphoethanolamine (18:0, 22:6 PE), 1-stearoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (18:0, 18:1 PE), 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (16:0, 18:1 PE), 1-stearoyl-2-docosahexaenoyl-sn-glycero-3-phosphoserine (18:0, 22:6 PS), 1-stearoyl-2-oleoyl-sn-glycero-3-phosphoserine (18:0, 18:1 PS), 1-stearoyl-2-arachidonoyl-sn-glycero-3-phospho(1′-myo-inositol-4′,5′-bisphosphate) [18:0, 20:4 PI(4,5)P2], 1,2-dioleoyl-sn-glycero-3-phospho(1′-myo-inositol-4′,5′-bisphosphate) [18:1, 18:1 PI(4,5)P2], 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoinositol (16:0, 18:1 PI).","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"46891800"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"44251424"}]},{"start":101,"end":119,"reference_id":"27191789","reference_source":"pmid","reference_html":"Synaptotagmin I's Intrinsically Disordered Region Interacts with Synaptic Vesicle Lipids and Exerts Allosteric Control over C2A. <i> Fealey ME, Mahling R, Rice AM, Dunleavy K, Kobany SE, Lohese KJ, Horn B, Hinderliter A. </i> Biochemistry, 2016","date":"2025-06-16T15:21:09.300Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"For nuclear magnetic resonance experiments, a linker region gene encoding residues 81–142, with additional codons for a single C-terminal tryptophan followed by a His tag, was designed: KKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKWHHHHHH."}]}],"ec_go":"EXP","region_id":"DP04145r006","sequence_construct":"KKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKWHHHHHH","statement":[{"text":"POPC:POPS SUVs showed little to no effect, largely causing peak broadening (and disappearance) presumably because of membrane association (Figure 4A). In contrast, synaptic lipid SUVs caused more pronounced spectral changes. For example, residues A101, I102, V107, T113, A118, and L119 seem to experience larger changes in their local environment as their membrane-free chemical shifts are missing in the presence of synaptic lipid SUVs (Figure 4B–D). More generally, the spectra show greater peak dispersion and some chemical exchange (Figure 4D).","type":"Results"},{"text":"In the presence of a complex lipid mixture that mimics the outer leaflet of a synaptic vesicle (Figure 1B), we found through DSC (Figure 2) and NMR (Figure 4) measurements that the IDR experiences endotherm and chemical shift changes, respectively, consistent with IDR–synaptic lipid interactions, though in a mostly disordered structural state.","type":"Discussion"},{"text":"Synaptic vesicle mimic were prepared in a final cholesterol content of ∼31% of total lipid and with the lipids: 1-stearoyl-2-docosahexaenoyl-sn-glycero-3-phosphoethanolamine (18:0, 22:6 PE), 1-stearoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (18:0, 18:1 PE), 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (16:0, 18:1 PE), 1-stearoyl-2-docosahexaenoyl-sn-glycero-3-phosphoserine (18:0, 22:6 PS), 1-stearoyl-2-oleoyl-sn-glycero-3-phosphoserine (18:0, 18:1 PS), 1-stearoyl-2-arachidonoyl-sn-glycero-3-phospho(1′-myo-inositol-4′,5′-bisphosphate) [18:0, 20:4 PI(4,5)P2], 1,2-dioleoyl-sn-glycero-3-phospho(1′-myo-inositol-4′,5′-bisphosphate) [18:1, 18:1 PI(4,5)P2], 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoinositol (16:0, 18:1 PI).","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":81,"end":142,"reference_id":"27191789","reference_source":"pmid","reference_html":"Synaptotagmin I's Intrinsically Disordered Region Interacts with Synaptic Vesicle Lipids and Exerts Allosteric Control over C2A. <i> Fealey ME, Mahling R, Rice AM, Dunleavy K, Kobany SE, Lohese KJ, Horn B, Hinderliter A. </i> Biochemistry, 2016","date":"2024-01-10T16:29:39.692Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0016050","term_name":"vesicle organization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001159","ec_ontology":"ECO","ec_name":"carboxyfluorescein diacetate succinimidyl ester staining evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","region_id":"DP04145r007","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5283499","statements":[{"type":"Figure","text":"LUVs containing 50 mM CF and consisting of a 38:38:24 POPE:SOPE:POPS molar ratio were cooled from 37 to 7 °C (temperature indicated by black dotted line)."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:9546742","statements":[{"type":"Figure","text":"LUVs containing 50 mM CF and consisting of a 38:38:24 POPE:SOPE:POPS molar ratio were cooled from 37 to 7 °C (temperature indicated by black dotted line)."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:5282290","statements":[{"type":"Figure","text":"LUVs containing 50 mM CF and consisting of a 38:38:24 POPE:SOPE:POPS molar ratio were cooled from 37 to 7 °C (temperature indicated by black dotted line)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:13518295"}],"statement":[{"text":"When the CF-containing vesicles were cooled through their transition temperature in the presence of juxtamembrane linker peptide, the percentage of maximal dye efflux increased by 28 relative to that of the liposomes alone (Figure 7). As a positive control, we also performed the experiment with Ca2+-bound short C2A and found that the percentage of maximal dye efflux was increased by 15. This indicates that the magnitude of dye efflux with the IDR is likely relevant to destabilizing the membrane as maximal efflux exceeds that of the known C2A intercalator. Consistent with the EPR measurements of partial insertion, the juxtamembrane linker destabilizes the membrane. This result may be relevant to protein intercalation as a way of destabilizing the membrane and consequently lowering the energetic barrier to fusion.","type":"Results"}],"term_comment":"","term_def":"\"A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a vesicle.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-16T13:22:10.682Z"}},{"start":81,"end":142,"reference_id":"27191789","reference_source":"pmid","reference_html":"Synaptotagmin I's Intrinsically Disordered Region Interacts with Synaptic Vesicle Lipids and Exerts Allosteric Control over C2A. <i> Fealey ME, Mahling R, Rice AM, Dunleavy K, Kobany SE, Lohese KJ, Horn B, Hinderliter A. </i> Biochemistry, 2016","date":"2024-01-10T16:41:15.238Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1901876","term_name":"regulation of calcium ion binding","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"29108","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04145r008","statement":[{"text":"In this case, the σ of ∼4 indicates that residues 96–139 confer modest positive cooperativity to C2A’s Ca2+-binding sites, consistent with terbium binding studies performed previously on these same two C2A constructs.","type":"Results"},{"text":"The end result of IDR inclusion, however, appears to be pronounced alteration of the thermodynamic parameters describing Ca2+ binding. Long C2A is still Ca2+ binding-competent as evidenced by the fact that addition of Ca2+ to the long C2A construct in the absence of any lipid ligand still results in an elevated unfolding temperature (Figure 6C) as would be expected from chelation of ligand.","type":"Results"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of calcium ion binding.\" [GOC:BHF, GOC:rl, GOC:TermGenie, PMID:16432188]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-16T13:22:07.256Z"}},{"start":81,"end":98,"reference_id":"25973365","reference_source":"pmid","reference_html":"The synaptotagmin juxtamembrane domain is involved in neuroexocytosis. <i> Caccin P, Scorzeto M, Damiano N, Marin O, Megighian A, Montecucco C. </i> FEBS Open Bio, 2015","date":"2025-06-16T15:35:30.300Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042734","term_name":"presynaptic membrane","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IDA","region_id":"DP04145r011","statement":[{"text":"Out of line with these results, unexpectedly, there is a comparatively lower staining by the h-FJMS peptide of the SVs, which are largely localized inside the motor axon terminal, as documented by comparison with the staining of an antibody specific for the vesicular acetylcholine transporter (Fig. 6). Taken together these data suggest that a large part of the fluorescent peptide inserts into the presynaptic membrane.","type":"Results"}],"term_comment":"","term_def":"\"A specialized area of membrane of the axon terminal that faces the plasma membrane of the neuron or muscle fiber with which the axon terminal establishes a synaptic junction; many synaptic junctions exhibit structural presynaptic characteristics, such as conical, electron-dense internal protrusions, that distinguish it from the remainder of the axon plasma membrane.\" [GOC:jl, ISBN:0815316194]","term_is_obsolete":false,"term_not_annotate":false},{"start":81,"end":98,"reference_id":"25973365","reference_source":"pmid","reference_html":"The synaptotagmin juxtamembrane domain is involved in neuroexocytosis. <i> Caccin P, Scorzeto M, Damiano N, Marin O, Megighian A, Montecucco C. </i> FEBS Open Bio, 2015","date":"2025-06-16T15:35:45.751Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005543","term_name":"phospholipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IDA","region_id":"DP04145r012","statement":[{"text":"Fig. 7 shows that the h-FJMS indeed binds anionic phospholipids, including phosphatidylserine and phosphatidylinositides (PIs), which are enriched in the SV membrane and on the cytosolic face of the PM [39], [41].","type":"Results"}],"term_comment":"","term_def":"\"Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester.\" [ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":12,"released":"2024_06","sequence":"MVSESHHEALAAPPVTTVATVLPSNATEPASPGEGKEDAFSKLKEKFMNELHKIPLPPWALIAIAIVAVLLVLTCCFCICKKCLFKKKNKKKGKEKGGKNAINMKDVKDLGKTMKDQALKDDDAETGLTDGEEKEEPKEEEKLGKLQYSLDYDFQNNQLLVGIIQAAELPALDMGGTSDPYVKVFLLPDKKKKFETKVHRKTLNPVFNEQFTFKVPYSELGGKTLVMAVYDFDRFSKHDIIGEFKVPMNTVDFGHVTEEWRDLQSAEKEEQEKLGDICFSLRYVPTAGKLTVVILEAKNLKKMDVGGLSDPYVKIHLMQNGKRLKKKKTTIKKNTLNPYYNESFSFEVPFEQIQKVQVVVTVLDYDKIGKNDAIGKVFVGYNSTGAELRHWSDMLANPRRPIAQWHTLQVEEEVDAMLAVKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.1895734597156398,"dataset":["NDDs-related proteins"],"disorder_content":0.14691943127962084,"disprot_consensus":{"full":[{"start":81,"end":142,"type":"D"}],"Structural state":[{"start":81,"end":142,"type":"D"}],"Disorder function":[{"start":81,"end":142,"type":"F"}],"Molecular function":[{"start":81,"end":142,"type":"F"}],"Biological process":[{"start":81,"end":142,"type":"F"}],"Cellular component":[{"start":81,"end":98,"type":"F"}]}},{"disprot_id":"DP04148","acc":"P08453","creator":"mmarengo","date":"2024-02-15T15:59:13.920Z","features":{"pfam":[{"id":"PF13016","name":"Cys-rich Gliadin N-terminal","start":167,"end":243}],"gene3D":[]},"genes":[],"length":327,"name":"Gamma-gliadin","ncbi_taxon_id":4565,"organism":"Triticum aestivum","regions":[{"start":1,"end":162,"reference_id":"32991891","reference_source":"pmid","reference_html":"New exploration of the γ-gliadin structure through its partial hydrolysis. <i> Sahli L, Boire A, Solé-Jamault V, Rogniaux H, Giuliani A, Roblin P, Renard D. </i> Int J Biol Macromol, 2020","date":"2024-02-15T17:34:43.426Z","curator_id":"mmarengo","curator_name":"Mauro Marengo","curator_orcid":"0000-0002-5389-3979","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006202","ec_ontology":"ECO","ec_name":"synchrotron radiation circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04148r001","statement":[{"text":"Spectral deconvolution of N-terminal domain spectrum using Bestsel\nsoftware [46] suggests the high disordered content of the N-terminal\ndomain (51.5% unordered structures, 2.5% α-helix, 27.3% β-strand,\n18.7% turn). ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-19T15:11:35.101Z"}},{"start":1,"end":162,"reference_id":"32991891","reference_source":"pmid","reference_html":"New exploration of the γ-gliadin structure through its partial hydrolysis. <i> Sahli L, Boire A, Solé-Jamault V, Rogniaux H, Giuliani A, Roblin P, Renard D. </i> Int J Biol Macromol, 2020","date":"2024-02-28T08:28:57.247Z","curator_id":"mmarengo","curator_name":"Mauro Marengo","curator_orcid":"0000-0002-5389-3979","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006202","ec_ontology":"ECO","ec_name":"synchrotron radiation circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04148r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16236","statements":[{"type":"Results","text":"N-terminal domain tends to lose disordered structures in favor of ß-strands (from 51.5% unordered structures, 27.3% ß-strands at 55% ethanol (v/v) to 41.1% unordered structures, 38.9% ß-strands at 20% ethanol (v/v))."}],"entry_name":"ethanol"}],"statement":[{"text":"N-terminal domain tends to lose disordered structures in favor of ß-strands (from 51.5% unordered structures, 27.3% ß-strands at 55% ethanol (v/v) to 41.1% unordered structures, 38.9% ß-strands at 20% ethanol (v/v)).","type":"Results"},{"text":"The repetitive N-terminal domain appears to fold into ß-strand structures while the non-repetitive C-terminal domain seems to gain α-helix and disordered content in detriment to the β structures. The presence of disorder to order transitions within the N-terminal may be consistent with the propensity of IDPs to this type of\ntransition, due their flexibility and lack of structural constraint\n[25,47,48].","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-04T08:43:55.752Z"}},{"start":1,"end":162,"reference_id":"32991891","reference_source":"pmid","reference_html":"New exploration of the γ-gliadin structure through its partial hydrolysis. <i> Sahli L, Boire A, Solé-Jamault V, Rogniaux H, Giuliani A, Roblin P, Renard D. </i> Int J Biol Macromol, 2020","date":"2024-03-04T11:29:50.701Z","curator_id":"mmarengo","curator_name":"Mauro Marengo","curator_orcid":"0000-0002-5389-3979","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006202","ec_ontology":"ECO","ec_name":"synchrotron radiation circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04148r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16236","entry_name":"ethanol"}],"statement":[{"text":"N-terminal domain tends to lose disordered structures in favor of ß-strands (from 51.5% unordered structures, 27.3% ß-strands at 55% ethanol (v/v) to 41.1% unordered structures, 38.9% ß-strands at 20% ethanol (v/v)).","type":"Results"},{"text":"The repetitive N-terminal domain appears to fold into ß-strand structures while the non-repetitive C-terminal domain seems to gain α-helix and disordered content in detriment to the β structures. The presence of disorder to order transitions within the N-terminal may be consistent with the propensity of IDPs to this type of transition, due their flexibility and lack of structural constraint [25,47,48].","type":"Results"}],"states_connection":[{"source":"DP04148r001","target":"DP04148r002"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-04T18:17:44.946Z"}},{"start":1,"end":162,"reference_id":"32991891","reference_source":"pmid","reference_html":"New exploration of the γ-gliadin structure through its partial hydrolysis. <i> Sahli L, Boire A, Solé-Jamault V, Rogniaux H, Giuliani A, Roblin P, Renard D. </i> Int J Biol Macromol, 2020","date":"2024-02-28T08:55:45.721Z","curator_id":"mmarengo","curator_name":"Mauro Marengo","curator_orcid":"0000-0002-5389-3979","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04148r004","statement":[{"text":"Contrary to the C-terminal domain, N-terminal domain exhibit over-estimated\napparent molecular weight (SDS-PAGE, Fig. 2A&B). This electrophoretic profile was also observed in the case of the γ44-gliadin full length [36] and suggests a conformational specificities of the domain, in line with our previous predictions. Since disordered proteins are known for their abnormal electrophoretic mobility due to their hydrodynamic radius, higher than those of the globular protein (such as C-terminal domain) [44,45], this may suggest that the repetitive N-terminal is indeed disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-04T08:43:57.179Z"}},{"start":1,"end":162,"reference_id":"32991891","reference_source":"pmid","reference_html":"New exploration of the γ-gliadin structure through its partial hydrolysis. <i> Sahli L, Boire A, Solé-Jamault V, Rogniaux H, Giuliani A, Roblin P, Renard D. </i> Int J Biol Macromol, 2020","date":"2024-02-28T08:59:11.632Z","curator_id":"mmarengo","curator_name":"Mauro Marengo","curator_orcid":"0000-0002-5389-3979","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04148r005","statement":[{"text":"The N-terminal domain radius is equivalent to the whole protein radius. These results may emphasize the expanded conformation of the N-terminal domain contrasting with the compact conformation of the C-terminal domain. As aforementioned, disordered proteins have larger hydrodynamic dimensions compared to conventional globular proteins [33,44].","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-04T08:43:59.022Z"}},{"start":1,"end":162,"reference_id":"32991891","reference_source":"pmid","reference_html":"New exploration of the γ-gliadin structure through its partial hydrolysis. <i> Sahli L, Boire A, Solé-Jamault V, Rogniaux H, Giuliani A, Roblin P, Renard D. </i> Int J Biol Macromol, 2020","date":"2024-02-28T09:39:57.502Z","curator_id":"mmarengo","curator_name":"Mauro Marengo","curator_orcid":"0000-0002-5389-3979","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04148r006","statement":[{"text":"The disorder of the N-terminal domain and the order of the C-terminal domain are visible in the shape of the pair distance. distribution functions p(r) (Fig. 6B). The maximum distance (Dmax) found for γ44-gliadin, N-terminal domain and C-terminal domain are respectively of 255 Å, 150 Å and 100 Å. The large Dmax of the N-terminal domain suggests an extended conformation, while the lower Dmax of the C-terminal domain suggests a compact conformation.","type":"Results"},{"text":"Finally, SAXS experiments provide ensemble-averaged structural information about the γ44-gliadin and its isolated domains. All structural data obtained are summarized in Table 3. SAXS experiments are complementary to CD results. They also suggest that the N-terminal domain is unordered in contrast to the globular-like shape of the C-terminal domain.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-04T08:44:02.331Z"}},{"start":1,"end":327,"reference_id":"31527735","reference_source":"pmid","reference_html":"Role of protein conformation and weak interactions on γ-gliadin liquid-liquid phase separation. <i> Sahli L, Renard D, Solé-Jamault V, Giuliani A, Boire A. </i> Sci Rep, 2019","date":"2024-03-12T09:50:41.725Z","curator_id":"mmarengo","curator_name":"Mauro Marengo","curator_orcid":"0000-0002-5389-3979","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","region_id":"DP04148r007","statement":[{"text":"Microscopic observations reveal that this increase of absorbance values is due to highly dynamic and spherical micrometric droplets (Fig. 4).","type":"Results"},{"text":"The number and the size of formed droplets increase with increasing protein concentration (Fig. 4B).","type":"Results"},{"text":"Microscopic imaging shows a decrease of the number of droplets with decreasing protein concentration until a total disappearance at low protein concentration (Fig. 4C). These observations show the ability of γ44-gliadin to form reversible assemblies upon solvent quality change.","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-13T13:22:05.190Z"}}],"regions_counter":7,"released":"2024_06","sequence":"MKTLLILTILAMAITIGTANIQVDPSGQVQWLQQQLVPQLQQPLSQQPQQTFPQPQQTFPHQPQQQVPQPQQPQQPFLQPQQPFPQQPQQPFPQTQQPQQPFPQQPQQPFPQTQQPQQPFPQQPQQPFPQTQQPQQPFPQLQQPQQPFPQPQQQLPQPQQPQQSFPQQQRPFIQPSLQQQLNPCKNILLQQSKPASLVSSLWSIIWPQSDCQVMRQQCCQQLAQIPQQLQCAAIHSVVHSIIMQQQQQQQQQQGIDIFLPLSQHEQVGQGSLVQGQGIIQPQQPAQLEAIRSLVLQTLPSMCNVYVPPECSIMRAPFASIVAGIGGQ","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","BOP clade","Pooideae","Triticodae","Triticeae","Triticinae","Triticum"],"alphafold_very_low_content":0.6605504587155964,"dataset":["Condensates-related proteins"],"disorder_content":0.4954128440366973,"disprot_consensus":{"full":[{"start":1,"end":162,"type":"T"},{"start":163,"end":327,"type":"F"}],"Structural state":[{"start":1,"end":162,"type":"D"}],"Structural transition":[{"start":1,"end":162,"type":"T"}],"Molecular function":[{"start":1,"end":327,"type":"F"}]}},{"disprot_id":"DP04149","acc":"P51788","creator":"vnugnes","date":"2024-02-16T15:24:48.427Z","features":{"pfam":[{"id":"PF00654","name":"Voltage gated chloride channel","start":146,"end":546}],"gene3D":[]},"genes":[{"name":{"value":"CLCN2"}}],"length":898,"name":"Chloride channel protein 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":88,"reference_id":"37296152","reference_source":"pmid","reference_html":"Cryo-EM structures of ClC-2 chloride channel reveal the blocking mechanism of its specific inhibitor AK-42. <i> Ma T, Wang L, Chai A, Liu C, Cui W, Yuan S, Wing Ngor Au S, Sun L, Zhang X, Zhang Z, Lu J, Gao Y, Wang P, Li Z, Liang Y, Vogel H, Wang YT, Wang D, Yan K, Zhang H. </i> Nat Commun, 2023","date":"2024-02-16T15:28:15.570Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"7XF5"},{"db":"EMDB","id":"EMD-33169"}],"region_id":"DP04149r001","statement":[{"text":"The refined atomic model contains residue numbers from 89 to 560, fitting well within the density of our TMD map, but lacking the flexible N- and C-terminal regions (Fig. 1b).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-19T14:45:10.254Z"}},{"start":650,"end":753,"reference_id":"37296152","reference_source":"pmid","reference_html":"Cryo-EM structures of ClC-2 chloride channel reveal the blocking mechanism of its specific inhibitor AK-42. <i> Ma T, Wang L, Chai A, Liu C, Cui W, Yuan S, Wing Ngor Au S, Sun L, Zhang X, Zhang Z, Lu J, Gao Y, Wang P, Li Z, Liang Y, Vogel H, Wang YT, Wang D, Yan K, Zhang H. </i> Nat Commun, 2023","date":"2024-02-16T15:30:14.740Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"7XF5"},{"db":"EMDB","id":"EMD-33169"}],"region_id":"DP04149r002","statement":[{"text":"The refined atomic model contains residue numbers from 89 to 560, fitting well within the density of our TMD map, but lacking the flexible N- and C-terminal regions (Fig. 1b).","type":"Results"},{"text":"However, the cytosolic C-terminal domain (CTD) had lower resolution, suggesting that the two tandem-linked CBS domains are quite flexible.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-19T14:45:11.266Z"}},{"start":846,"end":898,"reference_id":"37296152","reference_source":"pmid","reference_html":"Cryo-EM structures of ClC-2 chloride channel reveal the blocking mechanism of its specific inhibitor AK-42. <i> Ma T, Wang L, Chai A, Liu C, Cui W, Yuan S, Wing Ngor Au S, Sun L, Zhang X, Zhang Z, Lu J, Gao Y, Wang P, Li Z, Liang Y, Vogel H, Wang YT, Wang D, Yan K, Zhang H. </i> Nat Commun, 2023","date":"2024-02-16T15:30:45.265Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"7XF5"},{"db":"EMDB","id":"EMD-33169"}],"region_id":"DP04149r003","statement":[{"text":"The refined atomic model contains residue numbers from 89 to 560, fitting well within the density of our TMD map, but lacking the flexible N- and C-terminal regions (Fig. 1b).","type":"Results"},{"text":"However, the cytosolic C-terminal domain (CTD) had lower resolution, suggesting that the two tandem-linked CBS domains are quite flexible.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-19T14:45:13.452Z"}},{"start":561,"end":572,"reference_id":"37296152","reference_source":"pmid","reference_html":"Cryo-EM structures of ClC-2 chloride channel reveal the blocking mechanism of its specific inhibitor AK-42. <i> Ma T, Wang L, Chai A, Liu C, Cui W, Yuan S, Wing Ngor Au S, Sun L, Zhang X, Zhang Z, Lu J, Gao Y, Wang P, Li Z, Liang Y, Vogel H, Wang YT, Wang D, Yan K, Zhang H. </i> Nat Commun, 2023","date":"2024-02-16T15:34:51.134Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"7XF5"},{"db":"EMDB","id":"EMD-33169"}],"region_id":"DP04149r004","statement":[{"text":"The cryo-EM structure of the full length apo protein shows this region lacks electron density, indicating it is disordered. ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-19T14:45:15.298Z"}},{"start":645,"end":743,"reference_id":"38345841","reference_source":"pmid","reference_html":"CryoEM structures of the human CLC-2 voltage-gated chloride channel reveal a ball-and-chain gating mechanism. <i> Xu M, Neelands T, Powers AS, Liu Y, Miller SD, Pintilie GD, Bois JD, Dror RO, Chiu W, Maduke M. </i> Elife, 2024","date":"2024-02-16T15:46:24.637Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"8TA4"},{"db":"PDB","id":"8TA5"},{"db":"EMDB","id":"EMD-41129"},{"db":"EMDB","id":"EMD-41128"}],"region_id":"DP04149r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"}],"statement":[{"text":"In both classes, the CBS domains can be fit to the density; however, residues 645–743 in the CLC-2 CTD are not resolved and thus are omitted from the models and from the Q-score calculation (Pintilie et al., 2020, Figure 4—figure supplement 1).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-19T14:45:17.024Z"}},{"start":14,"end":28,"reference_id":"38345841","reference_source":"pmid","reference_html":"CryoEM structures of the human CLC-2 voltage-gated chloride channel reveal a ball-and-chain gating mechanism. <i> Xu M, Neelands T, Powers AS, Liu Y, Miller SD, Pintilie GD, Bois JD, Dror RO, Chiu W, Maduke M. </i> Elife, 2024","date":"2024-05-06T17:36:49.551Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"8TA4"},{"db":"PDB","id":"8TA5"},{"db":"EMDB","id":"EMD-41129"},{"db":"EMDB","id":"EMD-41128"}],"region_id":"DP04149r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":null}],"statement":[{"text":"The lack of sufficient density for modeling residues 1–87 suggests that the N terminal cytoplasmic region of CLC-2 is intrinsically disordered. However, our observation of a resolvable hairpin density at the intracellular pore, together with the previous hypothesis of N-terminal ball-and-chain gating for CLC-2, prompted us to consider whether the hairpin density corresponds to N-terminal residues. We tested several candidate fragments from the CLC-2 N-terminal region and found that the hairpin density fits perfectly with residues corresponding to 14–28 (Figure 5A). Inspection of the Q-score validation plot for these residues shows they have higher values than the Q-score expected for the corresponding resolution (Figure 5B), which indicates reliable model building at this resolution (Pintilie et al., 2020).","type":"Results"},{"text":"Along with the absence of hairpin density, the subunit with the rotated CTD exhibits a difference in the linker connecting TM helices J and K, which is poorly resolved and insufficient for model building. In contrast, the subunits with the hairpin density contain reliable density in the JK-linker region, allowing confident modeling of an alpha helix (‘JK-helix’, Figure 5A). This observation suggests that the JK-helix stabilizes the N-terminal hairpin peptide. Indeed, residues on the JK-helix interact directly with residues at the peptide’s hairpin turn (Figure 5C). Interactions with other regions in the TM domain (near helices C, D, J, and R) appear to further stabilize the hairpin in its binding site. In addition, the negative surface potential of the hairpin likely contributes to its interaction with the positive TM domain (Figure 5—figure supplement 3; Video 5).","type":"Results"}],"ec_go":"IDA","term_comment":"","term_def":"\"Binding to a domain within the same polypeptide.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":14,"end":27,"reference_id":"38345841","reference_source":"pmid","reference_html":"CryoEM structures of the human CLC-2 voltage-gated chloride channel reveal a ball-and-chain gating mechanism. <i> Xu M, Neelands T, Powers AS, Liu Y, Miller SD, Pintilie GD, Bois JD, Dror RO, Chiu W, Maduke M. </i> Elife, 2024","date":"2024-02-16T16:30:22.972Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000059","term_name":"self-inhibition","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ala14Thr27del","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"In the N-terminal deletion CLC-2 (Delta-N), residues 14–27 (ALQYEQTLMYGRYT) were removed from full-length (WT) CLC-2."}]}],"region_id":"DP04149r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"}],"statement":[{"text":"The hairpin structure appears to directly block the pore (Figure 5—figure supplement 5). To evaluate the potential functional effect of pore block by the N-terminal hairpin, we performed whole-cell patch-clamp recording on CLC-2, both WT and a deletion mutant lacking the hairpin residues (Delta-N), expressed in CHO cells. Delta-N CLC-2 exhibits currents that display less rectification and faster activation kinetics than WT CLC-2 (Figure 6A, B, Figure 6—figure supplement 1).","type":"Results"},{"text":"First, we demonstrate that the increase in current in hairpin-deleted channels reflects an increase in channel activity rather than an increase in surface expression (Figure 6D, E), consistent with loss of a channel-closing mechanism.","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-19T14:45:34.643Z"}},{"start":14,"end":27,"reference_id":"38345841","reference_source":"pmid","reference_html":"CryoEM structures of the human CLC-2 voltage-gated chloride channel reveal a ball-and-chain gating mechanism. <i> Xu M, Neelands T, Powers AS, Liu Y, Miller SD, Pintilie GD, Bois JD, Dror RO, Chiu W, Maduke M. </i> Elife, 2024","date":"2024-02-16T16:31:13.936Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0017081","term_name":"chloride channel regulator activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ala14Thr27del","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"In the N-terminal deletion CLC-2 (Delta-N), residues 14–27 (ALQYEQTLMYGRYT) were removed from full-length (WT) CLC-2."}]}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P51788","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04149r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"}],"statement":[{"text":"The hairpin structure appears to directly block the pore (Figure 5—figure supplement 5). To evaluate the potential functional effect of pore block by the N-terminal hairpin, we performed whole-cell patch-clamp recording on CLC-2, both WT and a deletion mutant lacking the hairpin residues (Delta-N), expressed in CHO cells. Delta-N CLC-2 exhibits currents that display less rectification and faster activation kinetics than WT CLC-2 (Figure 6A, B, Figure 6—figure supplement 1).","type":"Results"},{"text":"First, we demonstrate that the increase in current in hairpin-deleted channels reflects an increase in channel activity rather than an increase in surface expression (Figure 6D, E), consistent with loss of a channel-closing mechanism.","type":"Discussion"}],"term_comment":"","term_def":"\"Binds to and modulates the activity of a chloride channel.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-19T14:45:45.423Z"}},{"start":14,"end":28,"reference_id":"38345841","reference_source":"pmid","reference_html":"CryoEM structures of the human CLC-2 voltage-gated chloride channel reveal a ball-and-chain gating mechanism. <i> Xu M, Neelands T, Powers AS, Liu Y, Miller SD, Pintilie GD, Bois JD, Dror RO, Chiu W, Maduke M. </i> Elife, 2024","date":"2024-02-16T16:34:05.404Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"8TA5"},{"db":"PDB","id":"8TA4"},{"db":"EMDB","id":"EMD-41128"},{"db":"EMDB","id":"EMD-41129"}],"region_id":"DP04149r009","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"}],"statement":[{"text":"The lack of sufficient density for modeling residues 1–87 suggests that the N terminal cytoplasmic region of CLC-2 is intrinsically disordered. However, our observation of a resolvable hairpin density at the intracellular pore, together with the previous hypothesis of N-terminal ball-and-chain gating for CLC-2, prompted us to consider whether the hairpin density corresponds to N-terminal residues. We tested several candidate fragments from the CLC-2 N-terminal region and found that the hairpin density fits perfectly with residues corresponding to 14–28 (Figure 5A). Inspection of the Q-score validation plot for these residues shows they have higher values than the Q-score expected for the corresponding resolution (Figure 5B), which indicates reliable model building at this resolution (Pintilie et al., 2020).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-19T14:45:20.803Z"}},{"start":409,"end":418,"reference_id":"38345841","reference_source":"pmid","reference_html":"CryoEM structures of the human CLC-2 voltage-gated chloride channel reveal a ball-and-chain gating mechanism. <i> Xu M, Neelands T, Powers AS, Liu Y, Miller SD, Pintilie GD, Bois JD, Dror RO, Chiu W, Maduke M. </i> Elife, 2024","date":"2024-02-16T16:45:40.101Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"8TA5"},{"db":"PDB","id":"8TA4"},{"db":"EMDB","id":"EMD-41128"},{"db":"EMDB","id":"EMD-41129"}],"region_id":"DP04149r010","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"}],"statement":[{"text":"The cryo-EM structures of CLC-2 chloride channel transmembrane domain with octh symmetric and asymmetric C-terminal regions show this region is disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-19T14:45:23.463Z"}},{"start":14,"end":28,"reference_id":"38345841","reference_source":"pmid","reference_html":"CryoEM structures of the human CLC-2 voltage-gated chloride channel reveal a ball-and-chain gating mechanism. <i> Xu M, Neelands T, Powers AS, Liu Y, Miller SD, Pintilie GD, Bois JD, Dror RO, Chiu W, Maduke M. </i> Elife, 2024","date":"2024-02-16T16:53:07.144Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0007759","ec_ontology":"ECO","ec_name":"curator inference from database used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"8TA5"},{"db":"PDB","id":"8TA4"},{"db":"EMDB","id":"EMD-41128"},{"db":"EMDB","id":"EMD-41129"},{"db":"PDB","id":"7XF5"},{"db":"EMDB","id":"EMD-33169"}],"region_id":"DP04149r011","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":"chloride"}],"statement":[{"text":"The lack of sufficient density for modeling residues 1–87 suggests that the N terminal cytoplasmic region of CLC-2 is intrinsically disordered. However, our observation of a resolvable hairpin density at the intracellular pore, together with the previous hypothesis of N-terminal ball-and-chain gating for CLC-2, prompted us to consider whether the hairpin density corresponds to N-terminal residues. We tested several candidate fragments from the CLC-2 N-terminal region and found that the hairpin density fits perfectly with residues corresponding to 14–28 (Figure 5A). Inspection of the Q-score validation plot for these residues shows they have higher values than the Q-score expected for the corresponding resolution (Figure 5B), which indicates reliable model building at this resolution (Pintilie et al., 2020).","type":"Results"},{"text":"The cryo-EM structure of the Full length human CLC-2 channel in apo state (PDB 7XF5, pmid:37296152) shows the 1-88 region is fully disordered when there are no Chloride ion present in the sample. However structures obtained with Chloride show this region gains electron density by self associating in a hairpin and interacting with the TM domain of the protein.","type":"Curator statement"}],"states_connection":[{"source":"DP04149r001","target":"DP04149r009"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-19T14:45:28.737Z"}}],"regions_counter":11,"released":"2024_06","sequence":"MAAAAAEEGMEPRALQYEQTLMYGRYTQDLGAFAKEEAARIRLGGPEPWKGPPSSRAAPELLEYGRSRCARCRVCSVRCHKFLVSRVGEDWIFLVLLGLLMALVSWVMDYAIAACLQAQQWMSRGLNTSILLQYLAWVTYPVVLITFSAGFTQILAPQAVGSGIPEMKTILRGVVLKEYLTLKTFIAKVIGLTCALGSGMPLGKEGPFVHIASMCAALLSKFLSLFGGIYENESRNTEMLAAACAVGVGCCFAAPIGGVLFSIEVTSTFFAVRNYWRGFFAATFSAFIFRVLAVWNRDEETITALFKTRFRLDFPFDLQELPAFAVIGIASGFGGALFVYLNRKIVQVMRKQKTINRFLMRKRLLFPALVTLLISTLTFPPGFGQFMAGQLSQKETLVTLFDNRTWVRQGLVEELEPPSTSQAWNPPRANVFLTLVIFILMKFWMSALATTIPVPCGAFMPVFVIGAAFGRLVGESMAAWFPDGIHTDSSTYRIVPGGYAVVGAAALAGAVTHTVSTAVIVFELTGQIAHILPVMIAVILANAVAQSLQPSLYDSIIRIKKLPYLPELGWGRHQQYRVRVEDIMVRDVPHVALSCTFRDLRLALHRTKGRMLALVESPESMILLGSIERSQVVALLGAQLSPARRRQHMQERRATQTSPLSDQEGPPTPEASVCFQVNTEDSAFPAARGETHKPLKPALKRGPSVTRNLGESPTGSAESAGIALRSLFCGSPPPEAASEKLESCEKRKLKRVRISLASDADLEGEMSPEEILEWEEQQLDEPVNFSDCKIDPAPFQLVERTSLHKTHTIFSLLGVDHAYVTSIGRLIGIVTLKELRKAIEGSVTAQGVKVRPPLASFRDSATSSSDTETTEVHALWGPHSRHGLPREGSPSDSDDKCQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.24610244988864144,"dataset":["NDDs-related proteins"],"disorder_content":0.3028953229398664,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"D"},{"start":14,"end":28,"type":"T"},{"start":29,"end":88,"type":"D"},{"start":409,"end":418,"type":"D"},{"start":561,"end":572,"type":"D"},{"start":645,"end":753,"type":"D"},{"start":846,"end":898,"type":"D"}],"Structural state":[{"start":1,"end":88,"type":"D"},{"start":409,"end":418,"type":"D"},{"start":561,"end":572,"type":"D"},{"start":645,"end":753,"type":"D"},{"start":846,"end":898,"type":"D"}],"Disorder function":[{"start":14,"end":28,"type":"F"}],"Molecular function":[{"start":14,"end":27,"type":"F"}],"Structural transition":[{"start":14,"end":28,"type":"T"}]}},{"disprot_id":"DP04151","acc":"O49255","creator":"vnugnes","date":"2024-02-22T15:55:32.240Z","features":{"pfam":[{"id":"PF02365","name":"No apical meristem (NAM) protein","start":10,"end":134}],"gene3D":[]},"genes":[{"name":{"value":"NAC029"},"synonyms":[{"value":"ANAC029"},{"value":"NAC29"},{"value":"NAP"}],"orfNames":[{"value":"F10D13.14"}],"olnNames":[{"value":"At1g69490"}]}],"length":268,"name":"NAC transcription factor 29","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":162,"end":268,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2024-02-22T15:56:48.230Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04151r001","statement":[{"text":"Although the relative migration pattern of the recombinant proteins by SDS/PAGE was in accordance with their relative molecular mass values [NAP (162–268): 15.0 kDa; ANAC019 (163–317): 17.2 kDa; ANAC046 (172–338): 18.2 kDa; histidine–NTL8 (156–335): 20.3 kDa; histidine–SOG (210–449): 29.0 kDa; ANAC013 (161–498): 37.5 kDa], they displayed slow migration during SDS/PAGE compared with standard globular proteins, which is in accordance with their ID nature and previous analysis of two NAC TRDs [39].","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T09:39:11.974Z"}},{"start":162,"end":268,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2024-02-22T16:17:57.609Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04151r002","statement":[{"text":"This aspect was analysed by size-exclusion chromatography for the four untagged NAC TRDs. The hydrodynamic radii (Stokes radii) of ANAC046 (172–338), NAP (162–268) and ANAC019 (163–317) corresponded to pre-molten globule states, whereasANAC013 (161–498) had a more compact structure consistent with its disorder profile (Figures 1d and 3).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T09:39:14.419Z"}},{"start":162,"end":268,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2024-02-22T16:27:07.509Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04151r003","statement":[{"text":"Although the spectra of the six recombinant proteins showed different characteristics, they all had a minimum around 200 nm and only slightly negative ellipticities at 222 nm (Figure 4a). Both the [θ]222 and [θ]200 values suggested that histidine–NTL8 (156–335), ANAC013 (161–498), NAP (162–268) and ANAC019 (163–317) are similar, populating pre-molten globule like ensembles, whereas the values for histidine–SOG1 (210–449) and ANAC046 (172–338) suggest more random coil-like ensembles.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T09:39:17.733Z"}},{"start":206,"end":226,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2024-02-22T16:45:41.153Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140537","term_name":"transcription regulator activator activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006295","ec_ontology":"ECO","ec_name":"beta galactosidase functional complementation evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0693","term_name":"Gal4 DNA-binding domain tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"Coding regions of the three NAC genes were fused to yeast GAL4 DBD (Figures 7a–7c) and analysed for their ability to activate transcription through the ability to promote selective growth of yeast."}]}],"ec_go":"IPI","region_id":"DP04151r004","statement":[{"text":"Both full-length NAP and its TRD, NAP (163–268), activated\ntranscription in yeast.","type":"Results"},{"text":"This revealed that the ability to activate transcription was retained until the region with the MEME motif was removed, after which no activity was detected. Similar results were obtained from the same C-terminal truncations of full-length NAP, supporting the importance of the MEME motif region for transcriptional activation activity.","type":"Results"}],"term_comment":"Usage guidance: transcription regulator activators bind to a transcription regulator to allow it to reach the chromatin or to contact other transcriptional regulators. This activity does not occur at the promoter. For activities that do occur at the promoter, consider GO:0001216 ; DNA-binding transcription activator activity or GO:0003713; transcription coactivator activity; those activities respectively bind DNA themselves or positively regulate a transcription regulator when it is located at the chromatin.","term_def":"\"A molecular function regulator that increases the activity of a transcription regulator via direct binding and/or post-translational modification.\" [PMID:9597751]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T14:41:58.696Z"}}],"regions_counter":4,"released":"2024_06","sequence":"MEVTSQSTLPPGFRFHPTDEELIVYYLRNQTMSKPCPVSIIPEVDIYKFDPWQLPEKTEFGENEWYFFSPRERKYPNGVRPNRAAVSGYWKATGTDKAIHSGSSNVGVKKALVFYKGRPPKGIKTDWIMHEYRLHDSRKASTKRNGSMRLDEWVLCRIYKKRGASKLLNEQEGFMDEVLMEDETKVVVNEAERRTEEEIMMMTSMKLPRTCSLAHLLEMDYMGPVSHIDNFSQFDHLHQPDSESSWFGDLQFNQDEILNHHRQAMFKF","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"alphafold_very_low_content":0.35447761194029853,"disorder_content":0.39925373134328357,"disprot_consensus":{"full":[{"start":162,"end":268,"type":"D"}],"Structural state":[{"start":162,"end":268,"type":"D"}],"Molecular function":[{"start":206,"end":226,"type":"F"}]}},{"disprot_id":"DP04152","acc":"Q9C932","creator":"vnugnes","date":"2024-02-22T16:01:30.394Z","features":{"pfam":[{"id":"PF02365","name":"No apical meristem (NAM) protein","start":15,"end":139}],"gene3D":[]},"genes":[{"name":{"value":"NAC019"},"synonyms":[{"value":"ANAC"}],"orfNames":[{"value":"F14G24.16"}],"olnNames":[{"value":"At1g52890"}]}],"length":317,"name":"NAC domain-containing protein 19","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":163,"end":317,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2024-02-22T16:02:20.763Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04152r001","statement":[{"text":"Although the relative migration pattern of the recombinant proteins by SDS/PAGE was in accordance with their relative molecular mass values [NAP (162–268): 15.0 kDa; ANAC019 (163–317): 17.2 kDa; ANAC046 (172–338): 18.2 kDa; histidine–NTL8 (156–335): 20.3 kDa; histidine–SOG (210–449): 29.0 kDa; ANAC013 (161–498): 37.5 kDa], they displayed slow migration during SDS/PAGE compared with standard globular proteins, which is in accordance with their ID nature and previous analysis of two NAC TRDs [39].","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T09:40:02.280Z"}},{"start":163,"end":317,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2024-02-22T16:18:16.614Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04152r002","statement":[{"text":"This aspect was analysed by size-exclusion chromatography for the four untagged NAC TRDs. The hydrodynamic radii (Stokes radii) of ANAC046 (172–338), NAP (162–268) and ANAC019 (163–317) corresponded to pre-molten globule states, whereasANAC013 (161–498) had a more compact structure consistent with its disorder profile (Figures 1d and 3).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T09:40:04.000Z"}},{"start":163,"end":317,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2024-02-22T16:27:26.559Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04152r003","statement":[{"text":"Although the spectra of the six recombinant proteins showed different characteristics, they all had a minimum around 200 nm and only slightly negative ellipticities at 222 nm (Figure 4a). Both the [θ]222 and [θ]200 values suggested that histidine–NTL8 (156–335), ANAC013 (161–498), NAP (162–268) and ANAC019 (163–317) are similar, populating pre-molten globule like ensembles, whereas the values for histidine–SOG1 (210–449) and ANAC046 (172–338) suggest more random coil-like ensembles.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T09:40:05.325Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MGIQETDPLTQLSLPPGFRFYPTDEELMVQYLCRKAAGYDFSLQLIAEIDLYKFDPWVLPNKALFGEKEWYFFSPRDRKYPNGSRPNRVAGSGYWKATGTDKIISTEGQRVGIKKALVFYIGKAPKGTKTNWIMHEYRLIEPSRRNGSTKLDDWVLCRIYKKQSSAQKQVYDNGIANAREFSNNGTSSTTSSSSHFEDVLDSFHQEIDNRNFQFSNPNRISSLRPDLTEQKTGFHGLADTSNFDWASFAGNVEHNNSVPELGMSHVVPNLEYNCGYLKTEEEVESSHGFNNSGELAQKGYGVDSFGYSGQVGGFGFM","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"alphafold_very_low_content":0.3911671924290221,"disorder_content":0.4889589905362776,"disprot_consensus":{"full":[{"start":163,"end":317,"type":"D"}],"Structural state":[{"start":163,"end":317,"type":"D"}]}},{"disprot_id":"DP04153","acc":"Q6NQK2","creator":"vnugnes","date":"2024-02-22T16:03:03.388Z","features":{"pfam":[{"id":"PF02365","name":"No apical meristem (NAM) protein","start":59,"end":192}],"gene3D":[]},"genes":[{"name":{"value":"SOG1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"19549833","url":"http://www.ncbi.nlm.nih.gov/pubmed/19549833","alternativeUrl":"https://europepmc.org/abstract/MED/19549833"}}]},"synonyms":[{"value":"NAC008","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15029955","url":"http://www.ncbi.nlm.nih.gov/pubmed/15029955","alternativeUrl":"https://europepmc.org/abstract/MED/15029955"}}]}],"orfNames":[{"value":"F14G11.2","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAG50527.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAG50527.1"}}]},{"value":"F2J7.1","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAG50802.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAG50802.1"}}]}],"olnNames":[{"value":"At1g25580","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT1G25580","url":""}}]}]}],"length":449,"name":"SUPPRESSOR OF GAMMA RESPONSE 1","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":210,"end":449,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2024-02-22T16:04:28.730Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Soluble histidine–SOG1 (210–449) was\npurified on TALON resin using standard protocols (Clontech)."}]}],"region_id":"DP04153r001","statement":[{"text":"Although the relative migration pattern of the recombinant proteins by SDS/PAGE was in accordance with their relative molecular mass values [NAP (162–268): 15.0 kDa; ANAC019 (163–317): 17.2 kDa; ANAC046 (172–338): 18.2 kDa; histidine–NTL8 (156–335): 20.3 kDa; histidine–SOG (210–449): 29.0 kDa; ANAC013 (161–498): 37.5 kDa], they displayed slow migration during SDS/PAGE compared with standard globular proteins, which is in accordance with their ID nature and previous analysis of two NAC TRDs [39].","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T10:44:55.647Z"}},{"start":210,"end":449,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2024-02-22T16:27:46.357Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Soluble histidine–SOG1 (210–449) was\npurified on TALON resin using standard protocols (Clontech)."}]}],"region_id":"DP04153r002","statement":[{"text":"Although the spectra of the six recombinant proteins showed different characteristics, they all had a minimum around 200 nm and only slightly negative ellipticities at 222 nm (Figure 4a). Both the [θ]222 and [θ]200 values suggested that histidine–NTL8 (156–335), ANAC013 (161–498), NAP (162–268) and ANAC019 (163–317) are similar, populating pre-molten globule like ensembles, whereas the values for histidine–SOG1 (210–449) and ANAC046 (172–338) suggest more random coil-like ensembles.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T10:44:57.452Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MAGRSWLIDSNRIATKIMSASASSDPRQVVWKSNPSRHCPKCQHVIDNSDVVDDWPGLPRGVKFDPSDPEIIWHLLAKSGLSGLSSHPFIDEFIPTVNQDDGICYTHPKNLPGVKSDGTVSHFFHKAIKAYSTGTRKRRKIHDDDFGDVRWHKTGRTKPVVLDGVQRGCKKIMVLYGGKAVKTNWVMHQYHLGIEEDEKEGDYVVSKIFYQQPQQLVVKRGDKAEQEVSEDIFAAVTPTADPVTPKLATPEPRNAVRICSDSHIASDYVTPSDYVSAHEVSLAETSEVMCMEDEVQSIQPNHERPSSGPELEHGLENGAKEMLDDKEEQEKDRDNENQGEEDPTWFDSGSQFILNSQQLVEALSLCDDLLGSQDREENTNSGSLKDKQPCIADYAHLGPEDFKRDLEECQKIVLDPSNIELDTPPEFRLSQLEFGSQDSFLAWGTGKTD","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"alphafold_very_low_content":0.41870824053452116,"disorder_content":0.534521158129176,"disprot_consensus":{"full":[{"start":210,"end":449,"type":"D"}],"Structural state":[{"start":210,"end":449,"type":"D"}]}},{"disprot_id":"DP04154","acc":"Q9XIN7","creator":"vnugnes","date":"2024-02-22T16:05:27.193Z","features":{"pfam":[{"id":"PF02365","name":"No apical meristem (NAM) protein","start":16,"end":139}],"gene3D":[]},"genes":[{"name":{"value":"NTL8","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"17158162","url":"http://www.ncbi.nlm.nih.gov/pubmed/17158162","alternativeUrl":"https://europepmc.org/abstract/MED/17158162"}}]},"orfNames":[{"value":"F12K2.12","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAD41999.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD41999.1"}}]}],"olnNames":[{"value":"At2g27300","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT2G27300","url":""}}]}]}],"length":335,"name":"NAC domain-containing protein 40","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":156,"end":335,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2024-02-22T16:14:11.148Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Insoluble histidine–NTL8 (156–335) was dissolved in 20 mM\nTris/HCl, pH 7.5, 4.5 M urea and 0.1% (v/v) Triton X-100\nand centrifuged 10 min at 20000 g before affinity purification."}]}],"region_id":"DP04154r001","statement":[{"text":"Although the relative migration pattern of the recombinant proteins by SDS/PAGE was in accordance with their relative molecular mass values [NAP (162–268): 15.0 kDa; ANAC019 (163–317): 17.2 kDa; ANAC046 (172–338): 18.2 kDa; histidine–NTL8 (156–335): 20.3 kDa; histidine–SOG (210–449): 29.0 kDa; ANAC013 (161–498): 37.5 kDa], they displayed slow migration during SDS/PAGE compared with standard globular proteins, which is in accordance with their ID nature and previous analysis of two NAC TRDs [39].","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T10:45:14.107Z"}},{"start":156,"end":335,"reference_id":"25348421","reference_source":"pmid","reference_html":"Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1. <i> O'Shea C, Kryger M, Stender EG, Kragelund BB, Willemoës M, Skriver K. </i> Biochem J, 2015","date":"2024-02-22T16:28:05.751Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Insoluble histidine–NTL8 (156–335) was dissolved in 20 mM\nTris/HCl, pH 7.5, 4.5 M urea and 0.1% (v/v) Triton X-100\nand centrifuged 10 min at 20000 g before affinity purification."}]}],"region_id":"DP04154r002","statement":[{"text":"Although the spectra of the six recombinant proteins showed different characteristics, they all had a minimum around 200 nm and only slightly negative ellipticities at 222 nm (Figure 4a). Both the [θ]222 and [θ]200 values suggested that histidine–NTL8 (156–335), ANAC013 (161–498), NAP (162–268) and ANAC019 (163–317) are similar, populating pre-molten globule like ensembles, whereas the values for histidine–SOG1 (210–449) and ANAC046 (172–338) suggest more random coil-like ensembles.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T10:45:16.371Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MSKEAEMSIAVSALFPGFRFSPTDVELISYYLRRKIDGDENSVAVIAEVEIYKFEPWDLPEESKLKSENEWFYFCARGRKYPHGSQSRRATQLGYWKATGKERSVKSGNQVVGTKRTLVFHIGRAPRGERTEWIMHEYCIHGAPQDALVVCRLRKNADFRASSTQKMEDGVVQDDGYVGQRGGLEKEDKSYYESEHQIPNGDIAESSNVVEDQADTDDDCYAEILNDDIIKLDEEALKASQAFRPTNPTHQETISSESSSKRSKCGIKKESTETMNCYALFRIKNVAGTDSSWRFPNPFKIKKDDSQRLMKNVLATTVFLAILFSFFWTVLIARN","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"alphafold_very_low_content":0.3492537313432836,"dataset":["Stress response proteins"],"disorder_content":0.5373134328358209,"disprot_consensus":{"full":[{"start":156,"end":335,"type":"D"}],"Structural state":[{"start":156,"end":335,"type":"D"}]}},{"disprot_id":"DP04155","acc":"P28749","creator":"rpancsa","date":"2024-02-23T09:04:44.992Z","features":{"pfam":[{"id":"PF01857","name":"Retinoblastoma-associated protein B domain","start":787,"end":943},{"id":"PF01858","name":"Retinoblastoma-associated protein A domain","start":385,"end":578},{"id":"PF08934","name":"Rb C-terminal domain","start":960,"end":1046},{"id":"PF11934","name":"Domain of unknown function (DUF3452)","start":80,"end":212}],"gene3D":[]},"genes":[{"name":{"value":"RBL1"}}],"length":1068,"name":"Retinoblastoma-like protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":612,"end":687,"reference_id":"34661528","reference_source":"pmid","reference_html":"PP2A/B55α substrate recruitment as defined by the retinoblastoma-related protein p107. <i> Fowle H, Zhao Z, Xu Q, Wasserman JS, Wang X, Adeyemi M, Feiser F, Kurimchak AN, Atar D, McEwan BC, Kettenbach AN, Page R, Peti W, Dunbrack RL, Graña X. </i> Elife, 2021","date":"2024-02-28T21:38:18.338Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":null,"value":283,"statements":[{"type":"Methods","text":"NMR data were recorded at 283 K on a Bruker Neo 600 MHz or 800 MHz (1H Larmor frequency) NMR spectrometer equipped with a HCN TCI active z-gradient cryoprobe."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":6.8,"statements":[{"type":"Methods","text":"NMR measurements of p107612-687 were recorded using either 15N- or 15N,13C-labeled protein at a final concentration of 6 or 200 μM in NMR buffer (20 mM sodium phosphate pH 6.8, 250 or 50 mM NaCl, 0.5 mM TCEP) and 90% H2O/10% D2O."}]}],"cross_refs":[{"db":"BMRB","id":"28091"}],"region_id":"DP04155r001","statement":[{"text":"The 2D [1H,15N] HSQC spectrum of 15N-labeled p107 (residues M612-S687, which include R1, R2, and R3) shows all hallmarks of an intrinsically disordered protein (IDP), with a highly limited proton chemical shift dispersion due to the lack of a hydrogen bond network in secondary structure elements.","type":"Results"}],"construct_alterations":[{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Results","text":"The 2D [1H,15N] HSQC spectrum of 15N-labeled p107 (residues M612-S687, which include R1, R2, and R3) shows all hallmarks of an intrinsically disordered protein (IDP), with a highly limited proton chemical shift dispersion due to the lack of a hydrogen bond network in secondary structure elements."}]}],"sequence_construct":"MPMSPLMHPRVKEVRTDSGSLRRDMQPLSPISVHERYSSPTAGSAKRRLFGEDPPKEMLMDKIITEGTKLKIAPSS","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T07:05:04.349Z"}},{"start":614,"end":624,"reference_id":"34661528","reference_source":"pmid","reference_html":"PP2A/B55α substrate recruitment as defined by the retinoblastoma-related protein p107. <i> Fowle H, Zhao Z, Xu Q, Wasserman JS, Wang X, Adeyemi M, Feiser F, Kurimchak AN, Atar D, McEwan BC, Kettenbach AN, Page R, Peti W, Dunbrack RL, Graña X. </i> Elife, 2021","date":"2024-02-28T21:36:31.853Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":null,"value":283,"statements":[{"type":"Methods","text":"NMR data were recorded at 283 K on a Bruker Neo 600 MHz or 800 MHz (1H Larmor frequency) NMR spectrometer equipped with a HCN TCI active z-gradient cryoprobe."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":6.8,"statements":[{"type":"Methods","text":"NMR measurements of p107612-687 were recorded using either 15N- or 15N,13C-labeled protein at a final concentration of 6 or 200 μM in NMR buffer (20 mM sodium phosphate pH 6.8, 250 or 50 mM NaCl, 0.5 mM TCEP) and 90% H2O/10% D2O."}]}],"cross_refs":[{"db":"BMRB","id":"28091"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P63151","operator":null,"partner_start":1,"partner_end":447}],"region_id":"DP04155r002","statement":[{"text":"An overlay of the 2D [1H,15N] HSQC spectrum of 15N-labeled p107M612-S687 in the presence and absence of purified B55α shows that ~15 peaks have reduced intensity, typical for an IDP:protein interaction (Figure 1E and F). Upon completion of the sequence-specific backbone assignment of p107M612-S687, we identified that cross-peaks corresponding to p107 residues M614-E624 were most significantly broadened upon binding to B55α (Figure 1F).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Results","text":"An overlay of the 2D [1H,15N] HSQC spectrum of 15N-labeled p107M612-S687 in the presence and absence of purified B55α shows that ~15 peaks have reduced intensity, typical for an IDP:protein interaction (Figure 1E and F)."}]}],"sequence_construct":"MPMSPLMHPRVKEVRTDSGSLRRDMQPLSPISVHERYSSPTAGSAKRRLFGEDPPKEMLMDKIITEGTKLKIAPSS","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T07:05:11.305Z"}},{"start":615,"end":630,"reference_id":"34661528","reference_source":"pmid","reference_html":"PP2A/B55α substrate recruitment as defined by the retinoblastoma-related protein p107. <i> Fowle H, Zhao Z, Xu Q, Wasserman JS, Wang X, Adeyemi M, Feiser F, Kurimchak AN, Atar D, McEwan BC, Kettenbach AN, Page R, Peti W, Dunbrack RL, Graña X. </i> Elife, 2021","date":"2024-02-23T09:36:53.490Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P63151","operator":null,"partner_start":1,"partner_end":447}],"region_id":"DP04155r003","statement":[{"text":"To determine the contribution of each conserved region, we generated p107 deletion mutants and performed GST pull-down assays using U-2 OS whole-cell lysates. Figure 1D shows that a mutant lacking residues C-terminal of R2 binds B55α similarly to the full construct, indicating that residues C-terminal to the R2 domain are dispensable for B55α binding. R1 alone can bind B55α, although to a slightly lesser extent than R1/R2 (lane 3), while mutants lacking regions containing R1 do not bind B55α (lanes 6 and 7). Additional experiments highlighted that R1 is the key B55α binding region and that R2 enhances the interaction, but without R1 cannot recruit B55α alone (Figure 1D).","type":"Results"},{"text":"The authors have previously specified on Figure 1 panel C that Region 1 (R1) corresponds to residues 615-630 of p107.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T10:54:06.598Z"}},{"start":615,"end":630,"reference_id":"34661528","reference_source":"pmid","reference_html":"PP2A/B55α substrate recruitment as defined by the retinoblastoma-related protein p107. <i> Fowle H, Zhao Z, Xu Q, Wasserman JS, Wang X, Adeyemi M, Feiser F, Kurimchak AN, Atar D, McEwan BC, Kettenbach AN, Page R, Peti W, Dunbrack RL, Graña X. </i> Elife, 2021","date":"2024-02-28T21:34:24.870Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001247","ec_ontology":"ECO","ec_name":"point mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P63151","operator":null,"partner_start":1,"partner_end":447}],"region_id":"DP04155r004","statement":[{"text":"It has been shown that charged:charged interactions are central for B55α:TAU substrate recruitment. To test if charged:charged interactions are also important for p107 recruitment, we generated p107 R621A and K623A variants (in R1), R633A and R34A variants (in s2), and an R647A variant (in R2) using GST-p107-R1R2. As shown in Figure 1D, positive residues in R1 and R2, but not the connecting s2 ‘linker,’ led to a reduction in binding to B55α. Mutation of the cyclin A binding site in R2 (659KRRL-AAAA and 660RRL-AAA mutations to Ala), which also contains positive residues, also reduced binding (data not shown). Thus, positively charged residues participate in binding to B55α.","type":"Results"},{"text":"The authors have previously specified on Figure 1 panel C that Region 1 (R1) corresponds to residues 615-630 of p107.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"To test if charged:charged interactions are also important for p107 recruitment, we generated p107 R621A and K623A variants (in R1), R633A and R34A variants (in s2), and an R647A variant (in R2) using GST-p107-R1R2."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg621Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test if charged:charged interactions are also important for p107 recruitment, we generated p107 R621A and K623A variants (in R1), R633A and R34A variants (in s2), and an R647A variant (in R2) using GST-p107-R1R2."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys623Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test if charged:charged interactions are also important for p107 recruitment, we generated p107 R621A and K623A variants (in R1), R633A and R34A variants (in s2), and an R647A variant (in R2) using GST-p107-R1R2."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T07:05:19.178Z"}},{"start":647,"end":663,"reference_id":"34661528","reference_source":"pmid","reference_html":"PP2A/B55α substrate recruitment as defined by the retinoblastoma-related protein p107. <i> Fowle H, Zhao Z, Xu Q, Wasserman JS, Wang X, Adeyemi M, Feiser F, Kurimchak AN, Atar D, McEwan BC, Kettenbach AN, Page R, Peti W, Dunbrack RL, Graña X. </i> Elife, 2021","date":"2024-02-28T21:33:01.940Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001247","ec_ontology":"ECO","ec_name":"point mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P63151","operator":null,"partner_start":1,"partner_end":447}],"region_id":"DP04155r005","statement":[{"text":"It has been shown that charged:charged interactions are central for B55α:TAU substrate recruitment. To test if charged:charged interactions are also important for p107 recruitment, we generated p107 R621A and K623A variants (in R1), R633A and R34A variants (in s2), and an R647A variant (in R2) using GST-p107-R1R2. As shown in Figure 1D, positive residues in R1 and R2, but not the connecting s2 ‘linker,’ led to a reduction in binding to B55α. Mutation of the cyclin A binding site in R2 (659KRRL-AAAA and 660RRL-AAA mutations to Ala), which also contains positive residues, also reduced binding (data not shown). Thus, positively charged residues participate in binding to B55α.","type":"Results"},{"text":"The authors have previously specified on Figure 1 panel C that Region 2 (R2) corresponds to residues 647-663 of p107.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"To test if charged:charged interactions are also important for p107 recruitment, we generated p107 R621A and K623A variants (in R1), R633A and R34A variants (in s2), and an R647A variant (in R2) using GST-p107-R1R2."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg633Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test if charged:charged interactions are also important for p107 recruitment, we generated p107 R621A and K623A variants (in R1), R633A and R34A variants (in s2), and an R647A variant (in R2) using GST-p107-R1R2."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg634Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test if charged:charged interactions are also important for p107 recruitment, we generated p107 R621A and K623A variants (in R1), R633A and R34A variants (in s2), and an R647A variant (in R2) using GST-p107-R1R2."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T07:05:24.428Z"}},{"start":647,"end":663,"reference_id":"34661528","reference_source":"pmid","reference_html":"PP2A/B55α substrate recruitment as defined by the retinoblastoma-related protein p107. <i> Fowle H, Zhao Z, Xu Q, Wasserman JS, Wang X, Adeyemi M, Feiser F, Kurimchak AN, Atar D, McEwan BC, Kettenbach AN, Page R, Peti W, Dunbrack RL, Graña X. </i> Elife, 2021","date":"2024-02-23T10:40:13.506Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P63151","operator":null,"partner_start":1,"partner_end":447},{"db":"UniProt","id":"P24941","operator":"and","partner_start":1,"partner_end":298}],"region_id":"DP04155r006","statement":[{"text":"To determine the contribution of each conserved region, we generated p107 deletion mutants and performed GST pull-down assays using U-2 OS whole-cell lysates. Figure 1D shows that a mutant lacking residues C-terminal of R2 binds B55α similarly to the full construct, indicating that residues C-terminal to the R2 domain are dispensable for B55α binding. R1 alone can bind B55α, although to a slightly lesser extent than R1/R2 (lane 3), while mutants lacking regions containing R1 do not bind B55α (lanes 6 and 7). Additional experiments highlighted that R1 is the key B55α binding region and that R2 enhances the interaction, but without R1 cannot recruit B55α alone (Figure 1D). Conversely, binding of p107 to CDK2 (or cyclin A, not shown) strictly depends on the presence of R2 (lanes 2, 4, 5, and 6), which includes an RxL motif necessary for cyclin A/CDK2 binding (Adams et al., 1996; Chen et al., 1996).","type":"Results"},{"text":"The authors have previously specified on Figure 1 panel C that Region 2 (R2) corresponds to residues 647-663 of p107.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T07:05:26.261Z"}},{"start":647,"end":663,"reference_id":"34661528","reference_source":"pmid","reference_html":"PP2A/B55α substrate recruitment as defined by the retinoblastoma-related protein p107. <i> Fowle H, Zhao Z, Xu Q, Wasserman JS, Wang X, Adeyemi M, Feiser F, Kurimchak AN, Atar D, McEwan BC, Kettenbach AN, Page R, Peti W, Dunbrack RL, Graña X. </i> Elife, 2021","date":"2024-02-28T21:31:40.744Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P63151","operator":null,"partner_start":1,"partner_end":447}],"region_id":"DP04155r007","statement":[{"text":"An overlay of the 2D [1H,15N] HSQC spectrum of 15N-labeled p107M612-S687 in the presence and absence of purified B55α shows that ~15 peaks have reduced intensity, typical for an IDP:protein interaction (Figure 1E and F). Upon completion of the sequence-specific backbone assignment of p107M612-S687, we identified that cross-peaks corresponding to p107 residues M614-E624 were most significantly broadened upon binding to B55α (Figure 1F). Consistent with the mutation data, these residues form the core of R1. Furthermore, residues within the linker region and R2 also showed peak intensity attenuations, consistent with additional weaker interactions in R2 contributing and enhancing the interaction of R1.","type":"Results"},{"text":"The authors have previously specified on Figure 1 panel C that Region 2 (R2) corresponds to residues 647-663 of p107.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Results","text":"An overlay of the 2D [1H,15N] HSQC spectrum of 15N-labeled p107M612-S687 in the presence and absence of purified B55α shows that ~15 peaks have reduced intensity, typical for an IDP:protein interaction (Figure 1E and F)."}]}],"sequence_construct":"MPMSPLMHPRVKEVRTDSGSLRRDMQPLSPISVHERYSSPTAGSAKRRLFGEDPPKEMLMDKIITEGTKLKIAPSS","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T07:05:28.971Z"}},{"start":613,"end":617,"reference_id":"34661528","reference_source":"pmid","reference_html":"PP2A/B55α substrate recruitment as defined by the retinoblastoma-related protein p107. <i> Fowle H, Zhao Z, Xu Q, Wasserman JS, Wang X, Adeyemi M, Feiser F, Kurimchak AN, Atar D, McEwan BC, Kettenbach AN, Page R, Peti W, Dunbrack RL, Graña X. </i> Elife, 2021","date":"2024-02-28T21:28:04.122Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007184","ec_ontology":"ECO","ec_name":"protein mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04155r008","statement":[{"text":"To determine which sites on p107 were dephosphorylated, we generated p107 mutants in which only a single ‘SP’ site can be phosphorylated (i.e., S615A-S640A, S615A-S650A, and S640A-S650A), as well as a triple deletion control (S615A-S640A-S650A) (Figure 3B). To validate phosphorylation/dephosphorylation and determine which sites were targeted by PP2A/B55α, we used mass spectrometry (MS). MS identified pS615 and pS640 in CDK2-phosphorylated p107 and a significant reduction of pS615 and pS640 phosphorylation upon incubation with PP2A/B55α (Figure 3C).","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser640Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To determine which sites on p107 were dephosphorylated, we generated p107 mutants in which only a single ‘SP’ site can be phosphorylated (i.e., S615A-S640A, S615A-S650A, and S640A-S650A), as well as a triple deletion control (S615A-S640A-S650A) (Figure 3B)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser650Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To determine which sites on p107 were dephosphorylated, we generated p107 mutants in which only a single ‘SP’ site can be phosphorylated (i.e., S615A-S640A, S615A-S650A, and S640A-S650A), as well as a triple deletion control (S615A-S640A-S650A) (Figure 3B)."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T07:05:32.028Z"}},{"start":638,"end":642,"reference_id":"34661528","reference_source":"pmid","reference_html":"PP2A/B55α substrate recruitment as defined by the retinoblastoma-related protein p107. <i> Fowle H, Zhao Z, Xu Q, Wasserman JS, Wang X, Adeyemi M, Feiser F, Kurimchak AN, Atar D, McEwan BC, Kettenbach AN, Page R, Peti W, Dunbrack RL, Graña X. </i> Elife, 2021","date":"2024-02-28T21:27:28.280Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007184","ec_ontology":"ECO","ec_name":"protein mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04155r009","statement":[{"text":"To determine which sites on p107 were dephosphorylated, we generated p107 mutants in which only a single ‘SP’ site can be phosphorylated (i.e., S615A-S640A, S615A-S650A, and S640A-S650A), as well as a triple deletion control (S615A-S640A-S650A) (Figure 3B). To validate phosphorylation/dephosphorylation and determine which sites were targeted by PP2A/B55α, we used mass spectrometry (MS). MS identified pS615 and pS640 in CDK2-phosphorylated p107 and a significant reduction of pS615 and pS640 phosphorylation upon incubation with PP2A/B55α (Figure 3C).","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser615Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To determine which sites on p107 were dephosphorylated, we generated p107 mutants in which only a single ‘SP’ site can be phosphorylated (i.e., S615A-S640A, S615A-S650A, and S640A-S650A), as well as a triple deletion control (S615A-S640A-S650A) (Figure 3B)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser650Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To determine which sites on p107 were dephosphorylated, we generated p107 mutants in which only a single ‘SP’ site can be phosphorylated (i.e., S615A-S640A, S615A-S650A, and S640A-S650A), as well as a triple deletion control (S615A-S640A-S650A) (Figure 3B)."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T07:05:34.352Z"}},{"start":615,"end":630,"reference_id":"34661528","reference_source":"pmid","reference_html":"PP2A/B55α substrate recruitment as defined by the retinoblastoma-related protein p107. <i> Fowle H, Zhao Z, Xu Q, Wasserman JS, Wang X, Adeyemi M, Feiser F, Kurimchak AN, Atar D, McEwan BC, Kettenbach AN, Page R, Peti W, Dunbrack RL, Graña X. </i> Elife, 2021","date":"2024-02-23T10:21:53.982Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006309","ec_ontology":"ECO","ec_name":"competitive binding evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P63151","operator":null,"partner_start":1,"partner_end":447}],"region_id":"DP04155r010","statement":[{"text":"To understand which R1 residues are critical for the p107:B55α interaction, we performed binding competition assays. In this assay, we use increasing concentrations of R1 peptide to compete for B55α binding (Figure 5A). This peptide was able to compete with a p107 R1R2 construct.","type":"Results"},{"text":"The authors have previously specified on Figure 1 panel C that Region 1 (R1) corresponds to residues 615-630 of p107.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T07:05:39.527Z"}}],"regions_counter":10,"released":"2024_06","sequence":"MFEDKPHAEGAAVVAAAGEALQALCQELNLDEGSAAEALDDFTAIRGNYSLEGEVTHWLACSLYVACRKSIIPTVGKGIMEGNCVSLTRILRSAKLSLIQFFSKMKKWMDMSNLPQEFRERIERLERNFEVSTVIFKKYEPIFLDIFQNPYEEPPKLPRSRKQRRIPCSVKDLFNFCWTLFVYTKGNFRMIGDDLVNSYHLLLCCLDLIFANAIMCPNRQDLLNPSFKGLPSDFHTADFTASEEPPCIIAVLCELHDGLLVEAKGIKEHYFKPYISKLFDRKILKGECLLDLSSFTDNSKAVNKEYEEYVLTVGDFDERIFLGADAEEEIGTPRKFTRDTPLGKLTAQANVEYNLQQHFEKKRSFAPSTPLTGRRYLREKEAVITPVASATQSVSRLQSIVAGLKNAPSDQLINIFESCVRNPVENIMKILKGIGETFCQHYTQSTDEQPGSHIDFAVNRLKLAEILYYKILETVMVQETRRLHGMDMSVLLEQDIFHRSLMACCLEIVLFAYSSPRTFPWIIEVLNLQPFYFYKVIEVVIRSEEGLSRDMVKHLNSIEEQILESLAWSHDSALWEALQVSANKVPTCEEVIFPNNFETGNGGNVQGHLPLMPMSPLMHPRVKEVRTDSGSLRRDMQPLSPISVHERYSSPTAGSAKRRLFGEDPPKEMLMDKIITEGTKLKIAPSSSITAENVSILPGQTLLTMATAPVTGTTGHKVTIPLHGVANDAGEITLIPLSMNTNQESKVKSPVSLTAHSLIGASPKQTNLTKAQEVHSTGINRPKRTGSLALFYRKVYHLASVRLRDLCLKLDVSNELRRKIWTCFEFTLVHCPDLMKDRHLDQLLLCAFYIMAKVTKEERTFQEIMKSYRNQPQANSHVYRSVLLKSIPREVVAYNKNINDDFEMIDCDLEDATKTPDCSSGPVKEERGDLIKFYNTIYVGRVKSFALKYDLANQDHMMDAPPLSPFPHIKQQPGSPRRISQQHSIYISPHKNGSGLTPRSALLYKFNGSPSKSLKDINNMIRQGEQRTKKRVIAIDSDAESPAKRVCQENDDVLLKRLQDVVSERANH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.2406367041198502,"disorder_content":0.07116104868913857,"disprot_consensus":{"full":[{"start":612,"end":687,"type":"D"}],"Structural state":[{"start":612,"end":687,"type":"D"}],"Molecular function":[{"start":614,"end":630,"type":"F"},{"start":647,"end":663,"type":"F"}],"Disorder function":[{"start":613,"end":617,"type":"F"},{"start":638,"end":642,"type":"F"}]}},{"disprot_id":"DP04156","acc":"Q96B97","creator":"rpancsa","date":"2024-02-23T12:14:12.042Z","features":{"pfam":[{"id":"PF14604","name":"Variant SH3 domain","start":8,"end":53},{"id":"PF14604","name":"Variant SH3 domain","start":106,"end":153},{"id":"PF14604","name":"Variant SH3 domain","start":274,"end":324}],"gene3D":[]},"genes":[{"name":{"value":"SH3KBP1"},"synonyms":[{"value":"CIN85"}]}],"length":665,"name":"SH3 domain-containing kinase-binding protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":163,"end":263,"reference_id":"38111344","reference_source":"pmid","reference_html":"Autoinhibition in the Signal Transducer CIN85 Modulates B Cell Activation. <i> Sieme D, Engelke M, Rezaei-Ghaleh N, Becker S, Wienands J, Griesinger C. </i> J Am Chem Soc, 2024","date":"2024-02-23T12:26:04.290Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":6,"statements":[{"type":"Supplementary material","text":"The buffer\ncondition for the samples used for the backbone resonance assignment was as follows: 20 mM\nMES pH 6.0, 100 mM NaCl, 1.0 mM TCEP, 0.5 mM DSS, 5 vol% D2O, 0.5 mM EDTA and\n0.01% NaN3."}]}],"cross_refs":[{"db":"BMRB","id":"52081"}],"region_id":"DP04156r001","statement":[{"text":"We accomplished the near-complete assignment of the linker region containing CIN85-PRM1 by acquiring three-dimensional 13C-detected experiments on a shorter construct of the CIN85 protein (CIN85163–333; see Figure S6 for the different protein constructs used in this work and the spectral quality in Figure S7).","type":"Results"},{"text":"Within the disordered linker region (residues 163–263), we were successful in assigning 97% the backbone resonances, including the prolines inside CIN85-PRM1.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T10:48:53.213Z"}},{"start":163,"end":263,"reference_id":"38111344","reference_source":"pmid","reference_html":"Autoinhibition in the Signal Transducer CIN85 Modulates B Cell Activation. <i> Sieme D, Engelke M, Rezaei-Ghaleh N, Becker S, Wienands J, Griesinger C. </i> J Am Chem Soc, 2024","date":"2024-02-23T12:28:40.763Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":6,"statements":[{"type":"Supplementary material","text":"The buffer\ncondition for the samples used for the backbone resonance assignment was as follows: 20 mM\nMES pH 6.0, 100 mM NaCl, 1.0 mM TCEP, 0.5 mM DSS, 5 vol% D2O, 0.5 mM EDTA and\n0.01% NaN3."}]}],"cross_refs":[{"db":"BMRB","id":"52081"}],"region_id":"DP04156r002","statement":[{"text":"We accomplished the near-complete assignment of the linker region containing CIN85-PRM1 by acquiring three-dimensional 13C-detected experiments on a shorter construct of the CIN85 protein (CIN85163–333; see Figure S6 for the different protein constructs used in this work and the spectral quality in Figure S7).","type":"Results"},{"text":"Within the disordered linker region (residues 163–263), we were successful in assigning 97% the backbone resonances, including the prolines inside CIN85-PRM1.","type":"Results"},{"text":"The linker connects the 2nd and 3rd SH3 domains of SH3KBP1/CIN85. In the studied construct only the linker and the 3rd SH3 domain was included.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T10:49:09.793Z"}},{"start":219,"end":232,"reference_id":"38111344","reference_source":"pmid","reference_html":"Autoinhibition in the Signal Transducer CIN85 Modulates B Cell Activation. <i> Sieme D, Engelke M, Rezaei-Ghaleh N, Becker S, Wienands J, Griesinger C. </i> J Am Chem Soc, 2024","date":"2024-02-23T12:35:59.921Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7.2,"statements":[{"type":"Supplementary material","text":"The lyophilized peptides were dissolved in 20mmol HEPES, 100mM NaCl and the pH was again adjusted to 7.2. Standard 1H-15N HSQC experiments (Bruker pulse sequence hsqcetf3gpsi2) were\ncollected at every titration point and the peptide was added successively to the sample, ensuring sufficient mixing before acquiring each experiment. "}]}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q96B97","operator":null,"partner_start":264,"partner_end":333}],"region_id":"DP04156r003","statement":[{"text":"We further used NMR titrations to assess the interaction of CIN85-PRM1 with isolated SH3 domains of CIN85, observing chemical shift perturbations (CSP) in the 15N-labeled SH3 domains upon titration with a synthetic 14-residue peptide of the sequence 219FKDKPIKLRPRSIE232 (see Figure S2). All three domains displayed moderate to weak affinity, with SH3C showing 3- and 5-fold lower dissociation constants (KD) than SH3A and SH3B, respectively (KD ∼ 0.2–1.1 mM; see Table 1). This suggested the SH3C domain to be the dominant interaction partner to CIN85-PRM1.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T10:49:11.514Z"}},{"start":219,"end":232,"reference_id":"38111344","reference_source":"pmid","reference_html":"Autoinhibition in the Signal Transducer CIN85 Modulates B Cell Activation. <i> Sieme D, Engelke M, Rezaei-Ghaleh N, Becker S, Wienands J, Griesinger C. </i> J Am Chem Soc, 2024","date":"2024-02-29T07:20:55.315Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":1,"region_id":"DP04156r004","statement":[{"text":"Additionally, the secondary structure propensities (SSP) were predicted from the assigned chemical shifts using the ncSPC webserver37 and showed a distinct propensity for helical structures within CIN85-PRM1 (Figure ​Figure33B). Torsion angles predicted using TALOS-N38 were consistent with a 310 helix formed by I224, K225, and L226. This was lost upon introduction of the R/A mutations (Figure ​Figure33B). We assigned the resonances of the free peptide in order to determine whether the helical structures within CIN85-PRM1 form upon binding or are already present in the free peptide but disrupted by the R/A mutations (Figures S8 and S9). We found no significant propensity for helix in the free peptide and the helical structure thus likely forms through a disorder-to-order transition upon binding to SH3C.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-07T14:43:33.456Z"}},{"start":228,"end":232,"reference_id":"38111344","reference_source":"pmid","reference_html":"Autoinhibition in the Signal Transducer CIN85 Modulates B Cell Activation. <i> Sieme D, Engelke M, Rezaei-Ghaleh N, Becker S, Wienands J, Griesinger C. </i> J Am Chem Soc, 2024","date":"2024-02-23T12:46:13.453Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04156r005","statement":[{"text":"The serine residue at position 230 was shown to significantly weaken the CIN85-PRM1:SH3 association in its phosphorylated state (Figure ​Figure22B and Table 1). In addition, it was found to be highly phosphorylated in a multitude of phosphoproteomic studies (Figure S4).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T10:49:12.974Z"}},{"start":219,"end":232,"reference_id":"38111344","reference_source":"pmid","reference_html":"Autoinhibition in the Signal Transducer CIN85 Modulates B Cell Activation. <i> Sieme D, Engelke M, Rezaei-Ghaleh N, Becker S, Wienands J, Griesinger C. </i> J Am Chem Soc, 2024","date":"2024-02-23T12:58:34.544Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000059","term_name":"self-inhibition","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04156r006","statement":[{"text":"The SH3C Domain in CIN851–333 Is Autoinhibited by Binding to CIN85-PRM1 Intramolecularly","type":"Results"},{"text":"The authors have already defined previously that residues 219-232 correspond to PRM1.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T10:49:14.577Z"}}],"regions_counter":6,"released":"2024_06","sequence":"MVEAIVEFDYQAQHDDELTISVGEIITNIRKEDGGWWEGQINGRRGLFPDNFVREIKKEMKKDPLTNKAPEKPLHEVPSGNSLLSSETILRTNKRGERRRRRCQVAFSYLPQNDDELELKVGDIIEVVGEVEEGWWEGVLNGKTGMFPSNFIKELSGESDELGISQDEQLSKSSLRETTGSESDGGDSSSTKSEGANGTVATAAIQPKKVKGVGFGDIFKDKPIKLRPRSIEVENDFLPVEKTIGKKLPATTATPDSSKTEMDSRTKSKDYCKVIFPYEAQNDDELTIKEGDIVTLINKDCIDVGWWEGELNGRRGVFPDNFVKLLPPDFEKEGNRPKKPPPPSAPVIKQGAGTTERKHEIKKIPPERPEMLPNRTEEKERPEREPKLDLQKPSVPAIPPKKPRPPKTNSLSRPGALPPRRPERPVGPLTHTRGDSPKIDLAGSSLSGILDKDLSDRSNDIDLEGFDSVVSSTEKLSHPTTSRPKATGRRPPSQSLTSSSLSSPDIFDSPSPEEDKEEHISLAHRGVDASKKTSKTVTISQVSDNKASLPPKPGTMAAGGGGPAPLSSAAPSPLSSSLGTAGHRANSPSLFGTEGKPKMEPAASSQAAVEELRTQVRELRSIIETMKDQQKREIKQLLSELDEEKKIRLRLQMEVNDIKKALQSK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.5278195488721804,"dataset":["Condensates-related proteins","Stress response proteins"],"disorder_content":0.1518796992481203,"disprot_consensus":{"full":[{"start":163,"end":218,"type":"D"},{"start":219,"end":232,"type":"T"},{"start":233,"end":263,"type":"D"}],"Structural state":[{"start":163,"end":263,"type":"D"}],"Disorder function":[{"start":163,"end":263,"type":"F"}],"Molecular function":[{"start":219,"end":232,"type":"F"}],"Structural transition":[{"start":219,"end":232,"type":"T"}]}},{"disprot_id":"DP04157","acc":"O00418","creator":"gerdos","date":"2024-02-23T12:48:12.507Z","features":{"pfam":[{"id":"PF02816","name":"Alpha-kinase family","start":139,"end":318}],"gene3D":[]},"genes":[{"name":{"value":"EEF2K"}}],"length":725,"name":"Eukaryotic elongation factor 2 kinase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":562,"end":597,"reference_id":"31108082","reference_source":"pmid","reference_html":"Solution Structure of the Carboxy-Terminal Tandem Repeat Domain of Eukaryotic Elongation Factor 2 Kinase and Its Role in Substrate Recognition. <i> Piserchio A, Will N, Giles DH, Hajredini F, Dalby KN, Ghose R. </i> J Mol Biol, 2019","date":"2024-02-23T13:07:50.701Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04157r001","statement":[{"text":"The region G562-G597 was found to be disordered with an average {1H}−15N NOE value of 0.35 ± 0.08.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T10:51:16.470Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MADEDLIFRLEGVDGGQSPRAGHDGDSDGDSDDEEGYFICPITDDPSSNQNVNSKVNKYYSNLTKSERYSSSGSPANSFHFKEAWKHAIQKAKHMPDPWAEFHLEDIATERATRHRYNAVTGEWLDDEVLIKMASQPFGRGAMRECFRTKKLSNFLHAQQWKGASNYVAKRYIEPVDRDVYFEDVRLQMEAKLWGEEYNRHKPPKQVDIMQMCIIELKDRPGKPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTETGTDFGDGNLGVRGMALFFYSHACNRICESMGLAPFDLSPRERDAVNQNTKLLQSAKTILRGTEEKCGSPQVRTLSGSRPPLLRPLSENSGDENMSDVTFDSLPSSPSSATPHSQKLDHLHWPVFSDLDNMASRDHDHLDNHRESENSGDSGYPSEKRGELDDPEPREHGHSYSNRKYESDEDSLGSSGRVCVEKWNLLNSSRLHLPRASAVALEVQRLNALDLEKKIGKSILGKVHLAMVRYHEGGRFCEKGEEWDQESAVFHLEHAANLGELEAIVGLGLMYSQLPHHILADVSLKETEENKTKGFDYLLKAAEAGDRQSMILVARAFDSGQNLSPDRCQDWLEALHWYNTALEMTDCDEGGEYDGMQDEPRYMMLAREAEMLFTGGYGLEKDPQRSGDLYTQAAEAAMEAMKGRLANQYYQKAEEAWAQMEE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.27448275862068966,"dataset":["Autophagy-related proteins","Stress response proteins"],"disorder_content":0.0496551724137931,"disprot_consensus":{"full":[{"start":562,"end":597,"type":"D"}],"Structural state":[{"start":562,"end":597,"type":"D"}]}},{"disprot_id":"DP04158","acc":"Q9BX66","creator":"rpancsa","date":"2024-02-23T14:55:17.924Z","features":{"pfam":[{"id":"PF00018","name":"SH3 domain","start":873,"end":919},{"id":"PF02208","name":"Sorbin homologous domain","start":370,"end":411},{"id":"PF07653","name":"Variant SH3 domain","start":798,"end":849},{"id":"PF14604","name":"Variant SH3 domain","start":1238,"end":1288}],"gene3D":[]},"genes":[{"name":{"value":"SORBS1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:14565","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:14565"}}]},"synonyms":[{"value":"KIAA0894"},{"value":"KIAA1296"},{"value":"SH3D5"}]}],"length":1292,"name":"Sorbin and SH3 domain-containing protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":851,"end":867,"reference_id":"24878663","reference_source":"pmid","reference_html":"Structural investigation of the interaction between the tandem SH3 domains of c-Cbl-associated protein and vinculin. <i> Zhao D, Wang X, Peng J, Wang C, Li F, Sun Q, Zhang Y, Zhang J, Cai G, Zuo X, Wu J, Shi Y, Zhang Z, Gong Q. </i> J Struct Biol, 2014","date":"2024-02-23T15:05:12.232Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04158r001","statement":[{"text":"Our results showed that, in the free state, the residues of the\nSH3a and SH3b domains exhibit quite uniform NOEs with an aver-\nage of 0.70, whereas the residues of the linker region display much\nlower (even negative) NOE values (Fig. 6D). Upon binding with\nvin857, the residues in the linker region show no obvious change\nin their NOE values, indicating that the 20-residue linker of the\ntandem SH3 domains is still highly flexible even after binding with\nvin857 and may not participate in the interaction of the SH3\ndomains with vin 857.","type":"Results"},{"text":"The plot of NOE values and Figure 4A indicates that the flexible linker is between residues 851-867.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T10:51:26.230Z"}},{"start":851,"end":867,"reference_id":"24878663","reference_source":"pmid","reference_html":"Structural investigation of the interaction between the tandem SH3 domains of c-Cbl-associated protein and vinculin. <i> Zhao D, Wang X, Peng J, Wang C, Li F, Sun Q, Zhang Y, Zhang J, Cai G, Zuo X, Wu J, Shi Y, Zhang Z, Gong Q. </i> J Struct Biol, 2014","date":"2024-02-23T15:05:36.168Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04158r002","statement":[{"text":"Our results showed that, in the free state, the residues of the\nSH3a and SH3b domains exhibit quite uniform NOEs with an aver-\nage of 0.70, whereas the residues of the linker region display much\nlower (even negative) NOE values (Fig. 6D). Upon binding with\nvin857, the residues in the linker region show no obvious change\nin their NOE values, indicating that the 20-residue linker of the\ntandem SH3 domains is still highly flexible even after binding with\nvin857 and may not participate in the interaction of the SH3\ndomains with vin 857.","type":"Results"},{"text":"The plot of NOE values and Figure 4A indicates that the flexible linker is between residues 851-867.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T10:51:31.445Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MSSECDGGSKAVMNGLAPGSNGQDKATADPLRARSISAVKIIPVKTVKNASGLVLPTDMDLTKICTGKGAVTLRASSSYRETPSSSPASPQETRQHESKPGLEPEPSSADEWRLSSSADANGNAQPSSLAAKGYRSVHPNLPSDKSQDATSSSAAQPEVIVVPLYLVNTDRGQEGTARPPTPLGPLGCVPTIPATASAASPLTFPTLDDFIPPHLQRWPHHSQPARASGSFAPISQTPPSFSPPPPLVPPAPEDLRRVSEPDLTGAVSSTDSSPLLNEVSSSLIGTDSQAFPSVSKPSSAYPSTTIVNPTIVLLQHNREQQKRLSSLSDPVSERRVGEQDSAPTQEKPTSPGKAIEKRAKDDSRRVVKSTQDLSDVSMDEVGIPLRNTERSKDWYKTMFKQIHKLNRDTPEENPYFPTYKFPELPEIQQTSEEDNPYTPTYQFPASTPSPKSEDDDSDLYSPRYSFSEDTKSPLSVPRSKSEMSYIDGEKVVKRSATLPLPARSSSLKSSSERNDWEPPDKKVDTRKYRAEPKSIYEYQPGKSSVLTNEKMSRDISPEEIDLKNEPWYKFFSELEFGKPPPKKIWDYTPGDCSILPREDRKTNLDKDLSLCQTELEADLEKMETLNKAPSANVPQSSAISPTPEISSETPGYIYSSNFHAVKRESDGAPGDLTSLENERQIYKSVLEGGDIPLQGLSGLKRPSSSASTKDSESPRHFIPADYLESTEEFIRRRHDDKEKLLADQRRLKREQEEADIAARRHTGVIPTHHQFITNERFGDLLNIDDTAKRKSGSEMRPARAKFDFKAQTLKELPLQKGDIVYIYKQIDQNWYEGEHHGRVGIFPRTYIELLPPAEKAQPKKLTPVQVLEYGEAIAKFNFNGDTQVEMSFRKGERITLLRQVDENWYEGRIPGTSRQGIFPITYVDVIKRPLVKNPVDYMDLPFSSSPSRSATASPQFSSHSKLITPAPSSLPHSRRALSPEMHAVTSEWISLTVGVPGRRSLALTPPLPPLPEASIYNTDHLALSPRASPSLSLSLPHLSWSDRPTPRSVASPLALPSPHKTYSLAPTSQASLHMNGDGGVHTPSSGIHQDSFLQLPLGSSDSVISQLSDAFSSQSKRQPWREESGQYERKAERGAGERGPGGPKISKKSCLKPSDVVRCLSTEQRLSDLNTPEESRPGKPLGSAFPGSEAEQTERHRGGEQAGRKAARRGGSQQPQAQQRRVTPDRSQTSQDLFSYQALYSYIPQNDDELELRDGDIVDVMEKCDDGWFVGTSRRTKQFGTFPGNYVKPLYL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.739938080495356,"disorder_content":0.013157894736842105,"disprot_consensus":{"full":[{"start":851,"end":867,"type":"D"}],"Structural state":[{"start":851,"end":867,"type":"D"}],"Disorder function":[{"start":851,"end":867,"type":"F"}]}},{"disprot_id":"DP04159","acc":"A0A0H2ZJC1","creator":"rpancsa","date":"2024-02-23T15:13:21.954Z","features":{"pfam":[{"id":"PF20661","name":"SutA RNAP-binding domain","start":59,"end":92}],"gene3D":[]},"genes":[{"name":{"value":"sutA","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"26787849","url":"http://www.ncbi.nlm.nih.gov/pubmed/26787849","alternativeUrl":"https://europepmc.org/abstract/MED/26787849"}}]},"olnNames":[{"value":"PA14_69770","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"ABJ14670.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABJ14670.1"}}]}]}],"length":105,"name":"Transcriptional regulator SutA","ncbi_taxon_id":208963,"organism":"Pseudomonas aeruginosa (strain UCBPP-PA14)","regions":[{"start":1,"end":55,"reference_id":"31254296","reference_source":"pmid","reference_html":"The dormancy-specific regulator, SutA, is intrinsically disordered and modulates transcription initiation in Pseudomonas aeruginosa. <i> Bergkessel M, Babin BM, VanderVelde D, Sweredoski MJ, Moradian A, Eggleston-Rangel R, Hess S, Tirrell DA, Artsimovitch I, Newman DK. </i> Mol Microbiol, 2019","date":"2024-02-23T15:21:45.169Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":7,"statements":[{"type":"Methods","text":"For the full-length protein, 15N HSQC, 13C HSQC, HNCACB, and CBCACONH spectra were acquired at 7 °C on a Bruker AV III 700 MHz spectrometer with a TCI cryoprobe running Topspin 3.2, but 15N HSQC experiments modified for measurement of T2 and of 15N-1H NOE were collected on the Varian Inova 600 MHz NMR, as were 15N HSQC spectra for the SutA ΔN and SutA ΔC SutA proteins."}]}],"region_id":"DP04159r001","statement":[{"text":"However, for SutA, the results of these analyses lend credence to the bioinformatics predictions and suggest that much of the protein outside a central α-helix is disordered. Residues 56–76 show the positive Cα and CO and negative Hα secondary chemical shifts associated with an α-helix structure (Wishart et al., 1991), and also show fast R2 relaxation rates and positive (1H-15N)NOE, suggesting that they are not disordered (Reddy & Rainey, 2010). RDCs for the helix region are also positive, as has been observed for α-helical regions of a partially denatured protein (Mohana-Borges et al., 2004). The short β-strand is less strongly supported, but secondary shifts for those residues are mostly of the appropriate sign for a β-strand (albeit of small magnitudes). In the N-tail, a small number of isolated residues have a positive NOE signal or secondary shifts that are not near zero, but in general, the residues of this region have the low R2, secondary shift, and RDC values that are characteristic of disorder.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T10:51:37.893Z"}},{"start":77,"end":105,"reference_id":"31254296","reference_source":"pmid","reference_html":"The dormancy-specific regulator, SutA, is intrinsically disordered and modulates transcription initiation in Pseudomonas aeruginosa. <i> Bergkessel M, Babin BM, VanderVelde D, Sweredoski MJ, Moradian A, Eggleston-Rangel R, Hess S, Tirrell DA, Artsimovitch I, Newman DK. </i> Mol Microbiol, 2019","date":"2024-02-23T15:23:19.791Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":7,"statements":[{"type":"Methods","text":"For the full-length protein, 15N HSQC, 13C HSQC, HNCACB, and CBCACONH spectra were acquired at 7 °C on a Bruker AV III 700 MHz spectrometer with a TCI cryoprobe running Topspin 3.2, but 15N HSQC experiments modified for measurement of T2 and of 15N-1H NOE were collected on the Varian Inova 600 MHz NMR, as were 15N HSQC spectra for the SutA ΔN and SutA ΔC SutA proteins."}]}],"region_id":"DP04159r002","statement":[{"text":"However, for SutA, the results of these analyses lend credence to the bioinformatics predictions and suggest that much of the protein outside a central α-helix is disordered. Residues 56–76 show the positive Cα and CO and negative Hα secondary chemical shifts associated with an α-helix structure (Wishart et al., 1991), and also show fast R2 relaxation rates and positive (1H-15N)NOE, suggesting that they are not disordered (Reddy & Rainey, 2010). RDCs for the helix region are also positive, as has been observed for α-helical regions of a partially denatured protein (Mohana-Borges et al., 2004). The short β-strand is less strongly supported, but secondary shifts for those residues are mostly of the appropriate sign for a β-strand (albeit of small magnitudes).","type":"Results"},{"text":"The C-tail has several residues that show somewhat higher R2 values and non-zero RDCs, suggestive of some degree of structure, but classic secondary structure elements are not apparent.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T10:51:38.893Z"}},{"start":77,"end":105,"reference_id":"31254296","reference_source":"pmid","reference_html":"The dormancy-specific regulator, SutA, is intrinsically disordered and modulates transcription initiation in Pseudomonas aeruginosa. <i> Bergkessel M, Babin BM, VanderVelde D, Sweredoski MJ, Moradian A, Eggleston-Rangel R, Hess S, Tirrell DA, Artsimovitch I, Newman DK. </i> Mol Microbiol, 2019","date":"2024-02-23T15:24:11.968Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":7,"statements":[{"type":"Methods","text":"For the full-length protein, 15N HSQC, 13C HSQC, HNCACB, and CBCACONH spectra were acquired at 7 °C on a Bruker AV III 700 MHz spectrometer with a TCI cryoprobe running Topspin 3.2, but 15N HSQC experiments modified for measurement of T2 and of 15N-1H NOE were collected on the Varian Inova 600 MHz NMR, as were 15N HSQC spectra for the SutA ΔN and SutA ΔC SutA proteins."}]}],"region_id":"DP04159r003","statement":[{"text":"However, for SutA, the results of these analyses lend credence to the bioinformatics predictions and suggest that much of the protein outside a central α-helix is disordered. Residues 56–76 show the positive Cα and CO and negative Hα secondary chemical shifts associated with an α-helix structure (Wishart et al., 1991), and also show fast R2 relaxation rates and positive (1H-15N)NOE, suggesting that they are not disordered (Reddy & Rainey, 2010). RDCs for the helix region are also positive, as has been observed for α-helical regions of a partially denatured protein (Mohana-Borges et al., 2004). The short β-strand is less strongly supported, but secondary shifts for those residues are mostly of the appropriate sign for a β-strand (albeit of small magnitudes).","type":"Results"},{"text":"The C-tail has several residues that show somewhat higher R2 values and non-zero RDCs, suggestive of some degree of structure, but classic secondary structure elements are not apparent.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T10:51:41.487Z"}},{"start":1,"end":55,"reference_id":"31254296","reference_source":"pmid","reference_html":"The dormancy-specific regulator, SutA, is intrinsically disordered and modulates transcription initiation in Pseudomonas aeruginosa. <i> Bergkessel M, Babin BM, VanderVelde D, Sweredoski MJ, Moradian A, Eggleston-Rangel R, Hess S, Tirrell DA, Artsimovitch I, Newman DK. </i> Mol Microbiol, 2019","date":"2024-02-23T15:24:58.688Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":7,"statements":[{"type":"Methods","text":"For the full-length protein, 15N HSQC, 13C HSQC, HNCACB, and CBCACONH spectra were acquired at 7 °C on a Bruker AV III 700 MHz spectrometer with a TCI cryoprobe running Topspin 3.2, but 15N HSQC experiments modified for measurement of T2 and of 15N-1H NOE were collected on the Varian Inova 600 MHz NMR, as were 15N HSQC spectra for the SutA ΔN and SutA ΔC SutA proteins."}]}],"region_id":"DP04159r004","statement":[{"text":"However, for SutA, the results of these analyses lend credence to the bioinformatics predictions and suggest that much of the protein outside a central α-helix is disordered. Residues 56–76 show the positive Cα and CO and negative Hα secondary chemical shifts associated with an α-helix structure (Wishart et al., 1991), and also show fast R2 relaxation rates and positive (1H-15N)NOE, suggesting that they are not disordered (Reddy & Rainey, 2010). RDCs for the helix region are also positive, as has been observed for α-helical regions of a partially denatured protein (Mohana-Borges et al., 2004). The short β-strand is less strongly supported, but secondary shifts for those residues are mostly of the appropriate sign for a β-strand (albeit of small magnitudes). In the N-tail, a small number of isolated residues have a positive NOE signal or secondary shifts that are not near zero, but in general, the residues of this region have the low R2, secondary shift, and RDC values that are characteristic of disorder.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T10:51:44.993Z"}},{"start":95,"end":99,"reference_id":"31254296","reference_source":"pmid","reference_html":"The dormancy-specific regulator, SutA, is intrinsically disordered and modulates transcription initiation in Pseudomonas aeruginosa. <i> Bergkessel M, Babin BM, VanderVelde D, Sweredoski MJ, Moradian A, Eggleston-Rangel R, Hess S, Tirrell DA, Artsimovitch I, Newman DK. </i> Mol Microbiol, 2019","date":"2024-02-23T15:39:42.214Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":25,"statements":[{"type":"Methods","text":"To assess SutA binding to β1 by NMR, 15N-labeled SutA and β1 fragment were mixed together and the resulting complex subjected to size exclusion chromatography, resulting in a final concentration of complex of approximately 25 μM. In addition, 15N-labeled SutA was mixed with σS at 50 μM each, and 13C15N-labeled SutA at 50 μM was measured alone. These 15N HSQC spectra were acquired on a Bruker 800 MHZ AV III HD spectrometer with a TCI cryoprobe at 25 °C."}]}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q51561","operator":null,"partner_start":1,"partner_end":1357}],"region_id":"DP04159r005","statement":[{"text":"We collected 15N HSQC spectra for these mixtures, as well as for SutA alone, using a Bruker 800 MHZ AV III HD spectrometer to help overcome difficulties introduced by the low concentration of β1 domain we could produce. While the peak positions for SutA alone and for the SutA+σS mixture were nearly identical, several SutA residues showed chemical shift perturbations in the β1 mixture, compared with the other two samples (Fig. 2C). Three of these residues, K95, D97 and K99, would be on the same side of an extended peptide chain in the C-tail, suggesting that this tail could directly interact with β1 in an extended conformation.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T10:51:53.280Z"}},{"start":1,"end":55,"reference_id":"31254296","reference_source":"pmid","reference_html":"The dormancy-specific regulator, SutA, is intrinsically disordered and modulates transcription initiation in Pseudomonas aeruginosa. <i> Bergkessel M, Babin BM, VanderVelde D, Sweredoski MJ, Moradian A, Eggleston-Rangel R, Hess S, Tirrell DA, Artsimovitch I, Newman DK. </i> Mol Microbiol, 2019","date":"2024-02-23T15:48:52.263Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0045893","term_name":"positive regulation of transcription, DNA-templated","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001204","ec_ontology":"ECO","ec_name":"in vitro transcription assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","region_id":"DP04159r006","statement":[{"text":"We found that WT SutA increased transcription by both holoenzymes in vitro, but the magnitude of the effect was much larger for EσS (up to 6 times the amount of transcript produced in the absence of SutA) than for Eσ70 (up to 1.7 times) (Fig. 3B and Supporting Information, Fig. S13). In both cases, the effect saturated at concentrations of SutA between 125 and 500 nM, but transcription increased more than 2-fold for EσS even at 31 nM, the lowest concentration tested. The acidic N-tail is strictly required for activation, as the ΔN mutant inhibited transcription in a dose-dependent manner.","type":"Results"}],"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription.\" [GOC:go_curators, GOC:txnOH]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T10:51:51.107Z"}}],"regions_counter":6,"released":"2024_06","sequence":"MSEEELEQDELDGADEDDGEELAAADDGEADSSDGDEAPAPGKKAKAAVVEEELPSVEAKQKERDALAKAMEEFLSRGGKVQEIEPNVVADPPKKPDSKYGSRPI","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Pseudomonadales","Pseudomonadaceae","Pseudomonas"],"alphafold_very_low_content":0.21904761904761905,"dataset":["Stress response proteins"],"disorder_content":0.8,"disprot_consensus":{"full":[{"start":1,"end":55,"type":"D"},{"start":77,"end":105,"type":"D"}],"Structural state":[{"start":1,"end":55,"type":"D"},{"start":77,"end":105,"type":"D"}],"Disorder function":[{"start":1,"end":55,"type":"F"},{"start":77,"end":105,"type":"F"}],"Molecular function":[{"start":95,"end":99,"type":"F"}],"Biological process":[{"start":1,"end":55,"type":"F"}]}},{"disprot_id":"DP04160","acc":"Q0B311","creator":"rpancsa","date":"2024-02-23T16:41:50.185Z","features":{"pfam":[{"id":"PF00550","name":"Phosphopantetheine attachment site","start":229,"end":291}],"gene3D":[]},"genes":[{"olnNames":[{"value":"Bamb_5917","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ABI91462.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABI91462.1"}}]}]}],"length":315,"name":"Phosphopantetheine-binding protein","ncbi_taxon_id":339670,"organism":"Burkholderia ambifaria (strain ATCC BAA-244 / AMMD)","regions":[{"start":296,"end":315,"reference_id":"31548674","reference_source":"pmid","reference_html":"Structural basis for chain release from the enacyloxin polyketide synthase. <i> Kosol S, Gallo A, Griffiths D, Valentic TR, Masschelein J, Jenner M, de Los Santos ELC, Manzi L, Sydor PK, Rea D, Zhou S, Fülöp V, Oldham NJ, Tsai SC, Challis GL, Lewandowski JR. </i> Nat Chem, 2019","date":"2024-02-23T16:49:21.537Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":null,"value":288,"statements":[{"type":"Supplementary material","text":"All solution NMR experiments used for resonance assignments of the apo- and holo-Bamb_5917 PCP\ndomain and for structure calculations of the apo-Bamb_5917 PCP domain were recorded on Bruker\nAVANCE II 700 spectrometer, equipped with a TCI cryoprobe, on 0.6 mM 13C,15N–labelled or 15N–\nlabelled samples in 50 mM phosphate buffer, pH 7.4, containing 10% (v/v) D2O, 150 mM NaCl and\nDSS (for internal referencing) at 288 K."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7.4}],"cross_refs":[{"db":"PDB","id":"5MTI"},{"db":"BMRB","id":"34085"}],"region_id":"DP04160r001","statement":[{"text":"The disordered termini of the PCP domain are highly mobile on the fast ps-ns timescale as indicated by low heteronuclear nuclear Overhauser effects (NOEs), transverse relaxation rates (R2), and high longitudinal relaxation rates (R1) for these regions compared to the structured core (Fig. 1d and Supplementary Fig. 13). The overall rotational diffusion13 is consistent with a monomeric state, with a compact folded core and disordered termini (Supplementary Materials and Methods). The dynamic, disordered nature of the terminal regions is further confirmed by the low predicted S2 parameters (Fig. 1d and Supplementary Fig. 14; S2 of 1 and 0 indicate complete rigidity and unrestricted motion, respectively), typical chemical shift values for a random coil and a lack of long-range NOEs.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T10:52:40.363Z"}},{"start":296,"end":315,"reference_id":"31548674","reference_source":"pmid","reference_html":"Structural basis for chain release from the enacyloxin polyketide synthase. <i> Kosol S, Gallo A, Griffiths D, Valentic TR, Masschelein J, Jenner M, de Los Santos ELC, Manzi L, Sydor PK, Rea D, Zhou S, Fülöp V, Oldham NJ, Tsai SC, Challis GL, Lewandowski JR. </i> Nat Chem, 2019","date":"2024-02-23T16:49:57.202Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":null,"value":288,"statements":[{"type":"Supplementary material","text":"All solution NMR experiments used for resonance assignments of the apo- and holo-Bamb_5917 PCP\ndomain and for structure calculations of the apo-Bamb_5917 PCP domain were recorded on Bruker\nAVANCE II 700 spectrometer, equipped with a TCI cryoprobe, on 0.6 mM 13C,15N–labelled or 15N–\nlabelled samples in 50 mM phosphate buffer, pH 7.4, containing 10% (v/v) D2O, 150 mM NaCl and\nDSS (for internal referencing) at 288 K."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7.4}],"cross_refs":[{"db":"PDB","id":"5MTI"},{"db":"BMRB","id":"34085"}],"region_id":"DP04160r002","statement":[{"text":"The disordered termini of the PCP domain are highly mobile on the fast ps-ns timescale as indicated by low heteronuclear nuclear Overhauser effects (NOEs), transverse relaxation rates (R2), and high longitudinal relaxation rates (R1) for these regions compared to the structured core (Fig. 1d and Supplementary Fig. 13). The overall rotational diffusion13 is consistent with a monomeric state, with a compact folded core and disordered termini (Supplementary Materials and Methods). The dynamic, disordered nature of the terminal regions is further confirmed by the low predicted S2 parameters (Fig. 1d and Supplementary Fig. 14; S2 of 1 and 0 indicate complete rigidity and unrestricted motion, respectively), typical chemical shift values for a random coil and a lack of long-range NOEs.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T10:52:43.536Z"}},{"start":307,"end":315,"reference_id":"31548674","reference_source":"pmid","reference_html":"Structural basis for chain release from the enacyloxin polyketide synthase. <i> Kosol S, Gallo A, Griffiths D, Valentic TR, Masschelein J, Jenner M, de Los Santos ELC, Manzi L, Sydor PK, Rea D, Zhou S, Fülöp V, Oldham NJ, Tsai SC, Challis GL, Lewandowski JR. </i> Nat Chem, 2019","date":"2024-02-23T17:02:55.579Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":null,"value":288,"statements":[{"type":"Supplementary material","text":"All titration spectra were acquired in a 3 mm tube at 288K on a Bruker Avance II 700 MHz spectrometer\nequipped with a TCI cryoprobe. Bamb_5915 or the excised Bamb_5915 bHD domain were added\nstepwise (see Supplementary Table 5 for concentrations) and 2-D 15N-HSQC or 1H-15N BEST-TROSY-\nHSQC spectra were acquired at each titration step. containing 10% (v/v) D2O, 150 mM NaCl and\nDSS (for internal referencing) at 288 K."}]}],"cross_refs":[{"db":"BMRB","id":"27304"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q0B313","operator":null,"partner_start":1,"partner_end":67}],"region_id":"DP04160r003","statement":[{"text":"In the NMR titrations of the Bamb_5917 holo-PCP domain with both full-length Bamb_5915 and its excised βHD domain the system is in slow to intermediate exchange14 (Supplementary Fig. 16). Higher than average local apparent association constants, Ka, in the titrations with the excised βHD domain identify a Short Linear Motif (SLiM; S307-R315)11 in the disordered C-terminus of Bamb_5917 as the major interaction site (Fig. 2a-b).","type":"Results"},{"text":"Residues boundaries of the partner's βHD domain could be identified from a supplementary table.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-27T10:52:47.839Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MVSAPRQAVLPASPTVSNQADDAMTLATLQAAETADIIVLSAPGVDALRGAVWQLLGQLRALASDAAAEPFTLADLAYTLKSRPEAGGCRVAFVTRQLDDLAAGLEHYLRAHAQAEASVPRSVTPGRHGELVTILRGDLAADSGTARLLTGAAAATMARALWAARDLENLALIWVRGGQLDWDALREGPPPRRLAWPDQAPLEAGARPAPEAFEGAAAGVSAAGIEPDLTAIWQALFALPAVGRHQDFFALGGDSQLGLRMLAQLRERHGVDLPLRCLYEAPTVARLAETIVRLAAPAPSGDQDDASEYEEGVIR","taxonomy":["Bacteria","Pseudomonadota","Betaproteobacteria","Burkholderiales","Burkholderiaceae","Burkholderia","Burkholderia cepacia complex"],"alphafold_very_low_content":0.2222222222222222,"disorder_content":0.06349206349206349,"disprot_consensus":{"full":[{"start":296,"end":315,"type":"D"}],"Structural state":[{"start":296,"end":315,"type":"D"}],"Disorder function":[{"start":296,"end":315,"type":"F"}],"Molecular function":[{"start":307,"end":315,"type":"F"}]}},{"disprot_id":"DP04161","acc":"B7UM99","creator":"ndeutsch","date":"2024-02-26T19:31:17.961Z","features":{"pfam":[{"id":"PF03549","name":"Translocated intimin receptor (Tir) intimin-binding domain","start":271,"end":336},{"id":"PF07489","name":"Translocated intimin receptor (Tir) C-terminus","start":337,"end":550},{"id":"PF07490","name":"Translocated intimin receptor (Tir) N-terminus","start":1,"end":270}],"gene3D":[]},"genes":[{"name":{"value":"tir"},"synonyms":[{"value":"espE"}],"olnNames":[{"value":"E2348C_3941"}]}],"length":550,"name":"Translocated intimin receptor Tir","ncbi_taxon_id":574521,"organism":"Escherichia coli O127:H6 (strain E2348/69 / EPEC)","regions":[{"start":198,"end":233,"reference_id":"38351154","reference_source":"pmid","reference_html":"The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection. <i> Vieira MFM, Hernandez G, Zhong Q, Arbesú M, Veloso T, Gomes T, Martins ML, Monteiro H, Frazão C, Frankel G, Zanzoni A, Cordeiro TN. </i> Commun Biol, 2024","date":"2024-03-20T18:51:39.599Z","curator_id":"ndeutsch","curator_name":"Norbert Deutsch","curator_orcid":"0009-0006-7459-0201","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04161r001","statement":[{"text":"For this integrative study, we used the protein constructs encompassing the residues 1-233 and 388-550 from the N-terminal and C-terminal cytosolic regions of EPEC O127:H6 Tir, respectively.","type":"Results"},{"text":"The corresponding SAXS-driven ab initio reconstruction highlights an elongated S-shaped core for the N-Tir dimer (Supplementary Fig. 6). This extended dimer is largely disordered but contains stable secondary structural elements.","type":"Results"},{"text":"Nevertheless, we found that the 52 kDa dimer has a [15N-1HN]-HSQC NMR spectrum at 5 °C characterised by intense signals and low chemical shift dispersion akin to an IDP (Fig. 2d). We assigned the resonances at 5 °C mostly to the first 80 and last 35 residues of the N-Tir, meaning that those regions are flexible in solution.","type":"Results"}],"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":8,"statements":[{"type":"Methods","text":"The SEC mobile phase consisted of 20 mM Phosphate pH 6.5, 150 mM NaCl, and 1 mM EDTA, for C-Tir, and 100 mM Tris·HCl at pH 8.0, 150 mM NaCl, 2 mM DTT, and 1 mM EDTA for N-Tir and NS-Tir. "}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-26T15:56:12.423Z"}},{"start":1,"end":80,"reference_id":"38351154","reference_source":"pmid","reference_html":"The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection. <i> Vieira MFM, Hernandez G, Zhong Q, Arbesú M, Veloso T, Gomes T, Martins ML, Monteiro H, Frazão C, Frankel G, Zanzoni A, Cordeiro TN. </i> Commun Biol, 2024","date":"2024-03-20T18:50:02.952Z","curator_id":"ndeutsch","curator_name":"Norbert Deutsch","curator_orcid":"0009-0006-7459-0201","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":5,"statements":[{"type":"Results","text":"We assigned the resonances at 5 °C mostly to the first 80 and last 35 residues of the N-Tir, meaning that those regions are flexible in solution. "}]}],"region_id":"DP04161r002","statement":[{"text":" For this integrative study, we used the protein constructs encompassing the residues 1-233 and 388-550 from the N-terminal and C-terminal cytosolic regions of EPEC O127:H6 Tir, respectively (Fig. 1e, Supplementary Fig. 4, Supplementary Table 4)","type":"Results"},{"text":"Nevertheless, we found that the 52 kDa dimer has a [15N-1HN]-HSQC NMR spectrum at 5 °C characterised by intense signals and low chemical shift dispersion akin to an IDP (Fig. 2d). We assigned the resonances at 5 °C mostly to the first 80 and last 35 residues of the N-Tir, meaning that those regions are flexible in solution.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-26T15:56:29.252Z"}},{"start":388,"end":550,"reference_id":"38351154","reference_source":"pmid","reference_html":"The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection. <i> Vieira MFM, Hernandez G, Zhong Q, Arbesú M, Veloso T, Gomes T, Martins ML, Monteiro H, Frazão C, Frankel G, Zanzoni A, Cordeiro TN. </i> Commun Biol, 2024","date":"2024-03-28T09:08:07.888Z","curator_id":"ndeutsch","curator_name":"Norbert Deutsch","curator_orcid":"0009-0006-7459-0201","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04161r003","statement":[{"text":"We assessed the structural disorder propensity of EPEC O127:H6 N-Tir and C-Tir by multiple biophysical methods, including small-angle X-ray scattering (SAXS), circular dichroism (CD), and nuclear magnetic resonance (NMR).","type":"Results"},{"text":"For this integrative study, we used the protein constructs encompassing the residues 1-233 and 388-550 from the N-terminal and C-terminal cytosolic regions of EPEC O127:H6 Tir, respectively (Fig. 1e, Supplementary Fig. 4, Supplementary Table 4). ","type":"Results"},{"text":"Analytical SEC in combination with SAXS reveals a monomeric state for C-Tir in solution with an Rg of 38.8 ± 0.2 Å and a Dmax of 128.0 ± 5.0 Å (Supplementary Figure 6, Supplementary Table 5).","type":"Results"},{"text":"The SAXS-derived Kratky plot of C-Tir also shows characteristics of disordered or unfolded proteins, monotonically increasing without a well-defined maximum (Fig. 4a).","type":"Results"},{"text":" Likewise, the asymmetric pair distance distribution function, P(r), obtained from the scattering data, is compatible with a highly flexible protein sampling pairwise distances far exceeding those expected for a globular protein of the same molecular weight59 (Supplementary Figure 6).","type":"Results"}],"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":6.5,"statements":[{"type":"Methods","text":" The SEC mobile phase consisted of 20 mM Phosphate pH 6.5, 150 mM NaCl, and 1 mM EDTA, for C-Tir, and 100 mM Tris·HCl at pH 8.0, 150 mM NaCl, 2 mM DTT, and 1 mM EDTA for N-Tir and NS-Tir. "}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-28T13:59:11.549Z"}},{"start":388,"end":550,"reference_id":"38351154","reference_source":"pmid","reference_html":"The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection. <i> Vieira MFM, Hernandez G, Zhong Q, Arbesú M, Veloso T, Gomes T, Martins ML, Monteiro H, Frazão C, Frankel G, Zanzoni A, Cordeiro TN. </i> Commun Biol, 2024","date":"2024-03-28T15:41:09.257Z","curator_id":"ndeutsch","curator_name":"Norbert Deutsch","curator_orcid":"0009-0006-7459-0201","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04161r004","statement":[{"text":"We assessed the structural disorder propensity of EPEC O127:H6 N-Tir and C-Tir by multiple biophysical methods, including small-angle X-ray scattering (SAXS), circular dichroism (CD), and nuclear magnetic resonance (NMR).","type":"Results"},{"text":" For this integrative study, we used the protein constructs encompassing the residues 1-233 and 388-550 from the N-terminal and C-terminal cytosolic regions of EPEC O127:H6 Tir, respectively (Fig. 1e, Supplementary Fig. 4, Supplementary Table 4).","type":"Results"},{"text":"The intrinsic disorder of C-Tir is also reflected in its CD and [15N-1HN]-HSQC NMR spectra. C-Tir’s CD profile has negative ellipticity at 200 nm and a shallow band in the 210–230 nm range (Fig. 4b), indicating a high content of random coil with minimal ordered structural elements60.","type":"Results"}],"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":6.5,"statements":[{"type":"Methods","text":"We performed Far-UV CD spectroscopy in a J-815 spectrophotometer (Jasco), using a 1-mm optical pathlength cuvette for high performance (QS) (Hellma). The protein concentration was 6, 10, or 11.9 μM for N-Tir, NS-Tir, or C-Tir samples. N-Tir and NS-Tir were in 0.4 mM Tris-HCl pH 8, 15.0 mM NaF, and 0.1 mM TCEP. C-Tir was in 2 mM phosphate pH 6.5, 15 mM NaF and 0.1 mM EDTA supplemented with 0, 5, 10, 20, and 50% TFE. "}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-28T16:39:05.667Z"}},{"start":198,"end":233,"reference_id":"38351154","reference_source":"pmid","reference_html":"The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection. <i> Vieira MFM, Hernandez G, Zhong Q, Arbesú M, Veloso T, Gomes T, Martins ML, Monteiro H, Frazão C, Frankel G, Zanzoni A, Cordeiro TN. </i> Commun Biol, 2024","date":"2024-03-20T18:49:32.388Z","curator_id":"ndeutsch","curator_name":"Norbert Deutsch","curator_orcid":"0009-0006-7459-0201","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":5,"statements":[{"type":"Results","text":"Nevertheless, we found that the 52 kDa dimer has a [15N-1HN]-HSQC NMR spectrum at 5 °C characterised by intense signals and low chemical shift dispersion akin to an IDP (Fig. 2d). We assigned the resonances at 5 °C mostly to the first 80 and last 35 residues of the N-Tir, meaning that those regions are flexible in solution."}]}],"region_id":"DP04161r006","statement":[{"text":" For this integrative study, we used the protein constructs encompassing the residues 1-233 and 388-550 from the N-terminal and C-terminal cytosolic regions of EPEC O127:H6 Tir, respectively (Fig. 1e, Supplementary Fig. 4, Supplementary Table 4)","type":"Results"},{"text":"Nevertheless, we found that the 52 kDa dimer has a [15N-1HN]-HSQC NMR spectrum at 5 °C characterised by intense signals and low chemical shift dispersion akin to an IDP (Fig. 2d). We assigned the resonances at 5 °C mostly to the first 80 and last 35 residues of the N-Tir, meaning that those regions are flexible in solution.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-26T16:02:24.270Z"}},{"start":452,"end":456,"reference_id":"38351154","reference_source":"pmid","reference_html":"The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection. <i> Vieira MFM, Hernandez G, Zhong Q, Arbesú M, Veloso T, Gomes T, Martins ML, Monteiro H, Frazão C, Frankel G, Zanzoni A, Cordeiro TN. </i> Commun Biol, 2024","date":"2025-02-17T19:20:25.951Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":454,"end":454,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":474,"end":474,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":486,"end":486,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":511,"end":511,"position":"Specific residue"}],"cross_refs":[{"db":"BMRB","id":"50759"}],"region_id":"DP04161r007","statement":[{"text":"To this end, we incubated C-Tir with the Src family PTK Fyn, and quantitatively monitored its phosphorylation by NMR72. The sensitivity of chemical shifts to changes caused by phosphorylation allowed us to identify four phosphorylated tyrosine sites along the disordered C-Tir modified by Fyn (i.e., Y454, Y474, Y483, Y511). Phosphorylation caused small but noticeable changes in the chemical shifts of the tyrosines and adjacent residues. The [15N-1HN]-HSQC spectrum displayed low amide proton dispersion, a diagnostic that the C-Tir remains disordered upon multisite phosphorylation.","type":"Results"}]},{"start":472,"end":476,"reference_id":"38351154","reference_source":"pmid","reference_html":"The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection. <i> Vieira MFM, Hernandez G, Zhong Q, Arbesú M, Veloso T, Gomes T, Martins ML, Monteiro H, Frazão C, Frankel G, Zanzoni A, Cordeiro TN. </i> Commun Biol, 2024","date":"2025-02-17T19:20:51.036Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":454,"end":454,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":474,"end":474,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":486,"end":486,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":511,"end":511,"position":"Specific residue"}],"cross_refs":[{"db":"BMRB","id":"50759"}],"region_id":"DP04161r008","statement":[{"text":"To this end, we incubated C-Tir with the Src family PTK Fyn, and quantitatively monitored its phosphorylation by NMR72. The sensitivity of chemical shifts to changes caused by phosphorylation allowed us to identify four phosphorylated tyrosine sites along the disordered C-Tir modified by Fyn (i.e., Y454, Y474, Y483, Y511). Phosphorylation caused small but noticeable changes in the chemical shifts of the tyrosines and adjacent residues. The [15N-1HN]-HSQC spectrum displayed low amide proton dispersion, a diagnostic that the C-Tir remains disordered upon multisite phosphorylation.","type":"Results"}]},{"start":481,"end":485,"reference_id":"38351154","reference_source":"pmid","reference_html":"The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection. <i> Vieira MFM, Hernandez G, Zhong Q, Arbesú M, Veloso T, Gomes T, Martins ML, Monteiro H, Frazão C, Frankel G, Zanzoni A, Cordeiro TN. </i> Commun Biol, 2024","date":"2025-02-17T19:21:05.588Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":454,"end":454,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":474,"end":474,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":486,"end":486,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":511,"end":511,"position":"Specific residue"}],"cross_refs":[{"db":"BMRB","id":"50759"}],"region_id":"DP04161r009","statement":[{"text":"To this end, we incubated C-Tir with the Src family PTK Fyn, and quantitatively monitored its phosphorylation by NMR72. The sensitivity of chemical shifts to changes caused by phosphorylation allowed us to identify four phosphorylated tyrosine sites along the disordered C-Tir modified by Fyn (i.e., Y454, Y474, Y483, Y511). Phosphorylation caused small but noticeable changes in the chemical shifts of the tyrosines and adjacent residues. The [15N-1HN]-HSQC spectrum displayed low amide proton dispersion, a diagnostic that the C-Tir remains disordered upon multisite phosphorylation.","type":"Results"}]},{"start":509,"end":513,"reference_id":"38351154","reference_source":"pmid","reference_html":"The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection. <i> Vieira MFM, Hernandez G, Zhong Q, Arbesú M, Veloso T, Gomes T, Martins ML, Monteiro H, Frazão C, Frankel G, Zanzoni A, Cordeiro TN. </i> Commun Biol, 2024","date":"2025-02-17T19:21:23.089Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":454,"end":454,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":474,"end":474,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":486,"end":486,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":511,"end":511,"position":"Specific residue"}],"cross_refs":[{"db":"BMRB","id":"50759"}],"region_id":"DP04161r010","statement":[{"text":"To this end, we incubated C-Tir with the Src family PTK Fyn, and quantitatively monitored its phosphorylation by NMR72. The sensitivity of chemical shifts to changes caused by phosphorylation allowed us to identify four phosphorylated tyrosine sites along the disordered C-Tir modified by Fyn (i.e., Y454, Y474, Y483, Y511). Phosphorylation caused small but noticeable changes in the chemical shifts of the tyrosines and adjacent residues. The [15N-1HN]-HSQC spectrum displayed low amide proton dispersion, a diagnostic that the C-Tir remains disordered upon multisite phosphorylation.","type":"Results"}]},{"start":388,"end":550,"reference_id":"38351154","reference_source":"pmid","reference_html":"The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection. <i> Vieira MFM, Hernandez G, Zhong Q, Arbesú M, Veloso T, Gomes T, Martins ML, Monteiro H, Frazão C, Frankel G, Zanzoni A, Cordeiro TN. </i> Commun Biol, 2024","date":"2024-03-20T18:57:50.459Z","curator_id":"ndeutsch","curator_name":"Norbert Deutsch","curator_orcid":"0009-0006-7459-0201","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"BMRB","id":"50758"}],"region_id":"DP04161r011","statement":[{"text":"For this integrative study, we used the protein constructs encompassing the residues 1-233 and 388-550 from the N-terminal and C-terminal cytosolic regions of EPEC O127:H6 Tir, respectively (Fig. 1e, Supplementary Fig. 4, Supplementary Table 4)","type":"Results"},{"text":"This construct’s 2D-[15N-1HN]-HSQC NMR spectrum displays a typical IDP fingerprint with low chemical shift dispersion61 (Fig. 4c).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-26T16:01:44.442Z"}},{"start":509,"end":515,"reference_id":"38351154","reference_source":"pmid","reference_html":"The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection. <i> Vieira MFM, Hernandez G, Zhong Q, Arbesú M, Veloso T, Gomes T, Martins ML, Monteiro H, Frazão C, Frankel G, Zanzoni A, Cordeiro TN. </i> Commun Biol, 2024","date":"2024-03-20T21:54:21.633Z","curator_id":"ndeutsch","curator_name":"Norbert Deutsch","curator_orcid":"0009-0006-7459-0201","term_id":"GO:0042169","term_name":"SH2 domain binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P29350","operator":null,"partner_start":101,"partner_end":217}],"region_id":"DP04161r012","statement":[{"text":"Using the C-terminal SH2 domain (C-SH2) of phosphatase SHP-1, we identified, by NMR, that residues surrounding the unphosphorylated Y511 ITIM-like motif are involved in binding SH2 domains (Fig. 6a). Binding to C-Tir caused a selective loss of the backbone amide cross-peaks intensities, mainly from residues A512LLA515 (Fig. 6b). Visible NMR signals retained low dispersion, indicating that the protein remains mostly disordered and flexible in the complex","type":"Results"},{"text":"The Y511 points to the canonically defined “pTyr pocket”, and the SH2 recognizes the hydrophobic Leu residue in position +3 via the “specific pocket”70. Moreover, residue in position −2 interacts with αA, forming a “three-pronged plug” interaction altogether.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a SH2 domain (Src homology 2) of a protein, a protein domain of about 100 amino-acid residues and belonging to the alpha + beta domain class.\" [GOC:go_curators, Pfam:PF00017]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-26T16:04:02.654Z"}},{"start":454,"end":511,"reference_id":"38351154","reference_source":"pmid","reference_html":"The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection. <i> Vieira MFM, Hernandez G, Zhong Q, Arbesú M, Veloso T, Gomes T, Martins ML, Monteiro H, Frazão C, Frankel G, Zanzoni A, Cordeiro TN. </i> Commun Biol, 2024","date":"2026-01-07T17:12:29.449Z","curator_id":"ndeutsch","curator_name":"Norbert Deutsch","curator_orcid":"0009-0006-7459-0201","term_id":"GO:0042169","term_name":"SH2 domain binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":1,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":454,"end":454,"position":"Specific residue","statements":[{"type":"Results","text":"To fully assess Tir ability to recruit SH2 domains, we reconstructed C-Tir’s Tyr-phosphorylated state and evaluated its binding to C-SH2. To this end, we incubated C-Tir with the Src family PTK Fyn, and quantitatively monitored its phosphorylation by NMR72. The sensitivity of chemical shifts to changes caused by phosphorylation allowed us to identify four phosphorylated tyrosine sites along the disordered C-Tir modified by Fyn (i.e., Y454, Y474, Y483, Y511)."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":474,"end":474,"position":"Specific residue","statements":[{"type":"Results","text":"To fully assess Tir ability to recruit SH2 domains, we reconstructed C-Tir’s Tyr-phosphorylated state and evaluated its binding to C-SH2. To this end, we incubated C-Tir with the Src family PTK Fyn, and quantitatively monitored its phosphorylation by NMR72. The sensitivity of chemical shifts to changes caused by phosphorylation allowed us to identify four phosphorylated tyrosine sites along the disordered C-Tir modified by Fyn (i.e., Y454, Y474, Y483, Y511)."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":483,"end":483,"position":"Specific residue","statements":[{"type":"Results","text":"To fully assess Tir ability to recruit SH2 domains, we reconstructed C-Tir’s Tyr-phosphorylated state and evaluated its binding to C-SH2. To this end, we incubated C-Tir with the Src family PTK Fyn, and quantitatively monitored its phosphorylation by NMR72. The sensitivity of chemical shifts to changes caused by phosphorylation allowed us to identify four phosphorylated tyrosine sites along the disordered C-Tir modified by Fyn (i.e., Y454, Y474, Y483, Y511)."}]},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":511,"end":511,"position":"Specific residue","statements":[{"type":"Results","text":"To fully assess Tir ability to recruit SH2 domains, we reconstructed C-Tir’s Tyr-phosphorylated state and evaluated its binding to C-SH2. To this end, we incubated C-Tir with the Src family PTK Fyn, and quantitatively monitored its phosphorylation by NMR72. The sensitivity of chemical shifts to changes caused by phosphorylation allowed us to identify four phosphorylated tyrosine sites along the disordered C-Tir modified by Fyn (i.e., Y454, Y474, Y483, Y511)."}]}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P29350 ","operator":null,"partner_start":101,"partner_end":217}],"region_id":"DP04161r013","statement":[{"text":"With the resonance re-assignment of pC-Tir, we identified that upon phosphorylation, all tyrosine sites interact with C-SH2, and not exclusively the Y511-based motif as observed for unphosphorylated C-Tir.","type":"Results"},{"text":"Phosphorylation enhanced the binding to Y511 site by ~10 fold and enabled other tyrosine-based motifs to engage C-SH2. Among the four pYs, the resonances around pY454 were less broadened during the titration, suggesting lower local binding. The remaining pYs bind C-SH2 with similar strength (~3-9μM). Overall, phosphorylation at multiple tyrosine sites provides various SH2 docking sites and reinforces the role of Tir as a scaffolding hub.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a SH2 domain (Src homology 2) of a protein, a protein domain of about 100 amino-acid residues and belonging to the alpha + beta domain class.\" [GOC:go_curators, Pfam:PF00017]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-01-07T17:12:37.040Z"}},{"start":483,"end":515,"reference_id":"38351154","reference_source":"pmid","reference_html":"The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection. <i> Vieira MFM, Hernandez G, Zhong Q, Arbesú M, Veloso T, Gomes T, Martins ML, Monteiro H, Frazão C, Frankel G, Zanzoni A, Cordeiro TN. </i> Commun Biol, 2024","date":"2024-03-20T22:52:25.487Z","curator_id":"ndeutsch","curator_name":"Norbert Deutsch","curator_orcid":"0009-0006-7459-0201","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"45240","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04161r014","statement":[{"text":"In the presence of bicelles containing DMPC lipids, we observed a marked residue-specific decrease in the ratio of NMR signals around Y511, yet more subtle, also around Y483 (Fig. 8). This finding shows that C-Tir does interact with non-charged lipid bilayers predominantly via its Y511-based motif, including mostly hydrophobic residues, such as A512LLA515.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-26T16:05:30.160Z"}},{"start":35,"end":77,"reference_id":"30118511","reference_source":"pmid","reference_html":"Molecular basis for CesT recognition of type III secretion effectors in enteropathogenic Escherichia coli. <i> Little DJ, Coombes BK. </i> PLoS Pathog, 2018","date":"2025-02-14T17:10:45.224Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006074","ec_ontology":"ECO","ec_name":"co-purification evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P21244","operator":null,"partner_start":1,"partner_end":138}],"region_id":"DP04161r015","statement":[{"text":"Tir fragments containing residues 23–80, 32–80, and 35–77 co-purified CesT as seen by Ni2+-affinity pull-down and immunoblotting (Fig 1B and S1A Fig), whereas CesT alone was never pulled-down in the absence of Tir by the Ni2+-affinity resin, thus confirming specificity of our assay. When these Tir fragments were truncated further to residues 32–73, 37–80, and 37–73, they lost the ability to co-purify with CesT (Fig 1B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":35,"end":53,"reference_id":"30118511","reference_source":"pmid","reference_html":"Molecular basis for CesT recognition of type III secretion effectors in enteropathogenic Escherichia coli. <i> Little DJ, Coombes BK. </i> PLoS Pathog, 2018","date":"2026-01-07T17:27:43.611Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051087","term_name":"chaperone binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"cross_refs":[{"db":"PDB","id":"5WEZ"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P21244","operator":null,"partner_start":1,"partner_end":130}],"region_id":"DP04161r016","sequence_construct":"MGSSHHHHHHSQDPGGTGHLISSTGALGSRSLFSPLRNSMADSVDSRDIPGLPTNPSRLAAAT","statement":[{"text":"Tir32-80 adopts minimal regular secondary structure that is limited to two small β-strands, β1’ and β2’ (Fig 2A). The Tir32-80 fragment binds CesT138 in two distinct locations and is separated by a break in the peptide chain likely due to residue mobility in the crystal. Tir residues 35–53 adopt a β-hairpin-like fold and extend the 5-stranded β-sheet core of CesT138, while also being pinched between α1 and orthogonally below by α3 of CesT138 (Fig 2A).","type":"Results"},{"text":"The β-motif was originally identified in the SipA-InvB complex [31, 32], but appears to be a conserved mode of binding present in all class I chaperone-effector complexes [33].","type":"Results"}],"term_comment":"","term_def":"\"Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.\" [PMID:10585443]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":35,"end":53,"reference_id":"30118511","reference_source":"pmid","reference_html":"Molecular basis for CesT recognition of type III secretion effectors in enteropathogenic Escherichia coli. <i> Little DJ, Coombes BK. </i> PLoS Pathog, 2018","date":"2025-02-14T16:49:16.010Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"cross_refs":[{"db":"PDB","id":"5WEZ"}],"region_id":"DP04161r017","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P21244 "}],"sequence_construct":"MGSSHHHHHHSQDPGGTGHLISSTGALGSRSLFSPLRNSMADSVDSRDIPGLPTNPSRLAAAT","statement":[{"text":"Tir32-80 adopts minimal regular secondary structure that is limited to two small β-strands, β1’ and β2’ (Fig 2A). The Tir32-80 fragment binds CesT138 in two distinct locations and is separated by a break in the peptide chain likely due to residue mobility in the crystal. Tir residues 35–53 adopt a β-hairpin-like fold and extend the 5-stranded β-sheet core of CesT138, while also being pinched between α1 and orthogonally below by α3 of CesT138 (Fig 2A).","type":"Results"},{"text":"The β-motif was originally identified in the SipA-InvB complex [31, 32], but appears to be a conserved mode of binding present in all class I chaperone-effector complexes [33].","type":"Results"}]},{"start":35,"end":53,"reference_id":"30118511","reference_source":"pmid","reference_html":"Molecular basis for CesT recognition of type III secretion effectors in enteropathogenic Escherichia coli. <i> Little DJ, Coombes BK. </i> PLoS Pathog, 2018","date":"2025-02-14T16:49:55.140Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"cross_refs":[{"db":"PDB","id":"5WEZ"}],"region_id":"DP04161r018","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P21244 "}],"sequence_construct":"MGSSHHHHHHSQDPGGTGHLISSTGALGSRSLFSPLRNSMADSVDSRDIPGLPTNPSRLAAAT","statement":[{"text":"Tir32-80 adopts minimal regular secondary structure that is limited to two small β-strands, β1’ and β2’ (Fig 2A). The Tir32-80 fragment binds CesT138 in two distinct locations and is separated by a break in the peptide chain likely due to residue mobility in the crystal. Tir residues 35–53 adopt a β-hairpin-like fold and extend the 5-stranded β-sheet core of CesT138, while also being pinched between α1 and orthogonally below by α3 of CesT138 (Fig 2A).","type":"Results"},{"text":"The β-motif was originally identified in the SipA-InvB complex [31, 32], but appears to be a conserved mode of binding present in all class I chaperone-effector complexes [33].","type":"Results"}],"states_connection":[{"source":"DP04161r002","target":"DP04161r017"}]},{"start":65,"end":75,"reference_id":"30118511","reference_source":"pmid","reference_html":"Molecular basis for CesT recognition of type III secretion effectors in enteropathogenic Escherichia coli. <i> Little DJ, Coombes BK. </i> PLoS Pathog, 2018","date":"2026-01-07T17:17:46.634Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051087","term_name":"chaperone binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"cross_refs":[{"db":"PDB","id":"5WEZ"}],"region_id":"DP04161r019","sequence_construct":"MGSSHHHHHHSQDPGGTGHLISSTGALGSRSLFSPLRNSMADSVDSRDIPGLPTNPSRLAAAT","statement":[{"text":"Tir residues 65–75 are bound along the concave surface of the β-sheet core of CesT138 (Fig 2A).","type":"Results"},{"text":"Specifically, Tir residues I38 (purple), L44 (cyan), and L49 (cyan) anchor the β-hairpin-like peptide to CesT138 (Fig 2D); and L69 plus three additional proline residues make a second point of contact with the β-sheet core of CesT138 (Fig 2E).","type":"Results"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P21244","operator":null,"partner_start":1,"partner_end":130}],"term_comment":"","term_def":"\"Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.\" [PMID:10585443]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":490,"end":550,"reference_id":"30118511","reference_source":"pmid","reference_html":"Molecular basis for CesT recognition of type III secretion effectors in enteropathogenic Escherichia coli. <i> Little DJ, Coombes BK. </i> PLoS Pathog, 2018","date":"2026-01-07T17:13:33.584Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051087","term_name":"chaperone binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007074","ec_ontology":"ECO","ec_name":"bacterial 2-hybrid assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Figure","text":"BTH101 reporter cells producing the indicated Tir and CesT constructs fused to the T18 or T25 domain fragments of the Bordetella adenylate cyclase were spotted on LB-agar supplemented with IPTG and X-gal."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P21244","operator":null,"partner_start":1,"partner_end":138}],"region_id":"DP04161r020","statement":[{"text":"T18 fused to Tir490-550 showed a strong interaction with CesT fused to T25 by BACTH assays (Fig 4B), and was able to pull-down CesT in co-expression pull-down experiments (Fig 4D), confirming this site as a second CesT-binding region.","type":"Results"},{"text":"Furthermore, both of the Tir CesT-binding regions have a conserved sequence motif distinct from the known chaperone binding β-motif.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.\" [PMID:10585443]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":490,"end":550,"reference_id":"30118511","reference_source":"pmid","reference_html":"Molecular basis for CesT recognition of type III secretion effectors in enteropathogenic Escherichia coli. <i> Little DJ, Coombes BK. </i> PLoS Pathog, 2018","date":"2026-01-07T17:13:13.126Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051087","term_name":"chaperone binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006074","ec_ontology":"ECO","ec_name":"co-purification evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Figure","text":"The His6-Tir490-550 peptide was co-expressed with CesT-FLAG and soluble cell lysate (input, white circle) and Ni2+ pull-down (elution, grey circle) fractions were analyzed by SDS-PAGE and immunoblotting for the ability of the isolated C-terminal Tir peptide to co-purify CesT-FLAG."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P21244","operator":null,"partner_start":1,"partner_end":138}],"region_id":"DP04161r021","statement":[{"text":"T18 fused to Tir490-550 showed a strong interaction with CesT fused to T25 by BACTH assays (Fig 4B), and was able to pull-down CesT in co-expression pull-down experiments (Fig 4D), confirming this site as a second CesT-binding region.","type":"Results"},{"text":"Furthermore, both of the Tir CesT-binding regions have a conserved sequence motif distinct from the known chaperone binding β-motif.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.\" [PMID:10585443]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"}],"regions_counter":21,"released":"2024_06","sequence":"MPIGNLGNNVNGNHLIPPAPPLPSQTDGAARGGTGHLISSTGALGSRSLFSPLRNSMADSVDSRDIPGLPTNPSRLAAATSETCLLGGFEVLHDKGPLDILNTQIGPSAFRVEVQADGTHAAIGEKNGLEVSVTLSPQEWSSLQSIDTEGKNRFVFTGGRGGSGHPMVTVASDIAEARTKILAKLDPDNHGGRQPKDVDTRSVGVGSASGIDDGVVSETHTSTTNSSVRSDPKFWVSVGAIAAGLAGLAATGIAQALALTPEPDDPTTTDPDQAANAAESATKDQLTQEAFKNPENQKVNIDANGNAIPSGELKDDIVEQIAQQAKEAGEVARQQAVESNAQAQQRYEDQHARRQEELQLSSGIGYGLSSALIVAGGIGAGVTTALHRRNQPAEQTTTTTTHTVVQQQTGGNTPAQGGTDATRAEDASLNRRDSQGSVASTHWSDSSSEVVNPYAEVGGARNSLSAHQPEEHIYDEVAADPGYSVIQNFSGSGPVTGRLIGTPGQGIQSTYALLANSGGLRLGMGGLTSGGESAVSSVNAAPTPGPVRFV","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"alphafold_very_low_content":0.6927272727272727,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.5072727272727273,"disprot_consensus":{"full":[{"start":1,"end":34,"type":"D"},{"start":35,"end":53,"type":"T"},{"start":54,"end":80,"type":"D"},{"start":198,"end":233,"type":"D"},{"start":388,"end":550,"type":"D"}],"Structural state":[{"start":1,"end":80,"type":"D"},{"start":198,"end":233,"type":"D"},{"start":388,"end":550,"type":"D"}],"Disorder function":[{"start":452,"end":456,"type":"F"},{"start":472,"end":476,"type":"F"},{"start":481,"end":485,"type":"F"},{"start":509,"end":513,"type":"F"}],"Molecular function":[{"start":35,"end":77,"type":"F"},{"start":454,"end":550,"type":"F"}],"Structural transition":[{"start":35,"end":53,"type":"T"}]}},{"disprot_id":"DP04163","acc":"P32120-2","creator":"vnugnes","date":"2024-02-27T16:51:19.684Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"ARRB2"}}],"length":409,"name":"Isoform Short of Beta-arrestin-2","ncbi_taxon_id":9913,"organism":"Bos taurus","regions":[{"start":350,"end":393,"reference_id":"29127291","reference_source":"pmid","reference_html":"Structural basis of arrestin-3 activation and signaling. <i> Chen Q, Perry NA, Vishnivetskiy SA, Berndt S, Gilbert NC, Zhuo Y, Singh PK, Tholen J, Ohi MD, Gurevich EV, Brautigam CA, Klug CS, Gurevich VV, Iverson TM. </i> Nat Commun, 2017","date":"2024-02-27T17:02:04.821Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"5TV1"}],"region_id":"DP04163r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17401","entry_name":"myo-inositol hexakisphosphate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":"glycerol"}],"statement":[{"text":"The PDB structure shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"sequence_construct":"MGEKPGTRVFKKSSPNCKLTVYLGKRDFVDHLDKVDPVDGVVLVDPDYLKDRKVFVTLTCAFRYGREDLDVLGLSFRKDLFIANYQAFPPTPNPPRPPTRLQERLLRKLGQHAHPFFFTIPQNLPCSVTLQPGPEDTGKACGVDFEIRAFCAKSLEEKSHKRNSVRLVIRKVQFAPEKPGPQPSAETTRHFLMSDRSLHLEASLDKELYYHGEPLNVNVHVTNNSTKTVKKIKVSVRQYADICLFSTAQYKCPVAQVEQDDQVSPSSTFCKVYTITPLLSNNREKRGLALDGKLKHEDTNLASSTIVKEGANKEVLGILVSYRVKVKLVVSRGGDVSVELPFVLMHPKPHDHIALPRPQSAVPETDAPVDTNLIEFETNYATDDDIVFEDFAR","validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T07:23:37.722Z"}},{"start":349,"end":385,"reference_id":"21215759","reference_source":"pmid","reference_html":"Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual subtypes. <i> Zhan X, Gimenez LE, Gurevich VV, Spiller BW. </i> J Mol Biol, 2011","date":"2024-02-27T17:09:35.495Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"3P2D"}],"region_id":"DP04163r002","sequence_construct":"MGEKPGTRVFKKSSPNCKLTVYLGKRDFVDHLDKVDPVDGVVLVDPDYLKDRKVFVTLTCAFRYGREDLDVLGLSFRKDLFIANYQAFPPTPNPPRPPTRLQERLLRKLGQHAHPFFFTIPQNLPCSVTLQPGPEDTGKACGVDFEIRAFCAKSLEEKSHKRNSVRLVIRKVQFAPEKPGPQPSAETTRHFLMSDRSLHLEASLDKELYYHGEPLNVNVHVTNNSTKTVKKIKVSVRQYADICLFSTAQYKCPVAQVEQDDQVSPSSTFCKVYTITPLLSNNREKRGLALDGKLKHEDTNLASSTIVKEGANKEVLGILVSYRVKVKLVVSRGGDVSVELPFVLMHPKPHDHIALPRPQSAAPETDAPVDTNLIEFETNYATDDDIVFEDFAR","statement":[{"text":"The carboxy terminus folds back toward the N-terminal domain, becomes unstructured for ~35 residues and forms a highly conserved tripartite interaction with the N-terminal domain consisting of two hydrophobic interactions with β-strand I and α-helix I and one buried ion pair constituting part of the main arrestin phosphate sensor, the polar core20; 28.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T07:23:41.673Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MGEKPGTRVFKKSSPNCKLTVYLGKRDFVDHLDKVDPVDGVVLVDPDYLKDRKVFVTLTCAFRYGREDLDVLGLSFRKDLFIANYQAFPPTPNPPRPPTRLQERLLRKLGQHAHPFFFTIPQNLPCSVTLQPGPEDTGKACGVDFEIRAFCAKSLEEKSHKRNSVRLVIRKVQFAPEKPGPQPSAETTRHFLMSDRSLHLEASLDKELYYHGEPLNVNVHVTNNSTKTVKKIKVSVRQYADICLFSTAQYKCPVAQVEQDDQVSPSSTFCKVYTITPLLSNNREKRGLALDGKLKHEDTNLASSTIVKEGANKEVLGILVSYRVKVKLVVSRGGDVSVELPFVLMHPKPHDHIALPRPQSAAPETDAPVDTNLIEFETNYATDDDIVFEDFARLRLKGLKDEDYDDQFC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"disorder_content":0.1100244498777506,"disprot_consensus":{"full":[{"start":349,"end":393,"type":"D"}],"Structural state":[{"start":349,"end":393,"type":"D"}]}},{"disprot_id":"DP04164","acc":"O94885","creator":"rpancsa","date":"2024-02-28T22:59:16.817Z","features":{"pfam":[{"id":"PF00536","name":"SAM domain (Sterile alpha motif)","start":635,"end":693},{"id":"PF07647","name":"SAM domain (Sterile alpha motif)","start":1179,"end":1238},{"id":"PF07653","name":"Variant SH3 domain","start":558,"end":610},{"id":"PF12485","name":"SLy Proteins Associated Disordered Region","start":401,"end":555},{"id":"PF26285","name":"SASH1 homeodomain-like domain","start":53,"end":92},{"id":"PF26285","name":"SASH1 homeodomain-like domain","start":1093,"end":1162}],"gene3D":[]},"genes":[{"name":{"value":"SASH1"},"synonyms":[{"value":"KIAA0790"},{"value":"PEPE1"}]}],"length":1247,"name":"SAM and SH3 domain-containing protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":396,"end":564,"reference_id":"37155029","reference_source":"pmid","reference_html":"Solution NMR backbone assignment of the SASH1 SLy proteins associated disordered region (SPIDER). <i> Clements CM, Vögeli B, Shellman YG, Henen MA. </i> Biomol NMR Assign, 2023","date":"2024-02-28T23:07:49.191Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":5,"statements":[{"type":"Article","text":"The spectra were recorded on BRUKER Avance NEO 600 MHz triple-resonance cryoprobe spectrometers at 5 °C."}]}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser519Asn","start":null,"end":null,"position":null,"statements":[{"type":"Figure","text":"Deuteration combined with 3D TROSY and HNN experiments allowed for the assignment of 97.4% of the S519N variant of SPIDER."},{"type":"Article","text":"The construct which has a substitution at position 519 (S519N) was cloned into the expression vector pET-28a(+) with an N-terminal His-tag coupled to a thrombin cleavage site."}]}],"cross_refs":[{"db":"BMRB","id":"51747"}],"region_id":"DP04164r001","statement":[{"text":"The 1H-15N HSQC of the SPIDER showed a narrow dispersion of peaks characteristic of a disordered protein (Fig. 3), confirming the prediction.","type":"Article"},{"text":"We designed a construct that comprises residues 396–564 in SASH1.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T07:22:42.362Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MEDAGAAGPGPEPEPEPEPEPEPAPEPEPEPKPGAGTSEAFSRLWTDVMGILDGSLGNIDDLAQQYADYYNTCFSDVCERMEELRKRRVSQDLEVEKPDASPTSLQLRSQIEESLGFCSAVSTPEVERKNPLHKSNSEDSSVGKGDWKKKNKYFWQNFRKNQKGIMRQTSKGEDVGYVASEITMSDEERIQLMMMVKEKMITIEEALARLKEYEAQHRQSAALDPADWPDGSYPTFDGSSNCNSREQSDDETEESVKFKRLHKLVNSTRRVRKKLIRVEEMKKPSTEGGEEHVFENSPVLDERSALYSGVHKKPLFFDGSPEKPPEDDSDSLTTSPSSSSLDTWGAGRKLVKTFSKGESRGLIKPPKKMGTFFSYPEEEKAQKVSRSLTEGEMKKGLGSLSHGRTCSFGGFDLTNRSLHVGSNNSDPMGKEGDFVYKEVIKSPTASRISLGKKVKSVKETMRKRMSKKYSSSVSEQDSGLDGMPGSPPPSQPDPEHLDKPKLKAGGSVESLRSSLSGQSSMSGQTVSTTDSSTSNRESVKSEDGDDEEPPYRGPFCGRARVHTDFTPSPYDTDSLKLKKGDIIDIISKPPMGTWMGLLNNKVGTFKFIYVDVLSEDEEKPKRPTRRRRKGRPPQPKSVEDLLDRINLKEHMPTFLFNGYEDLDTFKLLEEEDLDELNIRDPEHRAVLLTAVELLQEYDSNSDQSGSQEKLLVDSQGLSGCSPRDSGCYESSENLENGKTRKASLLSAKSSTEPSLKSFSRNQLGNYPTLPLMKSGDALKQGQEEGRLGGGLAPDTSKSCDPPGVTGLNKNRRSLPVSICRSCETLEGPQTVDTWPRSHSLDDLQVEPGAEQDVPTEVTEPPPQIVPEVPQKTTASSTKAQPLEQDSAVDNALLLTQSKRFSEPQKLTTKKLEGSIAASGRGLSPPQCLPRNYDAQPPGAKHGLARTPLEGHRKGHEFEGTHHPLGTKEGVDAEQRMQPKIPSQPPPVPAKKSRERLANGLHPVPMGPSGALPSPDAPCLPVKRGSPASPTSPSDCPPALAPRPLSGQAPGSPPSTRPPPWLSELPENTSLQEHGVKLGPALTRKVSCARGVDLETLTENKLHAEGIDLTEEPYSDKHGRCGIPEALVQRYAEDLDQPERDVAANMDQIRVKQLRKQHRMAIPSGGLTEICRKPVSPGCISSVSDWLISIGLPMYAGTLSTAGFSTLSQVPSLSHTCLQEAGITEERHIRKLLSAARLFKLPPGPEAM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.6511627906976745,"disorder_content":0.13552526062550121,"disprot_consensus":{"full":[{"start":396,"end":564,"type":"D"}],"Structural state":[{"start":396,"end":564,"type":"D"}]}},{"disprot_id":"DP04165","acc":"E7CC86","creator":"rpancsa","date":"2024-02-28T23:29:41.955Z","features":{"pfam":[{"id":"PF01395","name":"PBP/GOBP family","start":25,"end":141}],"gene3D":[]},"genes":[{"name":{"value":"PBP3","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ADT78492.1","url":"https://www.ebi.ac.uk/ena/browser/view/ADT78492.1"}}]},"synonyms":[{"value":"OnubPBP3","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BBB15971.1","url":"https://www.ebi.ac.uk/ena/browser/view/BBB15971.1"}}]}]}],"length":166,"name":"Pheromone binding protein 3","ncbi_taxon_id":29057,"organism":"Ostrinia nubilalis","regions":[{"start":147,"end":166,"reference_id":"37498448","reference_source":"pmid","reference_html":"Backbone and side chain NMR assignments and secondary structure calculation of the pheromone binding protein3 of Ostrinia nubilalis, an agricultural pest. <i> Al-Danoon O, Mohanty S. </i> Biomol NMR Assign, 2023","date":"2024-02-28T23:37:42.328Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":35,"statements":[{"type":"Figure","text":"2D [1H, 15N]-HSQC spectrum of uniformly 15N,13C-enriched OnubPBP3 in 50 mM phosphate buffer, 1 mM EDTA, 0.01% sodium azide at pH 6.5 and temperature 35 °C on a Bruker Avance 800 MHz spectrometer fitted with a cryo-probe."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":6.5,"statements":[{"type":"Figure","text":"2D [1H, 15N]-HSQC spectrum of uniformly 15N,13C-enriched OnubPBP3 in 50 mM phosphate buffer, 1 mM EDTA, 0.01% sodium azide at pH 6.5 and temperature 35 °C on a Bruker Avance 800 MHz spectrometer fitted with a cryo-probe."}]}],"cross_refs":[{"db":"BMRB","id":"51937"}],"region_id":"DP04165r001","statement":[{"text":"The deviations of the Cα and Cβ chemical shifts (Δδ) from the mean random-coil values were calculated and the difference ΔδCα – ΔδCβ was plotted against the OnubPBP3 sequence to obtain the secondary structural information in the protein (Fig. 3). This plot shows that OnubPBP3 contained seven α-helices starting with the N-terminus as the first helix. The C-terminus of the protein was predicted to be unstructured.","type":"Article"},{"text":"Based on TALOS + calculations, the secondary structural elements in OnubPBP3 consist of six helices: 3–22, 27–34, 46–58, 71–79, 84–96, 108–124. The C-terminus of OnubPBP3 is unstructured, in stark contrast to the well-formed helix of the C-terminus of OfurPBP2.","type":"Article"},{"text":"The measured construct is the uniprot protein without the N-terminal 22 aa long signal peptide. The last helical amino acid mentioned (position 124) is therefore equivalent to UniProt position 146 and the disordered tail starts from the next residue (147-166).","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T07:22:04.729Z"}},{"start":147,"end":166,"reference_id":"37498448","reference_source":"pmid","reference_html":"Backbone and side chain NMR assignments and secondary structure calculation of the pheromone binding protein3 of Ostrinia nubilalis, an agricultural pest. <i> Al-Danoon O, Mohanty S. </i> Biomol NMR Assign, 2023","date":"2024-02-28T23:38:16.819Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":35,"statements":[{"type":"Figure","text":"2D [1H, 15N]-HSQC spectrum of uniformly 15N,13C-enriched OnubPBP3 in 50 mM phosphate buffer, 1 mM EDTA, 0.01% sodium azide at pH 6.5 and temperature 35 °C on a Bruker Avance 800 MHz spectrometer fitted with a cryo-probe."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":6.5,"statements":[{"type":"Figure","text":"2D [1H, 15N]-HSQC spectrum of uniformly 15N,13C-enriched OnubPBP3 in 50 mM phosphate buffer, 1 mM EDTA, 0.01% sodium azide at pH 6.5 and temperature 35 °C on a Bruker Avance 800 MHz spectrometer fitted with a cryo-probe."}]}],"cross_refs":[{"db":"BMRB","id":"51937"}],"region_id":"DP04165r002","statement":[{"text":"The deviations of the Cα and Cβ chemical shifts (Δδ) from the mean random-coil values were calculated and the difference ΔδCα – ΔδCβ was plotted against the OnubPBP3 sequence to obtain the secondary structural information in the protein (Fig. 3). This plot shows that OnubPBP3 contained seven α-helices starting with the N-terminus as the first helix. The C-terminus of the protein was predicted to be unstructured.","type":"Article"},{"text":"Based on TALOS + calculations, the secondary structural elements in OnubPBP3 consist of six helices: 3–22, 27–34, 46–58, 71–79, 84–96, 108–124. The C-terminus of OnubPBP3 is unstructured, in stark contrast to the well-formed helix of the C-terminus of OfurPBP2.","type":"Article"},{"text":"The measured construct is the uniprot protein without the N-terminal 22 aa long signal peptide. The last helical amino acid mentioned (position 124) is therefore equivalent to UniProt position 146 and the disordered tail starts from the next residue (147-166).","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T07:22:06.945Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MWLPKTLVVMAVMSSMSVVVHSSQTVMREMTRNFIKAYEVCAKEYNLPEATGSELINFWKEGHELTTREAGCAILCMSTKLNLLDVQGSVHRGNTVEFAKHHGSDDAMAHQVVDILHACEKATPNEDKCMLALSIAMCFKAEIHKLDWAPNHELMFEELVSDMWNS","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Lepidoptera","Glossata","Ditrysia","Pyraloidea","Crambidae","Pyraustinae","Ostrinia"],"alphafold_very_low_content":0.012048192771084338,"disorder_content":0.12048192771084337,"disprot_consensus":{"full":[{"start":147,"end":166,"type":"D"}],"Structural state":[{"start":147,"end":166,"type":"D"}],"Disorder function":[{"start":147,"end":166,"type":"F"}]}},{"disprot_id":"DP04166","acc":"P56536","creator":"rpancsa","date":"2024-02-28T23:46:09.549Z","features":{"pfam":[{"id":"PF00225","name":"Kinesin motor domain","start":15,"end":327}],"gene3D":[]},"genes":[{"name":{"value":"Kif5c"},"synonyms":[{"value":"Nkhc2"}]}],"length":955,"name":"Kinesin heavy chain isoform 5C","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions":[{"start":325,"end":338,"reference_id":"37861970","reference_source":"pmid","reference_html":"Solution NMR assignments and structure for the dimeric kinesin neck domain. <i> Seo D, Kammerer RA, Alexandrescu AT. </i> Biomol NMR Assign, 2023","date":"2024-02-28T23:58:16.371Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":37,"statements":[{"type":"Article","text":"NMR experiments for assignments and structure determination used samples that had kinesin neck monomer concentrations between 0.5 and 1 mM, in 5 mM sodium phosphate, 150 mM NaCl, pH 6.1. Sample temperatures were 37 °C unless otherwise noted."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":6.1,"statements":[{"type":"Article","text":"NMR experiments for assignments and structure determination used samples that had kinesin neck monomer concentrations between 0.5 and 1 mM, in 5 mM sodium phosphate, 150 mM NaCl, pH 6.1. Sample temperatures were 37 °C unless otherwise noted."}]}],"cross_refs":[{"db":"BMRB","id":"52075"},{"db":"PDB","id":"8TT7"}],"region_id":"DP04166r001","statement":[{"text":"Information on the secondary structure of the kinesin neck fragment based on secondary chemical shifts and NOEs is summarized in Fig. 2A. The beginning of the neck linker is disordered but residues T330-L335 show β-strand propensity. The neck coiled coil runs between residues A339 and R371 (Fig. 2A) and shows a typical HN chemical shift periodicity (Kaplan et al. 2017), except for the connection between the first and second heptad (Fig. 2B) that has polar residues at the a and d heptad positions (Kozielski et al. 1997). By contrast, the linker region preceding the coiled coil has a two-residue periodicity suggestive of a β-strand conformation.","type":"Article"},{"text":"Figure 2D shows chemical shift-based S2 order parameters for the neck domain calculated with Talos-N (Shen and Bax 2015). Note the β-strand region in the linker forms an island of intermediate S2 values of ~ 0.7, suggesting that this segment is not completely disordered but separated from the coiled coil by a dynamic hinge.","type":"Article"},{"text":"The neck linker is disordered relative to the coiled coil (Figs. 2D and 3A) with no NOEs observed between the two segments. Nevertheless, the linker has a 3–6 residue segment of relatively well defined extended β-strand structure, lacking a distinct orientation relative to the coiled coil due to flexibility of the E336-A339 hinge connecting the two segments.","type":"Conclusion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T07:21:35.632Z"}},{"start":325,"end":338,"reference_id":"37861970","reference_source":"pmid","reference_html":"Solution NMR assignments and structure for the dimeric kinesin neck domain. <i> Seo D, Kammerer RA, Alexandrescu AT. </i> Biomol NMR Assign, 2023","date":"2024-02-29T00:01:44.024Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":37,"statements":[{"type":"Article","text":"NMR experiments for assignments and structure determination used samples that had kinesin neck monomer concentrations between 0.5 and 1 mM, in 5 mM sodium phosphate, 150 mM NaCl, pH 6.1. Sample temperatures were 37 °C unless otherwise noted."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":6.1,"statements":[{"type":"Article","text":"NMR experiments for assignments and structure determination used samples that had kinesin neck monomer concentrations between 0.5 and 1 mM, in 5 mM sodium phosphate, 150 mM NaCl, pH 6.1. Sample temperatures were 37 °C unless otherwise noted."}]}],"cross_refs":[{"db":"BMRB","id":"52075"},{"db":"PDB","id":"8TT7"}],"region_id":"DP04166r002","statement":[{"text":"Information on the secondary structure of the kinesin neck fragment based on secondary chemical shifts and NOEs is summarized in Fig. 2A. The beginning of the neck linker is disordered but residues T330-L335 show β-strand propensity. The neck coiled coil runs between residues A339 and R371 (Fig. 2A) and shows a typical HN chemical shift periodicity (Kaplan et al. 2017), except for the connection between the first and second heptad (Fig. 2B) that has polar residues at the a and d heptad positions (Kozielski et al. 1997). By contrast, the linker region preceding the coiled coil has a two-residue periodicity suggestive of a β-strand conformation.","type":"Article"},{"text":"Figure 2D shows chemical shift-based S2 order parameters for the neck domain calculated with Talos-N (Shen and Bax 2015). Note the β-strand region in the linker forms an island of intermediate S2 values of ~ 0.7, suggesting that this segment is not completely disordered but separated from the coiled coil by a dynamic hinge.","type":"Article"},{"text":"The neck linker is disordered relative to the coiled coil (Figs. 2D and 3A) with no NOEs observed between the two segments. Nevertheless, the linker has a 3–6 residue segment of relatively well defined extended β-strand structure, lacking a distinct orientation relative to the coiled coil due to flexibility of the E336-A339 hinge connecting the two segments.","type":"Conclusion"},{"text":"This disordered linker connects the head domain of dimeric kinesin (missing in this construct) and the neck coiled-coil region.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T07:21:47.840Z"}},{"start":325,"end":338,"reference_id":"37861970","reference_source":"pmid","reference_html":"Solution NMR assignments and structure for the dimeric kinesin neck domain. <i> Seo D, Kammerer RA, Alexandrescu AT. </i> Biomol NMR Assign, 2023","date":"2024-02-29T00:20:20.030Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006196","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":6.1,"statements":[{"type":"Article","text":"Figure 2 C summarizes hydrogen exchange (HX) data for the neck domain measured for a sample at pH* 6.1 and a temperature of 23 °C, using 1H-15N HSQC spectra recorded as a function of incubation time in D2O."}]},{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":23,"statements":[{"type":"Article","text":"Figure 2 C summarizes hydrogen exchange (HX) data for the neck domain measured for a sample at pH* 6.1 and a temperature of 23 °C, using 1H-15N HSQC spectra recorded as a function of incubation time in D2O."}]}],"cross_refs":[{"db":"BMRB","id":"52075"}],"region_id":"DP04166r003","statement":[{"text":"Figure 2 C summarizes hydrogen exchange (HX) data for the neck domain measured for a sample at pH* 6.1 and a temperature of 23 °C, using 1H-15N HSQC spectra recorded as a function of incubation time in D2O.","type":"Article"},{"text":"Figure 2C clearly shows that the neck linker is not protected from HD exchange.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-02-29T07:21:39.230Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MADPAECSIKVMCRFRPLNEAEILRGDKFIPKFKGEETVVIGQGKPYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPQLMGIIPRIAHDIFDHIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPYVKGCTERFVSSPEEVMDVIDEGKANRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLSGKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTKTHVPYRDSKMTRILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQRAKTIKNTVSVNLELTAEEWKKKYEKEKEKNKALKSVIQHLEVELNRWRNGEAVPEDEQISAKDQKNLEPCDNTPIIDNITPVVDGISAEKEKYDEEITSLYRQLDDKDDEINQQSQLAEKLKQQMLDQDELLASTRRDYEKIQEELTRLQIENEAAKDEVKEVLQALEELAVNYDQKSQEVEDKTRANEQLTDELAQKTTTLTTTQRELSQLQELSNHQKKRATEILNLLLKDLGEIGGIIGTNDVKTLADVNGVIEEEFTMARLYISKMKSEVKSLVNRSKQLESAQTDSNRKMNASERELAACQLLISQHEAKIKSLTDYMQNMEQKRRQLEESQDSLSEELAKLRAQEKMHEVSFQDKEKEHLTRLQDAEEVKKALEQQMESHREAHQKQLSRLRDEIEEKQRIIDEIRDLNQKLQLEQERLSSDYNKLKIEDQEREVKLEKLLLLNDKREQAREDLKGLEETVSRELQTLHNLRKLFVQDLTTRVKKSVELDSDDGGGSAAQKQKISFLENNLEQLTKVHKQLVRDNADLRCELPKLEKRLRATAERVKALESALKEAKENAMRDRKRYQQEVDRIKEAVRAKNMARRAHSAQIAKPIRPGHYPASSPTAVHAVRGGGGSSNSTHYQK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"alphafold_very_low_content":0.03347280334728033,"disorder_content":0.014659685863874346,"disprot_consensus":{"full":[{"start":325,"end":338,"type":"D"}],"Structural state":[{"start":325,"end":338,"type":"D"}],"Disorder function":[{"start":325,"end":338,"type":"F"}]}},{"disprot_id":"DP04167","acc":"Q8N6T7","creator":"vnugnes","date":"2024-03-01T14:12:46.665Z","features":{"pfam":[{"id":"PF02146","name":"Sir2 family","start":86,"end":221}],"gene3D":[]},"genes":[{"name":{"value":"SIRT6","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10873683","url":"http://www.ncbi.nlm.nih.gov/pubmed/10873683","alternativeUrl":"https://europepmc.org/abstract/MED/10873683"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:14934","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:14934"}}]},"synonyms":[{"value":"SIR2L6"}]}],"length":355,"name":"NAD-dependent protein deacylase sirtuin-6","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":284,"end":355,"reference_id":"38415718","reference_source":"pmid","reference_html":"Binding to nucleosome poises human SIRT6 for histone H3 deacetylation. <i> Smirnova E, Bignon E, Schultz P, Papai G, Ben Shem A. </i> Elife, 2024","date":"2024-03-01T15:47:33.490Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"8OF4"},{"db":"EMDB","id":"16845"}],"region_id":"DP04167r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62799"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02281"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06897"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84233"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"Widom-601 145 bp DNA was produced using a plasmid harboring 16 copies of this sequence as described by Dyer et al., 2004."},{"type":"Curator statement","text":"Interacting dsDNA with sequence ATCAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGACAGCTCTAGCACCGCTTAAACGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGGATTACTCCCTAGTCTCCAGGCACGTGTCAGATATATACATCGAT."}]}],"statement":[{"text":"A biochemical study suggests that the intrinsically disordered C-terminal domain of SIRT6 is necessary for establishing tight interaction of SIRT6 with the nucleosome (Liu et al., 2020) via its ability to bind DNA.","type":"Results"},{"text":"The cryo EM structure of the Nucleosome Bound SIRT6 shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-04T09:11:35.075Z"}},{"start":1,"end":25,"reference_id":"38415718","reference_source":"pmid","reference_html":"Binding to nucleosome poises human SIRT6 for histone H3 deacetylation. <i> Smirnova E, Bignon E, Schultz P, Papai G, Ben Shem A. </i> Elife, 2024","date":"2024-03-01T15:47:59.927Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"8OF4"},{"db":"EMDB","id":"16845"}],"region_id":"DP04167r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62799"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02281"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06897"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84233"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"Widom-601 145 bp DNA was produced using a plasmid harboring 16 copies of this sequence as described by Dyer et al., 2004."},{"type":"Curator statement","text":"Interacting dsDNA with sequence ATCAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGACAGCTCTAGCACCGCTTAAACGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGGATTACTCCCTAGTCTCCAGGCACGTGTCAGATATATACATCGAT."}]}],"statement":[{"text":"The cryo EM structure of the Nucleosome Bound SIRT6 shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-04T09:11:37.217Z"}},{"start":62,"end":84,"reference_id":"38415718","reference_source":"pmid","reference_html":"Binding to nucleosome poises human SIRT6 for histone H3 deacetylation. <i> Smirnova E, Bignon E, Schultz P, Papai G, Ben Shem A. </i> Elife, 2024","date":"2024-03-01T15:48:20.930Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"8OF4"},{"db":"EMDB","id":"16845"}],"region_id":"DP04167r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62799"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02281"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06897"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84233"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"Widom-601 145 bp DNA was produced using a plasmid harboring 16 copies of this sequence as described by Dyer et al., 2004."},{"type":"Curator statement","text":"Interacting dsDNA with sequence ATCAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGACAGCTCTAGCACCGCTTAAACGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGGATTACTCCCTAGTCTCCAGGCACGTGTCAGATATATACATCGAT."}]}],"statement":[{"text":"The cryo EM structure of the Nucleosome Bound SIRT6 shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-04T09:11:40.108Z"}},{"start":293,"end":355,"reference_id":"33067423","reference_source":"pmid","reference_html":"Multivalent interactions drive nucleosome binding and efficient chromatin deacetylation by SIRT6. <i> Liu WH, Zheng J, Feldman JL, Klein MA, Kuznetsov VI, Peterson CL, Griffin PR, Denu JM. </i> Nat Commun, 2020","date":"2024-03-01T16:27:06.781Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031491","term_name":"nucleosome binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Pro293Ser355del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04167r004","statement":[{"text":"Thus, we introduced truncations of varying lengths at the C-terminus and evaluated these variants for nucleosome binding (Fig. 3b). The C-terminal deletion mutants exclusively formed 2:1 SIRT6:NCP complexes in the native gel without a detectable 1:1 intermediate, suggesting that the high affinity site was compromised, which led to a similar affinity for both binding events. As a result, the overall KD of SIRT6(1–292) and SIRT6(1–301) (KD = 254 and 139 nM, respectively) to nucleosomes is an order of magnitude weaker than full-length SIRT6 (Fig. 3c, Supplementary Fig. 4b, and Table 1). Thus, the C-terminally truncated mutants display impaired binding to NCPs, as well as a loss of the asymmetric binding mechanism.","type":"Results"},{"text":"The CTD of SIRT6 is required for high-affinity binding","type":"Results"},{"text":"Under this model, binding to the lower affinity site (KD(Low)) would be similar between SIRT6 and SIRT6(1–292). To test this mechanism, we first saturated the high affinity site on NCPs with 10 nM full-length SIRT6, then added increasing concentrations of SIRT6(1–292) and subjected the resulting complexes to native gel analysis (Fig. 3d and Table 1). The data revealed a dissociation constant (40 nM) similar to the KD(Low) value reported by the FRET experiment (Fig. 1e), supporting a model in which the CTD contributes to only the higher affinity binding event.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a nucleosome, a complex comprised of DNA wound around a multisubunit core and associated proteins, which forms the primary packing unit of DNA into higher order structures.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A310TM08"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06897"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A1L8EMY5"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62799"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"Recombinant nucleosomes with 601-positioning 147-bp DNA and x. laevis histones were reconstituted using the salt gradient dialysis method, in which equimolar histone octamers and DNA were slowly dialyzed from 2 M NaCl to 10 mM NaCl58."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-04T09:11:45.115Z"}},{"start":330,"end":348,"reference_id":"33067423","reference_source":"pmid","reference_html":"Multivalent interactions drive nucleosome binding and efficient chromatin deacetylation by SIRT6. <i> Liu WH, Zheng J, Feldman JL, Klein MA, Kuznetsov VI, Peterson CL, Griffin PR, Denu JM. </i> Nat Commun, 2020","date":"2024-03-01T16:33:25.992Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031491","term_name":"nucleosome binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000314","ec_ontology":"ECO","ec_name":"direct assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","region_id":"DP04167r005","statement":[{"text":"To further interrogate this mechanism, we used an antibody raised against SIRT6 C-terminal residues 330–348 as a probe in EMSA experiments. The antibody was allowed to bind full-length SIRT6 before nucleosome addition (Supplementary Fig. 4c). When only the 1:1 SIRT6:NCP complex is apparent at 20 nM SIRT6, the antibody fully disrupted this complex (lanes 3 and 4). When both the 1:1 and 2:1 complexes appeared at 100 nM SIRT6, the antibody displaced part of the bound population while supershifting the rest (lanes 5 and 6). Finally, when both binding sites were saturated, only supershifting occurred, likely due to CTD-independent interactions driving binding at higher SIRT6 concentrations (lanes 8 and 9). Collectively, the results are consistent with the observation that the CTD is not necessary for complete SIRT6:NCP assembly (Fig. 3b), yet is essential for tight and multivalent binding at a single, high affinity site.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a nucleosome, a complex comprised of DNA wound around a multisubunit core and associated proteins, which forms the primary packing unit of DNA into higher order structures.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A310TM08"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06897"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A1L8EMY5"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62799"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"Recombinant nucleosomes with 601-positioning 147-bp DNA and x. laevis histones were reconstituted using the salt gradient dialysis method, in which equimolar histone octamers and DNA were slowly dialyzed from 2 M NaCl to 10 mM NaCl58."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-04T09:11:52.915Z"}},{"start":293,"end":355,"reference_id":"33067423","reference_source":"pmid","reference_html":"Multivalent interactions drive nucleosome binding and efficient chromatin deacetylation by SIRT6. <i> Liu WH, Zheng J, Feldman JL, Klein MA, Kuznetsov VI, Peterson CL, Griffin PR, Denu JM. </i> Nat Commun, 2020","date":"2024-03-01T16:36:29.669Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Pro293Ser355del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04167r006","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"Recombinant nucleosomes with 601-positioning 147-bp DNA and x. laevis histones were reconstituted using the salt gradient dialysis method, in which equimolar histone octamers and DNA were slowly dialyzed from 2 M NaCl to 10 mM NaCl58."}]}],"statement":[{"text":"In EMSA experiments using 500 nM protein incubated with the 601-positioning DNA sequence, full-length SIRT6 displayed highest affinity for DNA, while the mutants bound noticeably weaker (Fig. 4a).","type":"Results"},{"text":"The CTD is an intrinsically disordered DNA-binding domain","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-04T09:11:54.523Z"}},{"start":270,"end":355,"reference_id":"33067423","reference_source":"pmid","reference_html":"Multivalent interactions drive nucleosome binding and efficient chromatin deacetylation by SIRT6. <i> Liu WH, Zheng J, Feldman JL, Klein MA, Kuznetsov VI, Peterson CL, Griffin PR, Denu JM. </i> Nat Commun, 2020","date":"2024-03-01T16:37:01.541Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04167r007","statement":[{"text":"To confirm that the CTD directly interacts with DNA, we expressed and purified the isolated domain (residues 270–355) and evaluated DNA binding capacity (Supplementary Fig. 1a).","type":"Results"},{"text":"To confirm these predictions, we determined the 1H NMR spectrum of the CTD and observed peak clustering at ~7.0–8.5 ppm, which is characteristic of intrinsically disordered domains (Fig. 4b).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-04T09:11:42.140Z"}},{"start":270,"end":355,"reference_id":"33067423","reference_source":"pmid","reference_html":"Multivalent interactions drive nucleosome binding and efficient chromatin deacetylation by SIRT6. <i> Liu WH, Zheng J, Feldman JL, Klein MA, Kuznetsov VI, Peterson CL, Griffin PR, Denu JM. </i> Nat Commun, 2020","date":"2024-03-01T16:38:23.467Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","region_id":"DP04167r008","statement":[{"text":"In EMSA experiments, we found that the CTD bound random sequences of DNA in a commercial 10 base pair ladder, as well as the 601-positioning sequence (Fig. 4c and Supplementary Fig. 5c). More strikingly, binding to the latter sequence with and without the histone octamer assembled on it produced exact binding isotherms. This reveals that the CTD is not only indiscriminate of DNA sequences, but recognizes both linear DNA as well as the curved, distorted DNA inherent in nucleosomes.","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-04T09:11:59.102Z"}},{"start":270,"end":355,"reference_id":"33067423","reference_source":"pmid","reference_html":"Multivalent interactions drive nucleosome binding and efficient chromatin deacetylation by SIRT6. <i> Liu WH, Zheng J, Feldman JL, Klein MA, Kuznetsov VI, Peterson CL, Griffin PR, Denu JM. </i> Nat Commun, 2020","date":"2024-03-01T16:50:50.851Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0032129","term_name":"histone deacetylase activity (H3-K9 specific)","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001272","ec_ontology":"ECO","ec_name":"high-performance liquid chromatography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P68431","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04167r009","statement":[{"text":"Our binding studies above predict that full-length SIRT6 would be a more efficient enzyme than a counterpart without the CTD. Indeed, when provided with MNase-digested nucleosomes as substrate, the full-length enzyme efficiently deacetylated endogenous H3K9ac, while SIRT6(1–292) and SIRT6(1–301) deacetylated the modification much slower (Fig. 5b and Supplementary Fig. 6a). Therefore, efficient chromatin deacetylation requires the CTD-dependent nucleosome-binding mechanism.","type":"Results"},{"text":"The CTD promotes efficient chromatin deacetylation by SIRT6","type":"Results"}],"term_comment":"","term_def":"\"Catalysis of the reaction: histone H3 N6-acetyl-L-lysine (position 9) + H2O = histone H3 L-lysine (position 9) + acetate. This reaction represents the removal of an acetyl group from lysine at position 9 of the histone H3 protein.\" [PMID:28450737]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-04T09:12:00.683Z"}},{"start":293,"end":344,"reference_id":"33067423","reference_source":"pmid","reference_html":"Multivalent interactions drive nucleosome binding and efficient chromatin deacetylation by SIRT6. <i> Liu WH, Zheng J, Feldman JL, Klein MA, Kuznetsov VI, Peterson CL, Griffin PR, Denu JM. </i> Nat Commun, 2020","date":"2024-03-01T16:55:53.643Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003682","term_name":"chromatin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Pro293Pro344del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Because the nuclear localization motif is among the last 11 amino acids, these residues were retained in the truncated proteins (SIRT6Δ293–344 and SIRT6Δ302–344)19."}]}],"ec_go":"IMP","region_id":"DP04167r010","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0291","entry_name":"HCT116wt"}],"statement":[{"text":"To analyze the sub-cellular distribution of the SIRT6 constructs, we fractionated HCT116 cells into cytoplasmic and nucleoplasmic fractions. Compared to wild-type SIRT6, SIRT6Δ293–344 and SIRT6Δ302–344 levels were higher in both fractions (Supplementary Fig. 6b), suggesting that truncating the CTD led to weakened chromatin association.","type":"Results"}],"term_comment":"","term_def":"\"Binding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.\" [GOC:jl, ISBN:0198506732, PMID:20404130]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-04T09:12:02.416Z"}},{"start":270,"end":355,"reference_id":"33067423","reference_source":"pmid","reference_html":"Multivalent interactions drive nucleosome binding and efficient chromatin deacetylation by SIRT6. <i> Liu WH, Zheng J, Feldman JL, Klein MA, Kuznetsov VI, Peterson CL, Griffin PR, Denu JM. </i> Nat Commun, 2020","date":"2024-03-01T17:01:53.042Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031492","term_name":"nucleosomal DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","region_id":"DP04167r011","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62799"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A1L8EMY5"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06897"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A310TM08"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":"","statements":[{"type":"Methods","text":"Recombinant nucleosomes with 601-positioning 147-bp DNA and x. laevis histones were reconstituted using the salt gradient dialysis method, in which equimolar histone octamers and DNA were slowly dialyzed from 2 M NaCl to 10 mM NaCl58."}]}],"statement":[{"text":"In EMSA experiments, we found that the CTD bound random sequences of DNA in a commercial 10 base pair ladder, as well as the 601-positioning sequence (Fig. 4c and Supplementary Fig. 5c). More strikingly, binding to the latter sequence with and without the histone octamer assembled on it produced exact binding isotherms. This reveals that the CTD is not only indiscriminate of DNA sequences, but recognizes both linear DNA as well as the curved, distorted DNA inherent in nucleosomes.","type":"Results"}],"term_comment":"","term_def":"\"Binding to the DNA portion of a nucleosome.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-04T09:12:03.665Z"}},{"start":290,"end":355,"reference_id":"20117128","reference_source":"pmid","reference_html":"Functional dissection of SIRT6: identification of domains that regulate histone deacetylase activity and chromatin localization. <i> Tennen RI, Berber E, Chua KF. </i> Mech Ageing Dev, 2010","date":"2024-03-01T17:20:03.668Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006606","term_name":"protein import into nucleus","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Pro290Ser355del","start":null,"end":null,"position":null},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IMP","region_id":"DP04167r012","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"Conversely, progressive deletion of the CTE of SIRT6 (ΔC2 and ΔC) resulted in a partial or dramatic mislocalization of SIRT6 from the nucleus to the cytoplasm (Figure 2B).","type":"Results"},{"text":"The ΔC2 construct comprises the region 1-289 and ΔC the 1-276 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"The directed movement of a protein from the cytoplasm to the nucleus.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-04T09:12:05.632Z"}},{"start":345,"end":351,"reference_id":"20117128","reference_source":"pmid","reference_html":"Functional dissection of SIRT6: identification of domains that regulate histone deacetylase activity and chromatin localization. <i> Tennen RI, Berber E, Chua KF. </i> Mech Ageing Dev, 2010","date":"2024-03-01T17:19:46.658Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006606","term_name":"protein import into nucleus","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys346Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg347Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys349Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys351Ala","start":null,"end":null,"position":null},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IMP","region_id":"DP04167r013","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"Inspection of the C-terminal sequence of SIRT6 identified a seven-amino acid sequence starting at residue 345—345PKRVKAK351—that resembles a canonical nuclear localization signal (NLS). We mutated the four basic residues (K346, R347, K349, K351) of this putative NLS to alanine in the context of the full-length protein (to generate SIRT6-mutNLS) and examined its localization. GFP-tagged SIRT6-mutNLS was partially mislocalized to the cytoplasm (Figure 2B), and this pattern was indistinguishable from that generated by deleting ∼80 amino acids of the C terminus (ΔC2). These data suggest that the 345PKRVKAK351 sequence at the C terminus of SIRT6 is an NLS essential for proper nuclear localization.","type":"Results"},{"text":"The ΔC2 construct comprises the region 1-289 and ΔC the 1-276 region.","type":"Curator statement"}],"term_comment":"","term_def":"\"The directed movement of a protein from the cytoplasm to the nucleus.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-04T09:12:07.005Z"}},{"start":272,"end":355,"reference_id":"20117128","reference_source":"pmid","reference_html":"Functional dissection of SIRT6: identification of domains that regulate histone deacetylase activity and chromatin localization. <i> Tennen RI, Berber E, Chua KF. </i> Mech Ageing Dev, 2010","date":"2024-03-01T17:21:54.383Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006606","term_name":"protein import into nucleus","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IDA","region_id":"DP04167r014","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"Finally, we analyzed the cellular localization of the isolated CTE and NTE sequences of SIRT6 fused to GFP. The CTE (and Δcore) were sufficient to direct nuclear localization of GFP, generating a pattern indistinguishable from that of full-length SIRT6 fused to GFP (Figure 2C). In contrast, the localization pattern of the NTE was indistinguishable from that of GFP alone (Figure 2C).","type":"Results"},{"text":"The CTE construct comprises the region 272-355.","type":"Curator statement"}],"term_comment":"","term_def":"\"The directed movement of a protein from the cytoplasm to the nucleus.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-03-04T09:12:08.778Z"}}],"regions_counter":14,"released":"2024_06","sequence":"MSVNYAAGLSPYADKGKCGLPEIFDPPEELERKVWELARLVWQSSSVVFHTGAGISTASGIPDFRGPHGVWTMEERGLAPKFDTTFESARPTQTHMALVQLERVGLLRFLVSQNVDGLHVRSGFPRDKLAELHGNMFVEECAKCKTQYVRDTVVGTMGLKATGRLCTVAKARGLRACRGELRDTILDWEDSLPDRDLALADEASRNADLSITLGTSLQIRPSGNLPLATKRRGGRLVIVNLQPTKHDRHADLRIHGYVDEVMTRLMKHLGLEIPAWDGPRVLERALPPLPRPPTPKLEPKEESPTRINGSIPAGPKQEPCAQHNGSEPASPKRERPTSPAPHRPPKRVKAKAVPS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.14084507042253522,"disorder_content":0.37746478873239436,"disprot_consensus":{"full":[{"start":1,"end":25,"type":"D"},{"start":62,"end":84,"type":"D"},{"start":270,"end":355,"type":"D"}],"Structural state":[{"start":1,"end":25,"type":"D"},{"start":62,"end":84,"type":"D"},{"start":270,"end":355,"type":"D"}],"Molecular function":[{"start":270,"end":355,"type":"F"}],"Biological process":[{"start":272,"end":355,"type":"F"}]}},{"disprot_id":"DP04169","acc":"O00499","creator":"ldobson","date":"2024-03-18T12:43:53.020Z","features":{"pfam":[{"id":"PF03114","name":"BAR domain","start":19,"end":264},{"id":"PF14604","name":"Variant SH3 domain","start":527,"end":590}],"gene3D":[]},"genes":[{"name":{"value":"BIN1"},"synonyms":[{"value":"AMPHL"}]}],"length":593,"name":"Myc box-dependent-interacting protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":41,"reference_id":"17059209","reference_source":"pmid","reference_html":"The crystal structure of the BAR domain from human Bin1/amphiphysin II and its implications for molecular recognition. <i> Casal E, Federici L, Zhang W, Fernandez-Recio J, Priego EM, Miguel RN, DuHadaway JB, Prendergast GC, Luisi BF, Laue ED. </i> Biochemistry, 2006","date":"2024-03-18T12:53:35.216Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"2FIC"}],"region_id":"DP04169r001","statement":[{"text":"Missing residues from PDB structure 2FIC.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-18T15:42:04.488Z"}},{"start":12,"end":30,"reference_id":"18658220","reference_source":"pmid","reference_html":"Structure and dynamics of helix-0 of the N-BAR domain in lipid micelles and bilayers. <i> Löw C, Weininger U, Lee H, Schweimer K, Neundorf I, Beck-Sickinger AG, Pastor RW, Balbach J. </i> Biophys J, 2008","date":"2024-03-18T12:56:21.800Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"2RND"},{"db":"PDB","id":"2RMY"}],"ec_go":"EXP","region_id":"DP04169r002","statement":[{"text":"The micelle environment generally stabilizes the helix, leading to a range of α-helicities of 40 to 50% (SDS1: 48%; SDS3: 50%; DPC: 40%) for residues 12–30 during the final simulated 20 ns.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-03-18T15:44:40.811Z"}},{"start":1,"end":33,"reference_id":"18658220","reference_source":"pmid","reference_html":"Structure and dynamics of helix-0 of the N-BAR domain in lipid micelles and bilayers. <i> Löw C, Weininger U, Lee H, Schweimer K, Neundorf I, Beck-Sickinger AG, Pastor RW, Balbach J. </i> Biophys J, 2008","date":"2024-03-18T15:48:23.019Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04169r003","statement":[{"text":"The isolated N-BAR peptide is unstructured in aqueous solution (Fig. 1 b, solid black line).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T08:24:07.097Z"}},{"start":1,"end":33,"reference_id":"18658220","reference_source":"pmid","reference_html":"Structure and dynamics of helix-0 of the N-BAR domain in lipid micelles and bilayers. <i> Löw C, Weininger U, Lee H, Schweimer K, Neundorf I, Beck-Sickinger AG, Pastor RW, Balbach J. </i> Biophys J, 2008","date":"2024-03-19T14:04:48.581Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04169r004","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"78018","entry_name":"dodecylphosphocholine"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"8984","entry_name":"sodium dodecyl sulfate"}],"statement":[{"text":"The isolated N-BAR peptide is unstructured in aqueous solution (Fig. 1 b, solid black line). As in the full-length protein, the ellipticity minima at 208 and 222 nm indicate that the peptide takes on a helical structure when bound to liposomes or micelles. The CD spectra of the N-BAR peptide in brain lipid liposomes or DPC or SDS micelles are virtually identical, indicating a similar secondary structure under these conditions (Fig. 1 b).","type":"Results"},{"text":"In the presence of liposomes (dashed dark gray line), SDS (solid gray line) or DPC (black dashed line) micelles, the peptide becomes structured.","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T08:24:15.739Z"}},{"start":1,"end":33,"reference_id":"18658220","reference_source":"pmid","reference_html":"Structure and dynamics of helix-0 of the N-BAR domain in lipid micelles and bilayers. <i> Löw C, Weininger U, Lee H, Schweimer K, Neundorf I, Beck-Sickinger AG, Pastor RW, Balbach J. </i> Biophys J, 2008","date":"2024-03-19T14:15:10.160Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"78018","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04169r005","statement":[{"text":"The isolated N-BAR peptide is unstructured in aqueous solution (Fig. 1 b, solid black line). As in the full-length protein, the ellipticity minima at 208 and 222 nm indicate that the peptide takes on a helical structure when bound to liposomes or micelles. The CD spectra of the N-BAR peptide in brain lipid liposomes or DPC or SDS micelles are virtually identical, indicating a similar secondary structure under these conditions (Fig. 1 b).","type":"Results"},{"text":"In the presence of liposomes (dashed dark gray line), SDS (solid gray line) or DPC (black dashed line) micelles, the peptide becomes structured.","type":"Figure"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T08:24:33.023Z"}},{"start":1,"end":33,"reference_id":"18658220","reference_source":"pmid","reference_html":"Structure and dynamics of helix-0 of the N-BAR domain in lipid micelles and bilayers. <i> Löw C, Weininger U, Lee H, Schweimer K, Neundorf I, Beck-Sickinger AG, Pastor RW, Balbach J. </i> Biophys J, 2008","date":"2024-03-19T14:17:34.334Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04169r006","statement":[{"text":"Binding of the N-BAR peptide to micelles results in a deviation of the backbone and, more obviously, the side-chain resonances in the 15N-HSQC spectrum (Fig. 2 b) from the random coil chemical shifts dominating the spectrum in aqueous solution (Fig. 2 a).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T08:24:09.318Z"}},{"start":8,"end":33,"reference_id":"18658220","reference_source":"pmid","reference_html":"Structure and dynamics of helix-0 of the N-BAR domain in lipid micelles and bilayers. <i> Löw C, Weininger U, Lee H, Schweimer K, Neundorf I, Beck-Sickinger AG, Pastor RW, Balbach J. </i> Biophys J, 2008","date":"2024-03-19T14:21:05.302Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04169r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"8984","entry_name":"sodium dodecyl sulfate"}],"statement":[{"text":"Binding of the N-BAR peptide to micelles results in a deviation of the backbone and, more obviously, the side-chain resonances in the 15N-HSQC spectrum (Fig. 2 b) from the random coil chemical shifts dominating the spectrum in aqueous solution (Fig. 2 a). This finding confirms the interaction of N-BAR with the micellar environment and the induction of a defined secondary structure in SDS or DPC observed by far-UV CD spectra.","type":"Results"},{"text":"Residues 8–34 in SDS and 10–34 in DPC micelles are well-ordered with a heavy atom root mean-square deviation < 1.1 Å.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T08:24:17.704Z"}},{"start":10,"end":33,"reference_id":"18658220","reference_source":"pmid","reference_html":"Structure and dynamics of helix-0 of the N-BAR domain in lipid micelles and bilayers. <i> Löw C, Weininger U, Lee H, Schweimer K, Neundorf I, Beck-Sickinger AG, Pastor RW, Balbach J. </i> Biophys J, 2008","date":"2024-03-19T14:21:36.991Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04169r008","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"78018","entry_name":"dodecylphosphocholine"}],"statement":[{"text":"Binding of the N-BAR peptide to micelles results in a deviation of the backbone and, more obviously, the side-chain resonances in the 15N-HSQC spectrum (Fig. 2 b) from the random coil chemical shifts dominating the spectrum in aqueous solution (Fig. 2 a). This finding confirms the interaction of N-BAR with the micellar environment and the induction of a defined secondary structure in SDS or DPC observed by far-UV CD spectra.","type":"Results"},{"text":" Residues 8–34 in SDS and 10–34 in DPC micelles are well-ordered with a heavy atom root mean-square deviation < 1.1 Å.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T08:24:25.300Z"}},{"start":1,"end":33,"reference_id":"18658220","reference_source":"pmid","reference_html":"Structure and dynamics of helix-0 of the N-BAR domain in lipid micelles and bilayers. <i> Löw C, Weininger U, Lee H, Schweimer K, Neundorf I, Beck-Sickinger AG, Pastor RW, Balbach J. </i> Biophys J, 2008","date":"2024-03-19T14:39:47.470Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0060988","term_name":"lipid tube assembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","region_id":"DP04169r009","statement":[{"text":"The human amphiphysin N-BAR domain can constrict liposomes into tubules but leads to vesiculation at higher protein concentrations (Fig. 8 b) (13). A deletion mutant lacking the N-terminal amphipathic helix (BAR) had much less influence on the liposome morphology (Fig. 8 c). In addition to extensive vesiculation, tube formation was observed for the N-BAR peptide (Fig. 8, d and e) and the extended 1–44 residue N-BAR peptide (Fig. 8 f).","type":"Results"}],"term_comment":"","term_def":"\"The aggregation, arrangement and bonding together of a set of macromolecules to form a macromolecular complex that contains a tube of lipid surrounded by a protein coat involved in membrane shaping of vesicle membranes as they fuse or undergo fission.\" [GOC:ascb_2009, GOC:dph, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T08:24:35.379Z"}},{"start":1,"end":33,"reference_id":"18658220","reference_source":"pmid","reference_html":"Structure and dynamics of helix-0 of the N-BAR domain in lipid micelles and bilayers. <i> Löw C, Weininger U, Lee H, Schweimer K, Neundorf I, Beck-Sickinger AG, Pastor RW, Balbach J. </i> Biophys J, 2008","date":"2024-03-19T14:40:56.183Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0061025","term_name":"membrane fusion","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","region_id":"DP04169r010","statement":[{"text":"FRET-based membrane fusion assays yield a more quantitative measure of the membrane fusion properties of the different BAR domain constructs. Liposomes were prepared with fluorescence-labeled lipids and subsequently mixed with unlabeled liposomes; fusion of labeled with unlabeled liposomes can be followed by the quench of the FRET signal concomitant with an increase of the donor fluorescence at 530 nm. Fig. 8, g and h, shows membrane fusion for the N-BAR domain and the N-BAR peptides but not for the BAR domain lacking helix-0.","type":"Results"}],"term_comment":"","term_def":"\"The membrane organization process that joins two lipid bilayers to form a single membrane.\" [GOC:dph, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T08:24:43.340Z"}},{"start":1,"end":33,"reference_id":"18658220","reference_source":"pmid","reference_html":"Structure and dynamics of helix-0 of the N-BAR domain in lipid micelles and bilayers. <i> Löw C, Weininger U, Lee H, Schweimer K, Neundorf I, Beck-Sickinger AG, Pastor RW, Balbach J. </i> Biophys J, 2008","date":"2024-03-19T14:44:50.885Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0097749","term_name":"membrane tubulation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04169r011","statement":[{"text":"The human amphiphysin N-BAR domain can constrict liposomes into tubules but leads to vesiculation at higher protein concentrations (Fig. 8 b) (13). A deletion mutant lacking the N-terminal amphipathic helix (BAR) had much less influence on the liposome morphology (Fig. 8 c). In addition to extensive vesiculation, tube formation was observed for the N-BAR peptide (Fig. 8, d and e) and the extended 1–44 residue N-BAR peptide (Fig. 8 f).","type":"Results"},{"text":"FRET-based membrane fusion assays yield a more quantitative measure of the membrane fusion properties of the different BAR domain constructs. Liposomes were prepared with fluorescence-labeled lipids and subsequently mixed with unlabeled liposomes; fusion of labeled with unlabeled liposomes can be followed by the quench of the FRET signal concomitant with an increase of the donor fluorescence at 530 nm. Fig. 8, g and h, shows membrane fusion for the N-BAR domain and the N-BAR peptides but not for the BAR domain lacking helix-0.","type":"Results"}],"term_comment":"","term_def":"\"A membrane organization process resulting in the formation of a tubular projection. This may face inwardly (as in tubular membrane invaginations) or outwardly (as in endosomal tubules).\" [GOC:pr]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T08:24:44.753Z"}}],"regions_counter":11,"released":"2024_06","sequence":"MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVYEPDWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKPVSLLEKAAPQWCQGKLQAHLVAQTNLLRNQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGLEKQHGSNTFTVKAQPSDNAPAKGNKSPSPPDGSPAATPEIRVNHEPEPAGGATPGATLPKSPSQLRKGPPVPPPPKHTPSKEVKQEQILSLFEDTFVPEISVTTPSQFEAPGPFSEQASLLDLDFDPLPPVTSPVKAPTPSGQSIPWDLWEPTESPAGSLPSGEPSAAEGTFAVSWPSQTAEPGPAQPAEASEVAGGTQPAAGAQEPGETAASEAASSSLPAVVVETFPATVNGTVEGGSGAGRLDLPPGFMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKELEKCRGVFPENFTERVP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.41652613827993257,"dataset":["Age-related disorders proteins"],"disorder_content":0.06913996627318718,"disprot_consensus":{"full":[{"start":1,"end":33,"type":"T"},{"start":34,"end":41,"type":"D"}],"Structural state":[{"start":1,"end":41,"type":"D"}],"Molecular function":[{"start":1,"end":33,"type":"F"}],"Structural transition":[{"start":1,"end":33,"type":"T"}],"Biological process":[{"start":1,"end":33,"type":"F"}]}},{"disprot_id":"DP04170","acc":"P34174","creator":"fquaglia","date":"2024-03-27T16:21:00.748Z","features":{"pfam":[{"id":"PF01395","name":"PBP/GOBP family","start":24,"end":142}],"gene3D":[]},"genes":[],"length":164,"name":"Pheromone-binding protein","ncbi_taxon_id":7091,"organism":"Bombyx mori","regions":[{"start":151,"end":164,"reference_id":"12417333","reference_source":"pmid","reference_html":"NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH. <i> Lee D, Damberger FF, Peng G, Horst R, Güntert P, Nikonova L, Leal WS, Wüthrich K. </i> FEBS Lett, 2002","date":"2024-03-27T16:25:26.660Z","curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"1LS8"}],"region_id":"DP04170r001","statement":[{"text":"To further characterize the apparent increased structural disorder in the C-terminal tail and the loop L2, we measured 15 N{1H}-NOEs (data not shown). These show clearly that the tail of residues 129-142 is flexibly disordered, and that the loop L2 of residues 33-45 also shows increased mobility. For both of these polypeptide segments, medium-range 1H-1H NOEs are scarce and there are no long-range NOEs, which is compatible with a fl£exibly disordered conformation.","type":"Results"},{"text":"The disordered C-terminal tail described in the publication, 129-142, corresponds to region 151-164 of Bombyx mori PBP due to the presence of a signal peptide.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-03T14:36:10.194Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MSIQGQIALALMVNMAVGSVDASQEVMKNLSLNFGKALDECKKEMTLTDAINEDFYNFWKEGYEIKNRETGCAIMCLSTKLNMLDPEGNLHHGNAMEFAKKHGADETMAQQLIDIVHGCEKSTPANDDKCIWTLGVATCFKAEIHKLNWAPSMDVAVGEILAEV","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Lepidoptera","Glossata","Ditrysia","Bombycoidea","Bombycidae","Bombycinae","Bombyx"],"alphafold_very_low_content":0.018292682926829267,"disorder_content":0.08536585365853659,"disprot_consensus":{"full":[{"start":151,"end":164,"type":"D"}],"Structural state":[{"start":151,"end":164,"type":"D"}]}},{"disprot_id":"DP04171","acc":"Q92784-1","creator":"vnugnes","date":"2024-04-04T16:08:13.681Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"DPF3"},"synonyms":[{"value":"BAF45C"},{"value":"CERD4"}]}],"length":378,"name":"Isoform 1 of Zinc finger protein DPF3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":60,"end":200,"reference_id":"35863661","reference_source":"pmid","reference_html":"Structural characterisation of amyloidogenic intrinsically disordered zinc finger protein isoforms DPF3b and DPF3a. <i> Mignon J, Mottet D, Leyder T, Uversky VN, Perpète EA, Michaux C. </i> Int J Biol Macromol, 2022","date":"2024-04-04T16:40:55.928Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04171r001","statement":[{"text":"Predictions, spectroscopy, and dynamic light scattering have revealed a high content in disorder: prevalence of random coil, aromatic residues partially to fully exposed to the solvent, and large hydrodynamic diameters.","type":"Abstract"},{"text":"From the N-terminus, the disorder profile includes the 2/3 domain (and beyond), which is considered mostly ordered (residues 1 to 90), although disorder scores varying between 0.2 and 0.5 indicate some chain flexibility, especially from residues 60 to 90. This is followed by a 110-residue-long IDR (IDR-1) up to the C2H2 zinc finger (ZnF), where the disorder score drops below the 0.5 threshold (residues 199 to 220), though retaining some flexibility.","type":"Results"},{"text":"Predictions and experimental evidence have been consistent with both isoforms being highly disordered proteins. CD spectroscopy has revealed similar footprints dominated by random coil, and measured hydrodynamic diameters by DLS indicate that they adopt expanded conformations.","type":"Conclusion"},{"text":"The boundaries of this disordered region were determined by the combination of the structural predictors used in the publication (PONDR and IUPred), AlphaFold and Mobi DB.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T08:23:33.185Z"}},{"start":222,"end":259,"reference_id":"35863661","reference_source":"pmid","reference_html":"Structural characterisation of amyloidogenic intrinsically disordered zinc finger protein isoforms DPF3b and DPF3a. <i> Mignon J, Mottet D, Leyder T, Uversky VN, Perpète EA, Michaux C. </i> Int J Biol Macromol, 2022","date":"2024-04-04T16:44:47.153Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04171r002","statement":[{"text":"Predictions, spectroscopy, and dynamic light scattering have revealed a high content in disorder: prevalence of random coil, aromatic residues partially to fully exposed to the solvent, and large hydrodynamic diameters.","type":"Abstract"},{"text":"A second shorter 40-residue-long IDR (IDR-2) is found between the C2H2 and PHD1 ZnFs (residues 221–260), followed by a gain in order at the level of the PHD1 finger (residues 261–292).","type":"Results"},{"text":"Predictions and experimental evidence have been consistent with both isoforms being highly disordered proteins. CD spectroscopy has revealed similar footprints dominated by random coil, and measured hydrodynamic diameters by DLS indicate that they adopt expanded conformations.","type":"Conclusion"},{"text":"The boundaries of this disordered region were determined by the combination of the structural predictors used in the publication (PONDR and IUPred), AlphaFold and Mobi DB.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T08:23:39.606Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MATVIHNPLKALGDQFYKEAIEHCRSYNSRLCAERSVRLPFLDSQTGVAQNNCYIWMEKRHRGPGLAPGQLYTYPARCWRKKRRLHPPEDPKLRLLEIKPEVELPLKKDGFTSESTTLEALLRGEGVEKKVDAREEESIQEIQRVLENDENVEEGNEEEDLEEDIPKRKNRTRGRARGSAGGRRRHDAASQEDHDKPYVCDICGKRYKNRPGLSYHYAHTHLASEEGDEAQDQETRSPPNHRNENHRPQKGPDGTVIPNNYCDFCLGGSNMNKKSGRPEELVSCADCGRSGHPTCLQFTLNMTEAVKTYKWQCIECKSCILCGTSENDDQLLFCDDCDRGYHMYCLNPPVAEPPEGSWSCHLCWELLKEKASAFGCQA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"disorder_content":0.47354497354497355,"disprot_consensus":{"full":[{"start":60,"end":200,"type":"D"},{"start":222,"end":259,"type":"D"}],"Structural state":[{"start":60,"end":200,"type":"D"},{"start":222,"end":259,"type":"D"}]}},{"disprot_id":"DP04172","acc":"Q61474","creator":"zskalman","date":"2024-04-07T08:19:31.512Z","features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":23,"end":90},{"id":"PF00076","name":"RNA recognition motif","start":111,"end":177}],"gene3D":[]},"genes":[{"name":{"value":"Msi1"},"synonyms":[{"value":"Msi1h"}]}],"length":362,"name":"RNA-binding protein Musashi homolog 1","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":185,"end":200,"reference_id":"28753936","reference_source":"pmid","reference_html":"Structural Insight into the Recognition of r(UAG) by Musashi-1 RBD2, and Construction of a Model of Musashi-1 RBD1-2 Bound to the Minimum Target RNA. <i> Iwaoka R, Nagata T, Tsuda K, Imai T, Okano H, Kobayashi N, Katahira M. </i> Molecules, 2017","date":"2024-05-03T07:38:29.278Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"cross_refs":[{"db":"PDB","id":"5X3Y"}],"region_id":"DP04172r001","sequence_construct":"GSHMKKIFVGGLSVNTTVEDVKHYFEQFGKVDDAMLMFDKTTNRHRGFGFVTFESEDIVEKVCEIHFHEINNKMVECKKAQPKEVMSPTGSARGRS","statement":[{"text":"The C-terminal region, Gln185–Ser200, was unstructured in the free form.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-06T17:54:25.659Z"}},{"start":194,"end":362,"reference_id":"32225071","reference_source":"pmid","reference_html":"Musashi-1: An Example of How Polyalanine Tracts Contribute to Self-Association in the Intrinsically Disordered Regions of RNA-Binding Proteins. <i> Chen TC, Huang JR. </i> Int J Mol Sci, 2020","date":"2024-05-06T17:27:39.508Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":5.5},{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":null,"value":283}],"cross_refs":[{"db":"BMRB","id":"50204"}],"region_id":"DP04172r002","statement":[{"text":"The chemical shift assignments for the IDRs of Musashi-1 (residues 194–362; BMRB access number: 50204) are shown in Figure 2A (pH 5.5, 283 K).","type":"Results"},{"text":" Although the PASTA algorithm [40] predicts four α-helices based on the primary sequence (Figure 2B), secondary chemical shift analysis indicates that just two regions, residues ~208–218 and ~270–284, form transient α-helices (Figure 2C–E), with populations (predicted using the δ2D algorithm [41] derived from the molecular dynamics simulation and experimental observations of conformational equilibrium of multiple states, using Cα, Cβ, C’, HN, and NH chemical shifts) of 28% and 45% at most (Figure 2F).","type":"Results"}]},{"start":194,"end":362,"reference_id":"32225071","reference_source":"pmid","reference_html":"Musashi-1: An Example of How Polyalanine Tracts Contribute to Self-Association in the Intrinsically Disordered Regions of RNA-Binding Proteins. <i> Chen TC, Huang JR. </i> Int J Mol Sci, 2020","date":"2024-05-06T17:50:31.946Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"Q61474","operator":null,"partner_start":194,"partner_end":362}],"region_id":"DP04172r003","statement":[{"text":"Micrographs of the oligomers that form at 293 and 303 K are shown in Figure 3D.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":194,"end":362,"reference_id":"32225071","reference_source":"pmid","reference_html":"Musashi-1: An Example of How Polyalanine Tracts Contribute to Self-Association in the Intrinsically Disordered Regions of RNA-Binding Proteins. <i> Chen TC, Huang JR. </i> Int J Mol Sci, 2020","date":"2024-05-06T17:53:32.129Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"Q61474","operator":null,"partner_start":194,"partner_end":362}],"region_id":"DP04172r004","statement":[{"text":"The protein is prone to aggregation and proline-rich (~12% in the sequence), so a specific assignment strategy was used, as described in the Material and Methods section and the Supplementary Information.","type":"Results"},{"text":"The precipitation of the protein made it difficult to use CD spectroscopy to estimate its secondary structure, as the Δε values (Equation (1)) used as input for the program became more uncertain as aggregates formed and the signal intensity decreased.","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":4,"released":"2024_06","sequence":"METDAPQPGLASPDSPHDPCKMFIGGLSWQTTQEGLREYFGQFGEVKECLVMRDPLTKRSRGFGFVTFMDQAGVDKVLAQSRHELDSKTIDPKVAFPRRAQPKMVTRTKKIFVGGLSVNTTVEDVKHYFEQFGKVDDAMLMFDKTTNRHRGFGFVTFESEDIVEKVCEIHFHEINNKMVECKKAQPKEVMSPTGSARGRSRVMPYGMDAFMLGIGMLGYPGFQATTYASRSYTGLAPGYTYQFPEFRVERSPLPSAPVLPELTAIPLTAYGPMAAAAAAAAVVRGTGSHPWTMAPPPGSTPSRTGGFLGTTSPGPMAELYGAANQDSGVSSYISAASPAPSTGFGHSLGGPLIATAFTNGYH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"alphafold_very_low_content":0.4696132596685083,"dataset":["RNA-binding proteins","Condensates-related proteins"],"disorder_content":0.49171270718232046,"disprot_consensus":{"full":[{"start":185,"end":362,"type":"D"}],"Structural state":[{"start":185,"end":362,"type":"D"}],"Molecular function":[{"start":194,"end":362,"type":"F"}]}},{"disprot_id":"DP04173","acc":"Q9BUR4","creator":"romanv","date":"2024-04-08T12:13:25.355Z","features":{"pfam":[{"id":"PF00400","name":"WD domain, G-beta repeat","start":172,"end":197},{"id":"PF00400","name":"WD domain, G-beta repeat","start":281,"end":303},{"id":"PF00400","name":"WD domain, G-beta repeat","start":357,"end":396},{"id":"PF00400","name":"WD domain, G-beta repeat","start":421,"end":441}],"gene3D":[]},"genes":[{"name":{"value":"WRAP53","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"19250907","url":"http://www.ncbi.nlm.nih.gov/pubmed/19250907","alternativeUrl":"https://europepmc.org/abstract/MED/19250907"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:25522","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:25522"}}]},"synonyms":[{"value":"TCAB1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"19179534","url":"http://www.ncbi.nlm.nih.gov/pubmed/19179534","alternativeUrl":"https://europepmc.org/abstract/MED/19179534"}}]},{"value":"WDR79","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"19285445","url":"http://www.ncbi.nlm.nih.gov/pubmed/19285445","alternativeUrl":"https://europepmc.org/abstract/MED/19285445"}}]}]}],"length":548,"name":"Telomerase Cajal body protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":150,"reference_id":"33883742","reference_source":"pmid","reference_html":"Structure of human telomerase holoenzyme with bound telomeric DNA. <i> Ghanim GE, Fountain AJ, van Roon AM, Rangan R, Das R, Collins K, Nguyen THD. </i> Nature, 2021","date":"2024-05-10T08:53:36.044Z","curator_id":"romanv","curator_name":"Roman Vilarullo ","curator_orcid":"0009-0008-1175-3506","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"7BGB"},{"db":"EMDB","id":"12177"}],"region_id":"DP04173r001","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60832"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NPE3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NY12"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NX24"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00004A7003_9606"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-18T14:25:33.331Z"}},{"start":199,"end":209,"reference_id":"33883742","reference_source":"pmid","reference_html":"Structure of human telomerase holoenzyme with bound telomeric DNA. <i> Ghanim GE, Fountain AJ, van Roon AM, Rangan R, Das R, Collins K, Nguyen THD. </i> Nature, 2021","date":"2024-05-10T08:51:54.412Z","curator_id":"romanv","curator_name":"Roman Vilarullo ","curator_orcid":"0009-0008-1175-3506","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"7BGB"},{"db":"EMDB","id":"12177"}],"region_id":"DP04173r002","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60832"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NPE3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NY12"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NX24"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00004A7003_9606"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-18T14:25:35.000Z"}},{"start":442,"end":452,"reference_id":"33883742","reference_source":"pmid","reference_html":"Structure of human telomerase holoenzyme with bound telomeric DNA. <i> Ghanim GE, Fountain AJ, van Roon AM, Rangan R, Das R, Collins K, Nguyen THD. </i> Nature, 2021","date":"2024-05-10T08:51:19.291Z","curator_id":"romanv","curator_name":"Roman Vilarullo ","curator_orcid":"0009-0008-1175-3506","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"7BGB"},{"db":"EMDB","id":"12177"}],"region_id":"DP04173r003","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60832"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NPE3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NY12"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NX24"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00004A7003_9606"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-18T14:25:39.796Z"}},{"start":486,"end":503,"reference_id":"33883742","reference_source":"pmid","reference_html":"Structure of human telomerase holoenzyme with bound telomeric DNA. <i> Ghanim GE, Fountain AJ, van Roon AM, Rangan R, Das R, Collins K, Nguyen THD. </i> Nature, 2021","date":"2024-05-10T08:50:55.550Z","curator_id":"romanv","curator_name":"Roman Vilarullo ","curator_orcid":"0009-0008-1175-3506","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"7BGB"},{"db":"EMDB","id":"12177"}],"region_id":"DP04173r004","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60832"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NPE3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NY12"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NX24"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00004A7003_9606"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-18T14:25:36.092Z"}},{"start":511,"end":548,"reference_id":"33883742","reference_source":"pmid","reference_html":"Structure of human telomerase holoenzyme with bound telomeric DNA. <i> Ghanim GE, Fountain AJ, van Roon AM, Rangan R, Das R, Collins K, Nguyen THD. </i> Nature, 2021","date":"2024-05-10T08:50:28.985Z","curator_id":"romanv","curator_name":"Roman Vilarullo ","curator_orcid":"0009-0008-1175-3506","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"7BGB"},{"db":"EMDB","id":"12177"}],"region_id":"DP04173r005","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60832"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NPE3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NY12"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NX24"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00004A7003_9606"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-18T14:25:38.253Z"}}],"regions_counter":5,"released":"2024_12","sequence":"MKTLETQPLAPDCCPSDQDPAPAHPSPHASPMNKNADSELMPPPPERGDPPRLSPDPVAGSAVSQELREGDPVSLSTPLETEFGSPSELSPRIEEQELSENTSLPAEEANGSLSEEEANGPELGSGKAMEDTSGEPAAEDEGDTAWNYSFSQLPRFLSGSWSEFSTQPENFLKGCKWAPDGSCILTNSADNILRIYNLPPELYHEGEQVEYAEMVPVLRMVEGDTIYDYCWYSLMSSAQPDTSYVASSSRENPIHIWDAFTGELRASFRAYNHLDELTAAHSLCFSPDGSQLFCGFNRTVRVFSTARPGRDCEVRATFAKKQGQSGIISCIAFSPAQPLYACGSYGRSLGLYAWDDGSPLALLGGHQGGITHLCFHPDGNRFFSGARKDAELLCWDLRQSGYPLWSLGREVTTNQRIYFDLDPTGQFLVSGSTSGAVSVWDTDGPGNDGKPEPVLSFLPQKDCTNGVSLHPSLPLLATASGQRVFPEPTESGDEGEELGLPLLSTRHVHLECRLQLWWCGGAPDSSIPDDHQGEKGQGGTEGGVGELI","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.3193430656934307,"dataset":[],"disorder_content":0.41605839416058393,"disprot_consensus":{"full":[{"start":1,"end":150,"type":"D"},{"start":199,"end":209,"type":"D"},{"start":442,"end":452,"type":"D"},{"start":486,"end":503,"type":"D"},{"start":511,"end":548,"type":"D"}],"Structural state":[{"start":1,"end":150,"type":"D"},{"start":199,"end":209,"type":"D"},{"start":442,"end":452,"type":"D"},{"start":486,"end":503,"type":"D"},{"start":511,"end":548,"type":"D"}]}},{"disprot_id":"DP04174","acc":"Q12211","creator":"vnugnes","date":"2024-04-08T13:42:33.230Z","features":{"pfam":[{"id":"PF01416","name":"tRNA pseudouridine synthase","start":303,"end":407}],"gene3D":[]},"genes":[{"name":{"value":"PUS1"},"olnNames":[{"value":"YPL212C"}]}],"length":544,"name":"tRNA pseudouridine synthase 1","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":71,"reference_id":"37939088","reference_source":"pmid","reference_html":"The structural basis of mRNA recognition and binding by yeast pseudouridine synthase PUS1. <i> Grünberg S, Doyle LA, Wolf EJ, Dai N, Corrêa IR, Yigit E, Stoddard BL. </i> PLoS One, 2023","date":"2024-04-08T13:47:57.695Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"7R9F"}],"region_id":"DP04174r001","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00023119C6_32630"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"The electron density maps from molecular replacement and subsequent rounds of refinement displayed well-ordered density for most of the protein chain (the first 70 residues, last 49 residues, and four subsequent surface loops ranging in length from 2 to 19 residues were disordered) and the first 12 bases of the RNA substrate (the final 6 base pairs were also disordered).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:57:50.693Z"}},{"start":254,"end":266,"reference_id":"37939088","reference_source":"pmid","reference_html":"The structural basis of mRNA recognition and binding by yeast pseudouridine synthase PUS1. <i> Grünberg S, Doyle LA, Wolf EJ, Dai N, Corrêa IR, Yigit E, Stoddard BL. </i> PLoS One, 2023","date":"2024-04-08T13:48:27.755Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"7R9F"}],"region_id":"DP04174r002","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00023119C6_32630"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"The electron density maps from molecular replacement and subsequent rounds of refinement displayed well-ordered density for most of the protein chain (the first 70 residues, last 49 residues, and four subsequent surface loops ranging in length from 2 to 19 residues were disordered) and the first 12 bases of the RNA substrate (the final 6 base pairs were also disordered).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:57:54.683Z"}},{"start":254,"end":266,"reference_id":"37939088","reference_source":"pmid","reference_html":"The structural basis of mRNA recognition and binding by yeast pseudouridine synthase PUS1. <i> Grünberg S, Doyle LA, Wolf EJ, Dai N, Corrêa IR, Yigit E, Stoddard BL. </i> PLoS One, 2023","date":"2024-04-08T13:48:36.971Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"7R9F"}],"region_id":"DP04174r003","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00023119C6_32630"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"The electron density maps from molecular replacement and subsequent rounds of refinement displayed well-ordered density for most of the protein chain (the first 70 residues, last 49 residues, and four subsequent surface loops ranging in length from 2 to 19 residues were disordered) and the first 12 bases of the RNA substrate (the final 6 base pairs were also disordered).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T08:18:27.644Z"}},{"start":464,"end":483,"reference_id":"37939088","reference_source":"pmid","reference_html":"The structural basis of mRNA recognition and binding by yeast pseudouridine synthase PUS1. <i> Grünberg S, Doyle LA, Wolf EJ, Dai N, Corrêa IR, Yigit E, Stoddard BL. </i> PLoS One, 2023","date":"2024-04-08T13:49:13.328Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"7R9F"}],"region_id":"DP04174r004","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00023119C6_32630"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"The electron density maps from molecular replacement and subsequent rounds of refinement displayed well-ordered density for most of the protein chain (the first 70 residues, last 49 residues, and four subsequent surface loops ranging in length from 2 to 19 residues were disordered) and the first 12 bases of the RNA substrate (the final 6 base pairs were also disordered).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T08:18:10.722Z"}},{"start":464,"end":483,"reference_id":"37939088","reference_source":"pmid","reference_html":"The structural basis of mRNA recognition and binding by yeast pseudouridine synthase PUS1. <i> Grünberg S, Doyle LA, Wolf EJ, Dai N, Corrêa IR, Yigit E, Stoddard BL. </i> PLoS One, 2023","date":"2024-04-08T13:50:04.210Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"7R9F"}],"region_id":"DP04174r005","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00023119C6_32630"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"The electron density maps from molecular replacement and subsequent rounds of refinement displayed well-ordered density for most of the protein chain (the first 70 residues, last 49 residues, and four subsequent surface loops ranging in length from 2 to 19 residues were disordered) and the first 12 bases of the RNA substrate (the final 6 base pairs were also disordered).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T08:18:32.568Z"}},{"start":494,"end":544,"reference_id":"37939088","reference_source":"pmid","reference_html":"The structural basis of mRNA recognition and binding by yeast pseudouridine synthase PUS1. <i> Grünberg S, Doyle LA, Wolf EJ, Dai N, Corrêa IR, Yigit E, Stoddard BL. </i> PLoS One, 2023","date":"2024-04-08T13:50:33.906Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"7R9F"}],"region_id":"DP04174r006","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00023119C6_32630"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"The electron density maps from molecular replacement and subsequent rounds of refinement displayed well-ordered density for most of the protein chain (the first 70 residues, last 49 residues, and four subsequent surface loops ranging in length from 2 to 19 residues were disordered) and the first 12 bases of the RNA substrate (the final 6 base pairs were also disordered).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T08:18:12.579Z"}}],"regions_counter":6,"released":"2024_06","sequence":"MSEENLRPAYDDQVNEDVYKRGAQSKLTKARKADFDDEKDKKKDNDKHIDKRPKSGPRLDENGNPLPKEPRLPKRKVAVMVGYCGTGYHGMQYNPPNPTIESALFKAFVEAGAISKDNSNDLKKNGFMRAARTDKGVHAGGNLISLKMIIEDPDIKQKINEKLPEGIRVWDIERVNKAFDCRKMCSSRWYEYLLPTYSLIGPKPGSILYRDIEESKTELPGVLDEDLESKEFWEEFKKDANEKFSTEEIEAILAYVPPARDEFDINEELYQKVKKYKQLENAHRRRYRISAAKLAKFRASTSQYLGAHNFHNFTLGKDFKEPSAIRFMKDIKVSDPFVIGDAQTEWISIKIHGQSFMLHQIRKMVSMATLITRCGCPVERISQAYGQQKINIPKAPALGLLLEAPVFEGYNKRLEQFGYKAIDFSKYQDEVDKFKMKHIYDKIYKEEVDENVFNAFFSYIDSFNKVTGAQGEETADKSGPAVQKSIFEFLTAKGIPGLTDAPESNKKIKQRKRMEEEEAASKKAEISSTTQSNEPEVQPEAAAN","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.15073529411764705,"dataset":["RNA-binding proteins"],"disorder_content":0.2849264705882353,"disprot_consensus":{"full":[{"start":1,"end":71,"type":"D"},{"start":254,"end":266,"type":"D"},{"start":464,"end":483,"type":"D"},{"start":494,"end":544,"type":"D"}],"Structural state":[{"start":1,"end":71,"type":"D"},{"start":254,"end":266,"type":"D"},{"start":464,"end":483,"type":"D"},{"start":494,"end":544,"type":"D"}],"Disorder function":[{"start":254,"end":266,"type":"F"},{"start":464,"end":483,"type":"F"}]}},{"disprot_id":"DP04175","acc":"Q08647","creator":"vnugnes","date":"2024-04-08T14:22:57.864Z","features":{"pfam":[{"id":"PF01142","name":"tRNA pseudouridine synthase D (TruD)","start":217,"end":658}],"gene3D":[]},"genes":[{"name":{"value":"PUS7","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"14561887","url":"http://www.ncbi.nlm.nih.gov/pubmed/14561887","alternativeUrl":"https://europepmc.org/abstract/MED/14561887"}},{"code":"ECO:0000312","source":{"name":"SGD","id":"S000005769","url":"https://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000005769"}}]},"orfNames":[{"value":"O5254"}],"olnNames":[{"value":"YOR243C"}]}],"length":676,"name":"Multisubstrate pseudouridine synthase 7","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":36,"reference_id":"35058356","reference_source":"pmid","reference_html":"Pseudouridine synthase 7 is an opportunistic enzyme that binds and modifies substrates with diverse sequences and structures. <i> Purchal MK, Eyler DE, Tardu M, Franco MK, Korn MM, Khan T, McNassor R, Giles R, Lev K, Sharma H, Monroe J, Mallik L, Koutmos M, Koutmou KS. </i> Proc Natl Acad Sci U S A, 2022","date":"2024-04-08T15:25:25.361Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":88,"end":88,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":145,"end":145,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":232,"end":232,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":284,"end":284,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":345,"end":345,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":405,"end":405,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":440,"end":440,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":449,"end":449,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":525,"end":525,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":558,"end":558,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":563,"end":563,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":621,"end":621,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":629,"end":629,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":653,"end":653,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":659,"end":659,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":669,"end":669,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"7MZV"}],"region_id":"DP04175r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"While it is not mentioned in the publication, this region lacks electron density in the PDB structure, indicating it is disordered.","type":"Curator statement"}]},{"start":485,"end":506,"reference_id":"35058356","reference_source":"pmid","reference_html":"Pseudouridine synthase 7 is an opportunistic enzyme that binds and modifies substrates with diverse sequences and structures. <i> Purchal MK, Eyler DE, Tardu M, Franco MK, Korn MM, Khan T, McNassor R, Giles R, Lev K, Sharma H, Monroe J, Mallik L, Koutmos M, Koutmou KS. </i> Proc Natl Acad Sci U S A, 2022","date":"2024-04-08T15:25:43.740Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":88,"end":88,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":145,"end":145,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":232,"end":232,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":284,"end":284,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":345,"end":345,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":405,"end":405,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":440,"end":440,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":449,"end":449,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":525,"end":525,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":558,"end":558,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":563,"end":563,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":621,"end":621,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":629,"end":629,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":653,"end":653,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":659,"end":659,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":669,"end":669,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"7MZV"}],"region_id":"DP04175r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"While it is not mentioned in the publication, this region lacks electron density in the PDB structure, indicating it is disordered.","type":"Curator statement"}]},{"start":662,"end":676,"reference_id":"35058356","reference_source":"pmid","reference_html":"Pseudouridine synthase 7 is an opportunistic enzyme that binds and modifies substrates with diverse sequences and structures. <i> Purchal MK, Eyler DE, Tardu M, Franco MK, Korn MM, Khan T, McNassor R, Giles R, Lev K, Sharma H, Monroe J, Mallik L, Koutmos M, Koutmou KS. </i> Proc Natl Acad Sci U S A, 2022","date":"2024-04-08T15:25:56.124Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":88,"end":88,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":145,"end":145,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":232,"end":232,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":284,"end":284,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":345,"end":345,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":405,"end":405,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":440,"end":440,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":449,"end":449,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":525,"end":525,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":558,"end":558,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":563,"end":563,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":621,"end":621,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":629,"end":629,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":653,"end":653,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":659,"end":659,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":669,"end":669,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"7MZV"}],"region_id":"DP04175r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"While it is not mentioned in the publication, this region lacks electron density in the PDB structure, indicating it is disordered.","type":"Curator statement"}]},{"start":87,"end":201,"reference_id":"35058356","reference_source":"pmid","reference_html":"Pseudouridine synthase 7 is an opportunistic enzyme that binds and modifies substrates with diverse sequences and structures. <i> Purchal MK, Eyler DE, Tardu M, Franco MK, Korn MM, Khan T, McNassor R, Giles R, Lev K, Sharma H, Monroe J, Mallik L, Koutmos M, Koutmou KS. </i> Proc Natl Acad Sci U S A, 2022","date":"2024-04-08T15:46:18.481Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006222","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with high relative B-factor values used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":88,"end":88,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":145,"end":145,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":232,"end":232,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":284,"end":284,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":345,"end":345,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":405,"end":405,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":440,"end":440,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":449,"end":449,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":525,"end":525,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":558,"end":558,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":563,"end":563,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":621,"end":621,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":629,"end":629,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":653,"end":653,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":659,"end":659,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":669,"end":669,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"7MZV"}],"region_id":"DP04175r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"However, we were unable to obtain a structure solution for insertion domain one, which necessitated the growth of Se-Met Pus7 crystals.","type":"Supplementary material"},{"text":"The electron density corresponding to the insertion domain is overall poor and of rather low resolution, as also reflected in the very high average B-factors (165.02) as compared to the average B-factors (117.44) for the rest of the protein (Figure S2E).","type":"Supplementary material"},{"text":"The B-factor values exceeding 170 in this region suggest a high degree of flexibility.","type":"Curator statement"}]}],"regions_counter":4,"released":"2024_06","sequence":"MSDSSEATVKRPLDAHVGPSENAAKKLKIEQRTQADGIHEADVGITLFLSPELPGFRGQIKQRYTDFLVNEIDQEGKVIHLTDKGFKMPKKPQRSKEEVNAEKESEAARRQEFNVDPELRNQLVEIFGEEDVLKIESVYRTANKMETAKNFEDKSVRTKIHQLLREAFKNELESVTTDTNTFKIARSNRNSRTNKQEKINQTRDANGVENWGYGPSKDFIHFTLHKENKDTMEAVNVITKLLRVPSRVIRYAGTKDRRAVTCQRVSISKIGLDRLNALNRTLKGMIIGNYNFSDASLNLGDLKGNEFVVVIRDVTTGNSEVSLEEIVSNGCKSLSENGFINYFGMQRFGTFSISTHTIGRELLLSNWKKAAELILSDQDNVLPKSKEARKIWAETKDAALALKQMPRQCLAENALLYSLSNQRKEEDGTYSENAYYTAIMKIPRNLRTMYVHAYQSYVWNSIASKRIELHGLKLVVGDLVIDTSEKSPLISGIDDEDFDEDVREAQFIRAKAVTQEDIDSVKYTMEDVVLPSPGFDVLYPSNEELKQLYVDILKADNMDPFNMRRKVRDFSLAGSYRTVIQKPKSLEYRIIHYDDPSQQLVNTDLDILNNTRAKESGQKYMKAKLDRYMPDKGGEKTAVVLKFQLGTSAYATMALRELMKLETSRRGDMCDVKENI","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.09615384615384616,"dataset":["RNA-binding proteins"],"disorder_content":0.2781065088757396,"disprot_consensus":{"full":[{"start":1,"end":36,"type":"D"},{"start":87,"end":201,"type":"D"},{"start":485,"end":506,"type":"D"},{"start":662,"end":676,"type":"D"}],"Structural state":[{"start":1,"end":36,"type":"D"},{"start":87,"end":201,"type":"D"},{"start":485,"end":506,"type":"D"},{"start":662,"end":676,"type":"D"}]}},{"disprot_id":"DP04176","acc":"P9WHP7","creator":"vnugnes","date":"2024-04-08T16:44:12.625Z","features":{"pfam":[{"id":"PF01509","name":"TruB family pseudouridylate synthase (N terminal domain)","start":27,"end":179},{"id":"PF09142","name":"tRNA Pseudouridine synthase II, C terminal","start":236,"end":291},{"id":"PF16198","name":"tRNA pseudouridylate synthase B C-terminal domain","start":180,"end":220}],"gene3D":[]},"genes":[{"name":{"value":"truB","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01080","url":"https://hamap.expasy.org/unirule/MF_01080"}}]},"orfNames":[{"value":"MTV002.58c"}],"olnNames":[{"value":"Rv2793c"}]}],"length":298,"name":"tRNA pseudouridine synthase B","ncbi_taxon_id":83332,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","regions":[{"start":112,"end":139,"reference_id":"15028724","reference_source":"pmid","reference_html":"Crystal structure of the apo forms of psi 55 tRNA pseudouridine synthase from Mycobacterium tuberculosis: a hinge at the base of the catalytic cleft. <i> Chaudhuri BN, Chan S, Perry LJ, Yeates TO. </i> J Biol Chem, 2004","date":"2024-04-08T16:46:19.588Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"1SGV"}],"region_id":"DP04176r001","statement":[{"text":"Residues 115-142 in MTB-TRUB-A and residues 112-139 in MTB-TRUB-B are missing in the electron density map (henceforth referred to as the disordered region) and are not modeled.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:56:54.383Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MSATGPGIVVIDKPAGMTSHDVVGRCRRIFATRRVGHAGTLDPMATGVLVIGIERATKILGLLTAAPKSYAATIRLGQTTSTEDAEGQVLQSVPAKHLTIEAIDAAMERLRGEIRQVPSSVSAIKVGGRRAYRLARQGRSVQLEARPIRIDRFELLAARRRDQLIDIDVEIDCSSGTYIRALARDLGDALGVGGHVTALRRTRVGRFELDQARSLDDLAERPALSLSLDEACLLMFARRDLTAAEASAAANGRSLPAVGIDGVYAACDADGRVIALLRDEGSRTRSVAVLRPATMHPG","taxonomy":["Bacteria","Actinomycetota","Actinomycetes","Mycobacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"alphafold_very_low_content":0.006711409395973154,"disorder_content":0.09395973154362416,"disprot_consensus":{"full":[{"start":112,"end":139,"type":"D"}],"Structural state":[{"start":112,"end":139,"type":"D"}]}},{"disprot_id":"DP04177","acc":"P05114","creator":"vnugnes","date":"2024-04-09T17:06:20.207Z","features":{"pfam":[{"id":"PF01101","name":"HMG14 and HMG17","start":2,"end":95}],"gene3D":[]},"genes":[{"name":{"value":"HMGN1"},"synonyms":[{"value":"HMG14"}]}],"length":100,"name":"Non-histone chromosomal protein HMG-14","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":100,"reference_id":"34458797","reference_source":"pmid","reference_html":"Site-specific modification and segmental isotope labelling of HMGN1 reveals long-range conformational perturbations caused by posttranslational modifications. <i> Niederacher G, Urwin D, Dijkwel Y, Tremethick DJ, Rosengren KJ, Becker CFW, Conibear AC. </i> RSC Chem Biol, 2021","date":"2024-04-09T17:11:51.475Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04177r001","sequence_construct":"SPKRKVSSAEGAAKEEPKRRSARLSAKPPAKVEAKPKKAAAKDKSSDKKVQTKGKRGAKGKQAEVANQETKEDLPAENGETKTEESPASDEAGEKEAKSD","statement":[{"text":"The desired molecular weight of 10.6 kDa was confirmed by mass spectrometry, however HMGN1 runs abnormally on SDS-PAGE, showing an apparent molecular weight of ∼22 kDa (Fig. 2b and d), likely due to its high content of charged residues and disordered nature.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:56:14.064Z"}},{"start":1,"end":100,"reference_id":"34458797","reference_source":"pmid","reference_html":"Site-specific modification and segmental isotope labelling of HMGN1 reveals long-range conformational perturbations caused by posttranslational modifications. <i> Niederacher G, Urwin D, Dijkwel Y, Tremethick DJ, Rosengren KJ, Becker CFW, Conibear AC. </i> RSC Chem Biol, 2021","date":"2024-04-09T17:12:00.627Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04177r002","sequence_construct":"SPKRKVSSAEGAAKEEPKRRSARLSAKPPAKVEAKPKKAAAKDKSSDKKVQTKGKRGAKGKQAEVANQETKEDLPAENGETKTEESPASDEAGEKEAKSD","statement":[{"text":"The lack of characteristic alpha-helix or beta-sheet maxima and minima in the CD spectrum (Fig. 2c) also gives evidence for the absence of secondary structural features.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:56:19.374Z"}},{"start":1,"end":100,"reference_id":"34458797","reference_source":"pmid","reference_html":"Site-specific modification and segmental isotope labelling of HMGN1 reveals long-range conformational perturbations caused by posttranslational modifications. <i> Niederacher G, Urwin D, Dijkwel Y, Tremethick DJ, Rosengren KJ, Becker CFW, Conibear AC. </i> RSC Chem Biol, 2021","date":"2024-04-09T17:13:29.700Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04177r003","sequence_construct":"SPKRKVSSAEGAAKEEPKRRSARLSAKPPAKVEAKPKKAAAKDKSSDKKVQTKGKRGAKGKQAEVANQETKEDLPAENGETKTEESPASDEAGEKEAKSD","statement":[{"text":"Three-dimensional HNCO, HNCA, HN(CA)CB, HN(CO)CA, HN(CO)(CA)CB, HN(CA)CO, HN(CO)(CA)(N)NH, and HN(CA)(N)NH spectra were acquired on a 700 MHz NMR spectrometer equipped with a cryoprobe and showed sharp signals typical of intrinsically disordered proteins.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:56:26.203Z"}},{"start":11,"end":64,"reference_id":"34458797","reference_source":"pmid","reference_html":"Site-specific modification and segmental isotope labelling of HMGN1 reveals long-range conformational perturbations caused by posttranslational modifications. <i> Niederacher G, Urwin D, Dijkwel Y, Tremethick DJ, Rosengren KJ, Becker CFW, Conibear AC. </i> RSC Chem Biol, 2021","date":"2024-04-09T17:44:28.644Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031491","term_name":"nucleosome binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","region_id":"DP04177r004","sequence_construct":"SPKRKVSSAEGAAKEEPKRRSARLSAKPPAKVEAKPKKAAAKDKSSDKKVQTKGKRGAKGKQAEVANQETKEDLPAENGETKTEESPASDEAGEKEAKSD","statement":[{"text":"Overall, the results show that all HMGN1 variants bind to nucleosomes and the major band at 2 : 1 HMGN1 : nucleosome ratios corresponds to two HMGN1 molecules per nucleosome (Fig. 5a), as would be expected from binding of one HMGN1 to each face of the nucleosome.","type":"Results"},{"text":"Truncated HMGN1 variants in which the N-terminal residues (1–10) or C-terminal residues (65–99) were missing were also compared with full-length HMGN1 for their nucleosome-binding properties, as shown in ESI,† Fig. S9.1. Considering the lower molecular weights, the truncated variants show similar nucleosome binding to full-length HMGN1, showing that the N- and C-terminal regions are not directly involved in nucleosome core binding.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a nucleosome, a complex comprised of DNA wound around a multisubunit core and associated proteins, which forms the primary packing unit of DNA into higher order structures.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Nucleosome cores were assembled onto a 147 bp AlexaFluor488 labelled DNA fragment containing the 601 nucleosome positioning sequence. Recombinant Xenopus laevis histone octamers were used to assemble nucleosomes, and were produced using standard protocols."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:56:35.576Z"}},{"start":11,"end":64,"reference_id":"34458797","reference_source":"pmid","reference_html":"Site-specific modification and segmental isotope labelling of HMGN1 reveals long-range conformational perturbations caused by posttranslational modifications. <i> Niederacher G, Urwin D, Dijkwel Y, Tremethick DJ, Rosengren KJ, Becker CFW, Conibear AC. </i> RSC Chem Biol, 2021","date":"2024-04-09T17:48:23.454Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031492","term_name":"nucleosomal DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","region_id":"DP04177r005","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Assessment was performed with the Widom 601 DNA sequence 5'-ntcggatgta tatatctgac acgtgcctgg agactaggga gtaatcccct tggcggttaa aacgcggggg acagcgcgta cgtgcgttta agcggtgcta gagctgtcta cgaccaattg agcggcctcg gcaccgggat tctcgat"}]}],"sequence_construct":"SPKRKVSSAEGAAKEEPKRRSARLSAKPPAKVEAKPKKAAAKDKSSDKKVQTKGKRGAKGKQAEVANQETKEDLPAENGETKTEESPASDEAGEKEAKSD","statement":[{"text":"Experiments in which the HMGN1 variants were mixed with DNA (147 bp AlexaFluor488 labelled DNA containing the 601 nucleosome positioning sequence, Supplementary Data Fig. S9.2, ESI†) indicated that there is no difference in binding of the HNGN1 variants to naked DNA.","type":"Results"}],"term_comment":"","term_def":"\"Binding to the DNA portion of a nucleosome.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:56:42.310Z"}}],"regions_counter":5,"released":"2024_06","sequence":"MPKRKVSSAEGAAKEEPKRRSARLSAKPPAKVEAKPKKAAAKDKSSDKKVQTKGKRGAKGKQAEVANQETKEDLPAENGETKTEESPASDEAGEKEAKSD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":100,"type":"D"}],"Structural state":[{"start":1,"end":100,"type":"D"}],"Molecular function":[{"start":11,"end":64,"type":"F"}]}},{"disprot_id":"DP04178","acc":"O14746","creator":"romanv","date":"2024-04-11T08:56:06.828Z","features":{"pfam":[{"id":"PF12009","name":"Telomerase ribonucleoprotein complex - RNA binding domain","start":460,"end":592},{"id":"PF21399","name":"Telomerase reverse transcriptase, C-terminal extension","start":968,"end":1097}],"gene3D":[]},"genes":[{"name":{"value":"TERT"},"synonyms":[{"value":"EST2"},{"value":"TCS1"},{"value":"TRT"}]}],"length":1132,"name":"Telomerase reverse transcriptase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":180,"end":321,"reference_id":"35201900","reference_source":"pmid","reference_html":"Structural basis of human telomerase recruitment by TPP1-POT1. <i> Sekne Z, Ghanim GE, van Roon AM, Nguyen THD. </i> Science, 2022","date":"2024-05-14T08:52:30.386Z","curator_id":"romanv","curator_name":"Roman Vilarullo ","curator_orcid":"0009-0008-1175-3506","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"7QXS"},{"db":"PDB","id":"7QXB"},{"db":"PDB","id":"7QXA"},{"db":"EMDB","id":"14197"},{"db":"EMDB","id":"14196"}],"region_id":"DP04178r001","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"B2R5B3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"B4DR52"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NUX5"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q96AP0"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00004A7003_9606"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting telomeric DNA (T2AG3)5 with sequence 5'-TTAGGGTTAGGGTTAGGGTTAGGGTTAGGG"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-14T14:52:06.782Z"}},{"start":418,"end":443,"reference_id":"35201900","reference_source":"pmid","reference_html":"Structural basis of human telomerase recruitment by TPP1-POT1. <i> Sekne Z, Ghanim GE, van Roon AM, Nguyen THD. </i> Science, 2022","date":"2024-05-09T10:25:57.497Z","curator_id":"romanv","curator_name":"Roman Vilarullo ","curator_orcid":"https://orcid.org/0009-0008-1175-3506","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"7QXS"},{"db":"PDB","id":"7QXB"},{"db":"PDB","id":"7QXA"},{"db":"EMDB","id":"14197 "},{"db":"EMDB","id":"14196"}],"region_id":"DP04178r002","statement":[{"text":"The PDB shows this region lacks electron density, indicating it is disordered","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"B2R5B3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"B4DR52"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q96AP0"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NUX5"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00004A7003_9606"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting telomeric DNA (T2AG3)5 with sequence 5'-TTAGGGTTAGGGTTAGGGTTAGGGTTAGGG"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-05-13T13:28:31.670Z"}},{"start":222,"end":240,"reference_id":"25999477","reference_source":"pmid","reference_html":"Akt-mediated phosphorylation increases the binding affinity of hTERT for importin α to promote nuclear translocation. <i> Jeong SA, Kim K, Lee JH, Cha JS, Khadka P, Cho HS, Chung IK. </i> J Cell Sci, 2015","date":"2024-10-18T15:02:04.544Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006606","term_name":"protein import into nucleus","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":1,"ec_go":"IMP","region_id":"DP04178r003","statement":[{"text":"To determine whether nuclear localization of hTERT is affected by different cellular backgrounds, several cell lines – including MCF7, H1299 and U2OS cells – were transfected with Flag–hTERT and various mutant constructs (Flag-7A, Flag-S227A and Flag-S227E, see Fig. 1A), and then subjected to immunofluorescence analyses using an antibody against Flag (supplementary material Fig. S1). The results indicated that both the bipartite NLS and Akt-mediated phosphorylation at S227 are required for efficient nuclear import of hTERT, suggesting that the mechanism of nuclear localization of hTERT is not cell-type specific.","type":"Results"}],"term_comment":"","term_def":"\"The directed movement of a protein from the cytoplasm to the nucleus.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg222Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"To generate a 7A mutant, the basic amino acids in both\nclusters are mutated to alanines. S227A and S227E mutants were constructed by replacing\nthe serine residue at 227 with alanine and glutamate, respectively."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg223Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"To generate a 7A mutant, the basic amino acids in both\nclusters are mutated to alanines. S227A and S227E mutants were constructed by replacing\nthe serine residue at 227 with alanine and glutamate, respectively."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg224Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"To generate a 7A mutant, the basic amino acids in both\nclusters are mutated to alanines. S227A and S227E mutants were constructed by replacing\nthe serine residue at 227 with alanine and glutamate, respectively"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys236Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"To generate a 7A mutant, the basic amino acids in both\nclusters are mutated to alanines. S227A and S227E mutants were constructed by replacing\nthe serine residue at 227 with alanine and glutamate, respectively."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg238Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"To generate a 7A mutant, the basic amino acids in both\nclusters are mutated to alanines. S227A and S227E mutants were constructed by replacing\nthe serine residue at 227 with alanine and glutamate, respectively."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg239Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"To generate a 7A mutant, the basic amino acids in both\nclusters are mutated to alanines. S227A and S227E mutants were constructed by replacing\nthe serine residue at 227 with alanine and glutamate, respectively."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg240Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"To generate a 7A mutant, the basic amino acids in both\nclusters are mutated to alanines. S227A and S227E mutants were constructed by replacing\nthe serine residue at 227 with alanine and glutamate, respectively."}]},{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser227Ala","start":null,"end":null,"position":null,"statements":[{"type":"Supplementary material","text":"To generate a 7A mutant, the basic amino acids in both\nclusters are mutated to alanines. S227A and S227E mutants were constructed by replacing\nthe serine residue at 227 with alanine and glutamate, respectively."}]}],"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0031","entry_name":"Michigan Cancer Foundation-7"},{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0060","entry_name":"NCIH1299"},{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0042","entry_name":"U-2 OS"}]}],"regions_counter":3,"released":"2024_06","sequence":"MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQVWKNPTFFLRVISDTASLCYSILKAKNAGMSLGAKGAAGPLPSEAVQWLCHQAFLLKLTRHRVTYVPLLGSLRTAQTQLSRKLPGTTLTALEAAANPALPSDFKTILD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.16784452296819788,"dataset":["Cancer-related proteins","RNA-binding proteins"],"disorder_content":0.14840989399293286,"disprot_consensus":{"full":[{"start":180,"end":321,"type":"D"},{"start":418,"end":443,"type":"D"}],"Structural state":[{"start":180,"end":321,"type":"D"},{"start":418,"end":443,"type":"D"}],"Biological process":[{"start":222,"end":240,"type":"F"}]}},{"disprot_id":"DP04179","acc":"P30519","creator":"romanv","date":"2024-04-16T08:50:21.629Z","features":{"pfam":[{"id":"PF01126","name":"Heme oxygenase","start":32,"end":236}],"gene3D":[]},"genes":[{"name":{"value":"HMOX2"},"synonyms":[{"value":"HO2"}]}],"length":316,"name":"Heme oxygenase 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":29,"reference_id":"17965015","reference_source":"pmid","reference_html":"Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2. <i> Bianchetti CM, Yi L, Ragsdale SW, Phillips GN. </i> J Biol Chem, 2007","date":"2024-10-18T15:22:00.440Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":1,"cross_refs":[{"db":"PDB","id":"2RGZ"}],"region_id":"DP04179r001","statement":[{"text":"The A molecule of heme-bound HO-2 was lacking electron density for Met1–Met28 and Thr243–Lys264. The B molecule of heme-bound HO-2 was missing density for Met1–Arg29 and Leu249–Lys264.","type":"Results"},{"text":"The PDB shows this region lacks electron density, indicating it is disordered","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15430","entry_name":"protoporphyrin"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys127Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The truncated HO-2 lacking the three HRMs and the membrane binding region was generated by replacing Cys-127 with Ala-127 and putting a stop codon “TAA” right before Cys-265, which will be referred to as HO-2 in this report."}]}],"sequence_construct":"MSAEVETSEGVDESEKKNSGALEKENQMRMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSALEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGENWEEQVQAPKAAQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFEYNMQIFNELDQAGSTLARETLEDGFPVHDGKGDMRK"},{"start":249,"end":264,"reference_id":"17965015","reference_source":"pmid","reference_html":"Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2. <i> Bianchetti CM, Yi L, Ragsdale SW, Phillips GN. </i> J Biol Chem, 2007","date":"2024-10-18T15:21:45.050Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":1,"cross_refs":[{"db":"PDB","id":"2RGZ"}],"region_id":"DP04179r002","statement":[{"text":"The A molecule of heme-bound HO-2 was lacking electron density for Met1–Met28 and Thr243–Lys264. The B molecule of heme-bound HO-2 was missing density for Met1–Arg29 and Leu249–Lys264.","type":"Results"},{"text":"The PDB shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15430","entry_name":"protoporphyrin"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys127Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The truncated HO-2 lacking the three HRMs and the membrane binding region was generated by replacing Cys-127 with Ala-127 and putting a stop codon “TAA” right before Cys-265, which will be referred to as HO-2 in this report."}]}],"sequence_construct":"MSAEVETSEGVDESEKKNSGALEKENQMRMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSALEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGENWEEQVQAPKAAQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFEYNMQIFNELDQAGSTLARETLEDGFPVHDGKGDMRK"},{"start":1,"end":29,"reference_id":"17965015","reference_source":"pmid","reference_html":"Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2. <i> Bianchetti CM, Yi L, Ragsdale SW, Phillips GN. </i> J Biol Chem, 2007","date":"2024-10-18T15:25:39.955Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys127Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The truncated HO-2 lacking the three HRMs and the membrane binding region was generated by replacing Cys-127 with Ala-127 and putting a stop codon “TAA” right before Cys-265, which will be referred to as HO-2 in this report."}]}],"cross_refs":[{"db":"PDB","id":"2RGZ"}],"region_id":"DP04179r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15430","entry_name":"protoporphyrin"}],"sequence_construct":"MSAEVETSEGVDESEKKNSGALEKENQMRMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSALEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGENWEEQVQAPKAAQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFEYNMQIFNELDQAGSTLARETLEDGFPVHDGKGDMRK","statement":[{"text":"The A molecule of heme-bound HO-2 was lacking electron density for Met1–Met28 and Thr243–Lys264. The B molecule of heme-bound HO-2 was missing density for Met1–Arg29 and Leu249–Lys264.","type":"Results"},{"text":"The PDB structure shows the 1-29 region lacks electron density, indicating it's disordered.","type":"Curator statement"}]}],"regions_counter":3,"released":"2024_12","sequence":"MSAEVETSEGVDESEKKNSGALEKENQMRMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSALEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGENWEEQVQCPKAAQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFEYNMQIFNELDQAGSTLARETLEDGFPVHDGKGDMRKCPFYAAEQDKGALEGSSCPFRTAMAVLRKPSLQFILAAGVALAAGLLAWYYM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.2310126582278481,"dataset":[],"disorder_content":0.14240506329113925,"disprot_consensus":{"full":[{"start":1,"end":29,"type":"D"},{"start":249,"end":264,"type":"D"}],"Structural state":[{"start":1,"end":29,"type":"D"},{"start":249,"end":264,"type":"D"}],"Disorder function":[{"start":1,"end":29,"type":"F"}]}},{"disprot_id":"DP04180","acc":"O60232","creator":"romanv","date":"2024-04-16T11:59:40.231Z","features":{"pfam":[{"id":"PF06677","name":"Sjogren's syndrome/scleroderma autoantigen 1 (Autoantigen p27)","start":37,"end":74}],"gene3D":[]},"genes":[{"name":{"value":"ZNRD2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11328","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11328"}}]},"synonyms":[{"value":"SSSCA1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:11328","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:11328"}}]}]}],"length":199,"name":"Protein ZNRD2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":12,"reference_id":"32170109","reference_source":"pmid","reference_html":"Sjögren syndrome/scleroderma autoantigen 1 is a direct Tankyrase binding partner in cancer cells. <i> Perdreau-Dahl H, Progida C, Barfeld SJ, Guldsten H, Thiede B, Arntzen M, Bakke O, Mills IG, Krauss S, Morth JP. </i> Commun Biol, 2020","date":"2024-10-18T15:32:35.772Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_12","version":1,"cross_refs":[{"db":"PDB","id":"6HCZ"}],"region_id":"DP04180r001","statement":[{"text":"We were not able to model residues 1–12 and 78–111 in the electron density map and coincidentally, these regions correlate with the intrinsic disorder prediction plot of SSSCA1 and confirm that these residues likely are disordered in the protein crystal as well (Fig. 1a).","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30751","entry_name":"formic acid"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}]},{"start":78,"end":111,"reference_id":"32170109","reference_source":"pmid","reference_html":"Sjögren syndrome/scleroderma autoantigen 1 is a direct Tankyrase binding partner in cancer cells. <i> Perdreau-Dahl H, Progida C, Barfeld SJ, Guldsten H, Thiede B, Arntzen M, Bakke O, Mills IG, Krauss S, Morth JP. </i> Commun Biol, 2020","date":"2024-10-18T15:32:16.366Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":1,"cross_refs":[{"db":"PDB","id":"6HCZ"}],"region_id":"DP04180r002","statement":[{"text":"We were not able to model residues 1–12 and 78–111 in the electron density map and coincidentally, these regions correlate with the intrinsic disorder prediction plot of SSSCA1 and confirm that these residues likely are disordered in the protein crystal as well (Fig. 1a).","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30751","entry_name":"formic acid"}]},{"start":1,"end":11,"reference_id":"32170109","reference_source":"pmid","reference_html":"Sjögren syndrome/scleroderma autoantigen 1 is a direct Tankyrase binding partner in cancer cells. <i> Perdreau-Dahl H, Progida C, Barfeld SJ, Guldsten H, Thiede B, Arntzen M, Bakke O, Mills IG, Krauss S, Morth JP. </i> Commun Biol, 2020","date":"2024-10-18T15:33:21.415Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04180r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30751","entry_name":"formic acid"}],"statement":[{"text":"We were not able to model residues 1–12 and 78–111 in the electron density map and coincidentally, these regions correlate with the intrinsic disorder prediction plot of SSSCA1 and confirm that these residues likely are disordered in the protein crystal as well (Fig. 1a).","type":"Results"}]}],"regions_counter":3,"released":"2024_12","sequence":"MALNGAEVDDFSWEPPTEAETKVLQARRERQDRISRLMGDYLLRGYRMLGETCADCGTILLQDKQRKIYCVACQELDSDVDKDNPALNAQAALSQAREHQLASASELPLGSRPAPQPPVPRPEHCEGAAAGLKAAQGPPAPAVPPNTDVMACTQTALLQKLTWASAELGSSTSLETSIQLCGLIRACAEALRSLQQLQH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.16080402010050251,"dataset":[],"disorder_content":0.23115577889447236,"disprot_consensus":{"full":[{"start":1,"end":12,"type":"D"},{"start":78,"end":111,"type":"D"}],"Structural state":[{"start":1,"end":12,"type":"D"},{"start":78,"end":111,"type":"D"}],"Disorder function":[{"start":1,"end":11,"type":"F"}]}},{"disprot_id":"DP04182","acc":"Q99453","creator":"cpintado","date":"2024-04-18T08:11:38.477Z","features":{"pfam":[{"id":"PF00046","name":"Homeodomain","start":99,"end":155}],"gene3D":[]},"genes":[{"name":{"value":"PHOX2B"},"synonyms":[{"value":"PMX2B"}]}],"length":314,"name":"Paired mesoderm homeobox protein 2B","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":228,"end":240,"reference_id":"38431667","reference_source":"pmid","reference_html":"Alternative low-populated conformations prompt phase transitions in polyalanine repeat expansions. <i> Antón R, Treviño MÁ, Pantoja-Uceda D, Félix S, Babu M, Cabrita EJ, Zweckstetter M, Tinnefeld P, Vera AM, Oroz J. </i> Nat Commun, 2024","date":"2024-04-18T08:14:25.918Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8PUI"}],"region_id":"DP04182r001","statement":[{"text":"NMR secondary chemical shift analysis and chemical shift-derived S2 order parameters calculated by TALOS-N36 indicate that the polyAla tract particularly populates α-helical conformations, while the rest of the protein remains largely disordered (Fig. 1D).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-21T13:45:19.055Z"}},{"start":261,"end":314,"reference_id":"38431667","reference_source":"pmid","reference_html":"Alternative low-populated conformations prompt phase transitions in polyalanine repeat expansions. <i> Antón R, Treviño MÁ, Pantoja-Uceda D, Félix S, Babu M, Cabrita EJ, Zweckstetter M, Tinnefeld P, Vera AM, Oroz J. </i> Nat Commun, 2024","date":"2024-04-18T08:14:46.487Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8PUI"}],"region_id":"DP04182r002","statement":[{"text":"NMR secondary chemical shift analysis and chemical shift-derived S2 order parameters calculated by TALOS-N36 indicate that the polyAla tract particularly populates α-helical conformations, while the rest of the protein remains largely disordered (Fig. 1D).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-21T13:45:19.865Z"}}],"regions_counter":2,"released":"2024_12","sequence":"MYKMEYSYLNSSAYESCMAGMDTSSLASAYADFSSCSQASGFQYNPIRTTFGATSGCPSLTPGSCSLGTLRDHQSSPYAAVPYKLFTDHGGLNEKRKQRRIRTTFTSAQLKELERVFAETHYPDIYTREELALKIDLTEARVQVWFQNRRAKFRKQERAAAAAAAAAKNGSSGKKSDSSRDDESKEAKSTDPDSTGGPGPNPNPTPSCGANGGGGGGPSPAGAPGAAGPGGPGGEPGKGGAAAAAAAAAAAAAAAAAAAAGGLAAAGGPGQGWAPGPGPITSIPDSLGGPFASVLSSLQRPNGAKAALVKSSMF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.4681528662420382,"dataset":["Cancer-related proteins"],"disorder_content":0.21337579617834396,"disprot_consensus":{"full":[{"start":228,"end":240,"type":"D"},{"start":261,"end":314,"type":"D"}],"Structural state":[{"start":228,"end":240,"type":"D"},{"start":261,"end":314,"type":"D"}]}},{"disprot_id":"DP04183","acc":"Q9ZHD1","creator":"cpintado","date":"2024-04-18T09:06:49.770Z","features":{"pfam":[{"id":"PF11604","name":"Copper binding periplasmic protein CusF","start":23,"end":89}],"gene3D":[]},"genes":[{"name":{"value":"ORF96","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAD11747.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD11747.1"}}]}}],"length":96,"name":"Copper ABC transporter substrate-binding protein","ncbi_taxon_id":90371,"organism":"Salmonella typhimurium","regions":[{"start":1,"end":21,"reference_id":"37394004","reference_source":"pmid","reference_html":"The battle for silver binding: How the interplay between the SilE, SilF, and SilB proteins contributes to the silver efflux pump mechanism. <i> Arrault C, Monneau YR, Martin M, Cantrelle FX, Boll E, Chirot F, Comby Zerbino C, Walker O, Hologne M. </i> J Biol Chem, 2023","date":"2024-04-18T09:08:48.799Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8C2Q"}],"region_id":"DP04183r001","statement":[{"text":"The first 21 residues are highly flexible and did not show any inter-residue NOE correlations.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-21T13:46:17.219Z"}}],"regions_counter":1,"released":"2024_12","sequence":"MLKHISHGDMNAASDASVQQVIKGTGIVKDIDMNSKKITISHEAIPAVGWPAMTMRFTFVNADDAINALKTGNHVDFSFIQQGNISLLKSINVTQS","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"],"alphafold_very_low_content":0.14583333333333334,"disorder_content":0.21875,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"}],"Structural state":[{"start":1,"end":21,"type":"D"}]}},{"disprot_id":"DP04184","acc":"P68633","creator":"cpintado","date":"2024-04-18T09:14:19.901Z","features":{"pfam":[{"id":"PF04584","name":"Poxvirus A28 family","start":2,"end":146}],"gene3D":[]},"genes":[{"name":{"value":"OPG155"},"orfNames":[{"value":"A28L"}],"olnNames":[{"value":"VACWR151"}]}],"length":146,"name":"Envelope protein OPG155","ncbi_taxon_id":10254,"organism":"Vaccinia virus (strain Western Reserve)","regions":[{"start":38,"end":67,"reference_id":"37948471","reference_source":"pmid","reference_html":"Structural and functional analysis of vaccinia viral fusion complex component protein A28 through NMR and molecular dynamic simulations. <i> Kao CF, Tsai MH, Carillo KJ, Tzou DL, Chang W. </i> PLoS Pathog, 2023","date":"2024-04-18T09:16:33.074Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"8GQO"}],"region_id":"DP04184r001","statement":[{"text":"The NMR structure of soluble tA28 revealed an α-β-α sandwich-like structural motif from residues 68–146, in which the β-strands are stabilized by multiple hydrogen bonds among strands sandwiched by two α-helices, whereas residues 38–67 were uncovered as a disordered domain.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-04-24T14:38:15.407Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MNSLSIFFIVVATAAVCLLFIQGYSIYENYGNIKEFNATHAAFEYSKSIGGTPALDRRVQDVNDTISDVKQKWRCVVYPGNGFVSASIFGFQAEVGPNNTRSIRKFNTMQQCIDFTFSDVININIYNPCVVPNINNAECQFLKSVL","taxonomy":["Viruses","Varidnaviria","Bamfordvirae","Nucleocytoviricota","Pokkesviricetes","Chitovirales","Poxviridae","Chordopoxvirinae","Orthopoxvirus","Vaccinia virus"],"dataset":["Viral proteins"],"disorder_content":0.2054794520547945,"disprot_consensus":{"full":[{"start":38,"end":67,"type":"D"}],"Structural state":[{"start":38,"end":67,"type":"D"}]}},{"disprot_id":"DP04185","acc":"C1LGM4","creator":"cpintado","date":"2024-04-18T09:20:54.821Z","features":{"pfam":[{"id":"PF00152","name":"tRNA synthetases class II (D, K and N)","start":225,"end":540},{"id":"PF01336","name":"OB-fold nucleic acid binding domain","start":127,"end":207},{"id":"PF20917","name":"Asparaginal-tRNA synthetase, N-terminal domain","start":18,"end":109}],"gene3D":[]},"genes":[{"name":{"value":"nars-prov","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAX73852.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAX73852.1"}}]},"orfNames":[{"value":"EWB00_000573","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"TNN16299.1","url":"https://www.ebi.ac.uk/ena/browser/view/TNN16299.1"}}]}]}],"length":546,"name":"Asparagine--tRNA ligase, cytoplasmic","ncbi_taxon_id":6182,"organism":"Schistosoma japonicum","regions":[{"start":74,"end":114,"reference_id":"37572327","reference_source":"pmid","reference_html":"Solution structure of the N-terminal extension domain of a <i>Schistosoma japonicum</i> asparaginyl-tRNA synthetase. <i> Peck Y, Pickering D, Mobli M, Liddell MJ, Wilson DT, Ruscher R, Ryan S, Buitrago G, McHugh C, Love NC, Pinlac T, Haertlein M, Kron MA, Loukas A, Daly NL. </i> J Biomol Struct Dyn, 2023","date":"2024-04-18T09:24:28.783Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8FA3"}],"region_id":"DP04185r001","statement":[{"text":"The backbone NH peaks of the well-structured region (residues 1–73) are highlighted in black, and the overlapped backbone NH peaks of the disordered region (residues 74–114) are highlighted in red, in the 2D 1H-15N HSQC spectrum (Supplementary Figure S2).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-21T13:47:02.933Z"}}],"regions_counter":1,"released":"2024_12","sequence":"MQIYTSEKRGSDTAGNGTEEAPLKTVLQAIVKLDGKIEADTRIWVDGTGDEMWDVVSKSKLKKATKQYHIQTKKQEKAPHEKIVSYENGDNVNLSEAINVQLTLDTKLPEAKELKIRDLQTMIDQRVCVFGWVHRIRRQSKTLMFIILRDGTGFLQCIFANNLCLTQEAITLSPESTVKVYGVVKQLPAGKSAPGGIELVADYWMVIGNAPAGGVDSVLTVESDIDTQLDNRHLVIRGENTAKVLRLISIALAAFRGHYIDRGYVEVLPPTFVQTQVEGGSTLFSLNYFGETAFMSQSSQLYLETCIPAIGDCFCITRSYRAEKSRTRRHLSEYNHVEAECPFIDFNGLLNRIEDLVVDVCDRIVKQSGDLLLDVNPQFKPPKGPFKRLKYEDAIVQLNNLGITNEDLTPFQFGDDIPEAPERRLVDTIGEPVLLTNFPAGLKAFYMLRTKGDPRLTDSVDLLVPGVGELVGGSMRMDNIDDLLKGYKSEEIDPTPYYWYTDQRKFGTCPHGGYGLGFERFCTWLLGKDHIRDVCLYPRFTSRCRP","taxonomy":["Eukaryota","Metazoa","Spiralia","Lophotrochozoa","Platyhelminthes","Trematoda","Digenea","Strigeidida","Schistosomatoidea","Schistosomatidae","Schistosoma"],"alphafold_very_low_content":0.03663003663003663,"dataset":["Neglected tropical diseases proteins"],"disorder_content":0.07509157509157509,"disprot_consensus":{"full":[{"start":74,"end":114,"type":"D"}],"Structural state":[{"start":74,"end":114,"type":"D"}]}},{"disprot_id":"DP04186","acc":"C7G3K3","creator":"cpintado","date":"2024-04-18T09:59:16.306Z","features":{"pfam":[{"id":"PF14866","name":"Long chain scorpion toxin, cysteine-stabilized alpha/beta domain","start":28,"end":79}],"gene3D":[]},"genes":[],"length":80,"name":"Peptide LaIT2","ncbi_taxon_id":431266,"organism":"Liocheles australasiae","regions":[{"start":22,"end":55,"reference_id":"35490851","reference_source":"pmid","reference_html":"Structural and functional studies of LaIT2, an antimicrobial and insecticidal peptide from Liocheles australasiae. <i> Tamura M, Tatsushiro C, Morita EH, Ohki S. </i> Toxicon, 2022","date":"2024-04-18T10:02:30.895Z","curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"7WKF"}],"region_id":"DP04186r001","statement":[{"text":"LaIT2 adopts a β-KTx-like structure with an unfolded N-domain and folded C-domain.","type":"Abstract"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-21T13:49:48.692Z"}}],"regions_counter":2,"released":"2024_12","sequence":"MAKHLIVMFLVIMVISSLVDCAKKPFVQRVKNAASKAYNKLKGLAMQSQYGCPIISNMCEDHCRRKKMEGQCDLLDCVCS","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Chelicerata","Arachnida","Scorpiones","Iurida","Scorpionoidea","Hemiscorpiidae","Liocheles"],"alphafold_very_low_content":0.0125,"disorder_content":0.425,"disprot_consensus":{"full":[{"start":22,"end":55,"type":"D"}],"Structural state":[{"start":22,"end":55,"type":"D"}]}},{"disprot_id":"DP04187","acc":"O25506","creator":"zskalman","date":"2024-05-03T09:01:34.870Z","features":{"pfam":[{"id":"PF00216","name":"Bacterial DNA-binding protein","start":1,"end":90}],"gene3D":[]},"genes":[{"name":{"value":"hup"},"olnNames":[{"value":"HP_0835"}]}],"length":94,"name":"DNA-binding protein HU","ncbi_taxon_id":85962,"organism":"Helicobacter pylori (strain ATCC 700392 / 26695)","regions":[{"start":55,"end":94,"reference_id":"29241299","reference_source":"pmid","reference_html":"NMR elucidation of monomer-dimer transition and conformational heterogeneity in histone-like DNA binding protein of Helicobacter pylori. <i> Jaiswal N, Raikwal N, Pandey H, Agarwal N, Arora A, Poluri KM, Kumar D. </i> Magn Reson Chem, 2018","date":"2024-10-21T14:26:38.767Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":1,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":6},{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":null,"value":310}],"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"region_id":"DP04187r001","sequence_construct":"GAMEMNKAEFIDLVKEAGKYNSKREAEEAISAFTLAVETALSKGESVELIGFGKFETAEQ\nKGKEGKVPGSDKTYKTEDKRVPKFKPGKTLKQKVEEGK","statement":[{"text":"Like D‐conformation of Hup, the secondary structure\nanalysis of M‐conformation revealed that it exhibits stable\nN‐terminal dimerization domain, whereas its C‐terminal\nDNA binding domain was found to be partially disordered\nas inferred by the significantly lower values of secondary\nshifts (i.e., <±0.2 ppm, Figure 2c).","type":"Results"},{"text":"Another important observation made here is that the C‐terminal half (from Glu55 to Lys94) was found to be disordered in monomeric M‐conformation (as evident from Figures 2c and 5c).","type":"Results"}]},{"start":55,"end":94,"reference_id":"29241299","reference_source":"pmid","reference_html":"NMR elucidation of monomer-dimer transition and conformational heterogeneity in histone-like DNA binding protein of Helicobacter pylori. <i> Jaiswal N, Raikwal N, Pandey H, Agarwal N, Arora A, Poluri KM, Kumar D. </i> Magn Reson Chem, 2018","date":"2024-10-21T14:26:27.647Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":1,"cross_refs":[{"db":"BMRB","id":"26942"}],"region_id":"DP04187r002","statement":[{"text":"Contrary to this, the HNN‐based amide correlations were\nnot discerned for D‐conformation of Hup suggesting that\nthis conformation is structurally stable and with slow\nmolecular tumbling rate—possibly due to its dimeric state\nin solution—rendering short T2 values for the amide spins.","type":"Results"},{"text":"The secondary structure analysis (Figure 2c) revealed that the D‐conformation of Hup at pH of 6.0 consists of (a) three α helical regions: Ile7‐Ala13 (α1), Lys19‐Ser38 (α2), and Lys84‐Glu92 (α3) and (b) five β strands: Glu41‐ Leu45 (β1), Gly49‐Gln56 (β2), Lys59‐Val63 (β3), Ser66‐ Glu73 (β4), and Arg76‐Gly83 (β5). ","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O25506"}],"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sequence_construct":"GAMEMNKAEFIDLVKEAGKY NSKREAEEAISAFTLAVETA LSKGESVELIGFGKFETAEQ KGKEGKVPGSDKTYKTEDKR VPKFKPGKTLKQKVEEGK","conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":null,"value":298}]},{"start":55,"end":94,"reference_id":"29241299","reference_source":"pmid","reference_html":"NMR elucidation of monomer-dimer transition and conformational heterogeneity in histone-like DNA binding protein of Helicobacter pylori. <i> Jaiswal N, Raikwal N, Pandey H, Agarwal N, Arora A, Poluri KM, Kumar D. </i> Magn Reson Chem, 2018","date":"2024-10-21T14:25:57.893Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":1,"cross_refs":[{"db":"BMRB","id":"26942"}],"region_id":"DP04187r003","statement":[{"text":"An important observation revealed by variable temperature study (temperature varied from 285 to 312 K) is that the protein undergoes a local, but reversible conformational change between D and M states with amid point around 300 +/−5 K for dimerization domain and around 305 +/−5 K for DNA binding domain.","type":"Results"},{"text":"The phenomenon of dimer dissociation was further corroborated by increased number of amide cross peaks (54 in number)corresponding to M‐conformation at 310 K compared to 48 peaks discerned at 298 K.","type":"Results"},{"text":"In solution the protein dimerize and the region is structured. When the monomeric form is encouraged (i.e by increasing the temperature) is possible to note that the same region is disordered. In the dimeric (D) form the C-terminal is ordered, while in the monomer form (M) this region is disordered.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O25506"}],"states_connection":[{"source":"DP04187r002","target":"DP04187r001"}],"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sequence_construct":"GAMEMNKAEFIDLVKEAGKY NSKREAEEAISAFTLAVETA LSKGESVELIGFGKFETAEQ KGKEGKVPGSDKTYKTEDKR VPKFKPGKTLKQKVEEGK","conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":null,"value":298},{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":null,"value":310}]}],"regions_counter":3,"released":"2024_12","sequence":"MNKAEFIDLVKEAGKYNSKREAEEAISAFTLAVETALSKGESVELIGFGKFETAEQKGKEGKVPGSDKTYKTEDKRVPKFKPGKTLKQKVEEGK","taxonomy":["Bacteria","Campylobacterota","Epsilonproteobacteria","Campylobacterales","Helicobacteraceae","Helicobacter"],"alphafold_very_low_content":0,"disorder_content":0.425531914893617,"disprot_consensus":{"full":[{"start":55,"end":94,"type":"T"}],"Structural state":[{"start":55,"end":94,"type":"D"}],"Structural transition":[{"start":55,"end":94,"type":"T"}]}},{"disprot_id":"DP04188","acc":"P49748","creator":"mlmarques","date":"2024-05-06T13:40:45.658Z","features":{"pfam":[{"id":"PF00441","name":"Acyl-CoA dehydrogenase, C-terminal domain","start":327,"end":473},{"id":"PF02770","name":"Acyl-CoA dehydrogenase, middle domain","start":213,"end":315},{"id":"PF02771","name":"Acyl-CoA dehydrogenase, N-terminal domain","start":103,"end":209},{"id":"PF21343","name":"ACAD9/ACADV, C-terminal domain","start":527,"end":647}],"gene3D":[]},"genes":[{"name":{"value":"ACADVL","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:92","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:92"}}]},"synonyms":[{"value":"VLCAD","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"7668252","url":"http://www.ncbi.nlm.nih.gov/pubmed/7668252","alternativeUrl":"https://europepmc.org/abstract/MED/7668252"}}]}]}],"length":655,"name":"Very long-chain specific acyl-CoA dehydrogenase, mitochondrial","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":486,"end":518,"reference_id":"18227065","reference_source":"pmid","reference_html":"Structural basis for substrate fatty acyl chain specificity: crystal structure of human very-long-chain acyl-CoA dehydrogenase. <i> McAndrew RP, Wang Y, Mohsen AW, He M, Vockley J, Kim JJ. </i> J Biol Chem, 2008","date":"2024-10-21T20:19:01.124Z","curator_id":"mlmarques","curator_name":"Monica Lopes Marques ","curator_orcid":"0000-0002-8597-4730","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"3B96"}],"region_id":"DP04188r001","statement":[{"text":"The electron density map is generally well ordered for the entire polypeptide chain with the exception of the first seven N-terminal amino acids and residues 446–478 (using the full-length mature VLCAD numbering scheme), which, therefore, were not included in the structural model.","type":"Results"},{"text":"However, the residues 446–478 are disordered in the VLCAD structure. Because of the proximity of residues both 445 and 479 to the surface (Fig. 4A), it is expected that the disordered residues also pack at the surface of the molecule. Fig. 4A shows a helix model built from residues 441–476, which include the disordered residues.","type":"Results"},{"text":"We have proposed that a region from residues 441 to 476 mediates membrane binding. This region is disordered in the crystal structure.","type":"Conclusion"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16238","entry_name":"FAD"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15532","entry_name":"myristoyl-CoA"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-22T12:51:14.471Z"}}],"regions_counter":1,"released":"2024_12","sequence":"MQAARMAASLGRQLLRLGGGSSRLTALLGQPRPGPARRPYAGGAAQLALDKSDSHPSDALTRKKPAKAESKSFAVGMFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPATGAVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVALQGCMDKGKELSGLGSALKNPFGNAGLLLGEAGKQLRRRAGLGSGLSLSGLVHPELSRSGELAVRALEQFATVVEAKLIKHKKGIVNEQFLLQRLADGAIDLYAMVVVLSRASRSLSEGHPTAQHEKMLCDTWCIEAAARIREGMAALQSDPWQQELYRNFKSISKALVERGGVVTSNPLGF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.10076335877862595,"disorder_content":0.050381679389312976,"disprot_consensus":{"full":[{"start":486,"end":518,"type":"D"}],"Structural state":[{"start":486,"end":518,"type":"D"}]}},{"disprot_id":"DP04189","acc":"P29372","creator":"mlmarques","date":"2024-05-06T15:55:04.379Z","features":{"pfam":[{"id":"PF02245","name":"Methylpurine-DNA glycosylase (MPG)","start":89,"end":283}],"gene3D":[]},"genes":[{"name":{"value":"MPG"},"synonyms":[{"value":"AAG"},{"value":"ANPG"},{"value":"MID1"}]}],"length":298,"name":"DNA-3-methyladenine glycosylase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":131,"end":141,"reference_id":"22148158","reference_source":"pmid","reference_html":"Searching for DNA lesions: structural evidence for lower- and higher-affinity DNA binding conformations of human alkyladenine DNA glycosylase. <i> Setser JW, Lingaraju GM, Davis CA, Samson LD, Drennan CL. </i> Biochemistry, 2012","date":"2024-05-07T11:19:54.051Z","curator_id":"mlmarques","curator_name":"Monica Lopes Marques ","curator_orcid":"0000-0002-8597-4730","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001171","ec_ontology":"ECO","ec_name":"crystallography evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"3UBY"}],"region_id":"DP04189r001","statement":[{"text":"The residues that lack electron density in the low-affinity complex, and are thus considered disordered, include Glu131- Arg141 (loop 1), Gly263 -Lys273 (loop 2), and C terminal residues after Asp289 (loop 3) (Figure 3A,B).","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1-Met83del","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Briefly, 84 residues at the N-terminus of the protein were truncated in this construct, and four extra residues from a PreScission Protease cleavage site (GE Healthcare) (Gly80, Pro81, His82, and Met83) were left behind after histidine tag cleavage. Therefore, Thr84 begins the wild-type AAG sequence, but four residues precede Thr84 such that Gly80 is now the N-terminus."}]}],"sequence_construct":"GPHMTRLGLEFFDQPAVPLARAFLGQVLVRRLPNGTELRGRIVETEAYLGPEDEAAHSRGGRQTPRNRGMFMKPGTLYVYIIYGMYFCMNISSQGDGACVLLRALEPLEGLETMRQLRSTLRKGTASRVLKDRELCSGPSKLCQALAINKSFDQRDLAQDEAVWLERGPLEPSEPAVVAAARVGVGHAGEWARKPLRFYVRGSPWVSVVDRVAEQDTQA","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-21T17:26:23.583Z"}},{"start":263,"end":273,"reference_id":"22148158","reference_source":"pmid","reference_html":"Searching for DNA lesions: structural evidence for lower- and higher-affinity DNA binding conformations of human alkyladenine DNA glycosylase. <i> Setser JW, Lingaraju GM, Davis CA, Samson LD, Drennan CL. </i> Biochemistry, 2012","date":"2024-05-07T11:18:43.865Z","curator_id":"mlmarques","curator_name":"Monica Lopes Marques ","curator_orcid":"0000-0002-8597-4730","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001171","ec_ontology":"ECO","ec_name":"crystallography evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"3UBY"}],"region_id":"DP04189r002","statement":[{"text":"The residues that lack electron density in the low-affinity complex, and are thus considered disordered, include Glu131- Arg141 (loop 1), Gly263 -Lys273 (loop 2), and C terminal residues after Asp289 (loop 3) (Figure 3A,B).","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1-Met83del","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Briefly, 84 residues at the N-terminus of the protein were truncated in this construct, and four extra residues from a PreScission Protease cleavage site (GE Healthcare) (Gly80, Pro81, His82, and Met83) were left behind after histidine tag cleavage. Therefore, Thr84 begins the wild-type AAG sequence, but four residues precede Thr84 such that Gly80 is now the N-terminus."}]}],"sequence_construct":"GPHMTRLGLEFFDQPAVPLARAFLGQVLVRRLPNGTELRGRIVETEAYLGPEDEAAHSRGGRQTPRNRGMFMKPGTLYVYIIYGMYFCMNISSQGDGACVLLRALEPLEGLETMRQLRSTLRKGTASRVLKDRELCSGPSKLCQALAINKSFDQRDLAQDEAVWLERGPLEPSEPAVVAAARVGVGHAGEWARKPLRFYVRGSPWVSVVDRVAEQDTQA","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-21T17:26:24.180Z"}},{"start":263,"end":273,"reference_id":"22148158","reference_source":"pmid","reference_html":"Searching for DNA lesions: structural evidence for lower- and higher-affinity DNA binding conformations of human alkyladenine DNA glycosylase. <i> Setser JW, Lingaraju GM, Davis CA, Samson LD, Drennan CL. </i> Biochemistry, 2012","date":"2024-10-21T18:13:59.744Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_12","version":1,"cross_refs":[{"db":"PDB","id":"3UBY"}],"region_id":"DP04189r003","statement":[{"text":"Figure 1B shows amino acid side and main chains in this region, are involved in DNA binding in the higher-affinity DNA binding conformation. This interaction also leads to the gain of structure in this region.","type":"Curator statement"}],"sequence_construct":"GPHMTRLGLEFFDQPAVPLARAFLGQVLVRRLPNGTELRGRIVETEAYLGPEDEAAHSRGGRQTPRNRGMFMKPGTLYVYIIYGMYFCMNISSQGDGACVLLRALEPLEGLETMRQLRSTLRKGTASRVLKDRELCSGPSKLCQALAINKSFDQRDLAQDEAVWLERGPLEPSEPAVVAAARVGVGHAGEWARKPLRFYVRGSPWVSVVDRVAEQDTQA","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"The protein is interacting with 13-mer single-stranded εC-containing DNA  with sequence 5′-GAC ATG εCTT GCC T-3′, εC being the inhibitor 3,N4-ethenocytosine."}]}],"ec_go":"EXP","term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false},{"start":131,"end":141,"reference_id":"22148158","reference_source":"pmid","reference_html":"Searching for DNA lesions: structural evidence for lower- and higher-affinity DNA binding conformations of human alkyladenine DNA glycosylase. <i> Setser JW, Lingaraju GM, Davis CA, Samson LD, Drennan CL. </i> Biochemistry, 2012","date":"2024-10-21T20:23:04.278Z","curator_id":"mlmarques","curator_name":"Monica Lopes Marques ","curator_orcid":"0000-0002-8597-4730","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0001171","ec_ontology":"ECO","ec_name":"crystallography evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"3UBY"}],"region_id":"DP04189r004","statement":[{"text":"Here, previously disordered loops are completely ordered to display the full potential of a continuous electrostatic surface for binding DNA; Tyr162 is fully inserted into the DNA, and a base lesion is bound tightly in the AAG active site.","type":"Discussion"},{"text":"After the release of the base-lesion contact, the active site and other loops of AAG would become partially disordered, decreasing the extent of order of the DNA \n binding surface, ultimately leaving AAG in its lower-affinity, nonspecific searching state once again.","type":"Discussion"}],"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1-Met83del","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Briefly, 84 residues at the N-terminus of the protein were truncated in this construct, and four extra residues from a PreScission Protease cleavage site (GE Healthcare) (Gly80, Pro81, His82, and Met83) were left behind after histidine tag cleavage. Therefore, Thr84 begins the wild-type AAG sequence, but four residues precede Thr84 such that Gly80 is now the N-terminus."}]}],"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"The protein is interacting with 13-mer single-stranded εC-containing DNA  with sequence 5′-GAC ATG εCTT GCC T-3′, εC being the inhibitor 3,N4-ethenocytosine."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-22T12:51:50.884Z"}},{"start":263,"end":273,"reference_id":"22148158","reference_source":"pmid","reference_html":"Searching for DNA lesions: structural evidence for lower- and higher-affinity DNA binding conformations of human alkyladenine DNA glycosylase. <i> Setser JW, Lingaraju GM, Davis CA, Samson LD, Drennan CL. </i> Biochemistry, 2012","date":"2024-10-21T20:26:14.091Z","curator_id":"mlmarques","curator_name":"Monica Lopes Marques ","curator_orcid":"0000-0002-8597-4730","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0001171","ec_ontology":"ECO","ec_name":"crystallography evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"3UBY"}],"region_id":"DP04189r005","statement":[{"text":"Here, previously disordered loops are completely ordered to display the full potential of a continuous electrostatic surface for binding DNA; Tyr162 is fully inserted into the DNA, and a base lesion is bound tightly in the AAG active site.","type":"Discussion"},{"text":"After the release of the base-lesion contact, the active site and other loops of AAG would become partially disordered, decreasing the extent of order of the DNA \n binding surface, ultimately leaving AAG in its lower-affinity, nonspecific searching state once again.","type":"Discussion"}],"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1-Met83del","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Briefly, 84 residues at the N-terminus of the protein were truncated in this construct, and four extra residues from a PreScission Protease cleavage site (GE Healthcare) (Gly80, Pro81, His82, and Met83) were left behind after histidine tag cleavage. Therefore, Thr84 begins the wild-type AAG sequence, but four residues precede Thr84 such that Gly80 is now the N-terminus."}]}],"sequence_construct":"GPHMTRLGLEFFDQPAVPLARAFLGQVLVRRLPNGTELRGRIVETEAYLGPEDEAAHSRGGRQTPRNRGMFMKPGTLYVYIIYGMYFCMNISSQGDGACVLLRALEPLEGLETMRQLRSTLRKGTASRVLKDRELCSGPSKLCQALAINKSFDQRDLAQDEAVWLERGPLEPSEPAVVAAARVGVGHAGEWARKPLRFYVRGSPWVSVVDRVAEQDTQA","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"The protein is interacting with 13-mer single-stranded εC-containing DNA  with sequence 5′-GAC ATG εCTT GCC T-3′, εC being the inhibitor 3,N4-ethenocytosine."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-22T12:51:51.665Z"}},{"start":131,"end":141,"reference_id":"22148158","reference_source":"pmid","reference_html":"Searching for DNA lesions: structural evidence for lower- and higher-affinity DNA binding conformations of human alkyladenine DNA glycosylase. <i> Setser JW, Lingaraju GM, Davis CA, Samson LD, Drennan CL. </i> Biochemistry, 2012","date":"2024-10-21T18:14:21.834Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"EXP","region_id":"DP04189r006","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"The protein is interacting with 13-mer single-stranded εC-containing DNA  with sequence 5′-GAC ATG εCTT GCC T-3′, εC being the inhibitor 3,N4-ethenocytosine."}]}],"statement":[{"text":"Figure 1B shows amino acid side and main chains in this region, are involved in DNA binding in the higher-affinity DNA binding conformation. This interaction also leads to the gain of structure in this region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"cross_refs":[{"db":"PDB","id":"3UBY"}],"sequence_construct":"GPHMTRLGLEFFDQPAVPLARAFLGQVLVRRLPNGTELRGRIVETEAYLGPEDEAAHSRGGRQTPRNRGMFMKPGTLYVYIIYGMYFCMNISSQGDGACVLLRALEPLEGLETMRQLRSTLRKGTASRVLKDRELCSGPSKLCQALAINKSFDQRDLAQDEAVWLERGPLEPSEPAVVAAARVGVGHAGEWARKPLRFYVRGSPWVSVVDRVAEQDTQA"}],"regions_counter":6,"released":"2024_12","sequence":"MVTPALQMKKPKQFCRRMGQKKQRPARAGQPHSSSDAAQAPAEQPHSSSDAAQAPCPRERCLGPPTTPGPYRSIYFSSPKGHLTRLGLEFFDQPAVPLARAFLGQVLVRRLPNGTELRGRIVETEAYLGPEDEAAHSRGGRQTPRNRGMFMKPGTLYVYIIYGMYFCMNISSQGDGACVLLRALEPLEGLETMRQLRSTLRKGTASRVLKDRELCSGPSKLCQALAINKSFDQRDLAQDEAVWLERGPLEPSEPAVVAAARVGVGHAGEWARKPLRFYVRGSPWVSVVDRVAEQDTQA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.19798657718120805,"disorder_content":0.0738255033557047,"disprot_consensus":{"full":[{"start":131,"end":141,"type":"T"},{"start":263,"end":273,"type":"T"}],"Structural state":[{"start":131,"end":141,"type":"D"},{"start":263,"end":273,"type":"D"}],"Molecular function":[{"start":131,"end":141,"type":"F"},{"start":263,"end":273,"type":"F"}],"Structural transition":[{"start":131,"end":141,"type":"T"},{"start":263,"end":273,"type":"T"}]}},{"disprot_id":"DP04190","acc":"P03170","creator":"ldobson","date":"2024-05-07T07:14:44.576Z","features":{"pfam":[{"id":"PF05363","name":"Herpesvirus US12 family","start":1,"end":82}],"gene3D":[]},"genes":[{"name":{"value":"US12"}}],"length":88,"name":"ICP47 protein","ncbi_taxon_id":10299,"organism":"Human herpesvirus 1 (strain 17)","regions":[{"start":4,"end":15,"reference_id":"10521276","reference_source":"pmid","reference_html":"Structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscopy. <i> Pfänder R, Neumann L, Zweckstetter M, Seger C, Holak TA, Tampé R. </i> Biochemistry, 1999","date":"2024-12-04T07:34:21.608Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04190r001","statement":[{"text":"In micellar solution of deuterated sodium dodecyl sulfate, the viral TAP inhibitor adopts an ordered structure. There are two helical regions extending from residues 4 to 15 and from residues 22 to 32.","type":"Abstract"}],"cross_refs":[{"db":"PDB","id":"1QLO"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"8984 ","entry_name":"sodium dodecyl sulfate"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-24T16:53:42.135Z"}},{"start":22,"end":32,"reference_id":"10521276","reference_source":"pmid","reference_html":"Structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscopy. <i> Pfänder R, Neumann L, Zweckstetter M, Seger C, Holak TA, Tampé R. </i> Biochemistry, 1999","date":"2024-12-04T07:36:56.452Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04190r002","statement":[{"text":"In micellar solution of deuterated sodium dodecyl sulfate, the viral TAP inhibitor adopts an ordered structure. There are two helical regions extending from residues 4 to 15 and from residues 22 to 32.","type":"Abstract"}],"cross_refs":[{"db":"PDB","id":"1QLO"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"8984 ","entry_name":"sodium dodecyl sulfate"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-24T16:53:42.458Z"}},{"start":1,"end":53,"reference_id":"9109681","reference_source":"pmid","reference_html":"Structure of the viral TAP-inhibitor ICP47 induced by membrane association. <i> Beinert D, Neumann L, Uebel S, Tampé R. </i> Biochemistry, 1997","date":"2024-05-07T07:39:31.339Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04190r003","statement":[{"text":"Surprisingly, the CD spectrum of ICP47(1-53) shows no characteristic of secondary structure in phosphate buffer (Figure 2A).","type":"Results"}],"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-22T14:22:46.885Z"}},{"start":1,"end":88,"reference_id":"9109681","reference_source":"pmid","reference_html":"Structure of the viral TAP-inhibitor ICP47 induced by membrane association. <i> Beinert D, Neumann L, Uebel S, Tampé R. </i> Biochemistry, 1997","date":"2024-10-22T14:27:12.858Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"region_id":"DP04190r005","statement":[{"text":"Surprisingly, the CD spectrum of ICP47(1−53) shows no characteristics of secondary structure in phosphate buffer (Figure 2a). The same result was obtained for full-length His-ICP47 (not shown).","type":"Results"}]},{"start":1,"end":88,"reference_id":"9109681","reference_source":"pmid","reference_html":"Structure of the viral TAP-inhibitor ICP47 induced by membrane association. <i> Beinert D, Neumann L, Uebel S, Tampé R. </i> Biochemistry, 1997","date":"2024-10-22T14:35:01.613Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04190r006","statement":[{"text":"At 10 and 37 °C, the fluorescence emission has its maximum at 355 nm, indicating that the tryptophan is completely solvent exposed (Figure 5). While hydrophobic side chains are usually buried in folded domains, the fluorescence data give further evidence that ICP47 is highly dynamic and mainly unstructured in aqueous solution.","type":"Results"}]},{"start":1,"end":13,"reference_id":"9109681","reference_source":"pmid","reference_html":"Structure of the viral TAP-inhibitor ICP47 induced by membrane association. <i> Beinert D, Neumann L, Uebel S, Tampé R. </i> Biochemistry, 1997","date":"2024-10-22T14:46:07.442Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04190r007","sample":[{"term_id":"IDPO:00489","term_name":"interacting membrane","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"45240","entry_name":"1,2-di-O-myristoyl-sn-glycero-3-phosphocholine"}],"statement":[{"text":"After addition of pure DMPC vesicles at 20 °C, the wavelength of the emission maximum remains constant and the fluorescence intensity increases slightly, reflecting only a very weak interaction of ICP47(1−53) with neutral changed phospholipids. By increasing the molar ratio of DMPG/DMPC vesicles, we observed drastic changes of the fluorescence emission. The emission maximum was shifted to 335 nm and the fluorescence intensity increased 2-fold. The changes of the secondary structure observed in different lipid charge densities are in very good agreement with the changes in tryptophan fluorescence.","type":"Results"},{"text":"However, in the presence of membrane mimetics, a drastic conformational change of ICP47 to a more α-helical structure was observed. This result is in line with secondary structure predictions, which propose two helices located within residues 3−13 and 35−43 (Figure 6a).","type":"Discussion"},{"text":"Therefore, we conclude that both predicted α-helices are formed under these conditions.","type":"Discussion"}]},{"start":1,"end":13,"reference_id":"9109681","reference_source":"pmid","reference_html":"Structure of the viral TAP-inhibitor ICP47 induced by membrane association. <i> Beinert D, Neumann L, Uebel S, Tampé R. </i> Biochemistry, 1997","date":"2024-10-22T15:11:35.707Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04190r008","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"84519","entry_name":"1,2-distearoyl-sn-glycero-3-phosphoserine"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"60523","entry_name":"phosphatidylglycerol(1-)"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"73246","entry_name":"1,2-dihexadecanoyl-sn-glycerol-3-phosphate"}],"statement":[{"text":"As summarized in Figure 3, lipid vesicles that contain negatively charged lipids, such as phosphatidic acid (PA), phosphatidylglycerol (PG), or phosphatidylserine (PS) (latter not shown), induce an α-helical conformation, whereas neutral or positively charged lipid vesicles, such as phosphatidylcholine (DMPC or POPC) or dihexadecyldimethylammonium bromide (DHDAB), hardly affect the secondary structure of ICP47(1−53). Therefore, we conclude that the viral TAP inhibitor adopts a more α-helical structure when bound to membranes and that negatively charged lipids induce membrane adsorption and conformational change.","type":"Results"},{"text":"However, in the presence of membrane mimetics, a drastic conformational change of ICP47 to a more α-helical structure was observed. This result is in line with secondary structure predictions, which propose two helices located within residues 3−13 and 35−43 (Figure 6a).","type":"Discussion"},{"text":"Therefore, we conclude that both predicted α-helices are formed under these conditions.","type":"Discussion"}]},{"start":1,"end":53,"reference_id":"9109681","reference_source":"pmid","reference_html":"Structure of the viral TAP-inhibitor ICP47 induced by membrane association. <i> Beinert D, Neumann L, Uebel S, Tampé R. </i> Biochemistry, 1997","date":"2024-10-22T16:32:25.790Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140313","term_name":"molecular sequestering activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001254","ec_ontology":"ECO","ec_name":"radioisotope assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"Q03518","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q03519","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04190r009","statement":[{"text":"Using a TAP inhibition assay as previously described (Ahn et al., 1996), we compared the activity of this fragment with the full-length protein expressed in E. coli. As summarized in Figure 1, we found the truncated ICP47(1−53) to be fully active with respect to inhibition of peptide binding to human TAP.","type":"Results"}],"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":53,"reference_id":"9109681","reference_source":"pmid","reference_html":"Structure of the viral TAP-inhibitor ICP47 induced by membrane association. <i> Beinert D, Neumann L, Uebel S, Tampé R. </i> Biochemistry, 1997","date":"2024-10-22T16:32:17.719Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0046977","term_name":"TAP binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006076","ec_ontology":"ECO","ec_name":"protein binding evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q03518","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q03519","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04190r010","statement":[{"text":"The binding constants of His-ICP47 and ICP47(1−53) for human TAP appear to be identical and were determined to be 50 and 60 nM, respectively. So we conclude that ICP47(1−53), lacking the redundant N-terminal fusion tag and the C-terminal domain, covers the active domain of the TAP inhibitor.","type":"Results"}],"term_comment":"","term_def":"\"Binding to TAP protein, transporter associated with antigen processing protein. TAP protein is a heterodimeric peptide transporter consisting of the subunits TAP1 and TAP2.\" [PMID:11133832]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":53,"reference_id":"9109681","reference_source":"pmid","reference_html":"Structure of the viral TAP-inhibitor ICP47 induced by membrane association. <i> Beinert D, Neumann L, Uebel S, Tampé R. </i> Biochemistry, 1997","date":"2024-10-22T15:14:18.059Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"84519","operator":null,"partner_start":null,"partner_end":null},{"db":"ChEBI","id":"60523","operator":"or","partner_start":null,"partner_end":null},{"db":"ChEBI","id":"73246","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP04190r011","statement":[{"text":"As summarized in Figure 3, lipid vesicles that contain negatively charged lipids, such as phosphatidic acid (PA), phosphatidylglycerol (PG), or phosphatidylserine (PS) (latter not shown), induce an α-helical conformation, whereas neutral or positively charged lipid vesicles, such as phosphatidylcholine (DMPC or POPC) or dihexadecyldimethylammonium bromide (DHDAB), hardly affect the secondary structure of ICP47(1−53). Therefore, we conclude that the viral TAP inhibitor adopts a more α-helical structure when bound to membranes and that negatively charged lipids induce membrane adsorption and conformational change.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":53,"reference_id":"9109681","reference_source":"pmid","reference_html":"Structure of the viral TAP-inhibitor ICP47 induced by membrane association. <i> Beinert D, Neumann L, Uebel S, Tampé R. </i> Biochemistry, 1997","date":"2024-10-22T15:15:59.915Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IDA","interaction_partner":[{"db":"ChEBI","id":"45240","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04190r012","statement":[{"text":"After addition of pure DMPC vesicles at 20 °C, the wavelength of the emission maximum remains constant and the fluorescence intensity increases slightly, reflecting only a very weak interaction of ICP47(1−53) with neutral changed phospholipids. By increasing the molar ratio of DMPG/DMPC vesicles, we observed drastic changes of the fluorescence emission. The emission maximum was shifted to 335 nm and the fluorescence intensity increased 2-fold. The changes of the secondary structure observed in different lipid charge densities are in very good agreement with the changes in tryptophan fluorescence.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":2,"end":34,"reference_id":"10521276","reference_source":"pmid","reference_html":"Structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscopy. <i> Pfänder R, Neumann L, Zweckstetter M, Seger C, Holak TA, Tampé R. </i> Biochemistry, 1999","date":"2024-10-22T16:32:47.551Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0032410","term_name":"negative regulation of transporter activity","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007122","ec_ontology":"ECO","ec_name":"in vitro assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IDA","region_id":"DP04190r013","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q03518"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q03519"}],"statement":[{"text":"ICP47(2−34) Blocks Peptide Binding to and Peptide Transport by TAP. The activity of the synthetic ICP47(2−34) was analyzed by an in vitro peptide transport assay based on specific N-glycosylation in microsomes. As shown in Figure 1A, ICP47(2−34) completely blocks TAP-specific peptide translocation of radiolabeled reporter peptides into microsomes.","type":"Results"}],"term_comment":"","term_def":"\"Any process that stops or reduces the activity of a transporter.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":2,"end":34,"reference_id":"10521276","reference_source":"pmid","reference_html":"Structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscopy. <i> Pfänder R, Neumann L, Zweckstetter M, Seger C, Holak TA, Tampé R. </i> Biochemistry, 1999","date":"2024-10-22T16:32:07.077Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0046977","term_name":"TAP binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007122","ec_ontology":"ECO","ec_name":"in vitro assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"Q03518","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q03519","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04190r014","statement":[{"text":"Moreover, we quantified the binding affinity of ICP47(2−34) to TAP and its ability to inhibit peptide binding by competition assays (Figure 1B). An affinity binding constant of Kd = 100 ± 14 nM was determined, which is in good agreement with the affinity constant for the full-length ICP47 ( 7, 8).","type":"Results"}],"term_comment":"","term_def":"\"Binding to TAP protein, transporter associated with antigen processing protein. TAP protein is a heterodimeric peptide transporter consisting of the subunits TAP1 and TAP2.\" [PMID:11133832]","term_is_obsolete":false,"term_not_annotate":false},{"start":2,"end":34,"reference_id":"10521276","reference_source":"pmid","reference_html":"Structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscopy. <i> Pfänder R, Neumann L, Zweckstetter M, Seger C, Holak TA, Tampé R. </i> Biochemistry, 1999","date":"2024-10-22T15:27:01.584Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140313","term_name":"molecular sequestering activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007122","ec_ontology":"ECO","ec_name":"in vitro assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"Q03518","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04190r015","statement":[{"text":"Moreover, we quantified the binding affinity of ICP47(2−34) to TAP and its ability to inhibit peptide binding by competition assays (Figure 1B). An affinity binding constant of Kd = 100 ± 14 nM was determined, which is in good agreement with the affinity constant for the full-length ICP47 ( 7, 8).","type":"Results"}],"term_comment":"","term_def":"\"The selective interaction of a protein with a specific molecule to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","term_is_obsolete":false,"term_not_annotate":false},{"start":2,"end":34,"reference_id":"10521276","reference_source":"pmid","reference_html":"Structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscopy. <i> Pfänder R, Neumann L, Zweckstetter M, Seger C, Holak TA, Tampé R. </i> Biochemistry, 1999","date":"2024-10-22T16:48:28.541Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005543","term_name":"phospholipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007122","ec_ontology":"ECO","ec_name":"in vitro assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IDA","region_id":"DP04190r016","statement":[{"text":"Microsomes prepared from noninfected insect cells were incubated with an increasing amount of radiolabeled ICP47(2−34) and washed, and the membrane-associated inhibitor was quantified. As shown in Figure 2 the polypeptide binds in a dose-dependent manner to microsomes, revealing an affinity constant Kd = 34 ± 9 μM. ICP47(2−34) shows a 350−400 times weaker affinity to microsomal membranes without than with human TAP.","type":"Results"},{"text":"Additionally, the membrane association explains the biphasic binding characteristics of ICP47 to TAP-containing microsomes (data not shown).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester.\" [ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false},{"start":4,"end":15,"reference_id":"10521276","reference_source":"pmid","reference_html":"Structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscopy. <i> Pfänder R, Neumann L, Zweckstetter M, Seger C, Holak TA, Tampé R. </i> Biochemistry, 1999","date":"2024-10-22T16:41:54.032Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04190r017","statement":[{"text":"The structure calculation shows that the conformation of the peptide bound to SDS consists of two major helices extending from residues 4 to 15 and from 22 to 32 (Figure 7).","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"8984","entry_name":"sodium dodecyl sulfate"}],"states_connection":[{"source":"DP04190r003","target":"DP04190r001"}],"cross_refs":[{"db":"PDB","id":"1QLO"}]},{"start":22,"end":32,"reference_id":"10521276","reference_source":"pmid","reference_html":"Structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscopy. <i> Pfänder R, Neumann L, Zweckstetter M, Seger C, Holak TA, Tampé R. </i> Biochemistry, 1999","date":"2024-10-22T16:41:45.637Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04190r018","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"8984","entry_name":"sodium dodecyl sulfate"}],"statement":[{"text":"The structure calculation shows that the conformation of the peptide bound to SDS consists of two major helices extending from residues 4 to 15 and from 22 to 32 (Figure 7).","type":"Results"}],"states_connection":[{"source":"DP04190r003","target":"DP04190r002"}],"cross_refs":[{"db":"PDB","id":"1QLO"}]}],"regions_counter":18,"released":"2024_12","sequence":"MSWALEMADTFLDTMRVGPRTYADVRDEINKRGREDREAARTAVHDPERPLLRSPGLLPEIAPNASLGVAHRRTGGTVTDSPRNPVTR","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Peploviricota","Herviviricetes","Herpesvirales","Orthoherpesviridae","Alphaherpesvirinae","Simplexvirus","Simplexvirus humanalpha1","Human herpesvirus 1"],"dataset":["Viral proteins"],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":15,"type":"T"},{"start":16,"end":21,"type":"D"},{"start":22,"end":32,"type":"T"},{"start":33,"end":88,"type":"D"}],"Structural state":[{"start":1,"end":88,"type":"D"}],"Structural transition":[{"start":1,"end":15,"type":"T"},{"start":22,"end":32,"type":"T"}],"Molecular function":[{"start":1,"end":53,"type":"F"}],"Biological process":[{"start":2,"end":34,"type":"F"}]}},{"disprot_id":"DP04191","acc":"Q99P72","creator":"ldobson","date":"2024-05-07T07:47:48.372Z","features":{"pfam":[{"id":"PF02453","name":"Reticulon","start":975,"end":1137}],"gene3D":[]},"genes":[{"name":{"value":"Rtn4","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:1915835","url":"http://www.informatics.jax.org/marker/MGI:1915835"}}]},"synonyms":[{"value":"Kiaa0886"},{"value":"Nogo","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"27786289","url":"http://www.ncbi.nlm.nih.gov/pubmed/27786289","alternativeUrl":"https://europepmc.org/abstract/MED/27786289"}}]}]}],"length":1162,"name":"Reticulon-4","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":1025,"end":1090,"reference_id":"20351248","reference_source":"pmid","reference_html":"Protein folding at the membrane interface, the structure of Nogo-66 requires interactions with a phosphocholine surface. <i> Vasudevan SV, Schulz J, Zhou C, Cocco MJ. </i> Proc Natl Acad Sci U S A, 2010","date":"2024-05-07T07:50:50.029Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04191r001","statement":[{"text":"We determined that the small amount of secondary structure evident in the CD spectrum is transient and not involved in a stable fold based on the following NMR data.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-22T16:52:36.490Z"}},{"start":1025,"end":1090,"reference_id":"20351248","reference_source":"pmid","reference_html":"Protein folding at the membrane interface, the structure of Nogo-66 requires interactions with a phosphocholine surface. <i> Vasudevan SV, Schulz J, Zhou C, Cocco MJ. </i> Proc Natl Acad Sci U S A, 2010","date":"2024-12-04T07:38:08.448Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"2KO2"}],"region_id":"DP04191r002","statement":[{"text":"The structure of Nogo-66 induced by DPC is a compact helical bundle consisting of five helices wrapping upon each other. Thirty-two of the 66 backbone amide hydrogens exchange slowly over a period of hours to days (Fig. S3B), indicating that Nogo-66 forms a stable fold on the DPC surface.","type":"Results"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sequence_construct":"MHHHHHHLVPRGMRIYKGVIQAIQKSDEGHPFRAYLESEVAISEELVQKYSNSALGHVNSTIKELRRLFLVDDLVDSLK","conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":4}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":100,"db":"PubChem","id":"CID:644308"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-05T13:06:19.662Z"}},{"start":1025,"end":1090,"reference_id":"20351248","reference_source":"pmid","reference_html":"Protein folding at the membrane interface, the structure of Nogo-66 requires interactions with a phosphocholine surface. <i> Vasudevan SV, Schulz J, Zhou C, Cocco MJ. </i> Proc Natl Acad Sci U S A, 2010","date":"2024-12-04T07:42:04.863Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"2KO2"}],"ec_go":"EXP","region_id":"DP04191r003","statement":[{"text":"Using NMR diffusion measurements we find Nogo-66 is fully bound to DPC at the concentrations used in our NMR experiments.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"78018","entry_name":"dodecylphosphocholine"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-05T13:06:34.693Z"}},{"start":1025,"end":1090,"reference_id":"20351248","reference_source":"pmid","reference_html":"Protein folding at the membrane interface, the structure of Nogo-66 requires interactions with a phosphocholine surface. <i> Vasudevan SV, Schulz J, Zhou C, Cocco MJ. </i> Proc Natl Acad Sci U S A, 2010","date":"2024-10-22T17:05:13.196Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04191r004","statement":[{"text":"In an aqueous environment, we find that Nogo-66 is largely disordered based on the following data. The CD spectrum of aqueous Nogo-66 indicates very little secondary structure (Fig. 1A, Red Trace).","type":"Results"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}]},{"start":1025,"end":1090,"reference_id":"20351248","reference_source":"pmid","reference_html":"Protein folding at the membrane interface, the structure of Nogo-66 requires interactions with a phosphocholine surface. <i> Vasudevan SV, Schulz J, Zhou C, Cocco MJ. </i> Proc Natl Acad Sci U S A, 2010","date":"2024-10-22T17:13:04.781Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"region_id":"DP04191r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"78018","entry_name":"dodecylphosphocholine"}],"statement":[{"text":"To determine the structural influence of phosphocholine (PC) on the fold of Nogo-66, we prepared DMPC lipid vesicles and collected CD data (Fig. 1A, Black Trace). Notably, Nogo-66 becomes significantly ordered in the presence of lipid vesicles, calculated to be 88% helix.","type":"Results"}]},{"start":1025,"end":1090,"reference_id":"20351248","reference_source":"pmid","reference_html":"Protein folding at the membrane interface, the structure of Nogo-66 requires interactions with a phosphocholine surface. <i> Vasudevan SV, Schulz J, Zhou C, Cocco MJ. </i> Proc Natl Acad Sci U S A, 2010","date":"2024-10-22T17:17:06.419Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"region_id":"DP04191r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"78018","entry_name":"dodecylphosphocholine"}],"statement":[{"text":"To determine the structural influence of phosphocholine (PC) on the fold of Nogo-66, we prepared DMPC lipid vesicles and collected CD data (Fig. 1A, Black Trace). Notably, Nogo-66 becomes significantly ordered in the presence of lipid vesicles, calculated to be 88% helix.","type":"Results"}],"states_connection":[{"source":"DP04191r004","target":"DP04191r005"}]},{"start":1025,"end":1090,"reference_id":"20351248","reference_source":"pmid","reference_html":"Protein folding at the membrane interface, the structure of Nogo-66 requires interactions with a phosphocholine surface. <i> Vasudevan SV, Schulz J, Zhou C, Cocco MJ. </i> Proc Natl Acad Sci U S A, 2010","date":"2024-10-22T17:11:31.568Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"cross_refs":[{"db":"PDB","id":"2KO2"}],"region_id":"DP04191r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"78018","entry_name":"dodecylphosphocholine"}],"statement":[{"text":"The structure of Nogo-66 induced by DPC is a compact helical bundle consisting of five helices wrapping upon each other. Thirty-two of the 66 backbone amide hydrogens exchange slowly over a period of hours to days (Fig. S3B), indicating that Nogo-66 forms a stable fold on the DPC surface","type":"Results"}],"states_connection":[{"source":"DP04191r001","target":"DP04191r002"}]}],"regions_counter":7,"released":"2024_12","sequence":"MEDIDQSSLVSSSADSPPRPPPAFKYQFVTEPEDEEDEEDEEEEEDDEDLEELEVLERKPAAGLSAAPVPPAAAPLLDFSSDSVPPAPRGPLPAAPPTAPERQPSWERSPAASAPSLPPAAAVLPSKLPEDDEPPARPPAPAGASPLAEPAAPPSTPAAPKRRGSGSVDETLFALPAASEPVIPSSAEKIMDLKEQPGNTVSSGQEDFPSVLFETAASLPSLSPLSTVSFKEHGYLGNLSAVASTEGTIEETLNEASRELPERATNPFVNRESAEFSVLEYSEMGSSFNGSPKGESAMLVENTKEEVIVRSKDKEDLVCSAALHNPQESPATLTKVVKEDGVMSPEKTMDIFNEMKMSVVAPVREEYADFKPFEQAWEVKDTYEGSRDVLAARANMESKVDKKCFEDSLEQKGHGKDSESRNENASFPRTPELVKDGSRAYITCDSFSSATESTAANIFPVLEDHTSENKTDEKKIEERKAQIITEKTSPKTSNPFLVAIHDSEADYVTTDNLSKVTEAVVATMPEGLTPDLVQEACESELNEATGTKIAYETKVDLVQTSEAIQESIYPTAQLCPSFEEAEATPSPVLPDIVMEAPLNSLLPSTGASVAQPSASPLEVPSPVSYDGIKLEPENPPPYEEAMSVALKTSDSKEEIKEPESFNAAAQEAEAPYISIACDLIKETKLSTEPSPEFSNYSEIAKFEKSVPDHCELVDDSSPESEPVDLFSDDSIPEVPQTQEEAVMLMKESLTEVSETVTQHKHKERLSASPQEVGKPYLESFQPNLHITKDAASNEIPTLTKKETISLQMEEFNTAIYSNDDLLSSKEDKMKESETFSDSSPIEIIDEFPTFVSAKDDSPKEYTDLEVSNKSEIANVQSGANSLPCSELPCDLSFKNTYPKDEAHVSDEFSKSRSSVSKVPLLLPNVSALESQIEMGNIVKPKVLTKEAEEKLPSDTEKEDRSLTAVLSAELNKTSVVDLLYWRDIKKTGVVFGASLFLLLSLTVFSIVSVTAYIALALLSVTISFRIYKGVIQAIQKSDEGHPFRAYLESEVAISEELVQKYSNSALGHVNSTIKELRRLFLVDDLVDSLKFAVLMWVFTYVGALFNGLTLLILALISLFSIPVIYERHQAQIDHYLGLANKSVKDAMAKIQAKIPGLKRKAE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"alphafold_very_low_content":0.8201376936316696,"disorder_content":0.05679862306368331,"disprot_consensus":{"full":[{"start":1025,"end":1090,"type":"T"}],"Structural state":[{"start":1025,"end":1090,"type":"D"}],"Molecular function":[{"start":1025,"end":1090,"type":"F"}],"Structural transition":[{"start":1025,"end":1090,"type":"T"}]}},{"disprot_id":"DP04192","acc":"P69019","creator":"ldobson","date":"2024-05-07T08:08:16.647Z","features":{"pfam":[{"id":"PF03032","name":"Frog skin active peptide family signal and propeptide","start":2,"end":49}],"gene3D":[]},"genes":[],"length":72,"name":"Aurein-2.5","ncbi_taxon_id":8371,"organism":"Ranoidea aurea","regions":[{"start":50,"end":65,"reference_id":"31358802","reference_source":"pmid","reference_html":"Temporin L and aurein 2.5 have identical conformations but subtly distinct membrane and antibacterial activities. <i> Manzo G, Ferguson PM, Hind CK, Clifford M, Gustilo VB, Ali H, Bansal SS, Bui TT, Drake AF, Atkinson RA, Sutton JM, Lorenz CD, Phoenix DA, Mason AJ. </i> Sci Rep, 2019","date":"2024-05-07T08:10:27.812Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04192r001","statement":[{"text":"After binding to lipid bilayers, in the steady-state far-UV CD again indicates similar ordered α-helix conformations are adopted by both peptides; in the absence of lipid both peptides adopt disordered conformations (Fig. S4).\n","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-22T17:29:21.651Z"}},{"start":50,"end":65,"reference_id":"31358802","reference_source":"pmid","reference_html":"Temporin L and aurein 2.5 have identical conformations but subtly distinct membrane and antibacterial activities. <i> Manzo G, Ferguson PM, Hind CK, Clifford M, Gustilo VB, Ali H, Bansal SS, Bui TT, Drake AF, Atkinson RA, Sutton JM, Lorenz CD, Phoenix DA, Mason AJ. </i> Sci Rep, 2019","date":"2024-11-25T15:57:40.782Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04192r002","statement":[{"text":"After binding to lipid bilayers, in the steady-state far-UV CD again indicates similar ordered α-helix conformations are adopted by both peptides; in the absence of lipid both peptides adopt disordered conformations (Fig. S4).\n","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"3423265 "}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-03T18:07:16.945Z"}},{"start":50,"end":65,"reference_id":"31358802","reference_source":"pmid","reference_html":"Temporin L and aurein 2.5 have identical conformations but subtly distinct membrane and antibacterial activities. <i> Manzo G, Ferguson PM, Hind CK, Clifford M, Gustilo VB, Ali H, Bansal SS, Bui TT, Drake AF, Atkinson RA, Sutton JM, Lorenz CD, Phoenix DA, Mason AJ. </i> Sci Rep, 2019","date":"2024-11-25T16:02:49.132Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"6GS9"},{"db":"BMRB","id":"34284"}],"region_id":"DP04192r003","statement":[{"text":"In SDS, both the far-UV CD and the NMR structures agree that both peptides\nadopt ordered α-helix conformations.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"3423265  "}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-03T18:09:47.381Z"}},{"start":50,"end":65,"reference_id":"31358802","reference_source":"pmid","reference_html":"Temporin L and aurein 2.5 have identical conformations but subtly distinct membrane and antibacterial activities. <i> Manzo G, Ferguson PM, Hind CK, Clifford M, Gustilo VB, Ali H, Bansal SS, Bui TT, Drake AF, Atkinson RA, Sutton JM, Lorenz CD, Phoenix DA, Mason AJ. </i> Sci Rep, 2019","date":"2024-12-04T07:42:57.599Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"EXP","region_id":"DP04192r004","statement":[{"text":"This shows that, while secondary amphipathic α-helix conformations are a vital element in the binding and disruption of bacterial plasma membranes, individual amino acids in the distinct structures make important structural and dynamic contributions that determine the precise mechanism of action, potency and species selectivity of AMPs.","type":"Conclusion"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"3423265  "}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-05T13:07:37.498Z"}},{"start":50,"end":65,"reference_id":"31358802","reference_source":"pmid","reference_html":"Temporin L and aurein 2.5 have identical conformations but subtly distinct membrane and antibacterial activities. <i> Manzo G, Ferguson PM, Hind CK, Clifford M, Gustilo VB, Ali H, Bansal SS, Bui TT, Drake AF, Atkinson RA, Sutton JM, Lorenz CD, Phoenix DA, Mason AJ. </i> Sci Rep, 2019","date":"2025-03-24T16:17:49.408Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0050829","term_name":"defense response to Gram-negative bacterium","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007699","ec_ontology":"ECO","ec_name":"cell growth assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","region_id":"DP04192r005","statement":[{"text":"In the present study, temporin L is shown to be more potent than aurein 2.5 against all strains included in both the Gram-positive and Gram-negative bacteria panels and Candida albicans (Table 2). For the Gram-positive strains, aurein 2.5 is outperformed by temporin L with, on average a 7.6-fold greater potency for the latter. For the Gram-negative strains, the difference between the potency of aurein 2.5 and temporin L is less, notably for both Acinetobacter baumannii isolates.","type":"Results"}],"term_comment":"","term_def":"\"Reactions triggered in response to the presence of a Gram-negative bacterium that act to protect the cell or organism.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":50,"end":65,"reference_id":"31358802","reference_source":"pmid","reference_html":"Temporin L and aurein 2.5 have identical conformations but subtly distinct membrane and antibacterial activities. <i> Manzo G, Ferguson PM, Hind CK, Clifford M, Gustilo VB, Ali H, Bansal SS, Bui TT, Drake AF, Atkinson RA, Sutton JM, Lorenz CD, Phoenix DA, Mason AJ. </i> Sci Rep, 2019","date":"2025-03-24T16:17:59.356Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0050830","term_name":"defense response to Gram-positive bacterium","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007699","ec_ontology":"ECO","ec_name":"cell growth assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","region_id":"DP04192r006","statement":[{"text":"In the present study, temporin L is shown to be more potent than aurein 2.5 against all strains included in both the Gram-positive and Gram-negative bacteria panels and Candida albicans (Table 2). For the Gram-positive strains, aurein 2.5 is outperformed by temporin L with, on average a 7.6-fold greater potency for the latter. For the Gram-negative strains, the difference between the potency of aurein 2.5 and temporin L is less, notably for both Acinetobacter baumannii isolates.","type":"Results"}],"term_comment":"","term_def":"\"Reactions triggered in response to the presence of a Gram-positive bacterium that act to protect the cell or organism.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":50,"end":65,"reference_id":"31358802","reference_source":"pmid","reference_html":"Temporin L and aurein 2.5 have identical conformations but subtly distinct membrane and antibacterial activities. <i> Manzo G, Ferguson PM, Hind CK, Clifford M, Gustilo VB, Ali H, Bansal SS, Bui TT, Drake AF, Atkinson RA, Sutton JM, Lorenz CD, Phoenix DA, Mason AJ. </i> Sci Rep, 2019","date":"2025-03-24T16:21:13.602Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0035915","term_name":"pore formation in membrane of another organism","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04192r007","statement":[{"text":"In the present study, temporin L is shown to be more potent than aurein 2.5 against all strains included in both the Gram-positive and Gram-negative bacteria panels and Candida albicans (Table 2). For the Gram-positive strains, aurein 2.5 is outperformed by temporin L with, on average a 7.6-fold greater potency for the latter. For the Gram-negative strains, the difference between the potency of aurein 2.5 and temporin L is less, notably for both Acinetobacter baumannii isolates.","type":"Results"},{"text":"In contrast, in the present study both aurein 2.5 and temporin L were found to be capable of inducing channel like activity (Fig. 6). For aurein 2.5 this was observed in both membrane types (Fig. 6A,B) whereas for temporin L this was only found when challenging membranes formed from DPhPG (Fig. 6D).","type":"Results"},{"text":"This shows that, while secondary amphipathic α-helix conformations are a vital element in the binding and disruption of bacterial plasma membranes, individual amino acids in the distinct structures make important structural and dynamic contributions that determine the precise mechanism of action, potency and species selectivity of AMPs.","type":"Conclusion"}],"term_comment":"","term_def":"\"The aggregation, arrangement and bonding together of a set of components by an organism to form a pore complex in a membrane of another organism.\" [GOC:bf, GOC:fj, PMID:21549739]","term_is_obsolete":false,"term_not_annotate":false},{"start":50,"end":65,"reference_id":"31358802","reference_source":"pmid","reference_html":"Temporin L and aurein 2.5 have identical conformations but subtly distinct membrane and antibacterial activities. <i> Manzo G, Ferguson PM, Hind CK, Clifford M, Gustilo VB, Ali H, Bansal SS, Bui TT, Drake AF, Atkinson RA, Sutton JM, Lorenz CD, Phoenix DA, Mason AJ. </i> Sci Rep, 2019","date":"2025-03-24T16:50:26.184Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0015267","term_name":"channel activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006006","ec_ontology":"ECO","ec_name":"electrophysiology assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","region_id":"DP04192r008","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:449312","statements":[{"type":"Curator statement","text":"DPhPG bilayers mimick Gram-positive bacteria cytoplasmic membranes."}]},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:102081740","statements":[{"type":"Curator statement","text":"DPhPE:DPhPG (60:40 mol:mol) mimickGram-negative bacteria cytoplasmic membranes."}]}],"statement":[{"text":"Similar to aurein 2.5, temporin L has channel like activity when challenging DPhPG membranes.","type":"Results"},{"text":"In contrast, in the present study both aurein 2.5 and temporin L were found to be capable of inducing channel like activity (Fig. 6). For aurein 2.5 this was observed in both membrane types (Fig. 6A,B) whereas for temporin L this was only found when challenging membranes formed from DPhPG (Fig. 6D).","type":"Results"}],"term_comment":"","term_def":"\"Enables the energy-independent facilitated diffusion, mediated by passage of a solute through a transmembrane aqueous pore or channel. Stereospecificity is not exhibited but this transport may be specific for a particular molecular species or class of molecules.\" [GOC:mtg_transport, ISBN:0815340729]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":8,"released":"2024_12","sequence":"MAFLKKSLFLVLFLGLVSLSICEKEKRQNEEDEDENEAANHEEGSEEKRGLFDIVKKVVGAFGSLGKRNDLE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Amphibia","Batrachia","Anura","Neobatrachia","Hyloidea","Hylidae","Pelodryadinae","Ranoidea"],"alphafold_very_low_content":0.06944444444444445,"disorder_content":0.2222222222222222,"disprot_consensus":{"full":[{"start":50,"end":65,"type":"T"}],"Structural state":[{"start":50,"end":65,"type":"D"}],"Structural transition":[{"start":50,"end":65,"type":"T"}],"Molecular function":[{"start":50,"end":65,"type":"F"}],"Biological process":[{"start":50,"end":65,"type":"F"}]}},{"disprot_id":"DP04193","acc":"P12969","creator":"ldobson","date":"2024-05-07T09:09:32.324Z","features":{"pfam":[{"id":"PF00214","name":"Calcitonin / CGRP / IAPP family","start":32,"end":77}],"gene3D":[]},"genes":[{"name":{"value":"Iapp"}}],"length":93,"name":"Islet amyloid polypeptide","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions":[{"start":55,"end":74,"reference_id":"19456151","reference_source":"pmid","reference_html":"Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy. <i> Nanga RP, Brender JR, Xu J, Hartman K, Subramanian V, Ramamoorthy A. </i> J Am Chem Soc, 2009","date":"2024-11-25T16:02:48.733Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"2KJ7"},{"db":"BMRB","id":"16314"}],"region_id":"DP04193r001","statement":[{"text":"The remainder of the peptide on the C-terminal end from\nGly24–Tyr37 is predominantly disordered.","type":"Results"},{"text":"This difference in backbone rmsd clearly shows that the 5–17 region of rat IAPP is relatively stable and that the helical region from residues 18–23 is more disordered.","type":"Results"},{"text":"Numbering is not according to Uniprot reference.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"644308"}],"sequence_construct":"KCNTATCATQRLANFLVRSSNNLGPVLPPTNVGSNTYX","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-23T14:19:09.966Z"}},{"start":38,"end":74,"reference_id":"17123962","reference_source":"pmid","reference_html":"Direct detection of transient alpha-helical states in islet amyloid polypeptide. <i> Williamson JA, Miranker AD. </i> Protein Sci, 2007","date":"2024-05-08T15:08:58.015Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"BMRB","id":"7311"}],"region_id":"DP04193r004","statement":[{"text":"The chemical shift dispersion was typical of a disordered peptide, yet there was sufficient resolution to identify all resonances.","type":"Results"}]},{"start":38,"end":54,"reference_id":"19456151","reference_source":"pmid","reference_html":"Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy. <i> Nanga RP, Brender JR, Xu J, Hartman K, Subramanian V, Ramamoorthy A. </i> J Am Chem Soc, 2009","date":"2024-11-25T16:09:50.485Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"16314"},{"db":"PDB","id":"2KJ7"}],"region_id":"DP04193r005","statement":[{"text":"Taken together, the NOE and CSI data support the presence of a predominantly α-helical structure within the Ala5–Leu23 region, with the stretch of residues from Ala5–Val17 and Ser20–Leu23 acting as a more stable core.","type":"Results"},{"text":"Numbering is not according to Uniprot reference.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"644308"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-23T14:19:07.927Z"}},{"start":38,"end":54,"reference_id":"19456151","reference_source":"pmid","reference_html":"Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy. <i> Nanga RP, Brender JR, Xu J, Hartman K, Subramanian V, Ramamoorthy A. </i> J Am Chem Soc, 2009","date":"2024-11-25T16:01:35.305Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP04193r006","statement":[{"text":"The CD spectra suggested\nthat the rIAPP–DPC micelle was quite stable even after several months and the peptide had\nsignificant helical structure in micelles, indicating that rIAPP remained bound to the DPC\nmicelle.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"644308"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-23T14:19:05.653Z"}},{"start":38,"end":54,"reference_id":"19456151","reference_source":"pmid","reference_html":"Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy. <i> Nanga RP, Brender JR, Xu J, Hartman K, Subramanian V, Ramamoorthy A. </i> J Am Chem Soc, 2009","date":"2024-11-25T16:01:46.452Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"2KJ7"},{"db":"BMRB","id":"16314"}],"region_id":"DP04193r007","statement":[{"text":"Taken together evidences from pmid:19456151 and pmid:17123962 it seems that rIAAP undergoes structural transition in DPC micelles.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"644308"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-23T14:19:06.075Z"}}],"regions_counter":7,"released":"2024_06","sequence":"MRCISRLPAVLLILSVALGHLRATPVGSGTNPQVDKRKCNTATCATQRLANFLVRSSNNLGPVLPPTNVGSNTYGKRNVAEDPNRESLDFLLL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"alphafold_very_low_content":0.010752688172043012,"disorder_content":0.3978494623655914,"disprot_consensus":{"full":[{"start":38,"end":54,"type":"T"},{"start":55,"end":74,"type":"D"}],"Structural state":[{"start":38,"end":74,"type":"D"}],"Molecular function":[{"start":38,"end":54,"type":"F"}],"Structural transition":[{"start":38,"end":54,"type":"T"}]}},{"disprot_id":"DP04195","acc":"Q4WE50","creator":"rpancsa","date":"2024-05-07T11:53:01.275Z","features":{"pfam":[{"id":"PF12754","name":"Get5, N-terminal domain","start":48,"end":198},{"id":"PF17183","name":"Get5, C-terminal domain","start":221,"end":271}],"gene3D":[]},"genes":[{"name":{"value":"get5","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"22262836","url":"http://www.ncbi.nlm.nih.gov/pubmed/22262836","alternativeUrl":"https://europepmc.org/abstract/MED/22262836"}}]},"orfNames":[{"value":"AFUA_5G01770"}]}],"length":272,"name":"Golgi to ER traffic protein 5","ncbi_taxon_id":330879,"organism":"Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)","regions":[{"start":159,"end":186,"reference_id":"22262836","reference_source":"pmid","reference_html":"Get5 carboxyl-terminal domain is a novel dimerization motif that tethers an extended Get4/Get5 complex. <i> Chartron JW, VanderVelde DG, Rao M, Clemons WM. </i> J Biol Chem, 2012","date":"2024-05-07T13:46:27.081Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04195r001","statement":[{"text":"Main chain chemical shifts indicated that residues 159–186 are likely random coil whereas 212–228 and 195–208 formed helices corresponding to H1 and H2 (supplemental Fig. 2B).","type":"Results"},{"text":"Residues 159–185 did not converge to a consistent structure due to a lack of interresidue NOE-derived distance restraints and were omitted from the final structure calculation.","type":"Results"}],"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Methods","text":"All NMR measurements were collected using a Varian INOVA 600 MHz spectrometer at 25 °C with a triple resonance probe."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:22:33.671Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MSTVDQSTVTTALSSSSSNRHQGNDTYSIPKHSGTTSTITITMNEVSFVKSYLSTLDSRPIKLRSDHVFDPEQVGLRVPYTLPRLHAPHPEMPKKTKQPLAPGSSKSITVHLKSARNPALEFSLPNTALTTTSVQDLKDAVRERVTDAQGNKISLDKIKILYKRKPVTGKTIAEVLADEPVRLSGGKEVEFGVMIIGGAQVAVSAGAGERASAEQKESYEPPKPAVGPSGESVVATEAFWDDLQGFLEQRLKDYDEANKLRVLFKEAWRSSF","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Eurotiomycetes","Eurotiomycetidae","Eurotiales","Aspergillaceae","Aspergillus","Aspergillus subgen. Fumigati"],"alphafold_very_low_content":0.22426470588235295,"disorder_content":0.10294117647058823,"disprot_consensus":{"full":[{"start":159,"end":186,"type":"D"}],"Structural state":[{"start":159,"end":186,"type":"D"}]}},{"disprot_id":"DP04196","acc":"Q12285","creator":"rpancsa","date":"2024-05-07T13:55:27.912Z","features":{"pfam":[{"id":"PF00240","name":"Ubiquitin family","start":80,"end":150},{"id":"PF16843","name":"Binding domain to Get4 on Get5, Golgi to ER traffic protein","start":8,"end":59},{"id":"PF18514","name":"Ubiquitin-like protein MDY2, C-terminal domain","start":175,"end":212}],"gene3D":[]},"genes":[{"name":{"value":"MDY2"},"synonyms":[{"value":"GET5"},{"value":"TMA24"}],"olnNames":[{"value":"YOL111C"}]}],"length":212,"name":"Ubiquitin-like protein MDY2","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":152,"end":175,"reference_id":"22262836","reference_source":"pmid","reference_html":"Get5 carboxyl-terminal domain is a novel dimerization motif that tethers an extended Get4/Get5 complex. <i> Chartron JW, VanderVelde DG, Rao M, Clemons WM. </i> J Biol Chem, 2012","date":"2024-05-07T14:00:05.523Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Methods","text":"All NMR measurements were collected using a Varian INOVA 600 MHz spectrometer at 25 °C with a triple resonance probe."}]}],"region_id":"DP04196r001","statement":[{"text":"The main chain chemical shifts (1HN, 15NN, 13CCO, 13Cα, 13Cβ, and 1Hα) of residues 152–175 have random coil character, whereas those of 179–190 and 194–210 are characteristic of helices (supplemental Fig. S2A).","type":"Results"},{"text":"Relaxation rates and heteronuclear NOE values also indicate rapid motions for residues 152–175.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:21:35.313Z"}},{"start":152,"end":177,"reference_id":"22262836","reference_source":"pmid","reference_html":"Get5 carboxyl-terminal domain is a novel dimerization motif that tethers an extended Get4/Get5 complex. <i> Chartron JW, VanderVelde DG, Rao M, Clemons WM. </i> J Biol Chem, 2012","date":"2024-05-07T14:01:42.169Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006196","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Methods","text":"All NMR measurements were collected using a Varian INOVA 600 MHz spectrometer at 25 °C with a triple resonance probe."}]}],"region_id":"DP04196r002","statement":[{"text":"Consistent with this secondary structure, 1HN of residues 182–187 and 200–208 were the most protected from solvent deuterium exchange whereas residues 152–177 readily exchanged. Therefore, we concluded that residues 152–175 were unstructured and not significantly contributing to the stability of the folded dimerization domain.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:21:37.581Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MSTSASGPEHEFVSKFLTLATLTEPKLPKSYTKPLKDVTNLGVPLPTLKYKYKQNRAKKLKLHQDQQGQDNAAVHLTLKKIQAPKFSIEHDFSPSDTILQIKQHLISEEKASHISEIKLLLKGKVLHDNLFLSDLKVTPANSTITVMIKPNPTISKEPEAEKSTNSPAPAPPQELTVPWDDIEALLKNNFENDQAAVRQVMERLQKGWSLAK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.1320754716981132,"disorder_content":0.12264150943396226,"disprot_consensus":{"full":[{"start":152,"end":177,"type":"D"}],"Structural state":[{"start":152,"end":177,"type":"D"}]}},{"disprot_id":"DP04197","acc":"P35187","creator":"zskalman","date":"2024-05-07T15:20:28.520Z","features":{"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":680,"end":851},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":891,"end":995},{"id":"PF09382","name":"RQC domain","start":1081,"end":1196},{"id":"PF11408","name":"Sgs1 RecQ helicase","start":1271,"end":1349},{"id":"PF16124","name":"RecQ zinc-binding","start":1007,"end":1073}],"gene3D":[]},"genes":[{"name":{"value":"SGS1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"7969174","url":"http://www.ncbi.nlm.nih.gov/pubmed/7969174","alternativeUrl":"https://europepmc.org/abstract/MED/7969174"}}]},"synonyms":[{"value":"TPS1","evidences":[{"code":"ECO:0000303","source":{"name":"Citation","id":"Ref.3","url":"https://www.uniprot.org/uniprot/null#ref3"}}]}],"orfNames":[{"value":"YM9646.02C"}],"olnNames":[{"value":"YMR190C","evidences":[{"code":"ECO:0000312","source":{"name":"SGD","id":"S000004802","url":"https://www.yeastgenome.org/cgi-bin/locus.fpl?dbid=S000004802"}}]}]}],"length":1447,"name":"ATP-dependent helicase SGS1","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":125,"reference_id":"24038467","reference_source":"pmid","reference_html":"A transient α-helical molecular recognition element in the disordered N-terminus of the Sgs1 helicase is critical for chromosome stability and binding of Top3/Rmi1. <i> Kennedy JA, Daughdrill GW, Schmidt KH. </i> Nucleic Acids Res, 2013","date":"2024-05-07T15:22:24.087Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04197r001","statement":[{"text":"Using nuclear magnetic resonance spectroscopy, we show that the N-terminal 125 residues of Sgs1 are disordered and contain a transient α-helix that extends from residue 25 to 38.","type":"Abstract"},{"text":"The NHNOE values observed for Sgs11−125 are consistent with a mostly disordered protein that contains two transiently ordered regions centered on residues F30 and E92 (Figure 3a).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-21T14:37:44.155Z"}},{"start":25,"end":33,"reference_id":"24038467","reference_source":"pmid","reference_html":"A transient α-helical molecular recognition element in the disordered N-terminus of the Sgs1 helicase is critical for chromosome stability and binding of Top3/Rmi1. <i> Kennedy JA, Daughdrill GW, Schmidt KH. </i> Nucleic Acids Res, 2013","date":"2024-10-21T15:58:07.589Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051276","term_name":"chromosome organization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":1,"region_id":"DP04197r002","statement":[{"text":"To determine if the inability of Sgs1 to interact with Top3 and Rmi1 also leads to increased genome instability, we tested the ability of D25P, K26P, V29P, F30P and I33P mutants of full-length Sgs1 expressed from a CEN/ARS plasmid to suppress the elevated GCR rate of an sgs1Δ mutant. Mirroring the results of the HU hypersensitivity assay, D25P, V29P, F30P and I33P were unable to complement the defects of sgs1Δ cells, whereas cells expressing the K26P mutant accumulated GCRs at a similar rate as cells expressing wild-type Sgs1 (Table 1).","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp25Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys26Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val29Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe30Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile33Pro","start":null,"end":null,"position":null}],"ec_go":"IMP","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":null,"id":null}],"term_comment":"","term_def":"\"A process that is carried out at the cellular level that results in the assembly, arrangement of constituent parts, or disassembly of chromosomes, structures composed of a very long molecule of DNA and associated proteins that carries hereditary information. This term covers covalent modifications at the molecular level as well as spatial relationships among the major components of a chromosome.\" [GOC:ai, GOC:dph, GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":34,"end":169,"reference_id":"https://mobidb.org/P35187","reference_source":"mobidb","reference_html":"An Entry Referenced from MobiDB","date":"2024-10-21T16:13:35.622Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008033","ec_ontology":"ECO","ec_name":"intrinsic disorder prediction evidence used in manual assertion","unpublished":true,"released":"2024_12","version":1,"region_id":"DP04197r003","statement":[{"text":"MobiDB shows this region is considered as disordered, and it aligns with other predictors results regarding the flexible character of this region.","type":"Curator statement"}]},{"start":243,"end":572,"reference_id":"24038467","reference_source":"pmid","reference_html":"A transient α-helical molecular recognition element in the disordered N-terminus of the Sgs1 helicase is critical for chromosome stability and binding of Top3/Rmi1. <i> Kennedy JA, Daughdrill GW, Schmidt KH. </i> Nucleic Acids Res, 2013","date":"2024-10-21T16:14:51.688Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008033","ec_ontology":"ECO","ec_name":"intrinsic disorder prediction evidence used in manual assertion","unpublished":true,"released":"2024_12","version":1,"ec_go":"EXP","region_id":"DP04197r004","statement":[{"text":"MobiDB shows this region is considered as disordered, and it aligns with other predictors results regarding the flexible character of this region.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":27,"end":31,"reference_id":"24038467","reference_source":"pmid","reference_html":"A transient α-helical molecular recognition element in the disordered N-terminus of the Sgs1 helicase is critical for chromosome stability and binding of Top3/Rmi1. <i> Kennedy JA, Daughdrill GW, Schmidt KH. </i> Nucleic Acids Res, 2013","date":"2024-10-21T14:55:35.129Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006281","term_name":"DNA repair","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val29Pro","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"V29 and F30 in the first helical region and W92 and L93 in the second helical region were changed to proline in the context of full-length Sgs1."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe30Pro","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"V29 and F30 in the first helical region and W92 and L93 in the second helical region were changed to proline in the context of full-length Sgs1."}]}],"ec_go":"IMP","region_id":"DP04197r005","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":null,"id":null}],"statement":[{"text":"Cells expressing the mutant helicases were plated on media containing 100 mM of the DNA-damaging agent HU (Figure 4). While the sgs1-V29P and sgs1-F30P mutants were as sensitive to HU as the sgs1Δ mutant, neither the W92P nor the L93P mutation caused increased sensitivity (Figure 4a and b), indicating that the α-helical structure centered on V29 and F30 contributes to Sgs1’s role in DNA damage repair, whereas that centered on W92 and L93 does not.","type":"Results"}],"term_comment":"","term_def":"\"The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.\" [PMID:11563486]","term_is_obsolete":false,"term_not_annotate":false},{"start":9,"end":30,"reference_id":"24038467","reference_source":"pmid","reference_html":"A transient α-helical molecular recognition element in the disordered N-terminus of the Sgs1 helicase is critical for chromosome stability and binding of Top3/Rmi1. <i> Kennedy JA, Daughdrill GW, Schmidt KH. </i> Nucleic Acids Res, 2013","date":"2024-10-21T15:05:18.556Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0044547","term_name":"DNA topoisomerase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu9Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.His13Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys17Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp25Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val29Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe30Pro","start":null,"end":null,"position":null},{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Plasmid pKHS462, expressing GST-Sgs11−250, was constructed by inserting the first 750 bp of SGS1 into pGEX-6p-2 (GE Healthcare) using BamHI and XhoI sites."}]}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P13099","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04197r006","statement":[{"text":"When we introduced L9P, H13P, K17P, D25P, V29P and F30P mutations into the Sgs11−250 fragment, its ability to pull down Top3 from cell extracts was diminished, whereas the T21P and K26P mutants were still able to bind Top3 (Figure 7g). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a DNA topoisomerase.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":9,"end":30,"reference_id":"24038467","reference_source":"pmid","reference_html":"A transient α-helical molecular recognition element in the disordered N-terminus of the Sgs1 helicase is critical for chromosome stability and binding of Top3/Rmi1. <i> Kennedy JA, Daughdrill GW, Schmidt KH. </i> Nucleic Acids Res, 2013","date":"2024-10-21T15:27:44.293Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu9Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.His13Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys17Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp25Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val29Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe30Pro","start":null,"end":null,"position":null},{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Plasmid pKHS462, expressing GST-Sgs11−250, was constructed by inserting the first 750 bp of SGS1 into pGEX-6p-2 (GE Healthcare) using BamHI and XhoI sites."}]}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q02685","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04197r007","statement":[{"text":"When we introduced L9P, H13P, K17P, D25P, V29P and F30P mutations into the Sgs11−250 fragment, its ability to pull down Top3 from cell extracts was diminished, whereas the T21P and K26P mutants were still able to bind Top3 (Figure 7g). Mutations of Sgs1 that disrupted binding to Top3 also disrupted binding to Rmi1 (Figure 7h).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":9,"end":30,"reference_id":"24038467","reference_source":"pmid","reference_html":"A transient α-helical molecular recognition element in the disordered N-terminus of the Sgs1 helicase is critical for chromosome stability and binding of Top3/Rmi1. <i> Kennedy JA, Daughdrill GW, Schmidt KH. </i> Nucleic Acids Res, 2013","date":"2024-10-21T15:28:55.864Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031422","term_name":"RecQ family helicase-topoisomerase III complex","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu9Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.His13Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys17Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp25Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val29Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe30Pro","start":null,"end":null,"position":null},{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Plasmid pKHS462, expressing GST-Sgs11−250, was constructed by inserting the first 750 bp of SGS1 into pGEX-6p-2 (GE Healthcare) using BamHI and XhoI sites."}]}],"ec_go":"IMP","region_id":"DP04197r008","statement":[{"text":"When we introduced L9P, H13P, K17P, D25P, V29P and F30P mutations into the Sgs11−250 fragment, its ability to pull down Top3 from cell extracts was diminished, whereas the T21P and K26P mutants were still able to bind Top3 (Figure 7g). Mutations of Sgs1 that disrupted binding to Top3 also disrupted binding to Rmi1 (Figure 7h).","type":"Results"}],"term_comment":"","term_def":"\"A complex containing a RecQ family helicase and a topoisomerase III homologue (a member of the topoisomerase type IA subfamily); may also include one or more additional proteins; conserved from E. coli to human.\" [GOC:bhm, GOC:krc, PMID:15889139]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":8,"released":"2024_12","sequence":"MVTKPSHNLRREHKWLKETATLQEDKDFVFQAIQKHIANKRPKTNSPPTTPSKDECGPGTTNFITSIPASGPTNTATKQHEVMQTLSNDTEWLSYTATSNQYADVPMVDIPASTSVVSNPRTPNGSKTHNFNTFRPHMASSLVENDSSRNLGSRNNNKSVIDNSSIGKQLENDIKLEVIRLQGSLIMALKEQSKLLLQKCSIIESTSLSEDAKRLQLSRDIRPQLSNMSIRIDSLEKEIIKAKKDGMSKDQSKGRSQVSSQDDNIISSILPSPLEYNTSSRNSNLTSTTATTVTKALAITGAKQNITNNTGKNSNNDSNNDDLIQVLDDEDDIDCDPPVILKEGAPHSPAFPHLHMTSEEQDELTRRRNMRSREPVNYRIPDRDDPFDYVMGKSLRDDYPDVEREEDELTMEAEDDAHSSYMTTRDEEKEENELLNQSDFDFVVNDDLDPTQDTDYHDNMDVSANIQESSQEGDTRSTITLSQNKNVQVILSSPTAQSVPSNGQNQIGVEHIDLLEDDLEKDAILDDSMSFSFGRQHMPMSHSDLELIDSEKENEDFEEDNNNNGIEYLSDSDLERFDEERENRTQVADIQELDNDLKIITERKLTGDNEHPPPSWSPKIKREKSSVSQKDEEDDFDDDFSLSDIVSKSNLSSKTNGPTYPWSDEVLYRLHEVFKLPGFRPNQLEAVNATLQGKDVFVLMPTGGGKSLCYQLPAVVKSGKTHGTTIVISPLISLMQDQVEHLLNKNIKASMFSSRGTAEQRRQTFNLFINGLLDLVYISPEMISASEQCKRAISRLYADGKLARIVVDEAHCVSNWGHDFRPDYKELKFFKREYPDIPMIALTATASEQVRMDIIHNLELKEPVFLKQSFNRTNLYYEVNKKTKNTIFEICDAVKSRFKNQTGIIYCHSKKSCEQTSAQMQRNGIKCAYYHAGMEPDERLSVQKAWQADEIQVICATVAFGMGIDKPDVRFVYHFTVPRTLEGYYQETGRAGRDGNYSYCITYFSFRDIRTMQTMIQKDKNLDRENKEKHLNKLQQVMAYCDNVTDCRRKLVLSYFNEDFDSKLCHKNCDNCRNSANVINEERDVTEPAKKIVKLVESIQNERVTIIYCQDVFKGSRSSKIVQANHDTLEEHGIGKSMQKSEIERIFFHLITIRVLQEYSIMNNSGFASSYVKVGPNAKKLLTGKMEIKMQFTISAPNSRPSTSSSFQANEDNIPVIAQKSTTIGGNVAANPPRFISAKEHLRSYTYGGSTMGSSHPITLKNTSDLRSTQELNNLRMTYERLRELSLNLGNRMVPPVGNFMPDSILKKMAAILPMNDSAFATLGTVEDKYRRRFKYFKATIADLSKKRSSEDHEKYDTILNDEFVNRAAASSNGIAQSTGTKSKFFGANLNEAKENEQIINQIRQSQLPKNTTSSKSGTRSISKSSKKSANGRRGFRNYRGHYRGRK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.47062888735314445,"disorder_content":0.34485141672425706,"disprot_consensus":{"full":[{"start":1,"end":169,"type":"D"},{"start":243,"end":572,"type":"D"}],"Structural state":[{"start":1,"end":169,"type":"D"},{"start":243,"end":572,"type":"D"}],"Biological process":[{"start":25,"end":33,"type":"F"}],"Molecular function":[{"start":9,"end":30,"type":"F"}],"Cellular component":[{"start":9,"end":30,"type":"F"}]}},{"disprot_id":"DP04198","acc":"P26663","creator":"zskalman","date":"2024-05-07T17:09:05.098Z","features":{"pfam":[{"id":"PF00998","name":"Viral RNA dependent RNA polymerase","start":2422,"end":2932},{"id":"PF01001","name":"Hepatitis C virus non-structural protein NS4b","start":1728,"end":1921},{"id":"PF01006","name":"Hepatitis C virus non-structural protein NS4a","start":1658,"end":1711},{"id":"PF01506","name":"Hepatitis C virus non-structural 5a protein membrane anchor","start":1974,"end":1996},{"id":"PF01538","name":"Hepatitis C virus non-structural protein NS2","start":811,"end":1005},{"id":"PF01539","name":"Hepatitis C virus envelope glycoprotein E1","start":193,"end":382},{"id":"PF01542","name":"Hepatitis C virus core protein","start":116,"end":190},{"id":"PF01543","name":"Hepatitis C virus capsid protein","start":2,"end":115},{"id":"PF01560","name":"Hepatitis C virus non-structural protein E2/NS1","start":386,"end":729},{"id":"PF02907","name":"Hepatitis C virus NS3 protease","start":1056,"end":1203},{"id":"PF07652","name":"Flavivirus DEAD domain","start":1294,"end":1355},{"id":"PF08300","name":"Hepatitis C virus non-structural 5a zinc finger domain","start":2006,"end":2067},{"id":"PF08301","name":"Hepatitis C virus non-structural 5a domain 1b","start":2068,"end":2168},{"id":"PF12941","name":"HCV NS5a protein C-terminal region","start":2179,"end":2419},{"id":"PF22027","name":"NS3 RNA helicase, C-terminal helical domain","start":1516,"end":1656}],"gene3D":[]},"genes":[],"length":3010,"name":"Genome polyprotein","ncbi_taxon_id":11105,"organism":"Hepatitis C virus genotype 1b (isolate BK)","regions":[{"start":2950,"end":2989,"reference_id":"26784321","reference_source":"pmid","reference_html":"C-Terminal Auto-Regulatory Motif of Hepatitis C Virus NS5B Interacts with Human VAPB-MSP to Form a Dynamic Replication Complex. <i> Gupta G, Song J. </i> PLoS One, 2016","date":"2024-05-07T17:11:03.078Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04198r001","statement":[{"text":"Therefore, as judged by its CD, 1D and HSQC spectra, the isolated\nC-linker appears to be predominantly disordered in solution, lacking of any well-formed\nsecondary structures and tight tertiary packing.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-23T12:48:20.919Z"}},{"start":2950,"end":2989,"reference_id":"26784321","reference_source":"pmid","reference_html":"C-Terminal Auto-Regulatory Motif of Hepatitis C Virus NS5B Interacts with Human VAPB-MSP to Form a Dynamic Replication Complex. <i> Gupta G, Song J. </i> PLoS One, 2016","date":"2024-05-07T17:11:28.086Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04198r002","statement":[{"text":"Therefore, as judged by its CD, 1D and HSQC spectra, the isolated\nC-linker appears to be predominantly disordered in solution, lacking of any well-formed\nsecondary structures and tight tertiary packing.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-22T18:18:10.599Z"}},{"start":2950,"end":2989,"reference_id":"26784321","reference_source":"pmid","reference_html":"C-Terminal Auto-Regulatory Motif of Hepatitis C Virus NS5B Interacts with Human VAPB-MSP to Form a Dynamic Replication Complex. <i> Gupta G, Song J. </i> PLoS One, 2016","date":"2024-05-07T17:17:32.157Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"O95292","operator":null,"partner_start":7,"partner_end":124}],"region_id":"DP04198r003","statement":[{"text":"These results together decipher that the C-linker of the HCV NS5B plays a central role in binding the MSP domain of\nthe human VAPB.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O95292"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-23T12:46:59.153Z"}},{"start":2950,"end":2989,"reference_id":"26784321","reference_source":"pmid","reference_html":"C-Terminal Auto-Regulatory Motif of Hepatitis C Virus NS5B Interacts with Human VAPB-MSP to Form a Dynamic Replication Complex. <i> Gupta G, Song J. </i> PLoS One, 2016","date":"2024-10-21T16:51:34.847Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04198r004","statement":[{"text":"By contrast, as shown in Fig 2A, the C-linker peptide has a far-UV CD spectrum typical of a highly-disordered protein with the maximal negative signal at 198 nm, and lacking any positive signal at 190 nm.","type":"Results"}]},{"start":2950,"end":2989,"reference_id":"26784321","reference_source":"pmid","reference_html":"C-Terminal Auto-Regulatory Motif of Hepatitis C Virus NS5B Interacts with Human VAPB-MSP to Form a Dynamic Replication Complex. <i> Gupta G, Song J. </i> PLoS One, 2016","date":"2024-10-21T16:52:07.491Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04198r005","statement":[{"text":"By contrast, as shown in Fig 2A, the C-linker peptide has a far-UV CD spectrum typical of a highly-disordered protein with the maximal negative signal at 198 nm, and lacking any positive signal at 190 nm.","type":"Results"},{"text":"Therefore, as judged by its CD, 1D and HSQC spectra, the isolated C-linker appears to be predominantly disordered in solution, lacking of any well-formed secondary structures and tight tertiary packing.","type":"Results"}]}],"regions_counter":5,"released":"2024_12","sequence":"MSTNPKPQRKTKRNTNRRPQDVKFPGGGQIVGGVYLLPRRGPRLGVRAPRKTSERSQPRGRRQPIPKARRPEGRTWAQPGYPWPLYGNEGLGWAGWLLSPRGSRPSWGPTDPRRRSRNLGKVIDTLTCGFADLMGYIPLVGAPLGGAARALAHGVRVLEDGVNYATGNLPGCSFSIFLLALLSCLTTPASAYEVHNVSGIYHVTNDCSNASIVYEAADLIMHTPGCVPCVREGNSSRCWVALTPTLAARNVTIPTTTIRRHVDLLVGAAAFCSAMYVGDLCGSVFLVSQLFTFSPRRHVTLQDCNCSIYPGHVSGHRMAWDMMMNWSPTTALVVSQLLRIPQAVVDMVAGAHWGVLAGLAYYSMAGNWAKVLIVMLLFAGVDGDTHVTGGAQAKTTNRLVSMFASGPSQKIQLINTNGSWHINRTALNCNDSLQTGFLAALFYTHSFNSSGCPERMAQCRTIDKFDQGWGPITYAESSRSDQRPYCWHYPPPQCTIVPASEVCGPVYCFTPSPVVVGTTDRFGVPTYRWGENETDVLLLNNTRPPQGNWFGCTWMNSTGFTKTCGGPPCNIGGVGNNTLTCPTDCFRKHPEATYTKCGSGPWLTPRCMVDYPYRLWHYPCTVNFTIFKVRMYVGGVEHRLNAACNWTRGERCDLEDRDRPELSPLLLSTTEWQVLPCSFTTLPALSTGLIHLHQNIVDVQYLYGIGSAVVSFAIKWEYVLLLFLLLADARVCACLWMMLLIAQAEAALENLVVLNSASVAGAHGILSFLVFFCAAWYIKGRLVPGATYALYGVWPLLLLLLALPPRAYAMDREMAASCGGAVFVGLVLLTLSPYYKVFLARLIWWLQYFTTRAEADLHVWIPPLNARGGRDAIILLMCAVHPELIFDITKLLIAILGPLMVLQAGITRVPYFVRAQGLIHACMLVRKVAGGHYVQMAFMKLGALTGTYIYNHLTPLRDWPRAGLRDLAVAVEPVVFSDMETKIITWGADTAACGDIILGLPVSARRGKEILLGPADSLEGRGLRLLAPITAYSQQTRGLLGCIITSLTGRDKNQVEGEVQVVSTATQSFLATCVNGVCWTVYHGAGSKTLAAPKGPITQMYTNVDQDLVGWPKPPGARSLTPCTCGSSDLYLVTRHADVIPVRRRGDSRGSLLSPRPVSYLKGSSGGPLLCPFGHAVGIFRAAVCTRGVAKAVDFVPVESMETTMRSPVFTDNSSPPAVPQSFQVAHLHAPTGSGKSTKVPAAYAAQGYKVLVLNPSVAATLGFGAYMSKAHGIDPNIRTGVRTITTGAPVTYSTYGKFLADGGCSGGAYDIIICDECHSTDSTTILGIGTVLDQAETAGARLVVLATATPPGSVTVPHPNIEEVALSNTGEIPFYGKAIPIEAIRGGRHLIFCHSKKKCDELAAKLSGLGINAVAYYRGLDVSVIPTIGDVVVVATDALMTGYTGDFDSVIDCNTCVTQTVDFSLDPTFTIETTTVPQDAVSRSQRRGRTGRGRRGIYRFVTPGERPSGMFDSSVLCECYDAGCAWYELTPAETSVRLRAYLNTPGLPVCQDHLEFWESVFTGLTHIDAHFLSQTKQAGDNFPYLVAYQATVCARAQAPPPSWDQMWKCLIRLKPTLHGPTPLLYRLGAVQNEVTLTHPITKYIMACMSADLEVVTSTWVLVGGVLAALAAYCLTTGSVVIVGRIILSGRPAIVPDRELLYQEFDEMEECASHLPYIEQGMQLAEQFKQKALGLLQTATKQAEAAAPVVESKWRALETFWAKHMWNFISGIQYLAGLSTLPGNPAIASLMAFTASITSPLTTQSTLLFNILGGWVAAQLAPPSAASAFVGAGIAGAAVGSIGLGKVLVDILAGYGAGVAGALVAFKVMSGEMPSTEDLVNLLPAILSPGALVVGVVCAAILRRHVGPGEGAVQWMNRLIAFASRGNHVSPTHYVPESDAAARVTQILSSLTITQLLKRLHQWINEDCSTPCSGSWLRDVWDWICTVLTDFKTWLQSKLLPQLPGVPFFSCQRGYKGVWRGDGIMQTTCPCGAQITGHVKNGSMRIVGPKTCSNTWHGTFPINAYTTGPCTPSPAPNYSRALWRVAAEEYVEVTRVGDFHYVTGMTTDNVKCPCQVPAPEFFSEVDGVRLHRYAPACRPLLREEVTFQVGLNQYLVGSQLPCEPEPDVAVLTSMLTDPSHITAETAKRRLARGSPPSLASSSASQLSAPSLKATCTTHHVSPDADLIEANLLWRQEMGGNITRVESENKVVVLDSFDPLRAEEDEREVSVPAEILRKSKKFPAAMPIWARPDYNPPLLESWKDPDYVPPVVHGCPLPPIKAPPIPPPRRKRTVVLTESSVSSALAELATKTFGSSESSAVDSGTATALPDQASDDGDKGSDVESYSSMPPLEGEPGDPDLSDGSWSTVSEEASEDVVCCSMSYTWTGALITPCAAEESKLPINALSNSLLRHHNMVYATTSRSAGLRQKKVTFDRLQVLDDHYRDVLKEMKAKASTVKAKLLSVEEACKLTPPHSAKSKFGYGAKDVRNLSSKAVNHIHSVWKDLLEDTVTPIDTTIMAKNEVFCVQPEKGGRKPARLIVFPDLGVRVCEKMALYDVVSTLPQVVMGSSYGFQYSPGQRVEFLVNTWKSKKNPMGFSYDTRCFDSTVTENDIRVEESIYQCCDLAPEARQAIKSLTERLYIGGPLTNSKGQNCGYRRCRASGVLTTSCGNTLTCYLKASAACRAAKLQDCTMLVNGDDLVVICESAGTQEDAASLRVFTEAMTRYSAPPGDPPQPEYDLELITSCSSNVSVAHDASGKRVYYLTRDPTTPLARAAWETARHTPVNSWLGNIIMYAPTLWARMILMTHFFSILLAQEQLEKALDCQIYGACYSIEPLDLPQIIERLHGLSAFSLHSYSPGEINRVASCLRKLGVPPLRVWRHRARSVRARLLSQGGRAATCGKYLFNWAVKTKLKLTPIPAASRLDLSGWFVAGYSGGDIYHSLSRARPRWFMLCLLLLSVGVGIYLLPNR","taxonomy":["Viruses","Riboviria","Orthornavirae","Kitrinoviricota","Flasuviricetes","Amarillovirales","Flaviviridae","Hepacivirus","Hepacivirus hominis"],"dataset":["Viral proteins"],"disorder_content":0.013289036544850499,"disprot_consensus":{"full":[{"start":2950,"end":2989,"type":"D"}],"Structural state":[{"start":2950,"end":2989,"type":"D"}],"Disorder function":[{"start":2950,"end":2989,"type":"F"}],"Molecular function":[{"start":2950,"end":2989,"type":"F"}]}},{"disprot_id":"DP04199","acc":"Q9C7W1","creator":"vnugnes","date":"2024-05-07T17:26:06.679Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"PARCL","evidences":[{"code":"ECO:0000313","source":{"name":"TAIR","id":"AT1G64370","url":"https://www.arabidopsis.org/servlets/TairObject?type=locus&name=AT1G64370"}}]},"orfNames":[{"value":"F15H21.1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAG51707.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAG51707.1"}}]},{"value":"F15H21_1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AEE34233.1","url":"https://www.ebi.ac.uk/ena/browser/view/AEE34233.1"}}]}],"olnNames":[{"value":"At1g64370","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AEE34233.1","url":"https://www.ebi.ac.uk/ena/browser/view/AEE34233.1"}}]}]}],"length":178,"name":"Filaggrin-like protein","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":1,"end":178,"reference_id":"36273579","reference_source":"pmid","reference_html":"Intrinsically disordered plant protein PARCL colocalizes with RNA in phase-separated condensates whose formation can be regulated by mutating the PLD. <i> Ostendorp A, Ostendorp S, Zhou Y, Chaudron Z, Wolffram L, Rombi K, von Pein L, Falke S, Jeffries CM, Svergun DI, Betzel C, Morris RJ, Kragler F, Kehr J. </i> J Biol Chem, 2022","date":"2024-05-07T17:29:19.738Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04199r001","statement":[{"text":"Consistent with the CD spectra, the Rg/Rh ratio of 1.2 to 1.3 (compared to a compact protein ratio of 0.8) and subsequent dimensionless Kratky plot (Fig. S7A) demonstrate that PARCL is an IDP.","type":"Results"}]},{"start":1,"end":178,"reference_id":"36273579","reference_source":"pmid","reference_html":"Intrinsically disordered plant protein PARCL colocalizes with RNA in phase-separated condensates whose formation can be regulated by mutating the PLD. <i> Ostendorp A, Ostendorp S, Zhou Y, Chaudron Z, Wolffram L, Rombi K, von Pein L, Falke S, Jeffries CM, Svergun DI, Betzel C, Morris RJ, Kragler F, Kehr J. </i> J Biol Chem, 2022","date":"2024-05-07T17:29:34.155Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04199r002","statement":[{"text":"The measurements showed that both proteins are highly unstructured with no detectable β-sheets and an α-helix content below 5% (Table 1 and Fig. S9).","type":"Results"}]},{"start":1,"end":178,"reference_id":"36273579","reference_source":"pmid","reference_html":"Intrinsically disordered plant protein PARCL colocalizes with RNA in phase-separated condensates whose formation can be regulated by mutating the PLD. <i> Ostendorp A, Ostendorp S, Zhou Y, Chaudron Z, Wolffram L, Rombi K, von Pein L, Falke S, Jeffries CM, Svergun DI, Betzel C, Morris RJ, Kragler F, Kehr J. </i> J Biol Chem, 2022","date":"2024-05-07T17:35:38.558Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008270","term_name":"zinc ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006082","ec_ontology":"ECO","ec_name":"affinity chromatography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"29105","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04199r003","statement":[{"text":"Since many RBPs need divalent metal ions for their interaction with RNA (30, 60, 61), we performed metal affinity chromatography experiments indicating that PARCL binds Zn2+, Ni2+, Cu2+, and Co2+, but not Mg2+, Ca2+, Fe3+, or Cd2+ (Fig. S10).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a zinc ion (Zn).\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":178,"reference_id":"36273579","reference_source":"pmid","reference_html":"Intrinsically disordered plant protein PARCL colocalizes with RNA in phase-separated condensates whose formation can be regulated by mutating the PLD. <i> Ostendorp A, Ostendorp S, Zhou Y, Chaudron Z, Wolffram L, Rombi K, von Pein L, Falke S, Jeffries CM, Svergun DI, Betzel C, Morris RJ, Kragler F, Kehr J. </i> J Biol Chem, 2022","date":"2024-05-07T17:36:49.841Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0016151","term_name":"nickel cation binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006082","ec_ontology":"ECO","ec_name":"affinity chromatography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"49786","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04199r004","statement":[{"text":"Since many RBPs need divalent metal ions for their interaction with RNA (30, 60, 61), we performed metal affinity chromatography experiments indicating that PARCL binds Zn2+, Ni2+, Cu2+, and Co2+, but not Mg2+, Ca2+, Fe3+, or Cd2+ (Fig. S10).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a nickel (Ni) cation.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":178,"reference_id":"36273579","reference_source":"pmid","reference_html":"Intrinsically disordered plant protein PARCL colocalizes with RNA in phase-separated condensates whose formation can be regulated by mutating the PLD. <i> Ostendorp A, Ostendorp S, Zhou Y, Chaudron Z, Wolffram L, Rombi K, von Pein L, Falke S, Jeffries CM, Svergun DI, Betzel C, Morris RJ, Kragler F, Kehr J. </i> J Biol Chem, 2022","date":"2024-05-07T17:38:02.783Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1903135","term_name":"cupric ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006082","ec_ontology":"ECO","ec_name":"affinity chromatography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"29036","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04199r005","statement":[{"text":"Since many RBPs need divalent metal ions for their interaction with RNA (30, 60, 61), we performed metal affinity chromatography experiments indicating that PARCL binds Zn2+, Ni2+, Cu2+, and Co2+, but not Mg2+, Ca2+, Fe3+, or Cd2+ (Fig. S10).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a cupric ion, copper(2+).\" [GO_REF:0000067, GOC:bf, GOC:PARL, GOC:TermGenie, PMID:24567322]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":178,"reference_id":"36273579","reference_source":"pmid","reference_html":"Intrinsically disordered plant protein PARCL colocalizes with RNA in phase-separated condensates whose formation can be regulated by mutating the PLD. <i> Ostendorp A, Ostendorp S, Zhou Y, Chaudron Z, Wolffram L, Rombi K, von Pein L, Falke S, Jeffries CM, Svergun DI, Betzel C, Morris RJ, Kragler F, Kehr J. </i> J Biol Chem, 2022","date":"2024-05-07T17:38:52.525Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0050897","term_name":"cobalt ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006082","ec_ontology":"ECO","ec_name":"affinity chromatography evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"48828","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04199r006","statement":[{"text":"Since many RBPs need divalent metal ions for their interaction with RNA (30, 60, 61), we performed metal affinity chromatography experiments indicating that PARCL binds Zn2+, Ni2+, Cu2+, and Co2+, but not Mg2+, Ca2+, Fe3+, or Cd2+ (Fig. S10).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a cobalt ion (Co).\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":178,"reference_id":"36273579","reference_source":"pmid","reference_html":"Intrinsically disordered plant protein PARCL colocalizes with RNA in phase-separated condensates whose formation can be regulated by mutating the PLD. <i> Ostendorp A, Ostendorp S, Zhou Y, Chaudron Z, Wolffram L, Rombi K, von Pein L, Falke S, Jeffries CM, Svergun DI, Betzel C, Morris RJ, Kragler F, Kehr J. </i> J Biol Chem, 2022","date":"2024-05-07T17:44:02.408Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140694","term_name":"non-membrane-bounded organelle assembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007060","ec_ontology":"ECO","ec_name":"confocal laser scanning microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IDA","region_id":"DP04199r007","statement":[{"text":"To analyze the subcellular localization of PARCL and the effect of mutations in the PLD or the C-terminus, N-terminally eYFP-tagged fusion constructs of PARCL were transiently expressed in Nicotiana benthamiana, and leaves were examined by confocal microscopy. In most cells, the eYFP-wildtype PARCL fusion (PARCLWT) appeared as condensates in the cytosol, in nuclei and nucleoli (Fig. 4, A and B).","type":"Results"}],"term_comment":"","term_def":"\"The aggregation, arrangement and bonding together of a set of components to form a non-membrane-bounded organelle.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":178,"reference_id":"36273579","reference_source":"pmid","reference_html":"Intrinsically disordered plant protein PARCL colocalizes with RNA in phase-separated condensates whose formation can be regulated by mutating the PLD. <i> Ostendorp A, Ostendorp S, Zhou Y, Chaudron Z, Wolffram L, Rombi K, von Pein L, Falke S, Jeffries CM, Svergun DI, Betzel C, Morris RJ, Kragler F, Kehr J. </i> J Biol Chem, 2022","date":"2024-05-07T17:49:16.047Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007060","ec_ontology":"ECO","ec_name":"confocal laser scanning microscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IDA","region_id":"DP04199r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46793","entry_name":null}],"statement":[{"text":"To further validate the phase separation properties of PARCL, in vitro assays were performed. Here, phase separation could be induced under physiological conditions in 10% PEG 3350 and low salt regime (<150 mM NaCl) at neutral pH (Fig. 5). Condensates started to emerge at PARCL concentrations higher than 1 μM (Fig. 5A). Higher protein concentrations first increased the number of condensates and at concentrations above 6 μM, their size increased (Fig. 5A).","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":178,"reference_id":"36273579","reference_source":"pmid","reference_html":"Intrinsically disordered plant protein PARCL colocalizes with RNA in phase-separated condensates whose formation can be regulated by mutating the PLD. <i> Ostendorp A, Ostendorp S, Zhou Y, Chaudron Z, Wolffram L, Rombi K, von Pein L, Falke S, Jeffries CM, Svergun DI, Betzel C, Morris RJ, Kragler F, Kehr J. </i> J Biol Chem, 2022","date":"2024-05-07T18:13:59.919Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006303","ec_ontology":"ECO","ec_name":"microscale thermophoresis evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"RNAcentral","id":"RS000078F763_3702","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04199r009","statement":[{"text":"C, difference in RNA binding of unphosphorylated and phosphorylated AtPARCL against labeled miR164 as measured by MST. Addition of multiple negative charges within the PLD (PARCLPLD Y-E) did not affect RNA-binding affinities, whereas a C-terminal hyperphosphorylation led to an entire loss of RNA binding within the measured concentration range.","type":"Figure"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":165,"end":178,"reference_id":"36273579","reference_source":"pmid","reference_html":"Intrinsically disordered plant protein PARCL colocalizes with RNA in phase-separated condensates whose formation can be regulated by mutating the PLD. <i> Ostendorp A, Ostendorp S, Zhou Y, Chaudron Z, Wolffram L, Rombi K, von Pein L, Falke S, Jeffries CM, Svergun DI, Betzel C, Morris RJ, Kragler F, Kehr J. </i> J Biol Chem, 2022","date":"2024-05-07T18:19:22.456Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser165Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser169Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser171Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser172Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser173Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser175Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser177Ala","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"RNAcentral","id":"RS000078F763_3702","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04199r010","statement":[{"text":"However, phosphorylation of PARCL by CKII at the predicted phosphorylation site at the S-rich C terminus (Fig. 1B) that was confirmed by mutating the S-segment serine to alanine residues (PARCLC-term S-A, Fig. S5) strongly reduced RNA-binding activity (Fig. 2C). These observations suggest that the C-terminus and not the PLD domain is involved in protein:RNA interactions.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":165,"end":178,"reference_id":"36273579","reference_source":"pmid","reference_html":"Intrinsically disordered plant protein PARCL colocalizes with RNA in phase-separated condensates whose formation can be regulated by mutating the PLD. <i> Ostendorp A, Ostendorp S, Zhou Y, Chaudron Z, Wolffram L, Rombi K, von Pein L, Falke S, Jeffries CM, Svergun DI, Betzel C, Morris RJ, Kragler F, Kehr J. </i> J Biol Chem, 2022","date":"2024-05-07T18:23:43.265Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser165Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser169Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser171Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser172Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser173Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser175Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser177Ala","start":null,"end":null,"position":null}],"region_id":"DP04199r011","statement":[{"text":"The S-rich region was stepwise mutated until all possible phosphorylation sites were replaced by alanines (PARCLC-term S-A). AtPARCL could be phosphorylated in vitro by CKII whereas the alanine mutant could not, indicating the S-segment as a phosphorylation target for CKII.","type":"Supplementary material"},{"text":"According to the results the serines residues at position 165, 169, 171, 172, 173, 175 and 177 are display sites for phosphorylation.","type":"Curator statement"}]},{"start":165,"end":178,"reference_id":"36273579","reference_source":"pmid","reference_html":"Intrinsically disordered plant protein PARCL colocalizes with RNA in phase-separated condensates whose formation can be regulated by mutating the PLD. <i> Ostendorp A, Ostendorp S, Zhou Y, Chaudron Z, Wolffram L, Rombi K, von Pein L, Falke S, Jeffries CM, Svergun DI, Betzel C, Morris RJ, Kragler F, Kehr J. </i> J Biol Chem, 2022","date":"2024-05-07T18:29:14.332Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0034337","term_name":"RNA folding","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","region_id":"DP04199r012","statement":[{"text":"In contrast to RNA alone (Kann = 0.0051 s−1), PARCL increased the 21R+ and 21R- RNA annealing activity about 4-fold (Kann = 0.019 s−1), a similar activity as measured with StpA that is known to facilitate RNA strand displacement and annealing (56, 57). The annealing activity was concentration dependent and decreased with RNA protein ratios lower than 1:100. Larger ratios led to a saturating effect with a Kann up to 0.02 s−1 (Fig. 3B). ","type":"Results"},{"text":"RNA chaperone effects and solution structure of AtPARCL.","type":"Results"}],"term_comment":"","term_def":"\"The process of assisting in the covalent and noncovalent assembly of single or multimeric RNAs into the correct tertiary structure.\" [GOC:mah, PMID:10393192]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":12,"released":"2024_06","sequence":"MQYYENREKDYYEVAQGQRNGYGQSQSHNHEGYGQSQSRGGYGQIHNREGYNQNREGYSQSQSRPVYGLSPTLNHRSHGGFLDGLFKGQNGQKGQSGLGTFLGQHKSQEAKKSQGHGKLLGQHDQKKTHETNSGLNGLGMFINNGEKKHRRKSEHKKKNKDGHGSGNESGSSSGSDSD","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"alphafold_very_low_content":0.5168539325842697,"dataset":["Condensates-related proteins","RNA-binding proteins"],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":178,"type":"D"}],"Structural state":[{"start":1,"end":178,"type":"D"}],"Molecular function":[{"start":1,"end":178,"type":"F"}],"Biological process":[{"start":1,"end":178,"type":"F"}],"Disorder function":[{"start":165,"end":178,"type":"F"}]}},{"disprot_id":"DP04200","acc":"A0A078IB52","creator":"vnugnes","date":"2024-05-07T17:30:10.039Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"BnaC09g11090D","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CDY46524.1","url":"https://www.ebi.ac.uk/ena/browser/view/CDY46524.1"}}]},"orfNames":[{"value":"DARMORV10_C09P17210.1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAF1720893.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAF1720893.1"}}]},{"value":"GSBRNA2T00084185001","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CDY46524.1","url":"https://www.ebi.ac.uk/ena/browser/view/CDY46524.1"}}]}]}],"length":150,"name":"(rape) hypothetical protein","ncbi_taxon_id":3708,"organism":"Brassica napus","regions":[{"start":1,"end":150,"reference_id":"36273579","reference_source":"pmid","reference_html":"Intrinsically disordered plant protein PARCL colocalizes with RNA in phase-separated condensates whose formation can be regulated by mutating the PLD. <i> Ostendorp A, Ostendorp S, Zhou Y, Chaudron Z, Wolffram L, Rombi K, von Pein L, Falke S, Jeffries CM, Svergun DI, Betzel C, Morris RJ, Kragler F, Kehr J. </i> J Biol Chem, 2022","date":"2024-05-07T17:31:53.784Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04200r001","statement":[{"text":"The purified AtPARCL and BnPARCL proteins were further subjected to CD measurements including diverse potential ligands like divalent ions, tRNA, and detergents for an initial structural characterization. The measurements showed that both proteins are highly unstructured with no detectable β-sheets and an α-helix content below 5% (Table 1 and Fig. S9). Although approximately 19% shorter than the Arabidopsis protein, BnPARCL showed the same level of disorder. Addition of tRNA had no effect on secondary structure (Table 1).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:55:18.390Z"}},{"start":1,"end":5,"reference_id":"36273579","reference_source":"pmid","reference_html":"Intrinsically disordered plant protein PARCL colocalizes with RNA in phase-separated condensates whose formation can be regulated by mutating the PLD. <i> Ostendorp A, Ostendorp S, Zhou Y, Chaudron Z, Wolffram L, Rombi K, von Pein L, Falke S, Jeffries CM, Svergun DI, Betzel C, Morris RJ, Kragler F, Kehr J. </i> J Biol Chem, 2022","date":"2024-05-07T17:53:01.069Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000039","term_name":"acetylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04200r002","statement":[{"text":"Additionally, an N-terminal acetylation site was identified by MS (Fig. S2).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:55:21.377Z"}},{"start":1,"end":150,"reference_id":"36273579","reference_source":"pmid","reference_html":"Intrinsically disordered plant protein PARCL colocalizes with RNA in phase-separated condensates whose formation can be regulated by mutating the PLD. <i> Ostendorp A, Ostendorp S, Zhou Y, Chaudron Z, Wolffram L, Rombi K, von Pein L, Falke S, Jeffries CM, Svergun DI, Betzel C, Morris RJ, Kragler F, Kehr J. </i> J Biol Chem, 2022","date":"2024-05-07T18:07:41.250Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006303","ec_ontology":"ECO","ec_name":"microscale thermophoresis evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"ec_go":"IPI","region_id":"DP04200r003","statement":[{"text":"To verify this, different long and short RNAs and DNAs were used for in vitro Microscale thermophoresis (MST) assays: the phloem-abundant 21 nucleotide long miRNAs 398, 164, and 396 (2, 3) as RNA and complementary DNA, full-length folded transfer tRNAMet, PARCL mRNA, and a 21-nucleotide long RNA probe (21R-) that does not form any secondary structures was used to confirm RNA chaperone activity (56, 57).","type":"Results"},{"text":"While the dissociation constants (Kd) for RNAs were in the low μM range, the Kd for DNA could not be determined (>500 μM), showing that PARCL has a strong preference for RNA (Fig. S3A and Table S3). PARCL showed similar binding affinities towards phloem RNAs of different lengths (miRNAs, tRNA, mRNA), with equilibrium dissociation constants (Kd) ranging between 1.3 and 2.9 μM (Fig. 2B and Table S3).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"RNAcentral","id":"URS0000BFA223_3708","operator":"and","partner_start":null,"partner_end":null},{"db":"RNAcentral","id":"URS0000C1E5DF_3708","operator":"or","partner_start":null,"partner_end":null},{"db":"RNAcentral","id":"URS0000D77E1E_3708","operator":"or","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:55:29.168Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MQYYETREKEYYDVAQGQSRQSYGQNHQGYGQSQSRPVYGNSPTLNYRSHGGFLDGLFKGKNGQKGQNGLGSFLGQHKNQDTNQGHGHGKLLGQHQKKTHETNKGVNGLGMFINNGEKKHKKQNEHKKKKNKDGHASGNESGSSSGSDSE","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Brassiceae","Brassica"],"alphafold_very_low_content":0.42,"dataset":["RNA-binding proteins"],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":150,"type":"D"}],"Structural state":[{"start":1,"end":150,"type":"D"}],"Disorder function":[{"start":1,"end":5,"type":"F"}],"Molecular function":[{"start":1,"end":150,"type":"F"}]}},{"disprot_id":"DP04201","acc":"Q9LYG9","creator":"vnugnes","date":"2024-05-08T17:14:49.088Z","features":{"pfam":[{"id":"PF00924","name":"Mechanosensitive ion channel, beta-domain","start":559,"end":623},{"id":"PF25886","name":"Mechanosensitive ion channel protein Msy1-like, transmembrane domain","start":174,"end":312}],"gene3D":[]},"genes":[{"name":{"value":"MSL10"},"orfNames":[{"value":"F14F18.230"},{"value":"MXC9.3"}],"olnNames":[{"value":"At5g12080"}]}],"length":734,"name":"Mechanosensitive ion channel protein 10","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":1,"end":164,"reference_id":"37547488","reference_source":"pmid","reference_html":"Mechanosensitive ion channels MSL8, MSL9, and MSL10 have environmentally sensitive intrinsically disordered regions with distinct biophysical characteristics in vitro. <i> Flynn AJ, Miller K, Codjoe JM, King MR, Haswell ES. </i> Plant Direct, 2023","date":"2024-05-08T17:15:57.477Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"region_id":"DP04201r001","statement":[{"text":"We purified recombinant C-terminally His-tagged MSL10N (Figure 2a) and performed far-UV circular dichroism (CD) spectroscopy. Measured spectra at 20°C presented a minimum near 200 nm (202 nm), which is typical of disordered proteins (Na et al., 2018) (Figure 2b). The slight shoulder visible at 222 nm is indicative of residual helical structure (Greenfield, 2006).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:54:22.169Z"}},{"start":1,"end":165,"reference_id":"37805510","reference_source":"pmid","reference_html":"Open structure and gating of the Arabidopsis mechanosensitive ion channel MSL10. <i> Zhang J, Maksaev G, Yuan P. </i> Nat Commun, 2023","date":"2024-05-08T17:28:30.730Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"EMDB","id":"41164"},{"db":"PDB","id":"8TDJ"}],"region_id":"DP04201r002","statement":[{"text":"However, the N-terminal ‘death’ domain (residues 1–165), part of the cytoplasmic domain between TM4 and TM5, including residues 335–386, 397–431, and 469–480, and the C-terminal end (residues 732–734), were not resolved in the reconstruction, and thus were absent in the final refined atomic model.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:54:28.249Z"}},{"start":335,"end":386,"reference_id":"37805510","reference_source":"pmid","reference_html":"Open structure and gating of the Arabidopsis mechanosensitive ion channel MSL10. <i> Zhang J, Maksaev G, Yuan P. </i> Nat Commun, 2023","date":"2024-05-08T17:28:49.915Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"EMDB","id":"41164"},{"db":"PDB","id":"8TDJ"}],"region_id":"DP04201r003","statement":[{"text":"However, the N-terminal ‘death’ domain (residues 1–165), part of the cytoplasmic domain between TM4 and TM5, including residues 335–386, 397–431, and 469–480, and the C-terminal end (residues 732–734), were not resolved in the reconstruction, and thus were absent in the final refined atomic model.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:54:32.396Z"}},{"start":397,"end":431,"reference_id":"37805510","reference_source":"pmid","reference_html":"Open structure and gating of the Arabidopsis mechanosensitive ion channel MSL10. <i> Zhang J, Maksaev G, Yuan P. </i> Nat Commun, 2023","date":"2024-05-08T17:28:59.969Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"EMDB","id":"41164"},{"db":"PDB","id":"8TDJ"}],"region_id":"DP04201r004","statement":[{"text":"However, the N-terminal ‘death’ domain (residues 1–165), part of the cytoplasmic domain between TM4 and TM5, including residues 335–386, 397–431, and 469–480, and the C-terminal end (residues 732–734), were not resolved in the reconstruction, and thus were absent in the final refined atomic model.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:54:36.218Z"}},{"start":469,"end":480,"reference_id":"37805510","reference_source":"pmid","reference_html":"Open structure and gating of the Arabidopsis mechanosensitive ion channel MSL10. <i> Zhang J, Maksaev G, Yuan P. </i> Nat Commun, 2023","date":"2024-05-08T17:29:07.998Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"EMDB","id":"41164"},{"db":"PDB","id":"8TDJ"}],"region_id":"DP04201r005","statement":[{"text":"However, the N-terminal ‘death’ domain (residues 1–165), part of the cytoplasmic domain between TM4 and TM5, including residues 335–386, 397–431, and 469–480, and the C-terminal end (residues 732–734), were not resolved in the reconstruction, and thus were absent in the final refined atomic model.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:54:43.338Z"}},{"start":313,"end":506,"reference_id":"37805510","reference_source":"pmid","reference_html":"Open structure and gating of the Arabidopsis mechanosensitive ion channel MSL10. <i> Zhang J, Maksaev G, Yuan P. </i> Nat Commun, 2023","date":"2024-05-08T17:37:53.777Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"EMDB","id":"41166"},{"db":"PDB","id":"8TDL"}],"region_id":"DP04201r006","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:16197909"}],"statement":[{"text":"Owing to the limited dimension of lipid nanodiscs generated by membrane scaffold proteins38, we decided to reconstitute AtMSL10 in a lipid environment using saposin lipid nanoparticles39 and determined the cryo-EM structure at an overall resolution of ~3.6 Å (Fig. 3d, Supplementary Fig. 4), which is similar to the structure of AtMSL10 in detergents (root-mean-square deviation (r.m.s.d) of ~1.6 Å for all Cα atoms).","type":"Results"},{"text":"Interestingly, the CLD between TM4 and TM5 was completely disordered in the lipid environment, further indicating structural flexibility of this peripheral domain.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:54:49.599Z"}},{"start":1,"end":164,"reference_id":"32280992","reference_source":"pmid","reference_html":"Interactions between the N- and C-termini of the mechanosensitive ion channel AtMSL10 are consistent with a three-step mechanism for activation. <i> Basu D, Shoots JM, Haswell ES. </i> J Exp Bot, 2020","date":"2024-05-08T17:49:05.478Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005805","ec_ontology":"ECO","ec_name":"yeast 2-hybrid evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"unspecified"}],"region_id":"DP04201r007","statement":[{"text":"Furthermore, the soluble N-terminus (MSL101–164) and the C-terminal half of MSL10 (MSL10461–734) interacted, as did the N-terminal half of MSL10 (MSL101–460) and the soluble C-terminus (MSL10553–734). This result showed that the middle part of the protein—which contains all the TM helices—is not required for self-association.","type":"Results"},{"text":"Here we present several lines of evidence in support of a direct interaction between the soluble N-terminus and the soluble C-terminus of the plant mechanosensitive ion channel AtMSL10.","type":"Discussion"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:54:55.858Z"}}],"regions_counter":7,"released":"2024_06","sequence":"MAEQKSSNGGGGGGDVVINVPVEEASRRSKEMASPESEKGVPFSKSPSPEISKLVGSPNKPPRAPNQNNVGLTQRKSFARSVYSKPKSRFVDPSCPVDTSILEEEVREQLGAGFSFSRASPNNKSNRSVGSPAPVTPSKVVVEKDEDEEIYKKVKLNREMRSKISTLALIESAFFVVILSALVASLTINVLKHHTFWGLEVWKWCVLVMVIFSGMLVTNWFMRLIVFLIETNFLLRRKVLYFVHGLKKSVQVFIWLCLILVAWILLFNHDVKRSPAATKVLKCITRTLISILTGAFFWLVKTLLLKILAANFNVNNFFDRIQDSVFHQYVLQTLSGLPLMEEAERVGREPSTGHLSFATVVKKGTVKEKKVIDMGKVHKMKREKVSAWTMRVLMEAVRTSGLSTISDTLDETAYGEGKEQADREITSEMEALAAAYHVFRNVAQPFFNYIEEEDLLRFMIKEEVDLVFPLFDGAAETGRITRKAFTEWVVKVYTSRRALAHSLNDTKTAVKQLNKLVTAILMVVTVVIWLLLLEVATTKVLLFFSTQLVALAFIIGSTCKNLFESIVFVFVMHPYDVGDRCVVDGVAMLVEEMNLLTTVFLKLNNEKVYYPNAVLATKPISNYFRSPNMGETVEFSISFSTPVSKIAHLKERIAEYLEQNPQHWAPVHSVVVKEIENMNKLKMALYSDHTITFQENRERNLRRTELSLAIKRMLEDLHIDYTLLPQDINLTKKN","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"alphafold_very_low_content":0.23978201634877383,"disorder_content":0.4891008174386921,"disprot_consensus":{"full":[{"start":1,"end":165,"type":"D"},{"start":313,"end":506,"type":"D"}],"Structural state":[{"start":1,"end":165,"type":"D"},{"start":313,"end":506,"type":"D"}],"Disorder function":[{"start":1,"end":164,"type":"F"}]}},{"disprot_id":"DP04202","acc":"P0A567","creator":"rpancsa","date":"2024-05-09T11:43:53.747Z","features":{"pfam":[{"id":"PF06013","name":"Proteins of 100 residues with WXG","start":4,"end":88}],"gene3D":[]},"genes":[{"name":{"value":"esxB"},"synonyms":[{"value":"cfp10"},{"value":"lhp"},{"value":"mtsA10"}],"olnNames":[{"value":"BQ2027_MB3904"}]}],"length":100,"name":"ESAT-6-like protein EsxB","ncbi_taxon_id":233413,"organism":"Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)","regions":[{"start":86,"end":100,"reference_id":"15973432","reference_source":"pmid","reference_html":"Structure and function of the complex formed by the tuberculosis virulence factors CFP-10 and ESAT-6. <i> Renshaw PS, Lightbody KL, Veverka V, Muskett FW, Kelly G, Frenkiel TA, Gordon SV, Hewinson RG, Burke B, Norman J, Williamson RA, Carr MD. </i> EMBO J, 2005","date":"2024-05-09T11:50:49.121Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":35,"statements":[{"type":"Methods","text":"NMR spectra were acquired at 35°C on either an 800 MHz Varian Inova or a 600 MHz Bruker Avance spectrometer."}]}],"cross_refs":[{"db":"PDB","id":"1WA8"}],"region_id":"DP04202r001","statement":[{"text":"A striking feature of the complex is the disordered N- and particularly C-termini of both proteins (residues 2–5 and 86–100 in CFP-10 and 1–3 and 86–95 in ESAT-6), which form long flexible arms at both ends of the four-helix bundle core.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:21:02.471Z"}},{"start":86,"end":100,"reference_id":"15973432","reference_source":"pmid","reference_html":"Structure and function of the complex formed by the tuberculosis virulence factors CFP-10 and ESAT-6. <i> Renshaw PS, Lightbody KL, Veverka V, Muskett FW, Kelly G, Frenkiel TA, Gordon SV, Hewinson RG, Burke B, Norman J, Williamson RA, Carr MD. </i> EMBO J, 2005","date":"2024-05-09T11:52:08.488Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":35,"statements":[{"type":"Methods","text":"NMR spectra were acquired at 35°C on either an 800 MHz Varian Inova or a 600 MHz Bruker Avance spectrometer."}]}],"cross_refs":[{"db":"PDB","id":"1WA8"}],"region_id":"DP04202r002","statement":[{"text":"A striking feature of the complex is the disordered N- and particularly C-termini of both proteins (residues 2–5 and 86–100 in CFP-10 and 1–3 and 86–95 in ESAT-6), which form long flexible arms at both ends of the four-helix bundle core.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:21:08.250Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MAEMKTDAATLAQEAGNFERISGDLKTQIDQVESTAGSLQGQWRGAAGTAAQAAVVRFQEAANKQKQELDEISTNIRQAGVQYSRADEEQQQALSSQMGF","taxonomy":["Bacteria","Actinomycetota","Actinomycetes","Mycobacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"alphafold_very_low_content":0,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.15,"disprot_consensus":{"full":[{"start":86,"end":100,"type":"D"}],"Structural state":[{"start":86,"end":100,"type":"D"}],"Disorder function":[{"start":86,"end":100,"type":"F"}]}},{"disprot_id":"DP04203","acc":"P9WNK7","creator":"rpancsa","date":"2024-05-09T11:52:44.791Z","features":{"pfam":[{"id":"PF06013","name":"Proteins of 100 residues with WXG","start":5,"end":87}],"gene3D":[]},"genes":[{"name":{"value":"esxA","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"19876390","url":"http://www.ncbi.nlm.nih.gov/pubmed/19876390","alternativeUrl":"https://europepmc.org/abstract/MED/19876390"}}]},"synonyms":[{"value":"esaT6"}],"orfNames":[{"value":"MTV027.10"}],"olnNames":[{"value":"Rv3875"}]}],"length":95,"name":"6 kDa early secretory antigenic target","ncbi_taxon_id":83332,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","regions":[{"start":86,"end":95,"reference_id":"15973432","reference_source":"pmid","reference_html":"Structure and function of the complex formed by the tuberculosis virulence factors CFP-10 and ESAT-6. <i> Renshaw PS, Lightbody KL, Veverka V, Muskett FW, Kelly G, Frenkiel TA, Gordon SV, Hewinson RG, Burke B, Norman J, Williamson RA, Carr MD. </i> EMBO J, 2005","date":"2024-05-09T11:55:16.567Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":35,"statements":[{"type":"Methods","text":"NMR spectra were acquired at 35°C on either an 800 MHz Varian Inova or a 600 MHz Bruker Avance spectrometer."}]}],"cross_refs":[{"db":"PDB","id":"1WA8"}],"region_id":"DP04203r001","statement":[{"text":"A striking feature of the complex is the disordered N- and particularly C-termini of both proteins (residues 2–5 and 86–100 in CFP-10 and 1–3 and 86–95 in ESAT-6), which form long flexible arms at both ends of the four-helix bundle core.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:20:27.076Z"}},{"start":86,"end":95,"reference_id":"15973432","reference_source":"pmid","reference_html":"Structure and function of the complex formed by the tuberculosis virulence factors CFP-10 and ESAT-6. <i> Renshaw PS, Lightbody KL, Veverka V, Muskett FW, Kelly G, Frenkiel TA, Gordon SV, Hewinson RG, Burke B, Norman J, Williamson RA, Carr MD. </i> EMBO J, 2005","date":"2024-05-09T11:56:28.998Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":35,"statements":[{"type":"Methods","text":"NMR spectra were acquired at 35°C on either an 800 MHz Varian Inova or a 600 MHz Bruker Avance spectrometer."}]}],"cross_refs":[{"db":"PDB","id":"1WA8"}],"region_id":"DP04203r002","statement":[{"text":"A striking feature of the complex is the disordered N- and particularly C-termini of both proteins (residues 2–5 and 86–100 in CFP-10 and 1–3 and 86–95 in ESAT-6), which form long flexible arms at both ends of the four-helix bundle core.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:20:29.310Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MTEQQWNFAGIEAAASAIQGNVTSIHSLLDEGKQSLTKLAAAWGGSGSEAYQGVQQKWDATATELNNALQNLARTISEAGQAMASTEGNVTGMFA","taxonomy":["Bacteria","Actinomycetota","Actinomycetes","Mycobacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"alphafold_very_low_content":0.010526315789473684,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.10526315789473684,"disprot_consensus":{"full":[{"start":86,"end":95,"type":"D"}],"Structural state":[{"start":86,"end":95,"type":"D"}],"Disorder function":[{"start":86,"end":95,"type":"F"}]}},{"disprot_id":"DP04208","acc":"T2B9R0","creator":"eficho","date":"2024-05-10T16:17:07.937Z","features":{"pfam":[{"id":"PF00937","name":"Coronavirus nucleocapsid","start":32,"end":272}],"gene3D":[]},"genes":[],"length":274,"name":"N protein","ncbi_taxon_id":1335626,"organism":"Middle East respiratory syndrome-related coronavirus","regions":[{"start":1,"end":30,"reference_id":"26894667","reference_source":"pmid","reference_html":"Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering. <i> Papageorgiou N, Lichière J, Baklouti A, Ferron F, Sévajol M, Canard B, Coutard B. </i> Acta Crystallogr D Struct Biol, 2016","date":"2024-05-10T16:20:04.280Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"4UD1"}],"region_id":"DP04208r001","statement":[{"text":"The first 30 residues of the N-terminal region of MERS-CoV NTD+, corresponding to a disordered region, could not be resolved. This region was previously scarcely resolved in all structures obtained using X-ray diffraction techniques, while it was resolved as far as amino acid 24 in the 1ssk structure measured in solution by NMR.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-03T18:38:50.011Z"}},{"start":1,"end":30,"reference_id":"26894667","reference_source":"pmid","reference_html":"Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering. <i> Papageorgiou N, Lichière J, Baklouti A, Ferron F, Sévajol M, Canard B, Coutard B. </i> Acta Crystallogr D Struct Biol, 2016","date":"2024-05-13T21:30:22.117Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"4UD1"}],"region_id":"DP04208r004","statement":[{"text":"The first 30 residues of the N-terminal region of MERS-CoV NTD+, corresponding to a disordered region, could not be resolved. This region was previously scarcely resolved in all structures obtained using X-ray diffraction techniques, while it was resolved as far as amino acid 24 in the 1ssk structure measured in solution by NMR","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-03T18:38:49.711Z"}}],"regions_counter":5,"released":"2024_12","sequence":"MASPAAPRAVSFADNNDITNTNLSRGRGRNPKPRAAPNNTVSWYTGLTQHGKVPLTFPPGQGVPLNANSTPAQNAGYWRRQDRKINTGNGIKQLAPRWYFYYTGTGPEAALPFRAVKDGIVWVHEDGATDAPSTFGTRNPNNDSAIVTQFAPGTKLPKNFHIEGTGGNSQSSSRASSVSRNSSRSSSQGSRSGNSTRGTSPGPSGIGAVGGDLLYLDLLNRLQALESGKVKQSQPKVITKKDAAAAKNKMRHKRTSTKSFNMVQAFGLRGPGDL","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Nidovirales","Cornidovirineae","Coronaviridae","Orthocoronavirinae","Betacoronavirus","Merbecovirus"],"dataset":["Viral proteins"],"disorder_content":0.10948905109489052,"disprot_consensus":{"full":[{"start":1,"end":30,"type":"D"}],"Structural state":[{"start":1,"end":30,"type":"D"}],"Disorder function":[{"start":1,"end":30,"type":"F"}]}},{"disprot_id":"DP04210","acc":"Q9FN03","creator":"eficho","date":"2024-05-11T18:31:09.442Z","features":{"pfam":[{"id":"PF00415","name":"Regulator of chromosome condensation (RCC1) repeat","start":36,"end":81},{"id":"PF25390","name":"RCC1-like domain","start":117,"end":377}],"gene3D":[]},"genes":[{"name":{"value":"UVR8","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12226503","url":"http://www.ncbi.nlm.nih.gov/pubmed/12226503","alternativeUrl":"https://europepmc.org/abstract/MED/12226503"}}]},"orfNames":[{"value":"MGI19.7","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"BAB11034.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAB11034.1"}}]}],"olnNames":[{"value":"At5g63860","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT5G63860","url":""}}]}]}],"length":440,"name":"Ultraviolet-B receptor UVR8","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":397,"end":423,"reference_id":"30692548","reference_source":"pmid","reference_html":"Proline 411 biases the conformation of the intrinsically disordered plant UVR8 photoreceptor C27 domain altering the functional properties of the peptide. <i> Wu M, Farkas D, Eriksson LA, Strid Å. </i> Sci Rep, 2019","date":"2024-05-11T18:45:31.419Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04210r002","statement":[{"text":"Our measurements showed characteristic intrinsically disordered protein (IDP)-like features for the UVR8C27 peptide, with a strong negative peak at 198 nm and a negative shoulder around 220 nm (Fig. 1A)","type":"Results"}],"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6,"statements":[{"type":"Supplementary material","text":"All measurements were conducted with a 33 μM peptide sample in deionized water (pH 6) using a Chirascan CD spectrometer (Applied Photophysics) equipped with a Quantum Northwest Peltier unit."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-08-19T13:17:54.999Z"}},{"start":397,"end":423,"reference_id":"30692548","reference_source":"pmid","reference_html":"Proline 411 biases the conformation of the intrinsically disordered plant UVR8 photoreceptor C27 domain altering the functional properties of the peptide. <i> Wu M, Farkas D, Eriksson LA, Strid Å. </i> Sci Rep, 2019","date":"2024-08-29T08:57:23.755Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Supplementary material","text":"Natural abundant 1H-15N HSQC spectrum was recorded using a Varian INOVA 800 MHz NMR spectrometer at 25 °C for a synthetic UVR8C27 peptide encompassing amino acids GKSW VSPAE RYAVV PDETG LTDGS SKG (UVR8 aa 397–423)."}]}],"region_id":"DP04210r003","statement":[{"text":"The naturally abundant 1H-15N HSQC NMR spectrum for UVR8C27 recorded at 25  °C in 10% D2O at pH6 is shown in Fig. 1E. From this spectrum it is obvious that all 24 backbone NH-groups (not counting prolines and the N-terminal residue) can be found within the same narrow spectral window (8.6 ppm-7.7 ppm) in the 1H-dimension. The indicated spectral range is typical for intrinsically disordered proteins reflecting the dynamic nature of the peptide24,25.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:49:03.474Z"}}],"regions_counter":3,"released":"2024_12","sequence":"MAEDMAADEVTAPPRKVLIISAGASHSVALLSGDIVCSWGRGEDGQLGHGDAEDRPSPTQLSALDGHQIVSVTCGADHTVAYSQSGMEVYSWGWGDFGRLGHGNSSDLFTPLPIKALHGIRIKQIACGDSHCLAVTMEGEVQSWGRNQNGQLGLGDTEDSLVPQKIQAFEGIRIKMVAAGAEHTAAVTEDGDLYGWGWGRYGNLGLGDRTDRLVPERVTSTGGEKMSMVACGWRHTISVSYSGALYTYGWSKYGQLGHGDLEDHLIPHKLEALSNSFISQISGGWRHTMALTSDGKLYGWGWNKFGQVGVGNNLDQCSPVQVRFPDDQKVVQVSCGWRHTLAVTERNNVFAWGRGTNGQLGIGESVDRNFPKIIEALSVDGASGQHIESSNIDPSSGKSWVSPAERYAVVPDETGLTDGSSKGNGGDISVPQTDVKRVRI","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"alphafold_very_low_content":0.12272727272727273,"disorder_content":0.06136363636363636,"disprot_consensus":{"full":[{"start":397,"end":423,"type":"D"}],"Structural state":[{"start":397,"end":423,"type":"D"}]}},{"disprot_id":"DP04211","acc":"Q9BZV1","creator":"eficho","date":"2024-05-11T19:12:08.672Z","features":{"pfam":[{"id":"PF00789","name":"UBX domain","start":333,"end":407},{"id":"PF09409","name":"PUB domain","start":169,"end":254}],"gene3D":[]},"genes":[{"name":{"value":"UBXN6","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:14928","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:14928"}}]},"synonyms":[{"value":"UBXD1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11342112","url":"http://www.ncbi.nlm.nih.gov/pubmed/11342112","alternativeUrl":"https://europepmc.org/abstract/MED/11342112"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:14928","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:14928"}}]},{"value":"UBXDC2"}]}],"length":441,"name":"UBX domain-containing protein 6","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":133,"reference_id":"26475856","reference_source":"pmid","reference_html":"The N-terminal Region of the Ubiquitin Regulatory X (UBX) Domain-containing Protein 1 (UBXD1) Modulates Interdomain Communication within the Valosin-containing Protein p97. <i> Trusch F, Matena A, Vuk M, Koerver L, Knævelsrud H, Freemont PS, Meyer H, Bayer P. </i> J Biol Chem, 2015","date":"2024-10-06T09:52:01.799Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04211r001","statement":[{"text":"Although the positive values correlated with most of the defined partially transient secondary structural elements and point toward restricted backbone motility, the overall hetNOE values were below 0.5, indicating that UBXD1-N is a flexible region lacking a rigid three-dimensional folding topology.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-09T09:16:51.354Z"}},{"start":1,"end":133,"reference_id":"26475856","reference_source":"pmid","reference_html":"The N-terminal Region of the Ubiquitin Regulatory X (UBX) Domain-containing Protein 1 (UBXD1) Modulates Interdomain Communication within the Valosin-containing Protein p97. <i> Trusch F, Matena A, Vuk M, Koerver L, Knævelsrud H, Freemont PS, Meyer H, Bayer P. </i> J Biol Chem, 2015","date":"2024-05-11T19:59:37.744Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Supplementary material","text":"CD spectra were recorded with 30 scans at 25 °C subtracted by the blank (buffer without protein). "}]}],"region_id":"DP04211r002","statement":[{"text":"CD spectrum of UBXD1-N showing an unstructured protein with α-helical character. deg, degrees. C, analysis of Hα chemical shift differences with respect to random coil values (30).","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-08-19T15:15:11.202Z"}},{"start":1,"end":133,"reference_id":"26475856","reference_source":"pmid","reference_html":"The N-terminal Region of the Ubiquitin Regulatory X (UBX) Domain-containing Protein 1 (UBXD1) Modulates Interdomain Communication within the Valosin-containing Protein p97. <i> Trusch F, Matena A, Vuk M, Koerver L, Knævelsrud H, Freemont PS, Meyer H, Bayer P. </i> J Biol Chem, 2015","date":"2024-08-29T09:03:58.979Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04211r004","statement":[{"text":"The flexible N-terminal region of UBXD1 contains the well defined α-helical VIM, which is known to bind the groove between the two subdomains of p97-N (23, 32). This interaction was also confirmed by our NMR spectroscopic studies at the atomic level.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-09-17T09:53:22.596Z"}},{"start":1,"end":154,"reference_id":"26475856","reference_source":"pmid","reference_html":"The N-terminal Region of the Ubiquitin Regulatory X (UBX) Domain-containing Protein 1 (UBXD1) Modulates Interdomain Communication within the Valosin-containing Protein p97. <i> Trusch F, Matena A, Vuk M, Koerver L, Knævelsrud H, Freemont PS, Meyer H, Bayer P. </i> J Biol Chem, 2015","date":"2024-10-06T09:50:22.009Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04211r005","statement":[{"text":"The 1H-15N HSQC NMR spectrum of UBXD1-N(1–133) (Fig. 2A) showed 109 NH signals, most of which were dispersed over less than 1 ppm along the 1H dimension (∼7.8–8.6 ppm). Neither extension of the N terminus of UBXD1 to Val154 nor reduction to Arg80 had any apparent effect on signal dispersion, indicating that all three constructs share a common core structure.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-09T09:18:23.731Z"}},{"start":52,"end":63,"reference_id":"26475856","reference_source":"pmid","reference_html":"The N-terminal Region of the Ubiquitin Regulatory X (UBX) Domain-containing Protein 1 (UBXD1) Modulates Interdomain Communication within the Valosin-containing Protein p97. <i> Trusch F, Matena A, Vuk M, Koerver L, Knævelsrud H, Freemont PS, Meyer H, Bayer P. </i> J Biol Chem, 2015","date":"2024-10-09T11:49:56.917Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0051117","term_name":"ATPase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg62Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Mutation of either the PUB domain (5xPUB) or the VIM (R62A/L63A) reduced, but did not abolish, endosome targeting."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu63Ala","start":null,"end":null,"position":null}],"region_id":"DP04211r006","statement":[{"text":"The mutation (R62A/L63A) of the VIM in UBXD1-N leads to a loss of binding of UBXD1-N to p97-N throughout the VIM, whereas binding still occurs through amino acids of the N terminus of UBXD1 (Gly20, Gln21, Lys22, and Lys30).","type":"Results"}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P55072","operator":null,"partner_start":null,"partner_end":null}],"term_comment":"","term_def":"\"Binding to an ATPase, any enzyme that catalyzes the hydrolysis of ATP.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-09T11:50:16.429Z"}}],"regions_counter":6,"released":"2024_12","sequence":"MKKFFQEFKADIKFKSAGPGQKLKESVGEKAHKEKPNQPAPRPPRQGPTNEAQMAAAAALARLEQKQSRAWGPTSQDTIRNQVRKELQAEATVSGSPEAPGTNVVSEPREEGSAHLAVPGVYFTCPLTGATLRKDQRDACIKEAILLHFSTDPVAASIMKIYTFNKDQDRVKLGVDTIAKYLDNIHLHPEEEKYRKIKLQNKVFQERINCLEGTHEFFEAIGFQKVLLPAQDQEDPEEFYVLSETTLAQPQSLERHKEQLLAAEPVRAKLDRQRRVFQPSPLASQFELPGDFFNLTAEEIKREQRLRSEAVERLSVLRTKAMREKEEQRGLRKYNYTLLRVRLPDGCLLQGTFYARERLGAVYGFVREALQSDWLPFELLASGGQKLSEDENLALNECGLVPSALLTFSWDMAVLEDIKAAGAEPDSILKPELLSAIEKLL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.08843537414965986,"disorder_content":0.3492063492063492,"disprot_consensus":{"full":[{"start":1,"end":154,"type":"D"}],"Structural state":[{"start":1,"end":154,"type":"D"}],"Disorder function":[{"start":1,"end":133,"type":"F"}],"Molecular function":[{"start":52,"end":63,"type":"F"}]}},{"disprot_id":"DP04214","acc":"P40399","creator":"rpancsa","date":"2024-05-13T11:48:46.220Z","features":{"pfam":[{"id":"PF07228","name":"Stage II sporulation protein E (SpoIIE)","start":146,"end":334},{"id":"PF08673","name":"Phosphoserine phosphatase RsbU, N-terminal domain","start":9,"end":83}],"gene3D":[]},"genes":[{"name":{"value":"rsbU"},"olnNames":[{"value":"BSU04700"}]}],"length":335,"name":"Phosphoserine phosphatase RsbU","ncbi_taxon_id":224308,"organism":"Bacillus subtilis (strain 168)","regions":[{"start":85,"end":112,"reference_id":"15263010","reference_source":"pmid","reference_html":"Functional and structural characterization of RsbU, a stress signaling protein phosphatase 2C. <i> Delumeau O, Dutta S, Brigulla M, Kuhnke G, Hardwick SW, Völker U, Yudkin MD, Lewis RJ. </i> J Biol Chem, 2004","date":"2024-05-14T07:33:00.634Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"1W53"}],"region_id":"DP04214r001","statement":[{"text":"The electron density map does not reveal the conformation of residues 85–112, and these amino acids are missing from the final structure; we assume them to be disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:47:01.560Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MDFREVIEQRYHQLLSRYIAELTETSLYQAQKFSRKTIEHQIPPEEIISIHRKVLKELYPSLPEDVFHSLDFLIEVMIGYGMAYQEHQTLRGIQQEIKSEIEIAANVQQTLLGTKVPQEEALDIGAISVPAKQMSGDYYHFVKDKESINIAIADVIGKGIPAALCMSMIKYAMDSLPETGIHPSQVLKNLNRVVEQNVDASMFITMFYANYNMDKHQFTYASAGHEPGFYYSQKDNTFYDLEAKGLVLGISQDYDYKQFDQHLEKGDMIVLFSDGVTECRTENGFLERPDLQKLIEEHMCSSAQEMVKNIYDSLLKLQDFQLHDDFTLIVLRRKV","taxonomy":["Bacteria","Bacillota","Bacilli","Bacillales","Bacillaceae","Bacillus"],"alphafold_very_low_content":0,"disorder_content":0.08358208955223881,"disprot_consensus":{"full":[{"start":85,"end":112,"type":"D"}],"Structural state":[{"start":85,"end":112,"type":"D"}]}},{"disprot_id":"DP04215","acc":"Q9JK62","creator":"rpancsa","date":"2024-05-13T12:29:48.771Z","features":{"pfam":[{"id":"PF07885","name":"Ion channel","start":79,"end":137},{"id":"PF07885","name":"Ion channel","start":172,"end":244}],"gene3D":[]},"genes":[{"name":{"value":"Kcnk5","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAH34012.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAH34012.1"}},{"code":"ECO:0000313","source":{"name":"Ensembl","id":"ENSMUSP00000024011.9","url":"https://www.ensembl.org/id/ENSMUSP00000024011.9"}},{"code":"ECO:0000313","source":{"name":"MGI","id":"MGI:1336175","url":"http://www.informatics.jax.org/marker/MGI:1336175"}}]}}],"length":502,"name":"Potassium channel TASK2","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":261,"end":335,"reference_id":"32999458","reference_source":"pmid","reference_html":"Structural basis for pH gating of the two-pore domain K<sup>+</sup> channel TASK2. <i> Li B, Rietmeijer RA, Brohawn SG. </i> Nature, 2020","date":"2024-05-13T12:42:55.085Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"cross_refs":[{"db":"PDB","id":"6WM0"},{"db":"PDB","id":"6WLV"}],"region_id":"DP04215r001","statement":[{"text":"The distal intracellular C-terminal region was not resolved, suggesting it is conformationally heterogenous or unstructured as observed in previous K2P crystal structures18-21.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:16:26.457Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MVDRGPLLTSAIIFYLAIGAAIFEVLEEPHWKEAKKNYYTQKLHLLKEFPCLSQEGLDKILQVVSDAADQGVAITGNQTFNNWNWPNAMIFAATVITTIGYGNVAPKTPAGRLFCVFYGLFGVPLCLTWISALGKFFGGRAKRLGQFLTRRGVSLRKAQITCTAIFIVWGVLVHLVIPPFVFMVTEEWNYIEGLYYSFITISTIGFGDFVAGVNPSANYHALYRYFVELWIYLGLAWLSLFVNWKVSMFVEVHKAIKKRRRRRKESFESSPHSRKALQMAGSTASKDVNIFSFLSKKEETYNDLIKQIGKKAMKTSGGGERVPGPGHGLGPQGDRLPTIPASLAPLVVYSKNRVPSLEEVSQTLKNKGHVSRPLGEEAGAQAPKDSYQTSEVFINQLDRISEEGEPWEALDYHPLIFQNANITFENEETGLSDEETSKSSVEDNLTSKEQPEQGPMAEAPLSSTGEFPSSDESTFTSTESELSVPYEQLMNEYNKADNPRGT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"alphafold_very_low_content":0.33266932270916333,"disorder_content":0.14940239043824702,"disprot_consensus":{"full":[{"start":261,"end":335,"type":"D"}],"Structural state":[{"start":261,"end":335,"type":"D"}]}},{"disprot_id":"DP04216","acc":"P0CAV4","creator":"rpancsa","date":"2024-05-13T13:57:26.271Z","features":{"pfam":[{"id":"PF07739","name":"TipAS antibiotic-recognition domain","start":133,"end":251},{"id":"PF13411","name":"MerR HTH family regulatory protein","start":4,"end":72}],"gene3D":[]},"genes":[{"name":{"value":"skgA"},"olnNames":[{"value":"CC_0694"}]}],"length":255,"name":"HTH-type transcriptional regulator SkgA","ncbi_taxon_id":190650,"organism":"Caulobacter vibrioides (strain ATCC 19089 / CB15)","regions":[{"start":139,"end":255,"reference_id":"33454020","reference_source":"pmid","reference_html":"Antibiotic binding releases autoinhibition of the TipA multidrug-resistance transcriptional regulator. <i> Jiang X, Zhang L, Teng M, Li X. </i> J Biol Chem, 2020","date":"2024-05-13T13:59:36.250Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04216r001","statement":[{"text":"Although full-length SkgA (residues 1–255) protein was used for crystallization, only residues 1–138 were observed in the final structure. The established structure consists of the N-terminal MerR-type HTH motif, coiled-coil region, and the initial two α-helices of the C-terminal TipAS domain (Fig. 1B and Fig. S1B), whereas the rest of the TipAS domain was still invisible in the current model, probably because of structural flexibility or diffraction damage.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"7CLA"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-05-14T07:15:44.571Z"}}],"regions_counter":1,"released":"2024_06","sequence":"MSVYTVKQMARLSGVSVRALHHYDAIGLLKPRAVGANGYRYYDRQDLLRLQQILFHRALETPLKDIQAALDQPGFDLAAALRAQRERLAAQAERYARLVDVVDRTLADLEGDETMDDKHLFEGFDPEKQARHEAWLVEHYGDEATRRIADAKAGMKSWGKKDWSQFQEEAKAIEHDLAKALTQGLPVDSAPVTAIMRRHWAWVGRSWNREPTPDAFAGLGHLYQANPEFTARYEAIAPGLTEYFSEAMRAFARGR","taxonomy":["Bacteria","Pseudomonadota","Alphaproteobacteria","Caulobacterales","Caulobacteraceae","Caulobacter"],"alphafold_very_low_content":0,"dataset":[],"disorder_content":0.4588235294117647,"disprot_consensus":{"full":[{"start":139,"end":255,"type":"D"}],"Structural state":[{"start":139,"end":255,"type":"D"}]}},{"disprot_id":"DP04217","acc":"Q2KHT3","creator":"ireményi","date":"2024-05-13T20:11:48.827Z","features":{"pfam":[{"id":"PF09758","name":"Uncharacterised conserved protein","start":51,"end":198},{"id":"PF19439","name":"CLEC16A C-terminal PH-like domain","start":696,"end":828},{"id":"PF29709","name":"CLEC16A helical domain","start":245,"end":692}],"gene3D":[]},"genes":[{"name":{"value":"CLEC16A","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:29013","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:29013"}}]},"synonyms":[{"value":"KIAA0350"}]}],"length":1053,"name":"Protein CLEC16A","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":892,"end":1050,"reference_id":"35604110","reference_source":"pmid","reference_html":"An intrinsically disordered protein region encoded by the human disease gene <i>CLEC16A</i> regulates mitophagy. <i> Gingerich MA, Liu X, Chai B, Pearson GL, Vincent MP, Stromer T, Zhu J, Sidarala V, Renberg A, Sahu D, Klionsky DJ, Schnell S, Soleimanpour SA. </i> Autophagy, 2023","date":"2024-05-13T20:26:38.679Z","curator_id":"ireményi","curator_name":"István Reményi ","curator_orcid":"0000-0003-4670-2406","term_id":"GO:0000423","term_name":"mitophagy","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005580","ec_ontology":"ECO","ec_name":"flow cytometry evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04217r001","statement":[{"text":"To determine whether loss of the CLEC16A C-terminal IDPR impairs mitophagy, we used several complementary approaches in primary islets and in MEFs. We examined key steps of mitophagy following mitochondrial damage, including turnover of outer mitochondrial membrane proteins, such as MFN2 (mitofusin 2), and clearance of damaged mitochondria by targeting to the lysosome [43]. We observed impaired MFN2 turnover in isolated Clec16acurt/curt islets following exposure to the mitochondrial ionophore valinomycin, which is suggestive of impaired mitophagy flux (Figure 3D and S4E). Next, we intercrossed the mt-Keima mitophagy reporter model with Clec16acurt/curt mice. Mt-Keima mice express a fluorescently labeled pH-sensitive mitochondrial biosensor that shifts excitation spectra based on pH [44]. Mt-Keima allows for detection of mitophagy as mitochondria are targeted to acidic autophagosomes/lysosomes for degradation. Flow cytometry of dissociated islets revealed that mt-Keima;Clec16acurt/curt β-cells had an increase in cells with mitochondria in acidic compartments (Figure 3E). This suggests that Clec16acurt/curt β-cells accumulate mitochondria in acidic autophagosomes or lysosomes that may be incompletely cleared, consistent with previous observations following CLEC16A deficiency in β-cells [6]. ","type":"Results"}],"ec_go":"IDA","term_comment":"Note that this terms refers to the macroautophagy process and is named by common usage. Be aware that there are a separate micromitophagy and mitophagy by induced vacuole formation processes.","term_def":"\"The selective autophagy process in which a mitochondrion is degraded by macroautophagy.\" [PMID:15798367]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:54:46.580Z"}},{"start":892,"end":1052,"reference_id":"35604110","reference_source":"pmid","reference_html":"An intrinsically disordered protein region encoded by the human disease gene <i>CLEC16A</i> regulates mitophagy. <i> Gingerich MA, Liu X, Chai B, Pearson GL, Vincent MP, Stromer T, Zhu J, Sidarala V, Renberg A, Sahu D, Klionsky DJ, Schnell S, Soleimanpour SA. </i> Autophagy, 2023","date":"2024-05-13T20:28:13.547Z","curator_id":"ireményi","curator_name":"István Reményi ","curator_orcid":"0000-0003-4670-2406","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04217r002","statement":[{"text":"We next investigated CLEC16A C-terminal structure using nuclear magnetic resonance (NMR). In an IDPR, backbone hydrogen atoms do not participate in hydrogen bonds that generate secondary structure, and instead are found in a flexible extended conformation. Thus, all backbone hydrogen atoms in an IDPR are in a similar chemical environment and are tightly clustered in the hydrogen dimension of an 1H-15N heteronuclear single quantum coherence/HSQC-NMR spectrum [35]. The heteronuclear single quantum coherence-NMR spectrum of the CLEC16A C terminus was tightly clustered in the hydrogen dimension between 8–8.5 ppm, which strongly suggests that the CLEC16A C terminus is an IDPR (Figure 1F).","type":"Results"},{"text":"1H-15N HSQC spectra of recombinant CLEC16A C terminus (AA 892–1050). Spectra clusters near 1H 8ppm, consistent with being an IDPR.","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:54:38.906Z"}},{"start":892,"end":1052,"reference_id":"35604110","reference_source":"pmid","reference_html":"An intrinsically disordered protein region encoded by the human disease gene <i>CLEC16A</i> regulates mitophagy. <i> Gingerich MA, Liu X, Chai B, Pearson GL, Vincent MP, Stromer T, Zhu J, Sidarala V, Renberg A, Sahu D, Klionsky DJ, Schnell S, Soleimanpour SA. </i> Autophagy, 2023","date":"2024-05-13T20:28:44.646Z","curator_id":"ireményi","curator_name":"István Reményi ","curator_orcid":"0000-0003-4670-2406","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04217r003","statement":[{"text":"While Flag epitope-tagged full-length CLEC16A and a C-terminal deficient CLEC16A mutant (CLEC16A ∆C) migrated at their expected molecular mass, a CLEC16A construct encoding only the C terminus migrated more slowly, at nearly double its expected molecular mass (Figure 1E). ","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-06-14T07:54:36.349Z"}}],"regions_counter":3,"released":"2024_06","sequence":"MFGRSRSWVGGGHGKTSRNIHSLDHLKYLYHVLTKNTTVTEQNRNLLVETIRSITEILIWGDQNDSSVFDFFLEKNMFVFFLNILRQKSGRYVCVQLLQTLNILFENISHETSLYYLLSNNYVNSIIVHKFDFSDEEIMAYYISFLKTLSLKLNNHTVHFFYNEHTNDFALYTEAIKFFNHPESMVRIAVRTITLNVYKVSLDNQAMLHYIRDKTAVPYFSNLVWFIGSHVIELDDCVQTDEEHRNRGKLSDLVAEHLDHLHYLNDILIINCEFLNDVLTDHLLNRLFLPLYVYSLENQDKGGERPKISLPVSLYLLSQVFLIIHHAPLVNSLAEVILNGDLSEMYAKTEQDIQRSSAKPSIRCFIKPTETLERSLEMNKHKGKRRVQKRPNYKNVGEEEDEEKGPTEDAQEDAEKAKGTEGGSKGIKTSGESEEIEMVIMERSKLSELAASTSVQEQNTTDEEKSAAATCSESTQWSRPFLDMVYHALDSPDDDYHALFVLCLLYAMSHNKGMDPEKLERIQLPVPNAAEKTTYNHPLAERLIRIMNNAAQPDGKIRLATLELSCLLLKQQVLMSAGCIMKDVHLACLEGAREESVHLVRHFYKGEDIFLDMFEDEYRSMTMKPMNVEYLMMDASILLPPTGTPLTGIDFVKRLPCGDVEKTRRAIRVFFMLRSLSLQLRGEPETQLPLTREEDLIKTDDVLDLNNSDLIACTVITKDGGMVQRFLAVDIYQMSLVEPDVSRLGWGVVKFAGLLQDMQVTGVEDDSRALNITIHKPASSPHSKPFPILQATFIFSDHIRCIIAKQRLAKGRIQARRMKMQRIAALLDLPIQPTTEVLGFGLGSSTSTQHLPFRFYDQGRRGSSDPTVQRSVFASVDKVPGFAVAQCINQHSSPSLSSQSPPSASGSPSGSGSTSHCDSGGTSSSSTPSTAQSPADAPMSPELPKPHLPDQLVIVNETEADSKPSKNVARSAAVETASLSPSLVPARQPTISLLCEDTADTLSVESLTLVPPVDPHSLRSLTGMPPLSTPAAACTEPVGEEAACAEPVGTAED","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.32193732193732194,"dataset":["Autophagy-related proteins"],"disorder_content":0.15289648622981955,"disprot_consensus":{"full":[{"start":892,"end":1052,"type":"D"}],"Structural state":[{"start":892,"end":1052,"type":"D"}],"Biological process":[{"start":892,"end":1050,"type":"F"}]}},{"acc":"Q9V9N4","sequence":"MEDLTKNIIFTNAINGQPATIQYQTADGTILKQPKIEGQKTEQQPTFYYTTNGNGGTVNLAQLATTDDNKTCYIAQPVGGYNYALVNGMPLNQGAALGIATVDAQGRIQIVNQNKPIAANTISNISFKCDVCSDMFPHLALLNAHKRMHTDGEQQQQQQHNAQAGGDSIAVVSAQGLVQAQNIIGNGQMGQIQIVSSDTLEPVQQSVMQQQQHESKASKCINCGSSMLQQSKRKGPKQVRCESCMQAEQTAQQQQQLFVAQDGQMAHPVQIISTTPQAQAQLQQIVAAQTGGTTPKREASSGSGHHPVKKRNSQQMTKCQKCNGSGVVLVGQHSHASHSGVGGSVKQSVTVKTENPSKPFSCNICGGLFSRYSSLWSHKKLHSGEKNYKCSICGLAFAKAVYLKNHARIHTGEKPYKCQTCGMQFSQSPHLKNHERTHSGERPYVCGVCDKGFARHATLWNHRRIHTGEKPYKCEICGSAFSQAAHLKNHAKVHSGEKPYKCEICSAAFADRFALKRHRGIHQKYGQTAPRQTSSDGMIVHKQEIPDMEDEAQQEVIIGGL","alphafold_very_low_content":"0.6488413547237076","creator":"ireményi","dataset":[],"date":"2024-05-13T20:48:42.042Z","disprot_id":"DP04218","features":{"pfam":[{"id":"PF00096","name":"Zinc finger, C2H2 type","start":360,"end":382},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":388,"end":410},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":416,"end":438},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":444,"end":466},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":472,"end":494},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":500,"end":522}],"gene3D":[]},"genes":[{"name":{"value":"Clamp","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/23873939","id":"23873939","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/23873939","_id":"6856ac1d7cd61eccdacd5c4a"},"code":"ECO:0000303","_id":"6856ac1d7cd61eccdacd5c49"},{"source":{"id":"FBgn0032979","name":"FlyBase","url":"http://flybase.org/reports/FBgn0032979.html","_id":"6856ac1d7cd61eccdacd5c4c"},"code":"ECO:0000312","_id":"6856ac1d7cd61eccdacd5c4b"}],"_id":"6856ac1d7cd61eccdacd5c4d"},"synonyms":[],"olnNames":[],"orfNames":[{"value":"CG1832","evidences":[{"source":{"id":"FBgn0032979","name":"FlyBase","url":"http://flybase.org/reports/FBgn0032979.html","_id":"6856ac1d7cd61eccdacd5c50"},"code":"ECO:0000312","_id":"6856ac1d7cd61eccdacd5c4f"}],"_id":"6856ac1d7cd61eccdacd5c4e"}],"_id":"6856ac1d7cd61eccdacd5c48"}],"length":561,"name":"Transcription factor Clamp","ncbi_taxon_id":7227,"organism":"Drosophila melanogaster","regions_counter":9,"released":"2024_12","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"regions":[{"annotation_extensions":[],"conditions":[{"deviation":"within normal range","statements":[{"type":"Methods","text":"The NMR samples contained 0.2 mM 15N-CLAMP1–113, 20 mM sodium phosphate at pH 7, and 5% (v/v) D2O for frequency lock. ","_id":"6856ac1d7cd61eccdacd5c56"}],"term_id":"NCIT:C45997","unit_id":"UO:0000196","unit_name":"pH","value":7,"_id":"6856ac1d7cd61eccdacd5c55"}],"construct_alterations":[],"cross_refs":[],"curator_id":"ireményi","curator_name":"István Reményi ","curator_orcid":"0000-0003-4670-2406","date":"2024-05-13T20:57:57.815Z","disprot_namespace":"Structural state","ec_id":"ECO:0006196","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","ec_ontology":"ECO","start":41,"end":86,"interaction_partner":[],"reference_html":"Dimerization Activity of a Disordered N-Terminal Domain from <i>Drosophila</i> CLAMP Protein. <i> Tikhonova E, Mariasina S, Arkova O, Maksimenko O, Georgiev P, Bonchuk A. </i> Int J Mol Sci, 2022","reference_id":"35409222","region_id":"DP04218r001","released":"2025_06","sample":[],"statement":[{"type":"Results","text":"All HN chemical shifts of the 1–86 region are plotted into the interval from 7.6 to 8.6 ppm. These chemical shift values correspond to the unstructured protein chain [49] (Figure 3a).","_id":"6856ac1d7cd61eccdacd5c52"},{"type":"Results","text":"To ensure that CLAMP41−86 is unstructured, we obtained 15N-labeled CLAMP41−153 and compared its HSQC spectrum with CLAMP87−153. As most signals in 87–153 are still present at their places in the spectrum of CLAMP40−153, we can assign the rest of the signals to the 41–86 region (Figure S5). In total, 38 peaks were found corresponding to that region (most probably several of them represent more than one signal because of peak overlapping). All HN chemical shifts of the 41–86 region also fall into the interval from 7.6 to 8.6 ppm, suggesting a lack of the secondary structure [49]. Additionally, we measured transverse relaxation rates (R2) to assess the protein chain mobility in different regions. R2 reflects protein chain mobility and can be used to measure disordered state of the protein [50]","_id":"6856ac1d7cd61eccdacd5c53"},{"type":"Results","text":"he averaged R2 value for 41–86 is 2.2 ± 1.3 s, whereas for 89–119 (unfolded region preceding the zinc-finger) it is 2.9 ± 0.8 s, and 4.6 ± 0.8 s for 122–151 (zinc-finger domain). Thus, we conclude that according to NMR data the CLAMP41−86 region is unstructured.","_id":"6856ac1d7cd61eccdacd5c54"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2025-06-23T14:34:47.206Z","_id":"685af15309b428148507156e"},"version":0,"_id":"6856ac1d7cd61eccdacd5c51","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[{"deviation":"increased","statements":[{"type":"Methods","text":"Briefly, for growth assays, plasmids were transformed into the yeast strain pJ69-4A by the lithium acetate method following the standard Clontech protocol and plated on media without tryptophan and leucine. After two days of growth at 30 °C, the cells were plated on selective media without tryptophan, leucine, histidine, or adenine, and their growth was compared after 2–3 days. Each assay was repeated three times.","_id":"6856ac1d7cd61eccdacd5c5c"}],"term_id":"NCIT:C25206","unit_id":"UO:0000027","unit_name":"°C","value":30,"_id":"6856ac1d7cd61eccdacd5c5b"}],"construct_alterations":[],"cross_refs":[],"curator_id":"ireményi","curator_name":"István Reményi ","curator_orcid":"0000-0003-4670-2406","date":"2024-05-13T20:57:14.674Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005805","ec_name":"yeast 2-hybrid evidence used in manual assertion","ec_ontology":"ECO","start":41,"end":86,"interaction_partner":[{"db":"UniProt","id":"Q9V9N4","operator":null,"partner_start":41,"partner_end":86,"_id":"6856ac1d7cd61eccdacd5c5d"}],"reference_html":"Dimerization Activity of a Disordered N-Terminal Domain from <i>Drosophila</i> CLAMP Protein. <i> Tikhonova E, Mariasina S, Arkova O, Maksimenko O, Georgiev P, Bonchuk A. </i> Int J Mol Sci, 2022","reference_id":"35409222","region_id":"DP04218r003","released":"2025_06","sample":[],"statement":[{"type":"Figure","text":"Results of the Y2H assay of dimerization activity of the CLAMP N-terminal region shown for the domain structure of the CLAMP protein. AD stands for GAL4 activation domain and BD stands for GAL4 DNA-binding domain. Positive interaction indicates the ability of yeast to grow on assay plates without histidine","_id":"6856ac1d7cd61eccdacd5c5e"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_id":"GO:0042803","term_is_obsolete":false,"term_name":"protein homodimerization activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2025-06-23T14:27:58.859Z","_id":"685af15309b4281485071577"},"version":0,"_id":"6856ac1d7cd61eccdacd5c5a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-10-22T13:41:37.151Z","disprot_namespace":"Structural state","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":86,"interaction_partner":[],"reference_html":"Dimerization Activity of a Disordered N-Terminal Domain from <i>Drosophila</i> CLAMP Protein. <i> Tikhonova E, Mariasina S, Arkova O, Maksimenko O, Georgiev P, Bonchuk A. </i> Int J Mol Sci, 2022","reference_id":"35409222","region_id":"DP04218r004","released":"2024_12","sample":[],"statement":[{"type":"Results","text":"All HN chemical shifts of the 1–86 region are plotted into the interval from 7.6 to 8.6 ppm. These chemical shift values correspond to the unstructured protein chain [49] (Figure 3a).","_id":"6856ac1d7cd61eccdacd5c60"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"version":0,"_id":"6856ac1d7cd61eccdacd5c5f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-10-22T13:42:07.727Z","disprot_namespace":"Structural state","ec_id":"ECO:0006198","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":89,"end":119,"interaction_partner":[],"reference_html":"Dimerization Activity of a Disordered N-Terminal Domain from <i>Drosophila</i> CLAMP Protein. <i> Tikhonova E, Mariasina S, Arkova O, Maksimenko O, Georgiev P, Bonchuk A. </i> Int J Mol Sci, 2022","reference_id":"35409222","region_id":"DP04218r005","released":"2024_12","sample":[],"statement":[{"type":"Results","text":"The averaged R2 value for 41–86 is 2.2 ± 1.3 s, whereas for 89–119 (unfolded region preceding the zinc-finger) it is 2.9 ± 0.8 s, and 4.6 ± 0.8 s for 122–151 (zinc-finger domain).","_id":"6856ac1d7cd61eccdacd5c62"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"version":0,"_id":"6856ac1d7cd61eccdacd5c61","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2024-10-22T14:02:59.455Z","disprot_namespace":"Structural state","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":113,"interaction_partner":[],"reference_html":"Dimerization Activity of a Disordered N-Terminal Domain from <i>Drosophila</i> CLAMP Protein. <i> Tikhonova E, Mariasina S, Arkova O, Maksimenko O, Georgiev P, Bonchuk A. </i> Int J Mol Sci, 2022","reference_id":"35409222","region_id":"DP04218r006","released":"2024_12","sample":[],"statement":[{"type":"Results","text":"The same plot of CLAMP1–113 only revealed the presence of a small bell-shaped area, suggesting that it does not represent a completely unfolded polypeptide chain but rather lacks a stable spatial structure (Figure 3c).","_id":"6856ac1d7cd61eccdacd5c64"},{"type":"Results","text":"Thus, the NMR and SAXS data suggest that the N-terminal domain of CLAMP preceding the zinc-finger has the features of an IDR.","_id":"6856ac1d7cd61eccdacd5c65"},{"type":"Curator statement","text":"This experiment shows this region lacks a fixed 3D structure.","_id":"6856ac1d7cd61eccdacd5c66"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"version":0,"_id":"6856ac1d7cd61eccdacd5c63","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","date":"2022-06-02T08:45:05.495Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001170","ec_name":"cross-linking evidence used in manual assertion","ec_ontology":"ECO","start":41,"end":86,"interaction_partner":[{"db":"UniProt","id":"Q8IGP5","operator":null,"partner_start":46,"partner_end":86,"_id":"6856af0a7cd61eccdacd5e9d"}],"reference_html":"Dimerization Activity of a Disordered N-Terminal Domain from <i>Drosophila</i> CLAMP Protein. <i> Tikhonova E, Mariasina S, Arkova O, Maksimenko O, Georgiev P, Bonchuk A. </i> Int J Mol Sci, 2022","reference_id":"35409222","region_id":"DP04218r007","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"Using chemical cross-linking (Figure 2a,c) and size-exclusion chromatography (Figure 2b) experiments, we demonstrated that the CLAMP1–127 can form multimers (presumably dimers) similar to CLAMP1–153. Shortening of the region to 1–113 amino acids and deleting the first 40 residues only weakly reduced the efficiency of cross-linking, supporting the data of Y2H (Figure 2a). Further shortening of the region decreased the cross-linking efficiency (Figure 2a and Figure S3), likely because cross-linking is dependent on the presence of neighbor lysines; thus, it is not suitable for the precise mapping of the dimerization motif and was not used on smaller fragments.","_id":"6856af0a7cd61eccdacd5e9e"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_id":"GO:0042803","term_is_obsolete":false,"term_name":"protein homodimerization activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-07T08:22:03.154Z","_id":"6856af0a7cd61eccdacd5e9f"},"version":0,"_id":"6856af0a7cd61eccdacd5e9c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","date":"2022-06-02T08:45:29.562Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0005640","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","ec_ontology":"ECO","start":41,"end":86,"interaction_partner":[{"db":"UniProt","id":"Q8IGP5","operator":null,"partner_start":1,"partner_end":113,"_id":"6856af0a7cd61eccdacd5ea1"}],"reference_html":"Dimerization Activity of a Disordered N-Terminal Domain from <i>Drosophila</i> CLAMP Protein. <i> Tikhonova E, Mariasina S, Arkova O, Maksimenko O, Georgiev P, Bonchuk A. </i> Int J Mol Sci, 2022","reference_id":"35409222","region_id":"DP04218r008","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"Interactions between 6xHis thioredoxin- or glutathione S-transferase (GST)-tagged CLAMP deletion derivatives were further studied with a pull-down assay after co-expression in bacteria cells (Figure 2c and Figure S4). Because CLAMP1–113 binds non-specifically to Ni-NTA resin, 6xHis pull-down was used only as protein expression control. CLAMP41–113 interacts efficiently with the larger GST-tagged CLAMP1–113 polypeptide; however, the interaction between CLAMP1–91 and CLAMP1–113 polypeptides was slightly impaired. The 87–153 fragment lacking most of the dimerization sequences did not interact with CLAMP1–113. Taken together, these results suggest that the 46–86 amino acids are sufficient for dimerization and include two modules that can both form dimers.","_id":"6856af0a7cd61eccdacd5ea2"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_id":"GO:0042803","term_is_obsolete":false,"term_name":"protein homodimerization activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-07T08:22:05.283Z","_id":"6856af0a7cd61eccdacd5ea3"},"version":0,"_id":"6856af0a7cd61eccdacd5ea0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","date":"2022-06-02T08:42:01.702Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":86,"interaction_partner":[{"db":"UniProt","id":"Q8IGP5","operator":null,"partner_start":1,"partner_end":113,"_id":"6856af0a7cd61eccdacd5ea5"}],"reference_html":"Dimerization Activity of a Disordered N-Terminal Domain from <i>Drosophila</i> CLAMP Protein. <i> Tikhonova E, Mariasina S, Arkova O, Maksimenko O, Georgiev P, Bonchuk A. </i> Int J Mol Sci, 2022","reference_id":"35409222","region_id":"DP04218r009","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"SAXS provides precise information about the size of macromolecules in solution that is almost independent of their shape [48].","_id":"6856af0a7cd61eccdacd5ea6"},{"type":"Results","text":"By contrast, the molecular weight estimation for CLAMP87–153 resulted in values in the range 5.1–6.8 kDa, which corresponds to the monomer. The estimated molecular weight CLAMP1–113 falls into the range of 20–24 kDa, which confirms that it exists as a dimer in solution.","_id":"6856af0a7cd61eccdacd5ea7"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_id":"GO:0042803","term_is_obsolete":false,"term_name":"protein homodimerization activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-07T08:22:08.921Z","_id":"6856af0a7cd61eccdacd5ea8"},"version":0,"_id":"6856af0a7cd61eccdacd5ea4","reference_source":"pmid"}],"__v":0,"disorder_content":0.21212121212121213,"disprot_consensus":{"full":[{"start":1,"end":119,"type":"D"}],"Structural state":[{"start":1,"end":119,"type":"D"}],"Molecular function":[{"start":1,"end":86,"type":"F"}]}},{"disprot_id":"DP04219","acc":"O95433","creator":"ireményi","date":"2024-05-13T21:15:42.872Z","features":{"pfam":[{"id":"PF08327","name":"Activator of Hsp90 ATPase homolog 1-like protein","start":217,"end":331},{"id":"PF09229","name":"Activator of Hsp90 ATPase, N-terminal","start":29,"end":158}],"gene3D":[]},"genes":[{"name":{"value":"AHSA1"},"synonyms":[{"value":"C14orf3"}],"orfNames":[{"value":"HSPC322"}]}],"length":338,"name":"Activator of 90 kDa heat shock protein ATPase homolog 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":162,"end":204,"reference_id":"33808352","reference_source":"pmid","reference_html":"Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity. <i> Hu H, Wang Q, Du J, Liu Z, Ding Y, Xue H, Zhou C, Feng L, Zhang N. </i> Molecules, 2021","date":"2024-10-24T13:17:01.570Z","curator_id":"ireményi","curator_name":"István Reményi ","curator_orcid":"0000-0003-4670-2406","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006196","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"7DMD"}],"region_id":"DP04219r002","statement":[{"text":"The solved solution structure ensemble of Aha128−335 indicates that human Aha1’s N-terminal domain and C-terminal domain are linked through a long unstructured loop (Figure 4a, Supplemental Figure S4), and there are no tight contacts between the two domains.","type":"Results"},{"text":"Figure 4 specifies the boundaries for the C-terminal and the N-terminal region.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-24T13:46:21.480Z"}},{"start":162,"end":204,"reference_id":"33808352","reference_source":"pmid","reference_html":"Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity. <i> Hu H, Wang Q, Du J, Liu Z, Ding Y, Xue H, Zhou C, Feng L, Zhang N. </i> Molecules, 2021","date":"2024-10-24T13:17:13.025Z","curator_id":"ireményi","curator_name":"István Reményi ","curator_orcid":"0000-0003-4670-2406","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006196","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"7DMD"}],"region_id":"DP04219r003","statement":[{"text":"The solved solution structure ensemble of Aha128−335 indicates that human Aha1’s N-terminal domain and C-terminal domain are linked through a long unstructured loop (Figure 4a, Supplemental Figure S4), and there are no tight contacts between the two domains.","type":"Results"},{"text":"Figure 4 specifies the boundaries for the C-terminal and the N-terminal region.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-24T13:46:24.662Z"}},{"start":1,"end":27,"reference_id":"37486705","reference_source":"pmid","reference_html":"Human Aha1's N-terminal extension confers it holdase activity in vitro. <i> Tang J, Hu H, Zhou C, Zhang N. </i> Protein Sci, 2023","date":"2024-10-23T13:18:38.170Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006196","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","unpublished":true,"released":"2024_12","version":1,"region_id":"DP04219r004","statement":[{"text":"This analysis revealed that the presence of N-terminal sequence motif spanning M1 to W27 does not modify the global fold of Aha1's N-terminal domain spanning T28 to G162 (Figure 3a). Moreover, The CSI data demonstrated that the N-terminal sequence motif of Aha1 spanning M1 to W27 mainly adopts a random coil conformation (Figure 3a). In support of this finding, compared with the dynamics behavior of the core region, extremely high flexibility was observed for the N-terminal sequence motif of Aha1 spanning M1 to W27 (Figure 3b,c).","type":"Results"}]},{"start":1,"end":27,"reference_id":"33808352","reference_source":"pmid","reference_html":"Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity. <i> Hu H, Wang Q, Du J, Liu Z, Ding Y, Xue H, Zhou C, Feng L, Zhang N. </i> Molecules, 2021","date":"2024-10-24T13:21:06.340Z","curator_id":"ireményi","curator_name":"István Reményi ","curator_orcid":"0000-0003-4670-2406","term_id":"GO:0044183","term_name":"protein folding chaperone","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006333","ec_ontology":"ECO","ec_name":"thioflavin T based fluorescence spectroscopy evidence","unpublished":true,"released":"2024_12","version":0,"ec_go":"EXP","region_id":"DP04219r005","statement":[{"text":"After the confirmation of the interaction between human Aha1 and α-synuclein, ThT assay and transmission electron microscopy (TEM) were applied to test the impact of Aha1 on the aggregation process of α-synuclein. Both the ThT data and the TEM results demonstrated that Aha1 presented an inhibition effect on α-synuclein aggregation (Figure 6d,e).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P37840"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-24T13:47:15.125Z"}},{"start":1,"end":27,"reference_id":"33808352","reference_source":"pmid","reference_html":"Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity. <i> Hu H, Wang Q, Du J, Liu Z, Ding Y, Xue H, Zhou C, Feng L, Zhang N. </i> Molecules, 2021","date":"2024-10-24T13:18:28.515Z","curator_id":"ireményi","curator_name":"István Reményi ","curator_orcid":"0000-0003-4670-2406","term_id":"GO:0051082","term_name":"unfolded protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006196","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy-based hydrogen-deuterium exchange evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"EXP","region_id":"DP04219r006","statement":[{"text":"In this study, to test if the N-terminal fragment M1-W27 of Aha1 plays a role in the recognition of disordered proteins, intrinsically disordered α-synuclein was selected as a model protein. 1H-15N-HSQC spectra using 15N-labeled Aha11−338, 15N-labeled Aha128−338 and 15N-labeled Aha128−335 without or with the presence of 10-fold molar excess of unlabeled α-synuclein were recorded (Figure 6). According to the acquired 1H-15N-HSQC titration data, both the N-terminal fragment M1-W27 and the C-terminal RLF (R336L337F338) motif of Aha1 contributed to the recognition of α-synuclein. ","type":"Results"}],"term_comment":"","term_def":"\"Binding to an unfolded protein.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P37840"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-10-24T13:46:45.376Z"}},{"start":1,"end":27,"reference_id":"37486705","reference_source":"pmid","reference_html":"Human Aha1's N-terminal extension confers it holdase activity in vitro. <i> Tang J, Hu H, Zhou C, Zhang N. </i> Protein Sci, 2023","date":"2024-10-23T16:15:17.060Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":1,"region_id":"DP04219r007","statement":[{"text":"This analysis revealed that the presence of N-terminal sequence motif spanning M1 to W27 does not modify the global fold of Aha1's N-terminal domain spanning T28 to G162 (Figure 3a). Moreover, The CSI data demonstrated that the N-terminal sequence motif of Aha1 spanning M1 to W27 mainly adopts a random coil conformation (Figure 3a). In support of this finding, compared with the dynamics behavior of the core region, extremely high flexibility was observed for the N-terminal sequence motif of Aha1 spanning M1 to W27 (Figure 3b,c).","type":"Results"},{"text":"In line with the finding derived from the AlphaFold2 prediction and the 1H-15N HSQC data, the determind 1H-15N hetNOE values for Aha11-162 at low protein concentration (40 μM) revealed that the N-terminal sequence motif of Aha1 spanning M1 to W27 exhibited an extremely high flexibility. The dynamics feature of Aha1's N-terminal sequence motif spanning M1 to W27 demonstrates that this region is in an unstructured state which independent to the core structure of Aha11-162.","type":"Results"}]},{"start":1,"end":27,"reference_id":"33808352","reference_source":"pmid","reference_html":"Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity. <i> Hu H, Wang Q, Du J, Liu Z, Ding Y, Xue H, Zhou C, Feng L, Zhang N. </i> Molecules, 2021","date":"2024-10-23T18:10:19.088Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0044183","term_name":"protein folding chaperone","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007044","ec_ontology":"ECO","ec_name":"transmission electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IDA","region_id":"DP04219r008","statement":[{"text":"According to the acquired 1H-15N-HSQC titration data, both the N-terminal fragment M1-W27 and the C-terminal RLF (R336L337F338) motif of Aha1 contributed to the recognition of α-synuclein.","type":"Results"},{"text":"After the confirmation of the interaction between human Aha1 and α-synuclein, ThT assay and transmission electron microscopy (TEM) were applied to test the impact of Aha1 on the aggregation process of α-synuclein. Both the ThT data and the TEM results demonstrated that Aha1 presented an inhibition effect on α-synuclein aggregation (Figure 6d,e).","type":"Results"},{"text":"Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity.","type":"Title"}],"term_comment":"","term_def":"\"Binding to a protein or a protein-containing complex to assist the protein folding process.\" [GOC:mtg_cambridge_2009]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P37840"}]},{"start":1,"end":16,"reference_id":"37486705","reference_source":"pmid","reference_html":"Human Aha1's N-terminal extension confers it holdase activity in vitro. <i> Tang J, Hu H, Zhou C, Zhang N. </i> Protein Sci, 2023","date":"2024-10-23T18:15:16.217Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0036506","term_name":"maintenance of unfolded protein","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IDA","region_id":"DP04219r009","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0AEX9"}],"statement":[{"text":"During the experiments, the refolding process of MBP without or with the addition of known chaperone SecB, BSA serving as a negative control or Aha1 and its truncations was monitored by the change in the intrinsic tryptophan fluorescence (Figure 5). According to the obtained data, only the full-length Aha1 (Aha11-338) showed a holdase activity against the denatured MBP (Figure 5a–c). The absence of Aha1's N-terminal extension (Aha117-338) fully abolished the holdase activity of the protein, and a similar fluorescence emission profile to that of MBP alone was observed for the MBP:Aha117-338 (molar ration at 1:4) mixture sample (Figure 5c). The fluorescence data indicated that human Aha1 could act as a holdase in vitro, and its N-terminal extension is essential for the holdase activity display.","type":"Results"},{"text":"Human Aha1's N-terminal extension confers it holdase activity in vitro","type":"Title"}],"term_comment":"","term_def":"\"Maintaining a protein in an unfolded, soluble state.\" [GOC:bf, GOC:BHF, GOC:nc, GOC:PARL, PMID:21636303]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":16,"reference_id":"37486705","reference_source":"pmid","reference_html":"Human Aha1's N-terminal extension confers it holdase activity in vitro. <i> Tang J, Hu H, Zhou C, Zhang N. </i> Protein Sci, 2023","date":"2024-10-23T18:15:50.623Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0036506","term_name":"maintenance of unfolded protein","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"EXP","region_id":"DP04219r010","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0AEX9"}],"statement":[{"text":"As shown in Figure 6a, after an incubation with either SecB or full-length Aha1, the 1H-15N HSQC spectra of MBP showed a feature of unstructured protein with the amide proton resonances crowdedly distributing to the region spanning 7.5–8.5 ppm. Meanwhile, when Aha117-338, Aha121-338, and Aha128-338 were applied, the 1H-15N HSQC data demonstrated that MBP switched from the unfolded state to the folded state.","type":"Results"},{"text":"When Aha11-338W2A was applied, the 1H-15N HSQC spectrum of MBP showed a feature of unstructured protein (Figure 6c).","type":"Results"}],"term_comment":"","term_def":"\"Maintaining a protein in an unfolded, soluble state.\" [GOC:bf, GOC:BHF, GOC:nc, GOC:PARL, PMID:21636303]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":10,"released":"2024_12","sequence":"MAKWGEGDPRWIVEERADATNVNNWHWTERDASNWSTDKLKTLFLAVQVQNEEGKCEVTEVSKLDGEASINNRKGKLIFFYEWSVKLNWTGTSKSGVQYKGHVEIPNLSDENSVDEVEISVSLAKDEPDTNLVALMKEEGVKLLREAMGIYISTLKTEFTQGMILPTMNGESVDPVGQPALKTEERKAKPAPSKTQARPVGVKIPTCKITLKETFLTSPEELYRVFTTQELVQAFTHAPATLEADRGGKFHMVDGNVSGEFTDLVPEKHIVMKWRFKSWPEGHFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.11538461538461539,"dataset":["Stress response proteins"],"disorder_content":0.20710059171597633,"disprot_consensus":{"full":[{"start":1,"end":27,"type":"D"},{"start":162,"end":204,"type":"D"}],"Structural state":[{"start":1,"end":27,"type":"D"},{"start":162,"end":204,"type":"D"}],"Disorder function":[{"start":1,"end":27,"type":"F"},{"start":162,"end":204,"type":"F"}],"Molecular function":[{"start":1,"end":27,"type":"F"}],"Biological process":[{"start":1,"end":16,"type":"F"}]}},{"disprot_id":"DP04220","acc":"Q9H4H8","creator":"zskalman","date":"2024-05-14T14:51:06.433Z","features":{"pfam":[{"id":"PF07894","name":"Scaffolding anchor of CK1 domain","start":20,"end":296}],"gene3D":[]},"genes":[{"name":{"value":"FAM83D","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:16122","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:16122"}}]},"synonyms":[{"value":"C20orf129","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:16122","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:16122"}}]}]}],"length":585,"name":"Protein FAM83D","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":380,"end":448,"reference_id":"26652654","reference_source":"pmid","reference_html":"The Anchored Flexibility Model in LC8 Motif Recognition: Insights from the Chica Complex. <i> Clark S, Nyarko A, Löhr F, Karplus PA, Barbar E. </i> Biochemistry, 2016","date":"2024-05-14T15:00:23.496Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"BMRB","id":"26684"}],"region_id":"DP04220r001","statement":[{"text":"Recombinant Chica410–478 structure is in agreement with the predicted disorder; its 15N HSQC spectrum (Figure 3a) has a pronounced lack of amide proton chemical shift dispersion, and the CD spectrum shows limited ellipticity at 220 nm and a large negative ellipticity at 200 nm (Figure 3b).","type":"Results"}],"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7},{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":null,"value":293}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-07-08T15:21:45.079Z"}}],"regions_counter":3,"released":"2024_12","sequence":"MALLSEGLDEVPAACLSPCGPPNPTELFSESRRLALEELVAGGPEAFAAFLRRERLARFLNPDEVHAILRAAERPGEEGAAAAAAAEDSFGSSHDCSSGTYFPEQSDLEPPLLELGWPAFYQGAYRGATRVETHFQPRGAGEGGPYGCKDALRQQLRSAREVIAVVMDVFTDIDIFRDLQEICRKQGVAVYILLDQALLSQFLDMCMDLKVHPEQEKLMTVRTITGNIYYARSGTKIIGKVHEKFTLIDGIRVATGSYSFTWTDGKLNSSNLVILSGQVVEHFDLEFRILYAQSKPISPKLLSHFQSSNKFDHLTNRKPQSKELTLGNLLRMRLARLSSTPRKADLDPEMPAEGKAERKPHDCESSTVSEEDYFSSHRDELQSRKAIDAATQTEPGEEMPGLSVSEVGTQTSITTACAGTQTAVITRIASSQTTIWSRSTTTQTDMDENILFPRGTQSTEGSPVSKMSVSRSSSLKSSSSVSSQGSVASSTGSPASIRTTDFHNPGYPKYLGTPHLELYLSDSLRNLNKERQFHFAGIRSRLNHMLAMLSRRTLFTENHLGLHSGNFSRVNLLAVRDVALYPSYQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.4547008547008547,"disorder_content":0.11794871794871795,"disprot_consensus":{"full":[{"start":380,"end":448,"type":"D"}],"Structural state":[{"start":380,"end":448,"type":"D"}]}},{"disprot_id":"DP04221","acc":"Q8GJM6","creator":"vnugnes","date":"2024-05-16T18:10:23.298Z","features":{"pfam":[{"id":"PF31208","name":"McdB, C-terminal domain","start":86,"end":140}],"gene3D":[]},"genes":[{"name":{"value":"mcdB","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"30520729","url":"http://www.ncbi.nlm.nih.gov/pubmed/30520729","alternativeUrl":"https://europepmc.org/abstract/MED/30520729"}}]},"synonyms":[{"value":"SEN0013","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAN46163.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAN46163.1"}}]}],"olnNames":[{"value":"Synpcc7942_1834","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"ABB57864.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABB57864.1"}}]}]}],"length":152,"name":"Maintenance of carboxysome distribution protein B","ncbi_taxon_id":1140,"organism":"Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)","regions":[{"start":1,"end":18,"reference_id":"37668016","reference_source":"pmid","reference_html":"Dissecting the phase separation and oligomerization activities of the carboxysome positioning protein McdB. <i> Basalla JL, Mak CA, Byrne JA, Ghalmi M, Hoang Y, Vecchiarelli AG. </i> Elife, 2023","date":"2024-05-16T18:19:30.597Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001191","ec_ontology":"ECO","ec_name":"in vitro cleavage assay evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"region_id":"DP04221r001","statement":[{"text":"Therefore, the first 18 amino acids at the N-terminus were digested within the first minute to produce band A, and further digestion progressed slowly from the C-terminus to produce bands B and C (Figure 1B, C).","type":"Results"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Wild-type and mutant variants of McdB were expressed with an N-terminal His-SUMO tag off a pET11b vector in E. coli BL21-AI (Invitrogen)."}]},{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Wild-type and mutant variants of McdB were expressed with an N-terminal His-SUMO tag off a pET11b vector in E. coli BL21-AI (Invitrogen)."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-07-08T15:17:07.383Z"}},{"start":1,"end":18,"reference_id":"37668016","reference_source":"pmid","reference_html":"Dissecting the phase separation and oligomerization activities of the carboxysome positioning protein McdB. <i> Basalla JL, Mak CA, Byrne JA, Ghalmi M, Hoang Y, Vecchiarelli AG. </i> Elife, 2023","date":"2024-05-16T18:21:11.085Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Wild-type and mutant variants of McdB were expressed with an N-terminal His-SUMO tag off a pET11b vector in E. coli BL21-AI (Invitrogen)."}]},{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Wild-type and mutant variants of McdB were expressed with an N-terminal His-SUMO tag off a pET11b vector in E. coli BL21-AI (Invitrogen)."}]}],"region_id":"DP04221r002","statement":[{"text":"CD spectra of these truncations showed that the N-terminus was indeed disordered on its own, and both the CC domain and CTD maintained α-helical signatures (Figure 2B, Figure 2—figure supplement 1A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-07-08T15:16:50.140Z"}}],"regions_counter":2,"released":"2024_06","sequence":"MTDAFDRLKKRSRTPIAREGSLTTGPELSDRPLQLLPREFETFCDRYAVHAGDVIEAALDLVLLDPDLQQRLLQRLRQGNGSDRVWLGTACPRSWQQQLQQQAQDQGLSEADLLQEAIAQRLDLVLGQTTLREEVTLLRQELDQLKRKLHGW","taxonomy":["Bacteria","Cyanobacteriota","Cyanophyceae","Synechococcales","Synechococcaceae","Synechococcus"],"alphafold_very_low_content":0.7763157894736842,"disorder_content":0.11842105263157894,"disprot_consensus":{"full":[{"start":1,"end":18,"type":"D"}],"Structural state":[{"start":1,"end":18,"type":"D"}]}},{"disprot_id":"DP04225","acc":"A0A7M7G9Q4","creator":"vnugnes","date":"2024-07-03T17:24:12.911Z","features":{"pfam":[{"id":"PF00094","name":"von Willebrand factor type D domain","start":1476,"end":1642},{"id":"PF01347","name":"Vitellogenin TPR domain","start":412,"end":732},{"id":"PF09172","name":"Vitellinogen, open beta-sheet","start":764,"end":1042},{"id":"PF29934","name":"Vitellogenin N-terminal domain","start":23,"end":303}],"gene3D":[]},"genes":[{"name":{"value":"100122102","evidences":[{"code":"ECO:0000313","source":{"name":"EnsemblMetazoa","id":"XP_001607388","url":"http://www.ensemblgenomes.org/id/XP_001607388"}}]}}],"length":1799,"name":"Vitellogenin","ncbi_taxon_id":7425,"organism":"Nasonia vitripennis","regions":[{"start":351,"end":385,"reference_id":"22573762","reference_source":"pmid","reference_html":"A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation. <i> Havukainen H, Underhaug J, Wolschin F, Amdam G, Halskau Ø. </i> J Exp Biol, 2012","date":"2024-07-03T17:26:38.014Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04225r001","statement":[{"text":"The UV spectra of the peptides show considerable differences, suggesting a random coil for AmVg(358–392) and a more structured nature for NvVg(351–385) (Fig. 4B,D).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-07-08T15:14:52.535Z"}},{"start":335,"end":372,"reference_id":"22573762","reference_source":"pmid","reference_html":"A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation. <i> Havukainen H, Underhaug J, Wolschin F, Amdam G, Halskau Ø. </i> J Exp Biol, 2012","date":"2024-07-03T17:28:04.460Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04225r002","statement":[{"text":"NvVg(335–372), with its C-terminus located where the helix occurs in the shorter peptide, shows marked changes, with an attenuation of its NOE pattern (supplementary material Fig. S5 and Table S1). Moreover, the changes are visible in the spectrum as a collapse of the signals (supplementary material Fig. S4C), relative to Fig. 4C. The corresponding CD spectra also indicate a random coil (supplementary material Fig. S4D).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-07-08T15:14:48.281Z"}},{"start":335,"end":372,"reference_id":"22573762","reference_source":"pmid","reference_html":"A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation. <i> Havukainen H, Underhaug J, Wolschin F, Amdam G, Halskau Ø. </i> J Exp Biol, 2012","date":"2024-07-03T17:29:28.336Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"2LID"}],"region_id":"DP04225r003","statement":[{"text":"NvVg(335–372), with its C-terminus located where the helix occurs in the shorter peptide, shows marked changes, with an attenuation of its NOE pattern (supplementary material Fig. S5 and Table S1). Moreover, the changes are visible in the spectrum as a collapse of the signals (supplementary material Fig. S4C), relative to Fig. 4C.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-07-08T15:14:46.545Z"}},{"start":351,"end":385,"reference_id":"22573762","reference_source":"pmid","reference_html":"A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation. <i> Havukainen H, Underhaug J, Wolschin F, Amdam G, Halskau Ø. </i> J Exp Biol, 2012","date":"2024-07-03T17:29:59.211Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"2LID"}],"region_id":"DP04225r004","statement":[{"text":"Solving the structure of the two peptides resulted in an ensemble of outstretched coil structures in the case of AmVg(358–392) (Fig. 6A), whereas that for NvVg(351–385) contains a helix between residues 371 and 377 (Fig. 5A,D, Fig. 6C, Table 1).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-07-08T15:14:45.254Z"}}],"regions_counter":4,"released":"2024_12","sequence":"MLWSPAILLLLAGAAFASPQNGWKDGKEYTYKIRSRTLAAFNRQSKQYTGIVMEARLTVQPNGDDLLRAKISLPRYTQIHTRLENGWDSEIPQSQMNMQTFPLSGKPFEIKTKNGVVRDLIVDKDVPTWEVNVLKSIVSQLQVDTQGENAVRSKHNQFPEGNQPYALFKVMEDSVGGMCEVLYDVSALPERVIQTNPELVPIPELREDGDIISLVKTKNYSNCDQRISYHFGLNGRNKWEPSGNSKYLSRSSVSRVIVSGNLKRYTIQSSVTTNKVVLNPDQLENQHGMVASRMNLTLHEVKDIAEQVPPPSNPQSTGNLVYNYNSPTESISTRRPNKLNLQRRHDHKSGEHKHSDESSSESFESIADNNDDSYFQRKPKLTEAPQSPMLPFFIGNNGNMIHKNGKIDVVKSAKSIAQEIGNEIQRPDSMPESQTLEKVTILSRLIRTMNAEQISEVQRDLYQQRQSSNQLHQRDQAQSSRRNAWVAFRDAVAQAGTGPALVNIKQWIQNKQIQGTEAAFVVDATAKSARTPTTEYMDAFFEIVSMQETKKQRILRDSSILAFADLIRHAMVNHRSAHNRYPVHTFGRLISKDSSNLLEKYIPYMAEELKNAIDMGESQKIQVYIAAIGRTAHPRILSVFEPYLEGRKPVSPFQRLEMVLQMYKLATSHPKLARPVLYKIYSNIADHYEIRCAALFTLMKTNPPASMLQRMADFTNYDVNKHVNAAVKSIIEVLSQLQDEEFRELSNAAKAALPLLTPEKYGPQYSRVLLKTFKNSETNSEFKLVATYMGSDDSIIPKGGYLVISPVFRGMKVPMIQIGGIVNSIQDTWKFVEQKFKNFQKESQSSRKAQQQKFSPENISKLLGIHGEEPEQIEGHFFATHRNGDHYISFDNHTLEQIPEQLREMAKSMKKGVDFEETRLSGYEVILSFPMETGYPFSFTLKAPTIVSVNAQSKLMTDSELSSSELPNSATVSGKARMVYGLKVQKRLGFVIPFEHQEYIAGLDKDIQVYVPFQSEVAFDRTKNEARFTLQPHEDEKEYKILQFKSQPFTSKHDILSLQPVSIDKNTHTVHKDRASPLSFELNDQSGKQRVQFTWQNQNSYQNDDSRENKDRNAIAAATSLVSSVASLYFPISIEKAEYEKYSIKLTPSSDMNVELKASYDSLITENKDSESSESWSPNARAPHLGQSLSQGERKEKLLSEVAKNINSAKAKSVDVSVKLNAGVKASMAFTAAVGYSNVDQKSRALLFAAGKDNEGQSYHFSAGFEGKSPDTDTLDFEETLKANTRHEFDAELHYGKGSGESSNEFKDTIRIQGKAKQSEERKNQIRQSREAEECNREHDKSGNKMTQSCQMANTRASSVDSGEIIVTFESGSPLKQLSMGLVDNAESVSQDFAKVQKNREDKHDSNKIKIDFKLSPRDDKMDITLKTPEGKVEITNIDTMINNSQEKLSSQSSRNNMQTSDSNTLQISSTCDLDKTMAKTFDNHRYSLRLGKCWHVAMSSFPKNDPDRPSQQQPIPNDMHVTVLTRENENGQKELKITLGDKEIELSTSGPHEPRAKINGESIRYSKQKSHQEKQDNQIVFEIFELSDKSVKVVSDKFNVKIIYDGSRAQIQAGDRYRDSVRGLCGNNDLEPENDQQTPRGCTLQKSEEFSATYALTSEGQCEGPAVQQAEKAKSSQCTFESTRPGNVISDAEAGRTSQSGRGSDDDDSRESRRCMTHRTKVVMKNNQICFSLRPLPSCSSSCRPEETKSRAVQFHCVARSSASEKVAERVEKGANPDLTQKSVTYTESYQLPISCRA","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Hymenoptera","Apocrita","Proctotrupomorpha","Chalcidoidea","Pteromalidae","Pteromalinae","Nasonia"],"disorder_content":0.028349082823790995,"disprot_consensus":{"full":[{"start":335,"end":385,"type":"D"}],"Structural state":[{"start":335,"end":385,"type":"D"}]}},{"disprot_id":"DP04226","acc":"Q93K76","creator":"rpancsa","date":"2024-07-20T21:55:57.362Z","features":{"pfam":[{"id":"PF03333","name":"Adhesin biosynthesis transcription regulatory protein","start":8,"end":96}],"gene3D":[]},"genes":[{"name":{"value":"sfaB","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAC43422.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAC43422.1"}}]},"synonyms":[{"value":"focB","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAP09077.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAP09077.1"}}]},{"value":"papB_2","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"STP17894.1","url":"https://www.ebi.ac.uk/ena/browser/view/STP17894.1"}}]},{"value":"papB_3","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"STP20859.1","url":"https://www.ebi.ac.uk/ena/browser/view/STP20859.1"}}]}],"orfNames":[{"value":"D9E49_26250","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"MIB63832.1","url":"https://www.ebi.ac.uk/ena/browser/view/MIB63832.1"}}]},{"value":"EPS76_13665","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"RXD15911.1","url":"https://www.ebi.ac.uk/ena/browser/view/RXD15911.1"}}]},{"value":"FPI65_32455","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"NDR95789.1","url":"https://www.ebi.ac.uk/ena/browser/view/NDR95789.1"}}]},{"value":"FVB16_05940","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"MPU48394.1","url":"https://www.ebi.ac.uk/ena/browser/view/MPU48394.1"}}]},{"value":"NCTC9075_01327","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"STP17894.1","url":"https://www.ebi.ac.uk/ena/browser/view/STP17894.1"}}]},{"value":"NCTC9075_04326","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"STP20859.1","url":"https://www.ebi.ac.uk/ena/browser/view/STP20859.1"}}]}]}],"length":109,"name":"FocB protein","ncbi_taxon_id":562,"organism":"Escherichia coli","regions":[{"start":100,"end":109,"reference_id":"20646069","reference_source":"pmid","reference_html":"Structure of FocB--a member of a family of transcription factors regulating fimbrial adhesin expression in uropathogenic Escherichia coli. <i> Hultdin UW, Lindberg S, Grundström C, Huang S, Uhlin BE, Sauer-Eriksson AE. </i> FEBS J, 2010","date":"2024-10-30T08:24:48.626Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"3M8J"}],"region_id":"DP04226r001","statement":[{"text":"The E. coli FocB structure (109 amino acid residues) was determined at a resolution of 1.4 Å by multiwavelength anomalous diffraction [26] from a single crystal of the selenomethionine labeled protein. The crystal comprised two molecules per asymmetric unit. Apart from several residues at the N- and C-terminal ends, all protein residues could be modeled into the electron density. The final model contains residues 10–99 of chain A and residues 10–97 of chain B.","type":"Results"},{"text":"The final R-values, Rwork = 0.196 and Rfree = 0.222, are higher than expected for this resolution. This is probably a result of the additional electron density ascribed to the N- and C-terminal residues of the protein, which were not modeled in the structure because of disorder.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T15:49:50.171Z"}},{"start":100,"end":109,"reference_id":"20646069","reference_source":"pmid","reference_html":"Structure of FocB--a member of a family of transcription factors regulating fimbrial adhesin expression in uropathogenic Escherichia coli. <i> Hultdin UW, Lindberg S, Grundström C, Huang S, Uhlin BE, Sauer-Eriksson AE. </i> FEBS J, 2010","date":"2024-10-30T08:28:01.233Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"3M8J"}],"region_id":"DP04226r002","statement":[{"text":"The E. coli FocB structure (109 amino acid residues) was determined at a resolution of 1.4 Å by multiwavelength anomalous diffraction [26] from a single crystal of the selenomethionine labeled protein. The crystal comprised two molecules per asymmetric unit. Apart from several residues at the N- and C-terminal ends, all protein residues could be modeled into the electron density. The final model contains residues 10–99 of chain A and residues 10–97 of chain B.","type":"Results"},{"text":"The final R-values, Rwork = 0.196 and Rfree = 0.222, are higher than expected for this resolution. This is probably a result of the additional electron density ascribed to the N- and C-terminal residues of the protein, which were not modeled in the structure because of disorder.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T15:49:54.463Z"}}],"regions_counter":2,"released":"2024_12","sequence":"MAQHEVITRGGDAFLLKLRESALSSGSMSEEQFFLLIGISSIHSDRVILAMKDYLVSGHSRKDVCEKYQMNNGYFSTTLGRLTRLNVLVARLAPYYTDSVSAIAEAASL","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"alphafold_very_low_content":0.10091743119266056,"dataset":[],"disorder_content":0.09174311926605505,"disprot_consensus":{"full":[{"start":100,"end":109,"type":"D"}],"Structural state":[{"start":100,"end":109,"type":"D"}],"Disorder function":[{"start":100,"end":109,"type":"F"}]}},{"disprot_id":"DP04227","acc":"P40727","creator":"rpancsa","date":"2024-07-22T08:17:33.984Z","features":{"pfam":[{"id":"PF01312","name":"FlhB HrpN YscU SpaS Family","start":7,"end":347}],"gene3D":[]},"genes":[{"name":{"value":"flhB"},"olnNames":[{"value":"STM1914"}]}],"length":383,"name":"Flagellar biosynthetic protein FlhB","ncbi_taxon_id":99287,"organism":"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","regions":[{"start":219,"end":229,"reference_id":"23633590","reference_source":"pmid","reference_html":"Inhibition of a type III secretion system by the deletion of a short loop in one of its membrane proteins. <i> Meshcheryakov VA, Kitao A, Matsunami H, Samatey FA. </i> Acta Crystallogr D Biol Crystallogr, 2013","date":"2024-07-22T08:22:53.873Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"3B0Z"}],"region_id":"DP04227r001","statement":[{"text":"In the case of SalFlhBC the final model comprises residues 229–353 out of 219–383 in the crystallized protein, with a cleavage after Asn269. No electron density was observed for residues 219–228 and 354–383.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-25T07:15:54.365Z"}},{"start":354,"end":383,"reference_id":"23633590","reference_source":"pmid","reference_html":"Inhibition of a type III secretion system by the deletion of a short loop in one of its membrane proteins. <i> Meshcheryakov VA, Kitao A, Matsunami H, Samatey FA. </i> Acta Crystallogr D Biol Crystallogr, 2013","date":"2024-07-22T08:25:26.729Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"3B0Z"}],"region_id":"DP04227r002","statement":[{"text":"In the case of SalFlhBC the final model comprises residues 229–353 out of 219–383 in the crystallized protein, with a cleavage after Asn269. No electron density was observed for residues 219–228 and 354–383.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-25T07:15:32.282Z"}}],"regions_counter":2,"released":"2024_12","sequence":"MAEESDDDKTEAPTPHRLEKAREEGQIPRSRELTSLLILLVGVCIIWFGGESLARQLAGMLSAGLHFDHRMVNDPNLILGQIILLIKAAMMALLPLIAGVVLVALISPVMLGGLIFSGKSLQPKFSKLNPLPGIKRMFSAQTGAELLKAVLKSTLVGCVTGFYLWHHWPQMMRLMAESPIVAMGNALDLVGLCALLVVLGVIPMVGFDVFFQIFSHLKKLRMSRQDIRDEFKESEGDPHVKGKIRQMQRAAAQRRMMEDVPKADVIVTNPTHYSVALQYDENKMSAPKVVAKGAGLIALRIREIGAEHRVPTLEAPPLARALYRHAEIGQQIPGQLYAAVAEVLAWVWQLKRWRLAGGQRPPQPENLPVPEALDFMNEKNTDG","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"],"alphafold_very_low_content":0.028720626631853787,"disorder_content":0.10704960835509138,"disprot_consensus":{"full":[{"start":219,"end":229,"type":"D"},{"start":354,"end":383,"type":"D"}],"Structural state":[{"start":219,"end":229,"type":"D"},{"start":354,"end":383,"type":"D"}]}},{"disprot_id":"DP04228","acc":"O67813","creator":"rpancsa","date":"2024-07-22T08:28:12.552Z","features":{"pfam":[{"id":"PF01312","name":"FlhB HrpN YscU SpaS Family","start":5,"end":341}],"gene3D":[]},"genes":[{"name":{"value":"flhB"},"olnNames":[{"value":"aq_2014"}]}],"length":350,"name":"Flagellar biosynthetic protein FlhB","ncbi_taxon_id":224324,"organism":"Aquifex aeolicus (strain VF5)","regions":[{"start":213,"end":231,"reference_id":"23633590","reference_source":"pmid","reference_html":"Inhibition of a type III secretion system by the deletion of a short loop in one of its membrane proteins. <i> Meshcheryakov VA, Kitao A, Matsunami H, Samatey FA. </i> Acta Crystallogr D Biol Crystallogr, 2013","date":"2024-07-22T08:29:42.157Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"3B1S"}],"region_id":"DP04228r001","statement":[{"text":"The three molecules in the asymmetric unit are very similar, with r.m.s.d.s on pairwise superposition in the range 0.40–0.76 Å. Each molecule consists of two polypeptide chains resulting from proteolytic cleavage after Asn263. In all molecules no electron density was observed for residues 213–231 at the N-terminus; depending on the molecule, two to six residues at the C-terminus were disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-25T07:17:48.825Z"}}],"regions_counter":1,"released":"2024_12","sequence":"MAEEHKTERATPYKRRKVREEGNVAKSHEIASSLVVLLSLLLLLFLGTYIAKEVILIFLAVTGYVHADISELGSLYENFYENIVKVLTPLFFLALLVVILSHVAQFGFIFTLKPLSFKWERINPFEGIKRLISLTTLFETVKNTLKAFLLIGIAVFVLKGSLYFFLSSSTYPLAETLKSFIKTSAITLITLGVVALLIAFLDYAFKRWQYEKKIMMSRRELKEEYKQLEGHPEVKSRIKARMRELAKSRMMAEVPKATVVITNPTHIAIALKYNPEKDKAPVVVAKGKGTIAQKIVEIAENYSIPVVRKPELARALYPAVEVGKEISPKFYKAVAEIIAYVMFKKKKVYA","taxonomy":["Bacteria","Aquificota","Aquificia","Aquificales","Aquificaceae","Aquifex"],"alphafold_very_low_content":0.008571428571428572,"disorder_content":0.054285714285714284,"disprot_consensus":{"full":[{"start":213,"end":231,"type":"D"}],"Structural state":[{"start":213,"end":231,"type":"D"}]}},{"disprot_id":"DP04229","acc":"P9WFG9","creator":"rpancsa","date":"2024-07-22T08:49:12.290Z","features":{"pfam":[{"id":"PF08768","name":"THAP4-like, heme-binding beta-barrel domain","start":65,"end":223}],"gene3D":[]},"genes":[{"olnNames":[{"value":"Rv0813c"}]}],"length":226,"name":"Peroxynitrite isomerase 2","ncbi_taxon_id":83332,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","regions":[{"start":132,"end":144,"reference_id":"17172346","reference_source":"pmid","reference_html":"The crystal structure of Rv0813c from Mycobacterium tuberculosis reveals a new family of fatty acid-binding protein-like proteins in bacteria. <i> Shepard W, Haouz A, Graña M, Buschiazzo A, Betton JM, Cole ST, Alzari PM. </i> J Bacteriol, 2007","date":"2024-07-22T08:54:15.846Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"2FWV"}],"region_id":"DP04229r001","statement":[{"text":"The 10-stranded β-barrel is well defined in density, except for the solvent-exposed loop 132 to 144, which is presumably disordered in the crystal structure.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-25T07:21:54.377Z"}},{"start":1,"end":26,"reference_id":"17172346","reference_source":"pmid","reference_html":"The crystal structure of Rv0813c from Mycobacterium tuberculosis reveals a new family of fatty acid-binding protein-like proteins in bacteria. <i> Shepard W, Haouz A, Graña M, Buschiazzo A, Betton JM, Cole ST, Alzari PM. </i> J Bacteriol, 2007","date":"2024-10-30T10:17:58.027Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"2FWV"}],"region_id":"DP04229r002","statement":[{"text":"This small domain is well conserved in homologous proteins from mycobacteria and corynebacteria (see below) and comprises a long amphipathic α-helix that extends into the solvent and is increasingly disordered toward its N terminus (no density is observed for the first 26 residues in the crystal structure).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T15:50:19.110Z"}},{"start":1,"end":26,"reference_id":"17172346","reference_source":"pmid","reference_html":"The crystal structure of Rv0813c from Mycobacterium tuberculosis reveals a new family of fatty acid-binding protein-like proteins in bacteria. <i> Shepard W, Haouz A, Graña M, Buschiazzo A, Betton JM, Cole ST, Alzari PM. </i> J Bacteriol, 2007","date":"2024-10-30T10:18:23.882Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"2FWV"}],"region_id":"DP04229r003","statement":[{"text":"This small domain is well conserved in homologous proteins from mycobacteria and corynebacteria (see below) and comprises a long amphipathic α-helix that extends into the solvent and is increasingly disordered toward its N terminus (no density is observed for the first 26 residues in the crystal structure).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T15:50:24.115Z"}}],"regions_counter":3,"released":"2024_12","sequence":"MSSGAGSDATGAGGVHAAGSGDRAVAAAVERAKATAARNIPAFDDLPVPADTANLREGADLNNALLALLPLVGVWRGEGEGRGPDGDYRFGQQIVVSHDGGDYLNWESRSWRLTATGDYQEPGLREAGFWRFVADPYDPSESQAIELLLAHSAGYVELFYGRPRTQSSWELVTDALARSRSGVLVGGAKRLYGIVEGGDLAYVEERVDADGGLVPHLSARLSRFVG","taxonomy":["Bacteria","Actinomycetota","Actinomycetes","Mycobacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"alphafold_very_low_content":0.07079646017699115,"disorder_content":0.17256637168141592,"disprot_consensus":{"full":[{"start":1,"end":26,"type":"D"},{"start":132,"end":144,"type":"D"}],"Structural state":[{"start":1,"end":26,"type":"D"},{"start":132,"end":144,"type":"D"}],"Disorder function":[{"start":1,"end":26,"type":"F"}]}},{"disprot_id":"DP04230","acc":"P43769","creator":"rpancsa","date":"2024-07-22T09:02:56.309Z","features":{"pfam":[{"id":"PF02472","name":"Biopolymer transport protein ExbD/TolR","start":10,"end":137}],"gene3D":[]},"genes":[{"name":{"value":"tolR","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_02203","url":"https://hamap.expasy.org/unirule/MF_02203"}}]},"olnNames":[{"value":"HI_0384"}]}],"length":139,"name":"Tol-Pal system protein TolR","ncbi_taxon_id":71421,"organism":"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","regions":[{"start":39,"end":58,"reference_id":"18269247","reference_source":"pmid","reference_html":"The periplasmic domain of TolR from Haemophilus influenzae forms a dimer with a large hydrophobic groove: NMR solution structure and comparison to SAXS data. <i> Parsons LM, Grishaev A, Bax A. </i> Biochemistry, 2008","date":"2024-10-30T08:30:11.843Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04230r001","statement":[{"text":"To further improve the spectral appearance, a third clone lacking residues 39-58 was constructed. These residues, which connect the transmembrane helix to the structured domain, were highly flexible based on a lack of 1 H-1 H NOE connectivities and low 15 N R2 relaxation rates (data not shown).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T15:51:12.588Z"}}],"regions_counter":1,"released":"2024_12","sequence":"MARRQRKAIKSEINIVPFLDVLLVLVLIFMATAPIISQSVQVELPDSVQSQEVSNEDKVPVILEVAGIGKYAISIGGERQEGLTEEMVTQLSRQEFDKDNNTLFLVGGAKEVPYEEVIKALNLLHLAGIKSVGLMTNPI","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Pasteurellales","Pasteurellaceae","Haemophilus"],"alphafold_very_low_content":0.05755395683453238,"dataset":["Viral proteins"],"disorder_content":0.14388489208633093,"disprot_consensus":{"full":[{"start":39,"end":58,"type":"D"}],"Structural state":[{"start":39,"end":58,"type":"D"}]}},{"disprot_id":"DP04231","acc":"P23023","creator":"rpancsa","date":"2024-07-22T09:37:33.138Z","features":{"pfam":[{"id":"PF00751","name":"DM DNA binding domain","start":41,"end":86},{"id":"PF08828","name":"Doublesex dimerisation domain","start":352,"end":399}],"gene3D":[]},"genes":[{"name":{"value":"dsx"},"orfNames":[{"value":"CG11094"}]}],"length":549,"name":"Protein doublesex","ncbi_taxon_id":7227,"organism":"Drosophila melanogaster","regions":[{"start":408,"end":427,"reference_id":"18184648","reference_source":"pmid","reference_html":"Doublesex and the regulation of sexual dimorphism in Drosophila melanogaster: structure, function, and mutagenesis of a female-specific domain. <i> Yang Y, Zhang W, Bayrer JR, Weiss MA. </i> J Biol Chem, 2008","date":"2024-10-30T15:19:40.472Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":30,"statements":[{"type":"Methods","text":"Protein samples were prepared in nitrogen-purged H 2O solution (7% D 2 O) containing 10 m M 2H-Tris-HCl (pH 6.5) and 250 mM NaCl in a 300-\u0003l Shigemi NMR tube; the\nprotein concentration was in each case \u00051.5 m M . One-, two-, and three-dimensional NMR spectra were acquired at 30 °C at 700 MHz using a triple resonance probe and a shielded (x, y, z)-gradient unit; four-dimensional 13 C/ 13 C NOESY spectra were acquired at 600 MHz."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.5,"statements":[{"type":"Methods","text":"Protein samples were prepared in nitrogen-purged H 2O solution (7% D 2 O) containing 10 m M 2H-Tris-HCl (pH 6.5) and 250 mM NaCl in a 300-\u0003l Shigemi NMR tube; the protein concentration was in each case \u00051.5 m M . One-, two-, and three-dimensional NMR spectra were acquired at 30 °C at 700 MHz using a triple resonance probe and a shielded (x, y, z)-gradient unit; four-dimensional 13 C/ 13 C NOESY spectra were acquired at 600 MHz."}]}],"cross_refs":[{"db":"PDB","id":"2JZ1"}],"region_id":"DP04231r001","statement":[{"text":"Evidence of disorder is provided by four sets of observations. First, resonances in the C-terminal tail exhibit motional narrowing relative to resonances in the UBA folds. Such differences in line widths lead to systematic differences in cross-peak patterns in the three-dimensional HNCACB spectrum (supplemental material). Although, due to line broadening, residues in the UBA fold predominantly exhibit intraresidue cross-peaks with few interresidue Cα and no Cβ cross-peaks, residues in the C-terminal portion of the sex-specific tail (residues 409 – 427) exhibit complete Cα and Cβ connectivities (supplemental material). Second, the pattern of chemical shifts in the C-terminal portion of the tail, unlike those in the UBA fold, is consistent with random coil. Third, the absence of stably folded tail structure is further indicated by an absence of medium and long range NOEs; only sequential and intraresidue NOEs were observed between residues 409 – 427 in three- and four-dimensional 13 C- and 15 N-edited NOESY spectra. Finally, truncation of the tail after residue 412 (i.e. comparison of CTD F -p and CTD F -pΔ) reveals a correspondence of chemical shifts and NOE patterns, demonstrating that the presence or absence of an intact tail does not modulate the folding of the core domain.","type":"Results"},{"text":"The proximal portion of the female-specific tail (residues 398 – 407) contributes to the α-helical structure of UBA fold, whereas the distal portion (residues 408 – 427) is largely disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T15:52:06.886Z"}}],"regions_counter":1,"released":"2024_12","sequence":"MVSEENWNSDTMSDSDMIDSKNDVCGGASSSSGSSISPRTPPNCARCRNHGLKITLKGHKRYCKFRYCTCEKCRLTADRQRVMALQTALRRAQAQDEQRALHMHEVPPANPAATTLLSHHHHVAAPAHVHAHHVHAHHAHGGHHSHHGHVLHHQQAAAAAAAAPSAPASHLGGSSTAASSIHGHAHAHHVHMAAAAAASVAQHQHQSHPHSHHHHHQNHHQHPHQQPATQTALRSPPHSDHGGSVGPATSSSGGGAPSSSNAAAATSSNGSSGGGGGGGGGSSGGGAGGGRSSGTSVITSADHHMTTVPTPAQSLEGSCDSSSPSPSSTSGAAILPISVSVNRKNGANVPLGQDVFLDYCQKLLEKFRYPWELMPLMYVILKDADANIEEASRRIEEARVEINRTVAQIYYNYYTPMALVNGAPMYLTYPSIEQGRYGAHFTHLPLTQICPPTPEPLALSRSPSSPSGPSAVHNQKPSRPGSSNGTVHSAASPTMVTTMATTSSTPTLSRRQRSRSATPTTPPPPPPAHSSSNGAYHHGHHLVSSTAAT","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"alphafold_very_low_content":0.6302367941712204,"dataset":[],"disorder_content":0.03642987249544627,"disprot_consensus":{"full":[{"start":408,"end":427,"type":"D"}],"Structural state":[{"start":408,"end":427,"type":"D"}]}},{"disprot_id":"DP04232","acc":"Q3U0P1","creator":"rpancsa","date":"2024-07-22T12:58:33.927Z","features":{"pfam":[{"id":"PF16756","name":"Partner and localizer of BRCA2 WD40 domain","start":758,"end":1102}],"gene3D":[]},"genes":[{"name":{"value":"Palb2"}}],"length":1104,"name":"Partner and localizer of BRCA2","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":1,"end":10,"reference_id":"30289697","reference_source":"pmid","reference_html":"Antiparallel Coiled-Coil Interactions Mediate the Homodimerization of the DNA Damage-Repair Protein PALB2. <i> Song F, Li M, Liu G, Swapna GVT, Daigham NS, Xia B, Montelione GT, Bunting SF. </i> Biochemistry, 2018","date":"2024-07-22T13:03:48.082Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":20,"statements":[{"type":"Methods","text":"All NMR data for resonance assignments and structure determination were collected at 20 °C using Bruker AVANCE II 600 MHz and 800 MHz NMR spectrometers equipped with 5-mm cryoprobes."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.5,"statements":[{"type":"Methods","text":"Uniformly 13C,15N- and 5% 13C, U-15N-enriched PALB2cc and [L24]-PALB2cc samples for NMR studies were prepared using standard protocols 24, and concentrated to 1.2-1.5 mM in 95% H2O and 5% 2H2O solution containing 20 mM MES buffer at pH 6.5, 200 mM NaCl, 10 mM DTT, and 5 mM CaCl2 (except where otherwise specified)."}]}],"cross_refs":[{"db":"PDB","id":"6E4H"},{"db":"BMRB","id":"27534"}],"region_id":"DP04232r001","statement":[{"text":"Ordered residue range: residues 11 – 39. RPF scores reflect the goodness of fit of the final ensemble of structures (including disordered residues) to the NMR data.","type":"Table"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-25T07:39:37.106Z"}},{"start":40,"end":60,"reference_id":"30289697","reference_source":"pmid","reference_html":"Antiparallel Coiled-Coil Interactions Mediate the Homodimerization of the DNA Damage-Repair Protein PALB2. <i> Song F, Li M, Liu G, Swapna GVT, Daigham NS, Xia B, Montelione GT, Bunting SF. </i> Biochemistry, 2018","date":"2024-07-22T13:04:07.632Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":20,"statements":[{"type":"Methods","text":"All NMR data for resonance assignments and structure determination were collected at 20 °C using Bruker AVANCE II 600 MHz and 800 MHz NMR spectrometers equipped with 5-mm cryoprobes."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.5,"statements":[{"type":"Methods","text":"Uniformly 13C,15N- and 5% 13C, U-15N-enriched PALB2cc and [L24]-PALB2cc samples for NMR studies were prepared using standard protocols 24, and concentrated to 1.2-1.5 mM in 95% H2O and 5% 2H2O solution containing 20 mM MES buffer at pH 6.5, 200 mM NaCl, 10 mM DTT, and 5 mM CaCl2 (except where otherwise specified)."}]}],"cross_refs":[{"db":"PDB","id":"6E4H"},{"db":"BMRB","id":"27534"}],"region_id":"DP04232r002","statement":[{"text":"Ordered residue range: residues 11 – 39. RPF scores reflect the goodness of fit of the final ensemble of structures (including disordered residues) to the NMR data.","type":"Table"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-25T07:39:32.273Z"}}],"regions_counter":2,"released":"2024_12","sequence":"MEELSGKPLSYAEKEKLKEKLAFLKKEYSRTLARLQRAKRAEKAKNSKKAIEDGVPQPEASSQLSHSESINKGFPCDTLQSNHLDEETGENISQILDVEPQSFNCKQGKEVLHTPRAGDIQGQLLHSTSSPDGKKEQNTLPGTTKTPWEKSSVSQEKEDYFDTNSLALLGKHRKGQESISRKNSRTPVSEKTHLLSLRSQIPDPPALVTGIGEGILIPPSGKSERGIDTLVRGNTVSAEAAVPSCTASNSNHSQHLEHTPPKSGCKITTQGPASSTNLVAQDQKMTIFTVNSVVYKAVRAHGQLPGSPNSCSVNDLTHSNLPANSTPNSKSLKSPSNTVDERNEPLQEDEILGPSKNFNLAAVSPPSTESQIHSCTMLEGLLFPAEYYVRTTRRMSDCQRKIALEAVIQSHLGVKKKELKKKTKATKAVVLSSEDTDQSESGMLDTSTGQSSSGSLSQKLLSPAEVSSPPGPAGKATTPPPGRGHRGKRKSARTSTLGHCQLLFPPCAALAVNRSKGKFTKHKCQNRGVVIHDFELPDEDFGLLKLEKLKSCSEKLIESPDSKNCGERLPREGNHAALEELQRDSETEGLEEELTVPPGEAYRPGPTLRRQPGSKDLSSSIVLFTPADTAAPNDSGRPPPSLCSPAFPILGMTPALGSQAAGETLSTEAAQPCSTSQPPLLGDTNSLVNNSKQCNSSACSPKPDTNLQASGRQGQPACDSDSGPQATPLPVESFTFRENQLCGNACLELHEHSTEQTETADRPACDNLNPGNLQLVSELKNPSSSCSVDVSAMWWERAGAKEPCIVTACEDVVSLWKPLNSLQWEKVHTWHFTEVPVLQIVPVPDVYNLICVALGSLEIREIRALLCSSGDDSEKQVLLKSGDIKAMLGLTKRRLVSSTGTFCNQQIQIMTFADDGSSKDEQLLMPPDETVLTFAEVQGTQEALLGTTTVNSIVIWNLKTGQLLKKMHIDDSYQASVCHGAYSEKGLLFVVVSQPCAKESQALGSPVFQLLVINPKTAQSVGVLLCSLPQGQAGRFLEGDVKDHVAAAVLTSGTIAIWDLLLGHCTALLPPVSDQSWSLVKWSGTDSHLLAGQKDGNIFIYRYF","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"alphafold_very_low_content":0.6222826086956522,"disorder_content":0.028079710144927536,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"},{"start":40,"end":60,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":40,"end":60,"type":"D"}]}},{"disprot_id":"DP04233","acc":"P9WMI9","creator":"rpancsa","date":"2024-07-22T14:07:57.700Z","features":{"pfam":[{"id":"PF01022","name":"Bacterial regulatory protein, arsR family","start":20,"end":64}],"gene3D":[]},"genes":[{"name":{"value":"cmtR"},"orfNames":[{"value":"MTCY39.25"}],"olnNames":[{"value":"Rv1994c"}]}],"length":118,"name":"HTH-type transcriptional regulator CmtR","ncbi_taxon_id":83332,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","regions":[{"start":106,"end":118,"reference_id":"17599915","reference_source":"pmid","reference_html":"NMR structural analysis of cadmium sensing by winged helix repressor CmtR. <i> Banci L, Bertini I, Cantini F, Ciofi-Baffoni S, Cavet JS, Dennison C, Graham AI, Harvie DR, Robinson NJ. </i> J Biol Chem, 2007","date":"2024-07-22T14:10:18.039Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"2JSC"}],"region_id":"DP04233r001","statement":[{"text":"The NH cross-peaks of the C-terminal region (residues 106 –118) are all clustered in the typical spectral region of unstructured proteins and are\nhighly flexible, displaying backbone mobility in the nanosecond to picosecond time scale, considerably faster than the overall protein tumbling rate (supplemental Fig. S4). Consequently this region is characterized by a very low number of long range NOEs (supplemental Fig. S5).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-25T07:40:42.628Z"}},{"start":106,"end":118,"reference_id":"17599915","reference_source":"pmid","reference_html":"NMR structural analysis of cadmium sensing by winged helix repressor CmtR. <i> Banci L, Bertini I, Cantini F, Ciofi-Baffoni S, Cavet JS, Dennison C, Graham AI, Harvie DR, Robinson NJ. </i> J Biol Chem, 2007","date":"2024-10-30T09:57:14.528Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"2JSC"}],"region_id":"DP04233r002","statement":[{"text":"The NH cross-peaks of the C-terminal region (residues 106 –118) are all clustered in the typical spectral region of unstructured proteins and are highly flexible, displaying backbone mobility in the nanosecond to picosecond time scale, considerably faster than the overall protein tumbling rate (supplemental Fig. S4). Consequently this region is characterized by a very low number of long range NOEs (supplemental Fig. S5).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T15:52:37.687Z"}}],"regions_counter":2,"released":"2024_12","sequence":"MLTCEMRESALARLGRALADPTRCRILVALLDGVCYPGQLAAHLGLTRSNVSNHLSCLRGCGLVVATYEGRQVRYALADSHLARALGELVQVVLAVDTDQPCVAERAASGEAVEMTGS","taxonomy":["Bacteria","Actinomycetota","Actinomycetes","Mycobacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"alphafold_very_low_content":0.1016949152542373,"dataset":[],"disorder_content":0.11016949152542373,"disprot_consensus":{"full":[{"start":106,"end":118,"type":"D"}],"Structural state":[{"start":106,"end":118,"type":"D"}],"Disorder function":[{"start":106,"end":118,"type":"F"}]}},{"disprot_id":"DP04234","acc":"O88574","creator":"rpancsa","date":"2024-07-22T17:53:58.276Z","features":{"pfam":[{"id":"PF13866","name":"SAP30 zinc-finger","start":64,"end":133},{"id":"PF13867","name":"Sin3 binding region of histone deacetylase complex subunit SAP30","start":153,"end":205}],"gene3D":[]},"genes":[{"name":{"value":"Sap30","evidences":[{"code":"ECO:0000312","source":{"name":"MGI","id":"MGI:1929129","url":"http://www.informatics.jax.org/marker/MGI:1929129"}}]}}],"length":220,"name":"Histone deacetylase complex subunit SAP30","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":130,"end":142,"reference_id":"21676866","reference_source":"pmid","reference_html":"Structure of the 30-kDa Sin3-associated protein (SAP30) in complex with the mammalian Sin3A corepressor and its role in nucleic acid binding. <i> Xie T, He Y, Korkeamaki H, Zhang Y, Imhoff R, Lohi O, Radhakrishnan I. </i> J Biol Chem, 2011","date":"2024-07-22T18:00:14.390Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":35,"statements":[{"type":"Methods","text":"All NMR data were acquired on a Varian Inova 600-MHz spectrometer equipped with a pulsed field gradient triple resonance cold probe at 35 °C."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.5,"statements":[{"type":"Methods","text":"The sample was exchanged into NMR buffer containing 20 mm sodium phosphate (pH 6.5), 2 mm DTT-d10, and 0.2% (w/v) NaN3 using a YM-3 Centricon unit with a 3000 Da cut-off (Millipore)."}]}],"cross_refs":[{"db":"PDB","id":"2LD7"},{"db":"BMRB","id":"17653"}],"region_id":"DP04234r001","statement":[{"text":"The vast majority of the residues of both mSin3A PAH3 and SAP30 SID adopt well defined conformations, although the four N-terminal and two C-terminal residues of mSin3A PAH3 as well as the 13 N-terminal and 11 C-terminal residues of SAP30 SID are disordered in the complex.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-25T07:42:56.430Z"}},{"start":210,"end":220,"reference_id":"21676866","reference_source":"pmid","reference_html":"Structure of the 30-kDa Sin3-associated protein (SAP30) in complex with the mammalian Sin3A corepressor and its role in nucleic acid binding. <i> Xie T, He Y, Korkeamaki H, Zhang Y, Imhoff R, Lohi O, Radhakrishnan I. </i> J Biol Chem, 2011","date":"2024-07-22T18:01:03.530Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":35,"statements":[{"type":"Methods","text":"All NMR data were acquired on a Varian Inova 600-MHz spectrometer equipped with a pulsed field gradient triple resonance cold probe at 35 °C."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.5,"statements":[{"type":"Methods","text":"The sample was exchanged into NMR buffer containing 20 mm sodium phosphate (pH 6.5), 2 mm DTT-d10, and 0.2% (w/v) NaN3 using a YM-3 Centricon unit with a 3000 Da cut-off (Millipore)."}]}],"cross_refs":[{"db":"PDB","id":"2LD7"},{"db":"BMRB","id":"17653"}],"region_id":"DP04234r002","statement":[{"text":"The vast majority of the residues of both mSin3A PAH3 and SAP30 SID adopt well defined conformations, although the four N-terminal and two C-terminal residues of mSin3A PAH3 as well as the 13 N-terminal and 11 C-terminal residues of SAP30 SID are disordered in the complex.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-25T07:42:52.328Z"}}],"regions_counter":2,"released":"2024_12","sequence":"MNGFTPEEMSRGGDAAAAVAAVVAAAAAAASAGNGNAAGGGAEVPGAGAVSASGPPGAAGPGPGQLCCLREDGERCGRAAGNASFSKRIQKSISQKKVKIELDKSARHLYICDYHKNLIQSVRNRRKRKGSDDDGGDSPVQDIDTPEVDLYQLQVNTLRRYKRHFKLPTRPGLNKAQLVEIVGCHFKSIPVNEKDTLTCFIYSVRNDKNKSDLKADSGVH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"alphafold_very_low_content":0.2545454545454545,"disorder_content":0.10909090909090909,"disprot_consensus":{"full":[{"start":130,"end":142,"type":"D"},{"start":210,"end":220,"type":"D"}],"Structural state":[{"start":130,"end":142,"type":"D"},{"start":210,"end":220,"type":"D"}]}},{"disprot_id":"DP04235","acc":"Q03390","creator":"rpancsa","date":"2024-07-22T18:32:22.618Z","features":{"pfam":[{"id":"PF03357","name":"Snf7","start":19,"end":183}],"gene3D":[]},"genes":[{"name":{"value":"VPS60"},"synonyms":[{"value":"CHM5"},{"value":"MOS10"}],"olnNames":[{"value":"YDR486C"}]}],"length":229,"name":"Vacuolar protein-sorting-associated protein 60","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":128,"end":186,"reference_id":"23105107","reference_source":"pmid","reference_html":"Structural basis of molecular recognition between ESCRT-III-like protein Vps60 and AAA-ATPase regulator Vta1 in the multivesicular body pathway. <i> Yang Z, Vild C, Ju J, Zhang X, Liu J, Shen J, Zhao B, Lan W, Gong F, Liu M, Cao C, Xu Z. </i> J Biol Chem, 2012","date":"2024-07-22T18:44:30.875Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04235r001","statement":[{"text":"To confirm this observation, we preformed CD spectroscopy on free Vps60(128–186), where negative absorption at ∼200 nm shows a random coil conformation (Fig. 2E).","type":"Results"}],"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Methods","text":"To probe the folding of free Vps60(128–186), the CD experiment was performed at 25 °C on a JASCO-715 spectropolarimeter (Jasco International Co., Tokyo, Japan)."}]}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-25T07:46:34.650Z"}},{"start":128,"end":186,"reference_id":"23105107","reference_source":"pmid","reference_html":"Structural basis of molecular recognition between ESCRT-III-like protein Vps60 and AAA-ATPase regulator Vta1 in the multivesicular body pathway. <i> Yang Z, Vild C, Ju J, Zhang X, Liu J, Shen J, Zhao B, Lan W, Gong F, Liu M, Cao C, Xu Z. </i> J Biol Chem, 2012","date":"2024-07-22T18:43:45.737Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":20,"statements":[{"type":"Methods","text":"All NMR experiments were performed at 20 °C on a Varian Unity Inova 600 NMR spectrometer (with cryo-probe) equipped with triple resonances and pulsed-field gradients or on a Bruker AVANCE III 800-MHz NMR spectrometer (with cryo-probe) equipped with four channels and z axis pulsed-field gradient."}]}],"region_id":"DP04235r002","statement":[{"text":"The two-dimensional NMR 1H-15N HSQC experiment with Vps60(128–186) in its free state (Fig. 2D) suggests that Vps60(128–186) in its free state is disordered because the cross-peaks are not dispersed, localizing mainly in the region between 8.0 and 8.5 ppm.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-25T07:46:30.382Z"}},{"start":128,"end":186,"reference_id":"23105107","reference_source":"pmid","reference_html":"Structural basis of molecular recognition between ESCRT-III-like protein Vps60 and AAA-ATPase regulator Vta1 in the multivesicular body pathway. <i> Yang Z, Vild C, Ju J, Zhang X, Liu J, Shen J, Zhao B, Lan W, Gong F, Liu M, Cao C, Xu Z. </i> J Biol Chem, 2012","date":"2024-07-22T18:46:52.066Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":20,"statements":[{"type":"Methods","text":"All NMR experiments were performed at 20 °C on a Varian Unity Inova 600 NMR spectrometer (with cryo-probe) equipped with triple resonances and pulsed-field gradients or on a Bruker AVANCE III 800-MHz NMR spectrometer (with cryo-probe) equipped with four channels and z axis pulsed-field gradient."}]}],"cross_refs":[{"db":"PDB","id":"2LUH"}],"region_id":"DP04235r003","statement":[{"text":"Upon binding to Vta1NTD, the cross-peaks in two-dimensional NMR 1H-15N HSQC of Vps60(128–186) became dispersed (Fig. 2D), suggesting that Vps60(128–186) folds into an ordered structure, coinciding with the structure determined below. This demonstrates that Vta1NTD binding stabilizes Vps60 helix conformation.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-25T07:46:57.204Z"}},{"start":140,"end":183,"reference_id":"23105107","reference_source":"pmid","reference_html":"Structural basis of molecular recognition between ESCRT-III-like protein Vps60 and AAA-ATPase regulator Vta1 in the multivesicular body pathway. <i> Yang Z, Vild C, Ju J, Zhang X, Liu J, Shen J, Zhao B, Lan W, Gong F, Liu M, Cao C, Xu Z. </i> J Biol Chem, 2012","date":"2025-06-16T17:04:53.879Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":20,"statements":[{"type":"Methods","text":"All NMR experiments were performed at 20 °C on a Varian Unity Inova 600 NMR spectrometer (with cryo-probe) equipped with triple resonances and pulsed-field gradients or on a Bruker AVANCE III 800-MHz NMR spectrometer (with cryo-probe) equipped with four channels and z axis pulsed-field gradient."}]}],"cross_refs":[{"db":"PDB","id":"2LUH"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q06263","operator":null,"partner_start":1,"partner_end":167}],"region_id":"DP04235r004","statement":[{"text":"The side chains of the residues located at Vps60(128–186) helix α4′, including Met-140′, Leu-141′, Leu-143′, Ile-144′, Leu-150′, Val-153′, and Leu-154′, are inserted into the groove of Vta1NTD helices 5 and 7. The Vps60(128–186) Ile-144′ side chain has a hydrophobic interaction with the Vta1NTD Ile-91, Leu-94, and Met-98 side chains, as Pro-171 functions in the complex Vps4A-CHMP6(168–179) (21). Besides the hydrophobic interactions, complementary salt bridges are also formed by two of the adjacent conserved Vps60(128–186) residues (Glu-149′ and Glu-152′) (Fig. 3B).","type":"Results"},{"text":"Moreover, the side chains of Vta1NTD Asn-95 and Asn-102 may form hydrogen bond interactions with the main chains of Met-140′ and Gln-146′, respectively. The second site on Vta1NTD binds mainly to the linker between α4′ and α5′ of Vps60(128–186) (Fig. 3C), most prominently to the side chains of Leu-163′ and Ile-166′. This site is also mainly hydrophobic and is lined by Tyr-153, Ile-156, and Tyr-157 and the aliphatic chains of Lys-149, Lys-152, and Lys-160, except that the side chain of Glu-162′ forms a complementary salt bridge with Lys-149.","type":"Results"},{"text":"The third binding site on Vta1 contacts Vps60(128–186) helix α5′ (Fig. 3D), including previously identified Vta1 residues important for Vps60 interaction, Trp-122 and Lys-152 (27, 29).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":128,"end":186,"reference_id":"23105107","reference_source":"pmid","reference_html":"Structural basis of molecular recognition between ESCRT-III-like protein Vps60 and AAA-ATPase regulator Vta1 in the multivesicular body pathway. <i> Yang Z, Vild C, Ju J, Zhang X, Liu J, Shen J, Zhao B, Lan W, Gong F, Liu M, Cao C, Xu Z. </i> J Biol Chem, 2012","date":"2024-07-22T18:55:08.389Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q06263","operator":null,"partner_start":1,"partner_end":167}],"region_id":"DP04235r005","statement":[{"text":"Binding affinities of Vps60(128–186) for wild-type and mutant Vta1NTD determined by isothermal titration calorimetry assay.","type":"Table"},{"text":"An affinity of Kd=0.7±0.1 μm was measured for the binding of the wild type protein constructs.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-25T07:46:45.044Z"}},{"start":128,"end":186,"reference_id":"23105107","reference_source":"pmid","reference_html":"Structural basis of molecular recognition between ESCRT-III-like protein Vps60 and AAA-ATPase regulator Vta1 in the multivesicular body pathway. <i> Yang Z, Vild C, Ju J, Zhang X, Liu J, Shen J, Zhao B, Lan W, Gong F, Liu M, Cao C, Xu Z. </i> J Biol Chem, 2012","date":"2024-07-22T18:57:48.745Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q06263","operator":null,"partner_start":1,"partner_end":167}],"region_id":"DP04235r006","statement":[{"text":"GST or GST-tagged Vps60(128–186) was used to pull down wild-type or mutant Vta1NTD as indicated.","type":"Figure"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-25T07:46:43.604Z"}}],"regions_counter":6,"released":"2024_12","sequence":"MNRIFGYGNKKSHDQLLQESNQSMNQAQQSLSNRISQLDTQIAQLNFQLQNIQKNLQRSNNKQPSLRKQALKILNKRKQLENMKDSLDSQSWSMTQAQLTNDNLQNTMITINALKQTNNAMKAQYGKINIDKLQDMQDEMLDLIEQGDELQEVLAMNNNSGELDDISDAELDAELDALAQEDFTLPTSENSLGNDMPSYLLGANAPPAFIDEEPNLDTEDKNKALESAQ","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.1965065502183406,"disorder_content":0.2576419213973799,"disprot_consensus":{"full":[{"start":128,"end":186,"type":"T"}],"Structural state":[{"start":128,"end":186,"type":"D"}],"Structural transition":[{"start":128,"end":186,"type":"T"}],"Molecular function":[{"start":128,"end":186,"type":"F"}]}},{"disprot_id":"DP04236","acc":"Q06263","creator":"rpancsa","date":"2024-07-22T19:03:11.820Z","features":{"pfam":[{"id":"PF04652","name":"Vta1 like","start":6,"end":165},{"id":"PF18097","name":"Vta1 C-terminal domain","start":293,"end":328}],"gene3D":[]},"genes":[{"name":{"value":"VTA1"},"olnNames":[{"value":"YLR181C"}]}],"length":330,"name":"Vacuolar protein sorting-associated protein VTA1","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":65,"end":75,"reference_id":"18194651","reference_source":"pmid","reference_html":"Structural basis of Vta1 function in the multivesicular body sorting pathway. <i> Xiao J, Xia H, Zhou J, Azmi IF, Davies BA, Katzmann DJ, Xu Z. </i> Dev Cell, 2008","date":"2024-07-22T19:05:10.393Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"2RKK"}],"region_id":"DP04236r001","statement":[{"text":"The entire structure can be visualized except for residues 65-75, which are presumed disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-25T08:07:02.505Z"}},{"start":65,"end":75,"reference_id":"23105107","reference_source":"pmid","reference_html":"Structural basis of molecular recognition between ESCRT-III-like protein Vps60 and AAA-ATPase regulator Vta1 in the multivesicular body pathway. <i> Yang Z, Vild C, Ju J, Zhang X, Liu J, Shen J, Zhao B, Lan W, Gong F, Liu M, Cao C, Xu Z. </i> J Biol Chem, 2012","date":"2024-07-22T19:10:24.433Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":20,"statements":[{"type":"Methods","text":"All NMR experiments were performed at 20 °C on a Varian Unity Inova 600 NMR spectrometer (with cryo-probe) equipped with triple resonances and pulsed-field gradients or on a Bruker AVANCE III 800-MHz NMR spectrometer (with cryo-probe) equipped with four channels and z axis pulsed-field gradient."}]}],"cross_refs":[{"db":"PDB","id":"2LUH"}],"region_id":"DP04236r002","statement":[{"text":"In the free Vta1NTD structure (29), the linker adopts largely a random coil structure, with only a one-turn α-helix occurring at residues 80–84. In particular, residues 65–75 appear to be disordered in the structure. Upon Vps60 binding, the linker becomes ordered. Residues 68–71 become a one-turn α-helix, and residues 73–84 adopt a longer helical structure (Fig. 2F). This conformational change might be caused by the interactions between helix α4 (positions 73–84) of Vta1NTD and a short N-terminal α-helix (positions 128–134) of Vps60(128–186) (Fig. 2G).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-25T08:07:23.405Z"}},{"start":65,"end":75,"reference_id":"23105107","reference_source":"pmid","reference_html":"Structural basis of molecular recognition between ESCRT-III-like protein Vps60 and AAA-ATPase regulator Vta1 in the multivesicular body pathway. <i> Yang Z, Vild C, Ju J, Zhang X, Liu J, Shen J, Zhao B, Lan W, Gong F, Liu M, Cao C, Xu Z. </i> J Biol Chem, 2012","date":"2024-07-22T19:11:58.387Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":20,"statements":[{"type":"Methods","text":"All NMR experiments were performed at 20 °C on a Varian Unity Inova 600 NMR spectrometer (with cryo-probe) equipped with triple resonances and pulsed-field gradients or on a Bruker AVANCE III 800-MHz NMR spectrometer (with cryo-probe) equipped with four channels and z axis pulsed-field gradient."}]}],"cross_refs":[{"db":"PDB","id":"2LUH"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q03390","operator":null,"partner_start":128,"partner_end":186}],"region_id":"DP04236r003","statement":[{"text":"In the free Vta1NTD structure (29), the linker adopts largely a random coil structure, with only a one-turn α-helix occurring at residues 80–84. In particular, residues 65–75 appear to be disordered in the structure. Upon Vps60 binding, the linker becomes ordered. Residues 68–71 become a one-turn α-helix, and residues 73–84 adopt a longer helical structure (Fig. 2F). This conformational change might be caused by the interactions between helix α4 (positions 73–84) of Vta1NTD and a short N-terminal α-helix (positions 128–134) of Vps60(128–186) (Fig. 2G).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-25T08:08:06.073Z"}},{"start":65,"end":75,"reference_id":"23105107","reference_source":"pmid","reference_html":"Structural basis of molecular recognition between ESCRT-III-like protein Vps60 and AAA-ATPase regulator Vta1 in the multivesicular body pathway. <i> Yang Z, Vild C, Ju J, Zhang X, Liu J, Shen J, Zhao B, Lan W, Gong F, Liu M, Cao C, Xu Z. </i> J Biol Chem, 2012","date":"2024-07-22T19:16:02.424Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q03390","operator":null,"partner_start":128,"partner_end":186}],"region_id":"DP04236r004","statement":[{"text":"Binding affinities of Vps60(128–186) for wild-type and mutant Vta1NTD determined by isothermal titration calorimetry assay.","type":"Table"},{"text":"An affinity of Kd=0.7±0.1 μm was measured for the binding of the wild type protein constructs.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-25T08:07:58.377Z"}},{"start":65,"end":75,"reference_id":"23105107","reference_source":"pmid","reference_html":"Structural basis of molecular recognition between ESCRT-III-like protein Vps60 and AAA-ATPase regulator Vta1 in the multivesicular body pathway. <i> Yang Z, Vild C, Ju J, Zhang X, Liu J, Shen J, Zhao B, Lan W, Gong F, Liu M, Cao C, Xu Z. </i> J Biol Chem, 2012","date":"2024-07-22T19:17:33.099Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q03390","operator":null,"partner_start":128,"partner_end":186}],"region_id":"DP04236r005","statement":[{"text":"GST or GST-tagged Vps60(128–186) was used to pull down wild-type or mutant Vta1NTD as indicated.","type":"Figure"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-25T08:07:31.491Z"}}],"regions_counter":5,"released":"2024_12","sequence":"MASNAARVVATAKDFDKVGLGIIGYYLQLYAVELILSEEDRSQEMTALATELLDTIEAFKKEIGGESEAEDSDKSLHVMNTLIHDQEKAKIYMLNFTMSLYNEKLKQLKDGPWDVMLKRSLWCCIDLFSCILHLWKENISETSTNSLQKRIKYCKIYLSKLAKGEIGSSDEKTLDYADFADDSEEIKDEDVDHQTSDLENNNNDKVEGLAPKDQTTSYEPVDEVPEFIDDADSVNEEEQTVDKNEDAITKDEQQVVKKEVDLTRPSAPSEPAAAEHKSYTKDELTKIMDRASKIEQIQKLAKYAISALNYEDLPTAKDELTKALDLLNSI","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.3181818181818182,"disorder_content":0.03333333333333333,"disprot_consensus":{"full":[{"start":65,"end":75,"type":"T"}],"Structural state":[{"start":65,"end":75,"type":"D"}],"Structural transition":[{"start":65,"end":75,"type":"T"}],"Molecular function":[{"start":65,"end":75,"type":"F"}]}},{"disprot_id":"DP04237","acc":"Q8N5K1","creator":"rpancsa","date":"2024-07-22T20:39:17.935Z","features":{"pfam":[{"id":"PF09360","name":"Iron-binding zinc finger CDGSH type","start":79,"end":115},{"id":"PF10660","name":"Iron-containing outer mitochondrial membrane protein N-terminus","start":4,"end":66}],"gene3D":[]},"genes":[{"name":{"value":"CISD2"},"synonyms":[{"value":"CDGSH2"},{"value":"ERIS"},{"value":"ZCD2"}]}],"length":135,"name":"CDGSH iron-sulfur domain-containing protein 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":57,"end":72,"reference_id":"19580816","reference_source":"pmid","reference_html":"Crystal structure of Miner1: The redox-active 2Fe-2S protein causative in Wolfram Syndrome 2. <i> Conlan AR, Axelrod HL, Cohen AE, Abresch EC, Zuris J, Yee D, Nechushtai R, Jennings PA, Paddock ML. </i> J Mol Biol, 2009","date":"2024-07-22T20:41:50.608Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"3FNV"}],"region_id":"DP04237r001","statement":[{"text":"Fifteen amino acids at the N-termini are disordered and not resolved in the electron density.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-25T07:57:44.905Z"}}],"regions_counter":1,"released":"2024_12","sequence":"MVLESVARIVKVQLPAYLKRLPVPESITGFARLTVSEWLRLLPFLGVLALLGYLAVRPFLPKKKQQKDSLINLKIQKENPKVVNEINIEDLCLTKAAYCRCWRSKTFPACDGSHNKHNELTGDNVGPLILKKKEV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0,"disorder_content":0.11851851851851852,"disprot_consensus":{"full":[{"start":57,"end":72,"type":"D"}],"Structural state":[{"start":57,"end":72,"type":"D"}]}},{"disprot_id":"DP04239","acc":"P53355","creator":"vnugnes","date":"2024-08-29T15:11:00.554Z","features":{"pfam":[{"id":"PF00023","name":"Ankyrin repeat","start":379,"end":410},{"id":"PF00069","name":"Protein kinase domain","start":13,"end":275},{"id":"PF00531","name":"Death domain","start":1311,"end":1392},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":430,"end":508},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":570,"end":637},{"id":"PF13637","name":"Ankyrin repeats (many copies)","start":525,"end":564}],"gene3D":[]},"genes":[{"name":{"value":"DAPK1"},"synonyms":[{"value":"DAPK"}]}],"length":1430,"name":"Death-associated protein kinase 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":303,"end":334,"reference_id":"24440081","reference_source":"pmid","reference_html":"A PEF/Y substrate recognition and signature motif plays a critical role in DAPK-related kinase activity. <i> Temmerman K, de Diego I, Pogenberg V, Simon B, Jonko W, Li X, Wilmanns M. </i> Chem Biol, 2014","date":"2024-08-29T15:14:03.450Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"2W4K"}],"region_id":"DP04239r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","statements":[{"type":"Results","text":"To decipher a possible structural role for the DAPK1 ARD as a pseudosubstrate, we determined a complementary crystal structure of the same DAPK1 construct (residues 1–334, abbreviated as DAPK1 throughout this paper) in the presence of Mg2+/ADP and in the absence of CaM (Figure 1\nA; Table 1; Figure S1 available online)."}],"entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","statements":[{"type":"Results","text":"To decipher a possible structural role for the DAPK1 ARD as a pseudosubstrate, we determined a complementary crystal structure of the same DAPK1 construct (residues 1–334, abbreviated as DAPK1 throughout this paper) in the presence of Mg2+/ADP and in the absence of CaM (Figure 1\nA; Table 1; Figure S1 available online)."}],"entry_name":"ADP"}],"statement":[{"text":"In contrast to the structure of the DAPK1-CaM complex (de Diego et al., 2010), part of the ARD beyond the Ser308 phosphorylation site (residues 303–334) remained invisible, indicating a transient binding of Ser308 to the CD during autophosphorylation (Figure S2).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T15:54:39.608Z"}},{"start":303,"end":320,"reference_id":"20103772","reference_source":"pmid","reference_html":"Molecular basis of the death-associated protein kinase-calcium/calmodulin regulator complex. <i> de Diego I, Kuper J, Bakalova N, Kursula P, Wilmanns M. </i> Sci Signal, 2010","date":"2024-08-29T15:53:58.060Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"2X0G"}],"region_id":"DP04239r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0DP23"}],"statement":[{"text":"In the DAPK(1–334)-CaM complex, the C-terminal portion of the ARD (residues 293 to 320) forms a long seven-turn helix.","type":"Results"},{"text":"In contrast to the apo-structure, the PDB complex structure shows the complete ARD (residues 278–320) to be folded into a α helix, which indicates that the 303-320 region gains order.","type":"Curator statement"}],"states_connection":[{"source":"DP04239r001","target":"DP04239r004"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T15:54:41.621Z"}},{"start":305,"end":312,"reference_id":"20103772","reference_source":"pmid","reference_html":"Molecular basis of the death-associated protein kinase-calcium/calmodulin regulator complex. <i> de Diego I, Kuper J, Bakalova N, Kursula P, Wilmanns M. </i> Sci Signal, 2010","date":"2024-08-29T16:39:25.076Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005516","term_name":"calmodulin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"2X0G"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P0DP23","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04239r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"In addition, several ARD residues (Trp305, Ser308, Val309, Ile312) project into well-formed pockets of the CaM C-terminal lobe (Figs. 2A, 3A, and fig. S2). Of these, the deepest and largest cavity is provided by as many as 10 different CaM residues for Trp305. The only side chain–specific interaction involves the DAPK autophosphorylation target Ser308 and CaM residue Glu114.","type":"Results"}],"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T15:55:00.481Z"}},{"start":303,"end":320,"reference_id":"20103772","reference_source":"pmid","reference_html":"Molecular basis of the death-associated protein kinase-calcium/calmodulin regulator complex. <i> de Diego I, Kuper J, Bakalova N, Kursula P, Wilmanns M. </i> Sci Signal, 2010","date":"2024-08-29T15:54:12.306Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"2X0G"}],"region_id":"DP04239r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0DP23"}],"statement":[{"text":"In the DAPK(1–334)-CaM complex, the C-terminal portion of the ARD (residues 293 to 320) forms a long seven-turn helix.","type":"Results"},{"text":"In contrast to the apo-structure, the PDB complex structure shows the complete ARD (residues 278–320) to be folded into a α helix, which indicates that the 303-320 region gains order.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T15:54:34.736Z"}},{"start":302,"end":320,"reference_id":"20103772","reference_source":"pmid","reference_html":"Molecular basis of the death-associated protein kinase-calcium/calmodulin regulator complex. <i> de Diego I, Kuper J, Bakalova N, Kursula P, Wilmanns M. </i> Sci Signal, 2010","date":"2024-08-29T15:58:21.096Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005516","term_name":"calmodulin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P0DP23","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04239r005","statement":[{"text":"We characterized the interaction of a synthetic DAPK(ARD) peptide (residues 302 to 320) with CaM by structural and biochemical analysis to determine potential differences in its CaM binding with that of the DAPK(1–334) protein (Fig. 1B, fig. S3, and table S1); the DAPK(ARD) (302–320) peptide-bound CaM with a dissociation constant of 24 nM, forming a high-affinity complex.","type":"Results"}],"term_comment":"","term_def":"\"Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states.\" [GOC:krc]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T15:54:54.906Z"}},{"start":306,"end":310,"reference_id":"20103772","reference_source":"pmid","reference_html":"Molecular basis of the death-associated protein kinase-calcium/calmodulin regulator complex. <i> de Diego I, Kuper J, Bakalova N, Kursula P, Wilmanns M. </i> Sci Signal, 2010","date":"2024-08-29T16:27:51.906Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04239r006","statement":[{"text":"Whereas Western blot analysis with phosphospecific antibodies revealed only slight Ser308 phosphorylation of DAPK coexpressed with CaM after adenosine triphosphate (ATP) incubation, we found strong Ser308 phosphorylation of the apoenzyme (Fig. 5C).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T15:54:53.374Z"}},{"start":306,"end":310,"reference_id":"20103772","reference_source":"pmid","reference_html":"Molecular basis of the death-associated protein kinase-calcium/calmodulin regulator complex. <i> de Diego I, Kuper J, Bakalova N, Kursula P, Wilmanns M. </i> Sci Signal, 2010","date":"2024-08-29T16:33:45.683Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0033673","term_name":"negative regulation of kinase activity","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007687","ec_ontology":"ECO","ec_name":"protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IDA","region_id":"DP04239r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15422","statements":[{"type":"Methods","text":"A synthetic peptide KKRPQRRYSNVF, previously identified as a DAPK consensus substrate (10), was used as phosphorylation substrate. Saturating concentrations of each of the two substrates were 2 mM (ATP) and 600 μM (peptide), with DAPK at a concentration range of 125 to 250 nM."}],"entry_name":"ATP"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"A synthetic peptide KKRPQRRYSNVF, previously identified as a DAPK consensus substrate (10), was used as phosphorylation substrate. Saturating concentrations of each of the two substrates were 2 mM (ATP) and 600 μM (peptide), with DAPK at a concentration range of 125 to 250 nM."}]}],"statement":[{"text":"That is, DAPK in complex with CaM, which prevented Ser308 phosphorylation, was as active as the constitutively active DAPK(CD) fragment, whereas the apo version of DAPK(1–334) showed little catalytic activity (Fig. 5B and Table 3).","type":"Results"},{"text":"Autophosphorylation at Ser-308 inhibits its catalytic activity.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T15:54:48.889Z"}},{"start":306,"end":310,"reference_id":"20103772","reference_source":"pmid","reference_html":"Molecular basis of the death-associated protein kinase-calcium/calmodulin regulator complex. <i> de Diego I, Kuper J, Bakalova N, Kursula P, Wilmanns M. </i> Sci Signal, 2010","date":"2024-08-29T16:34:15.305Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000059","term_name":"self-inhibition","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007687","ec_ontology":"ECO","ec_name":"protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04239r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15422","statements":[{"type":"Methods","text":"A synthetic peptide KKRPQRRYSNVF, previously identified as a DAPK consensus substrate (10), was used as phosphorylation substrate. Saturating concentrations of each of the two substrates were 2 mM (ATP) and 600 μM (peptide), with DAPK at a concentration range of 125 to 250 nM."}],"entry_name":"ATP"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"A synthetic peptide KKRPQRRYSNVF, previously identified as a DAPK consensus substrate (10), was used as phosphorylation substrate. Saturating concentrations of each of the two substrates were 2 mM (ATP) and 600 μM (peptide), with DAPK at a concentration range of 125 to 250 nM."}]}],"statement":[{"text":"That is, DAPK in complex with CaM, which prevented Ser308 phosphorylation, was as active as the constitutively active DAPK(CD) fragment, whereas the apo version of DAPK(1–334) showed little catalytic activity (Fig. 5B and Table 3).","type":"Results"},{"text":"Autophosphorylation at Ser-308 inhibits its catalytic activity.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T15:54:46.886Z"}}],"regions_counter":8,"released":"2024_12","sequence":"MTVFRQENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSREDIEREVSILKEIQHPNVITLHEVYENKTDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDFGLAHKIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSNTSALAKDFIRRLLVKDPKKRMTIQDSLQHPWIKPKDTQQALSRKASAVNMEKFKKFAARKKWKQSVRLISLCQRLSRSFLSRSNMSVARSDDTLDEEDSFVMKAIIHAINDDNVPGLQHLLGSLSNYDVNQPNKHGTPPLLIAAGCGNIQILQLLIKRGSRIDVQDKGGSNAVYWAARHGHVDTLKFLSENKCPLDVKDKSGEMALHVAARYGHADVAQLLCSFGSNPNIQDKEEETPLHCAAWHGYYSVAKALCEAGCNVNIKNREGETPLLTASARGYHDIVECLAEHGADLNACDKDGHIALHLAVRRCQMEVIKTLLSQGCFVDYQDRHGNTPLHVACKDGNMPIVVALCEANCNLDISNKYGRTPLHLAANNGILDVVRYLCLMGASVEALTTDGKTAEDLARSEQHEHVAGLLARLRKDTHRGLFIQQLRPTQNLQPRIKLKLFGHSGSGKTTLVESLKCGLLRSFFRRRRPRLSSTNSSRFPPSPLASKPTVSVSINNLYPGCENVSVRSRSMMFEPGLTKGMLEVFVAPTHHPHCSADDQSTKAIDIQNAYLNGVGDFSVWEFSGNPVYFCCYDYFAANDPTSIHVVVFSLEEPYEIQLNQVIFWLSFLKSLVPVEEPIAFGGKLKNPLQVVLVATHADIMNVPRPAGGEFGYDKDTSLLKEIRNRFGNDLHISNKLFVLDAGASGSKDMKVLRNHLQEIRSQIVSVCPPMTHLCEKIISTLPSWRKLNGPNQLMSLQQFVYDVQDQLNPLASEEDLRRIAQQLHSTGEINIMQSETVQDVLLLDPRWLCTNVLGKLLSVETPRALHHYRGRYTVEDIQRLVPDSDVEELLQILDAMDICARDLSSGTMVDVPALIKTDNLHRSWADEEDEVMVYGGVRIVPVEHLTPFPCGIFHKVQVNLCRWIHQQSTEGDADIRLWVNGCKLANRGAELLVLLVNHGQGIEVQVRGLETEKIKCCLLLDSVCSTIENVMATTLPGLLTVKHYLSPQQLREHHEPVMIYQPRDFFRAQTLKETSLTNTMGGYKESFSSIMCFGCHDVYSQASLGMDIHASDLNLLTRRKLSRLLDPPDPLGKDWCLLAMNLGLPDLVAKYNTSNGAPKDFLPSPLHALLREWTTYPESTVGTLMSKLRELGRRDAADFLLKASSVFKINLDGNGQEAYASSCNSGTSYNSISSVVSR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.1006993006993007,"dataset":["Autophagy-related proteins","Age-related disorders proteins","Stress response proteins"],"disorder_content":0.022377622377622378,"disprot_consensus":{"full":[{"start":302,"end":302,"type":"F"},{"start":303,"end":320,"type":"T"},{"start":321,"end":334,"type":"D"}],"Structural state":[{"start":303,"end":334,"type":"D"}],"Structural transition":[{"start":303,"end":320,"type":"T"}],"Molecular function":[{"start":302,"end":320,"type":"F"}],"Disorder function":[{"start":306,"end":310,"type":"F"}],"Biological process":[{"start":306,"end":310,"type":"F"}]}},{"disprot_id":"DP04240","acc":"Q8GXC2","creator":"vnugnes","date":"2024-09-02T15:01:42.412Z","features":{"pfam":[{"id":"PF00249","name":"Myb-like DNA-binding domain","start":233,"end":284},{"id":"PF14379","name":"MYB-CC type transfactor, LHEQLE motif","start":317,"end":361}],"gene3D":[]},"genes":[{"name":{"value":"PHL4","evidences":[{"code":"ECO:0000305"}]},"orfNames":[{"value":"F11A3.5","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAD21748.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD21748.1"}}]}],"olnNames":[{"value":"At2g20400","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT2G20400","url":""}}]}]}],"length":397,"name":"Myb family transcription factor PHL4","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":1,"end":227,"reference_id":"39005418","reference_source":"pmid","reference_html":"The Potent PHL4 Transcription Factor Effector Domain Contains Significant Disorder. <i> Fonda BD, Murray DT. </i> bioRxiv, 2024","date":"2024-09-02T15:07:32.480Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04240r001","statement":[{"text":"Figure 1d shows the CD spectra of PHL4effector and PHL4FL. Analysis of the spectra using BeStSel (Micsonai et al., 2022) with the “Disordered-Ordered” classification is summarized in Figure 1e. The prediction for the PHL4effector spectrum is consistent with a disordered protein, while the prediction for PHL4FL is consistent with a mixture of ordered secondary structure motifs accounting for approximately half of the protein.","type":"Results"},{"text":"CD spectra in Figure 1 shows this region is intrinsically disordered because of its large negative ellipticity at 200 nm. PHL4effector is used by the authors to refer to the first 227 N-terminal residues of this protein.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T15:57:37.308Z"}},{"start":1,"end":227,"reference_id":"39005418","reference_source":"pmid","reference_html":"The Potent PHL4 Transcription Factor Effector Domain Contains Significant Disorder. <i> Fonda BD, Murray DT. </i> bioRxiv, 2024","date":"2024-09-02T15:23:06.796Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04240r002","statement":[{"text":"For PHL4effector, the Rh measured using both SEC and diffusion NMR is consistent with monomeric, unfolded protein.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T15:57:31.401Z"}},{"start":1,"end":227,"reference_id":"39005418","reference_source":"pmid","reference_html":"The Potent PHL4 Transcription Factor Effector Domain Contains Significant Disorder. <i> Fonda BD, Murray DT. </i> bioRxiv, 2024","date":"2024-09-02T15:16:46.918Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04240r003","statement":[{"text":"For PHL4effector, the Rh measured using both SEC and diffusion NMR is consistent with monomeric, unfolded protein.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T15:55:48.193Z"}},{"start":1,"end":227,"reference_id":"39005418","reference_source":"pmid","reference_html":"The Potent PHL4 Transcription Factor Effector Domain Contains Significant Disorder. <i> Fonda BD, Murray DT. </i> bioRxiv, 2024","date":"2024-09-02T15:24:54.257Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"BMRB","id":"52525"},{"db":"BMRB","id":"52524"}],"region_id":"DP04240r004","statement":[{"text":"Large positive values over several adjacent residues indicates an a-helical structure, while large negative values for neighboring residues are consistent with a β-strand structure (Wishart, 2011). These plots show that the majority of the secondary chemical shift magnitudes are less than 2, a commonly used cutoff for well-defined structure (Wishart, 2011). The secondary chemical shifts are therefore consistent with the assigned residues in both PHL4FL and PHL4effector lacking well-defined secondary structure.","type":"Results"},{"text":"Overwhelmingly, random coil is the dominant prediction for PHL4effector, which is consistent with our interpretation for the measured Rh, CD spectra, and Trp fluorescence assays.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T15:55:32.535Z"}},{"start":369,"end":397,"reference_id":"39005418","reference_source":"pmid","reference_html":"The Potent PHL4 Transcription Factor Effector Domain Contains Significant Disorder. <i> Fonda BD, Murray DT. </i> bioRxiv, 2024","date":"2024-09-02T15:26:49.576Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"BMRB","id":"52524"}],"region_id":"DP04240r005","statement":[{"text":"The secondary chemical shifts are therefore consistent with the assigned residues in both PHL4FL and PHL4effector lacking well-defined secondary structure.","type":"Results"},{"text":"At the C-terminus of PHL4FL, in agreement with the secondary chemical shift analysis, the TALOS-N predictions predict a random coil arrangement.","type":"Results"},{"text":"The tetrameric state upper bound is near the value calculated for a completely unfolded PHL4FL, which is compatible with the domain structure of PHL4FL in Figure 1a showing the structured coiled-coil and helix-turn-helix domains occupying only ~28% of the PHL4FL sequence and our solution NMR measurements showing the N- and C-termini are disordered (vide infra).","type":"Results"},{"text":"(a) A domain map for PHL4. HTH DBD is the homology predicted helix-turn-helix DNA binding domain, CC is the homology predicted coiled-coil domain, and residues 1–227 and 369–397 are to be shown in this work as primarily disordered.","type":"Figure"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T15:55:28.155Z"}}],"regions_counter":5,"released":"2024_12","sequence":"MIPNDDDDANSMKNYPLNDDDANSMKNYPLNDDDANSMENYPLRSIPTELSHTCSLIPPSLPNPSEAAADMSFNSELNQIMARPCDMLPANGGAVGHNPFLEPGFNCPETTDWIPSPLPHIYFPSGSPNLIMEDGVIDEIHKQSDLPLWYDDLITTDEDPLMSSILGDLLLDTNFNSASKVQQPSMQSQIQQPQAVLQQPSSCVELRPLDRTVSSNSNNNSNSNNAAAAAKGRMRWTPELHEVFVDAVNQLGGSNEATPKGVLKHMKVEGLTIFHVKSHLQKYRTAKYIPVPSEGSPEARLTPLEQITSDDTKRGIDITETLRIQMEHQKKLHEQLESLRTMQLRIEEQGKALLMMIEKQNMGFGGPEQGEKTSAKTPENGSEESESPRPKRPRNEE","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"alphafold_very_low_content":0.48614609571788414,"disorder_content":0.6448362720403022,"disprot_consensus":{"full":[{"start":1,"end":227,"type":"D"},{"start":369,"end":397,"type":"D"}],"Structural state":[{"start":1,"end":227,"type":"D"},{"start":369,"end":397,"type":"D"}]}},{"disprot_id":"DP04241","acc":"P15146-3","creator":"vnugnes","date":"2024-09-02T16:02:49.976Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"Map2"},"synonyms":[{"value":"Mtap2"}]}],"length":467,"name":"Isoform 3 of Microtubule-associated protein 2","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions":[{"start":1,"end":467,"reference_id":"23877929","reference_source":"pmid","reference_html":"Efficient protocol for backbone and side-chain assignments of large, intrinsically disordered proteins: transient secondary structure analysis of 49.2 kDa microtubule associated protein 2c. <i> Nováček J, Janda L, Dopitová R, Žídek L, Sklenář V. </i> J Biomol NMR, 2013","date":"2024-09-02T16:08:42.670Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04241r001","statement":[{"text":"The MAP2c is a 49.2 kDa intrinsically disordered protein.","type":"Introduction"},{"text":"Figure 3 shows the backbone amide resonances of this protein fall between 8.0 and 8.5 p.p.m. The lack of chemical shift dispersion reflect the intrinsic mobility of this protein.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:16:38.871Z"}},{"start":1,"end":159,"reference_id":"39002671","reference_source":"pmid","reference_html":"Structural basis of binding the unique N-terminal domain of microtubule-associated protein 2c to proteins regulating kinases of signaling pathways. <i> Bartošík V, Plucarová J, Laníková A, Janáčková Z, Padrta P, Jansen S, Vařečka V, Gruber T, Feller SM, Žídek L. </i> J Biol Chem, 2024","date":"2024-09-02T16:35:34.263Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019901","term_name":"protein kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P13861","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04241r002","statement":[{"text":"Isothermal titration calorimetry (ITC) of MAP2c and hexahistidine-tagged N-terminal fragment of MAP2c containing residues 1 to 159 (N-MAP2c) titrated by RIIα-PKA and RIIDD2 provided steep-binding isotherms corresponding to the dissociation constants KD in a lower nanomolar range. Similar binding isotherms for MAP2c and N-MAP2c show that the main interaction site of RIIα-PKA is located in the N-terminal part of MAP2c. ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:21:39.360Z"}},{"start":80,"end":118,"reference_id":"39002671","reference_source":"pmid","reference_html":"Structural basis of binding the unique N-terminal domain of microtubule-associated protein 2c to proteins regulating kinases of signaling pathways. <i> Bartošík V, Plucarová J, Laníková A, Janáčková Z, Padrta P, Jansen S, Vařečka V, Gruber T, Feller SM, Žídek L. </i> J Biol Chem, 2024","date":"2024-09-02T16:37:59.762Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019901","term_name":"protein kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P13861","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04241r003","statement":[{"text":"The complex with RIIα-PKA exhibited a dramatic decrease in the same region of MAP2c, but a substantial broadening was also observed in other regions, especially in the proline-rich region P2 (residues Ser280–Leu300) and in the microtubule-binding repeat 3 (Val333–Arg363).","type":"Results"},{"text":"In summary, we confirmed that MAP2c binds RIIα-PKA via the residues Thr80–Asp118, in agreement with the literature (24). Interactions with other regions of MAP2c were also observed, but their contribution to the overall binding was weak.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:17:16.353Z"}},{"start":80,"end":118,"reference_id":"39002671","reference_source":"pmid","reference_html":"Structural basis of binding the unique N-terminal domain of microtubule-associated protein 2c to proteins regulating kinases of signaling pathways. <i> Bartošík V, Plucarová J, Laníková A, Janáčková Z, Padrta P, Jansen S, Vařečka V, Gruber T, Feller SM, Žídek L. </i> J Biol Chem, 2024","date":"2024-09-02T16:45:14.575Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"region_id":"DP04241r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P13861"}],"statement":[{"text":"NMR peak broadening was used to map the residues of MAP2c influenced by the interactions with RIIα-PKA. Peaks of intrinsically disordered residues of MAP2c are sharp due to its fast motions in spite of its large size. The MAP2c residues interacting with RIIα-PKA become a part of a large, well ordered complex and their peaks broaden dramatically.","type":"Results"},{"text":"In summary, we confirmed that MAP2c binds RIIα-PKA via the residues Thr80–Asp118, in agreement with the literature (24). Interactions with other regions of MAP2c were also observed, but their contribution to the overall binding was weak.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:16:44.861Z"}},{"start":65,"end":69,"reference_id":"39002671","reference_source":"pmid","reference_html":"Structural basis of binding the unique N-terminal domain of microtubule-associated protein 2c to proteins regulating kinases of signaling pathways. <i> Bartošík V, Plucarová J, Laníková A, Janáčková Z, Padrta P, Jansen S, Vařečka V, Gruber T, Feller SM, Žídek L. </i> J Biol Chem, 2024","date":"2024-09-02T17:06:25.569Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04241r005","statement":[{"text":"We first confirmed a residue-specific phosphorylation of MAP2c on Tyr67 by tyrosine kinase Fyn (Fig. S4 in Supporting Information).","type":"Results"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:17:10.331Z"}},{"start":288,"end":294,"reference_id":"39002671","reference_source":"pmid","reference_html":"Structural basis of binding the unique N-terminal domain of microtubule-associated protein 2c to proteins regulating kinases of signaling pathways. <i> Bartošík V, Plucarová J, Laníková A, Janáčková Z, Padrta P, Jansen S, Vařečka V, Gruber T, Feller SM, Žídek L. </i> J Biol Chem, 2024","date":"2024-09-02T17:09:21.995Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P62993","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04241r006","statement":[{"text":"Presence of Grb2 reduced peak heights of unphosphorylated MAP2c in several regions (black circles in Fig. 6A). The most notable peak broadening was observed for the class I canonical SH3-binding site 288RTPPKSP294. The peak height decreased also in the proline-rich regions (residues 230–300) with multiple minimal SH3-binding PXXP motifs. Even stronger peak broadening was observed in a region between residues 185 and 198, rich in prolines, but lacking the PXXP motif. ","type":"Results"},{"text":"In addition to the class I SH3-binding motif 288RTPPKSP294, Grb2 interacts with residues 185 to 198 in the variable central region of MAP2c (cf. Fig. 6).","type":"Discussion"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:17:04.614Z"}},{"start":185,"end":198,"reference_id":"39002671","reference_source":"pmid","reference_html":"Structural basis of binding the unique N-terminal domain of microtubule-associated protein 2c to proteins regulating kinases of signaling pathways. <i> Bartošík V, Plucarová J, Laníková A, Janáčková Z, Padrta P, Jansen S, Vařečka V, Gruber T, Feller SM, Žídek L. </i> J Biol Chem, 2024","date":"2024-09-02T17:06:05.448Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P62993","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04241r007","statement":[{"text":"Presence of Grb2 reduced peak heights of unphosphorylated MAP2c in several regions (black circles in Fig. 6A). The most notable peak broadening was observed for the class I canonical SH3-binding site 288RTPPKSP294. The peak height decreased also in the proline-rich regions (residues 230–300) with multiple minimal SH3-binding PXXP motifs. Even stronger peak broadening was observed in a region between residues 185 and 198, rich in prolines, but lacking the PXXP motif. ","type":"Results"},{"text":"In addition to the class I SH3-binding motif 288RTPPKSP294, Grb2 interacts with residues 185 to 198 in the variable central region of MAP2c (cf. Fig. 6).","type":"Discussion"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:16:58.403Z"}},{"start":60,"end":70,"reference_id":"39002671","reference_source":"pmid","reference_html":"Structural basis of binding the unique N-terminal domain of microtubule-associated protein 2c to proteins regulating kinases of signaling pathways. <i> Bartošík V, Plucarová J, Laníková A, Janáčková Z, Padrta P, Jansen S, Vařečka V, Gruber T, Feller SM, Žídek L. </i> J Biol Chem, 2024","date":"2024-09-02T17:09:43.940Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":67,"end":67,"position":"Specific residue"},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P62993","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04241r008","statement":[{"text":"Additional peak broadening of Fyn-phosphorylated MAP2c (compared to unphosphorylated MAP2c) in the presence of Grb2 revealed a phosphorylation-dependent binding site around pTyr67. The peak height was reduced below 50% for residues 60 to 70 (forest green circles in Fig. 6A).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:16:56.822Z"}},{"start":60,"end":70,"reference_id":"39002671","reference_source":"pmid","reference_html":"Structural basis of binding the unique N-terminal domain of microtubule-associated protein 2c to proteins regulating kinases of signaling pathways. <i> Bartošík V, Plucarová J, Laníková A, Janáčková Z, Padrta P, Jansen S, Vařečka V, Gruber T, Feller SM, Žídek L. </i> J Biol Chem, 2024","date":"2024-09-02T17:10:22.602Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042169","term_name":"SH2 domain binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":67,"end":67,"position":"Specific residue"},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P62993","operator":null,"partner_start":57,"partner_end":158}],"region_id":"DP04241r009","statement":[{"text":"Additional peak broadening of Fyn-phosphorylated MAP2c (compared to unphosphorylated MAP2c) in the presence of Grb2 revealed a phosphorylation-dependent binding site around pTyr67. The peak height was reduced below 50% for residues 60 to 70 (forest green circles in Fig. 6A).","type":"Results"},{"text":"Broadening of the peak of pTyr67 below the detection limit showed that pTyr67 became a part of a large, well-ordered complex in the presence of Grb2. The same experiment was performed with Fyn-phosphorylated MAP2c and Grb2-SH2. Peak broadening was observed in the same region of the MAP2c sequence as with full-length Grb2 (pale green circles in Fig. 6A), confirming that pTyr67 interacts with the SH2 domain.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a SH2 domain (Src homology 2) of a protein, a protein domain of about 100 amino-acid residues and belonging to the alpha + beta domain class.\" [GOC:go_curators, Pfam:PF00017]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:16:46.583Z"}},{"start":60,"end":70,"reference_id":"39002671","reference_source":"pmid","reference_html":"Structural basis of binding the unique N-terminal domain of microtubule-associated protein 2c to proteins regulating kinases of signaling pathways. <i> Bartošík V, Plucarová J, Laníková A, Janáčková Z, Padrta P, Jansen S, Vařečka V, Gruber T, Feller SM, Žídek L. </i> J Biol Chem, 2024","date":"2024-09-02T17:10:43.645Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":67,"end":67,"position":"Specific residue"},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"region_id":"DP04241r010","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62993"}],"statement":[{"text":"Additional peak broadening of Fyn-phosphorylated MAP2c (compared to unphosphorylated MAP2c) in the presence of Grb2 revealed a phosphorylation-dependent binding site around pTyr67. The peak height was reduced below 50% for residues 60 to 70 (forest green circles in Fig. 6A).","type":"Results"},{"text":"Broadening of the peak of pTyr67 below the detection limit showed that pTyr67 became a part of a large, well-ordered complex in the presence of Grb2. The same experiment was performed with Fyn-phosphorylated MAP2c and Grb2-SH2. Peak broadening was observed in the same region of the MAP2c sequence as with full-length Grb2 (pale green circles in Fig. 6A), confirming that pTyr67 interacts with the SH2 domain.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:16:40.472Z"}}],"regions_counter":10,"released":"2024_12","sequence":"MADERKDEGKAPHWTSASLTEAAAHPHSPEMKDQGGSGEGLSRSANGFPYREEEEGAFGEHGSQGTYSDTKENGINGELTSADRETAEEVSARIVQVVTAEAVAVLKGEQEKEAQHKDQPAALPLAAEETVNLPPSPPPSPASEQTAALEEATSGESAQAPSAFKQAKDKVTDGITKSPEKRSSLPRPSSILPPRRGVSGDREENSFSLNSSISSARRTTRSEPIRRAGKSGTSTPTTPGSTAITPGTPPSYSSRTPGTPGTPSYPRTPGTPKSGILVPSEKKVAIIRTPPKSPATPKQLRLINQPLPDLKNVKSKIGSTDNIKYQPKGGQVQIVTKKIDLSHVTSKCGSLKNIRHRPGGGRVKIESVKLDFKEKAQAKVGSLDNAHHVPGGGNVKIDSQKLNFREHAKARVDHGAEIITQSPSRSSVASPRRLSNVSSSGSINLLESPQLATLAEDVTAALAKQGL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":59,"type":"D"},{"start":60,"end":70,"type":"T"},{"start":71,"end":79,"type":"D"},{"start":80,"end":118,"type":"T"},{"start":119,"end":467,"type":"D"}],"Structural state":[{"start":1,"end":467,"type":"D"}],"Molecular function":[{"start":1,"end":159,"type":"F"},{"start":185,"end":198,"type":"F"},{"start":288,"end":294,"type":"F"}],"Structural transition":[{"start":60,"end":70,"type":"T"},{"start":80,"end":118,"type":"T"}],"Disorder function":[{"start":65,"end":69,"type":"F"}]}},{"disprot_id":"DP04242","acc":"P45973","creator":"vnugnes","date":"2024-09-02T17:31:07.765Z","features":{"pfam":[{"id":"PF00385","name":"Chromo (CHRromatin Organisation MOdifier) domain","start":20,"end":69},{"id":"PF01393","name":"Chromo shadow domain","start":117,"end":175}],"gene3D":[]},"genes":[{"name":{"value":"CBX5"},"synonyms":[{"value":"HP1A"}]}],"length":191,"name":"Chromobox protein homolog 5","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":21,"reference_id":"38895997","reference_source":"pmid","reference_html":"Conformational diversity of human HP1α. <i> Ukmar-Godec T, Yu T, de Opakua AI, Pantoja CF, Munari F, Zweckstetter M. </i> Protein Sci, 2024","date":"2024-09-02T17:35:34.254Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04242r001","statement":[{"text":"Secondary structure propensities predicted by TALOS N+ are in agreement with the high‐resolution structures of the individual CD and CSD, and suggested the presence of predominantly random coil conformation in the NTE, the HR, and the CTE (Figure 1c).","type":"Results"},{"text":"(a) Schematic of Hp1 dimer containing the ordered CD and CSD and disordered NTE, HR, and CTE.","type":"Figure"},{"text":"In Figure 1 authors define NTE as the 1-21 region, HR as the hinge region 79-123, and CTE as 178-191 C-terminal region. ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:22:48.409Z"}},{"start":79,"end":123,"reference_id":"38895997","reference_source":"pmid","reference_html":"Conformational diversity of human HP1α. <i> Ukmar-Godec T, Yu T, de Opakua AI, Pantoja CF, Munari F, Zweckstetter M. </i> Protein Sci, 2024","date":"2024-09-02T17:35:46.381Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04242r002","statement":[{"text":"Secondary structure propensities predicted by TALOS N+ are in agreement with the high‐resolution structures of the individual CD and CSD, and suggested the presence of predominantly random coil conformation in the NTE, the HR, and the CTE (Figure 1c).","type":"Results"},{"text":"(a) Schematic of Hp1 dimer containing the ordered CD and CSD and disordered NTE, HR, and CTE.","type":"Figure"},{"text":"In Figure 1 authors define NTE as the 1-21 region, HR as the hinge region 79-123, and CTE as 178-191 C-terminal region. ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:22:43.330Z"}},{"start":178,"end":191,"reference_id":"38895997","reference_source":"pmid","reference_html":"Conformational diversity of human HP1α. <i> Ukmar-Godec T, Yu T, de Opakua AI, Pantoja CF, Munari F, Zweckstetter M. </i> Protein Sci, 2024","date":"2024-09-02T17:35:57.682Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04242r003","statement":[{"text":"Secondary structure propensities predicted by TALOS N+ are in agreement with the high‐resolution structures of the individual CD and CSD, and suggested the presence of predominantly random coil conformation in the NTE, the HR, and the CTE (Figure 1c).","type":"Results"},{"text":"(a) Schematic of Hp1 dimer containing the ordered CD and CSD and disordered NTE, HR, and CTE.","type":"Figure"},{"text":"In Figure 1 authors define NTE as the 1-21 region, HR as the hinge region 79-123, and CTE as 178-191 C-terminal region. ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:22:41.788Z"}},{"start":178,"end":191,"reference_id":"38895997","reference_source":"pmid","reference_html":"Conformational diversity of human HP1α. <i> Ukmar-Godec T, Yu T, de Opakua AI, Pantoja CF, Munari F, Zweckstetter M. </i> Protein Sci, 2024","date":"2024-09-02T17:36:08.631Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04242r004","statement":[{"text":"Secondary structure propensities predicted by TALOS N+ are in agreement with the high‐resolution structures of the individual CD and CSD, and suggested the presence of predominantly random coil conformation in the NTE, the HR, and the CTE (Figure 1c).","type":"Results"},{"text":"(a) Schematic of Hp1 dimer containing the ordered CD and CSD and disordered NTE, HR, and CTE.","type":"Figure"},{"text":"In Figure 1 authors define NTE as the 1-21 region, HR as the hinge region 79-123, and CTE as 178-191 C-terminal region. ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:22:56.173Z"}},{"start":79,"end":123,"reference_id":"38895997","reference_source":"pmid","reference_html":"Conformational diversity of human HP1α. <i> Ukmar-Godec T, Yu T, de Opakua AI, Pantoja CF, Munari F, Zweckstetter M. </i> Protein Sci, 2024","date":"2024-09-02T17:46:35.206Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04242r005","statement":[{"text":"Secondary structure propensities predicted by TALOS N+ are in agreement with the high‐resolution structures of the individual CD and CSD, and suggested the presence of predominantly random coil conformation in the NTE, the HR, and the CTE (Figure 1c).","type":"Results"},{"text":"(a) Schematic of Hp1 dimer containing the ordered CD and CSD and disordered NTE, HR, and CTE.","type":"Figure"},{"text":"In Figure 1 authors define NTE as the 1-21 region, HR as the hinge region 79-123, and CTE as 178-191 C-terminal region. ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:22:54.700Z"}},{"start":1,"end":21,"reference_id":"38895997","reference_source":"pmid","reference_html":"Conformational diversity of human HP1α. <i> Ukmar-Godec T, Yu T, de Opakua AI, Pantoja CF, Munari F, Zweckstetter M. </i> Protein Sci, 2024","date":"2024-09-02T17:46:51.912Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04242r006","statement":[{"text":"Secondary structure propensities predicted by TALOS N+ are in agreement with the high‐resolution structures of the individual CD and CSD, and suggested the presence of predominantly random coil conformation in the NTE, the HR, and the CTE (Figure 1c).","type":"Results"},{"text":"(a) Schematic of Hp1 dimer containing the ordered CD and CSD and disordered NTE, HR, and CTE.","type":"Figure"},{"text":"In Figure 1 authors define NTE as the 1-21 region, HR as the hinge region 79-123, and CTE as 178-191 C-terminal region. ","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:22:50.254Z"}}],"regions_counter":6,"released":"2024_12","sequence":"MGKKTKRTADSSSSEDEEEYVVEKVLDRRVVKGQVEYLLKWKGFSEEHNTWEPEKNLDCPELISEFMKKYKKMKEGENNKPREKSESNKRKSNFSNSADDIKSKKKREQSNDIARGFERGLEPEKIIGATDSCGDLMFLMKWKDTDEADLVLAKEANVKCPQIVIAFYEERLTWHAYPEDAENKEKETAKS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.17801047120418848,"dataset":["Condensates-related proteins"],"disorder_content":0.418848167539267,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"},{"start":79,"end":123,"type":"D"},{"start":178,"end":191,"type":"D"}],"Structural state":[{"start":1,"end":21,"type":"D"},{"start":79,"end":123,"type":"D"},{"start":178,"end":191,"type":"D"}],"Disorder function":[{"start":1,"end":21,"type":"F"},{"start":79,"end":123,"type":"F"},{"start":178,"end":191,"type":"F"}]}},{"disprot_id":"DP04243","acc":"A0A0H2UWN8","creator":"vnugnes","date":"2024-09-02T18:12:25.996Z","features":{"pfam":[{"id":"PF24313","name":"Paratox","start":1,"end":59}],"gene3D":[]},"genes":[{"olnNames":[{"value":"SpyM3_1300","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAM79907.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAM79907.1"}}]}]}],"length":60,"name":"Paratox","ncbi_taxon_id":198466,"organism":"Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315)","regions":[{"start":1,"end":60,"reference_id":"38801244","reference_source":"pmid","reference_html":"The Streptococcus phage protein paratox is an intrinsically disordered protein. <i> Asakereh I, Rutbeek NR, Singh M, Davidson D, Prehna G, Khajehpour M. </i> Protein Sci, 2024","date":"2024-09-02T18:21:05.145Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04243r001","statement":[{"text":"As the CD spectrum demonstrated that the structure of Prx was unfolded at physiological buffer conditions, we then used NMR to gain further insight into the solution‐state fold of Prx. ","type":"Results"},{"text":"The Streptococcus phage protein paratox is an intrinsically disordered protein","type":"Title"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:23:22.677Z"}},{"start":1,"end":60,"reference_id":"38801244","reference_source":"pmid","reference_html":"The Streptococcus phage protein paratox is an intrinsically disordered protein. <i> Asakereh I, Rutbeek NR, Singh M, Davidson D, Prehna G, Khajehpour M. </i> Protein Sci, 2024","date":"2024-09-02T18:21:50.404Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04243r002","statement":[{"text":"It can be clearly seen that in the absence of high‐salt or crowding agents, the 1H‐15N HSQC dispersion pattern of Prx at pH 7 is similar to that measured under denaturing conditions. Specifically, all backbone chemical shifts show low dispersion and are clustered between 8.0 and 8.6 ppm in the hydrogen dimension. This 1H‐15N HSQC pattern is diagnostic of a protein that lacks secondary structure and is disordered (Pandey et al., 2023; Prehna et al., 2014).","type":"Results"},{"text":"The Streptococcus phage protein paratox is an intrinsically disordered protein","type":"Title"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:23:15.919Z"}},{"start":1,"end":60,"reference_id":"38801244","reference_source":"pmid","reference_html":"The Streptococcus phage protein paratox is an intrinsically disordered protein. <i> Asakereh I, Rutbeek NR, Singh M, Davidson D, Prehna G, Khajehpour M. </i> Protein Sci, 2024","date":"2024-09-02T18:23:00.341Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04243r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8DWI6"}],"statement":[{"text":"In contrast, the addition of unlabeled ComR DNA‐binding domain (DBD) to 15N‐labeled Prx results in a well resolved 1H‐15N HSQC indicative of an ordered and globular protein fold (Figure 3c).","type":"Results"}]},{"start":1,"end":60,"reference_id":"38801244","reference_source":"pmid","reference_html":"The Streptococcus phage protein paratox is an intrinsically disordered protein. <i> Asakereh I, Rutbeek NR, Singh M, Davidson D, Prehna G, Khajehpour M. </i> Protein Sci, 2024","date":"2024-09-02T18:24:28.239Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04243r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8DWI6"}],"statement":[{"text":"\"It can be clearly seen that in the absence of high‐salt or crowding agents, the 1H‐15N HSQC dispersion pattern of Prx at pH 7 is similar to that measured under denaturing conditions. Specifically, all backbone chemical shifts show low dispersion and are clustered between 8.0 and 8.6 ppm in the hydrogen dimension. This 1H‐15N HSQC pattern is diagnostic of a protein that lacks secondary structure and is disordered (Pandey et al., 2023; Prehna et al., 2014).","type":"Results"},{"text":"In contrast, the addition of unlabeled ComR DNA‐binding domain (DBD) to 15N‐labeled Prx results in a well resolved 1H‐15N HSQC indicative of an ordered and globular protein fold (Figure 3c).","type":"Results"}],"states_connection":[{"source":"DP04243r002","target":"DP04243r003"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:23:25.035Z"}},{"start":1,"end":60,"reference_id":"38801244","reference_source":"pmid","reference_html":"The Streptococcus phage protein paratox is an intrinsically disordered protein. <i> Asakereh I, Rutbeek NR, Singh M, Davidson D, Prehna G, Khajehpour M. </i> Protein Sci, 2024","date":"2024-09-02T18:27:50.028Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q8DWI6","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04243r005","statement":[{"text":"In contrast, the addition of unlabeled ComR DNA‐binding domain (DBD) to 15N‐labeled Prx results in a well resolved 1H‐15N HSQC indicative of an ordered and globular protein fold (Figure 3c).","type":"Results"},{"text":"Additionally, the data shows that Prx ultimately adopts a well‐ordered globular domain when bound to its biological interaction partner ComR.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:23:30.123Z"}},{"start":5,"end":10,"reference_id":"34298018","reference_source":"pmid","reference_html":"Molecular mechanism of quorum sensing inhibition in Streptococcus by the phage protein paratox. <i> Rutbeek NR, Rezasoltani H, Patel TR, Khajehpour M, Prehna G. </i> J Biol Chem, 2021","date":"2025-06-16T19:23:42.291Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7N1N"},{"db":"PDB","id":"7N10"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q8DWI6","operator":null,"partner_start":1,"partner_end":68}],"region_id":"DP04243r006","statement":[{"text":"This binding network is extended across the full face of the DBD:Prx interaction by Prx E6 making a hydrogen bond with the invariable ComR residue K49 and Prx E9 providing a mainchain hydrogen bond with ComR T44 (Fig. 3A).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":32,"end":44,"reference_id":"34298018","reference_source":"pmid","reference_html":"Molecular mechanism of quorum sensing inhibition in Streptococcus by the phage protein paratox. <i> Rutbeek NR, Rezasoltani H, Patel TR, Khajehpour M, Prehna G. </i> J Biol Chem, 2021","date":"2025-07-01T14:24:52.248Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7N1N"},{"db":"PDB","id":"7N10"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q8DWI6","operator":null,"partner_start":1,"partner_end":68}],"region_id":"DP04243r007","statement":[{"text":"Specifically, Prx utilizes D32 to make hydrogen bonds with both the essential arginine residues R33 and R37 in ComR that are responsible for DNA recognition (22) (Fig. 3A). Furthermore, residue D32 is the focal point for a stabilized hydrogen bonding network that positions Prx E44 to make a salt-bridge with ComR R33, Prx D38 to salt-bridge with ComR R37 and for the arginine side chains to be further stabilized by hydrogen bond interactions with the Prx mainchain. This binding network is extended across the full face of the DBD:Prx interaction by Prx E6 making a hydrogen bond with the invariable ComR residue K49 and Prx E9 providing a mainchain hydrogen bond with ComR T44 (Fig. 3A).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":30,"end":35,"reference_id":"34298018","reference_source":"pmid","reference_html":"Molecular mechanism of quorum sensing inhibition in Streptococcus by the phage protein paratox. <i> Rutbeek NR, Rezasoltani H, Patel TR, Khajehpour M, Prehna G. </i> J Biol Chem, 2021","date":"2025-06-16T19:26:08.156Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu6Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu9Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp32Ala","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"7N1N"},{"db":"PDB","id":"7N10"}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q8DWI6","operator":null,"partner_start":1,"partner_end":66}],"region_id":"DP04243r008","statement":[{"text":"Multiple Prx protein variants were assessed for their ability to bind to full-length ComR using SEC. Prx variants of the three residues highlighted in Figure 3A (PrxE6A, PrxE9A, PrxD32A) were unable to form a complex with ComR, while Prx D12A, which is not at the DBD interface, was still able to form a complex (Fig. 4, A and B, and Fig. S5).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":5,"end":10,"reference_id":"34298018","reference_source":"pmid","reference_html":"Molecular mechanism of quorum sensing inhibition in Streptococcus by the phage protein paratox. <i> Rutbeek NR, Rezasoltani H, Patel TR, Khajehpour M, Prehna G. </i> J Biol Chem, 2021","date":"2025-06-16T19:26:14.102Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu6Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu9Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp32Ala","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"7N1N"},{"db":"PDB","id":"7N10"}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q8DWI6","operator":null,"partner_start":1,"partner_end":66}],"region_id":"DP04243r009","statement":[{"text":"Multiple Prx protein variants were assessed for their ability to bind to full-length ComR using SEC. Prx variants of the three residues highlighted in Figure 3A (PrxE6A, PrxE9A, PrxD32A) were unable to form a complex with ComR, while Prx D12A, which is not at the DBD interface, was still able to form a complex (Fig. 4, A and B, and Fig. S5).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":60,"reference_id":"34298018","reference_source":"pmid","reference_html":"Molecular mechanism of quorum sensing inhibition in Streptococcus by the phage protein paratox. <i> Rutbeek NR, Rezasoltani H, Patel TR, Khajehpour M, Prehna G. </i> J Biol Chem, 2021","date":"2025-06-16T19:45:19.779Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0043392","term_name":"negative regulation of DNA binding","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q8DWI6","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04243r010","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A411IAX7"}],"statement":[{"text":"When ComR, XIP, and were Prx added together, Prx completely prevented ComR from binding DNA in a dose-dependent manner (Fig. 7A left).","type":"Results"},{"text":"When ComR and Prx were incubated together first followed by the addition of XIP and DNA, similar results were observed to when all components were added together (Fig. 7A middle).","type":"Results"},{"text":"Additionally, when Prx was added after the ComR:XIP:DNA complex was allowed to form Prx could still block the interaction of ComR with DNA (Fig. 7A right).","type":"Results"}],"term_comment":"","term_def":"\"Any process that stops or reduces the frequency, rate or extent of DNA binding. DNA binding is any process in which a gene product interacts selectively with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":60,"reference_id":"34298018","reference_source":"pmid","reference_html":"Molecular mechanism of quorum sensing inhibition in Streptococcus by the phage protein paratox. <i> Rutbeek NR, Rezasoltani H, Patel TR, Khajehpour M, Prehna G. </i> J Biol Chem, 2021","date":"2025-06-16T19:47:50.877Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0045808","term_name":"negative regulation of establishment of competence for transformation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04243r011","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A411IAX7"}],"statement":[{"text":"When ComR, XIP, and were Prx added together, Prx completely prevented ComR from binding DNA in a dose-dependent manner (Fig. 7A left).","type":"Results"},{"text":"When ComR and Prx were incubated together first followed by the addition of XIP and DNA, similar results were observed to when all components were added together (Fig. 7A middle).","type":"Results"},{"text":"Additionally, when Prx was added after the ComR:XIP:DNA complex was allowed to form Prx could still block the interaction of ComR with DNA (Fig. 7A right).","type":"Results"},{"text":"While the biological role of Prx relative to its genetically paired toxin remains to be determined, Prx has been shown to function as a negative regulator of natural competence in Streptococcus. Specifically, Prx binds directly to the apo-form of ComR preventing DNA binding in vitro and acts as a repressor of the S. pyogenes competence regulon in vivo (18).","type":"Introduction"}],"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of establishment of competence for transformation.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":11,"released":"2024_12","sequence":"MLYIDEFKEAIDKGYILGDTVAIVRKNGKIFDYVLPHEKVRDDEVVTVERVEEVMVELDK","taxonomy":["Bacteria","Bacillota","Bacilli","Lactobacillales","Streptococcaceae","Streptococcus"],"alphafold_very_low_content":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":60,"type":"T"}],"Structural state":[{"start":1,"end":60,"type":"D"}],"Structural transition":[{"start":1,"end":60,"type":"T"}],"Molecular function":[{"start":1,"end":60,"type":"F"}],"Biological process":[{"start":1,"end":60,"type":"F"}]}},{"disprot_id":"DP04244","acc":"P40205","creator":"vnugnes","date":"2024-09-03T17:57:20.255Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"MYCNOS"},"synonyms":[{"value":"CYMN"},{"value":"NCYM"}]}],"length":109,"name":"N-cym protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":109,"reference_id":"38526839","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>13</sup>C and <sup>15</sup>N backbone and side-chain resonance assignments of the human oncogenic protein NCYM. <i> Mouhand A, Nakatani K, Kono F, Hippo Y, Matsuo T, Barthe P, Peters J, Suenaga Y, Tamada T, Roumestand C. </i> Biomol NMR Assign, 2024","date":"2024-09-03T18:05:11.403Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Uniformly 15N- and 13C-labeled GST-tagged NCYM (GST-NCYM) was expressed from cell culture in a M9 medium containing 15N-NH4Cl and 13C-glycerol/glucose as sole source of nitrogen and carbon."}]},{"term_id":"MI:0379","term_name":"13C label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"Uniformly 15N- and 13C-labeled GST-tagged NCYM (GST-NCYM) was expressed from cell culture in a M9 medium containing 15N-NH4Cl and 13C-glycerol/glucose as sole source of nitrogen and carbon."}]},{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"Uniformly 15N- and 13C-labeled GST-tagged NCYM (GST-NCYM) was expressed from cell culture in a M9 medium containing 15N-NH4Cl and 13C-glycerol/glucose as sole source of nitrogen and carbon."}]}],"region_id":"DP04244r001","statement":[{"text":"The 1H-15N HSQC spectrum of NCYM is shown in Fig. 1: the poor dispersion observed for the amide proton resonances, centered at ≈ 8.4 ppm, strongly suggests the absence of a well-defined 3D structure for NYCM that behaves as an Intrinsically Disordered Protein (IDP).","type":"Article"},{"text":" The values obtained for the difference (SCS Cα—SCS Cβ) are indicative of an overall highly-disordered structure, but the predominance of positive values for successive residues in the central part of the peptide (segment 45–70) suggests their propensity to adopt an alpha-helical structure (Fig. 2A).","type":"Article"},{"text":"Nevertheless, TALOS-N Q-ratios calculated for the helix (Fig. 2B) on the residues belonging to this region are low (< 0.5), as well as the RCI-S2 order parameters (< 0.6) (Fig. 2D), indicating a highly dynamic region, where the alpha-helix can be formed only transiently. This conclusion is further supported by the absence of medium-range NOEs specific to helical secondary structure in the 3D NOESY-HSQC experiment.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:23:49.501Z"}},{"start":1,"end":109,"reference_id":"38074684","reference_source":"pmid","reference_html":"Structural characterization of human <i>de novo</i> protein NCYM and its complex with a newly identified DNA aptamer using atomic force microscopy and small-angle X-ray scattering. <i> Yamamoto S, Kono F, Nakatani K, Hirose M, Horii K, Hippo Y, Tamada T, Suenaga Y, Matsuo T. </i> Front Oncol, 2023","date":"2024-09-03T18:12:25.785Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04244r002","statement":[{"text":"The Kratky plot (Q2･I(Q) vs Q) (42) shows that the Q2･I(Q) value reaches a peak at around Q = 0.1 [Å-1] and decreases slightly, followed by the increase, suggesting that NCYM is not a completely unfolded protein, but a partially folded protein. This interpretation is further supported by the Q3 plot (Q3･I(Q) vs Q3), where the Q3･I(Q) value reaches a plateau, which is a hallmark of partially folded proteins (43). In contrast, no plateau was observed in the Porod-Debye plot (43), suggesting that NCYM is not a well-folded protein.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:23:48.097Z"}},{"start":1,"end":109,"reference_id":"24391509","reference_source":"pmid","reference_html":"NCYM, a Cis-antisense gene of MYCN, encodes a de novo evolved protein that inhibits GSK3β resulting in the stabilization of MYCN in human neuroblastomas. <i> Suenaga Y, Islam SM, Alagu J, Kaneko Y, Kato M, Tanaka Y, Kawana H, Hossain S, Matsumoto D, Yamamoto M, Shoji W, Itami M, Shibata T, Nakamura Y, Ohira M, Haraguchi S, Takatori A, Nakagawara A. </i> PLoS Genet, 2014","date":"2024-09-20T08:59:06.294Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0050821","term_name":"protein stabilization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006049","ec_ontology":"ECO","ec_name":"genetic transformation evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IMP","region_id":"DP04244r003","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_1771","entry_name":"TGW-I-nu"}],"statement":[{"text":"In addition, knockdown of NCYM decreased the stability of the MYCN protein (Figure S11B). This NCYM knockdown-mediated destabilization of MYCN could be inhibited using the proteasome inhibitor MG132 (Figure S11C).","type":"Results"}],"term_comment":"","term_def":"\"Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:25:40.121Z"}},{"start":1,"end":109,"reference_id":"24391509","reference_source":"pmid","reference_html":"NCYM, a Cis-antisense gene of MYCN, encodes a de novo evolved protein that inhibits GSK3β resulting in the stabilization of MYCN in human neuroblastomas. <i> Suenaga Y, Islam SM, Alagu J, Kaneko Y, Kato M, Tanaka Y, Kawana H, Hossain S, Matsumoto D, Yamamoto M, Shoji W, Itami M, Shibata T, Nakamura Y, Ohira M, Haraguchi S, Takatori A, Nakagawara A. </i> PLoS Genet, 2014","date":"2024-09-20T09:06:38.162Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005644","ec_ontology":"ECO","ec_name":"immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P49841","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P04198","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04244r004","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_1124","entry_name":"Children's Hospital of Philadelphia-134"}],"statement":[{"text":"Therefore, using immunoprecipitation, we next searched for factors interacting with NCYM that are able to induce MYCN stabilization, and found that NCYM forms a complex with MYCN and GSK3β in CHP134 cells (Figure 3F and G).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:25:38.202Z"}},{"start":1,"end":109,"reference_id":"24391509","reference_source":"pmid","reference_html":"NCYM, a Cis-antisense gene of MYCN, encodes a de novo evolved protein that inhibits GSK3β resulting in the stabilization of MYCN in human neuroblastomas. <i> Suenaga Y, Islam SM, Alagu J, Kaneko Y, Kato M, Tanaka Y, Kawana H, Hossain S, Matsumoto D, Yamamoto M, Shoji W, Itami M, Shibata T, Nakamura Y, Ohira M, Haraguchi S, Takatori A, Nakagawara A. </i> PLoS Genet, 2014","date":"2024-09-20T09:10:55.031Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P49841","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P04198","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04244r005","statement":[{"text":"In addition, purified NCYM was capable of interacting with purified GSK3β and MYCN in vitro (Figure 3H).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:24:16.640Z"}},{"start":1,"end":109,"reference_id":"24391509","reference_source":"pmid","reference_html":"NCYM, a Cis-antisense gene of MYCN, encodes a de novo evolved protein that inhibits GSK3β resulting in the stabilization of MYCN in human neuroblastomas. <i> Suenaga Y, Islam SM, Alagu J, Kaneko Y, Kato M, Tanaka Y, Kawana H, Hossain S, Matsumoto D, Yamamoto M, Shoji W, Itami M, Shibata T, Nakamura Y, Ohira M, Haraguchi S, Takatori A, Nakagawara A. </i> PLoS Genet, 2014","date":"2024-09-20T09:14:48.863Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006469","term_name":"negative regulation of protein kinase activity","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001202","ec_ontology":"ECO","ec_name":"in vitro protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IDA","region_id":"DP04244r006","statement":[{"text":"To examine the effect of NCYM on GSK3β-mediated phosphorylation of MYCN, we performed an in vitro kinase assay (Figure 3I). NCYM protein inhibited the phosphorylation of MYCN. Because the purified NCYM protein is not a substrate of GSK3β (Figure S12), it is unlikely that NCYM competes with MYCN for GSK3β as a substrate. Taken together these results suggest that the NCYM protein inhibits GSK3β-mediated MYCN phosphorylation and stabilizes the MYCN protein in vitro.","type":"Results"}],"term_comment":"","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of protein kinase activity.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:24:14.765Z"}},{"start":1,"end":109,"reference_id":"24391509","reference_source":"pmid","reference_html":"NCYM, a Cis-antisense gene of MYCN, encodes a de novo evolved protein that inhibits GSK3β resulting in the stabilization of MYCN in human neuroblastomas. <i> Suenaga Y, Islam SM, Alagu J, Kaneko Y, Kato M, Tanaka Y, Kawana H, Hossain S, Matsumoto D, Yamamoto M, Shoji W, Itami M, Shibata T, Nakamura Y, Ohira M, Haraguchi S, Takatori A, Nakagawara A. </i> PLoS Genet, 2014","date":"2024-09-20T09:23:31.596Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0043066","term_name":"negative regulation of apoptotic process","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001585","ec_ontology":"ECO","ec_name":"small interfering RNA knockdown evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IMP","region_id":"DP04244r007","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_1124","entry_name":"Children's Hospital of Philadelphia-134"},{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0529","entry_name":"SK-N-BE(2)C"}],"statement":[{"text":"We performed NCYM knockdown in BE (2)-C, CHP134, SK-N-AS and SH-SY5Y human neuroblastoma cells. SK-N-AS and SH-SY5Y cells are MYCN-single copy but have a high expression of MYC, while BE (2)-C and CHP134 are cell lines with MYCN-amplification and hence have a high expression of MYCN and NCYM (Figure S13A). NCYM knockdown did not affect the survival of the MYCN-single neuroblastoma cell lines, but promoted massive apoptosis of the MYCN-amplified neuroblastoma cells (Figure S13B and C). In addition, in BE (2)-C cells, NCYM knockdown was found to inhibit cell proliferation and invasion (Figure S14B and D). These results suggest that NCYM promotes the survival and aggressiveness of MYCN-amplified neuroblastoma cells.","type":"Results"}],"term_comment":"This term should only be used when it is not possible to determine which phase or subtype of the apoptotic process is negatively regulated by a gene product. Whenever detailed information is available, the more granular children terms should be used.","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.\" [GOC:jl, GOC:mtg_apoptosis]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:24:09.528Z"}},{"start":1,"end":109,"reference_id":"24391509","reference_source":"pmid","reference_html":"NCYM, a Cis-antisense gene of MYCN, encodes a de novo evolved protein that inhibits GSK3β resulting in the stabilization of MYCN in human neuroblastomas. <i> Suenaga Y, Islam SM, Alagu J, Kaneko Y, Kato M, Tanaka Y, Kawana H, Hossain S, Matsumoto D, Yamamoto M, Shoji W, Itami M, Shibata T, Nakamura Y, Ohira M, Haraguchi S, Takatori A, Nakagawara A. </i> PLoS Genet, 2014","date":"2024-09-20T09:37:30.542Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0030335","term_name":"positive regulation of cell migration","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001585","ec_ontology":"ECO","ec_name":"small interfering RNA knockdown evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IMP","region_id":"DP04244r008","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0529","entry_name":"SK-N-BE(2)C"}],"statement":[{"text":"We performed NCYM knockdown in BE (2)-C, CHP134, SK-N-AS and SH-SY5Y human neuroblastoma cells. SK-N-AS and SH-SY5Y cells are MYCN-single copy but have a high expression of MYC, while BE (2)-C and CHP134 are cell lines with MYCN-amplification and hence have a high expression of MYCN and NCYM (Figure S13A). NCYM knockdown did not affect the survival of the MYCN-single neuroblastoma cell lines, but promoted massive apoptosis of the MYCN-amplified neuroblastoma cells (Figure S13B and C). In addition, in BE (2)-C cells, NCYM knockdown was found to inhibit cell proliferation and invasion (Figure S14B and D). These results suggest that NCYM promotes the survival and aggressiveness of MYCN-amplified neuroblastoma cells.","type":"Results"}],"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of cell migration.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:24:00.534Z"}},{"start":1,"end":109,"reference_id":"24391509","reference_source":"pmid","reference_html":"NCYM, a Cis-antisense gene of MYCN, encodes a de novo evolved protein that inhibits GSK3β resulting in the stabilization of MYCN in human neuroblastomas. <i> Suenaga Y, Islam SM, Alagu J, Kaneko Y, Kato M, Tanaka Y, Kawana H, Hossain S, Matsumoto D, Yamamoto M, Shoji W, Itami M, Shibata T, Nakamura Y, Ohira M, Haraguchi S, Takatori A, Nakagawara A. </i> PLoS Genet, 2014","date":"2024-09-20T09:49:22.944Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0043066","term_name":"negative regulation of apoptotic process","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001266","ec_ontology":"ECO","ec_name":"transgenic organism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IMP","region_id":"DP04244r009","statement":[{"text":"We next examined the number of apoptotic cells in neuroblastomas from MYCN transgenic mice and MYCN/NCYM double transgenic mice by staining for cleaved caspase-3 (Figure S17). The number of apoptotic tumor cells was significantly decreased in the primary tumors of MYCN/NCYM double transgenic mice, suggesting that NCYM promotes the survival of neuroblastoma cells in vivo.","type":"Results"}],"term_comment":"This term should only be used when it is not possible to determine which phase or subtype of the apoptotic process is negatively regulated by a gene product. Whenever detailed information is available, the more granular children terms should be used.","term_def":"\"Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.\" [GOC:jl, GOC:mtg_apoptosis]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:23:59.178Z"}},{"start":1,"end":109,"reference_id":"24391509","reference_source":"pmid","reference_html":"NCYM, a Cis-antisense gene of MYCN, encodes a de novo evolved protein that inhibits GSK3β resulting in the stabilization of MYCN in human neuroblastomas. <i> Suenaga Y, Islam SM, Alagu J, Kaneko Y, Kato M, Tanaka Y, Kawana H, Hossain S, Matsumoto D, Yamamoto M, Shoji W, Itami M, Shibata T, Nakamura Y, Ohira M, Haraguchi S, Takatori A, Nakagawara A. </i> PLoS Genet, 2014","date":"2024-09-20T09:53:24.730Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0030335","term_name":"positive regulation of cell migration","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001266","ec_ontology":"ECO","ec_name":"transgenic organism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"ec_go":"IMP","region_id":"DP04244r010","statement":[{"text":"Although tumor formation was not accelerated in the MYCN/NCYM double transgenic mice (Figure S15E), the incidence of neuroblastomas with distant metastases was significantly increased in the MYCN/NCYM double transgenic mice (Figure 4, Figure S16, Table S3).","type":"Results"}],"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of cell migration.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:23:54.724Z"}}],"regions_counter":12,"released":"2024_12","sequence":"MQHPPCEPGNCLSLKEKKITEGSGGVCWGGETDASNPAPALTACCAAEREANVEQGLAGRLLLCNYERRVVRRCKIAGRGRAPLGTRPLDVSSFKLKEEGRPPCLKINK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.6880733944954128,"dataset":["Cancer-related proteins"],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":109,"type":"D"}],"Structural state":[{"start":1,"end":109,"type":"D"}],"Biological process":[{"start":1,"end":109,"type":"F"}],"Molecular function":[{"start":1,"end":109,"type":"F"}]}},{"disprot_id":"DP04246","acc":"Q4KL64","creator":"vnugnes","date":"2024-09-19T12:38:15.801Z","features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":77,"end":145},{"id":"PF13865","name":"C-terminal duplication domain of Friend of PRMT1","start":158,"end":213}],"gene3D":[]},"genes":[{"name":{"value":"Alyref2","evidences":[{"code":"ECO:0000313","source":{"name":"MGI","id":"MGI:1913144","url":"http://www.informatics.jax.org/marker/MGI:1913144"}}]},"synonyms":[{"value":"Refbp2","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAH99405.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAH99405.1"}}]}]}],"length":218,"name":"RNA and export factor binding protein 2","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":1,"end":73,"reference_id":"39282949","reference_source":"pmid","reference_html":"Cryo-EM structure of the CBC-ALYREF complex. <i> Clarke BP, Angelos AE, Mei M, Hill PS, Xie Y, Ren Y. </i> Elife, 2024","date":"2024-09-19T12:48:50.257Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2024_12","version":0,"cross_refs":[{"db":"PDB","id":"8SRR"},{"db":"EMDB","id":"40739"}],"region_id":"DP04246r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09161","statements":[{"type":"Methods","text":"NCBP1-NCBP2 at 1.2 μM was incubated with mALYREF2 (residues 1-155) at 3.6 μM in the presence of the 5’ cap analog m7GpppG (NEB) at 500 μM at 4 °C for 0.5 hr."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P52298","statements":[{"type":"Methods","text":"NCBP1-NCBP2 at 1.2 μM was incubated with mALYREF2 (residues 1-155) at 3.6 μM in the presence of the 5’ cap analog m7GpppG (NEB) at 500 μM at 4 °C for 0.5 hr."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"191209","statements":[{"type":"Methods","text":"NCBP1-NCBP2 at 1.2 μM was incubated with mALYREF2 (residues 1-155) at 3.6 μM in the presence of the 5’ cap analog m7GpppG (NEB) at 500 μM at 4 °C for 0.5 hr."}],"entry_name":"7-methyl-guanosine-5'-triphosphate-5'-guanosine"}],"statement":[{"text":"The N terminal region of mALYREF2 (residues 1 to 73) does not show traceable density and is possibly disordered.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:29:17.602Z"}}],"regions_counter":3,"released":"2024_12","sequence":"MADKMDMSLDDIIKLNRNQRRVNRGGGPRRNRPAIARGGRNRPAPYSRPKPLPDKWQHDLFDSGCGGGEGVETGAKLLVSNLDFGVSDADIQELFAEFGTLKKAAVDYDRSGRSLGTADVHFERRADALKAMKQYKGVPLDGRPMDIQLVTSQIDPQRRPAQSGNRGGMTRNRGSGGFGGRGSQGRGRGTGRNSKQQQLSAEELDAQLDAYNARRDTS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"alphafold_very_low_content":0.25229357798165136,"dataset":["RNA-binding proteins"],"disorder_content":0.3348623853211009,"disprot_consensus":{"full":[{"start":1,"end":73,"type":"D"}],"Structural state":[{"start":1,"end":73,"type":"D"}]}},{"disprot_id":"DP04247","acc":"Q8QL46","creator":"rpancsa","date":"2024-10-30T10:33:58.364Z","features":{"pfam":[{"id":"PF21432","name":"56B-like, Ribbon-helix-helix","start":22,"end":53}],"gene3D":[]},"genes":[{"orfNames":[{"value":"56B"}]}],"length":56,"name":"Uncharacterized protein 56B","ncbi_taxon_id":157898,"organism":"Sulfolobus islandicus rod-shaped virus 1","regions":[{"start":1,"end":12,"reference_id":"19535331","reference_source":"pmid","reference_html":"Structure, function, and targets of the transcriptional regulator SvtR from the hyperthermophilic archaeal virus SIRV1. <i> Guillière F, Peixeiro N, Kessler A, Raynal B, Desnoues N, Keller J, Delepierre M, Prangishvili D, Sezonov G, Guijarro JI. </i> J Biol Chem, 2009","date":"2024-10-30T10:37:40.533Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"2KEL"}],"region_id":"DP04247r001","statement":[{"text":"The protein forms a dimer in solution. The NMR solution structure of the protein consists of a ribbon-helix-helix (RHH) fold between residues 13 and 56 and a disordered N-terminal region (residues 1-12).","type":"Abstract"},{"text":"The structural ensemble of SvtR showed a well ordered region between residues 13 and 56 and an N-terminal non-convergent region between residues 1 and 12 (Fig. 1A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:29:33.222Z"}},{"start":1,"end":12,"reference_id":"19535331","reference_source":"pmid","reference_html":"Structure, function, and targets of the transcriptional regulator SvtR from the hyperthermophilic archaeal virus SIRV1. <i> Guillière F, Peixeiro N, Kessler A, Raynal B, Desnoues N, Keller J, Delepierre M, Prangishvili D, Sezonov G, Guijarro JI. </i> J Biol Chem, 2009","date":"2024-10-30T10:38:04.800Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"2KEL"}],"region_id":"DP04247r002","statement":[{"text":"The protein forms a dimer in solution. The NMR solution structure of the protein consists of a ribbon-helix-helix (RHH) fold between residues 13 and 56 and a disordered N-terminal region (residues 1-12).","type":"Abstract"},{"text":"The structural ensemble of SvtR showed a well ordered region between residues 13 and 56 and an N-terminal non-convergent region between residues 1 and 12 (Fig. 1A).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:29:38.050Z"}}],"regions_counter":2,"released":"2025_06","sequence":"MQTQEQSQKKKQKAVFGIYMDKDLKTRLKVYCAKNNLQLTQAIEEAIKEYLQKRNG","taxonomy":["Viruses","Adnaviria","Zilligvirae","Taleaviricota","Tokiviricetes","Ligamenvirales","Rudiviridae","Icerudivirus","Icerudivirus SIRV1"],"dataset":["Viral proteins"],"disorder_content":0.21428571428571427,"disprot_consensus":{"full":[{"start":1,"end":12,"type":"D"}],"Structural state":[{"start":1,"end":12,"type":"D"}],"Disorder function":[{"start":1,"end":12,"type":"F"}]}},{"disprot_id":"DP04248","acc":"C8ZKB3","creator":"rpancsa","date":"2024-10-30T10:43:23.284Z","features":{"pfam":[],"gene3D":[]},"genes":[],"length":99,"name":"Uncharacterized protein","ncbi_taxon_id":655097,"organism":"Pseudomonas phage LUZ7","regions":[{"start":1,"end":17,"reference_id":"31724707","reference_source":"pmid","reference_html":"'Drc', a structurally novel ssDNA-binding transcription regulator of N4-related bacterial viruses. <i> Boon M, De Zitter E, De Smet J, Wagemans J, Voet M, Pennemann FL, Schalck T, Kuznedelov K, Severinov K, Van Meervelt L, De Maeyer M, Lavigne R. </i> Nucleic Acids Res, 2020","date":"2024-10-30T10:46:04.276Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"6QLC"}],"region_id":"DP04248r001","statement":[{"text":"The N-terminal residues 1–17 of Drc and five amino acids that remained from the tag could not be resolved from the electron density maps. This region is predicted by ESpritz to be disordered (Supplementary Figure S3), which could explain the weak electron density (37).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:29:51.031Z"}},{"start":1,"end":17,"reference_id":"31724707","reference_source":"pmid","reference_html":"'Drc', a structurally novel ssDNA-binding transcription regulator of N4-related bacterial viruses. <i> Boon M, De Zitter E, De Smet J, Wagemans J, Voet M, Pennemann FL, Schalck T, Kuznedelov K, Severinov K, Van Meervelt L, De Maeyer M, Lavigne R. </i> Nucleic Acids Res, 2020","date":"2024-10-30T10:46:20.202Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"6QLC"}],"region_id":"DP04248r002","statement":[{"text":"The N-terminal residues 1–17 of Drc and five amino acids that remained from the tag could not be resolved from the electron density maps. This region is predicted by ESpritz to be disordered (Supplementary Figure S3), which could explain the weak electron density (37).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:29:57.183Z"}}],"regions_counter":2,"released":"2025_06","sequence":"MALVKKNQARNTQATDNKGASAYLNFHFPTRDGKDVRLVSLGLRADDALHMQLQEFLTVDDKGKPLSETAYAERCKKLVSRLIIKLGVTRSEEERALDL","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Uroviricota","Caudoviricetes","Schitoviridae","Migulavirinae","Luzseptimavirus","Luzseptimavirus LUZ7"],"dataset":["Viral proteins"],"disorder_content":0.1717171717171717,"disprot_consensus":{"full":[{"start":1,"end":17,"type":"D"}],"Structural state":[{"start":1,"end":17,"type":"D"}],"Disorder function":[{"start":1,"end":17,"type":"F"}]}},{"disprot_id":"DP04249","acc":"Q1D3H3","creator":"rpancsa","date":"2024-10-30T10:48:47.411Z","features":{"pfam":[{"id":"PF02195","name":"ParB N-terminal domain","start":296,"end":383}],"gene3D":[]},"genes":[{"name":{"value":"padC","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"29180656","url":"http://www.ncbi.nlm.nih.gov/pubmed/29180656","alternativeUrl":"https://europepmc.org/abstract/MED/29180656"}}]},"olnNames":[{"value":"MXAN_4634","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"ABF89778.1","url":"https://www.ebi.ac.uk/ena/browser/view/ABF89778.1"}}]}]}],"length":489,"name":"ParBC domain-containing protein","ncbi_taxon_id":246197,"organism":"Myxococcus xanthus (strain DK1622)","regions":[{"start":422,"end":489,"reference_id":"31835030","reference_source":"pmid","reference_html":"ParB-type DNA Segregation Proteins Are CTP-Dependent Molecular Switches. <i> Osorio-Valeriano M, Altegoer F, Steinchen W, Urban S, Liu Y, Bange G, Thanbichler M. </i> Cell, 2019","date":"2024-10-30T10:51:10.622Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"6RYK"}],"region_id":"DP04249r001","statement":[{"text":"The C-terminal region (aa 422–489) was not resolved in the crystal structure, suggesting that it is flexible.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:30:22.600Z"}},{"start":422,"end":489,"reference_id":"31835030","reference_source":"pmid","reference_html":"ParB-type DNA Segregation Proteins Are CTP-Dependent Molecular Switches. <i> Osorio-Valeriano M, Altegoer F, Steinchen W, Urban S, Liu Y, Bange G, Thanbichler M. </i> Cell, 2019","date":"2024-10-30T10:51:33.821Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"6RYK"}],"region_id":"DP04249r002","statement":[{"text":"The C-terminal region (aa 422–489) was not resolved in the crystal structure, suggesting that it is flexible.","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:30:24.264Z"}}],"regions_counter":2,"released":"2025_06","sequence":"MRARGLFRGATMDAEHRVDGQDGTAGAGPEGGSQAPSGQDGGQGGAVSAELHASGGPSGPQGEHRREDASPESGGEHRAEGTPPAEGSEQRAEGTPAAEGSEQRAEGKPSEQGVAQRAEDTPSEQGEPQNAGSAQGQGGEPPVASGDTQGEGERPHNAGGEAPGSADASGSEGSKDQAGSQEGGLQAEGTTSQGQAEPPAKDASHAQGEHQAVSDSHGQDGSESGGRSVANEEARAEQSPSDGEARVTPGLDERPQGAFWTGEADGDKSGDSDEASREDVLPEPEQRLSGRVTTVLLPLEKLQDESAFKLRPEGDVSGLATDIARLGQLFPVDVRPAGEDRYQLVCGFRRVAALRFLKRDAVQARIHLRLSDEDALVMSLAEAIHATPVGPEVLEAKRDELEAQGRLSAAVRDMLEKALATEDTLAPEGVEEEIDADELAQEVAQRLGAINQDLSLLADVFAALDESRKAELLMQLRYSSELVTYLEGL","taxonomy":["Bacteria","Myxococcota","Myxococcia","Myxococcales","Cystobacterineae","Myxococcaceae","Myxococcus"],"alphafold_very_low_content":0.5705521472392638,"disorder_content":0.1390593047034765,"disprot_consensus":{"full":[{"start":422,"end":489,"type":"D"}],"Structural state":[{"start":422,"end":489,"type":"D"}],"Disorder function":[{"start":422,"end":489,"type":"F"}]}},{"disprot_id":"DP04250","acc":"P0DJL7","creator":"rpancsa","date":"2024-10-30T10:56:42.386Z","features":{"pfam":[{"id":"PF01325","name":"Iron dependent repressor, N-terminal DNA binding domain","start":3,"end":61},{"id":"PF02742","name":"Iron dependent repressor, metal binding and dimerisation domain","start":65,"end":133},{"id":"PF18357","name":"Diphteria toxin repressor SH3 domain","start":148,"end":225}],"gene3D":[]},"genes":[{"name":{"value":"dtxR"},"olnNames":[{"value":"DIP1414"}]}],"length":226,"name":"Diphtheria toxin repressor","ncbi_taxon_id":257309,"organism":"Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)","regions":[{"start":130,"end":146,"reference_id":"10339551","reference_source":"pmid","reference_html":"Solution structure and peptide binding studies of the C-terminal src homology 3-like domain of the diphtheria toxin repressor protein. <i> Wang G, Wylie GP, Twigg PD, Caspar DL, Murphy JR, Logan TM. </i> Proc Natl Acad Sci U S A, 1999","date":"2024-10-30T11:38:45.217Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"1BYM"}],"region_id":"DP04250r001","statement":[{"text":"The solution structure of the C-terminal domain, consisting of residues N130-L226 plus a 13-residue N-terminal extension, has been determined by using NMR spectroscopy. Residues before A147 are highly mobile and adopt a random coil conformation, but residues A147-L226 form a single structured domain consisting of five beta-strands and three helices arranged into a partially orthogonal, two-sheet beta-barrel, similar to the structure observed in the crystalline Co2+ complex of full-length DtxR.","type":"Abstract"},{"text":"The structure of DtxR(130–226) consists of a disordered N-terminal region (residues N130-A146) followed by a folded domain (residues A147-L226) (Fig. 3).","type":"Results"},{"text":"Residues preceding A147 have negative heteronuclear NOEs (Fig. 1b), indicating high mobility (25).","type":"Results"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-10-30T16:30:42.095Z"}},{"start":130,"end":144,"reference_id":"10339551","reference_source":"pmid","reference_html":"Solution structure and peptide binding studies of the C-terminal src homology 3-like domain of the diphtheria toxin repressor protein. <i> Wang G, Wylie GP, Twigg PD, Caspar DL, Murphy JR, Logan TM. </i> Proc Natl Acad Sci U S A, 1999","date":"2025-06-30T15:46:13.589Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007688","ec_ontology":"ECO","ec_name":"gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"ec_go":"IDA","region_id":"DP04250r002","statement":[{"text":"During purification and characterization of DtxR(130–226), it was observed that highly purified protein ran as a series of bands in nondenaturing polyacrylamide gels that correlated in mass to multiples of the monomeric protein molecular weight (Fig. 4).","type":"Results"},{"text":"However, in contrast to DtxR(130–226), DtxR(144–226) migrated as a single band corresponding to monomer molecular weight in nondenaturing polyacrylamide gels (Fig. 4).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":3,"released":"2025_06","sequence":"MKDLVDTTEMYLRTIYELEEEGVTPLRARIAERLEQSGPTVSQTVARMERDGLVVVASDRSLQMTPTGRTLATAVMRKHRLAERLLTDIIGLDINKVHDEACRWEHVMSDEVERRLVKVLKDVSRSPFGNPIPGLDELGVGNSDAAVPGTRVIDAATSMPRKVRIVQINEIFQVETDQFTQLLDADIRVGSEVEIVDRDGHITLSHNGKDVELIDDLAHTIRIEEL","taxonomy":["Bacteria","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"],"alphafold_very_low_content":0,"dataset":[],"disorder_content":0.0752212389380531,"disprot_consensus":{"full":[{"start":130,"end":146,"type":"D"}],"Structural state":[{"start":130,"end":146,"type":"D"}],"Molecular function":[{"start":130,"end":144,"type":"F"}]}},{"disprot_id":"DP04251","acc":"O60832","creator":"vnugnes","date":"2024-11-01T14:48:34.894Z","features":{"pfam":[{"id":"PF01472","name":"PUA domain","start":297,"end":370},{"id":"PF01509","name":"TruB family pseudouridylate synthase (N terminal domain)","start":110,"end":226},{"id":"PF08068","name":"DKCLD (NUC011) domain","start":49,"end":106},{"id":"PF16198","name":"tRNA pseudouridylate synthase B C-terminal domain","start":227,"end":293}],"gene3D":[]},"genes":[{"name":{"value":"DKC1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:2890","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:2890"}}]},"synonyms":[{"value":"NOLA4"}]}],"length":514,"name":"H/ACA ribonucleoprotein complex subunit DKC1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":22,"reference_id":"38272871","reference_source":"pmid","reference_html":"2.7 Å cryo-EM structure of human telomerase H/ACA ribonucleoprotein. <i> Ghanim GE, Sekne Z, Balch S, van Roon AM, Nguyen THD. </i> Nat Commun, 2024","date":"2024-11-01T14:59:02.058Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"EMDB","id":"17191"},{"db":"EMDB","id":"17190"},{"db":"PDB","id":"8OUF"},{"db":"PDB","id":"8OUE"}],"region_id":"DP04251r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NY12"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NX24"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NPE3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9BUR4"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00004A7003"}],"statement":[{"text":"While the most N-terminal parts of dyskerin (residues 1-22 and 1-42 for the 5’ and 3’ dyskerin, respectively) are not visible in our structure, several disease mutations are located at our newly resolved inter-dyskerin interface (Fig. 2g)16.","type":"Results"},{"text":"The PDB structures show this region lacks electron density, indicating it is disordered. ","type":"Curator statement"}]},{"start":1,"end":22,"reference_id":"38272871","reference_source":"pmid","reference_html":"2.7 Å cryo-EM structure of human telomerase H/ACA ribonucleoprotein. <i> Ghanim GE, Sekne Z, Balch S, van Roon AM, Nguyen THD. </i> Nat Commun, 2024","date":"2024-11-01T14:59:14.566Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"EMDB","id":"17191"},{"db":"EMDB","id":"17190"},{"db":"PDB","id":"8OUF"},{"db":"PDB","id":"8OUE"}],"region_id":"DP04251r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NY12"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NX24"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NPE3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9BUR4"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00004A7003"}],"statement":[{"text":"While the most N-terminal parts of dyskerin (residues 1-22 and 1-42 for the 5’ and 3’ dyskerin, respectively) are not visible in our structure, several disease mutations are located at our newly resolved inter-dyskerin interface (Fig. 2g)16.","type":"Results"},{"text":"The PDB structures show this region lacks electron density, indicating it is disordered. ","type":"Curator statement"}]},{"start":422,"end":514,"reference_id":"38272871","reference_source":"pmid","reference_html":"2.7 Å cryo-EM structure of human telomerase H/ACA ribonucleoprotein. <i> Ghanim GE, Sekne Z, Balch S, van Roon AM, Nguyen THD. </i> Nat Commun, 2024","date":"2024-11-01T15:02:35.185Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"EMDB","id":"17191"},{"db":"EMDB","id":"17190"},{"db":"PDB","id":"8OUF"},{"db":"PDB","id":"8OUE"}],"region_id":"DP04251r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NY12"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NX24"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NPE3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9BUR4"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00004A7003"}],"statement":[{"text":"Dyskerin consists of four domains: an N-terminal extension (NTE), a pseudouridine synthase and achaeosine transglycosylase (PUA), a tRNA pseudouridine synthase B-like (TruB) and a C-terminal extension (CTE) domain (Fig. 2a).","type":"Results"},{"text":"The PDB structures show this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":422,"end":514,"reference_id":"38272871","reference_source":"pmid","reference_html":"2.7 Å cryo-EM structure of human telomerase H/ACA ribonucleoprotein. <i> Ghanim GE, Sekne Z, Balch S, van Roon AM, Nguyen THD. </i> Nat Commun, 2024","date":"2024-11-01T15:02:47.223Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"EMDB","id":"17191"},{"db":"EMDB","id":"17190"},{"db":"PDB","id":"8OUF"},{"db":"PDB","id":"8OUE"}],"region_id":"DP04251r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NY12"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NX24"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NPE3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9BUR4"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00004A7003"}],"statement":[{"text":"Dyskerin consists of four domains: an N-terminal extension (NTE), a pseudouridine synthase and achaeosine transglycosylase (PUA), a tRNA pseudouridine synthase B-like (TruB) and a C-terminal extension (CTE) domain (Fig. 2a).","type":"Results"},{"text":"The PDB structures show this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"regions_counter":4,"released":"2025_06","sequence":"MADAEVIILPKKHKKKKERKSLPEEDVAEIQHAEEFLIKPESKVAKLDTSQWPLLLKNFDKLNVRTTHYTPLACGSNPLKREIGDYIRTGFINLDKPSNPSSHEVVAWIRRILRVEKTGHSGTLDPKVTGCLIVCIERATRLVKSQQSAGKEYVGIVRLHNAIEGGTQLSRALETLTGALFQRPPLIAAVKRQLRVRTIYESKMIEYDPERRLGIFWVSCEAGTYIRTLCVHLGLLLGVGGQMQELRRVRSGVMSEKDHMVTMHDVLDAQWLYDNHKDESYLRRVVYPLEKLLTSHKRLVMKDSAVNAICYGAKIMLPGVLRYEDGIEVNQEIVVITTKGEAICMAIALMTTAVISTCDHGIVAKIKRVIMERDTYPRKWGLGPKASQKKLMIKQGLLDKHGKPTDSTPATWKQEYVDYSESAKKEVVAEVVKAPQVVAEAAKTAKRKRESESESDETPPAAPQLIKKEKKKSKKDKKAKAGLESGAEPGDGDSDTTKKKKKKKKAKEVELVSE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.22178988326848248,"dataset":["NDDs-related proteins","RNA-binding proteins"],"disorder_content":0.2237354085603113,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"},{"start":422,"end":514,"type":"D"}],"Structural state":[{"start":1,"end":22,"type":"D"},{"start":422,"end":514,"type":"D"}],"Disorder function":[{"start":1,"end":22,"type":"F"},{"start":422,"end":514,"type":"F"}]}},{"disprot_id":"DP04252","acc":"Q9NX24","creator":"vnugnes","date":"2024-11-01T15:12:30.032Z","features":{"pfam":[{"id":"PF01248","name":"Ribosomal protein L7Ae/L30e/S12e/Gadd45 family","start":46,"end":137}],"gene3D":[]},"genes":[{"name":{"value":"NHP2"},"synonyms":[{"value":"NOLA2"}],"orfNames":[{"value":"HSPC286"}]}],"length":153,"name":"H/ACA ribonucleoprotein complex subunit 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":22,"reference_id":"38272871","reference_source":"pmid","reference_html":"2.7 Å cryo-EM structure of human telomerase H/ACA ribonucleoprotein. <i> Ghanim GE, Sekne Z, Balch S, van Roon AM, Nguyen THD. </i> Nat Commun, 2024","date":"2024-11-01T15:23:22.680Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"EMDB","id":"17191"},{"db":"PDB","id":"8OUF"},{"db":"PDB","id":"8OUE"},{"db":"EMDB","id":"17190"}],"region_id":"DP04252r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NY12"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60832"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NPE3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9BUR4"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00004A7003"}],"statement":[{"text":"Secondary structures of dyskerin, GAR1, NHP2, NOP10 and\nTCAB1 obtained from our structure are shown at the top of each sequence.","type":"Supplementary material"},{"text":"Supplementary Table 2 shows this region couldn't be modelled. The PDB structures show this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":1,"end":22,"reference_id":"38272871","reference_source":"pmid","reference_html":"2.7 Å cryo-EM structure of human telomerase H/ACA ribonucleoprotein. <i> Ghanim GE, Sekne Z, Balch S, van Roon AM, Nguyen THD. </i> Nat Commun, 2024","date":"2024-11-01T15:23:32.125Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"EMDB","id":"17191"},{"db":"PDB","id":"8OUF"},{"db":"PDB","id":"8OUE"},{"db":"EMDB","id":"17190"}],"region_id":"DP04252r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NY12"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60832"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NPE3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9BUR4"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00004A7003"}],"statement":[{"text":"Secondary structures of dyskerin, GAR1, NHP2, NOP10 and\nTCAB1 obtained from our structure are shown at the top of each sequence.","type":"Supplementary material"},{"text":"Supplementary Table 2 shows this region couldn't be modelled. The PDB structures show this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"regions_counter":2,"released":"2025_06","sequence":"MTKIKADPDGPEAQAEACSGERTYQELLVNQNPIAQPLASRRLTRKLYKCIKKAVKQKQIRRGVKEVQKFVNKGEKGIMVLAGDTLPIEVYCHLPVMCEDRNLPYVYIPSKTDLGAAAGSKRPTCVIMVKPHEEYQEAYDECLEEVQSLPLPL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.1437908496732026,"dataset":["RNA-binding proteins"],"disorder_content":0.1437908496732026,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"}],"Structural state":[{"start":1,"end":22,"type":"D"}],"Disorder function":[{"start":1,"end":22,"type":"F"}]}},{"disprot_id":"DP04253","acc":"Q9NY12","creator":"vnugnes","date":"2024-11-01T15:24:41.797Z","features":{"pfam":[{"id":"PF04410","name":"Gar1/Naf1 RNA binding region","start":70,"end":158}],"gene3D":[]},"genes":[{"name":{"value":"GAR1"},"synonyms":[{"value":"NOLA1"}]}],"length":217,"name":"H/ACA ribonucleoprotein complex subunit 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":162,"end":217,"reference_id":"38272871","reference_source":"pmid","reference_html":"2.7 Å cryo-EM structure of human telomerase H/ACA ribonucleoprotein. <i> Ghanim GE, Sekne Z, Balch S, van Roon AM, Nguyen THD. </i> Nat Commun, 2024","date":"2024-11-01T15:30:31.305Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"EMDB","id":"17191"},{"db":"PDB","id":"8OUE"},{"db":"PDB","id":"8OUF"},{"db":"EMDB","id":"17190"}],"region_id":"DP04253r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60832"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NPE3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9BUR4"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NX24"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00004A7003"}],"statement":[{"text":"Secondary structures of dyskerin, GAR1, NHP2, NOP10 and TCAB1 obtained from our structure are shown at the top of each sequence.","type":"Supplementary material"},{"text":"Although the rest of the 3’ GAR1 CTE remains unresolved, our structure suggests that GAR1 helix 1 likely serves a similar role in substrate turnover in human H/ACA RNPs32.","type":"Results"},{"text":"Supplementary Table 2 shows this region couldn't be modelled. The PDB structures show this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":162,"end":217,"reference_id":"38272871","reference_source":"pmid","reference_html":"2.7 Å cryo-EM structure of human telomerase H/ACA ribonucleoprotein. <i> Ghanim GE, Sekne Z, Balch S, van Roon AM, Nguyen THD. </i> Nat Commun, 2024","date":"2024-11-01T15:30:44.837Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"EMDB","id":"17191"},{"db":"PDB","id":"8OUE"},{"db":"PDB","id":"8OUF"},{"db":"EMDB","id":"17190"}],"region_id":"DP04253r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60832"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NPE3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9BUR4"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NX24"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00004A7003"}],"statement":[{"text":"Secondary structures of dyskerin, GAR1, NHP2, NOP10 and TCAB1 obtained from our structure are shown at the top of each sequence.","type":"Supplementary material"},{"text":"Although the rest of the 3’ GAR1 CTE remains unresolved, our structure suggests that GAR1 helix 1 likely serves a similar role in substrate turnover in human H/ACA RNPs32.","type":"Results"},{"text":"Supplementary Table 2 shows this region couldn't be modelled. The PDB structures show this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":1,"end":64,"reference_id":"38272871","reference_source":"pmid","reference_html":"2.7 Å cryo-EM structure of human telomerase H/ACA ribonucleoprotein. <i> Ghanim GE, Sekne Z, Balch S, van Roon AM, Nguyen THD. </i> Nat Commun, 2024","date":"2024-11-01T15:34:01.147Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"EMDB","id":"17191"},{"db":"PDB","id":"8OUE"},{"db":"PDB","id":"8OUF"},{"db":"EMDB","id":"17190"}],"region_id":"DP04253r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60832"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NPE3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9BUR4"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NX24"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00004A7003"}],"statement":[{"text":"Secondary structures of dyskerin, GAR1, NHP2, NOP10 and TCAB1 obtained from our structure are shown at the top of each sequence.","type":"Supplementary material"},{"text":"Supplementary Table 2 shows this region couldn't be modelled. The PDB structures show this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":1,"end":64,"reference_id":"38272871","reference_source":"pmid","reference_html":"2.7 Å cryo-EM structure of human telomerase H/ACA ribonucleoprotein. <i> Ghanim GE, Sekne Z, Balch S, van Roon AM, Nguyen THD. </i> Nat Commun, 2024","date":"2024-11-01T15:34:09.155Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"EMDB","id":"17191"},{"db":"PDB","id":"8OUE"},{"db":"PDB","id":"8OUF"},{"db":"EMDB","id":"17190"}],"region_id":"DP04253r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O60832"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NPE3"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9BUR4"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NX24"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"URS00004A7003"}],"statement":[{"text":"Secondary structures of dyskerin, GAR1, NHP2, NOP10 and TCAB1 obtained from our structure are shown at the top of each sequence.","type":"Supplementary material"},{"text":"Supplementary Table 2 shows this region couldn't be modelled. The PDB structures show this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"regions_counter":4,"released":"2025_06","sequence":"MSFRGGGRGGFNRGGGGGGFNRGGSSNHFRGGGGGGGGGNFRGGGRGGFGRGGGRGGFNKGQDQGPPERVVLLGEFLHPCEDDIVCKCTTDENKVPYFNAPVYLENKEQIGKVDEIFGQLRDFYFSVKLSENMKASSFKKLQKFYIDPYKLLPLQRFLPRPPGEKGPPRGGGRGGRGGGRGGGGRGGGRGGGFRGGRGGGGGGFRGGRGGGFRGRGH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.4423963133640553,"disorder_content":0.5529953917050692,"disprot_consensus":{"full":[{"start":1,"end":64,"type":"D"},{"start":162,"end":217,"type":"D"}],"Structural state":[{"start":1,"end":64,"type":"D"},{"start":162,"end":217,"type":"D"}],"Disorder function":[{"start":1,"end":64,"type":"F"},{"start":162,"end":217,"type":"F"}]}},{"disprot_id":"DP04255","acc":"O60016","creator":"vnugnes","date":"2024-11-01T17:07:14.020Z","features":{"pfam":[{"id":"PF00385","name":"Chromo (CHRromatin Organisation MOdifier) domain","start":8,"end":60},{"id":"PF00856","name":"SET domain","start":339,"end":451},{"id":"PF05033","name":"Pre-SET motif","start":216,"end":320}],"gene3D":[]},"genes":[{"name":{"value":"clr4"},"synonyms":[{"value":"kmt1"}],"orfNames":[{"value":"SPBC428.08c"}]}],"length":490,"name":"Histone-lysine N-methyltransferase, H3 lysine-9 specific","ncbi_taxon_id":284812,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","regions":[{"start":69,"end":191,"reference_id":"31165882","reference_source":"pmid","reference_html":"Disordered region of H3K9 methyltransferase Clr4 binds the nucleosome and contributes to its activity. <i> Akoury E, Ma G, Demolin S, Brönner C, Zocco M, Cirilo A, Ivic N, Halic M. </i> Nucleic Acids Res, 2019","date":"2024-11-01T17:12:59.347Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"27903"}],"region_id":"DP04255r001","statement":[{"text":"The chromodomain and the SET domain are connected by a highly disordered region comprising residues S69-S191.","type":"Introduction"}]},{"start":69,"end":191,"reference_id":"31165882","reference_source":"pmid","reference_html":"Disordered region of H3K9 methyltransferase Clr4 binds the nucleosome and contributes to its activity. <i> Akoury E, Ma G, Demolin S, Brönner C, Zocco M, Cirilo A, Ivic N, Halic M. </i> Nucleic Acids Res, 2019","date":"2024-11-01T17:13:10.667Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"27903"}],"region_id":"DP04255r002","statement":[{"text":"The chromodomain and the SET domain are connected by a highly disordered region comprising residues S69-S191.","type":"Introduction"}]},{"start":69,"end":191,"reference_id":"31165882","reference_source":"pmid","reference_html":"Disordered region of H3K9 methyltransferase Clr4 binds the nucleosome and contributes to its activity. <i> Akoury E, Ma G, Demolin S, Brönner C, Zocco M, Cirilo A, Ivic N, Halic M. </i> Nucleic Acids Res, 2019","date":"2024-11-01T17:33:21.396Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031491","term_name":"nucleosome binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"All Clr4 constructs were generated through inverse polymerase chain reaction (PCR) using the Clr4 full-length plasmid cloned in a pET30a expression vector containing an N-terminal His-tag and C-terminal FLAG-tag (Supplementary Tables S1 and 2)."}]}],"ec_go":"IPI","region_id":"DP04255r003","statement":[{"text":"Our data show that the Clr4 ΔCD construct (residues 69–490) binds unmodified and tailless nucleosomes, while the Pre-SET-Post construct (residues 258–490) shows no binding to any kind of nucleosomes.","type":"Results"},{"text":"To further dissect the role of the disordered region in binding to the nucleosome, we generated Clr4 constructs comprising residues 1–191 (Clr4_1–191 which includes CD and the disordered region) and 192–490 (Clr4_192–460 which includes the SET domain). The pull-down assays revealed that the Clr4_1–191 construct, but not Clr4_192–490, binds H3KC9me3 and tailless nucleosomes (Figure 1C). These data show that Clr4 can bind the nucleosome independent of H3K9 methylation through the highly disordered region comprising residues 70–191.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a nucleosome, a complex comprised of DNA wound around a multisubunit core and associated proteins, which forms the primary packing unit of DNA into higher order structures.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"A0A310TTQ1","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P06898","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P02281","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P62799","operator":"and","partner_start":null,"partner_end":null}]},{"start":113,"end":170,"reference_id":"31165882","reference_source":"pmid","reference_html":"Disordered region of H3K9 methyltransferase Clr4 binds the nucleosome and contributes to its activity. <i> Akoury E, Ma G, Demolin S, Brönner C, Zocco M, Cirilo A, Ivic N, Halic M. </i> Nucleic Acids Res, 2019","date":"2024-11-01T17:39:56.076Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031491","term_name":"nucleosome binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"27905"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P62799","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P02281","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"P06898","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"A0A310TTQ1","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04255r004","statement":[{"text":"The interaction of the C-terminal α-helix of the chromodomain with the H3KC9me3 nucleosome is more extensive when the disordered region is present (Figure 2B and Supplementary Figure S2D), suggesting that the disordered region stabilizes the CD interaction with the core of the nucleosome (Supplementary Figure S4A and B).","type":"Results"},{"text":"Altogether, our data show that the disordered region tethers Clr4 CD to the nucleosome, and that CD interacts with the unmodified nucleosome in a similar way as with the H3KC9me3 nucleosome.","type":"Results"},{"text":"Moreover, we observe several interactions of the disordered region with the H3KC9me3 nucleosome. This includes the patches 113KKVFS117, 123RQSR126, 147TNSK150 and 164QKRELVS170 in the disordered region.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a nucleosome, a complex comprised of DNA wound around a multisubunit core and associated proteins, which forms the primary packing unit of DNA into higher order structures.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":164,"end":174,"reference_id":"31165882","reference_source":"pmid","reference_html":"Disordered region of H3K9 methyltransferase Clr4 binds the nucleosome and contributes to its activity. <i> Akoury E, Ma G, Demolin S, Brönner C, Zocco M, Cirilo A, Ivic N, Halic M. </i> Nucleic Acids Res, 2019","date":"2024-11-01T17:43:27.386Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"27905"},{"db":"BMRB","id":"27903"}],"region_id":"DP04255r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06898"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02281"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62799"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A310TTQ1"}],"statement":[{"text":"Notably, the propensity for secondary structure elements was visible at the intrinsically disordered region upon Clr4_1–191 binding to the H3KC9me3 nucleosome. The patch 113KKVFS117 incorporates the β-strand and 164QKRELVS174 shows features of an α-helix (Figure 2D).","type":"Results"},{"text":"Our data show that Clr4 binds the nucleosome with its disordered region independent of H3K9 methylation and this induces formation of an α-helix and β-sheet in this region.","type":"Results"},{"text":"Notably, we found the propensity for secondary structure elements in the intrinsically disordered region between S69 and S192 with β-sheet β4 (113KKVFS117) and α-helix α3 (164QKRELVS174). These data show that the nucleosome induces formation of secondary structure elements in the disordered region of Clr4 and these elements bind the core of the nucleosome (40–42).","type":"Discussion"}]},{"start":164,"end":170,"reference_id":"31165882","reference_source":"pmid","reference_html":"Disordered region of H3K9 methyltransferase Clr4 binds the nucleosome and contributes to its activity. <i> Akoury E, Ma G, Demolin S, Brönner C, Zocco M, Cirilo A, Ivic N, Halic M. </i> Nucleic Acids Res, 2019","date":"2024-11-01T18:07:38.144Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0046974","term_name":"histone methyltransferase activity (H3-K9 specific)","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00484","term_name":"deletion-insertion","term_namespace":"Protein mutation","value":"p.Gln164_Ser170delinsSerGlySerGlySerGlySer","start":null,"end":null,"position":null},{"term_id":"IDPO:00484","term_name":"deletion-insertion","term_namespace":"Protein mutation","value":"p.Thr147_Lys150delinsSerGlySerGly","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04255r006","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":null,"id":null}],"statement":[{"text":" We mutated two patches in the Clr4 disordered region that make contacts with the nucleosome in our NMR data. The patch 164QKRELVS170 in the clr4 gene was mutated to 164SGSGSGS170 and the patch 147TNSK150 to 147SGSG150, respectively, generating the MUT12 construct. We purified wild-type and mutant Clr4 and determined their methlytransferase activity by western blot (Supplementary Figure S7A). Our biochemical data show that mutations in these two patches reduced Clr4 interaction with the nucleosome and the methyltransferase activity (Figure 3A–C). This indicates that interaction of the disordered region with the nucleosome stabilizes Clr4 on the nucleosome and promotes H3K9 methylation.","type":"Results"},{"text":"This indicates that the interaction of Clr4 disordered region with the nucleosome increases efficiency and the kinetics of H3K9 methylation and heterochromatin establishment.","type":"Results"},{"text":"Taken together, our data show that in absence of H3K9 methylation, Clr4 disordered region binds the nucleosome which stabilizes the complex to deposit the initial H3K9 methylation. This interaction increases the efficiency of H3K9 methylation and heterochromatin establishment.","type":"Results"}],"term_comment":"","term_def":"\"Catalysis of the reaction: S-adenosyl-L-methionine + histone H3 L-lysine (position 9) = S-adenosyl-L-homocysteine + histone H3 N6-methyl-L-lysine (position 9). This reaction is the addition of a methyl group onto lysine at position 9 of the histone H3 protein.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":147,"end":151,"reference_id":"31165882","reference_source":"pmid","reference_html":"Disordered region of H3K9 methyltransferase Clr4 binds the nucleosome and contributes to its activity. <i> Akoury E, Ma G, Demolin S, Brönner C, Zocco M, Cirilo A, Ivic N, Halic M. </i> Nucleic Acids Res, 2019","date":"2024-11-01T18:08:20.652Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0046974","term_name":"histone methyltransferase activity (H3-K9 specific)","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00484","term_name":"deletion-insertion","term_namespace":"Protein mutation","value":"p.Gln164_Ser170delinsSerGlySerGlySerGlySer","start":null,"end":null,"position":null},{"term_id":"IDPO:00484","term_name":"deletion-insertion","term_namespace":"Protein mutation","value":"p.Thr147_Lys150delinsSerGlySerGly","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04255r007","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":null,"id":null}],"statement":[{"text":" We mutated two patches in the Clr4 disordered region that make contacts with the nucleosome in our NMR data. The patch 164QKRELVS170 in the clr4 gene was mutated to 164SGSGSGS170 and the patch 147TNSK150 to 147SGSG150, respectively, generating the MUT12 construct. We purified wild-type and mutant Clr4 and determined their methlytransferase activity by western blot (Supplementary Figure S7A). Our biochemical data show that mutations in these two patches reduced Clr4 interaction with the nucleosome and the methyltransferase activity (Figure 3A–C). This indicates that interaction of the disordered region with the nucleosome stabilizes Clr4 on the nucleosome and promotes H3K9 methylation.","type":"Results"},{"text":"This indicates that the interaction of Clr4 disordered region with the nucleosome increases efficiency and the kinetics of H3K9 methylation and heterochromatin establishment.","type":"Results"},{"text":"Taken together, our data show that in absence of H3K9 methylation, Clr4 disordered region binds the nucleosome which stabilizes the complex to deposit the initial H3K9 methylation. This interaction increases the efficiency of H3K9 methylation and heterochromatin establishment.","type":"Results"}],"term_comment":"","term_def":"\"Catalysis of the reaction: S-adenosyl-L-methionine + histone H3 L-lysine (position 9) = S-adenosyl-L-homocysteine + histone H3 N6-methyl-L-lysine (position 9). This reaction is the addition of a methyl group onto lysine at position 9 of the histone H3 protein.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":7,"released":"2025_06","sequence":"MSPKQEEYEVERIVDEKLDRNGAVKLYRIRWLNYSSRSDTWEPPENLSGCSAVLAEWKRRKRRLKGSNSDSDSPHHASNPHPNSRQKHQHQTSKSVPRSQRFSRELNVKKENKKVFSSQTTKRQSRKQSTALTTNDTSIILDDSLHTNSKKLGKTRNEVKEESQKRELVSNSIKEATSPKTSSILTKPRNPSKLDSYTHLSFYEKRELFRKKLREIEGPEVTLVNEVDDEPCPSLDFQFISQYRLTQGVIPPDPNFQSGCNCSSLGGCDLNNPSRCECLDDLDEPTHFAYDAQGRVRADTGAVIYECNSFCSCSMECPNRVVQRGRTLPLEIFKTKEKGWGVRSLRFAPAGTFITCYLGEVITSAEAAKRDKNYDDDGITYLFDLDMFDDASEYTVDAQNYGDVSRFFNHSCSPNIAIYSAVRNHGFRTIYDLAFFAIKDIQPLEELTFDYAGAKDFSPVQSQKSQQNRISKLRRQCKCGSANCRGWLFG","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"alphafold_very_low_content":0.3,"disorder_content":0.2510204081632653,"disprot_consensus":{"full":[{"start":69,"end":163,"type":"D"},{"start":164,"end":174,"type":"T"},{"start":175,"end":191,"type":"D"}],"Structural state":[{"start":69,"end":191,"type":"D"}],"Disorder function":[{"start":69,"end":191,"type":"F"}],"Molecular function":[{"start":69,"end":191,"type":"F"}],"Structural transition":[{"start":164,"end":174,"type":"T"}]}},{"disprot_id":"DP04256","acc":"P54820","creator":"vnugnes","date":"2024-11-04T17:59:42.272Z","features":{"pfam":[{"id":"PF00034","name":"Cytochrome c","start":81,"end":173}],"gene3D":[]},"genes":[{"name":{"value":"cycM"}}],"length":176,"name":"Cytochrome c-552","ncbi_taxon_id":266,"organism":"Paracoccus denitrificans","regions":[{"start":48,"end":69,"reference_id":"20606266","reference_source":"pmid","reference_html":"Structure at 1.5 A resolution of cytochrome c(552) with its flexible linker segment, a membrane-anchored protein from Paracoccus denitrificans. <i> Rajendran C, Ermler U, Ludwig B, Michel H. </i> Acta Crystallogr D Biol Crystallogr, 2010","date":"2024-11-04T18:25:03.374Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"3M97"}],"region_id":"DP04256r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"60562","entry_name":"ferroheme c"}],"statement":[{"text":"In the crystal structure this region is composed of an irregular segment containing residues 1–33 and a small α-helix (residues 34–41). The linker segment 13–32\nis essentially disordered in the electron density.","type":"Results"},{"text":"The region the authors report as 13-32, refers to the 48-69 region of the UniProt sequence.","type":"Curator statement"}]},{"start":38,"end":47,"reference_id":"20606266","reference_source":"pmid","reference_html":"Structure at 1.5 A resolution of cytochrome c(552) with its flexible linker segment, a membrane-anchored protein from Paracoccus denitrificans. <i> Rajendran C, Ermler U, Ludwig B, Michel H. </i> Acta Crystallogr D Biol Crystallogr, 2010","date":"2024-11-04T18:25:21.249Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"3M97"}],"region_id":"DP04256r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"60562","entry_name":"ferroheme c"}],"statement":[{"text":"In the crystal structure this region is composed of an irregular segment containing residues 1–33 and a small α-helix (residues 34–41). The linker segment 13–32\nis essentially disordered in the electron density. In contrast, residues 1–12 are clearly\nvisible in the electron-density map as they are artificially rigidified by a crystal contact to a neighbouring subunit mediated by Zn2+ ions (see x3.3). Therefore, we assume that in the cell the irregular segment is highly flexible as previously predicted by Berry & Trumpower (1985)","type":"Results"},{"text":"The region the authors report as 1-12, refers to the 38-47 region of the UniProt sequence. ","type":"Curator statement"}]},{"start":38,"end":69,"reference_id":"20606266","reference_source":"pmid","reference_html":"Structure at 1.5 A resolution of cytochrome c(552) with its flexible linker segment, a membrane-anchored protein from Paracoccus denitrificans. <i> Rajendran C, Ermler U, Ludwig B, Michel H. </i> Acta Crystallogr D Biol Crystallogr, 2010","date":"2024-11-04T18:24:20.718Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"3M97"}],"region_id":"DP04256r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"60562","entry_name":"ferroheme c"}],"statement":[{"text":"Residues 1–40 of fragment B link the globular cytochrome c domain and the N-terminal membrane anchor (the latter was absent in the construct used for crystallization).","type":"Results"},{"text":"In the crystal structure this region is composed of an irregular segment containing residues 1–33 and a small α-helix (residues 34–41). The linker segment 13–32\nis essentially disordered in the electron density. In contrast, residues 1–12 are clearly visible in the electron-density map as they are artificially rigidified by a crystal contact to a neighbouring subunit mediated by Zn2+ ions (see x3.3). Therefore, we assume that in the cell the irregular segment is highly flexible as previously predicted by Berry & Trumpower (1985).","type":"Results"},{"text":"The region the authors report as 1-40, refers to the 38-69 region of the UniProt sequence.","type":"Curator statement"}]}],"regions_counter":3,"released":"2025_06","sequence":"MFDTMTVTKAAGALIGSLLFLLLMSWAASGIFHVGTSGHGAEGEEHAQAYTYPVESAGGAEGEAVDEGPDFATVLASADPAAGEKVFGKCKACHKLDGNDGVGPHLNGVVGRTVAGVDGFNYSDPMKAHGGDWTPEALQEFLTNPKAVVKGTKMAFAGLPKIEDRANLIAYLEGQQ","taxonomy":["Bacteria","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Paracoccaceae","Paracoccus"],"alphafold_very_low_content":0.11931818181818182,"disorder_content":0.18181818181818182,"disprot_consensus":{"full":[{"start":38,"end":69,"type":"D"}],"Structural state":[{"start":38,"end":69,"type":"D"}],"Disorder function":[{"start":38,"end":69,"type":"F"}]}},{"disprot_id":"DP04257","acc":"Q9NZI8","creator":"zskalman","date":"2024-11-11T08:19:29.199Z","features":{"pfam":[{"id":"PF00013","name":"KH domain","start":198,"end":262},{"id":"PF00013","name":"KH domain","start":280,"end":344},{"id":"PF00013","name":"KH domain","start":408,"end":471},{"id":"PF00013","name":"KH domain","start":491,"end":555},{"id":"PF00076","name":"RNA recognition motif","start":4,"end":68},{"id":"PF00076","name":"RNA recognition motif","start":85,"end":150}],"gene3D":[]},"genes":[{"name":{"value":"IGF2BP1"},"synonyms":[{"value":"CRDBP"},{"value":"VICKZ1"},{"value":"ZBP1"}]}],"length":577,"name":"Insulin-like growth factor 2 mRNA-binding protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":157,"end":194,"reference_id":"39426983","reference_source":"pmid","reference_html":"IGF2BP1 phosphorylation in the disordered linkers regulates ribonucleoprotein condensate formation and RNA metabolism. <i> Hornegger H, Anisimova AS, Muratovic A, Bourgeois B, Spinetti E, Niedermoser I, Covino R, Madl T, Karagöz GE. </i> Nat Commun, 2024","date":"2024-11-11T08:31:26.370Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"52567"}],"region_id":"DP04257r001","statement":[{"text":"1H-15N Heteronuclear Single Quantum Coherence (HSQC) experiments revealed a small dispersion of backbone amide signals, thus validating the disordered nature of the linker segments (Supplementary Fig. 8A-D). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-11-11T16:41:14.783Z"}},{"start":344,"end":404,"reference_id":"39426983","reference_source":"pmid","reference_html":"IGF2BP1 phosphorylation in the disordered linkers regulates ribonucleoprotein condensate formation and RNA metabolism. <i> Hornegger H, Anisimova AS, Muratovic A, Bourgeois B, Spinetti E, Niedermoser I, Covino R, Madl T, Karagöz GE. </i> Nat Commun, 2024","date":"2024-11-12T07:44:48.713Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"52568"}],"region_id":"DP04257r002","statement":[{"text":"1H-15N Heteronuclear Single Quantum Coherence (HSQC) experiments revealed a small dispersion of backbone amide signals, thus validating the disordered nature of the linker segments (Supplementary Fig. 8A-D). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-04T14:40:02.318Z"}},{"start":179,"end":183,"reference_id":"39426983","reference_source":"pmid","reference_html":"IGF2BP1 phosphorylation in the disordered linkers regulates ribonucleoprotein condensate formation and RNA metabolism. <i> Hornegger H, Anisimova AS, Muratovic A, Bourgeois B, Spinetti E, Niedermoser I, Covino R, Madl T, Karagöz GE. </i> Nat Commun, 2024","date":"2024-11-11T16:08:45.702Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0062028","term_name":"regulation of stress granule assembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser181Glu","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04257r003","statement":[{"text":"Here, we map stress-regulated phosphorylation sites in IGF2BP1 by targeted mass spectrometry analyzes to uncover mechanisms that control IGF2BP1 outputs. Using in vitro reconstitution, biochemistry, and structural methods, we dissect how IGF2BP1 phosphorylation in its disordered linker regions regulates function. We show that phosphorylation of the disordered linkers regulates the propensity of IGF2BP1 to form RNP granules in vitro and in cells by modulating low affinity interaction networks.","type":"Results"},{"text":"Quantification of the IGF2BP1-RNA condensates (Supplementary Fig. 3A, see materials and methods) revealed that the average size of condensates and the total area of condensates formed by the S181E mutant were smaller compared to the wild-type IGF2BP1, indicating that the IGF2BP1 S181E mutant is impaired in condensate formation (Fig. 2H, J, Supplementary Fig. 4F-I, Supplementary Table 3, median area per condensate: wild-type: 7.0 µm, S181E: 5.7 µm, mean total area: wild-type: 7753 µm², S181E: 4691 µm², at 5 µM protein and RNA concentration).","type":"Results"},{"text":"IGF2BP1 is phosphorylated at Ser181 in response to proteotoxic stress. When this residue is replaced with a phosphomimetic mutant (Glu), the ability of IGF2BP1 to form condensates is impaired, indicating that stress-induced phosphorylation at this site regulates granule formation.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that modulates the rate, frequency or extent of stress granule assembly, the aggregation, arrangement and bonding together of proteins and RNA molecules to form a stress granule.\" [PMID:20180778]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"ENST00000216037","statements":[{"type":"Curator statement","text":"Interacting RNA sequence corresponding to 36 nt of the XBP1 human gene with sequence: GUGACAUGUCCUCUCUGCUUGGUGUAAACCAUUCUU"}]}]},{"start":394,"end":398,"reference_id":"39426983","reference_source":"pmid","reference_html":"IGF2BP1 phosphorylation in the disordered linkers regulates ribonucleoprotein condensate formation and RNA metabolism. <i> Hornegger H, Anisimova AS, Muratovic A, Bourgeois B, Spinetti E, Niedermoser I, Covino R, Madl T, Karagöz GE. </i> Nat Commun, 2024","date":"2024-11-11T16:12:43.728Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0062028","term_name":"regulation of stress granule assembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Tyr396Glu","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04257r004","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"ENST00000216037"}],"statement":[{"text":"Here, we map stress-regulated phosphorylation sites in IGF2BP1 by targeted mass spectrometry analyzes to uncover mechanisms that control IGF2BP1 outputs. Using in vitro reconstitution, biochemistry, and structural methods, we dissect how IGF2BP1 phosphorylation in its disordered linker regions regulates function. We show that phosphorylation of the disordered linkers regulates the propensity of IGF2BP1 to form RNP granules in vitro and in cells by modulating low affinity interaction networks.","type":"Results"},{"text":"Intriguingly, in contrast to the S181E mutant, the Y396E mutant formed larger condensates with a larger total area under the same experimental conditions (Fig. 2I, J, Supplementary Fig. 4 F, H, I, Supplementary Table 3, median area per droplet: Y396E 10.8 µm, mean total area: Y396E 9298 µm², at 5 µM protein and RNA concentration).","type":"Results"},{"text":"IGF2BP1 is phosphorylated at Tyr396 in response to proteotoxic stress. When this residue is replaced with a phosphomimetic mutant (Glu), the ability of IGF2BP1 to form condensates is affected, indicating that stress-induced phosphorylation at this site regulates granule formation","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that modulates the rate, frequency or extent of stress granule assembly, the aggregation, arrangement and bonding together of proteins and RNA molecules to form a stress granule.\" [PMID:20180778]","term_is_obsolete":false,"term_not_annotate":false},{"start":170,"end":175,"reference_id":"39426983","reference_source":"pmid","reference_html":"IGF2BP1 phosphorylation in the disordered linkers regulates ribonucleoprotein condensate formation and RNA metabolism. <i> Hornegger H, Anisimova AS, Muratovic A, Bourgeois B, Spinetti E, Niedermoser I, Covino R, Madl T, Karagöz GE. </i> Nat Commun, 2024","date":"2024-11-11T16:28:27.683Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP04257r005","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":"RNAcentral","id":"ENST00000216037"}],"statement":[{"text":"Linker 1 contains an RGG-RG motif which is in the vicinity of S181 that shows evolutionary conservation in mammals and some vertebrate species (Supplementary Fig. 1A). Therefore, we investigated whether linker 1 could contribute to protein-RNA interactions by measuring HSQC spectra of linker 1 in the presence of a model RNA (12xUG) that is recognized by RGG containing proteins through formation of an RNA quadruplex69 and a 10 nt RNA derived from XBP1. Titration of the wild-type linker 1 with the 12xUG RNA resulted in large chemical shift perturbations and a decrease in signal intensity of the residues around the RGG-RG motif (G170, G172 and G175, Fig. 5B-D and Supplementary Fig. 10J, K).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":179,"end":183,"reference_id":"39426983","reference_source":"pmid","reference_html":"IGF2BP1 phosphorylation in the disordered linkers regulates ribonucleoprotein condensate formation and RNA metabolism. <i> Hornegger H, Anisimova AS, Muratovic A, Bourgeois B, Spinetti E, Niedermoser I, Covino R, Madl T, Karagöz GE. </i> Nat Commun, 2024","date":"2024-11-11T16:31:48.299Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1905215","term_name":"negative regulation of RNA binding","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser181Glu","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04257r006","statement":[{"text":"Linker 1 contains an RGG-RG motif which is in the vicinity of S181 that shows evolutionary conservation in mammals and some vertebrate species (Supplementary Fig. 1A). Therefore, we investigated whether linker 1 could contribute to protein-RNA interactions by measuring HSQC spectra of linker 1 in the presence of a model RNA (12xUG) that is recognized by RGG containing proteins through formation of an RNA quadruplex69 and a 10 nt RNA derived from XBP1. Titration of the wild-type linker 1 with the 12xUG RNA resulted in large chemical shift perturbations and a decrease in signal intensity of the residues around the RGG-RG motif (G170, G172 and G175, Fig. 5B-D and Supplementary Fig. 10J, K).","type":"Results"},{"text":"Notably, the linker 1 phosphomimetic mutant S181E was impaired in binding to RNA, evident in lower CSPs and a lower drop in the signal intensity around the phosphorylation site upon its titration with the 12xUG RNA.","type":"Results"},{"text":"The NMR data revealed that while linker 1 binds to RNA, linker 2 forms low-affinity interactions with the folded domains in IGF2BP1, and both interactions are modulated in the relevant phosphomimetic mutants.","type":"Results"},{"text":"This evidence indicates the phosphorylated version of this region regulates negatively the RNA association. ","type":"Curator statement"}],"term_comment":"","term_def":"\"Any process that stops, prevents or reduces the frequency, rate or extent of RNA binding.\" [GO_REF:0000059, GOC:bf, GOC:PARL, GOC:TermGenie]","term_is_obsolete":false,"term_not_annotate":false},{"start":388,"end":395,"reference_id":"39426983","reference_source":"pmid","reference_html":"IGF2BP1 phosphorylation in the disordered linkers regulates ribonucleoprotein condensate formation and RNA metabolism. <i> Hornegger H, Anisimova AS, Muratovic A, Bourgeois B, Spinetti E, Niedermoser I, Covino R, Madl T, Karagöz GE. </i> Nat Commun, 2024","date":"2024-11-11T16:34:46.475Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000060","term_name":"self-assembly","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04257r007","statement":[{"text":"The NMR analyzes revealed that titration of wild-type linker 2 with RRM1-2 as well as the KH1-2 domains showed small CSPs around aa S388-P395 (aa 388-SSVTGAP-395) (CSP > 0.015) (Supplementary Fig. 11A-F) indicating that linker 2 interacts with these domains with a low affinity in the millimolar range.","type":"Results"},{"text":"Titration of linker 2 with KH3-4 domains displayed the largest CSPs observed for all folded domains, revealing that linker 2 most strongly interacts with KH3-4 dimers (Fig. 5E-G, Supplementary Fig. 11G-H).","type":"Results"},{"text":"The NMR data revealed that while linker 1 binds to RNA, linker 2 forms low-affinity interactions with the folded domains in IGF2BP1, and both interactions are modulated in the relevant phosphomimetic mutants.","type":"Results"}]},{"start":179,"end":183,"reference_id":"39426983","reference_source":"pmid","reference_html":"IGF2BP1 phosphorylation in the disordered linkers regulates ribonucleoprotein condensate formation and RNA metabolism. <i> Hornegger H, Anisimova AS, Muratovic A, Bourgeois B, Spinetti E, Niedermoser I, Covino R, Madl T, Karagöz GE. </i> Nat Commun, 2024","date":"2024-11-11T16:39:19.512Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04257r008","statement":[{"text":"The identified phosphopeptides mapped to the RRM1 domain (aa S73), disordered linker 1 (aa S181), KH1 (aa T249), KH2 and KH3 domains (aa S436, S438, T446) (Fig. 1C, Supplementary Fig. 1B).","type":"Results"}]},{"start":394,"end":398,"reference_id":"39426983","reference_source":"pmid","reference_html":"IGF2BP1 phosphorylation in the disordered linkers regulates ribonucleoprotein condensate formation and RNA metabolism. <i> Hornegger H, Anisimova AS, Muratovic A, Bourgeois B, Spinetti E, Niedermoser I, Covino R, Madl T, Karagöz GE. </i> Nat Commun, 2024","date":"2024-11-11T16:41:07.550Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04257r009","statement":[{"text":"In line with the published results7, we detected phosphorylation of the recombinant IGF2BP1 at Y396 by the Src kinase in vitro.","type":"Results"}]},{"start":157,"end":194,"reference_id":"39426983","reference_source":"pmid","reference_html":"IGF2BP1 phosphorylation in the disordered linkers regulates ribonucleoprotein condensate formation and RNA metabolism. <i> Hornegger H, Anisimova AS, Muratovic A, Bourgeois B, Spinetti E, Niedermoser I, Covino R, Madl T, Karagöz GE. </i> Nat Commun, 2024","date":"2024-11-11T16:42:21.652Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"52567"}],"region_id":"DP04257r010","statement":[{"text":"1H-15N Heteronuclear Single Quantum Coherence (HSQC) experiments revealed a small dispersion of backbone amide signals, thus validating the disordered nature of the linker segments (Supplementary Fig. 8A-D).","type":"Results"}]},{"start":344,"end":404,"reference_id":"39426983","reference_source":"pmid","reference_html":"IGF2BP1 phosphorylation in the disordered linkers regulates ribonucleoprotein condensate formation and RNA metabolism. <i> Hornegger H, Anisimova AS, Muratovic A, Bourgeois B, Spinetti E, Niedermoser I, Covino R, Madl T, Karagöz GE. </i> Nat Commun, 2024","date":"2024-11-11T16:45:30.296Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"52568"}],"region_id":"DP04257r011","statement":[{"text":"1H-15N Heteronuclear Single Quantum Coherence (HSQC) experiments revealed a small dispersion of backbone amide signals, thus validating the disordered nature of the linker segments (Supplementary Fig. 8A-D).","type":"Results"}]}],"regions_counter":11,"released":"2025_06","sequence":"MNKLYIGNLNESVTPADLEKVFAEHKISYSGQFLVKSGYAFVDCPDEHWAMKAIETFSGKVELQGKRLEIEHSVPKKQRSRKIQIRNIPPQLRWEVLDSLLAQYGTVENCEQVNTESETAVVNVTYSNREQTRQAIMKLNGHQLENHALKVSYIPDEQIAQGPENGRRGGFGSRGQPRQGSPVAAGAPAKQQQVDIPLRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAAEKAISVHSTPEGCSSACKMILEIMHKEAKDTKTADEVPLKILAHNNFVGRLIGKEGRNLKKVEQDTETKITISSLQDLTLYNPERTITVKGAIENCCRAEQEIMKKVREAYENDVAAMSLQSHLIPGLNLAAVGLFPASSSAVPPPPSSVTGAAPYSSFMQAPEQEMVQVFIPAQAVGAIIGKKGQHIKQLSRFASASIKIAPPETPDSKVRMVIITGPPEAQFKAQGRIYGKLKEENFFGPKEEVKLETHIRVPASAAGRVIGKGGKTVNELQNLTAAEVVVPRDQTPDENDQVIVKIIGHFYASQMAQRKIRDILAQVKQQHQKGQSNQAQARRK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.12998266897746968,"dataset":["RNA-binding proteins","Condensates-related proteins"],"disorder_content":0.17157712305025996,"disprot_consensus":{"full":[{"start":157,"end":194,"type":"D"},{"start":344,"end":404,"type":"D"}],"Structural state":[{"start":157,"end":194,"type":"D"},{"start":344,"end":404,"type":"D"}],"Biological process":[{"start":179,"end":183,"type":"F"},{"start":394,"end":398,"type":"F"}],"Molecular function":[{"start":170,"end":175,"type":"F"}],"Disorder function":[{"start":157,"end":194,"type":"F"},{"start":344,"end":404,"type":"F"}]}},{"disprot_id":"DP04258","acc":"Q15022","creator":"zskalman","date":"2024-11-11T10:00:29.286Z","features":{"pfam":[{"id":"PF09733","name":"VEFS-Box of polycomb protein","start":553,"end":672},{"id":"PF23320","name":"Polycomb protein SUZ12-like, Zn domain","start":427,"end":494}],"gene3D":[]},"genes":[{"name":{"value":"SUZ12"},"synonyms":[{"value":"CHET9"},{"value":"JJAZ1"},{"value":"KIAA0160"}]}],"length":739,"name":"Polycomb protein SUZ12","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":168,"end":181,"reference_id":"29499137","reference_source":"pmid","reference_html":"Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for Chromatin Binding. <i> Chen S, Jiao L, Shubbar M, Yang X, Liu X. </i> Mol Cell, 2018","date":"2025-04-02T09:04:17.285Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"5WAI"}],"region_id":"DP04258r001","statement":[{"text":"The L1, L3, L5, and L7 loops on the distal side away from Rbbp4 are all disordered, implicating that they may be involved in other functions (Fig. 3D).","type":"Results"}],"construct_alterations":[{"term_id":"MI:0988","term_name":"STREP","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"sequence_construct":"MEHVQADHELFLQAFEKPTQIYRFLRTRNLIAPIFLHRTLTYMSHRNSRTNIKRKTFKVDDMLSKVEKMKGEQESHSLSAHLQLTFTGFFHKNDKPSPNSENEQNSVTLEVLLVKVCHKKRKDVSCPIRQVPTGKKQVPLNPDLNQTKPGNFPSLAVSSNEFEPSNSHMVKSYSLLFRVTRPGRREFNGMINGETNENIDVNEELPARRKRNREDGEKTFVAQMTVFDKNRRLQLLDGEYEVAMQEMEECPISKKRATWETILDGKRLPPFETFSQGPTLQFTLRWTGETNDKSTAPIAKPLATRNSESLHQENKPGSVKPTQTIAVKESLTTDLQTRKEKDTPNENRQKLRIFYQFLYNNNTRQQTEARDDLHCPWCTLNCRKLYSLLKHLKLCHSRFIFNYVYHPKGARIDVSINECYDGSYAGNPQDIHRQPGFAFSRNGPVKRTPITHILVCRPKRTKASMSEFLEWSHPQFEK","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"32051"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92833"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6ZN18"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09028"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-04-02T18:41:15.583Z"}},{"start":256,"end":293,"reference_id":"29499137","reference_source":"pmid","reference_html":"Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for Chromatin Binding. <i> Chen S, Jiao L, Shubbar M, Yang X, Liu X. </i> Mol Cell, 2018","date":"2025-04-02T09:04:55.207Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"5WAI"}],"region_id":"DP04258r002","statement":[{"text":"The L1, L3, L5, and L7 loops on the distal side away from Rbbp4 are all disordered, implicating that they may be involved in other functions (Fig. 3D).","type":"Results"}],"construct_alterations":[{"term_id":"MI:0988","term_name":"STREP","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"sequence_construct":"MEHVQADHELFLQAFEKPTQIYRFLRTRNLIAPIFLHRTLTYMSHRNSRTNIKRKTFKVDDMLSKVEKMKGEQESHSLSAHLQLTFTGFFHKNDKPSPNSENEQNSVTLEVLLVKVCHKKRKDVSCPIRQVPTGKKQVPLNPDLNQTKPGNFPSLAVSSNEFEPSNSHMVKSYSLLFRVTRPGRREFNGMINGETNENIDVNEELPARRKRNREDGEKTFVAQMTVFDKNRRLQLLDGEYEVAMQEMEECPISKKRATWETILDGKRLPPFETFSQGPTLQFTLRWTGETNDKSTAPIAKPLATRNSESLHQENKPGSVKPTQTIAVKESLTTDLQTRKEKDTPNENRQKLRIFYQFLYNNNTRQQTEARDDLHCPWCTLNCRKLYSLLKHLKLCHSRFIFNYVYHPKGARIDVSINECYDGSYAGNPQDIHRQPGFAFSRNGPVKRTPITHILVCRPKRTKASMSEFLEWSHPQFEK","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"32051"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92833"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6ZN18"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09028"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-04-02T18:41:20.879Z"}},{"start":323,"end":350,"reference_id":"29499137","reference_source":"pmid","reference_html":"Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for Chromatin Binding. <i> Chen S, Jiao L, Shubbar M, Yang X, Liu X. </i> Mol Cell, 2018","date":"2025-04-02T09:05:14.278Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"5WAI"}],"region_id":"DP04258r003","statement":[{"text":"The L1, L3, L5, and L7 loops on the distal side away from Rbbp4 are all disordered, implicating that they may be involved in other functions (Fig. 3D).","type":"Results"}],"construct_alterations":[{"term_id":"MI:0988","term_name":"STREP","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"sequence_construct":"MEHVQADHELFLQAFEKPTQIYRFLRTRNLIAPIFLHRTLTYMSHRNSRTNIKRKTFKVDDMLSKVEKMKGEQESHSLSAHLQLTFTGFFHKNDKPSPNSENEQNSVTLEVLLVKVCHKKRKDVSCPIRQVPTGKKQVPLNPDLNQTKPGNFPSLAVSSNEFEPSNSHMVKSYSLLFRVTRPGRREFNGMINGETNENIDVNEELPARRKRNREDGEKTFVAQMTVFDKNRRLQLLDGEYEVAMQEMEECPISKKRATWETILDGKRLPPFETFSQGPTLQFTLRWTGETNDKSTAPIAKPLATRNSESLHQENKPGSVKPTQTIAVKESLTTDLQTRKEKDTPNENRQKLRIFYQFLYNNNTRQQTEARDDLHCPWCTLNCRKLYSLLKHLKLCHSRFIFNYVYHPKGARIDVSINECYDGSYAGNPQDIHRQPGFAFSRNGPVKRTPITHILVCRPKRTKASMSEFLEWSHPQFEK","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"32051"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92833"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6ZN18"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09028"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-04-02T18:42:15.037Z"}},{"start":364,"end":422,"reference_id":"29499137","reference_source":"pmid","reference_html":"Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for Chromatin Binding. <i> Chen S, Jiao L, Shubbar M, Yang X, Liu X. </i> Mol Cell, 2018","date":"2025-04-02T09:07:21.838Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"5WAI"}],"region_id":"DP04258r004","statement":[{"text":"The L1, L3, L5, and L7 loops on the distal side away from Rbbp4 are all disordered, implicating that they may be involved in other functions (Fig. 3D).","type":"Results"}],"construct_alterations":[{"term_id":"MI:0988","term_name":"STREP","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"sequence_construct":"MEHVQADHELFLQAFEKPTQIYRFLRTRNLIAPIFLHRTLTYMSHRNSRTNIKRKTFKVDDMLSKVEKMKGEQESHSLSAHLQLTFTGFFHKNDKPSPNSENEQNSVTLEVLLVKVCHKKRKDVSCPIRQVPTGKKQVPLNPDLNQTKPGNFPSLAVSSNEFEPSNSHMVKSYSLLFRVTRPGRREFNGMINGETNENIDVNEELPARRKRNREDGEKTFVAQMTVFDKNRRLQLLDGEYEVAMQEMEECPISKKRATWETILDGKRLPPFETFSQGPTLQFTLRWTGETNDKSTAPIAKPLATRNSESLHQENKPGSVKPTQTIAVKESLTTDLQTRKEKDTPNENRQKLRIFYQFLYNNNTRQQTEARDDLHCPWCTLNCRKLYSLLKHLKLCHSRFIFNYVYHPKGARIDVSINECYDGSYAGNPQDIHRQPGFAFSRNGPVKRTPITHILVCRPKRTKASMSEFLEWSHPQFEK","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"32051"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92833"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6ZN18"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09028"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-04-02T18:41:49.765Z"}},{"start":497,"end":513,"reference_id":"29499137","reference_source":"pmid","reference_html":"Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for Chromatin Binding. <i> Chen S, Jiao L, Shubbar M, Yang X, Liu X. </i> Mol Cell, 2018","date":"2025-04-02T09:08:01.952Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"5WAI"}],"region_id":"DP04258r005","statement":[{"text":"The L1, L3, L5, and L7 loops on the distal side away from Rbbp4 are all disordered, implicating that they may be involved in other functions (Fig. 3D).","type":"Results"}],"construct_alterations":[{"term_id":"MI:0988","term_name":"STREP","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"sequence_construct":"MEHVQADHELFLQAFEKPTQIYRFLRTRNLIAPIFLHRTLTYMSHRNSRTNIKRKTFKVDDMLSKVEKMKGEQESHSLSAHLQLTFTGFFHKNDKPSPNSENEQNSVTLEVLLVKVCHKKRKDVSCPIRQVPTGKKQVPLNPDLNQTKPGNFPSLAVSSNEFEPSNSHMVKSYSLLFRVTRPGRREFNGMINGETNENIDVNEELPARRKRNREDGEKTFVAQMTVFDKNRRLQLLDGEYEVAMQEMEECPISKKRATWETILDGKRLPPFETFSQGPTLQFTLRWTGETNDKSTAPIAKPLATRNSESLHQENKPGSVKPTQTIAVKESLTTDLQTRKEKDTPNENRQKLRIFYQFLYNNNTRQQTEARDDLHCPWCTLNCRKLYSLLKHLKLCHSRFIFNYVYHPKGARIDVSINECYDGSYAGNPQDIHRQPGFAFSRNGPVKRTPITHILVCRPKRTKASMSEFLEWSHPQFEK","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"32051"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92833"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6ZN18"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09028"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-04-02T18:41:30.949Z"}},{"start":150,"end":188,"reference_id":"29499137","reference_source":"pmid","reference_html":"Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for Chromatin Binding. <i> Chen S, Jiao L, Shubbar M, Yang X, Liu X. </i> Mol Cell, 2018","date":"2024-11-12T13:42:10.223Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0988","term_name":"STREP","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"PDB","id":"5WAK"}],"region_id":"DP04258r006","sequence_construct":"MEHVQADHELFLQAFEKPTQIYRFLRTRNLIAPIFLHRTLTYMSHRNSRTNIKRKTFKVDDMLSKVEKMKGEQESHSLSAHLQLTFTGFFHKNDKPSPNSENEQNSVTLEVLLVKVCHKKRKDVSCPIRQVPTGKKQVPLNPDLNQTKPGNFPSLAVSSNEFEPSNSHMVKSYSLLFRVTRPGRREFNGMINGETNENIDVNEELPARRKRNREDGEKTFVAQMTVFDKNRRLQLLDGEYEVAMQEMEECPISKKRATWETILDGKRLPPFETFSQGPTLQFTLRWTGETNDKSTAPIAKPLATRNSESLHQENKPGSVKPTQTIAVKESLTTDLQTRKEKDTPNENRQKLRIFYQFLYNNNTRQQTEARDDLHCPWCTLNCRKLYSLLKHLKLCHSRFIFNYVYHPKGARIDVSINECYDGSYAGNPQDIHRQPGFAFSRNGPVKRTPITHILVCRPKRTKASMSEFLEWSHPQFEK","statement":[{"text":"Missing electron density for the region.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"29105"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09028"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-04-02T18:41:27.579Z"}},{"start":201,"end":241,"reference_id":"29499137","reference_source":"pmid","reference_html":"Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for Chromatin Binding. <i> Chen S, Jiao L, Shubbar M, Yang X, Liu X. </i> Mol Cell, 2018","date":"2025-04-02T09:08:50.419Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0988","term_name":"STREP","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"PDB","id":"5WAK"}],"region_id":"DP04258r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"32051"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09028"}],"sequence_construct":"MEHVQADHELFLQAFEKPTQIYRFLRTRNLIAPIFLHRTLTYMSHRNSRTNIKRKTFKVDDMLSKVEKMKGEQESHSLSAHLQLTFTGFFHKNDKPSPNSENEQNSVTLEVLLVKVCHKKRKDVSCPIRQVPTGKKQVPLNPDLNQTKPGNFPSLAVSSNEFEPSNSHMVKSYSLLFRVTRPGRREFNGMINGETNENIDVNEELPARRKRNREDGEKTFVAQMTVFDKNRRLQLLDGEYEVAMQEMEECPISKKRATWETILDGKRLPPFETFSQGPTLQFTLRWTGETNDKSTAPIAKPLATRNSESLHQENKPGSVKPTQTIAVKESLTTDLQTRKEKDTPNENRQKLRIFYQFLYNNNTRQQTEARDDLHCPWCTLNCRKLYSLLKHLKLCHSRFIFNYVYHPKGARIDVSINECYDGSYAGNPQDIHRQPGFAFSRNGPVKRTPITHILVCRPKRTKASMSEFLEWSHPQFEK","statement":[{"text":"Missing electron density for the region.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-04-02T18:40:52.010Z"}},{"start":251,"end":367,"reference_id":"29499137","reference_source":"pmid","reference_html":"Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for Chromatin Binding. <i> Chen S, Jiao L, Shubbar M, Yang X, Liu X. </i> Mol Cell, 2018","date":"2025-04-02T09:11:00.563Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0988","term_name":"STREP","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"PDB","id":"5WAK"}],"region_id":"DP04258r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"32051"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09028"}],"sequence_construct":"MEHVQADHELFLQAFEKPTQIYRFLRTRNLIAPIFLHRTLTYMSHRNSRTNIKRKTFKVDDMLSKVEKMKGEQESHSLSAHLQLTFTGFFHKNDKPSPNSENEQNSVTLEVLLVKVCHKKRKDVSCPIRQVPTGKKQVPLNPDLNQTKPGNFPSLAVSSNEFEPSNSHMVKSYSLLFRVTRPGRREFNGMINGETNENIDVNEELPARRKRNREDGEKTFVAQMTVFDKNRRLQLLDGEYEVAMQEMEECPISKKRATWETILDGKRLPPFETFSQGPTLQFTLRWTGETNDKSTAPIAKPLATRNSESLHQENKPGSVKPTQTIAVKESLTTDLQTRKEKDTPNENRQKLRIFYQFLYNNNTRQQTEARDDLHCPWCTLNCRKLYSLLKHLKLCHSRFIFNYVYHPKGARIDVSINECYDGSYAGNPQDIHRQPGFAFSRNGPVKRTPITHILVCRPKRTKASMSEFLEWSHPQFEK","statement":[{"text":"Missing electron density for the region.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-04-02T18:40:55.573Z"}},{"start":380,"end":423,"reference_id":"29499137","reference_source":"pmid","reference_html":"Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for Chromatin Binding. <i> Chen S, Jiao L, Shubbar M, Yang X, Liu X. </i> Mol Cell, 2018","date":"2025-04-02T09:08:38.904Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0988","term_name":"STREP","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"PDB","id":"5WAK"}],"region_id":"DP04258r009","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"32051"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09028"}],"sequence_construct":"MEHVQADHELFLQAFEKPTQIYRFLRTRNLIAPIFLHRTLTYMSHRNSRTNIKRKTFKVDDMLSKVEKMKGEQESHSLSAHLQLTFTGFFHKNDKPSPNSENEQNSVTLEVLLVKVCHKKRKDVSCPIRQVPTGKKQVPLNPDLNQTKPGNFPSLAVSSNEFEPSNSHMVKSYSLLFRVTRPGRREFNGMINGETNENIDVNEELPARRKRNREDGEKTFVAQMTVFDKNRRLQLLDGEYEVAMQEMEECPISKKRATWETILDGKRLPPFETFSQGPTLQFTLRWTGETNDKSTAPIAKPLATRNSESLHQENKPGSVKPTQTIAVKESLTTDLQTRKEKDTPNENRQKLRIFYQFLYNNNTRQQTEARDDLHCPWCTLNCRKLYSLLKHLKLCHSRFIFNYVYHPKGARIDVSINECYDGSYAGNPQDIHRQPGFAFSRNGPVKRTPITHILVCRPKRTKASMSEFLEWSHPQFEK","statement":[{"text":"Missing electron density for the region.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-04-02T18:40:48.307Z"}},{"start":497,"end":510,"reference_id":"29499137","reference_source":"pmid","reference_html":"Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for Chromatin Binding. <i> Chen S, Jiao L, Shubbar M, Yang X, Liu X. </i> Mol Cell, 2018","date":"2025-04-02T09:08:27.481Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0988","term_name":"STREP","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"PDB","id":"5WAK"}],"region_id":"DP04258r010","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"32051"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09028"}],"sequence_construct":"MEHVQADHELFLQAFEKPTQIYRFLRTRNLIAPIFLHRTLTYMSHRNSRTNIKRKTFKVDDMLSKVEKMKGEQESHSLSAHLQLTFTGFFHKNDKPSPNSENEQNSVTLEVLLVKVCHKKRKDVSCPIRQVPTGKKQVPLNPDLNQTKPGNFPSLAVSSNEFEPSNSHMVKSYSLLFRVTRPGRREFNGMINGETNENIDVNEELPARRKRNREDGEKTFVAQMTVFDKNRRLQLLDGEYEVAMQEMEECPISKKRATWETILDGKRLPPFETFSQGPTLQFTLRWTGETNDKSTAPIAKPLATRNSESLHQENKPGSVKPTQTIAVKESLTTDLQTRKEKDTPNENRQKLRIFYQFLYNNNTRQQTEARDDLHCPWCTLNCRKLYSLLKHLKLCHSRFIFNYVYHPKGARIDVSINECYDGSYAGNPQDIHRQPGFAFSRNGPVKRTPITHILVCRPKRTKASMSEFLEWSHPQFEK","statement":[{"text":"Missing electron density for the region.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-04-02T18:41:23.343Z"}},{"start":201,"end":241,"reference_id":"29499137","reference_source":"pmid","reference_html":"Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for Chromatin Binding. <i> Chen S, Jiao L, Shubbar M, Yang X, Liu X. </i> Mol Cell, 2018","date":"2025-04-02T09:08:17.013Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0988","term_name":"STREP","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"PDB","id":"5WAI"}],"region_id":"DP04258r011","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"32051"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92833"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6ZN18"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09028"}],"sequence_construct":"MEHVQADHELFLQAFEKPTQIYRFLRTRNLIAPIFLHRTLTYMSHRNSRTNIKRKTFKVDDMLSKVEKMKGEQESHSLSAHLQLTFTGFFHKNDKPSPNSENEQNSVTLEVLLVKVCHKKRKDVSCPIRQVPTGKKQVPLNPDLNQTKPGNFPSLAVSSNEFEPSNSHMVKSYSLLFRVTRPGRREFNGMINGETNENIDVNEELPARRKRNREDGEKTFVAQMTVFDKNRRLQLLDGEYEVAMQEMEECPISKKRATWETILDGKRLPPFETFSQGPTLQFTLRWTGETNDKSTAPIAKPLATRNSESLHQENKPGSVKPTQTIAVKESLTTDLQTRKEKDTPNENRQKLRIFYQFLYNNNTRQQTEARDDLHCPWCTLNCRKLYSLLKHLKLCHSRFIFNYVYHPKGARIDVSINECYDGSYAGNPQDIHRQPGFAFSRNGPVKRTPITHILVCRPKRTKASMSEFLEWSHPQFEK","statement":[{"text":"Comparing the two structures, an additional domain of Suz12 becomes better ordered in S12R4J2A2 due to Aebp2 binding (Fig. 1 and S1A).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-04-02T18:40:43.711Z"}},{"start":201,"end":241,"reference_id":"29499137","reference_source":"pmid","reference_html":"Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for Chromatin Binding. <i> Chen S, Jiao L, Shubbar M, Yang X, Liu X. </i> Mol Cell, 2018","date":"2025-04-02T09:04:32.288Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0988","term_name":"STREP","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"PDB","id":"5WAI"},{"db":"PDB","id":"5WAK"}],"region_id":"DP04258r012","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"32051"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92833"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6ZN18"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q09028"}],"sequence_construct":"MEHVQADHELFLQAFEKPTQIYRFLRTRNLIAPIFLHRTLTYMSHRNSRTNIKRKTFKVDDMLSKVEKMKGEQESHSLSAHLQLTFTGFFHKNDKPSPNSENEQNSVTLEVLLVKVCHKKRKDVSCPIRQVPTGKKQVPLNPDLNQTKPGNFPSLAVSSNEFEPSNSHMVKSYSLLFRVTRPGRREFNGMINGETNENIDVNEELPARRKRNREDGEKTFVAQMTVFDKNRRLQLLDGEYEVAMQEMEECPISKKRATWETILDGKRLPPFETFSQGPTLQFTLRWTGETNDKSTAPIAKPLATRNSESLHQENKPGSVKPTQTIAVKESLTTDLQTRKEKDTPNENRQKLRIFYQFLYNNNTRQQTEARDDLHCPWCTLNCRKLYSLLKHLKLCHSRFIFNYVYHPKGARIDVSINECYDGSYAGNPQDIHRQPGFAFSRNGPVKRTPITHILVCRPKRTKASMSEFLEWSHPQFEK","statement":[{"text":"Comparing the two structures, an additional domain of Suz12 becomes better ordered in S12R4J2A2 due to Aebp2 binding (Fig. 1 and S1A).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-04-02T18:41:10.240Z"}}],"regions_counter":12,"released":"2025_06","sequence":"MAPQKHGGGGGGGSGPSAGSGGGGFGGSAAVAAATASGGKSGGGSCGGGGSYSASSSSSAAAAAGAAVLPVKKPKMEHVQADHELFLQAFEKPTQIYRFLRTRNLIAPIFLHRTLTYMSHRNSRTNIKRKTFKVDDMLSKVEKMKGEQESHSLSAHLQLTFTGFFHKNDKPSPNSENEQNSVTLEVLLVKVCHKKRKDVSCPIRQVPTGKKQVPLNPDLNQTKPGNFPSLAVSSNEFEPSNSHMVKSYSLLFRVTRPGRREFNGMINGETNENIDVNEELPARRKRNREDGEKTFVAQMTVFDKNRRLQLLDGEYEVAMQEMEECPISKKRATWETILDGKRLPPFETFSQGPTLQFTLRWTGETNDKSTAPIAKPLATRNSESLHQENKPGSVKPTQTIAVKESLTTDLQTRKEKDTPNENRQKLRIFYQFLYNNNTRQQTEARDDLHCPWCTLNCRKLYSLLKHLKLCHSRFIFNYVYHPKGARIDVSINECYDGSYAGNPQDIHRQPGFAFSRNGPVKRTPITHILVCRPKRTKASMSEFLESEDGEVEQQRTYSSGHNRLYFHSDTCLPLRPQEMEVDSEDEKDPEWLREKTITQIEEFSDVNEGEKEVMKLWNLHVMKHGFIADNQMNHACMLFVENYGQKIIKKNLCRNFMLHLVSMHDFNLISIMSIDKAVTKLREMQQKLEKGESASPANEEITEEQNGTANGFSEINSKEKALETDSVSGVSKQSKKQKL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.3125845737483085,"dataset":["Cancer-related proteins","NDDs-related proteins","RNA-binding proteins"],"disorder_content":0.36535859269282817,"disprot_consensus":{"full":[{"start":150,"end":188,"type":"D"},{"start":201,"end":241,"type":"T"},{"start":251,"end":423,"type":"D"},{"start":497,"end":513,"type":"D"}],"Structural state":[{"start":150,"end":188,"type":"D"},{"start":201,"end":241,"type":"D"},{"start":251,"end":423,"type":"D"},{"start":497,"end":513,"type":"D"}],"Structural transition":[{"start":201,"end":241,"type":"T"}]}},{"disprot_id":"DP04259","acc":"Q9H9Q4","creator":"zskalman","date":"2024-11-11T12:00:32.549Z","features":{"pfam":[{"id":"PF09302","name":"XLF N-terminal domain","start":12,"end":124},{"id":"PF21928","name":"XLF protein coiled-coil region","start":127,"end":174}],"gene3D":[]},"genes":[{"name":{"value":"NHEJ1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"17191205","url":"http://www.ncbi.nlm.nih.gov/pubmed/17191205","alternativeUrl":"https://europepmc.org/abstract/MED/17191205"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:25737","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:25737"}}]},"synonyms":[{"value":"XLF","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16439205","url":"http://www.ncbi.nlm.nih.gov/pubmed/16439205","alternativeUrl":"https://europepmc.org/abstract/MED/16439205"}}]}]}],"length":299,"name":"Non-homologous end-joining factor 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":229,"end":299,"reference_id":"38898102","reference_source":"pmid","reference_html":"Multivalent interactions of the disordered regions of XLF and XRCC4 foster robust cellular NHEJ and drive the formation of ligation-boosting condensates in vitro. <i> Vu DD, Bonucci A, Brenière M, Cisneros-Aguirre M, Pelupessy P, Wang Z, Carlier L, Bouvignies G, Cortes P, Aggarwal AK, Blackledge M, Gueroui Z, Belle V, Stark JM, Modesti M, Ferrage F. </i> Nat Struct Mol Biol, 2024","date":"2024-11-11T12:13:33.351Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"52387"}],"region_id":"DP04259r001","statement":[{"text":"1H chemical shift dispersion, secondary structural propensity, 15N–{1H} heteronuclear nuclear Overhauser effect (hNOE) and small-angle X-ray scattering (SAXS) experiments jointly indicated the lack of stable secondary structure elements in the XLFCTR either alone or in the context of the full-length protein construct (Supplementary Fig. 3a,b and Extended Data Fig. 2), defining it as an intrinsically disordered region (IDR).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-11-11T14:03:49.402Z"}},{"start":295,"end":299,"reference_id":"38898102","reference_source":"pmid","reference_html":"Multivalent interactions of the disordered regions of XLF and XRCC4 foster robust cellular NHEJ and drive the formation of ligation-boosting condensates in vitro. <i> Vu DD, Bonucci A, Brenière M, Cisneros-Aguirre M, Pelupessy P, Wang Z, Carlier L, Bouvignies G, Cortes P, Aggarwal AK, Blackledge M, Gueroui Z, Belle V, Stark JM, Modesti M, Ferrage F. </i> Nat Struct Mol Biol, 2024","date":"2025-04-02T08:59:37.996Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP04259r002","statement":[{"text":" We titrated 15N XLFCTR with the Ku80 von Willebrand domain (Ku80vWA) and observed that XLF–Ku interactions mainly involved the residue K293 and the last five residues (295RGLFS299), with notable chemical shift perturbations (CSPs) and peaks in the slow exchange regime, while residues 283–292 were only slightly perturbed upon binding to Ku80vWA (Fig. 2c,d).","type":"Results"},{"text":"Altogether, we show that the disordered CTR of XLF is an interaction hub, which binds weakly to Ku, DNA, LIG4 and the folded domain of XLF in an intramolecular or intermolecular fashion. ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"P13010","operator":"and","partner_start":253,"partner_end":452},{"db":"UniProt","id":"P49917","operator":"and","partner_start":654,"partner_end":759}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-04-02T18:43:15.918Z"}},{"start":282,"end":294,"reference_id":"38898102","reference_source":"pmid","reference_html":"Multivalent interactions of the disordered regions of XLF and XRCC4 foster robust cellular NHEJ and drive the formation of ligation-boosting condensates in vitro. <i> Vu DD, Bonucci A, Brenière M, Cisneros-Aguirre M, Pelupessy P, Wang Z, Carlier L, Bouvignies G, Cortes P, Aggarwal AK, Blackledge M, Gueroui Z, Belle V, Stark JM, Modesti M, Ferrage F. </i> Nat Struct Mol Biol, 2024","date":"2024-11-11T14:53:28.894Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP04259r003","statement":[{"text":"Therefore, the positively charged region (residues 282–294) is the core of the DNA-binding motif (DBM) (Fig. 2i).","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-04T15:30:50.026Z"}}],"regions_counter":3,"released":"2025_06","sequence":"MEELEQGLLMQPWAWLQLAENSLLAKVFITKQGYALLVSDLQQVWHEQVDTSVVSQRAKELNKRLTAPPAAFLCHLDNLLRPLLKDAAHPSEATFSCDCVADALILRVRSELSGLPFYWNFHCMLASPSLVSQHLIRPLMGMSLALQCQVRELATLLHMKDLEIQDYQESGATLIRDRLKTEPFEENSFLEQFMIEKLPEACSIGDGKPFVMNLQDLYMAVTTQEVQVGQKHQGAGDPHTSNSASLQGIDSQCVNQPEQLVSSAPTLSAPEKESTGTSGPLQRPQLSKVKRKKPRGLFS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.19732441471571907,"disorder_content":0.23745819397993312,"disprot_consensus":{"full":[{"start":229,"end":299,"type":"D"}],"Structural state":[{"start":229,"end":299,"type":"D"}],"Molecular function":[{"start":282,"end":299,"type":"F"}]}},{"disprot_id":"DP04260","acc":"P07196","creator":"tcordero","date":"2024-11-11T15:04:50.588Z","features":{"pfam":[{"id":"PF00038","name":"Intermediate filament protein","start":89,"end":399},{"id":"PF04732","name":"Intermediate filament head (DNA binding) region","start":9,"end":88}],"gene3D":[]},"genes":[{"name":{"value":"NEFL"},"synonyms":[{"value":"NF68"},{"value":"NFL"}]}],"length":543,"name":"Neurofilament light polypeptide","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":40,"end":63,"reference_id":"26016807","reference_source":"pmid","reference_html":"Investigating the Structural Variability and Binding Modes of the Glioma Targeting NFL-TBS.40-63 Peptide on Tubulin. <i> Laurin Y, Savarin P, Robert CH, Takahashi M, Eyer J, Prevost C, Sacquin-Mora S. </i> Biochemistry, 2015","date":"2024-12-06T17:33:51.559Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":5,"statements":[{"type":"Results","text":"The NMR structure of the free peptide with biotine at the N-terminal was investigated at pH 5."}]}],"construct_alterations":[{"term_id":"MI:0239","term_name":"biotin","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"The NMR structure of the free peptide with biotine at the N-terminal was investigated at pH 5."}]}],"region_id":"DP04260r004","statement":[{"text":"The values of the chemical shifts for the Hα protons, which are sensitive to the secondary structure, correspond to random coil structure. (56) Consequently, the peptide does not adopt any predominant regular secondary structure (see Figure 1). This was confirmed by the NOESY assignment.","type":"Results"}]},{"start":40,"end":63,"reference_id":"26016807","reference_source":"pmid","reference_html":"Investigating the Structural Variability and Binding Modes of the Glioma Targeting NFL-TBS.40-63 Peptide on Tubulin. <i> Laurin Y, Savarin P, Robert CH, Takahashi M, Eyer J, Prevost C, Sacquin-Mora S. </i> Biochemistry, 2015","date":"2024-12-06T17:54:38.820Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0015631","term_name":"tubulin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000314","ec_ontology":"ECO","ec_name":"direct assay evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0239","term_name":"biotin","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IDA","region_id":"DP04260r005","statement":[{"text":"The peptide (400 μM) was also studied in the presence of tubulin (60 μM), and a strong aggregation was then observed.","type":"Results"}],"term_comment":"","term_def":"\"Binding to monomeric or multimeric forms of tubulin, including microtubules.\" [GOC:clt]","term_is_obsolete":false,"term_not_annotate":false},{"start":40,"end":63,"reference_id":"23152907","reference_source":"pmid","reference_html":"Structure-function analysis of the glioma targeting NFL-TBS.40-63 peptide corresponding to the tubulin-binding site on the light neurofilament subunit. <i> Berges R, Balzeau J, Takahashi M, Prevost C, Eyer J. </i> PLoS One, 2012","date":"2024-12-06T17:57:39.138Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"MI:0239","term_name":"biotin","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"region_id":"DP04260r006","statement":[{"text":"The CD spectrum of the original NFL-TBS.40-63 peptide (wt NFL-TBS.40-63) in pure water indicates rather disordered conformation (black line in Figure 4A): the signal at 200 nm was negative while the ordered conformations (both α-helix and β-sheet) exhibit a positive CD signal at this UV region [31], [32].","type":"Results"}]}],"regions_counter":6,"released":"2024_12","sequence":"MSSFSYEPYYSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGSLMPSLENLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEISFLKKVHEEEIAELQAQIQYAQISVEMDVTKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRTTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRLSFTSVGSITSGYSQSSQVFGRSAYGGLQTSSYLMSTRSFPSYYTSHVQEEQIEVEETIEAAKAEEAKDEPPSEGEAEEEEKDKEEAEEEEAAEEEEAAKEESEEAKEEEEGGEGEEGEETKEAEEEEKKVEGAGEEQAAKKKD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.3296500920810313,"dataset":["Age-related disorders proteins"],"disorder_content":0.04419889502762431,"disprot_consensus":{"full":[{"start":40,"end":63,"type":"D"}],"Structural state":[{"start":40,"end":63,"type":"D"}],"Molecular function":[{"start":40,"end":63,"type":"F"}]}},{"disprot_id":"DP04261","acc":"P02489","creator":"ralderson","date":"2024-11-11T18:48:30.650Z","features":{"pfam":[{"id":"PF00011","name":"Hsp20/alpha crystallin family","start":64,"end":161},{"id":"PF00525","name":"Alpha crystallin A chain, N terminal","start":1,"end":54}],"gene3D":[]},"genes":[{"name":{"value":"CRYAA"},"synonyms":[{"value":"CRYA1"},{"value":"HSPB4"}]}],"length":173,"name":"Alpha-crystallin A chain","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":149,"end":173,"reference_id":"31792453","reference_source":"pmid","reference_html":"The structure and oxidation of the eye lens chaperone αA-crystallin. <i> Kaiser CJO, Peters C, Schmid PWN, Stavropoulou M, Zou J, Dahiya V, Mymrikov EV, Rockel B, Asami S, Haslbeck M, Rappsilber J, Reif B, Zacharias M, Buchner J, Weinkauf S. </i> Nat Struct Mol Biol, 2019","date":"2024-12-03T14:40:02.273Z","curator_id":"ralderson","curator_name":"Reid Alderson","curator_orcid":"0000-0001-5163-2276","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"27109"}],"region_id":"DP04261r001","statement":[{"text":"The CTR of αA-crystallin displays significant flexibility and can be detected by solution-state NMR (residues G149–S173, Fig. 3c).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-04T16:53:36.222Z"}},{"start":1,"end":60,"reference_id":"31792453","reference_source":"pmid","reference_html":"The structure and oxidation of the eye lens chaperone αA-crystallin. <i> Kaiser CJO, Peters C, Schmid PWN, Stavropoulou M, Zou J, Dahiya V, Mymrikov EV, Rockel B, Asami S, Haslbeck M, Rappsilber J, Reif B, Zacharias M, Buchner J, Weinkauf S. </i> Nat Struct Mol Biol, 2019","date":"2024-11-29T13:59:34.012Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04261r002","statement":[{"text":"During modeling using molecular dynamics flexible fitting, a homology-modeled structure for the NTR (residues 1-60) was used that contained three short helices connected by flexible loops (Extended Data Fig. 5a,b).","type":"Results"},{"text":"The fitting procedure resulted in an ensemble of solutions with the NTRs of both apical (Map) and equatorial (Meq) protomers adopting a variety of possible conformations (Extended Data Fig. 5c,d), consistent with their flexibility.","type":"Results"},{"text":"In agreement with previous studies49, peptides from the NTR were characterized by a moderate protection at short D2O exposure times, but became increasingly deuterated at longer exposure, consistent with the dynamic nature of this region sampling different conformations.","type":"Results"},{"text":"Extended Data Fig. 5 shows that the authors used a combination of secondary structure prediction and model building based on Cryo-EM data to determine that the NTD is highly mobile and flexible. The H/DX-MS experiment further supports this, demonstrating that the region lacks a fixed 3D structure.","type":"Curator statement"}]}],"regions_counter":2,"released":"2025_06","sequence":"MDVTIQHPWFKRTLGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVQDDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFCGPKIQTGLDATHAERAIPVSREEKPTSAPSS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.09826589595375723,"disorder_content":0.4913294797687861,"disprot_consensus":{"full":[{"start":1,"end":60,"type":"D"},{"start":149,"end":173,"type":"D"}],"Structural state":[{"start":1,"end":60,"type":"D"},{"start":149,"end":173,"type":"D"}]}},{"disprot_id":"DP04262","acc":"P04792","creator":"bjuhasz","date":"2024-11-11T18:55:21.148Z","features":{"pfam":[{"id":"PF00011","name":"Hsp20/alpha crystallin family","start":88,"end":184}],"gene3D":[]},"genes":[{"name":{"value":"HSPB1"},"synonyms":[{"value":"HSP27"},{"value":"HSP28"}]}],"length":205,"name":"Heat shock protein beta-1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":178,"end":205,"reference_id":"28547731","reference_source":"pmid","reference_html":"Proline isomerization in the C-terminal region of HSP27. <i> Alderson TR, Benesch JLP, Baldwin AJ. </i> Cell Stress Chaperones, 2017","date":"2024-12-03T14:41:11.925Z","curator_id":"ralderson","curator_name":"Reid Alderson","curator_orcid":"0000-0001-5163-2276","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"26994"}],"region_id":"DP04262r001","statement":[{"text":"This allowed us to unambiguously assign the observed resonances to residues E178–K205 (Fig. 2b). These data therefore reveal that the final 28 residues of HSP27, including the IPV motif, are predominately disordered in solution.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-04T16:53:47.934Z"}},{"start":1,"end":91,"reference_id":"31573509","reference_source":"pmid","reference_html":"Interplay of disordered and ordered regions of a human small heat shock protein yields an ensemble of 'quasi-ordered' states. <i> Clouser AF, Baughman HE, Basanta B, Guttman M, Nath A, Klevit RE. </i> Elife, 2019","date":"2026-06-18T12:04:21.460Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":"0009-0009-6028-6956","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04262r002","statement":[{"text":"In the human sHSP HSPB1, the disordered N-terminal region (NTR) represents nearly 50% of the sequence.","type":"Abstract"},{"text":"Together, these approaches revealed that, although the NTR is predominantly disordered, there are nevertheless specific interactions between the NTR and ACD in the context of full-length HSPB1.","type":"Introduction"}],"last_modified_by":"bjuhasz","last_modified_name":"Bernadett Juhász","cross_refs":[{"db":"BMRB","id":"27681"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp15Ser","start":null,"end":null,"position":null,"statements":[{"type":"Figure","text":"The dimer is generated by three phosphorylation-mimicking substitutions in the NTR (S15D, S78D, and S82D) and substitution of the CTR IXI motif to 'GXG' (179ITIPV183 to GTGPG) (Figure 1A)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp78Ser","start":null,"end":null,"position":null,"statements":[{"type":"Figure","text":"The dimer is generated by three phosphorylation-mimicking substitutions in the NTR (S15D, S78D, and S82D) and substitution of the CTR IXI motif to 'GXG' (179ITIPV183 to GTGPG) (Figure 1A)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp82Ser","start":null,"end":null,"position":null,"statements":[{"type":"Figure","text":"The dimer is generated by three phosphorylation-mimicking substitutions in the NTR (S15D, S78D, and S82D) and substitution of the CTR IXI motif to 'GXG' (179ITIPV183 to GTGPG) (Figure 1A)."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-19T13:03:35.346Z"}},{"start":1,"end":37,"reference_id":"31573509","reference_source":"pmid","reference_html":"Interplay of disordered and ordered regions of a human small heat shock protein yields an ensemble of 'quasi-ordered' states. <i> Clouser AF, Baughman HE, Basanta B, Guttman M, Nath A, Klevit RE. </i> Elife, 2019","date":"2026-06-18T12:14:29.713Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":"0009-0009-6028-6956","term_id":"GO:0042802","term_name":"identical protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"region_id":"DP04262r003","statement":[{"text":"Overall, the extent of perturbations observed in this mixing experiment reveals wide scale NTR-ACD contact and establishes that NTR/ACD interactions can occur between subunits within a dimer.","type":"Results"},{"text":"This is strong evidence that the large perturbations observed for these\npeaks in the NTR-ACD spectrum (relative to B1-ACD) are due to binding of the NTR distal region to\nthe b4/b8 groove.","type":"Results"},{"text":"(A) The distal peptide, consisting of HSPB1 residues 1–13, causes CSPs in the 15N-HSQC spectrum of B1-ACD (black). Peak shifts occur along a trajectory toward the peak positions of the same residues in the 15N-HSQC spectrum of NTR-ACD (gray, NTR-ACD; pink, five molar equivalents; red, 8.4 molar equivalents). (B) The strongest CSPs (red dots) map to residues in the β4/β8 groove. (C) The aromatic peptide (residues 12–27) causes CSPs in the spectrum of B1-ACD (green vs. black), but these are weakened when the peptide contains phosphoserine at site 15 (pink). (D) The CSPs map to residues in loops 3/4 and 5/6 and strand β6+7 (green dots). (E) The conserved peptide (residues 25–37) causes intensity loss in peaks in the 15N-HSQC spectrum of B1-ACD corresponding to strands β3, β6+7, and β9. Peaks that lose more than 30% of their original intensity are colored in orange.","type":"Figure"}],"last_modified_by":"bjuhasz","last_modified_name":"Bernadett Juhász","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp15Ser","start":null,"end":null,"position":null,"statements":[{"type":"Figure","text":"The dimer is generated by three phosphorylation-mimicking substitutions in the NTR (S15D, S78D, and S82D) and substitution of the CTR IXI motif to 'GXG' (179ITIPV183 to GTGPG) (Figure 1A)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp78Ser","start":null,"end":null,"position":null,"statements":[{"type":"Figure","text":"The dimer is generated by three phosphorylation-mimicking substitutions in the NTR (S15D, S78D, and S82D) and substitution of the CTR IXI motif to 'GXG' (179ITIPV183 to GTGPG) (Figure 1A)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp82Ser","start":null,"end":null,"position":null,"statements":[{"type":"Figure","text":"The dimer is generated by three phosphorylation-mimicking substitutions in the NTR (S15D, S78D, and S82D) and substitution of the CTR IXI motif to 'GXG' (179ITIPV183 to GTGPG) (Figure 1A)."}]}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P04792","operator":null,"partner_start":null,"partner_end":null}],"term_comment":"","term_def":"\"Binding to an identical protein or proteins.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-19T13:04:03.916Z"}},{"start":74,"end":91,"reference_id":"31573509","reference_source":"pmid","reference_html":"Interplay of disordered and ordered regions of a human small heat shock protein yields an ensemble of 'quasi-ordered' states. <i> Clouser AF, Baughman HE, Basanta B, Guttman M, Nath A, Klevit RE. </i> Elife, 2019","date":"2026-06-18T12:11:28.830Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":"0009-0009-6028-6956","term_id":"GO:0042802","term_name":"identical protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04262r004","statement":[{"text":"Overall, the extent of perturbations observed in this mixing experiment reveals wide scale NTR-ACD contact and establishes that NTR/ACD interactions can occur between subunits within a dimer.","type":"Results"},{"text":"This is strong evidence that the large perturbations observed for these peaks in the NTR-ACD spectrum (relative to B1-ACD) are due to binding of the NTR distal region to the b4/b8 groove.","type":"Results"},{"text":"(G)\nThe boundary peptide (residues 74–91) causes both CSPs and intensity loss.","type":"Figure"}],"last_modified_by":"bjuhasz","last_modified_name":"Bernadett Juhász","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp15Ser","start":null,"end":null,"position":null,"statements":[{"type":"Figure","text":"The dimer is generated by three phosphorylation-mimicking substitutions in the NTR (S15D, S78D, and S82D) and substitution of the CTR IXI motif to 'GXG' (179ITIPV183 to GTGPG) (Figure 1A)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp78Ser","start":null,"end":null,"position":null,"statements":[{"type":"Figure","text":"The dimer is generated by three phosphorylation-mimicking substitutions in the NTR (S15D, S78D, and S82D) and substitution of the CTR IXI motif to 'GXG' (179ITIPV183 to GTGPG) (Figure 1A)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp82Ser","start":null,"end":null,"position":null,"statements":[{"type":"Figure","text":"The dimer is generated by three phosphorylation-mimicking substitutions in the NTR (S15D, S78D, and S82D) and substitution of the CTR IXI motif to 'GXG' (179ITIPV183 to GTGPG) (Figure 1A)."}]}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P04792","operator":null,"partner_start":null,"partner_end":null}],"term_comment":"","term_def":"\"Binding to an identical protein or proteins.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-19T13:03:59.721Z"}},{"start":123,"end":137,"reference_id":"30842409","reference_source":"pmid","reference_html":"Local unfolding of the HSP27 monomer regulates chaperone activity. <i> Alderson TR, Roche J, Gastall HY, Dias DM, Pritišanac I, Ying J, Bax A, Benesch JLP, Baldwin AJ. </i> Nat Commun, 2019","date":"2026-06-10T19:53:14.296Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":null,"term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04262r005","statement":[{"text":"The central ACD exists as a stable dimer in which residue C137 at the dimer interface can access both reduced (blue, PDB 4mjh) and oxidised (red, PDB 2n3j) states.","type":"Figure"},{"text":"Notably, the second half of the β5 and first half of the β6 + 7 strands are not formed in the monomer, implying that these regions fold upon dimerisation.","type":"Results"},{"text":"This analysis confirmed that, while the disordered L5,6+7 spans from Q128 to Q132 in the dimer, it becomes substantially elongated in the monomer and includes residues between K123 and S137, thereby shortening the β5 and β6 + 7 strands.","type":"Results"},{"text":"The region between Q128 to Q132 is too short to be considered disordered and therefore the whole 123-137 region is considered to be ordered. ","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","construct_alterations":[{"term_id":"MI:0379","term_name":"13C label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"For preparation of uniformly-13C, 15N-labelled ([U-13C,15N]-) HSP27, the M9 minimal medium contained 2 g L−1 of [U-13C]-glucose and 1 g L−1 of 15NH4Cl."}]},{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"For preparation of uniformly-13C, 15N-labelled ([U-13C,15N]-) HSP27, the M9 minimal medium contained 2 g L−1 of [U-13C]-glucose and 1 g L−1 of 15NH4Cl."}]}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04792"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-10T19:54:38.322Z"}},{"start":123,"end":137,"reference_id":"30842409","reference_source":"pmid","reference_html":"Local unfolding of the HSP27 monomer regulates chaperone activity. <i> Alderson TR, Roche J, Gastall HY, Dias DM, Pritišanac I, Ying J, Bax A, Benesch JLP, Baldwin AJ. </i> Nat Commun, 2019","date":"2026-05-18T12:40:05.331Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04262r006","statement":[{"text":"This analysis confirmed that, while the disordered L5,6+7 spans from Q128 to Q132 in the dimer, it becomes substantially elongated in the monomer and includes residues between K123 and S137, thereby shortening the β5 and β6 + 7 strands. ","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys137Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Primers were designed to encode the single-point mutation C137S in cHSP27, and this plasmid was used to generate the double variant H124K/C137S via site-directed mutagenesis (Supplementary Table 6)."},{"type":"Curator statement","text":"This disulfide incompetent variant was created to mimic the reduced state of the protein."}]},{"term_id":"MI:0379","term_name":"13C label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"For preparation of uniformly-13C, 15N-labelled ([U-13C,15N]-) HSP27, the M9 minimal medium contained 2 g L−1 of [U-13C]-glucose and 1 g L−1 of 15NH4Cl."}]},{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Results","text":"For preparation of uniformly-13C, 15N-labelled ([U-13C,15N]-) HSP27, the M9 minimal medium contained 2 g L−1 of [U-13C]-glucose and 1 g L−1 of 15NH4Cl."}]}],"last_modified_by":"bjuhasz","last_modified_name":"Bernadett Juhász","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-10T19:47:48.858Z"}},{"start":123,"end":137,"reference_id":"30842409","reference_source":"pmid","reference_html":"Local unfolding of the HSP27 monomer regulates chaperone activity. <i> Alderson TR, Roche J, Gastall HY, Dias DM, Pritišanac I, Ying J, Bax A, Benesch JLP, Baldwin AJ. </i> Nat Commun, 2019","date":"2026-06-10T19:49:06.258Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":null,"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04262r007","statement":[{"text":"Using a combination of CPMG RD and high-pressure NMR, we established that the monomeric ACD of HSP27 partially unfolds upon dissociation (Fig. 7), such that the region responsible for the rigid interface in the dimer becomes highly dynamic.","type":"Results"},{"text":"Notably, the second half of the β5 and first half of the β6 + 7 strands are not formed in the monomer, implying that these regions fold upon dimerisation.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04792"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-10T19:49:14.786Z"}},{"start":187,"end":205,"reference_id":"30842409","reference_source":"pmid","reference_html":"Local unfolding of the HSP27 monomer regulates chaperone activity. <i> Alderson TR, Roche J, Gastall HY, Dias DM, Pritišanac I, Ying J, Bax A, Benesch JLP, Baldwin AJ. </i> Nat Commun, 2019","date":"2026-06-15T17:09:34.033Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04262r008","statement":[{"text":"Peptides within the aromatic, insert, and boundary regions in the NTR, along with the far C-terminal region (residues 187–205) of the CTR are all highly deuterated within 3 seconds, consistent with their lacking stable secondary structure.","type":"Results"}]},{"start":1,"end":11,"reference_id":"30842409","reference_source":"pmid","reference_html":"Local unfolding of the HSP27 monomer regulates chaperone activity. <i> Alderson TR, Roche J, Gastall HY, Dias DM, Pritišanac I, Ying J, Bax A, Benesch JLP, Baldwin AJ. </i> Nat Commun, 2019","date":"2026-06-15T17:12:09.095Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04262r009","statement":[{"text":"Peptides within the aromatic, insert, and boundary regions in the NTR, along with the far C-terminal region (residues 187–205) of the CTR are all highly deuterated within 3 seconds, consistent with their lacking stable secondary structure.","type":"Results"}]},{"start":42,"end":87,"reference_id":"30842409","reference_source":"pmid","reference_html":"Local unfolding of the HSP27 monomer regulates chaperone activity. <i> Alderson TR, Roche J, Gastall HY, Dias DM, Pritišanac I, Ying J, Bax A, Benesch JLP, Baldwin AJ. </i> Nat Commun, 2019","date":"2026-06-15T17:12:22.140Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04262r010","statement":[{"text":"Peptides within the aromatic, insert, and boundary regions in the NTR, along with the far C-terminal region (residues 187–205) of the CTR are all highly deuterated within 3 seconds, consistent with their lacking stable secondary structure.","type":"Results"}]}],"regions_counter":10,"released":"2025_06","sequence":"MTERRVPFSLLRGPSWDPFRDWYPHSRLFDQAFGLPRLPEEWSQWLGGSSWPGYVRPLPPAAIESPAVAAPAYSRALSRQLSSGVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQSNEITIPVTFESRAQLGGPEAAKSDETAAK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.28780487804878047,"dataset":["Condensates-related proteins","Stress response proteins"],"disorder_content":0.6536585365853659,"disprot_consensus":{"full":[{"start":1,"end":91,"type":"D"},{"start":123,"end":137,"type":"T"},{"start":178,"end":205,"type":"D"}],"Structural state":[{"start":1,"end":91,"type":"D"},{"start":123,"end":137,"type":"D"},{"start":178,"end":205,"type":"D"}],"Molecular function":[{"start":1,"end":37,"type":"F"},{"start":74,"end":91,"type":"F"}],"Structural transition":[{"start":123,"end":137,"type":"T"}]}},{"disprot_id":"DP04263","acc":"P18848","creator":"ralderson","date":"2024-11-11T19:02:46.199Z","features":{"pfam":[{"id":"PF00170","name":"bZIP transcription factor","start":276,"end":337}],"gene3D":[]},"genes":[{"name":{"value":"ATF4","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"2516827","url":"http://www.ncbi.nlm.nih.gov/pubmed/2516827","alternativeUrl":"https://europepmc.org/abstract/MED/2516827"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:786","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:786"}}]},"synonyms":[{"value":"CREB2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"1534408","url":"http://www.ncbi.nlm.nih.gov/pubmed/1534408","alternativeUrl":"https://europepmc.org/abstract/MED/1534408"}}]},{"value":"TXREB","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"1847461","url":"http://www.ncbi.nlm.nih.gov/pubmed/1847461","alternativeUrl":"https://europepmc.org/abstract/MED/1847461"}}]}]}],"length":351,"name":"Cyclic AMP-dependent transcription factor ATF-4","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":275,"reference_id":"35077711","reference_source":"pmid","reference_html":"Intricate coupling between the transactivation and basic-leucine zipper domains governs phosphorylation of transcription factor ATF4 by casein kinase 2. <i> Siang S, Underbakke ES, Roche J. </i> J Biol Chem, 2022","date":"2024-11-25T14:27:40.753Z","curator_id":"ralderson","curator_name":"Reid Alderson","curator_orcid":"0000-0001-5163-2276","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"51062"}],"region_id":"DP04263r001","statement":[{"text":"In good agreement with the CD data collected in the same conditions, the overall small 13C chemical shift deviations (displayed here as ΔCα- ΔCβ), all within +2 ppm and -1 ppm, confirm that ATF4-275 is predominantly disordered in solution (black in Fig. 3A).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-11-29T16:29:17.378Z"}}],"regions_counter":1,"released":"2025_06","sequence":"MTEMSFLSSEVLVGDLMSPFDQSGLGAEESLGLLDDYLEVAKHFKPHGFSSDKAKAGSSEWLAVDGLVSPSNNSKEDAFSGTDWMLEKMDLKEFDLDALLGIDDLETMPDDLLTTLDDTCDLFAPLVQETNKQPPQTVNPIGHLPESLTKPDQVAPFTFLQPLPLSPGVLSSTPDHSFSLELGSEVDITEGDRKPDYTAYVAMIPQCIKEEDTPSDNDSGICMSPESYLGSPQHSPSTRGSPNRSLPSPGVLCGSARPKPYDPPGEKMVAAKVKGEKLDKKLKKMEQNKTAATRYRQKKRAEQEALTGECKELEKKNEALKERADSLAKEIQYLKDLIEEVRKARGKKRVP","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.3190883190883191,"dataset":["Autophagy-related proteins"],"disorder_content":0.7834757834757835,"disprot_consensus":{"full":[{"start":1,"end":275,"type":"D"}],"Structural state":[{"start":1,"end":275,"type":"D"}]}},{"disprot_id":"DP04264","acc":"Q5SWA1","creator":"vnugnes","date":"2024-11-12T14:27:13.337Z","features":{"pfam":[{"id":"PF10472","name":"eIF2-alpha phosphatase phosphorylation constitutive repressor","start":1,"end":410},{"id":"PF10488","name":"Phosphatase-1 catalytic subunit binding region","start":469,"end":699}],"gene3D":[]},"genes":[{"name":{"value":"PPP1R15B"}}],"length":713,"name":"Protein phosphatase 1 regulatory subunit 15B","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":414,"end":613,"reference_id":"38159565","reference_source":"pmid","reference_html":"Recruitment of trimeric eIF2 by phosphatase non-catalytic subunit PPP1R15B. <i> Fatalska A, Hodgson G, Freund SMV, Maslen SL, Morgan T, Thorkelsson SR, van Slegtenhorst M, Lorenz S, Andreeva A, Kaat LD, Bertolotti A. </i> Mol Cell, 2024","date":"2024-11-12T14:29:45.625Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04264r001","statement":[{"text":"IDPs are problematic to study for many reasons. In HDX, they exchange rapidly, as observed here for R15B with saturated deuterium uptake observed after 3 s in heavy water (Figure S3A).","type":"Results"}]},{"start":556,"end":571,"reference_id":"38159565","reference_source":"pmid","reference_html":"Recruitment of trimeric eIF2 by phosphatase non-catalytic subunit PPP1R15B. <i> Fatalska A, Hodgson G, Freund SMV, Maslen SL, Morgan T, Thorkelsson SR, van Slegtenhorst M, Lorenz S, Andreeva A, Kaat LD, Bertolotti A. </i> Mol Cell, 2024","date":"2025-06-24T14:33:44.199Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0071074","term_name":"eukaryotic initiation factor eIF2 binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9BY44","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04264r002","statement":[{"text":"Addition of eIF2 resulted in increased protection throughout the sequence of R15B to various degrees (Figure 3; Table S1). The most pronounced changes localized to three short regions, 426–439, 471–495, and 556–571, with weaker changes in between (Figure 3). These HDX experiments suggest that the interaction with eIF2 occurs primarily through short and separated regions of R15B and that residues in between these regions, which exhibit weaker protection, may also contribute to the binding.","type":"Results"}],"term_comment":"","term_def":"\"Binding to eukaryotic initiation factor eIF2, a protein complex involved in the initiation of ribosome-mediated translation.\" [GOC:hjd]","term_is_obsolete":false,"term_not_annotate":false},{"start":414,"end":613,"reference_id":"38159565","reference_source":"pmid","reference_html":"Recruitment of trimeric eIF2 by phosphatase non-catalytic subunit PPP1R15B. <i> Fatalska A, Hodgson G, Freund SMV, Maslen SL, Morgan T, Thorkelsson SR, van Slegtenhorst M, Lorenz S, Andreeva A, Kaat LD, Bertolotti A. </i> Mol Cell, 2024","date":"2024-11-12T14:44:51.842Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"52233"}],"region_id":"DP04264r003","statement":[{"text":"The observed narrow dispersion in the 1H dimension (Figure 4A) indicates that R15B414–613 is predominantly intrinsically disordered in solution.","type":"Results"},{"text":"Together, our NMR data define R15B414–613 as a largely disordered protein with discrete regions with helical propensity.","type":"Results"}]},{"start":557,"end":561,"reference_id":"38159565","reference_source":"pmid","reference_html":"Recruitment of trimeric eIF2 by phosphatase non-catalytic subunit PPP1R15B. <i> Fatalska A, Hodgson G, Freund SMV, Maslen SL, Morgan T, Thorkelsson SR, van Slegtenhorst M, Lorenz S, Andreeva A, Kaat LD, Bertolotti A. </i> Mol Cell, 2024","date":"2025-06-24T14:36:57.210Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0071074","term_name":"eukaryotic initiation factor eIF2 binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9BY44","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04264r004","statement":[{"text":"Together, these NMR analyses revealed 3 sites in R15B that undergo binding-induced dynamic changes: those were most significant for residues 421–431, followed by residues 474–480 and, to a lesser extent, 558–560 (Figure 4D) and coincided with elements of R15B that adopt an α-helical conformation (Figure 4B). Less pronounced, but also significant, changes were observed between the first 2 helical binding elements (Figure 4D), suggesting that this extended region might contribute to the binding.","type":"Results"}],"term_comment":"","term_def":"\"Binding to eukaryotic initiation factor eIF2, a protein complex involved in the initiation of ribosome-mediated translation.\" [GOC:hjd]","term_is_obsolete":false,"term_not_annotate":false},{"start":425,"end":430,"reference_id":"38159565","reference_source":"pmid","reference_html":"Recruitment of trimeric eIF2 by phosphatase non-catalytic subunit PPP1R15B. <i> Fatalska A, Hodgson G, Freund SMV, Maslen SL, Morgan T, Thorkelsson SR, van Slegtenhorst M, Lorenz S, Andreeva A, Kaat LD, Bertolotti A. </i> Mol Cell, 2024","date":"2024-11-12T15:18:42.783Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0071074","term_name":"eukaryotic initiation factor eIF2 binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00484","term_name":"deletion-insertion","term_namespace":"Protein mutation","value":"p.Leu425_Leu430delinsAlaAlaAlaAlaAla","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"H1, H2, H3, and the ED motifs were replaced by alanines, generating H1A, H2A, H3A, and EDA mutants."}]},{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Table","text":"H1A R15B414-613 PXJ41 (N-FLAG) residues 425-430 AAAAA"}]}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q9BY44","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04264r005","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"R15B411–613 with the H1A mutation was immunoprecipitated at levels similar to the WT proteins, but the capture of eIF2α was dramatically reduced (Figure 5B). H2A was slightly compromised, whereas H3A seemed more efficient at capturing the substrate when compared to WT (Figure 5B).","type":"Results"},{"text":"Thus, we propose that H1 serves to anchor R15B to eIF2 and H2 contributes an additional binding site.","type":"Results"}],"term_comment":"","term_def":"\"Binding to eukaryotic initiation factor eIF2, a protein complex involved in the initiation of ribosome-mediated translation.\" [GOC:hjd]","term_is_obsolete":false,"term_not_annotate":false},{"start":420,"end":425,"reference_id":"38159565","reference_source":"pmid","reference_html":"Recruitment of trimeric eIF2 by phosphatase non-catalytic subunit PPP1R15B. <i> Fatalska A, Hodgson G, Freund SMV, Maslen SL, Morgan T, Thorkelsson SR, van Slegtenhorst M, Lorenz S, Andreeva A, Kaat LD, Bertolotti A. </i> Mol Cell, 2024","date":"2024-11-12T15:18:26.581Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0071074","term_name":"eukaryotic initiation factor eIF2 binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asn423Asp","start":null,"end":null,"position":null},{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q9BY44","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04264r006","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"A genetic variant in the substrate recognition module of R15B reduces its function and causes microcephaly, developmental delay, and intellectual disability","type":"Results"},{"text":" Whole exome sequencing identified a homozygous missense variant in the PPP1R15B gene, c.1267A>G resulting in a N423D mutation in the protein (Figure 6B).","type":"Results"},{"text":"When overexpressed in HEK293T cells, both H1A and N423D mutants captured significantly less eIF2α than the WT R15B411–613 fragment or full-length protein (Figures 6D and 6E).","type":"Results"}],"term_comment":"","term_def":"\"Binding to eukaryotic initiation factor eIF2, a protein complex involved in the initiation of ribosome-mediated translation.\" [GOC:hjd]","term_is_obsolete":false,"term_not_annotate":false},{"start":420,"end":425,"reference_id":"38159565","reference_source":"pmid","reference_html":"Recruitment of trimeric eIF2 by phosphatase non-catalytic subunit PPP1R15B. <i> Fatalska A, Hodgson G, Freund SMV, Maslen SL, Morgan T, Thorkelsson SR, van Slegtenhorst M, Lorenz S, Andreeva A, Kaat LD, Bertolotti A. </i> Mol Cell, 2024","date":"2024-11-12T15:28:21.057Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019888","term_name":"protein phosphatase regulator activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asn423Asp","start":null,"end":null,"position":null},{"term_id":"IDPO:00484","term_name":"deletion-insertion","term_namespace":"Protein mutation","value":"p.Leu425_Leu430delinsAlaAlaAlaAlaAla","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04264r007","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"This reduced eIF2α binding in the N423D and H1A mutants resulted in decreased, but not abolished, dephosphorylation activity to-ward P-eIF2α in cell lysates when compared with the WT R15B (Figures 6F and 6G). Thus, this identifies a disease-associated variant in R15B substrate recognition module that reduced its ability to recruit and dephosphorylate the substrate eIF2α.","type":"Results"}],"term_comment":"","term_def":"\"Binds to and modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":713,"reference_id":"28759048","reference_source":"pmid","reference_html":"Decoding the selectivity of eIF2α holophosphatases and PPP1R15A inhibitors. <i> Carrara M, Sigurdardottir A, Bertolotti A. </i> Nat Struct Mol Biol, 2017","date":"2024-11-12T15:38:49.908Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001191","ec_ontology":"ECO","ec_name":"in vitro cleavage assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04264r008","statement":[{"text":"As expected for natively unstructured proteins41, R15A and R15B were sensitive to a limited trypsin proteolysis (Fig. 4c).","type":"Results"}]},{"start":414,"end":639,"reference_id":"38159565","reference_source":"pmid","reference_html":"Recruitment of trimeric eIF2 by phosphatase non-catalytic subunit PPP1R15B. <i> Fatalska A, Hodgson G, Freund SMV, Maslen SL, Morgan T, Thorkelsson SR, van Slegtenhorst M, Lorenz S, Andreeva A, Kaat LD, Bertolotti A. </i> Mol Cell, 2024","date":"2024-11-12T15:43:28.434Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0071074","term_name":"eukaryotic initiation factor eIF2 binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9BY44","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04264r009","statement":[{"text":"Full-length R15B as well as R15B414–713 immunoprecipitated with both eIF2α and PP1, whereas R15B414–639 only immunoprecipitated eIF2α and R15B639–713 captured PP1, but not eIF2α (Figure 1B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to eukaryotic initiation factor eIF2, a protein complex involved in the initiation of ribosome-mediated translation.\" [GOC:hjd]","term_is_obsolete":false,"term_not_annotate":false},{"start":639,"end":713,"reference_id":"38159565","reference_source":"pmid","reference_html":"Recruitment of trimeric eIF2 by phosphatase non-catalytic subunit PPP1R15B. <i> Fatalska A, Hodgson G, Freund SMV, Maslen SL, Morgan T, Thorkelsson SR, van Slegtenhorst M, Lorenz S, Andreeva A, Kaat LD, Bertolotti A. </i> Mol Cell, 2024","date":"2024-11-12T15:45:55.558Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008157","term_name":"protein phosphatase 1 binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P62136","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04264r010","statement":[{"text":"Full-length R15B as well as R15B414–713 immunoprecipitated with both eIF2α and PP1, whereas R15B414–639 only immunoprecipitated eIF2α and R15B639–713 captured PP1, but not eIF2α (Figure 1B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein phosphatase 1.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":713,"reference_id":"38159565","reference_source":"pmid","reference_html":"Recruitment of trimeric eIF2 by phosphatase non-catalytic subunit PPP1R15B. <i> Fatalska A, Hodgson G, Freund SMV, Maslen SL, Morgan T, Thorkelsson SR, van Slegtenhorst M, Lorenz S, Andreeva A, Kaat LD, Bertolotti A. </i> Mol Cell, 2024","date":"2024-11-12T15:46:56.125Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0000164","term_name":"protein phosphatase type 1 complex","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IPI","region_id":"DP04264r011","statement":[{"text":"Full-length R15B as well as R15B414–713 immunoprecipitated with both eIF2α and PP1, whereas R15B414–639 only immunoprecipitated eIF2α and R15B639–713 captured PP1, but not eIF2α (Figure 1B).","type":"Results"}],"term_comment":"","term_def":"\"A protein complex that possesses magnesium-dependent protein serine/threonine phosphatase (AMD phosphatase) activity, and consists of a catalytic subunit and one or more regulatory subunits that dictates the phosphatase's substrate specificity, function, and activity.\" [GOC:mah, GOC:ssd]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"P62136","operator":"and","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9BY44","operator":"and","partner_start":null,"partner_end":null}]},{"start":1,"end":713,"reference_id":"34847777","reference_source":"pmid","reference_html":"Substrate recognition determinants of human eIF2α phosphatases. <i> Hodgson G, Andreeva A, Bertolotti A. </i> Open Biol, 2021","date":"2024-11-12T15:56:42.718Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0000164","term_name":"protein phosphatase type 1 complex","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"To identify functional regions in R15s, we generated a series of truncation mutants that were FLAG-tagged on their amino-termini."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9BY44","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P62136","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04264r012","statement":[{"text":"These experiments reveal that the binding of eIF2 and PP1 on R15B is not overlapping: R15B340–639 binds eIF2α while the carboxy-terminal region R15B639–713 binds PP1 (figure 1b; electronic supplementary material, figure S3).","type":"Results"}],"term_comment":"","term_def":"\"A protein complex that possesses magnesium-dependent protein serine/threonine phosphatase (AMD phosphatase) activity, and consists of a catalytic subunit and one or more regulatory subunits that dictates the phosphatase's substrate specificity, function, and activity.\" [GOC:mah, GOC:ssd]","term_is_obsolete":false,"term_not_annotate":false},{"start":340,"end":639,"reference_id":"34847777","reference_source":"pmid","reference_html":"Substrate recognition determinants of human eIF2α phosphatases. <i> Hodgson G, Andreeva A, Bertolotti A. </i> Open Biol, 2021","date":"2024-11-12T15:57:12.819Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0071074","term_name":"eukaryotic initiation factor eIF2 binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"To identify functional regions in R15s, we generated a series of truncation mutants that were FLAG-tagged on their amino-termini."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9BY44","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04264r013","statement":[{"text":"These experiments reveal that the binding of eIF2 and PP1 on R15B is not overlapping: R15B340–639 binds eIF2α while the carboxy-terminal region R15B639–713 binds PP1 (figure 1b; electronic supplementary material, figure S3).","type":"Results"}],"term_comment":"","term_def":"\"Binding to eukaryotic initiation factor eIF2, a protein complex involved in the initiation of ribosome-mediated translation.\" [GOC:hjd]","term_is_obsolete":false,"term_not_annotate":false},{"start":639,"end":713,"reference_id":"34847777","reference_source":"pmid","reference_html":"Substrate recognition determinants of human eIF2α phosphatases. <i> Hodgson G, Andreeva A, Bertolotti A. </i> Open Biol, 2021","date":"2024-11-12T15:57:59.074Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008157","term_name":"protein phosphatase 1 binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"To identify functional regions in R15s, we generated a series of truncation mutants that were FLAG-tagged on their amino-termini."}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P62136","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04264r014","statement":[{"text":"These experiments reveal that the binding of eIF2 and PP1 on R15B is not overlapping: R15B340–639 binds eIF2α while the carboxy-terminal region R15B639–713 binds PP1 (figure 1b; electronic supplementary material, figure S3).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein phosphatase 1.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":639,"end":713,"reference_id":"34847777","reference_source":"pmid","reference_html":"Substrate recognition determinants of human eIF2α phosphatases. <i> Hodgson G, Andreeva A, Bertolotti A. </i> Open Biol, 2021","date":"2024-11-12T16:06:03.060Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019888","term_name":"protein phosphatase regulator activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006170","ec_ontology":"ECO","ec_name":"quantitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IEP","interaction_partner":[{"db":"UniProt","id":"P62136","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04264r015","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"Similarly, full-length R15B1–713 as well as R15B340–713 were highly active (figure 3b). The amino-terminal regions of R15s, which do not bind the substrate nor PP1, as well as R15A325–554 and R15B340–639, which bind the substrate but not PP1, did not decrease phosphorylation of eIF2α (figure 3a,b). ","type":"Results"}],"term_comment":"","term_def":"\"Binds to and modulates the activity of a protein phosphatase, an enzyme which catalyzes of the removal of a phosphate group from a protein substrate molecule.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":426,"end":439,"reference_id":"38159565","reference_source":"pmid","reference_html":"Recruitment of trimeric eIF2 by phosphatase non-catalytic subunit PPP1R15B. <i> Fatalska A, Hodgson G, Freund SMV, Maslen SL, Morgan T, Thorkelsson SR, van Slegtenhorst M, Lorenz S, Andreeva A, Kaat LD, Bertolotti A. </i> Mol Cell, 2024","date":"2025-06-24T14:33:04.981Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0071074","term_name":"eukaryotic initiation factor eIF2 binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9BY44","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04264r016","statement":[{"text":"Addition of eIF2 resulted in increased protection throughout the sequence of R15B to various degrees (Figure 3; Table S1). The most pronounced changes localized to three short regions, 426–439, 471–495, and 556–571, with weaker changes in between (Figure 3). These HDX experiments suggest that the interaction with eIF2 occurs primarily through short and separated regions of R15B and that residues in between these regions, which exhibit weaker protection, may also contribute to the binding","type":"Results"}],"term_comment":"","term_def":"\"Binding to eukaryotic initiation factor eIF2, a protein complex involved in the initiation of ribosome-mediated translation.\" [GOC:hjd]","term_is_obsolete":false,"term_not_annotate":false},{"start":471,"end":495,"reference_id":"38159565","reference_source":"pmid","reference_html":"Recruitment of trimeric eIF2 by phosphatase non-catalytic subunit PPP1R15B. <i> Fatalska A, Hodgson G, Freund SMV, Maslen SL, Morgan T, Thorkelsson SR, van Slegtenhorst M, Lorenz S, Andreeva A, Kaat LD, Bertolotti A. </i> Mol Cell, 2024","date":"2025-06-24T14:33:33.457Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0071074","term_name":"eukaryotic initiation factor eIF2 binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9BY44","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04264r017","statement":[{"text":"Addition of eIF2 resulted in increased protection throughout the sequence of R15B to various degrees (Figure 3; Table S1). The most pronounced changes localized to three short regions, 426–439, 471–495, and 556–571, with weaker changes in between (Figure 3). These HDX experiments suggest that the interaction with eIF2 occurs primarily through short and separated regions of R15B and that residues in between these regions, which exhibit weaker protection, may also contribute to the binding","type":"Results"}],"term_comment":"","term_def":"\"Binding to eukaryotic initiation factor eIF2, a protein complex involved in the initiation of ribosome-mediated translation.\" [GOC:hjd]","term_is_obsolete":false,"term_not_annotate":false},{"start":421,"end":431,"reference_id":"38159565","reference_source":"pmid","reference_html":"Recruitment of trimeric eIF2 by phosphatase non-catalytic subunit PPP1R15B. <i> Fatalska A, Hodgson G, Freund SMV, Maslen SL, Morgan T, Thorkelsson SR, van Slegtenhorst M, Lorenz S, Andreeva A, Kaat LD, Bertolotti A. </i> Mol Cell, 2024","date":"2025-07-01T14:18:40.619Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0071074","term_name":"eukaryotic initiation factor eIF2 binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9BY44","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04264r018","statement":[{"text":"Addition of eIF2 resulted in increased protection throughout the sequence of R15B to various degrees (Figure 3; Table S1). The most pronounced changes localized to three short regions, 426–439, 471–495, and 556–571, with weaker changes in between (Figure 3). These HDX experiments suggest that the interaction with eIF2 occurs primarily through short and separated regions of R15B and that residues in between these regions, which exhibit weaker protection, may also contribute to the binding","type":"Results"}],"term_comment":"","term_def":"\"Binding to eukaryotic initiation factor eIF2, a protein complex involved in the initiation of ribosome-mediated translation.\" [GOC:hjd]","term_is_obsolete":false,"term_not_annotate":false},{"start":474,"end":480,"reference_id":"38159565","reference_source":"pmid","reference_html":"Recruitment of trimeric eIF2 by phosphatase non-catalytic subunit PPP1R15B. <i> Fatalska A, Hodgson G, Freund SMV, Maslen SL, Morgan T, Thorkelsson SR, van Slegtenhorst M, Lorenz S, Andreeva A, Kaat LD, Bertolotti A. </i> Mol Cell, 2024","date":"2025-07-01T14:18:48.537Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0071074","term_name":"eukaryotic initiation factor eIF2 binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9BY44","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04264r019","statement":[{"text":"Addition of eIF2 resulted in increased protection throughout the sequence of R15B to various degrees (Figure 3; Table S1). The most pronounced changes localized to three short regions, 426–439, 471–495, and 556–571, with weaker changes in between (Figure 3). These HDX experiments suggest that the interaction with eIF2 occurs primarily through short and separated regions of R15B and that residues in between these regions, which exhibit weaker protection, may also contribute to the binding","type":"Results"}],"term_comment":"","term_def":"\"Binding to eukaryotic initiation factor eIF2, a protein complex involved in the initiation of ribosome-mediated translation.\" [GOC:hjd]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":19,"released":"2025_06","sequence":"MEPGTGGSRKRLGPRAGFRFWPPFFPRRSQAGSSKFPTPLGPENSGNPTLLSSAQPETRVSYWTKLLSQLLAPLPGLLQKVLIWSQLFGGMFPTRWLDFAGVYSALRALKGREKPAAPTAQKSLSSLQLDSSDPSVTSPLDWLEEGIHWQYSPPDLKLELKAKGSALDPAAQAFLLEQQLWGVELLPSSLQSRLYSNRELGSSPSGPLNIQRIDNFSVVSYLLNPSYLDCFPRLEVSYQNSDGNSEVVGFQTLTPESSCLREDHCHPQPLSAELIPASWQGCPPLSTEGLPEIHHLRMKRLEFLQQASKGQDLPTPDQDNGYHSLEEEHSLLRMDPKHCRDNPTQFVPAAGDIPGNTQESTEEKIELLTTEVPLALEEESPSEGCPSSEIPMEKEPGEGRISVVDYSYLEGDLPISARPACSNKLIDYILGGASSDLETSSDPEGEDWDEEAEDDGFDSDSSLSDSDLEQDPEGLHLWNSFCSVDPYNPQNFTATIQTAARIVPEEPSDSEKDLSGKSDLENSSQSGSLPETPEHSSGEEDDWESSADEAESLKLWNSFCNSDDPYNPLNFKAPFQTSGENEKGCRDSKTPSESIVAISECHTLLSCKVQLLGSQESECPDSVQRDVLSGGRHTHVKRKKVTFLEEVTEYYISGDEDRKGPWEEFARDGCRFQKRIQETEDAIGYCLTFEHRERMFNRLQGTCFKGLNVLKQC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.6465638148667602,"dataset":["NDDs-related proteins"],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":713,"type":"D"}],"Structural state":[{"start":1,"end":713,"type":"D"}],"Molecular function":[{"start":340,"end":713,"type":"F"}],"Cellular component":[{"start":1,"end":713,"type":"F"}]}},{"disprot_id":"DP04267","acc":"Q9NPD8","creator":"vnugnes","date":"2024-11-12T18:09:44.623Z","features":{"pfam":[{"id":"PF00179","name":"Ubiquitin-conjugating enzyme","start":6,"end":146}],"gene3D":[]},"genes":[{"name":{"value":"UBE2T"},"orfNames":[{"value":"HSPC150"},{"value":"PIG50"}]}],"length":197,"name":"Ubiquitin-conjugating enzyme E2 T","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":157,"end":197,"reference_id":"37773242","reference_source":"pmid","reference_html":"Backbone <sup>1</sup>H, <sup>15</sup>N and <sup>13</sup>C resonance assignments for an E2 ubiquitin conjugating enzyme-UBE2T. <i> Huang Q, Ng HQ, Loh YY, Ke Z, Lim WH, Kang C. </i> Biomol NMR Assign, 2023","date":"2024-11-12T18:16:42.341Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04267r001","statement":[{"text":"The 1H-15N-HSQC spectra of both constructs were obtained and the cross-peaks corresponding to the C-terminal region appeared in the range of 7.5–8.5 ppm in the amide proton dimension (Fig. 1A). The narrow dispersion of the chemical shifts and high intensities of those cross-peaks suggest that the residues from the C-terminal region of UBE2T are not structured.","type":"Article"},{"text":" It contains an N-terminal UBC domain critical for its activity and a C-terminal short region formed by approximately 40 residues which are not structured.","type":"Article"}]},{"start":157,"end":197,"reference_id":"37773242","reference_source":"pmid","reference_html":"Backbone <sup>1</sup>H, <sup>15</sup>N and <sup>13</sup>C resonance assignments for an E2 ubiquitin conjugating enzyme-UBE2T. <i> Huang Q, Ng HQ, Loh YY, Ke Z, Lim WH, Kang C. </i> Biomol NMR Assign, 2023","date":"2024-11-12T18:18:28.234Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04267r002","statement":[{"text":"The 1H-15N-HSQC spectra of both constructs were obtained and the cross-peaks corresponding to the C-terminal region appeared in the range of 7.5–8.5 ppm in the amide proton dimension (Fig. 1A). The narrow dispersion of the chemical shifts and high intensities of those cross-peaks suggest that the residues from the C-terminal region of UBE2T are not structured.","type":"Article"},{"text":" It contains an N-terminal UBC domain critical for its activity and a C-terminal short region formed by approximately 40 residues which are not structured.","type":"Article"}]}],"regions_counter":2,"released":"2025_06","sequence":"MQRASRLKRELHMLATEPPPGITCWQDKDQMDDLRAQILGGANTPYEKGVFKLEVIIPERYPFEPPQIRFLTPIYHPNIDSAGRICLDVLKLPPKGAWRPSLNIATVLTSIQLLMSEPNPDDPLMADISSEFKYNKPAFLKNARQWTEKHARQKQKADEEEMLDNLPEAGDSRVHNSTQKRKASQLVGIEKKFHPDV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.1116751269035533,"disorder_content":0.20812182741116753,"disprot_consensus":{"full":[{"start":157,"end":197,"type":"D"}],"Structural state":[{"start":157,"end":197,"type":"D"}],"Disorder function":[{"start":157,"end":197,"type":"F"}]}},{"disprot_id":"DP04268","acc":"P93830","creator":"vnugnes","date":"2024-11-12T18:21:45.727Z","features":{"pfam":[{"id":"PF02309","name":"AUX/IAA family","start":11,"end":220}],"gene3D":[]},"genes":[{"name":{"value":"IAA17"},"synonyms":[{"value":"AXR3"}],"orfNames":[{"value":"F19P19.31"}],"olnNames":[{"value":"At1g04250"}]}],"length":229,"name":"Auxin-responsive protein IAA17","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":1,"end":101,"reference_id":"37756337","reference_source":"pmid","reference_html":"Intrinsic disorder and conformational coexistence in auxin coreceptors. <i> Ramans-Harborough S, Kalverda AP, Manfield IW, Thompson GS, Kieffer M, Uzunova V, Quareshy M, Prusinska JM, Roychoudhry S, Hayashi KI, Napier R, Genio CD, Kepinski S. </i> Proc Natl Acad Sci U S A, 2023","date":"2024-11-12T18:23:22.152Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"52109"}],"region_id":"DP04268r001","statement":[{"text":"The NMR data show an extensive region of intrinsic disorder encompassing the majority of the N-terminal domain (Fig. 1). The 1H–15N heteronuclear single quantum correlation (HSQC) spectrum for AXR31-101 is characterized by signals occurring in a narrow 1H chemical shift region (7.9 to 8.6 ppm), indicative of an IDP (Fig. 1 and SI Appendix, Table S1).","type":"Results"}]},{"start":1,"end":101,"reference_id":"37756337","reference_source":"pmid","reference_html":"Intrinsic disorder and conformational coexistence in auxin coreceptors. <i> Ramans-Harborough S, Kalverda AP, Manfield IW, Thompson GS, Kieffer M, Uzunova V, Quareshy M, Prusinska JM, Roychoudhry S, Hayashi KI, Napier R, Genio CD, Kepinski S. </i> Proc Natl Acad Sci U S A, 2023","date":"2024-11-12T18:29:46.359Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04268r002","statement":[{"text":"Here, we combine NMR and CD (circular dichroism) analysis with molecular dynamics (MD) simulations to study the disordered amino-terminal of the Aux/IAA protein AXR3 and to estimate its interactions with TIR1.","type":"Results"},{"text":"CD spectrum shows this peptide is intrinsically unstructured by its large negative ellipticity at 200 nm.","type":"Curator statement"}]},{"start":150,"end":172,"reference_id":"25512488","reference_source":"pmid","reference_html":"Structural basis for the auxin-induced transcriptional regulation by Aux/IAA17. <i> Han M, Park Y, Kim I, Kim EH, Yu TK, Rhee S, Suh JY. </i> Proc Natl Acad Sci U S A, 2014","date":"2024-11-12T18:49:17.594Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"25217"},{"db":"PDB","id":"2MUK"}],"region_id":"DP04268r003","statement":[{"text":"Superposition of the backbone atoms for the ensemble of the final 20 simulated annealing structures of IAA17M2 demonstrates that the secondary structures are well ordered except for the α1′ and α3 helices (Fig. 1A).","type":"Results"},{"text":"To investigate if the dynamic α1′ helix affects folding or oligomerization of IAA17M2, we prepared IAA17M2(Δ159−169) that removed the α1′ helix.","type":"Results"}]},{"start":150,"end":172,"reference_id":"25512488","reference_source":"pmid","reference_html":"Structural basis for the auxin-induced transcriptional regulation by Aux/IAA17. <i> Han M, Park Y, Kim I, Kim EH, Yu TK, Rhee S, Suh JY. </i> Proc Natl Acad Sci U S A, 2014","date":"2024-11-12T18:49:52.380Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"25217"},{"db":"PDB","id":"2MUK"}],"region_id":"DP04268r004","statement":[{"text":"Superposition of the backbone atoms for the ensemble of the final 20 simulated annealing structures of IAA17M2 demonstrates that the secondary structures are well ordered except for the α1′ and α3 helices (Fig. 1A).","type":"Results"},{"text":"To investigate if the dynamic α1′ helix affects folding or oligomerization of IAA17M2, we prepared IAA17M2(Δ159−169) that removed the α1′ helix.","type":"Results"},{"text":"The insert region forms the α1′ helix connecting α1 of domain III and β3 of domain IV (Fig. 1B).","type":"Results"}]}],"regions_counter":4,"released":"2025_06","sequence":"MMGSVELNLRETELCLGLPGGDTVAPVTGNKRGFSETVDLKLNLNNEPANKEGSTTHDVVTFDSKEKSACPKDPAKPPAKAQVVGWPPVRSYRKNVMVSCQKSSGGPEAAAFVKVSMDGAPYLRKIDLRMYKSYDELSNALSNMFSSFTMGKHGGEEGMIDFMNERKLMDLVNSWDYVPSYEDKDGDWMLVGDVPWPMFVDTCKRLRLMKGSDAIGLAPRAMEKCKSRA","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"alphafold_very_low_content":0.26200873362445415,"disorder_content":0.5414847161572053,"disprot_consensus":{"full":[{"start":1,"end":101,"type":"D"},{"start":150,"end":172,"type":"D"}],"Structural state":[{"start":1,"end":101,"type":"D"},{"start":150,"end":172,"type":"D"}],"Disorder function":[{"start":150,"end":172,"type":"F"}]}},{"disprot_id":"DP04270","acc":"Q8WXC6","creator":"zskalman","date":"2024-11-14T10:43:39.137Z","features":{"pfam":[{"id":"PF15004","name":"Myeloma-overexpressed-like","start":1,"end":55}],"gene3D":[]},"genes":[{"name":{"value":"COPS9","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:21314","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:21314"}}]},"synonyms":[{"value":"MYEOV2","evidences":[{"code":"ECO:0000303","source":{"name":"Citation","id":"Ref.1","url":"https://www.uniprot.org/uniprot/null#ref1"}}]}]}],"length":57,"name":"COP9 signalosome complex subunit 9","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":40,"reference_id":"34272906","reference_source":"pmid","reference_html":"The disordered PCI-binding human proteins CSNAP and DSS1 have diverged in structure and function. <i> Ruidiaz SF, Dreier JE, Hartmann-Petersen R, Kragelund BB. </i> Protein Sci, 2021","date":"2024-11-14T10:50:19.555Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"50908"}],"region_id":"DP04270r001","statement":[{"text":"For both proteins, the assigned 1H-15N HSQC spectra (Figure 2b) demonstrated low dispersion in the proton dimension characteristic of disordered proteins, in full accordance with the CD spectra.","type":"Results"}],"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sequence_construct":"GMKPAVDEMFPEGAGPYVDL DEAGGSTGLLMDLAANEKAV HADFFNDFEDLFDDDDIQ","conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":null,"value":283},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7.4}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-03T19:08:55.787Z"}},{"start":1,"end":57,"reference_id":"34272906","reference_source":"pmid","reference_html":"The disordered PCI-binding human proteins CSNAP and DSS1 have diverged in structure and function. <i> Ruidiaz SF, Dreier JE, Hartmann-Petersen R, Kragelund BB. </i> Protein Sci, 2021","date":"2025-02-03T18:47:26.646Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04270r002","statement":[{"text":"Both showed an intense negative ellipticity with a global minimum just under 200 nm, characteristic of highly unstructured proteins (Figure 2a). Negative ellipticity was also visible as a broad minimum around 220 nm suggesting the presence of transient structures, likely from α‐helices or poly‐proline II (PPII)/extended structures.","type":"Results"}]}],"regions_counter":2,"released":"2025_06","sequence":"MKPAVDEMFPEGAGPYVDLDEAGGSTGLLMDLAANEKAVHADFFNDFEDLFDDDDIQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.03508771929824561,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":57,"type":"D"}],"Structural state":[{"start":1,"end":57,"type":"D"}]}},{"disprot_id":"DP04271","acc":"P02647","creator":"tcordero","date":"2024-11-14T11:39:18.121Z","features":{"pfam":[{"id":"PF01442","name":"Apolipoprotein A1/A4/E domain","start":69,"end":256}],"gene3D":[]},"genes":[{"name":{"value":"APOA1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:600","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:600"}}]}}],"length":267,"name":"Apolipoprotein A-I","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":210,"end":267,"reference_id":"19850866","reference_source":"pmid","reference_html":"Helical structure and stability in human apolipoprotein A-I by hydrogen exchange and mass spectrometry. <i> Chetty PS, Mayne L, Lund-Katz S, Stranz D, Englander SW, Phillips MC. </i> Proc Natl Acad Sci U S A, 2009","date":"2024-12-05T13:41:10.877Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":5}],"region_id":"DP04271r001","statement":[{"text":"The total of 116 ± 8 helical residues in the 243-residue apoA-I polypeptide indicates a helix content of 48 ± 3%, consistent with CD data for wild-type apoA-I and the deletion mutant 190–243 (9, 11) at low concentration. All helices are located in the N-terminal domain between residues 1 and 178. The C-terminal\nresidues 186–243 are disordered (Table 1)","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-05T13:42:34.760Z"}},{"start":140,"end":170,"reference_id":"19850866","reference_source":"pmid","reference_html":"Helical structure and stability in human apolipoprotein A-I by hydrogen exchange and mass spectrometry. <i> Chetty PS, Mayne L, Lund-Katz S, Stranz D, Englander SW, Phillips MC. </i> Proc Natl Acad Sci U S A, 2009","date":"2024-12-05T13:33:28.448Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":5,"statements":[{"type":"Results","text":"HX data shown in Fig. 2 and Fig. S3 for peptide fragments\nobtained for monomeric apoA-I in solution at pD 7.0 and 5 °C\nillustrate the quality of the data and its analysis."}]}],"region_id":"DP04271r002","statement":[{"text":"The placement of helical structure in the N-terminal domain of apoA-I and disordered chain in the C-terminal domain (Table 1, Fig. 3) agrees with previous\nmutational analyses and modeling studies (11, 13, 29, 30, 31). Also, the detection by HX of the disordered region spanning residues 116–146 between helices 4 and 5 (Table 1) is consistent with studies of apoA-I (Δ121–142) mutants (36).","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-05T13:41:57.835Z"}},{"start":25,"end":267,"reference_id":"27992182","reference_source":"pmid","reference_html":"Heparin and Methionine Oxidation Promote the Formation of Apolipoprotein A-I Amyloid Comprising α-Helical and β-Sheet Structures. <i> Townsend D, Hughes E, Hussain R, Siligardi G, Baldock S, Madine J, Middleton DA. </i> Biochemistry, 2017","date":"2024-12-05T13:45:27.332Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"GO:0034205","term_name":"amyloid-beta formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006202","ec_ontology":"ECO","ec_name":"synchrotron radiation circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":4,"statements":[{"type":"Methods","text":"For the final read methods, apoA-I (36 μM) was incubated at pH 4 and 7 in the presence or absence of heparin."}]}],"region_id":"DP04271r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":0.014,"db":"ChEBI","id":"28304","statements":[{"type":"Methods","text":"For continuous read, apoA-I (at 7 μM) was incubated in a 96-well clear-bottom plate with agitation in McIlvaine buffer with 20 μM ThT in a total volume of 200 μL. Some solutions contained heparin [IdoA(2S)-GlcNS(6S) 14–15 kDa, >70%, Iduron] at a 2:1 molar ratio to apoA-I."}],"entry_name":"heparin"}],"statement":[{"text":"At pH 4, although a considerable amount of protein precipitation occurred, the remaining diluted solution of the protein retained a significant amount of α-helical structure even after 2 h (insoluble material was removed by centrifugation before analysis) (Figure 2B). Fitting of the spectrum suggests a partial loss of helical content and a gain of β-sheet and disordered elements (Table 1).","type":"Results"}],"ec_go":"EXP","term_comment":"Note that this term does not fall under the general GO definition for biosynthetic processes, which is 'The chemical reactions and pathways resulting in the formation of... ', because amyloid-beta can only be formed by the proteolysis of a larger molecule (see term definition). The word 'formation' is therefore used in place of biosynthesis. Also, note that this term refers to the production of the amyloid-beta polypeptide from the amyloid precursor protein (APP), and should be used to annotate e.g. secretases that cleave APP to form amyloid-beta. To annotate gene products involved in the formation of amyloid fibrils, please consider 'amyloid fibril formation' (GO:1990000).","term_def":"\"The generation of amyloid-beta by cleavage of the amyloid precursor protein (APP).\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-05T13:50:13.360Z"}},{"start":70,"end":83,"reference_id":"27992182","reference_source":"pmid","reference_html":"Heparin and Methionine Oxidation Promote the Formation of Apolipoprotein A-I Amyloid Comprising α-Helical and β-Sheet Structures. <i> Townsend D, Hughes E, Hussain R, Siligardi G, Baldock S, Madine J, Middleton DA. </i> Biochemistry, 2017","date":"2024-12-06T08:46:14.401Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006202","ec_ontology":"ECO","ec_name":"synchrotron radiation circular dichroism evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":25,"statements":[{"type":"Results","text":"Here, synthetic apoA-I(46–59) readily formed amyloid-like fibrils (∼10 nm width) in the absence of heparin (Figure 5A), and SRCD revealed a concomitant structural rearrangement from mainly unordered to β-sheet after incubation at 25 °C for 4 h (Figure 5B). "}]}],"region_id":"DP04271r004","statement":[{"text":"Here, synthetic apoA-I(46–59) readily formed amyloid-like fibrils (∼10 nm width) in the absence of heparin (Figure 5A), and SRCD revealed a concomitant structural rearrangement from mainly unordered to β-sheet after incubation at 25 °C for 4 h (Figure 5B). The minimum-to-maximum intensity transition around 194 nm after peptide aggregation is consistent with a conformational switch from an initial unfolded state to a predominantly β-sheet structure. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-06T16:47:14.263Z"}},{"start":70,"end":83,"reference_id":"27992182","reference_source":"pmid","reference_html":"Heparin and Methionine Oxidation Promote the Formation of Apolipoprotein A-I Amyloid Comprising α-Helical and β-Sheet Structures. <i> Townsend D, Hughes E, Hussain R, Siligardi G, Baldock S, Madine J, Middleton DA. </i> Biochemistry, 2017","date":"2024-12-03T09:59:45.039Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"GO:0034205","term_name":"amyloid-beta formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007044","ec_ontology":"ECO","ec_name":"transmission electron microscopy evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":25,"statements":[{"type":"Results","text":"Here, synthetic apoA-I(46−59) readily formed amyloid-like fibrils (∼10 nm width) in the absence of heparin (Figure 5A), and SRCD revealed a concomitant structural rearrangement from mainly unordered to β-sheet after incubation at 25 °C for 4 h (Figure 5B)."}]}],"region_id":"DP04271r005","statement":[{"text":"Here, synthetic apoA-I(46−59) readily formed amyloid-like fibrils (∼10 nm width) in the absence of heparin (Figure 5A), and SRCD revealed a concomitant structural rearrangement from mainly unordered to β-sheet after incubation at 25 °C for 4 h (Figure 5B). The minimum to maximum intensity transition around 194 nm after peptide aggregation is consistent with a conformational switch from an initial unfolded state to a predominantly β-sheet structure.","type":"Results"}],"ec_go":"IDA","term_comment":"Note that this term does not fall under the general GO definition for biosynthetic processes, which is 'The chemical reactions and pathways resulting in the formation of... ', because amyloid-beta can only be formed by the proteolysis of a larger molecule (see term definition). The word 'formation' is therefore used in place of biosynthesis. Also, note that this term refers to the production of the amyloid-beta polypeptide from the amyloid precursor protein (APP), and should be used to annotate e.g. secretases that cleave APP to form amyloid-beta. To annotate gene products involved in the formation of amyloid fibrils, please consider 'amyloid fibril formation' (GO:1990000).","term_def":"\"The generation of amyloid-beta by cleavage of the amyloid precursor protein (APP).\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-05T13:49:33.987Z"}},{"start":25,"end":267,"reference_id":"8610156","reference_source":"pmid","reference_html":"Thermal unfolding of human high-density apolipoprotein A-1: implications for a lipid-free molten globular state. <i> Gursky O, Atkinson D. </i> Proc Natl Acad Sci U S A, 1996","date":"2024-12-02T18:17:36.614Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006230","ec_ontology":"ECO","ec_name":"heat capacity-based evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04271r006","statement":[{"text":"The low cooperativity (ΔHv/ΔH - 0.16) of the thermal unfolding of lipid-free apoA-1 and the temperature dependence of the far- and near-UV CD spectra indicate that the a-helixes of apoA-1 are only weakly stabilized by tertiary interactions. These features suggest a molten globular-like state for apoA-1 in low-salt solution at 37°C and pH 7.\n","type":"Discussion"}]},{"start":44,"end":54,"reference_id":"19850866","reference_source":"pmid","reference_html":"Helical structure and stability in human apolipoprotein A-I by hydrogen exchange and mass spectrometry. <i> Chetty PS, Mayne L, Lund-Katz S, Stranz D, Englander SW, Phillips MC. </i> Proc Natl Acad Sci U S A, 2009","date":"2024-12-03T08:52:32.528Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04271r007","statement":[{"text":"A number of fragments (refer to Fig. S3 A and B) show an unstructured length following helix 1 with no apparent protection (peptides 46–50, 46–59, 47–56, 48–59, 50–57, and 51–57). ","type":"Results"},{"text":"Cylinders along the length of the parent apoA-I molecule (243 residues) place α-helix; lines represent disordered segments.","type":"Figure"},{"text":"Figure 3 represents the region 44-54 as disordered ","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-05T13:18:56.526Z"}}],"regions_counter":7,"released":"2024_12","sequence":"MKAAVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.0599250936329588,"dataset":["Age-related disorders proteins"],"disorder_content":0.9101123595505618,"disprot_consensus":{"full":[{"start":25,"end":69,"type":"D"},{"start":70,"end":83,"type":"T"},{"start":84,"end":267,"type":"D"}],"Structural state":[{"start":25,"end":267,"type":"D"}],"Biological process":[{"start":25,"end":267,"type":"F"}],"Structural transition":[{"start":70,"end":83,"type":"T"}]}},{"disprot_id":"DP04272","acc":"Q9V2F4","creator":"zskalman","date":"2024-11-14T12:38:18.106Z","features":{"pfam":[{"id":"PF03833","name":"DNA polymerase II large subunit DP2, N-terminal","start":9,"end":280},{"id":"PF14890","name":"Intein splicing domain","start":972,"end":1138},{"id":"PF24844","name":"DNA polymerase II large subunit DP2, central domain","start":321,"end":737},{"id":"PF24846","name":"DNA polymerase II large subunit DP2, catalytic domain","start":783,"end":968},{"id":"PF24846","name":"DNA polymerase II large subunit DP2, catalytic domain","start":1139,"end":1262}],"gene3D":[]},"genes":[{"name":{"value":"polC"},"orfNames":[{"value":"PAB2404"}],"olnNames":[{"value":"PYRAB01200"}]}],"length":1455,"name":"DNA polymerase II large subunit","ncbi_taxon_id":272844,"organism":"Pyrococcus abyssi (strain GE5 / Orsay)","regions":[{"start":1075,"end":1100,"reference_id":"21914805","reference_source":"pmid","reference_html":"Structural and mutational studies of a hyperthermophilic intein from DNA polymerase II of Pyrococcus abyssi. <i> Du Z, Liu J, Albracht CD, Hsu A, Chen W, Marieni MD, Colelli KM, Williams JE, Reitter JN, Mills KV, Wang C. </i> J Biol Chem, 2011","date":"2024-11-14T12:45:15.069Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"2LCJ"}],"region_id":"DP04272r001","statement":[{"text":"This Pab PolII-specific loop has few\nobserved long-range NOEs and shows 15N relaxation rates\ncharacteristic of disorder and flexibility (see below).","type":"Results"}],"sequence_construct":"CFPGDTRILVQIDGVPQKITLRELYELFEDERYENMVYVRKKPKREIKVYSIDLETGKVVLTDIEDVIKAPATDHLIRFELEDGRSFETTVDHPVLVYENGRFIEKRAFEVKEGDKVLVSELELVEQSSSSQDNPKNENLGSPEHDQLLEIKNIKYVRANDDFVFSLNAKKYHNVIINENIVTHQ","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-12T15:11:08.100Z"}},{"start":1225,"end":1246,"reference_id":"27548043","reference_source":"pmid","reference_html":"Shared active site architecture between archaeal PolD and multi-subunit RNA polymerases revealed by X-ray crystallography. <i> Sauguet L, Raia P, Henneke G, Delarue M. </i> Nat Commun, 2016","date":"2026-05-12T15:36:34.672Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"5IJL"}],"region_id":"DP04272r002","statement":[{"text":"The 50 residues of the CTD present in our construct (1,000–1,050) are partly disordered, except for two helices α32 and α33 (residues 1,011–1,039), which bind next to the interface between the central and catalytic domains through interactions with the DPPB-1 and helix α32.","type":"Results"},{"text":"The assessed protein is the processed version generated after self-protein splicing due to its intein activity.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Cys955_Gln1139del","start":null,"end":null,"position":null}],"sequence_construct":"GTGDGSELPKEMEEYFEMLQREIDKAYEIAKKARAQGKDPSLDVEIPQATDMAGRVESLVGPPGVAKRIRELVKEYGKEIAALKIVDEIIEGKFGDLGSREKYAEQAVRTALAILTEGIVSAPIEGIANVKIKRNTWADNSEYLALYYAGPIRSSGGTAQALSVLVGDYVRRKLGLDRFKPSEKHIERMVEEVDLYHRAVTRLQYHPSPEEVRLAMRNIPIEITGEATDDVEVSHRDVPGVETNQLRGGAILVLAEGVLQKAKKLVKYIDKMGIEGWEWLKEFVEAKEKGEPKEEGKEESLAESTLEETKVEVDMGFYYSLYQKFKEEIAPSDKYAKEVIGGRPLFSDPSKPGGFRLRYGRSRASGFATWGINPATMILVDEFLAIGTQLKTERPGKGAVVTPVTTIEGPIVKLKDGSVLRVDDYNLALKVREDVEEILYLGDAVIAFGDFVENNQTLLPANYCEEWWILEFVKALKEIYEVHLEPFTENEEESIEEASDYLEIDPEFLKEMLRDPLRVKPPVELAIHFSEVLGIPLHPYYTLYWNSVEPKDVEKLWRLLKNYAEIEWSNFRGIKFAKKIVISQEKLGDSKRTLELLGLPHTVRDGNVIVDYPWAAALLTPLGNLNWEFMAKPLYATIDIINENNEIKLRDRGISWIGARMGRPEKAKERKMKPPVQVLFPIGLAGGSSRDIKKAAEEGKVAEVEIAFFKCPKCGHVGPEHLCPNCGTRKELLWVCPRCNAEYPESQAEGYNYTCPKCNVKLRPYAKRKIRPSELLNRAMENVKVYGVDKLKGVMGMTSGWKMPEPLEKGLLRAKNDVYVFKDGTIRFDATDAPITHFRPREIGVSVEKLRELGYTHDFEGKPLVSEDQIVELKPQDIILSKEAGRYLLKVAKFVDDLLEKFYGLPRFYNAEKMEDLIGHLVIGLAPHTSAGIVGRIIGFVDALVGYAHPYFHAAKRRNCDGDEDAVMLLLDALLNFSRYYLPEKRGGKMDAPLVITTRLDPREVDSEVHNMDIVRYYPLEFYEATYELKSPKELVGVIERVEDRLGKPEMYYGLKFTHDTDDIAL","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-12T15:37:22.526Z"}},{"start":1183,"end":1195,"reference_id":"27548043","reference_source":"pmid","reference_html":"Shared active site architecture between archaeal PolD and multi-subunit RNA polymerases revealed by X-ray crystallography. <i> Sauguet L, Raia P, Henneke G, Delarue M. </i> Nat Commun, 2016","date":"2026-05-12T15:37:39.740Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"5IJL"}],"region_id":"DP04272r003","statement":[{"text":"The 50 residues of the CTD present in our construct (1,000–1,050) are partly disordered, except for two helices α32 and α33 (residues 1,011–1,039), which bind next to the interface between the central and catalytic domains through interactions with the DPPB-1 and helix α32.","type":"Results"},{"text":"The assessed protein is the processed version generated after self-protein splicing due to its intein activity.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Cys955_Gln1139del","start":null,"end":null,"position":null}],"sequence_construct":"GTGDGSELPKEMEEYFEMLQREIDKAYEIAKKARAQGKDPSLDVEIPQATDMAGRVESLVGPPGVAKRIRELVKEYGKEIAALKIVDEIIEGKFGDLGSREKYAEQAVRTALAILTEGIVSAPIEGIANVKIKRNTWADNSEYLALYYAGPIRSSGGTAQALSVLVGDYVRRKLGLDRFKPSEKHIERMVEEVDLYHRAVTRLQYHPSPEEVRLAMRNIPIEITGEATDDVEVSHRDVPGVETNQLRGGAILVLAEGVLQKAKKLVKYIDKMGIEGWEWLKEFVEAKEKGEPKEEGKEESLAESTLEETKVEVDMGFYYSLYQKFKEEIAPSDKYAKEVIGGRPLFSDPSKPGGFRLRYGRSRASGFATWGINPATMILVDEFLAIGTQLKTERPGKGAVVTPVTTIEGPIVKLKDGSVLRVDDYNLALKVREDVEEILYLGDAVIAFGDFVENNQTLLPANYCEEWWILEFVKALKEIYEVHLEPFTENEEESIEEASDYLEIDPEFLKEMLRDPLRVKPPVELAIHFSEVLGIPLHPYYTLYWNSVEPKDVEKLWRLLKNYAEIEWSNFRGIKFAKKIVISQEKLGDSKRTLELLGLPHTVRDGNVIVDYPWAAALLTPLGNLNWEFMAKPLYATIDIINENNEIKLRDRGISWIGARMGRPEKAKERKMKPPVQVLFPIGLAGGSSRDIKKAAEEGKVAEVEIAFFKCPKCGHVGPEHLCPNCGTRKELLWVCPRCNAEYPESQAEGYNYTCPKCNVKLRPYAKRKIRPSELLNRAMENVKVYGVDKLKGVMGMTSGWKMPEPLEKGLLRAKNDVYVFKDGTIRFDATDAPITHFRPREIGVSVEKLRELGYTHDFEGKPLVSEDQIVELKPQDIILSKEAGRYLLKVAKFVDDLLEKFYGLPRFYNAEKMEDLIGHLVIGLAPHTSAGIVGRIIGFVDALVGYAHPYFHAAKRRNCDGDEDAVMLLLDALLNFSRYYLPEKRGGKMDAPLVITTRLDPREVDSEVHNMDIVRYYPLEFYEATYELKSPKELVGVIERVEDRLGKPEMYYGLKFTHDTDDIAL","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-12T15:37:56.597Z"}},{"start":286,"end":307,"reference_id":"27548043","reference_source":"pmid","reference_html":"Shared active site architecture between archaeal PolD and multi-subunit RNA polymerases revealed by X-ray crystallography. <i> Sauguet L, Raia P, Henneke G, Delarue M. </i> Nat Commun, 2016","date":"2026-05-12T15:43:27.270Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Cys955_Gln1139del","start":null,"end":null,"position":null}],"region_id":"DP04272r004","statement":[{"text":"As a consequence of this flexibility, several fragments of the peptide chains, all located within this interfacial region, were not modelled due to a lack of interpretable electron density. In particular, the peptide chains connecting the NTD to the central domain (residues 286–307), strands β7 to β8 (residues 358–364), strands β8 to β9 (residues 376–392) and strand β18 to the catalytic domain (residues 654–668) were not visible in the electron density.","type":"Results"},{"text":"The assessed protein is the processed version generated after self-protein splicing due to its intein activity.","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"5IJL"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":286,"end":307,"reference_id":"27548043","reference_source":"pmid","reference_html":"Shared active site architecture between archaeal PolD and multi-subunit RNA polymerases revealed by X-ray crystallography. <i> Sauguet L, Raia P, Henneke G, Delarue M. </i> Nat Commun, 2016","date":"2026-05-12T15:43:19.985Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Cys955_Gln1139del","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"5IJL"}],"region_id":"DP04272r005","statement":[{"text":"As a consequence of this flexibility, several fragments of the peptide chains, all located within this interfacial region, were not modelled due to a lack of interpretable electron density. In particular, the peptide chains connecting the NTD to the central domain (residues 286–307), strands β7 to β8 (residues 358–364), strands β8 to β9 (residues 376–392) and strand β18 to the catalytic domain (residues 654–668) were not visible in the electron density.","type":"Results"},{"text":"The assessed protein is the processed version generated after self-protein splicing due to its intein activity.","type":"Curator statement"}]},{"start":324,"end":338,"reference_id":"27548043","reference_source":"pmid","reference_html":"Shared active site architecture between archaeal PolD and multi-subunit RNA polymerases revealed by X-ray crystallography. <i> Sauguet L, Raia P, Henneke G, Delarue M. </i> Nat Commun, 2016","date":"2026-05-12T15:44:49.237Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Cys955_Gln1139del","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"5IJL"}],"region_id":"DP04272r006","statement":[{"text":"As a consequence of this flexibility, several fragments of the peptide chains, all located within this interfacial region, were not modelled due to a lack of interpretable electron density. In particular, the peptide chains connecting the NTD to the central domain (residues 286–307), strands β7 to β8 (residues 358–364), strands β8 to β9 (residues 376–392) and strand β18 to the catalytic domain (residues 654–668) were not visible in the electron density.","type":"Results"},{"text":"The assessed protein is the processed version generated after self-protein splicing due to its intein activity.","type":"Curator statement"},{"text":"While not mention in the publication, this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":376,"end":392,"reference_id":"27548043","reference_source":"pmid","reference_html":"Shared active site architecture between archaeal PolD and multi-subunit RNA polymerases revealed by X-ray crystallography. <i> Sauguet L, Raia P, Henneke G, Delarue M. </i> Nat Commun, 2016","date":"2026-05-12T15:45:44.959Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Cys955_Gln1139del","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"5IJL"}],"region_id":"DP04272r007","statement":[{"text":"As a consequence of this flexibility, several fragments of the peptide chains, all located within this interfacial region, were not modelled due to a lack of interpretable electron density. In particular, the peptide chains connecting the NTD to the central domain (residues 286–307), strands β7 to β8 (residues 358–364), strands β8 to β9 (residues 376–392) and strand β18 to the catalytic domain (residues 654–668) were not visible in the electron density.","type":"Results"},{"text":"The assessed protein is the processed version generated after self-protein splicing due to its intein activity.","type":"Curator statement"}]},{"start":654,"end":668,"reference_id":"27548043","reference_source":"pmid","reference_html":"Shared active site architecture between archaeal PolD and multi-subunit RNA polymerases revealed by X-ray crystallography. <i> Sauguet L, Raia P, Henneke G, Delarue M. </i> Nat Commun, 2016","date":"2026-05-12T15:46:02.970Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Cys955_Gln1139del","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"5IJL"}],"region_id":"DP04272r008","statement":[{"text":"As a consequence of this flexibility, several fragments of the peptide chains, all located within this interfacial region, were not modelled due to a lack of interpretable electron density. In particular, the peptide chains connecting the NTD to the central domain (residues 286–307), strands β7 to β8 (residues 358–364), strands β8 to β9 (residues 376–392) and strand β18 to the catalytic domain (residues 654–668) were not visible in the electron density.","type":"Results"},{"text":"The assessed protein is the processed version generated after self-protein splicing due to its intein activity.","type":"Curator statement"}]},{"start":1380,"end":1455,"reference_id":"30657780","reference_source":"pmid","reference_html":"Structure of the DP1-DP2 PolD complex bound with DNA and its implications for the evolutionary history of DNA and RNA polymerases. <i> Raia P, Carroni M, Henry E, Pehau-Arnaudet G, Brûlé S, Béguin P, Henneke G, Lindahl E, Delarue M, Sauguet L. </i> PLoS Biol, 2019","date":"2026-05-12T17:06:42.098Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Cys955_Gln1139del","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"6HMS"}],"region_id":"DP04272r009","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9V2F3"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"A unit of 100 μM of template: 5′-ACTTTGACGCGGCCCGTCTC-3′ was mixed with 100 μM of primer: 5′-GAGACGGGCCGCGTC-3′ in the annealing buffer: 20 mM Tris HCl (pH 8), 10 mM MgCl2, and 1 mM EDTA; incubated for 5 min at 95°C; and slowly cooled to room temperature."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29034","entry_name":null}],"statement":[{"text":"Indeed, in the DP2 (1–1061) crystal structure, deletion of the CTD of DP2 causes a profound reorganization of the active site (Fig 3A): (1) the DPBB-1 domain is partly disordered and moves with respect to DPBB-2 from the canonical relative orientation of the two-DPBB catalytic center that is shared within all cellular transcriptases and full-length PolD, (2) clamp-1 and the accessory-1 domains are rotated by about 45° with respect to clamp-2, and (3) the KH-like domain moves by about 10 Å away from the catalytic center.","type":"Results"},{"text":"Two connecting loops (1149–1155) and (1171–1777) were omitted because of the lack of density. Secondary structures predictions from Jpred [27] of the P. abyssi PolD DP2–CTD are shown below the sequence alignment. (B) Structure of the DP1/DP2-CTD interface. Density surrounding the DP2–CTD is shown in gray mesh and contoured at 6 σ. Disordered loops are indicated by dotted blue lines.","type":"Figure"},{"text":"Several densities not covered by the crystal structures were observed in the catalytic core of DP2 and at the interface between DP1 and DP2 subunits. The C-terminal region of DP2 (1090–1195) dedicated to interaction with DP1 was built by homology modeling with the CTD of the catalytic subunit of human Polε [24] (PDB ID: 5VBN) using Phyre [36].","type":"Methods"},{"text":"The PDB-deposited data indicate that this region lacks electron density. As it appears to be part of the analyzed sample, the absence of electron density is likely due to its disordered nature, consistent with predicted data.","type":"Curator statement"}]},{"start":1224,"end":1257,"reference_id":"30657780","reference_source":"pmid","reference_html":"Structure of the DP1-DP2 PolD complex bound with DNA and its implications for the evolutionary history of DNA and RNA polymerases. <i> Raia P, Carroni M, Henry E, Pehau-Arnaudet G, Brûlé S, Béguin P, Henneke G, Lindahl E, Delarue M, Sauguet L. </i> PLoS Biol, 2019","date":"2026-05-12T17:06:57.611Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Cys955_Gln1139del","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"6HMS"}],"region_id":"DP04272r010","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9V2F3"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"A unit of 100 μM of template: 5′-ACTTTGACGCGGCCCGTCTC-3′ was mixed with 100 μM of primer: 5′-GAGACGGGCCGCGTC-3′ in the annealing buffer: 20 mM Tris HCl (pH 8), 10 mM MgCl2, and 1 mM EDTA; incubated for 5 min at 95°C; and slowly cooled to room temperature."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29034","entry_name":null}],"statement":[{"text":"Indeed, in the DP2 (1–1061) crystal structure, deletion of the CTD of DP2 causes a profound reorganization of the active site (Fig 3A): (1) the DPBB-1 domain is partly disordered and moves with respect to DPBB-2 from the canonical relative orientation of the two-DPBB catalytic center that is shared within all cellular transcriptases and full-length PolD, (2) clamp-1 and the accessory-1 domains are rotated by about 45° with respect to clamp-2, and (3) the KH-like domain moves by about 10 Å away from the catalytic center.","type":"Results"},{"text":"Two connecting loops (1149–1155) and (1171–1777) were omitted because of the lack of density. Secondary structures predictions from Jpred [27] of the P. abyssi PolD DP2–CTD are shown below the sequence alignment. (B) Structure of the DP1/DP2-CTD interface. Density surrounding the DP2–CTD is shown in gray mesh and contoured at 6 σ. Disordered loops are indicated by dotted blue lines.","type":"Figure"},{"text":"Several densities not covered by the crystal structures were observed in the catalytic core of DP2 and at the interface between DP1 and DP2 subunits. The C-terminal region of DP2 (1090–1195) dedicated to interaction with DP1 was built by homology modeling with the CTD of the catalytic subunit of human Polε [24] (PDB ID: 5VBN) using Phyre [36].","type":"Methods"},{"text":"The PDB-deposited data indicate that this region lacks electron density. As it appears to be part of the analyzed sample, the absence of electron density is likely due to its disordered nature, consistent with predicted data.","type":"Curator statement"}]},{"start":1183,"end":1195,"reference_id":"30657780","reference_source":"pmid","reference_html":"Structure of the DP1-DP2 PolD complex bound with DNA and its implications for the evolutionary history of DNA and RNA polymerases. <i> Raia P, Carroni M, Henry E, Pehau-Arnaudet G, Brûlé S, Béguin P, Henneke G, Lindahl E, Delarue M, Sauguet L. </i> PLoS Biol, 2019","date":"2026-05-12T17:07:15.373Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Cys955_Gln1139del","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"6HMS"}],"region_id":"DP04272r011","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9V2F3"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"A unit of 100 μM of template: 5′-ACTTTGACGCGGCCCGTCTC-3′ was mixed with 100 μM of primer: 5′-GAGACGGGCCGCGTC-3′ in the annealing buffer: 20 mM Tris HCl (pH 8), 10 mM MgCl2, and 1 mM EDTA; incubated for 5 min at 95°C; and slowly cooled to room temperature."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29034","entry_name":null}],"statement":[{"text":"Indeed, in the DP2 (1–1061) crystal structure, deletion of the CTD of DP2 causes a profound reorganization of the active site (Fig 3A): (1) the DPBB-1 domain is partly disordered and moves with respect to DPBB-2 from the canonical relative orientation of the two-DPBB catalytic center that is shared within all cellular transcriptases and full-length PolD, (2) clamp-1 and the accessory-1 domains are rotated by about 45° with respect to clamp-2, and (3) the KH-like domain moves by about 10 Å away from the catalytic center.","type":"Results"},{"text":"Two connecting loops (1149–1155) and (1171–1777) were omitted because of the lack of density. Secondary structures predictions from Jpred [27] of the P. abyssi PolD DP2–CTD are shown below the sequence alignment. (B) Structure of the DP1/DP2-CTD interface. Density surrounding the DP2–CTD is shown in gray mesh and contoured at 6 σ. Disordered loops are indicated by dotted blue lines.","type":"Figure"},{"text":"Several densities not covered by the crystal structures were observed in the catalytic core of DP2 and at the interface between DP1 and DP2 subunits. The C-terminal region of DP2 (1090–1195) dedicated to interaction with DP1 was built by homology modeling with the CTD of the catalytic subunit of human Polε [24] (PDB ID: 5VBN) using Phyre [36].","type":"Methods"},{"text":"The PDB-deposited data indicate that this region lacks electron density. As it appears to be part of the analyzed sample, the absence of electron density is likely due to its disordered nature, consistent with predicted data.","type":"Curator statement"}]},{"start":1382,"end":1387,"reference_id":"32221299","reference_source":"pmid","reference_html":"Structural basis for the increased processivity of D-family DNA polymerases in complex with PCNA. <i> Madru C, Henneke G, Raia P, Hugonneau-Beaufet I, Pehau-Arnaudet G, England P, Lindahl E, Delarue M, Carroni M, Sauguet L. </i> Nat Commun, 2020","date":"2026-05-12T17:44:02.698Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Cys955_Gln1139del","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"6T8H"}],"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"Q9UYX8","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04272r012","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9V2F3"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"The DNA duplex was prepared by mixing equivalent molar amounts of primer (5′-CGCCGGGCCGAGCCGTGC-3′) and template (5′-AGGTCGTGCACGGCTCGGCCCGGCG-3′)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29034","entry_name":null},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UYX8"}],"statement":[{"text":"First, the α-helices, α-40, and α-41 of the clamp-1 domain are connected by a loop of 17 amino acids, which is hooked into PCNA. This loop binds to the canonical PCNA PIP-binding pocket through an internal PIP-box (iPIP), which has never been identified so far (Fig. 3b). Six residues within this iPIP fill the PCNA PIP-binding pocket. Among them, the side chain of Q1198 penetrates deep into the pocket, making contacts with the canonical PCNA residue P245 (Fig. 3c). In addition, the bulky side chains of L1199, L1201, and I1202 make extensive contacts with hydrophobic residues, which line the PCNA PIP-binding pocket.","type":"Results"},{"text":"Numbering corresponds to a mutated version of the protein mimicking the processed version generated after self-protein splicing due to its intein activity. According to the UniProt sequence, the residues mentioned are Q1383, L1384, L1386 and I1387.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1402,"end":1441,"reference_id":"32221299","reference_source":"pmid","reference_html":"Structural basis for the increased processivity of D-family DNA polymerases in complex with PCNA. <i> Madru C, Henneke G, Raia P, Hugonneau-Beaufet I, Pehau-Arnaudet G, England P, Lindahl E, Delarue M, Carroni M, Sauguet L. </i> Nat Commun, 2020","date":"2026-05-12T18:01:43.403Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Cys955_Gln1139del","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"6T8H"}],"region_id":"DP04272r013","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9V2F3"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"The DNA duplex was prepared by mixing equivalent molar amounts of primer (5′-CGCCGGGCCGAGCCGTGC-3′) and template (5′-AGGTCGTGCACGGCTCGGCCCGGCG-3′)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29034","entry_name":null},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UYX8"}],"statement":[{"text":"In addition to the iPIP that was identified from our cryo-EM structure, the DP2 subunits of PolD from P. furiosus and P. abyssi have been shown to host a C-terminal PIP-box15,24. This second PIP-box (hereafter referred to as canonical PIP-box (cPIP)), is connected to DP2 by a 40-residue linker, which is variable in both length and amino-acid composition across archaea (Fig. 3b). Strikingly, both cPIP and the linker are not visible in the cryo-EM density of the DNA-bound PolD–PCNA complex.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":1441,"end":1449,"reference_id":"32221299","reference_source":"pmid","reference_html":"Structural basis for the increased processivity of D-family DNA polymerases in complex with PCNA. <i> Madru C, Henneke G, Raia P, Hugonneau-Beaufet I, Pehau-Arnaudet G, England P, Lindahl E, Delarue M, Carroni M, Sauguet L. </i> Nat Commun, 2020","date":"2026-05-12T18:03:37.873Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"cross_refs":[{"db":"PDB","id":"6T7Y"}],"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"Q9UYX8","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04272r014","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UYX8"}],"sequence_construct":"MRGSHHHHHHGSMPFEIVFEGAKEFAQLIETASRLIDEAAFKVTEEGISMRAMDPSRVVLIDLNLPASIFSKYEVDGEETIGVNMDHLKKVLKRGKAKETLILRKGEENFLEISLQGTATRTFKLPLIDVEEIEVDLPELPFTAKVVILGDVIKEAVKDASLVSDSMKFIAKENEFTMRAEGETQEVEVKLTLEDEGLLDIEVQEETKSAYGISYLSDMVKGLGKADEVTIKFGNEMPMQMEYYIRDEGRLIFLLAPRVEE","statement":[{"text":"To better characterize the role of cPIP, we co-crystallized PCNA from P. abyssi with a 12 amino-acid peptide mimicking the DP2 cPIP and solved its structure at 2.7 Å resolution (Supplementary Table 1 and Supplementary Fig. 5). The final model includes 9 of the 12 amino acids of the co-crystallized peptide. In contrast to the structure of iPIP, which differs from other structures of PIP-boxes, cPIP shares the same overall fold (Fig. 3d) as those described in the literature28. Hence, the cPIP structure shows an extended peptide chain, whose C-terminal region folds into a 310 helix.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1383,"end":1387,"reference_id":"32221299","reference_source":"pmid","reference_html":"Structural basis for the increased processivity of D-family DNA polymerases in complex with PCNA. <i> Madru C, Henneke G, Raia P, Hugonneau-Beaufet I, Pehau-Arnaudet G, England P, Lindahl E, Delarue M, Carroni M, Sauguet L. </i> Nat Commun, 2020","date":"2026-05-13T14:47:18.665Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003887","term_name":"DNA-directed DNA polymerase activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gln1383I1387del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04272r015","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9UYX8"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"Extension reactions of the fluorescent-labeled 32-mer primer 5′-Cy5-TGCCAAGCTTGCATGCCTGCAGGTCGACTCTA-3′ annealed to the single-stranded circular M13mp18 template (7 nM) were performed in 12.5 µl of 50 mM Tris (pH 8.0), 1 mM dithiothreitol, 50 mM NaCl, 5 mM MgCl2, and 200 µM each of dNTPs in the presence or absence of PCNA at the indicated concentrations."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9V2F3"}],"statement":[{"text":"Using primed-M13mp18 DNA template, PolD progressively became stimulated upon increasing the concentration of PCNA. At 300 nM PCNA, the maximum amount of full-length DNA products was reached. However, full-length DNA synthesis by PolDΔiPIP-ΔcPIP, devoid of both C-terminal PIP-boxes, was never obtained upon increasing PCNA concentrations even at 300 nM PCNA.","type":"Results"},{"text":"Albeit the C-terminal cPIP is important for the physical interaction with PCNA (see below) (Fig. 4c, d), these results show that the cPIP is dispensable for full-length DNA synthesis by the PolD–PCNA complex in vitro. Altogether, these results show that iPIP, but not cPIP, is required for full-length DNA synthesis by the PolD–PCNA complex.","type":"Results"}],"term_comment":"","term_def":"\"Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); the synthesis of DNA from deoxyribonucleotide triphosphates in the presence of a DNA template and a 3'hydroxyl group.\" [EC:2.7.7.7, GOC:vw, ISBN:0198547684]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":1381,"end":1452,"reference_id":"32221299","reference_source":"pmid","reference_html":"Structural basis for the increased processivity of D-family DNA polymerases in complex with PCNA. <i> Madru C, Henneke G, Raia P, Hugonneau-Beaufet I, Pehau-Arnaudet G, England P, Lindahl E, Delarue M, Carroni M, Sauguet L. </i> Nat Commun, 2020","date":"2026-05-13T14:36:21.220Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007736","ec_ontology":"ECO","ec_name":"molecule detection assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9UYX8","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9V291","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9V292","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP04272r016","statement":[{"text":"To assess the role of the C terminus of PolD in the interactions with PCNA and primase, we performed biolayer interferometry (BLI) experiments using His6-tagged maltose-binding protein (MBP) fusions of the C-terminal region of DP2, which were captured via surface-linked Ni-NTA. As expected, the MBP–iPIP-cPIP fusion (DP2:1196–1270) was found to readily bind to PCNA, with a KD of 472 ± 120 nM (Fig. 4c). Interestingly, the same construct was also able to interact with primase, with a measured KD of 237 ± 22 nM (Fig. 5a), which is very similar to the KD of 245 nM that was reported for the interaction within the C terminus of yeast Polα and the primase42.","type":"Results"},{"text":"In archaea and eukaryotes, the primase forms a heterodimer composed of a small PriS subunit with the polymerase activity and a larger regulatory PriL subunit.","type":"Results"},{"text":"Numbering corresponds to a mutated version of the protein mimicking the processed version generated after self-protein splicing due to its intein activity. According to the UniProt sequence, the region mentioned here is 1381–1455.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":1440,"end":1451,"reference_id":"30657780","reference_source":"pmid","reference_html":"Structure of the DP1-DP2 PolD complex bound with DNA and its implications for the evolutionary history of DNA and RNA polymerases. <i> Raia P, Carroni M, Henry E, Pehau-Arnaudet G, Brûlé S, Béguin P, Henneke G, Lindahl E, Delarue M, Sauguet L. </i> PLoS Biol, 2019","date":"2026-05-13T14:44:29.474Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001269","ec_ontology":"ECO","ec_name":"surface plasmon resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9UYX8","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9V291","operator":"or","partner_start":null,"partner_end":null},{"db":"UniProt","id":"Q9V292","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04272r017","statement":[{"text":"The cPIP binds to PCNA with a lower affinity (KD of 49 ± 4 μM), which differs by two orders of magnitude from the one observed for the MBP–iPIP–cPIP fusion (Supplementary Fig. 7), suggesting that the flanking region may be important for binding to PCNA.","type":"Results"},{"text":"Interestingly, cPIP binds to the primase substantially better than to PCNA, with a KD of 4.0 ± 1 μM (Fig. 5c). ","type":"Results"},{"text":"In archaea and eukaryotes, the primase forms a heterodimer composed of a small PriS subunit with the polymerase activity and a larger regulatory PriL subunit.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1381,"end":1452,"reference_id":"30657780","reference_source":"pmid","reference_html":"Structure of the DP1-DP2 PolD complex bound with DNA and its implications for the evolutionary history of DNA and RNA polymerases. <i> Raia P, Carroni M, Henry E, Pehau-Arnaudet G, Brûlé S, Béguin P, Henneke G, Lindahl E, Delarue M, Sauguet L. </i> PLoS Biol, 2019","date":"2026-05-13T14:53:57.709Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006270","term_name":"DNA replication initiation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04272r018","statement":[{"text":"Using primed-M13mp18 DNA template, PolD progressively became stimulated upon increasing the concentration of PCNA. At 300 nM PCNA, the maximum amount of full-length DNA products was reached. However, full-length DNA synthesis by PolDΔiPIP-ΔcPIP, devoid of both C-terminal PIP-boxes, was never obtained upon increasing PCNA concentrations even at 300 nM PCNA.","type":"Results"},{"text":"The ability of cPIP to recruit both PCNA and primase is consistent with the dual role of PolD in DNA replication initiation and elongation, which requires interaction with both partners.","type":"Results"},{"text":"Indeed, our work shows that cPIP has overlapping specificities and is capable of binding both PCNA and primase. Hence, PolD must be able to interact with the primase during the initiation of DNA replication and with PCNA to ensure processive extension of both leading and lagging strands.","type":"Discussion"}],"term_comment":"","term_def":"\"The process in which DNA-dependent DNA replication is started; this begins with the ATP dependent loading of an initiator complex onto the DNA, this is followed by DNA melting and helicase activity. In bacteria, the gene products that enable the helicase activity are loaded after the initial melting and in archaea and eukaryotes, the gene products that enable the helicase activity are inactive when they are loaded and subsequently activate.\" [ISBN:071673706X, ISBN:0815316194, PMID:28209641]","term_is_obsolete":false,"term_not_annotate":false},{"start":1381,"end":1452,"reference_id":"30657780","reference_source":"pmid","reference_html":"Structure of the DP1-DP2 PolD complex bound with DNA and its implications for the evolutionary history of DNA and RNA polymerases. <i> Raia P, Carroni M, Henry E, Pehau-Arnaudet G, Brûlé S, Béguin P, Henneke G, Lindahl E, Delarue M, Sauguet L. </i> PLoS Biol, 2019","date":"2026-05-13T14:55:47.826Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006271","term_name":"DNA strand elongation involved in DNA replication","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04272r019","statement":[{"text":"Using primed-M13mp18 DNA template, PolD progressively became stimulated upon increasing the concentration of PCNA. At 300 nM PCNA, the maximum amount of full-length DNA products was reached. However, full-length DNA synthesis by PolDΔiPIP-ΔcPIP, devoid of both C-terminal PIP-boxes, was never obtained upon increasing PCNA concentrations even at 300 nM PCNA.","type":"Results"},{"text":"The ability of cPIP to recruit both PCNA and primase is consistent with the dual role of PolD in DNA replication initiation and elongation, which requires interaction with both partners.","type":"Results"},{"text":"Indeed, our work shows that cPIP has overlapping specificities and is capable of binding both PCNA and primase. Hence, PolD must be able to interact with the primase during the initiation of DNA replication and with PCNA to ensure processive extension of both leading and lagging strands.","type":"Discussion"}],"term_comment":"","term_def":"\"The process in which an existing DNA strand is extended by activities including the addition of nucleotides to the 3' end of the strand, complementary to an existing template, as part of DNA replication.\" [GOC:mah, ISBN:071673706X, ISBN:0815316194]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":19,"released":"2026_06","sequence":"MELPKEMEEYFEMLQREIDKAYEIAKKARAQGKDPSLDVEIPQATDMAGRVESLVGPPGVAKRIRELVKEYGKEIAALKIVDEIIEGKFGDLGSREKYAEQAVRTALAILTEGIVSAPIEGIANVKIKRNTWADNSEYLALYYAGPIRSSGGTAQALSVLVGDYVRRKLGLDRFKPSEKHIERMVEEVDLYHRAVTRLQYHPSPEEVRLAMRNIPIEITGEATDDVEVSHRDVPGVETNQLRGGAILVLAEGVLQKAKKLVKYIDKMGIEGWEWLKEFVEAKEKGEPKEEGKEESLAESTLEETKVEVDMGFYYSLYQKFKEEIAPSDKYAKEVIGGRPLFSDPSKPGGFRLRYGRSRASGFATWGINPATMILVDEFLAIGTQLKTERPGKGAVVTPVTTIEGPIVKLKDGSVLRVDDYNLALKVREDVEEILYLGDAVIAFGDFVENNQTLLPANYCEEWWILEFVKALKEIYEVHLEPFTENEEESIEEASDYLEIDPEFLKEMLRDPLRVKPPVELAIHFSEVLGIPLHPYYTLYWNSVEPKDVEKLWRLLKNYAEIEWSNFRGIKFAKKIVISQEKLGDSKRTLELLGLPHTVRDGNVIVDYPWAAALLTPLGNLNWEFMAKPLYATIDIINENNEIKLRDRGISWIGARMGRPEKAKERKMKPPVQVLFPIGLAGGSSRDIKKAAEEGKVAEVEIAFFKCPKCGHVGPEHLCPNCGTRKELLWVCPRCNAEYPESQAEGYNYTCPKCNVKLRPYAKRKIRPSELLNRAMENVKVYGVDKLKGVMGMTSGWKMPEPLEKGLLRAKNDVYVFKDGTIRFDATDAPITHFRPREIGVSVEKLRELGYTHDFEGKPLVSEDQIVELKPQDIILSKEAGRYLLKVAKFVDDLLEKFYGLPRFYNAEKMEDLIGHLVIGLAPHTSAGIVGRIIGFVDALVGYAHPYFHAAKRRNCFPGDTRILVQIDGVPQKITLRELYELFEDERYENMVYVRKKPKREIKVYSIDLETGKVVLTDIEDVIKAPATDHLIRFELEDGRSFETTVDHPVLVYENGRFIEKRAFEVKEGDKVLVSELELVEQSSSSQDNPKNENLGSPEHDQLLEIKNIKYVRANDDFVFSLNAKKYHNVIINENIVTHQCDGDEDAVMLLLDALLNFSRYYLPEKRGGKMDAPLVITTRLDPREVDSEVHNMDIVRYYPLEFYEATYELKSPKELVGVIERVEDRLGKPEMYYGLKFTHDTDDIALGPKMSLYKQLGDMEEKVRRQLEVAKRIRAVDEHGVAEKILNSHLIPDLRGNLRSFTRQEFRCVKCNTKFRRPPLNGKCPVCGGKIVLTVSKGAIEKYLGTAKMLVTEYNVKNYTRQRICLTERDIDSLFENVFPETQLTLIVNPNDICQRLVMARTGEVNKSGLLENLSNGSKKTEKAEKAEKPRKKSDEKPKKKRVISLEEFFSRKSK","taxonomy":["Archaea","Euryarchaeota","Thermococci","Thermococcales","Thermococcaceae","Pyrococcus"],"alphafold_very_low_content":0.06666666666666667,"disorder_content":0.14982817869415807,"disprot_consensus":{"full":[{"start":286,"end":307,"type":"D"},{"start":324,"end":338,"type":"D"},{"start":376,"end":392,"type":"D"},{"start":654,"end":668,"type":"D"},{"start":1075,"end":1100,"type":"D"},{"start":1183,"end":1195,"type":"D"},{"start":1224,"end":1257,"type":"D"},{"start":1380,"end":1455,"type":"D"}],"Structural state":[{"start":286,"end":307,"type":"D"},{"start":324,"end":338,"type":"D"},{"start":376,"end":392,"type":"D"},{"start":654,"end":668,"type":"D"},{"start":1075,"end":1100,"type":"D"},{"start":1183,"end":1195,"type":"D"},{"start":1224,"end":1257,"type":"D"},{"start":1380,"end":1455,"type":"D"}],"Disorder function":[{"start":286,"end":307,"type":"F"},{"start":1402,"end":1441,"type":"F"}],"Molecular function":[{"start":1381,"end":1452,"type":"F"}],"Biological process":[{"start":1381,"end":1452,"type":"F"}]}},{"disprot_id":"DP04273","acc":"P33609","creator":"vnugnes","date":"2024-11-14T13:33:11.065Z","features":{"pfam":[{"id":"PF00136","name":"DNA polymerase family B","start":779,"end":1231},{"id":"PF03104","name":"DNA polymerase family B, exonuclease domain","start":479,"end":714},{"id":"PF08996","name":"DNA Polymerase alpha zinc finger","start":1270,"end":1458},{"id":"PF12254","name":"DNA polymerase alpha subunit p180 N terminal","start":41,"end":102}],"gene3D":[]},"genes":[{"name":{"value":"Pola1"},"synonyms":[{"value":"Pola"}]}],"length":1465,"name":"DNA polymerase alpha catalytic subunit","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":1,"end":330,"reference_id":"33711210","reference_source":"pmid","reference_html":"The intrinsically disordered N-terminal region of mouse DNA polymerase alpha mediates its interaction with POT1a/b at telomeres. <i> Mizuno T, Hirabayashi K, Miyazawa S, Kobayashi Y, Shoji K, Kobayashi M, Hanaoka F, Imamoto N, Torigoe H. </i> Genes Cells, 2021","date":"2024-11-14T13:34:08.159Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007688","ec_ontology":"ECO","ec_name":"gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04273r001","statement":[{"text":"Notably, during purification of p180 (1–330; Figure 2a), the sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) band corresponding to p180 (1–330), with an expected molecular weight of 37.2211 kDa, migrated almost the same distance as a 50 kDa protein (Figure 1d).","type":"Results"}]},{"start":1,"end":330,"reference_id":"33711210","reference_source":"pmid","reference_html":"The intrinsically disordered N-terminal region of mouse DNA polymerase alpha mediates its interaction with POT1a/b at telomeres. <i> Mizuno T, Hirabayashi K, Miyazawa S, Kobayashi Y, Shoji K, Kobayashi M, Hanaoka F, Imamoto N, Torigoe H. </i> Genes Cells, 2021","date":"2024-11-14T13:34:34.052Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04273r002","statement":[{"text":"The CD spectra showed that p180 (1–330) was a random coiled protein without a typical alpha helix or beta sheet structure.","type":"Results"}]},{"start":220,"end":330,"reference_id":"33711210","reference_source":"pmid","reference_html":"The intrinsically disordered N-terminal region of mouse DNA polymerase alpha mediates its interaction with POT1a/b at telomeres. <i> Mizuno T, Hirabayashi K, Miyazawa S, Kobayashi Y, Shoji K, Kobayashi M, Hanaoka F, Imamoto N, Torigoe H. </i> Genes Cells, 2021","date":"2024-11-14T13:41:01.473Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005805","ec_ontology":"ECO","ec_name":"yeast 2-hybrid evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"Full-length POT1a was fused to the LexA DNA-binding domain as the bait, and the N-terminal region of p180 (1–330) was fused to the B42 AD transcriptional activation domain as the prey"}]}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q91WC1","operator":null,"partner_start":307,"partner_end":640}],"region_id":"DP04273r003","statement":[{"text":"Mouse POT1a was associated with the N-terminal region (1–330) of p180 (Figure 1a).","type":"Results"},{"text":"The N-terminally truncated POT1a mutant (307–640; Figure 1b) and the N-terminal fragment of p180 (220–330; Figure 1c) interacted with a similar affinity to the interaction between full-length POT1a and p180 (1–330). We conclude that POT1a (307–640) and p180 (220–330) are the interaction domains required for the POT1a-p180 interaction.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":330,"reference_id":"33711210","reference_source":"pmid","reference_html":"The intrinsically disordered N-terminal region of mouse DNA polymerase alpha mediates its interaction with POT1a/b at telomeres. <i> Mizuno T, Hirabayashi K, Miyazawa S, Kobayashi Y, Shoji K, Kobayashi M, Hanaoka F, Imamoto N, Torigoe H. </i> Genes Cells, 2021","date":"2024-11-14T13:44:13.727Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q91WC1","operator":null,"partner_start":314,"partner_end":640},{"db":"UniProt","id":"H7BX60","operator":"or","partner_start":313,"partner_end":640}],"region_id":"DP04273r004","statement":[{"text":"His-p180 (1–330) associated with GST-POT1a (314–640) and GST- POT1b (313–640), but not the GST tag alone, despite being present in excess (Figure 1d). Hence, each of the C-terminal fragments of POT1a (314–640) or POT1b (313–640) and the N-terminal fragment (1–330) of p180 were physically associated in vitro.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":4,"released":"2025_06","sequence":"MAPMHEEDCKLEASAVSDSGSFAASRARREKKSKKGRQEALERLKKAKAGEKYKYEVEDLTSVYEEVDEEQYSKLVQARQDDDWIVDDDGIGYVEDGREIFDDDLEDDALDTCGKGSDGKAHRKDRKDVKKPSVTKPNNIKAMFIASAGKKTTDKAVDLSKDDLLGDILQDLNTETAQITPPPVLIPKKKRSTGALLNPFSVHTPKAIPSGKPASPVLRNEPLLTPIPLKRAELAGELAQPECPEDEQELGVMEFEDGDFDESMDTEKVDEKPVTAKTWDQETEPVERVEHEADPERGTTSYLENFLPDVSCWDIDQDDESIPQEVQVDSSNLPLVKGADDEQVFQFYWLDAYEDPYNQPGVVFLFGKVWIESVKTHVSCCVMVKNIERTLYFLPREMKFDLNTGKETAIPVTMKDVYEEFDSKISAKYKIMKFKSKIVEKNYAFEIPDVPEKSEYLEVRYSAEVPQLPQNLKGETFSHVFGTNTSSLELFLMNRKIKGPCWLEVKNPQLLNQPISWCKFEVMALKPDLVNVIKDVSPPPLVVMSFSMKTMQNVQNHQHEIIAMAALVHHSFALDKAPPEPPFQTHFCVVSKPKDCIFPCDFKEVISKKNMKVEIAATERTLIGFFLAKVHKIDPDILVGHNICSFELEVLLQRINECKVPYWSKIGRLRRSNMPKLGSRSGFGERNATCGRMICDVEISAKELIHCKSYHLSELVQQILKTERIVIPTENIRNMYSESSYLLYLLEHIWKDARFILQIMCELNVLPLALQITNIAGNIMSRTLMGGRSERNEFLLLHAFYENNYIVPDKQIFRKPQQKLGDEDEEIDGDTNKYKKGRKKATYAGGLVLDPKVGFYDKFILLLDFNSLYPSIIQEFNICFTTVQRVTSEVQKATEDEEQEQIPELPDPNLEMGILPREIRKLVERRKQVKQLMKQQDLNPDLVLQYDIRQKALKLTANSMYGCLGFSYSRFYAKPLAALVTYKGREILMHTKDMVQKMNLEVIYGDTDSIMINTNSTNLEEVFKLGNKVKSEVNKLYKLLEIDIDAVFKSLLLLKKKKYAALVVEPTSDGNYITKQELKGLDIVRRDWCDLAKDTGNFVIGQILSDQSRDTIVENIQKRLIEIGENVLNGSVPVSQFEINKALTKDPQDYPDRKSLPHVHVALWINSQGGRKVKAGDTVSYVICQDGSNLTATQRAYAPEQLQKLDNLAIDTQYYLAQQIHPVVARICEPIDGIDAVLIALWLGLDSTQFRVHQYHKDEENDALLGGPAQLTDEEKYKDCEKFKCLCPSCGTENIYDNVFEGSGLDMEPSLYRCSNVDCKVSPLTFMVQLSNKLIMDIRRCIKKYYDGWLICEEPTCCSRLRRLPLHFSRNGPLCPVCMKAVLRPEYSDKSLYTQLCFYRYIFDADCALEKLTEHEKDKLKKQFFPLRVLQDYRKVKNIAEQFLSWSGYSEVNLSKLFANYAGKS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"alphafold_very_low_content":0.2334470989761092,"disorder_content":0.22525597269624573,"disprot_consensus":{"full":[{"start":1,"end":330,"type":"D"}],"Structural state":[{"start":1,"end":330,"type":"D"}],"Molecular function":[{"start":1,"end":330,"type":"F"}]}},{"disprot_id":"DP04274","acc":"Q9Y2G2","creator":"vnugnes","date":"2024-11-14T13:59:21.180Z","features":{"pfam":[{"id":"PF00619","name":"Caspase recruitment domain","start":453,"end":535},{"id":"PF13553","name":"Function to find","start":174,"end":307},{"id":"PF23679","name":"UPA-FIIND domain","start":315,"end":432}],"gene3D":[]},"genes":[{"name":{"value":"CARD8","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11821383","url":"http://www.ncbi.nlm.nih.gov/pubmed/11821383","alternativeUrl":"https://europepmc.org/abstract/MED/11821383"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:17057","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:17057"}}]},"synonyms":[{"value":"DACAR","evidences":[{"code":"ECO:0000303","source":{"name":"Citation","id":"Ref.4","url":"https://www.uniprot.org/uniprot/null#ref4"}}]},{"value":"KIAA0955","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10231032","url":"http://www.ncbi.nlm.nih.gov/pubmed/10231032","alternativeUrl":"https://europepmc.org/abstract/MED/10231032"}}]},{"value":"NDPP1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11956601","url":"http://www.ncbi.nlm.nih.gov/pubmed/11956601","alternativeUrl":"https://europepmc.org/abstract/MED/11956601"}}]}]}],"length":537,"name":"Caspase recruitment domain-containing protein 8","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":162,"reference_id":"33053349","reference_source":"pmid","reference_html":"Activation of the CARD8 Inflammasome Requires a Disordered Region. <i> Chui AJ, Griswold AR, Taabazuing CY, Orth EL, Gai K, Rao SD, Ball DP, Hsiao JC, Bachovchin DA. </i> Cell Rep, 2020","date":"2024-11-14T14:35:52.194Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04274r001","statement":[{"text":"CARD8 only has a predicted N-terminal ~160-amino-acid-long unstructured region followed by a FIIND and a CARD (Figure 1A; Figure S1B).","type":"Introduction"},{"text":"(A) Diagram of human CARD8 (above) and its predicted disorder (below) as determined by the Sequence-Based Prediction of Disordered Residues for Proteins (SPOT-Disorder) program (Hanson et al., 2017).","type":"Figure"},{"text":"Consistent with these computational assessments, we observed that limited proteolysis of full-length MTMR1, D2HGDH, and CARD8 with trypsin or proteinase K resulted in rapid protein digestion (Figure 4B). In contrast, truncated proteins lacking the predicted disordered N-terminal regions were more stable under protease treatment (Figure 4B).","type":"Results"},{"text":"When the protein is lacking the first 162 residues it becomes more stable to proteolysis. The fact that this N-terminal region is prone to proteolysis, combined with the result of disorder predictors allows us to identify this region as disordered.","type":"Curator statement"}]},{"start":1,"end":162,"reference_id":"33053349","reference_source":"pmid","reference_html":"Activation of the CARD8 Inflammasome Requires a Disordered Region. <i> Chui AJ, Griswold AR, Taabazuing CY, Orth EL, Gai K, Rao SD, Ball DP, Hsiao JC, Bachovchin DA. </i> Cell Rep, 2020","date":"2024-11-14T14:15:07.386Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04274r002","statement":[{"text":"CARD8 only has a predicted N-terminal ~160-amino-acid-long unstructured region followed by a FIIND and a CARD (Figure 1A; Figure S1B).","type":"Introduction"},{"text":"(A) Diagram of human CARD8 (above) and its predicted disorder (below) as determined by the Sequence-Based Prediction of Disordered Residues for Proteins (SPOT-Disorder) program (Hanson et al., 2017).","type":"Figure"},{"text":"Consistent with these computational assessments, we observed that limited proteolysis of full-length MTMR1, D2HGDH, and CARD8 with trypsin or proteinase K resulted in rapid protein digestion (Figure 4B). In contrast, truncated proteins lacking the predicted disordered N-terminal regions were more stable under protease treatment (Figure 4B).","type":"Results"}]},{"start":1,"end":162,"reference_id":"33053349","reference_source":"pmid","reference_html":"Activation of the CARD8 Inflammasome Requires a Disordered Region. <i> Chui AJ, Griswold AR, Taabazuing CY, Orth EL, Gai K, Rao SD, Ball DP, Hsiao JC, Bachovchin DA. </i> Cell Rep, 2020","date":"2024-11-14T14:22:40.303Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0050729","term_name":"positive regulation of inflammatory response","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1Phe161del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To investigate the function of the putative disordered region of CARD8, we transiently transfected constructs encoding either full-length CARD8 (isoform 5, the longest isoform) or the ZU5-UPA-CARD (ZUC) domains of CARD8 (starting at residue 162) into HEK293T cells stably expressing CASP1 and GSDMD."}]}],"ec_go":"IMP","region_id":"DP04274r003","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"However, VbP induced GSDMD cleavage and lactate dehydrogenase (LDH) release only in cells expressing full-length CARD8 (Figures 1B and 1C), indicating that the predicted disordered region of CARD8 plays a functional role in VbP-induced inflammasome activation.","type":"Results"}],"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of the inflammatory response.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":162,"reference_id":"33053349","reference_source":"pmid","reference_html":"Activation of the CARD8 Inflammasome Requires a Disordered Region. <i> Chui AJ, Griswold AR, Taabazuing CY, Orth EL, Gai K, Rao SD, Ball DP, Hsiao JC, Bachovchin DA. </i> Cell Rep, 2020","date":"2024-11-14T14:46:14.758Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031648","term_name":"protein destabilization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IMP","region_id":"DP04274r004","statement":[{"text":"We discovered that VbP only induced the degradation of the full-length proteins (Figure 4C), demonstrating that the predicted disordered regions are required for the degradation of all three proteins.","type":"Results"}],"term_comment":"","term_def":"\"Any process that decreases the stability of a protein, making it more vulnerable to degradative processes or aggregation.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1Leu162del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"We next ectopically expressed full-length or N-terminally truncated MTMR1, D2HGDH, and CARD8 in HEK293T cells."}]}],"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}]}],"regions_counter":4,"released":"2025_06","sequence":"MEKKECPEKSSSSEEELPRRDSGSSRNIDASKLIRLQGSRKLLVDNSIRELQYTKTGIFFQAEACVTNDTVYRELPCVSETLCDISHFFQEDDETEAEPLLFRAVPECQLSGGDIPSVSEEQESSEGQDSGDICSEENQIVSSYASKVCFEIEEDYKNRQFLGPEGNVDVELIDKSTNRYSVWFPTAGWYLWSATGLGFLVRDEVTVTIAFGSWSQHLALDLQHHEQWLVGGPLFDVTAEPEEAVAEIHLPHFISLQAGEVDVSWFLVAHFKNEGMVLEHPARVEPFYAVLESPSFSLMGILLRIASGTRLSIPITSNTLIYYHPHPEDIKFHLYLVPSDALLTKAIDDEEDRFHGVRLQTSPPMEPLNFGSSYIVSNSANLKVMPKELKLSYRSPGEIQHFSKFYAGQMKEPIQLEITEKRHGTLVWDTEVKPVDLQLVAASAPPPFSGAAFVKENHRQLQARMGDLKGVLDDLQDNEVLTENEKELVEQEKTRQSKNEALLSMVEKKGDLALDVLFRSISERDPYLVSYLRQQNL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.31098696461824954,"disorder_content":0.3016759776536313,"disprot_consensus":{"full":[{"start":1,"end":162,"type":"D"}],"Structural state":[{"start":1,"end":162,"type":"D"}],"Disorder function":[{"start":1,"end":162,"type":"F"}],"Biological process":[{"start":1,"end":162,"type":"F"}]}},{"disprot_id":"DP04275","acc":"Q84T68","creator":"zskalman","date":"2024-11-14T13:59:43.636Z","features":{"pfam":[{"id":"PF01138","name":"3' exoribonuclease family, domain 1","start":13,"end":133}],"gene3D":[]},"genes":[{"name":{"value":"RRP46"},"olnNames":[{"value":"Os03g0854200"},{"value":"LOC_Os03g63720"}]}],"length":238,"name":"Exosome complex exonuclease RRP46 homolog","ncbi_taxon_id":39947,"organism":"Oryza sativa subsp. japonica","regions":[{"start":177,"end":191,"reference_id":"20660080","reference_source":"pmid","reference_html":"Structural and biochemical characterization of CRN-5 and Rrp46: an exosome component participating in apoptotic DNA degradation. <i> Yang CC, Wang YT, Hsiao YY, Doudeva LG, Kuo PH, Chow SY, Yuan HS. </i> RNA, 2010","date":"2024-11-14T14:05:17.681Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"3HKM"}],"region_id":"DP04275r001","statement":[{"text":"No observable electron density for the region.","type":"Curator statement"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"sequence_construct":"MEESRADGRNPNQLRPFSCTRNPLDRAHGSARWAQGDTIVLAAVYGPKPGTRKGENPEKASIEVVWKPMTGQIGKQEKEYEMTLKRTLQSICLLTVHPNTTTSVILQVVGNDGSLLPCAINACCAALVFAGIPLKHLAVAIGCGVLEDGEVILDTNKAEEQQLKSFAHLVFPNSRKSASSKEPNQKEEDSERGLITSITHGVMSEEDYFSCIERGLAASSRISDFMRTTLQKQAPGDVLEHHHHHH","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-11-14T17:54:13.133Z"}}],"regions_counter":1,"released":"2025_06","sequence":"MEESRADGRNPNQLRPFSCTRNPLDRAHGSARWAQGDTIVLAAVYGPKPGTRKGENPEKASIEVVWKPMTGQIGKQEKEYEMTLKRTLQSICLLTVHPNTTTSVILQVVGNDGSLLPCAINACCAALVFAGIPLKHLAVAIGCGVLEDGEVILDTNKAEEQQLKSFAHLVFPNSRKSASSKEPNQKEEDSERGLITSITHGVMSEEDYFSCIERGLAASSRISDFMRTTLQKQAPGDV","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","BOP clade","Oryzoideae","Oryzeae","Oryzinae","Oryza","Oryza sativa"],"alphafold_very_low_content":0.09663865546218488,"dataset":["RNA-binding proteins"],"disorder_content":0.06302521008403361,"disprot_consensus":{"full":[{"start":177,"end":191,"type":"D"}],"Structural state":[{"start":177,"end":191,"type":"D"}]}},{"disprot_id":"DP04276","acc":"Q13613","creator":"vnugnes","date":"2024-11-14T14:26:23.955Z","features":{"pfam":[{"id":"PF02893","name":"GRAM domain","start":103,"end":206},{"id":"PF06602","name":"Myotubularin-like phosphatase domain","start":213,"end":549}],"gene3D":[]},"genes":[{"name":{"value":"MTMR1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:7449","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:7449"}}]}}],"length":665,"name":"Phosphatidylinositol-3-phosphate phosphatase MTMR1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":94,"reference_id":"33053349","reference_source":"pmid","reference_html":"Activation of the CARD8 Inflammasome Requires a Disordered Region. <i> Chui AJ, Griswold AR, Taabazuing CY, Orth EL, Gai K, Rao SD, Ball DP, Hsiao JC, Bachovchin DA. </i> Cell Rep, 2020","date":"2024-11-14T14:36:10.983Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04276r001","statement":[{"text":"MTMR1, D2HGDH, and other significantly depleted proteins have predicted disordered regions (Figure 4A; Figure S4A). Consistent with these computational assessments, we observed that limited proteolysis of full-length MTMR1, D2HGDH, and CARD8 with trypsin or proteinase K resulted in rapid protein digestion (Figure 4B). In contrast, truncated proteins lacking the predicted disordered N-terminal regions were more stable under protease treatment (Figure 4B).","type":"Results"},{"text":"When the protein is lacking the first 94 residues it becomes more stable to proteolysis. The fact that this N-terminal region is prone to proteolysis, combined with the result of disorder predictors allows us to identify this region as disordered. ","type":"Curator statement"}]},{"start":1,"end":94,"reference_id":"33053349","reference_source":"pmid","reference_html":"Activation of the CARD8 Inflammasome Requires a Disordered Region. <i> Chui AJ, Griswold AR, Taabazuing CY, Orth EL, Gai K, Rao SD, Ball DP, Hsiao JC, Bachovchin DA. </i> Cell Rep, 2020","date":"2024-11-14T14:36:22.259Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2024_12","version":0,"region_id":"DP04276r002","statement":[{"text":"Consistent with these computational assessments, we observed that limited proteolysis of full-length MTMR1, D2HGDH, and CARD8 with trypsin or proteinase K resulted in rapid protein digestion (Figure 4B). In contrast, truncated proteins lacking the predicted disordered N-terminal regions were more stable under protease treatment (Figure 4B).","type":"Results"},{"text":"When the protein is lacking the first 94 residues it becomes more stable to proteolysis. The fact that this N-terminal region is prone to proteolysis, combined with the result of disorder predictors allows us to identify this region as disordered. ","type":"Curator statement"}]},{"start":1,"end":94,"reference_id":"33053349","reference_source":"pmid","reference_html":"Activation of the CARD8 Inflammasome Requires a Disordered Region. <i> Chui AJ, Griswold AR, Taabazuing CY, Orth EL, Gai K, Rao SD, Ball DP, Hsiao JC, Bachovchin DA. </i> Cell Rep, 2020","date":"2024-11-14T14:43:52.184Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031648","term_name":"protein destabilization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2024_12","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1Gln94del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"We next ectopically expressed full-length or N-terminally truncated MTMR1, D2HGDH, and CARD8 in HEK293T cells."}]}],"ec_go":"IMP","region_id":"DP04276r003","statement":[{"text":"We discovered that VbP only induced the degradation of the full-length proteins (Figure 4C), demonstrating that the predicted disordered regions are required for the degradation of all three proteins.","type":"Results"}],"term_comment":"","term_def":"\"Any process that decreases the stability of a protein, making it more vulnerable to degradative processes or aggregation.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}]}],"regions_counter":3,"released":"2024_12","sequence":"MDRPAAAAAAGCEGGGGPNPGPAGGRRPPRAAGGATAGSRQPSVETLDSPTGSHVEWCKQLIAATISSQISGSVTSENVSRDYKALRDGNKLAQMEEAPLFPGESIKAIVKDVMYICPFMGAVSGTLTVTDFKLYFKNVERDPHFILDVPLGVISRVEKIGAQSHGDNSCGIEIVCKDMRNLRLAYKQEEQSKLGIFENLNKHAFPLSNGQALFAFSYKEKFPINGWKVYDPVSEYKRQGLPNESWKISKINSNYEFCDTYPAIIVVPTSVKDDDLSKVAAFRAKGRVPVLSWIHPESQATITRCSQPLVGPNDKRCKEDEKYLQTIMDANAQSHKLIIFDARQNSVADTNKTKGGGYESESAYPNAELVFLEIHNIHVMRESLRKLKEIVYPSIDEARWLSNVDGTHWLEYIRMLLAGAVRIADKIESGKTSVVVHCSDGWDRTAQLTSLAMLMLDSYYRTIKGFETLVEKEWISFGHRFALRVGHGNDNHADADRSPIFLQFVDCVWQMTRQFPSAFEFNELFLITILDHLYSCLFGTFLCNCEQQRFKEDVYTKTISLWSYINSQLDEFSNPFFVNYENHVLYPVASLSHLELWVNYYVRWNPRMRPQMPIHQNLKELLAVRAELQKRVEGLQREVATRAVSSSSERGSSPSHSATSVHTSV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.1593984962406015,"dataset":["Age-related disorders proteins"],"disorder_content":0.14135338345864662,"disprot_consensus":{"full":[{"start":1,"end":94,"type":"D"}],"Structural state":[{"start":1,"end":94,"type":"D"}],"Disorder function":[{"start":1,"end":94,"type":"F"}],"Biological process":[{"start":1,"end":94,"type":"F"}]}},{"disprot_id":"DP04277","acc":"Q8N465","creator":"vnugnes","date":"2024-11-14T14:32:11.700Z","features":{"pfam":[{"id":"PF01565","name":"FAD binding domain","start":101,"end":238},{"id":"PF02913","name":"FAD linked oxidases, C-terminal domain","start":275,"end":515}],"gene3D":[]},"genes":[{"name":{"value":"D2HGDH"},"synonyms":[{"value":"D2HGD"}]}],"length":521,"name":"D-2-hydroxyglutarate dehydrogenase, mitochondrial","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":51,"reference_id":"33053349","reference_source":"pmid","reference_html":"Activation of the CARD8 Inflammasome Requires a Disordered Region. <i> Chui AJ, Griswold AR, Taabazuing CY, Orth EL, Gai K, Rao SD, Ball DP, Hsiao JC, Bachovchin DA. </i> Cell Rep, 2020","date":"2024-11-14T14:36:36.151Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04277r001","statement":[{"text":"MTMR1, D2HGDH, and other significantly depleted proteins have predicted disordered regions (Figure 4A; Figure S4A). Consistent with these computational assessments, we observed that limited proteolysis of full-length MTMR1, D2HGDH, and CARD8 with trypsin or proteinase K resulted in rapid protein digestion (Figure 4B).","type":"Results"},{"text":"When the protein is lacking the first 51 residues it becomes more stable to proteolysis. The fact that this N-terminal region is prone to proteolysis, combined with the result of disorder predictors allows us to identify this region as disordered. ","type":"Curator statement"}]},{"start":1,"end":51,"reference_id":"33053349","reference_source":"pmid","reference_html":"Activation of the CARD8 Inflammasome Requires a Disordered Region. <i> Chui AJ, Griswold AR, Taabazuing CY, Orth EL, Gai K, Rao SD, Ball DP, Hsiao JC, Bachovchin DA. </i> Cell Rep, 2020","date":"2024-11-14T14:37:13.212Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04277r002","statement":[{"text":"MTMR1, D2HGDH, and other significantly depleted proteins have predicted disordered regions (Figure 4A; Figure S4A). Consistent with these computational assessments, we observed that limited proteolysis of full-length MTMR1, D2HGDH, and CARD8 with trypsin or proteinase K resulted in rapid protein digestion (Figure 4B).","type":"Results"},{"text":"When the protein is lacking the first 51 residues it becomes more stable to proteolysis. The fact that this N-terminal region is prone to proteolysis, combined with the result of disorder predictors allows us to identify this region as disordered. ","type":"Curator statement"}]},{"start":1,"end":51,"reference_id":"33053349","reference_source":"pmid","reference_html":"Activation of the CARD8 Inflammasome Requires a Disordered Region. <i> Chui AJ, Griswold AR, Taabazuing CY, Orth EL, Gai K, Rao SD, Ball DP, Hsiao JC, Bachovchin DA. </i> Cell Rep, 2020","date":"2024-11-14T14:41:31.400Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0031648","term_name":"protein destabilization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1Arg51del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"We next ectopically expressed full-length or N-terminally truncated MTMR1, D2HGDH, and CARD8 in HEK293T cells."}]}],"ec_go":"IMP","region_id":"DP04277r003","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"We discovered that VbP only induced the degradation of the full-length proteins (Figure 4C), demonstrating that the predicted disordered regions are required for the degradation of all three proteins.","type":"Results"}],"term_comment":"","term_def":"\"Any process that decreases the stability of a protein, making it more vulnerable to degradative processes or aggregation.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":3,"released":"2025_06","sequence":"MLPRRPLAWPAWLLRGAPGAAGSWGRPVGPLARRGCCSAPGTPEVPLTRERYPVRRLPFSTVSKQDLAAFERIVPGGVVTDPEALQAPNVDWLRTLRGCSKVLLRPRTSEEVSHILRHCHERNLAVNPQGGNTGMVGGSVPVFDEIILSTARMNRVLSFHSVSGILVCQAGCVLEELSRYVEERDFIMPLDLGAKGSCHIGGNVATNAGGLRFLRYGSLHGTVLGLEVVLADGTVLDCLTSLRKDNTGYDLKQLFIGSEGTLGIITTVSILCPPKPRAVNVAFLGCPGFAEVLQTFSTCKGMLGEILSAFEFMDAVCMQLVGRHLHLASPVQESPFYVLIETSGSNAGHDAEKLGHFLEHALGSGLVTDGTMATDQRKVKMLWALRERITEALSRDGYVYKYDLSLPVERLYDIVTDLRARLGPHAKHVVGYGHLGDGNLHLNVTAEAFSPSLLAALEPHVYEWTAGQQGSVSAEHGVGFRKRDVLGYSKPPGALQLMQQLKALLDPKGILNPYKTLPSQA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.08061420345489444,"dataset":["NDDs-related proteins"],"disorder_content":0.09788867562380038,"disprot_consensus":{"full":[{"start":1,"end":51,"type":"D"}],"Structural state":[{"start":1,"end":51,"type":"D"}],"Disorder function":[{"start":1,"end":51,"type":"F"}],"Biological process":[{"start":1,"end":51,"type":"F"}]}},{"disprot_id":"DP04278","acc":"Q9UMY1","creator":"vnugnes","date":"2024-11-14T14:55:23.559Z","features":{"pfam":[{"id":"PF08157","name":"NUC129 domain","start":172,"end":234}],"gene3D":[]},"genes":[{"name":{"value":"NOL7","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:21040","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:21040"}}]},"synonyms":[{"value":"C6orf90"},{"value":"NOP27"}]}],"length":257,"name":"U3 small nucleolar RNA-associated protein NOL7","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":94,"reference_id":"39126896","reference_source":"pmid","reference_html":"PQBP3/NOL7 is an intrinsically disordered protein. <i> Homma H, Ngo KX, Yoshioka Y, Tanaka H, Inotsume M, Fujita K, Ando T, Okazawa H. </i> Biochem Biophys Res Commun, 2024","date":"2024-11-14T15:10:50.675Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007013","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04278r001","statement":[{"text":"Both of a per residue model confidence score (pLDDT) and predicted aligned error (PAE) supported by AlphaFold expected that N-terminal region of human PQBP3/NOL7 was unstructured (Fig. 2b), similarly to the prediction by the IUPred2A.","type":"Results"},{"text":"Consistent with the predictions that PQBP3/NOL7 is an IDP, HS-AFM revealed that a large portion of the purified PQBP3/NOL7 protein outside of globular region (Fig. 3a), which moved dynamically in live imaging (Fig. 3b, Supplementary Movie 1).","type":"Results"},{"text":"Multiple bioinformatics analyses predict that N-terminal region of PQBP3 is unstructured. High-speed atomic force microscopy (HS-AFM) reveals that N-terminal region of PQBP3 is dynamically changed in the structure consistently with the predictions of the bioinformatics analyses.","type":"Abstract"},{"text":"Figure 4 shows the region the authors describe as an IDR is the 1-94 N-terminal region of the protein. ","type":"Curator statement"}]},{"start":1,"end":94,"reference_id":"39126896","reference_source":"pmid","reference_html":"PQBP3/NOL7 is an intrinsically disordered protein. <i> Homma H, Ngo KX, Yoshioka Y, Tanaka H, Inotsume M, Fujita K, Ando T, Okazawa H. </i> Biochem Biophys Res Commun, 2024","date":"2024-11-14T15:11:04.311Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007013","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04278r002","statement":[{"text":"Both of a per residue model confidence score (pLDDT) and predicted aligned error (PAE) supported by AlphaFold expected that N-terminal region of human PQBP3/NOL7 was unstructured (Fig. 2b), similarly to the prediction by the IUPred2A.","type":"Results"},{"text":"Consistent with the predictions that PQBP3/NOL7 is an IDP, HS-AFM revealed that a large portion of the purified PQBP3/NOL7 protein outside of globular region (Fig. 3a), which moved dynamically in live imaging (Fig. 3b, Supplementary Movie 1).","type":"Results"},{"text":"Multiple bioinformatics analyses predict that N-terminal region of PQBP3 is unstructured. High-speed atomic force microscopy (HS-AFM) reveals that N-terminal region of PQBP3 is dynamically changed in the structure consistently with the predictions of the bioinformatics analyses.","type":"Abstract"},{"text":"Figure 4 shows the region the authors describe as an IDR is the 1-94 N-terminal region of the protein. ","type":"Curator statement"}]}],"regions_counter":2,"released":"2025_06","sequence":"MVQLRPRASRAPASAEAMVDEGQLASEEEEAEHGLLLGQPSSGAAAEPLEEDEEGDDEFDDEAPEELTFASAQAEAREEERRVRETVRRDKTLLKEKRKRREELFIEQKKRKLLPDTILEKLTTASQTNIKKSPGKVKEVNLQKKNEDCEKGNDSKKVKVQKVQSVSQNKSYLAVRLKDQDLRDSRQQAAQAFIHNSLYGPGTNRTTVNKFLSLANKRLPVKRAAVQFLNNAWGIQKKQNAKRFKRRWMVRKMKTKK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.22178988326848248,"disorder_content":0.3657587548638132,"disprot_consensus":{"full":[{"start":1,"end":94,"type":"D"}],"Structural state":[{"start":1,"end":94,"type":"D"}],"Disorder function":[{"start":1,"end":94,"type":"F"}]}},{"disprot_id":"DP04279","acc":"P49815-5","creator":"vnugnes","date":"2024-11-14T15:19:57.446Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"TSC2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"7558029","url":"http://www.ncbi.nlm.nih.gov/pubmed/7558029","alternativeUrl":"https://europepmc.org/abstract/MED/7558029"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:12363","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:12363"}}]},"synonyms":[{"value":"TSC4"}]}],"length":1740,"name":"Isoform 5 of Tuberin","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":50,"end":126,"reference_id":"33436626","reference_source":"pmid","reference_html":"Structural insights into TSC complex assembly and GAP activity on Rheb. <i> Yang H, Yu Z, Chen X, Li J, Li N, Cheng J, Gao N, Yuan HX, Ye D, Guan KL, Xu Y. </i> Nat Commun, 2021","date":"2024-11-14T15:27:58.034Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7DL2"},{"db":"EMDB","id":"30708"}],"region_id":"DP04279r001","statement":[{"text":"Residues of TSC1 (876–971), TSC2 (127–936, 1015–1082, 1182–1245, 1494–1732), and TBC1D7 (21–287) were traced and modeled with a TSC2a region (residues 127–315) and TSC1 (residues 746–875) being replaced by poly alanine due to the relatively weak cryo-EM density (Fig. 1a and Supplementary Fig. 4).","type":"Results"},{"text":"Other TSC1 regions were invisible in our cryo-EM map due to flexibility.","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92574"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9P0N9"}]},{"start":644,"end":682,"reference_id":"33436626","reference_source":"pmid","reference_html":"Structural insights into TSC complex assembly and GAP activity on Rheb. <i> Yang H, Yu Z, Chen X, Li J, Li N, Cheng J, Gao N, Yuan HX, Ye D, Guan KL, Xu Y. </i> Nat Commun, 2021","date":"2024-11-14T15:28:24.010Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7DL2"},{"db":"EMDB","id":"30708"}],"region_id":"DP04279r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9P0N9"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92574"}],"statement":[{"text":"Residues of TSC1 (876–971), TSC2 (127–936, 1015–1082, 1182–1245, 1494–1732), and TBC1D7 (21–287) were traced and modeled with a TSC2a region (residues 127–315) and TSC1 (residues 746–875) being replaced by poly alanine due to the relatively weak cryo-EM density (Fig. 1a and Supplementary Fig. 4).","type":"Results"},{"text":"Other TSC1 regions were invisible in our cryo-EM map due to flexibility.","type":"Results"}]},{"start":937,"end":970,"reference_id":"33436626","reference_source":"pmid","reference_html":"Structural insights into TSC complex assembly and GAP activity on Rheb. <i> Yang H, Yu Z, Chen X, Li J, Li N, Cheng J, Gao N, Yuan HX, Ye D, Guan KL, Xu Y. </i> Nat Commun, 2021","date":"2024-11-14T15:28:49.257Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7DL2"},{"db":"EMDB","id":"30708"}],"region_id":"DP04279r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9P0N9"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92574"}],"statement":[{"text":"Residues of TSC1 (876–971), TSC2 (127–936, 1015–1082, 1182–1245, 1494–1732), and TBC1D7 (21–287) were traced and modeled with a TSC2a region (residues 127–315) and TSC1 (residues 746–875) being replaced by poly alanine due to the relatively weak cryo-EM density (Fig. 1a and Supplementary Fig. 4).","type":"Results"},{"text":"Other TSC1 regions were invisible in our cryo-EM map due to flexibility.","type":"Results"}]},{"start":1039,"end":1137,"reference_id":"33436626","reference_source":"pmid","reference_html":"Structural insights into TSC complex assembly and GAP activity on Rheb. <i> Yang H, Yu Z, Chen X, Li J, Li N, Cheng J, Gao N, Yuan HX, Ye D, Guan KL, Xu Y. </i> Nat Commun, 2021","date":"2024-11-14T15:28:59.948Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7DL2"},{"db":"EMDB","id":"30708"}],"region_id":"DP04279r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9P0N9"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92574"}],"statement":[{"text":"Residues of TSC1 (876–971), TSC2 (127–936, 1015–1082, 1182–1245, 1494–1732), and TBC1D7 (21–287) were traced and modeled with a TSC2a region (residues 127–315) and TSC1 (residues 746–875) being replaced by poly alanine due to the relatively weak cryo-EM density (Fig. 1a and Supplementary Fig. 4).","type":"Results"},{"text":"Other TSC1 regions were invisible in our cryo-EM map due to flexibility.","type":"Results"}]},{"start":1202,"end":1426,"reference_id":"33436626","reference_source":"pmid","reference_html":"Structural insights into TSC complex assembly and GAP activity on Rheb. <i> Yang H, Yu Z, Chen X, Li J, Li N, Cheng J, Gao N, Yuan HX, Ye D, Guan KL, Xu Y. </i> Nat Commun, 2021","date":"2024-11-14T15:29:12.410Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7DL2"},{"db":"EMDB","id":"30708"}],"region_id":"DP04279r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9P0N9"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92574"}],"statement":[{"text":"Residues of TSC1 (876–971), TSC2 (127–936, 1015–1082, 1182–1245, 1494–1732), and TBC1D7 (21–287) were traced and modeled with a TSC2a region (residues 127–315) and TSC1 (residues 746–875) being replaced by poly alanine due to the relatively weak cryo-EM density (Fig. 1a and Supplementary Fig. 4).","type":"Results"},{"text":"Other TSC1 regions were invisible in our cryo-EM map due to flexibility.","type":"Results"}]},{"start":1689,"end":1740,"reference_id":"33436626","reference_source":"pmid","reference_html":"Structural insights into TSC complex assembly and GAP activity on Rheb. <i> Yang H, Yu Z, Chen X, Li J, Li N, Cheng J, Gao N, Yuan HX, Ye D, Guan KL, Xu Y. </i> Nat Commun, 2021","date":"2024-11-14T15:29:23.950Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7DL2"},{"db":"EMDB","id":"30708"}],"region_id":"DP04279r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9P0N9"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92574"}],"statement":[{"text":"Residues of TSC1 (876–971), TSC2 (127–936, 1015–1082, 1182–1245, 1494–1732), and TBC1D7 (21–287) were traced and modeled with a TSC2a region (residues 127–315) and TSC1 (residues 746–875) being replaced by poly alanine due to the relatively weak cryo-EM density (Fig. 1a and Supplementary Fig. 4).","type":"Results"},{"text":"Other TSC1 regions were invisible in our cryo-EM map due to flexibility.","type":"Results"}]},{"start":1689,"end":1740,"reference_id":"33436626","reference_source":"pmid","reference_html":"Structural insights into TSC complex assembly and GAP activity on Rheb. <i> Yang H, Yu Z, Chen X, Li J, Li N, Cheng J, Gao N, Yuan HX, Ye D, Guan KL, Xu Y. </i> Nat Commun, 2021","date":"2024-11-14T15:33:20.163Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7DL2"},{"db":"EMDB","id":"30708"}],"region_id":"DP04279r007","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9P0N9"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92574"}],"statement":[{"text":"Residues of TSC1 (876–971), TSC2 (127–936, 1015–1082, 1182–1245, 1494–1732), and TBC1D7 (21–287) were traced and modeled with a TSC2a region (residues 127–315) and TSC1 (residues 746–875) being replaced by poly alanine due to the relatively weak cryo-EM density (Fig. 1a and Supplementary Fig. 4).","type":"Results"},{"text":"Other TSC1 regions were invisible in our cryo-EM map due to flexibility.","type":"Results"}]}],"regions_counter":7,"released":"2025_06","sequence":"MAKPTSKDSGLKEKFKILLGLGTPRPNPRSAEGKQTEFIITAEILRELSMECGLNNRIRMIGQICEVAKTKKFEEHAVEALWKAVADLLQPERPLEARHAVLALLKAIVQGQGERLGVLRALFFKVIKDYPSNEDLHERLEVFKALTDNGRHITYLEEELADFVLQWMDVGLSSEFLLVLVNLVKFNSCYLDEYIARMVQMICLLCVRTASSVDIEVSLQVLDAVVCYNCLPAESLPLFIVTLCRTINVKELCEPCWKLMRNLLGTHLGHSAIYNMCHLMEDRAYMEDAPLLRGAVFFVGMALWGAHRLYSLRNSPTSVLPSFYQAMACPNEVVSYEIVLSITRLIKKYRKELQVVAWDILLNIIERLLQQLQTLDSPELRTIVHDLLTTVEELCDQNEFHGSQERYFELVERCADQRPESSLLNLISYRAQSIHPAKDGWIQNLQALMERFFRSESRGAVRIKVLDVLSFVLLINRQFYEEELINSVVISQLSHIPEDKDHQVRKLATQLLVDLAEGCHTHHFNSLLDIIEKVMARSLSPPPELEERDVAAYSASLEDVKTAVLGLLVILQTKLYTLPASHATRVYEMLVSHIQLHYKHSYTLPIASSIRLQAFDFLLLLRADSLHRLGLPNKDGVVRFSPYCVCDYMEPERGSEKKTSGPLSPPTGPPGPAPAGPAVRLGSVPYSLLFRVLLQCLKQESDWKVLKLVLGRLPESLRYKVLIFTSPCSVDQLCSALCSMLSGPKTLERLRGAPEGFSRTDLHLAVVPVLTALISYHNYLDKTKQREMVYCLEQGLIHRCASQCVVALSICSVEMPDIIIKALPVLVVKLTHISATASMAVPLLEFLSTLARLPHLYRNFAAEQYASVFAISLPYTNPSKFNQYIVCLAHHVIAMWFIRCRLPFRKDFVPFITKGLRSNVLLSFDDTPEKDSFRARSTSLNERPKRIQTSLTSASLGSADENSVAQADDSLKNLHLELTETCLDMMARYVFSNFTAVPKRSPVGEFLLAGGRTKTWLVGNKLVTVTTSVGTGTRSLLGLDSGELQSGPESSSSPGVHVRQTKEAPAKLESQAGQQVSRGARDRVRSMSGGHGLRVGALDVPASQFLGSATSPGPRTAPAAKPEKASAGTRVPVQEKTNLAAYVPLLTQGWAEILVRRPTGNTSWLMSLENPLSPFSSDINNMPLQELSNALMAAERFKEHRDTALYKSLSVPAASTAKPPPLPRSNTDSAVVMEEGSPGEVPVLVEPPGLEDVEAALGMDRRTDAYSRSSSVSSQEEKSLHAEELVGRGIPIERVVSSEGGRPSVDLSFQPSQPLSKSSSSPELQTLQDILGDPGDKADVGRLSPEVKARSQSGTLDGESAAWSASGEDSRGQPEGPLPSSSPRSPSGLRPRGYTISDSAPSRRGKRVERDALKSRATASNAEKVPGINPSFVFLQLYHSPFFGDESNKPILLPNESQSFERSVQLLDQIPSYDTHKIAVLYVGEGQSNSELAILSNEHGSYRYTEFLTGLGRLIELKDCQPDKVYLGGLDVCGEDGQFTYCWHDDIMQAVFHIATLMPTKDVDKHRCDKKRHLGNDFVSIVYNDSGEDFKLGTIKGQFNFVHVIVTPLDYECNLVSLQCRKDMEGLVDTSVAKIVSDRNLPFVARQMALHANMASQVHHSRSNPTDIYPSKWIARLRHIKRLRQRICEEAAYSNPSLPLVHPPSHSKAPAQTPAEPTPGYEVGQRKRLISSVEDFTEFV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"disorder_content":0.3022988505747126,"disprot_consensus":{"full":[{"start":50,"end":126,"type":"D"},{"start":644,"end":682,"type":"D"},{"start":937,"end":970,"type":"D"},{"start":1039,"end":1137,"type":"D"},{"start":1202,"end":1426,"type":"D"},{"start":1689,"end":1740,"type":"D"}],"Structural state":[{"start":50,"end":126,"type":"D"},{"start":644,"end":682,"type":"D"},{"start":937,"end":970,"type":"D"},{"start":1039,"end":1137,"type":"D"},{"start":1202,"end":1426,"type":"D"},{"start":1689,"end":1740,"type":"D"}],"Disorder function":[{"start":1689,"end":1740,"type":"F"}]}},{"disprot_id":"DP04280","acc":"P19970","creator":"vnugnes","date":"2024-11-14T15:42:29.001Z","features":{"pfam":[{"id":"PF09421","name":"Frequency clock protein","start":13,"end":984}],"gene3D":[]},"genes":[{"name":{"value":"frq"},"orfNames":[{"value":"B13D24.170"},{"value":"NCU02265"}]}],"length":989,"name":"Frequency clock protein","ncbi_taxon_id":367110,"organism":"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)","regions":[{"start":1,"end":989,"reference_id":"38526948","reference_source":"pmid","reference_html":"Phosphorylation, disorder, and phase separation govern the behavior of Frequency in the fungal circadian clock. <i> Tariq D, Maurici N, Bartholomai BM, Chandrasekaran S, Dunlap JC, Bah A, Crane BR. </i> Elife, 2024","date":"2024-11-14T15:52:05.670Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04280r001","statement":[{"text":"SEC-coupled small-angle X-ray scattering (SAXS) analyses revealed that both p-FRQ and np-FRQ shared characteristics of highly flexible proteins, but that p-FRQ was more extended than np-FRQ (Table 1).","type":"Results"}]},{"start":1,"end":989,"reference_id":"38526948","reference_source":"pmid","reference_html":"Phosphorylation, disorder, and phase separation govern the behavior of Frequency in the fungal circadian clock. <i> Tariq D, Maurici N, Bartholomai BM, Chandrasekaran S, Dunlap JC, Bah A, Crane BR. </i> Elife, 2024","date":"2024-11-14T15:52:44.182Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008031","ec_ontology":"ECO","ec_name":"author inference based on intrinsic disorder prediction","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04280r002","statement":[{"text":"Analysis of an AlphaFold 2.0 (Jumper et al., 2021) model of full-length FRQ indicates that FRQ lacks a defined arrangement of large folded domains; instead, most of the molecule is unstructured (Figure 1B), in agreement with previous studies predicting that FRQ mostly comprises intrinsically disordered regions (Hurley et al., 2013).","type":"Results"},{"text":"Four regions distributed throughout the length of FRQ (residues 194–212, 312–329, 709–719, and 801–817) have at least 10% helical propensity, and these helical regions mostly agree with those of the AlphaFold model (Figure 1B).","type":"Results"}]},{"start":1,"end":989,"reference_id":"38526948","reference_source":"pmid","reference_html":"Phosphorylation, disorder, and phase separation govern the behavior of Frequency in the fungal circadian clock. <i> Tariq D, Maurici N, Bartholomai BM, Chandrasekaran S, Dunlap JC, Bah A, Crane BR. </i> Elife, 2024","date":"2024-11-14T15:58:07.451Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP04280r003","statement":[{"text":"Four regions distributed throughout the length of FRQ (residues 194–212, 312–329, 709–719, and 801–817) have at least 10% helical propensity, and these helical regions mostly agree with those of the AlphaFold model (Figure 1B).","type":"Results"},{"text":"Authors refer as p-FRQ to phosphorylated FRQ (p-FRQ), whereas non-phosphorylated FRQ is mention as np-FRQ.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":989,"reference_id":"38526948","reference_source":"pmid","reference_html":"Phosphorylation, disorder, and phase separation govern the behavior of Frequency in the fungal circadian clock. <i> Tariq D, Maurici N, Bartholomai BM, Chandrasekaran S, Dunlap JC, Bah A, Crane BR. </i> Elife, 2024","date":"2024-11-14T16:02:38.201Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001230","ec_ontology":"ECO","ec_name":"mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04280r004","statement":[{"text":"To generate phosphorylated FRQ, the protein was co-expressed with (untagged) CK1, which forms a stable complex with FRQ and acts as its primary kinase (Querfurth et al., 2011).","type":"Results"},{"text":"The latter revealed a network of >80 phosphorylation sites (Figure 1—figure supplement 2), most of which agree with those found on natively expressed FRQ (Baker et al., 2009; Tang et al., 2009).","type":"Results"},{"text":"The phosphorylation sites are well distributed across the entire protein.","type":"Curator statement"}]},{"start":1,"end":989,"reference_id":"38526948","reference_source":"pmid","reference_html":"Phosphorylation, disorder, and phase separation govern the behavior of Frequency in the fungal circadian clock. <i> Tariq D, Maurici N, Bartholomai BM, Chandrasekaran S, Dunlap JC, Bah A, Crane BR. </i> Elife, 2024","date":"2024-11-14T16:07:56.808Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006287","ec_ontology":"ECO","ec_name":"electron paramagnetic resonance evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04280r005","statement":[{"text":"cw-ESR reveals that FRQ has regions of varying order that agree with computational predictions and that some of these sites undergo phosphorylation-dependent conformational changes (Figure 3C).","type":"Results"},{"text":"Such traces are indicative of long inter-spin distances and conformational flexibility, which would be consistent with the large mobility and intrinsic disorder of these peripheral regions (Figure 3—figure supplement 2, Figure 4—figure supplement 1).","type":"Results"}]},{"start":1,"end":989,"reference_id":"38526948","reference_source":"pmid","reference_html":"Phosphorylation, disorder, and phase separation govern the behavior of Frequency in the fungal circadian clock. <i> Tariq D, Maurici N, Bartholomai BM, Chandrasekaran S, Dunlap JC, Bah A, Crane BR. </i> Elife, 2024","date":"2024-11-14T16:15:18.820Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q1K502","operator":null,"partner_start":100,"partner_end":1106},{"db":"UniProt","id":"V5IR38","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04280r006","statement":[{"text":"The FFC was generated by mixing p-FRQ or np-FRQ with excess FRH and CK1, followed by SEC purification to give p-FFC or np-FFC, respectively. FRHΔN (residues 100–1106), which binds FRQ, was used to improve expression and enhance stability (Conrad et al., 2016; Hurley et al., 2013). The resulting symmetric SEC traces and SDS-PAGE gels revealed pure and homogeneous ternary complexes in each case (Figure 4A).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":989,"reference_id":"38526948","reference_source":"pmid","reference_html":"Phosphorylation, disorder, and phase separation govern the behavior of Frequency in the fungal circadian clock. <i> Tariq D, Maurici N, Bartholomai BM, Chandrasekaran S, Dunlap JC, Bah A, Crane BR. </i> Elife, 2024","date":"2024-11-14T16:17:06.179Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q1K502","operator":null,"partner_start":100,"partner_end":1106},{"db":"UniProt","id":"V5IR38","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04280r007","statement":[{"text":"MW estimates of the p-FFC and np-FFC from SAXS indicate a 1:1 stoichiometry of FRQ:FRH, with a likely single component of CK1 also contained within the complex (Table 1).","type":"Results"},{"text":"SEC-SAXS analysis of the FFC showed that both FRQ phospho-forms produced complexes that were more globular than FRQ alone, but still somewhat flexible, with the p-FFC being more flexible than the np-FFC (Figure 4B, Figure 2—figure supplement 1).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":989,"reference_id":"38526948","reference_source":"pmid","reference_html":"Phosphorylation, disorder, and phase separation govern the behavior of Frequency in the fungal circadian clock. <i> Tariq D, Maurici N, Bartholomai BM, Chandrasekaran S, Dunlap JC, Bah A, Crane BR. </i> Elife, 2024","date":"2024-11-14T16:21:24.968Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007056","ec_ontology":"ECO","ec_name":"differential interference contrast microscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","region_id":"DP04280r008","statement":[{"text":"FRQ exhibits behavior consistent with LLPS in vitro and in vivo","type":"Results"},{"text":"We tested whether both np-FRQ and p-FRQ can undergo LLPS in vitro. In each case, upon exchanging the purified protein into their respective phase separation buffers (which lack any crowding agents), we observed the appearance of a turbid solution that contained microscopic droplets (Figure 6B). These droplets scaled in size and number with increasing protein concentration, dissolved upon the addition of 1,6-hexanediol, and were shown to dock and fuse to one another, thereby confirming their liquid-like properties (Figure 6B, Figure 7—figure supplement 1)","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":989,"reference_id":"38526948","reference_source":"pmid","reference_html":"Phosphorylation, disorder, and phase separation govern the behavior of Frequency in the fungal circadian clock. <i> Tariq D, Maurici N, Bartholomai BM, Chandrasekaran S, Dunlap JC, Bah A, Crane BR. </i> Elife, 2024","date":"2024-11-14T16:22:03.135Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006307","ec_ontology":"ECO","ec_name":"turbidity measurement evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","region_id":"DP04280r009","statement":[{"text":"FRQ exhibits behavior consistent with LLPS in vitro and in vivo","type":"Results"},{"text":"UV-Vis turbidity assays as a function of temperature revealed that FRQ undergoes a low critical solution temperature (LCST) phase transition that is concentration and phosphorylation status-dependent (Figure 6C, Figure 7—figure supplement 1, Tables 6 and 7).","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":989,"reference_id":"38526948","reference_source":"pmid","reference_html":"Phosphorylation, disorder, and phase separation govern the behavior of Frequency in the fungal circadian clock. <i> Tariq D, Maurici N, Bartholomai BM, Chandrasekaran S, Dunlap JC, Bah A, Crane BR. </i> Elife, 2024","date":"2024-11-14T16:29:13.440Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005634","term_name":"nucleus","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"ec_go":"IDA","region_id":"DP04280r010","statement":[{"text":"Live-cell imaging of N. crassa expressing FRQ tagged with the fluorescent protein mNeonGreen at its C-terminus (FRQmNeonGreen) revealed heterogeneous patterning of FRQ in nuclei (Figure 6D and E).","type":"Results"}],"term_comment":"","term_def":"\"A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":989,"reference_id":"38526948","reference_source":"pmid","reference_html":"Phosphorylation, disorder, and phase separation govern the behavior of Frequency in the fungal circadian clock. <i> Tariq D, Maurici N, Bartholomai BM, Chandrasekaran S, Dunlap JC, Bah A, Crane BR. </i> Elife, 2024","date":"2024-11-14T16:32:59.363Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140694","term_name":"non-membrane-bounded organelle assembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"ec_go":"IDA","region_id":"DP04280r011","statement":[{"text":"FRQ exhibits behavior consistent with LLPS in vitro and in vivo","type":"Results"},{"text":"Nonetheless, bright and dynamic foci-like spots were observed well inside the nucleus and near the nuclear periphery, which is delineated by the cytoplasm-facing nucleoporin Son-1 tagged with mApple at its C-terminus (Figure 6D and E, Video 1). Such foci are characteristic of phase-separated IDPs (Bartholomai et al., 2022b; Caragliano et al., 2022; Gonzalez et al., 2021; Tatavosian et al., 2019) and share similar patterning to that seen for clock proteins in Drosophila (Meyer et al., 2006; Xiao et al., 2021), although the foci we observed are substantially more dynamic than those reported in Drosophila.","type":"Results"}],"term_comment":"","term_def":"\"The aggregation, arrangement and bonding together of a set of components to form a non-membrane-bounded organelle.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":11,"released":"2025_06","sequence":"MADSGDKSQGMRPPPFDSRGHPLPRRASPDKSITLENHRLARDTSSRVTSSSALGVTESQPQLKSSPTRRNSSGESEPTNWFNQSNRNPAAAFHDESHIMEVDPPFYQKETDSSNEESRYPPGRNPVHPPGGVQLPGFRPVAAHSSAADDYRSVIDDLTVENKRLKEELKRYKQFGSDVMRKEKLFEIKVHGLPRRKKRELEATLRDFAASLGDSSESTSQRRKTGRHGTAVHSSGVSLSKHDSSSSSRSRPVDSAYNSMSTGRSSHAPHSSGPSLGRPSLTRAKSVGTQKVENYLRDTPDGLLPHHIVMTDKEKKKLVVRRLEQLFTGKISGRNMQRNQSMPSMDAPLAPEGTNMAPPRPPPEGLREACIQLQDGDNPRKNRSSKDNGSASNSGGDQTELGGTGTGSGDGSGSGGRTGNNTSPPGAIAPDQRPTRPRDLDPDRVQIPSENMDYIRHLGLVSPEFLQGSRTSYQDVAPDAEGWVYLNLLCNLAQLHMVNVTPSFIRQAVSEKSTKFQLSADGRKIRWRGGTDGTKFSSDSSEDKSQQSPMTEDTEDGSDKNGRRKKRKTQQASSEIGRFGPSRSPSDTFHYKPMFVHRNSSSIETSLEESMSQGSEDAVDESNMGNSKWDFSGSGTTQQRRKRRYDGAIVYYTGAPFCTDLSGDPGDMSPTAQMTAGREVEGSGSGDEVEHVLQRTLSGSSLPIRPLSDDRARVAEVLDFDPGNPPELVADDGSSPNDEDFVFPWCEDPAKVRIQPIAKEVMEPSGLGGVLPDDHFVMLVTTRRVVRPILQRQLSRSTTSEDTAEFIAERLAAIRTSSPLPPRSHRLTVAPLQVEYVSGQFRRLNPAPLPPPAIFYPPFSTDSSWDDGDDLASDDEEVEEVEEDSYSEGQISRRANPHFSDNNTYMRKDDLAFDTETDVRMDSDDNRLSDSGHNMRAMMPRAEAVDGDDSPLAAVTGKEVDMLHTGSSVATAGGAESGYSSSMEDVSSS","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Sordariomycetidae","Sordariales","Sordariaceae","Neurospora"],"alphafold_very_low_content":0.5773508594539939,"dataset":["Condensates-related proteins"],"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":989,"type":"D"}],"Structural state":[{"start":1,"end":989,"type":"D"}],"Molecular function":[{"start":1,"end":989,"type":"F"}],"Disorder function":[{"start":1,"end":989,"type":"F"}],"Cellular component":[{"start":1,"end":989,"type":"F"}],"Biological process":[{"start":1,"end":989,"type":"F"}]}},{"disprot_id":"DP04281","acc":"P68431","creator":"vnugnes","date":"2024-11-14T17:01:21.215Z","features":{"pfam":[{"id":"PF00125","name":"Core histone H2A/H2B/H3/H4 domain","start":44,"end":131}],"gene3D":[]},"genes":[{"name":{"value":"H3C1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4766","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4766"}}]},"synonyms":[{"value":"H3FA"},{"value":"HIST1H3A"}]},{"name":{"value":"H3C2","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4776","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4776"}}]},"synonyms":[{"value":"H3FL"},{"value":"HIST1H3B"}]},{"name":{"value":"H3C3","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4768","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4768"}}]},"synonyms":[{"value":"H3FC HIST1H3C"}]},{"name":{"value":"H3C4","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4767","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4767"}}]},"synonyms":[{"value":"H3FB"},{"value":"HIST1H3D"}]},{"name":{"value":"H3C6","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4769","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4769"}}]},"synonyms":[{"value":"H3FD"},{"value":"HIST1H3E"}]},{"name":{"value":"H3C7","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4773","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4773"}}]},"synonyms":[{"value":"H3FI"},{"value":"HIST1H3F"}]},{"name":{"value":"H3C8","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4772","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4772"}}]},"synonyms":[{"value":"H3FH"},{"value":"HIST1H3G"}]},{"name":{"value":"H3C10","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4775","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4775"}}]},"synonyms":[{"value":"H3FK"},{"value":"HIST1H3H"}]},{"name":{"value":"H3C11","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4771","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4771"}}]},"synonyms":[{"value":"H3FF"},{"value":"HIST1H3I"}]},{"name":{"value":"H3C12","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:4774","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:4774"}}]},"synonyms":[{"value":"H3FJ"},{"value":"HIST1H3J"}]}],"length":136,"name":"Histone H3.1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":38,"reference_id":"22493481","reference_source":"pmid","reference_html":"Characterization of chromoshadow domain-mediated binding of heterochromatin protein 1α (HP1α) to histone H3. <i> Richart AN, Brunner CI, Stott K, Murzina NV, Thomas JO. </i> J Biol Chem, 2012","date":"2024-11-14T17:21:58.608Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04281r001","statement":[{"text":"Elevated {1H}15N heteronuclear NOE values measured for free H3(1–59) indicated that residues 39–55 are partially structured in the free peptide (Fig. 4C).","type":"Results"}]},{"start":1,"end":38,"reference_id":"22493481","reference_source":"pmid","reference_html":"Characterization of chromoshadow domain-mediated binding of heterochromatin protein 1α (HP1α) to histone H3. <i> Richart AN, Brunner CI, Stott K, Murzina NV, Thomas JO. </i> J Biol Chem, 2012","date":"2024-11-14T17:22:32.531Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04281r002","statement":[{"text":"Elevated {1H}15N heteronuclear NOE values measured for free H3(1–59) indicated that residues 39–55 are partially structured in the free peptide (Fig. 4C).","type":"Results"}]}],"regions_counter":2,"released":"2025_06","sequence":"MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.007352941176470588,"dataset":["Cancer-related proteins","Condensates-related proteins"],"disorder_content":0.27941176470588236,"disprot_consensus":{"full":[{"start":1,"end":38,"type":"D"}],"Structural state":[{"start":1,"end":38,"type":"D"}],"Disorder function":[{"start":1,"end":38,"type":"F"}]}},{"disprot_id":"DP04283","acc":"P69229","creator":"zskalman","date":"2024-11-15T11:23:31.766Z","features":{"pfam":[{"id":"PF00072","name":"Response regulator receiver domain","start":13,"end":122},{"id":"PF00486","name":"Transcriptional regulatory protein, C terminal","start":156,"end":231}],"gene3D":[]},"genes":[{"name":{"value":"baeR"},"olnNames":[{"value":"c2605"}]}],"length":240,"name":"Transcriptional regulatory protein BaeR","ncbi_taxon_id":199310,"organism":"Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)","regions":[{"start":127,"end":141,"reference_id":"23868292","reference_source":"pmid","reference_html":"The dimeric form of the unphosphorylated response regulator BaeR. <i> Choudhury HG, Beis K. </i> Protein Sci, 2013","date":"2024-11-18T10:29:37.992Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"4B09"}],"region_id":"DP04283r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"131704268  "}],"statement":[{"text":"The two domains are connected together by a linker of 15 residues in length; in our electron density maps we can observe some density for the linker but the resolution is not sufficient to be built (Supporting Information Fig. S2).","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr71Met","start":null,"end":null,"position":null},{"term_id":"MOD:00429","term_name":"dimethylated residue","term_namespace":"Protein modification","start":73,"end":73,"position":"Specific residue"},{"term_id":"MOD:00429","term_name":"dimethylated residue","term_namespace":"Protein modification","start":106,"end":106,"position":"Specific residue"}],"sequence_construct":"MTELPIDENTPRILIVEDEPKLGQLLIDYLRAASYAPTLISHGDQVLPYVRQTPPDLILLDLMLPGTDGLMLCREIRRFSDIPIVMVTAKIEEIDRLLGLEIGADDYICKPYSPREVVARVKTILRRCKPQRELQQQDAESPLIIDEGRFQASWRGKMLDLTPAEFRLLKTLSHEPGKVFSREQLLNHLYDDYRVVTDRTIDSHIKNLRRKLESLDAEQSFIRAVYGVGYRWEADACRIV","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-04T15:36:21.698Z"}}],"regions_counter":2,"released":"2025_06","sequence":"MTELPIDENTPRILIVEDEPKLGQLLIDYLRAASYAPTLISHGDQVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRFSDIPIVMVTAKIEEIDRLLGLEIGADDYICKPYSPREVVARVKTILRRCKPQRELQQQDAESPLIIDEGRFQASWRGKMLDLTPAEFRLLKTLSHEPGKVFSREQLLNHLYDDYRVVTDRTIDSHIKNLRRKLESLDAEQSFIRAVYGVGYRWEADACRIV","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"alphafold_very_low_content":0.06666666666666667,"disorder_content":0.0625,"disprot_consensus":{"full":[{"start":127,"end":141,"type":"D"}],"Structural state":[{"start":127,"end":141,"type":"D"}]}},{"disprot_id":"DP04284","acc":"Q8TDX7","creator":"zskalman","date":"2024-11-15T13:47:52.696Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":34,"end":286}],"gene3D":[]},"genes":[{"name":{"value":"NEK7","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11701951","url":"http://www.ncbi.nlm.nih.gov/pubmed/11701951","alternativeUrl":"https://europepmc.org/abstract/MED/11701951"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:13386","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:13386"}}]}}],"length":302,"name":"Serine/threonine-protein kinase Nek7","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":182,"end":195,"reference_id":"26522158","reference_source":"pmid","reference_html":"Mechanistic basis of Nek7 activation through Nek9 binding and induced dimerization. <i> Haq T, Richards MW, Burgess SG, Gallego P, Yeoh S, O'Regan L, Reverter D, Roig J, Fry AM, Bayliss R. </i> Nat Commun, 2015","date":"2024-11-15T13:57:54.924Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"5DE2"}],"region_id":"DP04284r001","statement":[{"text":"Residues 20–300 of Nek7Y97F were modelled with the exception of the activation loop residues 182–195 (chain A) and 181–199 (chain B), which were disordered.","type":"Results"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"sequence_construct":"MDEQSQGMQGPPVPQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRAACLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKFYASFIEDNELNIVLELADAGDLSRMIKHFKKQKRLIPERTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLCKKIEQCDYPPLPSDHYSEELRQLVNMCINPDPEKRPDVTYVYDVAKRMHACTASSLEHHHHHH","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8K1R7"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-04T16:32:42.652Z"}},{"start":190,"end":195,"reference_id":"12840024","reference_source":"pmid","reference_html":"A mitotic cascade of NIMA family kinases. Nercc1/Nek9 activates the Nek6 and Nek7 kinases. <i> Belham C, Roig J, Caldwell JA, Aoyama Y, Kemp BE, Comb M, Avruch J. </i> J Biol Chem, 2003","date":"2025-06-25T06:46:46.587Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001202","ec_ontology":"ECO","ec_name":"in vitro protein kinase assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04284r002","statement":[{"text":"Activated Nercc1 directly catalyzes the phosphorylation of Nek6 Ser206 (and of the equivalent site, Ser195, in Nek7) and generates a robust activation of wild type Nek6/7 in vitro. 3) ","type":"Results"}],"construct_alterations":[{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-30T16:25:04.781Z"}},{"start":182,"end":195,"reference_id":"26522158","reference_source":"pmid","reference_html":"Mechanistic basis of Nek7 activation through Nek9 binding and induced dimerization. <i> Haq T, Richards MW, Burgess SG, Gallego P, Yeoh S, O'Regan L, Reverter D, Roig J, Fry AM, Bayliss R. </i> Nat Commun, 2015","date":"2025-06-25T06:37:16.606Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"5DE2"}],"region_id":"DP04284r003","statement":[{"text":"Residues 20–300 of Nek7Y97F were modelled with the exception of the activation loop residues 182–195 (chain A) and 181–199 (chain B), which were disordered.","type":"Results"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"sequence_construct":"MDEQSQGMQGPPVPQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRAACLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKFYASFIEDNELNIVLELADAGDLSRMIKHFKKQKRLIPERTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLCKKIEQCDYPPLPSDHYSEELRQLVNMCINPDPEKRPDVTYVYDVAKRMHACTASSLEHHHHHH","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q8K1R7"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-30T16:24:47.152Z"}},{"start":1,"end":19,"reference_id":"26522158","reference_source":"pmid","reference_html":"Mechanistic basis of Nek7 activation through Nek9 binding and induced dimerization. <i> Haq T, Richards MW, Burgess SG, Gallego P, Yeoh S, O'Regan L, Reverter D, Roig J, Fry AM, Bayliss R. </i> Nat Commun, 2015","date":"2025-06-25T06:43:10.211Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"2WQM"}],"region_id":"DP04284r004","statement":[{"text":"Missing electron density for this region.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"934"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1117"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-30T16:23:35.407Z"}},{"start":1,"end":19,"reference_id":"26522158","reference_source":"pmid","reference_html":"Mechanistic basis of Nek7 activation through Nek9 binding and induced dimerization. <i> Haq T, Richards MW, Burgess SG, Gallego P, Yeoh S, O'Regan L, Reverter D, Roig J, Fry AM, Bayliss R. </i> Nat Commun, 2015","date":"2025-06-25T06:42:40.341Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"2WQM"}],"region_id":"DP04284r005","statement":[{"text":"Missing electron density for this region.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1117"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"934"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-30T16:23:36.999Z"}},{"start":190,"end":195,"reference_id":"12840024","reference_source":"pmid","reference_html":"A mitotic cascade of NIMA family kinases. Nercc1/Nek9 activates the Nek6 and Nek7 kinases. <i> Belham C, Roig J, Caldwell JA, Aoyama Y, Kemp BE, Comb M, Avruch J. </i> J Biol Chem, 2003","date":"2025-06-25T06:49:05.188Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"GO:0043549","term_name":"regulation of kinase activity","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001254","ec_ontology":"ECO","ec_name":"radioisotope assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","region_id":"DP04284r006","statement":[{"text":"As shown in Fig. 4C, Nercc1 catalyzes the phosphorylation of Nek6 (Ser206) and the equivalent site on Nek7 (Ser195), resulting in a 20–25-fold activation of Nek6/7 kinase activity.","type":"Results"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of kinase activity, the catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.\" [GOC:bf]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-30T16:24:50.656Z"}}],"regions_counter":6,"released":"2025_06","sequence":"MDEQSQGMQGPPVPQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRAACLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMIKHFKKQKRLIPERTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLCKKIEQCDYPPLPSDHYSEELRQLVNMCINPDPEKRPDVTYVYDVAKRMHACTASS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.07947019867549669,"disorder_content":0.10927152317880795,"disprot_consensus":{"full":[{"start":1,"end":19,"type":"D"},{"start":182,"end":195,"type":"D"}],"Structural state":[{"start":1,"end":19,"type":"D"},{"start":182,"end":195,"type":"D"}],"Disorder function":[{"start":1,"end":19,"type":"F"},{"start":182,"end":195,"type":"F"}],"Biological process":[{"start":190,"end":195,"type":"F"}]}},{"disprot_id":"DP04285","acc":"Q9UK59","creator":"vnugnes","date":"2024-11-15T15:17:23.969Z","features":{"pfam":[{"id":"PF00149","name":"Calcineurin-like phosphoesterase","start":1,"end":229},{"id":"PF05011","name":"Lariat debranching enzyme, C-terminal domain","start":247,"end":377}],"gene3D":[]},"genes":[{"name":{"value":"DBR1"}}],"length":544,"name":"Lariat debranching enzyme","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":394,"end":544,"reference_id":"37507019","reference_source":"pmid","reference_html":"Activation of human RNA lariat debranching enzyme Dbr1 by binding protein TTDN1 occurs though an intrinsically disordered C-terminal domain. <i> Clark NE, Katolik A, Gallant P, Welch A, Murphy E, Buerer L, Schorl C, Naik N, Naik MT, Holloway SP, Cano K, Weintraub ST, Howard KM, Hart PJ, Jogl G, Damha MJ, Fairbrother WG. </i> J Biol Chem, 2023","date":"2024-11-15T15:24:08.067Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04285r001","statement":[{"text":"The order/disorder predictor PONDR uses the relative frequency of charged and hydrophobic residues to forecast the presence of disordered regions (29), and PONDR clearly predicted that the C-terminal ∼150 aa of Dbr1 are unstructured (Fig. 1B). Consistent with this PONDR prediction, unstructured polypeptide is present in the C-terminal domain of an hDbr1 Alpha-Fold model (Fig. 1C) (30, 31).","type":"Results"},{"text":"The amide and aliphatic proton regions were indistinguishable for the two samples. We concluded that hDbr1 had the same folded state when expressed in prokaryotic or eukaryotic cells and that the presence of the random coil was not an artifact of heterologous expression in prokaryotic cells. A circular dichroism spectra of E. coli expressed hDbr1 is presented in Fig. S1B.","type":"Results"}]},{"start":503,"end":544,"reference_id":"37507019","reference_source":"pmid","reference_html":"Activation of human RNA lariat debranching enzyme Dbr1 by binding protein TTDN1 occurs though an intrinsically disordered C-terminal domain. <i> Clark NE, Katolik A, Gallant P, Welch A, Murphy E, Buerer L, Schorl C, Naik N, Naik MT, Holloway SP, Cano K, Weintraub ST, Howard KM, Hart PJ, Jogl G, Damha MJ, Fairbrother WG. </i> J Biol Chem, 2023","date":"2024-11-15T15:27:46.151Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0050821","term_name":"protein stabilization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP04285r002","statement":[{"text":"Full-length Dbr1 was monodisperse, with a narrow distribution of S-values centered around 4.3 (Fig. 2A). Dbr1-502 and Dbr1-399 showed considerable aggregation, with ∼20% of the samples sedimenting at very large S-values.","type":"Results"},{"text":"The disordered C terminus stabilizes Dbr1 but is not required for activity","type":"Results"}],"term_comment":"","term_def":"\"Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":394,"end":544,"reference_id":"37507019","reference_source":"pmid","reference_html":"Activation of human RNA lariat debranching enzyme Dbr1 by binding protein TTDN1 occurs though an intrinsically disordered C-terminal domain. <i> Clark NE, Katolik A, Gallant P, Welch A, Murphy E, Buerer L, Schorl C, Naik N, Naik MT, Holloway SP, Cano K, Weintraub ST, Howard KM, Hart PJ, Jogl G, Damha MJ, Fairbrother WG. </i> J Biol Chem, 2023","date":"2024-11-15T15:29:20.519Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04285r003","statement":[{"text":"The order/disorder predictor PONDR uses the relative frequency of charged and hydrophobic residues to forecast the presence of disordered regions (29), and PONDR clearly predicted that the C-terminal ∼150 aa of Dbr1 are unstructured (Fig. 1B). Consistent with this PONDR prediction, unstructured polypeptide is present in the C-terminal domain of an hDbr1 Alpha-Fold model (Fig. 1C) (30, 31).","type":"Results"},{"text":"The amide and aliphatic proton regions were indistinguishable for the two samples. We concluded that hDbr1 had the same folded state when expressed in prokaryotic or eukaryotic cells and that the presence of the random coil was not an artifact of heterologous expression in prokaryotic cells. A circular dichroism spectra of E. coli expressed hDbr1 is presented in Fig. S1B.","type":"Results"}]}],"regions_counter":3,"released":"2025_06","sequence":"MRVAVAGCCHGELDKIYETLALAERRGPGPVDLLLCCGDFQAVRNEADLRCMAVPPKYRHMQTFYRYYSGEKKAPVLTLFIGGNHEASNHLQELPYGGWVAPNIYYLGLAGVVKYRGVRIGGISGIFKSHDYRKGHFECPPYNSSTIRSIYHVRNIEVYKLKQLKQPIDIFLSHDWPRSIYHYGNKKQLLKTKSFFRQEVENNTLGSPAASELLEHLKPTYWFSAHLHVKFAALMQHQAKDKGQTARATKFLALDKCLPHRDFLQILEIEHDPSAPDYLEYDIEWLTILRATDDLINVTGRLWNMPENNGLHARWDYSATEEGMKEVLEKLNHDLKVPCNFSVTAACYDPSKPQTQMQLIHRINPQTTEFCAQLGIIDINVRLQKSKEEHHVCGEYEEQDDVESNDSGEDQSEYNTDTSALSSINPDEIMLDEEEDEDSIVSAHSGMNTPSVEPSDQASEFSASFSDVRILPGSMIVSSDDTVDSTIDREGKPGGTVESGNGEDLTKVPLKRLSDEHEPEQRKKIKRRNQAIYAAVDDDDDDAA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.2665441176470588,"disorder_content":0.2775735294117647,"disprot_consensus":{"full":[{"start":394,"end":544,"type":"D"}],"Structural state":[{"start":394,"end":544,"type":"D"}],"Biological process":[{"start":503,"end":544,"type":"F"}],"Disorder function":[{"start":394,"end":544,"type":"F"}]}},{"disprot_id":"DP04286","acc":"Q8TAP9","creator":"vnugnes","date":"2024-11-15T17:00:03.965Z","features":{"pfam":[{"id":"PF15502","name":"M-phase-specific PLK1-interacting protein","start":98,"end":178}],"gene3D":[]},"genes":[{"name":{"value":"MPLKIP"},"synonyms":[{"value":"C7orf11"},{"value":"TTDN1"}]}],"length":179,"name":"M-phase-specific PLK1-interacting protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":135,"reference_id":"37507019","reference_source":"pmid","reference_html":"Activation of human RNA lariat debranching enzyme Dbr1 by binding protein TTDN1 occurs though an intrinsically disordered C-terminal domain. <i> Clark NE, Katolik A, Gallant P, Welch A, Murphy E, Buerer L, Schorl C, Naik N, Naik MT, Holloway SP, Cano K, Weintraub ST, Howard KM, Hart PJ, Jogl G, Damha MJ, Fairbrother WG. </i> J Biol Chem, 2023","date":"2024-11-15T17:05:37.030Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04286r001","statement":[{"text":"We observed a drop in the amide region (8.2 ppm) at acidic pH (pH 4.5 versus 7.4), suggesting a collapse of structure at low pH. Circular dichroism of TTDN1 (pH 7.4) verified this helical content, with a minima around 220 nm (Fig. S1B). A predicted structure of TTDN1 also has short helical regions (Fig. S1C) (30, 31).","type":"Results"},{"text":"AlphaFold prediction shows the region 136-159 is the one \nthat is contributing to the structured component seen in the experimental approaches.","type":"Curator statement"}]},{"start":160,"end":179,"reference_id":"37507019","reference_source":"pmid","reference_html":"Activation of human RNA lariat debranching enzyme Dbr1 by binding protein TTDN1 occurs though an intrinsically disordered C-terminal domain. <i> Clark NE, Katolik A, Gallant P, Welch A, Murphy E, Buerer L, Schorl C, Naik N, Naik MT, Holloway SP, Cano K, Weintraub ST, Howard KM, Hart PJ, Jogl G, Damha MJ, Fairbrother WG. </i> J Biol Chem, 2023","date":"2024-11-15T17:08:45.293Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04286r002","statement":[{"text":"We observed a drop in the amide region (8.2 ppm) at acidic pH (pH 4.5 versus 7.4), suggesting a collapse of structure at low pH. Circular dichroism of TTDN1 (pH 7.4) verified this helical content, with a minima around 220 nm (Fig. S1B). A predicted structure of TTDN1 also has short helical regions (Fig. S1C) (30, 31).","type":"Results"},{"text":"AlphaFold prediction shows the region 136-159 is the one \nthat is contributing to the structured component seen in the experimental approaches.","type":"Curator statement"}]}],"regions_counter":2,"released":"2025_06","sequence":"MQRQNFRPPTPPYPGPGGGGWGSGSSFRGTPGGGGPRPPSPRDGYGSPHHTPPYGPRSRPYGSSHSPRHGGSFPGGRFGSPSPGGYPGSYSRSPAGSQQQFGYSPGQQQTHPQGSPRTSTPFGSGRVREKRMSNELENYFKPSMLEDPWAGLEPVSVVDISQQYSNTQTFTGKKGRYFC","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.46368715083798884,"dataset":["NDDs-related proteins"],"disorder_content":0.8659217877094972,"disprot_consensus":{"full":[{"start":1,"end":135,"type":"D"},{"start":160,"end":179,"type":"D"}],"Structural state":[{"start":1,"end":135,"type":"D"},{"start":160,"end":179,"type":"D"}]}},{"disprot_id":"DP04287","acc":"O14907","creator":"zskalman","date":"2024-11-17T16:13:28.181Z","features":{"pfam":[{"id":"PF00595","name":"PDZ domain","start":22,"end":109}],"gene3D":[]},"genes":[{"name":{"value":"TAX1BP3","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:30684","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:30684"}}]},"synonyms":[{"value":"TIP1","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAF43104.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAF43104.1"}}]}]}],"length":124,"name":"Tax1-binding protein 3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":10,"reference_id":"21417405","reference_source":"pmid","reference_html":"Promiscuous binding at the crossroads of numerous cancer pathways: insight from the binding of glutaminase interacting protein with glutaminase L. <i> Zoetewey DL, Ovee M, Banerjee M, Bhaskaran R, Mohanty S. </i> Biochemistry, 2011","date":"2024-11-17T16:15:23.232Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"17254"},{"db":"PDB","id":"2L4S"}],"region_id":"DP04287r001","statement":[{"text":"Residues M1−T10 and A113−S124 are not shown because they are highly disordered and have chemical shifts perturbations of <0.05 ppm. ","type":"Figure"}],"sequence_construct":"MSYIPGQPVTAVVQRVEIHKLRQGENLILGFSIGGGIDQDPSQNPFSEDKTDKGIYVTRVSEGGPAEIAGLQIGDKIMQVNGWDMTMVTHDQARKRLTKRSEEVVRLLVTRQSLQKAVQQSMLS","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-05T13:34:39.921Z"}},{"start":113,"end":124,"reference_id":"21417405","reference_source":"pmid","reference_html":"Promiscuous binding at the crossroads of numerous cancer pathways: insight from the binding of glutaminase interacting protein with glutaminase L. <i> Zoetewey DL, Ovee M, Banerjee M, Bhaskaran R, Mohanty S. </i> Biochemistry, 2011","date":"2024-11-17T16:15:12.938Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"17254"},{"db":"PDB","id":"2L4S"}],"region_id":"DP04287r002","statement":[{"text":"Residues M1−T10 and A113−S124 are not shown because they are highly disordered and have chemical shifts perturbations of <0.05 ppm. ","type":"Figure"}],"sequence_construct":"MSYIPGQPVTAVVQRVEIHKLRQGENLILGFSIGGGIDQDPSQNPFSEDKTDKGIYVTRVSEGGPAEIAGLQIGDKIMQVNGWDMTMVTHDQARKRLTKRSEEVVRLLVTRQSLQKAVQQSMLS","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-05T13:34:39.625Z"}}],"regions_counter":4,"released":"2025_06","sequence":"MSYIPGQPVTAVVQRVEIHKLRQGENLILGFSIGGGIDQDPSQNPFSEDKTDKGIYVTRVSEGGPAEIAGLQIGDKIMQVNGWDMTMVTHDQARKRLTKRSEEVVRLLVTRQSLQKAVQQSMLS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.04032258064516129,"disorder_content":0.1774193548387097,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"},{"start":113,"end":124,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":113,"end":124,"type":"D"}]}},{"disprot_id":"DP04288","acc":"P29066","creator":"zskalman","date":"2024-11-17T16:39:40.614Z","features":{"pfam":[{"id":"PF00339","name":"Arrestin (or S-antigen), N-terminal domain","start":19,"end":173},{"id":"PF02752","name":"Arrestin (or S-antigen), C-terminal domain","start":193,"end":355}],"gene3D":[]},"genes":[{"name":{"value":"Arrb1"}}],"length":418,"name":"Beta-arrestin-1","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions":[{"start":360,"end":382,"reference_id":"37399373","reference_source":"pmid","reference_html":"GPCR targeting of E3 ubiquitin ligase MDM2 by inactive β-arrestin. <i> Yun Y, Yoon HJ, Jeong Y, Choi Y, Jang S, Chung KY, Lee HH. </i> Proc Natl Acad Sci U S A, 2023","date":"2024-11-17T16:49:55.256Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"8HSV"}],"region_id":"DP04288r001","statement":[{"text":"No electron density was observed for residues 334–338 and 360–382 in chain A and chain B, respectively.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1117  "},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A8I6G5V3"}],"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys59Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys125Ser","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys140Leu","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys150Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys242Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys251Val","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys269Ser","start":null,"end":null,"position":null}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSHMGDKGTRVFKKASPNGKLTVYLGKRDFVDHIDLVDPVDGVVLVDPEYLKERRVYVTLTVAFRYGREDLDVLGLTFRKDLFVANVQSFPPAPEDKKPLTRLQERLIKKLGEHAYPFTFEIPPNLPSSVTLQPGPEDTGKALGVDYEVKAFVAENLEEKIHKRNSVRLVIRKVQYAPERPGPQPTAETTRQFLMSDKPLHLEASLDKEIYYHGEPISVNVHVTNNTNKTVKKIKISVRQYADIVLFNTAQYKVPVAMEEADDTVAPSSTFSKVYTLTPFLANNREKRGLALDGKLKHEDTNLASSTLLREGANREILGIIVSYKVKVKLVVSRGGLLGDLASSDVAVELPFTLMHPKPKEEPPHREVPESETPVDTNLIELDTNDDDIVFEDFARQ","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-05T13:38:12.979Z"}}],"regions_counter":1,"released":"2025_06","sequence":"MGDKGTRVFKKASPNGKLTVYLGKRDFVDHIDLVDPVDGVVLVDPEYLKERRVYVTLTCAFRYGREDLDVLGLTFRKDLFVANVQSFPPAPEDKKPLTRLQERLIKKLGEHAYPFTFEIPPNLPCSVTLQPGPEDTGKACGVDYEVKAFCAENLEEKIHKRNSVRLVIRKVQYAPERPGPQPTAETTRQFLMSDKPLHLEASLDKEIYYHGEPISVNVHVTNNTNKTVKKIKISVRQYADICLFNTAQYKCPVAMEEADDTVAPSSTFCKVYTLTPFLANNREKRGLALDGKLKHEDTNLASSTLLREGANREILGIIVSYKVKVKLVVSRGGLLGDLASSDVAVELPFTLMHPKPKEEPPHREVPESETPVDTNLIELDTNDDDIVFEDFARQRLKGMKDDKDEEDDGTGSPHLNNR","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"alphafold_very_low_content":0.11961722488038277,"disorder_content":0.05502392344497608,"disprot_consensus":{"full":[{"start":360,"end":382,"type":"D"}],"Structural state":[{"start":360,"end":382,"type":"D"}]}},{"disprot_id":"DP04290","acc":"Q9V6Q2","creator":"zskalman","date":"2024-11-18T09:09:36.953Z","features":{"pfam":[{"id":"PF00125","name":"Core histone H2A/H2B/H3/H4 domain","start":131,"end":218}],"gene3D":[]},"genes":[{"name":{"value":"cid","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0040477","url":"http://flybase.org/reports/FBgn0040477.html"}}]},"synonyms":[{"value":"CENP-A","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"24703848","url":"http://www.ncbi.nlm.nih.gov/pubmed/24703848","alternativeUrl":"https://europepmc.org/abstract/MED/24703848"}},{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0040477","url":"http://flybase.org/reports/FBgn0040477.html"}}]}],"orfNames":[{"value":"CG13329","evidences":[{"code":"ECO:0000312","source":{"name":"FlyBase","id":"FBgn0040477","url":"http://flybase.org/reports/FBgn0040477.html"}}]}]}],"length":225,"name":"Histone H3-like centromeric protein cid","ncbi_taxon_id":7227,"organism":"Drosophila melanogaster","regions":[{"start":101,"end":146,"reference_id":"32134144","reference_source":"pmid","reference_html":"Structural basis for centromere maintenance by Drosophila CENP-A chaperone CAL1. <i> Medina-Pritchard B, Lazou V, Zou J, Byron O, Abad MA, Rappsilber J, Heun P, Jeyaprakash AA. </i> EMBO J, 2020","date":"2025-04-02T08:23:07.526Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"6XWT"}],"region_id":"DP04290r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84040"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9VEN2"}],"sequence_construct":"MPRHSRAKRAPRPSANNSKSPNDDDTAFRSPEPEDGTDYGLEFTTSQLTLQDNNRRSSTLRRDAGRRQPAARDSSTSGEEEDQENRYPTTRSPQTRRMTVQQESKTRAAGPVAAQNQTRRRKAANPMSRAKRMDREIRRLQHHPGTLIPKLPFSRLVREFIVKYSDDEPLRVTEGALLAMQESCEMYLTQRLADSYMLTKHRNRVTLEVRDMALMAYICDRGRQF","statement":[{"text":"No observed electron density for this region.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-04-02T18:45:29.097Z"}},{"start":1,"end":131,"reference_id":"https://mobidb.org/P35187","reference_source":"mobidb","reference_html":"An Entry Referenced from MobiDB","date":"2025-02-05T14:31:20.941Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008033","ec_ontology":"ECO","ec_name":"intrinsic disorder prediction evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04290r003","statement":[{"text":"This region is classified as intrinsically disordered, based on the disorder consensus prediction from the corresponding MobiDB entry.","type":"Curator statement"}]}],"regions_counter":3,"released":"2025_06","sequence":"MPRHSRAKRAPRPSANNSKSPNDDDTAFRSPEPEDGTDYGLEFTTSQLTLQDNNRRSSTLRRDAGRRQPAARDSSTSGEEEDQENRYPTTRSPQTRRMTVQQESKTRAAGPVAAQNQTRRRKAANPMSRAKRMDREIRRLQHHPGTLIPKLPFSRLVREFIVKYSDDEPLRVTEGALLAMQESCEMYLTQRLADSYMLTKHRNRVTLEVRDMALMAYICDRGRQF","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"alphafold_very_low_content":0.31555555555555553,"disorder_content":0.6488888888888888,"disprot_consensus":{"full":[{"start":1,"end":146,"type":"D"}],"Structural state":[{"start":1,"end":146,"type":"D"}]}},{"disprot_id":"DP04294","acc":"I1KDC1","creator":"vnugnes","date":"2024-11-19T14:10:25.790Z","features":{"pfam":[{"id":"PF01429","name":"Methyl-CpG binding domain","start":17,"end":84}],"gene3D":[]},"genes":[{"name":{"value":"100796239","evidences":[{"code":"ECO:0000313","source":{"name":"EnsemblPlants","id":"KRH54899","url":"http://www.ensemblgenomes.org/id/KRH54899"}}]},"orfNames":[{"value":"GLYMA_06G217500","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"KRH54899.1","url":"https://www.ebi.ac.uk/ena/browser/view/KRH54899.1"}}]}]}],"length":305,"name":"MBD domain-containing protein","ncbi_taxon_id":3847,"organism":"Glycine max","regions":[{"start":80,"end":305,"reference_id":"37240035","reference_source":"pmid","reference_html":"The Moonlighting Function of Soybean Disordered Methyl-CpG-Binding Domain 10c Protein. <i> Li Y, Qin J, Chen M, Sun N, Tan F, Zhang H, Zou Y, Uversky VN, Liu Y. </i> Int J Mol Sci, 2023","date":"2024-11-19T14:32:23.402Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04294r001","statement":[{"text":"The far-UV CD spectra of GmMBD10c in water showed a deep minimum near 198 nm, which is indicative of a mostly disordered structure.","type":"Results"},{"text":"In water, GmMBD10c is largely disordered, with several disordered regions predicted in the region comprising aa 80–305.","type":"Discussion"},{"text":"The combination of experimental evidence and a variety of disorder predictors used by the authors allow us to determine 80-350 as the IDR's boundaries. ","type":"Curator statement"}]},{"start":80,"end":305,"reference_id":"37240035","reference_source":"pmid","reference_html":"The Moonlighting Function of Soybean Disordered Methyl-CpG-Binding Domain 10c Protein. <i> Li Y, Qin J, Chen M, Sun N, Tan F, Zhang H, Zou Y, Uversky VN, Liu Y. </i> Int J Mol Sci, 2023","date":"2024-11-19T14:33:02.777Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04294r002","statement":[{"text":"To confirm the disordered structure of GmMBD10c, a 1H NMR spectrum was obtained and analyzed. The peaks in the amide region of the spectrum (from 6.6 to 7.8 ppm) are not well dispersed, similar to that of soybean LOC protein, another partially unstructured protein [29].Therefore, we conclude that GmMBD10c is partially disordered in aqueous medium (Figure 4).","type":"Results"},{"text":"In water, GmMBD10c is largely disordered, with several disordered regions predicted in the region comprising aa 80–305.","type":"Discussion"},{"text":"The combination of experimental evidence and a variety of disorder predictors used by the authors allow us to determine 80-350 as the IDR's boundaries. ","type":"Curator statement"}]}],"regions_counter":2,"released":"2025_06","sequence":"MASAVEKEGGASEETLSLELPAPPGWKKQFIPKKAGTPKKNEIVFTAPTGEEINNRKQLEKYLKAHPGGPAVSEFDWGTGETPRRSTRISEKAKAAPPTQREPPKKRTKRSSASQKEISQEEKEEETKEAEMQEADDTTKGDNDIEKEKVVVNENHDKSVEDTDVNKSTRYGEEAKAGENVEVPIEEEKSNAADGELPALKDKADDKVTEGSEVFLRKDEEKIEQPQEETKEYSGFGEPEKLETCTTADKTVEVEGVNKEDHVKSTHEFEVGEIEGTKVNGEEHHKLDEINKAEAELTVNGTHES","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","fabids","Fabales","Fabaceae","Papilionoideae","50 kb inversion clade","NPAAA clade","indigoferoid/millettioid clade","Phaseoleae","Glycine","Glycine subgen. Soja"],"alphafold_very_low_content":0.38688524590163936,"disorder_content":0.740983606557377,"disprot_consensus":{"full":[{"start":80,"end":305,"type":"D"}],"Structural state":[{"start":80,"end":305,"type":"D"}]}},{"disprot_id":"DP04295","acc":"Q9Y572","creator":"vnugnes","date":"2024-11-19T15:27:09.345Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":22,"end":280},{"id":"PF12721","name":"RIP homotypic interaction motif","start":448,"end":468}],"gene3D":[]},"genes":[{"name":{"value":"RIPK3","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:10021","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:10021"}}]},"synonyms":[{"value":"RIP3","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"10339433","url":"http://www.ncbi.nlm.nih.gov/pubmed/10339433","alternativeUrl":"https://europepmc.org/abstract/MED/10339433"}}]}]}],"length":518,"name":"Receptor-interacting serine/threonine-protein kinase 3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":387,"end":518,"reference_id":"36870681","reference_source":"pmid","reference_html":"NMR characterization of an assembling RHIM (RIP homotypic interaction motif) amyloid reveals a cryptic region for self-recognition. <i> Pham CLL, Titaux-Delgado GA, Varghese NR, Polonio P, Wilde KL, Sunde M, Mompeán M. </i> J Biol Chem, 2023","date":"2024-11-19T15:29:01.094Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0379","term_name":"13C label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified"},{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified"}],"region_id":"DP04295r001","statement":[{"text":"The 1H-15N heteronuclear single quantum coherence (HSQC) spectra recorded on these protein samples, whose final concentrations are in the range 18 to 20 μM, revealed the typical pattern of disordered proteins.","type":"Results"}],"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":4},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":6.5}]},{"start":387,"end":518,"reference_id":"36870681","reference_source":"pmid","reference_html":"NMR characterization of an assembling RHIM (RIP homotypic interaction motif) amyloid reveals a cryptic region for self-recognition. <i> Pham CLL, Titaux-Delgado GA, Varghese NR, Polonio P, Wilde KL, Sunde M, Mompeán M. </i> J Biol Chem, 2023","date":"2024-11-19T15:48:41.321Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006333","ec_ontology":"ECO","ec_name":"thioflavin T based fluorescence spectroscopy evidence","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04295r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"76023","entry_name":"thioflavine T"}],"statement":[{"text":"According to thioflavin T (ThT) assays, the broadening and loss of intensity observed upon raising the pH is consistent with the assembly of amyloid fibrils when the pH is raised to 6.5 from pH 4.0 (Fig. 2B).","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":6.5}]},{"start":430,"end":465,"reference_id":"36870681","reference_source":"pmid","reference_html":"NMR characterization of an assembling RHIM (RIP homotypic interaction motif) amyloid reveals a cryptic region for self-recognition. <i> Pham CLL, Titaux-Delgado GA, Varghese NR, Polonio P, Wilde KL, Sunde M, Mompeán M. </i> J Biol Chem, 2023","date":"2024-11-19T16:07:26.006Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042802","term_name":"identical protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9Y572","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04295r003","statement":[{"text":"In order to establish whether monomers use this region preceding the RHIM to directly interact with the fibril surface in the amyloid-bound state, we prepared a 15N-labeled RIPK3 (387–518) sample to obtain the difference in transverse relaxation rates, ΔR2, under assembling (at 180 μM) and nonassembling (at 18 μM) conditions (Figs. 3F and S5).","type":"Results"},{"text":"Under these conditions, the resulting ΔR2 (i.e., R2 at 180 μM minus R2 at 18 μM) identifies which residues in the monomer establish specific contacts with the fibril during the dynamic equilibrium between unbound and amyloid-bound monomers (Fig. 3F).","type":"Results"},{"text":"More intriguing, our data reveal that in addition to the RHIM, its preceding ca. 20-residue stretch readily established contacts with the fibril surface in the assembled state.","type":"Abstract"}],"term_comment":"","term_def":"\"Binding to an identical protein or proteins.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":388,"end":447,"reference_id":"33790016","reference_source":"pmid","reference_html":"The structure of a minimum amyloid fibril core formed by necroptosis-mediating RHIM of human RIPK3. <i> Wu X, Ma Y, Zhao K, Zhang J, Sun Y, Li Y, Dong X, Hu H, Liu J, Wang J, Zhang X, Li B, Wang H, Li D, Sun B, Lu J, Liu C. </i> Proc Natl Acad Sci U S A, 2021","date":"2024-11-19T17:41:29.978Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"EMDB","id":"30622"},{"db":"PDB","id":"7DA4"}],"region_id":"DP04295r004","statement":[{"text":"The ssNMR and cryo-EM structures show that the core of the RIPK3-CTD fibril is very small, consisting of only ∼20 residues out of a total of over 100 residues of RIPK3-CTD (Fig. 3A). The rest of the residues in the CTD remain flexible and are invisible by either cryo-EM or ssNMR.","type":"Results"}]},{"start":470,"end":518,"reference_id":"33790016","reference_source":"pmid","reference_html":"The structure of a minimum amyloid fibril core formed by necroptosis-mediating RHIM of human RIPK3. <i> Wu X, Ma Y, Zhao K, Zhang J, Sun Y, Li Y, Dong X, Hu H, Liu J, Wang J, Zhang X, Li B, Wang H, Li D, Sun B, Lu J, Liu C. </i> Proc Natl Acad Sci U S A, 2021","date":"2024-11-19T17:42:04.367Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"EMDB","id":"30622"},{"db":"PDB","id":"7DA4"}],"region_id":"DP04295r005","statement":[{"text":"The ssNMR and cryo-EM structures show that the core of the RIPK3-CTD fibril is very small, consisting of only ∼20 residues out of a total of over 100 residues of RIPK3-CTD (Fig. 3A). The rest of the residues in the CTD remain flexible and are invisible by either cryo-EM or ssNMR.","type":"Results"}]},{"start":476,"end":518,"reference_id":"33790016","reference_source":"pmid","reference_html":"The structure of a minimum amyloid fibril core formed by necroptosis-mediating RHIM of human RIPK3. <i> Wu X, Ma Y, Zhao K, Zhang J, Sun Y, Li Y, Dong X, Hu H, Liu J, Wang J, Zhang X, Li B, Wang H, Li D, Sun B, Lu J, Liu C. </i> Proc Natl Acad Sci U S A, 2021","date":"2024-11-19T17:43:15.720Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7DAC"}],"region_id":"DP04295r006","statement":[{"text":"The ssNMR and cryo-EM structures show that the core of the RIPK3-CTD fibril is very small, consisting of only ∼20 residues out of a total of over 100 residues of RIPK3-CTD (Fig. 3A). The rest of the residues in the CTD remain flexible and are invisible by either cryo-EM or ssNMR.","type":"Results"}]},{"start":418,"end":446,"reference_id":"33790016","reference_source":"pmid","reference_html":"The structure of a minimum amyloid fibril core formed by necroptosis-mediating RHIM of human RIPK3. <i> Wu X, Ma Y, Zhao K, Zhang J, Sun Y, Li Y, Dong X, Hu H, Liu J, Wang J, Zhang X, Li B, Wang H, Li D, Sun B, Lu J, Liu C. </i> Proc Natl Acad Sci U S A, 2021","date":"2024-11-19T17:43:38.415Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7DAC"}],"region_id":"DP04295r007","statement":[{"text":"The ssNMR and cryo-EM structures show that the core of the RIPK3-CTD fibril is very small, consisting of only ∼20 residues out of a total of over 100 residues of RIPK3-CTD (Fig. 3A). The rest of the residues in the CTD remain flexible and are invisible by either cryo-EM or ssNMR.","type":"Results"}]},{"start":447,"end":475,"reference_id":"33790016","reference_source":"pmid","reference_html":"The structure of a minimum amyloid fibril core formed by necroptosis-mediating RHIM of human RIPK3. <i> Wu X, Ma Y, Zhao K, Zhang J, Sun Y, Li Y, Dong X, Hu H, Liu J, Wang J, Zhang X, Li B, Wang H, Li D, Sun B, Lu J, Liu C. </i> Proc Natl Acad Sci U S A, 2021","date":"2024-11-19T17:46:04.802Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7DAC"}],"region_id":"DP04295r008","statement":[{"text":"The ssNMR and cryo-EM structures show that the core of the RIPK3-CTD fibril is very small, consisting of only ∼20 residues out of a total of over 100 residues of RIPK3-CTD (Fig. 3A). The rest of the residues in the CTD remain flexible and are invisible by either cryo-EM or ssNMR.","type":"Results"},{"text":"Only residues from P448 to P475 gave ssNMR signals, indicating the location of the rigid fibril core (chemical shift assignment was shown in SI Appendix, Table S1).","type":"Results"},{"text":"The RIPK3-CTD fibril core is highly ordered and compact featuring an S-shaped architecture, consisting of three β-strands (strands 1 through 3) stacking along the fibril axis in a parallel and in-register fashion (Fig. 3D).","type":"Results"}]},{"start":447,"end":475,"reference_id":"33790016","reference_source":"pmid","reference_html":"The structure of a minimum amyloid fibril core formed by necroptosis-mediating RHIM of human RIPK3. <i> Wu X, Ma Y, Zhao K, Zhang J, Sun Y, Li Y, Dong X, Hu H, Liu J, Wang J, Zhang X, Li B, Wang H, Li D, Sun B, Lu J, Liu C. </i> Proc Natl Acad Sci U S A, 2021","date":"2024-11-19T17:47:32.708Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7DAC"}],"region_id":"DP04295r009","statement":[{"text":"The ssNMR and cryo-EM structures show that the core of the RIPK3-CTD fibril is very small, consisting of only ∼20 residues out of a total of over 100 residues of RIPK3-CTD (Fig. 3A). The rest of the residues in the CTD remain flexible and are invisible by either cryo-EM or ssNMR.","type":"Results"},{"text":"Only residues from P448 to P475 gave ssNMR signals, indicating the location of the rigid fibril core (chemical shift assignment was shown in SI Appendix, Table S1).","type":"Results"},{"text":"The RIPK3-CTD fibril core is highly ordered and compact featuring an S-shaped architecture, consisting of three β-strands (strands 1 through 3) stacking along the fibril axis in a parallel and in-register fashion (Fig. 3D).","type":"Results"},{"text":"Upon fibril formation this region gets compact and ordered as it act as the core of the fibrils.","type":"Curator statement"}],"states_connection":[{"source":"DP04295r001","target":"DP04295r008"}]},{"start":448,"end":469,"reference_id":"33790016","reference_source":"pmid","reference_html":"The structure of a minimum amyloid fibril core formed by necroptosis-mediating RHIM of human RIPK3. <i> Wu X, Ma Y, Zhao K, Zhang J, Sun Y, Li Y, Dong X, Hu H, Liu J, Wang J, Zhang X, Li B, Wang H, Li D, Sun B, Lu J, Liu C. </i> Proc Natl Acad Sci U S A, 2021","date":"2024-11-19T17:51:27.314Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7DA4"},{"db":"EMDB","id":"30622"}],"region_id":"DP04295r010","statement":[{"text":"The ssNMR and cryo-EM structures show that the core of the RIPK3-CTD fibril is very small, consisting of only ∼20 residues out of a total of over 100 residues of RIPK3-CTD (Fig. 3A). The rest of the residues in the CTD remain flexible and are invisible by either cryo-EM or ssNMR.","type":"Results"},{"text":"The RIPK3-CTD fibril core is highly ordered and compact featuring an S-shaped architecture, consisting of three β-strands (strands 1 through 3) stacking along the fibril axis in a parallel and in-register fashion (Fig. 3D).","type":"Results"},{"text":"Upon fibril formation this region gets compact and ordered as it act as the core of the fibrils.","type":"Curator statement"}],"states_connection":[{"source":"DP04295r001","target":"DP04295r011"}]},{"start":448,"end":469,"reference_id":"33790016","reference_source":"pmid","reference_html":"The structure of a minimum amyloid fibril core formed by necroptosis-mediating RHIM of human RIPK3. <i> Wu X, Ma Y, Zhao K, Zhang J, Sun Y, Li Y, Dong X, Hu H, Liu J, Wang J, Zhang X, Li B, Wang H, Li D, Sun B, Lu J, Liu C. </i> Proc Natl Acad Sci U S A, 2021","date":"2024-11-19T17:49:03.758Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7DA4"},{"db":"EMDB","id":"30622"}],"region_id":"DP04295r011","statement":[{"text":"The ssNMR and cryo-EM structures show that the core of the RIPK3-CTD fibril is very small, consisting of only ∼20 residues out of a total of over 100 residues of RIPK3-CTD (Fig. 3A). The rest of the residues in the CTD remain flexible and are invisible by either cryo-EM or ssNMR.","type":"Results"},{"text":"The RIPK3-CTD fibril core is highly ordered and compact featuring an S-shaped architecture, consisting of three β-strands (strands 1 through 3) stacking along the fibril axis in a parallel and in-register fashion (Fig. 3D).","type":"Results"},{"text":"Upon fibril formation this region gets compact and ordered as it act as the core of the fibrils.","type":"Curator statement"}]},{"start":388,"end":518,"reference_id":"33790016","reference_source":"pmid","reference_html":"The structure of a minimum amyloid fibril core formed by necroptosis-mediating RHIM of human RIPK3. <i> Wu X, Ma Y, Zhao K, Zhang J, Sun Y, Li Y, Dong X, Hu H, Liu J, Wang J, Zhang X, Li B, Wang H, Li D, Sun B, Lu J, Liu C. </i> Proc Natl Acad Sci U S A, 2021","date":"2024-11-19T18:13:40.737Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7DA4"},{"db":"EMDB","id":"30622"}],"ec_go":"IDA","region_id":"DP04295r012","statement":[{"text":"The cryo-EM structure reveals that the RIPK3-CTD fibril features a small fibril pitch of ∼23 nm and a large twist angle of −7.53° (Fig. 2C and SI Appendix, Fig. S3C). ","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false},{"start":388,"end":518,"reference_id":"29681455","reference_source":"pmid","reference_html":"The Structure of the Necrosome RIPK1-RIPK3 Core, a Human Hetero-Amyloid Signaling Complex. <i> Mompeán M, Li W, Li J, Laage S, Siemer AB, Bozkurt G, Wu H, McDermott AE. </i> Cell, 2018","date":"2024-11-19T18:20:08.310Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0097342","term_name":"ripoptosome","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"5V7Z"}],"ec_go":"EXP","region_id":"DP04295r013","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q13546"}],"statement":[{"text":"Here we present the high-resolution solid-state nuclear magnetic resonance (SSNMR) structure of the RIPK1-RIPK3 amyloidal signaling complex, featuring sequential and specific stacking to form a hetero-amyloid serpentine fold, stabilized by hydrophobic packing and enriched with interactions along the fibrillar axis such as Asn and Gln ladders, Tyr stacking, and an unusual Cys-Ser ladder.","type":"Results"}],"term_comment":"It has been shown that receptor-mediated necroptotic signaling pathway requires assembly of a ripoptosome protein complex consisting of caspase-8, caspase-10, Fas-associated death domain protein (FADD), casp8 and FADD-like apoptosis regulator (CFLAR) as well as the two receptor-interacting serine/threonine-protein kinases RIPK1 and RIPK3 (PMID:21737330). Optionally, depending on the receptor activated, this complex may contain TLR3 adaptor protein TRIF (PMID:21737330).","term_def":"\"A protein complex whose core components are the receptor-interacting serine/threonine-protein kinases RIPK1 and RIPK3 (also called RIP1 and RIP3). Formation of the ripoptosome can induce an extrinsic apoptotic signaling pathway or a necroptotic signaling pathway. The composition of this protein complex may depend on several factors including nature of the signal, cell type and more.\" [GOC:bhm, GOC:mtg_apoptosis, PMID:22265414, PMID:22274400]","term_is_obsolete":false,"term_not_annotate":false},{"start":448,"end":462,"reference_id":"29681455","reference_source":"pmid","reference_html":"The Structure of the Necrosome RIPK1-RIPK3 Core, a Human Hetero-Amyloid Signaling Complex. <i> Mompeán M, Li W, Li J, Laage S, Siemer AB, Bozkurt G, Wu H, McDermott AE. </i> Cell, 2018","date":"2024-11-19T18:29:51.589Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0120283","term_name":"protein serine/threonine kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"5V7Z"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q13546","operator":null,"partner_start":496,"partner_end":583}],"region_id":"DP04295r014","statement":[{"text":"Here we present the high-resolution solid-state nuclear magnetic resonance (SSNMR) structure of the RIPK1-RIPK3 amyloidal signaling complex, featuring sequential and specific stacking to form a hetero-amyloid serpentine fold, stabilized by hydrophobic packing and enriched with interactions along the fibrillar axis such as Asn and Gln ladders, Tyr stacking, and an unusual Cys-Ser ladder.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein serine/threonine kinase.\" [GOC:krc, GOC:sl, PMID:28608965]","term_is_obsolete":false,"term_not_annotate":false},{"start":446,"end":464,"reference_id":"22817896","reference_source":"pmid","reference_html":"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. <i> Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. </i> Cell, 2012","date":"2024-11-19T18:30:17.146Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0120283","term_name":"protein serine/threonine kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006077","ec_ontology":"ECO","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q13546","operator":null,"partner_start":525,"partner_end":555}],"region_id":"DP04295r015","statement":[{"text":"His-tag pull-down experiments of the coexpression constructs showed that the interaction was retained, even when RIP1 was only 31 residues (525–555) and RIP3 was only 19 residues (446–464) in length (Figures 3A, S3A, and S3B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein serine/threonine kinase.\" [GOC:krc, GOC:sl, PMID:28608965]","term_is_obsolete":false,"term_not_annotate":false},{"start":388,"end":518,"reference_id":"22817896","reference_source":"pmid","reference_html":"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. <i> Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. </i> Cell, 2012","date":"2024-11-20T16:25:41.640Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP04295r016","statement":[{"text":"(E) Superimposed Fourier transform infrared spectra of RIP/RIP3-RHIM (magenta) and the I539D mutant of RIP1 (cyan). Only the WT RIP1/RIP3 complexes, not the RHIM mutant, showed the amide I’ maxima at 1,623 cm−1 (dashed vertical red line), which is characteristic of β-amyloid.","type":"Figure"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q13546"}]},{"start":388,"end":518,"reference_id":"22817896","reference_source":"pmid","reference_html":"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. <i> Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. </i> Cell, 2012","date":"2024-11-20T16:33:17.958Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1901026","term_name":"ripoptosome assembly involved in necroptotic process","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IMP","region_id":"DP04295r017","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"},{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0320","entry_name":"HT 29"}],"statement":[{"text":"Clustering of RIP1 and RIP3 into punctate-like structures is a distinct feature of necrosis (Figures S6B–S6D). This was confirmed by immunogold EM (Figure 6F). When HeLa cells, which do not express endogenous RIP3, were transfected with RIP3-mCherry and stimulated with TNF, zVAD-fmk, and LBW242 to induce necrosis, they showed complete overlap of ThT staining with RIP3-mCherry puncta (Figure 6G).","type":"Results"},{"text":"As expected, WT RIP3-transfected cells underwent cell death, whereas the RHIM AAAA mutant was highly protected. Importantly, RIP3 mutants V458P, V460P, and G457D protected cells from TNF-induced necrosis, whereas the mutant N464D that did not show significant defects in vitro behaved most similar to the WT (Figure 7A). In addition, mutants V458P and V460P completely abolished puncta formation in response to necrosis stimulation, whereas G457D partially disrupted RIP3 clustering (Figure 7B).","type":"Results"}],"term_comment":"","term_def":"\"The aggregation, arrangement and bonding together of ripoptosome components leading to a necroptotic process.\" [GOC:mtg_apoptosis, GOC:TermGenie, PMID:22274400]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00484","term_name":"deletion-insertion","term_namespace":"Protein mutation","value":"p.Val458_Gln461delinsAlaAlaAlaAla","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu457Asn","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val458Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val460Pro","start":null,"end":null,"position":null},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}]},{"start":457,"end":461,"reference_id":"22817896","reference_source":"pmid","reference_html":"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. <i> Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. </i> Cell, 2012","date":"2024-11-19T19:13:46.988Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0070266","term_name":"necroptotic process","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00484","term_name":"deletion-insertion","term_namespace":"Protein mutation","value":"p.Val458_Gln461delinsAlaAlaAlaAla","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val458Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val460Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu457Asn","start":null,"end":null,"position":null},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"ec_go":"IMP","region_id":"DP04295r018","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"statement":[{"text":"RHIM Residues of RIP1 and RIP3 Are Crucial for Cluster Formation, Kinase Activation, and Programmed Necrosis","type":"Results"},{"text":"For RIP3, we stimulated HeLa cells transfected with WT and mutant RIP3-yellow fluorescent protein (YFP) with TNF, zVAD-fmk, and LBW242. As expected, WT RIP3-transfected cells underwent cell death, whereas the RHIM AAAA mutant was highly protected. Importantly, RIP3 mutants V458P, V460P, and G457D protected cells from TNF-induced necrosis, whereas the mutant N464D that did not show significant defects in vitro behaved most similar to the WT (Figure 7A).","type":"Results"}],"term_comment":"Examples of this are Birc2 and Birc3 (UniProt symbols Q62210 and O08863) in PMID:21052097.","term_def":"\"A programmed necrotic cell death process which begins when a cell receives a signal (e.g. a ligand binding to a death receptor or to a Toll-like receptor), and proceeds through a series of biochemical events (signaling pathways), characterized by activation of receptor-interacting serine/threonine-protein kinase 1 and/or 3 (RIPK1/3, also called RIP1/3) and by critical dependence on mixed lineage kinase domain-like (MLKL), and which typically lead to common morphological features of necrotic cell death. The process ends when the cell has died. The process is divided into a signaling phase, and an execution phase, which is triggered by the former.\" [GOC:BHF, GOC:dph, GOC:mah, GOC:mtg_apoptosis, GOC:tb, PMID:18846107, PMID:20823910, PMID:21737330, PMID:21760595, PMID:21876153]","term_is_obsolete":false,"term_not_annotate":false},{"start":457,"end":461,"reference_id":"22817896","reference_source":"pmid","reference_html":"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. <i> Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. </i> Cell, 2012","date":"2024-11-20T16:54:05.710Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0032147","term_name":"activation of protein kinase activity","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val458Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val460Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu457Asn","start":null,"end":null,"position":null},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"ec_go":"IMP","region_id":"DP04295r019","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"},{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0594","entry_name":"3T3-Swiss"}],"statement":[{"text":"RHIM Residues of RIP1 and RIP3 Are Crucial for Cluster Formation, Kinase Activation, and Programmed Necrosis","type":"Results"},{"text":"Expression of RIP3-YFP in 293T cells showed that the mutations V458P and V460P severely compromised RIP3 kinase activation by using myelin basic protein (MBP) as the substrate (Figure S7A). To further validate the results from transient expression, we stably reconstituted RIP3−/− fibroblasts with WT and mutant RIP3. In agreement with results in 293T cells, WT RIP3 showed robust kinase activity upon induction of necrosis, whereas the V458P, V460P, and G457D mutants were dramatically impaired in kinase activation (Figure 7C).","type":"Results"}],"term_comment":"","term_def":"\"Any process that initiates the activity of an inactive protein kinase.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":300,"end":518,"reference_id":"22817896","reference_source":"pmid","reference_html":"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. <i> Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. </i> Cell, 2012","date":"2024-11-20T15:26:35.671Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008035","ec_ontology":"ECO","ec_name":"author inference based on intrinsic disorder prediction used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04295r020","statement":[{"text":"We investigated why RIP1/3-RHIM and RIP1/3-FL could form such large complexes. Secondary structure predictions suggested that the region between the KD and the DD in RIP1 (~residues 300–560) and the region C-terminal to the KD in RIP3 (~residues 300-end) are mostly unstructured random coils (Rost et al., 2004).","type":"Results"}]}],"regions_counter":20,"released":"2025_06","sequence":"MSCVKLWPSGAPAPLVSIEELENQELVGKGGFGTVFRAQHRKWGYDVAVKIVNSKAISREVKAMASLDNEFVLRLEGVIEKVNWDQDPKPALVTKFMENGSLSGLLQSQCPRPWPLLCRLLKEVVLGMFYLHDQNPVLLHRDLKPSNVLLDPELHVKLADFGLSTFQGGSQSGTGSGEPGGTLGYLAPELFVNVNRKASTASDVYSFGILMWAVLAGREVELPTEPSLVYEAVCNRQNRPSLAELPQAGPETPGLEGLKELMQLCWSSEPKDRPSFQECLPKTDEVFQMVENNMNAAVSTVKDFLSQLRSSNRRFSIPESGQGGTEMDGFRRTIENQHSRNDVMVSEWLNKLNLEEPPSSVPKKCPSLTKRSRAQEEQVPQAWTAGTSSDSMAQPPQTPETSTFRNQMPSPTSTGTPSPGPRGNQGAERQGMNWSCRTPEPNPVTGRPLVNIYNCSGVQVGDNNYLTMQQTTALPTWGLAPSGKGRGLQHPPPVGSQEGPKDPEAWSRPQGWYNHSGK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.4015444015444015,"dataset":["Condensates-related proteins"],"disorder_content":0.42277992277992277,"disprot_consensus":{"full":[{"start":300,"end":446,"type":"D"},{"start":447,"end":475,"type":"T"},{"start":476,"end":518,"type":"D"}],"Structural state":[{"start":300,"end":518,"type":"D"}],"Biological process":[{"start":387,"end":518,"type":"F"}],"Molecular function":[{"start":430,"end":465,"type":"F"}],"Structural transition":[{"start":447,"end":475,"type":"T"}],"Cellular component":[{"start":388,"end":518,"type":"F"}]}},{"disprot_id":"DP04296","acc":"Q12517","creator":"zskalman","date":"2024-11-20T10:24:23.468Z","features":{"pfam":[{"id":"PF06058","name":"Dcp1-like decapping family","start":19,"end":77},{"id":"PF06058","name":"Dcp1-like decapping family","start":138,"end":219}],"gene3D":[]},"genes":[{"name":{"value":"DCP1"},"olnNames":[{"value":"YOL149W"}]}],"length":231,"name":"mRNA-decapping enzyme subunit 1","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":16,"reference_id":"14758354","reference_source":"pmid","reference_html":"Crystal structure of Dcp1p and its functional implications in mRNA decapping. <i> She M, Decker CJ, Sundramurthy K, Liu Y, Chen N, Parker R, Song H. </i> Nat Struct Mol Biol, 2004","date":"2024-11-20T10:25:55.878Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"1Q67"}],"region_id":"DP04296r001","statement":[{"text":"Several regions of the polypeptide are not visible in the electron density map and are assumed to be disordered, namely residues 1-21, 74-134 and 229-231 for molecule A, and residues 1-16 and 81-134 for molecule B in the crystallographic asymmetric unit. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-05T14:48:00.606Z"}},{"start":81,"end":134,"reference_id":"14758354","reference_source":"pmid","reference_html":"Crystal structure of Dcp1p and its functional implications in mRNA decapping. <i> She M, Decker CJ, Sundramurthy K, Liu Y, Chen N, Parker R, Song H. </i> Nat Struct Mol Biol, 2004","date":"2024-11-20T10:26:08.344Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"1Q67"}],"region_id":"DP04296r002","statement":[{"text":"Several regions of the polypeptide are not visible in the electron density map and are assumed to be disordered, namely residues 1-21, 74-134 and 229-231 for molecule A, and residues 1-16 and 81-134 for molecule B in the crystallographic asymmetric unit. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-05T14:48:00.900Z"}}],"regions_counter":2,"released":"2025_06","sequence":"MTGAATAAENSATQLEFYRKALNFNVIGRYDPKIKQLLFHTPHASLYKWDFKKDEWNKLEYQGVLAIYLRDVSQNTNLLPVSPQEVDIFDSQNGSNNIQVNNGSDNSNRNSSGNGNSYKSNDSLTYNCGKTLSGKDIYNYGLIILNRINPDNFSMGIVPNSVVNKRKVFNAEEDTLNPLECMGVEVKDELVIIKNLKHEVYGIWIHTVSDRQNIYELIKYLLENEPKDSFA","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.17316017316017315,"dataset":["Condensates-related proteins","RNA-binding proteins"],"disorder_content":0.30303030303030304,"disprot_consensus":{"full":[{"start":1,"end":16,"type":"D"},{"start":81,"end":134,"type":"D"}],"Structural state":[{"start":1,"end":16,"type":"D"},{"start":81,"end":134,"type":"D"}]}},{"disprot_id":"DP04297","acc":"Q9NPJ4","creator":"zskalman","date":"2024-11-20T10:31:49.533Z","features":{"pfam":[{"id":"PF15365","name":"Proline-rich nuclear receptor coactivator motif","start":93,"end":111}],"gene3D":[]},"genes":[{"name":{"value":"PNRC2"},"orfNames":[{"value":"HSPC208"}]}],"length":139,"name":"Proline-rich nuclear receptor coactivator 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":101,"reference_id":"23085078","reference_source":"pmid","reference_html":"Structural basis of the PNRC2-mediated link between mrna surveillance and decapping. <i> Lai T, Cho H, Liu Z, Bowler MW, Piao S, Parker R, Kim YK, Song H. </i> Structure, 2012","date":"2024-11-20T10:34:05.639Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"cross_refs":[{"db":"PDB","id":"4B6H"}],"region_id":"DP04297r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9NPI6"}],"sequence_construct":"MGSSHHHHHHSQDPMGGGERYNIPAPQSRNVSKNQQQLNRQKTKEQNSQMKIVHKKKERGHGYNSSAAAWQAMQNGGKNKNFPNNQSWNSSLSGPRLLFKSQANQNYAGAKFSEPPSPSVLPKPPSHWVPVSFNP","statement":[{"text":"Residues 1–130 of Dcp1aEVH1 and a stretch of PNRC2 polypeptide chain comprising 14 residues (residues 102 to 115) are visible in the electron density map with the rest of the residues in PNRC2 (residues 1–101 and residues 116–121) assumed to be disordered as there is no interpretable electron density for these regions. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-05T14:52:30.466Z"}}],"regions_counter":1,"released":"2025_06","sequence":"MGGGERYNIPAPQSRNVSKNQQQLNRQKTKEQNSQMKIVHKKKERGHGYNSSAAAWQAMQNGGKNKNFPNNQSWNSSLSGPRLLFKSQANQNYAGAKFSEPPSPSVLPKPPSHWVPVSFNPSDKEIMTFQLKTLLKVQV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.11510791366906475,"dataset":["RNA-binding proteins"],"disorder_content":0.7266187050359713,"disprot_consensus":{"full":[{"start":1,"end":101,"type":"D"}],"Structural state":[{"start":1,"end":101,"type":"D"}]}},{"disprot_id":"DP04298","acc":"Q13546","creator":"vnugnes","date":"2024-11-20T15:24:20.458Z","features":{"pfam":[{"id":"PF00531","name":"Death domain","start":585,"end":666},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":21,"end":284}],"gene3D":[]},"genes":[{"name":{"value":"RIPK1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:10019","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:10019"}}]},"synonyms":[{"value":"RIP","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8612133","url":"http://www.ncbi.nlm.nih.gov/pubmed/8612133","alternativeUrl":"https://europepmc.org/abstract/MED/8612133"}}]},{"value":"RIP1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"16603398","url":"http://www.ncbi.nlm.nih.gov/pubmed/16603398","alternativeUrl":"https://europepmc.org/abstract/MED/16603398"}}]}]}],"length":671,"name":"Receptor-interacting serine/threonine-protein kinase 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":300,"end":560,"reference_id":"22817896","reference_source":"pmid","reference_html":"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. <i> Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. </i> Cell, 2012","date":"2025-01-27T14:42:20.201Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008035","ec_ontology":"ECO","ec_name":"author inference based on intrinsic disorder prediction used in manual assertion","unpublished":true,"released":"2025_06","version":1,"region_id":"DP04298r001","statement":[{"text":"We investigated why RIP1/3-RHIM and RIP1/3-FL could form such large complexes. Secondary structure predictions suggested that the region between the KD and the DD in RIP1 (~residues 300–560) and the region C-terminal to the KD in RIP3 (~residues 300-end) are mostly unstructured random coils (Rost et al., 2004).","type":"Results"}]},{"start":496,"end":531,"reference_id":"22817896","reference_source":"pmid","reference_html":"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. <i> Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. </i> Cell, 2012","date":"2025-01-27T14:43:20.111Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"region_id":"DP04298r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y572"}],"statement":[{"text":"Using the mapped amyloid core sequences (Figures 1B and ​and3A)3A) as targets, the majority of the peaks in the NCA spectrum were assigned, with 16 residues of RIP1 (T532–Y544 and Y546–E548) and 6 consecutive residues of RIP3 (G457–D462) (Figures 3C and 3D).","type":"Results"},{"text":"The spectra recorded with cross-polarization (CP)-based solid-state NMR above 0°C can be explained by ~37 resolved residues. Most of the residues outside the β-amyloid core were unobserved and either too dynamic or disordered to be visible in these spectra.","type":"Results"},{"text":"blablbalba","type":"Abstract"}]},{"start":549,"end":583,"reference_id":"22817896","reference_source":"pmid","reference_html":"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. <i> Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. </i> Cell, 2012","date":"2025-01-27T14:50:17.134Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"region_id":"DP04298r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y572"}],"statement":[{"text":"Using the mapped amyloid core sequences (Figures 1B and ​and3A)3A) as targets, the majority of the peaks in the NCA spectrum were assigned, with 16 residues of RIP1 (T532–Y544 and Y546–E548) and 6 consecutive residues of RIP3 (G457–D462) (Figures 3C and 3D).","type":"Results"},{"text":"The spectra recorded with cross-polarization (CP)-based solid-state NMR above 0°C can be explained by ~37 resolved residues. Most of the residues outside the β-amyloid core were unobserved and either too dynamic or disordered to be visible in these spectra.","type":"Results"}]},{"start":496,"end":583,"reference_id":"22817896","reference_source":"pmid","reference_html":"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. <i> Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. </i> Cell, 2012","date":"2024-11-20T15:41:35.555Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006003","ec_ontology":"ECO","ec_name":"electron microscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","region_id":"DP04298r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y572"}],"statement":[{"text":"Upon limited proteolysis to remove the flanking domains by subtilisin, the same enzyme used in the nuclear magnetic resonance (NMR) sample preparation (see section “Amyloid Core of the RIP1/RIP3 Complex”), clear fibril structures were revealed for RIP1/3-FL, similar to RIP1/3-RHIM (Figure 1D).","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false},{"start":525,"end":555,"reference_id":"22817896","reference_source":"pmid","reference_html":"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. <i> Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. </i> Cell, 2012","date":"2024-11-20T15:43:30.739Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0120283","term_name":"protein serine/threonine kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006077","ec_ontology":"ECO","ec_name":"bait-prey hybrid interaction evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q9Y572","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04298r005","statement":[{"text":"His-tag pull-down experiments of the coexpression constructs showed that the interaction was retained, even when RIP1 was only 31 residues (525–555) and RIP3 was only 19 residues (446–464) in length (Figures 3A, S3A, and S3B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein serine/threonine kinase.\" [GOC:krc, GOC:sl, PMID:28608965]","term_is_obsolete":false,"term_not_annotate":false},{"start":532,"end":548,"reference_id":"22817896","reference_source":"pmid","reference_html":"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. <i> Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. </i> Cell, 2012","date":"2024-11-20T17:02:00.173Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0120283","term_name":"protein serine/threonine kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP04298r006","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"},{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0320","entry_name":"HT 29"}],"statement":[{"text":"To further elucidate the core size and the secondary structure of the RIP1/RIP3 complex, we used solid-state NMR.","type":"Results"},{"text":"Using the mapped amyloid core sequences (Figures 1B and ​and3A)3A) as targets, the majority of the peaks in the NCA spectrum were assigned, with 16 residues of RIP1 (T532–Y544 and Y546–E548) and 6 consecutive residues of RIP3 (G457–D462) (Figures 3C and 3D).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein serine/threonine kinase.\" [GOC:krc, GOC:sl, PMID:28608965]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"Q9Y572","operator":null,"partner_start":457,"partner_end":462}]},{"start":532,"end":549,"reference_id":"22817896","reference_source":"pmid","reference_html":"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. <i> Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. </i> Cell, 2012","date":"2024-11-20T16:12:01.955Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04298r007","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y572"}],"statement":[{"text":"Using the mapped amyloid core sequences (Figures 1B and ​and3A)3A) as targets, the majority of the peaks in the NCA spectrum were assigned, with 16 residues of RIP1 (T532–Y544 and Y546–E548) and 6 consecutive residues of RIP3 (G457–D462) (Figures 3C and 3D).","type":"Results"},{"text":"Negative and positive values of the difference in secondary chemical shifts between Cα and Cβ (i.e., ΔδCα-ΔδCβ or δCα for Gly) are indicative of β sheet and α-helical conformations, respectively. Most of the residues in the amyloid core are compatible with β sheet conformations, and the 4 central RHIM residues show consecutive negative shift differences (Figures 3D and S3E).","type":"Results"},{"text":"(D) Plot of the difference in secondary chemical shift between Cα and Cβ, indicative of secondary structures (only ΔδCα for Gly).","type":"Figure"}]},{"start":532,"end":549,"reference_id":"22817896","reference_source":"pmid","reference_html":"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. <i> Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. </i> Cell, 2012","date":"2024-11-20T16:12:33.704Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04298r008","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y572"}],"statement":[{"text":"Using the mapped amyloid core sequences (Figures 1B and ​and3A)3A) as targets, the majority of the peaks in the NCA spectrum were assigned, with 16 residues of RIP1 (T532–Y544 and Y546–E548) and 6 consecutive residues of RIP3 (G457–D462) (Figures 3C and 3D).","type":"Results"},{"text":"Negative and positive values of the difference in secondary chemical shifts between Cα and Cβ (i.e., ΔδCα-ΔδCβ or δCα for Gly) are indicative of β sheet and α-helical conformations, respectively. Most of the residues in the amyloid core are compatible with β sheet conformations, and the 4 central RHIM residues show consecutive negative shift differences (Figures 3D and S3E).","type":"Results"},{"text":"(D) Plot of the difference in secondary chemical shift between Cα and Cβ, indicative of secondary structures (only ΔδCα for Gly).","type":"Figure"}],"states_connection":[{"source":"DP04298r001","target":"DP04298r007"}]},{"start":496,"end":583,"reference_id":"22817896","reference_source":"pmid","reference_html":"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. <i> Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. </i> Cell, 2012","date":"2024-11-20T16:16:49.239Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP04298r009","statement":[{"text":"The RIP1 and RIP3 CD spectra showed similar secondary structures as the RIP1/RIP3 complex, and ThT fluorescence and CR absorption confirmed their amyloidal structures (Figure S4). EM of negatively stained RIP1 and RIP3 samples revealed that the homocomplexes are able to form fibrils by themselves as well (Figure 4B). However, these fibrils appeared to be less regular and shorter than those of the RIP1/RIP3 heterocomplex (Figure 1D).","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false},{"start":496,"end":583,"reference_id":"22817896","reference_source":"pmid","reference_html":"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. <i> Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. </i> Cell, 2012","date":"2024-11-20T16:17:03.577Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042802","term_name":"identical protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q13546","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04298r010","statement":[{"text":"The RIP1 and RIP3 CD spectra showed similar secondary structures as the RIP1/RIP3 complex, and ThT fluorescence and CR absorption confirmed their amyloidal structures (Figure S4). EM of negatively stained RIP1 and RIP3 samples revealed that the homocomplexes are able to form fibrils by themselves as well (Figure 4B). However, these fibrils appeared to be less regular and shorter than those of the RIP1/RIP3 heterocomplex (Figure 1D).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein or proteins.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":496,"end":583,"reference_id":"22817896","reference_source":"pmid","reference_html":"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. <i> Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. </i> Cell, 2012","date":"2024-11-20T16:17:17.891Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042802","term_name":"identical protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006333","ec_ontology":"ECO","ec_name":"thioflavin T based fluorescence spectroscopy evidence","unpublished":true,"released":"2025_06","version":0,"interaction_partner":[{"db":"UniProt","id":"Q13546","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04298r011","statement":[{"text":"The RIP1 and RIP3 CD spectra showed similar secondary structures as the RIP1/RIP3 complex, and ThT fluorescence and CR absorption confirmed their amyloidal structures (Figure S4). EM of negatively stained RIP1 and RIP3 samples revealed that the homocomplexes are able to form fibrils by themselves as well (Figure 4B). However, these fibrils appeared to be less regular and shorter than those of the RIP1/RIP3 heterocomplex (Figure 1D).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein or proteins.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":496,"end":583,"reference_id":"22817896","reference_source":"pmid","reference_html":"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. <i> Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. </i> Cell, 2012","date":"2024-11-20T16:17:26.331Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006333","ec_ontology":"ECO","ec_name":"thioflavin T based fluorescence spectroscopy evidence","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04298r012","statement":[{"text":"The RIP1 and RIP3 CD spectra showed similar secondary structures as the RIP1/RIP3 complex, and ThT fluorescence and CR absorption confirmed their amyloidal structures (Figure S4). EM of negatively stained RIP1 and RIP3 samples revealed that the homocomplexes are able to form fibrils by themselves as well (Figure 4B). However, these fibrils appeared to be less regular and shorter than those of the RIP1/RIP3 heterocomplex (Figure 1D).","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false},{"start":496,"end":583,"reference_id":"22817896","reference_source":"pmid","reference_html":"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. <i> Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. </i> Cell, 2012","date":"2024-11-20T16:31:56.305Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP04298r013","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y572"}],"statement":[{"text":"(E) Superimposed Fourier transform infrared spectra of RIP/RIP3-RHIM (magenta) and the I539D mutant of RIP1 (cyan). Only the WT RIP1/RIP3 complexes, not the RHIM mutant, showed the amide I’ maxima at 1,623 cm−1 (dashed vertical red line), which is characteristic of β-amyloid.","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false},{"start":539,"end":545,"reference_id":"22817896","reference_source":"pmid","reference_html":"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. <i> Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. </i> Cell, 2012","date":"2024-11-20T16:48:04.874Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0070266","term_name":"necroptotic process","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00484","term_name":"deletion-insertion","term_namespace":"Protein mutation","value":"p.Ile539_Glu542delinsAlaAlaAlaAla","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile539Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile541Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asn545Pro","start":null,"end":null,"position":null},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"ec_go":"IMP","region_id":"DP04298r014","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0594","entry_name":"3T3-Swiss"}],"statement":[{"text":"Like the RHIM AAAA mutant, the RIP1 mutants I539P, I541P, and N545P were much weaker in mediating necrosis than WT RIP1 (Figure 7D), recapitulating the in vitro interaction data.","type":"Results"},{"text":"Thus, these results define a critical role for RHIM-mediated amyloidal RIP1/RIP3 fibrils in the activation of RIP1/RIP3 kinase activity and the induction of programmed necrosis.","type":"Results"}],"term_comment":"Examples of this are Birc2 and Birc3 (UniProt symbols Q62210 and O08863) in PMID:21052097.","term_def":"\"A programmed necrotic cell death process which begins when a cell receives a signal (e.g. a ligand binding to a death receptor or to a Toll-like receptor), and proceeds through a series of biochemical events (signaling pathways), characterized by activation of receptor-interacting serine/threonine-protein kinase 1 and/or 3 (RIPK1/3, also called RIP1/3) and by critical dependence on mixed lineage kinase domain-like (MLKL), and which typically lead to common morphological features of necrotic cell death. The process ends when the cell has died. The process is divided into a signaling phase, and an execution phase, which is triggered by the former.\" [GOC:BHF, GOC:dph, GOC:mah, GOC:mtg_apoptosis, GOC:tb, PMID:18846107, PMID:20823910, PMID:21737330, PMID:21760595, PMID:21876153]","term_is_obsolete":false,"term_not_annotate":false},{"start":539,"end":545,"reference_id":"22817896","reference_source":"pmid","reference_html":"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. <i> Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. </i> Cell, 2012","date":"2024-11-20T16:49:07.753Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0032147","term_name":"activation of protein kinase activity","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile539Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile541Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asn545Pro","start":null,"end":null,"position":null},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"ec_go":"IMP","region_id":"DP04298r015","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0594","entry_name":"3T3-Swiss"}],"statement":[{"text":"All three RIP1 mutants, I539P, I541P, and N545P, showed defective kinase activation (Figure 7E).","type":"Results"},{"text":"Thus, these results define a critical role for RHIM-mediated amyloidal RIP1/RIP3 fibrils in the activation of RIP1/RIP3 kinase activity and the induction of programmed necrosis.","type":"Results"}],"term_comment":"","term_def":"\"Any process that initiates the activity of an inactive protein kinase.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":539,"end":545,"reference_id":"22817896","reference_source":"pmid","reference_html":"The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis. <i> Li J, McQuade T, Siemer AB, Napetschnig J, Moriwaki K, Hsiao YS, Damko E, Moquin D, Walz T, McDermott A, Chan FK, Wu H. </i> Cell, 2012","date":"2024-11-20T16:53:39.962Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1901026","term_name":"ripoptosome assembly involved in necroptotic process","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile539Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile541Pro","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asn545Pro","start":null,"end":null,"position":null},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"ec_go":"IMP","region_id":"DP04298r016","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0594","entry_name":"3T3-Swiss"}],"statement":[{"text":"Clustering of RIP1 and RIP3 into punctate-like structures is a distinct feature of necrosis (Figures S6B–S6D). This was confirmed by immunogold EM (Figure 6F). When HeLa cells, which do not express endogenous RIP3, were transfected with RIP3-mCherry and stimulated with TNF, zVAD-fmk, and LBW242 to induce necrosis, they showed complete overlap of ThT staining with RIP3-mCherry puncta (Figure 6G).","type":"Results"},{"text":"Similar defects in clustering in mutations within the core RHIM residues were observed with truncated RIP1 (residues 496–583) and RIP3 (residues 388–518) lacking the KDs and DD (Figure S7B).","type":"Results"},{"text":"Spontaneous assembly of RIP1-RHIM and RIP3-RHIM fibrils in vivo requires an intact RHIM. The indicated wild-type and mutant RIP1-CFP and/or RIP3-YFP plasmids were expressed in RIP3/ fibroblasts by transfection.","type":"Supplementary material"},{"text":"Mutations within the RHIM core disrupted the spontaneous assembly of these filaments in the truncation RHIM proteins.","type":"Supplementary material"}],"term_comment":"","term_def":"\"The aggregation, arrangement and bonding together of ripoptosome components leading to a necroptotic process.\" [GOC:mtg_apoptosis, GOC:TermGenie, PMID:22274400]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":17,"released":"2025_06","sequence":"MQPDMSLNVIKMKSSDFLESAELDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLNNEEHNELREVDGTAKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNRPDVDDITEYCPREIISLMKLCWEANPEARPTFPGIEEKFRPFYLSQLEESVEEDVKSLKKEYSNENAVVKRMQSLQLDCVAVPSSRSNSATEQPGSLHSSQGLGMGPVEESWFAPSLEHPQEENEPSLQSKLQDEANYHLYGSRMDRQTKQQPRQNVAYNREEERRRRVSHDPFAQQRPYENFQNTEGKGTAYSSAASHGNAVHQPSGLTSQPQVLYQNNGLYSSHGFGTRPLDPGTAGPRVWYRPIPSHMPSLHNIPVPETNYLGNTPTMPFSSLPPTDESIKYTIYNSTGIQIGAYNYMEIGGTSSSLLDSTNTNFKEEPAAKYQAIFDNTTSLTDKHLDPIRENLGKHWKNCARKLGFTQSQIDEIDHDYERDGLKEKVYQMLQKWVMREGIKGATVGKLAQALHQCSRIDLLSSLIYVSQN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.30402384500745155,"dataset":["Condensates-related proteins"],"disorder_content":0.4232488822652757,"disprot_consensus":{"full":[{"start":300,"end":531,"type":"D"},{"start":532,"end":549,"type":"T"},{"start":550,"end":583,"type":"D"}],"Structural state":[{"start":300,"end":583,"type":"D"}],"Biological process":[{"start":496,"end":583,"type":"F"}],"Molecular function":[{"start":496,"end":583,"type":"F"}],"Structural transition":[{"start":532,"end":549,"type":"T"}]}},{"disprot_id":"DP04299","acc":"O43353","creator":"vnugnes","date":"2024-11-20T17:03:06.071Z","features":{"pfam":[{"id":"PF00619","name":"Caspase recruitment domain","start":437,"end":519},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":22,"end":288}],"gene3D":[]},"genes":[{"name":{"value":"RIPK2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"30026309","url":"http://www.ncbi.nlm.nih.gov/pubmed/30026309","alternativeUrl":"https://europepmc.org/abstract/MED/30026309"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:10020","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:10020"}}]},"synonyms":[{"value":"CARDIAK","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9705938","url":"http://www.ncbi.nlm.nih.gov/pubmed/9705938","alternativeUrl":"https://europepmc.org/abstract/MED/9705938"}}]},{"value":"RICK","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9575181","url":"http://www.ncbi.nlm.nih.gov/pubmed/9575181","alternativeUrl":"https://europepmc.org/abstract/MED/9575181"}}]},{"value":"RIP2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9642260","url":"http://www.ncbi.nlm.nih.gov/pubmed/9642260","alternativeUrl":"https://europepmc.org/abstract/MED/9642260"}}]}],"orfNames":[{"value":"UNQ277/PRO314/PRO34092","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"12975309","url":"http://www.ncbi.nlm.nih.gov/pubmed/12975309","alternativeUrl":"https://europepmc.org/abstract/MED/12975309"}}]}]}],"length":540,"name":"Receptor-interacting serine/threonine-protein kinase 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":173,"end":183,"reference_id":"28545134","reference_source":"pmid","reference_html":"Structures of the inactive and active states of RIP2 kinase inform on the mechanism of activation. <i> Pellegrini E, Signor L, Singh S, Boeri Erba E, Cusack S. </i> PLoS One, 2017","date":"2024-11-20T17:40:34.809Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"5NG0"}],"region_id":"DP04299r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"48828","entry_name":"cobalt(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"40532","entry_name":"adenosine 5'-[beta,gamma-methylene]triphosphate"}],"statement":[{"text":"Both the RIP2K-AMPPCP and RIP2KD146N structures exhibit a disordered AS. Only residues 164–172 and 186–196 could be traced for RIP2K-AMPPCP chain B (S4 Fig), implying that there is no electron density for any of the phosphorylation sites detected by mass spectrometry.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu294Phe","start":null,"end":null,"position":null}]},{"start":519,"end":540,"reference_id":"30279485","reference_source":"pmid","reference_html":"RIP2 filament formation is required for NOD2 dependent NF-κB signalling. <i> Pellegrini E, Desfosses A, Wallmann A, Schulze WM, Rehbein K, Mas P, Signor L, Gaudon S, Zenkeviciute G, Hons M, Malet H, Gutsche I, Sachse C, Schoehn G, Oschkinat H, Cusack S. </i> Nat Commun, 2018","date":"2024-11-20T17:48:59.541Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"EMDB","id":"4399"},{"db":"PDB","id":"6GGS"}],"region_id":"DP04299r002","statement":[{"text":"Interestingly H6 is absent in both the crystal and NMR structures and replaced by a long C-terminal loop, visible only in the NMR structure, which contains putative phosphorylation sites41–43.","type":"Results"}]},{"start":512,"end":540,"reference_id":"30279485","reference_source":"pmid","reference_html":"RIP2 filament formation is required for NOD2 dependent NF-κB signalling. <i> Pellegrini E, Desfosses A, Wallmann A, Schulze WM, Rehbein K, Mas P, Signor L, Gaudon S, Zenkeviciute G, Hons M, Malet H, Gutsche I, Sachse C, Schoehn G, Oschkinat H, Cusack S. </i> Nat Commun, 2018","date":"2024-11-20T17:52:15.219Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"27555"}],"region_id":"DP04299r003","statement":[{"text":"Relying on the distribution of the respective amino acid types in the sequence, this strongly suggests that the missing signals concern residues in the C-terminal segment from 512 to 540. Especially the absence of three proline signal sets, only one being detected, indicates strong structural heterogeneity or mobility in that region where they cluster.","type":"Results"},{"text":"We were not able to assign any cross-peaks to the C-terminal 29 residues that were reported to be flexible by solution NMR investigations40. ","type":"Results"}]}],"regions_counter":3,"released":"2025_06","sequence":"MNGEAICSALPTIPYHKLADLRYLSRGASGTVSSARHADWRVQVAVKHLHIHTPLLDSERKDVLREAEILHKARFSYILPILGICNEPEFLGIVTEYMPNGSLNELLHRKTEYPDVAWPLRFRILHEIALGVNYLHNMTPPLLHHDLKTQNILLDNEFHVKIADFGLSKWRMMSLSQSRSSKSAPEGGTIIYMPPENYEPGQKSRASIKHDIYSYAVITWEVLSRKQPFEDVTNPLQIMYSVSQGHRPVINEESLPYDIPHRARMISLIESGWAQNPDERPSFLKCLIELEPVLRTFEEITFLEAVIQLKKTKLQSVSSAIHLCDKKKMELSLNIPVNHGPQEESCGSSQLHENSGSPETSRSLPAPQDNDFLSRKAQDCYFMKLHHCPGNHSWDSTISGSQRAAFCDHKTTPCSSAIINPLSTAGNSERLQPGIAQQWIQSKREDIVNQMTEACLNQSLDALLSRDLIMKEDYELVSTKPTRTSKVRQLLDTTDIQGEEFAKVIVQKLKDNKQMGLQPYPEILVVSRSPSLNLLQNKSM","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.26666666666666666,"dataset":["Stress response proteins"],"disorder_content":0.07407407407407407,"disprot_consensus":{"full":[{"start":173,"end":183,"type":"D"},{"start":512,"end":540,"type":"D"}],"Structural state":[{"start":173,"end":183,"type":"D"},{"start":512,"end":540,"type":"D"}]}},{"disprot_id":"DP04300","acc":"Q9UBB9","creator":"eficho","date":"2024-11-20T19:11:46.987Z","features":{"pfam":[{"id":"PF01585","name":"G-patch domain","start":149,"end":192},{"id":"PF07842","name":"GC-rich sequence DNA-binding factor-like protein","start":397,"end":666},{"id":"PF12457","name":"Tuftelin interacting protein N terminal","start":18,"end":107},{"id":"PF31031","name":"TFIP11 C-terminal domain","start":774,"end":837}],"gene3D":[]},"genes":[{"name":{"value":"TFIP11"},"synonyms":[{"value":"STIP"}],"orfNames":[{"value":"HSPC006"}]}],"length":837,"name":"Tuftelin-interacting protein 11","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":350,"reference_id":"39089542","reference_source":"pmid","reference_html":"Intrinsic disorder and salt-dependent conformational changes of the N-terminal region of TFIP11 splicing factor. <i> Juniku B, Mignon J, Carême R, Genco A, Obeid AM, Mottet D, Monari A, Michaux C. </i> Int J Biol Macromol, 2024","date":"2025-03-18T17:20:37.153Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04300r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":200,"db":"ChEBI","id":"26710","entry_name":"sodium chloride"}],"statement":[{"text":"First, the far-UV CD signature of the protein in 200 mM NaCl (Fig. 7), providing secondary structure information, is characteristic of random coil with a strong negative band at 205 nm. The very weak positive band between 195 and 200 nm further demonstrates for the first time at experimental level that the human TFIP11 N-TER is mainly disordered.","type":"Results"}],"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7.4}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-04-02T18:47:58.348Z"}},{"start":1,"end":350,"reference_id":"39089542","reference_source":"pmid","reference_html":"Intrinsic disorder and salt-dependent conformational changes of the N-terminal region of TFIP11 splicing factor. <i> Juniku B, Mignon J, Carême R, Genco A, Obeid AM, Mottet D, Monari A, Michaux C. </i> Int J Biol Macromol, 2024","date":"2025-03-18T17:19:18.477Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":20}],"region_id":"DP04300r002","statement":[{"text":"ITF data are in agreement with MD simulations, pointing out that the conformational ensemble of TFIP11 N-TER is more disordered in 200 mM than in 0 mM NaCl, due to the maximisation of electrostatic interactions with the ions in solution. ","type":"Results"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"26710","entry_name":"sodium chloride"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-04-02T18:47:30.507Z"}},{"start":1,"end":350,"reference_id":"39089542","reference_source":"pmid","reference_html":"Intrinsic disorder and salt-dependent conformational changes of the N-terminal region of TFIP11 splicing factor. <i> Juniku B, Mignon J, Carême R, Genco A, Obeid AM, Mottet D, Monari A, Michaux C. </i> Int J Biol Macromol, 2024","date":"2025-03-18T17:19:57.077Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":20}],"region_id":"DP04300r003","statement":[{"text":"ITF data are in agreement with MD simulations, pointing out that the conformational ensemble of TFIP11 N-TER is more disordered in 200 mM than in 0 mM NaCl, due to the maximisation of electrostatic interactions with the ions in solution. This indicates a conformational dynamic where the state of Trp residues can vary from fully exposed to more buried depending on the environment.","type":"Results"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"26710","entry_name":"sodium chloride"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-04-02T18:47:48.945Z"}},{"start":1,"end":350,"reference_id":"39089542","reference_source":"pmid","reference_html":"Intrinsic disorder and salt-dependent conformational changes of the N-terminal region of TFIP11 splicing factor. <i> Juniku B, Mignon J, Carême R, Genco A, Obeid AM, Mottet D, Monari A, Michaux C. </i> Int J Biol Macromol, 2024","date":"2025-02-25T14:44:48.216Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008035","ec_ontology":"ECO","ec_name":"author inference based on intrinsic disorder prediction used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04300r004","statement":[{"text":"The three IDRs are located at the N-TER region and are separated by shorter flexible segments for which the disorder score varies between 0.2 and 0.5. The first disordered region (IDR1) is comprised between residues 1 and 50 and is followed by two longer disordered regions comprising residues 85–145 (IDR2) and 190–265 (IDR3). Due to a much larger variability amongst the predictors for the residues comprised between the position 270 and 350, we restrain to assign this segment as an IDR. Nevertheless, scores close to the 0.5 threshold indicate that a large flexibility is still present in this region.","type":"Results"},{"text":"The TFIP11 N-TER region displays both low mean net charge and hydropathy and is found above the boundary defined by the equation <R ≥ 2.785<H > − 1.15, i.e. clearly laying in the IDP area, strongly supporting the assignation of the N-TER domain as a mainly disordered one.","type":"Results"}]},{"start":1,"end":350,"reference_id":"39089542","reference_source":"pmid","reference_html":"Intrinsic disorder and salt-dependent conformational changes of the N-terminal region of TFIP11 splicing factor. <i> Juniku B, Mignon J, Carême R, Genco A, Obeid AM, Mottet D, Monari A, Michaux C. </i> Int J Biol Macromol, 2024","date":"2025-02-25T14:58:06.813Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"TFIP11 N-TER recombinant protein was overexpressed with a 6xHis-tag at its N-terminus using a pET-like vector in E. coli BL21 (DE3) cells."}]}],"region_id":"DP04300r005","statement":[{"text":"First, the far-UV CD signature of the protein in 200 mM NaCl (Fig. 7), providing secondary structure information, is characteristic of random coil with a strong negative band at 205 nm. The very weak positive band between 195 and 200 nm further demonstrates for the first time at experimental level that the human TFIP11 N-TER is mainly disordered.","type":"Results"},{"text":"In 0 mM NaCl, a significant change is observed in the CD spectrum revealing two broad negative bands at 220 and 226 nm, as well as a broad positive band centred at 199 nm, indicating a significant decrease in the disorder content to give a predominance of ß-sheets.","type":"Results"},{"text":"Interestingly, the CD footprint observed at 0 mM NaCl shows an enrichment in ß-sheets, suggesting an amyloid-like fibrillation of the protein, as already observed for various IDPs which are prone to aggregate [66,67].","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":200,"db":"ChEBI","id":"26710","entry_name":"sodium chloride"}]},{"start":1,"end":350,"reference_id":"39089542","reference_source":"pmid","reference_html":"Intrinsic disorder and salt-dependent conformational changes of the N-terminal region of TFIP11 splicing factor. <i> Juniku B, Mignon J, Carême R, Genco A, Obeid AM, Mottet D, Monari A, Michaux C. </i> Int J Biol Macromol, 2024","date":"2025-02-25T15:01:06.741Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0034205","term_name":"amyloid-beta formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007013","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"TFIP11 N-TER recombinant protein was overexpressed with a 6xHis-tag at its N-terminus using a pET-like vector in E. coli BL21 (DE3) cells."}]}],"region_id":"DP04300r006","statement":[{"text":"Interestingly, the CD footprint observed at 0 mM NaCl shows an enrichment in ß-sheets, suggesting an amyloid-like fibrillation of the protein, as already observed for various IDPs which are prone to aggregate [66,67].","type":"Results"},{"text":"Interestingly, a second band appears at 470 nm, which is most likely associated to deep-blue autofluorescence (dbAF), an intrinsic fluorescence mainly found in proteins forming amyloid fibrils [70].","type":"Results"},{"text":"Nevertheless, the presence of such dbAF signal, in conjunction with the main ß-sheet CD signature, suggests that in the absence of salt, TFIP11 N-TER might tend to assemble into stable aggregates and adopt more ordered structures.","type":"Results"}],"term_comment":"Note that this term does not fall under the general GO definition for biosynthetic processes, which is 'The chemical reactions and pathways resulting in the formation of... ', because amyloid-beta can only be formed by the proteolysis of a larger molecule (see term definition). The word 'formation' is therefore used in place of biosynthesis. Also, note that this term refers to the production of the amyloid-beta polypeptide from the amyloid precursor protein (APP), and should be used to annotate e.g. secretases that cleave APP to form amyloid-beta. To annotate gene products involved in the formation of amyloid fibrils, please consider 'amyloid fibril formation' (GO:1990000).","term_def":"\"The generation of amyloid-beta by cleavage of the amyloid precursor protein (APP).\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":6,"released":"2025_06","sequence":"MSLSHLYRDGEGRIDDDDDERENFEITDWDLQNEFNPNRQRHWQTKEEATYGVWAERDSDDERPSFGGKRARDYSAPVNFISAGLKKGAAEEAELEDSDDEEKPVKQDDFPKDFGPRKLKTGGNFKPSQKGFAGGTKSFMDFGSWERHTKGIGQKLLQKMGYVPGRGLGKNAQGIINPIEAKQRKGKGAVGAYGSERTTQSMQDFPVVDSEEEAEEEFQKELSQWRKDPSGSKKKPKYSYKTVEELKAKGRISKKLTAPQKELSQVKVIDMTGREQKVYYSYSQISHKHNVPDDGLPLQSQQLPQSGKEAKAPGFALPELEHNLQLLIDLTEQEIIQNDRQLQYERDMVVNLFHELEKMTEVLDHEERVISNLSKVLEMVEECERRMQPDCSNPLTLDECARIFETLQDKYYEEYRMSDRVDLAVAIVYPLMKEYFKEWDPLKDCTYGTEIISKWKSLLENDQLLSHGGQDLSADAFHRLIWEVWMPFVRNIVTQWQPRNCDPMVDFLDSWVHIIPVWILDNILDQLIFPKLQKEVENWNPLTDTVPIHSWIHPWLPLMQARLEPLYSPIRSKLSSALQKWHPSDSSAKLILQPWKDVFTPGSWEAFMVKNIVPKLGMCLGELVINPHQQHMDAFYWVIDWEGMISVSSLVGLLEKHFFPKWLQVLCSWLSNSPNYEEITKWYLGWKSMFSDQVLAHPSVKDKFNEALDIMNRAVSSNVGAYMQPGARENIAYLTHTERRKDFQYEAMQERREAENMAQRGIGVAASSVPMNFKDLIETKAEEHNIVFMPVIGKRHEGKQLYTFGRIVIYIDRGVVFVQGEKTWVPTSLQSLIDMAK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.21027479091995221,"dataset":["RNA-binding proteins"],"disorder_content":0.41816009557945044,"disprot_consensus":{"full":[{"start":1,"end":350,"type":"T"}],"Structural state":[{"start":1,"end":350,"type":"D"}],"Structural transition":[{"start":1,"end":350,"type":"T"}],"Biological process":[{"start":1,"end":350,"type":"F"}]}},{"disprot_id":"DP04301","acc":"Q75PQ8","creator":"ldobson","date":"2024-11-21T08:01:49.576Z","features":{"pfam":[{"id":"PF04084","name":"Origin recognition complex subunit 2 RecA-like domain","start":285,"end":445},{"id":"PF24882","name":"ORC2 WHD","start":504,"end":561}],"gene3D":[]},"genes":[{"name":{"value":"Orc2"},"synonyms":[{"value":"Orc2l"}]}],"length":576,"name":"Origin recognition complex subunit 2","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions":[{"start":1,"end":10,"reference_id":"37551430","reference_source":"pmid","reference_html":"A dual role for the chromatin reader ORCA/LRWD1 in targeting the origin recognition complex to chromatin. <i> Sahu S, Ekundayo BE, Kumar A, Bleichert F. </i> EMBO J, 2023","date":"2024-11-21T08:09:27.542Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"8SIU"}],"region_id":"DP04301r001","statement":[{"text":"We anticipate that these interactions flexibly tether ORCA to ORC since the N‐terminal Orc2 region is predicted to be disordered and not visible in prior ORC structures (Jaremko et al, 2020; Schmidt & Bleichert, 2020).","type":"Results"},{"text":"This region is not visible in the structure.","type":"Curator statement"}],"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A140UHX1"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1117"}],"sequence_construct":"SNAMSTLRLKEAKVPSVQFVGDDDVLSHILDREGGTKLKKEKVQLLVNPQKVIKKAECELEKSDLEVLEDQNYVEVLGRNIQESLGNGSAVDGRNKVYSFQHR","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-21T16:51:34.935Z"}},{"start":29,"end":100,"reference_id":"37551430","reference_source":"pmid","reference_html":"A dual role for the chromatin reader ORCA/LRWD1 in targeting the origin recognition complex to chromatin. <i> Sahu S, Ekundayo BE, Kumar A, Bleichert F. </i> EMBO J, 2023","date":"2024-11-21T08:17:15.320Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"8SIU"}],"region_id":"DP04301r002","statement":[{"text":"We anticipate that these interactions flexibly tether ORCA to ORC since the N‐terminal Orc2 region is predicted to be disordered and not visible in prior ORC structures (Jaremko et al, 2020; Schmidt & Bleichert, 2020).","type":"Results"},{"text":"This region is not visible in the structure.","type":"Curator statement"}],"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A140UHX1"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1117"}],"sequence_construct":"SNAMSTLRLKEAKVPSVQFVGDDDVLSHILDREGGTKLKKEKVQLLVNPQKVIKKAECELEKSDLEVLEDQNYVEVLGRNIQESLGNGSAVDGRNKVYSFQHR","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-21T16:51:34.587Z"}}],"regions_counter":2,"released":"2025_06","sequence":"MSTLRLKEAKVPSVQFVGDDDVLSHILDREGGTKLKKEKVQLLVNPQKVIKKAECELEKSDLEVLEDQNYVEVLGRNIQESLGNGSAVDGRNKVYSFQHRKHPEEMTKLALELAKTSGKIDPLASNDPKITKNIARKSKGHSSEKAPLENNNKNEFPSIQPHNVRKRLIASRSHCDSESEYSASSSEDDEEVAKDDEEDTNVVRCSKKSQGQNRLLPAPVSKEILPKKRKRDKAGDLVEEYFEAHSSSKVLTSDRTLQKLRRARVDQKTLRNLLSKFVPSFSTEIGQLNQQHERLFDKWILQLRLGFNIVLYGLGSKRDLLEKFRTTMLQDSIHVVINGFFPGISVKSILNSITEDVLSHMGTFQSVLDQRDWIMNRFKEDSSLELFLLIHNLDSQMLRGDNSQQILGQLSSLRNVYLIASIDHLNAPLMWDHAKQSLYNWLWYETTTYSPYTEETSYENSLLVKQSGSLPLSSLIHVLRSLTPNARGIFRLLMKYQLDNQDCPSYIGLSFQDFYQQCREAFLVNSDLTLRAQLTEFRDHKLIRTKKGTDGVEYLLIPVDSGTLADFLEKEEEEES","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"alphafold_very_low_content":0.359375,"disorder_content":0.1423611111111111,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"},{"start":29,"end":100,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":29,"end":100,"type":"D"}]}},{"disprot_id":"DP04302","acc":"P06897","creator":"ldobson","date":"2024-11-21T08:31:01.404Z","features":{"pfam":[{"id":"PF00125","name":"Core histone H2A/H2B/H3/H4 domain","start":7,"end":89},{"id":"PF16211","name":"C-terminus of histone H2A","start":92,"end":125}],"gene3D":[]},"genes":[],"length":130,"name":"Histone H2A type 1","ncbi_taxon_id":8355,"organism":"Xenopus laevis","regions":[{"start":1,"end":11,"reference_id":"37551430","reference_source":"pmid","reference_html":"A dual role for the chromatin reader ORCA/LRWD1 in targeting the origin recognition complex to chromatin. <i> Sahu S, Ekundayo BE, Kumar A, Bleichert F. </i> EMBO J, 2023","date":"2026-05-13T15:20:28.695Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly100Arg","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"8SIY"}],"region_id":"DP04302r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A140UHX1"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62799"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02281"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q75PQ8"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84233"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null}],"sequence_construct":"SGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKKTESAKSAKSK","statement":[{"text":"This region is not visible in the structure.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-13T15:20:31.710Z"}},{"start":120,"end":130,"reference_id":"37551430","reference_source":"pmid","reference_html":"A dual role for the chromatin reader ORCA/LRWD1 in targeting the origin recognition complex to chromatin. <i> Sahu S, Ekundayo BE, Kumar A, Bleichert F. </i> EMBO J, 2023","date":"2024-11-21T08:34:24.186Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly100Arg","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"8SIY"}],"region_id":"DP04302r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A140UHX1"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62799"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02281"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q75PQ8"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84233"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null}],"sequence_construct":"SGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKKTESAKSAKSK","statement":[{"text":"This region is not visible in the structure.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-21T16:23:25.038Z"}},{"start":1,"end":11,"reference_id":"37551430","reference_source":"pmid","reference_html":"A dual role for the chromatin reader ORCA/LRWD1 in targeting the origin recognition complex to chromatin. <i> Sahu S, Ekundayo BE, Kumar A, Bleichert F. </i> EMBO J, 2023","date":"2026-05-13T15:32:36.446Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly100Arg","start":null,"end":null,"position":null}],"region_id":"DP04302r003","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting Widom 601 dsDNA with sequence: ATCCTGGAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGACAGCTCTAGCACCGCTTAAACGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGGATTACTCCCTAGTCTCCAGGCACGTGTCAGATATATACATCCTGTGAT"}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A140UHX1"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62799"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02281"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q75PQ8"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84233"}],"statement":[{"text":"The PDB-deposited data indicate that this region lacks electron density. As it appears to be part of the analyzed sample, the absence of electron density is likely due to its disordered nature, consistent with predicted data.","type":"Curator statement"}]},{"start":120,"end":130,"reference_id":"37551430","reference_source":"pmid","reference_html":"A dual role for the chromatin reader ORCA/LRWD1 in targeting the origin recognition complex to chromatin. <i> Sahu S, Ekundayo BE, Kumar A, Bleichert F. </i> EMBO J, 2023","date":"2026-05-13T15:32:44.106Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly100Arg","start":null,"end":null,"position":null}],"region_id":"DP04302r004","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting Widom 601 dsDNA with sequence: ATCCTGGAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGACAGCTCTAGCACCGCTTAAACGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGGATTACTCCCTAGTCTCCAGGCACGTGTCAGATATATACATCCTGTGAT"}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A140UHX1"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62799"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02281"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q75PQ8"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84233"}],"statement":[{"text":"The PDB-deposited data indicate that this region lacks electron density. As it appears to be part of the analyzed sample, the absence of electron density is likely due to its disordered nature, consistent with predicted data.","type":"Curator statement"}]}],"regions_counter":4,"released":"2025_06","sequence":"MSGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGGVTIAQGGVLPNIQSVLLPKKTESAKSAKSK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Amphibia","Batrachia","Anura","Pipoidea","Pipidae","Xenopodinae","Xenopus","Xenopus"],"alphafold_very_low_content":0.007692307692307693,"disorder_content":0.16923076923076924,"disprot_consensus":{"full":[{"start":1,"end":11,"type":"D"},{"start":120,"end":130,"type":"D"}],"Structural state":[{"start":1,"end":11,"type":"D"},{"start":120,"end":130,"type":"D"}],"Disorder function":[{"start":1,"end":11,"type":"F"},{"start":120,"end":130,"type":"F"}]}},{"disprot_id":"DP04303","acc":"P02281","creator":"ldobson","date":"2024-11-21T08:38:06.763Z","features":{"pfam":[{"id":"PF00125","name":"Core histone H2A/H2B/H3/H4 domain","start":20,"end":101}],"gene3D":[]},"genes":[],"length":126,"name":"Histone H2B 1.1","ncbi_taxon_id":8355,"organism":"Xenopus laevis","regions":[{"start":1,"end":32,"reference_id":"37551430","reference_source":"pmid","reference_html":"A dual role for the chromatin reader ORCA/LRWD1 in targeting the origin recognition complex to chromatin. <i> Sahu S, Ekundayo BE, Kumar A, Bleichert F. </i> EMBO J, 2023","date":"2026-05-13T15:17:53.117Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser33Thr","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"8SIY"}],"region_id":"DP04303r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A140UHX1"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62799"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06897"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q75PQ8"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84233"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null}],"sequence_construct":"AKSAPAPKKGSKKAVTKTQKKDGKKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK","statement":[{"text":"This region is not visible in the structure.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-13T15:17:55.202Z"}},{"start":1,"end":32,"reference_id":"37551430","reference_source":"pmid","reference_html":"A dual role for the chromatin reader ORCA/LRWD1 in targeting the origin recognition complex to chromatin. <i> Sahu S, Ekundayo BE, Kumar A, Bleichert F. </i> EMBO J, 2023","date":"2026-05-13T15:30:09.894Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser33Thr","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"8SIY"}],"region_id":"DP04303r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0A140UHX1"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62799"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P06897"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q75PQ8"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P84233"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting Widom 601 dsDNA with sequence: ATCCTGGAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGACAGCTCTAGCACCGCTTAAACGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGGATTACTCCCTAGTCTCCAGGCACGTGTCAGATATATACATCCTGTGAT"}]}],"statement":[{"text":"The PDB-deposited data indicate that this region lacks electron density. As it appears to be part of the analyzed sample, the absence of electron density is likely due to its disordered nature, consistent with predicted data.","type":"Curator statement"}]}],"regions_counter":2,"released":"2026_06","sequence":"MPEPAKSAPAPKKGSKKAVTKTQKKDGKKRRKSRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Amphibia","Batrachia","Anura","Pipoidea","Pipidae","Xenopodinae","Xenopus","Xenopus"],"alphafold_very_low_content":0,"disorder_content":0.25396825396825395,"disprot_consensus":{"full":[{"start":1,"end":32,"type":"D"}],"Structural state":[{"start":1,"end":32,"type":"D"}],"Disorder function":[{"start":1,"end":32,"type":"F"}]}},{"disprot_id":"DP04304","acc":"Q8I0V0","creator":"ldobson","date":"2024-11-21T09:58:22.089Z","features":{"pfam":[{"id":"PF00082","name":"Subtilase family","start":366,"end":639},{"id":"PF18213","name":"SUB1 protease Prodomain ProdP9","start":138,"end":217}],"gene3D":[]},"genes":[{"name":{"value":"SUB1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"18083098","url":"http://www.ncbi.nlm.nih.gov/pubmed/18083098","alternativeUrl":"https://europepmc.org/abstract/MED/18083098"}}]},"orfNames":[{"value":"PF3D7_0507500","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"CAD51440.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAD51440.1"}}]}]}],"length":688,"name":"Subtilisin-like protease 1","ncbi_taxon_id":36329,"organism":"Plasmodium falciparum (isolate 3D7)","regions":[{"start":218,"end":222,"reference_id":"38386597","reference_source":"pmid","reference_html":"Prodomain-driven enzyme dimerization: a pH-dependent autoinhibition mechanism that controls <i>Plasmodium</i> Sub1 activity before merozoite egress. <i> Martinez M, Bouillon A, Brûlé S, Raynal B, Haouz A, Alzari PM, Barale J-C. </i> mBio, 2024","date":"2025-03-21T17:31:14.844Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0097264","term_name":"self proteolysis","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"8POL"}],"ec_go":"EXP","region_id":"DP04304r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"Another common feature is that the PD had undergone autocleavage at its primary maturation site (Asp 217 in PfS1FL and Asp202 in PvS1FL) but remained tightly associated to the catalytic core in the crystal, partially occupying the active site.","type":"Results"}],"term_comment":"","term_def":"\"The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their own peptide bonds.\" [GOC:yaf, PMID:18676612, PMID:19144634]","term_is_obsolete":false,"term_not_annotate":false},{"start":218,"end":329,"reference_id":"38386597","reference_source":"pmid","reference_html":"Prodomain-driven enzyme dimerization: a pH-dependent autoinhibition mechanism that controls <i>Plasmodium</i> Sub1 activity before merozoite egress. <i> Martinez M, Bouillon A, Brûlé S, Raynal B, Haouz A, Alzari PM, Barale J-C. </i> mBio, 2024","date":"2025-03-21T17:35:05.179Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"8POL"}],"region_id":"DP04304r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":"calcium(2+)"}],"statement":[{"text":"Another common feature is that the PD had undergone autocleavage at its primary maturation site (Asp 217 in PfS1FL and Asp202 in PvS1FL) but remained tightly associated to the catalytic core in the crystal, partially occupying the active site.","type":"Results"},{"text":"The PD connecting segment between the two subunits (residues 116–153) and the N-terminal region of the mature catalytic domain (residues 236–347) are not visible in the electron density and are presumably disordered in the crystals.","type":"Figure"},{"text":"After the auto autocleavage at its Asp 217, this region becomes the flexible N-terminal tail of the mature catalytic domain.","type":"Curator statement"}]}],"regions_counter":6,"released":"2025_06","sequence":"MMLNKKVVALCTLTLHLFCIFLCLGKEVRSEENGKIQDDAKKIVSELRFLEKVEDVIEKSNIGGNEVDADENSFNPDTEVPIEEIEEIKMRELKDVKEEKNKNDNHNNNNNNISSSSSSSSNTFGEEKEEVSKKKKKLRLIVSENHATTPSFFQESLLEPDVLSFLESKGNLSNLKNINSMIIELKEDTTDDELISYIKILEEKGALIESDKLVSADNIDISGIKDAIRRGEENIDVNDYKSMLEVENDAEDYDKMFGMFNESHAATSKRKRHSTNERGYDTFSSPSYKTYSKSDYLYDDDNNNNNYYYSHSSNGHNSSSRNSSSSRSRPGKYHFNDEFRNLQWGLDLSRLDETQELINEHQVMSTRICVIDSGIDYNHPDLKDNIELNLKELHGRKGFDDDNNGIVDDIYGANFVNNSGNPMDDNYHGTHVSGIISAIGNNNIGVVGVDVNSKLIICKALDEHKLGRLGDMFKCLDYCISRNAHMINGSFSFDEYSGIFNSSVEYLQRKGILFFVSASNCSHPKSSTPDIRKCDLSINAKYPPILSTVYDNVISVANLKKNDNNNHYSLSINSFYSNKYCQLAAPGTNIYSTAPHNSYRKLNGTSMAAPHVAAIASLIFSINPDLSYKKVIQILKDSIVYLPSLKNMVAWAGYADINKAVNLAIKSKKTYINSNISNKWKKKSRYLH","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"alphafold_very_low_content":0.20784883720930233,"disorder_content":0,"disprot_consensus":{"full":[{"start":218,"end":329,"type":"F"}],"Structural state":[],"Biological process":[{"start":218,"end":222,"type":"F"}],"Disorder function":[{"start":218,"end":329,"type":"F"}]}},{"disprot_id":"DP04305","acc":"E6Y8B9","creator":"ldobson","date":"2024-11-21T10:03:37.505Z","features":{"pfam":[{"id":"PF00082","name":"Subtilase family","start":310,"end":592},{"id":"PF18213","name":"SUB1 protease Prodomain ProdP9","start":123,"end":202}],"gene3D":[]},"genes":[{"name":{"value":"sub1","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"ACT76164.1","url":"https://www.ebi.ac.uk/ena/browser/view/ACT76164.1"}}]},"orfNames":[{"value":"PVC01_100035100","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"SCO73277.1","url":"https://www.ebi.ac.uk/ena/browser/view/SCO73277.1"}}]},{"value":"PVT01_100029100","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"SCO67822.1","url":"https://www.ebi.ac.uk/ena/browser/view/SCO67822.1"}}]},{"value":"PVW1_100050600","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAG9475055.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAG9475055.1"}}]}]}],"length":630,"name":"subtilisin","ncbi_taxon_id":5855,"organism":"Plasmodium vivax","regions":[{"start":203,"end":276,"reference_id":"25204226","reference_source":"pmid","reference_html":"A novel Plasmodium-specific prodomain fold regulates the malaria drug target SUB1 subtilase. <i> Giganti D, Bouillon A, Tawk L, Robert F, Martinez M, Crublet E, Weber P, Girard-Blanc C, Petres S, Haouz A, Hernandez JF, Mercereau-Puijalon O, Alzari PM, Barale JC. </i> Nat Commun, 2014","date":"2024-11-21T10:07:40.915Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"},{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"PDB","id":"4TR2"}],"region_id":"DP04305r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1061"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"271  "}],"sequence_construct":"MLLVNQSHQGFNKEHTSKMVSAIVLYVLLAAAAHSAFAADPGDILPNEGKKEKDDVHKIISELRFLQKVETILESSNMSVSDVEADANAYNPDRDAPKEELQKLQDQQETPSKQPNNLRNSPQKRAEKKESPGKNKKSLRLIVSENHATSPSFFEESLLQEDVVSFIQSKGKLSNLKNLKSMIIDLNSDMTDEELAEYISLLERKGALIESDKLVGADDVSLASVKDAVRRGESSVNWGKLRSTMLEVPSGESPPSHAASSGSPFDDDDDLLSEAALHREEAHLAGSKTTKGYKFNDEYRNLQWGLDLARLDETQDLINANRVSVTKICVIDSGIDYNHPDLRNNIDVNVKELHGRKGVDDDSNGVVDDVYGANFVNNSGDPMDDNYHGTHVSGIISAVGNNGIGIVGVDGHSKLVICKALDQHKLGRLGDMFKCIDYCISRQAHMINGSFSFDEYSNIFNASVEHLRSLGILFFVSASNCAHDKLSKPDIAKCDLAVNHRYPPILSKTHNNVIAVANLKRDLDESYSLSVNSFYSNIYCQLAAPGTNIYSTTPMNNYRKLNGTSMASPHVAAIASIVRSINPNLTYLQIVEILRNAIVKLPSLTERVSWGGYVDILRAVNLAIDSKAAPYIKSHSWFRWKQGSRRHHHHHHSSRIPERPLQI","statement":[{"text":"The long connecting segment between these two structural domains (residues 203–276) is not visible in the electron density, as this region is disordered in the crystal. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-13T15:55:04.087Z"}},{"start":91,"end":117,"reference_id":"25204226","reference_source":"pmid","reference_html":"A novel Plasmodium-specific prodomain fold regulates the malaria drug target SUB1 subtilase. <i> Giganti D, Bouillon A, Tawk L, Robert F, Martinez M, Crublet E, Weber P, Girard-Blanc C, Petres S, Haouz A, Hernandez JF, Mercereau-Puijalon O, Alzari PM, Barale JC. </i> Nat Commun, 2014","date":"2024-11-21T10:08:23.731Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"},{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"PDB","id":"4TR2"}],"region_id":"DP04305r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1061"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"271  "}],"sequence_construct":"MLLVNQSHQGFNKEHTSKMVSAIVLYVLLAAAAHSAFAADPGDILPNEGKKEKDDVHKIISELRFLQKVETILESSNMSVSDVEADANAYNPDRDAPKEELQKLQDQQETPSKQPNNLRNSPQKRAEKKESPGKNKKSLRLIVSENHATSPSFFEESLLQEDVVSFIQSKGKLSNLKNLKSMIIDLNSDMTDEELAEYISLLERKGALIESDKLVGADDVSLASVKDAVRRGESSVNWGKLRSTMLEVPSGESPPSHAASSGSPFDDDDDLLSEAALHREEAHLAGSKTTKGYKFNDEYRNLQWGLDLARLDETQDLINANRVSVTKICVIDSGIDYNHPDLRNNIDVNVKELHGRKGVDDDSNGVVDDVYGANFVNNSGDPMDDNYHGTHVSGIISAVGNNGIGIVGVDGHSKLVICKALDQHKLGRLGDMFKCIDYCISRQAHMINGSFSFDEYSNIFNASVEHLRSLGILFFVSASNCAHDKLSKPDIAKCDLAVNHRYPPILSKTHNNVIAVANLKRDLDESYSLSVNSFYSNIYCQLAAPGTNIYSTTPMNNYRKLNGTSMASPHVAAIASIVRSINPNLTYLQIVEILRNAIVKLPSLTERVSWGGYVDILRAVNLAIDSKAAPYIKSHSWFRWKQGSRRHHHHHHSSRIPERPLQI","statement":[{"text":"Two views of PvSUB1 in cartoon representation showing the C-terminal subtilisin-like catalytic domain (cyan) coupled to its N-terminal pro-region that comprises the belt domain (shown in yellow) connected through a disordered linker (indicated by a thick dashed yellow–orange line) to a ‘classical’ bacterial-like prodomain (orange).","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-13T15:55:50.312Z"}},{"start":26,"end":37,"reference_id":"25204226","reference_source":"pmid","reference_html":"A novel Plasmodium-specific prodomain fold regulates the malaria drug target SUB1 subtilase. <i> Giganti D, Bouillon A, Tawk L, Robert F, Martinez M, Crublet E, Weber P, Girard-Blanc C, Petres S, Haouz A, Hernandez JF, Mercereau-Puijalon O, Alzari PM, Barale JC. </i> Nat Commun, 2014","date":"2024-11-21T10:09:04.183Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"},{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"PDB","id":"4TR2"}],"region_id":"DP04305r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1061"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"271  "}],"sequence_construct":"MLLVNQSHQGFNKEHTSKMVSAIVLYVLLAAAAHSAFAADPGDILPNEGKKEKDDVHKIISELRFLQKVETILESSNMSVSDVEADANAYNPDRDAPKEELQKLQDQQETPSKQPNNLRNSPQKRAEKKESPGKNKKSLRLIVSENHATSPSFFEESLLQEDVVSFIQSKGKLSNLKNLKSMIIDLNSDMTDEELAEYISLLERKGALIESDKLVGADDVSLASVKDAVRRGESSVNWGKLRSTMLEVPSGESPPSHAASSGSPFDDDDDLLSEAALHREEAHLAGSKTTKGYKFNDEYRNLQWGLDLARLDETQDLINANRVSVTKICVIDSGIDYNHPDLRNNIDVNVKELHGRKGVDDDSNGVVDDVYGANFVNNSGDPMDDNYHGTHVSGIISAVGNNGIGIVGVDGHSKLVICKALDQHKLGRLGDMFKCIDYCISRQAHMINGSFSFDEYSNIFNASVEHLRSLGILFFVSASNCAHDKLSKPDIAKCDLAVNHRYPPILSKTHNNVIAVANLKRDLDESYSLSVNSFYSNIYCQLAAPGTNIYSTTPMNNYRKLNGTSMASPHVAAIASIVRSINPNLTYLQIVEILRNAIVKLPSLTERVSWGGYVDILRAVNLAIDSKAAPYIKSHSWFRWKQGSRRHHHHHHSSRIPERPLQI","statement":[{"text":"Secondary structures (α-helices and β-sheets) and missing or disordered regions (open blue squares) in PvSUB1 crystal structure are indicated above the sequences.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-13T15:56:02.763Z"}},{"start":615,"end":630,"reference_id":"25204226","reference_source":"pmid","reference_html":"A novel Plasmodium-specific prodomain fold regulates the malaria drug target SUB1 subtilase. <i> Giganti D, Bouillon A, Tawk L, Robert F, Martinez M, Crublet E, Weber P, Girard-Blanc C, Petres S, Haouz A, Hernandez JF, Mercereau-Puijalon O, Alzari PM, Barale JC. </i> Nat Commun, 2014","date":"2026-05-13T15:57:15.431Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"},{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"PDB","id":"4TR2"}],"region_id":"DP04305r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1061"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"271  "}],"sequence_construct":"MLLVNQSHQGFNKEHTSKMVSAIVLYVLLAAAAHSAFAADPGDILPNEGKKEKDDVHKIISELRFLQKVETILESSNMSVSDVEADANAYNPDRDAPKEELQKLQDQQETPSKQPNNLRNSPQKRAEKKESPGKNKKSLRLIVSENHATSPSFFEESLLQEDVVSFIQSKGKLSNLKNLKSMIIDLNSDMTDEELAEYISLLERKGALIESDKLVGADDVSLASVKDAVRRGESSVNWGKLRSTMLEVPSGESPPSHAASSGSPFDDDDDLLSEAALHREEAHLAGSKTTKGYKFNDEYRNLQWGLDLARLDETQDLINANRVSVTKICVIDSGIDYNHPDLRNNIDVNVKELHGRKGVDDDSNGVVDDVYGANFVNNSGDPMDDNYHGTHVSGIISAVGNNGIGIVGVDGHSKLVICKALDQHKLGRLGDMFKCIDYCISRQAHMINGSFSFDEYSNIFNASVEHLRSLGILFFVSASNCAHDKLSKPDIAKCDLAVNHRYPPILSKTHNNVIAVANLKRDLDESYSLSVNSFYSNIYCQLAAPGTNIYSTTPMNNYRKLNGTSMASPHVAAIASIVRSINPNLTYLQIVEILRNAIVKLPSLTERVSWGGYVDILRAVNLAIDSKAAPYIKSHSWFRWKQGSRRHHHHHHSSRIPERPLQI","statement":[{"text":"Secondary structures (α-helices and β-sheets) and missing or disordered regions (open blue squares) in PvSUB1 crystal structure are indicated above the sequences.","type":"Figure"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-13T15:57:22.469Z"}},{"start":91,"end":117,"reference_id":"25204226","reference_source":"pmid","reference_html":"A novel Plasmodium-specific prodomain fold regulates the malaria drug target SUB1 subtilase. <i> Giganti D, Bouillon A, Tawk L, Robert F, Martinez M, Crublet E, Weber P, Girard-Blanc C, Petres S, Haouz A, Hernandez JF, Mercereau-Puijalon O, Alzari PM, Barale JC. </i> Nat Commun, 2014","date":"2024-11-21T10:11:48.197Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"},{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"PDB","id":"4TR2"}],"region_id":"DP04305r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1061"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"271  "}],"sequence_construct":"MLLVNQSHQGFNKEHTSKMVSAIVLYVLLAAAAHSAFAADPGDILPNEGKKEKDDVHKIISELRFLQKVETILESSNMSVSDVEADANAYNPDRDAPKEELQKLQDQQETPSKQPNNLRNSPQKRAEKKESPGKNKKSLRLIVSENHATSPSFFEESLLQEDVVSFIQSKGKLSNLKNLKSMIIDLNSDMTDEELAEYISLLERKGALIESDKLVGADDVSLASVKDAVRRGESSVNWGKLRSTMLEVPSGESPPSHAASSGSPFDDDDDLLSEAALHREEAHLAGSKTTKGYKFNDEYRNLQWGLDLARLDETQDLINANRVSVTKICVIDSGIDYNHPDLRNNIDVNVKELHGRKGVDDDSNGVVDDVYGANFVNNSGDPMDDNYHGTHVSGIISAVGNNGIGIVGVDGHSKLVICKALDQHKLGRLGDMFKCIDYCISRQAHMINGSFSFDEYSNIFNASVEHLRSLGILFFVSASNCAHDKLSKPDIAKCDLAVNHRYPPILSKTHNNVIAVANLKRDLDESYSLSVNSFYSNIYCQLAAPGTNIYSTTPMNNYRKLNGTSMASPHVAAIASIVRSINPNLTYLQIVEILRNAIVKLPSLTERVSWGGYVDILRAVNLAIDSKAAPYIKSHSWFRWKQGSRRHHHHHHSSRIPERPLQI","statement":[{"text":"Two views of PvSUB1 in cartoon representation showing the C-terminal subtilisin-like catalytic domain (cyan) coupled to its N-terminal pro-region that comprises the belt domain (shown in yellow) connected through a disordered linker (indicated by a thick dashed yellow–orange line) to a ‘classical’ bacterial-like prodomain (orange).","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-13T15:55:48.661Z"}}],"regions_counter":5,"released":"2026_06","sequence":"MVLTRRAALLLCPWVIQLVIKRTLAGDILPNEGKKEKDDVHKIISELRFLQKVETILESSNMSVSDVEADANAYNPDRDAPKEELQKLQDQQETPSKQPNNLRNSPQKRAEKKESPGKNKKSLRLIVSENHATSPSFFEESLLQEDVVSFIQSKGKLSNLKNLKSMIIDLNSDMTDEELAEYISLLERKGALIESDKLVGADDVSLASVKDAVRRGESSVNWGKLRSTMLEVPSGESPPSHAASSGSPFDDDDDLLSEAALHREEAHLAGSKTTKGYKFNDEYRNLQWGLDLARLDETQDLINANRVSVTKICVIDSGIDYNHPDLRNNIDVNVKELHGRKGVDDDSNGVVDDVYGANFVNNSGDPMDDNYHGTHVSGIISAVGNNGIGIVGVDGHSKLVICKALDQHKLGRLGDMFKCIDYCISRQAHMINGSFSFDEYSNIFNASVEHLRSLGILFFVSASNCAHDKLSKPDIAKCDLAVNHRYPPILSKTHNNVIAVANLKRDLDESYSLSVNSFYSNIYCQLAAPGTNIYSTTPMNNYRKLNGTSMASPHVAAIASIVRSINPNLTYLQIVEILRNAIVKLPSLTERVSWGGYVDILRAVNLAIDSKAAPYIKSHSWFRWKQGSRR","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Plasmodium)"],"alphafold_very_low_content":0.20952380952380953,"disorder_content":0.20476190476190476,"disprot_consensus":{"full":[{"start":26,"end":37,"type":"D"},{"start":91,"end":117,"type":"D"},{"start":203,"end":276,"type":"D"},{"start":615,"end":630,"type":"D"}],"Structural state":[{"start":26,"end":37,"type":"D"},{"start":91,"end":117,"type":"D"},{"start":203,"end":276,"type":"D"},{"start":615,"end":630,"type":"D"}],"Disorder function":[{"start":91,"end":117,"type":"F"}]}},{"disprot_id":"DP04306","acc":"Q8I384","creator":"ldobson","date":"2024-11-21T10:12:44.616Z","features":{"pfam":[{"id":"PF00491","name":"Arginase family","start":168,"end":377}],"gene3D":[]},"genes":[{"name":{"value":"ARG","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"19456858","url":"http://www.ncbi.nlm.nih.gov/pubmed/19456858","alternativeUrl":"https://europepmc.org/abstract/MED/19456858"}}]},"orfNames":[{"value":"PF3D7_0906500","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"CAD51750.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAD51750.1"}}]}]}],"length":411,"name":"Arginase","ncbi_taxon_id":36329,"organism":"Plasmodium falciparum (isolate 3D7)","regions":[{"start":72,"end":153,"reference_id":"20527960","reference_source":"pmid","reference_html":"Crystal structure of arginase from Plasmodium falciparum and implications for L-arginine depletion in malarial infection . <i> Dowling DP, Ilies M, Olszewski KL, Portugal S, Mota MM, Llinás M, Christianson DW. </i> Biochemistry, 2010","date":"2024-11-21T10:14:48.942Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"cross_refs":[{"db":"PDB","id":"3MMR"}],"region_id":"DP04306r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"9793992  "},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1567  "},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"23930  "}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSHMASKNVSIIGSPLAAGQPLGGVQLACDDLRKLGLHNVIDVLGWKYEDIGNIDNGDNEMKQEKKTNNYINNNDNNNDNNNDNNNDNNNNCYIPNGVIKEKKHDLSNNKMNGYVNHNFYGNYEENNVISTNDKYKNNCYYDNIRNIKEIGIFSKNLFDTMSNELRKKNFVLNIGGDHGVAFSSILSSLQMYQNLRVIWIDAHGDINIPETSPSGNYHGMTLAHTLGLFKKKVPYFEWSENLTYLKPENTAIIGIRDIDAYEKIILKKCNINYYTIFDIEKNGIYNTICTALEKIDPNSNCPIHISLDIDSVDNVFAPGTGTVAKGGLNYREINLLMKILAETKRVVSMDLVEYNPSLDEVDKKVHGDSLPILDNATKTGKLCLELIARVLGYDIV","statement":[{"text":"While the 11-residue insert in loop L8 is well ordered, the 74 residue LCR insert in loop L2 is largely disordered: only the flanking residues D70-N71 and C154-N158 are modeled into visible electron density, and C154 is refined with half occupancy. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-25T22:03:24.637Z"}}],"regions_counter":1,"released":"2025_06","sequence":"MLDTIESYIKSHKEKENLYVKKNVSIIGSPLAAGQPLGGVQLACDDLRKLGLHNVIDVLGWKYEDIGNIDNGDNEMKQEKKTNNYINNNDNNNDNNNDNNNDNNNNCYIPNGVIKEKKHDLSNNKMNGYVNHNFYGNYEENNVISTNDKYKNNCYYDNIRNIKEIGIFSKNLFDTMSNELRKKNFVLNIGGDHGVAFSSILSSLQMYQNLRVIWIDAHGDINIPETSPSGNYHGMTLAHTLGLFKKKVPYFEWSENLTYLKPENTAIIGIRDIDAYEKIILKKCNINYYTIFDIEKNGIYNTICTALEKIDPNSNCPIHISLDIDSVDNVFAPGTGTVAKGGLNYREINLLMKILAETKRVVSMDLVEYNPSLDEVDKKVHGDSLPILDNATKTGKLCLELIARVLGYDIV","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"alphafold_very_low_content":0.170316301703163,"disorder_content":0.19951338199513383,"disprot_consensus":{"full":[{"start":72,"end":153,"type":"D"}],"Structural state":[{"start":72,"end":153,"type":"D"}]}},{"disprot_id":"DP04307","acc":"Q86T24","creator":"ldobson","date":"2024-11-21T10:16:15.879Z","features":{"pfam":[{"id":"PF00651","name":"BTB/POZ domain","start":22,"end":114}],"gene3D":[]},"genes":[{"name":{"value":"ZBTB33"},"synonyms":[{"value":"KAISO"},{"value":"ZNF348"}]}],"length":672,"name":"Transcriptional regulator Kaiso","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":575,"end":604,"reference_id":"22949637","reference_source":"pmid","reference_html":"Molecular basis for recognition of methylated and specific DNA sequences by the zinc finger protein Kaiso. <i> Buck-Koehntop BA, Stanfield RL, Ekiert DC, Martinez-Yamout MA, Dyson HJ, Wilson IA, Wright PE. </i> Proc Natl Acad Sci U S A, 2012","date":"2024-11-21T10:18:50.281Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04307r001","statement":[{"text":"NMR experiments indicate that\nthe C-terminal region, residues 575–604, is intrinsically disordered\nin the free protein and undergoes a conformational change to a more ordered state upon binding to DNA.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-13T19:59:56.665Z"}},{"start":575,"end":600,"reference_id":"22949637","reference_source":"pmid","reference_html":"Molecular basis for recognition of methylated and specific DNA sequences by the zinc finger protein Kaiso. <i> Buck-Koehntop BA, Stanfield RL, Ekiert DC, Martinez-Yamout MA, Dyson HJ, Wilson IA, Wright PE. </i> Proc Natl Acad Sci U S A, 2012","date":"2026-05-13T20:14:34.551Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"cross_refs":[{"db":"BMRB","id":"18462"},{"db":"PDB","id":"2LT7"}],"region_id":"DP04307r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"32051"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence: GTGCTTCCTGCCAATAACG."}]}],"sequence_construct":"ANKRMKVKHDDHYELIVDGRVYYICIVCKRSYVCLTSLRRHFNIHSWEKKYPCRYCEKVFPLAEYRTKHEIHHTGERRYQ CLACGKSFINYQFMSSHIKSVHSQDPSGDSKLYRLHPCRSLQIRQYAYLSDRS","statement":[{"text":"NMR experiments indicate that the C-terminal region, residues 575–604, is intrinsically disordered in the free protein and undergoes a conformational change to a more ordered state upon binding to DNA. The cross peaks of many of these residues lie in the random coil region of the 1H-15N heteronuclear single-quantum coherence (HSQC) spectrum of free Kaiso but undergo large shifts in the spectrum of the KBS complex, indicating formation of folded structure in the presence of DNA (Fig. 2A).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-13T20:23:58.563Z"}},{"start":575,"end":600,"reference_id":"22949637","reference_source":"pmid","reference_html":"Molecular basis for recognition of methylated and specific DNA sequences by the zinc finger protein Kaiso. <i> Buck-Koehntop BA, Stanfield RL, Ekiert DC, Martinez-Yamout MA, Dyson HJ, Wilson IA, Wright PE. </i> Proc Natl Acad Sci U S A, 2012","date":"2026-05-13T20:14:43.431Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"region_id":"DP04307r003","statement":[{"text":"NMR experiments indicate that the C-terminal region, residues 575–604, is intrinsically disordered in the free protein and undergoes a conformational change to a more ordered state upon binding to DNA. The cross peaks of many of these residues lie in the random coil region of the 1H-15N heteronuclear single-quantum coherence (HSQC) spectrum of free Kaiso but undergo large shifts in the spectrum of the KBS complex, indicating formation of folded structure in the presence of DNA (Fig. 2A).","type":"Results"}],"cross_refs":[{"db":"BMRB","id":"18462"},{"db":"PDB","id":"2LT7"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"32051"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence: GTGCTTCCTGCCAATAACG"}]}],"states_connection":[{"source":"DP04307r001","target":"DP04307r002"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-13T20:23:59.864Z"}},{"start":472,"end":481,"reference_id":"22949637","reference_source":"pmid","reference_html":"Molecular basis for recognition of methylated and specific DNA sequences by the zinc finger protein Kaiso. <i> Buck-Koehntop BA, Stanfield RL, Ekiert DC, Martinez-Yamout MA, Dyson HJ, Wilson IA, Wright PE. </i> Proc Natl Acad Sci U S A, 2012","date":"2026-05-13T20:19:36.798Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"4F6M"}],"region_id":"DP04307r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"32051","statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence: GTGCTTCCTGCCAATAACG."}]}],"statement":[{"text":"There is no electron density for residues preceding the N-terminal β-strand of ZF1 in either crystal structure. The conformation of this region also is disordered in the NMR structural ensemble, but weak intermolecular NOEs from the Arg-475 and Lys-477 side chains indicate transient interactions with the DNA backbone across the minor groove (Fig. 1D).","type":"Results"},{"text":"The PDB-deposited data indicate that this region lacks electron density. As it appears to be part of the analyzed sample, the absence of electron density is likely due to its disordered nature, consistent with predicted data.","type":"Curator statement"}]}],"regions_counter":4,"released":"2026_06","sequence":"MESRKLISATDIQYSGSLLNSLNEQRGHGLFCDVTVIVEDRKFRAHKNILSASSTYFHQLFSVAGQVVELSFIRAEIFAEILNYIYSSKIVRVRSDLLDELIKSGQLLGVKFIAELGVPLSQVKSISGTAQDGNTEPLPPDSGDKNLVIQKSKDEAQDNGATIMPIITESFSLSAEDYEMKKIIVTDSDDDDDDVIFCSEILPTKETLPSNNTVAQVQSNPGPVAISDVAPSASNNSPPLTNITPTQKLPTPVNQATLSQTQGSEKLLVSSAPTHLTPNIILLNQTPLSTPPNVSSSLPNHMPSSINLLVQNQQTPNSAILTGNKANEEEEEEIIDDDDDTISSSPDSAVSNTSLVPQADTSQNTSFDGSLIQKMQIPTLLQEPLSNSLKISDIITRNTNDPGVGSKHLMEGQKIITLDTATEIEGLSTGCKVYANIGEDTYDIVIPVKDDPDEGEARLENEIPKTSGSEMANKRMKVKHDDHYELIVDGRVYYICIVCKRSYVCLTSLRRHFNIHSWEKKYPCRYCEKVFPLAEYRTKHEIHHTGERRYQCLACGKSFINYQFMSSHIKSVHSQDPSGDSKLYRLHPCRSLQIRQYAYLSDRSSTIPAMKDDGIGYKVDTGKEPPVGTTTSTQNKPMTWEDIFIQQENDSIFKQNVTDGSTEFEFIIPESY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.6294642857142857,"disorder_content":0.05952380952380952,"disprot_consensus":{"full":[{"start":472,"end":481,"type":"D"},{"start":575,"end":600,"type":"T"},{"start":601,"end":604,"type":"D"}],"Structural state":[{"start":472,"end":481,"type":"D"},{"start":575,"end":604,"type":"D"}],"Structural transition":[{"start":575,"end":600,"type":"T"}]}},{"disprot_id":"DP04308","acc":"P43586","creator":"ldobson","date":"2024-11-21T10:25:05.198Z","features":{"pfam":[{"id":"PF28225","name":"LOC1 helical domain","start":107,"end":165}],"gene3D":[]},"genes":[{"name":{"value":"LOC1"},"olnNames":[{"value":"YFR001W"}]}],"length":204,"name":"60S ribosomal subunit assembly/export protein LOC1","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":204,"reference_id":"39558160","reference_source":"pmid","reference_html":"Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation. <i> Niedner-Boblenz A, Monecke T, Hennig J, Klostermann M, Hofweber M, Davydova E, Gerber AP, Anosova I, Mayer W, Müller M, Heym RG, Janowski R, Paillart JC, Dormann D, Zarnack K, Sattler M, Niessing D. </i> Nucleic Acids Res, 2024","date":"2024-11-21T10:26:51.727Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04308r002","statement":[{"text":"The spectrum showed poor signal dispersion, confirming that Loc1p is largely unstructured in the absence of a binding partner.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-23T14:51:24.414Z"}},{"start":1,"end":14,"reference_id":"39558160","reference_source":"pmid","reference_html":"Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation. <i> Niedner-Boblenz A, Monecke T, Hennig J, Klostermann M, Hofweber M, Davydova E, Gerber AP, Anosova I, Mayer W, Müller M, Heym RG, Janowski R, Paillart JC, Dormann D, Zarnack K, Sattler M, Niessing D. </i> Nucleic Acids Res, 2024","date":"2024-11-21T10:28:21.214Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006090","ec_ontology":"ECO","ec_name":"protein-oligonucleotide microarray binding evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","region_id":"DP04308r003","statement":[{"text":"We identified eight short, positively charged, unfolded nucleic acid binding (PUN) motifs in Loc1p, which cooperatively act as potent RNA annealers.","type":"Introduction"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-23T16:33:09.725Z"}},{"start":39,"end":47,"reference_id":"39558160","reference_source":"pmid","reference_html":"Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation. <i> Niedner-Boblenz A, Monecke T, Hennig J, Klostermann M, Hofweber M, Davydova E, Gerber AP, Anosova I, Mayer W, Müller M, Heym RG, Janowski R, Paillart JC, Dormann D, Zarnack K, Sattler M, Niessing D. </i> Nucleic Acids Res, 2024","date":"2024-11-21T10:28:41.908Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006090","ec_ontology":"ECO","ec_name":"protein-oligonucleotide microarray binding evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","region_id":"DP04308r004","statement":[{"text":"We identified eight short, positively charged, unfolded nucleic acid binding (PUN) motifs in Loc1p, which cooperatively act as potent RNA annealers.","type":"Introduction"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-23T16:33:04.281Z"}},{"start":63,"end":69,"reference_id":"39558160","reference_source":"pmid","reference_html":"Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation. <i> Niedner-Boblenz A, Monecke T, Hennig J, Klostermann M, Hofweber M, Davydova E, Gerber AP, Anosova I, Mayer W, Müller M, Heym RG, Janowski R, Paillart JC, Dormann D, Zarnack K, Sattler M, Niessing D. </i> Nucleic Acids Res, 2024","date":"2024-11-21T10:28:53.094Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006090","ec_ontology":"ECO","ec_name":"protein-oligonucleotide microarray binding evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","region_id":"DP04308r005","statement":[{"text":"We identified eight short, positively charged, unfolded nucleic acid binding (PUN) motifs in Loc1p, which cooperatively act as potent RNA annealers.","type":"Introduction"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-23T16:33:04.587Z"}},{"start":89,"end":95,"reference_id":"39558160","reference_source":"pmid","reference_html":"Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation. <i> Niedner-Boblenz A, Monecke T, Hennig J, Klostermann M, Hofweber M, Davydova E, Gerber AP, Anosova I, Mayer W, Müller M, Heym RG, Janowski R, Paillart JC, Dormann D, Zarnack K, Sattler M, Niessing D. </i> Nucleic Acids Res, 2024","date":"2024-11-21T10:29:10.356Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006090","ec_ontology":"ECO","ec_name":"protein-oligonucleotide microarray binding evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","region_id":"DP04308r006","statement":[{"text":"We identified eight short, positively charged, unfolded nucleic acid binding (PUN) motifs in Loc1p, which cooperatively act as potent RNA annealers.","type":"Introduction"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-23T16:33:11.827Z"}},{"start":137,"end":147,"reference_id":"39558160","reference_source":"pmid","reference_html":"Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation. <i> Niedner-Boblenz A, Monecke T, Hennig J, Klostermann M, Hofweber M, Davydova E, Gerber AP, Anosova I, Mayer W, Müller M, Heym RG, Janowski R, Paillart JC, Dormann D, Zarnack K, Sattler M, Niessing D. </i> Nucleic Acids Res, 2024","date":"2024-11-21T10:30:05.652Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006090","ec_ontology":"ECO","ec_name":"protein-oligonucleotide microarray binding evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","region_id":"DP04308r007","statement":[{"text":"We identified eight short, positively charged, unfolded nucleic acid binding (PUN) motifs in Loc1p, which cooperatively act as potent RNA annealers.","type":"Introduction"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-23T16:33:17.750Z"}},{"start":154,"end":165,"reference_id":"39558160","reference_source":"pmid","reference_html":"Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation. <i> Niedner-Boblenz A, Monecke T, Hennig J, Klostermann M, Hofweber M, Davydova E, Gerber AP, Anosova I, Mayer W, Müller M, Heym RG, Janowski R, Paillart JC, Dormann D, Zarnack K, Sattler M, Niessing D. </i> Nucleic Acids Res, 2024","date":"2024-11-21T10:31:13.109Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006090","ec_ontology":"ECO","ec_name":"protein-oligonucleotide microarray binding evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","region_id":"DP04308r008","statement":[{"text":"We identified eight short, positively charged, unfolded nucleic acid binding (PUN) motifs in Loc1p, which cooperatively act as potent RNA annealers.","type":"Introduction"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-23T16:33:21.993Z"}},{"start":170,"end":178,"reference_id":"39558160","reference_source":"pmid","reference_html":"Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation. <i> Niedner-Boblenz A, Monecke T, Hennig J, Klostermann M, Hofweber M, Davydova E, Gerber AP, Anosova I, Mayer W, Müller M, Heym RG, Janowski R, Paillart JC, Dormann D, Zarnack K, Sattler M, Niessing D. </i> Nucleic Acids Res, 2024","date":"2024-11-21T10:31:33.521Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006090","ec_ontology":"ECO","ec_name":"protein-oligonucleotide microarray binding evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","region_id":"DP04308r009","statement":[{"text":"We identified eight short, positively charged, unfolded nucleic acid binding (PUN) motifs in Loc1p, which cooperatively act as potent RNA annealers.","type":"Introduction"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-23T16:33:26.190Z"}},{"start":191,"end":199,"reference_id":"39558160","reference_source":"pmid","reference_html":"Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation. <i> Niedner-Boblenz A, Monecke T, Hennig J, Klostermann M, Hofweber M, Davydova E, Gerber AP, Anosova I, Mayer W, Müller M, Heym RG, Janowski R, Paillart JC, Dormann D, Zarnack K, Sattler M, Niessing D. </i> Nucleic Acids Res, 2024","date":"2024-11-21T10:31:44.365Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"GO:0003723","term_name":"RNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006090","ec_ontology":"ECO","ec_name":"protein-oligonucleotide microarray binding evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","region_id":"DP04308r010","statement":[{"text":"We identified eight short, positively charged, unfolded nucleic acid binding (PUN) motifs in Loc1p, which cooperatively act as potent RNA annealers.","type":"Introduction"}],"term_comment":"","term_def":"\"Binding to an RNA molecule or a portion thereof.\" [GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-23T16:33:31.330Z"}},{"start":1,"end":204,"reference_id":"39558160","reference_source":"pmid","reference_html":"Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation. <i> Niedner-Boblenz A, Monecke T, Hennig J, Klostermann M, Hofweber M, Davydova E, Gerber AP, Anosova I, Mayer W, Müller M, Heym RG, Janowski R, Paillart JC, Dormann D, Zarnack K, Sattler M, Niessing D. </i> Nucleic Acids Res, 2024","date":"2025-06-23T16:28:48.855Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019843","term_name":"rRNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0677","term_name":"tandem tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IPI","region_id":"DP04308r011","statement":[{"text":"In order to assess the cellular binding targets of Loc1p, we immunoprecipitated TAP-tagged Loc1p expressed in yeast under the endogenous promoter and identified the co-purified RNAs by cDNA microarrays. Among the co-purified RNAs, the class of rRNAs was highly enriched (Supplementary Figure S1A and Supplementary Tables S2 and S3), suggesting that this nucleolar RNA-binding protein preferentially binds to rRNAs.","type":"Results"},{"text":"The interaction with both pro- and eukaryotic ribosomes suggests unspecific binding to rRNA or ribosomal proteins and a rather general mode of ribosome association.","type":"Results"},{"text":"Furthermore, Loc1p stabilizes the energetically most favored conformation of E3 in a time-course experiment with molecular beacons and antisense RNA strands (Supplementary Figure S6B).","type":"Results"},{"text":"Loc1p forms condensates with a 28nt E3 localization element (LE) of ASH1 mRNA and promotes conformational changes in its stem-loop.","type":"Supplementary material"}],"term_comment":"","term_def":"\"Binding to a ribosomal RNA.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"ChEBI","id":"18111","operator":"and","partner_start":null,"partner_end":null}]},{"start":1,"end":204,"reference_id":"39558160","reference_source":"pmid","reference_html":"Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation. <i> Niedner-Boblenz A, Monecke T, Hennig J, Klostermann M, Hofweber M, Davydova E, Gerber AP, Anosova I, Mayer W, Müller M, Heym RG, Janowski R, Paillart JC, Dormann D, Zarnack K, Sattler M, Niessing D. </i> Nucleic Acids Res, 2024","date":"2025-06-23T15:47:32.768Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140691","term_name":"RNA folding chaperone","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","region_id":"DP04308r012","statement":[{"text":"To assess this possibility, we performed in vitro RNA chaperone experiments with a 27-base stem–loop labeled at its 5′-end with a fluorescent dye and at its 3′-end with a quencher molecule (22,57). ","type":"Results"},{"text":"In contrast, in the presence of Loc1p we observed an ∼7-fold increased reaction rate toward the formation of the energetically favored dsRNA (Figure ​2C, right panel). Thus, similarly to a catalytic reaction, Loc1p accelerates the transition of folded RNAs toward their thermodynamically most favored state.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an RNA or an RNA-containing complex to assist the folding process.\" [PMID:31165735]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":204,"reference_id":"39558160","reference_source":"pmid","reference_html":"Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation. <i> Niedner-Boblenz A, Monecke T, Hennig J, Klostermann M, Hofweber M, Davydova E, Gerber AP, Anosova I, Mayer W, Müller M, Heym RG, Janowski R, Paillart JC, Dormann D, Zarnack K, Sattler M, Niessing D. </i> Nucleic Acids Res, 2024","date":"2025-06-23T15:53:43.636Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0033592","term_name":"RNA strand annealing activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001254","ec_ontology":"ECO","ec_name":"radioisotope assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","region_id":"DP04308r013","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Radioactively labeled TAR plus strand (TAR+) and unlabeled minus strand (TAR−) DNA were incubated with the different proteins at 37°C and the formation of double strands was assessed by native PAGE."}]}],"statement":[{"text":"In this assay, Loc1p showed by far the strongest annealing activity of all tested chaperones (Figure ​2D).","type":"Results"},{"text":"Thus, under these experimental conditions, Loc1p was the most potent nucleic acid annealing catalyst among the tested chaperones.","type":"Results"},{"text":"Loc1p (1–20)10 showed again a >50-fold improvement in activity over Loc1p (1–20)2 (Figure ​4G and H). These findings suggest that the RNA-binding motifs in Loc1p act cooperatively in nucleic acid annealing. Interestingly, wild-type Loc1p and Loc1p (1–20)10 showed comparable activities in this assay (Figure ​4G), suggesting that the concatenation of PUN motifs is sufficient to achieve wild-type annealing activity.","type":"Results"}],"term_comment":"","term_def":"\"An activity that facilitates the formation of a complementary double-stranded RNA molecule.\" [GOC:mah, PMID:7543843]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":204,"reference_id":"39558160","reference_source":"pmid","reference_html":"Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation. <i> Niedner-Boblenz A, Monecke T, Hennig J, Klostermann M, Hofweber M, Davydova E, Gerber AP, Anosova I, Mayer W, Müller M, Heym RG, Janowski R, Paillart JC, Dormann D, Zarnack K, Sattler M, Niessing D. </i> Nucleic Acids Res, 2024","date":"2025-06-23T16:27:18.928Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","region_id":"DP04308r014","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Total HeLa cell RNA "}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":"","statements":[{"type":"Curator statement","text":"Loc1p also forms condensates with a 28nt E3 localization element (LE) of ASH1\nmRNA."}]}],"statement":[{"text":"We first mixed increasing amounts of recombinant Loc1p with 0.5× mass ratio of total HeLa cell RNA and observed formation of microscopically visible condensates at Loc1p concentrations of 5 μM or higher (Figure ​(Figure5A).5A). The number and size of the condensates were clearly dependent on the Loc1p concentration, while 30 μM Loc1p without RNA did not result in phase separation.","type":"Results"},{"text":"Notably, formation of liquid-liquid phase separations (LLPS) with an in vitro transcribed 28-nt-long E3 (21) is observed for Loc1p concentrations >5 μM but not in the absence of RNA (Supplementary Figure S6A).","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":204,"reference_id":"39558160","reference_source":"pmid","reference_html":"Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation. <i> Niedner-Boblenz A, Monecke T, Hennig J, Klostermann M, Hofweber M, Davydova E, Gerber AP, Anosova I, Mayer W, Müller M, Heym RG, Janowski R, Paillart JC, Dormann D, Zarnack K, Sattler M, Niessing D. </i> Nucleic Acids Res, 2024","date":"2025-06-23T15:58:18.650Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006067","ec_ontology":"ECO","ec_name":"fluorescence recovery after photobleaching evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0857","term_name":"fluorescent dye label","term_namespace":"Labels and dyes","start":7,"end":null,"position":"Specific residue","statements":[{"type":"Results","text":"To directly demonstrate the presence of Loc1p in these condensates, we introduced a single cysteine (Loc1pS7C) and labeled the protein using Cy5-maleimide (Cy5-Loc1pS7C)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser7Cys","start":null,"end":null,"position":null}],"ec_go":"IDA","region_id":"DP04308r015","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Total HeLa cell RNA "}]}],"statement":[{"text":"Fluorescence of Cy5-Loc1pS7C/RNA condensates recovered after photobleaching on average to 20–30% after 30 s (Figure ​(Figure5E5E and Supplementary Movie S2), demonstrating a dynamic exchange of Loc1p between the droplets and the surrounding protein solution. Both the droplet fusion and the fluorescence recovery to around 20–30% are in line with the assumption that the observed condensates have liquid-like to gel-like properties.","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":20,"reference_id":"39558160","reference_source":"pmid","reference_html":"Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation. <i> Niedner-Boblenz A, Monecke T, Hennig J, Klostermann M, Hofweber M, Davydova E, Gerber AP, Anosova I, Mayer W, Müller M, Heym RG, Janowski R, Paillart JC, Dormann D, Zarnack K, Sattler M, Niessing D. </i> Nucleic Acids Res, 2024","date":"2025-06-23T16:20:47.680Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001232","ec_ontology":"ECO","ec_name":"microscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","interaction_partner":[{"db":"ChEBI","id":"33697","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04308r016","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Total HeLa cell RNA "}]}],"statement":[{"text":"Indeed, Loc1p (1–20)10 formed visible condensates already at a concentration of 2.5 μM protein and a mass ratio of 0.025× RNA (Figure ​5F). We further confirmed the robustness of the apparent PUN motif-mediated phase separation by providing a constant concentration of Loc1p (1–20)10 and increasing ratios of RNA (Figure ​5G). In all cases, RNA-dependent phase separation was observed.","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":16,"released":"2025_06","sequence":"MAPKKPSKRQNLRREVAPEVFQDSQARNQLANVPHLTEKSAQRKPSKTKVKKEQSLARLYGAKKDKKGKYSEKDLNIPTLNRAIVPGVKIRRGKKGKKFIADNDTLTLNRLITTIGDKYDDIAESKLEKARRLEEIRELKRKEIERKEALKQDKLEEKKDEIKKKSSVARTIRRKNKRDMLKSEAKASESKTEGRKVKKVSFAQ","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.004901960784313725,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":204,"type":"D"}],"Structural state":[{"start":1,"end":204,"type":"D"}],"Molecular function":[{"start":1,"end":204,"type":"F"}]}},{"disprot_id":"DP04309","acc":"Q9UJY1","creator":"tcordero","date":"2024-11-21T10:32:05.402Z","features":{"pfam":[{"id":"PF00011","name":"Hsp20/alpha crystallin family","start":95,"end":173}],"gene3D":[]},"genes":[{"name":{"value":"HSPB8"},"synonyms":[{"value":"CRYAC"},{"value":"E2IG1"},{"value":"HSP22"}],"orfNames":[{"value":"PP1629"}]}],"length":196,"name":"Heat shock protein beta-8","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":89,"reference_id":"19783089","reference_source":"pmid","reference_html":"Thermally induced structural changes of intrinsically disordered small heat shock protein Hsp22. <i> Kazakov AS, Markov DI, Gusev NB, Levitsky DI. </i> Biophys Chem, 2009","date":"2024-12-05T14:40:46.126Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2024_12","version":1,"region_id":"DP04309r003","statement":[{"text":"According to “double wavelength” plot, [θ]222 vs [θ]200, proposed by Uversky [13], the CD spectrum of Hsp22 roughly, but not entirely, corresponds to that of a protein in the pre-molten-globule-like state. These CD data indicate that the structure of Hsp22 is more ordered than that typical for proteins in the pre-molten-globule-like state.","type":"Results"},{"text":"The data of FTIR indicate that at 20 °C Hsp22 contains about 33% of β-sheets, about 12% of α-helices, about 34% of turns, and about 21% disordered random-coil structures. This estimation correlates well with the corresponding data obtained earlier by CD spectroscopy [9]. According to predictions, almost all β-strands of Hsp22 are located in the α-crystallin domain, while α-helices are mainly localized in the N-terminal part of the molecule [10].","type":"Results"},{"text":"These DSC data unambiguously indicate that at low temperature a significant portion of the Hsp22 molecule lacks rigid tertiary structure and therefore possesses properties of intrinsically disordered proteins. ","type":"Results"},{"text":"This conclusion agrees with the prediction of disordered regions in Hsp22 [10] indicating that three Trp residues are located in presumably unordered regions and only Trp96 is located in a more or less ordered region (residues 90–120 of α-crystallin domain).","type":"Results"},{"text":"According to the predictions of a structural disorder, it was assumed that Hsp22 belongs to the growing family of intrinsically disordered proteins (IDP), although some parts of its molecule are more or less ordered (residues 90–120 and 140–170 in the α-crystallin domain) [10].","type":"Introduction"},{"text":"The combination of experimental evidences and prediction approaches let us determine this region as intrinsically disordered.","type":"Curator statement"}]},{"start":171,"end":196,"reference_id":"19783089","reference_source":"pmid","reference_html":"Thermally induced structural changes of intrinsically disordered small heat shock protein Hsp22. <i> Kazakov AS, Markov DI, Gusev NB, Levitsky DI. </i> Biophys Chem, 2009","date":"2024-12-05T14:33:56.584Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2024_12","version":1,"region_id":"DP04309r004","statement":[{"text":"According to “double wavelength” plot, [θ]222 vs [θ]200, proposed by Uversky [13], the CD spectrum of Hsp22 roughly, but not entirely, corresponds to that of a protein in the pre-molten-globule-like state. These CD data indicate that the structure of Hsp22 is more ordered than that typical for proteins in the pre-molten-globule-like state.","type":"Results"},{"text":"This conclusion agrees with the prediction of disordered regions in Hsp22 [10] indicating that three Trp residues are located in presumably unordered regions and only Trp96 is located in a more or less ordered region (residues 90–120 of α-crystallin domain).","type":"Results"},{"text":"These DSC data unambiguously indicate that at low temperature a significant portion of the Hsp22 molecule lacks rigid tertiary structure and therefore possesses properties of intrinsically disordered proteins.","type":"Results"},{"text":"The data of FTIR indicate that at 20 °C Hsp22 contains about 33% of β-sheets, about 12% of α-helices, about 34% of turns, and about 21% disordered random-coil structures. This estimation correlates well with the corresponding data obtained earlier by CD spectroscopy [9]. According to predictions, almost all β-strands of Hsp22 are located in the α-crystallin domain, while α-helices are mainly localized in the N-terminal part of the molecule [10].","type":"Results"},{"text":"According to the predictions of a structural disorder, it was assumed that Hsp22 belongs to the growing family of intrinsically disordered proteins (IDP), although some parts of its molecule are more or less ordered (residues 90–120 and 140–170 in the α-crystallin domain) [10].","type":"Introduction"},{"text":"The combination of experimental evidences and prediction approaches let us determine this region as intrinsically disordered.","type":"Curator statement"}]}],"regions_counter":4,"released":"2024_12","sequence":"MADGQMPFSCHYPSRLRRDPFRDSPLSSRLLDDGFGMDPFPDDLTASWPDWALPRLSSAWPGTLRSGMVPRGPTATARFGVPAEGRTPPPFPGEPWKVCVNVHSFKPEELMVKTKDGYVEVSGKHEEKQQEGGIVSKNFTKKIQLPAEVDPVTVFASLSPEGLLIIEAPQVPPYSTFGESSFNNELPQDSQEVTCT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.24489795918367346,"dataset":["Autophagy-related proteins","Age-related disorders proteins","Stress response proteins"],"disorder_content":0.5867346938775511,"disprot_consensus":{"full":[{"start":1,"end":89,"type":"D"},{"start":171,"end":196,"type":"D"}],"Structural state":[{"start":1,"end":89,"type":"D"},{"start":171,"end":196,"type":"D"}]}},{"disprot_id":"DP04310","acc":"A0AVK6","creator":"ldobson","date":"2024-11-21T10:33:20.556Z","features":{"pfam":[{"id":"PF02319","name":"E2F/DP family winged-helix DNA-binding domain","start":114,"end":182},{"id":"PF02319","name":"E2F/DP family winged-helix DNA-binding domain","start":262,"end":347}],"gene3D":[]},"genes":[{"name":{"value":"E2F8"}}],"length":867,"name":"Transcription factor E2F8","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":213,"end":258,"reference_id":"26632596","reference_source":"pmid","reference_html":"Structural insights into the DNA-binding specificity of E2F family transcription factors. <i> Morgunova E, Yin Y, Jolma A, Dave K, Schmierer B, Popov A, Eremina N, Nilsson L, Taipale J. </i> Nat Commun, 2015","date":"2026-05-14T20:02:45.853Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"4YO2"}],"region_id":"DP04310r001","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence: TTTTCCCGCCAAAAA"}]}],"statement":[{"text":"The 23 amino acids of the linker close to DBD1 are folded into two α-helices, whereas the remaining 53 amino acids connected to DBD2 are disordered. \n","type":"Figure"},{"text":"Numbering is not according to the structure.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-14T20:04:10.776Z"}},{"start":213,"end":258,"reference_id":"26632596","reference_source":"pmid","reference_html":"Structural insights into the DNA-binding specificity of E2F family transcription factors. <i> Morgunova E, Yin Y, Jolma A, Dave K, Schmierer B, Popov A, Eremina N, Nilsson L, Taipale J. </i> Nat Commun, 2015","date":"2026-05-14T20:04:06.823Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04310r002","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence: TTTTCCCGCCAAAAA."}]}],"statement":[{"text":"The 23 amino acids of the linker close to DBD1 are folded into two α-helices, whereas the remaining 53 amino acids connected to DBD2 are disordered.  ","type":"Figure"},{"text":"Numbering is not according to the structure.","type":"Curator statement"}]}],"regions_counter":2,"released":"2026_06","sequence":"MENEKENLFCEPHKRGLMKTPLKESTTANIVLAEIQPDFGPLTTPTKPKEGSQGEPWTPTANLKMLISAVSPEIRNRDQKRGLFDNRSGLPEAKDCIHEHLSGDEFEKSQPSRKEKSLGLLCHKFLARYPNYPNPAVNNDICLDEVAEELNVERRRIYDIVNVLESLHMVSRLAKNRYTWHGRHNLNKTLGTLKSIGEENKYAEQIMMIKKKEYEQEFDFIKSYSIEDHIIKSNTGPNGHPDMCFVELPGVEFRAASVNSRKDKSLRVMSQKFVMLFLVSTPQIVSLEVAAKILIGEDHVEDLDKSKFKTKIRRLYDIANVLSSLDLIKKVHVTEERGRKPAFKWTGPEISPNTSGSSPVIHFTPSDLEVRRSSKENCAKNLFSTRGKPNFTRHPSLIKLVKSIESDRRKINSAPSSPIKTNKAESSQNSAPFPSKMAQLAAICKMQLEEQSSESRQKVKVQLARSGPCKPVAPLDPPVNAEMELTAPSLIQPLGMVPLIPSPLSSAVPLILPQAPSGPSYAIYLQPTQAHQSVTPPQGLSPTVCTTHSSKATGSKDSTDATTEKAANDTSKASASTRPGSLLPAPERQGAKSRTREPAGERGSKRASMLEDSGSKKKFKEDLKGLENVSATLFPSGYLIPLTQCSSLGAESILSGKENSSALSPNHRIYSSPIAGVIPVTSSELTAVNFPSFHVTPLKLMVSPTSVAAVPVGNSPALASSHPVPIQNPSSAIVNFTLQHLGLISPNVQLSASPGSGIVPVSPRIESVNVAPENAGTQQGRATNYDSPVPGQSQPNGQSVAVTGAQQPVPVTPKGSQLVAESFFRTPGGPTKPTSSSCMDFEGANKTSLGTLFVPQRKLEVSTEDVH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.6505190311418685,"disorder_content":0.0530565167243368,"disprot_consensus":{"full":[{"start":213,"end":258,"type":"D"}],"Structural state":[{"start":213,"end":258,"type":"D"}],"Disorder function":[{"start":213,"end":258,"type":"F"}]}},{"disprot_id":"DP04311","acc":"P84101","creator":"ldobson","date":"2024-11-21T10:35:49.749Z","features":{"pfam":[{"id":"PF04419","name":"Small EDRK-rich factor 1/2-like, N-terminal","start":1,"end":37}],"gene3D":[]},"genes":[{"name":{"value":"SERF2"},"synonyms":[{"value":"FAM2C"}]}],"length":59,"name":"Small EDRK-rich factor 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":59,"reference_id":"38466543","reference_source":"pmid","reference_html":"Backbone 1H, 13C, and 15N chemical shift assignments for human SERF2. <i> Sahoo BR, Subramanian V, Bardwell JCA. </i> Biomol NMR Assign, 2024","date":"2024-11-21T10:37:16.385Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04311r001","statement":[{"text":"At a physiological pH of 7.4 and temperature of 37°C, human SERF2 is highly disordered as indicated by its CD spectra as it shows a prominent minimum at ~ 205 nm.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-14T20:45:58.540Z"}},{"start":1,"end":59,"reference_id":"38466543","reference_source":"pmid","reference_html":"Backbone 1H, 13C, and 15N chemical shift assignments for human SERF2. <i> Sahoo BR, Subramanian V, Bardwell JCA. </i> Biomol NMR Assign, 2024","date":"2026-05-14T20:46:38.897Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":5.5},{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":null,"value":277.1}],"cross_refs":[{"db":"BMRB","id":"52141"}],"region_id":"DP04311r002","sequence_construct":"MTRGNQRELARQKNMKKQSDSVKGKRRDDGLSAAARKQRDSEIMQQKQKKANEKKEEPK\n","statement":[{"text":"The predicted secondary structure from NMR chemical shifts agrees with circular dichroism (CD) spectroscopy experiments that indicate that SERF2 has a disordered structure with ~ 30% helicity at 5°C that becomes more disordered at 37°C. ","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-14T20:46:43.752Z"}}],"regions_counter":2,"released":"2026_06","sequence":"MTRGNQRELARQKNMKKQSDSVKGKRRDDGLSAAARKQRDSEIMQQKQKKANEKKEEPK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":59,"type":"D"}],"Structural state":[{"start":1,"end":59,"type":"D"}]}},{"disprot_id":"DP04312","acc":"R4IT35","creator":"ldobson","date":"2024-11-21T10:40:40.042Z","features":{"pfam":[{"id":"PF00078","name":"Reverse transcriptase (RNA-dependent DNA polymerase)","start":569,"end":665},{"id":"PF12009","name":"Telomerase ribonucleoprotein complex - RNA binding domain","start":239,"end":367}],"gene3D":[]},"genes":[{"orfNames":[{"value":"OGATHE_002606","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"KAH3669794.1","url":"https://www.ebi.ac.uk/ena/browser/view/KAH3669794.1"}}]}]}],"length":782,"name":"Telomerase reverse transcriptase","ncbi_taxon_id":460523,"organism":"Ogataea polymorpha","regions":[{"start":137,"end":153,"reference_id":"26721464","reference_source":"pmid","reference_html":"NMR assignments of the N-terminal domain of Ogataea polymorpha telomerase reverse transcriptase. <i> Polshakov VI, Petrova OA, Parfenova YY, Efimov SV, Klochkov VV, Zvereva MI, Dontsova OA. </i> Biomol NMR Assign, 2016","date":"2026-06-09T15:22:19.947Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"BMRB","id":"25770"}],"region_id":"DP04312r001","sequence_construct":"MRFDQYVDENKSSDDFEPLIHDLFETRWHGTGREIWIERVKDRKIPSTLVKPNYSHEELIDMLIGYLADNRYENALINGLVTGDDLEIANSYGFKGRNAVTNLLKSPEFRLVHTIIGTETFLDLLINYSARMGNVYLWGELNESNYKTQCKSSENLYFQ","statement":[{"text":"The TALOS predictions of order parameters and measured 15N–1H NOEs revealed that several protein residues are located in disordered regions such as loop 77–84 and C-tail 137–159.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-09T15:23:00.889Z"}},{"start":84,"end":96,"reference_id":"29294091","reference_source":"pmid","reference_html":"Structure and function of the N-terminal domain of the yeast telomerase reverse transcriptase. <i> Petrova OA, Mantsyzov AB, Rodina EV, Efimov SV, Hackenberg C, Hakanpää J, Klochkov VV, Lebedev AA, Chugunova AA, Malyavko AN, Zatsepin TS, Mishin AV, Zvereva MI, Lamzin VS, Dontsova OA, Polshakov VI. </i> Nucleic Acids Res, 2018","date":"2026-06-09T15:17:49.596Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"5NPT"}],"region_id":"DP04312r002","statement":[{"text":"Overall the electron density maps were of somewhat lower quality than typically expected for 2.4 Å resolution structures, with several blobs and continuous non-interpretable patches of density, possibly owing to disordered regions including short polypeptides produced during crystallization under proteolytic conditions.","type":"Methods"},{"text":"Most of the unassigned residues belong to the fragments Asn70–Leu76 and Lys95–Ala99 and are clustered in the central part of the protein; residues Lys95 and Gly96 are also disordered in the crystal structure.","type":"Results"}]},{"start":144,"end":159,"reference_id":"29294091","reference_source":"pmid","reference_html":"Structure and function of the N-terminal domain of the yeast telomerase reverse transcriptase. <i> Petrova OA, Mantsyzov AB, Rodina EV, Efimov SV, Hackenberg C, Hakanpää J, Klochkov VV, Lebedev AA, Chugunova AA, Malyavko AN, Zatsepin TS, Mishin AV, Zvereva MI, Lamzin VS, Dontsova OA, Polshakov VI. </i> Nucleic Acids Res, 2018","date":"2026-06-09T15:18:18.445Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"5NPT"}],"region_id":"DP04312r003","statement":[{"text":"Overall the electron density maps were of somewhat lower quality than typically expected for 2.4 Å resolution structures, with several blobs and continuous non-interpretable patches of density, possibly owing to disordered regions including short polypeptides produced during crystallization under proteolytic conditions.","type":"Methods"},{"text":"The C-terminal residues 143–159 are missing in the crystal structure and are also disordered in the NMR model. ","type":"Results"}]},{"start":139,"end":156,"reference_id":"29294091","reference_source":"pmid","reference_html":"Structure and function of the N-terminal domain of the yeast telomerase reverse transcriptase. <i> Petrova OA, Mantsyzov AB, Rodina EV, Efimov SV, Hackenberg C, Hakanpää J, Klochkov VV, Lebedev AA, Chugunova AA, Malyavko AN, Zatsepin TS, Mishin AV, Zvereva MI, Lamzin VS, Dontsova OA, Polshakov VI. </i> Nucleic Acids Res, 2018","date":"2026-06-09T15:19:46.727Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"5LGF"}],"region_id":"DP04312r004","statement":[{"text":"The obtained ensemble of 20 NMR conformers of hpTEN (Figure 2B, Table 3) exhibits a well-structured αβ-core (residues 1–70, 100–138), a flexible central loop (residues 71–99) and an unstructured C-terminus (residues 139–159).","type":"Results"}]},{"start":71,"end":99,"reference_id":"29294091","reference_source":"pmid","reference_html":"Structure and function of the N-terminal domain of the yeast telomerase reverse transcriptase. <i> Petrova OA, Mantsyzov AB, Rodina EV, Efimov SV, Hackenberg C, Hakanpää J, Klochkov VV, Lebedev AA, Chugunova AA, Malyavko AN, Zatsepin TS, Mishin AV, Zvereva MI, Lamzin VS, Dontsova OA, Polshakov VI. </i> Nucleic Acids Res, 2018","date":"2026-06-09T15:21:34.654Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"5LGF"}],"region_id":"DP04312r005","statement":[{"text":"The obtained ensemble of 20 NMR conformers of hpTEN (Figure 2B, Table 3) exhibits a well-structured αβ-core (residues 1–70, 100–138), a flexible central loop (residues 71–99) and an unstructured C-terminus (residues 139–159).","type":"Results"},{"text":"The fast motions of the central loop, including the residues from helix α6, are also large in amplitude. The residues from the central flexible loop 71–99 that are close to the junction regions between the loop and the protein core, exhibit motions at the slower ms timescale. Interestingly, most of the unassigned residues belong to these regions. We attribute the motion of these regions to conformational exchange occurring at the ms timescale.","type":"Results"}]}],"regions_counter":5,"released":"2026_06","sequence":"MRFDQYVDENKSSDDFEPLIHDLFETRWHGTGREIWIERVKDRKIPSTLVKPNYSHEELIDMLIGYLADNRYENALINGLVTGDDLEIANSYGFKGRNAVTNLLKSPEFRLVHTIIGTETFLDLLINYSARMGNVYLWGELNESNYKTQCKSSQLSIKNMLYSEIWSLPRLNPLPESASLIYDVFKTEHGRHPKLEFLLESMRIYHMNHQPDYPYILDSICPEPTNIKSNFDLAVGKESVIKFVTIVLEKIMPKELFGSPHNKSVLFKKIAEVLNSHKKDSIYVCNVAKNFKITDVGWLVPERKMNKHEFLKAQNTWTQFIGWFFNSLLFKLVASFFHVTDVSQSFELLYYRHDTWRRISKHFKDKYYGRFLERRPQNLNSYYTYARNDDFIGSQKLLPKAHDLRFITMPFKGSRKNIFEYMDRHKNEVKIANLVLSHKRRKNCIDSVSDLPYELLKYKNQITGPVYALKFDIRQAYDTLPRTMILPLISELLKETPETFEFHIERYFVLSAPTATGKRQRRKLSVLQGHESVLSDKVLSHANTPSVLKKSEIMKIVEQQLEHAALLSSSETFHRKKGVFQGFPLSGIFCEIVYDKLTEYLLSLGGDNVKIIRLADDFLILSTQMDIIAKYQNLIEKRIPQFNLTVNKQKSTVSEETVDFLGTTINLKTLSVTKNLDSYDLTPVRVSSFKALYSTLLIHLKQALASDFFNADINDEDTLKQNIEILIQSLSMRFKKSKKSVARNDKMEITRFEQFLLLTEKLILTKVGTSYLTSIRSLLKAF","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Pichiaceae","Ogataea"],"alphafold_very_low_content":0.054987212276214836,"disorder_content":0.06649616368286446,"disprot_consensus":{"full":[{"start":71,"end":99,"type":"D"},{"start":137,"end":159,"type":"D"}],"Structural state":[{"start":71,"end":99,"type":"D"},{"start":137,"end":159,"type":"D"}]}},{"disprot_id":"DP04313","acc":"P41746","creator":"ldobson","date":"2024-11-21T10:46:17.240Z","features":{"pfam":[{"id":"PF01185","name":"Fungal hydrophobin","start":56,"end":154}],"gene3D":[]},"genes":[{"name":{"value":"rodA"},"synonyms":[{"value":"hyp1"}],"orfNames":[{"value":"AFUA_5G09580"}]}],"length":159,"name":"Hydrophobin","ncbi_taxon_id":330879,"organism":"Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)","regions":[{"start":19,"end":38,"reference_id":"24659460","reference_source":"pmid","reference_html":"(1)H, (13)C and (15)N resonance assignments of the RodA hydrophobin from the opportunistic pathogen Aspergillus fumigatus. <i> Pille A, Kwan AH, Cheung I, Hampsey M, Aimanianda V, Delepierre M, Latge JP, Sunde M, Guijarro JI. </i> Biomol NMR Assign, 2015","date":"2026-06-09T15:51:49.499Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"cross_refs":[{"db":"BMRB","id":"19782"}],"region_id":"DP04313r001","sequence_construct":"SLPQHDVNAAGNGVGNKGNANVRFPVPDDITVKQATEKCGDQAQLSCCNKATYAGDVTDIDEGILAGTLKNLIGGGSGTEGLGLFNQCSKLDLQIPVIGIPIQALVNQKCKQNIACCQNSPSDASGSLIGLGLPCIALGSIL\n","statement":[{"text":"The RCI values calculated for RodA indicated that the N-terminal region (S1–N19) is disordered and that the loops between cysteine residues C4–C5 and C7–C8, and to a lesser extent a region (N71–T79) of the long C3–C4 loop, are highly flexible (Fig. 2b).","type":"Results"},{"text":"The numbering is not in the order of reference.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-09T15:51:51.577Z"}},{"start":108,"end":122,"reference_id":"24659460","reference_source":"pmid","reference_html":"(1)H, (13)C and (15)N resonance assignments of the RodA hydrophobin from the opportunistic pathogen Aspergillus fumigatus. <i> Pille A, Kwan AH, Cheung I, Hampsey M, Aimanianda V, Delepierre M, Latge JP, Sunde M, Guijarro JI. </i> Biomol NMR Assign, 2015","date":"2026-06-09T15:51:26.406Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"BMRB","id":"19782"}],"region_id":"DP04313r002","statement":[{"text":"The RCI values calculated for RodA indicated that the N-terminal region (S1–N19) is disordered and that the loops between cysteine residues C4–C5 and C7–C8, and to a lesser extent a region (N71–T79) of the long C3–C4 loop, are highly flexible (Fig. 2b).","type":"Results"},{"text":"Author residue numbering has been mapped to the UniProt canonical sequence. Boundaries were determined based on residues with RCI values > 0.5.","type":"Curator statement"}]},{"start":135,"end":149,"reference_id":"24659460","reference_source":"pmid","reference_html":"(1)H, (13)C and (15)N resonance assignments of the RodA hydrophobin from the opportunistic pathogen Aspergillus fumigatus. <i> Pille A, Kwan AH, Cheung I, Hampsey M, Aimanianda V, Delepierre M, Latge JP, Sunde M, Guijarro JI. </i> Biomol NMR Assign, 2015","date":"2026-06-09T15:53:59.624Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"BMRB","id":"19782"}],"region_id":"DP04313r003","statement":[{"text":"The RCI values calculated for RodA indicated that the N-terminal region (S1–N19) is disordered and that the loops between cysteine residues C4–C5 and C7–C8, and to a lesser extent a region (N71–T79) of the long C3–C4 loop, are highly flexible (Fig. 2b).","type":"Results"},{"text":"Author residue numbering has been mapped to the UniProt canonical sequence. Boundaries were determined based on residues with RCI values > 0.5.","type":"Curator statement"}]}],"regions_counter":3,"released":"2026_06","sequence":"MKFSLSAAVLAFAVSVAALPQHDVNAAGNGVGNKGNANVRFPVPDDITVKQATEKCGDQAQLSCCNKATYAGDVTDIDEGILAGTLKNLIGGGSGTEGLGLFNQCSKLDLQIPVIGIPIQALVNQKCKQNIACCQNSPSDASGSLIGLGLPCIALGSIL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Eurotiomycetes","Eurotiomycetidae","Eurotiales","Aspergillaceae","Aspergillus","Aspergillus subgen. Fumigati"],"alphafold_very_low_content":0.18867924528301888,"disorder_content":0.31446540880503143,"disprot_consensus":{"full":[{"start":19,"end":38,"type":"D"},{"start":108,"end":122,"type":"D"},{"start":135,"end":149,"type":"D"}],"Structural state":[{"start":19,"end":38,"type":"D"},{"start":108,"end":122,"type":"D"},{"start":135,"end":149,"type":"D"}]}},{"disprot_id":"DP04315","acc":"P39687","creator":"ldobson","date":"2024-11-21T11:12:10.011Z","features":{"pfam":[{"id":"PF14580","name":"Leucine-rich repeat","start":52,"end":146}],"gene3D":[]},"genes":[{"name":{"value":"ANP32A"},"synonyms":[{"value":"C15orf1"},{"value":"LANP"},{"value":"MAPM"},{"value":"PHAP1"}]}],"length":249,"name":"Acidic leucine-rich nuclear phosphoprotein 32 family member A","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":149,"end":249,"reference_id":"32694517","reference_source":"pmid","reference_html":"Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A. <i> Camacho-Zarco AR, Kalayil S, Maurin D, Salvi N, Delaforge E, Milles S, Jensen MR, Hart DJ, Cusack S, Blackledge M. </i> Nat Commun, 2020","date":"2026-06-09T16:12:58.577Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"BMRB","id":"28135"}],"region_id":"DP04315r002","statement":[{"text":"Backbone resonance assignment was completed to 78% and 58%, respectively, revealing that h and avANP32A IDDs are indeed both intrinsically disordered (Supplementary Figs. 1 and 2), with a slight tendency (20%) towards helical conformation for the hexapeptide, but negligible secondary structural tendency elsewhere.","type":"Results"}]},{"start":189,"end":249,"reference_id":"35639917","reference_source":"pmid","reference_html":"The C-terminal LCAR of host ANP32 proteins interacts with the influenza A virus nucleoprotein to promote the replication of the viral RNA genome. <i> Wang F, Sheppard CM, Mistry B, Staller E, Barclay WS, Grimes JM, Fodor E, Fan H. </i> Nucleic Acids Res, 2022","date":"2026-06-09T16:55:43.240Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140272","term_name":"exogenous protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Glu189Asp249del","start":null,"end":null,"position":null},{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P03467","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04315r003","statement":[{"text":"In a GST pull-down assay, NP was found to interact with N-terminally GST-tagged, full-length huANP32A, huANP32B and chANP32A, while no interaction was observed between NP and the GST tag alone (Figure 2A). When using LCAR-truncated ANP32 proteins comprising amino acid residues 1–188, corresponding to the region that mediates influenza virus polymerase dimerization (9), much weaker interactions were observed, particularly with chANP32A (Figure 2A). These results indicate that the LCAR is the primary mediator of interaction between ANP32 proteins and NP.","type":"Results"}],"term_comment":"Note that as GO captures normal processes, it may be that exogenous proteins interactions are normal for one of the participating species but not the other. Therefore reciprocal annotations should not be made without confirming that it is physiological relevant.","term_def":"\"Binding to a protein or protein complex from a different species, for example a pathogen molecule binding to a host protein.\" [PMID:28861068]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":3,"released":"2026_06","sequence":"MEMGRRIHLELRNRTPSDVKELVLDNSRSNEGKLEGLTDEFEELEFLSTINVGLTSIANLPKLNKLKKLELSDNRVSGGLEVLAEKCPNLTHLNLSGNKIKDLSTIEPLKKLENLKSLDLFNCEVTNLNDYRENVFKLLPQLTYLDGYDRDDKEAPDSDAEGYVEGLDDEEEDEDEEEYDEDAQVVEDEEDEDEEEEGEEEDVSGEEEEDEEGYNDGEVDDEEDEEELGEEERGQKRKREPEDEGEDDD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.11646586345381527,"dataset":["NDDs-related proteins"],"disorder_content":0,"disprot_consensus":{"full":[{"start":149,"end":249,"type":"F"}],"Structural state":[],"Disorder function":[{"start":149,"end":249,"type":"F"}],"Molecular function":[{"start":189,"end":249,"type":"F"}]}},{"disprot_id":"DP04316","acc":"P12978","creator":"ldobson","date":"2024-11-21T16:31:44.859Z","features":{"pfam":[{"id":"PF25697","name":"EBNA-2 N-terminal domain","start":1,"end":58},{"id":"PF25698","name":"EBNA-2 core transactivation domain","start":101,"end":487}],"gene3D":[]},"genes":[{"name":{"value":"EBNA2"},"orfNames":[{"value":"BYRF1"}]}],"length":487,"name":"Epstein-Barr nuclear antigen 2","ncbi_taxon_id":10377,"organism":"Epstein-Barr virus (strain B95-8)","regions":[{"start":431,"end":487,"reference_id":"24675874","reference_source":"pmid","reference_html":"Structural and functional characterization of a complex between the acidic transactivation domain of EBNA2 and the Tfb1/p62 subunit of TFIIH. <i> Chabot PR, Raiola L, Lussier-Price M, Morse T, Arseneault G, Archambault J, Omichinski JG. </i> PLoS Pathog, 2014","date":"2026-05-06T14:27:20.062Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"region_id":"DP04316r001","statement":[{"text":"In addition, the experiments with the 15N-labeled EBNA2431–487 indicate that the TAD of EBNA2 is intrinsically disordered in the unbound state and that only 15–20 amino acids within this region are affected by the binding of Tfb1PH ( Figure 1B ).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-06T14:27:36.374Z"}},{"start":448,"end":471,"reference_id":"24675874","reference_source":"pmid","reference_html":"Structural and functional characterization of a complex between the acidic transactivation domain of EBNA2 and the Tfb1/p62 subunit of TFIIH. <i> Chabot PR, Raiola L, Lussier-Price M, Morse T, Arseneault G, Archambault J, Omichinski JG. </i> PLoS Pathog, 2014","date":"2026-05-06T14:39:48.220Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140272","term_name":"exogenous protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"cross_refs":[{"db":"BMRB","id":"19791"},{"db":"PDB","id":"2MKR"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P32780","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04316r002","statement":[{"text":"To determine whether Tfb1PH interacts with EBNA2448–471 in a similar manner as EBNA2431–487, NMR chemical shift perturbation studies were performed by incremental addition of unlabeled EBNA2448–471 to 15N-labeled Tfb1PH. Virtually identical changes are observed in both the 1H and 15N chemical shifts of Tfb1PH in the 1H-15N HSQC spectrum when compared to the changes induced by EBNA2431–487 ( Figure 1 C–D and Supplementary Figure S1C–D).","type":"Results"},{"text":"While the experiments were conducted with the yeast homolog (P32776), evidence points towards the interaction to the human (host) protein.","type":"Curator statement"}],"term_comment":"Note that as GO captures normal processes, it may be that exogenous proteins interactions are normal for one of the participating species but not the other. Therefore reciprocal annotations should not be made without confirming that it is physiological relevant.","term_def":"\"Binding to a protein or protein complex from a different species, for example a pathogen molecule binding to a host protein.\" [PMID:28861068]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P32776"}]},{"start":455,"end":464,"reference_id":"24675874","reference_source":"pmid","reference_html":"Structural and functional characterization of a complex between the acidic transactivation domain of EBNA2 and the Tfb1/p62 subunit of TFIIH. <i> Chabot PR, Raiola L, Lussier-Price M, Morse T, Arseneault G, Archambault J, Omichinski JG. </i> PLoS Pathog, 2014","date":"2026-05-06T14:33:43.148Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"BMRB","id":"19791"},{"db":"PDB","id":"2MKR"}],"region_id":"DP04316r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P32776"}],"statement":[{"text":"In complex with Tfb1PH, EBNA2448–471 forms a 9-residue α helix between Asp455 and Glu463 ( Figure 2B ), and this is consistent with results of the NMR chemical shift perturbation studies ( Figure 1B ).","type":"Results"}]},{"start":448,"end":471,"reference_id":"24675874","reference_source":"pmid","reference_html":"Structural and functional characterization of a complex between the acidic transactivation domain of EBNA2 and the Tfb1/p62 subunit of TFIIH. <i> Chabot PR, Raiola L, Lussier-Price M, Morse T, Arseneault G, Archambault J, Omichinski JG. </i> PLoS Pathog, 2014","date":"2026-05-06T14:40:25.525Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140272","term_name":"exogenous protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P32780","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04316r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P32776"}],"statement":[{"text":"Taken together, these results show that although the TAD of EBNA2 binds to the same region of Tfb1PH as the TAD of p53, there are differences in how these two disordered TADs recognize a common target site in Tfb1.","type":"Results"},{"text":"While the experiments were conducted with the yeast homolog (P32776), evidence points towards the interaction to the human (host) protein. ","type":"Curator statement"}],"term_comment":"Note that as GO captures normal processes, it may be that exogenous proteins interactions are normal for one of the participating species but not the other. Therefore reciprocal annotations should not be made without confirming that it is physiological relevant.","term_def":"\"Binding to a protein or protein complex from a different species, for example a pathogen molecule binding to a host protein.\" [PMID:28861068]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":455,"end":462,"reference_id":"24675874","reference_source":"pmid","reference_html":"Structural and functional characterization of a complex between the acidic transactivation domain of EBNA2 and the Tfb1/p62 subunit of TFIIH. <i> Chabot PR, Raiola L, Lussier-Price M, Morse T, Arseneault G, Archambault J, Omichinski JG. </i> PLoS Pathog, 2014","date":"2026-05-06T15:23:31.438Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140272","term_name":"exogenous protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp458Thr","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To assess the relative importance of these three residues of EBNA2 for binding to Tfb1PH, ITC experiments were performed to measure the relative KD's of three EBNA2448–471 mutants (W458T, I461S and F462S) for Tfb1PH ( Figure 5 )."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile461Ser","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe462Ser","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P32780","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04316r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P32776"}],"statement":[{"text":"As expected, all three EBNA2448–471 mutants displayed significantly weaker affinity for Tfb1PH ( Figure 5C ). No heat of interaction is detected with either the W458T or F462S mutant by ITC, whereas the binding to the I461S mutant is 8-fold weaker than to wild-type EBNA2448–471.","type":"Results"},{"text":"While the experiments were conducted with the yeast homolog (P32776), evidence points towards the interaction to the human (host) protein.","type":"Curator statement"}],"term_comment":"Note that as GO captures normal processes, it may be that exogenous proteins interactions are normal for one of the participating species but not the other. Therefore reciprocal annotations should not be made without confirming that it is physiological relevant.","term_def":"\"Binding to a protein or protein complex from a different species, for example a pathogen molecule binding to a host protein.\" [PMID:28861068]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":458,"end":462,"reference_id":"24675874","reference_source":"pmid","reference_html":"Structural and functional characterization of a complex between the acidic transactivation domain of EBNA2 and the Tfb1/p62 subunit of TFIIH. <i> Chabot PR, Raiola L, Lussier-Price M, Morse T, Arseneault G, Archambault J, Omichinski JG. </i> PLoS Pathog, 2014","date":"2026-05-06T15:09:27.335Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0045893","term_name":"positive regulation of transcription, DNA-templated","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp458Thr","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To assess the relative importance of these three residues of EBNA2 for binding to Tfb1PH, ITC experiments were performed to measure the relative KD's of three EBNA2448–471 mutants (W458T, I461S and F462S) for Tfb1PH ( Figure 5 )."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile461Ser","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe462Ser","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04316r006","statement":[{"text":"In addition, both the I461S (23±5%) and F462S (7±2%) mutants of EBNA2431–487 fused to the LexA-DBD display reduced activity similar to the W458T mutant under these assay conditions. Consistent with the structure of the Tfb1PH-EBNA2448–471 complex and the ITC experiments, the three hydrophobic residues within the ΦXXΦΦ motif are important for the ability of the TAD of EBNA2 to activate transcription in a yeast model system.","type":"Results"}],"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription.\" [GOC:go_curators, GOC:txnOH]","term_is_obsolete":false,"term_not_annotate":false},{"start":431,"end":487,"reference_id":"24675874","reference_source":"pmid","reference_html":"Structural and functional characterization of a complex between the acidic transactivation domain of EBNA2 and the Tfb1/p62 subunit of TFIIH. <i> Chabot PR, Raiola L, Lussier-Price M, Morse T, Arseneault G, Archambault J, Omichinski JG. </i> PLoS Pathog, 2014","date":"2026-05-06T15:26:19.161Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0045893","term_name":"positive regulation of transcription, DNA-templated","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005616","ec_ontology":"ECO","ec_name":"beta-galactosidase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"ec_go":"IEP","region_id":"DP04316r007","statement":[{"text":"For this assay, EBNA2431–487 and three related mutants (Trp458T, I462S and F462S) were fused to the DNA-binding domain (DBD) of LexA and their activity for a lacZ reporter gene was measured relative to a positive control (LexA-DBD-Gal474–881; residues 74–881 of Gal4 fused to the LexA DBD). In this yeast assay, the LexA-DBD-EBNA2431–487 fusion protein activates transcription at 93±17% of the positive control, whereas the W458T mutant of EBNA2431–487 fused to the LexA-DBD activates at only 20±5%.","type":"Results"}],"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription.\" [GOC:go_curators, GOC:txnOH]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":448,"end":471,"reference_id":"24675874","reference_source":"pmid","reference_html":"Structural and functional characterization of a complex between the acidic transactivation domain of EBNA2 and the Tfb1/p62 subunit of TFIIH. <i> Chabot PR, Raiola L, Lussier-Price M, Morse T, Arseneault G, Archambault J, Omichinski JG. </i> PLoS Pathog, 2014","date":"2026-05-06T15:20:11.068Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0035035","term_name":"histone acetyltransferase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q92793","operator":null,"partner_start":586,"partner_end":672}],"region_id":"DP04316r008","statement":[{"text":"Addition of unlabeled CBP KIX to a 15N-labeled EBNA2448–471 causes significant changes in both the 1H and 15N chemical shifts of several signals from EBNA2. The signals displaying the most significant changes in the 1H-15N-HSQC spectra belongs to residues composing the ΦXXΦΦ motif of EBNA2 and are very similar to those seen with Tfb1PH ( Figure 7 and Supplementary Figure S3).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an histone acetyltransferase.\" [GOC:bf]","term_is_obsolete":false,"term_not_annotate":false},{"start":448,"end":471,"reference_id":"24675874","reference_source":"pmid","reference_html":"Structural and functional characterization of a complex between the acidic transactivation domain of EBNA2 and the Tfb1/p62 subunit of TFIIH. <i> Chabot PR, Raiola L, Lussier-Price M, Morse T, Arseneault G, Archambault J, Omichinski JG. </i> PLoS Pathog, 2014","date":"2026-05-06T15:24:27.438Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0001091","term_name":"RNA polymerase II general transcription initiation factor binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"BMRB","id":"19791"},{"db":"PDB","id":"2MKR"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P32780","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04316r009","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P32776"}],"statement":[{"text":"To determine whether Tfb1PH interacts with EBNA2448–471 in a similar manner as EBNA2431–487, NMR chemical shift perturbation studies were performed by incremental addition of unlabeled EBNA2448–471 to 15N-labeled Tfb1PH. Virtually identical changes are observed in both the 1H and 15N chemical shifts of Tfb1PH in the 1H-15N HSQC spectrum when compared to the changes induced by EBNA2431–487 ( Figure 1 C–D and Supplementary Figure S1C–D).","type":"Results"},{"text":"While the experiments were conducted with the yeast homolog (P32776), evidence points towards the interaction to the human (host) protein.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a basal RNA polymerase II transcription factor, any of the factors involved in formation of the preinitiation complex (PIC) by RNA polymerase II and defined as a basal or general transcription factor.\" [GOC:txnOH, PMID:16858867]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":10,"released":"2026_06","sequence":"MPTFYLALHGGQTYHLIVDTDSLGNPSLSVIPSNPYQEQLSDTPLIPLTIFVGENTGVPPPLPPPPPPPPPPPPPPPPPPPPPPPPPPSPPPPPPPPPPPQRRDAWTQEPSPLDRDPLGYDVGHGPLASAMRMLWMANYIVRQSRGDRGLILPQGPQTAPQARLVQPHVPPLRPTAPTILSPLSQPRLTPPQPLMMPPRPTPPTPLPPATLTVPPRPTRPTTLPPTPLLTVLQRPTELQPTPSPPRMHLPVLHVPDQSMHPLTHQSTPNDPDSPEPRSPTVFYNIPPMPLPPSQLPPPAAPAQPPPGVINDQQLHHLPSGPPWWPPICDPPQPSKTQGQSRGQSRGRGRGRGRGRGKGKSRDKQRKPGGPWRPEPNTSSPSMPELSPVLGLHQGQGAGDSPTPGPSNAAPVCRNSHTATPNVSPIHEPESHNSPEAPILFPDDWYPPSIDPADLDESWDYIFETTESPSSDEDYVEGPSKRPRPSIQ","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Peploviricota","Herviviricetes","Herpesvirales","Orthoherpesviridae","Gammaherpesvirinae","Lymphocryptovirus","Lymphocryptovirus humangamma4","Epstein-Barr virus (strain GD1)"],"dataset":["Viral proteins","Condensates-related proteins"],"disorder_content":0.11704312114989733,"disprot_consensus":{"full":[{"start":431,"end":454,"type":"D"},{"start":455,"end":464,"type":"T"},{"start":465,"end":487,"type":"D"}],"Structural state":[{"start":431,"end":487,"type":"D"}],"Molecular function":[{"start":448,"end":471,"type":"F"}],"Structural transition":[{"start":455,"end":464,"type":"T"}],"Biological process":[{"start":431,"end":487,"type":"F"}]}},{"disprot_id":"DP04317","acc":"P10221","creator":"ldobson","date":"2024-11-25T17:04:10.624Z","features":{"pfam":[{"id":"PF03970","name":"Herpesvirus UL37 tegument protein","start":9,"end":1102}],"gene3D":[]},"genes":[{"name":{"value":"UL37"}}],"length":1123,"name":"Inner tegument protein","ncbi_taxon_id":10299,"organism":"Human herpesvirus 1 (strain 17)","regions":[{"start":1,"end":21,"reference_id":"28768862","reference_source":"pmid","reference_html":"Crystal Structure of the N-Terminal Half of the Traffic Controller UL37 from Herpes Simplex Virus 1. <i> Koenigsberg AL, Heldwein EE. </i> J Virol, 2017","date":"2026-06-09T17:04:09.845Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"5VYL"}],"region_id":"DP04317r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"923"}],"sequence_construct":"GPGSMADRGLPSEAPVVTTSPAGPPSDGPMQRLLASLAGLRQPPTPTAETANGADDPAFLATAKLRAAMAAFLLSGTAIAPADARDCWRPLLEHLCALHRAHGLPETALLAENLPGLLVHRLVVALPEAPDQAFREMEVIKDTILAVTGSDTSHALDSAGLRTAAALGPVRVRQCAVEWIDRWQTVTKSCLAMSPRTSIEALGETSLKMAPVPLGQPSANLTTPAYSLLFPAPFVQEGLRFLALVSNRVTLFSAHLQRIDDATLTPLTRALFTLALVDEYLTTPERGAVVPPPLLAQFQHTVREIDPAIMIPPLEANKMVRSREEVRVSTALSRVSPRSACAPPGTLMARVRTDVAVFDPDVPFLSSSALAVFQPAVSSLLQLGEQPSAGAQQRLLALLQQTWTLIQNTNSPSVVINTLIDAGFTPSHCTHYLSALEGFLAAGVPARTPTGHGLGEVQQLFGCIALAGSNVFGLAREYGYYANYVKTFRRVQGASEHTHGRLCEAVGLSGGVLSQTLARIMGPAVPTEHLASLRRALVGEFETAERRFSSGQPSLLRETALIWIDVYGQTHWDITPTTP","statement":[{"text":"The first 21 residues of H37N are not resolved and are predicted to be disordered according to the secondary structure prediction algorithm in PSIPRED (20). ","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-09T17:04:42.742Z"}},{"start":39,"end":54,"reference_id":"28768862","reference_source":"pmid","reference_html":"Crystal Structure of the N-Terminal Half of the Traffic Controller UL37 from Herpes Simplex Virus 1. <i> Koenigsberg AL, Heldwein EE. </i> J Virol, 2017","date":"2026-06-09T17:04:54.045Z","curator_id":"ldobson","curator_name":"László Dobson","curator_orcid":"0000-0003-2765-3872","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"5VYL"}],"region_id":"DP04317r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"923"}],"sequence_construct":"GPGSMADRGLPSEAPVVTTSPAGPPSDGPMQRLLASLAGLRQPPTPTAETANGADDPAFLATAKLRAAMAAFLLSGTAIAPADARDCWRPLLEHLCALHRAHGLPETALLAENLPGLLVHRLVVALPEAPDQAFREMEVIKDTILAVTGSDTSHALDSAGLRTAAALGPVRVRQCAVEWIDRWQTVTKSCLAMSPRTSIEALGETSLKMAPVPLGQPSANLTTPAYSLLFPAPFVQEGLRFLALVSNRVTLFSAHLQRIDDATLTPLTRALFTLALVDEYLTTPERGAVVPPPLLAQFQHTVREIDPAIMIPPLEANKMVRSREEVRVSTALSRVSPRSACAPPGTLMARVRTDVAVFDPDVPFLSSSALAVFQPAVSSLLQLGEQPSAGAQQRLLALLQQTWTLIQNTNSPSVVINTLIDAGFTPSHCTHYLSALEGFLAAGVPARTPTGHGLGEVQQLFGCIALAGSNVFGLAREYGYYANYVKTFRRVQGASEHTHGRLCEAVGLSGGVLSQTLARIMGPAVPTEHLASLRRALVGEFETAERRFSSGQPSLLRETALIWIDVYGQTHWDITPTTP","statement":[{"text":"Additionally, the linkers between α1 and α2, β1 and α13, and α17 and α18 are unresolved. ","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-09T17:06:02.018Z"}},{"start":313,"end":336,"reference_id":"28768862","reference_source":"pmid","reference_html":"Crystal Structure of the N-Terminal Half of the Traffic Controller UL37 from Herpes Simplex Virus 1. <i> Koenigsberg AL, Heldwein EE. </i> J Virol, 2017","date":"2026-06-09T17:05:47.073Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"5VYL"}],"region_id":"DP04317r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"923"}],"statement":[{"text":"Additionally, the linkers between α1 and α2, β1 and α13, and α17 and α18 are unresolved.","type":"Results"}]}],"regions_counter":3,"released":"2026_06","sequence":"MADRGLPSEAPVVTTSPAGPPSDGPMQRLLASLAGLRQPPTPTAETANGADDPAFLATAKLRAAMAAFLLSGTAIAPADARDCWRPLLEHLCALHRAHGLPETALLAENLPGLLVHRLVVALPEAPDQAFREMEVIKDTILAVTGSDTSHALDSAGLRTAAALGPVRVRQCAVEWIDRWQTVTKSCLAMSPRTSIEALGETSLKMAPVPLGQPSANLTTPAYSLLFPAPFVQEGLRFLALVSNRVTLFSAHLQRIDDATLTPLTRALFTLALVDEYLTTPERGAVVPPPLLAQFQHTVREIDPAIMIPPLEANKMVRSREEVRVSTALSRVSPRSACAPPGTLMARVRTDVAVFDPDVPFLSSSALAVFQPAVSSLLQLGEQPSAGAQQRLLALLQQTWTLIQNTNSPSVVINTLIDAGFTPSHCTHYLSALEGFLAAGVPARTPTGHGLGEVQQLFGCIALAGSNVFGLAREYGYYANYVKTFRRVQGASEHTHGRLCEAVGLSGGVLSQTLARIMGPAVPTEHLASLRRALVGEFETAERRFSSGQPSLLRETALIWIDVYGQTHWDITPTTPATPLSALLPVGQPSHAPSVHLAAATQIRFPALEGIHPNVLADPGFVPYVLALVVGDALRATCSAAYLPRPVEFALRVLAWARDFGLGYLPTVEGHRTKLGALITLLEPAARGGLGPTMQMADNIEQLLRELYVISRGAVEQLRPLVQLQPPPPPEVGTSLLLISMYALAARGVLQDLAERADPLIRQLEDAIVLLRLHMRTLSAFFECRFESDGRRLYAVVGDTPDRLGPWPPEAMGDAVSQYCSMYHDAKRALVASLASLRSVITETTAHLGVCDELAAQVSHEDNVLAVVRREIHGFLSVVSGIHARASKLLSGDQVPGFCFMGQFLARWRRLSACYQAARAAAGPEPVAEFVQELHDTWKGLQTERAVVVAPLVSSADQRAAAIREVMAHAPEDAPPQSPAADRVVLTSRRDLGAWGDYSLGPLGQTTAVPDSVDLSRQGLAVTLSMDWLLMNELLRVTDGVFRASAFRPLAGPESPRDLEVRDAGNSLPAPMPMDAQKPEAYGHGPRQADREGAPHSNTPVEDDEMIPEDTVAPPTDLPLTSYQ","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Peploviricota","Herviviricetes","Herpesvirales","Orthoherpesviridae","Alphaherpesvirinae","Simplexvirus","Simplexvirus humanalpha1","Human herpesvirus 1"],"dataset":["Viral proteins"],"disorder_content":0.05431878895814782,"disprot_consensus":{"full":[{"start":1,"end":21,"type":"D"},{"start":39,"end":54,"type":"D"},{"start":313,"end":336,"type":"D"}],"Structural state":[{"start":1,"end":21,"type":"D"},{"start":39,"end":54,"type":"D"},{"start":313,"end":336,"type":"D"}]}},{"disprot_id":"DP04318","acc":"Q53HL2","creator":"xcastro","date":"2024-11-26T20:14:10.986Z","features":{"pfam":[{"id":"PF10444","name":"Nbl1 / Borealin N terminal","start":20,"end":75},{"id":"PF10512","name":"Cell division cycle-associated protein 8","start":163,"end":274}],"gene3D":[]},"genes":[{"name":{"value":"CDCA8"},"synonyms":[{"value":"PESCRG3"}]}],"length":280,"name":"Borealin","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":207,"end":225,"reference_id":"19530738","reference_source":"pmid","reference_html":"Phosphorylation of a borealin dimerization domain is required for proper chromosome segregation. <i> Bourhis E, Lingel A, Phung Q, Fairbrother WJ, Cochran AG. </i> Biochemistry, 2009","date":"2024-11-26T20:22:58.251Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"2KDD"}],"region_id":"DP04318r001","statement":[{"text":"The N-terminal residues (207-225), as well as the C-terminus (residues 278-280), are conformationally undefined in the calculated structures as a result of the lack of long-range restraints. Furthermore, analysis of heteronuclear NOE data shows increased backbone dynamics for these regions of the protein (Supporting Information Figure S2).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-04T17:00:03.121Z"}},{"start":105,"end":185,"reference_id":"31481798","reference_source":"pmid","reference_html":"The inner centromere is a biomolecular condensate scaffolded by the chromosomal passenger complex. <i> Trivedi P, Palomba F, Niedzialkowska E, Digman MA, Gratton E, Stukenberg PT. </i> Nat Cell Biol, 2019","date":"2026-06-04T17:21:15.821Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008035","ec_ontology":"ECO","ec_name":"author inference based on intrinsic disorder prediction used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04318r002","statement":[{"text":"We deleted two regions in the central unstructured region of Borealin that were predicted to have a high propensity to phase-separate by CatGranule41,42 (Fig.6a, Supplementary Fig.5g–i).","type":"Results"},{"text":"(h) PONDR profile of Borealin showing disorder propensity of the protein, Orange and brown shaded region shows 139-160 and 165-180 amino acids of Borealin respectively.","type":"Supplementary material"},{"text":"The boundaries of this disordered region were determined by the combination of the structural predictor used in the publication (PONDR) and AlphaFold.","type":"Curator statement"}]}],"regions_counter":5,"released":"2026_06","sequence":"MAPRKGSSRVAKTNSLRRRKLASFLKDFDREVEIRIKQIESDRQNLLKEVDNLYNIEILRLPKALREMNWLDYFALGGNKQALEEAATADLDITEINKLTAEAIQTPLKSAKTRKVIQVDEMIVEEEEEEENERKNLQTARVKRCPPSKKRTQSIQGKGKGKRSSRANTVTPAVGRLEVSMVKPTPGLTPRFDSRVFKTPGLRTPAAGERIYNISGNGSPLADSKEIFLTVPVGGGESLRLLASDLQRHSIAQLDPEALGNIKKLSNRLAQICSSIRTHK","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.2392857142857143,"dataset":["Condensates-related proteins"],"disorder_content":0.35714285714285715,"disprot_consensus":{"full":[{"start":105,"end":185,"type":"D"},{"start":207,"end":225,"type":"D"}],"Structural state":[{"start":105,"end":185,"type":"D"},{"start":207,"end":225,"type":"D"}]}},{"disprot_id":"DP04319","acc":"P43912","creator":"rpancsa","date":"2024-11-26T20:28:27.679Z","features":{"pfam":[{"id":"PF01746","name":"tRNA (Guanine-1)-methyltransferase TrmD","start":1,"end":225}],"gene3D":[]},"genes":[{"name":{"value":"trmD"},"olnNames":[{"value":"HI_0202"}]}],"length":246,"name":"tRNA (guanine-N(1)-)-methyltransferase","ncbi_taxon_id":71421,"organism":"Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)","regions":[{"start":161,"end":173,"reference_id":"12773376","reference_source":"pmid","reference_html":"Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognition. <i> Ahn HJ, Kim HW, Yoon HJ, Lee BI, Suh SW, Yang JK. </i> EMBO J, 2003","date":"2024-11-26T20:39:28.854Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"1UAJ"}],"region_id":"DP04319r001","statement":[{"text":"An extended flexible linker (residues 157–175) connects these two domains, which do not contact each other in a monomer. The inter-domain linker is largely disordered in the apo structure, with 13 residues (161–173) being invisible.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-04T17:43:02.528Z"}},{"start":161,"end":173,"reference_id":"12773376","reference_source":"pmid","reference_html":"Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognition. <i> Ahn HJ, Kim HW, Yoon HJ, Lee BI, Suh SW, Yang JK. </i> EMBO J, 2003","date":"2026-06-04T17:42:45.270Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"1UAJ"},{"db":"PDB","id":"1UAM"}],"region_id":"DP04319r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16680","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18367","entry_name":null}],"statement":[{"text":"The region consisting of residues Gly161*–Asp169* (dashed lines in Figure 1C) plays a role as a lid for covering the active site cleft. This region, which is disordered in the apo structure as well as the structures of binary complexes with either AdoMet or AdoHcy, becomes largely ordered in the structure of the ternary complex with AdoHcy and phosphate.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","states_connection":[{"source":"DP04319r001","target":"DP04319r003"}]},{"start":161,"end":173,"reference_id":"12773376","reference_source":"pmid","reference_html":"Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognition. <i> Ahn HJ, Kim HW, Yoon HJ, Lee BI, Suh SW, Yang JK. </i> EMBO J, 2003","date":"2026-06-04T17:41:30.117Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"1UAM"}],"region_id":"DP04319r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16680","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18367","entry_name":null}],"statement":[{"text":"The inter-domain linker is largely disordered in the apo structure, with 13 residues (161–173) being invisible. However, it is more ordered in the binary complexes with either AdoMet or AdoHcy, with nine residues (161–169) being invisible. In the ternary complex, only two residues (164 and 165) are disordered.","type":"Results"},{"text":"The region consisting of residues Gly161*–Asp169* (dashed lines in Figure 1C) plays a role as a lid for covering the active site cleft. This region, which is disordered in the apo structure as well as the structures of binary complexes with either AdoMet or AdoHcy, becomes largely ordered in the structure of the ternary complex with AdoHcy and phosphate.","type":"Results"}]},{"start":161,"end":173,"reference_id":"12773376","reference_source":"pmid","reference_html":"Crystal structure of tRNA(m1G37)methyltransferase: insights into tRNA recognition. <i> Ahn HJ, Kim HW, Yoon HJ, Lee BI, Suh SW, Yang JK. </i> EMBO J, 2003","date":"2026-06-04T17:42:28.311Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"1UAJ"}],"region_id":"DP04319r004","statement":[{"text":"TrmD comprises two distinct domains, a larger NTD of α/β-fold (residues 1–156) and a smaller CTD (residues 176–246) (Figure 1). An extended flexible linker (residues 157–175) connects these two domains, which do not contact each other in a monomer. The inter-domain linker is largely disordered in the apo structure, with 13 residues (161–173) being invisible.","type":"Results"}]}],"regions_counter":4,"released":"2026_06","sequence":"MWIGVISLFPEMFKAITEFGVTGRAVKHNLLKVECWNPRDFTFDKHKTVDDRPYGGGPGMLMMVQPLRDAIHTAKAAAGEGAKVIYLSPQGRKLDQGGVTELAQNQKLILVCGRYEGIDERLIQTEIDEEWSIGDYVLTGGELPAMTLIDAVARFIPGVLGKQASAEEDSFADGLLDCPHYTRPEVLEGLTVPPVLMSGHHEEIRKWRLKQSLQRTWLRRPELLEGLALTDEQRKLLKEAQAEHNS","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Pasteurellales","Pasteurellaceae","Haemophilus"],"alphafold_very_low_content":0,"disorder_content":0.052845528455284556,"disprot_consensus":{"full":[{"start":161,"end":173,"type":"T"}],"Structural state":[{"start":161,"end":173,"type":"D"}],"Structural transition":[{"start":161,"end":173,"type":"T"}],"Disorder function":[{"start":161,"end":173,"type":"F"}]}},{"disprot_id":"DP04320","acc":"Q8WYQ5","creator":"rpancsa","date":"2024-11-26T20:46:20.327Z","features":{"pfam":[{"id":"PF00035","name":"Double-stranded RNA binding motif","start":513,"end":576},{"id":"PF00035","name":"Double-stranded RNA binding motif","start":620,"end":684}],"gene3D":[]},"genes":[{"name":{"value":"DGCR8"},"synonyms":[{"value":"C22orf12"},{"value":"DGCRK6"}],"orfNames":[{"value":"LP4941"}]}],"length":773,"name":"Microprocessor complex subunit DGCR8","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":276,"end":297,"reference_id":"20506313","reference_source":"pmid","reference_html":"Structure of the dimerization domain of DiGeorge critical region 8. <i> Senturia R, Faller M, Yin S, Loo JA, Cascio D, Sawaya MR, Hwang D, Clubb RT, Guo F. </i> Protein Sci, 2010","date":"2024-11-26T20:52:44.017Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"3LE4"}],"region_id":"DP04320r001","statement":[{"text":"We determined a crystal structure of the dimerization domain, human DGCR8 276–353, at 1.7 Å resolution using the single-wavelength anomalous dispersion (SAD) method (Table I). High-quality electron density maps allowed the structure of residues 298–352 to be traced with no ambiguity [Fig. 3(A)], while the remaining 23 terminal residues appeared to be disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-05T17:19:16.119Z"}}],"regions_counter":1,"released":"2026_06","sequence":"METDESPSPLPCGPAGEAVMESRARPFQALPREQSPPPPLQTSSGAEVMDVGSGGDGQSELPAEDPFNFYGASLLSKGSFSKGRLLIDPNCSGHSPRTARHAPAVRKFSPDLKLLKDVKISVSFTESCRSKDRKVLYTGAERDVRAECGLLLSPVSGDVHACPFGGSVGDGVGIGGESADKKDEENELDQEKRVEYAVLDELEDFTDNLELDEEGAGGFTAKAIVQRDRVDEEALNFPYEDDFDNDVDALLEEGLCAPKKRRTEEKYGGDSDHPSDGETSVQPMMTKIKTVLKSRGRPPTEPLPDGWIMTFHNSGVPVYLHRESRVVTWSRPYFLGTGSIRKHDPPLSSIPCLHYKKMKDNEEREQSSDLTPSGDVSPVKPLSRSAELEFPLDEPDSMGADPGPPDEKDPLGAEAAPGALGQVKAKVEVCKDESVDLEEFRSYLEKRFDFEQVTVKKFRTWAERRQFNREMKRKQAESERPILPANQKLITLSVQDAPTKKEFVINPNGKSEVCILHEYMQRVLKVRPVYNFFECENPSEPFGASVTIDGVTYGSGTASSKKLAKNKAARATLEILIPDFVKQTSEEKPKDSEELEYFNHISIEDSRVYELTSKAGLLSPYQILHECLKRNHGMGDTSIKFEVVPGKNQKSEYVMACGKHTVRGWCKNKRVGKQLASQKILQLLHPHVKNWGSLLRMYGRESSKMVKQETSDKSVIELQQYAKKNKPNLHILSKLQEEMKRLAEEREETRKKPKMSIVASAQPGGEPLCTVDV","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.425614489003881,"dataset":["Cancer-related proteins"],"disorder_content":0.028460543337645538,"disprot_consensus":{"full":[{"start":276,"end":297,"type":"D"}],"Structural state":[{"start":276,"end":297,"type":"D"}]}},{"disprot_id":"DP04324","acc":"Q969S2","creator":"eficho","date":"2024-11-27T18:07:16.464Z","features":{"pfam":[{"id":"PF06831","name":"Formamidopyrimidine-DNA glycosylase H2TH domain","start":197,"end":266}],"gene3D":[]},"genes":[{"name":{"value":"NEIL2"}}],"length":332,"name":"Endonuclease 8-like 2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":56,"end":129,"reference_id":"34757057","reference_source":"pmid","reference_html":"Dynamics and Conformational Changes in Human NEIL2 DNA Glycosylase Analyzed by Hydrogen/Deuterium Exchange Mass Spectrometry. <i> Zhdanova PV, Ishchenko AA, Chernonosov AA, Zharkov DO, Koval VV. </i> J Mol Biol, 2022","date":"2024-11-27T18:17:27.923Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":20,"statements":[{"type":"Results","text":"The protein was exposed to deuterium exchange at 20 °C and pD 7.6 followed by HDX-MS analysis."}]}],"region_id":"DP04324r001","statement":[{"text":"For example, amino acid residues 37–55 and 238–265 demonstrated essentially no exchange in the first 10 s, whereas residues 56–129 from the prolinerich region showed the largest deuterium uptake of 65%.","type":"Results"},{"text":"The full time course of H/D exchange events for each peptide is illustrated by the butterfly plot in Figure 3(A). It can be seen that the amide hydrogens of residues 56–129 exchange fast and reach the maximum of saturation within the first ten seconds, which is consistent with the behavior of unstructured regions.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-05-14T15:54:37.717Z"}}],"regions_counter":1,"released":"2025_06","sequence":"MPEGPLVRKFHHLVSPFVGQQVVKTGGSSKKLQPASLQSLWLQDTQVHGKKLFLRFDLDEEMGPPGSSPTPEPPQKEVQKEGAADPKQVGEPSGQKTLDGSSRSAELVPQGEDDSEYLERDAPAGDAGRWLRVSFGLFGSVWVNDFSRAKKANKRGDWRDPSPRLVLHFGGGGFLAFYNCQLSWSSSPVVTPTCDILSEKFHRGQALEALGQAQPVCYTLLDQRYFSGLGNIIKNEALYRAGIHPLSLGSVLSASRREVLVDHVVEFSTAWLQGKFQGRPQHTQVYQKEQCPAGHQVMKEAFGPEDGLQRLTWWCPQCQPQLSEEPEQCQFS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.22289156626506024,"disorder_content":0.22289156626506024,"disprot_consensus":{"full":[{"start":56,"end":129,"type":"D"}],"Structural state":[{"start":56,"end":129,"type":"D"}]}},{"disprot_id":"DP04325","acc":"O95714","creator":"eficho","date":"2024-11-27T18:27:58.839Z","features":{"pfam":[{"id":"PF00173","name":"Cytochrome b5-like Heme/Steroid binding domain","start":1212,"end":1282},{"id":"PF00415","name":"Regulator of chromosome condensation (RCC1) repeat","start":514,"end":566},{"id":"PF00415","name":"Regulator of chromosome condensation (RCC1) repeat","start":569,"end":612},{"id":"PF00415","name":"Regulator of chromosome condensation (RCC1) repeat","start":623,"end":672},{"id":"PF00415","name":"Regulator of chromosome condensation (RCC1) repeat","start":675,"end":724},{"id":"PF00415","name":"Regulator of chromosome condensation (RCC1) repeat","start":4163,"end":4212},{"id":"PF00415","name":"Regulator of chromosome condensation (RCC1) repeat","start":4215,"end":4263},{"id":"PF00415","name":"Regulator of chromosome condensation (RCC1) repeat","start":4267,"end":4316},{"id":"PF00569","name":"Zinc finger, ZZ type","start":2702,"end":2742},{"id":"PF00632","name":"HECT-domain (ubiquitin-transferase)","start":4513,"end":4789},{"id":"PF03256","name":"Anaphase-promoting complex, subunit 10 (APC10)","start":2803,"end":2871},{"id":"PF06701","name":"Mib_herc2","start":1870,"end":1929},{"id":"PF11515","name":"Mouse development and cellular proliferation protein Cullin-7","start":2554,"end":2630},{"id":"PF25390","name":"RCC1-like domain","start":2960,"end":3323},{"id":"PF25390","name":"RCC1-like domain","start":3950,"end":4152},{"id":"PF31077","name":"HERC2 UBA-like domain","start":2461,"end":2505}],"gene3D":[]},"genes":[{"name":{"value":"HERC2","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAD08657.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAD08657.1"}}]}}],"length":4834,"name":"E3 ubiquitin-protein ligase HERC2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":4793,"end":4834,"reference_id":"39565083","reference_source":"pmid","reference_html":"The disordered negatively charged C-terminus of the large HECT E3 ubiquitin ligase HERC2 provides structural and thermal stability to the HECT C-lobe. <i> Waters KL, Rich KJ, Schwaegerle ND, Yang T, Huo S, Spratt DE. </i> Protein Sci, 2024","date":"2024-11-27T18:30:05.709Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04325r001","statement":[{"text":"In contrast, the 15N‐HSQC spectrum for the HERC2 negatively charged C‐terminal tail showed that this region is disordered as indicated by the narrow distribution of amide peaks (Figure 5a).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-25T17:08:40.169Z"}},{"start":4793,"end":4834,"reference_id":"39565083","reference_source":"pmid","reference_html":"The disordered negatively charged C-terminus of the large HECT E3 ubiquitin ligase HERC2 provides structural and thermal stability to the HECT C-lobe. <i> Waters KL, Rich KJ, Schwaegerle ND, Yang T, Huo S, Spratt DE. </i> Protein Sci, 2024","date":"2024-11-27T18:31:56.417Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04325r002","statement":[{"text":"To determine their biological relevance, a 15N‐HSQC spectrum was collected for the HERC2 extended C‐lobe (residues G4676–H4834). When this spectrum was overlaid with the 15N‐HSQC spectra for the isolated HERC2 C‐lobe and negatively charged C‐terminal tail, there was a significant amount of peak overlap (Figure 6). These data show that the isolated HERC2 C‐lobe and negatively charged C‐terminal tail constructs are biologically relevant since the chemical environment of most residues was not significantly different when compared the HERC2 extended C‐lobe spectrum. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-25T17:09:42.373Z"}},{"start":4793,"end":4834,"reference_id":"39565083","reference_source":"pmid","reference_html":"The disordered negatively charged C-terminus of the large HECT E3 ubiquitin ligase HERC2 provides structural and thermal stability to the HECT C-lobe. <i> Waters KL, Rich KJ, Schwaegerle ND, Yang T, Huo S, Spratt DE. </i> Protein Sci, 2024","date":"2024-11-27T18:33:55.510Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04325r003","statement":[{"text":"Circular dichroism (CD) spectra and normalized melting curves indicate that the HERC2 negatively charged C‐terminal tail increases the stability of the HERC2 C‐lobe. ","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-25T17:08:58.746Z"}},{"start":4793,"end":4834,"reference_id":"39565083","reference_source":"pmid","reference_html":"The disordered negatively charged C-terminus of the large HECT E3 ubiquitin ligase HERC2 provides structural and thermal stability to the HECT C-lobe. <i> Waters KL, Rich KJ, Schwaegerle ND, Yang T, Huo S, Spratt DE. </i> Protein Sci, 2024","date":"2024-11-27T18:34:25.573Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0050821","term_name":"protein stabilization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP04325r004","statement":[{"text":"Circular dichroism (CD) spectra and normalized melting curves indicate that the HERC2 negatively charged C‐terminal tail increases the stability of the HERC2 C‐lobe. ","type":"Figure"}],"term_comment":"","term_def":"\"Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-02-25T17:08:50.447Z"}}],"regions_counter":4,"released":"2025_06","sequence":"MPSESFCLAAQARLDSKWLKTDIQLAFTRDGLCGLWNEMVKDGEIVYTGTESTQNGELPPRKDDSVEPSGTKKEDLNDKEKKDEEETPAPIYRAKSILDSWVWGKQPDVNELKECLSVLVKEQQALAVQSATTTLSALRLKQRLVILERYFIALNRTVFQENVKVKWKSSGISLPPVDKKSSRPAGKGVEGLARVGSRAALSFAFAFLRRAWRSGEDADLCSELLQESLDALRALPEASLFDESTVSSVWLEVVERATRFLRSVVTGDVHGTPATKGPGSIPLQDQHLALAILLELAVQRGTLSQMLSAILLLLQLWDSGAQETDNERSAQGTSAPLLPLLQRFQSIICRKDAPHSEGDMHLLSGPLSPNESFLRYLTLPQDNELAIDLRQTAVVVMAHLDRLATPCMPPLCSSPTSHKGSLQEVIGWGLIGWKYYANVIGPIQCEGLANLGVTQIACAEKRFLILSRNGRVYTQAYNSDTLAPQLVQGLASRNIVKIAAHSDGHHYLALAATGEVYSWGCGDGGRLGHGDTVPLEEPKVISAFSGKQAGKHVVHIACGSTYSAAITAEGELYTWGRGNYGRLGHGSSEDEAIPMLVAGLKGLKVIDVACGSGDAQTLAVTENGQVWSWGDGDYGKLGRGGSDGCKTPKLIEKLQDLDVVKVRCGSQFSIALTKDGQVYSWGKGDNQRLGHGTEEHVRYPKLLEGLQGKKVIDVAAGSTHCLALTEDSEVHSWGSNDQCQHFDTLRVTKPEPAALPGLDTKHIVGIACGPAQSFAWSSCSEWSIGLRVPFVVDICSMTFEQLDLLLRQVSEGMDGSADWPPPQEKECVAVATLNLLRLQLHAAISHQVDPEFLGLGLGSILLNSLKQTVVTLASSAGVLSTVQSAAQAVLQSGWSVLLPTAEERARALSALLPCAVSGNEVNISPGRRFMIDLLVGSLMADGGLESALHAAITAEIQDIEAKKEAQKEKEIDEQEANASTFHRSRTPLDKDLINTGICESSGKQCLPLVQLIQQLLRNIASQTVARLKDVARRISSCLDFEQHSRERSASLDLLLRFQRLLISKLYPGESIGQTSDISSPELMGVGSLLKKYTALLCTHIGDILPVAASIASTSWRHFAEVAYIVEGDFTGVLLPELVVSIVLLLSKNAGLMQEAGAVPLLGGLLEHLDRFNHLAPGKERDDHEELAWPGIMESFFTGQNCRNNEEVTLIRKADLENHNKDGGFWTVIDGKVYDIKDFQTQSLTGNSILAQFAGEDPVVALEAALQFEDTRESMHAFCVGQYLEPDQEIVTIPDLGSLSSPLIDTERNLGLLLGLHASYLAMSTPLSPVEIECAKWLQSSIFSGGLQTSQIHYSYNEEKDEDHCSSPGGTPASKSRLCSHRRALGDHSQAFLQAIADNNIQDHNVKDFLCQIERYCRQCHLTTPIMFPPEHPVEEVGRLLLCCLLKHEDLGHVALSLVHAGALGIEQVKHRTLPKSVVDVCRVVYQAKCSLIKTHQEQGRSYKEVCAPVIERLRFLFNELRPAVCNDLSIMSKFKLLSSLPRWRRIAQKIIRERRKKRVPKKPESTDDEEKIGNEESDLEEACILPHSPINVDKRPIAIKSPKDKWQPLLSTVTGVHKYKWLKQNVQGLYPQSPLLSTIAEFALKEEPVDVEKMRKCLLKQLERAEVRLEGIDTILKLASKNFLLPSVQYAMFCGWQRLIPEGIDIGEPLTDCLKDVDLIPPFNRMLLEVTFGKLYAWAVQNIRNVLMDASAKFKELGIQPVPLQTITNENPSGPSLGTIPQARFLLVMLSMLTLQHGANNLDLLLNSGMLALTQTALRLIGPSCDNVEEDMNASAQGASATVLEETRKETAPVQLPVSGPELAAMMKIGTRVMRGVDWKWGDQDGPPPGLGRVIGELGEDGWIRVQWDTGSTNSYRMGKEGKYDLKLAELPAAAQPSAEDSDTEDDSEAEQTERNIHPTAMMFTSTINLLQTLCLSAGVHAEIMQSEATKTLCGLLRMLVESGTTDKTSSPNRLVYREQHRSWCTLGFVRSIALTPQVCGALSSPQWITLLMKVVEGHAPFTATSLQRQILAVHLLQAVLPSWDKTERARDMKCLVEKLFDFLGSLLTTCSSDVPLLRESTLRRRRVRPQASLTATHSSTLAEEVVALLRTLHSLTQWNGLINKYINSQLRSITHSFVGRPSEGAQLEDYFPDSENPEVGGLMAVLAVIGGIDGRLRLGGQVMHDEFGEGTVTRITPKGKITVQFSDMRTCRVCPLNQLKPLPAVAFNVNNLPFTEPMLSVWAQLVNLAGSKLEKHKIKKSTKQAFAGQVDLDLLRCQQLKLYILKAGRALLSHQDKLRQILSQPAVQETGTVHTDDGAVVSPDLGDMSPEGPQPPMILLQQLLASATQPSPVKAIFDKQELEAAALAVCQCLAVESTHPSSPGFEDCSSSEATTPVAVQHIRPARVKRRKQSPVPALPIVVQLMEMGFSRRNIEFALKSLTGASGNASSLPGVEALVGWLLDHSDIQVTELSDADTVSDEYSDEEVVEDVDDAAYSMSTGAVVTESQTYKKRADFLSNDDYAVYVRENIQVGMMVRCCRAYEEVCEGDVGKVIKLDRDGLHDLNVQCDWQQKGGTYWVRYIHVELIGYPPPSSSSHIKIGDKVRVKASVTTPKYKWGSVTHQSVGVVKAFSANGKDIIVDFPQQSHWTGLLSEMELVPSIHPGVTCDGCQMFPINGSRFKCRNCDDFDFCETCFKTKKHNTRHTFGRINEPGQSAVFCGRSGKQLKRCHSSQPGMLLDSWSRMVKSLNVSSSVNQASRLIDGSEPCWQSSGSQGKHWIRLEIFPDVLVHRLKMIVDPADSSYMPSLVVVSGGNSLNNLIELKTININPSDTTVPLLNDCTEYHRYIEIAIKQCRSSGIDCKIHGLILLGRIRAEEEDLAAVPFLASDNEEEEDEKGNSGSLIRKKAAGLESAATIRTKVFVWGLNDKDQLGGLKGSKIKVPSFSETLSALNVVQVAGGSKSLFAVTVEGKVYACGEATNGRLGLGISSGTVPIPRQITALSSYVVKKVAVHSGGRHATALTVDGKVFSWGEGDDGKLGHFSRMNCDKPRLIEALKTKRIRDIACGSSHSAALTSSGELYTWGLGEYGRLGHGDNTTQLKPKMVKVLLGHRVIQVACGSRDAQTLALTDEGLVFSWGDGDFGKLGRGGSEGCNIPQNIERLNGQGVCQIECGAQFSLALTKSGVVWTWGKGDYFRLGHGSDVHVRKPQVVEGLRGKKIVHVAVGALHCLAVTDSGQVYAWGDNDHGQQGNGTTTVNRKPTLVQGLEGQKITRVACGSSHSVAWTTVDVATPSVHEPVLFQTARDPLGASYLGVPSDADSSAASNKISGASNSKPNRPSLAKILLSLDGNLAKQQALSHILTALQIMYARDAVVGALMPAAMIAPVECPSFSSAAPSDASAMASPMNGEECMLAVDIEDRLSPNPWQEKREIVSSEDAVTPSAVTPSAPSASARPFIPVTDDLGAASIIAETMTKTKEDVESQNKAAGPEPQALDEFTSLLIADDTRVVVDLLKLSVCSRAGDRGRDVLSAVLSGMGTAYPQVADMLLELCVTELEDVATDSQSGRLSSQPVVVESSHPYTDDTSTSGTVKIPGAEGLRVEFDRQCSTERRHDPLTVMDGVNRIVSVRSGREWSDWSSELRIPGDELKWKFISDGSVNGWGWRFTVYPIMPAAGPKELLSDRCVLSCPSMDLVTCLLDFRLNLASNRSIVPRLAASLAACAQLSALAASHRMWALQRLRKLLTTEFGQSININRLLGENDGETRALSFTGSALAALVKGLPEALQRQFEYEDPIVRGGKQLLHSPFFKVLVALACDLELDTLPCCAETHKWAWFRRYCMASRVAVALDKRTPLPRLFLDEVAKKIRELMADSENMDVLHESHDIFKREQDEQLVQWMNRRPDDWTLSAGGSGTIYGWGHNHRGQLGGIEGAKVKVPTPCEALATLRPVQLIGGEQTLFAVTADGKLYATGYGAGGRLGIGGTESVSTPTLLESIQHVFIKKVAVNSGGKHCLALSSEGEVYSWGEAEDGKLGHGNRSPCDRPRVIESLRGIEVVDVAAGGAHSACVTAAGDLYTWGKGRYGRLGHSDSEDQLKPKLVEALQGHRVVDIACGSGDAQTLCLTDDDTVWSWGDGDYGKLGRGGSDGCKVPMKIDSLTGLGVVKVECGSQFSVALTKSGAVYTWGKGDYHRLGHGSDDHVRRPRQVQGLQGKKVIAIATGSLHCVCCTEDGEVYTWGDNDEGQLGDGTTNAIQRPRLVAALQGKKVNRVACGSAHTLAWSTSKPASAGKLPAQVPMEYNHLQEIPIIALRNRLLLLHHLSELFCPCIPMFDLEGSLDETGLGPSVGFDTLRGILISQGKEAAFRKVVQATMVRDRQHGPVVELNRIQVKRSRSKGGLAGPDGTKSVFGQMCAKMSSFGPDSLLLPHRVWKVKFVGESVDDCGGGYSESIAEICEELQNGLTPLLIVTPNGRDESGANRDCYLLSPAARAPVHSSMFRFLGVLLGIAIRTGSPLSLNLAEPVWKQLAGMSLTIADLSEVDKDFIPGLMYIRDNEATSEEFEAMSLPFTVPSASGQDIQLSSKHTHITLDNRAEYVRLAINYRLHEFDEQVAAVREGMARVVPVPLLSLFTGYELETMVCGSPDIPLHLLKSVATYKGIEPSASLIQWFWEVMESFSNTERSLFLRFVWGRTRLPRTIADFRGRDFVIQVLDKYNPPDHFLPESYTCFFLLKLPRYSCKQVLEEKLKYAIHFCKSIDTDDYARIALTGEPAADDSSDDSDNEDVDSFASDSTQDYLTGH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"dataset":["NDDs-related proteins"],"disorder_content":0.008688456764584195,"disprot_consensus":{"full":[{"start":4793,"end":4834,"type":"D"}],"Structural state":[{"start":4793,"end":4834,"type":"D"}],"Disorder function":[{"start":4793,"end":4834,"type":"F"}],"Biological process":[{"start":4793,"end":4834,"type":"F"}]}},{"disprot_id":"DP04326","acc":"Q86YC2","creator":"eficho","date":"2024-11-27T18:47:51.556Z","features":{"pfam":[{"id":"PF16756","name":"Partner and localizer of BRCA2 WD40 domain","start":840,"end":1184}],"gene3D":[]},"genes":[{"name":{"value":"PALB2"},"synonyms":[{"value":"FANCN"}]}],"length":1186,"name":"Partner and localizer of BRCA2","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":22,"end":26,"reference_id":"39584160","reference_source":"pmid","reference_html":"The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction. <i> Kyriukha Y, Watkins MB, Redington JM, Chintalapati N, Ganti A, Dastvan R, Uversky VN, Hopkins JB, Pozzi N, Korolev S. </i> iScience, 2024","date":"2025-04-22T10:41:23.421Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q86YC2","operator":null,"partner_start":10,"partner_end":40}],"region_id":"DP04326r001","statement":[{"text":"MALS measurements unequivocally confirm the dimeric form of PALB2-DBD under both buffer conditions (Figures 4A and 4B) and the monomeric form of L24A mutant at 0.16 M NaCl (Figure 4C).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu24Ala","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-05-15T13:04:45.241Z"}},{"start":136,"end":145,"reference_id":"39584160","reference_source":"pmid","reference_html":"The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction. <i> Kyriukha Y, Watkins MB, Redington JM, Chintalapati N, Ganti A, Dastvan R, Uversky VN, Hopkins JB, Pozzi N, Korolev S. </i> iScience, 2024","date":"2025-06-17T19:43:42.245Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006287","ec_ontology":"ECO","ec_name":"electron paramagnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"9160","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04326r006","statement":[{"text":"The addition of dT40 causes a notable change in flexibility only at position 145 immediately next to the major DNA-binding site (146–149 aa) and a minor decrease at position 136 proximal to DNA binding site (Figures 3B and 3C).","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser136Cys","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser145Cys","start":null,"end":null,"position":null},{"term_id":"MI:0845","term_name":"spin label","term_namespace":"Labels and dyes","start":136,"end":136,"position":"Specific residue"},{"term_id":"MI:0845","term_name":"spin label","term_namespace":"Labels and dyes","start":145,"end":145,"position":"Specific residue"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:50:52.505Z"}},{"start":40,"end":195,"reference_id":"39584160","reference_source":"pmid","reference_html":"The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction. <i> Kyriukha Y, Watkins MB, Redington JM, Chintalapati N, Ganti A, Dastvan R, Uversky VN, Hopkins JB, Pozzi N, Korolev S. </i> iScience, 2024","date":"2025-03-18T17:27:57.789Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006287","ec_ontology":"ECO","ec_name":"electron paramagnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04326r008","statement":[{"text":"Most spectra correspond to a highly flexible conformation of local peptide in the label vicinity. Values of the h(+1)/h(0) ratio correspond to those for other IDPs (Figure 3C),71 with the exception of position 11 at the beginning of the PALB2-cc where a lower value corresponds to a more rigid structure near the coiled-coil region. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-05-15T13:01:14.362Z"}},{"start":41,"end":194,"reference_id":"39584160","reference_source":"pmid","reference_html":"The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction. <i> Kyriukha Y, Watkins MB, Redington JM, Chintalapati N, Ganti A, Dastvan R, Uversky VN, Hopkins JB, Pozzi N, Korolev S. </i> iScience, 2024","date":"2025-06-17T09:54:50.790Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04326r009","statement":[{"text":"The PALB2-DBD spectra are characterized by peaks corresponding to α-helical (223 nm) and disordered (204 nm) structures (Figure 2A, solid line). The spectrum of the Δ40-DBD fragment lacking the N-terminal α-helix does not display a peak corresponding to α-helix (Figure 2B).","type":"Results"},{"text":"Based on the Methods section, the PALB2 N-terminal fragments (1–195 I195W) was cloned into a pSMT-MBP plasmid containing an N-terminal 63His-SUMO and a C-terminal MBP tag using Gibson assembly, therefore residue 195 cannot be part of the IDR.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-17T15:57:47.961Z"}},{"start":1,"end":195,"reference_id":"39584160","reference_source":"pmid","reference_html":"The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction. <i> Kyriukha Y, Watkins MB, Redington JM, Chintalapati N, Ganti A, Dastvan R, Uversky VN, Hopkins JB, Pozzi N, Korolev S. </i> iScience, 2024","date":"2025-04-22T10:14:38.531Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04326r010","statement":[{"text":"SAXS analyses resulted in typical IDP scattering patterns, as illustrated by the slow decay of the tail when data are plotted as a dimensionless Kratky plot distribution (Figure 4D).","type":"Results"},{"text":"Interestingly, the distribution obtained for L24A monomer suggests a more disordered state (Figure 4D, dark red) than the dimer under either salt condition. In fact, an estimated Rg value of 52.3 (ν = 0.54) of the monomeric L24A mutant even larger than the Rg of the dimer under same conditions (Figures 4D and 4E), suggesting that the interaction between IDRs subunits leads to compaction of each monomer and of the entire dimer.","type":"Methods"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu24Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Interestingly, the distribution obtained for L24A monomer suggests a more disordered state (Figure 4D, dark red) than the dimer under either salt condition. "}]}],"cross_refs":[{"db":"SASBDB","id":"SASDVQ7"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-05-15T13:02:21.951Z"}},{"start":1,"end":195,"reference_id":"39584160","reference_source":"pmid","reference_html":"The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction. <i> Kyriukha Y, Watkins MB, Redington JM, Chintalapati N, Ganti A, Dastvan R, Uversky VN, Hopkins JB, Pozzi N, Korolev S. </i> iScience, 2024","date":"2024-11-27T19:06:36.397Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"9160","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04326r012","statement":[{"text":"Addition of DNA to protein resulted in a significantly more compact structure of the dimer, with a Kratky plot shape more characteristic of a globular protein than an IDP (Figure 4H). ","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-17T16:11:17.940Z"}},{"start":1,"end":195,"reference_id":"39584160","reference_source":"pmid","reference_html":"The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction. <i> Kyriukha Y, Watkins MB, Redington JM, Chintalapati N, Ganti A, Dastvan R, Uversky VN, Hopkins JB, Pozzi N, Korolev S. </i> iScience, 2024","date":"2024-11-27T19:08:51.065Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001183","ec_ontology":"ECO","ec_name":"fluorescence resonance energy transfer evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"9160","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04326r013","statement":[{"text":"A similar trend was observed for a dT50 substrate with Cy3 and Cy5 labels placed 25 nucleotides apart (Figure S13A). Mean FRET for free DNA is 0.45, the major peak at 1 μM PALB2-DBD is at FRET of 0.71, and the peak for 3 μM PALB2-DBD is at FRET of 0.89. DNA compaction is significant for this substrate as well, although it is challenging to deconvolute two separate peaks at each protein concentration due to the initially high FRET for free DNA.","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-17T15:51:29.995Z"}},{"start":1,"end":195,"reference_id":"39584160","reference_source":"pmid","reference_html":"The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction. <i> Kyriukha Y, Watkins MB, Redington JM, Chintalapati N, Ganti A, Dastvan R, Uversky VN, Hopkins JB, Pozzi N, Korolev S. </i> iScience, 2024","date":"2025-04-22T11:05:39.960Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q86YC2","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04326r015","statement":[{"text":"Analysis of SAXS data yielded an estimated molecular weight of 110 kDa (Table S4), which is very close to molecular weight of PAB2-DBD:dT50 complex at 4:1 stoichiometry of 107 kDa. Therefore, SAXS data revealed a tetrameric form of PALB2-DBD complex with ssDNA.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"cross_refs":[{"db":"SASBDB","id":"SASDVR7"}],"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"Therefore, SAXS data revealed a tetrameric form of PALB2-DBD complex with ssDNA."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-05-15T13:05:41.218Z"}},{"start":41,"end":194,"reference_id":"39584160","reference_source":"pmid","reference_html":"The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction. <i> Kyriukha Y, Watkins MB, Redington JM, Chintalapati N, Ganti A, Dastvan R, Uversky VN, Hopkins JB, Pozzi N, Korolev S. </i> iScience, 2024","date":"2025-02-25T18:02:16.037Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04326r017","statement":[{"text":"IDPs have different functionally relevant structural organizations ranging from compact molten globule (MG) structures to extended random coil (RC) conformations, which can be distinguished by a hydrodynamic volume (Vh) that is only 2–3 times larger than the volume of a folded globular structure of the same molecular weight for MG and up to 10 times larger for RC.","type":"Results"},{"text":"The elution volume under nondenaturing conditions corresponds to a globular protein with a molecular weight only twice that of Δ40-DBD.","type":"Results"}]},{"start":1,"end":194,"reference_id":"39584160","reference_source":"pmid","reference_html":"The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction. <i> Kyriukha Y, Watkins MB, Redington JM, Chintalapati N, Ganti A, Dastvan R, Uversky VN, Hopkins JB, Pozzi N, Korolev S. </i> iScience, 2024","date":"2025-03-17T16:03:14.204Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003697","term_name":"single-stranded DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"76376","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04326r018","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null}],"statement":[{"text":"Three peaks were observed upon addition of ssDNA at 1:2 DNA:protein ratio, one at low molecular weight position, corresponding to free DNA, the second at position of PALB2-DBD dimer (an apparent MW = 45.2 kDa), and the third at position with molecular weight of ∼78 kDa, corresponding to the tetramer.","type":"Results"}],"term_comment":"Note that this term is restricted to those cases where the binding is to a single-stranded DNA molecule, not to one of the stands of double-stranded DNA.","term_def":"\"Binding to single-stranded DNA.\" [GOC:elh, GOC:vw, PMID:22976174]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":194,"reference_id":"39584160","reference_source":"pmid","reference_html":"The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction. <i> Kyriukha Y, Watkins MB, Redington JM, Chintalapati N, Ganti A, Dastvan R, Uversky VN, Hopkins JB, Pozzi N, Korolev S. </i> iScience, 2024","date":"2025-03-17T16:05:34.068Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051289","term_name":"protein homotetramerization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"EXP","region_id":"DP04326r019","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting ssDNA with poly(dT) sequence."}]}],"statement":[{"text":"Three peaks were observed upon addition of ssDNA at 1:2 DNA:protein ratio, one at low molecular weight position, corresponding to free DNA, the second at position of PALB2-DBD dimer (an apparent MW = 45.2 kDa), and the third at position with molecular weight of ∼78 kDa, corresponding to the tetramer.","type":"Results"}],"term_comment":"","term_def":"\"The formation of a protein homotetramer, a macromolecular structure consisting of four noncovalently associated identical subunits.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":194,"reference_id":"39584160","reference_source":"pmid","reference_html":"The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction. <i> Kyriukha Y, Watkins MB, Redington JM, Chintalapati N, Ganti A, Dastvan R, Uversky VN, Hopkins JB, Pozzi N, Korolev S. </i> iScience, 2024","date":"2025-03-17T16:06:15.636Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q86YC2","operator":null,"partner_start":1,"partner_end":195}],"region_id":"DP04326r020","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting ssDNA with poly(dT) sequence."}]}],"statement":[{"text":"Three peaks were observed upon addition of ssDNA at 1:2 DNA:protein ratio, one at low molecular weight position, corresponding to free DNA, the second at position of PALB2-DBD dimer (an apparent MW = 45.2 kDa), and the third at position with molecular weight of ∼78 kDa, corresponding to the tetramer.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false},{"start":10,"end":40,"reference_id":"39584160","reference_source":"pmid","reference_html":"The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction. <i> Kyriukha Y, Watkins MB, Redington JM, Chintalapati N, Ganti A, Dastvan R, Uversky VN, Hopkins JB, Pozzi N, Korolev S. </i> iScience, 2024","date":"2025-04-22T11:09:51.663Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04326r021","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q86YC2"}],"statement":[{"text":"Interestingly, the distribution obtained for L24A monomer suggests a more disordered state (Figure 4D, dark red) than the dimer under either salt condition. In fact, an estimated Rg value of 52.3 (ν = 0.54) of the monomeric L24A mutant even larger than the Rg of the dimer under same conditions (Figures 4D and 4E), suggesting that the interaction between IDRs subunits leads to compaction of each monomer and of the entire dimer.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-05-15T13:03:43.558Z"}},{"start":145,"end":149,"reference_id":"31017574","reference_source":"pmid","reference_html":"Novel RNA and DNA strand exchange activity of the PALB2 DNA binding domain and its critical role for DNA repair in cells. <i> Deveryshetty J, Peterlini T, Ryzhikov M, Brahiti N, Dellaire G, Masson JY, Korolev S. </i> Elife, 2019","date":"2025-07-01T14:16:58.470Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003697","term_name":"single-stranded DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg146Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg147Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys148Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys149Ala","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"ChEBI","id":"75153","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04326r022","statement":[{"text":"The main DNA-binding cluster is formed by amino acids R146, R147, K148, and K149. Alanine substitution at these residues reduced binding affinity to ss49 by two orders of magnitude with a change in an apparent Kd from 4.0 ± 1.3 nM to 316 ± 59 nM in the case of N-DBD and from 4.8 ± 0.4 nM to 187 ± 55 nM in the case of PB2-573 (Figure 2).","type":"Results"},{"text":"From these experiments, we concluded that the main DNA binding site is formed by residues 146–149, with a potential minor contribution from other basic amino acids of the N-DBD.","type":"Results"}],"term_comment":"Note that this term is restricted to those cases where the binding is to a single-stranded DNA molecule, not to one of the stands of double-stranded DNA.","term_def":"\"Binding to single-stranded DNA.\" [GOC:elh, GOC:vw, PMID:22976174]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":22,"released":"2026_06","sequence":"MDEPPGKPLSCEEKEKLKEKLAFLKREYSKTLARLQRAQRAEKIKHSIKKTVEEQDCLSQQDLSPQLKHSEPKNKICVYDKLHIKTHLDEETGEKTSITLDVGPESFNPGDGPGGLPIQRTDDTQEHFPHRVSDPSGEQKQKLPSRRKKQQKRTFISQERDCVFGTDSLRLSGKRLKEQEEISSKNPARSPVTEIRTHLLSLKSELPDSPEPVTEINEDSVLIPPTAQPEKGVDTFLRRPNFTRATTVPLQTLSDSGSSQHLEHIPPKGSSELTTHDLKNIRFTSPVSLEAQGKKMTVSTDNLLVNKAISKSGQLPTSSNLEANISCSLNELTYNNLPANENQNLKEQNQTEKSLKSPSDTLDGRNENLQESEILSQPKSLSLEATSPLSAEKHSCTVPEGLLFPAEYYVRTTRSMSNCQRKVAVEAVIQSHLDVKKKGFKNKNKDASKNLNLSNEETDQSEIRMSGTCTGQPSSRTSQKLLSLTKVSSPAGPTEDNDLSRKAVAQAPGRRYTGKRKSACTPASDHCEPLLPTSSLSIVNRSKEEVTSHKYQHEKLFIQVKGKKSRHQKEDSLSWSNSAYLSLDDDAFTAPFHRDGMLSLKQLLSFLSITDFQLPDEDFGPLKLEKVKSCSEKPVEPFESKMFGERHLKEGSCIFPEELSPKRMDTEMEDLEEDLIVLPGKSHPKRPNSQSQHTKTGLSSSILLYTPLNTVAPDDNDRPTTDMCSPAFPILGTTPAFGPQGSYEKASTEVAGRTCCTPQLAHLKDSVCLASDTKQFDSSGSPAKPHTTLQVSGRQGQPTCDCDSVPPGTPPPIESFTFKENQLCRNTCQELHKHSVEQTETAELPASDSINPGNLQLVSELKNPSGSCSVDVSAMFWERAGCKEPCIITACEDVVSLWKALDAWQWEKLYTWHFAEVPVLQIVPVPDVYNLVCVALGNLEIREIRALFCSSDDESEKQVLLKSGNIKAVLGLTKRRLVSSSGTLSDQQVEVMTFAEDGGGKENQFLMPPEETILTFAEVQGMQEALLGTTIMNNIVIWNLKTGQLLKKMHIDDSYQASVCHKAYSEMGLLFIVLSHPCAKESESLRSPVFQLIVINPKTTLSVGVMLYCLPPGQAGRFLEGDVKDHCAAAILTSGTIAIWDLLLGQCTALLPPVSDQHWSFVKWSGTDSHLLAGQKDGNIFVYHYS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.6214165261382799,"dataset":["Cancer-related proteins","NDDs-related proteins"],"disorder_content":0.16441821247892074,"disprot_consensus":{"full":[{"start":1,"end":9,"type":"D"},{"start":10,"end":40,"type":"T"},{"start":41,"end":195,"type":"D"}],"Structural state":[{"start":1,"end":195,"type":"D"}],"Molecular function":[{"start":1,"end":195,"type":"F"}],"Biological process":[{"start":1,"end":194,"type":"F"}],"Structural transition":[{"start":10,"end":40,"type":"T"}]}},{"disprot_id":"DP04327","acc":"G5EET6","creator":"ireményi","date":"2024-11-27T20:08:23.934Z","features":{"pfam":[{"id":"PF01369","name":"Sec7 domain","start":383,"end":534},{"id":"PF15410","name":"Pleckstrin homology domain","start":571,"end":681}],"gene3D":[]},"genes":[{"name":{"value":"efa-6","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"17676955","url":"http://www.ncbi.nlm.nih.gov/pubmed/17676955","alternativeUrl":"https://europepmc.org/abstract/MED/17676955"}},{"code":"ECO:0000312","source":{"name":"WormBase","id":"Y55D9A.1a","url":"https://www.wormbase.org/db/seq/sequence?name=Y55D9A.1a;class=Transcript"}}]},"orfNames":[{"value":"Y55D9A.1","evidences":[{"code":"ECO:0000312","source":{"name":"WormBase","id":"Y55D9A.1a","url":"https://www.wormbase.org/db/seq/sequence?name=Y55D9A.1a;class=Transcript"}}]}]}],"length":818,"name":"Exchange factor for Arf-6","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions":[{"start":59,"end":175,"reference_id":"39305484","reference_source":"pmid","reference_html":"The microtubule regulator EFA-6 forms cortical foci dependent on its intrinsically disordered region and interactions with tubulins. <i> Sandhu A, Lyu X, Wan X, Meng X, Tang NH, Gonzalez G, Syed IN, Chen L, Jin Y, Chisholm AD. </i> Cell Rep, 2024","date":"2026-04-03T21:13:46.492Z","curator_id":"ireményi","curator_name":"István Reményi ","curator_orcid":"0000-0003-4670-2406","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":4,"region_id":"DP04327r003","statement":[{"text":"Purified GFP::EFA-6N or mCh::EFA-6N protein formed spherical droplets in vitro whose size was dependent on concentration (Figures S3D and S3E). Treatment with 1,6-hexanediol, which disrupts multivalent hydrophobic interactions in phase-separated condensates 35, was able to dissolve EFA-6N droplets (Figure S3D).","type":"Results"}],"ec_go":"IDA","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"43078","entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-04-03T21:13:48.775Z"}},{"start":59,"end":175,"reference_id":"39305484","reference_source":"pmid","reference_html":"The microtubule regulator EFA-6 forms cortical foci dependent on its intrinsically disordered region and interactions with tubulins. <i> Sandhu A, Lyu X, Wan X, Meng X, Tang NH, Gonzalez G, Syed IN, Chen L, Jin Y, Chisholm AD. </i> Cell Rep, 2024","date":"2026-04-03T21:13:56.522Z","curator_id":"ireményi","curator_name":"István Reményi ","curator_orcid":"0000-0003-4670-2406","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006067","ec_ontology":"ECO","ec_name":"fluorescence recovery after photobleaching evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"ec_go":"IDA","region_id":"DP04327r009","statement":[{"text":"FRAP analyses on the in vitro EFA-6N droplets revealed a slow and partial recovery of fluorescence within droplets after intra-droplet photobleaching (Figures S3F and S3G).","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-04-03T21:13:58.289Z"}},{"start":59,"end":347,"reference_id":"39305484","reference_source":"pmid","reference_html":"The microtubule regulator EFA-6 forms cortical foci dependent on its intrinsically disordered region and interactions with tubulins. <i> Sandhu A, Lyu X, Wan X, Meng X, Tang NH, Gonzalez G, Syed IN, Chen L, Jin Y, Chisholm AD. </i> Cell Rep, 2024","date":"2026-04-03T21:11:55.149Z","curator_id":"ireményi","curator_name":"István Reményi ","curator_orcid":"0000-0003-4670-2406","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"region_id":"DP04327r012","statement":[{"text":"Under normal culture temperature (20C), tba-1(gf) mutants displayed grossly normal body morphology, movement, and growth rate. However, when cultured at 25C, tba-1(gf) exhibited 100% embryonic lethality (Table S2). As EFA-6 is involved in embryonic cortical MT organization, we assessed whether efa-6 interacted with tba-1(gf) in embryonic development. We found that both efa-6(0) null and efa-6(DIDR1+IDR2) mutations significantly rescued the temperature-sensitive embryonic lethality of tba-1(gf), while the efa-6(DMTED+IDR1) mutation exhibited similar, but weaker, effects (Table S2).\n\n","type":"Results"},{"text":"The percentage of such abnormal embryos was significantly reduced in both\ntba-1(gf); efa-6(0) and tba-1(gf); efa-6(DIDR1+IDR2) (Figure S4E). These findings suggest that loss of EFA-6 function counteracts the effects of TBA-1(gf) on early development, dependent on aberrant condensation of EFA-6 and its IDR.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gly59_Thr347del","start":null,"end":null,"position":null}],"ec_go":"IMP","term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-04-03T21:14:00.972Z"}},{"start":59,"end":347,"reference_id":"39305484","reference_source":"pmid","reference_html":"The microtubule regulator EFA-6 forms cortical foci dependent on its intrinsically disordered region and interactions with tubulins. <i> Sandhu A, Lyu X, Wan X, Meng X, Tang NH, Gonzalez G, Syed IN, Chen L, Jin Y, Chisholm AD. </i> Cell Rep, 2024","date":"2026-04-03T21:06:25.979Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008035","ec_ontology":"ECO","ec_name":"author inference based on intrinsic disorder prediction used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04327r013","statement":[{"text":"EFA-6 N-terminal region also contains a large predicted intrinsically disordered region (IDR) that we divided into IDR1 and IDR2 for simplicity (Figures S2A and S2C).","type":"Results"}]}],"regions_counter":13,"released":"2026_06","sequence":"MAKVASSGAEEALATIDGAPRRNVKKSEAFVMSGDVLISLNRNVSSTYAKLLGDQLPPGTTVASSIHPHQLSRATASAGVSFPSMNRNGAAAQKLSRLPVPVSTSQIERRGSLARKTSEESSPTAIRMLKTAPIERMESTDVEESEEETVMMTTDEKENQKKPNENDDEVMVVDEEQFIVVSNDMKSPNEEIVAKSLRSAMFTMPTDNHHHSYNSSPQISTLSPHLRSNGDGPSRSPVYDDVDDDLNGSLDAKDMSNNSHQQSFRSPENYSEKDTPSKHSVVTIDGSGVSNHYDQDGMFSHVYYSTQDTTPKHGSPSLRKQIFESRTTPNTAASNSSASASPSLHATSESRGATGGVSLRSAESSNLNQTAVPSTSTNSVGGEREAAQIARNLYELKNCTSTQVADRLNEQNEFSFLILVKYLELFQFSTTRIDAALREFLSRVELRGESSARERLLRVFSARYLECNPAIFDSLDEVHTLTCALLLLNSDLHGPNMGKKMTARDFITNIAHTGCTFKREMLKTLFQSIKDNAISLQNSAKNSTANGSVASTSRRQPQQIYEVDPDSVVEYYSGFLMRKYVRETDGGKTPFGRRSWRMVYARLRGLVLYFDTDEHPKATSRYASLENAVSLHHALAEPAPDYKKKSFVFRVRIAHGGEILFQTSNQKELQEWCEKINFVAAAFSSPTLPLPVTSKPETAPMPRLPRIPCLAPITKQLSTHEARVAELNEMIEIVSQSVSPNQPQQLITDRWVLLSFEKRRYSTYINVLRRSLEARKASSATTMNIMMTPTRRQQQNQKPVVSEDRLSYTDAVNGAAAH","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"alphafold_very_low_content":0.49877750611246946,"disorder_content":0.3533007334963325,"disprot_consensus":{"full":[{"start":59,"end":347,"type":"D"}],"Structural state":[{"start":59,"end":347,"type":"D"}],"Molecular function":[{"start":59,"end":347,"type":"F"}]}},{"disprot_id":"DP04328","acc":"P32833","creator":"ireményi","date":"2024-11-27T20:49:40.340Z","features":{"pfam":[{"id":"PF04084","name":"Origin recognition complex subunit 2 RecA-like domain","start":290,"end":480},{"id":"PF24882","name":"ORC2 WHD","start":547,"end":608}],"gene3D":[]},"genes":[{"name":{"value":"ORC2"},"synonyms":[{"value":"RRR1"},{"value":"SIR5"}],"orfNames":[{"value":"YBR0523"}],"olnNames":[{"value":"YBR060C"}]}],"length":620,"name":"Origin recognition complex subunit 2","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":232,"reference_id":"35217664","reference_source":"pmid","reference_html":"A mechanism of origin licensing control through autoinhibition of S. cerevisiae ORC·DNA·Cdc6. <i> Schmidt JM, Yang R, Kumar A, Hunker O, Seebacher J, Bleichert F. </i> Nat Commun, 2022","date":"2025-06-23T17:00:18.255Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7TJF"},{"db":"EMDB","id":"25924"}],"region_id":"DP04328r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P38826"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P50874"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P54791"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P54790"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P54784"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Introduction","text":"Here, we report cryo-EM structures of ARS1-bound S. cerevisiae (Sc) ORC and of the ternary complex with Cdc6 at sub-3 Å resolutions."}]}],"statement":[{"text":"The cryo-EM structures of S. cerevisiae ORC bound to 84 bp ARS1 DNA shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":344,"end":354,"reference_id":"35217664","reference_source":"pmid","reference_html":"A mechanism of origin licensing control through autoinhibition of S. cerevisiae ORC·DNA·Cdc6. <i> Schmidt JM, Yang R, Kumar A, Hunker O, Seebacher J, Bleichert F. </i> Nat Commun, 2022","date":"2025-06-23T17:00:31.411Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7TJF"},{"db":"EMDB","id":"25924"}],"region_id":"DP04328r007","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P38826"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P50874"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P54791"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P54790"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P54784"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Introduction","text":"Here, we report cryo-EM structures of ARS1-bound S. cerevisiae (Sc) ORC and of the ternary complex with Cdc6 at sub-3 Å resolutions."}]}],"statement":[{"text":"The cryo-EM structures of S. cerevisiae ORC bound to 84 bp ARS1 DNA shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":498,"end":620,"reference_id":"35217664","reference_source":"pmid","reference_html":"A mechanism of origin licensing control through autoinhibition of S. cerevisiae ORC·DNA·Cdc6. <i> Schmidt JM, Yang R, Kumar A, Hunker O, Seebacher J, Bleichert F. </i> Nat Commun, 2022","date":"2025-06-23T17:00:43.540Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7TJF"},{"db":"EMDB","id":"25924"}],"region_id":"DP04328r008","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P38826"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P50874"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P54791"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P54790"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P54784"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Introduction","text":"Here, we report cryo-EM structures of ARS1-bound S. cerevisiae (Sc) ORC and of the ternary complex with Cdc6 at sub-3 Å resolutions."}]}],"statement":[{"text":"The cryo-EM structures of S. cerevisiae ORC bound to 84 bp ARS1 DNA shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":176,"end":200,"reference_id":"39271725","reference_source":"pmid","reference_html":"Replication licensing regulated by a short linear motif within an intrinsically disordered region of origin recognition complex. <i> Wu Y, Zhang Q, Lin Y, Lam WH, Zhai Y. </i> Nat Commun, 2024","date":"2025-06-26T15:28:47.158Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003682","term_name":"chromatin binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005640","ec_ontology":"ECO","ec_name":"glutathione S-transferase pull-down assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P33993","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P49736","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04328r009","statement":[{"text":"We found that both Cdt1-Mcm2-7 and OCCM can be pulled down by GST-Orc2N200, but not by GST-Orc2N175 or GST alone (Fig. 5a, b), indicating a direct interaction between Orc2-SH(175-200) and Mcm2-7 containing complexes.","type":"Results"}],"term_comment":"","term_def":"\"Binding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.\" [GOC:jl, ISBN:0198506732, PMID:20404130]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":9,"released":"2025_06","sequence":"MLNGEDFVEHNDILSSPAKSRNVTPKRVDPHGERQLRRIHSSKKNLLERISLVGNERKNTSPDPALKPKTPSKAPRKRGRPRKIQEELTDRIKKDEKDTISSKKKRKLDKDTSGNVNEESKTSNNKQVMEKTGIKEKREREKIQVATTTYEDNVTPQTDDNFVSNSPEPPEPATPSKKSLTTNHDFTSPLKQIIMNNLKEYKDSTSPGKLTLSRNFTPTPVPKNKKLYQTSETKSASSFLDTFEGYFDQRKIVRTNAKSRHTMSMAPDVTREEFSLVSNFFNENFQKRPRQKLFEIQKKMFPQYWFELTQGFSLLFYGVGSKRNFLEEFAIDYLSPKIAYSQLAYENELQQNKPVNSIPCLILNGYNPSCNYRDVFKEITDLLVPAELTRSETKYWGNHVILQIQKMIDFYKNQPLDIKLILVVHNLDGPSIRKNTFQTMLSFLSVIRQIAIVASTDHIYAPLLWDNMKAQNYNFVFHDISNFEPSTVESTFQDVMKMGKSDTSSGAEGAKYVLQSLTVNSKKMYKLLIETQMQNMGNLSANTGPKRGTQRTGVELKLFNHLCAADFIASNEIALRSMLREFIEHKMANITKNNSGMEIIWVPYTYAELEKLLKTVLNTL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.3774193548387097,"disorder_content":0.5903225806451613,"disprot_consensus":{"full":[{"start":1,"end":232,"type":"D"},{"start":344,"end":354,"type":"D"},{"start":498,"end":620,"type":"D"}],"Structural state":[{"start":1,"end":232,"type":"D"},{"start":344,"end":354,"type":"D"},{"start":498,"end":620,"type":"D"}],"Molecular function":[{"start":176,"end":200,"type":"F"}]}},{"disprot_id":"DP04330","acc":"O82089","creator":"ireményi","date":"2024-11-27T22:02:47.674Z","features":{"pfam":[{"id":"PF00403","name":"Heavy-metal-associated domain","start":7,"end":63}],"gene3D":[]},"genes":[{"name":{"value":"CCH"},"orfNames":[{"value":"F18O21.200"}],"olnNames":[{"value":"At3g56240"}]}],"length":121,"name":"Copper transport protein CCH","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":72,"end":121,"reference_id":"39154065","reference_source":"pmid","reference_html":"Structure and dimerization properties of the plant-specific copper chaperone CCH. <i> Dluhosch D, Kersten LS, Schott-Verdugo S, Hoppen C, Schwarten M, Willbold D, Gohlke H, Groth G. </i> Sci Rep, 2024","date":"2026-04-03T20:27:38.683Z","curator_id":"ireményi","curator_name":"István Reményi ","curator_orcid":"0000-0003-4670-2406","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"region_id":"DP04330r001","statement":[{"text":"In contrast, the signals for the C-terminal extension point for an overall unstructured domain, regardless of the addition of copper.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-04-03T20:27:40.356Z"}}],"regions_counter":7,"released":"2026_06","sequence":"MAQTVVLKVGMSCQGCVGAVNRVLGKMEGVESFDIDIKEQKVTVKGNVEPEAVFQTVSKTGKKTSYWPVEAEAEPKAEADPKVETVTETKTEAETKTEAKVDAKADVEPKAAEAETKPSQV","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"alphafold_very_low_content":0.2231404958677686,"disorder_content":0.4132231404958678,"disprot_consensus":{"full":[{"start":72,"end":121,"type":"D"}],"Structural state":[{"start":72,"end":121,"type":"D"}]}},{"disprot_id":"DP04332","acc":"B2CZL6","creator":"ireményi","date":"2024-11-28T10:00:48.453Z","features":{"pfam":[{"id":"PF00201","name":"UDP-glucoronosyl and UDP-glucosyl transferase","start":322,"end":519}],"gene3D":[]},"genes":[],"length":545,"name":"Glycosyltransferase","ncbi_taxon_id":221204,"organism":"Pilosella officinarum","regions":[{"start":1,"end":19,"reference_id":"39059496","reference_source":"pmid","reference_html":"Structural and biochemical basis for regiospecificity of the flavonoid glycosyltransferase UGT95A1. <i> Sirirungruang S, Blay V, Scott YF, Pereira JH, Hammel M, Barnum CR, Adams PD, Shih PM. </i> J Biol Chem, 2024","date":"2026-04-03T19:39:43.777Z","curator_id":"ireményi","curator_name":"István Reményi ","curator_orcid":"0000-0003-4670-2406","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"region_id":"DP04332r001","statement":[{"text":"UGT95A1 likely contains multiple disordered regions (DRs). The apo structure lacks electron density for six regions of amino acids, namely residues 1 to 22 (DR1), 89 to 116 (DR2), 211 to 246 (DR3), 303 to 317 (DR4), 376 to 402 (DR5), and 484 to 494 (DR6), suggesting that up to 25% of the protein may be structurally disordered, flexible, or variable.","type":"Results"},{"text":"Region mentioned by the authors corresponds to the 1-19 residues of the UniProt sequence.","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"9BCM"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-04-03T19:40:19.966Z"}},{"start":86,"end":113,"reference_id":"39059496","reference_source":"pmid","reference_html":"Structural and biochemical basis for regiospecificity of the flavonoid glycosyltransferase UGT95A1. <i> Sirirungruang S, Blay V, Scott YF, Pereira JH, Hammel M, Barnum CR, Adams PD, Shih PM. </i> J Biol Chem, 2024","date":"2026-04-03T19:40:15.343Z","curator_id":"ireményi","curator_name":"István Reményi ","curator_orcid":"0000-0003-4670-2406","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"region_id":"DP04332r002","statement":[{"text":"UGT95A1 likely contains multiple disordered regions (DRs). The apo structure lacks electron density for six regions of amino acids, namely residues 1 to 22 (DR1), 89 to 116 (DR2), 211 to 246 (DR3), 303 to 317 (DR4), 376 to 402 (DR5), and 484 to 494 (DR6), suggesting that up to 25% of the protein may be structurally disordered, flexible, or variable.","type":"Results"},{"text":"Region mentioned by the authors corresponds to the 86-113 residues of the UniProt sequence.","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"9BCM"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-04-03T19:50:41.781Z"}},{"start":208,"end":243,"reference_id":"39059496","reference_source":"pmid","reference_html":"Structural and biochemical basis for regiospecificity of the flavonoid glycosyltransferase UGT95A1. <i> Sirirungruang S, Blay V, Scott YF, Pereira JH, Hammel M, Barnum CR, Adams PD, Shih PM. </i> J Biol Chem, 2024","date":"2026-04-03T19:43:10.298Z","curator_id":"ireményi","curator_name":"István Reményi ","curator_orcid":"0000-0003-4670-2406","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":4,"region_id":"DP04332r003","statement":[{"text":"UGT95A1 likely contains multiple disordered regions (DRs). The apo structure lacks electron density for six regions of amino acids, namely residues 1 to 22 (DR1), 89 to 116 (DR2), 211 to 246 (DR3), 303 to 317 (DR4), 376 to 402 (DR5), and 484 to 494 (DR6), suggesting that up to 25% of the protein may be structurally disordered, flexible, or variable.","type":"Results"},{"text":"Region mentioned by the authors corresponds to the 208-243 residues of the UniProt sequence.","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"9BCM"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-04-03T19:50:41.494Z"}},{"start":300,"end":314,"reference_id":"39059496","reference_source":"pmid","reference_html":"Structural and biochemical basis for regiospecificity of the flavonoid glycosyltransferase UGT95A1. <i> Sirirungruang S, Blay V, Scott YF, Pereira JH, Hammel M, Barnum CR, Adams PD, Shih PM. </i> J Biol Chem, 2024","date":"2026-04-03T19:45:06.053Z","curator_id":"ireményi","curator_name":"István Reményi ","curator_orcid":"0000-0003-4670-2406","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04332r004","statement":[{"text":"UGT95A1 likely contains multiple disordered regions (DRs). The apo structure lacks electron density for six regions of amino acids, namely residues 1 to 22 (DR1), 89 to 116 (DR2), 211 to 246 (DR3), 303 to 317 (DR4), 376 to 402 (DR5), and 484 to 494 (DR6), suggesting that up to 25% of the protein may be structurally disordered, flexible, or variable.","type":"Results"},{"text":"Region mentioned by the authors corresponds to the 300-314 residues of the UniProt sequence.","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"9BCM"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-04-03T19:45:27.577Z"}},{"start":373,"end":399,"reference_id":"39059496","reference_source":"pmid","reference_html":"Structural and biochemical basis for regiospecificity of the flavonoid glycosyltransferase UGT95A1. <i> Sirirungruang S, Blay V, Scott YF, Pereira JH, Hammel M, Barnum CR, Adams PD, Shih PM. </i> J Biol Chem, 2024","date":"2026-04-03T19:46:35.908Z","curator_id":"ireményi","curator_name":"István Reményi ","curator_orcid":"0000-0003-4670-2406","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04332r005","statement":[{"text":"UGT95A1 likely contains multiple disordered regions (DRs). The apo structure lacks electron density for six regions of amino acids, namely residues 1 to 22 (DR1), 89 to 116 (DR2), 211 to 246 (DR3), 303 to 317 (DR4), 376 to 402 (DR5), and 484 to 494 (DR6), suggesting that up to 25% of the protein may be structurally disordered, flexible, or variable.","type":"Results"},{"text":"Region mentioned by the authors corresponds to the 373-399 residues of the UniProt sequence.","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"9BCM"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-04-03T19:50:28.292Z"}},{"start":484,"end":494,"reference_id":"39059496","reference_source":"pmid","reference_html":"Structural and biochemical basis for regiospecificity of the flavonoid glycosyltransferase UGT95A1. <i> Sirirungruang S, Blay V, Scott YF, Pereira JH, Hammel M, Barnum CR, Adams PD, Shih PM. </i> J Biol Chem, 2024","date":"2024-11-28T11:15:42.086Z","curator_id":"ireményi","curator_name":"István Reményi ","curator_orcid":"0000-0003-4670-2406","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04332r006","statement":[{"text":"UGT95A1 likely contains multiple disordered regions (DRs). The apo structure lacks electron density for six regions of amino acids, namely residues 1 to 22 (DR1), 89 to 116 (DR2), 211 to 246 (DR3), 303 to 317 (DR4), 376 to 402 (DR5), and 484 to 494 (DR6), suggesting that up to 25% of the protein may be structurally disordered, flexible, or variable.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-04-03T19:50:30.409Z"}},{"start":1,"end":19,"reference_id":"39059496","reference_source":"pmid","reference_html":"Structural and biochemical basis for regiospecificity of the flavonoid glycosyltransferase UGT95A1. <i> Sirirungruang S, Blay V, Scott YF, Pereira JH, Hammel M, Barnum CR, Adams PD, Shih PM. </i> J Biol Chem, 2024","date":"2026-04-03T19:47:27.194Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"9BCM"}],"region_id":"DP04332r012","statement":[{"text":"UGT95A1 likely contains multiple disordered regions (DRs). The apo structure lacks electron density for six regions of amino acids, namely residues 1 to 22 (DR1), 89 to 116 (DR2), 211 to 246 (DR3), 303 to 317 (DR4), 376 to 402 (DR5), and 484 to 494 (DR6), suggesting that up to 25% of the protein may be structurally disordered, flexible, or variable.","type":"Results"},{"text":"Region mentioned by the authors corresponds to the 1-19 residues of the UniProt sequence.","type":"Curator statement"}]},{"start":302,"end":315,"reference_id":"39059496","reference_source":"pmid","reference_html":"Structural and biochemical basis for regiospecificity of the flavonoid glycosyltransferase UGT95A1. <i> Sirirungruang S, Blay V, Scott YF, Pereira JH, Hammel M, Barnum CR, Adams PD, Shih PM. </i> J Biol Chem, 2024","date":"2026-04-03T20:15:12.306Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0035251","term_name":"UDP-glucosyltransferase activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ala302_Leu305del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Glu304_His309del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ser313_His3015del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04332r013","statement":[{"text":"On the other hand, many deletion variants lacking parts of the DRs in the C-terminal domain (DR4-6; Del 8–13 mutants) showed compromised activity or regiospecificity. Deletions of DR4 (Del 11–12) abolished activity entirely, while the deletion of DR6 (Del 13) severely affected activity (Fig. 5C).","type":"Results"}],"term_comment":"","term_def":"\"Catalysis of the transfer of a glucosyl group from UDP-glucose to an acceptor molecule.\" [PMID:19858195]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46229","entry_name":null}]},{"start":483,"end":489,"reference_id":"39059496","reference_source":"pmid","reference_html":"Structural and biochemical basis for regiospecificity of the flavonoid glycosyltransferase UGT95A1. <i> Sirirungruang S, Blay V, Scott YF, Pereira JH, Hammel M, Barnum CR, Adams PD, Shih PM. </i> J Biol Chem, 2024","date":"2026-04-03T20:18:21.050Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0035251","term_name":"UDP-glucosyltransferase activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ala433Pro489del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04332r014","statement":[{"text":"On the other hand, many deletion variants lacking parts of the DRs in the C-terminal domain (DR4-6; Del 8–13 mutants) showed compromised activity or regiospecificity. Deletions of DR4 (Del 11–12) abolished activity entirely, while the deletion of DR6 (Del 13) severely affected activity (Fig. 5C).","type":"Results"}],"term_comment":"","term_def":"\"Catalysis of the transfer of a glucosyl group from UDP-glucose to an acceptor molecule.\" [PMID:19858195]","term_is_obsolete":false,"term_not_annotate":false},{"start":377,"end":389,"reference_id":"39059496","reference_source":"pmid","reference_html":"Structural and biochemical basis for regiospecificity of the flavonoid glycosyltransferase UGT95A1. <i> Sirirungruang S, Blay V, Scott YF, Pereira JH, Hammel M, Barnum CR, Adams PD, Shih PM. </i> J Biol Chem, 2024","date":"2026-04-03T20:20:09.729Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0035251","term_name":"UDP-glucosyltransferase activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ala433Pro489del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04332r015","statement":[{"text":"Interestingly, DR5 could be significantly shortened by deleting residues 393 to 398 without affecting efficiency (Del 8; Fig. 5C); however, deleting residues 380 to 392 did affect overall activity and regioselectivity (Del 9,10; Fig. 5C).","type":"Results"},{"text":"Reported region adjusted by −3 residues at the N-terminus to match UniProt B2CZL6 canonical sequence, as the authors' construct carries a N-terminal extension.","type":"Curator statement"}],"term_comment":"","term_def":"\"Catalysis of the transfer of a glucosyl group from UDP-glucose to an acceptor molecule.\" [PMID:19858195]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":15,"released":"2026_06","sequence":"MDNETQIKKRKLQTATMEAKATGEIFVVPFFGQGHLFPAMELCKNISAHNYNVTLIIPSHLSSSIPSTFSNHSSFIHVTEISVAASPPPEAADEPGSGTEVRSSGPRGNPLQDQNLQMGKGIKSFLSARSGTRPTCVVIDVMMSWSKEIFVDHEIPVVSFSTSGATASAVGYGMWKAEVGNMKPGEIREIPGLPKEMAVTFADLSRGPQRRIRPPGGPGKSDGRAGPPNRMRSGSRHGPGGGPSPGPGQKPRWVDEVDGSIALLINTCDDLEHVFINYMAEQTKLPVWGVGPLLPEQFWKSAGELLHDHEMRSNHKSNYTEDEVVQWLESKPRESVIYISFGSEVGPTIEEYKELAKALEESDQPFIWVIQPGSGKSGIPRSFLGPAAAHTDDSEEEEGYYPDGLDVTVGNRGLIITGWAPQLLILSHPSTGGFLSHCGWNSTAEAIGRGVPILGWPIRGDQFDNAKLVAYHLKIGHVMSRGANGEVGPGKFTKDDITSGIEKLMKDEKVHKQAKELSKEFEGGFPVSSVKALGAFVEFISQKAT","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","asterids","campanulids","Asterales","Asteraceae","Cichorioideae","Cichorieae","Hieraciinae","Pilosella"],"alphafold_very_low_content":0.14128440366972478,"disorder_content":0.24954128440366974,"disprot_consensus":{"full":[{"start":1,"end":19,"type":"D"},{"start":86,"end":113,"type":"D"},{"start":208,"end":243,"type":"D"},{"start":300,"end":314,"type":"D"},{"start":315,"end":315,"type":"F"},{"start":373,"end":399,"type":"D"},{"start":483,"end":483,"type":"F"},{"start":484,"end":494,"type":"D"}],"Structural state":[{"start":1,"end":19,"type":"D"},{"start":86,"end":113,"type":"D"},{"start":208,"end":243,"type":"D"},{"start":300,"end":314,"type":"D"},{"start":373,"end":399,"type":"D"},{"start":484,"end":494,"type":"D"}],"Disorder function":[{"start":1,"end":19,"type":"F"}],"Molecular function":[{"start":302,"end":315,"type":"F"},{"start":377,"end":389,"type":"F"},{"start":483,"end":489,"type":"F"}]}},{"disprot_id":"DP04337","acc":"O60158","creator":"eficho","date":"2024-11-28T19:47:23.873Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"bqt4"},"orfNames":[{"value":"SPBC19C7.10"}]}],"length":432,"name":"Bouquet formation protein 4","ncbi_taxon_id":284812,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","regions":[{"start":364,"end":413,"reference_id":"38825008","reference_source":"pmid","reference_html":"Disordered region of nuclear membrane protein Bqt4 recruits phosphatidic acid to the nuclear envelope to maintain its structural integrity. <i> Hirano Y, Sato T, Miura A, Kubota Y, Shindo T, Fukase K, Fukagawa T, Kabayama K, Haraguchi T, Hiraoka Y. </i> J Biol Chem, 2024","date":"2025-06-17T19:42:46.373Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0101025","term_name":"nuclear membrane biogenesis","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","region_id":"DP04337r002","statement":[{"text":"Such abnormal vacuoles in the nucleus were located in close proximity to the NE, which is rich in nuclear pore complexes (NPCs) (Fig. 2H, asterisks and Fig. S4 for serial sectioning images). Notably, the nuclear protein did not leak out of the nucleus (Fig. S5), indicating that the NE retained its function as a barrier between the nucleus and the cytoplasm despite its abnormal morphology. The electron-dense patches were distributed over a wide area within the nucleoplasm but were scarcely distributed in the nucleolus (see serial sectioning images in Fig. S4B). Patches were observed in 45 of 50 nuclei overexpressing IDR. ","type":"Results"},{"text":"The atypical structures observed under live fluorescence imaging (Fig. 2E) were preserved without any obvious alterations during fixation for CLEM (Fig. S4A). We found two major abnormalities: a vacuole-like structure covered with a multilayered membrane within the nucleus, and electron-dense patches in the nucleoplasm (Fig. 2H, red and blue arrows, respectively), both of which were not observed in wild-type cells (Fig. 2I).","type":"Results"}],"term_comment":"","term_def":"\"The process in which a nuclear membrane is synthesized, aggregates, and bonds together.\" [GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":null,"id":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:50:32.107Z"}},{"start":364,"end":413,"reference_id":"38825008","reference_source":"pmid","reference_html":"Disordered region of nuclear membrane protein Bqt4 recruits phosphatidic acid to the nuclear envelope to maintain its structural integrity. <i> Hirano Y, Sato T, Miura A, Kubota Y, Shindo T, Fukase K, Fukagawa T, Kabayama K, Haraguchi T, Hiraoka Y. </i> J Biol Chem, 2024","date":"2025-06-17T09:49:36.402Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0051276","term_name":"chromosome organization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006063","ec_ontology":"ECO","ec_name":"over expression analysis evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IMP","region_id":"DP04337r003","statement":[{"text":"Overexpression of the GFP-IDR and GFP-IDR-TM fragments, but not GFP and GFP-KSE, caused dissociation of the centromeres from the NE and their declustering (Fig. 3, A and B).","type":"Results"}],"term_comment":"","term_def":"\"A process that is carried out at the cellular level that results in the assembly, arrangement of constituent parts, or disassembly of chromosomes, structures composed of a very long molecule of DNA and associated proteins that carries hereditary information. This term covers covalent modifications at the molecular level as well as spatial relationships among the major components of a chromosome.\" [GOC:ai, GOC:dph, GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":null,"id":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-17T15:56:02.420Z"}},{"start":364,"end":413,"reference_id":"38825008","reference_source":"pmid","reference_html":"Disordered region of nuclear membrane protein Bqt4 recruits phosphatidic acid to the nuclear envelope to maintain its structural integrity. <i> Hirano Y, Sato T, Miura A, Kubota Y, Shindo T, Fukase K, Fukagawa T, Kabayama K, Haraguchi T, Hiraoka Y. </i> J Biol Chem, 2024","date":"2025-06-17T09:42:42.940Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001226","ec_ontology":"ECO","ec_name":"lipid binding assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"16337","operator":null,"partner_start":null,"partner_end":null},{"db":"ChEBI","id":"28494","operator":"or","partner_start":null,"partner_end":null}],"region_id":"DP04337r004","statement":[{"text":"In this study, we focused on PA in the following experiments because the abnormal membrane proliferation observed with Bqt4 overexpression was similar to that observed in the ned1-deficient phenotype. To confirm the binding of PA to the IDR, we performed a liposome-mediated binding assay. Liposomes with different percentages of PA were prepared and incubated with purified GFP-IDR protein. After isolation of the liposomes via density gradient centrifugation, the proteins bound to the liposomes were electrophoresed and detected using silver staining. GFP-IDR co-sedimented with PA-containing liposomes but not with control liposomes (Fig. 4B). Therefore, we conclude that the IDR region directly binds to PA in vitro.","type":"Results"},{"text":"Because PA and cardiolipin are negatively charged lipids (Fig. 4A), and the IDR region, especially the KSE region, is biased toward a positive charge (Fig. 4C), we assumed that the interaction between PA and the IDR region is mediated via electrostatic interactions.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-17T15:56:14.091Z"}},{"start":372,"end":377,"reference_id":"38825008","reference_source":"pmid","reference_html":"Disordered region of nuclear membrane protein Bqt4 recruits phosphatidic acid to the nuclear envelope to maintain its structural integrity. <i> Hirano Y, Sato T, Miura A, Kubota Y, Shindo T, Fukase K, Fukagawa T, Kabayama K, Haraguchi T, Hiraoka Y. </i> J Biol Chem, 2024","date":"2025-06-17T09:46:47.104Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006067","ec_ontology":"ECO","ec_name":"fluorescence recovery after photobleaching evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","interaction_partner":[{"db":"ChEBI","id":"16337","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04337r005","statement":[{"text":"The FRAP analysis revealed that GFP-ΔKSE and GFP-4KRA moved faster than full-length Bqt4 (GFP-FL) in the INM, suggesting that Bqt4 forms a sub-stable complex with the INM by interacting with PA. To further confirm the electrostatic interaction between the IDR and PA, we generated mutants by scrambling and reversing the amino acid sequences in the KSE region to disturb its electrostatic potential (Fig. S7A). ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys372Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys374Ala","start":null,"end":null,"position":null},{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys375Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg376Ala","start":null,"end":null,"position":null}],"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":null,"id":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-30T23:47:06.547Z"}},{"start":364,"end":413,"reference_id":"38825008","reference_source":"pmid","reference_html":"Disordered region of nuclear membrane protein Bqt4 recruits phosphatidic acid to the nuclear envelope to maintain its structural integrity. <i> Hirano Y, Sato T, Miura A, Kubota Y, Shindo T, Fukase K, Fukagawa T, Kabayama K, Haraguchi T, Hiraoka Y. </i> J Biol Chem, 2024","date":"2025-06-08T20:00:22.161Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","region_id":"DP04337r006","statement":[{"text":"Purified GFP-IDR protein was mixed with an increased concentration of PA, and the mixture was observed using fluorescence microscopy. As shown in Figure 5, A and B, GFP-IDR formed fibrous aggregates in a PA-dependent manner. Consistent with the lipid binding assay results, aggregates were not formed with the neutral phospholipid phosphatidylcholine (PC).","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"64482","entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T21:36:35.341Z"}},{"start":364,"end":413,"reference_id":"38825008","reference_source":"pmid","reference_html":"Disordered region of nuclear membrane protein Bqt4 recruits phosphatidic acid to the nuclear envelope to maintain its structural integrity. <i> Hirano Y, Sato T, Miura A, Kubota Y, Shindo T, Fukase K, Fukagawa T, Kabayama K, Haraguchi T, Hiraoka Y. </i> J Biol Chem, 2024","date":"2025-06-08T20:00:52.919Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006335","ec_ontology":"ECO","ec_name":"fluorescence correlation spectroscopy evidence","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04337r007","statement":[{"text":"To further assess the aggregation state of GFP-IDR, we performed FCS analysis. In the presence of PA, fluorescence intensity fluctuations of approximately 100 kHz were accompanied by strong spike signals for the GFP-IDR (Fig. S9A), most likely originating from large fibrous aggregates observed in Figure 5, A and B passing through the confocal volume. Conversely, in the absence of PA, fluctuations were less than 10 kHz (Fig. S9A, compare inlets for GFP-IDR+PA and control), a range similar to that observed when using GFP instead of GFP-IDR, or PC instead of PA (Fig. S9A). The auto-correlation function (G(τ)), calculated from these fluctuations, showed that GFP-IDR exhibits slower diffusion with PA compared to other combinations (Fig. 5C). These results suggest that GFP-IDR formed microscopically invisible clusters with PA, in addition to large visible aggregates. As the large aggregates were not spherical, they are unlikely to have been formed by liquid-liquid phase separation. We also performed an FRAP assay on GFP-IDR within the aggregates and found that its molecular exchange rate was low (Fig. 5D), suggesting that the aggregates are of a solid phase, not a liquid phase. Collectively, the IDR tended to form a cluster in the presence of PA; ultimately, this cluster transitioned into a large, solid, fibrous aggregate in vitro.","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IDA","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"64482","entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T21:36:27.309Z"}},{"start":364,"end":413,"reference_id":"38825008","reference_source":"pmid","reference_html":"Disordered region of nuclear membrane protein Bqt4 recruits phosphatidic acid to the nuclear envelope to maintain its structural integrity. <i> Hirano Y, Sato T, Miura A, Kubota Y, Shindo T, Fukase K, Fukagawa T, Kabayama K, Haraguchi T, Hiraoka Y. </i> J Biol Chem, 2024","date":"2025-03-17T20:41:02.566Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008035","ec_ontology":"ECO","ec_name":"author inference based on intrinsic disorder prediction used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04337r009","statement":[{"text":"For this purpose, we examined the three-dimensional protein structure around the KSE domain predicted by Alphafold2 (https://alphafold.ebi.ac.uk/entry/O60158) and selected an unstructured region (364–413 aa; Fig. 2A) containing the KSE domain as a candidate. We termed this region as an intrinsically disordered region.","type":"Results"},{"text":" From this prediction, we examined the 340 to 383 aa region which consists of α-helix (340–363 aa) and low complex regions (364–383 aa) (Fig. 1D and red and blue squared regions in Fig. S1A).","type":"Results"}]},{"start":364,"end":383,"reference_id":"38825008","reference_source":"pmid","reference_html":"Disordered region of nuclear membrane protein Bqt4 recruits phosphatidic acid to the nuclear envelope to maintain its structural integrity. <i> Hirano Y, Sato T, Miura A, Kubota Y, Shindo T, Fukase K, Fukagawa T, Kabayama K, Haraguchi T, Hiraoka Y. </i> J Biol Chem, 2024","date":"2025-03-18T15:07:22.879Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0071763","term_name":"nuclear membrane organization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Lys364_Gln383del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04337r010","statement":[{"text":"Upon thiamine addition, GFP–GST–NLS severely leaked from the nucleus of ΔKSE mutant-expressing cells, but not from the nucleus of FL-expressing cells (Fig. 1, G and H), indicating NE rupture in the ΔKSE mutant-expressing cells. These results suggest that the KSE domain is vital for NE maintenance.","type":"Results"}],"term_comment":"","term_def":"\"A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nuclear inner or outer membrane.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"The ΔKSE mutant was expressed in lem2-shut-off bqt4Δ S. pombe cells."}]}]},{"start":364,"end":413,"reference_id":"38825008","reference_source":"pmid","reference_html":"Disordered region of nuclear membrane protein Bqt4 recruits phosphatidic acid to the nuclear envelope to maintain its structural integrity. <i> Hirano Y, Sato T, Miura A, Kubota Y, Shindo T, Fukase K, Fukagawa T, Kabayama K, Haraguchi T, Hiraoka Y. </i> J Biol Chem, 2024","date":"2025-03-18T15:40:05.780Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005635","term_name":"nuclear envelope","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IDA","region_id":"DP04337r011","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Peptide was expressed in lem2-shut-off bqt4Δ S. pombe cells."}]}],"statement":[{"text":"The IDR fragment of Bqt4 tagged with GFP (GFP-IDR) was localized to the NE despite the absence of TM and nucleoplasm under suppressive expression conditions (Fig. 2B, +thiamine).","type":"Results"}],"term_comment":"","term_def":"\"The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space).\" [ISBN:0198547684]","term_is_obsolete":false,"term_not_annotate":false},{"start":364,"end":413,"reference_id":"38825008","reference_source":"pmid","reference_html":"Disordered region of nuclear membrane protein Bqt4 recruits phosphatidic acid to the nuclear envelope to maintain its structural integrity. <i> Hirano Y, Sato T, Miura A, Kubota Y, Shindo T, Fukase K, Fukagawa T, Kabayama K, Haraguchi T, Hiraoka Y. </i> J Biol Chem, 2024","date":"2025-03-18T17:01:19.063Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006998","term_name":"nuclear envelope organization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006063","ec_ontology":"ECO","ec_name":"over expression analysis evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IMP","region_id":"DP04337r012","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Peptide was expressed in lem2-shut-off bqt4Δ S. pombe cells."}]}],"statement":[{"text":"When GFP-IDR was overexpressed in S. pombe cells under the control of the nmt1 promoter, its overexpression resulted in severe growth defects in the spot assay (Fig. 2D). These results indicate that the overexpression of IDR, but not KSE, confers dominant-negative effects on cell growth and suggest that the IDR domain is substantial for NE maintenance, causing loss-of-function and dominant-negative effects.","type":"Results"}],"term_comment":"","term_def":"\"A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nuclear envelope.\" [GOC:dph, GOC:ems, GOC:jl, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":364,"end":413,"reference_id":"38825008","reference_source":"pmid","reference_html":"Disordered region of nuclear membrane protein Bqt4 recruits phosphatidic acid to the nuclear envelope to maintain its structural integrity. <i> Hirano Y, Sato T, Miura A, Kubota Y, Shindo T, Fukase K, Fukagawa T, Kabayama K, Haraguchi T, Hiraoka Y. </i> J Biol Chem, 2024","date":"2025-03-18T16:56:31.566Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0072766","term_name":"centromere clustering at the mitotic interphase nuclear envelope","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006063","ec_ontology":"ECO","ec_name":"over expression analysis evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IMP","region_id":"DP04337r013","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Peptide was expressed S. pombe cells."}]}],"statement":[{"text":"Overexpression of the GFP-IDR and GFP-IDR-TM fragments, but not GFP and GFP-KSE, caused dissociation of the centromeres from the NE and their declustering (Fig. 3, A and B).","type":"Results"},{"text":"Time-lapse observation of the cells overexpressing IDR-TM revealed that aberrant nuclear membrane expansion occurred just after mitosis; subsequently, the clustered centromeres started to dissociate from the NE and then declustered (Fig. 3C and Movie S1). Consequently, the chromosome was missegregated during the next mitosis (Fig. 3C).","type":"Results"},{"text":"Overexpression of the IDR region disturbs centromere clustering.","type":"Figure"}],"term_comment":"","term_def":"\"The process in which chromatin, or kinetochores are anchored to the nuclear envelope. This process involves the microtubule cytoskeleton, and nuclear tethering factors and is responsible for the Rabl-like configuration of chromosomes in the interphase nuclei.\" [GOC:mah, GOC:vw, PMID:21965289, PMID:23166349]","term_is_obsolete":false,"term_not_annotate":false},{"start":364,"end":413,"reference_id":"38825008","reference_source":"pmid","reference_html":"Disordered region of nuclear membrane protein Bqt4 recruits phosphatidic acid to the nuclear envelope to maintain its structural integrity. <i> Hirano Y, Sato T, Miura A, Kubota Y, Shindo T, Fukase K, Fukagawa T, Kabayama K, Haraguchi T, Hiraoka Y. </i> J Biol Chem, 2024","date":"2025-03-18T17:41:52.256Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0097035","term_name":"regulation of membrane lipid distribution","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006063","ec_ontology":"ECO","ec_name":"over expression analysis evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IMP","region_id":"DP04337r014","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Peptide was expressed in S. pombe cells."}]}],"statement":[{"text":" These results suggested that Bqt4 collects PA-enriched membranes to the NE via its IDR domain. In IDR-overexpressing cells, GFP-IDR was localized in both the nucleoplasm and cytoplasm (Fig. 6A, IDR). Consequently, the PA sensor was redistributed from the nucleus to the cytoplasm (Fig. 6A; IDR). In contrast, KSE overexpression did not alter the localization of the PA sensor, although this fragment was localized in the cytoplasm, similar to IDR (Fig. 6A, KSE). Therefore, we conclude that IDR, but not KSE, controls intracellular PA localization depending on its localization and protein levels in S. pombe cells. ","type":"Results"},{"text":"Overexpression of IDR disturbs intracellular lipid distribution.","type":"Figure"}],"term_comment":"","term_def":"\"Any process that modulates the proportions or spatial arrangement of lipids in a cellular membrane.\" [GOC:mah, PMID:18441123, PMID:20823909]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":14,"released":"2025_06","sequence":"MTENEKSRSLPAERNPLYKDDTLDHTPLIPKCRAQVIEFPDGPATFVRLKCTNPESKVPHFLMRMAKDSSISATSMFRSAFPKATQEEEDLEMRWIRDNLNPIEDKRVAGLWVPPADALALAKDYSMTPFINALLEASSTPSTYATPSRPTAQKSETSEGEPESSTSATTTSVARRTRQRLAEHLENSKKTILQHDNKEEDKEIHSEENETKDEIKSEKKEPEIKKQEGGSSTEKVGQPSSSDDKAKGSTSKDQPSEEEEKTSDIQDRKIKTPIKPSLLGKIRSSVNKGMTDVASQVNRGMTDVASQVNKGVNGVASQVNKGMNGVANQVNKGVTGVASQVRKPVGKLEKKFENLEKSIGDTLKSSIRSSPKSKKRSREDFEENEDYNAMVPVKRSRITKLESEVYYEKRKVRALGGIAIGLGVGAILPFLF","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"alphafold_very_low_content":0.3333333333333333,"disorder_content":0.11574074074074074,"disprot_consensus":{"full":[{"start":364,"end":413,"type":"D"}],"Structural state":[{"start":364,"end":413,"type":"D"}],"Biological process":[{"start":364,"end":413,"type":"F"}],"Molecular function":[{"start":364,"end":413,"type":"F"}],"Cellular component":[{"start":364,"end":413,"type":"F"}]}},{"disprot_id":"DP04339","acc":"Q9FGJ3","creator":"eficho","date":"2024-11-29T08:55:36.411Z","features":{"pfam":[{"id":"PF00808","name":"Histone-like transcription factor (CBF/NF-Y) and archaeal histone","start":31,"end":95}],"gene3D":[]},"genes":[{"name":{"value":"NFYB2","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11250072","url":"http://www.ncbi.nlm.nih.gov/pubmed/11250072","alternativeUrl":"https://europepmc.org/abstract/MED/11250072"}}]},"synonyms":[{"value":"HAP3B","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9662544","url":"http://www.ncbi.nlm.nih.gov/pubmed/9662544","alternativeUrl":"https://europepmc.org/abstract/MED/9662544"}}]}],"orfNames":[{"value":"MNJ7.23","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"BAB09090.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAB09090.1"}}]}],"olnNames":[{"value":"At5g47640","evidences":[{"code":"ECO:0000312","source":{"name":"Araport","id":"AT5G47640","url":""}}]}]}],"length":190,"name":"Nuclear transcription factor Y subunit B-2","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions":[{"start":167,"end":190,"reference_id":"39567828","reference_source":"pmid","reference_html":"Molecular condensation of the CO/NF-YB/NF-YC/FT complex gates floral transition in Arabidopsis. <i> Huang X, Ma Z, He D, Han X, Liu X, Dong Q, Tan C, Yu B, Sun T, Nordenskiöld L, Lu L, Miao Y, Hou X. </i> EMBO J, 2025","date":"2026-04-03T13:41:09.732Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008035","ec_ontology":"ECO","ec_name":"author inference based on intrinsic disorder prediction used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04339r008","statement":[{"text":"Protein sequence intrinsically disordered prediction of NF-YC family members in Arabidopsis thaliana was performed using the IUPRED2A algorithm. ","type":"Supplementary material"},{"text":"The combination of the authors predictions with AlphaFold and Mobidb-Lite predictions, suggest this region is disordered.","type":"Curator statement"},{"text":"In contrast, highly intrinsically disordered NF-YB2 exhibited typical liquid-liquid phase separation by forming spherical droplets in a protein concentration- and ionic strength-dependent manner.","type":"Results"}]}],"regions_counter":8,"released":"2026_06","sequence":"MGDSDRDSGGGQNGNNQNGQSSLSPREQDRFLPIANVSRIMKKALPANAKISKDAKETMQECVSEFISFVTGEASDKCQKEKRKTINGDDLLWAMTTLGFEDYVEPLKVYLQRFREIEGERTGLGRPQTGGEVGEHQRDAVGDGGGFYGGGGGMQYHQHHQFLHQQNHMYGATGGGSDSGGGAASGRTRT","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"alphafold_very_low_content":0.2631578947368421,"disorder_content":0.12631578947368421,"disprot_consensus":{"full":[{"start":167,"end":190,"type":"D"}],"Structural state":[{"start":167,"end":190,"type":"D"}]}},{"disprot_id":"DP04340","acc":"P17433","creator":"vnugnes","date":"2024-12-02T15:08:02.972Z","features":{"pfam":[{"id":"PF00178","name":"Ets-domain","start":171,"end":255}],"gene3D":[]},"genes":[{"name":{"value":"Spi1"},"synonyms":[{"value":"Sfpi-1","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"1985210","url":"http://www.ncbi.nlm.nih.gov/pubmed/1985210","alternativeUrl":"https://europepmc.org/abstract/MED/1985210"}}]},{"value":"Sfpi1"}]}],"length":272,"name":"Transcription factor PU.1","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":1,"end":170,"reference_id":"38267599","reference_source":"pmid","reference_html":"Structural mechanism of synergistic targeting of the CX3CR1 nucleosome by PU.1 and C/EBPα. <i> Lian T, Guan R, Zhou BR, Bai Y. </i> Nat Struct Mol Biol, 2024","date":"2024-12-02T15:23:07.037Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"8EVH"},{"db":"EMDB","id":"28629"}],"region_id":"DP04340r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q16778"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P68431"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62805"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q16777"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting 162-bp DNA from the CX3CR1 enhancer loci, with sequence 5'-TAGGTGCAGGGCCTCTCGGCTGCTGATCTTCAGCTGGTTGCTGAGAGTTGCAGCATTGCTGAGTCTTAGCAATGGATACTTCCCGATTCCCCTCACAAAAATAGGTCAGTCTGTCTGGCTAGTTCTGTACTTGCAGACACAGGGCATGTGGGGTTCCTATTT"}]}],"statement":[{"text":"The N-terminal regions of both proteins that are involved in interactions with other factors are intrinsically disordered26,27.","type":"Article"},{"text":"The Cryo-EM structure shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-12-10T15:30:33.311Z"}},{"start":260,"end":272,"reference_id":"38267599","reference_source":"pmid","reference_html":"Structural mechanism of synergistic targeting of the CX3CR1 nucleosome by PU.1 and C/EBPα. <i> Lian T, Guan R, Zhou BR, Bai Y. </i> Nat Struct Mol Biol, 2024","date":"2024-12-02T15:22:53.202Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"8EVH"},{"db":"EMDB","id":"28629"}],"region_id":"DP04340r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q16778"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P68431"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P62805"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q16777"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting 162-bp DNA from the CX3CR1 enhancer loci, with sequence 5'-TAGGTGCAGGGCCTCTCGGCTGCTGATCTTCAGCTGGTTGCTGAGAGTTGCAGCATTGCTGAGTCTTAGCAATGGATACTTCCCGATTCCCCTCACAAAAATAGGTCAGTCTGTCTGGCTAGTTCTGTACTTGCAGACACAGGGCATGTGGGGTTCCTATTT"}]}],"statement":[{"text":"The N-terminal regions of both proteins that are involved in interactions with other factors are intrinsically disordered26,27.","type":"Article"},{"text":"The Cryo-EM structure shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2024-12-10T15:30:27.510Z"}}],"regions_counter":2,"released":"2025_06","sequence":"MLQACKMEGFSLTAPPSDDLVTYDSELYQRPMHDYYSFVGSDGESHSDHYWDFSAHHVHNNEFENFPENHFTELQSVQPPQLQQLYRHMELEQMHVLDTPMVPPHTGLSHQVSYMPRMCFPYQTLSPAHQQSSDEEEGERQSPPLEVSDGEADGLEPGPGLLHGETGSKKKIRLYQFLLDLLRSGDMKDSIWWVDKDKGTFQFSSKHKEALAHRWGIQKGNRKKMTYQKMARALRNYGKTGEVKKVKKKLTYQFSGEVLGRGGLAERRLPPH","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"alphafold_very_low_content":0.3713235294117647,"disorder_content":0.6727941176470589,"disprot_consensus":{"full":[{"start":1,"end":170,"type":"D"},{"start":260,"end":272,"type":"D"}],"Structural state":[{"start":1,"end":170,"type":"D"},{"start":260,"end":272,"type":"D"}]}},{"disprot_id":"DP04341","acc":"P08551","creator":"tcordero","date":"2024-12-11T10:18:13.761Z","features":{"pfam":[{"id":"PF00038","name":"Intermediate filament protein","start":89,"end":400},{"id":"PF04732","name":"Intermediate filament head (DNA binding) region","start":9,"end":88}],"gene3D":[]},"genes":[{"name":{"value":"Nefl"},"synonyms":[{"value":"Nf68"},{"value":"Nfl"}]}],"length":543,"name":"Neurofilament light polypeptide","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":440,"end":543,"reference_id":"38358563","reference_source":"pmid","reference_html":"From isolated polyelectrolytes to star-like assemblies: the role of sequence heterogeneity on the statistical structure of the intrinsically disordered neurofilament-low tail domain. <i> Kravikass M, Koren G, Saleh OA, Beck R. </i> Eur Phys J E Soft Matter, 2024","date":"2024-12-20T08:13:56.115Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04341r001","statement":[{"text":"SAXS measurements of WT and ΔN42 at different salinity (Cs). a For increasing Cs, the WT variant shows increased small-angle scattering, a signature for aggregation. In contrast, ΔN42 remains structurally intrinsically disordered as Cs vary.","type":"Figure"},{"text":"The ΔN42 variant remains disordered and unchanged with salinity, while the WT variant shows a hump at low q, typical for a collapse region. ","type":"Figure"},{"text":"In contrast, ΔN42 shows a separated Gaussian polymer profile (Figs. 1a, S1), nearly insensitive to total salinity (Cs=20-520 mM). Similarly, the data presented in Kratky format (qI2 vs. q, Fig. 1a) show the ΔN42 has the signature of a disordered polymer. ","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":150,"db":"ChEBI","id":"26710","entry_name":"sodium chloride"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-01-23T13:53:28.872Z"}},{"start":399,"end":439,"reference_id":"38358563","reference_source":"pmid","reference_html":"From isolated polyelectrolytes to star-like assemblies: the role of sequence heterogeneity on the statistical structure of the intrinsically disordered neurofilament-low tail domain. <i> Kravikass M, Koren G, Saleh OA, Beck R. </i> Eur Phys J E Soft Matter, 2024","date":"2024-12-17T11:59:20.669Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"GO:0042802","term_name":"identical protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04341r002","statement":[{"text":"Using synchrotron small-angle x-ray scattering, we find that the uncharged domain of the NFLt induces attractive interactions that cause it to self-assemble into star-like polymer brushes.","type":"Abstract"},{"text":"We found that the sequence heterogeneity differentiates between the structures of the entire WT NFLt and a variant lacking the N-terminal domain. In particular, the WT variant self-assembles into star-like structures, while the ΔN42 one remains isolated in all measured cases.","type":"Discussion"}],"ec_go":"EXP","term_comment":"","term_def":"\"Binding to an identical protein or proteins.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-19T15:01:11.254Z"}},{"start":399,"end":439,"reference_id":"38358563","reference_source":"pmid","reference_html":"From isolated polyelectrolytes to star-like assemblies: the role of sequence heterogeneity on the statistical structure of the intrinsically disordered neurofilament-low tail domain. <i> Kravikass M, Koren G, Saleh OA, Beck R. </i> Eur Phys J E Soft Matter, 2024","date":"2024-12-17T11:54:37.455Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP04341r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":150,"db":"ChEBI","id":"26710","statements":[{"type":"Figure","text":"WT measurements are in 20 mM Tris pH 8.0 with 0, 150, 250, and 500 mM added NaCl (from bottom to top)."}],"entry_name":"sodium chloride"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":250,"db":"ChEBI","id":"26710","entry_name":"sodium chloride"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":500,"db":"ChEBI","id":"26710","entry_name":"sodium chloride"}],"statement":[{"text":"Fig. 1 SAXS measurements of WT and ΔN42 at different salinity (Cs). a For increasing Cs, the WT variant shows increased small-angle scattering, a signature for aggregation.","type":"Figure"},{"text":"With increasing Cs, the hump at the lower q range becomes a sharper peak accompanied by a scattering rise at the higher q range. Such behavior indicates that the aggregation coexists with the WT variant’s highly dynamic and disordered regions.","type":"Figure"},{"text":"Dominantly at the low wave-vector (q) region, the WT variant scattering (I) rises with added NaCl salt. Such an increase at low q implies high molecular mass particles due to aggregation of the WT variant.","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2024-12-19T15:01:11.525Z"}},{"start":398,"end":543,"reference_id":"37459524","reference_source":"pmid","reference_html":"Intramolecular structural heterogeneity altered by long-range contacts in an intrinsically disordered protein. <i> Koren G, Meir S, Holschuh L, Mertens HDT, Ehm T, Yahalom N, Golombek A, Schwartz T, Svergun DI, Saleh OA, Dzubiella J, Beck R. </i> Proc Natl Acad Sci U S A, 2023","date":"2024-12-17T11:51:42.394Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04341r004","statement":[{"text":"All measurements are conducted in the presence of a 20 mM Tris, pH 8.0, to fully deprotonate the histidine residue. All S segments and the full NFLt are validated to be fully disordered by circular dichroism (SI Appendix, Fig. S4). ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-01-23T13:53:30.306Z"}},{"start":399,"end":439,"reference_id":"38358563","reference_source":"pmid","reference_html":"From isolated polyelectrolytes to star-like assemblies: the role of sequence heterogeneity on the statistical structure of the intrinsically disordered neurofilament-low tail domain. <i> Kravikass M, Koren G, Saleh OA, Beck R. </i> Eur Phys J E Soft Matter, 2024","date":"2024-12-20T08:11:54.520Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"GO:0045107","term_name":"intermediate filament polymerization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP04341r005","statement":[{"text":"Such SAXS resembles that of self-assembled decorated spherical micelles [36]. Variations of micelle models are shown to fit the data (Figs. 1, S4–S6). Sufficiently low aggregation number and core size distill the description of the spherical micelle into a ‘star-like’ brush.","type":"Results"},{"text":"a Schematic of the system’s structure variation with salinity (Cs). While ΔN42 remains disordered and segregated, the WT variant aggregates to a star-like polymer with a higher aggregation number at higher Cs.","type":"Figure"}],"term_comment":"","term_def":"\"Assembly of intermediate filaments by the addition of component monomers to a filament. Polymerization of intermediate filament proteins results from interactions among several distinct binding sites on the constituent proteins. Nuclear lamin head-to-tail polymers arise from one such interaction. Deletion analysis localized the binding sites to the ends of the rod domain that are highly conserved among all intermediate filament proteins. Data indicate that one type of interaction in intermediate filament protein polymerization is the longitudinal binding of dimers via the conserved end segments of the coiled-coil rod domain.\" [GOC:mah, PMID:8776884]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-01-23T13:53:27.191Z"}},{"start":398,"end":543,"reference_id":"37459524","reference_source":"pmid","reference_html":"Intramolecular structural heterogeneity altered by long-range contacts in an intrinsically disordered protein. <i> Koren G, Meir S, Holschuh L, Mertens HDT, Ehm T, Yahalom N, Golombek A, Schwartz T, Svergun DI, Saleh OA, Dzubiella J, Beck R. </i> Proc Natl Acad Sci U S A, 2023","date":"2024-12-20T09:17:07.911Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04341r006","statement":[{"text":"(A) Kratky plot of the SAXS measurements. Each line color is a different S segment (which is 20 amino acids long). The Kratky plot indicates that all segments are unfolded as Iq2/I0 intensity diverges at large q.","type":"Figure"},{"text":"Overall, the result by both SAXS and trFRET shows that the NFLt consists of intramolecular structural heterogeneity—different domains within the IDP occupy space differently, although all display disorder properties.","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-01-23T13:53:31.982Z"}}],"regions_counter":6,"released":"2025_06","sequence":"MSSFGYDPYFSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGSLMPSLENLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRSTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRLSFTSVGSITSGYSQSSQVFGRSAYSGLQSSSYLMSARSFPAYYTSHVQEEQTEVEETIEATKAEEAKDEPPSEGEAEEEEKEKEEGEEEEGAEEEEAAKDESEDTKEEEEGGEGEEEDTKESEEEEKKEESAGEEQVAKKKD","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"alphafold_very_low_content":0.35543278084714547,"disorder_content":0.26887661141804786,"disprot_consensus":{"full":[{"start":398,"end":543,"type":"D"}],"Structural state":[{"start":398,"end":543,"type":"D"}],"Molecular function":[{"start":399,"end":439,"type":"F"}],"Biological process":[{"start":399,"end":439,"type":"F"}]}},{"disprot_id":"DP04343","acc":"P0DOW4","creator":"xcastro","date":"2025-01-22T14:55:16.933Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"Dsup","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"27649274","url":"http://www.ncbi.nlm.nih.gov/pubmed/27649274","alternativeUrl":"https://europepmc.org/abstract/MED/27649274"}}]},"orfNames":[{"value":"RvY_17224","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"27649274","url":"http://www.ncbi.nlm.nih.gov/pubmed/27649274","alternativeUrl":"https://europepmc.org/abstract/MED/27649274"}}]}]}],"length":445,"name":"Damage suppressor protein","ncbi_taxon_id":947166,"organism":"Ramazzottius varieornatus","regions":[{"start":1,"end":445,"reference_id":"39358423","reference_source":"pmid","reference_html":"Structural study of the intrinsically disordered tardigrade damage suppressor protein (Dsup) and its complex with DNA. <i> Zarubin M, Murugova T, Ryzhykau Y, Ivankov O, Uversky VN, Kravchenko E. </i> Sci Rep, 2024","date":"2025-01-22T15:02:15.485Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04343r001","statement":[{"text":"In the Kratky plot, the scattering curves do not have the bell shape, inherent to globular proteins, but instead continuously increase with increasing of scattering vector q (Fig. 4b). Such type of scattering curves is characteristic for non-globular, flexible and disordered proteins, therefore further we described Dsup structure in terms of the Gaussian (random) coil suitable for IDPs.","type":"Results"},{"text":"The Flory`s coefficient ν for Dsup in all types of used solutions is far from the values corresponding to the globular state of proteins (νglobular = 0.33). In case of PBS, the ν is close to 0.5, which corresponds to a random coil structure.","type":"Results"},{"text":"The pair distance distribution function P(r) is Fourier transform of the small angle scattering profile and represents the distribution function of distances inside the particle, thus it describes the shape and dimensions of this particle. The P(r) functions for Dsup are asymmetric with a tailing profile for the longer distances that indicates a rather elongated shape of Dsup (Fig. 5).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-01-23T13:51:21.672Z"}},{"start":1,"end":445,"reference_id":"39358423","reference_source":"pmid","reference_html":"Structural study of the intrinsically disordered tardigrade damage suppressor protein (Dsup) and its complex with DNA. <i> Zarubin M, Murugova T, Ryzhykau Y, Ivankov O, Uversky VN, Kravchenko E. </i> Sci Rep, 2024","date":"2025-01-22T15:05:46.230Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04343r002","statement":[{"text":"Circular dichroism (CD) spectroscopy was applied for the determination of secondary structure content of Dsup in PBS and H2O under native conditions and in presence of chemical denaturant (urea 4.5 M) (Fig. 8).","type":"Results"},{"text":"The results obtained for Dsup in PBS and H2O indicate the presence of disordered regions (62–66%), α-helixes (5–7%) and β-sheets (30–31%) (Table 2).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-01-23T13:51:25.025Z"}},{"start":1,"end":445,"reference_id":"39358423","reference_source":"pmid","reference_html":"Structural study of the intrinsically disordered tardigrade damage suppressor protein (Dsup) and its complex with DNA. <i> Zarubin M, Murugova T, Ryzhykau Y, Ivankov O, Uversky VN, Kravchenko E. </i> Sci Rep, 2024","date":"2025-01-22T15:08:03.316Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP04343r003","statement":[{"text":"Differential CD spectra were obtained for the range of wavelength as the difference between spectra of Dsup-DNA complex and the sum of spectra of Dsup and DNA components (Fig. 8b). A slight signal shift (< 5%) indicates insignificant transitions in the secondary structure of the Dsup protein upon binding with dsDNA. Based on the consistent content of disordered regions in the free Dsup protein and DNA-bound Dsup protein, the Dsup/DNA complex was classified as a fuzzy complex.","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-01-23T13:51:28.768Z"}}],"regions_counter":8,"released":"2025_06","sequence":"MASTHQSSTEPSSTGKSEETKKDASQGSGQDSKNVTVTKGTGSSATSAAIVKTGGSQGKDSSTTAGSSSTQGQKFSTTPTDPKTFSSDQKEKSKSPAKEVPSGGDSKSQGDTKSQSDAKSSGQSQGQSKDSGKSSSDSSKSHSVIGAVKDVVAGAKDVAGKAVEDAPSIMHTAVDAVKNAATTVKDVASSAASTVAEKVVDAYHSVVGDKTDDKKEGEHSGDKKDDSKAGSGSGQGGDNKKSEGETSGQAESSSGNEGAAPAKGRGRGRPPAAAKGVAKGAAKGAAASKGAKSGAESSKGGEQSSGDIEMADASSKGGSDQRDSAATVGEGGASGSEGGAKKGRGRGAGKKADAGDTSAEPPRRSSRLTSSGTGAGSAPAAAKGGAKRAASSSSTPSNAKKQATGGAGKAAATKATAAKSAASKAPQNGAGAKKKGGKAGGRKRK","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Tardigrada","Eutardigrada","Parachela","Hypsibioidea","Ramazzottiidae","Ramazzottius"],"alphafold_very_low_content":0.550561797752809,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":445,"type":"D"}],"Structural state":[{"start":1,"end":445,"type":"D"}],"Molecular function":[{"start":1,"end":445,"type":"F"}]}},{"disprot_id":"DP04344","acc":"Q7BTX0","creator":"vnugnes","date":"2025-01-31T17:11:34.320Z","features":{"pfam":[{"id":"PF05932","name":"Tir chaperone protein (CesT) family","start":7,"end":119}],"gene3D":[]},"genes":[{"name":{"value":"sycH","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAC62591.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAC62591.1"}}]},"synonyms":[{"value":"Y0082","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAC69820.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAC69820.1"}}]}],"olnNames":[{"value":"YPCD1.95c","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAB54972.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAB54972.1"}}]}]}],"length":141,"name":"YopH targeting protein","ncbi_taxon_id":632,"organism":"Yersinia pestis","regions":[{"start":121,"end":141,"reference_id":"15333930","reference_source":"pmid","reference_html":"Structure of the Yersinia pestis type III secretion chaperone SycH in complex with a stable fragment of YscM2. <i> Phan J, Tropea JE, Waugh DS. </i> Acta Crystallogr D Biol Crystallogr, 2004","date":"2025-01-31T17:17:49.846Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"1TTW"}],"region_id":"DP04344r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q93KQ4"}],"statement":[{"text":"The final model included residues 3–120 of SycH and 33–50 of YscM2. Despite the high temperature factors, the structure of SycH was quite well resolved. However, side chains could only be assigned to the helical portion of YscM2. The remainder of this polypeptide was poorly ordered in the crystal.","type":"Results"},{"text":"The three C-terminal residues of SycH (139–141) were also efficiently removed by thermolysin in this experiment. Therefore, all SycH expression vectors were subsequently designed to produce residues 1–138.","type":"Results"}]},{"start":121,"end":141,"reference_id":"15333930","reference_source":"pmid","reference_html":"Structure of the Yersinia pestis type III secretion chaperone SycH in complex with a stable fragment of YscM2. <i> Phan J, Tropea JE, Waugh DS. </i> Acta Crystallogr D Biol Crystallogr, 2004","date":"2025-01-31T17:24:39.975Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04344r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q93KQ4"}],"statement":[{"text":"The final model included residues 3–120 of SycH and 33–50 of YscM2. Despite the high temperature factors, the structure of SycH was quite well resolved. However, side chains could only be assigned to the helical portion of YscM2. The remainder of this polypeptide was poorly ordered in the crystal.","type":"Results"},{"text":"The three C-terminal residues of SycH (139–141) were also efficiently removed by thermolysin in this experiment. Therefore, all SycH expression vectors were subsequently designed to produce residues 1–138.","type":"Results"}]}],"regions_counter":2,"released":"2025_06","sequence":"MRTYSSLLEEFATELGLEEIETNELGHGAVTIDKIWVVHLAPINEKELVAFMRAGILTGQSQLYDILRKNLFSPLSGVIRCALDKDDHWLLWSQLNINDTSGTQLASVLTSLVDKAVTLSCEPTMKKEEDDHRPSSSHLLV","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"],"alphafold_very_low_content":0.11347517730496454,"disorder_content":0.14893617021276595,"disprot_consensus":{"full":[{"start":121,"end":141,"type":"D"}],"Structural state":[{"start":121,"end":141,"type":"D"}],"Disorder function":[{"start":121,"end":141,"type":"F"}]}},{"disprot_id":"DP04347","acc":"P28360","creator":"eficho","date":"2025-02-20T09:58:06.017Z","features":{"pfam":[{"id":"PF00046","name":"Homeodomain","start":173,"end":229}],"gene3D":[]},"genes":[{"name":{"value":"MSX1","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:7391","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:7391"}}]},"synonyms":[{"value":"HOX7","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"1685479","url":"http://www.ncbi.nlm.nih.gov/pubmed/1685479","alternativeUrl":"https://europepmc.org/abstract/MED/1685479"}}]}]}],"length":303,"name":"Homeobox protein MSX-1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":172,"reference_id":"39843447","reference_source":"pmid","reference_html":"PRMT1-methylated MSX1 phase separates to control palate development. <i> Meng L, Jiang Y, You J, Chen Y, Guo S, Chen L, Ma J. </i> Nat Commun, 2025","date":"2025-03-20T17:20:58.380Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008035","ec_ontology":"ECO","ec_name":"author inference based on intrinsic disorder prediction used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04347r011","statement":[{"text":"VL3 in PONDR analysis revealed that the RD-containing N-terminal region in MSX1 is a largely unfolded IDR (Fig. 1A and Supplementary Fig. 1A)20.","type":"Results"},{"text":"AlphaFold prediction also agrees with this region being disordered. Authors refer to this region as IDR throughout the text.","type":"Curator statement"}]}],"regions_counter":11,"released":"2025_06","sequence":"MAPAADMTSLPLGVKVEDSAFGKPAGGGAGQAPSAAAATAAAMGADEEGAKPKVSPSLLPFSVEALMADHRKPGAKESALAPSEGVQAAGGSAQPLGVPPGSLGAPDAPSSPRPLGHFSVGGLLKLPEDALVKAESPEKPERTPWMQSPRFSPPPARRLSPPACTLRKHKTNRKPRTPFTTAQLLALERKFRQKQYLSIAERAEFSSSLSLTETQVKIWFQNRRAKAKRLQEAELEKLKMAAKPMLPPAAFGLSFPLGGPAAVAAAAGASLYGASGPFQRAALPVAPVGLYTAHVGYSMYHLT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.2739273927392739,"disorder_content":0.5676567656765676,"disprot_consensus":{"full":[{"start":1,"end":172,"type":"D"}],"Structural state":[{"start":1,"end":172,"type":"D"}]}},{"disprot_id":"DP04348","acc":"Q96PD5","creator":"eficho","date":"2025-02-20T12:37:50.159Z","features":{"pfam":[{"id":"PF01510","name":"N-acetylmuramoyl-L-alanine amidase","start":406,"end":533}],"gene3D":[]},"genes":[{"name":{"value":"PGLYRP2"},"synonyms":[{"value":"PGLYRPL"},{"value":"PGRPL"}],"orfNames":[{"value":"UNQ3103/PRO10102"}]}],"length":576,"name":"N-acetylmuramoyl-L-alanine amidase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":164,"end":208,"reference_id":"39946201","reference_source":"pmid","reference_html":"PGLYRP2 drives hepatocyte-intrinsic innate immunity by trapping and clearing hepatitis B virus. <i> Li Y, Ma H, Zhang Y, He T, Li B, Ren H, Feng J, Sheng J, Li K, Qian Y, Wang Y, Zhao H, He J, Li H, Wu H, Yao Y, Shi M. </i> J Clin Invest, 2025","date":"2025-04-22T11:29:51.832Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006323","ec_ontology":"ECO","ec_name":"fluorescence microscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04348r002","statement":[{"text":"The fluorescence of FAM-Enh II puncta recovered slowly after photobleaching\n(Fig. 3F), indicating that PGLYRP2, by inducing phase separation involving HBV DNA, likely sequesters the viral DNA from cellular machinery, thereby potentially obstructing its role in viral replication (Fig. 3G).","type":"Results"},{"text":"Purified DsRed-tagged PGLYRP2IDR/209–377\ntriggers the formation of membraneless condensates that colocalize\nwith HBV DNA FAM–Enh II. Meanwhile, condensates induced by\nDsRed-tagged PGLYRP2IDR do not include HBV DNA FAM–Enh\nII, suggesting that phase separation induced by PGLYRP2IDR might\nunderpin the viral suppression function of PGLYRP2209–377 (Figure\n3E). ","type":"Results"}],"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IDA","term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-02T14:49:01.836Z"}},{"start":164,"end":208,"reference_id":"39946201","reference_source":"pmid","reference_html":"PGLYRP2 drives hepatocyte-intrinsic innate immunity by trapping and clearing hepatitis B virus. <i> Li Y, Ma H, Zhang Y, He T, Li B, Ren H, Feng J, Sheng J, Li K, Qian Y, Wang Y, Zhao H, He J, Li H, Wu H, Yao Y, Shi M. </i> J Clin Invest, 2025","date":"2025-03-20T16:26:30.930Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008035","ec_ontology":"ECO","ec_name":"author inference based on intrinsic disorder prediction used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04348r003","statement":[{"text":"The intrinsically disordered region (IDR) of PGLYRP2, predicted using PONDR, spans amino acids 164-208 and is adjacent to the PGLYRP2209-377 20 domain (Fig. 3D).","type":"Results"},{"text":"AlphaFold prediction and MobiDB predictions also agree with this region being disordered.","type":"Curator statement"}]}],"regions_counter":3,"released":"2025_06","sequence":"MAQGVLWILLGLLLWSDPGTASLPLLMDSVIQALAELEQKVPAAKTRHTASAWLMSAPNSGPHNRLYHFLLGAWSLNATELDPCPLSPELLGLTKEVARHDVREGKEYGVVLAPDGSTVAVEPLLAGLEAGLQGRRVINLPLDSMAAPWETGDTFPDVVAIAPDVRATSSPGLRDGSPDVTTADIGANTPDATKGCPDVQASLPDAKAKSPPTMVDSLLAVTLAGNLGLTFLRGSQTQSHPDLGTEGCWDQLSAPRTFTLLDPKASLLTMAFLNGALDGVILGDYLSRTPEPRPSLSHLLSQYYGAGVARDPGFRSNFRRQNGAALTSASILAQQVWGTLVLLQRLEPVHLQLQCMSQEQLAQVAANATKEFTEAFLGCPAIHPRCRWGAAPYRGRPKLLQLPLGFLYVHHTYVPAPPCTDFTRCAANMRSMQRYHQDTQGWGDIGYSFVVGSDGYVYEGRGWHWVGAHTLGHNSRGFGVAIVGNYTAALPTEAALRTVRDTLPSCAVRAGLLRPDYALLGHRQLVRTDCPGDALFDLLRTWPHFTATVKPRPARSVSKRSRREPPPRTLPATDLQ","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.21006944444444445,"disorder_content":0.078125,"disprot_consensus":{"full":[{"start":164,"end":208,"type":"D"}],"Structural state":[{"start":164,"end":208,"type":"D"}],"Molecular function":[{"start":164,"end":208,"type":"F"}]}},{"disprot_id":"DP04349","acc":"Q8N114","creator":"eficho","date":"2025-02-21T14:28:53.920Z","features":{"pfam":[{"id":"PF13908","name":"Shisa, N-terminal domain","start":29,"end":72},{"id":"PF27717","name":"Shisa-5 N-terminal domain","start":106,"end":143}],"gene3D":[]},"genes":[{"name":{"value":"SHISA5"},"synonyms":[{"value":"SCOTIN"}],"orfNames":[{"value":"PSEC0133"}]}],"length":240,"name":"Protein shisa-5","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":126,"end":240,"reference_id":"37816329","reference_source":"pmid","reference_html":"Intrinsically disordered region-mediated condensation of IFN-inducible SCOTIN/SHISA-5 inhibits ER-to-Golgi vesicle transport. <i> Kim N, Kim TH, Kim C, Lee JE, Kang MG, Shin S, Jung M, Kim JS, Mun JY, Rhee HW, Park SY, Shin Y, Yoo JY. </i> Dev Cell, 2023","date":"2025-03-20T14:28:59.434Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008035","ec_ontology":"ECO","ec_name":"author inference based on intrinsic disorder prediction used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04349r003","statement":[{"text":" However, structure prediction by the AlphaFold program indicated that the PRD of SCOTIN does not have a strong structural signature36 (Figure 4D). Instead, it was intrinsically disordered, as illustrated by computational predictions for the unstructured low complexity of proteins (Figure 4E).","type":"Results"},{"text":"(D) AlphaFold predicted structure of SCOTIN. Orange color indicates unstructured residues.","type":"Figure"},{"text":"(E) Prediction of the IDR from five different predictors in the D2P2 resource.37 The threshold for all predictors except protein disorder prediction server (PrDOS) (threshold for PrDOS is shown as dotted line) is 0.5 (bold line). Gray box indicates the region of 150–177.","type":"Figure"}]},{"start":126,"end":240,"reference_id":"37816329","reference_source":"pmid","reference_html":"Intrinsically disordered region-mediated condensation of IFN-inducible SCOTIN/SHISA-5 inhibits ER-to-Golgi vesicle transport. <i> Kim N, Kim TH, Kim C, Lee JE, Kang MG, Shin S, Jung M, Kim JS, Mun JY, Rhee HW, Park SY, Shin Y, Yoo JY. </i> Dev Cell, 2023","date":"2025-03-20T14:53:56.035Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IMP","region_id":"DP04349r004","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"statement":[{"text":"The puncta-like structure of SCOTIN disappeared when SCOTIN(ΔPRD)-expressing cells were tested (Figure 4B). In contrast, overexpression of the SCOTIN(PRD) or SCOTIN(TMPRD) was sufficient to induce the formation of the puncta structure, indicating that the PRD of SCOTIN was needed to assemble this puncta structure (Figures 4B, 4C, S4A, and S4B).","type":"Results"},{"text":"These results together indicate that the intrinsically disordered region (IDR) of SCOTIN possesses the ability to form punctate structures in cells.","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false},{"start":150,"end":177,"reference_id":"37816329","reference_source":"pmid","reference_html":"Intrinsically disordered region-mediated condensation of IFN-inducible SCOTIN/SHISA-5 inhibits ER-to-Golgi vesicle transport. <i> Kim N, Kim TH, Kim C, Lee JE, Kang MG, Shin S, Jung M, Kim JS, Mun JY, Rhee HW, Park SY, Shin Y, Yoo JY. </i> Dev Cell, 2023","date":"2025-03-20T14:47:56.368Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001161","ec_ontology":"ECO","ec_name":"chimeric protein phenotypic evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"To verify whether the PRD is capable of inducing puncta structure while it is attached to the membrane, we tested a chimeric Sec61β-SCOTIN(PRD)-mEmerald construct (Figure 4H). In this construct, the PRD of SCOTIN was attached to the cytosolic side of the integral ER protein Sec61β. "}]},{"term_id":"IDPO:00479","term_name":"protein fragment (indexed by UniProt)","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Results","text":"To verify whether the PRD is capable of inducing puncta structure while it is attached to the membrane, we tested a chimeric Sec61β-SCOTIN(PRD)-mEmerald construct (Figure 4H). In this construct, the PRD of SCOTIN was attached to the cytosolic side of the integral ER protein Sec61β."}]}],"ec_go":"IMP","region_id":"DP04349r005","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"statement":[{"text":"Overexpressed Sec61β-mEmerald was detected in the tubular ER, without any evident puncta. Upon addition of SCOTIN(PRD), but not the PRD(Δ150–177), distinct punctate structures of sphere shape clearly appeared (Figures 4H and 4I).","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false},{"start":150,"end":177,"reference_id":"37816329","reference_source":"pmid","reference_html":"Intrinsically disordered region-mediated condensation of IFN-inducible SCOTIN/SHISA-5 inhibits ER-to-Golgi vesicle transport. <i> Kim N, Kim TH, Kim C, Lee JE, Kang MG, Shin S, Jung M, Kim JS, Mun JY, Rhee HW, Park SY, Shin Y, Yoo JY. </i> Dev Cell, 2023","date":"2025-03-20T14:53:44.536Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006049","ec_ontology":"ECO","ec_name":"genetic transformation evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IMP","region_id":"DP04349r006","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"statement":[{"text":"To further assess whether condensation occurs under endogenous protein levels as well as ectopic overexpression, a tet-ON SCOTIN-MYC cell line was generated in the SCOTIN KO and stimulated with doxycycline to reach a SCOTIN-MYC protein level similar to that of endogenous SCOTIN (Figure 4J). SCOTIN-MYC formed puncta under this condition (Figures 4K and 4L). In contrast, SCOTIN(Δ150–177)-MYC was diffusely localized when it was expressed at endogenous levels (Figures 4K and 4L).","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false},{"start":126,"end":240,"reference_id":"37816329","reference_source":"pmid","reference_html":"Intrinsically disordered region-mediated condensation of IFN-inducible SCOTIN/SHISA-5 inhibits ER-to-Golgi vesicle transport. <i> Kim N, Kim TH, Kim C, Lee JE, Kang MG, Shin S, Jung M, Kim JS, Mun JY, Rhee HW, Park SY, Shin Y, Yoo JY. </i> Dev Cell, 2023","date":"2025-03-20T14:59:36.031Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007056","ec_ontology":"ECO","ec_name":"differential interference contrast microscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","region_id":"DP04349r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46793","entry_name":"poly(ethylene glycol)"}],"statement":[{"text":"Under a physiological salt concentration and neutral pH, purified SCOTIN(PRD) assembled into droplets with the aid of the molecular crowding agent polyethylene glycol (PEG)-8000 (Figure 6D). The formation of SCOTIN(PRD) droplets depended on the protein concentration and pH (Figure 6E). SCOTIN(PRD) droplets coalesced into larger droplets without any energy source (Figure S5B).","type":"Results"},{"text":"SCOTIN condensates exhibit liquid- to gel-like properties","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false},{"start":150,"end":177,"reference_id":"37816329","reference_source":"pmid","reference_html":"Intrinsically disordered region-mediated condensation of IFN-inducible SCOTIN/SHISA-5 inhibits ER-to-Golgi vesicle transport. <i> Kim N, Kim TH, Kim C, Lee JE, Kang MG, Shin S, Jung M, Kim JS, Mun JY, Rhee HW, Park SY, Shin Y, Yoo JY. </i> Dev Cell, 2023","date":"2025-03-20T15:01:52.403Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140693","term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Thr150_Tyr177del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04349r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46793","entry_name":"poly(ethylene glycol)"}],"statement":[{"text":"Moreover, the SCOTIN(PRDΔ150–177) protein did not form droplets when tested under the same conditions (Figure 6D), confirming that residues 150–177 within the PRD of SCOTIN govern its ability to form condensates.","type":"Results"},{"text":"SCOTIN condensates exhibit liquid- to gel-like properties","type":"Results"}],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_is_obsolete":false,"term_not_annotate":false},{"start":150,"end":177,"reference_id":"37816329","reference_source":"pmid","reference_html":"Intrinsically disordered region-mediated condensation of IFN-inducible SCOTIN/SHISA-5 inhibits ER-to-Golgi vesicle transport. <i> Kim N, Kim TH, Kim C, Lee JE, Kang MG, Shin S, Jung M, Kim JS, Mun JY, Rhee HW, Park SY, Shin Y, Yoo JY. </i> Dev Cell, 2023","date":"2025-03-20T15:12:44.418Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0060628","term_name":"regulation of ER to Golgi vesicle-mediated transport","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Thr150_Tyr177del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04349r009","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"statement":[{"text":"As expected, ER-to-Golgi transport was significantly delayed by overexpression of SCOTIN but not by SCOTIN(Δ150–177) or Sec61β (Figures 7B and 7C), suggesting that the ability of SCOTIN to form condensates is required to exert an inhibitory effect.","type":"Results"},{"text":"The inhibitory effect of SCOTIN on VSV-G trafficking was separately confirmed using the EndoH assay. It distinguishes the fractional abundance of EndoH-sensitive (on ER) or Endo H-resistant (within Golgi or beyond) forms (Figure 7D). In empty vector- or Sec61β-overexpressing control cells, the EndoH-resistant VSV-G protein appeared with biotin treatment, suggesting its proper transport to the Golgi. In SCOTIN-expressing but not SCOTIN(Δ150–177)-expressing cells, the EndoH-resistant VSV-G protein was not increased, again confirming that the inhibition of vesicle transport by SCOTIN requires the ability of SCOTIN to form condensates.","type":"Results"},{"text":"Intrinsically disordered region-mediated condensation of IFN-inducible SCOTIN/SHISA-5 inhibits ER-to-Golgi vesicle transport","type":"Title"}],"term_comment":"","term_def":"\"Any process that modulates the rate, frequency, or extent of ER to Golgi vesicle-mediated transport, the directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi.\" [GOC:dph, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false},{"start":150,"end":177,"reference_id":"37816329","reference_source":"pmid","reference_html":"Intrinsically disordered region-mediated condensation of IFN-inducible SCOTIN/SHISA-5 inhibits ER-to-Golgi vesicle transport. <i> Kim N, Kim TH, Kim C, Lee JE, Kang MG, Shin S, Jung M, Kim JS, Mun JY, Rhee HW, Park SY, Shin Y, Yoo JY. </i> Dev Cell, 2023","date":"2025-03-20T15:18:07.323Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0090111","term_name":"regulation of COPII vesicle uncoating","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Thr150_Tyr177del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04349r010","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"statement":[{"text":"Condensation is required for the ER-to-Golgi transport delay and the disassembly of COPII by SCOTIN","type":"Figure"},{"text":"Finally, we verified whether SCOTIN condensates inhibit COPII-mediated vesicle formation from the ER membrane using in vitro budding assays (Figure 7H). The inhibition of COPII budding by SCOTIN was not observed after SCOTIN(Δ150–177) overexpression. These results together suggest that SCOTIN condensates preferentially recruit Sec31 and interfere with COPII vesicle formation on the ER membrane, thereby delaying transport from the ER to the Golgi.","type":"Results"}],"term_comment":"","term_def":"\"Any process that modulates the frequency, rate or extent of COPII vesicle uncoating, the process in which COPII vesicle coat proteins are disassembled, and released.\" [GOC:ascb_2009, GOC:dph, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false},{"start":150,"end":177,"reference_id":"39946235","reference_source":"pmid","reference_html":"Membrane-tethered SCOTIN condensates elicit an endoplasmic reticulum stress response by sequestering luminal BiP. <i> Jo A, Jung M, Mun JY, Kim YJ, Yoo JY. </i> Cell Rep, 2025","date":"2025-03-20T15:35:38.143Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1900103","term_name":"positive regulation of endoplasmic reticulum unfolded protein response","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Thr150_Tyr177del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04349r011","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"statement":[{"text":"Based on these results, we concluded that the ability of SCOTIN to condense on the ER is essential for activation of the UPR.","type":"Results"},{"text":"In contrast to SCOTIN-MYC overexpression, SCOTIN(Δ150–177)-MYC overexpression barely induced the UPR (Figure 2A).","type":"Results"},{"text":"Significantly fewer IRE1 foci were detected in SCOTIN(Δ150–177)-MYC-overexpressing cells than in SCOTIN-MYC-overexpressing cells, confirming that SCOTIN(Δ150–177)-MYC overexpression barely induces IRE1 oligomerization or the UPR (Figures 2B and 2C).","type":"Results"},{"text":"SCOTIN condensation is critical for inducing ER stress","type":"Results"}],"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of endoplasmic reticulum unfolded protein response.\" [GOC:TermGenie]","term_is_obsolete":false,"term_not_annotate":false},{"start":126,"end":240,"reference_id":"39946235","reference_source":"pmid","reference_html":"Membrane-tethered SCOTIN condensates elicit an endoplasmic reticulum stress response by sequestering luminal BiP. <i> Jo A, Jung M, Mun JY, Kim YJ, Yoo JY. </i> Cell Rep, 2025","date":"2025-03-20T16:00:45.474Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1905898","term_name":"positive regulation of response to endoplasmic reticulum stress","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000315","ec_ontology":"ECO","ec_name":"mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Thr150_Tyr177del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04349r012","statement":[{"text":"The most significant differences in ER stress activation were observed with the Δ150–177 mutant (Figure 6H). In all cases (C1, C2, and C3), the addition of the Δ150–177 mutation led to a marked reduction in both XBP1 and CHOP production, confirming that SCOTIN condensation via the cytosolic PRD is essential for BiP sequestration and induction of ER stress responses.","type":"Results"},{"text":"Our data thus far demonstrate that cytosolic condensation of the SCOTIN PRD results in the transduction of signals to the luminal side of the ER, resulting in the sequestration of BiP within SCOTIN condensates, ultimately triggering the ER stress response.","type":"Results"},{"text":"We thus sought to determine whether the mere presence of the 150–177 aa is sufficient to induce ER stress. To investigate this possibility, we generated mutant constructs by adding the 150–177 aa to the SCOTIN(ΔPRD) or SCOTIN(1–149) mutant, neither of which could induce ER stress (Figures 7A–7C).","type":"Results"},{"text":"Although adding 150–177 aa to the SCOTIN(ΔPRD) mutant resulted in a slight increase in the proportion of cells expressing F-XBP1ΔDBD-Venus, it was insufficient for full restoration to a proportion comparable to that observed among cells expressing full-length SCOTIN (Figures 7B and S4A).","type":"Results"},{"text":"These data suggest that the intrinsic activity of the entire PRD of SCOTIN is necessary for activating the ER stress response.","type":"Results"}],"term_comment":"","term_def":"\"Any process that activates or increases the frequency, rate or extent of response to endoplasmic reticulum stress.\" [GO_REF:0000058, GOC:aruk, GOC:bc, GOC:TermGenie, PMID:21803450]","term_is_obsolete":false,"term_not_annotate":false,"sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}]}],"regions_counter":12,"released":"2025_06","sequence":"MTAPVPAPRILLPLLLLLLLTPPPGARGEVCMASRGLSLFPESCPDFCCGTCDDQYCCSDVLKKFVWSEERCAVPEASVPASVEPVEQLGSALRFRPGYNDPMSGFGATLAVGLTIFVLSVVTIIICFTCSCCCLYKTCRRPRPVVTTTTSTTVVHAPYPQPPSVPPSYPGPSYQGYHTMPPQPGMPAAPYPMQYPPPYPAQPMGPPAYHETLAGGAAAPYPASQPPYNPAYMDAPKAAL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.3375,"dataset":[],"disorder_content":0.4791666666666667,"disprot_consensus":{"full":[{"start":126,"end":240,"type":"D"}],"Structural state":[{"start":126,"end":240,"type":"D"}],"Molecular function":[{"start":126,"end":240,"type":"F"}],"Biological process":[{"start":126,"end":240,"type":"F"}]}},{"disprot_id":"DP04352","acc":"A0A564ZT73","creator":"viglesias","date":"2025-03-18T09:11:33.319Z","features":{"pfam":[{"id":"PF00847","name":"AP2 domain","start":416,"end":468},{"id":"PF00847","name":"AP2 domain","start":619,"end":668},{"id":"PF14733","name":"AP2-coincident C-terminal","start":61,"end":139}],"gene3D":[]},"genes":[{"orfNames":[{"value":"PVP01_0807400","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"VUZ95203.1","url":"https://www.ebi.ac.uk/ena/browser/view/VUZ95203.1"}}]}]}],"length":1397,"name":"AP2 domain transcription factor AP2-I, putative","ncbi_taxon_id":5855,"organism":"Plasmodium vivax","regions":[{"start":29,"end":56,"reference_id":"39820027","reference_source":"pmid","reference_html":"Structural characterization of the ACDC domain from ApiAP2 proteins, a potential molecular target against apicomplexan parasites. <i> Le Berre M, Tubiana T, Reuterswärd Waldner P, Lazar N, Li de la Sierra-Gallay I, Santos JM, Llinás M, Nessler S. </i> Acta Crystallogr D Struct Biol, 2025","date":"2025-03-18T09:20:51.214Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"8RWU"}],"region_id":"DP04352r001","statement":[{"text":"Again, no electron density was observed for the N- and C-terminal extensions (residues 30–60 and 150–230, respectively).","type":"Results"},{"text":"Modified boundaries as missing residues in the deposited structure correspond to 29-56.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-18T14:57:05.176Z"}},{"start":148,"end":229,"reference_id":"39820027","reference_source":"pmid","reference_html":"Structural characterization of the ACDC domain from ApiAP2 proteins, a potential molecular target against apicomplexan parasites. <i> Le Berre M, Tubiana T, Reuterswärd Waldner P, Lazar N, Li de la Sierra-Gallay I, Santos JM, Llinás M, Nessler S. </i> Acta Crystallogr D Struct Biol, 2025","date":"2025-03-18T09:22:49.991Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"8RWU"}],"region_id":"DP04352r002","statement":[{"text":"Again, no electron density was observed for the N- and C-terminal extensions (residues 30–60 and 150–230, respectively).","type":"Results"},{"text":"Modified boundaries as missing residues in the deposited structure correspond to 148-229.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-03-18T14:57:04.828Z"}}],"regions_counter":2,"released":"2025_06","sequence":"MEALTTDKDMSIKNEERNENGTDLLIGLASLNEHEGEVAYDKKEDAEISMHMNEQDKLDVPSLVEICKQQLIVILKDMCADSNSSDEKASFMYHLNRLRSAVTVVDLHNYIAVFGPCLSYNKLPSTWNISVCDYLKQQLNILRAADSQQSSSNHVSYLELHNDYEDIIHDKKGNATTTASNSMQGNMNSNNLNSQLSMKGSSIHMNSANSTSNVSGNATGNASGHISINAEGGNLGCFTLGDHEDSNIVEDYYDCLMRTNLSDDSPNCLKYMMNSKNDSLSNTEVENVISYLKKYEVKANKNYCSLEEELKYSKDSDFEYQEDYLKDKTLYDSDLDDNNLFDSNLISSSRNMNDSGSSMMNMNLSIPNSGSANNNNSNNLSGKNYNMKYDSMKKNNSDVMNTWTRACTEGHPEYLPRIPGVRFNPKKQQWLAAWNDNTREIRRYFSVKQYGFEQARILAVKARQEAEKAGARCKPMFHVHGRKTVDSAANEAMKNNNDMGMEDGTMGNNNMGGSGVGGSMGMMSGSGNNASHAGTNAAMNSGGMSTGGTHEHMNKKDHLKNENNKGIKRGRGRPPKRKLSEDSQLSLDDMEQTLCRNGENADLMEAIDSFDKNCTRPMKGVSYNDRKGSWLAYWSIGKNFQMRRFPIKKLGFEKAKELAIQCRLEAEQAGATTTENRTKRIRNLLTMNSENTMDVMMDMNSLDPEDNLNDTNKNMNGNMIMSQMHHHYNAHGMNNNNNMHPNKMPHSDCQESENDYSPTKRTRAPRGRRMESLTARASALTPVEGVRFDPYSYSWFAKYLENENSKEPKISKYLLKKWGFNKAHSLAVHTVKCAYKAVPFTDEELINIFNVDSKNLMNNQNSLMNLAFKDTYGNNAGANGNAYNANNYGAMGVSSSANGALMGNMGYMNGAMGGAVGMDHVVGGMPIGGVSGVSGGNFAQSMGAYKGGVNAHGIMNSMGNSGGEKNADMGNMNDEETTIGNGSSNNANNMLSGMDGANGMLNSVEGANNMNAASKMGIMNGCAYNYSGGSSAVNDSAGGAVAGAGAATVGAATVGAATVGAATVGAAGQNNFHHGGLLPNSGIVVGAGLGENNVNGPSSMKGNATIANGVNVYMNEQMGLGANYSGKSFPSGEVLVAPGTSSAMMDDENPKVLNKAHLMESSNGAGNNAGGSVLQNSSVDNYLVVSECVLNNNNRKVGGAHVGNKTIGGAAAAAAAAFGHHHMEDPAVVGVVRLNEMHMNAENDINANQSNTQYGIASTGSNMNMNAEPVMSKAMVNSASGSVNLGTNKDSTGSIMEGRDVLDNSRGAEHPLEQRKFVNIMNESGNIDSGVSGVSGDSGANSSYANNNPYGPNAGANFNSYDGENAGAANMIGSNANELNESSMYYMSVKPEIKTEQ","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Plasmodium)"],"disorder_content":0.07874015748031496,"disprot_consensus":{"full":[{"start":29,"end":56,"type":"D"},{"start":148,"end":229,"type":"D"}],"Structural state":[{"start":29,"end":56,"type":"D"},{"start":148,"end":229,"type":"D"}]}},{"disprot_id":"DP04353","acc":"Q8IJW6","creator":"viglesias","date":"2025-03-18T09:23:42.405Z","features":{"pfam":[{"id":"PF00847","name":"AP2 domain","start":523,"end":575},{"id":"PF00847","name":"AP2 domain","start":775,"end":824},{"id":"PF14733","name":"AP2-coincident C-terminal","start":62,"end":140}],"gene3D":[]},"genes":[{"orfNames":[{"value":"PF3D7_1007700","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CZT98326.1","url":"https://www.ebi.ac.uk/ena/browser/view/CZT98326.1"}}]}]}],"length":1597,"name":"AP2 domain transcription factor AP2-I","ncbi_taxon_id":36329,"organism":"Plasmodium falciparum (isolate 3D7)","regions":[{"start":1,"end":48,"reference_id":"39820027","reference_source":"pmid","reference_html":"Structural characterization of the ACDC domain from ApiAP2 proteins, a potential molecular target against apicomplexan parasites. <i> Le Berre M, Tubiana T, Reuterswärd Waldner P, Lazar N, Li de la Sierra-Gallay I, Santos JM, Llinás M, Nessler S. </i> Acta Crystallogr D Struct Biol, 2025","date":"2026-05-08T20:38:29.210Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"8RXO"}],"region_id":"DP04353r001","statement":[{"text":"AlphaFold2 proposed confident models for the core ACDC domain of PfAP2-I (residues 60–150), but the N-terminal extension was predicted to be fully disordered.","type":"Results"},{"text":"Electron density could only be observed for the core ACDC domain, confirming that the N-terminal extension is disordered, at least in this truncated fragment of the protein.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-08T20:39:06.272Z"}},{"start":1,"end":48,"reference_id":"39820027","reference_source":"pmid","reference_html":"Structural characterization of the ACDC domain from ApiAP2 proteins, a potential molecular target against apicomplexan parasites. <i> Le Berre M, Tubiana T, Reuterswärd Waldner P, Lazar N, Li de la Sierra-Gallay I, Santos JM, Llinás M, Nessler S. </i> Acta Crystallogr D Struct Biol, 2025","date":"2026-05-08T20:39:02.898Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"8RXO"}],"region_id":"DP04353r002","statement":[{"text":"AlphaFold2 proposed confident models for the core ACDC domain of PfAP2-I (residues 60–150), but the N-terminal extension was predicted to be fully disordered.","type":"Results"},{"text":"Electron density could only be observed for the core ACDC domain, confirming that the N-terminal extension is disordered, at least in this truncated fragment of the protein.","type":"Results"}]}],"regions_counter":2,"released":"2026_06","sequence":"METLVNERDINIKNENSKDNNKEMMIGMSHMNHDDQDLIYEKKDDIESLRLHYTDQEKLDVPSLVEICKQQLIVILKDMCSDCSTTDEKTSFLYHLNRLRSAVTVVDLHNYIAVFGPCLSYNKLPSTWNISVCDYLKQQLNILRAADSQQNANNNNNNNNNNNNSNNNNNNNNNNNNNNNNNNNNNNNNNYLNYYDINNEYDEIMSDKKFLGINNFTHVNLSNNANGNYNNITNHANANANPTTSHSNIKGNSHLSNANNAMNYLYSDQDNVVDDYYDCLMRTKLTEETPNSLKYMINLKNETLSNAEFESVLSYLKKYEMKSSKGMNKNHLEDDNGMVKYNNNNNNNNSNNNNNNNNNISNNISNNKDCDEYDYQEEYLKDKALYDSDMDENTNQLHNNEHHTNQHHANVHHHKHQNQHLKQLIDHNNMINNNDNNIINNNNNYLINNMDNNNIDANNNNNNNNNNNNNINNLSHLIHNNMNNNSTLINRNHLIKSERIKKGDVGTTTWTKSTTEGHPEYLPRIPGVRFNPKKQQWLAAWNDNTREIRRYFSVKQYGFEQARILAVKARQEAEKAGARCKPMFHVHGSRKAVDAAITNDLLRSEMEENFNNMHMNHNNNNNNNNNNQHHHQNNNSNIHHNNHHMHNMNLNINPNHLGHNMSHNMNHNYNNNNNNMYINNNINNNNNNNNNNSNSNNNNNNNNIGNDVIHRKETVKVEIKGVKRGRGRPPKRKLSEESQMLLDDMEQTLCRNNNDNMELLECMEAYDKDCSRPMKGVSYNDRKGSWLAYWSIGKNFQMRRFPIKKLGFEKAKELAIQCRLEAEQAGATTTENRTKRMRNLLTLNSENALEMMIDQNSIDNDDSNIHQHMKEKGGGMNGNLRMSRMQNYAGAGISGQSVHQTNKLLNSDAGQDSENEFSPTKRTRAPRGRRMESLTARASALTPVEGVRFDPYSYSWFAKYLENENSKEPKISKYLLKKWGFNKAHSLAVHTVKCAYKAVPFTDEELVNIFNVDVNNLINNQNNMINLGFHDGFGTNGLMKTQLNNQMTNQMTNQMTNQMTNQMTNQMTNQMTNQMTNQMTNQMTNQVNNQMTNQMTNQMNNQMKNQVNSHINSQVAGHMNANMFNGNNSNGTNMLGNMNMLNNMVNSNMDNNVNNNYSNNYPGSGNNGLNNMTSCVMNNNGGEIDMDDNDNIENNDHENMMTLEKEDSINNDSIITTTTATNINSCNNNSNNANSLLNRLVMSNGSNGNTKLNIINNYNNNNNNNSSSGGGVMVNINNVHNNDNMNTYNNNNNNILNDGNSVVGNNESMIHKKNVVNCINNDVEDDLGNMNNNHNNNNNNNNNNNNNNNNNSNNNNNNNNNLNVFMNEHNNPTNNRGIYGSNESINNNGLMDEGRLNFIHTAGKHVDKNNMQSGSTTVVNVLNNDENYIKSNINYTNMDNMKNNDNPIDDDNPNNIVEMNLRVEKNILNNNNDEHIINNTEDMMSTNNKENCTLNGQSTILMNSNEENDETALDTIIQPPIEKRNYVNMMINEQGTADNNSNVDSSNNSYSNNVYTKNLNSNYNGFNNENSNTTTNEQNDSSLYFMNVNSEIQTEHL","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"alphafold_very_low_content":0.7989981214777708,"disorder_content":0.03005635566687539,"disprot_consensus":{"full":[{"start":1,"end":48,"type":"D"}],"Structural state":[{"start":1,"end":48,"type":"D"}],"Disorder function":[{"start":1,"end":48,"type":"F"}]}},{"disprot_id":"DP04358","acc":"P20711","creator":"viglesias","date":"2025-03-19T12:16:23.485Z","features":{"pfam":[{"id":"PF00282","name":"Pyridoxal-dependent decarboxylase conserved domain","start":35,"end":414}],"gene3D":[]},"genes":[{"name":{"value":"DDC","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15532536","url":"http://www.ncbi.nlm.nih.gov/pubmed/15532536","alternativeUrl":"https://europepmc.org/abstract/MED/15532536"}},{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:2719","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:2719"}}]},"synonyms":[{"value":"AADC","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"2590185","url":"http://www.ncbi.nlm.nih.gov/pubmed/2590185","alternativeUrl":"https://europepmc.org/abstract/MED/2590185"}}]}]}],"length":480,"name":"Aromatic-L-amino-acid decarboxylase","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":323,"end":354,"reference_id":"22143761","reference_source":"pmid","reference_html":"Open conformation of human DOPA decarboxylase reveals the mechanism of PLP addition to Group II decarboxylases. <i> Giardina G, Montioli R, Gianni S, Cellini B, Paiardini A, Voltattorni CB, Cutruzzolà F. </i> Proc Natl Acad Sci U S A, 2011","date":"2026-05-11T16:49:29.417Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"3RBL"},{"db":"PDB","id":"3RBF"}],"region_id":"DP04358r005","statement":[{"text":"Indeed both loop2 and 3 in the open conformation of hDDC are solvent exposed and appear to be mobile and therefore not visible in the electron density of both subunits, while in the closed form of the enzyme they are buried and well structured (with the exception of 13 residues of the flexible loop).","type":"Discussion"},{"text":"The active holo- form is responsible for the synthesis of biogenic amines, while the apo- open conformation, which exposes a wider protein surface and has more unstructured regions (loop2 and the flexible loop), is recognized by ubiquitin ligases and preferentially degraded by the ubiquitin proteasome system (UPS).","type":"Figure"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met17Val","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-11T16:49:33.687Z"}},{"start":340,"end":354,"reference_id":"22143761","reference_source":"pmid","reference_html":"Open conformation of human DOPA decarboxylase reveals the mechanism of PLP addition to Group II decarboxylases. <i> Giardina G, Montioli R, Gianni S, Cellini B, Paiardini A, Voltattorni CB, Cutruzzolà F. </i> Proc Natl Acad Sci U S A, 2011","date":"2026-05-11T16:45:53.873Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0007013","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"3RBL"},{"db":"PDB","id":"3RBF"}],"region_id":"DP04358r007","statement":[{"text":"Indeed both loop2 and 3 in the open conformation of hDDC are solvent exposed and appear to be mobile and therefore not visible in the electron density of both subunits, while in the closed form of the enzyme they are buried and well structured (with the exception of 13 residues of the flexible loop).","type":"Discussion"},{"text":"Author is comparing the human apoDDC (apo-hDDC) with that of the close orthologue pig kidney holoDDC The structure of the holo-pkDDC (pdb id: 1JS6).","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"}],"regions_counter":7,"released":"2026_06","sequence":"MNASEFRRRGKEMVDYMANYMEGIEGRQVYPDVEPGYLRPLIPAAAPQEPDTFEDIINDVEKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMDWLGKMLELPKAFLNEKAGEGGGVIQGSASEATLVALLAARTKVIHRLQAASPELTQAAIMEKLVAYSSDQAHSSVERAGLIGGVKLKAIPSDGNFAMRASALQEALERDKAAGLIPFFMVATLGTTTCCSFDNLLEVGPICNKEDIWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFNPHKWLLVNFDCSAMWVKKRTDLTGAFRLDPTYLKHSHQDSGLITDYRHWQIPLGRRFRSLKMWFVFRMYGVKGLQAYIRKHVQLSHEFESLVRQDPRFEICVEVILGLVCFRLKGSNKVNEALLQRINSAKKIHLVPCHLRDKFVLRFAICSRTVESAHVQRAWEHIKELAADVLRAERE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0,"dataset":["NDDs-related proteins"],"disorder_content":0.06666666666666667,"disprot_consensus":{"full":[{"start":323,"end":339,"type":"D"},{"start":340,"end":354,"type":"T"}],"Structural state":[{"start":323,"end":354,"type":"D"}],"Structural transition":[{"start":340,"end":354,"type":"T"}]}},{"disprot_id":"DP04359","acc":"Q8I3X4","creator":"viglesias","date":"2025-03-19T16:38:24.052Z","features":{"pfam":[{"id":"PF01048","name":"Phosphorylase superfamily","start":18,"end":218}],"gene3D":[]},"genes":[{"name":{"value":"PNP","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"18957439","url":"http://www.ncbi.nlm.nih.gov/pubmed/18957439","alternativeUrl":"https://europepmc.org/abstract/MED/18957439"}}]},"orfNames":[{"value":"PF3D7_0513300","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"CAD51497.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAD51497.1"}}]}]}],"length":245,"name":"Purine nucleoside phosphorylase","ncbi_taxon_id":36329,"organism":"Plasmodium falciparum (isolate 3D7)","regions":[{"start":208,"end":223,"reference_id":"16131758","reference_source":"pmid","reference_html":"Structures of Plasmodium falciparum purine nucleoside phosphorylase complexed with sulfate and its natural substrate inosine. <i> Schnick C, Robien MA, Brzozowski AM, Dodson EJ, Murshudov GN, Anderson L, Luft JR, Mehlin C, Hol WG, Brannigan JA, Wilkinson AJ. </i> Acta Crystallogr D Biol Crystallogr, 2005","date":"2026-05-08T20:29:12.260Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":3,"cross_refs":[{"db":"PDB","id":"1SQ6"}],"region_id":"DP04359r001","statement":[{"text":"The new structures presented here specifically highlight the likely roles of Asp206 and two loops flanking the active site: the beta7-alpha6 loop (residues approximately 161-169) and the beta9-alpha8 loop (residues approximately 208-223).","type":"Abstract"},{"text":"The loop above the binding pocket of the immucillin-H complex structure is complete and shows a water-mediated bond between residues Asp218 and Asp206, whereas in the other two structures the loop is disordered or flexible and the model cannot be built.","type":"Figure"},{"text":"A structural feature that may play a crucial role in substrate binding and catalysis is hinted at by the main-chain discontinuity between strand β9 and helix α8 in both of the PfPNP structures presented here, indicating the presence of a flexible loop. The disordered regions span residues 215–220 in PfPNP–ino and 208–223 in PfPNP–SO4. In the immucillin-bound PNP structure, this loop is well defined in the electron-density maps, which show that it forms a kind of lid over the substrate-binding pocket (Fig. 7[link]). This loop conformation is stabilized by a network of hydrogen bonds with the purine moiety of the tightly bound inhibitor, which would explain why the disordered segment in the nucleoside-free PfPNP–SO4 structure is even larger than in the inosine-bound structure. ","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-08T20:29:19.974Z"}},{"start":208,"end":223,"reference_id":"16131758","reference_source":"pmid","reference_html":"Structures of Plasmodium falciparum purine nucleoside phosphorylase complexed with sulfate and its natural substrate inosine. <i> Schnick C, Robien MA, Brzozowski AM, Dodson EJ, Murshudov GN, Anderson L, Luft JR, Mehlin C, Hol WG, Brannigan JA, Wilkinson AJ. </i> Acta Crystallogr D Biol Crystallogr, 2005","date":"2026-05-08T20:26:50.099Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0007013","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"1NW4"},{"db":"PDB","id":"1SQ6"}],"region_id":"DP04359r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"43362","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEMBL","id":"17824"}],"statement":[{"text":"The disordered regions span residues 215–220 in PfPNP–ino and 208–223 in PfPNP–SO4. In the immucillin-bound PNP structure, this loop is well defined in the electron-density maps, which show that it forms a kind of lid over the substrate-binding pocket (Fig. 7[link]). This loop conformation is stabilized by a network of hydrogen bonds with the purine moiety of the tightly bound inhibitor, which would explain why the disordered segment in the nucleoside-free PfPNP–SO4 structure is even larger than in the inosine-bound structure. In the immucillin structure there is a water-mediated interaction between Asp206 and Asp218 of the loop region (Fig. 7[link]), a bond that does not form when Asp206 is shifted away from the binding pocket as in PfPNP–SO4 or when Asp206 interacts with Ser91 as in the PfPNP–ino structure. A similar disorder to order transition of this loop accompanying ligand binding was observed for the T. thermophilus structure (Tahirov et al., 2004[Tahirov, T. H., Inagaki, E., Ohshima, N., Kitao, T., Kuroishi, C., Ukita, Y., Takio, K., Kobayashi, M., Kuramitsu, S., Yokoyama, S. & Miyano, M. (2004). J. Mol. Biol. 337, 1149-1160.]).","type":"Results"},{"text":"Author compares the obtained structure of the Plasmodium falciparum homolog of Uridine phosphorylase/Purine nucleoside phosphorylase with the PDB: 1NW4 structure that represents the transition state of the enzyme, obtained by Shi et al. (PMID: 14982926).","type":"Curator statement"}]}],"regions_counter":3,"released":"2026_06","sequence":"MDNLLRHLKISKEQITPVVLVVGDPGRVDKIKVVCDSYVDLAYNREYKSVECHYKGQKFLCVSHGVGSAGCAVCFEELCQNGAKVIIRAGSCGSLQPDLIKRGDICICNAAVREDRVSHLLIHGDFPAVGDFDVYDTLNKCAQELNVPVFNGISVSSDMYYPNKIIPSRLEDYSKANAAVVEMELATLMVIGTLRKVKTGGILIVDGCPFKWDEGDFDNNLVPHQLENMIKIALGACAKLATKYA","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"alphafold_very_low_content":0.004081632653061225,"disorder_content":0.0653061224489796,"disprot_consensus":{"full":[{"start":208,"end":223,"type":"T"}],"Structural state":[{"start":208,"end":223,"type":"D"}],"Structural transition":[{"start":208,"end":223,"type":"T"}]}},{"disprot_id":"DP04360","acc":"Q8II92","creator":"ldobson","date":"2025-03-19T16:56:09.553Z","features":{"pfam":[{"id":"PF00692","name":"dUTPase","start":86,"end":168}],"gene3D":[]},"genes":[{"orfNames":[{"value":"PF3D7_1127100","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CZT98933.1","url":"https://www.ebi.ac.uk/ena/browser/view/CZT98933.1"}}]}]}],"length":173,"name":"Deoxyuridine 5'-triphosphate nucleotidohydrolase","ncbi_taxon_id":36329,"organism":"Plasmodium falciparum (isolate 3D7)","regions":[{"start":64,"end":79,"reference_id":"15698576","reference_source":"pmid","reference_html":"dUTPase as a platform for antimalarial drug design: structural basis for the selectivity of a class of nucleoside inhibitors. <i> Whittingham JL, Leal I, Nguyen C, Kasinathan G, Bell E, Jones AF, Berry C, Benito A, Turkenburg JP, Dodson EJ, Ruiz Perez LM, Wilkinson AJ, Johansson NG, Brun R, Gilbert IH, Gonzalez Pacanowska D, Wilson KS. </i> Structure, 2005","date":"2026-05-08T17:04:20.417Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"1VYQ"}],"region_id":"DP04360r001","statement":[{"text":"Those residues absent from the model correspond to disordered regions of the PfdUTPase trimer, particularly in the LCR (residues 64–79) and the C termini (residues 156–173).","type":"Results"},{"text":"Extending from an otherwise compact tertiary structure are the C-terminal residues, which are invariably disordered in the absence of substrate (Nord et al., 2001), and the LCRs (residues 59–83) that form loops at the top of the molecule, away from the active site (Figure 4A). Where it is possible for residues of the LCRs to interact with the rest of the protein, they do in fact make very specific contacts. Within each subunit the main chain atoms of residues 55–59 hydrogen bond to those of residues 80–84 forming a twisted antiparallel β strand. In two of the three subunits the side chain of residue Asn83 hydrogen bonds to the main chain carbonyl group of residue Ala110, providing additional intramolecular interactions. Those residues on the outside of the loop constituting two thirds of the LCRs are disordered.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"4369390"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-08T17:04:48.798Z"}},{"start":160,"end":173,"reference_id":"15698576","reference_source":"pmid","reference_html":"dUTPase as a platform for antimalarial drug design: structural basis for the selectivity of a class of nucleoside inhibitors. <i> Whittingham JL, Leal I, Nguyen C, Kasinathan G, Bell E, Jones AF, Berry C, Benito A, Turkenburg JP, Dodson EJ, Ruiz Perez LM, Wilkinson AJ, Johansson NG, Brun R, Gilbert IH, Gonzalez Pacanowska D, Wilson KS. </i> Structure, 2005","date":"2026-05-08T17:05:20.102Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"1VYQ"}],"region_id":"DP04360r002","statement":[{"text":"Those residues absent from the model correspond to disordered regions of the PfdUTPase trimer, particularly in the LCR (residues 64–79) and the C termini (residues 156–173).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"4369390"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-08T17:09:48.330Z"}},{"start":160,"end":173,"reference_id":"15698576","reference_source":"pmid","reference_html":"dUTPase as a platform for antimalarial drug design: structural basis for the selectivity of a class of nucleoside inhibitors. <i> Whittingham JL, Leal I, Nguyen C, Kasinathan G, Bell E, Jones AF, Berry C, Benito A, Turkenburg JP, Dodson EJ, Ruiz Perez LM, Wilkinson AJ, Johansson NG, Brun R, Gilbert IH, Gonzalez Pacanowska D, Wilson KS. </i> Structure, 2005","date":"2026-05-08T17:24:36.135Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"1VYQ"}],"region_id":"DP04360r003","statement":[{"text":"Those residues absent from the model correspond to disordered regions of the PfdUTPase trimer, particularly in the LCR (residues 64–79) and the C termini (residues 156–173).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"4369390"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-08T17:24:37.931Z"}}],"regions_counter":3,"released":"2026_06","sequence":"MHLKIVCLSDEVREMYKNHKTHHEGDSGLDLFIVKDEVLKPKSTTFVKLGIKAIALQYKSNYYYKCEKSENKKKDDDKSNIVNTSFLLFPRSSISKTPLRLANSIGLIDAGYRGEIIAALDNTSDQEYHIKKNDKLVQLVSFTGEPLSFELVEELDETSRGEGGFGSTSNNKY","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"alphafold_very_low_content":0.08670520231213873,"disorder_content":0.17341040462427745,"disprot_consensus":{"full":[{"start":64,"end":79,"type":"D"},{"start":160,"end":173,"type":"D"}],"Structural state":[{"start":64,"end":79,"type":"D"},{"start":160,"end":173,"type":"D"}],"Disorder function":[{"start":160,"end":173,"type":"F"}]}},{"disprot_id":"DP04361","acc":"Q8I5Q6","creator":"viglesias","date":"2025-03-20T09:11:54.811Z","features":{"pfam":[{"id":"PF00578","name":"AhpC/TSA family","start":22,"end":155},{"id":"PF10417","name":"C-terminal domain of 1-Cys peroxiredoxin","start":179,"end":204}],"gene3D":[]},"genes":[{"orfNames":[{"value":"PF3D7_1215000","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CZT99311.1","url":"https://www.ebi.ac.uk/ena/browser/view/CZT99311.1"}}]}]}],"length":216,"name":"Thioredoxin peroxidase 2","ncbi_taxon_id":36329,"organism":"Plasmodium falciparum (isolate 3D7)","regions":[{"start":196,"end":216,"reference_id":"16879648","reference_source":"pmid","reference_html":"Structural and biochemical characterization of a mitochondrial peroxiredoxin from Plasmodium falciparum. <i> Boucher IW, McMillan PJ, Gabrielsen M, Akerman SE, Brannigan JA, Schnick C, Brzozowski AM, Wilkinson AJ, Müller S. </i> Mol Microbiol, 2006","date":"2026-05-08T16:59:57.958Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"2C0D"}],"region_id":"DP04361r001","statement":[{"text":"The electron density maps were generally of very good quality enabling confident modelling of residues 21–188 of chain A and 21–195 of chain B. The N-terminal histidine tag and residue 20 of both chains, residues 189–216 of chain A and residues 196–216 of chain B were not defined by the maps, and they were assumed to be disordered.","type":"Methods"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-08T17:00:11.013Z"}},{"start":196,"end":216,"reference_id":"16879648","reference_source":"pmid","reference_html":"Structural and biochemical characterization of a mitochondrial peroxiredoxin from Plasmodium falciparum. <i> Boucher IW, McMillan PJ, Gabrielsen M, Akerman SE, Brannigan JA, Schnick C, Brzozowski AM, Wilkinson AJ, Müller S. </i> Mol Microbiol, 2006","date":"2026-05-08T17:00:08.487Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"2C0D"}],"region_id":"DP04361r002","statement":[{"text":"The electron density maps were generally of very good quality enabling confident modelling of residues 21–188 of chain A and 21–195 of chain B. The N-terminal histidine tag and residue 20 of both chains, residues 189–216 of chain A and residues 196–216 of chain B were not defined by the maps, and they were assumed to be disordered.","type":"Methods"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-08T17:00:13.075Z"}}],"regions_counter":2,"released":"2026_06","sequence":"MFLKKLCRSNFFGNSRRSFSLVTKKAYNFTAQGLNKNNEIINVDLSSFIGQKYCCLLFYPLNYTFVCPTEIIEFNKHIKDFENKNVELLGISVDSVYSHLAWKNMPIEKGGIGNVEFTLVSDINKDISKNYNVLYDNSFALRGLFIIDKNGCVRHQTVNDLPIGRNVQEVLRTIDSIIHVDTSGEVCPINWKKGQKAFKPTTESLIDYMNNANKNV","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"alphafold_very_low_content":0.041666666666666664,"disorder_content":0.09722222222222222,"disprot_consensus":{"full":[{"start":196,"end":216,"type":"D"}],"Structural state":[{"start":196,"end":216,"type":"D"}],"Disorder function":[{"start":196,"end":216,"type":"F"}]}},{"disprot_id":"DP04362","acc":"Q9BH77","creator":"viglesias","date":"2025-03-20T09:35:37.450Z","features":{"pfam":[{"id":"PF13561","name":"Enoyl-(Acyl carrier protein) reductase","start":192,"end":345},{"id":"PF13561","name":"Enoyl-(Acyl carrier protein) reductase","start":369,"end":418}],"gene3D":[]},"genes":[{"name":{"value":"FabI","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAK38273.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAK38273.1"}}]}}],"length":432,"name":"Enoyl-ACP reductase","ncbi_taxon_id":5833,"organism":"Plasmodium falciparum","regions":[{"start":325,"end":365,"reference_id":"17327670","reference_source":"pmid","reference_html":"Studies of Toxoplasma gondii and Plasmodium falciparum enoyl acyl carrier protein reductase and implications for the development of antiparasitic agents. <i> Muench SP, Prigge ST, McLeod R, Rafferty JB, Kirisits MJ, Roberts CW, Mui EJ, Rice DW. </i> Acta Crystallogr D Biol Crystallogr, 2007","date":"2026-05-08T16:47:40.858Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"2O2Y"}],"region_id":"DP04362r001","statement":[{"text":"Moreover, in our crystal form and all of the previously solved PfENR structures, the loop region corresponding to the low-complexity insert common to the apicomplexan ENR family between residues Ile240 and Thr283 cannot be seen owing to disorder (Perozzo et al., 2002 ▶; Pidugu et al., 2004 ▶).","type":"Results"},{"text":"Missing residues","type":"Table"},{"text":"Ala1Glu14 (A,B,C), Ala1Lys12 (D), Lys242Asn282 (A,B,C), Asn241Asn282 (D), Asn347Glu340 (A,B), Glu348Glu340 (C), Arg346Glu340 (D).","type":"Table"},{"text":"PDB starts in position 84 of the UniProt protein sequence, therefore there's a shift in numbering residues.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"164200","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"13389","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-08T16:47:42.941Z"}},{"start":326,"end":365,"reference_id":"11792710","reference_source":"pmid","reference_html":"Structural elucidation of the specificity of the antibacterial agent triclosan for malarial enoyl acyl carrier protein reductase. <i> Perozzo R, Kuo M, Sidhu Ab, Valiyaveettil JT, Bittman R, Jacobs WR, Fidock DA, Sacchettini JC. </i> J Biol Chem, 2002","date":"2026-05-08T16:34:19.522Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"1VRW"}],"region_id":"DP04362r002","statement":[{"text":"Only 3 amino acids of the low complexity insertion were visible in the electron density maps, indicating that most of this region was disordered even in the presence of bound substrate and inhibitor. Nonetheless, the last visible amino acids just before (Lys325) and after (Tyr366) the low complexity region were in nearly the exact same position as the comparable loop residues in the E. coli enzyme structure (Fig. 3d).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16908","entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-08T16:37:03.770Z"}}],"regions_counter":3,"released":"2026_06","sequence":"MNKISQRLLFLFLHFYTIVCFIQNNTQKTFHNVLHNEQIRGKEKAFYRKEKRENIFIGNKMKHLNNMNNTHNNNHYMEKEEQDASNIYKIKEENKNEDICFIAGIGDTNGYGWGIAKELSKRNVKIIFGIWPPVYNIFMKNYKNGKFDNDMIIDKDKKMNILDMLPFDASFDTANDIDEETKNNKRYNMLQNYTIEDVANLIHQKYGKINMLVHSLANAKEVQKDLLNTSRKGYLDALSKSSYSLISLCKYFVNIMKPQSSIISLTYHASQKVVPGYGGGMSSAKAALESDTRVLAYHLGRNYNIRINTISAGPLKSRAATAINKLNNTYENNTNQNKNRNSHDVHNIMNNSGEKEEKKNSASQNYTFIDYAIEYSEKYAPLRQKLLSTDIGSVASFLLSRESRAITGQTIYVDNGLNIMFLPDDIYRNENE","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"alphafold_very_low_content":0.22685185185185186,"disorder_content":0.09490740740740741,"disprot_consensus":{"full":[{"start":325,"end":365,"type":"D"}],"Structural state":[{"start":325,"end":365,"type":"D"}]}},{"disprot_id":"DP04363","acc":"Q6UCJ9","creator":"viglesias","date":"2025-03-20T09:46:15.718Z","features":{"pfam":[{"id":"PF13561","name":"Enoyl-(Acyl carrier protein) reductase","start":208,"end":395}],"gene3D":[]},"genes":[{"name":{"value":"ENR","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAQ74987.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAQ74987.1"}}]},"orfNames":[{"value":"TGRH88_064800","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"KAF4638871.1","url":"https://www.ebi.ac.uk/ena/browser/view/KAF4638871.1"}}]}]}],"length":417,"name":"Enoyl-acyl carrier reductase","ncbi_taxon_id":5811,"organism":"Toxoplasma gondii","regions":[{"start":330,"end":342,"reference_id":"17327670","reference_source":"pmid","reference_html":"Studies of Toxoplasma gondii and Plasmodium falciparum enoyl acyl carrier protein reductase and implications for the development of antiparasitic agents. <i> Muench SP, Prigge ST, McLeod R, Rafferty JB, Kirisits MJ, Roberts CW, Mui EJ, Rice DW. </i> Acta Crystallogr D Biol Crystallogr, 2007","date":"2026-05-08T16:51:07.826Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"2O2S"},{"db":"PDB","id":"2O50"}],"region_id":"DP04363r001","statement":[{"text":"The most significant difference is the disorder of residues Lys228–Lys241, which form an ordered loop in the TgENR–NAD+–triclosan complex, with Ala230–Ser232 forming a helix which packs against the triclosan inhibitor.","type":"Results"},{"text":"This comparison showed only one region of difference, around the inhibitor-binding site between residues 190–209 in EcENR (229–249 in TgENR), corresponding to α6 and α7 (α7 and α8 in the Tg and Pf enzymes) and the flanking residues (Fig. 6 ▶ b). In the structure of the EcENR–NAD+ complex and in the TgENR apo enzyme, this region corresponds to a disordered loop. ","type":"Results"},{"text":"There's a 102 residue shift in numbering residues from PDB/publication to the UniProt reference sequence.","type":"Curator statement"}],"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":270,"end":270,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":295,"end":295,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":397,"end":397,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":null,"end":null,"position":"Specific residue"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-08T16:51:11.337Z"}},{"start":330,"end":342,"reference_id":"17327670","reference_source":"pmid","reference_html":"Studies of Toxoplasma gondii and Plasmodium falciparum enoyl acyl carrier protein reductase and implications for the development of antiparasitic agents. <i> Muench SP, Prigge ST, McLeod R, Rafferty JB, Kirisits MJ, Roberts CW, Mui EJ, Rice DW. </i> Acta Crystallogr D Biol Crystallogr, 2007","date":"2026-05-08T16:52:38.991Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"2O2S"},{"db":"PDB","id":"2O50"}],"region_id":"DP04363r002","statement":[{"text":"The most significant difference is the disorder of residues Lys228–Lys241, which form an ordered loop in the TgENR–NAD+–triclosan complex, with Ala230–Ser232 forming a helix which packs against the triclosan inhibitor.","type":"Results"},{"text":"There's a 102 residue shift in numbering residues from PDB/publication to the UniProt reference sequence.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"13389","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"164200","entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-08T16:52:43.651Z"}}],"regions_counter":2,"released":"2026_06","sequence":"MVGFKLLTLGAFVAGELTLVGPAGTMAFTVPNATGAKPLVTSVSVRPSWSSARQNAFSSSSSRSQSSVRPHSAFVTNRLETAGETGTQHRAADSAAGVGAAQSAFPIDLRGQTAFVAGVADSHGYGWAIAKHLASAGARVALGTWPPVLGLFQKSLQSGRLDEDRKLPDGSLIEFAGVYPLDAAFDKPEDVPQDIKDNKRYAGVDGYTIKEVAVKVKQDLGNIDILVHSLANGPEVTKPLLETSRKGYLAASSNSAYSFVSLLQHFGPIMNEGGSAVTLSYLAAERVVPGYGGGMSSAKAALESDTRTLAWEAGQKYGVRVNAISAGPLKSRAASAIGKSGEKSFIDYAIDYSYNNAPLRRDLHSDDVGGAALFLLSPLARAVSGVTLYVDNGLHAMGQAVDSRSMPPLQRATQEIN","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Conoidasida","Coccidia","Eucoccidiorida","Eimeriorina","Sarcocystidae","Toxoplasma"],"alphafold_very_low_content":0.2517985611510791,"disorder_content":0.03117505995203837,"disprot_consensus":{"full":[{"start":330,"end":342,"type":"T"}],"Structural state":[{"start":330,"end":342,"type":"D"}],"Structural transition":[{"start":330,"end":342,"type":"T"}]}},{"disprot_id":"DP04364","acc":"P0AEK4","creator":"viglesias","date":"2025-03-20T11:01:51.986Z","features":{"pfam":[{"id":"PF13561","name":"Enoyl-(Acyl carrier protein) reductase","start":13,"end":252}],"gene3D":[]},"genes":[{"name":{"value":"fabI"},"synonyms":[{"value":"envM"}],"olnNames":[{"value":"b1288"},{"value":"JW1281"}]}],"length":262,"name":"Enoyl-[acyl-carrier-protein] reductase [NADH] FabI","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions":[{"start":196,"end":205,"reference_id":"8953047","reference_source":"pmid","reference_html":"A mechanism of drug action revealed by structural studies of enoyl reductase. <i> Baldock C, Rafferty JB, Sedelnikova SE, Baker PJ, Stuitje AR, Slabas AR, Hawkes TR, Rice DW. </i> Science, 1996","date":"2026-05-08T16:20:54.629Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"1DFI"}],"region_id":"DP04364r001","statement":[{"text":"However, there is a break in the density for a stretch of 10 amino acid residues; these 10 residues form a loop, between strand β6 and helix α6, that borders the nucleotide-binding site.","type":"Results"},{"text":"In the resultant electron density map, calculated from the averaged phases, we were able to find clear density for all but the first residue, the last four residues, and 10 residues from the loop joining β6 and α6; using the graphics program FRODO (24), we were able to build with confidence a model comprising 247 of the 262 amino acids of E. coli ENR.","type":"Methods"},{"text":"Electron density map shows the 10 missing residues correspond to the stretch between 195 and 204.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"13389","entry_name":null}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-08T16:21:32.439Z"}},{"start":196,"end":205,"reference_id":"8953047","reference_source":"pmid","reference_html":"A mechanism of drug action revealed by structural studies of enoyl reductase. <i> Baldock C, Rafferty JB, Sedelnikova SE, Baker PJ, Stuitje AR, Slabas AR, Hawkes TR, Rice DW. </i> Science, 1996","date":"2026-05-08T16:21:24.550Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"cross_refs":[{"db":"PDB","id":"1DFI"},{"db":"PDB","id":"1DFH"},{"db":"PDB","id":"1DFG"}],"region_id":"DP04364r002","statement":[{"text":"However, there is a break in the density for a stretch of 10 amino acid residues; these 10 residues form a loop, between strand β6 and helix α6, that borders the nucleotide-binding site. In the structures of the ENR-NAD1-diazaborine complexes, this loop is well defined and provides two residues whose side chains are in van der Waals contact with the non–boroncontaining five- and six-membered rings of thienodiazaborine and benzodiazaborine, respectively","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"171833"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"13389","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"83945","entry_name":null}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","states_connection":[{"source":"DP04364r001","target":"DP04364r003"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-08T16:21:35.281Z"}},{"start":196,"end":205,"reference_id":"8953047","reference_source":"pmid","reference_html":"A mechanism of drug action revealed by structural studies of enoyl reductase. <i> Baldock C, Rafferty JB, Sedelnikova SE, Baker PJ, Stuitje AR, Slabas AR, Hawkes TR, Rice DW. </i> Science, 1996","date":"2026-05-08T16:20:33.598Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"1DFG"},{"db":"PDB","id":"1DFH"}],"region_id":"DP04364r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"13389","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"83945","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"171833"}],"statement":[{"text":"However, there is a break in the density for a stretch of 10 amino acid residues; these 10 residues form a loop, between strand β6 and helix α6, that borders the nucleotide-binding site. In the structures of the ENR-NAD1-diazaborine complexes, this loop is well defined and provides two residues whose side chains are in van der Waals contact with the non–boroncontaining five- and six-membered rings of thienodiazaborine and benzodiazaborine, respectively.","type":"Results"}]}],"regions_counter":3,"released":"2026_06","sequence":"MGFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEFAAQLGSDIVLQCDVAEDASIDTMFAELGKVWPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDISSYSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIKDFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGGFSIAAMNELELK","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"alphafold_very_low_content":0,"disorder_content":0.03816793893129771,"disprot_consensus":{"full":[{"start":196,"end":205,"type":"T"}],"Structural state":[{"start":196,"end":205,"type":"D"}],"Structural transition":[{"start":196,"end":205,"type":"T"}]}},{"disprot_id":"DP04368","acc":"Q99PZ6","creator":"xcastro","date":"2025-04-22T07:14:59.562Z","features":{"pfam":[{"id":"PF22303","name":"Protein kinase OspG, kinase domain","start":32,"end":183}],"gene3D":[]},"genes":[{"name":{"value":"ospG"},"orfNames":[{"value":"pWR501_0237"},{"value":"SFLP087"}],"olnNames":[{"value":"CP0227"}]}],"length":196,"name":"Protein kinase OspG","ncbi_taxon_id":623,"organism":"Shigella flexneri","regions":[{"start":1,"end":25,"reference_id":"24446487","reference_source":"pmid","reference_html":"E2~Ub conjugates regulate the kinase activity of Shigella effector OspG during pathogenesis. <i> Pruneda JN, Smith FD, Daurie A, Swaney DL, Villén J, Scott JD, Stadnyk AW, Le Trong I, Stenkamp RE, Klevit RE, Rohde JR, Brzovic PS. </i> EMBO J, 2014","date":"2025-06-17T08:02:03.104Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"4BVU"}],"region_id":"DP04368r001","statement":[{"text":"The structure of OspG in the complex is well defined by the electron density with the exception of a 10x‐His tag and 25 native residues at the N‐terminus that are disordered and may encode a sequence necessary for recognition by the Type III secretion apparatus.","type":"Results"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"The structure of OspG in the complex is well defined by the electron density with the exception of a 10x‐His tag and 25 native residues at the N‐terminus that are disordered and may encode a sequence necessary for recognition by the Type III secretion apparatus."}]}],"sequence_construct":"MGHHHHHHHHHHSSGMKITSTIIQTPFPFENNNSHAGIVTEPILGKLIGQGSTAEIFEDVNDSSALYKKYDLIGNQYNEILEMAWQESELFNAFYGDEASVVIQYGGDVYLRMLRVPGTPLSDIDTADIPDNIESLYLQLICKLNELSIIHYDLNTGNMLYDKESESLFPIDFRNIYAEYYAATKKDKEIIDRRLQMRTNDFYSLLNRKYL","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61077","statements":[{"type":"Methods","text":"The OspG/UbcH5c-O∼Ub complex was purified over SDX75 size exclusion chromatography into 50 mM HEPES (pH 7.5), 100 mM NaCl and concentrated to 200 μM."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0CG48","statements":[{"type":"Methods","text":"The OspG/UbcH5c-O∼Ub complex was purified over SDX75 size exclusion chromatography into 50 mM HEPES (pH 7.5), 100 mM NaCl and concentrated to 200 μM."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-17T15:47:01.659Z"}},{"start":1,"end":25,"reference_id":"24446487","reference_source":"pmid","reference_html":"E2~Ub conjugates regulate the kinase activity of Shigella effector OspG during pathogenesis. <i> Pruneda JN, Smith FD, Daurie A, Swaney DL, Villén J, Scott JD, Stadnyk AW, Le Trong I, Stenkamp RE, Klevit RE, Rohde JR, Brzovic PS. </i> EMBO J, 2014","date":"2025-06-17T08:03:10.543Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"The structure of OspG in the complex is well defined by the electron density with the exception of a 10x‐His tag and 25 native residues at the N‐terminus that are disordered and may encode a sequence necessary for recognition by the Type III secretion apparatus."}]}],"cross_refs":[{"db":"PDB","id":"4BVU"}],"region_id":"DP04368r002","sequence_construct":"MGHHHHHHHHHHSSGMKITSTIIQTPFPFENNNSHAGIVTEPILGKLIGQGSTAEIFEDVNDSSALYKKYDLIGNQYNEILEMAWQESELFNAFYGDEASVVIQYGGDVYLRMLRVPGTPLSDIDTADIPDNIESLYLQLICKLNELSIIHYDLNTGNMLYDKESESLFPIDFRNIYAEYYAATKKDKEIIDRRLQMRTNDFYSLLNRKYL","statement":[{"text":"The structure of OspG in the complex is well defined by the electron density with the exception of a 10x‐His tag and 25 native residues at the N‐terminus that are disordered and may encode a sequence necessary for recognition by the Type III secretion apparatus.","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61077","statements":[{"type":"Methods","text":"The OspG/UbcH5c-O∼Ub complex was purified over SDX75 size exclusion chromatography into 50 mM HEPES (pH 7.5), 100 mM NaCl and concentrated to 200 μM."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0CG48","statements":[{"type":"Methods","text":"The OspG/UbcH5c-O∼Ub complex was purified over SDX75 size exclusion chromatography into 50 mM HEPES (pH 7.5), 100 mM NaCl and concentrated to 200 μM."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-17T15:46:59.836Z"}}],"regions_counter":2,"released":"2025_06","sequence":"MKITSTIIQTPFPFENNNSHAGIVTEPILGKLIGQGSTAEIFEDVNDSSALYKKYDLIGNQYNEILEMAWQESELFNAFYGDEASVVIQYGGDVYLRMLRVPGTPLSDIDTADIPDNIESLYLQLICKLNELSIIHYDLNTGNMLYDKESESLFPIDFRNIYAEYYAATKKDKEIIDRRLQMRTNDFYSLLNRKYL","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Shigella"],"alphafold_very_low_content":0.11224489795918367,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.12755102040816327,"disprot_consensus":{"full":[{"start":1,"end":25,"type":"D"}],"Structural state":[{"start":1,"end":25,"type":"D"}],"Disorder function":[{"start":1,"end":25,"type":"F"}]}},{"disprot_id":"DP04369","acc":"A0A0H3JPC6","creator":"xcastro","date":"2025-04-22T09:13:11.958Z","features":{"pfam":[{"id":"PF00535","name":"Glycosyl transferase family 2","start":5,"end":132},{"id":"PF18674","name":"TarS beta-glycosyltransferase C-terminal domain 1","start":385,"end":486},{"id":"PF22181","name":"Glycosyl transferase TarS linker domain","start":219,"end":316},{"id":"PF22377","name":"TarS C-terminal domain 2","start":493,"end":570}],"gene3D":[]},"genes":[{"name":{"value":"tarS","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"27973583","url":"http://www.ncbi.nlm.nih.gov/pubmed/27973583","alternativeUrl":"https://europepmc.org/abstract/MED/27973583"}}]},"olnNames":[{"value":"SAV0258","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"BAB56420.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAB56420.1"}}]}]}],"length":573,"name":"Poly(ribitol-phosphate) beta-N-acetylglucosaminyltransferase TarS","ncbi_taxon_id":158878,"organism":"Staphylococcus aureus (strain Mu50 / ATCC 700699)","regions":[{"start":206,"end":216,"reference_id":"27973583","reference_source":"pmid","reference_html":"Structure and Mechanism of Staphylococcus aureus TarS, the Wall Teichoic Acid β-glycosyltransferase Involved in Methicillin Resistance. <i> Sobhanifar S, Worrall LJ, King DT, Wasney GA, Baumann L, Gale RT, Nosella M, Brown ED, Withers SG, Strynadka NC. </i> PLoS Pathog, 2016","date":"2025-06-17T08:06:20.986Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"5TZI"},{"db":"PDB","id":"5TZJ"}],"region_id":"DP04369r001","statement":[{"text":"The second loop (205–215), designated as the substrate access (SA) loop, is ordered only in the presence of UDP-GlcNAc and sterically occludes an otherwise open channel leading into the active site in the absence of the intact donor (Fig 2C). Based on these observations it may be inferred that in the native structure, the SA loop is disordered allowing binding of UDP-GlcNAc, upon which the CS loop moves closer to the active site center and the SA loop becomes ordered, occluding the active site channel.","type":"Results"}],"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":5.5,"statements":[{"type":"Methods","text":"Crystals of TarS1-349 (~20 mg/mL) were obtained by sitting-drop vapor diffusion in the presence (or absence) of 15 mM UDP-GlcNAc and 2 mM MnCl2 using a reservoir solution of 0.2 mM lithium sulfate, 27% w/v PEG 3350, and 0.1 M Bis-Tris pH 5.5."}]}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":"not specified","value":15,"db":"PubChem","id":"CID:9547196","statements":[{"type":"Methods","text":"Crystals of TarS1-349 (~20 mg/mL) were obtained by sitting-drop vapor diffusion in the presence (or absence) of 15 mM UDP-GlcNAc and 2 mM MnCl2 using a reservoir solution of 0.2 mM lithium sulfate, 27% w/v PEG 3350, and 0.1 M Bis-Tris pH 5.5."}]}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"The TarS truncation mutant (TarS1-349) was cloned into the expression vector pET41b with a C-terminal 6x His-tag."}]}],"sequence_construct":"MKFSVIVPTYNSEKYITELLNSLAKQDFPKTEFEVVVVDDCSTDQTLQIVEKYRNKLNLKVSQLETNSGGPGKPRNVALKQAEGEFVLFVDSDDYINKETLKDAAAFIDEHHSDVLLIKMKGVNGRGVPQSMFKETAPEVTLLNSRIIYTLSPTKIYRTALLKDNDIYFPEELKSAEDQLFTMKAYLNANRISVLSDKAYYYATKREGEHMSSAYVSPEDFYEVMRLIAVEILNADLEEAHKDQILAEFLNRHFSFSRTNGFSLKVKLEEQPQWINALGDFIQAVPERVDALVMSKLRPLLHYARAKDIDNYRTVEESYRQGQYYRFDIVDGKLNIQFNEGEPYFEGIDKLVPRGSAAAALEHHHHHH","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-17T15:47:26.761Z"}},{"start":208,"end":213,"reference_id":"27973583","reference_source":"pmid","reference_html":"Structure and Mechanism of Staphylococcus aureus TarS, the Wall Teichoic Acid β-glycosyltransferase Involved in Methicillin Resistance. <i> Sobhanifar S, Worrall LJ, King DT, Wasney GA, Baumann L, Gale RT, Nosella M, Brown ED, Withers SG, Strynadka NC. </i> PLoS Pathog, 2016","date":"2025-06-17T08:45:02.186Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"GO:0016798","term_name":"hydrolase activity, acting on glycosyl bonds","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IMP","region_id":"DP04369r002","statement":[{"text":"Several constructed active-site mutants were also tested for activity, along with a designed control (D198A) chosen distal from the catalytic center (Fig 5B). Based on these results, mutations R75A, D91A, D93A, D94A, E177A, and H210A abolished activity as defined by UDP-GlcNAc hydrolysis, whereas mutations D178N, R206A, and S212A led to severe decreases in activity, validating the importance of these residues for catalysis, as discussed above.","type":"Results"}],"term_comment":"","term_def":"\"Catalysis of the hydrolysis of any glycosyl bond.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.His210Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Several constructed active-site mutants were also tested for activity, along with a designed control (D198A) chosen distal from the catalytic center (Fig 5B). Based on these results, mutations R75A, D91A, D93A, D94A, E177A, and H210A abolished activity as defined by UDP-GlcNAc hydrolysis, whereas mutations D178N, R206A, and S212A led to severe decreases in activity, validating the importance of these residues for catalysis, as discussed above."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ser212Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Several constructed active-site mutants were also tested for activity, along with a designed control (D198A) chosen distal from the catalytic center (Fig 5B). Based on these results, mutations R75A, D91A, D93A, D94A, E177A, and H210A abolished activity as defined by UDP-GlcNAc hydrolysis, whereas mutations D178N, R206A, and S212A led to severe decreases in activity, validating the importance of these residues for catalysis, as discussed above."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-17T15:48:11.234Z"}},{"start":206,"end":216,"reference_id":"27973583","reference_source":"pmid","reference_html":"Structure and Mechanism of Staphylococcus aureus TarS, the Wall Teichoic Acid β-glycosyltransferase Involved in Methicillin Resistance. <i> Sobhanifar S, Worrall LJ, King DT, Wasney GA, Baumann L, Gale RT, Nosella M, Brown ED, Withers SG, Strynadka NC. </i> PLoS Pathog, 2016","date":"2025-06-17T08:04:03.301Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"5TZI"}],"region_id":"DP04369r004","statement":[{"text":"The second loop (205–215), designated as the substrate access (SA) loop, is ordered only in the presence of UDP-GlcNAc and sterically occludes an otherwise open channel leading into the active site in the absence of the intact donor (Fig 2C).","type":"Results"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"The TarS truncation mutant (TarS1-349) was cloned into the expression vector pET41b with a C-terminal 6x His-tag."}]}],"sequence_construct":"MKFSVIVPTYNSEKYITELLNSLAKQDFPKTEFEVVVVDDCSTDQTLQIVEKYRNKLNLKVSQLETNSGGPGKPRNVALKQAEGEFVLFVDSDDYINKETLKDAAAFIDEHHSDVLLIKMKGVNGRGVPQSMFKETAPEVTLLNSRIIYTLSPTKIYRTALLKDNDIYFPEELKSAEDQLFTMKAYLNANRISVLSDKAYYYATKREGEHMSSAYVSPEDFYEVMRLIAVEILNADLEEAHKDQILAEFLNRHFSFSRTNGFSLKVKLEEQPQWINALGDFIQAVPERVDALVMSKLRPLLHYARAKDIDNYRTVEESYRQGQYYRFDIVDGKLNIQFNEGEPYFEGIDKLVPRGSAAAALEHHHHHH","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-17T15:47:23.022Z"}}],"regions_counter":4,"released":"2025_06","sequence":"MMKFSVIVPTYNSEKYITELLNSLAKQDFPKTEFEVVVVDDCSTDQTLQIVEKYRNKLNLKVSQLETNSGGPGKPRNVALKQAEGEFVLFVDSDDYINKETLKDAAAFIDEHHSDVLLIKMKGVNGRGVPQSMFKETAPEVTLLNSRIIYTLSPTKIYRTALLKDNDIYFPEELKSAEDQLFTMKAYLNANRISVLSDKAYYYATKREGEHMSSAYVSPEDFYEVMRLIAVEILNADLEEAHKDQILAEFLNRHFSFSRTNGFSLKVKLEEQPQWINALGDFIQAVPERVDALVMSKLRPLLHYARAKDIDNYRTVEESYRQGQYYRFDIVDGKLNIQFNEGEPYFEGIDIAKPKVKMTAFKFDNHKIVTELTLNEFMIGEGHYDVRLKLHSRNKKHTMYVPLSVNANKQYRFNIMLEDIKAYLPKEKIWDVFLEVQIGTEVFEVRVGNQRNKYAYTAETSALIHLNNDFYRLTPYFTKDFNNISLYFTAITLTDSISMKLKGKNKIILTGLDRGYVFEEGMASVVLKDDMIMGMLSQTSENEVEILLSKDIKKRDFKNIVKLNTAHMTYSLK","taxonomy":["Bacteria","Bacillati","Bacillota","Bacilli","Bacillales","Staphylococcaceae","Staphylococcus"],"alphafold_very_low_content":0,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.019197207678883072,"disprot_consensus":{"full":[{"start":206,"end":216,"type":"T"}],"Structural state":[{"start":206,"end":216,"type":"D"}],"Structural transition":[{"start":206,"end":216,"type":"T"}],"Molecular function":[{"start":208,"end":213,"type":"F"}]}},{"disprot_id":"DP04370","acc":"L7N667","creator":"xcastro","date":"2025-04-22T12:18:12.414Z","features":{"pfam":[{"id":"PF00934","name":"PE family","start":5,"end":93},{"id":"PF12484","name":"PPE-SVP subfamily C-terminal region","start":192,"end":272}],"gene3D":[]},"genes":[{"name":{"value":"PE8","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"CCP43791.1","url":"https://www.ebi.ac.uk/ena/browser/view/CCP43791.1"}}]},"olnNames":[{"value":"Rv1040c","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"CCP43791.1","url":"https://www.ebi.ac.uk/ena/browser/view/CCP43791.1"}}]}]}],"length":275,"name":"PE family protein PE8","ncbi_taxon_id":83332,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","regions":[{"start":85,"end":99,"reference_id":"28842489","reference_source":"pmid","reference_html":"Structural basis of the PE-PPE protein interaction in <i>Mycobacterium tuberculosis</i>. <i> Chen X, Cheng HF, Zhou J, Chan CY, Lau KF, Tsui SK, Au SW. </i> J Biol Chem, 2017","date":"2025-06-17T08:55:04.276Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"5XFS"}],"region_id":"DP04370r001","statement":[{"text":"The electron density map was clearly defined throughout the structure, except for residues 85–99 in PE8 and residues 174–194 in PPE15, in line with a secondary structure prediction by Phyre2 (31), suggesting that these regions are highly disordered. This disordered region of PE8 includes the YXXXD/E secretion motif.","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P9WI31","statements":[{"type":"Methods","text":"Purified protein complex containing EspG5–PE81–99–PPE151–194 were pooled and concentrated in buffer containing 20 mm HEPES, pH 7.5, 300 mm NaCl for crystallization trials."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O53943","statements":[{"type":"Methods","text":"Purified protein complex containing EspG5–PE81–99–PPE151–194 were pooled and concentrated in buffer containing 20 mm HEPES, pH 7.5, 300 mm NaCl for crystallization trials."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-17T15:48:44.253Z"}}],"regions_counter":2,"released":"2025_06","sequence":"MSFLKTVPEELTAAAAQLGTIGAAMAAQNAAAAAPTTAIAPAALDEVSALQAALFTAYGTFYQQVSAEAQAMHDMFVNTLGISAGTYGVTESLNSSAAASPLSGITGEASAIIQATTGLFPPELSGGIGNILNIGAGNWASATSTLIGLAGGGLLPAEEAAEAASALGGEAALGELGALGAAEAALGEAGIAAGLGSASAIGMLSVPPAWAGQATLVSTTSTLPGAGWTAAAPQAAAGTFIPGMPGVASAARNSAGFGAPRYGVKPIVMPKPATV","taxonomy":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"alphafold_very_low_content":0.36,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.05454545454545454,"disprot_consensus":{"full":[{"start":85,"end":99,"type":"D"}],"Structural state":[{"start":85,"end":99,"type":"D"}]}},{"disprot_id":"DP04371","acc":"P40296","creator":"xcastro","date":"2025-04-22T13:22:06.909Z","features":{"pfam":[{"id":"PF01052","name":"Type III flagellar switch regulator (C-ring) FliN C-term","start":232,"end":301}],"gene3D":[]},"genes":[{"name":{"value":"yscQ"},"olnNames":[{"value":"pYV0070"}]}],"length":307,"name":"Yop proteins translocation protein Q","ncbi_taxon_id":273123,"organism":"Yersinia pseudotuberculosis serotype I (strain IP32953)","regions":[{"start":220,"end":229,"reference_id":"22320351","reference_source":"pmid","reference_html":"Two translation products of Yersinia yscQ assemble to form a complex essential to type III secretion. <i> Bzymek KP, Hamaoka BY, Ghosh P. </i> Biochemistry, 2012","date":"2025-06-17T09:05:13.084Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"G","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The coding sequence for YscQ (residues 1–307, with an S2G substitution to accommodate a DNA restriction site) and YscQ-C (residues 218–307, with an S219G substitution to accommodate a DNA restriction site) was amplified by polymerase chain reaction (PCR) from the pYV plasmid of Y. pseudotuberculosis 126 (23) and used for generation of pET28b(+) (EMD, San Diego, CA) and, in the case of YscQ, also pBAD-A (Invitrogen, Carlsbad, CA) expression constructs."}]}],"cross_refs":[{"db":"PDB","id":"3UEP"}],"region_id":"DP04371r001","sequence_construct":"MGHESDELNPEPLTDLNQLPVQVSFEVGRQILDWHTLTSLEPGSLIDLTTPVDGEVRLLANGRLLGHGRLVEIQGRLGVRIERLTEVTIS","statement":[{"text":"YscQ-C was expressed in E. coli, purified, and crystallized. The 2.25 Å resolution limit structure of YscQ-C was determined by single-wavelength anomalous dispersion (Table 1). Except for the first 11 residues, which were presumably flexible, the entirety of YscQ-C was visible and unambiguously traced.","type":"Results"},{"text":"However, the N-terminus of YscQ-C is disordered, and thus, the exact location of the start site is unlikely to be consequential.","type":"Discussion"},{"text":"The IDR characterized in the publication corresponds to region 220-228 of the amino acid sequence, since YscQ-C contains the residues 220–307 of YscQ.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-17T15:50:40.594Z"}}],"regions_counter":1,"released":"2025_06","sequence":"MSLLTLPQAKLSELSLRQRLSHYQQNYLWEEGKLELTVSEPPSSLNCILQLQWKGTHFTLYCFGNDLANWLTADLLGAPFFTLPKELQLALLERQTVFLPKLVCNDIATASLSVTQPLLSLRLSRDNAHISFWLTSAEALFALLPARPNSERIPLPILISLRWHKVYLTLDEVDSLRLGDVLLAPEGSGPNSPVLAYVGENPWGYFQLQSNKLEFIGMSHESDELNPEPLTDLNQLPVQVSFEVGRQILDWHTLTSLEPGSLIDLTTPVDGEVRLLANGRLLGHGRLVEIQGRLGVRIERLTEVTIS","taxonomy":["Bacteria","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"],"alphafold_very_low_content":0.009771986970684038,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.03257328990228013,"disprot_consensus":{"full":[{"start":220,"end":229,"type":"D"}],"Structural state":[{"start":220,"end":229,"type":"D"}]}},{"disprot_id":"DP04372","acc":"P0A367","creator":"xcastro","date":"2025-04-22T14:01:11.066Z","features":{"pfam":[{"id":"PF00555","name":"delta endotoxin","start":259,"end":460},{"id":"PF03944","name":"delta endotoxin","start":470,"end":606},{"id":"PF03945","name":"delta endotoxin, N-terminal domain","start":50,"end":251},{"id":"PF17997","name":"Insecticidal delta-endotoxin CryIA(c) domain 5","start":684,"end":867},{"id":"PF18449","name":"Pesticidal crystal protein Cry1Aa, domain IV","start":616,"end":678},{"id":"PF21463","name":"Cry1Ac, domain VII","start":981,"end":1060}],"gene3D":[]},"genes":[{"name":{"value":"cry1Aa"},"synonyms":[{"value":"cry-1-1"},{"value":"cry1A(a)"},{"value":"cryA"},{"value":"crybns3-1"},{"value":"cryIA(a)"},{"value":"icp"}]}],"length":1176,"name":"Pesticidal crystal protein Cry1Aa","ncbi_taxon_id":1433,"organism":"Bacillus thuringiensis subsp. aizawai","regions":[{"start":780,"end":818,"reference_id":"37922785","reference_source":"pmid","reference_html":"Crystal structure of the in-cell Cry1Aa purified from Bacillus thuringiensis. <i> Tanaka J, Abe S, Hayakawa T, Kojima M, Yamashita K, Hirata K, Ueno T. </i> Biochem Biophys Res Commun, 2023","date":"2025-04-22T14:08:30.735Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"8W7N"}],"region_id":"DP04372r001","statement":[{"text":"Disordered regions indicating the location of cysteine residues are shown in gray font (Met1-Gly32, Gly780-Glu818, Glu1064-Pro1140).","type":"Figure"},{"text":"The residues of Met1-Gly32, Ile369-Asn377, Gly442-Val444, Ser556-Asn559, Gly593, Thr609-Ala612, Gly780-Glu818, and Glu1064-Pro1140 could not be modelled because of missing of the corresponding electron density [25].","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T17:28:28.001Z"}},{"start":1,"end":32,"reference_id":"37922785","reference_source":"pmid","reference_html":"Crystal structure of the in-cell Cry1Aa purified from Bacillus thuringiensis. <i> Tanaka J, Abe S, Hayakawa T, Kojima M, Yamashita K, Hirata K, Ueno T. </i> Biochem Biophys Res Commun, 2023","date":"2025-04-22T14:22:10.438Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"8W7N"}],"region_id":"DP04372r002","statement":[{"text":"Disordered regions indicating the location of cysteine residues are shown in gray font (Met1-Gly32, Gly780-Glu818, Glu1064-Pro1140).","type":"Figure"},{"text":"The residues of Met1-Gly32, Ile369-Asn377, Gly442-Val444, Ser556-Asn559, Gly593, Thr609-Ala612, Gly780-Glu818, and Glu1064-Pro1140 could not be modelled because of missing of the corresponding electron density [25].","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T17:28:16.722Z"}},{"start":1064,"end":1136,"reference_id":"37922785","reference_source":"pmid","reference_html":"Crystal structure of the in-cell Cry1Aa purified from Bacillus thuringiensis. <i> Tanaka J, Abe S, Hayakawa T, Kojima M, Yamashita K, Hirata K, Ueno T. </i> Biochem Biophys Res Commun, 2023","date":"2025-04-28T09:35:53.105Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"8W7N"}],"region_id":"DP04372r003","statement":[{"text":"Disordered regions indicating the location of cysteine residues are shown in gray font (Met1-Gly32, Gly780-Glu818, Glu1064-Pro1140).","type":"Figure"},{"text":"The residues of Met1-Gly32, Ile369-Asn377, Gly442-Val444, Ser556-Asn559, Gly593, Thr609-Ala612, Gly780-Glu818, and Glu1064-Pro1140 could not be modelled because of missing of the corresponding electron density [25].","type":"Methods"},{"text":"The disordered region described in the publication (Glu1064-Pro1140) corresponds to residues [1064–1136] in the UniProt sequence.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T17:28:09.170Z"}},{"start":1,"end":32,"reference_id":"37922785","reference_source":"pmid","reference_html":"Crystal structure of the in-cell Cry1Aa purified from Bacillus thuringiensis. <i> Tanaka J, Abe S, Hayakawa T, Kojima M, Yamashita K, Hirata K, Ueno T. </i> Biochem Biophys Res Commun, 2023","date":"2025-05-19T07:46:46.349Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"8W7N"}],"region_id":"DP04372r004","statement":[{"text":"Disordered regions indicating the location of cysteine residues are shown in gray font (Met1-Gly32, Gly780-Glu818, Glu1064-Pro1140).","type":"Figure"},{"text":"The residues of Met1-Gly32, Ile369-Asn377, Gly442-Val444, Ser556-Asn559, Gly593, Thr609-Ala612, Gly780-Glu818, and Glu1064-Pro1140 could not be modelled because of missing of the corresponding electron density [25].","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T17:28:31.091Z"}}],"regions_counter":4,"released":"2025_06","sequence":"MDNNPNINECIPYNCLSNPEVEVLGGERIETGYTPIDISLSLTQFLLSEFVPGAGFVLGLVDIIWGIFGPSQWDAFLVQIEQLINQRIEEFARNQAISRLEGLSNLYQIYAESFREWEADPTNPALREEMRIQFNDMNSALTTAIPLFAVQNYQVPLLSVYVQAANLHLSVLRDVSVFGQRWGFDAATINSRYNDLTRLIGNYTDYAVRWYNTGLERVWGPDSRDWVRYNQFRRELTLTVLDIVALFSNYDSRRYPIRTVSQLTREIYTNPVLENFDGSFRGMAQRIEQNIRQPHLMDILNSITIYTDVHRGFNYWSGHQITASPVGFSGPEFAFPLFGNAGNAAPPVLVSLTGLGIFRTLSSPLYRRIILGSGPNNQELFVLDGTEFSFASLTTNLPSTIYRQRGTVDSLDVIPPQDNSVPPRAGFSHRLSHVTMLSQAAGAVYTLRAPTFSWQHRSAEFNNIIPSSQITQIPLTKSTNLGSGTSVVKGPGFTGGDILRRTSPGQISTLRVNITAPLSQRYRVRIRYASTTNLQFHTSIDGRPINQGNFSATMSSGSNLQSGSFRTVGFTTPFNFSNGSSVFTLSAHVFNSGNEVYIDRIEFVPAEVTFEAEYDLERAQKAVNELFTSSNQIGLKTDVTDYHIDQVSNLVECLSDEFCLDEKQELSEKVKHAKRLSDERNLLQDPNFRGINRQLDRGWRGSTDITIQGGDDVFKENYVTLLGTFDECYPTYLYQKIDESKLKAYTRYQLRGYIEDSQDLEIYLIRYNAKHETVNVPGTGSLWPLSAQSPIGKCGEPNRCAPHLEWNPDLDCSCRDGEKCAHHSHHFSLDIDVGCTDLNEDLGVWVIFKIKTQDGHARLGNLEFLEEKPLVGEALARVKRAEKKWRDKREKLEWETNIVYKEAKESVDALFVNSQYDQLQADTNIAMIHAADKRVHSIREAYLPELSVIPGVNAAIFEELEGRIFTAFSLYDARNVIKNGDFNNGLSCWNVKGHVDVEEQNNQRSVLVVPEWEAEVSQEVRVCPGRGYILRVTAYKEGYGEGCVTIHEIENNTDELKFSNCVEEEIYPNNTVTCNDYTVNQEEYGGAYTSRNRGYNEAPSVPADYASVYEEKSYTDGRRENPCEFNRGYRDYTPLPVGYVTKELEYFPETDKVWIEIGETEGTFIVDSVELLLMEE","taxonomy":["Bacteria","Bacillati","Bacillota","Bacilli","Bacillales","Bacillaceae","Bacillus","Bacillus cereus group"],"alphafold_very_low_content":0.12244897959183673,"dataset":["Unicellular toxins and antitoxins","Bacterial virulence-related proteins"],"disorder_content":0.12244897959183673,"disprot_consensus":{"full":[{"start":1,"end":32,"type":"D"},{"start":780,"end":818,"type":"D"},{"start":1064,"end":1136,"type":"D"}],"Structural state":[{"start":1,"end":32,"type":"D"},{"start":780,"end":818,"type":"D"},{"start":1064,"end":1136,"type":"D"}],"Disorder function":[{"start":1,"end":32,"type":"F"}]}},{"disprot_id":"DP04373","acc":"P9WI79","creator":"xcastro","date":"2025-04-22T15:02:06.432Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":15,"end":262},{"id":"PF01436","name":"NHL repeat","start":468,"end":489},{"id":"PF01436","name":"NHL repeat","start":509,"end":535},{"id":"PF01436","name":"NHL repeat","start":551,"end":577},{"id":"PF01436","name":"NHL repeat","start":596,"end":619},{"id":"PF01436","name":"NHL repeat","start":635,"end":661}],"gene3D":[]},"genes":[{"name":{"value":"pknD"},"orfNames":[{"value":"MTCY08C9.08"}],"olnNames":[{"value":"Rv0931c"}]}],"length":664,"name":"Serine/threonine-protein kinase PknD","ncbi_taxon_id":83332,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","regions":[{"start":403,"end":413,"reference_id":"15136047","reference_source":"pmid","reference_html":"Sensor domain of the Mycobacterium tuberculosis receptor Ser/Thr protein kinase, PknD, forms a highly symmetric beta propeller. <i> Good MC, Greenstein AE, Young TA, Ng HL, Alber T. </i> J Mol Biol, 2004","date":"2025-06-17T09:11:54.563Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"1RWI"},{"db":"PDB","id":"1RWL"}],"region_id":"DP04373r001","statement":[{"text":"Two regions of the structure were disordered in all three independent monomers: a four amino acid loop (455–458) in blade 1 and the N-terminal 11 residues (403–413) that connect the sensor domain to the transmembrane domain.","type":"Results"},{"text":"In contrast, the 11 N-terminal residues were disordered in both crystal forms.","type":"Results"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Results","text":"To characterize the sensor domain, we expressed and purified Mtb PknD residues 403–664. This sequence starts at the first charged residue following the predicted transmembrane helix. The expressed protein included a C-terminal His6 tag that was not removed."}]}],"sequence_construct":"RPSWSPTQASGQTVLPFTGIDFRLSPSGVAVDSAGNVYVTSEGMYGRVVKLATGSTGTTVLPFNGLYQPQGLAVDGAGTVYVTDFNNRVVTLAAGSNNQTVLPFDGLNYPEGLAVDTQGAVYVADRGNNRVVKLAAGSKTQTVLPFTGLNDPDGVAVDNSGNVYVTDTDNNRVVKLEAESNNQVVLPFTDITAPWGIAVDEAGTVYVTEHNTNQVVKLLAGSTTSTVLPFTGLNTPLAVAVDSDRTVYVADRGNDRVVKLTSLEHHHHHH","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":50,"db":"ChEBI","id":"48775","statements":[{"type":"Methods","text":"The PknD sensor domain (20 mg ml−1) was crystallized at 22 °C by vapor diffusion in hanging drops against 0.8 M sodium acetate (NaOAc), 0.1 M Hepes (pH 8.0) 0.05 M CdSO4."}],"entry_name":"cadmium(2+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-17T15:51:51.520Z"}},{"start":403,"end":413,"reference_id":"15136047","reference_source":"pmid","reference_html":"Sensor domain of the Mycobacterium tuberculosis receptor Ser/Thr protein kinase, PknD, forms a highly symmetric beta propeller. <i> Good MC, Greenstein AE, Young TA, Ng HL, Alber T. </i> J Mol Biol, 2004","date":"2025-06-17T09:12:47.983Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"1RWI"},{"db":"PDB","id":"1RWL"}],"region_id":"DP04373r002","statement":[{"text":"Two regions of the structure were disordered in all three independent monomers: a four amino acid loop (455–458) in blade 1 and the N-terminal 11 residues (403–413) that connect the sensor domain to the transmembrane domain.","type":"Results"},{"text":"Moreover, although the PknD sensor domain construct begins at the first residue following the predicted transmembrane helix, the first 11 residues of the sensor domain are disordered in all three independent monomers. This disorder suggests that the sensor domain is tethered flexibly to the transmembrane domain.","type":"Discussion"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Results","text":"To characterize the sensor domain, we expressed and purified Mtb PknD residues 403–664. This sequence starts at the first charged residue following the predicted transmembrane helix. The expressed protein included a C-terminal His6 tag that was not removed."}]}],"sequence_construct":"RPSWSPTQASGQTVLPFTGIDFRLSPSGVAVDSAGNVYVTSEGMYGRVVKLATGSTGTTVLPFNGLYQPQGLAVDGAGTVYVTDFNNRVVTLAAGSNNQTVLPFDGLNYPEGLAVDTQGAVYVADRGNNRVVKLAAGSKTQTVLPFTGLNDPDGVAVDNSGNVYVTDTDNNRVVKLEAESNNQVVLPFTDITAPWGIAVDEAGTVYVTEHNTNQVVKLLAGSTTSTVLPFTGLNTPLAVAVDSDRTVYVADRGNDRVVKLTSLEHHHHHH","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":50,"db":"ChEBI","id":"48775","statements":[{"type":"Methods","text":"The PknD sensor domain (20 mg ml−1) was crystallized at 22 °C by vapor diffusion in hanging drops against 0.8 M sodium acetate (NaOAc), 0.1 M Hepes (pH 8.0) 0.05 M CdSO4."}],"entry_name":"cadmium(2+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-17T15:51:51.212Z"}}],"regions_counter":2,"released":"2025_06","sequence":"MSDAVPQVGSQFGPYQLLRLLGRGGMGEVYEAEDTRKHRVVALKLISPQYSDNAVFRARMQREADTAGRLTEPHIVPIHDYGEINGQFFVEMRMIDGTSLRALLKQYGPLTPARAVAIVRQIAAALDAAHANGVTHRDVKPENILVTASDFAYLVDFGIARAASDPGLTQTGTAVGTYNYMAPERFTGDEVTYRADIYALACVLGECLTGAPPYRADSVERLIAAHLMDPAPQPSQLRPGRVPPALDQVIAKGMAKNPAERFMSAGDLAIAAHDALTTSEQHQATTILRRGDNATLLATPADTGLSQSESGIAGAGTGPPTPGAARWSPGDSATVAGPLAADSRGGNWPSQTGHSPAVPNALQASLGHAVPPAGNKRKVWAVVGAAAIVLVAIVAAAGYLVLRPSWSPTQASGQTVLPFTGIDFRLSPSGVAVDSAGNVYVTSEGMYGRVVKLATGSTGTTVLPFNGLYQPQGLAVDGAGTVYVTDFNNRVVTLAAGSNNQTVLPFDGLNYPEGLAVDTQGAVYVADRGNNRVVKLAAGSKTQTVLPFTGLNDPDGVAVDNSGNVYVTDTDNNRVVKLEAESNNQVVLPFTDITAPWGIAVDEAGTVYVTEHNTNQVVKLLAGSTTSTVLPFTGLNTPLAVAVDSDRTVYVADRGNDRVVKLTS","taxonomy":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"alphafold_very_low_content":0.1716867469879518,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.016566265060240965,"disprot_consensus":{"full":[{"start":403,"end":413,"type":"D"}],"Structural state":[{"start":403,"end":413,"type":"D"}],"Disorder function":[{"start":403,"end":413,"type":"F"}]}},{"disprot_id":"DP04375","acc":"P71875","creator":"xcastro","date":"2025-04-23T11:57:46.995Z","features":{"pfam":[{"id":"PF00355","name":"Rieske [2Fe-2S] domain","start":26,"end":109},{"id":"PF19298","name":"3-Ketosteroid 9alpha-hydroxylase C-terminal domain","start":128,"end":337}],"gene3D":[]},"genes":[{"name":{"value":"kshA"},"olnNames":[{"value":"Rv3526"}]}],"length":386,"name":"3-ketosteroid-9-alpha-monooxygenase, oxygenase component","ncbi_taxon_id":83332,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","regions":[{"start":211,"end":224,"reference_id":"25049233","reference_source":"pmid","reference_html":"Substrate specificities and conformational flexibility of 3-ketosteroid 9α-hydroxylases. <i> Penfield JS, Worrall LJ, Strynadka NC, Eltis LD. </i> J Biol Chem, 2014","date":"2025-06-17T09:19:35.476Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":7.5,"statements":[{"type":"Methods","text":"Crystals of KshA were grown aerobically at room temperature (21 °C) using the hanging drop vapor diffusion method. Drops of 1 μl contained a 1:1 ratio of 200–300 μm KshA (in 25 mm HEPES, pH 7.5, substrate (ADD or 1,4-BNC-CoA), 0.25 mm FAS, 1 mm DTT or tris(2-carboxyethyl)phosphine) and crystallization well solution."}]}],"cross_refs":[{"db":"PDB","id":"4QCK"}],"region_id":"DP04375r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:2193","statements":[{"type":"Methods","text":"Crystals of KshA were grown aerobically at room temperature (21 °C) using the hanging drop vapor diffusion method. Drops of 1 μl contained a 1:1 ratio of 200–300 μm KshA (in 25 mm HEPES, pH 7.5, substrate (ADD or 1,4-BNC-CoA), 0.25 mm FAS, 1 mm DTT or tris(2-carboxyethyl)phosphine) and crystallization well solution."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29034","entry_name":"iron(3+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18367","entry_name":"phosphate(3-)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"49601","entry_name":"Fe2S2 iron-sulfur cluster"}],"statement":[{"text":"The final model of the complex contains residues 14–375 except for residues 216–222 of the mouth loop.","type":"Results"},{"text":"The 15-residue loop between strands β14 and β15, which partly seals off the pocket in the substrate-free structure, is disordered in the ADD-bound structure. It is possible that this loop has multiple conformations in the presence of ADD.","type":"Results"},{"text":"The exact residue numbers of the \"mouth loop\" were not explicitly provided in the publication. However, the authors describe it as a \"15-residue loop between strands β14 and β15.\" Based on inspection of the referenced structure, this corresponds to residues 211–224, which span the loop connecting β14 and β15.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-17T15:52:24.117Z"}},{"start":1,"end":13,"reference_id":"25049233","reference_source":"pmid","reference_html":"Substrate specificities and conformational flexibility of 3-ketosteroid 9α-hydroxylases. <i> Penfield JS, Worrall LJ, Strynadka NC, Eltis LD. </i> J Biol Chem, 2014","date":"2025-06-05T17:46:51.547Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"4QCK"}],"region_id":"DP04375r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29034","entry_name":"iron(3+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18367","entry_name":"phosphate(3-)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"49601","entry_name":"Fe2S2 iron-sulfur cluster"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:2193"}],"statement":[{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":1,"end":13,"reference_id":"25049233","reference_source":"pmid","reference_html":"Substrate specificities and conformational flexibility of 3-ketosteroid 9α-hydroxylases. <i> Penfield JS, Worrall LJ, Strynadka NC, Eltis LD. </i> J Biol Chem, 2014","date":"2025-06-05T17:47:01.665Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"4QCK"}],"region_id":"DP04375r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29034","entry_name":"iron(3+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18367","entry_name":"phosphate(3-)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"49601","entry_name":"Fe2S2 iron-sulfur cluster"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:2193"}],"statement":[{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":375,"end":386,"reference_id":"25049233","reference_source":"pmid","reference_html":"Substrate specificities and conformational flexibility of 3-ketosteroid 9α-hydroxylases. <i> Penfield JS, Worrall LJ, Strynadka NC, Eltis LD. </i> J Biol Chem, 2014","date":"2025-06-05T17:47:20.546Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"4QCK"}],"region_id":"DP04375r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29034","entry_name":"iron(3+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18367","entry_name":"phosphate(3-)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"49601","entry_name":"Fe2S2 iron-sulfur cluster"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:2193"}],"statement":[{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":375,"end":386,"reference_id":"25049233","reference_source":"pmid","reference_html":"Substrate specificities and conformational flexibility of 3-ketosteroid 9α-hydroxylases. <i> Penfield JS, Worrall LJ, Strynadka NC, Eltis LD. </i> J Biol Chem, 2014","date":"2025-06-05T17:47:25.780Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"4QCK"}],"region_id":"DP04375r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29034","entry_name":"iron(3+)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18367","entry_name":"phosphate(3-)"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"49601","entry_name":"Fe2S2 iron-sulfur cluster"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"CID:2193"}],"statement":[{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"regions_counter":5,"released":"2025_06","sequence":"MSTDTSGVGVREIDAGALPTRYARGWHCLGVAKDYLEGKPHGVEAFGTKLVVFADSHGDLKVLDGYCRHMGGDLSEGTVKGDEVACPFHDWRWGGDGRCKLVPYARRTPRMARTRSWTTDVRSGLLFVWHDHEGNPPDPAVRIPEIPEAASDEWTDWRWNRILIEGSNCRDIIDNVTDMAHFFYIHFGLPTYFKNVFEGHIASQYLHNVGRPDVDDLGTSYGEAHLDSEASYFGPSFMINWLHNRYGNYKSESILINCHYPVTQNSFVLQWGVIVEKPKGMSEEMTDKLSRVFTEGVSKGFLQDVEIWKHKTRIDNPLLVEEDGAVYQLRRWYEQFYVDVADIKPEMVERFEIEVDTKRANEFWNAEVEKNLKSREVSDDVPAEQH","taxonomy":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"alphafold_very_low_content":0.018134715025906734,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.10103626943005181,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"D"},{"start":211,"end":224,"type":"D"},{"start":375,"end":386,"type":"D"}],"Structural state":[{"start":1,"end":13,"type":"D"},{"start":211,"end":224,"type":"D"},{"start":375,"end":386,"type":"D"}],"Disorder function":[{"start":1,"end":13,"type":"F"},{"start":375,"end":386,"type":"F"}]}},{"disprot_id":"DP04376","acc":"Q9I0F4","creator":"xcastro","date":"2025-04-23T13:22:37.774Z","features":{"pfam":[{"id":"PF03527","name":"RHS protein","start":1065,"end":1102},{"id":"PF05593","name":"RHS Repeat","start":381,"end":414},{"id":"PF05593","name":"RHS Repeat","start":489,"end":525},{"id":"PF05593","name":"RHS Repeat","start":531,"end":567},{"id":"PF05593","name":"RHS Repeat","start":594,"end":630},{"id":"PF05593","name":"RHS Repeat","start":636,"end":670},{"id":"PF05593","name":"RHS Repeat","start":927,"end":965},{"id":"PF20148","name":"Domain of unknown function (DUF6531)","start":46,"end":120}],"gene3D":[]},"genes":[{"name":{"value":"tse5","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"24794869","url":"http://www.ncbi.nlm.nih.gov/pubmed/24794869","alternativeUrl":"https://europepmc.org/abstract/MED/24794869"}}]},"olnNames":[{"value":"PA2684"}]}],"length":1317,"name":"Toxin protein Tse5","ncbi_taxon_id":208964,"organism":"Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)","regions":[{"start":1,"end":29,"reference_id":"38016939","reference_source":"pmid","reference_html":"Structural and functional insights into the delivery of a bacterial Rhs pore-forming toxin to the membrane. <i> González-Magaña A, Tascón I, Altuna-Alvarez J, Queralt-Martín M, Colautti J, Velázquez C, Zabala M, Rojas-Palomino J, Cárdenas M, Alcaraz A, Whitney JC, Ubarretxena-Belandia I, Albesa-Jové D. </i> Nat Commun, 2023","date":"2025-04-23T13:49:57.479Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"8CP6"},{"db":"EMDB","id":"16778"}],"region_id":"DP04376r001","statement":[{"text":"The cryo-EM density map was of high quality, allowing the ab initio model building of the structure except for residues 1–29, 873–909 and 1196–1317, as a result of their structural flexibility or disorder (Fig. 1b, Supplementary Fig. 1).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-09T15:40:15.350Z"}},{"start":873,"end":909,"reference_id":"38016939","reference_source":"pmid","reference_html":"Structural and functional insights into the delivery of a bacterial Rhs pore-forming toxin to the membrane. <i> González-Magaña A, Tascón I, Altuna-Alvarez J, Queralt-Martín M, Colautti J, Velázquez C, Zabala M, Rojas-Palomino J, Cárdenas M, Alcaraz A, Whitney JC, Ubarretxena-Belandia I, Albesa-Jové D. </i> Nat Commun, 2023","date":"2025-04-23T13:50:54.374Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"8CP6"},{"db":"EMDB","id":"16778"}],"region_id":"DP04376r002","statement":[{"text":"The cryo-EM density map was of high quality, allowing the ab initio model building of the structure except for residues 1–29, 873–909 and 1196–1317, as a result of their structural flexibility or disorder (Fig. 1b, Supplementary Fig. 1).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-09T15:40:01.719Z"}},{"start":1196,"end":1317,"reference_id":"38016939","reference_source":"pmid","reference_html":"Structural and functional insights into the delivery of a bacterial Rhs pore-forming toxin to the membrane. <i> González-Magaña A, Tascón I, Altuna-Alvarez J, Queralt-Martín M, Colautti J, Velázquez C, Zabala M, Rojas-Palomino J, Cárdenas M, Alcaraz A, Whitney JC, Ubarretxena-Belandia I, Albesa-Jové D. </i> Nat Commun, 2023","date":"2025-04-23T13:55:30.237Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"8CP6"},{"db":"EMDB","id":"16778"}],"region_id":"DP04376r003","statement":[{"text":"The cryo-EM density map was of high quality, allowing the ab initio model building of the structure except for residues 1–29, 873–909 and 1196–1317, as a result of their structural flexibility or disorder (Fig. 1b, Supplementary Fig. 1).","type":"Results"},{"text":"For Tse5-CT (residues 1169–1317), we could only assign the first 27 N-terminal residues (residues 1169–1195) inside the Tse5-Shell cavity. The cryo-EM density inside the Tse5-Shell cavity for the remaining C-terminal 1196–1317 residues of Tse5-CT was too weak (Supplementary Fig. 3a). Such weak density is consistent with the encapsulated Tse5-CT remaining mostly flexible or disordered, in agreement with cryo-EM maps of Rhs11 and RhsA2 where only 10% and 23% of their encapsulated C-terminal toxin fragments could be resolved, respectively.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-09T15:39:39.890Z"}},{"start":1196,"end":1317,"reference_id":"38016939","reference_source":"pmid","reference_html":"Structural and functional insights into the delivery of a bacterial Rhs pore-forming toxin to the membrane. <i> González-Magaña A, Tascón I, Altuna-Alvarez J, Queralt-Martín M, Colautti J, Velázquez C, Zabala M, Rojas-Palomino J, Cárdenas M, Alcaraz A, Whitney JC, Ubarretxena-Belandia I, Albesa-Jové D. </i> Nat Commun, 2023","date":"2025-05-19T08:19:28.316Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"8CP6"},{"db":"EMDB","id":"16778"}],"region_id":"DP04376r005","statement":[{"text":"The cryo-EM density map was of high quality, allowing the ab initio model building of the structure except for residues 1–29, 873–909 and 1196–1317, as a result of their structural flexibility or disorder (Fig. 1b, Supplementary Fig. 1).","type":"Results"},{"text":"For Tse5-CT (residues 1169–1317), we could only assign the first 27 N-terminal residues (residues 1169–1195) inside the Tse5-Shell cavity. The cryo-EM density inside the Tse5-Shell cavity for the remaining C-terminal 1196–1317 residues of Tse5-CT was too weak (Supplementary Fig. 3a). Such weak density is consistent with the encapsulated Tse5-CT remaining mostly flexible or disordered, in agreement with cryo-EM maps of Rhs11 and RhsA2 where only 10% and 23% of their encapsulated C-terminal toxin fragments could be resolved, respectively.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-09T15:40:22.598Z"}}],"regions_counter":5,"released":"2025_06","sequence":"MSGLPVSHVGEKVSGGVISTGSPTVHVGSSAVGLADRVSACVPLVGKPVNPMLGSKLLPEEVDFALAAPDTFTFARGYLSSNPRIGRLGRGWWLPGESMHLELSEDACVLVDAQGRRIGFPALAPGAQHYSGSEELWLRRGGSSGGEAQAWRGRWAAVPAELQTQEGSVLVLSGHSYLHFQRCPDGIWRLQASFGRAGYRTEFRWSGRGLLTGVRDSAGRSYALVYQQACEPSEGDDGLRLFGVILASHDGPPPDYIDPQSPGLDWLVRYQFSDSGDLIAVRDRLGQVVRVFAWREHMLVAHGEPGGLEVRYEWDVHAPHGRVVKQIEAGGLTRTFRYLRDATEVSDSLGRVERYEFAGEGGQRRWTALVRADGSRSEFDYDLFGRLVAMRDPLGRETRRRRDGQGRMLEEESPGKARYRKRVDEETGLLVELEDAMQRRWTFERDERGNATTVRGPAGSTRYAYEDPRLPDRPTRIVDPRGGERRLEWNRFGLLAALTDCSGQVWRYDYDNEGRLVASSDPLGQLTRRRYDPLGQLIGLELADGSALSYEYDALGRQTRIADAEGHATLFSWGHGDLLARVSDAGGGELSYLHDEAGRLVALTNENGVQAQFRYDLLDRLVEETGFDGRRQRYRYNAADELIAREDADGRETTYAYDRDGRLASIRVPATEHAPALVERYRWLADGRLASAGGADCEVRYTYDEVGNLRLESQVHADGWVYSVEHSHDALGVRQTSRYGDAPPVAWLTYGPGHLHGALVGAVELAFERDALHREVRRDARRDGQDDALFTQERQHAPLGRLQRSRLRLAGGFDWQRGYRYDGLGQLVGIDDNQYPSVRYEYDLGGRLLASRRAGAAASTYRYDAAGNRLEGVGEHAREDARQAFAENELYRSGFSRSETRASQAGEGPARWAGNRVERIAGNRYRFDALGNLVERIGADGERLRLAYDGAQRLVHLTRDYADGTRLEARYRYDALSRRIAKVVLRDGVEQQVRFGWDGDRQCAEAFARELRTTVHEPGGFVPLLRLEQACEPDPPELLQLRQAFAAEGQPLPAQCVPALGEARIAFFHTDHLGTPLQLSDERGQLRWQGVPDDWRAVAPERQPGAQPIRFQGQYHDEESGLYYNRYRYYLPEAGRYASQDPLGLGGGPNPYAYALNAPTLAYDPTGLIIPLVVIGAFAARAAIGAALGAGIELGMQTGKQVLGQMKDNWDSDRDLTDIKWKCIDINWKHVGASAAIGTVAPGMLSTGKTVVQSAKAIRTLSGQAANTANRAAKLAARKAAHADTIKKAVATQAAWQTGKQIVKCPLKDEEEECPPQ","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Pseudomonadales","Pseudomonadaceae","Pseudomonas"],"alphafold_very_low_content":0.16324981017463933,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.1427486712224753,"disprot_consensus":{"full":[{"start":1,"end":29,"type":"D"},{"start":873,"end":909,"type":"D"},{"start":1196,"end":1317,"type":"D"}],"Structural state":[{"start":1,"end":29,"type":"D"},{"start":873,"end":909,"type":"D"},{"start":1196,"end":1317,"type":"D"}],"Disorder function":[{"start":1196,"end":1317,"type":"F"}]}},{"disprot_id":"DP04377","acc":"Q51693","creator":"xcastro","date":"2025-04-24T07:31:43.962Z","features":{"pfam":[{"id":"PF01019","name":"Gamma-glutamyltranspeptidase","start":60,"end":523}],"gene3D":[]},"genes":[{"name":{"value":"capD"},"synonyms":[{"value":"dep"}],"olnNames":[{"value":"pXO2-55"},{"value":"BXB0063"},{"value":"GBAA_pXO2_0063"}]}],"length":528,"name":"Capsule biosynthesis protein CapD proenzyme","ncbi_taxon_id":1392,"organism":"Bacillus anthracis","regions":[{"start":336,"end":351,"reference_id":"19535342","reference_source":"pmid","reference_html":"Crystal structure of Bacillus anthracis transpeptidase enzyme CapD. <i> Wu R, Richter S, Zhang RG, Anderson VJ, Missiakas D, Joachimiak A. </i> J Biol Chem, 2009","date":"2025-06-17T10:06:36.913Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"3G9K"},{"db":"PDB","id":"3GA9"}],"region_id":"DP04377r001","statement":[{"text":"This crystal form contained two CapD molecules in the asymmetric unit, one with bound di-α-l-Glu and one unliganded (Table 2). Electron densities in both crystals were of high quality and generally continuous. Nevertheless, electron densities for residues 29–45 and 337–351, i.e. the first 17 and the last 15 residues of the L chain, and residue 528, the last residue of the S chain, were poorly defined, and these residues could not be modeled into the structure.","type":"Results"},{"text":"The P-segment, Cys336–Ser351, is disordered within the structure of CapD, as occurs with other Ntn hydrolases (36, 37).","type":"Discussion"}],"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":63,"end":63,"position":"Specific residue","statements":[{"type":"Results","text":"The structure of CapD was determined by single-wavelength anomalous diffraction phasing of the orthorhombic crystal form and SeMet-labeled protein using HKL3000 (29) and refined to 2.30 Å (R = 19.7%, Rfree = 25.2%) (Table 1)."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":99,"end":99,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":136,"end":136,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":148,"end":148,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":171,"end":171,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":257,"end":257,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":276,"end":276,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":296,"end":296,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":299,"end":299,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":322,"end":322,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":327,"end":327,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":336,"end":336,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":411,"end":411,"position":"Specific residue"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15966","statements":[{"type":"Results","text":"This crystal form contained one CapD molecule with bound l-Glu-l-Glu dipeptide (di-α-l-Glu), a non-hydrolyzable analog of poly-γ-d-glutamic acid, in the asymmetric unit."}],"entry_name":"D-glutamic acid"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-17T15:52:53.803Z"}},{"start":29,"end":45,"reference_id":"19535342","reference_source":"pmid","reference_html":"Crystal structure of Bacillus anthracis transpeptidase enzyme CapD. <i> Wu R, Richter S, Zhang RG, Anderson VJ, Missiakas D, Joachimiak A. </i> J Biol Chem, 2009","date":"2025-06-17T10:00:41.080Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"3G9K"},{"db":"PDB","id":"3GA9"}],"region_id":"DP04377r002","statement":[{"text":"This crystal form contained two CapD molecules in the asymmetric unit, one with bound di-α-l-Glu and one unliganded (Table 2). Electron densities in both crystals were of high quality and generally continuous. Nevertheless, electron densities for residues 29–45 and 337–351, i.e. the first 17 and the last 15 residues of the L chain, and residue 528, the last residue of the S chain, were poorly defined, and these residues could not be modeled into the structure.","type":"Results"}],"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":63,"end":63,"position":"Specific residue","statements":[{"type":"Results","text":"The structure of CapD was determined by single-wavelength anomalous diffraction phasing of the orthorhombic crystal form and SeMet-labeled protein using HKL3000 (29) and refined to 2.30 Å (R = 19.7%, Rfree = 25.2%) (Table 1)."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":99,"end":99,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":136,"end":136,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":148,"end":148,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":171,"end":171,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":257,"end":257,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":276,"end":276,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":296,"end":296,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":299,"end":299,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":322,"end":322,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":327,"end":327,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":336,"end":336,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":411,"end":411,"position":"Specific residue"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15966","statements":[{"type":"Results","text":"This crystal form contained one CapD molecule with bound l-Glu-l-Glu dipeptide (di-α-l-Glu), a non-hydrolyzable analog of poly-γ-d-glutamic acid, in the asymmetric unit."}],"entry_name":"D-glutamic acid"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-17T15:52:54.625Z"}}],"regions_counter":2,"released":"2025_06","sequence":"MNSFKWGKKIILFCLIVSLMGGIGVSCSFNKIKDSVKQKIDSMGDKGTYGVSASHPLAVEEGMKVLKNGGSAVDAAIVVSYVLGVVELHASGIGGGGGMLIISKDKETFIDYRETTPYFTGNQKPHIGVPGFVAGMEYIHDNYGSLPMGELLQPAINYAEKGFKVDDSLTMRLDLAKPRIYSDKLSIFYPNGEPIETGETLIQTDLARTLKKIQKEGAKGFYEGGVARAISKTAKISLEDIKGYKVEVRKPVKGNYMGYDVYTAPPPFSGVTLLQMLKLAEKKEVYKDVDHTATYMSKMEEISRIAYQDRKKNLGDPNYVNMDPNKMVSDKYISTMKNENGDALSEAEHESTTHFVIIDRDGTVVSSTNTLSNFFGTGKYTAGFFLNNQLQNFGSEGFNSYEPGKRSRTFMAPTVLKKDGETIGIGSPGGNRIPQILTPILDKYTHGKGSLQDIINEYRFTFEKNTAYTEIQLSSEVKNELSRKGLNVKKKVSPAFFGGVQALIKDERDNVITGAGDGRRNGTWKSNK","taxonomy":["Bacteria","Bacillati","Bacillota","Bacilli","Bacillales","Bacillaceae","Bacillus","Bacillus cereus group"],"alphafold_very_low_content":0.06818181818181818,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.0625,"disprot_consensus":{"full":[{"start":29,"end":45,"type":"D"},{"start":336,"end":351,"type":"D"}],"Structural state":[{"start":29,"end":45,"type":"D"},{"start":336,"end":351,"type":"D"}]}},{"disprot_id":"DP04378","acc":"O82882","creator":"xcastro","date":"2025-04-24T08:38:25.321Z","features":{"pfam":[{"id":"PF10462","name":"Peptidase M66","start":249,"end":549},{"id":"PF12561","name":"ToxR activated gene A lipoprotein domain","start":679,"end":774},{"id":"PF17945","name":"Beta/Gamma crystallin","start":807,"end":896},{"id":"PF20944","name":"Metalloprotease StcE, beta-sandwich domain","start":178,"end":244},{"id":"PF20944","name":"Metalloprotease StcE, beta-sandwich domain","start":602,"end":668}],"gene3D":[]},"genes":[{"name":{"value":"stcE"},"synonyms":[{"value":"tagA"}],"olnNames":[{"value":"L7031"},{"value":"ECO57PM83"}]}],"length":898,"name":"Metalloprotease StcE","ncbi_taxon_id":83334,"organism":"Escherichia coli O157:H7","regions":[{"start":138,"end":247,"reference_id":"22483117","reference_source":"pmid","reference_html":"Structural insight into the bacterial mucinase StcE essential to adhesion and immune evasion during enterohemorrhagic E. coli infection. <i> Yu AC, Worrall LJ, Strynadka NC. </i> Structure, 2012","date":"2025-06-18T07:32:01.193Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys318Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Initial needle clusters were obtained from StcEΔ35E447D. After various attempts to improve the diffraction quality, larger crystals of the quadruple mutant K318A/K320A/E321A/E447D were grown by the hanging-drop method at 18°C."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys320Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Initial needle clusters were obtained from StcEΔ35E447D. After various attempts to improve the diffraction quality, larger crystals of the quadruple mutant K318A/K320A/E321A/E447D were grown by the hanging-drop method at 18°C."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu321Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Initial needle clusters were obtained from StcEΔ35E447D. After various attempts to improve the diffraction quality, larger crystals of the quadruple mutant K318A/K320A/E321A/E447D were grown by the hanging-drop method at 18°C."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu447Asp","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Initial needle clusters were obtained from StcEΔ35E447D. After various attempts to improve the diffraction quality, larger crystals of the quadruple mutant K318A/K320A/E321A/E447D were grown by the hanging-drop method at 18°C."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":306,"end":306,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":335,"end":335,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":349,"end":349,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":359,"end":359,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":371,"end":371,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":518,"end":518,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":532,"end":532,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":569,"end":569,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":594,"end":594,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":598,"end":598,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":608,"end":608,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":709,"end":709,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":754,"end":754,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":874,"end":874,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":893,"end":893,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":205,"end":205,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"3UJZ"}],"region_id":"DP04378r001","sequence_construct":"GSHMASADNNSAIYFNTSQPINDLQGSLAAEVKFAQSQILPAHPKEGDSQPHLTSLRKSLLLVRPVKADDKTPVQVEARDDNNKILGTLTLYPPSSLPDTIYHLDGVPEGGIDFTPHNGTKKIINTVAEVNKLSDASGSSIHSHLTNNALVEIHTANGRWVRDIYLPQGPDLEGKMVRFVSSAGYSSTVFYGDRKVTLSVGNTLLFKYVNGQWFRSGELENNRITYAQHIWSAELPAHWIVPGLNLVIKQGNLSGRLNDIKIGAPGELLLHTIDIGMLTTPRDRFDFAADAAAHREYFQTIPVSRMIVNNYAPLHLKEVMLPTGELLTDMDPGNGGWHSGTMRQRIGKELVSHGIDNANYGLNSTAGLGENSHPYVVAQLAAHNSRGNYANGIQVHGGSGGGGIVTLDSTLGNEFSHDVGHNYGLGHYVDGFKGSVHRSAENNNSTWGWDGDKKRFIPNFYPSQTNEKSCLNNQCQEPFDGHKFGFDAMAGGSPFSAANRFTMYTPNSSAIIQRFFENKAVFDSRSSTGFSKWNADTQEMEPYEHTIDRAEQITASVNELSESKMAELMAEYAVVKVHMWNGNWTRNIYIPTASADNRGSILTINHEAGYNSYLFINGDEKVVSQGYKKSFVSDGQFWKERDVVDTREARKPEQFGVPVTTLVGYYDPEGTLSSYIYPAMYGAYGFTYSDDSQNLSDNDCQLQVDTKEGQLRFRLANHRANNTVMNKFHINVPTESQPTQATLVCNNKILDTKSLTPAPEGLTYTVNGQALPAKENEGCIVSVNSGKRYCLPVGQRSGYSLPDWIVGQEVYVDSGAKAKVLLSDWDNLSYNRIGEFVGNVNPADMKKVKAWNGQYLDFSKPRSMRVVYK","statement":[{"text":"The N-terminal domain IG adopts an immunoglobulin-like fold that consists of complementary segments spanning residues 57–122 and 257–287. Within domain IG, a sequence-variable region with weak electron density, which we designate as INS (insertion residues Lys150-Ser245), inserts between strands 5 and 6 of the immunoglobulin β sandwich (Figures 1A and 1B; Figure S2 sequence alignment).","type":"Results"},{"text":"Extending in opposite directions away from this axis are disordered structural elements, INS and D1, spanning Arg578-Arg676 (as judged by residual density and weak anomalous signals likely reflecting SeMet594, 598, and 608 in region D1).","type":"Results"},{"text":"The fact that we did not observe well-ordered density for INS in our model suggests this region may adopt multiple conformations that contribute to the ability of StcE to capture a variety of complex substrates at the cell surface.","type":"Results"},{"text":"This annotation of disorder in this region should be interpreted with caution: although the authors describe the region as disordered and it is not resolved in the full-length protein structure, the insertion domain (INS) adopts a well-defined, stable fold when expressed and crystallized independently at high resolution. The lack of electron density in the full-length structure may reflect flexibility introduced by the flanking linker regions, rather than intrinsic disorder of the INS domain itself.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:33:11.773Z"}},{"start":150,"end":247,"reference_id":"22483117","reference_source":"pmid","reference_html":"Structural insight into the bacterial mucinase StcE essential to adhesion and immune evasion during enterohemorrhagic E. coli infection. <i> Yu AC, Worrall LJ, Strynadka NC. </i> Structure, 2012","date":"2025-06-18T08:01:11.700Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"4DNY"},{"db":"PDB","id":"3UJZ"}],"region_id":"DP04378r002","statement":[{"text":"The fact that we did not observe well-ordered density for INS in our model suggests this region may adopt multiple conformations that contribute to the ability of StcE to capture a variety of complex substrates at the cell surface. To explore this hypothesis further, we solved the structure of the isolated INS domain using an iodide soak SIRAS technique. Indeed, domain INS folds independently as a mixed, eight-stranded β sandwich with homology to the T4 bacteriophage structural protein gp9 (Z-score of 6.2) and contains an additional β strand followed by a perpendicular arrangement of two α helices in its N-terminal region.","type":"Results"},{"text":"Domain INS (H132-N251) was cloned using 5′-CCGCAGGCTAGCCATCTGGATGGTGTTCCGGAAG-3′ and 5′- CCGCAGCTCGAGTTAATTATTCTCCAGTTCACCGGAG-3′.","type":"Methods"},{"text":"While this region has been annotated as a transition between disorder and order—based on its absence in the full-length protein structure and its well-defined, stable fold when expressed independently—this interpretation should be approached with caution. The apparent disorder in the context of the full-length protein may instead arise from conformational flexibility introduced by adjacent linker regions, rather than from intrinsic disorder within the domain itself.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys318Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Initial needle clusters were obtained from StcEΔ35E447D. After various attempts to improve the diffraction quality, larger crystals of the quadruple mutant K318A/K320A/E321A/E447D were grown by the hanging-drop method at 18°C."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys320Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Initial needle clusters were obtained from StcEΔ35E447D. After various attempts to improve the diffraction quality, larger crystals of the quadruple mutant K318A/K320A/E321A/E447D were grown by the hanging-drop method at 18°C."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu321Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Initial needle clusters were obtained from StcEΔ35E447D. After various attempts to improve the diffraction quality, larger crystals of the quadruple mutant K318A/K320A/E321A/E447D were grown by the hanging-drop method at 18°C."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu447Asp","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Initial needle clusters were obtained from StcEΔ35E447D. After various attempts to improve the diffraction quality, larger crystals of the quadruple mutant K318A/K320A/E321A/E447D were grown by the hanging-drop method at 18°C."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":205,"end":205,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":306,"end":306,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":335,"end":335,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":349,"end":349,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":359,"end":359,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":371,"end":371,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":518,"end":518,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":532,"end":532,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":569,"end":569,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":594,"end":594,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":598,"end":598,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":608,"end":608,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":709,"end":709,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":754,"end":754,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":874,"end":874,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":893,"end":893,"position":"Specific residue"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16382","entry_name":"iodide"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:33:55.033Z"}},{"start":578,"end":676,"reference_id":"22483117","reference_source":"pmid","reference_html":"Structural insight into the bacterial mucinase StcE essential to adhesion and immune evasion during enterohemorrhagic E. coli infection. <i> Yu AC, Worrall LJ, Strynadka NC. </i> Structure, 2012","date":"2025-06-18T07:37:35.429Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys318Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Initial needle clusters were obtained from StcEΔ35E447D. After various attempts to improve the diffraction quality, larger crystals of the quadruple mutant K318A/K320A/E321A/E447D were grown by the hanging-drop method at 18°C."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys320Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Initial needle clusters were obtained from StcEΔ35E447D. After various attempts to improve the diffraction quality, larger crystals of the quadruple mutant K318A/K320A/E321A/E447D were grown by the hanging-drop method at 18°C."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu321Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Initial needle clusters were obtained from StcEΔ35E447D. After various attempts to improve the diffraction quality, larger crystals of the quadruple mutant K318A/K320A/E321A/E447D were grown by the hanging-drop method at 18°C."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu447Asp","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Initial needle clusters were obtained from StcEΔ35E447D. After various attempts to improve the diffraction quality, larger crystals of the quadruple mutant K318A/K320A/E321A/E447D were grown by the hanging-drop method at 18°C."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":205,"end":205,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":306,"end":306,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":335,"end":335,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":349,"end":349,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":359,"end":359,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":371,"end":371,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":518,"end":518,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":532,"end":532,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":569,"end":569,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":594,"end":594,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":598,"end":598,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":608,"end":608,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":709,"end":709,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":754,"end":754,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":874,"end":874,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":893,"end":893,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"3UJZ"}],"region_id":"DP04378r004","sequence_construct":"GSHMASADNNSAIYFNTSQPINDLQGSLAAEVKFAQSQILPAHPKEGDSQPHLTSLRKSLLLVRPVKADDKTPVQVEARDDNNKILGTLTLYPPSSLPDTIYHLDGVPEGGIDFTPHNGTKKIINTVAEVNKLSDASGSSIHSHLTNNALVEIHTANGRWVRDIYLPQGPDLEGKMVRFVSSAGYSSTVFYGDRKVTLSVGNTLLFKYVNGQWFRSGELENNRITYAQHIWSAELPAHWIVPGLNLVIKQGNLSGRLNDIKIGAPGELLLHTIDIGMLTTPRDRFDFAADAAAHREYFQTIPVSRMIVNNYAPLHLKEVMLPTGELLTDMDPGNGGWHSGTMRQRIGKELVSHGIDNANYGLNSTAGLGENSHPYVVAQLAAHNSRGNYANGIQVHGGSGGGGIVTLDSTLGNEFSHDVGHNYGLGHYVDGFKGSVHRSAENNNSTWGWDGDKKRFIPNFYPSQTNEKSCLNNQCQEPFDGHKFGFDAMAGGSPFSAANRFTMYTPNSSAIIQRFFENKAVFDSRSSTGFSKWNADTQEMEPYEHTIDRAEQITASVNELSESKMAELMAEYAVVKVHMWNGNWTRNIYIPTASADNRGSILTINHEAGYNSYLFINGDEKVVSQGYKKSFVSDGQFWKERDVVDTREARKPEQFGVPVTTLVGYYDPEGTLSSYIYPAMYGAYGFTYSDDSQNLSDNDCQLQVDTKEGQLRFRLANHRANNTVMNKFHINVPTESQPTQATLVCNNKILDTKSLTPAPEGLTYTVNGQALPAKENEGCIVSVNSGKRYCLPVGQRSGYSLPDWIVGQEVYVDSGAKAKVLLSDWDNLSYNRIGEFVGNVNPADMKKVKAWNGQYLDFSKPRSMRVVYK","statement":[{"text":"Extending in opposite directions away from this axis are disordered structural elements, INS and D1, spanning Arg578-Arg676 (as judged by residual density and weak anomalous signals likely reflecting SeMet594, 598, and 608 in region D1).","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-07-01T17:44:12.727Z"}},{"start":150,"end":247,"reference_id":"22483117","reference_source":"pmid","reference_html":"Structural insight into the bacterial mucinase StcE essential to adhesion and immune evasion during enterohemorrhagic E. coli infection. <i> Yu AC, Worrall LJ, Strynadka NC. </i> Structure, 2012","date":"2025-06-10T17:33:06.689Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04378r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16382","entry_name":null}],"statement":[{"text":"To explore this hypothesis further, we solved the structure of the isolated INS domain using an iodide soak SIRAS technique. Indeed, domain INS folds independently as a mixed, eight-stranded β sandwich with homology to the T4 bacteriophage structural protein gp9 (Z-score of 6.2) and contains an additional β strand followed by a perpendicular arrangement of two α helices in its N-terminal region. We then positioned the compact module in the context of the existing model to obtain a more complete description of the StcE structure and function (correct placement was confirmed by the anomalous signal of SeMet205). A long loop (His132-Lys150) links the N terminus of INS to domain IG and provides flexibility, placing the putative exosite domain ∼35 Å away from the catalytic center in our model (Figure 5A).","type":"Results"}],"cross_refs":[{"db":"PDB","id":"4DNY"}]},{"start":138,"end":150,"reference_id":"22483117","reference_source":"pmid","reference_html":"Structural insight into the bacterial mucinase StcE essential to adhesion and immune evasion during enterohemorrhagic E. coli infection. <i> Yu AC, Worrall LJ, Strynadka NC. </i> Structure, 2012","date":"2025-06-10T17:27:33.178Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04378r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16382","entry_name":null}],"statement":[{"text":"To explore this hypothesis further, we solved the structure of the isolated INS domain using an iodide soak SIRAS technique. Indeed, domain INS folds independently as a mixed, eight-stranded β sandwich with homology to the T4 bacteriophage structural protein gp9 (Z-score of 6.2) and contains an additional β strand followed by a perpendicular arrangement of two α helices in its N-terminal region. We then positioned the compact module in the context of the existing model to obtain a more complete description of the StcE structure and function (correct placement was confirmed by the anomalous signal of SeMet205). A long loop (His132-Lys150) links the N terminus of INS to domain IG and provides flexibility, placing the putative exosite domain ∼35 Å away from the catalytic center in our model (Figure 5A).","type":"Results"},{"text":"Being flexibly linked, domain INS may exist in various conformations to present a potential protein-binding interface relative to its respective targets.","type":"Results"}]},{"start":140,"end":243,"reference_id":"22483117","reference_source":"pmid","reference_html":"Structural insight into the bacterial mucinase StcE essential to adhesion and immune evasion during enterohemorrhagic E. coli infection. <i> Yu AC, Worrall LJ, Strynadka NC. </i> Structure, 2012","date":"2025-06-10T17:56:44.935Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008233","term_name":"peptidase activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"annotation_extensions":[{"operator":null,"relation":"has_input","value":"P05155"}],"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gly140Phe243del","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The insertion deletion (ΔG140-F243) was chosen to be consistent with the StcE model and secondary structure prediction and removed by QuickChange using 5′-GGATGGTGTTCCGGAAGGTCGCTCCGGTGAACTGGAG and 5′-CTCCAGTTCACCGGAGCGACCTTCCGGAACACCATCC"}]}],"ec_go":"IMP","region_id":"DP04378r007","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P05155"}],"statement":[{"text":"Curiously, the poorly resolved density corresponding to the INS region (Lys150-Ser245) appears to approach the active site (Figure 1B). We generated a truncation mutant of this sequence-variable region (ΔINS) (Figure S2) to test its involvement in substrate binding. ΔINS exhibited decreased proteolytic activity toward C1-INH compared to WT StcE (Figure 4A) (circular dichroism spectrum confirmed no large perturbation to the overall structure due to the mutation, as shown in Figures 4B and 4C).","type":"Results"}],"term_comment":"","term_def":"\"Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.\" [GOC:jl, ISBN:0815332181]","term_is_obsolete":false,"term_not_annotate":false},{"start":140,"end":243,"reference_id":"22483117","reference_source":"pmid","reference_html":"Structural insight into the bacterial mucinase StcE essential to adhesion and immune evasion during enterohemorrhagic E. coli infection. <i> Yu AC, Worrall LJ, Strynadka NC. </i> Structure, 2012","date":"2025-06-10T17:56:57.048Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006508","term_name":"proteolysis","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Gly140Phe243del","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The insertion deletion (ΔG140-F243) was chosen to be consistent with the StcE model and secondary structure prediction and removed by QuickChange using 5′-GGATGGTGTTCCGGAAGGTCGCTCCGGTGAACTGGAG and 5′-CTCCAGTTCACCGGAGCGACCTTCCGGAACACCATCC"}]}],"ec_go":"IMP","region_id":"DP04378r008","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P05155"}],"statement":[{"text":"Curiously, the poorly resolved density corresponding to the INS region (Lys150-Ser245) appears to approach the active site (Figure 1B). We generated a truncation mutant of this sequence-variable region (ΔINS) (Figure S2) to test its involvement in substrate binding. ΔINS exhibited decreased proteolytic activity toward C1-INH compared to WT StcE (Figure 4A) (circular dichroism spectrum confirmed no large perturbation to the overall structure due to the mutation, as shown in Figures 4B and 4C).","type":"Results"}],"term_comment":"This term was intentionally placed under 'protein metabolic process ; GO:0019538' rather than 'protein catabolic process ; GO:0030163' to cover all processes centered on breaking peptide bonds, including those involved in protein processing.","term_def":"\"The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.\" [GOC:bf, GOC:mah]","term_is_obsolete":false,"term_not_annotate":false},{"start":719,"end":753,"reference_id":"22483117","reference_source":"pmid","reference_html":"Structural insight into the bacterial mucinase StcE essential to adhesion and immune evasion during enterohemorrhagic E. coli infection. <i> Yu AC, Worrall LJ, Strynadka NC. </i> Structure, 2012","date":"2025-06-18T08:16:20.495Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys318Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Initial needle clusters were obtained from StcEΔ35E447D. After various attempts to improve the diffraction quality, larger crystals of the quadruple mutant K318A/K320A/E321A/E447D were grown by the hanging-drop method at 18°C."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys320Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Initial needle clusters were obtained from StcEΔ35E447D. After various attempts to improve the diffraction quality, larger crystals of the quadruple mutant K318A/K320A/E321A/E447D were grown by the hanging-drop method at 18°C."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu321Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Initial needle clusters were obtained from StcEΔ35E447D. After various attempts to improve the diffraction quality, larger crystals of the quadruple mutant K318A/K320A/E321A/E447D were grown by the hanging-drop method at 18°C."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu447Asp","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Initial needle clusters were obtained from StcEΔ35E447D. After various attempts to improve the diffraction quality, larger crystals of the quadruple mutant K318A/K320A/E321A/E447D were grown by the hanging-drop method at 18°C."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":205,"end":205,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":306,"end":306,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":335,"end":335,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":349,"end":349,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":359,"end":359,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":371,"end":371,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":518,"end":518,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":532,"end":532,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":569,"end":569,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":594,"end":594,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":598,"end":598,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":608,"end":608,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":709,"end":709,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":754,"end":754,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":874,"end":874,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":893,"end":893,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"3UJZ"}],"region_id":"DP04378r009","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"statement":[{"text":"A partially resolved region, residues 679–798 (D2), docks against M on the opposite face of the active site.","type":"Results"},{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:34:10.773Z"}}],"regions_counter":9,"released":"2025_06","sequence":"MNTKMNERWRTPMKLKYLSCTILAPLAIGVFSATAADNNSAIYFNTSQPINDLQGSLAAEVKFAQSQILPAHPKEGDSQPHLTSLRKSLLLVRPVKADDKTPVQVEARDDNNKILGTLTLYPPSSLPDTIYHLDGVPEGGIDFTPHNGTKKIINTVAEVNKLSDASGSSIHSHLTNNALVEIHTANGRWVRDIYLPQGPDLEGKMVRFVSSAGYSSTVFYGDRKVTLSVGNTLLFKYVNGQWFRSGELENNRITYAQHIWSAELPAHWIVPGLNLVIKQGNLSGRLNDIKIGAPGELLLHTIDIGMLTTPRDRFDFAKDKEAHREYFQTIPVSRMIVNNYAPLHLKEVMLPTGELLTDMDPGNGGWHSGTMRQRIGKELVSHGIDNANYGLNSTAGLGENSHPYVVAQLAAHNSRGNYANGIQVHGGSGGGGIVTLDSTLGNEFSHEVGHNYGLGHYVDGFKGSVHRSAENNNSTWGWDGDKKRFIPNFYPSQTNEKSCLNNQCQEPFDGHKFGFDAMAGGSPFSAANRFTMYTPNSSAIIQRFFENKAVFDSRSSTGFSKWNADTQEMEPYEHTIDRAEQITASVNELSESKMAELMAEYAVVKVHMWNGNWTRNIYIPTASADNRGSILTINHEAGYNSYLFINGDEKVVSQGYKKSFVSDGQFWKERDVVDTREARKPEQFGVPVTTLVGYYDPEGTLSSYIYPAMYGAYGFTYSDDSQNLSDNDCQLQVDTKEGQLRFRLANHRANNTVMNKFHINVPTESQPTQATLVCNNKILDTKSLTPAPEGLTYTVNGQALPAKENEGCIVSVNSGKRYCLPVGQRSGYSLPDWIVGQEVYVDSGAKAKVLLSDWDNLSYNRIGEFVGNVNPADMKKVKAWNGQYLDFSKPRSMRVVYK","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"alphafold_very_low_content":0.042316258351893093,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.2717149220489978,"disprot_consensus":{"full":[{"start":138,"end":149,"type":"D"},{"start":150,"end":247,"type":"T"},{"start":578,"end":676,"type":"D"},{"start":719,"end":753,"type":"D"}],"Structural state":[{"start":138,"end":247,"type":"D"},{"start":578,"end":676,"type":"D"},{"start":719,"end":753,"type":"D"}],"Structural transition":[{"start":150,"end":247,"type":"T"}],"Disorder function":[{"start":138,"end":150,"type":"F"}],"Molecular function":[{"start":140,"end":243,"type":"F"}],"Biological process":[{"start":140,"end":243,"type":"F"}]}},{"disprot_id":"DP04379","acc":"Q8DR55","creator":"rpancsa","date":"2025-04-24T10:57:51.038Z","features":{"pfam":[{"id":"PF18041","name":"MapZ extracellular domain 1","start":188,"end":311},{"id":"PF18708","name":"MapZ extracellular C-terminal domain 2","start":376,"end":454}],"gene3D":[]},"genes":[{"name":{"value":"mapZ","evidences":[{"code":"ECO:0000255","source":{"name":"HAMAP-Rule","id":"MF_01941","url":"https://hamap.expasy.org/unirule/MF_01941"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"25470041","url":"http://www.ncbi.nlm.nih.gov/pubmed/25470041","alternativeUrl":"https://europepmc.org/abstract/MED/25470041"}}]},"synonyms":[{"value":"locZ","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"25550321","url":"http://www.ncbi.nlm.nih.gov/pubmed/25550321","alternativeUrl":"https://europepmc.org/abstract/MED/25550321"}}]}],"olnNames":[{"value":"spr0334","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAK99138.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAK99138.1"}}]}]}],"length":464,"name":"Mid-cell-anchored protein Z","ncbi_taxon_id":171101,"organism":"Streptococcus pneumoniae (strain ATCC BAA-255 / R6)","regions":[{"start":1,"end":159,"reference_id":"32132631","reference_source":"pmid","reference_html":"Structural features of the interaction of MapZ with FtsZ and membranes in Streptococcus pneumoniae. <i> Hosek T, Bougault CM, Lavergne JP, Martinez D, Ayala I, Fenel D, Restelli M, Morlot C, Habenstein B, Grangeasse C, Simorre JP. </i> Sci Rep, 2020","date":"2025-04-24T11:05:28.062Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"28006"}],"region_id":"DP04379r001","statement":[{"text":"The 1H-15N correlation spectrum of this MapZcyto construct displays typical features of an unfolded protein, i.e. intense narrow peaks and very low chemical shift dispersion, especially in the proton dimension (Fig. 1b).","type":"Results"},{"text":"The cytoplasmic domain of MapZ therefore appears to be mostly an intrinsically disordered region (IDR) with moderate tendency to be structured for the amino acid region 22 to 86.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-23T17:22:45.429Z"}},{"start":17,"end":43,"reference_id":"32132631","reference_source":"pmid","reference_html":"Structural features of the interaction of MapZ with FtsZ and membranes in Streptococcus pneumoniae. <i> Hosek T, Bougault CM, Lavergne JP, Martinez D, Ayala I, Fenel D, Restelli M, Morlot C, Habenstein B, Grangeasse C, Simorre JP. </i> Sci Rep, 2020","date":"2025-04-24T11:14:55.909Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q8DNV9","operator":null,"partner_start":1,"partner_end":419}],"region_id":"DP04379r002","statement":[{"text":"The N-terminal residues 17 to 43 experienced an intensity decrease of up to 70% for the MapZcyto:FtsZa 1:4.7 ratio, whereas other residues of the cytoplasmic domain of MapZ remained largely unaffected. Similar results were obtained with the FtsZb construct in the presence of which the intensity of the same signals decreased stronger at higher MapZcyto:FtsZb protein ratios (Fig. S4a). These results suggest that the 17-to-43 N-terminal region of MapZcyto interacts with monomeric FtsZ, whereas the remainder of the cytosolic region stays completely flexible in the protein-protein complex.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-23T17:19:10.217Z"}},{"start":11,"end":110,"reference_id":"32132631","reference_source":"pmid","reference_html":"Structural features of the interaction of MapZ with FtsZ and membranes in Streptococcus pneumoniae. <i> Hosek T, Bougault CM, Lavergne JP, Martinez D, Ayala I, Fenel D, Restelli M, Morlot C, Habenstein B, Grangeasse C, Simorre JP. </i> Sci Rep, 2020","date":"2025-04-24T11:28:01.876Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP04379r004","statement":[{"text":"Altogether, monitoring of MapZcyto with liquid-state NMR and deuterated liposomes with 2H 1D ssNMR shows that the N-terminal portion of MapZcyto (up to residue 110) interacts with membrane lipids. On one hand, the unfolded and positively charged region of MapZcyto (residues 3 to 11) interacts with the negatively charged lipid heads. On the other hand, the two amphipathic helices (residues 45 to 68 and 79 to 95), which present hydrophobic spots surrounded by positively charged and hydrophilic residues, induce packing defects of the lipids by increasing the mobility of their acyl chains","type":"Results"},{"text":"This evidence was specifically created for the solid-state NMR experiments.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-26T17:06:41.293Z"}},{"start":314,"end":354,"reference_id":"27346279","reference_source":"pmid","reference_html":"Structure-function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZ. <i> Manuse S, Jean NL, Guinot M, Lavergne JP, Laguri C, Bougault CM, VanNieuwenhze MS, Grangeasse C, Simorre JP. </i> Nat Commun, 2016","date":"2025-04-24T11:50:52.841Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04379r005","statement":[{"text":"The two MapZextra1 and MapZextra2 subdomains are linked by a long polypeptide containing a serine-rich region (serine-rich linker, SRL) from residues K314 to S354. Whereas the majority of the amide protons of this SRL were not detected in the 2D-[1H,15N] correlation spectrum recorded at pH 7.5, intense resonances appear at pH 4.5 with chemical shifts that were characteristic of a disordered structure (8.1–8.5 p.p.m.; Supplementary Fig. 3B).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-23T17:22:05.057Z"}},{"start":314,"end":354,"reference_id":"27346279","reference_source":"pmid","reference_html":"Structure-function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZ. <i> Manuse S, Jean NL, Guinot M, Lavergne JP, Laguri C, Bougault CM, VanNieuwenhze MS, Grangeasse C, Simorre JP. </i> Nat Commun, 2016","date":"2025-04-24T11:53:07.178Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04379r006","statement":[{"text":"The two MapZextra1 and MapZextra2 subdomains are linked by a long polypeptide containing a serine-rich region (serine-rich linker, SRL) from residues K314 to S354. Whereas the majority of the amide protons of this SRL were not detected in the 2D-[1H,15N] correlation spectrum recorded at pH 7.5, intense resonances appear at pH 4.5 with chemical shifts that were characteristic of a disordered structure (8.1–8.5 p.p.m.; Supplementary Fig. 3B).","type":"Results"},{"text":"All these results point out a bi-modular organization of the extracellular domain of MapZ, with two independent subdomains connected by a highly dynamic SRL.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-23T17:18:56.554Z"}},{"start":314,"end":354,"reference_id":"27346279","reference_source":"pmid","reference_html":"Structure-function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZ. <i> Manuse S, Jean NL, Guinot M, Lavergne JP, Laguri C, Bougault CM, VanNieuwenhze MS, Grangeasse C, Simorre JP. </i> Nat Commun, 2016","date":"2025-04-24T11:54:48.784Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04379r007","statement":[{"text":"The independent mobility of the two domains conferred by the flexible SRL was confirmed by small-angle X-ray scattering (SAXS) data recorded on the full-length extracellular domain at two concentrations (Supplementary Fig. 5A). Indeed, the Kratky plot derived from the experimental I(s) scattering curves showed a behaviour for s>2 nm−1 in agreement with the presence of a large flexibility.","type":"Results"},{"text":"All these results point out a bi-modular organization of the extracellular domain of MapZ, with two independent subdomains connected by a highly dynamic SRL.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-23T17:18:38.348Z"}},{"start":1,"end":41,"reference_id":"25470041","reference_source":"pmid","reference_html":"MapZ marks the division sites and positions FtsZ rings in Streptococcus pneumoniae. <i> Fleurie A, Lesterlin C, Manuse S, Zhao C, Cluzel C, Lavergne JP, Franz-Wachtel M, Macek B, Combet C, Kuru E, VanNieuwenhze MS, Brun YV, Sherratt D, Grangeasse C. </i> Nature, 2014","date":"2025-04-24T12:01:46.514Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q8DNV9","operator":null,"partner_start":1,"partner_end":419}],"region_id":"DP04379r008","statement":[{"text":"Co-immuno-precipitation revealed in vivo interaction between FtsZ and MapZ, which is mediated by the cytoplasmic domain of MapZ (Fig. 4a). The cytoplasmic domain of MapZ (MapZcyto) strongly interacts with FtsZ (KD= 8.76 nM), more precisely via its N-terminal peptide predicted as an alpha-helix (MapZ(1-41) from Met-1 to Gly-41) (KD= 20.4 nM) (Extended Data Fig. 7a-d).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-23T17:21:33.726Z"}},{"start":1,"end":41,"reference_id":"25470041","reference_source":"pmid","reference_html":"MapZ marks the division sites and positions FtsZ rings in Streptococcus pneumoniae. <i> Fleurie A, Lesterlin C, Manuse S, Zhao C, Cluzel C, Lavergne JP, Franz-Wachtel M, Macek B, Combet C, Kuru E, VanNieuwenhze MS, Brun YV, Sherratt D, Grangeasse C. </i> Nature, 2014","date":"2025-04-24T12:03:39.542Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q8DNV9","operator":null,"partner_start":1,"partner_end":419}],"region_id":"DP04379r009","statement":[{"text":"In vivo deletion of MapZ N-terminal peptide (mapZΔ(1-41)) did not impaired MapZ septal localization (Extended Data Fig. 6e), but resulted in delocalization of FtsZ (Extended Data Fig. 6f-g), which subsequently leads to aberrant cell morphogenesis, asymmetric division or cell lysis (Extended Data Fig. 1a and Fig. 6h, Supplementary Video 8). This was also observed in mapZΔcyto strain (Extended Data Fig. 6i, Supplementary Video 9). Therefore, MapZ direct interaction with FtsZ is strictly required for FtsZ positioning.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-26T16:50:36.663Z"}},{"start":65,"end":69,"reference_id":"25470041","reference_source":"pmid","reference_html":"MapZ marks the division sites and positions FtsZ rings in Streptococcus pneumoniae. <i> Fleurie A, Lesterlin C, Manuse S, Zhao C, Cluzel C, Lavergne JP, Franz-Wachtel M, Macek B, Combet C, Kuru E, VanNieuwenhze MS, Brun YV, Sherratt D, Grangeasse C. </i> Nature, 2014","date":"2025-04-24T12:05:56.955Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007184","ec_ontology":"ECO","ec_name":"protein mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04379r010","statement":[{"text":"Mass spectrometry analysis of MapZ further showed that MapZ is phosphorylated on Thr-67 and Thr-78 (Extended Data Fig. 8a-b).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-26T16:50:10.942Z"}},{"start":76,"end":80,"reference_id":"25470041","reference_source":"pmid","reference_html":"MapZ marks the division sites and positions FtsZ rings in Streptococcus pneumoniae. <i> Fleurie A, Lesterlin C, Manuse S, Zhao C, Cluzel C, Lavergne JP, Franz-Wachtel M, Macek B, Combet C, Kuru E, VanNieuwenhze MS, Brun YV, Sherratt D, Grangeasse C. </i> Nature, 2014","date":"2025-04-24T12:06:25.536Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007184","ec_ontology":"ECO","ec_name":"protein mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04379r011","statement":[{"text":"Mass spectrometry analysis of MapZ further showed that MapZ is phosphorylated on Thr-67 and Thr-78 (Extended Data Fig. 8a-b).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-26T16:50:10.547Z"}}],"regions_counter":11,"released":"2025_06","sequence":"MSKKRRNRHKKEAQEPQFDFDEAKELTVGQAIRKNEEVEAGVLPEDSILDKYVKQHRDEIEADKFATRQYKKEEFVETQSLDDLIQEMREAVEKSEASSEEVPSSEDILLPLPLDDEEQGLDPLLLDDENPTEMTEEVEEEQNLSRLDQEDSEKKSKKGFILTVLALVSVIICVSAYYVYRQVARSTKEIETSQSTTANQSDVDDFNTLYDAFYTNSNKTALKNSQFDKLSQLKTLLDKLEGSREHTLAKSKYDSLATQIKAIQDVNAQFEKPAIVDGVLDTNAKAKSDAKFTDIKTGNTELDKVLDKAISLGKSQQTSTSSSSSSQTSSSSSSQASSNTTSEPKPSSSNETRSSRSEVNMGLSSAGVAVQRSASRVAYNQSAIDDSNNSAWDFADGVLEQILATSRSRGYITGDQYILERVNIVNGNGYYNLYKPDGTYLFTLNCKTGYFVGNGAGHADDLDY","taxonomy":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Streptococcaceae","Streptococcus"],"alphafold_very_low_content":0.2543103448275862,"disorder_content":0.43103448275862066,"disprot_consensus":{"full":[{"start":1,"end":159,"type":"D"},{"start":314,"end":354,"type":"D"}],"Structural state":[{"start":1,"end":159,"type":"D"},{"start":314,"end":354,"type":"D"}],"Molecular function":[{"start":1,"end":110,"type":"F"}],"Disorder function":[{"start":65,"end":69,"type":"F"},{"start":76,"end":80,"type":"F"},{"start":314,"end":354,"type":"F"}]}},{"disprot_id":"DP04380","acc":"P15917","creator":"viglesias","date":"2025-04-24T12:25:48.263Z","features":{"pfam":[{"id":"PF07737","name":"Anthrax toxin lethal factor, N- and C-terminal domain","start":63,"end":279},{"id":"PF07737","name":"Anthrax toxin lethal factor, N- and C-terminal domain","start":591,"end":801},{"id":"PF09156","name":"Anthrax toxin lethal factor, middle domain","start":297,"end":583}],"gene3D":[]},"genes":[{"name":{"value":"lef","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"2509294","url":"http://www.ncbi.nlm.nih.gov/pubmed/2509294","alternativeUrl":"https://europepmc.org/abstract/MED/2509294"}}]},"olnNames":[{"value":"pXO1-107"},{"value":"BXA0172"},{"value":"GBAA_pXO1_0172"}]}],"length":809,"name":"Lethal factor","ncbi_taxon_id":1392,"organism":"Bacillus anthracis","regions":[{"start":34,"end":61,"reference_id":"11700563","reference_source":"pmid","reference_html":"Crystal structure of the anthrax lethal factor. <i> Pannifer AD, Wong TY, Schwarzenbacher R, Renatus M, Petosa C, Bienkowska J, Lacy DB, Collier RJ, Park S, Leppla SH, Hanna P, Liddington RC. </i> Nature, 2001","date":"2025-06-05T08:09:12.447Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"1J7N"}],"region_id":"DP04380r001","statement":[{"text":"The N-terminal 26 residues are invisible in our electron density maps, and we presume that they are disordered.","type":"Figure"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":"zinc(2+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T13:24:22.634Z"}},{"start":379,"end":400,"reference_id":"32810181","reference_source":"pmid","reference_html":"Cryo-EM structure of the fully-loaded asymmetric anthrax lethal toxin in its heptameric pre-pore state. <i> Antoni C, Quentin D, Lang AE, Aktories K, Gatsogiannis C, Raunser S. </i> PLoS Pathog, 2020","date":"2025-06-03T17:39:35.675Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"6ZXL"},{"db":"PDB","id":"6ZXK"},{"db":"PDB","id":"6ZXJ"}],"region_id":"DP04380r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P13423"}],"statement":[{"text":"Noteworthy, the 2β2-2β3 loop region (residues 300–323) which is implicated in pore formation was not resolved in our map. This indicates a high flexibility of this loop, which is in line with previous MD simulations [38].","type":"Results"}]}],"regions_counter":2,"released":"2025_06","sequence":"MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSEEGRGLLKKLQIPIEPKKDDIIHSLSQEEKELLKRIQIDSSDFLSTEEKEFLKKLQIDIRDSLSEEEKELLNRIQVDSSNPLSEKEKEFLKKLKLDIQPYDINQRLQDTGGLIDSPSINLDVRKQYKRDIQNIDALLHQSIGSTLYNKIYLYENMNINNLTATLGADLVDSTDNTKINRGIFNEFKKNFKYSISSNYMIVDINERPALDNERLKWRIQLSPDTRAGYLENGKLILQRNIGLEIKDVQIIKQSEKEYIRIDAKVVPKSKIDTKIQEAQLNINQEWNKALGLPKYTKLITFNVHNRYASNIVESAYLILNEWKNNIQSDLIKKVTNYLVDGNGRFVFTDITLPNIAEQYTHQDEIYEQVHSKGLYVPESRSILLHGPSKGVELRNDSEGFIHEFGHAVDDYAGYLLDKNQSDLVTNSKKFIDIFKEEGSNLTSYGRTNEAEFFAEAFRLMHSTDHAERLKVQKNAPKTFQFINDQIKFIINS","taxonomy":["Bacteria","Bacillati","Bacillota","Bacilli","Bacillales","Bacillaceae","Bacillus","Bacillus cereus group"],"alphafold_very_low_content":0.069221260815822,"dataset":["Unicellular toxins and antitoxins","Bacterial virulence-related proteins"],"disorder_content":0.06180469715698393,"disprot_consensus":{"full":[{"start":34,"end":61,"type":"D"},{"start":379,"end":400,"type":"D"}],"Structural state":[{"start":34,"end":61,"type":"D"},{"start":379,"end":400,"type":"D"}]}},{"disprot_id":"DP04381","acc":"P0CL43","creator":"rpancsa","date":"2025-04-24T13:51:46.694Z","features":{"pfam":[{"id":"PF04741","name":"InvH outer membrane lipoprotein","start":61,"end":140}],"gene3D":[]},"genes":[{"name":{"value":"invH","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"9068645","url":"http://www.ncbi.nlm.nih.gov/pubmed/9068645","alternativeUrl":"https://europepmc.org/abstract/MED/9068645"}}]},"synonyms":[{"value":"sctG","evidences":[{"code":"ECO:0000305"}]}],"olnNames":[{"value":"STM2900"}]}],"length":147,"name":"SPI-1 type 3 secretion system pilotin","ncbi_taxon_id":99287,"organism":"Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)","regions":[{"start":27,"end":69,"reference_id":"32877645","reference_source":"pmid","reference_html":"Characterization of the Pilotin-Secretin Complex from the Salmonella enterica Type III Secretion System Using Hybrid Structural Methods. <i> Majewski DD, Okon M, Heinkel F, Robb CS, Vuckovic M, McIntosh LP, Strynadka NCJ. </i> Structure, 2021","date":"2025-04-24T13:57:10.787Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04381r001","statement":[{"text":"The 15N HSQC spectrum from InvH27-147 also showed increased dispersion upon binding InvG520-562 (Figures S4A and S4B). Furthermore, additional amides not present in the InvH70-147 complex have 1NH chemical shifts in the narrow range of 8.0–8.5 ppm. Consistent with sequence-based predictions (Cheng et al., 2005; Jones and Cozzetto, 2015; Kelley et al., 2015), these chemical shifts indicate that the InvH linker is conformationally disordered (Konrat, 2014).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-03T17:57:46.858Z"}},{"start":27,"end":69,"reference_id":"32877645","reference_source":"pmid","reference_html":"Characterization of the Pilotin-Secretin Complex from the Salmonella enterica Type III Secretion System Using Hybrid Structural Methods. <i> Majewski DD, Okon M, Heinkel F, Robb CS, Vuckovic M, McIntosh LP, Strynadka NCJ. </i> Structure, 2021","date":"2025-04-24T13:59:41.641Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04381r002","statement":[{"text":"The 15N HSQC spectrum from InvH27-147 also showed increased dispersion upon binding InvG520-562 (Figures S4A and S4B). Furthermore, additional amides not present in the InvH70-147 complex have 1NH chemical shifts in the narrow range of 8.0–8.5 ppm. Consistent with sequence-based predictions (Cheng et al., 2005; Jones and Cozzetto, 2015; Kelley et al., 2015), these chemical shifts indicate that the InvH linker is conformationally disordered (Konrat, 2014).","type":"Results"},{"text":"Secondary structure analysis by Phyre2 for InvH predicted an α-helical C-terminal domain, joined by a long (∼50 residue) disordered linker region to the signature (L-A/S-G/A-C) N-terminal lipobox (Kelley et al., 2015).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-03T17:57:58.378Z"}},{"start":27,"end":69,"reference_id":"32877645","reference_source":"pmid","reference_html":"Characterization of the Pilotin-Secretin Complex from the Salmonella enterica Type III Secretion System Using Hybrid Structural Methods. <i> Majewski DD, Okon M, Heinkel F, Robb CS, Vuckovic M, McIntosh LP, Strynadka NCJ. </i> Structure, 2021","date":"2025-04-24T14:05:09.874Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04381r003","statement":[{"text":"In the case of the InvH27-147 construct, which includes the predicted disordered linker region, fitting of the SAXS data produced an envelope with additional scattering density extending from both poles of the InvH70-147 structure (Figure 2B). These poles correspond to the locations of the N termini of the InvH70-147 crystal structure where the linker residues would be joined. Collectively, the SEC-MALS and SAXS data confirm the formation of an InvH homodimer in solution, with the SAXS data additionally supporting the position of the InvH27-147 N-terminal linker region.","type":"Results"}],"cross_refs":[{"db":"SASBDB","id":"SASDJR4"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-03T17:57:55.335Z"}},{"start":70,"end":82,"reference_id":"32877645","reference_source":"pmid","reference_html":"Characterization of the Pilotin-Secretin Complex from the Salmonella enterica Type III Secretion System Using Hybrid Structural Methods. <i> Majewski DD, Okon M, Heinkel F, Robb CS, Vuckovic M, McIntosh LP, Strynadka NCJ. </i> Structure, 2021","date":"2025-06-03T17:55:57.095Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"BMRB","id":"30765"},{"db":"PDB","id":"6XFL"}],"region_id":"DP04381r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P35672"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":"sulfate"}],"statement":[{"text":"However, whereas the crystallized homodimer has two helices, α1a and α1b (residues 73–88 and 90–101, respectively), the heterodimer in solution has one extended helix spanning residues 83–101, and residues 70–82 are disordered.","type":"Results"}]}],"regions_counter":4,"released":"2025_06","sequence":"MKKFYSCLPVFLLIGCAQVPLPSSVSKPVQQPGAQKEQLANANSIDECQSLPYVPSDLAKNKSLSNHNADNSASKNSAISSSIFCEKYKQTKEQALTFFQEHPQYMRSKEDEEQLMTEFKKVLLEPGSKNLSIYQTLLAAHERLQAL","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"],"alphafold_very_low_content":0.36054421768707484,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.38095238095238093,"disprot_consensus":{"full":[{"start":27,"end":82,"type":"D"}],"Structural state":[{"start":27,"end":82,"type":"D"}],"Disorder function":[{"start":27,"end":69,"type":"F"}]}},{"disprot_id":"DP04382","acc":"P21860","creator":"rpancsa","date":"2025-04-24T14:58:08.926Z","features":{"pfam":[{"id":"PF00757","name":"Furin-like cysteine rich region","start":182,"end":332},{"id":"PF01030","name":"Receptor L domain","start":56,"end":166},{"id":"PF01030","name":"Receptor L domain","start":353,"end":472},{"id":"PF07714","name":"Protein tyrosine and serine/threonine kinase","start":711,"end":964},{"id":"PF14843","name":"Growth factor receptor domain IV","start":499,"end":629}],"gene3D":[]},"genes":[{"name":{"value":"ERBB3"},"synonyms":[{"value":"HER3"}]}],"length":1342,"name":"Receptor tyrosine-protein kinase erbB-3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":981,"end":1342,"reference_id":"27872189","reference_source":"pmid","reference_html":"Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases. <i> Keppel TR, Sarpong K, Murray EM, Monsey J, Zhu J, Bose R. </i> J Biol Chem, 2017","date":"2025-04-24T15:43:12.591Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04382r001","statement":[{"text":"We show that hydrogen/deuterium exchange occurs more rapidly in peptides from the CTT than those from the kinase domain (Fig. 2). Many peptides from the kinase domains (shown in blue) do not reach a maximum exchange plateau even within 2 h of exchange. However, peptides from the CTTs (shown in red) exchanged much more rapidly, often reaching a plateau before 5 s of exchange. This behavior was observed for all three ErbB ICH constructs analyzed. This indicates that the CTT region has faster hydrogen/deuterium exchange kinetics than the kinase domain with amide hydrogen protection from exchange being much weaker in the tail.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-04T17:53:25.844Z"}},{"start":981,"end":1342,"reference_id":"27872189","reference_source":"pmid","reference_html":"Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases. <i> Keppel TR, Sarpong K, Murray EM, Monsey J, Zhu J, Bose R. </i> J Biol Chem, 2017","date":"2025-04-24T15:43:43.328Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04382r002","statement":[{"text":"The CD spectrum for HER3 CTT shows similar features as the EGFR CTT with a minimum between 195 and 200 nm and slightly negative ellipticity at 222 nm (Fig. 5B). The HER3 CTT has mostly unordered content (60%) but slightly higher β-sheet content than EGFR CTT: regular β-strand (βR) = 15% and distorted β-strand (βD) = 7% for HER3 CTT as compared with βR = 6% and βD = 3% for EGFR CTT (Fig. 5C).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-04T17:48:59.827Z"}},{"start":981,"end":1342,"reference_id":"27872189","reference_source":"pmid","reference_html":"Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases. <i> Keppel TR, Sarpong K, Murray EM, Monsey J, Zhu J, Bose R. </i> J Biol Chem, 2017","date":"2025-04-24T15:49:12.867Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04382r003","statement":[{"text":"Another property of intrinsically disordered regions is a higher than expected apparent molecular mass during gel filtration separations (42). SEC can be used to separate proteins based on their hydrodynamic size, which is increased in IDRs depending on the degree of conformational extension.","type":"Results"},{"text":"The molecular masses, determined by MALS, of the HER CTT and EGFR kinase domain were 42 and 38 kDa, respectively. HER3 CTT eluted at about 14 ml of buffer, which is earlier than the EGFR kinase domain, which eluted between 16 and 17 ml of buffer. As with EGFR CTT, no multimeric peaks were observed in the HER3 CTT chromatogram.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-04T17:48:03.118Z"}},{"start":981,"end":1342,"reference_id":"27872189","reference_source":"pmid","reference_html":"Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases. <i> Keppel TR, Sarpong K, Murray EM, Monsey J, Zhu J, Bose R. </i> J Biol Chem, 2017","date":"2025-04-24T15:50:27.331Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007064","ec_ontology":"ECO","ec_name":"dynamic light scattering assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04382r004","statement":[{"text":"Similarly, HER3 CTT has a very large hydrodynamic radius (Fig. 6D). The hydrodynamic radius (RH) of HER3 CTT is 6.4 nm, although it has higher polydispersity than EGFR CTT.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-04T17:48:57.109Z"}},{"start":981,"end":1342,"reference_id":"27872189","reference_source":"pmid","reference_html":"Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases. <i> Keppel TR, Sarpong K, Murray EM, Monsey J, Zhu J, Bose R. </i> J Biol Chem, 2017","date":"2025-04-24T15:51:57.724Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006275","ec_ontology":"ECO","ec_name":"analytical ultracentrifugation evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04382r005","statement":[{"text":"For a globular protein, the expected f/fmin would fall between 1.15 and 1.3 (47–49). We determined the f/fmin value for EGFR CTT to be much greater, at 1.77, which is consistent with this being an IDR. Similarly, HER3 CTT has a f/fmin value of 1.52, which is also greater than the expected frictional ratio for globular proteins (Fig. 6F).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-04T17:48:46.797Z"}},{"start":981,"end":1342,"reference_id":"27872189","reference_source":"pmid","reference_html":"Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases. <i> Keppel TR, Sarpong K, Murray EM, Monsey J, Zhu J, Bose R. </i> J Biol Chem, 2017","date":"2025-04-24T15:54:26.605Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04382r006","statement":[{"text":"Without urea present, the HER3 CTT produces a slightly parabolic Kratky profile, with a defined local maximum observed, at lower momentum transfer values. Moving toward greater momentum transfer values then gives a more hyperbolic increase in I(s)·s2. For HER3 CTT with 4 m urea, the Kratky profile has a hyperbolic shape indicative of disorder, similar to the profile observed for the EGFR CTT (Fig. 7C). The difference in Kratky plots between HER3 CTT with or without urea, together with increased Rg, indicates that HER3 CTT possesses characteristics of IDRs but not of random coil structures when in solution.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-04T17:48:48.944Z"}},{"start":1287,"end":1291,"reference_id":"27872189","reference_source":"pmid","reference_html":"Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases. <i> Keppel TR, Sarpong K, Murray EM, Monsey J, Zhu J, Bose R. </i> J Biol Chem, 2017","date":"2025-05-08T14:25:09.027Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04382r007","statement":[{"text":"Furthermore, we used anti-HER3 Tyr(P)-1289 and general PY20 antibodies to verify that the HER3 CTT was phosphorylated by both the EGFR kinase domain and HER2 kinase domain via Western blotting.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-04T17:53:26.122Z"}},{"start":981,"end":1342,"reference_id":"27872189","reference_source":"pmid","reference_html":"Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases. <i> Keppel TR, Sarpong K, Murray EM, Monsey J, Zhu J, Bose R. </i> J Biol Chem, 2017","date":"2026-06-04T17:54:43.685Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04382r008","statement":[{"text":"Results from circular dichroism spectroscopy, size exclusion chromatography with multiangle light scattering, dynamic light scattering, analytical ultracentrifugation, and small angle X-ray scattering each provide evidence that the EGFR and HER3 C-terminal tails are intrinsically disordered with extended, non-globular structure in solution.","type":"Abstract"}]}],"regions_counter":8,"released":"2026_06","sequence":"MRANDALQVLGLLFSLARGSEVGNSQAVCPGTLNGLSVTGDAENQYQTLYKLYERCEVVMGNLEIVLTGHNADLSFLQWIREVTGYVLVAMNEFSTLPLPNLRVVRGTQVYDGKFAIFVMLNYNTNSSHALRQLRLTQLTEILSGGVYIEKNDKLCHMDTIDWRDIVRDRDAEIVVKDNGRSCPPCHEVCKGRCWGPGSEDCQTLTKTICAPQCNGHCFGPNPNQCCHDECAGGCSGPQDTDCFACRHFNDSGACVPRCPQPLVYNKLTFQLEPNPHTKYQYGGVCVASCPHNFVVDQTSCVRACPPDKMEVDKNGLKMCEPCGGLCPKACEGTGSGSRFQTVDSSNIDGFVNCTKILGNLDFLITGLNGDPWHKIPALDPEKLNVFRTVREITGYLNIQSWPPHMHNFSVFSNLTTIGGRSLYNRGFSLLIMKNLNVTSLGFRSLKEISAGRIYISANRQLCYHHSLNWTKVLRGPTEERLDIKHNRPRRDCVAEGKVCDPLCSSGGCWGPGPGQCLSCRNYSRGGVCVTHCNFLNGEPREFAHEAECFSCHPECQPMEGTATCNGSGSDTCAQCAHFRDGPHCVSSCPHGVLGAKGPIYKYPDVQNECRPCHENCTQGCKGPELQDCLGQTLVLIGKTHLTMALTVIAGLVVIFMMLGGTFLYWRGRRIQNKRAMRRYLERGESIEPLDPSEKANKVLARIFKETELRKLKVLGSGVFGTVHKGVWIPEGESIKIPVCIKVIEDKSGRQSFQAVTDHMLAIGSLDHAHIVRLLGLCPGSSLQLVTQYLPLGSLLDHVRQHRGALGPQLLLNWGVQIAKGMYYLEEHGMVHRNLAARNVLLKSPSQVQVADFGVADLLPPDDKQLLYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWELMTFGAEPYAGLRLAEVPDLLEKGERLAQPQICTIDVYMVMVKCWMIDENIRPTFKELANEFTRMARDPPRYLVIKRESGPGIAPGPEPHGLTNKKLEEVELEPELDLDLDLEAEEDNLATTTLGSALSLPVGTLNRPRGSQSLLSPSSGYMPMNQGNLGESCQESAVSGSSERCPRPVSLHPMPRGCLASESSEGHVTGSEAELQEKVSMCRSRSRSRSPRPRGDSAYHSQRHSLLTPVTPLSPPGLEEEDVNGYVMPDTHLKGTPSSREGTLSSVGLSSVLGTEEEDEDEEYEYMNRRRRHSPPHPPRPSSLEELGYEYMDVGSDLSASLGSTQSCPLHPVPIMPTAGTTPDEDYEYMNRQRDGGGPGGDYAAMGACPASEQGYEEMRAFQGPGHQAPHVHYARLKTLRSLEATDSAFDNPDYWHSRLFPKANAQRT","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.29806259314456035,"dataset":["Cancer-related proteins"],"disorder_content":0.2697466467958271,"disprot_consensus":{"full":[{"start":981,"end":1342,"type":"D"}],"Structural state":[{"start":981,"end":1342,"type":"D"}],"Disorder function":[{"start":981,"end":1342,"type":"F"}]}},{"disprot_id":"DP04383","acc":"D0ZRB2","creator":"xcastro","date":"2025-04-28T12:36:31.641Z","features":{"pfam":[{"id":"PF12468","name":"Type III secretion system leucine rich repeat protein","start":107,"end":170},{"id":"PF14496","name":"C-terminal novel E3 ligase, LRR-interacting","start":475,"end":680}],"gene3D":[]},"genes":[{"name":{"value":"slrP"},"olnNames":[{"value":"STM14_928"}]}],"length":765,"name":"E3 ubiquitin-protein ligase SlrP","ncbi_taxon_id":588858,"organism":"Salmonella typhimurium (strain 14028s / SGSC 2262)","regions":[{"start":709,"end":728,"reference_id":"25184225","reference_source":"pmid","reference_html":"The structure of the Slrp-Trx1 complex sheds light on the autoinhibition mechanism of the type III secretion system effectors of the NEL family. <i> Zouhir S, Bernal-Bayard J, Cordero-Alba M, Cardenal-Muñoz E, Guimaraes B, Lazar N, Ramos-Morales F, Nessler S. </i> Biochem J, 2014","date":"2025-04-28T12:51:38.751Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":18,"statements":[{"type":"Methods","text":"The co-crystals were manually reproduced and optimized at 18°C using the hanging drop method in a crystallization solution containing 0.1 M MgCl2, 0.2 M NaCl, 0.1 M Hepes, pH 7.8, and 15% PEG 4000, with a SlrP/Trx1 molar ratio of 1:2 by mixing 216 μM SlrP with 430 μM Trx1."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":8.8,"statements":[{"type":"Methods","text":"The co-crystals were manually reproduced and optimized at 18°C using the hanging drop method in a crystallization solution containing 0.1 M MgCl2, 0.2 M NaCl, 0.1 M Hepes, pH 7.8, and 15% PEG 4000, with a SlrP/Trx1 molar ratio of 1:2 by mixing 216 μM SlrP with 430 μM Trx1."}]}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The human trx1 gene and the slrP gene fragments from Salmonella enterica serovar Typhimurium corresponding to residues 1–140 and 140–765 were cloned into pQE30 plasmids and expressed with an N-terminal His6 tag as recombinant proteins in the E. coli M15/pREP4 strain."}]}],"cross_refs":[{"db":"PDB","id":"4PUF"}],"region_id":"DP04383r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":0.43,"db":"UniProt","id":"P10599","statements":[{"type":"Methods","text":"The co-crystals were manually reproduced and optimized at 18°C using the hanging drop method in a crystallization solution containing 0.1 M MgCl2, 0.2 M NaCl, 0.1 M Hepes, pH 7.8, and 15% PEG 4000, with a SlrP/Trx1 molar ratio of 1:2 by mixing 216 μM SlrP with 430 μM Trx1."}]}],"sequence_construct":"MRGSHHHHHHGSKDAVNYELIWSEWVKEAPAKEAANREEAVQRMRDCLKNNKTELRLKILGLTTIPAYIPEQITTLILDNNELKSLPENLQGNIKTLYANSNQLTSIPATLPDTIQEMELSINRITELPERLPSALQSLDLFHNKISCLPENLPEELRYLSVYDNSIRTLPAHLPSEITHLNVQSNSLTALPETLPPGLKTLEAGENALTSLPASLPPELQVLDVSKNQITVLPETLPPTITTLDVSRNALTNLPENLPAALQIMQASRNNLVRLPESLPHFRGEGPQPTRIIVEYNPFSERTIQNMQRLMSSVDYQGPRVLFAMGDFSIVRVTRPLHQAVQGWLTSLEEEDVNQWRAFEAEANAAAFSGFLDYLGDTQNTRHPDFKEQVSAWLMRLAEDSALRETVFIIAMNATISCEDRVTLAYHQMQEATLVHDAERGAFDSHLAELIMAGREIFRLEQIESLAREKVKRLFFIDEVEVFLGFQNQLRESLSLTTMTRDMRFYNVSGITESDLDEAEIRIKMAENRDFHKWFALWGPWHKVLERIAPEEWREMMAKRDECIETDEYQSRVNAELEDLRIADDSDAERTTEVQMDAERAIGIKIMEEINQTLFTEIMENILLKKEVSSLMSAYWR","statement":[{"text":"In both copies of the NEL domain there was no visible electron density for loop αM–αN (residues 709–728) of the C-terminal helix bundle. In contrast, the loop linking the LRR and NEL domains that was disordered in the published apo structures of IpaH3 [21] and SspH2 [22] is clearly defined in the Trx1-bound SlrP structure.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T18:02:39.522Z"}}],"regions_counter":1,"released":"2025_06","sequence":"MFNITNIQSTARHQSISNEASTEVPLKEEIWNKISAFFSSEHQVEAQNCIAYLCHPPETASPEEIKSKFECLRMLAFPAYADNIQYSRGGADQYCILSENSQEILSIVFNTEGYTVEGGGKSVTYTRVTESEQASSASGSKDAVNYELIWSEWVKEAPAKEAANREEAVQRMRDCLKNNKTELRLKILGLTTIPAYIPEQITTLILDNNELKSLPENLQGNIKTLYANSNQLTSIPATLPDTIQEMELSINRITELPERLPSALQSLDLFHNKISCLPENLPEELRYLSVYDNSIRTLPAHLPSEITHLNVQSNSLTALPETLPPGLKTLEAGENALTSLPASLPPELQVLDVSKNQITVLPETLPPTITTLDVSRNALTNLPENLPAALQIMQASRNNLVRLPESLPHFRGEGPQPTRIIVEYNPFSERTIQNMQRLMSSVDYQGPRVLFAMGDFSIVRVTRPLHQAVQGWLTSLEEEDVNQWRAFEAEANAAAFSGFLDYLGDTQNTRHPDFKEQVSAWLMRLAEDSALRETVFIIAMNATISCEDRVTLAYHQMQEATLVHDAERGAFDSHLAELIMAGREIFRLEQIESLAREKVKRLFFIDEVEVFLGFQNQLRESLSLTTMTRDMRFYNVSGITESDLDEAEIRIKMAENRDFHKWFALWGPWHKVLERIAPEEWREMMAKRDECIETDEYQSRVNAELEDLRIADDSDAERTTEVQMDAERAIGIKIMEEINQTLFTEIMENILLKKEVSSLMSAYWR","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Salmonella"],"alphafold_very_low_content":0.06274509803921569,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.026143790849673203,"disprot_consensus":{"full":[{"start":709,"end":728,"type":"D"}],"Structural state":[{"start":709,"end":728,"type":"D"}]}},{"disprot_id":"DP04384","acc":"Q7BCK4","creator":"xcastro","date":"2025-04-28T13:14:53.866Z","features":{"pfam":[{"id":"PF03797","name":"Autotransporter beta-domain","start":821,"end":1080},{"id":"PF12951","name":"Passenger-associated-transport-repeat","start":527,"end":554},{"id":"PF18883","name":"Autochaperone Domain Type 1","start":619,"end":720},{"id":"PF22364","name":"VirG insertion domain (VID)","start":422,"end":484}],"gene3D":[]},"genes":[{"name":{"value":"icsA","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11115111","url":"http://www.ncbi.nlm.nih.gov/pubmed/11115111","alternativeUrl":"https://europepmc.org/abstract/MED/11115111"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"12384590","url":"http://www.ncbi.nlm.nih.gov/pubmed/12384590","alternativeUrl":"https://europepmc.org/abstract/MED/12384590"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"14573649","url":"http://www.ncbi.nlm.nih.gov/pubmed/14573649","alternativeUrl":"https://europepmc.org/abstract/MED/14573649"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"2542950","url":"http://www.ncbi.nlm.nih.gov/pubmed/2542950","alternativeUrl":"https://europepmc.org/abstract/MED/2542950"}}]},"synonyms":[{"value":"virG","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"11292750","url":"http://www.ncbi.nlm.nih.gov/pubmed/11292750","alternativeUrl":"https://europepmc.org/abstract/MED/11292750"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"2644195","url":"http://www.ncbi.nlm.nih.gov/pubmed/2644195","alternativeUrl":"https://europepmc.org/abstract/MED/2644195"}}]}],"olnNames":[{"value":"CP0182"}]}],"length":1102,"name":"Outer membrane autotransporter IcsA","ncbi_taxon_id":623,"organism":"Shigella flexneri","regions":[{"start":741,"end":758,"reference_id":"21335457","reference_source":"pmid","reference_html":"Crystal structure of the autochaperone region from the Shigella flexneri autotransporter IcsA. <i> Kühnel K, Diezmann D. </i> J Bacteriol, 2011","date":"2025-06-18T08:21:12.700Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Abstract","text":"The construct used in this study comprises residues 591 to 758 and is abbreviated IcsA-AC. IcsA-AC was expressed with an N-terminal hexahistidine tag in Escherichia coli and was purified with a three-step procedure (see the supplemental material for a detailed description)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val725Ala","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"3ML3"}],"region_id":"DP04384r001","sequence_construct":"MGSSHHHHHHSSGLVPRGSHMSGTVLINNINAPFLPDPVIVTGNMTLEKNGHVILNNSSSNVGQTYVQKGNWHGKGGILSLGAVLGNDNSKTDRLEIAGHASGITYVAVTNEGGSGDKTLEGVQIISTDSSDKNAFIQKGRIVAGSYDYRLKQGTASGLNTNKWYLTSQMDNQESKQMSNQESTQMSSR","statement":[{"text":"The final model contains residues 591 to 740, in addition to six residues from the linker region of the N-terminal His tag (Fig. 1C). The last 18 residues of IcsA-AC are disordered.","type":"Abstract"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:34:45.400Z"}},{"start":741,"end":758,"reference_id":"28268178","reference_source":"pmid","reference_html":"Structural insights into the architecture of the Shigella flexneri virulence factor IcsA/VirG and motifs involved in polar distribution and secretion. <i> Leupold S, Büsing P, Mas PJ, Hart DJ, Scrima A. </i> J Struct Biol, 2017","date":"2025-06-18T08:18:35.733Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"5KE1"}],"region_id":"DP04384r002","statement":[{"text":"Furthermore, the chain can only be traced to residue 740, indicating that the last 18 amino acids are flexible in a manner consistent with it forming a linker connecting the extracellular α-domain to the β-barrel membrane anchor.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"49786","entry_name":"nickel(2+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:34:30.144Z"}},{"start":741,"end":758,"reference_id":"28268178","reference_source":"pmid","reference_html":"Structural insights into the architecture of the Shigella flexneri virulence factor IcsA/VirG and motifs involved in polar distribution and secretion. <i> Leupold S, Büsing P, Mas PJ, Hart DJ, Scrima A. </i> J Struct Biol, 2017","date":"2025-06-18T08:18:50.018Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"5KE1"}],"region_id":"DP04384r003","statement":[{"text":"Furthermore, the chain can only be traced to residue 740, indicating that the last 18 amino acids are flexible in a manner consistent with it forming a linker connecting the extracellular α-domain to the β-barrel membrane anchor.","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"49786","entry_name":"nickel(2+)"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:34:35.342Z"}}],"regions_counter":3,"released":"2025_06","sequence":"MNQIHKFFCNMTQCSQGGAGELPTVKEKTCKLSFSPFVVGASLLLGGPIAFATPLSGTQELHFSEDNYEKLLTPVDGLSPLGAGEDGMDAWYITSSNPSHASRTKLRINSDIMISAGHGGAGDNNDGNSCGGNGGDSITGSDLSIINQGMILGGSGGSGADHNGDGGEAVTGDNLFIINGEIISGGHGGDSYSDSDGGNGGDAVTGVNLPIINKGTISGGNGGNNYGEGDGGNGGDAITGSSLSVINKGTFAGGNGGAAYGYGYDGYGGNAITGDNLSVINNGAILGGNGGHWGDAINGSNMTIANSGYIISGKEDDGTQNVAGNAIHITGGNNSLILHEGSVITGDVQVNNSSILKIINNDYTGTTPTIEGDLCAGDCTTVSLSGNKFTVSGDVSFGENSSLNLAGISSLEASGNMSFGNNVKVEAIINNWAQKDYKLLSADKGITGFSVSNISIINPLLTTGAIDYTKSYISDQNKLIYGLSWNDTDGDSHGEFNLKENAELTVSTILADNLSHHNINSWDGKSLTKSGEGTLILAEKNTYSGFTNINAGILKMGTVEAMTRTAGVIVNKGATLNFSGMNQTVNTLLNSGTVLINNINAPFLPDPVIVTGNMTLEKNGHVILNNSSSNVGQTYVQKGNWHGKGGILSLGAVLGNDNSKTDRLEIAGHASGITYVAVTNEGGSGDKTLEGVQIISTDSSDKNAFIQKGRIVAGSYDYRLKQGTVSGLNTNKWYLTSQMDNQESKQMSNQESTQMSSRRASSQLVSSLNLGEGSIHTWRPEAGSYIANLIAMNTMFSPSLYDRHGSTIVDPTTGQLSETTMWIRTVGGHNEHNLADRQLKTTANRMVYQIGGDILKTNFTDHDGLHVGIMGAYGYQDSKTHNKYTSYSSRGTVSGYTAGLYSSWFQDEKERTGLYMDAWLQYSWFNNTVKGDGLTGEKYSSKGITGALEAGYIYPTIRWTAHNNIDNALYLNPQVQITRHGVKANDYIEHNGTMVTSSGGNNIQAKLGLRTSLISQSCIDKETLRKFEPFLEVNWKWSSKQYGVIMNGMSNHQIGNRNVIELKTGVGGRLADNLSIWGNVSQQLGNNSYRDTQGILGVKYTF","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Shigella"],"alphafold_very_low_content":0.08439201451905626,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.016333938294010888,"disprot_consensus":{"full":[{"start":741,"end":758,"type":"D"}],"Structural state":[{"start":741,"end":758,"type":"D"}],"Disorder function":[{"start":741,"end":758,"type":"F"}]}},{"disprot_id":"DP04385","acc":"Q9ZKJ5","creator":"xcastro","date":"2025-04-28T13:55:48.078Z","features":{"pfam":[{"id":"PF07804","name":"HipA-like C-terminal domain","start":24,"end":185}],"gene3D":[]},"genes":[{"name":{"value":"ctkA"},"olnNames":[{"value":"jhp_0940"}]}],"length":325,"name":"Serine/threonine-protein kinase CtkA","ncbi_taxon_id":85963,"organism":"Helicobacter pylori (strain J99 / ATCC 700824)","regions":[{"start":41,"end":50,"reference_id":"21098302","reference_source":"pmid","reference_html":"Helicobacter pylori proinflammatory protein up-regulates NF-kappaB as a cell-translocating Ser/Thr kinase. <i> Kim DJ, Park KS, Kim JH, Yang SH, Yoon JY, Han BG, Kim HS, Lee SJ, Jang JY, Kim KH, Kim MJ, Song JS, Kim HJ, Park CM, Lee SK, Lee BI, Suh SW. </i> Proc Natl Acad Sci U S A, 2010","date":"2025-04-28T14:00:36.878Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"3AKJ"}],"region_id":"DP04385r001","statement":[{"text":"Two flexible loop regions (Lys14−Gly22 and Lys41−Tyr50 in chain A; Lys14−Lys24 and Pro40−Ser49 in chain B), as well as the C-terminal region containing the eight-residue affinity tag (LEHHHHHH) (13 residues in chain A; 12 residues in chain B) have no electron density and are missing from the model.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-10T14:53:59.988Z"}},{"start":14,"end":23,"reference_id":"21098302","reference_source":"pmid","reference_html":"Helicobacter pylori proinflammatory protein up-regulates NF-kappaB as a cell-translocating Ser/Thr kinase. <i> Kim DJ, Park KS, Kim JH, Yang SH, Yoon JY, Han BG, Kim HS, Lee SJ, Jang JY, Kim KH, Kim MJ, Song JS, Kim HJ, Park CM, Lee SK, Lee BI, Suh SW. </i> Proc Natl Acad Sci U S A, 2010","date":"2025-06-18T08:23:06.632Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"3AKJ"}],"region_id":"DP04385r002","statement":[{"text":"Two flexible loop regions (Lys14−Gly22 and Lys41−Tyr50 in chain A; Lys14−Lys24 and Pro40−Ser49 in chain B), as well as the C-terminal region containing the eight-residue affinity tag (LEHHHHHH) (13 residues in chain A; 12 residues in chain B) have no electron density and are missing from the model.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:35:29.293Z"}},{"start":14,"end":23,"reference_id":"21098302","reference_source":"pmid","reference_html":"Helicobacter pylori proinflammatory protein up-regulates NF-kappaB as a cell-translocating Ser/Thr kinase. <i> Kim DJ, Park KS, Kim JH, Yang SH, Yoon JY, Han BG, Kim HS, Lee SJ, Jang JY, Kim KH, Kim MJ, Song JS, Kim HJ, Park CM, Lee SK, Lee BI, Suh SW. </i> Proc Natl Acad Sci U S A, 2010","date":"2025-06-18T08:23:28.705Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"3AKJ"},{"db":"PDB","id":"3AKK"},{"db":"PDB","id":"3AKL"}],"region_id":"DP04385r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":10,"db":"PubChem","id":"CID:6022","statements":[{"type":"Supplementary material","text":"The crystals of ADP-bound CtkA were grown using a reservoir solution consisting of 100 mM sodium acetate at pH 5.5, 0.2 M sodium thiocyanate, and 20% (vol∕vol) PEG 3350, while supplementing the protein solution with 2 mM MgCl2 and 10 mM of ADP."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":10,"db":"PubChem","id":"CID:33113","statements":[{"type":"Supplementary material","text":"The crystals of ADP-bound CtkA were grown using a reservoir solution consisting of 100 mM sodium acetate at pH 5.5, 0.2 M sodium thiocyanate, and 20% (vol∕vol) PEG 3350, while supplementing the protein solution with 2 mM MgCl2 and 10 mM of ADP."}]}],"statement":[{"text":"However, the nucleotide binding induces ordering in one of the two flexible loops that are disordered in the apo structure. That is, the glycine-rich loop (Lys14–Gly22) is disordered in the apo structure, whereas it becomes ordered upon binding ADP or AMP-PNP.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:35:42.925Z"}},{"start":41,"end":50,"reference_id":"21098302","reference_source":"pmid","reference_html":"Helicobacter pylori proinflammatory protein up-regulates NF-kappaB as a cell-translocating Ser/Thr kinase. <i> Kim DJ, Park KS, Kim JH, Yang SH, Yoon JY, Han BG, Kim HS, Lee SJ, Jang JY, Kim KH, Kim MJ, Song JS, Kim HJ, Park CM, Lee SK, Lee BI, Suh SW. </i> Proc Natl Acad Sci U S A, 2010","date":"2025-06-10T14:52:59.239Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"3AKK"}],"region_id":"DP04385r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16761","entry_name":"ADP"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":"magnesium(2+)"}],"statement":[{"text":"As shown in the PDB crystal structures, in the presence of ADP, this disordered loop also gains structure.","type":"Curator statement"}]}],"regions_counter":4,"released":"2025_06","sequence":"MPTIDFTFCEINPKKGFGGANGNKISLFYNNELYMVKFPPKPSTHKEMSYTNGCFSEYVACHIVNSLGLKVQETLLGTYKNKIVVACKDFTTHQYELVDFLSLKNTMIELEKSGKDTNLNDVLYAIDNQHFIEPKVLKCFFWDMFVADTLLGNFDRHNGNWGFLRASNSKEYQIAPIFDCGSCLYPQADDVVCQKVLSNIDELNARIYNFPQSILKDDNDKKINYYDFLTQTNNKDCLDALLRIYPRIDMNKIHSIIDNTPFMSEIHKEFLHTMLDERKSKIIDVAHTRAIELSLQHKQAHSNPYDNADDLDNSNEYTPTPKRRR","taxonomy":["Bacteria","Pseudomonadati","Campylobacterota","Epsilonproteobacteria","Campylobacterales","Helicobacteraceae","Helicobacter"],"alphafold_very_low_content":0.052307692307692305,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.06153846153846154,"disprot_consensus":{"full":[{"start":14,"end":23,"type":"T"},{"start":41,"end":50,"type":"T"}],"Structural state":[{"start":14,"end":23,"type":"D"},{"start":41,"end":50,"type":"D"}],"Structural transition":[{"start":14,"end":23,"type":"T"},{"start":41,"end":50,"type":"T"}]}},{"disprot_id":"DP04386","acc":"Q45914","creator":"xcastro","date":"2025-04-29T13:06:36.701Z","features":{"pfam":[{"id":"PF01742","name":"Clostridial neurotoxin zinc protease","start":2,"end":326},{"id":"PF07953","name":"Clostridium neurotoxin, N-terminal receptor binding","start":848,"end":1023},{"id":"PF08470","name":"Nontoxic nonhaemagglutinin C-terminal","start":1032,"end":1193},{"id":"PF22133","name":"Botulinum neurotoxin, helical domain","start":506,"end":781}],"gene3D":[]},"genes":[{"name":{"value":"ant","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"8521962","url":"http://www.ncbi.nlm.nih.gov/pubmed/8521962","alternativeUrl":"https://europepmc.org/abstract/MED/8521962"}}]},"synonyms":[{"value":"ntnh"}],"orfNames":[{"value":"ACP52_06665"}]}],"length":1193,"name":"Non-toxic nonhemagglutinin type A","ncbi_taxon_id":1491,"organism":"Clostridium botulinum","regions":[{"start":114,"end":148,"reference_id":"22363010","reference_source":"pmid","reference_html":"Botulinum neurotoxin is shielded by NTNHA in an interlocked complex. <i> Gu S, Rumpel S, Zhou J, Strotmeier J, Bigalke H, Perry K, Shoemaker CB, Rummel A, Jin R. </i> Science, 2012","date":"2025-06-18T08:24:49.027Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"3V0A"},{"db":"PDB","id":"3V0B"}],"region_id":"DP04386r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0DPI1","statements":[{"type":"Supplementary material","text":"After extensive manual optimization, the best M-PTC crystals were grown by hanging-drop vapor diffusion at 20 ºC, in which the protein (~5 mg/ml) was mixed in 1:1 ratio with a reservoir solution containing 1.2 M sodium malonate (pH 5.8) and 0.5% n-dodecyl-N,N-dimethylamine-Noxide (LDAO)."},{"type":"Article","text":"The free forms of BoNT/Ai and NTNHA-A are monomeric at pH = 6.0 and 7.5 (fig. S2) and assemble into a monomeric M-PTC at pH = 6.0 with a dissociation constant (Kd) of ~30.8 nM and 1:1 stoichiometry, as analyzed by analytic ultracentrifugation (AUC) and isothermal titration calorimetry (ITC) (fig. S2 and table S1)."}]}],"statement":[{"text":"NTNHA-A has a large insert in nLC (nGly116 to nAla148, termed the nLoop) that is not present in LC.","type":"Article"},{"text":"The crystal structure reveals that the nLoop is fully exposed on the M-PTC surface and has no visible electron density, presumably because of its high flexibility (Fig. 1C).","type":"Article"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:36:01.379Z"}}],"regions_counter":2,"released":"2025_06","sequence":"MNINDNLSINSPVDNKNVVVVRARKTDTVFKAFKVAPNIWVAPERYYGESLSIDEEYKVDGGIYDSNFLSQDSEKDKFLQAIITLLKRINSTNAGEKLLSLISTAIPFPYGYIGGGYYAPNMITFGSAPKSNKKLNSLISSTIPFPYAGYRETNYLSSEDNKSFYASNIVIFGPGANIVENNTVFYKKEDAENGMGTMTEIWFQPFLTYKYDEFYIDPAIELIKCLIKSLYFLYGIKPSDDLVIPYRLRSELENIEYSQLNIVDLLVSGGIDPKFINTDPYWFTDNYFSNAKKVFEDHRNIYETEIEGNNAIGNDIKLRLKQKFRININDIWELNLNYFSKEFSIMMPDRFNNALKHFYRKQYYKIDYPENYSINGFVNGQINAQLSLSDRNQDIINKPEEIINLLNGNNVSLMRSNIYGDGLKSTVDDFYSNYKIPYNRAYEYHFNNSNDSSLDNVNIGVIDNIPEIIDVNPYKENCDKFSPVQKITSTREINTNIPWPINYLQAQNTNNEKFSLSSDFVEVVSSKDKSLVYSFLSNVMFYLDSIKDNSPIDTDKKYYLWLREIFRNYSFDITATQEINTNCGINKVVTWFGKALNILNTSDSFVEEFQNLGAISLINKKENLSMPIIESYEIPNDMLGLPLNDLNEKLFNIYSKNTAYFKKIYYNFLDQWWTQYYSQYFDLICMAKRSVLAQETLIKRIIQKKLSYLIGNSNISSDNLALMNLTTTNTLRDISNESQIAMNNVDSFLNNAAICVFESNIYPKFISFMEQCINNINIKTKEFIQKCTNINEDEKLQLINQNVFNSLDFEFLNIQNMKSLFSSETALLIKEETWPYELVLYAFKEPGNNVIGDASGKNTSIEYSKDIGLVYGINSDALYLNGSNQSISFSNDFFENGLTNSFSIYFWLRNLGKDTIKSKLIGSKEDNCGWEIYFQDTGLVFNMIDSNGNEKNIYLSDVSNNSWHYITISVDRLKEQLLIFIDDNLVANESIKEILNIYSSNIISLLSENNPSYIEGLTILNKPTTSQEVLSNYFEVLNNSYIRDSNEERLEYNKTYQLYNYVFSDKPICEVKQNNNIYLTINNTNNLNLQASKFKLLSINPNKQYVQKLDEVIISVLDNMEKYIDISEDNRLQLIDNKNNAKKMIISNDIFISNCLTLSYNGKYICLSMKDENHNWMICNNDMSKYLYLWSFK","taxonomy":["Bacteria","Bacillati","Bacillota","Clostridia","Eubacteriales","Clostridiaceae","Clostridium"],"alphafold_very_low_content":0.02933780385582565,"dataset":["Unicellular toxins and antitoxins","Bacterial virulence-related proteins"],"disorder_content":0.02933780385582565,"disprot_consensus":{"full":[{"start":114,"end":148,"type":"D"}],"Structural state":[{"start":114,"end":148,"type":"D"}]}},{"disprot_id":"DP04387","acc":"A0A0H2XCS3","creator":"xcastro","date":"2025-04-29T14:57:05.730Z","features":{"pfam":[{"id":"PF00360","name":"Phytochrome region","start":325,"end":510},{"id":"PF01590","name":"GAF domain","start":150,"end":306},{"id":"PF08446","name":"PAS fold","start":13,"end":119},{"id":"PF13426","name":"PAS domain","start":539,"end":632}],"gene3D":[]},"genes":[{"name":{"value":"bphP"},"olnNames":[{"value":"XC_4241"}]}],"length":634,"name":"Bacteriophytochrome","ncbi_taxon_id":314565,"organism":"Xanthomonas campestris pv. campestris (strain 8004)","regions":[{"start":457,"end":469,"reference_id":"34818032","reference_source":"pmid","reference_html":"Structural basis for the Pr-Pfr long-range signaling mechanism of a full-length bacterial phytochrome at the atomic level. <i> Otero LH, Foscaldi S, Antelo GT, Rosano GL, Sirigu S, Klinke S, Defelipe LA, Sánchez-Lamas M, Battocchio G, Conforte V, Vojnov AA, Chavas LMG, Goldbaum FA, Mroginski MA, Rinaldi J, Bonomi HR. </i> Sci Adv, 2021","date":"2025-06-18T08:33:44.468Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The cloned ORF includes an N-terminal methionine and His-tag followed by the complete coding sequence (with the exception of its starting residue: 2 to 634), totaling 640 residues."}]}],"cross_refs":[{"db":"PDB","id":"6PL0"}],"region_id":"DP04387r001","sequence_construct":"MHHHHHHSTATNPLDLDVCAREPIHIPGLIQPYGVLLVIDPADGRIVQASTTAADLLGVPMAALLGMPYTQVLTLPEAQPFAVDDQPQHLMHAEVRFPQRATPPASAWVAAWHLYPQQWLVEMEPRDARLLDVTLREAMPLLRSVERDPGIAEAAVRVAKGLRSLIGFDRVMIYRFDEEWNGDIIAEARKPELEAYLGLHYPASDIPAQARALYLRNRVRQIADVGYQPSPIQPTVHPQLGTPVDLSDVSLRSVSPVHLEYLANMGVTATLVASIVVNDALWGLISCHHYSPHFTNHAMRDVTDAVARTLAGRIGALQAVARARLESVLLTVREKLITDFNDAEHMTVELLDDMAPDLMDVVDADGVAIFHGNDISRHGTTPDVAALRRIRDHIESEHHEALREDAVGALHVDAIGEVFPELADLAPLAAGFIFVPLMPQSRSALLWTRREQIQQIKWAGNPQLAKLEDIPNSRLSPRKSFDLWQQTVRGRARRWSPLHLESARSLRVLIELMERKRFQQDFTLLEASLSRLRDGVAIIERGTANAAHRLLFVNTAFADVCGSDVAELIGRELQTLYASDAPRANVELLQDALRNGRAAYVTLPLQVSDGAPVYRQFHLEPLPSPSGVTAHWLLQLRDPE","statement":[{"text":"Residues 456 to 470 from the β-hairpin loop were not visible in the electron density map, indicating a high flexibility for this region.","type":"Results"},{"text":"The disordered region of the β-hairpin loop in the Pr structure is represented by a curved dashed line.","type":"Figure"},{"text":"The 2mFo-DFc electron density maps allowed for a fairly complete trace of the protein backbones with the exception for the initial 8 to 10 N-terminal residues and the regions comprising the residues 457 to 469 for the wild-type protein; 393 to 398, 527 to 528, 601 to 606, and 616 to 623 for G454E; and 333 to 340 and 389 to 401 for ΔPAS9(1–511), which correspond to exposed loops.","type":"Methods"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17033","entry_name":"biliverdin"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:36:56.515Z"}},{"start":457,"end":469,"reference_id":"34818032","reference_source":"pmid","reference_html":"Structural basis for the Pr-Pfr long-range signaling mechanism of a full-length bacterial phytochrome at the atomic level. <i> Otero LH, Foscaldi S, Antelo GT, Rosano GL, Sirigu S, Klinke S, Defelipe LA, Sánchez-Lamas M, Battocchio G, Conforte V, Vojnov AA, Chavas LMG, Goldbaum FA, Mroginski MA, Rinaldi J, Bonomi HR. </i> Sci Adv, 2021","date":"2025-06-18T08:33:23.219Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The cloned ORF includes an N-terminal methionine and His-tag followed by the complete coding sequence (with the exception of its starting residue: 2 to 634), totaling 640 residues."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly454Glu","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Phe512Glu634del","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"6PL0"},{"db":"PDB","id":"7L5A"},{"db":"PDB","id":"7L59"}],"region_id":"DP04387r002","sequence_construct":"MHHHHHHSTATNPLDLDVCAREPIHIPGLIQPYGVLLVIDPADGRIVQASTTAADLLGVPMAALLGMPYTQVLTLPEAQPFAVDDQPQHLMHAEVRFPQRATPPASAWVAAWHLYPQQWLVEMEPRDARLLDVTLREAMPLLRSVERDPGIAEAAVRVAKGLRSLIGFDRVMIYRFDEEWNGDIIAEARKPELEAYLGLHYPASDIPAQARALYLRNRVRQIADVGYQPSPIQPTVHPQLGTPVDLSDVSLRSVSPVHLEYLANMGVTATLVASIVVNDALWGLISCHHYSPHFTNHAMRDVTDAVARTLAGRIGALQAVARARLESVLLTVREKLITDFNDAEHMTVELLDDMAPDLMDVVDADGVAIFHGNDISRHGTTPDVAALRRIRDHIESEHHEALREDAVGALHVDAIGEVFPELADLAPLAAGFIFVPLMPQSRSALLWTRREQIQQIKWAGNPQLAKLEDIPNSRLSPRKSFDLWQQTVRGRARRWSPLHLESARSLRVLIELMERKR","statement":[{"text":"Residues 456 to 470 from the β-hairpin loop were not visible in the electron density map, indicating a high flexibility for this region.","type":"Results"},{"text":"The disordered region of the β-hairpin loop in the Pr structure is represented by a curved dashed line.","type":"Figure"},{"text":"On the contrary, in the Pfr state, the tongue undergoes a conformational change interconverting the entrance and exit β strands in a loop and an α helix, respectively (Figs. 4B and 5A, middle).","type":"Results"},{"text":"The authors report that this region is disordered in the Pr (red light–absorbing) photostate and adopts an ordered conformation in the Pfr (far-red light–absorbing) photostate. To compare the structural differences between photostates, they analyzed wild-type protein crystals in the Pr state and two variants that favor the Pfr state: a deletion mutant lacking the PAS9 domain [ΔPAS9(1–511)] and a point mutant carrying the G454E substitution.","type":"Curator statement"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17033","entry_name":"biliverdin"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:36:54.036Z"}}],"regions_counter":3,"released":"2025_06","sequence":"MSTATNPLDLDVCAREPIHIPGLIQPYGVLLVIDPADGRIVQASTTAADLLGVPMAALLGMPYTQVLTLPEAQPFAVDDQPQHLMHAEVRFPQRATPPASAWVAAWHLYPQQWLVEMEPRDARLLDVTLREAMPLLRSVERDPGIAEAAVRVAKGLRSLIGFDRVMIYRFDEEWNGDIIAEARKPELEAYLGLHYPASDIPAQARALYLRNRVRQIADVGYQPSPIQPTVHPQLGTPVDLSDVSLRSVSPVHLEYLANMGVTATLVASIVVNDALWGLISCHHYSPHFTNHAMRDVTDAVARTLAGRIGALQAVARARLESVLLTVREKLITDFNDAEHMTVELLDDMAPDLMDVVDADGVAIFHGNDISRHGTTPDVAALRRIRDHIESEHHEALREDAVGALHVDAIGEVFPELADLAPLAAGFIFVPLMPQSRSALLWTRREQIQQIKWAGNPQLAKLEDIPNSRLSPRKSFDLWQQTVRGRARRWSPLHLESARSLRVLIELMERKRFQQDFTLLEASLSRLRDGVAIIERGTANAAHRLLFVNTAFADVCGSDVAELIGRELQTLYASDAPRANVELLQDALRNGRAAYVTLPLQVSDGAPVYRQFHLEPLPSPSGVTAHWLLQLRDPE","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Lysobacteraceae","Xanthomonas"],"alphafold_very_low_content":0.031545741324921134,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.02050473186119874,"disprot_consensus":{"full":[{"start":457,"end":469,"type":"T"}],"Structural state":[{"start":457,"end":469,"type":"D"}],"Structural transition":[{"start":457,"end":469,"type":"T"}]}},{"disprot_id":"DP04388","acc":"Q86VY4","creator":"rpancsa","date":"2025-04-30T06:30:34.303Z","features":{"pfam":[{"id":"PF00956","name":"Nucleosome assembly protein (NAP)","start":246,"end":339}],"gene3D":[]},"genes":[{"name":{"value":"TSPYL5"},"synonyms":[{"value":"KIAA1750"}]}],"length":417,"name":"Testis-specific Y-encoded-like protein 5","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":195,"reference_id":"40260937","reference_source":"pmid","reference_html":"Structural insights into the interaction between testis-specific Y-encoded-like protein 5 and ubiquitin-specific protease 7. <i> Ancia M, Wahni K, Chakrowf J, El Aakchioui A, Claude E, de Lhoneux G, Liberelle M, Janvier S, Baranova E, Malo Pueyo J, Jijon Vergara A, Papadopoulos N, Balty C, Dejeu J, Decottignies A, Messens J, Frédérick R. </i> Protein Sci, 2025","date":"2025-04-30T06:43:05.703Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04388r001","statement":[{"text":"Circular dichroism (CD) and nano differential scanning fluorimetry (nanoDSF) analysis revealed TSPYL5 FL exhibits at least partial folding, with an α-helical and β-sheet content (two minima near 208 nm and 222 nm) (Figure 2e) and a melting temperature of 63.2\u0001C (Figure 2f). In contrast, TSPYL5 TR showed profiles typical of unfolded proteins, consistent with structural predictions (Figure 2g,h).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-26T16:29:29.538Z"}},{"start":1,"end":195,"reference_id":"40260937","reference_source":"pmid","reference_html":"Structural insights into the interaction between testis-specific Y-encoded-like protein 5 and ubiquitin-specific protease 7. <i> Ancia M, Wahni K, Chakrowf J, El Aakchioui A, Claude E, de Lhoneux G, Liberelle M, Janvier S, Baranova E, Malo Pueyo J, Jijon Vergara A, Papadopoulos N, Balty C, Dejeu J, Decottignies A, Messens J, Frédérick R. </i> Protein Sci, 2025","date":"2025-04-30T06:43:50.592Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006334","ec_ontology":"ECO","ec_name":"differential scanning fluorimetry evidence","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04388r002","statement":[{"text":"Circular dichroism (CD) and nano differential scanning fluorimetry (nanoDSF) analysis revealed TSPYL5 FL exhibits at least partial folding, with an α-helical and β-sheet content (two minima near 208 nm and 222 nm) (Figure 2e) and a melting temperature of 63.2\u0001C (Figure 2f). In contrast, TSPYL5 TR showed profiles typical of unfolded proteins, consistent with structural predictions (Figure 2g,h).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-26T16:29:26.643Z"}},{"start":1,"end":242,"reference_id":"40260937","reference_source":"pmid","reference_html":"Structural insights into the interaction between testis-specific Y-encoded-like protein 5 and ubiquitin-specific protease 7. <i> Ancia M, Wahni K, Chakrowf J, El Aakchioui A, Claude E, de Lhoneux G, Liberelle M, Janvier S, Baranova E, Malo Pueyo J, Jijon Vergara A, Papadopoulos N, Balty C, Dejeu J, Decottignies A, Messens J, Frédérick R. </i> Protein Sci, 2025","date":"2025-04-30T07:33:08.823Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04388r003","statement":[{"text":"The HDx-MS data (Figure 2i) revealed that most of TSPYL5 exchanges deuterium rapidly, suggesting a predominantly flexible and disordered\nconformation. ","type":"Results"},{"text":"Examining Figure 1 (b) as well as  Figure 2 (d) and (i) panels clearly supports that not only the region 1-195 corresponding to the TSPYL5 TR construct (pink in panel (d)) has experienced very high H-D exchange in 60 seconds, but also the following log alpha helix. So the full region corresponding to previously used constructs TSPYL5 #1 and #2 (region 1-242) experiences very high H-D exchage rates that is a hallmark of the disodered state.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-26T16:41:01.789Z"}},{"start":1,"end":195,"reference_id":"40260937","reference_source":"pmid","reference_html":"Structural insights into the interaction between testis-specific Y-encoded-like protein 5 and ubiquitin-specific protease 7. <i> Ancia M, Wahni K, Chakrowf J, El Aakchioui A, Claude E, de Lhoneux G, Liberelle M, Janvier S, Baranova E, Malo Pueyo J, Jijon Vergara A, Papadopoulos N, Balty C, Dejeu J, Decottignies A, Messens J, Frédérick R. </i> Protein Sci, 2025","date":"2025-04-30T06:56:49.541Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006303","ec_ontology":"ECO","ec_name":"microscale thermophoresis evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q93009","operator":null,"partner_start":1,"partner_end":1102}],"region_id":"DP04388r004","statement":[{"text":"In line with the cellular data, TSPYL5 TR also demonstrated strong binding to USP7 with a Kd of 102.4 nM (Figure 3b)","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-26T16:41:46.489Z"}},{"start":1,"end":195,"reference_id":"40260937","reference_source":"pmid","reference_html":"Structural insights into the interaction between testis-specific Y-encoded-like protein 5 and ubiquitin-specific protease 7. <i> Ancia M, Wahni K, Chakrowf J, El Aakchioui A, Claude E, de Lhoneux G, Liberelle M, Janvier S, Baranova E, Malo Pueyo J, Jijon Vergara A, Papadopoulos N, Balty C, Dejeu J, Decottignies A, Messens J, Frédérick R. </i> Protein Sci, 2025","date":"2025-04-30T07:11:39.303Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0000353","ec_ontology":"ECO","ec_name":"physical interaction evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q93009","operator":null,"partner_start":68,"partner_end":195}],"region_id":"DP04388r005","statement":[{"text":"Similarly, the MATH domain exhibited comparable affinity for TSPYL5 TR, with a mean Kd of 2.1 nM.","type":"Results"},{"text":"This Kd was measured in a BLI experiment.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-26T16:43:25.425Z"}},{"start":65,"end":97,"reference_id":"40260937","reference_source":"pmid","reference_html":"Structural insights into the interaction between testis-specific Y-encoded-like protein 5 and ubiquitin-specific protease 7. <i> Ancia M, Wahni K, Chakrowf J, El Aakchioui A, Claude E, de Lhoneux G, Liberelle M, Janvier S, Baranova E, Malo Pueyo J, Jijon Vergara A, Papadopoulos N, Balty C, Dejeu J, Decottignies A, Messens J, Frédérick R. </i> Protein Sci, 2025","date":"2025-04-30T07:10:50.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006303","ec_ontology":"ECO","ec_name":"microscale thermophoresis evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q93009","operator":null,"partner_start":1,"partner_end":1102}],"region_id":"DP04388r006","statement":[{"text":"MST screening identified three overlapping peptides (peptides 9, 10, and 11) in the N-terminal region of TSPYL5 that bound to USP7, with dissociation constants (Kd) ranging from 12.6 to 500 μM (Figure 4d–e and Table S2). These peptides map to amino acids 65–97 of TSPYL5, suggesting this region forms a key interaction hotspot.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-30T23:49:50.608Z"}},{"start":1,"end":195,"reference_id":"40260937","reference_source":"pmid","reference_html":"Structural insights into the interaction between testis-specific Y-encoded-like protein 5 and ubiquitin-specific protease 7. <i> Ancia M, Wahni K, Chakrowf J, El Aakchioui A, Claude E, de Lhoneux G, Liberelle M, Janvier S, Baranova E, Malo Pueyo J, Jijon Vergara A, Papadopoulos N, Balty C, Dejeu J, Decottignies A, Messens J, Frédérick R. </i> Protein Sci, 2025","date":"2025-04-30T07:18:07.566Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0051260","term_name":"protein homooligomerization","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP04388r007","statement":[{"text":"To gain deeper insights into the oligomerization process of TSPYL5, we examined its truncated form (TSPYL5 TR, residues 1–195). Mass spectrometry determined its molecular weight (MW) to be 21 kDa, but size exclusion chromatography (SEC) analysis indicated a MW of ~65 kDa, suggesting trimer formation (Figure 2a).","type":"Results"},{"text":"These findings imply that the N-terminal region of TSPYL5 plays a crucial role in trimer formation, while the C-terminal region likely mediates the interaction of two trimers, leading to hexamer formation.","type":"Results"}],"term_comment":"","term_def":"\"The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-26T16:47:38.499Z"}},{"start":1,"end":123,"reference_id":"40260937","reference_source":"pmid","reference_html":"Structural insights into the interaction between testis-specific Y-encoded-like protein 5 and ubiquitin-specific protease 7. <i> Ancia M, Wahni K, Chakrowf J, El Aakchioui A, Claude E, de Lhoneux G, Liberelle M, Janvier S, Baranova E, Malo Pueyo J, Jijon Vergara A, Papadopoulos N, Balty C, Dejeu J, Decottignies A, Messens J, Frédérick R. </i> Protein Sci, 2025","date":"2025-04-30T07:23:19.201Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q93009","operator":null,"partner_start":1,"partner_end":1102}],"region_id":"DP04388r008","statement":[{"text":"As expected, FlagTSPYL5 FL efficiently co-immunoprecipitated USP7, confirming their interaction. Flag-TSPYL5 #1 also pulled down USP7, indicating that this part of TSPYL5 mediates the interaction.","type":"Results"},{"text":"TSPYL5 #1 corresponds to the region 1-123.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-26T16:30:04.131Z"}},{"start":124,"end":242,"reference_id":"40260937","reference_source":"pmid","reference_html":"Structural insights into the interaction between testis-specific Y-encoded-like protein 5 and ubiquitin-specific protease 7. <i> Ancia M, Wahni K, Chakrowf J, El Aakchioui A, Claude E, de Lhoneux G, Liberelle M, Janvier S, Baranova E, Malo Pueyo J, Jijon Vergara A, Papadopoulos N, Balty C, Dejeu J, Decottignies A, Messens J, Frédérick R. </i> Protein Sci, 2025","date":"2025-04-30T07:24:43.204Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006030","ec_ontology":"ECO","ec_name":"co-immunoprecipitation evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"Q93009","operator":null,"partner_start":1,"partner_end":1102}],"region_id":"DP04388r009","statement":[{"text":"Additionally, Flag-TSPYL5 #2, which includes the predicted α-helix, also recovered USP7, indicating an additional interaction site within this region. ","type":"Results"},{"text":"TSPYL5 #2 corresponds to the region 124-242.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-26T16:47:56.322Z"}}],"regions_counter":10,"released":"2025_06","sequence":"MSGRSRGRKSSRAKNRGKGRAKARVRPAPDDAPRDPDPSQYQSLGEDTQAAQVQAGAGWGGLEAAASAQLLRLGEEAACRLPLDCGLALRARAAGDHGQAAARPGPGKAASLSERLAADTVFVGTAGTVGRPKNAPRVGNRRGPAGKKAPETCSTAGRGPQVIAGGRQKKGAAGENTSVSAGEEKKEERDAGSGPPATEGSMDTLENVQLKLENMNAQADRAYLRLSRKFGQLRLQHLERRNHLIQNIPGFWGQAFQNHPQLASFLNSQEKEVLSYLNSLEVEELGLARLGYKIKFYFDRNPYFQNKVLIKEYGCGPSGQVVSRSTPIQWLPGHDLQSLSQGNPENNRSFFGWFSNHSSIESDKIVEIINEELWPNPLQFYLLSEGARVEKGKEKEGRQGPGKQPMETTQPGVSQSN","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.5011990407673861,"disorder_content":0.580335731414868,"disprot_consensus":{"full":[{"start":1,"end":242,"type":"D"}],"Structural state":[{"start":1,"end":242,"type":"D"}],"Molecular function":[{"start":1,"end":242,"type":"F"}],"Biological process":[{"start":1,"end":195,"type":"F"}]}},{"disprot_id":"DP04390","acc":"A1C3L3","creator":"xcastro","date":"2025-04-30T09:42:33.313Z","features":{"pfam":[{"id":"PF00746","name":"LPXTG cell wall anchor motif","start":2547,"end":2585},{"id":"PF04286","name":"Protein of unknown function (DUF445)","start":2292,"end":2544},{"id":"PF19258","name":"KxYKxGKxW signal peptide","start":12,"end":44}],"gene3D":[]},"genes":[{"name":{"value":"fap1"}}],"length":2587,"name":"Fap1 adhesin","ncbi_taxon_id":1318,"organism":"Streptococcus parasanguinis","regions":[{"start":201,"end":212,"reference_id":"20584910","reference_source":"pmid","reference_html":"Structural insights into serine-rich fimbriae from Gram-positive bacteria. <i> Ramboarina S, Garnett JA, Zhou M, Li Y, Peng Z, Taylor JD, Lee WC, Bodey A, Murray JW, Alguel Y, Bergeron J, Bardiaux B, Sawyer E, Isaacson R, Tagliaferri C, Cota E, Nilges M, Simpson P, Ruiz T, Wu H, Matthews S. </i> J Biol Chem, 2010","date":"2025-04-30T11:41:26.760Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":8,"statements":[{"type":"Results","text":"Two-dimensional 1H-15N HSQC spectra display excellent dispersion in backbone amide chemical shifts at pH 8, consistent with a folded polypeptide (supplemental Fig. S4)."},{"type":"Results","text":"The 15N relaxation rates at pH 8 for backbone amides between Glu-128 and Leu-208 reveal a well ordered structure with no flexible loops or residues in chemical exchange, although the termini (residues 116–127 and 209–231) are highly flexible."}]}],"cross_refs":[{"db":"PDB","id":"2KUB"}],"region_id":"DP04390r003","statement":[{"text":"The 15N relaxation rates at pH 8 for backbone amides between Glu-128 and Leu-208 reveal a well ordered structure with no flexible loops or residues in chemical exchange, although the termini (residues 116–127 and 209–231) are highly flexible.","type":"Results"},{"text":"The highly flexible regions reported by the authors in the paper correspond to residues 201-212 and 294-316 in the UniProt sequence.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-10T18:46:30.285Z"}},{"start":294,"end":316,"reference_id":"20584910","reference_source":"pmid","reference_html":"Structural insights into serine-rich fimbriae from Gram-positive bacteria. <i> Ramboarina S, Garnett JA, Zhou M, Li Y, Peng Z, Taylor JD, Lee WC, Bodey A, Murray JW, Alguel Y, Bergeron J, Bardiaux B, Sawyer E, Isaacson R, Tagliaferri C, Cota E, Nilges M, Simpson P, Ruiz T, Wu H, Matthews S. </i> J Biol Chem, 2010","date":"2025-04-30T11:41:53.995Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":8,"statements":[{"type":"Results","text":"Two-dimensional 1H-15N HSQC spectra display excellent dispersion in backbone amide chemical shifts at pH 8, consistent with a folded polypeptide (supplemental Fig. S4)."},{"type":"Results","text":"The 15N relaxation rates at pH 8 for backbone amides between Glu-128 and Leu-208 reveal a well ordered structure with no flexible loops or residues in chemical exchange, although the termini (residues 116–127 and 209–231) are highly flexible."}]}],"cross_refs":[{"db":"PDB","id":"2KUB"}],"region_id":"DP04390r004","statement":[{"text":"The 15N relaxation rates at pH 8 for backbone amides between Glu-128 and Leu-208 reveal a well ordered structure with no flexible loops or residues in chemical exchange, although the termini (residues 116–127 and 209–231) are highly flexible.","type":"Results"},{"text":"The highly flexible regions reported by the authors in the paper correspond to residues 201-212 and 294-316 in the UniProt sequence.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-10T18:46:29.685Z"}}],"regions_counter":4,"released":"2025_06","sequence":"MGKYKRAGETSRKTRVKMHKSGKNWVRTLISQIGLMHFLGGSISEKKINVDVYEQKNISASTILKGAVALGALTGATVVSGNVFADETVLAKETTLTTTDANEVKLSSENFDSEKAEEKISLSQSESASESVSESISESVSESVSTSESVSESVSESVSESISESVSESISESISESVSESTSTSIVLSESGAASGNKATSKGTEEKQDSVRENLDKMISEAEVLNDMAARKLITLDAEQQLELMKSLVATQSQLEATKNLIGDPNATVADLQIAYTTLGNNTQALGNELIKLNPNGQIYAVLNNTEASRAATLRSTTTGTKTTFTISDFSNGGTQYYWAGGNANNLKNPISSISAVYDSATGKISWTVEYDPTTILKSPALKTLKTYTGIYIDTSSDSKLSTPTNVLIDGAATNPVTNFYGNGSKGIEYVSKGTTKGVTKHTITFDTAFSGRANDLADLKIKMLAATTLSDPHFYEDGSKGNYGRYNGQTAPYVIANDSGTAIGGYQVSGVNADSIPSDTTSQSESTSKSESTSKSISESVIESISESVIGSVSESVSESVSESVSESITESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESISESVSESVSESISESVSESVSESISERTLPNTGENVSSSLGLVGLSGLLFGALLGRKKRKSEDAE","taxonomy":["Bacteria","Bacillati","Bacillota","Bacilli","Lactobacillales","Streptococcaceae","Streptococcus"],"alphafold_very_low_content":0.8793969849246231,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.01352918438345574,"disprot_consensus":{"full":[{"start":201,"end":212,"type":"D"},{"start":294,"end":316,"type":"D"}],"Structural state":[{"start":201,"end":212,"type":"D"},{"start":294,"end":316,"type":"D"}]}},{"disprot_id":"DP04391","acc":"A0AAI7ZGD2","creator":"rpancsa","date":"2025-04-30T11:50:49.148Z","features":{"pfam":[{"id":"PF10671","name":"Toxin co-regulated pilus biosynthesis protein Q","start":55,"end":124}],"gene3D":[]},"genes":[{"olnNames":[{"value":"XAC2622","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAM37471.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAM37471.1"}}]}]}],"length":139,"name":"Toxin co-regulated pilus biosynthesis protein Q C-terminal domain-containing protein","ncbi_taxon_id":190486,"organism":"Xanthomonas axonopodis pv. citri (strain 306)","regions":[{"start":24,"end":46,"reference_id":"38486495","reference_source":"pmid","reference_html":"Uncovering the Association Mechanism between Two Intrinsically Flexible Proteins. <i> Dávalos AL, Rivera Echeverri JD, Favaro DC, Junio de Oliveira R, Penteado Battesini Carretero G, Lacerda C, Midea Cuccovia I, Cangussu Cardoso MV, Farah CS, Kopke Salinas R. </i> ACS Chem Biol, 2024","date":"2025-04-30T11:52:55.999Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04391r001","statement":[{"text":"The CD spectrum of VirB7Nt is typical of a random coil, as expected for a short peptide in aqueous solution (Figure 2A). The VirB7Nt peptide is a good model for the N-terminal tail within VirB7, which shows fast\nbackbone motions, as revealed by measurements of 15N relaxation rates.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-04T13:52:17.815Z"}},{"start":24,"end":51,"reference_id":"21589901","reference_source":"pmid","reference_html":"A component of the Xanthomonadaceae type IV secretion system combines a VirB7 motif with a N0 domain found in outer membrane transport proteins. <i> Souza DP, Andrade MO, Alvarez-Martinez CE, Arantes GM, Farah CS, Salinas RK. </i> PLoS Pathog, 2011","date":"2025-04-30T20:23:17.410Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04391r002","statement":[{"text":"The solution structure of VirB7XAC2622_24–139 consists of a globular domain (residues 52–133), flanked by a long disordered N-terminus (amino acids 24–51) and a short flexible C-terminus (residues 134–139) (Figure 1A).","type":"Results"},{"text":"The relaxation data are consistent with the presence of a flexible N-terminal tail and a more rigid globular domain (Figure 5).","type":"Results"}],"cross_refs":[{"db":"PDB","id":"2L4W"},{"db":"BMRB","id":"17257"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-03T18:04:58.311Z"}},{"start":24,"end":50,"reference_id":"21589901","reference_source":"pmid","reference_html":"A component of the Xanthomonadaceae type IV secretion system combines a VirB7 motif with a N0 domain found in outer membrane transport proteins. <i> Souza DP, Andrade MO, Alvarez-Martinez CE, Arantes GM, Farah CS, Salinas RK. </i> PLoS Pathog, 2011","date":"2025-06-05T16:17:38.247Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0042802","term_name":"identical protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001170","ec_ontology":"ECO","ec_name":"cross-linking evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04391r004","statement":[{"text":"To investigate whether VirB7XAC2622_24–139 forms dimers or higher-order oligomers, glutaraldehyde cross-linking experiments were performed. These assays showed that VirB7XAC2622_24–139 forms dimers, trimers and higher order oligomers (Figure S4A). When the cross-linking experiment was performed in the presence of 1% SDS, no covalently cross-linked oligomers were observed, indicating that oligomerization requires the presence of a correctly folded protein (Figure S4A). As expected, no cross-links were observed when the experiment was performed using VirB7XAC2622_51–134 which lacks the disordered N-terminal region (Figure S4B).","type":"Results"}],"ec_go":"IPI","term_comment":"","term_def":"\"Binding to an identical protein or proteins.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"A0AAI7ZGD2","operator":"and","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T21:21:27.329Z"}},{"start":27,"end":41,"reference_id":"21589901","reference_source":"pmid","reference_html":"A component of the Xanthomonadaceae type IV secretion system combines a VirB7 motif with a N0 domain found in outer membrane transport proteins. <i> Souza DP, Andrade MO, Alvarez-Martinez CE, Arantes GM, Farah CS, Salinas RK. </i> PLoS Pathog, 2011","date":"2025-06-05T08:18:20.908Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"A0AAI8ESY0","operator":null,"partner_start":154,"partner_end":255}],"region_id":"DP04391r005","statement":[{"text":"In order to map the VirB9 binding site on the structure of VirB7, we assigned the backbone resonances of VirB7XAC2622_24–139 in complex with VirB9XAC2620_154–255 and analyzed the chemical shift differences (Figure 3A and B). This analysis showed that only residues 27–41, within the disordered VirB7 N-terminus, undergo significant chemical shift perturbations (Figure 3C and D).","type":"Results"},{"text":"Indeed, the perturbations observed in the 15N-HSQC spectra of VirB9XAC2620_154–255 in the presence of the full-length VirB7XAC2622_24–139 or the VirB7XAC2622_24–46 peptide are essentially the same (Figure 4 and Figure S8), demonstrating that the VirB7 N-terminal region is sufficient to interact with the VirB9XAC2620 C-terminal domain.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T13:27:24.978Z"}},{"start":24,"end":46,"reference_id":"27594685","reference_source":"pmid","reference_html":"VirB7 and VirB9 Interactions Are Required for the Assembly and Antibacterial Activity of a Type IV Secretion System. <i> Oliveira LC, Souza DP, Oka GU, Lima FDS, Oliveira RJ, Favaro DC, Wienk H, Boelens R, Farah CS, Salinas RK. </i> Structure, 2016","date":"2025-05-09T07:55:09.856Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"A0AAI8ESY0","operator":null,"partner_start":154,"partner_end":255}],"region_id":"DP04391r007","statement":[{"text":"VirB7NT binds to VirB9CT in slow exchange at the NMR chemical shift timescale (Souza et al., 2011), with an apparent dissociation constant of 1 μM as estimated by isothermal titration calorimetry (ITC) at 37°C (Table 1).","type":"Results"},{"text":"Authors previously defined that the VirB7NT construct used covers residues 24-46 of VirB7.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-04T14:19:30.566Z"}},{"start":29,"end":38,"reference_id":"27594685","reference_source":"pmid","reference_html":"VirB7 and VirB9 Interactions Are Required for the Assembly and Antibacterial Activity of a Type IV Secretion System. <i> Oliveira LC, Souza DP, Oka GU, Lima FDS, Oliveira RJ, Favaro DC, Wienk H, Boelens R, Farah CS, Salinas RK. </i> Structure, 2016","date":"2025-05-09T08:15:09.930Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"A0AAI8ESY0","operator":null,"partner_start":154,"partner_end":255}],"region_id":"DP04391r009","statement":[{"text":"While the segment between VirB7NT D29 and N38 of VirB7NT is well defined, the NMR structure displays lower precision at its N- and C-terminal tails (residues 24–28 and 39–46).","type":"Results"},{"text":"The authors list shifts/contacts of the different residues from which it is apparent that the region 29-38 of VirB7 is mainly responsible for VirB9CT binding. There is also foldig up on binding of a very short segment (residues 35-36) forming a short beta strand in the complex that augments a beta sheet of VirB9CT.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-04T14:17:35.211Z"}},{"start":42,"end":49,"reference_id":"21589901","reference_source":"pmid","reference_html":"A component of the Xanthomonadaceae type IV secretion system combines a VirB7 motif with a N0 domain found in outer membrane transport proteins. <i> Souza DP, Andrade MO, Alvarez-Martinez CE, Arantes GM, Farah CS, Salinas RK. </i> PLoS Pathog, 2011","date":"2025-06-05T08:15:01.689Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0042802","term_name":"identical protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"A0AAI7ZGD2","operator":null,"partner_start":52,"partner_end":133}],"region_id":"DP04391r010","statement":[{"text":"Chemical shift perturbation data showed that two regions are involved in VirB7XAC2622 self-interactions: a region in the unfolded N-terminus (residues 42–49) and a patch on the surface of the globular domain made up of residues 63–65, 85–93, 111–119 and 131 (Figure 2B and C).","type":"Results"}],"term_comment":"","term_def":"\"Binding to an identical protein or proteins.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T13:24:38.609Z"}},{"start":24,"end":46,"reference_id":"38486495","reference_source":"pmid","reference_html":"Uncovering the Association Mechanism between Two Intrinsically Flexible Proteins. <i> Dávalos AL, Rivera Echeverri JD, Favaro DC, Junio de Oliveira R, Penteado Battesini Carretero G, Lacerda C, Midea Cuccovia I, Cangussu Cardoso MV, Farah CS, Kopke Salinas R. </i> ACS Chem Biol, 2024","date":"2025-05-10T07:20:23.518Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"A0AAI8ESY0","operator":null,"partner_start":154,"partner_end":255}],"region_id":"DP04391r011","statement":[{"text":"Binding of VirB9Ct to VirB7Nt is enthalpically driven as indicated by isothermal titration calorimetry (ITC) experiments carried out at 10, 25, and 35 °C (Figure 3A,B). The VirB9Ct−VirB7Nt Kd app (see Experimental Section) is 0.70 μM at 35 °C, similar to the value reported before.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-04T13:52:46.704Z"}},{"start":24,"end":46,"reference_id":"38486495","reference_source":"pmid","reference_html":"Uncovering the Association Mechanism between Two Intrinsically Flexible Proteins. <i> Dávalos AL, Rivera Echeverri JD, Favaro DC, Junio de Oliveira R, Penteado Battesini Carretero G, Lacerda C, Midea Cuccovia I, Cangussu Cardoso MV, Farah CS, Kopke Salinas R. </i> ACS Chem Biol, 2024","date":"2025-05-10T08:24:54.011Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006337","ec_ontology":"ECO","ec_name":"stopped-flow fluorescence spectroscopy evidence","unpublished":true,"released":"2025_06","version":0,"interaction_partner":[{"db":"UniProt","id":"A0AAI8ESY0","operator":null,"partner_start":154,"partner_end":255}],"region_id":"DP04391r012","statement":[{"text":"The presence of tryptophan residues at positions 177 and 34 in VirB9Ct and VirB7Nt, respectively, and the millisecond exchange time scale\nbetween unbound and bound VirB9Ct states, favored the use of stopped-flow fluorescence to follow the VirB9Ct−VirB7Nt association kinetics.","type":"Results"},{"text":"These observations suggest that the VirB9Ct interaction with VirB7Nt could be described by a conformational-selection mechanism at 25 °C.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-04T13:53:44.322Z"}},{"start":24,"end":46,"reference_id":"38486495","reference_source":"pmid","reference_html":"Uncovering the Association Mechanism between Two Intrinsically Flexible Proteins. <i> Dávalos AL, Rivera Echeverri JD, Favaro DC, Junio de Oliveira R, Penteado Battesini Carretero G, Lacerda C, Midea Cuccovia I, Cangussu Cardoso MV, Farah CS, Kopke Salinas R. </i> ACS Chem Biol, 2024","date":"2025-05-10T08:32:45.353Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006301","ec_ontology":"ECO","ec_name":"protein thermal shift assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"A0AAI8ESY0","operator":null,"partner_start":154,"partner_end":255}],"region_id":"DP04391r013","statement":[{"text":"Notably, the thermal denaturation experiment showed that the complex has significantly higher unfolding enthalpy (29.57 kcal/mol) than the unbound VirB9Ct (10.42 kcal/mol; Figure 2C). This observation may be explained considering that VirB9Ct−VirB7Nt unfolding and dissociation occur within a single transition as a consequence of the coupling between these two processes.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-04T13:52:54.994Z"}},{"start":24,"end":46,"reference_id":"38486495","reference_source":"pmid","reference_html":"Uncovering the Association Mechanism between Two Intrinsically Flexible Proteins. <i> Dávalos AL, Rivera Echeverri JD, Favaro DC, Junio de Oliveira R, Penteado Battesini Carretero G, Lacerda C, Midea Cuccovia I, Cangussu Cardoso MV, Farah CS, Kopke Salinas R. </i> ACS Chem Biol, 2024","date":"2025-05-10T08:34:46.519Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"A0AAI8ESY0","operator":null,"partner_start":154,"partner_end":255}],"region_id":"DP04391r014","statement":[{"text":"The greater ANS fluorescence change observed upon addition of the free protein relative to the complex indicates that the unbound VirB9Ct exposes a greater amount of hydrophobic surface area than the complex.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-04T13:51:57.253Z"}},{"start":27,"end":49,"reference_id":"21589901","reference_source":"pmid","reference_html":"A component of the Xanthomonadaceae type IV secretion system combines a VirB7 motif with a N0 domain found in outer membrane transport proteins. <i> Souza DP, Andrade MO, Alvarez-Martinez CE, Arantes GM, Farah CS, Salinas RK. </i> PLoS Pathog, 2011","date":"2025-06-03T18:32:05.594Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0043684","term_name":"type IV secretion system complex","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP04391r015","statement":[{"text":"This analysis showed that only residues 27–41, within the disordered VirB7 N-terminus, undergo significant chemical shift perturbations (Figure 3C and D). This region is adjacent to, but does not overlap, the N-terminal region involved in VirB7XAC2622 oligomerization (residues 42–49).","type":"Results"},{"text":"Chemical shift perturbation data showed that two regions are involved in VirB7XAC2622 self-interactions: a region in the unfolded N-terminus (residues 42–49) and a patch on the surface of the globular domain made up of residues 63–65, 85–93, 111–119 and 131 (Figure 2B and C).","type":"Results"},{"text":"In well-characterized T4SSs, VirB7 is a lipoprotein attached to the periplasmic side of the outer membrane [28]. It has been shown to interact with several T4SS subunits [29], including itself [30] and the VirB9 C-terminal region [31], [32]. ","type":"Introduction"}],"term_comment":"","term_def":"\"A complex of proteins related to those involved in bacterial DNA conjugative transfer, that permits the transfer of DNA or proteins into the extracellular milieu or directly into host cells. In general the type IV complex forms a multisubunit cell-envelope-spanning structure composed of a secretion channel and often a pilus or other surface filament or protein(s).\" [GOC:ml]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":15,"released":"2025_06","sequence":"MNPMYVSKLSLVLVAAALVGACATKPAPDFGGRWKHVNHFDEAPTEIPLYTSYTYQATPMDGTLKTMLERWAADSNMQLSYNLPSDYTLIGPVSAISTTSVQQAATELSAVYAAQGVSVSVSANKLLVQPVPVSSGAKL","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Lysobacteraceae","Xanthomonas"],"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.2014388489208633,"disprot_consensus":{"full":[{"start":24,"end":51,"type":"D"}],"Structural state":[{"start":24,"end":51,"type":"D"}],"Molecular function":[{"start":24,"end":50,"type":"F"}],"Cellular component":[{"start":27,"end":49,"type":"F"}]}},{"disprot_id":"DP04392","acc":"Q83RJ4","creator":"xcastro","date":"2025-04-30T12:55:12.348Z","features":{"pfam":[{"id":"PF12468","name":"Type III secretion system leucine rich repeat protein","start":7,"end":51},{"id":"PF14496","name":"C-terminal novel E3 ligase, LRR-interacting","start":288,"end":497}],"gene3D":[]},"genes":[{"name":{"value":"ipaH3"},"olnNames":[{"value":"SF1383"}]}],"length":571,"name":"E3 ubiquitin-protein ligase ipaH3","ncbi_taxon_id":623,"organism":"Shigella flexneri","regions":[{"start":1,"end":24,"reference_id":"18997779","reference_source":"pmid","reference_html":"Structure of a Shigella effector reveals a new class of ubiquitin ligases. <i> Zhu Y, Li H, Hu L, Wang J, Zhou Y, Pang Z, Liu L, Shao F. </i> Nat Struct Mol Biol, 2008","date":"2025-06-18T08:58:31.409Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue","statements":[{"type":"Methods","text":"The final crystallization condition of SeMet-labeled IpaH3 was 2 M NaCl, 0.1 M Bis-Tris, pH 5.5, 0.025 g ml−1 poly(acrylic acid sodium salt) 5100 and 0.1 M sodium nitrate."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":4,"end":4,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":134,"end":134,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":154,"end":154,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":268,"end":268,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":344,"end":344,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":402,"end":402,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":434,"end":434,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":448,"end":448,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":467,"end":467,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":500,"end":500,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":508,"end":508,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":514,"end":514,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":541,"end":541,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":552,"end":552,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":562,"end":562,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"3CVR"}],"region_id":"DP04392r001","statement":[{"text":"The final model contains residues 25–561 and misses the N-terminal 24 residues, the C-terminal 10 residues and some residues in the disordered linking loops (broken lines in Fig. 2a) owing to the lack of electron density.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:37:59.816Z"}},{"start":562,"end":571,"reference_id":"18997779","reference_source":"pmid","reference_html":"Structure of a Shigella effector reveals a new class of ubiquitin ligases. <i> Zhu Y, Li H, Hu L, Wang J, Zhou Y, Pang Z, Liu L, Shao F. </i> Nat Struct Mol Biol, 2008","date":"2025-06-18T08:55:48.309Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue","statements":[{"type":"Methods","text":"The final crystallization condition of SeMet-labeled IpaH3 was 2 M NaCl, 0.1 M Bis-Tris, pH 5.5, 0.025 g ml−1 poly(acrylic acid sodium salt) 5100 and 0.1 M sodium nitrate."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":4,"end":4,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":134,"end":134,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":154,"end":154,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":268,"end":268,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":344,"end":344,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":402,"end":402,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":434,"end":434,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":448,"end":448,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":467,"end":467,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":500,"end":500,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":508,"end":508,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":514,"end":514,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":541,"end":541,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":552,"end":552,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":562,"end":562,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"3CVR"}],"region_id":"DP04392r002","statement":[{"text":"The final model contains residues 25–561 and misses the N-terminal 24 residues, the C-terminal 10 residues and some residues in the disordered linking loops (broken lines in Fig. 2a) owing to the lack of electron density.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:37:57.678Z"}},{"start":269,"end":278,"reference_id":"18997779","reference_source":"pmid","reference_html":"Structure of a Shigella effector reveals a new class of ubiquitin ligases. <i> Zhu Y, Li H, Hu L, Wang J, Zhou Y, Pang Z, Liu L, Shao F. </i> Nat Struct Mol Biol, 2008","date":"2025-06-18T08:44:30.299Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue","statements":[{"type":"Methods","text":"The final crystallization condition of SeMet-labeled IpaH3 was 2 M NaCl, 0.1 M Bis-Tris, pH 5.5, 0.025 g ml−1 poly(acrylic acid sodium salt) 5100 and 0.1 M sodium nitrate."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":4,"end":4,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":134,"end":134,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":154,"end":154,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":268,"end":268,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":344,"end":344,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":402,"end":402,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":434,"end":434,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":448,"end":448,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":467,"end":467,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":500,"end":500,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":508,"end":508,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":514,"end":514,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":541,"end":541,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":552,"end":552,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":562,"end":562,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"3CVR"}],"region_id":"DP04392r003","statement":[{"text":"The final model contains residues 25–561 and misses the N-terminal 24 residues, the C-terminal 10 residues and some residues in the disordered linking loops (broken lines in Fig. 2a) owing to the lack of electron density.","type":"Results"},{"text":"The two domains are linked by a long disordered loop (residues 269–278).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:37:42.722Z"}},{"start":269,"end":278,"reference_id":"18997779","reference_source":"pmid","reference_html":"Structure of a Shigella effector reveals a new class of ubiquitin ligases. <i> Zhu Y, Li H, Hu L, Wang J, Zhou Y, Pang Z, Liu L, Shao F. </i> Nat Struct Mol Biol, 2008","date":"2025-06-18T09:07:39.144Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue","statements":[{"type":"Methods","text":"The final crystallization condition of SeMet-labeled IpaH3 was 2 M NaCl, 0.1 M Bis-Tris, pH 5.5, 0.025 g ml−1 poly(acrylic acid sodium salt) 5100 and 0.1 M sodium nitrate."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":4,"end":4,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":134,"end":134,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":154,"end":154,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":268,"end":268,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":344,"end":344,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":402,"end":402,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":434,"end":434,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":448,"end":448,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":467,"end":467,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":500,"end":500,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":508,"end":508,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":514,"end":514,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":541,"end":541,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":552,"end":552,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":562,"end":562,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"3CVR"}],"region_id":"DP04392r004","statement":[{"text":"The final model contains residues 25–561 and misses the N-terminal 24 residues, the C-terminal 10 residues and some residues in the disordered linking loops (broken lines in Fig. 2a) owing to the lack of electron density.","type":"Results"},{"text":"The two domains are linked by a long disordered loop (residues 269–278).","type":"Results"},{"text":"In solution, the long flexible loop should allow for changes of distance and relative orientation between the catalytic domain and the putative substrate binding LRR domain (see below).","type":"Results"},{"text":"In IpaH3, the two domains are linked together by a long flexible loop. During elongation of polyubiquitin chains on the substrate, the distance between the last-added ubiquitin and the active site cysteine in E3 would increase and impede further ubiquitin transfer for a rigid structure. Thus, the linking loop probably provides an ideal structural flexibility that could help to shorten the distance between the catalytic cysteine in IpaH and ubiquitin at the end of the elongating chain, and therefore allows for ubiquitin transfer during chain elongation.","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:37:54.523Z"}},{"start":507,"end":540,"reference_id":"18997779","reference_source":"pmid","reference_html":"Structure of a Shigella effector reveals a new class of ubiquitin ligases. <i> Zhu Y, Li H, Hu L, Wang J, Zhou Y, Pang Z, Liu L, Shao F. </i> Nat Struct Mol Biol, 2008","date":"2025-06-18T08:48:17.451Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue","statements":[{"type":"Methods","text":"The final crystallization condition of SeMet-labeled IpaH3 was 2 M NaCl, 0.1 M Bis-Tris, pH 5.5, 0.025 g ml−1 poly(acrylic acid sodium salt) 5100 and 0.1 M sodium nitrate."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":4,"end":4,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":134,"end":134,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":154,"end":154,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":268,"end":268,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":344,"end":344,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":402,"end":402,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":434,"end":434,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":448,"end":448,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":467,"end":467,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":500,"end":500,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":508,"end":508,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":514,"end":514,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":541,"end":541,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":552,"end":552,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":562,"end":562,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"3CVR"}],"region_id":"DP04392r005","statement":[{"text":"The final model contains residues 25–561 and misses the N-terminal 24 residues, the C-terminal 10 residues and some residues in the disordered linking loops (broken lines in Fig. 2a) owing to the lack of electron density.","type":"Results"},{"text":"Notably, the C-terminal two helices, α14 and α15, connected by a long disordered loop of 35 residues, project outward from the core structure, which, together with parts of α8-α10, α12 and α13, generates a concave surface on the molecule.","type":"Results"},{"text":"Although the paper does not specify residue numbers, the disordered loop described as \"a long disordered loop of 35 residues\" connecting helices α14 and α15 can be mapped to residues 507–540 based on the analysis of the PDB structure.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:37:41.448Z"}},{"start":1,"end":24,"reference_id":"18997779","reference_source":"pmid","reference_html":"Structure of a Shigella effector reveals a new class of ubiquitin ligases. <i> Zhu Y, Li H, Hu L, Wang J, Zhou Y, Pang Z, Liu L, Shao F. </i> Nat Struct Mol Biol, 2008","date":"2025-06-18T09:05:24.398Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue","statements":[{"type":"Methods","text":"The final crystallization condition of SeMet-labeled IpaH3 was 2 M NaCl, 0.1 M Bis-Tris, pH 5.5, 0.025 g ml−1 poly(acrylic acid sodium salt) 5100 and 0.1 M sodium nitrate."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":4,"end":4,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":134,"end":134,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":154,"end":154,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":268,"end":268,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":344,"end":344,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":402,"end":402,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":434,"end":434,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":448,"end":448,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":467,"end":467,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":500,"end":500,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":508,"end":508,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":514,"end":514,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":541,"end":541,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":552,"end":552,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":562,"end":562,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"3CVR"}],"region_id":"DP04392r006","statement":[{"text":"The final model contains residues 25–561 and misses the N-terminal 24 residues, the C-terminal 10 residues and some residues in the disordered linking loops (broken lines in Fig. 2a) owing to the lack of electron density.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:38:02.476Z"}},{"start":562,"end":571,"reference_id":"18997779","reference_source":"pmid","reference_html":"Structure of a Shigella effector reveals a new class of ubiquitin ligases. <i> Zhu Y, Li H, Hu L, Wang J, Zhou Y, Pang Z, Liu L, Shao F. </i> Nat Struct Mol Biol, 2008","date":"2025-06-18T09:01:48.860Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue","statements":[{"type":"Methods","text":"The final crystallization condition of SeMet-labeled IpaH3 was 2 M NaCl, 0.1 M Bis-Tris, pH 5.5, 0.025 g ml−1 poly(acrylic acid sodium salt) 5100 and 0.1 M sodium nitrate."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":4,"end":4,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":134,"end":134,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":154,"end":154,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":268,"end":268,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":344,"end":344,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":402,"end":402,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":434,"end":434,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":448,"end":448,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":467,"end":467,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":500,"end":500,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":508,"end":508,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":514,"end":514,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":541,"end":541,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":552,"end":552,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":562,"end":562,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"3CVR"}],"region_id":"DP04392r007","statement":[{"text":"The final model contains residues 25–561 and misses the N-terminal 24 residues, the C-terminal 10 residues and some residues in the disordered linking loops (broken lines in Fig. 2a) owing to the lack of electron density.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:37:37.248Z"}}],"regions_counter":7,"released":"2025_06","sequence":"MSIMLPINNNFSLSQNSFYNTISGTYADYFSAWDKWEKQALPGENRNEAVSLLKECLINQFSELQLNRLNLSSLPDNLPPQITVLEITQNALISLPELPASLEYLDACDNRLSTLPELPASLKHLDVDNNQLTMLPELPALLEYINADNNQLTMLPELPTSLEVLSVRNNQLTFLPELPESLEALDVSTNLLESLPAVPVRNHHSEETEIFFRCRENRITHIPENILSLDPTCTIILEDNPLSSRIRESLSQQTAQPDYHGPRIYFSMSDGQQNTLHRPLADAVTAWFPENKQSDVSQIWHAFEHEEHANTFSAFLDRLSDTVSARNTSGFREQVAAWLEKLSTSAELRQQSFAVAADATESCEDRVALTWNNLRKTLLVHQASEGLFDNDTGALLSLGREMFRLEILEDIARDKVRTLHFVDEIEVYLAFQTMLAEKLQLSTAVKEMRFYGVSGVTANDLRTAEAMVRSREENEFTDWFSLWGPWHAVLKRTEADRWAQAEEQKYEMLENEYSQRVADRLKASGLSGDADAEREAGAQVMRETEQQIYRQVTDEVLALRLSENGSQLHHS","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Shigella"],"alphafold_very_low_content":0.06830122591943957,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.13660245183887915,"disprot_consensus":{"full":[{"start":1,"end":24,"type":"D"},{"start":269,"end":278,"type":"D"},{"start":507,"end":540,"type":"D"},{"start":562,"end":571,"type":"D"}],"Structural state":[{"start":1,"end":24,"type":"D"},{"start":269,"end":278,"type":"D"},{"start":507,"end":540,"type":"D"},{"start":562,"end":571,"type":"D"}],"Disorder function":[{"start":1,"end":24,"type":"F"},{"start":269,"end":278,"type":"F"},{"start":562,"end":571,"type":"F"}]}},{"disprot_id":"DP04393","acc":"P31489","creator":"xcastro","date":"2025-05-02T07:20:23.032Z","features":{"pfam":[{"id":"PF03895","name":"YadA-like membrane anchor domain","start":396,"end":455},{"id":"PF05658","name":"YadA head domain repeat (2 copies)","start":67,"end":93},{"id":"PF05658","name":"YadA head domain repeat (2 copies)","start":95,"end":115},{"id":"PF05658","name":"YadA head domain repeat (2 copies)","start":138,"end":161},{"id":"PF05658","name":"YadA head domain repeat (2 copies)","start":169,"end":191},{"id":"PF05662","name":"Coiled stalk of trimeric autotransporter adhesin","start":195,"end":228}],"gene3D":[]},"genes":[{"name":{"value":"yadA"},"synonyms":[{"value":"invA"},{"value":"yop1"},{"value":"yopA"}]}],"length":455,"name":"Adhesin YadA","ncbi_taxon_id":630,"organism":"Yersinia enterocolitica","regions":[{"start":52,"end":61,"reference_id":"14765110","reference_source":"pmid","reference_html":"The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel beta-roll. <i> Nummelin H, Merckel MC, Leo JC, Lankinen H, Skurnik M, Goldman A. </i> EMBO J, 2004","date":"2025-05-07T09:22:20.508Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":6.7,"statements":[{"type":"Methods","text":"The Se‐Met‐YadA26–241‐2M crystallised both in sitting and in hanging drops from 11% polyethylene glycol 8000, 0.2 M sodium acetate, 0.1 M Tris–HCl (pH 6.7)."}]}],"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":null,"end":null,"position":"unspecified","statements":[{"type":"Results","text":"The structure of YadA26–241 was solved utilising seleno‐methionyl labelled double mutant Yad26–241‐2M (I130M, I157M) and multiple anomalous dispersion (MAD)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile130Met","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"The structure of YadA26–241 was solved utilising seleno‐methionyl labelled double mutant Yad26–241‐2M (I130M, I157M) and multiple anomalous dispersion (MAD)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile157Met","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"The structure of YadA26–241 was solved utilising seleno‐methionyl labelled double mutant Yad26–241‐2M (I130M, I157M) and multiple anomalous dispersion (MAD)."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Briefly, the recombinant collagen‐binding fragment of YadA, YadA26–241, was expressed in E. coli and purified utilising metal affinity and size exclusion chromatography."}]}],"cross_refs":[{"db":"PDB","id":"1P9H"}],"region_id":"DP04393r001","sequence_construct":"MRGSHHHHHHDDYDGIPNLTAVQISPNADPALGLEYPVRPPVPGAGGLNASAKGIHSIAIGATAEAAKGAAVAVGAGSIATGVNSVAIGPLSKALGDSAVTYGAASTAQKDGVAIGARASTSDTGVAVGFNSKADAKNSVAIGHSSHVAANHGYSIAIGDRSKTDRENSVSIGHESLNRQLTHLAAGTKDTDAVNVAQLKKEIEKTQENTNKRSAELLANANAYAD","statement":[{"text":"The electron density quality was good throughout the structure (Figure 1), but 37 residues were disordered in the final model (see below).","type":"Results"},{"text":"Amino (N)‐terminal residues 26–31 and loop 52–61 are missing in the final model, as well as the start of the stalk domain (221–241). The head region is composed almost solely of β‐sheets making a novel nine coiled left‐handed parallel β‐roll (LPBR), surrounded by a partly disordered (N)‐terminal random coil and a C‐terminal neck region, which consists of a random coil and a short helix at the start of the stalk domain.","type":"Results"},{"text":"The rest of the proline‐rich loop (52‐PVRPPVPGAG‐61) is disordered, but one possibility is that the chain reverses direction at Y51, forming another IS and then loops around clockwise to connect to G62 (see Supplementary data, Figure 2).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-12T18:02:03.965Z"}},{"start":221,"end":241,"reference_id":"14765110","reference_source":"pmid","reference_html":"The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel beta-roll. <i> Nummelin H, Merckel MC, Leo JC, Lankinen H, Skurnik M, Goldman A. </i> EMBO J, 2004","date":"2025-05-07T09:21:54.243Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":null,"value":6.7,"statements":[{"type":"Methods","text":"The Se‐Met‐YadA26–241‐2M crystallised both in sitting and in hanging drops from 11% polyethylene glycol 8000, 0.2 M sodium acetate, 0.1 M Tris–HCl (pH 6.7)."}]}],"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":null,"end":null,"position":"unspecified","statements":[{"type":"Results","text":"The structure of YadA26–241 was solved utilising seleno‐methionyl labelled double mutant Yad26–241‐2M (I130M, I157M) and multiple anomalous dispersion (MAD)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile130Met","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"The structure of YadA26–241 was solved utilising seleno‐methionyl labelled double mutant Yad26–241‐2M (I130M, I157M) and multiple anomalous dispersion (MAD)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile157Met","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"The structure of YadA26–241 was solved utilising seleno‐methionyl labelled double mutant Yad26–241‐2M (I130M, I157M) and multiple anomalous dispersion (MAD)."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Briefly, the recombinant collagen‐binding fragment of YadA, YadA26–241, was expressed in E. coli and purified utilising metal affinity and size exclusion chromatography."}]}],"cross_refs":[{"db":"PDB","id":"1P9H"}],"region_id":"DP04393r002","sequence_construct":"MRGSHHHHHHDDYDGIPNLTAVQISPNADPALGLEYPVRPPVPGAGGLNASAKGIHSIAIGATAEAAKGAAVAVGAGSIATGVNSVAIGPLSKALGDSAVTYGAASTAQKDGVAIGARASTSDTGVAVGFNSKADAKNSVAIGHSSHVAANHGYSIAIGDRSKTDRENSVSIGHESLNRQLTHLAAGTKDTDAVNVAQLKKEIEKTQENTNKRSAELLANANAYAD","statement":[{"text":"The electron density quality was good throughout the structure (Figure 1), but 37 residues were disordered in the final model (see below).","type":"Results"},{"text":"Amino (N)‐terminal residues 26–31 and loop 52–61 are missing in the final model, as well as the start of the stalk domain (221–241). The head region is composed almost solely of β‐sheets making a novel nine coiled left‐handed parallel β‐roll (LPBR), surrounded by a partly disordered (N)‐terminal random coil and a C‐terminal neck region, which consists of a random coil and a short helix at the start of the stalk domain.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-12T18:02:01.518Z"}}],"regions_counter":2,"released":"2025_06","sequence":"MTKDFKISVSAALISALFSSPYAFADDYDGIPNLTAVQISPNADPALGLEYPVRPPVPGAGGLNASAKGIHSIAIGATAEAAKGAAVAVGAGSIATGVNSVAIGPLSKALGDSAVTYGAASTAQKDGVAIGARASTSDTGVAVGFNSKADAKNSVAIGHSSHVAANHGYSIAIGDRSKTDRENSVSIGHESLNRQLTHLAAGTKDTDAVNVAQLKKEIEKTQENTNKRSAELLANANAYADNKSSSVLGIANNYTDSKSAETLENARKEAFAQSKDVLNMAKAHSNSVARTTLETAEEHANSVARTTLETAEEHANKKSAEALASANVYADSKSSHTLKTANSYTDVTVSNSTKKAIRESNQYTDHKFRQLDNRLDKLDTRVDKGLASSAALNSLFQPYGVGKVNFTAGVGGYRSSQALAIGSGYRVNENVALKAGVAYAGSSDVMYNASFNIEW","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"],"alphafold_very_low_content":0.11868131868131868,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.06813186813186813,"disprot_consensus":{"full":[{"start":52,"end":61,"type":"D"},{"start":221,"end":241,"type":"D"}],"Structural state":[{"start":52,"end":61,"type":"D"},{"start":221,"end":241,"type":"D"}]}},{"disprot_id":"DP04394","acc":"P0C7U7","creator":"xcastro","date":"2025-05-02T07:51:28.557Z","features":{"pfam":[{"id":"PF04792","name":"V antigen (LcrV) protein","start":1,"end":323}],"gene3D":[]},"genes":[{"name":{"value":"lcrV"},"synonyms":[{"value":"icrV"}],"olnNames":[{"value":"YPCD1.31c"},{"value":"y5047"},{"value":"y0050"},{"value":"YP_pCD52"}]}],"length":326,"name":"Virulence-associated V antigen","ncbi_taxon_id":632,"organism":"Yersinia pestis","regions":[{"start":261,"end":279,"reference_id":"23695558","reference_source":"pmid","reference_html":"Structure of the Yersinia pestis tip protein LcrV refined to 1.65 Å resolution. <i> Chaudhury S, Battaile KP, Lovell S, Plano GV, De Guzman RN. </i> Acta Crystallogr Sect F Struct Biol Cryst Commun, 2013","date":"2025-06-18T09:15:06.338Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys273Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The DNA region coding for Y. pestis LcrV residues Gly28–Asp322 with a C273S point mutation was subcloned as a fusion protein with a His6-tagged streptococcal GB1 domain and a tobacco etch virus (TEV) protease site."}]}],"cross_refs":[{"db":"PDB","id":"4JBU"}],"region_id":"DP04394r001","sequence_construct":"GHMGSSVLEELVQLVKDKNIDISIKYDPRKDSEVFANRVITDDIELLKKILAYFLPEDAILKGGHYDNQLQNGIKRVKEFLESSPNTQWELRAFMAVMHFSLTADRIDDDILKVIVDSMNHHGDARSKLREELAELTAELKIYSVIQAEINKHLSSSGTINIHDKSINLMDKNLYGYTDEEIFKASAEYKILEKMPQTTIQVDGSEKKIVSIKDFLGSENKRTGALGNLKNSYSYNKDNNELSHFATTSSDKSRPLNDLVSQKTTQLSDITSRFNSAIEALNRFIQKYDSVMQRLLDD","statement":[{"text":"Residues Lys261–Pro279 could not be fitted to the electron density owing to disorder.","type":"Results"},{"text":"Similarly, in our model the residues Lys261–Pro279 could not be modeled owing to disorder.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:38:54.625Z"}},{"start":49,"end":63,"reference_id":"14962390","reference_source":"pmid","reference_html":"The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague. <i> Derewenda U, Mateja A, Devedjiev Y, Routzahn KM, Evdokimov AG, Derewenda ZS, Waugh DS. </i> Structure, 2004","date":"2025-06-18T09:14:31.378Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":null,"end":null,"position":"unspecified","statements":[{"type":"Results","text":"The structure of LcrV was solved by the multiple anomalous diffraction (MAD) technique, using scattering from six selenium atoms incorporated as selenomethionine (SeMet)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys40Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"A triple mutant (K40A/D41A/K42A) of LcrV yielded crystals that diffracted X-rays to 2.2 A˚ resolution."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp41Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"A triple mutant (K40A/D41A/K42A) of LcrV yielded crystals that diffracted X-rays to 2.2 A˚ resolution."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys42Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"A triple mutant (K40A/D41A/K42A) of LcrV yielded crystals that diffracted X-rays to 2.2 A˚ resolution."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys273Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"At the same time, the single cysteine in LcrV (Cys273) was replaced with a serine residue to prevent covalent dimerization of the protein which proved to be troublesome during purification."}]}],"cross_refs":[{"db":"PDB","id":"1R6F"}],"region_id":"DP04394r003","sequence_construct":"GLTGHGSSVLEELVQLVAAANIDISIKYDPRKDSEVFANRVITDDIELLKKILAYFLPEDAILKGGHYDNQLQNGIKRVKEFLESSPNTQWELRAFMAVMHFSLTADRIDDDILKVIVDSMNHHGDARSKLREELAELTAELKIYSVIQAEINKHLSSSGTINIHDKSINLMDKNLYGYTDEEIFKASAEYKILEKMPQTTIQVDGSEKKIVSIKDFLGSENKRTGALGNLKNSYSYNKDNNELSHFATTCSDKSRPLNDLVSQKTTQLSDITSRFNSAIEALNRFIQKYDSVMQRLLDDTSGKHHHHHH","statement":[{"text":"The N- and C termini of the protein (residues 23–27 and 323–326) are not visible in the electron density maps, nor is Tyr90 or the residues in two internal loops (49–63 and 260–275). The inherent flexibility of these regions may have impeded efforts to crystallize the wild-type protein.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:38:47.941Z"}},{"start":260,"end":275,"reference_id":"14962390","reference_source":"pmid","reference_html":"The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague. <i> Derewenda U, Mateja A, Devedjiev Y, Routzahn KM, Evdokimov AG, Derewenda ZS, Waugh DS. </i> Structure, 2004","date":"2025-06-18T09:14:43.726Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":null,"end":null,"position":"unspecified","statements":[{"type":"Results","text":"The structure of LcrV was solved by the multiple anomalous diffraction (MAD) technique, using scattering from six selenium atoms incorporated as selenomethionine (SeMet)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys40Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"A triple mutant (K40A/D41A/K42A) of LcrV yielded crystals that diffracted X-rays to 2.2 A˚ resolution."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp41Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"A triple mutant (K40A/D41A/K42A) of LcrV yielded crystals that diffracted X-rays to 2.2 A˚ resolution."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys42Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"A triple mutant (K40A/D41A/K42A) of LcrV yielded crystals that diffracted X-rays to 2.2 A˚ resolution."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys273Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"At the same time, the single cysteine in LcrV (Cys273) was replaced with a serine residue to prevent covalent dimerization of the protein which proved to be troublesome during purification."}]}],"cross_refs":[{"db":"PDB","id":"1R6F"}],"region_id":"DP04394r004","sequence_construct":"GLTGHGSSVLEELVQLVAAANIDISIKYDPRKDSEVFANRVITDDIELLKKILAYFLPEDAILKGGHYDNQLQNGIKRVKEFLESSPNTQWELRAFMAVMHFSLTADRIDDDILKVIVDSMNHHGDARSKLREELAELTAELKIYSVIQAEINKHLSSSGTINIHDKSINLMDKNLYGYTDEEIFKASAEYKILEKMPQTTIQVDGSEKKIVSIKDFLGSENKRTGALGNLKNSYSYNKDNNELSHFATTCSDKSRPLNDLVSQKTTQLSDITSRFNSAIEALNRFIQKYDSVMQRLLDDTSGKHHHHHH","statement":[{"text":"The N- and C termini of the protein (residues 23–27 and 323–326) are not visible in the electron density maps, nor is Tyr90 or the residues in two internal loops (49–63 and 260–275). The inherent flexibility of these regions may have impeded efforts to crystallize the wild-type protein.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:38:46.580Z"}}],"regions_counter":4,"released":"2025_06","sequence":"MIRAYEQNPQHFIEDLEKVRVEQLTGHGSSVLEELVQLVKDKNIDISIKYDPRKDSEVFANRVITDDIELLKKILAYFLPEDAILKGGHYDNQLQNGIKRVKEFLESSPNTQWELRAFMAVMHFSLTADRIDDDILKVIVDSMNHHGDARSKLREELAELTAELKIYSVIQAEINKHLSSSGTINIHDKSINLMDKNLYGYTDEEIFKASAEYKILEKMPQTTIQVDGSEKKIVSIKDFLGSENKRTGALGNLKNSYSYNKDNNELSHFATTCSDKSRPLNDLVSQKTTQLSDITSRFNSAIEALNRFIQKYDSVMQRLLDDTSGK","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"],"alphafold_very_low_content":0.018404907975460124,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.10736196319018405,"disprot_consensus":{"full":[{"start":49,"end":63,"type":"D"},{"start":260,"end":279,"type":"D"}],"Structural state":[{"start":49,"end":63,"type":"D"},{"start":260,"end":279,"type":"D"}]}},{"disprot_id":"DP04395","acc":"P9WNI7","creator":"xcastro","date":"2025-05-02T13:17:45.647Z","features":{"pfam":[{"id":"PF06013","name":"Proteins of 100 residues with WXG","start":3,"end":87}],"gene3D":[]},"genes":[{"name":{"value":"esxO","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"19876390","url":"http://www.ncbi.nlm.nih.gov/pubmed/19876390","alternativeUrl":"https://europepmc.org/abstract/MED/19876390"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"24312350","url":"http://www.ncbi.nlm.nih.gov/pubmed/24312350","alternativeUrl":"https://europepmc.org/abstract/MED/24312350"}}]},"orfNames":[{"value":"MTCY98.15c"}],"olnNames":[{"value":"Rv2346c"}]}],"length":94,"name":"ESAT-6-like protein EsxO","ncbi_taxon_id":83332,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","regions":[{"start":1,"end":12,"reference_id":"24312350","reference_source":"pmid","reference_html":"Heterologous expression of mycobacterial Esx complexes in Escherichia coli for structural studies is facilitated by the use of maltose binding protein fusions. <i> Arbing MA, Chan S, Harris L, Kuo E, Zhou TT, Ahn CJ, Nguyen L, He Q, Lu J, Menchavez PT, Shin A, Holton T, Sawaya MR, Cascio D, Eisenberg D. </i> PLoS One, 2013","date":"2025-06-18T09:19:15.035Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue","statements":[{"type":"Methods","text":"Selenomethionine(SeMet)-labeled EsxEFma, EsxGHms, and EsxOPmt complexes were expressed as previously described [26] in E. coli BL21 (DE3) with the following modifications: the EsxEFma and EsxGHms cultures were grown for 18 hours at 18°C after induction of protein expression with 0.5 mM IPTG while the EsxOPmt culture was grown under the same conditions but protein expression was induced with 1.0 mM IPTG."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"The pET28b (EMD Millipore, Billerica, MA) vector was used as the basis for the construction of expression vectors: pMA507, which contains an N-terminal hexahistidine tag (His6) followed by a tobacco etch virus (TEV) protease cleavage site; pMA510, which has an N-terminal MBP fusion followed by a His6 tag and TEV protease site; pMAPLe3, which allows intracellular processing of an N-terminal MBP fusion by TEV protease to yield a target protein with a C-terminal His6 tag; and pMAPLe4, which allows intracellular processing of an N-terminal MBP fusion by tobacco vein mottling virus (TVMV) protease to yield a target protein with a TEV protease cleavable N-terminal His6 tag."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":16,"end":16,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":82,"end":82,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"3OGI"}],"region_id":"DP04395r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P9WNI5","statements":[{"type":"Methods","text":"Crystals of EsxOPmt in crystal form I were grown by mixing protein stock solution 2∶1 with reservoir solution (9% isopropanol, 90 mM sodium acetate trihydrate pH 4.6, 200 mM CaCl2)."},{"type":"Introduction","text":"Using this expression approach we expressed and purified six Esx complexes and determined the crystal structures of M. abscessus EsxEF (EsxEFma), encoded by the MAB_3112 and MAB_3113 genes, M. smegmatis EsxGH (EsxGHms), encoded by the MSMEG_0620 and MSMEG_0621 genes, and M. tuberculosis EsxOP (EsxOPmt), encoded by the Rv2346c and Rv2347c genes, at resolutions of 1.96 Å, 2.70 Å, and 2.55 Å, respectively."}]}],"sequence_construct":"MTINYQFGDVDAHGAMIRAQAGLLEAEHQAIVRDVLAAGDFWGGAGSVACQEFITQLGRNFQVIYEQANAHGQKVQAAGNNMAQTDSAVGSSWATHHHHHH","statement":[{"text":"Additional regions of disorder are found at the N- and C-termini of the complexes with the EsxFma and EsxOmt subunits having a substantial number of disordered residues at their C-termini.","type":"Results"},{"text":"Although the original publication does not explicitly define the boundaries of the disordered regions, manual inspection of the structure indicates that the N-terminal residues 1–12 are not resolved in the electron density map, suggesting intrinsic disorder in this segment. The structured regions observed in the model correspond to residues A13–A39, A49–A69, and C13–C68, as listed in Table 2. Based on this analysis, the disordered region was annotated accordingly.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:39:12.197Z"}},{"start":70,"end":94,"reference_id":"24312350","reference_source":"pmid","reference_html":"Heterologous expression of mycobacterial Esx complexes in Escherichia coli for structural studies is facilitated by the use of maltose binding protein fusions. <i> Arbing MA, Chan S, Harris L, Kuo E, Zhou TT, Ahn CJ, Nguyen L, He Q, Lu J, Menchavez PT, Shin A, Holton T, Sawaya MR, Cascio D, Eisenberg D. </i> PLoS One, 2013","date":"2025-06-18T09:18:40.818Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue","statements":[{"type":"Methods","text":"Selenomethionine(SeMet)-labeled EsxEFma, EsxGHms, and EsxOPmt complexes were expressed as previously described [26] in E. coli BL21 (DE3) with the following modifications: the EsxEFma and EsxGHms cultures were grown for 18 hours at 18°C after induction of protein expression with 0.5 mM IPTG while the EsxOPmt culture was grown under the same conditions but protein expression was induced with 1.0 mM IPTG."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"The pET28b (EMD Millipore, Billerica, MA) vector was used as the basis for the construction of expression vectors: pMA507, which contains an N-terminal hexahistidine tag (His6) followed by a tobacco etch virus (TEV) protease cleavage site; pMA510, which has an N-terminal MBP fusion followed by a His6 tag and TEV protease site; pMAPLe3, which allows intracellular processing of an N-terminal MBP fusion by TEV protease to yield a target protein with a C-terminal His6 tag; and pMAPLe4, which allows intracellular processing of an N-terminal MBP fusion by tobacco vein mottling virus (TVMV) protease to yield a target protein with a TEV protease cleavable N-terminal His6 tag."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":16,"end":16,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":82,"end":82,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"3OGI"},{"db":"PDB","id":"4GZR"}],"region_id":"DP04395r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P9WNI5","statements":[{"type":"Methods","text":"Crystals of EsxOPmt in crystal form I were grown by mixing protein stock solution 2∶1 with reservoir solution (9% isopropanol, 90 mM sodium acetate trihydrate pH 4.6, 200 mM CaCl2)."},{"type":"Introduction","text":"Using this expression approach we expressed and purified six Esx complexes and determined the crystal structures of M. abscessus EsxEF (EsxEFma), encoded by the MAB_3112 and MAB_3113 genes, M. smegmatis EsxGH (EsxGHms), encoded by the MSMEG_0620 and MSMEG_0621 genes, and M. tuberculosis EsxOP (EsxOPmt), encoded by the Rv2346c and Rv2347c genes, at resolutions of 1.96 Å, 2.70 Å, and 2.55 Å, respectively."}]}],"sequence_construct":"MTINYQFGDVDAHGAMIRAQAGLLEAEHQAIVRDVLAAGDFWGGAGSVACQEFITQLGRNFQVIYEQANAHGQKVQAAGNNMAQTDSAVGSSWATHHHHHH","statement":[{"text":"Additional regions of disorder are found at the N- and C-termini of the complexes with the EsxFma and EsxOmt subunits having a substantial number of disordered residues at their C-termini.","type":"Results"},{"text":"Although the original publication does not explicitly define the boundaries of the disordered regions, manual inspection of the structure indicates that the C-terminal residues 70–94 are not resolved in the electron density map, suggesting intrinsic disorder in this segment. The structured regions observed in the model correspond to residues A13–A39, A49–A69, and C13–C68 in the case of 3OGI, and residues A12–A69; C9-C69 in 4GZR, as listed in Table 2. Based on this analysis, the disordered region was annotated accordingly.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:39:22.825Z"}}],"regions_counter":3,"released":"2025_06","sequence":"MTINYQFGDVDAHGAMIRAQAGLLEAEHQAIVRDVLAAGDFWGGAGSVACQEFITQLGRNFQVIYEQANAHGQKVQAAGNNMAQTDSAVGSSWA","taxonomy":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"alphafold_very_low_content":0,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.39361702127659576,"disprot_consensus":{"full":[{"start":1,"end":12,"type":"D"},{"start":70,"end":94,"type":"D"}],"Structural state":[{"start":1,"end":12,"type":"D"},{"start":70,"end":94,"type":"D"}]}},{"disprot_id":"DP04396","acc":"P9WGU1","creator":"xcastro","date":"2025-05-05T10:38:41.585Z","features":{"pfam":[{"id":"PF12849","name":"PBP superfamily domain","start":45,"end":342}],"gene3D":[]},"genes":[{"name":{"value":"pstS1"},"synonyms":[{"value":"phoS1"}],"orfNames":[{"value":"MTCY08D9.05c"}],"olnNames":[{"value":"Rv0934"}]}],"length":374,"name":"Phosphate-binding protein PstS 1","ncbi_taxon_id":83332,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","regions":[{"start":25,"end":41,"reference_id":"12842040","reference_source":"pmid","reference_html":"Crystal structure of M tuberculosis ABC phosphate transport receptor: specificity and charge compensation dominated by ion-dipole interactions. <i> Vyas NK, Vyas MN, Quiocho FA. </i> Structure, 2003","date":"2025-05-05T13:59:59.696Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"1PC3"}],"region_id":"DP04396r001","statement":[{"text":"N-terminal residues 2–18 are disordered, as electron densities for these residues were essentially absent in all three structures, consistent with high flexibility.","type":"Results"},{"text":"The recombinant PstS-1 lacks the first residue (Cys), and residues 2–18 (Figure 2) in the three independent structures show no interpretable densities.","type":"Figure"},{"text":"As indicated in Figure 1, residues 2–18 (GSKPPSGSPETGAGAGT) of the PstS-1 crystal structure are disordered.","type":"Figure"},{"text":"This tether is apparently highly flexible, since no interpretable electron density was observed for residues 2–18 in all three independent structures of PstS-1 in the asymmetric unit. (The recombinant PstS-1 lacks the Cys1 residue [see Experimental Procedures].)","type":"Results"},{"text":"The N-terminal segment that tethers PstS-1 on the cell surface is highly flexible.","type":"Conclusion"},{"text":"The disordered region from residues 2 to 18 mentioned in the paper corresponds to residues 25 to 41 of the UniProt sequence.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T20:19:49.074Z"}},{"start":25,"end":41,"reference_id":"12842040","reference_source":"pmid","reference_html":"Crystal structure of M tuberculosis ABC phosphate transport receptor: specificity and charge compensation dominated by ion-dipole interactions. <i> Vyas NK, Vyas MN, Quiocho FA. </i> Structure, 2003","date":"2025-06-16T20:19:37.095Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":1,"region_id":"DP04396r002","statement":[{"text":" As indicated in Figure 1, residues 2–18 (GSKPPSGSPETGAGAGT) of the PstS-1 crystal structure are disordered. The first 26 residues of the mature PstS-1 do not exist in PBP (Andersen, 1994; Chang et al., 1994; Lefevre et al., 1997).","type":"Figure"},{"text":"After processing, this region acts as the N-terminal tail of the mature protein.  ","type":"Curator statement"}]}],"regions_counter":2,"released":"2025_06","sequence":"MKIRLHTLLAVLTAAPLLLAAAGCGSKPPSGSPETGAGAGTVATTPASSPVTLAETGSTLLYPLFNLWGPAFHERYPNVTITAQGTGSGAGIAQAAAGTVNIGASDAYLSEGDMAAHKGLMNIALAISAQQVNYNLPGVSEHLKLNGKVLAAMYQGTIKTWDDPQIAALNPGVNLPGTAVVPLHRSDGSGDTFLFTQYLSKQDPEGWGKSPGFGTTVDFPAVPGALGENGNGGMVTGCAETPGCVAYIGISFLDQASQRGLGEAQLGNSSGNFLLPDAQSIQAAAAGFASKTPANQAISMIDGPAPDGYPIINYEYAIVNNRQKDAATAQTLQAFLHWAITDGNKASFLDQVHFQPLPPAVVKLSDALIATISS","taxonomy":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"alphafold_very_low_content":0.0748663101604278,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.045454545454545456,"disprot_consensus":{"full":[{"start":25,"end":41,"type":"D"}],"Structural state":[{"start":25,"end":41,"type":"D"}],"Disorder function":[{"start":25,"end":41,"type":"F"}]}},{"disprot_id":"DP04397","acc":"Q5ZTK6","creator":"xcastro","date":"2025-05-05T14:47:13.402Z","features":{"pfam":[{"id":"PF26375","name":"SidJ calmodulin-dependent glutamylase N-terminal domain","start":137,"end":318}],"gene3D":[]},"genes":[{"name":{"value":"sidJ","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"31330532","url":"http://www.ncbi.nlm.nih.gov/pubmed/31330532","alternativeUrl":"https://europepmc.org/abstract/MED/31330532"}}]},"olnNames":[{"value":"lpg2155"}]}],"length":873,"name":"Calmodulin-dependent glutamylase SidJ","ncbi_taxon_id":272624,"organism":"Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)","regions":[{"start":492,"end":501,"reference_id":"34702826","reference_source":"pmid","reference_html":"Structural basis for protein glutamylation by the Legionella pseudokinase SidJ. <i> Adams M, Sharma R, Colby T, Weis F, Matic I, Bhogaraju S. </i> Nat Commun, 2021","date":"2025-05-05T15:17:09.622Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7PQE"},{"db":"PDB","id":"7PPO"}],"region_id":"DP04397r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q5ZTK4","statements":[{"type":"Methods","text":"Equimolar quantities of SidJ E565A/CaM and SdeA were incubated on ice for 30 min in the presence of 150 mM NaCl, 50 mM HEPES, 10 mM MgCl2, and 10 mM ATP and loaded onto 5–20% glycerol gradients using 0–0.1% glutaraldehyde and 100 mM NaCl, 10 mM HEPES pH 7.5, 10 mM MgCl2, and the tubes were centrifuged at 164,000xg for 18 h at 4 °C."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0DP24","statements":[{"type":"Methods","text":"Equimolar quantities of SidJ E565A/CaM and SdeA were incubated on ice for 30 min in the presence of 150 mM NaCl, 50 mM HEPES, 10 mM MgCl2, and 10 mM ATP and loaded onto 5–20% glycerol gradients using 0–0.1% glutaraldehyde and 100 mM NaCl, 10 mM HEPES pH 7.5, 10 mM MgCl2, and the tubes were centrifuged at 164,000xg for 18 h at 4 °C. "}]}],"statement":[{"text":"Interestingly, post-glutamylation, the SidJ loop (residues 492–501) making up the migrated pocket becomes disordered in the structure, while the canonical pocket architecture remains intact (Fig. 4C, D).","type":"Results"},{"text":"Structural comparison between SidJ E565A (Yellow)/CaM + SdeA (Green) in its pre-glutamylation and post-catalytic states. Highlighted is a loop of SidJ (Red) located in the migrated pocket that undergoes structural change post-catalysis.","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T20:44:35.851Z"}},{"start":497,"end":501,"reference_id":"34702826","reference_source":"pmid","reference_html":"Structural basis for protein glutamylation by the Legionella pseudokinase SidJ. <i> Adams M, Sharma R, Colby T, Weis F, Matic I, Bhogaraju S. </i> Nat Commun, 2021","date":"2025-06-16T20:39:11.213Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0018117","term_name":"protein adenylylation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2025_06","version":1,"ec_go":"IMP","region_id":"DP04397r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q5ZTK4","statements":[{"type":"Methods","text":"Equimolar quantities of SidJ E565A/CaM and SdeA were incubated on ice for 30 min in the presence of 150 mM NaCl, 50 mM HEPES, 10 mM MgCl2, and 10 mM ATP and loaded onto 5–20% glycerol gradients using 0–0.1% glutaraldehyde and 100 mM NaCl, 10 mM HEPES pH 7.5, 10 mM MgCl2, and the tubes were centrifuged at 164,000xg for 18 h at 4 °C."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0DP24","statements":[{"type":"Methods","text":"Equimolar quantities of SidJ E565A/CaM and SdeA were incubated on ice for 30 min in the presence of 150 mM NaCl, 50 mM HEPES, 10 mM MgCl2, and 10 mM ATP and loaded onto 5–20% glycerol gradients using 0–0.1% glutaraldehyde and 100 mM NaCl, 10 mM HEPES pH 7.5, 10 mM MgCl2, and the tubes were centrifuged at 164,000xg for 18 h at 4 °C. "}]}],"statement":[{"text":"Since there is a cluster of glutamates (E497, E499, E501, and E565) concentrated in and around the bridging peptide of SidJ (Supplementary Fig. 9), we decided to mutagenize all these glutamates individually and combined. Mutating single glutamates in the bridging peptide did not result in the decrease of autoAMPylation, but mutating the cluster of glutamates resulted in a marked reduction in SidJ autoAMPylation (Fig. 5D).\"","type":"Discussion"}],"term_comment":"","term_def":"\"The addition of an adenylyl group (adenosine 5'-monophosphate; AMP) to a protein amino acid.\" [GOC:ai, GOC:jsg, GOC:sart, PMID:21607083]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu497Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu499Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu501Ala","start":null,"end":null,"position":null}]},{"start":492,"end":501,"reference_id":"34702826","reference_source":"pmid","reference_html":"Structural basis for protein glutamylation by the Legionella pseudokinase SidJ. <i> Adams M, Sharma R, Colby T, Weis F, Matic I, Bhogaraju S. </i> Nat Commun, 2021","date":"2025-05-19T09:13:44.862Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7PQE"}],"region_id":"DP04397r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q5ZTK4","statements":[{"type":"Methods","text":"Equimolar quantities of SidJ E565A/CaM and SdeA were incubated on ice for 30 min in the presence of 150 mM NaCl, 50 mM HEPES, 10 mM MgCl2, and 10 mM ATP and loaded onto 5–20% glycerol gradients using 0–0.1% glutaraldehyde and 100 mM NaCl, 10 mM HEPES pH 7.5, 10 mM MgCl2, and the tubes were centrifuged at 164,000xg for 18 h at 4 °C."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0DP24","statements":[{"type":"Methods","text":"Equimolar quantities of SidJ E565A/CaM and SdeA were incubated on ice for 30 min in the presence of 150 mM NaCl, 50 mM HEPES, 10 mM MgCl2, and 10 mM ATP and loaded onto 5–20% glycerol gradients using 0–0.1% glutaraldehyde and 100 mM NaCl, 10 mM HEPES pH 7.5, 10 mM MgCl2, and the tubes were centrifuged at 164,000xg for 18 h at 4 °C."}]}],"statement":[{"text":"Interestingly, post-glutamylation, the SidJ loop (residues 492–501) making up the migrated pocket becomes disordered in the structure, while the canonical pocket architecture remains intact (Fig. 4C, D).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T20:44:35.451Z"}}],"regions_counter":3,"released":"2025_06","sequence":"MFGFIKKVLDFFGVDQSEDNPSETAVETTDVSTKIKTTDTTQEESSVKTKTVVPTQPGGSVKPETIAPDQQKKHQIKTETTTSTTKQKGPKVTLMDGHVKQYYFARRGETSTHDTSLPPPVKVLSGRSIPLKEIPFEATRNELVQIYLTSIDKLIKSNKLNSIPSQQIASHYLFLRSLANSETDGIKKNQILSLAKPLGTYLASKEPHVWKMINELIEKSEYPIIHYLKNNRAHSNFMLALIHEYHKEPLTKNQSAFVQKFRDSSVFLFPNPIYTAWLAHSYDEDSSFNPMFRERLSTNFYHSTLTDNLLLRTEPKEVTLSSEHHYKKEKGPIDSSFRYQMSSDRLLRIQGRTLLFSTPQNDVVAVKVQKKGEPKSTLEEEFEMADYLLKHQRRLDVHSKLPQPLGQYSVKKSEILEISRGSLDFERFKTLIDDSKDLEVYVYKAPQSYFTYLHDKNQDLEDLTASVKTNVHDLFVLLREGIVFPQLADIFHTHFGEDEREDKGRYQALVQLLNVLQFQLGRIDKWQKAVEYVNLRSSGLADLGDSLPITSLFTSSDFTKHYFSELLTGGYHPTFFDKSSGTANSLFTGKRRLFGNYLYLNTIAEYLLVIQLTLGSYGDKVTRDMMDKPKKEAVWRELANVMFTSCAEAIHIMTGIPQSRALTLLKQRANIEKHFRQTQFWMTPDYSKLDEDTLQMEQYSIYSGEPEYEFTDKLVSGVGLSVDGVHQDLGGYNRESPLRELEKLLYATVTLIEGTMQLDKEFFKQLEQVEKILSGEIKTDANSCFEAVAQLLDLARPGCHFQKRLVLSYYEEAKLKYPSAPTDAYDSRFQVVARTNAAITIQRFWREARKNLSEKSDIDSEKPESERTTDKRL","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Legionellales","Legionellaceae","Legionella"],"alphafold_very_low_content":0.12256586483390607,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.011454753722794959,"disprot_consensus":{"full":[{"start":492,"end":501,"type":"T"}],"Structural state":[{"start":492,"end":501,"type":"D"}],"Structural transition":[{"start":492,"end":501,"type":"T"}],"Biological process":[{"start":497,"end":501,"type":"F"}]}},{"disprot_id":"DP04398","acc":"Q5ZTK4","creator":"xcastro","date":"2025-05-06T12:02:49.653Z","features":{"pfam":[{"id":"PF12252","name":"SidE phosphodiesterase (PDE) domain","start":255,"end":456},{"id":"PF19048","name":"SidE mono-ADP-ribosyltransferase domain","start":593,"end":931},{"id":"PF19049","name":"SidE DUB domain","start":1,"end":173}],"gene3D":[]},"genes":[{"name":{"value":"sdeA","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15773981","url":"http://www.ncbi.nlm.nih.gov/pubmed/15773981","alternativeUrl":"https://europepmc.org/abstract/MED/15773981"}}]},"olnNames":[{"value":"lpg2157","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"AAU28223.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAU28223.1"}}]}]}],"length":1499,"name":"Ubiquitinating/deubiquitinating enzyme SdeA","ncbi_taxon_id":272624,"organism":"Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)","regions":[{"start":590,"end":759,"reference_id":"34702826","reference_source":"pmid","reference_html":"Structural basis for protein glutamylation by the Legionella pseudokinase SidJ. <i> Adams M, Sharma R, Colby T, Weis F, Matic I, Bhogaraju S. </i> Nat Commun, 2021","date":"2025-06-18T09:22:07.950Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7PQE"}],"region_id":"DP04398r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q5ZTK6","statements":[{"type":"Methods","text":"Equimolar quantities of SidJ E565A/CaM and SdeA were incubated on ice for 30 min in the presence of 150 mM NaCl, 50 mM HEPES, 10 mM MgCl2, and 10 mM ATP and loaded onto 5–20% glycerol gradients using 0–0.1% glutaraldehyde and 100 mM NaCl, 10 mM HEPES pH 7.5, 10 mM MgCl2, and the tubes were centrifuged at 164,000xg for 18 h at 4 °C."},{"type":"Results","text":"We added l-glutamate to the prepared SidJ/CaM-SdeA pre-glutamylation complex right before applying the sample to the EM grid and analyzing it by single-particle cryo-EM (Supplementary Fig. 5 and Supplementary Table 1)."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0DP24"}],"statement":[{"text":"Interestingly, after 3D classification of the particles, we observed two well-resolved particle classes, Class I (15% of total particles) contained both SidJ/CaM and SdeA well resolved and Class II (17% of total particles) represented only SidJ/CaM with discernible density while SdeA was found to be disordered, presumably dissociated from SidJ but still tethered to it due to GraFix (Supplementary Fig. 5).","type":"Results"},{"text":"After manual inspection of the PDB structure, the disordered regions in SdeA mentioned by the authors in the post-catalytic state correspond to residues 590–759 and 903–1190.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:39:34.264Z"}},{"start":903,"end":1190,"reference_id":"34702826","reference_source":"pmid","reference_html":"Structural basis for protein glutamylation by the Legionella pseudokinase SidJ. <i> Adams M, Sharma R, Colby T, Weis F, Matic I, Bhogaraju S. </i> Nat Commun, 2021","date":"2025-06-18T09:21:45.165Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"7PQE"}],"region_id":"DP04398r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q5ZTK6","statements":[{"type":"Methods","text":"Equimolar quantities of SidJ E565A/CaM and SdeA were incubated on ice for 30 min in the presence of 150 mM NaCl, 50 mM HEPES, 10 mM MgCl2, and 10 mM ATP and loaded onto 5–20% glycerol gradients using 0–0.1% glutaraldehyde and 100 mM NaCl, 10 mM HEPES pH 7.5, 10 mM MgCl2, and the tubes were centrifuged at 164,000xg for 18 h at 4 °C."},{"type":"Results","text":"We added l-glutamate to the prepared SidJ/CaM-SdeA pre-glutamylation complex right before applying the sample to the EM grid and analyzing it by single-particle cryo-EM (Supplementary Fig. 5 and Supplementary Table 1)."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P0DP24"}],"statement":[{"text":"Interestingly, after 3D classification of the particles, we observed two well-resolved particle classes, Class I (15% of total particles) contained both SidJ/CaM and SdeA well resolved and Class II (17% of total particles) represented only SidJ/CaM with discernible density while SdeA was found to be disordered, presumably dissociated from SidJ but still tethered to it due to GraFix (Supplementary Fig. 5).","type":"Results"},{"text":"After manual inspection of the PDB structure, the disordered regions in SdeA mentioned by the authors in the post-catalytic state correspond to residues 590–759 and 903–1190.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-18T14:39:36.471Z"}}],"regions_counter":4,"released":"2025_06","sequence":"MPKYVEGVELTQEGMHAIFARMGYGDITSGSIYNGVPTIDTGALNRQGFMPVLTGVGPHRDSGHWIMLIKGPGNQYYLFDPLGKTSGEGYQNILAAQLPMGSTLSVIPNGSGLNMGLCGYWVASAGLRAHQALNQHNPPTLLNVGQTITNEMRNELDHDGYRKITGWLRAVADEFPEGDPQLDGKALRENTEKDLKIEIPTLVLPGKDTSPKEMSVKPTAPQDKSVPVWNGFSLYTDDTVKAAAQYAYDNYLGKPYTGSVESAPANFGGRMVYRQHHGLSHTLRTMAYAELIVEEARKAKLRGETLGKFKDGRTIADVTPQELKKIMIAQAFFVAGRDDEASDAKNYQKYHEQSRDAFLKYVKDNESTLIPDVFKDQEDVNFYARVIEDKSHDWESTPAHVLINQGHMVDLVRVKQPPESFLQRYFSSMQRWIGSQATEAVFGIQRQFFHATYEVVAGFDSDNKEPHLVVSGLGRYVIGEDGQPIREAPKKGQKEGDLKVFPQTYKLKENERLMRVDEFLKLPEIQNTFPGSGKHLQGGMPGMNEMDYWNRLNSLNRARCENDVDFCLKQLQTAHDKAKIEPIKQAFQSSKGKERRQPNVDEIAAARIIQQILANPDCIHDDHVLINGQKLEQQFFRDLLAKCEMAVVGSLLNDTDIGNIDTLMRHEKDTEFHSTNPEAVPVKIGEYWINDQRINNSSGNITQKKHDLIFLMQNDAWYFSRVNAIAQNRDKGSTFKEVLITTLMTPLTSKALVDTSQAKPPTRLFRGLNLSEEFTKGLIDQANAMIANTTERLFTDHSPEAFKQIKLNDLSKMSGRTNASTTTEIKLVKETWDSNVIFEMLDPDGLLHSKQVGRHGEGTESEFSVYLPEDVALVPVKVTLDGKTQKGENRYVFTFVAVKSPDFTPRHESGYAVEPFLRMQAAKLAEVKSSIEKAQRAPDLETIFNLQNEVEAVQYSHLSTGYKNFLKNTVGPVLENSLSGLMESDTDTLSKALAAFPSDTQWSAFNFEEARQAKRQMDAIKQMVGNKVVLDALTQCQDALEKQNIAGALDALKKIPSEKEMGTIRRELREQIQSARQELESLQRAVVTPVVTDEKKVRERYDALIENTSKKITELETGKLPNLDAVKKGISNLSNLKQEVTVLRNEKIRMHVGTDKVDFSDVEKLEQQIQVIDTKLADAYLLEVTKQISALDNTKPKNQTELKTKIAAFLDRTTDIEMLRNERIKKHGSSKDPLDLSDLDKLSGSLQRINQSLVSDLITTIRVSINQMEAKTFHEQEKEIQQNFELLAKLEKTLDKSKTSEKLREDIPKLNDLLVAKQKAYPQMVQMQLKSEVFVTQLREVCQANHDDLDKTRNARLRELDRLDREAGITRMVGNLIWGLTNKVGLTTDERLDIRTKQQSLARFKNELFNDKIDTDQLISNLARKRPSELQEGLGISTDNAMELHLLLTELAGKTTSPDELEERMKAIDDISTKIGREPEHLKFVMVEEDESNKKTIGF","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Legionellales","Legionellaceae","Legionella"],"alphafold_very_low_content":0.04336224149432955,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.3055370246831221,"disprot_consensus":{"full":[{"start":590,"end":759,"type":"D"},{"start":903,"end":1190,"type":"D"}],"Structural state":[{"start":590,"end":759,"type":"D"},{"start":903,"end":1190,"type":"D"}]}},{"disprot_id":"DP04399","acc":"P08062","creator":"xcastro","date":"2025-05-07T08:51:30.671Z","features":{"pfam":[{"id":"PF07229","name":"VirE2","start":2,"end":556}],"gene3D":[]},"genes":[{"name":{"value":"virE2"},"orfNames":[{"value":"AGR_pTi_28"}],"olnNames":[{"value":"Atu6190"}]}],"length":556,"name":"Single-strand DNA-binding protein","ncbi_taxon_id":176299,"organism":"Agrobacterium fabrum (strain C58 / ATCC 33970)","regions":[{"start":518,"end":556,"reference_id":"18678909","reference_source":"pmid","reference_html":"Crystal structure of the Agrobacterium virulence complex VirE1-VirE2 reveals a flexible protein that can accommodate different partners. <i> Dym O, Albeck S, Unger T, Jacobovitch J, Branzburg A, Michael Y, Frenkiel-Krispin D, Wolf SG, Elbaum M. </i> Proc Natl Acad Sci U S A, 2008","date":"2025-05-07T09:16:24.529Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"Selenomethionine VirE1 and VirE2 crystals were grown from a precipitating solution of 100 mM Hepes (pH = 7), 20% PEG 6000, 0.2M NH4Cl, and 1% Triton X-405."}]}],"cross_refs":[{"db":"PDB","id":"3BTP"}],"region_id":"DP04399r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08063","statements":[{"type":"Results","text":"Full-length nopaline VirE2 (P08062) (residues 1–556) was coexpressed with its small chaperone VirE1 (P08063) (residues 1–63), producing crystals that contained a single heterodimeric VirE1–VirE2 complex at a 1:1 ratio in the asymmetric unit cell."}]}],"sequence_construct":"MDPKAEGNGENITETAAGNVETSDFVNLKRQKREGVNSTGMSEIDMTGSQETPEHNMHGSPTHTDDLGPRLDADMLDSQSSHVSSSAQGNRSEVENELSNLFAKMALPGHDRRTDEYILVRQTGQDKFAGTTKCNLDHLPTKAEFNASCRLYRDGVGNYYPPPLAFERIDLPEQLAAQLHNLEPREQSKQCFQYKLEVWNRAHAEMGITGTDIFYQTDKNIKLDRNYKLRPEDRYIQTEKYGRREIQKRYEHQFQAGSLLPDILIKTPQNDIHFSYRFAGDAYANKRFEEFERAIKTKYGSDTEIKLKSKSGIMHDSKYLESWERGSADIRFAEFAGENRAHNKQFPAATVNMGRQPDGQGGMTRDRHVSVDYLLQNLPNSPWTQALKEGKLWDRVQVLARDGNRYMSPSRLEYSDPEHFTQLMDQVGLPVSMGRQSHANSVKFEQFDRQAAVIVADGPNLREVPDLSPEKLQQLSQKDVLIADRNEKGQRTGTYTNVVEYERLMMKLPSDAAQLLAEPSDRYSRAFVRPEPALPPISDSRRTYESRPRGPTVNSL","statement":[{"text":"Two large portions of the VirE2 molecule are not observed in the crystal structure. The experimental maps contained no electron density at the C terminus (last 39 residues), which suggests a flexible and possibly unstructured form.","type":"Results"},{"text":"No electron density was observed for these regions in a second crystal form that was obtained under different conditions and crystallized in a different space group (P21) (data not shown).","type":"Results"},{"text":"These findings suggest that the terminal regions of VirE2 are flexible or intrinsically unstructured, although partial proteolysis may also have occurred during crystallization.","type":"Results"},{"text":"The final model includes residues 112–179, 183–342, 345–356, 364–439, 445–473, and 476–517 of VirE2 and residues 30–57 of VirE1, 68 water molecules and one molecule of PEG.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T21:01:20.781Z"}},{"start":1,"end":111,"reference_id":"18678909","reference_source":"pmid","reference_html":"Crystal structure of the Agrobacterium virulence complex VirE1-VirE2 reveals a flexible protein that can accommodate different partners. <i> Dym O, Albeck S, Unger T, Jacobovitch J, Branzburg A, Michael Y, Frenkiel-Krispin D, Wolf SG, Elbaum M. </i> Proc Natl Acad Sci U S A, 2008","date":"2025-05-07T09:16:56.630Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"Selenomethionine VirE1 and VirE2 crystals were grown from a precipitating solution of 100 mM Hepes (pH = 7), 20% PEG 6000, 0.2M NH4Cl, and 1% Triton X-405."}]}],"cross_refs":[{"db":"PDB","id":"3BTP"}],"region_id":"DP04399r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08063","statements":[{"type":"Results","text":"Full-length nopaline VirE2 (P08062) (residues 1–556) was coexpressed with its small chaperone VirE1 (P08063) (residues 1–63), producing crystals that contained a single heterodimeric VirE1–VirE2 complex at a 1:1 ratio in the asymmetric unit cell."}]}],"sequence_construct":"MDPKAEGNGENITETAAGNVETSDFVNLKRQKREGVNSTGMSEIDMTGSQETPEHNMHGSPTHTDDLGPRLDADMLDSQSSHVSSSAQGNRSEVENELSNLFAKMALPGHDRRTDEYILVRQTGQDKFAGTTKCNLDHLPTKAEFNASCRLYRDGVGNYYPPPLAFERIDLPEQLAAQLHNLEPREQSKQCFQYKLEVWNRAHAEMGITGTDIFYQTDKNIKLDRNYKLRPEDRYIQTEKYGRREIQKRYEHQFQAGSLLPDILIKTPQNDIHFSYRFAGDAYANKRFEEFERAIKTKYGSDTEIKLKSKSGIMHDSKYLESWERGSADIRFAEFAGENRAHNKQFPAATVNMGRQPDGQGGMTRDRHVSVDYLLQNLPNSPWTQALKEGKLWDRVQVLARDGNRYMSPSRLEYSDPEHFTQLMDQVGLPVSMGRQSHANSVKFEQFDRQAAVIVADGPNLREVPDLSPEKLQQLSQKDVLIADRNEKGQRTGTYTNVVEYERLMMKLPSDAAQLLAEPSDRYSRAFVRPEPALPPISDSRRTYESRPRGPTVNSL","statement":[{"text":"A larger segment at the N terminus (111 residues) also lacks electron density. No electron density was observed for these regions in a second crystal form that was obtained under different conditions and crystallized in a different space group (P21) (data not shown).","type":"Results"},{"text":"These findings suggest that the terminal regions of VirE2 are flexible or intrinsically unstructured, although partial proteolysis may also have occurred during crystallization.","type":"Results"},{"text":"The final model includes residues 112–179, 183–342, 345–356, 364–439, 445–473, and 476–517 of VirE2 and residues 30–57 of VirE1, 68 water molecules and one molecule of PEG.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T21:00:50.701Z"}},{"start":1,"end":111,"reference_id":"18678909","reference_source":"pmid","reference_html":"Crystal structure of the Agrobacterium virulence complex VirE1-VirE2 reveals a flexible protein that can accommodate different partners. <i> Dym O, Albeck S, Unger T, Jacobovitch J, Branzburg A, Michael Y, Frenkiel-Krispin D, Wolf SG, Elbaum M. </i> Proc Natl Acad Sci U S A, 2008","date":"2025-05-19T09:37:58.282Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"Selenomethionine VirE1 and VirE2 crystals were grown from a precipitating solution of 100 mM Hepes (pH = 7), 20% PEG 6000, 0.2M NH4Cl, and 1% Triton X-405."}]}],"cross_refs":[{"db":"PDB","id":"3BTP"}],"region_id":"DP04399r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08063","statements":[{"type":"Results","text":"Full-length nopaline VirE2 (P08062) (residues 1–556) was coexpressed with its small chaperone VirE1 (P08063) (residues 1–63), producing crystals that contained a single heterodimeric VirE1–VirE2 complex at a 1:1 ratio in the asymmetric unit cell."}]}],"sequence_construct":"MDPKAEGNGENITETAAGNVETSDFVNLKRQKREGVNSTGMSEIDMTGSQETPEHNMHGSPTHTDDLGPRLDADMLDSQSSHVSSSAQGNRSEVENELSNLFAKMALPGHDRRTDEYILVRQTGQDKFAGTTKCNLDHLPTKAEFNASCRLYRDGVGNYYPPPLAFERIDLPEQLAAQLHNLEPREQSKQCFQYKLEVWNRAHAEMGITGTDIFYQTDKNIKLDRNYKLRPEDRYIQTEKYGRREIQKRYEHQFQAGSLLPDILIKTPQNDIHFSYRFAGDAYANKRFEEFERAIKTKYGSDTEIKLKSKSGIMHDSKYLESWERGSADIRFAEFAGENRAHNKQFPAATVNMGRQPDGQGGMTRDRHVSVDYLLQNLPNSPWTQALKEGKLWDRVQVLARDGNRYMSPSRLEYSDPEHFTQLMDQVGLPVSMGRQSHANSVKFEQFDRQAAVIVADGPNLREVPDLSPEKLQQLSQKDVLIADRNEKGQRTGTYTNVVEYERLMMKLPSDAAQLLAEPSDRYSRAFVRPEPALPPISDSRRTYESRPRGPTVNSL","statement":[{"text":"A larger segment at the N terminus (111 residues) also lacks electron density. No electron density was observed for these regions in a second crystal form that was obtained under different conditions and crystallized in a different space group (P21) (data not shown).","type":"Results"},{"text":"These findings suggest that the terminal regions of VirE2 are flexible or intrinsically unstructured, although partial proteolysis may also have occurred during crystallization.","type":"Results"},{"text":"The final model includes residues 112–179, 183–342, 345–356, 364–439, 445–473, and 476–517 of VirE2 and residues 30–57 of VirE1, 68 water molecules and one molecule of PEG.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T21:01:18.722Z"}},{"start":518,"end":556,"reference_id":"18678909","reference_source":"pmid","reference_html":"Crystal structure of the Agrobacterium virulence complex VirE1-VirE2 reveals a flexible protein that can accommodate different partners. <i> Dym O, Albeck S, Unger T, Jacobovitch J, Branzburg A, Michael Y, Frenkiel-Krispin D, Wolf SG, Elbaum M. </i> Proc Natl Acad Sci U S A, 2008","date":"2025-05-19T09:40:30.672Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2025_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"Selenomethionine VirE1 and VirE2 crystals were grown from a precipitating solution of 100 mM Hepes (pH = 7), 20% PEG 6000, 0.2M NH4Cl, and 1% Triton X-405."}]}],"cross_refs":[{"db":"PDB","id":"3BTP"}],"region_id":"DP04399r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P08063","statements":[{"type":"Results","text":"Full-length nopaline VirE2 (P08062) (residues 1–556) was coexpressed with its small chaperone VirE1 (P08063) (residues 1–63), producing crystals that contained a single heterodimeric VirE1–VirE2 complex at a 1:1 ratio in the asymmetric unit cell."}]}],"sequence_construct":"MDPKAEGNGENITETAAGNVETSDFVNLKRQKREGVNSTGMSEIDMTGSQETPEHNMHGSPTHTDDLGPRLDADMLDSQSSHVSSSAQGNRSEVENELSNLFAKMALPGHDRRTDEYILVRQTGQDKFAGTTKCNLDHLPTKAEFNASCRLYRDGVGNYYPPPLAFERIDLPEQLAAQLHNLEPREQSKQCFQYKLEVWNRAHAEMGITGTDIFYQTDKNIKLDRNYKLRPEDRYIQTEKYGRREIQKRYEHQFQAGSLLPDILIKTPQNDIHFSYRFAGDAYANKRFEEFERAIKTKYGSDTEIKLKSKSGIMHDSKYLESWERGSADIRFAEFAGENRAHNKQFPAATVNMGRQPDGQGGMTRDRHVSVDYLLQNLPNSPWTQALKEGKLWDRVQVLARDGNRYMSPSRLEYSDPEHFTQLMDQVGLPVSMGRQSHANSVKFEQFDRQAAVIVADGPNLREVPDLSPEKLQQLSQKDVLIADRNEKGQRTGTYTNVVEYERLMMKLPSDAAQLLAEPSDRYSRAFVRPEPALPPISDSRRTYESRPRGPTVNSL","statement":[{"text":"Two large portions of the VirE2 molecule are not observed in the crystal structure. The experimental maps contained no electron density at the C terminus (last 39 residues), which suggests a flexible and possibly unstructured form.","type":"Results"},{"text":"No electron density was observed for these regions in a second crystal form that was obtained under different conditions and crystallized in a different space group (P21) (data not shown).","type":"Results"},{"text":"These findings suggest that the terminal regions of VirE2 are flexible or intrinsically unstructured, although partial proteolysis may also have occurred during crystallization.","type":"Results"},{"text":"The final model includes residues 112–179, 183–342, 345–356, 364–439, 445–473, and 476–517 of VirE2 and residues 30–57 of VirE1, 68 water molecules and one molecule of PEG.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-16T21:01:00.625Z"}}],"regions_counter":5,"released":"2025_06","sequence":"MDPKAEGNGENITETAAGNVETSDFVNLKRQKREGVNSTGMSEIDMTGSQETPEHNMHGSPTHTDDLGPRLDADMLDSQSSHVSSSAQGNRSEVENELSNLFAKMALPGHDRRTDEYILVRQTGQDKFAGTTKCNLDHLPTKAEFNASCRLYRDGVGNYYPPPLAFERIDIPEQLAAQLHNLEPREQSKQCFQYKLEVWNRAHAEMGITGTDIFYQTDKNIKLDRNYKLRPEDRYIQTEKYGRREIQKRYEHQFQAGSLLPDILIKTPQNDIHFSYRFAGDAYANKRFEEFERAIKTKYGSDTEIKLKSKSGIMHDSKYLESWERGSADIRFAEFAGENRAHNKQFPAATVNMGRQPDGQGGMTRDRHVSVDYLLQNLPNSPWTQALKEGKLWDRVQVLARDGNRYMSPSRLEYSDPEHFTQLMDQVGLPVSMGRQSHANSVKFEQFDRQAAVIVADGPNLREVPDLSPEKLQQLSQKDVLIADRNEKGQRTGTYTNVVEYERLMMKLPSDAAQLLAEPSDRYSRAFVRPEPALPPISDSRRTYESRPRGPTVNSL","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"],"alphafold_very_low_content":0.24820143884892087,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.2697841726618705,"disprot_consensus":{"full":[{"start":1,"end":111,"type":"D"},{"start":518,"end":556,"type":"D"}],"Structural state":[{"start":1,"end":111,"type":"D"},{"start":518,"end":556,"type":"D"}],"Disorder function":[{"start":1,"end":111,"type":"F"},{"start":518,"end":556,"type":"F"}]}},{"disprot_id":"DP04401","acc":"A0AAI8ESY0","creator":"rpancsa","date":"2025-05-09T08:28:54.272Z","features":{"pfam":[{"id":"PF03524","name":"Conjugal transfer protein","start":28,"end":251}],"gene3D":[]},"genes":[{"name":{"value":"virB9","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAM37469.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAM37469.1"}}]},"olnNames":[{"value":"XAC2620","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAM37469.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAM37469.1"}}]}]}],"length":255,"name":"VirB9 protein","ncbi_taxon_id":190486,"organism":"Xanthomonas axonopodis pv. citri (strain 306)","regions":[{"start":154,"end":255,"reference_id":"27594685","reference_source":"pmid","reference_html":"VirB7 and VirB9 Interactions Are Required for the Assembly and Antibacterial Activity of a Type IV Secretion System. <i> Oliveira LC, Souza DP, Oka GU, Lima FDS, Oliveira RJ, Favaro DC, Wienk H, Boelens R, Farah CS, Salinas RK. </i> Structure, 2016","date":"2025-05-09T08:31:24.427Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04401r001","statement":[{"text":"In agreement with previous observations (Souza et al., 2011), the 1H-15N heteronuclear single quantum coherence (HSQC) spectrum of VirB9CT recorded at 37°C displays fewer cross peaks than expected and a broad distribution of line widths, characteristic of a domain with significant conformational freedom (Figure 1B).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-04T14:22:14.336Z"}},{"start":154,"end":255,"reference_id":"27594685","reference_source":"pmid","reference_html":"VirB7 and VirB9 Interactions Are Required for the Assembly and Antibacterial Activity of a Type IV Secretion System. <i> Oliveira LC, Souza DP, Oka GU, Lima FDS, Oliveira RJ, Favaro DC, Wienk H, Boelens R, Farah CS, Salinas RK. </i> Structure, 2016","date":"2025-06-05T08:22:45.855Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04401r002","statement":[{"text":"In contrast, the 1H-15N HSQC spectrum of 15N labeled VirB9CT in the presence of the unlabeled VirB7NT peptide displays the expected number of cross peaks and a narrower distribution of line widths (Figures 1B and S1), indicating that complex formation stabilizes a single VirB9CT conformation.","type":"Results"},{"text":"The profile of 15N order parameters along the backbone of VirB9CT in complex with VirB7NT is shown in Figures 4A and S6A and color-coded on the backbone of the complex (Figure 4B). VirB9CT displays S2 typical of a rigid protein with an average S2 value of 0.8.","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0AAI7ZGD2"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T13:28:34.103Z"}},{"start":154,"end":255,"reference_id":"27594685","reference_source":"pmid","reference_html":"VirB7 and VirB9 Interactions Are Required for the Assembly and Antibacterial Activity of a Type IV Secretion System. <i> Oliveira LC, Souza DP, Oka GU, Lima FDS, Oliveira RJ, Favaro DC, Wienk H, Boelens R, Farah CS, Salinas RK. </i> Structure, 2016","date":"2025-06-05T08:23:33.312Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000012","term_name":"molten globule to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04401r003","statement":[{"text":"In agreement with previous observations (Souza et al., 2011), the 1H-15N heteronuclear single quantum coherence (HSQC) spectrum of VirB9CT recorded at 37°C displays fewer cross peaks than expected and a broad distribution of line widths, characteristic of a domain with significant conformational freedom (Figure 1B). In contrast, the 1H-15N HSQC spectrum of 15N labeled VirB9CT in the presence of the unlabeled VirB7NT peptide displays the expected number of cross peaks and a narrower distribution of line widths (Figures 1B and S1), indicating that complex formation stabilizes a single VirB9CT conformation.","type":"Results"},{"text":"VirB9CT is only partially folded in solution but forms a tight and rigid complex upon binding to VirB7.","type":"Results"},{"text":"Here, we show that VirB7NT forms a short β strand upon binding to VirB9 and stabilizes it.","type":"Abstract"}],"states_connection":[{"source":"DP04401r001","target":"DP04401r002"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0AAI7ZGD2"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T13:28:50.909Z"}},{"start":154,"end":255,"reference_id":"38486495","reference_source":"pmid","reference_html":"Uncovering the Association Mechanism between Two Intrinsically Flexible Proteins. <i> Dávalos AL, Rivera Echeverri JD, Favaro DC, Junio de Oliveira R, Penteado Battesini Carretero G, Lacerda C, Midea Cuccovia I, Cangussu Cardoso MV, Farah CS, Kopke Salinas R. </i> ACS Chem Biol, 2024","date":"2025-05-09T09:58:20.471Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04401r004","statement":[{"text":"The greater ANS fluorescence change observed upon addition of the free protein relative to the complex indicates that the unbound VirB9Ct exposes a greater amount of hydrophobic surface area than the complex.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-04T13:46:13.559Z"}},{"start":154,"end":255,"reference_id":"38486495","reference_source":"pmid","reference_html":"Uncovering the Association Mechanism between Two Intrinsically Flexible Proteins. <i> Dávalos AL, Rivera Echeverri JD, Favaro DC, Junio de Oliveira R, Penteado Battesini Carretero G, Lacerda C, Midea Cuccovia I, Cangussu Cardoso MV, Farah CS, Kopke Salinas R. </i> ACS Chem Biol, 2024","date":"2025-06-05T08:25:11.545Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04401r005","statement":[{"text":"The greater ANS fluorescence change observed upon addition of the free protein relative to the complex indicates that the unbound VirB9Ct exposes a greater amount of hydrophobic surface area than the complex.","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0AAI7ZGD2"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T13:28:21.271Z"}},{"start":154,"end":255,"reference_id":"38486495","reference_source":"pmid","reference_html":"Uncovering the Association Mechanism between Two Intrinsically Flexible Proteins. <i> Dávalos AL, Rivera Echeverri JD, Favaro DC, Junio de Oliveira R, Penteado Battesini Carretero G, Lacerda C, Midea Cuccovia I, Cangussu Cardoso MV, Farah CS, Kopke Salinas R. </i> ACS Chem Biol, 2024","date":"2025-06-05T08:24:42.768Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000012","term_name":"molten globule to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04401r006","statement":[{"text":"The greater ANS fluorescence change observed upon addition of the free protein relative to the complex indicates that the unbound VirB9Ct exposes a greater amount of hydrophobic surface area than the complex.","type":"Results"}],"states_connection":[{"source":"DP04401r004","target":"DP04401r005"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0AAI7ZGD2"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T13:28:44.899Z"}},{"start":154,"end":255,"reference_id":"38486495","reference_source":"pmid","reference_html":"Uncovering the Association Mechanism between Two Intrinsically Flexible Proteins. <i> Dávalos AL, Rivera Echeverri JD, Favaro DC, Junio de Oliveira R, Penteado Battesini Carretero G, Lacerda C, Midea Cuccovia I, Cangussu Cardoso MV, Farah CS, Kopke Salinas R. </i> ACS Chem Biol, 2024","date":"2025-05-10T07:07:44.286Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001249","ec_ontology":"ECO","ec_name":"fluorescence evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"A0AAI7ZGD2","operator":null,"partner_start":24,"partner_end":46}],"region_id":"DP04401r007","statement":[{"text":"The greater ANS fluorescence change observed upon addition of the free protein relative to the complex indicates that the unbound VirB9Ct exposes a greater amount of hydrophobic surface area than the complex.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-04T14:06:41.985Z"}},{"start":154,"end":255,"reference_id":"38486495","reference_source":"pmid","reference_html":"Uncovering the Association Mechanism between Two Intrinsically Flexible Proteins. <i> Dávalos AL, Rivera Echeverri JD, Favaro DC, Junio de Oliveira R, Penteado Battesini Carretero G, Lacerda C, Midea Cuccovia I, Cangussu Cardoso MV, Farah CS, Kopke Salinas R. </i> ACS Chem Biol, 2024","date":"2025-05-10T07:08:40.894Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"A0AAI7ZGD2","operator":null,"partner_start":24,"partner_end":46}],"region_id":"DP04401r008","statement":[{"text":"In contrast, the 1H-15N HSQC spectrum of 15N labeled VirB9CT in the presence of the unlabeled VirB7NT peptide displays the expected number of cross peaks and a narrower distribution of line widths (Figures 1B and S1), indicating that complex formation stabilizes a single VirB9CT conformation.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-04T14:06:48.257Z"}},{"start":154,"end":255,"reference_id":"38486495","reference_source":"pmid","reference_html":"Uncovering the Association Mechanism between Two Intrinsically Flexible Proteins. <i> Dávalos AL, Rivera Echeverri JD, Favaro DC, Junio de Oliveira R, Penteado Battesini Carretero G, Lacerda C, Midea Cuccovia I, Cangussu Cardoso MV, Farah CS, Kopke Salinas R. </i> ACS Chem Biol, 2024","date":"2025-05-10T07:13:40.665Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006301","ec_ontology":"ECO","ec_name":"protein thermal shift assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"A0AAI7ZGD2","operator":null,"partner_start":24,"partner_end":46}],"region_id":"DP04401r009","statement":[{"text":"Notably, the thermal denaturation experiment showed that the complex has significantly higher unfolding enthalpy (29.57 kcal/mol) than the unbound VirB9Ct (10.42 kcal/mol; Figure 2C). This observation may be explained considering that VirB9Ct−VirB7Nt unfolding and dissociation\noccur within a single transition as a consequence of the coupling between these two processes.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-04T14:06:56.875Z"}},{"start":154,"end":255,"reference_id":"38486495","reference_source":"pmid","reference_html":"Uncovering the Association Mechanism between Two Intrinsically Flexible Proteins. <i> Dávalos AL, Rivera Echeverri JD, Favaro DC, Junio de Oliveira R, Penteado Battesini Carretero G, Lacerda C, Midea Cuccovia I, Cangussu Cardoso MV, Farah CS, Kopke Salinas R. </i> ACS Chem Biol, 2024","date":"2025-05-10T07:14:33.298Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006301","ec_ontology":"ECO","ec_name":"protein thermal shift assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04401r010","statement":[{"text":"Notably, the thermal denaturation experiment showed that the complex has significantly higher unfolding enthalpy (29.57 kcal/mol) than the unbound VirB9Ct (10.42 kcal/mol; Figure 2C). This observation may be explained considering that VirB9Ct−VirB7Nt unfolding and dissociation\noccur within a single transition as a consequence of the coupling between these two processes.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-04T13:47:05.982Z"}},{"start":154,"end":255,"reference_id":"38486495","reference_source":"pmid","reference_html":"Uncovering the Association Mechanism between Two Intrinsically Flexible Proteins. <i> Dávalos AL, Rivera Echeverri JD, Favaro DC, Junio de Oliveira R, Penteado Battesini Carretero G, Lacerda C, Midea Cuccovia I, Cangussu Cardoso MV, Farah CS, Kopke Salinas R. </i> ACS Chem Biol, 2024","date":"2025-06-05T08:25:56.718Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006301","ec_ontology":"ECO","ec_name":"protein thermal shift assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04401r011","statement":[{"text":"Notably, the thermal denaturation experiment showed that the complex has significantly higher unfolding enthalpy (29.57 kcal/mol) than the unbound VirB9Ct (10.42 kcal/mol; Figure 2C). This observation may be explained considering that VirB9Ct−VirB7Nt unfolding and dissociation\noccur within a single transition as a consequence of the coupling between these two processes.","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0AAI7ZGD2"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T13:28:08.717Z"}},{"start":154,"end":255,"reference_id":"38486495","reference_source":"pmid","reference_html":"Uncovering the Association Mechanism between Two Intrinsically Flexible Proteins. <i> Dávalos AL, Rivera Echeverri JD, Favaro DC, Junio de Oliveira R, Penteado Battesini Carretero G, Lacerda C, Midea Cuccovia I, Cangussu Cardoso MV, Farah CS, Kopke Salinas R. </i> ACS Chem Biol, 2024","date":"2025-06-05T08:26:40.149Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000012","term_name":"molten globule to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006301","ec_ontology":"ECO","ec_name":"protein thermal shift assay evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04401r012","statement":[{"text":"Notably, the thermal denaturation experiment showed that the complex has significantly higher unfolding enthalpy (29.57 kcal/mol) than the unbound VirB9Ct (10.42 kcal/mol; Figure 2C). This observation may be explained considering that VirB9Ct−VirB7Nt unfolding and dissociation\noccur within a single transition as a consequence of the coupling between these two processes.","type":"Results"}],"sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A0AAI7ZGD2"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T13:28:41.475Z"}},{"start":154,"end":255,"reference_id":"38486495","reference_source":"pmid","reference_html":"Uncovering the Association Mechanism between Two Intrinsically Flexible Proteins. <i> Dávalos AL, Rivera Echeverri JD, Favaro DC, Junio de Oliveira R, Penteado Battesini Carretero G, Lacerda C, Midea Cuccovia I, Cangussu Cardoso MV, Farah CS, Kopke Salinas R. </i> ACS Chem Biol, 2024","date":"2025-05-10T07:21:12.260Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"A0AAI7ZGD2","operator":null,"partner_start":24,"partner_end":46}],"region_id":"DP04401r013","statement":[{"text":"Binding of VirB9Ct to VirB7Nt is enthalpically driven as indicated by isothermal titration calorimetry (ITC) experiments carried out at 10, 25, and 35 °C (Figure 3A,B). The VirB9Ct−VirB7Nt Kd app (see Experimental Section) is 0.70 μM at 35 °C, similar to the value reported before.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-04T14:06:32.006Z"}},{"start":154,"end":171,"reference_id":"38486495","reference_source":"pmid","reference_html":"Uncovering the Association Mechanism between Two Intrinsically Flexible Proteins. <i> Dávalos AL, Rivera Echeverri JD, Favaro DC, Junio de Oliveira R, Penteado Battesini Carretero G, Lacerda C, Midea Cuccovia I, Cangussu Cardoso MV, Farah CS, Kopke Salinas R. </i> ACS Chem Biol, 2024","date":"2025-06-05T08:20:31.232Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04401r014","statement":[{"text":"The backbone 15N chemical shifts for residues 163−171 along the β1 showed a very good agreement with random coil chemical shifts predicted from the VirB9Ct amino acid sequence using the ncIDP online server, while a poorer agreement was observed along β2 (Figure 6A,B), suggesting that the VirB9Ct β1 is disordered in the absence of VirB7Nt.","type":"Results"},{"text":"The authors already stated in their earlier article (PMID:27594685) that the S2 order parameters of the termini of the VirB9Ct domain are low, so they are disodered (even in the complex), although residue boundaries were not mentioned, so the regions could not be annotated based on that statement. Here they show that in the unbound state the first beta strand, β1, is disodered, which ultimately means that the whole N-terminal region up until residue 171 must be disordered. This is further supported by the H−15N HSQC spectrum of unbound VirB9Ct in Figure 4A, where all the resolved peaks belonging to residues 154-171 show a narrow peak distribution around 8.5 pmm that is typical for disordered regions.","type":"Curator statement"},{"text":"NMR data obtained for VirB9Ct in the unbound state at 35 °C showed strong evidence that β1 is unstructured in the absence of VirB7Nt, while\nother residues also located at the VirB7Nt binding region experience an equilibrium between multiple conformations at the millisecond time scale.","type":"Discussion"}],"cross_refs":[{"db":"BMRB","id":"51836"},{"db":"BMRB","id":"52005"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-05T13:27:52.579Z"}},{"start":154,"end":255,"reference_id":"38486495","reference_source":"pmid","reference_html":"Uncovering the Association Mechanism between Two Intrinsically Flexible Proteins. <i> Dávalos AL, Rivera Echeverri JD, Favaro DC, Junio de Oliveira R, Penteado Battesini Carretero G, Lacerda C, Midea Cuccovia I, Cangussu Cardoso MV, Farah CS, Kopke Salinas R. </i> ACS Chem Biol, 2024","date":"2025-05-10T08:23:57.882Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006337","ec_ontology":"ECO","ec_name":"stopped-flow fluorescence spectroscopy evidence","unpublished":true,"released":"2025_06","version":0,"interaction_partner":[{"db":"UniProt","id":"A0AAI7ZGD2","operator":null,"partner_start":24,"partner_end":46}],"region_id":"DP04401r015","statement":[{"text":"The presence of tryptophan residues at positions 177 and 34 in VirB9Ct and VirB7Nt, respectively, and the millisecond exchange time scale\nbetween unbound and bound VirB9Ct states, favored the use of stopped-flow fluorescence to follow the VirB9Ct−VirB7Nt association kinetics.","type":"Results"},{"text":"These observations suggest that the VirB9Ct interaction with VirB7Nt could be described by a conformational-selection mechanism at 25 °C.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-06-04T13:54:51.936Z"}},{"start":154,"end":255,"reference_id":"21589901","reference_source":"pmid","reference_html":"A component of the Xanthomonadaceae type IV secretion system combines a VirB7 motif with a N0 domain found in outer membrane transport proteins. <i> Souza DP, Andrade MO, Alvarez-Martinez CE, Arantes GM, Farah CS, Salinas RK. </i> PLoS Pathog, 2011","date":"2025-06-03T18:35:37.697Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"region_id":"DP04401r016","statement":[{"text":"The 15N-HSQC spectrum of VirB9XAC2620_154–255 showed characteristics of poor line shape and chemical shift dispersion (Figure 4; red) suggestive of conformational disorder and a probable lack of stable tertiary structure.","type":"Results"}]},{"start":154,"end":255,"reference_id":"21589901","reference_source":"pmid","reference_html":"A component of the Xanthomonadaceae type IV secretion system combines a VirB7 motif with a N0 domain found in outer membrane transport proteins. <i> Souza DP, Andrade MO, Alvarez-Martinez CE, Arantes GM, Farah CS, Salinas RK. </i> PLoS Pathog, 2011","date":"2025-06-03T18:42:02.451Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0043684","term_name":"type IV secretion system complex","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","region_id":"DP04401r017","statement":[{"text":"This analysis showed that only residues 27–41, within the disordered VirB7 N-terminus, undergo significant chemical shift perturbations (Figure 3C and D). This region is adjacent to, but does not overlap, the N-terminal region involved in VirB7XAC2622 oligomerization (residues 42–49).","type":"Results"},{"text":"Chemical shift perturbation data showed that two regions are involved in VirB7XAC2622 self-interactions: a region in the unfolded N-terminus (residues 42–49) and a patch on the surface of the globular domain made up of residues 63–65, 85–93, 111–119 and 131 (Figure 2B and C).","type":"Results"},{"text":"In well-characterized T4SSs, VirB7 is a lipoprotein attached to the periplasmic side of the outer membrane [28]. It has been shown to interact with several T4SS subunits [29], including itself [30] and the VirB9 C-terminal region [31], [32].","type":"Introduction"}],"term_comment":"","term_def":"\"A complex of proteins related to those involved in bacterial DNA conjugative transfer, that permits the transfer of DNA or proteins into the extracellular milieu or directly into host cells. In general the type IV complex forms a multisubunit cell-envelope-spanning structure composed of a secretion channel and often a pilus or other surface filament or protein(s).\" [GOC:ml]","term_is_obsolete":false,"term_not_annotate":false},{"start":154,"end":255,"reference_id":"21589901","reference_source":"pmid","reference_html":"A component of the Xanthomonadaceae type IV secretion system combines a VirB7 motif with a N0 domain found in outer membrane transport proteins. <i> Souza DP, Andrade MO, Alvarez-Martinez CE, Arantes GM, Farah CS, Salinas RK. </i> PLoS Pathog, 2011","date":"2025-06-03T18:43:51.608Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"A0AAI7ZGD2","operator":null,"partner_start":27,"partner_end":41}],"region_id":"DP04401r018","statement":[{"text":"In order to map the VirB9 binding site on the structure of VirB7, we assigned the backbone resonances of VirB7XAC2622_24–139 in complex with VirB9XAC2620_154–255 and analyzed the chemical shift differences (Figure 3A and B). This analysis showed that only residues 27–41, within the disordered VirB7 N-terminus, undergo significant chemical shift perturbations (Figure 3C and D).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":18,"released":"2025_06","sequence":"MKLFNRYRVALLSALPLALCALSAAAQVVQEYEYAPDRIYQVRTGLGITTQVELSPNEKILDYSTGFTGGWELTRRENVFYLKPKNVDVDTNMMIRTATHSYILELKVVATDWQRLEQAKQAGVQYKVVFTYPKDTSFNNVADADTSKNGPLLNAKILKDRRYYYDYDYATRTKKSWLIPSRVYDDGKFTYINMDLTRFPTGNFPAVFAREKEHAEDFLVNTTVEGNTLIVHGTYPFLVVRHGDNVVGLRRNKQK","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Lysobacteraceae","Xanthomonas"],"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.4,"disprot_consensus":{"full":[{"start":154,"end":255,"type":"T"}],"Structural state":[{"start":154,"end":255,"type":"D"}],"Structural transition":[{"start":154,"end":255,"type":"T"}],"Molecular function":[{"start":154,"end":255,"type":"F"}],"Cellular component":[{"start":154,"end":255,"type":"F"}]}},{"disprot_id":"DP04406","acc":"Q8CGN5","creator":"eficho","date":"2025-05-15T11:44:40.158Z","features":{"pfam":[{"id":"PF03036","name":"Perilipin family","start":15,"end":415}],"gene3D":[]},"genes":[{"name":{"value":"Plin1"},"synonyms":[{"value":"Peri"},{"value":"Plin"}]}],"length":517,"name":"Perilipin-1","ncbi_taxon_id":10090,"organism":"Mus musculus","regions":[{"start":406,"end":517,"reference_id":"40109298","reference_source":"pmid","reference_html":"The C-terminal end of PLIN1 displays structural disorder. <i> Páez-Pérez ED, Llamas-García ML, Montero-Morán GM, Lara-González S. </i> Biochem Biophys Rep, 2025","date":"2026-03-31T14:40:41.875Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04406r001","statement":[{"text":"The spectrum of mPLIN1C is consistent with that of a disordered protein, exhibiting negative ellipticity at 200 nm (−15167 deg·cm2·dmol−1) and low ellipticity at 222 nm (−1326 deg·cm2·dmol−1) (Fig. 4A). These features have been associated with the presence of residual secondary structure, estimated to be around 10–20 % [54]. Analysis of the CD data using the BestSel algorithm [55] indicates that mPLIN1C is predominantly disordered, showing a content of approximately ∼54 % coil, ∼26.3 % β-strands, ∼19.7 % β-turns, and no contribution from α-helices (Table 1).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-31T14:40:57.078Z"}},{"start":406,"end":517,"reference_id":"40109298","reference_source":"pmid","reference_html":"The C-terminal end of PLIN1 displays structural disorder. <i> Páez-Pérez ED, Llamas-García ML, Montero-Morán GM, Lara-González S. </i> Biochem Biophys Rep, 2025","date":"2026-03-31T14:45:18.703Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000019","term_name":"disorder to pre-molten globule","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04406r002","statement":[{"text":"A deeper analysis conducted by FELLS regarding the possible position of these formed α-helices indicates two regions comprising residues 423 to 432 and 507 to 514. These results show that a segment of mPLIN1C residues undergoes a transition from disordered to ordered in the presence of micelles.","type":"Results"},{"text":"To determine the type of conformation present in the absence and presence of micelles, a dual-wavelength plot of ellipticity at 200 and 222 nm was analyzed (Fig. 4C). This approach has been used to differentiate IDPs into PMG and RC [49]. The data demonstrate that in the presence of micelles, mPLIN1C behaves like a PMG, which contrasts with our observations in solution, where the protein displayed a coil-like conformation.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"8984","statements":[{"type":"Results","text":"To determine the SDS concentration required to obtain micelles in the CD buffer, a DLS experiment was conducted, through which the critical micelle concentration (CMC) was estimated."}],"entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-31T14:47:09.606Z"}},{"start":406,"end":517,"reference_id":"40109298","reference_source":"pmid","reference_html":"The C-terminal end of PLIN1 displays structural disorder. <i> Páez-Pérez ED, Llamas-García ML, Montero-Morán GM, Lara-González S. </i> Biochem Biophys Rep, 2025","date":"2026-03-31T14:46:31.320Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006334","ec_ontology":"ECO","ec_name":"differential scanning fluorimetry evidence","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04406r003","statement":[{"text":"The DSF curve showed the typical behavior of an unfolded proteins (Fig. 6) [63].","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-31T14:46:40.052Z"}},{"start":406,"end":517,"reference_id":"40109298","reference_source":"pmid","reference_html":"The C-terminal end of PLIN1 displays structural disorder. <i> Páez-Pérez ED, Llamas-García ML, Montero-Morán GM, Lara-González S. </i> Biochem Biophys Rep, 2025","date":"2026-03-31T14:36:48.848Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"unspecified"}],"region_id":"DP04406r004","statement":[{"text":"However, mPLIN1C exhibited anomalous electrophoretic mobility, migrating at approximately 20 kDa (Fig. 2A). This was regarded as an initial indication of the protein's disordered behavior.","type":"Results"}]},{"start":406,"end":517,"reference_id":"40109298","reference_source":"pmid","reference_html":"The C-terminal end of PLIN1 displays structural disorder. <i> Páez-Pérez ED, Llamas-García ML, Montero-Morán GM, Lara-González S. </i> Biochem Biophys Rep, 2025","date":"2026-03-31T14:39:26.363Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001184","ec_ontology":"ECO","ec_name":"gel-filtration evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"unspecified"}],"region_id":"DP04406r005","statement":[{"text":"In the analytical SEC assay, the protein eluted as a single peak (Fig. 2B) with an elution volume corresponding to a RS of 28.3 Å (Fig. 2C). If we calculate the theoretical RS for this domain, assuming a molecular weight of 15.6 kDa and a globular conformation, we obtain a value of 19.6 Å according to equation (1). ","type":"Results"},{"text":" As can be appreciated in Fig. 2D, the experimental RS of mPLIN1C is situated between the pre-molten globule and coil-like conformations. ","type":"Results"}]}],"regions_counter":5,"released":"2026_06","sequence":"MSMNKGPTLLDGDLPEQENVLQRVLQLPVVSGTCECFQKTYNSTKEAHPLVASVCNAYEKGVQGASNLAAWSMEPVVRRLSTQFTAANELACRGLDHLEEKIPALQYPPEKIASELKGTISTRLRSARNSISVPIASTSDKVLGATLAGCELALGMAKETAEYAANTRVGRLASGGADLALGSIEKVVEFLLPPDKESAPSSGRQRTQKAPKAKPSLVRRVSTLANTLSRHTMQTTAWALKQGHSLAMWIPGVAPLSSLAQWGASAAMQVVSRRQSEVRVPWLHNLAASQDESHDDQTDTEGEETDDEEEEEESEAEENVLREVTALPNPRGLLGGVVHTVQNTLRNTISAVTWAPAAVLGTVGRILHLTPAQAVSSTKGRAMSLSDALKGVTDNVVDTVVHYVPLPRLSLMEPESEFRDIDNPSAEAERKGSGARPASPESTPRPGQPRGSLRSVRGLSAPSCPGLDDKTEASARPGFLAMPREKPARRVSDSFFRPSVMEPILGRAQYSQLRKKS","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"alphafold_very_low_content":0.4874274661508704,"disorder_content":0.21663442940038685,"disprot_consensus":{"full":[{"start":406,"end":517,"type":"T"}],"Structural state":[{"start":406,"end":517,"type":"D"}],"Structural transition":[{"start":406,"end":517,"type":"T"}]}},{"disprot_id":"DP04407","acc":"A9UJZ9","creator":"viglesias","date":"2025-05-21T18:29:31.677Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":25,"end":309}],"gene3D":[]},"genes":[{"name":{"value":"p38a","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"AAV52829.1","url":"https://www.ebi.ac.uk/ena/browser/view/AAV52829.1"}},{"code":"ECO:0000313","source":{"name":"RefSeq","id":"NP_001117170.1","url":"https://www.ncbi.nlm.nih.gov/protein/NP_001117170.1"}}]}}],"length":361,"name":"mitogen-activated protein kinase","ncbi_taxon_id":8030,"organism":"Salmo salar","regions":[{"start":171,"end":187,"reference_id":"21699901","reference_source":"pmid","reference_html":"p38α MAP kinase dimers with swapped activation segments and a novel catalytic loop conformation. <i> Rothweiler U, Åberg E, Johnson KA, Hansen TE, Jørgensen JB, Engh RA. </i> J Mol Biol, 2011","date":"2026-05-07T19:44:51.612Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"3OHT"}],"region_id":"DP04407r001","statement":[{"text":"The residues between Gly170 and Y188 (of conserved motifs DFG and YxAPE) are not defined in electron density. Despite their flexibility, they will add to the total dimerization interface.","type":"Results"},{"text":"Homo sapiens p38α numbering is used throughout this article.","type":"Results"},{"text":"Residues 31–33, 111–122 and 262–268 have weak or unclear electron density; the activation loop (residues 171–187) is apparently disordered and does not appear in the electron density map.","type":"Methods"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"49375","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-07T19:45:01.245Z"}}],"regions_counter":2,"released":"2026_06","sequence":"MSHKERPTFYRQELNKTIWEVPERYQTLSPVGSGAYGSVCSSYDVKSGLKIAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPATSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNMTVDIWSVGCIMAELLTGRTLFPGTDHINQLQQIMRLTGTPPASVISRMPSHEARNYINSLPQMPKRNFADVFIGANPLAVDLLEKMLVLDTDKRITASEALAHPYFSQYHDPDDEPESEPYDQSFESRQLEIEEWKRLTYEEVCSFETPPFDGDEMES","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Actinopterygii","Neopterygii","Teleostei","Protacanthopterygii","Salmoniformes","Salmonidae","Salmoninae","Salmo"],"alphafold_very_low_content":0.04709141274238227,"disorder_content":0.04709141274238227,"disprot_consensus":{"full":[{"start":171,"end":187,"type":"D"}],"Structural state":[{"start":171,"end":187,"type":"D"}]}},{"disprot_id":"DP04408","acc":"Q38AU6","creator":"viglesias","date":"2025-05-21T19:12:55.071Z","features":{"pfam":[{"id":"PF00583","name":"Acetyltransferase (GNAT) family","start":166,"end":287}],"gene3D":[]},"genes":[{"orfNames":[{"value":"Tb10.70.0180","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EAN78074.1","url":"https://www.ebi.ac.uk/ena/browser/view/EAN78074.1"}}]}]}],"length":348,"name":"N-acetyltransferase domain-containing protein","ncbi_taxon_id":185431,"organism":"Trypanosoma brucei brucei (strain 927/4 GUTat10.1)","regions":[{"start":72,"end":126,"reference_id":"39579771","reference_source":"pmid","reference_html":"The kinetoplastid kinetochore protein KKT23 acetyltransferase is a structural homolog of GCN5 that acetylates the histone H2A C-terminal tail. <i> Ludzia P, Ishii M, Deák G, Spanos C, Wilson MD, Redfield C, Akiyoshi B. </i> Structure, 2025","date":"2026-05-07T19:22:38.767Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"BMRB","id":"52461"}],"region_id":"DP04408r001","statement":[{"text":"The N-terminal helical domain and the C-terminal GNAT domain are linked by a stretch of unstructured residues\n","type":"Results"},{"text":"We have determined the structures of KKT232−70 and KKT23125−348. However, the region between these two domains, encompassing residues 72–126, is predicted to be disordered (Figure S1B). To gain insight into this region’s structural details, we expressed and purified 15N-labeled full-length KKT23. KKT232−348 gives a well-resolved 1H-15N BEST TROSY spectrum.","type":"Results"},{"text":"The analysis revealed hetNOE values below 0.4 for the 39 strongest peaks, indicating that they correspond to unstructured regions of KKT23, most likely the region between residues 72–126. In fact, some of these peaks were assigned to residues in the region of A91 to E100 (Figure S10A). In conclusion, our data show that the structure of KKT23 consists of an N-terminal helical region, a stretch of unstructured residues, and the GNAT domain at the protein C-terminus.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15351","entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-07T19:22:43.078Z"}},{"start":192,"end":201,"reference_id":"39579771","reference_source":"pmid","reference_html":"The kinetoplastid kinetochore protein KKT23 acetyltransferase is a structural homolog of GCN5 that acetylates the histone H2A C-terminal tail. <i> Ludzia P, Ishii M, Deák G, Spanos C, Wilson MD, Redfield C, Akiyoshi B. </i> Structure, 2025","date":"2026-05-07T19:30:00.834Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"BMRB","id":"52461"}],"region_id":"DP04408r002","statement":[{"text":"(C) The {1H}-15N heteronuclear NOE ratios were measured and plotted against the sequence of KKT23125−348. Most of the residues display hetNOE ratios >0.7 indicating a rigid conformation of the protein backbone. The regions with higher flexibility (ratios < 0.7) include 126–128, 137–143, and 192–201. The regions between 126–128 and 137–143 are coils according to the crystal structure, whereas no electron density is visible for residues 192–200 suggesting that all three regions are part of flexible loops.","type":"Results"},{"text":"The regions between 126–128, 137–143, and 192–201 show reduced hetNOE ratios suggesting a higher flexibility compared to the rest of the protein; this is consistent with the analysis of chemical shifts by TALOS-N that shows no secondary structure for these regions in solution. Moreover, the reduced hetNOE ratios are consistent with the elevated B-factors observed for regions 126–128 and 137–143, and the absence of electron density observed for 192–200 in the crystal structure (data not shown).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15351","entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-07T19:30:14.432Z"}},{"start":72,"end":126,"reference_id":"39579771","reference_source":"pmid","reference_html":"The kinetoplastid kinetochore protein KKT23 acetyltransferase is a structural homolog of GCN5 that acetylates the histone H2A C-terminal tail. <i> Ludzia P, Ishii M, Deák G, Spanos C, Wilson MD, Redfield C, Akiyoshi B. </i> Structure, 2025","date":"2026-05-07T19:23:27.713Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"BMRB","id":" 52461"}],"region_id":"DP04408r003","statement":[{"text":"The N-terminal helical domain and the C-terminal GNAT domain are linked by a stretch of unstructured residues","type":"Results"},{"text":"We have determined the structures of KKT232−70 and KKT23125−348. However, the region between these two domains, encompassing residues 72–126, is predicted to be disordered (Figure S1B). To gain insight into this region’s structural details, we expressed and purified 15N-labeled full-length KKT23. KKT232−348 gives a well-resolved 1H-15N BEST TROSY spectrum.","type":"Results"},{"text":"The analysis revealed hetNOE values below 0.4 for the 39 strongest peaks, indicating that they correspond to unstructured regions of KKT23, most likely the region between residues 72–126. In fact, some of these peaks were assigned to residues in the region of A91 to E100 (Figure S10A). In conclusion, our data show that the structure of KKT23 consists of an N-terminal helical region, a stretch of unstructured residues, and the GNAT domain at the protein C-terminus.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15351","entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-07T19:23:31.133Z"}}],"regions_counter":3,"released":"2026_06","sequence":"MLLSDEHLALLAKYYATVEFTGEQKDALIEKYWEANEAERKAIARAYASLFANDADFIQRLLAHYDMHVSPHVSQGASSCNENGEPCKSEAELSAGAPAEQDGNGSNNGSLPARPAKPSKGPSGQQLTYSQLVLRTAIQDQYSKLSGDGPFPMAFGLVLSEEERREVIDLYSLQFQYPDQPELQRLVILPQTHSTRTRRRAKGSYTWYLRSLNTNEMVCAVTIMAHHYETHHFVEVPLFATGVGYKKHGFGRLMNAALLQWCVETGFEFVMISADVKAIPFWSHLGYKTMEKSELTRIVFYYEHNCYKFKGAEVMIRYCRTWPTDGVKEALARVQKVIVSGHVGLMDA","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Trypanosoma"],"alphafold_very_low_content":0.20402298850574713,"disorder_content":0.1867816091954023,"disprot_consensus":{"full":[{"start":72,"end":126,"type":"D"},{"start":192,"end":201,"type":"D"}],"Structural state":[{"start":72,"end":126,"type":"D"},{"start":192,"end":201,"type":"D"}],"Disorder function":[{"start":72,"end":126,"type":"F"}]}},{"disprot_id":"DP04409","acc":"Q54HW9","creator":"viglesias","date":"2025-05-21T19:45:24.660Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"matA","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CBA34802.1","url":"https://www.ebi.ac.uk/ena/browser/view/CBA34802.1"}}]},"orfNames":[{"value":"DDB_G0289165","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"EAL62861.1","url":"https://www.ebi.ac.uk/ena/browser/view/EAL62861.1"}}]}]}],"length":107,"name":"MatA protein","ncbi_taxon_id":44689,"organism":"Dictyostelium discoideum","regions":[{"start":1,"end":34,"reference_id":"28879231","reference_source":"pmid","reference_html":"Homeodomain-like DNA binding proteins control the haploid-to-diploid transition in <i>Dictyostelium</i>. <i> Hedgethorne K, Eustermann S, Yang JC, Ogden TEH, Neuhaus D, Bloomfield G. </i> Sci Adv, 2017","date":"2025-05-23T14:11:38.548Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006285","ec_ontology":"ECO","ec_name":"magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"5NR5"},{"db":"BMRB","id":"34126"}],"region_id":"DP04409r001","statement":[{"text":"The NMR structure of MatA (Fig. 1, A and C; figs. S2 and S3; and table S1) shows that it consists of a well-ordered, folded core domain of approximately 50 amino acids arranged in three α helices (residues 36 to 50, 56 to 64, and 68 to 79) that pack together to form a structure resembling a homeodomain fold. This core domain is flanked by long, largely unstructured tails at both the N and C termini (Fig. 1C). ","type":"Results"},{"text":"The tail regions of MatA (C) and MatB (D) extend flexibly away from the well-folded core (N-terminal tails in pale cyan and C-terminal tails in light orange). Heteronuclear 15N{1H} NOE data for MatA (E) and MatB (F) suggest that, in both cases, there may be some structure in the disordered tails (see text).","type":"Figure"},{"text":"The plots for MatA and MatB share similar overall shapes, both showing high values of the NOE ratio for residues in a rigid core domain (approximately residues 35 to 80) and lower values in both N- and C-terminal tails.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T16:41:06.445Z"}},{"start":81,"end":107,"reference_id":"28879231","reference_source":"pmid","reference_html":"Homeodomain-like DNA binding proteins control the haploid-to-diploid transition in <i>Dictyostelium</i>. <i> Hedgethorne K, Eustermann S, Yang JC, Ogden TEH, Neuhaus D, Bloomfield G. </i> Sci Adv, 2017","date":"2025-05-23T14:11:50.430Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006285","ec_ontology":"ECO","ec_name":"magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"5NR5"},{"db":"BMRB","id":"34126"}],"region_id":"DP04409r002","statement":[{"text":"The NMR structure of MatA (Fig. 1, A and C; figs. S2 and S3; and table S1) shows that it consists of a well-ordered, folded core domain of approximately 50 amino acids arranged in three α helices (residues 36 to 50, 56 to 64, and 68 to 79) that pack together to form a structure resembling a homeodomain fold. This core domain is flanked by long, largely unstructured tails at both the N and C termini (Fig. 1C). ","type":"Results"},{"text":"The tail regions of MatA (C) and MatB (D) extend flexibly away from the well-folded core (N-terminal tails in pale cyan and C-terminal tails in light orange). Heteronuclear 15N{1H} NOE data for MatA (E) and MatB (F) suggest that, in both cases, there may be some structure in the disordered tails (see text).","type":"Figure"},{"text":"The plots for MatA and MatB share similar overall shapes, both showing high values of the NOE ratio for residues in a rigid core domain (approximately residues 35 to 80) and lower values in both N- and C-terminal tails.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T16:41:08.092Z"}},{"start":1,"end":34,"reference_id":"28879231","reference_source":"pmid","reference_html":"Homeodomain-like DNA binding proteins control the haploid-to-diploid transition in <i>Dictyostelium</i>. <i> Hedgethorne K, Eustermann S, Yang JC, Ogden TEH, Neuhaus D, Bloomfield G. </i> Sci Adv, 2017","date":"2025-05-23T14:10:59.622Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006285","ec_ontology":"ECO","ec_name":"magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"BMRB","id":"34126"},{"db":"PDB","id":"5NR5"}],"region_id":"DP04409r003","statement":[{"text":"The NMR structure of MatA (Fig. 1, A and C; figs. S2 and S3; and table S1) shows that it consists of a well-ordered, folded core domain of approximately 50 amino acids arranged in three α helices (residues 36 to 50, 56 to 64, and 68 to 79) that pack together to form a structure resembling a homeodomain fold. This core domain is flanked by long, largely unstructured tails at both the N and C termini (Fig. 1C). ","type":"Results"},{"text":"The tail regions of MatA (C) and MatB (D) extend flexibly away from the well-folded core (N-terminal tails in pale cyan and C-terminal tails in light orange). Heteronuclear 15N{1H} NOE data for MatA (E) and MatB (F) suggest that, in both cases, there may be some structure in the disordered tails (see text).","type":"Figure"},{"text":"The plots for MatA and MatB share similar overall shapes, both showing high values of the NOE ratio for residues in a rigid core domain (approximately residues 35 to 80) and lower values in both N- and C-terminal tails.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T16:41:05.055Z"}},{"start":81,"end":107,"reference_id":"28879231","reference_source":"pmid","reference_html":"Homeodomain-like DNA binding proteins control the haploid-to-diploid transition in <i>Dictyostelium</i>. <i> Hedgethorne K, Eustermann S, Yang JC, Ogden TEH, Neuhaus D, Bloomfield G. </i> Sci Adv, 2017","date":"2025-05-23T14:11:21.923Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006285","ec_ontology":"ECO","ec_name":"magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"BMRB","id":"34126"},{"db":"PDB","id":"5NR5"}],"region_id":"DP04409r004","statement":[{"text":"The NMR structure of MatA (Fig. 1, A and C; figs. S2 and S3; and table S1) shows that it consists of a well-ordered, folded core domain of approximately 50 amino acids arranged in three α helices (residues 36 to 50, 56 to 64, and 68 to 79) that pack together to form a structure resembling a homeodomain fold. This core domain is flanked by long, largely unstructured tails at both the N and C termini (Fig. 1C). ","type":"Results"},{"text":"The tail regions of MatA (C) and MatB (D) extend flexibly away from the well-folded core (N-terminal tails in pale cyan and C-terminal tails in light orange). Heteronuclear 15N{1H} NOE data for MatA (E) and MatB (F) suggest that, in both cases, there may be some structure in the disordered tails (see text).","type":"Figure"},{"text":"The plots for MatA and MatB share similar overall shapes, both showing high values of the NOE ratio for residues in a rigid core domain (approximately residues 35 to 80) and lower values in both N- and C-terminal tails.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T16:41:55.875Z"}}],"regions_counter":4,"released":"2026_06","sequence":"MDPLDKIINDIKKEANDSGVTLAPLSVPKPKLEELSEQQKIILAEYIAEVGLQNITAITLSKKLNITVEKAKNYIKNSNRLGRTNNLKTIGILQEEVSSMEAKSMTW","taxonomy":["Eukaryota","Amoebozoa","Evosea","Eumycetozoa","Dictyostelia","Dictyosteliales","Dictyosteliaceae","Dictyostelium"],"alphafold_very_low_content":0.028037383177570093,"disorder_content":0.5700934579439252,"disprot_consensus":{"full":[{"start":1,"end":34,"type":"D"},{"start":81,"end":107,"type":"D"}],"Structural state":[{"start":1,"end":34,"type":"D"},{"start":81,"end":107,"type":"D"}],"Disorder function":[{"start":1,"end":34,"type":"F"},{"start":81,"end":107,"type":"F"}]}},{"disprot_id":"DP04410","acc":"D3UFE5","creator":"viglesias","date":"2025-05-21T20:00:03.578Z","features":{"pfam":[],"gene3D":[]},"genes":[{"name":{"value":"matB","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CBA34794.1","url":"https://www.ebi.ac.uk/ena/browser/view/CBA34794.1"}}]}}],"length":107,"name":"MatB protein","ncbi_taxon_id":44689,"organism":"Dictyostelium discoideum","regions":[{"start":1,"end":34,"reference_id":"28879231","reference_source":"pmid","reference_html":"Homeodomain-like DNA binding proteins control the haploid-to-diploid transition in <i>Dictyostelium</i>. <i> Hedgethorne K, Eustermann S, Yang JC, Ogden TEH, Neuhaus D, Bloomfield G. </i> Sci Adv, 2017","date":"2026-03-30T16:33:23.456Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006285","ec_ontology":"ECO","ec_name":"magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"5NR6"},{"db":"BMRB","id":"34127"}],"region_id":"DP04410r001","statement":[{"text":"The plots for MatA and MatB share similar overall shapes, both showing high values of the NOE ratio for residues in a rigid core domain (approximately residues 35 to 80) and lower values in both N- and C-terminal tails.","type":"Results"},{"text":"We report that the nuclear magnetic resonance structures of two of them, MatA and MatB, contain helix-turn-helix folds flanked by largely disordered amino- and carboxyl-terminal tails.","type":"Abstract"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T16:34:08.856Z"}},{"start":81,"end":107,"reference_id":"28879231","reference_source":"pmid","reference_html":"Homeodomain-like DNA binding proteins control the haploid-to-diploid transition in <i>Dictyostelium</i>. <i> Hedgethorne K, Eustermann S, Yang JC, Ogden TEH, Neuhaus D, Bloomfield G. </i> Sci Adv, 2017","date":"2026-03-30T16:32:59.521Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006285","ec_ontology":"ECO","ec_name":"magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"5NR6"},{"db":"BMRB","id":"34127"}],"region_id":"DP04410r002","statement":[{"text":"The plots for MatA and MatB share similar overall shapes, both showing high values of the NOE ratio for residues in a rigid core domain (approximately residues 35 to 80) and lower values in both N- and C-terminal tails.","type":"Results"},{"text":"We report that the nuclear magnetic resonance structures of two of them, MatA and MatB, contain helix-turn-helix folds flanked by largely disordered amino- and carboxyl-terminal tails.","type":"Abstract"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T16:34:06.552Z"}},{"start":1,"end":34,"reference_id":"28879231","reference_source":"pmid","reference_html":"Homeodomain-like DNA binding proteins control the haploid-to-diploid transition in <i>Dictyostelium</i>. <i> Hedgethorne K, Eustermann S, Yang JC, Ogden TEH, Neuhaus D, Bloomfield G. </i> Sci Adv, 2017","date":"2026-03-30T16:34:00.764Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006285","ec_ontology":"ECO","ec_name":"magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"5NR6"},{"db":"BMRB","id":"34127"}],"region_id":"DP04410r003","statement":[{"text":"The plots for MatA and MatB share similar overall shapes, both showing high values of the NOE ratio for residues in a rigid core domain (approximately residues 35 to 80) and lower values in both N- and C-terminal tails.","type":"Results"},{"text":"We report that the nuclear magnetic resonance structures of two of them, MatA and MatB, contain helix-turn-helix folds flanked by largely disordered amino- and carboxyl-terminal tails.","type":"Abstract"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T16:34:13.041Z"}},{"start":81,"end":107,"reference_id":"28879231","reference_source":"pmid","reference_html":"Homeodomain-like DNA binding proteins control the haploid-to-diploid transition in <i>Dictyostelium</i>. <i> Hedgethorne K, Eustermann S, Yang JC, Ogden TEH, Neuhaus D, Bloomfield G. </i> Sci Adv, 2017","date":"2026-03-30T16:33:40.791Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006285","ec_ontology":"ECO","ec_name":"magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"5NR6"},{"db":"BMRB","id":"34127"}],"region_id":"DP04410r004","statement":[{"text":"The plots for MatA and MatB share similar overall shapes, both showing high values of the NOE ratio for residues in a rigid core domain (approximately residues 35 to 80) and lower values in both N- and C-terminal tails.\"","type":"Results"},{"text":"We report that the nuclear magnetic resonance structures of two of them, MatA and MatB, contain helix-turn-helix folds flanked by largely disordered amino- and carboxyl-terminal tails.","type":"Abstract"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T16:34:11.104Z"}}],"regions_counter":4,"released":"2026_06","sequence":"MDQLDEIIEQIQKEAINSNVVLKNPRVPTQKTGELSEEQKKIVADYISEVGLNNLNATELSKRLNITVDKSKTYIKNSNRMGRTNNFKTIKMFEDDVSSASAQPNLP","taxonomy":["Eukaryota","Amoebozoa","Evosea","Eumycetozoa","Dictyostelia","Dictyosteliales","Dictyosteliaceae","Dictyostelium"],"alphafold_very_low_content":0.19626168224299065,"disorder_content":0.5700934579439252,"disprot_consensus":{"full":[{"start":1,"end":34,"type":"D"},{"start":81,"end":107,"type":"D"}],"Structural state":[{"start":1,"end":34,"type":"D"},{"start":81,"end":107,"type":"D"}],"Disorder function":[{"start":1,"end":34,"type":"F"},{"start":81,"end":107,"type":"F"}]}},{"disprot_id":"DP04411","acc":"Q99181","creator":"viglesias","date":"2025-05-23T15:08:23.908Z","features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":11,"end":73},{"id":"PF00076","name":"RNA recognition motif","start":110,"end":178}],"gene3D":[]},"genes":[{"name":{"value":"HSH49"},"orfNames":[{"value":"O6142"}],"olnNames":[{"value":"YOR319W"}]}],"length":213,"name":"Protein HSH49","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":87,"end":105,"reference_id":"28348170","reference_source":"pmid","reference_html":"Crystal structure of U2 snRNP SF3b components: Hsh49p in complex with Cus1p-binding domain. <i> van Roon AM, Oubridge C, Obayashi E, Sposito B, Newman AJ, Séraphin B, Nagai K. </i> RNA, 2017","date":"2026-03-30T16:28:33.085Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"5LSB"}],"region_id":"DP04411r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q02554","statements":[{"type":"Results","text":"The Hsh49p–Cus1(290–368)p construct yielded small needle-like trigonal crystals, which diffracted to a maximum resolution of 2.7 Å"}]}],"statement":[{"text":"The refined model contains residues 8–86 of RRM1, 106–185 of RRM2, and residues 187–205 of a C-terminal extension of RRM2. No density was observed for the first seven residues of RRM1, the linker connecting RRM1 and RRM2 and the last eight C-terminal residues of Hsh49p. In the absence of density for the linker it is not possible to conclude which RRM1 and RRM2 in the crystal lattice are connected covalently","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T16:29:21.365Z"}},{"start":87,"end":105,"reference_id":"28348170","reference_source":"pmid","reference_html":"Crystal structure of U2 snRNP SF3b components: Hsh49p in complex with Cus1p-binding domain. <i> van Roon AM, Oubridge C, Obayashi E, Sposito B, Newman AJ, Séraphin B, Nagai K. </i> RNA, 2017","date":"2026-03-30T16:29:11.931Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"5LSB"}],"region_id":"DP04411r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q02554","statements":[{"type":"Results","text":"The Hsh49p–Cus1(290–368)p construct yielded small needle-like trigonal crystals, which diffracted to a maximum resolution of 2.7 Å"}]}],"statement":[{"text":"The refined model contains residues 8–86 of RRM1, 106–185 of RRM2, and residues 187–205 of a C-terminal extension of RRM2. No density was observed for the first seven residues of RRM1, the linker connecting RRM1 and RRM2 and the last eight C-terminal residues of Hsh49p. In the absence of density for the linker it is not possible to conclude which RRM1 and RRM2 in the crystal lattice are connected covalently","type":"Results"},{"text":"The distance between the C terminus of RRM1 and the N terminus of RRM2 of the closest pair within the asymmetric unit is 17–18 Å; to symmetry-related RRMs the distance is 30–39 Å. These distances can all be bridged by the disordered linker peptide so it is possible that a domain swap has occurred.","type":"Results"},{"text":"The flexible linker between RRM1 and RRM2 is about 20 amino acids long and should allow independent movement of the two RRMs, indicating that the relative orientation of both RRMs held together by the C-terminal helix in the crystal structure was indeed most likely due to crystal packing interactions.","type":"Results"},{"text":"Neither the disordered linker between RRM1 and RRM2 nor the C-terminal α-helix contribute to U2 snRNA oligo binding as Hsh49p–Cus1(290–368)p and RRM1–Cus1(290–368)p behave similarly in the fluorescence anisotropy experiments (Fig. 5E).","type":"Discussion"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T16:29:22.356Z"}}],"regions_counter":2,"released":"2026_06","sequence":"MNYSADSGNTVYVGNIDPRITKEQLYELFIQINPVLRIKYPKDKVLQAYQGYAFIEFYNQGDAQYAIKIMNNTVRLYDRLIKVRQVTNSTGTTNLPSNISKDMILPIAKLFIKNLADSIDSDQLVKIFNKFGKLIREPEIFYLSNGKLKCAYVYFEDFEKADLAIKSLNNQLVANNRITVDYAFKENGKGNAKYGDDVDRLLNKEALKHNMLK","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.107981220657277,"dataset":["RNA-binding proteins"],"disorder_content":0.0892018779342723,"disprot_consensus":{"full":[{"start":87,"end":105,"type":"D"}],"Structural state":[{"start":87,"end":105,"type":"D"}],"Disorder function":[{"start":87,"end":105,"type":"F"}]}},{"disprot_id":"DP04412","acc":"Q4QHJ8","creator":"viglesias","date":"2025-05-23T15:33:12.433Z","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":23,"end":319}],"gene3D":[]},"genes":[{"orfNames":[{"value":"LMJF_10_0200","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"CAJ02415.1","url":"https://www.ebi.ac.uk/ena/browser/view/CAJ02415.1"}}]}]}],"length":407,"name":"Putative mitogen-activated protein kinase","ncbi_taxon_id":5664,"organism":"Leishmania major","regions":[{"start":180,"end":194,"reference_id":"22884419","reference_source":"pmid","reference_html":"The crystal structure of the MAP kinase LmaMPK10 from Leishmania major reveals parasite-specific features and regulatory mechanisms. <i> Horjales S, Schmidt-Arras D, Limardo RR, Leclercq O, Obal G, Prina E, Turjanski AG, Späth GF, Buschiazzo A. </i> Structure, 2012","date":"2026-05-07T17:24:17.255Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"3PG1"}],"region_id":"DP04412r002","statement":[{"text":"Final electron density maps display excellent quality in the C-terminal lobe (see below for detailed structure description) (Figure 1A) and weaker signal to noise levels in the N-terminal lobe and particular segments. The model was built, including most of the amino acids, according to reliable electron density features, thus excluding the first 4 N-terminal residues, the last C-terminal one, and the zone spanning residues 180 to 194. The latter segment corresponds to the activation loop, and although electron density was visible, it was not sufficiently clear to allow for confident interpretation, instead suggesting high flexibility and/or the presence of alternative conformations that are not distinguishable at this resolution. ","type":"Results"},{"text":"Residue fragments 1–6, 17–24, 28–33, 57–63, 97–107, and 360–361 spanning solvent-exposed loops and β strands in the N-lobe domain, as well as the activation loop residues 180–191, could not be modeled because of a lack of interpretable electron density. The side chains of 19 residues, mostly belonging to the N-lobe domain, were not included in the model for the same reasons. The B factors of those parts of the N-lobe that do fit well in the electron density maps refine to extremely high values (Figure S4), revealing important flexibility of the molecule in this lobe. ","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-07T17:27:28.912Z"}},{"start":364,"end":407,"reference_id":"22884419","reference_source":"pmid","reference_html":"The crystal structure of the MAP kinase LmaMPK10 from Leishmania major reveals parasite-specific features and regulatory mechanisms. <i> Horjales S, Schmidt-Arras D, Limardo RR, Leclercq O, Obal G, Prina E, Turjanski AG, Späth GF, Buschiazzo A. </i> Structure, 2012","date":"2026-05-07T17:22:27.549Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04412r005","statement":[{"text":"Limited proteolysis and mass spectrometry analysis of LmaMPK10 confirmed the presence of a ∼40-residue C-terminal extension that is sensitive to proteolytic digestion, suggesting it might include an unstructured or more flexible segment.","type":"Results"}]},{"start":364,"end":407,"reference_id":"22884419","reference_source":"pmid","reference_html":"The crystal structure of the MAP kinase LmaMPK10 from Leishmania major reveals parasite-specific features and regulatory mechanisms. <i> Horjales S, Schmidt-Arras D, Limardo RR, Leclercq O, Obal G, Prina E, Turjanski AG, Späth GF, Buschiazzo A. </i> Structure, 2012","date":"2026-05-07T17:22:37.751Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007691","ec_ontology":"ECO","ec_name":"cleavage assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04412r006","statement":[{"text":"Limited proteolysis and mass spectrometry analysis of LmaMPK10 confirmed the presence of a ∼40-residue C-terminal extension that is sensitive to proteolytic digestion, suggesting it might include an unstructured or more flexible segment.","type":"Results"}]},{"start":189,"end":193,"reference_id":"22884419","reference_source":"pmid","reference_html":"The crystal structure of the MAP kinase LmaMPK10 from Leishmania major reveals parasite-specific features and regulatory mechanisms. <i> Horjales S, Schmidt-Arras D, Limardo RR, Leclercq O, Obal G, Prina E, Turjanski AG, Späth GF, Buschiazzo A. </i> Structure, 2012","date":"2026-05-07T17:33:06.293Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001582","ec_ontology":"ECO","ec_name":"liquid chromatography coupled with tandem mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04412r007","statement":[{"text":"LmaMPK10ΔC is able to use ATP to autophosphorylate specifically, needing a competent ePK-canonical architecture (i.e., Lys51 required to establish the salt bridge with Glu78). ","type":"Results"},{"text":"Phosphorylated variants of recombinant LmaMPK10 and LmaMPK10ΔC were identified by liquid chromatography-coupled electron spray mass spectrometry (Supplemental Experimental Procedures), after incubation with ATP (including both monophosphorylated variants on the THY motif of the activation loop), but this did not result in detectable increase of protein kinase activity (data not shown).","type":"Results"},{"text":"The phosphorylatable Thr190 and Tyr192 constituting the THY motif are seen embedded in a quite unusual context in LmaMPK10.","type":"Results"}]}],"regions_counter":7,"released":"2026_06","sequence":"MQAKGEAAMRDLIAELHAMQSPYTVQRFISSGSYGAVCAGVDSEGIPVAIKRVFNTVSDGRTVNILSDSFLCKRVLREIRLLNHFHHPNILGLRDIFVHFEEPAMHKLYLVTELMRTDLAQVIHDQRIVISPQHIQYFMYHILLGLHVLHEAGVVHRDLHPGNILLADNNDITICDFNLAREDTADANKTHYVTHRWYRAPELVMQFKGFTKLVDMWSAGCVMAEMFNRKALFRGSTFYNQLNKIVEVVGTPKIEDVVMFSSPSARDYLRNSLSNVPARAWTAVVPTADPVALDLIAKMLEFNPQRRISTEQALRHPYFESLFDPLDLTEGLSERFHFDESVTDVYDMHKIFTAEVERFNDLRERREEVARERAVAAQQQGEQVLGTDHMPRTHSLMELAGSAPAPS","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"alphafold_very_low_content":0.06388206388206388,"dataset":["Neglected tropical diseases proteins"],"disorder_content":0.14496314496314497,"disprot_consensus":{"full":[{"start":180,"end":194,"type":"D"},{"start":364,"end":407,"type":"D"}],"Structural state":[{"start":180,"end":194,"type":"D"},{"start":364,"end":407,"type":"D"}],"Disorder function":[{"start":189,"end":193,"type":"F"},{"start":364,"end":407,"type":"F"}]}},{"disprot_id":"DP04413","acc":"P61830","creator":"viglesias","date":"2025-05-25T15:23:42.057Z","features":{"pfam":[{"id":"PF00125","name":"Core histone H2A/H2B/H3/H4 domain","start":44,"end":131}],"gene3D":[]},"genes":[{"name":{"value":"HHT1"},"orfNames":[{"value":"YBR0201"}],"olnNames":[{"value":"YBR010W"}]},{"name":{"value":"HHT2"},"synonyms":[{"value":"SIN2"}],"orfNames":[{"value":"N2749"}],"olnNames":[{"value":"YNL031C"}]}],"length":136,"name":"Histone H3","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":38,"reference_id":"11566884","reference_source":"pmid","reference_html":"Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions. <i> White CL, Suto RK, Luger K. </i> EMBO J, 2001","date":"2026-05-07T17:05:34.151Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"1ID3"}],"region_id":"DP04413r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02309"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04911"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02294"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"The histone proteins were refolded to a histone octamer, and reconstituted into nucleosome core particles using a 146 bp palindromic DNA fragment derived from human α-satellite regions (Luger et al., 1997a)."},{"type":"Curator statement","text":"DNA with sequence: 5'-\nATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGGAAACTGCTCCATCAAAAGGCATGTTCAGCGGAATTCCGCTGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTGGTAGAATCTGCAGGTGGATATTGAT"}]}],"statement":[{"text":"cAtomic model: 757 amino acids (H2A, 15–124; H2A′, 12–119; H2B, 30–122; H2B′, 29–124; H3, 38–134; H3′, 38–134; H4, 24–102; H4′, 18–102), 60 water molecules and 17 manganese ions (a total of 12 129 atoms). The remainder of the histone tails was too disordered to be included in the final model.","type":"Figure"},{"text":"However, the histone tails quickly become disordered as they extend past the DNA superhelix.","type":"Results"},{"text":"We show for the first time that the H4 N-terminal tail can assume completely different conformations depending upon the structural context. We have evidence that this holds true for all histone tails (unpublished data). This structural heterogeneity might allow the histone tails to interact with a variety of different protein factors and to perform a large number of different functions (Hansen et al., 1998).","type":"Discussion"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-07T17:06:53.059Z"}},{"start":1,"end":38,"reference_id":"11566884","reference_source":"pmid","reference_html":"Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions. <i> White CL, Suto RK, Luger K. </i> EMBO J, 2001","date":"2026-05-07T17:06:29.957Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"1ID3"}],"region_id":"DP04413r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02309"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04911"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02294"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"The histone proteins were refolded to a histone octamer, and reconstituted into nucleosome core particles using a 146 bp palindromic DNA fragment derived from human α-satellite regions (Luger et al., 1997a)."},{"type":"Curator statement","text":"DNA with sequence: 5'-\nATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGGAAACTGCTCCATCAAAAGGCATGTTCAGCGGAATTCCGCTGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTGGTAGAATCTGCAGGTGGATATTGAT"}]}],"statement":[{"text":"cAtomic model: 757 amino acids (H2A, 15–124; H2A′, 12–119; H2B, 30–122; H2B′, 29–124; H3, 38–134; H3′, 38–134; H4, 24–102; H4′, 18–102), 60 water molecules and 17 manganese ions (a total of 12 129 atoms). The remainder of the histone tails was too disordered to be included in the final model.","type":"Figure"},{"text":"We show for the first time that the H4 N-terminal tail can assume completely different conformations depending upon the structural context. We have evidence that this holds true for all histone tails (unpublished data). This structural heterogeneity might allow the histone tails to interact with a variety of different protein factors and to perform a large number of different functions (Hansen et al., 1998).","type":"Discussion"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-07T17:06:51.492Z"}}],"regions_counter":2,"released":"2026_06","sequence":"MARTKQTARKSTGGKAPRKQLASKAARKSAPSTGGVKKPHRYKPGTVALREIRRFQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQESVEAYLVSLFEDTNLAAIHAKRVTIQKKDIKLARRLRGERS","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.014705882352941176,"disorder_content":0.27941176470588236,"disprot_consensus":{"full":[{"start":1,"end":38,"type":"D"}],"Structural state":[{"start":1,"end":38,"type":"D"}],"Disorder function":[{"start":1,"end":38,"type":"F"}]}},{"disprot_id":"DP04414","acc":"P04911","creator":"viglesias","date":"2025-05-25T15:51:19.401Z","features":{"pfam":[{"id":"PF00125","name":"Core histone H2A/H2B/H3/H4 domain","start":9,"end":90},{"id":"PF16211","name":"C-terminus of histone H2A","start":93,"end":127}],"gene3D":[]},"genes":[{"name":{"value":"HTA1"},"synonyms":[{"value":"H2A1"},{"value":"SPT11"}],"orfNames":[{"value":"YD9934.10"}],"olnNames":[{"value":"YDR225W"}]}],"length":132,"name":"Histone H2A.1","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":11,"reference_id":"11566884","reference_source":"pmid","reference_html":"Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions. <i> White CL, Suto RK, Luger K. </i> EMBO J, 2001","date":"2026-05-07T16:56:50.597Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"1ID3"}],"region_id":"DP04414r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61830"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02309"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02294"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"The histone proteins were refolded to a histone octamer, and reconstituted into nucleosome core particles using a 146 bp palindromic DNA fragment derived from human α-satellite regions (Luger et al., 1997a)."},{"type":"Curator statement","text":"DNA with sequence: 5'-\nATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGGAAACTGCTCCATCAAAAGGCATGTTCAGCGGAATTCCGCTGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTGGTAGAATCTGCAGGTGGATATTGAT"}]}],"statement":[{"text":"cAtomic model: 757 amino acids (H2A, 15–124; H2A′, 12–119; H2B, 30–122; H2B′, 29–124; H3, 38–134; H3′, 38–134; aH4, 24–102; H4′, 18–102), 60 water molecules and 17 manganese ions (a total of 12 129 atoms). The remainder of the histone tails was too disordered to be included in the final model.","type":"Figure"},{"text":"However, the histone tails quickly become disordered as they extend past the DNA superhelix.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-07T16:57:04.990Z"}},{"start":1,"end":11,"reference_id":"11566884","reference_source":"pmid","reference_html":"Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions. <i> White CL, Suto RK, Luger K. </i> EMBO J, 2001","date":"2026-05-07T16:54:17.190Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":3,"cross_refs":[{"db":"PDB","id":"1ID3"}],"region_id":"DP04414r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61830"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02309"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02294"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"The histone proteins were refolded to a histone octamer, and reconstituted into nucleosome core particles using a 146 bp palindromic DNA fragment derived from human α-satellite regions (Luger et al., 1997a)."},{"type":"Curator statement","text":"DNA with sequence: 5'-\nATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGGAAACTGCTCCATCAAAAGGCATGTTCAGCGGAATTCCGCTGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTGGTAGAATCTGCAGGTGGATATTGAT"}]}],"statement":[{"text":"cAtomic model: 757 amino acids (H2A, 15–124; H2A′, 12–119; H2B, 30–122; H2B′, 29–124; H3, 38–134; H3′, 38–134; aH4, 24–102; H4′, 18–102), 60 water molecules and 17 manganese ions (a total of 12 129 atoms). The remainder of the histone tails was too disordered to be included in the final model.","type":"Figure"},{"text":"However, the histone tails quickly become disordered as they extend past the DNA superhelix.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-07T16:54:28.286Z"}},{"start":122,"end":132,"reference_id":"11566884","reference_source":"pmid","reference_html":"Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions. <i> White CL, Suto RK, Luger K. </i> EMBO J, 2001","date":"2026-05-07T16:55:31.300Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"1ID3"}],"region_id":"DP04414r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61830"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02309"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02294"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"The histone proteins were refolded to a histone octamer, and reconstituted into nucleosome core particles using a 146 bp palindromic DNA fragment derived from human α-satellite regions (Luger et al., 1997a)."},{"type":"Curator statement","text":"DNA with sequence: 5'-\nATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGGAAACTGCTCCATCAAAAGGCATGTTCAGCGGAATTCCGCTGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTGGTAGAATCTGCAGGTGGATATTGAT"}]}],"statement":[{"text":"cAtomic model: 757 amino acids (H2A, 15–124; H2A′, 12–119; H2B, 30–122; H2B′, 29–124; H3, 38–134; H3′, 38–134; aH4, 24–102; H4′, 18–102), 60 water molecules and 17 manganese ions (a total of 12 129 atoms). The remainder of the histone tails was too disordered to be included in the final model.","type":"Figure"},{"text":"However, the histone tails quickly become disordered as they extend past the DNA superhelix.","type":"Results"},{"text":"We show for the first time that the H4 N-terminal tail can assume completely different conformations depending upon the structural context. We have evidence that this holds true for all histone tails (unpublished data). This structural heterogeneity might allow the histone tails to interact with a variety of different protein factors and to perform a large number of different functions (Hansen et al., 1998).","type":"Discussion"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-07T16:57:01.000Z"}},{"start":122,"end":132,"reference_id":"11566884","reference_source":"pmid","reference_html":"Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions. <i> White CL, Suto RK, Luger K. </i> EMBO J, 2001","date":"2026-05-07T16:59:51.197Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":4,"cross_refs":[{"db":"PDB","id":"1ID3"}],"region_id":"DP04414r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61830"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02309"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02294"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"The histone proteins were refolded to a histone octamer, and reconstituted into nucleosome core particles using a 146 bp palindromic DNA fragment derived from human α-satellite regions (Luger et al., 1997a)."},{"type":"Curator statement","text":"DNA with sequence: 5'-\nATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGGAAACTGCTCCATCAAAAGGCATGTTCAGCGGAATTCCGCTGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTGGTAGAATCTGCAGGTGGATATTGAT"}]}],"statement":[{"text":"cAtomic model: 757 amino acids (H2A, 15–124; H2A′, 12–119; H2B, 30–122; H2B′, 29–124; H3, 38–134; H3′, 38–134; aH4, 24–102; H4′, 18–102), 60 water molecules and 17 manganese ions (a total of 12 129 atoms). The remainder of the histone tails was too disordered to be included in the final model.","type":"Figure"},{"text":"However, the histone tails quickly become disordered as they extend past the DNA superhelix.","type":"Results"},{"text":"We show for the first time that the H4 N-terminal tail can assume completely different conformations depending upon the structural context. We have evidence that this holds true for all histone tails (unpublished data). This structural heterogeneity might allow the histone tails to interact with a variety of different protein factors and to perform a large number of different functions (Hansen et al., 1998).","type":"Discussion"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-07T17:01:02.532Z"}}],"regions_counter":4,"released":"2026_06","sequence":"MSGGKGGKAGSAAKASQSRSAKAGLTFPVGRVHRLLRRGNYAQRIGSGAPVYLTAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDDELNKLLGNVTIAQGGVLPNIHQNLLPKKSAKATKASQEL","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.015151515151515152,"disorder_content":0.16666666666666666,"disprot_consensus":{"full":[{"start":1,"end":11,"type":"D"},{"start":122,"end":132,"type":"D"}],"Structural state":[{"start":1,"end":11,"type":"D"},{"start":122,"end":132,"type":"D"}],"Disorder function":[{"start":1,"end":11,"type":"F"},{"start":122,"end":132,"type":"F"}]}},{"disprot_id":"DP04415","acc":"P02294","creator":"viglesias","date":"2025-05-25T16:00:34.879Z","features":{"pfam":[{"id":"PF00125","name":"Core histone H2A/H2B/H3/H4 domain","start":31,"end":104}],"gene3D":[]},"genes":[{"name":{"value":"HTB2"},"synonyms":[{"value":"H2B2"}],"orfNames":[{"value":"YBL0104"}],"olnNames":[{"value":"YBL002W"}]}],"length":131,"name":"Histone H2B.2","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":1,"end":35,"reference_id":"11566884","reference_source":"pmid","reference_html":"Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions. <i> White CL, Suto RK, Luger K. </i> EMBO J, 2001","date":"2026-05-07T17:03:06.683Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":5,"cross_refs":[{"db":"PDB","id":"1ID3"}],"region_id":"DP04415r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02309"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61830"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04911"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"The histone proteins were refolded to a histone octamer, and reconstituted into nucleosome core particles using a 146 bp palindromic DNA fragment derived from human α-satellite regions (Luger et al., 1997a)."},{"type":"Curator statement","text":"DNA with sequence: 5'-\nATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGGAAACTGCTCCATCAAAAGGCATGTTCAGCGGAATTCCGCTGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTGGTAGAATCTGCAGGTGGATATTGAT"}]}],"statement":[{"text":"cAtomic model: 757 amino acids (H2A, 15–124; H2A′, 12–119; H2B, 30–122; H2B′, 29–124; H3, 38–134; H3′, 38–134; aH4, 24–102; H4′, 18–102), 60 water molecules and 17 manganese ions (a total of 12 129 atoms). The remainder of the histone tails was too disordered to be included in the final model.","type":"Figure"},{"text":"However, the histone tails quickly become disordered as they extend past the DNA superhelix.","type":"Results"},{"text":"We show for the first time that the H4 N-terminal tail can assume completely different conformations depending upon the structural context. We have evidence that this holds true for all histone tails (unpublished data). This structural heterogeneity might allow the histone tails to interact with a variety of different protein factors and to perform a large number of different functions (Hansen et al., 1998).","type":"Discussion"},{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-07T17:03:18.762Z"}},{"start":1,"end":35,"reference_id":"11566884","reference_source":"pmid","reference_html":"Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions. <i> White CL, Suto RK, Luger K. </i> EMBO J, 2001","date":"2026-05-07T17:03:15.000Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":3,"cross_refs":[{"db":"PDB","id":"1ID3"}],"region_id":"DP04415r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P02309"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P61830"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04911"},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"The histone proteins were refolded to a histone octamer, and reconstituted into nucleosome core particles using a 146 bp palindromic DNA fragment derived from human α-satellite regions (Luger et al., 1997a)."},{"type":"Curator statement","text":"DNA with sequence: 5'-\nATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGGAAACTGCTCCATCAAAAGGCATGTTCAGCGGAATTCCGCTGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTGGTAGAATCTGCAGGTGGATATTGAT"}]}],"statement":[{"text":"cAtomic model: 757 amino acids (H2A, 15–124; H2A′, 12–119; H2B, 30–122; H2B′, 29–124; H3, 38–134; H3′, 38–134; aH4, 24–102; H4′, 18–102), 60 water molecules and 17 manganese ions (a total of 12 129 atoms). The remainder of the histone tails was too disordered to be included in the final model.","type":"Figure"},{"text":"However, the histone tails quickly become disordered as they extend past the DNA superhelix.","type":"Results"},{"text":"We show for the first time that the H4 N-terminal tail can assume completely different conformations depending upon the structural context. We have evidence that this holds true for all histone tails (unpublished data). This structural heterogeneity might allow the histone tails to interact with a variety of different protein factors and to perform a large number of different functions (Hansen et al., 1998).","type":"Discussion"},{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-07T17:03:17.654Z"}}],"regions_counter":2,"released":"2026_06","sequence":"MSSAAEKKPASKAPAEKKPAAKKTSTSVDGKKRSKVRKETYSSYIYKVLKQTHPDTGISQKSMSILNSFVNDIFERIATEASKLAAYNKKSTISAREIQTAVRLILPGELAKHAVSEGTRAVTKYSSSTQA","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.17557251908396945,"disorder_content":0.26717557251908397,"disprot_consensus":{"full":[{"start":1,"end":35,"type":"D"}],"Structural state":[{"start":1,"end":35,"type":"D"}],"Disorder function":[{"start":1,"end":35,"type":"F"}]}},{"disprot_id":"DP04416","acc":"O53692","creator":"vnugnes","date":"2025-06-04T16:55:31.618Z","features":{"pfam":[{"id":"PF06013","name":"Proteins of 100 residues with WXG","start":10,"end":87}],"gene3D":[]},"genes":[{"name":{"value":"esxG","evidences":[{"code":"ECO:0000303","source":{"name":"PubMed","id":"15336430","url":"http://www.ncbi.nlm.nih.gov/pubmed/15336430","alternativeUrl":"https://europepmc.org/abstract/MED/15336430"}},{"code":"ECO:0000303","source":{"name":"PubMed","id":"19876390","url":"http://www.ncbi.nlm.nih.gov/pubmed/19876390","alternativeUrl":"https://europepmc.org/abstract/MED/19876390"}}]},"olnNames":[{"value":"Rv0287","evidences":[{"code":"ECO:0000312","source":{"name":"EMBL","id":"CCP43017.1","url":"https://www.ebi.ac.uk/ena/browser/view/CCP43017.1"}}]}]}],"length":97,"name":"ESAT-6-like protein EsxG","ncbi_taxon_id":83332,"organism":"Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)","regions":[{"start":1,"end":14,"reference_id":"21730061","reference_source":"pmid","reference_html":"Solution structure of the Mycobacterium tuberculosis EsxG·EsxH complex: functional implications and comparisons with other M. tuberculosis Esx family complexes. <i> Ilghari D, Lightbody KL, Veverka V, Waters LC, Muskett FW, Renshaw PS, Carr MD. </i> J Biol Chem, 2011","date":"2025-06-04T16:57:58.889Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"2KG7"}],"region_id":"DP04416r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P9WNK3"}],"statement":[{"text":"The core of the complex is well defined (residues 15–79 in EsxG and 17–75 in EsxH), although there appears to be significant flexibility in the hairpin loop of EsxG (residues 40–47) as well as the N and C termini of EsxG and EsxH, which form flexible arms at both ends of the complex (Fig. 1).","type":"Results"}]},{"start":1,"end":14,"reference_id":"21730061","reference_source":"pmid","reference_html":"Solution structure of the Mycobacterium tuberculosis EsxG·EsxH complex: functional implications and comparisons with other M. tuberculosis Esx family complexes. <i> Ilghari D, Lightbody KL, Veverka V, Waters LC, Muskett FW, Renshaw PS, Carr MD. </i> J Biol Chem, 2011","date":"2025-06-04T16:58:08.434Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"2KG7"}],"region_id":"DP04416r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P9WNK3"}],"statement":[{"text":"The core of the complex is well defined (residues 15–79 in EsxG and 17–75 in EsxH), although there appears to be significant flexibility in the hairpin loop of EsxG (residues 40–47) as well as the N and C termini of EsxG and EsxH, which form flexible arms at both ends of the complex (Fig. 1).","type":"Results"}]},{"start":80,"end":97,"reference_id":"21730061","reference_source":"pmid","reference_html":"Solution structure of the Mycobacterium tuberculosis EsxG·EsxH complex: functional implications and comparisons with other M. tuberculosis Esx family complexes. <i> Ilghari D, Lightbody KL, Veverka V, Waters LC, Muskett FW, Renshaw PS, Carr MD. </i> J Biol Chem, 2011","date":"2025-06-04T16:58:24.860Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"2KG7"}],"region_id":"DP04416r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P9WNK3"}],"statement":[{"text":"The core of the complex is well defined (residues 15–79 in EsxG and 17–75 in EsxH), although there appears to be significant flexibility in the hairpin loop of EsxG (residues 40–47) as well as the N and C termini of EsxG and EsxH, which form flexible arms at both ends of the complex (Fig. 1).","type":"Results"}]},{"start":80,"end":97,"reference_id":"21730061","reference_source":"pmid","reference_html":"Solution structure of the Mycobacterium tuberculosis EsxG·EsxH complex: functional implications and comparisons with other M. tuberculosis Esx family complexes. <i> Ilghari D, Lightbody KL, Veverka V, Waters LC, Muskett FW, Renshaw PS, Carr MD. </i> J Biol Chem, 2011","date":"2025-06-04T16:58:32.884Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2025_06","version":0,"cross_refs":[{"db":"PDB","id":"2KG7"}],"region_id":"DP04416r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P9WNK3"}],"statement":[{"text":"The core of the complex is well defined (residues 15–79 in EsxG and 17–75 in EsxH), although there appears to be significant flexibility in the hairpin loop of EsxG (residues 40–47) as well as the N and C termini of EsxG and EsxH, which form flexible arms at both ends of the complex (Fig. 1).","type":"Results"}]}],"regions_counter":4,"released":"2025_06","sequence":"MSLLDAHIPQLVASQSAFAAKAGLMRHTIGQAEQAAMSAQAFHQGESSAAFQAAHARFVAAAAKVNTLLDVAQANLGEAAGTYVAADAAAASTYTGF","taxonomy":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium tuberculosis complex"],"alphafold_very_low_content":0.010309278350515464,"dataset":["Bacterial virulence-related proteins"],"disorder_content":0.32989690721649484,"disprot_consensus":{"full":[{"start":1,"end":14,"type":"D"},{"start":80,"end":97,"type":"D"}],"Structural state":[{"start":1,"end":14,"type":"D"},{"start":80,"end":97,"type":"D"}],"Disorder function":[{"start":1,"end":14,"type":"F"},{"start":80,"end":97,"type":"F"}]}},{"disprot_id":"DP04419","acc":"Q9UQF2","creator":"zskalman","date":"2025-06-18T17:58:33.378Z","features":{"pfam":[{"id":"PF00640","name":"Phosphotyrosine interaction domain (PTB/PID)","start":567,"end":700},{"id":"PF14604","name":"Variant SH3 domain","start":495,"end":543}],"gene3D":[]},"genes":[{"name":{"value":"MAPK8IP1"},"synonyms":[{"value":"IB1"},{"value":"JIP1"},{"value":"PRKM8IP"}]}],"length":711,"name":"C-Jun-amino-terminal kinase-interacting protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":145,"reference_id":"39999166","reference_source":"pmid","reference_html":"Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1. <i> Orand T, Delaforge E, Lee A, Kragelj J, Tengo M, Tengo L, Blackledge M, Boeri Erba E, Davis RJ, Palencia A, Jensen MR. </i> Proc Natl Acad Sci U S A, 2025","date":"2025-06-21T12:27:17.292Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"BMRB","id":"52858"}],"region_id":"DP04419r001","statement":[{"text":"The data therefore show that the JIP1 IDR is predominantly disordered with interspersed secondary structure elements of modest propensity.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-26T19:29:24.371Z"}},{"start":116,"end":266,"reference_id":"39999166","reference_source":"pmid","reference_html":"Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1. <i> Orand T, Delaforge E, Lee A, Kragelj J, Tengo M, Tengo L, Blackledge M, Boeri Erba E, Davis RJ, Palencia A, Jensen MR. </i> Proc Natl Acad Sci U S A, 2025","date":"2026-03-26T19:29:45.796Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"BMRB","id":"52859"}],"region_id":"DP04419r002","statement":[{"text":"The data therefore show that the JIP1 IDR is predominantly disordered with interspersed secondary structure elements of modest propensity.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-26T19:29:59.039Z"}},{"start":245,"end":372,"reference_id":"39999166","reference_source":"pmid","reference_html":"Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1. <i> Orand T, Delaforge E, Lee A, Kragelj J, Tengo M, Tengo L, Blackledge M, Boeri Erba E, Davis RJ, Palencia A, Jensen MR. </i> Proc Natl Acad Sci U S A, 2025","date":"2026-03-26T19:30:38.535Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"BMRB","id":"52860"}],"region_id":"DP04419r003","statement":[{"text":"The data therefore show that the JIP1 IDR is predominantly disordered with interspersed secondary structure elements of modest propensity.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-26T19:31:20.748Z"}},{"start":353,"end":553,"reference_id":"39999166","reference_source":"pmid","reference_html":"Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1. <i> Orand T, Delaforge E, Lee A, Kragelj J, Tengo M, Tengo L, Blackledge M, Boeri Erba E, Davis RJ, Palencia A, Jensen MR. </i> Proc Natl Acad Sci U S A, 2025","date":"2026-03-26T19:31:15.065Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"BMRB","id":"52861"}],"region_id":"DP04419r004","statement":[{"text":"The data therefore show that the JIP1 IDR is predominantly disordered with interspersed secondary structure elements of modest propensity.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-26T19:37:06.665Z"}},{"start":157,"end":170,"reference_id":"39999166","reference_source":"pmid","reference_html":"Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1. <i> Orand T, Delaforge E, Lee A, Kragelj J, Tengo M, Tengo L, Blackledge M, Boeri Erba E, Davis RJ, Palencia A, Jensen MR. </i> Proc Natl Acad Sci U S A, 2025","date":"2026-03-31T13:20:52.231Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"GO:0051019","term_name":"mitogen-activated protein kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"9FT9"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P45983","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04419r005","term_comment":"","term_def":"\"Binding to a mitogen-activated protein kinase.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"statement":[{"text":"The D- and F-motifs of JIP1 are well defined in the electron density (Fig. 5 C and D), however, the linker connecting the two motifs (16 residues in length in the construct used for X-ray crystallography) is not visible suggesting that it remains flexible and samples multiple conformations in complex with JNK1.","type":"Results"},{"text":"The D-motif adopts a conformation similar to previously solved crystal structures (19) with both electrostatic (Fig. 5 A, Left) and hydrophobic (Fig. 5 B, Left) binding features characteristic of canonical DRS/D-motif interactions (25).","type":"Results"}],"sequence_construct":"RPKRPTTLNLFPQVPRSQDKHSWQDRVSRSICLSDELP","construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Thr176_Lys184del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To obtain diffracting crystals, the linker between the D- and F-motifs was shortened to reduce flexibility following an NMR-guided approach (SI Appendix, Fig. S11)."}]},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ser196_His210del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To obtain diffracting crystals, the linker between the D- and F-motifs was shortened to reduce flexibility following an NMR-guided approach (SI Appendix, Fig. S11)."}]}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"47785","entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-31T13:24:13.319Z"}},{"start":211,"end":218,"reference_id":"39999166","reference_source":"pmid","reference_html":"Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1. <i> Orand T, Delaforge E, Lee A, Kragelj J, Tengo M, Tengo L, Blackledge M, Boeri Erba E, Davis RJ, Palencia A, Jensen MR. </i> Proc Natl Acad Sci U S A, 2025","date":"2026-03-31T13:21:09.711Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"GO:0051019","term_name":"mitogen-activated protein kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"9FT9"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P45983","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04419r006","term_comment":"","term_def":"\"Binding to a mitogen-activated protein kinase.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"sequence_construct":"RPKRPTTLNLFPQVPRSQDKHSWQDRVSRSICLSDELP","statement":[{"text":"The D- and F-motifs of JIP1 are well defined in the electron density (Fig. 5 C and D), however, the linker connecting the two motifs (16 residues in length in the construct used for X-ray crystallography) is not visible suggesting that it remains flexible and samples multiple conformations in complex with JNK1.","type":"Results"},{"text":"The F-motif binds to the FRS and folds into a single helical turn upon binding to JNK1 consistent with the NMR relaxation dispersion data (Fig. 3 G–J).","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Thr176_Lys184del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To obtain diffracting crystals, the linker between the D- and F-motifs was shortened to reduce flexibility following an NMR-guided approach (SI Appendix, Fig. S11)."}]},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ser196_His210del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To obtain diffracting crystals, the linker between the D- and F-motifs was shortened to reduce flexibility following an NMR-guided approach (SI Appendix, Fig. S11)."}]}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"47785","entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-31T13:24:11.453Z"}},{"start":171,"end":209,"reference_id":"39999166","reference_source":"pmid","reference_html":"Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1. <i> Orand T, Delaforge E, Lee A, Kragelj J, Tengo M, Tengo L, Blackledge M, Boeri Erba E, Davis RJ, Palencia A, Jensen MR. </i> Proc Natl Acad Sci U S A, 2025","date":"2026-03-31T13:23:52.224Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"region_id":"DP04419r007","statement":[{"text":"Our work highlights how MAPKs can exploit multiple motifs, even separated by long disordered linkers, for binding to their interaction partners.","type":"Abstract"},{"text":"Collectively, our data demonstrate that JNK1 binds to two separate motifs on the JIP1116–266 sequence with the intervening linker being dynamically restricted as evidenced by the simultaneous drop in signal intensities throughout the region encompassing residues 155 to 220.","type":"Results"},{"text":"The recruitment of JNK1 to JIP1 occurs through the high-affinity D-motif and a “locking in” of the F-motif into the FRS. The positioning of the F-motif is guided by the linker between the D- and F-motifs ensuring a high local effective concentration of the F-motif near the FRS.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-31T13:24:15.386Z"}},{"start":157,"end":167,"reference_id":"39999166","reference_source":"pmid","reference_html":"Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1. <i> Orand T, Delaforge E, Lee A, Kragelj J, Tengo M, Tengo L, Blackledge M, Boeri Erba E, Davis RJ, Palencia A, Jensen MR. </i> Proc Natl Acad Sci U S A, 2025","date":"2026-03-30T20:22:04.899Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051019","term_name":"mitogen-activated protein kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P45983","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04419r008","statement":[{"text":"JIP1116–266 shows extensive intensity loss of all resonances from residues 155 to 220 (Fig. 2 A and B), without displaying significant chemical shift perturbations (SI Appendix, Fig. S4A). Surprisingly, the observed intensity loss extends well beyond the D-motif (located at residues 157 to 167) suggesting the presence of additional JNK1-binding features on the JIP1 scaffold.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a mitogen-activated protein kinase.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false},{"start":211,"end":217,"reference_id":"39999166","reference_source":"pmid","reference_html":"Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1. <i> Orand T, Delaforge E, Lee A, Kragelj J, Tengo M, Tengo L, Blackledge M, Boeri Erba E, Davis RJ, Palencia A, Jensen MR. </i> Proc Natl Acad Sci U S A, 2025","date":"2026-03-30T20:28:31.498Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051019","term_name":"mitogen-activated protein kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P45983","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04419r009","statement":[{"text":"Surprisingly, the observed intensity loss extends well beyond the D-motif (located at residues 157 to 167) suggesting the presence of additional JNK1-binding features on the JIP1 scaffold.","type":"Results"},{"text":"The R1ρ relaxation rates only increase slightly for residues within the D-motif and more significantly at a second site (residues 205 to 220) located C-terminal to the D-motif.","type":"Results"},{"text":"Authors define a second binding site, noncanonical F-motif at region 211-217.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a mitogen-activated protein kinase.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":211,"end":217,"reference_id":"39999166","reference_source":"pmid","reference_html":"Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1. <i> Orand T, Delaforge E, Lee A, Kragelj J, Tengo M, Tengo L, Blackledge M, Boeri Erba E, Davis RJ, Palencia A, Jensen MR. </i> Proc Natl Acad Sci U S A, 2025","date":"2026-03-31T12:43:26.134Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051019","term_name":"mitogen-activated protein kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile211Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu213Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu217Ala","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P45983","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04419r010","statement":[{"text":"A simultaneous mutation of both I211 and L213 to alanine (hereafter named the IL mutant), completely abolished binding of JNK1 as evidenced from the absence of line broadening within the second motif upon addition of JNK1 (Fig. 2E). These results clearly show that binding of JNK1 at the second site is hydrophobically driven and identify either I211 and/or L213 as crucial residues for the interaction.","type":"Results"},{"text":"We evaluated the impact on JNK1 binding of three single point mutations (I211A, L213A, and L217A) in the F-motif of JIP1. Our results show that L213A and L217A impair the interaction, while I211A does not impact the binding to JNK1 (SI Appendix, Fig. S14). Nevertheless, full abrogation of the JNK1–JIP1 F-motif interaction is achieved with the double mutant I211A/L213A (Fig. 2E) suggesting that I211 also contributes to the interaction in the presence of L213.","type":"Results"},{"text":"Collectively, our results demonstrate that the second site should be characterized as a noncanonical F-motif, given the absence of phenylalanine residues within the motif sequence.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a mitogen-activated protein kinase.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":160,"end":166,"reference_id":"39999166","reference_source":"pmid","reference_html":"Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1. <i> Orand T, Delaforge E, Lee A, Kragelj J, Tengo M, Tengo L, Blackledge M, Boeri Erba E, Davis RJ, Palencia A, Jensen MR. </i> Proc Natl Acad Sci U S A, 2025","date":"2026-03-31T12:43:09.406Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051019","term_name":"mitogen-activated protein kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"construct_alterations":[{"term_id":"IDPO:00484","term_name":"deletion-insertion","term_namespace":"Protein mutation","value":"p.Arg160_Leu166AladelinsGlnAlaThrThrAlaAspAla","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P45983","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04419r011","statement":[{"text":"Next, we abolished binding to the canonical D-motif through the introduction of four single point mutations (R160E, P161A, L164A, L166A, hereafter named the RPLL mutant) (50). JNK1-binding to the D-motif was efficiently abrogated as shown by the absence of intensity loss within the D-motif upon addition of JNK1 (Fig. 2F). Binding was, however, still observed to the second site showing that it can interact with JNK1 independently of the D-motif (Fig. 2F and SI Appendix, Fig. S4B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a mitogen-activated protein kinase.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":157,"end":167,"reference_id":"39999166","reference_source":"pmid","reference_html":"Bipartite binding of the intrinsically disordered scaffold protein JIP1 to the kinase JNK1. <i> Orand T, Delaforge E, Lee A, Kragelj J, Tengo M, Tengo L, Blackledge M, Boeri Erba E, Davis RJ, Palencia A, Jensen MR. </i> Proc Natl Acad Sci U S A, 2025","date":"2026-03-31T12:43:49.830Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051019","term_name":"mitogen-activated protein kinase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P45983","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04419r012","sequence_construct":"RPKRPTTLNLF","statement":[{"text":"The ITC experiments show that the D-motif peptide binds with a Kd of 217 nM to JNK1 (Fig. 3A), while JIP1116–266 shows a 2.7-fold higher affinity (Kd = 81 nM, Fig. 3B).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a mitogen-activated protein kinase.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false}],"regions_counter":12,"released":"2026_06","sequence":"MAERESGGLGGGAASPPAASPFLGLHIASPPNFRLTHDISLEEFEDEDLSEITDECGISLQCKDTLSLRPPRAGLLSAGGGGAGSRLQAEMLQMDLIDATGDTPGAEDDEEDDDEERAARRPGAGPPKAESGQEPASRGQGQSQGQSQGPGSGDTYRPKRPTTLNLFPQVPRSQDTLNNNSLGKKHSWQDRVSRSSSPLKTGEQTPPHEHICLSDELPPQSGPAPTTDRGTSTDSPCRRSTATQMAPPGGPPAAPPGGRGHSHRDRIHYQADVRLEATEEIYLTPVQRPPDAAEPTSAFLPPTESRMSVSSDPDPAAYPSTAGRPHPSISEEEEGFDCLSSPERAEPPGGGWRGSLGEPPPPPRASLSSDTSALSYDSVKYTLVVDEHAQLELVSLRPCFGDYSDESDSATVYDNCASVSSPYESAIGEEYEEAPRPQPPACLSEDSTPDEPDVHFSKKFLNVFMSGRSRSSSAESFGLFSCIINGEEQEQTHRAIFRFVPRHEDELELEVDDPLLVELQAEDYWYEAYNMRTGARGVFPAYYAIEVTKEPEHMAALAKNSDWVDQFRVKFLGSVQVPYHKGNDVLCAAMQKIATTRRLTVHFNPPSSCVLEISVRGVKIGVKADDSQEAKGNKCSHFFQLKNISFCGYHPKNNKYFGFITKHPADHRFACHVFVSEDSTKALAESVGRAFQQFYKQFVEYTCPTEDIYLE","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.6638537271448663,"dataset":["Autophagy-related proteins"],"disorder_content":0.7777777777777778,"disprot_consensus":{"full":[{"start":1,"end":553,"type":"D"}],"Structural state":[{"start":1,"end":553,"type":"D"}],"Molecular function":[{"start":157,"end":170,"type":"F"},{"start":211,"end":218,"type":"F"}],"Disorder function":[{"start":171,"end":209,"type":"F"}]}},{"disprot_id":"DP04420","acc":"Q9Y216","creator":"zskalman","date":"2025-06-21T11:46:43.976Z","features":{"pfam":[{"id":"PF06602","name":"Myotubularin-like phosphatase domain","start":109,"end":448},{"id":"PF21098","name":"MTMR6-9, GRAM domain","start":8,"end":100}],"gene3D":[]},"genes":[{"name":{"value":"MTMR7","evidences":[{"code":"ECO:0000312","source":{"name":"HGNC","id":"HGNC:7454","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:7454"}}]}}],"length":660,"name":"Phosphatidylinositol-3-phosphate phosphatase MTMR7","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":514,"end":554,"reference_id":"38462034","reference_source":"pmid","reference_html":"Myotubularin-related-protein-7 inhibits mutant (G12V) K-RAS by direct interaction. <i> Weidner P, Saar D, Söhn M, Schroeder T, Yu Y, Zöllner FG, Ponelies N, Zhou X, Zwicky A, Rohrbacher FN, Pattabiraman VR, Tanriver M, Bauer A, Ahmed H, Ametamey SM, Riffel P, Seger R, Bode JW, Wade RC, Ebert MPA, Kragelund BB, Burgermeister E. </i> Cancer Lett, 2024","date":"2026-06-17T13:59:17.411Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"region_id":"DP04420r001","statement":[{"text":"The increase in helicity observed in CD, along with the reduction of NMR peak intensities, suggested that the M7-CC domain formed concentration-dependent oligomers of higher helicity than the disordered monomers.","type":"Results"}],"sequence_construct":"RQSWTDYLMAVKEETQQLEEELEALEERLEKIQKVQLNCTK","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val518Trp","start":null,"end":null,"position":null}],"cross_refs":[{"db":"BMRB","id":"52269"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-17T13:59:24.702Z"}},{"start":521,"end":550,"reference_id":"38462034","reference_source":"pmid","reference_html":"Myotubularin-related-protein-7 inhibits mutant (G12V) K-RAS by direct interaction. <i> Weidner P, Saar D, Söhn M, Schroeder T, Yu Y, Zöllner FG, Ponelies N, Zhou X, Zwicky A, Rohrbacher FN, Pattabiraman VR, Tanriver M, Bauer A, Ahmed H, Ametamey SM, Riffel P, Seger R, Bode JW, Wade RC, Ebert MPA, Kragelund BB, Burgermeister E. </i> Cancer Lett, 2024","date":"2026-06-17T13:39:46.197Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04420r002","statement":[{"text":"The overall helical content based on NMR shifts was 17 %, corresponding to the disordered monomer observed by CD.","type":"Results"},{"text":"Far-UV circular dichroism (CD) spectroscopy on the myristoylated MT revealed that the peptide adopted a largely disordered structure at low concentrations.","type":"Results"}],"construct_alterations":[{"term_id":"MOD:00438","term_name":"myristoylated residue","term_namespace":"Protein modification","start":521,"end":521,"position":"Specific residue","statements":[{"type":"Figure","text":"MT is myristoylated at the N-terminus (Myr) and amidated at the C-terminus."}]},{"term_id":"MOD:00674","term_name":"amidated residue","term_namespace":"Protein modification","start":550,"end":550,"position":"Specific residue","statements":[{"type":"Figure","text":"MT is myristoylated at the N-terminus (Myr) and amidated at the C-terminus."}]}],"sequence_construct":"LMAVKEETQQLEEELEALEERLEKIQKVQL","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-17T13:40:16.366Z"}},{"start":521,"end":550,"reference_id":"38462034","reference_source":"pmid","reference_html":"Myotubularin-related-protein-7 inhibits mutant (G12V) K-RAS by direct interaction. <i> Weidner P, Saar D, Söhn M, Schroeder T, Yu Y, Zöllner FG, Ponelies N, Zhou X, Zwicky A, Rohrbacher FN, Pattabiraman VR, Tanriver M, Bauer A, Ahmed H, Ametamey SM, Riffel P, Seger R, Bode JW, Wade RC, Ebert MPA, Kragelund BB, Burgermeister E. </i> Cancer Lett, 2024","date":"2026-06-17T13:58:46.259Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"region_id":"DP04420r003","statement":[{"text":"The increase in helicity observed in CD, along with the reduction of NMR peak intensities, suggested that the M7-CC domain formed concentration-dependent oligomers of higher helicity than the disordered monomers.","type":"Results"}],"construct_alterations":[{"term_id":"MOD:00438","term_name":"myristoylated residue","term_namespace":"Protein modification","start":521,"end":521,"position":"Specific residue","statements":[{"type":"Figure","text":"MT is myristoylated at the N-terminus (Myr) and amidated at the C-terminus."}]},{"term_id":"MOD:00674","term_name":"amidated residue","term_namespace":"Protein modification","start":550,"end":550,"position":"Specific residue","statements":[{"type":"Figure","text":"MT is myristoylated at the N-terminus (Myr) and amidated at the C-terminus."}]}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9Y216","operator":null,"partner_start":null,"partner_end":null}],"term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-17T13:59:22.584Z"}},{"start":514,"end":554,"reference_id":"38462034","reference_source":"pmid","reference_html":"Myotubularin-related-protein-7 inhibits mutant (G12V) K-RAS by direct interaction. <i> Weidner P, Saar D, Söhn M, Schroeder T, Yu Y, Zöllner FG, Ponelies N, Zhou X, Zwicky A, Rohrbacher FN, Pattabiraman VR, Tanriver M, Bauer A, Ahmed H, Ametamey SM, Riffel P, Seger R, Bode JW, Wade RC, Ebert MPA, Kragelund BB, Burgermeister E. </i> Cancer Lett, 2024","date":"2026-06-17T13:59:05.419Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"GO:0042803","term_name":"protein homodimerization activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"BMRB","id":"52269"}],"region_id":"DP04420r004","statement":[{"text":"The increase in helicity observed in CD, along with the reduction of NMR peak intensities, suggested that the M7-CC domain formed concentration-dependent oligomers of higher helicity than the disordered monomers.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val518Trp","start":null,"end":null,"position":null}],"sequence_construct":"RQSWTDYLMAVKEETQQLEEELEALEERLEKIQKVQLNCTK","ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9Y216","operator":null,"partner_start":null,"partner_end":null}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","term_comment":"","term_def":"\"Binding to an identical protein to form a homodimer.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-17T13:59:21.483Z"}},{"start":518,"end":527,"reference_id":"38462034","reference_source":"pmid","reference_html":"Myotubularin-related-protein-7 inhibits mutant (G12V) K-RAS by direct interaction. <i> Weidner P, Saar D, Söhn M, Schroeder T, Yu Y, Zöllner FG, Ponelies N, Zhou X, Zwicky A, Rohrbacher FN, Pattabiraman VR, Tanriver M, Bauer A, Ahmed H, Ametamey SM, Riffel P, Seger R, Bode JW, Wade RC, Ebert MPA, Kragelund BB, Burgermeister E. </i> Cancer Lett, 2024","date":"2026-06-17T13:53:44.605Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"GO:0031267","term_name":"small GTPase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"ec_go":"EXP","region_id":"DP04420r005","statement":[{"text":"Plotting the intensity loss per residue (Fig. 5C) revealed that both K-RAS variants interacted with the M7-CC domain via the same two interaction sites (IA1 and IA2) on MTMR7. IA1 included residues T518 – E527 and IA2, A537 – Q546. ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a small monomeric GTPase.\" [GOC:mah, PMID:27218782]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"P01116","operator":null,"partner_start":null,"partner_end":null}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-17T13:59:20.400Z"}},{"start":537,"end":546,"reference_id":"38462034","reference_source":"pmid","reference_html":"Myotubularin-related-protein-7 inhibits mutant (G12V) K-RAS by direct interaction. <i> Weidner P, Saar D, Söhn M, Schroeder T, Yu Y, Zöllner FG, Ponelies N, Zhou X, Zwicky A, Rohrbacher FN, Pattabiraman VR, Tanriver M, Bauer A, Ahmed H, Ametamey SM, Riffel P, Seger R, Bode JW, Wade RC, Ebert MPA, Kragelund BB, Burgermeister E. </i> Cancer Lett, 2024","date":"2026-06-17T13:53:23.230Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"GO:0031267","term_name":"small GTPase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"ec_go":"EXP","region_id":"DP04420r006","statement":[{"text":"Plotting the intensity loss per residue (Fig. 5C) revealed that both K-RAS variants interacted with the M7-CC domain via the same two interaction sites (IA1 and IA2) on MTMR7. IA1 included residues T518 – E527 and IA2, A537 – Q546. ","type":"Results"}],"term_comment":"","term_def":"\"Binding to a small monomeric GTPase.\" [GOC:mah, PMID:27218782]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"P01116","operator":null,"partner_start":null,"partner_end":null}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-17T13:59:19.139Z"}},{"start":499,"end":660,"reference_id":"39614773","reference_source":"pmid","reference_html":"The Myotubularin Related Proteins and the Untapped Interaction Potential of Their Disordered C-Terminal Regions. <i> Saar D, Lennartsson CLE, Weidner P, Burgermeister E, Kragelund BB. </i> Proteins, 2025","date":"2026-06-17T14:08:55.330Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008035","ec_ontology":"ECO","ec_name":"author inference based on intrinsic disorder prediction used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04420r007","statement":[{"text":"Beyond the core and CC domains, MTMRs have N- and C-terminal domains or tails (NTDs and CTDs) of varying lengths and thought to be largely disordered [2].","type":"Introduction"},{"text":"AF3 shows the remainder of the CTDs to be disordered (Figures S1 and S4), while the disorder predictor IUPRED [52], shows lower scores for large parts of the CTDs of MTMR8 and MTMR10, hinting at a potential to form stable structures (Figures S1 and S4). MTMR7 is shown as the representative of this group in Figure 2B.","type":"Results"},{"text":"Authors name CTD to the last 161 residue region, as shown in the Table 1.","type":"Curator statement"}]}],"regions_counter":7,"released":"2026_06","sequence":"MEHIRTPKVENVRLVDRVSPKKAALGTLYLTATHVIFVENSPDPRKETWILHSQISTIEKQATTATGCPLLIRCKNFQIIQLIIPQERDCHDVYISLIRLARPVKYEELYCFSFNPMLDKEEREQGWVLIDLSEEYTRMGLPNHYWQLSDVNRDYRVCDSYPTELYVPKSATAHIIVGSSKFRSRRRFPVLSYYYKDNHASICRSSQPLSGFSARCLEDEQMLQAIRKANPGSDFVYVVDTRPKLNAMANRAAGKGYENEDNYSNIKFQFIGIENIHVMRNSLQKMLEVCELKSPSMSDFLWGLENSGWLRHIKAIMDAGIFIAKAVSEEGASVLVHCSDGWDRTAQVCSVASLLLDPHYRTLKGFMVLIEKDWISFGHKFNHRYGNLDGDPKEISPVIDQFIECVWQLMEQFPCAFEFNERFLIHIQHHIYSCQFGNFLCNSQKERRELKIQERTYSLWAHLWKNRADYLNPLFRADHSQTQGTLHLPTTPCNFMYKFWSGMYNRFEKGMQPRQSVTDYLMAVKEETQQLEEELEALEERLEKIQKVQLNCTKVKSKQSEPSKHSGFSTSDNSIANTPQDYSGNMKSFPSRSPSQGDEDSALILTQDNLKSSDPDLSANSDQESGVEDLSCRSPSGGEHAPSEDSGKDRDSDEAVFLTA","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.16363636363636364,"disorder_content":0.24545454545454545,"disprot_consensus":{"full":[{"start":499,"end":660,"type":"D"}],"Structural state":[{"start":499,"end":660,"type":"D"}],"Molecular function":[{"start":514,"end":554,"type":"F"}]}},{"acc":"P0DXN6","sequence":"MATLLRSLALFKRNKDKPPITSGSGGAIRGIKHIIIVPIPGDSSITTRSRLLDRLVRLIGNPDVSGPKLTGALIGILSLFVESPGQLIQRITDDPDVSIRLLEVVQSDQSQSGLTFASRGTNMEDEADQYFSHDDPISSDQSRFGWFENKEISDIEVQDPEGFNMILGTILAQIWVLLAKAVTAPDTAADSELRRWIKYTQQRRVVGEFRLERKWLDVVRNRIAEDLSLRRFMVALILDIKRTPGNKPRIAEMICDIDTYIVEAGLASFILTIKFGIETMYPALGLHEFAGELSTLESLMNLYQQMGETAPYMVILENSIQNKFSAGSYPLLWSYAMGVGVELENSMGGLNFGRSYFDPAYFRLGQEMVRRSAGKVSSTLASELGITAEDARLVSEIAMHTTEDKISRAVGPRQAQVSFLHGDQSENELPRLGGKEDRRVKQSRGEARESYRETGPSRASDARAAHLPTGTPLDIDTASESSQDPQDSRRSADALLRLQAMAGISEEQGSDTDTPIVYNDRNLLD","creator":"System-tlazar","dataset":["Viral proteins","Condensates-related proteins","RNA-binding proteins"],"date":"2025-06-21T12:56:53.314Z","disprot_id":"DP04423","features":{"pfam":[{"id":"PF00973","name":"Paramyxovirus nucleocapsid protein","start":1,"end":399}]},"genes":[{"name":{"value":"N","evidences":[],"_id":"6856ac157cd61eccdacd5be7"},"synonyms":[{"value":"NP","evidences":[],"_id":"6856ac157cd61eccdacd5be8"}],"olnNames":[],"orfNames":[],"_id":"6856ac157cd61eccdacd5be6"}],"length":525,"name":"Nucleoprotein","ncbi_taxon_id":70146,"organism":"Measles virus (strain Edmonston B)","regions_counter":83,"released":"2025_06","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Haploviricotina","Monjiviricetes","Mononegavirales","Paramyxoviridae","Orthoparamyxovirinae","Morbillivirus","Morbillivirus hominis","Measles morbillivirus"],"regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":525,"interaction_partner":[],"reference_html":"The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein. <i> Longhi S, Receveur-Bréchot V, Karlin D, Johansson K, Darbon H, Bhella D, Yeo R, Finet S, Canard B. </i> J Biol Chem, 2003","reference_id":"12621042","region_id":"DP04423r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The very small spread of the resonance frequencies for amide protons (between 7.8 and 8.7 ppm; see frame in Fig.2A) together with the scarcity of nuclear Overhauser effects in the amide-amide region are typical of a protein without any stable secondary structure.","_id":"6856af027cd61eccdacd5ca4"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T11:41:10.415Z","_id":"6856af027cd61eccdacd5ca5"},"version":3,"_id":"6856af027cd61eccdacd5ca3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":525,"interaction_partner":[],"reference_html":"The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein. <i> Longhi S, Receveur-Bréchot V, Karlin D, Johansson K, Darbon H, Bhella D, Yeo R, Finet S, Canard B. </i> J Biol Chem, 2003","reference_id":"12621042","region_id":"DP04423r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In the case of NTAIL, RSN = 19 Å and RSU = 35 Å. Therefore, the Stokes radius experimentally measured for NTAIL (27 Å) is not compatible with a monomeric, globular protein. Rather, such a large value of the Stokes radius can be attributed either to dimerization or to an extended conformation.","_id":"6856af027cd61eccdacd5cb7"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T11:41:08.064Z","_id":"6856af027cd61eccdacd5cb8"},"version":3,"_id":"6856af027cd61eccdacd5cb6","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0001591","ec_name":"atomic force microscopy evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":525,"interaction_partner":[],"reference_html":"Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy. <i> Kodera N, Noshiro D, Dora SK, Mori T, Habchi J, Blocquel D, Gruet A, Dosnon M, Salladini E, Bignon C, Fujioka Y, Oda T, Noda NN, Sato M, Lotti M, Mizuguchi M, Longhi S, Ando T. </i> Nat Nanotechnol, 2021","reference_id":"33230318","region_id":"DP04423r030","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The IDR showed a temporarily appearing and disappearing small globule at the N terminus corresponding to Box1 (Fig. 4d). Except for this, the IDR was observed to be fully disordered (with mean height of 0.4−0.5 nm) (Extended Data Fig. 5a).","_id":"6856af027cd61eccdacd5cee"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T11:24:43.511Z","_id":"6856af027cd61eccdacd5cef"},"version":3,"_id":"6856af027cd61eccdacd5ced","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"IDA","ec_id":"ECO:0001591","ec_name":"atomic force microscopy evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":420,"interaction_partner":[],"reference_html":"Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy. <i> Kodera N, Noshiro D, Dora SK, Mori T, Habchi J, Blocquel D, Gruet A, Dosnon M, Salladini E, Bignon C, Fujioka Y, Oda T, Noda NN, Sato M, Lotti M, Mizuguchi M, Longhi S, Ando T. </i> Nat Nanotechnol, 2021","reference_id":"33230318","region_id":"DP04423r031","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The IDR showed a temporarily appearing and disappearing small globule at the N terminus corresponding to Box1 (Fig. 4d).","_id":"6856af027cd61eccdacd5cf1"},{"type":"Results","text":"he H2 value of 0.8 nm is larger than the height of fully disordered regions, indicating that Box1 and Box2 are both partially ordered, even in their lower height states.","_id":"6856af027cd61eccdacd5cf2"},{"type":"Curator statement","text":"Measles virus (MeV) nucleoprotein Box 1 region is comprised within the residues 401–420 ","_id":"6856af027cd61eccdacd5cf3"}],"states_connection":[],"term_id":"IDPO:0000018","term_name":"disorder to molten globule","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T11:52:15.678Z","_id":"6856af027cd61eccdacd5cf4"},"version":1,"_id":"6856af027cd61eccdacd5cf0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"IDA","ec_id":"ECO:0001591","ec_name":"atomic force microscopy evidence used in manual assertion","ec_ontology":"ECO","start":482,"end":502,"interaction_partner":[],"reference_html":"Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy. <i> Kodera N, Noshiro D, Dora SK, Mori T, Habchi J, Blocquel D, Gruet A, Dosnon M, Salladini E, Bignon C, Fujioka Y, Oda T, Noda NN, Sato M, Lotti M, Mizuguchi M, Longhi S, Ando T. </i> Nat Nanotechnol, 2021","reference_id":"33230318","region_id":"DP04423r032","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The H2 value of 0.8 nm is larger than the height of fully disordered regions, indicating that Box1 and Box2 are both partially ordered, even in their lower height states.","_id":"6856af027cd61eccdacd5cf6"},{"type":"Curator statement","text":"Measles virus (MeV) nucleoprotein Box 2 region is comprised within the residues 482–502.","_id":"6856af027cd61eccdacd5cf7"}],"states_connection":[],"term_id":"IDPO:0000018","term_name":"disorder to molten globule","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T11:52:08.194Z","_id":"6856af027cd61eccdacd5cf8"},"version":1,"_id":"6856af027cd61eccdacd5cf5","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0001230","ec_name":"mass spectrometry evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":525,"interaction_partner":[],"reference_html":"Molecular basis for structural heterogeneity of an intrinsically disordered protein bound to a partner by combined ESI-IM-MS and modeling. <i> D'Urzo A, Konijnenberg A, Rossetti G, Habchi J, Li J, Carloni P, Sobott F, Longhi S, Grandori R. </i> J Am Soc Mass Spectrom, 2015","reference_id":"25510932","region_id":"DP04423r033","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The spectra are dominated by the peaks of the free proteins, but signals specific to the NTAIL–PXD complex become evident at the higher protein concentration. The measured mass of the complex (21,187.4 ± 0.61 Da) corresponds closely to the sum of the theoretical values expected for NTAIL with the initial methionine and PXD without the initial methionine (21,187.46 Da), indicating a 1:1 stoichiometry.","_id":"6856af027cd61eccdacd5cfa"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T14:04:52.831Z","_id":"6856af027cd61eccdacd5cfb"},"version":1,"_id":"6856af027cd61eccdacd5cf9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":525,"interaction_partner":[{"db":"UniProt","id":"P03422","partner_start":null,"partner_end":null,"_id":"6856af027cd61eccdacd5cfd"}],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r034","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The molecular mass (MM) calculated from the forward scattering intensity I(0) is 23.5 ± 2 kDa, in agreement with the value expected for a 1:1 stoichiometric complex (21.3 kDa), thus suggesting that the complex did form in solution.","_id":"6856af027cd61eccdacd5cfe"},{"type":"Results","text":"The high value of Rg indicated that the overall structure of the NTAILHN–XD complex is not compact. ","_id":"6856af027cd61eccdacd5cff"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T14:04:08.450Z","_id":"6856af027cd61eccdacd5d00"},"version":1,"_id":"6856af027cd61eccdacd5cfc","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":516,"interaction_partner":[],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r035","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As shown in Figure 3B, the three NTAIL deletion proteins migrate in SDS-PAGE with an apparent MM of either 20 kDa (NTAILΔ3 and NTAILΔ1) or 18 kDa (NTAILΔ2,3) (expected MMs are 14.5, 13.4, and 11.5 kDa, respectively). This abnormal migratory behavior has already been documented for NTAIL, where mass spectrometry analysis and N-terminal sequencing gave the expected results (Longhi et al. 2003). The anomalous electrophoretic mobility is therefore due to a rather high content of acidic residues, as frequently observed in intrinsically disordered proteins (Tompa 2002).","_id":"6856af027cd61eccdacd5d02"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T11:24:38.818Z","_id":"6856af027cd61eccdacd5d03"},"version":1,"_id":"6856af027cd61eccdacd5d01","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":488,"interaction_partner":[],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r036","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As shown in Figure 3B, the three NTAIL deletion proteins migrate in SDS-PAGE with an apparent MM of either 20 kDa (NTAILΔ3 and NTAILΔ1) or 18 kDa (NTAILΔ2,3) (expected MMs are 14.5, 13.4, and 11.5 kDa, respectively). This abnormal migratory behavior has already been documented for NTAIL, where mass spectrometry analysis and N-terminal sequencing gave the expected results (Longhi et al. 2003). The anomalous electrophoretic mobility is therefore due to a rather high content of acidic residues, as frequently observed in intrinsically disordered proteins (Tompa 2002).","_id":"6856af027cd61eccdacd5d05"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T11:24:36.123Z","_id":"6856af027cd61eccdacd5d06"},"version":1,"_id":"6856af027cd61eccdacd5d04","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":421,"end":525,"interaction_partner":[],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r037","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As shown in Figure 3B, the three NTAIL deletion proteins migrate in SDS-PAGE with an apparent MM of either 20 kDa (NTAILΔ3 and NTAILΔ1) or 18 kDa (NTAILΔ2,3) (expected MMs are 14.5, 13.4, and 11.5 kDa, respectively). This abnormal migratory behavior has already been documented for NTAIL, where mass spectrometry analysis and N-terminal sequencing gave the expected results (Longhi et al. 2003). The anomalous electrophoretic mobility is therefore due to a rather high content of acidic residues, as frequently observed in intrinsically disordered proteins (Tompa 2002).","_id":"6856af027cd61eccdacd5d08"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T11:24:33.695Z","_id":"6856af027cd61eccdacd5d09"},"version":1,"_id":"6856af027cd61eccdacd5d07","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0001184","ec_name":"gel-filtration evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":516,"interaction_partner":[],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r038","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As expected for intrinsically disordered protein subdomains, the Stokes radius (RS) values, as inferred by gel filtration (27 ± 3 Å, 22 ± 3 Å, and 27 ± 3 Å for NTAILΔ3, NTAILΔ2,3, and NTAILΔ1, respectively), are consistent with extended conformations (see Materials and Methods). ","_id":"6856af027cd61eccdacd5d0b"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T11:24:24.907Z","_id":"6856af027cd61eccdacd5d0c"},"version":1,"_id":"6856af027cd61eccdacd5d0a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0001184","ec_name":"gel-filtration evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":488,"interaction_partner":[],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r039","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As expected for intrinsically disordered protein subdomains, the Stokes radius (RS) values, as inferred by gel filtration (27 ± 3 Å, 22 ± 3 Å, and 27 ± 3 Å for NTAILΔ3, NTAILΔ2,3, and NTAILΔ1, respectively), are consistent with extended conformations (see Materials and Methods). ","_id":"6856af027cd61eccdacd5d0e"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T11:24:21.523Z","_id":"6856af027cd61eccdacd5d0f"},"version":1,"_id":"6856af027cd61eccdacd5d0d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0001184","ec_name":"gel-filtration evidence used in manual assertion","ec_ontology":"ECO","start":421,"end":525,"interaction_partner":[],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r040","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As expected for intrinsically disordered protein subdomains, the Stokes radius (RS) values, as inferred by gel filtration (27 ± 3 Å, 22 ± 3 Å, and 27 ± 3 Å for NTAILΔ3, NTAILΔ2,3, and NTAILΔ1, respectively), are consistent with extended conformations (see Materials and Methods). ","_id":"6856af027cd61eccdacd5d11"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T11:24:19.428Z","_id":"6856af027cd61eccdacd5d12"},"version":1,"_id":"6856af027cd61eccdacd5d10","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":525,"interaction_partner":[],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r041","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The high value of Rg indicated that the overall structure of the NTAILHN–XD complex is not compact. The distances distribution function inferred from the scattering curve of the NTAILHN–XD complex exhibits a maximum at 20 Å, with a shoulder at about 30 Å and a long tail up to 146 Å, typical of an elongated object (see Fig. 2A).","_id":"6856af027cd61eccdacd5d14"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T11:24:13.946Z","_id":"6856af027cd61eccdacd5d15"},"version":1,"_id":"6856af027cd61eccdacd5d13","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001269","ec_name":"surface plasmon resonance evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":525,"interaction_partner":[{"db":"UniProt","id":"P03422","partner_start":null,"partner_end":null,"_id":"6856af027cd61eccdacd5d17"}],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r042","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Binding affinities between XD and NTAIL constructs were established using 180–225 RU of immobilized XD and NTAIL concentrations ranging from 0.1 to 10 μM (see Materials and Methods). Dosage-dependent binding was observed in this range. Reactions conformed to a 1:1 ligand-substrate (Langmuir) binding model, exhibiting an excellent fit (i.e., a χ2 value <1 and residuals within the range of ±2) following global analysis of sensorgrams.","_id":"6856af027cd61eccdacd5d18"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T14:04:06.597Z","_id":"6856af027cd61eccdacd5d19"},"version":1,"_id":"6856af027cd61eccdacd5d16","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001269","ec_name":"surface plasmon resonance evidence used in manual assertion","ec_ontology":"ECO","start":517,"end":525,"interaction_partner":[{"db":"UniProt","id":"P03422","partner_start":null,"partner_end":null,"_id":"6856af027cd61eccdacd5d1b"}],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r043","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In contrast, removal of either Box3 alone or Box2 plus Box3 results in a strong decrease (three orders of magnitude) in the equilibrium dissociation constant, where NTAILΔ3 and NTAILΔ2,3 display similar binding affinities (see Table 1). The strong decrease in the affinity resulting from removal of Box3 clearly indicates that Box2 is not the sole region involved in binding to XD, and attests that Box3 also plays a role in the interaction with XD, as already suggested by SAXS studies.","_id":"6856af027cd61eccdacd5d1c"},{"type":"Curator statement","text":"Measles virus (MeV) nucleoprotein Box 3 region is comprised within the residues 517-525.","_id":"6856af027cd61eccdacd5d1d"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T14:04:05.064Z","_id":"6856af027cd61eccdacd5d1e"},"version":1,"_id":"6856af027cd61eccdacd5d1a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001269","ec_name":"surface plasmon resonance evidence used in manual assertion","ec_ontology":"ECO","start":489,"end":525,"interaction_partner":[{"db":"UniProt","id":"P03422","partner_start":null,"partner_end":null,"_id":"6856af027cd61eccdacd5d20"}],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r044","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In contrast, removal of either Box3 alone or Box2 plus Box3 results in a strong decrease (three orders of magnitude) in the equilibrium dissociation constant, where NTAILΔ3 and NTAILΔ2,3 display similar binding affinities (see Table 1).","_id":"6856af027cd61eccdacd5d21"},{"type":"Curator statement","text":"Measles virus (MeV) nucleoprotein Box 2 and Box 3 region is comprised within the residues 488-525.","_id":"6856af027cd61eccdacd5d22"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T14:04:03.095Z","_id":"6856af027cd61eccdacd5d23"},"version":1,"_id":"6856af027cd61eccdacd5d1f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":516,"interaction_partner":[],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r045","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The far-UV circular dichroism (CD) spectra of NTAIL deletion proteins at neutral pH are typical of unstructured proteins, as seen by their large negative ellipticity at 198 nm and very low ellipticity at 185 nm (Fig. 4A–C).","_id":"6856af027cd61eccdacd5d25"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T11:22:24.536Z","_id":"6856af027cd61eccdacd5d26"},"version":1,"_id":"6856af027cd61eccdacd5d24","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":488,"interaction_partner":[],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r046","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The far-UV circular dichroism (CD) spectra of NTAIL deletion proteins at neutral pH are typical of unstructured proteins, as seen by their large negative ellipticity at 198 nm and very low ellipticity at 185 nm (Fig. 4A–C).","_id":"6856af027cd61eccdacd5d28"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T11:24:00.853Z","_id":"6856af027cd61eccdacd5d29"},"version":1,"_id":"6856af027cd61eccdacd5d27","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":421,"end":525,"interaction_partner":[],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r047","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The far-UV circular dichroism (CD) spectra of NTAIL deletion proteins at neutral pH are typical of unstructured proteins, as seen by their large negative ellipticity at 198 nm and very low ellipticity at 185 nm (Fig. 4A–C).","_id":"6856af027cd61eccdacd5d2b"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T11:19:03.632Z","_id":"6856af027cd61eccdacd5d2c"},"version":1,"_id":"6856af027cd61eccdacd5d2a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":525,"interaction_partner":[{"db":"UniProt","id":"P03422","partner_start":null,"partner_end":null,"_id":"6856af027cd61eccdacd5d2e"}],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r048","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"After mixing NTAILHNFC with different molar excesses of XD, the observed CD spectra differed from the corresponding theoretical average curves calculated from the individual spectra. ","_id":"6856af027cd61eccdacd5d2f"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T14:04:01.461Z","_id":"6856af027cd61eccdacd5d30"},"version":1,"_id":"6856af027cd61eccdacd5d2d","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":525,"interaction_partner":[],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r049","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Since the theoretical average curves correspond to the spectra that would be expected if no structural variations occur, deviations from these curves indicate structural transitions. The results obtained in the presence of a threefold molar excess of XD indicate a random coil to α-helix transition, as judged by the much more pronounced minima at 208 nm and 222 nm, and by the higher ellipticity at 190 nm of the experimentally observed spectrum compared to the corresponding theoretical average curve (see Fig. 5A).","_id":"6856af027cd61eccdacd5d32"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T11:50:58.134Z","_id":"6856af027cd61eccdacd5d33"},"version":1,"_id":"6856af027cd61eccdacd5d31","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":516,"interaction_partner":[],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r050","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Removal of Box3 significantly reduces, but does not abrogate, the folding ability of NTAIL. Indeed, the experimental CD spectrum does not significantly deviate from the average curve in the 200–260 nm region, but it considerably deviates from the average curve in the 185–195 region (58% mean increase of ellipticity) (Fig. 5B), thus supporting partial folding ability of NTAILΔ3 in the presence of XD.","_id":"6856af027cd61eccdacd5d35"},{"type":"Curator statement","text":"Measles virus (MeV) nucleoprotein Box 3 region is comprised within the residues 517-525","_id":"6856af027cd61eccdacd5d36"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T11:49:25.281Z","_id":"6856af027cd61eccdacd5d37"},"version":1,"_id":"6856af027cd61eccdacd5d34","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":421,"end":525,"interaction_partner":[],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r051","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Conversely, removal of Box1 does not affect the folding ability of NTAIL, as the deviations from the average spectrum are similar to those observed with the full-length form (Fig. 5, cf. D and A). The mean increase in ellipticity in the 185–195 nm region (77%) and the decrease in the ellipticity value at 220 nm (46%) observed with NTAILΔ1, are comparable to the corresponding values observed with NTAILHNFC (70% and 46%, respectively).","_id":"6856af027cd61eccdacd5d39"},{"type":"Curator statement","text":"Measles virus (MeV) nucleoprotein Box 1 region is comprised within the residues 401-420.","_id":"6856af027cd61eccdacd5d3a"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T11:49:10.014Z","_id":"6856af027cd61eccdacd5d3b"},"version":1,"_id":"6856af027cd61eccdacd5d38","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":416,"interaction_partner":[],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r052","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As shown in Figure 7, the same peaks undergoing the large displacement in the NTAILHN–XD complex are also observed in the NTAILΔ3–XD complex. In particular, among these peaks, the occurrence in both complexes of the 11 peaks that undergo the random coil to α-helix transition (see Fig. 7, stars), provides further support that the helical folding occurs within Box2.","_id":"6856af027cd61eccdacd5d3d"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T11:48:34.798Z","_id":"6856af027cd61eccdacd5d3e"},"version":1,"_id":"6856af027cd61eccdacd5d3c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":525,"interaction_partner":[],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r053","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The high value of Rg indicated that the overall structure of the NTAILHN–XD complex is not compact. The distances distribution function inferred from the scattering curve of the NTAILHN–XD complex exhibits a maximum at 20 Å, with a shoulder at about 30 Å and a long tail up to 146 Å, typical of an elongated object (see Fig. 2A). The bump most probably corresponds to the intramolecular distances within the globular portion of the complex (see below), while the tail indicates that NTAIL possesses regions with an extended conformation.","_id":"6856af027cd61eccdacd5d40"}],"states_connection":[],"term_id":"IDPO:0000030","term_name":"entropic chain","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T14:04:40.636Z","_id":"6856af027cd61eccdacd5d41"},"version":1,"_id":"6856af027cd61eccdacd5d3f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":525,"interaction_partner":[],"reference_html":"The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein. <i> Longhi S, Receveur-Bréchot V, Karlin D, Johansson K, Darbon H, Bhella D, Yeo R, Finet S, Canard B. </i> J Biol Chem, 2003","reference_id":"12621042","region_id":"DP04423r057","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As shown in Fig. 1B, NTAILdisplays an abnormally slow migration in SDS-PAGE even after heat denaturation. In particular, it migrates with an apparent molecular mass (MM) of 20 kDa, whereas the expected MM is 15 kDa. This abnormal behavior has already been observed in the case of the intrinsically disordered MV PNT (41) as well as in other intrinsically disordered proteins and can most likely be ascribed to their unusual sequence composition (30).","_id":"6856af027cd61eccdacd5d50"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T11:18:15.948Z","_id":"6856af027cd61eccdacd5d51"},"version":1,"_id":"6856af027cd61eccdacd5d4f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0007064","ec_name":"dynamic light scattering assay evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":525,"interaction_partner":[],"reference_html":"The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein. <i> Longhi S, Receveur-Bréchot V, Karlin D, Johansson K, Darbon H, Bhella D, Yeo R, Finet S, Canard B. </i> J Biol Chem, 2003","reference_id":"12621042","region_id":"DP04423r058","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Thus, the V of NTAIL calculated by DLS is about 3 times larger than the value expected for a globular protein and half of that expected for a denatured, fully unfolded protein. Rather, these hydrodynamic properties are consistent with the hypothesis that NTAIL is a native premolten globule (31).","_id":"6856af027cd61eccdacd5d53"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T10:36:12.081Z","_id":"6856af027cd61eccdacd5d54"},"version":1,"_id":"6856af027cd61eccdacd5d52","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":525,"interaction_partner":[],"reference_html":"The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein. <i> Longhi S, Receveur-Bréchot V, Karlin D, Johansson K, Darbon H, Bhella D, Yeo R, Finet S, Canard B. </i> J Biol Chem, 2003","reference_id":"12621042","region_id":"DP04423r059","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The far-UV CD spectrum of NTAIL at neutral pH is typical of an unstructured protein, as seen from its large negative ellipticity at 198 nm and very low ellipticity at 185 nm (Fig. 2B). However, the observed ellipticity values at 200 and 222 nm (−9700 and −2400 degrees cm2 dmol−1, respectively) (Fig. 2B) are consistent with the existence of some residual secondary structure, typical of the premolten globule state (39).","_id":"6856af027cd61eccdacd5d56"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T10:35:42.197Z","_id":"6856af027cd61eccdacd5d57"},"version":1,"_id":"6856af027cd61eccdacd5d55","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0007691","ec_name":"cleavage assay evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":525,"interaction_partner":[],"reference_html":"The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein. <i> Longhi S, Receveur-Bréchot V, Karlin D, Johansson K, Darbon H, Bhella D, Yeo R, Finet S, Canard B. </i> J Biol Chem, 2003","reference_id":"12621042","region_id":"DP04423r060","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"NCORE was obtained by limited proteolysis of purified N as described in Ref. 4, followed by gel filtration (data not shown).","_id":"6856af027cd61eccdacd5d59"},{"type":"Curator statement","text":"Measles virus (MeV) nucleoprotein NCORE region is comprised within 1–399 residues. Its obtention trough this methodology  proves that 400-525 region is susceptible to proteolysis, hallmark of intrinsic disorder.","_id":"6856af027cd61eccdacd5d5a"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T10:35:24.228Z","_id":"6856af027cd61eccdacd5d5b"},"version":1,"_id":"6856af027cd61eccdacd5d58","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0006082","ec_name":"affinity chromatography evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":525,"interaction_partner":[{"db":"UniProt","id":"P03422","partner_start":null,"partner_end":null,"_id":"6856af027cd61eccdacd5d5d"}],"reference_html":"The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein. <i> Longhi S, Receveur-Bréchot V, Karlin D, Johansson K, Darbon H, Bhella D, Yeo R, Finet S, Canard B. </i> J Biol Chem, 2003","reference_id":"12621042","region_id":"DP04423r061","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"When both lysates were mixed, the IMAC resin selectively pulled down NTAIL together with an additional protein that has the same electrophoretic mobility of P (Fig. 5B,lane Nt + P). The identity of this protein band was confirmed by Western blotting using an anti-P mAb (data not shown), thus proving that the NTAIL domain on its own is able to bind its physiological partner in bacterial lysates.","_id":"6856af027cd61eccdacd5d5e"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T14:04:00.237Z","_id":"6856af027cd61eccdacd5d5f"},"version":1,"_id":"6856af027cd61eccdacd5d5c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":525,"interaction_partner":[{"db":"UniProt","id":"P03422","partner_start":null,"partner_end":null,"_id":"6856af027cd61eccdacd5d61"}],"reference_html":"The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein. <i> Longhi S, Receveur-Bréchot V, Karlin D, Johansson K, Darbon H, Bhella D, Yeo R, Finet S, Canard B. </i> J Biol Chem, 2003","reference_id":"12621042","region_id":"DP04423r062","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"After mixing NTAIL with different molar excesses of PCT, the observed CD spectra of the mixtures differ from the corresponding theoretical average curves calculated from the individual spectra. Since the theoretical average curves correspond to the spectra that would be expected if no structural variations occur, deviations from these curves point out structural transitions.","_id":"6856af027cd61eccdacd5d62"},{"type":"Results","text":"Therefore, these results indicate that NTAIL undergoes an induced folding upon binding to PCT.","_id":"6856af027cd61eccdacd5d63"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T14:03:58.787Z","_id":"6856af027cd61eccdacd5d64"},"version":1,"_id":"6856af027cd61eccdacd5d60","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":525,"interaction_partner":[],"reference_html":"The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein. <i> Longhi S, Receveur-Bréchot V, Karlin D, Johansson K, Darbon H, Bhella D, Yeo R, Finet S, Canard B. </i> J Biol Chem, 2003","reference_id":"12621042","region_id":"DP04423r063","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"After mixing NTAIL with different molar excesses of PCT, the observed CD spectra of the mixtures differ from the corresponding theoretical average curves calculated from the individual spectra. Since the theoretical average curves correspond to the spectra that would be expected if no structural variations occur, deviations from these curves point out structural transitions.","_id":"6856af027cd61eccdacd5d66"},{"type":"Results","text":"In the presence of molar excesses of PCT, a random coil to α-helix transition can be observed, as indicated by the much more pronounced minima at 208 and 222 nm and by the higher ellipticity at 190 nm of the experimentally observed spectra compared with the corresponding theoretical average curves (Fig. 6A).","_id":"6856af027cd61eccdacd5d67"},{"type":"Results","text":"Therefore, these results indicate that NTAIL undergoes an induced folding upon binding to PCT.","_id":"6856af027cd61eccdacd5d68"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T11:48:22.850Z","_id":"6856af027cd61eccdacd5d69"},"version":1,"_id":"6856af027cd61eccdacd5d65","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":525,"interaction_partner":[],"reference_html":"The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein. <i> Longhi S, Receveur-Bréchot V, Karlin D, Johansson K, Darbon H, Bhella D, Yeo R, Finet S, Canard B. </i> J Biol Chem, 2003","reference_id":"12621042","region_id":"DP04423r064","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Therefore, the observedRg indicates that NTAIL is not globular. However, the protein is more compact than a random coil, suggesting that it possesses some residual structure.","_id":"6856af027cd61eccdacd5d6b"},{"type":"Results","text":"The Kratky plot of NTAIL displays a bump atq ≈ 0.08 Å−1 followed by a plateau forq > 0.15 Å−1 (see Fig. 3B). The absence of a maximum clearly indicates that NTAIL is not globular and does not possess a tightly packed core. However, the observed bump may be indicative of some residual structure.","_id":"6856af027cd61eccdacd5d6c"},{"type":"Results","text":"In the case of NTAIL, the RS andRg values obtained by DLS and SAXS, respectively, lead to a ratio of 1.1, which is consistent with a premolten globule. ","_id":"6856af027cd61eccdacd5d6d"}],"states_connection":[],"term_id":"IDPO:0000004","term_name":"pre-molten globule","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T10:34:46.461Z","_id":"6856af027cd61eccdacd5d6e"},"version":1,"_id":"6856af027cd61eccdacd5d6a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":525,"interaction_partner":[],"reference_html":"The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein. <i> Longhi S, Receveur-Bréchot V, Karlin D, Johansson K, Darbon H, Bhella D, Yeo R, Finet S, Canard B. </i> J Biol Chem, 2003","reference_id":"12621042","region_id":"DP04423r065","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"After mixing NTAIL with different molar excesses of PCT, the observed CD spectra of the mixtures differ from the corresponding theoretical average curves calculated from the individual spectra. Since the theoretical average curves correspond to the spectra that would be expected if no structural variations occur, deviations from these curves point out structural transitions.\" Results \"Therefore, these results indicate that NTAIL undergoes an induced folding upon binding to PCT","_id":"6856af027cd61eccdacd5d70"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T14:04:38.071Z","_id":"6856af027cd61eccdacd5d71"},"version":1,"_id":"6856af027cd61eccdacd5d6f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":525,"interaction_partner":[],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r069","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"After mixing NTAILHNFC with different molar excesses of XD, the observed CD spectra differed from the corresponding theoretical average curves calculated from the individual spectra.","_id":"6856af027cd61eccdacd5d80"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T14:04:33.087Z","_id":"6856af027cd61eccdacd5d81"},"version":1,"_id":"6856af027cd61eccdacd5d7f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-08T15:35:47.916Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001269","ec_name":"surface plasmon resonance evidence used in manual assertion","ec_ontology":"ECO","start":489,"end":525,"interaction_partner":[{"db":"UniProt","id":"P03422","operator":"and","partner_start":null,"partner_end":null,"_id":"6856af027cd61eccdacd5d85"}],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r070","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In contrast, removal of either Box3 alone or Box2 plus Box3 results in a strong decrease (three orders of magnitude) in the equilibrium dissociation constant, where NTAILΔ3 and NTAILΔ2,3 display similar binding affinities (see Table 1).","_id":"6856af027cd61eccdacd5d83"},{"type":"Curator statement","text":"Measles virus (MeV) nucleoprotein Box 2 and Box 3 region is comprised within the residues 488-525.","_id":"6856af027cd61eccdacd5d84"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-21T21:31:08.885Z","_id":"6856af027cd61eccdacd5d86"},"version":2,"_id":"6856af027cd61eccdacd5d82","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-03-08T15:35:29.571Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0001269","ec_name":"surface plasmon resonance evidence used in manual assertion","ec_ontology":"ECO","start":517,"end":525,"interaction_partner":[{"db":"UniProt","id":"P03422","operator":"and","partner_start":null,"partner_end":null,"_id":"6856af027cd61eccdacd5d8a"}],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r071","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In contrast, removal of either Box3 alone or Box2 plus Box3 results in a strong decrease (three orders of magnitude) in the equilibrium dissociation constant, where NTAILΔ3 and NTAILΔ2,3 display similar binding affinities (see Table 1). The strong decrease in the affinity resulting from removal of Box3 clearly indicates that Box2 is not the sole region involved in binding to XD, and attests that Box3 also plays a role in the interaction with XD, as already suggested by SAXS studies.","_id":"6856af027cd61eccdacd5d88"},{"type":"Curator statement","text":"Measles virus (MeV) nucleoprotein Box 3 region is comprised within the residues 517-525.","_id":"6856af027cd61eccdacd5d89"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-21T21:31:09.452Z","_id":"6856af027cd61eccdacd5d8b"},"version":2,"_id":"6856af027cd61eccdacd5d87","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":525,"interaction_partner":[],"reference_html":"The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded. <i> Bourhis JM, Receveur-Bréchot V, Oglesbee M, Zhang X, Buccellato M, Darbon H, Canard B, Finet S, Longhi S. </i> Protein Sci, 2005","reference_id":"16046624","region_id":"DP04423r073","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The molecular mass (MM) calculated from the forward scattering intensity I(0) is 23.5 ± 2 kDa, in agreement with the value expected for a 1:1 stoichiometric complex (21.3 kDa), thus suggesting that the complex did form in solution.","_id":"6856af027cd61eccdacd5d91"},{"type":"Results","text":"The high value of Rg indicated that the overall structure of the NTAILHN–XD complex is not compact.","_id":"6856af027cd61eccdacd5d92"}],"states_connection":[],"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","term_id":"GO:0060090","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T14:04:17.464Z","_id":"6856af027cd61eccdacd5d93"},"version":1,"_id":"6856af027cd61eccdacd5d90","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0001230","ec_name":"mass spectrometry evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":525,"interaction_partner":[],"reference_html":"Molecular basis for structural heterogeneity of an intrinsically disordered protein bound to a partner by combined ESI-IM-MS and modeling. <i> D'Urzo A, Konijnenberg A, Rossetti G, Habchi J, Li J, Carloni P, Sobott F, Longhi S, Grandori R. </i> J Am Soc Mass Spectrom, 2015","reference_id":"25510932","region_id":"DP04423r074","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The spectrum shows a very broad, bimodal charge-state distribution (CSD), indicating structural heterogeneity consistent with the intrinsically disordered nature of this protein.","_id":"6856af027cd61eccdacd5d95"},{"type":"Results","text":"The rest of the spectrum is characterized by a broad peak envelope that spans the region between the 10+ and the 24+ ions, with main charge state 16+. This component corresponds to disordered conformations, characterized by low compactness.","_id":"6856af027cd61eccdacd5d96"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T12:05:24.796Z","_id":"6856af027cd61eccdacd5d97"},"version":1,"_id":"6856af027cd61eccdacd5d94","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0001230","ec_name":"mass spectrometry evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":525,"interaction_partner":[],"reference_html":"Molecular basis for structural heterogeneity of an intrinsically disordered protein bound to a partner by combined ESI-IM-MS and modeling. <i> D'Urzo A, Konijnenberg A, Rossetti G, Habchi J, Li J, Carloni P, Sobott F, Longhi S, Grandori R. </i> J Am Soc Mass Spectrom, 2015","reference_id":"25510932","region_id":"DP04423r075","released":"2022_03","sample":[],"statement":[{"type":"Results","text":" In this case, two slightly different conformations are found to populate the compact state of the NTAIL–PXD complex (charge states 8+ to 10+). Average CCS of 1326 and 1422 Å2 can be derived for the two main peaks detectable for the 8+ charge state. This result suggests that the compact state of the complex is characterized by further structural heterogeneity. Thus, although its overall ionization suggests a collapsed structure, its arrival-time distribution reveals distinct peaks rather than the single peak typically observed for normally folded proteins. ","_id":"6856af027cd61eccdacd5d99"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T12:14:14.353Z","_id":"6856af027cd61eccdacd5d9a"},"version":1,"_id":"6856af027cd61eccdacd5d98","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0001230","ec_name":"mass spectrometry evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":525,"interaction_partner":[{"db":"UniProt","id":"P03422","partner_start":null,"partner_end":null,"_id":"6856af027cd61eccdacd5d9c"}],"reference_html":"Molecular basis for structural heterogeneity of an intrinsically disordered protein bound to a partner by combined ESI-IM-MS and modeling. <i> D'Urzo A, Konijnenberg A, Rossetti G, Habchi J, Li J, Carloni P, Sobott F, Longhi S, Grandori R. </i> J Am Soc Mass Spectrom, 2015","reference_id":"25510932","region_id":"DP04423r076","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The spectra are dominated by the peaks of the free proteins, but signals specific to the NTAIL–PXD complex become evident at the higher protein concentration. The measured mass of the complex (21,187.4 ± 0.61 Da) corresponds closely to the sum of the theoretical values expected for NTAIL with the initial methionine and PXD without the initial methionine (21,187.46 Da), indicating a 1:1 stoichiometry.","_id":"6856af027cd61eccdacd5d9d"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T14:03:56.812Z","_id":"6856af027cd61eccdacd5d9e"},"version":1,"_id":"6856af027cd61eccdacd5d9b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":401,"end":525,"interaction_partner":[{"db":"UniProt","id":"P03422","partner_start":null,"partner_end":null,"_id":"6856af027cd61eccdacd5da0"}],"reference_html":"Solution structure of the C-terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-terminal domain of the nucleoprotein. <i> Gely S, Lowry DF, Bernard C, Jensen MR, Blackledge M, Costanzo S, Bourhis JM, Darbon H, Daughdrill G, Longhi S. </i> J Mol Recognit, 2010","reference_id":"20058326","region_id":"DP04423r077","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Intermediate exchange between NTAIL and XD, especially at the binding interface, caused significant peak broadening thus reducing the number of resonance assignments possible for the NTAIL–XD complex.","_id":"6856af027cd61eccdacd5da1"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T14:03:54.125Z","_id":"6856af027cd61eccdacd5da2"},"version":1,"_id":"6856af027cd61eccdacd5d9f","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":475,"end":525,"interaction_partner":[{"db":"UniProt","id":"P03422","partner_start":null,"partner_end":null,"_id":"6856af027cd61eccdacd5da4"}],"reference_html":"Solution structure of the C-terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-terminal domain of the nucleoprotein. <i> Gely S, Lowry DF, Bernard C, Jensen MR, Blackledge M, Costanzo S, Bourhis JM, Darbon H, Daughdrill G, Longhi S. </i> J Mol Recognit, 2010","reference_id":"20058326","region_id":"DP04423r078","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"At low XD concentrations (0.037, 0.075, and 0.150 mM), most resonances in the HSQC experience no chemical shift changes (residues 401–474), some resonances undergo fast exchange and experience chemical shift changes with minimal line broadening (residues 475–482 and residues 507–525), and some resonances undergo intermediate exchange and experience significant line broadening (residues 483–506). ","_id":"6856af027cd61eccdacd5da5"},{"type":"Results","text":"For all the affected resonances (residues 475–525), small chemical shift differences were observed when increasing the XD concentration from 0.3 to 0.6 mM, suggesting that binding is saturated.","_id":"6856af027cd61eccdacd5da6"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-09-28T14:03:29.787Z","_id":"6856af027cd61eccdacd5da7"},"version":1,"_id":"6856af027cd61eccdacd5da3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":485,"end":505,"interaction_partner":[{"db":"UniProt","id":"P03422","partner_start":457,"partner_end":507,"_id":"6856af027cd61eccdacd5da9"}],"reference_html":"Measles virus nucleo- and phosphoproteins form liquid-like phase-separated compartments that promote nucleocapsid assembly. <i> Guseva S, Milles S, Jensen MR, Salvi N, Kleman JP, Maurin D, Ruigrok RWH, Blackledge M. </i> Sci Adv, 2020","reference_id":"32270045","region_id":"DP04423r079","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The sole intermolecular hydrogen bonding interaction observed in a chimeric crystal structure of N486–505:PXD involves S491 of NTAIL interacting with K489 and D493 of PXD (7). Mutation of N (S491) has been shown to abrogate the NTAIL:PXD interaction—this is also the case under our experimental conditions (Fig. 3D)—and to significantly decrease viral transcription in vivo (11). The critical nature of this interaction for LLPS was demonstrated via the S491L mutation, which resulted in suppression of phase separation.","_id":"6856af027cd61eccdacd5daa"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_go_domain":"F","term_id":"GO:0005515","term_is_binding":true,"term_is_obsolete":false,"term_name":"protein binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-22T13:07:53.585Z","_id":"6856af027cd61eccdacd5dab"},"version":1,"_id":"6856af027cd61eccdacd5da8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"0000-0003-2206-9968","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0005642","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":485,"end":505,"interaction_partner":[],"reference_html":"Measles virus nucleo- and phosphoproteins form liquid-like phase-separated compartments that promote nucleocapsid assembly. <i> Guseva S, Milles S, Jensen MR, Salvi N, Kleman JP, Maurin D, Ruigrok RWH, Blackledge M. </i> Sci Adv, 2020","reference_id":"32270045","region_id":"DP04423r080","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The sole intermolecular hydrogen bonding interaction observed in a chimeric crystal structure of N486–505:PXD involves S491 of NTAIL interacting with K489 and D493 of PXD (7). Mutation of N (S491) has been shown to abrogate the NTAIL:PXD interaction—this is also the case under our experimental conditions (Fig. 3D)—and to significantly decrease viral transcription in vivo (11). The critical nature of this interaction for LLPS was demonstrated via the S491L mutation, which resulted in suppression of phase separation.","_id":"6856af027cd61eccdacd5dad"}],"states_connection":[],"term_comment":"","term_def":"\"Binding and bringing together two or more macromolecules in contact, permitting those molecules to organize as a molecular condensate.\" [PMID:28225081]","term_go_domain":"F","term_id":"GO:0140693","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular condensate scaffold activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-10-22T13:07:01.556Z","_id":"6856af027cd61eccdacd5dae"},"version":1,"_id":"6856af027cd61eccdacd5dac","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","date":"2022-04-25T09:11:24.524Z","disprot_namespace":"Structural state","ec_id":"ECO:0001184","ec_name":"gel-filtration evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":525,"interaction_partner":[],"reference_html":"Distribution of Charged Residues Affects the Average Size and Shape of Intrinsically Disordered Proteins. <i> Bianchi G, Mangiagalli M, Barbiroli A, Longhi S, Grandori R, Santambrogio C, Brocca S. </i> Biomolecules, 2022","reference_id":"35454150","region_id":"DP04423r081","released":"2022_06","sample":[],"statement":[{"type":"Results","text":"Size-exclusion chromatography was employed to estimate the Rh values of the three sets of model IDPs (Table 2). Experimental Rh values of wt NTAIL and wt PNT4 (2.71 ± 0.09 and 2.34 ± 0.11 nm, respectively) are close to the theoretical ones (Table 1) and similar to the previously determined ones [9].","_id":"6856af027cd61eccdacd5db0"},{"type":"Curator statement","text":"Experimentally determined Rh matches the theoretical Rh for IDPs [Marsh & Forman-Kay, 2010].","_id":"6856af027cd61eccdacd5db1"},{"type":"Table","text":"Rt (nm) = 2.64","_id":"6856af027cd61eccdacd5db2"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2022-04-28T13:32:50.228Z","_id":"6856af027cd61eccdacd5db3"},"version":0,"_id":"6856af027cd61eccdacd5daf","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","date":"2022-04-25T09:11:43.640Z","disprot_namespace":"Structural state","ec_id":"ECO:0006283","ec_name":"electrospray ionization fourier transform ion cyclotron resonance mass spectrometry evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":525,"interaction_partner":[],"reference_html":"Distribution of Charged Residues Affects the Average Size and Shape of Intrinsically Disordered Proteins. <i> Bianchi G, Mangiagalli M, Barbiroli A, Longhi S, Grandori R, Santambrogio C, Brocca S. </i> Biomolecules, 2022","reference_id":"35454150","region_id":"DP04423r082","released":"2022_06","sample":[],"statement":[{"type":"Results","text":"Native MS was employed to assess the conformational properties of the three sets of IDPs. In this approach, the CSDs resulting from the nanoESI process reflect the overall compactness and relative amounts of the main conformers in the original solution [17,18,22]. Native-MS spectra obtained under non-denaturing conditions for the three variants of NTAIL (Figure 4a), NFM, and PNT4 (Figure S3) display multimodal CSDs, highlighting the heterogeneous conformational ensemble typical of IDPs.","_id":"6856af027cd61eccdacd5db5"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2022-04-28T13:32:51.394Z","_id":"6856af027cd61eccdacd5db6"},"version":0,"_id":"6856af027cd61eccdacd5db4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"tlazar","curator_name":"Tamas Lazar","curator_orcid":"0000-0001-7496-6711","date":"2022-04-25T09:11:54.705Z","disprot_namespace":"Structural state","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":400,"end":525,"interaction_partner":[],"reference_html":"Distribution of Charged Residues Affects the Average Size and Shape of Intrinsically Disordered Proteins. <i> Bianchi G, Mangiagalli M, Barbiroli A, Longhi S, Grandori R, Santambrogio C, Brocca S. </i> Biomolecules, 2022","reference_id":"35454150","region_id":"DP04423r083","released":"2022_06","sample":[],"statement":[{"type":"Supplementary material","text":"Figure S2. Far-UV CD spectra of model IDPs. CD spectra of NTAIL (a), NFM (b), and PNT4 (c) variants.","_id":"6856af027cd61eccdacd5db8"},{"type":"Curator statement","text":"Typical random coil-like far-UV CD spectrum is displayed for NTAIL.","_id":"6856af027cd61eccdacd5db9"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2022-04-28T13:32:53.341Z","_id":"6856af027cd61eccdacd5dba"},"version":0,"_id":"6856af027cd61eccdacd5db7","reference_source":"pmid"}],"__v":0,"disorder_content":0.24,"disprot_consensus":{"full":[{"start":400,"end":525,"type":"T"}],"Structural state":[{"start":400,"end":525,"type":"D"}],"Structural transition":[{"start":400,"end":525,"type":"T"}],"Molecular function":[{"start":400,"end":525,"type":"F"}],"Disorder function":[{"start":401,"end":525,"type":"F"}]}},{"acc":"A0A5P8YHT8","sequence":"MRYNRNHMLTLMFSLLIFDAYANEPKVCFYMDDDYNGESLCAAQGNSVASIPDKWNDRISSISIPHGLVVTVYEDVDFLGASRSFEADVDLVSDKDLIYLNDNISAFKIKKAVCFYGESNFTGDSLCLSSGEQFDLYRGNYPERKQSHLVNPLNDEVYSIKIPPGMQTTVYEDDDYNGKYFVLTEDYTPDDLLIIRMNNKISSMRVSQDEDFICDRFCSIKKSIKFKIQKSFGSYWIDPRIKYRDILLDFQLSDTDDYSIKFFDEGLIKVKNYKLFFFDGNEKHGEGFLFNLSDKSSNLSFLLRFNGGFFQIQFVESLNNEIVYSSPLIGTLFDDANSDVIFDINNVDANSPIVIDKMVLTVGKEHNRAERSTLGLATCWAIPILSIYNYIVQGHCNQADKFVHNAADFFGSPADKILQIFGSSLPLPPKNSNETLDDESALINFMSDVKGTLTYITTNMGEHALTVPATALACKASMREKILPHLRNRRDLAPGCIDWTLSILTDFTLLFGASIEYWNSKNFGRVIENIVREGEIGSAVADVDTASRLIESVQAHVAEATEVADIIHLKTAFDFSQLSYVSYVRHTEEEVVSPQSAQALPLGRYELALVDYHFIETVPRIRQDGRWVERPDLHFDIEVISGVPEETDASRQVLLPIIEAWQHSYSQQELLFHASDILPESSLARYEIEPLLEASRLTSEVAISWLRTSRDDFVYVVVRLEGEVISLTMAVDININDVGVAGSLTNPDYVITPNAEGAVRGAGTAAIRALADHFKRKGKISLVSSVISQPSAIVKKKVGFRFIEEL","creator":"System-ahatos","dataset":[],"date":"2025-06-21T12:56:57.272Z","disprot_id":"DP04425","features":{"pfam":[{"id":"PF08964","name":"Beta/Gamma crystallin","start":25,"end":90},{"id":"PF09101","name":"Exotoxin A binding","start":354,"end":403}]},"genes":[{"synonyms":[],"olnNames":[{"value":"YPO2884","evidences":[],"_id":"6856ac197cd61eccdacd5c00"}],"orfNames":[],"_id":"6856ac197cd61eccdacd5bff"}],"length":806,"name":"Exported protein","ncbi_taxon_id":632,"organism":"Yersinia pestis","regions_counter":21,"released":"2025_06","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Yersiniaceae","Yersinia"],"regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":21,"end":112,"interaction_partner":[],"reference_html":"Calcium-binding crystallins from Yersinia pestis. Characterization of two single betagamma-crystallin domains of a putative exported protein. <i> Jobby MK, Sharma Y. </i> J Biol Chem, 2005","reference_id":"15536081","region_id":"DP04425r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Far-UV CD of apoD1 showed a large negative ellipticity peak at 200 nm, suggesting that the protein is intrinsically unstructured (44), which disappeared on calcium addition and emerged as a positive peak (Fig. 7a).","_id":"6856af067cd61eccdacd5de1"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-06T10:36:49.235Z","_id":"6856af067cd61eccdacd5de2"},"version":3,"_id":"6856af067cd61eccdacd5de0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":21,"end":112,"interaction_partner":[{"db":"ChEBI","id":"29108","partner_start":null,"partner_end":null,"_id":"6856af067cd61eccdacd5de5"}],"reference_html":"Calcium-binding crystallins from Yersinia pestis. Characterization of two single betagamma-crystallin domains of a putative exported protein. <i> Jobby MK, Sharma Y. </i> J Biol Chem, 2005","reference_id":"15536081","region_id":"DP04425r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Calcium binding to D1 increased β-sheet content by 2-fold to 42.4%, largely at the expense of the unordered fraction, which reduced to 29.66%.","_id":"6856af067cd61eccdacd5de4"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","term_id":"GO:0043167","term_is_binding":true,"term_is_obsolete":false,"term_name":"ion binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-06T10:36:36.377Z","_id":"6856af067cd61eccdacd5de6"},"version":4,"_id":"6856af067cd61eccdacd5de3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":21,"end":112,"interaction_partner":[],"reference_html":"Calcium-binding crystallins from Yersinia pestis. Characterization of two single betagamma-crystallin domains of a putative exported protein. <i> Jobby MK, Sharma Y. </i> J Biol Chem, 2005","reference_id":"15536081","region_id":"DP04425r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Calcium binding to D1 increased β-sheet content by 2-fold to 42.4%, largely at the expense of the unordered fraction, which reduced to 29.66%.","_id":"6856af067cd61eccdacd5de8"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-06T10:36:41.389Z","_id":"6856af067cd61eccdacd5de9"},"version":3,"_id":"6856af067cd61eccdacd5de7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006206","ec_name":"near-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":21,"end":112,"interaction_partner":[],"reference_html":"Calcium-binding crystallins from Yersinia pestis. Characterization of two single betagamma-crystallin domains of a putative exported protein. <i> Jobby MK, Sharma Y. </i> J Biol Chem, 2005","reference_id":"15536081","region_id":"DP04425r004","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Near-UV CD of apoD1 showed a very weak signal, confirming that the protein was in an unstructured state.","_id":"6856af067cd61eccdacd5deb"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-06T10:36:47.983Z","_id":"6856af067cd61eccdacd5dec"},"version":3,"_id":"6856af067cd61eccdacd5dea","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006206","ec_name":"near-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":21,"end":112,"interaction_partner":[{"db":"ChEBI","id":"29108","partner_start":null,"partner_end":null,"_id":"6856af067cd61eccdacd5def"}],"reference_html":"Calcium-binding crystallins from Yersinia pestis. Characterization of two single betagamma-crystallin domains of a putative exported protein. <i> Jobby MK, Sharma Y. </i> J Biol Chem, 2005","reference_id":"15536081","region_id":"DP04425r005","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Upon the addition of calcium, two strong bands emerged in the spectra of the holoprotein, one at ∼290 nm for the 1Lb band of Trp and a broad peak ∼255–270 nm, with peaks at 262 and 268 nm characteristic of Phe (Fig. 8).","_id":"6856af067cd61eccdacd5dee"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","term_id":"GO:0043167","term_is_binding":true,"term_is_obsolete":false,"term_name":"ion binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-06T10:36:35.086Z","_id":"6856af067cd61eccdacd5df0"},"version":4,"_id":"6856af067cd61eccdacd5ded","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0006206","ec_name":"near-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":21,"end":112,"interaction_partner":[],"reference_html":"Calcium-binding crystallins from Yersinia pestis. Characterization of two single betagamma-crystallin domains of a putative exported protein. <i> Jobby MK, Sharma Y. </i> J Biol Chem, 2005","reference_id":"15536081","region_id":"DP04425r006","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Upon the addition of calcium, two strong bands emerged in the spectra of the holoprotein, one at ∼290 nm for the 1Lb band of Trp and a broad peak ∼255–270 nm, with peaks at 262 and 268 nm characteristic of Phe (Fig. 8).","_id":"6856af067cd61eccdacd5df2"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-06T10:36:40.421Z","_id":"6856af067cd61eccdacd5df3"},"version":3,"_id":"6856af067cd61eccdacd5df1","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":110,"end":215,"interaction_partner":[],"reference_html":"Calcium-binding crystallins from Yersinia pestis. Characterization of two single betagamma-crystallin domains of a putative exported protein. <i> Jobby MK, Sharma Y. </i> J Biol Chem, 2005","reference_id":"15536081","region_id":"DP04425r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Far-UV CD spectra of domain D2 showed a negative trough at ∼200 nm with a negative peak at 220 nm (Fig. 7b). The secondary structure analysis of the spectra showed that the protein had 31.83% β-sheet, 35.2% unordered, and 23% turns, with 9.6% helix (Table II).","_id":"6856af067cd61eccdacd5df5"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-06T10:36:46.573Z","_id":"6856af067cd61eccdacd5df6"},"version":3,"_id":"6856af067cd61eccdacd5df4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006206","ec_name":"near-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":110,"end":215,"interaction_partner":[],"reference_html":"Calcium-binding crystallins from Yersinia pestis. Characterization of two single betagamma-crystallin domains of a putative exported protein. <i> Jobby MK, Sharma Y. </i> J Biol Chem, 2005","reference_id":"15536081","region_id":"DP04425r009","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Near-UV CD of the D2 domain showed a broad band between 280 and 290 nm for Trp and Tyr with weak ellipticity (data not shown).","_id":"6856af067cd61eccdacd5dfa"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-06T10:36:45.964Z","_id":"6856af067cd61eccdacd5dfb"},"version":3,"_id":"6856af067cd61eccdacd5df9","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":110,"end":215,"interaction_partner":[],"reference_html":"Purification of a crystallin domain of Yersinia crystallin from inclusion bodies and its comparison to native protein from the soluble fraction. <i> Jobby MK, Sharma Y. </i> Biomed Chromatogr, 2006","reference_id":"16470515","region_id":"DP04425r011","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"As shown in Fig. 6 (spectrum 1), the far-UV CD spectrum of D2 purified from inclusion bodies resembles that of a poorly folded protein with low regular secondary structure content.","_id":"6856af067cd61eccdacd5dff"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-06T10:36:44.453Z","_id":"6856af067cd61eccdacd5e00"},"version":3,"_id":"6856af067cd61eccdacd5dfe","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"IDA","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":110,"end":215,"interaction_partner":[],"reference_html":"Purification of a crystallin domain of Yersinia crystallin from inclusion bodies and its comparison to native protein from the soluble fraction. <i> Jobby MK, Sharma Y. </i> Biomed Chromatogr, 2006","reference_id":"16470515","region_id":"DP04425r013","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"When D2 purified from inclusion bodies is excited at 295 nm it shows fluorescence emission maxima at 350 nm, indicating that the engineered Trp is solvent-exposed (Fig. 5, spectrum 1).","_id":"6856af067cd61eccdacd5e04"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-06T10:36:43.085Z","_id":"6856af067cd61eccdacd5e05"},"version":3,"_id":"6856af067cd61eccdacd5e03","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":110,"end":215,"interaction_partner":[{"db":"ChEBI","id":"29108","partner_start":null,"partner_end":null,"_id":"6856af067cd61eccdacd5e08"}],"reference_html":"Purification of a crystallin domain of Yersinia crystallin from inclusion bodies and its comparison to native protein from the soluble fraction. <i> Jobby MK, Sharma Y. </i> Biomed Chromatogr, 2006","reference_id":"16470515","region_id":"DP04425r014","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Calcium mimic dye Stains-all was used to probe calcium binding to D2 purified from insoluble fraction. As shown in Fig. 4, the dye–protein complex gives rise to a characteristic peak at 660 nm in the CD spectra. The intensity at 660 nm decreased upon calcium addition, indicating displacement of dye and calcium-binding to the protein. These results suggest that the refolded protein is able to bind calcium and is functionally active.","_id":"6856af067cd61eccdacd5e07"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","term_id":"GO:0043167","term_is_binding":true,"term_is_obsolete":false,"term_name":"ion binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-06T10:36:32.541Z","_id":"6856af067cd61eccdacd5e09"},"version":4,"_id":"6856af067cd61eccdacd5e06","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0007009","ec_name":"radioligand binding assay evidence used in manual assertion","ec_ontology":"ECO","start":110,"end":215,"interaction_partner":[{"db":"ChEBI","id":"29108","partner_start":null,"partner_end":null,"_id":"6856af067cd61eccdacd5e0c"}],"reference_html":"Calcium-binding crystallins from Yersinia pestis. Characterization of two single betagamma-crystallin domains of a putative exported protein. <i> Jobby MK, Sharma Y. </i> J Biol Chem, 2005","reference_id":"15536081","region_id":"DP04425r015","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Direct assay using radioactive 45Ca revealed that both domains, D1 and D2, bind calcium as shown in Fig. 5.","_id":"6856af067cd61eccdacd5e0b"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","term_id":"GO:0043167","term_is_binding":true,"term_is_obsolete":false,"term_name":"ion binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-06T10:36:28.061Z","_id":"6856af067cd61eccdacd5e0d"},"version":3,"_id":"6856af067cd61eccdacd5e0a","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IPI","ec_id":"ECO:0007009","ec_name":"radioligand binding assay evidence used in manual assertion","ec_ontology":"ECO","start":21,"end":112,"interaction_partner":[{"db":"ChEBI","id":"29108","partner_start":null,"partner_end":null,"_id":"6856af067cd61eccdacd5e0f"}],"reference_html":"Calcium-binding crystallins from Yersinia pestis. Characterization of two single betagamma-crystallin domains of a putative exported protein. <i> Jobby MK, Sharma Y. </i> J Biol Chem, 2005","reference_id":"15536081","region_id":"DP04425r016","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Direct assay using radioactive 45Ca revealed that both domains, D1 and D2, bind calcium as shown in Fig. 5.","_id":"6856af067cd61eccdacd5e10"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","term_id":"GO:0043167","term_is_binding":true,"term_is_obsolete":false,"term_name":"ion binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-06T10:36:29.558Z","_id":"6856af067cd61eccdacd5e11"},"version":3,"_id":"6856af067cd61eccdacd5e0e","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-12-06T10:36:25.126Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":21,"end":112,"interaction_partner":[],"reference_html":"Calcium-binding crystallins from Yersinia pestis. Characterization of two single betagamma-crystallin domains of a putative exported protein. <i> Jobby MK, Sharma Y. </i> J Biol Chem, 2005","reference_id":"15536081","region_id":"DP04425r019","released":"2022_12","sample":[],"statement":[{"type":"Results","text":"The presence of calcium drastically decreased the hydrodynamic volume, and the elution volume corresponds to a monomer (Fig. 10a). Thus, there is significant change in the Stokes radius of the D1 upon calcium binding, which could be attributed to the transition of the protein from an unstructured to a structured state and the resulting compaction (44, 46).","_id":"6856af067cd61eccdacd5e19"}],"states_connection":[],"term_comment":"","term_def":"\"The selective interaction of a protein with a calcium ion to prevent it from interacting with other partners or inhibiting its localization to other areas of the cell.\" [PMID:13130076]","term_id":"GO:0140314","term_is_binding":false,"term_is_obsolete":false,"term_name":"calcium ion sequestering activity","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2024-07-03T15:29:07.415Z","_id":"6856af067cd61eccdacd5e1a"},"version":4,"_id":"6856af067cd61eccdacd5e18","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural transition","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":21,"end":112,"interaction_partner":[],"reference_html":"Calcium-binding crystallins from Yersinia pestis. Characterization of two single betagamma-crystallin domains of a putative exported protein. <i> Jobby MK, Sharma Y. </i> J Biol Chem, 2005","reference_id":"15536081","region_id":"DP04425r020","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The presence of calcium drastically decreased the hydrodynamic volume, and the elution volume corresponds to a monomer (Fig. 10a). Thus, there is significant change in the Stokes radius of the D1 upon calcium binding, which could be attributed to the transition of the protein from an unstructured to a structured state and the resulting compaction (44, 46).","_id":"6856af067cd61eccdacd5e1c"}],"states_connection":[],"term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","term_ontology":"IDPO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-06T10:36:38.149Z","_id":"6856af067cd61eccdacd5e1d"},"version":2,"_id":"6856af067cd61eccdacd5e1b","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0007680","ec_name":"chromatography evidence used in manual assertion","ec_ontology":"ECO","start":21,"end":112,"interaction_partner":[{"db":"ChEBI","id":"29108","partner_start":null,"partner_end":null,"_id":"6856af067cd61eccdacd5e1f"}],"reference_html":"Calcium-binding crystallins from Yersinia pestis. Characterization of two single betagamma-crystallin domains of a putative exported protein. <i> Jobby MK, Sharma Y. </i> J Biol Chem, 2005","reference_id":"15536081","region_id":"DP04425r021","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The presence of calcium drastically decreased the hydrodynamic volume, and the elution volume corresponds to a monomer (Fig. 10a). Thus, there is significant change in the Stokes radius of the D1 upon calcium binding, which could be attributed to the transition of the protein from an unstructured to a structured state and the resulting compaction (44, 46).","_id":"6856af067cd61eccdacd5e20"}],"states_connection":[],"term_comment":"","term_def":"\"Binding to an ion, a charged atoms or groups of atoms.\" [GOC:jl]","term_id":"GO:0043167","term_is_binding":true,"term_is_obsolete":false,"term_name":"ion binding","term_namespace":"Molecular function","term_not_annotate":false,"term_ontology":"GO","validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-06T10:36:26.516Z","_id":"6856af067cd61eccdacd5e21"},"version":3,"_id":"6856af067cd61eccdacd5e1e","reference_source":"pmid"}],"__v":0,"disorder_content":0.24193548387096775,"disprot_consensus":{"full":[{"start":21,"end":112,"type":"T"},{"start":113,"end":215,"type":"D"}],"Structural state":[{"start":21,"end":215,"type":"D"}],"Molecular function":[{"start":21,"end":215,"type":"F"}],"Structural transition":[{"start":21,"end":112,"type":"T"}]}},{"acc":"A0A6L8PPD0","sequence":"MSTQTSRVTLVGEMLPAYNEILTPEALSFLKELHENFNERRIELLQKRMKKQQKIDAGEFPKFLEETKRIREADWTIAKLPKDLEDRRVEITGPVDRKMVINALNSGAHLFMADFEDSNSPTWENAIEGQINLRDAVKGTISHKNENGKEYRLNSKTAVLIVRPRGWHLEEKHMQVDGKNMSGSLVDFGLYFFHNAKALLEKGSGPYFYLPKMESYLEARLWNDVFVFAQKYIGIPNGTIKATVLLETIHASFEMDEILYELKDHSAGLNCGRWDYIFSFLKAFRNHNEFLLPDRAQVTMTAPFMRAYSLKVIQTCHRRNAPAIGGMAAQIPIKNNPEANEAAFEKVRADKEREALDGHDGTWVAHPGLVPVAMEVFNHIMKTPNQIFRKREEIHVTEKDLLEVPVGTITEEGLRMNISVGIQYIASWLSGRGAAPIYNLMEDAATAEISRAQVWQWIRHEGGKLNDGRNITLELMEELKEEELAKIEREIGKEAFKKGRFQEATTLFTNLVRNDEFVPFLTLPGYEIL","creator":"System-fquaglia","dataset":[],"date":"2025-06-21T12:56:58.189Z","disprot_id":"DP04426","features":{"pfam":[{"id":"PF01274","name":"Malate synthase, TIM barrel domain","start":159,"end":403},{"id":"PF20656","name":"Malate synthase, N-terminal domain","start":8,"end":68},{"id":"PF20659","name":"Malate synthase, C-terminal","start":409,"end":527}]},"genes":[{"name":{"value":"aceB","evidences":[{"source":{"id":"AAT30225.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/AAT30225.1","_id":"6856ac1a7cd61eccdacd5c0a"},"code":"ECO:0000313","_id":"6856ac1a7cd61eccdacd5c09"}],"_id":"6856ac1a7cd61eccdacd5c08"},"synonyms":[],"olnNames":[{"value":"GBAA_1131","evidences":[],"_id":"6856ac1a7cd61eccdacd5c0b"}],"orfNames":[],"_id":"6856ac1a7cd61eccdacd5c07"}],"length":529,"name":"Malate synthase","ncbi_taxon_id":1392,"organism":"Bacillus anthracis","regions_counter":1,"released":"2025_06","taxonomy":["Bacteria","Bacillati","Bacillota","Bacilli","Bacillales","Bacillaceae","Bacillus","Bacillus cereus group"],"regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"3CUX","_id":"6856af077cd61eccdacd5e29"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":326,"end":344,"interaction_partner":[],"reference_html":"Atomic resolution structures of Escherichia coli and Bacillus anthracis malate synthase A: comparison with isoform G and implications for structure-based drug discovery. <i> Lohman JR, Olson AC, Remington SJ. </i> Protein Sci, 2008","reference_id":"18714089","region_id":"DP04426r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Residues 326–344 could not be located because of weak electron density, and in the crystal cannot adopt the conformation of the corresponding region of apo ecMSA (residues 329–346) as they would clash with a symmetry mate.","_id":"6856af077cd61eccdacd5e28"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"version":2,"_id":"6856af077cd61eccdacd5e27","reference_source":"pmid"}],"__v":0,"disorder_content":0.035916824196597356,"disprot_consensus":{"full":[{"start":326,"end":344,"type":"D"}],"Structural state":[{"start":326,"end":344,"type":"D"}]}},{"acc":"Q9EU62","sequence":"MSVRTLLAATLVAGISVLAPAGIANAETSMVSTTAASSVEHAANTYDFAEAKSGSSIPAKVAAEQANSYSVHGLVTSLAVYQHFSLTVEGGGKTFTGDSGGISIPGVAVLEGTLFTEDLQHLYSDTVSFEYNAVGPYLNINFFDSHGTLLGHVQSGSIGTVSGIGGGTGGWQ","creator":"System-fquaglia","dataset":[],"date":"2025-06-21T12:56:58.372Z","disprot_id":"DP04427","features":{"pfam":[{"id":"PF05526","name":"Rhodococcus equi virulence-associated protein","start":50,"end":172}]},"genes":[{"name":{"value":"vapG","evidences":[{"source":{"id":"BAB16611.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/BAB16611.1","_id":"6856ac1a7cd61eccdacd5c15"},"code":"ECO:0000313","_id":"6856ac1a7cd61eccdacd5c14"}],"_id":"6856ac1a7cd61eccdacd5c13"},"synonyms":[{"value":"vapL","evidences":[],"_id":"6856ac1a7cd61eccdacd5c16"}],"olnNames":[],"orfNames":[{"value":"GS441_12665","evidences":[],"_id":"6856ac1a7cd61eccdacd5c17"},{"value":"GS453_17490","evidences":[],"_id":"6856ac1a7cd61eccdacd5c18"},{"value":"GS551_24755","evidences":[],"_id":"6856ac1a7cd61eccdacd5c19"},{"value":"GS882_07590","evidences":[],"_id":"6856ac1a7cd61eccdacd5c1a"},{"value":"GS947_23845","evidences":[],"_id":"6856ac1a7cd61eccdacd5c1b"},{"value":"pVAPA_vapG","evidences":[],"_id":"6856ac1a7cd61eccdacd5c1c"}],"_id":"6856ac1a7cd61eccdacd5c12"}],"length":172,"name":"R. equi VapG protein","ncbi_taxon_id":43767,"organism":"Rhodococcus hoagii","regions_counter":1,"released":"2025_06","taxonomy":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Nocardiaceae","Prescottella"],"regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"5AEO","_id":"6856af077cd61eccdacd5e39"}],"curator_id":"fquaglia","curator_name":"Federica Quaglia","curator_orcid":"0000-0002-0341-4888","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":27,"end":66,"interaction_partner":[],"reference_html":"Structural characterisation of the virulence-associated protein VapG from the horse pathogen Rhodococcus equi. <i> Okoko T, Blagova EV, Whittingham JL, Dover LG, Wilkinson AJ. </i> Vet Microbiol, 2015","reference_id":"25746683","region_id":"DP04427r001","released":"2022_03","sample":[],"statement":[{"type":"Abstract","text":"Electron density corresponding to the N-terminal domain was not visible suggesting that it is disordered.","_id":"6856af077cd61eccdacd5e36"},{"type":"Results","text":"The low complexity N-terminal regions (residues up to and including Asn41 of chain A, and Ala40 of chain B) were not visible in the electron density maps. These residues were assumed, therefore, to be disordered.","_id":"6856af077cd61eccdacd5e37"},{"type":"Conclusion","text":"The Vap proteins of R. equi consist of β-barrel domains with disordered regions at their N-termini.","_id":"6856af077cd61eccdacd5e38"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","version":2,"_id":"6856af077cd61eccdacd5e35","reference_source":"pmid"}],"__v":0,"disorder_content":0.23255813953488372,"disprot_consensus":{"full":[{"start":27,"end":66,"type":"D"}],"Structural state":[{"start":27,"end":66,"type":"D"}]}},{"acc":"A0A8I6XZQ2","sequence":"MIMSDPAMLPPGFRFHPTDEELILHYLRNRAAQSPCPVSIIADVDIYKFDPWALPSKASYGDREWYFFTPRDRKYPNGVRPNRAAGSGYWKATGTDKPIRCSATGESVGVKKALVFYKGRPPKGIKTNWIMHEYRLAAADAHAANTYRPMKFRNASMRLDDWVLCRIYKKTSQVSPMAVPPLSDHELDEPSGAGAYPMSSAGMTMQGGAGGYTLQAAVPGTQRMPKIPSISELLNDYSLAQLFDDSGHALMARHDQHAALFGHPIMSQFHVNSSGNNMSQLGQMDSPASTSVARDGAAGKRKRLSEEDGEHNGSTSQPAAAVTNKKPNSSCFGATTFQVGNNTLQGSLGQPLLHF","creator":"System-jssuarez","dataset":[],"date":"2025-06-21T12:56:58.531Z","disprot_id":"DP04428","features":{"pfam":[{"id":"PF02365","name":"No apical meristem (NAM) protein","start":10,"end":136}]},"genes":[],"length":355,"name":"NAC domain-containing protein","ncbi_taxon_id":112509,"organism":"Hordeum vulgare subsp. vulgare","regions_counter":3,"released":"2025_06","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","BOP clade","Pooideae","Triticodae","Triticeae","Hordeinae","Hordeum"],"regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006204","ec_name":"far-UV circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":173,"end":355,"interaction_partner":[],"reference_html":"Senescence-associated barley NAC (NAM, ATAF1,2, CUC) transcription factor interacts with radical-induced cell death 1 through a disordered regulatory domain. <i> Kjaersgaard T, Jensen MK, Christiansen MW, Gregersen P, Kragelund BB, Skriver K. </i> J Biol Chem, 2011","reference_id":"21856750","region_id":"DP04428r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The far-UV CD spectra showed a strong negative absorbance at 200 nm for His6-HvNAC005(173–355), His6-HvNAC013(177–346), and HvNAC013(177–346) with little ellipticity around 220 nm indicating lack of a significant amount of secondary structure and highly characteristic of unstructured proteins (Figs. 6, A and B, and ​77B).","_id":"6856af077cd61eccdacd5e3e"},{"type":"Curator statement","text":"HvNAC005 correspond to Hordeum vulgare NAC domain-containing protein.","_id":"6856af077cd61eccdacd5e3f"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-12-02T13:54:48.079Z","_id":"6856af077cd61eccdacd5e3d"},"version":2,"_id":"6856af077cd61eccdacd5e3c","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IMP","ec_id":"ECO:0007089","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","ec_ontology":"ECO","start":172,"end":355,"interaction_partner":[],"reference_html":"Barley plants over-expressing the NAC transcription factor gene HvNAC005 show stunting and delay in development combined with early senescence. <i> Christiansen MW, Matthewman C, Podzimska-Sroka D, O'Shea C, Lindemose S, Møllegaard NE, Holme IB, Hebelstrup K, Skriver K, Gregersen PL. </i> J Exp Bot, 2016","reference_id":"27436280","region_id":"DP04428r002","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"When adenine was added to the plates, both full-length HvNAC005, HvNAC005(1–355), and the HvNAC005 C-terminus, HvNAC005(172–355), were able to activate transcription of the reporter gene HIS3, as measured by the ability of transformed yeast to grow in the absence of histidine (Fig. 3B). By contrast and, as expected, the NAC domain, HvNAC005(1–172) alone was unable to activate transcription.","_id":"6856af077cd61eccdacd5e42"},{"type":"Curator statement","text":"HvNAC005 correspond to Hordeum vulgare NAC domain-containing protein.","_id":"6856af077cd61eccdacd5e43"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","term_id":"GO:0098772","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function regulator","term_namespace":"Molecular function","term_not_annotate":true,"term_ontology":"GO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-12-02T13:55:16.666Z","_id":"6856af077cd61eccdacd5e41"},"version":3,"_id":"6856af077cd61eccdacd5e40","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"jssuarez","curator_name":"Jaime Santos Suárez","curator_orcid":"0000-0001-9045-7765","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"IMP","ec_id":"ECO:0007089","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","ec_ontology":"ECO","start":172,"end":250,"interaction_partner":[],"reference_html":"Barley plants over-expressing the NAC transcription factor gene HvNAC005 show stunting and delay in development combined with early senescence. <i> Christiansen MW, Matthewman C, Podzimska-Sroka D, O'Shea C, Lindemose S, Møllegaard NE, Holme IB, Hebelstrup K, Skriver K, Gregersen PL. </i> J Exp Bot, 2016","reference_id":"27436280","region_id":"DP04428r003","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"Removal of the SC- and the KR-motifs from both full-length and C-terminal HvNAC005 did not affect the ability to activate transcription (Fig. 3B). By contrast, removal of the LL-motif abolished activity in both cases. ","_id":"6856af077cd61eccdacd5e46"},{"type":"Curator statement","text":"The region 172-250 corresponds to the shorter construct retaining the activator function.","_id":"6856af077cd61eccdacd5e47"}],"states_connection":[],"term_comment":"","term_def":"\"A molecular function regulator regulates the activity of its target via non-covalent binding that does not result in covalent modification to the target. Examples of molecular function regulators include regulatory subunits of multimeric enzymes and channels. Mechanisms of regulation include allosteric changes in the target and competitive inhibition.\" [GOC:dos, GOC:pt]","term_id":"GO:0098772","term_is_binding":true,"term_is_obsolete":false,"term_name":"molecular function regulator","term_namespace":"Molecular function","term_not_annotate":true,"term_ontology":"GO","validated":{"curator_id":"bmesza","curator_name":"Bálint Mészáros","timestamp":"2020-12-03T18:31:48.842Z","_id":"6856af077cd61eccdacd5e45"},"version":3,"_id":"6856af077cd61eccdacd5e44","reference_source":"pmid"}],"__v":0,"disorder_content":0.5154929577464789,"disprot_consensus":{"full":[{"start":172,"end":172,"type":"F"},{"start":173,"end":355,"type":"D"}],"Structural state":[{"start":173,"end":355,"type":"D"}],"Molecular function":[{"start":172,"end":355,"type":"F"}]}},{"acc":"E6MVD9","sequence":"MRTTPTFPTKTFKPTAMALAVATTLSACLGGGGGGTSAPDFNAGGTGIGSNSRATTAKSAAVSYAGIKNEMCKDRSMLCAGRDDVAVTDRDAKINRPPPPNLHTGDFPNPNDAYKNLINLKPAIEAGYTGRGVEVGIVDTGESVGSISFPELYGRKEHGYNENYKNYTAYMRKEAPEDGGGKDIEASFDDEAVIETEAKPTDIRHVKEIGHIDLVSHIIGGRSVDGRPAGGIAPDATLHIMNTNDGTKNEMMVAAIRNAWVKLGERGVRIVNNSFGTTSRAGTADLFQIANSEEQYRQALLDYSGGDKTDEGIRLMQQSDYGNLSYHIRNKNMLFIFSTGNDAQAQPNTYALLPFYEKDAQKGIITVAGVDRSGEKFKREMYGEPGTEPLEYGSNHCGITAMWCLSAPYEASVRFTRTNPIQIAGTSFSAPIVTGTAALLLQKYPWMSNDNLRTTLLTTAQDIGAVGVDSKFGWGLLDAGKAMNGPASFPFGDFTADTKGTSDIAYSFRNDISGTGGLIKKGGSQLQLHGNNTYTGKTIIEGGSLVLYGNNKSDMRVETKGALIYNGAASGGSLNSDGIVYLADTDQSGANETVHIKGSLQLDGKGTLYTRLGKLLKVDGTAIIGGKLYMSARGKGAGYLNSTGRRVPFLSAAKIGQDYSFFTNIETDGGLLASLDSVEKTAGSEGDTLSYYVRRGNAARTASAAAHSAPAGLKHAVEQGGSNLENLMVELDASESSATPETVETAAADRTDMPGIRPYGATFRAAAAVQHANAADGVRIFNSLAATVYADSTAAHADMQGRRLKAVSDGLDHNGTGLRVIAQTQQDGGTWEQGGVEGKMRGSTQTVGIAAKTGENTTAAATLGMGRSTWSENSANAKTDSISLFAGIRHDAGDIGYLKGLFSYGRYKNSISRSTGADEHAEGSVNGTLMQLGALGGVNVPFAATGDLTVEGGLRYDLLKQDAFAEKGSALGWSGNSLTEGTLVGLAGLKLSQPLSDKAVLFATAGVERDLNGRDYTVTGGFTGATAATGKTGARNMPHTRLVAGLGADVEFGNGWNGLARYSYAGSKQYGNHSGRVGVGYRF","creator":"System-esalladini","dataset":["Bacterial virulence-related proteins"],"date":"2025-06-21T12:57:01.077Z","disprot_id":"DP04429","features":{"pfam":[{"id":"PF00082","name":"Subtilase family","start":130,"end":475},{"id":"PF03797","name":"Autotransporter beta-domain","start":832,"end":1062},{"id":"PF12951","name":"Passenger-associated-transport-repeat","start":518,"end":547}]},"genes":[{"name":{"value":"nalP","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/14617158","id":"14617158","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/14617158","_id":"6856ac1d7cd61eccdacd5c30"},"code":"ECO:0000303","_id":"6856ac1d7cd61eccdacd5c2f"}],"_id":"6856ac1d7cd61eccdacd5c2e"},"synonyms":[],"olnNames":[],"orfNames":[{"value":"NMH_0145","evidences":[],"_id":"6856ac1d7cd61eccdacd5c31"}],"_id":"6856ac1d7cd61eccdacd5c2d"}],"length":1083,"name":"Neisserial autotransporter lipoprotein NalP","ncbi_taxon_id":909420,"organism":"Neisseria meningitidis serogroup B / serotype 15 (strain H44/76)","regions_counter":1,"released":"2025_06","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Neisseriaceae","Neisseria"],"regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"1UYO","_id":"6856af097cd61eccdacd5e5c"},{"db":"PDB","id":"1UYN","_id":"6856af097cd61eccdacd5e5d"}],"curator_id":"esalladini","curator_name":"Edoardo Salladini","curator_orcid":"0000-0002-5152-5953","date":"2022-02-16T12:21:41.194Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1021,"end":1035,"interaction_partner":[],"reference_html":"Structure of the translocator domain of a bacterial autotransporter. <i> Oomen CJ, van Ulsen P, van Gelder P, Feijen M, Tommassen J, Gros P. </i> EMBO J, 2004","reference_id":"15014442","region_id":"DP04429r001","released":"2023_12","sample":[],"statement":[{"type":"Figure","text":"Amino acids not visible in the electron density of space group P6122 are indicated in blue.","_id":"6856af097cd61eccdacd5e5e"},{"type":"Figure","text":"In space group C2221, no interpretable electron density was observed for residues 816–817, 834–836, 915–917, 943–945, 972–973 and 1024–1036.","_id":"6856af097cd61eccdacd5e5f"},{"type":"Curator statement","text":"The missing regions corresponds to 1021-1035 in UniProt.","_id":"6856af097cd61eccdacd5e60"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-08-04T17:38:25.578Z","_id":"6856af097cd61eccdacd5e61"},"version":0,"_id":"6856af097cd61eccdacd5e5b","reference_source":"pmid"}],"__v":0,"disorder_content":0.013850415512465374,"disprot_consensus":{"full":[{"start":1021,"end":1035,"type":"D"}],"Structural state":[{"start":1021,"end":1035,"type":"D"}]}},{"acc":"P38829","sequence":"MSEFLNENPDILEENQLPTRKEDSTKDLLLGGFSNEATLERRSLLLKIDHSLKSQVLQDIEVLDKLLSIRIPPELTSDEDSLPAESEDESVAGGGKEEEEPDLIDAQEIYDLIAHISDPEHPLSLGQLSVVNLEDIDVHDSGNQNEMAEVVIKITPTITHCSLATLIGLGIRVRLERSLPPRFRITILLKKGTHDSENQVNKQLNDKERVAAACENEQLLGVVSKMLVTCK","creator":"System-cpintado","dataset":[],"date":"2025-06-21T12:57:01.225Z","disprot_id":"DP04430","features":{"pfam":[{"id":"PF01883","name":"Iron-sulfur cluster assembly protein","start":107,"end":181}]},"genes":[{"synonyms":[],"olnNames":[{"value":"YHR122W","evidences":[],"_id":"6856ac1d7cd61eccdacd5c39"}],"orfNames":[],"_id":"6856ac1d7cd61eccdacd5c38"}],"length":231,"name":"MIP18 family protein YHR122W","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":3,"released":"2025_06","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","date":"2022-04-26T11:15:14.121Z","disprot_namespace":"Structural state","ec_id":"ECO:0006200","ec_name":"circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":102,"interaction_partner":[],"reference_html":"Defining the domains of Cia2 required for its essential function in vivo and in vitro. <i> Vo AT, Fleischman NM, Marquez MD, Camire EJ, Esonwune SU, Grossman JD, Gay KA, Cosman JA, Perlstein DL. </i> Metallomics, 2017","reference_id":"29057997","region_id":"DP04430r001","released":"2023_12","sample":[],"statement":[{"type":"Abstract","text":"Herein, we determine that Cia2 contains five conserved motifs distributed between an intrinsically disordered N-terminal domain and a C-terminal domain of unknown function 59 (DUF59).","_id":"6856af097cd61eccdacd5e67"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-07-07T13:33:31.214Z","_id":"6856af097cd61eccdacd5e68"},"version":0,"_id":"6856af097cd61eccdacd5e66","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","date":"2022-07-08T09:53:17.368Z","disprot_namespace":"Structural state","ec_id":"ECO:0007689","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":102,"interaction_partner":[],"reference_html":"Defining the domains of Cia2 required for its essential function in vivo and in vitro. <i> Vo AT, Fleischman NM, Marquez MD, Camire EJ, Esonwune SU, Grossman JD, Gay KA, Cosman JA, Perlstein DL. </i> Metallomics, 2017","reference_id":"29057997","region_id":"DP04430r003","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"We noticed that both the IMAC purified dtCia2 and refolded Cia2 exhibited aberrantly slow migration in SDS-PAGE.","_id":"6856af097cd61eccdacd5e6e"},{"type":"Results","text":"To determine if the N-terminus is disordered, we removed the first 102 residues (Δ102-Cia2) and refolded the protein from insoluble inclusions. Δ102-Cia2’s SDS-PAGE migration behavior normalized (Fig.2A, lane 3).","_id":"6856af097cd61eccdacd5e6f"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-07-11T12:55:23.602Z","_id":"6856af097cd61eccdacd5e70"},"version":0,"_id":"6856af097cd61eccdacd5e6d","reference_source":"pmid"}],"__v":0,"disorder_content":0.44155844155844154,"disprot_consensus":{"full":[{"start":1,"end":102,"type":"D"}],"Structural state":[{"start":1,"end":102,"type":"D"}]}},{"acc":"A0A936SUR2","sequence":"MIQSLMPERRERPGDPMPKSPSPLEEGGGPRRPETGSPDKDSLLKRMRRVDPKQAERYRQRTGE","creator":"System-rpancsa","dataset":[],"date":"2025-06-21T12:57:01.635Z","disprot_id":"DP04431","features":{"pfam":[]},"genes":[{"name":{"value":"ubact","evidences":[{"source":{"id":"MF_02133","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_02133","_id":"6856ac1d7cd61eccdacd5c43"},"code":"ECO:0000256","_id":"6856ac1d7cd61eccdacd5c42"}],"_id":"6856ac1d7cd61eccdacd5c41"},"synonyms":[],"olnNames":[],"orfNames":[{"value":"IPP12_11960","evidences":[],"_id":"6856ac1d7cd61eccdacd5c44"}],"_id":"6856ac1d7cd61eccdacd5c40"}],"length":64,"name":"Prokaryotic ubiquitin-like protein UBact","ncbi_taxon_id":70125,"organism":"Nitrospira sp","regions_counter":1,"released":"2025_06","taxonomy":["Bacteria","Pseudomonadati","Nitrospirota","Nitrospiria","Nitrospirales","Nitrospiraceae","Nitrospira"],"regions":[{"annotation_extensions":[],"conditions":[{"deviation":"within normal range","statements":[{"type":"Methods","text":"NMR samples of UBact (500 µM) were prepared in 20 mM sodium phosphate pH 6.8, 0.02% (w/v) sodium azide, 5% D2O. NMR experiments were acquired at 23 °C on a Bruker Avance III 600 MHz spectrometer equipped with TCI cryoprobe using Bruker standard and in-house pulse sequences.","_id":"6856af0a7cd61eccdacd5e78"}],"term_id":"NCIT:C25206","unit_id":"UO:0000027","unit_name":"°C","value":23,"_id":"6856af0a7cd61eccdacd5e77"},{"deviation":"within normal range","statements":[{"type":"Methods","text":"NMR samples of UBact (500 µM) were prepared in 20 mM sodium phosphate pH 6.8, 0.02% (w/v) sodium azide, 5% D2O. NMR experiments were acquired at 23 °C on a Bruker Avance III 600 MHz spectrometer equipped with TCI cryoprobe using Bruker standard and in-house pulse sequences.","_id":"6856af0a7cd61eccdacd5e7a"}],"term_id":"NCIT:C45997","unit_id":"UO:0000196","unit_name":"pH","value":6.8,"_id":"6856af0a7cd61eccdacd5e79"}],"construct_alterations":[],"cross_refs":[{"db":"BMRB","id":"51116","_id":"6856af0a7cd61eccdacd5e7b"}],"curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","date":"2022-06-01T12:09:31.995Z","disprot_namespace":"Structural state","ec_id":"ECO:0006165","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":64,"interaction_partner":[],"reference_html":"Backbone NMR resonance assignment of the intrinsically disordered UBact protein from Nitrospira nitrosa. <i> Bonn SM, Fushman D. </i> Biomol NMR Assign, 2022","reference_id":"35107780","region_id":"DP04431r001","released":"2023_12","sample":[],"statement":[{"type":"Abstract","text":"The 1H–15N HSQC spectrum shows a narrow spread of proton NMR signals, characteristic of an intrinsically disordered protein.","_id":"6856af0a7cd61eccdacd5e7c"},{"type":"Results","text":"The 1H–15N HSQC reveals a narrow spread of amide signals in the proton dimension, a hallmark of disordered proteins (Fig. 1).","_id":"6856af0a7cd61eccdacd5e7d"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-06-07T13:21:06.334Z","_id":"6856af0a7cd61eccdacd5e7e"},"version":0,"_id":"6856af0a7cd61eccdacd5e76","reference_source":"pmid"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":64,"type":"D"}],"Structural state":[{"start":1,"end":64,"type":"D"}]}},{"acc":"A0A3Q8IT45","sequence":"MPAKAAAKPVKPATKAAPKPANKAPAPKAAAAKPVAKAAPKAAAPAVRPASGSSNGVYVKNWGTGSVADATNVFSAAGKVVKVQLRRQRYALVFFENSAAVKKAIDLFNEKEVLGQTVLVVPAKASPKPDAHENSSCVFVSPIFRPSTTKAQVMELFAGVKVQRLRMYRQNFAYAYLDSPAAAKKFVEEKNGTAFRGHTLRVALSARSLEKLRARQEVANVVIAAHRHYKVHERQ","creator":"System-vnugnes","dataset":["Neglected tropical diseases proteins"],"date":"2025-06-21T12:57:01.874Z","disprot_id":"DP04432","features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":73,"end":118}]},"genes":[{"synonyms":[],"olnNames":[],"orfNames":[{"value":"CGC20_33720","evidences":[],"_id":"6856ac1d7cd61eccdacd5c6d"},{"value":"CGC21_19965","evidences":[],"_id":"6856ac1d7cd61eccdacd5c6e"},{"value":"LDBPK_320790","evidences":[],"_id":"6856ac1d7cd61eccdacd5c6f"},{"value":"LdCL_320013500","evidences":[],"_id":"6856ac1d7cd61eccdacd5c70"},{"value":"LDHU3_32.0990","evidences":[],"_id":"6856ac1d7cd61eccdacd5c71"}],"_id":"6856ac1d7cd61eccdacd5c6c"}],"length":235,"name":"RNA binding protein, putative","ncbi_taxon_id":5661,"organism":"Leishmania donovani","regions_counter":1,"released":"2025_06","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Leishmaniinae","Leishmania"],"regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":" 5OSG","_id":"6856af0a7cd61eccdacd5eb2"}],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-09-21T12:57:55.575Z","disprot_namespace":"Structural state","ec_id":"ECO:0006224","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":1,"end":54,"interaction_partner":[],"reference_html":"The cryo-EM Structure of a Novel 40S Kinetoplastid-Specific Ribosomal Protein. <i> Brito Querido J, Mancera-Martínez E, Vicens Q, Bochler A, Chicher J, Simonetti A, Hashem Y. </i> Structure, 2017","reference_id":"29107485","region_id":"DP04432r001","released":"2022_12","sample":[{"db":"UniProt","deviation":null,"id":"Q9NE83","statements":[],"term_id":"IDPO:00485","term_name":"interacting protein","unit_id":"UO:0000063","unit_name":"mM","value":null,"_id":"6856af0a7cd61eccdacd5eb3"},{"db":"RNAcentral","deviation":null,"id":"URS000004D6B4_5661","statements":[],"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_id":"UO:0000023","unit_name":"µg","value":null,"_id":"6856af0a7cd61eccdacd5eb4"}],"statement":[{"type":"Figure","text":"The black dashed line on the left panel represents a most likely flexible 55-aa N-terminal tail (68-aa in TcKSRP), which remained unmodeled due to its lack of density.","_id":"6856af0a7cd61eccdacd5eb5"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2022-12-15T17:40:19.923Z","_id":"6856af0a7cd61eccdacd5eb6"},"version":0,"_id":"6856af0a7cd61eccdacd5eb1","reference_source":"pmid"}],"__v":0,"disorder_content":0.2297872340425532,"disprot_consensus":{"full":[{"start":1,"end":54,"type":"D"}],"Structural state":[{"start":1,"end":54,"type":"D"}]}},{"acc":"P0DXF5","sequence":"MKPTMALKPLVFALAALMAVAAQAGPAEKWKPTPAPTGTVAAAVTDTQVSKDNKFDDTKTLNNAGANGSLSNSKGNLGANIAAGSGNQQDNAAAITSSAGDAATVFAVADIYQESKDNKFTNKGTQNNALLNNSANNSSGNVGVNVAAGQGNQQKNNLAIVTADGKNVAAASNTEQVSLDNHFLNEASSKHSYKPQYVVNNAGLLNSANNASGNIGVNVAAGAGNQQSNTLTLGSGCTVCAAGTGSKLAF","creator":"System-cpintado","dataset":["Condensates-related proteins"],"date":"2025-06-21T12:57:02.021Z","disprot_id":"DP04433","features":{"pfam":[{"id":"PF27129","name":"Functional amyloid protein FapB/FapC family","start":42,"end":233}]},"genes":[{"name":{"value":"fapC","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/20572935","id":"20572935","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/20572935","_id":"6856ac1e7cd61eccdacd5c7b"},"code":"ECO:0000303","_id":"6856ac1e7cd61eccdacd5c7a"}],"_id":"6856ac1e7cd61eccdacd5c79"},"synonyms":[{"value":"HZ99_04090","evidences":[],"_id":"6856ac1e7cd61eccdacd5c7c"},{"value":"PSUK4_00030","evidences":[],"_id":"6856ac1e7cd61eccdacd5c7d"}],"olnNames":[],"orfNames":[],"_id":"6856ac1e7cd61eccdacd5c78"}],"length":250,"name":"Functional amyloid subunit FapC","ncbi_taxon_id":294,"organism":"Pseudomonas fluorescens","regions_counter":5,"released":"2025_06","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Pseudomonadales","Pseudomonadaceae","Pseudomonas"],"regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","date":"2022-11-17T12:32:27.799Z","disprot_namespace":"Structural state","ec_id":"ECO:0001238","ec_name":"nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":250,"interaction_partner":[],"reference_html":"FapA is an intrinsically disordered chaperone for Pseudomonas functional amyloid FapC. <i> Rasmussen HØ, Kumar A, Shin B, Stylianou F, Sewell L, Xu Y, Otzen DE, Skov Pedersen J, Matthews SJ. </i> J Mol Biol, 2022","reference_id":"36368411","region_id":"DP04433r001","released":"2023_12","sample":[],"statement":[{"type":"Abstract","text":"Here we present a comprehensive biophysical and spectroscopy analysis of FapA, FapB and FapC and provide insight into their molecular interactions. We show that all three proteins are primarily disordered with some regions with structural propensities for α-helix and β-sheet. ","_id":"6856af0a7cd61eccdacd5ebe"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-26T15:19:59.441Z","_id":"6856af0a7cd61eccdacd5ebf"},"version":0,"_id":"6856af0a7cd61eccdacd5ebd","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-12-26T15:38:42.452Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007044","ec_name":"transmission electron microscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":250,"interaction_partner":[],"reference_html":"FapA is an Intrinsically Disordered Chaperone for Pseudomonas Functional Amyloid FapC. <i> Rasmussen HØ, Kumar A, Shin B, Stylianou F, Sewell L, Xu Y, Otzen DE, Pedersen JS, Matthews SJ. </i> J Mol Biol, 2022","reference_id":"36368411","region_id":"DP04433r002","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"Negative-stained TEM was used to visualize the fibrils formed in the ThT assays, both FapB and FapC fibrils alone (Figure 5(A) and (B)) as well as FapB and FapC fibrillated with FapA (Figure 5(C) and (D)).","_id":"6856af0a7cd61eccdacd5ec1"}],"states_connection":[],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_id":"GO:1990000","term_is_obsolete":false,"term_name":"amyloid fibril formation","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"6856af0a7cd61eccdacd5ec0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-12-26T15:39:13.726Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":250,"interaction_partner":[],"reference_html":"FapA is an Intrinsically Disordered Chaperone for Pseudomonas Functional Amyloid FapC. <i> Rasmussen HØ, Kumar A, Shin B, Stylianou F, Sewell L, Xu Y, Otzen DE, Pedersen JS, Matthews SJ. </i> J Mol Biol, 2022","reference_id":"36368411","region_id":"DP04433r003","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"Fibrils are clearly seen for all samples, as expected from the observed increase in ThT fluorescence (Figure 3(A), Figure 4(A)).","_id":"6856af0a7cd61eccdacd5ec3"}],"states_connection":[],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_id":"GO:1990000","term_is_obsolete":false,"term_name":"amyloid fibril formation","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"6856af0a7cd61eccdacd5ec2","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","date":"2023-01-09T08:44:57.335Z","disprot_namespace":"Structural state","ec_id":"ECO:0006200","ec_name":"circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":250,"interaction_partner":[],"reference_html":"FapA is an Intrinsically Disordered Chaperone for Pseudomonas Functional Amyloid FapC. <i> Rasmussen HØ, Kumar A, Shin B, Stylianou F, Sewell L, Xu Y, Otzen DE, Pedersen JS, Matthews SJ. </i> J Mol Biol, 2023","reference_id":"36368411","region_id":"DP04433r004","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"CD data show FapA, FapB, and FapC have deep minima around 200 nm (Figure 1(A)), which is typical for a random coil structure.","_id":"6856af0a7cd61eccdacd5ec5"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-01-09T12:47:29.281Z","_id":"6856af0a7cd61eccdacd5ec6"},"version":0,"_id":"6856af0a7cd61eccdacd5ec4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","date":"2023-01-09T08:45:34.668Z","disprot_namespace":"Structural state","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":250,"interaction_partner":[],"reference_html":"FapA is an Intrinsically Disordered Chaperone for Pseudomonas Functional Amyloid FapC. <i> Rasmussen HØ, Kumar A, Shin B, Stylianou F, Sewell L, Xu Y, Otzen DE, Pedersen JS, Matthews SJ. </i> J Mol Biol, 2023","reference_id":"36368411","region_id":"DP04433r005","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"The fitting with the simple Gaussian random coil model is in accordance with the trend of primarily random coil seen in CD.","_id":"6856af0a7cd61eccdacd5ec8"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-01-09T12:48:08.736Z","_id":"6856af0a7cd61eccdacd5ec9"},"version":0,"_id":"6856af0a7cd61eccdacd5ec7","reference_source":"pmid"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":250,"type":"D"}],"Structural state":[{"start":1,"end":250,"type":"D"}],"Biological process":[{"start":1,"end":250,"type":"F"}]}},{"acc":"P0DXF3","sequence":"MATLNQGSLSLLLISCVLGASVSVPASAEDGIIVTGRNVQGFMVGRPSFGKDPYPSTANANPSQQILRATGGELSDNDFAGVSSGSTITRAILPNGDLPGLSNTLGNNSAGLGAGAAAGHASGNSLGGQISGSIERGLAPLNNIGAMMGVQP","creator":"System-cpintado","dataset":["Condensates-related proteins"],"date":"2025-06-21T12:57:02.161Z","disprot_id":"DP04434","features":{"pfam":[{"id":"PF29617","name":"Functional amyloid chaperone FapA","start":4,"end":144}]},"genes":[{"name":{"value":"fapA","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/20572935","id":"20572935","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/20572935","_id":"6856ac1e7cd61eccdacd5c87"},"code":"ECO:0000303","_id":"6856ac1e7cd61eccdacd5c86"}],"_id":"6856ac1e7cd61eccdacd5c85"},"synonyms":[],"olnNames":[],"orfNames":[{"value":"HZ99_04080","evidences":[],"_id":"6856ac1e7cd61eccdacd5c88"},{"value":"PSUK4_00010","evidences":[],"_id":"6856ac1e7cd61eccdacd5c89"}],"_id":"6856ac1e7cd61eccdacd5c84"}],"length":152,"name":"Functional amyloid chaperone FapA","ncbi_taxon_id":294,"organism":"Pseudomonas fluorescens","regions_counter":4,"released":"2025_06","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Pseudomonadales","Pseudomonadaceae","Pseudomonas"],"regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","date":"2022-11-17T12:34:28.901Z","disprot_namespace":"Structural state","ec_id":"ECO:0001238","ec_name":"nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":152,"interaction_partner":[],"reference_html":"FapA is an intrinsically disordered chaperone for Pseudomonas functional amyloid FapC. <i> Rasmussen HØ, Kumar A, Shin B, Stylianou F, Sewell L, Xu Y, Otzen DE, Skov Pedersen J, Matthews SJ. </i> J Mol Biol, 2022","reference_id":"36368411","region_id":"DP04434r001","released":"2023_12","sample":[],"statement":[{"type":"Title","text":"FapA is an intrinsically disordered chaperone for Pseudomonas functional amyloid FapC.","_id":"6856af0a7cd61eccdacd5ed1"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-26T15:19:56.105Z","_id":"6856af0a7cd61eccdacd5ed2"},"version":0,"_id":"6856af0a7cd61eccdacd5ed0","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-12-26T15:52:16.673Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0001249","ec_name":"fluorescence evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":152,"interaction_partner":[],"reference_html":"FapA is an Intrinsically Disordered Chaperone for Pseudomonas Functional Amyloid FapC. <i> Rasmussen HØ, Kumar A, Shin B, Stylianou F, Sewell L, Xu Y, Otzen DE, Pedersen JS, Matthews SJ. </i> J Mol Biol, 2022","reference_id":"36368411","region_id":"DP04434r002","released":"2023_12","sample":[],"statement":[{"type":"Introduction","text":"FapA inhibits FapC fibrillation by targeting the nucleation step, whereas for FapB the elongation step is modulated.","_id":"6856af0a7cd61eccdacd5ed4"},{"type":"Results","text":"For both FapC concentrations, the ThT end level increased at larger FapA concentrations although FapA did not produce a ThT-positive signal in isolation (Figure 3(A)). This suggests that the interactions of ThT with fibrils has changed, most likely due to structural changes in the fibril surface structure.","_id":"6856af0a7cd61eccdacd5ed5"},{"type":"Results","text":"Thus, from both experiments it can be concluded that FapA inhibits FapC fibrillation by increasing tLag but without influencing rElong.","_id":"6856af0a7cd61eccdacd5ed6"},{"type":"Results","text":"Normalized data (Figure 4(B)) clearly show a systematic decrease in rElong (measured as the slope of the normalized curves from 1−4 hours for each triplicate) as a function of FapA concentration (inset of Figure 4(B)). Thus, FapA inhibits FapB fibrillation by reducing rElong but does not lead to a lag phase.","_id":"6856af0a7cd61eccdacd5ed7"}],"states_connection":[],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"Any process that stops, prevents or reduces the frequency, rate or extent of amyloid fibril formation.\" [GO_REF:0000058, GOC:aruk, GOC:bc, GOC:TermGenie, PMID:23106396]","term_id":"GO:1905907","term_is_obsolete":false,"term_name":"negative regulation of amyloid fibril formation","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"version":0,"_id":"6856af0a7cd61eccdacd5ed3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","date":"2023-01-09T08:35:35.083Z","disprot_namespace":"Structural state","ec_id":"ECO:0006200","ec_name":"circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":152,"interaction_partner":[],"reference_html":"FapA is an Intrinsically Disordered Chaperone for Pseudomonas Functional Amyloid FapC. <i> Rasmussen HØ, Kumar A, Shin B, Stylianou F, Sewell L, Xu Y, Otzen DE, Pedersen JS, Matthews SJ. </i> J Mol Biol, 2023","reference_id":"36368411","region_id":"DP04434r003","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"CD data show FapA, FapB, and FapC have deep minima around 200 nm (Figure 1(A)), which is typical for a random coil structure.","_id":"6856af0a7cd61eccdacd5ed9"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-01-09T12:48:18.372Z","_id":"6856af0a7cd61eccdacd5eda"},"version":0,"_id":"6856af0a7cd61eccdacd5ed8","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","date":"2023-01-09T08:47:01.543Z","disprot_namespace":"Structural state","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":152,"interaction_partner":[],"reference_html":"FapA is an Intrinsically Disordered Chaperone for Pseudomonas Functional Amyloid FapC. <i> Rasmussen HØ, Kumar A, Shin B, Stylianou F, Sewell L, Xu Y, Otzen DE, Pedersen JS, Matthews SJ. </i> J Mol Biol, 2023","reference_id":"36368411","region_id":"DP04434r004","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"The fitting with the simple Gaussian random coil model is in accordance with the trend of primarily random coil seen in CD.","_id":"6856af0a7cd61eccdacd5edc"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-01-09T12:48:17.173Z","_id":"6856af0a7cd61eccdacd5edd"},"version":0,"_id":"6856af0a7cd61eccdacd5edb","reference_source":"pmid"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":152,"type":"D"}],"Structural state":[{"start":1,"end":152,"type":"D"}],"Biological process":[{"start":1,"end":152,"type":"F"}]}},{"acc":"P0DXF4","sequence":"MTHSWLLLTVLGCSAAMADSNNQALIDNAGKQYTGVLSVNQAAGNQHQQINSRAISLGGQASDALIQKLDGKVDPSLNASAAIQGSAFSNGNGILGVNQSAGANNQMINAVRISTGPQSVDDNVLSQQNMTLLPDSRSPSTTGSRQVVTSDQAFTGSRGVVQVNQSAGVGNRMANTLGVTIK","creator":"System-cpintado","dataset":["Condensates-related proteins"],"date":"2025-06-21T12:57:02.303Z","disprot_id":"DP04435","features":{"pfam":[{"id":"PF27129","name":"Functional amyloid protein FapB/FapC family","start":18,"end":181}]},"genes":[{"name":{"value":"fapB","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/20572935","id":"20572935","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/20572935","_id":"6856ac1e7cd61eccdacd5c93"},"code":"ECO:0000303","_id":"6856ac1e7cd61eccdacd5c92"}],"_id":"6856ac1e7cd61eccdacd5c91"},"synonyms":[],"olnNames":[],"orfNames":[{"value":"HZ99_04085","evidences":[],"_id":"6856ac1e7cd61eccdacd5c94"},{"value":"PSUK4_00020","evidences":[],"_id":"6856ac1e7cd61eccdacd5c95"}],"_id":"6856ac1e7cd61eccdacd5c90"}],"length":182,"name":"Functional amyloid subunit FapB","ncbi_taxon_id":294,"organism":"Pseudomonas fluorescens","regions_counter":5,"released":"2025_06","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Pseudomonadales","Pseudomonadaceae","Pseudomonas"],"regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","date":"2022-11-17T12:36:30.971Z","disprot_namespace":"Structural state","ec_id":"ECO:0001238","ec_name":"nuclear magnetic resonance evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":182,"interaction_partner":[],"reference_html":"FapA is an intrinsically disordered chaperone for Pseudomonas functional amyloid FapC. <i> Rasmussen HØ, Kumar A, Shin B, Stylianou F, Sewell L, Xu Y, Otzen DE, Skov Pedersen J, Matthews SJ. </i> J Mol Biol, 2022","reference_id":"36368411","region_id":"DP04435r001","released":"2023_12","sample":[],"statement":[{"type":"Abstract","text":"Here we present a comprehensive biophysical and spectroscopy analysis of FapA, FapB and FapC and provide insight into their molecular interactions. We show that all three proteins are primarily disordered with some regions with structural propensities for α-helix and β-sheet.","_id":"6856af0a7cd61eccdacd5ee5"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2022-12-26T15:19:58.006Z","_id":"6856af0a7cd61eccdacd5ee6"},"version":0,"_id":"6856af0a7cd61eccdacd5ee4","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2022-12-26T15:38:01.402Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0007044","ec_name":"transmission electron microscopy evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":182,"interaction_partner":[],"reference_html":"FapA is an Intrinsically Disordered Chaperone for Pseudomonas Functional Amyloid FapC. <i> Rasmussen HØ, Kumar A, Shin B, Stylianou F, Sewell L, Xu Y, Otzen DE, Pedersen JS, Matthews SJ. </i> J Mol Biol, 2022","reference_id":"36368411","region_id":"DP04435r002","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"Negative-stained TEM was used to visualize the fibrils formed in the ThT assays, both FapB and FapC fibrils alone (Figure 5(A) and (B)) as well as FapB and FapC fibrillated with FapA (Figure 5(C) and (D)).","_id":"6856af0a7cd61eccdacd5ee8"}],"states_connection":[],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_id":"GO:1990000","term_is_obsolete":false,"term_name":"amyloid fibril formation","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-02-01T10:38:00.902Z","_id":"6856af0a7cd61eccdacd5ee9"},"version":0,"_id":"6856af0a7cd61eccdacd5ee7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","date":"2023-02-02T12:25:55.430Z","disprot_namespace":"Disorder function","ec_go":"IDA","ec_id":"ECO:0006333","ec_name":"thioflavin T based fluorescence spectroscopy evidence","ec_ontology":"ECO","start":1,"end":182,"interaction_partner":[],"reference_html":"FapA is an Intrinsically Disordered Chaperone for Pseudomonas Functional Amyloid FapC. <i> Rasmussen HØ, Kumar A, Shin B, Stylianou F, Sewell L, Xu Y, Otzen DE, Pedersen JS, Matthews SJ. </i> J Mol Biol, 2022","reference_id":"36368411","region_id":"DP04435r003","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"Fibrils are clearly seen for all samples, as expected from the observed increase in ThT fluorescence (Figure 3(A), Figure 4(A)).","_id":"6856af0a7cd61eccdacd5eeb"}],"states_connection":[],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_id":"GO:1990000","term_is_obsolete":false,"term_name":"amyloid fibril formation","term_namespace":"Biological process","term_not_annotate":false,"term_ontology":"GO","unpublished":true,"validated":{"curator_id":"fquaglia","curator_name":"Federica Quaglia","timestamp":"2023-02-02T15:48:52.298Z","_id":"6856af0a7cd61eccdacd5eec"},"version":0,"_id":"6856af0a7cd61eccdacd5eea","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","date":"2023-01-09T08:44:04.767Z","disprot_namespace":"Structural state","ec_id":"ECO:0006200","ec_name":"circular dichroism evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":182,"interaction_partner":[],"reference_html":"FapA is an Intrinsically Disordered Chaperone for Pseudomonas Functional Amyloid FapC. <i> Rasmussen HØ, Kumar A, Shin B, Stylianou F, Sewell L, Xu Y, Otzen DE, Pedersen JS, Matthews SJ. </i> J Mol Biol, 2023","reference_id":"36368411","region_id":"DP04435r004","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"CD data show FapA, FapB, and FapC have deep minima around 200 nm (Figure 1(A)), which is typical for a random coil structure.","_id":"6856af0a7cd61eccdacd5eee"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-01-09T12:47:25.351Z","_id":"6856af0a7cd61eccdacd5eef"},"version":0,"_id":"6856af0a7cd61eccdacd5eed","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[],"curator_id":"cpintado","curator_name":"Carlos Pintado Grima","curator_orcid":"0000-0002-8544-959X","date":"2023-01-09T08:46:27.113Z","disprot_namespace":"Structural state","ec_id":"ECO:0006210","ec_name":"small-angle X-ray scattering evidence used in manual assertion","ec_ontology":"ECO","start":1,"end":182,"interaction_partner":[],"reference_html":"FapA is an Intrinsically Disordered Chaperone for Pseudomonas Functional Amyloid FapC. <i> Rasmussen HØ, Kumar A, Shin B, Stylianou F, Sewell L, Xu Y, Otzen DE, Pedersen JS, Matthews SJ. </i> J Mol Biol, 2023","reference_id":"36368411","region_id":"DP04435r005","released":"2023_12","sample":[],"statement":[{"type":"Results","text":"The fitting with the simple Gaussian random coil model is in accordance with the trend of primarily random coil seen in CD.","_id":"6856af0a7cd61eccdacd5ef1"}],"states_connection":[],"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","unpublished":true,"validated":{"curator_id":"vnugnes","curator_name":"Victoria Nugnes","timestamp":"2023-01-09T12:48:13.049Z","_id":"6856af0a7cd61eccdacd5ef2"},"version":0,"_id":"6856af0a7cd61eccdacd5ef0","reference_source":"pmid"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":182,"type":"D"}],"Structural state":[{"start":1,"end":182,"type":"D"}],"Biological process":[{"start":1,"end":182,"type":"F"}]}},{"disprot_id":"DP04436","acc":"T2HRH7","creator":"zskalman","date":"2025-06-21T12:58:01.972Z","features":{"pfam":[{"id":"PF02037","name":"SAP domain","start":460,"end":493},{"id":"PF02755","name":"RPEL repeat","start":92,"end":113},{"id":"PF02755","name":"RPEL repeat","start":136,"end":158},{"id":"PF02755","name":"RPEL repeat","start":180,"end":200}],"gene3D":[]},"genes":[{"name":{"value":"MELODY","evidences":[{"code":"ECO:0000313","source":{"name":"EMBL","id":"BAN82605.1","url":"https://www.ebi.ac.uk/ena/browser/view/BAN82605.1"}}]}}],"length":1038,"name":"MKL1-elongated derivative of yield protein","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions":[{"start":85,"end":116,"reference_id":"24909411","reference_source":"pmid","reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","date":"2026-06-17T14:23:09.083Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04436r002","statement":[{"text":"The CD spectra of RPELs exhibited a strong negative band near 200 nm and a weak negative shoulder at 220 nm, which is characteristic of unfolded polypeptides21 (Figure 2).","type":"Results"},{"text":"The negative band near 200 nm is stronger in the order of RPEL3 > RPEL2 > RPEL1 (Figure 2).","type":"Results"},{"text":"Authors call RPEL1 the 85–116 region, REPEL2, the 129–160 region and RPEL3 the 173–204 region of MKL1.","type":"Curator statement"}]},{"start":129,"end":160,"reference_id":"24909411","reference_source":"pmid","reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","date":"2026-06-17T14:23:19.419Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04436r003","statement":[{"text":"The CD spectra of RPELs exhibited a strong negative band near 200 nm and a weak negative shoulder at 220 nm, which is characteristic of unfolded polypeptides21 (Figure 2).","type":"Results"},{"text":"The negative band near 200 nm is stronger in the order of RPEL3 > RPEL2 > RPEL1 (Figure 2).","type":"Results"},{"text":"Authors call RPEL1 the 85–116 region, REPEL2, the 129–160 region and RPEL3 the 173–204 region of MKL1.","type":"Curator statement"}]},{"start":173,"end":204,"reference_id":"24909411","reference_source":"pmid","reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","date":"2026-06-17T14:23:27.773Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04436r004","statement":[{"text":"The CD spectra of RPELs exhibited a strong negative band near 200 nm and a weak negative shoulder at 220 nm, which is characteristic of unfolded polypeptides21 (Figure 2).","type":"Results"},{"text":"The negative band near 200 nm is stronger in the order of RPEL3 > RPEL2 > RPEL1 (Figure 2).","type":"Results"},{"text":"Authors call RPEL1 the 85–116 region, REPEL2, the 129–160 region and RPEL3 the 173–204 region of MKL1.","type":"Curator statement"}]},{"start":173,"end":204,"reference_id":"24909411","reference_source":"pmid","reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","date":"2026-06-17T14:25:40.707Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04436r005","statement":[{"text":"The residues from Thr132 to Lys139 and from Leu149 to Met 152 of RPEL2 have a propensity to adopt an α-helical conformation (Figure 6a). On the other hand, RPEL3 exhibits no significant helical propensity (Figure 6b). Together, our results suggest that the helices α1 and α2 are transiently formed in RPEL1 and RPEL2, while the helix is not formed in RPEL3. ","type":"Results"},{"text":"Authors call RPEL1 the 85–116 region, REPEL2, the 129–160 region and RPEL3 the 173–204 region of MKL1.","type":"Curator statement"}]},{"start":129,"end":160,"reference_id":"24909411","reference_source":"pmid","reference_html":"Transient α-helices in the disordered RPEL motifs of the serum response factor coactivator MKL1. <i> Mizuguchi M, Fuju T, Obita T, Ishikawa M, Tsuda M, Tabuchi A. </i> Sci Rep, 2014","date":"2026-06-17T14:25:50.444Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04436r006","statement":[{"text":"The residues from Thr132 to Lys139 and from Leu149 to Met 152 of RPEL2 have a propensity to adopt an α-helical conformation (Figure 6a). On the other hand, RPEL3 exhibits no significant helical propensity (Figure 6b). Together, our results suggest that the helices α1 and α2 are transiently formed in RPEL1 and RPEL2, while the helix is not formed in RPEL3. ","type":"Results"},{"text":"Authors call RPEL1 the 85–116 region, REPEL2, the 129–160 region and RPEL3 the 173–204 region of MKL1.","type":"Curator statement"}]}],"regions_counter":6,"released":"2026_06","sequence":"MGGVTITKAKVDFSSVVCLPPSVIAVNGLDGGGAGENDEEPVLLSLSAAPSPQSEAVANELQELSLQPELTLGLHPGRNPNLPPLSERKNVLQLKLQQRRTREELVSQGIMPPLKSPAAFHEQRRSLERARTEDYLKRKIRSRPERSELVRMHILEETSAEPSLQAKQLKLKRARLADDLNEKIAQRPGPMELVEKNILPVESSLKEALIVGQVNYPKVADSSSFDEDSSDALSPEQPASHESQGSVPSPLESRASDLLPSATSISPTQVLSQLPMAPDPGETLFLAEQPPLPPPPLLPPSLTSGSIVPTAKPAPTLIKQSQPKSASEKSQRSKKAKELKPKVKKLKYHQYIPPDQKQDKGAPAMDSSYAKILQQQQLFLQLQILNQQQQQQQQQHYNYQAILPAPPKPSGETPGSSAPTPSRSLSTSSSSSSGTPGPGGLARQNSTALAGKPGALPANLDDMKVAELKQELKLRSLPVSGTKTELIERLRAYQDQVSPAPGAPKAPATTSVLSKAGEVVVAFPAALLSTGSALVTAGLAPAEMVVATVTSNGMVKFGSTGSTPPVSPTPSERSLLSTGDENSTPGDAFGEMVTSPLTQLTLQASPLQIVKEEGARAASCCLSPGARAELEGLDKDQMLQEKDKQIEELTRMLQQKQQLVELLRLQLEQQKRAQQPAPASSPVKRESSFSSCQLSCQPQGAARAFGPGLVVPTTNHGDAQAPAPESPPVVVKQEAGPPEPDLAPASQLLLGSQGTSFLKKVSPPTLVTDSTGTHLILTVTNKSADGPGLPTGSPQQPLSQPGSPAPGPPAQMDLEHPPQPSFATPTSLLKKEPPGYEETVTQQPKQQENGSSSQHMDDLFDILIQSGEISADFKEPPSLPGKEKSPPAEAYGPPLTPQPLPLSELPQAAPPPGSPTLPGRLEDFLESSTGLPLLTSGHEGPEPLSLIDDLHSQMLSSSAILDHPPSPMDTSELHFAPEPSSGMGLDLAVGHLDSMDWLELSSGGPVLSLAPLSTTAPSLFSMDFLDGHDLQLHWDSCL","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"alphafold_very_low_content":0.6936416184971098,"disorder_content":0.09248554913294797,"disprot_consensus":{"full":[{"start":85,"end":116,"type":"D"},{"start":129,"end":160,"type":"D"},{"start":173,"end":204,"type":"D"}],"Structural state":[{"start":85,"end":116,"type":"D"},{"start":129,"end":160,"type":"D"},{"start":173,"end":204,"type":"D"}]}},{"disprot_id":"DP04437","acc":"P21827","creator":"zskalman","date":"2025-06-21T13:36:16.604Z","features":{"pfam":[{"id":"PF25390","name":"RCC1-like domain","start":48,"end":462}],"gene3D":[]},"genes":[{"name":{"value":"SRM1"},"synonyms":[{"value":"MTR1"},{"value":"PRP20"}],"olnNames":[{"value":"YGL097W"}]}],"length":482,"name":"Guanine nucleotide exchange factor SRM1","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions":[{"start":6,"end":15,"reference_id":"24339986","reference_source":"pmid","reference_html":"Structural characterisation of the nuclear import receptor importin alpha in complex with the bipartite NLS of Prp20. <i> Roman N, Christie M, Swarbrick CM, Kobe B, Forwood JK. </i> PLoS One, 2013","date":"2026-06-17T14:34:34.390Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"4OIH"}],"region_id":"DP04437r001","statement":[{"text":"Residues 6–15 of Prp20 could not be discerned from the electron density, a common observation for bipartite NLSs with long linker regions [6] and these residues were omitted from the final model.","type":"Results"}],"sequence_construct":"GSMVKRTVATNGDASGAHRAKKMSKTH","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P52293"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-17T14:34:38.307Z"}},{"start":6,"end":15,"reference_id":"24339986","reference_source":"pmid","reference_html":"Structural characterisation of the nuclear import receptor importin alpha in complex with the bipartite NLS of Prp20. <i> Roman N, Christie M, Swarbrick CM, Kobe B, Forwood JK. </i> PLoS One, 2013","date":"2026-06-17T14:34:46.853Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"4OIH"}],"region_id":"DP04437r002","statement":[{"text":"Residues 6–15 of Prp20 could not be discerned from the electron density, a common observation for bipartite NLSs with long linker regions [6] and these residues were omitted from the final model.","type":"Results"}],"sequence_construct":"GSMVKRTVATNGDASGAHRAKKMSKTH","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P52293"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-17T14:40:19.870Z"}},{"start":122,"end":142,"reference_id":"21093592","reference_source":"pmid","reference_html":"The 1.9Å crystal structure of Prp20p from Saccharomyces cerevisiae and its binding properties to Gsp1p and histones. <i> Wu F, Liu Y, Zhu Z, Huang H, Ding B, Wu J, Shi Y. </i> J Struct Biol, 2011","date":"2026-06-17T14:39:55.612Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"region_id":"DP04437r003","statement":[{"text":"The central shaft is filled with a number of water molecules. The region of residues 122–142 is invisible in the density map, possibly because it is disordered.","type":"Results"},{"text":"Firstly, the region of residues 122–142 of Prp20p is invisible in the density map while the exactly same region is missing from the sequence of RCC1 (Fig. 2). This region is full of charged residues, especially acidic residues (E125, D129, D131, D134, D137, D138, E139, D140, and D142). Such a flexible loop with many negative charges might be a recognition site for the basic patch of some unknown protein.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"3OF7"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"}],"regions_counter":3,"released":"2026_06","sequence":"MVKRTVATNGDASGAHRAKKMSKTHASHIINAQEDYKHMYLSVQPLDIFCWGTGSMCELGLGPLAKNKEVKRPRLNPFLPRDEAKIISFAVGGMHTLALDEESNVWSWGCNDVGALGRDTSNAKEQLKDMDADDSSDDEDGDLNELESTPAKIPRESFPPLAEGHKVVQLAATDNMSCALFSNGEVYAWGTFRCNEGILGFYQDKIKIQKTPWKVPTFSKYNIVQLAPGKDHILFLDEEGMVFAWGNGQQNQLGRKVMERFRLKTLDPRPFGLRHVKYIASGENHCFALTKDNKLVSWGLNQFGQCGVSEDVEDGALVTKPKRLALPDNVVIRSIAAGEHHSLILSQDGDLYSCGRLDMFEVGIPKDNLPEYTYKDVHGKARAVPLPTKLNNVPKFKSVAAGSHHSVAVAQNGIAYSWGFGETYAVGLGPFEDDTEVPTRIKNTATQDHNIILVGCGGQFSVSGGVKLSDEDAEKRADEMDD","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"alphafold_very_low_content":0.056016597510373446,"disorder_content":0.06431535269709543,"disprot_consensus":{"full":[{"start":6,"end":15,"type":"D"},{"start":122,"end":142,"type":"D"}],"Structural state":[{"start":6,"end":15,"type":"D"},{"start":122,"end":142,"type":"D"}],"Disorder function":[{"start":6,"end":15,"type":"F"}]}},{"disprot_id":"DP04438","acc":"Q86YT6","creator":"zskalman","date":"2025-06-21T13:46:33.317Z","features":{"pfam":[{"id":"PF00023","name":"Ankyrin repeat","start":464,"end":495},{"id":"PF00569","name":"Zinc finger, ZZ type","start":79,"end":122},{"id":"PF06701","name":"Mib_herc2","start":15,"end":71},{"id":"PF06701","name":"Mib_herc2","start":154,"end":219},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":511,"end":593},{"id":"PF12796","name":"Ankyrin repeats (3 copies)","start":657,"end":714},{"id":"PF13920","name":"Zinc finger, C3HC4 type (RING finger)","start":817,"end":859},{"id":"PF13920","name":"Zinc finger, C3HC4 type (RING finger)","start":864,"end":906},{"id":"PF13920","name":"Zinc finger, C3HC4 type (RING finger)","start":960,"end":1001},{"id":"PF18346","name":"Mind bomb SH3 repeat domain","start":247,"end":311},{"id":"PF18346","name":"Mind bomb SH3 repeat domain","start":333,"end":397}],"gene3D":[]},"genes":[{"name":{"value":"MIB1"},"synonyms":[{"value":"DIP1"},{"value":"KIAA1323"},{"value":"ZZANK2"}]}],"length":1006,"name":"E3 ubiquitin-protein ligase MIB1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":236,"end":251,"reference_id":"25747658","reference_source":"pmid","reference_html":"A tail of two sites: a bipartite mechanism for recognition of notch ligands by mind bomb E3 ligases. <i> McMillan BJ, Schnute B, Ohlenhard N, Zimmerman B, Miles L, Beglova N, Klein T, Blacklow SC. </i> Mol Cell, 2015","date":"2026-06-17T14:50:59.220Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"4XI6"}],"region_id":"DP04438r001","statement":[{"text":"A 15-residue linker that connects the MZM and REP domains is not visible in the structure and is likely disordered (Figure 1B, dashed circles).","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1117"}],"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Asn315Thr330del","start":null,"end":null,"position":null,"statements":[{"type":"Figure","text":"Residues 315-330 of the linker connecting Mib repeats 1 and 2 were deleted to assist crystallization (arrowhead)."}]}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-17T14:51:50.485Z"}},{"start":236,"end":251,"reference_id":"25747658","reference_source":"pmid","reference_html":"A tail of two sites: a bipartite mechanism for recognition of notch ligands by mind bomb E3 ligases. <i> McMillan BJ, Schnute B, Ohlenhard N, Zimmerman B, Miles L, Beglova N, Klein T, Blacklow SC. </i> Mol Cell, 2015","date":"2026-06-17T14:51:47.103Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"4XI6"}],"region_id":"DP04438r002","statement":[{"text":"A 15-residue linker that connects the MZM and REP domains is not visible in the structure and is likely disordered (Figure 1B, dashed circles).","type":"Results"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1117"}],"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Asn315Thr330del","start":null,"end":null,"position":null,"statements":[{"type":"Figure","text":"Residues 315-330 of the linker connecting Mib repeats 1 and 2 were deleted to assist crystallization (arrowhead)."}]}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-17T14:51:49.733Z"}},{"start":315,"end":331,"reference_id":"25747658","reference_source":"pmid","reference_html":"A tail of two sites: a bipartite mechanism for recognition of notch ligands by mind bomb E3 ligases. <i> McMillan BJ, Schnute B, Ohlenhard N, Zimmerman B, Miles L, Beglova N, Klein T, Blacklow SC. </i> Mol Cell, 2015","date":"2026-06-17T14:56:50.617Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asn240Ser","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"4TSE"}],"region_id":"DP04438r003","statement":[{"text":"The dotted line represents the disordered linker (residues 315-331) connecting the first and second repeats.","type":"Figure"}]},{"start":315,"end":331,"reference_id":"25747658","reference_source":"pmid","reference_html":"A tail of two sites: a bipartite mechanism for recognition of notch ligands by mind bomb E3 ligases. <i> McMillan BJ, Schnute B, Ohlenhard N, Zimmerman B, Miles L, Beglova N, Klein T, Blacklow SC. </i> Mol Cell, 2015","date":"2026-06-17T14:57:13.038Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asn240Ser","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"4TSE"}],"region_id":"DP04438r004","statement":[{"text":"The dotted line represents the disordered linker (residues 315-331) connecting the first and second repeats.","type":"Figure"}]},{"start":409,"end":427,"reference_id":"39121852","reference_source":"pmid","reference_html":"Structural requirements for activity of Mind bomb1 in Notch signaling. <i> Cao R, Gozlan O, Airich A, Tveriakhina L, Zhou H, Jiang H, Cole PA, Aster JC, Klein T, Sprinzak D, Blacklow SC. </i> Structure, 2024","date":"2026-06-17T15:08:36.035Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"8V0E"}],"region_id":"DP04438r005","statement":[{"text":"The linkers connecting MZM-REP to ANK and ANK to the RING1–2 region are flexible (schematically illustrated by lighter shading of domains and arrows to indicate movement) and not required for the signal activation function of NOTCH ligands","type":"Figure"},{"text":"The PDB-deposited data indicate that this region lacks electron density. As it appears to be part of the analyzed sample, the absence of electron density is likely due to its disordered nature, consistent with predicted data.","type":"Curator statement"}]},{"start":409,"end":427,"reference_id":"39121852","reference_source":"pmid","reference_html":"Structural requirements for activity of Mind bomb1 in Notch signaling. <i> Cao R, Gozlan O, Airich A, Tveriakhina L, Zhou H, Jiang H, Cole PA, Aster JC, Klein T, Sprinzak D, Blacklow SC. </i> Structure, 2024","date":"2026-06-17T15:11:08.319Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"8V0E"}],"region_id":"DP04438r006","statement":[{"text":"The linkers connecting MZM-REP to ANK and ANK to the RING1–2 region are flexible (schematically illustrated by lighter shading of domains and arrows to indicate movement) and not required for the signal activation function of NOTCH ligands","type":"Figure"},{"text":"The PDB-deposited data indicate that this region lacks electron density. As it appears to be part of the analyzed sample, the absence of electron density is likely due to its disordered nature, consistent with predicted data.","type":"Curator statement"}]},{"start":725,"end":747,"reference_id":"39121852","reference_source":"pmid","reference_html":"Structural requirements for activity of Mind bomb1 in Notch signaling. <i> Cao R, Gozlan O, Airich A, Tveriakhina L, Zhou H, Jiang H, Cole PA, Aster JC, Klein T, Sprinzak D, Blacklow SC. </i> Structure, 2024","date":"2026-06-17T15:11:24.256Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"8V0E"}],"region_id":"DP04438r007","statement":[{"text":"The linkers connecting MZM-REP to ANK and ANK to the RING1–2 region are flexible (schematically illustrated by lighter shading of domains and arrows to indicate movement) and not required for the signal activation function of NOTCH ligands","type":"Figure"},{"text":"The PDB-deposited data indicate that this region lacks electron density. As it appears to be part of the analyzed sample, the absence of electron density is likely due to its disordered nature, consistent with predicted data.","type":"Curator statement"}]},{"start":725,"end":747,"reference_id":"39121852","reference_source":"pmid","reference_html":"Structural requirements for activity of Mind bomb1 in Notch signaling. <i> Cao R, Gozlan O, Airich A, Tveriakhina L, Zhou H, Jiang H, Cole PA, Aster JC, Klein T, Sprinzak D, Blacklow SC. </i> Structure, 2024","date":"2026-06-17T15:11:33.692Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"8V0E"}],"region_id":"DP04438r008","statement":[{"text":"The linkers connecting MZM-REP to ANK and ANK to the RING1–2 region are flexible (schematically illustrated by lighter shading of domains and arrows to indicate movement) and not required for the signal activation function of NOTCH ligands","type":"Figure"},{"text":"The PDB-deposited data indicate that this region lacks electron density. As it appears to be part of the analyzed sample, the absence of electron density is likely due to its disordered nature, consistent with predicted data.","type":"Curator statement"}]}],"regions_counter":8,"released":"2026_06","sequence":"MSNSRNNRVMVEGVGARVVRGPDWKWGKQDGGEGHVGTVRSFESPEEVVVVWDNGTAANYRCSGAYDLRILDSAPTGIKHDGTMCDTCRQQPIIGIRWKCAECTNYDLCTVCYHGDKHHLRHRFYRITTPGSERVLLESRRKSKKITARGIFAGARVVRGVDWQWEDQDGGNGRRGKVTEIQDWSASSPHSAAYVLWDNGAKNLYRVGFEGMSDLKCVQDAKGGSFYRDHCPVLGEQNGNRNPGGLQIGDLVNIDLDLEIVQSLQHGHGGWTDGMFETLTTTGTVCGIDEDHDIVVQYPSGNRWTFNPAVLTKANIVRSGDAAQGAEGGTSQFQVGDLVQVCYDLERIKLLQRGHGEWAEAMLPTLGKVGRVQQIYSDSDLKVEVCGTSWTYNPAAVSKVASAGSAISNASGERLSQLLKKLFETQESGDLNEELVKAAANGDVAKVEDLLKRPDVDVNGQCAGHTAMQAASQNGHVDILKLLLKQNVDVEAEDKDGDRAVHHAAFGDEGAVIEVLHRGSADLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISKKRDDILAVLLEAGADVTITNNNGFNALHHAALRGNPSAMRVLLSKLPRPWIVDEKKDDGYTALHLAALNNHVEVAELLVHQGNANLDIQNVNQQTALHLAVERQHTQIVRLLVRAGAKLDIQDKDGDTPLHEALRHHTLSQLRQLQDMQDVGKVDAAWEPSKNTLIMGLGTQGAEKKSAASIACFLAANGADLSIRNKKGQSPLDLCPDPNLCKALAKCHKEKVSGQVGSRSPSMISNDSETLEECMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICKEQVQSRTKIEECVVCSDKKAAVLFQPCGHMCACENCANLMKKCVQCRAVVERRVPFIMCCGGKSSEDATDDISSGNIPVLQKDKDNTNVNADVQKLQQQLQDIKEQTMCPVCLDRLKNMIFLCGHGTCQLCGDRMSECPICRKAIERRILLY","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"alphafold_very_low_content":0.1143141153081511,"disorder_content":0.07455268389662027,"disprot_consensus":{"full":[{"start":236,"end":251,"type":"D"},{"start":315,"end":331,"type":"D"},{"start":409,"end":427,"type":"D"},{"start":725,"end":747,"type":"D"}],"Structural state":[{"start":236,"end":251,"type":"D"},{"start":315,"end":331,"type":"D"},{"start":409,"end":427,"type":"D"},{"start":725,"end":747,"type":"D"}],"Disorder function":[{"start":236,"end":251,"type":"F"},{"start":315,"end":331,"type":"F"},{"start":409,"end":427,"type":"F"},{"start":725,"end":747,"type":"F"}]}},{"disprot_id":"DP04442","acc":"Q8TD57","creator":"vnugnes","date":"2025-08-04T17:50:48.788Z","features":{"pfam":[{"id":"PF03028","name":"Dynein heavy chain region D6 P-loop domain","start":3517,"end":3632},{"id":"PF08393","name":"Dynein heavy chain, N-terminal region 2","start":859,"end":1262},{"id":"PF12774","name":"Hydrolytic ATP binding site of dynein motor region","start":1391,"end":1717},{"id":"PF12775","name":"P-loop containing dynein motor region","start":2037,"end":2214},{"id":"PF12777","name":"Microtubule-binding stalk of dynein motor","start":2678,"end":3020},{"id":"PF12780","name":"P-loop containing dynein motor region D4","start":2404,"end":2664},{"id":"PF12781","name":"ATP-binding dynein motor region","start":3052,"end":3273},{"id":"PF17852","name":"Dynein heavy chain AAA lid domain","start":1884,"end":2027},{"id":"PF17857","name":"AAA+ lid domain","start":2247,"end":2341},{"id":"PF18198","name":"Dynein heavy chain AAA lid domain","start":3667,"end":3805},{"id":"PF18199","name":"Dynein heavy chain C-terminal domain","start":3812,"end":4112}],"gene3D":[]},"genes":[{"name":{"value":"DNAH3"},"synonyms":[{"value":"DNAHC3B"}]}],"length":4116,"name":"Dynein axonemal heavy chain 3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions":[{"start":1,"end":53,"reference_id":"37258679","reference_source":"pmid","reference_html":"Axonemal structures reveal mechanoregulatory and disease mechanisms. <i> Walton T, Gui M, Velkova S, Fassad MR, Hirst RA, Haarman E, O'Callaghan C, Bottier M, Burgoyne T, Mitchison HM, Brown A. </i> Nature, 2023","date":"2025-08-04T18:05:07.525Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"EMDB","id":"35888"},{"db":"PDB","id":"8J07"}],"region_id":"DP04442r001","statement":[{"text":"The PDB-deposited data of the axonemal complex structure and Supplementary Information of the publication, indicate that this region lacks electron density. As it appears to be part of the analysed sample, the absence of electron density is likely due to its disordered nature, consistent with predicted data.","type":"Curator statement"}]},{"start":1,"end":53,"reference_id":"37258679","reference_source":"pmid","reference_html":"Axonemal structures reveal mechanoregulatory and disease mechanisms. <i> Walton T, Gui M, Velkova S, Fassad MR, Hirst RA, Haarman E, O'Callaghan C, Bottier M, Burgoyne T, Mitchison HM, Brown A. </i> Nature, 2023","date":"2025-08-04T18:05:30.189Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"EMDB","id":"35888"},{"db":"PDB","id":"8J07"}],"region_id":"DP04442r002","statement":[{"text":"The PDB-deposited data of the axonemal complex structure and Supplementary Information of the publication, indicate that this region lacks electron density. As it appears to be part of the analysed sample, the absence of electron density is likely due to its disordered nature, consistent with predicted data.","type":"Curator statement"}]},{"start":130,"end":200,"reference_id":"37258679","reference_source":"pmid","reference_html":"Axonemal structures reveal mechanoregulatory and disease mechanisms. <i> Walton T, Gui M, Velkova S, Fassad MR, Hirst RA, Haarman E, O'Callaghan C, Bottier M, Burgoyne T, Mitchison HM, Brown A. </i> Nature, 2023","date":"2025-08-04T18:05:41.346Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"EMDB","id":"35888"},{"db":"PDB","id":"8J07"}],"region_id":"DP04442r003","statement":[{"text":"The PDB-deposited data of the axonemal complex structure and Supplementary Information of the publication, indicate that this region lacks electron density. As it appears to be part of the analysed sample, the absence of electron density is likely due to its disordered nature, consistent with predicted data.","type":"Curator statement"}]}],"regions_counter":3,"released":"2026_06","sequence":"MGATGRLELTLAAPPHPGPAFQRSKARETQGEEEGSEMQIAKSDSIHHMSHSQGQPELPPLPASANEEPSGLYQTVMSHSFYPPLMQRTSWTLAAPFKEQHHHRGPSDSIANNYSLMAQDLKLKDLLKVYQPATISVPRDRTGQGLPSSGNRSSSEPMRKKTKFSSRNKEDSTRIKLAFKTSIFSPMKKEVKTSLTFPGSRPMSPEQQLDVMLQQEMEMESKEKKPSESDLERYYYYLTNGIRKDMIAPEEGEVMVRISKLISNTLLTSPFLEPLMVVLVQEKENDYYCSLMKSIVDYILMDPMERKRLFIESIPRLFPQRVIRAPVPWHSVYRSAKKWNEEHLHTVNPMMLRLKELWFAEFRDLRFVRTAEILAGKLPLQPQEFWDVIQKHCLEAHQTLLNKWIPTCAQLFTSRKEHWIHFAPKSNYDSSRNIEEYFASVASFMSLQLRELVIKSLEDLVSLFMIHKDGNDFKEPYQEMKFFIPQLIMIKLEVSEPIIVFNPSFDGCWELIRDSFLEIIKNSNGIPKLKYIPLKFSFTAAAADRQCVKAAEPGEPSMHAAATAMAELKGYNLLLGTVNAEEKLVSDFLIQTFKVFQKNQVGPCKYLNVYKKYVDLLDNTAEQNIAAFLKENHDIDDFVTKINAIKKRRNEIASMNITVPLAMFCLDATALNHDLCERAQNLKDHLIQFQVDVNRDTNTSICNQYSHIADKVSEVPANTKELVSLIEFLKKSSAVTVFKLRRQLRDASERLEFLMDYADLPYQIEDIFDNSRNLLLHKRDQAEMDLIKRCSEFELRLEGYHRELESFRKREVMTTEEMKHNVEKLNELSKNLNRAFAEFELINKEEELLEKEKSTYPLLQAMLKNKVPYEQLWSTAYEFSIKSEEWMNGPLFLLNAEQIAEEIGNMWRTTYKLIKTLSDVPAPRRLAENVKIKIDKFKQYIPILSISCNPGMKDRHWQQISEIVGYEIKPTETTCLSNMLEFGFGKFVEKLEPIGAAASKEYSLEKNLDRMKLDWVNVTFSFVKYRDTDTNILCAIDDIQMLLDDHVIKTQTMCGSPFIKPIEAECRKWEEKLIRIQDNLDAWLKCQATWLYLEPIFSSEDIIAQMPEEGRKFGIVDSYWKSLMSQAVKDNRILVAADQPRMAEKLQEANFLLEDIQKGLNDYLEKKRLFFPRFFFLSNDELLEILSETKDPLRVQPHLKKCFEGIAKLEFTDNLEIVGMISSEKETVPFIQKIYPANAKGMVEKWLQQVEQMMLASMREVIGLGIEAYVKVPRNHWVLQWPGQVVICVSSIFWTQEVSQALAENTLLDFLKKSNDQIAQIVQLVRGKLSSGARLTLGALTVIDVHARDVVAKLSEDRVSDLNDFQWISQLRYYWVAKDVQVQIITTEALYGYEYLGNSPRLVITPLTDRCYRTLMGALKLNLGGAPEGPAGTGKTETTKDLAKALAKQCVVFNCSDGLDYKAMGKFFKGLAQAGAWACFDEFNRIEVEVLSVVAQQILSIQQAIIRKLKTFIFEGTELSLNPTCAVFITMNPGYAGRAELPDNLKALFRTVAMMVPDYALIGEISLYSMGFLDSRSLAQKIVATYRLCSEQLSSQHHYDYGMRAVKSVLTAAGNLKLKYPEENESVLLLRALLDVNLAKFLAQDVPLFQGIISDLFPGVVLPKPDYEVFLKVLNDNIKKMKLQPVPWFIGKIIQIYEMMLVRHGYMIVGDPMGGKTSAYKVLAAALGDLHAANQMEEFAVEYKIINPKAITMGQLYGCFDQVSHEWMDGVLANAFREQASSLSDDRKWIIFDGPVDAIWIENMNTVLDDNKKLCLMSGEIIQMNSKMSLIFEPADLEQASPATVSRCGMIYMEPHQLGWKPLKDSYMDTLPSSLTKEHKELVNDMFMWLVQPCLEFGRLHCKFVVQTSPIHLAFSMMRLYSSLLDEIRAVEEEEMELGEGLSSQQIFLWLQGLFLFSLVWTVAGTINADSRKKFDVFFRNLIMGMDDNHPRPKSVKLTKNNIFPERGSIYDFYFIKQASGHWETWTQYITKEEEKVPAGAKVSELIIPTMETARQSFFLKTYLDHEIPMLFVGPTGTGKSAITNNFLLHLPKNTYLPNCINFSARTSANQTQDIIMSKLDRRRKGLFGPPIGKKAVVFVDDLNMPAKEVYGAQPPIELLRQWIDHGYWFDKKDTTRLDIVDMLLVTAMGPPGGGRNDITGRFTRHLNIISINAFEDDILTKIFSSIVDWHFGKGFDVMFLRYGKMLVQATKTIYRDAVENFLPTPSKSHYVFNLRDFSRVIQGVLLCPHTHLQDVEKCIRLWIHEVYRVFYDRLIDKEDRQVFFNMVKETTSNCFKQTIEKVLIHLSPTGKIVDDNIRSLFFGDYFKPESDQKIYDEITDLKQLTVVMEHYLEEFNNISKAPMSLVMFRFAIEHISRICRVLKQDKGHLLLVGIGGSGRQSAAKLSTFMNAYELYQIEITKNYAGNDWREDLKKIILQVGVATKSTVFLFADNQIKDESFVEDINMLLNTGDVPNIFPADEKADIVEKMQTAARTQGEKVEVTPLSMYNFFIERVINKISFSLAMSPIGDAFRNRLRMFPSLINCCTIDWFQSWPTDALELVANKFLEDVELDDNIRVEVVSMCKYFQESVKKLSLDYYNKLRRHNYVTPTSYLELILTFKTLLNSKRQEVAMMRNRYLTGLQKLDFAASQVAVMQRELTALQPQLILTSEETAKMMVKIEAETREADGKKLLVQADEKEANVAAAIAQGIKNECEGDLAEAMPALEAALAALDTLNPADISLVKSMQNPPGPVKLVMESICIMKGMKPERKPDPSGSGKMIEDYWGVSKKILGDLKFLESLKTYDKDNIPPLTMKRIRERFINHPEFQPAVIKNVSSACEGLCKWVRAMEVYDRVAKVVAPKRERLREAEGKLAAQMQKLNQKRAELKLVVDRLQALNDDFEEMNTKKKDLEENIEICSQKLVRAEKLISGLGGEKDRWTEAARQLGIRYTNLTGDVLLSSGTVAYLGAFTVDYRVQCQNQWLAECKDKVIPGFSDFSLSHTLGDPIKIRAWQIAGLPVDSFSIDNGIIVSNSRRWALMIDPHGQANKWIKNMEKANKLAVIKFSDSNYMRMLENALQLGTPVLIENIGEELDASIEPILLKATFKQQGVEYMRLGENIIEYSRDFKLYITTRLRNPHYLPEVAVKVCLLNFMITPLGLQDQLLGIVAAKEKPELEEKKNQLIVESAKNKKHLKEIEDKILEVLSMSKGNILEDETAIKVLSSSKVLSEEISEKQKVASMTETQIDETRMGYKPVAVHSATIFFCISDLANIEPMYQYSLTWFINLYMHSLTHSTKSEELNLRIKYIIDHFTLSIYNNVCRSLFEKDKLLFSLLLTIGIMKQKKEITEEVWYFLLTGGIALDNPYPNPAPQWLSEKAWAEIVRASALPKLHGLMEHLEQNLGEWKLIYDSAWPHEEQLPGSWKFSQGLEKMVILRCLRPDKMVPAVREFIAEHMGKLYIEAPTFDLQGSYNDSSCCAPLIFVLSPSADPMAGLLKFADDLGMGGTRTQTISLGQGQGPIAAKMINNAIKDGTWVVLQNCHLAASWMPTLEKICEEVIVPESTNARFRLWLTSYPSEKFPVSILQNGIKMTNEPPKGLRANLLRSYLNDPISDPVFFQSCAKAVMWQKMLFGLCFFHAVVQERRNFGPLGWNIPYEFNESDLRISMWQIQMFLNDYKEVPFDALTYLTGECNYGGRVTDDKDRRLLLSLLSMFYCKEIEEDYYSLAPGDTYYIPPHGSYQSYIDYLRNLPITAHPEVFGLHENADITKDNQETNQLFEGVLLTLPRQSGGSGKSPQEVVEELAQDILSKLPRDFDLEEVMKLYPVVYEESMNTVLRQELIRFNRLTKVVRRSLINLGRAIKGQVLMSSELEEVFNSMLVGKVPAMWAAKSYPSLKPLGGYVADLLARLTFFQEWIDKGPPVVFWISGFYFTQSFLTGVSQNYARKYTIPIDHIGFEFEVTPQETVMENNPEDGAYIKGLFLEGARWDRKTMQIGESLPKILYDPLPIIWLKPGESAMFLHQDIYVCPVYKTSARRGTLSTTGHSTNYVLSIELPTDMPQKHWINRGVASLCQLDN","taxonomy":["E","u","k","a","r","y","o","t","a",",","","M","e","t","a","z","o","a",",","","C","h","o","r","d","a","t","a",",","","C","r","a","n","i","a","t","a",",","","V","e","r","t","e","b","r","a","t","a",",","","E","u","t","e","l","e","o","s","t","o","m","i",",","","M","a","m","m","a","l","i","a",",","","E","u","t","h","e","r","i","a",",","","E","u","a","r","c","h","o","n","t","o","g","l","i","r","e","s",",","","P","r","i","m","a","t","e","s",",","","H","a","p","l","o","r","r","h","i","n","i",",","","C","a","t","a","r","r","h","i","n","i",",","","H","o","m","i","n","i","d","a","e",",","","H","o","m","o"],"disorder_content":0.03012633624878523,"disprot_consensus":{"full":[{"start":1,"end":53,"type":"D"},{"start":130,"end":200,"type":"D"}],"Structural state":[{"start":1,"end":53,"type":"D"},{"start":130,"end":200,"type":"D"}],"Disorder function":[{"start":1,"end":53,"type":"F"}]}},{"acc":"P11142","sequence":"MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIINWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD","creator":"xcastro","dataset":["Autophagy-related proteins","Condensates-related proteins","Stress response proteins"],"date":"2025-10-16T12:24:40.087Z","disprot_id":"DP04445","features":{"pfam":[{"id":"PF00012","name":"Hsp70 protein","start":6,"end":612}]},"genes":[{"name":{"value":"HSPA8","evidences":[{"source":{"id":"HGNC:5241","name":"HGNC","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:5241","_id":"68f0e408953df1273414d5e6"},"code":"ECO:0000312","_id":"68f0e408953df1273414d5e5"}],"_id":"68f0e408953df1273414d5e4"},"synonyms":[{"value":"HSC70","_id":"68f0e408953df1273414d5e7","evidences":[]},{"value":"HSP73","_id":"68f0e408953df1273414d5e8","evidences":[]},{"value":"HSPA10","_id":"68f0e408953df1273414d5e9","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"68f0e408953df1273414d5e3"}],"length":646,"name":"Heat shock cognate 71 kDa protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":7,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":607,"end":646,"reference_id":"23865999","reference_source":"pmid","reference_html":"The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex. <i> Smith MC, Scaglione KM, Assimon VA, Patury S, Thompson AD, Dickey CA, Southworth DR, Paulson HL, Gestwicki JE, Zuiderweg ER. </i> Biochemistry, 2013","date":"2025-10-16T16:02:47.638Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Backbone assignments for the spectra of Hsc70 (391–646) were obtained from a 250 μM triple-labeled sample containing an N-terminal purification tag, which was not cleaved (MHHHHHHSSGVDLGTENLYFQNAM)."},{"type":"Methods","text":"Expression and purification of all Hsc70 proteins were carried out as previously described, (30) except the N-terminal His6 purification tag was not removed during the process."}]}],"region_id":"DP04445r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":1,"db":"ChEBI","id":"16761","statements":[{"type":"Methods","text":"The experiments for studying the interaction of Hsc70 with CHIP were carried out with full-length Hsc70 (71 kDa) containing the same N-terminal expression tag. The Hsc70 sample was 15N labeled, in 50 mM K2PO4, 110 μM NRLLLTG peptide, 1 mM ADP, 5 mM MgCl2, 10 mM KCl, 0.02% NaN3, pH 7.2, 25 0 °C."},{"type":"Methods","text":"The experiments for studying the 15N NMR relaxation of Hsc70 with or without CHIP were carried out with full-length Hsc70 (71 kDa) containing the same N-terminal expression tag. The Hsc70 sample was 15N labeled, at 67 μM in 50 mM K2PO4, 200 μM NRLLLTG, 1 mM ADP, 5 mM MgCl2, 10 mM KCl, 0.02% NaN3, pH 7.2, 25 °C."}],"entry_name":null}],"statement":[{"text":"To explore the Hsc70–CHIP complex in more detail, we turned to solution-state NMR. 1H–15N TROSY HSQC spectra were collected for 15N-labeled wtHsc70 (1–646) in the ADP and peptide (NRLLLTG) substrate-bound state.","type":"Results"},{"text":"The center of the TROSY spectrum was dominated by intense resonances with little chemical shift dispersion (Figure 3b). As identified in our previous study on the highly homologous prokaryotic Hsp70 molecule, DnaK, (31) these resonances likely correspond to amino acid stretches that form flexible random coils, such as the linker region between the NBD and SBD and the C-terminal tail (Figure 3a).","type":"Results"},{"text":"The results also suggest that the region between the GPTIEEVD sequence and the end of the Hsc70 SBD remains a dynamic random coil, even in the presence of bound CHIP.","type":"Results"},{"text":"(b) A 10× high-contour view of detailed area showing Hsc70s dynamic random coil residues including the ∼40 amino acid C-terminal tail; resonance assignments are included.","type":"Figure"},{"text":"(c) Depiction of the unstructured C-terminal tail of wtHsc70.","type":"Figure"},{"text":"The program found reliable assignments for the C-terminal 30 residues and the expression tag only. Table 1 in the Supporting Information lists the assignments obtained. High intensity of the assigned peaks as well as their random-coil chemical shifts showed that these areas are dynamic random coil.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-20T16:57:19.791Z"}},{"start":639,"end":646,"reference_id":"23865999","reference_source":"pmid","reference_html":"The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex. <i> Smith MC, Scaglione KM, Assimon VA, Patury S, Thompson AD, Dickey CA, Southworth DR, Paulson HL, Gestwicki JE, Zuiderweg ER. </i> Biochemistry, 2013","date":"2025-10-17T08:11:03.566Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"GO:0031625","term_name":"ubiquitin protein ligase binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"Backbone assignments for the spectra of Hsc70 (391–646) were obtained from a 250 μM triple-labeled sample containing an N-terminal purification tag, which was not cleaved (MHHHHHHSSGVDLGTENLYFQNAM)."},{"type":"Methods","text":"Expression and purification of all Hsc70 proteins were carried out as previously described, (30) except the N-terminal His6 purification tag was not removed during the process."}]}],"cross_refs":[{"db":"ELM","id":"ELME000130"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q9UNE7","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04445r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":1,"db":"ChEBI","id":"16761","statements":[{"type":"Methods","text":"The experiments for studying the interaction of Hsc70 with CHIP were carried out with full-length Hsc70 (71 kDa) containing the same N-terminal expression tag. The Hsc70 sample was 15N labeled, in 50 mM K2PO4, 110 μM NRLLLTG peptide, 1 mM ADP, 5 mM MgCl2, 10 mM KCl, 0.02% NaN3, pH 7.2, 25 0 °C."},{"type":"Methods","text":"The experiments for studying the 15N NMR relaxation of Hsc70 with or without CHIP were carried out with full-length Hsc70 (71 kDa) containing the same N-terminal expression tag. The Hsc70 sample was 15N labeled, at 67 μM in 50 mM K2PO4, 200 μM NRLLLTG, 1 mM ADP, 5 mM MgCl2, 10 mM KCl, 0.02% NaN3, pH 7.2, 25 °C."}],"entry_name":null}],"statement":[{"text":"We found that CHIP binds tightly to two molecules of Hsc70 forming a 210 kDa complex, with a Kd of approximately 60 nM, and that the IEEVD motif at the C-terminus of Hsc70 (residues 642–646) is both necessary and sufficient for binding. Moreover, the same motif is required for CHIP-mediated ubiquitination of Hsc70 in vitro, highlighting its functional importance.","type":"Abstract"},{"text":"Specifically, we found that binding to CHIP caused the resonances for residues 639-GPTIEEVD-646 to disappear from the wtHsc70 NMR spectrum, while the assigned resonances for the “upstream” residues 616–636 of the unstructured tail remained visible and relatively unaffected by the presence of CHIP (Figure 4b,c). These results suggest that the 70 kDa CHIP dimer sequesters the EEVD motif and a few more residues into a large molecular weight complex, broadening the corresponding NMR resonances beyond detection. The results also suggest that the region between the GPTIEEVD sequence and the end of the Hsc70 SBD remains a dynamic random coil, even in the presence of bound CHIP. Taken together, these data and the FP studies support a model in which CHIP binding is largely localized to the EEVD motif.","type":"Results"},{"text":"In fact, resonances for residues 639–646 (GPTIEEVD) disappear from the NMR spectrum, which is the expected result for residues involved in a high-molecular-weight complex.","type":"Discussion"},{"text":"This result suggests that CHIP only directly interacts, at a maximum, with residues 639–646 of Hsc70, a result supported by the FP studies (see Figure 2).","type":"Discussion"}],"term_comment":"","term_def":"\"Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.\" [GOC:vp]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-20T17:01:50.496Z"}},{"start":613,"end":646,"reference_id":"34571256","reference_source":"pmid","reference_html":"Structural, thermodynamic and functional studies of human 71 kDa heat shock cognate protein (HSPA8/hHsc70). <i> Silva NSM, Rodrigues LFC, Dores-Silva PR, Montanari CA, Ramos CHI, Barbosa LRS, Borges JC. </i> Biochim Biophys Acta Proteins Proteom, 2021","date":"2025-10-23T15:43:15.379Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007013","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"SASBDB","id":"SASDL42"}],"region_id":"DP04445r006","statement":[{"text":"From the data, we observe that both proteins seem folded, as indicated by the preservation of a well-defined peak, but deviations from a well-folded profile indicate that the domains may be effectively folded with considerably flexible regions, probably due to the linker connecting them as well as the His-tag on the N-terminal and C-terminal unstructured regions.","type":"Results"},{"text":"Hybrid rigid-body modeling was also performed by means of EOM software [70,71] to check for the degrees of flexibility of the interdomain linker and C-terminal regions. As inputs, data from proteins in the PDB were used; specifically, PDB ID 2QW9 [72] and PDB ID 4PO2 [73] were used for the rHSPA8 NBD and SBD regions, respectively. The program then modeled the missing regions (13 residues in the interdomain linker and the last 33 residues in the C-terminus) as beads, generating 10,000 structures and then applying a genetic algorithm to filter representative configurations of the protein, fitting them to the experimental data. These results were verified by the CorMap p-value metric.","type":"Results"},{"text":"Although the accompanying text does not specify exact residue boundaries, manual inspection of the data for HSPA8/Hsc70 indicates that the C-terminal segment 613–646 is disordered.","type":"Curator statement"}]}],"__v":0,"disorder_content":0.06191950464396285,"disprot_consensus":{"full":[{"start":607,"end":646,"type":"D"}],"Structural state":[{"start":607,"end":646,"type":"D"}],"Molecular function":[{"start":639,"end":646,"type":"F"}]}},{"acc":"P19120","sequence":"MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIINWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD","creator":"xcastro","dataset":["Stress response proteins"],"date":"2025-10-20T07:04:03.111Z","disprot_id":"DP04446","features":{"pfam":[{"id":"PF00012","name":"Hsp70 protein","start":6,"end":612}]},"genes":[{"name":{"value":"HSPA8","evidences":[{"source":{"id":"P11142","name":"UniProtKB","url":"https://www.uniprot.org/uniprot/P11142","_id":"68f5dee3953df1273414d655"},"code":"ECO:0000250","_id":"68f5dee3953df1273414d654"}],"_id":"68f5dee3953df1273414d653"},"synonyms":[{"value":"HSC70","_id":"68f5dee3953df1273414d656","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"68f5dee3953df1273414d652"}],"length":650,"name":"Heat shock cognate 71 kDa protein","ncbi_taxon_id":9913,"organism":"Bos taurus","regions_counter":5,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"regions":[{"start":384,"end":394,"reference_id":"16307916","reference_source":"pmid","reference_html":"Structural basis of interdomain communication in the Hsc70 chaperone. <i> Jiang J, Prasad K, Lafer EM, Sousa R. </i> Mol Cell, 2005","date":"2025-10-22T14:54:28.330Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"1YUW"}],"region_id":"DP04446r001","statement":[{"text":"The structure (Figures 1A and 1B) reveals the SBD (aa 395–554, orange) connected by an exposed linker (aa 384–394, red) to the NBD (aa 1–383, cyan), with residues 415–417 and helix A of the SBD (aa 513–524; helix lettering as in Zhu et al. [1996]) resting in a groove between lobes IA and IIA of the NBD.","type":"Results"},{"text":"Crystal and NMR structures of isolated SBDs reveal the interdomain linker in two conformations: a linker “out” form in which the linker projects into solvent and assumes a conformation like that seen in the structure reported here, and a linker “in” form in which the linker is packed onto a hydrophobic patch on the SBD (Zhu et al., 1996, Wang et al., 1998).","type":"Results"},{"text":"Although the text does not state that the interdomain linker is disordered, manual inspection of the X-ray structure shows this region is flexible and lacks a defined conformation.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu213Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"E213A/D214A was constructed subsequently based on the observation of high B factors for these residues in a human Hsp70 NBD (Sriram et al., 1997)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp214Ala","start":null,"end":null,"position":null}],"sequence_construct":"MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIAAGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVE","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-23T15:40:00.575Z"}},{"start":384,"end":394,"reference_id":"16307916","reference_source":"pmid","reference_html":"Structural basis of interdomain communication in the Hsc70 chaperone. <i> Jiang J, Prasad K, Lafer EM, Sousa R. </i> Mol Cell, 2005","date":"2025-10-22T14:56:08.364Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"1YUW"}],"region_id":"DP04446r002","statement":[{"text":"The structure (Figures 1A and 1B) reveals the SBD (aa 395–554, orange) connected by an exposed linker (aa 384–394, red) to the NBD (aa 1–383, cyan), with residues 415–417 and helix A of the SBD (aa 513–524; helix lettering as in Zhu et al. [1996]) resting in a groove between lobes IA and IIA of the NBD.","type":"Results"},{"text":"Crystal and NMR structures of isolated SBDs reveal the interdomain linker in two conformations: a linker “out” form in which the linker projects into solvent and assumes a conformation like that seen in the structure reported here, and a linker “in” form in which the linker is packed onto a hydrophobic patch on the SBD (Zhu et al., 1996, Wang et al., 1998).","type":"Results"},{"text":"Although the text does not state that the interdomain linker is disordered, manual inspection of the X-ray structure shows this region is flexible and lacks a defined conformation.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu213Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"E213A/D214A was constructed subsequently based on the observation of high B factors for these residues in a human Hsp70 NBD (Sriram et al., 1997)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp214Ala","start":null,"end":null,"position":null}],"sequence_construct":"MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIAAGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVE","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-23T15:40:13.665Z"}},{"start":384,"end":394,"reference_id":"16307916","reference_source":"pmid","reference_html":"Structural basis of interdomain communication in the Hsc70 chaperone. <i> Jiang J, Prasad K, Lafer EM, Sousa R. </i> Mol Cell, 2005","date":"2025-10-23T13:25:03.177Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001191","ec_ontology":"ECO","ec_name":"in vitro cleavage assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04446r003","statement":[{"text":"Digestion of wt enzyme in the absence of ATP leads to cleavage in the linker and rapid generation of the 44 kDa NBD as the major fragment. The fraction of 44 kDa fragment released from the wt enzyme is reduced 5- to 6-fold by ATP (Figures 5A and 5F), indicating that the linker becomes less protease accessible upon ATP binding.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-23T15:40:27.840Z"}},{"start":384,"end":394,"reference_id":"16307916","reference_source":"pmid","reference_html":"Structural basis of interdomain communication in the Hsc70 chaperone. <i> Jiang J, Prasad K, Lafer EM, Sousa R. </i> Mol Cell, 2005","date":"2025-10-22T15:02:03.201Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"GO:0072318","term_name":"clathrin coat disassembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Val388Cys","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"We also constructed V388C, L3We also constructed V388C, L393C, and a quadruple arginine substitution for residues 391–394 in the interdomain linker. The multiply arginine-substituted enzyme was proteolyzed in vivo and could not be purified.93C, and a quadruple arginine substitution for residues 391–394 in the interdomain linker."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu393Cys","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"We also constructed V388C, L393C, and a quadruple arginine substitution for residues 391–394 in the interdomain linker. The multiply arginine-substituted enzyme was proteolyzed in vivo and could not be purified."}]}],"ec_go":"IMP","region_id":"DP04446r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q27974","statements":[{"type":"Methods","text":"Cages assembled from clathrin and GST-AP180 at a clathrin concentration of 0.2 μM were mixed with auxilin at 0.1 μM in buffer C. Disassembly was initiated by adding Hsc70ΔCterm (0.3–1 μM) preincubated with 1 mM ATP to the reactions in the light-scattering cuvette and continuously monitoring light scattering for 20 min."}]},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"A7Z073"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04973"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P04975"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P49951"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":1,"db":"ChEBI","id":"15422","entry_name":null}],"sequence_construct":"MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENCQDLLCLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVE","statement":[{"text":"We also constructed V388C, L393C, and a quadruple arginine substitution for residues 391–394 in the interdomain linker. The multiply arginine-substituted enzyme was proteolyzed in vivo and could not be purified.","type":"Results"},{"text":"Mutations that affect interdomain communication may therefore affect clathrin cage disassembly. To quantitatively compare mutant enzyme disassembly activity, the decrease in light scattering that occurs as cages are disassembled was monitored continuously following initiation of disassembly by addition of Hsc70ΔCterm (preincubated with 1 mM ATP) to reactions containing auxilin and cages.","type":"Results"},{"text":"Substitutions at V388 and L393 in the linker reduce disassembly rates 4- to 6-fold.","type":"Results"}],"term_comment":"","term_def":"\"The disaggregation of a clathrin coat into its constituent components; results in stripping or removing the clathrin coat from clathrin-coated vesicles (CCV) before fusing with their targets. CVVs transport cargo from plasma membrane and trans-Golgi to the endosomal system.\" [PMID:11084334, PMID:11146663, PMID:8524399]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-23T15:41:24.485Z"}},{"start":384,"end":394,"reference_id":"38317495","reference_source":"pmid","reference_html":"Combined In-Solution Fragment Screening and Crystallographic Binding-Mode Analysis with a Two-Domain Hsp70 Construct. <i> Zehe M, Kehrein J, Schollmayer C, Plank C, Kovacs H, Merino Asumendi E, Holzgrabe U, Grimm C, Sotriffer C. </i> ACS Chem Biol, 2024","date":"2025-10-21T15:49:37.910Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu213Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp214Ala","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"4FL9"}],"region_id":"DP04446r005","statement":[{"text":"This is largely enabled by the flexible region between β-sandwich and α-helix, which is often poorly resolved in other crystal structures.","type":"Results"}]}],"__v":0,"disorder_content":0.016923076923076923,"disprot_consensus":{"full":[{"start":384,"end":394,"type":"D"}],"Structural state":[{"start":384,"end":394,"type":"D"}],"Disorder function":[{"start":384,"end":394,"type":"F"}],"Biological process":[{"start":384,"end":394,"type":"F"}]}},{"acc":"P25685","sequence":"MGKDYYQTLGLARGASDEEIKRAYRRQALRYHPDKNKEPGAEEKFKEIAEAYDVLSDPRKREIFDRYGEEGLKGSGPSGGSGGGANGTSFSYTFHGDPHAMFAEFFGGRNPFDTFFGQRNGEEGMDIDDPFSGFPMGMGGFTNVNFGRSRSAQEPARKKQDPPVTHDLRVSLEEIYSGCTKKMKISHKRLNPDGKSIRNEDKILTIEVKKGWKEGTKITFPKEGDQTSNNIPADIVFVLKDKPHNIFKRDGSDVIYPARISLREALCGCTVNVPTLDGRTIPVVFKDVIRPGMRRKVPGEGLPLPKTPEKRGDLIIEFEVIFPERIPQTSRTVLEQVLPI","creator":"xcastro","dataset":["Condensates-related proteins","Autophagy-related proteins","Stress response proteins"],"date":"2025-10-20T09:58:11.049Z","disprot_id":"DP04447","features":{"pfam":[{"id":"PF00226","name":"DnaJ domain","start":4,"end":65},{"id":"PF01556","name":"DnaJ C terminal domain","start":165,"end":323}]},"genes":[{"name":{"value":"DNAJB1","_id":"68f607b3953df1273414d666","evidences":[]},"synonyms":[{"value":"DNAJ1","_id":"68f607b3953df1273414d667","evidences":[]},{"value":"HDJ1","_id":"68f607b3953df1273414d668","evidences":[]},{"value":"HSPF1","_id":"68f607b3953df1273414d669","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"68f607b3953df1273414d665"}],"length":340,"name":"DnaJ homolog subfamily B member 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":3,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":75,"end":92,"reference_id":"33177718","reference_source":"pmid","reference_html":"HSP40 proteins use class-specific regulation to drive HSP70 functional diversity. <i> Faust O, Abayev-Avraham M, Wentink AS, Maurer M, Nillegoda NB, London N, Bukau B, Rosenzweig R. </i> Nature, 2020","date":"2025-10-22T15:11:44.254Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"6Z5N"},{"db":"BMRB","id":"50167"}],"region_id":"DP04447r001","statement":[{"text":"Given the minor differences in the J-domain-driven binding of the two co-chaperones to HSP70, we next investigated the importance of the disordered GF-rich linker, as this domain has previously been reported to be essential in bacteria for maximal stimulation of the ATPase activity of DnaK17,18,19.","type":"Results"},{"text":"Measurement of the local backbone flexibility on the nano-to-picosecond timescale further indicated that residues 93–107 in the GF-rich region are highly structured, with calculated order parameters of 0.9–1.0 (see Methods, Extended Data Fig. 2c).","type":"Results"},{"text":"Manual inspection of the NMR structure indicates that the GF-rich linker is disordered in the region 75-92.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-23T15:43:49.998Z"}},{"start":75,"end":92,"reference_id":"33177718","reference_source":"pmid","reference_html":"HSP40 proteins use class-specific regulation to drive HSP70 functional diversity. <i> Faust O, Abayev-Avraham M, Wentink AS, Maurer M, Nillegoda NB, London N, Bukau B, Rosenzweig R. </i> Nature, 2020","date":"2025-10-22T15:13:04.581Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"6Z5N"},{"db":"BMRB","id":"50167"}],"region_id":"DP04447r002","statement":[{"text":"Given the minor differences in the J-domain-driven binding of the two co-chaperones to HSP70, we next investigated the importance of the disordered GF-rich linker, as this domain has previously been reported to be essential in bacteria for maximal stimulation of the ATPase activity of DnaK17,18,19.","type":"Results"},{"text":"Measurement of the local backbone flexibility on the nano-to-picosecond timescale further indicated that residues 93–107 in the GF-rich region are highly structured, with calculated order parameters of 0.9–1.0 (see Methods, Extended Data Fig. 2c).","type":"Results"},{"text":"Manual inspection of the NMR structure indicates that the GF-rich linker is disordered in the region 75-97.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-23T15:43:49.700Z"}}],"__v":0,"disorder_content":0.052941176470588235,"disprot_consensus":{"full":[{"start":75,"end":92,"type":"D"}],"Structural state":[{"start":75,"end":92,"type":"D"}],"Disorder function":[{"start":75,"end":92,"type":"F"}]}},{"acc":"P02829","sequence":"MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVEKEVPIPEEEKKDEEKKDEEKKDEDDKKPKLEEVDEEEEKKPKTKKVKEEVQEIEELNKTKPLWTRNPSDITQEEYNAFYKSISNDWEDPLYVKHFSVEGQLEFRAILFIPKRAPFDLFESKKKKNNIKLYVRRVFITDEAEDLIPEWLSFVKGVVDSEDLPLNLSREMLQQNKIMKVIRKNIVKKLIEAFNEIAEDSEQFEKFYSAFSKNIKLGVHEDTQNRAALAKLLRYNSTKSVDELTSLTDYVTRMPEHQKNIYYITGESLKAVEKSPFLDALKAKNFEVLFLTDPIDEYAFTQLKEFEGKTLVDITKDFELEETDEEKAEREKEIKEYEPLTKALKEILGDQVEKVVVSYKLLDAPAAIRTGQFGWSANMERIMKAQALRDSSMSSYMSSKKTFEISPKSPIIKELKKRVDEGGAQDKTVKDLTKLLYETALLTSGFSLDEPTSFASRINRLISLGLNIDEDEETETAPEASTAAPVEEVPADTEMEEVD","creator":"xcastro","dataset":["Stress response proteins"],"date":"2025-10-20T14:08:19.941Z","disprot_id":"DP04448","features":{"pfam":[{"id":"PF00183","name":"Hsp90 protein","start":183,"end":693},{"id":"PF13589","name":"Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase","start":30,"end":145}]},"genes":[{"name":{"value":"HSP82","_id":"68f64254953df1273414d675","evidences":[]},"synonyms":[{"value":"HSP90","_id":"68f64254953df1273414d676","evidences":[]}],"olnNames":[{"value":"YPL240C","_id":"68f64254953df1273414d677","evidences":[]}],"orfNames":[],"_id":"68f64254953df1273414d674"}],"length":709,"name":"ATP-dependent molecular chaperone HSP82","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":6,"released":"2026_06","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"regions":[{"start":678,"end":709,"reference_id":"16625188","reference_source":"pmid","reference_html":"Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. <i> Ali MM, Roe SM, Vaughan CK, Meyer P, Panaretou B, Piper PW, Prodromou C, Pearl LH. </i> Nature, 2006","date":"2025-10-23T07:04:55.207Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala107Asn","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"A full-length construct of yeast Hsp90 harbouring the mutation Ala107Asn and with residues 221–255 in the charged linker region deleted and replaced by LQHMASVD; an N-terminal and middle-segment (M-C) construct of yeast Hsp90 (residues 273–709); and full-length yeast p23 (Sba1) were inserted with the addition of an N-terminal His6 tag and PreScission protease cleavage site into pRSETA and expressed in E. coli BL21(DE3) pLysS."}]},{"term_id":"IDPO:00484","term_name":"deletion-insertion","term_namespace":"Protein mutation","value":"p.Glu221_Pro255delinsLysGlnHisMetAlaSerValAsp","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"2CG9"}],"region_id":"DP04448r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P28707"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15422","statements":[{"type":"Results","text":"Yeast Hsp90, with an Ala107Asn mutation shown to activate the ATPase cycle of Hsp90 (ref. 19) and with truncation of the dispensable charged-linker connecting the N domain and middle segments23, was crystallized together with the non-hydrolysable ATP analogue AMP-PNP and Sba1, the yeast homologue of p23 (ref. 11)."}],"entry_name":null}],"sequence_construct":"MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMENLSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVEKEVPIPLQHMASVDKTKKVKEEVQEIEELNKTKPLWTRNPSDITQEEYNAFYKSISNDWEDPLYVKHFSVEGQLEFRAILFIPKRAPFDLFESKKKKNNIKLYVRRVFITDEAEDLIPEWLSFVKGVVDSEDLPLNLSREMLQQNKIMKVIRKNIVKKLIEAFNEIAEDSEQFEKFYSAFSKNIKLGVHEDTQNRAALAKLLRYNSTKSVDELTSLTDYVTRMPEHQKNIYYITGESLKAVEKSPFLDALKAKNFEVLFLTDPIDEYAFTQLKEFEGKTLVDITKDFELEETDEEKAEREKEIKEYEPLTKALKEILGDQVEKVVVSYKLLDAPAAIRTGQFGWSANMERIMKAQALRDSSMSSYMSSKKTFEISPKSPIIKELKKRVDEGGAQDKTVKDLTKLLYETALLTSGFSLDEPTSFASRINRLISLGLN","statement":[{"text":"Residues 678–709, which provide the C-terminal EEVD binding sequence for TPR-domain co-chaperones33, are disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-23T15:46:56.022Z"}},{"start":678,"end":709,"reference_id":"16625188","reference_source":"pmid","reference_html":"Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex. <i> Ali MM, Roe SM, Vaughan CK, Meyer P, Panaretou B, Piper PW, Prodromou C, Pearl LH. </i> Nature, 2006","date":"2025-10-23T07:06:22.780Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala107Asn","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"A full-length construct of yeast Hsp90 harbouring the mutation Ala107Asn and with residues 221–255 in the charged linker region deleted and replaced by LQHMASVD; an N-terminal and middle-segment (M-C) construct of yeast Hsp90 (residues 273–709); and full-length yeast p23 (Sba1) were inserted with the addition of an N-terminal His6 tag and PreScission protease cleavage site into pRSETA and expressed in E. coli BL21(DE3) pLysS."}]},{"term_id":"IDPO:00484","term_name":"deletion-insertion","term_namespace":"Protein mutation","value":"p.Glu221_Pro255delinsLysGlnHisMetAlaSerValAsp","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"2CG9"}],"region_id":"DP04448r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P28707"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15422","statements":[{"type":"Results","text":"Yeast Hsp90, with an Ala107Asn mutation shown to activate the ATPase cycle of Hsp90 (ref. 19) and with truncation of the dispensable charged-linker connecting the N domain and middle segments23, was crystallized together with the non-hydrolysable ATP analogue AMP-PNP and Sba1, the yeast homologue of p23 (ref. 11)."}],"entry_name":null}],"sequence_construct":"MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMENLSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVEKEVPIPLQHMASVDKTKKVKEEVQEIEELNKTKPLWTRNPSDITQEEYNAFYKSISNDWEDPLYVKHFSVEGQLEFRAILFIPKRAPFDLFESKKKKNNIKLYVRRVFITDEAEDLIPEWLSFVKGVVDSEDLPLNLSREMLQQNKIMKVIRKNIVKKLIEAFNEIAEDSEQFEKFYSAFSKNIKLGVHEDTQNRAALAKLLRYNSTKSVDELTSLTDYVTRMPEHQKNIYYITGESLKAVEKSPFLDALKAKNFEVLFLTDPIDEYAFTQLKEFEGKTLVDITKDFELEETDEEKAEREKEIKEYEPLTKALKEILGDQVEKVVVSYKLLDAPAAIRTGQFGWSANMERIMKAQALRDSSMSSYMSSKKTFEISPKSPIIKELKKRVDEGGAQDKTVKDLTKLLYETALLTSGFSLDEPTSFASRINRLISLGLN","statement":[{"text":"Residues 678–709, which provide the C-terminal EEVD binding sequence for TPR-domain co-chaperones, are disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-23T15:47:15.886Z"}},{"start":702,"end":709,"reference_id":"28278223","reference_source":"pmid","reference_html":"The structure of FKBP38 in complex with the MEEVD tetratricopeptide binding-motif of Hsp90. <i> Blundell KL, Pal M, Roe SM, Pearl LH, Prodromou C. </i> PLoS One, 2017","date":"2025-10-23T07:07:43.778Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"GO:0019899","term_name":"enzyme binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"5MGX"},{"db":"ELM","id":"ELME000130"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"Q14318","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04448r004","statement":[{"text":"Attempts to crystallise the C-terminal domain of yeast Hsp90 with FKBP92-380 yielded crystals of FKBP92-380 in complex with MEEVD containing peptides of the C-terminal domain of yeast Hsp90.","type":"Results"},{"text":"The bound peptides found were DTEMEEVD, ATEMEEVD (where the side chain of the first aspartate residue was modeled as an alanine), EMEEVD and EMEE.","type":"Results"}],"term_comment":"","term_def":"\"Binding to an enzyme, a protein with catalytic activity.\" [GOC:jl]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-23T15:47:51.515Z"}},{"start":704,"end":709,"reference_id":"24012479","reference_source":"pmid","reference_html":"High-resolution structural analysis shows how Tah1 tethers Hsp90 to the R2TP complex. <i> Back R, Dominguez C, Rothé B, Bobo C, Beaufils C, Moréra S, Meyer P, Charpentier B, Branlant C, Allain FH, Manival X. </i> Structure, 2013","date":"2025-10-23T07:09:08.750Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"GO:0030911","term_name":"TPR domain binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"ELM","id":"ELME000130"},{"db":"PDB","id":"2LSV"}],"ec_go":"EXP","region_id":"DP04448r006","statement":[{"text":"The first three N-terminal residues of the Hsp90 (A701DT703) peptide adopt a rather flexible conformation, in contrast to the six other ones (E704MEEVD709; Figure 4B).","type":"Results"},{"text":"No interaction was observed between A701, D702, and T703 of Hsp90 and Tah1. Our structure shows that both the two canonical TPR motifs of Tah1 and helix C interact with the Hsp90 EMEEVD segment.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a tetratricopeptide repeat (TPR) domain of a protein, the consensus sequence of which is defined by a pattern of small and large hydrophobic amino acids and a structure composed of helices.\" [GOC:mah]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"Q14318","operator":null,"partner_start":null,"partner_end":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-23T15:47:40.969Z"}}],"__v":0,"disorder_content":0.045133991537376586,"disprot_consensus":{"full":[{"start":678,"end":709,"type":"D"}],"Structural state":[{"start":678,"end":709,"type":"D"}],"Disorder function":[{"start":678,"end":709,"type":"F"}],"Molecular function":[{"start":702,"end":709,"type":"F"}]}},{"acc":"Q13217","sequence":"MVAPGSVTSRLGSVFPFLLVLVDLQYEGAECGVNADVEKHLELGKKLLAAGQLADALSQFHAAVDGDPDNYIAYYRRATVFLAMGKSKAALPDLTKVIQLKMDFTAARLQRGHLLLKQGKLDEAEDDFKKVLKSNPSENEEKEAQSQLIKSDEMQRLRSQALNAFGSGDYTAAIAFLDKILEVCVWDAELRELRAECFIKEGEPRKAISDLKAASKLKNDNTEAFYKISTLYYQLGDHELSLSEVRECLKLDQDHKRCFAHYKQVKKLNKLIESAEELIRDGRYTDATSKYESVMKTEPSIAEYTVRSKERICHCFSKDEKPVEAIRVCSEVLQMEPDNVNALKDRAEAYLIEEMYDEAIQDYETAQEHNENDQQIREGLEKAQRLLKQSQKRDYYKILGVKRNAKKQEIIKAYRKLALQWHPDNFQNEEEKKKAEKKFIDIAAAKEVLSDPEMRKKFDDGEDPLDAESQQGGGGNPFHRSWNSWQGFNPFSSGGPFRFKFHFN","creator":"xcastro","dataset":["Stress response proteins"],"date":"2025-10-20T14:40:00.838Z","disprot_id":"DP04449","features":{"pfam":[{"id":"PF00226","name":"DnaJ domain","start":394,"end":459},{"id":"PF00515","name":"Tetratricopeptide repeat","start":108,"end":137},{"id":"PF13181","name":"Tetratricopeptide repeat","start":223,"end":255},{"id":"PF13432","name":"Tetratricopeptide repeat","start":41,"end":93},{"id":"PF14559","name":"Tetratricopeptide repeat","start":319,"end":377}]},"genes":[{"name":{"value":"DNAJC3","_id":"68f649c0953df1273414d690","evidences":[]},"synonyms":[{"value":"P58IPK","_id":"68f649c0953df1273414d691","evidences":[]},{"value":"PRKRI","_id":"68f649c0953df1273414d692","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"68f649c0953df1273414d68f"}],"length":504,"name":"DnaJ homolog subfamily C member 3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":1,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":455,"end":504,"reference_id":"21799829","reference_source":"pmid","reference_html":"The crystal structure of the human co-chaperone P58(IPK). <i> Svärd M, Biterova EI, Bourhis JM, Guy JE. </i> PLoS One, 2011","date":"2025-10-21T13:58:33.998Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008035","ec_ontology":"ECO","ec_name":"author inference based on intrinsic disorder prediction used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"2Y4T"}],"region_id":"DP04449r001","statement":[{"text":"The last six residues of the J domain are not visible in the electron density, despite being present in the crystallised protein. This, together with our observation that protein constructs including the C-terminal amino acid residues are not soluble, would appear to confirm predictions that the extreme C-terminus of P58IPK (approximately residues 455–504) is unstructured.","type":"Results"},{"text":"No constructs including the 43 C-terminal amino acid residues, which are predicted to be unstructured, could be expressed in soluble form.","type":"Results"}]}],"__v":0,"disorder_content":0.0992063492063492,"disprot_consensus":{"full":[{"start":455,"end":504,"type":"D"}],"Structural state":[{"start":455,"end":504,"type":"D"}]}},{"acc":"O75165","sequence":"MNIIRENKDLACFYTTKHSWRGKYKRVFSVGTHAITTYNPNTLEVTNQWPYGDICSISPVGKGQGTEFNLTFRKGSGKKSETLKFSTEHRTELLTEALRFRTDFSEGKITGRRYNCYKHHWSDSRKPVILEVTPGGFDQINPATNRVLCSYDYRNIEGFVDLSDYQGGFCILYGGFSRLHLFASEQREEIIKSAIDHAGNYIGISLRIRKEPLEFEQYLNLRFGKYSTDESITSLAEFVVQKISPRHSEPVKRVLALTETCLVERDPATYNIATLKPLGEVFALVCDSENPQLFTIEFIKGQVRKYSSTERDSLLASLLDGVRASGNRDVCVKMTPTHKGQRWGLLSMPVDEEVESLHLRFLATPPNGNFADAVFRFNANISYSGVLHAVTQDGLFSENKEKLINNAITALLSQEGDVVASNAELESQFQAVRRLVASKAGFLAFTQLPKFRERLGVKVVKALKRSNNGIIHAAVDMLCALMCPMHDDYDLRQEQLNKASLLSSKKFLENLLEKFNSHVDHGTGALVISSLLDFLTFALCAPYSETTEGQQFDMLLEMVASNGRTLFKLFQHPSMAIIKGAGLVMKAIIEEGDKEIATKMQELALSEGALPRHLHTAMFTISSDQRMLTNRQLSRHLVGLWTADNATATNLLKRILPPGLLAYLESSDLVPEKDADRMHVRDNVKIAMDQYGKFNKVPEWQRLAGKAAKEVEKFAKEKVDLVLMHWRDRMGIAQKENINQKPVVLRKRRQRIKIEANWDLFYYRFGQDHARSNLIWNFKTREELKDTLESEMRAFNIDRELGSANVISWNHHEFEVKYECLAEEIKIGDYYLRLLLEEDENEESGSIKRSYEFFNELYHRFLLTPKVNMKCLCLQALAIVYGRCHEEIGPFTDTRYIIGMLERCTDKLERDRLILFLNKLILNKKNVKDLMDSNGIRILVDLLTLAHLHVSRATVPLQSNVIEAAPDMKRESEKEWYFGNADKERSGPYGFHEMQELWTKGMLNAKTRCWAQGMDGWRPLQSIPQLKWCLLASGQAVLNETDLATLILNMLITMCGYFPSRDQDNAIIRPLPKVKRLLSDSTCLPHIIQLLLTFDPILVEKVAILLYHIMQDNPQLPRLYLSGVFFFIMMYTGSNVLPVARFLKYTHTKQAFKSEETKGQDIFQRSILGHILPEAMVCYLENYEPEKFSEIFLGEFDTPEAIWSSEMRRLMIEKIAAHLADFTPRLQSNTRALYQYCPIPIINYPQLENELFCNIYYLKQLCDTLRFPDWPIKDPVKLLKDTLDAWKKEVEKKPPMMSIDDAYEVLNLPQGQGPHDESKIRKAYFRLAQKYHPDKNPEGRDMFEKVNKAYEFLCTKSAKIVDGPDPENIILILKTQSILFNRHKEDLQPYKYAGYPMLIRTITMETSDDLLFSKESPLLPAATELAFHTVNCSALNAEELRRENGLEVLQEAFSRCVAVLTRASKPSDMSVQVCGYISKCYSVAAQFEECREKITEMPSIIKDLCRVLYFGKSIPRVAALGVECVSSFAVDFWLQTHLFQAGILWYLLGFLFNYDYTLEESGIQKSEETNQQEVANSLAKLSVHALSRLGGYLAEEQATPENPTIRKSLAGMLTPYVARKLAVASVTEILKMLNSNTESPYLIWNNSTRAELLEFLESQQENMIKKGDCDKTYGSEFVYSDHAKELIVGEIFVRVYNEVPTFQLEVPKAFAASLLDYIGSQAQYLHTFMAITHAAKVESEQHGDRLPRVEMALEALRNVIKYNPGSESECIGHFKLIFSLLRVHGAGQVQQLALEVVNIVTSNQDCVNNIAESMVLSSLLALLHSLPSSRQLVLETLYALTSSTKIIKEAMAKGALIYLLDMFCNSTHPQVRAQTAELFAKMTADKLIGPKVRITLMKFLPSVFMDAMRDNPEAAVHIFEGTHENPELIWNDNSRDKVSTTVREMMLEHFKNQQDNPEANWKLPEDFAVVFGEAEGELAVGGVFLRIFIAQPAWVLRKPREFLIALLEKLTELLEKNNPHGETLETLTMATVCLFSAQPQLADQVPPLGHLPKVIQAMNHRNNAIPKSAIRVIHALSENELCVRAMASLETIGPLMNGMKKRADTVGLACEAINRMFQKEQSELVAQALKADLVPYLLKLLEGIGLENLDSPAATKAQIVKALKAMTRSLQYGEQVNEILCRSSVWSAFKDQKHDLFISESQTAGYLTGPGVAGYLTAGTSTSVMSNLPPPVDHEAGDLGYQT","creator":"vnugnes","dataset":[],"date":"2025-10-20T14:48:19.788Z","disprot_id":"DP04450","features":{"pfam":[{"id":"PF00226","name":"DnaJ domain","start":1301,"end":1357},{"id":"PF14237","name":"GYF domain 2","start":976,"end":1026},{"id":"PF19432","name":"DNAJ protein RME-8 N-terminal domain","start":12,"end":104},{"id":"PF29707","name":"DNAJ protein RME-8 2nd domain","start":114,"end":205},{"id":"PF29708","name":"DNAJ protein RME-8 4th domain","start":349,"end":482}]},"genes":[{"name":{"value":"DNAJC13","_id":"68f64bb3953df1273414d699","evidences":[]},"synonyms":[{"value":"KIAA0678","_id":"68f64bb3953df1273414d69a","evidences":[]},{"value":"RME8","_id":"68f64bb3953df1273414d69b","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"68f64bb3953df1273414d698"}],"length":2243,"name":"DnaJ homolog subfamily C member 13","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":2,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":2198,"end":2243,"reference_id":"40737286","reference_source":"pmid","reference_html":"DNAJC13 localization to endosomes is opposed by its J domain and its disordered C-terminus. <i> Adoff H, Novy B, Holland E, Lobingier BT. </i> Mol Biol Cell, 2025","date":"2025-10-20T14:50:06.717Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008031","ec_ontology":"ECO","ec_name":"author inference based on intrinsic disorder prediction","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04450r001","statement":[{"text":"We noted that the AF2 model of human DNAJC13 predicted the final 45 amino acids of its C-terminus to be an IDR (Figure 1A). We next examined two other structural prediction programs, the disorder predictor JRonn and five additional AF3 models, which also predicted the C-terminus of DNAJC13 to be disordered (Figure S1A) (Waterhouse et al., 2009; Troshin et al., 2011; Abramson et al., 2024).","type":"Results"}]},{"start":2199,"end":2243,"reference_id":"40737286","reference_source":"pmid","reference_html":"DNAJC13 localization to endosomes is opposed by its J domain and its disordered C-terminus. <i> Adoff H, Novy B, Holland E, Lobingier BT. </i> Mol Biol Cell, 2025","date":"2025-10-20T15:05:59.954Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0032456","term_name":"endocytic recycling","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ser2199Thr2243del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04450r002","statement":[{"text":"We first examined DNAJC13FL and found that overexpression of this construct had no effect on β2AR recycling relative to an empty vector control (Figure 5F). Comparatively, overexpression of DNAJC13 with single or double mutations to its J domain and/or disordered C-terminus resulted in an overt reduction in β2AR recycling (Figure 5F).","type":"Results"}],"term_comment":"","term_def":"\"The directed movement of membrane-bounded vesicles from endosomes back to the plasma membrane, a trafficking pathway that promotes the recycling of internalized transmembrane proteins.\" [PMID:16473635, PMID:23563491]","term_is_obsolete":false,"term_not_annotate":false}],"__v":0,"disorder_content":0.02050824788230049,"disprot_consensus":{"full":[{"start":2198,"end":2243,"type":"D"}],"Structural state":[{"start":2198,"end":2243,"type":"D"}],"Biological process":[{"start":2199,"end":2243,"type":"F"}]}},{"acc":"Q15759","sequence":"MSGPRAGFYRQELNKTVWEVPQRLQGLRPVGSGAYGSVCSAYDARLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHLKHENVIGLLDVFTPATSIEDFSEVYLVTTLMGADLNNIVKCQALSDEHVQFLVYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQADEEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLQGKALFPGSDYIDQLKRIMEVVGTPSPEVLAKISSEHARTYIQSLPPMPQKDLSSIFRGANPLAIDLLGRMLVLDSDQRVSAAEALAHAYFSQYHDPEDEPEAEPYDESVEAKERTLEEWKELTYQEVLSFKPPEPPKPPGSLEIEQ","creator":"xcastro","dataset":["Stress response proteins"],"date":"2025-10-21T12:30:56.924Z","disprot_id":"DP04451","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":27,"end":308}]},"genes":[{"name":{"value":"MAPK11","_id":"68f77d01953df1273414d6ce","evidences":[]},"synonyms":[{"value":"PRKM11","_id":"68f77d01953df1273414d6cf","evidences":[]},{"value":"SAPK2","_id":"68f77d01953df1273414d6d0","evidences":[]},{"value":"SAPK2B","_id":"68f77d01953df1273414d6d1","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"68f77d01953df1273414d6cd"}],"length":364,"name":"Mitogen-activated protein kinase 11","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":4,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":173,"end":183,"reference_id":"19622861","reference_source":"pmid","reference_html":"The three-dimensional structure of MAP kinase p38beta: different features of the ATP-binding site in p38beta compared with p38alpha. <i> Patel SB, Cameron PM, O'Keefe SJ, Frantz-Wattley B, Thompson J, O'Neill EA, Tennis T, Liu L, Becker JW, Scapin G. </i> Acta Crystallogr D Biol Crystallogr, 2009","date":"2025-10-23T13:36:13.342Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys119Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Crystals of the double C119S,C162S mutant were obtained after pre-incubation of the protein (10 mg ml−1 in 20 mM Tris pH 7.4, 100 mM NaCl, 5% glycerol and 2 mM TCEP) with a two­fold molar excess of compound 1 and 500 mM ZnCl2 for about 2 h in ice; crystals were obtained in hanging drops by mixing 1 µl protein solution and 1 µl reservoir solution and equilibrating against 0.5 ml of a reservoir solution containing 12–14% PEG, 0.12 M ammonium fluoride, 1% DMSO, 30 µM CTAB and 10–20 mM LiCl."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys162Ser","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"3GC9"}],"region_id":"DP04451r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29101","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"23532664"}],"sequence_construct":"GSHMLEMSGPRAGFYRQELNKTVWEVPQRLQGLRPVGSGAYGSVCSAYDARLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHLKHENVIGLLDVFTPATSIEDFSEVYLVTTLMGADLNNIVKSQALSDEHVQFLVYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDSELRILDFGLARQADEEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLQGKALFPGSDYIDQLKRIMEVVGTPSPEVLAKISSEHARTYIQSLPPMPQKDLSSIFRGANPLAIDLLGRMLVLDSDQRVSAAEALAHAYFSQYHDPEDEPEAEPYDESVEAKERTLEEWKELTYQEVLSFKPPEPPKPPGSLEIEQ","statement":[{"text":"The 2.05 Å structure of p38β contains residues 3–172 and 184–348 for the first monomer and residues 2–173 and 183–349 for the second monomer. No electron density was visible for the activation loop (residues 173–183) in either monomer. The two monomers in the asymmetric unit are substantially identical (the r.m.s.d. on Cα atoms for 325 residues is 0.725 Å), with the exception of the loop spanning residues 242–266, which appears to be more disordered in one of the monomers than in the other.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-23T15:49:41.740Z"}},{"start":350,"end":364,"reference_id":"19622861","reference_source":"pmid","reference_html":"The three-dimensional structure of MAP kinase p38beta: different features of the ATP-binding site in p38beta compared with p38alpha. <i> Patel SB, Cameron PM, O'Keefe SJ, Frantz-Wattley B, Thompson J, O'Neill EA, Tennis T, Liu L, Becker JW, Scapin G. </i> Acta Crystallogr D Biol Crystallogr, 2009","date":"2025-10-23T13:35:56.097Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys119Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Crystals of the double C119S,C162S mutant were obtained after pre-incubation of the protein (10 mg ml−1 in 20 mM Tris pH 7.4, 100 mM NaCl, 5% glycerol and 2 mM TCEP) with a two­fold molar excess of compound 1 and 500 mM ZnCl2 for about 2 h in ice; crystals were obtained in hanging drops by mixing 1 µl protein solution and 1 µl reservoir solution and equilibrating against 0.5 ml of a reservoir solution containing 12–14% PEG, 0.12 M ammonium fluoride, 1% DMSO, 30 µM CTAB and 10–20 mM LiCl."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys162Ser","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"3GC9"}],"region_id":"DP04451r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29101","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"23532664"}],"sequence_construct":"GSHMLEMSGPRAGFYRQELNKTVWEVPQRLQGLRPVGSGAYGSVCSAYDARLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHLKHENVIGLLDVFTPATSIEDFSEVYLVTTLMGADLNNIVKSQALSDEHVQFLVYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDSELRILDFGLARQADEEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLQGKALFPGSDYIDQLKRIMEVVGTPSPEVLAKISSEHARTYIQSLPPMPQKDLSSIFRGANPLAIDLLGRMLVLDSDQRVSAAEALAHAYFSQYHDPEDEPEAEPYDESVEAKERTLEEWKELTYQEVLSFKPPEPPKPPGSLEIEQ","statement":[{"text":"The 2.05 Å structure of p38β contains residues 3–172 and 184–348 for the first monomer and residues 2–173 and 183–349 for the second monomer. No electron density was visible for the activation loop (residues 173–183) in either monomer. The two monomers in the asymmetric unit are substantially identical (the r.m.s.d. on Cα atoms for 325 residues is 0.725 Å), with the exception of the loop spanning residues 242–266, which appears to be more disordered in one of the monomers than in the other.","type":"Results"},{"text":"Although the authors did not explicitly state it, manual inspection of the structure shows that the C-terminal region (residues 350–364) has missing residues, consistent with disorder.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-23T15:49:58.870Z"}},{"start":350,"end":364,"reference_id":"19622861","reference_source":"pmid","reference_html":"The three-dimensional structure of MAP kinase p38beta: different features of the ATP-binding site in p38beta compared with p38alpha. <i> Patel SB, Cameron PM, O'Keefe SJ, Frantz-Wattley B, Thompson J, O'Neill EA, Tennis T, Liu L, Becker JW, Scapin G. </i> Acta Crystallogr D Biol Crystallogr, 2009","date":"2025-10-23T13:36:03.840Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys119Ser","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Crystals of the double C119S,C162S mutant were obtained after pre-incubation of the protein (10 mg ml−1 in 20 mM Tris pH 7.4, 100 mM NaCl, 5% glycerol and 2 mM TCEP) with a two­fold molar excess of compound 1 and 500 mM ZnCl2 for about 2 h in ice; crystals were obtained in hanging drops by mixing 1 µl protein solution and 1 µl reservoir solution and equilibrating against 0.5 ml of a reservoir solution containing 12–14% PEG, 0.12 M ammonium fluoride, 1% DMSO, 30 µM CTAB and 10–20 mM LiCl."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys162Ser","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"3GC9"}],"region_id":"DP04451r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29101","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"23532664"}],"sequence_construct":"GSHMLEMSGPRAGFYRQELNKTVWEVPQRLQGLRPVGSGAYGSVCSAYDARLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHLKHENVIGLLDVFTPATSIEDFSEVYLVTTLMGADLNNIVKSQALSDEHVQFLVYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDSELRILDFGLARQADEEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLQGKALFPGSDYIDQLKRIMEVVGTPSPEVLAKISSEHARTYIQSLPPMPQKDLSSIFRGANPLAIDLLGRMLVLDSDQRVSAAEALAHAYFSQYHDPEDEPEAEPYDESVEAKERTLEEWKELTYQEVLSFKPPEPPKPPGSLEIEQ","statement":[{"text":"The 2.05 Å structure of p38β contains residues 3–172 and 184–348 for the first monomer and residues 2–173 and 183–349 for the second monomer. No electron density was visible for the activation loop (residues 173–183) in either monomer. The two monomers in the asymmetric unit are substantially identical (the r.m.s.d. on Cα atoms for 325 residues is 0.725 Å), with the exception of the loop spanning residues 242–266, which appears to be more disordered in one of the monomers than in the other.","type":"Results"},{"text":"Although the authors did not explicitly state it, manual inspection of the structure shows that the C-terminal region (residues 350–364) has missing residues, consistent with disorder.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-23T15:50:21.472Z"}},{"start":179,"end":183,"reference_id":"38270553","reference_source":"pmid","reference_html":"Proline-directed yeast and human MAP kinases phosphorylate the Dot1p/DOT1L histone H3K79 methyltransferase. <i> Separovich RJ, Karakatsanis NM, Gao K, Fuh D, Hamey JJ, Wilkins MR. </i> FEBS J, 2024","date":"2025-10-23T13:46:31.610Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001582","ec_ontology":"ECO","ec_name":"liquid chromatography coupled with tandem mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":180,"end":180,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":182,"end":182,"position":"Specific residue"}],"region_id":"DP04451r004","statement":[{"text":"DOT1L was incubated in the presence or the absence of p38β and ATP for 2 h (Fig. 7C), digested with trypsin, and resultant peptides were then analysed by high-resolution LC–MS/MS for phosphosite identification and quantification. We note that the activating phosphosites at T180 and Y182 of human p38β were identified in the bacterially expressed enzyme (Fig. 7D), thus making it suitable for use in in vitro kinase assays.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-23T15:26:36.155Z"}}],"__v":0,"disorder_content":0.07142857142857142,"disprot_consensus":{"full":[{"start":173,"end":183,"type":"D"},{"start":350,"end":364,"type":"D"}],"Structural state":[{"start":173,"end":183,"type":"D"},{"start":350,"end":364,"type":"D"}],"Disorder function":[{"start":179,"end":183,"type":"F"},{"start":350,"end":364,"type":"F"}]}},{"acc":"Q16539","sequence":"MSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGAELLKKISSESARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES","creator":"xcastro","dataset":["Stress response proteins"],"date":"2025-10-22T08:19:03.884Z","disprot_id":"DP04452","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":24,"end":308}]},"genes":[{"name":{"value":"MAPK14","evidences":[{"source":{"id":"HGNC:6876","name":"HGNC","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6876","_id":"68f893782ea0defb7a2f2d6b"},"code":"ECO:0000312","_id":"68f893782ea0defb7a2f2d6a"}],"_id":"68f893782ea0defb7a2f2d69"},"synonyms":[{"value":"CSBP","_id":"68f893782ea0defb7a2f2d6c","evidences":[]},{"value":"CSBP1","_id":"68f893782ea0defb7a2f2d6d","evidences":[]},{"value":"CSBP2","_id":"68f893782ea0defb7a2f2d6e","evidences":[]},{"value":"CSPB1","_id":"68f893782ea0defb7a2f2d6f","evidences":[]},{"value":"MXI2","_id":"68f893782ea0defb7a2f2d70","evidences":[]},{"value":"SAPK2A","_id":"68f893782ea0defb7a2f2d71","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"68f893782ea0defb7a2f2d68"}],"length":360,"name":"Mitogen-activated protein kinase 14","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":6,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":171,"end":182,"reference_id":"16342939","reference_source":"pmid","reference_html":"Prevention of MKK6-dependent activation by binding to p38alpha MAP kinase. <i> Sullivan JE, Holdgate GA, Campbell D, Timms D, Gerhardt S, Breed J, Breeze AL, Bermingham A, Pauptit RA, Norman RA, Embrey KJ, Read J, VanScyoc WS, Ward WH. </i> Biochemistry, 2005","date":"2025-10-22T09:52:26.098Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"2BAK"}],"region_id":"DP04452r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":1,"db":"PubChem","id":"5327065","statements":[{"type":"Methods","text":"For each compound, 200 μM nonphosphorylated p38α and 1 mM inhibitor were  incubated for 30 min at 4 °C and then centrifuged (14000 rpm, 4 °C, 15 min) immediately prior to using the supernatant."}]}],"statement":[{"text":"The docking groove residues 118−120 are not visible in the electron density, nor are residues 171−182 of the activation loop.","type":"Results"},{"text":"This loop is not ordered in many crystal structures, although it is defined in the complexes of p38α with SB203580 (DFG-in) and the pyrazolourea (DFG-out). An overlay of these structures (Figure 6) reveals the possible extent of movement of the activation loop and resultant differences in the environments of the phosphoryl acceptors at Thr180 and Tyr182. DFG-out evidently results in a range of conformations, ordered or disordered, which can be accommodated in the crystals.","type":"Discussion"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Supplementary material","text":"DNA constructs encoding p38α (residue 2 to C-terminus), with either an Nterminal-6His-16j tag (MGSSHHHHHHLVPRGSH), or an N-terminal-cmyc6His tag (MGSEQKLISEEDLNAHHHHHH), were cloned into a pT73.3 vector (1), using the Xho1 and Ase1 restriction enzyme sites."}]}],"sequence_construct":"HHHHHHSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGAELLKKISSESARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-22T16:41:36.718Z"}},{"start":179,"end":183,"reference_id":"7535770","reference_source":"pmid","reference_html":"Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine. <i> Raingeaud J, Gupta S, Rogers JS, Dickens M, Han J, Ulevitch RJ, Davis RJ. </i> J Biol Chem, 1995","date":"2025-10-22T09:35:54.109Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001243","ec_ontology":"ECO","ec_name":"phosphoamino acid analysis evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04452r002","statement":[{"text":"To test whether this motif is relevant to the activation of p38, we examined the effect of the replacement of Thr-Gly-Tyr with Ala-Gly-Phe. The wild-type and mutant forms of p38 were expressed at similar levels (Fig. 9A).","type":"Results"},{"text":"Significantly, the increased phosphorylation on Tyr and Thr was blocked by mutation of the dual phosphorylation motif Thr-Gly-Tyr (Fig. 4, A and B).","type":"Results"},{"text":"UV radiation caused a marked increase in the activity of wild-type (Thr-Gly-Tyr) p38 (Fig. 9C). In contrast, the mutated (Ala-Gly-Phe) p38 was found to be catalytically inactive (Fig. 9C). Together, these data demonstrate that p38 is activated by dual phosphorylation within the motif Thr-Gly-Tyr.","type":"Results"},{"text":"Panel A, COS-1 cells expressing wild-type (Thr180-Gly-Tyr182) or mutated (Ala180-Gly-Phe182) p38 MAP kinase were treated without and with UV-C (40 J/m2).","type":"Figure"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-22T17:23:00.848Z"}},{"start":179,"end":183,"reference_id":"7535770","reference_source":"pmid","reference_html":"Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine. <i> Raingeaud J, Gupta S, Rogers JS, Dickens M, Han J, Ulevitch RJ, Davis RJ. </i> J Biol Chem, 1995","date":"2025-10-23T07:24:39.546Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"GO:0004674","term_name":"protein serine/threonine kinase activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IMP","region_id":"DP04452r003","statement":[{"text":"To test whether this motif is relevant to the activation of p38, we examined the effect of the replacement of Thr-Gly-Tyr with Ala-Gly-Phe. The wild-type and mutant forms of p38 were expressed at similar levels (Fig. 9A).","type":"Results"},{"text":"Significantly, the increased phosphorylation on Tyr and Thr was blocked by mutation of the dual phosphorylation motif Thr-Gly-Tyr (Fig. 4, A and B).","type":"Results"},{"text":"UV radiation caused a marked increase in the activity of wild-type (Thr-Gly-Tyr) p38 (Fig. 9C). In contrast, the mutated (Ala-Gly-Phe) p38 was found to be catalytically inactive (Fig. 9C). Together, these data demonstrate that p38 is activated by dual phosphorylation within the motif Thr-Gly-Tyr.","type":"Results"},{"text":"Panel A, COS-1 cells expressing wild-type (Thr180-Gly-Tyr182) or mutated (Ala180-Gly-Phe182) p38 MAP kinase were treated without and with UV-C (40 J/m2).","type":"Figure"}],"term_comment":"","term_def":"\"Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.\" [GOC:bf, PMID:2956925]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr180Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test whether this motif is relevant to the activation of p38, we examined the effect of the replacement of Thr-Gly-Tyr with Ala-Gly-Phe."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Tyr182Phe","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-23T15:50:49.982Z"}},{"start":179,"end":183,"reference_id":"23079240","reference_source":"pmid","reference_html":"Lipid molecules induce p38α activation via a novel molecular switch. <i> Tzarum N, Eisenberg-Domovich Y, Gills JJ, Dennis PA, Livnah O. </i> J Mol Biol, 2012","date":"2025-10-22T17:01:08.049Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0000279","ec_ontology":"ECO","ec_name":"qualitative western immunoblotting evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04452r004","statement":[{"text":"The phosphorylation level of dually phosphorylated p38αwt was used as a positive control and that of inactive p38αwt was used as a negative control. Western blot analysis revealed that the three mutants at the αEF/αF loop were similarly phosphorylated on both Thr180 and Tyr182 as the activated p38αwt (Fig. 3a).","type":"Results"}]},{"start":171,"end":185,"reference_id":"23079240","reference_source":"pmid","reference_html":"Lipid molecules induce p38α activation via a novel molecular switch. <i> Tzarum N, Eisenberg-Domovich Y, Gills JJ, Dennis PA, Livnah O. </i> J Mol Biol, 2012","date":"2025-10-22T17:06:49.525Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"4E5B"}],"region_id":"DP04452r005","statement":[{"text":"This region lacks electron density in the PDB structure, indicating it is disordered.","type":"Results"}]},{"start":179,"end":183,"reference_id":"7535770","reference_source":"pmid","reference_html":"Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine. <i> Raingeaud J, Gupta S, Rogers JS, Dickens M, Han J, Ulevitch RJ, Davis RJ. </i> J Biol Chem, 1995","date":"2025-10-22T19:56:26.971Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051403","term_name":"stress-activated MAPK cascade","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr180Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test whether this motif is relevant to the activation of p38, we examined the effect of the replacement of Thr-Gly-Tyr with Ala-Gly-Phe."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Tyr182Phe","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test whether this motif is relevant to the activation of p38, we examined the effect of the replacement of Thr-Gly-Tyr with Ala-Gly-Phe."}]}],"ec_go":"IMP","region_id":"DP04452r006","statement":[{"text":"Phosphorylation of ATF2 caused by p38 resulted in an electrophoretic mobility shift during polyacrylamide gel electrophoresis. ","type":"Results"},{"text":"We conclude that p38 phosphorylates ATF2 within the NH2-terminal activation domain on Thr-69 and Thr-71. Significantly, the phosphorylation of ATF2 on these sites causes increased transcriptional activity(25). Thus, the transcription factor ATF2 is a potential target of signal transduction by p38 MAP kinase and JNK.","type":"Results"},{"text":"It was observed that environmental stress (UV radiation and osmotic shock) caused a marked increase in the activity of both p38 and JNK (Fig. 4 and Fig. 5).","type":"Results"},{"text":"The requirement of dual phosphorylation for activation establishes that p38 is a member of the MAP kinase group of signal transducing proteins(1).","type":"Discussion"},{"text":"When the residues Thr180 and Tyr182 are mutated, and prevented from being phosphorylated, MAPK13 is no longer activated as response to the UV stress, nor is capable to phosphorylate other actors like the transcription factor AFT2. This evidence shows how these residues are important for the protein involvement in the tress-activated MAPK cascade.","type":"Curator statement"}],"term_comment":"","term_def":"\"A series of molecular signals in which a stress-activated MAP kinase cascade relays one or more of the signals; MAP kinase cascades involve at least three protein kinase activities and culminate in the phosphorylation and activation of a MAP kinase.\" [GOC:ai, PMID:15936270]","term_is_obsolete":false,"term_not_annotate":false}],"__v":0,"disorder_content":0.041666666666666664,"disprot_consensus":{"full":[{"start":171,"end":185,"type":"D"}],"Structural state":[{"start":171,"end":185,"type":"D"}],"Disorder function":[{"start":179,"end":183,"type":"F"}],"Molecular function":[{"start":179,"end":183,"type":"F"}],"Biological process":[{"start":179,"end":183,"type":"F"}]}},{"acc":"Q8C6L5","sequence":"MEDPRRRTTAPRAKKPSAKRAPTQPSRTRAHAESCGPQRGARSRRAERDGDTTEKPRAPGPRVHPARATELTKDAQPSAMDAAGATARPAVRVPQQQAILDPELPAVREPQPPADPEARKVVRGPSHRRGARSTGQPRAPRGSRKEPDKLKKVLDKLRLKRKDISEAAETVNKVVERLLRRMQKRESEFKGVEQLNTGSYYEHVKISAPNEFDVMFKLEVPRIELQEYYETGAFYLVKFKRIPRGNPLSHFLEGEVLSATKMLSKFRKIIKEEVKEIKDIDVSVEKEKPGSPAVTLLIRNPEEISVDIILALESKGSWPISTKEGLPIQGWLGTKVRTNLRREPFYLVPKNAKDGNSFQGETWRLSFSHTEKYILNNHGIEKTCCESSGAKCCRKECLKLMKYLLEQLKKEFQELDAFCSYHVKTAIFHMWTQDPQDSQWDPRNLSSCFDKLLAFFLECLRTEKLDHYFIPKFNLFSQELIDRKSKEFLSKKIEYERNNGFPIFDKL","creator":"rpancsa","dataset":["Condensates-related proteins"],"date":"2025-10-22T08:25:37.246Z","disprot_id":"DP04453","features":{"pfam":[{"id":"PF03281","name":"Mab-21 protein nucleotidyltransferase domain","start":200,"end":377},{"id":"PF20266","name":"Mab-21 protein HhH/H2TH-like domain","start":393,"end":494}]},"genes":[{"name":{"value":"Cgas","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/23258413","id":"23258413","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/23258413","_id":"68f895012ea0defb7a2f2d7c"},"code":"ECO:0000303","_id":"68f895012ea0defb7a2f2d7b"},{"source":{"id":"MGI:2442261","name":"MGI","url":"http://www.informatics.jax.org/marker/MGI:2442261","_id":"68f895012ea0defb7a2f2d7e"},"code":"ECO:0000312","_id":"68f895012ea0defb7a2f2d7d"}],"_id":"68f895012ea0defb7a2f2d7a"},"synonyms":[{"value":"Mb21d1","_id":"68f895012ea0defb7a2f2d7f","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"68f895012ea0defb7a2f2d79"}],"length":507,"name":"Cyclic GMP-AMP synthase","ncbi_taxon_id":10090,"organism":"Mus musculus","regions_counter":1,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"regions":[{"start":1,"end":146,"reference_id":"39754705","reference_source":"pmid","reference_html":"Assignment of the N-terminal domain of mouse cGAS. <i> Aucharova H, Linser R. </i> Biomol NMR Assign, 2025","date":"2025-11-12T09:32:23.846Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"BMRB","id":"52649"}],"region_id":"DP04453r001","statement":[{"text":"The mNTD 1H-15N HSQC spectrum displays limited peak dispersion, with 1HN chemical shifts clustered between 7.7 and 8.7 ppm, indicating a predominantly disordered structure.","type":"Article"}],"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6,"statements":[{"type":"Article","text":"The protein was then concentrated again to a final volume of 2 ml and exchanged into NMR buffer (20 mM MES pH 6.0, 0.1 M NaCl, 5 mM TCEP, 1 mM PMSF)."}]},{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Article","text":"All NMR experiments were recorded at 25 °C on a Bruker Avance III HD 800 MHz spectrometer equipped with a 2H, 1H, 13C, 15N four-channel cryogenic TCI probe."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-26T19:22:41.994Z"}}],"__v":0,"disorder_content":0.2879684418145957,"disprot_consensus":{"full":[{"start":1,"end":146,"type":"D"}],"Structural state":[{"start":1,"end":146,"type":"D"}]}},{"acc":"P25294","sequence":"MVKETKLYDLLGVSPSANEQELKKGYRKAALKYHPDKPTGDTEKFKEISEAFEILNDPQKREIYDQYGLEAARSGGPSFGPGGPGGAGGAGGFPGGAGGFSGGHAFSNEDAFNIFSQFFGGSSPFGGADDSGFSFSSYPSGGGAGMGGMPGGMGGMHGGMGGMPGGFRSASSSPTYPEEETVQVNLPVSLEDLFVGKKKSFKIGRKGPHGASEKTQIDIQLKPGWKAGTKITYKNQGDYNPQTGRRKTLQFVIQEKSHPNFKRDGDDLIYTLPLSFKESLLGFSKTIQTIDGRTLPLSRVQPVQPSQTSTYPGQGMPTPKNPSQRGNLIVKYKVDYPISLNDAQKRAIDENF","creator":"rpancsa","dataset":["Condensates-related proteins"],"date":"2025-10-22T11:34:12.799Z","disprot_id":"DP04455","features":{"pfam":[{"id":"PF00226","name":"DnaJ domain","start":7,"end":65},{"id":"PF01556","name":"DnaJ C terminal domain","start":182,"end":337}]},"genes":[{"name":{"value":"SIS1","_id":"68f8c1352ea0defb7a2f2d9f","evidences":[]},"synonyms":[],"olnNames":[{"value":"YNL007C","_id":"68f8c1352ea0defb7a2f2da0","evidences":[]}],"orfNames":[{"value":"N2879","_id":"68f8c1352ea0defb7a2f2da1","evidences":[]}],"_id":"68f8c1352ea0defb7a2f2d9e"}],"length":352,"name":"Protein SIS1","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":2,"released":"2026_06","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"regions":[{"start":76,"end":180,"reference_id":"39738939","reference_source":"pmid","reference_html":"Backbone NMR resonance assignment of Sis1, a type B J-domain protein from Saccharomyces cerevisiae. <i> Pinheiro GMS, Amorim GC, Matos CO, Ramos CHI, Almeida FCL. </i> Biomol NMR Assign, 2025","date":"2025-11-12T09:50:41.144Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":7.5,"statements":[{"type":"Article","text":"The NMR samples were prepared with 250 μM Sis1 in 25 mM Tris-HCl (pH 7.5), 200 mM NaCl, and 10% D2O."}]},{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":"within normal range","value":303,"statements":[{"type":"Article","text":"All NMR spectra were acquired on a Bruker 950 MHz SB Avance III spectrometer equipped with a cryo TCI (1H, 13 C, 15 N, 2 H) probe, 5 mm, z-gradient (IBS NMR Platform) in Grenoble, France, and on a Bruker Avance III HD 900 MHz\nspectrometer equipped with an inverse-detection triple resonance z-gradient TXI probe at 303 K, at the National Center of Nuclear Magnetic Resonance, at the Federal University of Rio de Janeiro (CNRMN)."}]}],"cross_refs":[{"db":"BMRB","id":"51817"}],"region_id":"DP04455r001","statement":[{"text":"The results show S2 > 0.7, indicating order at the J-domain and CTDs and low-order parameters (S2 < 0.7) for the GF/GM region, as expected,\nowing to the intrinsic flexibility of this region.","type":"Article"},{"text":"The boundaries of the disordered linker are not named in the article but they could be derived from Figure 3, where the Random coil propensity jumps at approximately residues 76 and (with the exception of one single helix between residues 107-119) stays high until residue ~180.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-05T14:36:56.755Z"}},{"start":76,"end":180,"reference_id":"39738939","reference_source":"pmid","reference_html":"Backbone NMR resonance assignment of Sis1, a type B J-domain protein from Saccharomyces cerevisiae. <i> Pinheiro GMS, Amorim GC, Matos CO, Ramos CHI, Almeida FCL. </i> Biomol NMR Assign, 2025","date":"2025-11-12T09:53:29.463Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":7.5,"statements":[{"type":"Article","text":"The NMR samples were prepared with 250 μM Sis1 in 25 mM Tris-HCl (pH 7.5), 200 mM NaCl, and 10% D2O."}]},{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":"within normal range","value":303,"statements":[{"type":"Article","text":"All NMR spectra were acquired on a Bruker 950 MHz SB Avance III spectrometer equipped with a cryo TCI (1H, 13 C, 15 N, 2 H) probe, 5 mm, z-gradient (IBS NMR Platform) in Grenoble, France, and on a Bruker Avance III HD 900 MHz\nspectrometer equipped with an inverse-detection triple resonance z-gradient TXI probe at 303 K, at the National Center of Nuclear Magnetic Resonance, at the Federal University of Rio de Janeiro (CNRMN)."}]}],"cross_refs":[{"db":"BMRB","id":"51817"}],"region_id":"DP04455r002","statement":[{"text":"The results show S2 > 0.7, indicating order at the J-domain and CTDs and low-order parameters (S2 < 0.7) for the GF/GM region, as expected,\nowing to the intrinsic flexibility of this region.","type":"Article"},{"text":"The mentioned GF/GM region is a disordered linker between residues 76 and 180 that connects two folded domains, an N-terminal alpha-helical J-domain and a C-terminal beta-rich domain.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-05T14:36:57.756Z"}}],"__v":0,"disorder_content":0.29829545454545453,"disprot_consensus":{"full":[{"start":76,"end":180,"type":"D"}],"Structural state":[{"start":76,"end":180,"type":"D"}],"Disorder function":[{"start":76,"end":180,"type":"F"}]}},{"acc":"O15264","sequence":"MSLIRKKGFYKQDVNKTAWELPKTYVSPTHVGSGAYGSVCSAIDKRSGEKVAIKKLSRPFQSEIFAKRAYRELLLLKHMQHENVIGLLDVFTPASSLRNFYDFYLVMPFMQTDLQKIMGMEFSEEKIQYLVYQMLKGLKYIHSAGVVHRDLKPGNLAVNEDCELKILDFGLARHADAEMTGYVVTRWYRAPEVILSWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTGVPGTEFVQKLNDKAAKSYIQSLPQTPRKDFTQLFPRASPQAADLLEKMLELDVDKRLTAAQALTHPFFEPFRDPEEETEAQQPFDDSLEHEKLTVDEWKQHIYKEIVNFSPIARKDSRRRSGMKL","creator":"xcastro","dataset":["Stress response proteins"],"date":"2025-10-22T12:34:45.774Z","disprot_id":"DP04457","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":28,"end":308}]},"genes":[{"name":{"value":"MAPK13","_id":"68f8cf662ea0defb7a2f2dbf","evidences":[]},"synonyms":[{"value":"PRKM13","_id":"68f8cf662ea0defb7a2f2dc0","evidences":[]},{"value":"SAPK4","_id":"68f8cf662ea0defb7a2f2dc1","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"68f8cf662ea0defb7a2f2dbe"}],"length":365,"name":"Mitogen-activated protein kinase 13","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":5,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":172,"end":181,"reference_id":"27369736","reference_source":"pmid","reference_html":"First comprehensive structural and biophysical analysis of MAPK13 inhibitors targeting DFG-in and DFG-out binding modes. <i> Yurtsever Z, Patel DA, Kober DL, Su A, Miller CA, Romero AG, Holtzman MJ, Brett TJ. </i> Biochim Biophys Acta, 2016","date":"2025-10-22T12:57:10.173Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"For crystallization, a slightly truncated MAPK13 construct (1–352) was designed and cloned into pET28a as a N-terminal 6-His-tagged construct using the NdeI and XhoI restriction endonuclease sites."}]}],"cross_refs":[{"db":"PDB","id":"5EKN"},{"db":"PDB","id":"5EKO"}],"region_id":"DP04457r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"4369496","statements":[{"type":"Methods","text":"Co-crystal complexes with inhibitor compounds 58 and 117 were prepared by soaking, similar to our previous work."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"104103717"}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSMSLIRKKGFYKQDVNKTAWELPKTYVSPTHVGSGAYGSVCSAIDKRSGEKVAIKKLSRPFQSEIFAKRAYRELLLLKHMQHENVIGLLDVFTPASSLRNFYDFYLVMPFMQTDLQKIMGMEFSEEKIQYLVYQMLKGLKYIHSAGVVHRDLKPGNLAVNEDCELKILDFGLARHADAEMTGYVVTRWYRAPEVILSWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTGVPGTEFVQKLNDKAAKSYIQSLPQTPRKDFTQLFPRASPQAADLLEKMLELDVDKRLTAAQALTHPFFEPFRDPEEETEAQQPFDDSLEHEKLTVDEWKQHIYKEIVNFSPI","statement":[{"text":"We had noticed during our structural analysis of the inactive (MAPK13) and dually-phosphorylated active (MAPK13/pTpY) forms of the protein [22] that a significant portion of the activation loop (residues 173–180), which is ordered in the dual-phosphorylated protein, is not visible in our high resolution electron density maps of the unphosphorylated form.","type":"Results"},{"text":"Manual inspection of unphosphorylated structures shows missing residues at 170–183 and 172–180; we annotate 172–181 as disordered (core 172–180 with a one-residue extension to meet the 10-residue minimum).","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-22T19:14:36.499Z"}},{"start":178,"end":182,"reference_id":"9374491","reference_source":"pmid","reference_html":"Characterization of the structure and function of the fourth member of p38 group mitogen-activated protein kinases, p38delta. <i> Jiang Y, Gram H, Zhao M, New L, Gu J, Feng L, Di Padova F, Ulevitch RJ, Han J. </i> J Biol Chem, 1997","date":"2025-10-23T07:27:41.601Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04457r002","statement":[{"text":"To confirm if regulation of p38δ activity occurs through the dual TGY phosphorylation site, the kinase activity of Flag-tagged wild-type p38δ and the p38δ(AF) mutant co-expressed with MKK6b or MKK3b in COS-7 cells was compared. Neither phosphorylation of ATF2 nor MBP by p38δ(AF) immunoprecipitated from COS-7 cells was observed (data not shown). Thus Thr180 and Tyr182 are the regulatory phosphorylation sites of p38δ.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr180Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Tyr182Phe","start":null,"end":null,"position":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-23T15:51:21.972Z"}},{"start":179,"end":183,"reference_id":"25849390","reference_source":"pmid","reference_html":"The crystal structure of phosphorylated MAPK13 reveals common structural features and differences in p38 MAPK family activation. <i> Yurtsever Z, Scheaffer SM, Romero AG, Holtzman MJ, Brett TJ. </i> Acta Crystallogr D Biol Crystallogr, 2015","date":"2025-10-22T19:31:02.781Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"4MYG"}],"region_id":"DP04457r003","statement":[{"text":"Here, we demonstrate that MAPK13/pTpY is produced by autophosphorylation during expression in E. coli and that the unphosphorylated and phosphorylated MAPK13 can be separated using ion-exchange chromatography (Figs. 1b and 1c), producing protein of sufficient purity for the crystallization of both forms (Figs. 1d and 1e).","type":"Results"},{"text":"The residues Thr180 and Tyr182 were found to be phosphorylated.","type":"Curator statement"}]},{"start":172,"end":181,"reference_id":"25849390","reference_source":"pmid","reference_html":"The crystal structure of phosphorylated MAPK13 reveals common structural features and differences in p38 MAPK family activation. <i> Yurtsever Z, Scheaffer SM, Romero AG, Holtzman MJ, Brett TJ. </i> Acta Crystallogr D Biol Crystallogr, 2015","date":"2025-10-22T19:37:25.482Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":180,"end":180,"position":"Specific residue"},{"term_id":"MOD:00696","term_name":"phosphorylated residue","term_namespace":"Protein modification","start":182,"end":182,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"4MYG"}],"region_id":"DP04457r004","statement":[{"text":"The largest difference between the two structures occurs in the activation loop; much of this region is notably absent from electron-density maps and is therefore likely to be disordered in the MAPK13 structure, but it is very well ordered in the MAPK13/pTpY structure (Figs. 2c and 2d).","type":"Results"},{"text":"When the residues Thr180 and Tyr182 are phosphorylated this region becomes more structured.","type":"Curator statement"}]},{"start":178,"end":182,"reference_id":"9374491","reference_source":"pmid","reference_html":"Characterization of the structure and function of the fourth member of p38 group mitogen-activated protein kinases, p38delta. <i> Jiang Y, Gram H, Zhao M, New L, Gu J, Feng L, Di Padova F, Ulevitch RJ, Han J. </i> J Biol Chem, 1997","date":"2025-10-23T07:30:45.829Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"GO:0004674","term_name":"protein serine/threonine kinase activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr180Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Tyr182Phe","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04457r005","statement":[{"text":"To confirm if regulation of p38δ activity occurs through the dual TGY phosphorylation site, the kinase activity of Flag-tagged wild-type p38δ and the p38δ(AF) mutant co-expressed with MKK6b or MKK3b in COS-7 cells was compared. Neither phosphorylation of ATF2 nor MBP by p38δ(AF) immunoprecipitated from COS-7 cells was observed (data not shown). Thus Thr180 and Tyr182 are the regulatory phosphorylation sites of p38δ.","type":"Results"}],"term_comment":"","term_def":"\"Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate.\" [GOC:bf, PMID:2956925]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-10-23T15:51:43.366Z"}}],"__v":0,"disorder_content":0.0273972602739726,"disprot_consensus":{"full":[{"start":172,"end":181,"type":"T"},{"start":182,"end":183,"type":"F"}],"Structural state":[{"start":172,"end":181,"type":"D"}],"Disorder function":[{"start":178,"end":183,"type":"F"}],"Structural transition":[{"start":172,"end":181,"type":"T"}],"Molecular function":[{"start":178,"end":182,"type":"F"}]}},{"acc":"Q5XUX0","sequence":"MAVCARLCGVGPSRGCRRRQQRRGPAETAAADSEPDTDPEEERIEASAGVGGGLCAGPSPPPPRCSLLELPPELLVEIFASLPGTDLPSLAQVCTKFRRILHTDTIWRRRCREEYGVCENLRKLEITGVSCRDVYAKLLHRYRHILGLWQPDIGPYGGLLNVVVDGLFIIGWMYLPPHDPHVDDPMRFKPLFRIHLMERKAATVECMYGHKGPHHGHIQIVKKDEFSTKCNQTDHHRMSGGRQEEFRTWLREEWGRTLEDIFHEHMQELILMKFIYTSQYDNCLTYRRIYLPPSRPDDLIKPGLFKGTYGSHGLEIVMLSFHGRRARGTKITGDPNIPAGQQTVEIDLRHRIQLPDLENQRNFNELSRIVLEVRERVRQEQQEGGHEAGEGRGRQGPRESQPSPAQPRAEAPSKGPDGTPGEDGGEPGDAVAAAEQPAQCGQGQPFVLPVGVSSRNEDYPRTCRMCFYGTGLIAGHGFTSPERTPGVFILFDEDRFGFVWLELKSFSLYSRVQATFRNADAPSPQAFDEMLKNIQSLTS","creator":"xcastro","dataset":["NDDs-related proteins"],"date":"2025-10-23T12:12:18.046Z","disprot_id":"DP04458","features":{"pfam":[{"id":"PF12014","name":"Cyclin D1 binding domain","start":286,"end":513},{"id":"PF12937","name":"F-box-like","start":68,"end":112}]},"genes":[{"name":{"value":"FBXO31","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/15520277","id":"15520277","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/15520277","_id":"68fa1ba22ea0defb7a2f2e53"},"code":"ECO:0000303","_id":"68fa1ba22ea0defb7a2f2e52"},{"source":{"id":"HGNC:16510","name":"HGNC","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:16510","_id":"68fa1ba22ea0defb7a2f2e55"},"code":"ECO:0000312","_id":"68fa1ba22ea0defb7a2f2e54"}],"_id":"68fa1ba22ea0defb7a2f2e51"},"synonyms":[{"value":"FBX14","_id":"68fa1ba22ea0defb7a2f2e56","evidences":[]},{"value":"FBX31","_id":"68fa1ba22ea0defb7a2f2e57","evidences":[]}],"olnNames":[],"orfNames":[{"value":"PP2386","_id":"68fa1ba22ea0defb7a2f2e58","evidences":[]}],"_id":"68fa1ba22ea0defb7a2f2e50"}],"length":539,"name":"F-box only protein 31","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":3,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":384,"end":442,"reference_id":"29279382","reference_source":"pmid","reference_html":"Structural basis of the phosphorylation-independent recognition of cyclin D1 by the SCF<sup>FBXO31</sup> ubiquitin ligase. <i> Li Y, Jin K, Bunker E, Zhang X, Luo X, Liu X, Hao B. </i> Proc Natl Acad Sci U S A, 2018","date":"2026-05-29T17:23:20.263Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"5VZT"}],"region_id":"DP04458r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P63208","statements":[{"type":"Results","text":"We produced the binary Skp1–FBXO31core complex by coexpressing a truncated human Skp1 protein (28) and a core fragment of human FBXO31 (residues 66–539) that lacks the N-terminal 65 residues preceding the F-box domain."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18320","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1061"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"32051"}],"statement":[{"text":"The resultant electronic map allowed unambiguous tracing of the two polypeptide chains and the positioning of most side chains, except for a 59-residue disordered region in FBXO31 (residues 384–442).","type":"Results"}],"construct_alterations":[{"term_id":"MI:0988","term_name":"STREP","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Supplementary material","text":"N-terminal StrepII-tagged human FBXO31 (NP_079011) variants and truncated Skp1 (1) were coexpressed as a dicistronic message in Escherichia coli BL21(DE3)."}]}],"sequence_construct":"MASWSHPQFEKSGRSLLELPPELLVEIFASLPGTDLPSLAQVCTKFRRILHTDTIWRRRCREEYGVCENLRKLEITGVSCRDVYAKLLHRYRHILGLWQPDIGPYGGLLNVVVDGLFIIGWMYLPPHDPHVDDPMRFKPLFRIHLMERKAATVECMYGHKGPHHGHIQIVKKDEFSTKCNQTDHHRMSGGRQEEFRTWLREEWGRTLEDIFHEHMQELILMKFIYTSQYDNCLTYRRIYLPPSRPDDLIKPGLFKGTYGSHGLEIVMLSFHGRRARGTKITGDPNIPAGQQTVEIDLRHRIQLPDLENQRNFNELSRIVLEVRERVRQEQQEGGHEAGEGRGRQGPRESQPSPAQPRAEAPSKGPDGTPGEDGGEPGDAVAAAEQPAQCGQGQPFVLPVGVSSRNEDYPRTCRMCFYGTGLIAGHGFTSPERTPGVFILFDEDRFGFVWLELKSFSLYSRVQATFRNADAPSPQAFDEMLKNIQSLTS","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-29T17:36:09.525Z"}},{"start":417,"end":421,"reference_id":"30171069","reference_source":"pmid","reference_html":"The SCF<sup>FBXO46</sup> ubiquitin ligase complex mediates degradation of the tumor suppressor FBXO31 and thereby prevents premature cellular senescence. <i> Choppara S, Ganga S, Manne R, Dutta P, Singh S, Santra MK. </i> J Biol Chem, 2018","date":"2025-10-23T13:13:06.050Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000045","term_name":"phosphorylation display site","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001247","ec_ontology":"ECO","ec_name":"point mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr419Ala","start":null,"end":null,"position":null}],"region_id":"DP04458r002","statement":[{"text":"Finally, we checked the phosphorylation status of the FBXO31 mutant following JNK inhibition. The results revealed that phosphoserine/phosphothreonine levels of ΔD8-FBXO31 sharply declined (Fig. S2, F and G). In contrast, phosphoserine levels of ΔD8-S480A-FBXO31 and phosphothreonine levels of ΔD8-T419A-FBXO31 remained unaltered following inactivation of JNK, indicating that these sites might be the putative phosphorylation of JNK (Fig. S2, F and G).","type":"Results"},{"text":"Although MEK and JNK phosphorylate FBXO31 at Thr-419 and Ser-480, MEK, JNK, and mTOR share the common phosphorylation site (Thr-419).","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-29T17:24:58.389Z"}}],"__v":0,"disorder_content":0.10946196660482375,"disprot_consensus":{"full":[{"start":384,"end":442,"type":"D"}],"Structural state":[{"start":384,"end":442,"type":"D"}],"Disorder function":[{"start":417,"end":421,"type":"F"}]}},{"acc":"Q49AH0","sequence":"MWCASPVAVVAFCAGLLVSHPVLTQGQEAGGRPGADCEVCKEFLNRFYKSLIDRGVNFSLDTIEKELISFCLDTKGKENRLCYYLGATKDAATKILSEVTRPMSVHMPAMKICEKLKKLDSQICELKYEKTLDLASVDLRKMRVAELKQILHSWGEECRACAEKTDYVNLIQELAPKYAATHPKTEL","creator":"xcastro","dataset":[],"date":"2025-10-27T09:19:47.160Z","disprot_id":"DP04459","features":{"pfam":[{"id":"PF10208","name":"ARMET, C-terminal","start":136,"end":178},{"id":"PF20145","name":"ARMET, N-terminal","start":36,"end":132}]},"genes":[{"name":{"value":"CDNF","_id":"68ff393a2ea0defb7a2f2ed4","evidences":[]},"synonyms":[{"value":"ARMETL1","_id":"68ff393a2ea0defb7a2f2ed5","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"68ff393a2ea0defb7a2f2ed3"}],"length":187,"name":"Cerebral dopamine neurotrophic factor","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":2,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":125,"end":139,"reference_id":"26149686","reference_source":"pmid","reference_html":"The Solution Structure and Dynamics of Full-length Human Cerebral Dopamine Neurotrophic Factor and Its Neuroprotective Role against α-Synuclein Oligomers. <i> Latge C, Cabral KM, de Oliveira GA, Raymundo DP, Freitas JA, Johanson L, Romão LF, Palhano FL, Herrmann T, Almeida MS, Foguel D. </i> J Biol Chem, 2015","date":"2026-05-29T17:16:31.011Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04459r001","statement":[{"text":"The 310 helix that spans residues 95–102 (green shaded box in Fig. 2A) has a higher degree of flexibility and is therefore underrepresented among the CDNF conformers (present in 8 out 20 conformers). We speculate that this is because the 310 helix is contained within the relatively flexible linker region (residues 99–113) that connects the two domains.","type":"Results"},{"text":"The region 99-113 corresponds to 125-139 in the UniProt sequence, because the authors don't consider the signal peptide (first 26 residues).","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"4BIT"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-29T17:16:41.345Z"}},{"start":125,"end":139,"reference_id":"26149686","reference_source":"pmid","reference_html":"The Solution Structure and Dynamics of Full-length Human Cerebral Dopamine Neurotrophic Factor and Its Neuroprotective Role against α-Synuclein Oligomers. <i> Latge C, Cabral KM, de Oliveira GA, Raymundo DP, Freitas JA, Johanson L, Romão LF, Palhano FL, Herrmann T, Almeida MS, Foguel D. </i> J Biol Chem, 2015","date":"2026-05-29T17:16:38.463Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04459r002","statement":[{"text":"The 310 helix that spans residues 95–102 (green shaded box in Fig. 2A) has a higher degree of flexibility and is therefore underrepresented among the CDNF conformers (present in 8 out 20 conformers). We speculate that this is because the 310 helix is contained within the relatively flexible linker region (residues 99–113) that connects the two domains.","type":"Results"},{"text":"The region 99-113 corresponds to 125-139 in the UniProt sequence, because the authors don't consider the signal peptide (first 26 residues).","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"4BIT"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-29T17:16:40.298Z"}}],"__v":0,"disorder_content":0.08021390374331551,"disprot_consensus":{"full":[{"start":125,"end":139,"type":"D"}],"Structural state":[{"start":125,"end":139,"type":"D"}],"Disorder function":[{"start":125,"end":139,"type":"F"}]}},{"acc":"Q9RUB5","sequence":"MNELPGTSDTPLLDQIHGPKDLKRLSREQLPALTEELRGEIVRVCSRGGLHLASSLGAVDIITALHYVLDSPRDRILFDVGHQAYAHKILTGRRDQMADIKKEGGISGFTKVSESEHDAITVGHASTSLANALGMALARDAQGKDFHVAAVIGDGSLTGGMALAALNTIGDMGRKMLIVLNDNEMSISENVGAMNKFMRGLQVQKWFQEGEGAGKKAVEAVSKPLADFMSRAKNSTRHFFDPASVNPFAAMGVRYVGPVDGHNVQELVWLLERLVDLDGPTILHIVTTKGKGLSYAEADPIYWHGPAKFDPATGEYVPSSAYSWSAAFGEAVTEWAKTDPRTFVVTPAMREGSGLVEFSRVHPHRYLDVGIAEEVAVTTAAGMALQGMRPVVAIYSTFLQRAYDQVLHDVAIEHLNVTFCIDRAGIVGADGATHNGVFDLSFLRSIPGVRIGLPKDAAELRGMLKYAQTHDGPFAIRYPRGNTAQVPAGTWPDLKWGEWERLKGGDDVVILAGGKALDYALKAAEDLPGVGVVNARFVKPLDEEMLREVGGRARALITVEDNTVVGGFGGAVLEALNSMNLHPTVRVLGIPDEFQEHATAESVHARAGIDAPAIRTVLAELGVDVPIEV","creator":"xcastro","dataset":[],"date":"2025-10-27T14:52:19.180Z","disprot_id":"DP04460","features":{"pfam":[{"id":"PF02779","name":"Transketolase, pyrimidine binding domain","start":322,"end":483},{"id":"PF02780","name":"Transketolase, C-terminal domain","start":497,"end":614},{"id":"PF13292","name":"1-deoxy-D-xylulose-5-phosphate synthase","start":13,"end":287}]},"genes":[{"name":{"value":"dxs","_id":"68ff87242ea0defb7a2f2eef","evidences":[]},"synonyms":[],"olnNames":[{"value":"DR_1475","_id":"68ff87242ea0defb7a2f2ef0","evidences":[]}],"orfNames":[],"_id":"68ff87242ea0defb7a2f2eee"}],"length":629,"name":"1-deoxy-D-xylulose-5-phosphate synthase","ncbi_taxon_id":243230,"organism":"Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)","regions_counter":8,"released":"2026_06","taxonomy":["Bacteria","Thermotogati","Deinococcota","Deinococci","Deinococcales","Deinococcaceae","Deinococcus"],"regions":[{"start":199,"end":243,"reference_id":"17135236","reference_source":"pmid","reference_html":"Crystal structure of 1-deoxy-D-xylulose 5-phosphate synthase, a crucial enzyme for isoprenoids biosynthesis. <i> Xiang S, Usunow G, Lange G, Busch M, Tong L. </i> J Biol Chem, 2007","date":"2026-05-29T16:54:31.374Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"2O1X"}],"region_id":"DP04460r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1132","statements":[{"type":"Methods","text":"Prior to crystallization, the DXS proteins were supplemented with 1 mm thiamine pyrophosphate and 5 mm MgCl2."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"}],"statement":[{"text":"In the structure of D. radiodurans DXS, residues 199–242 in this connection are also disordered (Fig. 3A).","type":"Results"},{"text":"Residues 199–243 in domain I of D. radiodurans DXS are not observed in the structure, very likely because of disorder.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ala130Thr","start":null,"end":null,"position":null}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-29T16:54:35.744Z"}},{"start":292,"end":306,"reference_id":"31239351","reference_source":"pmid","reference_html":"X-ray crystallography-based structural elucidation of enzyme-bound intermediates along the 1-deoxy-d-xylulose 5-phosphate synthase reaction coordinate. <i> Chen PY, DeColli AA, Freel Meyers CL, Drennan CL. </i> J Biol Chem, 2019","date":"2025-10-29T08:46:34.620Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The purified dxs-pET28b(+) plasmid was fully sequenced by GENEWIZ to confirm the presence of WT D. radiodurans dxs and N-His6 tag."}]}],"cross_refs":[{"db":"PDB","id":"6OUW"}],"region_id":"DP04460r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"4369479"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"923"}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSHMMNELPGTSDTPLLDQIHGPKDLKRLSREQLPALTEELRGEIVRVCSRGGLHLASSLGAVDIITALHYVLDSPRDRILFDVGHQAYAHKILTGRRDQMADIKKEGGISGFTKVSESEHDAITVGHASTSLANALGMALARDAQGKDFHVAAVIGDGSLTGGMALAALNTIGDMGRKMLIVLNDNEMSISENVGAMNKFMRGLQVQKWFQEGEGAGKKAVEAVSKPLADFMSRAKNSTRHFFDPASVNPFAAMGVRYVGPVDGHNVQELVWLLERLVDLDGPTILHIVTTKGKGLSYAEADPIYWHGPAKFDPATGEYVPSSAYSWSAAFGEAVTEWAKTDPRTFVVTPAMREGSGLVEFSRVHPHRYLDVGIAEEVAVTTAAGMALQGMRPVVAIYSTFLQRAYDQVLHDVAIEHLNVTFCIDRAGIVGADGATHNGVFDLSFLRSIPGVRIGLPKDAAELRGMLKYAQTHDGPFAIRYPRGNTAQVPAGTWPDLKWGEWERLKGGDDVVILAGGKALDYALKAAEDLPGVGVVNARFVKPLDEEMLREVGGRARALITVEDNTVVGGFGGAVLEALNSMNLHPTVRVLGIPDEFQEHATAESVHARAGIDAPAIRTVLAELGVDVPIEV","statement":[{"text":"Residues 186–208, 217–224, 244–246, and 292–306 are not visible in this structure, although they were visible in the structure of PLThDP-bound DrDXPS (Table S3). SDS-PAGE analysis of reproduced protein crystals shows no sign of proteolysis (Fig. S11), indicating that the absent residues were disordered instead of proteolyzed in situ.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-29T16:35:07.054Z"}},{"start":292,"end":306,"reference_id":"31239351","reference_source":"pmid","reference_html":"X-ray crystallography-based structural elucidation of enzyme-bound intermediates along the 1-deoxy-d-xylulose 5-phosphate synthase reaction coordinate. <i> Chen PY, DeColli AA, Freel Meyers CL, Drennan CL. </i> J Biol Chem, 2019","date":"2025-10-29T08:49:29.420Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The purified dxs-pET28b(+) plasmid was fully sequenced by GENEWIZ to confirm the presence of WT D. radiodurans dxs and N-His6 tag."}]}],"cross_refs":[{"db":"PDB","id":"6OUV"}],"region_id":"DP04460r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"6518182"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"923"}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSHMMNELPGTSDTPLLDQIHGPKDLKRLSREQLPALTEELRGEIVRVCSRGGLHLASSLGAVDIITALHYVLDSPRDRILFDVGHQAYAHKILTGRRDQMADIKKEGGISGFTKVSESEHDAITVGHASTSLANALGMALARDAQGKDFHVAAVIGDGSLTGGMALAALNTIGDMGRKMLIVLNDNEMSISENVGAMNKFMRGLQVQKWFQEGEGAGKKAVEAVSKPLADFMSRAKNSTRHFFDPASVNPFAAMGVRYVGPVDGHNVQELVWLLERLVDLDGPTILHIVTTKGKGLSYAEADPIYWHGPAKFDPATGEYVPSSAYSWSAAFGEAVTEWAKTDPRTFVVTPAMREGSGLVEFSRVHPHRYLDVGIAEEVAVTTAAGMALQGMRPVVAIYSTFLQRAYDQVLHDVAIEHLNVTFCIDRAGIVGADGATHNGVFDLSFLRSIPGVRIGLPKDAAELRGMLKYAQTHDGPFAIRYPRGNTAQVPAGTWPDLKWGEWERLKGGDDVVILAGGKALDYALKAAEDLPGVGVVNARFVKPLDEEMLREVGGRARALITVEDNTVVGGFGGAVLEALNSMNLHPTVRVLGIPDEFQEHATAESVHARAGIDAPAIRTVLAELGVDVPIEV","statement":[{"text":"Residues 186–208, 217–224, 244–246, and 292–306 are not visible in this structure, although they were visible in the structure of PLThDP-bound DrDXPS (Table S3).","type":"Results"},{"text":"Based on the shape of the β-hairpin and the conformational changes observed, we name this region (residues 307–319), the spoon motif, and name the preceding region (residues 292–306), the fork motif.","type":"Results"},{"text":"In PLThDP-bound DXPS, both the spoon and fork motifs are fully ordered (Fig. 5A).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-29T16:34:55.968Z"}},{"start":292,"end":306,"reference_id":"31239351","reference_source":"pmid","reference_html":"X-ray crystallography-based structural elucidation of enzyme-bound intermediates along the 1-deoxy-d-xylulose 5-phosphate synthase reaction coordinate. <i> Chen PY, DeColli AA, Freel Meyers CL, Drennan CL. </i> J Biol Chem, 2019","date":"2025-10-29T08:54:39.483Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The purified dxs-pET28b(+) plasmid was fully sequenced by GENEWIZ to confirm the presence of WT D. radiodurans dxs and N-His6 tag."}]}],"cross_refs":[{"db":"PDB","id":"6OUW"},{"db":"PDB","id":"6OUV"}],"region_id":"DP04460r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"4369479"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"923"}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSHMMNELPGTSDTPLLDQIHGPKDLKRLSREQLPALTEELRGEIVRVCSRGGLHLASSLGAVDIITALHYVLDSPRDRILFDVGHQAYAHKILTGRRDQMADIKKEGGISGFTKVSESEHDAITVGHASTSLANALGMALARDAQGKDFHVAAVIGDGSLTGGMALAALNTIGDMGRKMLIVLNDNEMSISENVGAMNKFMRGLQVQKWFQEGEGAGKKAVEAVSKPLADFMSRAKNSTRHFFDPASVNPFAAMGVRYVGPVDGHNVQELVWLLERLVDLDGPTILHIVTTKGKGLSYAEADPIYWHGPAKFDPATGEYVPSSAYSWSAAFGEAVTEWAKTDPRTFVVTPAMREGSGLVEFSRVHPHRYLDVGIAEEVAVTTAAGMALQGMRPVVAIYSTFLQRAYDQVLHDVAIEHLNVTFCIDRAGIVGADGATHNGVFDLSFLRSIPGVRIGLPKDAAELRGMLKYAQTHDGPFAIRYPRGNTAQVPAGTWPDLKWGEWERLKGGDDVVILAGGKALDYALKAAEDLPGVGVVNARFVKPLDEEMLREVGGRARALITVEDNTVVGGFGGAVLEALNSMNLHPTVRVLGIPDEFQEHATAESVHARAGIDAPAIRTVLAELGVDVPIEV","statement":[{"text":"This movement of the spoon motif appears to “tug” on the fork motif, causing it to become disordered, such that residues 292–306 are no longer visible in the enamine structure (Fig. 5B, dashed line). Alternatively, an order-to-disorder transition of the fork motif might initiate movement of the spoon motif. Regardless, the movements of these two motifs appear to be coupled.","type":"Results"}],"states_connection":[{"source":"DP04460r003","target":"DP04460r002"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-29T16:36:09.417Z"}},{"start":186,"end":246,"reference_id":"31239351","reference_source":"pmid","reference_html":"X-ray crystallography-based structural elucidation of enzyme-bound intermediates along the 1-deoxy-d-xylulose 5-phosphate synthase reaction coordinate. <i> Chen PY, DeColli AA, Freel Meyers CL, Drennan CL. </i> J Biol Chem, 2019","date":"2025-10-29T09:29:04.903Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The purified dxs-pET28b(+) plasmid was fully sequenced by GENEWIZ to confirm the presence of WT D. radiodurans dxs and N-His6 tag."}]}],"cross_refs":[{"db":"PDB","id":"6OUW"}],"region_id":"DP04460r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"4369479"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"923"}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSHMMNELPGTSDTPLLDQIHGPKDLKRLSREQLPALTEELRGEIVRVCSRGGLHLASSLGAVDIITALHYVLDSPRDRILFDVGHQAYAHKILTGRRDQMADIKKEGGISGFTKVSESEHDAITVGHASTSLANALGMALARDAQGKDFHVAAVIGDGSLTGGMALAALNTIGDMGRKMLIVLNDNEMSISENVGAMNKFMRGLQVQKWFQEGEGAGKKAVEAVSKPLADFMSRAKNSTRHFFDPASVNPFAAMGVRYVGPVDGHNVQELVWLLERLVDLDGPTILHIVTTKGKGLSYAEADPIYWHGPAKFDPATGEYVPSSAYSWSAAFGEAVTEWAKTDPRTFVVTPAMREGSGLVEFSRVHPHRYLDVGIAEEVAVTTAAGMALQGMRPVVAIYSTFLQRAYDQVLHDVAIEHLNVTFCIDRAGIVGADGATHNGVFDLSFLRSIPGVRIGLPKDAAELRGMLKYAQTHDGPFAIRYPRGNTAQVPAGTWPDLKWGEWERLKGGDDVVILAGGKALDYALKAAEDLPGVGVVNARFVKPLDEEMLREVGGRARALITVEDNTVVGGFGGAVLEALNSMNLHPTVRVLGIPDEFQEHATAESVHARAGIDAPAIRTVLAELGVDVPIEV","statement":[{"text":"Residues 186–208, 217–224, 244–246, and 292–306 are not visible in this structure, although they were visible in the structure of PLThDP-bound DrDXPS (Table S3). SDS-PAGE analysis of reproduced protein crystals shows no sign of proteolysis (Fig. S11), indicating that the absent residues were disordered instead of proteolyzed in situ.","type":"Results"},{"text":"Manual inspection of the PDB structure shows missing residues in the entire 186–246 region, consistent with disorder.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-29T16:35:00.465Z"}},{"start":209,"end":243,"reference_id":"31239351","reference_source":"pmid","reference_html":"X-ray crystallography-based structural elucidation of enzyme-bound intermediates along the 1-deoxy-d-xylulose 5-phosphate synthase reaction coordinate. <i> Chen PY, DeColli AA, Freel Meyers CL, Drennan CL. </i> J Biol Chem, 2019","date":"2025-10-29T09:36:15.550Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The purified dxs-pET28b(+) plasmid was fully sequenced by GENEWIZ to confirm the presence of WT D. radiodurans dxs and N-His6 tag."}]}],"cross_refs":[{"db":"PDB","id":"6OUV"}],"region_id":"DP04460r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"6518182"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"923"}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSHMMNELPGTSDTPLLDQIHGPKDLKRLSREQLPALTEELRGEIVRVCSRGGLHLASSLGAVDIITALHYVLDSPRDRILFDVGHQAYAHKILTGRRDQMADIKKEGGISGFTKVSESEHDAITVGHASTSLANALGMALARDAQGKDFHVAAVIGDGSLTGGMALAALNTIGDMGRKMLIVLNDNEMSISENVGAMNKFMRGLQVQKWFQEGEGAGKKAVEAVSKPLADFMSRAKNSTRHFFDPASVNPFAAMGVRYVGPVDGHNVQELVWLLERLVDLDGPTILHIVTTKGKGLSYAEADPIYWHGPAKFDPATGEYVPSSAYSWSAAFGEAVTEWAKTDPRTFVVTPAMREGSGLVEFSRVHPHRYLDVGIAEEVAVTTAAGMALQGMRPVVAIYSTFLQRAYDQVLHDVAIEHLNVTFCIDRAGIVGADGATHNGVFDLSFLRSIPGVRIGLPKDAAELRGMLKYAQTHDGPFAIRYPRGNTAQVPAGTWPDLKWGEWERLKGGDDVVILAGGKALDYALKAAEDLPGVGVVNARFVKPLDEEMLREVGGRARALITVEDNTVVGGFGGAVLEALNSMNLHPTVRVLGIPDEFQEHATAESVHARAGIDAPAIRTVLAELGVDVPIEV","statement":[{"text":"Residues 186–208, 217–224, 244–246, and 292–306 are not visible in this structure, although they were visible in the structure of PLThDP-bound DrDXPS (Table S3). SDS-PAGE analysis of reproduced protein crystals shows no sign of proteolysis (Fig. S11), indicating that the absent residues were disordered instead of proteolyzed in situ.","type":"Results"},{"text":"Manual inspection of the PDB structure shows missing residues in chain A at 209–216 and 225–243. Because 217–224 is too short to be considered ordered, and chain B lacks residues 201–243, we consider 209–243 disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-29T16:52:20.902Z"}},{"start":302,"end":306,"reference_id":"31239351","reference_source":"pmid","reference_html":"X-ray crystallography-based structural elucidation of enzyme-bound intermediates along the 1-deoxy-d-xylulose 5-phosphate synthase reaction coordinate. <i> Chen PY, DeColli AA, Freel Meyers CL, Drennan CL. </i> J Biol Chem, 2019","date":"2025-10-29T10:11:48.520Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"GO:0043177","term_name":"organic acid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The purified dxs-pET28b(+) plasmid was fully sequenced by GENEWIZ to confirm the presence of WT D. radiodurans dxs and N-His6 tag."}]}],"cross_refs":[{"db":"PDB","id":"6OUV"}],"ec_go":"EXP","region_id":"DP04460r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"6518182"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"923"}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSHMMNELPGTSDTPLLDQIHGPKDLKRLSREQLPALTEELRGEIVRVCSRGGLHLASSLGAVDIITALHYVLDSPRDRILFDVGHQAYAHKILTGRRDQMADIKKEGGISGFTKVSESEHDAITVGHASTSLANALGMALARDAQGKDFHVAAVIGDGSLTGGMALAALNTIGDMGRKMLIVLNDNEMSISENVGAMNKFMRGLQVQKWFQEGEGAGKKAVEAVSKPLADFMSRAKNSTRHFFDPASVNPFAAMGVRYVGPVDGHNVQELVWLLERLVDLDGPTILHIVTTKGKGLSYAEADPIYWHGPAKFDPATGEYVPSSAYSWSAAFGEAVTEWAKTDPRTFVVTPAMREGSGLVEFSRVHPHRYLDVGIAEEVAVTTAAGMALQGMRPVVAIYSTFLQRAYDQVLHDVAIEHLNVTFCIDRAGIVGADGATHNGVFDLSFLRSIPGVRIGLPKDAAELRGMLKYAQTHDGPFAIRYPRGNTAQVPAGTWPDLKWGEWERLKGGDDVVILAGGKALDYALKAAEDLPGVGVVNARFVKPLDEEMLREVGGRARALITVEDNTVVGGFGGAVLEALNSMNLHPTVRVLGIPDEFQEHATAESVHARAGIDAPAIRTVLAELGVDVPIEV","statement":[{"text":"In the PLThDP-bound structure, the fork motif is positioned to contribute His-304 to the active site, and the spoon motif is filling in much of the active-site cleft (Figs. 5A, 6A, and S12A).","type":"Results"},{"text":"His-51 and His-304 form hydrogen bonds with the phosphonate, but at 5.7 Å, Tyr-395 is too far away to hydrogen bond.","type":"Figure"}],"term_comment":"","term_def":"\"Binding to an organic acid, any acidic compound containing carbon in covalent linkage.\" [GOC:jl, ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-29T16:44:18.197Z"}},{"start":186,"end":208,"reference_id":"31239351","reference_source":"pmid","reference_html":"X-ray crystallography-based structural elucidation of enzyme-bound intermediates along the 1-deoxy-d-xylulose 5-phosphate synthase reaction coordinate. <i> Chen PY, DeColli AA, Freel Meyers CL, Drennan CL. </i> J Biol Chem, 2019","date":"2026-05-29T16:50:57.333Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"cross_refs":[{"db":"PDB","id":"6OUW"},{"db":"PDB","id":"6OUV"}],"region_id":"DP04460r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"4369479"}],"statement":[{"text":"revious work showed that when EcDXPS is incubated with MAP, a pyruvate mimic, the HDX rates of three regions near the active site (residues 44–58, 185–201, and 283–303 in DrDXPS) decreased (Fig. 7A).","type":"Discussion"},{"text":"In the PLThDP-bound structure reported here, all three of these previously identified regions are buried by the fork and the spoon motifs (Fig. 7B), explaining the reduced HDX rates observed.","type":"Discussion"},{"text":"In this apparent open conformation, the solvent-accessible surface areas of residues 44–58, 185–201, and 283–291 are increased by 110–220 Å2 in each segment.","type":"Discussion"},{"text":"Residues 186–208 are not visible in the enamine-bound DrDXPS structure (PDB 6OUW), although they were visible in the PLThDP-bound structure (PDB 6OUV), indicating that this region becomes disordered upon transition to the open conformation.","type":"Curator statement"}]}],"__v":0,"disorder_content":0.12082670906200318,"disprot_consensus":{"full":[{"start":186,"end":208,"type":"T"},{"start":209,"end":246,"type":"D"},{"start":292,"end":306,"type":"T"}],"Structural state":[{"start":186,"end":246,"type":"D"},{"start":292,"end":306,"type":"D"}],"Structural transition":[{"start":186,"end":208,"type":"T"},{"start":292,"end":306,"type":"T"}],"Molecular function":[{"start":302,"end":306,"type":"F"}]}},{"acc":"P00748","sequence":"MRALLLLGFLLVSLESTLSIPPWEAPKEHKYKAEEHTVVLTVTGEPCHFPFQYHRQLYHKCTHKGRPGPQPWCATTPNFDQDQRWGYCLEPKKVKDHCSKHSPCQKGGTCVNMPSGPHCLCPQHLTGNHCQKEKCFEPQLLRFFHKNEIWYRTEQAAVARCQCKGPDAHCQRLASQACRTNPCLHGGRCLEVEGHRLCHCPVGYTGAFCDVDTKASCYDGRGLSYRGLARTTLSGAPCQPWASEATYRNVTAEQARNWGLGGHAFCRNPDNDIRPWCFVLNRDRLSWEYCDLAQCQTPTQAAPPTPVSPRLHVPLMPAQPAPPKPQPTTRTPPQSQTPGALPAKREQPPSLTRNGPLSCGQRLRKSLSSMTRVVGGLVALRGAHPYIAALYWGHSFCAGSLIAPCWVLTAAHCLQDRPAPEDLTVVLGQERRNHSCEPCQTLAVRSYRLHEAFSPVSYQHDLALLRLQEDADGSCALLSPYVQPVCLPSGAARPSETTLCQVAGWGHQFEGAEEYASFLQEAQVPFLSLERCSAPDVHGSSILPGMLCAGFLEGGTDACQGDSGGPLVCEDQAAERRLTLQGIISWGSGCGDRNKPGVYTDVAYYLAWIREHTVS","creator":"viglesias","dataset":["Extracellular matrix proteins"],"date":"2025-10-28T11:50:59.301Z","disprot_id":"DP04461","features":{"pfam":[{"id":"PF00008","name":"EGF-like domain","start":98,"end":129},{"id":"PF00008","name":"EGF-like domain","start":178,"end":207},{"id":"PF00039","name":"Fibronectin type I domain","start":135,"end":170},{"id":"PF00040","name":"Fibronectin type II domain","start":47,"end":88},{"id":"PF00051","name":"Kringle domain","start":217,"end":295},{"id":"PF00089","name":"Trypsin","start":373,"end":609}]},"genes":[{"name":{"value":"F12","_id":"6900ae272ea0defb7a2f2f27","evidences":[]},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"6900ae272ea0defb7a2f2f26"}],"length":615,"name":"Coagulation factor XII","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":6,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":20,"end":35,"reference_id":"40576968","reference_source":"pmid","reference_html":"Crystal structure of coagulation factor XII N-terminal domains 1-5. <i> Saleem M, Li C, Kaira BG, Brown AK, Pathak M, Najmudin S, Cowieson N, Dreveny I, Wilson C, Shamanaev A, Gailani D, Smith SA, Morrissey JH, Philippou H, Emsley J. </i> Acta Crystallogr D Struct Biol, 2025","date":"2026-03-30T16:23:01.767Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"8OS5"}],"region_id":"DP04461r004","statement":[{"text":"The final FXIIHC5 electron density is continuous for the main chain, spanning residues 18–278, in two molecules, while the FnII domain is absent in a third molecule (residues 77–278; Supplementary Fig. S4).","type":"Methods"},{"text":"His17 is not present in the FXIIHC5 structure and residues 1–17 are not visible in the FXIIHC5 electron density (shown as a dotted line in Fig. 7 ▸a), and Glu71 is in the linker region. ","type":"Results"},{"text":"Te region missing electron density corresponds to the 20-35 region of the UniProt sequence.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-31T13:55:01.449Z"}},{"start":296,"end":349,"reference_id":"35469101","reference_source":"pmid","reference_html":"Modeling and dynamical analysis of the full-length structure of factor XII with zinc. <i> Kılınç E, Can Timucin A, Selim Cinaroglu S, Timucin E, Timucin E. </i> J Mol Model, 2022","date":"2026-03-30T16:17:02.199Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008035","ec_ontology":"ECO","ec_name":"author inference based on intrinsic disorder prediction used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04461r005","statement":[{"text":"The heavy and light chains are interconnected by a proline-rich region which is a well-recognized intrinsically disordered region [57]. Not only the proline-rich domain but some of other portions of the light chain are also likely disordered regions. According to the protein disorder prediction by IUPred3 [58], in addition to the proline-rich region, other regions of the heavy chain including the residue spanning 47-to-88 and the Kringle domain were also found to be potentially disordered (Fig. S1).","type":"Results"},{"text":"Our model was more compact than the AF2 model given the extended conformation of the disordered proline-rich region.","type":"Results"},{"text":"Supplementary figure S1 shows this region is predicted to be disordered by IUPred3 as well. ","type":"Curator statement"}]},{"start":296,"end":349,"reference_id":"35469101","reference_source":"pmid","reference_html":"Modeling and dynamical analysis of the full-length structure of factor XII with zinc. <i> Kılınç E, Can Timucin A, Selim Cinaroglu S, Timucin E, Timucin E. </i> J Mol Model, 2022","date":"2026-03-30T16:17:18.121Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0008035","ec_ontology":"ECO","ec_name":"author inference based on intrinsic disorder prediction used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04461r006","statement":[{"text":"The heavy and light chains are interconnected by a proline-rich region which is a well-recognized intrinsically disordered region [57]. Not only the proline-rich domain but some of other portions of the light chain are also likely disordered regions. According to the protein disorder prediction by IUPred3 [58], in addition to the proline-rich region, other regions of the heavy chain including the residue spanning 47-to-88 and the Kringle domain were also found to be potentially disordered (Fig. S1).","type":"Results"},{"text":"Our model was more compact than the AF2 model given the extended conformation of the disordered proline-rich region.","type":"Results"},{"text":"Supplementary figure S1 shows this region is predicted to be disordered by IUPred3 as well. ","type":"Curator statement"}]}],"__v":0,"disorder_content":0.11382113821138211,"disprot_consensus":{"full":[{"start":20,"end":35,"type":"D"},{"start":296,"end":349,"type":"D"}],"Structural state":[{"start":20,"end":35,"type":"D"},{"start":296,"end":349,"type":"D"}],"Disorder function":[{"start":296,"end":349,"type":"F"}]}},{"acc":"P77488","sequence":"MSFDIAKYPTLALVDSTQELRLLPKESLPKLCDELRRYLLDSVSRSSGHFASGLGTVELTVALHYVYNTPFDQLIWDVGHQAYPHKILTGRRDKIGTIRQKGGLHPFPWRGESEYDVLSVGHSSTSISAGIGIAVAAEKEGKNRRTVCVIGDGAITAGMAFEAMNHAGDIRPDMLVILNDNEMSISENVGALNNHLAQLLSGKLYSSLREGGKKVFSGVPPIKELLKRTEEHIKGMVVPGTLFEELGFNYIGPVDGHDVLGLITTLKNMRDLKGPQFLHIMTKKGRGYEPAEKDPITFHAVPKFDPSSGCLPKSSGGLPSYSKIFGDWLCETAAKDNKLMAITPAMREGSGMVEFSRKFPDRYFDVAIAEQHAVTFAAGLAIGGYKPIVAIYSTFLQRAYDQVLHDVAIQKLPVLFAIDRAGIVGADGQTHQGAFDLSYLRCIPEMVIMTPSDENECRQMLYTGYHYNDGPSAVRYPRGNAVGVELTPLEKLPIGKGIVKRRGEKLAILNFGTLMPEAAKVAESLNATLVDMRFVKPLDEALILEMAASHEALVTVEENAIMGGAGSGVNEVLMAHRKPVPVLNIGLPDFFIPQGTQEEMRAELGLDAAGMEAKIKAWLA","creator":"xcastro","dataset":[],"date":"2025-10-29T10:38:24.122Z","disprot_id":"DP04462","features":{"pfam":[{"id":"PF02779","name":"Transketolase, pyrimidine binding domain","start":320,"end":480},{"id":"PF02780","name":"Transketolase, C-terminal domain","start":495,"end":610},{"id":"PF13292","name":"1-deoxy-D-xylulose-5-phosphate synthase","start":13,"end":282}]},"genes":[{"name":{"value":"dxs","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/9482846","id":"9482846","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/9482846","_id":"6901eea12ea0defb7a2f2f51"},"code":"ECO:0000303","_id":"6901eea12ea0defb7a2f2f50"}],"_id":"6901eea12ea0defb7a2f2f4f"},"synonyms":[{"value":"yajP","_id":"6901eea12ea0defb7a2f2f52","evidences":[]}],"olnNames":[{"value":"b0420","_id":"6901eea12ea0defb7a2f2f53","evidences":[]},{"value":"JW0410","_id":"6901eea12ea0defb7a2f2f54","evidences":[]}],"orfNames":[],"_id":"6901eea12ea0defb7a2f2f4e"}],"length":620,"name":"1-deoxy-D-xylulose-5-phosphate synthase","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions_counter":5,"released":"2026_06","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"regions":[{"start":183,"end":238,"reference_id":"17135236","reference_source":"pmid","reference_html":"Crystal structure of 1-deoxy-D-xylulose 5-phosphate synthase, a crucial enzyme for isoprenoids biosynthesis. <i> Xiang S, Usunow G, Lange G, Busch M, Tong L. </i> J Biol Chem, 2007","date":"2026-05-22T17:16:52.521Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"region_id":"DP04462r001","statement":[{"text":"We discovered that in situ proteolysis by a fungal protease was essential for the crystallization of this protein (22, 23), and two segments of the enzyme, residues 183–238 and 292–317, had no electron density. The remaining parts of the enzyme, 1–182, 239–291, and 318–620 are consistent with the 20- and 40-kDa species observed in SDS gels of the crystals (the 239–291 segment is too small to be visible in the gels), confirming that the two missing segments were removed by the fungal protease.","type":"Results"},{"text":"In fact, this connection is one of the two segments in E. coli DXS that were removed by proteolysis during crystallization (Fig. 3B). In the structure of D. radiodurans DXS, residues 199–242 in this connection are also disordered (Fig. 3A).","type":"Results"},{"text":"The cleavage of this region suggests that it is exposed to the medium. While this evidence might only indicate the presence of flexible residues flanking the whole region, the combination with structural predictors such as AlphaFold and MobiDB allows us to consider this whole region as disordered.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","cross_refs":[{"db":"PDB","id":"2O1S"}],"sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1132"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18361","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"813"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-22T17:17:52.085Z"}}],"__v":0,"disorder_content":0.09032258064516129,"disprot_consensus":{"full":[{"start":183,"end":238,"type":"D"}],"Structural state":[{"start":183,"end":238,"type":"D"}]}},{"acc":"A0A861B9Z9","sequence":"MLEVCIIGFGFSAIPLVRELARTQTEFQIISAESGSVWDRLSESGRLDFSLVSSFQTSFYSFDLVRDYEKDYYPTAKQFYEMHERWRSVYEEKIIRDFVTKIENFKDYSLISTRSGKTYEAKHVVLATGFDRLMNTFLSNFDNHVSNKTFVFDTMGDSANLLIAKLIPNNNKIILRTNGFTALDQEVQVLGKPFTLDQLESPNFRYVSSELYDRLMMSPVYPRTVNPAVSYNQFPLIRRDFSWVDSKSSPPNGLIAIKYWPIDQYYYHFNDDLENYISKGYLLNDIAMWLHTGKVILVPSDTPINFDKKTITYAGIERSFHQYVKGDAEQPRLPTILINGETPFEYLYRDTFMGVIPQRLNNIYFLGYTRPFTGGLANITEMQSLFIHKLITQPQFHQKIHQNLSKRITAYNQHYYGAAKPRKHDHTVPFGFYTEDIARLIGIHYQPNECRSVRDLLFYYAFPNNAFKYRLKGEYAVDGVDELIQKVNDKHDHYAQVFVQALSIRNMNSDEAAEWDHSARRFSFNDMRHKEGYRAFLDTYLKAYRQVENISVDDTVVDEEWNFMVKEACQVRDKVAPNIEEKTHYSKDEDVNKGIRLILSILDSDISSLPDSNGSRGSGNLKEGDRLCKFEAQSIEFIRRLLQPKNYELLFIRESTVSPGSHRHGETA","creator":"viglesias","dataset":[],"date":"2025-10-29T16:31:38.166Z","disprot_id":"DP04464","features":{"pfam":[]},"genes":[{"name":{"value":"aetF","evidences":[{"source":{"id":"QNL15176.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/QNL15176.1","_id":"6902416a2ea0defb7a2f2f7c"},"code":"ECO:0000313","_id":"6902416a2ea0defb7a2f2f7b"}],"_id":"6902416a2ea0defb7a2f2f7a"},"synonyms":[],"olnNames":[],"orfNames":[{"value":"G7B40_000615","_id":"6902416a2ea0defb7a2f2f7d","evidences":[]}],"_id":"6902416a2ea0defb7a2f2f79"}],"length":668,"name":"AetF","ncbi_taxon_id":2712845,"organism":"Aetokthonos hydrillicola Thurmond2011","regions_counter":1,"released":"2026_06","taxonomy":["Bacteria","Bacillati","Cyanobacteriota","Cyanophyceae","Nostocales","Hapalosiphonaceae","Aetokthonos"],"regions":[{"start":611,"end":628,"reference_id":"37314407","reference_source":"pmid","reference_html":"Structural basis of regioselective tryptophan dibromination by the single-component flavin-dependent halogenase AetF. <i> Gäfe S, Niemann HH. </i> Acta Crystallogr D Struct Biol, 2023","date":"2026-03-30T15:52:48.308Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"8CJD"}],"region_id":"DP04464r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEMBL","id":"CHEMBL1232653"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEMBL","id":"CHEMBL1235226"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"46807","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":null}],"statement":[{"text":"In all solved structures the complete sequence could be built except for the N-terminal (SG)3 linker and a disordered loop (residues 608 ± 2 to 630 ± 2).","type":"Results"},{"text":"Apo structure shows this region lacks electron density, indicating it is disordered.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T15:54:10.896Z"}}],"__v":0,"disorder_content":0.02694610778443114,"disprot_consensus":{"full":[{"start":611,"end":628,"type":"D"}],"Structural state":[{"start":611,"end":628,"type":"D"}]}},{"acc":"G2QFD0","sequence":"MLLSKLSILLAKWLSVAVYAGTLVHDEQFIPDHILRVSVAQVPSACENREDVVVNGTSPGPAIHLLPGARTWIRVYNDMNDRNLSMHWHGLSQRFAPFSDGTPSATQWPIPPGHFFDYEILTEPEDAGTYFYHSHVGMQALSCTGPLIVEDCGSSPYHYDDERILLFQDHFQKSDLEMIQGLTSTQFTWTGETRGILLNGRGVSPNQAAVQGRPGEASGFFGSHRFSNFRAGDGTSNSWDGIRGDDQIEPPTDCTLPVIDVEPGKTYRLRFIGATGLSLLTMGFEDHNDLTIVQVDGSEYNAPVTVDHIQLGGGQRFDVLLRTKTAEELRCNGDKTTYFLQFETRDRPDPYRGYGVLRYNLGTPVPAAPTTPALTLPAEVNNWLEYTFQPLHPSSSLSPTAEEVTRRVILEAEQKIDPATGRLVWKLAHMTWTDMSRDKPVLVDIYERGEAAMPDYAAALTNYGWDPATKLFPAKKDEVLEIVIQNTGSHYSGASGIVETHPFHAHGQHFYDVGSGPGKYDPEANNAKLASLGYRPIKRDTTMVYRYGEGKVAPGEPAGWRAWRMKMNNPGVWMVHCHILAHMIMGMETIWVVGDAEDIVTIPLSVSQNYFTYGGSVYGNDTHAPEVYHYFDDTNKCCAAGAGDSEDSGH","creator":"viglesias","dataset":[],"date":"2025-10-29T16:49:59.104Z","disprot_id":"DP04465","features":{"pfam":[{"id":"PF00394","name":"Multicopper oxidase","start":162,"end":326},{"id":"PF07731","name":"Multicopper oxidase","start":452,"end":595},{"id":"PF07732","name":"Multicopper oxidase","start":40,"end":151}]},"genes":[{"name":{"value":"LMCO1","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/30529567","id":"30529567","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/30529567","_id":"690245b72ea0defb7a2f2f87"},"code":"ECO:0000303","_id":"690245b72ea0defb7a2f2f86"}],"_id":"690245b72ea0defb7a2f2f85"},"synonyms":[],"olnNames":[],"orfNames":[{"value":"MYCTH_2063133","_id":"690245b72ea0defb7a2f2f88","evidences":[]}],"_id":"690245b72ea0defb7a2f2f84"}],"length":650,"name":"Laccase-like multicopper oxidase 1","ncbi_taxon_id":573729,"organism":"Thermothelomyces thermophilus (strain ATCC 42464 / BCRC 31852 / DSM 1799)","regions_counter":3,"released":"2026_06","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Sordariomycetidae","Sordariales","Chaetomiaceae","Thermothelomyces"],"regions":[{"start":227,"end":242,"reference_id":"37326583","reference_source":"pmid","reference_html":"Structure-function studies of a novel laccase-like multicopper oxidase from Thermothelomyces thermophila provide insights into its biological role. <i> Kosinas C, Zerva A, Topakas E, Dimarogona M. </i> Acta Crystallogr D Struct Biol, 2023","date":"2026-03-30T15:38:21.885Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"7ZN6"}],"region_id":"DP04465r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29036","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15379","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"506227","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":null}],"statement":[{"text":" Residues 209–224 were not included in the final model due to insufficient electron density, similarly to the first ten N-terminal and the last 20 C-terminal residues. ","type":"Results"},{"text":"The region referred to by the authors as 209–224 correspond to the 227-242 in the UniProt sequence.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T15:41:04.488Z"}},{"start":621,"end":650,"reference_id":"37326583","reference_source":"pmid","reference_html":"Structure-function studies of a novel laccase-like multicopper oxidase from Thermothelomyces thermophila provide insights into its biological role. <i> Kosinas C, Zerva A, Topakas E, Dimarogona M. </i> Acta Crystallogr D Struct Biol, 2023","date":"2026-03-30T15:39:36.146Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"7ZN6"}],"region_id":"DP04465r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15379","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29036","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"506227","entry_name":null}],"statement":[{"text":"Residues 209–224 were not included in the final model due to insufficient electron density, similarly to the first ten N-terminal and the last 20 C-terminal residues. ","type":"Results"},{"text":"Furthermore, since the last 20 amino acids of TtLMCO1 were not included in the final structure due to a lack of electron density, there is no indication that the C-terminus of TtLMCO1 penetrates the T3 tunnel.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T15:41:04.212Z"}},{"start":621,"end":650,"reference_id":"37326583","reference_source":"pmid","reference_html":"Structure-function studies of a novel laccase-like multicopper oxidase from Thermothelomyces thermophila provide insights into its biological role. <i> Kosinas C, Zerva A, Topakas E, Dimarogona M. </i> Acta Crystallogr D Struct Biol, 2023","date":"2026-03-30T15:40:34.152Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"7ZN6"}],"region_id":"DP04465r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"506227","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29036","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15379","entry_name":null}],"statement":[{"text":"Residues 209–224 were not included in the final model due to insufficient electron density, similarly to the first ten N-terminal and the last 20 C-terminal residues. ","type":"Results"},{"text":"Furthermore, since the last 20 amino acids of TtLMCO1 were not included in the final structure due to a lack of electron density, there is no indication that the C-terminus of TtLMCO1 penetrates the T3 tunnel.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T15:41:07.235Z"}}],"__v":0,"disorder_content":0.07076923076923076,"disprot_consensus":{"full":[{"start":227,"end":242,"type":"D"},{"start":621,"end":650,"type":"D"}],"Structural state":[{"start":227,"end":242,"type":"D"},{"start":621,"end":650,"type":"D"}],"Disorder function":[{"start":621,"end":650,"type":"F"}]}},{"acc":"Q8IDW0","sequence":"MIFNYVFFKNFVPVVLYILLIIYINLNGMNNKNQIKTEKIYIKKLNRLSRKNSLCSSKNKIACLFDIGNDDNRNTTYGYNVNVKNDDINSLLKNNYSNKLYMDKRKNINNVISTNKISGSISNICSRNQKENEQKRNKQRCLTQCHTYNMSHEQDKLANDNNRNNKKNFNLLFINYFNLKRMKNSLLNKDNFFYCKEKKLSFLHKAYKKKNCTFQNYSLKRKSNRDSHKLFSGEFDDYTNNNALYESEKKEYITLNNNNKNNNNKNNDNKNNDNNDYNNNNSCNNLGERSNHYDNYGGDNNNPCNNNNDKYDIGKYFKQINTFINIDEYKTIYGDEIYKEIYELYVERNIPEYYERKYFSEDIKKSVLFDIDKYNDVEFEKAIKEEFINNGVYINNIDNTYYKKENILIMKKILHYFPLLKLINNPSDLKKLKKQYLPLLAHELKIFLFFIVNITGGHFSSVLSSLEIQLLLLYIFNQPYDNVIYDIGHQAYVHKILTGRKLLFLSLRNKKGISGFLNIFESIYDKFGAGHSSTSLSAIQGYYEAEWQVKNKEKYGNGDIEISDNANVTNNERIFQKGIHNDNNINNNINNNNYINPSDVVGRENTNVPNVRNDNHNVDKVHIAIIGDGGLTGGMALEALNYISFLNSKILIIYNDNGQVSLPTNAVSISGNRPIGSISDHLHYFVSNIEANAGDNKLSKNAKENNIFENLNYDYIGVVNGNNTEELFKVLNNIKENKLKRATVLHVRTKKSNDFINSKSPISILHSIKKNEIFPFDTTILNGNIHKENKIEEEKNVSSSTKYDVNNKNNKNNDNSEIIKYEDMFSKETFTDIYTNEMLKYLKKDRNIIFLSPAMLGGSGLVKISERYPNNVYDVGIAEQHSVTFAAAMAMNKKLKIQLCIYSTFLQRAYDQIIHDLNLQNIPLKVIIGRSGLVGEDGATHQGIYDLSYLGTLNNAYIISPSNQVDLKRALRFAYLDKDHSVYIRIPRMNILSDKYMKGYLNIHMKNESKNIDVNVDINDDVDKYSEEYMDDDNFIKSFIGKSRIIKMDNENNNTNEHYSSRGDTQTKKKKVCIFNMGSMLFNVINAIKEIEKEQYISHNYSFSIVDMIFLNPLDKNMIDHVIKQNKHQYLITYEDNTIGGFSTHFNNYLIENNYITKHNLYVHNIYLSNEPIEHASFKDQQEVVKMDKCSLVNRIKNYLKNNPT","creator":"xcastro","dataset":[],"date":"2025-10-30T08:18:04.808Z","disprot_id":"DP04466","features":{"pfam":[{"id":"PF02779","name":"Transketolase, pyrimidine binding domain","start":829,"end":990},{"id":"PF02780","name":"Transketolase, C-terminal domain","start":1065,"end":1190},{"id":"PF13292","name":"1-deoxy-D-xylulose-5-phosphate synthase","start":420,"end":553},{"id":"PF13292","name":"1-deoxy-D-xylulose-5-phosphate synthase","start":614,"end":749}]},"genes":[{"synonyms":[],"olnNames":[],"orfNames":[{"value":"PF3D7_1337200","_id":"69031f402ea0defb7a2f2fa2","evidences":[]}],"_id":"69031f402ea0defb7a2f2fa1"}],"length":1205,"name":"1-deoxy-D-xylulose-5-phosphate synthase","ncbi_taxon_id":36329,"organism":"Plasmodium falciparum (isolate 3D7)","regions_counter":7,"released":"2026_06","taxonomy":["Eukaryota","Sar","Alveolata","Apicomplexa","Aconoidasida","Haemosporida","Plasmodiidae","Plasmodium","Plasmodium (Laverania)"],"regions":[{"start":554,"end":617,"reference_id":"39103329","reference_source":"pmid","reference_html":"Cryo-EM structure of 1-deoxy-D-xylulose 5-phosphate synthase DXPS from Plasmodium falciparum reveals a distinct N-terminal domain. <i> Gawriljuk VO, Godoy AS, Oerlemans R, Welker LAT, Hirsch AKH, Groves MR. </i> Nat Commun, 2024","date":"2025-10-30T08:39:23.183Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"cross_refs":[{"db":"PDB","id":"8R2H"},{"db":"EMDB","id":"18842"}],"region_id":"DP04466r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1132"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSHMYDIGKYFKQINTFINIDEYKTIYGDEIYKEIYELYVERNIPEYYERKYFSEDIKKSVLFDIDKYNDVEFEKAIKEEFINNGVYINNIDNTYYKKENILIMKKILHYFPLLKLINNPSDLKKLKKQYLPLLAHELKIFLFFIVNITGGHFSSVLSSLEIQLLLLYIFNQPYDNVIYDIGHQAYVHKILTGRKLLFLSLRNKKGISGFLNIFESIYDKFGAGHSSTSLSAIQGYYEAEWQVKNKEKYGNGDIEISDNANVTNNERIFQKGIHNDNNINNNINNNNYINPSDVVGRENTNVPNVRNDNHNVDKVHIAIIGDGGLTGGMALEALNYISFLNSKILIIYNDNGQVSLPTNAVSISGNRPIGSISDHLHYFVSNIEANAGDNKLSKNAKENNIFENLNYDYIGVVNGNNTEELFKVLNNIKENKLKRATVLHVRTKKSNDFINSKSPISILHSIKKNEIFPFDTTILNGNIHKENKIEEEKNVSSSTKYDVNNKNNKNNDNSEIIKYEDMFSKETFTDIYTNEMLKYLKKDRNIIFLSPAMLGGSGLVKISERYPNNVYDVGIAEQHSVTFAAAMAMNKKLKIQLCIYSTFLQRAYDQIIHDLNLQNIPLKVIIGRSGLVGEDGATHQGIYDLSYLGTLNNAYIISPSNQVDLKRALRFAYLDKDHSVYIRIPRMNILSDKYMKGYLNIHMKNESKNIDVNVDINDDVDKYSEEYMDDDNFIKSFIGKSRIIKMDNENNNTNEHYSSRGDTQTKKKKVCIFNMGSMLFNVINAIKEIEKEQYISHNYSFSIVDMIFLNPLDKNMIDHVIKQNKHQYLITYEDNTIGGFSTHFNNYLIENNYITKHNLYVHNIYLSNEPIEHASFKDQQEVVKMDKCSLVNRIKNYLKNNPT","statement":[{"text":"The PfDXPS structure has five regions with no density visible in the cryo-EM map obtained.","type":"Results"},{"text":"The first and longest one is 68 amino acids long and located within residues 554–617 (Fig. 2a).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T15:24:53.964Z"}},{"start":684,"end":704,"reference_id":"39103329","reference_source":"pmid","reference_html":"Cryo-EM structure of 1-deoxy-D-xylulose 5-phosphate synthase DXPS from Plasmodium falciparum reveals a distinct N-terminal domain. <i> Gawriljuk VO, Godoy AS, Oerlemans R, Welker LAT, Hirsch AKH, Groves MR. </i> Nat Commun, 2024","date":"2025-10-30T08:39:49.529Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"cross_refs":[{"db":"PDB","id":"8R2H"},{"db":"EMDB","id":"18842"}],"region_id":"DP04466r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1132"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSHMYDIGKYFKQINTFINIDEYKTIYGDEIYKEIYELYVERNIPEYYERKYFSEDIKKSVLFDIDKYNDVEFEKAIKEEFINNGVYINNIDNTYYKKENILIMKKILHYFPLLKLINNPSDLKKLKKQYLPLLAHELKIFLFFIVNITGGHFSSVLSSLEIQLLLLYIFNQPYDNVIYDIGHQAYVHKILTGRKLLFLSLRNKKGISGFLNIFESIYDKFGAGHSSTSLSAIQGYYEAEWQVKNKEKYGNGDIEISDNANVTNNERIFQKGIHNDNNINNNINNNNYINPSDVVGRENTNVPNVRNDNHNVDKVHIAIIGDGGLTGGMALEALNYISFLNSKILIIYNDNGQVSLPTNAVSISGNRPIGSISDHLHYFVSNIEANAGDNKLSKNAKENNIFENLNYDYIGVVNGNNTEELFKVLNNIKENKLKRATVLHVRTKKSNDFINSKSPISILHSIKKNEIFPFDTTILNGNIHKENKIEEEKNVSSSTKYDVNNKNNKNNDNSEIIKYEDMFSKETFTDIYTNEMLKYLKKDRNIIFLSPAMLGGSGLVKISERYPNNVYDVGIAEQHSVTFAAAMAMNKKLKIQLCIYSTFLQRAYDQIIHDLNLQNIPLKVIIGRSGLVGEDGATHQGIYDLSYLGTLNNAYIISPSNQVDLKRALRFAYLDKDHSVYIRIPRMNILSDKYMKGYLNIHMKNESKNIDVNVDINDDVDKYSEEYMDDDNFIKSFIGKSRIIKMDNENNNTNEHYSSRGDTQTKKKKVCIFNMGSMLFNVINAIKEIEKEQYISHNYSFSIVDMIFLNPLDKNMIDHVIKQNKHQYLITYEDNTIGGFSTHFNNYLIENNYITKHNLYVHNIYLSNEPIEHASFKDQQEVVKMDKCSLVNRIKNYLKNNPT","statement":[{"text":"The PfDXPS structure has five regions with no density visible in the cryo-EM map obtained.","type":"Results"},{"text":"The second is located directly after the metal-binding site (684–704) and is known to be poorly conserved and highly disordered in other DXPS32.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T15:24:54.232Z"}},{"start":754,"end":819,"reference_id":"39103329","reference_source":"pmid","reference_html":"Cryo-EM structure of 1-deoxy-D-xylulose 5-phosphate synthase DXPS from Plasmodium falciparum reveals a distinct N-terminal domain. <i> Gawriljuk VO, Godoy AS, Oerlemans R, Welker LAT, Hirsch AKH, Groves MR. </i> Nat Commun, 2024","date":"2025-10-30T08:40:03.945Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"cross_refs":[{"db":"PDB","id":"8R2H"},{"db":"EMDB","id":"18842"}],"region_id":"DP04466r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1132"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSHMYDIGKYFKQINTFINIDEYKTIYGDEIYKEIYELYVERNIPEYYERKYFSEDIKKSVLFDIDKYNDVEFEKAIKEEFINNGVYINNIDNTYYKKENILIMKKILHYFPLLKLINNPSDLKKLKKQYLPLLAHELKIFLFFIVNITGGHFSSVLSSLEIQLLLLYIFNQPYDNVIYDIGHQAYVHKILTGRKLLFLSLRNKKGISGFLNIFESIYDKFGAGHSSTSLSAIQGYYEAEWQVKNKEKYGNGDIEISDNANVTNNERIFQKGIHNDNNINNNINNNNYINPSDVVGRENTNVPNVRNDNHNVDKVHIAIIGDGGLTGGMALEALNYISFLNSKILIIYNDNGQVSLPTNAVSISGNRPIGSISDHLHYFVSNIEANAGDNKLSKNAKENNIFENLNYDYIGVVNGNNTEELFKVLNNIKENKLKRATVLHVRTKKSNDFINSKSPISILHSIKKNEIFPFDTTILNGNIHKENKIEEEKNVSSSTKYDVNNKNNKNNDNSEIIKYEDMFSKETFTDIYTNEMLKYLKKDRNIIFLSPAMLGGSGLVKISERYPNNVYDVGIAEQHSVTFAAAMAMNKKLKIQLCIYSTFLQRAYDQIIHDLNLQNIPLKVIIGRSGLVGEDGATHQGIYDLSYLGTLNNAYIISPSNQVDLKRALRFAYLDKDHSVYIRIPRMNILSDKYMKGYLNIHMKNESKNIDVNVDINDDVDKYSEEYMDDDNFIKSFIGKSRIIKMDNENNNTNEHYSSRGDTQTKKKKVCIFNMGSMLFNVINAIKEIEKEQYISHNYSFSIVDMIFLNPLDKNMIDHVIKQNKHQYLITYEDNTIGGFSTHFNNYLIENNYITKHNLYVHNIYLSNEPIEHASFKDQQEVVKMDKCSLVNRIKNYLKNNPT","statement":[{"text":"The PfDXPS structure has five regions with no density visible in the cryo-EM map obtained.","type":"Results"},{"text":"The third one lies within the region that is also known as ‘spoon-fork’ motif (754–819), which is not visible in most of the available DXPS structures, due to its high flexibility during the open and closed state transitions of the enzyme38,39. However, in PfDXPS, this region has additional residues with low-complexity that might increase the flexibility and disorder of this motif.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T15:24:55.898Z"}},{"start":999,"end":1029,"reference_id":"39103329","reference_source":"pmid","reference_html":"Cryo-EM structure of 1-deoxy-D-xylulose 5-phosphate synthase DXPS from Plasmodium falciparum reveals a distinct N-terminal domain. <i> Gawriljuk VO, Godoy AS, Oerlemans R, Welker LAT, Hirsch AKH, Groves MR. </i> Nat Commun, 2024","date":"2025-10-30T08:55:02.017Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"cross_refs":[{"db":"PDB","id":"8R2H"},{"db":"EMDB","id":"18842"}],"region_id":"DP04466r004","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1132"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSHMYDIGKYFKQINTFINIDEYKTIYGDEIYKEIYELYVERNIPEYYERKYFSEDIKKSVLFDIDKYNDVEFEKAIKEEFINNGVYINNIDNTYYKKENILIMKKILHYFPLLKLINNPSDLKKLKKQYLPLLAHELKIFLFFIVNITGGHFSSVLSSLEIQLLLLYIFNQPYDNVIYDIGHQAYVHKILTGRKLLFLSLRNKKGISGFLNIFESIYDKFGAGHSSTSLSAIQGYYEAEWQVKNKEKYGNGDIEISDNANVTNNERIFQKGIHNDNNINNNINNNNYINPSDVVGRENTNVPNVRNDNHNVDKVHIAIIGDGGLTGGMALEALNYISFLNSKILIIYNDNGQVSLPTNAVSISGNRPIGSISDHLHYFVSNIEANAGDNKLSKNAKENNIFENLNYDYIGVVNGNNTEELFKVLNNIKENKLKRATVLHVRTKKSNDFINSKSPISILHSIKKNEIFPFDTTILNGNIHKENKIEEEKNVSSSTKYDVNNKNNKNNDNSEIIKYEDMFSKETFTDIYTNEMLKYLKKDRNIIFLSPAMLGGSGLVKISERYPNNVYDVGIAEQHSVTFAAAMAMNKKLKIQLCIYSTFLQRAYDQIIHDLNLQNIPLKVIIGRSGLVGEDGATHQGIYDLSYLGTLNNAYIISPSNQVDLKRALRFAYLDKDHSVYIRIPRMNILSDKYMKGYLNIHMKNESKNIDVNVDINDDVDKYSEEYMDDDNFIKSFIGKSRIIKMDNENNNTNEHYSSRGDTQTKKKKVCIFNMGSMLFNVINAIKEIEKEQYISHNYSFSIVDMIFLNPLDKNMIDHVIKQNKHQYLITYEDNTIGGFSTHFNNYLIENNYITKHNLYVHNIYLSNEPIEHASFKDQQEVVKMDKCSLVNRIKNYLKNNPT","statement":[{"text":"The PfDXPS structure has five regions with no density visible in the cryo-EM map obtained.","type":"Results"},{"text":"The last two regions are located in close proximity and are only separated by a small conserved segment of 19 residues. The first (999–1029) connects domains II and III, while the second one (1049–1066) is a connection between two β-strands in Domain III (Fig. 2a).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T15:24:57.746Z"}},{"start":1049,"end":1066,"reference_id":"39103329","reference_source":"pmid","reference_html":"Cryo-EM structure of 1-deoxy-D-xylulose 5-phosphate synthase DXPS from Plasmodium falciparum reveals a distinct N-terminal domain. <i> Gawriljuk VO, Godoy AS, Oerlemans R, Welker LAT, Hirsch AKH, Groves MR. </i> Nat Commun, 2024","date":"2025-10-30T08:40:34.981Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"cross_refs":[{"db":"PDB","id":"8R2H"},{"db":"EMDB","id":"18842"}],"region_id":"DP04466r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1132"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSHMYDIGKYFKQINTFINIDEYKTIYGDEIYKEIYELYVERNIPEYYERKYFSEDIKKSVLFDIDKYNDVEFEKAIKEEFINNGVYINNIDNTYYKKENILIMKKILHYFPLLKLINNPSDLKKLKKQYLPLLAHELKIFLFFIVNITGGHFSSVLSSLEIQLLLLYIFNQPYDNVIYDIGHQAYVHKILTGRKLLFLSLRNKKGISGFLNIFESIYDKFGAGHSSTSLSAIQGYYEAEWQVKNKEKYGNGDIEISDNANVTNNERIFQKGIHNDNNINNNINNNNYINPSDVVGRENTNVPNVRNDNHNVDKVHIAIIGDGGLTGGMALEALNYISFLNSKILIIYNDNGQVSLPTNAVSISGNRPIGSISDHLHYFVSNIEANAGDNKLSKNAKENNIFENLNYDYIGVVNGNNTEELFKVLNNIKENKLKRATVLHVRTKKSNDFINSKSPISILHSIKKNEIFPFDTTILNGNIHKENKIEEEKNVSSSTKYDVNNKNNKNNDNSEIIKYEDMFSKETFTDIYTNEMLKYLKKDRNIIFLSPAMLGGSGLVKISERYPNNVYDVGIAEQHSVTFAAAMAMNKKLKIQLCIYSTFLQRAYDQIIHDLNLQNIPLKVIIGRSGLVGEDGATHQGIYDLSYLGTLNNAYIISPSNQVDLKRALRFAYLDKDHSVYIRIPRMNILSDKYMKGYLNIHMKNESKNIDVNVDINDDVDKYSEEYMDDDNFIKSFIGKSRIIKMDNENNNTNEHYSSRGDTQTKKKKVCIFNMGSMLFNVINAIKEIEKEQYISHNYSFSIVDMIFLNPLDKNMIDHVIKQNKHQYLITYEDNTIGGFSTHFNNYLIENNYITKHNLYVHNIYLSNEPIEHASFKDQQEVVKMDKCSLVNRIKNYLKNNPT","statement":[{"text":"The PfDXPS structure has five regions with no density visible in the cryo-EM map obtained.","type":"Results"},{"text":"The last two regions are located in close proximity and are only separated by a small conserved segment of 19 residues. The first (999–1029) connects domains II and III, while the second one (1049–1066) is a connection between two β-strands in Domain III (Fig. 2a).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T15:24:59.612Z"}},{"start":999,"end":1029,"reference_id":"39103329","reference_source":"pmid","reference_html":"Cryo-EM structure of 1-deoxy-D-xylulose 5-phosphate synthase DXPS from Plasmodium falciparum reveals a distinct N-terminal domain. <i> Gawriljuk VO, Godoy AS, Oerlemans R, Welker LAT, Hirsch AKH, Groves MR. </i> Nat Commun, 2024","date":"2025-10-30T08:35:38.297Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"cross_refs":[{"db":"PDB","id":"8R2H"},{"db":"EMDB","id":"18842"}],"region_id":"DP04466r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1132"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSHMYDIGKYFKQINTFINIDEYKTIYGDEIYKEIYELYVERNIPEYYERKYFSEDIKKSVLFDIDKYNDVEFEKAIKEEFINNGVYINNIDNTYYKKENILIMKKILHYFPLLKLINNPSDLKKLKKQYLPLLAHELKIFLFFIVNITGGHFSSVLSSLEIQLLLLYIFNQPYDNVIYDIGHQAYVHKILTGRKLLFLSLRNKKGISGFLNIFESIYDKFGAGHSSTSLSAIQGYYEAEWQVKNKEKYGNGDIEISDNANVTNNERIFQKGIHNDNNINNNINNNNYINPSDVVGRENTNVPNVRNDNHNVDKVHIAIIGDGGLTGGMALEALNYISFLNSKILIIYNDNGQVSLPTNAVSISGNRPIGSISDHLHYFVSNIEANAGDNKLSKNAKENNIFENLNYDYIGVVNGNNTEELFKVLNNIKENKLKRATVLHVRTKKSNDFINSKSPISILHSIKKNEIFPFDTTILNGNIHKENKIEEEKNVSSSTKYDVNNKNNKNNDNSEIIKYEDMFSKETFTDIYTNEMLKYLKKDRNIIFLSPAMLGGSGLVKISERYPNNVYDVGIAEQHSVTFAAAMAMNKKLKIQLCIYSTFLQRAYDQIIHDLNLQNIPLKVIIGRSGLVGEDGATHQGIYDLSYLGTLNNAYIISPSNQVDLKRALRFAYLDKDHSVYIRIPRMNILSDKYMKGYLNIHMKNESKNIDVNVDINDDVDKYSEEYMDDDNFIKSFIGKSRIIKMDNENNNTNEHYSSRGDTQTKKKKVCIFNMGSMLFNVINAIKEIEKEQYISHNYSFSIVDMIFLNPLDKNMIDHVIKQNKHQYLITYEDNTIGGFSTHFNNYLIENNYITKHNLYVHNIYLSNEPIEHASFKDQQEVVKMDKCSLVNRIKNYLKNNPT","statement":[{"text":"The PfDXPS structure has five regions with no density visible in the cryo-EM map obtained.","type":"Results"},{"text":"The last two regions are located in close proximity and are only separated by a small conserved segment of 19 residues. The first (999–1029) connects domains II and III, while the second one (1049–1066) is a connection between two β-strands in Domain III (Fig. 2a).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T15:27:08.674Z"}},{"start":754,"end":819,"reference_id":"39103329","reference_source":"pmid","reference_html":"Cryo-EM structure of 1-deoxy-D-xylulose 5-phosphate synthase DXPS from Plasmodium falciparum reveals a distinct N-terminal domain. <i> Gawriljuk VO, Godoy AS, Oerlemans R, Welker LAT, Hirsch AKH, Groves MR. </i> Nat Commun, 2024","date":"2026-03-30T15:26:36.161Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"cross_refs":[{"db":"PDB","id":"8R2H"},{"db":"EMDB","id":"18842"}],"region_id":"DP04466r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"1132"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"}],"sequence_construct":"MGSSHHHHHHSSGLVPRGSHMYDIGKYFKQINTFINIDEYKTIYGDEIYKEIYELYVERNIPEYYERKYFSEDIKKSVLFDIDKYNDVEFEKAIKEEFINNGVYINNIDNTYYKKENILIMKKILHYFPLLKLINNPSDLKKLKKQYLPLLAHELKIFLFFIVNITGGHFSSVLSSLEIQLLLLYIFNQPYDNVIYDIGHQAYVHKILTGRKLLFLSLRNKKGISGFLNIFESIYDKFGAGHSSTSLSAIQGYYEAEWQVKNKEKYGNGDIEISDNANVTNNERIFQKGIHNDNNINNNINNNNYINPSDVVGRENTNVPNVRNDNHNVDKVHIAIIGDGGLTGGMALEALNYISFLNSKILIIYNDNGQVSLPTNAVSISGNRPIGSISDHLHYFVSNIEANAGDNKLSKNAKENNIFENLNYDYIGVVNGNNTEELFKVLNNIKENKLKRATVLHVRTKKSNDFINSKSPISILHSIKKNEIFPFDTTILNGNIHKENKIEEEKNVSSSTKYDVNNKNNKNNDNSEIIKYEDMFSKETFTDIYTNEMLKYLKKDRNIIFLSPAMLGGSGLVKISERYPNNVYDVGIAEQHSVTFAAAMAMNKKLKIQLCIYSTFLQRAYDQIIHDLNLQNIPLKVIIGRSGLVGEDGATHQGIYDLSYLGTLNNAYIISPSNQVDLKRALRFAYLDKDHSVYIRIPRMNILSDKYMKGYLNIHMKNESKNIDVNVDINDDVDKYSEEYMDDDNFIKSFIGKSRIIKMDNENNNTNEHYSSRGDTQTKKKKVCIFNMGSMLFNVINAIKEIEKEQYISHNYSFSIVDMIFLNPLDKNMIDHVIKQNKHQYLITYEDNTIGGFSTHFNNYLIENNYITKHNLYVHNIYLSNEPIEHASFKDQQEVVKMDKCSLVNRIKNYLKNNPT","statement":[{"text":"The PfDXPS structure has five regions with no density visible in the cryo-EM map obtained.","type":"Results"},{"text":"The third one lies within the region that is also known as ‘spoon-fork’ motif (754–819), which is not visible in most of the available DXPS structures, due to its high flexibility during the open and closed state transitions of the enzyme38,39. However, in PfDXPS, this region has additional residues with low-complexity that might increase the flexibility and disorder of this motif.","type":"Results"},{"text":"This region is connecting domains I and II.","type":"Curator statement"},{"text":"Domain I (419–753) and Domain II (820–998) together compose the ThDP binding domain and active site; whereas Domain III (1030–1205) mainly makes dimerization contacts.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T15:27:11.062Z"}}],"__v":0,"disorder_content":0.16597510373443983,"disprot_consensus":{"full":[{"start":554,"end":617,"type":"D"},{"start":684,"end":704,"type":"D"},{"start":754,"end":819,"type":"D"},{"start":999,"end":1029,"type":"D"},{"start":1049,"end":1066,"type":"D"}],"Structural state":[{"start":554,"end":617,"type":"D"},{"start":684,"end":704,"type":"D"},{"start":754,"end":819,"type":"D"},{"start":999,"end":1029,"type":"D"},{"start":1049,"end":1066,"type":"D"}],"Disorder function":[{"start":754,"end":819,"type":"F"},{"start":999,"end":1029,"type":"F"}]}},{"acc":"D3WZ86","sequence":"MKWSNKDGYPWSKIIHAEKFFDKVIQNDTRPGKWEWADVVSGLRDLDKDPRMNSERRYVAIVNEDVGLGETKGIGITPGLFCGCQLIHPGEEVTSHRHNSVALYFIVEGTGELEVEGEVYSYKPFDIMTCPAWSYHAWRATGDKDTLMYVIHDMALLAYMRALFWEEPKGSENIRHMVKGSTHTWSNTKAPEVSKTQAAKELLKQGE","creator":"viglesias","dataset":[],"date":"2025-10-30T08:26:24.880Z","disprot_id":"DP04467","features":{"pfam":[{"id":"PF07883","name":"Cupin domain","start":86,"end":151}]},"genes":[{"name":{"value":"naaB","_id":"690321312ea0defb7a2f2faa","evidences":[]},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"690321312ea0defb7a2f2fa9"}],"length":207,"name":"5-nitrosalicylic acid 1,2-dioxygenase","ncbi_taxon_id":376,"organism":"Bradyrhizobium sp","regions_counter":2,"released":"2026_06","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"],"regions":[{"start":183,"end":207,"reference_id":"37326584","reference_source":"pmid","reference_html":"Crystal structure of the monocupin ring-cleaving dioxygenase 5-nitrosalicylate 1,2-dioxygenase from Bradyrhizobium sp. <i> Eppinger E, Stolz A, Ferraroni M. </i> Acta Crystallogr D Struct Biol, 2023","date":"2026-03-30T14:42:55.319Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"8CH4"}],"region_id":"DP04467r001","statement":[{"text":"Electron density was missing for residues 180–207 of chain A, residues 182–207 of chain B and C and residues 183–207 of chain D.","type":"Methods"},{"text":"The final model includes a total of 161 water molecules, residues 1–182 of each monomer (molecular mass of about 23.6 kD; the exceptions are reported in Section 3) and one iron(II) ion. The last 25 residues of every subunit of 5NSDO were not modeled due to the poor electron density corresponding to this part of the molecule.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16552","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29034","entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T14:43:44.937Z"}},{"start":183,"end":207,"reference_id":"37326584","reference_source":"pmid","reference_html":"Crystal structure of the monocupin ring-cleaving dioxygenase 5-nitrosalicylate 1,2-dioxygenase from Bradyrhizobium sp. <i> Eppinger E, Stolz A, Ferraroni M. </i> Acta Crystallogr D Struct Biol, 2023","date":"2026-03-30T14:43:35.594Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"8CH4"}],"region_id":"DP04467r002","statement":[{"text":"Electron density was missing for residues 180–207 of chain A, residues 182–207 of chain B and C and residues 183–207 of chain D.","type":"Methods"},{"text":"The final model includes a total of 161 water molecules, residues 1–182 of each monomer (molecular mass of about 23.6 kD; the exceptions are reported in Section 3) and one iron(II) ion. The last 25 residues of every subunit of 5NSDO were not modeled due to the poor electron density corresponding to this part of the molecule.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29034","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16552","entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T14:43:45.902Z"}}],"__v":0,"disorder_content":0.12077294685990338,"disprot_consensus":{"full":[{"start":183,"end":207,"type":"D"}],"Structural state":[{"start":183,"end":207,"type":"D"}],"Disorder function":[{"start":183,"end":207,"type":"F"}]}},{"acc":"Q38854","sequence":"MASSAFAFPSYIITKGGLSTDSCKSTSLSSSRSLVTDLPSPCLKPNNNSHSNRRAKVCASLAEKGEYYSNRPPTPLLDTINYPIHMKNLSVKELKQLSDELRSDVIFNVSKTGGHLGSSLGVVELTVALHYIFNTPQDKILWDVGHQSYPHKILTGRRGKMPTMRQTNGLSGFTKRGESEHDCFGTGHSSTTISAGLGMAVGRDLKGKNNNVVAVIGDGAMTAGQAYEAMNNAGYLDSDMIVILNDNKQVSLPTATLDGPSPPVGALSSALSRLQSNPALRELREVAKGMTKQIGGPMHQLAAKVDEYARGMISGTGSSLFEELGLYYIGPVDGHNIDDLVAILKEVKSTRTTGPVLIHVVTEKGRGYPYAERADDKYHGVVKFDPATGRQFKTTNKTQSYTTYFAEALVAEAEVDKDVVAIHAAMGGGTGLNLFQRRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAIYSSFMQRAYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTFMACLPNMIVMAPSDEADLFNMVATAVAIDDRPSCFRYPRGNGIGVALPPGNKGVPIEIGKGRILKEGERVALLGYGSAVQSCLGAAVMLEERGLNVTVADARFCKPLDRALIRSLAKSHEVLITVEEGSIGGFGSHVVQFLALDGLLDGKLKWRPMVLPDRYIDHGAPADQLAEAGLMPSHIAATALNLIGAPREALF","creator":"xcastro","dataset":[],"date":"2025-10-30T09:51:23.465Z","disprot_id":"DP04470","features":{"pfam":[{"id":"PF02779","name":"Transketolase, pyrimidine binding domain","start":399,"end":560},{"id":"PF02780","name":"Transketolase, C-terminal domain","start":578,"end":701},{"id":"PF13292","name":"1-deoxy-D-xylulose-5-phosphate synthase","start":77,"end":362}]},"genes":[{"name":{"value":"DXS","_id":"6903351b2ea0defb7a2f2fd2","evidences":[]},"synonyms":[{"value":"CLA1","_id":"6903351b2ea0defb7a2f2fd3","evidences":[]},{"value":"DEF","_id":"6903351b2ea0defb7a2f2fd4","evidences":[]}],"olnNames":[{"value":"At4g15560","_id":"6903351b2ea0defb7a2f2fd5","evidences":[]}],"orfNames":[{"value":"dl3821w","_id":"6903351b2ea0defb7a2f2fd6","evidences":[]}],"_id":"6903351b2ea0defb7a2f2fd1"}],"length":717,"name":"1-deoxy-D-xylulose-5-phosphate synthase, chloroplastic","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions_counter":6,"released":"2026_06","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"regions":[{"start":269,"end":326,"reference_id":"34021140","reference_source":"pmid","reference_html":"Structural basis of substrate recognition and thermal protection by a small heat shock protein. <i> Yu C, Leung SKP, Zhang W, Lai LTF, Chan YK, Wong MC, Benlekbir S, Cui Y, Jiang L, Lau WCY. </i> Nat Commun, 2021","date":"2026-05-15T10:58:03.892Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"The coding sequences for A. thaliana Hsp21 (UniProt code P31170) (44-227aa) and A. thaliana DXPS (UniProt code Q38854) (59-717aa) without their transit peptides were PCR-amplified from cDNA and cloned into a pETDuet-1 vector to generate versions of Hsp21 and DXPS with an N-terminal hexahistidine tag and a C-terminal hexahistidine-FLAG tandem affinity tag, respectively."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"PDB","id":"7BZX"}],"region_id":"DP04470r001","sequence_construct":"MADLNWISAGHAIADVGTASLAEKGEYYSNRPPTPLLDTINYPIHMKNLSVKELKQLSDELRSDVIFNVSKTGGHLGSSLGVVELTVALHYIFNTPQDKILWDVGHQSYPHKILTGRRGKMPTMRQTNGLSGFTKRGESEHDCFGTGHSSTTISAGLGMAVGRDLKGKNNNVVAVIGDGAMTAGQAYEAMNNAGYLDSDMIVILNDNKQVSLPTATLDGPSPPVGALSSALSRLQSNPALRELREVAKGMTKQIGGPMHQLAAKVDEYARGMISGTGSSLFEELGLYYIGPVDGHNIDDLVAILKEVKSTRTTGPVLIHVVTEKGRGYPYAERADDKYHGVVKFDPATGRQFKTTNKTQSYTTYFAEALVAEAEVDKDVVAIHAAMGGGTGLNLFQRRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAIYSSFMQRAYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTFMACLPNMIVMAPSDEADLFNMVATAVAIDDRPSCFRYPRGNGIGVALPPGNKGVPIEIGKGRILKEGERVALLGYGSAVQSCLGAAVMLEERGLNVTVADARFCKPLDRALIRSLAKSHEVLITVEEGSIGGFGSHVVQFLALDGLLDGKLKWRPMVLPDRYIDHGAPADQLAEAGLMPSHIAATALNLIGAPREALFHHHHHHDYKDDDDK","statement":[{"text":"Immediately after the segment 247–274, the density corresponding to a large surface loop of 52 residues long (residues 275–326), referred to as the mobile loop hereafter, is also missing in our structure due to flexibility (Fig. 2a and Supplementary Fig. 5a).","type":"Results"},{"text":"Manual inspection of the structures revealed that residues 269–317 are not observed in any chain. Residues 318–326 are visible but lack defined secondary structure and adopt multiple conformations.","type":"Curator statement"}],"last_modified_by":"xcastro","last_modified_name":"Ximena Aixa Castro","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T15:49:10.997Z"}},{"start":288,"end":326,"reference_id":"34021140","reference_source":"pmid","reference_html":"Structural basis of substrate recognition and thermal protection by a small heat shock protein. <i> Yu C, Leung SKP, Zhang W, Lai LTF, Chan YK, Wong MC, Benlekbir S, Cui Y, Jiang L, Lau WCY. </i> Nat Commun, 2021","date":"2026-05-15T10:57:44.171Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal","statements":[{"type":"Methods","text":"The coding sequences for A. thaliana Hsp21 (UniProt code P31170) (44-227aa) and A. thaliana DXPS (UniProt code Q38854) (59-717aa) without their transit peptides were PCR-amplified from cDNA and cloned into a pETDuet-1 vector to generate versions of Hsp21 and DXPS with an N-terminal hexahistidine tag and a C-terminal hexahistidine-FLAG tandem affinity tag, respectively."}]},{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"PDB","id":"7BZX"}],"region_id":"DP04470r005","sequence_construct":"MADLNWISAGHAIADVGTASLAEKGEYYSNRPPTPLLDTINYPIHMKNLSVKELKQLSDELRSDVIFNVSKTGGHLGSSLGVVELTVALHYIFNTPQDKILWDVGHQSYPHKILTGRRGKMPTMRQTNGLSGFTKRGESEHDCFGTGHSSTTISAGLGMAVGRDLKGKNNNVVAVIGDGAMTAGQAYEAMNNAGYLDSDMIVILNDNKQVSLPTATLDGPSPPVGALSSALSRLQSNPALRELREVAKGMTKQIGGPMHQLAAKVDEYARGMISGTGSSLFEELGLYYIGPVDGHNIDDLVAILKEVKSTRTTGPVLIHVVTEKGRGYPYAERADDKYHGVVKFDPATGRQFKTTNKTQSYTTYFAEALVAEAEVDKDVVAIHAAMGGGTGLNLFQRRFPTRCFDVGIAEQHAVTFAAGLACEGLKPFCAIYSSFMQRAYDQVVHDVDLQKLPVRFAMDRAGLVGADGPTHCGAFDVTFMACLPNMIVMAPSDEADLFNMVATAVAIDDRPSCFRYPRGNGIGVALPPGNKGVPIEIGKGRILKEGERVALLGYGSAVQSCLGAAVMLEERGLNVTVADARFCKPLDRALIRSLAKSHEVLITVEEGSIGGFGSHVVQFLALDGLLDGKLKWRPMVLPDRYIDHGAPADQLAEAGLMPSHIAATALNLIGAPREALFHHHHHHDYKDDDDK","statement":[{"text":"Opening of the active site has been postulated to occur along with the displacement of the linker region (spanning residues 288–328 between domains I and II) from the active site.","type":"Results"}],"last_modified_by":"xcastro","last_modified_name":"Ximena Aixa Castro","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T15:49:27.108Z"}},{"start":318,"end":322,"reference_id":"34021140","reference_source":"pmid","reference_html":"Structural basis of substrate recognition and thermal protection by a small heat shock protein. <i> Yu C, Leung SKP, Zhang W, Lai LTF, Chan YK, Wong MC, Benlekbir S, Cui Y, Jiang L, Lau WCY. </i> Nat Commun, 2021","date":"2026-03-17T17:39:51.970Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0051087","term_name":"chaperone binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"},{"term_id":"MI:0518","term_name":"flag","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"PDB","id":"7BZY"}],"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"P31170","operator":null,"partner_start":120,"partner_end":227}],"region_id":"DP04470r006","statement":[{"text":"The final interface is defined by the interaction between the hydrophobic groove of the ACD of Hsp21 and residues 318–322 within the mobile loops of the DXPS. This segment spanning residues 318–322 in the mobile loop are disordered in the native DXPS but becomes ordered upon Hsp21 binding.","type":"Results"},{"text":"In the Hsp21-DXPS structure, residues in the segment 318–322 of DXPS bind to the hydrophobic groove on the opposite side of this β-sandwich (Fig. 2b), despite utilizing a similar binding mode.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.\" [PMID:10585443]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"}],"__v":0,"disorder_content":0.08089260808926081,"disprot_consensus":{"full":[{"start":269,"end":326,"type":"D"}],"Structural state":[{"start":269,"end":326,"type":"D"}],"Disorder function":[{"start":288,"end":326,"type":"F"}],"Molecular function":[{"start":318,"end":322,"type":"F"}]}},{"acc":"E9RIY6","sequence":"MLSKVKKVPSPYVGNLLNKWHDYIMQEKVHESIEKRTEIKQLLSQAEDNKDLVDYFILLDHRHSLCFDQEASMGDVVNMLSKGSHDLLINFYFELFAGDYEFFKKNYVKAISFYEKAEQKLSSIPNIEETKFAEFHYKIGVAYYEIDQHLVSVNKVTKARDIYKKSDMWNLEAIQCSLVVGINLYDMGRLDDADAYFRDALTEALDHGYDKPITKIYHNLGLVHWQKGSLELALHYFREAYSHEWLRDSPKGQQTVYMLSRVLYTMGQNEEAYHWYELGIEMARKFDDHEYKAKHDILYHLYEQPSIDEVKQSLAFLEERNLWPDVSKIAKGISELYEKKGDLVTSHEFLKRAFYAKEQIQRITEALG","creator":"viglesias","dataset":[],"date":"2025-10-30T10:30:55.036Z","disprot_id":"DP04472","features":{"pfam":[{"id":"PF13181","name":"Tetratricopeptide repeat","start":257,"end":285},{"id":"PF13424","name":"Tetratricopeptide repeat","start":180,"end":241},{"id":"PF18801","name":"response regulator aspartate phosphatase H, N terminal","start":8,"end":66}]},"genes":[{"name":{"value":"rapA","evidences":[{"source":{"id":"BAJ76901.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/BAJ76901.1","_id":"69033e622ea0defb7a2f2fea"},"code":"ECO:0000313","_id":"69033e622ea0defb7a2f2fe9"}],"_id":"69033e622ea0defb7a2f2fe8"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"69033e622ea0defb7a2f2fe7"}],"length":368,"name":"Response regulator aspartate phosphatase","ncbi_taxon_id":86029,"organism":"Bacillus subtilis subsp. natto","regions_counter":2,"released":"2026_06","taxonomy":["Bacteria","Bacillati","Bacillota","Bacilli","Bacillales","Bacillaceae","Bacillus"],"regions":[{"start":68,"end":79,"reference_id":"32658272","reference_source":"pmid","reference_html":"Inactivation of the dimeric RappLS20 anti-repressor of the conjugation operon is mediated by peptide-induced tetramerization. <i> Crespo I, Bernardo N, Miguel-Arribas A, Singh PK, Luque-Ortega JR, Alfonso C, Malfois M, Meijer WJJ, Boer DR. </i> Nucleic Acids Res, 2020","date":"2026-03-30T14:27:38.518Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"6T3H"}],"region_id":"DP04472r001","statement":[{"text":"The loop between helices H3 and H4, indicated in red in Figure 1B, therefore marks the boundary between the NTD and the C-terminal TPR domain. This loop is the longest loop in the structure, consisting of 13 residues, and shows up poorly in the electron density maps, indicating a high degree of flexibility.","type":"Results"},{"text":"Figure 1A defines the end of helix H3 at residue 67 and helix H4 starting at residue 80.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T14:28:32.408Z"}},{"start":68,"end":79,"reference_id":"32658272","reference_source":"pmid","reference_html":"Inactivation of the dimeric RappLS20 anti-repressor of the conjugation operon is mediated by peptide-induced tetramerization. <i> Crespo I, Bernardo N, Miguel-Arribas A, Singh PK, Luque-Ortega JR, Alfonso C, Malfois M, Meijer WJJ, Boer DR. </i> Nucleic Acids Res, 2020","date":"2026-03-30T14:28:11.445Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"6T3H"}],"region_id":"DP04472r002","statement":[{"text":"The loop between helices H3 and H4, indicated in red in Figure 1B, therefore marks the boundary between the NTD and the C-terminal TPR domain. This loop is the longest loop in the structure, consisting of 13 residues, and shows up poorly in the electron density maps, indicating a high degree of flexibility.","type":"Results"},{"text":"Figure 1A defines the end of helix H3 at residue 67 and helix H4 starting at residue 80.","type":"Curator statement"},{"text":"The three helices of the NTD are approximately parallel and therefore do not form a HTH topology. Instead, their configuration resembles that of the TPR fold, but the domain is tilted with respect to the C-terminal TPR domain. The linker between helices 3 and 4 mentioned above provides the flexibility required for this change in orientation. This implies flexibility of the functionally important NTD domain, which relays peptide binding to a downstream response (6).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-30T14:28:31.316Z"}}],"__v":0,"disorder_content":0.03260869565217391,"disprot_consensus":{"full":[{"start":68,"end":79,"type":"D"}],"Structural state":[{"start":68,"end":79,"type":"D"}],"Disorder function":[{"start":68,"end":79,"type":"F"}]}},{"acc":"Q9KUY7","sequence":"MADPRTDNRNRKIPDAQVDAIKVPPHSLEAEQSVIGGLLLDNERWDTVSEHVMTQDFYSRPHRLIFDGVKSILEAGKPLDLITLSEYLEQREQLEDVGGFAYLADLAKNTPSAANINAYAEIVAERALVRNLIGVANEIADAGYDPQGRNAEDLLDLAESKVFAIAEARTSENEGPKNVDSILERTLERIELLYKTPQDGVTGVNTGFTDLNKKTAGLQGSDLIIVAARPSMGKTTFAMNLCENAAMEQDKPVLIFSLEMPAEQIMMRMLASLSRVDQTKIRTGQLDDEDWARISSTMGILMEKKNMYIDDSSGLTPTEVRSRARRIAREHGGLSLIMVDYLQLMRVPALTDNRTLEIAEISRSLKALAKELNVPVVALSQLNRSLEQRADKRPVNSDLRESGSIEQDADLIMFIYRDEVYHPDSPLKGTAEIIIGKQRNGPIGSVRLTFQGHYSRFDNYAGPAFDDE","creator":"viglesias","dataset":[],"date":"2025-10-30T10:58:33.926Z","disprot_id":"DP04473","features":{"pfam":[{"id":"PF00772","name":"DnaB-like helicase N terminal domain","start":24,"end":125},{"id":"PF03796","name":"DnaB-like helicase C terminal domain","start":203,"end":459}]},"genes":[{"synonyms":[],"olnNames":[{"value":"VC_0371","_id":"690344db2ea0defb7a2f2ff3","evidences":[]}],"orfNames":[],"_id":"690344db2ea0defb7a2f2ff2"}],"length":468,"name":"Replicative DNA helicase","ncbi_taxon_id":243277,"organism":"Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)","regions_counter":3,"released":"2026_06","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Vibrionales","Vibrionaceae","Vibrio"],"regions":[{"start":1,"end":20,"reference_id":"34107018","reference_source":"pmid","reference_html":"Study of the DnaB:DciA interplay reveals insights into the primary mode of loading of the bacterial replicative helicase. <i> Marsin S, Adam Y, Cargemel C, Andreani J, Baconnais S, Legrand P, Li de la Sierra-Gallay I, Humbert A, Aumont-Nicaise M, Velours C, Ochsenbein F, Durand D, Le Cam E, Walbott H, Possoz C, Quevillon-Cheruel S, Ferat JL. </i> Nucleic Acids Res, 2021","date":"2026-03-27T15:23:50.718Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"6T66"}],"region_id":"DP04473r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17752","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30111","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":null}],"statement":[{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":1,"end":20,"reference_id":"34107018","reference_source":"pmid","reference_html":"Study of the DnaB:DciA interplay reveals insights into the primary mode of loading of the bacterial replicative helicase. <i> Marsin S, Adam Y, Cargemel C, Andreani J, Baconnais S, Legrand P, Li de la Sierra-Gallay I, Humbert A, Aumont-Nicaise M, Velours C, Ochsenbein F, Durand D, Le Cam E, Walbott H, Possoz C, Quevillon-Cheruel S, Ferat JL. </i> Nucleic Acids Res, 2021","date":"2026-03-27T15:24:05.088Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"6T66"}],"region_id":"DP04473r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17752","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30111","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":null}],"statement":[{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"__v":0,"disorder_content":0.042735042735042736,"disprot_consensus":{"full":[{"start":1,"end":20,"type":"D"}],"Structural state":[{"start":1,"end":20,"type":"D"}],"Disorder function":[{"start":1,"end":20,"type":"F"}]}},{"acc":"Q7AL96","sequence":"MDDENDRAARAKKGSPFLNTAQAAFYIGLSQRTLEKMRLTGGGPKYRKHGRYVRYHIDELDDWSKGRPPEPGSDDDKGGSGSADEGARS","creator":"viglesias","dataset":[],"date":"2025-10-30T11:18:01.585Z","disprot_id":"DP04474","features":{"pfam":[{"id":"PF12728","name":"Helix-turn-helix domain","start":17,"end":63}]},"genes":[{"name":{"value":"msi109","evidences":[{"source":{"id":"CAD31514.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/CAD31514.1","_id":"690349692ea0defb7a2f3007"},"code":"ECO:0000313","_id":"690349692ea0defb7a2f3006"}],"_id":"690349692ea0defb7a2f3005"},"synonyms":[],"olnNames":[],"orfNames":[{"value":"A8145_28770","_id":"690349692ea0defb7a2f3008","evidences":[]},{"value":"BAE39_30655","_id":"690349692ea0defb7a2f3009","evidences":[]}],"_id":"690349692ea0defb7a2f3004"}],"length":89,"name":"Helix-turn-helix domain-containing protein","ncbi_taxon_id":381,"organism":"Rhizobium loti","regions_counter":2,"released":"2026_06","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Phyllobacteriaceae","Mesorhizobium"],"regions":[{"start":69,"end":89,"reference_id":"36189741","reference_source":"pmid","reference_html":"Crystallographic and X-ray scattering study of RdfS, a recombination directionality factor from an integrative and conjugative element. <i> Verdonk CJ, Marshall AC, Ramsay JP, Bond CS. </i> Acta Crystallogr D Struct Biol, 2022","date":"2026-03-27T14:58:44.553Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"8DGL"}],"region_id":"DP04474r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":null}],"statement":[{"text":"Additionally, RdfS has significant disorder in the C-terminal region of the protein, which is supported by the solution scattering data and the crystal structure. ","type":"Abstract"},{"text":"We note that the 21 C-terminal amino acids of the protein are completely dis­ordered, as expected from their sequence PPEPGSDDDKGGSGSADEGARS. This represents 24% of the native protein sequence.","type":"Conclusion"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-27T14:59:47.427Z"}},{"start":69,"end":89,"reference_id":"36189741","reference_source":"pmid","reference_html":"Crystallographic and X-ray scattering study of RdfS, a recombination directionality factor from an integrative and conjugative element. <i> Verdonk CJ, Marshall AC, Ramsay JP, Bond CS. </i> Acta Crystallogr D Struct Biol, 2022","date":"2026-03-27T14:59:36.750Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"8DGL"}],"region_id":"DP04474r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17996","entry_name":null}],"statement":[{"text":"Additionally, RdfS has significant disorder in the C-terminal region of the protein, which is supported by the solution scattering data and the crystal structure. ","type":"Abstract"},{"text":"We note that the 21 C-terminal amino acids of the protein are completely dis­ordered, as expected from their sequence PPEPGSDDDKGGSGSADEGARS. This represents 24% of the native protein sequence.","type":"Conclusion"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-27T14:59:46.074Z"}}],"__v":0,"disorder_content":0.23595505617977527,"disprot_consensus":{"full":[{"start":69,"end":89,"type":"D"}],"Structural state":[{"start":69,"end":89,"type":"D"}],"Disorder function":[{"start":69,"end":89,"type":"F"}]}},{"acc":"P31170","sequence":"MASTLSFAASALCSPLAPSPSVSSKSATPFSVSFPRKIPSRIRAQDQRENSIDVVQQGQQKGNQGSSVEKRPQQRLTMDVSPFGLLDPLSPMRTMRQMLDTMDRMFEDTMPVSGRNRGGSGVSEIRAPWDIKEEEHEIKMRFDMPGLSKEDVKISVEDNVLVIKGEQKKEDSDDSWSGRSVSSYGTRLQLPDNCEKDKIKAELKNGVLFITIPKTKVERKVIDVQIQ","creator":"xcastro","dataset":["Stress response proteins"],"date":"2025-10-30T11:22:00.892Z","disprot_id":"DP04475","features":{"pfam":[{"id":"PF00011","name":"Hsp20/alpha crystallin family","start":130,"end":227}]},"genes":[{"name":{"value":"HSP21","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/2038305","id":"2038305","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/2038305","_id":"69034a592ea0defb7a2f3013"},"code":"ECO:0000303","_id":"69034a592ea0defb7a2f3012"}],"_id":"69034a592ea0defb7a2f3011"},"synonyms":[{"value":"HSP25.3","_id":"69034a592ea0defb7a2f3014","evidences":[]}],"olnNames":[{"value":"At4g27670","_id":"69034a592ea0defb7a2f3015","evidences":[]}],"orfNames":[{"value":"T29A15.160","_id":"69034a592ea0defb7a2f3016","evidences":[]}],"_id":"69034a592ea0defb7a2f3010"}],"length":227,"name":"Heat shock protein 21, chloroplastic","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions_counter":6,"released":"2026_06","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"regions":[{"start":44,"end":126,"reference_id":"34021140","reference_source":"pmid","reference_html":"Structural basis of substrate recognition and thermal protection by a small heat shock protein. <i> Yu C, Leung SKP, Zhang W, Lai LTF, Chan YK, Wong MC, Benlekbir S, Cui Y, Jiang L, Lau WCY. </i> Nat Commun, 2021","date":"2025-10-30T11:42:32.870Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"cross_refs":[{"db":"PDB","id":"7BZW"}],"region_id":"DP04475r001","sequence_construct":"MGSSHHHHHHSQDPNSENLYFQSAQDQRENSIDVVQQGQQKGNQGSSVEKRPQQRLTMDVSPFGLLDPLSPMRTMRQMLDTMDRMFEDTMPVSGRNRGGSGVSEIRAPWDIKEEEHEIKMRFDMPGLSKEDVKISVEDNVLVIKGEQKKEDSDDSWSGRSVSSYGTRLQLPDNCEKDKIKAELKNGVLFITIPKTKVERKVIDVQIQ","statement":[{"text":"Only the densities for the ACD and CTR are visible (except for short stretches of NTRs, as described below), suggesting that the inherently flexible NTRs are confined to the inner cavity to some extent and contribute to the scattered densities","type":"Results"},{"text":"Residues 44–126 are missing in the Hsp21 dodecamer.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-17T17:28:51.183Z"}},{"start":44,"end":135,"reference_id":"34021140","reference_source":"pmid","reference_html":"Structural basis of substrate recognition and thermal protection by a small heat shock protein. <i> Yu C, Leung SKP, Zhang W, Lai LTF, Chan YK, Wong MC, Benlekbir S, Cui Y, Jiang L, Lau WCY. </i> Nat Commun, 2021","date":"2025-10-30T11:44:21.491Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The coding sequences for A. thaliana Hsp21 (UniProt code P31170) (44-227aa) and A. thaliana DXPS (UniProt code Q38854) (59-717aa) without their transit peptides were PCR-amplified from cDNA and cloned into a pETDuet-1 vector to generate versions of Hsp21 and DXPS with an N-terminal hexahistidine tag and a C-terminal hexahistidine-FLAG tandem affinity tag, respectively."}]}],"cross_refs":[{"db":"PDB","id":"7BZY"}],"region_id":"DP04475r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q38854"}],"sequence_construct":"MGSSHHHHHHSQDPNSENLYFQSAQDQRENSIDVVQQGQQKGNQGSSVEKRPQQRLTMDVSPFGLLDPLSPMRTMRQMLDTMDRMFEDTMPVSGRNRGGSGVSEIRAPWDIKEEEHEIKMRFDMPGLSKEDVKISVEDNVLVIKGEQKKEDSDDSWSGRSVSSYGTRLQLPDNCEKDKIKAELKNGVLFITIPKTKVERKVIDVQIQ","statement":[{"text":"Only the densities for the ACD and CTR are visible (except for short stretches of NTRs, as described below), suggesting that the inherently flexible NTRs are confined to the inner cavity to some extent and contribute to the scattered densities","type":"Results"},{"text":"The map permitted the construction of a model of the ACD with seven β strands (denoted as β2- β9, with β6 missing in our structure), in striking contrast to the six-stranded ACD structure identified in the Hsp21-DXPS complex, suggesting that the ACD partly unfolds to peel away the first β strand (β2) during its interaction with DXPS (Fig. 4).","type":"Results"},{"text":"The region 44–135 is missing in the Hsp21–DXPS complex.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-17T17:30:10.565Z"}},{"start":126,"end":135,"reference_id":"34021140","reference_source":"pmid","reference_html":"Structural basis of substrate recognition and thermal protection by a small heat shock protein. <i> Yu C, Leung SKP, Zhang W, Lai LTF, Chan YK, Wong MC, Benlekbir S, Cui Y, Jiang L, Lau WCY. </i> Nat Commun, 2021","date":"2025-10-30T11:46:26.178Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The coding sequences for A. thaliana Hsp21 (UniProt code P31170) (44-227aa) and A. thaliana DXPS (UniProt code Q38854) (59-717aa) without their transit peptides were PCR-amplified from cDNA and cloned into a pETDuet-1 vector to generate versions of Hsp21 and DXPS with an N-terminal hexahistidine tag and a C-terminal hexahistidine-FLAG tandem affinity tag, respectively."}]}],"cross_refs":[{"db":"PDB","id":"7BZY"},{"db":"PDB","id":"7BZW"}],"region_id":"DP04475r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q38854"}],"sequence_construct":"MGSSHHHHHHSQDPNSENLYFQSAQDQRENSIDVVQQGQQKGNQGSSVEKRPQQRLTMDVSPFGLLDPLSPMRTMRQMLDTMDRMFEDTMPVSGRNRGGSGVSEIRAPWDIKEEEHEIKMRFDMPGLSKEDVKISVEDNVLVIKGEQKKEDSDDSWSGRSVSSYGTRLQLPDNCEKDKIKAELKNGVLFITIPKTKVERKVIDVQIQ","statement":[{"text":"Only the densities for the ACD and CTR are visible (except for short stretches of NTRs, as described below), suggesting that the inherently flexible NTRs are confined to the inner cavity to some extent and contribute to the scattered densities","type":"Results"},{"text":"The map permitted the construction of a model of the ACD with seven β strands (denoted as β2- β9, with β6 missing in our structure), in striking contrast to the six-stranded ACD structure identified in the Hsp21-DXPS complex, suggesting that the ACD partly unfolds to peel away the first β strand (β2) during its interaction with DXPS (Fig. 4).","type":"Results"},{"text":"The region 44–135 is missing in the Hsp21–DXPS complex, while only residues 44–126 are missing in the Hsp21 dodecamer. Therefore, we can consider residues 127–135 to undergo an order-to-disorder transition upon DXPS binding.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-17T17:29:29.947Z"}},{"start":1,"end":82,"reference_id":"28325834","reference_source":"pmid","reference_html":"Structural model of dodecameric heat-shock protein Hsp21: Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity. <i> Rutsdottir G, Härmark J, Weide Y, Hebert H, Rasmussen MI, Wernersson S, Respondek M, Akke M, Højrup P, Koeck PJB, Söderberg CAG, Emanuelsson C. </i> J Biol Chem, 2017","date":"2025-10-30T13:50:02.531Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001191","ec_ontology":"ECO","ec_name":"in vitro cleavage assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04475r004","statement":[{"text":"Limited proteolysis showed that the NTR is rapidly degraded whereas Hsp21 remains dodecameric, in agreement with our previous data (44), and that all of NTR is degraded before ACD starts to be degraded (Fig. 6, A–D). This result indicates that the NTR behaves as an intrinsically disordered protein that is very prone to proteolysis and that the NTR is not primarily involved in maintaining the dodecamer.","type":"Results"},{"text":"In this study, we describe Hsp21, a chloroplast-localized sHsp, which has a long NTR (82 amino acids) with conserved methionine residues that are important for substrate binding and scavenging of reactive oxygen species (35, 44).","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-17T15:08:31.346Z"}},{"start":1,"end":82,"reference_id":"28325834","reference_source":"pmid","reference_html":"Structural model of dodecameric heat-shock protein Hsp21: Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity. <i> Rutsdottir G, Härmark J, Weide Y, Hebert H, Rasmussen MI, Wernersson S, Respondek M, Akke M, Højrup P, Koeck PJB, Söderberg CAG, Emanuelsson C. </i> J Biol Chem, 2017","date":"2025-10-30T13:53:21.724Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04475r005","statement":[{"text":"Using 3D 1H-15N NOESY-HSQC and 1H-15N TOCSY-HSQC spectroscopy, we could achieve residue-specific assignments for a subset of the observed peaks, namely the segment 8SIDVVQ13 (Fig. 6E). These results unequivocally show that this part of the NTR is flexible.","type":"Results"},{"text":"Taken together, the NMR data provide strong evidence that several copies of the NTR segment are highly flexible and extend away from the dodecamer core.","type":"Results"},{"text":"In this study, we describe Hsp21, a chloroplast-localized sHsp, which has a long NTR (82 amino acids) with conserved methionine residues that are important for substrate binding and scavenging of reactive oxygen species (35, 44).","type":"Discussion"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-17T15:14:42.784Z"}},{"start":1,"end":82,"reference_id":"28325834","reference_source":"pmid","reference_html":"Structural model of dodecameric heat-shock protein Hsp21: Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity. <i> Rutsdottir G, Härmark J, Weide Y, Hebert H, Rasmussen MI, Wernersson S, Respondek M, Akke M, Højrup P, Koeck PJB, Söderberg CAG, Emanuelsson C. </i> J Biol Chem, 2017","date":"2026-03-17T15:26:11.926Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04475r006","statement":[{"text":"Fit to SAXS data further validates the Hsp21 structure model based on cryo-EM and suggests that there are N-terminal arms that are flexible on the outside of the dodecamer.","type":"Figure"}]}],"__v":0,"disorder_content":0.5947136563876652,"disprot_consensus":{"full":[{"start":1,"end":125,"type":"D"},{"start":126,"end":135,"type":"T"}],"Structural state":[{"start":1,"end":135,"type":"D"}],"Structural transition":[{"start":126,"end":135,"type":"T"}]}},{"acc":"A0QP93","sequence":"MNRAVALRIAACGLLGLGAALLIAALLLTTYTKGKIAKIPLDIDTSLVSDGTATAFDPDSLVAERFKIDRDVPVALQQQMSVEAPSNADVVTFQVGTTLRRTDRQQDAGLLLALVDTVTMNRNTAEAVSSENNPGGAVQKPRAIEDEKPPTNIALPHEGLTYRFPFDTEKKTYPFFDPIAQKAFDANYDGEEDVNGLTTYRFVQNVGYDADGKLADPIKYSSLYEDDADASVTARAEVWGVPGEPDESITMDRFYAASRTFWVDPVSGTIVKSEEHGYQYYAREALKPEVTYVDFKVTTNEESVESQVAAASDERDRIALWTRILPITFTALGLVSLVGGAVLGSFALRTESTLIDPGLDTADHGFFDTQGIQVPGAEAKTEKLPAQRPTDLPPDRPI","creator":"viglesias","dataset":[],"date":"2025-10-30T11:44:02.968Z","disprot_id":"DP04476","features":{"pfam":[{"id":"PF11271","name":"Porin PorA","start":11,"end":342}]},"genes":[{"synonyms":[],"olnNames":[{"value":"MSMEG_0317","_id":"69034f842ea0defb7a2f3027","evidences":[]}],"orfNames":[],"_id":"69034f842ea0defb7a2f3026"}],"length":398,"name":"Integral membrane protein","ncbi_taxon_id":246196,"organism":"Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)","regions_counter":1,"released":"2026_06","taxonomy":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Mycobacteriaceae","Mycolicibacterium"],"regions":[{"start":129,"end":154,"reference_id":"35362472","reference_source":"pmid","reference_html":"Crystal structure of the putative cell-wall lipoglycan biosynthesis protein LmcA from Mycobacterium smegmatis. <i> Patel O, Brammananth R, Dai W, Panjikar S, Coppel RL, Lucet IS, Crellin PK. </i> Acta Crystallogr D Struct Biol, 2022","date":"2026-03-27T14:47:57.197Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"7N3V"}],"region_id":"DP04476r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"16189","entry_name":null}],"statement":[{"text":"In our MSMEG_0317Δ structure, loop 6 (residues 129–154) is disordered and would clash with the symmetry-related molecule if it were to adopt the conformation seen in the AlphaFold2 models (Figs. 2 ▸, 5 ▸ c and 5 ▸ d). ","type":"Results"},{"text":"Loop 6 was disordered (residues 129–151 in monomer 1 and residues 129–154 in monomer 2), as previously observed. ","type":"Results"},{"text":"This entrance is in the vicinity of the disordered region of loop 6 (129–154), which is likely to affect the opening and closing of this entrance. ","type":"Results"},{"text":"All the loops connecting the β-strands and α-turns are ordered except for residues 129–154 within loop 6, which connects β5 and β6 (Fig. 2 ▸ b)","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-27T14:47:59.369Z"}}],"__v":0,"disorder_content":0.06532663316582915,"disprot_consensus":{"full":[{"start":129,"end":154,"type":"D"}],"Structural state":[{"start":129,"end":154,"type":"D"}]}},{"acc":"A5D791","sequence":"MERATGPGSLARTLLLPLLLGLVAGTVTARRTSDLLAPTAEAAFGLGAAAAPTSATRVPATGAVIAAEVTVEDSEALPAAAGEQEAREPEPEPEEEPDIRPCGRSLVIISTLDGRIAALDPENHGKKQWDLDVGSGSLVSSSLSKPEVFGNKMIIPSLDGDLFQWDRDRESMETVPFTVESLLESSYKFGDDVVLVGGKSLTTYGLSAYSGKVRYICSALGCRQWDNDEMEQEEDILLLQRTQKTVRAVGPRSGNEKWNFSVGHFELRYIPDMETRAGFIESTLKPSGNKEQSKIISDVEEQEAVMMDTVIKVSVADWKVMAFNKKGGHLEWEYQFCTPIASAWLVKDGKVIPISLFDDTSYAPNDGVLEDEEDIVEAARGATENSVYLGMYRGQLYLQSSVRISEKFPTSPKALESVSSENAIIPLPTIKWKPLIHSPSRTPVLVGSDEFDKCLSNDKFSHEEYSNGALSILQYPYDNGYYLPYYKRERNKRSTQITVRFLDNPNYKNIRKKDPVLLLHWWKEIVGTIVFCIVATTFIVRRLFHPHPHRQRKESETQCQTENKYDAVSGEANDSSWNDIKNSGYVSRYLTDFEPIQCMGRGGFGVVFEARNKVDDCNYAIKRIRLPNRELAREKVMREVKALAKLEHPGIVRYFNAWLEAPPEKWQEKMDEIWLKDDSTDWPLSSPSPVDAPSVKIRRMDPFSTKECIEIIAPSPHSSRSFSVGISCSQTSSSESQFSPLEFSGMDHGNVSKSADAVCQLQDSCLTDCEGEDGTMDGNDEGHSFELCPSEASPYIRSRERTSSSIVFEDSGCDNASSKEEPRMNQPPVGNHYANKLSALRHSGSKSSEPTVSVSPSRPTTLSLDLTKSSVGKLQPSSPKVYLYIQMQLCRKENLKDWLNSRCTIEARERSVCLHIFLQIAEAVEFLHSKGLMHRDLKPSNIFFTMDDVVKVGDFGLVTAMDQDEEDQMVLTPMPGYARHTGQVGTKLYMSPEQIHGNSYSHKVDIFSLGLILFELLYPFGTQMERVRILTDVRDLKFPPLFAQKYPREYAMVQDMLSPSPTERPEAASIIENAIFEDLEFPEKTLLRQRSRSMSSPGAKHSRHSSSPHSPLPSN","creator":"xcastro","dataset":["Stress response proteins"],"date":"2025-10-30T14:42:08.642Z","disprot_id":"DP04478","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":594,"end":660},{"id":"PF00069","name":"Protein kinase domain","start":880,"end":1073}]},"genes":[{"name":{"value":"EIF2AK3","evidences":[{"source":{"id":"Q9NZJ5","name":"UniProtKB","url":"https://www.uniprot.org/uniprot/Q9NZJ5","_id":"690379462ea0defb7a2f3048"},"code":"ECO:0000250","_id":"690379462ea0defb7a2f3047"}],"_id":"690379462ea0defb7a2f3046"},"synonyms":[{"value":"PERK","_id":"690379462ea0defb7a2f3049","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"690379462ea0defb7a2f3045"}],"length":1115,"name":"Eukaryotic translation initiation factor 2-alpha kinase 3","ncbi_taxon_id":9913,"organism":"Bos taurus","regions_counter":7,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Laurasiatheria","Artiodactyla","Ruminantia","Pecora","Bovidae","Bovinae","Bos"],"regions":[{"start":272,"end":308,"reference_id":"29386355","reference_source":"pmid","reference_html":"The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization. <i> Wang P, Li J, Tao J, Sha B. </i> J Biol Chem, 2018","date":"2026-06-01T12:45:44.600Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"5V1D"}],"region_id":"DP04478r001","statement":[{"text":"In the ligand-free PERK luminal domain monomer, a large portion of the peptide-binding groove is not visible in the electron density map due to high flexibility.","type":"Results"},{"text":"Of the six conserved hydrophobic residues located at the bottom of the peptide-binding groove that are important for peptide substrate binding, four (Trp-165, Ala-316, Trp-318, and Tyr-388) are missing in the ligand-free conformation.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys337Ser","start":null,"end":null,"position":null}],"last_modified_by":"xcastro","last_modified_name":"Ximena Aixa Castro","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T15:48:20.432Z"}},{"start":359,"end":388,"reference_id":"29386355","reference_source":"pmid","reference_html":"The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization. <i> Wang P, Li J, Tao J, Sha B. </i> J Biol Chem, 2018","date":"2026-06-01T12:47:09.611Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"5V1D"}],"region_id":"DP04478r002","statement":[{"text":"In the ligand-free PERK luminal domain monomer, a large portion of the peptide-binding groove is not visible in the electron density map due to high flexibility.","type":"Results"},{"text":"Of the six conserved hydrophobic residues located at the bottom of the peptide-binding groove that are important for peptide substrate binding, four (Trp-165, Ala-316, Trp-318, and Tyr-388) are missing in the ligand-free conformation.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys337Ser","start":null,"end":null,"position":null}],"last_modified_by":"xcastro","last_modified_name":"Ximena Aixa Castro","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T15:48:19.106Z"}},{"start":402,"end":421,"reference_id":"29386355","reference_source":"pmid","reference_html":"The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization. <i> Wang P, Li J, Tao J, Sha B. </i> J Biol Chem, 2018","date":"2026-06-01T12:54:18.534Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"5V1D"}],"region_id":"DP04478r003","statement":[{"text":"In the ligand-free PERK luminal domain monomer, a large portion of the peptide-binding groove is not visible in the electron density map due to high flexibility.","type":"Results"},{"text":"Of the six conserved hydrophobic residues located at the bottom of the peptide-binding groove that are important for peptide substrate binding, four (Trp-165, Ala-316, Trp-318, and Tyr-388) are missing in the ligand-free conformation.","type":"Results"},{"text":"Manual inspection of the structure revealed missing residues in the region 402–421.","type":"Curator statement"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys337Ser","start":null,"end":null,"position":null}],"last_modified_by":"xcastro","last_modified_name":"Ximena Aixa Castro","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T15:48:18.289Z"}},{"start":202,"end":308,"reference_id":"29386355","reference_source":"pmid","reference_html":"The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization. <i> Wang P, Li J, Tao J, Sha B. </i> J Biol Chem, 2018","date":"2026-06-01T12:45:11.757Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys337Ser","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"5V1D"}],"region_id":"DP04478r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting peptide with sequence ADPQPWRFYAPR"}]}],"statement":[{"text":"The peptide substrate binding apparently stabilizes the PERK peptide-binding domain and the complete peptide-binding groove can be identified in the structure. In the β-sandwich subdomain, the third layer of β-sheet formed by B20, B21, and B24 is completely missing in the ligand-free monomer, whereas it is clearly present in the substrate-bound monomer. The β-strands B14 and B17 in the second layer of the β-sandwich subdomain are missing in the ligand-free monomer and are visible in the ligand-bound monomer. In the β-hairpin subdomain, the loop between B6 and B7 is flexible in the ligand-free monomer and is stabilized and visible in the ligand-bound monomer.","type":"Results"},{"text":"The crystal structure of the PERK luminal domain complexed with the peptide substrate suggests an induced fit model for PERK to interact with the misfolded proteins. The peptide-binding groove exhibits high flexibility as the peptide substrate-free conformation, whereas peptide substrate binding can stabilize the peptide-binding groove to accommodate the peptide ligand.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T15:48:23.337Z"}},{"start":375,"end":388,"reference_id":"29386355","reference_source":"pmid","reference_html":"The luminal domain of the ER stress sensor protein PERK binds misfolded proteins and thereby triggers PERK oligomerization. <i> Wang P, Li J, Tao J, Sha B. </i> J Biol Chem, 2018","date":"2026-06-01T12:51:51.303Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Cys337Ser","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"5V1D"}],"region_id":"DP04478r007","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting peptide with sequence ADPQPWRFYAPR"}]}],"statement":[{"text":"The peptide substrate binding apparently stabilizes the PERK peptide-binding domain and the complete peptide-binding groove can be identified in the structure. In the β-sandwich subdomain, the third layer of β-sheet formed by B20, B21, and B24 is completely missing in the ligand-free monomer, whereas it is clearly present in the substrate-bound monomer. The β-strands B14 and B17 in the second layer of the β-sandwich subdomain are missing in the ligand-free monomer and are visible in the ligand-bound monomer. In the β-hairpin subdomain, the loop between B6 and B7 is flexible in the ligand-free monomer and is stabilized and visible in the ligand-bound monomer.","type":"Results"},{"text":"The crystal structure of the PERK luminal domain complexed with the peptide substrate suggests an induced fit model for PERK to interact with the misfolded proteins. The peptide-binding groove exhibits high flexibility as the peptide substrate-free conformation, whereas peptide substrate binding can stabilize the peptide-binding groove to accommodate the peptide ligand.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T15:48:21.756Z"}}],"__v":0,"disorder_content":0.07802690582959641,"disprot_consensus":{"full":[{"start":202,"end":308,"type":"T"},{"start":359,"end":374,"type":"D"},{"start":375,"end":388,"type":"T"},{"start":402,"end":421,"type":"D"}],"Structural state":[{"start":272,"end":308,"type":"D"},{"start":359,"end":388,"type":"D"},{"start":402,"end":421,"type":"D"}],"Structural transition":[{"start":202,"end":308,"type":"T"},{"start":375,"end":388,"type":"T"}]}},{"acc":"Q9HWW5","sequence":"MRPLLLALVLLPFAAQAHDDHDHDHAHGSLGKHEHGVAQLNVALDGKTLELELDSPAMNLVGFEHAASTDADKAAVAKARAQLEKPLELFALPVTAGCSVASQELRSPLFGDKAPAHAHKEKAGHEHEHEHEHEHGHADIHAHYQLSCEKPELLKLLTLAEFFKRFPATQKIQVQLIGPDGQKGADLAPASAELKL","creator":"viglesias","dataset":[],"date":"2025-10-30T16:54:17.738Z","disprot_id":"DP04481","features":{"pfam":[{"id":"PF10986","name":"ZrgA family zinc uptake protein","start":32,"end":196}]},"genes":[{"synonyms":[],"olnNames":[{"value":"PA4063","_id":"6903983a2ea0defb7a2f307c","evidences":[]}],"orfNames":[],"_id":"6903983a2ea0defb7a2f307b"}],"length":196,"name":"DUF2796 domain-containing protein","ncbi_taxon_id":208964,"organism":"Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)","regions_counter":7,"released":"2026_06","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Pseudomonadales","Pseudomonadaceae","Pseudomonas"],"regions":[{"start":18,"end":36,"reference_id":"34726168","reference_source":"pmid","reference_html":"Structure and metal-binding properties of PA4063, a novel player in periplasmic zinc trafficking by Pseudomonas aeruginosa. <i> Fiorillo A, Battistoni A, Ammendola S, Secli V, Rinaldo S, Cutruzzolà F, Demitri N, Ilari A. </i> Acta Crystallogr D Struct Biol, 2021","date":"2026-03-26T15:13:05.363Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":4,"cross_refs":[{"db":"PDB","id":"7AHW"}],"region_id":"DP04481r001","statement":[{"text":"The histidine-rich stretches located at the N-terminus and between β3 and β4 are disordered in the apo structure, but a few residues become structured in the presence of zinc, contributing to coordination in one of the two sites. ","type":"Abstract"},{"text":"His-rich sequences of 19 and 24 amino acids, located at the N-terminus and between β3 and β4, respectively, are disordered and are not visible in the crystal structure, as usually observed in other proteins containing this motif (Blindauer, 2015 ▸; Ilari et al., 2011 ▸).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-26T15:19:12.142Z"}},{"start":111,"end":137,"reference_id":"34726168","reference_source":"pmid","reference_html":"Structure and metal-binding properties of PA4063, a novel player in periplasmic zinc trafficking by Pseudomonas aeruginosa. <i> Fiorillo A, Battistoni A, Ammendola S, Secli V, Rinaldo S, Cutruzzolà F, Demitri N, Ilari A. </i> Acta Crystallogr D Struct Biol, 2021","date":"2026-03-26T15:15:15.799Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":5,"cross_refs":[{"db":"PDB","id":"7AHW"}],"region_id":"DP04481r002","statement":[{"text":"The histidine-rich stretches located at the N-terminus and between β3 and β4 are disordered in the apo structure, but a few residues become structured in the presence of zinc, contributing to coordination in one of the two sites. ","type":"Abstract"},{"text":"His-rich sequences of 19 and 24 amino acids, located at the N-terminus and between β3 and β4, respectively, are disordered and are not visible in the crystal structure, as usually observed in other proteins containing this motif (Blindauer, 2015 ▸; Ilari et al., 2011 ▸).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-26T15:19:10.612Z"}},{"start":32,"end":36,"reference_id":"34726168","reference_source":"pmid","reference_html":"Structure and metal-binding properties of PA4063, a novel player in periplasmic zinc trafficking by Pseudomonas aeruginosa. <i> Fiorillo A, Battistoni A, Ammendola S, Secli V, Rinaldo S, Cutruzzolà F, Demitri N, Ilari A. </i> Acta Crystallogr D Struct Biol, 2021","date":"2026-03-26T15:31:18.950Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0008270","term_name":"zinc ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"7AMX"},{"db":"PDB","id":"7BGO"}],"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"29105","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04481r007","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":null}],"statement":[{"text":"Two strong anomalous peaks were observed for each monomer (>9σ), revealing two binding sites, according to the ITC experiments, indicated as site a and site b (Fig. 3 ▸ and Supplementary Fig. S5).","type":"Results"},{"text":"Site b is about 20 Å from site a, on the edge of the β-sheet where the His-rich sequences are inserted. Notably, a few residues belonging to these sequences, which are disordered in apo PA4063, become structured and take part in zinc coordination, although some variability is present. As for site a, the coordination is tetrahedral and three donor groups are provided by one glutamate, Glu47, and two histidines, His16 and His18 (Fig. 3 ▸ d).","type":"Results"},{"text":"The residues referred to by the authors as His16 and His18 correspond to His33 and His35 in the UniProt sequence.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a zinc ion (Zn).\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false}],"__v":0,"disorder_content":0.23469387755102042,"disprot_consensus":{"full":[{"start":18,"end":36,"type":"D"},{"start":111,"end":137,"type":"D"}],"Structural state":[{"start":18,"end":36,"type":"D"},{"start":111,"end":137,"type":"D"}],"Molecular function":[{"start":32,"end":36,"type":"F"}]}},{"acc":"F2NNS0","sequence":"MNRSRRALLKGSLLAGLGALGAQLLRPFALAHEGHAQAPGTHQTRHGGMTTVGEVDHEKNGFDPYAFLTHWETGEVSTLPSGQTLREFNIVAVDKEIEIAPGVYFPAWTYNGQVPGPTLRVTEGDRVRVHFHNAGSHPHTIHFHGIHPASMDGVPGTGPGMIYPGESFTYEFDAYPFGCHLYHCHAIPLKRHIHKGLYGAFIIDPDPERHPEYQAAARARLLGTPENQAWQEFVMVMNGFDTNFDEENEVYAVNTVAHAYMKRPIRIERDRPVRIYLINATEFDPINSFHLHANFFDYYDHGTTLTPTLKTVDTIMQCQGQRGILEFSFNGFEPGLYMFHAHQSEFAELGWMGNFEVIE","creator":"viglesias","dataset":[],"date":"2025-10-30T17:16:51.765Z","disprot_id":"DP04482","features":{"pfam":[{"id":"PF07731","name":"Multicopper oxidase","start":248,"end":357},{"id":"PF07732","name":"Multicopper oxidase","start":100,"end":206}]},"genes":[{"synonyms":[],"olnNames":[{"value":"Marky_0543","_id":"69039d882ea0defb7a2f3087","evidences":[]}],"orfNames":[],"_id":"69039d882ea0defb7a2f3086"}],"length":359,"name":"Copper-containing nitrite reductase","ncbi_taxon_id":869210,"organism":"Marinithermus hydrothermalis (strain DSM 14884 / JCM 11576 / T1)","regions_counter":6,"released":"2026_06","taxonomy":["Bacteria","Thermotogati","Deinococcota","Deinococci","Thermales","Thermaceae","Marinithermus"],"regions":[{"start":32,"end":60,"reference_id":"34605435","reference_source":"pmid","reference_html":"Crystal structures of a dodecameric multicopper oxidase from Marinithermus hydrothermalis. <i> Paavola JL, Battistin U, Ogata CM, Georgiadis MM. </i> Acta Crystallogr D Struct Biol, 2021","date":"2026-05-07T13:38:08.762Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"7RAB"}],"region_id":"DP04482r001","statement":[{"text":"The structure includes residues 61–359 of each subunit; the N-terminal regions including the hexahistidine tag and residues 32–60 are disordered in each subunit. The first ordered residue in each subunit is located on the outside surface of the trimeric units that make up the dodecamer. Thus, the disordered regions of each subunit would be expected to reside outside the dodecamer and would not be expected to interfere with the formation of the dodecamer (Supplementary Fig. S2).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29036","entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-07T13:38:10.634Z"}},{"start":32,"end":60,"reference_id":"34605435","reference_source":"pmid","reference_html":"Crystal structures of a dodecameric multicopper oxidase from Marinithermus hydrothermalis. <i> Paavola JL, Battistin U, Ogata CM, Georgiadis MM. </i> Acta Crystallogr D Struct Biol, 2021","date":"2026-05-07T13:38:20.346Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":4,"cross_refs":[{"db":"PDB","id":"7RAB"}],"region_id":"DP04482r002","statement":[{"text":"The structure includes residues 61–359 of each subunit; the N-terminal regions including the hexahistidine tag and residues 32–60 are disordered in each subunit. The first ordered residue in each subunit is located on the outside surface of the trimeric units that make up the dodecamer. Thus, the disordered regions of each subunit would be expected to reside outside the dodecamer and would not be expected to interfere with the formation of the dodecamer (Supplementary Fig. S2).","type":"Results"},{"text":"Residues 32–60 are the N-terminal tail of mature MhMCO (after signal peptide 1–31 cleavage.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29036","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-07T13:38:22.992Z"}}],"__v":0,"disorder_content":0.0807799442896936,"disprot_consensus":{"full":[{"start":32,"end":60,"type":"D"}],"Structural state":[{"start":32,"end":60,"type":"D"}],"Disorder function":[{"start":32,"end":60,"type":"F"}]}},{"acc":"Q8CJW1","sequence":"MRVLIVEDEPYLAEAIRDGLRLEAIAADIAGDGDTALELLSVNAYDIAVLDRDIPGPSGDEIAERIVASGSGMPILMLTAADRLDDKASGFGLGADDYLTKPFELQELALRLRALDRRRAHSRPPVREIAGLRLDPFRREVYRGGRYVALTRKQFAVLEVLVAAEGGVVSAEELLERAWDENADPFTNAVRITVSALRKRLGEPGIIATVPGVGYRIDTAPVSEQAGGDGG","creator":"viglesias","dataset":[],"date":"2025-10-30T17:36:57.540Z","disprot_id":"DP04483","features":{"pfam":[{"id":"PF00072","name":"Response regulator receiver domain","start":3,"end":112},{"id":"PF00486","name":"Transcriptional regulatory protein, C terminal","start":146,"end":217}]},"genes":[{"synonyms":[],"olnNames":[{"value":"SCO3590","_id":"6903a23f2ea0defb7a2f3096","evidences":[]}],"orfNames":[{"value":"SC66T3.01c","_id":"6903a23f2ea0defb7a2f3097","evidences":[]},{"value":"SCH66.11c","_id":"6903a23f2ea0defb7a2f3098","evidences":[]}],"_id":"6903a23f2ea0defb7a2f3095"}],"length":231,"name":"Two-component system response regulator","ncbi_taxon_id":100226,"organism":"Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)","regions_counter":6,"released":"2026_06","taxonomy":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces","Streptomyces albidoflavus group"],"regions":[{"start":220,"end":231,"reference_id":"34342276","reference_source":"pmid","reference_html":"Structures of full-length VanR from Streptomyces coelicolor in both the inactive and activated states. <i> Maciunas LJ, Porter N, Lee PJ, Gupta K, Loll PJ. </i> Acta Crystallogr D Struct Biol, 2021","date":"2026-03-26T14:45:09.766Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"7LZ9"},{"db":"PDB","id":"7LZA"}],"region_id":"DP04483r001","statement":[{"text":"For both conformational states, no electron density was observed for the 12 C-terminal residues (221–232), suggesting a highly flexible C-terminal tail.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-26T14:45:32.742Z"}},{"start":220,"end":231,"reference_id":"34342276","reference_source":"pmid","reference_html":"Structures of full-length VanR from Streptomyces coelicolor in both the inactive and activated states. <i> Maciunas LJ, Porter N, Lee PJ, Gupta K, Loll PJ. </i> Acta Crystallogr D Struct Biol, 2021","date":"2026-03-26T14:45:27.910Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"7LZ9"},{"db":"PDB","id":"7LZA"}],"region_id":"DP04483r002","statement":[{"text":"For both conformational states, no electron density was observed for the 12 C-terminal residues (221–232), suggesting a highly flexible C-terminal tail.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-26T14:45:33.958Z"}},{"start":82,"end":93,"reference_id":"34342276","reference_source":"pmid","reference_html":"Structures of full-length VanR from Streptomyces coelicolor in both the inactive and activated states. <i> Maciunas LJ, Porter N, Lee PJ, Gupta K, Loll PJ. </i> Acta Crystallogr D Struct Biol, 2021","date":"2026-03-26T14:44:38.832Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"7LZ9"}],"region_id":"DP04483r003","statement":[{"text":"Comparison of the two structures illustrates that phosphorylation of VanR is accompanied by a disorder-to-order transition of helix 4, which lies within the receiver domain of the protein.","type":"Abstract"},{"text":"Helix α4 is absent from the inactive VanRSc structure, reflecting presumptive disorder. ","type":"Figure"},{"text":"The most noticeable difference between the two receiver domains is the absence of helix α4 in the inactive structure, along with significantly different conformations of the loop connecting β4 to α4. In the inactive structure no electron density was observed for the entirety of α4, even though density is seen for the two flanking loops.","type":"Results"},{"text":"Residues on α4 that contribute to the dimer interface (Ala88, Phe91 and Lys87) must also move in the shift from the inactive to the activated conformation, but the precise nature of these motions remains unknown, since α4 is disordered in the inactive state. However, it is likely that the interactions made by these three residues serve to stabilize α4 in its disorder-to-order transition.","type":"Results"},{"text":"The exact range for the IDR can be defined by the unmodeled residues in the inactive, which comprise D82 to L93.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-26T14:44:41.939Z"}},{"start":82,"end":93,"reference_id":"34342276","reference_source":"pmid","reference_html":"Structures of full-length VanR from Streptomyces coelicolor in both the inactive and activated states. <i> Maciunas LJ, Porter N, Lee PJ, Gupta K, Loll PJ. </i> Acta Crystallogr D Struct Biol, 2021","date":"2026-03-26T14:55:32.968Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04483r005","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"152255","statements":[{"type":"Results","text":"The activated state was generated by treating the protein with beryllium fluoride, which has proven to act as a faithful mimic of aspartate phosphorylation in a variety of response regulators (Wemmer & Kern, 2005 ▸)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":null}],"statement":[{"text":"Comparison of the two structures illustrates that phosphorylation of VanR is accompanied by a disorder-to-order transition of helix 4, which lies within the receiver domain of the protein.","type":"Abstract"},{"text":"The most noticeable difference between the two receiver domains is the absence of helix α4 in the inactive structure, along with significantly different conformations of the loop connecting β4 to α4. In the inactive structure no electron density was observed for the entirety of α4, even though density is seen for the two flanking loops.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"7LZ9"},{"db":"PDB","id":"7LZA"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","states_connection":[{"source":"DP04483r003","target":"DP04483r006"}]},{"start":82,"end":93,"reference_id":"34342276","reference_source":"pmid","reference_html":"Structures of full-length VanR from Streptomyces coelicolor in both the inactive and activated states. <i> Maciunas LJ, Porter N, Lee PJ, Gupta K, Loll PJ. </i> Acta Crystallogr D Struct Biol, 2021","date":"2026-03-26T14:55:01.789Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"7LZA"}],"region_id":"DP04483r006","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"152255","statements":[{"type":"Results","text":"The activated state was generated by treating the protein with beryllium fluoride, which has proven to act as a faithful mimic of aspartate phosphorylation in a variety of response regulators (Wemmer & Kern, 2005 ▸)."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"18420","entry_name":null}],"statement":[{"text":"Comparison of the two structures illustrates that phosphorylation of VanR is accompanied by a disorder-to-order transition of helix 4, which lies within the receiver domain of the protein.","type":"Abstract"},{"text":"The domain adopts an α/β-sandwich fold composed of a central five-stranded parallel β-sheet with a 2–1–3–4–5 topology surrounded by three α-helices on one side (α2, α3 and α4) and two α-helices on the other (α1 and α5).","type":"Results"}]}],"__v":0,"disorder_content":0.1038961038961039,"disprot_consensus":{"full":[{"start":82,"end":93,"type":"T"},{"start":220,"end":231,"type":"D"}],"Structural state":[{"start":82,"end":93,"type":"D"},{"start":220,"end":231,"type":"D"}],"Disorder function":[{"start":220,"end":231,"type":"F"}],"Structural transition":[{"start":82,"end":93,"type":"T"}]}},{"acc":"O76290","sequence":"MEAPAAVVTGAAKRIGRAIAVKLHQTGYRVVIHYHNSAEAAVSLADELNKERSNTAVVCQADLTNSNVLPASCEEIINSCFRAFGRCDVLVNNASAFYPTPLVQGDHEDNSNGKTVETQVAELIGTNAIAPFLLTMSFAQRQKGTNPNCTSSNLSIVNLCDAMVDQPCMAFSLYNMGKHALVGLTQSAALELAPYGIRVNGVAPGVSLLPVAMGEEEKDKWRRKVPLGRREASAEQIADAVIFLVSGSAQYITGSIIKVDGGLSLVHA","creator":"viglesias","dataset":[],"date":"2025-10-31T10:53:05.885Z","disprot_id":"DP04486","features":{"pfam":[{"id":"PF13561","name":"Enoyl-(Acyl carrier protein) reductase","start":10,"end":264}]},"genes":[{"name":{"value":"PTR1","evidences":[{"source":{"id":"AAC23562.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/AAC23562.1","_id":"690495122ea0defb7a2f30c8"},"code":"ECO:0000313","_id":"690495122ea0defb7a2f30c7"}],"_id":"690495122ea0defb7a2f30c6"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"690495122ea0defb7a2f30c5"}],"length":268,"name":"Pteridine reductase","ncbi_taxon_id":5702,"organism":"Trypanosoma brucei brucei","regions_counter":2,"released":"2026_06","taxonomy":["Eukaryota","Discoba","Euglenozoa","Kinetoplastea","Metakinetoplastina","Trypanosomatida","Trypanosomatidae","Trypanosoma"],"regions":[{"start":207,"end":217,"reference_id":"32496217","reference_source":"pmid","reference_html":"High-resolution crystal structure of Trypanosoma brucei pteridine reductase 1 in complex with an innovative tricyclic-based inhibitor. <i> Landi G, Linciano P, Tassone G, Costi MP, Mangani S, Pozzi C. </i> Acta Crystallogr D Struct Biol, 2020","date":"2026-03-26T18:54:31.363Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"6TBX"}],"region_id":"DP04486r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"25523","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30089","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"21589971"}],"statement":[{"text":"In subunit C the substrate-binding loop, including residues 207–215, appears to be highly flexible, and residues 208–217 have been excluded from our model.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-26T18:54:42.127Z"}}],"__v":0,"disorder_content":0.041044776119402986,"disprot_consensus":{"full":[{"start":207,"end":217,"type":"D"}],"Structural state":[{"start":207,"end":217,"type":"D"}]}},{"acc":"Q5NBY9","sequence":"MERVNDASCGPSGCYTYQVSRHSTEMLHNLNQQRKNGGRFCDVLLRVGDESFPAHRAVLAACSEYFESVFSAQLGDGGAADGGPADVGGAAAAPGGGAGGSRELEMHTISSKVFGDILDFAYTSRIVVRLESFPELMTAAKFLLMRSVIEICQEVIKQSNVQILVPPARADIMLFRPPGTSDLGFPLDMTNGAAMAANSNGIAGSMQPEEEAARATGAAIAGQASLPVLPGVDRLPMVAGPLSPQLLTSPFPNVASSAPPLTSKRGRGRPRKANLLDSMFGSPGGLREAGILPCGLCGKVFTDANRLRQHEAQHGVTSLQLGYIDLPPPRLGENGLPISEDPDGPRKRSRTRKQVACEICGKIFRDVYHLNRHKLSHSGEKPYSCPVCGLRFKRKDRMSYHVRSHDGSVGKPYICQSCGKGFSRPDHLNGHIKQVHTSERPHKCQTCNASFATRDRLRSHLACHEDKVPCQVCGKYLRAAYMADHLKKHSEGPSNFCSICNRGFSSASYLKVHVKTHHGVPLPQVSRHQEPILNGGAAFHCARTYGNKEGQKCSHQDLIESSDSYGDLSDASDLKTPEKQSANGSFSCDVAVPKNKMESDGEKKYPCPECGSFFRSKSYLNKHIQKVHVRALGGPLGDLGPALGSPFSPQQNMSLLESFGFQIVQSAFASSLVDPEVDQQPMGPEGK","creator":"viglesias","dataset":[],"date":"2025-10-31T11:01:41.707Z","disprot_id":"DP04487","features":{"pfam":[{"id":"PF00096","name":"Zinc finger, C2H2 type","start":357,"end":377},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":383,"end":405},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":413,"end":436},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":497,"end":517},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":605,"end":628},{"id":"PF00651","name":"BTB/POZ domain","start":30,"end":159},{"id":"PF13912","name":"C2H2-type zinc finger","start":442,"end":466},{"id":"PF16637","name":"Putative zinc-finger between two C2H2 zinc-fingers on Patz","start":535,"end":604}]},"genes":[{"name":{"value":"Patz1","evidences":[{"source":{"id":"MGI:1891832","name":"MGI","url":"http://www.informatics.jax.org/marker/MGI:1891832","_id":"690497162ea0defb7a2f30d7"},"code":"ECO:0000312","_id":"690497162ea0defb7a2f30d6"}],"_id":"690497162ea0defb7a2f30d5"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"690497162ea0defb7a2f30d4"}],"length":687,"name":"POZ (BTB) and AT hook-containing zinc finger 1","ncbi_taxon_id":10090,"organism":"Mus musculus","regions_counter":1,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"regions":[{"start":75,"end":105,"reference_id":"32496219","reference_source":"pmid","reference_html":"Structural analysis of the PATZ1 BTB domain homodimer. <i> Piepoli S, Alt AO, Atilgan C, Mancini EJ, Erman B. </i> Acta Crystallogr D Struct Biol, 2020","date":"2026-03-26T14:26:49.361Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"6GUV"}],"region_id":"DP04487r001","statement":[{"text":"The mammalian PATZ1 (ZBTB19) protein is predicted to contain a 31-amino-acid A2/B3 loop (residues 75–105) that is partially conserved in cKrox (ZBTB15), which sets PATZ1 apart from the other ZBTB family members (Figs. 1 a and 1 b). ","type":"Results"},{"text":"This loop is glycine- and alanine-rich and is predicted to be partially disordered; however, a short β-strand is predicted for the last six residues. The single difference between the human and mouse PATZ1 BTB domains (T91A) is found within this large loop. In the crystal structure no density could be assigned to the residues belonging to the A2/B3 loop, suggesting that these amino acids are partially disordered or flexible.","type":"Results"},{"text":"This suggests that these seven amino acids were in fact important for stabilizing the B1–B2 β-sheet and for crystal packing (hence the better diffraction), yet their absence did not encourage the folding of the A2/B3 loop.","type":"Results"},{"text":"The coordinates of 31 residues in a central region, unique to mammalian PATZ1 BTB domains, could not be assigned (indicated by a dotted loop). ","type":"Figure"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-26T16:06:46.567Z"}}],"__v":0,"disorder_content":0.04512372634643377,"disprot_consensus":{"full":[{"start":75,"end":105,"type":"D"}],"Structural state":[{"start":75,"end":105,"type":"D"}]}},{"acc":"X1WGP9","sequence":"MERTEQPWNSSYTYQVSKHSAEMLHNLNGQRKDGGRFCDVILRVGEESFPAHKAVLAACSEYFESVFSCQTEDDGQGKELEMHTISPKVFRDILDFAYTSKIVVRLECFPELMTAAKFLLMRSVIEICQEVIKQSNVQILVPPSRGGEHSLFRAAEQLSYPLPVDMSNGSVSNGAVFTDNNDSDSADPSNISQPAAPGAPTADRLAVSPLEFSSGHLNIDGFKRGKPRPKKEPIAQPVTYNNSTGQNEEGALFSCGICGKMFPDEVQLRNHEAQHGTFTGVMSSGIELVVVDGPTMISHPGQQRFQGNGLPTDTRKRERTRRHVACDLCGKVFRDVYHLNRHKLSHSGEKPYACPVCGLRFKRKDRMSYHVRSHDGSVGKPYVCQSCGKGFSRPDHLNGHIKQVHTTERPHKCQICNASFATRDRLRSHLACHEDKIPCQVCGKYLRAAYMTDHLKKHSEGPHNYCGICNKDGQENAGKCPHQDSDGSDAVFGDLSNGMDLKAEHKVEGEEMEVTSFIFNGQPDDAVTSPEGSKNIPTTDQEKKFACGECGQAFRTKSYLNKHHHRVHKKRAAAASSLGDLASPFSPQQNMSLLESFGFQIVQSAFASSLVDSEIGSSGMGLGEK","creator":"viglesias","dataset":[],"date":"2025-10-31T11:09:47.358Z","disprot_id":"DP04488","features":{"pfam":[{"id":"PF00096","name":"Zinc finger, C2H2 type","start":253,"end":275},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":326,"end":346},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":352,"end":374},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":382,"end":405},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":545,"end":568},{"id":"PF00651","name":"BTB/POZ domain","start":27,"end":135},{"id":"PF13912","name":"C2H2-type zinc finger","start":411,"end":435},{"id":"PF16637","name":"Putative zinc-finger between two C2H2 zinc-fingers on Patz","start":462,"end":544}]},"genes":[{"name":{"value":"patz1","evidences":[{"source":{"id":"ENSDARP00000129407","name":"Ensembl","url":"https://www.ensembl.org/id/ENSDARP00000129407","_id":"690498fb2ea0defb7a2f30e1"},"code":"ECO:0000313","_id":"690498fb2ea0defb7a2f30e0"},{"source":{"id":"XP_009300883.1","name":"RefSeq","url":"https://www.ncbi.nlm.nih.gov/protein/XP_009300883.1","_id":"690498fb2ea0defb7a2f30e3"},"code":"ECO:0000313","_id":"690498fb2ea0defb7a2f30e2"},{"source":{"id":"ZDB-GENE-111223-4","name":"ZFIN","url":"http://zfin.org/cgi-bin/webdriver?MIval=aa-markerview.apg&OID=ZDB-GENE-111223-4","_id":"690498fb2ea0defb7a2f30e5"},"code":"ECO:0000313","_id":"690498fb2ea0defb7a2f30e4"}],"_id":"690498fb2ea0defb7a2f30df"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"690498fb2ea0defb7a2f30de"}],"length":625,"name":"POZ-, AT hook-, and zinc finger-containing protein 1 isoform X2","ncbi_taxon_id":7955,"organism":"Danio rerio","regions_counter":2,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Actinopterygii","Neopterygii","Teleostei","Ostariophysi","Cypriniformes","Danionidae","Danioninae","Danio"],"regions":[{"start":1,"end":10,"reference_id":"32496219","reference_source":"pmid","reference_html":"Structural analysis of the PATZ1 BTB domain homodimer. <i> Piepoli S, Alt AO, Atilgan C, Mancini EJ, Erman B. </i> Acta Crystallogr D Struct Biol, 2020","date":"2025-11-20T11:08:45.946Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"6GUW"}],"region_id":"DP04488r001","statement":[{"text":"The zebrafish PATZ1 BTB domain was expressed from a construct encoding amino acids 1–135 preceded at the N-terminus by 20 amino acids comprising a His tag and an HRV-3C protease digestion site. The 20 amino acids at the N-terminus and the first ten residues of the zebrafish PATZ1 BTB domain are not visible in the electron-density map. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-11-25T19:57:27.435Z"}},{"start":1,"end":10,"reference_id":"32496219","reference_source":"pmid","reference_html":"Structural analysis of the PATZ1 BTB domain homodimer. <i> Piepoli S, Alt AO, Atilgan C, Mancini EJ, Erman B. </i> Acta Crystallogr D Struct Biol, 2020","date":"2025-11-20T11:09:14.988Z","curator_id":"viglesias","curator_name":"Valentín Iglesias","curator_orcid":"0000-0002-6133-0869","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"6GUW"}],"region_id":"DP04488r002","statement":[{"text":"The zebrafish PATZ1 BTB domain was expressed from a construct encoding amino acids 1–135 preceded at the N-terminus by 20 amino acids comprising a His tag and an HRV-3C protease digestion site. The 20 amino acids at the N-terminus and the first ten residues of the zebrafish PATZ1 BTB domain are not visible in the electron-density map. ","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-11-25T19:57:30.084Z"}}],"__v":0,"disorder_content":0.016,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"D"}],"Structural state":[{"start":1,"end":10,"type":"D"}],"Disorder function":[{"start":1,"end":10,"type":"F"}]}},{"acc":"C1CZ84","sequence":"MTDPAPPPTALAAAKARMRELAASYGAGLPGRDTHSLMHGLDGITLTFMPMGQRDGAYDPEHHVILINSQVRPERQRFTLAHEISHALLLGDDDLLSDLHDEYEGDRLEQVIETLCNVGAAALLMPAELIDDLLTRFGPTGRALAELARRADVSATSALYALAERTAPPVIYAVCALSRQEDEGEGGGAKELTVRASSASAGVKYSLSAGTPVPDDHPAALALDTRLPLAQDSYVPFRSGRRMPAYVDAFPERQRVLVSFALPAGRSEPDADKPEAPGDQS","creator":"xcastro","dataset":["Stress response proteins"],"date":"2025-11-04T11:20:14.460Z","disprot_id":"DP04489","features":{"pfam":[{"id":"PF06114","name":"IrrE N-terminal-like domain","start":43,"end":162}]},"genes":[{"name":{"value":"irrE","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/19150362","id":"19150362","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/19150362","_id":"6909e16f2ea0defb7a2f310e"},"code":"ECO:0000303","_id":"6909e16f2ea0defb7a2f310d"}],"_id":"6909e16f2ea0defb7a2f310c"},"synonyms":[],"olnNames":[{"value":"Deide_03030","_id":"6909e16f2ea0defb7a2f310f","evidences":[]}],"orfNames":[],"_id":"6909e16f2ea0defb7a2f310b"}],"length":281,"name":"Radiation response metalloprotease IrrE","ncbi_taxon_id":546414,"organism":"Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115)","regions_counter":3,"released":"2026_06","taxonomy":["Bacteria","Thermotogati","Deinococcota","Deinococci","Deinococcales","Deinococcaceae","Deinococcus"],"regions":[{"start":264,"end":281,"reference_id":"19150362","reference_source":"pmid","reference_html":"Crystal structure of the IrrE protein, a central regulator of DNA damage repair in deinococcaceae. <i> Vujicić-Zagar A, Dulermo R, Le Gorrec M, Vannier F, Servant P, Sommer S, de Groot A, Serre L. </i> J Mol Biol, 2009","date":"2025-11-04T11:26:39.672Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The purified recombinant 32-kDa IrrE exhibits the additional peptide MGSSHHHHHHSSGENLYFQG that includes a TEV protease cleavage site."}]}],"cross_refs":[{"db":"PDB","id":"3DTI"},{"db":"PDB","id":"3DTE"},{"db":"PDB","id":"3DTK"}],"region_id":"DP04489r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"312"}],"sequence_construct":"MGSSHHHHHHSSGENLYFQGMTDPAPPPTALAAAKARMRELAASYGAGLPGRDTHSLMHGLDGITLTFMPMGQRDGAYDPEHHVILINSQVRPERQRFTLAHEISHALLLGDDDLLSDLHDEYEGDRLEQVIETLCNVGAAALLMPAELIDDLLTRFGPTGRALAELARRADVSATSALYALAERTAPPVIYAVCALSRQEDEGEGGGAKELTVRASSASAGVKYSLSAGTPVPDDHPAALALDTRLPLAQDSYVPFRSGRRMPAYVDAFPERQRVLVSFALPAGRSEPDADKPEAPGDQS","statement":[{"text":"No electron density was present in these models for the 6His tag, the first 7 and the last 17 residues as well as the loop constituted by residues 180 to 188.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-17T14:36:35.783Z"}},{"start":264,"end":281,"reference_id":"19150362","reference_source":"pmid","reference_html":"Crystal structure of the IrrE protein, a central regulator of DNA damage repair in deinococcaceae. <i> Vujicić-Zagar A, Dulermo R, Le Gorrec M, Vannier F, Servant P, Sommer S, de Groot A, Serre L. </i> J Mol Biol, 2009","date":"2025-11-04T11:26:59.126Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The purified recombinant 32-kDa IrrE exhibits the additional peptide MGSSHHHHHHSSGENLYFQG that includes a TEV protease cleavage site."}]}],"cross_refs":[{"db":"PDB","id":"3DTI"},{"db":"PDB","id":"3DTE"},{"db":"PDB","id":"3DTK"}],"region_id":"DP04489r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"32051"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"312"}],"sequence_construct":"MGSSHHHHHHSSGENLYFQGMTDPAPPPTALAAAKARMRELAASYGAGLPGRDTHSLMHGLDGITLTFMPMGQRDGAYDPEHHVILINSQVRPERQRFTLAHEISHALLLGDDDLLSDLHDEYEGDRLEQVIETLCNVGAAALLMPAELIDDLLTRFGPTGRALAELARRADVSATSALYALAERTAPPVIYAVCALSRQEDEGEGGGAKELTVRASSASAGVKYSLSAGTPVPDDHPAALALDTRLPLAQDSYVPFRSGRRMPAYVDAFPERQRVLVSFALPAGRSEPDADKPEAPGDQS","statement":[{"text":"No electron density was present in these models for the 6His tag, the first 7 and the last 17 residues as well as the loop constituted by residues 180 to 188.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-17T14:36:42.917Z"}},{"start":179,"end":191,"reference_id":"19150362","reference_source":"pmid","reference_html":"Crystal structure of the IrrE protein, a central regulator of DNA damage repair in deinococcaceae. <i> Vujicić-Zagar A, Dulermo R, Le Gorrec M, Vannier F, Servant P, Sommer S, de Groot A, Serre L. </i> J Mol Biol, 2009","date":"2025-11-04T11:33:05.379Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The purified recombinant 32-kDa IrrE exhibits the additional peptide MGSSHHHHHHSSGENLYFQG that includes a TEV protease cleavage site."}]}],"cross_refs":[{"db":"PDB","id":"3DTI"}],"region_id":"DP04489r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"32051"}],"sequence_construct":"MGSSHHHHHHSSGENLYFQGMTDPAPPPTALAAAKARMRELAASYGAGLPGRDTHSLMHGLDGITLTFMPMGQRDGAYDPEHHVILINSQVRPERQRFTLAHEISHALLLGDDDLLSDLHDEYEGDRLEQVIETLCNVGAAALLMPAELIDDLLTRFGPTGRALAELARRADVSATSALYALAERTAPPVIYAVCALSRQEDEGEGGGAKELTVRASSASAGVKYSLSAGTPVPDDHPAALALDTRLPLAQDSYVPFRSGRRMPAYVDAFPERQRVLVSFALPAGRSEPDADKPEAPGDQS","statement":[{"text":"No electron density was present in these models for the 6His tag, the first 7 and the last 17 residues as well as the loop constituted by residues 180 to 188.","type":"Results"},{"text":"In the PDB structure 3DTI, residues 179–191 of the loop are missing.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-17T14:34:26.231Z"}}],"__v":0,"disorder_content":0.1103202846975089,"disprot_consensus":{"full":[{"start":179,"end":191,"type":"D"},{"start":264,"end":281,"type":"D"}],"Structural state":[{"start":179,"end":191,"type":"D"},{"start":264,"end":281,"type":"D"}],"Disorder function":[{"start":264,"end":281,"type":"F"}]}},{"acc":"O60870","sequence":"MGKSDFLTPKAIANRIKSKGLQKLRWYCQMCQKQCRDENGFKCHCMSESHQRQLLLASENPQQFMDYFSEEFRNDFLELLRRRFGTKRVHNNIVYNEYISHREHIHMNATQWETLTDFTKWLGREGLCKVDETPKGWYIQYIDRDPETIRRQLELEKKKKQDLDDEEKTAKFIEEQVRRGLEGKEQEVPTFTELSRENDEEKVTFNLSKGACSSSGATSSKSSTLGPSALKTIGSSASVKRKESSQSSTQSKEKKKKKSALDEIMEIEEEKKRTARTDYWLQPEIIVKIITKKLGEKYHKKKAIVKEVIDKYTAVVKMIDSGDKLKLDQTHLETVIPAPGKRILVLNGGYRGNEGTLESINEKTFSATIVIETGPLKGRRVEGIQYEDISKLA","creator":"xcastro","dataset":["RNA-binding proteins","Stress response proteins"],"date":"2025-11-04T14:45:38.323Z","disprot_id":"DP04491","features":{"pfam":[{"id":"PF10357","name":"KIN17 WH-like domain","start":59,"end":177},{"id":"PF18131","name":"KN17 SH3-like domain","start":276,"end":328},{"id":"PF25092","name":"KIN17 C-terminal SH3 domain","start":337,"end":393},{"id":"PF25095","name":"KIN17 C2H2-type zinc finger domain","start":24,"end":53}]},"genes":[{"name":{"value":"KIN","evidences":[{"source":{"id":"HGNC:6327","name":"HGNC","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:6327","_id":"690a11922ea0defb7a2f3129"},"code":"ECO:0000312","_id":"690a11922ea0defb7a2f3128"}],"_id":"690a11922ea0defb7a2f3127"},"synonyms":[{"value":"BTCD","_id":"690a11922ea0defb7a2f312a","evidences":[]},{"value":"KIN17","_id":"690a11922ea0defb7a2f312b","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"690a11922ea0defb7a2f3126"}],"length":393,"name":"DNA/RNA-binding protein KIN17","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":6,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":51,"end":64,"reference_id":"18029424","reference_source":"pmid","reference_html":"Solution structure of the region 51-160 of human KIN17 reveals an atypical winged helix domain. <i> Carlier L, Couprie J, le Maire A, Guilhaudis L, Milazzo-Segalas I, Courçon M, Moutiez M, Gondry M, Davoust D, Gilquin B, Zinn-Justin S. </i> Protein Sci, 2007","date":"2025-11-04T14:50:18.927Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"2V1N"},{"db":"BMRB","id":"6938"}],"region_id":"DP04491r001","statement":[{"text":"The first 14 N-terminal residues and the five last C-terminal amino acids (residues 51–64 and 156–160, respectively) are disordered, whereas fragment 65–155 adopts a well-defined α/β fold.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-17T14:14:58.523Z"}},{"start":1,"end":59,"reference_id":"33243851","reference_source":"pmid","reference_html":"Mechanism of protein-guided folding of the active site U2/U6 RNA during spliceosome activation. <i> Townsend C, Leelaram MN, Agafonov DE, Dybkov O, Will CL, Bertram K, Urlaub H, Kastner B, Stark H, Lührmann R. </i> Science, 2020","date":"2025-11-04T15:32:01.857Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"7ABI"},{"db":"EMDB","id":"11697"}],"region_id":"DP04491r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15393"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75533"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y388"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6P2Q9"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"135398633"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"890"}],"statement":[{"text":"In the cryo-EM complex, residues 1–59 and 180–273 are missing, although this is not stated explicitly in the paper.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-17T14:12:31.966Z"}},{"start":1,"end":59,"reference_id":"33243851","reference_source":"pmid","reference_html":"Mechanism of protein-guided folding of the active site U2/U6 RNA during spliceosome activation. <i> Townsend C, Leelaram MN, Agafonov DE, Dybkov O, Will CL, Bertram K, Urlaub H, Kastner B, Stark H, Lührmann R. </i> Science, 2020","date":"2025-11-04T15:32:30.231Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"7ABI"},{"db":"EMDB","id":"11697"}],"region_id":"DP04491r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15393"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75533"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y388"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6P2Q9"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"135398633"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"890"}],"statement":[{"text":"In the cryo-EM complex, residues 1–59 and 180–273 are missing, although this is not stated explicitly in the paper.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-17T14:13:20.711Z"}},{"start":180,"end":273,"reference_id":"33243851","reference_source":"pmid","reference_html":"Mechanism of protein-guided folding of the active site U2/U6 RNA during spliceosome activation. <i> Townsend C, Leelaram MN, Agafonov DE, Dybkov O, Will CL, Bertram K, Urlaub H, Kastner B, Stark H, Lührmann R. </i> Science, 2020","date":"2025-11-04T15:32:46.469Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"7ABI"},{"db":"EMDB","id":"11697"}],"region_id":"DP04491r004","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15393"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75533"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y388"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6P2Q9"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"135398633"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"890"}],"statement":[{"text":"In the cryo-EM complex, residues 1–59 and 180–273 are missing, although this is not stated explicitly in the paper.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-17T14:12:37.277Z"}},{"start":180,"end":273,"reference_id":"33243851","reference_source":"pmid","reference_html":"Mechanism of protein-guided folding of the active site U2/U6 RNA during spliceosome activation. <i> Townsend C, Leelaram MN, Agafonov DE, Dybkov O, Will CL, Bertram K, Urlaub H, Kastner B, Stark H, Lührmann R. </i> Science, 2020","date":"2025-11-04T15:33:20.502Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"7ABI"},{"db":"EMDB","id":"11697"}],"region_id":"DP04491r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15393"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75533"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y388"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6P2Q9"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"135398633"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"890"}],"statement":[{"text":"In the cryo-EM complex, residues 1–59 and 180–273 are missing, although this is not stated explicitly in the paper.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-17T14:13:01.690Z"}},{"start":1,"end":393,"reference_id":"33243851","reference_source":"pmid","reference_html":"Mechanism of protein-guided folding of the active site U2/U6 RNA during spliceosome activation. <i> Townsend C, Leelaram MN, Agafonov DE, Dybkov O, Will CL, Bertram K, Urlaub H, Kastner B, Stark H, Lührmann R. </i> Science, 2020","date":"2025-11-04T15:41:49.526Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"GO:0071011","term_name":"precatalytic spliceosome","term_namespace":"Cellular component","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"7ABI"},{"db":"EMDB","id":"11697"}],"ec_go":"IDA","region_id":"DP04491r006","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q15393"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"O75533"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y388"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q6P2Q9"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"888"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"135398633"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"890"}],"statement":[{"text":"The positions of the U2 5′ domain, Brr2, and PRP8RH in pre-Bact-2 are likely stabilized by KIN17. The latter is a protein linked to ultraviolet-induced DNA repair (20) and it can be localized solely in the pre-Bact-2 complex, suggesting that it binds transiently at this stage.","type":"Results"}],"term_comment":"","term_def":"\"A spliceosomal complex that is formed by the recruitment of a preassembled U5-containing tri-snRNP to the prespliceosome. Although all 5 snRNPs are present, the precatalytic spliceosome is catalytically inactive. The precatalytic spliceosome includes many proteins in addition to those found in the associated snRNPs.\" [GOC:ab, GOC:krc, GOC:mah, PMID:18322460, PMID:19239890]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-20T16:37:02.935Z"}}],"__v":0,"disorder_content":0.4020356234096692,"disprot_consensus":{"full":[{"start":1,"end":64,"type":"D"},{"start":65,"end":179,"type":"F"},{"start":180,"end":273,"type":"D"},{"start":274,"end":393,"type":"F"}],"Structural state":[{"start":1,"end":64,"type":"D"},{"start":180,"end":273,"type":"D"}],"Disorder function":[{"start":1,"end":59,"type":"F"},{"start":180,"end":273,"type":"F"}],"Cellular component":[{"start":1,"end":393,"type":"F"}]}},{"acc":"O00170","sequence":"MADIIARLREDGIQKRVIQEGRGELPDFQDGTKATFHYRTLHSDDEGTVLDDSRARGKPMELIIGKKFKLPVWETIVCTMREGEIAQFLCDIKHVVLYPLVAKSLRNIAVGKDPLEGQRHCCGVAQMREHSSLGHADLDALQQNPQPLIFHMEMLKVESPGTYQQDPWAMTDEEKAKAVPLIHQEGNRLYREGHVKEAAAKYYDAIACLKNLQMKEQPGSPEWIQLDQQITPLLLNYCQCKLVVEEYYEVLDHCSSILNKYDDNVKAYFKRGKAHAAVWNAQEAQADFAKVLELDPALAPVVSRELRALEARIRQKDEEDKARFRGIFSH","creator":"xcastro","dataset":[],"date":"2025-11-05T08:53:14.844Z","disprot_id":"DP04492","features":{"pfam":[{"id":"PF23322","name":"AH receptor-interacting protein, N-terminal FKBP-type PPIase","start":13,"end":156}]},"genes":[{"name":{"value":"AIP","_id":"690b107e2ea0defb7a2f316d","evidences":[]},"synonyms":[{"value":"XAP2","_id":"690b107e2ea0defb7a2f316e","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"690b107e2ea0defb7a2f316c"}],"length":330,"name":"AH receptor-interacting protein","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":2,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":111,"end":135,"reference_id":"23418784","reference_source":"pmid","reference_html":"The FKBP-type domain of the human aryl hydrocarbon receptor-interacting protein reveals an unusual Hsp90 interaction. <i> Linnert M, Lin YJ, Manns A, Haupt K, Paschke AK, Fischer G, Weiwad M, Lücke C. </i> Biochemistry, 2013","date":"2025-11-05T09:03:04.629Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"BMRB","id":"18001"},{"db":"PDB","id":"2LKN"}],"region_id":"DP04492r001","statement":[{"text":"In AIP2–166, on the other hand, the insert encompasses 57 amino acid residues (Figure S3, Supporting Information), beginning with a rather long helical segment that comprises 19 residues (αIII), followed by an apparently mostly random-coil structure, and ending with the FKBP-atypic α-helix (αIV).","type":"Results"},{"text":"The nonstructured section of the βD-βE extension, i.e., residues Gly111–His135, includes the segment Arg119–Ser132, which features a large number of nonassigned residues, (26) suggesting that this region of AIP may exhibit pronounced amide proton exchange or conformational variability.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-20T16:16:25.686Z"}}],"__v":0,"disorder_content":0.07575757575757576,"disprot_consensus":{"full":[{"start":111,"end":135,"type":"D"}],"Structural state":[{"start":111,"end":135,"type":"D"}]}},{"acc":"P0A9P6","sequence":"MAEFETTFADLGLKAPILEALNDLGYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLQNLDPELKAPQILVLAPTRELAVQVAEAMTDFSKHMRGVNVVALYGGQRYDVQLRALRQGPQIVVGTPGRLLDHLKRGTLDLSKLSGLVLDEADEMLRMGFIEDVETIMAQIPEGHQTALFSATMPEAIRRITRRFMKEPQEVRIQSSVTTRPDISQSYWTVWGMRKNEALVRFLEAEDFDAAIIFVRTKNATLEVAEALERNGYNSAALNGDMNQALREQTLERLKDGRLDILIATDVAARGLDVERISLVVNYDIPMDSESYVHRIGRTGRAGRAGRALLFVENRERRLLRNIERTMKLTIPEVELPNAELLGKRRLEKFAAKVQQQLESSDLDQYRALLSKIQPTAEGEELDLETLAAALLKMAQGERTLIVPPDAPMRPKREFRDRDDRGPRDRNDRGPRGDREDRPRRERRDVGDMQLYRIEVGRDDGVEVRHIVGAIANEGDISSRYIGNIKLFASHSTIELPKGMPGEVLQHFTRTRILNKPMNMQLLGDAQPHTGGERRGGGRGFGGERREGGRNFSGERREGGRGDGRRFSGERREGRAPRRDDSTGRRRFGGDA","creator":"xcastro","dataset":["RNA-binding proteins","Condensates-related proteins","Stress response proteins"],"date":"2025-11-05T13:09:39.668Z","disprot_id":"DP04493","features":{"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":30,"end":196},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":232,"end":340},{"id":"PF03880","name":"DbpA RNA binding domain","start":489,"end":558},{"id":"PF12343","name":"DeaD helicase C-terminal disordered region","start":568,"end":629},{"id":"PF25399","name":"RNA helicase DeaD dimerization domain","start":374,"end":443}]},"genes":[{"name":{"value":"deaD","evidences":[{"source":{"id":"MF_00964","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_00964","_id":"690b4c932ea0defb7a2f3186"},"code":"ECO:0000255","_id":"690b4c932ea0defb7a2f3185"},{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/15554978","id":"15554978","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/15554978","_id":"690b4c932ea0defb7a2f3188"},"code":"ECO:0000303","_id":"690b4c932ea0defb7a2f3187"}],"_id":"690b4c932ea0defb7a2f3184"},"synonyms":[{"value":"csdA","_id":"690b4c932ea0defb7a2f3189","evidences":[]},{"value":"mssB","_id":"690b4c932ea0defb7a2f318a","evidences":[]},{"value":"rhlD","_id":"690b4c932ea0defb7a2f318b","evidences":[]}],"olnNames":[{"value":"b3162","_id":"690b4c932ea0defb7a2f318c","evidences":[]},{"value":"JW5531","_id":"690b4c932ea0defb7a2f318d","evidences":[]}],"orfNames":[],"_id":"690b4c932ea0defb7a2f3183"}],"length":629,"name":"ATP-dependent RNA helicase DeaD","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions_counter":2,"released":"2026_06","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"regions":[{"start":565,"end":629,"reference_id":"29107486","reference_source":"pmid","reference_html":"Insights into the Structure of Dimeric RNA Helicase CsdA and Indispensable Role of Its C-Terminal Regions. <i> Xu L, Wang L, Peng J, Li F, Wu L, Zhang B, Lv M, Zhang J, Gong Q, Zhang R, Zuo X, Zhang Z, Wu J, Tang Y, Shi Y. </i> Structure, 2017","date":"2026-03-17T13:54:46.218Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04493r001","statement":[{"text":"The narrow proton chemical shift range of NHs in HSQC spectra demonstrate that the C-tail 65 residues (following CsdA_RBD) are intrinsically disordered (Figure S4).","type":"Results"}],"cross_refs":[{"db":"PDB","id":"5B88"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":565,"end":629,"reference_id":"29107486","reference_source":"pmid","reference_html":"Insights into the Structure of Dimeric RNA Helicase CsdA and Indispensable Role of Its C-Terminal Regions. <i> Xu L, Wang L, Peng J, Li F, Wu L, Zhang B, Lv M, Zhang J, Gong Q, Zhang R, Zuo X, Zhang Z, Wu J, Tang Y, Shi Y. </i> Structure, 2017","date":"2025-11-05T13:16:01.930Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04493r002","statement":[{"text":"The narrow proton chemical shift range of NHs in HSQC spectra demonstrate that the C-tail 65 residues (following CsdA_RBD) are intrinsically disordered (Figure S4).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-17T14:08:29.112Z"}}],"__v":0,"disorder_content":0.10333863275039745,"disprot_consensus":{"full":[{"start":565,"end":629,"type":"D"}],"Structural state":[{"start":565,"end":629,"type":"D"}],"Disorder function":[{"start":565,"end":629,"type":"F"}]}},{"acc":"P0A8P3","sequence":"MSRTIFCTFLQREAEGQDFQLYPGELGKRIYNEISKEAWAQWQHKQTMLINEKKLNMMNAEHRKLLEQEMVNFLFEGKEVHIEGYTPEDKK","creator":"xcastro","dataset":["Stress response proteins"],"date":"2025-11-05T15:28:32.264Z","disprot_id":"DP04494","features":{"pfam":[{"id":"PF04362","name":"Bacterial Fe(2+) trafficking","start":1,"end":87}]},"genes":[{"name":{"value":"yggX","_id":"690b6d232ea0defb7a2f319e","evidences":[]},"synonyms":[],"olnNames":[{"value":"b2962","_id":"690b6d232ea0defb7a2f319f","evidences":[]},{"value":"JW2929","_id":"690b6d232ea0defb7a2f31a0","evidences":[]}],"orfNames":[],"_id":"690b6d232ea0defb7a2f319d"}],"length":91,"name":"Probable Fe(2+)-trafficking protein","ncbi_taxon_id":83333,"organism":"Escherichia coli (strain K12)","regions_counter":2,"released":"2026_06","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"regions":[{"start":76,"end":91,"reference_id":"15883188","reference_source":"pmid","reference_html":"The solution structure of the oxidative stress-related protein YggX from Escherichia coli. <i> Osborne MJ, Siddiqui N, Landgraf D, Pomposiello PJ, Gehring K. </i> Protein Sci, 2005","date":"2025-12-15T17:57:43.439Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"PDB","id":"1YHD"},{"db":"BMRB","id":"6453"}],"region_id":"DP04494r001","sequence_construct":"MGSRTIFCTFLQREAEGQDFQLYPGELGKRIYNEISKEAWAQWQHKQTMLINEKKLNMMNAEHRKLLEQEMVNFLFEGKEVHIEGYTPEDKKLEHHHHHH","statement":[{"text":"YggX is a single domain protein (Fig. 1) consisting of two small N-terminal antiparallel β-sheets (T5-F7, E14-E16); a core body comprising three helices: helix α1 (G25-E34), helix α2 (K37-K54), helix α3 (A61-F74); and an unstructured C-terminal extension (E77-H96, plus the C-terminal 6xHis tag).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-12-15T17:58:06.877Z"}},{"start":76,"end":91,"reference_id":"15883188","reference_source":"pmid","reference_html":"The solution structure of the oxidative stress-related protein YggX from Escherichia coli. <i> Osborne MJ, Siddiqui N, Landgraf D, Pomposiello PJ, Gehring K. </i> Protein Sci, 2005","date":"2025-12-15T17:58:53.891Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"PDB","id":"1YHD"},{"db":"BMRB","id":"6453"}],"region_id":"DP04494r002","sequence_construct":"MGSRTIFCTFLQREAEGQDFQLYPGELGKRIYNEISKEAWAQWQHKQTMLINEKKLNMMNAEHRKLLEQEMVNFLFEGKEVHIEGYTPEDKKLEHHHHHH","statement":[{"text":"YggX is a single domain protein (Fig. 1) consisting of two small N-terminal antiparallel β-sheets (T5-F7, E14-E16); a core body comprising three helices: helix α1 (G25-E34), helix α2 (K37-K54), helix α3 (A61-F74); and an unstructured C-terminal extension (E77-H96, plus the C-terminal 6xHis tag).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-12-15T17:59:00.376Z"}}],"__v":0,"disorder_content":0.17582417582417584,"disprot_consensus":{"full":[{"start":76,"end":91,"type":"D"}],"Structural state":[{"start":76,"end":91,"type":"D"}],"Disorder function":[{"start":76,"end":91,"type":"F"}]}},{"acc":"B7LE66","sequence":"MIASKFGIGQQVRHSLLGYLGVVVDIDPVYSLSEPSPDELAVNDELRAAPWYHVVMEDDNGLPVHTYLAEAQLSSELQDEHPEQPSMDELAQTIRKQLQAPRLRN","creator":"xcastro","dataset":["Stress response proteins"],"date":"2025-11-05T16:02:29.784Z","disprot_id":"DP04501","features":{"pfam":[{"id":"PF08755","name":"Hemimethylated DNA-binding protein YccV like","start":5,"end":96}]},"genes":[{"name":{"value":"hspQ","evidences":[{"source":{"id":"MF_01194","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_01194","_id":"690b75162ea0defb7a2f31e7"},"code":"ECO:0000255","_id":"690b75162ea0defb7a2f31e6"}],"_id":"690b75162ea0defb7a2f31e5"},"synonyms":[],"olnNames":[{"value":"EC55989_1015","_id":"690b75162ea0defb7a2f31e8","evidences":[]}],"orfNames":[],"_id":"690b75162ea0defb7a2f31e4"}],"length":105,"name":"Heat shock protein HspQ","ncbi_taxon_id":585055,"organism":"Escherichia coli (strain 55989 / EAEC)","regions_counter":1,"released":"2026_06","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"regions":[{"start":30,"end":46,"reference_id":"29083032","reference_source":"pmid","reference_html":"X-ray crystal structure of Escherichia coli HspQ, a protein involved in the retardation of replication initiation. <i> Abe Y, Shioi S, Kita S, Nakata H, Maenaka K, Kohda D, Katayama T, Ueda T. </i> FEBS Lett, 2017","date":"2025-11-05T16:21:27.925Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue","statements":[{"type":"Methods","text":"The crystals of HspQ labeled with selenomethionine were obtained in 100 mm HEPES/NaOH buffer pH 7.5 containing 1.4 m ammonium sulfate, 4% (w/v) PEG400 and 150 mm MgCl2, and belong to the Rombohedral space group H32, with unit cell constants of a = 76.822 Å, b = 76.822 Å, c = 85.888 Å, α = β = 90°, γ = 120°."}]},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":56,"end":56,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":87,"end":87,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"5YCQ "}],"region_id":"DP04501r001","statement":[{"text":"No electron density was observed for Loop2 (residues 30–46), which was designated as a distal loop.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-12-15T17:54:10.627Z"}}],"__v":0,"disorder_content":0.1619047619047619,"disprot_consensus":{"full":[{"start":30,"end":46,"type":"D"}],"Structural state":[{"start":30,"end":46,"type":"D"}]}},{"acc":"Q7TN99","sequence":"MQDDLLMDKSKTQPQSQQQQRQQQQQQQQLQPEPGAAEAPSTPLSSEIPKPEDSSAVPALSPASAPPAPNGPDKMQMESPLLPGLSFHQPPQQPPPPQEPTAPGASLSPSFGSTWSTGTTNAVEDSFFQGITPVNGTMLFQNFPHHVNPVFGGTFSPQIGLAQTQHHQQPPPPAPQPPQPAQPPQAQPSQQRRSPASPSQAPYAQRSAAAYGHQPIMTSKPSSSSAVAAAAAAAAASSASSSWNTHQSVNAAWSAPSNPWGGLQAGRDPRRAVGVGVGVGVGVPSPLNPISPLKKPFSSNVIAPPKFPRAAPLTSKSWMEDNAFRTDNGNNLLPFQDRSRPYDTFNLHSLENSLMDMIRTDHEPLKGKHYPNSGPPMSFADIMWRNHFAGRMGINFHHPGTDNIMALNTRSYGRRRGRSSLFPFEDAFLDDSHGDQALSSGLSSPTRCQNGERVERYSRKVFVGGLPPDIDEDEITASFRRFGPLVVDWPHKAESKSYFPPKGYAFLLFQEESSVQALIDACLEEDGKLYLCVSSPTIKDKPVQIRPWNLSDSDFVMDGSQPLDPRKTIFVGGVPRPLRAVELAMIMDRLYGGVCYAGIDTDPELKYPKGAGRVAFSNQQSYIAAISARFVQLQHNDIDKRVEVKPYVLDDQMCDECQGTRCGGKFAPFFCANVTCLQYYCEYCWASIHSRAGREFHKPLVKEGGDRPRHVPFRWS","creator":"bjuhasz","dataset":["RNA-binding proteins"],"date":"2025-11-12T10:09:00.947Z","disprot_id":"DP04507","features":{"pfam":[{"id":"PF16366","name":"Cytoplasmic polyadenylation element-binding protein ZZ domain","start":640,"end":702},{"id":"PF16367","name":"RNA recognition motif","start":458,"end":547}]},"genes":[{"name":{"value":"Cpeb3","_id":"69145cbf2ea0defb7a2f3291","evidences":[]},"synonyms":[{"value":"Kiaa0940","_id":"69145cbf2ea0defb7a2f3292","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"69145cbf2ea0defb7a2f3290"}],"length":716,"name":"Cytoplasmic polyadenylation element-binding protein 3","ncbi_taxon_id":10090,"organism":"Mus musculus","regions_counter":5,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"regions":[{"start":101,"end":200,"reference_id":"40156755","reference_source":"pmid","reference_html":"Backbone resonance assignments of the CPEB3 [101-200] and CPEB3 [294-410]. <i> Saito H, Lee Y, Ueno M, Sekiyama N, So M, Furukawa A, Sugase K. </i> Biomol NMR Assign, 2025","date":"2025-11-12T11:05:25.348Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":"within normal range","value":298,"statements":[{"type":"Article","text":"NMR spectra were measured at 298 K using a 600 MHz AVANCE III HD spectrometer (Bruker) for CPEB3 [101–200] and an 800 MHz AVANCE III HD spectrometer (Bruker) for CPEB3 [294–410]."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"decreased","value":5.5,"statements":[{"type":"Figure","text":"Both spectra were acquired in 50 mM MES pH 5.5, 5% D2O."}]}],"cross_refs":[{"db":"BMRB","id":"26353"}],"region_id":"DP04507r001","statement":[{"text":"The 1H-15N HSQC signals of CPEB3 [101–200] and CPEB3 [294–410] were clustered in a narrow 1H region, which is characteristic of IDR.","type":"Article"},{"text":"The predicted secondary structure propensity of CPEB3 [101–200] indicated that this region is predominantly disordered.","type":"Article"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-20T16:01:43.278Z"}},{"start":294,"end":410,"reference_id":"40156755","reference_source":"pmid","reference_html":"Backbone resonance assignments of the CPEB3 [101-200] and CPEB3 [294-410]. <i> Saito H, Lee Y, Ueno M, Sekiyama N, So M, Furukawa A, Sugase K. </i> Biomol NMR Assign, 2025","date":"2025-11-12T11:04:15.148Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":"within normal range","value":298,"statements":[{"type":"Article","text":"NMR spectra were measured at 298 K using a 600 MHz AVANCE III HD spectrometer (Bruker) for CPEB3 [101–200] and an 800 MHz AVANCE III HD spectrometer (Bruker) for CPEB3 [294–410]."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"decreased","value":5.5,"statements":[{"type":"Figure","text":"Both spectra were acquired in 50 mM MES pH 5.5, 5% D2O."}]}],"cross_refs":[{"db":"BMRB","id":"26352"}],"region_id":"DP04507r002","statement":[{"text":"The 1H-15N HSQC signals of CPEB3 [101–200] and CPEB3 [294–410] were clustered in a narrow 1H region, which is characteristic of IDR.","type":"Article"},{"text":"In contrast, CPEB3 [294–410] tended to form partial α-helices at regions Leu347–Met357 and Phe379–Arg391. The relatively low SSP scores and broader linewidths observed for the regions Lys347–Arg359 and Phe379–His387 suggest that the α-helices in CPEB3 [294–410] are not stable and are only partially formed.","type":"Article"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-20T16:01:44.631Z"}}],"__v":0,"disorder_content":0.30307262569832405,"disprot_consensus":{"full":[{"start":101,"end":200,"type":"D"},{"start":294,"end":410,"type":"D"}],"Structural state":[{"start":101,"end":200,"type":"D"},{"start":294,"end":410,"type":"D"}]}},{"acc":"P11229","sequence":"MNTSAPPAVSPNITVLAPGKGPWQVAFIGITTGLLSLATVTGNLLVLISFKVNTELKTVNNYFLLSLACADLIIGTFSMNLYTTYLLMGHWALGTLACDLWLALDYVASNASVMNLLLISFDRYFSVTRPLSYRAKRTPRRAALMIGLAWLVSFVLWAPAILFWQYLVGERTVLAGQCYIQFLSQPIITFGTAMAAFYLPVTVMCTLYWRIYRETENRARELAALQGSETPGKGGGSSSSSERSQPGAEGSPETPPGRCCRCCRAPRLLQAYSWKEEEEEDEGSMESLTSSEGEEPGSEVVIKMPMVDPEAQAPTKQPPRSSPNTVKRPTKKGRDRAGKGQKPRGKEQLAKRKTFSLVKEKKAARTLSAILLAFILTWTPYNIMVLVSTFCKDCVPETLWELGYWLCYVNSTINPMCYALCNKAFRDTFRLLLLCRWDKRRWRKIPKRPGSVHRTPSRQC","creator":"rpancsa","dataset":[],"date":"2025-11-12T11:17:09.497Z","disprot_id":"DP04508","features":{"pfam":[{"id":"PF00001","name":"7 transmembrane receptor (rhodopsin family)","start":42,"end":418}]},"genes":[{"name":{"value":"CHRM1","_id":"69146cb52ea0defb7a2f329d","evidences":[]},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"69146cb52ea0defb7a2f329c"}],"length":460,"name":"Muscarinic acetylcholine receptor M1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":1,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":226,"end":353,"reference_id":"40178795","reference_source":"pmid","reference_html":"&lt;sup&gt;1&lt;/sup&gt;H, &lt;sup&gt;13&lt;/sup&gt;C and &lt;sup&gt;15&lt;/sup&gt;N resonance assignments of the third intracellular loop of the muscarinic acetylcholine receptor M1. <i> Wang J, Niu X, Jin C, Hu Y. </i> Biomol NMR Assign, 2025","date":"2025-11-12T12:08:09.727Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"conditions":[{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.7,"statements":[{"type":"Article","text":"The NMR samples were prepared in a buffer containing 20 mM HEPES, 0.1 M NaCl, 5 mM DTT (pH 6.7). 5% D2O was added into the samples for field lock and sodium\n2,2-dimethyl-2-silapentane-5 sulfonate (DSS) was added as the internal chemical shift reference."}]},{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Article","text":"All NMR experiments were recorded at 25 °C on a Bruker Avance 950 MHz spectrometer equipped with four RF channels and a triple-resonance cryoprobe with pulsed field gradients."}]}],"cross_refs":[{"db":"BMRB","id":"52865"}],"region_id":"DP04508r001","statement":[{"text":"The backbone amide resonances are clustered in the central region of the spectrum, mostly falling into the proton chemical shift range of 7.7–8.7 ppm, which is characteristic of intrinsic structural disorder.","type":"Article"},{"text":"The SSP scores are generally close to zero, with an average value of -0.13, which is consistent with a disordered conformation.","type":"Article"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-20T15:56:39.496Z"}}],"__v":0,"disorder_content":0.2782608695652174,"disprot_consensus":{"full":[{"start":226,"end":353,"type":"D"}],"Structural state":[{"start":226,"end":353,"type":"D"}]}},{"acc":"P41765","sequence":"MVDHISPRASPGPIRSSQTRRARKLRDSCTSCASSKVRCTKEKPACARCIERGLACQYMVSKRMGRNPRAPSPLDSTRRPSESLPSARSEQGLPAHNTYSTPHAHTQAHTHAHSHPQPHPQSHPQSNQPPHALPTPNGSSSVSAIFSHQSPPPPVETQGLGGDLAGQEQSTLSSLTVDSEFGGSLQSMEHGNHVDFLAESTGSLFDAFLEVGTPMIDPFLESAPLPPFQARYCCFSLALQTLTHLFPHAPLGCQLRLTDGEDSSCNLMTTDMVISGNKRATDAVRKILGCSCAQDGYLLSMVVLIVLKVLAWYAAAAGTQCTSTAAGGETNSGSCSNSPATVSSGCLTEERVLHLPSMMGEDCVDEEDQPRVAAQLVLSELHRVQSLVNLLAKRLQEGGDDAAGIPAHHPASPFSLLGFSGLEANLRHRLRAVSSDIIDYLHRE","creator":"rpancsa","dataset":[],"date":"2025-11-12T12:32:28.347Z","disprot_id":"DP04509","features":{"pfam":[{"id":"PF00172","name":"Fungal Zn(2)-Cys(6) binuclear cluster domain","start":28,"end":62},{"id":"PF08493","name":"Aflatoxin regulatory protein","start":232,"end":326}]},"genes":[{"name":{"value":"aflR","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/8074521","id":"8074521","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/8074521","_id":"69147e5c2ea0defb7a2f32a7"},"code":"ECO:0000303","_id":"69147e5c2ea0defb7a2f32a6"}],"_id":"69147e5c2ea0defb7a2f32a5"},"synonyms":[{"value":"afl-2","_id":"69147e5c2ea0defb7a2f32a8","evidences":[]},{"value":"afl2","_id":"69147e5c2ea0defb7a2f32a9","evidences":[]},{"value":"apa-2","_id":"69147e5c2ea0defb7a2f32aa","evidences":[]}],"olnNames":[],"orfNames":[{"value":"AFLA_139360","_id":"69147e5c2ea0defb7a2f32ab","evidences":[]}],"_id":"69147e5c2ea0defb7a2f32a4"}],"length":444,"name":"Aflatoxin biosynthesis regulatory protein","ncbi_taxon_id":332952,"organism":"Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167)","regions_counter":15,"released":"2026_06","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Eurotiomycetes","Eurotiomycetidae","Eurotiales","Aspergillaceae","Aspergillus","Aspergillus subgen. Circumdati"],"regions":[{"start":15,"end":28,"reference_id":"41053219","reference_source":"pmid","reference_html":"Conformational plasticity of disordered regions enables sequence-diverse DNA recognition by transcription factor AflR. <i> Wu S, Wang F, Zhou W, Zhang X, Zhan L, Zhang W, Wang W, Zhang W, Huang S, Fernie AR, Liu Z, Yan S. </i> Nat Commun, 2025","date":"2025-11-12T12:51:31.387Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"BMRB","id":"52862"}],"region_id":"DP04509r001","statement":[{"text":"The ¹H-¹⁵N HSQC spectrum exhibited a distinctive pattern wherein several peaks corresponding to the zinc cluster motif showed notable dispersion in the ¹H dimension (8.5–10 ppm, black labels), while the majority of signals displayed limited amide proton chemical shift dispersion, consistent with significant conformational flexibility (Fig. 1g). Chemical shift-based secondary structure propensity (SSP) analysis revealed strong α-helical propensity within the zinc cluster motif, while the remainder exhibited weak structural propensities, confirming the predominantly disordered nature of regions outside the zinc-binding core (Fig. 1h).","type":"Results"},{"text":"The zinc cluster motif is defined between residues 29 and 56 in the legend of Figure 1. The surrounding regions are disodered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-20T14:56:47.895Z"}},{"start":57,"end":79,"reference_id":"41053219","reference_source":"pmid","reference_html":"Conformational plasticity of disordered regions enables sequence-diverse DNA recognition by transcription factor AflR. <i> Wu S, Wang F, Zhou W, Zhang X, Zhan L, Zhang W, Wang W, Zhang W, Huang S, Fernie AR, Liu Z, Yan S. </i> Nat Commun, 2025","date":"2025-11-12T12:51:59.917Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"BMRB","id":"52862"}],"region_id":"DP04509r002","statement":[{"text":"The ¹H-¹⁵N HSQC spectrum exhibited a distinctive pattern wherein several peaks corresponding to the zinc cluster motif showed notable dispersion in the ¹H dimension (8.5–10 ppm, black labels), while the majority of signals displayed limited amide proton chemical shift dispersion, consistent with significant conformational flexibility (Fig. 1g). Chemical shift-based secondary structure propensity (SSP) analysis revealed strong α-helical propensity within the zinc cluster motif, while the remainder exhibited weak structural propensities, confirming the predominantly disordered nature of regions outside the zinc-binding core (Fig. 1h).","type":"Results"},{"text":"The zinc cluster motif is defined between residues 29 and 56 in the legend of Figure 1. The surrounding regions are disodered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-20T14:56:46.131Z"}},{"start":8,"end":28,"reference_id":"41053219","reference_source":"pmid","reference_html":"Conformational plasticity of disordered regions enables sequence-diverse DNA recognition by transcription factor AflR. <i> Wu S, Wang F, Zhou W, Zhang X, Zhan L, Zhang W, Wang W, Zhang W, Huang S, Fernie AR, Liu Z, Yan S. </i> Nat Commun, 2025","date":"2025-11-12T14:19:36.461Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04509r003","statement":[{"text":"Secondary structure analysis using far-UV circular dichroism (CD) spectroscopy revealed similar characteristics for fragments 8–98 and 15–79. Both displayed a minor peak at 222 nm, indicating limited helical content likely corresponding to the zinc cluster motif helices, along with a pronounced negative molar ellipticity minimum at 202 nm, suggesting a predominantly disordered structure (Fig. 1f). Notably, the relatively higher negative molar ellipticity observed at 202 nm for fragment 8–98 compared to fragment 15–79 suggests a more significant proportion of unstructured regions in the longer construct.","type":"Results"},{"text":"The zinc cluster motif is defined between residues 29 and 56 in the legend of Figure 1. The surrounding regions are disodered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-20T14:56:44.432Z"}},{"start":57,"end":98,"reference_id":"41053219","reference_source":"pmid","reference_html":"Conformational plasticity of disordered regions enables sequence-diverse DNA recognition by transcription factor AflR. <i> Wu S, Wang F, Zhou W, Zhang X, Zhan L, Zhang W, Wang W, Zhang W, Huang S, Fernie AR, Liu Z, Yan S. </i> Nat Commun, 2025","date":"2025-11-12T14:19:23.628Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04509r004","statement":[{"text":"Secondary structure analysis using far-UV circular dichroism (CD) spectroscopy revealed similar characteristics for fragments 8–98 and 15–79. Both displayed a minor peak at 222 nm, indicating limited helical content likely corresponding to the zinc cluster motif helices, along with a pronounced negative molar ellipticity minimum at 202 nm, suggesting a predominantly disordered structure (Fig. 1f). Notably, the relatively higher negative molar ellipticity observed at 202 nm for fragment 8–98 compared to fragment 15–79 suggests a more significant proportion of unstructured regions in the longer construct.","type":"Results"},{"text":"The zinc cluster motif is defined between residues 29 and 56 in the legend of Figure 1. The surrounding regions are disodered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-20T14:56:34.571Z"}},{"start":23,"end":28,"reference_id":"41053219","reference_source":"pmid","reference_html":"Conformational plasticity of disordered regions enables sequence-diverse DNA recognition by transcription factor AflR. <i> Wu S, Wang F, Zhou W, Zhang X, Zhan L, Zhang W, Wang W, Zhang W, Huang S, Fernie AR, Liu Z, Yan S. </i> Nat Commun, 2025","date":"2026-06-09T14:40:14.132Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0000976","term_name":"transcription cis-regulatory region binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"ec_go":"EXP","region_id":"DP04509r005","statement":[{"text":"Comparative analysis of NMR signal intensity reduction upon DNA binding with maximum contact ratios derived from simulations showed remarkable correlation in specific regions (Supplementary Fig. 23), identifying key interaction sites distributed from the N-terminal region (residues 23, 27, 28) to the C-terminal region (residues 61, 62, 62, 63, 65, 66).","type":"Results"},{"text":"The zinc cluster motif is defined between residues 29 and 56 in the legend of Figure 1. The surrounding regions are disodered.","type":"Curator statement"}],"term_comment":"Note that this term is meant to also capture non-specific binding to regulatory regions. Also, to minimize ambiguity in the use of the word \"promoter\" in GO, we have chosen the phrase \"transcription regulatory region\" to refer to all of the regulatory regions. Regulatory regions in the DNA which control initiation may include the \"core promoter\" where the basal transcription machinery binds, the \"core promoter proximal region\" where regulatory factors other than the basal machinery bind. There are also additional regulatory regions, in both the DNA and the RNA transcript, which regulate elongation or termination of transcription.","term_def":"\"Binding to a specific sequence of DNA that is part of a regulatory region that controls transcription of that section of the DNA. The transcribed region might be described as a gene, cistron, or operon.\" [GOC:txnOH]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-09T14:46:00.199Z"}},{"start":61,"end":66,"reference_id":"41053219","reference_source":"pmid","reference_html":"Conformational plasticity of disordered regions enables sequence-diverse DNA recognition by transcription factor AflR. <i> Wu S, Wang F, Zhou W, Zhang X, Zhan L, Zhang W, Wang W, Zhang W, Huang S, Fernie AR, Liu Z, Yan S. </i> Nat Commun, 2025","date":"2026-06-09T14:40:34.521Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0000976","term_name":"transcription cis-regulatory region binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"ec_go":"EXP","region_id":"DP04509r006","statement":[{"text":"Comparative analysis of NMR signal intensity reduction upon DNA binding with maximum contact ratios derived from simulations showed remarkable correlation in specific regions (Supplementary Fig. 23), identifying key interaction sites distributed from the N-terminal region (residues 23, 27, 28) to the C-terminal region (residues 61, 62, 62, 63, 65, 66).","type":"Results"},{"text":"The zinc cluster motif is defined between residues 29 and 56 in the legend of Figure 1. The surrounding regions are disodered.","type":"Curator statement"}],"term_comment":"Note that this term is meant to also capture non-specific binding to regulatory regions. Also, to minimize ambiguity in the use of the word \"promoter\" in GO, we have chosen the phrase \"transcription regulatory region\" to refer to all of the regulatory regions. Regulatory regions in the DNA which control initiation may include the \"core promoter\" where the basal transcription machinery binds, the \"core promoter proximal region\" where regulatory factors other than the basal machinery bind. There are also additional regulatory regions, in both the DNA and the RNA transcript, which regulate elongation or termination of transcription.","term_def":"\"Binding to a specific sequence of DNA that is part of a regulatory region that controls transcription of that section of the DNA. The transcribed region might be described as a gene, cistron, or operon.\" [GOC:txnOH]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-09T14:46:01.242Z"}},{"start":61,"end":66,"reference_id":"41053219","reference_source":"pmid","reference_html":"Conformational plasticity of disordered regions enables sequence-diverse DNA recognition by transcription factor AflR. <i> Wu S, Wang F, Zhou W, Zhang X, Zhan L, Zhang W, Wang W, Zhang W, Huang S, Fernie AR, Liu Z, Yan S. </i> Nat Commun, 2025","date":"2026-06-09T14:40:44.494Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0000976","term_name":"transcription cis-regulatory region binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001247","ec_ontology":"ECO","ec_name":"point mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"ec_go":"IMP","region_id":"DP04509r007","statement":[{"text":"Comparative analysis of NMR signal intensity reduction upon DNA binding with maximum contact ratios derived from simulations showed remarkable correlation in specific regions (Supplementary Fig. 23), identifying key interaction sites distributed from the N-terminal region (residues 23, 27, 28) to the C-terminal region (residues 61, 62, 62, 63, 65, 66).","type":"Results"},{"text":"Notably, C-terminal mutations displayed both the most severe and sequence-dependent effects on complex formation. R63A showed ~1.8-fold variation in KD-app values between ver1 (39.5 ± 16.4 μM²) and norA (72.3 ± 16.5 μM²). Most dramatically, R66A exhibited a ~3.4-fold difference between its impact on vbs (58.1 ± 22.6 μM²) and norA (197.9 ± 196.7 μM²), with substantially higher variability in norA measurements. G65A almost abolished binding to all promoters, highlighting its universal importance.","type":"Results"}],"term_comment":"Note that this term is meant to also capture non-specific binding to regulatory regions. Also, to minimize ambiguity in the use of the word \"promoter\" in GO, we have chosen the phrase \"transcription regulatory region\" to refer to all of the regulatory regions. Regulatory regions in the DNA which control initiation may include the \"core promoter\" where the basal transcription machinery binds, the \"core promoter proximal region\" where regulatory factors other than the basal machinery bind. There are also additional regulatory regions, in both the DNA and the RNA transcript, which regulate elongation or termination of transcription.","term_def":"\"Binding to a specific sequence of DNA that is part of a regulatory region that controls transcription of that section of the DNA. The transcribed region might be described as a gene, cistron, or operon.\" [GOC:txnOH]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg63Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"R63A showed ~1.8-fold variation in KD-app values between ver1 (39.5 ± 16.4 μM²) and norA (72.3 ± 16.5 μM²)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly65Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"G65A almost abolished binding to all promoters, highlighting its universal importance."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg66Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"Most dramatically, R66A exhibited a ~3.4-fold difference between its impact on vbs (58.1 ± 22.6 μM²) and norA (197.9 ± 196.7 μM²), with substantially higher variability in norA measurements."}]}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sequence_construct":"RSSQTRRARKLRDSCTSCASSKVRCTKEKPACARCIERGLACQYMVSKRMGRNPRAPSPLDSTRR","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-09T14:46:02.291Z"}},{"start":23,"end":28,"reference_id":"41053219","reference_source":"pmid","reference_html":"Conformational plasticity of disordered regions enables sequence-diverse DNA recognition by transcription factor AflR. <i> Wu S, Wang F, Zhou W, Zhang X, Zhan L, Zhang W, Wang W, Zhang W, Huang S, Fernie AR, Liu Z, Yan S. </i> Nat Commun, 2025","date":"2026-06-09T14:40:57.840Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0000976","term_name":"transcription cis-regulatory region binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001247","ec_ontology":"ECO","ec_name":"point mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"ec_go":"IMP","region_id":"DP04509r008","statement":[{"text":"Comparative analysis of NMR signal intensity reduction upon DNA binding with maximum contact ratios derived from simulations showed remarkable correlation in specific regions (Supplementary Fig. 23), identifying key interaction sites distributed from the N-terminal region (residues 23, 27, 28) to the C-terminal region (residues 61, 62, 62, 63, 65, 66).","type":"Results"},{"text":"N-terminal mutations (R23A, D27A) showed moderate effects on binding (1.2–10.3 μM²), with R23A slightly enhanced binding to vbs and norA while reducing affinity for ver1.","type":"Results"}],"term_comment":"Note that this term is meant to also capture non-specific binding to regulatory regions. Also, to minimize ambiguity in the use of the word \"promoter\" in GO, we have chosen the phrase \"transcription regulatory region\" to refer to all of the regulatory regions. Regulatory regions in the DNA which control initiation may include the \"core promoter\" where the basal transcription machinery binds, the \"core promoter proximal region\" where regulatory factors other than the basal machinery bind. There are also additional regulatory regions, in both the DNA and the RNA transcript, which regulate elongation or termination of transcription.","term_def":"\"Binding to a specific sequence of DNA that is part of a regulatory region that controls transcription of that section of the DNA. The transcribed region might be described as a gene, cistron, or operon.\" [GOC:txnOH]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg23Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"N-terminal mutations (R23A, D27A) showed moderate effects on binding (1.2–10.3 μM²), with R23A slightly enhanced binding to vbs and norA while reducing affinity for ver1."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp27Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"N-terminal mutations (R23A, D27A) showed moderate effects on binding (1.2–10.3 μM²), with R23A slightly enhanced binding to vbs and norA while reducing affinity for ver1."}]}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sequence_construct":"RSSQTRRARKLRDSCTSCASSKVRCTKEKPACARCIERGLACQYMVSKRMGRNPRAPSPLDSTRR","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-09T14:46:03.633Z"}},{"start":58,"end":79,"reference_id":"41053219","reference_source":"pmid","reference_html":"Conformational plasticity of disordered regions enables sequence-diverse DNA recognition by transcription factor AflR. <i> Wu S, Wang F, Zhou W, Zhang X, Zhan L, Zhang W, Wang W, Zhang W, Huang S, Fernie AR, Liu Z, Yan S. </i> Nat Commun, 2025","date":"2026-06-09T14:41:09.839Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0000976","term_name":"transcription cis-regulatory region binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001175","ec_ontology":"ECO","ec_name":"deletion mutation phenotypic evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"ec_go":"IMP","region_id":"DP04509r009","statement":[{"text":"To further assess the functional importance of terminal regions in DNA recognition, we tested additional truncation constructs lacking either the C-terminal region (15–57) or both terminal regions (28–57) for their ability to bind promoter DNA. While the DBD (15–79) formed stable complexes with all three promoters, removal of either the C-terminal region alone or both terminal regions completely abolished DNA binding.","type":"Results"}],"term_comment":"Note that this term is meant to also capture non-specific binding to regulatory regions. Also, to minimize ambiguity in the use of the word \"promoter\" in GO, we have chosen the phrase \"transcription regulatory region\" to refer to all of the regulatory regions. Regulatory regions in the DNA which control initiation may include the \"core promoter\" where the basal transcription machinery binds, the \"core promoter proximal region\" where regulatory factors other than the basal machinery bind. There are also additional regulatory regions, in both the DNA and the RNA transcript, which regulate elongation or termination of transcription.","term_def":"\"Binding to a specific sequence of DNA that is part of a regulatory region that controls transcription of that section of the DNA. The transcribed region might be described as a gene, cistron, or operon.\" [GOC:txnOH]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Tyr58_Pro79del","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To further assess the functional importance of terminal regions in DNA recognition, we tested additional truncation constructs lacking either the C-terminal region (15–57) or both terminal regions (28–57) for their ability to bind promoter DNA. While the DBD (15–79) formed stable complexes with all three promoters, removal of either the C-terminal region alone or both terminal regions completely abolished DNA binding."}]}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sequence_construct":"RSSQTRRARKLRDSCTSCASSKVRCTKEKPACARCIERGLACQYMVSKRMGRNPRAPSPLDSTRR","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-09T14:46:04.544Z"}},{"start":15,"end":25,"reference_id":"41053219","reference_source":"pmid","reference_html":"Conformational plasticity of disordered regions enables sequence-diverse DNA recognition by transcription factor AflR. <i> Wu S, Wang F, Zhou W, Zhang X, Zhan L, Zhang W, Wang W, Zhang W, Huang S, Fernie AR, Liu Z, Yan S. </i> Nat Commun, 2025","date":"2026-06-09T14:41:23.326Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0000976","term_name":"transcription cis-regulatory region binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"ec_go":"EXP","region_id":"DP04509r012","statement":[{"text":"Constructs 15–69 (C-terminal truncation) and 26–79 (N-terminal truncation) had previously demonstrated substantially reduced binding affinities for the ver1 promoter compared to the intact DBD (Fig. 1d, e). These findings provide direct experimental evidence that both terminal regions, particularly the C-terminus, are essential for DNA recognition.","type":"Results"},{"text":"Reduced DNA-binding of the truncated versions was shown by analytical gel filtration chromatography and FCS titrations. The baseline was the WT 15-79 construct, the truncated ones were evaluated in comparison to this one.","type":"Curator statement"}],"term_comment":"Note that this term is meant to also capture non-specific binding to regulatory regions. Also, to minimize ambiguity in the use of the word \"promoter\" in GO, we have chosen the phrase \"transcription regulatory region\" to refer to all of the regulatory regions. Regulatory regions in the DNA which control initiation may include the \"core promoter\" where the basal transcription machinery binds, the \"core promoter proximal region\" where regulatory factors other than the basal machinery bind. There are also additional regulatory regions, in both the DNA and the RNA transcript, which regulate elongation or termination of transcription.","term_def":"\"Binding to a specific sequence of DNA that is part of a regulatory region that controls transcription of that section of the DNA. The transcribed region might be described as a gene, cistron, or operon.\" [GOC:txnOH]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-09T14:46:05.643Z"}},{"start":70,"end":79,"reference_id":"41053219","reference_source":"pmid","reference_html":"Conformational plasticity of disordered regions enables sequence-diverse DNA recognition by transcription factor AflR. <i> Wu S, Wang F, Zhou W, Zhang X, Zhan L, Zhang W, Wang W, Zhang W, Huang S, Fernie AR, Liu Z, Yan S. </i> Nat Commun, 2025","date":"2026-06-09T14:45:29.855Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0000976","term_name":"transcription cis-regulatory region binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"ec_go":"EXP","region_id":"DP04509r013","statement":[{"text":"Constructs 15–69 (C-terminal truncation) and 26–79 (N-terminal truncation) had previously demonstrated substantially reduced binding affinities for the ver1 promoter compared to the intact DBD (Fig. 1d, e). These findings provide direct experimental evidence that both terminal regions, particularly the C-terminus, are essential for DNA recognition.","type":"Results"},{"text":"Reduced DNA-binding of the truncated versions was shown by analytical gel filtration chromatography and FCS titrations. The baseline was the WT 15-79 construct, the truncated ones were evaluated in comparison to this one.","type":"Curator statement"}],"term_comment":"Note that this term is meant to also capture non-specific binding to regulatory regions. Also, to minimize ambiguity in the use of the word \"promoter\" in GO, we have chosen the phrase \"transcription regulatory region\" to refer to all of the regulatory regions. Regulatory regions in the DNA which control initiation may include the \"core promoter\" where the basal transcription machinery binds, the \"core promoter proximal region\" where regulatory factors other than the basal machinery bind. There are also additional regulatory regions, in both the DNA and the RNA transcript, which regulate elongation or termination of transcription.","term_def":"\"Binding to a specific sequence of DNA that is part of a regulatory region that controls transcription of that section of the DNA. The transcribed region might be described as a gene, cistron, or operon.\" [GOC:txnOH]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-09T14:46:07.278Z"}},{"start":15,"end":25,"reference_id":"41053219","reference_source":"pmid","reference_html":"Conformational plasticity of disordered regions enables sequence-diverse DNA recognition by transcription factor AflR. <i> Wu S, Wang F, Zhou W, Zhang X, Zhan L, Zhang W, Wang W, Zhang W, Huang S, Fernie AR, Liu Z, Yan S. </i> Nat Commun, 2025","date":"2026-06-09T14:45:41.960Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0000976","term_name":"transcription cis-regulatory region binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006335","ec_ontology":"ECO","ec_name":"fluorescence correlation spectroscopy evidence","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04509r014","statement":[{"text":"Constructs 15–69 (C-terminal truncation) and 26–79 (N-terminal truncation) had previously demonstrated substantially reduced binding affinities for the ver1 promoter compared to the intact DBD (Fig. 1d, e). These findings provide direct experimental evidence that both terminal regions, particularly the C-terminus, are essential for DNA recognition.","type":"Results"},{"text":"Reduced DNA-binding of the truncated versions was shown by analytical gel filtration chromatography and FCS titrations. The baseline was the WT 15-79 construct, the truncated ones were evaluated in comparison to this one.","type":"Curator statement"}],"term_comment":"Note that this term is meant to also capture non-specific binding to regulatory regions. Also, to minimize ambiguity in the use of the word \"promoter\" in GO, we have chosen the phrase \"transcription regulatory region\" to refer to all of the regulatory regions. Regulatory regions in the DNA which control initiation may include the \"core promoter\" where the basal transcription machinery binds, the \"core promoter proximal region\" where regulatory factors other than the basal machinery bind. There are also additional regulatory regions, in both the DNA and the RNA transcript, which regulate elongation or termination of transcription.","term_def":"\"Binding to a specific sequence of DNA that is part of a regulatory region that controls transcription of that section of the DNA. The transcribed region might be described as a gene, cistron, or operon.\" [GOC:txnOH]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-09T14:46:08.752Z"}},{"start":70,"end":79,"reference_id":"41053219","reference_source":"pmid","reference_html":"Conformational plasticity of disordered regions enables sequence-diverse DNA recognition by transcription factor AflR. <i> Wu S, Wang F, Zhou W, Zhang X, Zhan L, Zhang W, Wang W, Zhang W, Huang S, Fernie AR, Liu Z, Yan S. </i> Nat Commun, 2025","date":"2026-06-09T14:45:53.110Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0000976","term_name":"transcription cis-regulatory region binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006335","ec_ontology":"ECO","ec_name":"fluorescence correlation spectroscopy evidence","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04509r015","statement":[{"text":"Constructs 15–69 (C-terminal truncation) and 26–79 (N-terminal truncation) had previously demonstrated substantially reduced binding affinities for the ver1 promoter compared to the intact DBD (Fig. 1d, e). These findings provide direct experimental evidence that both terminal regions, particularly the C-terminus, are essential for DNA recognition.","type":"Results"},{"text":"Reduced DNA-binding of the truncated versions was shown by analytical gel filtration chromatography and FCS titrations. The baseline was the WT 15-79 construct, the truncated ones were evaluated in comparison to this one.","type":"Curator statement"}],"term_comment":"Note that this term is meant to also capture non-specific binding to regulatory regions. Also, to minimize ambiguity in the use of the word \"promoter\" in GO, we have chosen the phrase \"transcription regulatory region\" to refer to all of the regulatory regions. Regulatory regions in the DNA which control initiation may include the \"core promoter\" where the basal transcription machinery binds, the \"core promoter proximal region\" where regulatory factors other than the basal machinery bind. There are also additional regulatory regions, in both the DNA and the RNA transcript, which regulate elongation or termination of transcription.","term_def":"\"Binding to a specific sequence of DNA that is part of a regulatory region that controls transcription of that section of the DNA. The transcribed region might be described as a gene, cistron, or operon.\" [GOC:txnOH]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-09T14:46:09.790Z"}}],"__v":0,"disorder_content":0.14189189189189189,"disprot_consensus":{"full":[{"start":8,"end":28,"type":"D"},{"start":57,"end":98,"type":"D"}],"Structural state":[{"start":8,"end":28,"type":"D"},{"start":57,"end":98,"type":"D"}],"Molecular function":[{"start":15,"end":28,"type":"F"},{"start":58,"end":79,"type":"F"}]}},{"acc":"Q99683","sequence":"MSTEADEGITFSVPPFAPSGFCTIPEGGICRRGGAAAVGEGEEHQLPPPPPGSFWNVESAAAPGIGCPAATSSSSATRGRGSSVGGGSRRTTVAYVINEASQGQLVVAESEALQSLREACETVGATLETLHFGKLDFGETTVLDRFYNADIAVVEMSDAFRQPSLFYHLGVRESFSMANNIILYCDTNSDSLQSLKEIICQKNTMCTGNYTFVPYMITPHNKVYCCDSSFMKGLTELMQPNFELLLGPICLPLVDRFIQLLKVAQASSSQYFRESILNDIRKARNLYTGKELAAELARIRQRVDNIEVLTADIVINLLLSYRDIQDYDSIVKLVETLEKLPTFDLASHHHVKFHYAFALNRRNLPGDRAKALDIMIPMVQSEGQVASDMYCLVGRIYKDMFLDSNFTDTESRDHGASWFKKAFESEPTLQSGINYAVLLLAAGHQFESSFELRKVGVKLSSLLGKKGNLEKLQSYWEVGFFLGASVLANDHMRVIQASEKLFKLKTPAWYLKSIVETILIYKHFVKLTTEQPVAKQELVDFWMDFLVEATKTDVTVVRFPVLILEPTKIYQPSYLSINNEVEEKTISIWHVLPDDKKGIHEWNFSASSVRGVSISKFEERCCFLYVLHNSDDFQIYFCTELHCKKFFEMVNTITEEKGRSTEEGDCESDLLEYDYEYDENGDRVVLGKGTYGIVYAGRDLSNQVRIAIKEIPERDSRYSQPLHEEIALHKHLKHKNIVQYLGSFSENGFIKIFMEQVPGGSLSALLRSKWGPLKDNEQTIGFYTKQILEGLKYLHDNQIVHRDIKGDNVLINTYSGVLKISDFGTSKRLAGINPCTETFTGTLQYMAPEIIDKGPRGYGKAADIWSLGCTIIEMATGKPPFYELGEPQAAMFKVGMFKVHPEIPESMSAEAKAFILKCFEPDPDKRACANDLLVDEFLKVSSKKKKTQPKLSALSAGSNEYLRSISLPVPVLVEDTSSSSEYGSVSPDTELKVDPFSFKTRAKSCGERDVKGIRTLFLGIPDENFEDHSAPPSPEEKDSGFFMLRKDSERRATLHRILTEDQDKIVRNLMESLAQGAEEPKLKWEHITTLIASLREFVRSTDRKIIATTLSKLKLELDFDSHGISQVQVVLFGFQDAVNKVLRNHNIKPHWMFALDSIIRKAVQTAITILVPELRPHFSLASESDTADQEDLDVEDDHEEQPSNQTVRRPQAVIEDAVATSGVSTLSSTVSHDSQSAHRSLNVQLGRMKIETNRLLEELVRKEKELQALLHRAIEEKDQEIKHLKLKSQPIEIPELPVFHLNSSGTNTEDSELTDWLRVNGADEDTISRFLAEDYTLLDVLYYVTRDDLKCLRLRGGMLCTLWKAIIDFRNKQT","creator":"tcordero","dataset":["Stress response proteins"],"date":"2025-11-20T16:46:49.545Z","disprot_id":"DP04510","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":685,"end":937},{"id":"PF13281","name":"MAP3K TRAFs-binding domain","start":165,"end":545},{"id":"PF19039","name":"ASK kinase PH domain","start":556,"end":653},{"id":"PF20302","name":"HisK-N-like globin domain of the ASK signalosome","start":1042,"end":1173},{"id":"PF20309","name":"Deoxyribohydrolase (DRHyd) domain of the ASK signalosome","start":115,"end":150}]},"genes":[{"name":{"value":"MAP3K5","_id":"691f45f92ea0defb7a2f3345","evidences":[]},"synonyms":[{"value":"ASK1","_id":"691f45f92ea0defb7a2f3346","evidences":[]},{"value":"MAPKKK5","_id":"691f45f92ea0defb7a2f3347","evidences":[]},{"value":"MEKK5","_id":"691f45f92ea0defb7a2f3348","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"691f45f92ea0defb7a2f3344"}],"length":1374,"name":"Mitogen-activated protein kinase kinase kinase 5","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":4,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":228,"end":245,"reference_id":"38536085","reference_source":"pmid","reference_html":"The cryo-EM structure of ASK1 reveals an asymmetric architecture allosterically modulated by TRX1. <i> Honzejkova K, Kosek D, Obsilova V, Obsil T. </i> Elife, 2024","date":"2026-03-26T14:16:09.615Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"8QGY"}],"region_id":"DP04510r001","statement":[{"text":"In addition, this region appears to be very flexible as no interpretable density was found for residues 228–245 in both TBDs.","type":"Results"},{"text":"This result is consistent with a previous NMR characterization of isolated TBD, which showed that this domain retains substantial conformational plasticity (Psenakova et al., 2020).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-26T14:16:11.775Z"}},{"start":655,"end":670,"reference_id":"38536085","reference_source":"pmid","reference_html":"The cryo-EM structure of ASK1 reveals an asymmetric architecture allosterically modulated by TRX1. <i> Honzejkova K, Kosek D, Obsilova V, Obsil T. </i> Elife, 2024","date":"2026-03-26T14:15:16.919Z","curator_id":"tcordero","curator_name":"Trinidad Cordero","curator_orcid":"0000-0003-4991-7170","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"8QGY"}],"region_id":"DP04510r003","statement":[{"text":"Significant protection was also observed in residues 655–670, which form a linker connecting PH and KD (Figure 4A). This linker should be quite flexible as no interpretable density was found in this region, in either protomer.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-26T14:15:24.904Z"}},{"start":228,"end":245,"reference_id":"38536085","reference_source":"pmid","reference_html":"The cryo-EM structure of ASK1 reveals an asymmetric architecture allosterically modulated by TRX1. <i> Honzejkova K, Kosek D, Obsilova V, Obsil T. </i> Elife, 2024","date":"2026-03-20T14:50:35.522Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"8QGY"}],"region_id":"DP04510r004","statement":[{"text":"Significant protection was also observed in residues 655–670, which form a linker connecting PH and KD (Figure 4A).","type":"Results"},{"text":"In addition, this region appears to be very flexible as no interpretable density was found for residues 228–245 in both TBDs.","type":"Results"}]}],"__v":0,"disorder_content":0.024745269286754003,"disprot_consensus":{"full":[{"start":228,"end":245,"type":"D"},{"start":655,"end":670,"type":"D"}],"Structural state":[{"start":228,"end":245,"type":"D"},{"start":655,"end":670,"type":"D"}],"Disorder function":[{"start":228,"end":245,"type":"F"}]}},{"acc":"P0C6L6","sequence":"MSRSESRKNRGGREEILEQWVAGRKKLEELERDLRKTKKKLKKIEDENPWLGNIKGILGKKDKDGEGAPPAKRARTDQMEVDSGPRKRPLRGGFTDKERQDHRRRKALENKKKQLSAGGKNLSKEEEEELRRLTEEDERRERRVAGPPVGGVIPLEGGSRGAPGGGFVPSLQGVPESPFSRTGEGLDIRGNRGFPWDILFPADPPFSPQSCRPQ","creator":"xcastro","dataset":["Viral proteins","RNA-binding proteins"],"date":"2025-12-04T13:22:15.163Z","disprot_id":"DP04511","features":{"pfam":[{"id":"PF01517","name":"Hepatitis delta virus delta antigen","start":1,"end":174}]},"genes":[],"length":214,"name":"Large delta antigen","ncbi_taxon_id":10423,"organism":"Hepatitis delta virus genotype I (isolate Italian)","regions_counter":5,"released":"2026_06","taxonomy":["Viruses","Ribozyviria","Kolmioviridae","Deltavirus","Hepatitis delta virus"],"regions":[{"start":56,"end":95,"reference_id":"40324079","reference_source":"pmid","reference_html":"Structure and nucleic acid interactions of the S&lt;sup&gt;Δ60&lt;/sup&gt; domain of the hepatitis delta virus small antigen. <i> Yang Y, Delcourte L, van Belleghem C, Fonte S, Gerard K, Baconnais S, Callon M, Le Cam E, Fogeron ML, Levrero M, Faivre-Moskalenko C, Böckmann A, Lecoq L. </i> Proc Natl Acad Sci U S A, 2025","date":"2025-12-04T13:29:47.711Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"9FLG"},{"db":"BMRB","id":"51340"}],"region_id":"DP04511r001","statement":[{"text":"The structure reveals two disordered domains, separated by two well-defined α-helices, α1 (residues D96-A117) and α2 (residues K124-R142), forming a helix–loop–helix (HLH) motif (Fig. 2A and SI Appendix, Fig. S2A).","type":"Results"},{"text":"Comparison with a solution-state 2D SOFAST experiment indicates that the resonances that belong to the disordered domain are observed also in the INEPT spectrum (Fig. 3), confirming that they remain dynamic in the full-length protein.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-20T13:46:32.092Z"}},{"start":143,"end":195,"reference_id":"40324079","reference_source":"pmid","reference_html":"Structure and nucleic acid interactions of the S&lt;sup&gt;Δ60&lt;/sup&gt; domain of the hepatitis delta virus small antigen. <i> Yang Y, Delcourte L, van Belleghem C, Fonte S, Gerard K, Baconnais S, Callon M, Le Cam E, Fogeron ML, Levrero M, Faivre-Moskalenko C, Böckmann A, Lecoq L. </i> Proc Natl Acad Sci U S A, 2025","date":"2025-12-04T13:31:16.526Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"9FLG"},{"db":"BMRB","id":"51340"}],"region_id":"DP04511r002","statement":[{"text":"The structure reveals two disordered domains, separated by two well-defined α-helices, α1 (residues D96-A117) and α2 (residues K124-R142), forming a helix–loop–helix (HLH) motif (Fig. 2A and SI Appendix, Fig. S2A).","type":"Results"},{"text":"Comparison with a solution-state 2D SOFAST experiment indicates that the resonances that belong to the disordered domain are observed also in the INEPT spectrum (Fig. 3), confirming that they remain dynamic in the full-length protein.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-20T13:46:31.238Z"}}],"__v":0,"disorder_content":0.43457943925233644,"disprot_consensus":{"full":[{"start":56,"end":95,"type":"D"},{"start":143,"end":195,"type":"D"}],"Structural state":[{"start":56,"end":95,"type":"D"},{"start":143,"end":195,"type":"D"}]}},{"acc":"P0DTC6","sequence":"MFHLVDFQVTIAEILLIIMRTFKVSIWNLDYIINLIIKNLSKSLTENKYSQLDEEQPMEID","creator":"xcastro","dataset":["Viral proteins"],"date":"2025-12-10T14:11:40.744Z","disprot_id":"DP04516","features":{"pfam":[{"id":"PF12133","name":"Betacoronavirus NS6 protein","start":1,"end":61}]},"genes":[{"synonyms":[],"olnNames":[],"orfNames":[{"value":"6","_id":"69397f9c38549a2e1d36c9f3","evidences":[]}],"_id":"69397f9c38549a2e1d36c9f2"}],"length":61,"name":"ORF6 protein","ncbi_taxon_id":2697049,"organism":"Severe acute respiratory syndrome coronavirus 2","regions_counter":25,"released":"2026_06","taxonomy":["Viruses","Riboviria","Orthornavirae","Pisuviricota","Pisoniviricetes","Nidovirales","Cornidovirineae","Coronaviridae","Orthocoronavirinae","Betacoronavirus","Sarbecovirus","Severe acute respiratory syndrome coronavirus"],"regions":[{"start":41,"end":52,"reference_id":"35096974","reference_source":"pmid","reference_html":"Molecular Mechanism of SARS-CoVs Orf6 Targeting the Rae1-Nup98 Complex to Compete With mRNA Nuclear Export. <i> Li T, Wen Y, Guo H, Yang T, Yang H, Ji X. </i> Front Mol Biosci, 2021","date":"2025-12-16T07:22:18.517Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"7VPH"}],"region_id":"DP04516r001","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P78406"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P52948"}],"statement":[{"text":"A 21-mer peptide (residues 41–61) of SARS-CoV-2 Orf6, a 22-mer peptide (residues 42–63) of SARS-CoV-1 Orf6 and the M58A/M58R mutants of SARS-CoV-2 Orf6CTT were synthesized from KS-V Peptide Co., Hefei, China.","type":"Methods"},{"text":"The composite omit map of two structures unequivocally showed that residues 53–61 of SARS-CoV-2 Orf6 and residues 50–62 of SARS-CoV-1 Orf6 accommodate the same site of Rae1 (Supplementary Figure S2).","type":"Results"},{"text":"The electron densities for other residues in peptides of Orf6CTT were poorly defined that no atoms could be positioned, suggesting a highly flexible region of the peptide without any close contact to Rae1 or Nup98.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2025-12-23T15:25:45.304Z"}},{"start":41,"end":61,"reference_id":"39340152","reference_source":"pmid","reference_html":"An integrative characterization of proline cis and trans conformers in a disordered peptide. <i> Pettitt AJ, Shukla VK, Figueiredo AM, Newton LS, McCarthy S, Tabor AB, Heller GT, Lorenz CD, Hansen DF. </i> Biophys J, 2024","date":"2025-12-23T14:23:31.782Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"cross_refs":[{"db":"BMRB","id":"52459"}],"region_id":"DP04516r002","statement":[{"text":"2D 1H-15N HSQC spectra show sharp resonances with a limited chemical shift dispersion in the 1HN dimension, suggesting that these resonances arise from disordered residues (Fig. 2 A).","type":"Results"},{"text":"The 15N R1 and R2 relaxation rates report on protein motions occurring at timescales faster than the effective rotational correlation time, which is usually on the nanosecond timescale for disordered proteins. The rates obtained for the ORF6CTR cis-P57 and trans-P57 subensembles are very similar, and both show the expected bell shape for a random coil disordered state (Figs. 5, A and B and S16, A and B) (31,75).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":41,"end":61,"reference_id":"35096974","reference_source":"pmid","reference_html":"Molecular Mechanism of SARS-CoVs Orf6 Targeting the Rae1-Nup98 Complex to Compete With mRNA Nuclear Export. <i> Li T, Wen Y, Guo H, Yang T, Yang H, Ji X. </i> Front Mol Biosci, 2021","date":"2025-12-23T14:47:01.032Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140272","term_name":"exogenous protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P78406","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P52948","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04516r003","statement":[{"text":"The results showed that binding of each SARS-CoV Orf6CTT to the Rae1–Nup98GLEBS complex occurred at a 1:1 ratio in the nanomolar range (K d = 277.8 nM for SARS-CoV-1 Orf6 and K d = 141.6 nM for SARS-CoV-2 Orf6), which is approximately 50- to 100-fold higher than that for a 14-mer poly(U) ssRNA binding to Rae1–Nup98GLEBS (Figure 1B).","type":"Results"}],"term_comment":"Note that as GO captures normal processes, it may be that exogenous proteins interactions are normal for one of the participating species but not the other. Therefore reciprocal annotations should not be made without confirming that it is physiological relevant.","term_def":"\"Binding to a protein or protein complex from a different species, for example a pathogen molecule binding to a host protein.\" [PMID:28861068]","term_is_obsolete":false,"term_not_annotate":false},{"start":41,"end":61,"reference_id":"35096974","reference_source":"pmid","reference_html":"Molecular Mechanism of SARS-CoVs Orf6 Targeting the Rae1-Nup98 Complex to Compete With mRNA Nuclear Export. <i> Li T, Wen Y, Guo H, Yang T, Yang H, Ji X. </i> Front Mol Biosci, 2021","date":"2025-12-23T15:10:12.950Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P52948 ","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P78406","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04516r004","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting degenerate decameric ssRNA oligonucleotide"}]}],"statement":[{"text":"The results showed that both SARS-CoV-2 Orf6CTT and SARS-CoV-1 Orf6CTT competed with ssRNA for binding to the Rae1–Nup98GLEBS in a concentration-dependent manner (Figure 1C). Collectively, these results demonstrate that the Orf6CTT from SARS-CoV-2 and SARS-CoV-1 can closely contact the Rae1–Nup98GLEBS complex and further inhibit RNA binding.","type":"Results"}],"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":53,"end":61,"reference_id":"35096974","reference_source":"pmid","reference_html":"Molecular Mechanism of SARS-CoVs Orf6 Targeting the Rae1-Nup98 Complex to Compete With mRNA Nuclear Export. <i> Li T, Wen Y, Guo H, Yang T, Yang H, Ji X. </i> Front Mol Biosci, 2021","date":"2025-12-23T15:24:28.445Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140272","term_name":"exogenous protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P78406","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04516r005","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P59634"}],"statement":[{"text":"The composite omit map of two structures unequivocally showed that residues 53–61 of SARS-CoV-2 Orf6 and residues 50–62 of SARS-CoV-1 Orf6 accommodate the same site of Rae1 (Supplementary Figure S2). Each peptide of Orf6CTT adopts an identical elongated loop conformation (0.43 Å RMSD for 9 Cαs) and binds to the Rae1–Nup98GLEBS heterodimer alongside blades 5 to 6 of Rae1 β-propeller (Figure 2A).","type":"Results"}],"term_comment":"Note that as GO captures normal processes, it may be that exogenous proteins interactions are normal for one of the participating species but not the other. Therefore reciprocal annotations should not be made without confirming that it is physiological relevant.","term_def":"\"Binding to a protein or protein complex from a different species, for example a pathogen molecule binding to a host protein.\" [PMID:28861068]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":56,"end":60,"reference_id":"35096974","reference_source":"pmid","reference_html":"Molecular Mechanism of SARS-CoVs Orf6 Targeting the Rae1-Nup98 Complex to Compete With mRNA Nuclear Export. <i> Li T, Wen Y, Guo H, Yang T, Yang H, Ji X. </i> Front Mol Biosci, 2021","date":"2025-12-23T15:46:14.831Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140272","term_name":"exogenous protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met58Arg","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met58Ala","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P78406","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04516r006","statement":[{"text":"ITC results showed that the Orf6CTT M58A/M58R mutations led to complete loss of Rae1 binding (Figure 2E), indicating that M58 of SARS-CoVs Orf6CTT is critical for high-affinity Rae1 binding.","type":"Results"}],"term_comment":"Note that as GO captures normal processes, it may be that exogenous proteins interactions are normal for one of the participating species but not the other. Therefore reciprocal annotations should not be made without confirming that it is physiological relevant.","term_def":"\"Binding to a protein or protein complex from a different species, for example a pathogen molecule binding to a host protein.\" [PMID:28861068]","term_is_obsolete":false,"term_not_annotate":false},{"start":53,"end":61,"reference_id":"35970938","reference_source":"pmid","reference_html":"Structural basis for Sarbecovirus ORF6 mediated blockage of nucleocytoplasmic transport. <i> Gao X, Tian H, Zhu K, Li Q, Hao W, Wang L, Qin B, Deng H, Cui S. </i> Nat Commun, 2022","date":"2025-12-23T16:01:02.352Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140272","term_name":"exogenous protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"7F60"}],"ec_go":"EXP","interaction_partner":[{"db":"UniProt","id":"P78406","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04516r007","statement":[{"text":"Our crystal structures revealed that both SARS-CoV-2 ORF6 C3 and SARS-CoV ORF6 C3 peptides target a positively charged groove (also known as a putative RNA binding groove, Fig. 2a, b) on the rim of Rae1 β-propellers, and we did not find contact between the peptides and Nup98GLEBS.","type":"Results"}],"term_comment":"Note that as GO captures normal processes, it may be that exogenous proteins interactions are normal for one of the participating species but not the other. Therefore reciprocal annotations should not be made without confirming that it is physiological relevant.","term_def":"\"Binding to a protein or protein complex from a different species, for example a pathogen molecule binding to a host protein.\" [PMID:28861068]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":48,"end":61,"reference_id":"35970938","reference_source":"pmid","reference_html":"Structural basis for Sarbecovirus ORF6 mediated blockage of nucleocytoplasmic transport. <i> Gao X, Tian H, Zhu K, Li Q, Hao W, Wang L, Qin B, Deng H, Cui S. </i> Nat Commun, 2022","date":"2025-12-23T16:20:24.770Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P52948","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P78406","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04516r008","statement":[{"text":"As anticipated, we found that both SARS-CoV-2 and SARS-CoV ORF6 CTTs (C3 peptides) could dislocate single-stranded (ss) RNA from the Rae1-Nup98 complex in a concentration-dependent manner (0–64 μM) in our electrophoretic mobility shift assays (EMSA, Fig. 3k, l).","type":"Results"}],"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":57,"end":61,"reference_id":"35970938","reference_source":"pmid","reference_html":"Structural basis for Sarbecovirus ORF6 mediated blockage of nucleocytoplasmic transport. <i> Gao X, Tian H, Zhu K, Li Q, Hao W, Wang L, Qin B, Deng H, Cui S. </i> Nat Commun, 2022","date":"2025-12-23T16:28:47.370Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140678","term_name":"molecular function inhibitor activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met58Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile60Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro57Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp61Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu59Ala","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"P52948","operator":null,"partner_start":null,"partner_end":null},{"db":"UniProt","id":"P78406","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04516r009","statement":[{"text":"The Co-IP results revealed that both SARS-CoV-2 and SARS-CoV ORF6 interacted with Rae1-Nup98, while introducing mutations to Sarbecovirus ORF6, reduced its binding affinity to Rae1-Nup98 to different degrees (Fig. 4a), which agreed with our ITC results. M58A nearly abolished the binding of SARS-CoV-2 ORF6 to Rae1-Nup98, therefore this key methionine was also essential for their interaction in cells. While I60A and P57A mutations impaired the binding of SARS-CoV-2 ORF6 to Rae1-Nup98, D61A and E59A had only minor effects (Fig. 4a).","type":"Results"}],"term_comment":"","term_def":"\"A molecular function regulator that inhibits or decreases the activity of its target via non-covalent binding that does not result in covalent modification to the target.\" [GOC:curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":46,"end":61,"reference_id":"35970938","reference_source":"pmid","reference_html":"Structural basis for Sarbecovirus ORF6 mediated blockage of nucleocytoplasmic transport. <i> Gao X, Tian H, Zhu K, Li Q, Hao W, Wang L, Qin B, Deng H, Cui S. </i> Nat Commun, 2022","date":"2025-12-23T16:53:16.518Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0039657","term_name":"suppression by virus of host gene expression","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met58Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile60Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro57Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp61Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu59Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu46Lys","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04516r010","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"Overexpressing wild-type SARS-CoV-2 ORF6 significantly downregulated GFP expression level (Fig. 4b, c), indicating that ORF6 restricted GFP mRNAs nuclear transport. The ORF6 mutations that reduced its binding to Rae1-Nup98 (as identified in ITC and Co-IP) also impaired its ability of inhibiting GFP expression to different levels (Fig. 4b, c). Of note, ORF6 mutations M58A, E46K, I60 and E56Q nearly abolished its ability in inhibiting GFP expression. By contrast, ORF6 mutations that marginally affected binding to Rae1-Nup98, such as D61A and E59A, elicited little effects on inhibiting GFP expression.","type":"Results"}],"term_comment":"","term_def":"\"Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of gene expression in the host organism. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA (for protein-coding genes) and the translation of that mRNA into protein. Some protein processing events may be included when they are required to form an active form of a product from an inactive precursor form.\" [UniProtKB-KW:KW-1190, VZ:1582]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":61,"reference_id":"35970938","reference_source":"pmid","reference_html":"Structural basis for Sarbecovirus ORF6 mediated blockage of nucleocytoplasmic transport. <i> Gao X, Tian H, Zhu K, Li Q, Hao W, Wang L, Qin B, Deng H, Cui S. </i> Nat Commun, 2022","date":"2025-12-23T16:55:07.807Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0039657","term_name":"suppression by virus of host gene expression","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005636","ec_ontology":"ECO","ec_name":"green fluorescent protein reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"ec_go":"IEP","region_id":"DP04516r011","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"Overexpressing wild-type SARS-CoV-2 ORF6 significantly downregulated GFP expression level (Fig. 4b, c), indicating that ORF6 restricted GFP mRNAs nuclear transport. The ORF6 mutations that reduced its binding to Rae1-Nup98 (as identified in ITC and Co-IP) also impaired its ability of inhibiting GFP expression to different levels (Fig. 4b, c). Of note, ORF6 mutations M58A, E46K, I60 and E56Q nearly abolished its ability in inhibiting GFP expression. By contrast, ORF6 mutations that marginally affected binding to Rae1-Nup98, such as D61A and E59A, elicited little effects on inhibiting GFP expression.","type":"Results"}],"term_comment":"","term_def":"\"Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of gene expression in the host organism. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA (for protein-coding genes) and the translation of that mRNA into protein. Some protein processing events may be included when they are required to form an active form of a product from an inactive precursor form.\" [UniProtKB-KW:KW-1190, VZ:1582]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":46,"end":61,"reference_id":"35970938","reference_source":"pmid","reference_html":"Structural basis for Sarbecovirus ORF6 mediated blockage of nucleocytoplasmic transport. <i> Gao X, Tian H, Zhu K, Li Q, Hao W, Wang L, Qin B, Deng H, Cui S. </i> Nat Commun, 2022","date":"2025-12-23T17:01:38.940Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0039522","term_name":"suppression by virus of host mRNA export from nucleus","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met58Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile60Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro57Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp61Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu59Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu46Lys","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04516r012","statement":[{"text":"To verify that the observed GFP expression inhibition was caused by ORF6-mediated imprisonment of GFP mRNA in the nucleus, we quantified the nuclear to cytoplasmic (Nu/Cyto) ratio of GFP transcripts as described previously22. Overexpressing SARS-CoV-2 and SARS-CoV ORF6 proteins resulted in the accumulation of GFP mRNAs in the nucleus, as indicated by a high Nu/Cyto ratio of GFP transcripts (Fig. 4d). By contrast, the ORF6 mutants that lost the binding affinity to Rae1-Nup98 failed in trapping GFP mRNA in the nucleus. SARS-CoV-2 ORF6 E46K and SARS-CoV ORF6 E56Q (i.e., mutants that lost anti-IFN activity) could not block GFP mRNA nuclear export (Fig. 4b–d). Taken together, these results provide experimental evidence that ORF6-mediated blocking of mRNA nuclear export and inhibition of GFP expression depend on the binding of ORF6 to the Rae1-Nup98 complex. Disrupting this interaction impairs the function of ORF6.","type":"Results"}],"term_comment":"","term_def":"\"Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of movement of mRNA from the nucleus to the cytoplasm in the host organism.\" [GOC:bf, GOC:sp, UniProtKB-KW:KW-1099, VZ:902]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":1,"end":61,"reference_id":"35970938","reference_source":"pmid","reference_html":"Structural basis for Sarbecovirus ORF6 mediated blockage of nucleocytoplasmic transport. <i> Gao X, Tian H, Zhu K, Li Q, Hao W, Wang L, Qin B, Deng H, Cui S. </i> Nat Commun, 2022","date":"2025-12-23T17:01:16.425Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0039522","term_name":"suppression by virus of host mRNA export from nucleus","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001567","ec_ontology":"ECO","ec_name":"quantitative reverse transcription polymerase chain reaction evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"ec_go":"EXP","region_id":"DP04516r013","statement":[{"text":"To verify that the observed GFP expression inhibition was caused by ORF6-mediated imprisonment of GFP mRNA in the nucleus, we quantified the nuclear to cytoplasmic (Nu/Cyto) ratio of GFP transcripts as described previously22. Overexpressing SARS-CoV-2 and SARS-CoV ORF6 proteins resulted in the accumulation of GFP mRNAs in the nucleus, as indicated by a high Nu/Cyto ratio of GFP transcripts (Fig. 4d). By contrast, the ORF6 mutants that lost the binding affinity to Rae1-Nup98 failed in trapping GFP mRNA in the nucleus. SARS-CoV-2 ORF6 E46K and SARS-CoV ORF6 E56Q (i.e., mutants that lost anti-IFN activity) could not block GFP mRNA nuclear export (Fig. 4b–d). Taken together, these results provide experimental evidence that ORF6-mediated blocking of mRNA nuclear export and inhibition of GFP expression depend on the binding of ORF6 to the Rae1-Nup98 complex. Disrupting this interaction impairs the function of ORF6.","type":"Results"}],"term_comment":"","term_def":"\"Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of movement of mRNA from the nucleus to the cytoplasm in the host organism.\" [GOC:bf, GOC:sp, UniProtKB-KW:KW-1099, VZ:902]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":1,"end":61,"reference_id":"35970938","reference_source":"pmid","reference_html":"Structural basis for Sarbecovirus ORF6 mediated blockage of nucleocytoplasmic transport. <i> Gao X, Tian H, Zhu K, Li Q, Hao W, Wang L, Qin B, Deng H, Cui S. </i> Nat Commun, 2022","date":"2025-12-23T17:18:34.541Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0039502","term_name":"suppression by virus of host type I interferon-mediated signaling pathway","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005648","ec_ontology":"ECO","ec_name":"luciferase reporter gene assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"ec_go":"IEP","region_id":"DP04516r014","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"Overexpressing SARS-CoV-2 and SARS-CoV ORF6 dramatically inhibited the IFN-sensitive response element-driven luciferase activity triggered by IFN-α and IFN-β, while ORF6 mutants that lost the binding affinity to Rae1-Nup98 also lost their inhibitory activity to different extents (Fig. 4e, f).","type":"Results"}],"term_comment":"","term_def":"\"Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of type I interferon-mediated signaling in the host organism. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.\" [GOC:add, GOC:bf, GOC:sp, UniProtKB-KW:KW-1114, VZ:883]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":46,"end":61,"reference_id":"35970938","reference_source":"pmid","reference_html":"Structural basis for Sarbecovirus ORF6 mediated blockage of nucleocytoplasmic transport. <i> Gao X, Tian H, Zhu K, Li Q, Hao W, Wang L, Qin B, Deng H, Cui S. </i> Nat Commun, 2022","date":"2025-12-23T17:23:19.401Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0039502","term_name":"suppression by virus of host type I interferon-mediated signaling pathway","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met58Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile60Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro57Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Asp61Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu59Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu46Lys","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04516r015","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"Overexpressing SARS-CoV-2 and SARS-CoV ORF6 dramatically inhibited the IFN-sensitive response element-driven luciferase activity triggered by IFN-α and IFN-β, while ORF6 mutants that lost the binding affinity to Rae1-Nup98 also lost their inhibitory activity to different extents (Fig. 4e, f). Specifically, ORF6 harboring the M58A and E46K mutation exhibited the strongest loss of inhibitory activity. The activity of the M58A mutant was similar to that of the negative control (i.e., empty vector). These results indicate that residues M58 and E46 of SARS-CoV-2 ORF6 are essential for its antagonistic activity against IFN-signaling.","type":"Results"}],"term_comment":"","term_def":"\"Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of type I interferon-mediated signaling in the host organism. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.\" [GOC:add, GOC:bf, GOC:sp, UniProtKB-KW:KW-1114, VZ:883]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":1,"end":61,"reference_id":"35970938","reference_source":"pmid","reference_html":"Structural basis for Sarbecovirus ORF6 mediated blockage of nucleocytoplasmic transport. <i> Gao X, Tian H, Zhu K, Li Q, Hao W, Wang L, Qin B, Deng H, Cui S. </i> Nat Commun, 2022","date":"2025-12-23T18:12:19.826Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0052038","term_name":"modulation by symbiont of host intracellular transport","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005601","ec_ontology":"ECO","ec_name":"immunofluorescence confocal microscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"ec_go":"IDA","region_id":"DP04516r016","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"While IFN-β treatment induced STAT1 nuclear import, overexpressing ORF6 blocked STAT1 translocation into the nucleus. Consistent with results from other experiments in this study, ORF6 mutants that lost the binding affinity to Rae1-Nup98 also lost their inhibitory activity (Fig. 4g, h).","type":"Results"},{"text":"Together, we provide here a wealth of experimental evidence demonstrating that binding of ORF6 to Rae1-Nup98 is a fundamental step for blocking nucleocytoplasmic trafficking.","type":"Results"}],"term_comment":"","term_def":"\"Any process in which an organism modulates the frequency, rate or extent of the directed movement of substances within the cell or cells of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.\" [GOC:mtg_pamgo_17jul06]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":46,"end":60,"reference_id":"35970938","reference_source":"pmid","reference_html":"Structural basis for Sarbecovirus ORF6 mediated blockage of nucleocytoplasmic transport. <i> Gao X, Tian H, Zhu K, Li Q, Hao W, Wang L, Qin B, Deng H, Cui S. </i> Nat Commun, 2022","date":"2025-12-23T18:11:56.992Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0052038","term_name":"modulation by symbiont of host intracellular transport","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Met58Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Ile60Ala","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu46Lys","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04516r017","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0063","entry_name":"Human Embryonic Kidney 293T"}],"statement":[{"text":"While IFN-β treatment induced STAT1 nuclear import, overexpressing ORF6 blocked STAT1 translocation into the nucleus. Consistent with results from other experiments in this study, ORF6 mutants that lost the binding affinity to Rae1-Nup98 also lost their inhibitory activity (Fig. 4g, h).","type":"Results"},{"text":"Together, we provide here a wealth of experimental evidence demonstrating that binding of ORF6 to Rae1-Nup98 is a fundamental step for blocking nucleocytoplasmic trafficking.","type":"Results"}],"term_comment":"","term_def":"\"Any process in which an organism modulates the frequency, rate or extent of the directed movement of substances within the cell or cells of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction.\" [GOC:mtg_pamgo_17jul06]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":1,"end":61,"reference_id":"35970938","reference_source":"pmid","reference_html":"Structural basis for Sarbecovirus ORF6 mediated blockage of nucleocytoplasmic transport. <i> Gao X, Tian H, Zhu K, Li Q, Hao W, Wang L, Qin B, Deng H, Cui S. </i> Nat Commun, 2022","date":"2025-12-23T18:22:41.008Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0052170","term_name":"suppression by symbiont of host innate immune response","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04516r018","statement":[{"text":"Together, we provide here a wealth of experimental evidence demonstrating that binding of ORF6 to Rae1-Nup98 is a fundamental step for blocking nucleocytoplasmic trafficking. Blocking nucleocytoplasmic trafficking ultimately results in innate immunity suppression that facilitates CoV infection. Importantly, this work identifies key determinants in the ORF6 CTT that govern its antagonistic functions.","type":"Results"},{"text":"We prove that the binding affinity of ORF6 to Rae1-Nup98 accounts for its role in nucleocytoplasmic trafficking blockade and IFNs suppression.","type":"Results"}],"term_comment":"","term_def":"\"Any process in which a symbiont stops, prevents, or reduces the frequency, rate or extent of the innate immune response of the host organism, the host's first line of defense against infection. The host is defined as the larger of the organisms involved in a symbiotic interaction.\" [GOC:mtg_pamgo_17jul06]","term_is_obsolete":false,"term_not_annotate":false},{"start":38,"end":61,"reference_id":"39724814","reference_source":"pmid","reference_html":"Met58 and di-acidic motif located at C-terminal region of SARS-CoV-2 ORF6 plays a crucial role in its structural conformations. <i> Kumar P, Saumya KU, Bhardwaj T, Giri R. </i> Biophys Chem, 2025","date":"2026-01-12T08:18:45.014Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04516r019","statement":[{"text":"To validate these predictions, we have recorded a Far UV CD spectrum of CTR in isolation where the negative ellipticity peak lies at ∼198 nm, a signature spectrum for unstructured proteins/regions (Fig. 1b).","type":"Results"},{"text":"The ORF6-CTR peptide with sequence 38-KNLSKSLTENKYSQLDEEQPMEID-61 was commercially synthesized and obtained from Genscript LLC, USA.","type":"Methods"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-22T16:24:56.692Z"}},{"start":44,"end":61,"reference_id":"40372136","reference_source":"pmid","reference_html":"NMR Structural Characterization of SARS-CoV-2 ORF6 Reveals an N-Terminal Membrane Anchor. <i> Ninot-Pedrosa M, Pálfy G, Razmazma H, Crowley J, Fogeron ML, Bersch B, Barnes A, Brutscher B, Monticelli L, Böckmann A, Meier BH, Lecoq L. </i> J Am Chem Soc, 2025","date":"2026-05-22T16:14:13.426Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":5,"construct_alterations":[{"term_id":"MI:0988","term_name":"STREP","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"BMRB","id":"52654"}],"region_id":"DP04516r020","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"43769","entry_name":null}],"statement":[{"text":"Backbone resonance assignments revealed that C-terminal residues 46 to 61 are visible in DDM, and residues 40 to 61 in DPC-d38 (Figure S1 and Table S2), as well as residues from the ST in the C-terminus. This observation indicates that the C-terminal part of the protein remains highly flexible, while the N-terminal part (residues 1 to 40) must be embedded in the micelle, leading to slow molecular tumbling and extensive NMR line broadening, thereby preventing detection. The secondary structure propensities (SSP) (31) of the C-terminal part were derived from the measured CO, Cα, and Cβ chemical shifts and are shown in Figure 1B. In detergent micelles, the SSP score of the first observed residues (40–43) indicates a high propensity for α-helical conformation. After residue 43, ORF6 undergoes a transition from α-helical to random-coil structure (SSP < 0.5).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-22T16:24:58.991Z"}},{"start":40,"end":49,"reference_id":"40372136","reference_source":"pmid","reference_html":"NMR Structural Characterization of SARS-CoV-2 ORF6 Reveals an N-Terminal Membrane Anchor. <i> Ninot-Pedrosa M, Pálfy G, Razmazma H, Crowley J, Fogeron ML, Bersch B, Barnes A, Brutscher B, Monticelli L, Böckmann A, Meier BH, Lecoq L. </i> J Am Chem Soc, 2025","date":"2026-05-22T16:19:26.499Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"BMRB","id":"52654"}],"region_id":"DP04516r021","statement":[{"text":"However, only the last 11 residues (50–61) were visible in the solid-state INEPT spectra, revealing that the conformational dynamics of the C-terminal end is mostly unchanged between detergent micelles and lipid bilayers, while residues 40–50 are more rigid in membranes compared to detergent micelles (Figure S6).\nAltogether, the results show that the C-terminal tail is flexible and either fully disordered (random coil) or with residual α-helical structures. Its dynamics are fast from residue 50 onward, regardless of whether ORF6 is found on lipid bilayers or in detergent micelles.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00489","term_name":"interacting membrane","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"ERGIC-PI4P was prepared by mixing in chloroform POPC:POPE:PI4P:POPS:Chol (47.8:20.1:16.5:7.6:8) as described (62) using PI4P instead of phosphatidylinositol."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-22T16:25:00.185Z"}},{"start":40,"end":49,"reference_id":"40372136","reference_source":"pmid","reference_html":"NMR Structural Characterization of SARS-CoV-2 ORF6 Reveals an N-Terminal Membrane Anchor. <i> Ninot-Pedrosa M, Pálfy G, Razmazma H, Crowley J, Fogeron ML, Bersch B, Barnes A, Brutscher B, Monticelli L, Böckmann A, Meier BH, Lecoq L. </i> J Am Chem Soc, 2025","date":"2026-05-22T16:22:37.574Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"BMRB","id":"52654"}],"region_id":"DP04516r022","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"43769","entry_name":null},{"term_id":"IDPO:00489","term_name":"interacting membrane","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"ERGIC-PI4P was prepared by mixing in chloroform POPC:POPE:PI4P:POPS:Chol (47.8:20.1:16.5:7.6:8) as described (62) using PI4P instead of phosphatidylinositol."}]}],"statement":[{"text":"Backbone resonance assignments revealed that C-terminal residues 46 to 61 are visible in DDM, and residues 40 to 61 in DPC-d38 (Figure S1 and Table S2), as well as residues from the ST in the C-terminus. This observation indicates that the C-terminal part of the protein remains highly flexible, while the N-terminal part (residues 1 to 40) must be embedded in the micelle, leading to slow molecular tumbling and extensive NMR line broadening, thereby preventing detection. The secondary structure propensities (SSP) (31) of the C-terminal part were derived from the measured CO, Cα, and Cβ chemical shifts and are shown in Figure 1B. In detergent micelles, the SSP score of the first observed residues (40–43) indicates a high propensity for α-helical conformation. After residue 43, ORF6 undergoes a transition from α-helical to random-coil structure (SSP < 0.5).","type":"Results"},{"text":"However, only the last 11 residues (50–61) were visible in the solid-state INEPT spectra, revealing that the conformational dynamics of the C-terminal end is mostly unchanged between detergent micelles and lipid bilayers, while residues 40–50 are more rigid in membranes compared to detergent micelles (Figure S6). Altogether, the results show that the C-terminal tail is flexible and either fully disordered (random coil) or with residual α-helical structures. Its dynamics are fast from residue 50 onward, regardless of whether ORF6 is found on lipid bilayers or in detergent micelles.","type":"Results"},{"text":"Residues 40–50 of ORF6 show increased rigidity in ERGIC-PI4P lipid bilayers compared to detergent micelles, consistent with a transition from flexible to ordered conformation upon membrane reconstitution.","type":"Curator statement"}],"states_connection":[{"source":"DP04516r002","target":"DP04516r021"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-22T16:24:55.095Z"}}],"__v":0,"disorder_content":0.39344262295081966,"disprot_consensus":{"full":[{"start":1,"end":37,"type":"F"},{"start":38,"end":39,"type":"D"},{"start":40,"end":49,"type":"T"},{"start":50,"end":61,"type":"D"}],"Structural state":[{"start":38,"end":61,"type":"D"}],"Molecular function":[{"start":41,"end":61,"type":"F"}],"Biological process":[{"start":1,"end":61,"type":"F"}],"Structural transition":[{"start":40,"end":49,"type":"T"}]}},{"acc":"P54198","sequence":"MKLLKPTWVNHNGKPIFSVDIHPDGTKFATGGQGQDSGKVVIWNMSPVLQEDDEKDENIPKMLCQMDNHLACVNCVRWSNSGMYLASGGDDKLIMVWKRATYIGPSTVFGSSGKLANVEQWRCVSILRNHSGDVMDVAWSPHDAWLASCSVDNTVVIWNAVKFPEILATLRGHSGLVKGLTWDPVGKYIASQADDRSLKVWRTLDWQLETSITKPFDECGGTTHVLRLSWSPDGHYLVSAHAMNNSGPTAQIIEREGWKTNMDFVGHRKAVTVVKFNPKIFKKKQKNGSSAKPSCPYCCCAVGSKDRSLSVWLTCLKRPLVVIHELFDKSIMDISWTLNGLGILVCSMDGSVAFLDFSQDELGDPLSEEEKSRIHQSTYGKSLAIMTEAQLSTAVIENPEMLKYQRRQQQQQLDQKSAATREMGSATSVAGVVNGESLEDIRKNLLKKQVETRTADGRRRITPLCIAQLDTGDFSTAFFNSIPLSGSLAGTMLSSHSSPQLLPLDSSTPNSFGASKPCTEPVVAASARPAGDSVNKDSMNATSTPAALSPSVLTTPSKIEPMKAFDSRFTERSKATPGAPALTSMTPTAVERLKEQNLVKELRPRDLLESSSDSDEKVPLAKASSLSKRKLELEVETVEKKKKGRPRKDSRLMPVSLSVQSPAALTAEKEAMCLSAPALALKLPIPSPQRAFTLQVSSDPSMYIEVENEVTVVGGVKLSRLKCNREGKEWETVLTSRILTAAGSCDVVCVACEKRMLSVFSTCGRRLLSPILLPSPISTLHCTGSYVMALTAAATLSVWDVHRQVVVVKEESLHSILAGSDMTVSQILLTQHGIPVMNLSDGKAYCFNPSLSTWNLVSDKQDSLAQCADFRSSLPSQDAMLCSGPLAIIQGRTSNSGRQAARLFSVPHVVQQETTLAYLENQVAAALTLQSSHEYRHWLLVYARYLVNEGFEYRLREICKDLLGPVHYSTGSQWESTVVGLRKRELLKELLPVIGQNLRFQRLFTECQEQLDILRDK","creator":"zskalman","dataset":["NDDs-related proteins"],"date":"2025-12-11T16:46:52.950Z","disprot_id":"DP04518","features":{"pfam":[{"id":"PF07569","name":"TUP1-like enhancer of split","start":764,"end":962},{"id":"PF24105","name":"CAF1B/HIR1 beta-propeller domain","start":1,"end":212}]},"genes":[{"name":{"value":"HIRA","_id":"693af57d38549a2e1d36cb05","evidences":[]},"synonyms":[{"value":"DGCR1","_id":"693af57d38549a2e1d36cb06","evidences":[]},{"value":"HIR","_id":"693af57d38549a2e1d36cb07","evidences":[]},{"value":"TUPLE1","_id":"693af57d38549a2e1d36cb08","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"693af57d38549a2e1d36cb04"}],"length":1017,"name":"Protein HIRA","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":1,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":425,"end":445,"reference_id":"16980972","reference_source":"pmid","reference_html":"Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly. <i> Tang Y, Poustovoitov MV, Zhao K, Garfinkel M, Canutescu A, Dunbrack R, Adams PD, Marmorstein R. </i> Nat Struct Mol Biol, 2006","date":"2026-06-17T15:29:05.784Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"2I32"}],"region_id":"DP04518r001","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q9Y294"}],"statement":[{"text":"One HIRA fragment could be confidently built into the electron density map from residues 446 to 466 and the other from residues 449 to 464 (Fig. 3b). We presume that the remainder of the HIRA fragments is disordered.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-17T15:38:26.541Z"}}],"__v":0,"disorder_content":0.02064896755162242,"disprot_consensus":{"full":[{"start":425,"end":445,"type":"D"}],"Structural state":[{"start":425,"end":445,"type":"D"}]}},{"acc":"Q16643","sequence":"MAGVSFSGHRLELLAAYEEVIREESAADWALYTYEDGSDDLKLAASGEGGLQELSGHFENQKVMYGFCSVKDSQAALPKYVLINWVGEDVPDARKCACASHVAKVAEFFQGVDVIVNASSVEDIDAGAIGQRLSNGLARLSSPVLHRLRLREDENAEPVGTTYQKTDAAVEMKRINREQFWEQAKKEEELRKEEERKKALDERLRFEQERMEQERQEQEERERRYREREQQIEEHRRKQQTLEAEEAKRRLKEQSIFGDHRDEEEETHMKKSESEVEEAAAIIAQRPDNPREFFKQQERVASASAGSCDVPSPFNHRPGSHLDSHRRMAPTPIPTRSPSDSSTASTPVAEQIERALDEVTSSQPPPLPPPPPPAQETQEPSPILDSEETRAAAPQAWAGPMEEPPQAQAPPRGPGSPAEDLMFMESAEQAVLAAPVEPATADATEIHDAADTIETDTATADTTVANNVPPAATSLIDLWPGNGEGASTLQGEPRAPTPPSGTEVTLAEVPLLDEVAPEPLLPAGEGCATLLNFDELPEPPATFCDPEEVEGESLAAPQTPTLPSALEELEQEQEPEPHLLTNGETTQKEGTQASEGYFSQSQEEEFAQSEELCAKAPPPVFYNKPPEIDITCWDADPVPEEEEGFEGGD","creator":"rpancsa","dataset":[],"date":"2025-12-15T15:38:08.304Z","disprot_id":"DP04521","features":{"pfam":[{"id":"PF00241","name":"Cofilin/tropomyosin-type actin-binding protein","start":10,"end":133}]},"genes":[{"name":{"value":"DBN1","_id":"69402b6038549a2e1d36cc69","evidences":[]},"synonyms":[{"value":"D0S117E","_id":"69402b6038549a2e1d36cc6a","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"69402b6038549a2e1d36cc68"}],"length":649,"name":"Drebrin","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":1,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":233,"end":317,"reference_id":"40515930","reference_source":"pmid","reference_html":"Resonance assignment of the intrinsically disordered actin-binding region of Drebrin. <i> Varga S, Kaasen JM, Gáspári Z, Péterfia BF, Mulder FAA. </i> Biomol NMR Assign, 2025","date":"2025-12-15T16:14:07.706Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Figure","text":"1H-15N HSQC spectrum of the D233 construct in 50 mM NaCl,\n17 mM NaH 2PO4, 3 mM Na2HPO4, pH 6.0, 5 mM TCEP measured at 25 °C."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6,"statements":[{"type":"Figure","text":"1H-15N HSQC spectrum of the D233 construct in 50 mM NaCl,\n17 mM NaH 2PO4, 3 mM Na2HPO4, pH 6.0, 5 mM TCEP measured at 25 °C."}]}],"construct_alterations":[{"term_id":"MI:0507","term_name":"Tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Article","text":"The D233 protein construct used for NMR experiments\nhad the following sequence: gshmEEHRRK QQTLEAEEAK RRLKEQSIFG DHRDEEEETH MKKSESEVEE\nAAAIIAQRPD NPREFFKQQE RVASASAGSC DVPSPFNHR."},{"type":"Curator statement","text":"The first four residues \"gshm\", indicated with small case letters in the corresponding sentence, do not belong to the protein sequence according to UniProt."}]}],"cross_refs":[{"db":"BMRB","id":"52895"}],"region_id":"DP04521r001","sequence_construct":"GSHMEEHRRKQQTLEAEEAKRRLKEQSIFGDHRDEEEETHMKKSESEVEEAAAIIAQRPDNPREFFKQQERVASASAGSCDVPSPFNHR","statement":[{"text":"To bridge this gap, we designed the intrinsically disordered construct D233\nand employed 3D (HN)CO(CO)NH NMR spectroscopy to accomplish a near-complete backbone resonance assignment.","type":"Abstract"},{"text":"In Figure 3, the H-15N HSQC spectrum of the D233 construct shows very narrow peak dispersion, which is characteristic for disordered proteins.","type":"Curator statement"},{"text":"In comparison, CheSPI results indicate only a shorter segment with minor secondary structure propensity, harbored by disordered regions, which appears to be more accurate when looking at the chemical shift values. Following the first 20 residues, the construct adapts a mostly disordered conformation with a minor region of decreased mobility around residue 60.","type":"Article"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-03-20T13:38:11.495Z"}}],"__v":0,"disorder_content":0.13097072419106318,"disprot_consensus":{"full":[{"start":233,"end":317,"type":"D"}],"Structural state":[{"start":233,"end":317,"type":"D"}]}},{"acc":"O75381","sequence":"MASSEQAEQPSQPSSTPGSENVLPREPLIATAVKFLQNSRVRQSPLATRRAFLKKKGLTDEEIDMAFQQSGTAADEPSSLGPATQVVPVQPPHLISQPYSPAGSRWRDYGALAIIMAGIAFGFHQLYKKYLLPLILGGREDRKQLERMEAGLSELSGSVAQTVTQLQTTLASVQELLIQQQQKIQELAHELAAAKATTSTNWILESQNINELKSEINSLKGLLLNRRQFPPSPSAPKIPSWQIPVKSPSPSSPAAVNHHSSSDISPVSNESTSSSPGKEGHSPEGSTVTYHLLGPQEEGEGVVDVKGQVRMEVQGEEEKREDKEDEEDEEDDDVSHVDEEDCLGVQREDRRGGDGQINEQVEKLRRPEGASNESERD","creator":"rpancsa","dataset":["Autophagy-related proteins"],"date":"2025-12-18T09:36:47.408Z","disprot_id":"DP04522","features":{"pfam":[{"id":"PF04695","name":"Pex14 N-terminal domain","start":25,"end":68}]},"genes":[{"name":{"value":"PEX14","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/9653144","id":"9653144","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/9653144","_id":"6943cb2f38549a2e1d36cd28"},"code":"ECO:0000303","_id":"6943cb2f38549a2e1d36cd27"},{"source":{"id":"HGNC:8856","name":"HGNC","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:8856","_id":"6943cb2f38549a2e1d36cd2a"},"code":"ECO:0000312","_id":"6943cb2f38549a2e1d36cd29"}],"_id":"6943cb2f38549a2e1d36cd26"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"6943cb2f38549a2e1d36cd25"}],"length":377,"name":"Peroxisomal membrane protein PEX14","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":2,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":1,"end":15,"reference_id":"33937250","reference_source":"pmid","reference_html":"Membrane Interactions of the Peroxisomal Proteins PEX5 and PEX14. <i> Gaussmann S, Gopalswamy M, Eberhardt M, Reuter M, Zou P, Schliebs W, Erdmann R, Sattler M. </i> Front Cell Dev Biol, 2021","date":"2025-12-18T09:39:55.607Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04522r001","statement":[{"text":"We first confirmed that the N-terminal region of PEX14 up to the transmembrane span (residues 1–104) harbors the α-helical globular domain (residues 16–80) but is otherwise unstructured (Figure 3B). This is indeed demonstrated by the virtually identical secondary chemical shifts for the region comprising the globular domain, while the flanking regions exhibit random coil chemical shifts and low heteronuclear NOE values and are thus intrinsically disordered (Figures 3B,C).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-06T13:00:35.914Z"}},{"start":81,"end":104,"reference_id":"33937250","reference_source":"pmid","reference_html":"Membrane Interactions of the Peroxisomal Proteins PEX5 and PEX14. <i> Gaussmann S, Gopalswamy M, Eberhardt M, Reuter M, Zou P, Schliebs W, Erdmann R, Sattler M. </i> Front Cell Dev Biol, 2021","date":"2025-12-18T09:40:22.524Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04522r002","statement":[{"text":"We first confirmed that the N-terminal region of PEX14 up to the transmembrane span (residues 1–104) harbors the α-helical globular domain (residues 16–80) but is otherwise unstructured (Figure 3B). This is indeed demonstrated by the virtually identical secondary chemical shifts for the region comprising the globular domain, while the flanking regions exhibit random coil chemical shifts and low heteronuclear NOE values and are thus intrinsically disordered (Figures 3B,C).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-06T13:00:55.087Z"}}],"__v":0,"disorder_content":0.10344827586206896,"disprot_consensus":{"full":[{"start":1,"end":15,"type":"D"},{"start":81,"end":104,"type":"D"}],"Structural state":[{"start":1,"end":15,"type":"D"},{"start":81,"end":104,"type":"D"}]}},{"acc":"Q96B01","sequence":"MVRPVRHKKPVNYSQFDHSDSDDDFVSATVPLNKKSRTAPKELKQDKPKPNLNNLRKEEIPVQEKTPKKRLPEGTFSIPASAVPCTKMALDDKLYQRDLEVALALSVKELPTVTTNVQNSQDKSIEKHGSSKIETMNKSPHISNCSVASDYLDLDKITVEDDVGGVQGKRKAASKAAAQQRKILLEGSDGDSANDTEPDFAPGEDSEDDSDFCESEDNDEDFSMRKSKVKEIKKKEVKVKSPVEKKEKKSKSKCNALVTSVDSAPAAVKSESQSLPKKVSLSSDTTRKPLEIRSPSAESKKPKWVPPAASGGSRSSSSPLVVVSVKSPNQSLRLGLSRLARVKPLHPNATST","creator":"vnugnes","dataset":[],"date":"2025-12-18T13:23:02.210Z","disprot_id":"DP04523","features":{"pfam":[{"id":"PF15696","name":"RAD51 interacting motif","start":311,"end":349}]},"genes":[{"name":{"value":"RAD51AP1","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/16990250","id":"16990250","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/16990250","_id":"6944003638549a2e1d36cd47"},"code":"ECO:0000303","_id":"6944003638549a2e1d36cd46"},{"source":{"id":"HGNC:16956","name":"HGNC","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:16956","_id":"6944003638549a2e1d36cd49"},"code":"ECO:0000312","_id":"6944003638549a2e1d36cd48"}],"_id":"6944003638549a2e1d36cd45"},"synonyms":[{"value":"PIR51","_id":"6944003638549a2e1d36cd4a","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"6944003638549a2e1d36cd44"}],"length":352,"name":"RAD51-associated protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":17,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":1,"end":352,"reference_id":"17996710","reference_source":"pmid","reference_html":"RAD51AP1 is a structure-specific DNA binding protein that stimulates joint molecule formation during RAD51-mediated homologous recombination. <i> Modesti M, Budzowska M, Baldeyron C, Demmers JA, Ghirlando R, Kanaar R. </i> Mol Cell, 2007","date":"2025-12-18T13:25:08.742Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007689","ec_ontology":"ECO","ec_name":"sodium dodecyl sulfate polyacrylamide gel electrophoresis evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04523r001","statement":[{"text":"Recombinant RAD51AP1 migrated slower than expected during denaturing SDS polyacrylamide gel electrophoresis under reducing conditions, because it displayed an apparent molecular weight of ∼48 kDa as compared to its calculated molecular weight of 39,417 Da (Figures 3A and 3B). This retarded mobility was also observed for the endogenous protein detected in human cell extracts (Figure S1A).","type":"Results"}]},{"start":1,"end":352,"reference_id":"17996710","reference_source":"pmid","reference_html":"RAD51AP1 is a structure-specific DNA binding protein that stimulates joint molecule formation during RAD51-mediated homologous recombination. <i> Modesti M, Budzowska M, Baldeyron C, Demmers JA, Ghirlando R, Kanaar R. </i> Mol Cell, 2007","date":"2025-12-18T13:46:39.950Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000244","ec_ontology":"ECO","ec_name":"combinatorial evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04523r002","statement":[{"text":"RAD51AP1 also behaved as a single and larger than expected entity during Sephacryl 200 gel permeation chromatography (∼180 kDa, Figures 3B and 3C), suggesting assembly of an oligomer in solution and/or an elongated monomeric structure.","type":"Results"},{"text":"The sedimentation profiles collected at a single loading concentration were consistent with the presence of a single ideal solute having an experimental molecular mass of 40.9 ± 0.8 kDa. This corresponds to a stoichiometry of 1.04 ± 0.02, demonstrating that the protein is both monomeric and monodisperse in solution.","type":"Results"}]},{"start":1,"end":352,"reference_id":"17996710","reference_source":"pmid","reference_html":"RAD51AP1 is a structure-specific DNA binding protein that stimulates joint molecule formation during RAD51-mediated homologous recombination. <i> Modesti M, Budzowska M, Baldeyron C, Demmers JA, Ghirlando R, Kanaar R. </i> Mol Cell, 2007","date":"2025-12-18T16:36:24.693Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0000724","term_name":"double-strand break repair via homologous recombination","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001585","ec_ontology":"ECO","ec_name":"small interfering RNA knockdown evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"ec_go":"IMP","region_id":"DP04523r003","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"statement":[{"text":"Depletion of RAD51AP1 (Figure S1A in the Supplemental Data available with this article online) increased the sensitivity of HeLa cells to treatment with interstrand DNA crosslinking agents (mitomycin C or cis-platin, Figures 1A and 1B) and ionizing radiation (Figure 1C).","type":"Results"},{"text":"RAD51AP1-depleted cells also showed increased sensitivity to camptothecin, a topoisomerase I inhibitor known to trigger accumulation of DSBs in S phase after passage and collapse of a replication fork (Figure 1D).","type":"Results"},{"text":"Taken together, our results are consistent with a role for RAD51AP1 in homologous recombination-mediated DSB repair.","type":"Results"}],"term_comment":"","term_def":"\"The error-free repair of a double-strand break in DNA in which the broken DNA molecule is repaired using homologous sequences. A strand in the broken DNA searches for a homologous region in an intact chromosome to serve as the template for DNA synthesis. The restoration of two intact DNA molecules results in the exchange, reciprocal or nonreciprocal, of genetic material between the intact DNA molecule and the broken DNA molecule.\" [GOC:elh, PMID:10357855]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":1,"end":352,"reference_id":"17996710","reference_source":"pmid","reference_html":"RAD51AP1 is a structure-specific DNA binding protein that stimulates joint molecule formation during RAD51-mediated homologous recombination. <i> Modesti M, Budzowska M, Baldeyron C, Demmers JA, Ghirlando R, Kanaar R. </i> Mol Cell, 2007","date":"2025-12-18T16:44:17.273Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006974","term_name":"cellular response to DNA damage stimulus","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007142","ec_ontology":"ECO","ec_name":"green fluorescent protein immunolocalization evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0687","term_name":"fluorescent protein tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"ec_go":"IDA","region_id":"DP04523r004","sample":[{"term_id":"IDPO:00492","term_name":"in-cell experiment","unit_name":"cells/ml","unit_id":"UO:0000201","deviation":null,"value":null,"db":"Cellosaurus","id":"CVCL_0030","entry_name":"Henrietta Lacks cells"}],"statement":[{"text":"Indeed, HeLa cells stably expressing GFP-RAD51AP1 (Figure S1A) displayed spontaneous RAD51AP1 foci that colocalized with RAD51 (Figure 2A). As is the case for RAD51, the number of RAD51AP1 foci increased when the cells were treated with ionizing radiation. Both spontaneous and DNA damaged induced RAD51AP1 foci were less plentiful compared to RAD51. However, most if not all, RAD51AP1 foci did colocalize with RAD51.","type":"Results"}],"term_comment":"","term_def":"\"Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":352,"reference_id":"17996710","reference_source":"pmid","reference_html":"RAD51AP1 is a structure-specific DNA binding protein that stimulates joint molecule formation during RAD51-mediated homologous recombination. <i> Modesti M, Budzowska M, Baldeyron C, Demmers JA, Ghirlando R, Kanaar R. </i> Mol Cell, 2007","date":"2025-12-18T17:12:37.522Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0120230","term_name":"recombinase activator activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001254","ec_ontology":"ECO","ec_name":"radioisotope assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"ec_go":"IDA","region_id":"DP04523r005","statement":[{"text":"Therefore, we tested whether RAD51AP1 augments this crucial activity of RAD51 in an established D loop formation assay (Bugreev and Mazin, 2004; Mazin et al., 2000) (Figure 4). Ss oligonucleotides were preincubated with RAD51 at a ratio of one RAD51 monomer per three nucleotides to allow assembly of nucleoprotein filaments. A recipient supercoiled plasmid harboring a sequence homologous to the oligonucleotide was then added to the reaction mixture to start D loop formation. Using these standard conditions and in the presence of Mg2+ ions and ATP, the addition of RAD51AP1 substantially stimulated D loop formation by RAD51 (Figures 4A–4C). Levels of D loop products were increased up to ∼8-fold (see Experimental Procedures for quantification).","type":"Results"},{"text":"RAD51AP1 Specifically Stimulates D Loop Formation by RAD51","type":"Results"}],"term_comment":"","term_def":"\"Binds to and increases the activity of a recombinase.\" [GOC:mah, PMID:32414915]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","interaction_partner":[{"db":"UniProt","id":"Q06609","operator":null,"partner_start":null,"partner_end":null}]},{"start":1,"end":352,"reference_id":"17996710","reference_source":"pmid","reference_html":"RAD51AP1 is a structure-specific DNA binding protein that stimulates joint molecule formation during RAD51-mediated homologous recombination. <i> Modesti M, Budzowska M, Baldeyron C, Demmers JA, Ghirlando R, Kanaar R. </i> Mol Cell, 2007","date":"2025-12-18T17:15:50.687Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140619","term_name":"DNA strand exchange activator activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001254","ec_ontology":"ECO","ec_name":"radioisotope assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IDA","region_id":"DP04523r006","statement":[{"text":"Therefore, we tested whether RAD51AP1 augments this crucial activity of RAD51 in an established D loop formation assay (Bugreev and Mazin, 2004; Mazin et al., 2000) (Figure 4). Ss oligonucleotides were preincubated with RAD51 at a ratio of one RAD51 monomer per three nucleotides to allow assembly of nucleoprotein filaments. A recipient supercoiled plasmid harboring a sequence homologous to the oligonucleotide was then added to the reaction mixture to start D loop formation. Using these standard conditions and in the presence of Mg2+ ions and ATP, the addition of RAD51AP1 substantially stimulated D loop formation by RAD51 (Figures 4A–4C). Levels of D loop products were increased up to ∼8-fold (see Experimental Procedures for quantification).","type":"Results"}],"term_comment":"","term_def":"\"Binds to and increases a DNA strand exchange activity.\" [PMID:33493431]","term_is_obsolete":false,"term_not_annotate":false},{"start":327,"end":352,"reference_id":"17996710","reference_source":"pmid","reference_html":"RAD51AP1 is a structure-specific DNA binding protein that stimulates joint molecule formation during RAD51-mediated homologous recombination. <i> Modesti M, Budzowska M, Baldeyron C, Demmers JA, Ghirlando R, Kanaar R. </i> Mol Cell, 2007","date":"2025-12-18T17:22:09.621Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ser327_Thr352del","start":null,"end":null,"position":null}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q06609","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04523r007","statement":[{"text":"To test this notion, we deleted residues 327–352, the 26 C-terminal residues of RAD51AP1 that contain a RAD51 interaction domain identified by two-hybrid experiments (Kovalenko et al., 2006). This C-terminally truncated RAD51AP1 protein lost its ability to physically interact with RAD51 in the coimmunoprecipitation assay described above (Figure 7C, lane 4) and was strongly affected in its ability to stimulate D loop formation by RAD51 (Figure 4C).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":352,"reference_id":"17996710","reference_source":"pmid","reference_html":"RAD51AP1 is a structure-specific DNA binding protein that stimulates joint molecule formation during RAD51-mediated homologous recombination. <i> Modesti M, Budzowska M, Baldeyron C, Demmers JA, Ghirlando R, Kanaar R. </i> Mol Cell, 2007","date":"2025-12-18T17:39:29.844Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0000217","term_name":"DNA secondary structure binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"ec_go":"IPI","region_id":"DP04523r008","statement":[{"text":"Although subtle differences in affinity could be observed, a comparison with their unbranched ss and ds derivates (Figure 5C, upper panel) revealed that the dominant feature determining formation of specific RAD51AP1-DNA complexes was the branched nature of the DNA substrate (Figure 5C, lower panel). We conclude that RAD51AP1 is a structure-specific DNA binding protein having a preference for branched-DNA structures.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a DNA secondary structure element such as a four-way junction, a bubble, a loop, Y-form DNA, or a double-strand/single-strand junction.\" [GOC:krc]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":1,"end":352,"reference_id":"17996710","reference_source":"pmid","reference_html":"RAD51AP1 is a structure-specific DNA binding protein that stimulates joint molecule formation during RAD51-mediated homologous recombination. <i> Modesti M, Budzowska M, Baldeyron C, Demmers JA, Ghirlando R, Kanaar R. </i> Mol Cell, 2007","date":"2025-12-18T17:31:58.003Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0000400","term_name":"four-way junction DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IPI","region_id":"DP04523r009","statement":[{"text":"Strikingly, RAD51AP1 showed a marked preference for binding to branched-DNA substrates, including a splayed-arm branched-DNA structure and a four-way junction (Figure 5A and Figure S3).DNA structures.","type":"Results"},{"text":"Under the experimental conditions tested, RAD51AP1 exhibited the highest affinity for a four-way Holliday junction structure with homologous sequence at its core (Figure S3A).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a DNA segment containing four-way junctions, also known as Holliday junctions, a structure where two DNA double strands are held together by reciprocal exchange of two of the four strands, one strand each from the two original helices.\" [GOC:krc, ISBN:0815332181, PMID:15563464]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":352,"reference_id":"17996710","reference_source":"pmid","reference_html":"RAD51AP1 is a structure-specific DNA binding protein that stimulates joint molecule formation during RAD51-mediated homologous recombination. <i> Modesti M, Budzowska M, Baldeyron C, Demmers JA, Ghirlando R, Kanaar R. </i> Mol Cell, 2007","date":"2025-12-18T17:33:06.036Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0000403","term_name":"Y-form DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IPI","region_id":"DP04523r010","statement":[{"text":"Strikingly, RAD51AP1 showed a marked preference for binding to branched-DNA substrates, including a splayed-arm branched-DNA structure and a four-way junction (Figure 5A and Figure S3). In particular, with the branched-DNA substrates RAD51AP1 formed discrete complexes, consistent with specific protein-DNA interactions.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a DNA segment shaped like a Y. This shape occurs when DNA contains a region of paired double-stranded DNA on one end and a region of unpaired DNA strands on the opposite end.\" [GOC:elh, PMID:16781730]","term_is_obsolete":false,"term_not_annotate":false},{"start":243,"end":326,"reference_id":"17996710","reference_source":"pmid","reference_html":"RAD51AP1 is a structure-specific DNA binding protein that stimulates joint molecule formation during RAD51-mediated homologous recombination. <i> Modesti M, Budzowska M, Baldeyron C, Demmers JA, Ghirlando R, Kanaar R. </i> Mol Cell, 2007","date":"2025-12-18T17:55:17.513Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ser327_Thr352del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1_Pro242del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04523r011","statement":[{"text":"The first 242 N-terminal residues of RAD51AP1 could be deleted without a major effect on its ability to bind RAD51, to bind the SEI DNA intermediate, and to stimulate D loop formation by RAD51. The smallest RAD51AP1 polypeptide (RAD51AP1Δ1–283 containing the last 69 C-terminal residues) was defective in stimulation of D loop formation by RAD51 but still bound RAD51. Thus, the domain involved in binding to the SEI DNA intermediate is likely located between residues 243 and 326.","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false},{"start":243,"end":352,"reference_id":"17996710","reference_source":"pmid","reference_html":"RAD51AP1 is a structure-specific DNA binding protein that stimulates joint molecule formation during RAD51-mediated homologous recombination. <i> Modesti M, Budzowska M, Baldeyron C, Demmers JA, Ghirlando R, Kanaar R. </i> Mol Cell, 2007","date":"2025-12-18T18:01:29.283Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0098530","term_name":"positive regulation of strand invasion","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Ser327_Thr352del","start":null,"end":null,"position":null},{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Met1_Pro242del","start":null,"end":null,"position":null}],"region_id":"DP04523r012","statement":[{"text":"The first 242 N-terminal residues of RAD51AP1 could be deleted without a major effect on its ability to bind RAD51, to bind the SEI DNA intermediate, and to stimulate D loop formation by RAD51. The smallest RAD51AP1 polypeptide (RAD51AP1Δ1–283 containing the last 69 C-terminal residues) was defective in stimulation of D loop formation by RAD51 but still bound RAD51.","type":"Results"},{"text":"In addition, because the truncated version RAD51AP1Δ1–283 still exhibited a weak but detectable binding to the SEI DNA intermediate, at least one residue critical for RAD51AP1 DNA binding should be located within positions 284–326. Finally, the C-terminal truncation that failed to interact with RAD51 and stimulate RAD51 D loop formation activity (Figure 4C) bound the SEI DNA intermediate in a manner similar to the wild-type RAD51AP1 (Figure 7E, first panel).","type":"Results"},{"text":"We conclude that both the RAD51 binding and the structure-specific SEI DNA intermediate binding ability of RAD51AP1 are required for efficient stimulation of D loop formation by RAD51","type":"Results"}],"term_comment":"","term_def":"\"Any process that increases the rate, frequency or extent of strand invasion. Strand invasion is the process in which the nucleoprotein complex (composed of the broken single-strand DNA and the recombinase) searches and identifies a region of homology in intact duplex DNA. The broken single-strand DNA displaces the like strand and forms Watson-Crick base pairs with its complement, forming a duplex in which each strand is from one of the two recombining DNA molecules.\" [GOC:dos, GOC:dph, GOC:elh, GOC:tb]","term_is_obsolete":false,"term_not_annotate":false},{"start":344,"end":348,"reference_id":"41337480","reference_source":"pmid","reference_html":"RAD51AP1 is a versatile RAD51 modulator. <i> Kuhlen L, Argunhan B, Liang P, Zhong J, Masino L, Zhang X. </i> Proc Natl Acad Sci U S A, 2025","date":"2025-12-19T13:43:06.919Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.His346Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"We also included the known mutant (RAD51AP1-H346A) that disrupts RAD51 binding in our analysis as a Site-C mutant, and designed a RAD51AP1 variant in which both sites are mutated (referred to as NC)."}]}],"ec_go":"IMP","region_id":"DP04523r013","statement":[{"text":"As expected, RAD51 can be pulled down by RAD51AP1 and the Site-C mutant showed a reduction in binding (Fig. 1 B and C).","type":"Results"},{"text":"Interestingly, when both binding sites were mutated, the binding was almost abolished (Fig. 1 B and C).","type":"Results"},{"text":"Wild-type protein has a dissociation constant of ~0.6 μM, which is comparable to the Site-N mutant, whereas the Site-C mutant decreased the binding affinity by ~2.5-fold, and the Site-NC double mutant showed a ~fourfold reduction in affinity (Fig. 1D). These results indicate that RAD51AP1 binds to RAD51 via at least two distinct sites, and these two sites synergistically enhance the binding, although Site-C is the major binding site.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false,"interaction_partner":[{"db":"UniProt","id":"Q06609","operator":"and","partner_start":null,"partner_end":null}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":300,"end":307,"reference_id":"41337480","reference_source":"pmid","reference_html":"RAD51AP1 is a versatile RAD51 modulator. <i> Kuhlen L, Argunhan B, Liang P, Zhong J, Masino L, Zhang X. </i> Proc Natl Acad Sci U S A, 2025","date":"2025-12-19T13:51:08.139Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys300Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test this, we mutated five conserved residues (K300, K303, W304, P306, and P307) in Site-N to alanine."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys303Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test this, we mutated five conserved residues (K300, K303, W304, P306, and P307) in Site-N to alanine."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys300Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test this, we mutated five conserved residues (K300, K303, W304, P306, and P307) in Site-N to alanine."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Trp304Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test this, we mutated five conserved residues (K300, K303, W304, P306, and P307) in Site-N to alanine."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe306Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test this, we mutated five conserved residues (K300, K303, W304, P306, and P307) in Site-N to alanine."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Phe307Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"To test this, we mutated five conserved residues (K300, K303, W304, P306, and P307) in Site-N to alanine."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.His346Ala","start":null,"end":null,"position":null,"statements":[{"type":"Results","text":"We also included the known mutant (RAD51AP1-H346A) that disrupts RAD51 binding in our analysis as a Site-C mutant, and designed a RAD51AP1 variant in which both sites are mutated (referred to as NC)."}]}],"ec_go":"IMP","interaction_partner":[{"db":"UniProt","id":"Q06609","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04523r014","statement":[{"text":"As expected, RAD51 can be pulled down by RAD51AP1 and the Site-C mutant showed a reduction in binding (Fig. 1 B and C).","type":"Results"},{"text":"Interestingly, when both binding sites were mutated, the binding was almost abolished (Fig. 1 B and C).","type":"Results"},{"text":"Wild-type protein has a dissociation constant of ~0.6 μM, which is comparable to the Site-N mutant, whereas the Site-C mutant decreased the binding affinity by ~2.5-fold, and the Site-NC double mutant showed a ~fourfold reduction in affinity (Fig. 1D). These results indicate that RAD51AP1 binds to RAD51 via at least two distinct sites, and these two sites synergistically enhance the binding, although Site-C is the major binding site.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":352,"reference_id":"41337480","reference_source":"pmid","reference_html":"RAD51AP1 is a versatile RAD51 modulator. <i> Kuhlen L, Argunhan B, Liang P, Zhong J, Masino L, Zhang X. </i> Proc Natl Acad Sci U S A, 2025","date":"2025-12-22T12:10:16.747Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0140619","term_name":"DNA strand exchange activator activity","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007122","ec_ontology":"ECO","ec_name":"in vitro assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"ec_go":"IDA","region_id":"DP04523r015","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"dsDNA oligo LK_M50 with sequence:\nAACAACAACAACAACAACAACAACAACAACAACAACAACAACAACAACAACAACAACAAC"}]},{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"116 nts ssDNA"}]}],"statement":[{"text":"Fluorescently labeling the complementary strand on the dsDNA allowed the detection of this product following electrophoresis (Fig. 2G). Indeed, under these experimental conditions, strand exchange was enhanced by RAD51AP1, with the Site-C and Site-N and Site-C double mutants displaying a noticeable defect in this assay (Fig. 2H).","type":"Results"}],"term_comment":"","term_def":"\"Binds to and increases a DNA strand exchange activity.\" [PMID:33493431]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":329,"end":349,"reference_id":"41337480","reference_source":"pmid","reference_html":"RAD51AP1 is a versatile RAD51 modulator. <i> Kuhlen L, Argunhan B, Liang P, Zhong J, Masino L, Zhang X. </i> Proc Natl Acad Sci U S A, 2025","date":"2025-12-22T12:15:02.243Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"9QN8"}],"ec_go":"IDA","interaction_partner":[{"db":"UniProt","id":"Q06609","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04523r016","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15422","entry_name":null}],"statement":[{"text":"There is additional density on the surface of some of the RAD51 monomers that could correspond to RAD51AP1 (Fig. 2I). Using AlphaFold3 (36) to model a complex between a RAD51 dimer and C59 (SI Appendix, Fig. S2D), we obtained a structural model that allowed the residues 329 to 349 of RAD51AP1 to be fitted into the extra density (Fig. 2I).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":228,"reference_id":"41337480","reference_source":"pmid","reference_html":"RAD51AP1 is a versatile RAD51 modulator. <i> Kuhlen L, Argunhan B, Liang P, Zhong J, Masino L, Zhang X. </i> Proc Natl Acad Sci U S A, 2025","date":"2025-12-22T12:19:42.429Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"9QN8"}],"region_id":"DP04523r017","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15422","entry_name":null}],"statement":[{"text":"This region lacks electron density, indicating it is disordered.","type":"Results"}]}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":352,"type":"D"}],"Structural state":[{"start":1,"end":352,"type":"D"}],"Biological process":[{"start":1,"end":352,"type":"F"}],"Molecular function":[{"start":1,"end":352,"type":"F"}]}},{"acc":"Q8KDK7","sequence":"MSDHQSHSRGKNAREWFEEWFDHPLYLKVYHHRDAEEAERCVRTILDLTGIDPAWQPPHSVLDIACGAGRHALSFARTGLRVTANDLSPYLLDQARKQAKAEGINMEFSRQDMRTIRFERRFDLIAQLFSSFGYFETDQEDRDVIANIASLLNPGGWYVLDLINPVQLKSQFTPRTERNSESLSIIEERTLSERHVTKKITLHEANGRKHSFTESVRIYSPAEAFSLLESGGFAVERVVGDYEGSPFDEATSPRMMLLARLLVSRS","creator":"vnugnes","dataset":[],"date":"2025-12-22T16:20:04.488Z","disprot_id":"DP04524","features":{"pfam":[{"id":"PF13649","name":"Methyltransferase domain","start":61,"end":156}]},"genes":[{"synonyms":[],"olnNames":[{"value":"CT1040","_id":"69496fb438549a2e1d36cde0","evidences":[]}],"orfNames":[],"_id":"69496fb438549a2e1d36cddf"}],"length":266,"name":"Methyltransferase, putative","ncbi_taxon_id":194439,"organism":"Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)","regions_counter":1,"released":"2026_06","taxonomy":["Bacteria","Pseudomonadati","Chlorobiota","Chlorobiia","Chlorobiales","Chlorobiaceae","Chlorobaculum"],"regions":[{"start":170,"end":193,"reference_id":"41338164","reference_source":"pmid","reference_html":"The methyltransferase NmbA methylates the low-molecular weight thiol bacillithiol, and displays a specific structural architecture. <i> Hammerstad M, Steinvik E, Hersleth HP. </i> Redox Biol, 2025","date":"2025-12-22T16:29:30.858Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"9RI2"}],"region_id":"DP04524r001","statement":[{"text":"The Cap domains could be rebuilt to avoid clashing between the two monomers and with a good fit to the electron density, except for residues 170–193, which did not show any electron density. The disorder of these residues was also indicated by the D2P2: Database of Disorder Protein Predictions [62].","type":"Methods"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"}],"__v":0,"disorder_content":0.09022556390977443,"disprot_consensus":{"full":[{"start":170,"end":193,"type":"D"}],"Structural state":[{"start":170,"end":193,"type":"D"}]}},{"acc":"Q9C0K0","sequence":"MSRRKQGNPQHLSQRELITPEADHVEAAILEEDEGLEIEEPSGLGLMVGGPDPDLLTCGQCQMNFPLGDILVFIEHKRKQCGGSLGACYDKALDKDSPPPSSRSELRKVSEPVEIGIQVTPDEDDHLLSPTKGICPKQENIAGPCRPAQLPAVAPIAASSHPHSSVITSPLRALGALPPCLPLPCCSARPVSGDGTQGEGQTEAPFGCQCQLSGKDEPSSYICTTCKQPFNSAWFLLQHAQNTHGFRIYLEPGPASSSLTPRLTIPPPLGPEAVAQSPLMNFLGDSNPFNLLRMTGPILRDHPGFGEGRLPGTPPLFSPPPRHHLDPHRLSAEEMGLVAQHPSAFDRVMRLNPMAIDSPAMDFSRRLRELAGNSSTPPPVSPGRGNPMHRLLNPFQPSPKSPFLSTPPLPPMPPGGTPPPQPPAKSKSCEFCGKTFKFQSNLIVHRRSHTGEKPYKCQLCDHACSQASKLKRHMKTHMHKAGSLAGRSDDGLSAASSPEPGTSELAGEGLKAADGDFRHHESDPSLGHEPEEEDEEEEEEEEELLLENESRPESSFSMDSELSRNRENGGGGVPGVPGAGGGAAKALADEKALVLGKVMENVGLGALPQYGELLADKQKRGAFLKRAAGGGDAGDDDDAGGCGDAGAGGAVNGRGGGFAPGTEPFPGLFPRKPAPLPSPGLNSAAKRIKVEKDLELPPAALIPSENVYSQWLVGYAASRHFMKDPFLGFTDARQSPFATSSEHSSENGSLRFSTPPGDLLDGGLSGRSGTASGGSTPHLGGPGPGRPSSKEGRRSDTCEYCGKVFKNCSNLTVHRRSHTGERPYKCELCNYACAQSSKLTRHMKTHGQIGKEVYRCDICQMPFSVYSTLEKHMKKWHGEHLLTNDVKIEQAERS","creator":"vnugnes","dataset":["Cancer-related proteins","NDDs-related proteins"],"date":"2025-12-22T18:43:55.519Z","disprot_id":"DP04525","features":{"pfam":[{"id":"PF00096","name":"Zinc finger, C2H2 type","start":428,"end":449},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":455,"end":477},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":797,"end":818},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":854,"end":877},{"id":"PF23611","name":"C2H2 zinc finger","start":824,"end":847},{"id":"PF25491","name":"BCL-11A-like CCHC zinc finger","start":55,"end":82}]},"genes":[{"name":{"value":"BCL11B","_id":"6949916b38549a2e1d36cdec","evidences":[]},"synonyms":[{"value":"CTIP2","_id":"6949916b38549a2e1d36cded","evidences":[]},{"value":"RIT1","_id":"6949916b38549a2e1d36cdee","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"6949916b38549a2e1d36cdeb"}],"length":894,"name":"B-cell lymphoma/leukemia 11B","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":3,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":42,"end":94,"reference_id":"41347450","reference_source":"pmid","reference_html":"Zinc-mediated multimerization of the N-terminal CCHC zinc finger domain of BCL11B: a key to stability and a potential therapeutic target. <i> Susemihl A, Nagel F, Grabarczyk P, Schmidt CA, Delcea M. </i> Phys Chem Chem Phys, 2025","date":"2025-12-22T18:45:41.086Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04525r001","statement":[{"text":"With the removal of the central zinc ions, a structural change is being observed, indicating the unfolding of the domains. The peaks observed at 228 nm are no longer visible, and the peaks at 208/205 nm shift to 200 nm. With the addition of Zn2+, the native zinc finger fold could be restored in all BCL11B42–94 species.","type":"Results"}]},{"start":42,"end":94,"reference_id":"41347450","reference_source":"pmid","reference_html":"Zinc-mediated multimerization of the N-terminal CCHC zinc finger domain of BCL11B: a key to stability and a potential therapeutic target. <i> Susemihl A, Nagel F, Grabarczyk P, Schmidt CA, Delcea M. </i> Phys Chem Chem Phys, 2025","date":"2025-12-22T18:51:10.525Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04525r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":null}],"statement":[{"text":"We already showed that BCL11B42–94 WT exhibits the typical ββα-fold for zinc finger domains in the presence of zinc.32,36 C81H shows the same spectrum with typical α-helical peaks at 208 and 228 nm.","type":"Results"},{"text":"With the removal of the central zinc ions, a structural change is being observed, indicating the unfolding of the domains. The peaks observed at 228 nm are no longer visible, and the peaks at 208/205 nm shift to 200 nm. With the addition of Zn2+, the native zinc finger fold could be restored in all BCL11B42–94 species. ","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","states_connection":[{"source":"DP04525r001","target":"DP04525r003"}]},{"start":42,"end":94,"reference_id":"41347450","reference_source":"pmid","reference_html":"Zinc-mediated multimerization of the N-terminal CCHC zinc finger domain of BCL11B: a key to stability and a potential therapeutic target. <i> Susemihl A, Nagel F, Grabarczyk P, Schmidt CA, Delcea M. </i> Phys Chem Chem Phys, 2025","date":"2025-12-22T18:50:42.479Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04525r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":null}],"statement":[{"text":"We already showed that BCL11B42–94 WT exhibits the typical ββα-fold for zinc finger domains in the presence of zinc.32,36 C81H shows the same spectrum with typical α-helical peaks at 208 and 228 nm.","type":"Results"},{"text":"Circular dichroism spectra shown in the supplementary materials shows the region is folded in the presence of Zn+2.","type":"Curator statement"}]}],"__v":0,"disorder_content":0.0592841163310962,"disprot_consensus":{"full":[{"start":42,"end":94,"type":"T"}],"Structural state":[{"start":42,"end":94,"type":"D"}],"Structural transition":[{"start":42,"end":94,"type":"T"}]}},{"acc":"Q9RWH8","sequence":"MPSRTELLAEEYLRREGHDPQKFRYVHPDGTPYTDADGLARIARLAVPPAYQDVYVSPDAENELQAFGRDAAGRLQYRYHPDFVQAGALKKWQRLTRFAGALPTLKVATTADLRASGLPPRKVMALMTRLLHVARFRVGSDIYARQHKTYGLSTLRQRHVVVDGNTVTFRFKGKHGVSQHKATSDRTLAANMQKLLDLPGPWLFQTVDAGGGERRRIHSTELNAYLREVIGPFTAKDFRTWGGTLLAAEYLAQQGTESSERQAKKVLVDCVKFVADDLGNTPAVTRGSYICPVIFDRYLDGKVLDDYEPRTERQEAELEGLTRSEGALKRMLESERTLRQRGRALK","creator":"rpancsa","dataset":[],"date":"2026-01-02T10:12:25.858Z","disprot_id":"DP04526","features":{"pfam":[{"id":"PF01028","name":"Eukaryotic DNA topoisomerase I, catalytic core","start":89,"end":286},{"id":"PF21338","name":"Bacterial DNA topoisomerase IB, N-terminal domain","start":22,"end":70}]},"genes":[{"synonyms":[],"olnNames":[{"value":"DR_0690","_id":"69579a0a38549a2e1d36ce8c","evidences":[]}],"orfNames":[],"_id":"69579a0a38549a2e1d36ce8b"}],"length":346,"name":"DNA topoisomerase","ncbi_taxon_id":243230,"organism":"Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)","regions_counter":5,"released":"2026_06","taxonomy":["Bacteria","Thermotogati","Deinococcota","Deinococci","Deinococcales","Deinococcaceae","Deinococcus"],"regions":[{"start":139,"end":148,"reference_id":"16368685","reference_source":"pmid","reference_html":"Crystal structure of a bacterial type IB DNA topoisomerase reveals a preassembled active site in the absence of DNA. <i> Patel A, Shuman S, Mondragón A. </i> J Biol Chem, 2006","date":"2026-06-05T14:42:08.911Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04526r001","statement":[{"text":"Most of the amino acids in the C domain were clearly visible in the electron density map (e.g. see Fig. 2), except for a disordered loop from residues 139–148.","type":"Results"}],"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":124,"end":124,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":127,"end":127,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":192,"end":192,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":331,"end":331,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"2F4Q"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-05T14:44:48.136Z"}},{"start":25,"end":38,"reference_id":"16368685","reference_source":"pmid","reference_html":"Crystal structure of a bacterial type IB DNA topoisomerase reveals a preassembled active site in the absence of DNA. <i> Patel A, Shuman S, Mondragón A. </i> J Biol Chem, 2006","date":"2026-06-05T14:44:22.626Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":1,"end":1,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":124,"end":124,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":127,"end":127,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":192,"end":192,"position":"Specific residue"},{"term_id":"MOD:00530 ","term_name":"L-selenomethionine","term_namespace":"Non-standard amino acid","start":331,"end":331,"position":"Specific residue"}],"cross_refs":[{"db":"PDB","id":"2F4Q"}],"region_id":"DP04526r002","statement":[{"text":"The density in the N domain was of poorer quality, with several disordered loops and missing side chains, especially near the amino terminus.","type":"Results"},{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":139,"end":148,"reference_id":"20541510","reference_source":"pmid","reference_html":"Crystal structure of a bacterial topoisomerase IB in complex with DNA reveals a secondary DNA binding site. <i> Patel A, Yakovleva L, Shuman S, Mondragón A. </i> Structure, 2010","date":"2026-06-05T14:58:33.712Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"3M4A"}],"region_id":"DP04526r003","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence: 5'-GAATAAGGGCGC."}]}],"statement":[{"text":"Moreover, the 139GSDIYARQHK148 peptide is disordered in the crystal structure of apo-DraTopIB (Patel et al., 2006). In contrast, we find presently that in the DraTopIB-DNA cocrystal, the previously disordered peptide segment forms a well-ordered α helix that mimics the specificity helix of poxvirus TopIB (Figure 2B).","type":"Results"},{"text":"The equivalent α helix in DraTopIB makes a single (nonspecific) contact to a backbone phosphate in a symmetry-related 12-mer DNA and one contact to a nucleobase.","type":"Results"}]},{"start":139,"end":148,"reference_id":"20541510","reference_source":"pmid","reference_html":"Crystal structure of a bacterial topoisomerase IB in complex with DNA reveals a secondary DNA binding site. <i> Patel A, Yakovleva L, Shuman S, Mondragón A. </i> Structure, 2010","date":"2026-06-05T15:00:18.472Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"2F4Q"},{"db":"PDB","id":"3M4A"}],"region_id":"DP04526r004","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence: 5'-GAATAAGGGCGC."}]}],"statement":[{"text":"Moreover, the 139GSDIYARQHK148 peptide is disordered in the crystal structure of apo-DraTopIB (Patel et al., 2006). In contrast, we find presently that in the DraTopIB-DNA cocrystal, the previously disordered peptide segment forms a well-ordered α helix that mimics the specificity helix of poxvirus TopIB (Figure 2B).","type":"Results"},{"text":"Because the catalytic Arg137 is already poised in the active site in the DraTopIB apoenzyme, we presume that the induced folding of the specificity helix is critical for recognition of the target sites for DNA transesterification, which (though clearly different from that of the poxvirus TopIB) are presently uncharted.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","states_connection":[{"source":"DP04526r001","target":"DP04526r003"}]},{"start":10,"end":39,"reference_id":"20541510","reference_source":"pmid","reference_html":"Crystal structure of a bacterial topoisomerase IB in complex with DNA reveals a secondary DNA binding site. <i> Patel A, Yakovleva L, Shuman S, Mondragón A. </i> Structure, 2010","date":"2026-06-05T15:01:51.937Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"3M4A"}],"region_id":"DP04526r005","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence: 5'-GAATAAGGGCGC."}]}],"statement":[{"text":"After refinement, the entire DNA and most of the C-terminal domain were built, but some regions of the N-terminal domain were disordered.","type":"Methods"},{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"__v":0,"disorder_content":0.11560693641618497,"disprot_consensus":{"full":[{"start":10,"end":39,"type":"D"},{"start":139,"end":148,"type":"T"}],"Structural state":[{"start":10,"end":39,"type":"D"},{"start":139,"end":148,"type":"D"}],"Structural transition":[{"start":139,"end":148,"type":"T"}]}},{"acc":"P03700","sequence":"MGRRRSHERRDLPPNLYIRNNGYYCYRDPRTGKEFGLGRDRRIAITEAIQANIELFSGHKHKPLTARINSDNSVTLHSWLDRYEKILASRGIKQKTLINYMSKIKAIRRGLPDAPLEDITTKEIAAMLNGYIDEGKAASAKLIRSTLSDAFREAIAEGHITTNHVAATRAAKSEVRRSRLTADEYLKIYQAAESSPCWLRLAMELAVVTGQRVGDLCEMKWSDIVDGYLYVEQSKTGVKIAIPTALHIDALGISMKETLDKCKEILGGETIIASTRREPLSSGTVSRYFMRARKASGLSFEGDPPTFHELRSLSARLYEKQISDKFAQHLLGHKSDTMASQYRDDRGREWDKIEIK","creator":"rpancsa","dataset":["Viral proteins"],"date":"2026-01-02T10:42:56.828Z","disprot_id":"DP04527","features":{"pfam":[{"id":"PF00589","name":"Phage integrase family","start":179,"end":345},{"id":"PF02899","name":"Phage integrase, N-terminal SAM-like domain","start":81,"end":158},{"id":"PF09003","name":"Bacteriophage lambda integrase, Arm DNA-binding domain","start":1,"end":69}]},"genes":[{"name":{"value":"int","_id":"6957a13138549a2e1d36ce96","evidences":[]},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"6957a13138549a2e1d36ce95"}],"length":356,"name":"Integrase","ncbi_taxon_id":2681611,"organism":"Escherichia phage lambda","regions_counter":18,"released":"2026_06","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Uroviricota","Caudoviricetes","Lambdavirus","Lambdavirus lambda"],"regions":[{"start":1,"end":10,"reference_id":"11904406","reference_source":"pmid","reference_html":"Arm-site binding by lambda -integrase: solution structure and functional characterization of its amino-terminal domain. <i> Wojciak JM, Sarkar D, Landy A, Clubb RT. </i> Proc Natl Acad Sci U S A, 2002","date":"2026-01-02T11:05:37.892Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04527r001","statement":[{"text":"Residues Met-1-Arg-10 and Lys-60-Leu-64 do not exhibit any long-range NOEs and were omitted from the final simulated annealing calculations.","type":"Methods"},{"text":"Residues Arg-3–Arg-10 and Lys-60–Leu-64 are disordered in the structure and highly mobile on the picosecond time scale, as judged by the small magnitude of their 15N-{1H} heteronuclear NOEs (less than 0.4, Fig. 2C).","type":"Results"},{"text":"Although the first 10 aa of the INT-DBD1–64 are unstructured and flexible in the absence of DNA, this portion of the polypeptide contains three sequential Arg residues (Arg-3–Arg-5), which are of the correct charge to interact with DNA.","type":"Results"}],"cross_refs":[{"db":"PDB","id":"1KJK"}],"last_modified_by":"rpancsa","last_modified_name":"Rita Pancsa","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-05T15:07:24.953Z"}},{"start":3,"end":10,"reference_id":"11904406","reference_source":"pmid","reference_html":"Arm-site binding by lambda -integrase: solution structure and functional characterization of its amino-terminal domain. <i> Wojciak JM, Sarkar D, Landy A, Clubb RT. </i> Proc Natl Acad Sci U S A, 2002","date":"2026-01-02T11:05:25.835Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"EXP","region_id":"DP04527r002","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Results","text":"However, when the 14-bp duplex DNA containing the P′1 site is added, these cross-peaks are affected significantly, exhibiting either large changes in their chemical shifts or resonance line-broadening (Fig. 4C). These data support the biochemical studies (Fig. 3) and suggest that the β-sheet and N-terminal tail comprise or are near the protein–DNA interface."}]}],"statement":[{"text":"For example, in the absence of DNA, the amide cross-peaks of residues Arg-3 to Arg-10 exhibit narrow line-widths and chemical shifts that indicate they adopt a random-coil conformation (Fig. 4C). However, when the 14-bp duplex DNA containing the P′1 site is added, these cross-peaks are affected significantly, exhibiting either large changes in their chemical shifts or resonance line-broadening (Fig. 4C). These data support the biochemical studies (Fig. 3) and suggest that the β-sheet and N-terminal tail comprise or are near the protein–DNA interface.","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-05T15:30:01.318Z"}},{"start":1,"end":10,"reference_id":"11904406","reference_source":"pmid","reference_html":"Arm-site binding by lambda -integrase: solution structure and functional characterization of its amino-terminal domain. <i> Wojciak JM, Sarkar D, Landy A, Clubb RT. </i> Proc Natl Acad Sci U S A, 2002","date":"2026-06-05T15:06:56.927Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"1KJK"}],"region_id":"DP04527r003","statement":[{"text":"Residues Met-1-Arg-10 and Lys-60-Leu-64 do not exhibit any long-range NOEs and were omitted from the final simulated annealing calculations.","type":"Methods"},{"text":"Residues Arg-3–Arg-10 and Lys-60–Leu-64 are disordered in the structure and highly mobile on the picosecond time scale, as judged by the small magnitude of their 15N-{1H} heteronuclear NOEs (less than 0.4, Fig. 2C).","type":"Results"}]},{"start":1,"end":10,"reference_id":"19324050","reference_source":"pmid","reference_html":"NMR structure of the amino-terminal domain of the lambda integrase protein in complex with DNA: immobilization of a flexible tail facilitates beta-sheet recognition of the major groove. <i> Fadeev EA, Sam MD, Clubb RT. </i> J Mol Biol, 2009","date":"2026-06-05T15:37:02.530Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"2WCC"}],"region_id":"DP04527r004","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Results","text":"NMR was used to determine the structure of the N-terminal domain of Int (IntN, residues Met 1 to Leu 64) in complex with a 15-base pair oligonucleotide corresponding to the P’2 arm-type site within the phage (5′- G CAG TCA AAA T C -3′// 3′- C GTC AGT TTT A G -5′, binding site underlined)."}]}],"statement":[{"text":"However, in the structure of the IntN-DNA complex this core domain is supplemented by an ordered amino-terminal extension that has not been observed previously (colored green in Fig. 2B). This appendage immediately precedes the beta-sheet and consists of a 310 helix (Glu8 to Arg10) that rests against the phosphodiester backbone of the duplex, and an amino-terminal tail that is inserted deep into the minor groove. The presence of the 310 helix and other secondary structural elements is substantiated by characteristic NOE patterns in the NOESY data (Fig. S2).","type":"Results"}]},{"start":1,"end":10,"reference_id":"19324050","reference_source":"pmid","reference_html":"NMR structure of the amino-terminal domain of the lambda integrase protein in complex with DNA: immobilization of a flexible tail facilitates beta-sheet recognition of the major groove. <i> Fadeev EA, Sam MD, Clubb RT. </i> J Mol Biol, 2009","date":"2026-06-05T15:38:52.649Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"2WCC"}],"region_id":"DP04527r005","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Results","text":"NMR was used to determine the structure of the N-terminal domain of Int (IntN, residues Met 1 to Leu 64) in complex with a 15-base pair oligonucleotide corresponding to the P’2 arm-type site within the phage (5′- G CAG TCA AAA T C -3′// 3′- C GTC AGT TTT A G -5′, binding site underlined)."}]}],"statement":[{"text":"In the NMR structure of IntN solved the absence of DNA these residues are part of an eleven amino acid disordered tail that precedes strand B1 15. Electron density for these residues is also absent in all previously reported crystal structures of full-length Int 16. Our results indicate that the tail undergoes a disordered-ordered transition upon binding the duplex as result of extensive hydrogen bonding to the minor groove. ","type":"Results"},{"text":"In the apo-form, residues preceding strand B1 are unfolded and dynamic as evidenced by small magnitude or negative NOE values. However, upon complex formation the entire N-terminus becomes ordered, as its residues exhibit large NOE values similar to amino acids in the remainder of the domain.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","states_connection":[{"source":"DP04527r001","target":"DP04527r004"}]},{"start":1,"end":9,"reference_id":"19324050","reference_source":"pmid","reference_html":"NMR structure of the amino-terminal domain of the lambda integrase protein in complex with DNA: immobilization of a flexible tail facilitates beta-sheet recognition of the major groove. <i> Fadeev EA, Sam MD, Clubb RT. </i> J Mol Biol, 2009","date":"2026-06-05T15:40:51.852Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"2WCC"}],"ec_go":"EXP","region_id":"DP04527r006","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Results","text":"NMR was used to determine the structure of the N-terminal domain of Int (IntN, residues Met 1 to Leu 64) in complex with a 15-base pair oligonucleotide corresponding to the P’2 arm-type site within the phage (5′- G CAG TCA AAA T C -3′// 3′- C GTC AGT TTT A G -5′, binding site underlined)."}]}],"statement":[{"text":"Inspection of the NMR structure reveals that DNA binding induces the folding of residues Glu8-Arg10 into a 310 helix as a result of stabilizing contacts from the side chains of Ser6 and Arg9 to the phosphates of Thy18 and Thy17, respectively (Fig. 3B). Residues Met1-Gly2-Arg3 preceding the 310 helix then extend into the minor groove enabling the backbone amide of Gly2 to hydrogen bond to the N3 group of Ade10 and the side chain of Met1 to form non-polar interactions with the Ade10-Thy11 base step (Fig. 3B). The tail is further positioned by contacts from by the side chain of Arg3, which is poised to interact with the phosphate of Gua19.","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false},{"start":2,"end":6,"reference_id":"11904406","reference_source":"pmid","reference_html":"Arm-site binding by lambda -integrase: solution structure and functional characterization of its amino-terminal domain. <i> Wojciak JM, Sarkar D, Landy A, Clubb RT. </i> Proc Natl Acad Sci U S A, 2002","date":"2026-06-05T16:01:53.697Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Arg3Arg4Arg5del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04527r007","statement":[{"text":"However, when two Arg residues are deleted to give a net loss of one positive charge (mutant G2KΔ2R), recombinase activity and arm-type DNA binding both are reduced. Deletion of three Arg residues (net loss of two positive charges) virtually abolishes arm-type DNA binding and recombinase activity. These results suggest that Arg-4 and Arg-5, which are disordered in the absence of DNA, nevertheless are important for recombinase activity, presumably because they are involved in arm-type DNA binding (see below).","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false},{"start":75,"end":176,"reference_id":"18001133","reference_source":"pmid","reference_html":"DNA recognition via mutual-induced fit by the core-binding domain of bacteriophage lambda integrase. <i> Kamadurai HB, Kamadurai HB, Foster MP. </i> Biochemistry, 2007","date":"2026-06-05T16:15:53.046Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04527r008","statement":[{"text":"The 15N-edited HSQC spectrum of free IntCB (Figure 2A) exhibits few well-resolved peaks, while also being marked by broad or less dispersed, intense peaks. The scarcity of peaks in the spectrum is indicative of severe resonance broadening due to exchange between multiple conformational states, suggesting that IntCB is not a well-folded protein domain.","type":"Results"}]},{"start":75,"end":176,"reference_id":"18001133","reference_source":"pmid","reference_html":"DNA recognition via mutual-induced fit by the core-binding domain of bacteriophage lambda integrase. <i> Kamadurai HB, Kamadurai HB, Foster MP. </i> Biochemistry, 2007","date":"2026-06-05T16:19:29.529Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"BMRB","id":"15213"}],"region_id":"DP04527r009","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence 5'-GCTCAAGGGAGTACG."}]}],"statement":[{"text":"In contrast to the free protein, the HSQC spectrum of IntCB recorded in the presence of a cognate DNA half-site exhibits a nearly complete set of well-resolved NMR signals (Figure 2B). The appearance of well-resolved and well-dispersed signals indicates that in the presence of DNA the backbone amide protons populate unique environments as would be expected in a well-folded protein, suggesting that IntCB becomes better folded upon binding to DNA. Binding-coupled folding was not limited to interactions with the cognate DNA (a core half-site), as similar improvement in the spectrum was observed upon addition of a noncognate DNA ligand ( 15). ","type":"Results"}]},{"start":75,"end":176,"reference_id":"18001133","reference_source":"pmid","reference_html":"DNA recognition via mutual-induced fit by the core-binding domain of bacteriophage lambda integrase. <i> Kamadurai HB, Kamadurai HB, Foster MP. </i> Biochemistry, 2007","date":"2026-06-05T16:20:23.367Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"BMRB","id":"15213"}],"region_id":"DP04527r010","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence 5'-GCTCAAGGGAGTACG."}]}],"statement":[{"text":"NMR spectra reveal DNA-induced folding of IntCB. (A) 15N-edited HSQC spectrum of the free IntCB. Poor signal and limited dispersion in the spectrum are indicative of a poorly folded protein. (B) 15N-edited HSQC spectrum of IntCB in a 1:1 complex with the cognate DNA. An increase in the number of signals and their improved dispersion are consistent with binding-coupled folding of IntCB.","type":"Results"},{"text":"Binding-coupled folding was not limited to interactions with the cognate DNA (a core half-site), as similar improvement in the spectrum was observed upon addition of a noncognate DNA ligand ( 15).","type":"Results"}]},{"start":75,"end":176,"reference_id":"18001133","reference_source":"pmid","reference_html":"DNA recognition via mutual-induced fit by the core-binding domain of bacteriophage lambda integrase. <i> Kamadurai HB, Kamadurai HB, Foster MP. </i> Biochemistry, 2007","date":"2026-06-05T16:25:01.346Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006200","ec_ontology":"ECO","ec_name":"circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04527r011","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence 5'-GCTCAAGGGAGTACG"}]}],"statement":[{"text":"The CD spectrum of free IntCB exhibited signal minima at 208 and 220 nm, as expected for a helical protein ( 12), indicating the presence of significant secondary structure. The amplitude of the CD signal at 222 nm increased ∼15% in the presence of equimolar amounts of DNA (i.e., compare the “Sum” and “Complex” spectra), indicating that DNA binding increases the secondary structure content of IntCB (Figure 3A).","type":"Results"},{"text":"The melting curve of free IntCB was very broad and  incomplete over the sampled temperature range, indicative of noncooperative unfolding. In contrast, the IntCB−DNA complex exhibits a classical sigmoidal feature during thermal denaturation (Figure 3B), indicative of a well-folded structure that unfolds cooperatively ( 12, 16).","type":"Results"},{"text":"Titration of DNA with IntCB resulted in an incremental increase in intensity in the near-UV region of the spectrum, indicating structural changes in the DNA upon binding to IntCB (Figure 3C).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":75,"end":176,"reference_id":"18001133","reference_source":"pmid","reference_html":"DNA recognition via mutual-induced fit by the core-binding domain of bacteriophage lambda integrase. <i> Kamadurai HB, Kamadurai HB, Foster MP. </i> Biochemistry, 2007","date":"2026-06-05T16:24:08.990Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006200","ec_ontology":"ECO","ec_name":"circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04527r012","statement":[{"text":"The CD spectrum of free IntCB exhibited signal minima at 208 and 220 nm, as expected for a helical protein ( 12), indicating the presence of significant secondary structure.","type":"Results"},{"text":"The melting curve of free IntCB was very broad and  incomplete over the sampled temperature range, indicative of noncooperative unfolding.","type":"Results"},{"text":"Circular dichroism spectroscopy of free IntCB shows an α-helical signature (minima at 208 and 220 nm); however, thermal denaturation monitored at 222 nm is highly non-cooperative, indicating the absence of a stable, cooperatively folded tertiary structure.","type":"Curator statement"}]},{"start":75,"end":176,"reference_id":"18001133","reference_source":"pmid","reference_html":"DNA recognition via mutual-induced fit by the core-binding domain of bacteriophage lambda integrase. <i> Kamadurai HB, Kamadurai HB, Foster MP. </i> Biochemistry, 2007","date":"2026-06-05T16:27:53.944Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006336","ec_ontology":"ECO","ec_name":"intrinsic fluorescence-based protein conformation evidence","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04527r013","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence 5'-GCTCAAGGGAGTACG."}]}],"statement":[{"text":"The data could be fit, however, to a model allowing for multiple IntCB-binding sites on the DNA, yielding an apparent dissociation constant KD of 34 ± 10 nM and 2 ± 0.03 binding sites (n) for the 15 bp cognate DNA. Titration experiments with a noncognate DNA of similar size yielded a similar value for n, but weaker binding (KD = 80 ± 20 nM); since the signal being monitored reports on protein folding, these data indicate IntCB folding does not require a cognate DNA sequence. Experiments with a longer 29 bp noncognate DNA revealed similar weak binding (KD = 89 ± 13 nM), but n increased to ∼6.5, reflecting the capacity of IntCB for nonspecific DNA binding (Figure 5B).","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false},{"start":75,"end":176,"reference_id":"18001133","reference_source":"pmid","reference_html":"DNA recognition via mutual-induced fit by the core-binding domain of bacteriophage lambda integrase. <i> Kamadurai HB, Kamadurai HB, Foster MP. </i> Biochemistry, 2007","date":"2026-06-05T16:28:58.528Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IPI","region_id":"DP04527r014","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence 5'-GCTCAAGGGAGTACG."}]}],"statement":[{"text":"Thus, these experiments demonstrate that IntCB is capable of binding the 15 bp half-site DNA with a 2:1 stoichiometry when the DNA concentration is limiting, but with a 1:1 stoichiometry when the DNA is in excess. Importantly, the data establish thermodynamic parameters for the two classes of binding sites, which we classify as arising from “specific” (tighter) and “nonspecific” (weaker) protein−DNA interactions.","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false},{"start":75,"end":80,"reference_id":"18001133","reference_source":"pmid","reference_html":"DNA recognition via mutual-induced fit by the core-binding domain of bacteriophage lambda integrase. <i> Kamadurai HB, Kamadurai HB, Foster MP. </i> Biochemistry, 2007","date":"2026-06-05T16:57:55.617Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"ec_go":"EXP","region_id":"DP04527r015","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence 5'-GCTCAAGGGAGTACG."}]}],"statement":[{"text":"Perturbations in the 1N−15H resonance shifts of IntCB during DNA titration from 2:1 to 1:1 molar equiv (protein:DNA) map to the protein−DNA interface. (A) 15N-edited HSQC spectra were recorded with 0.5 (black), 0.67 (magenta), 0.8 (red), 1.0 (green) and 1.2 molar equiv of DNA (blue) with respect to IntCB. The peaks that are significantly perturbed due to DNA addition are labeled.","type":"Figure"},{"text":"NMR chemical shift perturbation mapping of IntCB during titration from 2:1 to 1:1 protein:DNA molar ratio using a 15 bp cognate DNA half-site identifies residues in four regions (approximately residues 75–80, 90–109, 129–143, and 165–174) as part of the DNA-binding interface (Figure 7A). The strong inverse correlation between chemical shift perturbations and distance to DNA confirms that these perturbations reflect protein–DNA interactions rather than protein–protein contacts (Figure S2).","type":"Curator statement"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":90,"end":109,"reference_id":"18001133","reference_source":"pmid","reference_html":"DNA recognition via mutual-induced fit by the core-binding domain of bacteriophage lambda integrase. <i> Kamadurai HB, Kamadurai HB, Foster MP. </i> Biochemistry, 2007","date":"2026-06-05T16:59:47.203Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"ec_go":"EXP","region_id":"DP04527r016","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence 5'-GCTCAAGGGAGTACG."}]}],"statement":[{"text":"Perturbations in the 1N−15H resonance shifts of IntCB during DNA titration from 2:1 to 1:1 molar equiv (protein:DNA) map to the protein−DNA interface. (A) 15N-edited HSQC spectra were recorded with 0.5 (black), 0.67 (magenta), 0.8 (red), 1.0 (green) and 1.2 molar equiv of DNA (blue) with respect to IntCB. The peaks that are significantly perturbed due to DNA addition are labeled.","type":"Figure"},{"text":"NMR chemical shift perturbation mapping of IntCB identifies residues in the region 95-100 as showing the largest perturbations upon DNA binding (Δδ ~0.12 ppm), consistent with direct involvement in the DNA-binding interface (Figure 7A, Figure S2). Residue N99 within this region mediates the sole base-specific contact with the cognate DNA.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":129,"end":143,"reference_id":"18001133","reference_source":"pmid","reference_html":"DNA recognition via mutual-induced fit by the core-binding domain of bacteriophage lambda integrase. <i> Kamadurai HB, Kamadurai HB, Foster MP. </i> Biochemistry, 2007","date":"2026-06-05T17:00:29.983Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"EXP","region_id":"DP04527r017","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence 5'-GCTCAAGGGAGTACG."}]}],"statement":[{"text":"Perturbations in the 1N−15H resonance shifts of IntCB during DNA titration from 2:1 to 1:1 molar equiv (protein:DNA) map to the protein−DNA interface. (A) 15N-edited HSQC spectra were recorded with 0.5 (black), 0.67 (magenta), 0.8 (red), 1.0 (green) and 1.2 molar equiv of DNA (blue) with respect to IntCB. The peaks that are significantly perturbed due to DNA addition are labeled.","type":"Figure"},{"text":"NMR chemical shift perturbation mapping of IntCB during titration from 2:1 to 1:1 protein:DNA molar ratio using a 15 bp cognate DNA half-site identifies residues in four regions (approximately residues 75–80, 90–109, 129–143, and 165–174) as part of the DNA-binding interface (Figure 7A). The strong inverse correlation between chemical shift perturbations and distance to DNA confirms that these perturbations reflect protein–DNA interactions rather than protein–protein contacts (Figure S2).","type":"Curator statement"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false},{"start":165,"end":174,"reference_id":"18001133","reference_source":"pmid","reference_html":"DNA recognition via mutual-induced fit by the core-binding domain of bacteriophage lambda integrase. <i> Kamadurai HB, Kamadurai HB, Foster MP. </i> Biochemistry, 2007","date":"2026-06-05T17:00:40.307Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"EXP","region_id":"DP04527r018","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence 5'-GCTCAAGGGAGTACG."}]}],"statement":[{"text":"Perturbations in the 1N−15H resonance shifts of IntCB during DNA titration from 2:1 to 1:1 molar equiv (protein:DNA) map to the protein−DNA interface. (A) 15N-edited HSQC spectra were recorded with 0.5 (black), 0.67 (magenta), 0.8 (red), 1.0 (green) and 1.2 molar equiv of DNA (blue) with respect to IntCB. The peaks that are significantly perturbed due to DNA addition are labeled.","type":"Figure"},{"text":"NMR chemical shift perturbation mapping of IntCB during titration from 2:1 to 1:1 protein:DNA molar ratio using a 15 bp cognate DNA half-site identifies residues in four regions (approximately residues 75–80, 90–109, 129–143, and 165–174) as part of the DNA-binding interface (Figure 7A). The strong inverse correlation between chemical shift perturbations and distance to DNA confirms that these perturbations reflect protein–DNA interactions rather than protein–protein contacts (Figure S2).","type":"Curator statement"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false}],"__v":0,"disorder_content":0.3146067415730337,"disprot_consensus":{"full":[{"start":1,"end":10,"type":"T"},{"start":75,"end":176,"type":"T"}],"Structural state":[{"start":1,"end":10,"type":"D"},{"start":75,"end":176,"type":"D"}],"Molecular function":[{"start":1,"end":10,"type":"F"},{"start":75,"end":176,"type":"F"}],"Disorder function":[{"start":1,"end":10,"type":"F"}],"Structural transition":[{"start":1,"end":10,"type":"T"},{"start":75,"end":176,"type":"T"}]}},{"acc":"P22808","sequence":"MTTSASLERTPSKRDRDRERDNSSGLGSAGSLPASPQSAITVSPSSPATPKRPLRTSTPSLERKREREDREDREDRKERQERHERDRDHERFAAVFSTASTTVPTNTSSSSGLAPEQLRIPTGAAAFSGFPGLHSMSSLMLPSSAAVAAAAAAPFLPWSPILLPPWNHALLPAAFYPAALRNALPGLFDAKVPSSQRSGFHISDILNLEGSELKNAAAAAAAAAHHGSDLSHHSASESTSGHRGQGSHTSPSALSPTPAGVSADEHHNGSGTGGGAGEADHHSTTEHHAPPSHPQQQHPHHQQHHHPHLLLPQQHHQQAVAPLPLAHHQSGEAQSHAHANAAAAHLLASHNAAAAAAVAAGQYLPNLPKNFPGSFGDEMSSYHHMAQTMLQHSGRSAWIKENELYGTQQPASPDSTSPVTSEVSYTYIGSNCQTSPALSGDYKSYSRSADSDALSVGDALHTLHGSSGNGSAGGAPTAHALHNNNNNTTNNNNHSLKAEGINGAGSGHDDSLNEDGIEEDIDDVDDADGSGGGDANGSDGLPNKKRKRRVLFTKAQTYELERRFRQQRYLSAPEREHLASLIRLTPTQVKIWFQNHRYKTKRAQNEKGYEGHPGLLHGHATHPHHPSALPSPRRVAVPVLVRNGKPCLGDSSKLGADCVSVSSATATAMQNAAAHHLVALNGAAAYQHAAAAAAGLHAHAHAHAHAHGHGHPHAHAQRAAWWP","creator":"rpancsa","dataset":[],"date":"2026-01-02T12:08:02.449Z","disprot_id":"DP04528","features":{"pfam":[{"id":"PF00046","name":"Homeodomain","start":546,"end":602}]},"genes":[{"name":{"value":"vnd","_id":"6957b52238549a2e1d36cea3","evidences":[]},"synonyms":[{"value":"NK2","_id":"6957b52238549a2e1d36cea4","evidences":[]}],"olnNames":[],"orfNames":[{"value":"CG6172","_id":"6957b52238549a2e1d36cea5","evidences":[]}],"_id":"6957b52238549a2e1d36cea2"}],"length":723,"name":"Homeobox protein vnd","ncbi_taxon_id":7227,"organism":"Drosophila melanogaster","regions_counter":2,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"regions":[{"start":537,"end":549,"reference_id":"7643404","reference_source":"pmid","reference_html":"The three-dimensional solution structure of the NK-2 homeodomain from Drosophila. <i> Tsao DH, Gruschus JM, Wang LH, Nirenberg M, Ferretti JA. </i> J Mol Biol, 1995","date":"2026-01-21T15:52:27.275Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"1VND"}],"region_id":"DP04528r001","statement":[{"text":"The low number of cross-peaks for the N-terminal (residues −8 to 5) and the C-terminal (residues 65 to 77) is a result of lack of long range interactions for these residues, since the ends of the protein turned out to\nbe unstructured.","type":"Results"},{"text":"The 77-residue construct studied corresponds to residues 537 to 613 of the protein, UniProt P22808.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-04T16:42:46.922Z"}},{"start":597,"end":613,"reference_id":"7643404","reference_source":"pmid","reference_html":"The three-dimensional solution structure of the NK-2 homeodomain from Drosophila. <i> Tsao DH, Gruschus JM, Wang LH, Nirenberg M, Ferretti JA. </i> J Mol Biol, 1995","date":"2026-01-21T15:52:16.198Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"1VND"}],"region_id":"DP04528r002","statement":[{"text":"The low number of cross-peaks for the N-terminal (residues −8 to 5) and the C-terminal (residues 65 to 77) is a result of lack of long range interactions for these residues, since the ends of the protein turned out to\nbe unstructured.","type":"Results"},{"text":"The 77-residue construct studied corresponds to residues 537 to 613 of the protein, UniProt P22808.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-04T16:38:43.297Z"}}],"__v":0,"disorder_content":0.04149377593360996,"disprot_consensus":{"full":[{"start":537,"end":549,"type":"D"},{"start":597,"end":613,"type":"D"}],"Structural state":[{"start":537,"end":549,"type":"D"},{"start":597,"end":613,"type":"D"}]}},{"acc":"P04390","sequence":"MSLRSDLINALYDENQKYDVCGIISAEGKIYPLGSDTKVLSTIFELFSRPIINKIAEKHGYIVEEPKQQNHYPDFTLYKPSEPNKKIAIDIKTTYTNKENEKIKFTLGGYTSFIRNNTKNIVYPFDQYIAHWIIGYVYTRVATRKSSLKTYNINELNEIPKPYKGVKVFLQDKWVIAGDLAGSGNTTNIGSIHAHYKDFVEGKGIFDSEDEFLDYWRNYERTSQLRNDKYNNISEYRNWIYRGRK","creator":"rpancsa","dataset":[],"date":"2026-01-02T13:13:57.265Z","disprot_id":"DP04530","features":{"pfam":[{"id":"PF09233","name":"Restriction endonuclease EcoRV","start":15,"end":239}]},"genes":[{"name":{"value":"ecoRVR","_id":"6957c49538549a2e1d36cebd","evidences":[]},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"6957c49538549a2e1d36cebc"}],"length":245,"name":"Type II restriction enzyme EcoRV","ncbi_taxon_id":562,"organism":"Escherichia coli","regions_counter":4,"released":"2026_06","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"regions":[{"start":218,"end":245,"reference_id":"9367757","reference_source":"pmid","reference_html":"Conformational transitions and structural deformability of EcoRV endonuclease revealed by crystallographic analysis. <i> Perona JJ, Martin AM. </i> J Mol Biol, 1997","date":"2026-06-09T14:13:48.180Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":3,"cross_refs":[{"db":"PDB","id":"1AZ3"},{"db":"PDB","id":"1AZ4"}],"region_id":"DP04530r001","statement":[{"text":"Comparison of the free enzyme structure between the two crystal forms further reveals that the C-terminal 28 amino acid residues are disordered and undergo an extensive local folding transition upon DNA binding.","type":"Abstract"},{"text":"The crystal structure of EcoRV T93A determined in form B (see below) similarly shows a lack of interpretable electron density for residues 218 to 245 of subunit I.","type":"Results"},{"text":"Therefore, it appears that the final 28 amino acid residues Asn218 to Lys245 of EcoRV, including an α-helix spanning residues Ile233 to Tyr241, are at least partially disordered in the unliganded state. The ability to visualize C-terminal amino acid residues in subunits I and II of form A and subunit II of form B apparently arises from the formation of lattice contacts. Analysis of the crystal packing interactions shows that intermolecular contacts with C-terminal amino acid residues are present for each of these three monomers.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-09T14:13:50.577Z"}},{"start":218,"end":245,"reference_id":"9367757","reference_source":"pmid","reference_html":"Conformational transitions and structural deformability of EcoRV endonuclease revealed by crystallographic analysis. <i> Perona JJ, Martin AM. </i> J Mol Biol, 1997","date":"2026-06-09T14:15:31.211Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":3,"cross_refs":[{"db":"PDB","id":"1AZ0"}],"region_id":"DP04530r002","statement":[{"text":"Comparison of the free enzyme structure between the two crystal forms further reveals that the C-terminal 28 amino acid residues are disordered and undergo an extensive local folding transition upon DNA binding.","type":"Abstract"},{"text":"Comparison of the unliganded enzyme in form A with the enzyme-DNA complex had previously shown that a mobile surface loop at amino acid residues 221 to 228 becomes ordered during DNA binding (Winkler et al., 1993). This is an example of local ordering of a surface loop in response to DNA-binding, with interactions made by enzyme residues Arg221, Ser223 and Arg226. However, it now appears that these contacts may also promote the folding of a considerably larger portion of the enzyme. The folding transition may be triggered by intramolecular interactions formed between newly stabilized amino acid residues in the 221 to 228 loop and residues in the adjacent segments 229 to 232 and 218 to 220 (Figure 3).","type":"Results"},{"text":"A total of 33 amino acid residues per monomer encompassing the interactions of an enzyme surface loop in the DNA major groove (R-loop; Figure 4), together with the C-terminal 28 residues, become ordered during the binding event.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence 5'-AAAGATATCTT."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-09T14:15:34.248Z"}},{"start":218,"end":245,"reference_id":"9367757","reference_source":"pmid","reference_html":"Conformational transitions and structural deformability of EcoRV endonuclease revealed by crystallographic analysis. <i> Perona JJ, Martin AM. </i> J Mol Biol, 1997","date":"2026-06-09T14:10:08.296Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"1AZ4"},{"db":"PDB","id":"1AZ3"},{"db":"PDB","id":"1AZ0"}],"region_id":"DP04530r003","statement":[{"text":"Comparison of the free enzyme structure between the two crystal forms further reveals that the C-terminal 28 amino acid residues are disordered and undergo an extensive local folding transition upon DNA binding.","type":"Abstract"},{"text":"Comparison of the unliganded enzyme in form A with the enzyme-DNA complex had previously shown that a mobile surface loop at amino acid residues 221 to 228 becomes ordered during DNA binding (Winkler et al., 1993). This is an example of local ordering of a surface loop in response to DNA-binding, with interactions made by enzyme residues Arg221, Ser223 and Arg226. However, it now appears that these contacts may also promote the folding of a considerably larger portion of the enzyme. The folding transition may be triggered by intramolecular interactions formed between newly stabilized amino acid residues in the 221 to 228 loop and residues in the adjacent segments 229 to 232 and 218 to 220 (Figure 3).","type":"Results"},{"text":"Therefore, it appears that the final 28 amino acid residues Asn218 to Lys245 of EcoRV, including an a-helix spanning residues Ile233 to Tyr241, are at least partially disordered in the unliganded state.","type":"Results"},{"text":"A total of 33 amino acid residues per monomer encompassing the interactions of an enzyme surface loop in the DNA major groove (R-loop; Figure 4), together with the C-terminal 28 residues, become ordered during the binding event.","type":"Results"}],"states_connection":[{"source":"DP04530r001","target":"DP04530r002"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence 5'-AAAGATATCTT"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-09T14:15:43.384Z"}},{"start":219,"end":226,"reference_id":"9367757","reference_source":"pmid","reference_html":"Conformational transitions and structural deformability of EcoRV endonuclease revealed by crystallographic analysis. <i> Perona JJ, Martin AM. </i> J Mol Biol, 1997","date":"2026-06-09T14:25:22.937Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"1AZ0"}],"ec_go":"EXP","region_id":"DP04530r004","statement":[{"text":"Comparison of the free enzyme structure between the two crystal forms further reveals that the C-terminal 28 amino acid residues are disordered and undergo an extensive local folding transition upon DNA binding.","type":"Abstract"},{"text":"Comparison of the unliganded enzyme in form A with the enzyme-DNA complex had previously shown that a mobile surface loop at amino acid residues 221 to 228 becomes ordered during DNA binding (Winkler et al., 1993). This is an example of local ordering of a surface loop in response to DNA-binding, with interactions made by enzyme residues Arg221, Ser223 and Arg226.","type":"Results"},{"text":"A total of 33 amino acid residues per monomer encompassing the interactions of an enzyme surface loop in the DNA major groove (R-loop; Figure 4), together with the C-terminal 28 residues, become ordered during the binding event.","type":"Results"},{"text":"Side-chains that interact with DNA are shown in black. Arg221 interacts with DNA at the opposite side of the undecamer (not shown). The enzyme C terminus is indicated at the bottom.","type":"Figure"},{"text":"The residues shown with side chains in Figure 3 are Arg221, Ser223, Arg226, Tyr219, Asn231, Tyr230, and Ile233. Although not all of them make direct contacts with DNA, Arg221, Ser223, and Arg226 are the residues that have been confirmed to interact directly with the DNA.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-09T14:25:28.073Z"}}],"__v":0,"disorder_content":0.11428571428571428,"disprot_consensus":{"full":[{"start":218,"end":245,"type":"T"}],"Structural state":[{"start":218,"end":245,"type":"D"}],"Structural transition":[{"start":218,"end":245,"type":"T"}],"Molecular function":[{"start":219,"end":226,"type":"F"}]}},{"acc":"P34707","sequence":"MGGSSRRQRSTSATRRDDKRRRRQCFSSVADDEEETTSIYGVSSIFIWILATSSLILVISSPSSNTSIQSSSYDRITTKHLLDNISPTFKMYTDSNNRNFDEVNHQHQQEQDFNGQSKYDYPQFNRPMGLRWRDDQRMMEYFMSNGPVETVPVMPILTEHPPASPFGRGPSTERPTTSSRYEYSSPSLEDIDLIDVLWRSDIAGEKGTRQVAPADQYECDLQTLTEKSTVAPLTAEENARYEDLSKGFYNGFFESFNNNQYQQKHQQQQREQIKTPTLEHPTQKAELEDDLFDEDLAQLFEDVSREEGQLNQLFDNKQQHPVINNVSLSEGIVYNQANLTEMQEMRDSCNQVSISTIPTTSTAQPETLFNVTDSQTVEQWLPTEVVPNDVFPTSNYAYIGMQNDSLQAVVSNGQIDYDHSYQSTGQTPLSPLIIGSSGRQQQTQTSPGSVTVTATATQSLFDPYHSQRHSFSDCTTDSSSTCSRLSSESPRYTSESSTGTHESRFYGKLAPSSGSRYQRSSSPRSSQSSIKIARVVPLASGQRKRGRQSKDEQLASDNELPVSAFQISEMSLSELQQVLKNESLSEYQRQLIRKIRRRGKNKVAARTCRQRRTDRHDKMSHYI","creator":"rpancsa","dataset":["Stress response proteins"],"date":"2026-01-02T14:49:05.311Z","disprot_id":"DP04531","features":{"pfam":[{"id":"PF03131","name":"bZIP Maf transcription factor","start":566,"end":618}]},"genes":[{"name":{"value":"skn-1","_id":"6957dae138549a2e1d36cedb","evidences":[]},"synonyms":[],"olnNames":[],"orfNames":[{"value":"T19E7.2","_id":"6957dae138549a2e1d36cedc","evidences":[]}],"_id":"6957dae138549a2e1d36ceda"}],"length":623,"name":"Protein skinhead-1","ncbi_taxon_id":6239,"organism":"Caenorhabditis elegans","regions_counter":16,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Nematoda","Chromadorea","Rhabditida","Rhabditina","Rhabditomorpha","Rhabditoidea","Rhabditidae","Peloderinae","Caenorhabditis"],"regions":[{"start":601,"end":615,"reference_id":"9159111","reference_source":"pmid","reference_html":"Skn-1: evidence for a bipartite recognition helix in DNA binding. <i> Pal S, Lo MC, Schmidt D, Pelczer I, Thurber S, Walker S. </i> Proc Natl Acad Sci U S A, 1997","date":"2026-01-02T15:00:21.996Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04531r001","statement":[{"text":"Sequential assignments have been made for residues L16–R59. In addition, several of the resonances in the basic region of N5-C77 have been assigned, including N63, V65, A66, A67, T69, S70, and T75. These basic region residues have 1H chemical shifts very close to the random coil values, supporting the CD studies which suggested that the basic region is unstructured in solution.","type":"Results"},{"text":"Based on Figure 1, the N5-C77 construct studied by NMR corresponds to residues 543-615 of Skn-1 (UniProt: P34707). The C-terminal tail of the studied construct comprises the basic region, which is disordered.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-05T17:04:46.050Z"}},{"start":596,"end":623,"reference_id":"7939715","reference_source":"pmid","reference_html":"Formation of a monomeric DNA binding domain by Skn-1 bZIP and homeodomain elements. <i> Blackwell TK, Bowerman B, Priess JR, Weintraub H. </i> Science, 1994","date":"2026-06-09T13:32:20.183Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"ec_go":"IMP","region_id":"DP04531r002","statement":[{"text":"In contrast, DNA binding is dramatically reduced (undetectable) by either deletion of nine amino acids from the NH2-terminus of the Skn domain (Δ1-9; Fig. 4B, lane 4), or by removal of the BR from Skn-1 (ΔS; Fig. 4A) (15).","type":"Article"},{"text":"Skn-1 deletion mutants, dia-grammed approximately to scale. In ΔS 28 COOH-terminal Skn-1 residues have been de-leted.","type":"Figure"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Arg596Ile623del","start":null,"end":null,"position":null}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":" Interacting dsDNA with sequence 5'- TGACAATGTCATCCC."}]}],"sequence_construct":"ASGQRKRGRQSKDEQLASDNELPVSAFQISEMSLSELQQVLKNESLSEYQRQLIRKI","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-09T13:32:22.699Z"}},{"start":599,"end":615,"reference_id":"9671699","reference_source":"pmid","reference_html":"The solution structure of the DNA-binding domain of Skn-1. <i> Lo MC, Ha S, Pelczer I, Pal S, Walker S. </i> Proc Natl Acad Sci U S A, 1998","date":"2026-01-02T16:43:47.059Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04531r003","statement":[{"text":"The data show that the protein is unstructured from residues 1–8 and 57–73, as indicated by near-random coil chemical shift values (32) for the Cα protons of spin systems that can be assigned, including the two threonines, two alanines, and one valine in the basic region (Fig. 1b). In addition, the amides assigned to the N and C termini of the protein have negative 1H-15N NOEs (Fig. 2a) and significantly longer 15N T1 and T2 relaxation times (Fig. 2 b and c) than amides in the internal region of the protein. The lack of structure leads to extensive resonance overlap and weak sequential NOEs, so it was not possible to complete sequence-specific assignments for the N- and C-terminal residues from homonuclear experiments.","type":"Results"},{"text":"Residues 57-73 of the studied construct correspond to residues 599-615 in the full Skn-1 protein sequence.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-08T15:11:48.778Z"}},{"start":539,"end":623,"reference_id":"9303538","reference_source":"pmid","reference_html":"SKN-1 domain folding and basic region monomer stabilization upon DNA binding. <i> Carroll AS, Gilbert DE, Liu X, Cheung JW, Michnowicz JE, Wagner G, Ellenberger TE, Blackwell TK. </i> Genes Dev, 1997","date":"2026-06-08T19:42:14.280Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":5,"ec_go":"EXP","region_id":"DP04531r004","statement":[{"text":"At 25°C, the far-ultraviolet CD spectrum of the free Skn-domain displays the characteristic α-helix minimum at 222 nm and indicates a helical content of ∼26% (Fig. 2A, see Materials and Methods). When bound to cognate DNA, the helical content of the Skn domain is ∼46% (Fig. 2A), an increase consistent with formation of a BR α-helix. Addition of nonspecific DNA does not affect the Skn domain CD spectrum (not shown), indicating that this folding transition requires specific DNA binding.","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence 5'- TGACAATGTCATCCC"}]}]},{"start":539,"end":623,"reference_id":"9303538","reference_source":"pmid","reference_html":"SKN-1 domain folding and basic region monomer stabilization upon DNA binding. <i> Carroll AS, Gilbert DE, Liu X, Cheung JW, Michnowicz JE, Wagner G, Ellenberger TE, Blackwell TK. </i> Genes Dev, 1997","date":"2026-01-02T18:12:07.234Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"EXP","region_id":"DP04531r005","statement":[{"text":"Comparison of heteronuclear single-quantum coherence (HSQC) spectra (Fig. 6B) of the free Skn domain, however, and of a 1:1 complex of the Skn domain bound specifically to DNA, reveals structural changes accompanying DNA binding. The free protein spectrum (Fig. 6B, panel 1) is highly overlapped and has a narrow range of amide proton chemical shifts, consistent with α-helical and random coil structure. In contrast, the spectrum of the complex (Fig. 6B, panel 2) shows much improved resolution of the cross peaks, and a somewhat broader range of amide proton chemical shifts, consistent with the BR becoming helical and the Skn domain adopting a tertiary structure.","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-08T19:45:12.608Z"}},{"start":593,"end":615,"reference_id":"9628487","reference_source":"pmid","reference_html":"A new DNA-binding motif in the Skn-1 binding domain-DNA complex. <i> Rupert PB, Daughdrill GW, Bowerman B, Matthews BW. </i> Nat Struct Biol, 1998","date":"2026-06-09T13:51:15.711Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"cross_refs":[{"db":"PDB","id":"1SKN"}],"ec_go":"EXP","region_id":"DP04531r006","statement":[{"text":"At the C-terminus, a helix extends from the domain to occupy the major groove of DNA in a manner similar to bZip proteins.","type":"Article"},{"text":"Arg 506 and Arg 503 both interact with the phosphate oxygen of Gua-B4.","type":"Article"},{"text":"Arg 508, Lys 460 and Arg 507 all interact with the phosphate oxygens of Cyt-Al0.","type":"Article"},{"text":"The side chains of Ala 514 and Cys 518 make van der Waals contacts\nwith C7 of Thy-B7.\n","type":"Article"},{"text":"NH2 of Arg 519 forms a hydrogen bond to N7 of Gua-A8. The presence of an equivalent nitrogen on adenine explains the ability of Skn-1 to bind to either purine base. The methyl of Ala 515 makes van der Waals contacts with C7 of Thy-A9. Asn 511 makes hydrogen bonds to both N4 of Cyt-AlO and 04 of Thy-B7. The side chains of Ala 514 and Cys 518 make van der Waals contacts with C7 ofThy-B7.","type":"Curator statement"},{"text":"Arg 521 forms a salt bridge with the phosphate of Thy-B7, and Arg 522 contacts the phosphate of Gua-B8. Finally, Arg 525 weakly interacts with the phosphate of Thy-B7.","type":"Curator statement"},{"text":"Author residue numbering has been mapped to the UniProt canonical sequence. The authors report interaction with DNA for residues 547, 550, 572, 593, 596, 597, 598, 600, 601, 602, 605, 606, 607, 608, 609, 611, 612 and 615.","type":"Title"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence 5'- TGACAATGTCATCCC."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-09T13:51:24.941Z"}},{"start":598,"end":619,"reference_id":"9628487","reference_source":"pmid","reference_html":"A new DNA-binding motif in the Skn-1 binding domain-DNA complex. <i> Rupert PB, Daughdrill GW, Bowerman B, Matthews BW. </i> Nat Struct Biol, 1998","date":"2026-06-08T15:47:11.859Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"1SKN"}],"region_id":"DP04531r007","statement":[{"text":"At the C-terminus, a helix extends from the domain to occupy the major groove of DNA in a manner similar to bZip proteins.","type":"Results"},{"text":"In the X-ray structure of the DNA-bound form the disordered basic region adopts a folded, a-helical form, contacting the major groove of the DNA.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence 5'- TGACAATGTCATCCC"}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"131762","entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-08T15:47:21.125Z"}},{"start":598,"end":619,"reference_id":"9628487","reference_source":"pmid","reference_html":"A new DNA-binding motif in the Skn-1 binding domain-DNA complex. <i> Rupert PB, Daughdrill GW, Bowerman B, Matthews BW. </i> Nat Struct Biol, 1998","date":"2026-06-08T17:11:23.238Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"1SKN"}],"region_id":"DP04531r008","statement":[{"text":"At the C-terminus, a helix extends from the domain to occupy the major groove of DNA in a manner similar to bZip proteins.","type":"Results"},{"text":"In the X-ray structure of the DNA-bound form the disordered basic region adopts a folded, a-helical form, contacting the major groove of the DNA.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","states_connection":[{"source":"DP04531r003","target":"DP04531r007"}],"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence 5'- TGACAATGTCATCCC"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-08T17:11:45.620Z"}},{"start":598,"end":615,"reference_id":"9303538","reference_source":"pmid","reference_html":"SKN-1 domain folding and basic region monomer stabilization upon DNA binding. <i> Carroll AS, Gilbert DE, Liu X, Cheung JW, Michnowicz JE, Wagner G, Ellenberger TE, Blackwell TK. </i> Genes Dev, 1997","date":"2026-06-08T15:47:41.890Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"region_id":"DP04531r009","statement":[{"text":"Comparison of heteronuclear single-quantum coherence (HSQC) spectra (Fig. 6B) of the free Skn domain, however, and of a 1:1 complex of the Skn domain bound specifically to DNA, reveals structural changes accompanying DNA binding. The free protein spectrum (Fig. 6B, panel 1) is highly overlapped and has a narrow range of amide proton chemical shifts, consistent with α-helical and random coil structure. In contrast, the spectrum of the complex (Fig. 6B, panel 2) shows much improved resolution of the cross peaks, and a somewhat broader range of amide proton chemical shifts, consistent with the BR becoming helical and the Skn domain adopting a tertiary structure.","type":"Results"},{"text":"In the DNA-bound form, the BR region folds up on binding into helical conformation.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","states_connection":[{"source":"DP04531r010","target":"DP04531r011"}],"sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence 5'- TGACAATGTCATCCC"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-08T17:11:02.497Z"}},{"start":598,"end":615,"reference_id":"9303538","reference_source":"pmid","reference_html":"SKN-1 domain folding and basic region monomer stabilization upon DNA binding. <i> Carroll AS, Gilbert DE, Liu X, Cheung JW, Michnowicz JE, Wagner G, Ellenberger TE, Blackwell TK. </i> Genes Dev, 1997","date":"2026-01-02T18:40:08.000Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04531r010","statement":[{"text":"Comparison of heteronuclear single-quantum coherence (HSQC) spectra (Fig. 6B) of the free Skn domain, however, and of a 1:1 complex of the Skn domain bound specifically to DNA, reveals structural changes accompanying DNA binding. The free protein spectrum (Fig. 6B, panel 1) is highly overlapped and has a narrow range of amide proton chemical shifts, consistent with α-helical and random coil structure. In contrast, the spectrum of the complex (Fig. 6B, panel 2) shows much improved resolution of the cross peaks, and a somewhat broader range of amide proton chemical shifts, consistent with the BR becoming helical and the Skn domain adopting a tertiary structure.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-08T15:40:34.516Z"}},{"start":598,"end":615,"reference_id":"9303538","reference_source":"pmid","reference_html":"SKN-1 domain folding and basic region monomer stabilization upon DNA binding. <i> Carroll AS, Gilbert DE, Liu X, Cheung JW, Michnowicz JE, Wagner G, Ellenberger TE, Blackwell TK. </i> Genes Dev, 1997","date":"2026-06-08T15:42:48.901Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04531r011","statement":[{"text":"Comparison of heteronuclear single-quantum coherence (HSQC) spectra (Fig. 6B) of the free Skn domain, however, and of a 1:1 complex of the Skn domain bound specifically to DNA, reveals structural changes accompanying DNA binding. The free protein spectrum (Fig. 6B, panel 1) is highly overlapped and has a narrow range of amide proton chemical shifts, consistent with α-helical and random coil structure. In contrast, the spectrum of the complex (Fig. 6B, panel 2) shows much improved resolution of the cross peaks, and a somewhat broader range of amide proton chemical shifts, consistent with the BR becoming helical and the Skn domain adopting a tertiary structure.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence 5'- TGACAATGTCATCCC"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-08T15:47:22.881Z"}},{"start":539,"end":623,"reference_id":"9303538","reference_source":"pmid","reference_html":"SKN-1 domain folding and basic region monomer stabilization upon DNA binding. <i> Carroll AS, Gilbert DE, Liu X, Cheung JW, Michnowicz JE, Wagner G, Ellenberger TE, Blackwell TK. </i> Genes Dev, 1997","date":"2026-06-08T16:57:40.985Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04531r012","statement":[{"text":"However, although numerous short and medium range NOEs define the α-helical secondary structures, no long-range NOEs are observed. This makes it impossible to orient the helices relative to one another and supports the idea that they are not folded in a stable tertiary structure.","type":"Results"},{"text":"A secondary structure in the absence of a tertiary fold is characteristic of a molten globule (Kuwajima 1989; Ptitsyn 1996).","type":"Discussion"},{"text":"The Skn domain is a native molten globule that folds to perform a specific function (BR stabilization).","type":"Discussion"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":539,"end":623,"reference_id":"9303538","reference_source":"pmid","reference_html":"SKN-1 domain folding and basic region monomer stabilization upon DNA binding. <i> Carroll AS, Gilbert DE, Liu X, Cheung JW, Michnowicz JE, Wagner G, Ellenberger TE, Blackwell TK. </i> Genes Dev, 1997","date":"2026-06-08T19:44:16.085Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000012","term_name":"molten globule to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"region_id":"DP04531r013","statement":[{"text":"At 25°C, the far-ultraviolet CD spectrum of the free Skn-domain displays the characteristic α-helix minimum at 222 nm and indicates a helical content of ∼26% (Fig. 2A, see Materials and Methods). When bound to cognate DNA, the helical content of the Skn domain is ∼46% (Fig. 2A), an increase consistent with formation of a BR α-helix. Addition of nonspecific DNA does not affect the Skn domain CD spectrum (not shown), indicating that this folding transition requires specific DNA binding.","type":"Results"},{"text":"When the Skn domain is denatured in the absence of specific DNA, its helical content decreases approximately linearly with temperature (as indicated by increasing ellipticity; Fig. 2B), showing that it has little stable tertiary structure. In contrast, the Skn-domain–DNA complex shows a broad cooperative unfolding transition that has a midpoint at 37°C (Fig. 2B), indicating that the Skn domain adopts a tertiary structure when it forms a complex with cognate DNA.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence 5'- TGACAATGTCATCCC"}]}]},{"start":539,"end":623,"reference_id":"9303538","reference_source":"pmid","reference_html":"SKN-1 domain folding and basic region monomer stabilization upon DNA binding. <i> Carroll AS, Gilbert DE, Liu X, Cheung JW, Michnowicz JE, Wagner G, Ellenberger TE, Blackwell TK. </i> Genes Dev, 1997","date":"2026-06-08T17:03:27.793Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000003","term_name":"molten globule","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04531r014","statement":[{"text":"When the Skn domain is denatured in the absence of specific DNA, its helical content decreases approximately linearly with temperature (as indicated by increasing ellipticity; Fig. 2B), showing that it has little stable tertiary structure.","type":"Results"},{"text":"The Skn domain is a native molten globule that folds to perform a specific function (BR stabilization).","type":"Discussion"}]},{"start":539,"end":623,"reference_id":"9303538","reference_source":"pmid","reference_html":"SKN-1 domain folding and basic region monomer stabilization upon DNA binding. <i> Carroll AS, Gilbert DE, Liu X, Cheung JW, Michnowicz JE, Wagner G, Ellenberger TE, Blackwell TK. </i> Genes Dev, 1997","date":"2026-06-08T19:44:58.131Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001807","ec_ontology":"ECO","ec_name":"electrophoretic mobility shift assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"ec_go":"IPI","region_id":"DP04531r015","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence 5'- TGACAATGTCATCCC."}]}],"statement":[{"text":"EMSA titrations indicate that the Skn domain binds to an oligonucleotide containing its cognate site with a dissociation constant (Kd) of ∼1 (±0.5) × 10−9 m (not shown; see Materials and Methods).","type":"Results"},{"text":"Together, these findings indicate that the amino-terminal arm binds in the AT-rich region in the minor groove, but is not essential for stabilizing the fold of the Skn domain, or for positioning it on DNA.","type":"Results"},{"text":"The Skn domain binds DNA with an affinity comparable to that of full-length SKN-1 (Blackwell et al. 1994), indicating that the remainder of SKN-1 is dispensable for binding, but other SKN-1 residues (or another protein) could potentially stabilize a Skn-domain fold off DNA.","type":"Discussion"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":539,"end":547,"reference_id":"7939715","reference_source":"pmid","reference_html":"Formation of a monomeric DNA binding domain by Skn-1 bZIP and homeodomain elements. <i> Blackwell TK, Bowerman B, Priess JR, Weintraub H. </i> Science, 1994","date":"2026-06-09T13:30:51.154Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Arg539Asn547del","start":null,"end":null,"position":null}],"ec_go":"IMP","region_id":"DP04531r016","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Curator statement","text":"Interacting dsDNA with sequence 5'- TGACAATGTCATCCC"}]}],"sequence_construct":"NELPVSAFQISEMSLSELQQVLKNESLSEYQRQLIRKIRRRGKNKVAARTCRQRRTDRHDKMSHYI","statement":[{"text":"In contrast, DNA binding is dramatically reduced (undetectable) by either deletion of nine amino acids from the NH2-terminus of the Skn domain (Δ1-9; Fig. 4B, lane 4), or by removal of the BR from Skn-1 (ΔS; Fig. 4A) (15).","type":"Results"},{"text":"In Δ1-9 the nine N*H_{2} terminal Skn domain amino acids have been deleted.","type":"Figure"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false}],"__v":0,"disorder_content":0.13643659711075443,"disprot_consensus":{"full":[{"start":539,"end":623,"type":"T"}],"Structural state":[{"start":539,"end":623,"type":"D"}],"Molecular function":[{"start":539,"end":623,"type":"F"}],"Structural transition":[{"start":539,"end":623,"type":"T"}]}},{"acc":"Q14865","sequence":"MEPNSLQWVGSPCGLHGPYIFYKAFQFHLEGKPRILSLGDFFFVRCTPKDPICIAELQLLWEERTSRQLLSSSKLYFLPEDTPQGRNSDHGEDEVIAVSEKVIVKLEDLVKWVHSDFSKWRCGFHAGPVKTEALGRNGQKEALLKYRQSTLNSGLNFKDVLKEKADLGEDEEETNVIVLSYPQYCRYRSMLKRIQDKPSSILTDQFALALGGIAVVSRNPQILYCRDTFDHPTLIENESICDEFAPNLKGRPRKKKPCPQRRDSFSGVKDSNNNSDGKAVAKVKCEARSALTKPKNNHNCKKVSNEEKPKVAIGEECRADEQAFLVALYKYMKERKTPIERIPYLGFKQINLWTMFQAAQKLGGYETITARRQWKHIYDELGGNPGSTSAATCTRRHYERLILPYERFIKGEEDKPLPPIKPRKQENSSQENENKTKVSGTKRIKHEIPKSKKEKENAPKPQDAAEVSSEQEKEQETLISQKSIPEPLPAADMKKKIEGYQEFSAKPLASRVDPEKDNETDQGSNSEKVAEEAGEKGPTPPLPSAPLAPEKDSALVPGASKQPLTSPSALVDSKQESKLCCFTESPESEPQEASFPSFPTTQPPLANQNETEDDKLPAMADYIANCTVKVDQLGSDDIHNALKQTPKVLVVQSFDMFKDKDLTGPMNENHGLNYTPLLYSRGNPGIMSPLAKKKLLSQVSGASLSSSYPYGSPPPLISKKKLIARDDLCSSLSQTHHGQSTDHMAVSRPSVIQHVQSFRSKPSEERKTINDIFKHEKLSRSDPHRCSFSKHHLNPLADSYVLKQEIQEGKDKLLEKRALPHSHMPSFLADFYSSPHLHSLYRHTEHHLHNEQTSKYPSRDMYRESENSSFPSHRHQEKLHVNYLTSLHLQDKKSAAAEAPTDDQPTDLSLPKNPHKPTGKVLGLAHSTTGPQESKGISQFQVLGSQSRDCHPKACRVSPMTMSGPKKYPESLSRSGKPHHVRLENFRKMEGMVHPILHRKMSPQNIGAARPIKRSLEDLDLVIAGKKARAVSPLDPSKEVSGKEKASEQESEGSKAAHGGHSGGGSEGHKLPLSSPIFPGLYSGSLCNSGLNSRLPAGYSHSLQYLKNQTVLSPLMQPLAFHSLVMQRGIFTSPTNSQQLYRHLAAATPVGSSYGDLLHNSIYPLAAINPQAAFPSSQLSSVHPSTKL","creator":"rpancsa","dataset":[],"date":"2026-01-02T20:43:30.687Z","disprot_id":"DP04533","features":{"pfam":[{"id":"PF01388","name":"ARID/BRIGHT DNA binding domain","start":321,"end":406}]},"genes":[{"name":{"value":"ARID5B","_id":"69582df238549a2e1d36cf13","evidences":[]},"synonyms":[{"value":"DESRT","_id":"69582df238549a2e1d36cf14","evidences":[]},{"value":"MRF2","_id":"69582df238549a2e1d36cf15","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"69582df238549a2e1d36cf12"}],"length":1188,"name":"AT-rich interactive domain-containing protein 5B","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":2,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":414,"end":424,"reference_id":"11478881","reference_source":"pmid","reference_html":"Dynamics of the Mrf-2 DNA-binding domain free and in complex with DNA. <i> Zhu L, Hu J, Lin D, Whitson R, Itakura K, Chen Y. </i> Biochemistry, 2001","date":"2026-01-05T15:04:24.016Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04533r001","statement":[{"text":"In addition, these residues have small S2 values. [Mean S2 is 0.30 ((0.03)\nfor residues from 109 to 119. These S2 values were adjusted to match the overall global correlation time by multiplying the ratio of the individual correlation time to the τm of 11.6 ns.] These results indicate that the C-terminus has a high mobility which is largely independent of the rest of the free protein.","type":"Results"},{"text":"From the NMR spectrum on Figure 1 it is clear that the disordered region C-terminal to the ARID domain (residues 109-119 of the studied construct) corresponds to residues 414-424 in the UniProt protein.","type":"Curator statement"}],"cross_refs":[{"db":"PDB","id":"1IG6"},{"db":"BMRB","id":"4100"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-01-05T15:04:42.217Z"}},{"start":415,"end":424,"reference_id":"11478881","reference_source":"pmid","reference_html":"Dynamics of the Mrf-2 DNA-binding domain free and in complex with DNA. <i> Zhu L, Hu J, Lin D, Whitson R, Itakura K, Chen Y. </i> Biochemistry, 2001","date":"2026-01-05T15:05:21.272Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"ec_go":"EXP","region_id":"DP04533r002","statement":[{"text":"This mobility is reduced considerably upon DNA binding. All residues in the C-terminus can fit to the model-free formalism using the same overall correlation time as other residues. However, models with two-time-scale internal motions are necessary for residues 110-119. The S2 values\nof the C-terminal residues in the complex have increased with an average value of 0.64 ((0.04) for the last 10 residues. Albeit the conformational flexibility is reduced dramatically, likely due to direct contacts with the DNA, the C-terminus still has significant internal motions, with τe in\nthe ns range.","type":"Results"},{"text":"From the NMR spectrum on Figure 1 it is clear that the disordered region C-terminal to the ARID domain (residues 109-119 of the studied construct) corresponds to residues 414-424 in the UniProt protein.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","cross_refs":[{"db":"PDB","id":"1IG6"},{"db":"BMRB","id":"4100"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-01-05T15:05:27.736Z"}}],"__v":0,"disorder_content":0.009259259259259259,"disprot_consensus":{"full":[{"start":414,"end":424,"type":"D"}],"Structural state":[{"start":414,"end":424,"type":"D"}],"Molecular function":[{"start":415,"end":424,"type":"F"}]}},{"acc":"Q8L7L8","sequence":"MVSHKCVEEFGYASYLVPSNARAPRSARKRRSIEKRISKEDDNMCAIDLLATVAGHLSFESGSSLMSIDKLIEDHRVKEEFPEEEKPLMPVALSPYRGSLSPCGFSSVINGKVENEVDGFSYSGGSDACQVGNFSQDVKPDIDGDAVVLDARPNVVVSLGSSSRTEVPSIGNCVSHGVRDDVNLFSRDDDENFSKYIHPRVTKHSPRTVPRIGDRRIRKILASRHWKGGSRHSDTKPWRNYYLHQQRSYPIKKRKNFDHISDSVTDDYRMRTKMHRGSRKGQGASFVASDSHVKLRIKSFRVPELFIEIPETATVGSLKRMVMEAVSTLLSDGHRVGLMVQGKKVRDDNKTLHQTGISQDNSHLDSLDFSLEPSSEMPQLLTSHPLGHACEELLPVCQATKIDNVLESDHHDSALFPSDSLGNNNVTEDSKAMISVALNELSSQSQPPSRKSRRSEQQQQQAAQRRIRRPFSVAEVEALVQAVEKLGTGRWRDVKLCAFEDADHRTYVDLKDKWKTLVHTAKISPQQRRGEPVPQELLNRVLNAHGYWTQQQMQQLQQNVNKLEQETQSQTTEGLLLL","creator":"rpancsa","dataset":[],"date":"2026-01-04T15:25:53.889Z","disprot_id":"DP04534","features":{"pfam":[{"id":"PF23603","name":"Telomere repeat-binding protein 1-like, ubiquitin-like domain","start":292,"end":360}]},"genes":[{"name":{"value":"TRP1","_id":"695a868138549a2e1d36cf2b","evidences":[]},"synonyms":[],"olnNames":[{"value":"At5g59430","_id":"695a868138549a2e1d36cf2c","evidences":[]}],"orfNames":[{"value":"F2O15.20","_id":"695a868138549a2e1d36cf2d","evidences":[]}],"_id":"695a868138549a2e1d36cf2a"}],"length":578,"name":"Telomere repeat-binding protein 1","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions_counter":5,"released":"2026_06","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"regions":[{"start":561,"end":578,"reference_id":"16337232","reference_source":"pmid","reference_html":"Solution structure of the Arabidopsis thaliana telomeric repeat-binding protein DNA binding domain: a new fold with an additional C-terminal helix. <i> Sue SC, Hsiao HH, Chung BC, Cheng YH, Hsueh KL, Chen CM, Ho CH, Huang TH. </i> J Mol Biol, 2006","date":"2026-01-05T13:25:32.117Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"2AJE"}],"region_id":"DP04534r003","statement":[{"text":"The spectrum of AtTRP1 464-578 contains all resonances observed in\nAtTRP1 464-560 , and few additional resonances located around the disordered chemical shift region. ","type":"Results"},{"text":"The resonance spectrum of this longer construct was compared to that of 464-560. The resonances of the extra 18 residues could be identified and they were in the disordered range.","type":"Curator statement"}],"last_modified_by":"rpancsa","last_modified_name":"Rita Pancsa","conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Methods","text":"All NMR spectra were obtained at 25 8C on Bruker AVANCE500 and AVANCE600 spectrometers, both\nequipped with cryo-probes. The NMR samples contained 2 mM AtTRP1 464-560 protein in NMR buffer (50 mM phosphate, 150 mM NaCl, pH 7.0)."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":7,"statements":[{"type":"Methods","text":"All NMR spectra were obtained at 25 8C on Bruker AVANCE500 and AVANCE600 spectrometers, both\nequipped with cryo-probes. The NMR samples contained 2 mM AtTRP1 464-560 protein in NMR buffer (50 mM phosphate, 150 mM NaCl, pH 7.0)."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-05T17:40:19.479Z"}},{"start":520,"end":535,"reference_id":"16337232","reference_source":"pmid","reference_html":"Solution structure of the Arabidopsis thaliana telomeric repeat-binding protein DNA binding domain: a new fold with an additional C-terminal helix. <i> Sue SC, Hsiao HH, Chung BC, Cheng YH, Hsueh KL, Chen CM, Ho CH, Huang TH. </i> J Mol Biol, 2006","date":"2026-01-05T13:23:19.184Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"2AJE"},{"db":"BMRB","id":"6727"}],"region_id":"DP04534r004","statement":[{"text":"The three long helices, H1, H3 and H4, were well defined, whilst the shorter H2 helix displayed some structural variations among the 15 structures, due to fewer NOE restraints observed for this helix. The terminal residues Gln464-Ser472 and Gln552-Val560 and the long loop (L1), Thr520-Gln535, exhibit significant disorder. ","type":"Results"}],"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":25,"statements":[{"type":"Figure","text":"15 N-HSQC NMR spectrum of [U- 15 N, 13 C]AtTRP1464-560. The spectrum was taken at 25 C in a Bruker AVANCE600 spectrometer equipped with a Z-gradient triple resonance cryo-probe. The NMR sample contains 2 mM\nprotein in 10 mM phosphate buffer, 150 mM NaCl at pH 7.4."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":7.4,"statements":[{"type":"Figure","text":"15 N-HSQC NMR spectrum of [U- 15 N, 13 C]AtTRP1464-560. The spectrum was taken at 25 C in a Bruker AVANCE600 spectrometer equipped with a Z-gradient triple resonance cryo-probe. The NMR sample contains 2 mM\nprotein in 10 mM phosphate buffer, 150 mM NaCl at pH 7.4."}]}],"last_modified_by":"rpancsa","last_modified_name":"Rita Pancsa","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-05T17:40:18.389Z"}},{"start":522,"end":527,"reference_id":"16337232","reference_source":"pmid","reference_html":"Solution structure of the Arabidopsis thaliana telomeric repeat-binding protein DNA binding domain: a new fold with an additional C-terminal helix. <i> Sue SC, Hsiao HH, Chung BC, Cheng YH, Hsueh KL, Chen CM, Ho CH, Huang TH. </i> J Mol Biol, 2006","date":"2026-06-05T17:37:18.109Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"2AJE"}],"ec_go":"EXP","region_id":"DP04534r005","statement":[{"text":"All resonances in the 15 N-HSQC spectrum of [U- 15 N]AtTRP1 464-560 /DNA complex have been completely assigned. The qualitative features of\nthe protein/DNA interactions can be extracted from the chemical shift perturbations induced by DNA binding (Figure 6(a)).","type":"Results"},{"text":"The majority of the most perturbed residues (DdO 0.2 ppm) are located at the N terminus, H3, and the L1 loop between H3 and H4.","type":"Results"},{"text":"Surface charge distribution analysis of AtTRP1 464-560 showed that four lysine and six arginine residues cluster together to form two prominent positively charged surfaces that are likely to be the DNA binding sites (Figure 6(c)). The contributing charged residues are: Arg465, Arg466, Arg468 and Arg469 at the N terminus; Lys511, Lys513 and Lys515 in H3; and Lys522, Arg528 and Arg529 in loop L1. ","type":"Results"},{"text":"The disordered loop (residues 520-535) takes part in DNA-binding.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-05T17:39:55.402Z"}}],"__v":0,"disorder_content":0.058823529411764705,"disprot_consensus":{"full":[{"start":520,"end":535,"type":"D"},{"start":561,"end":578,"type":"D"}],"Structural state":[{"start":520,"end":535,"type":"D"},{"start":561,"end":578,"type":"D"}],"Molecular function":[{"start":522,"end":527,"type":"F"}]}},{"acc":"P07270","sequence":"MGRTTSEGIHGFVDDLEPKSSILDKVGDFITVNTKRHDGREDFNEQNDELNSQENHNSSENGNENENEQDSLALDDLDRAFELVEGMDMDWMMPSHAHHSPATTATIKPRLLYSPLIHTQSAVPVTISPNLVATATSTTSANKVTKNKSNSSPYLNKRRGKPGPDSATSLFELPDSVIPTPKPKPKPKQYPKVILPSNSTRRVSPVTAKTSSSAEGVVVASESPVIAPHGSSHSRSLSKRRSSGALVDDDKRESHKHAEQARRNRLAVALHELASLIPAEWKQQNVSAAPSKATTVEAACRYIRHLQQNVST","creator":"rpancsa","dataset":[],"date":"2026-01-04T18:53:27.449Z","disprot_id":"DP04535","features":{"pfam":[{"id":"PF00010","name":"Helix-loop-helix DNA-binding domain","start":251,"end":307}]},"genes":[{"name":{"value":"PHO4","_id":"695ab72738549a2e1d36cf43","evidences":[]},"synonyms":[],"olnNames":[{"value":"YFR034C","_id":"695ab72738549a2e1d36cf44","evidences":[]}],"orfNames":[],"_id":"695ab72738549a2e1d36cf42"}],"length":312,"name":"Phosphate system positive regulatory protein PHO4","ncbi_taxon_id":559292,"organism":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","regions_counter":10,"released":"2026_06","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"],"regions":[{"start":248,"end":265,"reference_id":"11206057","reference_source":"pmid","reference_html":"Backbone dynamics of sequence specific recognition and binding by the yeast Pho4 bHLH domain probed by NMR. <i> Cave JW, Kremer W, Wemmer DE. </i> Protein Sci, 2000","date":"2026-06-05T17:42:03.185Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"region_id":"DP04535r001","statement":[{"text":"The basic region residues display significant changes between the unbound protein and DNA complexes. In the absence of DNA, the spectral density values of the basic region form a gradient that runs from the N-terminus to the start of helix 1. The residues at the N-terminus are dominated by high frequency motions (large J(0.87ωH) and small Jeff(0) values) and reflect a random coil backbone conformation. The intensity of these high frequency motions progressively diminishes until the junction with helix 1 where the spectral density values reflect those of the well ordered helices of the HLH fold.","type":"Results"},{"text":"The studied construct was residues 248-312 of the UniProt protein and the basic region corresponds to residues 248-265 based on Figure 1A.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-05T17:42:06.742Z"}},{"start":252,"end":265,"reference_id":"11206057","reference_source":"pmid","reference_html":"Backbone dynamics of sequence specific recognition and binding by the yeast Pho4 bHLH domain probed by NMR. <i> Cave JW, Kremer W, Wemmer DE. </i> Protein Sci, 2000","date":"2026-06-08T15:04:13.054Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":5,"region_id":"DP04535r002","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"The sequences used were 5'-CGCGCGGGATCCCGCGCG-3' for the nonspecific complex and 5'-CGCGCGCACGTGCGCGCG-3' for the cognate sequence."}]}],"statement":[{"text":"Upon complexation with DNA, the spectral density values of the\nbasic region residues become similar to those of the well-ordered\nHLH helices. This change in the spectral density for these residues\nis expected based on the CD, (Ca)1 H CSI, and NOE data that\ndetail a coil to helix transition associated with DNA binding.","type":"Results"},{"text":"The studied construct was residues 248-312 of the UniProt protein and the basic region corresponds to residues 248-265 based on Figure 1A.","type":"Curator statement"},{"text":"Only the residues D3 and K4 appear to remain unstructured in the basic region of the DNA complexes.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-08T15:05:39.635Z"}},{"start":250,"end":265,"reference_id":"11206057","reference_source":"pmid","reference_html":"Backbone dynamics of sequence specific recognition and binding by the yeast Pho4 bHLH domain probed by NMR. <i> Cave JW, Kremer W, Wemmer DE. </i> Protein Sci, 2000","date":"2026-06-08T15:05:34.246Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":5,"ec_go":"EXP","region_id":"DP04535r003","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"The sequences used were 5'-CGCGCGGGATCCCGCGCG-3' for the nonspecific complex and 5'-CGCGCGCACGTGCGCGCG-3' for the cognate sequence."}]}],"statement":[{"text":"Upon complexation with DNA, the spectral density values of the\nbasic region residues become similar to those of the well-ordered\nHLH helices. This change in the spectral density for these residues\nis expected based on the CD, (Ca)1 H CSI, and NOE data that\ndetail a coil to helix transition associated with DNA binding.","type":"Results"},{"text":"The studied construct was residues 248-312 of the UniProt protein and the basic region corresponds to residues 248-265 based on Figure 1A.","type":"Curator statement"},{"text":"Only the residues D3 and K4 appear to remain unstructured in\nthe basic region of the DNA complexes.","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-08T15:05:36.080Z"}},{"start":250,"end":265,"reference_id":"11206057","reference_source":"pmid","reference_html":"Backbone dynamics of sequence specific recognition and binding by the yeast Pho4 bHLH domain probed by NMR. <i> Cave JW, Kremer W, Wemmer DE. </i> Protein Sci, 2000","date":"2026-06-05T18:02:47.946Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"region_id":"DP04535r004","statement":[{"text":"Upon complexation with DNA, the spectral density values of the\nbasic region residues become similar to those of the well-ordered\nHLH helices. This change in the spectral density for these residues\nis expected based on the CD, (Ca)1 H CSI, and NOE data that\ndetail a coil to helix transition associated with DNA binding.","type":"Results"},{"text":"Relative to the unbound form, we show that formation of either the nonspecific and cognate DNA bound complexes involves a large change in conformation and backbone dynamics of the basic region. ","type":"Abstract"},{"text":"The studied construct was residues 248-312 of the UniProt protein and the basic region corresponds to residues 248-265 based on Figure 1A.","type":"Curator statement"}],"states_connection":[{"source":"DP04535r001","target":"DP04535r002"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"The sequences used were 5'-CGCGCGGGATCCCGCGCG-3' for the nonspecific complex and 5'-CGCGCGCACGTGCGCGCG-3' for the cognate sequence."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-05T18:02:51.890Z"}},{"start":248,"end":265,"reference_id":"11206057","reference_source":"pmid","reference_html":"Backbone dynamics of sequence specific recognition and binding by the yeast Pho4 bHLH domain probed by NMR. <i> Cave JW, Kremer W, Wemmer DE. </i> Protein Sci, 2000","date":"2026-01-04T19:12:57.262Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04535r005","statement":[{"text":"CD measurements (Fig. 5) demonstrated that the presence of either nonspecific or cognate DNA results in an approximate 25% increase in the observed helical content. This observed increase in helical content is approximately equivalent to the percentage of the basic region relative to the entire Pho4 construct.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-05T20:46:43.490Z"}},{"start":248,"end":265,"reference_id":"11206057","reference_source":"pmid","reference_html":"Backbone dynamics of sequence specific recognition and binding by the yeast Pho4 bHLH domain probed by NMR. <i> Cave JW, Kremer W, Wemmer DE. </i> Protein Sci, 2000","date":"2026-01-04T19:13:48.857Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04535r006","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Results","text":"CD measurements (Fig. 5) demonstrated that the presence of either nonspecific or cognate DNA results in an approximate 25% increase in the observed helical content. This observed increase in helical content is approximately equivalent to the percentage of the basic region relative to the entire Pho4 construct."}]}],"statement":[{"text":"CD measurements (Fig. 5) demonstrated that the presence of either nonspecific or cognate DNA results in an approximate 25% increase in the observed helical content. This observed increase in helical content is approximately equivalent to the percentage of the basic region relative to the entire Pho4 construct.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-05T18:08:09.923Z"}},{"start":248,"end":265,"reference_id":"11206057","reference_source":"pmid","reference_html":"Backbone dynamics of sequence specific recognition and binding by the yeast Pho4 bHLH domain probed by NMR. <i> Cave JW, Kremer W, Wemmer DE. </i> Protein Sci, 2000","date":"2026-01-04T19:14:47.131Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"EXP","region_id":"DP04535r007","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Results","text":"CD measurements (Fig. 5) demonstrated that the presence of either nonspecific or cognate DNA results in an approximate 25% increase in the observed helical content. This observed increase in helical content is approximately equivalent to the percentage of the basic region relative to the entire Pho4 construct."}]}],"statement":[{"text":"CD measurements (Fig. 5) demonstrated that the presence of either nonspecific or cognate DNA results in an approximate 25% increase in the observed helical content. This observed increase in helical content is approximately equivalent to the percentage of the basic region relative to the entire Pho4 construct.","type":"Results"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-08T14:53:36.930Z"}},{"start":248,"end":265,"reference_id":"11206057","reference_source":"pmid","reference_html":"Backbone dynamics of sequence specific recognition and binding by the yeast Pho4 bHLH domain probed by NMR. <i> Cave JW, Kremer W, Wemmer DE. </i> Protein Sci, 2000","date":"2026-06-05T18:03:14.250Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04535r008","statement":[{"text":"CD measurements (Fig. 5) demonstrated that the presence of either nonspecific or cognate DNA results in an approximate 25% increase in the observed helical content. This observed increase in helical content is approximately equivalent to the percentage of the basic region relative to the entire Pho4 construct.","type":"Results"}],"states_connection":[{"source":"DP04535r005","target":"DP04535r006"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"The sequences used were 5'-CGCGCGGGATCCCGCGCG-3' for the nonspecific complex and 5'-CGCGCGCACGTGCGCGCG-3' for the cognate sequence."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-05T18:03:19.698Z"}},{"start":251,"end":265,"reference_id":"9303313","reference_source":"pmid","reference_html":"Crystal structure of PHO4 bHLH domain-DNA complex: flanking base recognition. <i> Shimizu T, Toumoto A, Ihara K, Shimizu M, Kyogoku Y, Ogawa N, Oshima Y, Hakoshima T. </i> EMBO J, 1997","date":"2026-06-08T14:58:56.787Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"cross_refs":[{"db":"PDB","id":"1A0A"}],"ec_go":"EXP","region_id":"DP04535r009","statement":[{"text":"PHO4 binds to DNA as a homodimer with direct reading of both the core E-box sequence CACGTG and its 3'-flanking bases. The 3'-flanking bases GG are recognized by Arg2 and His5. The residues involved in the E-box recognition are His5, Glu9 and Arg13, as already reported for bHLH/Zip proteins MAX and USF, and are different from those recognized by bHLH proteins MyoD and E47, although PHO4 is a bHLH protein.","type":"Abstract"},{"text":"A number of residues involving Lys1, Lys6, Gln10, Arg12 and Arg15 in the basic region make contacts with phosphate groups.","type":"Results"},{"text":"Figure 4 shows that almost all residues of the basic region, corresponding to UniProt residues 250-263 are in contact with DNA in the DNA-bound form of the protein.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Results","text":"The crystal structure of a DNA-binding domain of PHO4 complexed with DNA at 2.8 Å resolution revealed that the domain folds into a basic–helix–loop–helix (bHLH) motif with a long but compact loop that contains a short α-helical segment."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-08T14:59:04.200Z"}},{"start":251,"end":265,"reference_id":"9303313","reference_source":"pmid","reference_html":"Crystal structure of PHO4 bHLH domain-DNA complex: flanking base recognition. <i> Shimizu T, Toumoto A, Ihara K, Shimizu M, Kyogoku Y, Ogawa N, Oshima Y, Hakoshima T. </i> EMBO J, 1997","date":"2026-06-08T15:04:56.943Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"1A0A"}],"region_id":"DP04535r010","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Abstract","text":"The crystal structure of a DNA-binding domain of PHO4 complexed with DNA at 2.8 A resolution revealed that the domain folds into a basic-helix-loop-helix (bHLH) motif with a long but compact loop that contains a short alpha-helical segment."}]}],"statement":[{"text":"PHO4 binds to DNA as a homodimer with direct reading of both the core E-box sequence CACGTG and its 3'-flanking bases. The 3'-flanking bases GG are recognized by Arg2 and His5. The residues involved in the E-box recognition are His5, Glu9 and Arg13, as already reported for bHLH/Zip proteins MAX and USF, and are different from those recognized by bHLH proteins MyoD and E47, although PHO4 is a bHLH protein.","type":"Abstract"},{"text":"A number of residues involving Lys1, Lys6, Gln10, Arg12 and Arg15 in the basic region make contacts with phosphate groups.","type":"Results"},{"text":"Figure 4 shows that almost all residues of the basic region, corresponding to UniProt residues 250-265 are in contact with DNA in the DNA-bound form of the protein, so they are visible in the X-ray structure. They obtain an ordered form in the presence of DNA.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-08T15:05:41.454Z"}}],"__v":0,"disorder_content":0.057692307692307696,"disprot_consensus":{"full":[{"start":248,"end":265,"type":"T"}],"Structural state":[{"start":248,"end":265,"type":"D"}],"Molecular function":[{"start":248,"end":265,"type":"F"}],"Structural transition":[{"start":248,"end":265,"type":"T"}]}},{"acc":"O13988","sequence":"MGEDVIDSLQLNELLNAGEYKIGELTFQSIRSSQELQKKNTIVNLFGIVKDFTPSRQSLHGTKDWVTTVYLWDPTCDTSSIGLQIHLFSKQGNDLPVIKQVGQPLLLHQITLRSYRDRTQGLSKDQFRYALWPDFSSNSKDTLCPQPMPRLMKTGDKEEQFALLLNKIWDEQTNKHKNGELLSTSSARQNQTGLSYPSVSFSLLSQITPHQRCSFYAQVIKTWYSDKNFTLYVTDYTENELFFPMSPYTSSSRWRGPFGRFSIRCILWDEHDFYCRNYIKEGDYVVMKNVRTKIDHLGYLECILHGDSAKRYNMSIEKVDSEEPELNEIKSRKRLYVQNCQNGIEAVIEKLSQSQQSENPFIAHELKQTSVNEITAHVINEPASLKLTTISTILHAPLQNLLKPRKHRLRVQVVDFWPKSLTQFAVLSQPPSSYVWMFALLVRDVSNVTLPVIFFDSDAAELINSSKIQPCNLADHPQMTLQLKERLFLIWGNLEERIQHHISKGESPTLAAEDVETPWFDIYVKEYIPVIGNTKDHQSLTFLQKRWRGFGTKIV","creator":"rpancsa","dataset":[],"date":"2026-01-05T09:56:48.659Z","disprot_id":"DP04536","features":{"pfam":[{"id":"PF02765","name":"Telomeric single stranded DNA binding POT1/CDC13","start":24,"end":178},{"id":"PF16686","name":"ssDNA-binding domain of telomere protection protein","start":203,"end":338}]},"genes":[{"name":{"value":"pot1","_id":"695b8ae038549a2e1d36cf74","evidences":[]},"synonyms":[],"olnNames":[],"orfNames":[{"value":"SPAC26H5.06","_id":"695b8ae038549a2e1d36cf75","evidences":[]}],"_id":"695b8ae038549a2e1d36cf73"}],"length":555,"name":"Protection of telomeres protein 1","ncbi_taxon_id":284812,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","regions_counter":11,"released":"2026_06","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"regions":[{"start":1,"end":18,"reference_id":"19232358","reference_source":"pmid","reference_html":"Insights into the dynamics of specific telomeric single-stranded DNA recognition by Pot1pN. <i> Croy JE, Wuttke DS. </i> J Mol Biol, 2009","date":"2026-01-05T12:58:08.155Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The 22-kDa (His)6-Pot1pN DBD from the S. pombe Pot1 protein was expressed in Escherichia coli, purified, and stored according to the protocols established by Lei et al.10 with final purified yields of 25 mg/L. Uniform 13C–15N or 15N labeling was performed by expressing each protein in modified minimal M9 media."}]}],"region_id":"DP04536r001","sequence_construct":"MRGSHHHHHHGSMGEDVIDSLQLNELLNAGEYKIGELTFQSIRSSQELQKKNTIVNLFGIVKDFTPSRQSLHGTKDWVTTVYLWDPTCDTSSIGLQIHLFSKQGNDLPVIKQVGQPLLLHQITLRSYRDRTQGLSKDQFRYALWPDFSSNSKDTLCPQPMPRLMKTGDKEEQFALLLNKIWDEQTNKHKNGELLSTS","statement":[{"text":"As expected, the terminal amides (1–30 and 188–197) and the majority of those present in the loops connecting individual β-strands in Pot1pNF and Pot1pNB experience dynamic motions on the fast timescale that are unaffected by the binding of d(GGTTAC) and are consistent with unstructured protein elements (Fig. 4 and Supplemental Fig. 4).","type":"Results"},{"text":"The studied construct contains an N-terminal tag of 12 residues and the first 185 of the protein (this is evident from Supplementary Table 1.), together 197 residues. The 30 N-terminal disordered residues therefore correspond to the 12 residues of the tag and first 18 residues of the protein.","type":"Curator statement"}],"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":30,"statements":[{"type":"Figure","text":"15N HSQC spectrum of the Pot1pNF collected on a Varian 500-MHz spectrophotometer equipped with a room temperature probe at 30 °C."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.15,"statements":[{"type":"Methods","text":"Complexes of 15N-labeled Pot1pN and d(GGTTAC) at 1.25 mM in NMR sample buffer (50 mM KH2PO4, pH 6.15, 50 mM NaCl, 1 mM d-DTT, and 10% D2O) contained an excess of 0.25 molar equivalents of d(GGTTAC) to ensure that Pot1pN was present in a homogeneous ssDNA-bound complex."}]}],"last_modified_by":"rpancsa","last_modified_name":"Rita Pancsa","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-02-02T14:35:20.686Z"}},{"start":176,"end":185,"reference_id":"19232358","reference_source":"pmid","reference_html":"Insights into the dynamics of specific telomeric single-stranded DNA recognition by Pot1pN. <i> Croy JE, Wuttke DS. </i> J Mol Biol, 2009","date":"2026-01-05T12:58:40.334Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The 22-kDa (His)6-Pot1pN DBD from the S. pombe Pot1 protein was expressed in Escherichia coli, purified, and stored according to the protocols established by Lei et al.10 with final purified yields of 25 mg/L. Uniform 13C–15N or 15N labeling was performed by expressing each protein in modified minimal M9 media."}]}],"region_id":"DP04536r002","sequence_construct":"MRGSHHHHHHGSMGEDVIDSLQLNELLNAGEYKIGELTFQSIRSSQELQKKNTIVNLFGIVKDFTPSRQSLHGTKDWVTTVYLWDPTCDTSSIGLQIHLFSKQGNDLPVIKQVGQPLLLHQITLRSYRDRTQGLSKDQFRYALWPDFSSNSKDTLCPQPMPRLMKTGDKEEQFALLLNKIWDEQTNKHKNGELLSTS","statement":[{"text":"As expected, the terminal amides (1–30 and 188–197) and the majority of those present in the loops connecting individual β-strands in Pot1pNF and Pot1pNB experience dynamic motions on the fast timescale that are unaffected by the binding of d(GGTTAC) and are consistent with unstructured protein elements (Fig. 4 and Supplemental Fig. 4).","type":"Results"},{"text":"The studied construct contains an N-terminal tag of 12 residues and the first 185 of the protein (this is evident from Supplementary Table 1.), together 197 residues. The C-terminal disordered residues therefore correspond to residues 176-185 of the protein.","type":"Curator statement"}],"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":30,"statements":[{"type":"Figure","text":"15N HSQC spectrum of the Pot1pNF collected on a Varian 500-MHz spectrophotometer equipped with a room temperature probe at 30 °C."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.15,"statements":[{"type":"Methods","text":"Complexes of 15N-labeled Pot1pN and d(GGTTAC) at 1.25 mM in NMR sample buffer (50 mM KH2PO4, pH 6.15, 50 mM NaCl, 1 mM d-DTT, and 10% D2O) contained an excess of 0.25 molar equivalents of d(GGTTAC) to ensure that Pot1pN was present in a homogeneous ssDNA-bound complex."}]}],"last_modified_by":"rpancsa","last_modified_name":"Rita Pancsa","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-02-02T14:35:47.134Z"}},{"start":54,"end":64,"reference_id":"19232358","reference_source":"pmid","reference_html":"Insights into the dynamics of specific telomeric single-stranded DNA recognition by Pot1pN. <i> Croy JE, Wuttke DS. </i> J Mol Biol, 2009","date":"2026-01-05T12:59:09.346Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":4,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The 22-kDa (His)6-Pot1pN DBD from the S. pombe Pot1 protein was expressed in Escherichia coli, purified, and stored according to the protocols established by Lei et al.10 with final purified yields of 25 mg/L. Uniform 13C–15N or 15N labeling was performed by expressing each protein in modified minimal M9 media."}]}],"region_id":"DP04536r003","sequence_construct":"MRGSHHHHHHGSMGEDVIDSLQLNELLNAGEYKIGELTFQSIRSSQELQKKNTIVNLFGIVKDFTPSRQSLHGTKDWVTTVYLWDPTCDTSSIGLQIHLFSKQGNDLPVIKQVGQPLLLHQITLRSYRDRTQGLSKDQFRYALWPDFSSNSKDTLCPQPMPRLMKTGDKEEQFALLLNKIWDEQTNKHKNGELLSTS","statement":[{"text":"As expected, the terminal amides (1–30 and 188–197) and the majority of those present in the loops connecting individual β-strands in Pot1pNF and Pot1pNB experience dynamic motions on the fast timescale that are unaffected by the binding of d(GGTTAC) and are consistent with unstructured protein elements (Fig. 4 and Supplemental Fig. 4).","type":"Results"},{"text":"The studied construct contains an N-terminal tag of 12 residues and the first 185 of the protein (this is evident from Supplementary Table 1.), together 197 residues. Residues 54 to 64 correspond to the Loop12 that is one of the longest disordered loops that also takes part in DNA-binding. Residues boundaries of the loops were derived from Supplementary Table X, column \"Pot1pNF Derived Residue Limits\", taking into account that the studied sequence started with a 12-residue tag. ","type":"Curator statement"}],"last_modified_by":"rpancsa","last_modified_name":"Rita Pancsa","conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":30,"statements":[{"type":"Figure","text":"15N HSQC spectrum of the Pot1pNF collected on a Varian 500-MHz spectrophotometer equipped with a room temperature probe at 30 °C."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.15,"statements":[{"type":"Methods","text":"Complexes of 15N-labeled Pot1pN and d(GGTTAC) at 1.25 mM in NMR sample buffer (50 mM KH2PO4, pH 6.15, 50 mM NaCl, 1 mM d-DTT, and 10% D2O) contained an excess of 0.25 molar equivalents of d(GGTTAC) to ensure that Pot1pN was present in a homogeneous ssDNA-bound complex."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-06T13:10:05.963Z"}},{"start":71,"end":82,"reference_id":"19232358","reference_source":"pmid","reference_html":"Insights into the dynamics of specific telomeric single-stranded DNA recognition by Pot1pN. <i> Croy JE, Wuttke DS. </i> J Mol Biol, 2009","date":"2026-01-05T12:59:37.974Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The 22-kDa (His)6-Pot1pN DBD from the S. pombe Pot1 protein was expressed in Escherichia coli, purified, and stored according to the protocols established by Lei et al.10 with final purified yields of 25 mg/L. Uniform 13C–15N or 15N labeling was performed by expressing each protein in modified minimal M9 media."}]}],"region_id":"DP04536r004","sequence_construct":"MRGSHHHHHHGSMGEDVIDSLQLNELLNAGEYKIGELTFQSIRSSQELQKKNTIVNLFGIVKDFTPSRQSLHGTKDWVTTVYLWDPTCDTSSIGLQIHLFSKQGNDLPVIKQVGQPLLLHQITLRSYRDRTQGLSKDQFRYALWPDFSSNSKDTLCPQPMPRLMKTGDKEEQFALLLNKIWDEQTNKHKNGELLSTS","statement":[{"text":"As expected, the terminal amides (1–30 and 188–197) and the majority of those present in the loops connecting individual β-strands in Pot1pNF and Pot1pNB experience dynamic motions on the fast timescale that are unaffected by the binding of d(GGTTAC) and are consistent with unstructured protein elements (Fig. 4 and Supplemental Fig. 4).","type":"Results"},{"text":"The studied construct contains an N-terminal tag of 12 residues and the first 185 of the protein (this is evident from Supplementary Table 1.), together 197 residues. Residues 71 to 82 correspond to the Loop23 that is one of the longest disordered loops connecting individual β-strands. Residues boundaries of the loops were derived from Supplementary Table X, column \"Pot1pNF Derived Residue Limits\", taking into account that the studied sequence started with a 12-residue tag. ","type":"Curator statement"}],"last_modified_by":"rpancsa","last_modified_name":"Rita Pancsa","conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":30,"statements":[{"type":"Figure","text":"15N HSQC spectrum of the Pot1pNF collected on a Varian 500-MHz spectrophotometer equipped with a room temperature probe at 30 °C."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.15,"statements":[{"type":"Methods","text":"Complexes of 15N-labeled Pot1pN and d(GGTTAC) at 1.25 mM in NMR sample buffer (50 mM KH2PO4, pH 6.15, 50 mM NaCl, 1 mM d-DTT, and 10% D2O) contained an excess of 0.25 molar equivalents of d(GGTTAC) to ensure that Pot1pN was present in a homogeneous ssDNA-bound complex."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-06T13:06:21.747Z"}},{"start":91,"end":103,"reference_id":"19232358","reference_source":"pmid","reference_html":"Insights into the dynamics of specific telomeric single-stranded DNA recognition by Pot1pN. <i> Croy JE, Wuttke DS. </i> J Mol Biol, 2009","date":"2026-01-05T13:00:20.324Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The 22-kDa (His)6-Pot1pN DBD from the S. pombe Pot1 protein was expressed in Escherichia coli, purified, and stored according to the protocols established by Lei et al.10 with final purified yields of 25 mg/L. Uniform 13C–15N or 15N labeling was performed by expressing each protein in modified minimal M9 media."}]}],"region_id":"DP04536r005","sequence_construct":"MRGSHHHHHHGSMGEDVIDSLQLNELLNAGEYKIGELTFQSIRSSQELQKKNTIVNLFGIVKDFTPSRQSLHGTKDWVTTVYLWDPTCDTSSIGLQIHLFSKQGNDLPVIKQVGQPLLLHQITLRSYRDRTQGLSKDQFRYALWPDFSSNSKDTLCPQPMPRLMKTGDKEEQFALLLNKIWDEQTNKHKNGELLSTS","statement":[{"text":"As expected, the terminal amides (1–30 and 188–197) and the majority of those present in the loops connecting individual β-strands in Pot1pNF and Pot1pNB experience dynamic motions on the fast timescale that are unaffected by the binding of d(GGTTAC) and are consistent with unstructured protein elements (Fig. 4 and Supplemental Fig. 4).","type":"Results"},{"text":"The studied construct contains an N-terminal tag of 12 residues and the first 185 of the protein (this is evident from Supplementary Table 1.), together 197 residues. Residues 91 to 103 correspond to the Loop34 that is one of the longest disordered loops connecting individual β-strands. Residues boundaries of the loops were derived from Supplementary Table X, column \"Pot1pNF Derived Residue Limits\", taking into account that the studied sequence started with a 12-residue tag. ","type":"Curator statement"}],"last_modified_by":"rpancsa","last_modified_name":"Rita Pancsa","conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":30,"statements":[{"type":"Figure","text":"15N HSQC spectrum of the Pot1pNF collected on a Varian 500-MHz spectrophotometer equipped with a room temperature probe at 30 °C."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.15,"statements":[{"type":"Methods","text":"Complexes of 15N-labeled Pot1pN and d(GGTTAC) at 1.25 mM in NMR sample buffer (50 mM KH2PO4, pH 6.15, 50 mM NaCl, 1 mM d-DTT, and 10% D2O) contained an excess of 0.25 molar equivalents of d(GGTTAC) to ensure that Pot1pN was present in a homogeneous ssDNA-bound complex."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-06T13:06:14.878Z"}},{"start":54,"end":64,"reference_id":"19232358","reference_source":"pmid","reference_html":"Insights into the dynamics of specific telomeric single-stranded DNA recognition by Pot1pN. <i> Croy JE, Wuttke DS. </i> J Mol Biol, 2009","date":"2026-01-05T13:01:31.859Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The 22-kDa (His)6-Pot1pN DBD from the S. pombe Pot1 protein was expressed in Escherichia coli, purified, and stored according to the protocols established by Lei et al.10 with final purified yields of 25 mg/L. Uniform 13C–15N or 15N labeling was performed by expressing each protein in modified minimal M9 media."}]}],"region_id":"DP04536r006","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"Complexes of 15N-labeled Pot1pN and d(GGTTAC) at 1.25 mM in NMR sample buffer (50 mM KH2PO4, pH 6.15, 50 mM NaCl, 1 mM d-DTT, and 10% D2O) contained an excess of 0.25 molar equivalents of d(GGTTAC) to ensure that Pot1pN was present in a homogeneous ssDNA-bound complex."}]}],"sequence_construct":"MRGSHHHHHHGSMGEDVIDSLQLNELLNAGEYKIGELTFQSIRSSQELQKKNTIVNLFGIVKDFTPSRQSLHGTKDWVTTVYLWDPTCDTSSIGLQIHLFSKQGNDLPVIKQVGQPLLLHQITLRSYRDRTQGLSKDQFRYALWPDFSSNSKDTLCPQPMPRLMKTGDKEEQFALLLNKIWDEQTNKHKNGELLSTS","statement":[{"text":"For Loop12, significant increases in the HetNOE ratios (Fig. 4) (average change of Loop12 amides from 0.54 in Pot1pNF to 0.73 in Pot1pNB) indicate a decrease in the dynamic behavior of these amides in response to ssDNA binding, moving from a partially disordered state to a highly ordered structure (Fig. 4 and Supplemental Fig. 4). ","type":"Results"},{"text":"The studied construct contains an N-terminal tag of 12 residues and the first 185 of the protein (this is evident from Supplementary Table 1.), together 197 residues. Residues 54 to 64 correspond to the Loop12 that is one of the longest disordered loops connecting individual β-strands. Residues boundaries of the loops were derived from Supplementary Table X, column \"Pot1pNF Derived Residue Limits\", taking into account that the studied sequence started with a 12-residue tag. ","type":"Curator statement"}],"last_modified_by":"rpancsa","last_modified_name":"Rita Pancsa","conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":30,"statements":[{"type":"Figure","text":"Parameters determined from 15N relaxation experiments. HetNOE (upper panel), R1 (middle panel), and R2 (lower panel) are plotted as a function of residue number for Pot1pNF (black) and Pot1pNB (magenta) collected at 500 MHz at 30 °C."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.15,"statements":[{"type":"Methods","text":"Complexes of 15N-labeled Pot1pN and d(GGTTAC) at 1.25 mM in NMR sample buffer (50 mM KH2PO4, pH 6.15, 50 mM NaCl, 1 mM d-DTT, and 10% D2O) contained an excess of 0.25 molar equivalents of d(GGTTAC) to ensure that Pot1pN was present in a homogeneous ssDNA-bound complex."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-06T13:04:58.633Z"}},{"start":54,"end":64,"reference_id":"19232358","reference_source":"pmid","reference_html":"Insights into the dynamics of specific telomeric single-stranded DNA recognition by Pot1pN. <i> Croy JE, Wuttke DS. </i> J Mol Biol, 2009","date":"2026-01-05T13:06:15.272Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The 22-kDa (His)6-Pot1pN DBD from the S. pombe Pot1 protein was expressed in Escherichia coli, purified, and stored according to the protocols established by Lei et al.10 with final purified yields of 25 mg/L. Uniform 13C–15N or 15N labeling was performed by expressing each protein in modified minimal M9 media."}]}],"ec_go":"EXP","region_id":"DP04536r007","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"Complexes of 15N-labeled Pot1pN and d(GGTTAC) at 1.25 mM in NMR sample buffer (50 mM KH2PO4, pH 6.15, 50 mM NaCl, 1 mM d-DTT, and 10% D2O) contained an excess of 0.25 molar equivalents of d(GGTTAC) to ensure that Pot1pN was present in a homogeneous ssDNA-bound complex."}]}],"sequence_construct":"MRGSHHHHHHGSMGEDVIDSLQLNELLNAGEYKIGELTFQSIRSSQELQKKNTIVNLFGIVKDFTPSRQSLHGTKDWVTTVYLWDPTCDTSSIGLQIHLFSKQGNDLPVIKQVGQPLLLHQITLRSYRDRTQGLSKDQFRYALWPDFSSNSKDTLCPQPMPRLMKTGDKEEQFALLLNKIWDEQTNKHKNGELLSTS","statement":[{"text":"For Loop12, significant increases in the HetNOE ratios (Fig. 4) (average change of Loop12 amides from 0.54 in Pot1pNF to 0.73 in Pot1pNB) indicate a decrease in the dynamic behavior of these amides in response to ssDNA binding, moving from a partially disordered state to a highly ordered structure (Fig. 4 and Supplemental Fig. 4). ","type":"Results"},{"text":"The studied construct contains an N-terminal tag of 12 residues and the first 185 of the protein (this is evident from Supplementary Table 1.), together 197 residues. Residues 54 to 64 correspond to the Loop12 that is one of the longest disordered loops connecting individual β-strands. Residues boundaries of the loops were derived from Supplementary Table X, column \"Pot1pNF Derived Residue Limits\", taking into account that the studied sequence started with a 12-residue tag. ","type":"Curator statement"},{"text":"Unlike the G1/G2-binding pocket, which is well ordered in the presence and in the absence of ssDNA, picosecond–nanosecond motions show that backbone amides present in Loop12, which forms the centerpiece of the T3/T4-binding pocket, are significantly disordered in the absence of ssDNA and ordered upon binding (Fig. 4). This loop is well structured in Pot1pNB, suggesting that formation of the T3/T4-binding pocket proceeds via a “mutually” induced-fit type of mechanism that requires the coordinated co-folding of both Loop12 and Loop34 with the unstructured oligonucleotide40,45 (Fig. 4).","type":"Discussion"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"rpancsa","last_modified_name":"Rita Pancsa","conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":30,"statements":[{"type":"Figure","text":"Parameters determined from 15N relaxation experiments. HetNOE (upper panel), R1 (middle panel), and R2 (lower panel) are plotted as a function of residue number for Pot1pNF (black) and Pot1pNB (magenta) collected at 500 MHz at 30 °C. "}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.15,"statements":[{"type":"Methods","text":"Complexes of 15N-labeled Pot1pN and d(GGTTAC) at 1.25 mM in NMR sample buffer (50 mM KH2PO4, pH 6.15, 50 mM NaCl, 1 mM d-DTT, and 10% D2O) contained an excess of 0.25 molar equivalents of d(GGTTAC) to ensure that Pot1pN was present in a homogeneous ssDNA-bound complex."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-06T13:10:11.893Z"}},{"start":54,"end":64,"reference_id":"19232358","reference_source":"pmid","reference_html":"Insights into the dynamics of specific telomeric single-stranded DNA recognition by Pot1pN. <i> Croy JE, Wuttke DS. </i> J Mol Biol, 2009","date":"2026-01-05T13:04:36.223Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The 22-kDa (His)6-Pot1pN DBD from the S. pombe Pot1 protein was expressed in Escherichia coli, purified, and stored according to the protocols established by Lei et al.10 with final purified yields of 25 mg/L. Uniform 13C–15N or 15N labeling was performed by expressing each protein in modified minimal M9 media."}]}],"region_id":"DP04536r008","sequence_construct":"MRGSHHHHHHGSMGEDVIDSLQLNELLNAGEYKIGELTFQSIRSSQELQKKNTIVNLFGIVKDFTPSRQSLHGTKDWVTTVYLWDPTCDTSSIGLQIHLFSKQGNDLPVIKQVGQPLLLHQITLRSYRDRTQGLSKDQFRYALWPDFSSNSKDTLCPQPMPRLMKTGDKEEQFALLLNKIWDEQTNKHKNGELLSTS","statement":[{"text":"For Loop12, significant increases in the HetNOE ratios (Fig. 4) (average change of Loop12 amides from 0.54 in Pot1pNF to 0.73 in Pot1pNB) indicate a decrease in the dynamic behavior of these amides in response to ssDNA binding, moving from a partially disordered state to a highly ordered structure (Fig. 4 and Supplemental Fig. 4). ","type":"Results"},{"text":"Unlike the G1/G2-binding pocket, which is well ordered in the presence and in the absence of ssDNA, picosecond–nanosecond motions show that backbone amides present in Loop12, which forms the centerpiece of the T3/T4-binding pocket, are significantly disordered in the absence of ssDNA and ordered upon binding (Fig. 4). This loop is well structured in Pot1pNB, suggesting that formation of the T3/T4-binding pocket proceeds via a “mutually” induced-fit type of mechanism that requires the coordinated co-folding of both Loop12 and Loop34 with the unstructured oligonucleotide40,45 (Fig. 4).","type":"Discussion"},{"text":"The studied construct contains an N-terminal tag of 12 residues and the first 185 of the protein (this is evident from Supplementary Table 1.), together 197 residues. Residues 54 to 64 correspond to the Loop12 that is one of the longest disordered loops connecting individual β-strands. Residues boundaries of the loops were derived from Supplementary Table X, column \"Pot1pNF Derived Residue Limits\", taking into account that the studied sequence started with a 12-residue tag.","type":"Curator statement"}],"states_connection":[{"source":"DP04536r003","target":"DP04536r006"}],"last_modified_by":"rpancsa","last_modified_name":"Rita Pancsa","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-06T13:10:09.353Z"}},{"start":91,"end":103,"reference_id":"19232358","reference_source":"pmid","reference_html":"Insights into the dynamics of specific telomeric single-stranded DNA recognition by Pot1pN. <i> Croy JE, Wuttke DS. </i> J Mol Biol, 2009","date":"2026-01-05T13:03:07.577Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The 22-kDa (His)6-Pot1pN DBD from the S. pombe Pot1 protein was expressed in Escherichia coli, purified, and stored according to the protocols established by Lei et al.10 with final purified yields of 25 mg/L. Uniform 13C–15N or 15N labeling was performed by expressing each protein in modified minimal M9 media."}]}],"region_id":"DP04536r009","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"Complexes of 15N-labeled Pot1pN and d(GGTTAC) at 1.25 mM in NMR sample buffer (50 mM KH2PO4, pH 6.15, 50 mM NaCl, 1 mM d-DTT, and 10% D2O) contained an excess of 0.25 molar equivalents of d(GGTTAC) to ensure that Pot1pN was present in a homogeneous ssDNA-bound complex."}]}],"sequence_construct":"MRGSHHHHHHGSMGEDVIDSLQLNELLNAGEYKIGELTFQSIRSSQELQKKNTIVNLFGIVKDFTPSRQSLHGTKDWVTTVYLWDPTCDTSSIGLQIHLFSKQGNDLPVIKQVGQPLLLHQITLRSYRDRTQGLSKDQFRYALWPDFSSNSKDTLCPQPMPRLMKTGDKEEQFALLLNKIWDEQTNKHKNGELLSTS","statement":[{"text":"Additionally, we also observed a significant loss of dynamic motion in amides present within the T3/T4-binding pocket upon binding d(GGTTAC), specifically with respect to those found in Loop12 and Loop34. ","type":"Results"},{"text":"Unlike the G1/G2-binding pocket, which is well ordered in the presence and in the absence of ssDNA, picosecond–nanosecond motions show that backbone amides present in Loop12, which forms the centerpiece of the T3/T4-binding pocket, are significantly disordered in the absence of ssDNA and ordered upon binding (Fig. 4). This loop is well structured in Pot1pNB, suggesting that formation of the T3/T4-binding pocket proceeds via a “mutually” induced-fit type of mechanism that requires the coordinated co-folding of both Loop12 and Loop34 with the unstructured oligonucleotide40,45 (Fig. 4).","type":"Discussion"},{"text":"The studied construct contains an N-terminal tag of 12 residues and the first 185 of the protein (this is evident from Supplementary Table 1.), together 197 residues. Residues 91 to 103 correspond to the Loop34 that is one of the longest disordered loops that also takes part in DNA-binding. Residues boundaries of the loops were derived from Supplementary Table X, column \"Pot1pNF Derived Residue Limits\", taking into account that the studied sequence started with a 12-residue tag.","type":"Curator statement"}],"last_modified_by":"rpancsa","last_modified_name":"Rita Pancsa","conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":30,"statements":[{"type":"Figure","text":"Parameters determined from 15N relaxation experiments. HetNOE (upper panel), R1 (middle panel), and R2 (lower panel) are plotted as a function of residue number for Pot1pNF (black) and Pot1pNB (magenta) collected at 500 MHz at 30 °C. "}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.15,"statements":[{"type":"Methods","text":"Complexes of 15N-labeled Pot1pN and d(GGTTAC) at 1.25 mM in NMR sample buffer (50 mM KH2PO4, pH 6.15, 50 mM NaCl, 1 mM d-DTT, and 10% D2O) contained an excess of 0.25 molar equivalents of d(GGTTAC) to ensure that Pot1pN was present in a homogeneous ssDNA-bound complex."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-06T13:06:04.748Z"}},{"start":91,"end":103,"reference_id":"19232358","reference_source":"pmid","reference_html":"Insights into the dynamics of specific telomeric single-stranded DNA recognition by Pot1pN. <i> Croy JE, Wuttke DS. </i> J Mol Biol, 2009","date":"2026-01-05T13:06:58.451Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"GO:0003677","term_name":"DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The 22-kDa (His)6-Pot1pN DBD from the S. pombe Pot1 protein was expressed in Escherichia coli, purified, and stored according to the protocols established by Lei et al.10 with final purified yields of 25 mg/L. Uniform 13C–15N or 15N labeling was performed by expressing each protein in modified minimal M9 media."}]}],"ec_go":"EXP","region_id":"DP04536r010","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Methods","text":"Complexes of 15N-labeled Pot1pN and d(GGTTAC) at 1.25 mM in NMR sample buffer (50 mM KH2PO4, pH 6.15, 50 mM NaCl, 1 mM d-DTT, and 10% D2O) contained an excess of 0.25 molar equivalents of d(GGTTAC) to ensure that Pot1pN was present in a homogeneous ssDNA-bound complex."}]}],"sequence_construct":"MRGSHHHHHHGSMGEDVIDSLQLNELLNAGEYKIGELTFQSIRSSQELQKKNTIVNLFGIVKDFTPSRQSLHGTKDWVTTVYLWDPTCDTSSIGLQIHLFSKQGNDLPVIKQVGQPLLLHQITLRSYRDRTQGLSKDQFRYALWPDFSSNSKDTLCPQPMPRLMKTGDKEEQFALLLNKIWDEQTNKHKNGELLSTS","statement":[{"text":"Additionally, we also observed a significant loss of dynamic motion in amides present within the T3/T4-binding pocket upon binding d(GGTTAC), specifically with respect to those found in Loop12 and Loop34. ","type":"Results"},{"text":"Unlike the G1/G2-binding pocket, which is well ordered in the presence and in the absence of ssDNA, picosecond–nanosecond motions show that backbone amides present in Loop12, which forms the centerpiece of the T3/T4-binding pocket, are significantly disordered in the absence of ssDNA and ordered upon binding (Fig. 4). This loop is well structured in Pot1pNB, suggesting that formation of the T3/T4-binding pocket proceeds via a “mutually” induced-fit type of mechanism that requires the coordinated co-folding of both Loop12 and Loop34 with the unstructured oligonucleotide40,45 (Fig. 4).","type":"Discussion"},{"text":"The studied construct contains an N-terminal tag of 12 residues and the first 185 of the protein (this is evident from Supplementary Table 1.), together 197 residues. Residues 91 to 103 correspond to the Loop34 that is one of the longest disordered loops that also takes part in DNA-binding. Residues boundaries of the loops were derived from Supplementary Table X, column \"Pot1pNF Derived Residue Limits\", taking into account that the studied sequence started with a 12-residue tag.","type":"Curator statement"}],"term_comment":"","term_def":"\"Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).\" [GOC:dph, GOC:jl, GOC:tb, GOC:vw]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"rpancsa","last_modified_name":"Rita Pancsa","conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":"within normal range","value":30,"statements":[{"type":"Figure","text":"Parameters determined from 15N relaxation experiments. HetNOE (upper panel), R1 (middle panel), and R2 (lower panel) are plotted as a function of residue number for Pot1pNF (black) and Pot1pNB (magenta) collected at 500 MHz at 30 °C."}]},{"term_id":"NCIT:C45997","term_name":"pH","unit_name":"pH","unit_id":"UO:0000196","deviation":"within normal range","value":6.15,"statements":[{"type":"Methods","text":"Complexes of 15N-labeled Pot1pN and d(GGTTAC) at 1.25 mM in NMR sample buffer (50 mM KH2PO4, pH 6.15, 50 mM NaCl, 1 mM d-DTT, and 10% D2O) contained an excess of 0.25 molar equivalents of d(GGTTAC) to ensure that Pot1pN was present in a homogeneous ssDNA-bound complex."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-06T13:08:20.325Z"}},{"start":91,"end":103,"reference_id":"19232358","reference_source":"pmid","reference_html":"Insights into the dynamics of specific telomeric single-stranded DNA recognition by Pot1pN. <i> Croy JE, Wuttke DS. </i> J Mol Biol, 2009","date":"2026-01-05T12:33:53.951Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal"}],"region_id":"DP04536r011","sequence_construct":"MRGSHHHHHHGSMGEDVIDSLQLNELLNAGEYKIGELTFQSIRSSQELQKKNTIVNLFGIVKDFTPSRQSLHGTKDWVTTVYLWDPTCDTSSIGLQIHLFSKQGNDLPVIKQVGQPLLLHQITLRSYRDRTQGLSKDQFRYALWPDFSSNSKDTLCPQPMPRLMKTGDKEEQFALLLNKIWDEQTNKHKNGELLSTS","statement":[{"text":"Additionally, we also observed a significant loss of dynamic motion in amides present within the T3/T4-binding pocket upon binding d(GGTTAC), specifically with respect to those found in Loop12 and Loop34. ","type":"Results"},{"text":"Unlike the G1/G2-binding pocket, which is well ordered in the presence and in the absence of ssDNA, picosecond–nanosecond motions show that backbone amides present in Loop12, which forms the centerpiece of the T3/T4-binding pocket, are significantly disordered in the absence of ssDNA and ordered upon binding (Fig. 4). This loop is well structured in Pot1pNB, suggesting that formation of the T3/T4-binding pocket proceeds via a “mutually” induced-fit type of mechanism that requires the coordinated co-folding of both Loop12 and Loop34 with the unstructured oligonucleotide40,45 (Fig. 4).","type":"Discussion"},{"text":"The studied construct contains an N-terminal tag of 12 residues and the first 185 of the protein (this is evident from Supplementary Table 1.), together 197 residues. Residues 91 to 103 correspond to the Loop34 that is one of the longest disordered loops connecting individual β-strands. Residues boundaries of the loops were derived from Supplementary Table X, column \"Pot1pNF Derived Residue Limits\", taking into account that the studied sequence started with a 12-residue tag.","type":"Curator statement"}],"states_connection":[{"source":"DP04536r005","target":"DP04536r009"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-05-06T13:10:07.650Z"}}],"__v":0,"disorder_content":0.11531531531531532,"disprot_consensus":{"full":[{"start":1,"end":18,"type":"D"},{"start":54,"end":64,"type":"T"},{"start":71,"end":82,"type":"D"},{"start":91,"end":103,"type":"T"},{"start":176,"end":185,"type":"D"}],"Structural state":[{"start":1,"end":18,"type":"D"},{"start":54,"end":64,"type":"D"},{"start":71,"end":82,"type":"D"},{"start":91,"end":103,"type":"D"},{"start":176,"end":185,"type":"D"}],"Molecular function":[{"start":54,"end":64,"type":"F"},{"start":91,"end":103,"type":"F"}],"Structural transition":[{"start":54,"end":64,"type":"T"},{"start":91,"end":103,"type":"T"}]}},{"acc":"O13615","sequence":"MTEAKNISDDTDVLSLTTNSLRTSKTLFGAEFGSVTSFDDTVAQNLKRTYKEHLEYGSVLGGTVGKRKNRHYEEDTIGSNALTVRADSENPSSQVITKFSDPNKKIAGQVSMQSLEKIKGVPEAAHRIAGESQASLVKRTLAEQIRPEWHAPWTLMRVISGHLGWVRCVDVEPGNQWFCTGAGDRTIKIWDLASGVLKLTLTGHIATVRGLAVSPRHPYLFSCGEDKMVKCWDLETNKVIRHYHGHLSGVYALKLHPTLDVLVTAGRDAVARVWDMRTRQNVHVLSGHKSTVASLAVQEFDPQVVTGSMDSTIRLWDLAAGKTLTTLTHHKKTVRALSLHPDEFTFASGSSDNIKHWKFPEGAFMGNFEGHNAIVNTLSINSDNVMFSGADNGSMCFWDWKSGHKYQELQSVVQPGSLDSEAGIFASSFDKTGLRLITCEADKSVKIYKQVDNATPETHPNLPWTPSNLRRRY","creator":"vnugnes","dataset":[],"date":"2026-01-07T14:18:29.079Z","disprot_id":"DP04537","features":{"pfam":[{"id":"PF00400","name":"WD domain, G-beta repeat","start":154,"end":191},{"id":"PF23098","name":"Nucleolar protein 10-like, N-terminal domain","start":209,"end":392}]},"genes":[{"name":{"value":"prp5","_id":"695e6b3538549a2e1d36cfeb","evidences":[]},"synonyms":[{"value":"cwf1","_id":"695e6b3538549a2e1d36cfec","evidences":[]}],"olnNames":[],"orfNames":[{"value":"pi024","_id":"695e6b3538549a2e1d36cfed","evidences":[]},{"value":"SPBP22H7.07","_id":"695e6b3538549a2e1d36cfee","evidences":[]}],"_id":"695e6b3538549a2e1d36cfea"}],"length":473,"name":"Pre-mRNA-splicing factor prp5","ncbi_taxon_id":284812,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","regions_counter":1,"released":"2026_06","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"regions":[{"start":1,"end":82,"reference_id":"39833470","reference_source":"pmid","reference_html":"Structures of aberrant spliceosome intermediates on their way to disassembly. <i> Soni K, Horvath A, Dybkov O, Schwan M, Trakansuebkul S, Flemming D, Wild K, Urlaub H, Fischer T, Sinning I. </i> Nat Struct Mol Biol, 2025","date":"2026-01-07T14:22:50.594Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"9ESI"},{"db":"PDB","id":"9ESH"},{"db":"EMDB","id":"19942"}],"region_id":"DP04537r001","statement":[{"text":"This region lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"__v":0,"disorder_content":0.1733615221987315,"disprot_consensus":{"full":[{"start":1,"end":82,"type":"D"}],"Structural state":[{"start":1,"end":82,"type":"D"}]}},{"acc":"O14011","sequence":"MFCSISGETPKEPVISRVSGNVYEKRLIEQVIRETSKDPVTQQECTLEDLVPVKVPDFVRPRPPSATSLPALLSLFQEEWDSVALEQFELRRNLTETKQELSTALYSLDAALRVISRLTKERDEAREALAKFSDNIGTVSSKTIEVQEVEMGESDDQLKTSLRSTVEKTFQELSSKRKRTKLQPKWATDDAVSQLLQATPSTILENLETESTTSFFPSPENSSFVLCLHKDELLCLDIQSNSTLKIFEGSALACCWLTSSKIAVATADAISIFEFPVSSSGLQSVGEPTSSIPIDEKVNFLQAHPSGEYLLAASNEKCYIFSLKSQVYNITVAQHITSLAVHPDGNLFVAGLENGELRFFETSSGNELTKFGPHSSPVKTLQFGENGYWLVVTTNDDSDIFIWDLRKSELVQKIPLQTKVAAVSLDITSQLLVSSDGETLYVHIYVKSSKSWRCMSQTHVSSISNLVWLNELHQLLFSTSNGAILRLG","creator":"vnugnes","dataset":[],"date":"2026-01-07T14:25:11.815Z","disprot_id":"DP04538","features":{"pfam":[{"id":"PF08606","name":"Prp19/Pso4-like","start":66,"end":131},{"id":"PF12894","name":"Anaphase-promoting complex subunit 4 WD40 domain","start":324,"end":386}]},"genes":[{"name":{"value":"prp19","_id":"695e6cc838549a2e1d36cff8","evidences":[]},"synonyms":[{"value":"cwf8","_id":"695e6cc838549a2e1d36cff9","evidences":[]}],"olnNames":[],"orfNames":[{"value":"SPAC29A4.08c","_id":"695e6cc838549a2e1d36cffa","evidences":[]}],"_id":"695e6cc838549a2e1d36cff7"}],"length":488,"name":"Pre-mRNA-processing factor 19","ncbi_taxon_id":284812,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","regions_counter":1,"released":"2026_06","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"regions":[{"start":136,"end":172,"reference_id":"26292707","reference_source":"pmid","reference_html":"Structure of a yeast spliceosome at 3.6-angstrom resolution. <i> Yan C, Hang J, Wan R, Huang M, Wong CC, Shi Y. </i> Science, 2015","date":"2026-01-07T14:27:36.999Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"EMDB","id":"6413"},{"db":"PDB","id":"3JB9"}],"region_id":"DP04538r001","statement":[{"text":"Some areas of very weak EM density, probably reflecting dynamic components of the spliceosome, remain unassigned.","type":"Results"}]}],"__v":0,"disorder_content":0.07581967213114754,"disprot_consensus":{"full":[{"start":136,"end":172,"type":"D"}],"Structural state":[{"start":136,"end":172,"type":"D"}]}},{"acc":"P39964","sequence":"MVVLKGGAWKNTEDEILKAAVSKYGKNQWARISSLLVRKTPKQCKARWYEWIDPSIKKTEWSREEDEKLLHLAKLLPTQWRTIAPIVGRTATQCLERYQKLLDDLEAKENEQLGLISGEGAEAAAPVNDPNSRLRFGEAEPNLETLPALPDAIDMDEDEKEMLSEARARLANTQGKKAKRKDREKQLELTRRLSHLQKRRELKAAGINIKLFRRKKNEMDYNASIPFEKKPAIGFYDTSEEDRQNFREKREADQKIIENGIRNNEMESEGRKFGHFEKPKPIDRVKKPNKDAQEEKMRRLAEAEQMSKRRKLNLPSPTVSQDELDKVVKLGFAGDRARAMTDTTPDANYSTNLLGKYTQIERATPLRTPISGELEGREDSVTIEVRNQLMRNREQSSLLGQESIPLQPGGTGYTGVTPSHAANGSALAAPQATPFRTPRDTFSINAAAERAGRLASERENKIRLKALRELLAKLPKPKNDYELMEPRFADETDVEATVGVLEEDATDRERRIQERIAEKERLAKARRSQVIQRDLIRPSVTQPEKWKRSLENEDPTANVLLKEMIALISSDAINYPFGNSKVKGTANKVPDLSNEEIERCRLLLKKEIGQLESDDYIQFEKEFLETYSALHNTSSLLPGLVIYEEDDEDVEAAEKFYTNDIQRDLAKKALECNKLENRVYDLVRSSYEQRNFLIKKISHAWKALQTERKNLTCYEFLYNQERLALPNRLEAAEIELSKMQQIEAYAQQDYARVTGQN","creator":"vnugnes","dataset":[],"date":"2026-01-07T14:34:30.651Z","disprot_id":"DP04539","features":{"pfam":[{"id":"PF11831","name":"pre-mRNA splicing factor component","start":416,"end":612},{"id":"PF13921","name":"Myb-like DNA-binding domain","start":9,"end":69}]},"genes":[{"name":{"value":"cdc5","_id":"695e6ef638549a2e1d36d006","evidences":[]},"synonyms":[],"olnNames":[],"orfNames":[{"value":"SPAC644.12","_id":"695e6ef638549a2e1d36d007","evidences":[]}],"_id":"695e6ef638549a2e1d36d005"}],"length":757,"name":"Pre-mRNA-splicing factor cdc5","ncbi_taxon_id":284812,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","regions_counter":4,"released":"2026_06","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"regions":[{"start":272,"end":501,"reference_id":"26292707","reference_source":"pmid","reference_html":"Structure of a yeast spliceosome at 3.6-angstrom resolution. <i> Yan C, Hang J, Wan R, Huang M, Wong CC, Shi Y. </i> Science, 2015","date":"2026-01-07T14:35:31.306Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"EMDB","id":"6413"},{"db":"PDB","id":"3JB9"}],"region_id":"DP04539r001","statement":[{"text":"Some areas of very weak EM density, probably reflecting dynamic components of the spliceosome, remain unassigned.","type":"Results"},{"text":"The Cryo-EM structure of the yeast spliceosome complex shows this region of the protein lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":110,"end":153,"reference_id":"26292707","reference_source":"pmid","reference_html":"Structure of a yeast spliceosome at 3.6-angstrom resolution. <i> Yan C, Hang J, Wan R, Huang M, Wong CC, Shi Y. </i> Science, 2015","date":"2026-01-07T14:35:54.317Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"EMDB","id":"6413"},{"db":"PDB","id":"3JB9"}],"region_id":"DP04539r002","statement":[{"text":"Some areas of very weak EM density, probably reflecting dynamic components of the spliceosome, remain unassigned.","type":"Results"},{"text":"The Cryo-EM structure of the yeast spliceosome complex shows this region of the protein lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":204,"end":220,"reference_id":"26292707","reference_source":"pmid","reference_html":"Structure of a yeast spliceosome at 3.6-angstrom resolution. <i> Yan C, Hang J, Wan R, Huang M, Wong CC, Shi Y. </i> Science, 2015","date":"2026-01-07T14:36:06.526Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"EMDB","id":"6413"},{"db":"PDB","id":"3JB9"}],"region_id":"DP04539r003","statement":[{"text":"Some areas of very weak EM density, probably reflecting dynamic components of the spliceosome, remain unassigned.","type":"Results"},{"text":"The Cryo-EM structure of the yeast spliceosome complex shows this region of the protein lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":640,"end":651,"reference_id":"26292707","reference_source":"pmid","reference_html":"Structure of a yeast spliceosome at 3.6-angstrom resolution. <i> Yan C, Hang J, Wan R, Huang M, Wong CC, Shi Y. </i> Science, 2015","date":"2026-01-07T14:36:31.025Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"EMDB","id":"6413"},{"db":"PDB","id":"3JB9"}],"region_id":"DP04539r004","statement":[{"text":"Some areas of very weak EM density, probably reflecting dynamic components of the spliceosome, remain unassigned.","type":"Results"},{"text":"The Cryo-EM structure of the yeast spliceosome complex shows this region of the protein lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"__v":0,"disorder_content":0.4002642007926024,"disprot_consensus":{"full":[{"start":110,"end":153,"type":"D"},{"start":204,"end":220,"type":"D"},{"start":272,"end":501,"type":"D"},{"start":640,"end":651,"type":"D"}],"Structural state":[{"start":110,"end":153,"type":"D"},{"start":204,"end":220,"type":"D"},{"start":272,"end":501,"type":"D"},{"start":640,"end":651,"type":"D"}]}},{"acc":"Q7LL14","sequence":"MNQNTLYVNNLNDKINKNDLRTALYMLFSTYGTVVDIVALKTPKMRGQAHVVFFDPSAAAIAMKALKNFIFFGKEMKIQYAHSKSKIIERIVAENDSRGPLKRLRDEADLE","creator":"vnugnes","dataset":["RNA-binding proteins"],"date":"2026-01-07T14:39:30.490Z","disprot_id":"DP04540","features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":6,"end":77}]},"genes":[{"name":{"value":"msl1","_id":"695e702238549a2e1d36d015","evidences":[]},"synonyms":[],"olnNames":[],"orfNames":[{"value":"pi056","_id":"695e702238549a2e1d36d016","evidences":[]},{"value":"SPBC8D2.09c","_id":"695e702238549a2e1d36d017","evidences":[]}],"_id":"695e702238549a2e1d36d014"}],"length":111,"name":"Probable U2 small nuclear ribonucleoprotein B''","ncbi_taxon_id":284812,"organism":"Schizosaccharomyces pombe (strain 972 / ATCC 24843)","regions_counter":2,"released":"2026_06","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Taphrinomycotina","Schizosaccharomycetes","Schizosaccharomycetales","Schizosaccharomycetaceae","Schizosaccharomyces"],"regions":[{"start":94,"end":111,"reference_id":"26292707","reference_source":"pmid","reference_html":"Structure of a yeast spliceosome at 3.6-angstrom resolution. <i> Yan C, Hang J, Wan R, Huang M, Wong CC, Shi Y. </i> Science, 2015","date":"2026-01-07T14:40:28.597Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"EMDB","id":"6413"},{"db":"PDB","id":"3JB9"}],"region_id":"DP04540r001","statement":[{"text":"Some areas of very weak EM density, probably reflecting dynamic components of the spliceosome, remain unassigned.","type":"Article"},{"text":"The Cryo-EM structure of the yeast spliceosome complex shows this region of the protein lacks electron density, indicating it is disordered.","type":"Curator statement"}]},{"start":94,"end":111,"reference_id":"26292707","reference_source":"pmid","reference_html":"Structure of a yeast spliceosome at 3.6-angstrom resolution. <i> Yan C, Hang J, Wan R, Huang M, Wong CC, Shi Y. </i> Science, 2015","date":"2026-01-07T14:40:40.875Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"EMDB","id":"6413"},{"db":"PDB","id":"3JB9"}],"region_id":"DP04540r002","statement":[{"text":"Some areas of very weak EM density, probably reflecting dynamic components of the spliceosome, remain unassigned.","type":"Article"},{"text":"The Cryo-EM structure of the yeast spliceosome complex shows this region of the protein lacks electron density, indicating it is disordered.","type":"Curator statement"}]}],"__v":0,"disorder_content":0.16216216216216217,"disprot_consensus":{"full":[{"start":94,"end":111,"type":"D"}],"Structural state":[{"start":94,"end":111,"type":"D"}],"Disorder function":[{"start":94,"end":111,"type":"F"}]}},{"acc":"Q92959","sequence":"MGLLPKLGASQGSDTSTSRAGRCARSVFGNIKVFVLCQGLLQLCQLLYSAYFKSSLTTIEKRFGLSSSSSGLISSLNEISNAILIIFVSYFGSRVHRPRLIGIGGLFLAAGAFILTLPHFLSEPYQYTLASTGNNSRLQAELCQKHWQDLPPSKCHSTTQNPQKETSSMWGLMVVAQLLAGIGTVPIQPFGISYVDDFSEPSNSPLYISILFAISVFGPAFGYLLGSVMLQIFVDYGRVNTAAVNLVPGDPRWIGAWWLGLLISSALLVLTSFPFFFFPRAMPIGAKRAPATADEARKLEEAKSRGSLVDFIKRFPCIFLRLLMNSLFVLVVLAQCTFSSVIAGLSTFLNKFLEKQYGTSAAYANFLIGAVNLPAAALGMLFGGILMKRFVFSLQAIPRIATTIITISMILCVPLFFMGCSTPTVAEVYPPSTSSSIHPQSPACRRDCSCPDSIFHPVCGDNGIEYLSPCHAGCSNINMSSATSKQLIYLNCSCVTGGSASAKTGSCPVPCAHFLLPAIFLISFVSLIACISHNPLYMMVLRVVNQEEKSFAIGVQFLLMRLLAWLPSPALYGLTIDHSCIRWNSLCLGRRGACAYYDNDALRDRYLGLQMGYKALGMLLLCFISWRVKKNKEYNVQKAAGLI","creator":"vnugnes","dataset":[],"date":"2026-01-21T15:48:54.534Z","disprot_id":"DP04542","features":{"pfam":[{"id":"PF03137","name":"Organic Anion Transporter Polypeptide (OATP) family","start":33,"end":446},{"id":"PF03137","name":"Organic Anion Transporter Polypeptide (OATP) family","start":495,"end":602},{"id":"PF07648","name":"Kazal-type serine protease inhibitor domain","start":447,"end":494}]},"genes":[{"name":{"value":"SLCO2A1","evidences":[{"source":{"id":"HGNC:10955","name":"HGNC","url":"https://www.genenames.org/cgi-bin/gene_symbol_report?hgnc_id=HGNC:10955","_id":"6970f56619ab84cf24162801"},"code":"ECO:0000312","_id":"6970f56619ab84cf24162800"}],"_id":"6970f56619ab84cf241627ff"},"synonyms":[{"value":"OATP2A1","_id":"6970f56619ab84cf24162802","evidences":[]},{"value":"SLC21A2","_id":"6970f56619ab84cf24162803","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"6970f56619ab84cf241627fe"}],"length":643,"name":"Solute carrier organic anion transporter family member 2A1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":11,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":421,"end":513,"reference_id":"41326388","reference_source":"pmid","reference_html":"Molecular basis of prostaglandin E&lt;sub&gt;2&lt;/sub&gt; reuptake by organic anion transporter PGT. <i> Zhu Z, Li Y, Xia H, Yang C, Zhou Z, Chao Y, Ba Q, Li D, Qu Q. </i> Nat Commun, 2025","date":"2026-01-21T17:16:57.220Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":4,"cross_refs":[{"db":"PDB","id":"8KGI"},{"db":"EMDB","id":"37222"}],"region_id":"DP04542r001","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"73001","entry_name":null},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"34086","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"138742","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"49839603"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92959"}],"statement":[{"text":"Aside from the monomeric PGT structures, a substantial population of dimeric PGT particles was observed in both the apo and the PGE2-incubated samples (Supplementary Fig. 2a, b).","type":"Results"},{"text":"Interestingly, no obvious ligand density was discernible in the transport funnels of the PGE2/PGT dimeric map. Given the striking similarity between the two dimer maps, we merged the two datasets to generate an improved dimer map (PGTdd) with a global resolution of 3.16 Å (Supplementary Fig. 2c–e and Supplementary Table 1). To our surprise, the ECD and TM12 were not resolved despite their overall map resolution being comparable to PGTapo (Fig. 5a and Supplementary Fig. 3).","type":"Results"},{"text":"To investigate whether this conformational dynamics was an artifact induced by the detergent micelle, we reconstituted the PGT protein into a lipid nanodisc (Supplementary Fig. 1c). A considerable number of dimeric PGT averages were identified in this lipid environment, suggesting the dimer formation of the transporter in the membrane. Despite having a lower resolution (4.24 Å), the map of the nanodisc sample (PGTdn) shares a similar configuration, including the ill-defined ECDs and the missing TM12 helices, with PGTdd (Supplementary Fig. 12d).","type":"Results"},{"text":"As a transmembrane protein, PGT was studied in membrane-mimetic \nenvironments using detergent micelles (LMNG/CHS) and lipid nanodiscs (POPC:POPS). In both contexts, PGT acquired a dimeric conformation that showed disorder regions in the extracellular domain (ECD, including the Kazal-like domain residues ~425-508) and the C-terminal transmembrane helix TM12.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":572,"end":643,"reference_id":"41326388","reference_source":"pmid","reference_html":"Molecular basis of prostaglandin E&lt;sub&gt;2&lt;/sub&gt; reuptake by organic anion transporter PGT. <i> Zhu Z, Li Y, Xia H, Yang C, Zhou Z, Chao Y, Ba Q, Li D, Qu Q. </i> Nat Commun, 2025","date":"2026-01-21T17:17:12.168Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"8KGI"},{"db":"EMDB","id":"37222"}],"region_id":"DP04542r002","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"73001","entry_name":null},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"34086","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"138742","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"49839603"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92959"}],"statement":[{"text":"Aside from the monomeric PGT structures, a substantial population of dimeric PGT particles was observed in both the apo and the PGE2-incubated samples (Supplementary Fig. 2a, b).","type":"Results"},{"text":"Interestingly, no obvious ligand density was discernible in the transport funnels of the PGE2/PGT dimeric map. Given the striking similarity between the two dimer maps, we merged the two datasets to generate an improved dimer map (PGTdd) with a global resolution of 3.16 Å (Supplementary Fig. 2c–e and Supplementary Table 1). To our surprise, the ECD and TM12 were not resolved despite their overall map resolution being comparable to PGTapo (Fig. 5a and Supplementary Fig. 3).","type":"Results"},{"text":"To investigate whether this conformational dynamics was an artifact induced by the detergent micelle, we reconstituted the PGT protein into a lipid nanodisc (Supplementary Fig. 1c). A considerable number of dimeric PGT averages were identified in this lipid environment, suggesting the dimer formation of the transporter in the membrane. Despite having a lower resolution (4.24 Å), the map of the nanodisc sample (PGTdn) shares a similar configuration, including the ill-defined ECDs and the missing TM12 helices, with PGTdd (Supplementary Fig. 12d).","type":"Results"},{"text":"As a transmembrane protein, PGT was studied in membrane-mimetic \nenvironments using detergent micelles (LMNG/CHS) and lipid nanodiscs (POPC:POPS). In both contexts, PGT acquired a dimeric conformation that showed disorder regions in the extracellular domain (ECD, including the Kazal-like domain residues ~425-508) and the C-terminal transmembrane helix TM12.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":1,"end":22,"reference_id":"41326388","reference_source":"pmid","reference_html":"Molecular basis of prostaglandin E&lt;sub&gt;2&lt;/sub&gt; reuptake by organic anion transporter PGT. <i> Zhu Z, Li Y, Xia H, Yang C, Zhou Z, Chao Y, Ba Q, Li D, Qu Q. </i> Nat Commun, 2025","date":"2026-01-21T17:18:31.827Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"EMDB","id":"37234"},{"db":"PDB","id":"8KGW"},{"db":"EMDB","id":"37222"},{"db":"PDB","id":"8KGI"},{"db":"EMDB","id":"37233"},{"db":"PDB","id":"8KGV"}],"region_id":"DP04542r003","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"73001","entry_name":null},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"34086","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15551","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"138742","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"49839603"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92959"}],"statement":[{"text":"While not described in the publication, specific regions lack electron density in all three deposited PDB structures regardless of oligomeric state (monomer vs. dimer), ligand occupancy (apo vs. PGE2-bound), or membrane-mimetic environment (detergent), indicating these regions are disordered upon any of those conditions.","type":"Curator statement"}]},{"start":127,"end":166,"reference_id":"41326388","reference_source":"pmid","reference_html":"Molecular basis of prostaglandin E&lt;sub&gt;2&lt;/sub&gt; reuptake by organic anion transporter PGT. <i> Zhu Z, Li Y, Xia H, Yang C, Zhou Z, Chao Y, Ba Q, Li D, Qu Q. </i> Nat Commun, 2025","date":"2026-01-21T17:18:54.979Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"EMDB","id":"37234"},{"db":"PDB","id":"8KGW"},{"db":"EMDB","id":"37222"},{"db":"PDB","id":"8KGI"},{"db":"EMDB","id":"37233"},{"db":"PDB","id":"8KGV"}],"region_id":"DP04542r004","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"73001","entry_name":null},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"34086","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15551","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"138742","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"49839603"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92959"}],"statement":[{"text":"While not described in the publication, specific regions lack electron density in all three deposited PDB structures regardless of oligomeric state (monomer vs. dimer), ligand occupancy (apo vs. PGE2-bound), or membrane-mimetic environment (detergent), indicating these regions are disordered upon any of those conditions.","type":"Curator statement"}]},{"start":284,"end":305,"reference_id":"41326388","reference_source":"pmid","reference_html":"Molecular basis of prostaglandin E&lt;sub&gt;2&lt;/sub&gt; reuptake by organic anion transporter PGT. <i> Zhu Z, Li Y, Xia H, Yang C, Zhou Z, Chao Y, Ba Q, Li D, Qu Q. </i> Nat Commun, 2025","date":"2026-01-21T17:20:03.770Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"EMDB","id":"37234"},{"db":"PDB","id":"8KGW"},{"db":"EMDB","id":"37222"},{"db":"PDB","id":"8KGI"},{"db":"EMDB","id":"37233"},{"db":"PDB","id":"8KGV"}],"region_id":"DP04542r005","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"73001","entry_name":null},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"34086","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15551","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"138742","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"49839603"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92959"}],"statement":[{"text":"While not described in the publication, specific regions lack electron density in all three deposited PDB structures regardless of oligomeric state (monomer vs. dimer), ligand occupancy (apo vs. PGE2-bound), or membrane-mimetic environment (detergent), indicating these regions are disordered upon any of those conditions.","type":"Curator statement"}]},{"start":421,"end":513,"reference_id":"41326388","reference_source":"pmid","reference_html":"Molecular basis of prostaglandin E&lt;sub&gt;2&lt;/sub&gt; reuptake by organic anion transporter PGT. <i> Zhu Z, Li Y, Xia H, Yang C, Zhou Z, Chao Y, Ba Q, Li D, Qu Q. </i> Nat Commun, 2025","date":"2026-01-21T17:40:32.212Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"EMDB","id":"37222"},{"db":"PDB","id":"8KGI"},{"db":"EMDB","id":"37233"},{"db":"PDB","id":"8KGV"},{"db":"PDB","id":"8KGW"},{"db":"EMDB","id":"37234"}],"region_id":"DP04542r006","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"73001","entry_name":null},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"34086","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"138742","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"49839603"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92959"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15551","entry_name":null}],"statement":[{"text":"To our surprise, the ECD and TM12 were not resolved despite their overall map resolution being comparable to PGTapo (Fig. 5a and Supplementary Fig. 3).","type":"Results"},{"text":"As mentioned above, TM12 and the extracellular regions, including the Kazal-like domain, became flexible.","type":"Results"},{"text":"When studied under membrane-mimetic environments using detergent micelles (LMNG/CHS) and lipid nanodiscs (POPC:POPS) PGT acquired a dimeric conformation that presented disorder regions that were ordered both in the apo- and PGE2-bounded structures.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","states_connection":[{"source":"DP04542r009","target":"DP04542r001"}]},{"start":572,"end":643,"reference_id":"41326388","reference_source":"pmid","reference_html":"Molecular basis of prostaglandin E&lt;sub&gt;2&lt;/sub&gt; reuptake by organic anion transporter PGT. <i> Zhu Z, Li Y, Xia H, Yang C, Zhou Z, Chao Y, Ba Q, Li D, Qu Q. </i> Nat Commun, 2025","date":"2026-01-21T17:40:10.618Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000014","term_name":"order to disorder","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"EMDB","id":"37222"},{"db":"PDB","id":"8KGI"},{"db":"EMDB","id":"37233"},{"db":"PDB","id":"8KGV"},{"db":"PDB","id":"8KGW"},{"db":"EMDB","id":"37234"}],"region_id":"DP04542r007","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"73001","entry_name":null},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"34086","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"138742","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"49839603"},{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"Q92959"},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15551","entry_name":null}],"statement":[{"text":"To our surprise, the ECD and TM12 were not resolved despite their overall map resolution being comparable to PGTapo (Fig. 5a and Supplementary Fig. 3).","type":"Results"},{"text":"As mentioned above, TM12 and the extracellular regions, including the Kazal-like domain, became flexible.","type":"Results"},{"text":"When studied under membrane-mimetic environments using detergent micelles (LMNG/CHS) and lipid nanodiscs (POPC:POPS) PGT acquired a dimeric conformation that presented disorder regions that were ordered both in the apo- and PGE2-bounded structures.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","states_connection":[{"source":"DP04542r008","target":"DP04542r002"}]},{"start":572,"end":643,"reference_id":"41326388","reference_source":"pmid","reference_html":"Molecular basis of prostaglandin E&lt;sub&gt;2&lt;/sub&gt; reuptake by organic anion transporter PGT. <i> Zhu Z, Li Y, Xia H, Yang C, Zhou Z, Chao Y, Ba Q, Li D, Qu Q. </i> Nat Commun, 2025","date":"2026-01-21T17:38:35.452Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"EMDB","id":"37233"},{"db":"PDB","id":"8KGV"},{"db":"PDB","id":"8KGW"},{"db":"EMDB","id":"37234"}],"region_id":"DP04542r008","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15551","entry_name":null}],"statement":[{"text":"As mentioned above, TM12 and the extracellular regions, including the Kazal-like domain, became flexible.","type":"Results"},{"text":"While when dimeric, under membrane-mimetic environments, this region is disodered, in the apo- and PGE2-bounded structures this regions are ordered.","type":"Curator statement"}]},{"start":421,"end":513,"reference_id":"41326388","reference_source":"pmid","reference_html":"Molecular basis of prostaglandin E&lt;sub&gt;2&lt;/sub&gt; reuptake by organic anion transporter PGT. <i> Zhu Z, Li Y, Xia H, Yang C, Zhou Z, Chao Y, Ba Q, Li D, Qu Q. </i> Nat Commun, 2025","date":"2026-01-21T17:39:39.907Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000006","term_name":"order","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"EMDB","id":"37233"},{"db":"PDB","id":"8KGV"},{"db":"PDB","id":"8KGW"},{"db":"EMDB","id":"37234"}],"region_id":"DP04542r009","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15551","entry_name":null}],"statement":[{"text":"As mentioned above, TM12 and the extracellular regions, including the Kazal-like domain, became flexible.","type":"Results"},{"text":"While when dimeric, under membrane-mimetic environments, this region is disodered, in the apo- and PGE2-bounded structures this regions are ordered.","type":"Curator statement"}]}],"__v":0,"disorder_content":0.38724727838258166,"disprot_consensus":{"full":[{"start":1,"end":22,"type":"D"},{"start":127,"end":166,"type":"D"},{"start":284,"end":305,"type":"D"},{"start":421,"end":513,"type":"T"},{"start":572,"end":643,"type":"T"}],"Structural state":[{"start":1,"end":22,"type":"D"},{"start":127,"end":166,"type":"D"},{"start":284,"end":305,"type":"D"},{"start":421,"end":513,"type":"D"},{"start":572,"end":643,"type":"D"}],"Structural transition":[{"start":421,"end":513,"type":"T"},{"start":572,"end":643,"type":"T"}]}},{"acc":"O60664","sequence":"MSADGAEADGSTQVTVEEPVQQPSVVDRVASMPLISSTCDMVSAAYASTKESYPHIKTVCDAAEKGVRTLTAAAVSGAQPILSKLEPQIASASEYAHRGLDKLEENLPILQQPTEKVLADTKELVSSKVSGAQEMVSSAKDTVATQLSEAVDATRGAVQSGVDKTKSVVTGGVQSVMGSRLGQMVLSGVDTVLGKSEEWADNHLPLTDAELARIATSLDGFDVASVQQQRQEQSYFVRLGSLSERLRQHAYEHSLGKLRATKQRAQEALLQLSQVLSLMETVKQGVDQKLVEGQEKLHQMWLSWNQKQLQGPEKEPPKPEQVESRALTMFRDIAQQLQATCTSLGSSIQGLPTNVKDQVQQARRQVEDLQATFSSIHSFQDLSSSILAQSRERVASAREALDHMVEYVAQNTPVTWLVGPFAPGITEKAPEEKK","creator":"vnugnes","dataset":[],"date":"2026-03-31T16:05:09.045Z","disprot_id":"DP04560","features":{"pfam":[{"id":"PF03036","name":"Perilipin family","start":20,"end":424}]},"genes":[{"name":{"value":"PLIN3","_id":"69cbf0b557069de95ea67490","evidences":[]},"synonyms":[{"value":"M6PRBP1","_id":"69cbf0b557069de95ea67491","evidences":[]},{"value":"TIP47","_id":"69cbf0b557069de95ea67492","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"69cbf0b557069de95ea6748f"}],"length":434,"name":"Perilipin-3","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":6,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":1,"end":200,"reference_id":"37268630","reference_source":"pmid","reference_html":"Structural insights into perilipin 3 membrane association in response to diacylglycerol accumulation. <i> Choi YM, Ajjaji D, Fleming KD, Borbat PP, Jenkins ML, Moeller BE, Fernando S, Bhatia SR, Freed JH, Burke JE, Thiam AR, Airola MV. </i> Nat Commun, 2023","date":"2026-03-31T16:05:52.797Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04560r001","statement":[{"text":"After the deuterium pulse, the first 200 residues of PLIN3 comprising the PAT domain and 11-mer repeats were fully deuterated, indicating these regions are completely disordered in the absence of membranes (Fig. 2a).","type":"Results"}]},{"start":1,"end":200,"reference_id":"37268630","reference_source":"pmid","reference_html":"Structural insights into perilipin 3 membrane association in response to diacylglycerol accumulation. <i> Choi YM, Ajjaji D, Fleming KD, Borbat PP, Jenkins ML, Moeller BE, Fernando S, Bhatia SR, Freed JH, Burke JE, Thiam AR, Airola MV. </i> Nat Commun, 2023","date":"2026-03-31T16:54:30.476Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005543","term_name":"phospholipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"ec_go":"EXP","region_id":"DP04560r002","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"183654","entry_name":null},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"9963917"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"136212542"}],"statement":[{"text":"In comparison to previous results that demonstrated the 11-mer repeats are sufficient for the lipid droplet association30,31, this suggests that the PAT domain and 11-mer repeats are both major contributors to membrane binding. Consistently, we found that a purified PAT/11-mer repeats fragment displayed similar membrane recruitment as full-length PLIN3 to DO liposomes enriched in DAG and PA, and 4ME liposomes (Fig. 2c, d).","type":"Results"}],"term_comment":"","term_def":"\"Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester.\" [ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":1,"end":200,"reference_id":"37268630","reference_source":"pmid","reference_html":"Structural insights into perilipin 3 membrane association in response to diacylglycerol accumulation. <i> Choi YM, Ajjaji D, Fleming KD, Borbat PP, Jenkins ML, Moeller BE, Fernando S, Bhatia SR, Freed JH, Burke JE, Thiam AR, Airola MV. </i> Nat Commun, 2023","date":"2026-03-31T16:31:18.169Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04560r003","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"183654","entry_name":null},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"9963917"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"136212542"}],"statement":[{"text":"The HDX-MS results suggested that membrane binding induces the formation of a secondary structure in the PAT domain and 11-mer repeats.","type":"Results"},{"text":"Based on these results we concluded that the PAT domain and 11-mer repeats of PLIN3 are intrinsically disordered in the absence of membranes, with inducible amphipathic alpha helices being stabilized upon membrane binding.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":22,"end":116,"reference_id":"37268630","reference_source":"pmid","reference_html":"Structural insights into perilipin 3 membrane association in response to diacylglycerol accumulation. <i> Choi YM, Ajjaji D, Fleming KD, Borbat PP, Jenkins ML, Moeller BE, Fernando S, Bhatia SR, Freed JH, Burke JE, Thiam AR, Airola MV. </i> Nat Commun, 2023","date":"2026-03-31T16:38:22.056Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0019992","term_name":"diacylglycerol binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006236","ec_ontology":"ECO","ec_name":"protein hydrogen-deuterium exchange mass spectrometry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"EXP","interaction_partner":[{"db":"ChEBI","id":"75466","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04560r004","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"183654","entry_name":null},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"9963917"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"136212542"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"75466","statements":[{"type":"Results","text":"To investigate the PAT domain boundaries and membrane interaction capabilities, we purified several C-terminal extended PAT domain constructs and the corresponding 11-mer repeats counterparts (Fig. 3c) and assessed the ability of these fragments to bind DO liposomes containing either 20 mol% PA or 20 mol% DAG."}],"entry_name":null}],"statement":[{"text":"Taken together, the data suggests that the PAT region does form a domain that spans residues 22–116 in PLIN3. Notably, this expanded PAT domain is capable of membrane binding and displays a preference for binding DAG enriched membranes, while the 11-mer repeats of PLIN3 do not.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a diacylglycerol, a diester of glycerol and two fatty acids.\" [GOC:ma]","term_is_obsolete":false,"term_not_annotate":false},{"start":1,"end":200,"reference_id":"37268630","reference_source":"pmid","reference_html":"Structural insights into perilipin 3 membrane association in response to diacylglycerol accumulation. <i> Choi YM, Ajjaji D, Fleming KD, Borbat PP, Jenkins ML, Moeller BE, Fernando S, Bhatia SR, Freed JH, Burke JE, Thiam AR, Airola MV. </i> Nat Commun, 2023","date":"2026-03-31T16:40:04.375Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04560r005","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"183654","entry_name":null},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"9963917"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"136212542"}],"statement":[{"text":"In contrast, the PAT/11-mer repeats adopted a mostly random coil structure in solution with a negative peak around 200 nm, and a shift to alpha helices in the presence of liposomes as indicated by a large negative peak at 222 nm. Liposomes induced similar changes in the CD spectra for both the PAT domain and 11-mer repeats alone. Taken together, this confirms that the increase in helicity observed in full-length PLIN3 by membranes was due to the PAT/11-mer repeats undergoing a disorder/alpha helical transition.","type":"Results"}]},{"start":22,"end":116,"reference_id":"37268630","reference_source":"pmid","reference_html":"Structural insights into perilipin 3 membrane association in response to diacylglycerol accumulation. <i> Choi YM, Ajjaji D, Fleming KD, Borbat PP, Jenkins ML, Moeller BE, Fernando S, Bhatia SR, Freed JH, Burke JE, Thiam AR, Airola MV. </i> Nat Commun, 2023","date":"2026-03-31T16:45:29.562Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006289","ec_ontology":"ECO","ec_name":"site-directed spin-labelling electron paramagnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04560r006","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"183654","entry_name":null},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"9963917"},{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"PubChem","id":"136212542"}],"statement":[{"text":"Taken together, we concluded that the PAT domain does form a folded domain when bound to membranes and this domain is likely mobile with a structure similar but not identical to the AlphaFold and RoseTTAFold predictions.","type":"Results"},{"text":"Membrane-induced conformational rearrangements are consistent with a PAT domain tertiary structure.","type":"Figure"}]}],"__v":0,"disorder_content":0.4608294930875576,"disprot_consensus":{"full":[{"start":1,"end":200,"type":"T"}],"Structural state":[{"start":1,"end":200,"type":"D"}],"Molecular function":[{"start":1,"end":200,"type":"F"}],"Structural transition":[{"start":1,"end":200,"type":"T"}]}},{"acc":"O60240","sequence":"MAVNKGLTLLDGDLPEQENVLQRVLQLPVVSGTCECFQKTYTSTKEAHPLVASVCNAYEKGVQSASSLAAWSMEPVVRRLSTQFTAANELACRGLDHLEEKIPALQYPPEKIASELKDTISTRLRSARNSISVPIASTSDKVLGAALAGCELAWGVARDTAEFAANTRAGRLASGGADLALGSIEKVVEYLLPPDKEESAPAPGHQQAQKSPKAKPSLLSRVGALTNTLSRYTVQTMARALEQGHTVAMWIPGVVPLSSLAQWGASVAMQAVSRRRSEVRVPWLHSLAAAQEEDHEDQTDTEGEDTEEEEELETEENKFSEVAALPGPRGLLGGVAHTLQKTLQTTISAVTWAPAAVLGMAGRVLHLTPAPAVSSTKGRAMSLSDALKGVTDNVVDTVVHYVPLPRLSLMEPESEFRDIDNPPAEVERREAERRASGAPSAGPEPAPRLAQPRRSLRSAQSPGAPPGPGLEDEVATPAAPRPGFPAVPREKPKRRVSDSFFRPSVMEPILGRTHYSQLRKKS","creator":"vnugnes","dataset":[],"date":"2026-03-31T17:01:10.527Z","disprot_id":"DP04561","features":{"pfam":[{"id":"PF03036","name":"Perilipin family","start":15,"end":413}]},"genes":[{"name":{"value":"PLIN1","_id":"69cbfdd657069de95ea674ad","evidences":[]},"synonyms":[{"value":"PERI","_id":"69cbfdd657069de95ea674ae","evidences":[]},{"value":"PLIN","_id":"69cbfdd657069de95ea674af","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"69cbfdd657069de95ea674ac"}],"length":522,"name":"Perilipin-1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":3,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":93,"end":192,"reference_id":"26742848","reference_source":"pmid","reference_html":"Conserved Amphipathic Helices Mediate Lipid Droplet Targeting of Perilipins 1-3. <i> Rowe ER, Mimmack ML, Barbosa AD, Haider A, Isaac I, Ouberai MM, Thiam AR, Patel S, Saudek V, Siniossoglou S, Savage DB. </i> J Biol Chem, 2016","date":"2026-03-31T17:05:52.313Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04561r001","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"131762","entry_name":null}],"statement":[{"text":" Analysis of the secondary structure of this purified peptide by circular dichroism spectroscopy suggested that both the WT′ and L143D′ mutant peptides were largely unstructured in solution (Fig. 11F). The addition of a membrane-mimicking detergent (LDAO) at a concentration above the critical micelle concentration resulted in a substantial increase in the helicity of the WT′ peptide (Fig. 11F), whereas the change in helicity of the L143D′ mutant peptide was considerably less than that of the WT′. Deconvolution of the CD spectra estimated that the WT′ peptide increased in helicity from 15 to 59% in the presence of LDAO, whereas the L143D′ mutant peptide had a limited increase in helicity from 16 to 23%.","type":"Results"}]},{"start":93,"end":192,"reference_id":"26742848","reference_source":"pmid","reference_html":"Conserved Amphipathic Helices Mediate Lipid Droplet Targeting of Perilipins 1-3. <i> Rowe ER, Mimmack ML, Barbosa AD, Haider A, Isaac I, Ouberai MM, Thiam AR, Patel S, Saudek V, Siniossoglou S, Savage DB. </i> J Biol Chem, 2016","date":"2026-03-31T17:07:32.406Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0005543","term_name":"phospholipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"EXP","region_id":"DP04561r002","sample":[{"term_id":"IDPO:00488","term_name":"interacting lipid","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"131762","entry_name":null}],"statement":[{"text":"Analysis of the secondary structure of this purified peptide by circular dichroism spectroscopy suggested that both the WT′ and L143D′ mutant peptides were largely unstructured in solution (Fig. 11F). The addition of a membrane-mimicking detergent (LDAO) at a concentration above the critical micelle concentration resulted in a substantial increase in the helicity of the WT′ peptide (Fig. 11F), whereas the change in helicity of the L143D′ mutant peptide was considerably less than that of the WT′. Deconvolution of the CD spectra estimated that the WT′ peptide increased in helicity from 15 to 59% in the presence of LDAO, whereas the L143D′ mutant peptide had a limited increase in helicity from 16 to 23%.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester.\" [ISBN:0198506732]","term_is_obsolete":false,"term_not_annotate":false},{"start":93,"end":192,"reference_id":"26742848","reference_source":"pmid","reference_html":"Conserved Amphipathic Helices Mediate Lipid Droplet Targeting of Perilipins 1-3. <i> Rowe ER, Mimmack ML, Barbosa AD, Haider A, Isaac I, Ouberai MM, Thiam AR, Patel S, Saudek V, Siniossoglou S, Savage DB. </i> J Biol Chem, 2016","date":"2026-03-31T17:13:42.195Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04561r003","statement":[{"text":"Analysis of the secondary structure of this purified peptide by circular dichroism spectroscopy suggested that both the WT′ and L143D′ mutant peptides were largely unstructured in solution (Fig. 11F).","type":"Results"}]}],"__v":0,"disorder_content":0.19157088122605365,"disprot_consensus":{"full":[{"start":93,"end":192,"type":"T"}],"Structural state":[{"start":93,"end":192,"type":"D"}],"Structural transition":[{"start":93,"end":192,"type":"T"}],"Molecular function":[{"start":93,"end":192,"type":"F"}]}},{"acc":"C8CHL5","sequence":"MGVFDRIRGALGRGLDVFRGDLPQVQPPAPQPAPAPAITPAAVQVGGWGFAWIDNEDFSPTGLAWRSGEYFALAQMKTPETAHFRIAAQERRLRIYLRGQKVVNGRNLSDPDSRTVNLPFLMQTPQGAPTLPSTYHPDVAVWAKVGSTWQPCVITAINYSTGDVTFTEPAGVTASDGIEIYYVHGDGQFRLRVARDAGGVDDSAATVFNQSFSTMHSVDQNNVETMIAWPQQVELVPGTRLVLEVFTTQVPMVWNERSGHYIQIAAMGRRIEVLDKGGLQRLAELEARGGL","creator":"bjuhasz","dataset":["Viral proteins"],"date":"2026-04-10T12:26:35.725Z","disprot_id":"DP04563","features":{"pfam":[{"id":"PF22210","name":"Large MCP VP17 central beta-barrel","start":103,"end":184}]},"genes":[],"length":291,"name":"VP17","ncbi_taxon_id":1714272,"organism":"Thermus virus P23-77","regions_counter":4,"released":"2026_06","taxonomy":["Viruses","Singelaviria","Helvetiavirae","Dividoviricota","Laserviricetes","Halopanivirales","Matsushitaviridae","Hukuchivirus","Hukuchivirus P2377"],"regions":[{"start":1,"end":42,"reference_id":"23623731","reference_source":"pmid","reference_html":"Bacteriophage P23-77 capsid protein structures reveal the archetype of an ancient branch from a major virus lineage. <i> Rissanen I, Grimes JM, Pawlowski A, Mäntynen S, Harlos K, Bamford JK, Stuart DI. </i> Structure, 2013","date":"2026-06-15T18:01:59.291Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"3ZMN"}],"region_id":"DP04563r001","statement":[{"text":"For monomeric VP17, 42 N-terminal and 18 C-terminal amino acids are disordered.","type":"Results"},{"text":"The crystal structure of VP17 has 42 undetermined amino acids at the N-terminus and 18 at the C-terminus, consistent with flexible domains stretching beneath the capsid shell.","type":"Supplementary material"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-15T18:07:16.437Z"}},{"start":274,"end":291,"reference_id":"23623731","reference_source":"pmid","reference_html":"Bacteriophage P23-77 capsid protein structures reveal the archetype of an ancient branch from a major virus lineage. <i> Rissanen I, Grimes JM, Pawlowski A, Mäntynen S, Harlos K, Bamford JK, Stuart DI. </i> Structure, 2013","date":"2026-06-15T18:01:46.628Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"3ZMN"}],"region_id":"DP04563r002","statement":[{"text":"For monomeric VP17, 42 N-terminal and 18 C-terminal amino acids are disordered.","type":"Results"},{"text":"The crystal structure of VP17 has 42 undetermined amino acids at the N-terminus and 18 at the C-terminus, consistent with flexible domains stretching beneath the capsid shell.","type":"Supplementary material"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-15T18:07:17.745Z"}},{"start":274,"end":291,"reference_id":"23623731","reference_source":"pmid","reference_html":"Bacteriophage P23-77 capsid protein structures reveal the archetype of an ancient branch from a major virus lineage. <i> Rissanen I, Grimes JM, Pawlowski A, Mäntynen S, Harlos K, Bamford JK, Stuart DI. </i> Structure, 2013","date":"2026-06-15T18:08:54.231Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":3,"region_id":"DP04563r003","statement":[{"text":"or monomeric VP17, 42 N-terminal and 18 C-terminal amino acids are disordered.","type":"Results"},{"text":"The crystal structure of VP17 has 42 undetermined amino acids at the N-terminus and 18 at the C-terminus, consistent with flexible domains stretching beneath the capsid shell.","type":"Supplementary material"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","cross_refs":[{"db":"PDB","id":"3ZMN"}]},{"start":1,"end":42,"reference_id":"23623731","reference_source":"pmid","reference_html":"Bacteriophage P23-77 capsid protein structures reveal the archetype of an ancient branch from a major virus lineage. <i> Rissanen I, Grimes JM, Pawlowski A, Mäntynen S, Harlos K, Bamford JK, Stuart DI. </i> Structure, 2013","date":"2026-06-15T18:09:02.365Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"region_id":"DP04563r004","statement":[{"text":"or monomeric VP17, 42 N-terminal and 18 C-terminal amino acids are disordered.","type":"Results"},{"text":"The crystal structure of VP17 has 42 undetermined amino acids at the N-terminus and 18 at the C-terminus, consistent with flexible domains stretching beneath the capsid shell.","type":"Supplementary material"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","cross_refs":[{"db":"PDB","id":"3ZMN"}]}],"__v":0,"disorder_content":0.20618556701030927,"disprot_consensus":{"full":[{"start":1,"end":42,"type":"D"},{"start":274,"end":291,"type":"D"}],"Structural state":[{"start":1,"end":42,"type":"D"},{"start":274,"end":291,"type":"D"}],"Disorder function":[{"start":1,"end":42,"type":"F"},{"start":274,"end":291,"type":"F"}]}},{"acc":"Q9BLZ2","sequence":"MGVKVLFALICIAVAEAKPTENNEDFNIVAVASNFATTDLDADRGKLPGKKLPLEVLKEMEANARKAGCTRGCLICLSHIKCTPKMKKFIPGRCHTYEGDKESAQGGIGEAIVDIPEIPGFKDLEPMEQFIAQVDLCVDCTTGCLKGLANVQCSDLLKKWLPQRCATFASKIQGQVDKIKGAGGD","creator":"bjuhasz","dataset":[],"date":"2026-04-10T14:48:51.964Z","disprot_id":"DP04564","features":{"pfam":[]},"genes":[],"length":185,"name":"Luciferase","ncbi_taxon_id":148582,"organism":"Gaussia princeps","regions_counter":5,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Crustacea","Multicrustacea","Hexanauplia","Copepoda","Calanoida","Metridinidae","Gaussia"],"regions":[{"start":163,"end":185,"reference_id":"33208800","reference_source":"pmid","reference_html":"Solution structure of Gaussia Luciferase with five disulfide bonds and identification of a putative coelenterazine binding cavity by heteronuclear NMR. <i> Wu N, Kobayashi N, Tsuda K, Unzai S, Saotome T, Kuroda Y, Yamazaki T. </i> Sci Rep, 2020","date":"2026-06-15T18:41:17.298Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"cross_refs":[{"db":"PDB","id":"7D2O"},{"db":"BMRB","id":"36385"}],"region_id":"DP04564r001","statement":[{"text":"The N- (residues 1–9) and C-terminus (residues 146–168) of GLuc are highly disordered (Fig. 2c). ","type":"Results"},{"text":"Because of the cleaved secretion tag the residue numbering in the paper is differing from the canonical UniProt sequence.","type":"Curator statement"},{"text":"A DNA sequence encoding the wild-type GLuc gene (UniProtKB ID: Q9BLZ2) without the 17 residues secretion tag and with an E100A and G103R mutations that increased protein expression was synthesized as reported previously13.","type":"Methods"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu117Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"A DNA sequence encoding the wild-type GLuc gene (UniProtKB ID: Q9BLZ2) without the 17 residues secretion tag and with an E100A and G103R mutations that increased protein expression was synthesized as reported previously."},{"type":"Curator statement","text":"Because of the cleaved secretion tag the residue numbering in the paper is differing from the canonical UniProt sequence.\n"}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly120Arg","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"A DNA sequence encoding the wild-type GLuc gene (UniProtKB ID: Q9BLZ2) without the 17 residues secretion tag and with an E100A and G103R mutations that increased protein expression was synthesized as reported previously.\n"},{"type":"Curator statement","text":"Because of the cleaved secretion tag the residue numbering in the paper is differing from the canonical UniProt sequence.\n"}]},{"term_id":"MI:0379","term_name":"13C label","term_namespace":"Labels and dyes","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"NMR experiments for resonance assignments and \n1\nH–\n15\nN heteronuclear NOE experiment were conducted using 0.2 mM \n15\nN single or \n15\nN, \n13\nC double labeled GLuc protein dissolved in 50 mM MES buffer pH 6.0 and 2 mM NaN\n3,\n at 293 K with 8%(v/v) D\n2\nO in a 5 mm Shigemi microtube (Shigemi co., Ltd, Tokyo, Japan). \n"}]},{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"NMR experiments for resonance assignments and \n1\nH–\n15\nN heteronuclear NOE experiment were conducted using 0.2 mM \n15\nN single or \n15\nN, \n13\nC double labeled GLuc protein dissolved in 50 mM MES buffer pH 6.0 and 2 mM NaN\n3,\n at 293 K with 8%(v/v) D\n2\nO in a 5 mm Shigemi microtube (Shigemi co., Ltd, Tokyo, Japan). \n"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-15T18:41:31.701Z"}},{"start":36,"end":51,"reference_id":"33208800","reference_source":"pmid","reference_html":"Solution structure of Gaussia Luciferase with five disulfide bonds and identification of a putative coelenterazine binding cavity by heteronuclear NMR. <i> Wu N, Kobayashi N, Tsuda K, Unzai S, Saotome T, Kuroda Y, Yamazaki T. </i> Sci Rep, 2020","date":"2026-06-15T18:41:29.305Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"cross_refs":[{"db":"PDB","id":"7D2O"},{"db":"BMRB","id":"36385"}],"region_id":"DP04564r002","statement":[{"text":"Residues 19–34 and 82–96 were highly disordered and can be considered as intrinsically disordered regions (IDR27, Figs. 2d, and 3).","type":"Results"},{"text":"Because of the cleaved secretion tag the residue numbering in the paper is differing from the canonical UniProt sequence.\n","type":"Curator statement"},{"text":"A DNA sequence encoding the wild-type GLuc gene (UniProtKB ID: Q9BLZ2) without the 17 residues secretion tag and with an E100A and G103R mutations that increased protein expression was synthesized as reported previously13.\n","type":"Methods"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu117Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"A DNA sequence encoding the wild-type GLuc gene (UniProtKB ID: Q9BLZ2) without the 17 residues secretion tag and with an E100A and G103R mutations that increased protein expression was synthesized as reported previously."},{"type":"Curator statement","text":"Because of the cleaved secretion tag the residue numbering in the paper is differing from the canonical UniProt sequence."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly120Arg","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"A DNA sequence encoding the wild-type GLuc gene (UniProtKB ID: Q9BLZ2) without the 17 residues secretion tag and with an E100A and G103R mutations that increased protein expression was synthesized as reported previously."},{"type":"Curator statement","text":"Because of the cleaved secretion tag the residue numbering in the paper is differing from the canonical UniProt sequence.\n"}]},{"term_id":"MI:0379","term_name":"13C label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"NMR experiments for resonance assignments and \n1\nH–\n15\nN heteronuclear NOE experiment were conducted using 0.2 mM \n15\nN single or \n15\nN, \n13\nC double labeled GLuc protein dissolved in 50 mM MES buffer pH 6.0 and 2 mM NaN\n3,\n at 293 K with 8%(v/v) D\n2\nO in a 5 mm Shigemi microtube (Shigemi co., Ltd, Tokyo, Japan). \n\nThe GLuc sequence was flanked with an N terminal His-tag and a C terminal SEP-tag (Solubility Enhancement Peptide tag, C9D) to facilitate protein expression, refolding, and purification.\n"}]},{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"NMR experiments for resonance assignments and \n1\nH–\n15\nN heteronuclear NOE experiment were conducted using 0.2 mM \n15\nN single or \n15\nN, \n13\nC double labeled GLuc protein dissolved in 50 mM MES buffer pH 6.0 and 2 mM NaN\n3,\n at 293 K with 8%(v/v) D\n2\nO in a 5 mm Shigemi microtube (Shigemi co., Ltd, Tokyo, Japan). \n\nThe GLuc sequence was flanked with an N terminal His-tag and a C terminal SEP-tag (Solubility Enhancement Peptide tag, C9D) to facilitate protein expression, refolding, and purification.\n"}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-15T18:41:32.717Z"}},{"start":99,"end":113,"reference_id":"33208800","reference_source":"pmid","reference_html":"Solution structure of Gaussia Luciferase with five disulfide bonds and identification of a putative coelenterazine binding cavity by heteronuclear NMR. <i> Wu N, Kobayashi N, Tsuda K, Unzai S, Saotome T, Kuroda Y, Yamazaki T. </i> Sci Rep, 2020","date":"2026-06-15T18:41:05.669Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":3,"cross_refs":[{"db":"PDB","id":"7D2O"},{"db":"BMRB","id":"36385"}],"region_id":"DP04564r003","statement":[{"text":"Residues 19–34 and 82–96 were highly disordered and can be considered as intrinsically disordered regions (IDR27, Figs. 2d, and 3).","type":"Results"},{"text":"Because of the cleaved secretion tag the residue numbering in the paper is differing from the canonical UniProt sequence.","type":"Curator statement"},{"text":"A DNA sequence encoding the wild-type GLuc gene (UniProtKB ID: Q9BLZ2) without the 17 residues secretion tag and with an E100A and G103R mutations that increased protein expression was synthesized as reported previously13.","type":"Methods"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu117Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"A DNA sequence encoding the wild-type GLuc gene (UniProtKB ID: Q9BLZ2) without the 17 residues secretion tag and with an E100A and G103R mutations that increased protein expression was synthesized as reported previously."},{"type":"Curator statement","text":"Because of the cleaved secretion tag the residue numbering in the paper is differing from the canonical UniProt sequence."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly120Arg","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"A DNA sequence encoding the wild-type GLuc gene (UniProtKB ID: Q9BLZ2) without the 17 residues secretion tag and with an E100A and G103R mutations that increased protein expression was synthesized as reported previously."},{"type":"Curator statement","text":"Because of the cleaved secretion tag the residue numbering in the paper is differing from the canonical UniProt sequence."}]},{"term_id":"MI:0379","term_name":"13C label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"NMR experiments for resonance assignments and 1H–15N heteronuclear NOE experiment were conducted using 0.2 mM 15N single or 15N, 13C double labeled GLuc protein dissolved in 50 mM MES buffer pH 6.0 and 2 mM NaN3, at 293 K with 8%(v/v) D2O in a 5 mm Shigemi microtube (Shigemi co., Ltd, Tokyo, Japan)."}]},{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"NMR experiments for resonance assignments and 1H–15N heteronuclear NOE experiment were conducted using 0.2 mM 15N single or 15N, 13C double labeled GLuc protein dissolved in 50 mM MES buffer pH 6.0 and 2 mM NaN3, at 293 K with 8%(v/v) D2O in a 5 mm Shigemi microtube (Shigemi co., Ltd, Tokyo, Japan)."}]}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-15T18:41:33.799Z"}},{"start":163,"end":185,"reference_id":"33208800","reference_source":"pmid","reference_html":"Solution structure of Gaussia Luciferase with five disulfide bonds and identification of a putative coelenterazine binding cavity by heteronuclear NMR. <i> Wu N, Kobayashi N, Tsuda K, Unzai S, Saotome T, Kuroda Y, Yamazaki T. </i> Sci Rep, 2020","date":"2026-06-15T18:40:47.524Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000031","term_name":"flexible C-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Gly120Arg","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Glu117Ala","start":null,"end":null,"position":null}],"cross_refs":[{"db":"BMRB","id":"36385"},{"db":"PDB","id":"7D2O"}],"region_id":"DP04564r005","statement":[{"text":"The N- (residues 1–9) and C-terminus (residues 146–168) of GLuc are highly disordered (Fig. 2c).","type":"Results"},{"text":"Author residue numbering has been mapped to the UniProt canonical sequence. The assessed peptide lacked the secretion tag and corresponds to the processed protein.","type":"Curator statement"}]}],"__v":0,"disorder_content":0.2918918918918919,"disprot_consensus":{"full":[{"start":36,"end":51,"type":"D"},{"start":99,"end":113,"type":"D"},{"start":163,"end":185,"type":"D"}],"Structural state":[{"start":36,"end":51,"type":"D"},{"start":99,"end":113,"type":"D"},{"start":163,"end":185,"type":"D"}],"Disorder function":[{"start":163,"end":185,"type":"F"}]}},{"acc":"Q9V1Z1","sequence":"MVIEMKKRMPATRLYIKDILEGYFVKSEGDFEPNYLITKYARKVYRAKIVGTVVREPLIAEDETYGKFQVDDGTGVIWVLGFRDDTKFAKLVRKGDLVQVIGKIAEWRDDKQILVEGVSKVHPNMWILHRYETLKEKIEHIKKAKIALEIYNQYGITAKSKVIAKNKGIEEELLEVIDELYGIMMEERSIEEPMEELLEEEIPEEKEENELLEKAKEDILNILRQKRTAISRKYILKKLGDKYDEETIDDAITELLAQGEIYEPETGYYKLL","creator":"bjuhasz","dataset":[],"date":"2026-04-17T11:40:42.332Z","disprot_id":"DP04565","features":{"pfam":[{"id":"PF01336","name":"OB-fold nucleic acid binding domain","start":49,"end":119}]},"genes":[{"synonyms":[],"olnNames":[{"value":"PAB2165","_id":"69e21c3acde2e6b639bd2544","evidences":[]}],"orfNames":[],"_id":"69e21c3acde2e6b639bd2543"}],"length":272,"name":"RPA32 subunit of the hetero-oligomeric complex involved in homologous recombination","ncbi_taxon_id":272844,"organism":"Pyrococcus abyssi (strain GE5 / Orsay)","regions_counter":1,"released":"2026_06","taxonomy":["Archaea","Methanobacteriati","Methanobacteriota","Thermococci","Thermococcales","Thermococcaceae","Pyrococcus"],"regions":[{"start":182,"end":205,"reference_id":"39738083","reference_source":"pmid","reference_html":"Communication between DNA polymerases and Replication Protein A within the archaeal replisome. <i> Martínez-Carranza M, Vialle L, Madru C, Cordier F, Tekpinar AD, Haouz A, Legrand P, Le Meur RA, England P, Dulermo R, Guijarro JI, Henneke G, Sauguet L. </i> Nat Commun, 2024","date":"2026-06-15T19:01:06.008Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"9F27"},{"db":"BMRB","id":"34913"}],"region_id":"DP04565r001","statement":[{"text":"In contrast, the N-terminal region (178–205) is essentially disordered as indicated by the lack of distance constraints that results in poor convergence of the structures (high backbone root mean square deviations) (colored in red in Fig. 2c).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-15T19:04:01.927Z"}}],"__v":0,"disorder_content":0.08823529411764706,"disprot_consensus":{"full":[{"start":182,"end":205,"type":"D"}],"Structural state":[{"start":182,"end":205,"type":"D"}]}},{"acc":"Q8CG76","sequence":"MLRAASRAVGRAAVRSAQRSGTSVGRPLAMSRPPPPRAASGAPLRPATVLGTMEMGRRMDASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGDCTVKIATKANPWEGKSLKPDSIRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTVYQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGNNWAETYRNRFWKEHHFEAIALVEKALQTTYGTNAPRMTSAALRWMYHHSQLQGTRGDAVILGMSSLEQLEQNLAATEEGPLEPAVVEAFDQAWNMVAHECPNYFR","creator":"bjuhasz","dataset":[],"date":"2026-04-23T09:35:37.850Z","disprot_id":"DP04566","features":{"pfam":[{"id":"PF00248","name":"Aldo/keto reductase family","start":49,"end":355}]},"genes":[{"name":{"value":"Akr7a2","evidences":[{"source":{"id":"O43488","name":"UniProtKB","url":"https://www.uniprot.org/uniprot/O43488","_id":"69e9e7e9cde2e6b639bd261a"},"code":"ECO:0000250","_id":"69e9e7e9cde2e6b639bd2619"}],"_id":"69e9e7e9cde2e6b639bd2618"},"synonyms":[{"value":"Afar","_id":"69e9e7e9cde2e6b639bd261b","evidences":[]},{"value":"Akr7a5","_id":"69e9e7e9cde2e6b639bd261c","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"69e9e7e9cde2e6b639bd2617"}],"length":367,"name":"Aflatoxin B1 aldehyde reductase member 2","ncbi_taxon_id":10090,"organism":"Mus musculus","regions_counter":1,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"regions":[{"start":30,"end":43,"reference_id":"16460003","reference_source":"pmid","reference_html":"Crystal structure of mouse succinic semialdehyde reductase AKR7A5: structural basis for substrate specificity. <i> Zhu X, Lapthorn AJ, Ellis EM. </i> Biochemistry, 2006","date":"2026-06-15T21:53:29.702Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Results","text":"The N-terminus of AKR7A5 is disordered in the structure and not visible in the electron density; this includes the polyhistidine tag and the first 14 amino acid residues of the native protein (MSRPPPPRAASGAP)."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Arg162Cys","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"2C91"}],"region_id":"DP04566r001","statement":[{"text":"The N-terminus of AKR7A5 is disordered in the structure and not visible in the electron density; this includes the polyhistidine tag and the first 14 amino acid residues of the native protein (MSRPPPPRAASGAP).","type":"Results"},{"text":"The given N-terminal sequence refers to residues 30-43 in the canonical sequence.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"44409","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"15671","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17754","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"35780","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"39005","entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-15T21:53:32.760Z"}}],"__v":0,"disorder_content":0.03814713896457766,"disprot_consensus":{"full":[{"start":30,"end":43,"type":"D"}],"Structural state":[{"start":30,"end":43,"type":"D"}]}},{"acc":"P22813","sequence":"MSRSRSSAKAVQFKHESEEEEEDEEEQLPSRRMHSYGDAAAIGSGVPAFLAKLWRLVDDADTNRLICWTKDGQSFVIQNQAQFAKELLPLNYKHNNMASFIRQLNMYGFHKITSIDNGGLRFDRDEIEFSHPFFKRNSPFLLDQIKRKISNNKNGDDKGVLKPEAMSKILTDVKVMRGRQDNLDSRFSAMKQENEVLWREIASLRQKHAKQQQIVNKLIQFLITIVQPSRNMSGVKRHVQLMINNTPEIDRARTTSETESESGGGPVIHELREELLDEVMNPSPAGYTAASHYDQESVSPPAVERPRSNMSISSHNVDYSNQSVEDLLLQGNGTAGGNILVGGAASPMAQSVSQSPAQHDVYTVTEAPDSHVQEVPNSPPYYEEQNVLTTPMVREQEQQKRQQLKENNKLRRQAGDVILDAGDILVDSSSPKAQRTSIQHSTQPDVMVQPMIIKSEPENSSGLMDLMTPANDLYSVNFISEDMPTDIFEDALLPDGVEEAAKLDQQQKFGQSTVSSGKFASNFDVPTNSTLLDANQASTSKAAAKAQASEEEGMAVAKYSGAENGNNRDTNNSQLLRMASVDELHGHLESMQDELETLKDLLRGDGVAIDQNMLMGLFNDSDLMDNYGLSFPNDSISSEKKAPSGSELISYQPMYDLSDILDTDDGNNDQEASRRQMQTQSSVLNTPRHEL","creator":"bjuhasz","dataset":["Stress response proteins"],"date":"2026-04-23T10:24:12.918Z","disprot_id":"DP04567","features":{"pfam":[{"id":"PF00447","name":"HSF-type DNA-binding","start":49,"end":148},{"id":"PF06546","name":"Vertebrate heat shock transcription factor","start":530,"end":633}]},"genes":[{"name":{"value":"Hsf","_id":"69e9f34dcde2e6b639bd2626","evidences":[]},"synonyms":[],"olnNames":[],"orfNames":[{"value":"CG5748","_id":"69e9f34dcde2e6b639bd2627","evidences":[]}],"_id":"69e9f34dcde2e6b639bd2625"}],"length":691,"name":"Heat shock factor protein","ncbi_taxon_id":7227,"organism":"Drosophila melanogaster","regions_counter":3,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"regions":[{"start":33,"end":45,"reference_id":"8286326","reference_source":"pmid","reference_html":"NMR evidence for similarities between the DNA-binding regions of Drosophila melanogaster heat shock factor and the helix-turn-helix and HNF-3/forkhead families of transcription factors. <i> Vuister GW, Kim SJ, Wu C, Bax A. </i> Biochemistry, 1994","date":"2026-04-23T10:32:41.544Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04567r001","statement":[{"text":"The amides of residues Met33-Gly45,Thrl 13-Arg124,and\nArg147-G1~166\nall exhibit fast amide hydrogen exchange and\nhave low values for the 15N-{'H} heteronuclear NOE. This\nis indicative of a high degree bf internal mobility and non-\nhydrogen-bonded amide protons. Moreover, Ha, Ca, and Cb\nresonances of these residues all resonate close to their random\ncoil values, which is further evidence of extensive conformational averaging.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-16T14:20:24.464Z"}},{"start":113,"end":124,"reference_id":"8286326","reference_source":"pmid","reference_html":"NMR evidence for similarities between the DNA-binding regions of Drosophila melanogaster heat shock factor and the helix-turn-helix and HNF-3/forkhead families of transcription factors. <i> Vuister GW, Kim SJ, Wu C, Bax A. </i> Biochemistry, 1994","date":"2026-04-23T10:33:26.662Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04567r002","statement":[{"text":"The amides of residues Met33-Gly45,Thrl 13-Arg124,and\nArg147-G1~166\nall exhibit fast amide hydrogen exchange and\nhave low values for the 15N-{'H} heteronuclear NOE. This\nis indicative of a high degree bf internal mobility and non-\nhydrogen-bonded amide protons. Moreover, Ha, Ca, and Cb\nresonances of these residues all resonate close to their random\ncoil values, which is further evidence of extensive conformational averaging.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-16T14:20:26.182Z"}},{"start":147,"end":164,"reference_id":"8286326","reference_source":"pmid","reference_html":"NMR evidence for similarities between the DNA-binding regions of Drosophila melanogaster heat shock factor and the helix-turn-helix and HNF-3/forkhead families of transcription factors. <i> Vuister GW, Kim SJ, Wu C, Bax A. </i> Biochemistry, 1994","date":"2026-06-16T14:19:36.488Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04567r003","statement":[{"text":"The amides of residues Met33-Gly45,Thrl 13-Arg124,and\nArg147-G1~166\nall exhibit fast amide hydrogen exchange and\nhave low values for the 15N-{'H} heteronuclear NOE. This\nis indicative of a high degree bf internal mobility and non-\nhydrogen-bonded amide protons. Moreover, Ha, Ca, and Cb\nresonances of these residues all resonate close to their random\ncoil values, which is further evidence of extensive conformational averaging.","type":"Results"},{"text":"Residues 164-166 are vector-derived (Ala-Ala-Glu from pJC20).","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-16T14:19:52.024Z"}}],"__v":0,"disorder_content":0.06222865412445731,"disprot_consensus":{"full":[{"start":33,"end":45,"type":"D"},{"start":113,"end":124,"type":"D"},{"start":147,"end":164,"type":"D"}],"Structural state":[{"start":33,"end":45,"type":"D"},{"start":113,"end":124,"type":"D"},{"start":147,"end":164,"type":"D"}]}},{"acc":"P11716","sequence":"MGDGGEGEDEVQFLRTDDEVVLQCSATVLKEQLKLCLAAEGFGNRLCFLEPTSNAQNVPPDLAICCFTLEQSLSVRALQEMLANTVEAGVESSQGGGHRTLLYGHAILLRHAHSRMYLSCLTTSRSMTDKLAFDVGLQEDATGEACWWTMHPASKQRSEGEKVRVGDDLILVSVSSERYLHLSTASGELQVDASFMQTLWNMNPICSCCEEGYVTGGHVLRLFHGHMDECLTISAADSDDQRRLVYYEGGAVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVTTGRYLALTEDQGLVVVDACKAHTKATSFCFRVSKEKLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKALRLGVLKKKAILHQEGHMDDALFLTRCQQEESQAARMIHSTAGLYNQFIKGLDSFSGKPRGSGPPAGPALPIEAVILSLQDLIGYFEPPSEELQHEEKQSKLRSLRNRQSLFQEEGMLSLVLNCIDRLNVYTTAAHFAEYAGEEAAESWKEIVNLLYELLASLIRGNRANCALFSTNLDWVVSKLDRLEASSGILEVLYCVLIESPEVLNIIQENHIKSIISLLDKHGRNHKVLDVLCSLCVCNGVAVRSNQDLITENLLPGRELLLQTNLINYVTSIRPNIFVGRAEGSTQYGKWYFEVMVDEVVPFLTAQATHLRVGWALTEGYSPYPGGGEGWGGNGVGDDLYSYGFDGLHLWTGHVARPVTSPGQHLLAPEDVVSCCLDLSVPSISFRINGCPVQGVFEAFNLDGLFFPVVSFSAGVKVRFLLGGRHGEFKFLPPPGYAPCHEAVLPRERLRLEPIKEYRREGPRGPHLVGPSRCLSHTDFVPCPVDTVQIVLPPHLERIREKLAENIHELWALTRIEQGWTYGPVRDDNKRLHPCLVNFHSLPEPERNYNLQMSGETLKTLLALGCHVGMADEKAEDNLKKTKLPKTYMMSNGYKPAPLDLSHVRLTPAQTTLVDRLAENGHNVWARDRVAQGWSYSAVQDIPARRNPRLVPYRLLDEATKRSNRDSLCQAVRTLLGYGYNIEPPDQEPSQVENQSRWDRVRIFRAEKSYTVQSGRWYFEFEAVTTGEMRVGWARPELRPDVELGADELAYVFNGHRGQRWHLGSEPFGRPWQSGDVVGCMIDLTENTIIFTLNGEVLMSDSGSETAFREIEIGDGFLPVCSLGPGQVGHLNLGQDVSSLRFFAICGLQEGFEPFAINMQRPVTTWFSKSLPQFEPVPPEHPHYEVARMDGTVDTPPCLRLAHRTWGSQNSLVEMLFLRLSLPVQFHQHFRCTAGATPLAPPGLQPPAEDEARAAEPDPDYENLRRSAGGWGEAEGGKEGTAKEGTPGGTPQPGVEAQPVRAENEKDATTEKNKKRGFLFKAKKAAMMTQPPATPALPRLPHDVVPADNRDDPEIILNTTTYYYSVRVFAGQEPSCVWVGWVTPDYHQHDMNFDLSKVRAVTVTMGDEQGNVHSSLKCSNCYMVWGGDFVSPGQQGRISHTDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNTKLFPAVFVLPTHQNVIQFELGKQKNIMPLSAAMFLSERKNPAPQCPPRLEVQMLMPVSWSRMPNHFLQVETRRAGERLGWAVQCQDPLTMMALHIPEENRCMDILELSERLDLQRFHSHTLRLYRAVCALGNNRVAHALCSHVDQAQLLHALEDAHLPGPLRAGYYDLLISIHLESACRSRRSMLSEYIVPLTPETRAITLFPPGRKGGNARRHGLPGVGVTTSLRPPHHFSPPCFVAALPAAGVAEAPARLSPAIPLEALRDKALRMLGEAVRDGGQHARDPVGGSVEFQFVPVLKLVSTLLVMGIFGDEDVKQILKMIEPEVFTEEEEEEEEEEEEEEEEEEDEEEKEEDEEEEEKEDAEKEEEEAPEGEKEDLEEGLLQMKLPESVKLQMCNLLEYFCDQELQHRVESLAAFAERYVDKLQANQRSRYALLMRAFTMSAAETARRTREFRSPPQEQINMLLHFKDEADEEDCPLPEDIRQDLQDFHQDLLAHCGIQLEGEEEEPEEETSLSSRLRSLLETVRLVKKKEEKPEEELPAEEKKPQSLQELVSHMVVRWAQEDYVQSPELVRAMFSLLHRQYDGLGELLRALPRAYTISPSSVEDTMSLLECLGQIRSLLIVQMGPQEENLMIQSIGNIMNNKVFYQHPNLMRALGMHETVMEVMVNVLGGGETKEIRFPKMVTSCCRFLCYFCRISRQNQRSMFDHLSYLLENSGIGLGMQGSTPLDVAAASVIDNNELALALQEQDLEKVVSYLAGCGLQSCPMLLAKGYPDIGWNPCGGERYLDFLRFAVFVNGESVEENANVVVRLLIRKPECFGPALRGEGGSGLLAAIEEAIRISEDPARDGPGVRRDRRREHFGEEPPEENRVHLGHAIMSFYAALIDLLGRCAPEMHLIQAGKGEALRIRAILRSLVPLDDLVGIISLPLQIPTLGKDGALVQPKMSASFVPDHKASMVLFLDRVYGIENQDFLLHVLDVGFLPDMRAAASLDTATFSTTEMALALNRYLCLAVLPLITKCAPLFAGTEHRAIMVDSMLHTVYRLSRGRSLTKAQRDVIEDCLMALCRYIRPSMLQHLLRRLVFDVPILNEFAKMPLKLLTNHYERCWKYYCLPTGWANFGVTSEEELHLTRKLFWGIFDSLAHKKYDQELYRMAMPCLCAIAGALPPDYVDASYSSKAEKKATVDAEGNFDPRPVETLNVIIPEKLDSFINKFAEYTHEKWAFDKIQNNWSYGENVDEELKTHPMLRPYKTFSEKDKEIYRWPIKESLKAMIAWEWTIEKAREGEEERTEKKKTRKISQTAQTYDPREGYNPQPPDLSGVTLSRELQAMAEQLAENYHNTWGRKKKQELEAKGGGTHPLLVPYDTLTAKEKARDREKAQELLKFLQMNGYAVTRGLKDMELDTSSIEKRFAFGFLQQLLRWMDISQEFIAHLEAVVSSGRVEKSPHEQEIKFFAKILLPLINQYFTNHCLYFLSTPAKVLGSGGHASNKEKEMITSLFCKLAALVRHRVSLFGTDAPAVVNCLHILARSLDARTVMKSGPEIVKAGLRSFFESASEDIEKMVENLRLGKVSQARTQVKGVGQNLTYTTVALLPVLTTLFQHIAQHQFGDDVILDDVQVSCYRTLCSIYSLGTTKNTYVEKLRPALGECLARLAAAMPVAFLEPQLNEYNACSVYTTKSPRERAILGLPNSVEEMCPDIPVLDRLMADIGGLAESGARYTEMPHVIEITLPMLCSYLPRWWERGPEAPPPALPAGAPPPCTAVTSDHLNSLLGNILRIIVNNLGIDEATWMKRLAVFAQPIVSRARPELLHSHFIPTIGRLRKRAGKVVAEEEQLRLEAKAEAEEGELLVRDEFSVLCRDLYALYPLLIRYVDNNRAHWLTEPNANAEELFRMVGEIFIYWSKSHNFKREEQNFVVQNEINNMSFLTADSKSKMAKAGDAQSGGSDQERTKKKRRGDRYSVQTSLIVATLKKMLPIGLNMCAPTDQDLIMLAKTRYALKDTDEEVREFLQNNLHLQGKVEGSPSLRWQMALYRGLPGREEDADDPEKIVRRVQEVSAVLYHLEQTEHPYKSKKAVWHKLLSKQRRRAVVACFRMTPLYNLPTHRACNMFLESYKAAWILTEDHSFEDRMIDDLSKAGEQEEEEEEVEEKKPDPLHQLVLHFSRTALTEKSKLDEDYLYMAYADIMAKSCHLEEGGENGEAEEEEVEVSFEEKEMEKQRLLYQQSRLHTRGAAEMVLQMISACKGETGAMVSSTLKLGISILNGGNAEVQQKMLDYLKDKKEVGFFQSIQALMQTCSVLDLNAFERQNKAEGLGMVNEDGTVINRQNGEKVMADDEFTQDLFRFLQLLCEGHNNDFQNYLRTQTGNTTTINIIICTVDYLLRLQESISDFYWYYSGKDVIEEQGKRNFSKAMSVAKQVFNSLTEYIQGPCTGNQQSLAHSRLWDAVVGFLHVFAHMMMKLAQDSSQIELLKELLDLQKDMVVMLLSLLEGNVVNGMIARQMVDMLVESSSNVEMILKFFDMFLKLKDIVGSEAFQDYVTDPRGLISKKDFQKAMDSQKQFTGPEIQFLLSCSEADENEMINFEEFANRFQEPARDIGFNVAVLLTNLSEHVPHDPRLRNFLELAESILEYFRPYLGRIEIMGASRRIERIYFEISETNRAQWEMPQVKESKRQFIFDVVNEGGEAEKMELFVSFCEDTIFEMQIAAQISEPEGEPEADEDEGMGEAAAEGAEEGAAGAEGAAGTVAAGATARLAAAAARALRGLSYRSLRRRVRRLRRLTAREAATALAALLWAVVARAGAAGAGAAAGALRLLWGSLFGGGLVEGAKKVTVTELLAGMPDPTSDEVHGEQPAGPGGDADGAGEGEGEGDAAEGDGDEEVAGHEAGPGGAEGVVAVADGGPFRPEGAGGLGDMGDTTPAEPPTPEGSPILKRKLGVDGEEEELVPEPEPEPEPEPEKADEENGEKEEVPEAPPEPPKKAPPSPPAKKEEAGGAGMEFWGELEVQRVKFLNYLSRNFYTLRFLALFLAFAINFILLFYKVSDSPPGEDDMEGSAAGDLAGAGSGGGSGWGSGAGEEAEGDEDENMVYYFLEESTGYMEPALWCLSLLHTLVAFLCIIGYNCLKVPLVIFKREKELARKLEFDGLYITEQPGDDDVKGQWDRLVLNTPSFPSNYWDKFVKRKVLDKHGDIFGRERIAELLGMDLASLEITAHNERKPDPPPGLLTWLMSIDVKYQIWKFGVIFTDNSFLYLGWYMVMSLLGHYNNFFFAAHLLDIAMGVKTLRTILSSVTHNGKQLVMTVGLLAVVVYLYTVVAFNFFRKFYNKSEDEDEPDMKCDDMMTCYLFHMYVGVRAGGGIGDEIEDPAGDEYELYRVVFDITFFFFVIVILLAIIQGLIIDAFGELRDQQEQVKEDMETKCFICGIGSDYFDTTPHGFETHTLEEHNLANYMFFLMYLINKDETEHTGQESYVWKMYQERCWDFFPAGDCFRKQYEDQLS","creator":"bjuhasz","dataset":[],"date":"2026-04-24T14:59:16.194Z","disprot_id":"DP04568","features":{"pfam":[{"id":"PF00520","name":"Ion transport protein","start":4789,"end":4947},{"id":"PF00622","name":"SPRY domain","start":661,"end":795},{"id":"PF00622","name":"SPRY domain","start":1087,"end":1206},{"id":"PF00622","name":"SPRY domain","start":1433,"end":1569},{"id":"PF01365","name":"RIH domain","start":444,"end":637},{"id":"PF01365","name":"RIH domain","start":2160,"end":2368},{"id":"PF02026","name":"RyR domain","start":851,"end":940},{"id":"PF02026","name":"RyR domain","start":965,"end":1054},{"id":"PF02026","name":"RyR domain","start":2735,"end":2825},{"id":"PF02026","name":"RyR domain","start":2855,"end":2939},{"id":"PF02815","name":"MIR domain","start":212,"end":390},{"id":"PF06459","name":"Ryanodine Receptor TM 4-6","start":4382,"end":4670},{"id":"PF08454","name":"RyR and IP3R Homology associated","start":3877,"end":3992},{"id":"PF08709","name":"Inositol 1,4,5-trisphosphate/ryanodine receptor","start":10,"end":210},{"id":"PF21119","name":"Ryanodine receptor junctional solenoid repeat","start":1663,"end":2126}]},"genes":[{"name":{"value":"RYR1","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/10601232","id":"10601232","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/10601232","_id":"69eb8544cde2e6b639bd2674"},"code":"ECO:0000303","_id":"69eb8544cde2e6b639bd2673"}],"_id":"69eb8544cde2e6b639bd2672"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"69eb8544cde2e6b639bd2671"}],"length":5037,"name":"Ryanodine receptor 1","ncbi_taxon_id":9986,"organism":"Oryctolagus cuniculus","regions_counter":2,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Lagomorpha","Leporidae","Oryctolagus"],"regions":[{"start":2830,"end":2849,"reference_id":"22913516","reference_source":"pmid","reference_html":"Structural determination of the phosphorylation domain of the ryanodine receptor. <i> Sharma P, Ishiyama N, Nair U, Li W, Dong A, Miyake T, Wilson A, Ryan T, MacLennan DH, Kislinger T, Ikura M, Dhe-Paganon S, Gramolini AO. </i> FEBS J, 2012","date":"2026-06-19T13:30:44.707Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":"0009-0009-6028-6956","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"3RQR"}],"region_id":"DP04568r001","statement":[{"text":"Observed was weak electron density for the backbone of about five residues of the 19-residue linker, and these unlabeled residues were included in the final model. The observation that the phosphorylated residue was within a 19-residue (2830-2849) flexible linker supported the notion that the residue is a physiologically relevant phosphorylatable site. ","type":"Results"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Methods","text":"The protein was purified by the Streamline purification method using His-link resin from Promega as described previously [48]."},{"type":"Curator statement","text":"The RyR1 C3 construct was cloned into pET28a-LIC and purified using His-link resin; therefore, the crystallized construct likely contained an uncleaved N-terminal 6×His-tag-containing fusion sequence."}]}],"last_modified_by":"bjuhasz","last_modified_name":"Bernadett Juhász","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-22T16:36:00.574Z"}}],"__v":0,"disorder_content":0.0039706174310105225,"disprot_consensus":{"full":[{"start":2830,"end":2849,"type":"D"}],"Structural state":[{"start":2830,"end":2849,"type":"D"}]}},{"acc":"Q9SRX6","sequence":"MARSLANAKIQSVFGSEKLSNAVFRRGFAAAAKTALDGSVSTAEMKKRAGEASSEKAPWVPDPKTGYYRPETVSEEIDPAELRAILLNNKQ","creator":"grivas","dataset":["Stress response proteins"],"date":"2026-04-28T11:31:04.228Z","disprot_id":"DP04569","features":{"pfam":[{"id":"PF03242","name":"Late embryogenesis abundant protein (LEA_3a subfamily)","start":1,"end":91}]},"genes":[{"name":{"value":"LEA2","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/25005920","id":"25005920","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/25005920","_id":"69f09a79cde2e6b639bd273b"},"code":"ECO:0000303","_id":"69f09a79cde2e6b639bd273a"}],"_id":"69f09a79cde2e6b639bd2739"},"synonyms":[{"value":"AtLEA3","_id":"69f09a79cde2e6b639bd273c","evidences":[]}],"olnNames":[{"value":"At1g02820","_id":"69f09a79cde2e6b639bd273d","evidences":[]}],"orfNames":[{"value":"F22D16.18","_id":"69f09a79cde2e6b639bd273e","evidences":[]}],"_id":"69f09a79cde2e6b639bd2738"}],"length":91,"name":"Late embryogenis abundant protein 2","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions_counter":2,"released":"2026_06","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"regions":[{"start":29,"end":91,"reference_id":"33474748","reference_source":"pmid","reference_html":"The in vitro structure and functions of the disordered late embryogenesis abundant three proteins. <i> Singh KK, Graether SP. </i> Protein Sci, 2021","date":"2026-06-18T15:09:45.895Z","curator_id":"grivas","curator_name":"Gabriel Alejandro Rivas","curator_orcid":"0000-0001-9987-3159","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04569r001","statement":[{"text":"Note that studies have shown that AtLEA3‐3 does not locate to the mitochondrion, but is found in the cytoplasm and the nucleus.37,44 However, the full‐length AtLEA3‐3 protein could not be expressed in soluble form for biochemical characterization (data not shown), so we therefore truncated the AtLEA3‐3 gene at the position equivalent to residue 29, although this MTS cleavage site may not be cut in vivo.","type":"Results"},{"text":"The results show that all four proteins possess similar CD spectra; a large negative minimum ellipticity is observed at ~200 nm, and a small negative signal is seen after 212 nm (Figure 1(c)), suggesting that these proteins are largely disordered when alone in solution.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sequence_construct":"AAAAKTALDGSVSTAEMKKRAGEASSEKAPWVPDPKTGYYRPETVSEEIDPAELRAILLNNKQ","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T15:10:05.364Z"}},{"start":29,"end":91,"reference_id":"33474748","reference_source":"pmid","reference_html":"The in vitro structure and functions of the disordered late embryogenesis abundant three proteins. <i> Singh KK, Graether SP. </i> Protein Sci, 2021","date":"2026-06-08T11:30:15.684Z","curator_id":"grivas","curator_name":"Gabriel Alejandro Rivas","curator_orcid":"0000-0001-9987-3159","term_id":"GO:0009631","term_name":"cold acclimation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IDA","region_id":"DP04569r002","statement":[{"text":"It has previously been shown that multiple freeze–thaw cycles can reduce LDH activity to essentially zero,52 and that LEA proteins from several different groups can protect the enzyme from losing activity.22,53","type":"Results"},{"text":"Since LEA3 proteins have not been previously tested, and expression data has shown that AtLEA3-1 and AtLEA3-2 proteins are upregulated in response to cold stress,39,54 we examined the protective effects of the four AtLEA3 proteins on freeze–thaw damaged LDH.","type":"Results"},{"text":"For all proteins studied here, AtLEA3-1 (91 μg/ml) and AtLEA3-4 (92 μg/ml) had relatively similar PD50 values, with AtLEA3-2 (79 μg/ml) being slightly more efficient and AtLEA3-3 (58 μg/ml) being the most efficient of the group.","type":"Discussion"}],"term_comment":"","term_def":"\"Any process that increases freezing tolerance of an organism in response to low, nonfreezing temperatures.\" [GOC:syr]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"grivas","last_modified_name":"Gabriel Alejandro Rivas","sequence_construct":"AAAAKTALDGSVSTAEMKKRAGEASSEKAPWVPDPKTGYYRPETVSEEIDPAELRAILLNNKQ","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T15:11:17.177Z"}}],"__v":0,"disorder_content":0.6923076923076923,"disprot_consensus":{"full":[{"start":29,"end":91,"type":"D"}],"Structural state":[{"start":29,"end":91,"type":"D"}],"Biological process":[{"start":29,"end":91,"type":"F"}]}},{"acc":"Q93WF6","sequence":"MARSISNVKIVSAFVSRELSNAIFRRGYAATAAQGSVSSGGRSGAVASAVMKKKGVEESTQKISWVPDPKTGYYRPETGSNEIDAAELRAALLNNKQ","creator":"grivas","dataset":["Stress response proteins"],"date":"2026-04-28T12:19:59.348Z","disprot_id":"DP04570","features":{"pfam":[{"id":"PF03242","name":"Late embryogenesis abundant protein (LEA_3a subfamily)","start":1,"end":97}]},"genes":[{"name":{"value":"SAG21","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/9617813","id":"9617813","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/9617813","_id":"69f0a5efcde2e6b639bd275d"},"code":"ECO:0000303","_id":"69f0a5efcde2e6b639bd275c"}],"_id":"69f0a5efcde2e6b639bd275b"},"synonyms":[{"value":"LEA38","_id":"69f0a5efcde2e6b639bd275e","evidences":[]},{"value":"LEA5","_id":"69f0a5efcde2e6b639bd275f","evidences":[]}],"olnNames":[{"value":"At4g02380","_id":"69f0a5efcde2e6b639bd2760","evidences":[]}],"orfNames":[{"value":"T14P8.2","_id":"69f0a5efcde2e6b639bd2761","evidences":[]}],"_id":"69f0a5efcde2e6b639bd275a"}],"length":97,"name":"Protein SENESCENCE-ASSOCIATED GENE 21, mitochondrial","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions_counter":2,"released":"2026_06","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"regions":[{"start":29,"end":97,"reference_id":"33474748","reference_source":"pmid","reference_html":"The in vitro structure and functions of the disordered late embryogenesis abundant three proteins. <i> Singh KK, Graether SP. </i> Protein Sci, 2021","date":"2026-06-08T11:40:25.042Z","curator_id":"grivas","curator_name":"Gabriel Alejandro Rivas","curator_orcid":"0000-0001-9987-3159","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04570r001","statement":[{"text":"The results show that all four proteins possess similar CD spectra; a large negative minimum ellipticity is observed at ~200 nm, and a small negative signal is seen after 212 nm (Figure 1(c)), suggesting that these proteins are largely disordered when alone in solution.","type":"Results"},{"text":"We therefore expressed the mature form of the protein, where sequence before the predicted cut-site (Figure 1(a), black triangles) were removed from the corresponding DNA sequence, which resulted in soluble protein expression.","type":"Results"}],"last_modified_by":"grivas","last_modified_name":"Gabriel Alejandro Rivas","sequence_construct":"AATAAQGSVSSGGRSGAVASAVMKKKGVEESTQKISWVPDPKTGYYRPETGSNEIDAAELRAALLNNKQ","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T15:25:32.215Z"}},{"start":29,"end":97,"reference_id":"33474748","reference_source":"pmid","reference_html":"The in vitro structure and functions of the disordered late embryogenesis abundant three proteins. <i> Singh KK, Graether SP. </i> Protein Sci, 2021","date":"2026-06-08T12:04:35.706Z","curator_id":"grivas","curator_name":"Gabriel Alejandro Rivas","curator_orcid":"0000-0001-9987-3159","term_id":"GO:0009631","term_name":"cold acclimation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IDA","region_id":"DP04570r002","statement":[{"text":"For all biochemical and structural experiments presented here, we used the mature form of the AtLEA3 proteins.","type":"Results"},{"text":"It has previously been shown that multiple freeze–thaw cycles can reduce LDH activity to essentially zero,52 and that LEA proteins from several different groups can protect the enzyme from losing activity.22,53","type":"Results"},{"text":"Since LEA3 proteins have not been previously tested, and expression data has shown that AtLEA3‐1 and AtLEA3‐2 proteins are upregulated in response to cold stress,39,54 we examined the protective effects of the four AtLEA3 proteins on freeze–thaw damaged LDH.","type":"Results"},{"text":"For all proteins studied here, AtLEA3‐1 (91 μg/ml) and AtLEA3‐4 (92 μg/ml) had relatively similar PD50 values, with AtLEA3‐2 (79 μg/ml) being slightly more efficient and AtLEA3‐3 (58 μg/ml) being the most efficient of the group.","type":"Discussion"}],"term_comment":"","term_def":"\"Any process that increases freezing tolerance of an organism in response to low, nonfreezing temperatures.\" [GOC:syr]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"grivas","last_modified_name":"Gabriel Alejandro Rivas","sequence_construct":"AATAAQGSVSSGGRSGAVASAVMKKKGVEESTQKISWVPDPKTGYYRPETGSNEIDAAELRAALLNNKQ","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T15:22:59.611Z"}}],"__v":0,"disorder_content":0.711340206185567,"disprot_consensus":{"full":[{"start":29,"end":97,"type":"D"}],"Structural state":[{"start":29,"end":97,"type":"D"}],"Biological process":[{"start":29,"end":97,"type":"F"}]}},{"acc":"Q39084","sequence":"MAARSLSGAVKSLCSAASGSLSCSIVLRRSYVATSQNVTAAGLSKGGSTRVMVGKMEQRGLDQEAESAWGPDPVTGYYRPSNRAAEIDPAELRELLLKNKAKSF","creator":"grivas","dataset":[],"date":"2026-04-29T08:33:05.785Z","disprot_id":"DP04571","features":{"pfam":[{"id":"PF03242","name":"Late embryogenesis abundant protein (LEA_3a subfamily)","start":2,"end":100}]},"genes":[{"name":{"value":"LEA41","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/25005920","id":"25005920","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/25005920","_id":"69f1c241cde2e6b639bd27a7"},"code":"ECO:0000303","_id":"69f1c241cde2e6b639bd27a6"}],"_id":"69f1c241cde2e6b639bd27a5"},"synonyms":[{"value":"DI21","_id":"69f1c241cde2e6b639bd27a8","evidences":[]}],"olnNames":[{"value":"At4g15910","_id":"69f1c241cde2e6b639bd27a9","evidences":[]}],"orfNames":[{"value":"dl3995w","_id":"69f1c241cde2e6b639bd27aa","evidences":[]},{"value":"FCAALL.235","_id":"69f1c241cde2e6b639bd27ab","evidences":[]}],"_id":"69f1c241cde2e6b639bd27a4"}],"length":104,"name":"Late embryogenis abundant protein 41","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions_counter":2,"released":"2026_06","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"regions":[{"start":32,"end":104,"reference_id":"33474748","reference_source":"pmid","reference_html":"The in vitro structure and functions of the disordered late embryogenesis abundant three proteins. <i> Singh KK, Graether SP. </i> Protein Sci, 2021","date":"2026-06-08T12:16:37.175Z","curator_id":"grivas","curator_name":"Gabriel Alejandro Rivas","curator_orcid":"0000-0001-9987-3159","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04571r001","sequence_construct":"VATSQNVTAAGLSKGGSTRVMVGKMEQRGLDQEAESAWGPDPVTGYYRPSNRAAEIDPAELRELLLKNKAKSF","statement":[{"text":"We therefore expressed the mature form of the protein, where sequence before the predicted cut-site (Figure 1(a), black triangles) were removed from the corresponding DNA sequence, which resulted in soluble protein expression.","type":"Results"},{"text":"The results show that all four proteins possess similar CD spectra; a large negative minimum ellipticity is observed at ~200 nm, and a small negative signal is seen after 212 nm (Figure 1(c)), suggesting that these proteins are largely disordered when alone in solution.","type":"Results"}],"last_modified_by":"grivas","last_modified_name":"Gabriel Alejandro Rivas","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T15:26:57.829Z"}},{"start":32,"end":104,"reference_id":"33474748","reference_source":"pmid","reference_html":"The in vitro structure and functions of the disordered late embryogenesis abundant three proteins. <i> Singh KK, Graether SP. </i> Protein Sci, 2021","date":"2026-06-08T12:22:29.902Z","curator_id":"grivas","curator_name":"Gabriel Alejandro Rivas","curator_orcid":"0000-0001-9987-3159","term_id":"GO:0009631","term_name":"cold acclimation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IDA","region_id":"DP04571r002","sequence_construct":"VATSQNVTAAGLSKGGSTRVMVGKMEQRGLDQEAESAWGPDPVTGYYRPSNRAAEIDPAELRELLLKNKAKSF","statement":[{"text":"It has previously been shown that multiple freeze–thaw cycles can reduce LDH activity to essentially zero,52 and that LEA proteins from several different groups can protect the enzyme from losing activity.22,53","type":"Results"},{"text":"Since LEA3 proteins have not been previously tested, and expression data has shown that AtLEA3‐1 and AtLEA3‐2 proteins are upregulated in response to cold stress,39,54 we examined the protective effects of the four AtLEA3 proteins on freeze–thaw damaged LDH.","type":"Results"},{"text":"For all proteins studied here, AtLEA3‐1 (91 μg/ml) and AtLEA3‐4 (92 μg/ml) had relatively similar PD50 values, with AtLEA3‐2 (79 μg/ml) being slightly more efficient and AtLEA3‐3 (58 μg/ml) being the most efficient of the group.","type":"Discussion"}],"term_comment":"","term_def":"\"Any process that increases freezing tolerance of an organism in response to low, nonfreezing temperatures.\" [GOC:syr]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"grivas","last_modified_name":"Gabriel Alejandro Rivas","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T15:26:47.923Z"}}],"__v":0,"disorder_content":0.7019230769230769,"disprot_consensus":{"full":[{"start":32,"end":104,"type":"D"}],"Structural state":[{"start":32,"end":104,"type":"D"}],"Biological process":[{"start":32,"end":104,"type":"F"}]}},{"acc":"Q9M349","sequence":"MSQSLFNLKSLSRSINNTIRMRRYIVITKASQRAYTIGSSQEKPSWASDPDTGYFRPETAAKELDPYIAKTSQVQGKMMRGEELWWMPDPQTGYYRPDNFARELDAVELRSLHFNKNQKTYVVS","creator":"grivas","dataset":[],"date":"2026-04-29T09:52:04.500Z","disprot_id":"DP04572","features":{"pfam":[{"id":"PF03242","name":"Late embryogenesis abundant protein (LEA_3a subfamily)","start":29,"end":66},{"id":"PF03242","name":"Late embryogenesis abundant protein (LEA_3a subfamily)","start":74,"end":117}]},"genes":[{"name":{"value":"LEA37","evidences":[{"source":{"alternativeUrl":"https://europepmc.org/abstract/MED/25005920","id":"25005920","name":"PubMed","url":"http://www.ncbi.nlm.nih.gov/pubmed/25005920","_id":"69f1d4c4cde2e6b639bd27d1"},"code":"ECO:0000303","_id":"69f1d4c4cde2e6b639bd27d0"}],"_id":"69f1d4c4cde2e6b639bd27cf"},"synonyms":[],"olnNames":[{"value":"At3g53770","_id":"69f1d4c4cde2e6b639bd27d2","evidences":[]}],"orfNames":[{"value":"F5K20.70","_id":"69f1d4c4cde2e6b639bd27d3","evidences":[]}],"_id":"69f1d4c4cde2e6b639bd27ce"}],"length":124,"name":"Late embryogenesis abundant protein 37","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions_counter":10,"released":"2026_06","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"regions":[{"start":36,"end":124,"reference_id":"33474748","reference_source":"pmid","reference_html":"The in vitro structure and functions of the disordered late embryogenesis abundant three proteins. <i> Singh KK, Graether SP. </i> Protein Sci, 2021","date":"2026-06-09T12:17:02.041Z","curator_id":"grivas","curator_name":"Gabriel Alejandro Rivas","curator_orcid":"0000-0001-9987-3159","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04572r001","sequence_construct":"TIGSSQEKPSWASDPDTGYFRPETAAKELDPYIAKTSQVQGKMMRGEELWWMPDPQTGYYRPDNFARELDAVELRSLHFNKNQKTYVVS","statement":[{"text":"For all biochemical and structural experiments presented here, we used the mature form of the AtLEA3 proteins.","type":"Results"},{"text":"The results show that all four proteins possess similar CD spectra; a large negative minimum ellipticity is observed at ~200 nm, and a small negative signal is seen after 212 nm (Figure 1(c)), suggesting that these proteins are largely disordered when alone in solution.","type":"Results"}],"last_modified_by":"grivas","last_modified_name":"Gabriel Alejandro Rivas","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T15:28:34.380Z"}},{"start":36,"end":124,"reference_id":"33474748","reference_source":"pmid","reference_html":"The in vitro structure and functions of the disordered late embryogenesis abundant three proteins. <i> Singh KK, Graether SP. </i> Protein Sci, 2021","date":"2026-06-09T12:27:55.612Z","curator_id":"grivas","curator_name":"Gabriel Alejandro Rivas","curator_orcid":"0000-0001-9987-3159","term_id":"GO:0009631","term_name":"cold acclimation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005801","ec_ontology":"ECO","ec_name":"enzymatic activity assay evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IDA","region_id":"DP04572r002","sequence_construct":"TIGSSQEKPSWASDPDTGYFRPETAAKELDPYIAKTSQVQGKMMRGEELWWMPDPQTGYYRPDNFARELDAVELRSLHFNKNQKTYVVS","statement":[{"text":"For all biochemical and structural experiments presented here, we used the mature form of the AtLEA3 proteins.","type":"Results"},{"text":"Since LEA3 proteins have not been previously tested, and expression data has shown that AtLEA3-1 and AtLEA3-2 proteins are upregulated in response to cold stress,39,54 we examined the protective effects of the four AtLEA3 proteins on freeze–thaw damaged LDH.","type":"Results"},{"text":"For all proteins studied here, AtLEA3-1 (91 μg/ml) and AtLEA3-4 (92 μg/ml) had relatively similar PD50 values, with AtLEA3-2 (79 μg/ml) being slightly more efficient and AtLEA3-3 (58 μg/ml) being the most efficient of the group.","type":"Discussion"}],"term_comment":"","term_def":"\"Any process that increases freezing tolerance of an organism in response to low, nonfreezing temperatures.\" [GOC:syr]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"grivas","last_modified_name":"Gabriel Alejandro Rivas","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T15:28:50.240Z"}},{"start":36,"end":124,"reference_id":"33474748","reference_source":"pmid","reference_html":"The in vitro structure and functions of the disordered late embryogenesis abundant three proteins. <i> Singh KK, Graether SP. </i> Protein Sci, 2021","date":"2026-06-22T09:16:07.570Z","curator_id":"grivas","curator_name":"Gabriel Alejandro Rivas","curator_orcid":"0000-0001-9987-3159","term_id":"GO:0005507","term_name":"copper ion binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IPI","region_id":"DP04572r003","term_comment":"","term_def":"\"Binding to a copper (Cu) ion.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"grivas","last_modified_name":"Gabriel Alejandro Rivas","statement":[{"text":"Only AtLEA3-4 bound two of the tested metals, specifically Cu2+ and Fe3+ (Figure S2).","type":"Results"},{"text":"Fitting the calorimetric data suggested a one-site binding model for Cu²⁺, which showed basic exothermic behavior.","type":"Results"},{"text":"The binding affinity for both metals was in the low micromolar range, although the binding affinity of AtLEA3-4 for Fe³⁺ was stronger than for Cu²⁺.","type":"Results"},{"text":"The ITC data support Cu²⁺ binding by AtLEA3-4 and were fitted using a one-site binding model. However, the publication does not map the Cu²⁺ binding site to specific residues or to a smaller region of the protein. Therefore, the copper ion binding annotation is assigned to the full experimentally tested mature AtLEA3-4 construct, corresponding to Q9M349 residues 36–124.","type":"Curator statement"}],"interaction_partner":[{"db":"ChEBI","id":"29036","operator":"and","partner_start":null,"partner_end":null}],"sequence_construct":"TIGSSQEKPSWASDPDTGYFRPETAAKELDPYIAKTSQVQGKMMRGEELWWMPDPQTGYYRPDNFARELDAVELRSLHFNKNQKTYVVS","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-22T13:00:16.597Z"}},{"start":36,"end":124,"reference_id":"33474748","reference_source":"pmid","reference_html":"The in vitro structure and functions of the disordered late embryogenesis abundant three proteins. <i> Singh KK, Graether SP. </i> Protein Sci, 2021","date":"2026-06-22T09:16:54.486Z","curator_id":"grivas","curator_name":"Gabriel Alejandro Rivas","curator_orcid":"0000-0001-9987-3159","term_id":"GO:0008199","term_name":"ferric iron binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"ChEBI","id":"29034","operator":"and","partner_start":null,"partner_end":null}],"region_id":"DP04572r004","statement":[{"text":"Only AtLEA3-4 bound two of the tested metals, specifically Cu²⁺ and Fe³⁺ (Figure S2).","type":"Results"},{"text":"The fit for Fe³⁺ suggested a two-site binding model, and displayed a more complex behavior involving both exothermic and endothermic processes.","type":"Results"},{"text":"The binding affinity for both metals was in the low micromolar range, although the binding affinity of AtLEA3-4 for Fe³⁺ was stronger than for Cu²⁺.","type":"Results"},{"text":"The ITC data support Fe³⁺ binding by AtLEA3-4 and were fitted using a two-site binding model. However, the publication does not identify the residues corresponding to either Fe³⁺ binding site. Therefore, the ferric iron binding annotation is assigned to the full experimentally tested mature AtLEA3-4 construct, corresponding to Q9M349 residues 36–124.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a ferric iron ion, Fe(III).\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"grivas","last_modified_name":"Gabriel Alejandro Rivas","sequence_construct":"TIGSSQEKPSWASDPDTGYFRPETAAKELDPYIAKTSQVQGKMMRGEELWWMPDPQTGYYRPDNFARELDAVELRSLHFNKNQKTYVVS","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-22T13:00:30.364Z"}},{"start":86,"end":104,"reference_id":"33474748","reference_source":"pmid","reference_html":"The in vitro structure and functions of the disordered late embryogenesis abundant three proteins. <i> Singh KK, Graether SP. </i> Protein Sci, 2021","date":"2026-06-10T09:13:46.884Z","curator_id":"grivas","curator_name":"Gabriel Alejandro Rivas","curator_orcid":"0000-0001-9987-3159","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04572r005","statement":[{"text":"We chose to use dodecylphosphocholine micelles (DPC micelles) as a membrane mimetic since phosphocholine is a major constituent of the mitochondrial outer membrane, 55 and these micelles are highly amenable to structural characterization by CD and nuclear magnetic resonance (NMR).","type":"Results"},{"text":"The larger shift changes (i.e., above one standard deviation of the average) occurred in residues 45–47, 54–56, 94–96 and 104–106. Residues 45–47 and 54–56 are found in the first W-motif, residues 94–96 are found in the second W-motif, and residues 104–106 are found in the C-terminal DAELR motif. In addition, residues 64–69, 86–90, and 98–103 appeared to be in slow or intermediate exchange (shown with red asterisks), which can be also interpreted as residues that are binding DPC. ","type":"Results"},{"text":"DPC was used as a lipid membrane-mimetic component in this study. Therefore, this feature is curated as lipid binding.","type":"Curator statement"}],"ec_go":"EXP","last_modified_by":"grivas","last_modified_name":"Gabriel Alejandro Rivas","term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"sequence_construct":"TIGSSQEKPSWASDPDTGYFRPETAAKELDPYIAKTSQVQGKMMRGEELWWMPDPQTGYYRPDNFARELDAVELRSLHFNKNQKTYVVS","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"78018","statements":[{"type":"Methods","text":"For the titration experiments, 15N‐HSQC spectra of AtLEA3‐4 protein were collected in the presence of 0, 1, 2, 3, 5, 7.5, 10, 20, 30, 50, 75 and 100 mM DPC."}],"entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T15:39:53.374Z"}},{"start":40,"end":50,"reference_id":"33474748","reference_source":"pmid","reference_html":"The in vitro structure and functions of the disordered late embryogenesis abundant three proteins. <i> Singh KK, Graether SP. </i> Protein Sci, 2021","date":"2026-06-10T09:00:54.856Z","curator_id":"grivas","curator_name":"Gabriel Alejandro Rivas","curator_orcid":"0000-0001-9987-3159","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04572r006","statement":[{"text":"To provide residue-specific information on the AtLEA3-4 interaction with DPC, we examined the structure of the protein in the presence and absence of DPC micelles using protein NMR.","type":"Results"},{"text":"The program δ2D56 was used to analyze the HN, Hα, Cα, Cβ, C0, and backbone N chemical shifts of AtLEA3-4 alone and in the presence of DPC.","type":"Results"},{"text":"In the presence of DPC (Figure 7(c)), several residues in residues 40–50 (first W-motif ), 76–82 (first DAELR motif), and 90–100 (second W-motif ) show a gain in α-helicity, while residues 110–114 gain β-strand, and residues 120–123 lose α-helicity and gain β-strand.","type":"Results"},{"text":"DPC micelles were used as a lipid membrane-mimetic component. Therefore, this transition is interpreted as an in vitro DPC-induced disorder-to-alpha-helix transition.","type":"Curator statement"}],"last_modified_by":"grivas","last_modified_name":"Gabriel Alejandro Rivas","sequence_construct":"TIGSSQEKPSWASDPDTGYFRPETAAKELDPYIAKTSQVQGKMMRGEELWWMPDPQTGYYRPDNFARELDAVELRSLHFNKNQKTYVVS","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"78018","statements":[{"type":"Methods","text":"For the titration experiments, 15N‐HSQC spectra of AtLEA3‐4 protein were collected in the presence of 0, 1, 2, 3, 5, 7.5, 10, 20, 30, 50, 75 and 100 mM DPC."}],"entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T15:42:10.742Z"}},{"start":90,"end":100,"reference_id":"33474748","reference_source":"pmid","reference_html":"The in vitro structure and functions of the disordered late embryogenesis abundant three proteins. <i> Singh KK, Graether SP. </i> Protein Sci, 2021","date":"2026-06-10T09:13:18.834Z","curator_id":"grivas","curator_name":"Gabriel Alejandro Rivas","curator_orcid":"0000-0001-9987-3159","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04572r007","statement":[{"text":"To provide residue-specific information on the AtLEA3-4 interaction with DPC, we examined the structure of the protein in the presence and absence of DPC micelles using protein NMR.\" ","type":"Results"},{"text":"The program δ2D56 was used to analyze the HN, Hα, Cα, Cβ, C0, and backbone N chemical shifts of AtLEA3-4 alone and in the presence of DPC.","type":"Results"},{"text":"In the presence of DPC (Figure 7(c)), several residues in residues 40–50 (first W-motif ), 76–82 (first DAELR motif), and 90–100 (second W-motif ) show a gain in α-helicity, while residues 110–114 gain β-strand, and residues 120–123 lose α-helicity and gain β-strand.","type":"Results"},{"text":"DPC micelles were used as a lipid membrane-mimetic component. Therefore, this transition is interpreted as an in vitro DPC-induced disorder-to-alpha-helix transition.","type":"Curator statement"}],"last_modified_by":"grivas","last_modified_name":"Gabriel Alejandro Rivas","sequence_construct":"TIGSSQEKPSWASDPDTGYFRPETAAKELDPYIAKTSQVQGKMMRGEELWWMPDPQTGYYRPDNFARELDAVELRSLHFNKNQKTYVVS","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"78018","statements":[{"type":"Methods","text":"For the titration experiments, 15N‐HSQC spectra of AtLEA3‐4 protein were collected in the presence of 0, 1, 2, 3, 5, 7.5, 10, 20, 30, 50, 75 and 100 mM DPC."}],"entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T15:42:07.199Z"}},{"start":64,"end":69,"reference_id":"33474748","reference_source":"pmid","reference_html":"The in vitro structure and functions of the disordered late embryogenesis abundant three proteins. <i> Singh KK, Graether SP. </i> Protein Sci, 2021","date":"2026-06-10T09:12:58.204Z","curator_id":"grivas","curator_name":"Gabriel Alejandro Rivas","curator_orcid":"0000-0001-9987-3159","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"EXP","region_id":"DP04572r008","statement":[{"text":"We chose to use dodecylphosphocholine micelles (DPC micelles) as a membrane mimetic since phosphocholine is a major constituent of the mitochondrial outer membrane, 55 and these micelles are highly amenable to structural characterization by CD and nuclear magnetic resonance (NMR).","type":"Results"},{"text":"Residues 64–69 are found in what appears to be a second, previously unidentified DAELR motif that occurs after the first W‐motif, neither of which are found in the other three AtLEA3 proteins (Figure 6(c), S3). In addition, residues 64–69, 86–90, and 98–103 appeared to be in slow or intermediate exchange (shown with red asterisks), which can be also interpreted as residues that are binding DPC.","type":"Results"},{"text":"DPC was used as a lipid membrane-mimetic component in this study. Therefore, this feature is curated as lipid binding.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"grivas","last_modified_name":"Gabriel Alejandro Rivas","sequence_construct":"TIGSSQEKPSWASDPDTGYFRPETAAKELDPYIAKTSQVQGKMMRGEELWWMPDPQTGYYRPDNFARELDAVELRSLHFNKNQKTYVVS","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"78018","statements":[{"type":"Methods","text":"For the titration experiments, 15N‐HSQC spectra of AtLEA3‐4 protein were collected in the presence of 0, 1, 2, 3, 5, 7.5, 10, 20, 30, 50, 75 and 100 mM DPC."}],"entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T15:40:32.998Z"}},{"start":45,"end":56,"reference_id":"33474748","reference_source":"pmid","reference_html":"The in vitro structure and functions of the disordered late embryogenesis abundant three proteins. <i> Singh KK, Graether SP. </i> Protein Sci, 2021","date":"2026-06-10T09:12:32.805Z","curator_id":"grivas","curator_name":"Gabriel Alejandro Rivas","curator_orcid":"0000-0001-9987-3159","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"EXP","region_id":"DP04572r009","statement":[{"text":"We chose to use dodecylphosphocholine micelles (DPC micelles) as a membrane mimetic since phosphocholine is a major constituent of the mitochondrial outer membrane, 55 and these micelles are highly amenable to structural characterization by CD and nuclear magnetic resonance (NMR).","type":"Results"},{"text":"Residues 64–69 are found in what appears to be a second, previously unidentified DAELR motif that occurs after the first W‐motif, neither of which are found in the other three AtLEA3 proteins (Figure 6(c), S3). In addition, residues 64–69, 86–90, and 98–103 appeared to be in slow or intermediate exchange (shown with red asterisks), which can be also interpreted as residues that are binding DPC.","type":"Results"},{"text":"DPC was used as a lipid membrane-mimetic component in this study. Therefore, this feature is curated as lipid binding.","type":"Curator statement"}],"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"grivas","last_modified_name":"Gabriel Alejandro Rivas","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"78018","statements":[{"type":"Methods","text":"For the titration experiments, 15N‐HSQC spectra of AtLEA3‐4 protein were collected in the presence of 0, 1, 2, 3, 5, 7.5, 10, 20, 30, 50, 75 and 100 mM DPC."}],"entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T15:41:15.291Z"}}],"__v":0,"disorder_content":0.717741935483871,"disprot_consensus":{"full":[{"start":36,"end":39,"type":"D"},{"start":40,"end":50,"type":"T"},{"start":51,"end":89,"type":"D"},{"start":90,"end":100,"type":"T"},{"start":101,"end":124,"type":"D"}],"Structural state":[{"start":36,"end":124,"type":"D"}],"Biological process":[{"start":36,"end":124,"type":"F"}],"Molecular function":[{"start":36,"end":124,"type":"F"}],"Structural transition":[{"start":40,"end":50,"type":"T"},{"start":90,"end":100,"type":"T"}]}},{"acc":"P23246","sequence":"MSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGQSGPKPPIPPPPPHQQQQQPPPQQPPPQQPPPHQPPPHPQPHQQQQPPPPPQDSSKPVVAQGPGPAPGVGSAPPASSSAPPATPPTSGAPPGSGPGPTPTPPPAVTSAPPGAPPPTPPSSGVPTTPPQAGGPPPPPAAVPGPGPGPKQGPGPGGPKGGKMPGGPKPGGGPGLSTPGGHPKPPHRGGGEPRGGRQHHPPYHQQHHQGPPPGGPGGRSEEKISDSEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGRQLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFASKPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRFAQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLLRQDLMRRQEELRRMEELHNQEMQKRKEMQLRQEEERRRREEEMMIRQREMEEQMRRQREESYSRMGYMDPRERDMRMGGGGAMNMGDPYGSGGQKFPPLGGGGGIGYEANPGVPPATMSGSMMGSDMRTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPNKKPRF","creator":"grivas","dataset":["Cancer-related proteins","Condensates-related proteins","RNA-binding proteins"],"date":"2026-05-07T11:39:02.080Z","disprot_id":"DP04574","features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":299,"end":363},{"id":"PF00076","name":"RNA recognition motif","start":374,"end":433},{"id":"PF08075","name":"NOPS (NUC059) domain","start":444,"end":495}]},"genes":[{"name":{"value":"SFPQ","_id":"69fc79d6cde2e6b639bd298f","evidences":[]},"synonyms":[{"value":"PSF","_id":"69fc79d6cde2e6b639bd2990","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"69fc79d6cde2e6b639bd298e"}],"length":707,"name":"Splicing factor, proline- and glutamine-rich","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":4,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":1,"end":277,"reference_id":"40574713","reference_source":"pmid","reference_html":"Structural dynamics of IDR interactions in human SFPQ and implications for liquid-liquid phase separation. <i> Koning HJ, Lai V, Sethi A, Sethi A, Chakraborty S, Ang CS, Fox AH, Duff AP, Whitten AE, Marshall AC, Bond CS. </i> Acta Crystallogr D Struct Biol, 2025","date":"2026-06-08T09:34:28.802Z","curator_id":"grivas","curator_name":"Gabriel Alejandro Rivas","curator_orcid":"0000-0001-9987-3159","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"SASBDB","id":"SASDV57"},{"db":"SASBDB","id":"SASDFK3"}],"region_id":"DP04574r001","statement":[{"text":"Our solution scattering data demonstrate experimentally that the N- and C-terminal IDRs of SFPQ are long, disordered and flexible in solution.","type":"Introduction"},{"text":"The dimensionless Kratky plots for these experiments indicate a progression from globular to partly rod-like to flexible upon the addition of either the N-terminal or both IDRs (Fig. 2g), corroborating the predictions that both the C- and N-terminal IDRs are long, flexible and disordered.","type":"Results"},{"text":"Boundaries 1-277 correspond to the N-terminal region of SFPQ outside the folded DBHS core, according to the domain organization used by the authors. The annotation is supported by comparative SAXS analyses of IDR-containing SFPQ variants, including full-length SFPQ and SFPQ1-598, against IDR-lacking DBHS core constructs.","type":"Curator statement"}],"last_modified_by":"grivas","last_modified_name":"Gabriel Alejandro Rivas","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T14:54:23.004Z"}},{"start":599,"end":707,"reference_id":"40574713","reference_source":"pmid","reference_html":"Structural dynamics of IDR interactions in human SFPQ and implications for liquid-liquid phase separation. <i> Koning HJ, Lai V, Sethi A, Sethi A, Chakraborty S, Ang CS, Fox AH, Duff AP, Whitten AE, Marshall AC, Bond CS. </i> Acta Crystallogr D Struct Biol, 2025","date":"2026-06-08T09:36:42.337Z","curator_id":"grivas","curator_name":"Gabriel Alejandro Rivas","curator_orcid":"0000-0001-9987-3159","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"SASBDB","id":"SASDV57"},{"db":"SASBDB","id":"SASDV67"}],"region_id":"DP04574r002","statement":[{"text":"The dimensionless Kratky plots for these experiments indicate a progression from globular to partly rod-like to flexible upon the addition of either the N-terminal or both IDRs (Fig. 2g), corroborating the predictions that both the C- and N-terminal IDRs are long, flexible and disordered","type":"Results"},{"text":"Upon further consideration, it is likely that this peak corresponds to vectors contributed by the C-terminal IDRs, which are anchored ∼270 Å apart and should naturally contribute many pairwise distances at r > 270 Å (Supplementary Fig. S5)","type":"Results"},{"text":"The annotated region corresponds to the C-terminal intrinsically disordered region of human SFPQ. Boundaries 599-707 were selected because SFPQ1-598 lacks the C-terminal IDR, whereas full-length SFPQ1-707 includes it. Comparative SEC-SAXS, P(r), Kratky plot and EOM analyses support that the C-terminal region contributes to an extended, flexible and disordered conformational ensemble in solution.","type":"Curator statement"}],"last_modified_by":"grivas","last_modified_name":"Gabriel Alejandro Rivas","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-18T14:55:03.452Z"}}],"__v":0,"disorder_content":0.545968882602546,"disprot_consensus":{"full":[{"start":1,"end":277,"type":"D"},{"start":599,"end":707,"type":"D"}],"Structural state":[{"start":1,"end":277,"type":"D"},{"start":599,"end":707,"type":"D"}]}},{"acc":"Q9V2F3","sequence":"MDELVKALERAGYLLTPSAYYLLVDHFKEGKFSLVELVKFAKSKGVFIIDGDLAYEFLQFLGLGVPQEIKESYISTGEEAEKTVESQETRASELEEGGVSQVSSGELQELKEESPEISTTEEEIGGLELVQSSISTGSEVEYNNGENGESVVVLDKYGYPILYAPEEIGEEKEYSKYEDVVIEWNPSVTPVQIEKNYEVKFDVRQVKLRPPKVKNGSGKEGEIIVEAYASLFKSRLSKLKRILRENPEISNVVDIGKLNYVSGDEEVTIIGLVNSKRETNRGLIFEVEDKTGIVKVFLPKDSEDYREAFKVLPDAVVAFKGFYSKKGIFFANKFYLPDVPLYRKQKPPLEEKVYAILISDIHVGSREFCEKAFLKFLEWLNGHVESKEEEEIVSRVKYLIIAGDVVDGIGIYPGQYSDLVIPDIFDQYEALANLLANVPEHITMFIGPGNHDAARPAIPQPEFYKEYAKPIYKLKNAIIISNPAVIRLHGRDFLIAHGRGIEDVVSFVPGLTHHKPGLPMVELLKMRHLAPTFGGKVPIAPDPEDLLVIEEVPDLVQMGHVHVYDAVVYRGVQLVNSATWQAQTEFQKMVNIVPTPAKVPVVDVESARVVKVLDFSGWC","creator":"vnugnes","dataset":[],"date":"2026-05-12T15:57:23.288Z","disprot_id":"DP04578","features":{"pfam":[{"id":"PF00149","name":"Calcineurin-like phosphoesterase","start":357,"end":564},{"id":"PF22317","name":"DNA polymerase II small subunit, N-terminal domain","start":5,"end":59}]},"genes":[{"name":{"value":"polB","_id":"6a034de3cde2e6b639bd2b6d","evidences":[]},"synonyms":[],"olnNames":[{"value":"PYRAB01210","_id":"6a034de3cde2e6b639bd2b6e","evidences":[]}],"orfNames":[{"value":"PAB2266","_id":"6a034de3cde2e6b639bd2b6f","evidences":[]}],"_id":"6a034de3cde2e6b639bd2b6c"}],"length":619,"name":"DNA polymerase II small subunit","ncbi_taxon_id":272844,"organism":"Pyrococcus abyssi (strain GE5 / Orsay)","regions_counter":3,"released":"2026_06","taxonomy":["Archaea","Methanobacteriati","Methanobacteriota","Thermococci","Thermococcales","Thermococcaceae","Pyrococcus"],"regions":[{"start":164,"end":173,"reference_id":"27548043","reference_source":"pmid","reference_html":"Shared active site architecture between archaeal PolD and multi-subunit RNA polymerases revealed by X-ray crystallography. <i> Sauguet L, Raia P, Henneke G, Delarue M. </i> Nat Commun, 2016","date":"2026-05-12T16:24:35.099Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"5IHE"}],"region_id":"DP04578r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29034","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30089","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17713","entry_name":null}],"statement":[{"text":"Residues 144–151, 164–173, 213–224 and 514–517 (only in chain B), which were not visible in the electron density, were not included in the final model.","type":"Methods"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":66,"end":144,"reference_id":"27548043","reference_source":"pmid","reference_html":"Shared active site architecture between archaeal PolD and multi-subunit RNA polymerases revealed by X-ray crystallography. <i> Sauguet L, Raia P, Henneke G, Delarue M. </i> Nat Commun, 2016","date":"2026-05-12T16:23:07.343Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008035","ec_ontology":"ECO","ec_name":"author inference based on intrinsic disorder prediction used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04578r002","statement":[{"text":"The structure of DP1 presented here encompasses amino acids 144–622, leaving out a flexible N-terminal region that is not evolutionary conserved and not needed for exonuclease activity (Fig. 1a).","type":"Results"},{"text":"The boundaries of this disordered region were determined by the combination of the structural predictors available, including AlphaFold and Mobi DB.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":213,"end":224,"reference_id":"27548043","reference_source":"pmid","reference_html":"Shared active site architecture between archaeal PolD and multi-subunit RNA polymerases revealed by X-ray crystallography. <i> Sauguet L, Raia P, Henneke G, Delarue M. </i> Nat Commun, 2016","date":"2026-05-12T16:24:52.429Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"5IHE"}],"region_id":"DP04578r003","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30742","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29034","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29108","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"30089","entry_name":null},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"17713","entry_name":null}],"statement":[{"text":"Residues 144–151, 164–173, 213–224 and 514–517 (only in chain B), which were not visible in the electron density, were not included in the final model.","type":"Methods"}]}],"__v":0,"disorder_content":0.1631663974151858,"disprot_consensus":{"full":[{"start":66,"end":144,"type":"D"},{"start":164,"end":173,"type":"D"},{"start":213,"end":224,"type":"D"}],"Structural state":[{"start":66,"end":144,"type":"D"},{"start":164,"end":173,"type":"D"},{"start":213,"end":224,"type":"D"}]}},{"acc":"Q9LZ65","sequence":"MGAKAKKALKKNMKKVAASASSSQLPLPQNPKPSADFLPLEGGPARKAPVTTPPLQNKATVLYIGRIPHGFYETEIEAFFSQFGTVKRVRVARNKKTGKSKHFGFIQFEDPEVAEIAAGAMNDYLLMEHMLKVHVIEPENVKPNLWRGFKCNFKPVDSVQIERRQLNKERTLEEHRKMLQKIVKKDQKRRKRIEAAGIEYECPELVGNTQPVPKRIKFSEED","creator":"grivas","dataset":[],"date":"2026-05-14T12:32:50.555Z","disprot_id":"DP04582","features":{"pfam":[{"id":"PF00076","name":"RNA recognition motif","start":62,"end":130}]},"genes":[{"name":{"value":"T32M21_200","evidences":[{"source":{"id":"CAB85566.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/CAB85566.1","_id":"6a05c0f2cde2e6b639bd2c74"},"code":"ECO:0000313","_id":"6a05c0f2cde2e6b639bd2c73"}],"_id":"6a05c0f2cde2e6b639bd2c72"},"synonyms":[],"olnNames":[{"value":"At5g04600","_id":"6a05c0f2cde2e6b639bd2c75","evidences":[]}],"orfNames":[{"value":"T1E3.1","_id":"6a05c0f2cde2e6b639bd2c76","evidences":[]}],"_id":"6a05c0f2cde2e6b639bd2c71"}],"length":222,"name":"AT5g04600/T32M21_200","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions_counter":1,"released":"2026_06","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"regions":[{"start":1,"end":59,"reference_id":"37316549","reference_source":"pmid","reference_html":"Structural and functional analysis of a plant nucleolar RNA chaperone-like protein. <i> Fernandes R, Ostendorp A, Ostendorp S, Mehrmann J, Falke S, Graewert MA, Weingartner M, Kehr J, Hoth S. </i> Sci Rep, 2023","date":"2026-06-03T17:05:40.281Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0007014","ec_ontology":"ECO","ec_name":"combinatorial experimental and curator inference evidence used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"SASBDB","id":"SASDRN5"}],"region_id":"DP04582r001","statement":[{"text":"SREFLEX estimates the flexibility of pre-existing high-resolution models creating new models that aid in finding a conformation that fits the data better. The AlphaFold model was used as input. The resulting fit showed a major improvement (χ2 = 3.04). The DAMMIN P1 and GASBOR P1 models were superimposed with the SREFLEX top model (Fig. 3). The superimposition indicated that both termini did not fit perfectly. This was even more prominent for the N-terminus that besides being flexible was also highly disordered.","type":"Results"},{"text":"As supplementary evidence to the experimental assessment, the boundaries of this disordered region were determined by combining the experimental findings with structural predictions from AlphaFold and MobiDB.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"}],"__v":0,"disorder_content":0.26576576576576577,"disprot_consensus":{"full":[{"start":1,"end":59,"type":"D"}],"Structural state":[{"start":1,"end":59,"type":"D"}]}},{"acc":"Q6VY07","sequence":"MAERGGAGGGPGGAGGGSGQRGSGVAQSPQQPPPQQQQQQPPQQPTPPKLAQATSSSSSTSAAAASSSSSSTSTSMAVAVASGSAPPGGPGPGRTPAPVQMNLYATWEVDRSSSSCVPRLFSLTLKKLVMLKEMDKDLNSVVIAVKLQGSKRILRSNEIVLPASGLVETELQLTFSLQYPHFLKRDANKLQIMLQRRKRYKNRTILGYKTLAVGLINMAEVMQHPNEGALVLGLHSNVKDVSVPVAEIKIYSLSSQPIDHEGIKSKLSDRSPDIDNYSEEEEESFSSEQEGSDDPLHGQDLFYEDEDLRKVKKTRRKLTSTSAITRQPNIKQKFVALLKRFKVSDEVGFGLEHVSREQIREVEEDLDELYDSLEMYNPSDSGPEMEETESILSTPKPKLKPFFEGMSQSSSQTEIGSLNSKGSLGKDTTSPMELAALEKIKSTWIKNQDDSLTETDTLEITDQDMFGDASTSLVVPEKVKTPMKSSKTDLQGSASPSKVEGVHTPRQKRSTPLKERQLSKPLSERTNSSDSERSPDLGHSTQIPRKVVYDQLNQILVSDAALPENVILVNTTDWQGQYVAELLQDQRKPVVCTCSTVEVQAVLSALLTRIQRYCNCNSSMPRPVKVAAVGGQSYLSSILRFFVKSLANKTSDWLGYMRFLIIPLGSHPVAKYLGSVDSKYSSSFLDSGWRDLFSRSEPPVSEQLDVAGRVMQYVNGAATTHQLPVAEAMLTCRHKFPDEDSYQKFIPFIGVVKVGLVEDSPSTAGDGDDSPVVSLTVPSTSPPSSSGLSRDATATPPSSPSMSSALAIVGSPNSPYGDVIGLQVDYWLGHPGERRREGDKRDASSKNTLKSVFRSVQVSRLPHSGEAQLSGTMAMTVVTKEKNKKVPTIFLSKKPREKEVDSKSQVIEGISRLICSAKQQQTMLRVSIDGVEWSDIKFFQLAAQWPTHVKHFPVGLFSGSKAT","creator":"bjuhasz","dataset":[],"date":"2026-05-21T10:05:39.695Z","disprot_id":"DP04587","features":{"pfam":[{"id":"PF10254","name":"PACS-1 cytosolic sorting protein","start":548,"end":958},{"id":"PF25332","name":"N-terminal C2 domain of phosphofurin acidic cluster sorting protein","start":99,"end":259}]},"genes":[{"name":{"value":"PACS1","_id":"6a0ed8f3fb076a9c7ac71214","evidences":[]},"synonyms":[{"value":"KIAA1175","_id":"6a0ed8f3fb076a9c7ac71215","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"6a0ed8f3fb076a9c7ac71213"}],"length":963,"name":"Phosphofurin acidic cluster sorting protein 1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":1,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":260,"end":273,"reference_id":"41858172","reference_source":"pmid","reference_html":"The R203W substitution drives PACS-1 syndrome by disrupting intramolecular regulation. <i> Krzysiak TC, Byeon IL, Ponticelli R, Lucas ME, Thompson L, DeHaven C, Thomas G, Gronenborn AM. </i> FEBS J, 2026","date":"2026-06-18T12:23:18.102Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":"0009-0009-6028-6956","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"For isotopically (13C, 15N) enriched proteins, cells were grown at 37 °C in modified M9 medium, supplemented with 15N-ammonium chloride or 15N-ammonium chloride and 13C-glucose until OD600 = 0.6. "}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro244Lys","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Reversions of V241A, S242P, V245A did not affect the quality of the spectrum, while K249W and Y251A were critical for spectral improvement. In addition, P244K enhanced the yield of the purified protein."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Lys249Trp","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Reversions of V241A, S242P, V245A did not affect the quality of the spectrum, while K249W and Y251A were critical for spectral improvement. In addition, P244K enhanced the yield of the purified protein."}]},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Tyr251Ala","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"Reversions of V241A, S242P, V245A did not affect the quality of the spectrum, while K249W and Y251A were critical for spectral improvement. In addition, P244K enhanced the yield of the purified protein."}]}],"cross_refs":[{"db":"PDB","id":"9Z30"},{"db":"BMRB","id":"31281"}],"region_id":"DP04587r001","statement":[{"text":" The largest r.m.s.d. values (> 3 Å) were observed for the unstructured C-terminus (residues 260–273) and the first loop (residues 110–113) due to a low number of experimental constraints (Fig. 3A).","type":"Results"}],"last_modified_by":"bjuhasz","last_modified_name":"Bernadett Juhász","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-19T13:05:03.398Z"}}],"__v":0,"disorder_content":0.014537902388369679,"disprot_consensus":{"full":[{"start":260,"end":273,"type":"D"}],"Structural state":[{"start":260,"end":273,"type":"D"}]}},{"acc":"Q9W3J0","sequence":"MIKVQPPPDVAGGYHNLRCGEVLFSAPASYEVSCLLCDQRLPLDGYPEHFRLKHFTNSSSSLCSNELESDPIAQDVVEVQGNEELHEELAKEASPDLEEEEEEKEEGSKRQHYQRAAAMKNTLVETREDLLDIELDWTGGEQSEHNETHEEEEGESDDDDTKDSNDTKDMLFQCDQCDRAYNTKRSLQSHRRLKHSEANGGSLDKSASERNSKKRKGPPKVYKCNEEACNQTFRTERDLRGHRWKHTGIFCDICGKPFTQSGNMMRHRQRHSGIKPHKCPECDATFYTQKELSSHSICHTGRMPCICEVCGRPCRDRGVLTAHMRRHTGERPAKCEVCGKAFYSFHDLNVHAVSHTNLRPFVCDVCGSTFQRKKALRVHKLLHSEQRKYACKLCGKTFAQSGGLNAHMRSHDPARVKGAVKPLPQSVTIEVIEGKSPPTTTITMAIDLNVEEQLVKQTETAPTTWRLAN","creator":"bjuhasz","dataset":[],"date":"2026-05-21T11:36:43.459Z","disprot_id":"DP04588","features":{"pfam":[{"id":"PF00096","name":"Zinc finger, C2H2 type","start":172,"end":195},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":251,"end":271},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":306,"end":327},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":334,"end":355},{"id":"PF00096","name":"Zinc finger, C2H2 type","start":389,"end":411},{"id":"PF13912","name":"C2H2-type zinc finger","start":221,"end":246},{"id":"PF13912","name":"C2H2-type zinc finger","start":277,"end":299},{"id":"PF13912","name":"C2H2-type zinc finger","start":361,"end":380}]},"genes":[{"name":{"value":"Imzf","evidences":[{"source":{"id":"FBgn0030012","name":"FlyBase","url":"http://flybase.org/reports/FBgn0030012.html","_id":"6a0eee4bfb076a9c7ac7122a"},"code":"ECO:0000313","_id":"6a0eee4bfb076a9c7ac71229"}],"_id":"6a0eee4bfb076a9c7ac71228"},"synonyms":[{"value":"CG18262-RA","_id":"6a0eee4bfb076a9c7ac7122b","evidences":[]},{"value":"Dmel\\CG18262","_id":"6a0eee4bfb076a9c7ac7122c","evidences":[]}],"olnNames":[],"orfNames":[{"value":"CG18262","_id":"6a0eee4bfb076a9c7ac7122d","evidences":[]},{"value":"Dmel_CG18262","_id":"6a0eee4bfb076a9c7ac7122e","evidences":[]}],"_id":"6a0eee4bfb076a9c7ac71227"}],"length":469,"name":"FI23536p1","ncbi_taxon_id":7227,"organism":"Drosophila melanogaster","regions_counter":2,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Ecdysozoa","Arthropoda","Hexapoda","Insecta","Pterygota","Neoptera","Endopterygota","Diptera","Brachycera","Muscomorpha","Ephydroidea","Drosophilidae","Drosophila","Sophophora"],"regions":[{"start":1,"end":13,"reference_id":"41495890","reference_source":"pmid","reference_html":"Beyond DNA binding: single C2H2 zinc fingers with adjacent β-strands mediate dimerization in Drosophila transcription factors. <i> Balagurov KI, Mariasina SS, Dukhalin SD, Sluchanko NN, Golovnina AA, Khrustaleva AM, Maksimenko OG, Arkova OV, Stepanenko AA, Bocharov EV, Polshakov VI, Georgiev PG, Bonchuk AN. </i> Nucleic Acids Res, 2026","date":"2026-06-16T15:22:47.221Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"NMR samples were prepared at protein concentrations of 0.73 mM for uniformly 13C,15N-labeled IMZF1-62 and 1.0 mM for 15N-labeled IMZF1-62, in 20 mM sodium phosphate buffer (pH 7.0) containing 50 mM NaCl and 0.02% (w/v) sodium azide. "}]},{"term_id":"MI:0379","term_name":"13C label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"NMR samples were prepared at protein concentrations of 0.73 mM for uniformly 13C,15N-labeled IMZF1-62 and 1.0 mM for 15N-labeled IMZF1-62, in 20 mM sodium phosphate buffer (pH 7.0) containing 50 mM NaCl and 0.02% (w/v) sodium azide. "}]}],"cross_refs":[{"db":"PDB","id":"9VCD"},{"db":"BMRB","id":"52953"}],"region_id":"DP04588r001","statement":[{"text":"Notably, the domain contains an additional N-terminal β-strand (residues 14–25) that includes the conserved CGxΦ motif, as well as a disordered N-terminal tail (residues 1–13) extending beyond the structured core (Fig. 3C).","type":"Results"},{"text":"The heteronuclear NOE values (panel A) and low order parameters (S² < 0.5, panel D) confirmed the disordered nature of the N-terminal tail (residues 1–13).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":null}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-16T15:22:50.418Z"}},{"start":1,"end":13,"reference_id":"41495890","reference_source":"pmid","reference_html":"Beyond DNA binding: single C2H2 zinc fingers with adjacent β-strands mediate dimerization in Drosophila transcription factors. <i> Balagurov KI, Mariasina SS, Dukhalin SD, Sluchanko NN, Golovnina AA, Khrustaleva AM, Maksimenko OG, Arkova OV, Stepanenko AA, Bocharov EV, Polshakov VI, Georgiev PG, Bonchuk AN. </i> Nucleic Acids Res, 2026","date":"2026-06-16T15:24:30.149Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005642","ec_ontology":"ECO","ec_name":"heteronuclear single quantum coherence spectroscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"BMRB","id":"52953"}],"region_id":"DP04588r002","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"ChEBI","id":"29105","entry_name":null}],"statement":[{"text":"The heteronuclear NOE values (panel A) and low order parameters (S² < 0.5, panel D) confirmed the disordered nature of the N-terminal tail (residues 1–13).","type":"Results"}]}],"__v":0,"disorder_content":0.02771855010660981,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"D"}],"Structural state":[{"start":1,"end":13,"type":"D"}],"Disorder function":[{"start":1,"end":13,"type":"F"}]}},{"acc":"Q9QWL7","sequence":"MTTTIRQFTSSSSIKGSSGLGGGSSRTSCRLSGSLGAGSCRLGSASGLGSALGSNSYSSCYSFGTGSGYGGNFGGVDGLLAGGEKATMQNLNDRLASYLDKVRALEEANTELEVKIRDWYQKQAPGPARDYSAYYHTIEDLKNKILVATVDNASILLQIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARADLEMQIENLKEELAYLKKNHEEEMNALRGQVGGEINVEMDAAPGVDLSRILSEMRDQYEKMAEKNRKDAEDWFFSKTEELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASLEGSLAETENRYCVQLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAHLTQYKPKEPVTTRQVRTIVEEVQDGKVISSREQVHQTTR","creator":"bjuhasz","dataset":[],"date":"2026-05-22T14:06:20.366Z","disprot_id":"DP04593","features":{"pfam":[{"id":"PF00038","name":"Intermediate filament protein","start":84,"end":393}]},"genes":[{"name":{"value":"Krt17","_id":"6a1062dcfb076a9c7ac712e7","evidences":[]},"synonyms":[{"value":"Krt1-17","_id":"6a1062dcfb076a9c7ac712e8","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"6a1062dcfb076a9c7ac712e6"}],"length":433,"name":"Keratin, type I cytoskeletal 17","ncbi_taxon_id":10090,"organism":"Mus musculus","regions_counter":3,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"regions":[{"start":390,"end":433,"reference_id":"41043210","reference_source":"pmid","reference_html":"Structure and function of the keratin 17 tail domain associated with keratin intermediate filament organization. <i> Yeom J, Lee S, Ko YH, Hong E, Kim JH, Coulombe PA, Lee CH. </i> Eur J Cell Biol, 2025","date":"2026-05-22T14:21:44.123Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0379","term_name":"13C label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"For NMR experiments, [U-13C; U-15N]-K17T samples were prepared at a concentration of 0.34 mg/mL in a buffer containing 50 mM sodium phosphate (pH 7.4) and 7 % deuterium oxide (Cambridge isotope). "}]},{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"For NMR experiments, [U-13C; U-15N]-K17T samples were prepared at a concentration of 0.34 mg/mL in a buffer containing 50 mM sodium phosphate (pH 7.4) and 7 % deuterium oxide (Cambridge isotope). "}]}],"cross_refs":[{"db":"PDB","id":"9M1Y"}],"region_id":"DP04593r001","statement":[{"text":"The probability of each residue adopting an α-helix, β-strand, or loop (coil) conformation was determined. The central region (V408–V412) of K17T exhibited a higher probability of forming a β-strand, though only 40 %–60 %. The remaining residues were predominantly predicted to form loop structures (Fig. 4A). This analysis suggests that K17T is a highly disordered region with a minimally stable secondary structure.","type":"Results"},{"text":"Most residues of K17T had RCI-S² values near or below 0.6 (Fig. 4B). Combined with the secondary structure prediction, this data strongly suggests that K17T is an intrinsically disordered region (IDR).","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-16T17:37:50.020Z"}},{"start":404,"end":410,"reference_id":"41043210","reference_source":"pmid","reference_html":"Structure and function of the keratin 17 tail domain associated with keratin intermediate filament organization. <i> Yeom J, Lee S, Ko YH, Hong E, Kim JH, Coulombe PA, Lee CH. </i> Eur J Cell Biol, 2025","date":"2026-06-19T13:37:57.311Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":"0009-0009-6028-6956","term_id":"GO:0045110","term_name":"intermediate filament bundle assembly","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007089","ec_ontology":"ECO","ec_name":"loss-of-function mutant phenotype evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IMP","region_id":"DP04593r002","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P50446","statements":[{"type":"Methods","text":"Filament bundles were visualized with differential interference (DIC) microscopy, also described previously (Lee and Coulombe, 2009). Briefly, a keratin solution (30 μL per sample) was put on a glass slide with the barriers of hydrophobic nail polish solution."},{"type":"Figure","text":"(I-K) DIC images for bundled keratin filaments of K6/K17, K6/K17∆T, and K6/K17∆CT. The scale bars represent 500 μm."}]}],"statement":[{"text":"To provide an alternative approach to visualizing keratin filament bundle formation involving a large fraction of the samples, DIC microscopy was conducted. While K6/K17 wild-type readily formed relatively thick filament bundles (Fig. 7I), the K6/K17∆T and K6/K17∆CT mutants only formed very thin bundles (Fig. 7J and K). These analyses involving the K6/K17∆CT mutant confirmed that the curved core region (T404-T410) seen by NMR microscopy is required to form K6/K17 keratin bundles.","type":"Results"}],"term_comment":"","term_def":"\"The formation of the bundles of intermediate filaments. Intermediate filament-associated proteins (IFAPs) cross-link intermediate filaments with one another, forming a bundle or a network, and with other cell structures, including the plasma membrane. The organization of intermediate filaments and their supportive function in various cells types depends in large part on their linkage to other cell structures via IFAPs.\" [ISBN:0716731363]","term_is_obsolete":false,"term_not_annotate":false,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Thr404Thr410del","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"The DNA gene of the K17 deletion mutant of the curved tail region (K17∆CT; full-length K17 internally deleted from T404 to T410) was synthesized and subcloned into pET-28b."}]}],"last_modified_by":"bjuhasz","last_modified_name":"Bernadett Juhász","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-22T16:35:31.037Z"}},{"start":390,"end":433,"reference_id":"41043210","reference_source":"pmid","reference_html":"Structure and function of the keratin 17 tail domain associated with keratin intermediate filament organization. <i> Yeom J, Lee S, Ko YH, Hong E, Kim JH, Coulombe PA, Lee CH. </i> Eur J Cell Biol, 2025","date":"2026-06-19T13:55:06.421Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":"0009-0009-6028-6956","term_id":"GO:0005519","term_name":"cytoskeletal regulatory protein binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0001170","ec_ontology":"ECO","ec_name":"cross-linking evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IPI","interaction_partner":[{"db":"UniProt","id":"P50446","operator":null,"partner_start":null,"partner_end":null}],"region_id":"DP04593r003","sample":[{"term_id":"IDPO:00485","term_name":"interacting protein","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":null,"db":"UniProt","id":"P50446","statements":[{"type":"Results","text":"These results provide strong evidence that the K17 tail domain specifically interacts with the K6 rod domain, and this interaction is influenced by bundling-promoting buffer conditions."}]},{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":"not specified","value":null,"db":"ChEBI","id":"50684","statements":[{"type":"Methods","text":"Cross-linking assays were performed using disuccinimidyl suberate (DSS; S1885; Sigma-Aldrich). DSS was dissolved in DMSO and added at a 20-fold molar excess relative to the protein concentration. "}],"entry_name":null}],"statement":[{"text":"To test this hypothesis, we performed in vitro cross-linking experiments using the chemical cross-linker disuccinimidyl suberate (DSS) and Western blot using an antibody specific to the K17T sequence.","type":"Results"},{"text":"These results provide strong evidence that the K17 tail domain specifically interacts with the K6 rod domain, and this interaction is influenced by bundling-promoting buffer conditions.","type":"Results"}],"term_comment":"","term_def":"\"Binding to a protein involved in modulating the reorganization of the cytoskeleton.\" [GOC:go_curators, PMID:15163540]","term_is_obsolete":false,"term_not_annotate":false,"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-22T16:35:08.535Z"}}],"__v":0,"disorder_content":0.10161662817551963,"disprot_consensus":{"full":[{"start":390,"end":433,"type":"D"}],"Structural state":[{"start":390,"end":433,"type":"D"}],"Biological process":[{"start":404,"end":410,"type":"F"}],"Molecular function":[{"start":390,"end":433,"type":"F"}]}},{"acc":"Q73VY8","sequence":"MTASLLVANRGEIALRIIRTATELGMRTVAVYAADDAHSPHVHAADEAMPLPGSGPPAYLNQAALLAVAENTGATLIHPGYGFLSENAEFAKACAAASHTFVGPDGRVLELLGNKTAARRAAIAAGVPTLAATDGPSGVEDIEAFFAAHPGGIMIKALAGGGGRGMRKVHNAAQIAGAYQRCAAEARLGFGDPALFAEALLGDARHIEVQVVAAPAGHQTHALAVGDRDCSMQRRYQKLIEIAPAQGLSEELRRALHQAAVRLCARVGLRGLATVEFLVSGERFVFLEVNPRIQVEHTVTEQTTGLDLVAVQLAIAGGESYYRLGLPAGIASDGTEVIGEPAAQRGIAIQLRVNAETFGADFSVLPSAGTLTAFCPPSGPGVRVDTYGRPGLVVSPQYDSLLAKVIVAVHGSSWRAAMRKADTALSEFGVEGVATNIGFLRRLLAEQRLETGWVNTDFVDEKLPELAAAALTHQPGPQPGAVELYPGEDALRAQLAGTVVEVAPEGADYPAGAQLVVLEAMKMQHVLAAPDALRTVRVLVTPGQVVGTGDPLLVFTRTTGGDDGESETAATDLDLTRADLDEVIERHARTLDEGRPDAVAKRHRQGRRTARENIDDLVDPGSFVEYGALAIAAQRSRRSEEDLIANTPADGLVAGLATVGADRFGPAAAQAVVASYDYTVLAGTQGMRNHAKTDRVFDLAARKRLPVVLFAEGGGGRPGDTDVGGAAGLDVPTFRMLAGLRGRVPLVSVVSGRCFAGNAALAGVCDVIIATPDANIGMGGPAMIEGGGLGVYPPEAIGPIAVQRRNGVVGLVARDEAHAVSLAKQYLSYFQGRLDRWQAPDPRVARHVVPQNRLRAYDVHRAIEAIVDVGSVLELRPDYGVGIVTALVRVEGVPYGLIANSTHHLGGAIDAEAADKAGDFLALCESFGLPVISLCDTPGFMVGPDAETQAAVRRFGRMFVLGARLTVPLGMIILRKGYGLGAMAMAGGSFRAPQFTVAWPTGEIGGMGLESAVRLGYRKELAAVTDPAERQNLFDRLVAAAYQHGKALRAATTFELDDVIDPAASRAWITRLSGG","creator":"bjuhasz","dataset":[],"date":"2026-05-28T11:12:09.996Z","disprot_id":"DP04604","features":{"pfam":[{"id":"PF00289","name":"Biotin carboxylase, N-terminal domain","start":2,"end":108},{"id":"PF00364","name":"Biotin-requiring enzyme","start":506,"end":554},{"id":"PF01039","name":"Carboxyl transferase domain","start":602,"end":1068},{"id":"PF02785","name":"Biotin carboxylase C-terminal domain","start":350,"end":460},{"id":"PF02786","name":"Carbamoyl-phosphate synthase L chain, ATP binding domain","start":115,"end":320}]},"genes":[{"synonyms":[],"olnNames":[{"value":"MAP_2873c","_id":"6a18230a200fd5d2ef05aabe","evidences":[]}],"orfNames":[],"_id":"6a18230a200fd5d2ef05aabd"}],"length":1075,"name":"acetyl-CoA carboxylase","ncbi_taxon_id":262316,"organism":"Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)","regions_counter":5,"released":"2026_06","taxonomy":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Mycobacteriaceae","Mycobacterium","Mycobacterium avium complex (MAC)"],"regions":[{"start":471,"end":481,"reference_id":"25383525","reference_source":"pmid","reference_html":"Structure and function of a single-chain, multi-domain long-chain acyl-CoA carboxylase. <i> Tran TH, Hsiao YS, Jo J, Chou CY, Dietrich LE, Walz T, Tong L. </i> Nature, 2015","date":"2026-06-16T15:35:39.740Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":"0009-0009-6028-6956","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"4RCN"}],"region_id":"DP04604r001","statement":[{"text":"Therefore, there are two linkers from BCCP to the rest of the protein. The amino acid sequences of these two linkers in the LCC enzymes are not conserved (Extended Data Fig. 3). Therefore, they are likely to be flexible and allow the movement of BCCP during catalysis, consistent with the fact that a portion of both linkers is disordered in the structure (Fig. 1b).","type":"Results"},{"text":"In Extended Data Fig. 3 the boundaries of the linker are clearly labeled.","type":"Curator statement"},{"text":"The disordered region of the BCCP-CT linker is indicated with the dashed line (black).","type":"Figure"},{"text":"This region lacks electron density in the PDB structure, indicating it is disordered.","type":"Curator statement"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-16T15:37:25.086Z"}},{"start":559,"end":575,"reference_id":"25383525","reference_source":"pmid","reference_html":"Structure and function of a single-chain, multi-domain long-chain acyl-CoA carboxylase. <i> Tran TH, Hsiao YS, Jo J, Chou CY, Dietrich LE, Walz T, Tong L. </i> Nature, 2015","date":"2026-06-16T15:34:41.593Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":"0009-0009-6028-6956","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"4RCN"}],"region_id":"DP04604r002","statement":[{"text":"Therefore, there are two linkers from BCCP to the rest of the protein. The amino acid sequences of these two linkers in the LCC enzymes are not conserved (Extended Data Fig. 3). Therefore, they are likely to be flexible and allow the movement of BCCP during catalysis, consistent with the fact that a portion of both linkers is disordered in the structure (Fig. 1b).","type":"Results"},{"text":"In Extended Data Fig. 3 the boundaries of the linker are clearly labeled.","type":"Curator statement"},{"text":"This region lacks electron density in the PDB structure, indicating it is disordered.","type":"Curator statement"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-16T15:37:24.027Z"}},{"start":559,"end":575,"reference_id":"25383525","reference_source":"pmid","reference_html":"Structure and function of a single-chain, multi-domain long-chain acyl-CoA carboxylase. <i> Tran TH, Hsiao YS, Jo J, Chou CY, Dietrich LE, Walz T, Tong L. </i> Nature, 2015","date":"2026-06-16T15:36:22.865Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":"0009-0009-6028-6956","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"4RCN"}],"region_id":"DP04604r003","statement":[{"text":"Therefore, there are two linkers from BCCP to the rest of the protein. The amino acid sequences of these two linkers in the LCC enzymes are not conserved (Extended Data Fig. 3). Therefore, they are likely to be flexible and allow the movement of BCCP during catalysis, consistent with the fact that a portion of both linkers is disordered in the structure (Fig. 1b).","type":"Results"},{"text":"The BCCP domain, while not located in either active site, can readily access both of them, through conformational changes in its linkers.","type":"Results"},{"text":"Therefore, there are two linkers from BCCP to the rest of the protein. The amino acid sequences of these two linkers in the LCC enzymes are not conserved (Extended Data Fig. 3). Therefore, they are likely to be flexible and allow the movement of BCCP during catalysis, consistent with the fact that a portion of both linkers is disordered in the structure (Fig. 1b).","type":"Results"},{"text":"This region lacks electron density in the PDB structure, indicating it is disordered.","type":"Curator statement"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-16T15:37:27.171Z"}},{"start":471,"end":481,"reference_id":"25383525","reference_source":"pmid","reference_html":"Structure and function of a single-chain, multi-domain long-chain acyl-CoA carboxylase. <i> Tran TH, Hsiao YS, Jo J, Chou CY, Dietrich LE, Walz T, Tong L. </i> Nature, 2015","date":"2026-06-16T15:37:19.512Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":"0009-0009-6028-6956","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"4RCN"}],"region_id":"DP04604r004","statement":[{"text":"Therefore, there are two linkers from BCCP to the rest of the protein. The amino acid sequences of these two linkers in the LCC enzymes are not conserved (Extended Data Fig. 3). Therefore, they are likely to be flexible and allow the movement of BCCP during catalysis, consistent with the fact that a portion of both linkers is disordered in the structure (Fig. 1b).","type":"Results"},{"text":"The BCCP domain, while not located in either active site, can readily access both of them, through conformational changes in its linkers.","type":"Results"},{"text":"Therefore, there are two linkers from BCCP to the rest of the protein. The amino acid sequences of these two linkers in the LCC enzymes are not conserved (Extended Data Fig. 3). Therefore, they are likely to be flexible and allow the movement of BCCP during catalysis, consistent with the fact that a portion of both linkers is disordered in the structure (Fig. 1b).","type":"Results"},{"text":"This region lacks electron density in the PDB structure, indicating it is disordered.","type":"Curator statement"}],"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-16T15:37:26.113Z"}},{"start":171,"end":194,"reference_id":"25383525","reference_source":"pmid","reference_html":"Structure and function of a single-chain, multi-domain long-chain acyl-CoA carboxylase. <i> Tran TH, Hsiao YS, Jo J, Chou CY, Dietrich LE, Walz T, Tong L. </i> Nature, 2015","date":"2026-06-16T15:43:49.353Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0521","term_name":"his","term_namespace":"Tag","start":null,"end":null,"position":"C-terminal"}],"cross_refs":[{"db":"PDB","id":"4RCN"}],"region_id":"DP04604r005","statement":[{"text":"This region lacks electron density in the PDB structure, indicating it is disordered.","type":"Curator statement"}]}],"__v":0,"disorder_content":0.04837209302325581,"disprot_consensus":{"full":[{"start":171,"end":194,"type":"D"},{"start":471,"end":481,"type":"D"},{"start":559,"end":575,"type":"D"}],"Structural state":[{"start":171,"end":194,"type":"D"},{"start":471,"end":481,"type":"D"},{"start":559,"end":575,"type":"D"}],"Disorder function":[{"start":471,"end":481,"type":"F"},{"start":559,"end":575,"type":"F"}]}},{"acc":"P09651-2","sequence":"MSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKPRNQGGYGGSSSSSSYGSGRRF","alphafold_very_low_content":"NaN","creator":"bjuhasz","dataset":[],"date":"2026-05-28T15:12:02.720Z","disprot_id":"DP04605","features":{"pfam":[]},"genes":[{"name":{"value":"HNRNPA1","_id":"6a185b43cce615d745cf3f70","evidences":[]},"synonyms":[{"value":"HNRPA1","_id":"6a185b43cce615d745cf3f71","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"6a185b43cce615d745cf3f6f"}],"length":320,"name":"Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1","ncbi_taxon_id":9606,"organism":"Homo sapiens","regions_counter":13,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"],"regions":[{"start":296,"end":320,"reference_id":"37481159","reference_source":"pmid","reference_html":"Cryo-EM Structure of the Full-length hnRNPA1 Amyloid Fibril. <i> Sharma K, Banerjee S, Savran D, Rajes C, Wiese S, Girdhar A, Schwierz N, Lee C, Shorter J, Schmidt M, Guo L, Fändrich M. </i> J Mol Biol, 2023","date":"2026-06-01T10:17:42.372Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":"0009-0009-6028-6956","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"7ZJ2"},{"db":"EMDB","id":"EMD-14739"}],"region_id":"DP04605r001","statement":[{"text":"The LCD of recombinant and putatively monomeric hnRNPA1 protein is structurally flexible and lacks stable conformational elements [2,9]. ","type":"Abstract"},{"text":"Residues Met1 to Asp250 and Phe296 to Phe320 are not seen in our 3D map suggesting that these N- and C-terminal segments of the fibril protein are conformationally disordered. ","type":"Results"}],"last_modified_by":"bjuhasz","last_modified_name":"Bernadett Juhász","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-16T16:52:13.418Z"}},{"start":186,"end":250,"reference_id":"33311513","reference_source":"pmid","reference_html":"The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structure. <i> Sun Y, Zhao K, Xia W, Feng G, Gu J, Ma Y, Gui X, Zhang X, Fang Y, Sun B, Wang R, Liu C, Li D. </i> Nat Commun, 2020","date":"2026-06-16T16:16:31.567Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"7BX7"},{"db":"EMDB","id":"30235"}],"region_id":"DP04605r003","statement":[{"text":"Recombinant hnRNPA1 LC (residues 186–320) was incubated at 16 °C for 2 days to form amyloid fibrils (Fig. 1a). The fibrils were irreversible as warmed up to 25 °C for 30 min (Supplementary Fig. 1a).","type":"Results"},{"text":"Despite that the fibrils were formed by hnRNPA1 residues 186–320, only residues 251–295 were involved in the fibril core (Fig. 1d).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":296,"end":320,"reference_id":"33311513","reference_source":"pmid","reference_html":"The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structure. <i> Sun Y, Zhao K, Xia W, Feng G, Gu J, Ma Y, Gui X, Zhang X, Fang Y, Sun B, Wang R, Liu C, Li D. </i> Nat Commun, 2020","date":"2026-06-16T16:16:19.584Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006224","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04605r004","statement":[{"text":"Recombinant hnRNPA1 LC (residues 186–320) was incubated at 16 °C for 2 days to form amyloid fibrils (Fig. 1a). The fibrils were irreversible as warmed up to 25 °C for 30 min (Supplementary Fig. 1a).","type":"Results"},{"text":"Despite that the fibrils were formed by hnRNPA1 residues 186–320, only residues 251–295 were involved in the fibril core (Fig. 1d).","type":"Results"}],"cross_refs":[{"db":"PDB","id":"7BX7"},{"db":"EMDB","id":"30235"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":186,"end":320,"reference_id":"33311513","reference_source":"pmid","reference_html":"The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structure. <i> Sun Y, Zhao K, Xia W, Feng G, Gu J, Ma Y, Gui X, Zhang X, Fang Y, Sun B, Wang R, Liu C, Li D. </i> Nat Commun, 2020","date":"2026-06-16T16:11:30.690Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0000302","ec_ontology":"ECO","ec_name":"author statement used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04605r005","statement":[{"text":"Recombinant hnRNPA1 LC (residues 186–320) was incubated at 16 °C for 2 days to form amyloid fibrils (Fig. 1a). The fibrils were irreversible as warmed up to 25 °C for 30 min (Supplementary Fig. 1a).","type":"Results"},{"text":" HnRNPA1 contains two globular RNA recognition motifs (RRM1 and RRM2) for the specific binding with mRNA precursor, followed by an unstructured low complexity (LC) C-terminal domain. HnRNPA1 LC consists of a cluster of RGG repeats with interspersed aromatic residues and a nuclear localization sequence (termed PY-NLS)8–10. HnRNPA1 LC is intrinsically disordered and exhibits a characteristic feature of homogenous and heterogeneous supermolecular polymerization11–14.","type":"Introduction"},{"text":"The classification of this region as disordered is based on structural predictions from AlphaFold and MobiDB, combined with the authors' statements.","type":"Curator statement"}]},{"start":251,"end":295,"reference_id":"33311513","reference_source":"pmid","reference_html":"The nuclear localization sequence mediates hnRNPA1 amyloid fibril formation revealed by cryoEM structure. <i> Sun Y, Zhao K, Xia W, Feng G, Gu J, Ma Y, Gui X, Zhang X, Fang Y, Sun B, Wang R, Liu C, Li D. </i> Nat Commun, 2020","date":"2026-06-16T16:15:49.750Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0006208","ec_ontology":"ECO","ec_name":"cryogenic electron microscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"°C","unit_id":"UO:0000027","deviation":null,"value":16}],"cross_refs":[{"db":"EMDB","id":"30235"}],"ec_go":"IDA","region_id":"DP04605r006","statement":[{"text":"Recombinant hnRNPA1 LC (residues 186–320) was incubated at 16 °C for 2 days to form amyloid fibrils (Fig. 1a). The fibrils were irreversible as warmed up to 25 °C for 30 min (Supplementary Fig. 1a).","type":"Results"},{"text":"The density map showed two protofilaments intertwining along an approximate twofold screw axis to form a left-handed helix with a width of ~7 nm and a half pitch of ~45 nm (Fig. 1c).","type":"Results"},{"text":"Based on the high-resolution cryoEM density map, we were able to unambiguously build an atomic structure model for hnRNPA1 LC fibril (Fig. 1d). Despite that the fibrils were formed by hnRNPA1 residues 186–320, only residues 251–295 were involved in the fibril core (Fig. 1d).","type":"Results"},{"text":"PY-NLS is structurally disordered in free hnRNPA1. In the complex with Kapβ2, residues 263–289 of PY-NLS form an extended conformation to line in the C-terminal arch of Kapβ28 (Fig. 4a, b). Strikingly, upon amyloid fibril formation, this same region forms the main part of fibril core (Fig. 4a, c).","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false},{"start":92,"end":102,"reference_id":"11917013","reference_source":"pmid","reference_html":"Correlated alternative side chain conformations in the RNA-recognition motif of heterogeneous nuclear ribonucleoprotein A1. <i> Vitali J, Ding J, Jiang J, Zhang Y, Krainer AR, Xu RM. </i> Nucleic Acids Res, 2002","date":"2026-06-16T16:22:54.280Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04605r007","statement":[{"text":"Three regions were not modeled because of poor electron density: the first seven residues at the N-terminus, the last 16 residues at the C-terminus and the internal linker residues Arg92–Leu102. These regions were disordered in the original 1.75 and 1.9 Å structures (35,36) and they remained uninterpretable even in the present high resolution analysis.","type":"Results"}]},{"start":182,"end":196,"reference_id":"11917013","reference_source":"pmid","reference_html":"Correlated alternative side chain conformations in the RNA-recognition motif of heterogeneous nuclear ribonucleoprotein A1. <i> Vitali J, Ding J, Jiang J, Zhang Y, Krainer AR, Xu RM. </i> Nucleic Acids Res, 2002","date":"2026-06-16T16:23:08.931Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04605r008","statement":[{"text":"Three regions were not modeled because of poor electron density: the first seven residues at the N-terminus, the last 16 residues at the C-terminus and the internal linker residues Arg92–Leu102. These regions were disordered in the original 1.75 and 1.9 Å structures (35,36) and they remained uninterpretable even in the present high resolution analysis.","type":"Results"}]},{"start":92,"end":102,"reference_id":"11917013","reference_source":"pmid","reference_html":"Correlated alternative side chain conformations in the RNA-recognition motif of heterogeneous nuclear ribonucleoprotein A1. <i> Vitali J, Ding J, Jiang J, Zhang Y, Krainer AR, Xu RM. </i> Nucleic Acids Res, 2002","date":"2026-06-16T16:23:39.654Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04605r009","statement":[{"text":"Three regions were not modeled because of poor electron density: the first seven residues at the N-terminus, the last 16 residues at the C-terminus and the internal linker residues Arg92–Leu102. These regions were disordered in the original 1.75 and 1.9 Å structures (35,36) and they remained uninterpretable even in the present high resolution analysis.","type":"Results"}]},{"start":92,"end":102,"reference_id":"10323862","reference_source":"pmid","reference_html":"Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA. <i> Ding J, Hayashi MK, Zhang Y, Manche L, Krainer AR, Xu RM. </i> Genes Dev, 1999","date":"2026-06-16T16:30:24.277Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000011","term_name":"disorder to order","term_namespace":"Structural transition","disprot_namespace":"Structural transition","term_ontology":"IDPO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04605r010","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Introduction","text":"We report here the crystal structure of the amino-terminal UP1 domain of hnRNP A1 complexed with human telomeric ssDNA repeats, d(TTAGGG)2, at 2.1 Å resolution."}]}],"statement":[{"text":"Second, the linker connecting the two RRMs becomes ordered on TR2 binding (Fig. 2A). Third, the region near the carboxyl terminus of UP1 (Lys-183–Ser-190), which was disordered in the absence of DNA, also becomes ordered in the presence of DNA and forms an α-helix (Fig. 2A).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"},{"start":92,"end":102,"reference_id":"10323862","reference_source":"pmid","reference_html":"Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA. <i> Ding J, Hayashi MK, Zhang Y, Manche L, Krainer AR, Xu RM. </i> Genes Dev, 1999","date":"2026-06-16T16:35:06.408Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0042162","term_name":"telomeric DNA binding","term_namespace":"Molecular function","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"EXP","region_id":"DP04605r011","sample":[{"term_id":"IDPO:00487","term_name":"interacting nucleic acid","unit_name":"µg","unit_id":"UO:0000023","deviation":null,"value":null,"db":null,"id":null,"statements":[{"type":"Introduction","text":"We report here the crystal structure of the amino-terminal UP1 domain of hnRNP A1 complexed with human telomeric ssDNA repeats, d(TTAGGG)2, at 2.1 Å resolution."}]}],"statement":[{"text":"Second, the linker connecting the two RRMs becomes ordered on TR2 binding (Fig. 2A). Third, the region near the carboxyl terminus of UP1 (Lys-183–Ser-190), which was disordered in the absence of DNA, also becomes ordered in the presence of DNA and forms an α-helix (Fig. 2A).","type":"Results"},{"text":"Arg-92 makes contacts with three bases, Gua-4, Gua-5, and Thy-7, and the guanidino moiety is locked between the three bases (Figs. 4 and 5A). Ser-95 makes a hydrogen bond with the N2 atom of Gua-4. The imidazole ring of His-101 stacks with the purine ring of Ade-3, which is sandwiched between His-101 and Phe-17.","type":"Results"},{"text":"The present structure demonstrates the direct involvement of the linker segment in both protein–protein and protein–ssDNA interactions. Several residues located within this region contact ssDNA directly (Fig. 4).","type":"Discussion"},{"text":"We report here the crystal structure of the amino-terminal UP1 domain of hnRNP A1 complexed with human telomeric ssDNA repeats, d(TTAGGG)2, at 2.1 Å resolution.","type":"Introduction"}],"term_comment":"","term_def":"\"Binding to a telomere, a specific structure at the end of a linear chromosome required for the integrity and maintenance of the end.\" [GOC:jl, SO:0000624]","term_is_obsolete":false,"term_not_annotate":false},{"start":209,"end":217,"reference_id":"31043593","reference_source":"pmid","reference_html":"Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly. <i> Gui X, Luo F, Li Y, Zhou H, Qin Z, Liu Z, Gu J, Xie M, Zhao K, Dai B, Shin WS, He J, He L, Jiang L, Zhao M, Sun B, Li X, Liu C, Li D. </i> Nat Commun, 2019","date":"2026-06-16T16:48:26.586Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0007044","ec_ontology":"ECO","ec_name":"transmission electron microscopy evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"ec_go":"IDA","region_id":"DP04605r012","statement":[{"text":"To identify the reversible amyloid core (RAC) of hnRNPA1, we synthesized a series of segments selected from the LC domain with different lengths from 5 to 12 residues. The segments contain [S/G]Y/F[S/G] and/or RGG motifs that are characteristic in LC21,25–27 (Supplementary Fig. 4). The segments were screened for reversible amyloid formation. The result showed that segment 209GFGGNDNFG217 (named hnRAC1), but not the others, formed hydrogel at 4 °C. The hydrogel was composed of amyloid fibrils observed by TEM (Fig. 2a).","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false},{"start":209,"end":217,"reference_id":"31043593","reference_source":"pmid","reference_html":"Structural basis for reversible amyloids of hnRNPA1 elucidates their role in stress granule assembly. <i> Gui X, Luo F, Li Y, Zhou H, Qin Z, Liu Z, Gu J, Xie M, Zhao K, Dai B, Shin WS, He J, He L, Jiang L, Zhao M, Sun B, Li X, Liu C, Li D. </i> Nat Commun, 2019","date":"2026-06-16T16:51:15.360Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:1990000","term_name":"amyloid fibril formation","term_namespace":"Biological process","disprot_namespace":"Disorder function","term_ontology":"GO","ec_id":"ECO:0005670","ec_ontology":"ECO","ec_name":"x-ray crystallography evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"5ZGD"},{"db":"PDB","id":"6J60"}],"ec_go":"EXP","region_id":"DP04605r013","statement":[{"text":"The structure revealed a cross-β architecture (or steric zipper18) with hydrophilic sheet interface composed by N213 and N215 (Fig. 3b).","type":"Results"},{"text":"Moreover, the hnRAC1 structure exhibits a distinct feature of negatively charged D214 continuously stacking along the parallel in-register β-sheets (Fig. 3b).","type":"Results"}],"term_comment":"Although deposition of amyloid fibrils is associated with diseases, e.g. Alzheimer's disease, amyloid formation is a normal process. Disease occurs when the balance between amyloid formation and clearance is disrupted (reviewed e.g. in PMID:29654159 and PMID:28937655). An example of a normal amyloid complex is composed of human RIP1 and RIP3 kinases  (PMID:22817896).","term_def":"\"The generation of amyloid fibrils, insoluble fibrous protein aggregates exhibiting beta sheet structure, from proteins.\" [GOC:cvs, GOC:jj, GOC:ppm, GOC:sj, PMID:21148556, PMID:22817896, PMID:28937655, PMID:29654159]","term_is_obsolete":false,"term_not_annotate":false,"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes"}],"__v":0,"disorder_content":0.46875,"disprot_consensus":{"full":[{"start":92,"end":102,"type":"T"},{"start":182,"end":320,"type":"D"}],"Structural state":[{"start":92,"end":102,"type":"D"},{"start":182,"end":320,"type":"D"}],"Biological process":[{"start":209,"end":217,"type":"F"},{"start":251,"end":295,"type":"F"}],"Disorder function":[{"start":92,"end":102,"type":"F"}],"Structural transition":[{"start":92,"end":102,"type":"T"}],"Molecular function":[{"start":92,"end":102,"type":"F"}]}},{"acc":"Q62871-3","sequence":"MSDKSELKAELERKKQRLAQIREEKKRKEEERKKKETDQKKEAAVSVQEESDLEKKRREAEALLQSMGLTTDSPIVPPPMSPSSKSVSTPSEAGSQDSGDGAVGSRRGPIKLGMAKITQVDFPPREIVTYTKETQTPVTAQPKEDEEEEDDVAAPKPPVEPEEEKILKKDEENDSKAPPHELTEEEKQQILHSEEFLSFFDHSTRIVERALSEQINIFFDYSGRDLEDKEGEIQAGAKLSLNRQFFDERWSKHRVVSCLDWSSQYPELLVASYNNNEEAPHEPDGVALVWNMKYKKTTPEYVFHCQSAVMSATFAKFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLISISTDGKICSWSLDMLSHPQDSMELVHKQSKAVAVTSMSFPVGDVNNFVVGSEEGSVYTACRHGSKAGISEMFEGHQGPITGIHCHAAVGAVDFSHLFVTSSFDWTVKLWSTKNNKPLYSFEDNSDYVYDVIGSPTHPALFACVDGMGRLDLWNLNNDTEVPTASISVEGNPALNRVRWTHSGREIAVGDSEGQIVIYDVGEQIAVPRNDEWARFGRTLAEINASRADAEEEAATRIPA","alphafold_very_low_content":"NaN","creator":"bjuhasz","dataset":[],"date":"2026-05-29T12:41:50.300Z","disprot_id":"DP04607","features":{"pfam":[]},"genes":[{"name":{"value":"Dync1i2","_id":"6a19898ecce615d745cf3fc1","evidences":[]},"synonyms":[{"value":"Dnci2","_id":"6a19898ecce615d745cf3fc2","evidences":[]},{"value":"Dncic2","_id":"6a19898ecce615d745cf3fc3","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"6a19898ecce615d745cf3fc0"}],"length":612,"name":"Isoform 2C of Cytoplasmic dynein 1 intermediate chain 2","ncbi_taxon_id":10116,"organism":"Rattus norvegicus","regions_counter":3,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Rattus"],"regions":[{"start":67,"end":96,"reference_id":"40782957","reference_source":"pmid","reference_html":"NMR Approaches to Identify Transient Structure and Interactions of Intrinsically Disordered Dynein Intermediate Chain. <i> Loening NM, Jara KA, Barbar EJ. </i> J Mol Biol, 2025","date":"2026-06-15T17:55:22.041Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":"0009-0009-6028-6956","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"MI:0381","term_name":"2H label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":" For deuterated IC-2C1–96, Rosetta(DE3) Escherichia coli cells (Merck KGaA, Darmstadt, Germany) transformed with plasmid for IC-2C1–96 were grown in Luria broth prepared in 99.9% D2O overnight."}]}],"region_id":"DP04607r001","statement":[{"text":"The disordered L2 region shows only modest decreases in peak heights as it is dynamic enough to experience motional averaging, even when a 1:1 ratio of the proteins is achieved.","type":"Results"},{"text":"In addition, with the MTSL label located in the intrinsically disordered L2 region (A93C), a very small increase in the PRE values in the middle of the SAH region was observed, indicating a lowfrequency, transient interaction between those parts of IC-2C.","type":"Discussion"},{"text":"The region schematic in the same figure places L2 after H2 ending at ~66, so this is approximately 66–96.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-15T17:56:18.099Z"}},{"start":39,"end":51,"reference_id":"40782957","reference_source":"pmid","reference_html":"NMR Approaches to Identify Transient Structure and Interactions of Intrinsically Disordered Dynein Intermediate Chain. <i> Loening NM, Jara KA, Barbar EJ. </i> J Mol Biol, 2025","date":"2026-06-15T17:55:02.789Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":"0009-0009-6028-6956","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"MI:0381","term_name":"2H label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":" For deuterated IC-2C1–96, Rosetta(DE3) Escherichia coli cells (Merck KGaA, Darmstadt, Germany) transformed with plasmid for IC-2C1–96 were grown in Luria broth prepared in 99.9% D2O overnight."}]}],"region_id":"DP04607r002","statement":[{"text":"Here, we focus on the p150Glued and NudE/Nudel binding domain of IC, which contains the SAH region of approximately 35 residues and a shorter helix of approximately 10 residues (H2) that is separated from the SAH region by a disordered linker (L1).","type":"Discussion"},{"text":"In contrast, the signals for the L1 region decrease despite its intrinsic disorder because its tethering to the structured SAH and H2 regions limits it motion in the bound complex, resulting in signal decreases that match those observed for the H2 region.","type":"Results"},{"text":"The region schematic in the same figure places L1 between the SAH ending at ~38 and H2 starting at ~52, so this is approximately 39–51.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-15T17:56:23.058Z"}},{"start":39,"end":51,"reference_id":"40782957","reference_source":"pmid","reference_html":"NMR Approaches to Identify Transient Structure and Interactions of Intrinsically Disordered Dynein Intermediate Chain. <i> Loening NM, Jara KA, Barbar EJ. </i> J Mol Biol, 2025","date":"2026-06-15T17:55:11.398Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":"0009-0009-6028-6956","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0001238","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":1,"construct_alterations":[{"term_id":"MI:0381","term_name":"2H label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":" For deuterated IC-2C1–96, Rosetta(DE3) Escherichia coli cells (Merck KGaA, Darmstadt, Germany) transformed with plasmid for IC-2C1–96 were grown in Luria broth prepared in 99.9% D2O overnight."}]}],"region_id":"DP04607r003","statement":[{"text":"In contrast, when the MTSL label was located at residue 44 in the intrinsically disordered linker region (L1), a somewhat larger range of residues were affected as the lack of structure and presence of dynamics allowed more residues to come into close contact with the paramagnetic tag.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-15T17:56:19.145Z"}}],"__v":0,"disorder_content":0.07026143790849673,"disprot_consensus":{"full":[{"start":39,"end":51,"type":"D"},{"start":67,"end":96,"type":"D"}],"Structural state":[{"start":39,"end":51,"type":"D"},{"start":67,"end":96,"type":"D"}],"Disorder function":[{"start":39,"end":51,"type":"F"}]}},{"acc":"Q9Z2B5","sequence":"MERATRPGPRALLLLLFLLLGCAAGISAVAPARSLLAPASETVFGLGAAAAPTSAARVPAVATAEVTVEDAEALPAAAGEPESRATEPDDDVELRPRGRSLVIISTLDGRIAALDAENDGKKQWDLDVGSGSLVSSSLSKPEVFGNKMIIPSLDGDLFQWDRDRESMEAVPFTVESLLESSYKFGDDVVLVGGKSLITYGLSAYSGKLRYICSALGCRRWDSDEMEEEEDILLLQRTQKTVRAVGPRSGSEKWNFSVGHFELRYIPDMETRAGFIESTFKPGGNKEDSKIISDVEEQEATMLDTVIKVSVADWKVMAFSRKGGRLEWEYQFCTPIASAWLVRDGKVIPISLFDDTSYTASEEALGDEEDIVEAARGATENSVYLGMYRGQLYLQSSVRVSEKFPTSPKALESVNGENAIIPLPTIKWKPLIHSPSRTPVLVGSDEFDKCLSNDKYSHEEYSNGALSILQYPYDNGYYLPYYKRERNKRSTQITVRFLDSPHYSKNIRKKDPILLLHWWKEIFGTILLCIVATTFIVRRLFHPQPHRQRKESETQCQTESKYDSVSADVSDNSWNDMKYSGYVSRYLTDFEPIQCMGRGGFGVVFEAKNKVDDCNYAIKRIRLPNRELAREKVMREVKALAKLEHPGIVRYFNAWLETPPEKWQEEMDEIWLKDESTDWPLSSPSPMDAPSVKIRRMDPFSTKEQIEVIAPSPERSRSFSVGISCGQTSSSESQFSPLEFSGTDCGDNSDSADAAYNLQDSCLTDCEDVEDGTVDGNDEGHSFELCPSEASPYTRSREGTSSSIVFEDSGCGNASSKEEPRGNRLHDGNHYVNKLTDLKCSSSRSSSEATTLSTSPTRPTTLSLDFTKNTVGQLQPSSPKVYLYIQMQLCRKENLKDWMNRRCSLEDREHGVCLHIFLQIAEAVEFLHSKGLMHRDLKPSNIFFTMDDVVKVGDFGLVTAMDQDEEEQTVLTPMPAYATHTGQVGTKLYMSPEQIHGNNYSHKVDIFSLGLILFELLYPFSTQMERVRILTDVRNLKFPLLFTQKYPQEHMMVQDMLSPSPTERPEATDIIENAIFENLEFPGKTVLRQRSRSMSSSGTKHSRQPSCSYSPLPGN","alphafold_very_low_content":"NaN","creator":"xcastro","dataset":["Stress response proteins"],"date":"2026-06-01T08:27:32.707Z","disprot_id":"DP04609","features":{"pfam":[{"id":"PF00069","name":"Protein kinase domain","start":590,"end":656},{"id":"PF00069","name":"Protein kinase domain","start":878,"end":1072}]},"genes":[{"name":{"value":"Eif2ak3","evidences":[{"source":{"id":"MGI:1341830","name":"MGI","url":"http://www.informatics.jax.org/marker/MGI:1341830","_id":"6a1d4275cce615d745cf4055"},"code":"ECO:0000312","_id":"6a1d4275cce615d745cf4054"}],"_id":"6a1d4275cce615d745cf4053"},"synonyms":[{"value":"Pek","_id":"6a1d4275cce615d745cf4056","evidences":[]},{"value":"Perk","_id":"6a1d4275cce615d745cf4057","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"6a1d4275cce615d745cf4052"}],"length":1114,"name":"Eukaryotic translation initiation factor 2-alpha kinase 3","ncbi_taxon_id":10090,"organism":"Mus musculus","regions_counter":5,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"regions":[{"start":964,"end":977,"reference_id":"21543844","reference_source":"pmid","reference_html":"The structure of the PERK kinase domain suggests the mechanism for its activation. <i> Cui W, Li J, Ron D, Sha B. </i> Acta Crystallogr D Biol Crystallogr, 2011","date":"2026-06-01T08:55:54.245Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Lys702_Thr866del","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"To reveal the structure of mPERK KD, we cloned the mPERK fragment Arg584–Asn1114 with the deletion of the large heavily phosphorylated N-terminal kinase insert loop (Lys702–Thr866)."}]}],"cross_refs":[{"db":"PDB","id":"3QD2"}],"region_id":"DP04609r001","statement":[{"text":"15 residues (residues 964–977 and 984) in the activation loop are not visible in the electron-density map. This means the activation loop is still partially disordered. 36 residues at the C-terminus of mPERK KD are also missing in the structure that we have determined.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-24T17:47:34.292Z"}},{"start":1079,"end":1114,"reference_id":"21543844","reference_source":"pmid","reference_html":"The structure of the PERK kinase domain suggests the mechanism for its activation. <i> Cui W, Li J, Ron D, Sha B. </i> Acta Crystallogr D Biol Crystallogr, 2011","date":"2026-06-01T08:57:06.524Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00481","term_name":"deletion","term_namespace":"Protein mutation","value":"p.Lys702_Thr866del","start":null,"end":null,"position":null,"statements":[{"type":"Methods","text":"To reveal the structure of mPERK KD, we cloned the mPERK fragment Arg584–Asn1114 with the deletion of the large heavily phosphorylated N-terminal kinase insert loop (Lys702–Thr866)."}]}],"cross_refs":[{"db":"PDB","id":"3QD2"}],"region_id":"DP04609r002","statement":[{"text":"15 residues (residues 964–977 and 984) in the activation loop are not visible in the electron-density map. This means the activation loop is still partially disordered. 36 residues at the C-terminus of mPERK KD are also missing in the structure that we have determined.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-24T17:47:34.024Z"}},{"start":140,"end":186,"reference_id":"25925385","reference_source":"pmid","reference_html":"Crystal structures reveal transient PERK luminal domain tetramerization in endoplasmic reticulum stress signaling. <i> Carrara M, Prischi F, Nowak PR, Ali MM. </i> EMBO J, 2015","date":"2026-06-01T13:12:06.819Z","curator_id":"xcastro","curator_name":"Ximena Aixa Castro","curator_orcid":"0000-0002-9211-1255","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"4YZY"}],"region_id":"DP04609r003","sequence_construct":"ASLVIISTLDGRIAALDAENDGKKQWDLDVGSGSLVSSSLSKPEVFGNKMIIPSLDGDLFQWDRDRESMEAVPFTVESLLESSYKFGDDVVLVGGKSLTTYGLSAYSGKLRYICSALGCRRWDSDEMEEEEDILLLQRTQKTVRAVGPRSGSEKWNFSVGHFELRYIPDMETRAGFIESTFKPGGNKEDSKIISDVEEQEATMLDTVIKVSVADWKVMAFSRKGGRLEWEYQFCTPIASAWLVRDGKVIPISLFDDTSYTASEEALGDEEDIVEAARGATENSVYLGMYRGQLYLQSSVRV","statement":[{"text":"The only significant difference between the mouse and human monomer is that in the mouse structure, the tetramer subdomain is disordered.","type":"Results"},{"text":"B. Mouse PERK monomer organized into three subdomains with dimerization domain in red and β‐sandwich domain in blue. The tetramer subdomain is disordered and is not visible within the structure.","type":"Figure"},{"text":"Manual inspection of the structure locates the tetramer subdomain in the region 140-186.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-24T17:47:39.148Z"}},{"start":267,"end":301,"reference_id":"25925385","reference_source":"pmid","reference_html":"Crystal structures reveal transient PERK luminal domain tetramerization in endoplasmic reticulum stress signaling. <i> Carrara M, Prischi F, Nowak PR, Ali MM. </i> EMBO J, 2015","date":"2026-06-24T17:32:23.615Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"4YZY"}],"region_id":"DP04609r004","statement":[{"text":"The PDB-deposited data indicate that this region lacks electron density. As it appears to be part of the analyzed sample, the absence of electron density is likely due to its disordered nature, consistent with predicted data.","type":"Curator statement"}]},{"start":702,"end":866,"reference_id":"21543844","reference_source":"pmid","reference_html":"The structure of the PERK kinase domain suggests the mechanism for its activation. <i> Cui W, Li J, Ron D, Sha B. </i> Acta Crystallogr D Biol Crystallogr, 2011","date":"2026-06-24T17:54:43.921Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0008035","ec_ontology":"ECO","ec_name":"author inference based on intrinsic disorder prediction used in manual assertion","unpublished":true,"released":"2026_06","version":0,"region_id":"DP04609r005","statement":[{"text":"To reveal the structure of mPERK KD, we cloned the mPERK fragment Arg584–Asn1114 with the deletion of the large heavily phosphorylated N-terminal kinase insert loop (Lys702–Thr866). A similar deletion was performed in the crystallographic studies of PKR and GCN2 to facilitate crystallization because this segment is highly disordered.","type":"Results"},{"text":"The region is additionally predicted to be disordered by AlphaFold and MobiDB-lite.","type":"Curator statement"}]}],"__v":0,"disorder_content":0.2666068222621185,"disprot_consensus":{"full":[{"start":140,"end":186,"type":"D"},{"start":267,"end":301,"type":"D"},{"start":702,"end":866,"type":"D"},{"start":964,"end":977,"type":"D"},{"start":1079,"end":1114,"type":"D"}],"Structural state":[{"start":140,"end":186,"type":"D"},{"start":267,"end":301,"type":"D"},{"start":702,"end":866,"type":"D"},{"start":964,"end":977,"type":"D"},{"start":1079,"end":1114,"type":"D"}]}},{"acc":"Q2FZ56","sequence":"MRGETLKLKKDKRREAIRQQIDSNPFITDHELSDLFQVSIQTIRLDRTYLNIPELRKRIKLVAEKNYDQISSIEEQEFIGDLIQVNPNVKAQSILDITSDSVFHKTGIARGHVLFAQANSLCVALIKQPTVLTHESSIQFIEKVKLNDTVRAEARVVNQTAKHYYVEVKSYVKHTLVFKGNFKMFYDKRG","alphafold_very_low_content":"NaN","creator":"gerdos","dataset":[],"date":"2026-06-01T11:55:41.858Z","disprot_id":"DP04615","features":{"pfam":[{"id":"PF03061","name":"Thioesterase superfamily","start":116,"end":169}]},"genes":[{"name":{"value":"fapR","evidences":[{"source":{"id":"MF_01814","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_01814","_id":"6a1d733ecce615d745cf40e5"},"code":"ECO:0000256","_id":"6a1d733ecce615d745cf40e4"}],"_id":"6a1d733ecce615d745cf40e3"},"synonyms":[],"olnNames":[{"value":"SAOUHSC_01196","_id":"6a1d733ecce615d745cf40e6","evidences":[]}],"orfNames":[],"_id":"6a1d733ecce615d745cf40e2"}],"length":190,"name":"Transcription factor FapR","ncbi_taxon_id":93061,"organism":"Staphylococcus aureus (strain NCTC 8325 / PS 47)","regions_counter":1,"released":"2026_06","taxonomy":["Bacteria","Bacillati","Bacillota","Bacilli","Bacillales","Staphylococcaceae","Staphylococcus"],"regions":[{"start":1,"end":71,"reference_id":"23300457","reference_source":"pmid","reference_html":"Structural basis for feed-forward transcriptional regulation of membrane lipid homeostasis in Staphylococcus aureus. <i> Albanesi D, Reh G, Guerin ME, Schaeffer F, Debarbouille M, Buschiazzo A, Schujman GE, de Mendoza D, Alzari PM. </i> PLoS Pathog, 2013","date":"2026-06-12T17:47:34.475Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"4A0Y"}],"region_id":"DP04615r001","statement":[{"text":"However, the helix-turn-helix motifs display high temperature factors or even partial disorder, and are engaged in extensive crystal contacts, suggesting the coexistence of alternative conformational states in solution characterized by flexible DBDs. In that sense, in one protomer of the crystal form 2 (Table 1) both helix αL and its associated DBD are highly flexible and could not be modeled, suggesting a marginal stability of the observed quaternary arrangement. Moreover, the first visible residues of this same monomer (positions 72–77, connecting helix αL with the first β-strand of the EBD) adopt a conformation that differs from that observed in the other ligand-free or malonyl-CoA-bound protomers, but resembles that found for one subunit of the asymmetric DNA-bound form of the repressor (Fig. 4B).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-12T17:47:39.896Z"}}],"__v":0,"disorder_content":0.3736842105263158,"disprot_consensus":{"full":[{"start":1,"end":71,"type":"D"}],"Structural state":[{"start":1,"end":71,"type":"D"}]}},{"acc":"O64527","sequence":"MNQLQQLQNPGESPPVHPFVAPLSYLLGTWRGQGEGEYPTIPSFRYGEEIRFSHSGKPVIAYTQKTWKLESGAPMHAESGYFRPRPDGSIEVVIAQSTGLVEVQKGTYNVDEQSIKLKSDLVGNASKVKEISREFELVDGKLSYVVRMSTTTNPLQPHLKAILDKL","alphafold_very_low_content":"NaN","creator":"gerdos","dataset":[],"date":"2026-06-01T12:46:56.232Z","disprot_id":"DP04619","features":{"pfam":[{"id":"PF08768","name":"THAP4-like, heme-binding beta-barrel domain","start":20,"end":165}]},"genes":[{"synonyms":[],"olnNames":[{"value":"At1g79260","_id":"6a1d7f40cce615d745cf4129","evidences":[]}],"orfNames":[{"value":"YUP8H12R.14","_id":"6a1d7f40cce615d745cf412a","evidences":[]}],"_id":"6a1d7f40cce615d745cf4128"}],"length":166,"name":"Peroxynitrite isomerase Rv2717c","ncbi_taxon_id":3702,"organism":"Arabidopsis thaliana","regions_counter":2,"released":"2026_06","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"regions":[{"start":1,"end":13,"reference_id":"19938152","reference_source":"pmid","reference_html":"The structure and NO binding properties of the nitrophorin-like heme-binding protein from Arabidopsis thaliana gene locus At1g79260.1. <i> Bianchetti CM, Blouin GC, Bitto E, Olson JS, Phillips GN. </i> Proteins, 2010","date":"2026-06-01T12:47:50.464Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"2A13"}],"region_id":"DP04619r001","statement":[{"text":"In both the apo and heme-bound nitrobindin structures well-defined electron density was observed for residues 14–166. Electron density was lacking for the N-terminal residues 1–13, presumably resulting from intrinsic disorder.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-11T14:02:25.385Z"}},{"start":1,"end":13,"reference_id":"19938152","reference_source":"pmid","reference_html":"The structure and NO binding properties of the nitrophorin-like heme-binding protein from Arabidopsis thaliana gene locus At1g79260.1. <i> Bianchetti CM, Blouin GC, Bitto E, Olson JS, Phillips GN. </i> Proteins, 2010","date":"2026-06-11T14:02:22.480Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"2A13"}],"region_id":"DP04619r002","statement":[{"text":"In both the apo and heme-bound nitrobindin structures well-defined electron density was observed for residues 14–166. Electron density was lacking for the N-terminal residues 1–13, presumably resulting from intrinsic disorder.","type":"Results"}]}],"__v":0,"disorder_content":0.0783132530120482,"disprot_consensus":{"full":[{"start":1,"end":13,"type":"D"}],"Structural state":[{"start":1,"end":13,"type":"D"}],"Disorder function":[{"start":1,"end":13,"type":"F"}]}},{"acc":"P27318","sequence":"MENKIVASTKEEFNTWYKQFAEKHKLNNKYTESASFCAEIPQLDTYKYKMELASTDNERDAIYSSALIEATRFCAPIMECAWASCTGTVKRGLEWFDKNKDSDTVKVWDANYQKLRTETPPAEALLAYQKAALNWRKDVGFSIGEYTSILKKAVAAEYKVPGTVINNIKEMLSDMIRRRNRIINGGSDDAPKRGPVGREHLDWCREFASGKFLNAFNPPWGEINKAGKSGYPLLATGLAKLVELEGKDVMDKAKASIAQLEGWVKENKDQVDQDKAEDLLKGVRESYKTALALAKLSNAFRAQGAQIDTVFSSYYWPWKAGVTPVTFPSVSQFLFELGKNPKGQKKMQKALINTPLKWGKRLIELFADNDFTENRIYMHPCVLTSGRMSELGISFGAVPVTSPDDAAQGSGHTKAVLNYKTKTEVGNPCACIISSLFEIQKAGYDIESMDIVASEHLLHQSLVGKRSPFQNAYLIKGNATNINII","creator":"gerdos","dataset":["Viral proteins","RNA-binding proteins"],"date":"2026-06-02T11:24:30.840Z","disprot_id":"DP04643","features":{"pfam":[{"id":"PF02477","name":"Nucleocapsid N protein","start":1,"end":444}]},"genes":[{"name":{"value":"N","_id":"6a1ebd6ecce615d745cf42fd","evidences":[]},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"6a1ebd6ecce615d745cf42fc"}],"length":485,"name":"Nucleoprotein","ncbi_taxon_id":11597,"organism":"Hazara virus (isolate JC280)","regions_counter":2,"released":"2026_06","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Polyploviricotina","Bunyaviricetes","Hareavirales","Nairoviridae","Orthonairovirus","Orthonairovirus hazaraense"],"regions":[{"start":187,"end":196,"reference_id":"26715309","reference_source":"pmid","reference_html":"The crystal structure of the Hazara virus nucleocapsid protein. <i> Surtees R, Ariza A, Punch EK, Trinh CH, Dowall SD, Hewson R, Hiscox JA, Barr JN, Edwards TA. </i> BMC Struct Biol, 2015","date":"2026-06-11T15:11:34.029Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"5A97"}],"region_id":"DP04643r001","statement":[{"text":"In each of the four HAZV N monomers in the AU, only 475 amino acid residues were built into the model; residues 187–196 are missing in the electron density and are thought to form a disordered loop that links the arm domain to the N terminus of the globular domain.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu296Gln","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro317Leu","start":null,"end":null,"position":null}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-11T15:11:38.346Z"}},{"start":187,"end":196,"reference_id":"26715309","reference_source":"pmid","reference_html":"The crystal structure of the Hazara virus nucleocapsid protein. <i> Surtees R, Ariza A, Punch EK, Trinh CH, Dowall SD, Hewson R, Hiscox JA, Barr JN, Edwards TA. </i> BMC Struct Biol, 2015","date":"2026-06-11T15:12:05.515Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000033","term_name":"flexible linker","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Leu296Gln","start":null,"end":null,"position":null},{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Pro317Leu","start":null,"end":null,"position":null}],"cross_refs":[{"db":"PDB","id":"5A97"}],"region_id":"DP04643r002","statement":[{"text":"A single alpha helix (helix α13) provides the only link visible in this model between the arm domain and the globular domain, as the loop linking the N-terminus of the globular domain to the arm domain (residues 187–196) is not visible in the electron density and is presumed disordered.","type":"Results"}]}],"__v":0,"disorder_content":0.020618556701030927,"disprot_consensus":{"full":[{"start":187,"end":196,"type":"D"}],"Structural state":[{"start":187,"end":196,"type":"D"}],"Disorder function":[{"start":187,"end":196,"type":"F"}]}},{"acc":"O67305","sequence":"MPLTEHLRELRYRLIISIIAFLIGSGIAFYFAKYVFEILKEPILKSYPEVELITLSPTEPLFILIKISLAVGFIIASPVILYQFWRFIEPALYSHEKRAFIPLLLGSILLFMLGALFAYFIVLPLALKFLLGLGFTQLLATPYLSVDMYISFVLKLVVAFGIAFEMPIVLYVLQKAGVITPEQLASFRKYFIVIAFVIGAIIAPDVSTQVLMAIPLLLLYEISIFLGKLATRKKKEIQKA","alphafold_very_low_content":"NaN","creator":"gerdos","dataset":[],"date":"2026-06-02T12:40:56.144Z","disprot_id":"DP04659","features":{"pfam":[{"id":"PF00902","name":"Sec-independent protein translocase protein (TatC)","start":5,"end":215}]},"genes":[{"name":{"value":"tatC","evidences":[{"source":{"id":"MF_00902","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_00902","_id":"6a1ecf58cce615d745cf43ea"},"code":"ECO:0000255","_id":"6a1ecf58cce615d745cf43e9"}],"_id":"6a1ecf58cce615d745cf43e8"},"synonyms":[],"olnNames":[{"value":"aq_1267","_id":"6a1ecf58cce615d745cf43eb","evidences":[]}],"orfNames":[],"_id":"6a1ecf58cce615d745cf43e7"}],"length":240,"name":"Sec-independent protein translocase protein TatC","ncbi_taxon_id":224324,"organism":"Aquifex aeolicus (strain VF5)","regions_counter":1,"released":"2026_06","taxonomy":["Bacteria","Pseudomonadati","Aquificota","Aquificia","Aquificales","Aquificaceae","Aquifex"],"regions":[{"start":230,"end":240,"reference_id":"23201679","reference_source":"pmid","reference_html":"Structure of the TatC core of the twin-arginine protein transport system. <i> Rollauer SE, Tarry MJ, Graham JE, Jääskeläinen M, Jäger F, Johnson S, Krehenbrink M, Liu SM, Lukey MJ, Marcoux J, McDowell MA, Rodriguez F, Roversi P, Stansfeld PJ, Robinson CV, Sansom MS, Palmer T, Högbom M, Berks BC, Lea SM. </i> Nature, 2012","date":"2026-06-11T17:35:53.245Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":3,"cross_refs":[{"db":"PDB","id":"4B4A"}],"region_id":"DP04659r001","statement":[{"text":"The first four and last eleven amino acids of AaTatC are disordered and are not included in the structure (Supplementary Fig. 3).","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-11T17:35:56.238Z"}}],"__v":0,"disorder_content":0.04583333333333333,"disprot_consensus":{"full":[{"start":230,"end":240,"type":"D"}],"Structural state":[{"start":230,"end":240,"type":"D"}]}},{"acc":"Q1K502","sequence":"MDDLFEVFEEQPRAQKKRKASPDVEMADGAAAAAPVANAAAAVTHPQAQAAPAPQKDNIDNNDNNNNNTTTSAVQPTIPNGDAAAAADDVQSPQSPHGLGDNKRRKKTDEAEPIMTDAFQTAESREVTGAQGFAPTEGESIVLSHNIQHQVALPPDLDYEYIPLSEHKPPAEPARTYSFKLDPFQALSVASIEREESVLVSAHTSAGKTVVAEYAIAQCLKKNQRVIYTSPIKALSNQKYRDFQAEFGDVGLMTGDVTINPTASCLVMTTEILRSMLYRGSEIMREVAWVVFDEIHYMRDKIRGVVWEETIILLPDKVRYVFLSATIPNAFQFAEWIAKIHRQACHVVYTDFRPTPLQNYFFPAGGKGILLIVDEKGNFKENNFNQAMAMIEEKKGTDSNDWSAKQKGKGKNKKTNKGGEAADEKADIAKIIKMILKKNFQPVIVFNFSKRECEQMALASSSMKFNAPDEENMVNKVFENALASLSEDDKNLPQISNILPLLRKGIGVHHSGLLPILKETIEILFQEGLIKVLFATETFSIGLNMPARTVVFTQVTKWDGQQRRPLTSSEYIQMAGRAGRRGLDDRGIVIMMVDDKLEPETARAIVVGNQDKLNSAFHLGYNMVLNLLRIEAISPEYMLERCFFQFQNAASVPQLERELISLQQERDAIIIPDESIVKDYYGVRQQLEEYNKDMVFVIQHPQNCLGFFQEGRLIHIKSPSGVDYGWGVLIKHIQRQTPKNGQPPYPEQESYVLDVLLKVSGDFNPKTRGEGPMPEGIMPAGKDSKNARWEVVPCLLNCLRALGQLRVFLPKRLESADEKDGVGKAVDEISRRFPDGIPILDPMENMGINDDSFKKLLRKIEVLESRLVANPLHNSPLLVELWNQYSLKMQLGEQIKEKKKAIARAHSVAQLDELKSRKRVLRRLGFINDAEVVQMKARVACEISSTEGHELLLAELLFNRFFNELSPEICACILSCFIFDEKIETQALKEELAKPFREIQAQARIIAKVSAESKLDVNEDEYVQSLKWQLMETVLAWAQGRPFSEICKMTNVYEGSLIRLFRRLEELLRQMAEAARVMGSEELKDKFELSLSKIRRDIVSFNSLYL","alphafold_very_low_content":"NaN","creator":"gerdos","dataset":[],"date":"2026-06-03T08:57:19.562Z","disprot_id":"DP04717","features":{"pfam":[{"id":"PF00270","name":"DEAD/DEAH box helicase","start":183,"end":329},{"id":"PF00271","name":"Helicase conserved C-terminal domain","start":505,"end":582},{"id":"PF08148","name":"DSHCT (NUC185) domain","start":931,"end":1101},{"id":"PF13234","name":"Mtr4-like, beta-barrel domain","start":700,"end":903},{"id":"PF21408","name":"Exosome RNA helicase MTR4-like, stalk","start":636,"end":698}]},"genes":[{"name":{"value":"frh","evidences":[{"source":{"id":"EAA27062.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/EAA27062.1","_id":"6a1fec6fcce615d745cf475f"},"code":"ECO:0000313","_id":"6a1fec6fcce615d745cf475e"}],"_id":"6a1fec6fcce615d745cf475d"},"synonyms":[],"olnNames":[],"orfNames":[{"value":"NCU03363","_id":"6a1fec6fcce615d745cf4760","evidences":[]}],"_id":"6a1fec6fcce615d745cf475c"}],"length":1106,"name":"FRQ-interacting RNA helicase","ncbi_taxon_id":367110,"organism":"Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)","regions_counter":2,"released":"2026_06","taxonomy":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Sordariomycetidae","Sordariales","Sordariaceae","Neurospora"],"regions":[{"start":1,"end":140,"reference_id":"29718972","reference_source":"pmid","reference_html":"Structure of frequency-interacting RNA helicase from Neurospora crassa reveals high flexibility in a domain critical for circadian rhythm and RNA surveillance. <i> Morales Y, Olsen KJ, Bulcher JM, Johnson SJ. </i> PLoS One, 2018","date":"2026-06-12T17:12:25.962Z","curator_id":"gerdos","curator_name":"Gábor Erdős","curator_orcid":"0000-0001-6218-5192","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":1,"cross_refs":[{"db":"PDB","id":"6BB8"}],"region_id":"DP04717r001","statement":[{"text":"The N-terminal region adopts a random coil structure that deviates substantially from the previous structure (Fig 1B). The visible N-terminal region is shorter than that observed in the FRHOrtho structures, beginning at residue 141 for FRHTrig as opposed to residue 114 for FRHOrtho.","type":"Results"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-12T17:18:08.762Z"}},{"start":395,"end":424,"reference_id":"29718972","reference_source":"pmid","reference_html":"Structure of frequency-interacting RNA helicase from Neurospora crassa reveals high flexibility in a domain critical for circadian rhythm and RNA surveillance. <i> Morales Y, Olsen KJ, Bulcher JM, Johnson SJ. </i> PLoS One, 2018","date":"2026-06-12T17:18:02.011Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":0,"cross_refs":[{"db":"PDB","id":"6BB8"}],"region_id":"DP04717r002","statement":[{"text":"The PDB-deposited data indicate that this region lacks electron density. As it appears to be part of the analyzed sample, the absence of electron density is likely due to its disordered nature, consistent with predicted data.","type":"Curator statement"}]}],"__v":0,"disorder_content":0.15370705244122965,"disprot_consensus":{"full":[{"start":1,"end":140,"type":"D"},{"start":395,"end":424,"type":"D"}],"Structural state":[{"start":1,"end":140,"type":"D"},{"start":395,"end":424,"type":"D"}]}},{"acc":"Q9CS84","sequence":"MGTALVQRGGCCLLCLSLLLLGCWAELGSGLEFPGAEGQWTRFPKWNACCESEMSFQLKTRSARGLVLYFDDEGFCDFLELILTRGGRLQLSFSIFCAEPATLLADTPVNDGAWHSVRIRRQFRNTTLYIDRAEAKWVEVKSKRRDMTVFSGLFVGGLPPELRAAALKLTLASVREREPFKGWIRDVRVNSSQALPVDGGEVKLDDEPPNSGGGSPCEAGEEGEGGVCLNGGVCSVVDDQAVCDCSRTGFRGKDCSQEDNNVEGLAHLMMGDQGKSKGKEEYIATFKGSEYFCYDLSQNPIQSSSDEITLSFKTLQRNGLMLHTGKSADYVNLALKNGAVSLVINLGSGAFEALVEPVNGKFNDNAWHDVKVTRNLRQHSGIGHAMVNKLHCSVTISVDGILTTTGYTQEDYTMLGSDDFFYVGGSPSTADLPGSPVSNNFMGCLKEVVYKNNDVRLELSRLAKQGDPKMKIHGVVAFKCENVATLDPITFETPESFISLPKWNAKKTGSISFDFRTTEPNGLILFSHGKPRHQKDAKHPQMIKVDFFAIEMLDGHLYLLLDMGSGTIKIKALQKKVNDGEWYHVDFQRDGRSGTISVNTLRTPYTAPGESEILDLDDELYLGGLPENKAGLVFPTEVWTALLNYGYVGCIRDLFIDGQSKDIRQMAEIQSTAGVKPSCSKETAKPCLSNPCKNNGMCRDGWNRYVCDCSGTGYLGRSCEREATVLSYDGSMFMKIQLPVVMHTEAEDVSLRFRSQRAYGILMATTSRDSADTLRLELDAGRVKLTVNLDCIRINCNSSKGPETLFAGYNLNDNEWHTVRVVRRGKSLKLTVDDQQAMTGQMAGDHTRLEFHNIETGIITERRYLSSVPSNFIGHLQSLTFNGMAYIDLCKNGDIDYCELNARFGFRNIIADPVTFKTKSSYVALATLQAYTSMHLFFQFKTTSLDGLILYNSGDGNDFIVVELVKGYLHYVFDLGNGANLIKGSSNKPLNDNQWHNVMISRDTSNLHTVKIDTKITTQITAGARNLDLKSDLYIGGVAKETYKSLPKLVHAKEGFQGCLASVDLNGRLPDLISDALFCNGQIERGCEGPSTTCQEDSCSNQGVCLQQWDGFSCDCSMTSFSGPLCNDPGTTYIFSKGGGQITYKWPPNDRPSTRADRLAIGFSTVQKEAVLVRVDSSSGLGDYLELHIHQGKIGVKFNVGTDDIAIEESNAIINDGKYHVVRFTRSGGNATLQVDSWPVIERYPAGNNDNERLAIARQRIPYRLGRVVDEWLLDKGRQLTIFNSQATIIIGGKEQGQPFQGQLSGLYYNGLKVLNMAAENDANIAIVGNVRLVGEVPSSMTTESTATAMQSEMSTSIMETTTTLATSTARRGKPPTKEPISQTTDDILVASAECPSDDEDIDPCEPSSGGLANPTRVGGREPYPGSAEVIRESSSTTGMVVGIVAAAALCILILLYAMYKYRNRDEGSYHVDESRNYISNSAQSNGAVVKEKQPSSAKSANKNKKNKDKEYYV","alphafold_very_low_content":"NaN","creator":"bjuhasz","dataset":[],"date":"2026-06-19T13:59:15.979Z","disprot_id":"DP04750","features":{"pfam":[{"id":"PF00008","name":"EGF-like domain","start":687,"end":714},{"id":"PF01034","name":"Syndecan domain","start":1439,"end":1478},{"id":"PF02210","name":"Laminin G domain","start":58,"end":191},{"id":"PF02210","name":"Laminin G domain","start":312,"end":452},{"id":"PF02210","name":"Laminin G domain","start":515,"end":659},{"id":"PF02210","name":"Laminin G domain","start":753,"end":883},{"id":"PF02210","name":"Laminin G domain","start":940,"end":1068},{"id":"PF02210","name":"Laminin G domain","start":1163,"end":1311}]},"genes":[{"name":{"value":"Nrxn1","_id":"6a354b34511fbd6cb6fb4e17","evidences":[]},"synonyms":[{"value":"Kiaa0578","_id":"6a354b34511fbd6cb6fb4e18","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"6a354b34511fbd6cb6fb4e16"}],"length":1514,"name":"Neurexin-1","ncbi_taxon_id":10090,"organism":"Mus musculus","regions_counter":1,"released":"2026_06","taxonomy":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Glires","Rodentia","Myomorpha","Muroidea","Muridae","Murinae","Mus","Mus"],"regions":[{"start":201,"end":230,"reference_id":"18334216","reference_source":"pmid","reference_html":"Crystal structures of beta-neurexin 1 and beta-neurexin 2 ectodomains and dynamics of splice insertion sequence 4. <i> Koehnke J, Jin X, Trbovic N, Katsamba PS, Brasch J, Ahlsen G, Scheiffele P, Honig B, Palmer AG, Shapiro L. </i> Structure, 2008","date":"2026-06-19T14:03:12.768Z","curator_id":"bjuhasz","curator_name":"Bernadett Juhász","curator_orcid":"0009-0009-6028-6956","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006198","ec_ontology":"ECO","ec_name":"proton-based nuclear magnetic resonance evidence used in manual assertion","unpublished":true,"released":"2026_06","version":0,"construct_alterations":[{"term_id":"MI:0380","term_name":"15N label","term_namespace":"Labels and dyes","start":null,"end":null,"position":"unspecified","statements":[{"type":"Methods","text":"Samples for NMR studies were produced as above except that E. coli were grown in M9 minimal medium (Sambrook et al., 2001) prepared with 15NH4Cl (Cambridge Isotope Laboratories)."}]}],"region_id":"DP04750r001","statement":[{"text":"NMR studies of β-NRX1 Δ and β-NRX1+4 show that the splice-inserted sequence forms an unstructured loop in isolation, and remains at least partially disordered in a βNRX1+4 / NL complex.","type":"Abstract"},{"text":"NMR chemical shifts and nuclear Overhauser effect measurements for the Δ and +4 splice forms of β-NRX1 suggest that the peptide segment inserted at splice insertion 4 is disordered both in the absence of neurexin-binding partners and in the presence of at least one binding partner, neuroligin.","type":"Introduction"},{"text":"Our inability to obtain crystals of neurexins that include splice insertion sequences suggested that the insertions might be structurally disordered, and thereby hamper crystallization.","type":"Results"},{"text":"These data suggest that inclusion of the splice insertion sequence shifts the conformational equilibrium that leads to supernumerary peaks for β-NRX1Δ to favor the major species, and that the splice insertion itself gives rise to the group of peaks, not present in the Δ isoform, which appear to be disordered.","type":"Results"},{"text":"In contrast, a set of resonances is observed at resonance frequencies corresponding to amide groups with NOEs < 0.5 in the free β-NRX1+4 protein, most of which are unique to β-NRX1+4. Observation of these resonances suggests that the splice insertion in β-NRX1+4 remains largely disordered in the complex with NL1A.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-19T16:54:30.193Z"}}],"__v":0,"disorder_content":0.019815059445178335,"disprot_consensus":{"full":[{"start":201,"end":230,"type":"D"}],"Structural state":[{"start":201,"end":230,"type":"D"}]}},{"acc":"A0ABQ8E5R8","sequence":"MADNKQSFQAGQAAGRAEEKGNVLMDKVKDAATAAGASAQTAGQKITEAAGGAVNLVKEKTGMNK","creator":"System-mnecci","dataset":[],"date":"2026-07-03T10:56:04.535Z","disprot_id":"DP04806","features":{"pfam":[{"id":"PF27970","name":"LEA protein 1/2/D7/Stress-induced protein KIN2","start":5,"end":65}]},"genes":[{"synonyms":[],"olnNames":[],"orfNames":[{"value":"HID58_004436","_id":"6a479544636e23eee351228f","evidences":[]}],"_id":"6a479544636e23eee351228e"}],"length":65,"name":"Uncharacterized protein","ncbi_taxon_id":3708,"organism":"Brassica napus","regions_counter":2,"released":"2026_06","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Brassiceae","Brassica"],"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":65,"region_id":"DP04806r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Purification, characterization, and structural analysis of a plant low-temperature-induced protein. <i> Boothe JG, Sönnichsen FD, de Beus MD, Johnson-Flanagan AM. </i> Plant Physiol, 1997","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"9046590","version":2,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Structural state","ec_ontology":"ECO","end":65,"region_id":"DP04806r002","released":"2022_03","ec_id":"ECO:0006204","reference_html":"Purification, characterization, and structural analysis of a plant low-temperature-induced protein. <i> Boothe JG, Sönnichsen FD, de Beus MD, Johnson-Flanagan AM. </i> Plant Physiol, 1997","term_id":"IDPO:0000002","curator_id":"mnecci","start":1,"term_ontology":"IDPO","curator_name":"Marco Necci","reference_id":"9046590","version":2,"ec_name":"far-UV circular dichroism evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"0000-0001-9377-482X","ec_go":"EXP","disprot_namespace":"Structural state"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":65,"type":"D"}],"Structural state":[{"start":1,"end":65,"type":"D"}]}},{"acc":"Q66554","sequence":"MGSLEMVPMGAGPPSPGGDPDGDDGGNNSQYPSASGSSGNTPTPPNDEERESNEEPPPPYEDPYWGNGDRHSDYQPLGTQDQSLYLGLQHDGNDGLPPPPYSPRDDSSQHIYEEAGRG","creator":"System-jbergier","dataset":["Viral proteins"],"date":"2026-07-03T10:56:04.798Z","disprot_id":"DP04807","features":{"pfam":[{"id":"PF07415","name":"Gammaherpesvirus latent membrane protein (LMP2) protein","start":1,"end":118}]},"genes":[{"name":{"value":"LMP2","evidences":[{"source":{"id":"CAA57374.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/CAA57374.1","_id":"6a479544636e23eee3512299"},"code":"ECO:0000313","_id":"6a479544636e23eee3512298"}],"_id":"6a479544636e23eee3512297"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"6a479544636e23eee3512296"}],"length":118,"name":"Latent membrane protein 2A","ncbi_taxon_id":10376,"organism":"Epstein-Barr virus","regions_counter":10,"released":"2026_06","taxonomy":["Viruses","Duplodnaviria","Heunggongvirae","Peploviricota","Herviviricetes","Herpesvirales","Orthoherpesviridae","Gammaherpesvirinae","Lymphocryptovirus","Lymphocryptovirus humangamma4"],"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":118,"region_id":"DP04807r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Identification of the WW domain-interaction sites in the unstructured N-terminal domain of EBV LMP 2A. <i> Seo MD, Park SJ, Kim HJ, Lee BJ. </i> FEBS Lett, 2007","term_id":"IDPO:0000002","curator_id":"jbergier","start":1,"term_ontology":"IDPO","curator_name":"Julian Bergier","reference_id":"17174309","version":3,"ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","curator_orcid":"","statement":[{"text":"As expected, many peaks in the NOE spectrum of LMP2A NTD were negative, indicating an overall flexible structure.","type":"Results"},{"text":"Indeed, the chemical shift dispersion was limited to a mere 1.2 ppm, which immediately confirmed the macroscopic unfolded nature of the protein. Fortunately, the resolution of each peak and the peak dispersion along the nitrogen axis (about 25 ppm) were sufficient to achieve the peak assignment. As expected, the overall chemical shifts of the LMP2A NTD are similar to those of a random-coil structure, and the CSI results also showed that the LMP2A NTD adopts a random-coil structure in its native state.","type":"Discussion"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-23T09:33:11.839Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":60,"end":67,"reference_id":"17174309","reference_source":"pmid","reference_html":"Identification of the WW domain-interaction sites in the unstructured N-terminal domain of EBV LMP 2A. <i> Seo MD, Park SJ, Kim HJ, Lee BJ. </i> FEBS Lett, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP04807r002","statement":[{"text":"Upon the binding of the WW2 peptide, six residues (Tyr60, Glu61, Asp62, Trp65, Gly66, and Asn67) just behind the N-terminal PY motif and nine residues (Leu84, Tyr85, Leu86, Gly87, Gln89, His90, Asp94, Gly95, and Leu96) preceding to the C-terminal PY motif of the LMP2A NTD completely disappeared, which means that these residues are directly involved in WW2 domain binding.","type":"Discussion"},{"text":"To analyze the binding of the WW2 and WW3 peptides to the LMP2A NTD, 200 μM aliquots of chemically synthesized WW2 and WW3 peptides (WW2 and WW3 domains of human Nedd4-like ubiquitin-protein ligases AIP4) were each added to 100 μM of the LMP2A NTD, and the chemical shift changes of the LMP2A NTD were monitored in HSQC spectra (WW2:Ac-PLPPGWERRVDNMGRIYYVDHFTRTTTWQRPTLE-NH2 WW3:Ac-GPLPPGWEKRTDSNGRVYFVNHNTRITQWEDPRS-NH2).","type":"Methods"}],"interaction_partner":[{"db":"UniProt","id":"Q96J02","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-23T09:43:41.771Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":84,"end":96,"reference_id":"17174309","reference_source":"pmid","reference_html":"Identification of the WW domain-interaction sites in the unstructured N-terminal domain of EBV LMP 2A. <i> Seo MD, Park SJ, Kim HJ, Lee BJ. </i> FEBS Lett, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP04807r003","statement":[{"text":"Upon the binding of the WW2 peptide, six residues (Tyr60, Glu61, Asp62, Trp65, Gly66, and Asn67) just behind the N-terminal PY motif and nine residues (Leu84, Tyr85, Leu86, Gly87, Gln89, His90, Asp94, Gly95, and Leu96) preceding to the C-terminal PY motif of the LMP2A NTD completely disappeared, which means that these residues are directly involved in WW2 domain binding.","type":"Discussion"},{"text":"To analyze the binding of the WW2 and WW3 peptides to the LMP2A NTD, 200 μM aliquots of chemically synthesized WW2 and WW3 peptides (WW2 and WW3 domains of human Nedd4-like ubiquitin-protein ligases AIP4) were each added to 100 μM of the LMP2A NTD, and the chemical shift changes of the LMP2A NTD were monitored in HSQC spectra (WW2:Ac-PLPPGWERRVDNMGRIYYVDHFTRTTTWQRPTLE-NH2 WW3:Ac-GPLPPGWEKRTDSNGRVYFVNHNTRITQWEDPRS-NH2).","type":"Methods"}],"interaction_partner":[{"db":"UniProt","id":"Q96J02","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-23T09:33:53.396Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":60,"end":66,"reference_id":"17174309","reference_source":"pmid","reference_html":"Identification of the WW domain-interaction sites in the unstructured N-terminal domain of EBV LMP 2A. <i> Seo MD, Park SJ, Kim HJ, Lee BJ. </i> FEBS Lett, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"Q96J02","partner_start":null,"partner_end":null}],"region_id":"DP04807r004","statement":[{"text":"Upon WW3 peptide binding, the resonances of five residues (Tyr60, Glu61, Asp62, Trp65, and Gly66) just behind the N-terminal PY motif of the LMP2A NTD disappeared, a similar situation as with WW2 binding.","type":"Discussion"},{"text":"To analyze the binding of the WW2 and WW3 peptides to the LMP2A NTD, 200 μM aliquots of chemically synthesized WW2 and WW3 peptides (WW2 and WW3 domains of human Nedd4-like ubiquitin-protein ligases AIP4) were each added to 100 μM of the LMP2A NTD, and the chemical shift changes of the LMP2A NTD were monitored in HSQC spectra (WW2:Ac-PLPPGWERRVDNMGRIYYVDHFTRTTTWQRPTLE-NH2 WW3:Ac-GPLPPGWEKRTDSNGRVYFVNHNTRITQWEDPRS-NH2).","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-23T09:33:41.842Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":86,"end":110,"reference_id":"17174309","reference_source":"pmid","reference_html":"Identification of the WW domain-interaction sites in the unstructured N-terminal domain of EBV LMP 2A. <i> Seo MD, Park SJ, Kim HJ, Lee BJ. </i> FEBS Lett, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","term_id":"GO:0005515","term_name":"protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"Q96J02","partner_start":null,"partner_end":null}],"region_id":"DP04807r005","statement":[{"text":"Upon WW3 peptide binding, the resonances of three residues (Leu86, Gly87, and Asp94) in region 9 completely disappeared, and the resonances of three residues (Ser108, Gln109, and His110) in region 10 showed chemical shift changes.","type":"Discussion"},{"text":"To analyze the binding of the WW2 and WW3 peptides to the LMP2A NTD, 200 μM aliquots of chemically synthesized WW2 and WW3 peptides (WW2 and WW3 domains of human Nedd4-like ubiquitin-protein ligases AIP4) were each added to 100 μM of the LMP2A NTD, and the chemical shift changes of the LMP2A NTD were monitored in HSQC spectra (WW2:Ac-PLPPGWERRVDNMGRIYYVDHFTRTTTWQRPTLE-NH2 WW3:Ac-GPLPPGWEKRTDSNGRVYFVNHNTRITQWEDPRS-NH2).","type":"Methods"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-23T09:33:25.680Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a protein.\" [GOC:go_curators]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":86,"end":110,"reference_id":"17174309","reference_source":"pmid","reference_html":"Identification of the WW domain-interaction sites in the unstructured N-terminal domain of EBV LMP 2A. <i> Seo MD, Park SJ, Kim HJ, Lee BJ. </i> FEBS Lett, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP04807r006","statement":[{"text":"The LMP2A NTD-WW3 peptide complex.","type":"Figure"},{"text":"Like the WW2 peptide, the WW3 peptide forms a complex with the LMP2A NTD, although the number of residues showing chemical shift changes was relatively smaller than that of the WW2 peptide (Fig. 3b).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-23T10:15:40.843Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":60,"end":66,"reference_id":"17174309","reference_source":"pmid","reference_html":"Identification of the WW domain-interaction sites in the unstructured N-terminal domain of EBV LMP 2A. <i> Seo MD, Park SJ, Kim HJ, Lee BJ. </i> FEBS Lett, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP04807r007","statement":[{"text":"The LMP2A NTD-WW3 peptide complex.","type":"Figure"},{"text":"Like the WW2 peptide, the WW3 peptide forms a complex with the LMP2A NTD, although the number of residues showing chemical shift changes was relatively smaller than that of the WW2 peptide (Fig. 3b).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-23T10:15:38.882Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":60,"end":67,"reference_id":"17174309","reference_source":"pmid","reference_html":"Identification of the WW domain-interaction sites in the unstructured N-terminal domain of EBV LMP 2A. <i> Seo MD, Park SJ, Kim HJ, Lee BJ. </i> FEBS Lett, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP04807r008","statement":[{"text":"Two-dimensional 1H–15N HSQC spectra of the LMP2A NTD-WW2 peptide complex.","type":"Figure"},{"text":"Like the WW2 peptide, the WW3 peptide forms a complex with the LMP2A NTD, although the number of residues showing chemical shift changes was relatively smaller than that of the WW2 peptide (Fig. 3b).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-23T10:15:37.082Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":84,"end":96,"reference_id":"17174309","reference_source":"pmid","reference_html":"Identification of the WW domain-interaction sites in the unstructured N-terminal domain of EBV LMP 2A. <i> Seo MD, Park SJ, Kim HJ, Lee BJ. </i> FEBS Lett, 2007","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","term_id":"GO:0060090","term_name":"molecular adaptor activity","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP04807r009","statement":[{"text":"Two-dimensional 1H–15N HSQC spectra of the LMP2A NTD-WW2 peptide complex.","type":"Figure"},{"text":"Like the WW2 peptide, the WW3 peptide forms a complex with the LMP2A NTD, although the number of residues showing chemical shift changes was relatively smaller than that of the WW2 peptide (Fig. 3b).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-23T10:15:35.732Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.\" [GOC:mtg_MIT_16mar07, GOC:vw]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":118,"reference_id":"15802216","reference_source":"pmid","reference_html":"Expression and characterization of N-terminal domain of Epstein-Barr virus latent membrane protein 2A in Escherichia coli. <i> Park SJ, Seo MD, Lee SK, Ikeda M, Longnecker R, Lee BJ. </i> Protein Expr Purif, 2005","date":"2022-02-14T09:00:00.000Z","curator_id":"jbergier","curator_name":"Julian Bergier","curator_orcid":"","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP04807r010","statement":[{"text":"Therefore, the structure of LMP2A NTD seems to be intrinsically unordered without any regular structures.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-09-23T09:24:07.035Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":118,"type":"D"}],"Structural state":[{"start":1,"end":118,"type":"D"}],"Molecular function":[{"start":60,"end":67,"type":"F"},{"start":84,"end":110,"type":"F"}]}},{"acc":"C0RVT5","sequence":"MSNMDIDGINTGTIDKAPEEITSGTSGTTRPIIRPATLAPPSNKRTRNPSPERATTISEADVGRKTQKKQTPTEIKKSVYNMVVKLGEFYNQMMVKAGLNDDMERNLIQNAHAVERILLAATDDKKTEFQKKKNARDVKEGKEEIDHNKTGGTFYKMVRDDKTIYFSPIRVTFLKEEVKTMYKTTMGSDGFSGLNHIMIGHSQMNDVCFQRSKALKRVGLDPSLISTFAGSTLPRRSGATGVAIKGGGTLVAEAIRFIGRAMADRGLLRDIKAKTAYEKILLNLKNKCSAPQQKALVDQVIGSRNPGIADIEDLTLLARSMVVVRPSVASKVVLPISIYAKIPQLGFNVEEYSMVGYEAMALYNMATPVSILRVGDDAKDKSQLFFMSCFGAAYEDLRVLSALTGTEFKPRSALKCKGFHVPAKEQVEGMGAALMSIKLQFWAPMTRSGGNEVGGDGGSGQISCSPVFAVERPIALSKQAVRRMLSMNIEGRDADVKGNLLKMMNDSMAKKTNGNAFIGKKMFQISDKNKTNPVEIPIKQTIPNFFFGRDTAEDYDDLDY","creator":"System-mmacossay","dataset":["Viral proteins"],"date":"2026-07-03T10:56:06.594Z","disprot_id":"DP04808","features":{"pfam":[{"id":"PF00506","name":"Influenza virus nucleoprotein","start":38,"end":557}]},"genes":[{"name":{"value":"NP","evidences":[{"source":{"id":"MF_04070","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04070","_id":"6a479546636e23eee35122a3"},"code":"ECO:0000256","_id":"6a479546636e23eee35122a2"},{"source":{"id":"RU361251","name":"RuleBase","url":"https://www.uniprot.org/unirule/RU361251","_id":"6a479546636e23eee35122a5"},"code":"ECO:0000256","_id":"6a479546636e23eee35122a4"},{"source":{"id":"ACO05962.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/ACO05962.1","_id":"6a479546636e23eee35122a7"},"code":"ECO:0000313","_id":"6a479546636e23eee35122a6"}],"_id":"6a479546636e23eee35122a1"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"6a479546636e23eee35122a0"}],"length":560,"name":"Nucleoprotein","ncbi_taxon_id":464417,"organism":"Influenza B virus (strain B/Malaysia/2506/2004)","regions_counter":14,"released":"2026_06","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Polyploviricotina","Insthoviricetes","Articulavirales","Orthomyxoviridae","Betainfluenzavirus","Betainfluenzavirus influenzae","Influenza B virus"],"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":70,"region_id":"DP04808r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Structural analysis of the complex between influenza B nucleoprotein and human importin-α. <i> Labaronne A, Milles S, Donchet A, Jensen MR, Blackledge M, Bourhis JM, Ruigrok RWH, Crépin T. </i> Sci Rep, 2017","statement":[{"text":"We calculated secondary structure propensities (SSPs) based on experimental Cα and Cβ chemical shifts, which indicate that no strong propensities for either α-helical or extended structure exist (Fig. 2a).","type":"Results"},{"text":" The obtained conformational ensembles describe B/NPTAIL as a protein behaving much like a statistical coil, with the exception of a region starting around residue 59 that had a slightly increased propensity to form right handed α-helices as compared to random coil. ","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29215074","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-25T12:26:44.127Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":70,"term_name":"importin-alpha family protein binding","released":"2022_03","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","reference_html":"Structural analysis of the complex between influenza B nucleoprotein and human importin-α. <i> Labaronne A, Milles S, Donchet A, Jensen MR, Blackledge M, Bourhis JM, Ruigrok RWH, Crépin T. </i> Sci Rep, 2017","statement":[{"text":"Interestingly, the interaction between B/NPTAIL and importin-α involves all residues of the disordered tail between amino acids 30 and 71 (Fig. 4c).","type":"Results"}],"term_id":"GO:0061676","curator_id":"vnugnes","start":1,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"29215074","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006165","region_id":"DP04808r002","interaction_partner":[{"db":"UniProt","id":"O60684","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-25T12:44:49.153Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a member of the importin-alpha family.\" [PMID:15350979, PMID:17170104, PMID:23734157]","disprot_namespace":"Disorder function","term_is_binding":true},{"term_namespace":"Structural state","ec_ontology":"ECO","end":70,"region_id":"DP04808r003","released":"2022_03","ec_id":"ECO:0006210","reference_html":"Structural analysis of the complex between influenza B nucleoprotein and human importin-α. <i> Labaronne A, Milles S, Donchet A, Jensen MR, Blackledge M, Bourhis JM, Ruigrok RWH, Crépin T. </i> Sci Rep, 2017","statement":[{"text":"The experimental SAXS curve of full length B/NP was in reasonable agreement (chi2 below 1) with this conformational ensemble (Fig. 2d).","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"vnugnes","start":1,"term_ontology":"IDPO","curator_name":"Victoria Nugnes","ec_name":"small-angle X-ray scattering evidence used in manual assertion","version":3,"curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"29215074","validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-25T12:26:38.244Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"term_namespace":"Molecular function","ec_ontology":"ECO","end":70,"term_name":"importin-alpha family protein binding","released":"2022_03","ec_name":"small-angle X-ray scattering evidence used in manual assertion","reference_html":"Structural analysis of the complex between influenza B nucleoprotein and human importin-α. <i> Labaronne A, Milles S, Donchet A, Jensen MR, Blackledge M, Bourhis JM, Ruigrok RWH, Crépin T. </i> Sci Rep, 2017","statement":[{"text":"An absence of linearity in the Guinier plot reflects the presence of aggregates and/or attractive/repulsive interactions between the scattering particles.","type":"Results"},{"text":"The complex between importin-α7 and B/NP was studied with SAXS. The analysis shows the volumes of the two proteins. Although the SAXS envelope of a disordered chain cannot give a single structure for B/NTAIL the complex shows that importin-α binds two thirds of the tail, concordant with the results from NMR, and no other parts of B/NP.","type":"Discussion"}],"term_id":"GO:0061676","curator_id":"vnugnes","start":1,"term_ontology":"GO","curator_name":"Victoria Nugnes","reference_id":"29215074","version":4,"curator_orcid":"0000-0001-8399-7907","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","ec_id":"ECO:0006210","region_id":"DP04808r004","interaction_partner":[{"db":"UniProt","id":"O60684","partner_start":null,"partner_end":null}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-25T12:44:50.512Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a member of the importin-alpha family.\" [PMID:15350979, PMID:17170104, PMID:23734157]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":70,"reference_id":"29215074","reference_source":"pmid","reference_html":"Structural analysis of the complex between influenza B nucleoprotein and human importin-α. <i> Labaronne A, Milles S, Donchet A, Jensen MR, Blackledge M, Bourhis JM, Ruigrok RWH, Crépin T. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0061676","term_name":"importin-alpha family protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"O60684","partner_start":null,"partner_end":null}],"region_id":"DP04808r005","statement":[{"text":"The peak eluted at 12.5 mL corresponds to the B/NPTAIL and the SDS-PAGE gel confirms the presence of the protein contained in that elution peak (band at 15 kDa). The elution peak at 10.5 mL corresponds to importin-α7 alone and the peak at 10.1 mL corresponds to the complex between B/NPTAIL and importin-α7. These results confirm that importin-α7 binds the full-length influenza B nucleoprotein and its N-terminal tail but not B/NPCORE.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-25T12:44:51.799Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a member of the importin-alpha family.\" [PMID:15350979, PMID:17170104, PMID:23734157]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":70,"reference_id":"29215074","reference_source":"pmid","reference_html":"Structural analysis of the complex between influenza B nucleoprotein and human importin-α. <i> Labaronne A, Milles S, Donchet A, Jensen MR, Blackledge M, Bourhis JM, Ruigrok RWH, Crépin T. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0061676","term_name":"importin-alpha family protein binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0005647","ec_ontology":"ECO","ec_name":"isothermal titration calorimetry evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"interaction_partner":[{"db":"UniProt","id":"O60684","partner_start":null,"partner_end":null}],"region_id":"DP04808r006","statement":[{"text":"B/NPTAIL binds human importin-α7 with a K d of 844 nM, similar to the affinity measured between A/NP and the mouse importin-α1 (K d between 2 and 5 µM)19,20.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-25T12:44:55.466Z"},"ec_go":"IPI","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a member of the importin-alpha family.\" [PMID:15350979, PMID:17170104, PMID:23734157]","disprot_namespace":"Disorder function","term_is_binding":true},{"start":1,"end":70,"reference_id":"29215074","reference_source":"pmid","reference_html":"Structural analysis of the complex between influenza B nucleoprotein and human importin-α. <i> Labaronne A, Milles S, Donchet A, Jensen MR, Blackledge M, Bourhis JM, Ruigrok RWH, Crépin T. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006607","term_name":"NLS-bearing protein import into nucleus","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0007680","ec_ontology":"ECO","ec_name":"chromatography evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP04808r012","statement":[{"text":"The peak eluted at 12.5 mL corresponds to the B/NPTAIL and the SDS-PAGE gel confirms the presence of the protein contained in that elution peak (band at 15 kDa). The elution peak at 10.5 mL corresponds to importin-α7 alone and the peak at 10.1 mL corresponds to the complex between B/NPTAIL and importin-α7. These results confirm that importin-α7 binds the full-length influenza B nucleoprotein and its N-terminal tail but not B/NPCORE.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-25T12:31:30.075Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The directed movement of a protein bearing a nuclear localization signal (NLS) from the cytoplasm into the nucleus, across the nuclear envelope.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":70,"reference_id":"29215074","reference_source":"pmid","reference_html":"Structural analysis of the complex between influenza B nucleoprotein and human importin-α. <i> Labaronne A, Milles S, Donchet A, Jensen MR, Blackledge M, Bourhis JM, Ruigrok RWH, Crépin T. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006607","term_name":"NLS-bearing protein import into nucleus","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0006210","ec_ontology":"ECO","ec_name":"small-angle X-ray scattering evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP04808r013","statement":[{"text":"The complex between importin-α7 and B/NP was studied with SAXS. The analysis shows the volumes of the two proteins. Although the SAXS envelope of a disordered chain cannot give a single structure for B/NTAIL the complex shows that importin-α binds two thirds of the tail, concordant with the results from NMR, and no other parts of B/NP.","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-25T12:31:28.900Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The directed movement of a protein bearing a nuclear localization signal (NLS) from the cytoplasm into the nucleus, across the nuclear envelope.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":false},{"start":1,"end":70,"reference_id":"29215074","reference_source":"pmid","reference_html":"Structural analysis of the complex between influenza B nucleoprotein and human importin-α. <i> Labaronne A, Milles S, Donchet A, Jensen MR, Blackledge M, Bourhis JM, Ruigrok RWH, Crépin T. </i> Sci Rep, 2017","date":"2022-02-14T09:00:00.000Z","curator_id":"vnugnes","curator_name":"Victoria Nugnes","curator_orcid":"0000-0001-8399-7907","term_id":"GO:0006607","term_name":"NLS-bearing protein import into nucleus","term_namespace":"Biological process","term_ontology":"GO","term_go_domain":"P","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":1,"region_id":"DP04808r014","statement":[{"text":"Interestingly, the interaction between B/NPTAIL and importin-α involves all residues of the disordered tail between amino acids 30 and 71 (Fig. 4c).","type":"Results"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-10-25T12:31:22.503Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"The directed movement of a protein bearing a nuclear localization signal (NLS) from the cytoplasm into the nucleus, across the nuclear envelope.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":false}],"__v":0,"disorder_content":0.125,"disprot_consensus":{"full":[{"start":1,"end":70,"type":"D"}],"Structural state":[{"start":1,"end":70,"type":"D"}],"Molecular function":[{"start":1,"end":70,"type":"F"}],"Biological process":[{"start":1,"end":70,"type":"F"}]}},{"acc":"A0A9R1FWH6","sequence":"MEGEKNSSGDLMSSSKLVAEAAKTAYEKKSVEGIDKEKVAAASADILDSAAKYGKLEDKPVGQYLEKAEGYLKQYSSGGTEKEKTDAPAAADAPKPDAPKEAAPAPAPAAEEEKSSDGFGLDDVMKGAASLSGKKSGEEEKESGGGGGFMKMAQGFMK","alphafold_very_low_content":"NaN","creator":"System-achasapi","dataset":[],"date":"2026-07-03T10:56:06.811Z","disprot_id":"DP04809","features":{"pfam":[]},"genes":[{"name":{"value":"WCI16","evidences":[{"source":{"id":"BAN63108.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/BAN63108.1","_id":"6a479546636e23eee35122b1"},"code":"ECO:0000313","_id":"6a479546636e23eee35122b0"}],"_id":"6a479546636e23eee35122af"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"6a479546636e23eee35122ae"}],"length":158,"name":"Cold induced 16","ncbi_taxon_id":4565,"organism":"Triticum aestivum","regions_counter":1,"released":"2026_06","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","Liliopsida","Poales","Poaceae","BOP clade","Pooideae","Triticodae","Triticeae","Triticinae","Triticum"],"regions":[{"term_namespace":"Structural state","ec_ontology":"ECO","end":158,"region_id":"DP04809r001","released":"2022_03","ec_id":"ECO:0006165","reference_html":"Identification of a novel LEA protein involved in freezing tolerance in wheat. <i> Sasaki K, Christov NK, Tsuda S, Imai R. </i> Plant Cell Physiol, 2014","statement":[{"text":"No significant secondary shifts were observed in the high-field-shifted methyl region (0–1.0 p.p.m.), suggesting that hydrophobic side chains including aromatic rings do not form any clustered regions in WCI16. [...] WCI16 does not form definitive secondary structure, such as an α-helix or β-strand. [...] there is no significant specific three-dimensional structure in WCI16.","type":"Results"}],"term_id":"IDPO:0000002","curator_id":"achasapi","start":1,"term_ontology":"IDPO","curator_name":"Anastasia Chasapi","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","version":2,"curator_orcid":"0000-0003-1986-5007","date":"2022-02-14T09:00:00.000Z","reference_source":"pmid","term_name":"disorder","reference_id":"24265272","ec_go":"EXP","disprot_namespace":"Structural state"}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":158,"type":"D"}],"Structural state":[{"start":1,"end":158,"type":"D"}]}},{"acc":"Q6TDU5","sequence":"MMSIAQVRSAGSAGNYYTDKDNYYVLGSMGERWAGKGAEQLGLQGSVDKDVFTRLLEGRLPDGADLSRMQDGSNKHRPGYDLTFSAPKSVSMMAMLGGDKRLIDAHNQAVDFAVRQVEALASTRVMTDGQSETVLTGNLVMALFNHDTSRDQEPQLHTHAVVANVTQHNGEWKTLSSDKVGKTGFIENVYANQIAFGRLYREKLKEQVEALGYETEVVGKHGMWEMPGVPVEAFSGRSQAIREAVGEDASLKSRDVAALDTRKSKQHVDPEIRMAEWMQTLKETGFDIRAYRDAADQRTEIRTQAPGPASQDGPDVQQAVTQAIAGLSERKVQFTYTDVLARTVGILPPENGVIERARAGIDEAISREQLIPLDREKGLFTSGIHVLDELSVRALSRDIMKQNRVTVHPEKSVPRTAGYSDAVSVLAQDRPSLAIVSGQGGAAGQRERVAELVMMAREQGREVQIIAADRRSQMNLKQDERLSGELITGRRQLLEGMAFTPGSTVIVDQGEKLSLKETLTLLDGAARHNVQVLITDSGQRTGTGSALMAMKDAGVNTYRWQGGEQRPATIISEPDRNVRYARLAGDFAASVKAGEESVAQVSGVREQAILTQAIRSELKTQGVLGHPEVTMTALSPVWLDSRSRYLRDMYRPGMVMEQWNPETRSHDRYVIDRVTAQSHSLTLRDAQGETQVVRISSLDSSWSLFRPEKMPVADGERLRVTGKIPGLRVSGGDRLQVASVSEDAMTVVVPGRAEPASLPVSDSPFTALKLENGWVETPGHSVSDSATVFASVTQMAMDNATLNGLARSGRDVRLYSSLDETRTAEKLARHPSFTVVSEQIKARAGETLLETAISLQKAGLHTPAQQAIHLALPVLESKNLAFSMVDLLTEAKSFAAEGTGFTELGGEINAQIKRGDLLYVDVAKGYGTGLLVSRASYEAEKSILRHILEGKEAVTPLMERVPGELMETLTSGQRAATRMILETSDRFTVVQGYAGVGKTTQFRAVMSAVNMLPASERPRVVGLGPTHRAVGEMRSAGVDAQTLASFLHDTQLQQRSGETPDFSNTLFLLDESSMVGNTEMARAYALIAAGGGRAVASGDTDQLQAIAPGQSFRLQQTRSAADVVIMKEIVRQTPELREAVYSLINRDVERALSGLESVKPSQVPRLEGAWAPEHSVTEFSHSQEAKLAEAQQKAMLKGEAFPDIPMTLYEAIVRDYTGRTPEAREQTLIVTHLNEDRRVLNSMIHDAREKAGELGKEQVMVPVLNTANIRDGELRRLSTWEKNPDALALVDNVYHRIAGISKDDGLITLQDAEGNTRLISPREAVAEGVTLYTPDKIRVGTGDRMRFTKSDRERGYVANSVWTVTAVSGDSVTLSDGQQTRVIRPGQERAEQHIDLAYAITAHGAQGASETFAIALEGTEGNRKLMAGFESAYVALSRMKQHVQVYTDNRQGWTDAINNAVQKGTAHDVLEPKPDREVMNAQRLFSTARELRDVAAGRAVLRQAGLAGGDSPARFIAPGRKYPQPYVALPAFDRNGKSAGIWLNPLTTDDGNGLRGFSGEGRVKGSGDAQFVALQGSRNGESLLADNMQDGVRIARDNPDSGVVVRIAGEGRPWNPGAITGGRVWGDIPDNSVQPGAGNGEPVTAEVLAQRQAEEAIRRETERRADEIVRKMAENKPDLPDGKTELAVRDIAGQERDRSAISERETALPESVLRESQREREAVREVARENLLQERLQQMERDMVRDLQKEKTLGGD","creator":"System-eficho","dataset":[],"date":"2026-07-03T10:56:07.425Z","disprot_id":"DP04810","features":{"pfam":[{"id":"PF07057","name":"DNA helicase TraI, C-terminal","start":1465,"end":1622},{"id":"PF08751","name":"TrwC relaxase","start":11,"end":283},{"id":"PF13604","name":"AAA domain","start":969,"end":1155},{"id":"PF18272","name":"single-stranded DNA binding TraI N-terminal subdomain","start":575,"end":626},{"id":"PF18340","name":"DNA relaxase TraI 2B/2B-like domain","start":633,"end":712},{"id":"PF22232","name":"TraI helicase-associated ssDNA bd, N-terminal","start":438,"end":536}]},"genes":[{"name":{"value":"traI","evidences":[{"source":{"id":"AAQ98619.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/AAQ98619.1","_id":"6a479547636e23eee35122bb"},"code":"ECO:0000312","_id":"6a479547636e23eee35122ba"}],"_id":"6a479547636e23eee35122b9"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"6a479547636e23eee35122b8"}],"length":1756,"name":"Multifunctional conjugation protein TraI","ncbi_taxon_id":562,"organism":"Escherichia coli","regions_counter":1,"released":"2026_06","taxonomy":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"],"regions":[{"start":1630,"end":1756,"reference_id":"30617945","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>13</sup>C, <sup>15</sup>N resonance assignment of the C-terminal domain of the bifunctional enzyme TraI of plasmid R1. <i> Krishna B, Gubensäk N, Wagner GE, Zechner E, Raffl S, Becker W, Schrank E, Zangger K. </i> Biomol NMR Assign, 2019","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":2,"cross_refs":[{"db":"BMRB","id":"27596"}],"region_id":"DP04810r001","statement":[{"text":"The 1H–15N HSQC spectrum of R1 TraIC126 and the apparent limited peak dispersion along the hydrogen dimension, all the backbone amide peaks between 7.6 and 8.7 ppm, shows that R1 TraIC126 is at least partially disordered.","type":"Article"},{"text":"Secondary structure information was obtained from the backbone chemical shifts processed using Talos-N. The prediction shows major disordered regions, as expected from the 1H–15N HSQC spectrum’s poor peak dispersion along the hydrogen dimension. Talos prediction shows that two stretches of helices, spanning from residues 16 to 41 and 102 to 111 are connected through a loop region. The residues 3 to 15, 42 to 101 and 112 to 127 are predicted to be loop / disordered regions.","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-05T10:44:50.224Z"},"ec_go":"EXP","disprot_namespace":"Structural state"}],"__v":0,"disorder_content":0.07232346241457858,"disprot_consensus":{"full":[{"start":1630,"end":1756,"type":"D"}],"Structural state":[{"start":1630,"end":1756,"type":"D"}]}},{"acc":"A0A096W0X9","sequence":"MSLLTEVETPTRSEWECRCSDSSDPLVIAANIIGILHLILWITDRLFFKCIYRRFKYGLKRGPSTEGVPESMREEYQQEQQSAVDVDDGHFVNIELE","creator":"System-eficho","dataset":["Viral proteins"],"date":"2026-07-03T10:56:07.988Z","disprot_id":"DP04811","features":{"pfam":[{"id":"PF00599","name":"Influenza Matrix protein (M2)","start":1,"end":97}]},"genes":[{"name":{"value":"M2","evidences":[{"source":{"id":"AGY42500.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/AGY42500.1","_id":"6a479548636e23eee35122c5"},"code":"ECO:0000313","_id":"6a479548636e23eee35122c4"}],"_id":"6a479548636e23eee35122c3"},"synonyms":[{"value":"M","_id":"6a479548636e23eee35122c6","evidences":[]}],"olnNames":[],"orfNames":[],"_id":"6a479548636e23eee35122c2"}],"length":97,"name":"Matrix protein 2","ncbi_taxon_id":1402874,"organism":"Influenza A virus","regions_counter":4,"released":"2026_06","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Polyploviricotina","Insthoviricetes","Articulavirales","Orthomyxoviridae","Alphainfluenzavirus","Alphainfluenzavirus influenzae","Influenza A virus"],"regions":[{"start":44,"end":97,"reference_id":"32157574","reference_source":"pmid","reference_html":"pH-dependent secondary structure propensity of the influenza A virus M2 cytoplasmic tail. <i> Claridge JK, Mohd-Kipli F, Florea A, Gate T, Schnell JR. </i> Biomol NMR Assign, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":2,"cross_refs":[{"db":"BMRB","id":"50113"},{"db":"BMRB","id":"50127"}],"region_id":"DP04811r001","statement":[{"text":"The cytoplasmic tail residues are mostly disordered but an extended backbone conformation is adopted by the LC3 binding motif and the putative M1 interaction site has partial helical content with a small pH-dependence.","type":"Abstract"},{"text":"All measured heteronuclear NOEs were negative, indicating that the distal cytoplasmic tail was highly dynamic throughout. ","type":"Article"},{"text":"Backbone amide resonances for residues 44–64 were largely missing due to chemical exchange broadening.","type":"Article"},{"text":"The whole cytoplasmic tail of MP2 (residues 44-97) was found to be disordered based on heteronuclear NOEs. Within this longer region, residues 44-64 were also affected by chemical exchange broadening.","type":"Curator statement"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-08T14:12:09.600Z"},"ec_go":"EXP","disprot_namespace":"Structural state"},{"start":46,"end":62,"reference_id":"32157574","reference_source":"pmid","reference_html":"pH-dependent secondary structure propensity of the influenza A virus M2 cytoplasmic tail. <i> Claridge JK, Mohd-Kipli F, Florea A, Gate T, Schnell JR. </i> Biomol NMR Assign, 2020","date":"2022-02-14T09:00:00.000Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"GO:0008289","term_name":"lipid binding","term_namespace":"Molecular function","term_ontology":"GO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2022_03","version":3,"region_id":"DP04811r002","statement":[{"text":"A membrane proximal cytoplasmic region (residues ~ 46–97) contains a membrane-interacting amphipathic helix (APH; residues ~ 46–62) that is important in lipid raft targeting and virus scission.","type":"Article"},{"text":"HMQC spectra of the M2-APH-CT construct were acquired in the presence of 50 mM LMPC:LMPG micelles (4:1) or POPC:POPG liposomes (4:1; 17 mM total lipid) at pH 7.2. The detectable amides of the APH residues Gly58 and Gly62 were perturbed upon addition of the membrane mimetics. By contrast, none of the detectable resonances for residues outside of the APH were perturbed upon addition of either micelles or liposomes at pH 7.2 or pH 5.5, consistent with there being no interactions of the distal cytoplasmic tail with membranes.","type":"Article"}],"validated":{"curator_name":"Edoardo Salladini","curator_id":"esalladini","timestamp":"2021-07-08T14:12:13.875Z"},"ec_go":"EXP","term_not_annotate":false,"term_is_obsolete":false,"term_comment":"","term_def":"\"Binding to a lipid.\" [GOC:ai]","disprot_namespace":"Disorder function","term_is_binding":true}],"__v":0,"disorder_content":0.5567010309278351,"disprot_consensus":{"full":[{"start":44,"end":97,"type":"D"}],"Structural state":[{"start":44,"end":97,"type":"D"}],"Molecular function":[{"start":46,"end":62,"type":"F"}]}},{"acc":"A0ABF7SXN4","sequence":"MATKGTKRSYEQMETDGERQNATEIRASVGKMIDGIGRFYIQMCTELKLSDYEGRLIQNSLTIERMVLSAFDERRNKYLEEHPSAGKDPKKTGGPIYRRVDGKWRRELILYDKEEIRRIWRQANNGDDATAGLTHMMIWHSNLNDATYQRTRALVRTGMDPRMCSLMQGSTLPRRSGAAGAAVKGVGTMVMELIRMIKRGINDRNFWRGENGRRTRIAYERMCNILKGKFQTAAQRTMVDQVRESRNPGNAEFEDLIFLARSALILRGSVAHKSCLPACVYGSAVASGYDFEREGYSLVGIDPFRLLQNSQVYSLIRPNENPAHKSQLVWMACHSAAFEDLRVSSFIRGTKVVPRGKLSTRGVQIASNENMETMESSTLELRSRYWAIRTRSGGNTNQQRASSGQISIQPTFSVQRNLPFDRPTIMAAFTGNTEGRTSDMRTEIIRLMESARPEDVSFQGRGVFELSDEKATSPIVPSFDMSNEGSYFFGDNAEEYDN","creator":"System-gbalatti","dataset":["Viral proteins"],"date":"2026-07-03T10:56:08.528Z","disprot_id":"DP04812","features":{"pfam":[{"id":"PF00506","name":"Influenza virus nucleoprotein","start":1,"end":498}]},"genes":[{"name":{"value":"NP","evidences":[{"source":{"id":"MF_04070","name":"HAMAP-Rule","url":"https://hamap.expasy.org/unirule/MF_04070","_id":"6a479548636e23eee35122d0"},"code":"ECO:0000256","_id":"6a479548636e23eee35122cf"},{"source":{"id":"RU361251","name":"RuleBase","url":"https://www.uniprot.org/unirule/RU361251","_id":"6a479548636e23eee35122d2"},"code":"ECO:0000256","_id":"6a479548636e23eee35122d1"},{"source":{"id":"ACF54602.1","name":"EMBL","url":"https://www.ebi.ac.uk/ena/browser/view/ACF54602.1","_id":"6a479548636e23eee35122d4"},"code":"ECO:0000313","_id":"6a479548636e23eee35122d3"}],"_id":"6a479548636e23eee35122ce"},"synonyms":[],"olnNames":[],"orfNames":[],"_id":"6a479548636e23eee35122cd"}],"length":498,"name":"Nucleoprotein","ncbi_taxon_id":382835,"organism":"Influenza A virus","regions_counter":7,"released":"2026_06","taxonomy":["Viruses","Riboviria","Orthornavirae","Negarnaviricota","Polyploviricotina","Insthoviricetes","Articulavirales","Orthomyxoviridae","Alphainfluenzavirus","Alphainfluenzavirus influenzae","Influenza A virus"],"regions":[{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2IQH","_id":"685af523b4ac24d5329d97b6"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0005670","ec_name":"x-ray crystallography evidence used in manual assertion","ec_ontology":"ECO","start":8,"end":21,"interaction_partner":[],"reference_html":"The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA. <i> Ye Q, Krug RM, Tao YJ. </i> Nature, 2006","reference_id":"17151603","region_id":"DP04812r001","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"The nNLS sequence is located at the outer periphery of the nucleoprotein trimer where it is highly accessible to solvent (Fig. 3d). In addition, this region is disordered in electron density maps, and this flexibility should allow the nNLS to fit easily into the substrate recognition pocket on importin-a","_id":"685af523b4ac24d5329d97b4"},{"type":"Curator statement","text":"Correct UniProt entry is Q1K9H2 [Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1))]","_id":"685af523b4ac24d5329d97b5"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-07T08:09:18.796Z","_id":"685af523b4ac24d5329d97b7"},"version":1,"_id":"685af523b4ac24d5329d97b3","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2IQH","_id":"685af523b4ac24d5329d97c8"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":73,"end":91,"interaction_partner":[],"reference_html":"The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA. <i> Ye Q, Krug RM, Tao YJ. </i> Nature, 2006","reference_id":"17151603","region_id":"DP04812r005","released":"2022_03","sample":[],"statement":[{"type":"Figure","text":"Residues preceding and succeeding disordered regions are marked and connected by dotted lines.","_id":"685af523b4ac24d5329d97c9"},{"type":"Curator statement","text":"Missing residues on PDB entry 2IQH","_id":"685af523b4ac24d5329d97ca"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-06T11:56:24.508Z","_id":"685af523b4ac24d5329d97cb"},"version":1,"_id":"685af523b4ac24d5329d97c7","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2IQH","_id":"685af523b4ac24d5329d97cd"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Structural state","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":203,"end":212,"interaction_partner":[],"reference_html":"The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA. <i> Ye Q, Krug RM, Tao YJ. </i> Nature, 2006","reference_id":"17151603","region_id":"DP04812r006","released":"2022_03","sample":[],"statement":[{"type":"Figure","text":"Residues preceding and succeeding disordered regions are marked and connected by dotted lines.","_id":"685af523b4ac24d5329d97ce"},{"type":"Curator statement","text":"Missing residues on PDB entry 2IQH","_id":"685af523b4ac24d5329d97cf"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-06T11:57:03.353Z","_id":"685af523b4ac24d5329d97d0"},"version":1,"_id":"685af523b4ac24d5329d97cc","reference_source":"pmid"},{"annotation_extensions":[],"conditions":[],"construct_alterations":[],"cross_refs":[{"db":"PDB","id":"2IQH","_id":"685af523b4ac24d5329d97d2"}],"curator_id":"gbalatti","curator_name":"Galo Balatti","curator_orcid":"0000-0003-1900-1188","date":"2022-02-14T09:00:00.000Z","disprot_namespace":"Disorder function","ec_go":"EXP","ec_id":"ECO:0006220","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","ec_ontology":"ECO","start":8,"end":21,"interaction_partner":[],"reference_html":"The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA. <i> Ye Q, Krug RM, Tao YJ. </i> Nature, 2006","reference_id":"17151603","region_id":"DP04812r007","released":"2022_03","sample":[],"statement":[{"type":"Results","text":"In addition, this region is disordered in electron density maps, and this flexibility should allow the nNLS to fit easily into the substrate recognition pocket on importin-alpha.","_id":"685af523b4ac24d5329d97d3"}],"states_connection":[],"term_go_domain":null,"term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","term_ontology":"IDPO","term_xref":null,"unpublished":true,"validated":{"curator_id":"esalladini","curator_name":"Edoardo Salladini","timestamp":"2021-12-07T08:09:19.728Z","_id":"685af523b4ac24d5329d97d4"},"version":1,"_id":"685af523b4ac24d5329d97d1","reference_source":"pmid"}],"__v":0,"disorder_content":0.08634538152610442,"disprot_consensus":{"full":[{"start":8,"end":21,"type":"D"},{"start":73,"end":91,"type":"D"},{"start":203,"end":212,"type":"D"}],"Structural state":[{"start":8,"end":21,"type":"D"},{"start":73,"end":91,"type":"D"},{"start":203,"end":212,"type":"D"}],"Disorder function":[{"start":8,"end":21,"type":"F"}]}},{"acc":"P29997","sequence":"MSRSESRKNRGGREEILEQWVAGRKKLEELERDLRKTKKKLKKIEDENPWLGNIKGILGKKDKDGEGAPPAKRARTDQMEVDSGPRKRPLRGGFTDKERQDHRRRKALENKKKQLSAGGKNLSKEEEEELRRLTEEDERRERRVAGPPVGGVNPLEGGSRGAPGGGFVPNLQGVPESPFSRTGEGLDIRGNQGFP","creator":"System-rpancsa","dataset":["Viral proteins"],"date":"2026-07-03T10:56:08.809Z","disprot_id":"DP04813","features":{"pfam":[{"id":"PF01517","name":"Hepatitis delta virus delta antigen","start":1,"end":174}]},"genes":[],"length":195,"name":"Small delta antigen","ncbi_taxon_id":31764,"organism":"Hepatitis delta virus genotype I (isolate Woodchuck)","regions_counter":2,"released":"2026_06","taxonomy":["Viruses","Ribozyviria","Ribozyviria incertae sedis","Kolmioviridae","Deltavirus","Deltavirus italiense","Hepatitis delta virus"],"regions":[{"start":61,"end":91,"reference_id":"35749039","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>15</sup>N and <sup>13</sup>C backbone and side chain solution NMR assignments of the truncated small hepatitis delta antigen Δ60-S-HDAg. <i> Yang Y, Delcourte L, Fogeron ML, Böckmann A, Lecoq L. </i> Biomol NMR Assign, 2022","date":"2023-01-16T14:06:34.663Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":"within normal range","value":298,"statements":[{"type":"Article","text":"All NMR experiments were acquired at 298 K on a Bruker Avance III 600 spectrometer equipped with a cryoprobe."}]}],"construct_alterations":[{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Article","text":"Resin was washed with PBS, equilibrated in Cleavage buffer (50 mM Tris–HCl pH 8.0, 100 mM NaCl, 1 mM EDTA, 1 mM DTT), and GST-tag was cleaved by digestion with 200 units of PreScission protease overnight at 4 °C. The cleavage left five additional residues (GPLGS) at the N-terminus of SΔ60."}]}],"cross_refs":[{"db":"BMRB","id":"51340"}],"region_id":"DP04813r001","sequence_construct":"GPLGSKDKDGEGAPPAKRARTDQMEVDSGPGKRPLRGGFTDKERQDHRRRKALENKKKQLSAGGKNLSKEEEEELRRLTEEDERRERRVAGPPVGGVNPLEGGSRGAPGGGFVPNLQGVPESPFSRTGEGLDIRGNQGFP","statement":[{"text":"The 2D [1H–15N]-BTROSY-HSQC spectrum of 15N-13C-labelled SΔ60 is shown in Fig.1. The spectrum displays a high quality, with a dispersion corresponding to a partially disordered protein.","type":"Article"},{"text":"Similarly, the residues of the disordered parts (N-ter residues 58–91 and C-ter residues 150–194) show strong shielding effects with increasing temperature, meaning that their bond lengths are more sensitive to temperature changes, and thus that these regions are less involved in hydrogen bonds.","type":"Article"},{"text":"Although the authors mention residue 58 as the start of the disordered region, that is still part of the five residues remaining from the GST tag after cleavage. The  first residue that is part of the actual protein sequence is residue 61.","type":"Curator statement"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-19T18:07:07.020Z"}},{"start":150,"end":194,"reference_id":"35749039","reference_source":"pmid","reference_html":"<sup>1</sup>H, <sup>15</sup>N and <sup>13</sup>C backbone and side chain solution NMR assignments of the truncated small hepatitis delta antigen Δ60-S-HDAg. <i> Yang Y, Delcourte L, Fogeron ML, Böckmann A, Lecoq L. </i> Biomol NMR Assign, 2022","date":"2023-01-16T14:07:09.371Z","curator_id":"rpancsa","curator_name":"Rita Pancsa","curator_orcid":"0000-0003-0849-9312","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006165","ec_ontology":"ECO","ec_name":"nuclear magnetic resonance spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_06","version":0,"conditions":[{"term_id":"NCIT:C25206","term_name":"Temperature","unit_name":"K","unit_id":"UO:0000012","deviation":"within normal range","value":298,"statements":[{"type":"Article","text":"All NMR experiments were acquired at 298 K on a Bruker Avance III 600 spectrometer equipped with a cryoprobe."}]}],"construct_alterations":[{"term_id":"MI:0519","term_name":"glutathione s tranferase tag","term_namespace":"Tag","start":null,"end":null,"position":"N-terminal","statements":[{"type":"Article","text":"Resin was washed with PBS, equilibrated in Cleavage buffer (50 mM Tris–HCl pH 8.0, 100 mM NaCl, 1 mM EDTA, 1 mM DTT), and GST-tag was cleaved by digestion with 200 units of PreScission protease overnight at 4 °C. The cleavage left five additional residues (GPLGS) at the N-terminus of SΔ60."}]}],"cross_refs":[{"db":"BMRB","id":"51340"}],"region_id":"DP04813r002","sequence_construct":"GPLGSKDKDGEGAPPAKRARTDQMEVDSGPGKRPLRGGFTDKERQDHRRRKALENKKKQLSAGGKNLSKEEEEELRRLTEEDERRERRVAGPPVGGVNPLEGGSRGAPGGGFVPNLQGVPESPFSRTGEGLDIRGNQGFP","statement":[{"text":"The 2D [1H–15N]-BTROSY-HSQC spectrum of 15N-13C-labelled SΔ60 is shown in Fig.1. The spectrum displays a high quality, with a dispersion corresponding to a partially disordered protein.","type":"Article"},{"text":"Similarly, the residues of the disordered parts (N-ter residues 58–91 and C-ter residues 150–194) show strong shielding effects with increasing temperature, meaning that their bond lengths are more sensitive to temperature changes, and thus that these regions are less involved in hydrogen bonds.","type":"Article"}],"validated":{"curator_name":"Federica Quaglia","curator_id":"fquaglia","timestamp":"2023-01-19T18:07:12.654Z"}}],"__v":0,"disorder_content":0.38974358974358975,"disprot_consensus":{"full":[{"start":61,"end":91,"type":"D"},{"start":150,"end":194,"type":"D"}],"Structural state":[{"start":61,"end":91,"type":"D"},{"start":150,"end":194,"type":"D"}]}},{"acc":"A0A8T2G6V8","sequence":"MSKSEEKQELPLETSPYTKYEDIEDYKKNAYGTSGHQDVKPGHGGGTTDAPTPSGDAAPSAIDSANQKAKK","alphafold_very_low_content":"NaN","creator":"System-eficho","dataset":[],"date":"2026-07-03T10:56:09.008Z","disprot_id":"DP04814","features":{"pfam":[{"id":"PF10714","name":"Late embryogenesis abundant protein 18","start":3,"end":65}]},"genes":[{"synonyms":[],"olnNames":[],"orfNames":[{"value":"ISN44_As02g028460","_id":"6a479549636e23eee35122e2","evidences":[]}],"_id":"6a479549636e23eee35122e1"}],"length":71,"name":"Late embryogenesis abundant protein LEA-18","ncbi_taxon_id":45249,"organism":"Arabidopsis suecica","regions_counter":4,"released":"2026_06","taxonomy":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Brassicales","Brassicaceae","Camelineae","Arabidopsis"],"regions":[{"start":1,"end":71,"reference_id":"22155233","reference_source":"pmid","reference_html":"Influence of drying on the secondary structure of intrinsically disordered and globular proteins. <i> Hundertmark M, Popova AV, Rausch S, Seckler R, Hincha DK. </i> Biochem Biophys Res Commun, 2012","date":"2023-05-18T14:06:05.142Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006204","ec_ontology":"ECO","ec_name":"far-UV circular dichroism evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04814r001","statement":[{"text":"In solution the spectrum of LEA15 (Fig. 2A) showed typical features of a largely unstructured protein with a well defined minimal ellipticity at around 200 nm.\nAfter drying the spectrum was massively changed, indicating a gain of structure. However, the CD spectrum of LEA15 did not exhibit the double minimum at 208 and 222 nm characteristic of predominantly a-helical proteins. The CD spectra of the other investigated LEA proteins, both in the hydrated and dry state, were\nsimilar to those presented in Fig. 2A and are therefore not shown.\nSecondary structure estimates derived from these CD spectra indicated that the hydrated LEA proteins were between 61% (LEA17) and 68% (LEA20) unstructured (Fig. 2B). In addition, they contained around 20% b-sheet and only a negligible fraction of a-helices.","type":"Results"},{"text":"Based on the statement of the authors and figure 2B, the structural composition of the five investigated LEA proteins are similar to each other, both in the hydrated and dry state.","type":"Curator statement"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T09:03:44.650Z"}},{"start":1,"end":71,"reference_id":"22155233","reference_source":"pmid","reference_html":"Influence of drying on the secondary structure of intrinsically disordered and globular proteins. <i> Hundertmark M, Popova AV, Rausch S, Seckler R, Hincha DK. </i> Biochem Biophys Res Commun, 2012","date":"2023-05-18T14:08:12.243Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006228","ec_ontology":"ECO","ec_name":"Fourier-transform infrared spectroscopy evidence used in manual assertion","unpublished":true,"released":"2023_12","version":0,"region_id":"DP04814r003","statement":[{"text":"The Amide I peaks from all hydrated proteins were situated between 1646 and 1650 cm-1 in agreement with the CD spectra indicating them to be largely unstructured.","type":"Results"}],"validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2023-06-21T09:03:46.221Z"}}],"__v":0,"disorder_content":1,"disprot_consensus":{"full":[{"start":1,"end":71,"type":"D"}],"Structural state":[{"start":1,"end":71,"type":"D"}]}},{"acc":"P39064","sequence":"MKLRRERFERRNGSGKNSQSSSSWMVTFTDLITLILVFFILLFSMSQIDLQKFKAAVDSIQKEGNGLQPDQTSIEKKNTSPSDTKKQEDQQDQLLKKVNTYIKDNHLKAQMTAKRDERGVVLVLQEAVLFDTGEAKVLKNAETLLHQIAVLLQTIPNDIQVEGHTDSRNISTYRYPSNWELSAARASGVIQYFTSKEKLPSKRFIAVGYADTKPVKDNKTNEHMKENRRVEIVIKKSKTTSS","alphafold_very_low_content":"NaN","creator":"System-eficho","dataset":[],"date":"2026-07-03T10:56:09.790Z","disprot_id":"DP04817","features":{"pfam":[{"id":"PF00691","name":"OmpA family","start":129,"end":228},{"id":"PF13677","name":"Membrane MotB of proton-channel complex MotA/MotB","start":15,"end":62}]},"genes":[{"name":{"value":"ytxE","_id":"6a479549636e23eee35122fd","evidences":[]},"synonyms":[],"olnNames":[{"value":"BSU29720","_id":"6a479549636e23eee35122fe","evidences":[]}],"orfNames":[],"_id":"6a479549636e23eee35122fc"}],"length":242,"name":"Uncharacterized protein YtxE","ncbi_taxon_id":224308,"organism":"Bacillus subtilis (strain 168)","regions_counter":1,"released":"2026_06","taxonomy":["Bacteria","Bacillati","Bacillota","Bacilli","Bacillales","Bacillaceae","Bacillus"],"regions":[{"start":68,"end":82,"reference_id":"40001605","reference_source":"pmid","reference_html":"Sodium-Dependent Conformational Change in Flagellar Stator Protein MotS from &lt;i&gt;Bacillus subtilis&lt;/i&gt;. <i> Takekawa N, Yamaguchi A, Nishiuchi K, Uehori M, Kinoshita M, Minamino T, Imada K. </i> Biomolecules, 2025","date":"2026-06-17T15:44:39.264Z","curator_id":"eficho","curator_name":"Erzsébet Fichó","curator_orcid":"0000-0002-3965-8438","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006220","ec_ontology":"ECO","ec_name":"X-ray crystallography-based structural model with missing residue coordinates used in manual assertion","unpublished":true,"released":"2026_06","version":2,"cross_refs":[{"db":"PDB","id":"9LJL"}],"region_id":"DP04817r001","sample":[{"term_id":"IDPO:00486","term_name":"interacting small molecule","unit_name":"mM","unit_id":"UO:0000063","deviation":null,"value":300,"db":"ChEBI","id":"26710","entry_name":null}],"statement":[{"text":"The N-terminal 15 to 19 residues and C-terminal 5 residues were disordered.","type":"Results"}],"construct_alterations":[{"term_id":"IDPO:00480","term_name":"substitution","term_namespace":"Protein mutation","value":"p.Thr79Ile","start":null,"end":null,"position":null}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-17T15:44:40.987Z"}}],"__v":0,"disorder_content":0.06198347107438017,"disprot_consensus":{"full":[{"start":68,"end":82,"type":"D"}],"Structural state":[{"start":68,"end":82,"type":"D"}]}},{"acc":"O83732","sequence":"MNRPLLSVAGSLFVAAWALYIFSCFQHGHVPPRRIPPHDTFGALPTAALPSNARDTAAHPSDTADNTSGSSTTTDPRSHGNAPPAPVGGAAQTHTQPPVQTAMRIALWNRATHGEQGALQHLLAGLWIQTEISPNSGDIHPLLFFDREHAEITFSRASVQEIFLVDSAHTHRKTVSFLTRNTAISSIRRRLEVTFESHEVIHVRAVEDVARLKIGSTSMWDGQYTRYHAGPASAPSP","alphafold_very_low_content":"NaN","creator":"System-zskalman","dataset":[],"date":"2026-07-03T10:56:10.030Z","disprot_id":"DP04818","features":{"pfam":[{"id":"PF18663","name":"Pallilysin beta barrel domain","start":112,"end":226}]},"genes":[{"synonyms":[],"olnNames":[{"value":"TP_0751","_id":"6a47954a636e23eee3512306","evidences":[]}],"orfNames":[],"_id":"6a47954a636e23eee3512305"}],"length":237,"name":"Uncharacterized protein TP_0751","ncbi_taxon_id":243276,"organism":"Treponema pallidum (strain DSM 117211 / Nichols)","regions_counter":2,"released":"2026_06","taxonomy":["Bacteria","Pseudomonadati","Spirochaetota","Spirochaetia","Spirochaetales","Treponemataceae","Treponema"],"regions":[{"start":25,"end":96,"reference_id":"32936831","reference_source":"pmid","reference_html":"Evidence that immunization with TP0751, a bipartite Treponema pallidum lipoprotein with an intrinsically disordered region and lipocalin fold, fails to protect in the rabbit model of experimental syphilis. <i> Luthra A, Montezuma-Rusca JM, La Vake CJ, LeDoyt M, Delgado KN, Davenport TC, Fiel-Gan M, Caimano MJ, Radolf JD, Hawley KL. </i> PLoS Pathog, 2020","date":"2026-06-22T12:52:42.356Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000002","term_name":"disorder","term_namespace":"Structural state","disprot_namespace":"Structural state","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2026_06","version":1,"region_id":"DP04818r001","statement":[{"text":"Small angle X-ray scattering analysis of full-length protein revealed a bipartite topology consisting of an N-terminal, intrinsically disordered region (IDR) and the previously characterized C-terminal lipocalin domain.","type":"Abstract"},{"text":"In our hands, however, a full-length C-terminal His6-tagged construct (TP075125-237) was stable and migrated by SDS-PAGE with an apparent molecular weight of ~31 kDa (S1A Fig); as previously suggested [42], the large number (18) of proline residues throughout the protein likely explains the slower than expected (24.6 kDa) electrophoretic migration.","type":"Results"},{"text":"Analysis of TP075125-237 using PrDOS [57], IUPred [58] and PONDR [59] predicts that TP075125-96 is intrinsically disordered (Fig 2A).","type":"Results"}],"sequence_construct":"FQHGHVPPRRIPPHDTFGALPTAALPSNARDTAAHPSDTADNTSGSSTTTDPRSHGNAPPAPVGGAAQTHTQ","last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-22T12:53:34.404Z"}},{"start":25,"end":96,"reference_id":"32936831","reference_source":"pmid","reference_html":"Evidence that immunization with TP0751, a bipartite Treponema pallidum lipoprotein with an intrinsically disordered region and lipocalin fold, fails to protect in the rabbit model of experimental syphilis. <i> Luthra A, Montezuma-Rusca JM, La Vake CJ, LeDoyt M, Delgado KN, Davenport TC, Fiel-Gan M, Caimano MJ, Radolf JD, Hawley KL. </i> PLoS Pathog, 2020","date":"2026-06-22T12:53:31.230Z","curator_id":"zskalman","curator_name":"Zsófia Kálmán","curator_orcid":"0000-0003-4634-0433","term_id":"IDPO:0000032","term_name":"flexible N-terminal tail","term_namespace":"Disorder function","disprot_namespace":"Disorder function","term_ontology":"IDPO","ec_id":"ECO:0006218","ec_ontology":"ECO","ec_name":"combinatorial experimental and author inference evidence contained in single publication used in manual assertion","unpublished":true,"released":"2026_06","version":2,"region_id":"DP04818r002","sequence_construct":"FQHGHVPPRRIPPHDTFGALPTAALPSNARDTAAHPSDTADNTSGSSTTTDPRSHGNAPPAPVGGAAQTHTQ","statement":[{"text":"Small angle X-ray scattering analysis of full-length protein revealed a bipartite topology consisting of an N-terminal, intrinsically disordered region (IDR) and the previously characterized C-terminal lipocalin domain.","type":"Abstract"},{"text":"In our hands, however, a full-length C-terminal His6-tagged construct (TP075125-237) was stable and migrated by SDS-PAGE with an apparent molecular weight of ~31 kDa (S1A Fig); as previously suggested [42], the large number (18) of proline residues throughout the protein likely explains the slower than expected (24.6 kDa) electrophoretic migration.","type":"Results"},{"text":"Analysis of TP075125-237 using PrDOS [57], IUPred [58] and PONDR [59] predicts that TP075125-96 is intrinsically disordered (Fig 2A).","type":"Results"},{"text":"The first 24 residues of the sequence protein corresponds to a signal peptide that is processed, leaving the disordered region as the N-terminal flexible tail.","type":"Curator statement"}],"last_modified_by":"vnugnes","last_modified_name":"Victoria Nugnes","validated":{"curator_name":"Victoria Nugnes","curator_id":"vnugnes","timestamp":"2026-06-22T12:53:33.201Z"}}],"__v":0,"disorder_content":0.3037974683544304,"disprot_consensus":{"full":[{"start":25,"end":96,"type":"D"}],"Structural state":[{"start":25,"end":96,"type":"D"}],"Disorder function":[{"start":25,"end":96,"type":"F"}]}}],"size":3337}